data_3SJF # _entry.id 3SJF # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3SJF RCSB RCSB066275 WWPDB D_1000066275 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3SJE . unspecified PDB 3SJG . unspecified PDB 3SJX . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3SJF _pdbx_database_status.recvd_initial_deposition_date 2011-06-21 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Plechanovova, A.' 1 'Byun, Y.' 2 'Alquicer, G.' 3 'Skultetyova, L.' 4 'Mlcochova, P.' 5 'Nemcova, A.' 6 'Kim, H.' 7 'Navratil, M.' 8 'Mease, R.' 9 'Lubkowski, J.' 10 'Pomper, M.' 11 'Konvalinka, J.' 12 'Rulisek, L.' 13 'Barinka, C.' 14 # _citation.id primary _citation.title 'Novel Substrate-Based Inhibitors of Human Glutamate Carboxypeptidase II with Enhanced Lipophilicity.' _citation.journal_abbrev J.Med.Chem. _citation.journal_volume 54 _citation.page_first 7535 _citation.page_last 7546 _citation.year 2011 _citation.journal_id_ASTM JMCMAR _citation.country US _citation.journal_id_ISSN 0022-2623 _citation.journal_id_CSD 0151 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 21923190 _citation.pdbx_database_id_DOI 10.1021/jm200807m # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Plechanovova, A.' 1 primary 'Byun, Y.' 2 primary 'Alquicer, G.' 3 primary 'Skultetyova, L.' 4 primary 'Mlcochova, P.' 5 primary 'Nemcova, A.' 6 primary 'Kim, H.J.' 7 primary 'Navratil, M.' 8 primary 'Mease, R.' 9 primary 'Lubkowski, J.' 10 primary 'Pomper, M.' 11 primary 'Konvalinka, J.' 12 primary 'Rulisek, L.' 13 primary 'Barinka, C.' 14 # _cell.entry_id 3SJF _cell.length_a 101.545 _cell.length_b 130.431 _cell.length_c 159.156 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3SJF _symmetry.space_group_name_H-M 'I 2 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 23 _symmetry.space_group_name_Hall ? # 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 'Glutamate carboxypeptidase 2' 79859.031 1 3.4.17.21 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 11 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 5 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 6 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 7 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 8 non-polymer syn 'N~2~-{[(1S)-1-carboxy-3-(methylsulfanyl)propyl]carbamoyl}-N~6~-(4-iodobenzoyl)-L-lysine' 551.396 1 ? ? ? ? 9 water nat water 18.015 584 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ;Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Membrane glutamate carboxypeptidase, mGCP, N-acetylated-alpha-linked acidic dipeptidase I, NAALADase I, Prostate-specific membrane antigen, PSM, PSMA, Pteroylpoly-gamma-glutamate carboxypeptidase ; # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;RSKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPN KTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIV IARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRR GIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGT LRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRL LQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDF EVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYA VVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGL PDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_seq_one_letter_code_can ;RSKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPN KTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIV IARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRR GIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGT LRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRL LQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDF EVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYA VVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGL PDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ARG n 1 2 SER n 1 3 LYS n 1 4 SER n 1 5 SER n 1 6 ASN n 1 7 GLU n 1 8 ALA n 1 9 THR n 1 10 ASN n 1 11 ILE n 1 12 THR n 1 13 PRO n 1 14 LYS n 1 15 HIS n 1 16 ASN n 1 17 MET n 1 18 LYS n 1 19 ALA n 1 20 PHE n 1 21 LEU n 1 22 ASP n 1 23 GLU n 1 24 LEU n 1 25 LYS n 1 26 ALA n 1 27 GLU n 1 28 ASN n 1 29 ILE n 1 30 LYS n 1 31 LYS n 1 32 PHE n 1 33 LEU n 1 34 TYR n 1 35 ASN n 1 36 PHE n 1 37 THR n 1 38 GLN n 1 39 ILE n 1 40 PRO n 1 41 HIS n 1 42 LEU n 1 43 ALA n 1 44 GLY n 1 45 THR n 1 46 GLU n 1 47 GLN n 1 48 ASN n 1 49 PHE n 1 50 GLN n 1 51 LEU n 1 52 ALA n 1 53 LYS n 1 54 GLN n 1 55 ILE n 1 56 GLN n 1 57 SER n 1 58 GLN n 1 59 TRP n 1 60 LYS n 1 61 GLU n 1 62 PHE n 1 63 GLY n 1 64 LEU n 1 65 ASP n 1 66 SER n 1 67 VAL n 1 68 GLU n 1 69 LEU n 1 70 ALA n 1 71 HIS n 1 72 TYR n 1 73 ASP n 1 74 VAL n 1 75 LEU n 1 76 LEU n 1 77 SER n 1 78 TYR n 1 79 PRO n 1 80 ASN n 1 81 LYS n 1 82 THR n 1 83 HIS n 1 84 PRO n 1 85 ASN n 1 86 TYR n 1 87 ILE n 1 88 SER n 1 89 ILE n 1 90 ILE n 1 91 ASN n 1 92 GLU n 1 93 ASP n 1 94 GLY n 1 95 ASN n 1 96 GLU n 1 97 ILE n 1 98 PHE n 1 99 ASN n 1 100 THR n 1 101 SER n 1 102 LEU n 1 103 PHE n 1 104 GLU n 1 105 PRO n 1 106 PRO n 1 107 PRO n 1 108 PRO n 1 109 GLY n 1 110 TYR n 1 111 GLU n 1 112 ASN n 1 113 VAL n 1 114 SER n 1 115 ASP n 1 116 ILE n 1 117 VAL n 1 118 PRO n 1 119 PRO n 1 120 PHE n 1 121 SER n 1 122 ALA n 1 123 PHE n 1 124 SER n 1 125 PRO n 1 126 GLN n 1 127 GLY n 1 128 MET n 1 129 PRO n 1 130 GLU n 1 131 GLY n 1 132 ASP n 1 133 LEU n 1 134 VAL n 1 135 TYR n 1 136 VAL n 1 137 ASN n 1 138 TYR n 1 139 ALA n 1 140 ARG n 1 141 THR n 1 142 GLU n 1 143 ASP n 1 144 PHE n 1 145 PHE n 1 146 LYS n 1 147 LEU n 1 148 GLU n 1 149 ARG n 1 150 ASP n 1 151 MET n 1 152 LYS n 1 153 ILE n 1 154 ASN n 1 155 CYS n 1 156 SER n 1 157 GLY n 1 158 LYS n 1 159 ILE n 1 160 VAL n 1 161 ILE n 1 162 ALA n 1 163 ARG n 1 164 TYR n 1 165 GLY n 1 166 LYS n 1 167 VAL n 1 168 PHE n 1 169 ARG n 1 170 GLY n 1 171 ASN n 1 172 LYS n 1 173 VAL n 1 174 LYS n 1 175 ASN n 1 176 ALA n 1 177 GLN n 1 178 LEU n 1 179 ALA n 1 180 GLY n 1 181 ALA n 1 182 LYS n 1 183 GLY n 1 184 VAL n 1 185 ILE n 1 186 LEU n 1 187 TYR n 1 188 SER n 1 189 ASP n 1 190 PRO n 1 191 ALA n 1 192 ASP n 1 193 TYR n 1 194 PHE n 1 195 ALA n 1 196 PRO n 1 197 GLY n 1 198 VAL n 1 199 LYS n 1 200 SER n 1 201 TYR n 1 202 PRO n 1 203 ASP n 1 204 GLY n 1 205 TRP n 1 206 ASN n 1 207 LEU n 1 208 PRO n 1 209 GLY n 1 210 GLY n 1 211 GLY n 1 212 VAL n 1 213 GLN n 1 214 ARG n 1 215 GLY n 1 216 ASN n 1 217 ILE n 1 218 LEU n 1 219 ASN n 1 220 LEU n 1 221 ASN n 1 222 GLY n 1 223 ALA n 1 224 GLY n 1 225 ASP n 1 226 PRO n 1 227 LEU n 1 228 THR n 1 229 PRO n 1 230 GLY n 1 231 TYR n 1 232 PRO n 1 233 ALA n 1 234 ASN n 1 235 GLU n 1 236 TYR n 1 237 ALA n 1 238 TYR n 1 239 ARG n 1 240 ARG n 1 241 GLY n 1 242 ILE n 1 243 ALA n 1 244 GLU n 1 245 ALA n 1 246 VAL n 1 247 GLY n 1 248 LEU n 1 249 PRO n 1 250 SER n 1 251 ILE n 1 252 PRO n 1 253 VAL n 1 254 HIS n 1 255 PRO n 1 256 ILE n 1 257 GLY n 1 258 TYR n 1 259 TYR n 1 260 ASP n 1 261 ALA n 1 262 GLN n 1 263 LYS n 1 264 LEU n 1 265 LEU n 1 266 GLU n 1 267 LYS n 1 268 MET n 1 269 GLY n 1 270 GLY n 1 271 SER n 1 272 ALA n 1 273 PRO n 1 274 PRO n 1 275 ASP n 1 276 SER n 1 277 SER n 1 278 TRP n 1 279 ARG n 1 280 GLY n 1 281 SER n 1 282 LEU n 1 283 LYS n 1 284 VAL n 1 285 PRO n 1 286 TYR n 1 287 ASN n 1 288 VAL n 1 289 GLY n 1 290 PRO n 1 291 GLY n 1 292 PHE n 1 293 THR n 1 294 GLY n 1 295 ASN n 1 296 PHE n 1 297 SER n 1 298 THR n 1 299 GLN n 1 300 LYS n 1 301 VAL n 1 302 LYS n 1 303 MET n 1 304 HIS n 1 305 ILE n 1 306 HIS n 1 307 SER n 1 308 THR n 1 309 ASN n 1 310 GLU n 1 311 VAL n 1 312 THR n 1 313 ARG n 1 314 ILE n 1 315 TYR n 1 316 ASN n 1 317 VAL n 1 318 ILE n 1 319 GLY n 1 320 THR n 1 321 LEU n 1 322 ARG n 1 323 GLY n 1 324 ALA n 1 325 VAL n 1 326 GLU n 1 327 PRO n 1 328 ASP n 1 329 ARG n 1 330 TYR n 1 331 VAL n 1 332 ILE n 1 333 LEU n 1 334 GLY n 1 335 GLY n 1 336 HIS n 1 337 ARG n 1 338 ASP n 1 339 SER n 1 340 TRP n 1 341 VAL n 1 342 PHE n 1 343 GLY n 1 344 GLY n 1 345 ILE n 1 346 ASP n 1 347 PRO n 1 348 GLN n 1 349 SER n 1 350 GLY n 1 351 ALA n 1 352 ALA n 1 353 VAL n 1 354 VAL n 1 355 HIS n 1 356 GLU n 1 357 ILE n 1 358 VAL n 1 359 ARG n 1 360 SER n 1 361 PHE n 1 362 GLY n 1 363 THR n 1 364 LEU n 1 365 LYS n 1 366 LYS n 1 367 GLU n 1 368 GLY n 1 369 TRP n 1 370 ARG n 1 371 PRO n 1 372 ARG n 1 373 ARG n 1 374 THR n 1 375 ILE n 1 376 LEU n 1 377 PHE n 1 378 ALA n 1 379 SER n 1 380 TRP n 1 381 ASP n 1 382 ALA n 1 383 GLU n 1 384 GLU n 1 385 PHE n 1 386 GLY n 1 387 LEU n 1 388 LEU n 1 389 GLY n 1 390 SER n 1 391 THR n 1 392 GLU n 1 393 TRP n 1 394 ALA n 1 395 GLU n 1 396 GLU n 1 397 ASN n 1 398 SER n 1 399 ARG n 1 400 LEU n 1 401 LEU n 1 402 GLN n 1 403 GLU n 1 404 ARG n 1 405 GLY n 1 406 VAL n 1 407 ALA n 1 408 TYR n 1 409 ILE n 1 410 ASN n 1 411 ALA n 1 412 ASP n 1 413 SER n 1 414 SER n 1 415 ILE n 1 416 GLU n 1 417 GLY n 1 418 ASN n 1 419 TYR n 1 420 THR n 1 421 LEU n 1 422 ARG n 1 423 VAL n 1 424 ASP n 1 425 CYS n 1 426 THR n 1 427 PRO n 1 428 LEU n 1 429 MET n 1 430 TYR n 1 431 SER n 1 432 LEU n 1 433 VAL n 1 434 HIS n 1 435 ASN n 1 436 LEU n 1 437 THR n 1 438 LYS n 1 439 GLU n 1 440 LEU n 1 441 LYS n 1 442 SER n 1 443 PRO n 1 444 ASP n 1 445 GLU n 1 446 GLY n 1 447 PHE n 1 448 GLU n 1 449 GLY n 1 450 LYS n 1 451 SER n 1 452 LEU n 1 453 TYR n 1 454 GLU n 1 455 SER n 1 456 TRP n 1 457 THR n 1 458 LYS n 1 459 LYS n 1 460 SER n 1 461 PRO n 1 462 SER n 1 463 PRO n 1 464 GLU n 1 465 PHE n 1 466 SER n 1 467 GLY n 1 468 MET n 1 469 PRO n 1 470 ARG n 1 471 ILE n 1 472 SER n 1 473 LYS n 1 474 LEU n 1 475 GLY n 1 476 SER n 1 477 GLY n 1 478 ASN n 1 479 ASP n 1 480 PHE n 1 481 GLU n 1 482 VAL n 1 483 PHE n 1 484 PHE n 1 485 GLN n 1 486 ARG n 1 487 LEU n 1 488 GLY n 1 489 ILE n 1 490 ALA n 1 491 SER n 1 492 GLY n 1 493 ARG n 1 494 ALA n 1 495 ARG n 1 496 TYR n 1 497 THR n 1 498 LYS n 1 499 ASN n 1 500 TRP n 1 501 GLU n 1 502 THR n 1 503 ASN n 1 504 LYS n 1 505 PHE n 1 506 SER n 1 507 GLY n 1 508 TYR n 1 509 PRO n 1 510 LEU n 1 511 TYR n 1 512 HIS n 1 513 SER n 1 514 VAL n 1 515 TYR n 1 516 GLU n 1 517 THR n 1 518 TYR n 1 519 GLU n 1 520 LEU n 1 521 VAL n 1 522 GLU n 1 523 LYS n 1 524 PHE n 1 525 TYR n 1 526 ASP n 1 527 PRO n 1 528 MET n 1 529 PHE n 1 530 LYS n 1 531 TYR n 1 532 HIS n 1 533 LEU n 1 534 THR n 1 535 VAL n 1 536 ALA n 1 537 GLN n 1 538 VAL n 1 539 ARG n 1 540 GLY n 1 541 GLY n 1 542 MET n 1 543 VAL n 1 544 PHE n 1 545 GLU n 1 546 LEU n 1 547 ALA n 1 548 ASN n 1 549 SER n 1 550 ILE n 1 551 VAL n 1 552 LEU n 1 553 PRO n 1 554 PHE n 1 555 ASP n 1 556 CYS n 1 557 ARG n 1 558 ASP n 1 559 TYR n 1 560 ALA n 1 561 VAL n 1 562 VAL n 1 563 LEU n 1 564 ARG n 1 565 LYS n 1 566 TYR n 1 567 ALA n 1 568 ASP n 1 569 LYS n 1 570 ILE n 1 571 TYR n 1 572 SER n 1 573 ILE n 1 574 SER n 1 575 MET n 1 576 LYS n 1 577 HIS n 1 578 PRO n 1 579 GLN n 1 580 GLU n 1 581 MET n 1 582 LYS n 1 583 THR n 1 584 TYR n 1 585 SER n 1 586 VAL n 1 587 SER n 1 588 PHE n 1 589 ASP n 1 590 SER n 1 591 LEU n 1 592 PHE n 1 593 SER n 1 594 ALA n 1 595 VAL n 1 596 LYS n 1 597 ASN n 1 598 PHE n 1 599 THR n 1 600 GLU n 1 601 ILE n 1 602 ALA n 1 603 SER n 1 604 LYS n 1 605 PHE n 1 606 SER n 1 607 GLU n 1 608 ARG n 1 609 LEU n 1 610 GLN n 1 611 ASP n 1 612 PHE n 1 613 ASP n 1 614 LYS n 1 615 SER n 1 616 ASN n 1 617 PRO n 1 618 ILE n 1 619 VAL n 1 620 LEU n 1 621 ARG n 1 622 MET n 1 623 MET n 1 624 ASN n 1 625 ASP n 1 626 GLN n 1 627 LEU n 1 628 MET n 1 629 PHE n 1 630 LEU n 1 631 GLU n 1 632 ARG n 1 633 ALA n 1 634 PHE n 1 635 ILE n 1 636 ASP n 1 637 PRO n 1 638 LEU n 1 639 GLY n 1 640 LEU n 1 641 PRO n 1 642 ASP n 1 643 ARG n 1 644 PRO n 1 645 PHE n 1 646 TYR n 1 647 ARG n 1 648 HIS n 1 649 VAL n 1 650 ILE n 1 651 TYR n 1 652 ALA n 1 653 PRO n 1 654 SER n 1 655 SER n 1 656 HIS n 1 657 ASN n 1 658 LYS n 1 659 TYR n 1 660 ALA n 1 661 GLY n 1 662 GLU n 1 663 SER n 1 664 PHE n 1 665 PRO n 1 666 GLY n 1 667 ILE n 1 668 TYR n 1 669 ASP n 1 670 ALA n 1 671 LEU n 1 672 PHE n 1 673 ASP n 1 674 ILE n 1 675 GLU n 1 676 SER n 1 677 LYS n 1 678 VAL n 1 679 ASP n 1 680 PRO n 1 681 SER n 1 682 LYS n 1 683 ALA n 1 684 TRP n 1 685 GLY n 1 686 GLU n 1 687 VAL n 1 688 LYS n 1 689 ARG n 1 690 GLN n 1 691 ILE n 1 692 TYR n 1 693 VAL n 1 694 ALA n 1 695 ALA n 1 696 PHE n 1 697 THR n 1 698 VAL n 1 699 GLN n 1 700 ALA n 1 701 ALA n 1 702 ALA n 1 703 GLU n 1 704 THR n 1 705 LEU n 1 706 SER n 1 707 GLU n 1 708 VAL n 1 709 ALA n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'FOLH1, FOLH, NAALAD1, PSM, PSMA, GIG27' _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 'Drosophila melanogaster' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7227 _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 ;Schneider's S2 cells ; _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 ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code FOLH1_HUMAN _struct_ref.pdbx_db_accession Q04609 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;KSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKT HPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIA RYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGI AEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLR GAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQ ERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEV FFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVV LRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPD RPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _struct_ref.pdbx_align_begin 44 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3SJF _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 3 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 709 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q04609 _struct_ref_seq.db_align_beg 44 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 750 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 44 _struct_ref_seq.pdbx_auth_seq_align_end 750 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 3SJF ARG A 1 ? UNP Q04609 ? ? 'EXPRESSION TAG' 42 1 1 3SJF SER A 2 ? UNP Q04609 ? ? 'EXPRESSION TAG' 43 2 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 JRG non-polymer . 'N~2~-{[(1S)-1-carboxy-3-(methylsulfanyl)propyl]carbamoyl}-N~6~-(4-iodobenzoyl)-L-lysine' ? 'C19 H26 I N3 O6 S' 551.396 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 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 3SJF _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.30 _exptl_crystal.density_percent_sol 62.72 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8.0 _exptl_crystal_grow.pdbx_details ;33% (v/v) pentaerythritol propoxylate PO/OH 5/4, 0.5 % (w/v) PEG 3350, 100 mM Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K ; _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MARMOSAIC 225 mm CCD' _diffrn_detector.pdbx_collection_date 2006-06-11 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Si 111, Rosenbaum-Rock double-crystal monochromator' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.00 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 22-ID' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 22-ID _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.00 # _reflns.entry_id 3SJF _reflns.observed_criterion_sigma_I -3 _reflns.observed_criterion_sigma_F -3 _reflns.d_resolution_low 30 _reflns.d_resolution_high 1.65 _reflns.number_obs 125829 _reflns.number_all 125829 _reflns.percent_possible_obs 99.7 _reflns.pdbx_Rmerge_I_obs 0.076 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 20.9 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 7.3 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _refine.entry_id 3SJF _refine.ls_number_reflns_obs 124196 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 29.52 _refine.ls_d_res_high 1.65 _refine.ls_percent_reflns_obs 99.38 _refine.ls_R_factor_obs 0.15929 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.15911 _refine.ls_R_factor_R_free 0.17811 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 1.0 _refine.ls_number_reflns_R_free 1258 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.972 _refine.correlation_coeff_Fo_to_Fc_free 0.961 _refine.B_iso_mean 28.457 _refine.aniso_B[1][1] 0.00 _refine.aniso_B[2][2] 0.01 _refine.aniso_B[3][3] -0.01 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'FOURIER SYNTHESIS' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R_Free 0.069 _refine.overall_SU_ML 0.044 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 2.770 _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_overall_ESU_R ? _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 5528 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 210 _refine_hist.number_atoms_solvent 584 _refine_hist.number_atoms_total 6322 _refine_hist.d_res_high 1.65 _refine_hist.d_res_low 29.52 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_restraint_function _refine_ls_restr.pdbx_refine_id r_bond_refined_d 0.016 0.022 ? 6365 ? 'X-RAY DIFFRACTION' r_bond_other_d ? ? ? ? ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.602 1.996 ? 8687 ? 'X-RAY DIFFRACTION' r_angle_other_deg ? ? ? ? ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 5.637 5.000 ? 782 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 36.754 24.133 ? 300 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 13.876 15.000 ? 1094 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 13.620 15.000 ? 35 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.121 0.200 ? 934 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.010 0.021 ? 4910 ? 'X-RAY DIFFRACTION' r_gen_planes_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbd_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbd_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbtor_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbtor_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_metal_ion_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_metal_ion_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_vdw_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_vdw_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_hbond_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_hbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_metal_ion_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_metal_ion_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcbond_it 0.919 1.500 ? 3668 ? 'X-RAY DIFFRACTION' r_mcbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcangle_it 1.567 2.000 ? 6010 ? 'X-RAY DIFFRACTION' r_scbond_it 2.436 3.000 ? 2697 ? 'X-RAY DIFFRACTION' r_scangle_it 3.945 4.500 ? 2644 ? 'X-RAY DIFFRACTION' r_rigid_bond_restr ? ? ? ? ? 'X-RAY DIFFRACTION' r_sphericity_free ? ? ? ? ? 'X-RAY DIFFRACTION' r_sphericity_bonded ? ? ? ? ? 'X-RAY DIFFRACTION' # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.65 _refine_ls_shell.d_res_low 1.694 _refine_ls_shell.number_reflns_R_work 8831 _refine_ls_shell.R_factor_R_work 0.244 _refine_ls_shell.percent_reflns_obs 96.61 _refine_ls_shell.R_factor_R_free 0.272 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 85 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 3SJF _struct.title 'X-ray structure of human glutamate carboxypeptidase II in complex with a urea-based inhibitor (A25)' _struct.pdbx_descriptor 'Glutamate carboxypeptidase 2 (E.C.3.4.17.21)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3SJF _struct_keywords.pdbx_keywords 'Hydrolase/hydrolase inhibitor' _struct_keywords.text 'hydrolase, metallopeptidase, Hydrolase-hydrolase inhibitor complex' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 2 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 2 ? I N N 2 ? J N N 2 ? K N N 2 ? L N N 2 ? M N N 3 ? N N N 4 ? O N N 5 ? P N N 5 ? Q N N 6 ? R N N 7 ? S N N 8 ? T N N 9 ? # _struct_biol.id 1 _struct_biol.details ? # 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 1 ASN A 16 ? LEU A 24 ? ASN A 57 LEU A 65 1 ? 9 HELX_P HELX_P2 2 LYS A 25 ? THR A 37 ? LYS A 66 THR A 78 1 ? 13 HELX_P HELX_P3 3 THR A 45 ? GLY A 63 ? THR A 86 GLY A 104 1 ? 19 HELX_P HELX_P4 4 ARG A 140 ? ASP A 150 ? ARG A 181 ASP A 191 1 ? 11 HELX_P HELX_P5 5 PHE A 168 ? ALA A 179 ? PHE A 209 ALA A 220 1 ? 12 HELX_P HELX_P6 6 ASP A 189 ? PHE A 194 ? ASP A 230 PHE A 235 1 ? 6 HELX_P HELX_P7 7 GLY A 241 ? ALA A 245 ? GLY A 282 ALA A 286 5 ? 5 HELX_P HELX_P8 8 GLY A 257 ? GLU A 266 ? GLY A 298 GLU A 307 1 ? 10 HELX_P HELX_P9 9 ASP A 275 ? ARG A 279 ? ASP A 316 ARG A 320 5 ? 5 HELX_P HELX_P10 10 THR A 293 ? SER A 297 ? THR A 334 SER A 338 5 ? 5 HELX_P HELX_P11 11 PRO A 347 ? GLU A 367 ? PRO A 388 GLU A 408 1 ? 21 HELX_P HELX_P12 12 ALA A 382 ? GLY A 386 ? ALA A 423 GLY A 427 5 ? 5 HELX_P HELX_P13 13 LEU A 387 ? ARG A 404 ? LEU A 428 ARG A 445 1 ? 18 HELX_P HELX_P14 14 MET A 429 ? LEU A 440 ? MET A 470 LEU A 481 1 ? 12 HELX_P HELX_P15 15 SER A 451 ? SER A 460 ? SER A 492 SER A 501 1 ? 10 HELX_P HELX_P16 16 PHE A 480 ? ARG A 486 ? PHE A 521 ARG A 527 1 ? 7 HELX_P HELX_P17 17 TRP A 500 ? LYS A 504 ? TRP A 541 LYS A 545 5 ? 5 HELX_P HELX_P18 18 THR A 517 ? TYR A 525 ? THR A 558 TYR A 566 1 ? 9 HELX_P HELX_P19 19 PHE A 529 ? SER A 549 ? PHE A 570 SER A 590 1 ? 21 HELX_P HELX_P20 20 ASP A 555 ? MET A 575 ? ASP A 596 MET A 616 1 ? 21 HELX_P HELX_P21 21 HIS A 577 ? TYR A 584 ? HIS A 618 TYR A 625 1 ? 8 HELX_P HELX_P22 22 PHE A 588 ? PHE A 612 ? PHE A 629 PHE A 653 1 ? 25 HELX_P HELX_P23 23 ASN A 616 ? ALA A 633 ? ASN A 657 ALA A 674 1 ? 18 HELX_P HELX_P24 24 PHE A 664 ? PHE A 672 ? PHE A 705 PHE A 713 1 ? 9 HELX_P HELX_P25 25 ASP A 673 ? LYS A 677 ? ASP A 714 LYS A 718 5 ? 5 HELX_P HELX_P26 26 ASP A 679 ? THR A 704 ? ASP A 720 THR A 745 1 ? 26 # _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 covale1 covale ? ? L NAG . O4 ? ? ? 1_555 M BMA . C1 ? ? A NAG 1764 A BMA 1765 1_555 ? ? ? ? ? ? ? 1.417 ? covale2 covale ? ? A ASN 35 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 76 A NAG 1755 1_555 ? ? ? ? ? ? ? 1.430 ? covale3 covale ? ? A ASN 597 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 638 A NAG 1763 1_555 ? ? ? ? ? ? ? 1.433 ? covale4 covale ? ? K NAG . O4 ? ? ? 1_555 L NAG . C1 ? ? A NAG 1763 A NAG 1764 1_555 ? ? ? ? ? ? ? 1.438 ? covale5 covale ? ? A ASN 418 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 459 A NAG 1760 1_555 ? ? ? ? ? ? ? 1.441 ? covale6 covale ? ? A ASN 435 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 476 A NAG 1761 1_555 ? ? ? ? ? ? ? 1.441 ? covale7 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 1755 A NAG 1756 1_555 ? ? ? ? ? ? ? 1.444 ? covale8 covale ? ? A ASN 80 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 121 A NAG 1757 1_555 ? ? ? ? ? ? ? 1.446 ? covale9 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 1761 A NAG 1762 1_555 ? ? ? ? ? ? ? 1.449 ? covale10 covale ? ? A ASN 99 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 140 A NAG 1758 1_555 ? ? ? ? ? ? ? 1.449 ? covale11 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 1758 A NAG 1767 1_555 ? ? ? ? ? ? ? 1.450 ? covale12 covale ? ? A ASN 154 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 195 A NAG 1759 1_555 ? ? ? ? ? ? ? 1.452 ? covale13 covale ? ? M BMA . O3 ? ? ? 1_555 N MAN . C1 ? ? A BMA 1765 A MAN 1766 1_555 ? ? ? ? ? ? ? 1.458 ? metalc1 metalc ? ? P ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 1752 A HOH 2476 1_555 ? ? ? ? ? ? ? 1.887 ? metalc2 metalc ? ? A ASP 412 OD2 ? ? ? 1_555 P ZN . ZN ? ? A ASP 453 A ZN 1752 1_555 ? ? ? ? ? ? ? 1.940 ? metalc3 metalc ? ? A ASP 346 OD1 ? ? ? 1_555 P ZN . ZN ? ? A ASP 387 A ZN 1752 1_555 ? ? ? ? ? ? ? 1.970 ? metalc4 metalc ? ? A HIS 336 NE2 ? ? ? 1_555 P ZN . ZN ? ? A HIS 377 A ZN 1752 1_555 ? ? ? ? ? ? ? 2.004 ? metalc5 metalc ? ? O ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 1751 A HOH 2476 1_555 ? ? ? ? ? ? ? 2.005 ? metalc6 metalc ? ? A HIS 512 NE2 ? ? ? 1_555 O ZN . ZN ? ? A HIS 553 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.043 ? metalc7 metalc ? ? A ASP 346 OD2 ? ? ? 1_555 O ZN . ZN ? ? A ASP 387 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.087 ? metalc8 metalc ? ? A GLU 384 OE2 ? ? ? 1_555 O ZN . ZN ? ? A GLU 425 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.111 ? metalc9 metalc ? ? A TYR 231 O ? ? ? 1_555 Q CA . CA ? ? A TYR 272 A CA 1753 1_555 ? ? ? ? ? ? ? 2.299 ? metalc10 metalc ? ? A GLU 395 OE2 ? ? ? 1_555 Q CA . CA ? ? A GLU 436 A CA 1753 1_555 ? ? ? ? ? ? ? 2.306 ? metalc11 metalc ? ? A THR 228 O ? ? ? 1_555 Q CA . CA ? ? A THR 269 A CA 1753 1_555 ? ? ? ? ? ? ? 2.399 ? metalc12 metalc ? ? Q CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 1753 A HOH 1773 1_555 ? ? ? ? ? ? ? 2.416 ? metalc13 metalc ? ? A GLU 384 OE1 ? ? ? 1_555 O ZN . ZN ? ? A GLU 425 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.443 ? metalc14 metalc ? ? A GLU 392 OE2 ? ? ? 1_555 Q CA . CA ? ? A GLU 433 A CA 1753 1_555 ? ? ? ? ? ? ? 2.485 ? metalc15 metalc ? ? A THR 228 OG1 ? ? ? 1_555 Q CA . CA ? ? A THR 269 A CA 1753 1_555 ? ? ? ? ? ? ? 2.486 ? metalc16 metalc ? ? A GLU 392 OE1 ? ? ? 1_555 Q CA . CA ? ? A GLU 433 A CA 1753 1_555 ? ? ? ? ? ? ? 2.491 ? metalc17 metalc ? ? O ZN . ZN ? ? ? 1_555 S JRG . OAD ? ? A ZN 1751 A JRG 1 1_555 ? ? ? ? ? ? ? 2.633 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference covale ? ? metalc ? ? # 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 TYR 201 A . ? TYR 242 A PRO 202 A ? PRO 243 A 1 9.80 2 GLY 289 A . ? GLY 330 A PRO 290 A ? PRO 331 A 1 -1.04 3 ASP 346 A . ? ASP 387 A PRO 347 A ? PRO 388 A 1 9.22 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 7 ? B ? 4 ? C ? 2 ? D ? 4 ? E ? 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 A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? parallel D 1 2 ? parallel D 2 3 ? parallel D 3 4 ? parallel E 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 A 1 SER A 66 ? TYR A 78 ? SER A 107 TYR A 119 A 2 THR A 308 ? LEU A 321 ? THR A 349 LEU A 362 A 3 ARG A 373 ? TRP A 380 ? ARG A 414 TRP A 421 A 4 GLU A 326 ? HIS A 336 ? GLU A 367 HIS A 377 A 5 GLY A 405 ? ASN A 410 ? GLY A 446 ASN A 451 A 6 ALA A 490 ? THR A 497 ? ALA A 531 THR A 538 A 7 THR A 420 ? CYS A 425 ? THR A 461 CYS A 466 B 1 GLU A 96 ? ASN A 99 ? GLU A 137 ASN A 140 B 2 TYR A 86 ? ILE A 90 ? TYR A 127 ILE A 131 B 3 LYS A 300 ? HIS A 304 ? LYS A 341 HIS A 345 B 4 GLU A 130 ? GLY A 131 ? GLU A 171 GLY A 172 C 1 SER A 121 ? ALA A 122 ? SER A 162 ALA A 163 C 2 GLY A 215 ? ASN A 216 ? GLY A 256 ASN A 257 D 1 LEU A 133 ? TYR A 135 ? LEU A 174 TYR A 176 D 2 ILE A 159 ? ARG A 163 ? ILE A 200 ARG A 204 D 3 GLY A 183 ? TYR A 187 ? GLY A 224 TYR A 228 D 4 VAL A 253 ? ILE A 256 ? VAL A 294 ILE A 297 E 1 TYR A 651 ? SER A 654 ? TYR A 692 SER A 695 E 2 ASN A 657 ? SER A 663 ? ASN A 698 SER A 704 # 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 A 1 2 N ALA A 70 ? N ALA A 111 O ASN A 316 ? O ASN A 357 A 2 3 N GLY A 319 ? N GLY A 360 O PHE A 377 ? O PHE A 418 A 3 4 O LEU A 376 ? O LEU A 417 N LEU A 333 ? N LEU A 374 A 4 5 N ILE A 332 ? N ILE A 373 O ILE A 409 ? O ILE A 450 A 5 6 N ASN A 410 ? N ASN A 451 O GLY A 492 ? O GLY A 533 A 6 7 O THR A 497 ? O THR A 538 N THR A 420 ? N THR A 461 B 1 2 O ILE A 97 ? O ILE A 138 N ILE A 89 ? N ILE A 130 B 2 3 N SER A 88 ? N SER A 129 O LYS A 302 ? O LYS A 343 B 3 4 O VAL A 301 ? O VAL A 342 N GLY A 131 ? N GLY A 172 C 1 2 O ALA A 122 ? O ALA A 163 N GLY A 215 ? N GLY A 256 D 1 2 N VAL A 134 ? N VAL A 175 O ILE A 161 ? O ILE A 202 D 2 3 N VAL A 160 ? N VAL A 201 O ILE A 185 ? O ILE A 226 D 3 4 N LEU A 186 ? N LEU A 227 O ILE A 256 ? O ILE A 297 E 1 2 N SER A 654 ? N SER A 695 O ALA A 660 ? O ALA A 701 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 1755' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 1756' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 1757' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 1758' AC5 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 1767' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 1759' AC7 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 1760' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 1761' AC9 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 1762' BC1 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 1763' BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 1764' BC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE BMA A 1765' BC4 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE MAN A 1766' BC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ZN A 1751' BC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE ZN A 1752' BC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 1753' BC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CL A 1754' BC9 Software ? ? ? ? 21 'BINDING SITE FOR RESIDUE JRG A 1' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 ASN A 35 ? ASN A 76 . ? 1_555 ? 2 AC1 6 GLN A 54 ? GLN A 95 . ? 1_555 ? 3 AC1 6 GLN A 58 ? GLN A 99 . ? 1_555 ? 4 AC1 6 NAG C . ? NAG A 1756 . ? 1_555 ? 5 AC1 6 HOH T . ? HOH A 2016 . ? 1_555 ? 6 AC1 6 HOH T . ? HOH A 2057 . ? 1_555 ? 7 AC2 3 NAG B . ? NAG A 1755 . ? 1_555 ? 8 AC2 3 HOH T . ? HOH A 2026 . ? 1_555 ? 9 AC2 3 HOH T . ? HOH A 2471 . ? 1_555 ? 10 AC3 5 ASN A 80 ? ASN A 121 . ? 1_555 ? 11 AC3 5 THR A 82 ? THR A 123 . ? 1_555 ? 12 AC3 5 HIS A 83 ? HIS A 124 . ? 1_555 ? 13 AC3 5 THR A 308 ? THR A 349 . ? 1_555 ? 14 AC3 5 HOH T . ? HOH A 2443 . ? 1_555 ? 15 AC4 5 TYR A 86 ? TYR A 127 . ? 1_555 ? 16 AC4 5 GLU A 96 ? GLU A 137 . ? 1_555 ? 17 AC4 5 ILE A 97 ? ILE A 138 . ? 1_555 ? 18 AC4 5 ASN A 99 ? ASN A 140 . ? 1_555 ? 19 AC4 5 NAG F . ? NAG A 1767 . ? 1_555 ? 20 AC5 2 NAG E . ? NAG A 1758 . ? 1_555 ? 21 AC5 2 HOH T . ? HOH A 2447 . ? 1_555 ? 22 AC6 3 ASN A 154 ? ASN A 195 . ? 1_555 ? 23 AC6 3 HOH T . ? HOH A 2474 . ? 1_555 ? 24 AC6 3 HOH T . ? HOH A 2493 . ? 1_555 ? 25 AC7 8 TRP A 205 ? TRP A 246 . ? 1_555 ? 26 AC7 8 ASN A 418 ? ASN A 459 . ? 1_555 ? 27 AC7 8 PHE A 524 ? PHE A 565 . ? 1_555 ? 28 AC7 8 TYR A 525 ? TYR A 566 . ? 1_555 ? 29 AC7 8 HOH T . ? HOH A 1845 . ? 1_555 ? 30 AC7 8 HOH T . ? HOH A 2044 . ? 1_555 ? 31 AC7 8 HOH T . ? HOH A 2162 . ? 1_555 ? 32 AC7 8 HOH T . ? HOH A 2387 . ? 1_555 ? 33 AC8 5 SER A 431 ? SER A 472 . ? 1_555 ? 34 AC8 5 ASN A 435 ? ASN A 476 . ? 1_555 ? 35 AC8 5 PRO A 553 ? PRO A 594 . ? 1_555 ? 36 AC8 5 NAG J . ? NAG A 1762 . ? 1_555 ? 37 AC8 5 HOH T . ? HOH A 2102 . ? 1_555 ? 38 AC9 5 GLN A 610 ? GLN A 651 . ? 1_555 ? 39 AC9 5 NAG I . ? NAG A 1761 . ? 1_555 ? 40 AC9 5 HOH T . ? HOH A 2432 . ? 1_555 ? 41 AC9 5 HOH T . ? HOH A 2437 . ? 1_555 ? 42 AC9 5 HOH T . ? HOH A 2506 . ? 1_555 ? 43 BC1 9 GLU A 235 ? GLU A 276 . ? 2_565 ? 44 BC1 9 SER A 590 ? SER A 631 . ? 1_555 ? 45 BC1 9 SER A 593 ? SER A 634 . ? 1_555 ? 46 BC1 9 ASN A 597 ? ASN A 638 . ? 1_555 ? 47 BC1 9 GLN A 699 ? GLN A 740 . ? 1_555 ? 48 BC1 9 NAG L . ? NAG A 1764 . ? 1_555 ? 49 BC1 9 HOH T . ? HOH A 1894 . ? 1_555 ? 50 BC1 9 HOH T . ? HOH A 1928 . ? 2_565 ? 51 BC1 9 HOH T . ? HOH A 2133 . ? 1_555 ? 52 BC2 4 GLU A 235 ? GLU A 276 . ? 2_565 ? 53 BC2 4 NAG K . ? NAG A 1763 . ? 1_555 ? 54 BC2 4 BMA M . ? BMA A 1765 . ? 1_555 ? 55 BC2 4 HOH T . ? HOH A 2061 . ? 2_565 ? 56 BC3 7 HIS A 71 ? HIS A 112 . ? 2_565 ? 57 BC3 7 GLU A 235 ? GLU A 276 . ? 2_565 ? 58 BC3 7 ARG A 313 ? ARG A 354 . ? 2_565 ? 59 BC3 7 NAG L . ? NAG A 1764 . ? 1_555 ? 60 BC3 7 MAN N . ? MAN A 1766 . ? 1_555 ? 61 BC3 7 HOH T . ? HOH A 2375 . ? 1_555 ? 62 BC3 7 HOH T . ? HOH A 2376 . ? 1_555 ? 63 BC4 9 PHE A 194 ? PHE A 235 . ? 7_555 ? 64 BC4 9 LYS A 199 ? LYS A 240 . ? 7_555 ? 65 BC4 9 SER A 200 ? SER A 241 . ? 7_555 ? 66 BC4 9 GLU A 235 ? GLU A 276 . ? 2_565 ? 67 BC4 9 BMA M . ? BMA A 1765 . ? 1_555 ? 68 BC4 9 HOH T . ? HOH A 1959 . ? 1_555 ? 69 BC4 9 HOH T . ? HOH A 2131 . ? 1_555 ? 70 BC4 9 HOH T . ? HOH A 2134 . ? 7_555 ? 71 BC4 9 HOH T . ? HOH A 2362 . ? 7_555 ? 72 BC5 6 JRG S . ? JRG A 1 . ? 1_555 ? 73 BC5 6 ASP A 346 ? ASP A 387 . ? 1_555 ? 74 BC5 6 GLU A 384 ? GLU A 425 . ? 1_555 ? 75 BC5 6 HIS A 512 ? HIS A 553 . ? 1_555 ? 76 BC5 6 ZN P . ? ZN A 1752 . ? 1_555 ? 77 BC5 6 HOH T . ? HOH A 2476 . ? 1_555 ? 78 BC6 7 HIS A 336 ? HIS A 377 . ? 1_555 ? 79 BC6 7 ASP A 346 ? ASP A 387 . ? 1_555 ? 80 BC6 7 GLU A 383 ? GLU A 424 . ? 1_555 ? 81 BC6 7 GLU A 384 ? GLU A 425 . ? 1_555 ? 82 BC6 7 ASP A 412 ? ASP A 453 . ? 1_555 ? 83 BC6 7 ZN O . ? ZN A 1751 . ? 1_555 ? 84 BC6 7 HOH T . ? HOH A 2476 . ? 1_555 ? 85 BC7 5 THR A 228 ? THR A 269 . ? 1_555 ? 86 BC7 5 TYR A 231 ? TYR A 272 . ? 1_555 ? 87 BC7 5 GLU A 392 ? GLU A 433 . ? 1_555 ? 88 BC7 5 GLU A 395 ? GLU A 436 . ? 1_555 ? 89 BC7 5 HOH T . ? HOH A 1773 . ? 1_555 ? 90 BC8 4 ASN A 410 ? ASN A 451 . ? 1_555 ? 91 BC8 4 ASP A 412 ? ASP A 453 . ? 1_555 ? 92 BC8 4 ARG A 493 ? ARG A 534 . ? 1_555 ? 93 BC8 4 ARG A 495 ? ARG A 536 . ? 1_555 ? 94 BC9 21 ARG A 169 ? ARG A 210 . ? 1_555 ? 95 BC9 21 ASN A 216 ? ASN A 257 . ? 1_555 ? 96 BC9 21 GLU A 383 ? GLU A 424 . ? 1_555 ? 97 BC9 21 GLU A 384 ? GLU A 425 . ? 1_555 ? 98 BC9 21 GLY A 386 ? GLY A 427 . ? 1_555 ? 99 BC9 21 ARG A 422 ? ARG A 463 . ? 1_555 ? 100 BC9 21 ASP A 424 ? ASP A 465 . ? 1_555 ? 101 BC9 21 GLY A 477 ? GLY A 518 . ? 1_555 ? 102 BC9 21 ASN A 478 ? ASN A 519 . ? 1_555 ? 103 BC9 21 ARG A 493 ? ARG A 534 . ? 1_555 ? 104 BC9 21 ARG A 495 ? ARG A 536 . ? 1_555 ? 105 BC9 21 TYR A 511 ? TYR A 552 . ? 1_555 ? 106 BC9 21 HIS A 512 ? HIS A 553 . ? 1_555 ? 107 BC9 21 LYS A 658 ? LYS A 699 . ? 1_555 ? 108 BC9 21 TYR A 659 ? TYR A 700 . ? 1_555 ? 109 BC9 21 ZN O . ? ZN A 1751 . ? 1_555 ? 110 BC9 21 HOH T . ? HOH A 1776 . ? 1_555 ? 111 BC9 21 HOH T . ? HOH A 2476 . ? 1_555 ? 112 BC9 21 HOH T . ? HOH A 2477 . ? 1_555 ? 113 BC9 21 HOH T . ? HOH A 2478 . ? 1_555 ? 114 BC9 21 HOH T . ? HOH A 2501 . ? 1_555 ? # _database_PDB_matrix.entry_id 3SJF _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 3SJF _atom_sites.fract_transf_matrix[1][1] 0.009848 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.007667 _atom_sites.fract_transf_matrix[2][3] 0.000000 _atom_sites.fract_transf_matrix[3][1] 0.000000 _atom_sites.fract_transf_matrix[3][2] 0.000000 _atom_sites.fract_transf_matrix[3][3] 0.006283 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CA CL I N O S ZN # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . LYS A 1 14 ? 16.593 45.551 82.749 1.00 58.94 ? 55 LYS A N 1 ATOM 2 C CA . LYS A 1 14 ? 16.039 46.727 82.014 1.00 57.62 ? 55 LYS A CA 1 ATOM 3 C C . LYS A 1 14 ? 15.753 46.404 80.548 1.00 55.36 ? 55 LYS A C 1 ATOM 4 O O . LYS A 1 14 ? 16.388 45.522 79.949 1.00 55.52 ? 55 LYS A O 1 ATOM 5 C CB . LYS A 1 14 ? 17.002 47.913 82.114 1.00 58.48 ? 55 LYS A CB 1 ATOM 6 C CG . LYS A 1 14 ? 16.342 49.300 82.086 1.00 60.49 ? 55 LYS A CG 1 ATOM 7 C CD . LYS A 1 14 ? 16.943 50.207 83.186 1.00 64.03 ? 55 LYS A CD 1 ATOM 8 C CE . LYS A 1 14 ? 18.443 50.469 82.965 1.00 64.70 ? 55 LYS A CE 1 ATOM 9 N NZ . LYS A 1 14 ? 19.230 50.336 84.229 1.00 68.06 ? 55 LYS A NZ 1 ATOM 10 N N . HIS A 1 15 ? 14.778 47.115 79.990 1.00 52.73 ? 56 HIS A N 1 ATOM 11 C CA . HIS A 1 15 ? 14.427 46.989 78.582 1.00 49.91 ? 56 HIS A CA 1 ATOM 12 C C . HIS A 1 15 ? 14.880 48.235 77.847 1.00 47.01 ? 56 HIS A C 1 ATOM 13 O O . HIS A 1 15 ? 14.132 49.212 77.728 1.00 48.49 ? 56 HIS A O 1 ATOM 14 C CB . HIS A 1 15 ? 12.923 46.795 78.426 1.00 49.84 ? 56 HIS A CB 1 ATOM 15 C CG . HIS A 1 15 ? 12.443 45.447 78.857 1.00 52.47 ? 56 HIS A CG 1 ATOM 16 N ND1 . HIS A 1 15 ? 11.324 45.273 79.643 1.00 54.22 ? 56 HIS A ND1 1 ATOM 17 C CD2 . HIS A 1 15 ? 12.937 44.208 78.620 1.00 53.01 ? 56 HIS A CD2 1 ATOM 18 C CE1 . HIS A 1 15 ? 11.142 43.982 79.861 1.00 56.63 ? 56 HIS A CE1 1 ATOM 19 N NE2 . HIS A 1 15 ? 12.106 43.315 79.250 1.00 55.93 ? 56 HIS A NE2 1 ATOM 20 N N . ASN A 1 16 ? 16.113 48.197 77.351 1.00 42.65 ? 57 ASN A N 1 ATOM 21 C CA . ASN A 1 16 ? 16.690 49.327 76.648 1.00 38.31 ? 57 ASN A CA 1 ATOM 22 C C . ASN A 1 16 ? 17.307 48.788 75.376 1.00 34.86 ? 57 ASN A C 1 ATOM 23 O O . ASN A 1 16 ? 17.112 47.610 75.049 1.00 32.45 ? 57 ASN A O 1 ATOM 24 C CB . ASN A 1 16 ? 17.776 49.981 77.500 1.00 37.95 ? 57 ASN A CB 1 ATOM 25 C CG . ASN A 1 16 ? 18.688 48.973 78.159 1.00 39.71 ? 57 ASN A CG 1 ATOM 26 O OD1 . ASN A 1 16 ? 18.856 47.850 77.687 1.00 37.35 ? 57 ASN A OD1 1 ATOM 27 N ND2 . ASN A 1 16 ? 19.269 49.365 79.299 1.00 41.83 ? 57 ASN A ND2 1 ATOM 28 N N . MET A 1 17 ? 18.062 49.623 74.671 1.00 34.23 ? 58 MET A N 1 ATOM 29 C CA . MET A 1 17 ? 18.547 49.128 73.379 1.00 33.16 ? 58 MET A CA 1 ATOM 30 C C . MET A 1 17 ? 19.573 48.016 73.565 1.00 33.34 ? 58 MET A C 1 ATOM 31 O O . MET A 1 17 ? 19.595 47.089 72.771 1.00 31.74 ? 58 MET A O 1 ATOM 32 C CB A MET A 1 17 ? 19.197 50.267 72.581 0.65 33.21 ? 58 MET A CB 1 ATOM 33 C CB B MET A 1 17 ? 19.052 50.179 72.418 0.35 32.12 ? 58 MET A CB 1 ATOM 34 C CG A MET A 1 17 ? 19.650 49.875 71.129 0.65 36.03 ? 58 MET A CG 1 ATOM 35 C CG B MET A 1 17 ? 19.075 49.567 71.003 0.35 29.60 ? 58 MET A CG 1 ATOM 36 S SD A MET A 1 17 ? 20.168 51.300 70.136 0.65 41.88 ? 58 MET A SD 1 ATOM 37 S SD B MET A 1 17 ? 20.245 50.369 69.970 0.35 27.52 ? 58 MET A SD 1 ATOM 38 C CE A MET A 1 17 ? 21.598 51.899 71.012 0.65 44.15 ? 58 MET A CE 1 ATOM 39 C CE B MET A 1 17 ? 19.404 51.954 69.729 0.35 25.01 ? 58 MET A CE 1 ATOM 40 N N . LYS A 1 18 ? 20.401 48.105 74.589 1.00 33.91 ? 59 LYS A N 1 ATOM 41 C CA . LYS A 1 18 ? 21.371 47.049 74.832 1.00 34.53 ? 59 LYS A CA 1 ATOM 42 C C . LYS A 1 18 ? 20.678 45.692 75.020 1.00 33.35 ? 59 LYS A C 1 ATOM 43 O O . LYS A 1 18 ? 21.151 44.684 74.507 1.00 33.50 ? 59 LYS A O 1 ATOM 44 C CB . LYS A 1 18 ? 22.230 47.381 76.056 1.00 35.89 ? 59 LYS A CB 1 ATOM 45 C CG . LYS A 1 18 ? 23.403 46.449 76.242 1.00 39.04 ? 59 LYS A CG 1 ATOM 46 C CD . LYS A 1 18 ? 24.268 46.947 77.402 1.00 45.49 ? 59 LYS A CD 1 ATOM 47 C CE . LYS A 1 18 ? 25.647 46.301 77.371 1.00 50.58 ? 59 LYS A CE 1 ATOM 48 N NZ . LYS A 1 18 ? 25.590 44.830 77.644 1.00 52.48 ? 59 LYS A NZ 1 ATOM 49 N N . ALA A 1 19 ? 19.545 45.671 75.723 1.00 33.42 ? 60 ALA A N 1 ATOM 50 C CA . ALA A 1 19 ? 18.802 44.416 75.895 1.00 33.89 ? 60 ALA A CA 1 ATOM 51 C C . ALA A 1 19 ? 18.335 43.862 74.537 1.00 32.36 ? 60 ALA A C 1 ATOM 52 O O . ALA A 1 19 ? 18.451 42.666 74.286 1.00 32.68 ? 60 ALA A O 1 ATOM 53 C CB . ALA A 1 19 ? 17.611 44.608 76.812 1.00 35.32 ? 60 ALA A CB 1 ATOM 54 N N . PHE A 1 20 ? 17.794 44.751 73.708 1.00 30.19 ? 61 PHE A N 1 ATOM 55 C CA . PHE A 1 20 ? 17.373 44.370 72.357 1.00 29.39 ? 61 PHE A CA 1 ATOM 56 C C . PHE A 1 20 ? 18.571 43.815 71.563 1.00 28.29 ? 61 PHE A C 1 ATOM 57 O O . PHE A 1 20 ? 18.499 42.721 70.977 1.00 28.18 ? 61 PHE A O 1 ATOM 58 C CB . PHE A 1 20 ? 16.709 45.536 71.641 1.00 27.60 ? 61 PHE A CB 1 ATOM 59 C CG . PHE A 1 20 ? 16.630 45.325 70.170 1.00 27.88 ? 61 PHE A CG 1 ATOM 60 C CD1 . PHE A 1 20 ? 15.671 44.459 69.634 1.00 28.30 ? 61 PHE A CD1 1 ATOM 61 C CD2 . PHE A 1 20 ? 17.560 45.911 69.344 1.00 27.13 ? 61 PHE A CD2 1 ATOM 62 C CE1 . PHE A 1 20 ? 15.631 44.223 68.239 1.00 27.98 ? 61 PHE A CE1 1 ATOM 63 C CE2 . PHE A 1 20 ? 17.521 45.692 67.941 1.00 28.40 ? 61 PHE A CE2 1 ATOM 64 C CZ . PHE A 1 20 ? 16.566 44.842 67.411 1.00 28.01 ? 61 PHE A CZ 1 ATOM 65 N N . LEU A 1 21 ? 19.672 44.555 71.551 1.00 28.36 ? 62 LEU A N 1 ATOM 66 C CA . LEU A 1 21 ? 20.822 44.148 70.745 1.00 29.05 ? 62 LEU A CA 1 ATOM 67 C C . LEU A 1 21 ? 21.447 42.837 71.237 1.00 30.18 ? 62 LEU A C 1 ATOM 68 O O . LEU A 1 21 ? 21.858 42.008 70.429 1.00 30.26 ? 62 LEU A O 1 ATOM 69 C CB . LEU A 1 21 ? 21.905 45.241 70.728 1.00 29.61 ? 62 LEU A CB 1 ATOM 70 C CG . LEU A 1 21 ? 21.510 46.554 70.040 1.00 28.40 ? 62 LEU A CG 1 ATOM 71 C CD1 . LEU A 1 21 ? 22.549 47.619 70.382 1.00 31.46 ? 62 LEU A CD1 1 ATOM 72 C CD2 . LEU A 1 21 ? 21.348 46.374 68.506 1.00 27.44 ? 62 LEU A CD2 1 ATOM 73 N N . ASP A 1 22 ? 21.496 42.649 72.550 1.00 32.00 ? 63 ASP A N 1 ATOM 74 C CA . ASP A 1 22 ? 22.095 41.430 73.110 1.00 34.19 ? 63 ASP A CA 1 ATOM 75 C C . ASP A 1 22 ? 21.289 40.176 72.792 1.00 34.13 ? 63 ASP A C 1 ATOM 76 O O . ASP A 1 22 ? 21.839 39.073 72.798 1.00 35.76 ? 63 ASP A O 1 ATOM 77 C CB . ASP A 1 22 ? 22.221 41.555 74.628 1.00 35.72 ? 63 ASP A CB 1 ATOM 78 C CG . ASP A 1 22 ? 23.386 42.443 75.057 1.00 40.22 ? 63 ASP A CG 1 ATOM 79 O OD1 . ASP A 1 22 ? 24.258 42.786 74.218 1.00 43.06 ? 63 ASP A OD1 1 ATOM 80 O OD2 . ASP A 1 22 ? 23.412 42.813 76.252 1.00 42.36 ? 63 ASP A OD2 1 ATOM 81 N N . GLU A 1 23 ? 19.993 40.337 72.538 1.00 33.38 ? 64 GLU A N 1 ATOM 82 C CA . GLU A 1 23 ? 19.135 39.201 72.263 1.00 33.20 ? 64 GLU A CA 1 ATOM 83 C C . GLU A 1 23 ? 19.394 38.624 70.860 1.00 32.20 ? 64 GLU A C 1 ATOM 84 O O . GLU A 1 23 ? 19.180 37.428 70.655 1.00 32.52 ? 64 GLU A O 1 ATOM 85 C CB . GLU A 1 23 ? 17.660 39.552 72.493 1.00 34.22 ? 64 GLU A CB 1 ATOM 86 C CG . GLU A 1 23 ? 16.628 38.428 72.297 1.00 36.17 ? 64 GLU A CG 1 ATOM 87 C CD . GLU A 1 23 ? 16.840 37.213 73.188 1.00 41.08 ? 64 GLU A CD 1 ATOM 88 O OE1 . GLU A 1 23 ? 17.190 37.367 74.391 1.00 42.72 ? 64 GLU A OE1 1 ATOM 89 O OE2 . GLU A 1 23 ? 16.681 36.074 72.690 1.00 41.01 ? 64 GLU A OE2 1 ATOM 90 N N . LEU A 1 24 ? 19.873 39.466 69.935 1.00 30.28 ? 65 LEU A N 1 ATOM 91 C CA . LEU A 1 24 ? 20.205 39.042 68.547 1.00 29.46 ? 65 LEU A CA 1 ATOM 92 C C . LEU A 1 24 ? 21.338 38.028 68.525 1.00 30.56 ? 65 LEU A C 1 ATOM 93 O O . LEU A 1 24 ? 22.375 38.266 69.133 1.00 31.03 ? 65 LEU A O 1 ATOM 94 C CB . LEU A 1 24 ? 20.656 40.259 67.745 1.00 27.77 ? 65 LEU A CB 1 ATOM 95 C CG . LEU A 1 24 ? 19.630 41.381 67.599 1.00 26.60 ? 65 LEU A CG 1 ATOM 96 C CD1 . LEU A 1 24 ? 20.346 42.578 67.030 1.00 26.66 ? 65 LEU A CD1 1 ATOM 97 C CD2 . LEU A 1 24 ? 18.441 40.964 66.681 1.00 24.94 ? 65 LEU A CD2 1 ATOM 98 N N . LYS A 1 25 ? 21.174 36.945 67.760 1.00 29.12 ? 66 LYS A N 1 ATOM 99 C CA . LYS A 1 25 ? 22.188 35.891 67.743 1.00 29.77 ? 66 LYS A CA 1 ATOM 100 C C . LYS A 1 25 ? 22.552 35.483 66.320 1.00 28.72 ? 66 LYS A C 1 ATOM 101 O O . LYS A 1 25 ? 21.663 35.218 65.511 1.00 27.91 ? 66 LYS A O 1 ATOM 102 C CB A LYS A 1 25 ? 21.657 34.660 68.482 0.65 31.07 ? 66 LYS A CB 1 ATOM 103 C CB B LYS A 1 25 ? 21.723 34.680 68.552 0.35 30.70 ? 66 LYS A CB 1 ATOM 104 C CG A LYS A 1 25 ? 21.287 34.931 69.951 0.65 34.09 ? 66 LYS A CG 1 ATOM 105 C CG B LYS A 1 25 ? 21.742 34.944 70.054 0.35 32.41 ? 66 LYS A CG 1 ATOM 106 C CD A LYS A 1 25 ? 22.550 35.022 70.810 0.65 39.21 ? 66 LYS A CD 1 ATOM 107 C CD B LYS A 1 25 ? 20.645 34.189 70.768 0.35 33.58 ? 66 LYS A CD 1 ATOM 108 C CE A LYS A 1 25 ? 22.230 34.979 72.306 0.65 41.62 ? 66 LYS A CE 1 ATOM 109 C CE B LYS A 1 25 ? 20.333 34.856 72.098 0.35 32.76 ? 66 LYS A CE 1 ATOM 110 N NZ A LYS A 1 25 ? 21.514 36.211 72.730 0.65 40.70 ? 66 LYS A NZ 1 ATOM 111 N NZ B LYS A 1 25 ? 18.923 34.628 72.487 0.35 32.82 ? 66 LYS A NZ 1 ATOM 112 N N . ALA A 1 26 ? 23.856 35.387 66.058 1.00 28.50 ? 67 ALA A N 1 ATOM 113 C CA . ALA A 1 26 ? 24.364 34.969 64.755 1.00 28.40 ? 67 ALA A CA 1 ATOM 114 C C . ALA A 1 26 ? 23.836 33.570 64.402 1.00 28.66 ? 67 ALA A C 1 ATOM 115 O O . ALA A 1 26 ? 23.500 33.317 63.217 1.00 26.61 ? 67 ALA A O 1 ATOM 116 C CB . ALA A 1 26 ? 25.915 34.990 64.772 1.00 28.67 ? 67 ALA A CB 1 ATOM 117 N N . GLU A 1 27 ? 23.769 32.681 65.410 1.00 29.81 ? 68 GLU A N 1 ATOM 118 C CA A GLU A 1 27 ? 23.357 31.305 65.135 0.50 30.72 ? 68 GLU A CA 1 ATOM 119 C CA B GLU A 1 27 ? 23.319 31.285 65.280 0.50 31.25 ? 68 GLU A CA 1 ATOM 120 C C . GLU A 1 27 ? 21.894 31.234 64.707 1.00 30.30 ? 68 GLU A C 1 ATOM 121 O O . GLU A 1 27 ? 21.547 30.378 63.885 1.00 29.37 ? 68 GLU A O 1 ATOM 122 C CB A GLU A 1 27 ? 23.651 30.366 66.315 0.50 32.06 ? 68 GLU A CB 1 ATOM 123 C CB B GLU A 1 27 ? 23.424 30.555 66.665 0.50 32.84 ? 68 GLU A CB 1 ATOM 124 C CG A GLU A 1 27 ? 23.263 28.921 66.070 0.50 34.11 ? 68 GLU A CG 1 ATOM 125 C CG B GLU A 1 27 ? 22.401 31.022 67.745 0.50 36.43 ? 68 GLU A CG 1 ATOM 126 C CD A GLU A 1 27 ? 24.026 28.314 64.915 0.50 38.27 ? 68 GLU A CD 1 ATOM 127 C CD B GLU A 1 27 ? 22.818 30.881 69.235 0.50 42.29 ? 68 GLU A CD 1 ATOM 128 O OE1 A GLU A 1 27 ? 25.272 28.426 64.906 0.50 35.48 ? 68 GLU A OE1 1 ATOM 129 O OE1 B GLU A 1 27 ? 22.064 30.218 69.979 0.50 43.65 ? 68 GLU A OE1 1 ATOM 130 O OE2 A GLU A 1 27 ? 23.369 27.739 64.013 0.50 40.76 ? 68 GLU A OE2 1 ATOM 131 O OE2 B GLU A 1 27 ? 23.852 31.444 69.682 0.50 43.37 ? 68 GLU A OE2 1 ATOM 132 N N . ASN A 1 28 ? 21.049 32.142 65.197 1.00 28.81 ? 69 ASN A N 1 ATOM 133 C CA . ASN A 1 28 ? 19.659 32.193 64.705 1.00 28.34 ? 69 ASN A CA 1 ATOM 134 C C . ASN A 1 28 ? 19.580 32.675 63.274 1.00 26.43 ? 69 ASN A C 1 ATOM 135 O O . ASN A 1 28 ? 18.806 32.141 62.483 1.00 26.38 ? 69 ASN A O 1 ATOM 136 C CB . ASN A 1 28 ? 18.776 33.067 65.592 1.00 28.86 ? 69 ASN A CB 1 ATOM 137 C CG . ASN A 1 28 ? 18.549 32.444 66.951 1.00 30.80 ? 69 ASN A CG 1 ATOM 138 O OD1 . ASN A 1 28 ? 18.563 31.214 67.102 1.00 33.42 ? 69 ASN A OD1 1 ATOM 139 N ND2 . ASN A 1 28 ? 18.370 33.281 67.956 1.00 31.33 ? 69 ASN A ND2 1 ATOM 140 N N . ILE A 1 29 ? 20.380 33.681 62.941 1.00 25.05 ? 70 ILE A N 1 ATOM 141 C CA . ILE A 1 29 ? 20.370 34.229 61.563 1.00 24.09 ? 70 ILE A CA 1 ATOM 142 C C . ILE A 1 29 ? 20.796 33.109 60.601 1.00 24.10 ? 70 ILE A C 1 ATOM 143 O O . ILE A 1 29 ? 20.189 32.931 59.543 1.00 24.51 ? 70 ILE A O 1 ATOM 144 C CB . ILE A 1 29 ? 21.286 35.469 61.440 1.00 24.21 ? 70 ILE A CB 1 ATOM 145 C CG1 . ILE A 1 29 ? 20.764 36.589 62.377 1.00 23.63 ? 70 ILE A CG1 1 ATOM 146 C CG2 . ILE A 1 29 ? 21.316 35.964 60.007 1.00 23.41 ? 70 ILE A CG2 1 ATOM 147 C CD1 . ILE A 1 29 ? 21.785 37.706 62.582 1.00 27.76 ? 70 ILE A CD1 1 ATOM 148 N N . LYS A 1 30 ? 21.811 32.335 61.009 1.00 24.33 ? 71 LYS A N 1 ATOM 149 C CA . LYS A 1 30 ? 22.293 31.214 60.192 1.00 24.91 ? 71 LYS A CA 1 ATOM 150 C C . LYS A 1 30 ? 21.174 30.182 59.965 1.00 26.27 ? 71 LYS A C 1 ATOM 151 O O . LYS A 1 30 ? 20.939 29.738 58.836 1.00 25.48 ? 71 LYS A O 1 ATOM 152 C CB . LYS A 1 30 ? 23.489 30.549 60.919 1.00 25.64 ? 71 LYS A CB 1 ATOM 153 C CG . LYS A 1 30 ? 24.047 29.333 60.200 1.00 28.18 ? 71 LYS A CG 1 ATOM 154 C CD . LYS A 1 30 ? 25.225 28.793 60.982 1.00 30.81 ? 71 LYS A CD 1 ATOM 155 C CE . LYS A 1 30 ? 25.868 27.641 60.257 1.00 34.66 ? 71 LYS A CE 1 ATOM 156 N NZ . LYS A 1 30 ? 27.038 27.089 61.057 1.00 34.92 ? 71 LYS A NZ 1 ATOM 157 N N . LYS A 1 31 ? 20.492 29.796 61.041 1.00 26.99 ? 72 LYS A N 1 ATOM 158 C CA . LYS A 1 31 ? 19.390 28.823 60.940 1.00 27.75 ? 72 LYS A CA 1 ATOM 159 C C . LYS A 1 31 ? 18.262 29.339 60.040 1.00 26.11 ? 72 LYS A C 1 ATOM 160 O O . LYS A 1 31 ? 17.723 28.602 59.225 1.00 25.30 ? 72 LYS A O 1 ATOM 161 C CB . LYS A 1 31 ? 18.834 28.466 62.326 1.00 28.96 ? 72 LYS A CB 1 ATOM 162 C CG . LYS A 1 31 ? 19.817 27.652 63.146 1.00 35.76 ? 72 LYS A CG 1 ATOM 163 C CD . LYS A 1 31 ? 19.328 27.427 64.568 1.00 40.15 ? 72 LYS A CD 1 ATOM 164 C CE . LYS A 1 31 ? 20.338 26.591 65.364 1.00 45.90 ? 72 LYS A CE 1 ATOM 165 N NZ . LYS A 1 31 ? 19.961 26.689 66.804 1.00 48.96 ? 72 LYS A NZ 1 ATOM 166 N N . PHE A 1 32 ? 17.937 30.618 60.162 1.00 24.21 ? 73 PHE A N 1 ATOM 167 C CA . PHE A 1 32 ? 16.889 31.182 59.306 1.00 23.48 ? 73 PHE A CA 1 ATOM 168 C C . PHE A 1 32 ? 17.328 31.229 57.847 1.00 22.85 ? 73 PHE A C 1 ATOM 169 O O . PHE A 1 32 ? 16.531 30.932 56.927 1.00 22.99 ? 73 PHE A O 1 ATOM 170 C CB . PHE A 1 32 ? 16.527 32.606 59.801 1.00 22.82 ? 73 PHE A CB 1 ATOM 171 C CG . PHE A 1 32 ? 15.934 32.622 61.187 1.00 24.47 ? 73 PHE A CG 1 ATOM 172 C CD1 . PHE A 1 32 ? 15.203 31.534 61.681 1.00 27.97 ? 73 PHE A CD1 1 ATOM 173 C CD2 . PHE A 1 32 ? 16.065 33.758 61.986 1.00 23.30 ? 73 PHE A CD2 1 ATOM 174 C CE1 . PHE A 1 32 ? 14.673 31.550 62.971 1.00 30.60 ? 73 PHE A CE1 1 ATOM 175 C CE2 . PHE A 1 32 ? 15.538 33.808 63.260 1.00 26.40 ? 73 PHE A CE2 1 ATOM 176 C CZ . PHE A 1 32 ? 14.807 32.722 63.765 1.00 29.17 ? 73 PHE A CZ 1 ATOM 177 N N . LEU A 1 33 ? 18.584 31.617 57.618 1.00 22.14 ? 74 LEU A N 1 ATOM 178 C CA . LEU A 1 33 ? 19.075 31.696 56.235 1.00 21.94 ? 74 LEU A CA 1 ATOM 179 C C . LEU A 1 33 ? 18.991 30.314 55.592 1.00 22.73 ? 74 LEU A C 1 ATOM 180 O O . LEU A 1 33 ? 18.492 30.188 54.491 1.00 22.63 ? 74 LEU A O 1 ATOM 181 C CB . LEU A 1 33 ? 20.521 32.220 56.152 1.00 22.94 ? 74 LEU A CB 1 ATOM 182 C CG . LEU A 1 33 ? 20.984 32.340 54.694 1.00 20.90 ? 74 LEU A CG 1 ATOM 183 C CD1 . LEU A 1 33 ? 20.232 33.442 53.927 1.00 20.36 ? 74 LEU A CD1 1 ATOM 184 C CD2 . LEU A 1 33 ? 22.488 32.645 54.615 1.00 24.72 ? 74 LEU A CD2 1 ATOM 185 N N . TYR A 1 34 ? 19.454 29.270 56.288 1.00 23.46 ? 75 TYR A N 1 ATOM 186 C CA . TYR A 1 34 ? 19.332 27.909 55.750 1.00 23.85 ? 75 TYR A CA 1 ATOM 187 C C . TYR A 1 34 ? 17.865 27.570 55.431 1.00 24.40 ? 75 TYR A C 1 ATOM 188 O O . TYR A 1 34 ? 17.540 27.071 54.345 1.00 25.06 ? 75 TYR A O 1 ATOM 189 C CB . TYR A 1 34 ? 19.927 26.913 56.763 1.00 24.35 ? 75 TYR A CB 1 ATOM 190 C CG . TYR A 1 34 ? 19.860 25.496 56.258 1.00 25.52 ? 75 TYR A CG 1 ATOM 191 C CD1 . TYR A 1 34 ? 20.866 25.007 55.439 1.00 27.04 ? 75 TYR A CD1 1 ATOM 192 C CD2 . TYR A 1 34 ? 18.757 24.697 56.531 1.00 30.08 ? 75 TYR A CD2 1 ATOM 193 C CE1 . TYR A 1 34 ? 20.816 23.709 54.946 1.00 29.79 ? 75 TYR A CE1 1 ATOM 194 C CE2 . TYR A 1 34 ? 18.685 23.370 56.040 1.00 33.74 ? 75 TYR A CE2 1 ATOM 195 C CZ . TYR A 1 34 ? 19.724 22.898 55.250 1.00 35.36 ? 75 TYR A CZ 1 ATOM 196 O OH . TYR A 1 34 ? 19.691 21.605 54.747 1.00 38.49 ? 75 TYR A OH 1 ATOM 197 N N . ASN A 1 35 ? 16.971 27.907 56.347 1.00 23.69 ? 76 ASN A N 1 ATOM 198 C CA . ASN A 1 35 ? 15.564 27.578 56.194 1.00 24.56 ? 76 ASN A CA 1 ATOM 199 C C . ASN A 1 35 ? 14.911 28.277 54.986 1.00 23.34 ? 76 ASN A C 1 ATOM 200 O O . ASN A 1 35 ? 13.965 27.723 54.369 1.00 24.17 ? 76 ASN A O 1 ATOM 201 C CB . ASN A 1 35 ? 14.844 27.962 57.467 1.00 24.97 ? 76 ASN A CB 1 ATOM 202 C CG . ASN A 1 35 ? 13.364 27.665 57.422 1.00 26.39 ? 76 ASN A CG 1 ATOM 203 O OD1 . ASN A 1 35 ? 12.550 28.503 57.043 1.00 27.17 ? 76 ASN A OD1 1 ATOM 204 N ND2 . ASN A 1 35 ? 13.011 26.444 57.802 1.00 28.84 ? 76 ASN A ND2 1 ATOM 205 N N . PHE A 1 36 ? 15.403 29.467 54.638 1.00 22.23 ? 77 PHE A N 1 ATOM 206 C CA . PHE A 1 36 ? 14.769 30.264 53.589 1.00 21.88 ? 77 PHE A CA 1 ATOM 207 C C . PHE A 1 36 ? 15.349 30.011 52.200 1.00 21.80 ? 77 PHE A C 1 ATOM 208 O O . PHE A 1 36 ? 14.883 30.652 51.236 1.00 21.57 ? 77 PHE A O 1 ATOM 209 C CB . PHE A 1 36 ? 14.969 31.788 53.855 1.00 21.05 ? 77 PHE A CB 1 ATOM 210 C CG . PHE A 1 36 ? 14.249 32.335 55.063 1.00 21.54 ? 77 PHE A CG 1 ATOM 211 C CD1 . PHE A 1 36 ? 13.289 31.577 55.776 1.00 23.33 ? 77 PHE A CD1 1 ATOM 212 C CD2 . PHE A 1 36 ? 14.574 33.627 55.517 1.00 21.98 ? 77 PHE A CD2 1 ATOM 213 C CE1 . PHE A 1 36 ? 12.642 32.119 56.921 1.00 23.42 ? 77 PHE A CE1 1 ATOM 214 C CE2 . PHE A 1 36 ? 13.910 34.203 56.640 1.00 22.34 ? 77 PHE A CE2 1 ATOM 215 C CZ . PHE A 1 36 ? 12.938 33.457 57.336 1.00 23.67 ? 77 PHE A CZ 1 ATOM 216 N N . THR A 1 37 ? 16.387 29.144 52.082 1.00 21.77 ? 78 THR A N 1 ATOM 217 C CA . THR A 1 37 ? 17.127 29.072 50.811 1.00 21.89 ? 78 THR A CA 1 ATOM 218 C C . THR A 1 37 ? 17.217 27.664 50.217 1.00 22.88 ? 78 THR A C 1 ATOM 219 O O . THR A 1 37 ? 18.044 27.412 49.348 1.00 23.60 ? 78 THR A O 1 ATOM 220 C CB . THR A 1 37 ? 18.573 29.595 51.013 1.00 21.37 ? 78 THR A CB 1 ATOM 221 O OG1 . THR A 1 37 ? 19.161 28.857 52.093 1.00 22.09 ? 78 THR A OG1 1 ATOM 222 C CG2 . THR A 1 37 ? 18.557 31.111 51.354 1.00 20.53 ? 78 THR A CG2 1 ATOM 223 N N . GLN A 1 38 ? 16.384 26.744 50.700 1.00 23.24 ? 79 GLN A N 1 ATOM 224 C CA . GLN A 1 38 ? 16.447 25.349 50.231 1.00 25.68 ? 79 GLN A CA 1 ATOM 225 C C . GLN A 1 38 ? 15.755 25.117 48.896 1.00 25.85 ? 79 GLN A C 1 ATOM 226 O O . GLN A 1 38 ? 16.076 24.137 48.204 1.00 27.31 ? 79 GLN A O 1 ATOM 227 C CB . GLN A 1 38 ? 15.856 24.417 51.299 1.00 26.74 ? 79 GLN A CB 1 ATOM 228 C CG . GLN A 1 38 ? 16.674 24.430 52.587 1.00 28.32 ? 79 GLN A CG 1 ATOM 229 C CD . GLN A 1 38 ? 18.170 24.282 52.288 1.00 32.50 ? 79 GLN A CD 1 ATOM 230 O OE1 . GLN A 1 38 ? 18.592 23.210 51.851 1.00 36.07 ? 79 GLN A OE1 1 ATOM 231 N NE2 . GLN A 1 38 ? 18.967 25.363 52.477 1.00 32.23 ? 79 GLN A NE2 1 ATOM 232 N N . ILE A 1 39 ? 14.759 25.952 48.591 1.00 25.66 ? 80 ILE A N 1 ATOM 233 C CA . ILE A 1 39 ? 13.995 25.863 47.332 1.00 26.06 ? 80 ILE A CA 1 ATOM 234 C C . ILE A 1 39 ? 13.820 27.251 46.762 1.00 23.96 ? 80 ILE A C 1 ATOM 235 O O . ILE A 1 39 ? 13.932 28.235 47.531 1.00 24.38 ? 80 ILE A O 1 ATOM 236 C CB . ILE A 1 39 ? 12.595 25.238 47.549 1.00 26.90 ? 80 ILE A CB 1 ATOM 237 C CG1 . ILE A 1 39 ? 11.721 26.153 48.385 1.00 27.70 ? 80 ILE A CG1 1 ATOM 238 C CG2 . ILE A 1 39 ? 12.713 23.769 48.099 1.00 30.46 ? 80 ILE A CG2 1 ATOM 239 C CD1 . ILE A 1 39 ? 10.327 25.627 48.534 1.00 31.84 ? 80 ILE A CD1 1 ATOM 240 N N . PRO A 1 40 ? 13.556 27.353 45.442 1.00 23.48 ? 81 PRO A N 1 ATOM 241 C CA . PRO A 1 40 ? 13.350 28.696 44.888 1.00 23.18 ? 81 PRO A CA 1 ATOM 242 C C . PRO A 1 40 ? 12.092 29.352 45.465 1.00 22.42 ? 81 PRO A C 1 ATOM 243 O O . PRO A 1 40 ? 11.095 28.663 45.768 1.00 24.05 ? 81 PRO A O 1 ATOM 244 C CB . PRO A 1 40 ? 13.190 28.430 43.377 1.00 23.72 ? 81 PRO A CB 1 ATOM 245 C CG . PRO A 1 40 ? 13.940 27.102 43.148 1.00 24.57 ? 81 PRO A CG 1 ATOM 246 C CD . PRO A 1 40 ? 13.552 26.317 44.391 1.00 25.03 ? 81 PRO A CD 1 ATOM 247 N N . HIS A 1 41 ? 12.111 30.679 45.580 1.00 20.36 ? 82 HIS A N 1 ATOM 248 C CA . HIS A 1 41 ? 10.914 31.442 46.026 1.00 20.69 ? 82 HIS A CA 1 ATOM 249 C C . HIS A 1 41 ? 10.572 32.576 45.041 1.00 19.30 ? 82 HIS A C 1 ATOM 250 O O . HIS A 1 41 ? 10.459 33.740 45.417 1.00 20.03 ? 82 HIS A O 1 ATOM 251 C CB . HIS A 1 41 ? 11.107 31.998 47.452 1.00 22.05 ? 82 HIS A CB 1 ATOM 252 C CG . HIS A 1 41 ? 11.285 30.916 48.467 1.00 21.36 ? 82 HIS A CG 1 ATOM 253 N ND1 . HIS A 1 41 ? 12.521 30.607 48.999 1.00 22.56 ? 82 HIS A ND1 1 ATOM 254 C CD2 . HIS A 1 41 ? 10.406 30.021 48.978 1.00 21.01 ? 82 HIS A CD2 1 ATOM 255 C CE1 . HIS A 1 41 ? 12.383 29.591 49.837 1.00 22.18 ? 82 HIS A CE1 1 ATOM 256 N NE2 . HIS A 1 41 ? 11.111 29.214 49.842 1.00 23.25 ? 82 HIS A NE2 1 ATOM 257 N N . LEU A 1 42 ? 10.388 32.200 43.784 1.00 19.99 ? 83 LEU A N 1 ATOM 258 C CA . LEU A 1 42 ? 10.095 33.170 42.739 1.00 20.07 ? 83 LEU A CA 1 ATOM 259 C C . LEU A 1 42 ? 8.728 33.792 42.985 1.00 18.99 ? 83 LEU A C 1 ATOM 260 O O . LEU A 1 42 ? 7.752 33.118 43.356 1.00 20.51 ? 83 LEU A O 1 ATOM 261 C CB . LEU A 1 42 ? 10.146 32.474 41.352 1.00 20.06 ? 83 LEU A CB 1 ATOM 262 C CG . LEU A 1 42 ? 9.979 33.385 40.121 1.00 19.11 ? 83 LEU A CG 1 ATOM 263 C CD1 . LEU A 1 42 ? 11.141 34.328 39.914 1.00 20.64 ? 83 LEU A CD1 1 ATOM 264 C CD2 . LEU A 1 42 ? 9.898 32.358 38.842 1.00 20.28 ? 83 LEU A CD2 1 ATOM 265 N N . ALA A 1 43 ? 8.654 35.115 42.824 1.00 18.66 ? 84 ALA A N 1 ATOM 266 C CA . ALA A 1 43 ? 7.363 35.810 42.980 1.00 18.43 ? 84 ALA A CA 1 ATOM 267 C C . ALA A 1 43 ? 6.267 35.187 42.126 1.00 18.76 ? 84 ALA A C 1 ATOM 268 O O . ALA A 1 43 ? 6.500 34.792 40.968 1.00 19.36 ? 84 ALA A O 1 ATOM 269 C CB . ALA A 1 43 ? 7.491 37.305 42.633 1.00 18.10 ? 84 ALA A CB 1 ATOM 270 N N . GLY A 1 44 ? 5.094 35.019 42.739 1.00 19.68 ? 85 GLY A N 1 ATOM 271 C CA . GLY A 1 44 ? 3.924 34.494 42.024 1.00 21.78 ? 85 GLY A CA 1 ATOM 272 C C . GLY A 1 44 ? 3.828 32.993 42.049 1.00 23.80 ? 85 GLY A C 1 ATOM 273 O O . GLY A 1 44 ? 2.833 32.445 41.545 1.00 25.44 ? 85 GLY A O 1 ATOM 274 N N . THR A 1 45 ? 4.825 32.305 42.612 1.00 22.04 ? 86 THR A N 1 ATOM 275 C CA . THR A 1 45 ? 4.796 30.841 42.640 1.00 22.46 ? 86 THR A CA 1 ATOM 276 C C . THR A 1 45 ? 4.270 30.323 43.976 1.00 23.31 ? 86 THR A C 1 ATOM 277 O O . THR A 1 45 ? 4.299 31.018 44.996 1.00 22.90 ? 86 THR A O 1 ATOM 278 C CB . THR A 1 45 ? 6.198 30.216 42.371 1.00 22.62 ? 86 THR A CB 1 ATOM 279 O OG1 . THR A 1 45 ? 7.083 30.535 43.465 1.00 23.19 ? 86 THR A OG1 1 ATOM 280 C CG2 . THR A 1 45 ? 6.799 30.713 41.038 1.00 23.68 ? 86 THR A CG2 1 ATOM 281 N N . GLU A 1 46 ? 3.809 29.071 43.968 1.00 24.56 ? 87 GLU A N 1 ATOM 282 C CA . GLU A 1 46 ? 3.275 28.446 45.180 1.00 25.76 ? 87 GLU A CA 1 ATOM 283 C C . GLU A 1 46 ? 4.298 28.405 46.339 1.00 24.97 ? 87 GLU A C 1 ATOM 284 O O . GLU A 1 46 ? 3.924 28.642 47.500 1.00 25.27 ? 87 GLU A O 1 ATOM 285 C CB . GLU A 1 46 ? 2.753 27.030 44.867 1.00 28.76 ? 87 GLU A CB 1 ATOM 286 C CG . GLU A 1 46 ? 2.227 26.300 46.096 1.00 34.63 ? 87 GLU A CG 1 ATOM 287 C CD . GLU A 1 46 ? 0.933 26.862 46.687 1.00 43.90 ? 87 GLU A CD 1 ATOM 288 O OE1 . GLU A 1 46 ? 0.585 26.430 47.821 1.00 47.10 ? 87 GLU A OE1 1 ATOM 289 O OE2 . GLU A 1 46 ? 0.256 27.716 46.056 1.00 47.22 ? 87 GLU A OE2 1 ATOM 290 N N A GLN A 1 47 ? 5.548 28.105 45.988 0.50 24.43 ? 88 GLN A N 1 ATOM 291 N N B GLN A 1 47 ? 5.558 28.118 46.051 0.50 25.38 ? 88 GLN A N 1 ATOM 292 C CA A GLN A 1 47 ? 6.663 28.061 46.927 0.50 23.79 ? 88 GLN A CA 1 ATOM 293 C CA B GLN A 1 47 ? 6.524 28.030 47.141 0.50 25.53 ? 88 GLN A CA 1 ATOM 294 C C A GLN A 1 47 ? 6.748 29.349 47.743 0.50 22.78 ? 88 GLN A C 1 ATOM 295 C C B GLN A 1 47 ? 6.815 29.384 47.800 0.50 24.06 ? 88 GLN A C 1 ATOM 296 O O A GLN A 1 47 ? 6.893 29.327 48.967 0.50 22.51 ? 88 GLN A O 1 ATOM 297 O O B GLN A 1 47 ? 7.173 29.436 48.976 0.50 23.57 ? 88 GLN A O 1 ATOM 298 C CB A GLN A 1 47 ? 7.978 27.813 46.175 0.50 23.31 ? 88 GLN A CB 1 ATOM 299 C CB B GLN A 1 47 ? 7.795 27.298 46.712 0.50 26.58 ? 88 GLN A CB 1 ATOM 300 C CG A GLN A 1 47 ? 8.096 26.373 45.605 0.50 25.36 ? 88 GLN A CG 1 ATOM 301 C CG B GLN A 1 47 ? 7.584 25.787 46.508 0.50 30.92 ? 88 GLN A CG 1 ATOM 302 C CD A GLN A 1 47 ? 7.350 26.160 44.292 0.50 28.98 ? 88 GLN A CD 1 ATOM 303 C CD B GLN A 1 47 ? 6.842 25.069 47.666 0.50 36.94 ? 88 GLN A CD 1 ATOM 304 O OE1 A GLN A 1 47 ? 6.881 27.103 43.649 0.50 23.57 ? 88 GLN A OE1 1 ATOM 305 O OE1 B GLN A 1 47 ? 6.007 24.195 47.423 0.50 40.97 ? 88 GLN A OE1 1 ATOM 306 N NE2 A GLN A 1 47 ? 7.276 24.899 43.865 0.50 31.01 ? 88 GLN A NE2 1 ATOM 307 N NE2 B GLN A 1 47 ? 7.141 25.438 48.911 0.50 38.14 ? 88 GLN A NE2 1 ATOM 308 N N . ASN A 1 48 ? 6.645 30.474 47.057 1.00 22.42 ? 89 ASN A N 1 ATOM 309 C CA A ASN A 1 48 ? 6.778 31.764 47.734 0.50 21.81 ? 89 ASN A CA 1 ATOM 310 C CA B ASN A 1 48 ? 6.757 31.804 47.659 0.50 23.14 ? 89 ASN A CA 1 ATOM 311 C C . ASN A 1 48 ? 5.550 32.102 48.590 1.00 24.02 ? 89 ASN A C 1 ATOM 312 O O . ASN A 1 48 ? 5.701 32.728 49.664 1.00 25.03 ? 89 ASN A O 1 ATOM 313 C CB A ASN A 1 48 ? 7.087 32.878 46.734 0.50 21.16 ? 89 ASN A CB 1 ATOM 314 C CB B ASN A 1 48 ? 6.900 32.847 46.539 0.50 23.08 ? 89 ASN A CB 1 ATOM 315 C CG A ASN A 1 48 ? 7.644 34.109 47.411 0.50 18.15 ? 89 ASN A CG 1 ATOM 316 C CG B ASN A 1 48 ? 6.834 34.257 47.055 0.50 25.08 ? 89 ASN A CG 1 ATOM 317 O OD1 A ASN A 1 48 ? 8.377 34.005 48.395 0.50 15.15 ? 89 ASN A OD1 1 ATOM 318 O OD1 B ASN A 1 48 ? 5.876 34.623 47.718 0.50 28.72 ? 89 ASN A OD1 1 ATOM 319 N ND2 A ASN A 1 48 ? 7.305 35.288 46.879 0.50 17.62 ? 89 ASN A ND2 1 ATOM 320 N ND2 B ASN A 1 48 ? 7.835 35.059 46.748 0.50 27.26 ? 89 ASN A ND2 1 ATOM 321 N N . PHE A 1 49 ? 4.349 31.657 48.176 1.00 22.94 ? 90 PHE A N 1 ATOM 322 C CA . PHE A 1 49 ? 3.132 31.789 48.999 1.00 23.79 ? 90 PHE A CA 1 ATOM 323 C C . PHE A 1 49 ? 3.277 30.941 50.260 1.00 24.20 ? 90 PHE A C 1 ATOM 324 O O . PHE A 1 49 ? 2.965 31.396 51.367 1.00 23.48 ? 90 PHE A O 1 ATOM 325 C CB . PHE A 1 49 ? 1.882 31.359 48.186 1.00 24.25 ? 90 PHE A CB 1 ATOM 326 C CG . PHE A 1 49 ? 0.597 31.305 48.978 1.00 26.72 ? 90 PHE A CG 1 ATOM 327 C CD1 . PHE A 1 49 ? 0.164 32.367 49.787 1.00 26.81 ? 90 PHE A CD1 1 ATOM 328 C CD2 . PHE A 1 49 ? -0.214 30.178 48.872 1.00 34.24 ? 90 PHE A CD2 1 ATOM 329 C CE1 . PHE A 1 49 ? -1.051 32.315 50.469 1.00 28.52 ? 90 PHE A CE1 1 ATOM 330 C CE2 . PHE A 1 49 ? -1.441 30.108 49.573 1.00 38.99 ? 90 PHE A CE2 1 ATOM 331 C CZ . PHE A 1 49 ? -1.850 31.178 50.371 1.00 34.94 ? 90 PHE A CZ 1 ATOM 332 N N A GLN A 1 50 ? 3.798 29.721 50.114 0.60 24.24 ? 91 GLN A N 1 ATOM 333 N N B GLN A 1 50 ? 3.805 29.727 50.100 0.40 24.16 ? 91 GLN A N 1 ATOM 334 C CA A GLN A 1 50 ? 4.028 28.909 51.313 0.60 25.47 ? 91 GLN A CA 1 ATOM 335 C CA B GLN A 1 50 ? 4.077 28.870 51.256 0.40 25.08 ? 91 GLN A CA 1 ATOM 336 C C A GLN A 1 50 ? 5.011 29.560 52.295 0.60 24.27 ? 91 GLN A C 1 ATOM 337 C C B GLN A 1 50 ? 5.037 29.506 52.272 0.40 24.19 ? 91 GLN A C 1 ATOM 338 O O A GLN A 1 50 ? 4.765 29.537 53.511 0.60 24.14 ? 91 GLN A O 1 ATOM 339 O O B GLN A 1 50 ? 4.797 29.427 53.485 0.40 24.40 ? 91 GLN A O 1 ATOM 340 C CB A GLN A 1 50 ? 4.454 27.483 50.959 0.60 26.14 ? 91 GLN A CB 1 ATOM 341 C CB B GLN A 1 50 ? 4.564 27.493 50.799 0.40 25.50 ? 91 GLN A CB 1 ATOM 342 C CG A GLN A 1 50 ? 3.336 26.673 50.297 0.60 29.98 ? 91 GLN A CG 1 ATOM 343 C CG B GLN A 1 50 ? 3.422 26.650 50.250 0.40 28.08 ? 91 GLN A CG 1 ATOM 344 C CD A GLN A 1 50 ? 2.075 26.529 51.147 0.60 34.81 ? 91 GLN A CD 1 ATOM 345 C CD B GLN A 1 50 ? 3.879 25.394 49.529 0.40 29.72 ? 91 GLN A CD 1 ATOM 346 O OE1 A GLN A 1 50 ? 0.962 26.523 50.613 0.60 38.88 ? 91 GLN A OE1 1 ATOM 347 O OE1 B GLN A 1 50 ? 4.982 25.328 48.987 0.40 31.43 ? 91 GLN A OE1 1 ATOM 348 N NE2 A GLN A 1 50 ? 2.238 26.379 52.466 0.60 35.07 ? 91 GLN A NE2 1 ATOM 349 N NE2 B GLN A 1 50 ? 3.009 24.393 49.495 0.40 34.11 ? 91 GLN A NE2 1 ATOM 350 N N . LEU A 1 51 ? 6.094 30.156 51.779 1.00 23.26 ? 92 LEU A N 1 ATOM 351 C CA . LEU A 1 51 ? 7.037 30.857 52.655 1.00 22.49 ? 92 LEU A CA 1 ATOM 352 C C . LEU A 1 51 ? 6.360 32.046 53.337 1.00 21.66 ? 92 LEU A C 1 ATOM 353 O O . LEU A 1 51 ? 6.566 32.273 54.544 1.00 21.68 ? 92 LEU A O 1 ATOM 354 C CB . LEU A 1 51 ? 8.319 31.273 51.904 1.00 21.27 ? 92 LEU A CB 1 ATOM 355 C CG . LEU A 1 51 ? 9.372 31.912 52.791 1.00 22.28 ? 92 LEU A CG 1 ATOM 356 C CD1 . LEU A 1 51 ? 9.858 30.945 53.934 1.00 24.40 ? 92 LEU A CD1 1 ATOM 357 C CD2 . LEU A 1 51 ? 10.552 32.346 51.923 1.00 21.83 ? 92 LEU A CD2 1 ATOM 358 N N . ALA A 1 52 ? 5.531 32.772 52.596 1.00 20.51 ? 93 ALA A N 1 ATOM 359 C CA . ALA A 1 52 ? 4.775 33.870 53.219 1.00 21.07 ? 93 ALA A CA 1 ATOM 360 C C . ALA A 1 52 ? 3.957 33.365 54.399 1.00 21.79 ? 93 ALA A C 1 ATOM 361 O O . ALA A 1 52 ? 3.918 34.007 55.465 1.00 21.61 ? 93 ALA A O 1 ATOM 362 C CB . ALA A 1 52 ? 3.845 34.543 52.195 1.00 21.77 ? 93 ALA A CB 1 ATOM 363 N N . LYS A 1 53 ? 3.282 32.235 54.214 1.00 22.24 ? 94 LYS A N 1 ATOM 364 C CA . LYS A 1 53 ? 2.458 31.709 55.310 1.00 23.63 ? 94 LYS A CA 1 ATOM 365 C C . LYS A 1 53 ? 3.296 31.276 56.508 1.00 23.52 ? 94 LYS A C 1 ATOM 366 O O . LYS A 1 53 ? 2.883 31.441 57.672 1.00 24.09 ? 94 LYS A O 1 ATOM 367 C CB . LYS A 1 53 ? 1.567 30.565 54.788 1.00 24.78 ? 94 LYS A CB 1 ATOM 368 C CG . LYS A 1 53 ? 0.440 31.112 53.921 1.00 27.56 ? 94 LYS A CG 1 ATOM 369 C CD . LYS A 1 53 ? -0.542 30.021 53.549 1.00 37.02 ? 94 LYS A CD 1 ATOM 370 C CE . LYS A 1 53 ? 0.030 29.181 52.436 1.00 40.02 ? 94 LYS A CE 1 ATOM 371 N NZ . LYS A 1 53 ? -0.862 28.048 52.035 1.00 45.91 ? 94 LYS A NZ 1 ATOM 372 N N . GLN A 1 54 ? 4.481 30.731 56.226 1.00 23.23 ? 95 GLN A N 1 ATOM 373 C CA . GLN A 1 54 ? 5.400 30.318 57.310 1.00 24.28 ? 95 GLN A CA 1 ATOM 374 C C . GLN A 1 54 ? 5.854 31.547 58.114 1.00 24.14 ? 95 GLN A C 1 ATOM 375 O O . GLN A 1 54 ? 5.833 31.534 59.332 1.00 25.40 ? 95 GLN A O 1 ATOM 376 C CB . GLN A 1 54 ? 6.613 29.610 56.717 1.00 23.67 ? 95 GLN A CB 1 ATOM 377 C CG . GLN A 1 54 ? 7.642 29.276 57.803 1.00 24.86 ? 95 GLN A CG 1 ATOM 378 C CD . GLN A 1 54 ? 8.979 28.932 57.217 1.00 25.67 ? 95 GLN A CD 1 ATOM 379 O OE1 . GLN A 1 54 ? 9.066 28.186 56.220 1.00 25.91 ? 95 GLN A OE1 1 ATOM 380 N NE2 . GLN A 1 54 ? 10.036 29.437 57.843 1.00 26.42 ? 95 GLN A NE2 1 ATOM 381 N N . ILE A 1 55 ? 6.237 32.614 57.404 1.00 23.40 ? 96 ILE A N 1 ATOM 382 C CA . ILE A 1 55 ? 6.708 33.835 58.066 1.00 23.06 ? 96 ILE A CA 1 ATOM 383 C C . ILE A 1 55 ? 5.587 34.436 58.898 1.00 22.78 ? 96 ILE A C 1 ATOM 384 O O . ILE A 1 55 ? 5.794 34.840 60.068 1.00 22.99 ? 96 ILE A O 1 ATOM 385 C CB . ILE A 1 55 ? 7.240 34.849 57.036 1.00 22.61 ? 96 ILE A CB 1 ATOM 386 C CG1 A ILE A 1 55 ? 8.446 34.304 56.276 0.65 25.01 ? 96 ILE A CG1 1 ATOM 387 C CG1 B ILE A 1 55 ? 8.578 34.313 56.513 0.35 22.29 ? 96 ILE A CG1 1 ATOM 388 C CG2 . ILE A 1 55 ? 7.504 36.224 57.720 1.00 23.41 ? 96 ILE A CG2 1 ATOM 389 C CD1 A ILE A 1 55 ? 9.601 34.063 57.104 0.65 26.12 ? 96 ILE A CD1 1 ATOM 390 C CD1 B ILE A 1 55 ? 9.058 34.929 55.220 0.35 18.58 ? 96 ILE A CD1 1 ATOM 391 N N . GLN A 1 56 ? 4.390 34.478 58.313 1.00 22.69 ? 97 GLN A N 1 ATOM 392 C CA . GLN A 1 56 ? 3.242 34.987 59.054 1.00 22.86 ? 97 GLN A CA 1 ATOM 393 C C . GLN A 1 56 ? 3.065 34.209 60.358 1.00 24.58 ? 97 GLN A C 1 ATOM 394 O O . GLN A 1 56 ? 2.864 34.825 61.431 1.00 25.41 ? 97 GLN A O 1 ATOM 395 C CB . GLN A 1 56 ? 1.990 34.874 58.195 1.00 23.43 ? 97 GLN A CB 1 ATOM 396 C CG . GLN A 1 56 ? 0.685 35.243 58.967 1.00 24.75 ? 97 GLN A CG 1 ATOM 397 C CD . GLN A 1 56 ? -0.559 35.036 58.117 1.00 27.66 ? 97 GLN A CD 1 ATOM 398 O OE1 . GLN A 1 56 ? -0.624 34.137 57.257 1.00 28.87 ? 97 GLN A OE1 1 ATOM 399 N NE2 . GLN A 1 56 ? -1.563 35.877 58.352 1.00 25.96 ? 97 GLN A NE2 1 ATOM 400 N N . SER A 1 57 ? 3.122 32.877 60.279 1.00 24.91 ? 98 SER A N 1 ATOM 401 C CA . SER A 1 57 ? 2.925 32.055 61.487 1.00 26.14 ? 98 SER A CA 1 ATOM 402 C C . SER A 1 57 ? 4.021 32.298 62.527 1.00 25.72 ? 98 SER A C 1 ATOM 403 O O . SER A 1 57 ? 3.750 32.422 63.733 1.00 26.32 ? 98 SER A O 1 ATOM 404 C CB . SER A 1 57 ? 2.889 30.575 61.084 1.00 26.47 ? 98 SER A CB 1 ATOM 405 O OG A SER A 1 57 ? 2.709 29.773 62.223 0.50 25.44 ? 98 SER A OG 1 ATOM 406 O OG B SER A 1 57 ? 1.597 30.259 60.562 0.50 30.09 ? 98 SER A OG 1 ATOM 407 N N . GLN A 1 58 ? 5.262 32.386 62.055 1.00 24.60 ? 99 GLN A N 1 ATOM 408 C CA . GLN A 1 58 ? 6.397 32.568 62.955 1.00 25.50 ? 99 GLN A CA 1 ATOM 409 C C . GLN A 1 58 ? 6.400 33.945 63.602 1.00 24.74 ? 99 GLN A C 1 ATOM 410 O O . GLN A 1 58 ? 6.717 34.057 64.789 1.00 25.42 ? 99 GLN A O 1 ATOM 411 C CB . GLN A 1 58 ? 7.707 32.320 62.225 1.00 24.91 ? 99 GLN A CB 1 ATOM 412 C CG . GLN A 1 58 ? 7.866 30.814 61.895 1.00 27.69 ? 99 GLN A CG 1 ATOM 413 C CD . GLN A 1 58 ? 9.225 30.511 61.315 1.00 31.49 ? 99 GLN A CD 1 ATOM 414 O OE1 . GLN A 1 58 ? 9.599 31.061 60.293 1.00 30.33 ? 99 GLN A OE1 1 ATOM 415 N NE2 . GLN A 1 58 ? 9.970 29.632 61.982 1.00 38.93 ? 99 GLN A NE2 1 ATOM 416 N N . TRP A 1 59 ? 6.087 35.000 62.831 1.00 23.41 ? 100 TRP A N 1 ATOM 417 C CA . TRP A 1 59 ? 6.000 36.331 63.440 1.00 23.22 ? 100 TRP A CA 1 ATOM 418 C C . TRP A 1 59 ? 4.925 36.403 64.524 1.00 25.08 ? 100 TRP A C 1 ATOM 419 O O . TRP A 1 59 ? 5.083 37.122 65.515 1.00 25.46 ? 100 TRP A O 1 ATOM 420 C CB . TRP A 1 59 ? 5.736 37.402 62.357 1.00 22.24 ? 100 TRP A CB 1 ATOM 421 C CG . TRP A 1 59 ? 6.948 37.693 61.556 1.00 20.49 ? 100 TRP A CG 1 ATOM 422 C CD1 . TRP A 1 59 ? 8.159 37.046 61.609 1.00 21.80 ? 100 TRP A CD1 1 ATOM 423 C CD2 . TRP A 1 59 ? 7.067 38.674 60.526 1.00 20.39 ? 100 TRP A CD2 1 ATOM 424 N NE1 . TRP A 1 59 ? 9.039 37.597 60.702 1.00 22.44 ? 100 TRP A NE1 1 ATOM 425 C CE2 . TRP A 1 59 ? 8.394 38.598 60.021 1.00 19.81 ? 100 TRP A CE2 1 ATOM 426 C CE3 . TRP A 1 59 ? 6.187 39.636 59.999 1.00 21.54 ? 100 TRP A CE3 1 ATOM 427 C CZ2 . TRP A 1 59 ? 8.867 39.439 58.975 1.00 20.25 ? 100 TRP A CZ2 1 ATOM 428 C CZ3 . TRP A 1 59 ? 6.632 40.468 58.965 1.00 20.24 ? 100 TRP A CZ3 1 ATOM 429 C CH2 . TRP A 1 59 ? 7.968 40.366 58.460 1.00 19.71 ? 100 TRP A CH2 1 ATOM 430 N N . LYS A 1 60 ? 3.832 35.668 64.326 1.00 25.68 ? 101 LYS A N 1 ATOM 431 C CA A LYS A 1 60 ? 2.791 35.552 65.356 0.50 28.17 ? 101 LYS A CA 1 ATOM 432 C CA B LYS A 1 60 ? 2.790 35.575 65.354 0.50 27.85 ? 101 LYS A CA 1 ATOM 433 C C . LYS A 1 60 ? 3.357 34.884 66.618 1.00 28.54 ? 101 LYS A C 1 ATOM 434 O O . LYS A 1 60 ? 3.169 35.396 67.747 1.00 29.97 ? 101 LYS A O 1 ATOM 435 C CB A LYS A 1 60 ? 1.593 34.742 64.841 0.50 28.94 ? 101 LYS A CB 1 ATOM 436 C CB B LYS A 1 60 ? 1.574 34.809 64.813 0.50 28.39 ? 101 LYS A CB 1 ATOM 437 C CG A LYS A 1 60 ? 0.479 35.580 64.259 0.50 31.61 ? 101 LYS A CG 1 ATOM 438 C CG B LYS A 1 60 ? 0.848 35.492 63.658 0.50 29.25 ? 101 LYS A CG 1 ATOM 439 C CD A LYS A 1 60 ? -0.703 34.738 63.767 0.50 35.02 ? 101 LYS A CD 1 ATOM 440 C CD B LYS A 1 60 ? -0.134 34.547 62.957 0.50 31.53 ? 101 LYS A CD 1 ATOM 441 C CE A LYS A 1 60 ? -1.483 35.498 62.671 0.50 36.02 ? 101 LYS A CE 1 ATOM 442 C CE B LYS A 1 60 ? -1.222 35.339 62.214 0.50 33.10 ? 101 LYS A CE 1 ATOM 443 N NZ A LYS A 1 60 ? -2.787 36.026 63.131 0.50 38.53 ? 101 LYS A NZ 1 ATOM 444 N NZ B LYS A 1 60 ? -2.358 34.429 61.855 0.50 35.80 ? 101 LYS A NZ 1 ATOM 445 N N A GLU A 1 61 ? 4.043 33.760 66.456 0.40 28.58 ? 102 GLU A N 1 ATOM 446 N N B GLU A 1 61 ? 4.047 33.755 66.414 0.60 28.76 ? 102 GLU A N 1 ATOM 447 C CA A GLU A 1 61 ? 4.582 33.042 67.616 0.40 29.39 ? 102 GLU A CA 1 ATOM 448 C CA B GLU A 1 61 ? 4.686 32.958 67.485 0.60 30.08 ? 102 GLU A CA 1 ATOM 449 C C A GLU A 1 61 ? 5.752 33.803 68.254 0.40 29.05 ? 102 GLU A C 1 ATOM 450 C C B GLU A 1 61 ? 5.666 33.863 68.242 0.60 29.48 ? 102 GLU A C 1 ATOM 451 O O A GLU A 1 61 ? 6.019 33.640 69.454 0.40 29.35 ? 102 GLU A O 1 ATOM 452 O O B GLU A 1 61 ? 5.718 33.858 69.493 0.60 29.42 ? 102 GLU A O 1 ATOM 453 C CB A GLU A 1 61 ? 4.960 31.602 67.251 0.40 29.98 ? 102 GLU A CB 1 ATOM 454 C CB B GLU A 1 61 ? 5.446 31.741 66.895 0.60 30.78 ? 102 GLU A CB 1 ATOM 455 C CG A GLU A 1 61 ? 5.975 30.944 68.191 0.40 33.12 ? 102 GLU A CG 1 ATOM 456 C CG B GLU A 1 61 ? 4.597 30.697 66.119 0.60 35.42 ? 102 GLU A CG 1 ATOM 457 C CD A GLU A 1 61 ? 5.390 30.517 69.522 0.40 40.30 ? 102 GLU A CD 1 ATOM 458 C CD B GLU A 1 61 ? 5.424 29.682 65.262 0.60 40.04 ? 102 GLU A CD 1 ATOM 459 O OE1 A GLU A 1 61 ? 4.162 30.279 69.605 0.40 43.44 ? 102 GLU A OE1 1 ATOM 460 O OE1 B GLU A 1 61 ? 6.601 29.386 65.593 0.60 39.75 ? 102 GLU A OE1 1 ATOM 461 O OE2 A GLU A 1 61 ? 6.170 30.403 70.493 0.40 41.45 ? 102 GLU A OE2 1 ATOM 462 O OE2 B GLU A 1 61 ? 4.885 29.166 64.242 0.60 40.74 ? 102 GLU A OE2 1 ATOM 463 N N . PHE A 1 62 ? 6.410 34.673 67.477 1.00 27.41 ? 103 PHE A N 1 ATOM 464 C CA . PHE A 1 62 ? 7.443 35.560 68.044 1.00 27.60 ? 103 PHE A CA 1 ATOM 465 C C . PHE A 1 62 ? 6.878 36.665 68.946 1.00 28.13 ? 103 PHE A C 1 ATOM 466 O O . PHE A 1 62 ? 7.604 37.224 69.751 1.00 30.52 ? 103 PHE A O 1 ATOM 467 C CB . PHE A 1 62 ? 8.299 36.245 66.944 1.00 26.01 ? 103 PHE A CB 1 ATOM 468 C CG . PHE A 1 62 ? 9.241 35.312 66.169 1.00 26.50 ? 103 PHE A CG 1 ATOM 469 C CD1 . PHE A 1 62 ? 9.616 34.039 66.628 1.00 28.71 ? 103 PHE A CD1 1 ATOM 470 C CD2 . PHE A 1 62 ? 9.733 35.752 64.961 1.00 26.38 ? 103 PHE A CD2 1 ATOM 471 C CE1 . PHE A 1 62 ? 10.501 33.222 65.851 1.00 31.16 ? 103 PHE A CE1 1 ATOM 472 C CE2 . PHE A 1 62 ? 10.607 34.958 64.189 1.00 26.56 ? 103 PHE A CE2 1 ATOM 473 C CZ . PHE A 1 62 ? 10.983 33.701 64.625 1.00 27.61 ? 103 PHE A CZ 1 ATOM 474 N N . GLY A 1 63 ? 5.600 36.995 68.786 1.00 27.78 ? 104 GLY A N 1 ATOM 475 C CA . GLY A 1 63 ? 4.932 37.881 69.730 1.00 28.58 ? 104 GLY A CA 1 ATOM 476 C C . GLY A 1 63 ? 4.302 39.106 69.121 1.00 27.86 ? 104 GLY A C 1 ATOM 477 O O . GLY A 1 63 ? 3.771 39.937 69.844 1.00 29.01 ? 104 GLY A O 1 ATOM 478 N N . LEU A 1 64 ? 4.349 39.258 67.795 1.00 26.48 ? 105 LEU A N 1 ATOM 479 C CA . LEU A 1 64 ? 3.704 40.458 67.225 1.00 26.24 ? 105 LEU A CA 1 ATOM 480 C C . LEU A 1 64 ? 2.196 40.533 67.507 1.00 26.85 ? 105 LEU A C 1 ATOM 481 O O . LEU A 1 64 ? 1.520 39.505 67.634 1.00 28.91 ? 105 LEU A O 1 ATOM 482 C CB . LEU A 1 64 ? 3.972 40.527 65.716 1.00 25.26 ? 105 LEU A CB 1 ATOM 483 C CG . LEU A 1 64 ? 5.437 40.675 65.306 1.00 24.48 ? 105 LEU A CG 1 ATOM 484 C CD1 . LEU A 1 64 ? 5.501 41.036 63.813 1.00 23.35 ? 105 LEU A CD1 1 ATOM 485 C CD2 . LEU A 1 64 ? 6.159 41.775 66.106 1.00 24.74 ? 105 LEU A CD2 1 ATOM 486 N N . ASP A 1 65 ? 1.651 41.745 67.589 1.00 26.98 ? 106 ASP A N 1 ATOM 487 C CA . ASP A 1 65 ? 0.230 41.922 67.921 1.00 29.03 ? 106 ASP A CA 1 ATOM 488 C C . ASP A 1 65 ? -0.724 41.445 66.817 1.00 30.28 ? 106 ASP A C 1 ATOM 489 O O . ASP A 1 65 ? -1.793 40.886 67.097 1.00 31.83 ? 106 ASP A O 1 ATOM 490 C CB . ASP A 1 65 ? -0.052 43.395 68.217 1.00 27.83 ? 106 ASP A CB 1 ATOM 491 C CG . ASP A 1 65 ? 0.637 43.861 69.479 1.00 31.17 ? 106 ASP A CG 1 ATOM 492 O OD1 . ASP A 1 65 ? 0.384 43.235 70.541 1.00 32.28 ? 106 ASP A OD1 1 ATOM 493 O OD2 . ASP A 1 65 ? 1.453 44.794 69.410 1.00 28.64 ? 106 ASP A OD2 1 ATOM 494 N N . SER A 1 66 ? -0.347 41.703 65.571 1.00 28.40 ? 107 SER A N 1 ATOM 495 C CA . SER A 1 66 ? -1.138 41.252 64.431 1.00 27.35 ? 107 SER A CA 1 ATOM 496 C C . SER A 1 66 ? -0.165 40.931 63.297 1.00 25.75 ? 107 SER A C 1 ATOM 497 O O . SER A 1 66 ? 0.870 41.579 63.182 1.00 23.01 ? 107 SER A O 1 ATOM 498 C CB . SER A 1 66 ? -2.170 42.342 64.042 1.00 28.18 ? 107 SER A CB 1 ATOM 499 O OG A SER A 1 66 ? -1.583 43.489 63.475 0.50 26.62 ? 107 SER A OG 1 ATOM 500 O OG B SER A 1 66 ? -2.527 42.289 62.671 0.50 30.23 ? 107 SER A OG 1 ATOM 501 N N . VAL A 1 67 ? -0.497 39.930 62.487 1.00 23.69 ? 108 VAL A N 1 ATOM 502 C CA . VAL A 1 67 ? 0.353 39.644 61.310 1.00 23.52 ? 108 VAL A CA 1 ATOM 503 C C . VAL A 1 67 ? -0.614 39.193 60.224 1.00 24.38 ? 108 VAL A C 1 ATOM 504 O O . VAL A 1 67 ? -1.273 38.153 60.366 1.00 25.18 ? 108 VAL A O 1 ATOM 505 C CB . VAL A 1 67 ? 1.373 38.519 61.551 1.00 23.85 ? 108 VAL A CB 1 ATOM 506 C CG1 . VAL A 1 67 ? 2.337 38.468 60.374 1.00 23.36 ? 108 VAL A CG1 1 ATOM 507 C CG2 . VAL A 1 67 ? 2.190 38.772 62.860 1.00 24.00 ? 108 VAL A CG2 1 ATOM 508 N N . GLU A 1 68 ? -0.687 39.974 59.148 1.00 24.40 ? 109 GLU A N 1 ATOM 509 C CA . GLU A 1 68 ? -1.635 39.712 58.067 1.00 25.50 ? 109 GLU A CA 1 ATOM 510 C C . GLU A 1 68 ? -0.935 39.555 56.739 1.00 24.77 ? 109 GLU A C 1 ATOM 511 O O . GLU A 1 68 ? 0.180 40.046 56.569 1.00 24.48 ? 109 GLU A O 1 ATOM 512 C CB . GLU A 1 68 ? -2.620 40.875 57.926 1.00 28.02 ? 109 GLU A CB 1 ATOM 513 C CG . GLU A 1 68 ? -3.470 41.082 59.207 1.00 34.56 ? 109 GLU A CG 1 ATOM 514 C CD . GLU A 1 68 ? -4.316 39.842 59.596 1.00 44.75 ? 109 GLU A CD 1 ATOM 515 O OE1 . GLU A 1 68 ? -4.907 39.182 58.695 1.00 45.17 ? 109 GLU A OE1 1 ATOM 516 O OE2 . GLU A 1 68 ? -4.403 39.524 60.820 1.00 50.45 ? 109 GLU A OE2 1 ATOM 517 N N . LEU A 1 69 ? -1.581 38.875 55.798 1.00 23.67 ? 110 LEU A N 1 ATOM 518 C CA . LEU A 1 69 ? -1.081 38.916 54.430 1.00 24.02 ? 110 LEU A CA 1 ATOM 519 C C . LEU A 1 69 ? -1.858 39.991 53.676 1.00 24.39 ? 110 LEU A C 1 ATOM 520 O O . LEU A 1 69 ? -3.088 40.126 53.864 1.00 26.19 ? 110 LEU A O 1 ATOM 521 C CB . LEU A 1 69 ? -1.263 37.576 53.733 1.00 24.46 ? 110 LEU A CB 1 ATOM 522 C CG . LEU A 1 69 ? -0.593 36.355 54.334 1.00 27.28 ? 110 LEU A CG 1 ATOM 523 C CD1 . LEU A 1 69 ? -0.819 35.193 53.361 1.00 30.81 ? 110 LEU A CD1 1 ATOM 524 C CD2 . LEU A 1 69 ? 0.857 36.614 54.478 1.00 27.67 ? 110 LEU A CD2 1 ATOM 525 N N . ALA A 1 70 ? -1.147 40.783 52.883 1.00 22.29 ? 111 ALA A N 1 ATOM 526 C CA . ALA A 1 70 ? -1.779 41.778 52.006 1.00 21.34 ? 111 ALA A CA 1 ATOM 527 C C . ALA A 1 70 ? -1.462 41.301 50.603 1.00 21.16 ? 111 ALA A C 1 ATOM 528 O O . ALA A 1 70 ? -0.267 41.244 50.218 1.00 23.01 ? 111 ALA A O 1 ATOM 529 C CB . ALA A 1 70 ? -1.219 43.172 52.237 1.00 22.84 ? 111 ALA A CB 1 ATOM 530 N N . HIS A 1 71 ? -2.512 40.932 49.855 1.00 20.23 ? 112 HIS A N 1 ATOM 531 C CA . HIS A 1 71 ? -2.267 40.397 48.487 1.00 20.15 ? 112 HIS A CA 1 ATOM 532 C C . HIS A 1 71 ? -2.733 41.381 47.403 1.00 18.51 ? 112 HIS A C 1 ATOM 533 O O . HIS A 1 71 ? -3.654 42.189 47.620 1.00 19.97 ? 112 HIS A O 1 ATOM 534 C CB . HIS A 1 71 ? -2.937 39.022 48.288 1.00 21.52 ? 112 HIS A CB 1 ATOM 535 C CG . HIS A 1 71 ? -4.431 39.064 48.333 1.00 24.90 ? 112 HIS A CG 1 ATOM 536 N ND1 . HIS A 1 71 ? -5.144 38.840 49.491 1.00 29.17 ? 112 HIS A ND1 1 ATOM 537 C CD2 . HIS A 1 71 ? -5.344 39.256 47.354 1.00 26.06 ? 112 HIS A CD2 1 ATOM 538 C CE1 . HIS A 1 71 ? -6.443 38.917 49.228 1.00 30.70 ? 112 HIS A CE1 1 ATOM 539 N NE2 . HIS A 1 71 ? -6.595 39.156 47.935 1.00 29.65 ? 112 HIS A NE2 1 ATOM 540 N N . TYR A 1 72 ? -2.101 41.257 46.227 1.00 19.77 ? 113 TYR A N 1 ATOM 541 C CA . TYR A 1 72 ? -2.396 42.118 45.041 1.00 18.67 ? 113 TYR A CA 1 ATOM 542 C C . TYR A 1 72 ? -2.256 41.256 43.820 1.00 19.10 ? 113 TYR A C 1 ATOM 543 O O . TYR A 1 72 ? -1.537 40.261 43.858 1.00 20.12 ? 113 TYR A O 1 ATOM 544 C CB . TYR A 1 72 ? -1.397 43.313 44.941 1.00 17.56 ? 113 TYR A CB 1 ATOM 545 C CG . TYR A 1 72 ? -1.397 44.115 46.231 1.00 17.66 ? 113 TYR A CG 1 ATOM 546 C CD1 . TYR A 1 72 ? -2.399 45.064 46.455 1.00 18.75 ? 113 TYR A CD1 1 ATOM 547 C CD2 . TYR A 1 72 ? -0.509 43.817 47.252 1.00 20.21 ? 113 TYR A CD2 1 ATOM 548 C CE1 . TYR A 1 72 ? -2.459 45.759 47.678 1.00 20.91 ? 113 TYR A CE1 1 ATOM 549 C CE2 . TYR A 1 72 ? -0.559 44.476 48.433 1.00 20.56 ? 113 TYR A CE2 1 ATOM 550 C CZ . TYR A 1 72 ? -1.525 45.440 48.657 1.00 21.29 ? 113 TYR A CZ 1 ATOM 551 O OH . TYR A 1 72 ? -1.588 46.080 49.915 1.00 21.87 ? 113 TYR A OH 1 ATOM 552 N N . ASP A 1 73 ? -2.894 41.655 42.717 1.00 18.71 ? 114 ASP A N 1 ATOM 553 C CA . ASP A 1 73 ? -2.759 40.917 41.441 1.00 19.94 ? 114 ASP A CA 1 ATOM 554 C C . ASP A 1 73 ? -2.069 41.830 40.456 1.00 19.51 ? 114 ASP A C 1 ATOM 555 O O . ASP A 1 73 ? -2.664 42.825 39.982 1.00 19.22 ? 114 ASP A O 1 ATOM 556 C CB . ASP A 1 73 ? -4.156 40.485 40.941 1.00 20.70 ? 114 ASP A CB 1 ATOM 557 C CG . ASP A 1 73 ? -4.823 39.536 41.907 1.00 26.98 ? 114 ASP A CG 1 ATOM 558 O OD1 . ASP A 1 73 ? -4.174 38.548 42.270 1.00 26.78 ? 114 ASP A OD1 1 ATOM 559 O OD2 . ASP A 1 73 ? -5.978 39.792 42.292 1.00 29.64 ? 114 ASP A OD2 1 ATOM 560 N N . VAL A 1 74 ? -0.792 41.510 40.181 1.00 18.23 ? 115 VAL A N 1 ATOM 561 C CA . VAL A 1 74 ? 0.091 42.427 39.445 1.00 18.20 ? 115 VAL A CA 1 ATOM 562 C C . VAL A 1 74 ? 0.651 41.765 38.181 1.00 19.17 ? 115 VAL A C 1 ATOM 563 O O . VAL A 1 74 ? 0.723 40.549 38.114 1.00 19.90 ? 115 VAL A O 1 ATOM 564 C CB . VAL A 1 74 ? 1.283 42.918 40.336 1.00 17.99 ? 115 VAL A CB 1 ATOM 565 C CG1 . VAL A 1 74 ? 0.725 43.685 41.557 1.00 17.67 ? 115 VAL A CG1 1 ATOM 566 C CG2 . VAL A 1 74 ? 2.208 41.769 40.780 1.00 16.62 ? 115 VAL A CG2 1 ATOM 567 N N . LEU A 1 75 ? 1.145 42.574 37.245 1.00 18.78 ? 116 LEU A N 1 ATOM 568 C CA . LEU A 1 75 ? 1.749 41.991 36.035 1.00 18.33 ? 116 LEU A CA 1 ATOM 569 C C . LEU A 1 75 ? 3.117 41.433 36.370 1.00 18.80 ? 116 LEU A C 1 ATOM 570 O O . LEU A 1 75 ? 4.014 42.196 36.792 1.00 19.90 ? 116 LEU A O 1 ATOM 571 C CB . LEU A 1 75 ? 1.872 43.076 34.949 1.00 17.68 ? 116 LEU A CB 1 ATOM 572 C CG . LEU A 1 75 ? 2.179 42.464 33.564 1.00 20.00 ? 116 LEU A CG 1 ATOM 573 C CD1 . LEU A 1 75 ? 0.908 41.804 32.995 1.00 20.85 ? 116 LEU A CD1 1 ATOM 574 C CD2 . LEU A 1 75 ? 2.626 43.579 32.618 1.00 22.95 ? 116 LEU A CD2 1 ATOM 575 N N . LEU A 1 76 ? 3.297 40.122 36.137 1.00 18.50 ? 117 LEU A N 1 ATOM 576 C CA . LEU A 1 76 ? 4.623 39.478 36.266 1.00 18.47 ? 117 LEU A CA 1 ATOM 577 C C . LEU A 1 76 ? 5.017 38.937 34.894 1.00 19.84 ? 117 LEU A C 1 ATOM 578 O O . LEU A 1 76 ? 4.261 39.139 33.927 1.00 22.16 ? 117 LEU A O 1 ATOM 579 C CB . LEU A 1 76 ? 4.640 38.354 37.301 1.00 18.57 ? 117 LEU A CB 1 ATOM 580 C CG . LEU A 1 76 ? 4.269 38.789 38.730 1.00 18.67 ? 117 LEU A CG 1 ATOM 581 C CD1 . LEU A 1 76 ? 4.472 37.583 39.696 1.00 20.12 ? 117 LEU A CD1 1 ATOM 582 C CD2 . LEU A 1 76 ? 5.113 39.985 39.270 1.00 19.87 ? 117 LEU A CD2 1 ATOM 583 N N . SER A 1 77 ? 6.217 38.368 34.783 1.00 19.45 ? 118 SER A N 1 ATOM 584 C CA . SER A 1 77 ? 6.726 37.891 33.479 1.00 20.51 ? 118 SER A CA 1 ATOM 585 C C . SER A 1 77 ? 7.465 36.585 33.705 1.00 21.29 ? 118 SER A C 1 ATOM 586 O O . SER A 1 77 ? 8.277 36.471 34.628 1.00 21.48 ? 118 SER A O 1 ATOM 587 C CB . SER A 1 77 ? 7.708 38.951 32.931 1.00 21.85 ? 118 SER A CB 1 ATOM 588 O OG . SER A 1 77 ? 8.474 38.457 31.809 1.00 23.08 ? 118 SER A OG 1 ATOM 589 N N . TYR A 1 78 ? 7.219 35.590 32.848 1.00 20.72 ? 119 TYR A N 1 ATOM 590 C CA . TYR A 1 78 ? 7.892 34.313 32.984 1.00 21.20 ? 119 TYR A CA 1 ATOM 591 C C . TYR A 1 78 ? 8.255 33.728 31.632 1.00 22.16 ? 119 TYR A C 1 ATOM 592 O O . TYR A 1 78 ? 7.512 33.893 30.653 1.00 23.93 ? 119 TYR A O 1 ATOM 593 C CB . TYR A 1 78 ? 6.953 33.286 33.611 1.00 22.38 ? 119 TYR A CB 1 ATOM 594 C CG . TYR A 1 78 ? 6.438 33.652 34.997 1.00 22.13 ? 119 TYR A CG 1 ATOM 595 C CD1 . TYR A 1 78 ? 7.279 33.580 36.109 1.00 23.73 ? 119 TYR A CD1 1 ATOM 596 C CD2 . TYR A 1 78 ? 5.099 34.023 35.175 1.00 25.65 ? 119 TYR A CD2 1 ATOM 597 C CE1 . TYR A 1 78 ? 6.790 33.897 37.409 1.00 22.33 ? 119 TYR A CE1 1 ATOM 598 C CE2 . TYR A 1 78 ? 4.602 34.324 36.441 1.00 26.49 ? 119 TYR A CE2 1 ATOM 599 C CZ . TYR A 1 78 ? 5.449 34.220 37.543 1.00 25.85 ? 119 TYR A CZ 1 ATOM 600 O OH . TYR A 1 78 ? 4.952 34.499 38.804 1.00 24.26 ? 119 TYR A OH 1 ATOM 601 N N . PRO A 1 79 ? 9.369 32.986 31.578 1.00 22.42 ? 120 PRO A N 1 ATOM 602 C CA . PRO A 1 79 ? 9.575 32.237 30.310 1.00 24.45 ? 120 PRO A CA 1 ATOM 603 C C . PRO A 1 79 ? 8.511 31.192 30.042 1.00 26.58 ? 120 PRO A C 1 ATOM 604 O O . PRO A 1 79 ? 7.770 30.762 30.935 1.00 26.06 ? 120 PRO A O 1 ATOM 605 C CB . PRO A 1 79 ? 10.942 31.531 30.506 1.00 25.03 ? 120 PRO A CB 1 ATOM 606 C CG . PRO A 1 79 ? 11.530 32.130 31.742 1.00 23.97 ? 120 PRO A CG 1 ATOM 607 C CD . PRO A 1 79 ? 10.421 32.744 32.574 1.00 22.66 ? 120 PRO A CD 1 ATOM 608 N N . ASN A 1 80 ? 8.440 30.784 28.771 1.00 27.59 ? 121 ASN A N 1 ATOM 609 C CA . ASN A 1 80 ? 7.525 29.715 28.390 1.00 30.68 ? 121 ASN A CA 1 ATOM 610 C C . ASN A 1 80 ? 8.281 28.395 28.565 1.00 32.47 ? 121 ASN A C 1 ATOM 611 O O . ASN A 1 80 ? 9.307 28.174 27.932 1.00 31.96 ? 121 ASN A O 1 ATOM 612 C CB . ASN A 1 80 ? 7.064 29.917 26.962 1.00 30.53 ? 121 ASN A CB 1 ATOM 613 C CG . ASN A 1 80 ? 6.017 28.893 26.547 1.00 34.22 ? 121 ASN A CG 1 ATOM 614 O OD1 . ASN A 1 80 ? 6.025 27.758 27.009 1.00 38.38 ? 121 ASN A OD1 1 ATOM 615 N ND2 . ASN A 1 80 ? 5.109 29.301 25.696 1.00 37.87 ? 121 ASN A ND2 1 ATOM 616 N N . LYS A 1 81 ? 7.793 27.555 29.476 1.00 35.14 ? 122 LYS A N 1 ATOM 617 C CA . LYS A 1 81 ? 8.447 26.283 29.822 1.00 38.90 ? 122 LYS A CA 1 ATOM 618 C C . LYS A 1 81 ? 8.597 25.314 28.639 1.00 39.88 ? 122 LYS A C 1 ATOM 619 O O . LYS A 1 81 ? 9.538 24.507 28.591 1.00 41.63 ? 122 LYS A O 1 ATOM 620 C CB . LYS A 1 81 ? 7.698 25.613 30.978 1.00 39.74 ? 122 LYS A CB 1 ATOM 621 C CG . LYS A 1 81 ? 8.056 26.160 32.376 1.00 44.38 ? 122 LYS A CG 1 ATOM 622 C CD . LYS A 1 81 ? 7.125 25.582 33.462 1.00 51.19 ? 122 LYS A CD 1 ATOM 623 C CE . LYS A 1 81 ? 7.158 24.038 33.471 1.00 55.54 ? 122 LYS A CE 1 ATOM 624 N NZ . LYS A 1 81 ? 8.537 23.460 33.631 1.00 58.49 ? 122 LYS A NZ 1 ATOM 625 N N . THR A 1 82 ? 7.693 25.411 27.669 1.00 40.24 ? 123 THR A N 1 ATOM 626 C CA . THR A 1 82 ? 7.766 24.533 26.496 1.00 40.75 ? 123 THR A CA 1 ATOM 627 C C . THR A 1 82 ? 8.233 25.225 25.201 1.00 40.28 ? 123 THR A C 1 ATOM 628 O O . THR A 1 82 ? 8.212 24.625 24.124 1.00 40.78 ? 123 THR A O 1 ATOM 629 C CB . THR A 1 82 ? 6.425 23.781 26.280 1.00 42.01 ? 123 THR A CB 1 ATOM 630 O OG1 . THR A 1 82 ? 5.383 24.727 26.031 1.00 43.04 ? 123 THR A OG1 1 ATOM 631 C CG2 . THR A 1 82 ? 6.063 22.961 27.524 1.00 43.56 ? 123 THR A CG2 1 ATOM 632 N N . HIS A 1 83 ? 8.696 26.467 25.304 1.00 37.63 ? 124 HIS A N 1 ATOM 633 C CA . HIS A 1 83 ? 9.182 27.218 24.157 1.00 37.64 ? 124 HIS A CA 1 ATOM 634 C C . HIS A 1 83 ? 10.348 28.110 24.613 1.00 35.99 ? 124 HIS A C 1 ATOM 635 O O . HIS A 1 83 ? 10.182 29.329 24.770 1.00 35.25 ? 124 HIS A O 1 ATOM 636 C CB . HIS A 1 83 ? 8.056 28.065 23.591 1.00 38.53 ? 124 HIS A CB 1 ATOM 637 C CG . HIS A 1 83 ? 8.281 28.524 22.186 1.00 42.44 ? 124 HIS A CG 1 ATOM 638 N ND1 . HIS A 1 83 ? 7.424 29.399 21.550 1.00 46.94 ? 124 HIS A ND1 1 ATOM 639 C CD2 . HIS A 1 83 ? 9.261 28.240 21.295 1.00 47.73 ? 124 HIS A CD2 1 ATOM 640 C CE1 . HIS A 1 83 ? 7.852 29.610 20.316 1.00 48.84 ? 124 HIS A CE1 1 ATOM 641 N NE2 . HIS A 1 83 ? 8.969 28.926 20.138 1.00 50.39 ? 124 HIS A NE2 1 ATOM 642 N N . PRO A 1 84 ? 11.518 27.507 24.850 1.00 34.95 ? 125 PRO A N 1 ATOM 643 C CA . PRO A 1 84 ? 12.529 28.291 25.591 1.00 33.49 ? 125 PRO A CA 1 ATOM 644 C C . PRO A 1 84 ? 13.205 29.417 24.803 1.00 32.75 ? 125 PRO A C 1 ATOM 645 O O . PRO A 1 84 ? 13.260 29.412 23.558 1.00 32.88 ? 125 PRO A O 1 ATOM 646 C CB . PRO A 1 84 ? 13.545 27.249 26.052 1.00 35.13 ? 125 PRO A CB 1 ATOM 647 C CG . PRO A 1 84 ? 13.300 26.035 25.224 1.00 36.53 ? 125 PRO A CG 1 ATOM 648 C CD . PRO A 1 84 ? 11.939 26.116 24.596 1.00 36.63 ? 125 PRO A CD 1 ATOM 649 N N . ASN A 1 85 ? 13.693 30.394 25.565 1.00 29.98 ? 126 ASN A N 1 ATOM 650 C CA . ASN A 1 85 ? 14.397 31.547 25.016 1.00 29.47 ? 126 ASN A CA 1 ATOM 651 C C . ASN A 1 85 ? 15.828 31.159 24.713 1.00 29.08 ? 126 ASN A C 1 ATOM 652 O O . ASN A 1 85 ? 16.448 30.421 25.489 1.00 30.28 ? 126 ASN A O 1 ATOM 653 C CB . ASN A 1 85 ? 14.413 32.678 26.056 1.00 27.18 ? 126 ASN A CB 1 ATOM 654 C CG . ASN A 1 85 ? 13.020 33.127 26.439 1.00 29.71 ? 126 ASN A CG 1 ATOM 655 O OD1 . ASN A 1 85 ? 12.113 33.125 25.615 1.00 28.42 ? 126 ASN A OD1 1 ATOM 656 N ND2 . ASN A 1 85 ? 12.844 33.515 27.701 1.00 27.09 ? 126 ASN A ND2 1 ATOM 657 N N . TYR A 1 86 ? 16.334 31.609 23.572 1.00 29.18 ? 127 TYR A N 1 ATOM 658 C CA . TYR A 1 86 ? 17.781 31.430 23.287 1.00 29.14 ? 127 TYR A CA 1 ATOM 659 C C . TYR A 1 86 ? 18.182 32.367 22.178 1.00 29.36 ? 127 TYR A C 1 ATOM 660 O O . TYR A 1 86 ? 17.333 32.994 21.541 1.00 29.61 ? 127 TYR A O 1 ATOM 661 C CB . TYR A 1 86 ? 18.098 29.963 22.903 1.00 30.38 ? 127 TYR A CB 1 ATOM 662 C CG . TYR A 1 86 ? 17.571 29.492 21.562 1.00 31.81 ? 127 TYR A CG 1 ATOM 663 C CD1 . TYR A 1 86 ? 18.441 29.253 20.491 1.00 33.51 ? 127 TYR A CD1 1 ATOM 664 C CD2 . TYR A 1 86 ? 16.211 29.258 21.368 1.00 32.63 ? 127 TYR A CD2 1 ATOM 665 C CE1 . TYR A 1 86 ? 17.958 28.786 19.254 1.00 35.83 ? 127 TYR A CE1 1 ATOM 666 C CE2 . TYR A 1 86 ? 15.722 28.801 20.132 1.00 35.24 ? 127 TYR A CE2 1 ATOM 667 C CZ . TYR A 1 86 ? 16.602 28.577 19.088 1.00 37.49 ? 127 TYR A CZ 1 ATOM 668 O OH . TYR A 1 86 ? 16.100 28.143 17.880 1.00 39.86 ? 127 TYR A OH 1 ATOM 669 N N . ILE A 1 87 ? 19.491 32.475 21.957 1.00 29.44 ? 128 ILE A N 1 ATOM 670 C CA . ILE A 1 87 ? 20.015 33.296 20.887 1.00 29.98 ? 128 ILE A CA 1 ATOM 671 C C . ILE A 1 87 ? 20.845 32.365 19.998 1.00 31.08 ? 128 ILE A C 1 ATOM 672 O O . ILE A 1 87 ? 21.486 31.423 20.497 1.00 30.59 ? 128 ILE A O 1 ATOM 673 C CB . ILE A 1 87 ? 20.940 34.381 21.453 1.00 29.66 ? 128 ILE A CB 1 ATOM 674 C CG1 . ILE A 1 87 ? 20.131 35.307 22.383 1.00 28.81 ? 128 ILE A CG1 1 ATOM 675 C CG2 . ILE A 1 87 ? 21.608 35.165 20.332 1.00 31.69 ? 128 ILE A CG2 1 ATOM 676 C CD1 . ILE A 1 87 ? 20.981 36.041 23.379 1.00 30.39 ? 128 ILE A CD1 1 ATOM 677 N N . SER A 1 88 ? 20.829 32.635 18.694 1.00 32.46 ? 129 SER A N 1 ATOM 678 C CA . SER A 1 88 ? 21.661 31.902 17.724 1.00 33.98 ? 129 SER A CA 1 ATOM 679 C C . SER A 1 88 ? 22.560 32.790 16.892 1.00 34.74 ? 129 SER A C 1 ATOM 680 O O . SER A 1 88 ? 22.273 33.976 16.682 1.00 34.41 ? 129 SER A O 1 ATOM 681 C CB . SER A 1 88 ? 20.783 31.135 16.722 1.00 34.22 ? 129 SER A CB 1 ATOM 682 O OG . SER A 1 88 ? 19.948 30.232 17.393 1.00 39.07 ? 129 SER A OG 1 ATOM 683 N N . ILE A 1 89 ? 23.639 32.185 16.364 1.00 35.35 ? 130 ILE A N 1 ATOM 684 C CA . ILE A 1 89 ? 24.271 32.715 15.174 1.00 36.60 ? 130 ILE A CA 1 ATOM 685 C C . ILE A 1 89 ? 23.709 31.842 14.051 1.00 38.29 ? 130 ILE A C 1 ATOM 686 O O . ILE A 1 89 ? 23.671 30.607 14.164 1.00 36.88 ? 130 ILE A O 1 ATOM 687 C CB . ILE A 1 89 ? 25.797 32.631 15.213 1.00 36.14 ? 130 ILE A CB 1 ATOM 688 C CG1 . ILE A 1 89 ? 26.370 33.562 16.308 1.00 35.93 ? 130 ILE A CG1 1 ATOM 689 C CG2 . ILE A 1 89 ? 26.358 32.965 13.808 1.00 38.15 ? 130 ILE A CG2 1 ATOM 690 C CD1 . ILE A 1 89 ? 27.879 33.296 16.552 1.00 38.18 ? 130 ILE A CD1 1 ATOM 691 N N . ILE A 1 90 ? 23.204 32.518 13.025 1.00 40.83 ? 131 ILE A N 1 ATOM 692 C CA A ILE A 1 90 ? 22.564 31.860 11.896 0.50 43.41 ? 131 ILE A CA 1 ATOM 693 C CA B ILE A 1 90 ? 22.576 31.857 11.878 0.50 43.40 ? 131 ILE A CA 1 ATOM 694 C C . ILE A 1 90 ? 23.357 32.140 10.608 1.00 45.72 ? 131 ILE A C 1 ATOM 695 O O . ILE A 1 90 ? 23.837 33.263 10.398 1.00 46.00 ? 131 ILE A O 1 ATOM 696 C CB A ILE A 1 90 ? 21.060 32.301 11.821 0.50 43.04 ? 131 ILE A CB 1 ATOM 697 C CB B ILE A 1 90 ? 21.082 32.276 11.678 0.50 43.31 ? 131 ILE A CB 1 ATOM 698 C CG1 A ILE A 1 90 ? 20.214 31.320 11.010 0.50 44.07 ? 131 ILE A CG1 1 ATOM 699 C CG1 B ILE A 1 90 ? 20.894 33.795 11.755 0.50 43.22 ? 131 ILE A CG1 1 ATOM 700 C CG2 A ILE A 1 90 ? 20.908 33.743 11.332 0.50 43.82 ? 131 ILE A CG2 1 ATOM 701 C CG2 B ILE A 1 90 ? 20.196 31.609 12.697 0.50 42.32 ? 131 ILE A CG2 1 ATOM 702 C CD1 A ILE A 1 90 ? 18.715 31.627 11.096 0.50 42.54 ? 131 ILE A CD1 1 ATOM 703 C CD1 B ILE A 1 90 ? 19.682 34.287 10.966 0.50 44.90 ? 131 ILE A CD1 1 ATOM 704 N N . ASN A 1 91 ? 23.529 31.115 9.770 1.00 48.43 ? 132 ASN A N 1 ATOM 705 C CA . ASN A 1 91 ? 24.198 31.341 8.467 1.00 52.12 ? 132 ASN A CA 1 ATOM 706 C C . ASN A 1 91 ? 23.209 31.855 7.411 1.00 54.41 ? 132 ASN A C 1 ATOM 707 O O . ASN A 1 91 ? 22.004 31.972 7.687 1.00 54.02 ? 132 ASN A O 1 ATOM 708 C CB . ASN A 1 91 ? 25.043 30.139 7.983 1.00 53.53 ? 132 ASN A CB 1 ATOM 709 C CG . ASN A 1 91 ? 24.214 28.888 7.696 1.00 53.48 ? 132 ASN A CG 1 ATOM 710 O OD1 . ASN A 1 91 ? 23.007 28.954 7.432 1.00 54.73 ? 132 ASN A OD1 1 ATOM 711 N ND2 . ASN A 1 91 ? 24.871 27.734 7.766 1.00 52.00 ? 132 ASN A ND2 1 ATOM 712 N N . GLU A 1 92 ? 23.711 32.165 6.215 1.00 57.88 ? 133 GLU A N 1 ATOM 713 C CA . GLU A 1 92 ? 22.863 32.713 5.148 1.00 60.51 ? 133 GLU A CA 1 ATOM 714 C C . GLU A 1 92 ? 21.782 31.734 4.661 1.00 61.57 ? 133 GLU A C 1 ATOM 715 O O . GLU A 1 92 ? 20.778 32.149 4.081 1.00 62.32 ? 133 GLU A O 1 ATOM 716 C CB . GLU A 1 92 ? 23.721 33.169 3.976 1.00 61.76 ? 133 GLU A CB 1 ATOM 717 C CG . GLU A 1 92 ? 24.693 32.094 3.483 1.00 64.78 ? 133 GLU A CG 1 ATOM 718 C CD . GLU A 1 92 ? 25.563 32.563 2.334 1.00 68.00 ? 133 GLU A CD 1 ATOM 719 O OE1 . GLU A 1 92 ? 25.948 33.757 2.312 1.00 68.34 ? 133 GLU A OE1 1 ATOM 720 O OE2 . GLU A 1 92 ? 25.865 31.726 1.459 1.00 69.68 ? 133 GLU A OE2 1 ATOM 721 N N . ASP A 1 93 ? 21.996 30.444 4.911 1.00 62.22 ? 134 ASP A N 1 ATOM 722 C CA . ASP A 1 93 ? 21.017 29.409 4.572 1.00 63.23 ? 134 ASP A CA 1 ATOM 723 C C . ASP A 1 93 ? 19.927 29.276 5.636 1.00 61.87 ? 134 ASP A C 1 ATOM 724 O O . ASP A 1 93 ? 18.946 28.551 5.446 1.00 62.88 ? 134 ASP A O 1 ATOM 725 C CB . ASP A 1 93 ? 21.715 28.060 4.358 1.00 64.16 ? 134 ASP A CB 1 ATOM 726 C CG . ASP A 1 93 ? 22.696 28.084 3.193 1.00 66.81 ? 134 ASP A CG 1 ATOM 727 O OD1 . ASP A 1 93 ? 22.466 28.852 2.232 1.00 68.84 ? 134 ASP A OD1 1 ATOM 728 O OD2 . ASP A 1 93 ? 23.699 27.337 3.237 1.00 67.27 ? 134 ASP A OD2 1 ATOM 729 N N . GLY A 1 94 ? 20.111 29.961 6.760 1.00 59.63 ? 135 GLY A N 1 ATOM 730 C CA . GLY A 1 94 ? 19.150 29.915 7.846 1.00 57.74 ? 135 GLY A CA 1 ATOM 731 C C . GLY A 1 94 ? 19.391 28.776 8.822 1.00 55.99 ? 135 GLY A C 1 ATOM 732 O O . GLY A 1 94 ? 18.499 28.426 9.592 1.00 56.38 ? 135 GLY A O 1 ATOM 733 N N . ASN A 1 95 ? 20.589 28.195 8.801 1.00 54.52 ? 136 ASN A N 1 ATOM 734 C CA . ASN A 1 95 ? 20.945 27.197 9.800 1.00 52.26 ? 136 ASN A CA 1 ATOM 735 C C . ASN A 1 95 ? 21.501 27.871 11.053 1.00 49.05 ? 136 ASN A C 1 ATOM 736 O O . ASN A 1 95 ? 22.373 28.740 10.967 1.00 48.23 ? 136 ASN A O 1 ATOM 737 C CB . ASN A 1 95 ? 21.954 26.193 9.251 1.00 53.18 ? 136 ASN A CB 1 ATOM 738 C CG . ASN A 1 95 ? 21.438 25.446 8.025 1.00 57.72 ? 136 ASN A CG 1 ATOM 739 O OD1 . ASN A 1 95 ? 20.252 25.129 7.924 1.00 60.96 ? 136 ASN A OD1 1 ATOM 740 N ND2 . ASN A 1 95 ? 22.332 25.163 7.090 1.00 58.72 ? 136 ASN A ND2 1 ATOM 741 N N . GLU A 1 96 ? 20.984 27.476 12.212 1.00 46.39 ? 137 GLU A N 1 ATOM 742 C CA . GLU A 1 96 ? 21.466 28.028 13.483 1.00 43.81 ? 137 GLU A CA 1 ATOM 743 C C . GLU A 1 96 ? 22.705 27.233 13.861 1.00 43.16 ? 137 GLU A C 1 ATOM 744 O O . GLU A 1 96 ? 22.609 26.064 14.250 1.00 44.16 ? 137 GLU A O 1 ATOM 745 C CB . GLU A 1 96 ? 20.364 27.950 14.551 1.00 42.20 ? 137 GLU A CB 1 ATOM 746 C CG . GLU A 1 96 ? 19.132 28.757 14.120 1.00 41.91 ? 137 GLU A CG 1 ATOM 747 C CD . GLU A 1 96 ? 18.030 28.870 15.149 1.00 42.26 ? 137 GLU A CD 1 ATOM 748 O OE1 . GLU A 1 96 ? 17.948 28.027 16.054 1.00 42.22 ? 137 GLU A OE1 1 ATOM 749 O OE2 . GLU A 1 96 ? 17.218 29.810 15.019 1.00 43.03 ? 137 GLU A OE2 1 ATOM 750 N N . ILE A 1 97 ? 23.871 27.850 13.685 1.00 42.40 ? 138 ILE A N 1 ATOM 751 C CA . ILE A 1 97 ? 25.155 27.155 13.869 1.00 42.14 ? 138 ILE A CA 1 ATOM 752 C C . ILE A 1 97 ? 25.751 27.238 15.275 1.00 40.74 ? 138 ILE A C 1 ATOM 753 O O . ILE A 1 97 ? 26.680 26.504 15.613 1.00 41.15 ? 138 ILE A O 1 ATOM 754 C CB . ILE A 1 97 ? 26.208 27.569 12.813 1.00 43.65 ? 138 ILE A CB 1 ATOM 755 C CG1 . ILE A 1 97 ? 26.567 29.057 12.952 1.00 43.22 ? 138 ILE A CG1 1 ATOM 756 C CG2 . ILE A 1 97 ? 25.704 27.199 11.412 1.00 44.98 ? 138 ILE A CG2 1 ATOM 757 C CD1 . ILE A 1 97 ? 27.800 29.473 12.105 1.00 46.41 ? 138 ILE A CD1 1 ATOM 758 N N . PHE A 1 98 ? 25.203 28.113 16.104 1.00 38.82 ? 139 PHE A N 1 ATOM 759 C CA . PHE A 1 98 ? 25.599 28.152 17.489 1.00 37.09 ? 139 PHE A CA 1 ATOM 760 C C . PHE A 1 98 ? 24.375 28.599 18.262 1.00 35.01 ? 139 PHE A C 1 ATOM 761 O O . PHE A 1 98 ? 23.646 29.469 17.793 1.00 34.05 ? 139 PHE A O 1 ATOM 762 C CB . PHE A 1 98 ? 26.731 29.150 17.731 1.00 37.60 ? 139 PHE A CB 1 ATOM 763 C CG . PHE A 1 98 ? 26.832 29.596 19.171 1.00 38.27 ? 139 PHE A CG 1 ATOM 764 C CD1 . PHE A 1 98 ? 27.460 28.796 20.122 1.00 38.69 ? 139 PHE A CD1 1 ATOM 765 C CD2 . PHE A 1 98 ? 26.274 30.806 19.576 1.00 37.82 ? 139 PHE A CD2 1 ATOM 766 C CE1 . PHE A 1 98 ? 27.518 29.225 21.474 1.00 39.31 ? 139 PHE A CE1 1 ATOM 767 C CE2 . PHE A 1 98 ? 26.330 31.223 20.915 1.00 37.68 ? 139 PHE A CE2 1 ATOM 768 C CZ . PHE A 1 98 ? 26.957 30.435 21.849 1.00 37.42 ? 139 PHE A CZ 1 ATOM 769 N N . ASN A 1 99 ? 24.131 27.956 19.399 1.00 33.97 ? 140 ASN A N 1 ATOM 770 C CA . ASN A 1 99 ? 23.027 28.342 20.287 1.00 33.69 ? 140 ASN A CA 1 ATOM 771 C C . ASN A 1 99 ? 23.505 28.598 21.691 1.00 33.23 ? 140 ASN A C 1 ATOM 772 O O . ASN A 1 99 ? 24.294 27.811 22.235 1.00 33.40 ? 140 ASN A O 1 ATOM 773 C CB . ASN A 1 99 ? 22.024 27.197 20.382 1.00 34.46 ? 140 ASN A CB 1 ATOM 774 C CG . ASN A 1 99 ? 21.277 26.945 19.072 1.00 37.26 ? 140 ASN A CG 1 ATOM 775 O OD1 . ASN A 1 99 ? 21.044 27.860 18.283 1.00 37.20 ? 140 ASN A OD1 1 ATOM 776 N ND2 . ASN A 1 99 ? 20.906 25.684 18.845 1.00 40.54 ? 140 ASN A ND2 1 ATOM 777 N N . THR A 1 100 ? 22.990 29.672 22.297 1.00 31.51 ? 141 THR A N 1 ATOM 778 C CA . THR A 1 100 ? 23.267 29.935 23.707 1.00 31.28 ? 141 THR A CA 1 ATOM 779 C C . THR A 1 100 ? 22.527 28.912 24.563 1.00 31.26 ? 141 THR A C 1 ATOM 780 O O . THR A 1 100 ? 21.608 28.228 24.079 1.00 32.15 ? 141 THR A O 1 ATOM 781 C CB . THR A 1 100 ? 22.907 31.385 24.121 1.00 30.21 ? 141 THR A CB 1 ATOM 782 O OG1 . THR A 1 100 ? 21.501 31.603 23.969 1.00 30.43 ? 141 THR A OG1 1 ATOM 783 C CG2 . THR A 1 100 ? 23.671 32.388 23.268 1.00 31.61 ? 141 THR A CG2 1 ATOM 784 N N . SER A 1 101 ? 22.948 28.801 25.822 1.00 30.70 ? 142 SER A N 1 ATOM 785 C CA . SER A 1 101 ? 22.463 27.773 26.736 1.00 31.25 ? 142 SER A CA 1 ATOM 786 C C . SER A 1 101 ? 20.994 27.952 27.096 1.00 30.90 ? 142 SER A C 1 ATOM 787 O O . SER A 1 101 ? 20.474 29.093 27.157 1.00 31.46 ? 142 SER A O 1 ATOM 788 C CB . SER A 1 101 ? 23.285 27.852 28.021 1.00 32.43 ? 142 SER A CB 1 ATOM 789 O OG A SER A 1 101 ? 22.802 28.927 28.818 0.50 28.76 ? 142 SER A OG 1 ATOM 790 O OG B SER A 1 101 ? 23.055 26.745 28.867 0.50 33.04 ? 142 SER A OG 1 ATOM 791 N N . LEU A 1 102 ? 20.323 26.847 27.408 1.00 31.56 ? 143 LEU A N 1 ATOM 792 C CA . LEU A 1 102 ? 18.931 26.930 27.842 1.00 31.90 ? 143 LEU A CA 1 ATOM 793 C C . LEU A 1 102 ? 18.776 27.018 29.367 1.00 31.36 ? 143 LEU A C 1 ATOM 794 O O . LEU A 1 102 ? 17.670 27.288 29.876 1.00 32.06 ? 143 LEU A O 1 ATOM 795 C CB . LEU A 1 102 ? 18.106 25.778 27.262 1.00 33.45 ? 143 LEU A CB 1 ATOM 796 C CG . LEU A 1 102 ? 18.113 25.658 25.718 1.00 36.02 ? 143 LEU A CG 1 ATOM 797 C CD1 . LEU A 1 102 ? 17.291 24.456 25.254 1.00 41.02 ? 143 LEU A CD1 1 ATOM 798 C CD2 . LEU A 1 102 ? 17.608 26.944 25.053 1.00 37.51 ? 143 LEU A CD2 1 ATOM 799 N N . PHE A 1 103 ? 19.875 26.827 30.092 1.00 30.99 ? 144 PHE A N 1 ATOM 800 C CA . PHE A 1 103 ? 19.824 26.904 31.559 1.00 30.89 ? 144 PHE A CA 1 ATOM 801 C C . PHE A 1 103 ? 21.241 26.989 32.105 1.00 30.34 ? 144 PHE A C 1 ATOM 802 O O . PHE A 1 103 ? 22.176 26.591 31.407 1.00 31.27 ? 144 PHE A O 1 ATOM 803 C CB . PHE A 1 103 ? 19.079 25.688 32.131 1.00 31.40 ? 144 PHE A CB 1 ATOM 804 C CG . PHE A 1 103 ? 19.743 24.376 31.817 1.00 34.94 ? 144 PHE A CG 1 ATOM 805 C CD1 . PHE A 1 103 ? 20.747 23.874 32.645 1.00 35.54 ? 144 PHE A CD1 1 ATOM 806 C CD2 . PHE A 1 103 ? 19.377 23.638 30.689 1.00 39.51 ? 144 PHE A CD2 1 ATOM 807 C CE1 . PHE A 1 103 ? 21.389 22.679 32.368 1.00 38.54 ? 144 PHE A CE1 1 ATOM 808 C CE2 . PHE A 1 103 ? 20.011 22.428 30.401 1.00 42.26 ? 144 PHE A CE2 1 ATOM 809 C CZ . PHE A 1 103 ? 21.016 21.944 31.244 1.00 41.72 ? 144 PHE A CZ 1 ATOM 810 N N . GLU A 1 104 ? 21.411 27.509 33.327 1.00 28.34 ? 145 GLU A N 1 ATOM 811 C CA . GLU A 1 104 ? 22.715 27.474 34.018 1.00 28.85 ? 145 GLU A CA 1 ATOM 812 C C . GLU A 1 104 ? 22.951 26.079 34.599 1.00 29.37 ? 145 GLU A C 1 ATOM 813 O O . GLU A 1 104 ? 22.055 25.516 35.222 1.00 29.89 ? 145 GLU A O 1 ATOM 814 C CB . GLU A 1 104 ? 22.747 28.430 35.223 1.00 28.90 ? 145 GLU A CB 1 ATOM 815 C CG . GLU A 1 104 ? 22.690 29.893 34.909 1.00 28.55 ? 145 GLU A CG 1 ATOM 816 C CD . GLU A 1 104 ? 22.634 30.731 36.221 1.00 27.25 ? 145 GLU A CD 1 ATOM 817 O OE1 . GLU A 1 104 ? 21.542 30.798 36.824 1.00 27.07 ? 145 GLU A OE1 1 ATOM 818 O OE2 . GLU A 1 104 ? 23.705 31.244 36.671 1.00 27.43 ? 145 GLU A OE2 1 ATOM 819 N N . PRO A 1 105 ? 24.153 25.525 34.426 1.00 30.20 ? 146 PRO A N 1 ATOM 820 C CA . PRO A 1 105 ? 24.450 24.244 35.103 1.00 30.79 ? 146 PRO A CA 1 ATOM 821 C C . PRO A 1 105 ? 24.177 24.345 36.610 1.00 30.81 ? 146 PRO A C 1 ATOM 822 O O . PRO A 1 105 ? 24.677 25.270 37.268 1.00 31.53 ? 146 PRO A O 1 ATOM 823 C CB . PRO A 1 105 ? 25.947 24.042 34.828 1.00 32.53 ? 146 PRO A CB 1 ATOM 824 C CG . PRO A 1 105 ? 26.189 24.893 33.535 1.00 32.45 ? 146 PRO A CG 1 ATOM 825 C CD . PRO A 1 105 ? 25.321 26.097 33.735 1.00 31.86 ? 146 PRO A CD 1 ATOM 826 N N . PRO A 1 106 ? 23.297 23.500 37.149 1.00 30.44 ? 147 PRO A N 1 ATOM 827 C CA . PRO A 1 106 ? 22.944 23.754 38.545 1.00 30.97 ? 147 PRO A CA 1 ATOM 828 C C . PRO A 1 106 ? 24.077 23.403 39.502 1.00 31.42 ? 147 PRO A C 1 ATOM 829 O O . PRO A 1 106 ? 24.894 22.527 39.172 1.00 33.41 ? 147 PRO A O 1 ATOM 830 C CB . PRO A 1 106 ? 21.731 22.861 38.793 1.00 31.53 ? 147 PRO A CB 1 ATOM 831 C CG . PRO A 1 106 ? 21.742 21.881 37.695 1.00 32.42 ? 147 PRO A CG 1 ATOM 832 C CD . PRO A 1 106 ? 22.414 22.512 36.513 1.00 32.28 ? 147 PRO A CD 1 ATOM 833 N N . PRO A 1 107 ? 24.102 24.077 40.677 1.00 31.73 ? 148 PRO A N 1 ATOM 834 C CA . PRO A 1 107 ? 25.193 23.801 41.605 1.00 32.00 ? 148 PRO A CA 1 ATOM 835 C C . PRO A 1 107 ? 25.138 22.399 42.233 1.00 31.72 ? 148 PRO A C 1 ATOM 836 O O . PRO A 1 107 ? 24.078 21.791 42.287 1.00 31.36 ? 148 PRO A O 1 ATOM 837 C CB . PRO A 1 107 ? 25.016 24.880 42.686 1.00 30.97 ? 148 PRO A CB 1 ATOM 838 C CG . PRO A 1 107 ? 23.620 25.311 42.629 1.00 31.65 ? 148 PRO A CG 1 ATOM 839 C CD . PRO A 1 107 ? 23.170 25.097 41.185 1.00 32.35 ? 148 PRO A CD 1 ATOM 840 N N . PRO A 1 108 ? 26.276 21.920 42.768 1.00 31.72 ? 149 PRO A N 1 ATOM 841 C CA . PRO A 1 108 ? 26.342 20.571 43.364 1.00 32.31 ? 149 PRO A CA 1 ATOM 842 C C . PRO A 1 108 ? 25.240 20.303 44.404 1.00 32.13 ? 149 PRO A C 1 ATOM 843 O O . PRO A 1 108 ? 25.072 21.082 45.353 1.00 31.75 ? 149 PRO A O 1 ATOM 844 C CB . PRO A 1 108 ? 27.724 20.540 44.022 1.00 33.19 ? 149 PRO A CB 1 ATOM 845 C CG . PRO A 1 108 ? 28.512 21.614 43.284 1.00 32.36 ? 149 PRO A CG 1 ATOM 846 C CD . PRO A 1 108 ? 27.559 22.646 42.838 1.00 32.50 ? 149 PRO A CD 1 ATOM 847 N N . GLY A 1 109 ? 24.506 19.203 44.218 1.00 33.40 ? 150 GLY A N 1 ATOM 848 C CA . GLY A 1 109 ? 23.483 18.816 45.175 1.00 34.46 ? 150 GLY A CA 1 ATOM 849 C C . GLY A 1 109 ? 22.108 19.410 44.870 1.00 36.10 ? 150 GLY A C 1 ATOM 850 O O . GLY A 1 109 ? 21.144 19.024 45.513 1.00 37.28 ? 150 GLY A O 1 ATOM 851 N N . TYR A 1 110 ? 22.054 20.309 43.889 1.00 36.53 ? 151 TYR A N 1 ATOM 852 C CA . TYR A 1 110 ? 20.802 20.973 43.434 1.00 38.06 ? 151 TYR A CA 1 ATOM 853 C C . TYR A 1 110 ? 20.498 20.645 41.983 1.00 40.63 ? 151 TYR A C 1 ATOM 854 O O . TYR A 1 110 ? 19.621 21.279 41.370 1.00 41.49 ? 151 TYR A O 1 ATOM 855 C CB . TYR A 1 110 ? 20.971 22.470 43.445 1.00 36.28 ? 151 TYR A CB 1 ATOM 856 C CG . TYR A 1 110 ? 21.173 23.111 44.774 1.00 33.40 ? 151 TYR A CG 1 ATOM 857 C CD1 . TYR A 1 110 ? 20.093 23.643 45.485 1.00 30.47 ? 151 TYR A CD1 1 ATOM 858 C CD2 . TYR A 1 110 ? 22.439 23.260 45.292 1.00 28.63 ? 151 TYR A CD2 1 ATOM 859 C CE1 . TYR A 1 110 ? 20.280 24.288 46.698 1.00 28.81 ? 151 TYR A CE1 1 ATOM 860 C CE2 . TYR A 1 110 ? 22.641 23.874 46.489 1.00 27.86 ? 151 TYR A CE2 1 ATOM 861 C CZ . TYR A 1 110 ? 21.566 24.408 47.188 1.00 27.95 ? 151 TYR A CZ 1 ATOM 862 O OH . TYR A 1 110 ? 21.791 25.011 48.372 1.00 26.86 ? 151 TYR A OH 1 ATOM 863 N N . GLU A 1 111 ? 21.251 19.723 41.395 1.00 43.26 ? 152 GLU A N 1 ATOM 864 C CA . GLU A 1 111 ? 21.002 19.343 40.011 1.00 45.89 ? 152 GLU A CA 1 ATOM 865 C C . GLU A 1 111 ? 19.603 18.680 39.819 1.00 47.67 ? 152 GLU A C 1 ATOM 866 O O . GLU A 1 111 ? 19.146 18.528 38.680 1.00 49.09 ? 152 GLU A O 1 ATOM 867 C CB . GLU A 1 111 ? 22.162 18.492 39.438 1.00 46.59 ? 152 GLU A CB 1 ATOM 868 C CG . GLU A 1 111 ? 23.591 18.971 39.858 1.00 46.90 ? 152 GLU A CG 1 ATOM 869 C CD . GLU A 1 111 ? 24.152 18.295 41.142 1.00 48.53 ? 152 GLU A CD 1 ATOM 870 O OE1 . GLU A 1 111 ? 23.372 17.871 42.009 1.00 46.89 ? 152 GLU A OE1 1 ATOM 871 O OE2 . GLU A 1 111 ? 25.393 18.211 41.293 1.00 48.87 ? 152 GLU A OE2 1 ATOM 872 N N . ASN A 1 112 ? 18.922 18.328 40.923 1.00 49.02 ? 153 ASN A N 1 ATOM 873 C CA . ASN A 1 112 ? 17.558 17.726 40.867 1.00 49.87 ? 153 ASN A CA 1 ATOM 874 C C . ASN A 1 112 ? 16.445 18.620 41.439 1.00 49.63 ? 153 ASN A C 1 ATOM 875 O O . ASN A 1 112 ? 15.290 18.212 41.557 1.00 50.49 ? 153 ASN A O 1 ATOM 876 C CB . ASN A 1 112 ? 17.516 16.349 41.544 1.00 51.22 ? 153 ASN A CB 1 ATOM 877 C CG . ASN A 1 112 ? 16.251 15.552 41.190 1.00 52.89 ? 153 ASN A CG 1 ATOM 878 O OD1 . ASN A 1 112 ? 15.970 15.282 40.016 1.00 54.54 ? 153 ASN A OD1 1 ATOM 879 N ND2 . ASN A 1 112 ? 15.491 15.172 42.212 1.00 54.69 ? 153 ASN A ND2 1 ATOM 880 N N . VAL A 1 113 ? 16.798 19.841 41.804 1.00 48.53 ? 154 VAL A N 1 ATOM 881 C CA . VAL A 1 113 ? 15.788 20.802 42.190 1.00 47.24 ? 154 VAL A CA 1 ATOM 882 C C . VAL A 1 113 ? 14.982 21.193 40.937 1.00 47.30 ? 154 VAL A C 1 ATOM 883 O O . VAL A 1 113 ? 15.535 21.424 39.846 1.00 48.14 ? 154 VAL A O 1 ATOM 884 C CB . VAL A 1 113 ? 16.386 22.020 42.924 1.00 46.74 ? 154 VAL A CB 1 ATOM 885 C CG1 . VAL A 1 113 ? 15.275 23.057 43.267 1.00 44.41 ? 154 VAL A CG1 1 ATOM 886 C CG2 . VAL A 1 113 ? 17.098 21.564 44.195 1.00 48.28 ? 154 VAL A CG2 1 ATOM 887 N N . SER A 1 114 ? 13.663 21.198 41.099 1.00 46.48 ? 155 SER A N 1 ATOM 888 C CA . SER A 1 114 ? 12.779 21.595 40.027 1.00 45.55 ? 155 SER A CA 1 ATOM 889 C C . SER A 1 114 ? 12.409 23.069 40.191 1.00 43.54 ? 155 SER A C 1 ATOM 890 O O . SER A 1 114 ? 12.620 23.702 41.277 1.00 42.85 ? 155 SER A O 1 ATOM 891 C CB . SER A 1 114 ? 11.508 20.730 40.017 1.00 47.09 ? 155 SER A CB 1 ATOM 892 O OG A SER A 1 114 ? 10.748 20.957 41.198 0.50 46.71 ? 155 SER A OG 1 ATOM 893 O OG B SER A 1 114 ? 11.231 20.277 38.700 0.50 47.42 ? 155 SER A OG 1 ATOM 894 N N . ASP A 1 115 ? 11.855 23.611 39.113 1.00 40.43 ? 156 ASP A N 1 ATOM 895 C CA . ASP A 1 115 ? 11.358 24.960 39.124 1.00 37.31 ? 156 ASP A CA 1 ATOM 896 C C . ASP A 1 115 ? 12.456 25.986 39.356 1.00 32.97 ? 156 ASP A C 1 ATOM 897 O O . ASP A 1 115 ? 12.210 27.009 39.993 1.00 31.84 ? 156 ASP A O 1 ATOM 898 C CB . ASP A 1 115 ? 10.285 25.142 40.207 1.00 39.18 ? 156 ASP A CB 1 ATOM 899 C CG . ASP A 1 115 ? 9.073 24.247 40.003 1.00 44.41 ? 156 ASP A CG 1 ATOM 900 O OD1 . ASP A 1 115 ? 8.815 23.810 38.847 1.00 50.86 ? 156 ASP A OD1 1 ATOM 901 O OD2 . ASP A 1 115 ? 8.378 23.985 41.014 1.00 50.88 ? 156 ASP A OD2 1 ATOM 902 N N . ILE A 1 116 ? 13.666 25.725 38.867 1.00 28.63 ? 157 ILE A N 1 ATOM 903 C CA . ILE A 1 116 ? 14.622 26.826 38.771 1.00 25.40 ? 157 ILE A CA 1 ATOM 904 C C . ILE A 1 116 ? 14.279 27.566 37.478 1.00 24.82 ? 157 ILE A C 1 ATOM 905 O O . ILE A 1 116 ? 14.323 26.968 36.376 1.00 24.38 ? 157 ILE A O 1 ATOM 906 C CB . ILE A 1 116 ? 16.055 26.296 38.710 1.00 24.08 ? 157 ILE A CB 1 ATOM 907 C CG1 . ILE A 1 116 ? 16.426 25.624 40.032 1.00 25.06 ? 157 ILE A CG1 1 ATOM 908 C CG2 . ILE A 1 116 ? 17.024 27.423 38.324 1.00 23.99 ? 157 ILE A CG2 1 ATOM 909 C CD1 . ILE A 1 116 ? 17.786 24.883 40.015 1.00 25.51 ? 157 ILE A CD1 1 ATOM 910 N N . VAL A 1 117 ? 13.917 28.839 37.570 1.00 23.52 ? 158 VAL A N 1 ATOM 911 C CA . VAL A 1 117 ? 13.586 29.596 36.367 1.00 23.35 ? 158 VAL A CA 1 ATOM 912 C C . VAL A 1 117 ? 14.853 29.792 35.544 1.00 23.62 ? 158 VAL A C 1 ATOM 913 O O . VAL A 1 117 ? 15.871 30.196 36.073 1.00 22.99 ? 158 VAL A O 1 ATOM 914 C CB . VAL A 1 117 ? 12.862 30.961 36.737 1.00 22.27 ? 158 VAL A CB 1 ATOM 915 C CG1 . VAL A 1 117 ? 13.872 32.032 37.282 1.00 21.75 ? 158 VAL A CG1 1 ATOM 916 C CG2 . VAL A 1 117 ? 12.121 31.476 35.537 1.00 24.93 ? 158 VAL A CG2 1 ATOM 917 N N . PRO A 1 118 ? 14.822 29.453 34.249 1.00 23.60 ? 159 PRO A N 1 ATOM 918 C CA . PRO A 1 118 ? 16.035 29.698 33.438 1.00 24.78 ? 159 PRO A CA 1 ATOM 919 C C . PRO A 1 118 ? 16.319 31.196 33.290 1.00 23.70 ? 159 PRO A C 1 ATOM 920 O O . PRO A 1 118 ? 15.405 32.024 33.455 1.00 23.85 ? 159 PRO A O 1 ATOM 921 C CB . PRO A 1 118 ? 15.666 29.122 32.067 1.00 25.65 ? 159 PRO A CB 1 ATOM 922 C CG . PRO A 1 118 ? 14.160 29.118 32.004 1.00 27.10 ? 159 PRO A CG 1 ATOM 923 C CD . PRO A 1 118 ? 13.697 28.914 33.461 1.00 25.14 ? 159 PRO A CD 1 ATOM 924 N N . PRO A 1 119 ? 17.568 31.565 32.969 1.00 23.49 ? 160 PRO A N 1 ATOM 925 C CA . PRO A 1 119 ? 17.874 32.993 32.809 1.00 23.41 ? 160 PRO A CA 1 ATOM 926 C C . PRO A 1 119 ? 16.999 33.632 31.743 1.00 22.21 ? 160 PRO A C 1 ATOM 927 O O . PRO A 1 119 ? 16.743 33.037 30.695 1.00 23.14 ? 160 PRO A O 1 ATOM 928 C CB . PRO A 1 119 ? 19.341 32.985 32.360 1.00 23.29 ? 160 PRO A CB 1 ATOM 929 C CG . PRO A 1 119 ? 19.905 31.689 32.959 1.00 25.71 ? 160 PRO A CG 1 ATOM 930 C CD . PRO A 1 119 ? 18.756 30.704 32.823 1.00 24.26 ? 160 PRO A CD 1 ATOM 931 N N . PHE A 1 120 ? 16.480 34.812 32.083 1.00 22.22 ? 161 PHE A N 1 ATOM 932 C CA . PHE A 1 120 ? 15.632 35.590 31.182 1.00 21.64 ? 161 PHE A CA 1 ATOM 933 C C . PHE A 1 120 ? 15.621 36.996 31.685 1.00 20.78 ? 161 PHE A C 1 ATOM 934 O O . PHE A 1 120 ? 15.959 37.234 32.848 1.00 20.45 ? 161 PHE A O 1 ATOM 935 C CB . PHE A 1 120 ? 14.183 35.036 31.069 1.00 21.39 ? 161 PHE A CB 1 ATOM 936 C CG . PHE A 1 120 ? 13.296 35.332 32.256 1.00 20.21 ? 161 PHE A CG 1 ATOM 937 C CD1 . PHE A 1 120 ? 12.143 36.095 32.077 1.00 19.63 ? 161 PHE A CD1 1 ATOM 938 C CD2 . PHE A 1 120 ? 13.560 34.782 33.534 1.00 22.29 ? 161 PHE A CD2 1 ATOM 939 C CE1 . PHE A 1 120 ? 11.260 36.357 33.166 1.00 19.43 ? 161 PHE A CE1 1 ATOM 940 C CE2 . PHE A 1 120 ? 12.674 35.036 34.630 1.00 20.53 ? 161 PHE A CE2 1 ATOM 941 C CZ . PHE A 1 120 ? 11.530 35.856 34.446 1.00 21.14 ? 161 PHE A CZ 1 ATOM 942 N N . SER A 1 121 ? 15.218 37.924 30.809 1.00 20.21 ? 162 SER A N 1 ATOM 943 C CA . SER A 1 121 ? 15.041 39.314 31.206 1.00 20.12 ? 162 SER A CA 1 ATOM 944 C C . SER A 1 121 ? 13.551 39.548 31.422 1.00 20.24 ? 162 SER A C 1 ATOM 945 O O . SER A 1 121 ? 12.785 39.555 30.456 1.00 20.85 ? 162 SER A O 1 ATOM 946 C CB . SER A 1 121 ? 15.545 40.238 30.105 1.00 21.86 ? 162 SER A CB 1 ATOM 947 O OG . SER A 1 121 ? 16.969 40.063 29.931 1.00 21.32 ? 162 SER A OG 1 ATOM 948 N N . ALA A 1 122 ? 13.147 39.755 32.674 1.00 20.25 ? 163 ALA A N 1 ATOM 949 C CA . ALA A 1 122 ? 11.702 39.877 32.926 1.00 19.50 ? 163 ALA A CA 1 ATOM 950 C C . ALA A 1 122 ? 11.145 41.119 32.233 1.00 20.43 ? 163 ALA A C 1 ATOM 951 O O . ALA A 1 122 ? 11.741 42.205 32.325 1.00 19.37 ? 163 ALA A O 1 ATOM 952 C CB . ALA A 1 122 ? 11.450 39.958 34.456 1.00 19.38 ? 163 ALA A CB 1 ATOM 953 N N . PHE A 1 123 ? 9.981 40.907 31.595 1.00 19.43 ? 164 PHE A N 1 ATOM 954 C CA . PHE A 1 123 ? 9.152 41.878 30.847 1.00 19.61 ? 164 PHE A CA 1 ATOM 955 C C . PHE A 1 123 ? 9.666 42.117 29.444 1.00 20.96 ? 164 PHE A C 1 ATOM 956 O O . PHE A 1 123 ? 9.135 42.985 28.768 1.00 22.89 ? 164 PHE A O 1 ATOM 957 C CB . PHE A 1 123 ? 8.903 43.184 31.606 1.00 19.64 ? 164 PHE A CB 1 ATOM 958 C CG . PHE A 1 123 ? 8.238 42.965 32.937 1.00 19.04 ? 164 PHE A CG 1 ATOM 959 C CD1 . PHE A 1 123 ? 6.843 42.742 33.012 1.00 20.10 ? 164 PHE A CD1 1 ATOM 960 C CD2 . PHE A 1 123 ? 8.990 42.942 34.110 1.00 19.23 ? 164 PHE A CD2 1 ATOM 961 C CE1 . PHE A 1 123 ? 6.200 42.568 34.253 1.00 19.44 ? 164 PHE A CE1 1 ATOM 962 C CE2 . PHE A 1 123 ? 8.355 42.754 35.350 1.00 19.34 ? 164 PHE A CE2 1 ATOM 963 C CZ . PHE A 1 123 ? 6.940 42.580 35.426 1.00 19.21 ? 164 PHE A CZ 1 ATOM 964 N N . SER A 1 124 ? 10.644 41.336 28.995 1.00 21.79 ? 165 SER A N 1 ATOM 965 C CA . SER A 1 124 ? 10.991 41.418 27.562 1.00 22.16 ? 165 SER A CA 1 ATOM 966 C C . SER A 1 124 ? 9.727 41.126 26.736 1.00 24.35 ? 165 SER A C 1 ATOM 967 O O . SER A 1 124 ? 8.971 40.200 27.067 1.00 24.99 ? 165 SER A O 1 ATOM 968 C CB . SER A 1 124 ? 12.022 40.355 27.165 1.00 23.08 ? 165 SER A CB 1 ATOM 969 O OG . SER A 1 124 ? 12.281 40.483 25.771 1.00 23.66 ? 165 SER A OG 1 ATOM 970 N N . PRO A 1 125 ? 9.495 41.906 25.653 1.00 24.79 ? 166 PRO A N 1 ATOM 971 C CA . PRO A 1 125 ? 8.494 41.442 24.706 1.00 26.58 ? 166 PRO A CA 1 ATOM 972 C C . PRO A 1 125 ? 8.962 40.201 23.935 1.00 27.22 ? 166 PRO A C 1 ATOM 973 O O . PRO A 1 125 ? 10.162 39.858 23.927 1.00 26.15 ? 166 PRO A O 1 ATOM 974 C CB . PRO A 1 125 ? 8.382 42.615 23.714 1.00 27.71 ? 166 PRO A CB 1 ATOM 975 C CG . PRO A 1 125 ? 9.726 43.256 23.732 1.00 26.11 ? 166 PRO A CG 1 ATOM 976 C CD . PRO A 1 125 ? 10.185 43.126 25.188 1.00 25.25 ? 166 PRO A CD 1 ATOM 977 N N . GLN A 1 126 ? 8.014 39.545 23.280 1.00 27.96 ? 167 GLN A N 1 ATOM 978 C CA . GLN A 1 126 ? 8.324 38.419 22.399 1.00 29.05 ? 167 GLN A CA 1 ATOM 979 C C . GLN A 1 126 ? 8.862 38.905 21.064 1.00 30.36 ? 167 GLN A C 1 ATOM 980 O O . GLN A 1 126 ? 8.516 40.001 20.606 1.00 31.41 ? 167 GLN A O 1 ATOM 981 C CB . GLN A 1 126 ? 7.061 37.608 22.156 1.00 29.40 ? 167 GLN A CB 1 ATOM 982 C CG . GLN A 1 126 ? 6.450 36.992 23.451 1.00 32.37 ? 167 GLN A CG 1 ATOM 983 C CD . GLN A 1 126 ? 5.258 36.098 23.168 1.00 39.68 ? 167 GLN A CD 1 ATOM 984 O OE1 . GLN A 1 126 ? 4.796 36.026 22.045 1.00 44.64 ? 167 GLN A OE1 1 ATOM 985 N NE2 . GLN A 1 126 ? 4.755 35.418 24.195 1.00 41.10 ? 167 GLN A NE2 1 ATOM 986 N N . GLY A 1 127 ? 9.710 38.093 20.448 1.00 31.23 ? 168 GLY A N 1 ATOM 987 C CA . GLY A 1 127 ? 10.108 38.361 19.070 1.00 32.58 ? 168 GLY A CA 1 ATOM 988 C C . GLY A 1 127 ? 11.235 37.461 18.645 1.00 33.14 ? 168 GLY A C 1 ATOM 989 O O . GLY A 1 127 ? 11.850 36.769 19.472 1.00 32.07 ? 168 GLY A O 1 ATOM 990 N N . MET A 1 128 ? 11.500 37.476 17.331 1.00 33.86 ? 169 MET A N 1 ATOM 991 C CA . MET A 1 128 ? 12.620 36.746 16.772 1.00 35.37 ? 169 MET A CA 1 ATOM 992 C C . MET A 1 128 ? 13.459 37.621 15.842 1.00 35.27 ? 169 MET A C 1 ATOM 993 O O . MET A 1 128 ? 13.726 37.220 14.670 1.00 36.98 ? 169 MET A O 1 ATOM 994 C CB . MET A 1 128 ? 12.117 35.500 16.034 1.00 37.23 ? 169 MET A CB 1 ATOM 995 C CG . MET A 1 128 ? 11.507 34.462 16.955 1.00 41.20 ? 169 MET A CG 1 ATOM 996 S SD . MET A 1 128 ? 11.125 32.960 16.034 1.00 56.64 ? 169 MET A SD 1 ATOM 997 C CE . MET A 1 128 ? 9.923 32.174 17.109 1.00 52.83 ? 169 MET A CE 1 ATOM 998 N N . PRO A 1 129 ? 13.915 38.786 16.332 1.00 34.77 ? 170 PRO A N 1 ATOM 999 C CA . PRO A 1 129 ? 14.700 39.694 15.495 1.00 36.19 ? 170 PRO A CA 1 ATOM 1000 C C . PRO A 1 129 ? 16.004 39.026 15.046 1.00 37.66 ? 170 PRO A C 1 ATOM 1001 O O . PRO A 1 129 ? 16.615 38.290 15.831 1.00 36.28 ? 170 PRO A O 1 ATOM 1002 C CB . PRO A 1 129 ? 14.996 40.872 16.417 1.00 35.44 ? 170 PRO A CB 1 ATOM 1003 C CG . PRO A 1 129 ? 14.878 40.324 17.799 1.00 34.46 ? 170 PRO A CG 1 ATOM 1004 C CD . PRO A 1 129 ? 13.821 39.267 17.733 1.00 33.24 ? 170 PRO A CD 1 ATOM 1005 N N . GLU A 1 130 ? 16.381 39.269 13.787 1.00 39.15 ? 171 GLU A N 1 ATOM 1006 C CA A GLU A 1 130 ? 17.639 38.767 13.260 0.50 40.76 ? 171 GLU A CA 1 ATOM 1007 C CA B GLU A 1 130 ? 17.618 38.752 13.176 0.50 40.85 ? 171 GLU A CA 1 ATOM 1008 C C . GLU A 1 130 ? 18.415 39.949 12.706 1.00 41.62 ? 171 GLU A C 1 ATOM 1009 O O . GLU A 1 130 ? 17.860 40.796 11.996 1.00 43.01 ? 171 GLU A O 1 ATOM 1010 C CB A GLU A 1 130 ? 17.391 37.708 12.180 0.50 41.91 ? 171 GLU A CB 1 ATOM 1011 C CB B GLU A 1 130 ? 17.331 37.927 11.909 0.50 42.24 ? 171 GLU A CB 1 ATOM 1012 C CG A GLU A 1 130 ? 18.644 37.165 11.501 0.50 44.22 ? 171 GLU A CG 1 ATOM 1013 C CG B GLU A 1 130 ? 16.459 36.705 12.053 0.50 43.37 ? 171 GLU A CG 1 ATOM 1014 C CD A GLU A 1 130 ? 18.328 36.249 10.338 0.50 46.19 ? 171 GLU A CD 1 ATOM 1015 C CD B GLU A 1 130 ? 16.021 36.118 10.712 0.50 45.37 ? 171 GLU A CD 1 ATOM 1016 O OE1 A GLU A 1 130 ? 17.378 35.443 10.456 0.50 47.66 ? 171 GLU A OE1 1 ATOM 1017 O OE1 B GLU A 1 130 ? 16.711 36.328 9.673 0.50 46.99 ? 171 GLU A OE1 1 ATOM 1018 O OE2 A GLU A 1 130 ? 19.039 36.322 9.312 0.50 47.25 ? 171 GLU A OE2 1 ATOM 1019 O OE2 B GLU A 1 130 ? 14.972 35.437 10.694 0.50 46.21 ? 171 GLU A OE2 1 ATOM 1020 N N . GLY A 1 131 ? 19.706 40.020 13.026 1.00 40.77 ? 172 GLY A N 1 ATOM 1021 C CA . GLY A 1 131 ? 20.477 41.144 12.531 1.00 40.67 ? 172 GLY A CA 1 ATOM 1022 C C . GLY A 1 131 ? 21.957 41.100 12.809 1.00 40.55 ? 172 GLY A C 1 ATOM 1023 O O . GLY A 1 131 ? 22.492 40.074 13.234 1.00 40.93 ? 172 GLY A O 1 ATOM 1024 N N . ASP A 1 132 ? 22.608 42.229 12.560 1.00 39.73 ? 173 ASP A N 1 ATOM 1025 C CA . ASP A 1 132 ? 24.037 42.374 12.799 1.00 39.82 ? 173 ASP A CA 1 ATOM 1026 C C . ASP A 1 132 ? 24.215 42.955 14.189 1.00 37.55 ? 173 ASP A C 1 ATOM 1027 O O . ASP A 1 132 ? 23.413 43.792 14.621 1.00 36.11 ? 173 ASP A O 1 ATOM 1028 C CB . ASP A 1 132 ? 24.659 43.316 11.778 1.00 41.91 ? 173 ASP A CB 1 ATOM 1029 C CG . ASP A 1 132 ? 24.632 42.754 10.350 1.00 46.40 ? 173 ASP A CG 1 ATOM 1030 O OD1 . ASP A 1 132 ? 25.006 41.571 10.154 1.00 51.12 ? 173 ASP A OD1 1 ATOM 1031 O OD2 . ASP A 1 132 ? 24.251 43.510 9.421 1.00 49.34 ? 173 ASP A OD2 1 ATOM 1032 N N . LEU A 1 133 ? 25.278 42.520 14.858 1.00 36.50 ? 174 LEU A N 1 ATOM 1033 C CA . LEU A 1 133 ? 25.576 42.956 16.217 1.00 35.66 ? 174 LEU A CA 1 ATOM 1034 C C . LEU A 1 133 ? 26.337 44.284 16.240 1.00 35.26 ? 174 LEU A C 1 ATOM 1035 O O . LEU A 1 133 ? 27.197 44.537 15.389 1.00 37.07 ? 174 LEU A O 1 ATOM 1036 C CB . LEU A 1 133 ? 26.423 41.868 16.901 1.00 35.39 ? 174 LEU A CB 1 ATOM 1037 C CG A LEU A 1 133 ? 26.264 41.385 18.342 0.50 34.01 ? 174 LEU A CG 1 ATOM 1038 C CG B LEU A 1 133 ? 25.759 40.545 17.297 0.50 33.94 ? 174 LEU A CG 1 ATOM 1039 C CD1 A LEU A 1 133 ? 24.800 41.309 18.816 0.50 32.55 ? 174 LEU A CD1 1 ATOM 1040 C CD1 B LEU A 1 133 ? 26.825 39.608 17.855 0.50 33.55 ? 174 LEU A CD1 1 ATOM 1041 C CD2 A LEU A 1 133 ? 26.933 40.035 18.476 0.50 33.57 ? 174 LEU A CD2 1 ATOM 1042 C CD2 B LEU A 1 133 ? 24.603 40.727 18.291 0.50 32.22 ? 174 LEU A CD2 1 ATOM 1043 N N . VAL A 1 134 ? 25.997 45.134 17.216 1.00 34.53 ? 175 VAL A N 1 ATOM 1044 C CA . VAL A 1 134 ? 26.868 46.246 17.585 1.00 33.72 ? 175 VAL A CA 1 ATOM 1045 C C . VAL A 1 134 ? 27.181 46.124 19.065 1.00 33.19 ? 175 VAL A C 1 ATOM 1046 O O . VAL A 1 134 ? 26.260 45.907 19.868 1.00 31.23 ? 175 VAL A O 1 ATOM 1047 C CB . VAL A 1 134 ? 26.227 47.609 17.263 1.00 34.53 ? 175 VAL A CB 1 ATOM 1048 C CG1 . VAL A 1 134 ? 27.089 48.740 17.775 1.00 33.91 ? 175 VAL A CG1 1 ATOM 1049 C CG2 . VAL A 1 134 ? 26.051 47.739 15.728 1.00 34.71 ? 175 VAL A CG2 1 ATOM 1050 N N . TYR A 1 135 ? 28.456 46.268 19.416 1.00 32.11 ? 176 TYR A N 1 ATOM 1051 C CA . TYR A 1 135 ? 28.881 46.205 20.824 1.00 31.17 ? 176 TYR A CA 1 ATOM 1052 C C . TYR A 1 135 ? 28.944 47.615 21.404 1.00 30.87 ? 176 TYR A C 1 ATOM 1053 O O . TYR A 1 135 ? 29.565 48.499 20.826 1.00 31.34 ? 176 TYR A O 1 ATOM 1054 C CB . TYR A 1 135 ? 30.230 45.465 20.949 1.00 32.09 ? 176 TYR A CB 1 ATOM 1055 C CG . TYR A 1 135 ? 30.885 45.627 22.308 1.00 30.97 ? 176 TYR A CG 1 ATOM 1056 C CD1 . TYR A 1 135 ? 30.304 45.068 23.450 1.00 29.55 ? 176 TYR A CD1 1 ATOM 1057 C CD2 . TYR A 1 135 ? 32.087 46.327 22.453 1.00 33.07 ? 176 TYR A CD2 1 ATOM 1058 C CE1 . TYR A 1 135 ? 30.890 45.232 24.731 1.00 29.38 ? 176 TYR A CE1 1 ATOM 1059 C CE2 . TYR A 1 135 ? 32.691 46.477 23.716 1.00 32.09 ? 176 TYR A CE2 1 ATOM 1060 C CZ . TYR A 1 135 ? 32.082 45.931 24.848 1.00 30.23 ? 176 TYR A CZ 1 ATOM 1061 O OH . TYR A 1 135 ? 32.677 46.084 26.087 1.00 30.90 ? 176 TYR A OH 1 ATOM 1062 N N . VAL A 1 136 ? 28.295 47.801 22.559 1.00 29.68 ? 177 VAL A N 1 ATOM 1063 C CA . VAL A 1 136 ? 28.019 49.148 23.103 1.00 30.02 ? 177 VAL A CA 1 ATOM 1064 C C . VAL A 1 136 ? 28.561 49.347 24.517 1.00 28.85 ? 177 VAL A C 1 ATOM 1065 O O . VAL A 1 136 ? 28.104 50.235 25.251 1.00 28.47 ? 177 VAL A O 1 ATOM 1066 C CB . VAL A 1 136 ? 26.508 49.473 23.056 1.00 29.35 ? 177 VAL A CB 1 ATOM 1067 C CG1 . VAL A 1 136 ? 26.009 49.415 21.633 1.00 31.74 ? 177 VAL A CG1 1 ATOM 1068 C CG2 . VAL A 1 136 ? 25.692 48.496 23.922 1.00 31.38 ? 177 VAL A CG2 1 ATOM 1069 N N . ASN A 1 137 ? 29.580 48.559 24.860 1.00 28.78 ? 178 ASN A N 1 ATOM 1070 C CA . ASN A 1 137 ? 30.212 48.632 26.179 1.00 28.74 ? 178 ASN A CA 1 ATOM 1071 C C . ASN A 1 137 ? 29.134 48.386 27.244 1.00 28.03 ? 178 ASN A C 1 ATOM 1072 O O . ASN A 1 137 ? 28.415 47.397 27.150 1.00 27.60 ? 178 ASN A O 1 ATOM 1073 C CB . ASN A 1 137 ? 30.930 49.987 26.349 1.00 28.49 ? 178 ASN A CB 1 ATOM 1074 C CG . ASN A 1 137 ? 32.016 49.956 27.409 1.00 30.31 ? 178 ASN A CG 1 ATOM 1075 O OD1 . ASN A 1 137 ? 32.505 48.890 27.787 1.00 29.25 ? 178 ASN A OD1 1 ATOM 1076 N ND2 . ASN A 1 137 ? 32.408 51.135 27.886 1.00 30.67 ? 178 ASN A ND2 1 ATOM 1077 N N . TYR A 1 138 ? 28.991 49.293 28.216 1.00 25.67 ? 179 TYR A N 1 ATOM 1078 C CA . TYR A 1 138 ? 27.971 49.120 29.260 1.00 24.85 ? 179 TYR A CA 1 ATOM 1079 C C . TYR A 1 138 ? 26.609 49.671 28.868 1.00 24.18 ? 179 TYR A C 1 ATOM 1080 O O . TYR A 1 138 ? 25.670 49.672 29.705 1.00 23.56 ? 179 TYR A O 1 ATOM 1081 C CB . TYR A 1 138 ? 28.405 49.834 30.546 1.00 25.11 ? 179 TYR A CB 1 ATOM 1082 C CG . TYR A 1 138 ? 29.636 49.241 31.181 1.00 25.68 ? 179 TYR A CG 1 ATOM 1083 C CD1 . TYR A 1 138 ? 29.560 48.059 31.927 1.00 26.32 ? 179 TYR A CD1 1 ATOM 1084 C CD2 . TYR A 1 138 ? 30.880 49.881 31.063 1.00 26.99 ? 179 TYR A CD2 1 ATOM 1085 C CE1 . TYR A 1 138 ? 30.728 47.509 32.547 1.00 26.68 ? 179 TYR A CE1 1 ATOM 1086 C CE2 . TYR A 1 138 ? 32.034 49.330 31.665 1.00 28.78 ? 179 TYR A CE2 1 ATOM 1087 C CZ . TYR A 1 138 ? 31.936 48.164 32.420 1.00 27.87 ? 179 TYR A CZ 1 ATOM 1088 O OH . TYR A 1 138 ? 33.041 47.637 33.050 1.00 30.76 ? 179 TYR A OH 1 ATOM 1089 N N . ALA A 1 139 ? 26.473 50.140 27.632 1.00 24.81 ? 180 ALA A N 1 ATOM 1090 C CA . ALA A 1 139 ? 25.217 50.704 27.117 1.00 24.75 ? 180 ALA A CA 1 ATOM 1091 C C . ALA A 1 139 ? 24.755 51.914 27.954 1.00 24.97 ? 180 ALA A C 1 ATOM 1092 O O . ALA A 1 139 ? 23.553 52.186 28.079 1.00 24.33 ? 180 ALA A O 1 ATOM 1093 C CB . ALA A 1 139 ? 24.085 49.620 27.020 1.00 25.24 ? 180 ALA A CB 1 ATOM 1094 N N . ARG A 1 140 ? 25.724 52.634 28.522 1.00 24.68 ? 181 ARG A N 1 ATOM 1095 C CA . ARG A 1 140 ? 25.406 53.855 29.283 1.00 24.10 ? 181 ARG A CA 1 ATOM 1096 C C . ARG A 1 140 ? 25.113 55.004 28.325 1.00 24.91 ? 181 ARG A C 1 ATOM 1097 O O . ARG A 1 140 ? 25.437 54.958 27.128 1.00 25.63 ? 181 ARG A O 1 ATOM 1098 C CB . ARG A 1 140 ? 26.587 54.236 30.169 1.00 24.54 ? 181 ARG A CB 1 ATOM 1099 C CG . ARG A 1 140 ? 26.856 53.246 31.305 1.00 25.62 ? 181 ARG A CG 1 ATOM 1100 C CD . ARG A 1 140 ? 28.210 53.468 31.899 1.00 26.54 ? 181 ARG A CD 1 ATOM 1101 N NE . ARG A 1 140 ? 29.262 53.389 30.877 1.00 27.48 ? 181 ARG A NE 1 ATOM 1102 C CZ . ARG A 1 140 ? 30.560 53.560 31.123 1.00 30.71 ? 181 ARG A CZ 1 ATOM 1103 N NH1 . ARG A 1 140 ? 30.984 53.779 32.363 1.00 31.15 ? 181 ARG A NH1 1 ATOM 1104 N NH2 . ARG A 1 140 ? 31.449 53.462 30.132 1.00 30.68 ? 181 ARG A NH2 1 ATOM 1105 N N . THR A 1 141 ? 24.521 56.076 28.847 1.00 23.67 ? 182 THR A N 1 ATOM 1106 C CA . THR A 1 141 ? 24.265 57.248 27.995 1.00 25.02 ? 182 THR A CA 1 ATOM 1107 C C . THR A 1 141 ? 25.555 57.712 27.313 1.00 26.76 ? 182 THR A C 1 ATOM 1108 O O . THR A 1 141 ? 25.552 57.979 26.108 1.00 28.28 ? 182 THR A O 1 ATOM 1109 C CB . THR A 1 141 ? 23.700 58.385 28.860 1.00 25.33 ? 182 THR A CB 1 ATOM 1110 O OG1 . THR A 1 141 ? 22.452 57.948 29.379 1.00 25.83 ? 182 THR A OG1 1 ATOM 1111 C CG2 . THR A 1 141 ? 23.504 59.648 28.018 1.00 26.57 ? 182 THR A CG2 1 ATOM 1112 N N . GLU A 1 142 ? 26.670 57.745 28.054 1.00 27.16 ? 183 GLU A N 1 ATOM 1113 C CA . GLU A 1 142 ? 27.919 58.237 27.458 1.00 29.22 ? 183 GLU A CA 1 ATOM 1114 C C . GLU A 1 142 ? 28.490 57.228 26.458 1.00 29.53 ? 183 GLU A C 1 ATOM 1115 O O . GLU A 1 142 ? 29.218 57.613 25.545 1.00 30.70 ? 183 GLU A O 1 ATOM 1116 C CB . GLU A 1 142 ? 28.962 58.556 28.528 1.00 30.63 ? 183 GLU A CB 1 ATOM 1117 C CG . GLU A 1 142 ? 29.288 57.371 29.454 1.00 32.43 ? 183 GLU A CG 1 ATOM 1118 C CD . GLU A 1 142 ? 28.465 57.333 30.746 1.00 36.42 ? 183 GLU A CD 1 ATOM 1119 O OE1 . GLU A 1 142 ? 27.219 57.636 30.765 1.00 34.27 ? 183 GLU A OE1 1 ATOM 1120 O OE2 . GLU A 1 142 ? 29.089 56.949 31.756 1.00 38.60 ? 183 GLU A OE2 1 ATOM 1121 N N . ASP A 1 143 ? 28.155 55.944 26.608 1.00 28.67 ? 184 ASP A N 1 ATOM 1122 C CA . ASP A 1 143 ? 28.672 54.935 25.627 1.00 29.08 ? 184 ASP A CA 1 ATOM 1123 C C . ASP A 1 143 ? 27.962 55.138 24.294 1.00 29.42 ? 184 ASP A C 1 ATOM 1124 O O . ASP A 1 143 ? 28.586 55.064 23.215 1.00 30.30 ? 184 ASP A O 1 ATOM 1125 C CB . ASP A 1 143 ? 28.420 53.501 26.138 1.00 28.99 ? 184 ASP A CB 1 ATOM 1126 C CG . ASP A 1 143 ? 29.214 53.176 27.364 1.00 28.16 ? 184 ASP A CG 1 ATOM 1127 O OD1 . ASP A 1 143 ? 30.388 53.613 27.464 1.00 29.66 ? 184 ASP A OD1 1 ATOM 1128 O OD2 . ASP A 1 143 ? 28.664 52.477 28.246 1.00 27.47 ? 184 ASP A OD2 1 ATOM 1129 N N . PHE A 1 144 ? 26.651 55.425 24.351 1.00 29.33 ? 185 PHE A N 1 ATOM 1130 C CA . PHE A 1 144 ? 25.907 55.700 23.114 1.00 29.23 ? 185 PHE A CA 1 ATOM 1131 C C . PHE A 1 144 ? 26.286 57.044 22.504 1.00 31.30 ? 185 PHE A C 1 ATOM 1132 O O . PHE A 1 144 ? 26.313 57.172 21.275 1.00 32.20 ? 185 PHE A O 1 ATOM 1133 C CB . PHE A 1 144 ? 24.383 55.588 23.331 1.00 28.04 ? 185 PHE A CB 1 ATOM 1134 C CG . PHE A 1 144 ? 23.891 54.170 23.332 1.00 27.83 ? 185 PHE A CG 1 ATOM 1135 C CD1 . PHE A 1 144 ? 23.614 53.513 24.528 1.00 28.68 ? 185 PHE A CD1 1 ATOM 1136 C CD2 . PHE A 1 144 ? 23.709 53.479 22.125 1.00 29.65 ? 185 PHE A CD2 1 ATOM 1137 C CE1 . PHE A 1 144 ? 23.144 52.205 24.532 1.00 29.20 ? 185 PHE A CE1 1 ATOM 1138 C CE2 . PHE A 1 144 ? 23.246 52.146 22.113 1.00 28.54 ? 185 PHE A CE2 1 ATOM 1139 C CZ . PHE A 1 144 ? 22.971 51.500 23.330 1.00 29.72 ? 185 PHE A CZ 1 ATOM 1140 N N . PHE A 1 145 ? 26.628 58.028 23.346 1.00 31.58 ? 186 PHE A N 1 ATOM 1141 C CA . PHE A 1 145 ? 27.142 59.308 22.823 1.00 33.49 ? 186 PHE A CA 1 ATOM 1142 C C . PHE A 1 145 ? 28.429 59.048 22.022 1.00 35.57 ? 186 PHE A C 1 ATOM 1143 O O . PHE A 1 145 ? 28.605 59.573 20.903 1.00 37.12 ? 186 PHE A O 1 ATOM 1144 C CB . PHE A 1 145 ? 27.455 60.317 23.933 1.00 32.96 ? 186 PHE A CB 1 ATOM 1145 C CG . PHE A 1 145 ? 26.254 61.048 24.503 1.00 32.96 ? 186 PHE A CG 1 ATOM 1146 C CD1 . PHE A 1 145 ? 25.005 61.068 23.868 1.00 34.06 ? 186 PHE A CD1 1 ATOM 1147 C CD2 . PHE A 1 145 ? 26.396 61.752 25.688 1.00 32.39 ? 186 PHE A CD2 1 ATOM 1148 C CE1 . PHE A 1 145 ? 23.907 61.767 24.448 1.00 34.42 ? 186 PHE A CE1 1 ATOM 1149 C CE2 . PHE A 1 145 ? 25.316 62.455 26.259 1.00 30.92 ? 186 PHE A CE2 1 ATOM 1150 C CZ . PHE A 1 145 ? 24.076 62.457 25.644 1.00 31.05 ? 186 PHE A CZ 1 ATOM 1151 N N . LYS A 1 146 ? 29.334 58.252 22.600 1.00 35.96 ? 187 LYS A N 1 ATOM 1152 C CA . LYS A 1 146 ? 30.614 57.906 21.945 1.00 37.01 ? 187 LYS A CA 1 ATOM 1153 C C . LYS A 1 146 ? 30.374 57.222 20.596 1.00 38.26 ? 187 LYS A C 1 ATOM 1154 O O . LYS A 1 146 ? 30.974 57.609 19.571 1.00 38.60 ? 187 LYS A O 1 ATOM 1155 C CB . LYS A 1 146 ? 31.481 57.037 22.874 1.00 37.41 ? 187 LYS A CB 1 ATOM 1156 C CG . LYS A 1 146 ? 32.865 56.556 22.326 1.00 40.45 ? 187 LYS A CG 1 ATOM 1157 C CD . LYS A 1 146 ? 33.966 57.617 22.404 1.00 47.57 ? 187 LYS A CD 1 ATOM 1158 C CE . LYS A 1 146 ? 34.370 57.885 23.871 1.00 51.08 ? 187 LYS A CE 1 ATOM 1159 N NZ . LYS A 1 146 ? 35.466 58.893 23.981 1.00 56.72 ? 187 LYS A NZ 1 ATOM 1160 N N . LEU A 1 147 ? 29.495 56.223 20.581 1.00 37.79 ? 188 LEU A N 1 ATOM 1161 C CA . LEU A 1 147 ? 29.169 55.485 19.352 1.00 39.72 ? 188 LEU A CA 1 ATOM 1162 C C . LEU A 1 147 ? 28.600 56.358 18.247 1.00 40.57 ? 188 LEU A C 1 ATOM 1163 O O . LEU A 1 147 ? 29.118 56.350 17.127 1.00 40.83 ? 188 LEU A O 1 ATOM 1164 C CB . LEU A 1 147 ? 28.144 54.383 19.639 1.00 39.47 ? 188 LEU A CB 1 ATOM 1165 C CG . LEU A 1 147 ? 28.646 53.030 20.080 1.00 41.54 ? 188 LEU A CG 1 ATOM 1166 C CD1 . LEU A 1 147 ? 27.438 52.263 20.650 1.00 44.85 ? 188 LEU A CD1 1 ATOM 1167 C CD2 . LEU A 1 147 ? 29.288 52.309 18.929 1.00 43.86 ? 188 LEU A CD2 1 ATOM 1168 N N A GLU A 1 148 ? 27.579 57.133 18.593 0.60 39.71 ? 189 GLU A N 1 ATOM 1169 N N B GLU A 1 148 ? 27.504 57.072 18.538 0.40 39.96 ? 189 GLU A N 1 ATOM 1170 C CA A GLU A 1 148 ? 26.778 57.835 17.614 0.60 40.74 ? 189 GLU A CA 1 ATOM 1171 C CA B GLU A 1 148 ? 26.811 57.874 17.517 0.40 41.09 ? 189 GLU A CA 1 ATOM 1172 C C A GLU A 1 148 ? 27.364 59.196 17.225 0.60 41.64 ? 189 GLU A C 1 ATOM 1173 C C B GLU A 1 148 ? 27.597 59.131 17.173 0.40 41.86 ? 189 GLU A C 1 ATOM 1174 O O A GLU A 1 148 ? 27.309 59.576 16.053 0.60 42.65 ? 189 GLU A O 1 ATOM 1175 O O B GLU A 1 148 ? 27.895 59.384 16.005 0.40 42.71 ? 189 GLU A O 1 ATOM 1176 C CB A GLU A 1 148 ? 25.332 57.934 18.126 0.60 39.82 ? 189 GLU A CB 1 ATOM 1177 C CB B GLU A 1 148 ? 25.369 58.256 17.931 0.40 40.64 ? 189 GLU A CB 1 ATOM 1178 C CG A GLU A 1 148 ? 24.695 56.550 18.322 0.60 41.35 ? 189 GLU A CG 1 ATOM 1179 C CG B GLU A 1 148 ? 24.537 58.864 16.762 0.40 43.37 ? 189 GLU A CG 1 ATOM 1180 C CD A GLU A 1 148 ? 23.317 56.585 18.980 0.60 41.97 ? 189 GLU A CD 1 ATOM 1181 C CD B GLU A 1 148 ? 23.257 59.591 17.193 0.40 46.17 ? 189 GLU A CD 1 ATOM 1182 O OE1 A GLU A 1 148 ? 23.160 57.179 20.057 0.60 44.24 ? 189 GLU A OE1 1 ATOM 1183 O OE1 B GLU A 1 148 ? 23.340 60.584 17.946 0.40 46.87 ? 189 GLU A OE1 1 ATOM 1184 O OE2 A GLU A 1 148 ? 22.379 56.011 18.407 0.60 44.56 ? 189 GLU A OE2 1 ATOM 1185 O OE2 B GLU A 1 148 ? 22.157 59.183 16.757 0.40 46.70 ? 189 GLU A OE2 1 ATOM 1186 N N . ARG A 1 149 ? 27.940 59.910 18.195 1.00 41.39 ? 190 ARG A N 1 ATOM 1187 C CA . ARG A 1 149 ? 28.472 61.262 17.983 1.00 42.92 ? 190 ARG A CA 1 ATOM 1188 C C . ARG A 1 149 ? 29.928 61.276 17.556 1.00 44.43 ? 190 ARG A C 1 ATOM 1189 O O . ARG A 1 149 ? 30.318 62.053 16.666 1.00 46.28 ? 190 ARG A O 1 ATOM 1190 C CB . ARG A 1 149 ? 28.269 62.148 19.233 1.00 41.49 ? 190 ARG A CB 1 ATOM 1191 C CG . ARG A 1 149 ? 26.802 62.320 19.628 1.00 40.72 ? 190 ARG A CG 1 ATOM 1192 C CD . ARG A 1 149 ? 26.651 63.078 20.953 1.00 38.14 ? 190 ARG A CD 1 ATOM 1193 N NE . ARG A 1 149 ? 25.254 63.371 21.225 1.00 38.84 ? 190 ARG A NE 1 ATOM 1194 C CZ . ARG A 1 149 ? 24.834 64.159 22.220 1.00 37.13 ? 190 ARG A CZ 1 ATOM 1195 N NH1 . ARG A 1 149 ? 25.717 64.699 23.045 1.00 35.12 ? 190 ARG A NH1 1 ATOM 1196 N NH2 . ARG A 1 149 ? 23.544 64.387 22.398 1.00 37.91 ? 190 ARG A NH2 1 ATOM 1197 N N . ASP A 1 150 ? 30.743 60.425 18.174 1.00 45.06 ? 191 ASP A N 1 ATOM 1198 C CA . ASP A 1 150 ? 32.173 60.425 17.861 1.00 46.75 ? 191 ASP A CA 1 ATOM 1199 C C . ASP A 1 150 ? 32.585 59.401 16.797 1.00 47.15 ? 191 ASP A C 1 ATOM 1200 O O . ASP A 1 150 ? 33.357 59.714 15.873 1.00 47.73 ? 191 ASP A O 1 ATOM 1201 C CB . ASP A 1 150 ? 33.008 60.229 19.123 1.00 46.93 ? 191 ASP A CB 1 ATOM 1202 C CG . ASP A 1 150 ? 32.645 61.210 20.220 1.00 51.08 ? 191 ASP A CG 1 ATOM 1203 O OD1 . ASP A 1 150 ? 32.234 62.352 19.899 1.00 56.59 ? 191 ASP A OD1 1 ATOM 1204 O OD2 . ASP A 1 150 ? 32.772 60.844 21.405 1.00 53.67 ? 191 ASP A OD2 1 ATOM 1205 N N . MET A 1 151 ? 32.078 58.182 16.931 1.00 45.99 ? 192 MET A N 1 ATOM 1206 C CA . MET A 1 151 ? 32.492 57.087 16.057 1.00 46.80 ? 192 MET A CA 1 ATOM 1207 C C . MET A 1 151 ? 31.599 56.987 14.840 1.00 47.03 ? 192 MET A C 1 ATOM 1208 O O . MET A 1 151 ? 31.917 56.248 13.896 1.00 47.77 ? 192 MET A O 1 ATOM 1209 C CB . MET A 1 151 ? 32.457 55.757 16.814 1.00 45.60 ? 192 MET A CB 1 ATOM 1210 C CG . MET A 1 151 ? 33.455 55.659 17.938 1.00 47.09 ? 192 MET A CG 1 ATOM 1211 S SD . MET A 1 151 ? 33.323 54.048 18.710 1.00 48.19 ? 192 MET A SD 1 ATOM 1212 C CE . MET A 1 151 ? 34.411 53.076 17.645 1.00 48.73 ? 192 MET A CE 1 ATOM 1213 N N . LYS A 1 152 ? 30.480 57.710 14.880 1.00 46.08 ? 193 LYS A N 1 ATOM 1214 C CA . LYS A 1 152 ? 29.504 57.773 13.789 1.00 47.35 ? 193 LYS A CA 1 ATOM 1215 C C . LYS A 1 152 ? 28.931 56.408 13.438 1.00 47.20 ? 193 LYS A C 1 ATOM 1216 O O . LYS A 1 152 ? 28.744 56.088 12.255 1.00 48.40 ? 193 LYS A O 1 ATOM 1217 C CB . LYS A 1 152 ? 30.120 58.448 12.541 1.00 49.18 ? 193 LYS A CB 1 ATOM 1218 C CG . LYS A 1 152 ? 29.713 59.891 12.321 1.00 52.59 ? 193 LYS A CG 1 ATOM 1219 C CD . LYS A 1 152 ? 30.243 60.841 13.385 1.00 54.69 ? 193 LYS A CD 1 ATOM 1220 C CE . LYS A 1 152 ? 30.096 62.286 12.921 1.00 57.22 ? 193 LYS A CE 1 ATOM 1221 N NZ . LYS A 1 152 ? 29.768 63.189 14.055 1.00 58.57 ? 193 LYS A NZ 1 ATOM 1222 N N . ILE A 1 153 ? 28.681 55.587 14.459 1.00 45.33 ? 194 ILE A N 1 ATOM 1223 C CA . ILE A 1 153 ? 28.096 54.265 14.238 1.00 46.03 ? 194 ILE A CA 1 ATOM 1224 C C . ILE A 1 153 ? 26.608 54.323 14.539 1.00 44.86 ? 194 ILE A C 1 ATOM 1225 O O . ILE A 1 153 ? 26.198 54.823 15.584 1.00 44.38 ? 194 ILE A O 1 ATOM 1226 C CB . ILE A 1 153 ? 28.838 53.150 15.024 1.00 45.92 ? 194 ILE A CB 1 ATOM 1227 C CG1 . ILE A 1 153 ? 30.174 52.867 14.342 1.00 48.46 ? 194 ILE A CG1 1 ATOM 1228 C CG2 . ILE A 1 153 ? 28.011 51.847 15.076 1.00 46.41 ? 194 ILE A CG2 1 ATOM 1229 C CD1 . ILE A 1 153 ? 31.209 52.173 15.183 1.00 50.70 ? 194 ILE A CD1 1 ATOM 1230 N N . ASN A 1 154 ? 25.799 53.836 13.608 1.00 45.46 ? 195 ASN A N 1 ATOM 1231 C CA . ASN A 1 154 ? 24.342 53.931 13.731 1.00 45.33 ? 195 ASN A CA 1 ATOM 1232 C C . ASN A 1 154 ? 23.780 52.589 14.219 1.00 43.91 ? 195 ASN A C 1 ATOM 1233 O O . ASN A 1 154 ? 23.945 51.567 13.549 1.00 43.23 ? 195 ASN A O 1 ATOM 1234 C CB . ASN A 1 154 ? 23.760 54.334 12.359 1.00 47.91 ? 195 ASN A CB 1 ATOM 1235 C CG . ASN A 1 154 ? 22.258 54.606 12.389 1.00 50.71 ? 195 ASN A CG 1 ATOM 1236 O OD1 . ASN A 1 154 ? 21.592 54.436 13.417 1.00 51.20 ? 195 ASN A OD1 1 ATOM 1237 N ND2 . ASN A 1 154 ? 21.715 55.027 11.233 1.00 57.66 ? 195 ASN A ND2 1 ATOM 1238 N N . CYS A 1 155 ? 23.129 52.587 15.395 1.00 41.29 ? 196 CYS A N 1 ATOM 1239 C CA . CYS A 1 155 ? 22.553 51.352 15.928 1.00 41.21 ? 196 CYS A CA 1 ATOM 1240 C C . CYS A 1 155 ? 21.180 50.991 15.386 1.00 41.08 ? 196 CYS A C 1 ATOM 1241 O O . CYS A 1 155 ? 20.608 49.965 15.791 1.00 40.34 ? 196 CYS A O 1 ATOM 1242 C CB . CYS A 1 155 ? 22.464 51.413 17.470 1.00 38.94 ? 196 CYS A CB 1 ATOM 1243 S SG . CYS A 1 155 ? 24.070 51.437 18.245 1.00 42.70 ? 196 CYS A SG 1 ATOM 1244 N N . SER A 1 156 ? 20.624 51.820 14.503 1.00 41.32 ? 197 SER A N 1 ATOM 1245 C CA . SER A 1 156 ? 19.277 51.560 14.012 1.00 41.66 ? 197 SER A CA 1 ATOM 1246 C C . SER A 1 156 ? 19.180 50.247 13.245 1.00 41.78 ? 197 SER A C 1 ATOM 1247 O O . SER A 1 156 ? 19.962 49.990 12.302 1.00 42.22 ? 197 SER A O 1 ATOM 1248 C CB . SER A 1 156 ? 18.730 52.740 13.197 1.00 43.17 ? 197 SER A CB 1 ATOM 1249 O OG . SER A 1 156 ? 17.536 52.378 12.502 1.00 46.36 ? 197 SER A OG 1 ATOM 1250 N N . GLY A 1 157 ? 18.229 49.414 13.668 1.00 40.43 ? 198 GLY A N 1 ATOM 1251 C CA . GLY A 1 157 ? 18.002 48.108 13.065 1.00 40.26 ? 198 GLY A CA 1 ATOM 1252 C C . GLY A 1 157 ? 19.021 47.041 13.444 1.00 39.43 ? 198 GLY A C 1 ATOM 1253 O O . GLY A 1 157 ? 18.972 45.940 12.909 1.00 40.60 ? 198 GLY A O 1 ATOM 1254 N N . LYS A 1 158 ? 19.927 47.358 14.376 1.00 37.97 ? 199 LYS A N 1 ATOM 1255 C CA . LYS A 1 158 ? 20.979 46.415 14.801 1.00 37.06 ? 199 LYS A CA 1 ATOM 1256 C C . LYS A 1 158 ? 20.576 45.744 16.121 1.00 35.31 ? 199 LYS A C 1 ATOM 1257 O O . LYS A 1 158 ? 19.712 46.242 16.846 1.00 34.34 ? 199 LYS A O 1 ATOM 1258 C CB . LYS A 1 158 ? 22.313 47.150 14.987 1.00 37.38 ? 199 LYS A CB 1 ATOM 1259 C CG . LYS A 1 158 ? 22.753 47.977 13.770 1.00 40.81 ? 199 LYS A CG 1 ATOM 1260 C CD . LYS A 1 158 ? 23.354 47.093 12.719 1.00 44.76 ? 199 LYS A CD 1 ATOM 1261 C CE . LYS A 1 158 ? 23.934 47.907 11.561 1.00 48.64 ? 199 LYS A CE 1 ATOM 1262 N NZ . LYS A 1 158 ? 22.966 48.062 10.445 1.00 51.39 ? 199 LYS A NZ 1 ATOM 1263 N N . ILE A 1 159 ? 21.182 44.600 16.406 1.00 34.63 ? 200 ILE A N 1 ATOM 1264 C CA . ILE A 1 159 ? 21.060 43.976 17.729 1.00 33.72 ? 200 ILE A CA 1 ATOM 1265 C C . ILE A 1 159 ? 22.243 44.464 18.542 1.00 33.26 ? 200 ILE A C 1 ATOM 1266 O O . ILE A 1 159 ? 23.388 44.356 18.114 1.00 33.78 ? 200 ILE A O 1 ATOM 1267 C CB . ILE A 1 159 ? 21.031 42.445 17.646 1.00 34.44 ? 200 ILE A CB 1 ATOM 1268 C CG1 . ILE A 1 159 ? 19.732 41.999 16.945 1.00 35.82 ? 200 ILE A CG1 1 ATOM 1269 C CG2 . ILE A 1 159 ? 21.117 41.821 19.051 1.00 35.08 ? 200 ILE A CG2 1 ATOM 1270 C CD1 . ILE A 1 159 ? 19.713 40.542 16.605 1.00 38.45 ? 200 ILE A CD1 1 ATOM 1271 N N . VAL A 1 160 ? 21.970 45.044 19.703 1.00 31.33 ? 201 VAL A N 1 ATOM 1272 C CA . VAL A 1 160 ? 23.071 45.575 20.494 1.00 31.57 ? 201 VAL A CA 1 ATOM 1273 C C . VAL A 1 160 ? 23.475 44.505 21.515 1.00 30.51 ? 201 VAL A C 1 ATOM 1274 O O . VAL A 1 160 ? 22.615 43.801 22.059 1.00 29.19 ? 201 VAL A O 1 ATOM 1275 C CB . VAL A 1 160 ? 22.688 46.946 21.129 1.00 32.27 ? 201 VAL A CB 1 ATOM 1276 C CG1 A VAL A 1 160 ? 22.345 47.976 20.037 0.50 31.96 ? 201 VAL A CG1 1 ATOM 1277 C CG1 B VAL A 1 160 ? 23.111 47.068 22.593 0.50 29.39 ? 201 VAL A CG1 1 ATOM 1278 C CG2 A VAL A 1 160 ? 21.579 46.807 22.078 0.50 29.46 ? 201 VAL A CG2 1 ATOM 1279 C CG2 B VAL A 1 160 ? 23.176 48.093 20.241 0.50 33.63 ? 201 VAL A CG2 1 ATOM 1280 N N . ILE A 1 161 ? 24.781 44.360 21.720 1.00 29.02 ? 202 ILE A N 1 ATOM 1281 C CA . ILE A 1 161 ? 25.298 43.532 22.808 1.00 27.76 ? 202 ILE A CA 1 ATOM 1282 C C . ILE A 1 161 ? 26.051 44.416 23.806 1.00 27.52 ? 202 ILE A C 1 ATOM 1283 O O . ILE A 1 161 ? 26.928 45.222 23.439 1.00 28.01 ? 202 ILE A O 1 ATOM 1284 C CB . ILE A 1 161 ? 26.141 42.321 22.278 1.00 28.49 ? 202 ILE A CB 1 ATOM 1285 C CG1 . ILE A 1 161 ? 26.657 41.457 23.440 1.00 27.87 ? 202 ILE A CG1 1 ATOM 1286 C CG2 . ILE A 1 161 ? 27.266 42.795 21.316 1.00 28.88 ? 202 ILE A CG2 1 ATOM 1287 C CD1 . ILE A 1 161 ? 27.045 40.008 22.977 1.00 30.32 ? 202 ILE A CD1 1 ATOM 1288 N N . ALA A 1 162 ? 25.647 44.303 25.068 1.00 26.50 ? 203 ALA A N 1 ATOM 1289 C CA . ALA A 1 162 ? 26.156 45.171 26.125 1.00 26.75 ? 203 ALA A CA 1 ATOM 1290 C C . ALA A 1 162 ? 26.590 44.327 27.305 1.00 26.25 ? 203 ALA A C 1 ATOM 1291 O O . ALA A 1 162 ? 25.922 43.347 27.622 1.00 26.63 ? 203 ALA A O 1 ATOM 1292 C CB . ALA A 1 162 ? 25.035 46.136 26.572 1.00 25.68 ? 203 ALA A CB 1 ATOM 1293 N N . ARG A 1 163 ? 27.690 44.715 27.965 1.00 26.80 ? 204 ARG A N 1 ATOM 1294 C CA . ARG A 1 163 ? 28.042 44.075 29.212 1.00 25.88 ? 204 ARG A CA 1 ATOM 1295 C C . ARG A 1 163 ? 27.269 44.663 30.379 1.00 24.67 ? 204 ARG A C 1 ATOM 1296 O O . ARG A 1 163 ? 27.019 45.877 30.434 1.00 24.55 ? 204 ARG A O 1 ATOM 1297 C CB . ARG A 1 163 ? 29.538 44.081 29.510 1.00 26.99 ? 204 ARG A CB 1 ATOM 1298 C CG . ARG A 1 163 ? 30.239 45.390 29.295 1.00 28.06 ? 204 ARG A CG 1 ATOM 1299 C CD . ARG A 1 163 ? 31.673 45.211 29.800 1.00 30.83 ? 204 ARG A CD 1 ATOM 1300 N NE . ARG A 1 163 ? 32.508 46.363 29.468 1.00 30.84 ? 204 ARG A NE 1 ATOM 1301 C CZ . ARG A 1 163 ? 33.727 46.536 29.953 1.00 32.73 ? 204 ARG A CZ 1 ATOM 1302 N NH1 . ARG A 1 163 ? 34.211 45.677 30.850 1.00 31.53 ? 204 ARG A NH1 1 ATOM 1303 N NH2 . ARG A 1 163 ? 34.442 47.603 29.579 1.00 30.54 ? 204 ARG A NH2 1 ATOM 1304 N N . TYR A 1 164 ? 26.854 43.780 31.284 1.00 22.86 ? 205 TYR A N 1 ATOM 1305 C CA . TYR A 1 164 ? 26.266 44.200 32.541 1.00 23.17 ? 205 TYR A CA 1 ATOM 1306 C C . TYR A 1 164 ? 27.288 44.992 33.329 1.00 22.97 ? 205 TYR A C 1 ATOM 1307 O O . TYR A 1 164 ? 28.498 44.813 33.190 1.00 23.97 ? 205 TYR A O 1 ATOM 1308 C CB . TYR A 1 164 ? 25.920 42.953 33.328 1.00 22.08 ? 205 TYR A CB 1 ATOM 1309 C CG . TYR A 1 164 ? 24.549 42.329 33.114 1.00 22.11 ? 205 TYR A CG 1 ATOM 1310 C CD1 . TYR A 1 164 ? 24.417 40.952 32.863 1.00 21.32 ? 205 TYR A CD1 1 ATOM 1311 C CD2 . TYR A 1 164 ? 23.382 43.084 33.302 1.00 21.47 ? 205 TYR A CD2 1 ATOM 1312 C CE1 . TYR A 1 164 ? 23.160 40.360 32.799 1.00 21.80 ? 205 TYR A CE1 1 ATOM 1313 C CE2 . TYR A 1 164 ? 22.149 42.511 33.223 1.00 22.02 ? 205 TYR A CE2 1 ATOM 1314 C CZ . TYR A 1 164 ? 22.038 41.161 32.997 1.00 22.04 ? 205 TYR A CZ 1 ATOM 1315 O OH . TYR A 1 164 ? 20.804 40.593 32.994 1.00 22.55 ? 205 TYR A OH 1 ATOM 1316 N N . GLY A 1 165 ? 26.790 45.863 34.202 1.00 22.83 ? 206 GLY A N 1 ATOM 1317 C CA . GLY A 1 165 ? 27.665 46.584 35.126 1.00 23.06 ? 206 GLY A CA 1 ATOM 1318 C C . GLY A 1 165 ? 27.386 48.076 35.083 1.00 23.72 ? 206 GLY A C 1 ATOM 1319 O O . GLY A 1 165 ? 26.802 48.572 34.108 1.00 23.99 ? 206 GLY A O 1 ATOM 1320 N N . LYS A 1 166 ? 27.860 48.780 36.110 1.00 23.17 ? 207 LYS A N 1 ATOM 1321 C CA . LYS A 1 166 ? 27.852 50.261 36.171 1.00 23.65 ? 207 LYS A CA 1 ATOM 1322 C C . LYS A 1 166 ? 26.521 50.929 36.336 1.00 22.95 ? 207 LYS A C 1 ATOM 1323 O O . LYS A 1 166 ? 26.432 51.858 37.173 1.00 23.35 ? 207 LYS A O 1 ATOM 1324 C CB . LYS A 1 166 ? 28.542 50.944 34.967 1.00 24.04 ? 207 LYS A CB 1 ATOM 1325 C CG . LYS A 1 166 ? 29.959 50.387 34.652 1.00 27.23 ? 207 LYS A CG 1 ATOM 1326 C CD . LYS A 1 166 ? 30.879 50.677 35.771 1.00 32.62 ? 207 LYS A CD 1 ATOM 1327 C CE . LYS A 1 166 ? 32.310 50.293 35.333 1.00 35.08 ? 207 LYS A CE 1 ATOM 1328 N NZ . LYS A 1 166 ? 33.226 50.381 36.514 1.00 40.25 ? 207 LYS A NZ 1 ATOM 1329 N N . VAL A 1 167 ? 25.490 50.499 35.592 1.00 22.36 ? 208 VAL A N 1 ATOM 1330 C CA . VAL A 1 167 ? 24.153 51.110 35.688 1.00 21.33 ? 208 VAL A CA 1 ATOM 1331 C C . VAL A 1 167 ? 23.080 50.035 35.668 1.00 19.96 ? 208 VAL A C 1 ATOM 1332 O O . VAL A 1 167 ? 23.313 48.922 35.139 1.00 20.85 ? 208 VAL A O 1 ATOM 1333 C CB . VAL A 1 167 ? 23.865 52.181 34.551 1.00 22.16 ? 208 VAL A CB 1 ATOM 1334 C CG1 . VAL A 1 167 ? 24.961 53.287 34.532 1.00 20.09 ? 208 VAL A CG1 1 ATOM 1335 C CG2 . VAL A 1 167 ? 23.717 51.557 33.121 1.00 24.73 ? 208 VAL A CG2 1 ATOM 1336 N N . PHE A 1 168 ? 21.897 50.384 36.160 1.00 18.90 ? 209 PHE A N 1 ATOM 1337 C CA . PHE A 1 168 ? 20.753 49.472 36.115 1.00 18.28 ? 209 PHE A CA 1 ATOM 1338 C C . PHE A 1 168 ? 20.459 48.984 34.697 1.00 18.94 ? 209 PHE A C 1 ATOM 1339 O O . PHE A 1 168 ? 20.467 49.762 33.718 1.00 20.20 ? 209 PHE A O 1 ATOM 1340 C CB . PHE A 1 168 ? 19.530 50.220 36.657 1.00 17.40 ? 209 PHE A CB 1 ATOM 1341 C CG . PHE A 1 168 ? 18.241 49.455 36.523 1.00 18.53 ? 209 PHE A CG 1 ATOM 1342 C CD1 . PHE A 1 168 ? 18.105 48.189 37.084 1.00 20.23 ? 209 PHE A CD1 1 ATOM 1343 C CD2 . PHE A 1 168 ? 17.143 50.025 35.843 1.00 20.11 ? 209 PHE A CD2 1 ATOM 1344 C CE1 . PHE A 1 168 ? 16.874 47.472 36.966 1.00 22.16 ? 209 PHE A CE1 1 ATOM 1345 C CE2 . PHE A 1 168 ? 15.908 49.313 35.709 1.00 21.62 ? 209 PHE A CE2 1 ATOM 1346 C CZ . PHE A 1 168 ? 15.805 48.016 36.277 1.00 21.69 ? 209 PHE A CZ 1 ATOM 1347 N N . ARG A 1 169 ? 20.221 47.668 34.562 1.00 18.43 ? 210 ARG A N 1 ATOM 1348 C CA . ARG A 1 169 ? 20.025 47.111 33.208 1.00 20.00 ? 210 ARG A CA 1 ATOM 1349 C C . ARG A 1 169 ? 18.829 47.714 32.458 1.00 20.59 ? 210 ARG A C 1 ATOM 1350 O O . ARG A 1 169 ? 18.847 47.730 31.226 1.00 20.68 ? 210 ARG A O 1 ATOM 1351 C CB . ARG A 1 169 ? 19.933 45.567 33.261 1.00 20.41 ? 210 ARG A CB 1 ATOM 1352 C CG . ARG A 1 169 ? 18.651 45.080 33.978 1.00 20.57 ? 210 ARG A CG 1 ATOM 1353 C CD . ARG A 1 169 ? 18.665 43.522 34.159 1.00 21.02 ? 210 ARG A CD 1 ATOM 1354 N NE . ARG A 1 169 ? 19.405 43.118 35.372 1.00 19.01 ? 210 ARG A NE 1 ATOM 1355 C CZ . ARG A 1 169 ? 18.991 43.347 36.629 1.00 21.82 ? 210 ARG A CZ 1 ATOM 1356 N NH1 . ARG A 1 169 ? 17.823 43.945 36.885 1.00 20.28 ? 210 ARG A NH1 1 ATOM 1357 N NH2 . ARG A 1 169 ? 19.754 42.939 37.659 1.00 20.76 ? 210 ARG A NH2 1 ATOM 1358 N N . GLY A 1 170 ? 17.785 48.177 33.173 1.00 20.18 ? 211 GLY A N 1 ATOM 1359 C CA . GLY A 1 170 ? 16.672 48.826 32.494 1.00 21.44 ? 211 GLY A CA 1 ATOM 1360 C C . GLY A 1 170 ? 17.131 50.110 31.782 1.00 20.81 ? 211 GLY A C 1 ATOM 1361 O O . GLY A 1 170 ? 16.572 50.428 30.739 1.00 21.03 ? 211 GLY A O 1 ATOM 1362 N N . ASN A 1 171 ? 18.082 50.839 32.373 1.00 20.52 ? 212 ASN A N 1 ATOM 1363 C CA . ASN A 1 171 ? 18.628 52.010 31.674 1.00 21.11 ? 212 ASN A CA 1 ATOM 1364 C C . ASN A 1 171 ? 19.346 51.652 30.376 1.00 22.32 ? 212 ASN A C 1 ATOM 1365 O O . ASN A 1 171 ? 19.204 52.374 29.362 1.00 23.54 ? 212 ASN A O 1 ATOM 1366 C CB . ASN A 1 171 ? 19.539 52.823 32.565 1.00 21.56 ? 212 ASN A CB 1 ATOM 1367 C CG . ASN A 1 171 ? 18.776 53.506 33.687 1.00 23.84 ? 212 ASN A CG 1 ATOM 1368 O OD1 . ASN A 1 171 ? 18.694 52.982 34.814 1.00 22.24 ? 212 ASN A OD1 1 ATOM 1369 N ND2 . ASN A 1 171 ? 18.148 54.651 33.364 1.00 22.86 ? 212 ASN A ND2 1 ATOM 1370 N N . LYS A 1 172 ? 20.099 50.538 30.403 1.00 20.82 ? 213 LYS A N 1 ATOM 1371 C CA . LYS A 1 172 ? 20.764 50.037 29.176 1.00 22.16 ? 213 LYS A CA 1 ATOM 1372 C C . LYS A 1 172 ? 19.760 49.802 28.047 1.00 22.93 ? 213 LYS A C 1 ATOM 1373 O O . LYS A 1 172 ? 19.989 50.173 26.888 1.00 23.29 ? 213 LYS A O 1 ATOM 1374 C CB . LYS A 1 172 ? 21.514 48.724 29.463 1.00 21.10 ? 213 LYS A CB 1 ATOM 1375 C CG . LYS A 1 172 ? 22.557 48.814 30.616 1.00 22.34 ? 213 LYS A CG 1 ATOM 1376 C CD . LYS A 1 172 ? 23.211 47.434 30.855 1.00 22.96 ? 213 LYS A CD 1 ATOM 1377 C CE . LYS A 1 172 ? 24.124 47.378 32.069 1.00 23.25 ? 213 LYS A CE 1 ATOM 1378 N NZ . LYS A 1 172 ? 25.512 47.780 31.687 1.00 23.01 ? 213 LYS A NZ 1 ATOM 1379 N N . VAL A 1 173 ? 18.639 49.171 28.406 1.00 22.30 ? 214 VAL A N 1 ATOM 1380 C CA . VAL A 1 173 ? 17.636 48.777 27.455 1.00 22.39 ? 214 VAL A CA 1 ATOM 1381 C C . VAL A 1 173 ? 16.938 50.034 26.907 1.00 22.99 ? 214 VAL A C 1 ATOM 1382 O O . VAL A 1 173 ? 16.723 50.136 25.693 1.00 23.80 ? 214 VAL A O 1 ATOM 1383 C CB . VAL A 1 173 ? 16.641 47.790 28.068 1.00 22.55 ? 214 VAL A CB 1 ATOM 1384 C CG1 . VAL A 1 173 ? 15.482 47.535 27.113 1.00 23.19 ? 214 VAL A CG1 1 ATOM 1385 C CG2 . VAL A 1 173 ? 17.346 46.432 28.352 1.00 22.93 ? 214 VAL A CG2 1 ATOM 1386 N N . LYS A 1 174 ? 16.615 50.975 27.790 1.00 22.66 ? 215 LYS A N 1 ATOM 1387 C CA A LYS A 1 174 ? 16.021 52.253 27.385 0.50 24.11 ? 215 LYS A CA 1 ATOM 1388 C CA B LYS A 1 174 ? 15.995 52.223 27.341 0.50 24.19 ? 215 LYS A CA 1 ATOM 1389 C C . LYS A 1 174 ? 16.938 52.941 26.381 1.00 24.89 ? 215 LYS A C 1 ATOM 1390 O O . LYS A 1 174 ? 16.485 53.406 25.325 1.00 25.47 ? 215 LYS A O 1 ATOM 1391 C CB A LYS A 1 174 ? 15.797 53.153 28.601 0.50 23.99 ? 215 LYS A CB 1 ATOM 1392 C CB B LYS A 1 174 ? 15.609 53.120 28.513 0.50 24.07 ? 215 LYS A CB 1 ATOM 1393 C CG A LYS A 1 174 ? 15.521 54.613 28.232 0.50 26.06 ? 215 LYS A CG 1 ATOM 1394 C CG B LYS A 1 174 ? 14.867 54.403 28.104 0.50 26.26 ? 215 LYS A CG 1 ATOM 1395 C CD A LYS A 1 174 ? 14.895 55.382 29.365 0.50 29.33 ? 215 LYS A CD 1 ATOM 1396 C CD B LYS A 1 174 ? 14.556 55.253 29.355 0.50 31.33 ? 215 LYS A CD 1 ATOM 1397 C CE A LYS A 1 174 ? 14.655 56.807 28.931 0.50 31.92 ? 215 LYS A CE 1 ATOM 1398 C CE B LYS A 1 174 ? 15.789 55.426 30.247 0.50 33.34 ? 215 LYS A CE 1 ATOM 1399 N NZ A LYS A 1 174 ? 15.880 57.611 29.110 0.50 32.61 ? 215 LYS A NZ 1 ATOM 1400 N NZ B LYS A 1 174 ? 15.638 56.462 31.328 0.50 38.14 ? 215 LYS A NZ 1 ATOM 1401 N N . ASN A 1 175 ? 18.239 53.000 26.725 1.00 24.51 ? 216 ASN A N 1 ATOM 1402 C CA . ASN A 1 175 ? 19.218 53.628 25.837 1.00 24.78 ? 216 ASN A CA 1 ATOM 1403 C C . ASN A 1 175 ? 19.289 52.950 24.466 1.00 25.72 ? 216 ASN A C 1 ATOM 1404 O O . ASN A 1 175 ? 19.306 53.630 23.447 1.00 26.89 ? 216 ASN A O 1 ATOM 1405 C CB . ASN A 1 175 ? 20.608 53.653 26.501 1.00 24.50 ? 216 ASN A CB 1 ATOM 1406 C CG . ASN A 1 175 ? 20.630 54.523 27.785 1.00 27.09 ? 216 ASN A CG 1 ATOM 1407 O OD1 . ASN A 1 175 ? 19.716 55.337 28.023 1.00 28.80 ? 216 ASN A OD1 1 ATOM 1408 N ND2 . ASN A 1 175 ? 21.669 54.356 28.610 1.00 25.25 ? 216 ASN A ND2 1 ATOM 1409 N N . ALA A 1 176 ? 19.335 51.623 24.460 1.00 25.55 ? 217 ALA A N 1 ATOM 1410 C CA . ALA A 1 176 ? 19.407 50.854 23.201 1.00 26.58 ? 217 ALA A CA 1 ATOM 1411 C C . ALA A 1 176 ? 18.128 51.099 22.367 1.00 27.92 ? 217 ALA A C 1 ATOM 1412 O O . ALA A 1 176 ? 18.193 51.275 21.139 1.00 30.03 ? 217 ALA A O 1 ATOM 1413 C CB . ALA A 1 176 ? 19.578 49.366 23.509 1.00 26.37 ? 217 ALA A CB 1 ATOM 1414 N N . GLN A 1 177 ? 16.982 51.147 23.037 1.00 28.67 ? 218 GLN A N 1 ATOM 1415 C CA . GLN A 1 177 ? 15.711 51.338 22.353 1.00 31.16 ? 218 GLN A CA 1 ATOM 1416 C C . GLN A 1 177 ? 15.702 52.700 21.628 1.00 31.73 ? 218 GLN A C 1 ATOM 1417 O O . GLN A 1 177 ? 15.320 52.804 20.444 1.00 32.21 ? 218 GLN A O 1 ATOM 1418 C CB . GLN A 1 177 ? 14.593 51.252 23.397 1.00 31.52 ? 218 GLN A CB 1 ATOM 1419 C CG . GLN A 1 177 ? 13.262 50.857 22.882 1.00 38.28 ? 218 GLN A CG 1 ATOM 1420 C CD . GLN A 1 177 ? 12.289 50.619 24.035 1.00 42.84 ? 218 GLN A CD 1 ATOM 1421 O OE1 . GLN A 1 177 ? 12.452 49.677 24.839 1.00 42.91 ? 218 GLN A OE1 1 ATOM 1422 N NE2 . GLN A 1 177 ? 11.284 51.495 24.140 1.00 44.90 ? 218 GLN A NE2 1 ATOM 1423 N N . LEU A 1 178 ? 16.157 53.733 22.322 1.00 31.72 ? 219 LEU A N 1 ATOM 1424 C CA . LEU A 1 178 ? 16.164 55.081 21.753 1.00 33.70 ? 219 LEU A CA 1 ATOM 1425 C C . LEU A 1 178 ? 17.223 55.271 20.691 1.00 34.20 ? 219 LEU A C 1 ATOM 1426 O O . LEU A 1 178 ? 17.106 56.173 19.842 1.00 35.27 ? 219 LEU A O 1 ATOM 1427 C CB . LEU A 1 178 ? 16.294 56.140 22.849 1.00 33.45 ? 219 LEU A CB 1 ATOM 1428 C CG . LEU A 1 178 ? 15.085 56.239 23.802 1.00 37.99 ? 219 LEU A CG 1 ATOM 1429 C CD1 . LEU A 1 178 ? 15.393 57.274 24.882 1.00 40.21 ? 219 LEU A CD1 1 ATOM 1430 C CD2 . LEU A 1 178 ? 13.737 56.526 23.097 1.00 41.53 ? 219 LEU A CD2 1 ATOM 1431 N N . ALA A 1 179 ? 18.238 54.407 20.696 1.00 32.11 ? 220 ALA A N 1 ATOM 1432 C CA . ALA A 1 179 ? 19.253 54.395 19.633 1.00 33.34 ? 220 ALA A CA 1 ATOM 1433 C C . ALA A 1 179 ? 18.747 53.639 18.410 1.00 33.68 ? 220 ALA A C 1 ATOM 1434 O O . ALA A 1 179 ? 19.438 53.569 17.381 1.00 35.11 ? 220 ALA A O 1 ATOM 1435 C CB . ALA A 1 179 ? 20.516 53.756 20.143 1.00 32.81 ? 220 ALA A CB 1 ATOM 1436 N N . GLY A 1 180 ? 17.550 53.064 18.493 1.00 33.60 ? 221 GLY A N 1 ATOM 1437 C CA . GLY A 1 180 ? 16.986 52.354 17.341 1.00 33.82 ? 221 GLY A CA 1 ATOM 1438 C C . GLY A 1 180 ? 17.304 50.864 17.256 1.00 33.51 ? 221 GLY A C 1 ATOM 1439 O O . GLY A 1 180 ? 16.986 50.232 16.260 1.00 34.28 ? 221 GLY A O 1 ATOM 1440 N N . ALA A 1 181 ? 17.882 50.279 18.318 1.00 32.60 ? 222 ALA A N 1 ATOM 1441 C CA . ALA A 1 181 ? 18.210 48.834 18.329 1.00 31.81 ? 222 ALA A CA 1 ATOM 1442 C C . ALA A 1 181 ? 16.952 47.987 18.138 1.00 31.61 ? 222 ALA A C 1 ATOM 1443 O O . ALA A 1 181 ? 15.866 48.400 18.550 1.00 31.38 ? 222 ALA A O 1 ATOM 1444 C CB . ALA A 1 181 ? 18.920 48.436 19.632 1.00 30.56 ? 222 ALA A CB 1 ATOM 1445 N N . LYS A 1 182 ? 17.064 46.826 17.491 1.00 31.56 ? 223 LYS A N 1 ATOM 1446 C CA . LYS A 1 182 ? 15.882 45.949 17.455 1.00 31.65 ? 223 LYS A CA 1 ATOM 1447 C C . LYS A 1 182 ? 15.939 44.798 18.457 1.00 30.76 ? 223 LYS A C 1 ATOM 1448 O O . LYS A 1 182 ? 15.029 43.979 18.515 1.00 30.04 ? 223 LYS A O 1 ATOM 1449 C CB . LYS A 1 182 ? 15.549 45.468 16.047 1.00 34.65 ? 223 LYS A CB 1 ATOM 1450 C CG . LYS A 1 182 ? 16.536 44.538 15.463 1.00 36.08 ? 223 LYS A CG 1 ATOM 1451 C CD . LYS A 1 182 ? 16.119 44.232 14.017 1.00 41.65 ? 223 LYS A CD 1 ATOM 1452 C CE . LYS A 1 182 ? 17.077 43.285 13.425 1.00 44.18 ? 223 LYS A CE 1 ATOM 1453 N NZ . LYS A 1 182 ? 16.775 43.025 11.971 1.00 46.92 ? 223 LYS A NZ 1 ATOM 1454 N N . GLY A 1 183 ? 16.998 44.768 19.262 1.00 29.75 ? 224 GLY A N 1 ATOM 1455 C CA . GLY A 1 183 ? 17.124 43.751 20.321 1.00 29.29 ? 224 GLY A CA 1 ATOM 1456 C C . GLY A 1 183 ? 18.336 44.049 21.173 1.00 28.00 ? 224 GLY A C 1 ATOM 1457 O O . GLY A 1 183 ? 19.218 44.787 20.738 1.00 28.59 ? 224 GLY A O 1 ATOM 1458 N N . VAL A 1 184 ? 18.387 43.490 22.385 1.00 25.99 ? 225 VAL A N 1 ATOM 1459 C CA . VAL A 1 184 ? 19.522 43.715 23.288 1.00 25.66 ? 225 VAL A CA 1 ATOM 1460 C C . VAL A 1 184 ? 19.936 42.380 23.880 1.00 25.91 ? 225 VAL A C 1 ATOM 1461 O O . VAL A 1 184 ? 19.095 41.632 24.401 1.00 26.14 ? 225 VAL A O 1 ATOM 1462 C CB . VAL A 1 184 ? 19.159 44.634 24.474 1.00 25.19 ? 225 VAL A CB 1 ATOM 1463 C CG1 . VAL A 1 184 ? 20.384 44.840 25.367 1.00 24.85 ? 225 VAL A CG1 1 ATOM 1464 C CG2 . VAL A 1 184 ? 18.642 45.974 23.932 1.00 27.43 ? 225 VAL A CG2 1 ATOM 1465 N N . ILE A 1 185 ? 21.225 42.101 23.820 1.00 26.03 ? 226 ILE A N 1 ATOM 1466 C CA . ILE A 1 185 ? 21.791 40.941 24.493 1.00 25.29 ? 226 ILE A CA 1 ATOM 1467 C C . ILE A 1 185 ? 22.673 41.481 25.606 1.00 24.71 ? 226 ILE A C 1 ATOM 1468 O O . ILE A 1 185 ? 23.569 42.282 25.341 1.00 25.81 ? 226 ILE A O 1 ATOM 1469 C CB . ILE A 1 185 ? 22.625 40.119 23.501 1.00 26.71 ? 226 ILE A CB 1 ATOM 1470 C CG1 . ILE A 1 185 ? 21.722 39.619 22.354 1.00 27.58 ? 226 ILE A CG1 1 ATOM 1471 C CG2 . ILE A 1 185 ? 23.361 38.973 24.224 1.00 26.98 ? 226 ILE A CG2 1 ATOM 1472 C CD1 . ILE A 1 185 ? 22.508 38.956 21.180 1.00 27.33 ? 226 ILE A CD1 1 ATOM 1473 N N . LEU A 1 186 ? 22.401 41.054 26.845 1.00 23.57 ? 227 LEU A N 1 ATOM 1474 C CA . LEU A 1 186 ? 23.153 41.482 28.035 1.00 23.33 ? 227 LEU A CA 1 ATOM 1475 C C . LEU A 1 186 ? 24.051 40.321 28.449 1.00 23.10 ? 227 LEU A C 1 ATOM 1476 O O . LEU A 1 186 ? 23.615 39.156 28.415 1.00 24.38 ? 227 LEU A O 1 ATOM 1477 C CB . LEU A 1 186 ? 22.183 41.805 29.182 1.00 21.05 ? 227 LEU A CB 1 ATOM 1478 C CG . LEU A 1 186 ? 21.240 42.995 28.924 1.00 24.54 ? 227 LEU A CG 1 ATOM 1479 C CD1 . LEU A 1 186 ? 20.097 43.058 29.988 1.00 25.39 ? 227 LEU A CD1 1 ATOM 1480 C CD2 . LEU A 1 186 ? 22.041 44.290 28.963 1.00 28.84 ? 227 LEU A CD2 1 ATOM 1481 N N . TYR A 1 187 ? 25.314 40.592 28.784 1.00 22.99 ? 228 TYR A N 1 ATOM 1482 C CA . TYR A 1 187 ? 26.173 39.478 29.247 1.00 23.16 ? 228 TYR A CA 1 ATOM 1483 C C . TYR A 1 187 ? 27.065 39.930 30.396 1.00 24.62 ? 228 TYR A C 1 ATOM 1484 O O . TYR A 1 187 ? 27.316 41.141 30.575 1.00 24.22 ? 228 TYR A O 1 ATOM 1485 C CB . TYR A 1 187 ? 27.042 38.869 28.092 1.00 23.30 ? 228 TYR A CB 1 ATOM 1486 C CG . TYR A 1 187 ? 28.291 39.659 27.802 1.00 23.38 ? 228 TYR A CG 1 ATOM 1487 C CD1 . TYR A 1 187 ? 29.503 39.309 28.396 1.00 24.84 ? 228 TYR A CD1 1 ATOM 1488 C CD2 . TYR A 1 187 ? 28.241 40.796 26.977 1.00 23.43 ? 228 TYR A CD2 1 ATOM 1489 C CE1 . TYR A 1 187 ? 30.691 40.079 28.122 1.00 25.61 ? 228 TYR A CE1 1 ATOM 1490 C CE2 . TYR A 1 187 ? 29.380 41.588 26.741 1.00 24.93 ? 228 TYR A CE2 1 ATOM 1491 C CZ . TYR A 1 187 ? 30.582 41.225 27.331 1.00 26.94 ? 228 TYR A CZ 1 ATOM 1492 O OH . TYR A 1 187 ? 31.670 42.005 27.124 1.00 29.49 ? 228 TYR A OH 1 ATOM 1493 N N . SER A 1 188 ? 27.565 38.954 31.158 1.00 23.96 ? 229 SER A N 1 ATOM 1494 C CA . SER A 1 188 ? 28.446 39.224 32.299 1.00 23.86 ? 229 SER A CA 1 ATOM 1495 C C . SER A 1 188 ? 29.916 39.058 31.875 1.00 24.52 ? 229 SER A C 1 ATOM 1496 O O . SER A 1 188 ? 30.359 37.950 31.589 1.00 25.65 ? 229 SER A O 1 ATOM 1497 C CB . SER A 1 188 ? 28.076 38.261 33.436 1.00 22.51 ? 229 SER A CB 1 ATOM 1498 O OG . SER A 1 188 ? 26.771 38.561 33.934 1.00 24.65 ? 229 SER A OG 1 ATOM 1499 N N . ASP A 1 189 ? 30.667 40.152 31.786 1.00 23.66 ? 230 ASP A N 1 ATOM 1500 C CA . ASP A 1 189 ? 32.076 40.048 31.382 1.00 25.94 ? 230 ASP A CA 1 ATOM 1501 C C . ASP A 1 189 ? 32.868 39.712 32.638 1.00 25.86 ? 230 ASP A C 1 ATOM 1502 O O . ASP A 1 189 ? 32.590 40.253 33.705 1.00 25.32 ? 230 ASP A O 1 ATOM 1503 C CB . ASP A 1 189 ? 32.541 41.401 30.824 1.00 25.87 ? 230 ASP A CB 1 ATOM 1504 C CG . ASP A 1 189 ? 33.828 41.293 30.018 1.00 27.83 ? 230 ASP A CG 1 ATOM 1505 O OD1 . ASP A 1 189 ? 33.749 41.322 28.758 1.00 29.49 ? 230 ASP A OD1 1 ATOM 1506 O OD2 . ASP A 1 189 ? 34.914 41.115 30.634 1.00 28.04 ? 230 ASP A OD2 1 ATOM 1507 N N . PRO A 1 190 ? 33.875 38.831 32.525 1.00 27.36 ? 231 PRO A N 1 ATOM 1508 C CA . PRO A 1 190 ? 34.682 38.544 33.706 1.00 28.26 ? 231 PRO A CA 1 ATOM 1509 C C . PRO A 1 190 ? 35.416 39.778 34.246 1.00 29.55 ? 231 PRO A C 1 ATOM 1510 O O . PRO A 1 190 ? 35.726 39.801 35.421 1.00 28.96 ? 231 PRO A O 1 ATOM 1511 C CB . PRO A 1 190 ? 35.698 37.503 33.219 1.00 29.36 ? 231 PRO A CB 1 ATOM 1512 C CG . PRO A 1 190 ? 35.299 37.125 31.851 1.00 32.49 ? 231 PRO A CG 1 ATOM 1513 C CD . PRO A 1 190 ? 34.147 37.933 31.386 1.00 27.37 ? 231 PRO A CD 1 ATOM 1514 N N . ALA A 1 191 ? 35.637 40.822 33.433 1.00 29.28 ? 232 ALA A N 1 ATOM 1515 C CA . ALA A 1 191 ? 36.216 42.062 33.997 1.00 29.81 ? 232 ALA A CA 1 ATOM 1516 C C . ALA A 1 191 ? 35.406 42.600 35.184 1.00 29.50 ? 232 ALA A C 1 ATOM 1517 O O . ALA A 1 191 ? 35.967 43.131 36.151 1.00 29.37 ? 232 ALA A O 1 ATOM 1518 C CB . ALA A 1 191 ? 36.321 43.135 32.923 1.00 30.62 ? 232 ALA A CB 1 ATOM 1519 N N . ASP A 1 192 ? 34.084 42.458 35.104 1.00 27.51 ? 233 ASP A N 1 ATOM 1520 C CA . ASP A 1 192 ? 33.168 43.010 36.095 1.00 27.32 ? 233 ASP A CA 1 ATOM 1521 C C . ASP A 1 192 ? 32.697 41.944 37.096 1.00 27.57 ? 233 ASP A C 1 ATOM 1522 O O . ASP A 1 192 ? 32.267 42.290 38.209 1.00 28.00 ? 233 ASP A O 1 ATOM 1523 C CB . ASP A 1 192 ? 31.957 43.590 35.351 1.00 27.72 ? 233 ASP A CB 1 ATOM 1524 C CG . ASP A 1 192 ? 32.372 44.591 34.277 1.00 27.54 ? 233 ASP A CG 1 ATOM 1525 O OD1 . ASP A 1 192 ? 32.703 45.736 34.672 1.00 30.93 ? 233 ASP A OD1 1 ATOM 1526 O OD2 . ASP A 1 192 ? 32.415 44.228 33.077 1.00 30.16 ? 233 ASP A OD2 1 ATOM 1527 N N . TYR A 1 193 ? 32.718 40.671 36.699 1.00 25.84 ? 234 TYR A N 1 ATOM 1528 C CA . TYR A 1 193 ? 32.122 39.604 37.536 1.00 25.09 ? 234 TYR A CA 1 ATOM 1529 C C . TYR A 1 193 ? 33.056 38.458 37.908 1.00 26.45 ? 234 TYR A C 1 ATOM 1530 O O . TYR A 1 193 ? 32.612 37.383 38.324 1.00 25.62 ? 234 TYR A O 1 ATOM 1531 C CB . TYR A 1 193 ? 30.817 39.074 36.891 1.00 25.59 ? 234 TYR A CB 1 ATOM 1532 C CG . TYR A 1 193 ? 29.775 40.164 36.815 1.00 23.74 ? 234 TYR A CG 1 ATOM 1533 C CD1 . TYR A 1 193 ? 29.607 40.922 35.652 1.00 23.54 ? 234 TYR A CD1 1 ATOM 1534 C CD2 . TYR A 1 193 ? 29.031 40.498 37.931 1.00 23.14 ? 234 TYR A CD2 1 ATOM 1535 C CE1 . TYR A 1 193 ? 28.683 41.982 35.596 1.00 25.04 ? 234 TYR A CE1 1 ATOM 1536 C CE2 . TYR A 1 193 ? 28.093 41.556 37.903 1.00 24.42 ? 234 TYR A CE2 1 ATOM 1537 C CZ . TYR A 1 193 ? 27.926 42.275 36.717 1.00 25.99 ? 234 TYR A CZ 1 ATOM 1538 O OH . TYR A 1 193 ? 27.028 43.309 36.678 1.00 22.96 ? 234 TYR A OH 1 ATOM 1539 N N . PHE A 1 194 ? 34.366 38.668 37.754 1.00 27.38 ? 235 PHE A N 1 ATOM 1540 C CA . PHE A 1 194 ? 35.322 37.616 38.091 1.00 28.95 ? 235 PHE A CA 1 ATOM 1541 C C . PHE A 1 194 ? 36.519 38.309 38.732 1.00 30.49 ? 235 PHE A C 1 ATOM 1542 O O . PHE A 1 194 ? 37.357 38.852 38.021 1.00 32.73 ? 235 PHE A O 1 ATOM 1543 C CB . PHE A 1 194 ? 35.771 36.846 36.846 1.00 28.96 ? 235 PHE A CB 1 ATOM 1544 C CG . PHE A 1 194 ? 36.508 35.574 37.157 1.00 29.14 ? 235 PHE A CG 1 ATOM 1545 C CD1 . PHE A 1 194 ? 35.820 34.365 37.224 1.00 30.28 ? 235 PHE A CD1 1 ATOM 1546 C CD2 . PHE A 1 194 ? 37.884 35.583 37.405 1.00 32.04 ? 235 PHE A CD2 1 ATOM 1547 C CE1 . PHE A 1 194 ? 36.483 33.168 37.541 1.00 32.09 ? 235 PHE A CE1 1 ATOM 1548 C CE2 . PHE A 1 194 ? 38.549 34.395 37.719 1.00 32.43 ? 235 PHE A CE2 1 ATOM 1549 C CZ . PHE A 1 194 ? 37.854 33.182 37.774 1.00 32.91 ? 235 PHE A CZ 1 ATOM 1550 N N . ALA A 1 195 ? 36.577 38.311 40.056 1.00 30.72 ? 236 ALA A N 1 ATOM 1551 C CA . ALA A 1 195 ? 37.712 38.931 40.746 1.00 33.32 ? 236 ALA A CA 1 ATOM 1552 C C . ALA A 1 195 ? 38.978 38.114 40.519 1.00 35.79 ? 236 ALA A C 1 ATOM 1553 O O . ALA A 1 195 ? 38.944 36.901 40.628 1.00 35.12 ? 236 ALA A O 1 ATOM 1554 C CB . ALA A 1 195 ? 37.412 39.024 42.217 1.00 32.72 ? 236 ALA A CB 1 ATOM 1555 N N . PRO A 1 196 ? 40.098 38.782 40.194 1.00 37.83 ? 237 PRO A N 1 ATOM 1556 C CA . PRO A 1 196 ? 41.360 38.072 39.999 1.00 39.65 ? 237 PRO A CA 1 ATOM 1557 C C . PRO A 1 196 ? 41.730 37.243 41.236 1.00 39.04 ? 237 PRO A C 1 ATOM 1558 O O . PRO A 1 196 ? 41.546 37.714 42.362 1.00 39.16 ? 237 PRO A O 1 ATOM 1559 C CB . PRO A 1 196 ? 42.361 39.205 39.742 1.00 41.30 ? 237 PRO A CB 1 ATOM 1560 C CG . PRO A 1 196 ? 41.499 40.326 39.178 1.00 41.28 ? 237 PRO A CG 1 ATOM 1561 C CD . PRO A 1 196 ? 40.200 40.230 39.901 1.00 38.87 ? 237 PRO A CD 1 ATOM 1562 N N . GLY A 1 197 ? 42.174 36.004 41.006 1.00 39.63 ? 238 GLY A N 1 ATOM 1563 C CA . GLY A 1 197 ? 42.726 35.136 42.060 1.00 39.79 ? 238 GLY A CA 1 ATOM 1564 C C . GLY A 1 197 ? 41.717 34.409 42.932 1.00 39.50 ? 238 GLY A C 1 ATOM 1565 O O . GLY A 1 197 ? 42.103 33.731 43.888 1.00 41.47 ? 238 GLY A O 1 ATOM 1566 N N . VAL A 1 198 ? 40.431 34.505 42.589 1.00 35.18 ? 239 VAL A N 1 ATOM 1567 C CA . VAL A 1 198 ? 39.383 33.755 43.297 1.00 33.36 ? 239 VAL A CA 1 ATOM 1568 C C . VAL A 1 198 ? 38.787 32.738 42.335 1.00 32.87 ? 239 VAL A C 1 ATOM 1569 O O . VAL A 1 198 ? 38.731 32.962 41.138 1.00 33.24 ? 239 VAL A O 1 ATOM 1570 C CB . VAL A 1 198 ? 38.311 34.730 43.965 1.00 33.10 ? 239 VAL A CB 1 ATOM 1571 C CG1 A VAL A 1 198 ? 38.351 36.068 43.336 0.50 34.60 ? 239 VAL A CG1 1 ATOM 1572 C CG1 B VAL A 1 198 ? 37.199 33.957 44.675 0.50 30.71 ? 239 VAL A CG1 1 ATOM 1573 C CG2 A VAL A 1 198 ? 36.918 34.130 43.969 0.50 30.51 ? 239 VAL A CG2 1 ATOM 1574 C CG2 B VAL A 1 198 ? 39.004 35.726 44.911 0.50 32.60 ? 239 VAL A CG2 1 ATOM 1575 N N . LYS A 1 199 ? 38.418 31.585 42.865 1.00 32.53 ? 240 LYS A N 1 ATOM 1576 C CA . LYS A 1 199 ? 37.870 30.505 42.076 1.00 32.97 ? 240 LYS A CA 1 ATOM 1577 C C . LYS A 1 199 ? 36.379 30.733 41.785 1.00 31.57 ? 240 LYS A C 1 ATOM 1578 O O . LYS A 1 199 ? 35.715 31.437 42.550 1.00 31.75 ? 240 LYS A O 1 ATOM 1579 C CB . LYS A 1 199 ? 38.038 29.204 42.859 1.00 33.85 ? 240 LYS A CB 1 ATOM 1580 C CG . LYS A 1 199 ? 39.523 28.672 42.889 1.00 36.90 ? 240 LYS A CG 1 ATOM 1581 C CD . LYS A 1 199 ? 40.124 28.553 41.482 1.00 43.26 ? 240 LYS A CD 1 ATOM 1582 C CE . LYS A 1 199 ? 41.591 28.038 41.528 1.00 47.70 ? 240 LYS A CE 1 ATOM 1583 N NZ . LYS A 1 199 ? 42.256 27.975 40.173 1.00 50.36 ? 240 LYS A NZ 1 ATOM 1584 N N . SER A 1 200 ? 35.883 30.153 40.686 1.00 31.18 ? 241 SER A N 1 ATOM 1585 C CA A SER A 1 200 ? 34.448 30.144 40.333 0.50 30.19 ? 241 SER A CA 1 ATOM 1586 C CA B SER A 1 200 ? 34.454 30.261 40.436 0.50 30.16 ? 241 SER A CA 1 ATOM 1587 C C . SER A 1 200 ? 33.687 29.237 41.271 1.00 29.22 ? 241 SER A C 1 ATOM 1588 O O . SER A 1 200 ? 34.252 28.220 41.741 1.00 30.22 ? 241 SER A O 1 ATOM 1589 C CB A SER A 1 200 ? 34.223 29.549 38.927 0.50 31.29 ? 241 SER A CB 1 ATOM 1590 C CB B SER A 1 200 ? 34.135 30.155 38.935 0.50 30.95 ? 241 SER A CB 1 ATOM 1591 O OG A SER A 1 200 ? 34.890 30.235 37.886 0.50 32.81 ? 241 SER A OG 1 ATOM 1592 O OG B SER A 1 200 ? 34.669 28.967 38.369 0.50 34.10 ? 241 SER A OG 1 ATOM 1593 N N . TYR A 1 201 ? 32.390 29.530 41.461 1.00 27.90 ? 242 TYR A N 1 ATOM 1594 C CA . TYR A 1 201 ? 31.512 28.675 42.219 1.00 28.13 ? 242 TYR A CA 1 ATOM 1595 C C . TYR A 1 201 ? 31.538 27.270 41.594 1.00 29.70 ? 242 TYR A C 1 ATOM 1596 O O . TYR A 1 201 ? 31.507 27.171 40.365 1.00 30.74 ? 242 TYR A O 1 ATOM 1597 C CB . TYR A 1 201 ? 30.082 29.251 42.212 1.00 27.02 ? 242 TYR A CB 1 ATOM 1598 C CG . TYR A 1 201 ? 29.332 28.667 43.358 1.00 27.61 ? 242 TYR A CG 1 ATOM 1599 C CD1 . TYR A 1 201 ? 29.605 29.097 44.656 1.00 29.68 ? 242 TYR A CD1 1 ATOM 1600 C CD2 . TYR A 1 201 ? 28.454 27.596 43.166 1.00 30.51 ? 242 TYR A CD2 1 ATOM 1601 C CE1 . TYR A 1 201 ? 28.986 28.526 45.722 1.00 30.96 ? 242 TYR A CE1 1 ATOM 1602 C CE2 . TYR A 1 201 ? 27.813 27.018 44.234 1.00 31.03 ? 242 TYR A CE2 1 ATOM 1603 C CZ . TYR A 1 201 ? 28.080 27.509 45.506 1.00 32.29 ? 242 TYR A CZ 1 ATOM 1604 O OH . TYR A 1 201 ? 27.503 26.916 46.577 1.00 37.62 ? 242 TYR A OH 1 ATOM 1605 N N . PRO A 1 202 ? 31.584 26.192 42.422 1.00 30.70 ? 243 PRO A N 1 ATOM 1606 C CA . PRO A 1 202 ? 31.428 26.072 43.890 1.00 31.13 ? 243 PRO A CA 1 ATOM 1607 C C . PRO A 1 202 ? 32.689 26.176 44.743 1.00 32.95 ? 243 PRO A C 1 ATOM 1608 O O . PRO A 1 202 ? 32.613 25.966 45.957 1.00 34.23 ? 243 PRO A O 1 ATOM 1609 C CB . PRO A 1 202 ? 30.802 24.686 44.039 1.00 31.31 ? 243 PRO A CB 1 ATOM 1610 C CG . PRO A 1 202 ? 31.584 23.879 42.969 1.00 31.42 ? 243 PRO A CG 1 ATOM 1611 C CD . PRO A 1 202 ? 31.572 24.853 41.785 1.00 31.64 ? 243 PRO A CD 1 ATOM 1612 N N . ASP A 1 203 ? 33.815 26.492 44.120 1.00 33.12 ? 244 ASP A N 1 ATOM 1613 C CA . ASP A 1 203 ? 35.103 26.474 44.816 1.00 34.75 ? 244 ASP A CA 1 ATOM 1614 C C . ASP A 1 203 ? 35.514 27.854 45.300 1.00 33.39 ? 244 ASP A C 1 ATOM 1615 O O . ASP A 1 203 ? 36.501 27.997 46.008 1.00 34.37 ? 244 ASP A O 1 ATOM 1616 C CB . ASP A 1 203 ? 36.162 25.802 43.940 1.00 36.62 ? 244 ASP A CB 1 ATOM 1617 C CG . ASP A 1 203 ? 35.737 24.387 43.524 1.00 41.76 ? 244 ASP A CG 1 ATOM 1618 O OD1 . ASP A 1 203 ? 35.399 23.558 44.418 1.00 44.87 ? 244 ASP A OD1 1 ATOM 1619 O OD2 . ASP A 1 203 ? 35.643 24.130 42.301 1.00 49.47 ? 244 ASP A OD2 1 ATOM 1620 N N . GLY A 1 204 ? 34.706 28.864 44.960 1.00 32.19 ? 245 GLY A N 1 ATOM 1621 C CA . GLY A 1 204 ? 34.958 30.229 45.383 1.00 29.78 ? 245 GLY A CA 1 ATOM 1622 C C . GLY A 1 204 ? 33.732 31.044 45.021 1.00 29.27 ? 245 GLY A C 1 ATOM 1623 O O . GLY A 1 204 ? 32.703 30.478 44.597 1.00 30.35 ? 245 GLY A O 1 ATOM 1624 N N . TRP A 1 205 ? 33.842 32.358 45.173 1.00 27.65 ? 246 TRP A N 1 ATOM 1625 C CA . TRP A 1 205 ? 32.654 33.208 45.004 1.00 26.44 ? 246 TRP A CA 1 ATOM 1626 C C . TRP A 1 205 ? 32.524 33.894 43.637 1.00 26.26 ? 246 TRP A C 1 ATOM 1627 O O . TRP A 1 205 ? 31.644 34.744 43.441 1.00 25.61 ? 246 TRP A O 1 ATOM 1628 C CB . TRP A 1 205 ? 32.520 34.215 46.179 1.00 26.52 ? 246 TRP A CB 1 ATOM 1629 C CG . TRP A 1 205 ? 33.793 34.969 46.536 1.00 29.23 ? 246 TRP A CG 1 ATOM 1630 C CD1 . TRP A 1 205 ? 34.739 34.577 47.426 1.00 32.40 ? 246 TRP A CD1 1 ATOM 1631 C CD2 . TRP A 1 205 ? 34.232 36.229 46.000 1.00 28.93 ? 246 TRP A CD2 1 ATOM 1632 N NE1 . TRP A 1 205 ? 35.741 35.529 47.496 1.00 34.26 ? 246 TRP A NE1 1 ATOM 1633 C CE2 . TRP A 1 205 ? 35.452 36.550 46.630 1.00 31.53 ? 246 TRP A CE2 1 ATOM 1634 C CE3 . TRP A 1 205 ? 33.709 37.116 45.051 1.00 32.53 ? 246 TRP A CE3 1 ATOM 1635 C CZ2 . TRP A 1 205 ? 36.171 37.721 46.338 1.00 32.49 ? 246 TRP A CZ2 1 ATOM 1636 C CZ3 . TRP A 1 205 ? 34.418 38.290 44.759 1.00 35.25 ? 246 TRP A CZ3 1 ATOM 1637 C CH2 . TRP A 1 205 ? 35.645 38.583 45.412 1.00 33.34 ? 246 TRP A CH2 1 ATOM 1638 N N . ASN A 1 206 ? 33.340 33.486 42.666 1.00 26.59 ? 247 ASN A N 1 ATOM 1639 C CA . ASN A 1 206 ? 33.284 34.068 41.306 1.00 26.36 ? 247 ASN A CA 1 ATOM 1640 C C . ASN A 1 206 ? 32.221 33.427 40.415 1.00 26.47 ? 247 ASN A C 1 ATOM 1641 O O . ASN A 1 206 ? 31.773 32.308 40.680 1.00 25.86 ? 247 ASN A O 1 ATOM 1642 C CB . ASN A 1 206 ? 34.653 33.988 40.585 1.00 26.91 ? 247 ASN A CB 1 ATOM 1643 C CG . ASN A 1 206 ? 35.500 35.224 40.805 1.00 26.83 ? 247 ASN A CG 1 ATOM 1644 O OD1 . ASN A 1 206 ? 34.992 36.295 41.199 1.00 28.07 ? 247 ASN A OD1 1 ATOM 1645 N ND2 . ASN A 1 206 ? 36.827 35.079 40.591 1.00 27.74 ? 247 ASN A ND2 1 ATOM 1646 N N . LEU A 1 207 ? 31.816 34.164 39.373 1.00 25.62 ? 248 LEU A N 1 ATOM 1647 C CA . LEU A 1 207 ? 30.856 33.673 38.401 1.00 24.29 ? 248 LEU A CA 1 ATOM 1648 C C . LEU A 1 207 ? 31.533 32.755 37.391 1.00 25.32 ? 248 LEU A C 1 ATOM 1649 O O . LEU A 1 207 ? 32.499 33.156 36.742 1.00 26.87 ? 248 LEU A O 1 ATOM 1650 C CB . LEU A 1 207 ? 30.256 34.866 37.646 1.00 23.97 ? 248 LEU A CB 1 ATOM 1651 C CG . LEU A 1 207 ? 29.145 34.607 36.628 1.00 25.42 ? 248 LEU A CG 1 ATOM 1652 C CD1 . LEU A 1 207 ? 27.884 34.160 37.323 1.00 24.21 ? 248 LEU A CD1 1 ATOM 1653 C CD2 . LEU A 1 207 ? 28.899 35.902 35.826 1.00 26.34 ? 248 LEU A CD2 1 ATOM 1654 N N . PRO A 1 208 ? 31.000 31.545 37.225 1.00 25.45 ? 249 PRO A N 1 ATOM 1655 C CA . PRO A 1 208 ? 31.508 30.694 36.146 1.00 25.23 ? 249 PRO A CA 1 ATOM 1656 C C . PRO A 1 208 ? 30.977 31.106 34.779 1.00 25.29 ? 249 PRO A C 1 ATOM 1657 O O . PRO A 1 208 ? 30.015 31.880 34.682 1.00 25.13 ? 249 PRO A O 1 ATOM 1658 C CB . PRO A 1 208 ? 30.978 29.293 36.498 1.00 27.57 ? 249 PRO A CB 1 ATOM 1659 C CG . PRO A 1 208 ? 30.002 29.449 37.492 1.00 25.71 ? 249 PRO A CG 1 ATOM 1660 C CD . PRO A 1 208 ? 29.961 30.884 38.032 1.00 25.48 ? 249 PRO A CD 1 ATOM 1661 N N . GLY A 1 209 ? 31.588 30.545 33.733 1.00 27.29 ? 250 GLY A N 1 ATOM 1662 C CA . GLY A 1 209 ? 31.276 30.998 32.375 1.00 28.07 ? 250 GLY A CA 1 ATOM 1663 C C . GLY A 1 209 ? 29.866 30.668 31.938 1.00 26.91 ? 250 GLY A C 1 ATOM 1664 O O . GLY A 1 209 ? 29.365 31.255 30.970 1.00 27.31 ? 250 GLY A O 1 ATOM 1665 N N . GLY A 1 210 ? 29.270 29.682 32.596 1.00 26.38 ? 251 GLY A N 1 ATOM 1666 C CA . GLY A 1 210 ? 27.856 29.338 32.379 1.00 25.50 ? 251 GLY A CA 1 ATOM 1667 C C . GLY A 1 210 ? 26.878 30.083 33.276 1.00 25.59 ? 251 GLY A C 1 ATOM 1668 O O . GLY A 1 210 ? 25.675 29.912 33.128 1.00 24.81 ? 251 GLY A O 1 ATOM 1669 N N . GLY A 1 211 ? 27.367 30.886 34.224 1.00 25.17 ? 252 GLY A N 1 ATOM 1670 C CA . GLY A 1 211 ? 26.429 31.648 35.075 1.00 23.28 ? 252 GLY A CA 1 ATOM 1671 C C . GLY A 1 211 ? 25.810 32.829 34.334 1.00 22.80 ? 252 GLY A C 1 ATOM 1672 O O . GLY A 1 211 ? 26.437 33.418 33.447 1.00 23.78 ? 252 GLY A O 1 ATOM 1673 N N . VAL A 1 212 ? 24.589 33.171 34.721 1.00 22.83 ? 253 VAL A N 1 ATOM 1674 C CA . VAL A 1 212 ? 23.861 34.257 34.087 1.00 21.92 ? 253 VAL A CA 1 ATOM 1675 C C . VAL A 1 212 ? 23.070 35.050 35.132 1.00 21.45 ? 253 VAL A C 1 ATOM 1676 O O . VAL A 1 212 ? 22.468 34.487 36.054 1.00 22.86 ? 253 VAL A O 1 ATOM 1677 C CB . VAL A 1 212 ? 22.840 33.698 33.042 1.00 21.60 ? 253 VAL A CB 1 ATOM 1678 C CG1 . VAL A 1 212 ? 22.259 34.863 32.226 1.00 23.80 ? 253 VAL A CG1 1 ATOM 1679 C CG2 . VAL A 1 212 ? 23.522 32.682 32.069 1.00 23.07 ? 253 VAL A CG2 1 ATOM 1680 N N . GLN A 1 213 ? 23.085 36.368 34.959 1.00 20.69 ? 254 GLN A N 1 ATOM 1681 C CA . GLN A 1 213 ? 22.388 37.286 35.872 1.00 19.71 ? 254 GLN A CA 1 ATOM 1682 C C . GLN A 1 213 ? 20.980 37.505 35.326 1.00 20.01 ? 254 GLN A C 1 ATOM 1683 O O . GLN A 1 213 ? 20.829 38.078 34.231 1.00 21.47 ? 254 GLN A O 1 ATOM 1684 C CB . GLN A 1 213 ? 23.158 38.610 35.878 1.00 19.66 ? 254 GLN A CB 1 ATOM 1685 C CG . GLN A 1 213 ? 22.476 39.704 36.760 1.00 19.33 ? 254 GLN A CG 1 ATOM 1686 C CD . GLN A 1 213 ? 23.077 41.087 36.568 1.00 21.28 ? 254 GLN A CD 1 ATOM 1687 O OE1 . GLN A 1 213 ? 22.339 42.071 36.572 1.00 20.85 ? 254 GLN A OE1 1 ATOM 1688 N NE2 . GLN A 1 213 ? 24.396 41.186 36.467 1.00 21.27 ? 254 GLN A NE2 1 ATOM 1689 N N . ARG A 1 214 ? 19.970 37.038 36.064 1.00 19.87 ? 255 ARG A N 1 ATOM 1690 C CA . ARG A 1 214 ? 18.578 37.408 35.794 1.00 20.07 ? 255 ARG A CA 1 ATOM 1691 C C . ARG A 1 214 ? 18.294 38.864 36.184 1.00 19.71 ? 255 ARG A C 1 ATOM 1692 O O . ARG A 1 214 ? 19.071 39.493 36.885 1.00 19.54 ? 255 ARG A O 1 ATOM 1693 C CB . ARG A 1 214 ? 17.639 36.509 36.629 1.00 19.34 ? 255 ARG A CB 1 ATOM 1694 C CG . ARG A 1 214 ? 17.627 35.054 36.081 1.00 19.83 ? 255 ARG A CG 1 ATOM 1695 C CD . ARG A 1 214 ? 17.225 34.071 37.185 1.00 19.50 ? 255 ARG A CD 1 ATOM 1696 N NE . ARG A 1 214 ? 17.417 32.664 36.779 1.00 21.51 ? 255 ARG A NE 1 ATOM 1697 C CZ . ARG A 1 214 ? 18.627 32.080 36.743 1.00 22.79 ? 255 ARG A CZ 1 ATOM 1698 N NH1 . ARG A 1 214 ? 19.730 32.781 37.050 1.00 23.01 ? 255 ARG A NH1 1 ATOM 1699 N NH2 . ARG A 1 214 ? 18.747 30.787 36.392 1.00 22.54 ? 255 ARG A NH2 1 ATOM 1700 N N . GLY A 1 215 ? 17.144 39.369 35.744 1.00 19.25 ? 256 GLY A N 1 ATOM 1701 C CA . GLY A 1 215 ? 16.667 40.650 36.299 1.00 19.36 ? 256 GLY A CA 1 ATOM 1702 C C . GLY A 1 215 ? 15.719 41.359 35.382 1.00 20.55 ? 256 GLY A C 1 ATOM 1703 O O . GLY A 1 215 ? 15.796 41.209 34.173 1.00 19.53 ? 256 GLY A O 1 ATOM 1704 N N . ASN A 1 216 ? 14.839 42.170 35.963 1.00 19.05 ? 257 ASN A N 1 ATOM 1705 C CA . ASN A 1 216 ? 13.879 42.874 35.129 1.00 19.48 ? 257 ASN A CA 1 ATOM 1706 C C . ASN A 1 216 ? 14.504 44.039 34.406 1.00 18.82 ? 257 ASN A C 1 ATOM 1707 O O . ASN A 1 216 ? 15.540 44.582 34.824 1.00 18.99 ? 257 ASN A O 1 ATOM 1708 C CB . ASN A 1 216 ? 12.647 43.308 35.950 1.00 19.23 ? 257 ASN A CB 1 ATOM 1709 C CG . ASN A 1 216 ? 12.855 44.623 36.673 1.00 21.26 ? 257 ASN A CG 1 ATOM 1710 O OD1 . ASN A 1 216 ? 12.876 45.699 36.062 1.00 22.22 ? 257 ASN A OD1 1 ATOM 1711 N ND2 . ASN A 1 216 ? 12.913 44.563 38.005 1.00 22.59 ? 257 ASN A ND2 1 ATOM 1712 N N . ILE A 1 217 ? 13.866 44.415 33.300 1.00 19.85 ? 258 ILE A N 1 ATOM 1713 C CA . ILE A 1 217 ? 14.389 45.476 32.448 1.00 19.93 ? 258 ILE A CA 1 ATOM 1714 C C . ILE A 1 217 ? 13.372 46.608 32.289 1.00 20.87 ? 258 ILE A C 1 ATOM 1715 O O . ILE A 1 217 ? 13.354 47.337 31.283 1.00 22.40 ? 258 ILE A O 1 ATOM 1716 C CB . ILE A 1 217 ? 14.829 44.929 31.052 1.00 20.32 ? 258 ILE A CB 1 ATOM 1717 C CG1 . ILE A 1 217 ? 13.709 44.054 30.461 1.00 20.65 ? 258 ILE A CG1 1 ATOM 1718 C CG2 . ILE A 1 217 ? 16.144 44.125 31.186 1.00 22.03 ? 258 ILE A CG2 1 ATOM 1719 C CD1 . ILE A 1 217 ? 13.910 43.771 28.939 1.00 25.13 ? 258 ILE A CD1 1 ATOM 1720 N N . LEU A 1 218 ? 12.518 46.759 33.279 1.00 21.80 ? 259 LEU A N 1 ATOM 1721 C CA . LEU A 1 218 ? 11.466 47.797 33.254 1.00 23.64 ? 259 LEU A CA 1 ATOM 1722 C C . LEU A 1 218 ? 12.025 49.162 33.533 1.00 24.35 ? 259 LEU A C 1 ATOM 1723 O O . LEU A 1 218 ? 13.005 49.314 34.234 1.00 26.62 ? 259 LEU A O 1 ATOM 1724 C CB . LEU A 1 218 ? 10.441 47.538 34.387 1.00 23.77 ? 259 LEU A CB 1 ATOM 1725 C CG . LEU A 1 218 ? 9.521 46.315 34.252 1.00 25.92 ? 259 LEU A CG 1 ATOM 1726 C CD1 . LEU A 1 218 ? 8.711 46.145 35.570 1.00 29.56 ? 259 LEU A CD1 1 ATOM 1727 C CD2 . LEU A 1 218 ? 8.577 46.471 33.124 1.00 28.32 ? 259 LEU A CD2 1 ATOM 1728 N N . ASN A 1 219 ? 11.314 50.173 33.035 1.00 24.61 ? 260 ASN A N 1 ATOM 1729 C CA A ASN A 1 219 ? 11.614 51.559 33.410 0.50 24.38 ? 260 ASN A CA 1 ATOM 1730 C CA B ASN A 1 219 ? 11.588 51.576 33.328 0.50 25.17 ? 260 ASN A CA 1 ATOM 1731 C C . ASN A 1 219 ? 10.314 52.182 33.939 1.00 23.80 ? 260 ASN A C 1 ATOM 1732 O O . ASN A 1 219 ? 9.632 52.966 33.266 1.00 25.12 ? 260 ASN A O 1 ATOM 1733 C CB A ASN A 1 219 ? 12.175 52.322 32.205 0.50 25.52 ? 260 ASN A CB 1 ATOM 1734 C CB B ASN A 1 219 ? 11.916 52.260 31.989 0.50 26.46 ? 260 ASN A CB 1 ATOM 1735 C CG A ASN A 1 219 ? 13.611 51.929 31.865 0.50 26.03 ? 260 ASN A CG 1 ATOM 1736 C CG B ASN A 1 219 ? 12.163 53.752 32.128 0.50 30.24 ? 260 ASN A CG 1 ATOM 1737 O OD1 A ASN A 1 219 ? 14.566 52.418 32.471 0.50 30.09 ? 260 ASN A OD1 1 ATOM 1738 O OD1 B ASN A 1 219 ? 12.523 54.228 33.202 0.50 33.54 ? 260 ASN A OD1 1 ATOM 1739 N ND2 A ASN A 1 219 ? 13.768 51.074 30.870 0.50 24.14 ? 260 ASN A ND2 1 ATOM 1740 N ND2 B ASN A 1 219 ? 11.967 54.499 31.034 0.50 32.77 ? 260 ASN A ND2 1 ATOM 1741 N N . LEU A 1 220 ? 9.957 51.788 35.168 1.00 22.63 ? 261 LEU A N 1 ATOM 1742 C CA . LEU A 1 220 ? 8.651 52.161 35.758 1.00 21.72 ? 261 LEU A CA 1 ATOM 1743 C C . LEU A 1 220 ? 8.650 53.550 36.371 1.00 22.05 ? 261 LEU A C 1 ATOM 1744 O O . LEU A 1 220 ? 7.559 54.128 36.589 1.00 20.00 ? 261 LEU A O 1 ATOM 1745 C CB . LEU A 1 220 ? 8.278 51.211 36.932 1.00 23.09 ? 261 LEU A CB 1 ATOM 1746 C CG . LEU A 1 220 ? 7.981 49.755 36.524 1.00 23.51 ? 261 LEU A CG 1 ATOM 1747 C CD1 . LEU A 1 220 ? 7.865 48.851 37.774 1.00 24.75 ? 261 LEU A CD1 1 ATOM 1748 C CD2 . LEU A 1 220 ? 6.679 49.708 35.747 1.00 24.27 ? 261 LEU A CD2 1 ATOM 1749 N N . ASN A 1 221 ? 9.841 54.075 36.647 1.00 19.86 ? 262 ASN A N 1 ATOM 1750 C CA . ASN A 1 221 ? 9.955 55.406 37.320 1.00 20.04 ? 262 ASN A CA 1 ATOM 1751 C C . ASN A 1 221 ? 9.046 55.546 38.528 1.00 19.26 ? 262 ASN A C 1 ATOM 1752 O O . ASN A 1 221 ? 8.377 56.573 38.731 1.00 19.90 ? 262 ASN A O 1 ATOM 1753 C CB . ASN A 1 221 ? 9.722 56.558 36.352 1.00 20.36 ? 262 ASN A CB 1 ATOM 1754 C CG . ASN A 1 221 ? 10.824 56.645 35.314 1.00 22.46 ? 262 ASN A CG 1 ATOM 1755 O OD1 . ASN A 1 221 ? 11.981 56.362 35.625 1.00 23.72 ? 262 ASN A OD1 1 ATOM 1756 N ND2 . ASN A 1 221 ? 10.467 56.984 34.072 1.00 25.80 ? 262 ASN A ND2 1 ATOM 1757 N N . GLY A 1 222 ? 8.968 54.472 39.282 1.00 17.90 ? 263 GLY A N 1 ATOM 1758 C CA . GLY A 1 222 ? 8.294 54.544 40.557 1.00 17.67 ? 263 GLY A CA 1 ATOM 1759 C C . GLY A 1 222 ? 6.837 54.186 40.504 1.00 16.52 ? 263 GLY A C 1 ATOM 1760 O O . GLY A 1 222 ? 6.147 54.304 41.543 1.00 17.73 ? 263 GLY A O 1 ATOM 1761 N N . ALA A 1 223 ? 6.343 53.702 39.371 1.00 16.09 ? 264 ALA A N 1 ATOM 1762 C CA . ALA A 1 223 ? 4.881 53.513 39.267 1.00 16.01 ? 264 ALA A CA 1 ATOM 1763 C C . ALA A 1 223 ? 4.363 52.251 39.983 1.00 17.27 ? 264 ALA A C 1 ATOM 1764 O O . ALA A 1 223 ? 3.154 52.197 40.328 1.00 20.30 ? 264 ALA A O 1 ATOM 1765 C CB . ALA A 1 223 ? 4.438 53.433 37.752 1.00 17.57 ? 264 ALA A CB 1 ATOM 1766 N N . GLY A 1 224 ? 5.224 51.264 40.197 1.00 18.18 ? 265 GLY A N 1 ATOM 1767 C CA . GLY A 1 224 ? 4.723 49.954 40.730 1.00 17.72 ? 265 GLY A CA 1 ATOM 1768 C C . GLY A 1 224 ? 4.130 49.082 39.625 1.00 17.82 ? 265 GLY A C 1 ATOM 1769 O O . GLY A 1 224 ? 4.610 49.113 38.488 1.00 19.50 ? 265 GLY A O 1 ATOM 1770 N N . ASP A 1 225 ? 3.083 48.317 39.928 1.00 16.75 ? 266 ASP A N 1 ATOM 1771 C CA . ASP A 1 225 ? 2.477 47.441 38.892 1.00 18.24 ? 266 ASP A CA 1 ATOM 1772 C C . ASP A 1 225 ? 2.218 48.249 37.616 1.00 19.69 ? 266 ASP A C 1 ATOM 1773 O O . ASP A 1 225 ? 1.538 49.271 37.653 1.00 19.54 ? 266 ASP A O 1 ATOM 1774 C CB . ASP A 1 225 ? 1.164 46.883 39.459 1.00 20.01 ? 266 ASP A CB 1 ATOM 1775 C CG . ASP A 1 225 ? 0.320 46.214 38.404 1.00 21.08 ? 266 ASP A CG 1 ATOM 1776 O OD1 . ASP A 1 225 ? 0.846 45.453 37.567 1.00 20.67 ? 266 ASP A OD1 1 ATOM 1777 O OD2 . ASP A 1 225 ? -0.914 46.448 38.442 1.00 19.74 ? 266 ASP A OD2 1 ATOM 1778 N N . PRO A 1 226 ? 2.680 47.740 36.461 1.00 21.28 ? 267 PRO A N 1 ATOM 1779 C CA . PRO A 1 226 ? 2.529 48.496 35.250 1.00 22.22 ? 267 PRO A CA 1 ATOM 1780 C C . PRO A 1 226 ? 1.056 48.790 34.842 1.00 20.96 ? 267 PRO A C 1 ATOM 1781 O O . PRO A 1 226 ? 0.781 49.765 34.094 1.00 22.41 ? 267 PRO A O 1 ATOM 1782 C CB . PRO A 1 226 ? 3.175 47.570 34.187 1.00 23.53 ? 267 PRO A CB 1 ATOM 1783 C CG . PRO A 1 226 ? 4.169 46.762 34.926 1.00 24.17 ? 267 PRO A CG 1 ATOM 1784 C CD . PRO A 1 226 ? 3.640 46.614 36.341 1.00 21.54 ? 267 PRO A CD 1 ATOM 1785 N N . LEU A 1 227 ? 0.125 47.960 35.324 1.00 19.51 ? 268 LEU A N 1 ATOM 1786 C CA . LEU A 1 227 ? -1.289 48.096 34.927 1.00 20.38 ? 268 LEU A CA 1 ATOM 1787 C C . LEU A 1 227 ? -2.134 49.013 35.821 1.00 18.37 ? 268 LEU A C 1 ATOM 1788 O O . LEU A 1 227 ? -3.248 49.386 35.420 1.00 19.06 ? 268 LEU A O 1 ATOM 1789 C CB . LEU A 1 227 ? -1.945 46.701 34.830 1.00 19.41 ? 268 LEU A CB 1 ATOM 1790 C CG . LEU A 1 227 ? -1.216 45.710 33.910 1.00 22.04 ? 268 LEU A CG 1 ATOM 1791 C CD1 . LEU A 1 227 ? -2.039 44.450 33.861 1.00 24.33 ? 268 LEU A CD1 1 ATOM 1792 C CD2 . LEU A 1 227 ? -1.054 46.296 32.504 1.00 24.68 ? 268 LEU A CD2 1 ATOM 1793 N N . THR A 1 228 ? -1.620 49.424 36.994 1.00 18.04 ? 269 THR A N 1 ATOM 1794 C CA . THR A 1 228 ? -2.437 50.162 37.958 1.00 18.11 ? 269 THR A CA 1 ATOM 1795 C C . THR A 1 228 ? -1.716 51.351 38.594 1.00 18.19 ? 269 THR A C 1 ATOM 1796 O O . THR A 1 228 ? -1.728 51.514 39.814 1.00 17.29 ? 269 THR A O 1 ATOM 1797 C CB . THR A 1 228 ? -2.885 49.190 39.124 1.00 17.27 ? 269 THR A CB 1 ATOM 1798 O OG1 . THR A 1 228 ? -1.719 48.604 39.752 1.00 16.78 ? 269 THR A OG1 1 ATOM 1799 C CG2 . THR A 1 228 ? -3.857 48.067 38.558 1.00 19.30 ? 269 THR A CG2 1 ATOM 1800 N N . PRO A 1 229 ? -1.076 52.207 37.780 1.00 18.50 ? 270 PRO A N 1 ATOM 1801 C CA . PRO A 1 229 ? -0.315 53.293 38.406 1.00 17.93 ? 270 PRO A CA 1 ATOM 1802 C C . PRO A 1 229 ? -1.175 54.239 39.211 1.00 18.20 ? 270 PRO A C 1 ATOM 1803 O O . PRO A 1 229 ? -2.234 54.699 38.724 1.00 19.83 ? 270 PRO A O 1 ATOM 1804 C CB . PRO A 1 229 ? 0.341 54.017 37.204 1.00 19.09 ? 270 PRO A CB 1 ATOM 1805 C CG . PRO A 1 229 ? -0.604 53.676 36.027 1.00 19.18 ? 270 PRO A CG 1 ATOM 1806 C CD . PRO A 1 229 ? -1.005 52.248 36.298 1.00 20.35 ? 270 PRO A CD 1 ATOM 1807 N N . GLY A 1 230 ? -0.761 54.460 40.473 1.00 18.39 ? 271 GLY A N 1 ATOM 1808 C CA . GLY A 1 230 ? -1.511 55.356 41.371 1.00 18.23 ? 271 GLY A CA 1 ATOM 1809 C C . GLY A 1 230 ? -2.399 54.681 42.387 1.00 19.24 ? 271 GLY A C 1 ATOM 1810 O O . GLY A 1 230 ? -2.797 55.311 43.351 1.00 20.16 ? 271 GLY A O 1 ATOM 1811 N N . TYR A 1 231 ? -2.814 53.437 42.103 1.00 18.34 ? 272 TYR A N 1 ATOM 1812 C CA . TYR A 1 231 ? -3.849 52.787 42.907 1.00 17.73 ? 272 TYR A CA 1 ATOM 1813 C C . TYR A 1 231 ? -3.474 51.328 43.168 1.00 16.85 ? 272 TYR A C 1 ATOM 1814 O O . TYR A 1 231 ? -2.827 50.673 42.314 1.00 17.62 ? 272 TYR A O 1 ATOM 1815 C CB . TYR A 1 231 ? -5.218 52.845 42.134 1.00 17.74 ? 272 TYR A CB 1 ATOM 1816 C CG . TYR A 1 231 ? -5.535 54.276 41.761 1.00 19.10 ? 272 TYR A CG 1 ATOM 1817 C CD1 . TYR A 1 231 ? -6.090 55.154 42.700 1.00 19.47 ? 272 TYR A CD1 1 ATOM 1818 C CD2 . TYR A 1 231 ? -5.182 54.773 40.514 1.00 20.25 ? 272 TYR A CD2 1 ATOM 1819 C CE1 . TYR A 1 231 ? -6.316 56.490 42.393 1.00 18.36 ? 272 TYR A CE1 1 ATOM 1820 C CE2 . TYR A 1 231 ? -5.350 56.098 40.188 1.00 19.70 ? 272 TYR A CE2 1 ATOM 1821 C CZ . TYR A 1 231 ? -5.942 56.963 41.125 1.00 18.93 ? 272 TYR A CZ 1 ATOM 1822 O OH . TYR A 1 231 ? -6.137 58.278 40.774 1.00 19.33 ? 272 TYR A OH 1 ATOM 1823 N N . PRO A 1 232 ? -3.894 50.770 44.313 1.00 17.71 ? 273 PRO A N 1 ATOM 1824 C CA . PRO A 1 232 ? -3.505 49.388 44.573 1.00 17.43 ? 273 PRO A CA 1 ATOM 1825 C C . PRO A 1 232 ? -4.236 48.390 43.645 1.00 18.25 ? 273 PRO A C 1 ATOM 1826 O O . PRO A 1 232 ? -5.415 48.561 43.332 1.00 17.98 ? 273 PRO A O 1 ATOM 1827 C CB . PRO A 1 232 ? -3.905 49.168 46.049 1.00 17.63 ? 273 PRO A CB 1 ATOM 1828 C CG . PRO A 1 232 ? -5.103 50.155 46.255 1.00 19.14 ? 273 PRO A CG 1 ATOM 1829 C CD . PRO A 1 232 ? -4.661 51.364 45.431 1.00 18.80 ? 273 PRO A CD 1 ATOM 1830 N N . ALA A 1 233 ? -3.494 47.348 43.260 1.00 17.75 ? 274 ALA A N 1 ATOM 1831 C CA . ALA A 1 233 ? -3.978 46.305 42.344 1.00 18.26 ? 274 ALA A CA 1 ATOM 1832 C C . ALA A 1 233 ? -4.813 45.283 43.137 1.00 20.00 ? 274 ALA A C 1 ATOM 1833 O O . ALA A 1 233 ? -4.471 44.110 43.266 1.00 20.89 ? 274 ALA A O 1 ATOM 1834 C CB . ALA A 1 233 ? -2.732 45.646 41.674 1.00 19.56 ? 274 ALA A CB 1 ATOM 1835 N N . ASN A 1 234 ? -5.908 45.791 43.696 1.00 20.11 ? 275 ASN A N 1 ATOM 1836 C CA . ASN A 1 234 ? -6.811 44.988 44.532 1.00 22.34 ? 275 ASN A CA 1 ATOM 1837 C C . ASN A 1 234 ? -7.830 44.248 43.652 1.00 24.21 ? 275 ASN A C 1 ATOM 1838 O O . ASN A 1 234 ? -7.669 44.191 42.422 1.00 24.03 ? 275 ASN A O 1 ATOM 1839 C CB . ASN A 1 234 ? -7.466 45.889 45.588 1.00 23.91 ? 275 ASN A CB 1 ATOM 1840 C CG . ASN A 1 234 ? -8.292 47.017 44.966 1.00 23.56 ? 275 ASN A CG 1 ATOM 1841 O OD1 . ASN A 1 234 ? -8.795 46.895 43.854 1.00 25.11 ? 275 ASN A OD1 1 ATOM 1842 N ND2 . ASN A 1 234 ? -8.462 48.146 45.721 1.00 26.95 ? 275 ASN A ND2 1 ATOM 1843 N N . GLU A 1 235 ? -8.861 43.652 44.285 1.00 26.06 ? 276 GLU A N 1 ATOM 1844 C CA A GLU A 1 235 ? -9.774 42.793 43.543 0.50 28.15 ? 276 GLU A CA 1 ATOM 1845 C CA B GLU A 1 235 ? -9.881 42.819 43.642 0.50 28.87 ? 276 GLU A CA 1 ATOM 1846 C C . GLU A 1 235 ? -10.619 43.522 42.508 1.00 28.80 ? 276 GLU A C 1 ATOM 1847 O O . GLU A 1 235 ? -10.997 42.910 41.495 1.00 32.25 ? 276 GLU A O 1 ATOM 1848 C CB A GLU A 1 235 ? -10.722 42.018 44.479 0.50 29.80 ? 276 GLU A CB 1 ATOM 1849 C CB B GLU A 1 235 ? -10.963 42.387 44.687 0.50 30.52 ? 276 GLU A CB 1 ATOM 1850 C CG A GLU A 1 235 ? -10.127 40.810 45.061 0.50 31.02 ? 276 GLU A CG 1 ATOM 1851 C CG B GLU A 1 235 ? -11.325 43.510 45.692 0.50 34.26 ? 276 GLU A CG 1 ATOM 1852 C CD A GLU A 1 235 ? -10.072 39.649 44.094 0.50 30.25 ? 276 GLU A CD 1 ATOM 1853 C CD B GLU A 1 235 ? -12.815 43.633 46.088 0.50 37.79 ? 276 GLU A CD 1 ATOM 1854 O OE1 A GLU A 1 235 ? -10.715 39.639 43.009 0.50 34.81 ? 276 GLU A OE1 1 ATOM 1855 O OE1 B GLU A 1 235 ? -13.697 43.092 45.377 0.50 41.56 ? 276 GLU A OE1 1 ATOM 1856 O OE2 A GLU A 1 235 ? -9.400 38.708 44.450 0.50 30.23 ? 276 GLU A OE2 1 ATOM 1857 O OE2 B GLU A 1 235 ? -13.100 44.318 47.122 0.50 39.95 ? 276 GLU A OE2 1 ATOM 1858 N N . TYR A 1 236 ? -10.919 44.799 42.732 1.00 26.44 ? 277 TYR A N 1 ATOM 1859 C CA . TYR A 1 236 ? -11.779 45.522 41.806 1.00 27.85 ? 277 TYR A CA 1 ATOM 1860 C C . TYR A 1 236 ? -11.069 46.544 40.958 1.00 27.52 ? 277 TYR A C 1 ATOM 1861 O O . TYR A 1 236 ? -11.703 47.361 40.271 1.00 28.81 ? 277 TYR A O 1 ATOM 1862 C CB . TYR A 1 236 ? -12.963 46.140 42.555 1.00 27.59 ? 277 TYR A CB 1 ATOM 1863 C CG . TYR A 1 236 ? -12.517 47.093 43.595 1.00 27.11 ? 277 TYR A CG 1 ATOM 1864 C CD1 . TYR A 1 236 ? -12.283 48.441 43.273 1.00 28.24 ? 277 TYR A CD1 1 ATOM 1865 C CD2 . TYR A 1 236 ? -12.286 46.659 44.913 1.00 26.81 ? 277 TYR A CD2 1 ATOM 1866 C CE1 . TYR A 1 236 ? -11.834 49.341 44.251 1.00 29.52 ? 277 TYR A CE1 1 ATOM 1867 C CE2 . TYR A 1 236 ? -11.844 47.556 45.892 1.00 28.76 ? 277 TYR A CE2 1 ATOM 1868 C CZ . TYR A 1 236 ? -11.618 48.888 45.530 1.00 28.85 ? 277 TYR A CZ 1 ATOM 1869 O OH . TYR A 1 236 ? -11.162 49.759 46.493 1.00 33.22 ? 277 TYR A OH 1 ATOM 1870 N N . ALA A 1 237 ? -9.741 46.458 40.933 1.00 26.60 ? 278 ALA A N 1 ATOM 1871 C CA . ALA A 1 237 ? -8.956 47.450 40.244 1.00 27.49 ? 278 ALA A CA 1 ATOM 1872 C C . ALA A 1 237 ? -9.277 47.448 38.760 1.00 28.31 ? 278 ALA A C 1 ATOM 1873 O O . ALA A 1 237 ? -9.554 46.370 38.198 1.00 29.76 ? 278 ALA A O 1 ATOM 1874 C CB . ALA A 1 237 ? -7.471 47.120 40.425 1.00 27.42 ? 278 ALA A CB 1 ATOM 1875 N N . TYR A 1 238 ? -9.322 48.644 38.161 1.00 28.66 ? 279 TYR A N 1 ATOM 1876 C CA . TYR A 1 238 ? -9.396 48.760 36.709 1.00 29.50 ? 279 TYR A CA 1 ATOM 1877 C C . TYR A 1 238 ? -7.945 48.750 36.229 1.00 27.72 ? 279 TYR A C 1 ATOM 1878 O O . TYR A 1 238 ? -7.037 49.355 36.837 1.00 29.89 ? 279 TYR A O 1 ATOM 1879 C CB . TYR A 1 238 ? -10.163 50.040 36.208 1.00 31.92 ? 279 TYR A CB 1 ATOM 1880 C CG A TYR A 1 238 ? -10.558 49.964 34.741 0.50 30.02 ? 279 TYR A CG 1 ATOM 1881 C CG B TYR A 1 238 ? -9.482 50.732 34.978 0.50 33.43 ? 279 TYR A CG 1 ATOM 1882 C CD1 A TYR A 1 238 ? -11.549 49.092 34.300 0.50 33.36 ? 279 TYR A CD1 1 ATOM 1883 C CD1 B TYR A 1 238 ? -10.099 50.764 33.735 0.50 37.01 ? 279 TYR A CD1 1 ATOM 1884 C CD2 A TYR A 1 238 ? -9.902 50.744 33.795 0.50 32.95 ? 279 TYR A CD2 1 ATOM 1885 C CD2 B TYR A 1 238 ? -8.217 51.309 35.080 0.50 35.84 ? 279 TYR A CD2 1 ATOM 1886 C CE1 A TYR A 1 238 ? -11.881 49.006 32.961 0.50 35.59 ? 279 TYR A CE1 1 ATOM 1887 C CE1 B TYR A 1 238 ? -9.478 51.365 32.629 0.50 37.98 ? 279 TYR A CE1 1 ATOM 1888 C CE2 A TYR A 1 238 ? -10.239 50.662 32.450 0.50 32.65 ? 279 TYR A CE2 1 ATOM 1889 C CE2 B TYR A 1 238 ? -7.582 51.901 33.984 0.50 37.66 ? 279 TYR A CE2 1 ATOM 1890 C CZ A TYR A 1 238 ? -11.221 49.802 32.048 0.50 35.16 ? 279 TYR A CZ 1 ATOM 1891 C CZ B TYR A 1 238 ? -8.227 51.936 32.759 0.50 39.09 ? 279 TYR A CZ 1 ATOM 1892 O OH A TYR A 1 238 ? -11.541 49.724 30.717 0.50 38.19 ? 279 TYR A OH 1 ATOM 1893 O OH B TYR A 1 238 ? -7.620 52.542 31.667 0.50 40.56 ? 279 TYR A OH 1 ATOM 1894 N N . ARG A 1 239 ? -7.692 47.941 35.214 1.00 25.62 ? 280 ARG A N 1 ATOM 1895 C CA . ARG A 1 239 ? -6.342 47.811 34.700 1.00 25.10 ? 280 ARG A CA 1 ATOM 1896 C C . ARG A 1 239 ? -6.194 48.457 33.348 1.00 27.13 ? 280 ARG A C 1 ATOM 1897 O O . ARG A 1 239 ? -7.048 48.298 32.478 1.00 26.93 ? 280 ARG A O 1 ATOM 1898 C CB A ARG A 1 239 ? -5.958 46.318 34.593 0.50 25.44 ? 280 ARG A CB 1 ATOM 1899 C CB B ARG A 1 239 ? -5.966 46.346 34.574 0.50 24.77 ? 280 ARG A CB 1 ATOM 1900 C CG A ARG A 1 239 ? -5.271 45.690 35.844 0.50 24.49 ? 280 ARG A CG 1 ATOM 1901 C CG B ARG A 1 239 ? -5.911 45.710 35.914 0.50 22.97 ? 280 ARG A CG 1 ATOM 1902 C CD A ARG A 1 239 ? -6.235 45.368 37.018 0.50 27.38 ? 280 ARG A CD 1 ATOM 1903 C CD B ARG A 1 239 ? -5.332 44.334 35.857 0.50 17.58 ? 280 ARG A CD 1 ATOM 1904 N NE A ARG A 1 239 ? -5.536 44.740 38.163 0.50 25.07 ? 280 ARG A NE 1 ATOM 1905 N NE B ARG A 1 239 ? -5.052 43.902 37.199 0.50 19.74 ? 280 ARG A NE 1 ATOM 1906 C CZ A ARG A 1 239 ? -6.153 44.247 39.232 0.50 25.52 ? 280 ARG A CZ 1 ATOM 1907 C CZ B ARG A 1 239 ? -5.955 43.549 38.088 0.50 18.15 ? 280 ARG A CZ 1 ATOM 1908 N NH1 A ARG A 1 239 ? -7.472 44.265 39.278 0.50 27.86 ? 280 ARG A NH1 1 ATOM 1909 N NH1 B ARG A 1 239 ? -7.274 43.505 37.774 0.50 20.20 ? 280 ARG A NH1 1 ATOM 1910 N NH2 A ARG A 1 239 ? -5.476 43.727 40.252 0.50 20.37 ? 280 ARG A NH2 1 ATOM 1911 N NH2 B ARG A 1 239 ? -5.544 43.199 39.286 0.50 21.63 ? 280 ARG A NH2 1 ATOM 1912 N N . ARG A 1 240 ? -5.054 49.116 33.142 1.00 26.16 ? 281 ARG A N 1 ATOM 1913 C CA . ARG A 1 240 ? -4.700 49.493 31.770 1.00 29.06 ? 281 ARG A CA 1 ATOM 1914 C C . ARG A 1 240 ? -4.597 48.285 30.882 1.00 30.52 ? 281 ARG A C 1 ATOM 1915 O O . ARG A 1 240 ? -4.204 47.184 31.319 1.00 30.34 ? 281 ARG A O 1 ATOM 1916 C CB . ARG A 1 240 ? -3.366 50.198 31.750 1.00 28.30 ? 281 ARG A CB 1 ATOM 1917 C CG . ARG A 1 240 ? -3.448 51.498 32.472 1.00 29.67 ? 281 ARG A CG 1 ATOM 1918 C CD . ARG A 1 240 ? -2.161 52.261 32.324 1.00 30.40 ? 281 ARG A CD 1 ATOM 1919 N NE . ARG A 1 240 ? -2.358 53.604 32.873 1.00 31.58 ? 281 ARG A NE 1 ATOM 1920 C CZ . ARG A 1 240 ? -1.503 54.610 32.715 1.00 35.77 ? 281 ARG A CZ 1 ATOM 1921 N NH1 . ARG A 1 240 ? -0.406 54.429 32.015 1.00 36.11 ? 281 ARG A NH1 1 ATOM 1922 N NH2 . ARG A 1 240 ? -1.741 55.794 33.266 1.00 37.73 ? 281 ARG A NH2 1 ATOM 1923 N N . GLY A 1 241 ? -4.958 48.502 29.617 1.00 33.09 ? 282 GLY A N 1 ATOM 1924 C CA . GLY A 1 241 ? -4.635 47.550 28.575 1.00 35.87 ? 282 GLY A CA 1 ATOM 1925 C C . GLY A 1 241 ? -3.120 47.464 28.468 1.00 37.01 ? 282 GLY A C 1 ATOM 1926 O O . GLY A 1 241 ? -2.408 48.432 28.752 1.00 36.66 ? 282 GLY A O 1 ATOM 1927 N N . ILE A 1 242 ? -2.620 46.296 28.077 1.00 39.24 ? 283 ILE A N 1 ATOM 1928 C CA . ILE A 1 242 ? -1.161 46.096 27.934 1.00 40.30 ? 283 ILE A CA 1 ATOM 1929 C C . ILE A 1 242 ? -0.473 47.166 27.065 1.00 40.57 ? 283 ILE A C 1 ATOM 1930 O O . ILE A 1 242 ? 0.638 47.593 27.390 1.00 40.86 ? 283 ILE A O 1 ATOM 1931 C CB A ILE A 1 242 ? -0.825 44.638 27.470 0.65 40.84 ? 283 ILE A CB 1 ATOM 1932 C CB B ILE A 1 242 ? -0.799 44.672 27.411 0.35 40.69 ? 283 ILE A CB 1 ATOM 1933 C CG1 A ILE A 1 242 ? 0.640 44.285 27.740 0.65 40.92 ? 283 ILE A CG1 1 ATOM 1934 C CG1 B ILE A 1 242 ? -0.938 43.637 28.526 0.35 40.71 ? 283 ILE A CG1 1 ATOM 1935 C CG2 A ILE A 1 242 ? -1.251 44.387 26.011 0.65 41.99 ? 283 ILE A CG2 1 ATOM 1936 C CG2 B ILE A 1 242 ? 0.630 44.622 26.851 0.35 41.06 ? 283 ILE A CG2 1 ATOM 1937 C CD1 A ILE A 1 242 ? 0.931 43.999 29.202 0.65 39.42 ? 283 ILE A CD1 1 ATOM 1938 C CD1 B ILE A 1 242 ? 0.115 43.772 29.630 0.35 39.23 ? 283 ILE A CD1 1 ATOM 1939 N N . ALA A 1 243 ? -1.135 47.631 25.999 1.00 41.55 ? 284 ALA A N 1 ATOM 1940 C CA . ALA A 1 243 ? -0.537 48.669 25.136 1.00 42.30 ? 284 ALA A CA 1 ATOM 1941 C C . ALA A 1 243 ? -0.333 50.011 25.843 1.00 41.92 ? 284 ALA A C 1 ATOM 1942 O O . ALA A 1 243 ? 0.451 50.847 25.390 1.00 42.04 ? 284 ALA A O 1 ATOM 1943 C CB . ALA A 1 243 ? -1.378 48.865 23.851 1.00 43.56 ? 284 ALA A CB 1 ATOM 1944 N N . GLU A 1 244 ? -1.038 50.219 26.958 1.00 40.78 ? 285 GLU A N 1 ATOM 1945 C CA . GLU A 1 244 ? -0.916 51.459 27.731 1.00 40.28 ? 285 GLU A CA 1 ATOM 1946 C C . GLU A 1 244 ? -0.142 51.226 29.038 1.00 38.70 ? 285 GLU A C 1 ATOM 1947 O O . GLU A 1 244 ? 0.014 52.157 29.838 1.00 39.33 ? 285 GLU A O 1 ATOM 1948 C CB . GLU A 1 244 ? -2.304 52.069 28.036 1.00 41.19 ? 285 GLU A CB 1 ATOM 1949 C CG . GLU A 1 244 ? -2.952 52.781 26.846 1.00 45.44 ? 285 GLU A CG 1 ATOM 1950 C CD . GLU A 1 244 ? -3.568 51.818 25.829 1.00 53.44 ? 285 GLU A CD 1 ATOM 1951 O OE1 . GLU A 1 244 ? -4.208 50.806 26.235 1.00 54.77 ? 285 GLU A OE1 1 ATOM 1952 O OE2 . GLU A 1 244 ? -3.409 52.076 24.607 1.00 57.49 ? 285 GLU A OE2 1 ATOM 1953 N N . ALA A 1 245 ? 0.360 50.008 29.238 1.00 37.30 ? 286 ALA A N 1 ATOM 1954 C CA . ALA A 1 245 ? 1.071 49.687 30.485 1.00 36.76 ? 286 ALA A CA 1 ATOM 1955 C C . ALA A 1 245 ? 2.270 50.595 30.668 1.00 36.78 ? 286 ALA A C 1 ATOM 1956 O O . ALA A 1 245 ? 2.856 51.094 29.705 1.00 37.72 ? 286 ALA A O 1 ATOM 1957 C CB . ALA A 1 245 ? 1.494 48.245 30.526 1.00 35.84 ? 286 ALA A CB 1 ATOM 1958 N N . VAL A 1 246 ? 2.626 50.805 31.928 1.00 34.60 ? 287 VAL A N 1 ATOM 1959 C CA . VAL A 1 246 ? 3.750 51.660 32.239 1.00 34.03 ? 287 VAL A CA 1 ATOM 1960 C C . VAL A 1 246 ? 5.044 50.871 32.182 1.00 33.84 ? 287 VAL A C 1 ATOM 1961 O O . VAL A 1 246 ? 5.123 49.778 32.768 1.00 33.82 ? 287 VAL A O 1 ATOM 1962 C CB . VAL A 1 246 ? 3.579 52.257 33.655 1.00 33.51 ? 287 VAL A CB 1 ATOM 1963 C CG1 . VAL A 1 246 ? 4.817 53.044 34.047 1.00 33.15 ? 287 VAL A CG1 1 ATOM 1964 C CG2 . VAL A 1 246 ? 2.288 53.099 33.692 1.00 35.04 ? 287 VAL A CG2 1 ATOM 1965 N N . GLY A 1 247 ? 6.040 51.404 31.468 1.00 33.59 ? 288 GLY A N 1 ATOM 1966 C CA . GLY A 1 247 ? 7.446 50.969 31.636 1.00 31.98 ? 288 GLY A CA 1 ATOM 1967 C C . GLY A 1 247 ? 7.980 49.759 30.882 1.00 31.92 ? 288 GLY A C 1 ATOM 1968 O O . GLY A 1 247 ? 9.134 49.356 31.096 1.00 30.66 ? 288 GLY A O 1 ATOM 1969 N N . LEU A 1 248 ? 7.152 49.188 30.015 1.00 31.04 ? 289 LEU A N 1 ATOM 1970 C CA . LEU A 1 248 ? 7.531 47.963 29.273 1.00 30.68 ? 289 LEU A CA 1 ATOM 1971 C C . LEU A 1 248 ? 8.450 48.260 28.110 1.00 31.29 ? 289 LEU A C 1 ATOM 1972 O O . LEU A 1 248 ? 8.203 49.170 27.329 1.00 32.06 ? 289 LEU A O 1 ATOM 1973 C CB A LEU A 1 248 ? 6.292 47.224 28.728 0.65 30.60 ? 289 LEU A CB 1 ATOM 1974 C CB B LEU A 1 248 ? 6.302 47.181 28.780 0.35 30.88 ? 289 LEU A CB 1 ATOM 1975 C CG A LEU A 1 248 ? 5.186 46.844 29.720 0.65 31.09 ? 289 LEU A CG 1 ATOM 1976 C CG B LEU A 1 248 ? 5.767 46.063 29.685 0.35 31.18 ? 289 LEU A CG 1 ATOM 1977 C CD1 A LEU A 1 248 ? 4.026 46.205 28.995 0.65 32.93 ? 289 LEU A CD1 1 ATOM 1978 C CD1 B LEU A 1 248 ? 5.374 46.589 31.087 0.35 31.81 ? 289 LEU A CD1 1 ATOM 1979 C CD2 A LEU A 1 248 ? 5.752 45.889 30.783 0.65 33.65 ? 289 LEU A CD2 1 ATOM 1980 C CD2 B LEU A 1 248 ? 4.602 45.338 28.993 0.35 31.73 ? 289 LEU A CD2 1 ATOM 1981 N N . PRO A 1 249 ? 9.488 47.442 27.952 1.00 31.61 ? 290 PRO A N 1 ATOM 1982 C CA . PRO A 1 249 ? 10.389 47.630 26.814 1.00 31.84 ? 290 PRO A CA 1 ATOM 1983 C C . PRO A 1 249 ? 9.715 47.267 25.498 1.00 31.94 ? 290 PRO A C 1 ATOM 1984 O O . PRO A 1 249 ? 8.786 46.433 25.479 1.00 32.32 ? 290 PRO A O 1 ATOM 1985 C CB . PRO A 1 249 ? 11.544 46.661 27.110 1.00 32.95 ? 290 PRO A CB 1 ATOM 1986 C CG . PRO A 1 249 ? 10.967 45.638 28.027 1.00 31.78 ? 290 PRO A CG 1 ATOM 1987 C CD . PRO A 1 249 ? 9.894 46.338 28.840 1.00 31.80 ? 290 PRO A CD 1 ATOM 1988 N N . SER A 1 250 ? 10.217 47.820 24.393 1.00 31.80 ? 291 SER A N 1 ATOM 1989 C CA A SER A 1 250 ? 9.603 47.599 23.083 0.50 32.04 ? 291 SER A CA 1 ATOM 1990 C CA B SER A 1 250 ? 9.609 47.602 23.079 0.50 32.28 ? 291 SER A CA 1 ATOM 1991 C C . SER A 1 250 ? 10.410 46.647 22.193 1.00 31.93 ? 291 SER A C 1 ATOM 1992 O O . SER A 1 250 ? 9.995 46.308 21.073 1.00 32.14 ? 291 SER A O 1 ATOM 1993 C CB A SER A 1 250 ? 9.383 48.935 22.367 0.50 33.74 ? 291 SER A CB 1 ATOM 1994 C CB B SER A 1 250 ? 9.428 48.938 22.362 0.50 34.00 ? 291 SER A CB 1 ATOM 1995 O OG A SER A 1 250 ? 10.618 49.561 22.066 0.50 34.41 ? 291 SER A OG 1 ATOM 1996 O OG B SER A 1 250 ? 8.943 49.916 23.257 0.50 35.27 ? 291 SER A OG 1 ATOM 1997 N N . ILE A 1 251 ? 11.580 46.233 22.676 1.00 29.74 ? 292 ILE A N 1 ATOM 1998 C CA . ILE A 1 251 ? 12.441 45.317 21.897 1.00 28.75 ? 292 ILE A CA 1 ATOM 1999 C C . ILE A 1 251 ? 12.826 44.132 22.769 1.00 27.32 ? 292 ILE A C 1 ATOM 2000 O O . ILE A 1 251 ? 12.888 44.276 23.973 1.00 26.36 ? 292 ILE A O 1 ATOM 2001 C CB . ILE A 1 251 ? 13.729 46.020 21.357 1.00 29.19 ? 292 ILE A CB 1 ATOM 2002 C CG1 . ILE A 1 251 ? 14.514 46.673 22.490 1.00 27.78 ? 292 ILE A CG1 1 ATOM 2003 C CG2 . ILE A 1 251 ? 13.355 47.039 20.288 1.00 32.12 ? 292 ILE A CG2 1 ATOM 2004 C CD1 . ILE A 1 251 ? 15.835 47.387 22.014 1.00 30.61 ? 292 ILE A CD1 1 ATOM 2005 N N . PRO A 1 252 ? 13.024 42.948 22.178 1.00 27.44 ? 293 PRO A N 1 ATOM 2006 C CA . PRO A 1 252 ? 13.403 41.770 22.977 1.00 26.10 ? 293 PRO A CA 1 ATOM 2007 C C . PRO A 1 252 ? 14.795 41.876 23.618 1.00 25.68 ? 293 PRO A C 1 ATOM 2008 O O . PRO A 1 252 ? 15.708 42.482 23.038 1.00 25.51 ? 293 PRO A O 1 ATOM 2009 C CB . PRO A 1 252 ? 13.421 40.637 21.938 1.00 27.19 ? 293 PRO A CB 1 ATOM 2010 C CG . PRO A 1 252 ? 12.501 41.156 20.829 1.00 30.24 ? 293 PRO A CG 1 ATOM 2011 C CD . PRO A 1 252 ? 12.796 42.601 20.754 1.00 27.92 ? 293 PRO A CD 1 ATOM 2012 N N . VAL A 1 253 ? 14.936 41.283 24.814 1.00 23.51 ? 294 VAL A N 1 ATOM 2013 C CA . VAL A 1 253 ? 16.175 41.354 25.568 1.00 22.98 ? 294 VAL A CA 1 ATOM 2014 C C . VAL A 1 253 ? 16.444 40.000 26.218 1.00 22.04 ? 294 VAL A C 1 ATOM 2015 O O . VAL A 1 253 ? 15.510 39.327 26.637 1.00 23.26 ? 294 VAL A O 1 ATOM 2016 C CB . VAL A 1 253 ? 15.983 42.384 26.706 1.00 22.86 ? 294 VAL A CB 1 ATOM 2017 C CG1 . VAL A 1 253 ? 17.289 42.495 27.520 1.00 22.39 ? 294 VAL A CG1 1 ATOM 2018 C CG2 . VAL A 1 253 ? 15.586 43.767 26.125 1.00 23.90 ? 294 VAL A CG2 1 ATOM 2019 N N . HIS A 1 254 ? 17.712 39.573 26.271 1.00 23.07 ? 295 HIS A N 1 ATOM 2020 C CA . HIS A 1 254 ? 18.017 38.306 26.919 1.00 21.97 ? 295 HIS A CA 1 ATOM 2021 C C . HIS A 1 254 ? 19.440 38.358 27.479 1.00 22.90 ? 295 HIS A C 1 ATOM 2022 O O . HIS A 1 254 ? 20.330 38.941 26.841 1.00 24.22 ? 295 HIS A O 1 ATOM 2023 C CB . HIS A 1 254 ? 17.913 37.164 25.858 1.00 23.68 ? 295 HIS A CB 1 ATOM 2024 C CG . HIS A 1 254 ? 17.933 35.783 26.440 1.00 23.54 ? 295 HIS A CG 1 ATOM 2025 N ND1 . HIS A 1 254 ? 16.916 35.294 27.234 1.00 24.44 ? 295 HIS A ND1 1 ATOM 2026 C CD2 . HIS A 1 254 ? 18.843 34.777 26.321 1.00 24.33 ? 295 HIS A CD2 1 ATOM 2027 C CE1 . HIS A 1 254 ? 17.208 34.055 27.600 1.00 25.76 ? 295 HIS A CE1 1 ATOM 2028 N NE2 . HIS A 1 254 ? 18.365 33.713 27.055 1.00 25.58 ? 295 HIS A NE2 1 ATOM 2029 N N . PRO A 1 255 ? 19.671 37.749 28.656 1.00 21.74 ? 296 PRO A N 1 ATOM 2030 C CA . PRO A 1 255 ? 20.990 37.747 29.283 1.00 21.21 ? 296 PRO A CA 1 ATOM 2031 C C . PRO A 1 255 ? 21.697 36.403 29.066 1.00 22.81 ? 296 PRO A C 1 ATOM 2032 O O . PRO A 1 255 ? 21.041 35.336 29.008 1.00 23.62 ? 296 PRO A O 1 ATOM 2033 C CB . PRO A 1 255 ? 20.662 37.932 30.780 1.00 21.34 ? 296 PRO A CB 1 ATOM 2034 C CG . PRO A 1 255 ? 19.316 37.138 30.944 1.00 22.12 ? 296 PRO A CG 1 ATOM 2035 C CD . PRO A 1 255 ? 18.631 37.199 29.557 1.00 21.00 ? 296 PRO A CD 1 ATOM 2036 N N . ILE A 1 256 ? 23.022 36.469 28.964 1.00 23.17 ? 297 ILE A N 1 ATOM 2037 C CA . ILE A 1 256 ? 23.873 35.279 28.744 1.00 22.82 ? 297 ILE A CA 1 ATOM 2038 C C . ILE A 1 256 ? 25.161 35.371 29.577 1.00 23.91 ? 297 ILE A C 1 ATOM 2039 O O . ILE A 1 256 ? 25.502 36.458 30.114 1.00 23.62 ? 297 ILE A O 1 ATOM 2040 C CB . ILE A 1 256 ? 24.258 35.081 27.237 1.00 24.34 ? 297 ILE A CB 1 ATOM 2041 C CG1 . ILE A 1 256 ? 25.130 36.250 26.722 1.00 25.02 ? 297 ILE A CG1 1 ATOM 2042 C CG2 . ILE A 1 256 ? 23.006 34.884 26.388 1.00 24.73 ? 297 ILE A CG2 1 ATOM 2043 C CD1 . ILE A 1 256 ? 25.585 36.085 25.278 1.00 26.07 ? 297 ILE A CD1 1 ATOM 2044 N N . GLY A 1 257 ? 25.843 34.225 29.681 1.00 23.20 ? 298 GLY A N 1 ATOM 2045 C CA . GLY A 1 257 ? 27.055 34.108 30.462 1.00 24.82 ? 298 GLY A CA 1 ATOM 2046 C C . GLY A 1 257 ? 28.249 34.381 29.556 1.00 25.78 ? 298 GLY A C 1 ATOM 2047 O O . GLY A 1 257 ? 28.080 34.624 28.354 1.00 26.58 ? 298 GLY A O 1 ATOM 2048 N N . TYR A 1 258 ? 29.450 34.418 30.120 1.00 26.03 ? 299 TYR A N 1 ATOM 2049 C CA . TYR A 1 258 ? 30.586 34.807 29.285 1.00 27.34 ? 299 TYR A CA 1 ATOM 2050 C C . TYR A 1 258 ? 31.135 33.710 28.353 1.00 28.83 ? 299 TYR A C 1 ATOM 2051 O O . TYR A 1 258 ? 31.825 34.028 27.378 1.00 31.02 ? 299 TYR A O 1 ATOM 2052 C CB . TYR A 1 258 ? 31.724 35.483 30.068 1.00 27.54 ? 299 TYR A CB 1 ATOM 2053 C CG . TYR A 1 258 ? 32.311 34.729 31.244 1.00 26.59 ? 299 TYR A CG 1 ATOM 2054 C CD1 . TYR A 1 258 ? 31.881 34.992 32.553 1.00 26.43 ? 299 TYR A CD1 1 ATOM 2055 C CD2 . TYR A 1 258 ? 33.354 33.811 31.066 1.00 29.06 ? 299 TYR A CD2 1 ATOM 2056 C CE1 . TYR A 1 258 ? 32.422 34.324 33.650 1.00 28.19 ? 299 TYR A CE1 1 ATOM 2057 C CE2 . TYR A 1 258 ? 33.923 33.159 32.170 1.00 28.80 ? 299 TYR A CE2 1 ATOM 2058 C CZ . TYR A 1 258 ? 33.453 33.429 33.457 1.00 28.01 ? 299 TYR A CZ 1 ATOM 2059 O OH . TYR A 1 258 ? 34.013 32.759 34.525 1.00 30.24 ? 299 TYR A OH 1 ATOM 2060 N N . TYR A 1 259 ? 30.832 32.439 28.620 1.00 28.44 ? 300 TYR A N 1 ATOM 2061 C CA . TYR A 1 259 ? 31.173 31.414 27.610 1.00 29.55 ? 300 TYR A CA 1 ATOM 2062 C C . TYR A 1 259 ? 30.400 31.679 26.321 1.00 30.13 ? 300 TYR A C 1 ATOM 2063 O O . TYR A 1 259 ? 30.981 31.693 25.228 1.00 31.77 ? 300 TYR A O 1 ATOM 2064 C CB . TYR A 1 259 ? 30.875 29.996 28.098 1.00 29.36 ? 300 TYR A CB 1 ATOM 2065 C CG . TYR A 1 259 ? 31.784 29.459 29.170 1.00 29.69 ? 300 TYR A CG 1 ATOM 2066 C CD1 . TYR A 1 259 ? 33.099 29.954 29.339 1.00 32.85 ? 300 TYR A CD1 1 ATOM 2067 C CD2 . TYR A 1 259 ? 31.366 28.402 29.987 1.00 31.03 ? 300 TYR A CD2 1 ATOM 2068 C CE1 . TYR A 1 259 ? 33.930 29.430 30.307 1.00 34.80 ? 300 TYR A CE1 1 ATOM 2069 C CE2 . TYR A 1 259 ? 32.228 27.846 30.954 1.00 33.13 ? 300 TYR A CE2 1 ATOM 2070 C CZ . TYR A 1 259 ? 33.493 28.362 31.104 1.00 36.25 ? 300 TYR A CZ 1 ATOM 2071 O OH . TYR A 1 259 ? 34.344 27.806 32.051 1.00 36.83 ? 300 TYR A OH 1 ATOM 2072 N N . ASP A 1 260 ? 29.097 31.938 26.460 1.00 28.63 ? 301 ASP A N 1 ATOM 2073 C CA . ASP A 1 260 ? 28.266 32.256 25.307 1.00 29.84 ? 301 ASP A CA 1 ATOM 2074 C C . ASP A 1 260 ? 28.611 33.608 24.678 1.00 30.15 ? 301 ASP A C 1 ATOM 2075 O O . ASP A 1 260 ? 28.635 33.738 23.457 1.00 31.66 ? 301 ASP A O 1 ATOM 2076 C CB . ASP A 1 260 ? 26.783 32.226 25.688 1.00 28.77 ? 301 ASP A CB 1 ATOM 2077 C CG . ASP A 1 260 ? 26.230 30.796 25.805 1.00 29.41 ? 301 ASP A CG 1 ATOM 2078 O OD1 . ASP A 1 260 ? 26.846 29.855 25.264 1.00 34.50 ? 301 ASP A OD1 1 ATOM 2079 O OD2 . ASP A 1 260 ? 25.170 30.622 26.454 1.00 29.95 ? 301 ASP A OD2 1 ATOM 2080 N N . ALA A 1 261 ? 28.874 34.617 25.509 1.00 29.11 ? 302 ALA A N 1 ATOM 2081 C CA . ALA A 1 261 ? 29.278 35.927 24.981 1.00 29.43 ? 302 ALA A CA 1 ATOM 2082 C C . ALA A 1 261 ? 30.521 35.874 24.113 1.00 31.49 ? 302 ALA A C 1 ATOM 2083 O O . ALA A 1 261 ? 30.594 36.540 23.084 1.00 31.79 ? 302 ALA A O 1 ATOM 2084 C CB . ALA A 1 261 ? 29.474 36.930 26.122 1.00 29.54 ? 302 ALA A CB 1 ATOM 2085 N N . GLN A 1 262 ? 31.507 35.109 24.561 1.00 30.29 ? 303 GLN A N 1 ATOM 2086 C CA . GLN A 1 262 ? 32.748 34.931 23.822 1.00 32.68 ? 303 GLN A CA 1 ATOM 2087 C C . GLN A 1 262 ? 32.439 34.479 22.385 1.00 33.28 ? 303 GLN A C 1 ATOM 2088 O O . GLN A 1 262 ? 33.042 34.965 21.424 1.00 34.06 ? 303 GLN A O 1 ATOM 2089 C CB . GLN A 1 262 ? 33.548 33.842 24.514 1.00 32.93 ? 303 GLN A CB 1 ATOM 2090 C CG . GLN A 1 262 ? 34.831 33.480 23.823 1.00 40.55 ? 303 GLN A CG 1 ATOM 2091 C CD . GLN A 1 262 ? 35.946 34.177 24.506 1.00 45.45 ? 303 GLN A CD 1 ATOM 2092 O OE1 . GLN A 1 262 ? 36.450 35.183 24.011 1.00 52.97 ? 303 GLN A OE1 1 ATOM 2093 N NE2 . GLN A 1 262 ? 36.297 33.703 25.697 1.00 44.24 ? 303 GLN A NE2 1 ATOM 2094 N N . LYS A 1 263 ? 31.480 33.570 22.246 1.00 33.77 ? 304 LYS A N 1 ATOM 2095 C CA A LYS A 1 263 ? 31.146 33.013 20.936 0.50 34.67 ? 304 LYS A CA 1 ATOM 2096 C CA B LYS A 1 263 ? 31.150 33.017 20.933 0.50 34.60 ? 304 LYS A CA 1 ATOM 2097 C C . LYS A 1 263 ? 30.480 34.066 20.049 1.00 34.98 ? 304 LYS A C 1 ATOM 2098 O O . LYS A 1 263 ? 30.696 34.089 18.841 1.00 36.75 ? 304 LYS A O 1 ATOM 2099 C CB A LYS A 1 263 ? 30.271 31.772 21.087 0.50 34.61 ? 304 LYS A CB 1 ATOM 2100 C CB B LYS A 1 263 ? 30.291 31.764 21.072 0.50 34.45 ? 304 LYS A CB 1 ATOM 2101 C CG A LYS A 1 263 ? 30.915 30.638 21.891 0.50 35.95 ? 304 LYS A CG 1 ATOM 2102 C CG B LYS A 1 263 ? 31.031 30.579 21.685 0.50 35.73 ? 304 LYS A CG 1 ATOM 2103 C CD A LYS A 1 263 ? 31.939 29.869 21.058 0.50 40.44 ? 304 LYS A CD 1 ATOM 2104 C CD B LYS A 1 263 ? 32.058 30.003 20.704 0.50 38.95 ? 304 LYS A CD 1 ATOM 2105 C CE A LYS A 1 263 ? 31.420 29.649 19.650 0.50 41.60 ? 304 LYS A CE 1 ATOM 2106 C CE B LYS A 1 263 ? 32.972 28.992 21.380 0.50 39.65 ? 304 LYS A CE 1 ATOM 2107 N NZ A LYS A 1 263 ? 32.127 28.550 18.948 0.50 45.19 ? 304 LYS A NZ 1 ATOM 2108 N NZ B LYS A 1 263 ? 33.926 28.406 20.389 0.50 42.66 ? 304 LYS A NZ 1 ATOM 2109 N N . LEU A 1 264 ? 29.680 34.949 20.659 1.00 33.28 ? 305 LEU A N 1 ATOM 2110 C CA . LEU A 1 264 ? 29.061 36.051 19.921 1.00 34.46 ? 305 LEU A CA 1 ATOM 2111 C C . LEU A 1 264 ? 30.033 37.192 19.587 1.00 35.54 ? 305 LEU A C 1 ATOM 2112 O O . LEU A 1 264 ? 29.897 37.822 18.531 1.00 37.65 ? 305 LEU A O 1 ATOM 2113 C CB . LEU A 1 264 ? 27.827 36.606 20.663 1.00 32.12 ? 305 LEU A CB 1 ATOM 2114 C CG . LEU A 1 264 ? 26.671 35.625 20.900 1.00 33.20 ? 305 LEU A CG 1 ATOM 2115 C CD1 . LEU A 1 264 ? 25.557 36.262 21.717 1.00 32.83 ? 305 LEU A CD1 1 ATOM 2116 C CD2 . LEU A 1 264 ? 26.088 35.106 19.600 1.00 32.66 ? 305 LEU A CD2 1 ATOM 2117 N N . LEU A 1 265 ? 31.004 37.457 20.464 1.00 34.23 ? 306 LEU A N 1 ATOM 2118 C CA . LEU A 1 265 ? 31.902 38.601 20.294 1.00 34.09 ? 306 LEU A CA 1 ATOM 2119 C C . LEU A 1 265 ? 33.131 38.275 19.470 1.00 35.29 ? 306 LEU A C 1 ATOM 2120 O O . LEU A 1 265 ? 33.744 39.176 18.892 1.00 35.86 ? 306 LEU A O 1 ATOM 2121 C CB . LEU A 1 265 ? 32.374 39.093 21.635 1.00 32.56 ? 306 LEU A CB 1 ATOM 2122 C CG . LEU A 1 265 ? 31.260 39.640 22.559 1.00 32.81 ? 306 LEU A CG 1 ATOM 2123 C CD1 . LEU A 1 265 ? 31.832 39.845 23.932 1.00 34.35 ? 306 LEU A CD1 1 ATOM 2124 C CD2 . LEU A 1 265 ? 30.695 40.946 22.030 1.00 33.91 ? 306 LEU A CD2 1 ATOM 2125 N N . GLU A 1 266 ? 33.520 37.006 19.454 1.00 35.87 ? 307 GLU A N 1 ATOM 2126 C CA . GLU A 1 266 ? 34.823 36.660 18.819 1.00 37.43 ? 307 GLU A CA 1 ATOM 2127 C C . GLU A 1 266 ? 34.910 36.976 17.320 1.00 39.51 ? 307 GLU A C 1 ATOM 2128 O O . GLU A 1 266 ? 36.006 37.245 16.802 1.00 39.76 ? 307 GLU A O 1 ATOM 2129 C CB . GLU A 1 266 ? 35.206 35.212 19.098 1.00 37.91 ? 307 GLU A CB 1 ATOM 2130 C CG . GLU A 1 266 ? 34.333 34.208 18.408 1.00 40.29 ? 307 GLU A CG 1 ATOM 2131 C CD . GLU A 1 266 ? 34.607 32.787 18.860 1.00 46.42 ? 307 GLU A CD 1 ATOM 2132 O OE1 . GLU A 1 266 ? 35.489 32.593 19.739 1.00 50.80 ? 307 GLU A OE1 1 ATOM 2133 O OE2 . GLU A 1 266 ? 33.946 31.865 18.314 1.00 47.29 ? 307 GLU A OE2 1 ATOM 2134 N N . LYS A 1 267 ? 33.773 36.924 16.629 1.00 39.90 ? 308 LYS A N 1 ATOM 2135 C CA . LYS A 1 267 ? 33.738 37.181 15.191 1.00 41.44 ? 308 LYS A CA 1 ATOM 2136 C C . LYS A 1 267 ? 33.456 38.638 14.838 1.00 41.42 ? 308 LYS A C 1 ATOM 2137 O O . LYS A 1 267 ? 33.405 38.971 13.656 1.00 42.42 ? 308 LYS A O 1 ATOM 2138 C CB . LYS A 1 267 ? 32.672 36.305 14.527 1.00 42.22 ? 308 LYS A CB 1 ATOM 2139 C CG . LYS A 1 267 ? 33.031 34.837 14.391 1.00 45.03 ? 308 LYS A CG 1 ATOM 2140 C CD . LYS A 1 267 ? 31.798 34.004 14.041 1.00 46.44 ? 308 LYS A CD 1 ATOM 2141 C CE . LYS A 1 267 ? 32.193 32.560 13.720 1.00 50.63 ? 308 LYS A CE 1 ATOM 2142 N NZ . LYS A 1 267 ? 30.984 31.735 13.415 1.00 52.03 ? 308 LYS A NZ 1 ATOM 2143 N N . MET A 1 268 ? 33.291 39.505 15.843 1.00 39.72 ? 309 MET A N 1 ATOM 2144 C CA . MET A 1 268 ? 32.966 40.921 15.580 1.00 40.27 ? 309 MET A CA 1 ATOM 2145 C C . MET A 1 268 ? 34.017 41.705 14.784 1.00 41.68 ? 309 MET A C 1 ATOM 2146 O O . MET A 1 268 ? 35.226 41.599 15.033 1.00 41.54 ? 309 MET A O 1 ATOM 2147 C CB . MET A 1 268 ? 32.570 41.645 16.857 1.00 39.13 ? 309 MET A CB 1 ATOM 2148 C CG A MET A 1 268 ? 31.122 41.238 17.165 0.50 38.40 ? 309 MET A CG 1 ATOM 2149 C CG B MET A 1 268 ? 31.346 41.134 17.553 0.50 41.13 ? 309 MET A CG 1 ATOM 2150 S SD A MET A 1 268 ? 30.263 42.108 18.459 0.50 34.86 ? 309 MET A SD 1 ATOM 2151 S SD B MET A 1 268 ? 29.917 41.864 16.800 0.50 44.23 ? 309 MET A SD 1 ATOM 2152 C CE A MET A 1 268 ? 30.084 43.728 17.710 0.50 37.59 ? 309 MET A CE 1 ATOM 2153 C CE B MET A 1 268 ? 30.227 43.619 17.030 0.50 42.91 ? 309 MET A CE 1 ATOM 2154 N N . GLY A 1 269 ? 33.526 42.471 13.813 1.00 42.25 ? 310 GLY A N 1 ATOM 2155 C CA . GLY A 1 269 ? 34.384 43.262 12.932 1.00 44.12 ? 310 GLY A CA 1 ATOM 2156 C C . GLY A 1 269 ? 34.053 44.740 13.004 1.00 44.50 ? 310 GLY A C 1 ATOM 2157 O O . GLY A 1 269 ? 33.765 45.262 14.091 1.00 43.39 ? 310 GLY A O 1 ATOM 2158 N N . GLY A 1 270 ? 34.087 45.422 11.854 1.00 45.66 ? 311 GLY A N 1 ATOM 2159 C CA . GLY A 1 270 ? 33.843 46.867 11.844 1.00 46.02 ? 311 GLY A CA 1 ATOM 2160 C C . GLY A 1 270 ? 34.944 47.584 12.614 1.00 46.20 ? 311 GLY A C 1 ATOM 2161 O O . GLY A 1 270 ? 36.114 47.202 12.529 1.00 46.70 ? 311 GLY A O 1 ATOM 2162 N N . SER A 1 271 ? 34.567 48.602 13.381 1.00 45.08 ? 312 SER A N 1 ATOM 2163 C CA . SER A 1 271 ? 35.515 49.485 14.065 1.00 45.52 ? 312 SER A CA 1 ATOM 2164 C C . SER A 1 271 ? 36.142 48.878 15.329 1.00 45.06 ? 312 SER A C 1 ATOM 2165 O O . SER A 1 271 ? 35.475 48.156 16.079 1.00 44.14 ? 312 SER A O 1 ATOM 2166 C CB . SER A 1 271 ? 34.802 50.797 14.425 1.00 45.39 ? 312 SER A CB 1 ATOM 2167 O OG A SER A 1 271 ? 35.725 51.772 14.880 0.50 46.69 ? 312 SER A OG 1 ATOM 2168 O OG B SER A 1 271 ? 34.267 51.428 13.264 0.50 44.96 ? 312 SER A OG 1 ATOM 2169 N N . ALA A 1 272 ? 37.422 49.169 15.563 1.00 45.39 ? 313 ALA A N 1 ATOM 2170 C CA . ALA A 1 272 ? 38.084 48.804 16.823 1.00 44.61 ? 313 ALA A CA 1 ATOM 2171 C C . ALA A 1 272 ? 37.411 49.519 18.023 1.00 43.53 ? 313 ALA A C 1 ATOM 2172 O O . ALA A 1 272 ? 36.745 50.537 17.826 1.00 43.25 ? 313 ALA A O 1 ATOM 2173 C CB . ALA A 1 272 ? 39.586 49.146 16.736 1.00 45.94 ? 313 ALA A CB 1 ATOM 2174 N N . PRO A 1 273 ? 37.560 48.981 19.262 1.00 42.30 ? 314 PRO A N 1 ATOM 2175 C CA . PRO A 1 273 ? 37.033 49.700 20.436 1.00 41.88 ? 314 PRO A CA 1 ATOM 2176 C C . PRO A 1 273 ? 37.738 51.057 20.508 1.00 42.67 ? 314 PRO A C 1 ATOM 2177 O O . PRO A 1 273 ? 38.929 51.137 20.134 1.00 42.87 ? 314 PRO A O 1 ATOM 2178 C CB . PRO A 1 273 ? 37.440 48.804 21.612 1.00 40.85 ? 314 PRO A CB 1 ATOM 2179 C CG . PRO A 1 273 ? 38.614 47.995 21.084 1.00 41.78 ? 314 PRO A CG 1 ATOM 2180 C CD . PRO A 1 273 ? 38.309 47.766 19.643 1.00 42.63 ? 314 PRO A CD 1 ATOM 2181 N N . PRO A 1 274 ? 37.026 52.118 20.928 1.00 42.35 ? 315 PRO A N 1 ATOM 2182 C CA . PRO A 1 274 ? 37.630 53.454 20.843 1.00 43.70 ? 315 PRO A CA 1 ATOM 2183 C C . PRO A 1 274 ? 38.779 53.673 21.827 1.00 44.80 ? 315 PRO A C 1 ATOM 2184 O O . PRO A 1 274 ? 39.645 54.520 21.598 1.00 45.57 ? 315 PRO A O 1 ATOM 2185 C CB . PRO A 1 274 ? 36.444 54.391 21.116 1.00 42.67 ? 315 PRO A CB 1 ATOM 2186 C CG . PRO A 1 274 ? 35.464 53.538 21.918 1.00 41.36 ? 315 PRO A CG 1 ATOM 2187 C CD . PRO A 1 274 ? 35.586 52.191 21.253 1.00 40.79 ? 315 PRO A CD 1 ATOM 2188 N N . ASP A 1 275 ? 38.801 52.899 22.903 1.00 44.57 ? 316 ASP A N 1 ATOM 2189 C CA . ASP A 1 275 ? 39.859 52.995 23.911 1.00 45.27 ? 316 ASP A CA 1 ATOM 2190 C C . ASP A 1 275 ? 39.726 51.814 24.859 1.00 44.62 ? 316 ASP A C 1 ATOM 2191 O O . ASP A 1 275 ? 38.776 51.024 24.733 1.00 43.57 ? 316 ASP A O 1 ATOM 2192 C CB . ASP A 1 275 ? 39.814 54.345 24.661 1.00 45.56 ? 316 ASP A CB 1 ATOM 2193 C CG . ASP A 1 275 ? 38.553 54.525 25.485 1.00 46.54 ? 316 ASP A CG 1 ATOM 2194 O OD1 . ASP A 1 275 ? 38.379 53.760 26.450 1.00 49.76 ? 316 ASP A OD1 1 ATOM 2195 O OD2 . ASP A 1 275 ? 37.743 55.439 25.197 1.00 48.57 ? 316 ASP A OD2 1 ATOM 2196 N N . SER A 1 276 ? 40.648 51.706 25.811 1.00 44.65 ? 317 SER A N 1 ATOM 2197 C CA . SER A 1 276 ? 40.732 50.528 26.673 1.00 45.35 ? 317 SER A CA 1 ATOM 2198 C C . SER A 1 276 ? 39.555 50.374 27.659 1.00 43.35 ? 317 SER A C 1 ATOM 2199 O O . SER A 1 276 ? 39.308 49.261 28.146 1.00 44.06 ? 317 SER A O 1 ATOM 2200 C CB . SER A 1 276 ? 42.065 50.521 27.431 1.00 46.41 ? 317 SER A CB 1 ATOM 2201 O OG . SER A 1 276 ? 42.050 51.542 28.415 1.00 49.03 ? 317 SER A OG 1 ATOM 2202 N N . SER A 1 277 ? 38.840 51.464 27.963 1.00 41.72 ? 318 SER A N 1 ATOM 2203 C CA . SER A 1 277 ? 37.684 51.408 28.884 1.00 39.10 ? 318 SER A CA 1 ATOM 2204 C C . SER A 1 277 ? 36.512 50.648 28.258 1.00 37.61 ? 318 SER A C 1 ATOM 2205 O O . SER A 1 277 ? 35.506 50.381 28.933 1.00 37.17 ? 318 SER A O 1 ATOM 2206 C CB . SER A 1 277 ? 37.216 52.808 29.309 1.00 39.49 ? 318 SER A CB 1 ATOM 2207 O OG . SER A 1 277 ? 36.546 53.477 28.238 1.00 39.45 ? 318 SER A OG 1 ATOM 2208 N N . TRP A 1 278 ? 36.637 50.336 26.966 1.00 36.14 ? 319 TRP A N 1 ATOM 2209 C CA . TRP A 1 278 ? 35.634 49.546 26.238 1.00 34.89 ? 319 TRP A CA 1 ATOM 2210 C C . TRP A 1 278 ? 35.996 48.061 26.197 1.00 34.68 ? 319 TRP A C 1 ATOM 2211 O O . TRP A 1 278 ? 35.176 47.241 25.815 1.00 33.75 ? 319 TRP A O 1 ATOM 2212 C CB . TRP A 1 278 ? 35.455 50.071 24.806 1.00 35.56 ? 319 TRP A CB 1 ATOM 2213 C CG . TRP A 1 278 ? 34.542 51.242 24.762 1.00 33.79 ? 319 TRP A CG 1 ATOM 2214 C CD1 . TRP A 1 278 ? 34.687 52.430 25.442 1.00 34.52 ? 319 TRP A CD1 1 ATOM 2215 C CD2 . TRP A 1 278 ? 33.330 51.350 24.014 1.00 31.72 ? 319 TRP A CD2 1 ATOM 2216 N NE1 . TRP A 1 278 ? 33.625 53.262 25.171 1.00 34.04 ? 319 TRP A NE1 1 ATOM 2217 C CE2 . TRP A 1 278 ? 32.779 52.635 24.293 1.00 33.87 ? 319 TRP A CE2 1 ATOM 2218 C CE3 . TRP A 1 278 ? 32.643 50.485 23.146 1.00 31.92 ? 319 TRP A CE3 1 ATOM 2219 C CZ2 . TRP A 1 278 ? 31.556 53.072 23.741 1.00 33.23 ? 319 TRP A CZ2 1 ATOM 2220 C CZ3 . TRP A 1 278 ? 31.431 50.917 22.589 1.00 32.23 ? 319 TRP A CZ3 1 ATOM 2221 C CH2 . TRP A 1 278 ? 30.899 52.204 22.903 1.00 32.44 ? 319 TRP A CH2 1 ATOM 2222 N N . ARG A 1 279 ? 37.234 47.719 26.559 1.00 35.10 ? 320 ARG A N 1 ATOM 2223 C CA . ARG A 1 279 ? 37.650 46.316 26.550 1.00 35.85 ? 320 ARG A CA 1 ATOM 2224 C C . ARG A 1 279 ? 37.470 45.635 27.906 1.00 34.82 ? 320 ARG A C 1 ATOM 2225 O O . ARG A 1 279 ? 37.944 46.135 28.927 1.00 35.10 ? 320 ARG A O 1 ATOM 2226 C CB . ARG A 1 279 ? 39.104 46.193 26.090 1.00 36.44 ? 320 ARG A CB 1 ATOM 2227 C CG . ARG A 1 279 ? 39.249 46.313 24.590 1.00 42.38 ? 320 ARG A CG 1 ATOM 2228 C CD . ARG A 1 279 ? 40.674 46.025 24.127 1.00 50.02 ? 320 ARG A CD 1 ATOM 2229 N NE . ARG A 1 279 ? 41.357 47.275 23.821 1.00 59.74 ? 320 ARG A NE 1 ATOM 2230 C CZ . ARG A 1 279 ? 42.243 47.873 24.616 1.00 62.50 ? 320 ARG A CZ 1 ATOM 2231 N NH1 . ARG A 1 279 ? 42.579 47.329 25.785 1.00 63.60 ? 320 ARG A NH1 1 ATOM 2232 N NH2 . ARG A 1 279 ? 42.794 49.018 24.238 1.00 63.35 ? 320 ARG A NH2 1 ATOM 2233 N N . GLY A 1 280 ? 36.766 44.505 27.905 1.00 34.36 ? 321 GLY A N 1 ATOM 2234 C CA . GLY A 1 280 ? 36.688 43.600 29.054 1.00 33.30 ? 321 GLY A CA 1 ATOM 2235 C C . GLY A 1 280 ? 37.866 42.641 29.087 1.00 34.18 ? 321 GLY A C 1 ATOM 2236 O O . GLY A 1 280 ? 38.941 42.952 28.523 1.00 35.07 ? 321 GLY A O 1 ATOM 2237 N N . SER A 1 281 ? 37.681 41.491 29.741 1.00 33.37 ? 322 SER A N 1 ATOM 2238 C CA . SER A 1 281 ? 38.778 40.544 30.025 1.00 36.22 ? 322 SER A CA 1 ATOM 2239 C C . SER A 1 281 ? 38.745 39.283 29.163 1.00 35.93 ? 322 SER A C 1 ATOM 2240 O O . SER A 1 281 ? 39.606 38.416 29.314 1.00 37.38 ? 322 SER A O 1 ATOM 2241 C CB . SER A 1 281 ? 38.779 40.158 31.514 1.00 36.82 ? 322 SER A CB 1 ATOM 2242 O OG . SER A 1 281 ? 39.058 41.291 32.323 1.00 39.58 ? 322 SER A OG 1 ATOM 2243 N N . LEU A 1 282 ? 37.763 39.165 28.271 1.00 34.57 ? 323 LEU A N 1 ATOM 2244 C CA . LEU A 1 282 ? 37.724 38.021 27.351 1.00 34.42 ? 323 LEU A CA 1 ATOM 2245 C C . LEU A 1 282 ? 38.797 38.152 26.275 1.00 36.69 ? 323 LEU A C 1 ATOM 2246 O O . LEU A 1 282 ? 39.238 39.261 25.943 1.00 36.45 ? 323 LEU A O 1 ATOM 2247 C CB . LEU A 1 282 ? 36.358 37.913 26.665 1.00 33.59 ? 323 LEU A CB 1 ATOM 2248 C CG . LEU A 1 282 ? 35.155 37.640 27.585 1.00 33.47 ? 323 LEU A CG 1 ATOM 2249 C CD1 . LEU A 1 282 ? 33.824 37.756 26.792 1.00 31.15 ? 323 LEU A CD1 1 ATOM 2250 C CD2 . LEU A 1 282 ? 35.320 36.251 28.208 1.00 34.17 ? 323 LEU A CD2 1 ATOM 2251 N N . LYS A 1 283 ? 39.126 37.016 25.687 1.00 37.76 ? 324 LYS A N 1 ATOM 2252 C CA . LYS A 1 283 ? 40.122 36.967 24.619 1.00 41.11 ? 324 LYS A CA 1 ATOM 2253 C C . LYS A 1 283 ? 39.470 37.231 23.275 1.00 41.17 ? 324 LYS A C 1 ATOM 2254 O O . LYS A 1 283 ? 39.465 36.367 22.389 1.00 41.82 ? 324 LYS A O 1 ATOM 2255 C CB . LYS A 1 283 ? 40.861 35.624 24.660 1.00 43.01 ? 324 LYS A CB 1 ATOM 2256 C CG . LYS A 1 283 ? 41.555 35.391 26.001 1.00 47.64 ? 324 LYS A CG 1 ATOM 2257 C CD . LYS A 1 283 ? 42.571 36.502 26.288 1.00 54.59 ? 324 LYS A CD 1 ATOM 2258 C CE . LYS A 1 283 ? 42.743 36.736 27.790 1.00 57.92 ? 324 LYS A CE 1 ATOM 2259 N NZ . LYS A 1 283 ? 43.840 37.723 28.037 1.00 58.92 ? 324 LYS A NZ 1 ATOM 2260 N N . VAL A 1 284 ? 38.887 38.426 23.159 1.00 39.77 ? 325 VAL A N 1 ATOM 2261 C CA . VAL A 1 284 ? 38.317 38.945 21.914 1.00 40.14 ? 325 VAL A CA 1 ATOM 2262 C C . VAL A 1 284 ? 38.797 40.387 21.712 1.00 40.31 ? 325 VAL A C 1 ATOM 2263 O O . VAL A 1 284 ? 39.251 41.029 22.677 1.00 40.26 ? 325 VAL A O 1 ATOM 2264 C CB . VAL A 1 284 ? 36.761 38.930 21.929 1.00 38.80 ? 325 VAL A CB 1 ATOM 2265 C CG1 . VAL A 1 284 ? 36.230 37.514 22.087 1.00 40.58 ? 325 VAL A CG1 1 ATOM 2266 C CG2 . VAL A 1 284 ? 36.213 39.841 23.045 1.00 37.17 ? 325 VAL A CG2 1 ATOM 2267 N N . PRO A 1 285 ? 38.676 40.916 20.475 1.00 40.86 ? 326 PRO A N 1 ATOM 2268 C CA . PRO A 1 285 ? 39.125 42.294 20.200 1.00 41.15 ? 326 PRO A CA 1 ATOM 2269 C C . PRO A 1 285 ? 38.231 43.400 20.774 1.00 39.53 ? 326 PRO A C 1 ATOM 2270 O O . PRO A 1 285 ? 38.693 44.539 20.907 1.00 39.57 ? 326 PRO A O 1 ATOM 2271 C CB . PRO A 1 285 ? 39.116 42.376 18.666 1.00 42.51 ? 326 PRO A CB 1 ATOM 2272 C CG . PRO A 1 285 ? 38.105 41.313 18.223 1.00 44.13 ? 326 PRO A CG 1 ATOM 2273 C CD . PRO A 1 285 ? 38.170 40.220 19.268 1.00 41.99 ? 326 PRO A CD 1 ATOM 2274 N N . TYR A 1 286 ? 36.984 43.058 21.117 1.00 37.44 ? 327 TYR A N 1 ATOM 2275 C CA . TYR A 1 286 ? 35.953 44.037 21.547 1.00 36.05 ? 327 TYR A CA 1 ATOM 2276 C C . TYR A 1 286 ? 35.674 45.074 20.469 1.00 36.95 ? 327 TYR A C 1 ATOM 2277 O O . TYR A 1 286 ? 35.448 46.247 20.763 1.00 36.88 ? 327 TYR A O 1 ATOM 2278 C CB . TYR A 1 286 ? 36.335 44.691 22.874 1.00 35.57 ? 327 TYR A CB 1 ATOM 2279 C CG . TYR A 1 286 ? 36.182 43.730 24.012 1.00 33.60 ? 327 TYR A CG 1 ATOM 2280 C CD1 . TYR A 1 286 ? 34.926 43.526 24.617 1.00 32.67 ? 327 TYR A CD1 1 ATOM 2281 C CD2 . TYR A 1 286 ? 37.274 42.978 24.460 1.00 33.87 ? 327 TYR A CD2 1 ATOM 2282 C CE1 . TYR A 1 286 ? 34.777 42.631 25.663 1.00 32.29 ? 327 TYR A CE1 1 ATOM 2283 C CE2 . TYR A 1 286 ? 37.136 42.086 25.519 1.00 33.67 ? 327 TYR A CE2 1 ATOM 2284 C CZ . TYR A 1 286 ? 35.892 41.897 26.097 1.00 34.33 ? 327 TYR A CZ 1 ATOM 2285 O OH . TYR A 1 286 ? 35.739 41.021 27.153 1.00 32.36 ? 327 TYR A OH 1 ATOM 2286 N N . ASN A 1 287 ? 35.715 44.624 19.209 1.00 37.98 ? 328 ASN A N 1 ATOM 2287 C CA . ASN A 1 287 ? 35.319 45.439 18.075 1.00 38.88 ? 328 ASN A CA 1 ATOM 2288 C C . ASN A 1 287 ? 33.871 45.835 18.218 1.00 37.82 ? 328 ASN A C 1 ATOM 2289 O O . ASN A 1 287 ? 33.043 45.086 18.731 1.00 36.60 ? 328 ASN A O 1 ATOM 2290 C CB . ASN A 1 287 ? 35.507 44.679 16.762 1.00 38.97 ? 328 ASN A CB 1 ATOM 2291 C CG . ASN A 1 287 ? 36.976 44.505 16.370 1.00 41.73 ? 328 ASN A CG 1 ATOM 2292 O OD1 . ASN A 1 287 ? 37.866 45.265 16.790 1.00 42.78 ? 328 ASN A OD1 1 ATOM 2293 N ND2 . ASN A 1 287 ? 37.228 43.494 15.556 1.00 41.31 ? 328 ASN A ND2 1 ATOM 2294 N N . VAL A 1 288 ? 33.569 47.039 17.775 1.00 38.63 ? 329 VAL A N 1 ATOM 2295 C CA . VAL A 1 288 ? 32.259 47.598 18.027 1.00 37.68 ? 329 VAL A CA 1 ATOM 2296 C C . VAL A 1 288 ? 31.256 47.144 16.956 1.00 38.31 ? 329 VAL A C 1 ATOM 2297 O O . VAL A 1 288 ? 30.047 47.167 17.166 1.00 36.55 ? 329 VAL A O 1 ATOM 2298 C CB . VAL A 1 288 ? 32.374 49.122 18.132 1.00 38.82 ? 329 VAL A CB 1 ATOM 2299 C CG1 . VAL A 1 288 ? 31.017 49.751 17.997 1.00 39.51 ? 329 VAL A CG1 1 ATOM 2300 C CG2 . VAL A 1 288 ? 32.996 49.505 19.508 1.00 37.73 ? 329 VAL A CG2 1 ATOM 2301 N N . GLY A 1 289 ? 31.773 46.702 15.813 1.00 39.62 ? 330 GLY A N 1 ATOM 2302 C CA . GLY A 1 289 ? 30.920 46.298 14.691 1.00 41.38 ? 330 GLY A CA 1 ATOM 2303 C C . GLY A 1 289 ? 30.633 47.497 13.801 1.00 42.48 ? 330 GLY A C 1 ATOM 2304 O O . GLY A 1 289 ? 31.438 48.419 13.739 1.00 42.66 ? 330 GLY A O 1 ATOM 2305 N N . PRO A 1 290 ? 29.476 47.506 13.118 1.00 43.31 ? 331 PRO A N 1 ATOM 2306 C CA . PRO A 1 290 ? 28.429 46.484 13.093 1.00 43.16 ? 331 PRO A CA 1 ATOM 2307 C C . PRO A 1 290 ? 28.858 45.210 12.365 1.00 43.44 ? 331 PRO A C 1 ATOM 2308 O O . PRO A 1 290 ? 29.686 45.255 11.417 1.00 44.27 ? 331 PRO A O 1 ATOM 2309 C CB . PRO A 1 290 ? 27.303 47.163 12.310 1.00 43.67 ? 331 PRO A CB 1 ATOM 2310 C CG . PRO A 1 290 ? 28.034 48.113 11.372 1.00 46.59 ? 331 PRO A CG 1 ATOM 2311 C CD . PRO A 1 290 ? 29.144 48.652 12.245 1.00 45.00 ? 331 PRO A CD 1 ATOM 2312 N N . GLY A 1 291 ? 28.300 44.083 12.796 1.00 42.44 ? 332 GLY A N 1 ATOM 2313 C CA . GLY A 1 291 ? 28.478 42.819 12.074 1.00 43.28 ? 332 GLY A CA 1 ATOM 2314 C C . GLY A 1 291 ? 29.819 42.129 12.294 1.00 43.11 ? 332 GLY A C 1 ATOM 2315 O O . GLY A 1 291 ? 30.660 42.588 13.095 1.00 42.10 ? 332 GLY A O 1 ATOM 2316 N N . PHE A 1 292 ? 30.011 41.020 11.578 1.00 44.17 ? 333 PHE A N 1 ATOM 2317 C CA . PHE A 1 292 ? 31.166 40.150 11.780 1.00 43.87 ? 333 PHE A CA 1 ATOM 2318 C C . PHE A 1 292 ? 32.269 40.421 10.735 1.00 45.81 ? 333 PHE A C 1 ATOM 2319 O O . PHE A 1 292 ? 31.999 40.995 9.683 1.00 45.50 ? 333 PHE A O 1 ATOM 2320 C CB . PHE A 1 292 ? 30.754 38.669 11.691 1.00 44.29 ? 333 PHE A CB 1 ATOM 2321 C CG . PHE A 1 292 ? 29.831 38.192 12.797 1.00 43.66 ? 333 PHE A CG 1 ATOM 2322 C CD1 . PHE A 1 292 ? 28.834 37.266 12.503 1.00 44.35 ? 333 PHE A CD1 1 ATOM 2323 C CD2 . PHE A 1 292 ? 29.965 38.635 14.112 1.00 44.13 ? 333 PHE A CD2 1 ATOM 2324 C CE1 . PHE A 1 292 ? 27.983 36.789 13.478 1.00 44.95 ? 333 PHE A CE1 1 ATOM 2325 C CE2 . PHE A 1 292 ? 29.105 38.159 15.109 1.00 42.75 ? 333 PHE A CE2 1 ATOM 2326 C CZ . PHE A 1 292 ? 28.110 37.236 14.788 1.00 41.75 ? 333 PHE A CZ 1 ATOM 2327 N N . THR A 1 293 ? 33.491 39.992 11.033 1.00 46.68 ? 334 THR A N 1 ATOM 2328 C CA . THR A 1 293 ? 34.617 40.127 10.077 1.00 50.00 ? 334 THR A CA 1 ATOM 2329 C C . THR A 1 293 ? 34.403 39.360 8.767 1.00 52.60 ? 334 THR A C 1 ATOM 2330 O O . THR A 1 293 ? 33.615 38.405 8.704 1.00 52.66 ? 334 THR A O 1 ATOM 2331 C CB . THR A 1 293 ? 35.969 39.665 10.686 1.00 50.83 ? 334 THR A CB 1 ATOM 2332 O OG1 . THR A 1 293 ? 35.874 38.296 11.100 1.00 51.77 ? 334 THR A OG1 1 ATOM 2333 C CG2 . THR A 1 293 ? 36.367 40.527 11.862 1.00 50.02 ? 334 THR A CG2 1 ATOM 2334 N N . GLY A 1 294 ? 35.146 39.778 7.739 1.00 54.28 ? 335 GLY A N 1 ATOM 2335 C CA . GLY A 1 294 ? 35.028 39.277 6.366 1.00 57.31 ? 335 GLY A CA 1 ATOM 2336 C C . GLY A 1 294 ? 34.468 37.893 6.077 1.00 58.13 ? 335 GLY A C 1 ATOM 2337 O O . GLY A 1 294 ? 33.461 37.769 5.376 1.00 59.43 ? 335 GLY A O 1 ATOM 2338 N N . ASN A 1 295 ? 35.111 36.853 6.598 1.00 57.99 ? 336 ASN A N 1 ATOM 2339 C CA . ASN A 1 295 ? 34.661 35.477 6.358 1.00 58.99 ? 336 ASN A CA 1 ATOM 2340 C C . ASN A 1 295 ? 33.250 35.169 6.855 1.00 57.12 ? 336 ASN A C 1 ATOM 2341 O O . ASN A 1 295 ? 32.549 34.335 6.286 1.00 57.59 ? 336 ASN A O 1 ATOM 2342 C CB . ASN A 1 295 ? 35.652 34.473 6.964 1.00 60.06 ? 336 ASN A CB 1 ATOM 2343 C CG . ASN A 1 295 ? 37.000 34.484 6.266 1.00 64.63 ? 336 ASN A CG 1 ATOM 2344 O OD1 . ASN A 1 295 ? 37.166 35.084 5.192 1.00 69.36 ? 336 ASN A OD1 1 ATOM 2345 N ND2 . ASN A 1 295 ? 37.975 33.797 6.861 1.00 69.00 ? 336 ASN A ND2 1 ATOM 2346 N N . PHE A 1 296 ? 32.836 35.857 7.911 1.00 54.23 ? 337 PHE A N 1 ATOM 2347 C CA . PHE A 1 296 ? 31.556 35.566 8.548 1.00 52.20 ? 337 PHE A CA 1 ATOM 2348 C C . PHE A 1 296 ? 30.548 36.677 8.321 1.00 51.62 ? 337 PHE A C 1 ATOM 2349 O O . PHE A 1 296 ? 29.518 36.733 8.995 1.00 49.69 ? 337 PHE A O 1 ATOM 2350 C CB . PHE A 1 296 ? 31.773 35.357 10.044 1.00 50.95 ? 337 PHE A CB 1 ATOM 2351 C CG . PHE A 1 296 ? 32.920 34.454 10.362 1.00 51.21 ? 337 PHE A CG 1 ATOM 2352 C CD1 . PHE A 1 296 ? 34.117 34.977 10.824 1.00 51.86 ? 337 PHE A CD1 1 ATOM 2353 C CD2 . PHE A 1 296 ? 32.814 33.078 10.170 1.00 52.93 ? 337 PHE A CD2 1 ATOM 2354 C CE1 . PHE A 1 296 ? 35.189 34.150 11.118 1.00 51.57 ? 337 PHE A CE1 1 ATOM 2355 C CE2 . PHE A 1 296 ? 33.890 32.235 10.459 1.00 52.68 ? 337 PHE A CE2 1 ATOM 2356 C CZ . PHE A 1 296 ? 35.073 32.775 10.938 1.00 53.12 ? 337 PHE A CZ 1 ATOM 2357 N N . SER A 1 297 ? 30.838 37.546 7.355 1.00 52.53 ? 338 SER A N 1 ATOM 2358 C CA . SER A 1 297 ? 30.065 38.770 7.134 1.00 52.13 ? 338 SER A CA 1 ATOM 2359 C C . SER A 1 297 ? 28.604 38.491 6.823 1.00 51.23 ? 338 SER A C 1 ATOM 2360 O O . SER A 1 297 ? 27.748 39.351 7.072 1.00 50.90 ? 338 SER A O 1 ATOM 2361 C CB . SER A 1 297 ? 30.678 39.595 6.004 1.00 53.62 ? 338 SER A CB 1 ATOM 2362 O OG . SER A 1 297 ? 30.385 39.002 4.752 1.00 55.96 ? 338 SER A OG 1 ATOM 2363 N N . THR A 1 298 ? 28.327 37.292 6.307 1.00 50.65 ? 339 THR A N 1 ATOM 2364 C CA . THR A 1 298 ? 26.964 36.897 5.922 1.00 50.80 ? 339 THR A CA 1 ATOM 2365 C C . THR A 1 298 ? 26.179 36.185 7.026 1.00 49.07 ? 339 THR A C 1 ATOM 2366 O O . THR A 1 298 ? 24.976 35.927 6.878 1.00 49.59 ? 339 THR A O 1 ATOM 2367 C CB . THR A 1 298 ? 26.945 36.019 4.641 1.00 51.78 ? 339 THR A CB 1 ATOM 2368 O OG1 . THR A 1 298 ? 27.699 34.817 4.862 1.00 53.09 ? 339 THR A OG1 1 ATOM 2369 C CG2 . THR A 1 298 ? 27.531 36.786 3.457 1.00 55.25 ? 339 THR A CG2 1 ATOM 2370 N N . GLN A 1 299 ? 26.856 35.858 8.124 1.00 47.11 ? 340 GLN A N 1 ATOM 2371 C CA . GLN A 1 299 ? 26.170 35.318 9.312 1.00 44.64 ? 340 GLN A CA 1 ATOM 2372 C C . GLN A 1 299 ? 25.494 36.461 10.060 1.00 43.63 ? 340 GLN A C 1 ATOM 2373 O O . GLN A 1 299 ? 25.910 37.613 9.939 1.00 43.17 ? 340 GLN A O 1 ATOM 2374 C CB . GLN A 1 299 ? 27.157 34.565 10.208 1.00 43.75 ? 340 GLN A CB 1 ATOM 2375 C CG . GLN A 1 299 ? 27.795 33.352 9.496 1.00 46.68 ? 340 GLN A CG 1 ATOM 2376 C CD . GLN A 1 299 ? 28.916 32.667 10.277 1.00 46.85 ? 340 GLN A CD 1 ATOM 2377 O OE1 . GLN A 1 299 ? 29.274 33.069 11.382 1.00 46.60 ? 340 GLN A OE1 1 ATOM 2378 N NE2 . GLN A 1 299 ? 29.465 31.609 9.695 1.00 45.70 ? 340 GLN A NE2 1 ATOM 2379 N N . LYS A 1 300 ? 24.424 36.137 10.792 1.00 41.79 ? 341 LYS A N 1 ATOM 2380 C CA . LYS A 1 300 ? 23.681 37.118 11.571 1.00 40.50 ? 341 LYS A CA 1 ATOM 2381 C C . LYS A 1 300 ? 23.480 36.537 12.955 1.00 39.24 ? 341 LYS A C 1 ATOM 2382 O O . LYS A 1 300 ? 23.813 35.379 13.208 1.00 38.21 ? 341 LYS A O 1 ATOM 2383 C CB . LYS A 1 300 ? 22.292 37.392 10.959 1.00 40.94 ? 341 LYS A CB 1 ATOM 2384 C CG . LYS A 1 300 ? 22.254 37.841 9.479 1.00 43.76 ? 341 LYS A CG 1 ATOM 2385 C CD . LYS A 1 300 ? 22.542 39.325 9.325 1.00 48.62 ? 341 LYS A CD 1 ATOM 2386 C CE . LYS A 1 300 ? 22.837 39.675 7.872 1.00 53.62 ? 341 LYS A CE 1 ATOM 2387 N NZ . LYS A 1 300 ? 24.188 40.320 7.722 1.00 56.54 ? 341 LYS A NZ 1 ATOM 2388 N N . VAL A 1 301 ? 22.929 37.358 13.842 1.00 37.17 ? 342 VAL A N 1 ATOM 2389 C CA . VAL A 1 301 ? 22.483 36.892 15.150 1.00 36.03 ? 342 VAL A CA 1 ATOM 2390 C C . VAL A 1 301 ? 20.965 36.928 15.196 1.00 35.33 ? 342 VAL A C 1 ATOM 2391 O O . VAL A 1 301 ? 20.352 37.887 14.737 1.00 36.02 ? 342 VAL A O 1 ATOM 2392 C CB . VAL A 1 301 ? 23.117 37.732 16.279 1.00 35.14 ? 342 VAL A CB 1 ATOM 2393 C CG1 . VAL A 1 301 ? 22.435 37.458 17.606 1.00 35.57 ? 342 VAL A CG1 1 ATOM 2394 C CG2 . VAL A 1 301 ? 24.623 37.407 16.353 1.00 36.25 ? 342 VAL A CG2 1 ATOM 2395 N N . LYS A 1 302 ? 20.360 35.879 15.742 1.00 34.87 ? 343 LYS A N 1 ATOM 2396 C CA . LYS A 1 302 ? 18.916 35.822 15.846 1.00 34.27 ? 343 LYS A CA 1 ATOM 2397 C C . LYS A 1 302 ? 18.517 35.530 17.291 1.00 34.26 ? 343 LYS A C 1 ATOM 2398 O O . LYS A 1 302 ? 19.029 34.583 17.915 1.00 33.78 ? 343 LYS A O 1 ATOM 2399 C CB . LYS A 1 302 ? 18.349 34.764 14.877 1.00 36.27 ? 343 LYS A CB 1 ATOM 2400 C CG . LYS A 1 302 ? 16.818 34.593 14.959 1.00 34.19 ? 343 LYS A CG 1 ATOM 2401 C CD . LYS A 1 302 ? 16.424 33.551 13.900 1.00 39.54 ? 343 LYS A CD 1 ATOM 2402 C CE . LYS A 1 302 ? 14.909 33.491 13.746 1.00 42.43 ? 343 LYS A CE 1 ATOM 2403 N NZ . LYS A 1 302 ? 14.599 32.792 12.457 1.00 46.31 ? 343 LYS A NZ 1 ATOM 2404 N N . MET A 1 303 ? 17.603 36.335 17.818 1.00 32.50 ? 344 MET A N 1 ATOM 2405 C CA . MET A 1 303 ? 17.091 36.101 19.167 1.00 32.13 ? 344 MET A CA 1 ATOM 2406 C C . MET A 1 303 ? 15.783 35.314 19.070 1.00 32.61 ? 344 MET A C 1 ATOM 2407 O O . MET A 1 303 ? 15.058 35.431 18.071 1.00 33.48 ? 344 MET A O 1 ATOM 2408 C CB . MET A 1 303 ? 16.851 37.437 19.884 1.00 30.73 ? 344 MET A CB 1 ATOM 2409 C CG . MET A 1 303 ? 18.092 38.336 19.948 1.00 31.47 ? 344 MET A CG 1 ATOM 2410 S SD . MET A 1 303 ? 17.748 39.898 20.820 1.00 31.26 ? 344 MET A SD 1 ATOM 2411 C CE . MET A 1 303 ? 17.573 39.271 22.506 1.00 28.10 ? 344 MET A CE 1 ATOM 2412 N N . HIS A 1 304 ? 15.462 34.527 20.102 1.00 31.23 ? 345 HIS A N 1 ATOM 2413 C CA . HIS A 1 304 ? 14.170 33.822 20.129 1.00 31.29 ? 345 HIS A CA 1 ATOM 2414 C C . HIS A 1 304 ? 13.624 34.021 21.536 1.00 29.57 ? 345 HIS A C 1 ATOM 2415 O O . HIS A 1 304 ? 14.043 33.321 22.461 1.00 29.85 ? 345 HIS A O 1 ATOM 2416 C CB . HIS A 1 304 ? 14.323 32.306 19.868 1.00 32.33 ? 345 HIS A CB 1 ATOM 2417 C CG . HIS A 1 304 ? 15.211 31.961 18.708 1.00 35.71 ? 345 HIS A CG 1 ATOM 2418 N ND1 . HIS A 1 304 ? 16.587 32.017 18.784 1.00 38.06 ? 345 HIS A ND1 1 ATOM 2419 C CD2 . HIS A 1 304 ? 14.924 31.504 17.463 1.00 36.75 ? 345 HIS A CD2 1 ATOM 2420 C CE1 . HIS A 1 304 ? 17.110 31.654 17.623 1.00 38.56 ? 345 HIS A CE1 1 ATOM 2421 N NE2 . HIS A 1 304 ? 16.123 31.338 16.803 1.00 40.60 ? 345 HIS A NE2 1 ATOM 2422 N N . ILE A 1 305 ? 12.695 34.957 21.686 1.00 28.55 ? 346 ILE A N 1 ATOM 2423 C CA . ILE A 1 305 ? 12.168 35.293 23.031 1.00 27.96 ? 346 ILE A CA 1 ATOM 2424 C C . ILE A 1 305 ? 10.670 35.052 23.031 1.00 29.14 ? 346 ILE A C 1 ATOM 2425 O O . ILE A 1 305 ? 9.961 35.591 22.178 1.00 30.25 ? 346 ILE A O 1 ATOM 2426 C CB . ILE A 1 305 ? 12.486 36.749 23.419 1.00 27.82 ? 346 ILE A CB 1 ATOM 2427 C CG1 . ILE A 1 305 ? 13.987 37.066 23.217 1.00 29.88 ? 346 ILE A CG1 1 ATOM 2428 C CG2 . ILE A 1 305 ? 12.040 37.007 24.853 1.00 26.32 ? 346 ILE A CG2 1 ATOM 2429 C CD1 . ILE A 1 305 ? 14.980 36.185 24.047 1.00 32.06 ? 346 ILE A CD1 1 ATOM 2430 N N . HIS A 1 306 ? 10.201 34.238 23.981 1.00 28.10 ? 347 HIS A N 1 ATOM 2431 C CA . HIS A 1 306 ? 8.800 33.799 24.021 1.00 28.84 ? 347 HIS A CA 1 ATOM 2432 C C . HIS A 1 306 ? 8.159 33.920 25.403 1.00 27.95 ? 347 HIS A C 1 ATOM 2433 O O . HIS A 1 306 ? 7.079 33.326 25.677 1.00 28.59 ? 347 HIS A O 1 ATOM 2434 C CB . HIS A 1 306 ? 8.713 32.362 23.508 1.00 29.34 ? 347 HIS A CB 1 ATOM 2435 C CG . HIS A 1 306 ? 9.349 32.175 22.159 1.00 34.11 ? 347 HIS A CG 1 ATOM 2436 N ND1 . HIS A 1 306 ? 10.540 31.502 21.980 1.00 38.68 ? 347 HIS A ND1 1 ATOM 2437 C CD2 . HIS A 1 306 ? 8.978 32.626 20.935 1.00 37.00 ? 347 HIS A CD2 1 ATOM 2438 C CE1 . HIS A 1 306 ? 10.850 31.498 20.693 1.00 39.72 ? 347 HIS A CE1 1 ATOM 2439 N NE2 . HIS A 1 306 ? 9.923 32.181 20.040 1.00 42.11 ? 347 HIS A NE2 1 ATOM 2440 N N . SER A 1 307 ? 8.810 34.721 26.252 1.00 26.16 ? 348 SER A N 1 ATOM 2441 C CA . SER A 1 307 ? 8.287 34.993 27.585 1.00 25.33 ? 348 SER A CA 1 ATOM 2442 C C . SER A 1 307 ? 6.920 35.633 27.515 1.00 26.32 ? 348 SER A C 1 ATOM 2443 O O . SER A 1 307 ? 6.609 36.306 26.538 1.00 26.84 ? 348 SER A O 1 ATOM 2444 C CB . SER A 1 307 ? 9.240 35.919 28.351 1.00 25.00 ? 348 SER A CB 1 ATOM 2445 O OG . SER A 1 307 ? 10.523 35.304 28.365 1.00 25.34 ? 348 SER A OG 1 ATOM 2446 N N . THR A 1 308 ? 6.128 35.455 28.578 1.00 25.35 ? 349 THR A N 1 ATOM 2447 C CA . THR A 1 308 ? 4.780 36.046 28.596 1.00 25.70 ? 349 THR A CA 1 ATOM 2448 C C . THR A 1 308 ? 4.574 36.857 29.847 1.00 24.81 ? 349 THR A C 1 ATOM 2449 O O . THR A 1 308 ? 5.091 36.510 30.896 1.00 25.57 ? 349 THR A O 1 ATOM 2450 C CB . THR A 1 308 ? 3.649 35.013 28.498 1.00 27.67 ? 349 THR A CB 1 ATOM 2451 O OG1 . THR A 1 308 ? 3.725 34.097 29.587 1.00 32.56 ? 349 THR A OG1 1 ATOM 2452 C CG2 . THR A 1 308 ? 3.809 34.230 27.216 1.00 28.25 ? 349 THR A CG2 1 ATOM 2453 N N . ASN A 1 309 ? 3.836 37.937 29.703 1.00 24.40 ? 350 ASN A N 1 ATOM 2454 C CA . ASN A 1 309 ? 3.466 38.754 30.854 1.00 24.14 ? 350 ASN A CA 1 ATOM 2455 C C . ASN A 1 309 ? 2.113 38.256 31.318 1.00 25.05 ? 350 ASN A C 1 ATOM 2456 O O . ASN A 1 309 ? 1.214 38.021 30.507 1.00 27.41 ? 350 ASN A O 1 ATOM 2457 C CB . ASN A 1 309 ? 3.332 40.216 30.444 1.00 24.48 ? 350 ASN A CB 1 ATOM 2458 C CG . ASN A 1 309 ? 4.645 40.811 29.988 1.00 27.36 ? 350 ASN A CG 1 ATOM 2459 O OD1 . ASN A 1 309 ? 5.710 40.410 30.455 1.00 29.53 ? 350 ASN A OD1 1 ATOM 2460 N ND2 . ASN A 1 309 ? 4.580 41.767 29.038 1.00 29.84 ? 350 ASN A ND2 1 ATOM 2461 N N . GLU A 1 310 ? 1.953 38.106 32.629 1.00 24.62 ? 351 GLU A N 1 ATOM 2462 C CA . GLU A 1 310 ? 0.759 37.453 33.192 1.00 25.93 ? 351 GLU A CA 1 ATOM 2463 C C . GLU A 1 310 ? 0.395 38.153 34.501 1.00 23.85 ? 351 GLU A C 1 ATOM 2464 O O . GLU A 1 310 ? 1.251 38.283 35.366 1.00 23.03 ? 351 GLU A O 1 ATOM 2465 C CB . GLU A 1 310 ? 1.043 35.977 33.574 1.00 27.78 ? 351 GLU A CB 1 ATOM 2466 C CG A GLU A 1 310 ? 1.747 35.135 32.512 0.50 30.65 ? 351 GLU A CG 1 ATOM 2467 C CG B GLU A 1 310 ? -0.264 35.260 34.077 0.50 31.66 ? 351 GLU A CG 1 ATOM 2468 C CD A GLU A 1 310 ? 1.582 33.652 32.774 0.50 36.12 ? 351 GLU A CD 1 ATOM 2469 C CD B GLU A 1 310 ? -0.070 33.939 34.894 0.50 37.61 ? 351 GLU A CD 1 ATOM 2470 O OE1 A GLU A 1 310 ? 1.071 32.952 31.875 0.50 40.91 ? 351 GLU A OE1 1 ATOM 2471 O OE1 B GLU A 1 310 ? -0.485 32.889 34.358 0.50 38.67 ? 351 GLU A OE1 1 ATOM 2472 O OE2 A GLU A 1 310 ? 1.906 33.195 33.893 0.50 35.91 ? 351 GLU A OE2 1 ATOM 2473 O OE2 B GLU A 1 310 ? 0.435 33.934 36.068 0.50 34.71 ? 351 GLU A OE2 1 ATOM 2474 N N . VAL A 1 311 ? -0.868 38.536 34.671 1.00 23.35 ? 352 VAL A N 1 ATOM 2475 C CA . VAL A 1 311 ? -1.315 39.055 35.993 1.00 22.33 ? 352 VAL A CA 1 ATOM 2476 C C . VAL A 1 311 ? -1.374 37.897 36.994 1.00 22.26 ? 352 VAL A C 1 ATOM 2477 O O . VAL A 1 311 ? -2.007 36.833 36.740 1.00 23.54 ? 352 VAL A O 1 ATOM 2478 C CB . VAL A 1 311 ? -2.680 39.725 35.891 1.00 22.17 ? 352 VAL A CB 1 ATOM 2479 C CG1 . VAL A 1 311 ? -3.168 40.162 37.257 1.00 23.60 ? 352 VAL A CG1 1 ATOM 2480 C CG2 . VAL A 1 311 ? -2.603 40.982 34.980 1.00 24.91 ? 352 VAL A CG2 1 ATOM 2481 N N . THR A 1 312 ? -0.673 38.088 38.119 1.00 20.78 ? 353 THR A N 1 ATOM 2482 C CA . THR A 1 312 ? -0.377 37.010 39.049 1.00 20.51 ? 353 THR A CA 1 ATOM 2483 C C . THR A 1 312 ? -0.506 37.552 40.487 1.00 18.72 ? 353 THR A C 1 ATOM 2484 O O . THR A 1 312 ? -0.165 38.708 40.748 1.00 18.33 ? 353 THR A O 1 ATOM 2485 C CB . THR A 1 312 ? 1.043 36.497 38.789 1.00 21.71 ? 353 THR A CB 1 ATOM 2486 O OG1 . THR A 1 312 ? 1.170 36.158 37.390 1.00 24.56 ? 353 THR A OG1 1 ATOM 2487 C CG2 . THR A 1 312 ? 1.347 35.270 39.614 1.00 21.63 ? 353 THR A CG2 1 ATOM 2488 N N . ARG A 1 313 ? -1.020 36.722 41.394 1.00 20.16 ? 354 ARG A N 1 ATOM 2489 C CA . ARG A 1 313 ? -1.188 37.147 42.806 1.00 19.38 ? 354 ARG A CA 1 ATOM 2490 C C . ARG A 1 313 ? 0.159 37.138 43.552 1.00 20.14 ? 354 ARG A C 1 ATOM 2491 O O . ARG A 1 313 ? 0.947 36.201 43.396 1.00 20.72 ? 354 ARG A O 1 ATOM 2492 C CB . ARG A 1 313 ? -2.233 36.273 43.523 1.00 21.17 ? 354 ARG A CB 1 ATOM 2493 C CG . ARG A 1 313 ? -2.552 36.790 44.921 1.00 22.27 ? 354 ARG A CG 1 ATOM 2494 C CD . ARG A 1 313 ? -3.976 36.338 45.350 1.00 24.06 ? 354 ARG A CD 1 ATOM 2495 N NE . ARG A 1 313 ? -4.967 37.103 44.585 1.00 25.56 ? 354 ARG A NE 1 ATOM 2496 C CZ . ARG A 1 313 ? -6.277 37.068 44.805 1.00 27.77 ? 354 ARG A CZ 1 ATOM 2497 N NH1 . ARG A 1 313 ? -6.757 36.272 45.744 1.00 27.47 ? 354 ARG A NH1 1 ATOM 2498 N NH2 . ARG A 1 313 ? -7.097 37.831 44.087 1.00 28.33 ? 354 ARG A NH2 1 ATOM 2499 N N . ILE A 1 314 ? 0.374 38.171 44.362 1.00 18.10 ? 355 ILE A N 1 ATOM 2500 C CA . ILE A 1 314 ? 1.580 38.299 45.205 1.00 18.02 ? 355 ILE A CA 1 ATOM 2501 C C . ILE A 1 314 ? 1.119 38.582 46.630 1.00 18.79 ? 355 ILE A C 1 ATOM 2502 O O . ILE A 1 314 ? -0.010 39.027 46.821 1.00 18.65 ? 355 ILE A O 1 ATOM 2503 C CB . ILE A 1 314 ? 2.510 39.421 44.696 1.00 17.20 ? 355 ILE A CB 1 ATOM 2504 C CG1 . ILE A 1 314 ? 1.809 40.788 44.681 1.00 16.38 ? 355 ILE A CG1 1 ATOM 2505 C CG2 . ILE A 1 314 ? 2.991 39.057 43.276 1.00 17.42 ? 355 ILE A CG2 1 ATOM 2506 C CD1 . ILE A 1 314 ? 2.789 42.009 44.590 1.00 17.54 ? 355 ILE A CD1 1 ATOM 2507 N N . TYR A 1 315 ? 1.997 38.334 47.605 1.00 17.96 ? 356 TYR A N 1 ATOM 2508 C CA . TYR A 1 315 ? 1.572 38.389 49.019 1.00 17.69 ? 356 TYR A CA 1 ATOM 2509 C C . TYR A 1 315 ? 2.641 39.084 49.819 1.00 18.07 ? 356 TYR A C 1 ATOM 2510 O O . TYR A 1 315 ? 3.749 38.570 49.917 1.00 18.91 ? 356 TYR A O 1 ATOM 2511 C CB . TYR A 1 315 ? 1.429 36.953 49.559 1.00 18.43 ? 356 TYR A CB 1 ATOM 2512 C CG . TYR A 1 315 ? 0.373 36.113 48.882 1.00 19.39 ? 356 TYR A CG 1 ATOM 2513 C CD1 . TYR A 1 315 ? -0.953 36.139 49.326 1.00 21.67 ? 356 TYR A CD1 1 ATOM 2514 C CD2 . TYR A 1 315 ? 0.693 35.359 47.748 1.00 20.30 ? 356 TYR A CD2 1 ATOM 2515 C CE1 . TYR A 1 315 ? -1.936 35.349 48.694 1.00 22.37 ? 356 TYR A CE1 1 ATOM 2516 C CE2 . TYR A 1 315 ? -0.277 34.564 47.108 1.00 22.87 ? 356 TYR A CE2 1 ATOM 2517 C CZ . TYR A 1 315 ? -1.579 34.604 47.569 1.00 23.84 ? 356 TYR A CZ 1 ATOM 2518 O OH . TYR A 1 315 ? -2.535 33.841 46.912 1.00 26.05 ? 356 TYR A OH 1 ATOM 2519 N N . ASN A 1 316 ? 2.292 40.171 50.500 1.00 17.61 ? 357 ASN A N 1 ATOM 2520 C CA . ASN A 1 316 ? 3.205 40.779 51.480 1.00 17.85 ? 357 ASN A CA 1 ATOM 2521 C C . ASN A 1 316 ? 2.826 40.282 52.867 1.00 18.41 ? 357 ASN A C 1 ATOM 2522 O O . ASN A 1 316 ? 1.645 40.150 53.148 1.00 21.91 ? 357 ASN A O 1 ATOM 2523 C CB . ASN A 1 316 ? 3.074 42.304 51.521 1.00 17.89 ? 357 ASN A CB 1 ATOM 2524 C CG . ASN A 1 316 ? 3.398 42.976 50.188 1.00 18.38 ? 357 ASN A CG 1 ATOM 2525 O OD1 . ASN A 1 316 ? 4.269 42.558 49.461 1.00 16.87 ? 357 ASN A OD1 1 ATOM 2526 N ND2 . ASN A 1 316 ? 2.727 44.109 49.928 1.00 20.01 ? 357 ASN A ND2 1 ATOM 2527 N N . VAL A 1 317 ? 3.795 40.058 53.739 1.00 17.79 ? 358 VAL A N 1 ATOM 2528 C CA . VAL A 1 317 ? 3.411 39.790 55.149 1.00 17.98 ? 358 VAL A CA 1 ATOM 2529 C C . VAL A 1 317 ? 3.622 41.116 55.915 1.00 18.83 ? 358 VAL A C 1 ATOM 2530 O O . VAL A 1 317 ? 4.685 41.714 55.800 1.00 18.59 ? 358 VAL A O 1 ATOM 2531 C CB . VAL A 1 317 ? 4.292 38.702 55.788 1.00 18.92 ? 358 VAL A CB 1 ATOM 2532 C CG1 . VAL A 1 317 ? 3.749 38.359 57.200 1.00 19.74 ? 358 VAL A CG1 1 ATOM 2533 C CG2 . VAL A 1 317 ? 4.323 37.445 54.931 1.00 20.64 ? 358 VAL A CG2 1 ATOM 2534 N N . ILE A 1 318 ? 2.614 41.536 56.699 1.00 19.18 ? 359 ILE A N 1 ATOM 2535 C CA . ILE A 1 318 ? 2.708 42.815 57.419 1.00 18.81 ? 359 ILE A CA 1 ATOM 2536 C C . ILE A 1 318 ? 2.483 42.522 58.897 1.00 18.94 ? 359 ILE A C 1 ATOM 2537 O O . ILE A 1 318 ? 1.383 42.065 59.270 1.00 21.14 ? 359 ILE A O 1 ATOM 2538 C CB . ILE A 1 318 ? 1.599 43.807 56.930 1.00 19.18 ? 359 ILE A CB 1 ATOM 2539 C CG1 . ILE A 1 318 ? 1.670 44.009 55.410 1.00 20.89 ? 359 ILE A CG1 1 ATOM 2540 C CG2 . ILE A 1 318 ? 1.731 45.154 57.678 1.00 19.93 ? 359 ILE A CG2 1 ATOM 2541 C CD1 . ILE A 1 318 ? 2.989 44.650 54.920 1.00 21.92 ? 359 ILE A CD1 1 ATOM 2542 N N . GLY A 1 319 ? 3.509 42.748 59.695 1.00 19.69 ? 360 GLY A N 1 ATOM 2543 C CA . GLY A 1 319 ? 3.411 42.505 61.165 1.00 20.69 ? 360 GLY A CA 1 ATOM 2544 C C . GLY A 1 319 ? 3.378 43.811 61.918 1.00 20.27 ? 360 GLY A C 1 ATOM 2545 O O . GLY A 1 319 ? 4.026 44.767 61.534 1.00 21.97 ? 360 GLY A O 1 ATOM 2546 N N . THR A 1 320 ? 2.590 43.869 62.992 1.00 20.93 ? 361 THR A N 1 ATOM 2547 C CA . THR A 1 320 ? 2.470 45.132 63.753 1.00 21.75 ? 361 THR A CA 1 ATOM 2548 C C . THR A 1 320 ? 2.877 44.888 65.187 1.00 23.43 ? 361 THR A C 1 ATOM 2549 O O . THR A 1 320 ? 2.397 43.924 65.808 1.00 23.82 ? 361 THR A O 1 ATOM 2550 C CB . THR A 1 320 ? 1.002 45.595 63.752 1.00 24.01 ? 361 THR A CB 1 ATOM 2551 O OG1 . THR A 1 320 ? 0.614 45.851 62.386 1.00 24.90 ? 361 THR A OG1 1 ATOM 2552 C CG2 . THR A 1 320 ? 0.831 46.899 64.478 1.00 25.56 ? 361 THR A CG2 1 ATOM 2553 N N . LEU A 1 321 ? 3.718 45.770 65.721 1.00 22.30 ? 362 LEU A N 1 ATOM 2554 C CA . LEU A 1 321 ? 4.011 45.809 67.171 1.00 23.90 ? 362 LEU A CA 1 ATOM 2555 C C . LEU A 1 321 ? 3.513 47.175 67.643 1.00 23.78 ? 362 LEU A C 1 ATOM 2556 O O . LEU A 1 321 ? 4.167 48.180 67.422 1.00 23.41 ? 362 LEU A O 1 ATOM 2557 C CB . LEU A 1 321 ? 5.519 45.615 67.398 1.00 24.30 ? 362 LEU A CB 1 ATOM 2558 C CG . LEU A 1 321 ? 6.001 45.600 68.868 1.00 28.65 ? 362 LEU A CG 1 ATOM 2559 C CD1 . LEU A 1 321 ? 5.168 44.664 69.718 1.00 32.07 ? 362 LEU A CD1 1 ATOM 2560 C CD2 . LEU A 1 321 ? 7.465 45.226 68.903 1.00 29.13 ? 362 LEU A CD2 1 ATOM 2561 N N . ARG A 1 322 ? 2.345 47.196 68.276 1.00 22.76 ? 363 ARG A N 1 ATOM 2562 C CA . ARG A 1 322 ? 1.663 48.470 68.625 1.00 24.55 ? 363 ARG A CA 1 ATOM 2563 C C . ARG A 1 322 ? 2.488 49.284 69.650 1.00 24.51 ? 363 ARG A C 1 ATOM 2564 O O . ARG A 1 322 ? 2.950 48.739 70.682 1.00 25.75 ? 363 ARG A O 1 ATOM 2565 C CB . ARG A 1 322 ? 0.273 48.150 69.195 1.00 24.91 ? 363 ARG A CB 1 ATOM 2566 C CG . ARG A 1 322 ? -0.502 49.396 69.673 1.00 30.00 ? 363 ARG A CG 1 ATOM 2567 C CD . ARG A 1 322 ? -1.940 49.081 70.054 1.00 39.86 ? 363 ARG A CD 1 ATOM 2568 N NE . ARG A 1 322 ? -2.126 47.661 70.364 1.00 47.91 ? 363 ARG A NE 1 ATOM 2569 C CZ . ARG A 1 322 ? -1.955 47.095 71.555 1.00 50.34 ? 363 ARG A CZ 1 ATOM 2570 N NH1 . ARG A 1 322 ? -1.619 47.819 72.625 1.00 52.79 ? 363 ARG A NH1 1 ATOM 2571 N NH2 . ARG A 1 322 ? -2.145 45.783 71.673 1.00 51.86 ? 363 ARG A NH2 1 ATOM 2572 N N . GLY A 1 323 ? 2.652 50.581 69.387 1.00 23.58 ? 364 GLY A N 1 ATOM 2573 C CA . GLY A 1 323 ? 3.330 51.486 70.331 1.00 24.53 ? 364 GLY A CA 1 ATOM 2574 C C . GLY A 1 323 ? 2.551 51.733 71.622 1.00 25.13 ? 364 GLY A C 1 ATOM 2575 O O . GLY A 1 323 ? 1.310 51.799 71.639 1.00 26.97 ? 364 GLY A O 1 ATOM 2576 N N . ALA A 1 324 ? 3.302 51.877 72.706 1.00 26.52 ? 365 ALA A N 1 ATOM 2577 C CA . ALA A 1 324 ? 2.685 52.137 74.023 1.00 27.45 ? 365 ALA A CA 1 ATOM 2578 C C . ALA A 1 324 ? 2.162 53.553 74.198 1.00 28.46 ? 365 ALA A C 1 ATOM 2579 O O . ALA A 1 324 ? 1.205 53.794 74.992 1.00 29.98 ? 365 ALA A O 1 ATOM 2580 C CB . ALA A 1 324 ? 3.690 51.846 75.084 1.00 28.36 ? 365 ALA A CB 1 ATOM 2581 N N . VAL A 1 325 ? 2.829 54.513 73.565 1.00 27.35 ? 366 VAL A N 1 ATOM 2582 C CA . VAL A 1 325 ? 2.548 55.944 73.824 1.00 28.73 ? 366 VAL A CA 1 ATOM 2583 C C . VAL A 1 325 ? 2.064 56.668 72.553 1.00 27.55 ? 366 VAL A C 1 ATOM 2584 O O . VAL A 1 325 ? 1.084 57.433 72.569 1.00 27.09 ? 366 VAL A O 1 ATOM 2585 C CB . VAL A 1 325 ? 3.792 56.648 74.405 1.00 30.10 ? 366 VAL A CB 1 ATOM 2586 C CG1 . VAL A 1 325 ? 3.526 58.147 74.596 1.00 31.17 ? 366 VAL A CG1 1 ATOM 2587 C CG2 . VAL A 1 325 ? 4.205 56.002 75.729 1.00 32.75 ? 366 VAL A CG2 1 ATOM 2588 N N . GLU A 1 326 ? 2.744 56.406 71.435 1.00 24.53 ? 367 GLU A N 1 ATOM 2589 C CA . GLU A 1 326 ? 2.342 56.964 70.129 1.00 25.29 ? 367 GLU A CA 1 ATOM 2590 C C . GLU A 1 326 ? 2.040 55.857 69.101 1.00 22.34 ? 367 GLU A C 1 ATOM 2591 O O . GLU A 1 326 ? 2.806 55.670 68.115 1.00 21.75 ? 367 GLU A O 1 ATOM 2592 C CB . GLU A 1 326 ? 3.419 57.882 69.577 1.00 24.75 ? 367 GLU A CB 1 ATOM 2593 C CG . GLU A 1 326 ? 3.787 59.056 70.533 1.00 28.20 ? 367 GLU A CG 1 ATOM 2594 C CD . GLU A 1 326 ? 4.737 59.999 69.835 1.00 30.62 ? 367 GLU A CD 1 ATOM 2595 O OE1 . GLU A 1 326 ? 4.246 60.902 69.120 1.00 31.70 ? 367 GLU A OE1 1 ATOM 2596 O OE2 . GLU A 1 326 ? 5.969 59.856 70.037 1.00 33.00 ? 367 GLU A OE2 1 ATOM 2597 N N . PRO A 1 327 ? 0.923 55.131 69.306 1.00 23.36 ? 368 PRO A N 1 ATOM 2598 C CA . PRO A 1 327 ? 0.607 54.038 68.392 1.00 22.97 ? 368 PRO A CA 1 ATOM 2599 C C . PRO A 1 327 ? 0.292 54.507 66.980 1.00 22.16 ? 368 PRO A C 1 ATOM 2600 O O . PRO A 1 327 ? 0.338 53.707 66.063 1.00 22.93 ? 368 PRO A O 1 ATOM 2601 C CB . PRO A 1 327 ? -0.615 53.379 69.033 1.00 24.66 ? 368 PRO A CB 1 ATOM 2602 C CG . PRO A 1 327 ? -1.235 54.450 69.852 1.00 25.85 ? 368 PRO A CG 1 ATOM 2603 C CD . PRO A 1 327 ? -0.058 55.201 70.427 1.00 24.93 ? 368 PRO A CD 1 ATOM 2604 N N . ASP A 1 328 ? -0.018 55.800 66.827 1.00 22.17 ? 369 ASP A N 1 ATOM 2605 C CA . ASP A 1 328 ? -0.298 56.338 65.494 1.00 22.48 ? 369 ASP A CA 1 ATOM 2606 C C . ASP A 1 328 ? 0.935 56.924 64.836 1.00 20.80 ? 369 ASP A C 1 ATOM 2607 O O . ASP A 1 328 ? 0.817 57.813 63.979 1.00 20.19 ? 369 ASP A O 1 ATOM 2608 C CB . ASP A 1 328 ? -1.389 57.423 65.597 1.00 22.83 ? 369 ASP A CB 1 ATOM 2609 C CG . ASP A 1 328 ? -0.899 58.680 66.300 1.00 28.20 ? 369 ASP A CG 1 ATOM 2610 O OD1 . ASP A 1 328 ? 0.052 58.639 67.132 1.00 29.28 ? 369 ASP A OD1 1 ATOM 2611 O OD2 . ASP A 1 328 ? -1.517 59.764 66.059 1.00 30.09 ? 369 ASP A OD2 1 ATOM 2612 N N . ARG A 1 329 ? 2.127 56.450 65.238 1.00 21.37 ? 370 ARG A N 1 ATOM 2613 C CA . ARG A 1 329 ? 3.382 56.825 64.569 1.00 19.84 ? 370 ARG A CA 1 ATOM 2614 C C . ARG A 1 329 ? 4.065 55.544 64.184 1.00 20.23 ? 370 ARG A C 1 ATOM 2615 O O . ARG A 1 329 ? 4.195 54.660 65.043 1.00 20.14 ? 370 ARG A O 1 ATOM 2616 C CB . ARG A 1 329 ? 4.275 57.677 65.494 1.00 19.70 ? 370 ARG A CB 1 ATOM 2617 C CG . ARG A 1 329 ? 3.634 59.057 65.805 1.00 19.83 ? 370 ARG A CG 1 ATOM 2618 C CD . ARG A 1 329 ? 3.850 59.942 64.578 1.00 20.77 ? 370 ARG A CD 1 ATOM 2619 N NE . ARG A 1 329 ? 3.194 61.282 64.665 1.00 20.71 ? 370 ARG A NE 1 ATOM 2620 C CZ . ARG A 1 329 ? 1.960 61.597 64.210 1.00 21.61 ? 370 ARG A CZ 1 ATOM 2621 N NH1 . ARG A 1 329 ? 1.078 60.679 63.808 1.00 20.45 ? 370 ARG A NH1 1 ATOM 2622 N NH2 . ARG A 1 329 ? 1.557 62.887 64.189 1.00 22.47 ? 370 ARG A NH2 1 ATOM 2623 N N . TYR A 1 330 ? 4.450 55.417 62.919 1.00 17.97 ? 371 TYR A N 1 ATOM 2624 C CA . TYR A 1 330 ? 4.928 54.129 62.403 1.00 18.42 ? 371 TYR A CA 1 ATOM 2625 C C . TYR A 1 330 ? 6.384 54.181 62.028 1.00 18.94 ? 371 TYR A C 1 ATOM 2626 O O . TYR A 1 330 ? 6.812 55.037 61.224 1.00 20.08 ? 371 TYR A O 1 ATOM 2627 C CB . TYR A 1 330 ? 4.181 53.737 61.125 1.00 17.29 ? 371 TYR A CB 1 ATOM 2628 C CG . TYR A 1 330 ? 2.678 53.661 61.277 1.00 18.57 ? 371 TYR A CG 1 ATOM 2629 C CD1 . TYR A 1 330 ? 2.060 53.287 62.473 1.00 21.75 ? 371 TYR A CD1 1 ATOM 2630 C CD2 . TYR A 1 330 ? 1.867 53.974 60.207 1.00 18.48 ? 371 TYR A CD2 1 ATOM 2631 C CE1 . TYR A 1 330 ? 0.665 53.246 62.588 1.00 21.55 ? 371 TYR A CE1 1 ATOM 2632 C CE2 . TYR A 1 330 ? 0.479 53.897 60.298 1.00 18.89 ? 371 TYR A CE2 1 ATOM 2633 C CZ . TYR A 1 330 ? -0.127 53.515 61.469 1.00 21.49 ? 371 TYR A CZ 1 ATOM 2634 O OH . TYR A 1 330 ? -1.504 53.471 61.524 1.00 21.36 ? 371 TYR A OH 1 ATOM 2635 N N . VAL A 1 331 ? 7.152 53.232 62.564 1.00 17.78 ? 372 VAL A N 1 ATOM 2636 C CA . VAL A 1 331 ? 8.537 53.013 62.150 1.00 17.61 ? 372 VAL A CA 1 ATOM 2637 C C . VAL A 1 331 ? 8.486 51.675 61.375 1.00 18.07 ? 372 VAL A C 1 ATOM 2638 O O . VAL A 1 331 ? 7.994 50.690 61.904 1.00 19.33 ? 372 VAL A O 1 ATOM 2639 C CB . VAL A 1 331 ? 9.487 52.961 63.370 1.00 19.29 ? 372 VAL A CB 1 ATOM 2640 C CG1 . VAL A 1 331 ? 10.882 52.547 62.901 1.00 18.72 ? 372 VAL A CG1 1 ATOM 2641 C CG2 . VAL A 1 331 ? 9.583 54.355 64.006 1.00 19.17 ? 372 VAL A CG2 1 ATOM 2642 N N . ILE A 1 332 ? 8.972 51.651 60.138 1.00 16.45 ? 373 ILE A N 1 ATOM 2643 C CA . ILE A 1 332 ? 8.756 50.468 59.302 1.00 17.16 ? 373 ILE A CA 1 ATOM 2644 C C . ILE A 1 332 ? 10.111 49.842 59.013 1.00 16.94 ? 373 ILE A C 1 ATOM 2645 O O . ILE A 1 332 ? 11.034 50.521 58.568 1.00 19.11 ? 373 ILE A O 1 ATOM 2646 C CB . ILE A 1 332 ? 8.077 50.884 57.975 1.00 15.92 ? 373 ILE A CB 1 ATOM 2647 C CG1 . ILE A 1 332 ? 6.759 51.610 58.309 1.00 19.56 ? 373 ILE A CG1 1 ATOM 2648 C CG2 . ILE A 1 332 ? 7.835 49.591 57.106 1.00 19.08 ? 373 ILE A CG2 1 ATOM 2649 C CD1 . ILE A 1 332 ? 6.054 52.154 57.017 1.00 25.07 ? 373 ILE A CD1 1 ATOM 2650 N N . LEU A 1 333 ? 10.221 48.534 59.240 1.00 16.88 ? 374 LEU A N 1 ATOM 2651 C CA . LEU A 1 333 ? 11.400 47.760 58.785 1.00 16.20 ? 374 LEU A CA 1 ATOM 2652 C C . LEU A 1 333 ? 10.884 46.801 57.719 1.00 18.12 ? 374 LEU A C 1 ATOM 2653 O O . LEU A 1 333 ? 10.069 45.932 57.998 1.00 18.44 ? 374 LEU A O 1 ATOM 2654 C CB . LEU A 1 333 ? 11.962 46.945 59.965 1.00 18.78 ? 374 LEU A CB 1 ATOM 2655 C CG . LEU A 1 333 ? 13.135 45.991 59.594 1.00 17.67 ? 374 LEU A CG 1 ATOM 2656 C CD1 . LEU A 1 333 ? 14.365 46.781 59.137 1.00 19.56 ? 374 LEU A CD1 1 ATOM 2657 C CD2 . LEU A 1 333 ? 13.511 45.154 60.894 1.00 20.41 ? 374 LEU A CD2 1 ATOM 2658 N N . GLY A 1 334 ? 11.363 46.964 56.505 1.00 18.50 ? 375 GLY A N 1 ATOM 2659 C CA . GLY A 1 334 ? 10.837 46.123 55.416 1.00 18.07 ? 375 GLY A CA 1 ATOM 2660 C C . GLY A 1 334 ? 11.916 45.572 54.527 1.00 19.42 ? 375 GLY A C 1 ATOM 2661 O O . GLY A 1 334 ? 12.925 46.216 54.274 1.00 20.21 ? 375 GLY A O 1 ATOM 2662 N N . GLY A 1 335 ? 11.671 44.379 54.000 1.00 18.95 ? 376 GLY A N 1 ATOM 2663 C CA . GLY A 1 335 ? 12.607 43.893 52.956 1.00 19.77 ? 376 GLY A CA 1 ATOM 2664 C C . GLY A 1 335 ? 11.874 42.794 52.231 1.00 18.85 ? 376 GLY A C 1 ATOM 2665 O O . GLY A 1 335 ? 10.864 42.284 52.723 1.00 20.30 ? 376 GLY A O 1 ATOM 2666 N N . HIS A 1 336 ? 12.379 42.428 51.054 1.00 17.85 ? 377 HIS A N 1 ATOM 2667 C CA . HIS A 1 336 ? 11.608 41.448 50.295 1.00 16.50 ? 377 HIS A CA 1 ATOM 2668 C C . HIS A 1 336 ? 11.978 39.995 50.546 1.00 18.17 ? 377 HIS A C 1 ATOM 2669 O O . HIS A 1 336 ? 13.034 39.677 51.149 1.00 19.63 ? 377 HIS A O 1 ATOM 2670 C CB . HIS A 1 336 ? 11.680 41.811 48.796 1.00 16.07 ? 377 HIS A CB 1 ATOM 2671 C CG . HIS A 1 336 ? 12.988 41.490 48.113 1.00 15.83 ? 377 HIS A CG 1 ATOM 2672 N ND1 . HIS A 1 336 ? 13.095 40.415 47.247 1.00 17.15 ? 377 HIS A ND1 1 ATOM 2673 C CD2 . HIS A 1 336 ? 14.137 42.197 47.972 1.00 17.04 ? 377 HIS A CD2 1 ATOM 2674 C CE1 . HIS A 1 336 ? 14.290 40.431 46.673 1.00 16.77 ? 377 HIS A CE1 1 ATOM 2675 N NE2 . HIS A 1 336 ? 14.948 41.498 47.095 1.00 17.06 ? 377 HIS A NE2 1 ATOM 2676 N N . ARG A 1 337 ? 11.103 39.121 50.062 1.00 17.49 ? 378 ARG A N 1 ATOM 2677 C CA . ARG A 1 337 ? 11.166 37.673 50.304 1.00 18.58 ? 378 ARG A CA 1 ATOM 2678 C C . ARG A 1 337 ? 11.283 36.924 48.990 1.00 19.12 ? 378 ARG A C 1 ATOM 2679 O O . ARG A 1 337 ? 11.836 35.815 48.956 1.00 19.12 ? 378 ARG A O 1 ATOM 2680 C CB . ARG A 1 337 ? 9.823 37.278 50.944 1.00 19.75 ? 378 ARG A CB 1 ATOM 2681 C CG . ARG A 1 337 ? 9.718 35.804 51.320 1.00 20.75 ? 378 ARG A CG 1 ATOM 2682 C CD . ARG A 1 337 ? 8.322 35.466 51.822 1.00 21.56 ? 378 ARG A CD 1 ATOM 2683 N NE . ARG A 1 337 ? 7.284 35.561 50.762 1.00 19.80 ? 378 ARG A NE 1 ATOM 2684 C CZ . ARG A 1 337 ? 6.423 36.548 50.593 1.00 20.44 ? 378 ARG A CZ 1 ATOM 2685 N NH1 . ARG A 1 337 ? 6.364 37.593 51.427 1.00 19.70 ? 378 ARG A NH1 1 ATOM 2686 N NH2 . ARG A 1 337 ? 5.566 36.493 49.565 1.00 20.69 ? 378 ARG A NH2 1 ATOM 2687 N N . ASP A 1 338 ? 10.763 37.507 47.895 1.00 18.42 ? 379 ASP A N 1 ATOM 2688 C CA . ASP A 1 338 ? 10.821 36.799 46.588 1.00 17.99 ? 379 ASP A CA 1 ATOM 2689 C C . ASP A 1 338 ? 12.272 36.800 46.104 1.00 18.57 ? 379 ASP A C 1 ATOM 2690 O O . ASP A 1 338 ? 13.003 37.769 46.316 1.00 19.02 ? 379 ASP A O 1 ATOM 2691 C CB . ASP A 1 338 ? 9.925 37.505 45.568 1.00 17.17 ? 379 ASP A CB 1 ATOM 2692 C CG . ASP A 1 338 ? 10.405 38.916 45.243 1.00 18.45 ? 379 ASP A CG 1 ATOM 2693 O OD1 . ASP A 1 338 ? 10.427 39.774 46.166 1.00 17.85 ? 379 ASP A OD1 1 ATOM 2694 O OD2 . ASP A 1 338 ? 10.678 39.169 44.064 1.00 18.03 ? 379 ASP A OD2 1 ATOM 2695 N N . SER A 1 339 ? 12.672 35.746 45.401 1.00 18.44 ? 380 SER A N 1 ATOM 2696 C CA . SER A 1 339 ? 14.039 35.668 44.909 1.00 18.80 ? 380 SER A CA 1 ATOM 2697 C C . SER A 1 339 ? 13.985 35.196 43.460 1.00 20.13 ? 380 SER A C 1 ATOM 2698 O O . SER A 1 339 ? 12.957 34.669 43.032 1.00 20.27 ? 380 SER A O 1 ATOM 2699 C CB . SER A 1 339 ? 14.833 34.660 45.757 1.00 20.75 ? 380 SER A CB 1 ATOM 2700 O OG . SER A 1 339 ? 14.221 33.363 45.742 1.00 22.17 ? 380 SER A OG 1 ATOM 2701 N N . TRP A 1 340 ? 15.066 35.373 42.712 1.00 19.24 ? 381 TRP A N 1 ATOM 2702 C CA . TRP A 1 340 ? 15.115 34.808 41.366 1.00 19.69 ? 381 TRP A CA 1 ATOM 2703 C C . TRP A 1 340 ? 15.226 33.296 41.419 1.00 21.68 ? 381 TRP A C 1 ATOM 2704 O O . TRP A 1 340 ? 14.473 32.612 40.749 1.00 21.39 ? 381 TRP A O 1 ATOM 2705 C CB . TRP A 1 340 ? 16.258 35.414 40.500 1.00 20.03 ? 381 TRP A CB 1 ATOM 2706 C CG . TRP A 1 340 ? 15.845 36.768 40.011 1.00 19.42 ? 381 TRP A CG 1 ATOM 2707 C CD1 . TRP A 1 340 ? 16.379 37.999 40.345 1.00 19.48 ? 381 TRP A CD1 1 ATOM 2708 C CD2 . TRP A 1 340 ? 14.746 37.029 39.148 1.00 17.85 ? 381 TRP A CD2 1 ATOM 2709 N NE1 . TRP A 1 340 ? 15.681 39.026 39.702 1.00 18.62 ? 381 TRP A NE1 1 ATOM 2710 C CE2 . TRP A 1 340 ? 14.675 38.436 38.956 1.00 18.80 ? 381 TRP A CE2 1 ATOM 2711 C CE3 . TRP A 1 340 ? 13.813 36.189 38.490 1.00 20.72 ? 381 TRP A CE3 1 ATOM 2712 C CZ2 . TRP A 1 340 ? 13.677 39.030 38.165 1.00 18.57 ? 381 TRP A CZ2 1 ATOM 2713 C CZ3 . TRP A 1 340 ? 12.801 36.781 37.706 1.00 18.72 ? 381 TRP A CZ3 1 ATOM 2714 C CH2 . TRP A 1 340 ? 12.745 38.197 37.581 1.00 18.09 ? 381 TRP A CH2 1 ATOM 2715 N N . VAL A 1 341 ? 16.136 32.783 42.240 1.00 20.53 ? 382 VAL A N 1 ATOM 2716 C CA . VAL A 1 341 ? 16.244 31.323 42.443 1.00 20.37 ? 382 VAL A CA 1 ATOM 2717 C C . VAL A 1 341 ? 16.285 31.077 43.959 1.00 20.99 ? 382 VAL A C 1 ATOM 2718 O O . VAL A 1 341 ? 15.263 31.220 44.621 1.00 20.42 ? 382 VAL A O 1 ATOM 2719 C CB . VAL A 1 341 ? 17.421 30.648 41.672 1.00 21.08 ? 382 VAL A CB 1 ATOM 2720 C CG1 . VAL A 1 341 ? 17.178 29.132 41.695 1.00 23.22 ? 382 VAL A CG1 1 ATOM 2721 C CG2 . VAL A 1 341 ? 17.425 31.078 40.201 1.00 23.70 ? 382 VAL A CG2 1 ATOM 2722 N N . PHE A 1 342 ? 17.438 30.697 44.504 1.00 20.43 ? 383 PHE A N 1 ATOM 2723 C CA . PHE A 1 342 ? 17.487 30.350 45.940 1.00 20.82 ? 383 PHE A CA 1 ATOM 2724 C C . PHE A 1 342 ? 17.639 31.544 46.839 1.00 22.00 ? 383 PHE A C 1 ATOM 2725 O O . PHE A 1 342 ? 17.336 31.444 48.028 1.00 22.85 ? 383 PHE A O 1 ATOM 2726 C CB . PHE A 1 342 ? 18.633 29.361 46.221 1.00 21.30 ? 383 PHE A CB 1 ATOM 2727 C CG . PHE A 1 342 ? 18.486 28.089 45.438 1.00 23.82 ? 383 PHE A CG 1 ATOM 2728 C CD1 . PHE A 1 342 ? 17.455 27.182 45.763 1.00 23.41 ? 383 PHE A CD1 1 ATOM 2729 C CD2 . PHE A 1 342 ? 19.301 27.850 44.330 1.00 25.35 ? 383 PHE A CD2 1 ATOM 2730 C CE1 . PHE A 1 342 ? 17.275 25.996 44.976 1.00 25.54 ? 383 PHE A CE1 1 ATOM 2731 C CE2 . PHE A 1 342 ? 19.136 26.668 43.544 1.00 23.34 ? 383 PHE A CE2 1 ATOM 2732 C CZ . PHE A 1 342 ? 18.103 25.782 43.852 1.00 24.70 ? 383 PHE A CZ 1 ATOM 2733 N N . GLY A 1 343 ? 18.114 32.662 46.295 1.00 21.23 ? 384 GLY A N 1 ATOM 2734 C CA . GLY A 1 343 ? 18.231 33.905 47.114 1.00 21.50 ? 384 GLY A CA 1 ATOM 2735 C C . GLY A 1 343 ? 19.174 33.873 48.323 1.00 21.38 ? 384 GLY A C 1 ATOM 2736 O O . GLY A 1 343 ? 18.927 34.583 49.318 1.00 21.18 ? 384 GLY A O 1 ATOM 2737 N N . GLY A 1 344 ? 20.281 33.139 48.200 1.00 21.16 ? 385 GLY A N 1 ATOM 2738 C CA . GLY A 1 344 ? 21.266 32.966 49.269 1.00 21.64 ? 385 GLY A CA 1 ATOM 2739 C C . GLY A 1 344 ? 21.709 34.276 49.859 1.00 21.20 ? 385 GLY A C 1 ATOM 2740 O O . GLY A 1 344 ? 21.798 34.415 51.094 1.00 23.10 ? 385 GLY A O 1 ATOM 2741 N N . ILE A 1 345 ? 22.005 35.244 48.993 1.00 20.68 ? 386 ILE A N 1 ATOM 2742 C CA . ILE A 1 345 ? 22.286 36.604 49.441 1.00 19.77 ? 386 ILE A CA 1 ATOM 2743 C C . ILE A 1 345 ? 21.026 37.460 49.238 1.00 19.98 ? 386 ILE A C 1 ATOM 2744 O O . ILE A 1 345 ? 20.518 38.053 50.206 1.00 19.76 ? 386 ILE A O 1 ATOM 2745 C CB . ILE A 1 345 ? 23.523 37.218 48.728 1.00 19.30 ? 386 ILE A CB 1 ATOM 2746 C CG1 . ILE A 1 345 ? 24.773 36.488 49.238 1.00 21.91 ? 386 ILE A CG1 1 ATOM 2747 C CG2 . ILE A 1 345 ? 23.646 38.736 49.027 1.00 21.29 ? 386 ILE A CG2 1 ATOM 2748 C CD1 . ILE A 1 345 ? 26.037 36.856 48.478 1.00 25.09 ? 386 ILE A CD1 1 ATOM 2749 N N . ASP A 1 346 ? 20.557 37.537 47.999 1.00 20.06 ? 387 ASP A N 1 ATOM 2750 C CA . ASP A 1 346 ? 19.471 38.466 47.633 1.00 18.72 ? 387 ASP A CA 1 ATOM 2751 C C . ASP A 1 346 ? 18.142 37.661 47.488 1.00 18.98 ? 387 ASP A C 1 ATOM 2752 O O . ASP A 1 346 ? 17.981 36.944 46.495 1.00 19.28 ? 387 ASP A O 1 ATOM 2753 C CB . ASP A 1 346 ? 19.871 39.120 46.309 1.00 18.40 ? 387 ASP A CB 1 ATOM 2754 C CG . ASP A 1 346 ? 18.892 40.088 45.815 1.00 18.48 ? 387 ASP A CG 1 ATOM 2755 O OD1 . ASP A 1 346 ? 17.898 40.323 46.532 1.00 18.39 ? 387 ASP A OD1 1 ATOM 2756 O OD2 . ASP A 1 346 ? 19.100 40.594 44.679 1.00 20.13 ? 387 ASP A OD2 1 ATOM 2757 N N . PRO A 1 347 ? 17.218 37.753 48.446 1.00 18.10 ? 388 PRO A N 1 ATOM 2758 C CA . PRO A 1 347 ? 17.169 38.672 49.596 1.00 16.78 ? 388 PRO A CA 1 ATOM 2759 C C . PRO A 1 347 ? 17.360 37.947 50.931 1.00 18.50 ? 388 PRO A C 1 ATOM 2760 O O . PRO A 1 347 ? 17.221 38.597 51.965 1.00 18.97 ? 388 PRO A O 1 ATOM 2761 C CB . PRO A 1 347 ? 15.701 39.169 49.546 1.00 17.02 ? 388 PRO A CB 1 ATOM 2762 C CG . PRO A 1 347 ? 14.935 37.884 49.161 1.00 18.12 ? 388 PRO A CG 1 ATOM 2763 C CD . PRO A 1 347 ? 15.871 37.141 48.229 1.00 18.24 ? 388 PRO A CD 1 ATOM 2764 N N . GLN A 1 348 ? 17.582 36.626 50.937 1.00 19.06 ? 389 GLN A N 1 ATOM 2765 C CA . GLN A 1 348 ? 17.327 35.944 52.206 1.00 20.11 ? 389 GLN A CA 1 ATOM 2766 C C . GLN A 1 348 ? 18.362 36.258 53.277 1.00 20.82 ? 389 GLN A C 1 ATOM 2767 O O . GLN A 1 348 ? 18.074 36.086 54.463 1.00 20.54 ? 389 GLN A O 1 ATOM 2768 C CB . GLN A 1 348 ? 17.277 34.422 52.025 1.00 21.24 ? 389 GLN A CB 1 ATOM 2769 C CG . GLN A 1 348 ? 16.221 33.946 51.002 1.00 20.31 ? 389 GLN A CG 1 ATOM 2770 C CD . GLN A 1 348 ? 14.785 34.505 51.242 1.00 19.81 ? 389 GLN A CD 1 ATOM 2771 O OE1 . GLN A 1 348 ? 14.449 35.064 52.291 1.00 21.35 ? 389 GLN A OE1 1 ATOM 2772 N NE2 . GLN A 1 348 ? 13.927 34.317 50.243 1.00 20.38 ? 389 GLN A NE2 1 ATOM 2773 N N . SER A 1 349 ? 19.539 36.719 52.879 1.00 19.64 ? 390 SER A N 1 ATOM 2774 C CA . SER A 1 349 ? 20.481 37.213 53.921 1.00 21.26 ? 390 SER A CA 1 ATOM 2775 C C . SER A 1 349 ? 19.911 38.421 54.679 1.00 20.64 ? 390 SER A C 1 ATOM 2776 O O . SER A 1 349 ? 20.193 38.601 55.881 1.00 21.75 ? 390 SER A O 1 ATOM 2777 C CB . SER A 1 349 ? 21.871 37.499 53.312 1.00 22.52 ? 390 SER A CB 1 ATOM 2778 O OG . SER A 1 349 ? 21.851 38.658 52.527 1.00 23.52 ? 390 SER A OG 1 ATOM 2779 N N . GLY A 1 350 ? 19.094 39.218 53.998 1.00 19.56 ? 391 GLY A N 1 ATOM 2780 C CA . GLY A 1 350 ? 18.347 40.329 54.626 1.00 18.86 ? 391 GLY A CA 1 ATOM 2781 C C . GLY A 1 350 ? 17.137 39.809 55.395 1.00 20.06 ? 391 GLY A C 1 ATOM 2782 O O . GLY A 1 350 ? 16.916 40.226 56.513 1.00 20.03 ? 391 GLY A O 1 ATOM 2783 N N . ALA A 1 351 ? 16.356 38.910 54.788 1.00 18.36 ? 392 ALA A N 1 ATOM 2784 C CA . ALA A 1 351 ? 15.134 38.408 55.418 1.00 19.90 ? 392 ALA A CA 1 ATOM 2785 C C . ALA A 1 351 ? 15.420 37.641 56.706 1.00 20.17 ? 392 ALA A C 1 ATOM 2786 O O . ALA A 1 351 ? 14.627 37.713 57.643 1.00 20.27 ? 392 ALA A O 1 ATOM 2787 C CB . ALA A 1 351 ? 14.340 37.550 54.461 1.00 20.35 ? 392 ALA A CB 1 ATOM 2788 N N . ALA A 1 352 ? 16.557 36.943 56.749 1.00 20.86 ? 393 ALA A N 1 ATOM 2789 C CA . ALA A 1 352 ? 16.963 36.211 57.954 1.00 20.79 ? 393 ALA A CA 1 ATOM 2790 C C . ALA A 1 352 ? 17.258 37.180 59.068 1.00 22.22 ? 393 ALA A C 1 ATOM 2791 O O . ALA A 1 352 ? 17.004 36.885 60.241 1.00 21.56 ? 393 ALA A O 1 ATOM 2792 C CB . ALA A 1 352 ? 18.239 35.327 57.662 1.00 22.03 ? 393 ALA A CB 1 ATOM 2793 N N . VAL A 1 353 ? 17.852 38.317 58.706 1.00 20.61 ? 394 VAL A N 1 ATOM 2794 C CA . VAL A 1 353 ? 18.151 39.380 59.689 1.00 20.74 ? 394 VAL A CA 1 ATOM 2795 C C . VAL A 1 353 ? 16.840 39.995 60.206 1.00 21.04 ? 394 VAL A C 1 ATOM 2796 O O . VAL A 1 353 ? 16.699 40.209 61.429 1.00 21.25 ? 394 VAL A O 1 ATOM 2797 C CB . VAL A 1 353 ? 19.090 40.423 59.038 1.00 20.60 ? 394 VAL A CB 1 ATOM 2798 C CG1 . VAL A 1 353 ? 19.019 41.802 59.735 1.00 21.25 ? 394 VAL A CG1 1 ATOM 2799 C CG2 . VAL A 1 353 ? 20.552 39.881 59.032 1.00 19.85 ? 394 VAL A CG2 1 ATOM 2800 N N . VAL A 1 354 ? 15.882 40.281 59.303 1.00 19.96 ? 395 VAL A N 1 ATOM 2801 C CA . VAL A 1 354 ? 14.594 40.829 59.718 1.00 20.74 ? 395 VAL A CA 1 ATOM 2802 C C . VAL A 1 354 ? 13.933 39.820 60.670 1.00 20.45 ? 395 VAL A C 1 ATOM 2803 O O . VAL A 1 354 ? 13.395 40.196 61.714 1.00 20.83 ? 395 VAL A O 1 ATOM 2804 C CB . VAL A 1 354 ? 13.665 41.075 58.529 1.00 20.30 ? 395 VAL A CB 1 ATOM 2805 C CG1 . VAL A 1 354 ? 12.274 41.510 59.068 1.00 19.23 ? 395 VAL A CG1 1 ATOM 2806 C CG2 . VAL A 1 354 ? 14.261 42.212 57.625 1.00 21.22 ? 395 VAL A CG2 1 ATOM 2807 N N . HIS A 1 355 ? 14.002 38.538 60.330 1.00 21.08 ? 396 HIS A N 1 ATOM 2808 C CA . HIS A 1 355 ? 13.352 37.498 61.154 1.00 21.04 ? 396 HIS A CA 1 ATOM 2809 C C . HIS A 1 355 ? 13.910 37.517 62.562 1.00 23.11 ? 396 HIS A C 1 ATOM 2810 O O . HIS A 1 355 ? 13.155 37.497 63.554 1.00 23.66 ? 396 HIS A O 1 ATOM 2811 C CB . HIS A 1 355 ? 13.547 36.113 60.471 1.00 22.26 ? 396 HIS A CB 1 ATOM 2812 C CG . HIS A 1 355 ? 12.382 35.174 60.590 1.00 22.68 ? 396 HIS A CG 1 ATOM 2813 N ND1 . HIS A 1 355 ? 11.087 35.536 60.270 1.00 23.48 ? 396 HIS A ND1 1 ATOM 2814 C CD2 . HIS A 1 355 ? 12.327 33.861 60.947 1.00 26.25 ? 396 HIS A CD2 1 ATOM 2815 C CE1 . HIS A 1 355 ? 10.289 34.496 60.430 1.00 24.80 ? 396 HIS A CE1 1 ATOM 2816 N NE2 . HIS A 1 355 ? 11.020 33.461 60.814 1.00 26.94 ? 396 HIS A NE2 1 ATOM 2817 N N . GLU A 1 356 ? 15.229 37.630 62.679 1.00 22.57 ? 397 GLU A N 1 ATOM 2818 C CA . GLU A 1 356 ? 15.847 37.662 64.009 1.00 24.62 ? 397 GLU A CA 1 ATOM 2819 C C . GLU A 1 356 ? 15.572 38.949 64.758 1.00 23.89 ? 397 GLU A C 1 ATOM 2820 O O . GLU A 1 356 ? 15.455 38.952 65.979 1.00 25.47 ? 397 GLU A O 1 ATOM 2821 C CB . GLU A 1 356 ? 17.350 37.399 63.879 1.00 25.96 ? 397 GLU A CB 1 ATOM 2822 C CG . GLU A 1 356 ? 18.171 37.426 65.213 1.00 24.72 ? 397 GLU A CG 1 ATOM 2823 C CD . GLU A 1 356 ? 17.814 36.347 66.198 1.00 30.74 ? 397 GLU A CD 1 ATOM 2824 O OE1 . GLU A 1 356 ? 16.811 35.616 65.991 1.00 30.03 ? 397 GLU A OE1 1 ATOM 2825 O OE2 . GLU A 1 356 ? 18.551 36.210 67.212 1.00 30.43 ? 397 GLU A OE2 1 ATOM 2826 N N . ILE A 1 357 ? 15.440 40.057 64.026 1.00 22.42 ? 398 ILE A N 1 ATOM 2827 C CA . ILE A 1 357 ? 15.014 41.327 64.646 1.00 21.94 ? 398 ILE A CA 1 ATOM 2828 C C . ILE A 1 357 ? 13.602 41.251 65.219 1.00 22.65 ? 398 ILE A C 1 ATOM 2829 O O . ILE A 1 357 ? 13.357 41.652 66.378 1.00 23.10 ? 398 ILE A O 1 ATOM 2830 C CB . ILE A 1 357 ? 15.170 42.505 63.647 1.00 20.60 ? 398 ILE A CB 1 ATOM 2831 C CG1 . ILE A 1 357 ? 16.667 42.828 63.450 1.00 21.54 ? 398 ILE A CG1 1 ATOM 2832 C CG2 . ILE A 1 357 ? 14.406 43.761 64.166 1.00 20.85 ? 398 ILE A CG2 1 ATOM 2833 C CD1 . ILE A 1 357 ? 16.961 43.702 62.211 1.00 21.35 ? 398 ILE A CD1 1 ATOM 2834 N N . VAL A 1 358 ? 12.680 40.686 64.443 1.00 21.77 ? 399 VAL A N 1 ATOM 2835 C CA . VAL A 1 358 ? 11.305 40.455 64.947 1.00 23.78 ? 399 VAL A CA 1 ATOM 2836 C C . VAL A 1 358 ? 11.329 39.559 66.201 1.00 24.26 ? 399 VAL A C 1 ATOM 2837 O O . VAL A 1 358 ? 10.684 39.885 67.217 1.00 25.38 ? 399 VAL A O 1 ATOM 2838 C CB . VAL A 1 358 ? 10.398 39.821 63.872 1.00 23.00 ? 399 VAL A CB 1 ATOM 2839 C CG1 . VAL A 1 358 ? 9.005 39.526 64.457 1.00 23.66 ? 399 VAL A CG1 1 ATOM 2840 C CG2 . VAL A 1 358 ? 10.246 40.794 62.626 1.00 23.28 ? 399 VAL A CG2 1 ATOM 2841 N N . ARG A 1 359 ? 12.082 38.454 66.151 1.00 24.17 ? 400 ARG A N 1 ATOM 2842 C CA . ARG A 1 359 ? 12.201 37.548 67.300 1.00 25.35 ? 400 ARG A CA 1 ATOM 2843 C C . ARG A 1 359 ? 12.691 38.305 68.542 1.00 26.91 ? 400 ARG A C 1 ATOM 2844 O O . ARG A 1 359 ? 12.141 38.112 69.651 1.00 28.00 ? 400 ARG A O 1 ATOM 2845 C CB . ARG A 1 359 ? 13.140 36.368 66.985 1.00 24.27 ? 400 ARG A CB 1 ATOM 2846 C CG . ARG A 1 359 ? 12.949 35.176 67.978 1.00 26.26 ? 400 ARG A CG 1 ATOM 2847 C CD . ARG A 1 359 ? 14.137 34.178 67.926 1.00 27.98 ? 400 ARG A CD 1 ATOM 2848 N NE . ARG A 1 359 ? 15.386 34.868 68.241 1.00 29.93 ? 400 ARG A NE 1 ATOM 2849 C CZ . ARG A 1 359 ? 15.810 35.180 69.465 1.00 33.31 ? 400 ARG A CZ 1 ATOM 2850 N NH1 . ARG A 1 359 ? 16.961 35.817 69.617 1.00 32.36 ? 400 ARG A NH1 1 ATOM 2851 N NH2 . ARG A 1 359 ? 15.100 34.853 70.544 1.00 33.84 ? 400 ARG A NH2 1 ATOM 2852 N N . SER A 1 360 ? 13.697 39.165 68.364 1.00 26.78 ? 401 SER A N 1 ATOM 2853 C CA . SER A 1 360 ? 14.243 39.924 69.492 1.00 28.90 ? 401 SER A CA 1 ATOM 2854 C C . SER A 1 360 ? 13.253 40.945 70.052 1.00 28.76 ? 401 SER A C 1 ATOM 2855 O O . SER A 1 360 ? 13.068 41.002 71.282 1.00 29.32 ? 401 SER A O 1 ATOM 2856 C CB . SER A 1 360 ? 15.602 40.568 69.182 1.00 29.20 ? 401 SER A CB 1 ATOM 2857 O OG A SER A 1 360 ? 16.028 41.342 70.329 0.50 26.18 ? 401 SER A OG 1 ATOM 2858 O OG B SER A 1 360 ? 16.523 39.541 68.815 0.50 30.72 ? 401 SER A OG 1 ATOM 2859 N N . PHE A 1 361 ? 12.588 41.713 69.186 1.00 28.01 ? 402 PHE A N 1 ATOM 2860 C CA . PHE A 1 361 ? 11.573 42.648 69.676 1.00 28.01 ? 402 PHE A CA 1 ATOM 2861 C C . PHE A 1 361 ? 10.463 41.892 70.375 1.00 30.23 ? 402 PHE A C 1 ATOM 2862 O O . PHE A 1 361 ? 9.982 42.332 71.424 1.00 30.37 ? 402 PHE A O 1 ATOM 2863 C CB . PHE A 1 361 ? 10.980 43.510 68.524 1.00 26.11 ? 402 PHE A CB 1 ATOM 2864 C CG . PHE A 1 361 ? 11.797 44.719 68.167 1.00 26.22 ? 402 PHE A CG 1 ATOM 2865 C CD1 . PHE A 1 361 ? 11.963 45.767 69.091 1.00 27.12 ? 402 PHE A CD1 1 ATOM 2866 C CD2 . PHE A 1 361 ? 12.337 44.875 66.891 1.00 24.27 ? 402 PHE A CD2 1 ATOM 2867 C CE1 . PHE A 1 361 ? 12.678 46.910 68.765 1.00 26.15 ? 402 PHE A CE1 1 ATOM 2868 C CE2 . PHE A 1 361 ? 13.065 46.051 66.548 1.00 23.95 ? 402 PHE A CE2 1 ATOM 2869 C CZ . PHE A 1 361 ? 13.252 47.056 67.489 1.00 26.65 ? 402 PHE A CZ 1 ATOM 2870 N N . GLY A 1 362 ? 10.080 40.740 69.822 1.00 29.44 ? 403 GLY A N 1 ATOM 2871 C CA . GLY A 1 362 ? 9.030 39.911 70.417 1.00 30.80 ? 403 GLY A CA 1 ATOM 2872 C C . GLY A 1 362 ? 9.425 39.369 71.792 1.00 32.30 ? 403 GLY A C 1 ATOM 2873 O O . GLY A 1 362 ? 8.575 39.235 72.686 1.00 33.76 ? 403 GLY A O 1 ATOM 2874 N N . THR A 1 363 ? 10.709 39.103 72.000 1.00 33.04 ? 404 THR A N 1 ATOM 2875 C CA . THR A 1 363 ? 11.162 38.617 73.313 1.00 33.91 ? 404 THR A CA 1 ATOM 2876 C C . THR A 1 363 ? 10.954 39.692 74.373 1.00 34.63 ? 404 THR A C 1 ATOM 2877 O O . THR A 1 363 ? 10.492 39.384 75.488 1.00 36.54 ? 404 THR A O 1 ATOM 2878 C CB . THR A 1 363 ? 12.637 38.125 73.319 1.00 34.50 ? 404 THR A CB 1 ATOM 2879 O OG1 A THR A 1 363 ? 12.744 37.002 72.444 0.50 34.36 ? 404 THR A OG1 1 ATOM 2880 O OG1 B THR A 1 363 ? 13.551 39.230 73.294 0.50 34.65 ? 404 THR A OG1 1 ATOM 2881 C CG2 A THR A 1 363 ? 13.088 37.733 74.701 0.50 33.41 ? 404 THR A CG2 1 ATOM 2882 C CG2 B THR A 1 363 ? 12.915 37.185 72.171 0.50 34.17 ? 404 THR A CG2 1 ATOM 2883 N N . LEU A 1 364 ? 11.277 40.933 74.015 1.00 32.94 ? 405 LEU A N 1 ATOM 2884 C CA . LEU A 1 364 ? 11.061 42.056 74.922 1.00 33.38 ? 405 LEU A CA 1 ATOM 2885 C C . LEU A 1 364 ? 9.573 42.230 75.168 1.00 33.39 ? 405 LEU A C 1 ATOM 2886 O O . LEU A 1 364 ? 9.152 42.444 76.309 1.00 32.65 ? 405 LEU A O 1 ATOM 2887 C CB . LEU A 1 364 ? 11.664 43.373 74.368 1.00 33.64 ? 405 LEU A CB 1 ATOM 2888 C CG A LEU A 1 364 ? 13.177 43.449 74.131 0.50 34.13 ? 405 LEU A CG 1 ATOM 2889 C CG B LEU A 1 364 ? 13.134 43.662 74.701 0.50 34.17 ? 405 LEU A CG 1 ATOM 2890 C CD1 A LEU A 1 364 ? 13.522 44.782 73.487 0.50 34.26 ? 405 LEU A CD1 1 ATOM 2891 C CD1 B LEU A 1 364 ? 14.062 42.594 74.114 0.50 33.50 ? 405 LEU A CD1 1 ATOM 2892 C CD2 A LEU A 1 364 ? 13.949 43.247 75.442 0.50 35.64 ? 405 LEU A CD2 1 ATOM 2893 C CD2 B LEU A 1 364 ? 13.543 45.036 74.206 0.50 34.41 ? 405 LEU A CD2 1 ATOM 2894 N N . LYS A 1 365 ? 8.776 42.145 74.106 1.00 32.10 ? 406 LYS A N 1 ATOM 2895 C CA . LYS A 1 365 ? 7.320 42.262 74.232 1.00 33.27 ? 406 LYS A CA 1 ATOM 2896 C C . LYS A 1 365 ? 6.749 41.221 75.208 1.00 35.14 ? 406 LYS A C 1 ATOM 2897 O O . LYS A 1 365 ? 5.891 41.567 76.032 1.00 35.65 ? 406 LYS A O 1 ATOM 2898 C CB . LYS A 1 365 ? 6.617 42.181 72.865 1.00 33.74 ? 406 LYS A CB 1 ATOM 2899 C CG . LYS A 1 365 ? 5.095 42.260 73.001 1.00 35.84 ? 406 LYS A CG 1 ATOM 2900 C CD . LYS A 1 365 ? 4.408 42.390 71.677 1.00 42.05 ? 406 LYS A CD 1 ATOM 2901 C CE . LYS A 1 365 ? 2.904 42.219 71.847 1.00 43.85 ? 406 LYS A CE 1 ATOM 2902 N NZ . LYS A 1 365 ? 2.551 40.819 72.218 1.00 46.30 ? 406 LYS A NZ 1 ATOM 2903 N N . LYS A 1 366 ? 7.226 39.975 75.129 1.00 35.15 ? 407 LYS A N 1 ATOM 2904 C CA . LYS A 1 366 ? 6.707 38.920 76.030 1.00 37.44 ? 407 LYS A CA 1 ATOM 2905 C C . LYS A 1 366 ? 7.033 39.184 77.491 1.00 39.32 ? 407 LYS A C 1 ATOM 2906 O O . LYS A 1 366 ? 6.336 38.682 78.383 1.00 40.68 ? 407 LYS A O 1 ATOM 2907 C CB . LYS A 1 366 ? 7.157 37.531 75.582 1.00 37.85 ? 407 LYS A CB 1 ATOM 2908 C CG . LYS A 1 366 ? 6.426 37.059 74.321 1.00 39.47 ? 407 LYS A CG 1 ATOM 2909 C CD . LYS A 1 366 ? 7.044 35.791 73.759 1.00 42.68 ? 407 LYS A CD 1 ATOM 2910 C CE . LYS A 1 366 ? 6.317 35.357 72.500 1.00 41.90 ? 407 LYS A CE 1 ATOM 2911 N NZ . LYS A 1 366 ? 6.828 34.049 72.041 1.00 46.16 ? 407 LYS A NZ 1 ATOM 2912 N N . GLU A 1 367 ? 8.072 39.983 77.736 1.00 39.69 ? 408 GLU A N 1 ATOM 2913 C CA . GLU A 1 367 ? 8.444 40.404 79.104 1.00 42.09 ? 408 GLU A CA 1 ATOM 2914 C C . GLU A 1 367 ? 7.714 41.674 79.590 1.00 41.75 ? 408 GLU A C 1 ATOM 2915 O O . GLU A 1 367 ? 7.967 42.171 80.706 1.00 43.24 ? 408 GLU A O 1 ATOM 2916 C CB . GLU A 1 367 ? 9.957 40.627 79.210 1.00 42.58 ? 408 GLU A CB 1 ATOM 2917 C CG . GLU A 1 367 ? 10.815 39.403 78.924 1.00 48.14 ? 408 GLU A CG 1 ATOM 2918 C CD . GLU A 1 367 ? 12.316 39.666 79.081 1.00 54.56 ? 408 GLU A CD 1 ATOM 2919 O OE1 . GLU A 1 367 ? 12.978 38.872 79.778 1.00 59.50 ? 408 GLU A OE1 1 ATOM 2920 O OE2 . GLU A 1 367 ? 12.841 40.653 78.509 1.00 58.25 ? 408 GLU A OE2 1 ATOM 2921 N N . GLY A 1 368 ? 6.807 42.198 78.775 1.00 40.41 ? 409 GLY A N 1 ATOM 2922 C CA . GLY A 1 368 ? 5.993 43.349 79.168 1.00 39.92 ? 409 GLY A CA 1 ATOM 2923 C C . GLY A 1 368 ? 6.371 44.683 78.549 1.00 38.57 ? 409 GLY A C 1 ATOM 2924 O O . GLY A 1 368 ? 5.763 45.726 78.854 1.00 38.59 ? 409 GLY A O 1 ATOM 2925 N N . TRP A 1 369 ? 7.374 44.674 77.673 1.00 35.89 ? 410 TRP A N 1 ATOM 2926 C CA . TRP A 1 369 ? 7.835 45.920 77.072 1.00 34.32 ? 410 TRP A CA 1 ATOM 2927 C C . TRP A 1 369 ? 7.030 46.181 75.793 1.00 32.04 ? 410 TRP A C 1 ATOM 2928 O O . TRP A 1 369 ? 6.564 45.252 75.133 1.00 32.39 ? 410 TRP A O 1 ATOM 2929 C CB . TRP A 1 369 ? 9.322 45.805 76.740 1.00 34.77 ? 410 TRP A CB 1 ATOM 2930 C CG . TRP A 1 369 ? 9.935 46.919 75.888 1.00 35.46 ? 410 TRP A CG 1 ATOM 2931 C CD1 . TRP A 1 369 ? 10.487 48.088 76.344 1.00 37.14 ? 410 TRP A CD1 1 ATOM 2932 C CD2 . TRP A 1 369 ? 10.062 46.948 74.461 1.00 34.28 ? 410 TRP A CD2 1 ATOM 2933 N NE1 . TRP A 1 369 ? 10.976 48.821 75.297 1.00 34.37 ? 410 TRP A NE1 1 ATOM 2934 C CE2 . TRP A 1 369 ? 10.714 48.159 74.124 1.00 34.85 ? 410 TRP A CE2 1 ATOM 2935 C CE3 . TRP A 1 369 ? 9.693 46.066 73.438 1.00 34.64 ? 410 TRP A CE3 1 ATOM 2936 C CZ2 . TRP A 1 369 ? 11.025 48.506 72.803 1.00 31.17 ? 410 TRP A CZ2 1 ATOM 2937 C CZ3 . TRP A 1 369 ? 9.982 46.409 72.126 1.00 30.41 ? 410 TRP A CZ3 1 ATOM 2938 C CH2 . TRP A 1 369 ? 10.635 47.653 71.824 1.00 30.40 ? 410 TRP A CH2 1 ATOM 2939 N N . ARG A 1 370 ? 6.831 47.444 75.484 1.00 30.16 ? 411 ARG A N 1 ATOM 2940 C CA . ARG A 1 370 ? 6.418 47.828 74.101 1.00 28.86 ? 411 ARG A CA 1 ATOM 2941 C C . ARG A 1 370 ? 7.209 49.050 73.727 1.00 27.13 ? 411 ARG A C 1 ATOM 2942 O O . ARG A 1 370 ? 7.557 49.854 74.598 1.00 28.01 ? 411 ARG A O 1 ATOM 2943 C CB . ARG A 1 370 ? 4.948 48.233 74.046 1.00 30.31 ? 411 ARG A CB 1 ATOM 2944 C CG . ARG A 1 370 ? 3.963 47.101 74.063 1.00 31.44 ? 411 ARG A CG 1 ATOM 2945 C CD . ARG A 1 370 ? 2.506 47.650 74.002 1.00 33.36 ? 411 ARG A CD 1 ATOM 2946 N NE . ARG A 1 370 ? 1.672 46.470 73.948 1.00 35.25 ? 411 ARG A NE 1 ATOM 2947 C CZ . ARG A 1 370 ? 1.487 45.737 72.840 1.00 31.72 ? 411 ARG A CZ 1 ATOM 2948 N NH1 . ARG A 1 370 ? 1.994 46.109 71.629 1.00 26.82 ? 411 ARG A NH1 1 ATOM 2949 N NH2 . ARG A 1 370 ? 0.763 44.627 72.948 1.00 34.06 ? 411 ARG A NH2 1 ATOM 2950 N N . PRO A 1 371 ? 7.456 49.232 72.422 1.00 25.92 ? 412 PRO A N 1 ATOM 2951 C CA . PRO A 1 371 ? 8.133 50.430 71.966 1.00 25.10 ? 412 PRO A CA 1 ATOM 2952 C C . PRO A 1 371 ? 7.230 51.633 72.140 1.00 23.78 ? 412 PRO A C 1 ATOM 2953 O O . PRO A 1 371 ? 6.020 51.497 72.246 1.00 25.42 ? 412 PRO A O 1 ATOM 2954 C CB . PRO A 1 371 ? 8.369 50.172 70.452 1.00 24.88 ? 412 PRO A CB 1 ATOM 2955 C CG . PRO A 1 371 ? 7.269 49.193 70.054 1.00 24.76 ? 412 PRO A CG 1 ATOM 2956 C CD . PRO A 1 371 ? 7.000 48.351 71.327 1.00 25.40 ? 412 PRO A CD 1 ATOM 2957 N N . ARG A 1 372 ? 7.814 52.804 72.164 1.00 23.19 ? 413 ARG A N 1 ATOM 2958 C CA . ARG A 1 372 ? 7.022 54.028 72.286 1.00 24.15 ? 413 ARG A CA 1 ATOM 2959 C C . ARG A 1 372 ? 6.063 54.206 71.082 1.00 23.47 ? 413 ARG A C 1 ATOM 2960 O O . ARG A 1 372 ? 4.845 54.429 71.222 1.00 24.51 ? 413 ARG A O 1 ATOM 2961 C CB . ARG A 1 372 ? 7.943 55.224 72.388 1.00 24.34 ? 413 ARG A CB 1 ATOM 2962 C CG . ARG A 1 372 ? 7.183 56.552 72.501 1.00 26.67 ? 413 ARG A CG 1 ATOM 2963 C CD . ARG A 1 372 ? 8.117 57.734 72.419 1.00 29.39 ? 413 ARG A CD 1 ATOM 2964 N NE . ARG A 1 372 ? 7.332 58.973 72.376 1.00 32.40 ? 413 ARG A NE 1 ATOM 2965 C CZ . ARG A 1 372 ? 6.891 59.638 73.447 1.00 36.14 ? 413 ARG A CZ 1 ATOM 2966 N NH1 . ARG A 1 372 ? 7.180 59.218 74.677 1.00 30.56 ? 413 ARG A NH1 1 ATOM 2967 N NH2 . ARG A 1 372 ? 6.167 60.741 73.281 1.00 32.53 ? 413 ARG A NH2 1 ATOM 2968 N N . ARG A 1 373 ? 6.643 54.069 69.904 1.00 21.16 ? 414 ARG A N 1 ATOM 2969 C CA . ARG A 1 373 ? 5.874 54.176 68.648 1.00 20.42 ? 414 ARG A CA 1 ATOM 2970 C C . ARG A 1 373 ? 5.639 52.776 68.077 1.00 21.71 ? 414 ARG A C 1 ATOM 2971 O O . ARG A 1 373 ? 6.346 51.812 68.414 1.00 21.52 ? 414 ARG A O 1 ATOM 2972 C CB . ARG A 1 373 ? 6.652 55.005 67.611 1.00 20.22 ? 414 ARG A CB 1 ATOM 2973 C CG . ARG A 1 373 ? 7.121 56.393 68.118 1.00 21.74 ? 414 ARG A CG 1 ATOM 2974 C CD . ARG A 1 373 ? 7.888 57.237 67.049 1.00 22.40 ? 414 ARG A CD 1 ATOM 2975 N NE . ARG A 1 373 ? 8.124 58.508 67.723 1.00 21.20 ? 414 ARG A NE 1 ATOM 2976 C CZ . ARG A 1 373 ? 9.081 58.737 68.619 1.00 21.95 ? 414 ARG A CZ 1 ATOM 2977 N NH1 . ARG A 1 373 ? 10.016 57.837 68.846 1.00 20.98 ? 414 ARG A NH1 1 ATOM 2978 N NH2 . ARG A 1 373 ? 9.092 59.908 69.294 1.00 22.46 ? 414 ARG A NH2 1 ATOM 2979 N N . THR A 1 374 ? 4.626 52.670 67.219 1.00 20.06 ? 415 THR A N 1 ATOM 2980 C CA . THR A 1 374 ? 4.356 51.407 66.507 1.00 20.45 ? 415 THR A CA 1 ATOM 2981 C C . THR A 1 374 ? 5.484 51.045 65.536 1.00 20.04 ? 415 THR A C 1 ATOM 2982 O O . THR A 1 374 ? 5.982 51.890 64.788 1.00 20.01 ? 415 THR A O 1 ATOM 2983 C CB . THR A 1 374 ? 3.001 51.541 65.749 1.00 19.74 ? 415 THR A CB 1 ATOM 2984 O OG1 . THR A 1 374 ? 1.971 51.584 66.736 1.00 20.62 ? 415 THR A OG1 1 ATOM 2985 C CG2 . THR A 1 374 ? 2.723 50.345 64.811 1.00 19.86 ? 415 THR A CG2 1 ATOM 2986 N N . ILE A 1 375 ? 5.863 49.773 65.563 1.00 18.27 ? 416 ILE A N 1 ATOM 2987 C CA . ILE A 1 375 ? 6.783 49.238 64.564 1.00 18.68 ? 416 ILE A CA 1 ATOM 2988 C C . ILE A 1 375 ? 6.030 48.329 63.628 1.00 18.69 ? 416 ILE A C 1 ATOM 2989 O O . ILE A 1 375 ? 5.271 47.468 64.080 1.00 20.75 ? 416 ILE A O 1 ATOM 2990 C CB . ILE A 1 375 ? 7.988 48.478 65.199 1.00 18.39 ? 416 ILE A CB 1 ATOM 2991 C CG1 . ILE A 1 375 ? 8.726 49.372 66.202 1.00 21.37 ? 416 ILE A CG1 1 ATOM 2992 C CG2 . ILE A 1 375 ? 8.899 48.002 64.058 1.00 19.20 ? 416 ILE A CG2 1 ATOM 2993 C CD1 . ILE A 1 375 ? 9.765 48.586 67.067 1.00 21.20 ? 416 ILE A CD1 1 ATOM 2994 N N . LEU A 1 376 ? 6.203 48.555 62.307 1.00 18.10 ? 417 LEU A N 1 ATOM 2995 C CA . LEU A 1 376 ? 5.588 47.662 61.310 1.00 19.26 ? 417 LEU A CA 1 ATOM 2996 C C . LEU A 1 376 ? 6.757 46.907 60.690 1.00 19.25 ? 417 LEU A C 1 ATOM 2997 O O . LEU A 1 376 ? 7.805 47.517 60.355 1.00 19.80 ? 417 LEU A O 1 ATOM 2998 C CB . LEU A 1 376 ? 4.902 48.482 60.210 1.00 18.51 ? 417 LEU A CB 1 ATOM 2999 C CG . LEU A 1 376 ? 3.768 49.384 60.731 1.00 21.33 ? 417 LEU A CG 1 ATOM 3000 C CD1 . LEU A 1 376 ? 3.087 50.122 59.540 1.00 21.02 ? 417 LEU A CD1 1 ATOM 3001 C CD2 . LEU A 1 376 ? 2.737 48.575 61.509 1.00 22.14 ? 417 LEU A CD2 1 ATOM 3002 N N . PHE A 1 377 ? 6.565 45.608 60.478 1.00 17.69 ? 418 PHE A N 1 ATOM 3003 C CA . PHE A 1 377 ? 7.576 44.765 59.851 1.00 17.55 ? 418 PHE A CA 1 ATOM 3004 C C . PHE A 1 377 ? 6.967 44.218 58.546 1.00 17.92 ? 418 PHE A C 1 ATOM 3005 O O . PHE A 1 377 ? 5.797 43.822 58.538 1.00 18.63 ? 418 PHE A O 1 ATOM 3006 C CB . PHE A 1 377 ? 7.891 43.584 60.762 1.00 18.01 ? 418 PHE A CB 1 ATOM 3007 C CG . PHE A 1 377 ? 8.465 43.976 62.082 1.00 19.41 ? 418 PHE A CG 1 ATOM 3008 C CD1 . PHE A 1 377 ? 9.833 44.243 62.217 1.00 21.22 ? 418 PHE A CD1 1 ATOM 3009 C CD2 . PHE A 1 377 ? 7.614 44.115 63.192 1.00 22.52 ? 418 PHE A CD2 1 ATOM 3010 C CE1 . PHE A 1 377 ? 10.367 44.608 63.502 1.00 21.63 ? 418 PHE A CE1 1 ATOM 3011 C CE2 . PHE A 1 377 ? 8.135 44.496 64.438 1.00 23.97 ? 418 PHE A CE2 1 ATOM 3012 C CZ . PHE A 1 377 ? 9.503 44.724 64.593 1.00 22.08 ? 418 PHE A CZ 1 ATOM 3013 N N . ALA A 1 378 ? 7.727 44.230 57.454 1.00 18.84 ? 419 ALA A N 1 ATOM 3014 C CA . ALA A 1 378 ? 7.153 43.787 56.190 1.00 17.39 ? 419 ALA A CA 1 ATOM 3015 C C . ALA A 1 378 ? 8.099 42.824 55.509 1.00 17.78 ? 419 ALA A C 1 ATOM 3016 O O . ALA A 1 378 ? 9.315 43.037 55.475 1.00 19.25 ? 419 ALA A O 1 ATOM 3017 C CB . ALA A 1 378 ? 6.922 45.006 55.268 1.00 18.42 ? 419 ALA A CB 1 ATOM 3018 N N . SER A 1 379 ? 7.487 41.770 54.966 1.00 17.37 ? 420 SER A N 1 ATOM 3019 C CA . SER A 1 379 ? 8.138 40.843 54.053 1.00 16.68 ? 420 SER A CA 1 ATOM 3020 C C . SER A 1 379 ? 7.491 41.089 52.674 1.00 16.73 ? 420 SER A C 1 ATOM 3021 O O . SER A 1 379 ? 6.371 40.636 52.432 1.00 17.73 ? 420 SER A O 1 ATOM 3022 C CB . SER A 1 379 ? 7.845 39.431 54.558 1.00 17.78 ? 420 SER A CB 1 ATOM 3023 O OG . SER A 1 379 ? 8.355 38.453 53.633 1.00 18.29 ? 420 SER A OG 1 ATOM 3024 N N . TRP A 1 380 ? 8.162 41.848 51.819 1.00 16.27 ? 421 TRP A N 1 ATOM 3025 C CA . TRP A 1 380 ? 7.542 42.253 50.542 1.00 15.65 ? 421 TRP A CA 1 ATOM 3026 C C . TRP A 1 380 ? 7.679 41.170 49.485 1.00 17.68 ? 421 TRP A C 1 ATOM 3027 O O . TRP A 1 380 ? 8.648 40.410 49.451 1.00 17.99 ? 421 TRP A O 1 ATOM 3028 C CB . TRP A 1 380 ? 8.288 43.467 49.968 1.00 15.69 ? 421 TRP A CB 1 ATOM 3029 C CG . TRP A 1 380 ? 8.353 44.706 50.864 1.00 15.74 ? 421 TRP A CG 1 ATOM 3030 C CD1 . TRP A 1 380 ? 9.479 45.349 51.239 1.00 16.35 ? 421 TRP A CD1 1 ATOM 3031 C CD2 . TRP A 1 380 ? 7.231 45.434 51.434 1.00 15.06 ? 421 TRP A CD2 1 ATOM 3032 N NE1 . TRP A 1 380 ? 9.158 46.471 52.012 1.00 15.08 ? 421 TRP A NE1 1 ATOM 3033 C CE2 . TRP A 1 380 ? 7.784 46.526 52.151 1.00 15.81 ? 421 TRP A CE2 1 ATOM 3034 C CE3 . TRP A 1 380 ? 5.836 45.247 51.422 1.00 16.27 ? 421 TRP A CE3 1 ATOM 3035 C CZ2 . TRP A 1 380 ? 6.989 47.447 52.846 1.00 16.85 ? 421 TRP A CZ2 1 ATOM 3036 C CZ3 . TRP A 1 380 ? 5.015 46.169 52.100 1.00 16.74 ? 421 TRP A CZ3 1 ATOM 3037 C CH2 . TRP A 1 380 ? 5.611 47.255 52.824 1.00 17.21 ? 421 TRP A CH2 1 ATOM 3038 N N . ASP A 1 381 ? 6.705 41.163 48.584 1.00 16.77 ? 422 ASP A N 1 ATOM 3039 C CA . ASP A 1 381 ? 6.770 40.231 47.458 1.00 16.03 ? 422 ASP A CA 1 ATOM 3040 C C . ASP A 1 381 ? 7.069 41.015 46.182 1.00 16.87 ? 422 ASP A C 1 ATOM 3041 O O . ASP A 1 381 ? 6.916 42.244 46.108 1.00 17.49 ? 422 ASP A O 1 ATOM 3042 C CB . ASP A 1 381 ? 5.403 39.517 47.328 1.00 17.05 ? 422 ASP A CB 1 ATOM 3043 C CG . ASP A 1 381 ? 5.487 38.155 46.591 1.00 18.35 ? 422 ASP A CG 1 ATOM 3044 O OD1 . ASP A 1 381 ? 6.519 37.784 46.003 1.00 19.24 ? 422 ASP A OD1 1 ATOM 3045 O OD2 . ASP A 1 381 ? 4.473 37.431 46.631 1.00 18.69 ? 422 ASP A OD2 1 ATOM 3046 N N . ALA A 1 382 ? 7.506 40.262 45.179 1.00 16.29 ? 423 ALA A N 1 ATOM 3047 C CA . ALA A 1 382 ? 7.702 40.761 43.810 1.00 16.63 ? 423 ALA A CA 1 ATOM 3048 C C . ALA A 1 382 ? 8.597 42.001 43.742 1.00 15.38 ? 423 ALA A C 1 ATOM 3049 O O . ALA A 1 382 ? 8.450 42.852 42.853 1.00 16.11 ? 423 ALA A O 1 ATOM 3050 C CB . ALA A 1 382 ? 6.329 41.004 43.112 1.00 16.64 ? 423 ALA A CB 1 ATOM 3051 N N . GLU A 1 383 ? 9.589 42.088 44.640 1.00 15.56 ? 424 GLU A N 1 ATOM 3052 C CA . GLU A 1 383 ? 10.555 43.197 44.514 1.00 16.68 ? 424 GLU A CA 1 ATOM 3053 C C . GLU A 1 383 ? 11.326 43.014 43.236 1.00 16.22 ? 424 GLU A C 1 ATOM 3054 O O . GLU A 1 383 ? 11.649 44.012 42.546 1.00 16.56 ? 424 GLU A O 1 ATOM 3055 C CB . GLU A 1 383 ? 11.496 43.169 45.734 1.00 14.76 ? 424 GLU A CB 1 ATOM 3056 C CG . GLU A 1 383 ? 12.492 44.334 45.785 1.00 16.41 ? 424 GLU A CG 1 ATOM 3057 C CD . GLU A 1 383 ? 13.769 44.115 44.972 1.00 18.82 ? 424 GLU A CD 1 ATOM 3058 O OE1 . GLU A 1 383 ? 14.028 43.004 44.407 1.00 18.11 ? 424 GLU A OE1 1 ATOM 3059 O OE2 . GLU A 1 383 ? 14.567 45.114 44.901 1.00 19.54 ? 424 GLU A OE2 1 ATOM 3060 N N . GLU A 1 384 ? 11.611 41.755 42.869 1.00 16.25 ? 425 GLU A N 1 ATOM 3061 C CA . GLU A 1 384 ? 12.495 41.534 41.726 1.00 17.32 ? 425 GLU A CA 1 ATOM 3062 C C . GLU A 1 384 ? 11.823 41.931 40.410 1.00 16.37 ? 425 GLU A C 1 ATOM 3063 O O . GLU A 1 384 ? 12.502 42.113 39.394 1.00 18.42 ? 425 GLU A O 1 ATOM 3064 C CB . GLU A 1 384 ? 12.942 40.072 41.678 1.00 16.51 ? 425 GLU A CB 1 ATOM 3065 C CG . GLU A 1 384 ? 13.829 39.618 42.846 1.00 18.32 ? 425 GLU A CG 1 ATOM 3066 C CD . GLU A 1 384 ? 15.250 40.265 42.873 1.00 17.29 ? 425 GLU A CD 1 ATOM 3067 O OE1 . GLU A 1 384 ? 15.528 41.225 42.124 1.00 17.91 ? 425 GLU A OE1 1 ATOM 3068 O OE2 . GLU A 1 384 ? 16.083 39.870 43.712 1.00 18.65 ? 425 GLU A OE2 1 ATOM 3069 N N . PHE A 1 385 ? 10.497 42.063 40.439 1.00 16.60 ? 426 PHE A N 1 ATOM 3070 C CA . PHE A 1 385 ? 9.782 42.424 39.223 1.00 16.43 ? 426 PHE A CA 1 ATOM 3071 C C . PHE A 1 385 ? 9.409 43.889 39.196 1.00 17.80 ? 426 PHE A C 1 ATOM 3072 O O . PHE A 1 385 ? 8.527 44.265 38.413 1.00 19.27 ? 426 PHE A O 1 ATOM 3073 C CB . PHE A 1 385 ? 8.504 41.566 39.118 1.00 17.06 ? 426 PHE A CB 1 ATOM 3074 C CG . PHE A 1 385 ? 8.772 40.132 38.793 1.00 17.06 ? 426 PHE A CG 1 ATOM 3075 C CD1 . PHE A 1 385 ? 8.687 39.722 37.462 1.00 18.39 ? 426 PHE A CD1 1 ATOM 3076 C CD2 . PHE A 1 385 ? 9.132 39.193 39.786 1.00 18.15 ? 426 PHE A CD2 1 ATOM 3077 C CE1 . PHE A 1 385 ? 8.946 38.353 37.079 1.00 18.91 ? 426 PHE A CE1 1 ATOM 3078 C CE2 . PHE A 1 385 ? 9.403 37.835 39.447 1.00 20.21 ? 426 PHE A CE2 1 ATOM 3079 C CZ . PHE A 1 385 ? 9.290 37.408 38.077 1.00 20.45 ? 426 PHE A CZ 1 ATOM 3080 N N . GLY A 1 386 ? 10.089 44.720 40.019 1.00 17.44 ? 427 GLY A N 1 ATOM 3081 C CA . GLY A 1 386 ? 9.844 46.168 39.940 1.00 17.15 ? 427 GLY A CA 1 ATOM 3082 C C . GLY A 1 386 ? 9.292 46.781 41.214 1.00 16.63 ? 427 GLY A C 1 ATOM 3083 O O . GLY A 1 386 ? 8.585 47.800 41.151 1.00 17.13 ? 427 GLY A O 1 ATOM 3084 N N . LEU A 1 387 ? 9.703 46.249 42.357 1.00 15.39 ? 428 LEU A N 1 ATOM 3085 C CA . LEU A 1 387 ? 9.281 46.819 43.660 1.00 15.50 ? 428 LEU A CA 1 ATOM 3086 C C . LEU A 1 387 ? 7.741 46.741 43.784 1.00 15.45 ? 428 LEU A C 1 ATOM 3087 O O . LEU A 1 387 ? 7.092 47.616 44.376 1.00 15.57 ? 428 LEU A O 1 ATOM 3088 C CB . LEU A 1 387 ? 9.774 48.288 43.839 1.00 16.77 ? 428 LEU A CB 1 ATOM 3089 C CG . LEU A 1 387 ? 11.186 48.582 43.318 1.00 15.50 ? 428 LEU A CG 1 ATOM 3090 C CD1 . LEU A 1 387 ? 11.515 50.085 43.582 1.00 15.54 ? 428 LEU A CD1 1 ATOM 3091 C CD2 . LEU A 1 387 ? 12.202 47.651 43.998 1.00 15.27 ? 428 LEU A CD2 1 ATOM 3092 N N . LEU A 1 388 ? 7.152 45.660 43.253 1.00 15.57 ? 429 LEU A N 1 ATOM 3093 C CA . LEU A 1 388 ? 5.686 45.673 43.090 1.00 15.39 ? 429 LEU A CA 1 ATOM 3094 C C . LEU A 1 388 ? 4.943 45.557 44.427 1.00 15.73 ? 429 LEU A C 1 ATOM 3095 O O . LEU A 1 388 ? 3.949 46.250 44.624 1.00 17.39 ? 429 LEU A O 1 ATOM 3096 C CB . LEU A 1 388 ? 5.247 44.596 42.106 1.00 16.39 ? 429 LEU A CB 1 ATOM 3097 C CG . LEU A 1 388 ? 5.983 44.681 40.758 1.00 17.14 ? 429 LEU A CG 1 ATOM 3098 C CD1 . LEU A 1 388 ? 5.320 43.575 39.846 1.00 17.97 ? 429 LEU A CD1 1 ATOM 3099 C CD2 . LEU A 1 388 ? 5.816 46.033 40.011 1.00 17.94 ? 429 LEU A CD2 1 ATOM 3100 N N . GLY A 1 389 ? 5.384 44.676 45.315 1.00 15.70 ? 430 GLY A N 1 ATOM 3101 C CA . GLY A 1 389 ? 4.647 44.445 46.579 1.00 15.41 ? 430 GLY A CA 1 ATOM 3102 C C . GLY A 1 389 ? 4.705 45.673 47.502 1.00 15.46 ? 430 GLY A C 1 ATOM 3103 O O . GLY A 1 389 ? 3.674 46.079 48.060 1.00 16.37 ? 430 GLY A O 1 ATOM 3104 N N . SER A 1 390 ? 5.883 46.260 47.656 1.00 14.82 ? 431 SER A N 1 ATOM 3105 C CA . SER A 1 390 ? 6.008 47.430 48.548 1.00 14.58 ? 431 SER A CA 1 ATOM 3106 C C . SER A 1 390 ? 5.207 48.588 47.940 1.00 14.52 ? 431 SER A C 1 ATOM 3107 O O . SER A 1 390 ? 4.535 49.313 48.651 1.00 14.87 ? 431 SER A O 1 ATOM 3108 C CB . SER A 1 390 ? 7.497 47.804 48.697 1.00 13.92 ? 431 SER A CB 1 ATOM 3109 O OG . SER A 1 390 ? 8.105 48.149 47.439 1.00 15.72 ? 431 SER A OG 1 ATOM 3110 N N . THR A 1 391 ? 5.318 48.757 46.633 1.00 14.17 ? 432 THR A N 1 ATOM 3111 C CA . THR A 1 391 ? 4.640 49.914 46.013 1.00 14.70 ? 432 THR A CA 1 ATOM 3112 C C . THR A 1 391 ? 3.133 49.773 46.040 1.00 14.71 ? 432 THR A C 1 ATOM 3113 O O . THR A 1 391 ? 2.441 50.754 46.364 1.00 14.74 ? 432 THR A O 1 ATOM 3114 C CB . THR A 1 391 ? 5.143 50.127 44.548 1.00 14.80 ? 432 THR A CB 1 ATOM 3115 O OG1 . THR A 1 391 ? 6.568 50.269 44.576 1.00 16.14 ? 432 THR A OG1 1 ATOM 3116 C CG2 . THR A 1 391 ? 4.542 51.429 43.960 1.00 16.89 ? 432 THR A CG2 1 ATOM 3117 N N . GLU A 1 392 ? 2.588 48.582 45.770 1.00 14.51 ? 433 GLU A N 1 ATOM 3118 C CA . GLU A 1 392 ? 1.117 48.425 45.836 1.00 15.21 ? 433 GLU A CA 1 ATOM 3119 C C . GLU A 1 392 ? 0.605 48.649 47.271 1.00 15.06 ? 433 GLU A C 1 ATOM 3120 O O . GLU A 1 392 ? -0.417 49.308 47.459 1.00 15.91 ? 433 GLU A O 1 ATOM 3121 C CB . GLU A 1 392 ? 0.649 47.037 45.327 1.00 16.45 ? 433 GLU A CB 1 ATOM 3122 C CG . GLU A 1 392 ? 0.980 46.847 43.827 1.00 17.14 ? 433 GLU A CG 1 ATOM 3123 C CD . GLU A 1 392 ? 0.379 47.954 42.972 1.00 17.78 ? 433 GLU A CD 1 ATOM 3124 O OE1 . GLU A 1 392 ? -0.850 48.205 43.108 1.00 17.12 ? 433 GLU A OE1 1 ATOM 3125 O OE2 . GLU A 1 392 ? 1.087 48.595 42.203 1.00 17.77 ? 433 GLU A OE2 1 ATOM 3126 N N . TRP A 1 393 ? 1.340 48.133 48.252 1.00 15.64 ? 434 TRP A N 1 ATOM 3127 C CA . TRP A 1 393 ? 0.918 48.325 49.653 1.00 15.20 ? 434 TRP A CA 1 ATOM 3128 C C . TRP A 1 393 ? 0.995 49.812 50.039 1.00 16.47 ? 434 TRP A C 1 ATOM 3129 O O . TRP A 1 393 ? 0.081 50.308 50.703 1.00 17.18 ? 434 TRP A O 1 ATOM 3130 C CB . TRP A 1 393 ? 1.772 47.458 50.545 1.00 17.41 ? 434 TRP A CB 1 ATOM 3131 C CG . TRP A 1 393 ? 1.360 47.506 51.992 1.00 14.94 ? 434 TRP A CG 1 ATOM 3132 C CD1 . TRP A 1 393 ? 0.406 46.706 52.609 1.00 17.50 ? 434 TRP A CD1 1 ATOM 3133 C CD2 . TRP A 1 393 ? 1.912 48.369 53.013 1.00 18.10 ? 434 TRP A CD2 1 ATOM 3134 N NE1 . TRP A 1 393 ? 0.347 47.046 53.968 1.00 18.92 ? 434 TRP A NE1 1 ATOM 3135 C CE2 . TRP A 1 393 ? 1.257 48.044 54.227 1.00 18.68 ? 434 TRP A CE2 1 ATOM 3136 C CE3 . TRP A 1 393 ? 2.905 49.364 53.011 1.00 17.25 ? 434 TRP A CE3 1 ATOM 3137 C CZ2 . TRP A 1 393 ? 1.557 48.700 55.453 1.00 20.14 ? 434 TRP A CZ2 1 ATOM 3138 C CZ3 . TRP A 1 393 ? 3.216 50.047 54.233 1.00 19.13 ? 434 TRP A CZ3 1 ATOM 3139 C CH2 . TRP A 1 393 ? 2.536 49.689 55.440 1.00 19.39 ? 434 TRP A CH2 1 ATOM 3140 N N . ALA A 1 394 ? 2.061 50.497 49.611 1.00 16.00 ? 435 ALA A N 1 ATOM 3141 C CA . ALA A 1 394 ? 2.145 51.935 49.894 1.00 15.06 ? 435 ALA A CA 1 ATOM 3142 C C . ALA A 1 394 ? 1.044 52.697 49.170 1.00 14.95 ? 435 ALA A C 1 ATOM 3143 O O . ALA A 1 394 ? 0.496 53.665 49.711 1.00 16.32 ? 435 ALA A O 1 ATOM 3144 C CB . ALA A 1 394 ? 3.530 52.481 49.545 1.00 16.32 ? 435 ALA A CB 1 ATOM 3145 N N . GLU A 1 395 ? 0.693 52.289 47.947 1.00 15.38 ? 436 GLU A N 1 ATOM 3146 C CA . GLU A 1 395 ? -0.441 52.945 47.282 1.00 14.30 ? 436 GLU A CA 1 ATOM 3147 C C . GLU A 1 395 ? -1.755 52.746 48.050 1.00 16.79 ? 436 GLU A C 1 ATOM 3148 O O . GLU A 1 395 ? -2.582 53.690 48.178 1.00 17.66 ? 436 GLU A O 1 ATOM 3149 C CB . GLU A 1 395 ? -0.596 52.453 45.826 1.00 16.02 ? 436 GLU A CB 1 ATOM 3150 C CG . GLU A 1 395 ? 0.554 53.004 44.958 1.00 16.16 ? 436 GLU A CG 1 ATOM 3151 C CD . GLU A 1 395 ? 0.405 52.643 43.467 1.00 19.11 ? 436 GLU A CD 1 ATOM 3152 O OE1 . GLU A 1 395 ? 0.796 53.483 42.630 1.00 17.88 ? 436 GLU A OE1 1 ATOM 3153 O OE2 . GLU A 1 395 ? -0.147 51.548 43.177 1.00 18.83 ? 436 GLU A OE2 1 ATOM 3154 N N . GLU A 1 396 ? -1.959 51.517 48.522 1.00 16.33 ? 437 GLU A N 1 ATOM 3155 C CA . GLU A 1 396 ? -3.158 51.241 49.304 1.00 16.78 ? 437 GLU A CA 1 ATOM 3156 C C . GLU A 1 396 ? -3.209 52.106 50.580 1.00 16.80 ? 437 GLU A C 1 ATOM 3157 O O . GLU A 1 396 ? -4.284 52.614 50.953 1.00 17.42 ? 437 GLU A O 1 ATOM 3158 C CB . GLU A 1 396 ? -3.130 49.770 49.684 1.00 18.21 ? 437 GLU A CB 1 ATOM 3159 C CG . GLU A 1 396 ? -4.452 49.319 50.354 1.00 21.89 ? 437 GLU A CG 1 ATOM 3160 C CD . GLU A 1 396 ? -4.664 47.831 50.007 1.00 31.36 ? 437 GLU A CD 1 ATOM 3161 O OE1 . GLU A 1 396 ? -3.929 47.050 50.550 1.00 30.33 ? 437 GLU A OE1 1 ATOM 3162 O OE2 . GLU A 1 396 ? -5.495 47.457 49.146 1.00 41.98 ? 437 GLU A OE2 1 ATOM 3163 N N . ASN A 1 397 ? -2.070 52.262 51.233 1.00 15.41 ? 438 ASN A N 1 ATOM 3164 C CA . ASN A 1 397 ? -2.039 52.844 52.591 1.00 15.76 ? 438 ASN A CA 1 ATOM 3165 C C . ASN A 1 397 ? -1.420 54.243 52.623 1.00 15.74 ? 438 ASN A C 1 ATOM 3166 O O . ASN A 1 397 ? -1.031 54.737 53.682 1.00 16.40 ? 438 ASN A O 1 ATOM 3167 C CB . ASN A 1 397 ? -1.247 51.877 53.499 1.00 16.39 ? 438 ASN A CB 1 ATOM 3168 C CG . ASN A 1 397 ? -2.004 50.613 53.713 1.00 18.81 ? 438 ASN A CG 1 ATOM 3169 O OD1 . ASN A 1 397 ? -3.073 50.634 54.343 1.00 23.06 ? 438 ASN A OD1 1 ATOM 3170 N ND2 . ASN A 1 397 ? -1.521 49.500 53.132 1.00 18.66 ? 438 ASN A ND2 1 ATOM 3171 N N . SER A 1 398 ? -1.364 54.908 51.449 1.00 15.89 ? 439 SER A N 1 ATOM 3172 C CA . SER A 1 398 ? -0.618 56.168 51.350 1.00 16.01 ? 439 SER A CA 1 ATOM 3173 C C . SER A 1 398 ? -1.085 57.232 52.350 1.00 16.84 ? 439 SER A C 1 ATOM 3174 O O . SER A 1 398 ? -0.264 58.008 52.840 1.00 17.55 ? 439 SER A O 1 ATOM 3175 C CB . SER A 1 398 ? -0.736 56.754 49.889 1.00 16.99 ? 439 SER A CB 1 ATOM 3176 O OG . SER A 1 398 ? -2.099 56.982 49.572 1.00 18.38 ? 439 SER A OG 1 ATOM 3177 N N . ARG A 1 399 ? -2.387 57.299 52.626 1.00 15.98 ? 440 ARG A N 1 ATOM 3178 C CA . ARG A 1 399 ? -2.877 58.316 53.551 1.00 15.95 ? 440 ARG A CA 1 ATOM 3179 C C . ARG A 1 399 ? -2.409 58.044 54.962 1.00 16.57 ? 440 ARG A C 1 ATOM 3180 O O . ARG A 1 399 ? -2.076 59.006 55.701 1.00 17.48 ? 440 ARG A O 1 ATOM 3181 C CB . ARG A 1 399 ? -4.400 58.345 53.548 1.00 17.20 ? 440 ARG A CB 1 ATOM 3182 C CG . ARG A 1 399 ? -4.903 58.911 52.218 1.00 20.20 ? 440 ARG A CG 1 ATOM 3183 C CD . ARG A 1 399 ? -6.242 58.308 51.821 1.00 23.95 ? 440 ARG A CD 1 ATOM 3184 N NE . ARG A 1 399 ? -6.625 58.805 50.466 1.00 20.99 ? 440 ARG A NE 1 ATOM 3185 C CZ . ARG A 1 399 ? -6.194 58.371 49.297 1.00 23.34 ? 440 ARG A CZ 1 ATOM 3186 N NH1 . ARG A 1 399 ? -5.394 57.277 49.214 1.00 23.33 ? 440 ARG A NH1 1 ATOM 3187 N NH2 . ARG A 1 399 ? -6.636 58.993 48.204 1.00 22.35 ? 440 ARG A NH2 1 ATOM 3188 N N . LEU A 1 400 ? -2.394 56.772 55.371 1.00 16.46 ? 441 LEU A N 1 ATOM 3189 C CA . LEU A 1 400 ? -1.880 56.484 56.707 1.00 16.85 ? 441 LEU A CA 1 ATOM 3190 C C . LEU A 1 400 ? -0.368 56.758 56.771 1.00 17.92 ? 441 LEU A C 1 ATOM 3191 O O . LEU A 1 400 ? 0.146 57.303 57.752 1.00 18.42 ? 441 LEU A O 1 ATOM 3192 C CB . LEU A 1 400 ? -2.101 54.991 57.052 1.00 17.75 ? 441 LEU A CB 1 ATOM 3193 C CG . LEU A 1 400 ? -3.508 54.480 56.812 1.00 21.23 ? 441 LEU A CG 1 ATOM 3194 C CD1 . LEU A 1 400 ? -3.585 53.003 57.213 1.00 25.05 ? 441 LEU A CD1 1 ATOM 3195 C CD2 . LEU A 1 400 ? -4.569 55.272 57.616 1.00 23.12 ? 441 LEU A CD2 1 ATOM 3196 N N . LEU A 1 401 ? 0.333 56.418 55.703 1.00 16.63 ? 442 LEU A N 1 ATOM 3197 C CA . LEU A 1 401 ? 1.793 56.548 55.712 1.00 17.90 ? 442 LEU A CA 1 ATOM 3198 C C . LEU A 1 401 ? 2.206 58.025 55.659 1.00 18.59 ? 442 LEU A C 1 ATOM 3199 O O . LEU A 1 401 ? 3.159 58.414 56.343 1.00 20.92 ? 442 LEU A O 1 ATOM 3200 C CB . LEU A 1 401 ? 2.369 55.810 54.472 1.00 17.17 ? 442 LEU A CB 1 ATOM 3201 C CG . LEU A 1 401 ? 2.194 54.313 54.532 1.00 17.53 ? 442 LEU A CG 1 ATOM 3202 C CD1 . LEU A 1 401 ? 2.549 53.698 53.155 1.00 18.54 ? 442 LEU A CD1 1 ATOM 3203 C CD2 . LEU A 1 401 ? 3.162 53.690 55.594 1.00 21.15 ? 442 LEU A CD2 1 ATOM 3204 N N A GLN A 1 402 ? 1.463 58.805 54.838 0.50 18.62 ? 443 GLN A N 1 ATOM 3205 N N B GLN A 1 402 ? 1.563 58.856 54.861 0.50 18.29 ? 443 GLN A N 1 ATOM 3206 C CA A GLN A 1 402 ? 1.610 60.284 54.683 0.50 18.93 ? 443 GLN A CA 1 ATOM 3207 C CA B GLN A 1 402 ? 2.078 60.225 54.835 0.50 18.23 ? 443 GLN A CA 1 ATOM 3208 C C A GLN A 1 402 ? 1.637 60.949 56.063 0.50 18.50 ? 443 GLN A C 1 ATOM 3209 C C B GLN A 1 402 ? 1.624 61.065 56.070 0.50 18.11 ? 443 GLN A C 1 ATOM 3210 O O A GLN A 1 402 ? 2.576 61.691 56.420 0.50 16.92 ? 443 GLN A O 1 ATOM 3211 O O B GLN A 1 402 ? 2.225 62.122 56.328 0.50 17.53 ? 443 GLN A O 1 ATOM 3212 C CB A GLN A 1 402 ? 0.453 60.871 53.828 0.50 19.49 ? 443 GLN A CB 1 ATOM 3213 C CB B GLN A 1 402 ? 1.740 60.890 53.525 0.50 16.79 ? 443 GLN A CB 1 ATOM 3214 C CG A GLN A 1 402 ? 0.251 62.333 53.967 0.50 19.85 ? 443 GLN A CG 1 ATOM 3215 C CG B GLN A 1 402 ? 0.250 61.128 53.390 0.50 15.88 ? 443 GLN A CG 1 ATOM 3216 C CD A GLN A 1 402 ? 1.163 63.115 53.098 0.50 24.25 ? 443 GLN A CD 1 ATOM 3217 C CD B GLN A 1 402 ? -0.105 61.397 51.975 0.50 19.08 ? 443 GLN A CD 1 ATOM 3218 O OE1 A GLN A 1 402 ? 1.611 62.608 52.049 0.50 26.32 ? 443 GLN A OE1 1 ATOM 3219 O OE1 B GLN A 1 402 ? 0.740 61.290 51.071 0.50 18.83 ? 443 GLN A OE1 1 ATOM 3220 N NE2 A GLN A 1 402 ? 1.464 64.360 53.513 0.50 20.26 ? 443 GLN A NE2 1 ATOM 3221 N NE2 B GLN A 1 402 ? -1.367 61.752 51.750 0.50 20.99 ? 443 GLN A NE2 1 ATOM 3222 N N . GLU A 1 403 ? 0.627 60.605 56.851 1.00 18.32 ? 444 GLU A N 1 ATOM 3223 C CA . GLU A 1 403 ? 0.305 61.366 58.037 1.00 18.27 ? 444 GLU A CA 1 ATOM 3224 C C . GLU A 1 403 ? 0.942 60.758 59.280 1.00 18.03 ? 444 GLU A C 1 ATOM 3225 O O . GLU A 1 403 ? 1.043 61.467 60.303 1.00 18.80 ? 444 GLU A O 1 ATOM 3226 C CB . GLU A 1 403 ? -1.219 61.515 58.255 1.00 19.69 ? 444 GLU A CB 1 ATOM 3227 C CG . GLU A 1 403 ? -1.945 62.155 57.021 1.00 21.51 ? 444 GLU A CG 1 ATOM 3228 C CD . GLU A 1 403 ? -1.317 63.452 56.479 1.00 26.91 ? 444 GLU A CD 1 ATOM 3229 O OE1 . GLU A 1 403 ? -0.374 64.019 57.108 1.00 24.56 ? 444 GLU A OE1 1 ATOM 3230 O OE2 . GLU A 1 403 ? -1.812 63.946 55.409 1.00 27.44 ? 444 GLU A OE2 1 ATOM 3231 N N . ARG A 1 404 ? 1.410 59.513 59.179 1.00 16.81 ? 445 ARG A N 1 ATOM 3232 C CA . ARG A 1 404 ? 1.888 58.800 60.396 1.00 16.72 ? 445 ARG A CA 1 ATOM 3233 C C . ARG A 1 404 ? 3.254 58.186 60.278 1.00 18.29 ? 445 ARG A C 1 ATOM 3234 O O . ARG A 1 404 ? 3.798 57.689 61.271 1.00 19.22 ? 445 ARG A O 1 ATOM 3235 C CB . ARG A 1 404 ? 0.925 57.657 60.735 1.00 16.56 ? 445 ARG A CB 1 ATOM 3236 C CG . ARG A 1 404 ? -0.540 58.160 60.990 1.00 17.98 ? 445 ARG A CG 1 ATOM 3237 C CD . ARG A 1 404 ? -1.485 56.985 61.243 1.00 18.15 ? 445 ARG A CD 1 ATOM 3238 N NE . ARG A 1 404 ? -2.879 57.436 61.187 1.00 18.67 ? 445 ARG A NE 1 ATOM 3239 C CZ . ARG A 1 404 ? -3.939 56.629 61.182 1.00 18.20 ? 445 ARG A CZ 1 ATOM 3240 N NH1 . ARG A 1 404 ? -3.753 55.310 61.189 1.00 18.67 ? 445 ARG A NH1 1 ATOM 3241 N NH2 . ARG A 1 404 ? -5.160 57.145 61.105 1.00 18.77 ? 445 ARG A NH2 1 ATOM 3242 N N . GLY A 1 405 ? 3.804 58.201 59.083 1.00 17.50 ? 446 GLY A N 1 ATOM 3243 C CA . GLY A 1 405 ? 5.088 57.482 58.810 1.00 17.77 ? 446 GLY A CA 1 ATOM 3244 C C . GLY A 1 405 ? 6.294 58.263 59.324 1.00 17.66 ? 446 GLY A C 1 ATOM 3245 O O . GLY A 1 405 ? 6.641 59.348 58.804 1.00 19.97 ? 446 GLY A O 1 ATOM 3246 N N . VAL A 1 406 ? 6.954 57.706 60.317 1.00 18.24 ? 447 VAL A N 1 ATOM 3247 C CA . VAL A 1 406 ? 8.173 58.333 60.833 1.00 18.36 ? 447 VAL A CA 1 ATOM 3248 C C . VAL A 1 406 ? 9.399 58.010 59.974 1.00 17.57 ? 447 VAL A C 1 ATOM 3249 O O . VAL A 1 406 ? 10.158 58.904 59.597 1.00 17.92 ? 447 VAL A O 1 ATOM 3250 C CB . VAL A 1 406 ? 8.418 57.832 62.266 1.00 20.65 ? 447 VAL A CB 1 ATOM 3251 C CG1 . VAL A 1 406 ? 9.763 58.241 62.788 1.00 22.37 ? 447 VAL A CG1 1 ATOM 3252 C CG2 . VAL A 1 406 ? 7.312 58.397 63.145 1.00 23.17 ? 447 VAL A CG2 1 ATOM 3253 N N . ALA A 1 407 ? 9.626 56.734 59.697 1.00 18.06 ? 448 ALA A N 1 ATOM 3254 C CA . ALA A 1 407 ? 10.826 56.306 58.978 1.00 16.58 ? 448 ALA A CA 1 ATOM 3255 C C . ALA A 1 407 ? 10.631 54.913 58.396 1.00 17.13 ? 448 ALA A C 1 ATOM 3256 O O . ALA A 1 407 ? 9.791 54.144 58.904 1.00 18.64 ? 448 ALA A O 1 ATOM 3257 C CB . ALA A 1 407 ? 12.028 56.249 59.944 1.00 18.60 ? 448 ALA A CB 1 ATOM 3258 N N . TYR A 1 408 ? 11.404 54.637 57.344 1.00 16.80 ? 449 TYR A N 1 ATOM 3259 C CA . TYR A 1 408 ? 11.441 53.317 56.708 1.00 15.99 ? 449 TYR A CA 1 ATOM 3260 C C . TYR A 1 408 ? 12.896 52.904 56.651 1.00 17.30 ? 449 TYR A C 1 ATOM 3261 O O . TYR A 1 408 ? 13.757 53.636 56.143 1.00 17.80 ? 449 TYR A O 1 ATOM 3262 C CB . TYR A 1 408 ? 10.851 53.414 55.272 1.00 15.07 ? 449 TYR A CB 1 ATOM 3263 C CG . TYR A 1 408 ? 10.942 52.094 54.571 1.00 15.79 ? 449 TYR A CG 1 ATOM 3264 C CD1 . TYR A 1 408 ? 9.939 51.169 54.686 1.00 16.69 ? 449 TYR A CD1 1 ATOM 3265 C CD2 . TYR A 1 408 ? 12.066 51.770 53.816 1.00 17.60 ? 449 TYR A CD2 1 ATOM 3266 C CE1 . TYR A 1 408 ? 10.036 49.893 54.092 1.00 17.94 ? 449 TYR A CE1 1 ATOM 3267 C CE2 . TYR A 1 408 ? 12.174 50.523 53.172 1.00 16.69 ? 449 TYR A CE2 1 ATOM 3268 C CZ . TYR A 1 408 ? 11.159 49.609 53.313 1.00 18.24 ? 449 TYR A CZ 1 ATOM 3269 O OH . TYR A 1 408 ? 11.270 48.384 52.696 1.00 18.95 ? 449 TYR A OH 1 ATOM 3270 N N . ILE A 1 409 ? 13.181 51.693 57.140 1.00 17.24 ? 450 ILE A N 1 ATOM 3271 C CA . ILE A 1 409 ? 14.517 51.095 57.063 1.00 16.30 ? 450 ILE A CA 1 ATOM 3272 C C . ILE A 1 409 ? 14.387 49.869 56.178 1.00 16.87 ? 450 ILE A C 1 ATOM 3273 O O . ILE A 1 409 ? 13.590 48.970 56.440 1.00 16.82 ? 450 ILE A O 1 ATOM 3274 C CB . ILE A 1 409 ? 14.994 50.681 58.502 1.00 16.88 ? 450 ILE A CB 1 ATOM 3275 C CG1 . ILE A 1 409 ? 15.094 51.908 59.454 1.00 20.20 ? 450 ILE A CG1 1 ATOM 3276 C CG2 . ILE A 1 409 ? 16.364 49.941 58.452 1.00 18.40 ? 450 ILE A CG2 1 ATOM 3277 C CD1 . ILE A 1 409 ? 15.951 53.056 58.914 1.00 21.48 ? 450 ILE A CD1 1 ATOM 3278 N N . ASN A 1 410 ? 15.172 49.833 55.112 1.00 16.62 ? 451 ASN A N 1 ATOM 3279 C CA . ASN A 1 410 ? 15.083 48.681 54.206 1.00 16.92 ? 451 ASN A CA 1 ATOM 3280 C C . ASN A 1 410 ? 15.960 47.531 54.705 1.00 19.03 ? 451 ASN A C 1 ATOM 3281 O O . ASN A 1 410 ? 16.890 47.715 55.513 1.00 21.79 ? 451 ASN A O 1 ATOM 3282 C CB . ASN A 1 410 ? 15.619 49.103 52.836 1.00 17.28 ? 451 ASN A CB 1 ATOM 3283 C CG . ASN A 1 410 ? 15.009 48.298 51.696 1.00 19.51 ? 451 ASN A CG 1 ATOM 3284 O OD1 . ASN A 1 410 ? 13.792 48.158 51.592 1.00 22.15 ? 451 ASN A OD1 1 ATOM 3285 N ND2 . ASN A 1 410 ? 15.901 47.712 50.839 1.00 19.89 ? 451 ASN A ND2 1 ATOM 3286 N N . ALA A 1 411 ? 15.649 46.331 54.243 1.00 18.33 ? 452 ALA A N 1 ATOM 3287 C CA . ALA A 1 411 ? 16.443 45.165 54.676 1.00 19.83 ? 452 ALA A CA 1 ATOM 3288 C C . ALA A 1 411 ? 16.479 44.104 53.606 1.00 20.46 ? 452 ALA A C 1 ATOM 3289 O O . ALA A 1 411 ? 15.984 42.969 53.798 1.00 20.63 ? 452 ALA A O 1 ATOM 3290 C CB . ALA A 1 411 ? 15.791 44.601 55.968 1.00 20.88 ? 452 ALA A CB 1 ATOM 3291 N N . ASP A 1 412 ? 17.088 44.455 52.478 1.00 20.85 ? 453 ASP A N 1 ATOM 3292 C CA . ASP A 1 412 ? 17.428 43.461 51.469 1.00 19.84 ? 453 ASP A CA 1 ATOM 3293 C C . ASP A 1 412 ? 18.789 42.897 51.922 1.00 21.66 ? 453 ASP A C 1 ATOM 3294 O O . ASP A 1 412 ? 19.119 42.957 53.114 1.00 22.06 ? 453 ASP A O 1 ATOM 3295 C CB . ASP A 1 412 ? 17.412 44.054 50.047 1.00 18.88 ? 453 ASP A CB 1 ATOM 3296 C CG . ASP A 1 412 ? 17.338 42.992 48.950 1.00 20.30 ? 453 ASP A CG 1 ATOM 3297 O OD1 . ASP A 1 412 ? 17.401 41.810 49.278 1.00 22.42 ? 453 ASP A OD1 1 ATOM 3298 O OD2 . ASP A 1 412 ? 17.301 43.378 47.778 1.00 18.30 ? 453 ASP A OD2 1 ATOM 3299 N N A SER A 1 413 ? 19.535 42.327 50.994 0.80 20.48 ? 454 SER A N 1 ATOM 3300 N N B SER A 1 413 ? 19.535 42.308 50.993 0.20 21.28 ? 454 SER A N 1 ATOM 3301 C CA A SER A 1 413 ? 20.788 41.616 51.265 0.80 21.76 ? 454 SER A CA 1 ATOM 3302 C CA B SER A 1 413 ? 20.740 41.539 51.311 0.20 21.97 ? 454 SER A CA 1 ATOM 3303 C C A SER A 1 413 ? 21.614 42.263 52.385 0.80 22.02 ? 454 SER A C 1 ATOM 3304 C C B SER A 1 413 ? 21.629 42.214 52.350 0.20 22.26 ? 454 SER A C 1 ATOM 3305 O O A SER A 1 413 ? 21.878 43.482 52.357 0.80 22.63 ? 454 SER A O 1 ATOM 3306 O O B SER A 1 413 ? 21.996 43.382 52.204 0.20 22.40 ? 454 SER A O 1 ATOM 3307 C CB A SER A 1 413 ? 21.604 41.589 49.990 0.80 22.29 ? 454 SER A CB 1 ATOM 3308 C CB B SER A 1 413 ? 21.543 41.291 50.046 0.20 22.13 ? 454 SER A CB 1 ATOM 3309 O OG A SER A 1 413 ? 20.838 41.082 48.895 0.80 19.88 ? 454 SER A OG 1 ATOM 3310 O OG B SER A 1 413 ? 22.015 42.514 49.515 0.20 21.64 ? 454 SER A OG 1 ATOM 3311 N N . SER A 1 414 ? 21.955 41.472 53.404 1.00 22.49 ? 455 SER A N 1 ATOM 3312 C CA . SER A 1 414 ? 22.768 42.001 54.505 1.00 23.78 ? 455 SER A CA 1 ATOM 3313 C C . SER A 1 414 ? 24.239 42.078 54.141 1.00 24.30 ? 455 SER A C 1 ATOM 3314 O O . SER A 1 414 ? 24.985 42.817 54.763 1.00 24.60 ? 455 SER A O 1 ATOM 3315 C CB . SER A 1 414 ? 22.633 41.082 55.715 1.00 25.05 ? 455 SER A CB 1 ATOM 3316 O OG . SER A 1 414 ? 21.296 41.209 56.188 1.00 28.47 ? 455 SER A OG 1 ATOM 3317 N N . ILE A 1 415 ? 24.676 41.274 53.175 1.00 25.05 ? 456 ILE A N 1 ATOM 3318 C CA . ILE A 1 415 ? 26.095 41.205 52.834 1.00 27.61 ? 456 ILE A CA 1 ATOM 3319 C C . ILE A 1 415 ? 26.232 41.223 51.319 1.00 28.28 ? 456 ILE A C 1 ATOM 3320 O O . ILE A 1 415 ? 25.429 40.617 50.614 1.00 31.63 ? 456 ILE A O 1 ATOM 3321 C CB . ILE A 1 415 ? 26.759 39.931 53.444 1.00 27.21 ? 456 ILE A CB 1 ATOM 3322 C CG1 . ILE A 1 415 ? 25.929 38.654 53.108 1.00 29.77 ? 456 ILE A CG1 1 ATOM 3323 C CG2 . ILE A 1 415 ? 26.824 40.067 54.973 1.00 29.47 ? 456 ILE A CG2 1 ATOM 3324 C CD1 . ILE A 1 415 ? 26.715 37.416 52.753 1.00 36.94 ? 456 ILE A CD1 1 ATOM 3325 N N . GLU A 1 416 ? 27.215 41.925 50.798 1.00 26.23 ? 457 GLU A N 1 ATOM 3326 C CA . GLU A 1 416 ? 27.602 41.741 49.405 1.00 26.62 ? 457 GLU A CA 1 ATOM 3327 C C . GLU A 1 416 ? 29.115 41.673 49.383 1.00 26.75 ? 457 GLU A C 1 ATOM 3328 O O . GLU A 1 416 ? 29.751 41.727 48.328 1.00 27.00 ? 457 GLU A O 1 ATOM 3329 C CB . GLU A 1 416 ? 27.049 42.875 48.537 1.00 26.27 ? 457 GLU A CB 1 ATOM 3330 C CG . GLU A 1 416 ? 27.511 44.241 49.004 1.00 27.34 ? 457 GLU A CG 1 ATOM 3331 C CD . GLU A 1 416 ? 26.926 45.427 48.198 1.00 29.76 ? 457 GLU A CD 1 ATOM 3332 O OE1 . GLU A 1 416 ? 25.922 45.283 47.458 1.00 30.07 ? 457 GLU A OE1 1 ATOM 3333 O OE2 . GLU A 1 416 ? 27.518 46.512 48.303 1.00 30.10 ? 457 GLU A OE2 1 ATOM 3334 N N . GLY A 1 417 ? 29.688 41.539 50.581 1.00 26.56 ? 458 GLY A N 1 ATOM 3335 C CA . GLY A 1 417 ? 31.133 41.437 50.786 1.00 27.53 ? 458 GLY A CA 1 ATOM 3336 C C . GLY A 1 417 ? 31.393 41.356 52.275 1.00 27.98 ? 458 GLY A C 1 ATOM 3337 O O . GLY A 1 417 ? 30.453 41.343 53.086 1.00 27.59 ? 458 GLY A O 1 ATOM 3338 N N . ASN A 1 418 ? 32.661 41.339 52.643 1.00 27.42 ? 459 ASN A N 1 ATOM 3339 C CA . ASN A 1 418 ? 33.026 41.210 54.049 1.00 28.95 ? 459 ASN A CA 1 ATOM 3340 C C . ASN A 1 418 ? 34.033 42.270 54.490 1.00 28.34 ? 459 ASN A C 1 ATOM 3341 O O . ASN A 1 418 ? 34.813 42.058 55.426 1.00 31.06 ? 459 ASN A O 1 ATOM 3342 C CB . ASN A 1 418 ? 33.532 39.768 54.323 1.00 30.24 ? 459 ASN A CB 1 ATOM 3343 C CG . ASN A 1 418 ? 34.831 39.436 53.607 1.00 33.64 ? 459 ASN A CG 1 ATOM 3344 O OD1 . ASN A 1 418 ? 35.516 40.304 53.044 1.00 34.74 ? 459 ASN A OD1 1 ATOM 3345 N ND2 . ASN A 1 418 ? 35.197 38.150 53.646 1.00 43.38 ? 459 ASN A ND2 1 ATOM 3346 N N . TYR A 1 419 ? 34.038 43.408 53.808 1.00 27.08 ? 460 TYR A N 1 ATOM 3347 C CA . TYR A 1 419 ? 35.086 44.418 54.023 1.00 27.96 ? 460 TYR A CA 1 ATOM 3348 C C . TYR A 1 419 ? 34.662 45.497 55.019 1.00 27.35 ? 460 TYR A C 1 ATOM 3349 O O . TYR A 1 419 ? 35.337 45.687 56.040 1.00 28.21 ? 460 TYR A O 1 ATOM 3350 C CB . TYR A 1 419 ? 35.515 45.042 52.691 1.00 28.06 ? 460 TYR A CB 1 ATOM 3351 C CG . TYR A 1 419 ? 36.590 46.087 52.806 1.00 32.30 ? 460 TYR A CG 1 ATOM 3352 C CD1 . TYR A 1 419 ? 37.878 45.734 53.170 1.00 37.13 ? 460 TYR A CD1 1 ATOM 3353 C CD2 . TYR A 1 419 ? 36.322 47.417 52.507 1.00 37.27 ? 460 TYR A CD2 1 ATOM 3354 C CE1 . TYR A 1 419 ? 38.890 46.687 53.267 1.00 42.39 ? 460 TYR A CE1 1 ATOM 3355 C CE2 . TYR A 1 419 ? 37.339 48.386 52.596 1.00 39.52 ? 460 TYR A CE2 1 ATOM 3356 C CZ . TYR A 1 419 ? 38.596 48.008 52.968 1.00 42.50 ? 460 TYR A CZ 1 ATOM 3357 O OH . TYR A 1 419 ? 39.607 48.949 53.050 1.00 47.66 ? 460 TYR A OH 1 ATOM 3358 N N . THR A 1 420 ? 33.543 46.167 54.745 1.00 26.38 ? 461 THR A N 1 ATOM 3359 C CA . THR A 1 420 ? 33.120 47.226 55.662 1.00 25.96 ? 461 THR A CA 1 ATOM 3360 C C . THR A 1 420 ? 31.648 47.526 55.467 1.00 23.69 ? 461 THR A C 1 ATOM 3361 O O . THR A 1 420 ? 30.982 46.908 54.614 1.00 23.45 ? 461 THR A O 1 ATOM 3362 C CB . THR A 1 420 ? 33.986 48.508 55.543 1.00 27.39 ? 461 THR A CB 1 ATOM 3363 O OG1 . THR A 1 420 ? 33.736 49.360 56.676 1.00 27.46 ? 461 THR A OG1 1 ATOM 3364 C CG2 . THR A 1 420 ? 33.647 49.292 54.289 1.00 26.52 ? 461 THR A CG2 1 ATOM 3365 N N . LEU A 1 421 ? 31.153 48.437 56.292 1.00 23.63 ? 462 LEU A N 1 ATOM 3366 C CA . LEU A 1 421 ? 29.745 48.865 56.204 1.00 22.67 ? 462 LEU A CA 1 ATOM 3367 C C . LEU A 1 421 ? 29.498 49.777 54.985 1.00 23.43 ? 462 LEU A C 1 ATOM 3368 O O . LEU A 1 421 ? 30.404 50.529 54.542 1.00 24.19 ? 462 LEU A O 1 ATOM 3369 C CB . LEU A 1 421 ? 29.366 49.609 57.505 1.00 22.23 ? 462 LEU A CB 1 ATOM 3370 C CG . LEU A 1 421 ? 27.854 49.769 57.709 1.00 22.60 ? 462 LEU A CG 1 ATOM 3371 C CD1 . LEU A 1 421 ? 27.214 48.388 58.006 1.00 24.46 ? 462 LEU A CD1 1 ATOM 3372 C CD2 . LEU A 1 421 ? 27.697 50.711 58.918 1.00 24.23 ? 462 LEU A CD2 1 ATOM 3373 N N . ARG A 1 422 ? 28.283 49.700 54.448 1.00 21.86 ? 463 ARG A N 1 ATOM 3374 C CA . ARG A 1 422 ? 27.822 50.597 53.368 1.00 22.42 ? 463 ARG A CA 1 ATOM 3375 C C . ARG A 1 422 ? 26.496 51.144 53.860 1.00 22.49 ? 463 ARG A C 1 ATOM 3376 O O . ARG A 1 422 ? 25.678 50.391 54.349 1.00 23.18 ? 463 ARG A O 1 ATOM 3377 C CB . ARG A 1 422 ? 27.656 49.802 52.040 1.00 21.62 ? 463 ARG A CB 1 ATOM 3378 C CG . ARG A 1 422 ? 27.441 50.680 50.799 1.00 24.24 ? 463 ARG A CG 1 ATOM 3379 C CD . ARG A 1 422 ? 27.315 49.813 49.527 1.00 25.44 ? 463 ARG A CD 1 ATOM 3380 N NE . ARG A 1 422 ? 26.983 50.637 48.357 1.00 28.47 ? 463 ARG A NE 1 ATOM 3381 C CZ . ARG A 1 422 ? 26.920 50.184 47.106 1.00 27.65 ? 463 ARG A CZ 1 ATOM 3382 N NH1 . ARG A 1 422 ? 27.178 48.891 46.815 1.00 27.74 ? 463 ARG A NH1 1 ATOM 3383 N NH2 . ARG A 1 422 ? 26.618 51.038 46.105 1.00 29.11 ? 463 ARG A NH2 1 ATOM 3384 N N . VAL A 1 423 ? 26.292 52.455 53.768 1.00 21.83 ? 464 VAL A N 1 ATOM 3385 C CA . VAL A 1 423 ? 25.028 53.063 54.222 1.00 22.01 ? 464 VAL A CA 1 ATOM 3386 C C . VAL A 1 423 ? 24.578 54.103 53.216 1.00 22.22 ? 464 VAL A C 1 ATOM 3387 O O . VAL A 1 423 ? 25.375 54.916 52.748 1.00 22.66 ? 464 VAL A O 1 ATOM 3388 C CB . VAL A 1 423 ? 25.201 53.746 55.602 1.00 22.46 ? 464 VAL A CB 1 ATOM 3389 C CG1 . VAL A 1 423 ? 23.921 54.421 56.065 1.00 22.24 ? 464 VAL A CG1 1 ATOM 3390 C CG2 . VAL A 1 423 ? 25.718 52.750 56.660 1.00 24.36 ? 464 VAL A CG2 1 ATOM 3391 N N . ASP A 1 424 ? 23.296 54.098 52.882 1.00 21.18 ? 465 ASP A N 1 ATOM 3392 C CA . ASP A 1 424 ? 22.672 55.166 52.091 1.00 21.67 ? 465 ASP A CA 1 ATOM 3393 C C . ASP A 1 424 ? 21.487 55.588 52.934 1.00 20.33 ? 465 ASP A C 1 ATOM 3394 O O . ASP A 1 424 ? 20.691 54.758 53.328 1.00 20.38 ? 465 ASP A O 1 ATOM 3395 C CB . ASP A 1 424 ? 22.073 54.643 50.762 1.00 21.50 ? 465 ASP A CB 1 ATOM 3396 C CG . ASP A 1 424 ? 23.127 54.302 49.681 1.00 26.43 ? 465 ASP A CG 1 ATOM 3397 O OD1 . ASP A 1 424 ? 24.334 54.282 49.948 1.00 30.96 ? 465 ASP A OD1 1 ATOM 3398 O OD2 . ASP A 1 424 ? 22.704 54.064 48.532 1.00 31.52 ? 465 ASP A OD2 1 ATOM 3399 N N . CYS A 1 425 ? 21.280 56.893 53.151 1.00 20.13 ? 466 CYS A N 1 ATOM 3400 C CA . CYS A 1 425 ? 20.101 57.312 53.941 1.00 19.91 ? 466 CYS A CA 1 ATOM 3401 C C . CYS A 1 425 ? 19.884 58.776 53.790 1.00 20.72 ? 466 CYS A C 1 ATOM 3402 O O . CYS A 1 425 ? 20.728 59.488 53.274 1.00 24.10 ? 466 CYS A O 1 ATOM 3403 C CB . CYS A 1 425 ? 20.230 56.994 55.461 1.00 20.90 ? 466 CYS A CB 1 ATOM 3404 S SG . CYS A 1 425 ? 21.555 57.866 56.343 1.00 22.45 ? 466 CYS A SG 1 ATOM 3405 N N . THR A 1 426 ? 18.727 59.250 54.258 1.00 19.03 ? 467 THR A N 1 ATOM 3406 C CA . THR A 1 426 ? 18.480 60.669 54.284 1.00 18.78 ? 467 THR A CA 1 ATOM 3407 C C . THR A 1 426 ? 19.432 61.389 55.247 1.00 18.90 ? 467 THR A C 1 ATOM 3408 O O . THR A 1 426 ? 19.842 60.824 56.251 1.00 18.65 ? 467 THR A O 1 ATOM 3409 C CB . THR A 1 426 ? 17.048 60.908 54.754 1.00 17.99 ? 467 THR A CB 1 ATOM 3410 O OG1 . THR A 1 426 ? 16.861 62.324 54.970 1.00 19.23 ? 467 THR A OG1 1 ATOM 3411 C CG2 . THR A 1 426 ? 16.738 60.162 56.081 1.00 20.26 ? 467 THR A CG2 1 ATOM 3412 N N . PRO A 1 427 ? 19.791 62.630 54.939 1.00 18.38 ? 468 PRO A N 1 ATOM 3413 C CA . PRO A 1 427 ? 20.619 63.388 55.926 1.00 20.01 ? 468 PRO A CA 1 ATOM 3414 C C . PRO A 1 427 ? 20.001 63.409 57.319 1.00 19.98 ? 468 PRO A C 1 ATOM 3415 O O . PRO A 1 427 ? 20.734 63.560 58.282 1.00 21.00 ? 468 PRO A O 1 ATOM 3416 C CB . PRO A 1 427 ? 20.625 64.834 55.342 1.00 21.84 ? 468 PRO A CB 1 ATOM 3417 C CG . PRO A 1 427 ? 20.531 64.580 53.872 1.00 21.57 ? 468 PRO A CG 1 ATOM 3418 C CD . PRO A 1 427 ? 19.594 63.394 53.679 1.00 18.74 ? 468 PRO A CD 1 ATOM 3419 N N . LEU A 1 428 ? 18.659 63.314 57.417 1.00 19.44 ? 469 LEU A N 1 ATOM 3420 C CA . LEU A 1 428 ? 18.053 63.338 58.754 1.00 20.60 ? 469 LEU A CA 1 ATOM 3421 C C . LEU A 1 428 ? 18.500 62.204 59.652 1.00 20.26 ? 469 LEU A C 1 ATOM 3422 O O . LEU A 1 428 ? 18.385 62.313 60.867 1.00 22.26 ? 469 LEU A O 1 ATOM 3423 C CB . LEU A 1 428 ? 16.523 63.288 58.634 1.00 20.51 ? 469 LEU A CB 1 ATOM 3424 C CG . LEU A 1 428 ? 15.885 64.519 58.063 1.00 20.24 ? 469 LEU A CG 1 ATOM 3425 C CD1 . LEU A 1 428 ? 14.388 64.301 57.976 1.00 22.29 ? 469 LEU A CD1 1 ATOM 3426 C CD2 . LEU A 1 428 ? 16.216 65.769 58.923 1.00 22.20 ? 469 LEU A CD2 1 ATOM 3427 N N . MET A 1 429 ? 19.053 61.133 59.075 1.00 19.81 ? 470 MET A N 1 ATOM 3428 C CA A MET A 1 429 ? 19.536 59.950 59.809 0.50 20.17 ? 470 MET A CA 1 ATOM 3429 C CA B MET A 1 429 ? 19.533 60.041 59.918 0.50 20.72 ? 470 MET A CA 1 ATOM 3430 C C . MET A 1 429 ? 21.052 59.907 60.019 1.00 21.23 ? 470 MET A C 1 ATOM 3431 O O . MET A 1 429 ? 21.551 58.997 60.674 1.00 21.43 ? 470 MET A O 1 ATOM 3432 C CB A MET A 1 429 ? 19.120 58.651 59.079 0.50 19.72 ? 470 MET A CB 1 ATOM 3433 C CB B MET A 1 429 ? 18.858 58.723 59.533 0.50 21.35 ? 470 MET A CB 1 ATOM 3434 C CG A MET A 1 429 ? 17.629 58.359 59.153 0.50 18.65 ? 470 MET A CG 1 ATOM 3435 C CG B MET A 1 429 ? 17.399 58.730 59.923 0.50 21.23 ? 470 MET A CG 1 ATOM 3436 S SD A MET A 1 429 ? 17.245 56.756 58.458 0.50 17.50 ? 470 MET A SD 1 ATOM 3437 S SD B MET A 1 429 ? 16.586 57.148 59.747 0.50 26.22 ? 470 MET A SD 1 ATOM 3438 C CE A MET A 1 429 ? 15.438 56.787 58.437 0.50 15.59 ? 470 MET A CE 1 ATOM 3439 C CE B MET A 1 429 ? 16.265 57.127 57.987 0.50 26.92 ? 470 MET A CE 1 ATOM 3440 N N . TYR A 1 430 ? 21.801 60.870 59.477 1.00 21.02 ? 471 TYR A N 1 ATOM 3441 C CA . TYR A 1 430 ? 23.268 60.800 59.581 1.00 22.29 ? 471 TYR A CA 1 ATOM 3442 C C . TYR A 1 430 ? 23.743 60.704 61.024 1.00 22.78 ? 471 TYR A C 1 ATOM 3443 O O . TYR A 1 430 ? 24.601 59.862 61.358 1.00 23.48 ? 471 TYR A O 1 ATOM 3444 C CB . TYR A 1 430 ? 23.919 62.028 58.986 1.00 21.61 ? 471 TYR A CB 1 ATOM 3445 C CG . TYR A 1 430 ? 23.884 62.151 57.473 1.00 20.79 ? 471 TYR A CG 1 ATOM 3446 C CD1 . TYR A 1 430 ? 23.454 61.112 56.633 1.00 20.54 ? 471 TYR A CD1 1 ATOM 3447 C CD2 . TYR A 1 430 ? 24.372 63.312 56.885 1.00 22.56 ? 471 TYR A CD2 1 ATOM 3448 C CE1 . TYR A 1 430 ? 23.417 61.313 55.205 1.00 22.91 ? 471 TYR A CE1 1 ATOM 3449 C CE2 . TYR A 1 430 ? 24.384 63.493 55.515 1.00 25.50 ? 471 TYR A CE2 1 ATOM 3450 C CZ . TYR A 1 430 ? 23.921 62.497 54.681 1.00 25.77 ? 471 TYR A CZ 1 ATOM 3451 O OH . TYR A 1 430 ? 23.946 62.707 53.303 1.00 27.32 ? 471 TYR A OH 1 ATOM 3452 N N . SER A 1 431 ? 23.185 61.564 61.891 1.00 22.61 ? 472 SER A N 1 ATOM 3453 C CA . SER A 1 431 ? 23.665 61.615 63.296 1.00 23.25 ? 472 SER A CA 1 ATOM 3454 C C . SER A 1 431 ? 23.290 60.365 64.043 1.00 23.62 ? 472 SER A C 1 ATOM 3455 O O . SER A 1 431 ? 24.110 59.852 64.819 1.00 23.41 ? 472 SER A O 1 ATOM 3456 C CB . SER A 1 431 ? 23.096 62.860 63.973 1.00 24.88 ? 472 SER A CB 1 ATOM 3457 O OG A SER A 1 431 ? 23.773 64.009 63.421 0.50 27.91 ? 472 SER A OG 1 ATOM 3458 O OG B SER A 1 431 ? 23.464 62.959 65.340 0.50 21.48 ? 472 SER A OG 1 ATOM 3459 N N . LEU A 1 432 ? 22.095 59.839 63.769 1.00 22.93 ? 473 LEU A N 1 ATOM 3460 C CA . LEU A 1 432 ? 21.645 58.553 64.336 1.00 23.84 ? 473 LEU A CA 1 ATOM 3461 C C . LEU A 1 432 ? 22.624 57.432 63.970 1.00 22.87 ? 473 LEU A C 1 ATOM 3462 O O . LEU A 1 432 ? 23.072 56.669 64.819 1.00 23.94 ? 473 LEU A O 1 ATOM 3463 C CB . LEU A 1 432 ? 20.234 58.201 63.822 1.00 23.18 ? 473 LEU A CB 1 ATOM 3464 C CG . LEU A 1 432 ? 19.702 56.774 64.088 1.00 23.63 ? 473 LEU A CG 1 ATOM 3465 C CD1 . LEU A 1 432 ? 19.734 56.432 65.566 1.00 27.98 ? 473 LEU A CD1 1 ATOM 3466 C CD2 . LEU A 1 432 ? 18.310 56.656 63.517 1.00 28.06 ? 473 LEU A CD2 1 ATOM 3467 N N . VAL A 1 433 ? 22.957 57.347 62.689 1.00 22.89 ? 474 VAL A N 1 ATOM 3468 C CA . VAL A 1 433 ? 23.880 56.278 62.230 1.00 23.39 ? 474 VAL A CA 1 ATOM 3469 C C . VAL A 1 433 ? 25.254 56.434 62.838 1.00 24.40 ? 474 VAL A C 1 ATOM 3470 O O . VAL A 1 433 ? 25.850 55.432 63.300 1.00 24.47 ? 474 VAL A O 1 ATOM 3471 C CB . VAL A 1 433 ? 23.985 56.316 60.696 1.00 22.38 ? 474 VAL A CB 1 ATOM 3472 C CG1 . VAL A 1 433 ? 25.050 55.317 60.192 1.00 26.98 ? 474 VAL A CG1 1 ATOM 3473 C CG2 . VAL A 1 433 ? 22.646 55.944 60.087 1.00 25.28 ? 474 VAL A CG2 1 ATOM 3474 N N . HIS A 1 434 ? 25.776 57.667 62.864 1.00 24.30 ? 475 HIS A N 1 ATOM 3475 C CA . HIS A 1 434 ? 27.099 57.880 63.485 1.00 26.73 ? 475 HIS A CA 1 ATOM 3476 C C . HIS A 1 434 ? 27.066 57.450 64.948 1.00 26.45 ? 475 HIS A C 1 ATOM 3477 O O . HIS A 1 434 ? 27.931 56.693 65.402 1.00 27.14 ? 475 HIS A O 1 ATOM 3478 C CB . HIS A 1 434 ? 27.535 59.338 63.406 1.00 26.78 ? 475 HIS A CB 1 ATOM 3479 C CG . HIS A 1 434 ? 27.773 59.815 62.011 1.00 30.97 ? 475 HIS A CG 1 ATOM 3480 N ND1 . HIS A 1 434 ? 27.616 61.137 61.648 1.00 38.41 ? 475 HIS A ND1 1 ATOM 3481 C CD2 . HIS A 1 434 ? 28.061 59.144 60.870 1.00 32.88 ? 475 HIS A CD2 1 ATOM 3482 C CE1 . HIS A 1 434 ? 27.859 61.264 60.354 1.00 36.93 ? 475 HIS A CE1 1 ATOM 3483 N NE2 . HIS A 1 434 ? 28.170 60.076 59.869 1.00 31.73 ? 475 HIS A NE2 1 ATOM 3484 N N . ASN A 1 435 ? 26.060 57.923 65.680 1.00 25.27 ? 476 ASN A N 1 ATOM 3485 C CA . ASN A 1 435 ? 25.997 57.601 67.118 1.00 26.55 ? 476 ASN A CA 1 ATOM 3486 C C . ASN A 1 435 ? 25.815 56.114 67.373 1.00 26.71 ? 476 ASN A C 1 ATOM 3487 O O . ASN A 1 435 ? 26.425 55.564 68.297 1.00 27.81 ? 476 ASN A O 1 ATOM 3488 C CB . ASN A 1 435 ? 24.847 58.364 67.790 1.00 26.87 ? 476 ASN A CB 1 ATOM 3489 C CG . ASN A 1 435 ? 25.130 59.837 67.931 1.00 29.44 ? 476 ASN A CG 1 ATOM 3490 O OD1 . ASN A 1 435 ? 26.161 60.336 67.493 1.00 30.55 ? 476 ASN A OD1 1 ATOM 3491 N ND2 . ASN A 1 435 ? 24.189 60.550 68.553 1.00 27.97 ? 476 ASN A ND2 1 ATOM 3492 N N . LEU A 1 436 ? 24.964 55.452 66.583 1.00 25.51 ? 477 LEU A N 1 ATOM 3493 C CA . LEU A 1 436 ? 24.728 54.018 66.812 1.00 24.87 ? 477 LEU A CA 1 ATOM 3494 C C . LEU A 1 436 ? 26.002 53.229 66.522 1.00 24.31 ? 477 LEU A C 1 ATOM 3495 O O . LEU A 1 436 ? 26.363 52.344 67.282 1.00 25.10 ? 477 LEU A O 1 ATOM 3496 C CB . LEU A 1 436 ? 23.570 53.517 65.891 1.00 24.60 ? 477 LEU A CB 1 ATOM 3497 C CG . LEU A 1 436 ? 23.322 52.011 65.910 1.00 27.29 ? 477 LEU A CG 1 ATOM 3498 C CD1 . LEU A 1 436 ? 23.037 51.571 67.342 1.00 27.15 ? 477 LEU A CD1 1 ATOM 3499 C CD2 . LEU A 1 436 ? 22.196 51.622 64.985 1.00 26.16 ? 477 LEU A CD2 1 ATOM 3500 N N . THR A 1 437 ? 26.646 53.528 65.401 1.00 24.08 ? 478 THR A N 1 ATOM 3501 C CA . THR A 1 437 ? 27.853 52.758 65.031 1.00 24.33 ? 478 THR A CA 1 ATOM 3502 C C . THR A 1 437 ? 29.008 52.971 65.996 1.00 26.52 ? 478 THR A C 1 ATOM 3503 O O . THR A 1 437 ? 29.874 52.094 66.121 1.00 26.92 ? 478 THR A O 1 ATOM 3504 C CB . THR A 1 437 ? 28.312 52.992 63.562 1.00 24.88 ? 478 THR A CB 1 ATOM 3505 O OG1 . THR A 1 437 ? 28.642 54.373 63.347 1.00 24.47 ? 478 THR A OG1 1 ATOM 3506 C CG2 . THR A 1 437 ? 27.175 52.554 62.546 1.00 25.22 ? 478 THR A CG2 1 ATOM 3507 N N . LYS A 1 438 ? 29.021 54.098 66.708 1.00 26.45 ? 479 LYS A N 1 ATOM 3508 C CA . LYS A 1 438 ? 30.048 54.314 67.744 1.00 29.01 ? 479 LYS A CA 1 ATOM 3509 C C . LYS A 1 438 ? 29.842 53.417 68.956 1.00 30.66 ? 479 LYS A C 1 ATOM 3510 O O . LYS A 1 438 ? 30.792 53.210 69.737 1.00 31.39 ? 479 LYS A O 1 ATOM 3511 C CB . LYS A 1 438 ? 30.064 55.791 68.184 1.00 29.76 ? 479 LYS A CB 1 ATOM 3512 C CG . LYS A 1 438 ? 30.615 56.730 67.117 1.00 31.47 ? 479 LYS A CG 1 ATOM 3513 C CD . LYS A 1 438 ? 30.587 58.190 67.561 1.00 34.43 ? 479 LYS A CD 1 ATOM 3514 C CE . LYS A 1 438 ? 31.018 59.084 66.412 1.00 36.98 ? 479 LYS A CE 1 ATOM 3515 N NZ . LYS A 1 438 ? 30.864 60.566 66.721 1.00 38.75 ? 479 LYS A NZ 1 ATOM 3516 N N . GLU A 1 439 ? 28.624 52.905 69.123 1.00 31.41 ? 480 GLU A N 1 ATOM 3517 C CA A GLU A 1 439 ? 28.267 52.054 70.260 0.50 32.58 ? 480 GLU A CA 1 ATOM 3518 C CA B GLU A 1 439 ? 28.268 52.054 70.265 0.50 33.26 ? 480 GLU A CA 1 ATOM 3519 C C . GLU A 1 439 ? 28.269 50.568 69.920 1.00 32.60 ? 480 GLU A C 1 ATOM 3520 O O . GLU A 1 439 ? 28.121 49.732 70.808 1.00 34.94 ? 480 GLU A O 1 ATOM 3521 C CB A GLU A 1 439 ? 26.881 52.441 70.787 0.50 32.78 ? 480 GLU A CB 1 ATOM 3522 C CB B GLU A 1 439 ? 26.895 52.461 70.839 0.50 33.85 ? 480 GLU A CB 1 ATOM 3523 C CG A GLU A 1 439 ? 26.742 53.901 71.154 0.50 34.19 ? 480 GLU A CG 1 ATOM 3524 C CG B GLU A 1 439 ? 26.556 51.829 72.210 0.50 39.35 ? 480 GLU A CG 1 ATOM 3525 C CD A GLU A 1 439 ? 27.595 54.321 72.320 0.50 38.33 ? 480 GLU A CD 1 ATOM 3526 C CD B GLU A 1 439 ? 25.549 50.681 72.117 0.50 44.00 ? 480 GLU A CD 1 ATOM 3527 O OE1 A GLU A 1 439 ? 27.729 55.554 72.516 0.50 42.23 ? 480 GLU A OE1 1 ATOM 3528 O OE1 B GLU A 1 439 ? 24.468 50.900 71.531 0.50 46.61 ? 480 GLU A OE1 1 ATOM 3529 O OE2 A GLU A 1 439 ? 28.116 53.444 73.048 0.50 40.25 ? 480 GLU A OE2 1 ATOM 3530 O OE2 B GLU A 1 439 ? 25.836 49.570 72.633 0.50 47.38 ? 480 GLU A OE2 1 ATOM 3531 N N . LEU A 1 440 ? 28.450 50.227 68.639 1.00 29.90 ? 481 LEU A N 1 ATOM 3532 C CA . LEU A 1 440 ? 28.531 48.824 68.229 1.00 28.82 ? 481 LEU A CA 1 ATOM 3533 C C . LEU A 1 440 ? 29.975 48.359 68.043 1.00 30.39 ? 481 LEU A C 1 ATOM 3534 O O . LEU A 1 440 ? 30.838 49.151 67.653 1.00 32.06 ? 481 LEU A O 1 ATOM 3535 C CB . LEU A 1 440 ? 27.777 48.578 66.896 1.00 26.97 ? 481 LEU A CB 1 ATOM 3536 C CG . LEU A 1 440 ? 26.301 49.005 66.882 1.00 26.90 ? 481 LEU A CG 1 ATOM 3537 C CD1 . LEU A 1 440 ? 25.737 48.821 65.478 1.00 25.48 ? 481 LEU A CD1 1 ATOM 3538 C CD2 . LEU A 1 440 ? 25.518 48.151 67.875 1.00 28.19 ? 481 LEU A CD2 1 ATOM 3539 N N . LYS A 1 441 ? 30.187 47.070 68.277 1.00 30.25 ? 482 LYS A N 1 ATOM 3540 C CA A LYS A 1 441 ? 31.507 46.435 68.150 0.50 32.26 ? 482 LYS A CA 1 ATOM 3541 C CA B LYS A 1 441 ? 31.516 46.462 68.148 0.50 32.28 ? 482 LYS A CA 1 ATOM 3542 C C . LYS A 1 441 ? 31.824 46.210 66.677 1.00 31.51 ? 482 LYS A C 1 ATOM 3543 O O . LYS A 1 441 ? 30.941 45.778 65.913 1.00 32.19 ? 482 LYS A O 1 ATOM 3544 C CB A LYS A 1 441 ? 31.517 45.072 68.846 0.50 33.05 ? 482 LYS A CB 1 ATOM 3545 C CB B LYS A 1 441 ? 31.588 45.144 68.924 0.50 33.25 ? 482 LYS A CB 1 ATOM 3546 C CG A LYS A 1 441 ? 31.056 45.059 70.300 0.50 35.30 ? 482 LYS A CG 1 ATOM 3547 C CG B LYS A 1 441 ? 31.606 45.306 70.443 0.50 35.67 ? 482 LYS A CG 1 ATOM 3548 C CD A LYS A 1 441 ? 31.152 43.628 70.845 0.50 38.22 ? 482 LYS A CD 1 ATOM 3549 C CD B LYS A 1 441 ? 31.798 43.951 71.151 0.50 38.96 ? 482 LYS A CD 1 ATOM 3550 C CE A LYS A 1 441 ? 30.684 43.543 72.299 0.50 40.43 ? 482 LYS A CE 1 ATOM 3551 C CE B LYS A 1 441 ? 33.000 43.169 70.622 0.50 42.35 ? 482 LYS A CE 1 ATOM 3552 N NZ A LYS A 1 441 ? 31.241 44.647 73.118 0.50 45.48 ? 482 LYS A NZ 1 ATOM 3553 N NZ B LYS A 1 441 ? 33.405 42.038 71.525 0.50 45.34 ? 482 LYS A NZ 1 ATOM 3554 N N . SER A 1 442 ? 33.042 46.528 66.256 1.00 31.41 ? 483 SER A N 1 ATOM 3555 C CA . SER A 1 442 ? 33.458 46.154 64.887 1.00 31.76 ? 483 SER A CA 1 ATOM 3556 C C . SER A 1 442 ? 33.652 44.644 64.794 1.00 31.42 ? 483 SER A C 1 ATOM 3557 O O . SER A 1 442 ? 34.280 44.031 65.696 1.00 31.70 ? 483 SER A O 1 ATOM 3558 C CB . SER A 1 442 ? 34.777 46.828 64.472 1.00 32.03 ? 483 SER A CB 1 ATOM 3559 O OG . SER A 1 442 ? 35.134 46.385 63.160 1.00 32.29 ? 483 SER A OG 1 ATOM 3560 N N . PRO A 1 443 ? 33.170 44.024 63.707 1.00 30.01 ? 484 PRO A N 1 ATOM 3561 C CA . PRO A 1 443 ? 33.391 42.586 63.563 1.00 31.23 ? 484 PRO A CA 1 ATOM 3562 C C . PRO A 1 443 ? 34.667 42.308 62.774 1.00 32.21 ? 484 PRO A C 1 ATOM 3563 O O . PRO A 1 443 ? 34.969 41.139 62.512 1.00 32.74 ? 484 PRO A O 1 ATOM 3564 C CB . PRO A 1 443 ? 32.193 42.134 62.724 1.00 29.78 ? 484 PRO A CB 1 ATOM 3565 C CG . PRO A 1 443 ? 31.919 43.342 61.834 1.00 29.24 ? 484 PRO A CG 1 ATOM 3566 C CD . PRO A 1 443 ? 32.226 44.561 62.694 1.00 29.68 ? 484 PRO A CD 1 ATOM 3567 N N . ASP A 1 444 ? 35.381 43.361 62.373 1.00 32.35 ? 485 ASP A N 1 ATOM 3568 C CA . ASP A 1 444 ? 36.467 43.222 61.387 1.00 32.82 ? 485 ASP A CA 1 ATOM 3569 C C . ASP A 1 444 ? 37.748 42.710 62.020 1.00 34.24 ? 485 ASP A C 1 ATOM 3570 O O . ASP A 1 444 ? 38.077 43.103 63.149 1.00 34.33 ? 485 ASP A O 1 ATOM 3571 C CB . ASP A 1 444 ? 36.827 44.584 60.782 1.00 32.26 ? 485 ASP A CB 1 ATOM 3572 C CG . ASP A 1 444 ? 35.674 45.217 59.979 1.00 32.33 ? 485 ASP A CG 1 ATOM 3573 O OD1 . ASP A 1 444 ? 34.585 44.620 59.870 1.00 35.03 ? 485 ASP A OD1 1 ATOM 3574 O OD2 . ASP A 1 444 ? 35.884 46.324 59.448 1.00 33.30 ? 485 ASP A OD2 1 ATOM 3575 N N . GLU A 1 445 ? 38.473 41.874 61.279 1.00 35.13 ? 486 GLU A N 1 ATOM 3576 C CA A GLU A 1 445 ? 39.813 41.452 61.700 0.50 37.15 ? 486 GLU A CA 1 ATOM 3577 C CA B GLU A 1 445 ? 39.830 41.453 61.666 0.50 36.79 ? 486 GLU A CA 1 ATOM 3578 C C . GLU A 1 445 ? 40.718 42.680 61.872 1.00 37.22 ? 486 GLU A C 1 ATOM 3579 O O . GLU A 1 445 ? 40.759 43.575 61.021 1.00 37.78 ? 486 GLU A O 1 ATOM 3580 C CB A GLU A 1 445 ? 40.417 40.487 60.674 0.50 37.55 ? 486 GLU A CB 1 ATOM 3581 C CB B GLU A 1 445 ? 40.421 40.568 60.561 0.50 36.90 ? 486 GLU A CB 1 ATOM 3582 C CG A GLU A 1 445 ? 39.786 39.086 60.618 0.50 40.39 ? 486 GLU A CG 1 ATOM 3583 C CG B GLU A 1 445 ? 41.890 40.173 60.755 0.50 39.30 ? 486 GLU A CG 1 ATOM 3584 C CD A GLU A 1 445 ? 40.643 38.099 59.823 0.50 44.23 ? 486 GLU A CD 1 ATOM 3585 C CD B GLU A 1 445 ? 42.564 39.705 59.458 0.50 41.76 ? 486 GLU A CD 1 ATOM 3586 O OE1 A GLU A 1 445 ? 41.818 37.901 60.204 0.50 46.04 ? 486 GLU A OE1 1 ATOM 3587 O OE1 B GLU A 1 445 ? 41.918 39.708 58.379 0.50 43.65 ? 486 GLU A OE1 1 ATOM 3588 O OE2 A GLU A 1 445 ? 40.152 37.524 58.819 0.50 46.73 ? 486 GLU A OE2 1 ATOM 3589 O OE2 B GLU A 1 445 ? 43.753 39.345 59.523 0.50 43.26 ? 486 GLU A OE2 1 ATOM 3590 N N . GLY A 1 446 ? 41.433 42.745 62.993 1.00 38.97 ? 487 GLY A N 1 ATOM 3591 C CA . GLY A 1 446 ? 42.327 43.874 63.226 1.00 39.78 ? 487 GLY A CA 1 ATOM 3592 C C . GLY A 1 446 ? 41.695 45.027 63.986 1.00 40.44 ? 487 GLY A C 1 ATOM 3593 O O . GLY A 1 446 ? 42.394 45.950 64.401 1.00 42.18 ? 487 GLY A O 1 ATOM 3594 N N . PHE A 1 447 ? 40.374 44.973 64.171 1.00 38.22 ? 488 PHE A N 1 ATOM 3595 C CA . PHE A 1 447 ? 39.655 46.014 64.896 1.00 37.80 ? 488 PHE A CA 1 ATOM 3596 C C . PHE A 1 447 ? 38.944 45.433 66.108 1.00 38.85 ? 488 PHE A C 1 ATOM 3597 O O . PHE A 1 447 ? 37.929 45.980 66.562 1.00 37.44 ? 488 PHE A O 1 ATOM 3598 C CB . PHE A 1 447 ? 38.627 46.686 63.968 1.00 36.40 ? 488 PHE A CB 1 ATOM 3599 C CG . PHE A 1 447 ? 39.245 47.475 62.874 1.00 35.78 ? 488 PHE A CG 1 ATOM 3600 C CD1 . PHE A 1 447 ? 39.471 48.834 63.034 1.00 36.40 ? 488 PHE A CD1 1 ATOM 3601 C CD2 . PHE A 1 447 ? 39.636 46.853 61.686 1.00 36.27 ? 488 PHE A CD2 1 ATOM 3602 C CE1 . PHE A 1 447 ? 40.048 49.592 62.021 1.00 37.02 ? 488 PHE A CE1 1 ATOM 3603 C CE2 . PHE A 1 447 ? 40.194 47.613 60.651 1.00 37.34 ? 488 PHE A CE2 1 ATOM 3604 C CZ . PHE A 1 447 ? 40.418 48.973 60.831 1.00 38.28 ? 488 PHE A CZ 1 ATOM 3605 N N . GLU A 1 448 ? 39.458 44.329 66.638 1.00 40.07 ? 489 GLU A N 1 ATOM 3606 C CA . GLU A 1 448 ? 38.865 43.759 67.850 1.00 41.99 ? 489 GLU A CA 1 ATOM 3607 C C . GLU A 1 448 ? 38.929 44.769 69.013 1.00 41.76 ? 489 GLU A C 1 ATOM 3608 O O . GLU A 1 448 ? 39.961 45.405 69.267 1.00 43.87 ? 489 GLU A O 1 ATOM 3609 C CB . GLU A 1 448 ? 39.390 42.338 68.232 1.00 42.86 ? 489 GLU A CB 1 ATOM 3610 C CG . GLU A 1 448 ? 40.739 41.855 67.707 1.00 47.77 ? 489 GLU A CG 1 ATOM 3611 C CD . GLU A 1 448 ? 40.866 41.752 66.191 1.00 44.58 ? 489 GLU A CD 1 ATOM 3612 O OE1 . GLU A 1 448 ? 40.438 40.760 65.549 1.00 46.31 ? 489 GLU A OE1 1 ATOM 3613 O OE2 . GLU A 1 448 ? 41.495 42.667 65.647 1.00 47.24 ? 489 GLU A OE2 1 ATOM 3614 N N . GLY A 1 449 ? 37.794 44.975 69.672 1.00 40.87 ? 490 GLY A N 1 ATOM 3615 C CA . GLY A 1 449 ? 37.738 45.980 70.749 1.00 40.45 ? 490 GLY A CA 1 ATOM 3616 C C . GLY A 1 449 ? 37.489 47.410 70.268 1.00 38.62 ? 490 GLY A C 1 ATOM 3617 O O . GLY A 1 449 ? 37.410 48.335 71.079 1.00 40.45 ? 490 GLY A O 1 ATOM 3618 N N . LYS A 1 450 ? 37.378 47.606 68.954 1.00 35.96 ? 491 LYS A N 1 ATOM 3619 C CA A LYS A 1 450 ? 37.142 48.919 68.368 0.50 35.19 ? 491 LYS A CA 1 ATOM 3620 C CA B LYS A 1 450 ? 37.130 48.926 68.406 0.50 35.21 ? 491 LYS A CA 1 ATOM 3621 C C . LYS A 1 450 ? 35.680 49.007 67.956 1.00 33.17 ? 491 LYS A C 1 ATOM 3622 O O . LYS A 1 450 ? 35.023 47.981 67.776 1.00 32.93 ? 491 LYS A O 1 ATOM 3623 C CB A LYS A 1 450 ? 38.016 49.139 67.134 0.50 34.98 ? 491 LYS A CB 1 ATOM 3624 C CB B LYS A 1 450 ? 38.072 49.226 67.245 0.50 35.18 ? 491 LYS A CB 1 ATOM 3625 C CG A LYS A 1 450 ? 39.526 49.071 67.410 0.50 36.75 ? 491 LYS A CG 1 ATOM 3626 C CG B LYS A 1 450 ? 39.553 49.053 67.628 0.50 36.84 ? 491 LYS A CG 1 ATOM 3627 C CD A LYS A 1 450 ? 39.981 50.312 68.159 0.50 38.48 ? 491 LYS A CD 1 ATOM 3628 C CD B LYS A 1 450 ? 39.863 49.863 68.886 0.50 39.10 ? 491 LYS A CD 1 ATOM 3629 C CE A LYS A 1 450 ? 41.507 50.327 68.320 0.50 42.19 ? 491 LYS A CE 1 ATOM 3630 C CE B LYS A 1 450 ? 41.337 49.736 69.307 0.50 42.59 ? 491 LYS A CE 1 ATOM 3631 N NZ A LYS A 1 450 ? 42.186 50.393 66.996 0.50 43.21 ? 491 LYS A NZ 1 ATOM 3632 N NZ B LYS A 1 450 ? 41.599 48.494 70.080 0.50 44.74 ? 491 LYS A NZ 1 ATOM 3633 N N . SER A 1 451 ? 35.197 50.223 67.792 1.00 33.07 ? 492 SER A N 1 ATOM 3634 C CA . SER A 1 451 ? 33.796 50.432 67.392 1.00 31.09 ? 492 SER A CA 1 ATOM 3635 C C . SER A 1 451 ? 33.640 50.162 65.905 1.00 29.99 ? 492 SER A C 1 ATOM 3636 O O . SER A 1 451 ? 34.583 50.290 65.140 1.00 29.52 ? 492 SER A O 1 ATOM 3637 C CB . SER A 1 451 ? 33.358 51.862 67.699 1.00 32.18 ? 492 SER A CB 1 ATOM 3638 O OG . SER A 1 451 ? 33.908 52.781 66.767 1.00 33.08 ? 492 SER A OG 1 ATOM 3639 N N . LEU A 1 452 ? 32.417 49.850 65.497 1.00 28.67 ? 493 LEU A N 1 ATOM 3640 C CA . LEU A 1 452 ? 32.103 49.764 64.076 1.00 28.28 ? 493 LEU A CA 1 ATOM 3641 C C . LEU A 1 452 ? 32.347 51.132 63.418 1.00 28.81 ? 493 LEU A C 1 ATOM 3642 O O . LEU A 1 452 ? 32.817 51.197 62.277 1.00 27.88 ? 493 LEU A O 1 ATOM 3643 C CB . LEU A 1 452 ? 30.626 49.364 63.903 1.00 26.81 ? 493 LEU A CB 1 ATOM 3644 C CG . LEU A 1 452 ? 30.058 49.274 62.485 1.00 26.29 ? 493 LEU A CG 1 ATOM 3645 C CD1 . LEU A 1 452 ? 30.890 48.298 61.593 1.00 26.09 ? 493 LEU A CD1 1 ATOM 3646 C CD2 . LEU A 1 452 ? 28.589 48.821 62.556 1.00 25.08 ? 493 LEU A CD2 1 ATOM 3647 N N . TYR A 1 453 ? 32.018 52.236 64.114 1.00 28.38 ? 494 TYR A N 1 ATOM 3648 C CA . TYR A 1 453 ? 32.273 53.548 63.530 1.00 28.77 ? 494 TYR A CA 1 ATOM 3649 C C . TYR A 1 453 ? 33.755 53.683 63.154 1.00 29.08 ? 494 TYR A C 1 ATOM 3650 O O . TYR A 1 453 ? 34.063 54.238 62.101 1.00 29.77 ? 494 TYR A O 1 ATOM 3651 C CB . TYR A 1 453 ? 31.877 54.684 64.504 1.00 29.27 ? 494 TYR A CB 1 ATOM 3652 C CG . TYR A 1 453 ? 32.098 56.089 63.946 1.00 29.81 ? 494 TYR A CG 1 ATOM 3653 C CD1 . TYR A 1 453 ? 31.091 56.735 63.242 1.00 28.41 ? 494 TYR A CD1 1 ATOM 3654 C CD2 . TYR A 1 453 ? 33.304 56.763 64.133 1.00 31.74 ? 494 TYR A CD2 1 ATOM 3655 C CE1 . TYR A 1 453 ? 31.279 58.037 62.737 1.00 30.00 ? 494 TYR A CE1 1 ATOM 3656 C CE2 . TYR A 1 453 ? 33.503 58.056 63.630 1.00 31.05 ? 494 TYR A CE2 1 ATOM 3657 C CZ . TYR A 1 453 ? 32.483 58.687 62.937 1.00 31.94 ? 494 TYR A CZ 1 ATOM 3658 O OH . TYR A 1 453 ? 32.653 59.953 62.426 1.00 32.89 ? 494 TYR A OH 1 ATOM 3659 N N . GLU A 1 454 ? 34.644 53.232 64.036 1.00 29.44 ? 495 GLU A N 1 ATOM 3660 C CA A GLU A 1 454 ? 36.087 53.359 63.805 0.50 31.55 ? 495 GLU A CA 1 ATOM 3661 C CA B GLU A 1 454 ? 36.088 53.350 63.809 0.50 31.22 ? 495 GLU A CA 1 ATOM 3662 C C . GLU A 1 454 ? 36.533 52.580 62.559 1.00 31.01 ? 495 GLU A C 1 ATOM 3663 O O . GLU A 1 454 ? 37.209 53.138 61.697 1.00 31.51 ? 495 GLU A O 1 ATOM 3664 C CB A GLU A 1 454 ? 36.901 52.973 65.052 0.50 32.93 ? 495 GLU A CB 1 ATOM 3665 C CB B GLU A 1 454 ? 36.879 52.904 65.043 0.50 32.35 ? 495 GLU A CB 1 ATOM 3666 C CG A GLU A 1 454 ? 38.388 52.762 64.751 0.50 35.95 ? 495 GLU A CG 1 ATOM 3667 C CG B GLU A 1 454 ? 38.361 53.262 64.960 0.50 34.02 ? 495 GLU A CG 1 ATOM 3668 C CD A GLU A 1 454 ? 39.327 53.442 65.741 0.50 40.48 ? 495 GLU A CD 1 ATOM 3669 C CD B GLU A 1 454 ? 39.165 52.684 66.109 0.50 36.24 ? 495 GLU A CD 1 ATOM 3670 O OE1 A GLU A 1 454 ? 38.859 54.036 66.738 0.50 41.26 ? 495 GLU A OE1 1 ATOM 3671 O OE1 B GLU A 1 454 ? 38.721 52.843 67.265 0.50 38.06 ? 495 GLU A OE1 1 ATOM 3672 O OE2 A GLU A 1 454 ? 40.553 53.379 65.510 0.50 41.94 ? 495 GLU A OE2 1 ATOM 3673 O OE2 B GLU A 1 454 ? 40.242 52.083 65.865 0.50 35.80 ? 495 GLU A OE2 1 ATOM 3674 N N . SER A 1 455 ? 36.111 51.318 62.441 1.00 30.93 ? 496 SER A N 1 ATOM 3675 C CA . SER A 1 455 ? 36.514 50.489 61.280 1.00 31.20 ? 496 SER A CA 1 ATOM 3676 C C . SER A 1 455 ? 35.908 51.018 59.983 1.00 31.06 ? 496 SER A C 1 ATOM 3677 O O . SER A 1 455 ? 36.573 51.112 58.950 1.00 31.53 ? 496 SER A O 1 ATOM 3678 C CB . SER A 1 455 ? 36.212 48.983 61.481 1.00 31.79 ? 496 SER A CB 1 ATOM 3679 O OG . SER A 1 455 ? 34.835 48.696 61.697 1.00 30.95 ? 496 SER A OG 1 ATOM 3680 N N . TRP A 1 456 ? 34.624 51.354 60.040 1.00 29.43 ? 497 TRP A N 1 ATOM 3681 C CA . TRP A 1 456 ? 33.932 51.894 58.889 1.00 29.12 ? 497 TRP A CA 1 ATOM 3682 C C . TRP A 1 456 ? 34.573 53.191 58.395 1.00 30.04 ? 497 TRP A C 1 ATOM 3683 O O . TRP A 1 456 ? 34.752 53.372 57.185 1.00 29.12 ? 497 TRP A O 1 ATOM 3684 C CB . TRP A 1 456 ? 32.463 52.095 59.259 1.00 27.89 ? 497 TRP A CB 1 ATOM 3685 C CG . TRP A 1 456 ? 31.579 52.712 58.213 1.00 28.33 ? 497 TRP A CG 1 ATOM 3686 C CD1 . TRP A 1 456 ? 31.675 52.599 56.854 1.00 27.31 ? 497 TRP A CD1 1 ATOM 3687 C CD2 . TRP A 1 456 ? 30.421 53.484 58.477 1.00 26.49 ? 497 TRP A CD2 1 ATOM 3688 N NE1 . TRP A 1 456 ? 30.641 53.286 56.249 1.00 25.26 ? 497 TRP A NE1 1 ATOM 3689 C CE2 . TRP A 1 456 ? 29.865 53.861 57.225 1.00 26.31 ? 497 TRP A CE2 1 ATOM 3690 C CE3 . TRP A 1 456 ? 29.806 53.940 59.665 1.00 27.66 ? 497 TRP A CE3 1 ATOM 3691 C CZ2 . TRP A 1 456 ? 28.705 54.650 57.121 1.00 27.56 ? 497 TRP A CZ2 1 ATOM 3692 C CZ3 . TRP A 1 456 ? 28.655 54.713 59.562 1.00 27.33 ? 497 TRP A CZ3 1 ATOM 3693 C CH2 . TRP A 1 456 ? 28.119 55.076 58.288 1.00 27.80 ? 497 TRP A CH2 1 ATOM 3694 N N . THR A 1 457 ? 34.875 54.108 59.328 1.00 29.61 ? 498 THR A N 1 ATOM 3695 C CA . THR A 1 457 ? 35.458 55.383 58.955 1.00 31.77 ? 498 THR A CA 1 ATOM 3696 C C . THR A 1 457 ? 36.858 55.209 58.340 1.00 32.90 ? 498 THR A C 1 ATOM 3697 O O . THR A 1 457 ? 37.194 55.894 57.360 1.00 33.12 ? 498 THR A O 1 ATOM 3698 C CB . THR A 1 457 ? 35.470 56.354 60.157 1.00 33.00 ? 498 THR A CB 1 ATOM 3699 O OG1 A THR A 1 457 ? 34.112 56.648 60.501 1.00 31.70 ? 498 THR A OG1 1 ATOM 3700 C CG2 A THR A 1 457 ? 36.132 57.666 59.779 1.00 36.51 ? 498 THR A CG2 1 ATOM 3701 N N . LYS A 1 458 ? 37.611 54.256 58.868 1.00 33.60 ? 499 LYS A N 1 ATOM 3702 C CA A LYS A 1 458 ? 38.955 53.979 58.360 0.50 34.97 ? 499 LYS A CA 1 ATOM 3703 C CA B LYS A 1 458 ? 38.953 53.964 58.364 0.50 34.76 ? 499 LYS A CA 1 ATOM 3704 C C . LYS A 1 458 ? 38.880 53.418 56.936 1.00 34.59 ? 499 LYS A C 1 ATOM 3705 O O . LYS A 1 458 ? 39.635 53.842 56.058 1.00 35.68 ? 499 LYS A O 1 ATOM 3706 C CB A LYS A 1 458 ? 39.718 53.041 59.303 0.50 35.85 ? 499 LYS A CB 1 ATOM 3707 C CB B LYS A 1 458 ? 39.680 52.986 59.291 0.50 35.58 ? 499 LYS A CB 1 ATOM 3708 C CG A LYS A 1 458 ? 41.229 52.959 59.047 0.50 38.96 ? 499 LYS A CG 1 ATOM 3709 C CG B LYS A 1 458 ? 41.066 52.574 58.799 0.50 37.26 ? 499 LYS A CG 1 ATOM 3710 C CD A LYS A 1 458 ? 41.935 52.287 60.230 0.50 41.18 ? 499 LYS A CD 1 ATOM 3711 C CD B LYS A 1 458 ? 42.054 53.723 58.967 0.50 40.13 ? 499 LYS A CD 1 ATOM 3712 C CE A LYS A 1 458 ? 43.321 52.882 60.534 0.50 42.91 ? 499 LYS A CE 1 ATOM 3713 C CE B LYS A 1 458 ? 43.461 53.298 58.556 0.50 40.55 ? 499 LYS A CE 1 ATOM 3714 N NZ A LYS A 1 458 ? 44.405 52.160 59.809 0.50 45.41 ? 499 LYS A NZ 1 ATOM 3715 N NZ B LYS A 1 458 ? 44.344 54.482 58.512 0.50 42.93 ? 499 LYS A NZ 1 ATOM 3716 N N . LYS A 1 459 ? 37.929 52.514 56.696 1.00 32.79 ? 500 LYS A N 1 ATOM 3717 C CA . LYS A 1 459 ? 37.842 51.785 55.411 1.00 32.43 ? 500 LYS A CA 1 ATOM 3718 C C . LYS A 1 459 ? 37.086 52.503 54.317 1.00 33.49 ? 500 LYS A C 1 ATOM 3719 O O . LYS A 1 459 ? 37.293 52.222 53.126 1.00 34.13 ? 500 LYS A O 1 ATOM 3720 C CB . LYS A 1 459 ? 37.227 50.422 55.646 1.00 32.45 ? 500 LYS A CB 1 ATOM 3721 C CG . LYS A 1 459 ? 38.170 49.478 56.431 1.00 32.50 ? 500 LYS A CG 1 ATOM 3722 C CD . LYS A 1 459 ? 37.497 48.119 56.664 1.00 33.77 ? 500 LYS A CD 1 ATOM 3723 C CE . LYS A 1 459 ? 38.472 47.125 57.253 1.00 36.67 ? 500 LYS A CE 1 ATOM 3724 N NZ . LYS A 1 459 ? 37.849 45.781 57.473 1.00 34.92 ? 500 LYS A NZ 1 ATOM 3725 N N . SER A 1 460 ? 36.178 53.381 54.725 1.00 31.80 ? 501 SER A N 1 ATOM 3726 C CA . SER A 1 460 ? 35.312 54.099 53.790 1.00 32.17 ? 501 SER A CA 1 ATOM 3727 C C . SER A 1 460 ? 35.181 55.575 54.203 1.00 33.60 ? 501 SER A C 1 ATOM 3728 O O . SER A 1 460 ? 34.124 56.021 54.644 1.00 32.89 ? 501 SER A O 1 ATOM 3729 C CB . SER A 1 460 ? 33.948 53.409 53.746 1.00 31.08 ? 501 SER A CB 1 ATOM 3730 O OG . SER A 1 460 ? 33.192 53.873 52.648 1.00 34.27 ? 501 SER A OG 1 ATOM 3731 N N . PRO A 1 461 ? 36.290 56.335 54.074 1.00 35.09 ? 502 PRO A N 1 ATOM 3732 C CA . PRO A 1 461 ? 36.321 57.715 54.503 1.00 36.81 ? 502 PRO A CA 1 ATOM 3733 C C . PRO A 1 461 ? 35.396 58.575 53.670 1.00 37.78 ? 502 PRO A C 1 ATOM 3734 O O . PRO A 1 461 ? 35.249 58.370 52.462 1.00 37.24 ? 502 PRO A O 1 ATOM 3735 C CB . PRO A 1 461 ? 37.798 58.132 54.306 1.00 37.90 ? 502 PRO A CB 1 ATOM 3736 C CG . PRO A 1 461 ? 38.402 57.087 53.453 1.00 37.81 ? 502 PRO A CG 1 ATOM 3737 C CD . PRO A 1 461 ? 37.610 55.845 53.628 1.00 35.97 ? 502 PRO A CD 1 ATOM 3738 N N . SER A 1 462 ? 34.762 59.528 54.338 1.00 39.33 ? 503 SER A N 1 ATOM 3739 C CA . SER A 1 462 ? 34.009 60.562 53.676 1.00 42.67 ? 503 SER A CA 1 ATOM 3740 C C . SER A 1 462 ? 34.948 61.334 52.766 1.00 44.87 ? 503 SER A C 1 ATOM 3741 O O . SER A 1 462 ? 36.068 61.666 53.181 1.00 46.36 ? 503 SER A O 1 ATOM 3742 C CB . SER A 1 462 ? 33.448 61.527 54.719 1.00 42.22 ? 503 SER A CB 1 ATOM 3743 O OG . SER A 1 462 ? 32.905 62.655 54.074 1.00 46.11 ? 503 SER A OG 1 ATOM 3744 N N . PRO A 1 463 ? 34.510 61.596 51.525 1.00 46.76 ? 504 PRO A N 1 ATOM 3745 C CA . PRO A 1 463 ? 35.244 62.471 50.594 1.00 49.64 ? 504 PRO A CA 1 ATOM 3746 C C . PRO A 1 463 ? 35.260 63.936 51.083 1.00 52.45 ? 504 PRO A C 1 ATOM 3747 O O . PRO A 1 463 ? 36.213 64.684 50.804 1.00 53.67 ? 504 PRO A O 1 ATOM 3748 C CB . PRO A 1 463 ? 34.468 62.331 49.276 1.00 48.64 ? 504 PRO A CB 1 ATOM 3749 C CG . PRO A 1 463 ? 33.117 61.772 49.662 1.00 47.03 ? 504 PRO A CG 1 ATOM 3750 C CD . PRO A 1 463 ? 33.312 60.987 50.916 1.00 45.95 ? 504 PRO A CD 1 ATOM 3751 N N . GLU A 1 464 ? 34.233 64.311 51.848 1.00 54.23 ? 505 GLU A N 1 ATOM 3752 C CA . GLU A 1 464 ? 34.088 65.672 52.396 1.00 56.74 ? 505 GLU A CA 1 ATOM 3753 C C . GLU A 1 464 ? 34.831 65.922 53.726 1.00 57.80 ? 505 GLU A C 1 ATOM 3754 O O . GLU A 1 464 ? 35.550 66.916 53.850 1.00 58.74 ? 505 GLU A O 1 ATOM 3755 C CB . GLU A 1 464 ? 32.601 66.034 52.566 1.00 56.45 ? 505 GLU A CB 1 ATOM 3756 C CG . GLU A 1 464 ? 31.641 65.532 51.465 1.00 59.67 ? 505 GLU A CG 1 ATOM 3757 C CD . GLU A 1 464 ? 31.745 66.318 50.152 1.00 65.21 ? 505 GLU A CD 1 ATOM 3758 O OE1 . GLU A 1 464 ? 32.264 67.466 50.158 1.00 67.71 ? 505 GLU A OE1 1 ATOM 3759 O OE2 . GLU A 1 464 ? 31.288 65.784 49.109 1.00 67.15 ? 505 GLU A OE2 1 ATOM 3760 N N . PHE A 1 465 ? 34.655 65.042 54.717 1.00 57.75 ? 506 PHE A N 1 ATOM 3761 C CA . PHE A 1 465 ? 35.096 65.363 56.077 1.00 58.49 ? 506 PHE A CA 1 ATOM 3762 C C . PHE A 1 465 ? 36.015 64.342 56.718 1.00 58.26 ? 506 PHE A C 1 ATOM 3763 O O . PHE A 1 465 ? 35.780 63.124 56.659 1.00 57.87 ? 506 PHE A O 1 ATOM 3764 C CB . PHE A 1 465 ? 33.900 65.631 57.001 1.00 58.92 ? 506 PHE A CB 1 ATOM 3765 C CG . PHE A 1 465 ? 32.805 66.461 56.369 1.00 60.38 ? 506 PHE A CG 1 ATOM 3766 C CD1 . PHE A 1 465 ? 31.687 65.844 55.806 1.00 60.60 ? 506 PHE A CD1 1 ATOM 3767 C CD2 . PHE A 1 465 ? 32.888 67.859 56.343 1.00 62.74 ? 506 PHE A CD2 1 ATOM 3768 C CE1 . PHE A 1 465 ? 30.667 66.596 55.220 1.00 61.38 ? 506 PHE A CE1 1 ATOM 3769 C CE2 . PHE A 1 465 ? 31.869 68.624 55.752 1.00 63.68 ? 506 PHE A CE2 1 ATOM 3770 C CZ . PHE A 1 465 ? 30.754 67.983 55.191 1.00 62.38 ? 506 PHE A CZ 1 ATOM 3771 N N . SER A 1 466 ? 37.056 64.860 57.353 1.00 57.96 ? 507 SER A N 1 ATOM 3772 C CA . SER A 1 466 ? 38.027 64.037 58.058 1.00 56.90 ? 507 SER A CA 1 ATOM 3773 C C . SER A 1 466 ? 37.379 63.368 59.263 1.00 54.68 ? 507 SER A C 1 ATOM 3774 O O . SER A 1 466 ? 36.610 64.007 60.007 1.00 54.85 ? 507 SER A O 1 ATOM 3775 C CB . SER A 1 466 ? 39.221 64.887 58.517 1.00 58.67 ? 507 SER A CB 1 ATOM 3776 O OG . SER A 1 466 ? 40.396 64.521 57.816 1.00 60.93 ? 507 SER A OG 1 ATOM 3777 N N . GLY A 1 467 ? 37.677 62.084 59.444 1.00 51.50 ? 508 GLY A N 1 ATOM 3778 C CA . GLY A 1 467 ? 37.223 61.366 60.633 1.00 48.34 ? 508 GLY A CA 1 ATOM 3779 C C . GLY A 1 467 ? 35.742 61.008 60.599 1.00 44.04 ? 508 GLY A C 1 ATOM 3780 O O . GLY A 1 467 ? 35.167 60.646 61.638 1.00 43.52 ? 508 GLY A O 1 ATOM 3781 N N . MET A 1 468 ? 35.145 61.146 59.413 1.00 41.71 ? 509 MET A N 1 ATOM 3782 C CA A MET A 1 468 ? 33.745 60.747 59.127 0.50 39.63 ? 509 MET A CA 1 ATOM 3783 C CA B MET A 1 468 ? 33.789 60.654 59.187 0.50 39.88 ? 509 MET A CA 1 ATOM 3784 C C . MET A 1 468 ? 33.681 59.645 58.055 1.00 38.31 ? 509 MET A C 1 ATOM 3785 O O . MET A 1 468 ? 34.483 59.653 57.128 1.00 37.94 ? 509 MET A O 1 ATOM 3786 C CB A MET A 1 468 ? 32.933 61.925 58.588 0.50 39.13 ? 509 MET A CB 1 ATOM 3787 C CB B MET A 1 468 ? 32.833 61.792 58.940 0.50 39.30 ? 509 MET A CB 1 ATOM 3788 C CG A MET A 1 468 ? 33.035 63.226 59.371 0.50 40.53 ? 509 MET A CG 1 ATOM 3789 C CG B MET A 1 468 ? 32.099 62.164 60.185 0.50 41.56 ? 509 MET A CG 1 ATOM 3790 S SD A MET A 1 468 ? 32.433 63.034 61.044 0.50 41.74 ? 509 MET A SD 1 ATOM 3791 S SD B MET A 1 468 ? 31.485 63.815 60.041 0.50 42.19 ? 509 MET A SD 1 ATOM 3792 C CE A MET A 1 468 ? 30.730 62.602 60.732 0.50 38.28 ? 509 MET A CE 1 ATOM 3793 C CE B MET A 1 468 ? 30.908 63.793 58.364 0.50 42.43 ? 509 MET A CE 1 ATOM 3794 N N . PRO A 1 469 ? 32.674 58.749 58.138 1.00 35.90 ? 510 PRO A N 1 ATOM 3795 C CA . PRO A 1 469 ? 32.519 57.749 57.075 1.00 34.28 ? 510 PRO A CA 1 ATOM 3796 C C . PRO A 1 469 ? 31.669 58.230 55.895 1.00 32.16 ? 510 PRO A C 1 ATOM 3797 O O . PRO A 1 469 ? 30.909 59.194 56.012 1.00 31.83 ? 510 PRO A O 1 ATOM 3798 C CB . PRO A 1 469 ? 31.801 56.608 57.802 1.00 33.82 ? 510 PRO A CB 1 ATOM 3799 C CG . PRO A 1 469 ? 30.886 57.333 58.791 1.00 34.29 ? 510 PRO A CG 1 ATOM 3800 C CD . PRO A 1 469 ? 31.745 58.509 59.261 1.00 35.63 ? 510 PRO A CD 1 ATOM 3801 N N . ARG A 1 470 ? 31.752 57.532 54.767 1.00 30.57 ? 511 ARG A N 1 ATOM 3802 C CA . ARG A 1 470 ? 30.928 57.842 53.624 1.00 29.38 ? 511 ARG A CA 1 ATOM 3803 C C . ARG A 1 470 ? 29.484 57.329 53.825 1.00 28.00 ? 511 ARG A C 1 ATOM 3804 O O . ARG A 1 470 ? 29.259 56.188 54.220 1.00 27.19 ? 511 ARG A O 1 ATOM 3805 C CB . ARG A 1 470 ? 31.542 57.141 52.384 1.00 30.86 ? 511 ARG A CB 1 ATOM 3806 C CG . ARG A 1 470 ? 30.776 57.328 51.095 1.00 31.54 ? 511 ARG A CG 1 ATOM 3807 C CD . ARG A 1 470 ? 31.375 56.435 49.998 1.00 37.42 ? 511 ARG A CD 1 ATOM 3808 N NE . ARG A 1 470 ? 32.698 56.925 49.621 1.00 40.67 ? 511 ARG A NE 1 ATOM 3809 C CZ . ARG A 1 470 ? 32.914 57.819 48.651 1.00 45.34 ? 511 ARG A CZ 1 ATOM 3810 N NH1 . ARG A 1 470 ? 31.889 58.312 47.953 1.00 46.07 ? 511 ARG A NH1 1 ATOM 3811 N NH2 . ARG A 1 470 ? 34.158 58.215 48.370 1.00 46.19 ? 511 ARG A NH2 1 ATOM 3812 N N . ILE A 1 471 ? 28.506 58.187 53.562 1.00 26.05 ? 512 ILE A N 1 ATOM 3813 C CA . ILE A 1 471 ? 27.102 57.772 53.459 1.00 25.91 ? 512 ILE A CA 1 ATOM 3814 C C . ILE A 1 471 ? 26.558 58.322 52.146 1.00 26.37 ? 512 ILE A C 1 ATOM 3815 O O . ILE A 1 471 ? 26.729 59.529 51.879 1.00 28.53 ? 512 ILE A O 1 ATOM 3816 C CB . ILE A 1 471 ? 26.243 58.360 54.640 1.00 24.29 ? 512 ILE A CB 1 ATOM 3817 C CG1 . ILE A 1 471 ? 26.759 57.846 56.011 1.00 27.80 ? 512 ILE A CG1 1 ATOM 3818 C CG2 . ILE A 1 471 ? 24.713 58.074 54.375 1.00 23.37 ? 512 ILE A CG2 1 ATOM 3819 C CD1 . ILE A 1 471 ? 25.961 58.379 57.263 1.00 28.31 ? 512 ILE A CD1 1 ATOM 3820 N N . SER A 1 472 ? 25.930 57.479 51.335 1.00 25.17 ? 513 SER A N 1 ATOM 3821 C CA . SER A 1 472 ? 25.547 57.892 50.000 1.00 25.28 ? 513 SER A CA 1 ATOM 3822 C C . SER A 1 472 ? 24.090 58.289 49.943 1.00 25.27 ? 513 SER A C 1 ATOM 3823 O O . SER A 1 472 ? 23.367 58.095 50.904 1.00 23.88 ? 513 SER A O 1 ATOM 3824 C CB . SER A 1 472 ? 25.849 56.800 48.979 1.00 26.16 ? 513 SER A CB 1 ATOM 3825 O OG . SER A 1 472 ? 27.288 56.667 48.933 1.00 28.57 ? 513 SER A OG 1 ATOM 3826 N N A LYS A 1 473 ? 23.697 58.826 48.797 0.70 25.42 ? 514 LYS A N 1 ATOM 3827 N N B LYS A 1 473 ? 23.669 58.780 48.774 0.30 25.08 ? 514 LYS A N 1 ATOM 3828 C CA A LYS A 1 473 ? 22.311 59.265 48.567 0.70 24.70 ? 514 LYS A CA 1 ATOM 3829 C CA B LYS A 1 473 ? 22.291 59.264 48.565 0.30 24.46 ? 514 LYS A CA 1 ATOM 3830 C C A LYS A 1 473 ? 21.459 58.049 48.240 0.70 25.60 ? 514 LYS A C 1 ATOM 3831 C C B LYS A 1 473 ? 21.352 58.258 47.891 0.30 24.51 ? 514 LYS A C 1 ATOM 3832 O O A LYS A 1 473 ? 21.972 57.027 47.761 0.70 26.18 ? 514 LYS A O 1 ATOM 3833 O O B LYS A 1 473 ? 21.675 57.578 46.895 0.30 22.16 ? 514 LYS A O 1 ATOM 3834 C CB A LYS A 1 473 ? 22.287 60.241 47.386 0.70 24.85 ? 514 LYS A CB 1 ATOM 3835 C CB B LYS A 1 473 ? 22.276 60.585 47.793 0.30 25.18 ? 514 LYS A CB 1 ATOM 3836 C CG A LYS A 1 473 ? 23.171 61.487 47.633 0.70 23.75 ? 514 LYS A CG 1 ATOM 3837 C CG B LYS A 1 473 ? 22.761 60.478 46.375 0.30 25.07 ? 514 LYS A CG 1 ATOM 3838 C CD A LYS A 1 473 ? 23.045 62.546 46.540 0.70 24.99 ? 514 LYS A CD 1 ATOM 3839 C CD B LYS A 1 473 ? 22.712 61.819 45.679 0.30 25.56 ? 514 LYS A CD 1 ATOM 3840 C CE A LYS A 1 473 ? 23.696 62.144 45.241 0.70 26.69 ? 514 LYS A CE 1 ATOM 3841 C CE B LYS A 1 473 ? 23.399 62.910 46.475 0.30 26.69 ? 514 LYS A CE 1 ATOM 3842 N NZ A LYS A 1 473 ? 25.194 62.209 45.335 0.70 26.91 ? 514 LYS A NZ 1 ATOM 3843 N NZ B LYS A 1 473 ? 24.873 62.898 46.265 0.30 28.80 ? 514 LYS A NZ 1 ATOM 3844 N N . LEU A 1 474 ? 20.156 58.187 48.442 1.00 24.71 ? 515 LEU A N 1 ATOM 3845 C CA . LEU A 1 474 ? 19.176 57.206 47.960 1.00 25.23 ? 515 LEU A CA 1 ATOM 3846 C C . LEU A 1 474 ? 18.665 57.495 46.541 1.00 27.05 ? 515 LEU A C 1 ATOM 3847 O O . LEU A 1 474 ? 18.195 58.596 46.229 1.00 29.13 ? 515 LEU A O 1 ATOM 3848 C CB . LEU A 1 474 ? 17.969 57.188 48.924 1.00 24.65 ? 515 LEU A CB 1 ATOM 3849 C CG . LEU A 1 474 ? 18.184 56.678 50.361 1.00 22.26 ? 515 LEU A CG 1 ATOM 3850 C CD1 . LEU A 1 474 ? 16.953 57.092 51.237 1.00 22.20 ? 515 LEU A CD1 1 ATOM 3851 C CD2 . LEU A 1 474 ? 18.387 55.147 50.446 1.00 21.52 ? 515 LEU A CD2 1 ATOM 3852 N N . GLY A 1 475 ? 18.653 56.453 45.702 1.00 27.87 ? 516 GLY A N 1 ATOM 3853 C CA . GLY A 1 475 ? 17.961 56.553 44.428 1.00 26.53 ? 516 GLY A CA 1 ATOM 3854 C C . GLY A 1 475 ? 16.833 55.544 44.387 1.00 24.84 ? 516 GLY A C 1 ATOM 3855 O O . GLY A 1 475 ? 15.813 55.687 45.054 1.00 24.50 ? 516 GLY A O 1 ATOM 3856 N N . SER A 1 476 ? 16.952 54.546 43.493 1.00 25.11 ? 517 SER A N 1 ATOM 3857 C CA . SER A 1 476 ? 16.013 53.472 43.514 1.00 23.60 ? 517 SER A CA 1 ATOM 3858 C C . SER A 1 476 ? 16.751 52.103 43.494 1.00 22.04 ? 517 SER A C 1 ATOM 3859 O O . SER A 1 476 ? 17.914 51.957 43.887 1.00 25.58 ? 517 SER A O 1 ATOM 3860 C CB . SER A 1 476 ? 15.051 53.619 42.338 1.00 25.57 ? 517 SER A CB 1 ATOM 3861 O OG . SER A 1 476 ? 14.123 52.528 42.211 1.00 30.45 ? 517 SER A OG 1 ATOM 3862 N N . GLY A 1 477 ? 16.041 51.085 43.035 1.00 19.63 ? 518 GLY A N 1 ATOM 3863 C CA . GLY A 1 477 ? 16.611 49.744 42.957 1.00 19.91 ? 518 GLY A CA 1 ATOM 3864 C C . GLY A 1 477 ? 16.164 48.853 44.111 1.00 18.65 ? 518 GLY A C 1 ATOM 3865 O O . GLY A 1 477 ? 16.555 47.680 44.170 1.00 19.72 ? 518 GLY A O 1 ATOM 3866 N N . ASN A 1 478 ? 15.432 49.421 45.089 1.00 16.85 ? 519 ASN A N 1 ATOM 3867 C CA . ASN A 1 478 ? 14.947 48.575 46.208 1.00 16.96 ? 519 ASN A CA 1 ATOM 3868 C C . ASN A 1 478 ? 13.713 49.157 46.851 1.00 17.23 ? 519 ASN A C 1 ATOM 3869 O O . ASN A 1 478 ? 13.290 50.250 46.453 1.00 16.31 ? 519 ASN A O 1 ATOM 3870 C CB . ASN A 1 478 ? 16.059 48.286 47.229 1.00 16.73 ? 519 ASN A CB 1 ATOM 3871 C CG . ASN A 1 478 ? 16.034 46.857 47.657 1.00 19.02 ? 519 ASN A CG 1 ATOM 3872 O OD1 . ASN A 1 478 ? 15.049 46.390 48.272 1.00 20.28 ? 519 ASN A OD1 1 ATOM 3873 N ND2 . ASN A 1 478 ? 17.090 46.122 47.295 1.00 18.05 ? 519 ASN A ND2 1 ATOM 3874 N N . ASP A 1 479 ? 13.152 48.469 47.847 1.00 16.28 ? 520 ASP A N 1 ATOM 3875 C CA . ASP A 1 479 ? 11.759 48.711 48.279 1.00 16.13 ? 520 ASP A CA 1 ATOM 3876 C C . ASP A 1 479 ? 11.545 49.985 49.067 1.00 15.98 ? 520 ASP A C 1 ATOM 3877 O O . ASP A 1 479 ? 10.414 50.363 49.278 1.00 16.81 ? 520 ASP A O 1 ATOM 3878 C CB . ASP A 1 479 ? 11.273 47.519 49.120 1.00 16.13 ? 520 ASP A CB 1 ATOM 3879 C CG . ASP A 1 479 ? 10.920 46.300 48.250 1.00 18.86 ? 520 ASP A CG 1 ATOM 3880 O OD1 . ASP A 1 479 ? 10.219 46.477 47.220 1.00 18.41 ? 520 ASP A OD1 1 ATOM 3881 O OD2 . ASP A 1 479 ? 11.355 45.170 48.576 1.00 18.10 ? 520 ASP A OD2 1 ATOM 3882 N N . PHE A 1 480 ? 12.612 50.691 49.430 1.00 16.07 ? 521 PHE A N 1 ATOM 3883 C CA . PHE A 1 480 ? 12.436 52.004 50.055 1.00 17.29 ? 521 PHE A CA 1 ATOM 3884 C C . PHE A 1 480 ? 11.920 53.057 49.048 1.00 16.81 ? 521 PHE A C 1 ATOM 3885 O O . PHE A 1 480 ? 11.554 54.146 49.453 1.00 16.56 ? 521 PHE A O 1 ATOM 3886 C CB . PHE A 1 480 ? 13.802 52.488 50.632 1.00 18.03 ? 521 PHE A CB 1 ATOM 3887 C CG . PHE A 1 480 ? 14.857 52.707 49.538 1.00 16.97 ? 521 PHE A CG 1 ATOM 3888 C CD1 . PHE A 1 480 ? 14.903 53.928 48.812 1.00 18.04 ? 521 PHE A CD1 1 ATOM 3889 C CD2 . PHE A 1 480 ? 15.735 51.668 49.205 1.00 21.63 ? 521 PHE A CD2 1 ATOM 3890 C CE1 . PHE A 1 480 ? 15.851 54.052 47.756 1.00 20.39 ? 521 PHE A CE1 1 ATOM 3891 C CE2 . PHE A 1 480 ? 16.672 51.815 48.163 1.00 21.18 ? 521 PHE A CE2 1 ATOM 3892 C CZ . PHE A 1 480 ? 16.669 52.993 47.432 1.00 21.91 ? 521 PHE A CZ 1 ATOM 3893 N N . GLU A 1 481 ? 11.978 52.771 47.732 1.00 15.50 ? 522 GLU A N 1 ATOM 3894 C CA . GLU A 1 481 ? 11.750 53.827 46.723 1.00 16.70 ? 522 GLU A CA 1 ATOM 3895 C C . GLU A 1 481 ? 10.405 54.519 46.933 1.00 16.04 ? 522 GLU A C 1 ATOM 3896 O O . GLU A 1 481 ? 10.331 55.770 46.930 1.00 16.24 ? 522 GLU A O 1 ATOM 3897 C CB . GLU A 1 481 ? 11.796 53.237 45.298 1.00 17.68 ? 522 GLU A CB 1 ATOM 3898 C CG . GLU A 1 481 ? 11.772 54.333 44.174 1.00 18.74 ? 522 GLU A CG 1 ATOM 3899 C CD . GLU A 1 481 ? 11.311 53.711 42.841 1.00 28.73 ? 522 GLU A CD 1 ATOM 3900 O OE1 . GLU A 1 481 ? 10.148 53.255 42.746 1.00 33.74 ? 522 GLU A OE1 1 ATOM 3901 O OE2 . GLU A 1 481 ? 12.093 53.653 41.897 1.00 28.69 ? 522 GLU A OE2 1 ATOM 3902 N N . VAL A 1 482 ? 9.305 53.754 47.070 1.00 14.81 ? 523 VAL A N 1 ATOM 3903 C CA . VAL A 1 482 ? 8.008 54.435 47.177 1.00 16.12 ? 523 VAL A CA 1 ATOM 3904 C C . VAL A 1 482 ? 7.915 55.283 48.453 1.00 16.22 ? 523 VAL A C 1 ATOM 3905 O O . VAL A 1 482 ? 7.357 56.357 48.435 1.00 16.68 ? 523 VAL A O 1 ATOM 3906 C CB . VAL A 1 482 ? 6.858 53.423 47.078 1.00 17.20 ? 523 VAL A CB 1 ATOM 3907 C CG1 . VAL A 1 482 ? 6.845 52.429 48.305 1.00 16.58 ? 523 VAL A CG1 1 ATOM 3908 C CG2 . VAL A 1 482 ? 5.517 54.118 46.905 1.00 16.70 ? 523 VAL A CG2 1 ATOM 3909 N N . PHE A 1 483 ? 8.487 54.775 49.533 1.00 15.02 ? 524 PHE A N 1 ATOM 3910 C CA . PHE A 1 483 ? 8.392 55.503 50.808 1.00 15.15 ? 524 PHE A CA 1 ATOM 3911 C C . PHE A 1 483 ? 9.156 56.808 50.753 1.00 15.52 ? 524 PHE A C 1 ATOM 3912 O O . PHE A 1 483 ? 8.649 57.828 51.261 1.00 16.76 ? 524 PHE A O 1 ATOM 3913 C CB . PHE A 1 483 ? 8.953 54.606 51.926 1.00 15.39 ? 524 PHE A CB 1 ATOM 3914 C CG . PHE A 1 483 ? 8.163 53.350 52.062 1.00 16.75 ? 524 PHE A CG 1 ATOM 3915 C CD1 . PHE A 1 483 ? 6.919 53.399 52.728 1.00 18.11 ? 524 PHE A CD1 1 ATOM 3916 C CD2 . PHE A 1 483 ? 8.595 52.162 51.482 1.00 17.30 ? 524 PHE A CD2 1 ATOM 3917 C CE1 . PHE A 1 483 ? 6.125 52.221 52.838 1.00 21.66 ? 524 PHE A CE1 1 ATOM 3918 C CE2 . PHE A 1 483 ? 7.830 50.992 51.564 1.00 16.06 ? 524 PHE A CE2 1 ATOM 3919 C CZ . PHE A 1 483 ? 6.597 51.021 52.243 1.00 19.56 ? 524 PHE A CZ 1 ATOM 3920 N N . PHE A 1 484 ? 10.330 56.792 50.147 1.00 15.81 ? 525 PHE A N 1 ATOM 3921 C CA . PHE A 1 484 ? 11.198 57.981 50.150 1.00 15.48 ? 525 PHE A CA 1 ATOM 3922 C C . PHE A 1 484 ? 10.884 58.912 48.968 1.00 15.85 ? 525 PHE A C 1 ATOM 3923 O O . PHE A 1 484 ? 10.534 60.090 49.195 1.00 15.83 ? 525 PHE A O 1 ATOM 3924 C CB . PHE A 1 484 ? 12.682 57.557 50.098 1.00 16.30 ? 525 PHE A CB 1 ATOM 3925 C CG . PHE A 1 484 ? 13.601 58.704 50.304 1.00 15.76 ? 525 PHE A CG 1 ATOM 3926 C CD1 . PHE A 1 484 ? 13.568 59.412 51.531 1.00 16.41 ? 525 PHE A CD1 1 ATOM 3927 C CD2 . PHE A 1 484 ? 14.500 59.076 49.302 1.00 18.77 ? 525 PHE A CD2 1 ATOM 3928 C CE1 . PHE A 1 484 ? 14.481 60.471 51.790 1.00 19.63 ? 525 PHE A CE1 1 ATOM 3929 C CE2 . PHE A 1 484 ? 15.412 60.173 49.544 1.00 20.86 ? 525 PHE A CE2 1 ATOM 3930 C CZ . PHE A 1 484 ? 15.373 60.874 50.782 1.00 19.58 ? 525 PHE A CZ 1 ATOM 3931 N N . GLN A 1 485 ? 10.961 58.394 47.730 1.00 15.77 ? 526 GLN A N 1 ATOM 3932 C CA . GLN A 1 485 ? 10.838 59.252 46.543 1.00 15.94 ? 526 GLN A CA 1 ATOM 3933 C C . GLN A 1 485 ? 9.366 59.672 46.247 1.00 15.19 ? 526 GLN A C 1 ATOM 3934 O O . GLN A 1 485 ? 9.134 60.771 45.701 1.00 16.77 ? 526 GLN A O 1 ATOM 3935 C CB A GLN A 1 485 ? 11.367 58.451 45.283 0.65 16.76 ? 526 GLN A CB 1 ATOM 3936 C CB B GLN A 1 485 ? 11.530 58.633 45.312 0.35 17.11 ? 526 GLN A CB 1 ATOM 3937 C CG A GLN A 1 485 ? 12.813 57.830 45.394 0.65 15.77 ? 526 GLN A CG 1 ATOM 3938 C CG B GLN A 1 485 ? 13.042 58.863 45.275 0.35 20.32 ? 526 GLN A CG 1 ATOM 3939 C CD A GLN A 1 485 ? 13.899 58.916 45.548 0.65 14.04 ? 526 GLN A CD 1 ATOM 3940 C CD B GLN A 1 485 ? 13.835 57.728 45.897 0.35 20.77 ? 526 GLN A CD 1 ATOM 3941 O OE1 A GLN A 1 485 ? 13.568 60.078 45.482 0.65 15.03 ? 526 GLN A OE1 1 ATOM 3942 O OE1 B GLN A 1 485 ? 13.263 56.787 46.471 0.35 23.18 ? 526 GLN A OE1 1 ATOM 3943 N NE2 A GLN A 1 485 ? 15.168 58.546 45.702 0.65 16.73 ? 526 GLN A NE2 1 ATOM 3944 N NE2 B GLN A 1 485 ? 15.172 57.788 45.769 0.35 20.47 ? 526 GLN A NE2 1 ATOM 3945 N N . ARG A 1 486 ? 8.388 58.814 46.564 1.00 14.22 ? 527 ARG A N 1 ATOM 3946 C CA . ARG A 1 486 ? 6.976 59.214 46.351 1.00 14.82 ? 527 ARG A CA 1 ATOM 3947 C C . ARG A 1 486 ? 6.376 59.855 47.555 1.00 16.55 ? 527 ARG A C 1 ATOM 3948 O O . ARG A 1 486 ? 5.739 60.923 47.430 1.00 15.78 ? 527 ARG A O 1 ATOM 3949 C CB . ARG A 1 486 ? 6.102 58.004 45.879 1.00 15.71 ? 527 ARG A CB 1 ATOM 3950 C CG . ARG A 1 486 ? 4.843 58.527 45.210 1.00 14.71 ? 527 ARG A CG 1 ATOM 3951 C CD . ARG A 1 486 ? 3.737 57.442 45.103 1.00 17.58 ? 527 ARG A CD 1 ATOM 3952 N NE . ARG A 1 486 ? 4.104 56.378 44.137 1.00 16.66 ? 527 ARG A NE 1 ATOM 3953 C CZ . ARG A 1 486 ? 3.171 55.585 43.564 1.00 16.51 ? 527 ARG A CZ 1 ATOM 3954 N NH1 . ARG A 1 486 ? 1.869 55.780 43.799 1.00 18.00 ? 527 ARG A NH1 1 ATOM 3955 N NH2 . ARG A 1 486 ? 3.555 54.597 42.727 1.00 16.78 ? 527 ARG A NH2 1 ATOM 3956 N N . LEU A 1 487 ? 6.558 59.237 48.723 1.00 15.11 ? 528 LEU A N 1 ATOM 3957 C CA . LEU A 1 487 ? 5.837 59.738 49.890 1.00 15.28 ? 528 LEU A CA 1 ATOM 3958 C C . LEU A 1 487 ? 6.598 60.679 50.807 1.00 15.71 ? 528 LEU A C 1 ATOM 3959 O O . LEU A 1 487 ? 5.960 61.325 51.637 1.00 18.18 ? 528 LEU A O 1 ATOM 3960 C CB . LEU A 1 487 ? 5.286 58.554 50.715 1.00 15.35 ? 528 LEU A CB 1 ATOM 3961 C CG . LEU A 1 487 ? 4.360 57.620 49.935 1.00 16.91 ? 528 LEU A CG 1 ATOM 3962 C CD1 . LEU A 1 487 ? 3.868 56.437 50.839 1.00 19.29 ? 528 LEU A CD1 1 ATOM 3963 C CD2 . LEU A 1 487 ? 3.107 58.392 49.431 1.00 19.96 ? 528 LEU A CD2 1 ATOM 3964 N N . GLY A 1 488 ? 7.921 60.720 50.697 1.00 15.14 ? 529 GLY A N 1 ATOM 3965 C CA . GLY A 1 488 ? 8.710 61.633 51.506 1.00 15.31 ? 529 GLY A CA 1 ATOM 3966 C C . GLY A 1 488 ? 8.809 61.188 52.953 1.00 14.96 ? 529 GLY A C 1 ATOM 3967 O O . GLY A 1 488 ? 8.775 62.055 53.857 1.00 15.42 ? 529 GLY A O 1 ATOM 3968 N N . ILE A 1 489 ? 8.970 59.880 53.168 1.00 15.07 ? 530 ILE A N 1 ATOM 3969 C CA . ILE A 1 489 ? 9.231 59.346 54.534 1.00 14.65 ? 530 ILE A CA 1 ATOM 3970 C C . ILE A 1 489 ? 10.742 59.110 54.646 1.00 15.30 ? 530 ILE A C 1 ATOM 3971 O O . ILE A 1 489 ? 11.322 58.450 53.774 1.00 16.51 ? 530 ILE A O 1 ATOM 3972 C CB . ILE A 1 489 ? 8.454 58.029 54.704 1.00 14.68 ? 530 ILE A CB 1 ATOM 3973 C CG1 . ILE A 1 489 ? 6.975 58.361 54.700 1.00 17.16 ? 530 ILE A CG1 1 ATOM 3974 C CG2 . ILE A 1 489 ? 8.842 57.347 56.078 1.00 16.60 ? 530 ILE A CG2 1 ATOM 3975 C CD1 . ILE A 1 489 ? 6.050 57.111 54.523 1.00 17.57 ? 530 ILE A CD1 1 ATOM 3976 N N . ALA A 1 490 ? 11.333 59.668 55.711 1.00 16.31 ? 531 ALA A N 1 ATOM 3977 C CA . ALA A 1 490 ? 12.778 59.485 55.986 1.00 16.14 ? 531 ALA A CA 1 ATOM 3978 C C . ALA A 1 490 ? 13.156 58.003 55.867 1.00 18.06 ? 531 ALA A C 1 ATOM 3979 O O . ALA A 1 490 ? 12.519 57.166 56.495 1.00 17.74 ? 531 ALA A O 1 ATOM 3980 C CB . ALA A 1 490 ? 13.061 59.979 57.426 1.00 17.71 ? 531 ALA A CB 1 ATOM 3981 N N . SER A 1 491 ? 14.151 57.668 55.039 1.00 15.65 ? 532 SER A N 1 ATOM 3982 C CA . SER A 1 491 ? 14.461 56.250 54.755 1.00 16.74 ? 532 SER A CA 1 ATOM 3983 C C . SER A 1 491 ? 15.961 56.005 54.886 1.00 18.10 ? 532 SER A C 1 ATOM 3984 O O . SER A 1 491 ? 16.770 56.922 54.696 1.00 18.77 ? 532 SER A O 1 ATOM 3985 C CB . SER A 1 491 ? 13.983 55.860 53.342 1.00 17.30 ? 532 SER A CB 1 ATOM 3986 O OG . SER A 1 491 ? 12.567 55.930 53.285 1.00 17.26 ? 532 SER A OG 1 ATOM 3987 N N . GLY A 1 492 ? 16.331 54.768 55.189 1.00 17.24 ? 533 GLY A N 1 ATOM 3988 C CA . GLY A 1 492 ? 17.766 54.398 55.183 1.00 18.15 ? 533 GLY A CA 1 ATOM 3989 C C . GLY A 1 492 ? 17.943 52.909 54.902 1.00 19.37 ? 533 GLY A C 1 ATOM 3990 O O . GLY A 1 492 ? 16.987 52.129 54.975 1.00 19.64 ? 533 GLY A O 1 ATOM 3991 N N . ARG A 1 493 ? 19.194 52.549 54.638 1.00 18.98 ? 534 ARG A N 1 ATOM 3992 C CA . ARG A 1 493 ? 19.588 51.163 54.356 1.00 19.83 ? 534 ARG A CA 1 ATOM 3993 C C . ARG A 1 493 ? 21.058 51.029 54.731 1.00 19.93 ? 534 ARG A C 1 ATOM 3994 O O . ARG A 1 493 ? 21.814 52.007 54.731 1.00 19.51 ? 534 ARG A O 1 ATOM 3995 C CB . ARG A 1 493 ? 19.342 50.820 52.886 1.00 20.44 ? 534 ARG A CB 1 ATOM 3996 C CG . ARG A 1 493 ? 20.133 51.667 51.903 1.00 20.49 ? 534 ARG A CG 1 ATOM 3997 C CD . ARG A 1 493 ? 19.729 51.465 50.391 1.00 20.81 ? 534 ARG A CD 1 ATOM 3998 N NE . ARG A 1 493 ? 19.683 50.063 49.976 1.00 23.10 ? 534 ARG A NE 1 ATOM 3999 C CZ . ARG A 1 493 ? 19.698 49.633 48.710 1.00 24.00 ? 534 ARG A CZ 1 ATOM 4000 N NH1 . ARG A 1 493 ? 19.608 48.323 48.475 1.00 23.22 ? 534 ARG A NH1 1 ATOM 4001 N NH2 . ARG A 1 493 ? 19.739 50.487 47.674 1.00 24.56 ? 534 ARG A NH2 1 ATOM 4002 N N . ALA A 1 494 ? 21.431 49.808 55.102 1.00 19.90 ? 535 ALA A N 1 ATOM 4003 C CA . ALA A 1 494 ? 22.829 49.530 55.501 1.00 19.76 ? 535 ALA A CA 1 ATOM 4004 C C . ALA A 1 494 ? 23.124 48.059 55.267 1.00 21.60 ? 535 ALA A C 1 ATOM 4005 O O . ALA A 1 494 ? 22.250 47.208 55.480 1.00 20.63 ? 535 ALA A O 1 ATOM 4006 C CB . ALA A 1 494 ? 22.997 49.854 56.992 1.00 20.10 ? 535 ALA A CB 1 ATOM 4007 N N . ARG A 1 495 ? 24.330 47.763 54.767 1.00 20.33 ? 536 ARG A N 1 ATOM 4008 C CA . ARG A 1 495 ? 24.763 46.362 54.590 1.00 20.87 ? 536 ARG A CA 1 ATOM 4009 C C . ARG A 1 495 ? 26.278 46.277 54.673 1.00 20.65 ? 536 ARG A C 1 ATOM 4010 O O . ARG A 1 495 ? 26.960 47.291 54.714 1.00 20.71 ? 536 ARG A O 1 ATOM 4011 C CB . ARG A 1 495 ? 24.304 45.806 53.236 1.00 21.30 ? 536 ARG A CB 1 ATOM 4012 C CG . ARG A 1 495 ? 24.915 46.506 52.045 1.00 22.89 ? 536 ARG A CG 1 ATOM 4013 C CD . ARG A 1 495 ? 24.524 45.735 50.766 1.00 26.50 ? 536 ARG A CD 1 ATOM 4014 N NE . ARG A 1 495 ? 23.056 45.810 50.538 1.00 27.71 ? 536 ARG A NE 1 ATOM 4015 C CZ . ARG A 1 495 ? 22.459 45.463 49.397 1.00 26.44 ? 536 ARG A CZ 1 ATOM 4016 N NH1 . ARG A 1 495 ? 23.166 45.019 48.354 1.00 26.68 ? 536 ARG A NH1 1 ATOM 4017 N NH2 . ARG A 1 495 ? 21.129 45.520 49.310 1.00 25.62 ? 536 ARG A NH2 1 ATOM 4018 N N . TYR A 1 496 ? 26.801 45.062 54.708 1.00 21.58 ? 537 TYR A N 1 ATOM 4019 C CA . TYR A 1 496 ? 28.246 44.900 54.603 1.00 22.56 ? 537 TYR A CA 1 ATOM 4020 C C . TYR A 1 496 ? 28.592 44.771 53.132 1.00 23.47 ? 537 TYR A C 1 ATOM 4021 O O . TYR A 1 496 ? 27.833 44.163 52.368 1.00 23.16 ? 537 TYR A O 1 ATOM 4022 C CB . TYR A 1 496 ? 28.806 43.708 55.437 1.00 22.17 ? 537 TYR A CB 1 ATOM 4023 C CG . TYR A 1 496 ? 29.727 44.192 56.506 1.00 23.78 ? 537 TYR A CG 1 ATOM 4024 C CD1 . TYR A 1 496 ? 29.236 44.931 57.573 1.00 24.98 ? 537 TYR A CD1 1 ATOM 4025 C CD2 . TYR A 1 496 ? 31.105 43.980 56.420 1.00 23.08 ? 537 TYR A CD2 1 ATOM 4026 C CE1 . TYR A 1 496 ? 30.083 45.420 58.586 1.00 25.64 ? 537 TYR A CE1 1 ATOM 4027 C CE2 . TYR A 1 496 ? 31.978 44.481 57.435 1.00 26.32 ? 537 TYR A CE2 1 ATOM 4028 C CZ . TYR A 1 496 ? 31.436 45.186 58.500 1.00 25.40 ? 537 TYR A CZ 1 ATOM 4029 O OH . TYR A 1 496 ? 32.254 45.727 59.483 1.00 29.11 ? 537 TYR A OH 1 ATOM 4030 N N . THR A 1 497 ? 29.728 45.347 52.751 1.00 23.95 ? 538 THR A N 1 ATOM 4031 C CA . THR A 1 497 ? 30.121 45.409 51.337 1.00 23.99 ? 538 THR A CA 1 ATOM 4032 C C . THR A 1 497 ? 31.587 45.025 51.122 1.00 25.77 ? 538 THR A C 1 ATOM 4033 O O . THR A 1 497 ? 32.297 44.761 52.067 1.00 26.15 ? 538 THR A O 1 ATOM 4034 C CB . THR A 1 497 ? 29.857 46.819 50.730 1.00 25.09 ? 538 THR A CB 1 ATOM 4035 O OG1 . THR A 1 497 ? 29.959 46.761 49.295 1.00 26.52 ? 538 THR A OG1 1 ATOM 4036 C CG2 . THR A 1 497 ? 30.810 47.886 51.301 1.00 24.25 ? 538 THR A CG2 1 ATOM 4037 N N . LYS A 1 498 ? 31.954 44.981 49.846 1.00 26.86 ? 539 LYS A N 1 ATOM 4038 C CA . LYS A 1 498 ? 33.326 44.686 49.399 1.00 30.31 ? 539 LYS A CA 1 ATOM 4039 C C . LYS A 1 498 ? 34.156 45.942 49.289 1.00 32.84 ? 539 LYS A C 1 ATOM 4040 O O . LYS A 1 498 ? 33.666 47.043 49.497 1.00 32.95 ? 539 LYS A O 1 ATOM 4041 C CB . LYS A 1 498 ? 33.292 43.935 48.045 1.00 31.11 ? 539 LYS A CB 1 ATOM 4042 C CG A LYS A 1 498 ? 32.906 44.784 46.827 0.50 32.12 ? 539 LYS A CG 1 ATOM 4043 C CD A LYS A 1 498 ? 31.403 44.848 46.631 0.50 34.19 ? 539 LYS A CD 1 ATOM 4044 C CE A LYS A 1 498 ? 31.009 45.576 45.334 0.50 37.78 ? 539 LYS A CE 1 ATOM 4045 N NZ A LYS A 1 498 ? 30.469 44.672 44.255 0.50 35.64 ? 539 LYS A NZ 1 ATOM 4046 N N . ASN A 1 499 ? 35.442 45.746 48.995 1.00 36.12 ? 540 ASN A N 1 ATOM 4047 C CA . ASN A 1 499 ? 36.347 46.802 48.605 1.00 39.98 ? 540 ASN A CA 1 ATOM 4048 C C . ASN A 1 499 ? 36.510 46.671 47.088 1.00 41.52 ? 540 ASN A C 1 ATOM 4049 O O . ASN A 1 499 ? 37.463 46.020 46.620 1.00 41.71 ? 540 ASN A O 1 ATOM 4050 C CB . ASN A 1 499 ? 37.718 46.556 49.268 1.00 40.66 ? 540 ASN A CB 1 ATOM 4051 C CG . ASN A 1 499 ? 38.691 47.697 49.051 1.00 43.81 ? 540 ASN A CG 1 ATOM 4052 O OD1 . ASN A 1 499 ? 38.316 48.771 48.561 1.00 45.98 ? 540 ASN A OD1 1 ATOM 4053 N ND2 . ASN A 1 499 ? 39.959 47.479 49.431 1.00 47.17 ? 540 ASN A ND2 1 ATOM 4054 N N . TRP A 1 500 ? 35.570 47.224 46.321 1.00 42.69 ? 541 TRP A N 1 ATOM 4055 C CA . TRP A 1 500 ? 35.658 47.208 44.842 1.00 44.95 ? 541 TRP A CA 1 ATOM 4056 C C . TRP A 1 500 ? 34.867 48.398 44.293 1.00 46.01 ? 541 TRP A C 1 ATOM 4057 O O . TRP A 1 500 ? 33.740 48.239 43.793 1.00 45.02 ? 541 TRP A O 1 ATOM 4058 C CB . TRP A 1 500 ? 35.128 45.878 44.257 1.00 44.94 ? 541 TRP A CB 1 ATOM 4059 C CG . TRP A 1 500 ? 35.597 45.552 42.833 1.00 45.80 ? 541 TRP A CG 1 ATOM 4060 C CD1 . TRP A 1 500 ? 36.226 46.400 41.946 1.00 46.62 ? 541 TRP A CD1 1 ATOM 4061 C CD2 . TRP A 1 500 ? 35.429 44.292 42.132 1.00 46.69 ? 541 TRP A CD2 1 ATOM 4062 N NE1 . TRP A 1 500 ? 36.470 45.735 40.751 1.00 48.34 ? 541 TRP A NE1 1 ATOM 4063 C CE2 . TRP A 1 500 ? 35.991 44.450 40.840 1.00 46.54 ? 541 TRP A CE2 1 ATOM 4064 C CE3 . TRP A 1 500 ? 34.861 43.048 42.478 1.00 47.06 ? 541 TRP A CE3 1 ATOM 4065 C CZ2 . TRP A 1 500 ? 36.016 43.405 39.892 1.00 46.56 ? 541 TRP A CZ2 1 ATOM 4066 C CZ3 . TRP A 1 500 ? 34.885 42.004 41.529 1.00 47.67 ? 541 TRP A CZ3 1 ATOM 4067 C CH2 . TRP A 1 500 ? 35.460 42.201 40.253 1.00 44.69 ? 541 TRP A CH2 1 ATOM 4068 N N . GLU A 1 501 ? 35.464 49.590 44.400 1.00 47.82 ? 542 GLU A N 1 ATOM 4069 C CA . GLU A 1 501 ? 34.730 50.849 44.188 1.00 48.93 ? 542 GLU A CA 1 ATOM 4070 C C . GLU A 1 501 ? 34.071 50.984 42.820 1.00 48.09 ? 542 GLU A C 1 ATOM 4071 O O . GLU A 1 501 ? 32.896 51.394 42.723 1.00 48.16 ? 542 GLU A O 1 ATOM 4072 C CB . GLU A 1 501 ? 35.620 52.064 44.486 1.00 50.94 ? 542 GLU A CB 1 ATOM 4073 C CG . GLU A 1 501 ? 35.521 52.577 45.933 1.00 56.25 ? 542 GLU A CG 1 ATOM 4074 C CD . GLU A 1 501 ? 34.188 53.274 46.253 1.00 61.68 ? 542 GLU A CD 1 ATOM 4075 O OE1 . GLU A 1 501 ? 33.206 53.120 45.482 1.00 64.70 ? 542 GLU A OE1 1 ATOM 4076 O OE2 . GLU A 1 501 ? 34.118 53.984 47.290 1.00 64.38 ? 542 GLU A OE2 1 ATOM 4077 N N . THR A 1 502 ? 34.812 50.610 41.779 1.00 47.98 ? 543 THR A N 1 ATOM 4078 C CA . THR A 1 502 ? 34.321 50.669 40.397 1.00 46.92 ? 543 THR A CA 1 ATOM 4079 C C . THR A 1 502 ? 33.179 49.681 40.131 1.00 44.59 ? 543 THR A C 1 ATOM 4080 O O . THR A 1 502 ? 32.514 49.730 39.069 1.00 45.13 ? 543 THR A O 1 ATOM 4081 C CB . THR A 1 502 ? 35.469 50.410 39.380 1.00 48.03 ? 543 THR A CB 1 ATOM 4082 O OG1 . THR A 1 502 ? 36.144 49.183 39.711 1.00 49.03 ? 543 THR A OG1 1 ATOM 4083 C CG2 . THR A 1 502 ? 36.457 51.573 39.374 1.00 49.34 ? 543 THR A CG2 1 ATOM 4084 N N . ASN A 1 503 ? 32.951 48.783 41.083 1.00 42.01 ? 544 ASN A N 1 ATOM 4085 C CA A ASN A 1 503 ? 31.894 47.777 40.955 0.50 40.02 ? 544 ASN A CA 1 ATOM 4086 C CA B ASN A 1 503 ? 31.879 47.808 40.936 0.50 40.39 ? 544 ASN A CA 1 ATOM 4087 C C . ASN A 1 503 ? 30.695 48.041 41.868 1.00 38.49 ? 544 ASN A C 1 ATOM 4088 O O . ASN A 1 503 ? 29.874 47.141 42.068 1.00 37.88 ? 544 ASN A O 1 ATOM 4089 C CB A ASN A 1 503 ? 32.448 46.359 41.209 0.50 40.21 ? 544 ASN A CB 1 ATOM 4090 C CB B ASN A 1 503 ? 32.427 46.389 41.090 0.50 41.02 ? 544 ASN A CB 1 ATOM 4091 C CG A ASN A 1 503 ? 32.445 45.481 39.953 0.50 40.11 ? 544 ASN A CG 1 ATOM 4092 C CG B ASN A 1 503 ? 33.147 45.917 39.847 0.50 42.54 ? 544 ASN A CG 1 ATOM 4093 O OD1 A ASN A 1 503 ? 32.713 45.951 38.845 0.50 38.65 ? 544 ASN A OD1 1 ATOM 4094 O OD1 B ASN A 1 503 ? 34.034 46.606 39.326 0.50 45.97 ? 544 ASN A OD1 1 ATOM 4095 N ND2 A ASN A 1 503 ? 32.138 44.201 40.130 0.50 37.52 ? 544 ASN A ND2 1 ATOM 4096 N ND2 B ASN A 1 503 ? 32.766 44.740 39.356 0.50 41.24 ? 544 ASN A ND2 1 ATOM 4097 N N . LYS A 1 504 ? 30.589 49.261 42.416 1.00 36.12 ? 545 LYS A N 1 ATOM 4098 C CA . LYS A 1 504 ? 29.559 49.533 43.423 1.00 34.56 ? 545 LYS A CA 1 ATOM 4099 C C . LYS A 1 504 ? 28.096 49.430 42.932 1.00 32.02 ? 545 LYS A C 1 ATOM 4100 O O . LYS A 1 504 ? 27.193 49.265 43.758 1.00 31.00 ? 545 LYS A O 1 ATOM 4101 C CB . LYS A 1 504 ? 29.774 50.877 44.126 1.00 35.86 ? 545 LYS A CB 1 ATOM 4102 C CG . LYS A 1 504 ? 29.428 52.077 43.278 1.00 39.35 ? 545 LYS A CG 1 ATOM 4103 C CD . LYS A 1 504 ? 29.798 53.392 43.982 1.00 44.84 ? 545 LYS A CD 1 ATOM 4104 C CE . LYS A 1 504 ? 29.879 54.531 42.946 1.00 48.27 ? 545 LYS A CE 1 ATOM 4105 N NZ . LYS A 1 504 ? 29.735 55.885 43.569 1.00 53.81 ? 545 LYS A NZ 1 ATOM 4106 N N . PHE A 1 505 ? 27.863 49.539 41.624 1.00 28.93 ? 546 PHE A N 1 ATOM 4107 C CA . PHE A 1 505 ? 26.498 49.329 41.072 1.00 26.87 ? 546 PHE A CA 1 ATOM 4108 C C . PHE A 1 505 ? 26.411 48.060 40.214 1.00 27.45 ? 546 PHE A C 1 ATOM 4109 O O . PHE A 1 505 ? 25.410 47.823 39.565 1.00 27.58 ? 546 PHE A O 1 ATOM 4110 C CB . PHE A 1 505 ? 26.020 50.529 40.234 1.00 27.10 ? 546 PHE A CB 1 ATOM 4111 C CG . PHE A 1 505 ? 25.879 51.812 41.034 1.00 26.88 ? 546 PHE A CG 1 ATOM 4112 C CD1 . PHE A 1 505 ? 25.063 51.861 42.151 1.00 29.47 ? 546 PHE A CD1 1 ATOM 4113 C CD2 . PHE A 1 505 ? 26.576 52.966 40.656 1.00 31.50 ? 546 PHE A CD2 1 ATOM 4114 C CE1 . PHE A 1 505 ? 24.928 53.054 42.899 1.00 29.93 ? 546 PHE A CE1 1 ATOM 4115 C CE2 . PHE A 1 505 ? 26.429 54.165 41.381 1.00 29.61 ? 546 PHE A CE2 1 ATOM 4116 C CZ . PHE A 1 505 ? 25.614 54.189 42.521 1.00 30.39 ? 546 PHE A CZ 1 ATOM 4117 N N . SER A 1 506 ? 27.444 47.234 40.216 1.00 27.35 ? 547 SER A N 1 ATOM 4118 C CA . SER A 1 506 ? 27.406 46.091 39.282 1.00 27.45 ? 547 SER A CA 1 ATOM 4119 C C . SER A 1 506 ? 26.842 44.837 39.921 1.00 27.22 ? 547 SER A C 1 ATOM 4120 O O . SER A 1 506 ? 26.369 43.960 39.208 1.00 29.15 ? 547 SER A O 1 ATOM 4121 C CB . SER A 1 506 ? 28.802 45.834 38.675 1.00 27.70 ? 547 SER A CB 1 ATOM 4122 O OG . SER A 1 506 ? 29.245 47.036 38.026 1.00 29.24 ? 547 SER A OG 1 ATOM 4123 N N . GLY A 1 507 ? 26.832 44.770 41.260 1.00 26.10 ? 548 GLY A N 1 ATOM 4124 C CA . GLY A 1 507 ? 26.457 43.531 41.948 1.00 26.87 ? 548 GLY A CA 1 ATOM 4125 C C . GLY A 1 507 ? 27.695 42.660 42.187 1.00 27.32 ? 548 GLY A C 1 ATOM 4126 O O . GLY A 1 507 ? 28.710 42.811 41.498 1.00 29.83 ? 548 GLY A O 1 ATOM 4127 N N . TYR A 1 508 ? 27.631 41.818 43.218 1.00 25.18 ? 549 TYR A N 1 ATOM 4128 C CA . TYR A 1 508 ? 28.659 40.820 43.514 1.00 23.99 ? 549 TYR A CA 1 ATOM 4129 C C . TYR A 1 508 ? 28.640 39.779 42.365 1.00 22.93 ? 549 TYR A C 1 ATOM 4130 O O . TYR A 1 508 ? 27.673 39.726 41.565 1.00 22.55 ? 549 TYR A O 1 ATOM 4131 C CB . TYR A 1 508 ? 28.395 40.188 44.900 1.00 23.52 ? 549 TYR A CB 1 ATOM 4132 C CG . TYR A 1 508 ? 26.943 39.807 45.096 1.00 24.13 ? 549 TYR A CG 1 ATOM 4133 C CD1 . TYR A 1 508 ? 26.489 38.513 44.851 1.00 23.52 ? 549 TYR A CD1 1 ATOM 4134 C CD2 . TYR A 1 508 ? 26.025 40.764 45.516 1.00 24.48 ? 549 TYR A CD2 1 ATOM 4135 C CE1 . TYR A 1 508 ? 25.117 38.191 44.996 1.00 23.68 ? 549 TYR A CE1 1 ATOM 4136 C CE2 . TYR A 1 508 ? 24.695 40.448 45.640 1.00 24.10 ? 549 TYR A CE2 1 ATOM 4137 C CZ . TYR A 1 508 ? 24.252 39.181 45.401 1.00 22.10 ? 549 TYR A CZ 1 ATOM 4138 O OH . TYR A 1 508 ? 22.897 38.928 45.517 1.00 24.63 ? 549 TYR A OH 1 ATOM 4139 N N . PRO A 1 509 ? 29.689 38.967 42.252 1.00 22.91 ? 550 PRO A N 1 ATOM 4140 C CA . PRO A 1 509 ? 29.784 38.156 41.000 1.00 22.77 ? 550 PRO A CA 1 ATOM 4141 C C . PRO A 1 509 ? 28.574 37.234 40.759 1.00 22.64 ? 550 PRO A C 1 ATOM 4142 O O . PRO A 1 509 ? 28.163 37.057 39.622 1.00 23.26 ? 550 PRO A O 1 ATOM 4143 C CB . PRO A 1 509 ? 31.086 37.352 41.207 1.00 23.73 ? 550 PRO A CB 1 ATOM 4144 C CG . PRO A 1 509 ? 31.954 38.377 41.974 1.00 24.10 ? 550 PRO A CG 1 ATOM 4145 C CD . PRO A 1 509 ? 30.986 39.002 42.976 1.00 23.76 ? 550 PRO A CD 1 ATOM 4146 N N . LEU A 1 510 ? 28.012 36.657 41.815 1.00 21.07 ? 551 LEU A N 1 ATOM 4147 C CA . LEU A 1 510 ? 26.926 35.668 41.644 1.00 21.59 ? 551 LEU A CA 1 ATOM 4148 C C . LEU A 1 510 ? 25.537 36.274 41.746 1.00 20.75 ? 551 LEU A C 1 ATOM 4149 O O . LEU A 1 510 ? 24.538 35.536 41.826 1.00 22.29 ? 551 LEU A O 1 ATOM 4150 C CB . LEU A 1 510 ? 27.096 34.525 42.650 1.00 20.37 ? 551 LEU A CB 1 ATOM 4151 C CG . LEU A 1 510 ? 28.420 33.795 42.379 1.00 21.90 ? 551 LEU A CG 1 ATOM 4152 C CD1 . LEU A 1 510 ? 28.637 32.760 43.441 1.00 25.04 ? 551 LEU A CD1 1 ATOM 4153 C CD2 . LEU A 1 510 ? 28.374 33.145 40.967 1.00 21.89 ? 551 LEU A CD2 1 ATOM 4154 N N . TYR A 1 511 ? 25.482 37.608 41.697 1.00 20.47 ? 552 TYR A N 1 ATOM 4155 C CA . TYR A 1 511 ? 24.198 38.343 41.756 1.00 20.04 ? 552 TYR A CA 1 ATOM 4156 C C . TYR A 1 511 ? 23.173 37.819 40.758 1.00 18.67 ? 552 TYR A C 1 ATOM 4157 O O . TYR A 1 511 ? 23.392 37.801 39.540 1.00 20.78 ? 552 TYR A O 1 ATOM 4158 C CB . TYR A 1 511 ? 24.549 39.814 41.563 1.00 19.14 ? 552 TYR A CB 1 ATOM 4159 C CG . TYR A 1 511 ? 23.389 40.763 41.357 1.00 19.24 ? 552 TYR A CG 1 ATOM 4160 C CD1 . TYR A 1 511 ? 22.445 41.002 42.384 1.00 20.22 ? 552 TYR A CD1 1 ATOM 4161 C CD2 . TYR A 1 511 ? 23.288 41.463 40.156 1.00 21.30 ? 552 TYR A CD2 1 ATOM 4162 C CE1 . TYR A 1 511 ? 21.399 41.912 42.171 1.00 18.57 ? 552 TYR A CE1 1 ATOM 4163 C CE2 . TYR A 1 511 ? 22.273 42.401 39.964 1.00 20.24 ? 552 TYR A CE2 1 ATOM 4164 C CZ . TYR A 1 511 ? 21.330 42.574 40.955 1.00 19.22 ? 552 TYR A CZ 1 ATOM 4165 O OH . TYR A 1 511 ? 20.293 43.458 40.716 1.00 20.60 ? 552 TYR A OH 1 ATOM 4166 N N . HIS A 1 512 ? 22.014 37.412 41.284 1.00 20.19 ? 553 HIS A N 1 ATOM 4167 C CA . HIS A 1 512 ? 20.851 36.990 40.459 1.00 19.78 ? 553 HIS A CA 1 ATOM 4168 C C . HIS A 1 512 ? 21.102 35.729 39.628 1.00 20.80 ? 553 HIS A C 1 ATOM 4169 O O . HIS A 1 512 ? 20.383 35.460 38.640 1.00 20.07 ? 553 HIS A O 1 ATOM 4170 C CB . HIS A 1 512 ? 20.346 38.152 39.587 1.00 19.51 ? 553 HIS A CB 1 ATOM 4171 C CG . HIS A 1 512 ? 19.583 39.214 40.349 1.00 17.77 ? 553 HIS A CG 1 ATOM 4172 N ND1 . HIS A 1 512 ? 18.968 40.246 39.676 1.00 16.38 ? 553 HIS A ND1 1 ATOM 4173 C CD2 . HIS A 1 512 ? 19.354 39.431 41.675 1.00 18.77 ? 553 HIS A CD2 1 ATOM 4174 C CE1 . HIS A 1 512 ? 18.341 41.033 40.541 1.00 17.79 ? 553 HIS A CE1 1 ATOM 4175 N NE2 . HIS A 1 512 ? 18.524 40.543 41.759 1.00 17.24 ? 553 HIS A NE2 1 ATOM 4176 N N . SER A 1 513 ? 22.103 34.966 40.054 1.00 20.69 ? 554 SER A N 1 ATOM 4177 C CA . SER A 1 513 ? 22.418 33.668 39.431 1.00 19.24 ? 554 SER A CA 1 ATOM 4178 C C . SER A 1 513 ? 21.908 32.486 40.313 1.00 23.04 ? 554 SER A C 1 ATOM 4179 O O . SER A 1 513 ? 21.676 32.654 41.463 1.00 21.55 ? 554 SER A O 1 ATOM 4180 C CB . SER A 1 513 ? 23.949 33.563 39.239 1.00 19.66 ? 554 SER A CB 1 ATOM 4181 O OG A SER A 1 513 ? 24.630 33.298 40.442 0.50 22.35 ? 554 SER A OG 1 ATOM 4182 O OG B SER A 1 513 ? 24.363 32.216 39.006 0.50 19.68 ? 554 SER A OG 1 ATOM 4183 N N . VAL A 1 514 ? 21.811 31.299 39.690 1.00 20.39 ? 555 VAL A N 1 ATOM 4184 C CA . VAL A 1 514 ? 21.450 30.092 40.425 1.00 22.11 ? 555 VAL A CA 1 ATOM 4185 C C . VAL A 1 514 ? 22.488 29.784 41.516 1.00 22.76 ? 555 VAL A C 1 ATOM 4186 O O . VAL A 1 514 ? 22.199 28.998 42.453 1.00 24.65 ? 555 VAL A O 1 ATOM 4187 C CB . VAL A 1 514 ? 21.316 28.899 39.457 1.00 22.43 ? 555 VAL A CB 1 ATOM 4188 C CG1 . VAL A 1 514 ? 22.733 28.446 38.952 1.00 22.32 ? 555 VAL A CG1 1 ATOM 4189 C CG2 . VAL A 1 514 ? 20.635 27.706 40.134 1.00 23.43 ? 555 VAL A CG2 1 ATOM 4190 N N . TYR A 1 515 ? 23.699 30.349 41.400 1.00 21.33 ? 556 TYR A N 1 ATOM 4191 C CA . TYR A 1 515 ? 24.785 29.962 42.309 1.00 23.62 ? 556 TYR A CA 1 ATOM 4192 C C . TYR A 1 515 ? 24.700 30.701 43.648 1.00 23.74 ? 556 TYR A C 1 ATOM 4193 O O . TYR A 1 515 ? 25.479 30.384 44.571 1.00 25.45 ? 556 TYR A O 1 ATOM 4194 C CB . TYR A 1 515 ? 26.185 30.138 41.655 1.00 23.15 ? 556 TYR A CB 1 ATOM 4195 C CG . TYR A 1 515 ? 26.273 29.352 40.387 1.00 24.26 ? 556 TYR A CG 1 ATOM 4196 C CD1 . TYR A 1 515 ? 26.155 27.943 40.399 1.00 23.69 ? 556 TYR A CD1 1 ATOM 4197 C CD2 . TYR A 1 515 ? 26.445 29.993 39.158 1.00 25.62 ? 556 TYR A CD2 1 ATOM 4198 C CE1 . TYR A 1 515 ? 26.188 27.214 39.204 1.00 24.19 ? 556 TYR A CE1 1 ATOM 4199 C CE2 . TYR A 1 515 ? 26.507 29.257 37.964 1.00 25.17 ? 556 TYR A CE2 1 ATOM 4200 C CZ . TYR A 1 515 ? 26.365 27.889 38.001 1.00 24.00 ? 556 TYR A CZ 1 ATOM 4201 O OH . TYR A 1 515 ? 26.389 27.161 36.840 1.00 26.58 ? 556 TYR A OH 1 ATOM 4202 N N . GLU A 1 516 ? 23.755 31.644 43.784 1.00 22.76 ? 557 GLU A N 1 ATOM 4203 C CA . GLU A 1 516 ? 23.667 32.311 45.100 1.00 23.90 ? 557 GLU A CA 1 ATOM 4204 C C . GLU A 1 516 ? 22.805 31.489 46.062 1.00 23.57 ? 557 GLU A C 1 ATOM 4205 O O . GLU A 1 516 ? 21.585 31.466 46.032 1.00 23.60 ? 557 GLU A O 1 ATOM 4206 C CB . GLU A 1 516 ? 23.346 33.815 45.040 1.00 27.13 ? 557 GLU A CB 1 ATOM 4207 C CG . GLU A 1 516 ? 22.196 34.292 44.347 1.00 27.23 ? 557 GLU A CG 1 ATOM 4208 C CD . GLU A 1 516 ? 21.913 35.754 44.854 1.00 29.42 ? 557 GLU A CD 1 ATOM 4209 O OE1 . GLU A 1 516 ? 21.950 36.731 44.099 1.00 28.60 ? 557 GLU A OE1 1 ATOM 4210 O OE2 . GLU A 1 516 ? 21.639 35.896 46.049 1.00 26.76 ? 557 GLU A OE2 1 ATOM 4211 N N . THR A 1 517 ? 23.528 30.688 46.836 1.00 22.97 ? 558 THR A N 1 ATOM 4212 C CA . THR A 1 517 ? 22.951 29.663 47.669 1.00 22.86 ? 558 THR A CA 1 ATOM 4213 C C . THR A 1 517 ? 23.375 29.886 49.126 1.00 22.74 ? 558 THR A C 1 ATOM 4214 O O . THR A 1 517 ? 24.270 30.685 49.417 1.00 22.36 ? 558 THR A O 1 ATOM 4215 C CB . THR A 1 517 ? 23.497 28.292 47.277 1.00 23.87 ? 558 THR A CB 1 ATOM 4216 O OG1 . THR A 1 517 ? 24.936 28.313 47.385 1.00 26.67 ? 558 THR A OG1 1 ATOM 4217 C CG2 . THR A 1 517 ? 23.097 27.921 45.839 1.00 25.45 ? 558 THR A CG2 1 ATOM 4218 N N . TYR A 1 518 ? 22.771 29.112 50.027 1.00 23.32 ? 559 TYR A N 1 ATOM 4219 C CA . TYR A 1 518 ? 23.218 29.065 51.410 1.00 23.50 ? 559 TYR A CA 1 ATOM 4220 C C . TYR A 1 518 ? 24.725 28.751 51.494 1.00 24.13 ? 559 TYR A C 1 ATOM 4221 O O . TYR A 1 518 ? 25.457 29.365 52.266 1.00 24.88 ? 559 TYR A O 1 ATOM 4222 C CB . TYR A 1 518 ? 22.450 28.017 52.182 1.00 23.45 ? 559 TYR A CB 1 ATOM 4223 C CG . TYR A 1 518 ? 22.982 27.785 53.561 1.00 23.10 ? 559 TYR A CG 1 ATOM 4224 C CD1 . TYR A 1 518 ? 22.652 28.641 54.594 1.00 25.84 ? 559 TYR A CD1 1 ATOM 4225 C CD2 . TYR A 1 518 ? 23.814 26.697 53.832 1.00 28.27 ? 559 TYR A CD2 1 ATOM 4226 C CE1 . TYR A 1 518 ? 23.150 28.427 55.903 1.00 26.57 ? 559 TYR A CE1 1 ATOM 4227 C CE2 . TYR A 1 518 ? 24.326 26.493 55.122 1.00 30.32 ? 559 TYR A CE2 1 ATOM 4228 C CZ . TYR A 1 518 ? 23.981 27.363 56.143 1.00 29.97 ? 559 TYR A CZ 1 ATOM 4229 O OH . TYR A 1 518 ? 24.459 27.153 57.416 1.00 30.67 ? 559 TYR A OH 1 ATOM 4230 N N . GLU A 1 519 ? 25.183 27.806 50.676 1.00 25.34 ? 560 GLU A N 1 ATOM 4231 C CA . GLU A 1 519 ? 26.595 27.402 50.742 1.00 25.65 ? 560 GLU A CA 1 ATOM 4232 C C . GLU A 1 519 ? 27.538 28.521 50.350 1.00 25.37 ? 560 GLU A C 1 ATOM 4233 O O . GLU A 1 519 ? 28.607 28.658 50.946 1.00 26.67 ? 560 GLU A O 1 ATOM 4234 C CB . GLU A 1 519 ? 26.838 26.155 49.867 1.00 26.95 ? 560 GLU A CB 1 ATOM 4235 C CG . GLU A 1 519 ? 26.201 24.887 50.412 1.00 28.55 ? 560 GLU A CG 1 ATOM 4236 C CD . GLU A 1 519 ? 24.690 24.850 50.179 1.00 30.31 ? 560 GLU A CD 1 ATOM 4237 O OE1 . GLU A 1 519 ? 24.236 25.356 49.150 1.00 30.10 ? 560 GLU A OE1 1 ATOM 4238 O OE2 . GLU A 1 519 ? 23.980 24.295 51.034 1.00 32.31 ? 560 GLU A OE2 1 ATOM 4239 N N . LEU A 1 520 ? 27.145 29.317 49.356 1.00 24.00 ? 561 LEU A N 1 ATOM 4240 C CA . LEU A 1 520 ? 27.913 30.505 49.004 1.00 23.33 ? 561 LEU A CA 1 ATOM 4241 C C . LEU A 1 520 ? 28.173 31.377 50.227 1.00 24.32 ? 561 LEU A C 1 ATOM 4242 O O . LEU A 1 520 ? 29.312 31.821 50.454 1.00 24.44 ? 561 LEU A O 1 ATOM 4243 C CB . LEU A 1 520 ? 27.208 31.319 47.904 1.00 23.85 ? 561 LEU A CB 1 ATOM 4244 C CG . LEU A 1 520 ? 27.881 32.652 47.603 1.00 22.66 ? 561 LEU A CG 1 ATOM 4245 C CD1 . LEU A 1 520 ? 29.302 32.463 47.038 1.00 24.98 ? 561 LEU A CD1 1 ATOM 4246 C CD2 . LEU A 1 520 ? 27.010 33.483 46.647 1.00 24.62 ? 561 LEU A CD2 1 ATOM 4247 N N . VAL A 1 521 ? 27.107 31.647 50.998 1.00 23.66 ? 562 VAL A N 1 ATOM 4248 C CA . VAL A 1 521 ? 27.244 32.557 52.143 1.00 24.00 ? 562 VAL A CA 1 ATOM 4249 C C . VAL A 1 521 ? 28.055 31.889 53.257 1.00 25.25 ? 562 VAL A C 1 ATOM 4250 O O . VAL A 1 521 ? 29.003 32.493 53.798 1.00 26.15 ? 562 VAL A O 1 ATOM 4251 C CB . VAL A 1 521 ? 25.865 32.957 52.692 1.00 23.66 ? 562 VAL A CB 1 ATOM 4252 C CG1 . VAL A 1 521 ? 26.032 33.829 53.959 1.00 24.36 ? 562 VAL A CG1 1 ATOM 4253 C CG2 . VAL A 1 521 ? 25.111 33.746 51.590 1.00 24.59 ? 562 VAL A CG2 1 ATOM 4254 N N . GLU A 1 522 ? 27.681 30.655 53.597 1.00 25.37 ? 563 GLU A N 1 ATOM 4255 C CA . GLU A 1 522 ? 28.274 29.956 54.741 1.00 27.94 ? 563 GLU A CA 1 ATOM 4256 C C . GLU A 1 522 ? 29.751 29.623 54.510 1.00 28.83 ? 563 GLU A C 1 ATOM 4257 O O . GLU A 1 522 ? 30.571 29.705 55.444 1.00 29.88 ? 563 GLU A O 1 ATOM 4258 C CB . GLU A 1 522 ? 27.474 28.671 55.025 1.00 29.55 ? 563 GLU A CB 1 ATOM 4259 C CG . GLU A 1 522 ? 27.822 27.976 56.362 1.00 33.91 ? 563 GLU A CG 1 ATOM 4260 C CD . GLU A 1 522 ? 29.013 27.037 56.256 1.00 41.43 ? 563 GLU A CD 1 ATOM 4261 O OE1 . GLU A 1 522 ? 29.264 26.481 55.152 1.00 40.85 ? 563 GLU A OE1 1 ATOM 4262 O OE2 . GLU A 1 522 ? 29.711 26.852 57.293 1.00 43.22 ? 563 GLU A OE2 1 ATOM 4263 N N . LYS A 1 523 ? 30.115 29.274 53.273 1.00 28.29 ? 564 LYS A N 1 ATOM 4264 C CA . LYS A 1 523 ? 31.511 28.942 52.978 1.00 28.71 ? 564 LYS A CA 1 ATOM 4265 C C . LYS A 1 523 ? 32.396 30.160 52.722 1.00 29.53 ? 564 LYS A C 1 ATOM 4266 O O . LYS A 1 523 ? 33.553 30.200 53.166 1.00 32.01 ? 564 LYS A O 1 ATOM 4267 C CB . LYS A 1 523 ? 31.614 28.007 51.776 1.00 27.78 ? 564 LYS A CB 1 ATOM 4268 C CG . LYS A 1 523 ? 30.987 26.653 51.972 1.00 29.37 ? 564 LYS A CG 1 ATOM 4269 C CD . LYS A 1 523 ? 31.096 25.836 50.658 1.00 32.68 ? 564 LYS A CD 1 ATOM 4270 C CE . LYS A 1 523 ? 30.323 24.503 50.699 1.00 39.61 ? 564 LYS A CE 1 ATOM 4271 N NZ . LYS A 1 523 ? 30.680 23.724 51.884 1.00 44.65 ? 564 LYS A NZ 1 ATOM 4272 N N . PHE A 1 524 ? 31.889 31.105 51.946 1.00 28.18 ? 565 PHE A N 1 ATOM 4273 C CA . PHE A 1 524 ? 32.739 32.133 51.393 1.00 28.54 ? 565 PHE A CA 1 ATOM 4274 C C . PHE A 1 524 ? 32.508 33.542 51.884 1.00 28.80 ? 565 PHE A C 1 ATOM 4275 O O . PHE A 1 524 ? 33.426 34.343 51.785 1.00 31.66 ? 565 PHE A O 1 ATOM 4276 C CB . PHE A 1 524 ? 32.689 32.113 49.875 1.00 28.08 ? 565 PHE A CB 1 ATOM 4277 C CG . PHE A 1 524 ? 33.086 30.782 49.293 1.00 29.18 ? 565 PHE A CG 1 ATOM 4278 C CD1 . PHE A 1 524 ? 34.372 30.270 49.537 1.00 30.44 ? 565 PHE A CD1 1 ATOM 4279 C CD2 . PHE A 1 524 ? 32.177 30.032 48.553 1.00 27.97 ? 565 PHE A CD2 1 ATOM 4280 C CE1 . PHE A 1 524 ? 34.746 29.046 49.009 1.00 32.09 ? 565 PHE A CE1 1 ATOM 4281 C CE2 . PHE A 1 524 ? 32.535 28.763 48.018 1.00 29.74 ? 565 PHE A CE2 1 ATOM 4282 C CZ . PHE A 1 524 ? 33.825 28.270 48.250 1.00 31.57 ? 565 PHE A CZ 1 ATOM 4283 N N . TYR A 1 525 ? 31.307 33.871 52.363 1.00 27.07 ? 566 TYR A N 1 ATOM 4284 C CA . TYR A 1 525 ? 31.076 35.245 52.770 1.00 26.20 ? 566 TYR A CA 1 ATOM 4285 C C . TYR A 1 525 ? 31.180 35.456 54.266 1.00 26.71 ? 566 TYR A C 1 ATOM 4286 O O . TYR A 1 525 ? 31.843 36.416 54.712 1.00 27.78 ? 566 TYR A O 1 ATOM 4287 C CB . TYR A 1 525 ? 29.705 35.754 52.250 1.00 24.07 ? 566 TYR A CB 1 ATOM 4288 C CG . TYR A 1 525 ? 29.786 36.260 50.827 1.00 24.76 ? 566 TYR A CG 1 ATOM 4289 C CD1 . TYR A 1 525 ? 29.812 35.357 49.757 1.00 25.36 ? 566 TYR A CD1 1 ATOM 4290 C CD2 . TYR A 1 525 ? 29.853 37.626 50.542 1.00 27.34 ? 566 TYR A CD2 1 ATOM 4291 C CE1 . TYR A 1 525 ? 29.906 35.780 48.446 1.00 25.81 ? 566 TYR A CE1 1 ATOM 4292 C CE2 . TYR A 1 525 ? 29.948 38.078 49.217 1.00 25.57 ? 566 TYR A CE2 1 ATOM 4293 C CZ . TYR A 1 525 ? 29.974 37.140 48.179 1.00 26.68 ? 566 TYR A CZ 1 ATOM 4294 O OH . TYR A 1 525 ? 30.091 37.572 46.889 1.00 26.19 ? 566 TYR A OH 1 ATOM 4295 N N . ASP A 1 526 ? 30.507 34.614 55.049 1.00 25.25 ? 567 ASP A N 1 ATOM 4296 C CA . ASP A 1 526 ? 30.302 34.922 56.463 1.00 25.84 ? 567 ASP A CA 1 ATOM 4297 C C . ASP A 1 526 ? 30.111 33.647 57.283 1.00 26.94 ? 567 ASP A C 1 ATOM 4298 O O . ASP A 1 526 ? 29.049 33.426 57.857 1.00 26.98 ? 567 ASP A O 1 ATOM 4299 C CB . ASP A 1 526 ? 29.083 35.851 56.600 1.00 23.87 ? 567 ASP A CB 1 ATOM 4300 C CG . ASP A 1 526 ? 29.013 36.536 57.967 1.00 25.25 ? 567 ASP A CG 1 ATOM 4301 O OD1 . ASP A 1 526 ? 29.981 36.458 58.771 1.00 28.19 ? 567 ASP A OD1 1 ATOM 4302 O OD2 . ASP A 1 526 ? 27.973 37.121 58.231 1.00 25.69 ? 567 ASP A OD2 1 ATOM 4303 N N . PRO A 1 527 ? 31.157 32.804 57.364 1.00 28.37 ? 568 PRO A N 1 ATOM 4304 C CA . PRO A 1 527 ? 30.972 31.503 58.024 1.00 29.34 ? 568 PRO A CA 1 ATOM 4305 C C . PRO A 1 527 ? 30.509 31.576 59.475 1.00 30.00 ? 568 PRO A C 1 ATOM 4306 O O . PRO A 1 527 ? 29.800 30.661 59.928 1.00 31.15 ? 568 PRO A O 1 ATOM 4307 C CB . PRO A 1 527 ? 32.369 30.837 57.961 1.00 30.75 ? 568 PRO A CB 1 ATOM 4308 C CG . PRO A 1 527 ? 33.198 31.697 57.103 1.00 31.97 ? 568 PRO A CG 1 ATOM 4309 C CD . PRO A 1 527 ? 32.498 32.972 56.770 1.00 28.89 ? 568 PRO A CD 1 ATOM 4310 N N A MET A 1 528 ? 30.901 32.634 60.186 0.50 29.54 ? 569 MET A N 1 ATOM 4311 N N B MET A 1 528 ? 30.916 32.631 60.189 0.50 29.96 ? 569 MET A N 1 ATOM 4312 C CA A MET A 1 528 ? 30.528 32.822 61.592 0.50 30.41 ? 569 MET A CA 1 ATOM 4313 C CA B MET A 1 528 ? 30.543 32.846 61.597 0.50 31.17 ? 569 MET A CA 1 ATOM 4314 C C A MET A 1 528 ? 29.284 33.713 61.747 0.50 28.95 ? 569 MET A C 1 ATOM 4315 C C B MET A 1 528 ? 29.227 33.625 61.736 0.50 29.41 ? 569 MET A C 1 ATOM 4316 O O A MET A 1 528 ? 28.837 33.989 62.875 0.50 28.59 ? 569 MET A O 1 ATOM 4317 O O B MET A 1 528 ? 28.684 33.747 62.847 0.50 29.20 ? 569 MET A O 1 ATOM 4318 C CB A MET A 1 528 ? 31.711 33.400 62.378 0.50 31.53 ? 569 MET A CB 1 ATOM 4319 C CB B MET A 1 528 ? 31.656 33.601 62.344 0.50 32.62 ? 569 MET A CB 1 ATOM 4320 C CG A MET A 1 528 ? 32.962 32.547 62.280 0.50 35.22 ? 569 MET A CG 1 ATOM 4321 C CG B MET A 1 528 ? 32.995 32.884 62.372 0.50 37.90 ? 569 MET A CG 1 ATOM 4322 S SD A MET A 1 528 ? 32.658 30.881 62.874 0.50 39.41 ? 569 MET A SD 1 ATOM 4323 S SD B MET A 1 528 ? 34.344 33.906 63.028 0.50 46.32 ? 569 MET A SD 1 ATOM 4324 C CE A MET A 1 528 ? 32.265 31.180 64.590 0.50 38.16 ? 569 MET A CE 1 ATOM 4325 C CE B MET A 1 528 ? 33.893 34.129 64.746 0.50 45.27 ? 569 MET A CE 1 ATOM 4326 N N . PHE A 1 529 ? 28.736 34.163 60.621 1.00 27.95 ? 570 PHE A N 1 ATOM 4327 C CA . PHE A 1 529 ? 27.531 35.019 60.635 1.00 26.23 ? 570 PHE A CA 1 ATOM 4328 C C . PHE A 1 529 ? 27.701 36.293 61.486 1.00 26.35 ? 570 PHE A C 1 ATOM 4329 O O . PHE A 1 529 ? 26.722 36.903 61.952 1.00 26.11 ? 570 PHE A O 1 ATOM 4330 C CB . PHE A 1 529 ? 26.253 34.194 60.940 1.00 26.71 ? 570 PHE A CB 1 ATOM 4331 C CG . PHE A 1 529 ? 25.815 33.382 59.765 1.00 26.47 ? 570 PHE A CG 1 ATOM 4332 C CD1 . PHE A 1 529 ? 24.824 33.861 58.895 1.00 27.23 ? 570 PHE A CD1 1 ATOM 4333 C CD2 . PHE A 1 529 ? 26.443 32.162 59.488 1.00 27.81 ? 570 PHE A CD2 1 ATOM 4334 C CE1 . PHE A 1 529 ? 24.474 33.124 57.743 1.00 26.49 ? 570 PHE A CE1 1 ATOM 4335 C CE2 . PHE A 1 529 ? 26.084 31.419 58.341 1.00 27.76 ? 570 PHE A CE2 1 ATOM 4336 C CZ . PHE A 1 529 ? 25.088 31.927 57.482 1.00 25.81 ? 570 PHE A CZ 1 ATOM 4337 N N . LYS A 1 530 ? 28.959 36.706 61.642 1.00 26.49 ? 571 LYS A N 1 ATOM 4338 C CA . LYS A 1 530 ? 29.276 37.900 62.407 1.00 27.18 ? 571 LYS A CA 1 ATOM 4339 C C . LYS A 1 530 ? 28.969 39.158 61.608 1.00 25.80 ? 571 LYS A C 1 ATOM 4340 O O . LYS A 1 530 ? 28.606 40.160 62.209 1.00 25.81 ? 571 LYS A O 1 ATOM 4341 C CB . LYS A 1 530 ? 30.740 37.889 62.881 1.00 28.69 ? 571 LYS A CB 1 ATOM 4342 C CG . LYS A 1 530 ? 31.751 38.033 61.789 1.00 29.57 ? 571 LYS A CG 1 ATOM 4343 C CD . LYS A 1 530 ? 33.162 37.996 62.405 1.00 31.16 ? 571 LYS A CD 1 ATOM 4344 C CE . LYS A 1 530 ? 34.199 38.198 61.336 1.00 33.81 ? 571 LYS A CE 1 ATOM 4345 N NZ . LYS A 1 530 ? 35.564 38.402 61.995 1.00 35.69 ? 571 LYS A NZ 1 ATOM 4346 N N . TYR A 1 531 ? 29.133 39.131 60.285 1.00 25.45 ? 572 TYR A N 1 ATOM 4347 C CA . TYR A 1 531 ? 28.785 40.317 59.497 1.00 25.00 ? 572 TYR A CA 1 ATOM 4348 C C . TYR A 1 531 ? 27.260 40.472 59.451 1.00 24.46 ? 572 TYR A C 1 ATOM 4349 O O . TYR A 1 531 ? 26.752 41.604 59.557 1.00 25.23 ? 572 TYR A O 1 ATOM 4350 C CB . TYR A 1 531 ? 29.406 40.323 58.093 1.00 24.01 ? 572 TYR A CB 1 ATOM 4351 C CG . TYR A 1 531 ? 30.902 40.214 58.172 1.00 26.47 ? 572 TYR A CG 1 ATOM 4352 C CD1 . TYR A 1 531 ? 31.667 41.256 58.719 1.00 28.72 ? 572 TYR A CD1 1 ATOM 4353 C CD2 . TYR A 1 531 ? 31.551 39.069 57.748 1.00 29.48 ? 572 TYR A CD2 1 ATOM 4354 C CE1 . TYR A 1 531 ? 33.025 41.148 58.839 1.00 30.71 ? 572 TYR A CE1 1 ATOM 4355 C CE2 . TYR A 1 531 ? 32.921 38.962 57.877 1.00 30.99 ? 572 TYR A CE2 1 ATOM 4356 C CZ . TYR A 1 531 ? 33.643 40.008 58.392 1.00 29.71 ? 572 TYR A CZ 1 ATOM 4357 O OH . TYR A 1 531 ? 35.014 39.846 58.502 1.00 35.34 ? 572 TYR A OH 1 ATOM 4358 N N . HIS A 1 532 ? 26.540 39.359 59.305 1.00 23.20 ? 573 HIS A N 1 ATOM 4359 C CA . HIS A 1 532 ? 25.067 39.373 59.396 1.00 23.14 ? 573 HIS A CA 1 ATOM 4360 C C . HIS A 1 532 ? 24.651 39.956 60.764 1.00 22.98 ? 573 HIS A C 1 ATOM 4361 O O . HIS A 1 532 ? 23.720 40.764 60.829 1.00 22.30 ? 573 HIS A O 1 ATOM 4362 C CB . HIS A 1 532 ? 24.484 37.980 59.296 1.00 23.27 ? 573 HIS A CB 1 ATOM 4363 C CG . HIS A 1 532 ? 24.367 37.450 57.896 1.00 23.72 ? 573 HIS A CG 1 ATOM 4364 N ND1 . HIS A 1 532 ? 25.449 36.956 57.197 1.00 23.26 ? 573 HIS A ND1 1 ATOM 4365 C CD2 . HIS A 1 532 ? 23.285 37.259 57.099 1.00 24.29 ? 573 HIS A CD2 1 ATOM 4366 C CE1 . HIS A 1 532 ? 25.048 36.506 56.017 1.00 25.62 ? 573 HIS A CE1 1 ATOM 4367 N NE2 . HIS A 1 532 ? 23.735 36.654 55.945 1.00 26.05 ? 573 HIS A NE2 1 ATOM 4368 N N . LEU A 1 533 ? 25.321 39.524 61.840 1.00 24.10 ? 574 LEU A N 1 ATOM 4369 C CA . LEU A 1 533 ? 24.913 39.988 63.162 1.00 24.20 ? 574 LEU A CA 1 ATOM 4370 C C . LEU A 1 533 ? 25.125 41.502 63.278 1.00 24.07 ? 574 LEU A C 1 ATOM 4371 O O . LEU A 1 533 ? 24.262 42.210 63.809 1.00 23.73 ? 574 LEU A O 1 ATOM 4372 C CB . LEU A 1 533 ? 25.683 39.249 64.276 1.00 25.17 ? 574 LEU A CB 1 ATOM 4373 C CG . LEU A 1 533 ? 25.322 39.765 65.689 1.00 25.46 ? 574 LEU A CG 1 ATOM 4374 C CD1 . LEU A 1 533 ? 23.831 39.547 65.985 1.00 26.97 ? 574 LEU A CD1 1 ATOM 4375 C CD2 . LEU A 1 533 ? 26.166 38.978 66.686 1.00 28.08 ? 574 LEU A CD2 1 ATOM 4376 N N . THR A 1 534 ? 26.283 41.987 62.816 1.00 24.28 ? 575 THR A N 1 ATOM 4377 C CA . THR A 1 534 ? 26.572 43.430 62.796 1.00 23.49 ? 575 THR A CA 1 ATOM 4378 C C . THR A 1 534 ? 25.504 44.205 62.031 1.00 22.70 ? 575 THR A C 1 ATOM 4379 O O . THR A 1 534 ? 25.005 45.224 62.502 1.00 22.79 ? 575 THR A O 1 ATOM 4380 C CB . THR A 1 534 ? 27.979 43.702 62.230 1.00 24.40 ? 575 THR A CB 1 ATOM 4381 O OG1 . THR A 1 534 ? 28.942 43.167 63.161 1.00 25.86 ? 575 THR A OG1 1 ATOM 4382 C CG2 . THR A 1 534 ? 28.240 45.220 62.071 1.00 25.26 ? 575 THR A CG2 1 ATOM 4383 N N . VAL A 1 535 ? 25.149 43.718 60.854 1.00 21.41 ? 576 VAL A N 1 ATOM 4384 C CA . VAL A 1 535 ? 24.066 44.357 60.067 1.00 20.15 ? 576 VAL A CA 1 ATOM 4385 C C . VAL A 1 535 ? 22.726 44.327 60.820 1.00 20.73 ? 576 VAL A C 1 ATOM 4386 O O . VAL A 1 535 ? 21.962 45.315 60.812 1.00 22.02 ? 576 VAL A O 1 ATOM 4387 C CB . VAL A 1 535 ? 23.998 43.782 58.636 1.00 20.53 ? 576 VAL A CB 1 ATOM 4388 C CG1 . VAL A 1 535 ? 22.787 44.419 57.883 1.00 19.22 ? 576 VAL A CG1 1 ATOM 4389 C CG2 . VAL A 1 535 ? 25.320 44.133 57.926 1.00 21.85 ? 576 VAL A CG2 1 ATOM 4390 N N . ALA A 1 536 ? 22.435 43.231 61.509 1.00 20.65 ? 577 ALA A N 1 ATOM 4391 C CA . ALA A 1 536 ? 21.206 43.164 62.318 1.00 21.35 ? 577 ALA A CA 1 ATOM 4392 C C . ALA A 1 536 ? 21.212 44.204 63.426 1.00 21.89 ? 577 ALA A C 1 ATOM 4393 O O . ALA A 1 536 ? 20.174 44.824 63.721 1.00 21.44 ? 577 ALA A O 1 ATOM 4394 C CB . ALA A 1 536 ? 20.994 41.786 62.892 1.00 22.16 ? 577 ALA A CB 1 ATOM 4395 N N . GLN A 1 537 ? 22.363 44.384 64.052 1.00 22.59 ? 578 GLN A N 1 ATOM 4396 C CA . GLN A 1 537 ? 22.493 45.423 65.093 1.00 22.46 ? 578 GLN A CA 1 ATOM 4397 C C . GLN A 1 537 ? 22.312 46.839 64.525 1.00 22.57 ? 578 GLN A C 1 ATOM 4398 O O . GLN A 1 537 ? 21.713 47.708 65.187 1.00 23.04 ? 578 GLN A O 1 ATOM 4399 C CB . GLN A 1 537 ? 23.838 45.298 65.850 1.00 23.74 ? 578 GLN A CB 1 ATOM 4400 C CG . GLN A 1 537 ? 23.969 43.990 66.593 1.00 23.89 ? 578 GLN A CG 1 ATOM 4401 C CD . GLN A 1 537 ? 25.360 43.771 67.165 1.00 29.89 ? 578 GLN A CD 1 ATOM 4402 O OE1 . GLN A 1 537 ? 26.266 44.561 66.919 1.00 29.33 ? 578 GLN A OE1 1 ATOM 4403 N NE2 . GLN A 1 537 ? 25.526 42.681 67.923 1.00 30.28 ? 578 GLN A NE2 1 ATOM 4404 N N . VAL A 1 538 ? 22.847 47.090 63.334 1.00 21.72 ? 579 VAL A N 1 ATOM 4405 C CA . VAL A 1 538 ? 22.679 48.417 62.700 1.00 21.91 ? 579 VAL A CA 1 ATOM 4406 C C . VAL A 1 538 ? 21.222 48.626 62.325 1.00 21.34 ? 579 VAL A C 1 ATOM 4407 O O . VAL A 1 538 ? 20.629 49.637 62.715 1.00 21.37 ? 579 VAL A O 1 ATOM 4408 C CB . VAL A 1 538 ? 23.570 48.560 61.453 1.00 21.87 ? 579 VAL A CB 1 ATOM 4409 C CG1 . VAL A 1 538 ? 23.257 49.866 60.744 1.00 21.90 ? 579 VAL A CG1 1 ATOM 4410 C CG2 . VAL A 1 538 ? 25.053 48.582 61.886 1.00 22.94 ? 579 VAL A CG2 1 ATOM 4411 N N . ARG A 1 539 ? 20.637 47.715 61.544 1.00 20.53 ? 580 ARG A N 1 ATOM 4412 C CA . ARG A 1 539 ? 19.240 47.910 61.114 1.00 20.54 ? 580 ARG A CA 1 ATOM 4413 C C . ARG A 1 539 ? 18.301 47.906 62.298 1.00 21.87 ? 580 ARG A C 1 ATOM 4414 O O . ARG A 1 539 ? 17.427 48.764 62.404 1.00 20.61 ? 580 ARG A O 1 ATOM 4415 C CB . ARG A 1 539 ? 18.817 46.831 60.111 1.00 20.28 ? 580 ARG A CB 1 ATOM 4416 C CG . ARG A 1 539 ? 19.605 46.902 58.820 1.00 19.85 ? 580 ARG A CG 1 ATOM 4417 C CD . ARG A 1 539 ? 19.285 45.687 57.936 1.00 21.25 ? 580 ARG A CD 1 ATOM 4418 N NE . ARG A 1 539 ? 20.015 45.789 56.681 1.00 21.31 ? 580 ARG A NE 1 ATOM 4419 C CZ . ARG A 1 539 ? 20.000 44.854 55.738 1.00 21.11 ? 580 ARG A CZ 1 ATOM 4420 N NH1 . ARG A 1 539 ? 19.301 43.728 55.929 1.00 22.82 ? 580 ARG A NH1 1 ATOM 4421 N NH2 . ARG A 1 539 ? 20.652 45.066 54.589 1.00 21.52 ? 580 ARG A NH2 1 ATOM 4422 N N . GLY A 1 540 ? 18.468 46.943 63.192 1.00 21.09 ? 581 GLY A N 1 ATOM 4423 C CA . GLY A 1 540 ? 17.591 46.829 64.361 1.00 22.00 ? 581 GLY A CA 1 ATOM 4424 C C . GLY A 1 540 ? 17.788 47.972 65.327 1.00 22.34 ? 581 GLY A C 1 ATOM 4425 O O . GLY A 1 540 ? 16.806 48.498 65.884 1.00 21.70 ? 581 GLY A O 1 ATOM 4426 N N . GLY A 1 541 ? 19.046 48.358 65.538 1.00 21.76 ? 582 GLY A N 1 ATOM 4427 C CA . GLY A 1 541 ? 19.327 49.506 66.421 1.00 21.79 ? 582 GLY A CA 1 ATOM 4428 C C . GLY A 1 541 ? 18.689 50.798 65.907 1.00 22.23 ? 582 GLY A C 1 ATOM 4429 O O . GLY A 1 541 ? 18.182 51.614 66.701 1.00 22.20 ? 582 GLY A O 1 ATOM 4430 N N . MET A 1 542 ? 18.726 50.997 64.585 1.00 20.53 ? 583 MET A N 1 ATOM 4431 C CA A MET A 1 542 ? 18.084 52.174 63.996 0.50 20.33 ? 583 MET A CA 1 ATOM 4432 C CA B MET A 1 542 ? 18.083 52.157 63.961 0.50 21.30 ? 583 MET A CA 1 ATOM 4433 C C . MET A 1 542 ? 16.580 52.140 64.254 1.00 20.77 ? 583 MET A C 1 ATOM 4434 O O . MET A 1 542 ? 16.000 53.138 64.715 1.00 20.72 ? 583 MET A O 1 ATOM 4435 C CB A MET A 1 542 ? 18.390 52.318 62.499 0.50 19.59 ? 583 MET A CB 1 ATOM 4436 C CB B MET A 1 542 ? 18.338 52.180 62.445 0.50 21.40 ? 583 MET A CB 1 ATOM 4437 C CG A MET A 1 542 ? 19.812 52.751 62.229 0.50 19.87 ? 583 MET A CG 1 ATOM 4438 C CG B MET A 1 542 ? 19.809 52.347 62.072 0.50 25.70 ? 583 MET A CG 1 ATOM 4439 S SD A MET A 1 542 ? 20.237 52.794 60.490 0.50 17.40 ? 583 MET A SD 1 ATOM 4440 S SD B MET A 1 542 ? 20.338 54.038 62.311 0.50 36.64 ? 583 MET A SD 1 ATOM 4441 C CE A MET A 1 542 ? 19.477 54.315 59.951 0.50 17.99 ? 583 MET A CE 1 ATOM 4442 C CE B MET A 1 542 ? 19.462 54.831 60.941 0.50 32.49 ? 583 MET A CE 1 ATOM 4443 N N . VAL A 1 543 ? 15.950 50.982 64.010 1.00 20.00 ? 584 VAL A N 1 ATOM 4444 C CA . VAL A 1 543 ? 14.501 50.844 64.244 1.00 20.29 ? 584 VAL A CA 1 ATOM 4445 C C . VAL A 1 543 ? 14.209 51.087 65.735 1.00 20.80 ? 584 VAL A C 1 ATOM 4446 O O . VAL A 1 543 ? 13.259 51.822 66.058 1.00 20.59 ? 584 VAL A O 1 ATOM 4447 C CB . VAL A 1 543 ? 14.043 49.448 63.797 1.00 19.62 ? 584 VAL A CB 1 ATOM 4448 C CG1 . VAL A 1 543 ? 12.605 49.133 64.271 1.00 20.67 ? 584 VAL A CG1 1 ATOM 4449 C CG2 . VAL A 1 543 ? 14.138 49.320 62.247 1.00 18.98 ? 584 VAL A CG2 1 ATOM 4450 N N . PHE A 1 544 ? 15.027 50.487 66.624 1.00 21.53 ? 585 PHE A N 1 ATOM 4451 C CA . PHE A 1 544 ? 14.835 50.694 68.062 1.00 21.74 ? 585 PHE A CA 1 ATOM 4452 C C . PHE A 1 544 ? 14.845 52.172 68.462 1.00 22.36 ? 585 PHE A C 1 ATOM 4453 O O . PHE A 1 544 ? 13.924 52.641 69.163 1.00 23.18 ? 585 PHE A O 1 ATOM 4454 C CB . PHE A 1 544 ? 15.906 49.933 68.873 1.00 22.12 ? 585 PHE A CB 1 ATOM 4455 C CG . PHE A 1 544 ? 15.602 49.897 70.356 1.00 24.26 ? 585 PHE A CG 1 ATOM 4456 C CD1 . PHE A 1 544 ? 15.021 48.761 70.901 1.00 24.95 ? 585 PHE A CD1 1 ATOM 4457 C CD2 . PHE A 1 544 ? 15.816 51.010 71.155 1.00 26.66 ? 585 PHE A CD2 1 ATOM 4458 C CE1 . PHE A 1 544 ? 14.677 48.715 72.270 1.00 28.21 ? 585 PHE A CE1 1 ATOM 4459 C CE2 . PHE A 1 544 ? 15.490 50.981 72.514 1.00 25.62 ? 585 PHE A CE2 1 ATOM 4460 C CZ . PHE A 1 544 ? 14.910 49.823 73.059 1.00 28.63 ? 585 PHE A CZ 1 ATOM 4461 N N . GLU A 1 545 ? 15.838 52.916 67.994 1.00 22.59 ? 586 GLU A N 1 ATOM 4462 C CA A GLU A 1 545 ? 15.966 54.342 68.327 0.50 23.78 ? 586 GLU A CA 1 ATOM 4463 C CA B GLU A 1 545 ? 15.936 54.329 68.375 0.50 23.42 ? 586 GLU A CA 1 ATOM 4464 C C . GLU A 1 545 ? 14.835 55.162 67.743 1.00 22.81 ? 586 GLU A C 1 ATOM 4465 O O . GLU A 1 545 ? 14.269 56.019 68.396 1.00 22.72 ? 586 GLU A O 1 ATOM 4466 C CB A GLU A 1 545 ? 17.304 54.883 67.823 0.50 24.52 ? 586 GLU A CB 1 ATOM 4467 C CB B GLU A 1 545 ? 17.313 54.894 68.033 0.50 24.14 ? 586 GLU A CB 1 ATOM 4468 C CG A GLU A 1 545 ? 18.502 54.407 68.636 0.50 27.77 ? 586 GLU A CG 1 ATOM 4469 C CG B GLU A 1 545 ? 17.630 56.229 68.682 0.50 25.00 ? 586 GLU A CG 1 ATOM 4470 C CD A GLU A 1 545 ? 18.456 54.905 70.074 0.50 33.21 ? 586 GLU A CD 1 ATOM 4471 C CD B GLU A 1 545 ? 17.788 56.158 70.195 0.50 28.88 ? 586 GLU A CD 1 ATOM 4472 O OE1 A GLU A 1 545 ? 18.100 54.115 70.970 0.50 36.17 ? 586 GLU A OE1 1 ATOM 4473 O OE1 B GLU A 1 545 ? 17.607 55.068 70.785 0.50 28.39 ? 586 GLU A OE1 1 ATOM 4474 O OE2 A GLU A 1 545 ? 18.746 56.097 70.308 0.50 37.92 ? 586 GLU A OE2 1 ATOM 4475 O OE2 B GLU A 1 545 ? 18.122 57.200 70.804 0.50 32.60 ? 586 GLU A OE2 1 ATOM 4476 N N . LEU A 1 546 ? 14.505 54.888 66.481 1.00 20.84 ? 587 LEU A N 1 ATOM 4477 C CA . LEU A 1 546 ? 13.417 55.612 65.836 1.00 20.20 ? 587 LEU A CA 1 ATOM 4478 C C . LEU A 1 546 ? 12.092 55.343 66.544 1.00 21.37 ? 587 LEU A C 1 ATOM 4479 O O . LEU A 1 546 ? 11.251 56.241 66.655 1.00 21.84 ? 587 LEU A O 1 ATOM 4480 C CB . LEU A 1 546 ? 13.328 55.175 64.353 1.00 21.37 ? 587 LEU A CB 1 ATOM 4481 C CG . LEU A 1 546 ? 14.497 55.694 63.517 1.00 19.16 ? 587 LEU A CG 1 ATOM 4482 C CD1 . LEU A 1 546 ? 14.684 54.778 62.286 1.00 18.70 ? 587 LEU A CD1 1 ATOM 4483 C CD2 . LEU A 1 546 ? 14.191 57.159 63.076 1.00 22.87 ? 587 LEU A CD2 1 ATOM 4484 N N . ALA A 1 547 ? 11.889 54.108 67.011 1.00 21.18 ? 588 ALA A N 1 ATOM 4485 C CA . ALA A 1 547 ? 10.611 53.763 67.634 1.00 22.35 ? 588 ALA A CA 1 ATOM 4486 C C . ALA A 1 547 ? 10.572 54.115 69.135 1.00 23.01 ? 588 ALA A C 1 ATOM 4487 O O . ALA A 1 547 ? 9.481 54.142 69.682 1.00 24.07 ? 588 ALA A O 1 ATOM 4488 C CB . ALA A 1 547 ? 10.298 52.287 67.426 1.00 22.76 ? 588 ALA A CB 1 ATOM 4489 N N . ASN A 1 548 ? 11.721 54.384 69.761 1.00 22.97 ? 589 ASN A N 1 ATOM 4490 C CA . ASN A 1 548 ? 11.722 54.539 71.240 1.00 23.35 ? 589 ASN A CA 1 ATOM 4491 C C . ASN A 1 548 ? 12.209 55.851 71.782 1.00 24.68 ? 589 ASN A C 1 ATOM 4492 O O . ASN A 1 548 ? 11.862 56.203 72.934 1.00 27.44 ? 589 ASN A O 1 ATOM 4493 C CB . ASN A 1 548 ? 12.471 53.370 71.878 1.00 23.20 ? 589 ASN A CB 1 ATOM 4494 C CG A ASN A 1 548 ? 11.819 52.877 73.134 0.50 24.52 ? 589 ASN A CG 1 ATOM 4495 C CG B ASN A 1 548 ? 11.659 52.099 71.777 0.50 25.14 ? 589 ASN A CG 1 ATOM 4496 O OD1 A ASN A 1 548 ? 10.616 52.602 73.152 0.50 25.63 ? 589 ASN A OD1 1 ATOM 4497 O OD1 B ASN A 1 548 ? 10.677 51.935 72.490 0.50 25.86 ? 589 ASN A OD1 1 ATOM 4498 N ND2 A ASN A 1 548 ? 12.616 52.726 74.201 0.50 29.06 ? 589 ASN A ND2 1 ATOM 4499 N ND2 B ASN A 1 548 ? 12.029 51.215 70.841 0.50 25.71 ? 589 ASN A ND2 1 ATOM 4500 N N . SER A 1 549 ? 13.003 56.586 71.005 1.00 23.63 ? 590 SER A N 1 ATOM 4501 C CA A SER A 1 549 ? 13.551 57.865 71.487 0.50 23.77 ? 590 SER A CA 1 ATOM 4502 C CA B SER A 1 549 ? 13.536 57.864 71.490 0.50 24.91 ? 590 SER A CA 1 ATOM 4503 C C . SER A 1 549 ? 12.405 58.838 71.741 1.00 24.33 ? 590 SER A C 1 ATOM 4504 O O . SER A 1 549 ? 11.459 58.920 70.964 1.00 24.66 ? 590 SER A O 1 ATOM 4505 C CB A SER A 1 549 ? 14.562 58.439 70.478 0.50 23.78 ? 590 SER A CB 1 ATOM 4506 C CB B SER A 1 549 ? 14.523 58.438 70.480 0.50 25.10 ? 590 SER A CB 1 ATOM 4507 O OG A SER A 1 549 ? 15.192 59.609 70.986 0.50 21.22 ? 590 SER A OG 1 ATOM 4508 O OG B SER A 1 549 ? 15.698 57.672 70.505 0.50 29.13 ? 590 SER A OG 1 ATOM 4509 N N . ILE A 1 550 ? 12.465 59.561 72.852 1.00 24.14 ? 591 ILE A N 1 ATOM 4510 C CA A ILE A 1 550 ? 11.392 60.517 73.136 0.50 24.50 ? 591 ILE A CA 1 ATOM 4511 C CA B ILE A 1 550 ? 11.402 60.533 73.146 0.50 24.22 ? 591 ILE A CA 1 ATOM 4512 C C . ILE A 1 550 ? 11.324 61.592 72.061 1.00 24.16 ? 591 ILE A C 1 ATOM 4513 O O . ILE A 1 550 ? 10.246 61.873 71.531 1.00 24.43 ? 591 ILE A O 1 ATOM 4514 C CB A ILE A 1 550 ? 11.550 61.120 74.540 0.50 25.00 ? 591 ILE A CB 1 ATOM 4515 C CB B ILE A 1 550 ? 11.631 61.197 74.515 0.50 24.42 ? 591 ILE A CB 1 ATOM 4516 C CG1 A ILE A 1 550 ? 11.565 59.973 75.543 0.50 27.86 ? 591 ILE A CG1 1 ATOM 4517 C CG1 B ILE A 1 550 ? 11.404 60.168 75.610 0.50 26.89 ? 591 ILE A CG1 1 ATOM 4518 C CG2 A ILE A 1 550 ? 10.394 62.068 74.833 0.50 26.34 ? 591 ILE A CG2 1 ATOM 4519 C CG2 B ILE A 1 550 ? 10.697 62.390 74.691 0.50 25.26 ? 591 ILE A CG2 1 ATOM 4520 C CD1 A ILE A 1 550 ? 10.361 59.090 75.423 0.50 28.46 ? 591 ILE A CD1 1 ATOM 4521 C CD1 B ILE A 1 550 ? 12.176 60.508 76.839 0.50 24.42 ? 591 ILE A CD1 1 ATOM 4522 N N . VAL A 1 551 ? 12.473 62.176 71.749 1.00 25.27 ? 592 VAL A N 1 ATOM 4523 C CA . VAL A 1 551 ? 12.527 63.109 70.626 1.00 25.28 ? 592 VAL A CA 1 ATOM 4524 C C . VAL A 1 551 ? 13.000 62.269 69.436 1.00 23.84 ? 592 VAL A C 1 ATOM 4525 O O . VAL A 1 551 ? 13.963 61.501 69.584 1.00 25.50 ? 592 VAL A O 1 ATOM 4526 C CB . VAL A 1 551 ? 13.494 64.238 70.902 1.00 26.03 ? 592 VAL A CB 1 ATOM 4527 C CG1 . VAL A 1 551 ? 13.641 65.153 69.688 1.00 28.70 ? 592 VAL A CG1 1 ATOM 4528 C CG2 . VAL A 1 551 ? 12.977 65.068 72.105 1.00 29.00 ? 592 VAL A CG2 1 ATOM 4529 N N . LEU A 1 552 ? 12.359 62.421 68.271 1.00 23.48 ? 593 LEU A N 1 ATOM 4530 C CA . LEU A 1 552 ? 12.776 61.647 67.092 1.00 22.55 ? 593 LEU A CA 1 ATOM 4531 C C . LEU A 1 552 ? 14.250 61.929 66.823 1.00 22.35 ? 593 LEU A C 1 ATOM 4532 O O . LEU A 1 552 ? 14.701 63.076 66.933 1.00 24.46 ? 593 LEU A O 1 ATOM 4533 C CB . LEU A 1 552 ? 11.909 62.030 65.879 1.00 21.31 ? 593 LEU A CB 1 ATOM 4534 C CG . LEU A 1 552 ? 10.525 61.391 65.863 1.00 24.11 ? 593 LEU A CG 1 ATOM 4535 C CD1 . LEU A 1 552 ? 9.724 61.945 64.666 1.00 22.79 ? 593 LEU A CD1 1 ATOM 4536 C CD2 . LEU A 1 552 ? 10.670 59.832 65.733 1.00 25.85 ? 593 LEU A CD2 1 ATOM 4537 N N . PRO A 1 553 ? 15.034 60.881 66.490 1.00 22.02 ? 594 PRO A N 1 ATOM 4538 C CA . PRO A 1 553 ? 16.486 61.045 66.367 1.00 23.78 ? 594 PRO A CA 1 ATOM 4539 C C . PRO A 1 553 ? 16.919 61.535 64.951 1.00 23.93 ? 594 PRO A C 1 ATOM 4540 O O . PRO A 1 553 ? 17.655 60.850 64.229 1.00 25.30 ? 594 PRO A O 1 ATOM 4541 C CB . PRO A 1 553 ? 17.005 59.617 66.641 1.00 23.60 ? 594 PRO A CB 1 ATOM 4542 C CG . PRO A 1 553 ? 15.949 58.744 66.013 1.00 24.29 ? 594 PRO A CG 1 ATOM 4543 C CD . PRO A 1 553 ? 14.638 59.468 66.400 1.00 21.99 ? 594 PRO A CD 1 ATOM 4544 N N . PHE A 1 554 ? 16.405 62.694 64.572 1.00 22.93 ? 595 PHE A N 1 ATOM 4545 C CA . PHE A 1 554 ? 16.659 63.340 63.268 1.00 22.85 ? 595 PHE A CA 1 ATOM 4546 C C . PHE A 1 554 ? 17.340 64.659 63.532 1.00 24.87 ? 595 PHE A C 1 ATOM 4547 O O . PHE A 1 554 ? 16.912 65.389 64.484 1.00 26.27 ? 595 PHE A O 1 ATOM 4548 C CB . PHE A 1 554 ? 15.339 63.692 62.590 1.00 21.51 ? 595 PHE A CB 1 ATOM 4549 C CG . PHE A 1 554 ? 14.542 62.520 62.082 1.00 20.83 ? 595 PHE A CG 1 ATOM 4550 C CD1 . PHE A 1 554 ? 15.135 61.296 61.798 1.00 22.46 ? 595 PHE A CD1 1 ATOM 4551 C CD2 . PHE A 1 554 ? 13.193 62.688 61.799 1.00 22.35 ? 595 PHE A CD2 1 ATOM 4552 C CE1 . PHE A 1 554 ? 14.363 60.228 61.272 1.00 20.53 ? 595 PHE A CE1 1 ATOM 4553 C CE2 . PHE A 1 554 ? 12.421 61.615 61.315 1.00 23.65 ? 595 PHE A CE2 1 ATOM 4554 C CZ . PHE A 1 554 ? 13.013 60.391 61.055 1.00 20.51 ? 595 PHE A CZ 1 ATOM 4555 N N . ASP A 1 555 ? 18.392 64.989 62.777 1.00 23.49 ? 596 ASP A N 1 ATOM 4556 C CA . ASP A 1 555 ? 19.066 66.287 62.942 1.00 23.50 ? 596 ASP A CA 1 ATOM 4557 C C . ASP A 1 555 ? 18.877 67.132 61.691 1.00 24.32 ? 596 ASP A C 1 ATOM 4558 O O . ASP A 1 555 ? 19.521 66.869 60.640 1.00 24.33 ? 596 ASP A O 1 ATOM 4559 C CB . ASP A 1 555 ? 20.556 66.138 63.270 1.00 24.17 ? 596 ASP A CB 1 ATOM 4560 C CG . ASP A 1 555 ? 21.152 67.441 63.783 1.00 26.80 ? 596 ASP A CG 1 ATOM 4561 O OD1 . ASP A 1 555 ? 20.566 68.517 63.576 1.00 26.58 ? 596 ASP A OD1 1 ATOM 4562 O OD2 . ASP A 1 555 ? 22.208 67.368 64.473 1.00 28.84 ? 596 ASP A OD2 1 ATOM 4563 N N . CYS A 1 556 ? 17.954 68.097 61.770 1.00 23.00 ? 597 CYS A N 1 ATOM 4564 C CA . CYS A 1 556 ? 17.703 68.928 60.587 1.00 23.36 ? 597 CYS A CA 1 ATOM 4565 C C . CYS A 1 556 ? 18.939 69.703 60.122 1.00 23.15 ? 597 CYS A C 1 ATOM 4566 O O . CYS A 1 556 ? 19.024 70.091 58.943 1.00 23.31 ? 597 CYS A O 1 ATOM 4567 C CB . CYS A 1 556 ? 16.544 69.894 60.847 1.00 22.99 ? 597 CYS A CB 1 ATOM 4568 S SG . CYS A 1 556 ? 16.834 71.015 62.271 1.00 28.68 ? 597 CYS A SG 1 ATOM 4569 N N . ARG A 1 557 ? 19.900 69.977 61.000 1.00 22.73 ? 598 ARG A N 1 ATOM 4570 C CA . ARG A 1 557 ? 21.072 70.741 60.579 1.00 23.32 ? 598 ARG A CA 1 ATOM 4571 C C . ARG A 1 557 ? 21.910 69.969 59.542 1.00 24.28 ? 598 ARG A C 1 ATOM 4572 O O . ARG A 1 557 ? 22.633 70.561 58.733 1.00 25.40 ? 598 ARG A O 1 ATOM 4573 C CB . ARG A 1 557 ? 21.939 71.086 61.792 1.00 24.44 ? 598 ARG A CB 1 ATOM 4574 C CG . ARG A 1 557 ? 21.203 72.020 62.738 1.00 23.44 ? 598 ARG A CG 1 ATOM 4575 C CD . ARG A 1 557 ? 21.993 72.177 64.067 1.00 25.07 ? 598 ARG A CD 1 ATOM 4576 N NE . ARG A 1 557 ? 22.105 70.892 64.733 1.00 27.24 ? 598 ARG A NE 1 ATOM 4577 C CZ . ARG A 1 557 ? 22.749 70.707 65.895 1.00 31.58 ? 598 ARG A CZ 1 ATOM 4578 N NH1 . ARG A 1 557 ? 23.284 71.740 66.520 1.00 32.67 ? 598 ARG A NH1 1 ATOM 4579 N NH2 . ARG A 1 557 ? 22.825 69.500 66.435 1.00 31.43 ? 598 ARG A NH2 1 ATOM 4580 N N . ASP A 1 558 ? 21.821 68.645 59.581 1.00 22.97 ? 599 ASP A N 1 ATOM 4581 C CA . ASP A 1 558 ? 22.553 67.817 58.612 1.00 23.35 ? 599 ASP A CA 1 ATOM 4582 C C . ASP A 1 558 ? 21.968 67.993 57.210 1.00 22.67 ? 599 ASP A C 1 ATOM 4583 O O . ASP A 1 558 ? 22.696 67.914 56.219 1.00 23.47 ? 599 ASP A O 1 ATOM 4584 C CB . ASP A 1 558 ? 22.542 66.353 59.053 1.00 22.79 ? 599 ASP A CB 1 ATOM 4585 C CG . ASP A 1 558 ? 23.538 66.098 60.211 1.00 29.61 ? 599 ASP A CG 1 ATOM 4586 O OD1 . ASP A 1 558 ? 24.541 66.828 60.315 1.00 38.44 ? 599 ASP A OD1 1 ATOM 4587 O OD2 . ASP A 1 558 ? 23.297 65.236 61.059 1.00 29.77 ? 599 ASP A OD2 1 ATOM 4588 N N . TYR A 1 559 ? 20.665 68.237 57.128 1.00 21.33 ? 600 TYR A N 1 ATOM 4589 C CA . TYR A 1 559 ? 20.075 68.524 55.805 1.00 20.27 ? 600 TYR A CA 1 ATOM 4590 C C . TYR A 1 559 ? 20.616 69.870 55.325 1.00 21.38 ? 600 TYR A C 1 ATOM 4591 O O . TYR A 1 559 ? 20.922 70.033 54.142 1.00 20.84 ? 600 TYR A O 1 ATOM 4592 C CB . TYR A 1 559 ? 18.539 68.579 55.862 1.00 20.12 ? 600 TYR A CB 1 ATOM 4593 C CG . TYR A 1 559 ? 17.880 67.624 54.887 1.00 19.89 ? 600 TYR A CG 1 ATOM 4594 C CD1 . TYR A 1 559 ? 18.251 67.629 53.538 1.00 20.71 ? 600 TYR A CD1 1 ATOM 4595 C CD2 . TYR A 1 559 ? 16.931 66.722 55.312 1.00 21.11 ? 600 TYR A CD2 1 ATOM 4596 C CE1 . TYR A 1 559 ? 17.658 66.753 52.629 1.00 22.23 ? 600 TYR A CE1 1 ATOM 4597 C CE2 . TYR A 1 559 ? 16.335 65.812 54.404 1.00 20.23 ? 600 TYR A CE2 1 ATOM 4598 C CZ . TYR A 1 559 ? 16.715 65.859 53.057 1.00 21.85 ? 600 TYR A CZ 1 ATOM 4599 O OH . TYR A 1 559 ? 16.117 64.973 52.167 1.00 21.22 ? 600 TYR A OH 1 ATOM 4600 N N . ALA A 1 560 ? 20.747 70.845 56.225 1.00 20.91 ? 601 ALA A N 1 ATOM 4601 C CA . ALA A 1 560 ? 21.253 72.150 55.802 1.00 21.45 ? 601 ALA A CA 1 ATOM 4602 C C . ALA A 1 560 ? 22.660 72.056 55.182 1.00 22.50 ? 601 ALA A C 1 ATOM 4603 O O . ALA A 1 560 ? 22.932 72.673 54.128 1.00 22.99 ? 601 ALA A O 1 ATOM 4604 C CB . ALA A 1 560 ? 21.221 73.154 56.985 1.00 21.53 ? 601 ALA A CB 1 ATOM 4605 N N . VAL A 1 561 ? 23.546 71.284 55.822 1.00 23.14 ? 602 VAL A N 1 ATOM 4606 C CA . VAL A 1 561 ? 24.885 71.068 55.320 1.00 23.85 ? 602 VAL A CA 1 ATOM 4607 C C . VAL A 1 561 ? 24.874 70.492 53.898 1.00 23.61 ? 602 VAL A C 1 ATOM 4608 O O . VAL A 1 561 ? 25.529 71.044 53.015 1.00 25.30 ? 602 VAL A O 1 ATOM 4609 C CB . VAL A 1 561 ? 25.657 70.157 56.264 1.00 25.26 ? 602 VAL A CB 1 ATOM 4610 C CG1 . VAL A 1 561 ? 27.067 69.804 55.660 1.00 28.47 ? 602 VAL A CG1 1 ATOM 4611 C CG2 . VAL A 1 561 ? 25.826 70.941 57.532 1.00 29.22 ? 602 VAL A CG2 1 ATOM 4612 N N . VAL A 1 562 ? 24.106 69.429 53.686 1.00 21.75 ? 603 VAL A N 1 ATOM 4613 C CA . VAL A 1 562 ? 24.098 68.786 52.346 1.00 21.72 ? 603 VAL A CA 1 ATOM 4614 C C . VAL A 1 562 ? 23.442 69.662 51.296 1.00 21.48 ? 603 VAL A C 1 ATOM 4615 O O . VAL A 1 562 ? 23.875 69.648 50.145 1.00 21.52 ? 603 VAL A O 1 ATOM 4616 C CB . VAL A 1 562 ? 23.581 67.341 52.296 1.00 22.53 ? 603 VAL A CB 1 ATOM 4617 C CG1 . VAL A 1 562 ? 24.363 66.451 53.330 1.00 24.37 ? 603 VAL A CG1 1 ATOM 4618 C CG2 . VAL A 1 562 ? 22.102 67.272 52.475 1.00 24.42 ? 603 VAL A CG2 1 ATOM 4619 N N . LEU A 1 563 ? 22.443 70.441 51.683 1.00 19.88 ? 604 LEU A N 1 ATOM 4620 C CA . LEU A 1 563 ? 21.746 71.271 50.687 1.00 20.33 ? 604 LEU A CA 1 ATOM 4621 C C . LEU A 1 563 ? 22.726 72.281 50.119 1.00 20.78 ? 604 LEU A C 1 ATOM 4622 O O . LEU A 1 563 ? 22.682 72.580 48.914 1.00 22.19 ? 604 LEU A O 1 ATOM 4623 C CB . LEU A 1 563 ? 20.521 71.983 51.286 1.00 19.05 ? 604 LEU A CB 1 ATOM 4624 C CG . LEU A 1 563 ? 19.315 71.058 51.535 1.00 19.17 ? 604 LEU A CG 1 ATOM 4625 C CD1 . LEU A 1 563 ? 18.309 71.800 52.388 1.00 21.07 ? 604 LEU A CD1 1 ATOM 4626 C CD2 . LEU A 1 563 ? 18.664 70.575 50.177 1.00 20.42 ? 604 LEU A CD2 1 ATOM 4627 N N . ARG A 1 564 ? 23.646 72.801 50.955 1.00 21.82 ? 605 ARG A N 1 ATOM 4628 C CA . ARG A 1 564 ? 24.651 73.741 50.450 1.00 22.26 ? 605 ARG A CA 1 ATOM 4629 C C . ARG A 1 564 ? 25.606 73.039 49.495 1.00 22.06 ? 605 ARG A C 1 ATOM 4630 O O . ARG A 1 564 ? 25.916 73.581 48.431 1.00 22.09 ? 605 ARG A O 1 ATOM 4631 C CB . ARG A 1 564 ? 25.404 74.422 51.605 1.00 22.84 ? 605 ARG A CB 1 ATOM 4632 C CG . ARG A 1 564 ? 26.533 75.338 51.126 1.00 26.61 ? 605 ARG A CG 1 ATOM 4633 C CD . ARG A 1 564 ? 26.017 76.463 50.198 1.00 29.98 ? 605 ARG A CD 1 ATOM 4634 N NE . ARG A 1 564 ? 27.137 77.276 49.736 1.00 34.65 ? 605 ARG A NE 1 ATOM 4635 C CZ . ARG A 1 564 ? 27.581 78.351 50.383 1.00 40.00 ? 605 ARG A CZ 1 ATOM 4636 N NH1 . ARG A 1 564 ? 27.004 78.730 51.529 1.00 38.62 ? 605 ARG A NH1 1 ATOM 4637 N NH2 . ARG A 1 564 ? 28.622 79.036 49.909 1.00 43.29 ? 605 ARG A NH2 1 ATOM 4638 N N A LYS A 1 565 ? 26.077 71.843 49.882 0.70 22.09 ? 606 LYS A N 1 ATOM 4639 N N B LYS A 1 565 ? 26.064 71.831 49.835 0.30 21.89 ? 606 LYS A N 1 ATOM 4640 C CA A LYS A 1 565 ? 26.864 70.995 49.003 0.70 23.07 ? 606 LYS A CA 1 ATOM 4641 C CA B LYS A 1 565 ? 26.925 71.092 48.911 0.30 22.24 ? 606 LYS A CA 1 ATOM 4642 C C A LYS A 1 565 ? 26.197 70.799 47.625 0.70 22.38 ? 606 LYS A C 1 ATOM 4643 C C B LYS A 1 565 ? 26.214 70.744 47.588 0.30 21.80 ? 606 LYS A C 1 ATOM 4644 O O A LYS A 1 565 ? 26.841 71.002 46.584 0.70 22.10 ? 606 LYS A O 1 ATOM 4645 O O B LYS A 1 565 ? 26.844 70.786 46.527 0.30 21.94 ? 606 LYS A O 1 ATOM 4646 C CB A LYS A 1 565 ? 27.082 69.636 49.682 0.70 24.16 ? 606 LYS A CB 1 ATOM 4647 C CB B LYS A 1 565 ? 27.534 69.851 49.574 0.30 22.88 ? 606 LYS A CB 1 ATOM 4648 C CG A LYS A 1 565 ? 28.041 68.712 48.934 0.70 27.00 ? 606 LYS A CG 1 ATOM 4649 C CG B LYS A 1 565 ? 28.081 70.100 50.954 0.30 22.80 ? 606 LYS A CG 1 ATOM 4650 C CD A LYS A 1 565 ? 28.336 67.432 49.762 0.70 31.91 ? 606 LYS A CD 1 ATOM 4651 C CD B LYS A 1 565 ? 29.189 69.106 51.331 0.30 29.62 ? 606 LYS A CD 1 ATOM 4652 C CE A LYS A 1 565 ? 27.070 66.589 49.970 0.70 31.70 ? 606 LYS A CE 1 ATOM 4653 C CE B LYS A 1 565 ? 28.617 67.708 51.606 0.30 28.96 ? 606 LYS A CE 1 ATOM 4654 N NZ A LYS A 1 565 ? 27.370 65.199 50.410 0.70 34.01 ? 606 LYS A NZ 1 ATOM 4655 N NZ B LYS A 1 565 ? 27.895 67.597 52.921 0.30 29.72 ? 606 LYS A NZ 1 ATOM 4656 N N . TYR A 1 566 ? 24.914 70.438 47.641 1.00 21.00 ? 607 TYR A N 1 ATOM 4657 C CA . TYR A 1 566 ? 24.179 70.121 46.394 1.00 20.16 ? 607 TYR A CA 1 ATOM 4658 C C . TYR A 1 566 ? 23.979 71.394 45.575 1.00 20.18 ? 607 TYR A C 1 ATOM 4659 O O . TYR A 1 566 ? 24.084 71.343 44.344 1.00 20.69 ? 607 TYR A O 1 ATOM 4660 C CB . TYR A 1 566 ? 22.823 69.512 46.680 1.00 19.54 ? 607 TYR A CB 1 ATOM 4661 C CG . TYR A 1 566 ? 22.877 68.188 47.441 1.00 19.20 ? 607 TYR A CG 1 ATOM 4662 C CD1 . TYR A 1 566 ? 24.009 67.402 47.454 1.00 19.18 ? 607 TYR A CD1 1 ATOM 4663 C CD2 . TYR A 1 566 ? 21.770 67.769 48.178 1.00 20.11 ? 607 TYR A CD2 1 ATOM 4664 C CE1 . TYR A 1 566 ? 24.030 66.191 48.177 1.00 20.68 ? 607 TYR A CE1 1 ATOM 4665 C CE2 . TYR A 1 566 ? 21.774 66.569 48.866 1.00 20.08 ? 607 TYR A CE2 1 ATOM 4666 C CZ . TYR A 1 566 ? 22.918 65.793 48.862 1.00 24.20 ? 607 TYR A CZ 1 ATOM 4667 O OH . TYR A 1 566 ? 22.943 64.604 49.582 1.00 25.33 ? 607 TYR A OH 1 ATOM 4668 N N . ALA A 1 567 ? 23.756 72.513 46.245 1.00 20.02 ? 608 ALA A N 1 ATOM 4669 C CA . ALA A 1 567 ? 23.592 73.766 45.516 1.00 21.25 ? 608 ALA A CA 1 ATOM 4670 C C . ALA A 1 567 ? 24.904 74.165 44.847 1.00 22.50 ? 608 ALA A C 1 ATOM 4671 O O . ALA A 1 567 ? 24.902 74.604 43.700 1.00 24.00 ? 608 ALA A O 1 ATOM 4672 C CB . ALA A 1 567 ? 23.142 74.884 46.466 1.00 21.50 ? 608 ALA A CB 1 ATOM 4673 N N . ASP A 1 568 ? 26.024 74.073 45.581 1.00 23.38 ? 609 ASP A N 1 ATOM 4674 C CA . ASP A 1 568 ? 27.352 74.342 44.995 1.00 24.78 ? 609 ASP A CA 1 ATOM 4675 C C . ASP A 1 568 ? 27.594 73.440 43.746 1.00 24.07 ? 609 ASP A C 1 ATOM 4676 O O . ASP A 1 568 ? 28.091 73.907 42.727 1.00 23.79 ? 609 ASP A O 1 ATOM 4677 C CB . ASP A 1 568 ? 28.465 74.064 46.029 1.00 26.17 ? 609 ASP A CB 1 ATOM 4678 C CG . ASP A 1 568 ? 28.566 75.125 47.124 1.00 31.60 ? 609 ASP A CG 1 ATOM 4679 O OD1 . ASP A 1 568 ? 28.076 76.235 46.960 1.00 34.92 ? 609 ASP A OD1 1 ATOM 4680 O OD2 . ASP A 1 568 ? 29.214 74.839 48.176 1.00 37.47 ? 609 ASP A OD2 1 ATOM 4681 N N . LYS A 1 569 ? 27.193 72.176 43.834 1.00 22.50 ? 610 LYS A N 1 ATOM 4682 C CA . LYS A 1 569 ? 27.462 71.224 42.771 1.00 23.73 ? 610 LYS A CA 1 ATOM 4683 C C . LYS A 1 569 ? 26.630 71.572 41.532 1.00 22.60 ? 610 LYS A C 1 ATOM 4684 O O . LYS A 1 569 ? 27.146 71.574 40.417 1.00 24.18 ? 610 LYS A O 1 ATOM 4685 C CB . LYS A 1 569 ? 27.106 69.817 43.244 1.00 23.65 ? 610 LYS A CB 1 ATOM 4686 C CG . LYS A 1 569 ? 27.309 68.764 42.185 1.00 27.08 ? 610 LYS A CG 1 ATOM 4687 C CD . LYS A 1 569 ? 26.893 67.434 42.751 1.00 31.46 ? 610 LYS A CD 1 ATOM 4688 C CE . LYS A 1 569 ? 27.635 66.275 42.100 1.00 37.14 ? 610 LYS A CE 1 ATOM 4689 N NZ . LYS A 1 569 ? 26.908 65.001 42.406 1.00 40.54 ? 610 LYS A NZ 1 ATOM 4690 N N . ILE A 1 570 ? 25.338 71.862 41.735 1.00 21.73 ? 611 ILE A N 1 ATOM 4691 C CA . ILE A 1 570 ? 24.485 72.143 40.567 1.00 21.46 ? 611 ILE A CA 1 ATOM 4692 C C . ILE A 1 570 ? 24.870 73.501 39.911 1.00 21.61 ? 611 ILE A C 1 ATOM 4693 O O . ILE A 1 570 ? 24.888 73.613 38.667 1.00 21.87 ? 611 ILE A O 1 ATOM 4694 C CB . ILE A 1 570 ? 22.971 72.033 40.908 1.00 21.50 ? 611 ILE A CB 1 ATOM 4695 C CG1 . ILE A 1 570 ? 22.128 72.015 39.633 1.00 23.95 ? 611 ILE A CG1 1 ATOM 4696 C CG2 . ILE A 1 570 ? 22.502 73.167 41.824 1.00 22.81 ? 611 ILE A CG2 1 ATOM 4697 C CD1 . ILE A 1 570 ? 22.288 70.740 38.808 1.00 25.33 ? 611 ILE A CD1 1 ATOM 4698 N N . TYR A 1 571 ? 25.230 74.503 40.730 1.00 22.14 ? 612 TYR A N 1 ATOM 4699 C CA . TYR A 1 571 ? 25.744 75.760 40.231 1.00 24.73 ? 612 TYR A CA 1 ATOM 4700 C C . TYR A 1 571 ? 27.005 75.515 39.374 1.00 24.83 ? 612 TYR A C 1 ATOM 4701 O O . TYR A 1 571 ? 27.168 76.099 38.305 1.00 24.65 ? 612 TYR A O 1 ATOM 4702 C CB . TYR A 1 571 ? 26.071 76.690 41.436 1.00 24.44 ? 612 TYR A CB 1 ATOM 4703 C CG . TYR A 1 571 ? 26.850 77.905 41.014 1.00 29.79 ? 612 TYR A CG 1 ATOM 4704 C CD1 . TYR A 1 571 ? 26.200 78.981 40.408 1.00 32.83 ? 612 TYR A CD1 1 ATOM 4705 C CD2 . TYR A 1 571 ? 28.240 77.938 41.169 1.00 34.81 ? 612 TYR A CD2 1 ATOM 4706 C CE1 . TYR A 1 571 ? 26.937 80.117 40.008 1.00 38.38 ? 612 TYR A CE1 1 ATOM 4707 C CE2 . TYR A 1 571 ? 28.992 79.048 40.757 1.00 38.77 ? 612 TYR A CE2 1 ATOM 4708 C CZ . TYR A 1 571 ? 28.320 80.116 40.176 1.00 41.25 ? 612 TYR A CZ 1 ATOM 4709 O OH . TYR A 1 571 ? 29.081 81.202 39.770 1.00 50.68 ? 612 TYR A OH 1 ATOM 4710 N N . SER A 1 572 ? 27.891 74.627 39.842 1.00 25.05 ? 613 SER A N 1 ATOM 4711 C CA . SER A 1 572 ? 29.145 74.391 39.138 1.00 27.04 ? 613 SER A CA 1 ATOM 4712 C C . SER A 1 572 ? 28.893 73.715 37.777 1.00 26.98 ? 613 SER A C 1 ATOM 4713 O O . SER A 1 572 ? 29.615 73.990 36.827 1.00 28.75 ? 613 SER A O 1 ATOM 4714 C CB . SER A 1 572 ? 30.109 73.561 40.002 1.00 27.47 ? 613 SER A CB 1 ATOM 4715 O OG A SER A 1 572 ? 30.586 74.376 41.048 0.50 29.81 ? 613 SER A OG 1 ATOM 4716 O OG B SER A 1 572 ? 29.763 72.198 39.973 0.50 30.23 ? 613 SER A OG 1 ATOM 4717 N N . ILE A 1 573 ? 27.867 72.856 37.688 1.00 26.19 ? 614 ILE A N 1 ATOM 4718 C CA . ILE A 1 573 ? 27.492 72.260 36.404 1.00 25.39 ? 614 ILE A CA 1 ATOM 4719 C C . ILE A 1 573 ? 27.014 73.332 35.432 1.00 26.29 ? 614 ILE A C 1 ATOM 4720 O O . ILE A 1 573 ? 27.423 73.371 34.257 1.00 26.88 ? 614 ILE A O 1 ATOM 4721 C CB . ILE A 1 573 ? 26.399 71.157 36.590 1.00 25.04 ? 614 ILE A CB 1 ATOM 4722 C CG1 . ILE A 1 573 ? 27.041 69.941 37.276 1.00 25.05 ? 614 ILE A CG1 1 ATOM 4723 C CG2 . ILE A 1 573 ? 25.751 70.783 35.241 1.00 26.92 ? 614 ILE A CG2 1 ATOM 4724 C CD1 . ILE A 1 573 ? 25.992 68.934 37.786 1.00 24.80 ? 614 ILE A CD1 1 ATOM 4725 N N . SER A 1 574 ? 26.156 74.226 35.929 1.00 24.88 ? 615 SER A N 1 ATOM 4726 C CA . SER A 1 574 ? 25.625 75.299 35.090 1.00 25.29 ? 615 SER A CA 1 ATOM 4727 C C . SER A 1 574 ? 26.730 76.212 34.603 1.00 27.33 ? 615 SER A C 1 ATOM 4728 O O . SER A 1 574 ? 26.715 76.679 33.446 1.00 27.40 ? 615 SER A O 1 ATOM 4729 C CB . SER A 1 574 ? 24.575 76.094 35.880 1.00 25.40 ? 615 SER A CB 1 ATOM 4730 O OG . SER A 1 574 ? 23.876 76.986 35.025 1.00 26.63 ? 615 SER A OG 1 ATOM 4731 N N . MET A 1 575 ? 27.684 76.473 35.490 1.00 26.85 ? 616 MET A N 1 ATOM 4732 C CA . MET A 1 575 ? 28.780 77.402 35.173 1.00 29.93 ? 616 MET A CA 1 ATOM 4733 C C . MET A 1 575 ? 29.761 76.897 34.123 1.00 31.50 ? 616 MET A C 1 ATOM 4734 O O . MET A 1 575 ? 30.662 77.644 33.715 1.00 33.14 ? 616 MET A O 1 ATOM 4735 C CB . MET A 1 575 ? 29.485 77.857 36.437 1.00 30.57 ? 616 MET A CB 1 ATOM 4736 C CG . MET A 1 575 ? 28.723 78.979 37.131 1.00 34.05 ? 616 MET A CG 1 ATOM 4737 S SD . MET A 1 575 ? 28.585 80.513 36.124 1.00 44.60 ? 616 MET A SD 1 ATOM 4738 C CE . MET A 1 575 ? 30.291 80.975 35.915 1.00 40.78 ? 616 MET A CE 1 ATOM 4739 N N . LYS A 1 576 ? 29.572 75.667 33.650 1.00 32.39 ? 617 LYS A N 1 ATOM 4740 C CA . LYS A 1 576 ? 30.282 75.228 32.438 1.00 33.72 ? 617 LYS A CA 1 ATOM 4741 C C . LYS A 1 576 ? 29.778 75.972 31.186 1.00 32.97 ? 617 LYS A C 1 ATOM 4742 O O . LYS A 1 576 ? 30.438 75.917 30.148 1.00 33.25 ? 617 LYS A O 1 ATOM 4743 C CB . LYS A 1 576 ? 30.176 73.711 32.218 1.00 35.36 ? 617 LYS A CB 1 ATOM 4744 C CG . LYS A 1 576 ? 30.654 72.820 33.370 1.00 39.59 ? 617 LYS A CG 1 ATOM 4745 C CD . LYS A 1 576 ? 32.168 72.863 33.584 1.00 50.07 ? 617 LYS A CD 1 ATOM 4746 C CE . LYS A 1 576 ? 32.581 71.949 34.765 1.00 53.33 ? 617 LYS A CE 1 ATOM 4747 N NZ . LYS A 1 576 ? 34.048 72.048 35.006 1.00 58.44 ? 617 LYS A NZ 1 ATOM 4748 N N . HIS A 1 577 ? 28.667 76.710 31.309 1.00 29.84 ? 618 HIS A N 1 ATOM 4749 C CA . HIS A 1 577 ? 28.019 77.434 30.184 1.00 29.85 ? 618 HIS A CA 1 ATOM 4750 C C . HIS A 1 577 ? 27.844 78.929 30.502 1.00 30.47 ? 618 HIS A C 1 ATOM 4751 O O . HIS A 1 577 ? 26.704 79.431 30.552 1.00 29.60 ? 618 HIS A O 1 ATOM 4752 C CB . HIS A 1 577 ? 26.631 76.840 29.921 1.00 29.26 ? 618 HIS A CB 1 ATOM 4753 C CG . HIS A 1 577 ? 26.620 75.344 29.866 1.00 32.58 ? 618 HIS A CG 1 ATOM 4754 N ND1 . HIS A 1 577 ? 26.828 74.649 28.695 1.00 35.07 ? 618 HIS A ND1 1 ATOM 4755 C CD2 . HIS A 1 577 ? 26.414 74.411 30.832 1.00 35.12 ? 618 HIS A CD2 1 ATOM 4756 C CE1 . HIS A 1 577 ? 26.760 73.351 28.941 1.00 34.71 ? 618 HIS A CE1 1 ATOM 4757 N NE2 . HIS A 1 577 ? 26.519 73.177 30.230 1.00 36.04 ? 618 HIS A NE2 1 ATOM 4758 N N . PRO A 1 578 ? 28.957 79.649 30.737 1.00 31.12 ? 619 PRO A N 1 ATOM 4759 C CA . PRO A 1 578 ? 28.796 81.025 31.211 1.00 31.43 ? 619 PRO A CA 1 ATOM 4760 C C . PRO A 1 578 ? 28.107 81.945 30.209 1.00 32.02 ? 619 PRO A C 1 ATOM 4761 O O . PRO A 1 578 ? 27.319 82.797 30.637 1.00 31.88 ? 619 PRO A O 1 ATOM 4762 C CB . PRO A 1 578 ? 30.231 81.499 31.472 1.00 33.40 ? 619 PRO A CB 1 ATOM 4763 C CG . PRO A 1 578 ? 31.117 80.507 30.704 1.00 34.30 ? 619 PRO A CG 1 ATOM 4764 C CD . PRO A 1 578 ? 30.369 79.220 30.737 1.00 32.04 ? 619 PRO A CD 1 ATOM 4765 N N . GLN A 1 579 ? 28.375 81.797 28.906 1.00 32.15 ? 620 GLN A N 1 ATOM 4766 C CA A GLN A 1 579 ? 27.730 82.706 27.952 0.50 32.42 ? 620 GLN A CA 1 ATOM 4767 C CA B GLN A 1 579 ? 27.729 82.618 27.865 0.50 33.10 ? 620 GLN A CA 1 ATOM 4768 C C . GLN A 1 579 ? 26.198 82.514 27.962 1.00 31.32 ? 620 GLN A C 1 ATOM 4769 O O . GLN A 1 579 ? 25.462 83.501 27.881 1.00 31.48 ? 620 GLN A O 1 ATOM 4770 C CB A GLN A 1 579 ? 28.330 82.598 26.541 0.50 33.85 ? 620 GLN A CB 1 ATOM 4771 C CB B GLN A 1 579 ? 28.199 82.138 26.480 0.50 34.39 ? 620 GLN A CB 1 ATOM 4772 C CG A GLN A 1 579 ? 27.901 83.709 25.542 0.50 35.40 ? 620 GLN A CG 1 ATOM 4773 C CG B GLN A 1 579 ? 27.497 82.754 25.268 0.50 39.09 ? 620 GLN A CG 1 ATOM 4774 C CD A GLN A 1 579 ? 27.965 85.124 26.107 0.50 36.31 ? 620 GLN A CD 1 ATOM 4775 C CD B GLN A 1 579 ? 28.270 82.548 23.960 0.50 45.93 ? 620 GLN A CD 1 ATOM 4776 O OE1 A GLN A 1 579 ? 29.040 85.736 26.203 0.50 40.07 ? 620 GLN A OE1 1 ATOM 4777 O OE1 B GLN A 1 579 ? 29.276 81.822 23.911 0.50 49.39 ? 620 GLN A OE1 1 ATOM 4778 N NE2 A GLN A 1 579 ? 26.802 85.672 26.439 0.50 29.75 ? 620 GLN A NE2 1 ATOM 4779 N NE2 B GLN A 1 579 ? 27.810 83.204 22.895 0.50 47.41 ? 620 GLN A NE2 1 ATOM 4780 N N . GLU A 1 580 ? 25.711 81.280 28.097 1.00 29.74 ? 621 GLU A N 1 ATOM 4781 C CA . GLU A 1 580 ? 24.260 81.076 28.131 1.00 28.12 ? 621 GLU A CA 1 ATOM 4782 C C . GLU A 1 580 ? 23.672 81.621 29.424 1.00 27.25 ? 621 GLU A C 1 ATOM 4783 O O . GLU A 1 580 ? 22.541 82.120 29.450 1.00 27.72 ? 621 GLU A O 1 ATOM 4784 C CB . GLU A 1 580 ? 23.903 79.594 27.952 1.00 29.49 ? 621 GLU A CB 1 ATOM 4785 C CG . GLU A 1 580 ? 24.169 79.059 26.523 1.00 33.60 ? 621 GLU A CG 1 ATOM 4786 C CD . GLU A 1 580 ? 25.630 78.897 26.160 1.00 39.19 ? 621 GLU A CD 1 ATOM 4787 O OE1 . GLU A 1 580 ? 26.495 78.667 27.034 1.00 40.55 ? 621 GLU A OE1 1 ATOM 4788 O OE2 . GLU A 1 580 ? 25.930 79.012 24.958 1.00 46.82 ? 621 GLU A OE2 1 ATOM 4789 N N . MET A 1 581 ? 24.398 81.465 30.528 1.00 26.25 ? 622 MET A N 1 ATOM 4790 C CA . MET A 1 581 ? 23.880 81.995 31.792 1.00 25.95 ? 622 MET A CA 1 ATOM 4791 C C . MET A 1 581 ? 23.757 83.527 31.711 1.00 27.09 ? 622 MET A C 1 ATOM 4792 O O . MET A 1 581 ? 22.831 84.082 32.285 1.00 26.84 ? 622 MET A O 1 ATOM 4793 C CB . MET A 1 581 ? 24.735 81.561 32.975 1.00 26.14 ? 622 MET A CB 1 ATOM 4794 C CG . MET A 1 581 ? 24.649 80.064 33.245 1.00 26.28 ? 622 MET A CG 1 ATOM 4795 S SD . MET A 1 581 ? 25.606 79.623 34.728 1.00 28.42 ? 622 MET A SD 1 ATOM 4796 C CE . MET A 1 581 ? 24.732 80.469 36.086 1.00 26.04 ? 622 MET A CE 1 ATOM 4797 N N . LYS A 1 582 ? 24.677 84.178 30.981 1.00 28.18 ? 623 LYS A N 1 ATOM 4798 C CA . LYS A 1 582 ? 24.609 85.635 30.753 1.00 29.93 ? 623 LYS A CA 1 ATOM 4799 C C . LYS A 1 582 ? 23.407 85.974 29.860 1.00 30.60 ? 623 LYS A C 1 ATOM 4800 O O . LYS A 1 582 ? 22.566 86.841 30.210 1.00 30.45 ? 623 LYS A O 1 ATOM 4801 C CB . LYS A 1 582 ? 25.914 86.160 30.112 1.00 31.20 ? 623 LYS A CB 1 ATOM 4802 C CG . LYS A 1 582 ? 27.083 86.039 31.033 1.00 30.63 ? 623 LYS A CG 1 ATOM 4803 C CD . LYS A 1 582 ? 28.371 86.549 30.406 1.00 36.97 ? 623 LYS A CD 1 ATOM 4804 C CE . LYS A 1 582 ? 29.435 86.238 31.421 1.00 41.72 ? 623 LYS A CE 1 ATOM 4805 N NZ . LYS A 1 582 ? 30.774 86.152 30.849 1.00 48.32 ? 623 LYS A NZ 1 ATOM 4806 N N . THR A 1 583 ? 23.312 85.256 28.739 1.00 30.38 ? 624 THR A N 1 ATOM 4807 C CA . THR A 1 583 ? 22.297 85.511 27.715 1.00 32.53 ? 624 THR A CA 1 ATOM 4808 C C . THR A 1 583 ? 20.888 85.355 28.246 1.00 31.04 ? 624 THR A C 1 ATOM 4809 O O . THR A 1 583 ? 20.006 86.201 27.997 1.00 31.32 ? 624 THR A O 1 ATOM 4810 C CB . THR A 1 583 ? 22.516 84.569 26.499 1.00 33.18 ? 624 THR A CB 1 ATOM 4811 O OG1 . THR A 1 583 ? 23.733 84.944 25.853 1.00 36.62 ? 624 THR A OG1 1 ATOM 4812 C CG2 . THR A 1 583 ? 21.356 84.688 25.485 1.00 37.04 ? 624 THR A CG2 1 ATOM 4813 N N . TYR A 1 584 ? 20.677 84.275 28.999 1.00 29.38 ? 625 TYR A N 1 ATOM 4814 C CA . TYR A 1 584 ? 19.349 83.958 29.524 1.00 28.14 ? 625 TYR A CA 1 ATOM 4815 C C . TYR A 1 584 ? 19.125 84.376 30.982 1.00 27.46 ? 625 TYR A C 1 ATOM 4816 O O . TYR A 1 584 ? 18.092 84.029 31.549 1.00 27.70 ? 625 TYR A O 1 ATOM 4817 C CB . TYR A 1 584 ? 18.996 82.477 29.289 1.00 28.10 ? 625 TYR A CB 1 ATOM 4818 C CG . TYR A 1 584 ? 19.118 82.136 27.829 1.00 29.54 ? 625 TYR A CG 1 ATOM 4819 C CD1 . TYR A 1 584 ? 18.235 82.679 26.904 1.00 33.13 ? 625 TYR A CD1 1 ATOM 4820 C CD2 . TYR A 1 584 ? 20.139 81.315 27.369 1.00 32.81 ? 625 TYR A CD2 1 ATOM 4821 C CE1 . TYR A 1 584 ? 18.381 82.416 25.531 1.00 35.30 ? 625 TYR A CE1 1 ATOM 4822 C CE2 . TYR A 1 584 ? 20.284 81.024 26.013 1.00 35.50 ? 625 TYR A CE2 1 ATOM 4823 C CZ . TYR A 1 584 ? 19.385 81.574 25.104 1.00 37.91 ? 625 TYR A CZ 1 ATOM 4824 O OH . TYR A 1 584 ? 19.537 81.325 23.761 1.00 41.01 ? 625 TYR A OH 1 ATOM 4825 N N . SER A 1 585 ? 20.072 85.141 31.554 1.00 27.05 ? 626 SER A N 1 ATOM 4826 C CA . SER A 1 585 ? 19.945 85.660 32.923 1.00 27.29 ? 626 SER A CA 1 ATOM 4827 C C . SER A 1 585 ? 19.643 84.520 33.925 1.00 26.05 ? 626 SER A C 1 ATOM 4828 O O . SER A 1 585 ? 18.663 84.546 34.706 1.00 26.95 ? 626 SER A O 1 ATOM 4829 C CB A SER A 1 585 ? 18.857 86.748 32.980 0.65 27.36 ? 626 SER A CB 1 ATOM 4830 C CB B SER A 1 585 ? 18.856 86.729 33.000 0.35 27.76 ? 626 SER A CB 1 ATOM 4831 O OG A SER A 1 585 ? 19.228 87.858 32.172 0.65 27.07 ? 626 SER A OG 1 ATOM 4832 O OG B SER A 1 585 ? 18.768 87.209 34.321 0.35 31.16 ? 626 SER A OG 1 ATOM 4833 N N . VAL A 1 586 ? 20.472 83.486 33.879 1.00 25.28 ? 627 VAL A N 1 ATOM 4834 C CA . VAL A 1 586 ? 20.253 82.287 34.703 1.00 24.67 ? 627 VAL A CA 1 ATOM 4835 C C . VAL A 1 586 ? 20.950 82.518 36.044 1.00 25.85 ? 627 VAL A C 1 ATOM 4836 O O . VAL A 1 586 ? 22.194 82.600 36.106 1.00 27.96 ? 627 VAL A O 1 ATOM 4837 C CB . VAL A 1 586 ? 20.837 81.039 34.011 1.00 24.49 ? 627 VAL A CB 1 ATOM 4838 C CG1 . VAL A 1 586 ? 20.593 79.760 34.863 1.00 23.90 ? 627 VAL A CG1 1 ATOM 4839 C CG2 . VAL A 1 586 ? 20.286 80.915 32.586 1.00 25.28 ? 627 VAL A CG2 1 ATOM 4840 N N . SER A 1 587 ? 20.158 82.747 37.076 1.00 26.63 ? 628 SER A N 1 ATOM 4841 C CA . SER A 1 587 ? 20.706 83.034 38.420 1.00 26.77 ? 628 SER A CA 1 ATOM 4842 C C . SER A 1 587 ? 20.350 81.928 39.393 1.00 24.87 ? 628 SER A C 1 ATOM 4843 O O . SER A 1 587 ? 19.183 81.456 39.437 1.00 24.70 ? 628 SER A O 1 ATOM 4844 C CB . SER A 1 587 ? 20.121 84.316 38.973 1.00 29.02 ? 628 SER A CB 1 ATOM 4845 O OG . SER A 1 587 ? 20.726 84.570 40.227 1.00 33.58 ? 628 SER A OG 1 ATOM 4846 N N . PHE A 1 588 ? 21.338 81.528 40.186 1.00 25.07 ? 629 PHE A N 1 ATOM 4847 C CA . PHE A 1 588 ? 21.083 80.569 41.266 1.00 23.96 ? 629 PHE A CA 1 ATOM 4848 C C . PHE A 1 588 ? 20.875 81.311 42.600 1.00 23.72 ? 629 PHE A C 1 ATOM 4849 O O . PHE A 1 588 ? 20.747 80.673 43.650 1.00 22.84 ? 629 PHE A O 1 ATOM 4850 C CB . PHE A 1 588 ? 22.247 79.549 41.365 1.00 23.47 ? 629 PHE A CB 1 ATOM 4851 C CG . PHE A 1 588 ? 22.181 78.489 40.324 1.00 23.04 ? 629 PHE A CG 1 ATOM 4852 C CD1 . PHE A 1 588 ? 21.653 77.241 40.621 1.00 23.09 ? 629 PHE A CD1 1 ATOM 4853 C CD2 . PHE A 1 588 ? 22.642 78.748 39.014 1.00 25.52 ? 629 PHE A CD2 1 ATOM 4854 C CE1 . PHE A 1 588 ? 21.569 76.245 39.639 1.00 23.86 ? 629 PHE A CE1 1 ATOM 4855 C CE2 . PHE A 1 588 ? 22.567 77.769 38.047 1.00 24.52 ? 629 PHE A CE2 1 ATOM 4856 C CZ . PHE A 1 588 ? 22.015 76.512 38.371 1.00 24.01 ? 629 PHE A CZ 1 ATOM 4857 N N . ASP A 1 589 ? 20.808 82.642 42.549 1.00 24.80 ? 630 ASP A N 1 ATOM 4858 C CA . ASP A 1 589 ? 20.679 83.447 43.797 1.00 25.86 ? 630 ASP A CA 1 ATOM 4859 C C . ASP A 1 589 ? 19.502 82.989 44.683 1.00 24.01 ? 630 ASP A C 1 ATOM 4860 O O . ASP A 1 589 ? 19.648 82.908 45.939 1.00 24.02 ? 630 ASP A O 1 ATOM 4861 C CB . ASP A 1 589 ? 20.600 84.959 43.490 1.00 27.41 ? 630 ASP A CB 1 ATOM 4862 C CG . ASP A 1 589 ? 21.950 85.559 43.030 1.00 33.91 ? 630 ASP A CG 1 ATOM 4863 O OD1 . ASP A 1 589 ? 22.983 84.851 42.951 1.00 35.69 ? 630 ASP A OD1 1 ATOM 4864 O OD2 . ASP A 1 589 ? 21.943 86.777 42.732 1.00 38.28 ? 630 ASP A OD2 1 ATOM 4865 N N . SER A 1 590 ? 18.352 82.666 44.076 1.00 23.03 ? 631 SER A N 1 ATOM 4866 C CA . SER A 1 590 ? 17.217 82.251 44.905 1.00 21.27 ? 631 SER A CA 1 ATOM 4867 C C . SER A 1 590 ? 17.477 80.950 45.625 1.00 20.59 ? 631 SER A C 1 ATOM 4868 O O . SER A 1 590 ? 17.032 80.780 46.765 1.00 20.03 ? 631 SER A O 1 ATOM 4869 C CB . SER A 1 590 ? 15.891 82.147 44.116 1.00 22.36 ? 631 SER A CB 1 ATOM 4870 O OG . SER A 1 590 ? 16.070 81.189 43.048 1.00 24.68 ? 631 SER A OG 1 ATOM 4871 N N . LEU A 1 591 ? 18.172 80.021 44.971 1.00 20.55 ? 632 LEU A N 1 ATOM 4872 C CA . LEU A 1 591 ? 18.396 78.735 45.588 1.00 20.07 ? 632 LEU A CA 1 ATOM 4873 C C . LEU A 1 591 ? 19.413 78.878 46.743 1.00 20.94 ? 632 LEU A C 1 ATOM 4874 O O . LEU A 1 591 ? 19.200 78.326 47.811 1.00 19.75 ? 632 LEU A O 1 ATOM 4875 C CB . LEU A 1 591 ? 18.899 77.725 44.544 1.00 21.20 ? 632 LEU A CB 1 ATOM 4876 C CG . LEU A 1 591 ? 19.246 76.343 45.121 1.00 21.04 ? 632 LEU A CG 1 ATOM 4877 C CD1 . LEU A 1 591 ? 18.006 75.668 45.712 1.00 19.78 ? 632 LEU A CD1 1 ATOM 4878 C CD2 . LEU A 1 591 ? 19.741 75.504 43.971 1.00 21.55 ? 632 LEU A CD2 1 ATOM 4879 N N . PHE A 1 592 ? 20.466 79.665 46.550 1.00 20.77 ? 633 PHE A N 1 ATOM 4880 C CA . PHE A 1 592 ? 21.405 79.868 47.651 1.00 22.31 ? 633 PHE A CA 1 ATOM 4881 C C . PHE A 1 592 ? 20.736 80.613 48.815 1.00 22.56 ? 633 PHE A C 1 ATOM 4882 O O . PHE A 1 592 ? 21.015 80.310 50.002 1.00 24.37 ? 633 PHE A O 1 ATOM 4883 C CB . PHE A 1 592 ? 22.642 80.607 47.132 1.00 23.19 ? 633 PHE A CB 1 ATOM 4884 C CG . PHE A 1 592 ? 23.587 79.691 46.408 1.00 24.74 ? 633 PHE A CG 1 ATOM 4885 C CD1 . PHE A 1 592 ? 24.349 78.763 47.126 1.00 25.43 ? 633 PHE A CD1 1 ATOM 4886 C CD2 . PHE A 1 592 ? 23.708 79.724 45.032 1.00 29.05 ? 633 PHE A CD2 1 ATOM 4887 C CE1 . PHE A 1 592 ? 25.202 77.855 46.458 1.00 26.37 ? 633 PHE A CE1 1 ATOM 4888 C CE2 . PHE A 1 592 ? 24.583 78.834 44.365 1.00 29.20 ? 633 PHE A CE2 1 ATOM 4889 C CZ . PHE A 1 592 ? 25.311 77.894 45.097 1.00 27.30 ? 633 PHE A CZ 1 ATOM 4890 N N . SER A 1 593 ? 19.835 81.555 48.490 1.00 21.70 ? 634 SER A N 1 ATOM 4891 C CA . SER A 1 593 ? 19.064 82.258 49.541 1.00 23.12 ? 634 SER A CA 1 ATOM 4892 C C . SER A 1 593 ? 18.214 81.295 50.354 1.00 21.96 ? 634 SER A C 1 ATOM 4893 O O . SER A 1 593 ? 18.169 81.356 51.605 1.00 21.77 ? 634 SER A O 1 ATOM 4894 C CB . SER A 1 593 ? 18.191 83.352 48.923 1.00 23.81 ? 634 SER A CB 1 ATOM 4895 O OG . SER A 1 593 ? 17.379 83.997 49.909 1.00 25.55 ? 634 SER A OG 1 ATOM 4896 N N . ALA A 1 594 ? 17.506 80.403 49.652 1.00 19.95 ? 635 ALA A N 1 ATOM 4897 C CA . ALA A 1 594 ? 16.706 79.402 50.337 1.00 19.30 ? 635 ALA A CA 1 ATOM 4898 C C . ALA A 1 594 ? 17.543 78.490 51.244 1.00 19.93 ? 635 ALA A C 1 ATOM 4899 O O . ALA A 1 594 ? 17.156 78.216 52.389 1.00 21.07 ? 635 ALA A O 1 ATOM 4900 C CB . ALA A 1 594 ? 15.864 78.597 49.333 1.00 19.48 ? 635 ALA A CB 1 ATOM 4901 N N . VAL A 1 595 ? 18.705 78.075 50.751 1.00 19.77 ? 636 VAL A N 1 ATOM 4902 C CA . VAL A 1 595 ? 19.596 77.198 51.527 1.00 19.97 ? 636 VAL A CA 1 ATOM 4903 C C . VAL A 1 595 ? 20.109 77.953 52.774 1.00 21.46 ? 636 VAL A C 1 ATOM 4904 O O . VAL A 1 595 ? 20.162 77.380 53.881 1.00 21.27 ? 636 VAL A O 1 ATOM 4905 C CB . VAL A 1 595 ? 20.729 76.707 50.634 1.00 20.65 ? 636 VAL A CB 1 ATOM 4906 C CG1 . VAL A 1 595 ? 21.767 75.966 51.462 1.00 22.91 ? 636 VAL A CG1 1 ATOM 4907 C CG2 . VAL A 1 595 ? 20.147 75.732 49.556 1.00 20.72 ? 636 VAL A CG2 1 ATOM 4908 N N . LYS A 1 596 ? 20.465 79.228 52.602 1.00 22.48 ? 637 LYS A N 1 ATOM 4909 C CA . LYS A 1 596 ? 20.904 80.066 53.731 1.00 23.48 ? 637 LYS A CA 1 ATOM 4910 C C . LYS A 1 596 ? 19.791 80.181 54.780 1.00 23.08 ? 637 LYS A C 1 ATOM 4911 O O . LYS A 1 596 ? 20.025 79.978 55.989 1.00 22.83 ? 637 LYS A O 1 ATOM 4912 C CB . LYS A 1 596 ? 21.288 81.458 53.214 1.00 24.76 ? 637 LYS A CB 1 ATOM 4913 C CG . LYS A 1 596 ? 21.566 82.504 54.334 1.00 30.58 ? 637 LYS A CG 1 ATOM 4914 C CD . LYS A 1 596 ? 22.154 83.780 53.732 1.00 36.20 ? 637 LYS A CD 1 ATOM 4915 C CE . LYS A 1 596 ? 22.497 84.823 54.830 1.00 40.05 ? 637 LYS A CE 1 ATOM 4916 N NZ . LYS A 1 596 ? 21.219 85.374 55.412 1.00 44.65 ? 637 LYS A NZ 1 ATOM 4917 N N . ASN A 1 597 ? 18.553 80.400 54.312 1.00 21.11 ? 638 ASN A N 1 ATOM 4918 C CA . ASN A 1 597 ? 17.429 80.485 55.211 1.00 22.37 ? 638 ASN A CA 1 ATOM 4919 C C . ASN A 1 597 ? 17.171 79.159 55.937 1.00 22.12 ? 638 ASN A C 1 ATOM 4920 O O . ASN A 1 597 ? 16.944 79.142 57.162 1.00 23.45 ? 638 ASN A O 1 ATOM 4921 C CB . ASN A 1 597 ? 16.171 80.924 54.457 1.00 20.72 ? 638 ASN A CB 1 ATOM 4922 C CG . ASN A 1 597 ? 16.207 82.360 54.036 1.00 23.09 ? 638 ASN A CG 1 ATOM 4923 O OD1 . ASN A 1 597 ? 17.101 83.161 54.439 1.00 24.82 ? 638 ASN A OD1 1 ATOM 4924 N ND2 . ASN A 1 597 ? 15.230 82.729 53.200 1.00 23.21 ? 638 ASN A ND2 1 ATOM 4925 N N . PHE A 1 598 ? 17.271 78.040 55.218 1.00 20.11 ? 639 PHE A N 1 ATOM 4926 C CA . PHE A 1 598 ? 17.061 76.737 55.823 1.00 19.85 ? 639 PHE A CA 1 ATOM 4927 C C . PHE A 1 598 ? 18.099 76.520 56.941 1.00 21.11 ? 639 PHE A C 1 ATOM 4928 O O . PHE A 1 598 ? 17.766 76.040 58.044 1.00 21.68 ? 639 PHE A O 1 ATOM 4929 C CB . PHE A 1 598 ? 17.180 75.629 54.753 1.00 19.10 ? 639 PHE A CB 1 ATOM 4930 C CG . PHE A 1 598 ? 16.796 74.274 55.245 1.00 19.18 ? 639 PHE A CG 1 ATOM 4931 C CD1 . PHE A 1 598 ? 15.593 73.705 54.835 1.00 20.31 ? 639 PHE A CD1 1 ATOM 4932 C CD2 . PHE A 1 598 ? 17.651 73.530 56.064 1.00 19.91 ? 639 PHE A CD2 1 ATOM 4933 C CE1 . PHE A 1 598 ? 15.237 72.439 55.294 1.00 22.82 ? 639 PHE A CE1 1 ATOM 4934 C CE2 . PHE A 1 598 ? 17.303 72.296 56.499 1.00 21.12 ? 639 PHE A CE2 1 ATOM 4935 C CZ . PHE A 1 598 ? 16.080 71.733 56.145 1.00 22.76 ? 639 PHE A CZ 1 ATOM 4936 N N . THR A 1 599 ? 19.332 76.916 56.660 1.00 21.20 ? 640 THR A N 1 ATOM 4937 C CA . THR A 1 599 ? 20.447 76.757 57.626 1.00 23.57 ? 640 THR A CA 1 ATOM 4938 C C . THR A 1 599 ? 20.142 77.554 58.896 1.00 24.83 ? 640 THR A C 1 ATOM 4939 O O . THR A 1 599 ? 20.285 77.013 60.020 1.00 24.55 ? 640 THR A O 1 ATOM 4940 C CB . THR A 1 599 ? 21.764 77.200 56.983 1.00 23.20 ? 640 THR A CB 1 ATOM 4941 O OG1 . THR A 1 599 ? 21.980 76.458 55.769 1.00 23.67 ? 640 THR A OG1 1 ATOM 4942 C CG2 . THR A 1 599 ? 22.981 76.933 57.929 1.00 26.77 ? 640 THR A CG2 1 ATOM 4943 N N . GLU A 1 600 ? 19.712 78.812 58.732 1.00 23.97 ? 641 GLU A N 1 ATOM 4944 C CA A GLU A 1 600 ? 19.450 79.670 59.883 0.50 25.59 ? 641 GLU A CA 1 ATOM 4945 C CA B GLU A 1 600 ? 19.419 79.695 59.889 0.50 26.25 ? 641 GLU A CA 1 ATOM 4946 C C . GLU A 1 600 ? 18.255 79.131 60.686 1.00 25.31 ? 641 GLU A C 1 ATOM 4947 O O . GLU A 1 600 ? 18.308 79.046 61.915 1.00 25.56 ? 641 GLU A O 1 ATOM 4948 C CB A GLU A 1 600 ? 19.264 81.131 59.425 0.50 26.03 ? 641 GLU A CB 1 ATOM 4949 C CB B GLU A 1 600 ? 19.115 81.160 59.471 0.50 26.93 ? 641 GLU A CB 1 ATOM 4950 C CG A GLU A 1 600 ? 20.575 81.766 58.951 0.50 29.06 ? 641 GLU A CG 1 ATOM 4951 C CG B GLU A 1 600 ? 17.628 81.489 59.137 0.50 32.39 ? 641 GLU A CG 1 ATOM 4952 C CD A GLU A 1 600 ? 20.427 83.173 58.365 0.50 32.80 ? 641 GLU A CD 1 ATOM 4953 C CD B GLU A 1 600 ? 16.822 82.235 60.262 0.50 36.39 ? 641 GLU A CD 1 ATOM 4954 O OE1 A GLU A 1 600 ? 21.418 83.686 57.810 0.50 35.61 ? 641 GLU A OE1 1 ATOM 4955 O OE1 B GLU A 1 600 ? 15.982 83.117 59.918 0.50 36.49 ? 641 GLU A OE1 1 ATOM 4956 O OE2 A GLU A 1 600 ? 19.339 83.772 58.470 0.50 34.97 ? 641 GLU A OE2 1 ATOM 4957 O OE2 B GLU A 1 600 ? 17.007 81.932 61.471 0.50 39.96 ? 641 GLU A OE2 1 ATOM 4958 N N . ILE A 1 601 ? 17.184 78.737 59.991 1.00 23.45 ? 642 ILE A N 1 ATOM 4959 C CA . ILE A 1 601 ? 15.970 78.309 60.659 1.00 23.52 ? 642 ILE A CA 1 ATOM 4960 C C . ILE A 1 601 ? 16.217 76.976 61.339 1.00 23.63 ? 642 ILE A C 1 ATOM 4961 O O . ILE A 1 601 ? 15.755 76.742 62.452 1.00 24.52 ? 642 ILE A O 1 ATOM 4962 C CB . ILE A 1 601 ? 14.752 78.248 59.680 1.00 23.00 ? 642 ILE A CB 1 ATOM 4963 C CG1 . ILE A 1 601 ? 14.392 79.677 59.284 1.00 21.63 ? 642 ILE A CG1 1 ATOM 4964 C CG2 . ILE A 1 601 ? 13.535 77.588 60.334 1.00 26.44 ? 642 ILE A CG2 1 ATOM 4965 C CD1 . ILE A 1 601 ? 13.432 79.710 58.063 1.00 23.87 ? 642 ILE A CD1 1 ATOM 4966 N N . ALA A 1 602 ? 16.953 76.096 60.667 1.00 23.36 ? 643 ALA A N 1 ATOM 4967 C CA . ALA A 1 602 ? 17.279 74.786 61.258 1.00 23.60 ? 643 ALA A CA 1 ATOM 4968 C C . ALA A 1 602 ? 18.097 74.976 62.539 1.00 25.09 ? 643 ALA A C 1 ATOM 4969 O O . ALA A 1 602 ? 17.879 74.259 63.523 1.00 25.24 ? 643 ALA A O 1 ATOM 4970 C CB . ALA A 1 602 ? 18.061 73.906 60.269 1.00 24.44 ? 643 ALA A CB 1 ATOM 4971 N N . SER A 1 603 ? 19.041 75.912 62.520 1.00 25.15 ? 644 SER A N 1 ATOM 4972 C CA A SER A 1 603 ? 19.845 76.182 63.730 0.50 26.24 ? 644 SER A CA 1 ATOM 4973 C CA B SER A 1 603 ? 19.840 76.188 63.722 0.50 26.85 ? 644 SER A CA 1 ATOM 4974 C C . SER A 1 603 ? 18.964 76.632 64.890 1.00 27.19 ? 644 SER A C 1 ATOM 4975 O O . SER A 1 603 ? 19.156 76.173 66.043 1.00 28.32 ? 644 SER A O 1 ATOM 4976 C CB A SER A 1 603 ? 20.923 77.227 63.465 0.50 27.28 ? 644 SER A CB 1 ATOM 4977 C CB B SER A 1 603 ? 20.897 77.233 63.405 0.50 27.86 ? 644 SER A CB 1 ATOM 4978 O OG A SER A 1 603 ? 21.756 77.373 64.615 0.50 29.00 ? 644 SER A OG 1 ATOM 4979 O OG B SER A 1 603 ? 21.996 76.610 62.769 0.50 32.42 ? 644 SER A OG 1 ATOM 4980 N N . LYS A 1 604 ? 18.019 77.515 64.608 1.00 26.50 ? 645 LYS A N 1 ATOM 4981 C CA . LYS A 1 604 ? 17.116 78.010 65.653 1.00 27.57 ? 645 LYS A CA 1 ATOM 4982 C C . LYS A 1 604 ? 16.173 76.909 66.144 1.00 26.29 ? 645 LYS A C 1 ATOM 4983 O O . LYS A 1 604 ? 15.941 76.767 67.330 1.00 26.80 ? 645 LYS A O 1 ATOM 4984 C CB . LYS A 1 604 ? 16.371 79.263 65.185 1.00 28.69 ? 645 LYS A CB 1 ATOM 4985 C CG A LYS A 1 604 ? 17.312 80.437 64.863 0.50 31.95 ? 645 LYS A CG 1 ATOM 4986 C CG B LYS A 1 604 ? 17.252 80.531 65.085 0.50 31.06 ? 645 LYS A CG 1 ATOM 4987 C CD A LYS A 1 604 ? 16.549 81.695 64.542 0.50 36.26 ? 645 LYS A CD 1 ATOM 4988 C CD B LYS A 1 604 ? 17.768 80.959 66.451 0.50 34.54 ? 645 LYS A CD 1 ATOM 4989 C CE A LYS A 1 604 ? 17.435 82.957 64.623 0.50 41.25 ? 645 LYS A CE 1 ATOM 4990 C CE B LYS A 1 604 ? 18.819 82.070 66.361 0.50 38.36 ? 645 LYS A CE 1 ATOM 4991 N NZ A LYS A 1 604 ? 17.610 83.600 63.274 0.50 42.17 ? 645 LYS A NZ 1 ATOM 4992 N NZ B LYS A 1 604 ? 19.377 82.390 67.709 0.50 42.29 ? 645 LYS A NZ 1 ATOM 4993 N N . PHE A 1 605 ? 15.659 76.085 65.222 1.00 23.91 ? 646 PHE A N 1 ATOM 4994 C CA . PHE A 1 605 ? 14.852 74.949 65.633 1.00 24.24 ? 646 PHE A CA 1 ATOM 4995 C C . PHE A 1 605 ? 15.609 73.980 66.547 1.00 24.92 ? 646 PHE A C 1 ATOM 4996 O O . PHE A 1 605 ? 15.063 73.518 67.572 1.00 26.71 ? 646 PHE A O 1 ATOM 4997 C CB . PHE A 1 605 ? 14.361 74.184 64.380 1.00 23.76 ? 646 PHE A CB 1 ATOM 4998 C CG . PHE A 1 605 ? 13.530 72.984 64.703 1.00 23.74 ? 646 PHE A CG 1 ATOM 4999 C CD1 . PHE A 1 605 ? 12.149 73.108 64.902 1.00 24.15 ? 646 PHE A CD1 1 ATOM 5000 C CD2 . PHE A 1 605 ? 14.127 71.728 64.810 1.00 25.90 ? 646 PHE A CD2 1 ATOM 5001 C CE1 . PHE A 1 605 ? 11.374 71.995 65.206 1.00 25.56 ? 646 PHE A CE1 1 ATOM 5002 C CE2 . PHE A 1 605 ? 13.359 70.605 65.129 1.00 27.87 ? 646 PHE A CE2 1 ATOM 5003 C CZ . PHE A 1 605 ? 11.986 70.734 65.310 1.00 24.47 ? 646 PHE A CZ 1 ATOM 5004 N N . SER A 1 606 ? 16.861 73.685 66.205 1.00 24.89 ? 647 SER A N 1 ATOM 5005 C CA . SER A 1 606 ? 17.674 72.801 67.030 1.00 26.91 ? 647 SER A CA 1 ATOM 5006 C C . SER A 1 606 ? 17.855 73.360 68.453 1.00 28.60 ? 647 SER A C 1 ATOM 5007 O O . SER A 1 606 ? 17.851 72.582 69.401 1.00 28.98 ? 647 SER A O 1 ATOM 5008 C CB . SER A 1 606 ? 19.044 72.632 66.419 1.00 27.12 ? 647 SER A CB 1 ATOM 5009 O OG A SER A 1 606 ? 18.919 72.090 65.124 0.50 26.99 ? 647 SER A OG 1 ATOM 5010 O OG B SER A 1 606 ? 19.721 71.528 67.005 0.50 29.28 ? 647 SER A OG 1 ATOM 5011 N N . GLU A 1 607 ? 18.035 74.673 68.558 1.00 28.79 ? 648 GLU A N 1 ATOM 5012 C CA A GLU A 1 607 ? 18.149 75.336 69.864 0.50 30.77 ? 648 GLU A CA 1 ATOM 5013 C CA B GLU A 1 607 ? 18.159 75.325 69.864 0.50 30.54 ? 648 GLU A CA 1 ATOM 5014 C C . GLU A 1 607 ? 16.864 75.115 70.658 1.00 30.93 ? 648 GLU A C 1 ATOM 5015 O O . GLU A 1 607 ? 16.901 74.740 71.851 1.00 31.63 ? 648 GLU A O 1 ATOM 5016 C CB A GLU A 1 607 ? 18.421 76.832 69.694 0.50 31.90 ? 648 GLU A CB 1 ATOM 5017 C CB B GLU A 1 607 ? 18.502 76.814 69.706 0.50 31.66 ? 648 GLU A CB 1 ATOM 5018 C CG A GLU A 1 607 ? 19.770 77.165 69.081 0.50 34.39 ? 648 GLU A CG 1 ATOM 5019 C CG B GLU A 1 607 ? 18.713 77.526 71.034 0.50 33.57 ? 648 GLU A CG 1 ATOM 5020 C CD A GLU A 1 607 ? 20.016 78.672 68.987 0.50 38.23 ? 648 GLU A CD 1 ATOM 5021 C CD B GLU A 1 607 ? 19.237 78.954 70.924 0.50 38.79 ? 648 GLU A CD 1 ATOM 5022 O OE1 A GLU A 1 607 ? 19.054 79.451 68.848 0.50 40.76 ? 648 GLU A OE1 1 ATOM 5023 O OE1 B GLU A 1 607 ? 19.088 79.600 69.858 0.50 40.81 ? 648 GLU A OE1 1 ATOM 5024 O OE2 A GLU A 1 607 ? 21.187 79.086 69.069 0.50 44.10 ? 648 GLU A OE2 1 ATOM 5025 O OE2 B GLU A 1 607 ? 19.790 79.440 71.943 0.50 40.29 ? 648 GLU A OE2 1 ATOM 5026 N N . ARG A 1 608 ? 15.705 75.318 70.010 1.00 28.72 ? 649 ARG A N 1 ATOM 5027 C CA . ARG A 1 608 ? 14.456 75.129 70.731 1.00 29.34 ? 649 ARG A CA 1 ATOM 5028 C C . ARG A 1 608 ? 14.285 73.682 71.125 1.00 29.70 ? 649 ARG A C 1 ATOM 5029 O O . ARG A 1 608 ? 13.714 73.408 72.150 1.00 30.87 ? 649 ARG A O 1 ATOM 5030 C CB . ARG A 1 608 ? 13.236 75.580 69.913 1.00 28.48 ? 649 ARG A CB 1 ATOM 5031 C CG . ARG A 1 608 ? 13.226 77.061 69.618 1.00 30.33 ? 649 ARG A CG 1 ATOM 5032 C CD . ARG A 1 608 ? 11.823 77.578 69.201 1.00 29.41 ? 649 ARG A CD 1 ATOM 5033 N NE . ARG A 1 608 ? 11.274 76.825 68.052 1.00 27.36 ? 649 ARG A NE 1 ATOM 5034 C CZ . ARG A 1 608 ? 11.620 77.043 66.781 1.00 28.68 ? 649 ARG A CZ 1 ATOM 5035 N NH1 . ARG A 1 608 ? 12.553 77.957 66.501 1.00 27.89 ? 649 ARG A NH1 1 ATOM 5036 N NH2 . ARG A 1 608 ? 11.049 76.335 65.793 1.00 27.04 ? 649 ARG A NH2 1 ATOM 5037 N N . LEU A 1 609 ? 14.750 72.745 70.292 1.00 29.34 ? 650 LEU A N 1 ATOM 5038 C CA . LEU A 1 609 ? 14.539 71.342 70.540 1.00 31.36 ? 650 LEU A CA 1 ATOM 5039 C C . LEU A 1 609 ? 15.351 70.900 71.757 1.00 34.72 ? 650 LEU A C 1 ATOM 5040 O O . LEU A 1 609 ? 14.942 69.997 72.484 1.00 34.61 ? 650 LEU A O 1 ATOM 5041 C CB . LEU A 1 609 ? 14.982 70.519 69.297 1.00 32.41 ? 650 LEU A CB 1 ATOM 5042 C CG . LEU A 1 609 ? 14.526 69.071 69.155 1.00 32.84 ? 650 LEU A CG 1 ATOM 5043 C CD1 . LEU A 1 609 ? 13.033 68.931 68.978 1.00 30.84 ? 650 LEU A CD1 1 ATOM 5044 C CD2 . LEU A 1 609 ? 15.324 68.396 67.989 1.00 33.29 ? 650 LEU A CD2 1 ATOM 5045 N N . GLN A 1 610 ? 16.507 71.516 71.925 1.00 37.09 ? 651 GLN A N 1 ATOM 5046 C CA A GLN A 1 610 ? 17.383 71.124 73.019 0.50 40.47 ? 651 GLN A CA 1 ATOM 5047 C CA B GLN A 1 610 ? 17.419 71.166 73.014 0.50 40.45 ? 651 GLN A CA 1 ATOM 5048 C C . GLN A 1 610 ? 16.913 71.785 74.308 1.00 41.61 ? 651 GLN A C 1 ATOM 5049 O O . GLN A 1 610 ? 17.119 71.212 75.384 1.00 43.72 ? 651 GLN A O 1 ATOM 5050 C CB A GLN A 1 610 ? 18.861 71.419 72.714 0.50 40.70 ? 651 GLN A CB 1 ATOM 5051 C CB B GLN A 1 610 ? 18.857 71.629 72.711 0.50 40.92 ? 651 GLN A CB 1 ATOM 5052 C CG A GLN A 1 610 ? 19.480 70.500 71.667 0.50 42.58 ? 651 GLN A CG 1 ATOM 5053 C CG B GLN A 1 610 ? 19.130 73.099 73.036 0.50 43.37 ? 651 GLN A CG 1 ATOM 5054 C CD A GLN A 1 610 ? 20.998 70.616 71.612 0.50 43.73 ? 651 GLN A CD 1 ATOM 5055 C CD B GLN A 1 610 ? 20.410 73.625 72.402 0.50 47.97 ? 651 GLN A CD 1 ATOM 5056 O OE1 A GLN A 1 610 ? 21.654 70.842 72.631 0.50 48.36 ? 651 GLN A OE1 1 ATOM 5057 O OE1 B GLN A 1 610 ? 21.076 72.917 71.643 0.50 48.28 ? 651 GLN A OE1 1 ATOM 5058 N NE2 A GLN A 1 610 ? 21.561 70.457 70.420 0.50 45.29 ? 651 GLN A NE2 1 ATOM 5059 N NE2 B GLN A 1 610 ? 20.757 74.876 72.712 0.50 49.18 ? 651 GLN A NE2 1 ATOM 5060 N N . ASP A 1 611 ? 16.255 72.952 74.175 1.00 42.95 ? 652 ASP A N 1 ATOM 5061 C CA . ASP A 1 611 ? 15.812 73.887 75.249 1.00 45.59 ? 652 ASP A CA 1 ATOM 5062 C C . ASP A 1 611 ? 14.354 73.821 75.675 1.00 44.58 ? 652 ASP A C 1 ATOM 5063 O O . ASP A 1 611 ? 13.959 74.525 76.599 1.00 46.06 ? 652 ASP A O 1 ATOM 5064 C CB . ASP A 1 611 ? 15.949 75.348 74.777 1.00 46.83 ? 652 ASP A CB 1 ATOM 5065 C CG . ASP A 1 611 ? 17.350 75.935 74.958 1.00 52.53 ? 652 ASP A CG 1 ATOM 5066 O OD1 . ASP A 1 611 ? 18.287 75.225 75.395 1.00 58.05 ? 652 ASP A OD1 1 ATOM 5067 O OD2 . ASP A 1 611 ? 17.488 77.148 74.645 1.00 59.21 ? 652 ASP A OD2 1 ATOM 5068 N N . PHE A 1 612 ? 13.511 73.078 74.975 1.00 43.44 ? 653 PHE A N 1 ATOM 5069 C CA . PHE A 1 612 ? 12.094 73.160 75.315 1.00 42.84 ? 653 PHE A CA 1 ATOM 5070 C C . PHE A 1 612 ? 11.733 72.434 76.593 1.00 44.01 ? 653 PHE A C 1 ATOM 5071 O O . PHE A 1 612 ? 10.750 72.860 77.225 1.00 46.40 ? 653 PHE A O 1 ATOM 5072 C CB . PHE A 1 612 ? 11.184 72.695 74.172 1.00 40.64 ? 653 PHE A CB 1 ATOM 5073 C CG . PHE A 1 612 ? 11.045 71.202 74.048 1.00 38.54 ? 653 PHE A CG 1 ATOM 5074 C CD1 . PHE A 1 612 ? 9.963 70.542 74.616 1.00 34.17 ? 653 PHE A CD1 1 ATOM 5075 C CD2 . PHE A 1 612 ? 11.941 70.485 73.290 1.00 37.20 ? 653 PHE A CD2 1 ATOM 5076 C CE1 . PHE A 1 612 ? 9.781 69.200 74.433 1.00 40.41 ? 653 PHE A CE1 1 ATOM 5077 C CE2 . PHE A 1 612 ? 11.787 69.118 73.100 1.00 40.51 ? 653 PHE A CE2 1 ATOM 5078 C CZ . PHE A 1 612 ? 10.707 68.468 73.658 1.00 41.12 ? 653 PHE A CZ 1 ATOM 5079 N N A SER A 1 615 ? 8.885 69.067 80.071 0.50 27.78 ? 656 SER A N 1 ATOM 5080 N N B SER A 1 615 ? 7.946 66.343 79.239 0.50 26.36 ? 656 SER A N 1 ATOM 5081 C CA A SER A 1 615 ? 7.718 68.399 80.613 0.50 28.79 ? 656 SER A CA 1 ATOM 5082 C CA B SER A 1 615 ? 6.845 65.713 79.964 0.50 26.48 ? 656 SER A CA 1 ATOM 5083 C C A SER A 1 615 ? 6.447 68.486 79.729 0.50 26.91 ? 656 SER A C 1 ATOM 5084 C C B SER A 1 615 ? 5.506 66.424 79.641 0.50 27.58 ? 656 SER A C 1 ATOM 5085 O O A SER A 1 615 ? 5.383 67.952 80.094 0.50 27.70 ? 656 SER A O 1 ATOM 5086 O O B SER A 1 615 ? 4.461 66.173 80.264 0.50 28.81 ? 656 SER A O 1 ATOM 5087 C CB A SER A 1 615 ? 7.405 69.034 81.964 0.50 27.65 ? 656 SER A CB 1 ATOM 5088 C CB B SER A 1 615 ? 7.163 65.724 81.498 0.50 26.54 ? 656 SER A CB 1 ATOM 5089 O OG A SER A 1 615 ? 7.065 70.391 81.810 0.50 29.07 ? 656 SER A OG 1 ATOM 5090 O OG B SER A 1 615 ? 6.923 67.048 81.993 0.50 29.64 ? 656 SER A OG 1 ATOM 5091 N N A ASN A 1 616 ? 6.521 69.207 78.617 0.50 26.20 ? 657 ASN A N 1 ATOM 5092 N N B ASN A 1 616 ? 5.541 67.367 78.716 0.50 27.02 ? 657 ASN A N 1 ATOM 5093 C CA A ASN A 1 616 ? 5.328 69.509 77.821 0.50 25.93 ? 657 ASN A CA 1 ATOM 5094 C CA B ASN A 1 616 ? 4.308 68.003 78.260 0.50 28.86 ? 657 ASN A CA 1 ATOM 5095 C C A ASN A 1 616 ? 5.215 68.586 76.617 0.50 25.22 ? 657 ASN A C 1 ATOM 5096 C C B ASN A 1 616 ? 3.870 67.287 76.973 0.50 27.94 ? 657 ASN A C 1 ATOM 5097 O O A ASN A 1 616 ? 6.016 68.657 75.680 0.50 23.28 ? 657 ASN A O 1 ATOM 5098 O O B ASN A 1 616 ? 4.414 67.528 75.907 0.50 27.19 ? 657 ASN A O 1 ATOM 5099 C CB A ASN A 1 616 ? 5.338 70.968 77.397 0.50 25.97 ? 657 ASN A CB 1 ATOM 5100 C CB B ASN A 1 616 ? 4.578 69.508 78.050 0.50 28.89 ? 657 ASN A CB 1 ATOM 5101 C CG A ASN A 1 616 ? 4.007 71.405 76.799 0.50 25.61 ? 657 ASN A CG 1 ATOM 5102 C CG B ASN A 1 616 ? 3.368 70.279 77.535 0.50 30.85 ? 657 ASN A CG 1 ATOM 5103 O OD1 A ASN A 1 616 ? 3.356 70.638 76.105 0.50 23.34 ? 657 ASN A OD1 1 ATOM 5104 O OD1 B ASN A 1 616 ? 2.579 69.761 76.733 0.50 33.05 ? 657 ASN A OD1 1 ATOM 5105 N ND2 A ASN A 1 616 ? 3.597 72.638 77.084 0.50 29.02 ? 657 ASN A ND2 1 ATOM 5106 N ND2 B ASN A 1 616 ? 3.267 71.545 77.931 0.50 30.50 ? 657 ASN A ND2 1 ATOM 5107 N N A PRO A 1 617 ? 4.248 67.653 76.655 0.50 24.57 ? 658 PRO A N 1 ATOM 5108 N N B PRO A 1 617 ? 2.882 66.376 77.071 0.50 28.45 ? 658 PRO A N 1 ATOM 5109 C CA A PRO A 1 617 ? 4.202 66.637 75.602 0.50 23.75 ? 658 PRO A CA 1 ATOM 5110 C CA B PRO A 1 617 ? 2.544 65.574 75.885 0.50 27.08 ? 658 PRO A CA 1 ATOM 5111 C C A PRO A 1 617 ? 3.669 67.186 74.294 0.50 22.39 ? 658 PRO A C 1 ATOM 5112 C C B PRO A 1 617 ? 2.225 66.337 74.592 0.50 26.14 ? 658 PRO A C 1 ATOM 5113 O O A PRO A 1 617 ? 3.895 66.574 73.248 0.50 21.19 ? 658 PRO A O 1 ATOM 5114 O O B PRO A 1 617 ? 2.641 65.888 73.526 0.50 24.70 ? 658 PRO A O 1 ATOM 5115 C CB A PRO A 1 617 ? 3.189 65.622 76.138 0.50 23.36 ? 658 PRO A CB 1 ATOM 5116 C CB B PRO A 1 617 ? 1.325 64.765 76.344 0.50 27.90 ? 658 PRO A CB 1 ATOM 5117 C CG A PRO A 1 617 ? 2.248 66.491 76.989 0.50 24.85 ? 658 PRO A CG 1 ATOM 5118 C CG B PRO A 1 617 ? 1.463 64.721 77.874 0.50 29.74 ? 658 PRO A CG 1 ATOM 5119 C CD A PRO A 1 617 ? 3.194 67.466 77.673 0.50 26.55 ? 658 PRO A CD 1 ATOM 5120 C CD B PRO A 1 617 ? 2.048 66.036 78.241 0.50 28.88 ? 658 PRO A CD 1 ATOM 5121 N N A ILE A 1 618 ? 2.913 68.282 74.370 0.50 23.65 ? 659 ILE A N 1 ATOM 5122 N N B ILE A 1 618 ? 1.493 67.446 74.640 0.50 26.16 ? 659 ILE A N 1 ATOM 5123 C CA A ILE A 1 618 ? 2.346 68.921 73.176 0.50 23.68 ? 659 ILE A CA 1 ATOM 5124 C CA B ILE A 1 618 ? 1.160 68.097 73.353 0.50 26.08 ? 659 ILE A CA 1 ATOM 5125 C C A ILE A 1 618 ? 3.472 69.618 72.428 0.50 22.24 ? 659 ILE A C 1 ATOM 5126 C C B ILE A 1 618 ? 2.347 68.882 72.793 0.50 24.76 ? 659 ILE A C 1 ATOM 5127 O O A ILE A 1 618 ? 3.538 69.529 71.225 0.50 21.28 ? 659 ILE A O 1 ATOM 5128 O O B ILE A 1 618 ? 2.610 68.869 71.593 0.50 24.68 ? 659 ILE A O 1 ATOM 5129 C CB A ILE A 1 618 ? 1.245 69.993 73.490 0.50 25.28 ? 659 ILE A CB 1 ATOM 5130 C CB B ILE A 1 618 ? -0.122 68.938 73.399 0.50 26.54 ? 659 ILE A CB 1 ATOM 5131 C CG1 A ILE A 1 618 ? 0.165 69.493 74.463 0.50 27.39 ? 659 ILE A CG1 1 ATOM 5132 C CG1 B ILE A 1 618 ? -1.307 67.999 73.565 0.50 28.81 ? 659 ILE A CG1 1 ATOM 5133 C CG2 A ILE A 1 618 ? 0.610 70.508 72.222 0.50 25.24 ? 659 ILE A CG2 1 ATOM 5134 C CG2 B ILE A 1 618 ? -0.298 69.740 72.122 0.50 27.82 ? 659 ILE A CG2 1 ATOM 5135 C CD1 A ILE A 1 618 ? -0.342 68.129 74.149 0.50 30.52 ? 659 ILE A CD1 1 ATOM 5136 C CD1 B ILE A 1 618 ? -1.007 66.606 73.082 0.50 28.37 ? 659 ILE A CD1 1 ATOM 5137 N N A VAL A 1 619 ? 4.343 70.319 73.153 0.50 22.32 ? 660 VAL A N 1 ATOM 5138 N N B VAL A 1 619 ? 3.085 69.569 73.656 0.50 24.65 ? 660 VAL A N 1 ATOM 5139 C CA A VAL A 1 619 ? 5.473 70.976 72.522 0.50 22.52 ? 660 VAL A CA 1 ATOM 5140 C CA B VAL A 1 619 ? 4.292 70.248 73.160 0.50 23.16 ? 660 VAL A CA 1 ATOM 5141 C C A VAL A 1 619 ? 6.407 69.925 71.928 0.50 21.33 ? 660 VAL A C 1 ATOM 5142 C C B VAL A 1 619 ? 5.307 69.261 72.525 0.50 21.95 ? 660 VAL A C 1 ATOM 5143 O O A VAL A 1 619 ? 6.909 70.085 70.804 0.50 21.37 ? 660 VAL A O 1 ATOM 5144 O O B VAL A 1 619 ? 5.853 69.508 71.429 0.50 21.65 ? 660 VAL A O 1 ATOM 5145 C CB A VAL A 1 619 ? 6.248 71.885 73.502 0.50 22.71 ? 660 VAL A CB 1 ATOM 5146 C CB B VAL A 1 619 ? 4.926 71.131 74.239 0.50 24.48 ? 660 VAL A CB 1 ATOM 5147 C CG1 A VAL A 1 619 ? 7.585 72.294 72.912 0.50 23.95 ? 660 VAL A CG1 1 ATOM 5148 C CG1 B VAL A 1 619 ? 6.278 71.703 73.744 0.50 24.05 ? 660 VAL A CG1 1 ATOM 5149 C CG2 A VAL A 1 619 ? 5.415 73.102 73.853 0.50 25.12 ? 660 VAL A CG2 1 ATOM 5150 C CG2 B VAL A 1 619 ? 3.963 72.260 74.650 0.50 25.01 ? 660 VAL A CG2 1 ATOM 5151 N N A LEU A 1 620 ? 6.608 68.838 72.674 0.50 21.09 ? 661 LEU A N 1 ATOM 5152 N N B LEU A 1 620 ? 5.506 68.101 73.142 0.50 20.73 ? 661 LEU A N 1 ATOM 5153 C CA A LEU A 1 620 ? 7.427 67.706 72.243 0.50 19.59 ? 661 LEU A CA 1 ATOM 5154 C CA B LEU A 1 620 ? 6.394 67.086 72.576 0.50 20.76 ? 661 LEU A CA 1 ATOM 5155 C C A LEU A 1 620 ? 6.848 67.134 70.944 0.50 20.22 ? 661 LEU A C 1 ATOM 5156 C C B LEU A 1 620 ? 5.839 66.598 71.240 0.50 20.30 ? 661 LEU A C 1 ATOM 5157 O O A LEU A 1 620 ? 7.550 67.035 69.960 0.50 19.09 ? 661 LEU A O 1 ATOM 5158 O O B LEU A 1 620 ? 6.572 66.334 70.267 0.50 19.88 ? 661 LEU A O 1 ATOM 5159 C CB A LEU A 1 620 ? 7.490 66.642 73.353 0.50 21.33 ? 661 LEU A CB 1 ATOM 5160 C CB B LEU A 1 620 ? 6.524 65.893 73.515 0.50 20.36 ? 661 LEU A CB 1 ATOM 5161 C CG A LEU A 1 620 ? 8.061 65.265 72.986 0.50 21.16 ? 661 LEU A CG 1 ATOM 5162 C CG B LEU A 1 620 ? 7.361 64.705 72.992 0.50 23.85 ? 661 LEU A CG 1 ATOM 5163 C CD1 A LEU A 1 620 ? 9.395 65.321 72.258 0.50 23.04 ? 661 LEU A CD1 1 ATOM 5164 C CD1 B LEU A 1 620 ? 8.796 65.118 72.699 0.50 23.46 ? 661 LEU A CD1 1 ATOM 5165 C CD2 A LEU A 1 620 ? 8.117 64.347 74.227 0.50 21.53 ? 661 LEU A CD2 1 ATOM 5166 C CD2 B LEU A 1 620 ? 7.342 63.591 74.044 0.50 23.50 ? 661 LEU A CD2 1 ATOM 5167 N N A ARG A 1 621 ? 5.552 66.822 70.947 0.50 19.99 ? 662 ARG A N 1 ATOM 5168 N N B ARG A 1 621 ? 4.531 66.437 71.202 0.50 20.96 ? 662 ARG A N 1 ATOM 5169 C CA A ARG A 1 621 ? 4.934 66.179 69.795 0.50 20.81 ? 662 ARG A CA 1 ATOM 5170 C CA B ARG A 1 621 ? 3.908 66.079 69.918 0.50 21.38 ? 662 ARG A CA 1 ATOM 5171 C C A ARG A 1 621 ? 4.826 67.165 68.694 0.50 21.10 ? 662 ARG A C 1 ATOM 5172 C C B ARG A 1 621 ? 4.178 67.058 68.725 0.50 21.88 ? 662 ARG A C 1 ATOM 5173 O O A ARG A 1 621 ? 5.145 66.814 67.559 0.50 18.68 ? 662 ARG A O 1 ATOM 5174 O O B ARG A 1 621 ? 4.342 66.600 67.600 0.50 20.66 ? 662 ARG A O 1 ATOM 5175 C CB A ARG A 1 621 ? 3.537 65.638 70.100 0.50 20.88 ? 662 ARG A CB 1 ATOM 5176 C CB B ARG A 1 621 ? 2.430 65.747 70.125 0.50 21.67 ? 662 ARG A CB 1 ATOM 5177 C CG A ARG A 1 621 ? 2.730 65.311 68.850 0.50 21.42 ? 662 ARG A CG 1 ATOM 5178 C CG B ARG A 1 621 ? 1.718 65.320 68.867 0.50 20.85 ? 662 ARG A CG 1 ATOM 5179 C CD A ARG A 1 621 ? 3.071 63.935 68.293 0.50 19.57 ? 662 ARG A CD 1 ATOM 5180 C CD B ARG A 1 621 ? 1.848 63.854 68.547 0.50 29.01 ? 662 ARG A CD 1 ATOM 5181 N NE A ARG A 1 621 ? 1.840 63.522 67.635 0.50 24.93 ? 662 ARG A NE 1 ATOM 5182 N NE B ARG A 1 621 ? 0.721 63.454 67.693 0.50 30.31 ? 662 ARG A NE 1 ATOM 5183 C CZ A ARG A 1 621 ? 1.304 62.311 67.682 0.50 21.27 ? 662 ARG A CZ 1 ATOM 5184 C CZ B ARG A 1 621 ? 0.312 62.210 67.493 0.50 29.12 ? 662 ARG A CZ 1 ATOM 5185 N NH1 A ARG A 1 621 ? 1.901 61.296 68.312 0.50 23.44 ? 662 ARG A NH1 1 ATOM 5186 N NH1 B ARG A 1 621 ? 0.959 61.182 68.045 0.50 30.61 ? 662 ARG A NH1 1 ATOM 5187 N NH2 A ARG A 1 621 ? 0.150 62.130 67.070 0.50 25.85 ? 662 ARG A NH2 1 ATOM 5188 N NH2 B ARG A 1 621 ? -0.744 62.001 66.710 0.50 30.58 ? 662 ARG A NH2 1 ATOM 5189 N N . MET A 1 622 ? 4.319 68.369 68.997 1.00 23.01 ? 663 MET A N 1 ATOM 5190 C CA . MET A 1 622 ? 4.503 69.454 67.977 1.00 24.04 ? 663 MET A CA 1 ATOM 5191 C C . MET A 1 622 ? 5.913 69.428 67.358 1.00 24.54 ? 663 MET A C 1 ATOM 5192 O O . MET A 1 622 ? 6.090 69.493 66.145 1.00 22.90 ? 663 MET A O 1 ATOM 5193 C CB A MET A 1 622 ? 4.336 70.851 68.602 0.50 24.48 ? 663 MET A CB 1 ATOM 5194 C CB B MET A 1 622 ? 4.027 70.809 68.542 0.50 24.79 ? 663 MET A CB 1 ATOM 5195 C CG A MET A 1 622 ? 4.885 72.008 67.709 0.50 24.49 ? 663 MET A CG 1 ATOM 5196 C CG B MET A 1 622 ? 2.544 70.730 69.027 0.50 24.43 ? 663 MET A CG 1 ATOM 5197 S SD A MET A 1 622 ? 4.474 73.624 68.423 0.50 22.97 ? 663 MET A SD 1 ATOM 5198 S SD B MET A 1 622 ? 1.611 72.231 69.495 0.50 27.27 ? 663 MET A SD 1 ATOM 5199 C CE A MET A 1 622 ? 2.804 73.243 68.944 0.50 28.89 ? 663 MET A CE 1 ATOM 5200 C CE B MET A 1 622 ? 2.398 72.638 71.099 0.50 18.53 ? 663 MET A CE 1 ATOM 5201 N N . MET A 1 623 ? 6.971 69.333 68.184 1.00 22.87 ? 664 MET A N 1 ATOM 5202 C CA . MET A 1 623 ? 8.297 69.314 67.638 1.00 22.79 ? 664 MET A CA 1 ATOM 5203 C C . MET A 1 623 ? 8.639 67.996 66.911 1.00 22.09 ? 664 MET A C 1 ATOM 5204 O O . MET A 1 623 ? 9.375 67.995 65.916 1.00 23.51 ? 664 MET A O 1 ATOM 5205 C CB A MET A 1 623 ? 9.261 69.406 68.843 0.50 24.52 ? 664 MET A CB 1 ATOM 5206 C CB B MET A 1 623 ? 9.390 69.755 68.635 0.50 23.53 ? 664 MET A CB 1 ATOM 5207 C CG A MET A 1 623 ? 8.840 70.445 69.858 0.50 27.40 ? 664 MET A CG 1 ATOM 5208 C CG B MET A 1 623 ? 9.352 71.237 68.874 0.50 20.45 ? 664 MET A CG 1 ATOM 5209 S SD A MET A 1 623 ? 9.067 72.029 69.098 0.50 31.30 ? 664 MET A SD 1 ATOM 5210 S SD B MET A 1 623 ? 10.737 71.870 69.859 0.50 24.14 ? 664 MET A SD 1 ATOM 5211 C CE A MET A 1 623 ? 10.648 72.528 69.773 0.50 27.39 ? 664 MET A CE 1 ATOM 5212 C CE B MET A 1 623 ? 11.759 72.479 68.537 0.50 19.34 ? 664 MET A CE 1 ATOM 5213 N N . ASN A 1 624 ? 8.110 66.888 67.434 1.00 23.21 ? 665 ASN A N 1 ATOM 5214 C CA . ASN A 1 624 ? 8.304 65.587 66.765 1.00 21.52 ? 665 ASN A CA 1 ATOM 5215 C C . ASN A 1 624 ? 7.574 65.614 65.423 1.00 21.40 ? 665 ASN A C 1 ATOM 5216 O O . ASN A 1 624 ? 8.098 65.081 64.477 1.00 21.14 ? 665 ASN A O 1 ATOM 5217 C CB . ASN A 1 624 ? 7.817 64.431 67.603 1.00 23.14 ? 665 ASN A CB 1 ATOM 5218 C CG . ASN A 1 624 ? 8.921 63.930 68.577 1.00 23.17 ? 665 ASN A CG 1 ATOM 5219 O OD1 . ASN A 1 624 ? 10.119 64.115 68.312 1.00 24.05 ? 665 ASN A OD1 1 ATOM 5220 N ND2 . ASN A 1 624 ? 8.507 63.312 69.657 1.00 23.68 ? 665 ASN A ND2 1 ATOM 5221 N N . ASP A 1 625 ? 6.409 66.240 65.387 1.00 20.84 ? 666 ASP A N 1 ATOM 5222 C CA . ASP A 1 625 ? 5.705 66.383 64.072 1.00 21.02 ? 666 ASP A CA 1 ATOM 5223 C C . ASP A 1 625 ? 6.521 67.255 63.105 1.00 21.16 ? 666 ASP A C 1 ATOM 5224 O O . ASP A 1 625 ? 6.618 66.944 61.902 1.00 20.27 ? 666 ASP A O 1 ATOM 5225 C CB . ASP A 1 625 ? 4.309 66.972 64.280 1.00 20.88 ? 666 ASP A CB 1 ATOM 5226 C CG . ASP A 1 625 ? 3.278 65.959 64.782 1.00 23.90 ? 666 ASP A CG 1 ATOM 5227 O OD1 . ASP A 1 625 ? 3.638 64.761 64.943 1.00 25.85 ? 666 ASP A OD1 1 ATOM 5228 O OD2 . ASP A 1 625 ? 2.092 66.374 64.957 1.00 26.09 ? 666 ASP A OD2 1 ATOM 5229 N N . GLN A 1 626 ? 7.126 68.343 63.592 1.00 19.48 ? 667 GLN A N 1 ATOM 5230 C CA . GLN A 1 626 ? 8.010 69.121 62.706 1.00 19.74 ? 667 GLN A CA 1 ATOM 5231 C C . GLN A 1 626 ? 9.164 68.288 62.172 1.00 19.68 ? 667 GLN A C 1 ATOM 5232 O O . GLN A 1 626 ? 9.510 68.377 60.995 1.00 21.01 ? 667 GLN A O 1 ATOM 5233 C CB . GLN A 1 626 ? 8.526 70.389 63.433 1.00 19.72 ? 667 GLN A CB 1 ATOM 5234 C CG . GLN A 1 626 ? 7.376 71.404 63.587 1.00 21.07 ? 667 GLN A CG 1 ATOM 5235 C CD . GLN A 1 626 ? 7.818 72.618 64.317 1.00 21.79 ? 667 GLN A CD 1 ATOM 5236 O OE1 . GLN A 1 626 ? 7.945 72.590 65.551 1.00 23.83 ? 667 GLN A OE1 1 ATOM 5237 N NE2 . GLN A 1 626 ? 8.067 73.714 63.578 1.00 21.27 ? 667 GLN A NE2 1 ATOM 5238 N N . LEU A 1 627 ? 9.745 67.432 63.020 1.00 20.59 ? 668 LEU A N 1 ATOM 5239 C CA . LEU A 1 627 ? 10.809 66.555 62.558 1.00 20.75 ? 668 LEU A CA 1 ATOM 5240 C C . LEU A 1 627 ? 10.331 65.510 61.543 1.00 19.99 ? 668 LEU A C 1 ATOM 5241 O O . LEU A 1 627 ? 11.007 65.297 60.510 1.00 21.53 ? 668 LEU A O 1 ATOM 5242 C CB . LEU A 1 627 ? 11.465 65.843 63.756 1.00 21.76 ? 668 LEU A CB 1 ATOM 5243 C CG . LEU A 1 627 ? 12.340 66.840 64.553 1.00 26.01 ? 668 LEU A CG 1 ATOM 5244 C CD1 . LEU A 1 627 ? 12.780 66.186 65.848 1.00 28.32 ? 668 LEU A CD1 1 ATOM 5245 C CD2 . LEU A 1 627 ? 13.578 67.307 63.719 1.00 25.67 ? 668 LEU A CD2 1 ATOM 5246 N N . MET A 1 628 ? 9.168 64.941 61.819 1.00 20.90 ? 669 MET A N 1 ATOM 5247 C CA . MET A 1 628 ? 8.613 63.888 60.959 1.00 21.11 ? 669 MET A CA 1 ATOM 5248 C C . MET A 1 628 ? 8.198 64.441 59.596 1.00 19.94 ? 669 MET A C 1 ATOM 5249 O O . MET A 1 628 ? 8.400 63.790 58.553 1.00 20.81 ? 669 MET A O 1 ATOM 5250 C CB . MET A 1 628 ? 7.386 63.267 61.602 1.00 22.05 ? 669 MET A CB 1 ATOM 5251 C CG . MET A 1 628 ? 6.696 62.195 60.708 1.00 25.23 ? 669 MET A CG 1 ATOM 5252 S SD . MET A 1 628 ? 5.270 61.425 61.540 1.00 29.20 ? 669 MET A SD 1 ATOM 5253 C CE . MET A 1 628 ? 4.003 62.699 61.369 1.00 26.35 ? 669 MET A CE 1 ATOM 5254 N N . PHE A 1 629 ? 7.610 65.615 59.613 1.00 18.39 ? 670 PHE A N 1 ATOM 5255 C CA . PHE A 1 629 ? 7.097 66.223 58.331 1.00 18.81 ? 670 PHE A CA 1 ATOM 5256 C C . PHE A 1 629 ? 8.171 66.989 57.566 1.00 18.90 ? 670 PHE A C 1 ATOM 5257 O O . PHE A 1 629 ? 7.904 67.502 56.466 1.00 19.05 ? 670 PHE A O 1 ATOM 5258 C CB . PHE A 1 629 ? 5.869 67.079 58.596 1.00 18.78 ? 670 PHE A CB 1 ATOM 5259 C CG . PHE A 1 629 ? 4.614 66.283 58.905 1.00 19.58 ? 670 PHE A CG 1 ATOM 5260 C CD1 . PHE A 1 629 ? 4.099 65.340 57.995 1.00 21.98 ? 670 PHE A CD1 1 ATOM 5261 C CD2 . PHE A 1 629 ? 3.902 66.527 60.087 1.00 22.61 ? 670 PHE A CD2 1 ATOM 5262 C CE1 . PHE A 1 629 ? 2.921 64.638 58.299 1.00 24.35 ? 670 PHE A CE1 1 ATOM 5263 C CE2 . PHE A 1 629 ? 2.719 65.849 60.379 1.00 25.25 ? 670 PHE A CE2 1 ATOM 5264 C CZ . PHE A 1 629 ? 2.237 64.886 59.487 1.00 24.72 ? 670 PHE A CZ 1 ATOM 5265 N N . LEU A 1 630 ? 9.407 67.039 58.073 1.00 19.18 ? 671 LEU A N 1 ATOM 5266 C CA . LEU A 1 630 ? 10.475 67.760 57.372 1.00 18.50 ? 671 LEU A CA 1 ATOM 5267 C C . LEU A 1 630 ? 10.849 67.029 56.071 1.00 17.97 ? 671 LEU A C 1 ATOM 5268 O O . LEU A 1 630 ? 10.920 67.670 55.026 1.00 18.75 ? 671 LEU A O 1 ATOM 5269 C CB . LEU A 1 630 ? 11.686 67.948 58.308 1.00 19.73 ? 671 LEU A CB 1 ATOM 5270 C CG . LEU A 1 630 ? 12.850 68.637 57.614 1.00 19.83 ? 671 LEU A CG 1 ATOM 5271 C CD1 . LEU A 1 630 ? 12.513 70.038 57.096 1.00 21.93 ? 671 LEU A CD1 1 ATOM 5272 C CD2 . LEU A 1 630 ? 13.978 68.769 58.721 1.00 21.95 ? 671 LEU A CD2 1 ATOM 5273 N N . GLU A 1 631 ? 11.075 65.708 56.122 1.00 17.49 ? 672 GLU A N 1 ATOM 5274 C CA . GLU A 1 631 ? 11.303 64.983 54.858 1.00 17.35 ? 672 GLU A CA 1 ATOM 5275 C C . GLU A 1 631 ? 10.075 65.170 53.925 1.00 15.56 ? 672 GLU A C 1 ATOM 5276 O O . GLU A 1 631 ? 10.217 65.327 52.669 1.00 17.03 ? 672 GLU A O 1 ATOM 5277 C CB . GLU A 1 631 ? 11.518 63.484 55.120 1.00 17.93 ? 672 GLU A CB 1 ATOM 5278 C CG . GLU A 1 631 ? 12.103 62.794 53.875 1.00 16.94 ? 672 GLU A CG 1 ATOM 5279 C CD . GLU A 1 631 ? 13.598 63.083 53.807 1.00 20.84 ? 672 GLU A CD 1 ATOM 5280 O OE1 . GLU A 1 631 ? 14.298 62.626 54.733 1.00 20.01 ? 672 GLU A OE1 1 ATOM 5281 O OE2 . GLU A 1 631 ? 14.052 63.733 52.819 1.00 21.00 ? 672 GLU A OE2 1 ATOM 5282 N N . ARG A 1 632 ? 8.886 65.145 54.496 1.00 16.16 ? 673 ARG A N 1 ATOM 5283 C CA . ARG A 1 632 ? 7.663 65.300 53.730 1.00 16.03 ? 673 ARG A CA 1 ATOM 5284 C C . ARG A 1 632 ? 7.608 66.644 52.966 1.00 16.58 ? 673 ARG A C 1 ATOM 5285 O O . ARG A 1 632 ? 7.033 66.732 51.876 1.00 17.18 ? 673 ARG A O 1 ATOM 5286 C CB . ARG A 1 632 ? 6.438 65.160 54.672 1.00 18.47 ? 673 ARG A CB 1 ATOM 5287 C CG . ARG A 1 632 ? 5.229 64.533 53.981 1.00 17.46 ? 673 ARG A CG 1 ATOM 5288 C CD . ARG A 1 632 ? 5.407 62.978 54.154 1.00 18.96 ? 673 ARG A CD 1 ATOM 5289 N NE . ARG A 1 632 ? 4.946 62.428 55.481 1.00 16.22 ? 673 ARG A NE 1 ATOM 5290 C CZ . ARG A 1 632 ? 5.760 61.866 56.362 1.00 17.83 ? 673 ARG A CZ 1 ATOM 5291 N NH1 . ARG A 1 632 ? 7.107 61.790 56.167 1.00 18.29 ? 673 ARG A NH1 1 ATOM 5292 N NH2 . ARG A 1 632 ? 5.219 61.399 57.485 1.00 19.93 ? 673 ARG A NH2 1 ATOM 5293 N N . ALA A 1 633 ? 8.220 67.680 53.556 1.00 15.80 ? 674 ALA A N 1 ATOM 5294 C CA . ALA A 1 633 ? 8.176 68.989 52.932 1.00 15.79 ? 674 ALA A CA 1 ATOM 5295 C C . ALA A 1 633 ? 8.924 69.038 51.620 1.00 15.48 ? 674 ALA A C 1 ATOM 5296 O O . ALA A 1 633 ? 8.731 69.994 50.865 1.00 17.89 ? 674 ALA A O 1 ATOM 5297 C CB . ALA A 1 633 ? 8.748 70.030 53.914 1.00 17.76 ? 674 ALA A CB 1 ATOM 5298 N N . PHE A 1 634 ? 9.851 68.100 51.382 1.00 16.03 ? 675 PHE A N 1 ATOM 5299 C CA . PHE A 1 634 ? 10.557 68.132 50.088 1.00 15.49 ? 675 PHE A CA 1 ATOM 5300 C C . PHE A 1 634 ? 9.805 67.505 48.960 1.00 16.46 ? 675 PHE A C 1 ATOM 5301 O O . PHE A 1 634 ? 10.261 67.564 47.801 1.00 16.78 ? 675 PHE A O 1 ATOM 5302 C CB . PHE A 1 634 ? 11.914 67.444 50.263 1.00 16.25 ? 675 PHE A CB 1 ATOM 5303 C CG . PHE A 1 634 ? 12.810 68.203 51.166 1.00 17.47 ? 675 PHE A CG 1 ATOM 5304 C CD1 . PHE A 1 634 ? 13.281 69.473 50.810 1.00 18.04 ? 675 PHE A CD1 1 ATOM 5305 C CD2 . PHE A 1 634 ? 13.253 67.610 52.356 1.00 20.41 ? 675 PHE A CD2 1 ATOM 5306 C CE1 . PHE A 1 634 ? 14.164 70.203 51.649 1.00 19.93 ? 675 PHE A CE1 1 ATOM 5307 C CE2 . PHE A 1 634 ? 14.155 68.346 53.191 1.00 21.09 ? 675 PHE A CE2 1 ATOM 5308 C CZ . PHE A 1 634 ? 14.583 69.644 52.817 1.00 20.51 ? 675 PHE A CZ 1 ATOM 5309 N N . ILE A 1 635 ? 8.586 67.025 49.225 1.00 16.13 ? 676 ILE A N 1 ATOM 5310 C CA . ILE A 1 635 ? 7.723 66.438 48.175 1.00 15.73 ? 676 ILE A CA 1 ATOM 5311 C C . ILE A 1 635 ? 7.008 67.549 47.415 1.00 16.26 ? 676 ILE A C 1 ATOM 5312 O O . ILE A 1 635 ? 6.435 68.485 48.030 1.00 19.30 ? 676 ILE A O 1 ATOM 5313 C CB . ILE A 1 635 ? 6.702 65.502 48.867 1.00 16.04 ? 676 ILE A CB 1 ATOM 5314 C CG1 . ILE A 1 635 ? 7.425 64.264 49.450 1.00 17.41 ? 676 ILE A CG1 1 ATOM 5315 C CG2 . ILE A 1 635 ? 5.583 65.062 47.840 1.00 16.58 ? 676 ILE A CG2 1 ATOM 5316 C CD1 . ILE A 1 635 ? 8.209 63.372 48.396 1.00 19.51 ? 676 ILE A CD1 1 ATOM 5317 N N . ASP A 1 636 ? 7.009 67.456 46.081 1.00 15.50 ? 677 ASP A N 1 ATOM 5318 C CA . ASP A 1 636 ? 6.219 68.354 45.240 1.00 16.88 ? 677 ASP A CA 1 ATOM 5319 C C . ASP A 1 636 ? 5.059 67.543 44.697 1.00 17.13 ? 677 ASP A C 1 ATOM 5320 O O . ASP A 1 636 ? 5.273 66.512 44.065 1.00 17.30 ? 677 ASP A O 1 ATOM 5321 C CB . ASP A 1 636 ? 7.074 68.776 44.054 1.00 17.24 ? 677 ASP A CB 1 ATOM 5322 C CG . ASP A 1 636 ? 6.418 69.843 43.201 1.00 18.96 ? 677 ASP A CG 1 ATOM 5323 O OD1 . ASP A 1 636 ? 5.159 69.883 43.086 1.00 18.79 ? 677 ASP A OD1 1 ATOM 5324 O OD2 . ASP A 1 636 ? 7.189 70.632 42.586 1.00 20.25 ? 677 ASP A OD2 1 ATOM 5325 N N . PRO A 1 637 ? 3.833 67.960 44.971 1.00 19.01 ? 678 PRO A N 1 ATOM 5326 C CA . PRO A 1 637 ? 2.695 67.135 44.583 1.00 21.88 ? 678 PRO A CA 1 ATOM 5327 C C . PRO A 1 637 ? 2.550 67.066 43.069 1.00 22.93 ? 678 PRO A C 1 ATOM 5328 O O . PRO A 1 637 ? 1.803 66.218 42.570 1.00 26.73 ? 678 PRO A O 1 ATOM 5329 C CB . PRO A 1 637 ? 1.496 67.889 45.187 1.00 21.85 ? 678 PRO A CB 1 ATOM 5330 C CG . PRO A 1 637 ? 1.978 69.284 45.454 1.00 23.80 ? 678 PRO A CG 1 ATOM 5331 C CD . PRO A 1 637 ? 3.458 69.159 45.748 1.00 19.64 ? 678 PRO A CD 1 ATOM 5332 N N . LEU A 1 638 ? 3.260 67.902 42.319 1.00 18.71 ? 679 LEU A N 1 ATOM 5333 C CA . LEU A 1 638 ? 3.195 67.767 40.847 1.00 19.09 ? 679 LEU A CA 1 ATOM 5334 C C . LEU A 1 638 ? 4.225 66.795 40.254 1.00 20.56 ? 679 LEU A C 1 ATOM 5335 O O . LEU A 1 638 ? 4.180 66.487 39.046 1.00 21.24 ? 679 LEU A O 1 ATOM 5336 C CB . LEU A 1 638 ? 3.334 69.150 40.204 1.00 18.87 ? 679 LEU A CB 1 ATOM 5337 C CG . LEU A 1 638 ? 2.246 70.151 40.629 1.00 21.19 ? 679 LEU A CG 1 ATOM 5338 C CD1 . LEU A 1 638 ? 2.481 71.517 39.954 1.00 22.61 ? 679 LEU A CD1 1 ATOM 5339 C CD2 . LEU A 1 638 ? 0.830 69.562 40.233 1.00 23.70 ? 679 LEU A CD2 1 ATOM 5340 N N . GLY A 1 639 ? 5.123 66.291 41.099 1.00 18.96 ? 680 GLY A N 1 ATOM 5341 C CA . GLY A 1 639 ? 6.180 65.351 40.698 1.00 19.13 ? 680 GLY A CA 1 ATOM 5342 C C . GLY A 1 639 ? 7.280 66.022 39.875 1.00 20.23 ? 680 GLY A C 1 ATOM 5343 O O . GLY A 1 639 ? 7.201 67.198 39.549 1.00 22.06 ? 680 GLY A O 1 ATOM 5344 N N . LEU A 1 640 ? 8.280 65.253 39.474 1.00 19.98 ? 681 LEU A N 1 ATOM 5345 C CA . LEU A 1 640 ? 9.299 65.773 38.586 1.00 21.01 ? 681 LEU A CA 1 ATOM 5346 C C . LEU A 1 640 ? 8.847 65.631 37.131 1.00 22.29 ? 681 LEU A C 1 ATOM 5347 O O . LEU A 1 640 ? 7.936 64.863 36.830 1.00 22.34 ? 681 LEU A O 1 ATOM 5348 C CB . LEU A 1 640 ? 10.600 64.972 38.835 1.00 20.96 ? 681 LEU A CB 1 ATOM 5349 C CG . LEU A 1 640 ? 11.187 65.265 40.226 1.00 21.75 ? 681 LEU A CG 1 ATOM 5350 C CD1 . LEU A 1 640 ? 12.230 64.199 40.605 1.00 25.23 ? 681 LEU A CD1 1 ATOM 5351 C CD2 . LEU A 1 640 ? 11.843 66.706 40.298 1.00 26.10 ? 681 LEU A CD2 1 ATOM 5352 N N . PRO A 1 641 ? 9.483 66.372 36.195 1.00 24.45 ? 682 PRO A N 1 ATOM 5353 C CA . PRO A 1 641 ? 9.059 66.330 34.796 1.00 25.54 ? 682 PRO A CA 1 ATOM 5354 C C . PRO A 1 641 ? 8.963 64.947 34.171 1.00 25.45 ? 682 PRO A C 1 ATOM 5355 O O . PRO A 1 641 ? 9.941 64.188 34.137 1.00 26.71 ? 682 PRO A O 1 ATOM 5356 C CB . PRO A 1 641 ? 10.158 67.172 34.076 1.00 26.77 ? 682 PRO A CB 1 ATOM 5357 C CG . PRO A 1 641 ? 10.526 68.137 35.106 1.00 26.88 ? 682 PRO A CG 1 ATOM 5358 C CD . PRO A 1 641 ? 10.604 67.311 36.391 1.00 26.04 ? 682 PRO A CD 1 ATOM 5359 N N . ASP A 1 642 ? 7.758 64.620 33.709 1.00 25.50 ? 683 ASP A N 1 ATOM 5360 C CA . ASP A 1 642 ? 7.427 63.333 33.106 1.00 26.40 ? 683 ASP A CA 1 ATOM 5361 C C . ASP A 1 642 ? 7.705 62.127 33.988 1.00 24.54 ? 683 ASP A C 1 ATOM 5362 O O . ASP A 1 642 ? 7.660 60.980 33.501 1.00 24.69 ? 683 ASP A O 1 ATOM 5363 C CB . ASP A 1 642 ? 8.137 63.139 31.772 1.00 29.28 ? 683 ASP A CB 1 ATOM 5364 C CG . ASP A 1 642 ? 7.800 64.235 30.789 1.00 35.71 ? 683 ASP A CG 1 ATOM 5365 O OD1 . ASP A 1 642 ? 6.594 64.410 30.494 1.00 39.43 ? 683 ASP A OD1 1 ATOM 5366 O OD2 . ASP A 1 642 ? 8.751 64.913 30.358 1.00 41.35 ? 683 ASP A OD2 1 ATOM 5367 N N . ARG A 1 643 ? 7.907 62.382 35.288 1.00 22.09 ? 684 ARG A N 1 ATOM 5368 C CA . ARG A 1 643 ? 8.090 61.302 36.288 1.00 21.06 ? 684 ARG A CA 1 ATOM 5369 C C . ARG A 1 643 ? 7.204 61.628 37.508 1.00 19.41 ? 684 ARG A C 1 ATOM 5370 O O . ARG A 1 643 ? 7.681 61.958 38.623 1.00 19.56 ? 684 ARG A O 1 ATOM 5371 C CB . ARG A 1 643 ? 9.572 61.084 36.670 1.00 21.83 ? 684 ARG A CB 1 ATOM 5372 C CG . ARG A 1 643 ? 10.397 60.660 35.418 1.00 20.84 ? 684 ARG A CG 1 ATOM 5373 C CD . ARG A 1 643 ? 11.820 60.164 35.840 1.00 21.90 ? 684 ARG A CD 1 ATOM 5374 N NE . ARG A 1 643 ? 12.590 61.292 36.425 1.00 23.14 ? 684 ARG A NE 1 ATOM 5375 C CZ . ARG A 1 643 ? 13.770 61.190 37.056 1.00 22.95 ? 684 ARG A CZ 1 ATOM 5376 N NH1 . ARG A 1 643 ? 14.376 60.006 37.223 1.00 23.00 ? 684 ARG A NH1 1 ATOM 5377 N NH2 . ARG A 1 643 ? 14.338 62.302 37.553 1.00 22.41 ? 684 ARG A NH2 1 ATOM 5378 N N . PRO A 1 644 ? 5.885 61.474 37.334 1.00 19.25 ? 685 PRO A N 1 ATOM 5379 C CA . PRO A 1 644 ? 4.946 61.904 38.377 1.00 19.21 ? 685 PRO A CA 1 ATOM 5380 C C . PRO A 1 644 ? 5.061 61.169 39.719 1.00 18.03 ? 685 PRO A C 1 ATOM 5381 O O . PRO A 1 644 ? 4.611 61.707 40.728 1.00 19.36 ? 685 PRO A O 1 ATOM 5382 C CB . PRO A 1 644 ? 3.539 61.664 37.758 1.00 20.38 ? 685 PRO A CB 1 ATOM 5383 C CG . PRO A 1 644 ? 3.764 60.652 36.675 1.00 20.05 ? 685 PRO A CG 1 ATOM 5384 C CD . PRO A 1 644 ? 5.208 60.935 36.131 1.00 20.37 ? 685 PRO A CD 1 ATOM 5385 N N . PHE A 1 645 ? 5.665 59.990 39.737 1.00 16.60 ? 686 PHE A N 1 ATOM 5386 C CA . PHE A 1 645 ? 5.843 59.239 40.976 1.00 16.84 ? 686 PHE A CA 1 ATOM 5387 C C . PHE A 1 645 ? 7.176 59.459 41.662 1.00 16.95 ? 686 PHE A C 1 ATOM 5388 O O . PHE A 1 645 ? 7.414 58.904 42.769 1.00 17.89 ? 686 PHE A O 1 ATOM 5389 C CB . PHE A 1 645 ? 5.567 57.741 40.719 1.00 17.82 ? 686 PHE A CB 1 ATOM 5390 C CG . PHE A 1 645 ? 4.153 57.503 40.253 1.00 16.81 ? 686 PHE A CG 1 ATOM 5391 C CD1 . PHE A 1 645 ? 3.081 57.846 41.084 1.00 17.39 ? 686 PHE A CD1 1 ATOM 5392 C CD2 . PHE A 1 645 ? 3.895 57.000 38.991 1.00 19.01 ? 686 PHE A CD2 1 ATOM 5393 C CE1 . PHE A 1 645 ? 1.758 57.635 40.611 1.00 16.70 ? 686 PHE A CE1 1 ATOM 5394 C CE2 . PHE A 1 645 ? 2.603 56.824 38.504 1.00 20.31 ? 686 PHE A CE2 1 ATOM 5395 C CZ . PHE A 1 645 ? 1.523 57.128 39.348 1.00 18.97 ? 686 PHE A CZ 1 ATOM 5396 N N A TYR A 1 646 ? 8.037 60.262 41.041 0.50 15.84 ? 687 TYR A N 1 ATOM 5397 N N B TYR A 1 646 ? 8.046 60.271 41.050 0.50 15.95 ? 687 TYR A N 1 ATOM 5398 C CA A TYR A 1 646 ? 9.217 60.729 41.753 0.50 15.93 ? 687 TYR A CA 1 ATOM 5399 C CA B TYR A 1 646 ? 9.252 60.727 41.761 0.50 16.10 ? 687 TYR A CA 1 ATOM 5400 C C A TYR A 1 646 ? 8.856 62.150 42.139 0.50 16.00 ? 687 TYR A C 1 ATOM 5401 C C B TYR A 1 646 ? 8.992 62.169 42.168 0.50 16.30 ? 687 TYR A C 1 ATOM 5402 O O A TYR A 1 646 ? 8.747 63.037 41.276 0.50 17.42 ? 687 TYR A O 1 ATOM 5403 O O B TYR A 1 646 ? 9.143 63.095 41.358 0.50 17.82 ? 687 TYR A O 1 ATOM 5404 C CB A TYR A 1 646 ? 10.460 60.652 40.855 0.50 16.71 ? 687 TYR A CB 1 ATOM 5405 C CB B TYR A 1 646 ? 10.503 60.645 40.870 0.50 16.89 ? 687 TYR A CB 1 ATOM 5406 C CG A TYR A 1 646 ? 10.912 59.219 40.558 0.50 15.60 ? 687 TYR A CG 1 ATOM 5407 C CG B TYR A 1 646 ? 10.975 59.230 40.538 0.50 16.02 ? 687 TYR A CG 1 ATOM 5408 C CD1 A TYR A 1 646 ? 10.624 58.178 41.447 0.50 17.20 ? 687 TYR A CD1 1 ATOM 5409 C CD1 B TYR A 1 646 ? 10.705 58.160 41.392 0.50 18.04 ? 687 TYR A CD1 1 ATOM 5410 C CD2 A TYR A 1 646 ? 11.654 58.931 39.431 0.50 18.07 ? 687 TYR A CD2 1 ATOM 5411 C CD2 B TYR A 1 646 ? 11.736 58.994 39.403 0.50 18.22 ? 687 TYR A CD2 1 ATOM 5412 C CE1 A TYR A 1 646 ? 11.061 56.869 41.212 0.50 18.95 ? 687 TYR A CE1 1 ATOM 5413 C CE1 B TYR A 1 646 ? 11.169 56.864 41.112 0.50 19.43 ? 687 TYR A CE1 1 ATOM 5414 C CE2 A TYR A 1 646 ? 12.073 57.611 39.176 0.50 17.57 ? 687 TYR A CE2 1 ATOM 5415 C CE2 B TYR A 1 646 ? 12.184 57.691 39.107 0.50 18.88 ? 687 TYR A CE2 1 ATOM 5416 C CZ A TYR A 1 646 ? 11.784 56.603 40.082 0.50 19.05 ? 687 TYR A CZ 1 ATOM 5417 C CZ B TYR A 1 646 ? 11.901 56.652 39.972 0.50 20.36 ? 687 TYR A CZ 1 ATOM 5418 O OH A TYR A 1 646 ? 12.217 55.305 39.819 0.50 20.06 ? 687 TYR A OH 1 ATOM 5419 O OH B TYR A 1 646 ? 12.365 55.382 39.654 0.50 20.57 ? 687 TYR A OH 1 ATOM 5420 N N . ARG A 1 647 ? 8.643 62.361 43.434 1.00 14.62 ? 688 ARG A N 1 ATOM 5421 C CA . ARG A 1 647 ? 8.115 63.667 43.896 1.00 14.16 ? 688 ARG A CA 1 ATOM 5422 C C . ARG A 1 647 ? 9.080 64.432 44.810 1.00 14.56 ? 688 ARG A C 1 ATOM 5423 O O . ARG A 1 647 ? 8.794 65.576 45.136 1.00 16.03 ? 688 ARG A O 1 ATOM 5424 C CB A ARG A 1 647 ? 6.776 63.507 44.600 0.65 14.22 ? 688 ARG A CB 1 ATOM 5425 C CB B ARG A 1 647 ? 6.823 63.401 44.653 0.35 14.96 ? 688 ARG A CB 1 ATOM 5426 C CG A ARG A 1 647 ? 5.772 62.810 43.641 0.65 12.76 ? 688 ARG A CG 1 ATOM 5427 C CG B ARG A 1 647 ? 5.960 62.353 43.923 0.35 16.74 ? 688 ARG A CG 1 ATOM 5428 C CD A ARG A 1 647 ? 4.347 62.862 44.144 0.65 9.97 ? 688 ARG A CD 1 ATOM 5429 C CD B ARG A 1 647 ? 4.607 62.255 44.559 0.35 21.80 ? 688 ARG A CD 1 ATOM 5430 N NE A ARG A 1 647 ? 4.168 62.479 45.569 0.65 10.76 ? 688 ARG A NE 1 ATOM 5431 N NE B ARG A 1 647 ? 3.655 61.667 43.626 0.35 24.26 ? 688 ARG A NE 1 ATOM 5432 C CZ A ARG A 1 647 ? 3.103 62.776 46.301 0.65 14.36 ? 688 ARG A CZ 1 ATOM 5433 C CZ B ARG A 1 647 ? 2.923 62.373 42.786 0.35 29.35 ? 688 ARG A CZ 1 ATOM 5434 N NH1 A ARG A 1 647 ? 3.100 62.404 47.595 0.65 12.89 ? 688 ARG A NH1 1 ATOM 5435 N NH1 B ARG A 1 647 ? 2.072 61.762 41.950 0.35 26.87 ? 688 ARG A NH1 1 ATOM 5436 N NH2 A ARG A 1 647 ? 2.071 63.451 45.773 0.65 15.42 ? 688 ARG A NH2 1 ATOM 5437 N NH2 B ARG A 1 647 ? 3.066 63.693 42.760 0.35 32.20 ? 688 ARG A NH2 1 ATOM 5438 N N . HIS A 1 648 ? 10.220 63.829 45.181 1.00 14.75 ? 689 HIS A N 1 ATOM 5439 C CA . HIS A 1 648 ? 11.135 64.487 46.128 1.00 15.19 ? 689 HIS A CA 1 ATOM 5440 C C . HIS A 1 648 ? 11.962 65.442 45.278 1.00 16.24 ? 689 HIS A C 1 ATOM 5441 O O . HIS A 1 648 ? 12.477 65.068 44.219 1.00 17.42 ? 689 HIS A O 1 ATOM 5442 C CB . HIS A 1 648 ? 12.003 63.409 46.758 1.00 16.44 ? 689 HIS A CB 1 ATOM 5443 C CG . HIS A 1 648 ? 12.654 63.819 48.044 1.00 15.41 ? 689 HIS A CG 1 ATOM 5444 N ND1 . HIS A 1 648 ? 13.633 64.799 48.125 1.00 16.37 ? 689 HIS A ND1 1 ATOM 5445 C CD2 . HIS A 1 648 ? 12.461 63.356 49.298 1.00 15.80 ? 689 HIS A CD2 1 ATOM 5446 C CE1 . HIS A 1 648 ? 14.019 64.919 49.390 1.00 18.20 ? 689 HIS A CE1 1 ATOM 5447 N NE2 . HIS A 1 648 ? 13.336 64.043 50.121 1.00 17.22 ? 689 HIS A NE2 1 ATOM 5448 N N . VAL A 1 649 ? 12.071 66.678 45.731 1.00 15.32 ? 690 VAL A N 1 ATOM 5449 C CA . VAL A 1 649 ? 12.751 67.716 44.911 1.00 15.11 ? 690 VAL A CA 1 ATOM 5450 C C . VAL A 1 649 ? 14.275 67.687 45.135 1.00 16.66 ? 690 VAL A C 1 ATOM 5451 O O . VAL A 1 649 ? 15.031 68.188 44.290 1.00 17.92 ? 690 VAL A O 1 ATOM 5452 C CB . VAL A 1 649 ? 12.110 69.108 45.244 1.00 15.40 ? 690 VAL A CB 1 ATOM 5453 C CG1 . VAL A 1 649 ? 12.878 70.284 44.596 1.00 18.25 ? 690 VAL A CG1 1 ATOM 5454 C CG2 . VAL A 1 649 ? 10.649 69.160 44.783 1.00 17.16 ? 690 VAL A CG2 1 ATOM 5455 N N . ILE A 1 650 ? 14.731 67.121 46.259 1.00 15.94 ? 691 ILE A N 1 ATOM 5456 C CA . ILE A 1 650 ? 16.177 67.128 46.525 1.00 16.99 ? 691 ILE A CA 1 ATOM 5457 C C . ILE A 1 650 ? 16.835 65.898 45.929 1.00 16.97 ? 691 ILE A C 1 ATOM 5458 O O . ILE A 1 650 ? 17.962 65.969 45.463 1.00 18.06 ? 691 ILE A O 1 ATOM 5459 C CB . ILE A 1 650 ? 16.491 67.144 48.035 1.00 17.12 ? 691 ILE A CB 1 ATOM 5460 C CG1 . ILE A 1 650 ? 15.679 68.241 48.768 1.00 17.91 ? 691 ILE A CG1 1 ATOM 5461 C CG2 . ILE A 1 650 ? 18.023 67.386 48.227 1.00 18.75 ? 691 ILE A CG2 1 ATOM 5462 C CD1 . ILE A 1 650 ? 15.798 69.663 48.120 1.00 20.82 ? 691 ILE A CD1 1 ATOM 5463 N N . TYR A 1 651 ? 16.121 64.763 45.948 1.00 17.35 ? 692 TYR A N 1 ATOM 5464 C CA . TYR A 1 651 ? 16.706 63.479 45.479 1.00 17.71 ? 692 TYR A CA 1 ATOM 5465 C C . TYR A 1 651 ? 15.786 62.837 44.491 1.00 18.67 ? 692 TYR A C 1 ATOM 5466 O O . TYR A 1 651 ? 14.554 62.871 44.676 1.00 20.07 ? 692 TYR A O 1 ATOM 5467 C CB . TYR A 1 651 ? 16.821 62.518 46.677 1.00 18.13 ? 692 TYR A CB 1 ATOM 5468 C CG . TYR A 1 651 ? 17.798 62.959 47.736 1.00 16.60 ? 692 TYR A CG 1 ATOM 5469 C CD1 . TYR A 1 651 ? 19.182 63.033 47.425 1.00 18.92 ? 692 TYR A CD1 1 ATOM 5470 C CD2 . TYR A 1 651 ? 17.386 63.274 49.041 1.00 18.77 ? 692 TYR A CD2 1 ATOM 5471 C CE1 . TYR A 1 651 ? 20.096 63.444 48.382 1.00 19.33 ? 692 TYR A CE1 1 ATOM 5472 C CE2 . TYR A 1 651 ? 18.287 63.677 50.000 1.00 20.08 ? 692 TYR A CE2 1 ATOM 5473 C CZ . TYR A 1 651 ? 19.635 63.745 49.668 1.00 20.42 ? 692 TYR A CZ 1 ATOM 5474 O OH . TYR A 1 651 ? 20.614 64.080 50.601 1.00 20.76 ? 692 TYR A OH 1 ATOM 5475 N N . ALA A 1 652 ? 16.334 62.186 43.468 1.00 17.45 ? 693 ALA A N 1 ATOM 5476 C CA . ALA A 1 652 ? 15.528 61.206 42.694 1.00 17.67 ? 693 ALA A CA 1 ATOM 5477 C C . ALA A 1 652 ? 16.503 60.197 42.149 1.00 18.78 ? 693 ALA A C 1 ATOM 5478 O O . ALA A 1 652 ? 17.719 60.419 42.107 1.00 19.46 ? 693 ALA A O 1 ATOM 5479 C CB . ALA A 1 652 ? 14.830 61.881 41.493 1.00 17.99 ? 693 ALA A CB 1 ATOM 5480 N N . PRO A 1 653 ? 15.988 59.040 41.720 1.00 17.63 ? 694 PRO A N 1 ATOM 5481 C CA . PRO A 1 653 ? 16.893 58.120 41.037 1.00 18.39 ? 694 PRO A CA 1 ATOM 5482 C C . PRO A 1 653 ? 17.417 58.767 39.762 1.00 18.13 ? 694 PRO A C 1 ATOM 5483 O O . PRO A 1 653 ? 16.672 59.459 39.064 1.00 19.55 ? 694 PRO A O 1 ATOM 5484 C CB . PRO A 1 653 ? 15.966 56.944 40.658 1.00 17.89 ? 694 PRO A CB 1 ATOM 5485 C CG . PRO A 1 653 ? 14.847 57.060 41.674 1.00 17.46 ? 694 PRO A CG 1 ATOM 5486 C CD . PRO A 1 653 ? 14.597 58.561 41.811 1.00 18.77 ? 694 PRO A CD 1 ATOM 5487 N N . SER A 1 654 ? 18.705 58.587 39.469 1.00 18.17 ? 695 SER A N 1 ATOM 5488 C CA . SER A 1 654 ? 19.296 59.157 38.265 1.00 19.29 ? 695 SER A CA 1 ATOM 5489 C C . SER A 1 654 ? 18.570 58.707 37.021 1.00 20.49 ? 695 SER A C 1 ATOM 5490 O O . SER A 1 654 ? 18.273 57.521 36.859 1.00 20.36 ? 695 SER A O 1 ATOM 5491 C CB . SER A 1 654 ? 20.763 58.696 38.155 1.00 20.11 ? 695 SER A CB 1 ATOM 5492 O OG . SER A 1 654 ? 21.324 59.154 36.938 1.00 22.26 ? 695 SER A OG 1 ATOM 5493 N N . SER A 1 655 ? 18.295 59.635 36.114 1.00 19.87 ? 696 SER A N 1 ATOM 5494 C CA . SER A 1 655 ? 17.634 59.287 34.840 1.00 21.63 ? 696 SER A CA 1 ATOM 5495 C C . SER A 1 655 ? 18.536 58.410 33.952 1.00 21.30 ? 696 SER A C 1 ATOM 5496 O O . SER A 1 655 ? 18.051 57.881 32.948 1.00 24.02 ? 696 SER A O 1 ATOM 5497 C CB . SER A 1 655 ? 17.265 60.587 34.064 1.00 21.30 ? 696 SER A CB 1 ATOM 5498 O OG A SER A 1 655 ? 16.224 61.272 34.745 0.50 15.76 ? 696 SER A OG 1 ATOM 5499 O OG B SER A 1 655 ? 18.412 61.322 33.699 0.50 29.34 ? 696 SER A OG 1 ATOM 5500 N N . HIS A 1 656 ? 19.802 58.279 34.309 1.00 21.91 ? 697 HIS A N 1 ATOM 5501 C CA . HIS A 1 656 ? 20.779 57.440 33.560 1.00 23.10 ? 697 HIS A CA 1 ATOM 5502 C C . HIS A 1 656 ? 21.112 56.163 34.275 1.00 23.53 ? 697 HIS A C 1 ATOM 5503 O O . HIS A 1 656 ? 21.800 55.294 33.734 1.00 24.05 ? 697 HIS A O 1 ATOM 5504 C CB . HIS A 1 656 ? 22.041 58.270 33.265 1.00 24.66 ? 697 HIS A CB 1 ATOM 5505 C CG . HIS A 1 656 ? 21.695 59.565 32.598 1.00 25.43 ? 697 HIS A CG 1 ATOM 5506 N ND1 . HIS A 1 656 ? 21.439 59.657 31.247 1.00 28.94 ? 697 HIS A ND1 1 ATOM 5507 C CD2 . HIS A 1 656 ? 21.465 60.801 33.111 1.00 29.06 ? 697 HIS A CD2 1 ATOM 5508 C CE1 . HIS A 1 656 ? 21.092 60.899 30.951 1.00 32.10 ? 697 HIS A CE1 1 ATOM 5509 N NE2 . HIS A 1 656 ? 21.091 61.612 32.065 1.00 29.04 ? 697 HIS A NE2 1 ATOM 5510 N N . ASN A 1 657 ? 20.658 56.026 35.514 1.00 21.02 ? 698 ASN A N 1 ATOM 5511 C CA . ASN A 1 657 ? 21.042 54.851 36.315 1.00 20.55 ? 698 ASN A CA 1 ATOM 5512 C C . ASN A 1 657 ? 20.160 54.816 37.544 1.00 19.97 ? 698 ASN A C 1 ATOM 5513 O O . ASN A 1 657 ? 20.454 55.470 38.537 1.00 20.76 ? 698 ASN A O 1 ATOM 5514 C CB . ASN A 1 657 ? 22.525 54.946 36.787 1.00 21.47 ? 698 ASN A CB 1 ATOM 5515 C CG . ASN A 1 657 ? 22.927 53.778 37.710 1.00 21.08 ? 698 ASN A CG 1 ATOM 5516 O OD1 . ASN A 1 657 ? 22.171 52.799 37.843 1.00 21.03 ? 698 ASN A OD1 1 ATOM 5517 N ND2 . ASN A 1 657 ? 24.100 53.885 38.352 1.00 21.24 ? 698 ASN A ND2 1 ATOM 5518 N N . LYS A 1 658 ? 19.120 53.995 37.500 1.00 21.12 ? 699 LYS A N 1 ATOM 5519 C CA A LYS A 1 658 ? 18.160 53.945 38.598 0.50 21.04 ? 699 LYS A CA 1 ATOM 5520 C CA B LYS A 1 658 ? 18.141 53.830 38.604 0.50 21.50 ? 699 LYS A CA 1 ATOM 5521 C C . LYS A 1 658 ? 18.777 53.613 39.968 1.00 21.03 ? 699 LYS A C 1 ATOM 5522 O O . LYS A 1 658 ? 18.226 54.025 40.992 1.00 21.66 ? 699 LYS A O 1 ATOM 5523 C CB A LYS A 1 658 ? 17.057 52.957 38.231 0.50 21.63 ? 699 LYS A CB 1 ATOM 5524 C CB B LYS A 1 658 ? 17.212 52.624 38.321 0.50 21.98 ? 699 LYS A CB 1 ATOM 5525 C CG A LYS A 1 658 ? 15.990 52.800 39.228 0.50 24.14 ? 699 LYS A CG 1 ATOM 5526 C CG B LYS A 1 658 ? 16.052 52.914 37.388 0.50 27.24 ? 699 LYS A CG 1 ATOM 5527 C CD A LYS A 1 658 ? 15.015 51.756 38.723 0.50 25.94 ? 699 LYS A CD 1 ATOM 5528 C CD B LYS A 1 658 ? 14.808 53.070 38.190 0.50 30.85 ? 699 LYS A CD 1 ATOM 5529 C CE A LYS A 1 658 ? 13.588 52.098 39.154 0.50 28.06 ? 699 LYS A CE 1 ATOM 5530 C CE B LYS A 1 658 ? 13.560 53.025 37.342 0.50 33.84 ? 699 LYS A CE 1 ATOM 5531 N NZ A LYS A 1 658 ? 12.670 51.042 38.736 0.50 32.68 ? 699 LYS A NZ 1 ATOM 5532 N NZ B LYS A 1 658 ? 12.440 52.638 38.221 0.50 36.06 ? 699 LYS A NZ 1 ATOM 5533 N N . TYR A 1 659 ? 19.933 52.941 39.995 1.00 20.35 ? 700 TYR A N 1 ATOM 5534 C CA . TYR A 1 659 ? 20.542 52.581 41.275 1.00 20.28 ? 700 TYR A CA 1 ATOM 5535 C C . TYR A 1 659 ? 21.167 53.769 41.981 1.00 21.38 ? 700 TYR A C 1 ATOM 5536 O O . TYR A 1 659 ? 21.406 53.687 43.174 1.00 22.75 ? 700 TYR A O 1 ATOM 5537 C CB . TYR A 1 659 ? 21.678 51.584 41.090 1.00 20.65 ? 700 TYR A CB 1 ATOM 5538 C CG . TYR A 1 659 ? 21.247 50.206 40.606 1.00 20.94 ? 700 TYR A CG 1 ATOM 5539 C CD1 . TYR A 1 659 ? 20.093 49.613 41.068 1.00 21.97 ? 700 TYR A CD1 1 ATOM 5540 C CD2 . TYR A 1 659 ? 22.045 49.502 39.705 1.00 22.17 ? 700 TYR A CD2 1 ATOM 5541 C CE1 . TYR A 1 659 ? 19.696 48.314 40.633 1.00 23.18 ? 700 TYR A CE1 1 ATOM 5542 C CE2 . TYR A 1 659 ? 21.670 48.214 39.250 1.00 22.96 ? 700 TYR A CE2 1 ATOM 5543 C CZ . TYR A 1 659 ? 20.513 47.639 39.747 1.00 23.20 ? 700 TYR A CZ 1 ATOM 5544 O OH . TYR A 1 659 ? 20.139 46.376 39.325 1.00 23.41 ? 700 TYR A OH 1 ATOM 5545 N N . ALA A 1 660 ? 21.520 54.816 41.237 1.00 20.08 ? 701 ALA A N 1 ATOM 5546 C CA . ALA A 1 660 ? 22.227 55.953 41.828 1.00 21.05 ? 701 ALA A CA 1 ATOM 5547 C C . ALA A 1 660 ? 21.239 57.050 42.194 1.00 22.07 ? 701 ALA A C 1 ATOM 5548 O O . ALA A 1 660 ? 20.297 57.310 41.438 1.00 22.98 ? 701 ALA A O 1 ATOM 5549 C CB . ALA A 1 660 ? 23.182 56.496 40.798 1.00 21.90 ? 701 ALA A CB 1 ATOM 5550 N N . GLY A 1 661 ? 21.460 57.728 43.307 1.00 20.74 ? 702 GLY A N 1 ATOM 5551 C CA . GLY A 1 661 ? 20.608 58.919 43.592 1.00 21.26 ? 702 GLY A CA 1 ATOM 5552 C C . GLY A 1 661 ? 21.247 60.137 42.934 1.00 21.00 ? 702 GLY A C 1 ATOM 5553 O O . GLY A 1 661 ? 22.480 60.189 42.782 1.00 23.19 ? 702 GLY A O 1 ATOM 5554 N N . GLU A 1 662 ? 20.416 61.085 42.518 1.00 18.90 ? 703 GLU A N 1 ATOM 5555 C CA . GLU A 1 662 ? 20.888 62.336 41.944 1.00 19.30 ? 703 GLU A CA 1 ATOM 5556 C C . GLU A 1 662 ? 20.341 63.448 42.844 1.00 19.07 ? 703 GLU A C 1 ATOM 5557 O O . GLU A 1 662 ? 19.214 63.356 43.275 1.00 20.39 ? 703 GLU A O 1 ATOM 5558 C CB . GLU A 1 662 ? 20.384 62.489 40.510 1.00 19.59 ? 703 GLU A CB 1 ATOM 5559 C CG . GLU A 1 662 ? 20.971 63.752 39.837 1.00 21.76 ? 703 GLU A CG 1 ATOM 5560 C CD . GLU A 1 662 ? 22.498 63.728 39.898 1.00 26.05 ? 703 GLU A CD 1 ATOM 5561 O OE1 . GLU A 1 662 ? 23.089 62.955 39.105 1.00 26.16 ? 703 GLU A OE1 1 ATOM 5562 O OE2 . GLU A 1 662 ? 23.125 64.430 40.778 1.00 28.38 ? 703 GLU A OE2 1 ATOM 5563 N N . SER A 1 663 ? 21.131 64.502 43.087 1.00 19.25 ? 704 SER A N 1 ATOM 5564 C CA A SER A 1 663 ? 20.644 65.643 43.884 0.50 17.77 ? 704 SER A CA 1 ATOM 5565 C CA B SER A 1 663 ? 20.587 65.624 43.879 0.50 19.80 ? 704 SER A CA 1 ATOM 5566 C C . SER A 1 663 ? 20.115 66.737 42.972 1.00 18.90 ? 704 SER A C 1 ATOM 5567 O O . SER A 1 663 ? 20.602 66.875 41.830 1.00 19.05 ? 704 SER A O 1 ATOM 5568 C CB A SER A 1 663 ? 21.747 66.200 44.812 0.50 18.30 ? 704 SER A CB 1 ATOM 5569 C CB B SER A 1 663 ? 21.605 66.187 44.868 0.50 20.68 ? 704 SER A CB 1 ATOM 5570 O OG A SER A 1 663 ? 23.003 66.395 44.153 0.50 13.07 ? 704 SER A OG 1 ATOM 5571 O OG B SER A 1 663 ? 22.540 65.206 45.242 0.50 28.14 ? 704 SER A OG 1 ATOM 5572 N N . PHE A 1 664 ? 19.137 67.522 43.483 1.00 17.99 ? 705 PHE A N 1 ATOM 5573 C CA . PHE A 1 664 ? 18.452 68.556 42.651 1.00 17.86 ? 705 PHE A CA 1 ATOM 5574 C C . PHE A 1 664 ? 18.198 67.973 41.242 1.00 18.43 ? 705 PHE A C 1 ATOM 5575 O O . PHE A 1 664 ? 18.538 68.583 40.240 1.00 18.37 ? 705 PHE A O 1 ATOM 5576 C CB . PHE A 1 664 ? 19.247 69.896 42.609 1.00 17.94 ? 705 PHE A CB 1 ATOM 5577 C CG . PHE A 1 664 ? 19.155 70.651 43.902 1.00 17.91 ? 705 PHE A CG 1 ATOM 5578 C CD1 . PHE A 1 664 ? 17.883 70.936 44.452 1.00 17.23 ? 705 PHE A CD1 1 ATOM 5579 C CD2 . PHE A 1 664 ? 20.296 71.060 44.565 1.00 19.95 ? 705 PHE A CD2 1 ATOM 5580 C CE1 . PHE A 1 664 ? 17.746 71.605 45.696 1.00 18.06 ? 705 PHE A CE1 1 ATOM 5581 C CE2 . PHE A 1 664 ? 20.181 71.751 45.800 1.00 19.89 ? 705 PHE A CE2 1 ATOM 5582 C CZ . PHE A 1 664 ? 18.893 72.024 46.363 1.00 18.83 ? 705 PHE A CZ 1 ATOM 5583 N N . PRO A 1 665 ? 17.498 66.830 41.185 1.00 17.21 ? 706 PRO A N 1 ATOM 5584 C CA . PRO A 1 665 ? 17.321 66.122 39.909 1.00 17.92 ? 706 PRO A CA 1 ATOM 5585 C C . PRO A 1 665 ? 16.621 66.940 38.853 1.00 17.70 ? 706 PRO A C 1 ATOM 5586 O O . PRO A 1 665 ? 16.931 66.756 37.675 1.00 19.30 ? 706 PRO A O 1 ATOM 5587 C CB . PRO A 1 665 ? 16.454 64.878 40.297 1.00 16.85 ? 706 PRO A CB 1 ATOM 5588 C CG . PRO A 1 665 ? 15.749 65.299 41.633 1.00 18.94 ? 706 PRO A CG 1 ATOM 5589 C CD . PRO A 1 665 ? 16.888 66.105 42.326 1.00 17.06 ? 706 PRO A CD 1 ATOM 5590 N N . GLY A 1 666 ? 15.667 67.808 39.237 1.00 18.09 ? 707 GLY A N 1 ATOM 5591 C CA . GLY A 1 666 ? 14.948 68.557 38.187 1.00 17.88 ? 707 GLY A CA 1 ATOM 5592 C C . GLY A 1 666 ? 15.917 69.518 37.504 1.00 18.50 ? 707 GLY A C 1 ATOM 5593 O O . GLY A 1 666 ? 15.897 69.660 36.257 1.00 18.84 ? 707 GLY A O 1 ATOM 5594 N N . ILE A 1 667 ? 16.792 70.176 38.290 1.00 17.00 ? 708 ILE A N 1 ATOM 5595 C CA . ILE A 1 667 ? 17.791 71.068 37.662 1.00 18.38 ? 708 ILE A CA 1 ATOM 5596 C C . ILE A 1 667 ? 18.841 70.235 36.892 1.00 19.16 ? 708 ILE A C 1 ATOM 5597 O O . ILE A 1 667 ? 19.219 70.588 35.768 1.00 20.55 ? 708 ILE A O 1 ATOM 5598 C CB . ILE A 1 667 ? 18.498 71.984 38.685 1.00 16.76 ? 708 ILE A CB 1 ATOM 5599 C CG1 . ILE A 1 667 ? 17.480 72.685 39.592 1.00 20.03 ? 708 ILE A CG1 1 ATOM 5600 C CG2 . ILE A 1 667 ? 19.303 73.043 37.908 1.00 19.92 ? 708 ILE A CG2 1 ATOM 5601 C CD1 . ILE A 1 667 ? 18.173 73.440 40.777 1.00 20.86 ? 708 ILE A CD1 1 ATOM 5602 N N . TYR A 1 668 ? 19.279 69.129 37.490 1.00 19.64 ? 709 TYR A N 1 ATOM 5603 C CA . TYR A 1 668 ? 20.309 68.299 36.886 1.00 21.31 ? 709 TYR A CA 1 ATOM 5604 C C . TYR A 1 668 ? 19.824 67.846 35.492 1.00 20.13 ? 709 TYR A C 1 ATOM 5605 O O . TYR A 1 668 ? 20.562 67.966 34.509 1.00 20.70 ? 709 TYR A O 1 ATOM 5606 C CB . TYR A 1 668 ? 20.624 67.089 37.760 1.00 19.06 ? 709 TYR A CB 1 ATOM 5607 C CG . TYR A 1 668 ? 21.737 66.277 37.124 1.00 21.02 ? 709 TYR A CG 1 ATOM 5608 C CD1 . TYR A 1 668 ? 23.076 66.503 37.479 1.00 22.84 ? 709 TYR A CD1 1 ATOM 5609 C CD2 . TYR A 1 668 ? 21.438 65.327 36.125 1.00 22.20 ? 709 TYR A CD2 1 ATOM 5610 C CE1 . TYR A 1 668 ? 24.137 65.767 36.855 1.00 23.44 ? 709 TYR A CE1 1 ATOM 5611 C CE2 . TYR A 1 668 ? 22.463 64.613 35.489 1.00 22.85 ? 709 TYR A CE2 1 ATOM 5612 C CZ . TYR A 1 668 ? 23.792 64.838 35.871 1.00 25.76 ? 709 TYR A CZ 1 ATOM 5613 O OH . TYR A 1 668 ? 24.789 64.107 35.247 1.00 26.40 ? 709 TYR A OH 1 ATOM 5614 N N . ASP A 1 669 ? 18.609 67.310 35.412 1.00 20.84 ? 710 ASP A N 1 ATOM 5615 C CA . ASP A 1 669 ? 18.128 66.841 34.115 1.00 21.10 ? 710 ASP A CA 1 ATOM 5616 C C . ASP A 1 669 ? 17.914 67.985 33.109 1.00 21.64 ? 710 ASP A C 1 ATOM 5617 O O . ASP A 1 669 ? 18.163 67.810 31.897 1.00 23.40 ? 710 ASP A O 1 ATOM 5618 C CB . ASP A 1 669 ? 16.857 66.018 34.296 1.00 21.37 ? 710 ASP A CB 1 ATOM 5619 C CG . ASP A 1 669 ? 17.151 64.605 34.809 1.00 25.24 ? 710 ASP A CG 1 ATOM 5620 O OD1 . ASP A 1 669 ? 18.317 64.138 34.786 1.00 24.67 ? 710 ASP A OD1 1 ATOM 5621 O OD2 . ASP A 1 669 ? 16.191 63.926 35.224 1.00 26.55 ? 710 ASP A OD2 1 ATOM 5622 N N . ALA A 1 670 ? 17.486 69.161 33.590 1.00 19.56 ? 711 ALA A N 1 ATOM 5623 C CA . ALA A 1 670 ? 17.339 70.321 32.676 1.00 20.54 ? 711 ALA A CA 1 ATOM 5624 C C . ALA A 1 670 ? 18.694 70.738 32.066 1.00 21.65 ? 711 ALA A C 1 ATOM 5625 O O . ALA A 1 670 ? 18.763 71.190 30.910 1.00 22.23 ? 711 ALA A O 1 ATOM 5626 C CB . ALA A 1 670 ? 16.701 71.540 33.416 1.00 21.74 ? 711 ALA A CB 1 ATOM 5627 N N . LEU A 1 671 ? 19.766 70.578 32.833 1.00 21.53 ? 712 LEU A N 1 ATOM 5628 C CA . LEU A 1 671 ? 21.123 70.948 32.378 1.00 21.59 ? 712 LEU A CA 1 ATOM 5629 C C . LEU A 1 671 ? 21.836 69.864 31.553 1.00 22.29 ? 712 LEU A C 1 ATOM 5630 O O . LEU A 1 671 ? 22.781 70.144 30.846 1.00 24.97 ? 712 LEU A O 1 ATOM 5631 C CB . LEU A 1 671 ? 21.989 71.275 33.609 1.00 23.05 ? 712 LEU A CB 1 ATOM 5632 C CG . LEU A 1 671 ? 21.684 72.654 34.214 1.00 21.94 ? 712 LEU A CG 1 ATOM 5633 C CD1 . LEU A 1 671 ? 22.375 72.704 35.596 1.00 23.23 ? 712 LEU A CD1 1 ATOM 5634 C CD2 . LEU A 1 671 ? 22.248 73.730 33.269 1.00 22.98 ? 712 LEU A CD2 1 ATOM 5635 N N . PHE A 1 672 ? 21.375 68.614 31.691 1.00 21.83 ? 713 PHE A N 1 ATOM 5636 C CA . PHE A 1 672 ? 22.142 67.501 31.115 1.00 23.49 ? 713 PHE A CA 1 ATOM 5637 C C . PHE A 1 672 ? 22.164 67.599 29.593 1.00 24.15 ? 713 PHE A C 1 ATOM 5638 O O . PHE A 1 672 ? 21.092 67.690 28.960 1.00 25.46 ? 713 PHE A O 1 ATOM 5639 C CB . PHE A 1 672 ? 21.548 66.143 31.534 1.00 23.02 ? 713 PHE A CB 1 ATOM 5640 C CG . PHE A 1 672 ? 22.389 64.989 31.046 1.00 25.21 ? 713 PHE A CG 1 ATOM 5641 C CD1 . PHE A 1 672 ? 23.559 64.636 31.740 1.00 27.28 ? 713 PHE A CD1 1 ATOM 5642 C CD2 . PHE A 1 672 ? 22.069 64.350 29.848 1.00 26.73 ? 713 PHE A CD2 1 ATOM 5643 C CE1 . PHE A 1 672 ? 24.377 63.600 31.262 1.00 30.23 ? 713 PHE A CE1 1 ATOM 5644 C CE2 . PHE A 1 672 ? 22.897 63.310 29.341 1.00 29.08 ? 713 PHE A CE2 1 ATOM 5645 C CZ . PHE A 1 672 ? 24.042 62.945 30.046 1.00 29.80 ? 713 PHE A CZ 1 ATOM 5646 N N . ASP A 1 673 ? 23.374 67.583 29.015 1.00 25.92 ? 714 ASP A N 1 ATOM 5647 C CA . ASP A 1 673 ? 23.537 67.627 27.544 1.00 28.43 ? 714 ASP A CA 1 ATOM 5648 C C . ASP A 1 673 ? 22.838 68.849 26.938 1.00 30.10 ? 714 ASP A C 1 ATOM 5649 O O . ASP A 1 673 ? 22.371 68.801 25.797 1.00 30.91 ? 714 ASP A O 1 ATOM 5650 C CB . ASP A 1 673 ? 22.992 66.318 26.917 1.00 28.33 ? 714 ASP A CB 1 ATOM 5651 C CG . ASP A 1 673 ? 23.452 66.120 25.461 1.00 31.66 ? 714 ASP A CG 1 ATOM 5652 O OD1 . ASP A 1 673 ? 24.633 66.442 25.147 1.00 34.15 ? 714 ASP A OD1 1 ATOM 5653 O OD2 . ASP A 1 673 ? 22.613 65.627 24.654 1.00 34.46 ? 714 ASP A OD2 1 ATOM 5654 N N . ILE A 1 674 ? 22.780 69.963 27.684 1.00 29.05 ? 715 ILE A N 1 ATOM 5655 C CA . ILE A 1 674 ? 21.978 71.115 27.225 1.00 28.93 ? 715 ILE A CA 1 ATOM 5656 C C . ILE A 1 674 ? 22.561 71.746 25.954 1.00 31.50 ? 715 ILE A C 1 ATOM 5657 O O . ILE A 1 674 ? 21.811 72.331 25.158 1.00 31.00 ? 715 ILE A O 1 ATOM 5658 C CB . ILE A 1 674 ? 21.776 72.173 28.360 1.00 28.42 ? 715 ILE A CB 1 ATOM 5659 C CG1 . ILE A 1 674 ? 20.738 73.220 27.948 1.00 27.27 ? 715 ILE A CG1 1 ATOM 5660 C CG2 . ILE A 1 674 ? 23.102 72.758 28.833 1.00 28.48 ? 715 ILE A CG2 1 ATOM 5661 C CD1 . ILE A 1 674 ? 20.248 74.009 29.135 1.00 26.23 ? 715 ILE A CD1 1 ATOM 5662 N N . GLU A 1 675 ? 23.873 71.604 25.771 1.00 32.69 ? 716 GLU A N 1 ATOM 5663 C CA . GLU A 1 675 ? 24.545 72.161 24.583 1.00 36.64 ? 716 GLU A CA 1 ATOM 5664 C C . GLU A 1 675 ? 24.096 71.497 23.272 1.00 37.82 ? 716 GLU A C 1 ATOM 5665 O O . GLU A 1 675 ? 24.366 72.025 22.174 1.00 39.44 ? 716 GLU A O 1 ATOM 5666 C CB . GLU A 1 675 ? 26.073 72.118 24.741 1.00 37.07 ? 716 GLU A CB 1 ATOM 5667 C CG . GLU A 1 675 ? 26.717 70.726 24.652 1.00 39.27 ? 716 GLU A CG 1 ATOM 5668 C CD . GLU A 1 675 ? 26.747 69.948 25.974 1.00 42.23 ? 716 GLU A CD 1 ATOM 5669 O OE1 . GLU A 1 675 ? 26.014 70.280 26.951 1.00 37.96 ? 716 GLU A OE1 1 ATOM 5670 O OE2 . GLU A 1 675 ? 27.517 68.961 26.019 1.00 47.02 ? 716 GLU A OE2 1 ATOM 5671 N N . SER A 1 676 ? 23.403 70.367 23.381 1.00 37.96 ? 717 SER A N 1 ATOM 5672 C CA . SER A 1 676 ? 22.858 69.650 22.224 1.00 39.70 ? 717 SER A CA 1 ATOM 5673 C C . SER A 1 676 ? 21.406 69.967 21.936 1.00 40.61 ? 717 SER A C 1 ATOM 5674 O O . SER A 1 676 ? 20.877 69.502 20.929 1.00 42.15 ? 717 SER A O 1 ATOM 5675 C CB . SER A 1 676 ? 23.027 68.132 22.409 1.00 39.53 ? 717 SER A CB 1 ATOM 5676 O OG . SER A 1 676 ? 24.411 67.854 22.567 1.00 41.27 ? 717 SER A OG 1 ATOM 5677 N N . LYS A 1 677 ? 20.753 70.769 22.781 1.00 39.35 ? 718 LYS A N 1 ATOM 5678 C CA . LYS A 1 677 ? 19.348 71.106 22.539 1.00 40.25 ? 718 LYS A CA 1 ATOM 5679 C C . LYS A 1 677 ? 19.214 72.119 21.407 1.00 42.01 ? 718 LYS A C 1 ATOM 5680 O O . LYS A 1 677 ? 20.006 73.065 21.303 1.00 42.90 ? 718 LYS A O 1 ATOM 5681 C CB . LYS A 1 677 ? 18.666 71.640 23.803 1.00 39.14 ? 718 LYS A CB 1 ATOM 5682 C CG . LYS A 1 677 ? 18.648 70.650 24.953 1.00 40.66 ? 718 LYS A CG 1 ATOM 5683 C CD . LYS A 1 677 ? 17.890 69.372 24.608 1.00 44.15 ? 718 LYS A CD 1 ATOM 5684 C CE . LYS A 1 677 ? 17.989 68.351 25.760 1.00 45.52 ? 718 LYS A CE 1 ATOM 5685 N NZ . LYS A 1 677 ? 17.217 68.781 26.981 1.00 45.13 ? 718 LYS A NZ 1 ATOM 5686 N N . VAL A 1 678 ? 18.209 71.930 20.557 1.00 42.87 ? 719 VAL A N 1 ATOM 5687 C CA . VAL A 1 678 ? 18.097 72.783 19.362 1.00 44.32 ? 719 VAL A CA 1 ATOM 5688 C C . VAL A 1 678 ? 17.568 74.190 19.649 1.00 43.92 ? 719 VAL A C 1 ATOM 5689 O O . VAL A 1 678 ? 17.839 75.120 18.885 1.00 45.40 ? 719 VAL A O 1 ATOM 5690 C CB . VAL A 1 678 ? 17.241 72.131 18.250 1.00 45.17 ? 719 VAL A CB 1 ATOM 5691 C CG1 . VAL A 1 678 ? 18.013 70.973 17.605 1.00 47.15 ? 719 VAL A CG1 1 ATOM 5692 C CG2 . VAL A 1 678 ? 15.872 71.684 18.801 1.00 45.41 ? 719 VAL A CG2 1 ATOM 5693 N N . ASP A 1 679 ? 16.811 74.330 20.741 1.00 41.76 ? 720 ASP A N 1 ATOM 5694 C CA . ASP A 1 679 ? 16.222 75.610 21.132 1.00 40.74 ? 720 ASP A CA 1 ATOM 5695 C C . ASP A 1 679 ? 16.804 75.990 22.498 1.00 38.72 ? 720 ASP A C 1 ATOM 5696 O O . ASP A 1 679 ? 16.219 75.636 23.539 1.00 37.68 ? 720 ASP A O 1 ATOM 5697 C CB . ASP A 1 679 ? 14.698 75.462 21.243 1.00 40.46 ? 720 ASP A CB 1 ATOM 5698 C CG . ASP A 1 679 ? 13.986 76.795 21.435 1.00 43.14 ? 720 ASP A CG 1 ATOM 5699 O OD1 . ASP A 1 679 ? 14.640 77.815 21.741 1.00 45.40 ? 720 ASP A OD1 1 ATOM 5700 O OD2 . ASP A 1 679 ? 12.751 76.831 21.267 1.00 48.36 ? 720 ASP A OD2 1 ATOM 5701 N N . PRO A 1 680 ? 17.945 76.700 22.507 1.00 37.92 ? 721 PRO A N 1 ATOM 5702 C CA . PRO A 1 680 ? 18.619 77.004 23.775 1.00 36.77 ? 721 PRO A CA 1 ATOM 5703 C C . PRO A 1 680 ? 17.765 77.903 24.675 1.00 35.51 ? 721 PRO A C 1 ATOM 5704 O O . PRO A 1 680 ? 17.834 77.775 25.898 1.00 33.46 ? 721 PRO A O 1 ATOM 5705 C CB . PRO A 1 680 ? 19.909 77.721 23.361 1.00 38.07 ? 721 PRO A CB 1 ATOM 5706 C CG . PRO A 1 680 ? 20.005 77.619 21.853 1.00 39.97 ? 721 PRO A CG 1 ATOM 5707 C CD . PRO A 1 680 ? 18.640 77.283 21.334 1.00 39.88 ? 721 PRO A CD 1 ATOM 5708 N N . SER A 1 681 ? 16.973 78.798 24.076 1.00 35.48 ? 722 SER A N 1 ATOM 5709 C CA . SER A 1 681 ? 16.061 79.655 24.859 1.00 35.36 ? 722 SER A CA 1 ATOM 5710 C C . SER A 1 681 ? 15.099 78.828 25.694 1.00 33.35 ? 722 SER A C 1 ATOM 5711 O O . SER A 1 681 ? 14.954 79.058 26.895 1.00 31.39 ? 722 SER A O 1 ATOM 5712 C CB . SER A 1 681 ? 15.267 80.612 23.962 1.00 37.19 ? 722 SER A CB 1 ATOM 5713 O OG . SER A 1 681 ? 14.521 81.501 24.788 1.00 40.55 ? 722 SER A OG 1 ATOM 5714 N N . LYS A 1 682 ? 14.440 77.867 25.056 1.00 31.42 ? 723 LYS A N 1 ATOM 5715 C CA A LYS A 1 682 ? 13.509 76.978 25.728 0.50 30.84 ? 723 LYS A CA 1 ATOM 5716 C CA B LYS A 1 682 ? 13.501 77.027 25.774 0.50 31.16 ? 723 LYS A CA 1 ATOM 5717 C C . LYS A 1 682 ? 14.212 76.147 26.803 1.00 29.28 ? 723 LYS A C 1 ATOM 5718 O O . LYS A 1 682 ? 13.706 75.985 27.920 1.00 28.50 ? 723 LYS A O 1 ATOM 5719 C CB A LYS A 1 682 ? 12.859 76.050 24.693 0.50 31.61 ? 723 LYS A CB 1 ATOM 5720 C CB B LYS A 1 682 ? 12.638 76.201 24.807 0.50 32.07 ? 723 LYS A CB 1 ATOM 5721 C CG A LYS A 1 682 ? 11.753 75.174 25.260 0.50 31.16 ? 723 LYS A CG 1 ATOM 5722 C CG B LYS A 1 682 ? 11.345 76.906 24.402 0.50 34.69 ? 723 LYS A CG 1 ATOM 5723 C CD A LYS A 1 682 ? 11.135 74.292 24.179 0.50 34.78 ? 723 LYS A CD 1 ATOM 5724 C CD B LYS A 1 682 ? 10.490 76.061 23.451 0.50 37.41 ? 723 LYS A CD 1 ATOM 5725 C CE A LYS A 1 682 ? 9.996 73.446 24.741 0.50 35.47 ? 723 LYS A CE 1 ATOM 5726 C CE B LYS A 1 682 ? 9.381 76.892 22.816 0.50 38.89 ? 723 LYS A CE 1 ATOM 5727 N NZ A LYS A 1 682 ? 9.479 72.507 23.695 0.50 38.62 ? 723 LYS A NZ 1 ATOM 5728 N NZ B LYS A 1 682 ? 8.844 76.234 21.591 0.50 41.77 ? 723 LYS A NZ 1 ATOM 5729 N N . ALA A 1 683 ? 15.383 75.609 26.440 1.00 28.32 ? 724 ALA A N 1 ATOM 5730 C CA . ALA A 1 683 ? 16.128 74.698 27.335 1.00 26.76 ? 724 ALA A CA 1 ATOM 5731 C C . ALA A 1 683 ? 16.604 75.463 28.595 1.00 25.21 ? 724 ALA A C 1 ATOM 5732 O O . ALA A 1 683 ? 16.459 74.968 29.714 1.00 23.96 ? 724 ALA A O 1 ATOM 5733 C CB . ALA A 1 683 ? 17.333 74.151 26.582 1.00 28.27 ? 724 ALA A CB 1 ATOM 5734 N N . TRP A 1 684 ? 17.161 76.659 28.397 1.00 24.69 ? 725 TRP A N 1 ATOM 5735 C CA . TRP A 1 684 ? 17.608 77.460 29.560 1.00 24.75 ? 725 TRP A CA 1 ATOM 5736 C C . TRP A 1 684 ? 16.423 77.994 30.354 1.00 24.75 ? 725 TRP A C 1 ATOM 5737 O O . TRP A 1 684 ? 16.493 78.142 31.597 1.00 23.44 ? 725 TRP A O 1 ATOM 5738 C CB . TRP A 1 684 ? 18.587 78.542 29.125 1.00 25.31 ? 725 TRP A CB 1 ATOM 5739 C CG . TRP A 1 684 ? 19.938 77.917 28.877 1.00 25.41 ? 725 TRP A CG 1 ATOM 5740 C CD1 . TRP A 1 684 ? 20.472 77.559 27.657 1.00 27.98 ? 725 TRP A CD1 1 ATOM 5741 C CD2 . TRP A 1 684 ? 20.904 77.531 29.867 1.00 24.58 ? 725 TRP A CD2 1 ATOM 5742 N NE1 . TRP A 1 684 ? 21.723 77.006 27.831 1.00 29.29 ? 725 TRP A NE1 1 ATOM 5743 C CE2 . TRP A 1 684 ? 22.000 76.953 29.177 1.00 25.87 ? 725 TRP A CE2 1 ATOM 5744 C CE3 . TRP A 1 684 ? 20.944 77.600 31.280 1.00 25.27 ? 725 TRP A CE3 1 ATOM 5745 C CZ2 . TRP A 1 684 ? 23.142 76.477 29.839 1.00 25.80 ? 725 TRP A CZ2 1 ATOM 5746 C CZ3 . TRP A 1 684 ? 22.083 77.122 31.945 1.00 25.47 ? 725 TRP A CZ3 1 ATOM 5747 C CH2 . TRP A 1 684 ? 23.166 76.557 31.227 1.00 25.13 ? 725 TRP A CH2 1 ATOM 5748 N N . GLY A 1 685 ? 15.311 78.265 29.672 1.00 24.75 ? 726 GLY A N 1 ATOM 5749 C CA . GLY A 1 685 ? 14.077 78.612 30.399 1.00 24.24 ? 726 GLY A CA 1 ATOM 5750 C C . GLY A 1 685 ? 13.651 77.526 31.387 1.00 23.43 ? 726 GLY A C 1 ATOM 5751 O O . GLY A 1 685 ? 13.206 77.812 32.513 1.00 23.57 ? 726 GLY A O 1 ATOM 5752 N N . GLU A 1 686 ? 13.774 76.272 30.956 1.00 22.56 ? 727 GLU A N 1 ATOM 5753 C CA A GLU A 1 686 ? 13.402 75.169 31.824 0.50 21.20 ? 727 GLU A CA 1 ATOM 5754 C CA B GLU A 1 686 ? 13.456 75.120 31.781 0.50 22.59 ? 727 GLU A CA 1 ATOM 5755 C C . GLU A 1 686 ? 14.424 74.984 32.953 1.00 20.47 ? 727 GLU A C 1 ATOM 5756 O O . GLU A 1 686 ? 14.037 74.613 34.049 1.00 20.94 ? 727 GLU A O 1 ATOM 5757 C CB A GLU A 1 686 ? 13.192 73.890 31.014 0.50 21.79 ? 727 GLU A CB 1 ATOM 5758 C CB B GLU A 1 686 ? 13.476 73.876 30.898 0.50 23.45 ? 727 GLU A CB 1 ATOM 5759 C CG A GLU A 1 686 ? 12.884 72.660 31.865 0.50 17.95 ? 727 GLU A CG 1 ATOM 5760 C CG B GLU A 1 686 ? 12.239 73.797 30.022 0.50 28.47 ? 727 GLU A CG 1 ATOM 5761 C CD A GLU A 1 686 ? 11.532 72.696 32.584 0.50 18.39 ? 727 GLU A CD 1 ATOM 5762 C CD B GLU A 1 686 ? 10.964 74.139 30.792 0.50 33.18 ? 727 GLU A CD 1 ATOM 5763 O OE1 A GLU A 1 686 ? 10.713 73.622 32.368 0.50 22.70 ? 727 GLU A OE1 1 ATOM 5764 O OE1 B GLU A 1 686 ? 10.740 73.545 31.867 0.50 34.48 ? 727 GLU A OE1 1 ATOM 5765 O OE2 A GLU A 1 686 ? 11.314 71.785 33.394 0.50 19.97 ? 727 GLU A OE2 1 ATOM 5766 O OE2 B GLU A 1 686 ? 10.189 75.016 30.329 0.50 35.75 ? 727 GLU A OE2 1 ATOM 5767 N N . VAL A 1 687 ? 15.714 75.275 32.705 1.00 21.22 ? 728 VAL A N 1 ATOM 5768 C CA . VAL A 1 687 ? 16.662 75.316 33.832 1.00 20.39 ? 728 VAL A CA 1 ATOM 5769 C C . VAL A 1 687 ? 16.198 76.345 34.880 1.00 20.49 ? 728 VAL A C 1 ATOM 5770 O O . VAL A 1 687 ? 16.167 76.051 36.067 1.00 19.04 ? 728 VAL A O 1 ATOM 5771 C CB . VAL A 1 687 ? 18.104 75.666 33.348 1.00 21.14 ? 728 VAL A CB 1 ATOM 5772 C CG1 . VAL A 1 687 ? 19.073 75.892 34.586 1.00 22.73 ? 728 VAL A CG1 1 ATOM 5773 C CG2 . VAL A 1 687 ? 18.627 74.565 32.379 1.00 21.02 ? 728 VAL A CG2 1 ATOM 5774 N N . LYS A 1 688 ? 15.859 77.548 34.423 1.00 21.05 ? 729 LYS A N 1 ATOM 5775 C CA . LYS A 1 688 ? 15.375 78.587 35.352 1.00 20.74 ? 729 LYS A CA 1 ATOM 5776 C C . LYS A 1 688 ? 14.100 78.152 36.073 1.00 21.05 ? 729 LYS A C 1 ATOM 5777 O O . LYS A 1 688 ? 13.949 78.398 37.274 1.00 20.22 ? 729 LYS A O 1 ATOM 5778 C CB B LYS A 1 688 ? 15.111 79.882 34.597 0.65 21.10 ? 729 LYS A CB 1 ATOM 5779 C CB C LYS A 1 688 ? 15.160 79.902 34.616 0.35 21.63 ? 729 LYS A CB 1 ATOM 5780 C CG B LYS A 1 688 ? 16.437 80.511 34.091 0.65 21.83 ? 729 LYS A CG 1 ATOM 5781 C CG C LYS A 1 688 ? 16.485 80.483 34.104 0.35 22.66 ? 729 LYS A CG 1 ATOM 5782 C CD B LYS A 1 688 ? 16.222 81.783 33.257 0.65 23.22 ? 729 LYS A CD 1 ATOM 5783 C CD C LYS A 1 688 ? 16.299 81.856 33.488 0.35 24.68 ? 729 LYS A CD 1 ATOM 5784 C CE B LYS A 1 688 ? 15.671 82.964 34.068 0.65 23.66 ? 729 LYS A CE 1 ATOM 5785 C CE C LYS A 1 688 ? 15.549 81.770 32.175 0.35 26.68 ? 729 LYS A CE 1 ATOM 5786 N NZ B LYS A 1 688 ? 15.821 84.253 33.295 0.65 27.37 ? 729 LYS A NZ 1 ATOM 5787 N NZ C LYS A 1 688 ? 15.594 83.082 31.467 0.35 28.47 ? 729 LYS A NZ 1 ATOM 5788 N N . ARG A 1 689 ? 13.187 77.500 35.356 1.00 19.19 ? 730 ARG A N 1 ATOM 5789 C CA . ARG A 1 689 ? 12.010 76.981 36.047 1.00 18.56 ? 730 ARG A CA 1 ATOM 5790 C C . ARG A 1 689 ? 12.336 76.021 37.181 1.00 18.28 ? 730 ARG A C 1 ATOM 5791 O O . ARG A 1 689 ? 11.779 76.115 38.288 1.00 17.63 ? 730 ARG A O 1 ATOM 5792 C CB . ARG A 1 689 ? 11.037 76.329 35.044 1.00 19.32 ? 730 ARG A CB 1 ATOM 5793 C CG . ARG A 1 689 ? 9.681 76.105 35.730 1.00 21.44 ? 730 ARG A CG 1 ATOM 5794 C CD . ARG A 1 689 ? 8.639 75.523 34.756 1.00 24.61 ? 730 ARG A CD 1 ATOM 5795 N NE . ARG A 1 689 ? 8.878 74.128 34.474 1.00 26.26 ? 730 ARG A NE 1 ATOM 5796 C CZ . ARG A 1 689 ? 8.408 73.136 35.236 1.00 29.69 ? 730 ARG A CZ 1 ATOM 5797 N NH1 . ARG A 1 689 ? 7.725 73.404 36.362 1.00 30.13 ? 730 ARG A NH1 1 ATOM 5798 N NH2 . ARG A 1 689 ? 8.664 71.877 34.901 1.00 31.00 ? 730 ARG A NH2 1 ATOM 5799 N N . GLN A 1 690 ? 13.248 75.102 36.906 1.00 18.02 ? 731 GLN A N 1 ATOM 5800 C CA . GLN A 1 690 ? 13.686 74.131 37.924 1.00 18.23 ? 731 GLN A CA 1 ATOM 5801 C C . GLN A 1 690 ? 14.449 74.779 39.086 1.00 18.73 ? 731 GLN A C 1 ATOM 5802 O O . GLN A 1 690 ? 14.300 74.309 40.233 1.00 17.70 ? 731 GLN A O 1 ATOM 5803 C CB . GLN A 1 690 ? 14.519 73.022 37.289 1.00 19.22 ? 731 GLN A CB 1 ATOM 5804 C CG . GLN A 1 690 ? 13.658 72.230 36.265 1.00 18.64 ? 731 GLN A CG 1 ATOM 5805 C CD . GLN A 1 690 ? 12.504 71.503 36.942 1.00 21.38 ? 731 GLN A CD 1 ATOM 5806 O OE1 . GLN A 1 690 ? 12.612 71.037 38.077 1.00 20.45 ? 731 GLN A OE1 1 ATOM 5807 N NE2 . GLN A 1 690 ? 11.358 71.458 36.257 1.00 27.12 ? 731 GLN A NE2 1 ATOM 5808 N N . ILE A 1 691 ? 15.224 75.841 38.818 1.00 17.94 ? 732 ILE A N 1 ATOM 5809 C CA . ILE A 1 691 ? 15.836 76.570 39.943 1.00 18.40 ? 732 ILE A CA 1 ATOM 5810 C C . ILE A 1 691 ? 14.752 77.158 40.848 1.00 18.70 ? 732 ILE A C 1 ATOM 5811 O O . ILE A 1 691 ? 14.825 77.039 42.075 1.00 20.46 ? 732 ILE A O 1 ATOM 5812 C CB . ILE A 1 691 ? 16.765 77.683 39.419 1.00 18.81 ? 732 ILE A CB 1 ATOM 5813 C CG1 . ILE A 1 691 ? 17.963 77.058 38.706 1.00 19.78 ? 732 ILE A CG1 1 ATOM 5814 C CG2 . ILE A 1 691 ? 17.238 78.613 40.567 1.00 20.57 ? 732 ILE A CG2 1 ATOM 5815 C CD1 . ILE A 1 691 ? 18.789 78.122 37.931 1.00 20.87 ? 732 ILE A CD1 1 ATOM 5816 N N . TYR A 1 692 ? 13.739 77.781 40.236 1.00 18.13 ? 733 TYR A N 1 ATOM 5817 C CA . TYR A 1 692 ? 12.590 78.329 41.018 1.00 19.62 ? 733 TYR A CA 1 ATOM 5818 C C . TYR A 1 692 ? 11.881 77.253 41.831 1.00 18.45 ? 733 TYR A C 1 ATOM 5819 O O . TYR A 1 692 ? 11.598 77.466 43.019 1.00 18.20 ? 733 TYR A O 1 ATOM 5820 C CB . TYR A 1 692 ? 11.625 78.985 40.063 1.00 18.91 ? 733 TYR A CB 1 ATOM 5821 C CG . TYR A 1 692 ? 10.164 79.238 40.441 1.00 23.07 ? 733 TYR A CG 1 ATOM 5822 C CD1 . TYR A 1 692 ? 9.822 79.979 41.575 1.00 25.56 ? 733 TYR A CD1 1 ATOM 5823 C CD2 . TYR A 1 692 ? 9.122 78.840 39.560 1.00 25.11 ? 733 TYR A CD2 1 ATOM 5824 C CE1 . TYR A 1 692 ? 8.451 80.289 41.850 1.00 25.68 ? 733 TYR A CE1 1 ATOM 5825 C CE2 . TYR A 1 692 ? 7.799 79.147 39.802 1.00 23.96 ? 733 TYR A CE2 1 ATOM 5826 C CZ . TYR A 1 692 ? 7.461 79.878 40.957 1.00 26.53 ? 733 TYR A CZ 1 ATOM 5827 O OH . TYR A 1 692 ? 6.114 80.229 41.191 1.00 28.36 ? 733 TYR A OH 1 ATOM 5828 N N . VAL A 1 693 ? 11.560 76.123 41.208 1.00 17.07 ? 734 VAL A N 1 ATOM 5829 C CA . VAL A 1 693 ? 10.902 75.062 41.983 1.00 16.72 ? 734 VAL A CA 1 ATOM 5830 C C . VAL A 1 693 ? 11.765 74.595 43.174 1.00 17.18 ? 734 VAL A C 1 ATOM 5831 O O . VAL A 1 693 ? 11.259 74.391 44.287 1.00 18.43 ? 734 VAL A O 1 ATOM 5832 C CB . VAL A 1 693 ? 10.564 73.872 41.027 1.00 17.49 ? 734 VAL A CB 1 ATOM 5833 C CG1 . VAL A 1 693 ? 10.074 72.654 41.876 1.00 18.61 ? 734 VAL A CG1 1 ATOM 5834 C CG2 . VAL A 1 693 ? 9.426 74.329 40.071 1.00 20.48 ? 734 VAL A CG2 1 ATOM 5835 N N . ALA A 1 694 ? 13.065 74.434 42.939 1.00 16.69 ? 735 ALA A N 1 ATOM 5836 C CA . ALA A 1 694 ? 13.951 73.958 44.004 1.00 17.30 ? 735 ALA A CA 1 ATOM 5837 C C . ALA A 1 694 ? 14.096 75.013 45.090 1.00 16.26 ? 735 ALA A C 1 ATOM 5838 O O . ALA A 1 694 ? 14.039 74.663 46.300 1.00 16.69 ? 735 ALA A O 1 ATOM 5839 C CB . ALA A 1 694 ? 15.346 73.616 43.440 1.00 17.78 ? 735 ALA A CB 1 ATOM 5840 N N . ALA A 1 695 ? 14.288 76.282 44.709 1.00 16.29 ? 736 ALA A N 1 ATOM 5841 C CA . ALA A 1 695 ? 14.410 77.351 45.722 1.00 17.72 ? 736 ALA A CA 1 ATOM 5842 C C . ALA A 1 695 ? 13.146 77.454 46.552 1.00 17.89 ? 736 ALA A C 1 ATOM 5843 O O . ALA A 1 695 ? 13.181 77.534 47.807 1.00 17.37 ? 736 ALA A O 1 ATOM 5844 C CB . ALA A 1 695 ? 14.715 78.719 45.031 1.00 18.05 ? 736 ALA A CB 1 ATOM 5845 N N . PHE A 1 696 ? 11.995 77.405 45.868 1.00 17.25 ? 737 PHE A N 1 ATOM 5846 C CA . PHE A 1 696 ? 10.727 77.460 46.588 1.00 18.23 ? 737 PHE A CA 1 ATOM 5847 C C . PHE A 1 696 ? 10.599 76.296 47.556 1.00 17.36 ? 737 PHE A C 1 ATOM 5848 O O . PHE A 1 696 ? 10.201 76.477 48.711 1.00 17.45 ? 737 PHE A O 1 ATOM 5849 C CB . PHE A 1 696 ? 9.541 77.460 45.603 1.00 17.76 ? 737 PHE A CB 1 ATOM 5850 C CG . PHE A 1 696 ? 8.220 77.123 46.279 1.00 18.34 ? 737 PHE A CG 1 ATOM 5851 C CD1 . PHE A 1 696 ? 7.685 78.007 47.250 1.00 19.88 ? 737 PHE A CD1 1 ATOM 5852 C CD2 . PHE A 1 696 ? 7.658 75.874 46.096 1.00 20.26 ? 737 PHE A CD2 1 ATOM 5853 C CE1 . PHE A 1 696 ? 6.497 77.614 47.942 1.00 21.92 ? 737 PHE A CE1 1 ATOM 5854 C CE2 . PHE A 1 696 ? 6.429 75.497 46.752 1.00 18.91 ? 737 PHE A CE2 1 ATOM 5855 C CZ . PHE A 1 696 ? 5.918 76.396 47.697 1.00 18.36 ? 737 PHE A CZ 1 ATOM 5856 N N . THR A 1 697 ? 10.944 75.107 47.096 1.00 16.11 ? 738 THR A N 1 ATOM 5857 C CA . THR A 1 697 ? 10.735 73.897 47.917 1.00 15.65 ? 738 THR A CA 1 ATOM 5858 C C . THR A 1 697 ? 11.650 73.940 49.135 1.00 16.95 ? 738 THR A C 1 ATOM 5859 O O . THR A 1 697 ? 11.223 73.622 50.248 1.00 17.19 ? 738 THR A O 1 ATOM 5860 C CB . THR A 1 697 ? 10.956 72.612 47.073 1.00 16.26 ? 738 THR A CB 1 ATOM 5861 O OG1 . THR A 1 697 ? 10.027 72.643 45.979 1.00 16.90 ? 738 THR A OG1 1 ATOM 5862 C CG2 . THR A 1 697 ? 10.600 71.400 47.974 1.00 17.61 ? 738 THR A CG2 1 ATOM 5863 N N . VAL A 1 698 ? 12.922 74.324 48.934 1.00 16.02 ? 739 VAL A N 1 ATOM 5864 C CA . VAL A 1 698 ? 13.823 74.423 50.109 1.00 17.48 ? 739 VAL A CA 1 ATOM 5865 C C . VAL A 1 698 ? 13.296 75.455 51.107 1.00 18.55 ? 739 VAL A C 1 ATOM 5866 O O . VAL A 1 698 ? 13.288 75.197 52.347 1.00 17.82 ? 739 VAL A O 1 ATOM 5867 C CB . VAL A 1 698 ? 15.224 74.750 49.637 1.00 17.45 ? 739 VAL A CB 1 ATOM 5868 C CG1 . VAL A 1 698 ? 16.141 75.117 50.821 1.00 19.01 ? 739 VAL A CG1 1 ATOM 5869 C CG2 . VAL A 1 698 ? 15.793 73.525 48.866 1.00 17.96 ? 739 VAL A CG2 1 ATOM 5870 N N . GLN A 1 699 ? 12.857 76.620 50.623 1.00 18.60 ? 740 GLN A N 1 ATOM 5871 C CA . GLN A 1 699 ? 12.315 77.633 51.558 1.00 18.76 ? 740 GLN A CA 1 ATOM 5872 C C . GLN A 1 699 ? 11.048 77.132 52.273 1.00 18.09 ? 740 GLN A C 1 ATOM 5873 O O . GLN A 1 699 ? 10.866 77.361 53.485 1.00 18.11 ? 740 GLN A O 1 ATOM 5874 C CB . GLN A 1 699 ? 12.004 78.936 50.817 1.00 19.56 ? 740 GLN A CB 1 ATOM 5875 C CG . GLN A 1 699 ? 11.419 80.019 51.719 1.00 18.76 ? 740 GLN A CG 1 ATOM 5876 C CD . GLN A 1 699 ? 12.449 80.630 52.630 1.00 20.93 ? 740 GLN A CD 1 ATOM 5877 O OE1 . GLN A 1 699 ? 13.663 80.589 52.343 1.00 22.64 ? 740 GLN A OE1 1 ATOM 5878 N NE2 . GLN A 1 699 ? 11.975 81.220 53.745 1.00 23.65 ? 740 GLN A NE2 1 ATOM 5879 N N . ALA A 1 700 ? 10.180 76.449 51.534 1.00 17.37 ? 741 ALA A N 1 ATOM 5880 C CA . ALA A 1 700 ? 8.944 75.932 52.133 1.00 17.67 ? 741 ALA A CA 1 ATOM 5881 C C . ALA A 1 700 ? 9.259 74.881 53.205 1.00 17.70 ? 741 ALA A C 1 ATOM 5882 O O . ALA A 1 700 ? 8.629 74.906 54.273 1.00 18.46 ? 741 ALA A O 1 ATOM 5883 C CB . ALA A 1 700 ? 8.036 75.333 51.036 1.00 17.95 ? 741 ALA A CB 1 ATOM 5884 N N . ALA A 1 701 ? 10.232 73.992 52.957 1.00 17.07 ? 742 ALA A N 1 ATOM 5885 C CA . ALA A 1 701 ? 10.683 73.015 53.970 1.00 17.67 ? 742 ALA A CA 1 ATOM 5886 C C . ALA A 1 701 ? 11.267 73.752 55.174 1.00 18.15 ? 742 ALA A C 1 ATOM 5887 O O . ALA A 1 701 ? 10.947 73.395 56.331 1.00 18.64 ? 742 ALA A O 1 ATOM 5888 C CB . ALA A 1 701 ? 11.769 72.109 53.348 1.00 16.67 ? 742 ALA A CB 1 ATOM 5889 N N . ALA A 1 702 ? 12.091 74.779 54.923 1.00 18.08 ? 743 ALA A N 1 ATOM 5890 C CA . ALA A 1 702 ? 12.640 75.568 56.052 1.00 19.53 ? 743 ALA A CA 1 ATOM 5891 C C . ALA A 1 702 ? 11.536 76.126 56.921 1.00 20.36 ? 743 ALA A C 1 ATOM 5892 O O . ALA A 1 702 ? 11.588 76.072 58.156 1.00 20.12 ? 743 ALA A O 1 ATOM 5893 C CB . ALA A 1 702 ? 13.488 76.710 55.534 1.00 19.80 ? 743 ALA A CB 1 ATOM 5894 N N . GLU A 1 703 ? 10.501 76.676 56.279 1.00 18.68 ? 744 GLU A N 1 ATOM 5895 C CA . GLU A 1 703 ? 9.437 77.301 57.036 1.00 20.06 ? 744 GLU A CA 1 ATOM 5896 C C . GLU A 1 703 ? 8.614 76.344 57.899 1.00 19.09 ? 744 GLU A C 1 ATOM 5897 O O . GLU A 1 703 ? 7.968 76.802 58.841 1.00 20.16 ? 744 GLU A O 1 ATOM 5898 C CB . GLU A 1 703 ? 8.523 78.109 56.097 1.00 21.11 ? 744 GLU A CB 1 ATOM 5899 C CG . GLU A 1 703 ? 9.285 79.340 55.603 1.00 21.90 ? 744 GLU A CG 1 ATOM 5900 C CD . GLU A 1 703 ? 8.545 80.235 54.646 1.00 29.42 ? 744 GLU A CD 1 ATOM 5901 O OE1 . GLU A 1 703 ? 7.388 79.918 54.276 1.00 30.46 ? 744 GLU A OE1 1 ATOM 5902 O OE2 . GLU A 1 703 ? 9.121 81.300 54.286 1.00 29.79 ? 744 GLU A OE2 1 ATOM 5903 N N . THR A 1 704 ? 8.660 75.036 57.600 1.00 17.73 ? 745 THR A N 1 ATOM 5904 C CA . THR A 1 704 ? 7.978 74.050 58.468 1.00 18.42 ? 745 THR A CA 1 ATOM 5905 C C . THR A 1 704 ? 8.686 73.918 59.813 1.00 19.28 ? 745 THR A C 1 ATOM 5906 O O . THR A 1 704 ? 8.093 73.418 60.755 1.00 21.05 ? 745 THR A O 1 ATOM 5907 C CB . THR A 1 704 ? 7.847 72.632 57.838 1.00 16.83 ? 745 THR A CB 1 ATOM 5908 O OG1 . THR A 1 704 ? 9.132 71.991 57.765 1.00 18.04 ? 745 THR A OG1 1 ATOM 5909 C CG2 . THR A 1 704 ? 7.239 72.719 56.395 1.00 18.00 ? 745 THR A CG2 1 ATOM 5910 N N . LEU A 1 705 ? 9.936 74.392 59.865 1.00 18.83 ? 746 LEU A N 1 ATOM 5911 C CA . LEU A 1 705 ? 10.730 74.404 61.111 1.00 19.14 ? 746 LEU A CA 1 ATOM 5912 C C . LEU A 1 705 ? 10.634 75.710 61.886 1.00 20.44 ? 746 LEU A C 1 ATOM 5913 O O . LEU A 1 705 ? 11.138 75.786 63.022 1.00 21.67 ? 746 LEU A O 1 ATOM 5914 C CB . LEU A 1 705 ? 12.212 74.061 60.836 1.00 19.03 ? 746 LEU A CB 1 ATOM 5915 C CG . LEU A 1 705 ? 12.418 72.737 60.122 1.00 20.96 ? 746 LEU A CG 1 ATOM 5916 C CD1 . LEU A 1 705 ? 13.921 72.619 59.854 1.00 21.37 ? 746 LEU A CD1 1 ATOM 5917 C CD2 . LEU A 1 705 ? 11.911 71.566 60.973 1.00 21.96 ? 746 LEU A CD2 1 ATOM 5918 N N . SER A 1 706 ? 10.020 76.750 61.303 1.00 20.80 ? 747 SER A N 1 ATOM 5919 C CA . SER A 1 706 ? 9.805 78.007 62.049 1.00 21.52 ? 747 SER A CA 1 ATOM 5920 C C . SER A 1 706 ? 8.856 77.775 63.230 1.00 22.11 ? 747 SER A C 1 ATOM 5921 O O . SER A 1 706 ? 8.093 76.799 63.253 1.00 21.52 ? 747 SER A O 1 ATOM 5922 C CB . SER A 1 706 ? 9.192 79.029 61.102 1.00 23.84 ? 747 SER A CB 1 ATOM 5923 O OG . SER A 1 706 ? 10.128 79.345 60.084 1.00 26.28 ? 747 SER A OG 1 ATOM 5924 N N . GLU A 1 707 ? 8.841 78.697 64.195 1.00 22.51 ? 748 GLU A N 1 ATOM 5925 C CA . GLU A 1 707 ? 7.758 78.669 65.189 1.00 25.45 ? 748 GLU A CA 1 ATOM 5926 C C . GLU A 1 707 ? 6.381 78.630 64.488 1.00 23.47 ? 748 GLU A C 1 ATOM 5927 O O . GLU A 1 707 ? 6.151 79.289 63.454 1.00 25.31 ? 748 GLU A O 1 ATOM 5928 C CB . GLU A 1 707 ? 7.844 79.853 66.141 1.00 27.22 ? 748 GLU A CB 1 ATOM 5929 C CG . GLU A 1 707 ? 9.140 79.693 66.939 1.00 32.25 ? 748 GLU A CG 1 ATOM 5930 C CD . GLU A 1 707 ? 9.197 80.501 68.197 1.00 44.06 ? 748 GLU A CD 1 ATOM 5931 O OE1 . GLU A 1 707 ? 9.554 81.697 68.110 1.00 47.27 ? 748 GLU A OE1 1 ATOM 5932 O OE2 . GLU A 1 707 ? 8.929 79.923 69.274 1.00 49.40 ? 748 GLU A OE2 1 ATOM 5933 N N . VAL A 1 708 ? 5.505 77.803 65.025 1.00 24.16 ? 749 VAL A N 1 ATOM 5934 C CA . VAL A 1 708 ? 4.292 77.419 64.266 1.00 24.19 ? 749 VAL A CA 1 ATOM 5935 C C . VAL A 1 708 ? 3.234 78.524 64.268 1.00 25.93 ? 749 VAL A C 1 ATOM 5936 O O . VAL A 1 708 ? 2.301 78.548 63.444 1.00 26.24 ? 749 VAL A O 1 ATOM 5937 C CB . VAL A 1 708 ? 3.693 76.078 64.747 1.00 23.97 ? 749 VAL A CB 1 ATOM 5938 C CG1 . VAL A 1 708 ? 4.716 74.954 64.672 1.00 24.68 ? 749 VAL A CG1 1 ATOM 5939 C CG2 . VAL A 1 708 ? 3.130 76.224 66.211 1.00 24.84 ? 749 VAL A CG2 1 ATOM 5940 N N . ALA A 1 709 ? 3.414 79.472 65.188 1.00 26.20 ? 750 ALA A N 1 ATOM 5941 C CA . ALA A 1 709 ? 2.508 80.644 65.325 1.00 28.61 ? 750 ALA A CA 1 ATOM 5942 C C . ALA A 1 709 ? 3.167 81.678 66.250 1.00 32.26 ? 750 ALA A C 1 ATOM 5943 C CB . ALA A 1 709 ? 1.150 80.229 65.862 1.00 28.84 ? 750 ALA A CB 1 ATOM 5944 O OXT . ALA A 1 709 ? 4.034 81.290 67.045 1.00 32.63 ? 750 ALA A OXT 1 HETATM 5945 C C1 . NAG B 2 . ? 11.627 26.086 57.844 1.00 22.81 ? 1755 NAG A C1 1 HETATM 5946 C C2 . NAG B 2 . ? 11.434 24.636 57.424 1.00 26.82 ? 1755 NAG A C2 1 HETATM 5947 C C3 . NAG B 2 . ? 9.981 24.202 57.628 1.00 28.72 ? 1755 NAG A C3 1 HETATM 5948 C C4 . NAG B 2 . ? 9.434 24.561 59.003 1.00 27.08 ? 1755 NAG A C4 1 HETATM 5949 C C5 . NAG B 2 . ? 9.815 26.001 59.360 1.00 26.18 ? 1755 NAG A C5 1 HETATM 5950 C C6 . NAG B 2 . ? 9.401 26.369 60.794 1.00 27.86 ? 1755 NAG A C6 1 HETATM 5951 C C7 . NAG B 2 . ? 12.965 23.935 55.686 1.00 34.34 ? 1755 NAG A C7 1 HETATM 5952 C C8 . NAG B 2 . ? 13.271 23.889 54.218 1.00 35.27 ? 1755 NAG A C8 1 HETATM 5953 N N2 . NAG B 2 . ? 11.820 24.529 56.031 1.00 29.66 ? 1755 NAG A N2 1 HETATM 5954 O O3 . NAG B 2 . ? 9.935 22.802 57.516 1.00 30.85 ? 1755 NAG A O3 1 HETATM 5955 O O4 . NAG B 2 . ? 8.020 24.466 58.958 1.00 27.24 ? 1755 NAG A O4 1 HETATM 5956 O O5 . NAG B 2 . ? 11.205 26.205 59.188 1.00 22.71 ? 1755 NAG A O5 1 HETATM 5957 O O6 . NAG B 2 . ? 10.082 25.514 61.686 1.00 31.27 ? 1755 NAG A O6 1 HETATM 5958 O O7 . NAG B 2 . ? 13.755 23.451 56.509 1.00 37.60 ? 1755 NAG A O7 1 HETATM 5959 C C1 . NAG C 2 . ? 7.503 23.582 59.976 1.00 31.46 ? 1756 NAG A C1 1 HETATM 5960 C C2 . NAG C 2 . ? 6.018 23.915 60.158 1.00 32.97 ? 1756 NAG A C2 1 HETATM 5961 C C3 . NAG C 2 . ? 5.308 22.898 61.061 1.00 36.52 ? 1756 NAG A C3 1 HETATM 5962 C C4 . NAG C 2 . ? 5.674 21.442 60.743 1.00 37.56 ? 1756 NAG A C4 1 HETATM 5963 C C5 . NAG C 2 . ? 7.193 21.265 60.555 1.00 37.69 ? 1756 NAG A C5 1 HETATM 5964 C C6 . NAG C 2 . ? 7.542 19.867 60.040 1.00 38.45 ? 1756 NAG A C6 1 HETATM 5965 C C7 . NAG C 2 . ? 5.480 26.385 60.157 1.00 31.42 ? 1756 NAG A C7 1 HETATM 5966 C C8 . NAG C 2 . ? 5.306 26.368 58.676 1.00 27.56 ? 1756 NAG A C8 1 HETATM 5967 N N2 . NAG C 2 . ? 5.819 25.235 60.757 1.00 30.83 ? 1756 NAG A N2 1 HETATM 5968 O O3 . NAG C 2 . ? 3.916 23.113 60.909 1.00 38.16 ? 1756 NAG A O3 1 HETATM 5969 O O4 . NAG C 2 . ? 5.185 20.573 61.766 1.00 39.56 ? 1756 NAG A O4 1 HETATM 5970 O O5 . NAG C 2 . ? 7.686 22.222 59.617 1.00 35.67 ? 1756 NAG A O5 1 HETATM 5971 O O6 . NAG C 2 . ? 7.162 19.794 58.673 1.00 37.99 ? 1756 NAG A O6 1 HETATM 5972 O O7 . NAG C 2 . ? 5.313 27.459 60.795 1.00 31.69 ? 1756 NAG A O7 1 HETATM 5973 C C1 . NAG D 2 . ? 4.130 28.321 25.280 1.00 29.81 ? 1757 NAG A C1 1 HETATM 5974 C C2 . NAG D 2 . ? 2.752 28.901 25.016 1.00 33.09 ? 1757 NAG A C2 1 HETATM 5975 C C3 . NAG D 2 . ? 1.766 27.917 24.379 1.00 34.57 ? 1757 NAG A C3 1 HETATM 5976 C C4 . NAG D 2 . ? 2.422 27.005 23.330 1.00 35.97 ? 1757 NAG A C4 1 HETATM 5977 C C5 . NAG D 2 . ? 3.788 26.494 23.835 1.00 35.92 ? 1757 NAG A C5 1 HETATM 5978 C C6 . NAG D 2 . ? 4.511 25.540 22.868 1.00 37.66 ? 1757 NAG A C6 1 HETATM 5979 C C7 . NAG D 2 . ? 2.021 30.692 26.463 1.00 36.39 ? 1757 NAG A C7 1 HETATM 5980 C C8 . NAG D 2 . ? 2.166 31.612 25.283 1.00 34.53 ? 1757 NAG A C8 1 HETATM 5981 N N2 . NAG D 2 . ? 2.292 29.401 26.288 1.00 33.88 ? 1757 NAG A N2 1 HETATM 5982 O O3 . NAG D 2 . ? 0.813 28.758 23.785 1.00 36.12 ? 1757 NAG A O3 1 HETATM 5983 O O4 . NAG D 2 . ? 1.580 25.902 22.960 1.00 36.76 ? 1757 NAG A O4 1 HETATM 5984 O O5 . NAG D 2 . ? 4.624 27.609 24.169 1.00 32.28 ? 1757 NAG A O5 1 HETATM 5985 O O6 . NAG D 2 . ? 4.734 26.153 21.613 1.00 42.33 ? 1757 NAG A O6 1 HETATM 5986 O O7 . NAG D 2 . ? 1.650 31.138 27.542 1.00 38.45 ? 1757 NAG A O7 1 HETATM 5987 C C1 . NAG E 2 . ? 20.146 25.280 17.679 1.00 22.60 ? 1758 NAG A C1 1 HETATM 5988 C C2 . NAG E 2 . ? 20.686 24.045 16.972 1.00 23.99 ? 1758 NAG A C2 1 HETATM 5989 C C3 . NAG E 2 . ? 19.840 23.751 15.745 1.00 25.33 ? 1758 NAG A C3 1 HETATM 5990 C C4 . NAG E 2 . ? 18.346 23.695 16.071 1.00 25.75 ? 1758 NAG A C4 1 HETATM 5991 C C5 . NAG E 2 . ? 17.887 24.882 16.957 1.00 24.48 ? 1758 NAG A C5 1 HETATM 5992 C C6 . NAG E 2 . ? 16.444 24.734 17.460 1.00 22.97 ? 1758 NAG A C6 1 HETATM 5993 C C7 . NAG E 2 . ? 23.096 23.786 17.138 1.00 28.43 ? 1758 NAG A C7 1 HETATM 5994 C C8 . NAG E 2 . ? 24.441 24.155 16.577 1.00 29.11 ? 1758 NAG A C8 1 HETATM 5995 N N2 . NAG E 2 . ? 22.035 24.326 16.547 1.00 24.92 ? 1758 NAG A N2 1 HETATM 5996 O O3 . NAG E 2 . ? 20.275 22.523 15.196 1.00 23.38 ? 1758 NAG A O3 1 HETATM 5997 O O4 . NAG E 2 . ? 17.667 23.752 14.840 1.00 30.61 ? 1758 NAG A O4 1 HETATM 5998 O O5 . NAG E 2 . ? 18.783 25.063 18.042 1.00 24.55 ? 1758 NAG A O5 1 HETATM 5999 O O6 . NAG E 2 . ? 16.259 23.529 18.177 1.00 21.89 ? 1758 NAG A O6 1 HETATM 6000 O O7 . NAG E 2 . ? 23.013 23.018 18.087 1.00 30.19 ? 1758 NAG A O7 1 HETATM 6001 C C1 . NAG F 2 . ? 16.717 22.667 14.693 1.00 35.35 ? 1767 NAG A C1 1 HETATM 6002 C C2 . NAG F 2 . ? 15.675 23.116 13.667 1.00 36.58 ? 1767 NAG A C2 1 HETATM 6003 C C3 . NAG F 2 . ? 14.653 22.009 13.416 1.00 39.09 ? 1767 NAG A C3 1 HETATM 6004 C C4 . NAG F 2 . ? 15.362 20.707 13.050 1.00 39.63 ? 1767 NAG A C4 1 HETATM 6005 C C5 . NAG F 2 . ? 16.312 20.368 14.211 1.00 39.41 ? 1767 NAG A C5 1 HETATM 6006 C C6 . NAG F 2 . ? 16.968 18.997 14.079 1.00 40.30 ? 1767 NAG A C6 1 HETATM 6007 C C7 . NAG F 2 . ? 15.372 25.552 13.639 1.00 36.90 ? 1767 NAG A C7 1 HETATM 6008 C C8 . NAG F 2 . ? 14.564 26.707 14.147 1.00 36.04 ? 1767 NAG A C8 1 HETATM 6009 N N2 . NAG F 2 . ? 14.995 24.338 14.071 1.00 36.88 ? 1767 NAG A N2 1 HETATM 6010 O O3 . NAG F 2 . ? 13.800 22.409 12.376 1.00 39.77 ? 1767 NAG A O3 1 HETATM 6011 O O4 . NAG F 2 . ? 14.401 19.694 12.782 1.00 41.77 ? 1767 NAG A O4 1 HETATM 6012 O O5 . NAG F 2 . ? 17.288 21.406 14.344 1.00 36.44 ? 1767 NAG A O5 1 HETATM 6013 O O6 . NAG F 2 . ? 18.056 19.085 13.188 1.00 41.84 ? 1767 NAG A O6 1 HETATM 6014 O O7 . NAG F 2 . ? 16.322 25.762 12.874 1.00 35.11 ? 1767 NAG A O7 1 HETATM 6015 C C1 . NAG G 2 . ? 20.309 55.322 11.022 1.00 44.26 ? 1759 NAG A C1 1 HETATM 6016 C C2 . NAG G 2 . ? 20.056 56.792 10.690 1.00 48.94 ? 1759 NAG A C2 1 HETATM 6017 C C3 . NAG G 2 . ? 18.556 56.990 10.534 1.00 49.60 ? 1759 NAG A C3 1 HETATM 6018 C C4 . NAG G 2 . ? 18.097 56.191 9.318 1.00 49.66 ? 1759 NAG A C4 1 HETATM 6019 C C5 . NAG G 2 . ? 18.463 54.709 9.445 1.00 48.46 ? 1759 NAG A C5 1 HETATM 6020 C C6 . NAG G 2 . ? 18.439 54.110 8.039 1.00 48.73 ? 1759 NAG A C6 1 HETATM 6021 C C7 . NAG G 2 . ? 21.813 58.290 11.517 1.00 50.90 ? 1759 NAG A C7 1 HETATM 6022 C C8 . NAG G 2 . ? 22.258 59.199 12.630 1.00 50.36 ? 1759 NAG A C8 1 HETATM 6023 N N2 . NAG G 2 . ? 20.624 57.697 11.683 1.00 49.45 ? 1759 NAG A N2 1 HETATM 6024 O O3 . NAG G 2 . ? 18.279 58.357 10.351 1.00 51.42 ? 1759 NAG A O3 1 HETATM 6025 O O4 . NAG G 2 . ? 16.703 56.332 9.127 1.00 50.84 ? 1759 NAG A O4 1 HETATM 6026 O O5 . NAG G 2 . ? 19.754 54.465 10.015 1.00 46.57 ? 1759 NAG A O5 1 HETATM 6027 O O6 . NAG G 2 . ? 18.055 52.756 8.091 1.00 49.07 ? 1759 NAG A O6 1 HETATM 6028 O O7 . NAG G 2 . ? 22.534 58.123 10.522 1.00 50.21 ? 1759 NAG A O7 1 HETATM 6029 C C1 . NAG H 2 . ? 36.423 37.707 53.032 1.00 30.56 ? 1760 NAG A C1 1 HETATM 6030 C C2 . NAG H 2 . ? 36.425 37.718 51.507 1.00 29.58 ? 1760 NAG A C2 1 HETATM 6031 C C3 . NAG H 2 . ? 37.698 36.998 51.029 1.00 34.25 ? 1760 NAG A C3 1 HETATM 6032 C C4 . NAG H 2 . ? 38.958 37.672 51.576 1.00 36.46 ? 1760 NAG A C4 1 HETATM 6033 C C5 . NAG H 2 . ? 38.821 37.752 53.105 1.00 36.04 ? 1760 NAG A C5 1 HETATM 6034 C C6 . NAG H 2 . ? 40.053 38.395 53.773 1.00 36.69 ? 1760 NAG A C6 1 HETATM 6035 C C7 . NAG H 2 . ? 34.458 37.707 50.113 1.00 24.86 ? 1760 NAG A C7 1 HETATM 6036 C C8 . NAG H 2 . ? 33.289 36.988 49.535 1.00 25.23 ? 1760 NAG A C8 1 HETATM 6037 N N2 . NAG H 2 . ? 35.253 37.063 50.951 1.00 25.98 ? 1760 NAG A N2 1 HETATM 6038 O O3 . NAG H 2 . ? 37.742 37.023 49.628 1.00 36.65 ? 1760 NAG A O3 1 HETATM 6039 O O4 . NAG H 2 . ? 40.164 36.991 51.169 1.00 38.97 ? 1760 NAG A O4 1 HETATM 6040 O O5 . NAG H 2 . ? 37.603 38.395 53.479 1.00 32.46 ? 1760 NAG A O5 1 HETATM 6041 O O6 . NAG H 2 . ? 40.216 39.754 53.407 1.00 37.21 ? 1760 NAG A O6 1 HETATM 6042 O O7 . NAG H 2 . ? 34.649 38.866 49.787 1.00 21.84 ? 1760 NAG A O7 1 HETATM 6043 C C1 . NAG I 2 . ? 24.363 61.963 68.777 1.00 15.71 ? 1761 NAG A C1 1 HETATM 6044 C C2 . NAG I 2 . ? 22.975 62.547 69.052 1.00 15.64 ? 1761 NAG A C2 1 HETATM 6045 C C3 . NAG I 2 . ? 23.174 63.990 69.450 1.00 16.94 ? 1761 NAG A C3 1 HETATM 6046 C C4 . NAG I 2 . ? 24.126 64.123 70.645 1.00 16.92 ? 1761 NAG A C4 1 HETATM 6047 C C5 . NAG I 2 . ? 25.441 63.423 70.296 1.00 16.60 ? 1761 NAG A C5 1 HETATM 6048 C C6 . NAG I 2 . ? 26.494 63.356 71.414 1.00 22.17 ? 1761 NAG A C6 1 HETATM 6049 C C7 . NAG I 2 . ? 20.946 61.976 67.717 1.00 25.98 ? 1761 NAG A C7 1 HETATM 6050 C C8 . NAG I 2 . ? 20.319 61.556 69.005 1.00 26.72 ? 1761 NAG A C8 1 HETATM 6051 N N2 . NAG I 2 . ? 22.178 62.452 67.813 1.00 20.57 ? 1761 NAG A N2 1 HETATM 6052 O O3 . NAG I 2 . ? 21.920 64.577 69.737 1.00 20.64 ? 1761 NAG A O3 1 HETATM 6053 O O4 . NAG I 2 . ? 24.397 65.487 70.755 1.00 19.60 ? 1761 NAG A O4 1 HETATM 6054 O O5 . NAG I 2 . ? 25.137 62.086 69.938 1.00 18.02 ? 1761 NAG A O5 1 HETATM 6055 O O6 . NAG I 2 . ? 25.897 62.873 72.602 1.00 26.88 ? 1761 NAG A O6 1 HETATM 6056 O O7 . NAG I 2 . ? 20.259 61.921 66.617 1.00 29.34 ? 1761 NAG A O7 1 HETATM 6057 C C1 . NAG J 2 . ? 24.180 65.928 72.118 1.00 21.71 ? 1762 NAG A C1 1 HETATM 6058 C C2 . NAG J 2 . ? 24.801 67.323 72.198 1.00 26.44 ? 1762 NAG A C2 1 HETATM 6059 C C3 . NAG J 2 . ? 24.540 67.945 73.571 1.00 28.59 ? 1762 NAG A C3 1 HETATM 6060 C C4 . NAG J 2 . ? 23.043 67.870 73.952 1.00 27.47 ? 1762 NAG A C4 1 HETATM 6061 C C5 . NAG J 2 . ? 22.495 66.453 73.734 1.00 27.04 ? 1762 NAG A C5 1 HETATM 6062 C C6 . NAG J 2 . ? 20.979 66.417 73.940 1.00 29.00 ? 1762 NAG A C6 1 HETATM 6063 C C7 . NAG J 2 . ? 26.798 67.644 70.768 1.00 31.51 ? 1762 NAG A C7 1 HETATM 6064 C C8 . NAG J 2 . ? 25.960 68.202 69.661 1.00 30.96 ? 1762 NAG A C8 1 HETATM 6065 N N2 . NAG J 2 . ? 26.237 67.244 71.926 1.00 30.04 ? 1762 NAG A N2 1 HETATM 6066 O O3 . NAG J 2 . ? 24.993 69.291 73.558 1.00 26.91 ? 1762 NAG A O3 1 HETATM 6067 O O4 . NAG J 2 . ? 22.860 68.218 75.324 1.00 30.14 ? 1762 NAG A O4 1 HETATM 6068 O O5 . NAG J 2 . ? 22.785 66.017 72.399 1.00 22.68 ? 1762 NAG A O5 1 HETATM 6069 O O6 . NAG J 2 . ? 20.348 67.354 73.083 1.00 32.23 ? 1762 NAG A O6 1 HETATM 6070 O O7 . NAG J 2 . ? 28.019 67.556 70.580 1.00 37.09 ? 1762 NAG A O7 1 HETATM 6071 C C1 . NAG K 2 . ? 15.167 84.099 52.785 1.00 16.07 ? 1763 NAG A C1 1 HETATM 6072 C C2 . NAG K 2 . ? 14.167 84.217 51.616 1.00 14.24 ? 1763 NAG A C2 1 HETATM 6073 C C3 . NAG K 2 . ? 13.948 85.690 51.276 1.00 17.33 ? 1763 NAG A C3 1 HETATM 6074 C C4 . NAG K 2 . ? 13.518 86.439 52.564 1.00 18.63 ? 1763 NAG A C4 1 HETATM 6075 C C5 . NAG K 2 . ? 14.463 86.143 53.741 1.00 22.34 ? 1763 NAG A C5 1 HETATM 6076 C C6 . NAG K 2 . ? 13.906 86.771 55.027 1.00 22.95 ? 1763 NAG A C6 1 HETATM 6077 C C7 . NAG K 2 . ? 13.739 82.721 49.713 1.00 16.71 ? 1763 NAG A C7 1 HETATM 6078 C C8 . NAG K 2 . ? 14.343 82.016 48.542 1.00 16.56 ? 1763 NAG A C8 1 HETATM 6079 N N2 . NAG K 2 . ? 14.592 83.450 50.443 1.00 13.64 ? 1763 NAG A N2 1 HETATM 6080 O O3 . NAG K 2 . ? 12.895 85.778 50.326 1.00 19.56 ? 1763 NAG A O3 1 HETATM 6081 O O4 . NAG K 2 . ? 13.592 87.845 52.415 1.00 24.05 ? 1763 NAG A O4 1 HETATM 6082 O O5 . NAG K 2 . ? 14.534 84.743 53.896 1.00 19.16 ? 1763 NAG A O5 1 HETATM 6083 O O6 . NAG K 2 . ? 14.931 87.004 55.984 1.00 31.26 ? 1763 NAG A O6 1 HETATM 6084 O O7 . NAG K 2 . ? 12.531 82.598 49.969 1.00 15.70 ? 1763 NAG A O7 1 HETATM 6085 C C1 . NAG L 2 . ? 12.481 88.367 51.666 1.00 24.00 ? 1764 NAG A C1 1 HETATM 6086 C C2 . NAG L 2 . ? 12.016 89.683 52.263 1.00 26.14 ? 1764 NAG A C2 1 HETATM 6087 C C3 . NAG L 2 . ? 11.011 90.386 51.339 1.00 24.71 ? 1764 NAG A C3 1 HETATM 6088 C C4 . NAG L 2 . ? 11.592 90.538 49.932 1.00 25.46 ? 1764 NAG A C4 1 HETATM 6089 C C5 . NAG L 2 . ? 11.986 89.130 49.482 1.00 25.42 ? 1764 NAG A C5 1 HETATM 6090 C C6 . NAG L 2 . ? 12.587 89.127 48.088 1.00 30.79 ? 1764 NAG A C6 1 HETATM 6091 C C7 . NAG L 2 . ? 12.047 89.909 54.683 1.00 31.96 ? 1764 NAG A C7 1 HETATM 6092 C C8 . NAG L 2 . ? 13.413 90.531 54.601 1.00 31.30 ? 1764 NAG A C8 1 HETATM 6093 N N2 . NAG L 2 . ? 11.408 89.505 53.573 1.00 29.69 ? 1764 NAG A N2 1 HETATM 6094 O O3 . NAG L 2 . ? 10.734 91.656 51.905 1.00 27.04 ? 1764 NAG A O3 1 HETATM 6095 O O4 . NAG L 2 . ? 10.638 91.003 48.972 1.00 24.51 ? 1764 NAG A O4 1 HETATM 6096 O O5 . NAG L 2 . ? 12.970 88.634 50.381 1.00 24.13 ? 1764 NAG A O5 1 HETATM 6097 O O6 . NAG L 2 . ? 13.731 89.949 48.077 1.00 38.43 ? 1764 NAG A O6 1 HETATM 6098 O O7 . NAG L 2 . ? 11.535 89.766 55.789 1.00 39.04 ? 1764 NAG A O7 1 HETATM 6099 C C1 . BMA M 3 . ? 10.595 92.418 48.905 1.00 24.35 ? 1765 BMA A C1 1 HETATM 6100 C C2 . BMA M 3 . ? 10.318 92.816 47.452 1.00 24.82 ? 1765 BMA A C2 1 HETATM 6101 C C3 . BMA M 3 . ? 10.087 94.300 47.335 1.00 25.22 ? 1765 BMA A C3 1 HETATM 6102 C C4 . BMA M 3 . ? 9.012 94.734 48.352 1.00 25.97 ? 1765 BMA A C4 1 HETATM 6103 C C5 . BMA M 3 . ? 9.369 94.260 49.762 1.00 27.18 ? 1765 BMA A C5 1 HETATM 6104 C C6 . BMA M 3 . ? 8.298 94.594 50.789 1.00 26.91 ? 1765 BMA A C6 1 HETATM 6105 O O2 . BMA M 3 . ? 9.158 92.096 46.995 1.00 25.96 ? 1765 BMA A O2 1 HETATM 6106 O O3 . BMA M 3 . ? 9.709 94.569 45.968 1.00 23.05 ? 1765 BMA A O3 1 HETATM 6107 O O4 . BMA M 3 . ? 8.844 96.135 48.339 1.00 25.84 ? 1765 BMA A O4 1 HETATM 6108 O O5 . BMA M 3 . ? 9.527 92.839 49.746 1.00 23.35 ? 1765 BMA A O5 1 HETATM 6109 O O6 . BMA M 3 . ? 8.702 93.982 52.025 1.00 27.33 ? 1765 BMA A O6 1 HETATM 6110 C C1 . MAN N 4 . ? 10.401 95.725 45.410 1.00 25.34 ? 1766 MAN A C1 1 HETATM 6111 C C2 . MAN N 4 . ? 9.622 96.153 44.162 1.00 25.28 ? 1766 MAN A C2 1 HETATM 6112 C C3 . MAN N 4 . ? 9.704 95.062 43.077 1.00 28.19 ? 1766 MAN A C3 1 HETATM 6113 C C4 . MAN N 4 . ? 11.154 94.691 42.755 1.00 29.59 ? 1766 MAN A C4 1 HETATM 6114 C C5 . MAN N 4 . ? 11.863 94.356 44.074 1.00 27.77 ? 1766 MAN A C5 1 HETATM 6115 C C6 . MAN N 4 . ? 13.333 93.967 43.875 1.00 31.12 ? 1766 MAN A C6 1 HETATM 6116 O O2 . MAN N 4 . ? 10.170 97.374 43.711 1.00 25.94 ? 1766 MAN A O2 1 HETATM 6117 O O3 . MAN N 4 . ? 9.020 95.430 41.897 1.00 33.36 ? 1766 MAN A O3 1 HETATM 6118 O O4 . MAN N 4 . ? 11.173 93.561 41.883 1.00 30.10 ? 1766 MAN A O4 1 HETATM 6119 O O5 . MAN N 4 . ? 11.737 95.421 45.012 1.00 24.93 ? 1766 MAN A O5 1 HETATM 6120 O O6 . MAN N 4 . ? 14.024 95.120 43.448 1.00 31.88 ? 1766 MAN A O6 1 HETATM 6121 ZN ZN . ZN O 5 . ? 17.601 41.306 43.414 1.00 15.48 ? 1751 ZN A ZN 1 HETATM 6122 ZN ZN . ZN P 5 . ? 16.814 41.968 46.537 1.00 14.87 ? 1752 ZN A ZN 1 HETATM 6123 CA CA . CA Q 6 . ? -0.759 50.098 41.491 1.00 13.91 ? 1753 CA A CA 1 HETATM 6124 CL CL . CL R 7 . ? 19.049 47.039 51.598 1.00 20.07 ? 1754 CL A CL 1 HETATM 6125 C C . JRG S 8 . ? 20.141 45.633 45.817 1.00 23.70 ? 1 JRG A C 1 HETATM 6126 N N . JRG S 8 . ? 18.658 45.396 43.946 1.00 21.87 ? 1 JRG A N 1 HETATM 6127 O O . JRG S 8 . ? 19.626 46.778 46.057 1.00 23.61 ? 1 JRG A O 1 HETATM 6128 C CA . JRG S 8 . ? 19.973 45.001 44.433 1.00 23.69 ? 1 JRG A CA 1 HETATM 6129 C CB . JRG S 8 . ? 20.984 45.636 43.427 1.00 25.04 ? 1 JRG A CB 1 HETATM 6130 C CAA . JRG S 8 . ? 13.915 48.847 40.176 1.00 34.56 ? 1 JRG A CAA 1 HETATM 6131 O OAC . JRG S 8 . ? 17.888 45.637 40.395 1.00 27.14 ? 1 JRG A OAC 1 HETATM 6132 O OAD . JRG S 8 . ? 18.429 43.655 42.561 1.00 20.91 ? 1 JRG A OAD 1 HETATM 6133 O OAE . JRG S 8 . ? 22.255 49.667 43.938 1.00 40.12 ? 1 JRG A OAE 1 HETATM 6134 O OAG . JRG S 8 . ? 16.949 43.916 39.381 1.00 26.35 ? 1 JRG A OAG 1 HETATM 6135 I IAH . JRG S 8 . ? 23.637 50.304 51.377 1.00 34.50 ? 1 JRG A IAH 1 HETATM 6136 C CAI . JRG S 8 . ? 23.380 50.913 48.110 1.00 35.64 ? 1 JRG A CAI 1 HETATM 6137 C CAJ . JRG S 8 . ? 23.502 48.657 48.538 1.00 35.29 ? 1 JRG A CAJ 1 HETATM 6138 C CAK . JRG S 8 . ? 23.252 50.681 46.709 1.00 35.42 ? 1 JRG A CAK 1 HETATM 6139 C CAL . JRG S 8 . ? 23.401 48.383 47.128 1.00 37.12 ? 1 JRG A CAL 1 HETATM 6140 C CAM . JRG S 8 . ? 23.420 45.941 42.670 1.00 32.05 ? 1 JRG A CAM 1 HETATM 6141 C CAN . JRG S 8 . ? 22.445 45.217 43.673 1.00 29.05 ? 1 JRG A CAN 1 HETATM 6142 C CAO . JRG S 8 . ? 23.397 47.475 42.685 1.00 32.58 ? 1 JRG A CAO 1 HETATM 6143 C CAP . JRG S 8 . ? 14.823 46.616 41.139 1.00 27.09 ? 1 JRG A CAP 1 HETATM 6144 C CAR . JRG S 8 . ? 14.738 45.140 41.190 1.00 23.52 ? 1 JRG A CAR 1 HETATM 6145 N NAS . JRG S 8 . ? 23.668 47.968 44.055 1.00 32.69 ? 1 JRG A NAS 1 HETATM 6146 N NAU . JRG S 8 . ? 16.746 45.125 42.714 1.00 22.46 ? 1 JRG A NAU 1 HETATM 6147 S SAV . JRG S 8 . ? 13.273 47.228 40.373 1.00 27.14 ? 1 JRG A SAV 1 HETATM 6148 C CAX . JRG S 8 . ? 17.041 44.716 40.337 1.00 26.40 ? 1 JRG A CAX 1 HETATM 6149 C CAY . JRG S 8 . ? 17.970 44.691 43.049 1.00 23.10 ? 1 JRG A CAY 1 HETATM 6150 C CAZ . JRG S 8 . ? 23.104 49.051 44.591 1.00 36.21 ? 1 JRG A CAZ 1 HETATM 6151 C CBA . JRG S 8 . ? 23.495 49.938 49.152 1.00 38.20 ? 1 JRG A CBA 1 HETATM 6152 C CBB . JRG S 8 . ? 23.295 49.374 46.136 1.00 33.94 ? 1 JRG A CBB 1 HETATM 6153 C CBD . JRG S 8 . ? 16.090 44.504 41.559 1.00 20.93 ? 1 JRG A CBD 1 HETATM 6154 O OXT . JRG S 8 . ? 20.752 44.909 46.627 1.00 25.57 ? 1 JRG A OXT 1 HETATM 6155 O O . HOH T 9 . ? 8.232 44.835 46.438 1.00 13.10 ? 1768 HOH A O 1 HETATM 6156 O O . HOH T 9 . ? 6.873 58.516 37.478 1.00 15.96 ? 1769 HOH A O 1 HETATM 6157 O O . HOH T 9 . ? 7.985 69.787 59.209 1.00 14.29 ? 1770 HOH A O 1 HETATM 6158 O O . HOH T 9 . ? 13.642 44.832 49.943 1.00 17.11 ? 1771 HOH A O 1 HETATM 6159 O O . HOH T 9 . ? 9.190 50.827 46.568 1.00 15.78 ? 1772 HOH A O 1 HETATM 6160 O O . HOH T 9 . ? 1.032 50.683 39.979 1.00 15.46 ? 1773 HOH A O 1 HETATM 6161 O O . HOH T 9 . ? 12.031 61.980 43.735 1.00 16.33 ? 1774 HOH A O 1 HETATM 6162 O O . HOH T 9 . ? 13.620 30.029 40.151 1.00 15.54 ? 1775 HOH A O 1 HETATM 6163 O O . HOH T 9 . ? 15.217 42.043 38.882 1.00 15.77 ? 1776 HOH A O 1 HETATM 6164 O O . HOH T 9 . ? 9.626 61.003 57.765 1.00 14.63 ? 1777 HOH A O 1 HETATM 6165 O O . HOH T 9 . ? 10.956 36.906 42.369 1.00 14.31 ? 1778 HOH A O 1 HETATM 6166 O O . HOH T 9 . ? -5.409 59.881 59.875 1.00 14.28 ? 1779 HOH A O 1 HETATM 6167 O O . HOH T 9 . ? 13.669 27.152 51.727 1.00 14.89 ? 1780 HOH A O 1 HETATM 6168 O O . HOH T 9 . ? 7.448 71.981 45.309 1.00 19.06 ? 1781 HOH A O 1 HETATM 6169 O O . HOH T 9 . ? 5.708 69.140 55.519 1.00 16.93 ? 1782 HOH A O 1 HETATM 6170 O O . HOH T 9 . ? 16.871 37.273 44.071 1.00 15.11 ? 1783 HOH A O 1 HETATM 6171 O O . HOH T 9 . ? -3.601 62.308 54.026 1.00 17.85 ? 1784 HOH A O 1 HETATM 6172 O O . HOH T 9 . ? 29.446 36.238 44.478 1.00 13.69 ? 1785 HOH A O 1 HETATM 6173 O O . HOH T 9 . ? 6.430 76.156 61.093 1.00 15.45 ? 1786 HOH A O 1 HETATM 6174 O O . HOH T 9 . ? -3.444 60.260 61.961 1.00 15.03 ? 1787 HOH A O 1 HETATM 6175 O O . HOH T 9 . ? 19.359 47.937 54.681 1.00 25.09 ? 1788 HOH A O 1 HETATM 6176 O O . HOH T 9 . ? 3.947 70.605 64.541 1.00 17.73 ? 1789 HOH A O 1 HETATM 6177 O O . HOH T 9 . ? 19.153 62.343 36.633 1.00 16.22 ? 1790 HOH A O 1 HETATM 6178 O O . HOH T 9 . ? -6.993 51.732 51.570 1.00 17.34 ? 1791 HOH A O 1 HETATM 6179 O O . HOH T 9 . ? 17.984 40.777 32.386 1.00 16.24 ? 1792 HOH A O 1 HETATM 6180 O O . HOH T 9 . ? 20.095 61.641 62.962 1.00 16.31 ? 1793 HOH A O 1 HETATM 6181 O O . HOH T 9 . ? -4.411 59.635 57.352 1.00 16.06 ? 1794 HOH A O 1 HETATM 6182 O O . HOH T 9 . ? 3.572 72.173 43.570 1.00 19.60 ? 1795 HOH A O 1 HETATM 6183 O O . HOH T 9 . ? 30.150 42.750 32.590 1.00 15.02 ? 1796 HOH A O 1 HETATM 6184 O O . HOH T 9 . ? 24.107 46.207 34.906 1.00 16.38 ? 1797 HOH A O 1 HETATM 6185 O O . HOH T 9 . ? 14.921 37.089 28.003 1.00 13.58 ? 1798 HOH A O 1 HETATM 6186 O O . HOH T 9 . ? 18.482 33.698 43.590 1.00 17.04 ? 1799 HOH A O 1 HETATM 6187 O O . HOH T 9 . ? 29.027 33.982 32.949 1.00 16.18 ? 1800 HOH A O 1 HETATM 6188 O O . HOH T 9 . ? 5.978 75.545 54.252 1.00 18.14 ? 1801 HOH A O 1 HETATM 6189 O O . HOH T 9 . ? 3.648 62.484 50.628 1.00 19.90 ? 1802 HOH A O 1 HETATM 6190 O O . HOH T 9 . ? 14.630 32.241 48.159 1.00 14.64 ? 1803 HOH A O 1 HETATM 6191 O O . HOH T 9 . ? 4.580 35.152 45.427 1.00 18.45 ? 1804 HOH A O 1 HETATM 6192 O O . HOH T 9 . ? 0.242 57.071 45.765 1.00 21.58 ? 1805 HOH A O 1 HETATM 6193 O O . HOH T 9 . ? -0.189 64.886 66.106 0.50 16.82 ? 1806 HOH A O 1 HETATM 6194 O O . HOH T 9 . ? -0.397 43.620 60.782 1.00 19.93 ? 1807 HOH A O 1 HETATM 6195 O O . HOH T 9 . ? 14.566 38.287 34.976 1.00 14.64 ? 1808 HOH A O 1 HETATM 6196 O O . HOH T 9 . ? 22.183 88.171 32.538 1.00 13.44 ? 1809 HOH A O 1 HETATM 6197 O O . HOH T 9 . ? 23.367 67.896 34.411 1.00 18.16 ? 1810 HOH A O 1 HETATM 6198 O O . HOH T 9 . ? 23.185 68.940 43.089 1.00 17.07 ? 1811 HOH A O 1 HETATM 6199 O O . HOH T 9 . ? 20.841 45.946 36.585 1.00 15.34 ? 1812 HOH A O 1 HETATM 6200 O O . HOH T 9 . ? 24.627 37.381 32.730 1.00 15.34 ? 1813 HOH A O 1 HETATM 6201 O O . HOH T 9 . ? 16.352 55.963 35.499 1.00 19.55 ? 1814 HOH A O 1 HETATM 6202 O O . HOH T 9 . ? 25.835 37.169 38.227 1.00 14.82 ? 1815 HOH A O 1 HETATM 6203 O O . HOH T 9 . ? 9.600 29.320 43.115 1.00 16.58 ? 1816 HOH A O 1 HETATM 6204 O O . HOH T 9 . ? 27.637 31.278 28.900 1.00 15.36 ? 1817 HOH A O 1 HETATM 6205 O O . HOH T 9 . ? 20.649 27.537 48.926 1.00 17.58 ? 1818 HOH A O 1 HETATM 6206 O O . HOH T 9 . ? 10.195 31.269 26.719 1.00 19.07 ? 1819 HOH A O 1 HETATM 6207 O O . HOH T 9 . ? 29.037 60.728 57.312 1.00 26.05 ? 1820 HOH A O 1 HETATM 6208 O O . HOH T 9 . ? 17.021 62.192 38.472 1.00 17.10 ? 1821 HOH A O 1 HETATM 6209 O O . HOH T 9 . ? 19.297 36.222 43.243 1.00 17.77 ? 1822 HOH A O 1 HETATM 6210 O O . HOH T 9 . ? 20.205 31.366 43.683 1.00 18.31 ? 1823 HOH A O 1 HETATM 6211 O O . HOH T 9 . ? 8.183 50.599 40.713 1.00 22.38 ? 1824 HOH A O 1 HETATM 6212 O O . HOH T 9 . ? -2.543 44.374 37.780 1.00 16.73 ? 1825 HOH A O 1 HETATM 6213 O O . HOH T 9 . ? 6.588 60.949 67.284 1.00 19.67 ? 1826 HOH A O 1 HETATM 6214 O O . HOH T 9 . ? 5.228 64.956 37.085 1.00 20.38 ? 1827 HOH A O 1 HETATM 6215 O O . HOH T 9 . ? 14.773 80.982 38.335 1.00 17.10 ? 1828 HOH A O 1 HETATM 6216 O O . HOH T 9 . ? 6.881 55.483 43.783 1.00 23.56 ? 1829 HOH A O 1 HETATM 6217 O O . HOH T 9 . ? 14.010 40.907 53.609 1.00 18.73 ? 1830 HOH A O 1 HETATM 6218 O O . HOH T 9 . ? 11.141 27.571 54.446 1.00 17.11 ? 1831 HOH A O 1 HETATM 6219 O O . HOH T 9 . ? 23.234 44.556 36.791 1.00 18.94 ? 1832 HOH A O 1 HETATM 6220 O O . HOH T 9 . ? 14.054 68.179 34.792 1.00 19.43 ? 1833 HOH A O 1 HETATM 6221 O O . HOH T 9 . ? 4.288 67.182 51.565 1.00 19.82 ? 1834 HOH A O 1 HETATM 6222 O O . HOH T 9 . ? 4.044 68.784 49.341 1.00 19.07 ? 1835 HOH A O 1 HETATM 6223 O O . HOH T 9 . ? -4.573 55.367 51.850 1.00 19.00 ? 1836 HOH A O 1 HETATM 6224 O O . HOH T 9 . ? 2.630 33.279 45.387 1.00 17.99 ? 1838 HOH A O 1 HETATM 6225 O O . HOH T 9 . ? -3.901 57.765 46.438 1.00 24.61 ? 1839 HOH A O 1 HETATM 6226 O O . HOH T 9 . ? 11.066 63.635 58.320 1.00 24.11 ? 1840 HOH A O 1 HETATM 6227 O O . HOH T 9 . ? 28.707 53.948 52.773 1.00 19.16 ? 1841 HOH A O 1 HETATM 6228 O O . HOH T 9 . ? 13.821 71.510 40.643 1.00 17.34 ? 1842 HOH A O 1 HETATM 6229 O O . HOH T 9 . ? 19.017 27.862 35.174 1.00 15.55 ? 1843 HOH A O 1 HETATM 6230 O O . HOH T 9 . ? 13.317 77.961 63.728 1.00 21.11 ? 1844 HOH A O 1 HETATM 6231 O O . HOH T 9 . ? 34.478 41.695 50.444 1.00 22.25 ? 1845 HOH A O 1 HETATM 6232 O O . HOH T 9 . ? 26.536 39.043 36.429 1.00 15.33 ? 1846 HOH A O 1 HETATM 6233 O O . HOH T 9 . ? -2.562 59.439 48.600 1.00 22.96 ? 1847 HOH A O 1 HETATM 6234 O O . HOH T 9 . ? 8.797 74.790 66.769 1.00 18.72 ? 1848 HOH A O 1 HETATM 6235 O O . HOH T 9 . ? 24.490 31.848 28.814 1.00 16.91 ? 1849 HOH A O 1 HETATM 6236 O O . HOH T 9 . ? 5.662 62.796 65.107 1.00 24.34 ? 1850 HOH A O 1 HETATM 6237 O O . HOH T 9 . ? 14.433 32.131 29.530 1.00 16.89 ? 1851 HOH A O 1 HETATM 6238 O O . HOH T 9 . ? 12.098 35.123 53.750 1.00 17.71 ? 1852 HOH A O 1 HETATM 6239 O O . HOH T 9 . ? 10.648 37.538 54.549 1.00 23.95 ? 1853 HOH A O 1 HETATM 6240 O O . HOH T 9 . ? 21.299 63.716 61.068 1.00 18.32 ? 1854 HOH A O 1 HETATM 6241 O O . HOH T 9 . ? 3.533 27.773 41.375 1.00 26.84 ? 1855 HOH A O 1 HETATM 6242 O O . HOH T 9 . ? 19.252 60.320 50.133 1.00 23.02 ? 1857 HOH A O 1 HETATM 6243 O O . HOH T 9 . ? 20.296 53.350 47.624 1.00 22.95 ? 1858 HOH A O 1 HETATM 6244 O O . HOH T 9 . ? 31.230 40.041 46.761 1.00 20.11 ? 1859 HOH A O 1 HETATM 6245 O O . HOH T 9 . ? 5.397 78.260 54.597 1.00 21.33 ? 1860 HOH A O 1 HETATM 6246 O O . HOH T 9 . ? 32.268 35.113 59.449 1.00 18.36 ? 1861 HOH A O 1 HETATM 6247 O O . HOH T 9 . ? 21.991 61.735 36.947 1.00 18.42 ? 1862 HOH A O 1 HETATM 6248 O O . HOH T 9 . ? 16.414 72.218 29.757 1.00 16.08 ? 1863 HOH A O 1 HETATM 6249 O O . HOH T 9 . ? 14.692 59.092 74.672 1.00 17.61 ? 1864 HOH A O 1 HETATM 6250 O O . HOH T 9 . ? 29.512 70.578 46.231 1.00 19.61 ? 1865 HOH A O 1 HETATM 6251 O O . HOH T 9 . ? -2.175 55.743 46.246 1.00 23.66 ? 1866 HOH A O 1 HETATM 6252 O O . HOH T 9 . ? 24.042 40.807 69.554 1.00 20.48 ? 1867 HOH A O 1 HETATM 6253 O O . HOH T 9 . ? 5.659 62.944 70.650 1.00 18.09 ? 1868 HOH A O 1 HETATM 6254 O O . HOH T 9 . ? 16.726 68.382 64.413 1.00 18.78 ? 1869 HOH A O 1 HETATM 6255 O O . HOH T 9 . ? 25.186 32.991 68.017 1.00 16.81 ? 1870 HOH A O 1 HETATM 6256 O O . HOH T 9 . ? -6.342 58.911 38.126 1.00 26.66 ? 1871 HOH A O 1 HETATM 6257 O O . HOH T 9 . ? 15.010 61.957 73.220 1.00 20.65 ? 1872 HOH A O 1 HETATM 6258 O O . HOH T 9 . ? 0.175 31.513 58.339 1.00 21.60 ? 1873 HOH A O 1 HETATM 6259 O O . HOH T 9 . ? 18.649 55.540 30.577 1.00 28.01 ? 1874 HOH A O 1 HETATM 6260 O O . HOH T 9 . ? 9.020 69.184 41.006 1.00 20.76 ? 1875 HOH A O 1 HETATM 6261 O O . HOH T 9 . ? 12.244 37.244 28.664 1.00 15.27 ? 1876 HOH A O 1 HETATM 6262 O O . HOH T 9 . ? 0.529 33.514 43.385 1.00 19.54 ? 1877 HOH A O 1 HETATM 6263 O O . HOH T 9 . ? 1.109 63.500 43.063 1.00 27.02 ? 1878 HOH A O 1 HETATM 6264 O O . HOH T 9 . ? 33.959 48.057 59.075 1.00 20.30 ? 1879 HOH A O 1 HETATM 6265 O O . HOH T 9 . ? 17.289 81.860 37.407 1.00 19.34 ? 1880 HOH A O 1 HETATM 6266 O O . HOH T 9 . ? 15.249 69.273 41.708 1.00 22.53 ? 1881 HOH A O 1 HETATM 6267 O O . HOH T 9 . ? 16.482 26.395 34.659 1.00 18.23 ? 1882 HOH A O 1 HETATM 6268 O O . HOH T 9 . ? 23.554 55.412 31.517 1.00 19.90 ? 1883 HOH A O 1 HETATM 6269 O O . HOH T 9 . ? 17.671 82.657 41.263 1.00 24.66 ? 1884 HOH A O 1 HETATM 6270 O O . HOH T 9 . ? 24.108 75.246 54.722 1.00 19.00 ? 1885 HOH A O 1 HETATM 6271 O O . HOH T 9 . ? 23.168 67.668 40.770 1.00 22.61 ? 1886 HOH A O 1 HETATM 6272 O O . HOH T 9 . ? 8.012 51.956 43.015 1.00 24.54 ? 1887 HOH A O 1 HETATM 6273 O O . HOH T 9 . ? 29.970 27.145 33.789 1.00 19.62 ? 1888 HOH A O 1 HETATM 6274 O O . HOH T 9 . ? 6.336 39.149 26.428 1.00 23.82 ? 1889 HOH A O 1 HETATM 6275 O O . HOH T 9 . ? 18.834 69.170 65.946 1.00 23.35 ? 1890 HOH A O 1 HETATM 6276 O O . HOH T 9 . ? 25.896 59.462 46.673 1.00 30.90 ? 1891 HOH A O 1 HETATM 6277 O O . HOH T 9 . ? 21.824 74.710 60.734 1.00 21.58 ? 1892 HOH A O 1 HETATM 6278 O O . HOH T 9 . ? -2.116 34.106 40.601 1.00 20.51 ? 1893 HOH A O 1 HETATM 6279 O O . HOH T 9 . ? 13.444 82.957 55.838 1.00 20.65 ? 1894 HOH A O 1 HETATM 6280 O O . HOH T 9 . ? 25.743 35.664 68.295 1.00 18.28 ? 1895 HOH A O 1 HETATM 6281 O O . HOH T 9 . ? 23.799 73.366 59.416 1.00 20.73 ? 1896 HOH A O 1 HETATM 6282 O O . HOH T 9 . ? -1.290 61.746 62.314 1.00 22.67 ? 1897 HOH A O 1 HETATM 6283 O O . HOH T 9 . ? 10.042 36.131 70.128 1.00 22.47 ? 1898 HOH A O 1 HETATM 6284 O O . HOH T 9 . ? 14.121 57.692 35.257 1.00 23.02 ? 1899 HOH A O 1 HETATM 6285 O O . HOH T 9 . ? 13.672 29.737 28.587 1.00 18.83 ? 1900 HOH A O 1 HETATM 6286 O O . HOH T 9 . ? 36.747 42.590 65.392 1.00 21.53 ? 1901 HOH A O 1 HETATM 6287 O O . HOH T 9 . ? 10.846 29.181 40.472 1.00 21.65 ? 1902 HOH A O 1 HETATM 6288 O O . HOH T 9 . ? 11.800 41.059 55.514 1.00 21.09 ? 1903 HOH A O 1 HETATM 6289 O O . HOH T 9 . ? 19.398 63.740 32.390 1.00 29.14 ? 1904 HOH A O 1 HETATM 6290 O O A HOH T 9 . ? 12.747 53.470 36.353 0.50 22.57 ? 1905 HOH A O 1 HETATM 6291 O O . HOH T 9 . ? 23.415 56.884 45.244 1.00 23.70 ? 1906 HOH A O 1 HETATM 6292 O O . HOH T 9 . ? 21.875 61.327 51.666 1.00 26.00 ? 1907 HOH A O 1 HETATM 6293 O O . HOH T 9 . ? 25.866 27.428 24.383 1.00 21.82 ? 1908 HOH A O 1 HETATM 6294 O O . HOH T 9 . ? 25.724 56.173 37.778 1.00 21.56 ? 1909 HOH A O 1 HETATM 6295 O O . HOH T 9 . ? 20.270 31.629 26.354 1.00 20.33 ? 1910 HOH A O 1 HETATM 6296 O O . HOH T 9 . ? 30.942 52.433 52.774 1.00 23.72 ? 1911 HOH A O 1 HETATM 6297 O O . HOH T 9 . ? 6.557 76.536 67.539 1.00 21.58 ? 1912 HOH A O 1 HETATM 6298 O O . HOH T 9 . ? 10.543 55.676 75.257 1.00 24.01 ? 1913 HOH A O 1 HETATM 6299 O O . HOH T 9 . ? 21.427 32.620 28.729 1.00 18.35 ? 1914 HOH A O 1 HETATM 6300 O O . HOH T 9 . ? 25.477 70.732 31.354 1.00 20.16 ? 1915 HOH A O 1 HETATM 6301 O O . HOH T 9 . ? 19.185 69.730 28.657 1.00 21.55 ? 1916 HOH A O 1 HETATM 6302 O O . HOH T 9 . ? 23.522 79.194 50.712 1.00 20.24 ? 1917 HOH A O 1 HETATM 6303 O O . HOH T 9 . ? -9.779 46.165 34.353 1.00 31.30 ? 1918 HOH A O 1 HETATM 6304 O O . HOH T 9 . ? 29.223 40.405 65.043 1.00 21.09 ? 1919 HOH A O 1 HETATM 6305 O O . HOH T 9 . ? 11.743 28.158 29.222 1.00 24.88 ? 1920 HOH A O 1 HETATM 6306 O O . HOH T 9 . ? 25.269 63.617 50.206 1.00 24.67 ? 1921 HOH A O 1 HETATM 6307 O O . HOH T 9 . ? 16.247 29.336 28.068 1.00 19.82 ? 1922 HOH A O 1 HETATM 6308 O O . HOH T 9 . ? 13.871 80.055 68.131 1.00 24.92 ? 1923 HOH A O 1 HETATM 6309 O O . HOH T 9 . ? 5.174 31.950 30.265 1.00 31.65 ? 1924 HOH A O 1 HETATM 6310 O O . HOH T 9 . ? 14.348 81.452 40.811 1.00 29.73 ? 1925 HOH A O 1 HETATM 6311 O O . HOH T 9 . ? 10.238 81.267 63.784 1.00 24.90 ? 1926 HOH A O 1 HETATM 6312 O O . HOH T 9 . ? 4.235 63.636 72.880 1.00 19.66 ? 1927 HOH A O 1 HETATM 6313 O O . HOH T 9 . ? -10.446 48.765 48.698 1.00 27.04 ? 1928 HOH A O 1 HETATM 6314 O O . HOH T 9 . ? 21.817 84.298 47.218 1.00 21.22 ? 1929 HOH A O 1 HETATM 6315 O O . HOH T 9 . ? 18.006 21.402 38.835 1.00 36.10 ? 1930 HOH A O 1 HETATM 6316 O O . HOH T 9 . ? 20.940 50.640 76.180 1.00 26.37 ? 1932 HOH A O 1 HETATM 6317 O O . HOH T 9 . ? 7.711 38.984 29.340 1.00 22.90 ? 1933 HOH A O 1 HETATM 6318 O O . HOH T 9 . ? 38.363 34.589 26.859 1.00 22.57 ? 1934 HOH A O 1 HETATM 6319 O O . HOH T 9 . ? 4.599 62.192 75.271 1.00 17.97 ? 1935 HOH A O 1 HETATM 6320 O O . HOH T 9 . ? -1.591 32.408 44.799 1.00 27.05 ? 1936 HOH A O 1 HETATM 6321 O O . HOH T 9 . ? -12.852 47.669 37.711 1.00 29.01 ? 1937 HOH A O 1 HETATM 6322 O O . HOH T 9 . ? -9.974 43.977 47.211 1.00 26.73 ? 1940 HOH A O 1 HETATM 6323 O O . HOH T 9 . ? 29.940 25.337 47.458 1.00 27.07 ? 1941 HOH A O 1 HETATM 6324 O O . HOH T 9 . ? 29.644 54.445 35.113 1.00 21.72 ? 1942 HOH A O 1 HETATM 6325 O O . HOH T 9 . ? -0.683 58.330 43.364 1.00 20.87 ? 1944 HOH A O 1 HETATM 6326 O O . HOH T 9 . ? -2.979 38.682 63.174 1.00 27.87 ? 1946 HOH A O 1 HETATM 6327 O O . HOH T 9 . ? 11.607 38.482 56.752 1.00 28.72 ? 1947 HOH A O 1 HETATM 6328 O O . HOH T 9 . ? 25.834 67.128 30.359 1.00 21.37 ? 1948 HOH A O 1 HETATM 6329 O O . HOH T 9 . ? 16.972 69.216 20.895 1.00 41.10 ? 1949 HOH A O 1 HETATM 6330 O O . HOH T 9 . ? 12.160 63.947 35.598 1.00 27.62 ? 1950 HOH A O 1 HETATM 6331 O O . HOH T 9 . ? 25.079 66.064 40.484 1.00 33.86 ? 1951 HOH A O 1 HETATM 6332 O O . HOH T 9 . ? 32.127 55.350 26.699 1.00 23.56 ? 1952 HOH A O 1 HETATM 6333 O O . HOH T 9 . ? 18.115 31.200 29.213 1.00 18.34 ? 1953 HOH A O 1 HETATM 6334 O O . HOH T 9 . ? 28.908 26.154 36.203 1.00 20.31 ? 1954 HOH A O 1 HETATM 6335 O O . HOH T 9 . ? 16.690 79.784 21.218 1.00 30.84 ? 1955 HOH A O 1 HETATM 6336 O O . HOH T 9 . ? 20.002 25.841 36.931 1.00 23.11 ? 1956 HOH A O 1 HETATM 6337 O O . HOH T 9 . ? 28.080 45.384 69.049 1.00 19.32 ? 1957 HOH A O 1 HETATM 6338 O O . HOH T 9 . ? 17.854 52.544 75.082 1.00 22.60 ? 1958 HOH A O 1 HETATM 6339 O O . HOH T 9 . ? 13.235 93.624 40.288 1.00 27.22 ? 1959 HOH A O 1 HETATM 6340 O O . HOH T 9 . ? 25.761 25.722 20.092 1.00 24.40 ? 1962 HOH A O 1 HETATM 6341 O O . HOH T 9 . ? 35.241 51.055 31.560 1.00 27.57 ? 1963 HOH A O 1 HETATM 6342 O O . HOH T 9 . ? 20.728 30.439 29.910 1.00 22.40 ? 1964 HOH A O 1 HETATM 6343 O O . HOH T 9 . ? 12.984 69.655 32.767 1.00 29.76 ? 1965 HOH A O 1 HETATM 6344 O O . HOH T 9 . ? 24.712 29.699 30.367 1.00 19.68 ? 1966 HOH A O 1 HETATM 6345 O O . HOH T 9 . ? 26.673 40.414 13.562 1.00 19.11 ? 1967 HOH A O 1 HETATM 6346 O O . HOH T 9 . ? -2.711 32.962 55.962 1.00 31.38 ? 1968 HOH A O 1 HETATM 6347 O O . HOH T 9 . ? 24.104 82.444 42.500 1.00 29.72 ? 1969 HOH A O 1 HETATM 6348 O O . HOH T 9 . ? 29.263 79.204 27.583 1.00 25.89 ? 1970 HOH A O 1 HETATM 6349 O O . HOH T 9 . ? 10.397 27.327 51.713 1.00 22.61 ? 1971 HOH A O 1 HETATM 6350 O O . HOH T 9 . ? 5.334 40.728 23.231 1.00 26.58 ? 1972 HOH A O 1 HETATM 6351 O O . HOH T 9 . ? 36.137 43.005 57.624 1.00 24.78 ? 1973 HOH A O 1 HETATM 6352 O O . HOH T 9 . ? 36.791 52.453 68.681 1.00 20.75 ? 1974 HOH A O 1 HETATM 6353 O O . HOH T 9 . ? 9.979 69.981 38.695 1.00 26.67 ? 1975 HOH A O 1 HETATM 6354 O O . HOH T 9 . ? 23.019 65.530 66.179 1.00 26.91 ? 1976 HOH A O 1 HETATM 6355 O O . HOH T 9 . ? 27.182 57.144 70.508 1.00 21.41 ? 1977 HOH A O 1 HETATM 6356 O O . HOH T 9 . ? 6.985 75.996 37.709 1.00 26.90 ? 1978 HOH A O 1 HETATM 6357 O O . HOH T 9 . ? 35.010 41.456 19.736 1.00 28.45 ? 1979 HOH A O 1 HETATM 6358 O O . HOH T 9 . ? 39.812 44.050 58.537 1.00 23.62 ? 1980 HOH A O 1 HETATM 6359 O O . HOH T 9 . ? 26.861 16.995 40.028 1.00 34.68 ? 1981 HOH A O 1 HETATM 6360 O O . HOH T 9 . ? 27.961 72.396 53.198 1.00 26.44 ? 1982 HOH A O 1 HETATM 6361 O O . HOH T 9 . ? 5.200 31.773 24.481 1.00 27.08 ? 1984 HOH A O 1 HETATM 6362 O O . HOH T 9 . ? 26.860 60.516 31.029 1.00 33.41 ? 1987 HOH A O 1 HETATM 6363 O O . HOH T 9 . ? -1.599 46.118 55.836 1.00 28.43 ? 1989 HOH A O 1 HETATM 6364 O O . HOH T 9 . ? 1.477 31.258 64.882 1.00 24.25 ? 1990 HOH A O 1 HETATM 6365 O O . HOH T 9 . ? 21.652 25.392 23.920 1.00 23.65 ? 1991 HOH A O 1 HETATM 6366 O O . HOH T 9 . ? 0.658 66.341 63.120 1.00 34.33 ? 1992 HOH A O 1 HETATM 6367 O O . HOH T 9 . ? 24.102 61.515 35.071 1.00 24.83 ? 1993 HOH A O 1 HETATM 6368 O O . HOH T 9 . ? 11.210 76.699 28.640 1.00 28.41 ? 1994 HOH A O 1 HETATM 6369 O O . HOH T 9 . ? 26.320 23.561 45.736 1.00 27.36 ? 1995 HOH A O 1 HETATM 6370 O O . HOH T 9 . ? 20.832 44.335 11.617 1.00 25.14 ? 1996 HOH A O 1 HETATM 6371 O O . HOH T 9 . ? -4.012 37.688 56.658 1.00 29.79 ? 1997 HOH A O 1 HETATM 6372 O O . HOH T 9 . ? 16.200 67.625 72.691 1.00 39.55 ? 1998 HOH A O 1 HETATM 6373 O O . HOH T 9 . ? 5.535 66.313 33.821 1.00 42.14 ? 2000 HOH A O 1 HETATM 6374 O O . HOH T 9 . ? -2.878 38.136 32.601 1.00 24.43 ? 2001 HOH A O 1 HETATM 6375 O O . HOH T 9 . ? 24.241 78.076 53.231 1.00 26.65 ? 2002 HOH A O 1 HETATM 6376 O O . HOH T 9 . ? 20.981 74.598 23.856 1.00 30.27 ? 2003 HOH A O 1 HETATM 6377 O O . HOH T 9 . ? 10.378 51.971 39.903 1.00 20.85 ? 2004 HOH A O 1 HETATM 6378 O O . HOH T 9 . ? 30.760 84.349 28.630 1.00 21.50 ? 2005 HOH A O 1 HETATM 6379 O O . HOH T 9 . ? 26.883 66.294 26.698 1.00 29.14 ? 2007 HOH A O 1 HETATM 6380 O O . HOH T 9 . ? 14.886 23.181 37.598 1.00 29.62 ? 2008 HOH A O 1 HETATM 6381 O O . HOH T 9 . ? 31.740 46.853 36.978 1.00 21.82 ? 2009 HOH A O 1 HETATM 6382 O O . HOH T 9 . ? 28.551 64.007 23.397 1.00 36.15 ? 2010 HOH A O 1 HETATM 6383 O O . HOH T 9 . ? -4.274 53.322 37.301 1.00 27.77 ? 2011 HOH A O 1 HETATM 6384 O O . HOH T 9 . ? 28.666 44.494 65.625 1.00 25.34 ? 2012 HOH A O 1 HETATM 6385 O O . HOH T 9 . ? 8.403 82.573 51.960 1.00 31.92 ? 2013 HOH A O 1 HETATM 6386 O O . HOH T 9 . ? 33.146 30.193 24.566 1.00 24.97 ? 2014 HOH A O 1 HETATM 6387 O O . HOH T 9 . ? 15.145 24.696 58.572 1.00 24.78 ? 2016 HOH A O 1 HETATM 6388 O O . HOH T 9 . ? 4.212 43.827 76.059 1.00 28.62 ? 2017 HOH A O 1 HETATM 6389 O O . HOH T 9 . ? 9.428 52.330 75.272 1.00 25.25 ? 2018 HOH A O 1 HETATM 6390 O O . HOH T 9 . ? 19.034 66.030 28.144 1.00 31.65 ? 2019 HOH A O 1 HETATM 6391 O O . HOH T 9 . ? 17.883 32.354 70.792 1.00 23.93 ? 2020 HOH A O 1 HETATM 6392 O O . HOH T 9 . ? 14.270 50.639 19.054 1.00 26.14 ? 2021 HOH A O 1 HETATM 6393 O O . HOH T 9 . ? 24.330 61.239 51.283 1.00 39.93 ? 2024 HOH A O 1 HETATM 6394 O O . HOH T 9 . ? 17.948 65.394 30.610 1.00 26.95 ? 2025 HOH A O 1 HETATM 6395 O O . HOH T 9 . ? 3.122 27.412 57.226 1.00 36.27 ? 2026 HOH A O 1 HETATM 6396 O O . HOH T 9 . ? 22.060 58.785 69.876 1.00 41.66 ? 2027 HOH A O 1 HETATM 6397 O O . HOH T 9 . ? 25.802 24.840 57.778 1.00 23.07 ? 2029 HOH A O 1 HETATM 6398 O O . HOH T 9 . ? 3.660 27.330 54.759 1.00 24.15 ? 2031 HOH A O 1 HETATM 6399 O O . HOH T 9 . ? 15.106 81.682 28.534 1.00 33.36 ? 2032 HOH A O 1 HETATM 6400 O O . HOH T 9 . ? 23.660 45.440 39.324 1.00 32.68 ? 2033 HOH A O 1 HETATM 6401 O O . HOH T 9 . ? -4.391 54.105 34.592 1.00 33.98 ? 2034 HOH A O 1 HETATM 6402 O O . HOH T 9 . ? 21.608 75.415 67.111 1.00 35.25 ? 2035 HOH A O 1 HETATM 6403 O O . HOH T 9 . ? 34.571 32.785 27.601 1.00 23.16 ? 2036 HOH A O 1 HETATM 6404 O O . HOH T 9 . ? 21.273 88.729 44.263 1.00 22.40 ? 2038 HOH A O 1 HETATM 6405 O O . HOH T 9 . ? -4.380 37.183 51.677 1.00 40.85 ? 2039 HOH A O 1 HETATM 6406 O O . HOH T 9 . ? 33.916 28.943 34.276 1.00 28.25 ? 2040 HOH A O 1 HETATM 6407 O O . HOH T 9 . ? -5.962 41.642 44.341 1.00 32.63 ? 2041 HOH A O 1 HETATM 6408 O O . HOH T 9 . ? 8.894 78.813 49.804 1.00 33.93 ? 2042 HOH A O 1 HETATM 6409 O O . HOH T 9 . ? 14.133 65.395 36.341 1.00 36.92 ? 2043 HOH A O 1 HETATM 6410 O O . HOH T 9 . ? 33.787 40.129 47.644 1.00 28.24 ? 2044 HOH A O 1 HETATM 6411 O O . HOH T 9 . ? 11.922 50.335 36.929 1.00 32.61 ? 2045 HOH A O 1 HETATM 6412 O O . HOH T 9 . ? 31.450 31.952 17.265 1.00 19.64 ? 2046 HOH A O 1 HETATM 6413 O O . HOH T 9 . ? 30.748 59.955 25.643 1.00 25.04 ? 2047 HOH A O 1 HETATM 6414 O O . HOH T 9 . ? 5.491 53.294 77.865 1.00 32.77 ? 2048 HOH A O 1 HETATM 6415 O O . HOH T 9 . ? 12.674 43.977 17.279 1.00 24.57 ? 2049 HOH A O 1 HETATM 6416 O O . HOH T 9 . ? 26.727 69.428 29.266 1.00 28.44 ? 2050 HOH A O 1 HETATM 6417 O O A HOH T 9 . ? -5.133 42.216 50.674 0.50 17.89 ? 2051 HOH A O 1 HETATM 6418 O O B HOH T 9 . ? -4.438 43.769 50.059 0.50 27.60 ? 2051 HOH A O 1 HETATM 6419 O O . HOH T 9 . ? 36.604 43.124 49.566 1.00 26.75 ? 2052 HOH A O 1 HETATM 6420 O O . HOH T 9 . ? 19.629 58.433 68.769 1.00 39.72 ? 2053 HOH A O 1 HETATM 6421 O O . HOH T 9 . ? 13.584 28.333 17.018 1.00 29.95 ? 2054 HOH A O 1 HETATM 6422 O O . HOH T 9 . ? -3.264 47.172 53.312 1.00 29.81 ? 2055 HOH A O 1 HETATM 6423 O O . HOH T 9 . ? -7.271 48.344 48.149 1.00 36.63 ? 2056 HOH A O 1 HETATM 6424 O O . HOH T 9 . ? 10.053 24.455 54.328 1.00 30.83 ? 2057 HOH A O 1 HETATM 6425 O O . HOH T 9 . ? -0.911 32.366 60.645 1.00 30.54 ? 2059 HOH A O 1 HETATM 6426 O O . HOH T 9 . ? 16.243 79.397 69.283 1.00 33.24 ? 2060 HOH A O 1 HETATM 6427 O O . HOH T 9 . ? -8.664 41.609 48.035 1.00 31.07 ? 2061 HOH A O 1 HETATM 6428 O O . HOH T 9 . ? 20.094 56.286 23.262 1.00 26.83 ? 2062 HOH A O 1 HETATM 6429 O O . HOH T 9 . ? 32.943 43.054 20.391 1.00 26.90 ? 2063 HOH A O 1 HETATM 6430 O O . HOH T 9 . ? 21.258 24.128 51.261 1.00 30.11 ? 2064 HOH A O 1 HETATM 6431 O O . HOH T 9 . ? 16.831 63.648 69.047 1.00 34.19 ? 2065 HOH A O 1 HETATM 6432 O O . HOH T 9 . ? 29.297 28.086 59.605 1.00 37.29 ? 2067 HOH A O 1 HETATM 6433 O O . HOH T 9 . ? 27.226 20.290 39.907 1.00 23.37 ? 2068 HOH A O 1 HETATM 6434 O O . HOH T 9 . ? 5.158 27.725 30.744 1.00 36.10 ? 2069 HOH A O 1 HETATM 6435 O O . HOH T 9 . ? 5.423 81.851 54.041 1.00 37.00 ? 2071 HOH A O 1 HETATM 6436 O O . HOH T 9 . ? 8.318 29.709 33.396 1.00 30.87 ? 2072 HOH A O 1 HETATM 6437 O O . HOH T 9 . ? -1.129 51.677 72.755 1.00 25.31 ? 2073 HOH A O 1 HETATM 6438 O O . HOH T 9 . ? 39.164 31.216 45.767 1.00 32.89 ? 2074 HOH A O 1 HETATM 6439 O O . HOH T 9 . ? 37.345 61.117 55.723 0.50 26.93 ? 2075 HOH A O 1 HETATM 6440 O O . HOH T 9 . ? 8.947 56.670 43.831 1.00 28.84 ? 2076 HOH A O 1 HETATM 6441 O O . HOH T 9 . ? 23.148 75.923 25.564 1.00 25.41 ? 2077 HOH A O 1 HETATM 6442 O O . HOH T 9 . ? 6.082 68.625 37.209 1.00 30.86 ? 2078 HOH A O 1 HETATM 6443 O O . HOH T 9 . ? 12.343 28.027 21.404 1.00 27.39 ? 2079 HOH A O 1 HETATM 6444 O O . HOH T 9 . ? 29.242 28.560 24.966 1.00 29.19 ? 2080 HOH A O 1 HETATM 6445 O O . HOH T 9 . ? 38.724 55.353 62.206 1.00 28.38 ? 2081 HOH A O 1 HETATM 6446 O O . HOH T 9 . ? 12.990 71.959 80.322 1.00 27.67 ? 2082 HOH A O 1 HETATM 6447 O O . HOH T 9 . ? 11.688 81.247 61.423 1.00 30.67 ? 2083 HOH A O 1 HETATM 6448 O O . HOH T 9 . ? 1.380 37.095 68.659 1.00 25.89 ? 2084 HOH A O 1 HETATM 6449 O O . HOH T 9 . ? 42.652 31.077 41.206 1.00 31.26 ? 2085 HOH A O 1 HETATM 6450 O O . HOH T 9 . ? 12.879 33.063 71.033 1.00 25.80 ? 2088 HOH A O 1 HETATM 6451 O O . HOH T 9 . ? 3.674 31.515 38.679 1.00 37.59 ? 2089 HOH A O 1 HETATM 6452 O O . HOH T 9 . ? 15.044 73.149 23.683 1.00 43.87 ? 2090 HOH A O 1 HETATM 6453 O O . HOH T 9 . ? 18.929 40.771 76.222 1.00 23.25 ? 2091 HOH A O 1 HETATM 6454 O O . HOH T 9 . ? 20.140 45.967 79.215 1.00 26.59 ? 2092 HOH A O 1 HETATM 6455 O O . HOH T 9 . ? 5.781 56.700 35.761 1.00 32.02 ? 2093 HOH A O 1 HETATM 6456 O O . HOH T 9 . ? 23.550 60.343 40.060 1.00 29.34 ? 2096 HOH A O 1 HETATM 6457 O O . HOH T 9 . ? 30.712 71.788 43.800 1.00 27.22 ? 2097 HOH A O 1 HETATM 6458 O O . HOH T 9 . ? 8.515 74.940 75.621 1.00 30.32 ? 2098 HOH A O 1 HETATM 6459 O O . HOH T 9 . ? 3.186 38.879 27.017 1.00 34.22 ? 2100 HOH A O 1 HETATM 6460 O O . HOH T 9 . ? 38.882 38.650 35.504 1.00 29.16 ? 2101 HOH A O 1 HETATM 6461 O O . HOH T 9 . ? 18.083 59.850 70.243 1.00 37.99 ? 2102 HOH A O 1 HETATM 6462 O O . HOH T 9 . ? 38.383 43.086 55.438 1.00 36.57 ? 2103 HOH A O 1 HETATM 6463 O O . HOH T 9 . ? 26.836 31.099 64.088 1.00 42.41 ? 2105 HOH A O 1 HETATM 6464 O O . HOH T 9 . ? 25.230 86.067 42.683 1.00 24.15 ? 2106 HOH A O 1 HETATM 6465 O O . HOH T 9 . ? -14.175 42.621 41.572 1.00 36.23 ? 2108 HOH A O 1 HETATM 6466 O O . HOH T 9 . ? 22.001 80.876 23.014 1.00 30.53 ? 2109 HOH A O 1 HETATM 6467 O O . HOH T 9 . ? 40.868 45.294 20.009 1.00 23.37 ? 2110 HOH A O 1 HETATM 6468 O O . HOH T 9 . ? 10.605 36.726 76.548 1.00 26.83 ? 2111 HOH A O 1 HETATM 6469 O O . HOH T 9 . ? 28.347 53.764 37.407 1.00 23.85 ? 2113 HOH A O 1 HETATM 6470 O O . HOH T 9 . ? 28.544 61.226 68.470 1.00 31.95 ? 2115 HOH A O 1 HETATM 6471 O O . HOH T 9 . ? 24.445 23.042 53.334 1.00 33.86 ? 2117 HOH A O 1 HETATM 6472 O O . HOH T 9 . ? 25.286 66.699 56.809 1.00 29.02 ? 2118 HOH A O 1 HETATM 6473 O O . HOH T 9 . ? 15.427 25.813 30.036 1.00 33.62 ? 2119 HOH A O 1 HETATM 6474 O O . HOH T 9 . ? 30.958 61.573 23.357 1.00 29.76 ? 2120 HOH A O 1 HETATM 6475 O O . HOH T 9 . ? 7.807 58.107 33.648 1.00 35.67 ? 2122 HOH A O 1 HETATM 6476 O O . HOH T 9 . ? 15.195 73.168 78.862 1.00 42.46 ? 2123 HOH A O 1 HETATM 6477 O O . HOH T 9 . ? 6.698 42.929 27.435 1.00 29.80 ? 2124 HOH A O 1 HETATM 6478 O O . HOH T 9 . ? 35.233 44.291 68.295 1.00 27.97 ? 2125 HOH A O 1 HETATM 6479 O O . HOH T 9 . ? 31.061 35.842 16.986 1.00 27.11 ? 2126 HOH A O 1 HETATM 6480 O O . HOH T 9 . ? 37.154 25.955 47.949 1.00 36.01 ? 2127 HOH A O 1 HETATM 6481 O O . HOH T 9 . ? 12.091 29.620 19.105 1.00 26.66 ? 2128 HOH A O 1 HETATM 6482 O O . HOH T 9 . ? 27.099 28.480 28.363 1.00 36.70 ? 2129 HOH A O 1 HETATM 6483 O O . HOH T 9 . ? 15.682 55.010 72.409 1.00 37.48 ? 2130 HOH A O 1 HETATM 6484 O O . HOH T 9 . ? 6.262 96.021 42.402 1.00 39.42 ? 2131 HOH A O 1 HETATM 6485 O O . HOH T 9 . ? 9.508 75.152 69.716 1.00 34.88 ? 2132 HOH A O 1 HETATM 6486 O O . HOH T 9 . ? 10.420 84.254 51.365 1.00 32.62 ? 2133 HOH A O 1 HETATM 6487 O O . HOH T 9 . ? 40.914 32.230 39.550 1.00 21.84 ? 2134 HOH A O 1 HETATM 6488 O O . HOH T 9 . ? 30.206 76.149 43.422 1.00 34.78 ? 2135 HOH A O 1 HETATM 6489 O O . HOH T 9 . ? 1.010 64.127 38.636 1.00 47.64 ? 2136 HOH A O 1 HETATM 6490 O O . HOH T 9 . ? 25.304 65.161 44.758 1.00 27.13 ? 2137 HOH A O 1 HETATM 6491 O O . HOH T 9 . ? 25.366 56.903 32.647 1.00 28.55 ? 2138 HOH A O 1 HETATM 6492 O O . HOH T 9 . ? 32.491 85.152 32.578 1.00 34.48 ? 2139 HOH A O 1 HETATM 6493 O O . HOH T 9 . ? 39.263 57.688 57.753 1.00 30.76 ? 2140 HOH A O 1 HETATM 6494 O O . HOH T 9 . ? 8.588 54.647 31.521 1.00 45.13 ? 2142 HOH A O 1 HETATM 6495 O O . HOH T 9 . ? 23.843 24.788 30.515 1.00 30.12 ? 2143 HOH A O 1 HETATM 6496 O O . HOH T 9 . ? 6.188 45.167 25.639 1.00 44.91 ? 2144 HOH A O 1 HETATM 6497 O O . HOH T 9 . ? 4.917 63.952 76.918 1.00 25.46 ? 2145 HOH A O 1 HETATM 6498 O O . HOH T 9 . ? 17.260 25.855 59.632 1.00 21.13 ? 2146 HOH A O 1 HETATM 6499 O O . HOH T 9 . ? 0.015 29.937 44.856 1.00 43.64 ? 2147 HOH A O 1 HETATM 6500 O O . HOH T 9 . ? 2.690 63.588 40.611 1.00 32.48 ? 2148 HOH A O 1 HETATM 6501 O O . HOH T 9 . ? -4.244 44.133 27.764 1.00 49.09 ? 2151 HOH A O 1 HETATM 6502 O O . HOH T 9 . ? 21.314 24.264 26.922 1.00 26.86 ? 2152 HOH A O 1 HETATM 6503 O O . HOH T 9 . ? 34.548 46.150 69.966 1.00 32.11 ? 2153 HOH A O 1 HETATM 6504 O O . HOH T 9 . ? 42.450 34.711 38.353 1.00 28.53 ? 2155 HOH A O 1 HETATM 6505 O O . HOH T 9 . ? 29.387 73.181 50.040 1.00 32.90 ? 2156 HOH A O 1 HETATM 6506 O O . HOH T 9 . ? 22.250 83.743 49.976 1.00 27.05 ? 2158 HOH A O 1 HETATM 6507 O O . HOH T 9 . ? 12.395 81.238 69.970 0.50 20.11 ? 2159 HOH A O 1 HETATM 6508 O O . HOH T 9 . ? 24.326 82.366 24.509 1.00 32.96 ? 2160 HOH A O 1 HETATM 6509 O O . HOH T 9 . ? 29.697 30.686 15.271 1.00 27.73 ? 2161 HOH A O 1 HETATM 6510 O O . HOH T 9 . ? 35.940 34.296 51.352 1.00 34.49 ? 2162 HOH A O 1 HETATM 6511 O O . HOH T 9 . ? 24.260 83.744 45.897 1.00 35.55 ? 2163 HOH A O 1 HETATM 6512 O O . HOH T 9 . ? 26.381 62.491 65.714 1.00 31.81 ? 2164 HOH A O 1 HETATM 6513 O O . HOH T 9 . ? 5.504 79.161 38.600 1.00 31.07 ? 2167 HOH A O 1 HETATM 6514 O O . HOH T 9 . ? 24.673 68.341 63.196 1.00 41.94 ? 2169 HOH A O 1 HETATM 6515 O O . HOH T 9 . ? 37.105 48.398 30.451 1.00 35.25 ? 2170 HOH A O 1 HETATM 6516 O O . HOH T 9 . ? 30.823 72.107 48.016 1.00 33.61 ? 2171 HOH A O 1 HETATM 6517 O O . HOH T 9 . ? -5.027 44.731 31.044 1.00 33.70 ? 2172 HOH A O 1 HETATM 6518 O O . HOH T 9 . ? 27.054 65.182 34.911 1.00 34.28 ? 2173 HOH A O 1 HETATM 6519 O O . HOH T 9 . ? 17.888 64.738 67.210 1.00 31.81 ? 2174 HOH A O 1 HETATM 6520 O O . HOH T 9 . ? 27.352 63.258 63.280 1.00 39.34 ? 2175 HOH A O 1 HETATM 6521 O O . HOH T 9 . ? 33.961 53.349 32.380 1.00 30.81 ? 2179 HOH A O 1 HETATM 6522 O O . HOH T 9 . ? 30.983 70.597 37.556 1.00 35.81 ? 2180 HOH A O 1 HETATM 6523 O O . HOH T 9 . ? 22.422 80.683 57.378 1.00 30.33 ? 2181 HOH A O 1 HETATM 6524 O O . HOH T 9 . ? 3.006 65.107 51.005 1.00 28.04 ? 2183 HOH A O 1 HETATM 6525 O O . HOH T 9 . ? -8.255 49.537 50.131 1.00 33.90 ? 2184 HOH A O 1 HETATM 6526 O O . HOH T 9 . ? -4.233 58.277 36.382 1.00 33.62 ? 2185 HOH A O 1 HETATM 6527 O O . HOH T 9 . ? 9.471 28.792 38.005 1.00 33.46 ? 2186 HOH A O 1 HETATM 6528 O O . HOH T 9 . ? 15.311 25.108 32.601 1.00 30.18 ? 2187 HOH A O 1 HETATM 6529 O O . HOH T 9 . ? -1.808 63.724 48.971 1.00 29.67 ? 2188 HOH A O 1 HETATM 6530 O O . HOH T 9 . ? 29.116 25.792 31.608 1.00 26.04 ? 2189 HOH A O 1 HETATM 6531 O O . HOH T 9 . ? 26.967 65.022 29.061 1.00 30.01 ? 2190 HOH A O 1 HETATM 6532 O O . HOH T 9 . ? 25.675 68.133 32.891 1.00 25.89 ? 2191 HOH A O 1 HETATM 6533 O O . HOH T 9 . ? 28.130 63.770 57.557 1.00 41.14 ? 2192 HOH A O 1 HETATM 6534 O O . HOH T 9 . ? 29.780 67.818 45.657 1.00 33.62 ? 2193 HOH A O 1 HETATM 6535 O O . HOH T 9 . ? 27.460 66.266 46.434 1.00 28.94 ? 2195 HOH A O 1 HETATM 6536 O O . HOH T 9 . ? 34.710 35.570 58.546 1.00 32.56 ? 2197 HOH A O 1 HETATM 6537 O O . HOH T 9 . ? 24.433 79.647 55.270 1.00 37.06 ? 2198 HOH A O 1 HETATM 6538 O O . HOH T 9 . ? 21.576 56.739 25.392 1.00 28.27 ? 2200 HOH A O 1 HETATM 6539 O O . HOH T 9 . ? 36.009 37.593 57.183 1.00 33.63 ? 2201 HOH A O 1 HETATM 6540 O O . HOH T 9 . ? 28.241 35.974 67.609 1.00 30.19 ? 2202 HOH A O 1 HETATM 6541 O O . HOH T 9 . ? 29.585 37.953 66.427 1.00 26.33 ? 2203 HOH A O 1 HETATM 6542 O O . HOH T 9 . ? 13.849 80.701 63.127 1.00 30.98 ? 2204 HOH A O 1 HETATM 6543 O O . HOH T 9 . ? 11.839 73.837 81.799 1.00 31.02 ? 2205 HOH A O 1 HETATM 6544 O O . HOH T 9 . ? 35.331 49.156 33.483 1.00 25.39 ? 2206 HOH A O 1 HETATM 6545 O O . HOH T 9 . ? 38.037 41.522 37.156 1.00 28.08 ? 2207 HOH A O 1 HETATM 6546 O O . HOH T 9 . ? -3.778 32.677 53.307 1.00 39.47 ? 2208 HOH A O 1 HETATM 6547 O O . HOH T 9 . ? 14.910 70.236 81.927 1.00 25.15 ? 2210 HOH A O 1 HETATM 6548 O O . HOH T 9 . ? 25.679 71.916 60.878 1.00 39.04 ? 2212 HOH A O 1 HETATM 6549 O O . HOH T 9 . ? 23.422 74.727 65.650 1.00 29.87 ? 2213 HOH A O 1 HETATM 6550 O O . HOH T 9 . ? 14.671 70.152 30.328 1.00 30.30 ? 2214 HOH A O 1 HETATM 6551 O O . HOH T 9 . ? 11.111 27.576 31.842 1.00 38.27 ? 2216 HOH A O 1 HETATM 6552 O O . HOH T 9 . ? 16.461 85.013 40.861 1.00 36.35 ? 2217 HOH A O 1 HETATM 6553 O O . HOH T 9 . ? -1.833 44.887 58.734 1.00 37.26 ? 2218 HOH A O 1 HETATM 6554 O O . HOH T 9 . ? 28.960 63.856 68.838 1.00 35.68 ? 2219 HOH A O 1 HETATM 6555 O O . HOH T 9 . ? 31.286 70.147 41.790 1.00 28.91 ? 2220 HOH A O 1 HETATM 6556 O O . HOH T 9 . ? 27.284 65.342 38.544 1.00 44.22 ? 2221 HOH A O 1 HETATM 6557 O O . HOH T 9 . ? -5.400 34.187 47.478 1.00 32.83 ? 2222 HOH A O 1 HETATM 6558 O O . HOH T 9 . ? 12.897 50.579 27.669 1.00 34.39 ? 2223 HOH A O 1 HETATM 6559 O O . HOH T 9 . ? 13.621 81.602 66.002 1.00 35.41 ? 2225 HOH A O 1 HETATM 6560 O O . HOH T 9 . ? 7.641 26.661 54.660 1.00 38.81 ? 2227 HOH A O 1 HETATM 6561 O O . HOH T 9 . ? 18.409 58.356 29.950 1.00 39.62 ? 2229 HOH A O 1 HETATM 6562 O O . HOH T 9 . ? 21.037 79.598 65.870 1.00 36.05 ? 2230 HOH A O 1 HETATM 6563 O O . HOH T 9 . ? 5.237 30.292 37.136 1.00 42.46 ? 2231 HOH A O 1 HETATM 6564 O O . HOH T 9 . ? 16.816 71.123 79.282 1.00 32.80 ? 2232 HOH A O 1 HETATM 6565 O O . HOH T 9 . ? 1.104 32.064 67.496 1.00 32.55 ? 2233 HOH A O 1 HETATM 6566 O O . HOH T 9 . ? 28.634 29.688 62.377 1.00 34.61 ? 2234 HOH A O 1 HETATM 6567 O O . HOH T 9 . ? 15.811 82.812 57.481 1.00 48.12 ? 2235 HOH A O 1 HETATM 6568 O O . HOH T 9 . ? 37.086 56.958 63.897 1.00 28.87 ? 2236 HOH A O 1 HETATM 6569 O O . HOH T 9 . ? 15.107 30.626 67.166 1.00 49.70 ? 2238 HOH A O 1 HETATM 6570 O O . HOH T 9 . ? 12.567 28.633 60.726 1.00 34.52 ? 2241 HOH A O 1 HETATM 6571 O O . HOH T 9 . ? 11.106 41.580 17.759 1.00 33.80 ? 2242 HOH A O 1 HETATM 6572 O O . HOH T 9 . ? 32.425 26.272 33.980 1.00 33.54 ? 2244 HOH A O 1 HETATM 6573 O O . HOH T 9 . ? 21.416 73.405 69.062 1.00 36.38 ? 2245 HOH A O 1 HETATM 6574 O O . HOH T 9 . ? 32.598 27.635 56.435 1.00 27.82 ? 2246 HOH A O 1 HETATM 6575 O O . HOH T 9 . ? 19.133 54.347 73.179 1.00 33.82 ? 2247 HOH A O 1 HETATM 6576 O O . HOH T 9 . ? 25.965 74.733 58.442 1.00 33.69 ? 2249 HOH A O 1 HETATM 6577 O O . HOH T 9 . ? -9.029 46.470 32.052 0.50 29.16 ? 2250 HOH A O 1 HETATM 6578 O O . HOH T 9 . ? 27.489 62.226 29.146 1.00 35.54 ? 2251 HOH A O 1 HETATM 6579 O O . HOH T 9 . ? 30.185 42.119 66.657 1.00 28.16 ? 2252 HOH A O 1 HETATM 6580 O O . HOH T 9 . ? 27.306 25.983 22.343 1.00 30.35 ? 2253 HOH A O 1 HETATM 6581 O O . HOH T 9 . ? 29.156 64.476 25.916 1.00 26.08 ? 2254 HOH A O 1 HETATM 6582 O O . HOH T 9 . ? 39.927 57.106 60.181 1.00 37.24 ? 2256 HOH A O 1 HETATM 6583 O O . HOH T 9 . ? 7.436 81.774 62.885 1.00 46.96 ? 2257 HOH A O 1 HETATM 6584 O O . HOH T 9 . ? 35.721 31.663 53.697 1.00 39.23 ? 2258 HOH A O 1 HETATM 6585 O O . HOH T 9 . ? 28.632 56.776 34.354 1.00 34.31 ? 2259 HOH A O 1 HETATM 6586 O O . HOH T 9 . ? 26.330 75.059 55.805 1.00 35.55 ? 2260 HOH A O 1 HETATM 6587 O O . HOH T 9 . ? -9.134 45.923 48.784 1.00 39.17 ? 2261 HOH A O 1 HETATM 6588 O O . HOH T 9 . ? -3.901 47.056 24.987 1.00 38.49 ? 2264 HOH A O 1 HETATM 6589 O O . HOH T 9 . ? 40.593 45.569 17.026 1.00 20.80 ? 2265 HOH A O 1 HETATM 6590 O O . HOH T 9 . ? 24.511 81.895 50.575 1.00 35.20 ? 2266 HOH A O 1 HETATM 6591 O O . HOH T 9 . ? 33.715 27.038 36.225 1.00 37.83 ? 2271 HOH A O 1 HETATM 6592 O O . HOH T 9 . ? 15.628 30.242 12.835 1.00 28.71 ? 2273 HOH A O 1 HETATM 6593 O O . HOH T 9 . ? -5.181 36.424 40.724 1.00 42.26 ? 2274 HOH A O 1 HETATM 6594 O O . HOH T 9 . ? 14.264 72.143 25.952 1.00 42.67 ? 2275 HOH A O 1 HETATM 6595 O O . HOH T 9 . ? 2.277 66.950 37.132 1.00 45.96 ? 2276 HOH A O 1 HETATM 6596 O O . HOH T 9 . ? -5.598 50.960 28.490 1.00 40.40 ? 2277 HOH A O 1 HETATM 6597 O O . HOH T 9 . ? 31.861 74.100 44.250 1.00 38.08 ? 2278 HOH A O 1 HETATM 6598 O O . HOH T 9 . ? 34.113 55.192 67.948 1.00 35.93 ? 2279 HOH A O 1 HETATM 6599 O O . HOH T 9 . ? 19.749 41.672 78.394 1.00 32.93 ? 2281 HOH A O 1 HETATM 6600 O O . HOH T 9 . ? -12.486 45.859 35.525 1.00 39.15 ? 2282 HOH A O 1 HETATM 6601 O O . HOH T 9 . ? 28.445 42.066 68.739 1.00 28.82 ? 2284 HOH A O 1 HETATM 6602 O O . HOH T 9 . ? 16.845 20.908 51.863 1.00 32.58 ? 2285 HOH A O 1 HETATM 6603 O O . HOH T 9 . ? 20.415 57.928 27.734 1.00 33.07 ? 2286 HOH A O 1 HETATM 6604 O O . HOH T 9 . ? 4.111 78.889 68.962 1.00 34.60 ? 2287 HOH A O 1 HETATM 6605 O O . HOH T 9 . ? 40.686 41.586 26.959 1.00 23.97 ? 2288 HOH A O 1 HETATM 6606 O O . HOH T 9 . ? 32.513 41.667 67.671 1.00 30.79 ? 2289 HOH A O 1 HETATM 6607 O O . HOH T 9 . ? 25.059 43.205 71.595 1.00 39.76 ? 2290 HOH A O 1 HETATM 6608 O O . HOH T 9 . ? -0.396 41.023 71.505 1.00 39.93 ? 2291 HOH A O 1 HETATM 6609 O O . HOH T 9 . ? 16.163 68.153 29.565 1.00 36.93 ? 2292 HOH A O 1 HETATM 6610 O O . HOH T 9 . ? 10.418 26.989 36.431 1.00 47.87 ? 2294 HOH A O 1 HETATM 6611 O O . HOH T 9 . ? 14.171 68.940 75.560 1.00 30.38 ? 2296 HOH A O 1 HETATM 6612 O O . HOH T 9 . ? -8.716 43.465 35.088 1.00 37.98 ? 2298 HOH A O 1 HETATM 6613 O O . HOH T 9 . ? 1.952 41.249 27.057 1.00 42.23 ? 2299 HOH A O 1 HETATM 6614 O O . HOH T 9 . ? 32.169 74.796 36.742 1.00 33.98 ? 2301 HOH A O 1 HETATM 6615 O O . HOH T 9 . ? -4.392 35.198 56.886 1.00 42.38 ? 2302 HOH A O 1 HETATM 6616 O O . HOH T 9 . ? 34.044 54.319 28.671 1.00 31.85 ? 2303 HOH A O 1 HETATM 6617 O O . HOH T 9 . ? 30.875 61.618 64.187 1.00 36.94 ? 2304 HOH A O 1 HETATM 6618 O O . HOH T 9 . ? 9.693 47.424 80.078 1.00 41.01 ? 2305 HOH A O 1 HETATM 6619 O O . HOH T 9 . ? 8.802 22.685 46.843 1.00 42.88 ? 2307 HOH A O 1 HETATM 6620 O O . HOH T 9 . ? 30.394 25.893 38.433 1.00 35.57 ? 2310 HOH A O 1 HETATM 6621 O O . HOH T 9 . ? 18.121 24.212 36.129 1.00 32.83 ? 2311 HOH A O 1 HETATM 6622 O O . HOH T 9 . ? 35.660 33.971 55.031 1.00 33.78 ? 2316 HOH A O 1 HETATM 6623 O O . HOH T 9 . ? 26.850 63.592 47.557 1.00 40.83 ? 2317 HOH A O 1 HETATM 6624 O O . HOH T 9 . ? 17.353 66.275 70.754 1.00 44.46 ? 2319 HOH A O 1 HETATM 6625 O O . HOH T 9 . ? 15.758 78.315 72.242 1.00 37.31 ? 2322 HOH A O 1 HETATM 6626 O O . HOH T 9 . ? -6.862 40.252 37.767 1.00 45.62 ? 2325 HOH A O 1 HETATM 6627 O O . HOH T 9 . ? 25.741 63.194 38.744 1.00 37.90 ? 2329 HOH A O 1 HETATM 6628 O O . HOH T 9 . ? 42.797 39.387 64.524 0.50 22.90 ? 2331 HOH A O 1 HETATM 6629 O O . HOH T 9 . ? 38.938 38.991 64.859 1.00 29.32 ? 2333 HOH A O 1 HETATM 6630 O O . HOH T 9 . ? 14.514 40.779 12.202 0.50 20.84 ? 2334 HOH A O 1 HETATM 6631 O O . HOH T 9 . ? -3.535 32.824 42.437 1.00 39.03 ? 2337 HOH A O 1 HETATM 6632 O O . HOH T 9 . ? 25.291 69.371 60.741 1.00 39.61 ? 2340 HOH A O 1 HETATM 6633 O O . HOH T 9 . ? 12.375 25.146 32.902 1.00 39.89 ? 2348 HOH A O 1 HETATM 6634 O O . HOH T 9 . ? 5.986 53.716 30.266 1.00 45.74 ? 2349 HOH A O 1 HETATM 6635 O O . HOH T 9 . ? -0.146 60.680 48.465 1.00 32.92 ? 2350 HOH A O 1 HETATM 6636 O O . HOH T 9 . ? 8.048 56.553 75.855 1.00 20.35 ? 2353 HOH A O 1 HETATM 6637 O O . HOH T 9 . ? 6.798 53.999 75.653 1.00 19.77 ? 2354 HOH A O 1 HETATM 6638 O O . HOH T 9 . ? 11.303 52.520 28.407 1.00 52.32 ? 2356 HOH A O 1 HETATM 6639 O O . HOH T 9 . ? 29.549 61.129 52.538 1.00 31.47 ? 2357 HOH A O 1 HETATM 6640 O O . HOH T 9 . ? 36.368 31.563 34.019 1.00 29.87 ? 2362 HOH A O 1 HETATM 6641 O O . HOH T 9 . ? -2.022 41.439 30.418 1.00 49.38 ? 2363 HOH A O 1 HETATM 6642 O O . HOH T 9 . ? 38.992 35.625 19.546 0.50 15.09 ? 2365 HOH A O 1 HETATM 6643 O O . HOH T 9 . ? 36.762 46.548 32.107 1.00 27.36 ? 2366 HOH A O 1 HETATM 6644 O O . HOH T 9 . ? 27.090 64.621 59.873 1.00 43.58 ? 2369 HOH A O 1 HETATM 6645 O O . HOH T 9 . ? 8.931 94.110 54.390 1.00 40.69 ? 2375 HOH A O 1 HETATM 6646 O O . HOH T 9 . ? 6.629 93.925 53.373 1.00 35.42 ? 2376 HOH A O 1 HETATM 6647 O O . HOH T 9 . ? 8.039 27.362 50.635 1.00 41.77 ? 2377 HOH A O 1 HETATM 6648 O O . HOH T 9 . ? 3.976 64.276 34.901 1.00 37.42 ? 2378 HOH A O 1 HETATM 6649 O O . HOH T 9 . ? 38.238 34.247 48.710 1.00 34.75 ? 2387 HOH A O 1 HETATM 6650 O O . HOH T 9 . ? 11.747 55.209 26.807 1.00 42.42 ? 2388 HOH A O 1 HETATM 6651 O O . HOH T 9 . ? 39.904 42.535 14.684 1.00 23.32 ? 2389 HOH A O 1 HETATM 6652 O O . HOH T 9 . ? 27.543 65.985 55.299 1.00 33.22 ? 2398 HOH A O 1 HETATM 6653 O O . HOH T 9 . ? 25.821 57.169 35.042 1.00 32.31 ? 2403 HOH A O 1 HETATM 6654 O O . HOH T 9 . ? 29.190 60.787 49.918 1.00 47.52 ? 2410 HOH A O 1 HETATM 6655 O O . HOH T 9 . ? -7.521 41.923 40.986 1.00 30.82 ? 2415 HOH A O 1 HETATM 6656 O O . HOH T 9 . ? 23.271 78.497 22.957 1.00 33.21 ? 2416 HOH A O 1 HETATM 6657 O O . HOH T 9 . ? 15.806 86.152 35.358 1.00 32.81 ? 2418 HOH A O 1 HETATM 6658 O O . HOH T 9 . ? 29.784 34.693 65.154 1.00 37.68 ? 2430 HOH A O 1 HETATM 6659 O O . HOH T 9 . ? 18.489 68.327 74.994 1.00 28.32 ? 2432 HOH A O 1 HETATM 6660 O O . HOH T 9 . ? 1.275 59.546 46.477 1.00 25.36 ? 2433 HOH A O 1 HETATM 6661 O O . HOH T 9 . ? 19.546 53.782 45.278 1.00 28.40 ? 2434 HOH A O 1 HETATM 6662 O O . HOH T 9 . ? 28.057 54.482 50.328 1.00 31.81 ? 2435 HOH A O 1 HETATM 6663 O O . HOH T 9 . ? 23.027 58.673 24.485 1.00 30.81 ? 2436 HOH A O 1 HETATM 6664 O O . HOH T 9 . ? 23.184 68.098 69.053 1.00 41.26 ? 2437 HOH A O 1 HETATM 6665 O O . HOH T 9 . ? 0.464 63.436 48.200 1.00 33.66 ? 2438 HOH A O 1 HETATM 6666 O O . HOH T 9 . ? 29.495 70.029 39.737 1.00 31.42 ? 2439 HOH A O 1 HETATM 6667 O O . HOH T 9 . ? 22.161 51.072 11.319 1.00 25.12 ? 2440 HOH A O 1 HETATM 6668 O O . HOH T 9 . ? -6.386 42.388 46.803 1.00 35.28 ? 2441 HOH A O 1 HETATM 6669 O O . HOH T 9 . ? 29.039 58.515 48.227 1.00 43.26 ? 2442 HOH A O 1 HETATM 6670 O O . HOH T 9 . ? 2.221 34.249 24.105 1.00 45.19 ? 2443 HOH A O 1 HETATM 6671 O O . HOH T 9 . ? 12.383 57.026 31.684 1.00 38.22 ? 2444 HOH A O 1 HETATM 6672 O O . HOH T 9 . ? 35.789 50.006 35.868 1.00 37.46 ? 2445 HOH A O 1 HETATM 6673 O O . HOH T 9 . ? 6.150 33.535 20.594 1.00 44.43 ? 2446 HOH A O 1 HETATM 6674 O O . HOH T 9 . ? 19.091 25.280 12.259 1.00 29.54 ? 2447 HOH A O 1 HETATM 6675 O O . HOH T 9 . ? 1.329 60.184 43.792 1.00 28.81 ? 2448 HOH A O 1 HETATM 6676 O O . HOH T 9 . ? 29.686 62.091 27.472 1.00 34.22 ? 2449 HOH A O 1 HETATM 6677 O O . HOH T 9 . ? 18.037 22.295 48.735 1.00 34.13 ? 2450 HOH A O 1 HETATM 6678 O O . HOH T 9 . ? 31.620 51.359 50.160 1.00 35.58 ? 2451 HOH A O 1 HETATM 6679 O O . HOH T 9 . ? 40.930 42.599 24.092 1.00 28.71 ? 2452 HOH A O 1 HETATM 6680 O O . HOH T 9 . ? 32.058 50.324 11.940 1.00 26.23 ? 2453 HOH A O 1 HETATM 6681 O O . HOH T 9 . ? 29.123 67.341 39.130 1.00 41.95 ? 2454 HOH A O 1 HETATM 6682 O O . HOH T 9 . ? 24.018 58.567 36.954 1.00 37.82 ? 2455 HOH A O 1 HETATM 6683 O O . HOH T 9 . ? 16.045 85.962 29.465 1.00 29.85 ? 2456 HOH A O 1 HETATM 6684 O O . HOH T 9 . ? 24.868 60.094 32.599 1.00 37.54 ? 2457 HOH A O 1 HETATM 6685 O O . HOH T 9 . ? 32.633 58.009 26.984 1.00 34.69 ? 2458 HOH A O 1 HETATM 6686 O O . HOH T 9 . ? -10.593 43.768 38.547 1.00 42.53 ? 2459 HOH A O 1 HETATM 6687 O O . HOH T 9 . ? 32.049 55.038 35.826 1.00 35.66 ? 2460 HOH A O 1 HETATM 6688 O O . HOH T 9 . ? 10.758 82.878 56.649 1.00 45.75 ? 2461 HOH A O 1 HETATM 6689 O O . HOH T 9 . ? 12.238 25.292 35.612 1.00 49.27 ? 2462 HOH A O 1 HETATM 6690 O O . HOH T 9 . ? 33.045 54.646 70.332 1.00 30.71 ? 2463 HOH A O 1 HETATM 6691 O O . HOH T 9 . ? 36.696 39.213 15.176 1.00 26.46 ? 2464 HOH A O 1 HETATM 6692 O O . HOH T 9 . ? 10.308 28.467 34.000 1.00 41.06 ? 2465 HOH A O 1 HETATM 6693 O O . HOH T 9 . ? 40.764 47.436 29.556 1.00 40.41 ? 2466 HOH A O 1 HETATM 6694 O O . HOH T 9 . ? 21.751 54.654 16.563 1.00 29.39 ? 2467 HOH A O 1 HETATM 6695 O O . HOH T 9 . ? 25.818 25.786 46.566 1.00 26.49 ? 2468 HOH A O 1 HETATM 6696 O O . HOH T 9 . ? 23.481 61.209 20.242 1.00 34.75 ? 2469 HOH A O 1 HETATM 6697 O O . HOH T 9 . ? 26.900 26.658 30.366 1.00 46.38 ? 2470 HOH A O 1 HETATM 6698 O O . HOH T 9 . ? 3.618 18.950 62.880 1.00 48.68 ? 2471 HOH A O 1 HETATM 6699 O O . HOH T 9 . ? 39.257 39.955 14.717 1.00 28.92 ? 2472 HOH A O 1 HETATM 6700 O O . HOH T 9 . ? 9.496 42.298 19.878 1.00 39.65 ? 2473 HOH A O 1 HETATM 6701 O O . HOH T 9 . ? 19.567 51.317 6.914 1.00 48.84 ? 2474 HOH A O 1 HETATM 6702 O O . HOH T 9 . ? 18.288 85.493 54.615 1.00 37.00 ? 2475 HOH A O 1 HETATM 6703 O O . HOH T 9 . ? 16.800 42.570 44.749 1.00 13.99 ? 2476 HOH A O 1 HETATM 6704 O O . HOH T 9 . ? 21.534 42.251 46.416 1.00 24.63 ? 2477 HOH A O 1 HETATM 6705 O O . HOH T 9 . ? 19.505 49.292 45.076 1.00 23.56 ? 2478 HOH A O 1 HETATM 6706 O O . HOH T 9 . ? 26.136 53.260 48.800 1.00 30.10 ? 2479 HOH A O 1 HETATM 6707 O O . HOH T 9 . ? -0.603 31.001 63.113 1.00 35.87 ? 2480 HOH A O 1 HETATM 6708 O O . HOH T 9 . ? 2.880 34.433 70.766 1.00 38.33 ? 2481 HOH A O 1 HETATM 6709 O O . HOH T 9 . ? 30.956 41.482 40.639 1.00 23.73 ? 2482 HOH A O 1 HETATM 6710 O O . HOH T 9 . ? 23.466 54.265 45.845 1.00 28.42 ? 2483 HOH A O 1 HETATM 6711 O O . HOH T 9 . ? 29.595 50.340 39.328 1.00 26.43 ? 2484 HOH A O 1 HETATM 6712 O O . HOH T 9 . ? 19.195 18.600 43.819 1.00 42.34 ? 2485 HOH A O 1 HETATM 6713 O O . HOH T 9 . ? 31.126 48.725 47.319 1.00 36.96 ? 2486 HOH A O 1 HETATM 6714 O O . HOH T 9 . ? 40.654 53.460 69.117 1.00 37.00 ? 2487 HOH A O 1 HETATM 6715 O O . HOH T 9 . ? 14.229 59.824 33.147 1.00 40.10 ? 2488 HOH A O 1 HETATM 6716 O O . HOH T 9 . ? 37.967 49.580 45.819 1.00 37.20 ? 2489 HOH A O 1 HETATM 6717 O O . HOH T 9 . ? 4.969 50.264 28.463 1.00 39.66 ? 2490 HOH A O 1 HETATM 6718 O O . HOH T 9 . ? 10.992 82.380 66.047 1.00 35.18 ? 2491 HOH A O 1 HETATM 6719 O O . HOH T 9 . ? 6.026 54.868 34.622 1.00 36.70 ? 2492 HOH A O 1 HETATM 6720 O O . HOH T 9 . ? 14.543 55.690 10.616 1.00 50.78 ? 2493 HOH A O 1 HETATM 6721 O O . HOH T 9 . ? 35.135 56.162 51.005 1.00 41.30 ? 2494 HOH A O 1 HETATM 6722 O O . HOH T 9 . ? 31.899 57.142 31.946 1.00 32.13 ? 2495 HOH A O 1 HETATM 6723 O O . HOH T 9 . ? 37.611 41.077 58.688 1.00 29.44 ? 2496 HOH A O 1 HETATM 6724 O O . HOH T 9 . ? 23.595 58.890 21.669 1.00 34.57 ? 2497 HOH A O 1 HETATM 6725 O O . HOH T 9 . ? 30.535 52.776 39.418 1.00 42.79 ? 2498 HOH A O 1 HETATM 6726 O O . HOH T 9 . ? 18.523 15.584 38.473 1.00 38.93 ? 2499 HOH A O 1 HETATM 6727 O O . HOH T 9 . ? 33.793 48.988 47.421 1.00 38.75 ? 2500 HOH A O 1 HETATM 6728 O O A HOH T 9 . ? 25.916 46.586 45.129 0.50 26.23 ? 2501 HOH A O 1 HETATM 6729 O O B HOH T 9 . ? 27.319 46.121 43.946 0.50 19.31 ? 2501 HOH A O 1 HETATM 6730 O O B HOH T 9 . ? 14.976 51.659 33.675 0.50 21.59 ? 2502 HOH A O 1 HETATM 6731 O O . HOH T 9 . ? 13.180 36.666 12.321 1.00 31.21 ? 2503 HOH A O 1 HETATM 6732 O O . HOH T 9 . ? 11.958 49.067 29.619 1.00 45.17 ? 2504 HOH A O 1 HETATM 6733 O O . HOH T 9 . ? 6.840 26.889 40.777 1.00 50.21 ? 2505 HOH A O 1 HETATM 6734 O O . HOH T 9 . ? 27.964 66.149 73.773 1.00 32.74 ? 2506 HOH A O 1 HETATM 6735 O O . HOH T 9 . ? 12.097 75.690 73.200 1.00 41.19 ? 2507 HOH A O 1 HETATM 6736 O O . HOH T 9 . ? 38.017 46.259 38.582 1.00 37.09 ? 2508 HOH A O 1 HETATM 6737 O O . HOH T 9 . ? 38.158 52.934 16.974 1.00 33.31 ? 2509 HOH A O 1 HETATM 6738 O O . HOH T 9 . ? -2.829 45.956 68.649 1.00 37.50 ? 2510 HOH A O 1 HETATM 6739 O O . HOH T 9 . ? 12.272 50.929 76.445 1.00 35.53 ? 2511 HOH A O 1 HETATM 6740 O O . HOH T 9 . ? 26.075 53.932 46.143 1.00 34.03 ? 2512 HOH A O 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 . LYS A 14 ? 0.9573 0.7512 0.5310 0.2221 -0.0792 0.0290 55 LYS A N 2 C CA . LYS A 14 ? 0.9311 0.7372 0.5209 0.2140 -0.0756 0.0232 55 LYS A CA 3 C C . LYS A 14 ? 0.8875 0.7073 0.5085 0.2015 -0.0679 0.0244 55 LYS A C 4 O O . LYS A 14 ? 0.8835 0.7065 0.5194 0.1986 -0.0703 0.0258 55 LYS A O 5 C CB . LYS A 14 ? 0.9389 0.7500 0.5330 0.2160 -0.0914 0.0117 55 LYS A CB 6 C CG . LYS A 14 ? 0.9630 0.7786 0.5568 0.2137 -0.0892 0.0061 55 LYS A CG 7 C CD . LYS A 14 ? 1.0172 0.8251 0.5906 0.2235 -0.1027 -0.0014 55 LYS A CD 8 C CE . LYS A 14 ? 1.0188 0.8322 0.6072 0.2239 -0.1205 -0.0102 55 LYS A CE 9 N NZ . LYS A 14 ? 1.0740 0.8746 0.6375 0.2365 -0.1336 -0.0126 55 LYS A NZ 10 N N . HIS A 15 ? 0.8488 0.6761 0.4788 0.1947 -0.0588 0.0236 56 HIS A N 11 C CA . HIS A 15 ? 0.7991 0.6396 0.4576 0.1830 -0.0520 0.0238 56 HIS A CA 12 C C . HIS A 15 ? 0.7523 0.6049 0.4290 0.1776 -0.0597 0.0142 56 HIS A C 13 O O . HIS A 15 ? 0.7696 0.6259 0.4469 0.1750 -0.0554 0.0118 56 HIS A O 14 C CB . HIS A 15 ? 0.7989 0.6390 0.4558 0.1790 -0.0354 0.0308 56 HIS A CB 15 C CG . HIS A 15 ? 0.8392 0.6694 0.4852 0.1817 -0.0260 0.0410 56 HIS A CG 16 N ND1 . HIS A 15 ? 0.8706 0.6919 0.4978 0.1854 -0.0142 0.0480 56 HIS A ND1 17 C CD2 . HIS A 15 ? 0.8450 0.6724 0.4967 0.1813 -0.0265 0.0454 56 HIS A CD2 18 C CE1 . HIS A 15 ? 0.9053 0.7187 0.5274 0.1869 -0.0075 0.0567 56 HIS A CE1 19 N NE2 . HIS A 15 ? 0.8906 0.7073 0.5271 0.1844 -0.0150 0.0552 56 HIS A NE2 20 N N . ASN A 16 ? 0.6899 0.5484 0.3820 0.1760 -0.0709 0.0088 57 ASN A N 21 C CA . ASN A 16 ? 0.6251 0.4948 0.3357 0.1709 -0.0787 -0.0002 57 ASN A CA 22 C C . ASN A 16 ? 0.5689 0.4492 0.3063 0.1629 -0.0792 -0.0010 57 ASN A C 23 O O . ASN A 16 ? 0.5377 0.4167 0.2786 0.1611 -0.0727 0.0052 57 ASN A O 24 C CB . ASN A 16 ? 0.6252 0.4906 0.3263 0.1786 -0.0941 -0.0075 57 ASN A CB 25 C CG . ASN A 16 ? 0.6532 0.5107 0.3448 0.1861 -0.1019 -0.0055 57 ASN A CG 26 O OD1 . ASN A 16 ? 0.6201 0.4786 0.3204 0.1838 -0.0982 -0.0006 57 ASN A OD1 27 N ND2 . ASN A 16 ? 0.6893 0.5381 0.3620 0.1957 -0.1131 -0.0095 57 ASN A ND2 28 N N . MET A 17 ? 0.5513 0.4418 0.3076 0.1583 -0.0869 -0.0087 58 MET A N 29 C CA . MET A 17 ? 0.5258 0.4267 0.3074 0.1502 -0.0855 -0.0092 58 MET A CA 30 C C . MET A 17 ? 0.5285 0.4264 0.3120 0.1543 -0.0918 -0.0080 58 MET A C 31 O O . MET A 17 ? 0.5029 0.4044 0.2989 0.1498 -0.0864 -0.0047 58 MET A O 32 C CB A MET A 17 ? 0.5159 0.4281 0.3177 0.1445 -0.0919 -0.0172 58 MET A CB 33 C CB B MET A 17 ? 0.5014 0.4143 0.3047 0.1433 -0.0899 -0.0164 58 MET A CB 34 C CG A MET A 17 ? 0.5390 0.4627 0.3673 0.1357 -0.0893 -0.0180 58 MET A CG 35 C CG B MET A 17 ? 0.4588 0.3814 0.2845 0.1344 -0.0834 -0.0146 58 MET A CG 36 S SD A MET A 17 ? 0.6015 0.5377 0.4520 0.1281 -0.0937 -0.0260 58 MET A SD 37 S SD B MET A 17 ? 0.4195 0.3549 0.2714 0.1282 -0.0911 -0.0227 58 MET A SD 38 C CE A MET A 17 ? 0.6310 0.5655 0.4810 0.1349 -0.1103 -0.0338 58 MET A CE 39 C CE B MET A 17 ? 0.3863 0.3254 0.2386 0.1239 -0.0882 -0.0258 58 MET A CE 40 N N . LYS A 18 ? 0.5421 0.4332 0.3132 0.1629 -0.1031 -0.0110 59 LYS A N 41 C CA . LYS A 18 ? 0.5508 0.4383 0.3228 0.1677 -0.1097 -0.0099 59 LYS A CA 42 C C . LYS A 18 ? 0.5424 0.4215 0.3033 0.1694 -0.0998 -0.0003 59 LYS A C 43 O O . LYS A 18 ? 0.5399 0.4208 0.3123 0.1678 -0.0993 0.0019 59 LYS A O 44 C CB . LYS A 18 ? 0.5757 0.4555 0.3322 0.1779 -0.1238 -0.0142 59 LYS A CB 45 C CG . LYS A 18 ? 0.6148 0.4927 0.3759 0.1828 -0.1330 -0.0147 59 LYS A CG 46 C CD . LYS A 18 ? 0.7033 0.5746 0.4507 0.1926 -0.1485 -0.0203 59 LYS A CD 47 C CE . LYS A 18 ? 0.7628 0.6363 0.5228 0.1961 -0.1602 -0.0235 59 LYS A CE 48 N NZ . LYS A 18 ? 0.7931 0.6577 0.5432 0.2006 -0.1564 -0.0153 59 LYS A NZ 49 N N . ALA A 19 ? 0.5532 0.4233 0.2931 0.1724 -0.0914 0.0055 60 ALA A N 50 C CA . ALA A 19 ? 0.5651 0.4270 0.2955 0.1734 -0.0808 0.0151 60 ALA A CA 51 C C . ALA A 19 ? 0.5352 0.4063 0.2881 0.1630 -0.0708 0.0175 60 ALA A C 52 O O . ALA A 19 ? 0.5387 0.4070 0.2959 0.1626 -0.0676 0.0223 60 ALA A O 53 C CB . ALA A 19 ? 0.5947 0.4466 0.3008 0.1775 -0.0723 0.0206 60 ALA A CB 54 N N . PHE A 20 ? 0.5000 0.3812 0.2659 0.1552 -0.0664 0.0142 61 PHE A N 55 C CA . PHE A 20 ? 0.4797 0.3703 0.2669 0.1454 -0.0581 0.0153 61 PHE A CA 56 C C . PHE A 20 ? 0.4571 0.3543 0.2637 0.1431 -0.0646 0.0118 61 PHE A C 57 O O . PHE A 20 ? 0.4527 0.3500 0.2680 0.1401 -0.0593 0.0156 61 PHE A O 58 C CB . PHE A 20 ? 0.4506 0.3506 0.2476 0.1384 -0.0541 0.0117 61 PHE A CB 59 C CG . PHE A 20 ? 0.4427 0.3536 0.2630 0.1289 -0.0494 0.0105 61 PHE A CG 60 C CD1 . PHE A 20 ? 0.4469 0.3573 0.2712 0.1243 -0.0384 0.0164 61 PHE A CD1 61 C CD2 . PHE A 20 ? 0.4239 0.3448 0.2620 0.1248 -0.0562 0.0037 61 PHE A CD2 62 C CE1 . PHE A 20 ? 0.4327 0.3527 0.2779 0.1159 -0.0347 0.0149 61 PHE A CE1 63 C CE2 . PHE A 20 ? 0.4300 0.3606 0.2886 0.1163 -0.0516 0.0027 61 PHE A CE2 64 C CZ . PHE A 20 ? 0.4244 0.3542 0.2856 0.1122 -0.0413 0.0081 61 PHE A CZ 65 N N . LEU A 21 ? 0.4536 0.3562 0.2677 0.1444 -0.0758 0.0044 62 LEU A N 66 C CA . LEU A 21 ? 0.4530 0.3633 0.2876 0.1418 -0.0814 0.0004 62 LEU A CA 67 C C . LEU A 21 ? 0.4716 0.3740 0.3011 0.1480 -0.0848 0.0041 62 LEU A C 68 O O . LEU A 21 ? 0.4661 0.3727 0.3110 0.1447 -0.0831 0.0044 62 LEU A O 69 C CB . LEU A 21 ? 0.4545 0.3719 0.2988 0.1424 -0.0931 -0.0082 62 LEU A CB 70 C CG . LEU A 21 ? 0.4328 0.3594 0.2869 0.1354 -0.0907 -0.0126 62 LEU A CG 71 C CD1 . LEU A 21 ? 0.4687 0.3990 0.3278 0.1379 -0.1032 -0.0205 62 LEU A CD1 72 C CD2 . LEU A 21 ? 0.4098 0.3472 0.2857 0.1256 -0.0831 -0.0128 62 LEU A CD2 73 N N . ASP A 22 ? 0.5060 0.3965 0.3133 0.1573 -0.0894 0.0068 63 ASP A N 74 C CA . ASP A 22 ? 0.5390 0.4206 0.3395 0.1641 -0.0933 0.0106 63 ASP A CA 75 C C . ASP A 22 ? 0.5404 0.4167 0.3398 0.1616 -0.0816 0.0189 63 ASP A C 76 O O . ASP A 22 ? 0.5615 0.4335 0.3636 0.1645 -0.0835 0.0215 63 ASP A O 77 C CB . ASP A 22 ? 0.5716 0.4403 0.3454 0.1751 -0.1004 0.0122 63 ASP A CB 78 C CG . ASP A 22 ? 0.6267 0.4988 0.4028 0.1797 -0.1157 0.0036 63 ASP A CG 79 O OD1 . ASP A 22 ? 0.6507 0.5348 0.4505 0.1750 -0.1212 -0.0031 63 ASP A OD1 80 O OD2 . ASP A 22 ? 0.6644 0.5269 0.4182 0.1881 -0.1220 0.0035 63 ASP A OD2 81 N N . GLU A 23 ? 0.5321 0.4083 0.3280 0.1565 -0.0698 0.0230 64 GLU A N 82 C CA . GLU A 23 ? 0.5316 0.4027 0.3271 0.1537 -0.0585 0.0307 64 GLU A CA 83 C C . GLU A 23 ? 0.5074 0.3881 0.3281 0.1457 -0.0555 0.0286 64 GLU A C 84 O O . GLU A 23 ? 0.5122 0.3879 0.3353 0.1451 -0.0501 0.0337 64 GLU A O 85 C CB . GLU A 23 ? 0.5492 0.4172 0.3337 0.1512 -0.0471 0.0356 64 GLU A CB 86 C CG . GLU A 23 ? 0.5760 0.4382 0.3602 0.1481 -0.0345 0.0440 64 GLU A CG 87 C CD . GLU A 23 ? 0.6478 0.4957 0.4173 0.1556 -0.0345 0.0512 64 GLU A CD 88 O OE1 . GLU A 23 ? 0.6788 0.5170 0.4272 0.1647 -0.0403 0.0526 64 GLU A OE1 89 O OE2 . GLU A 23 ? 0.6447 0.4904 0.4233 0.1527 -0.0290 0.0553 64 GLU A OE2 90 N N . LEU A 24 ? 0.4727 0.3665 0.3112 0.1401 -0.0590 0.0211 65 LEU A N 91 C CA . LEU A 24 ? 0.4512 0.3549 0.3132 0.1327 -0.0566 0.0182 65 LEU A CA 92 C C . LEU A 24 ? 0.4635 0.3651 0.3325 0.1367 -0.0628 0.0175 65 LEU A C 93 O O . LEU A 24 ? 0.4705 0.3713 0.3371 0.1428 -0.0734 0.0141 65 LEU A O 94 C CB . LEU A 24 ? 0.4204 0.3373 0.2974 0.1274 -0.0605 0.0103 65 LEU A CB 95 C CG . LEU A 24 ? 0.4056 0.3262 0.2789 0.1229 -0.0552 0.0098 65 LEU A CG 96 C CD1 . LEU A 24 ? 0.3984 0.3300 0.2847 0.1196 -0.0614 0.0021 65 LEU A CD1 97 C CD2 . LEU A 24 ? 0.3816 0.3046 0.2614 0.1153 -0.0433 0.0135 65 LEU A CD2 98 N N . LYS A 25 ? 0.4418 0.3434 0.3213 0.1331 -0.0568 0.0200 66 LYS A N 99 C CA . LYS A 25 ? 0.4487 0.3475 0.3349 0.1372 -0.0619 0.0197 66 LYS A CA 100 C C . LYS A 25 ? 0.4244 0.3331 0.3336 0.1304 -0.0591 0.0157 66 LYS A C 101 O O . LYS A 25 ? 0.4116 0.3224 0.3265 0.1237 -0.0498 0.0174 66 LYS A O 102 C CB A LYS A 25 ? 0.4748 0.3591 0.3467 0.1418 -0.0575 0.0283 66 LYS A CB 103 C CB B LYS A 25 ? 0.4705 0.3544 0.3416 0.1424 -0.0582 0.0282 66 LYS A CB 104 C CG A LYS A 25 ? 0.5254 0.3980 0.3717 0.1495 -0.0594 0.0333 66 LYS A CG 105 C CG B LYS A 25 ? 0.5037 0.3767 0.3510 0.1515 -0.0635 0.0317 66 LYS A CG 106 C CD A LYS A 25 ? 0.5936 0.4627 0.4334 0.1587 -0.0727 0.0304 66 LYS A CD 107 C CD B LYS A 25 ? 0.5290 0.3884 0.3585 0.1538 -0.0546 0.0413 66 LYS A CD 108 C CE A LYS A 25 ? 0.6383 0.4928 0.4502 0.1678 -0.0747 0.0363 66 LYS A CE 109 C CE B LYS A 25 ? 0.5298 0.3806 0.3345 0.1608 -0.0570 0.0441 66 LYS A CE 110 N NZ A LYS A 25 ? 0.6301 0.4861 0.4302 0.1669 -0.0728 0.0352 66 LYS A NZ 111 N NZ B LYS A 25 ? 0.5377 0.3805 0.3289 0.1593 -0.0448 0.0521 66 LYS A NZ 112 N N . ALA A 26 ? 0.4156 0.3298 0.3375 0.1327 -0.0671 0.0103 67 ALA A N 113 C CA . ALA A 26 ? 0.4040 0.3274 0.3475 0.1274 -0.0649 0.0060 67 ALA A CA 114 C C . ALA A 26 ? 0.4095 0.3257 0.3539 0.1263 -0.0576 0.0110 67 ALA A C 115 O O . ALA A 26 ? 0.3772 0.2993 0.3344 0.1193 -0.0509 0.0092 67 ALA A O 116 C CB . ALA A 26 ? 0.4016 0.3305 0.3574 0.1318 -0.0752 0.0001 67 ALA A CB 117 N N . GLU A 27 ? 0.4329 0.3360 0.3638 0.1331 -0.0590 0.0170 68 GLU A N 118 C CA A GLU A 27 ? 0.4464 0.3417 0.3790 0.1325 -0.0528 0.0218 68 GLU A CA 119 C CA B GLU A 27 ? 0.4544 0.3482 0.3847 0.1332 -0.0529 0.0225 68 GLU A CA 120 C C . GLU A 27 ? 0.4426 0.3363 0.3724 0.1256 -0.0415 0.0258 68 GLU A C 121 O O . GLU A 27 ? 0.4277 0.3210 0.3674 0.1213 -0.0355 0.0264 68 GLU A O 122 C CB A GLU A 27 ? 0.4729 0.3537 0.3915 0.1416 -0.0569 0.0278 68 GLU A CB 123 C CB B GLU A 27 ? 0.4858 0.3643 0.3978 0.1426 -0.0567 0.0294 68 GLU A CB 124 C CG A GLU A 27 ? 0.5012 0.3728 0.4221 0.1412 -0.0506 0.0329 68 GLU A CG 125 C CG B GLU A 27 ? 0.5418 0.4114 0.4311 0.1448 -0.0532 0.0358 68 GLU A CG 126 C CD A GLU A 27 ? 0.5442 0.4232 0.4866 0.1384 -0.0514 0.0272 68 GLU A CD 127 C CD B GLU A 27 ? 0.6270 0.4843 0.4955 0.1555 -0.0606 0.0401 68 GLU A CD 128 O OE1 A GLU A 27 ? 0.5044 0.3886 0.4552 0.1425 -0.0601 0.0221 68 GLU A OE1 129 O OE1 B GLU A 27 ? 0.6540 0.4980 0.5065 0.1586 -0.0551 0.0485 68 GLU A OE1 130 O OE2 A GLU A 27 ? 0.5725 0.4523 0.5237 0.1321 -0.0433 0.0276 68 GLU A OE2 131 O OE2 B GLU A 27 ? 0.6400 0.5003 0.5075 0.1609 -0.0716 0.0353 68 GLU A OE2 132 N N . ASN A 28 ? 0.4278 0.3211 0.3456 0.1243 -0.0388 0.0280 69 ASN A N 133 C CA . ASN A 28 ? 0.4217 0.3156 0.3395 0.1173 -0.0284 0.0309 69 ASN A CA 134 C C . ASN A 28 ? 0.3874 0.2943 0.3226 0.1089 -0.0257 0.0246 69 ASN A C 135 O O . ASN A 28 ? 0.3841 0.2915 0.3266 0.1032 -0.0184 0.0256 69 ASN A O 136 C CB . ASN A 28 ? 0.4350 0.3255 0.3361 0.1184 -0.0259 0.0346 69 ASN A CB 137 C CG . ASN A 28 ? 0.4710 0.3466 0.3526 0.1260 -0.0256 0.0424 69 ASN A CG 138 O OD1 . ASN A 28 ? 0.5074 0.3740 0.3885 0.1282 -0.0233 0.0471 69 ASN A OD1 139 N ND2 . ASN A 28 ? 0.4843 0.3568 0.3494 0.1304 -0.0279 0.0439 69 ASN A ND2 140 N N . ILE A 29 ? 0.3642 0.2813 0.3062 0.1083 -0.0316 0.0181 70 ILE A N 141 C CA . ILE A 29 ? 0.3428 0.2723 0.3003 0.1007 -0.0290 0.0122 70 ILE A CA 142 C C . ILE A 29 ? 0.3379 0.2684 0.3094 0.0987 -0.0271 0.0101 70 ILE A C 143 O O . ILE A 29 ? 0.3390 0.2735 0.3188 0.0923 -0.0211 0.0087 70 ILE A O 144 C CB . ILE A 29 ? 0.3392 0.2786 0.3020 0.1008 -0.0359 0.0059 70 ILE A CB 145 C CG1 . ILE A 29 ? 0.3372 0.2749 0.2857 0.1026 -0.0376 0.0076 70 ILE A CG1 146 C CG2 . ILE A 29 ? 0.3202 0.2713 0.2981 0.0933 -0.0327 0.0006 70 ILE A CG2 147 C CD1 . ILE A 29 ? 0.3861 0.3308 0.3380 0.1047 -0.0462 0.0020 70 ILE A CD1 148 N N . LYS A 30 ? 0.3417 0.2679 0.3150 0.1047 -0.0326 0.0100 71 LYS A N 149 C CA . LYS A 30 ? 0.3446 0.2709 0.3308 0.1040 -0.0312 0.0079 71 LYS A CA 150 C C . LYS A 30 ? 0.3654 0.2833 0.3494 0.1010 -0.0232 0.0128 71 LYS A C 151 O O . LYS A 30 ? 0.3504 0.2720 0.3456 0.0958 -0.0187 0.0099 71 LYS A O 152 C CB . LYS A 30 ? 0.3556 0.2768 0.3419 0.1122 -0.0390 0.0080 71 LYS A CB 153 C CG . LYS A 30 ? 0.3840 0.3040 0.3830 0.1126 -0.0380 0.0060 71 LYS A CG 154 C CD . LYS A 30 ? 0.4188 0.3342 0.4178 0.1212 -0.0464 0.0061 71 LYS A CD 155 C CE . LYS A 30 ? 0.4630 0.3780 0.4759 0.1221 -0.0459 0.0034 71 LYS A CE 156 N NZ . LYS A 30 ? 0.4677 0.3779 0.4811 0.1311 -0.0548 0.0036 71 LYS A NZ 157 N N . LYS A 31 ? 0.3831 0.2897 0.3529 0.1043 -0.0214 0.0202 72 LYS A N 158 C CA . LYS A 31 ? 0.3960 0.2940 0.3643 0.1015 -0.0136 0.0255 72 LYS A CA 159 C C . LYS A 31 ? 0.3713 0.2761 0.3447 0.0930 -0.0067 0.0240 72 LYS A C 160 O O . LYS A 31 ? 0.3584 0.2623 0.3405 0.0884 -0.0017 0.0235 72 LYS A O 161 C CB . LYS A 31 ? 0.4215 0.3063 0.3725 0.1067 -0.0121 0.0342 72 LYS A CB 162 C CG . LYS A 31 ? 0.5124 0.3880 0.4583 0.1151 -0.0182 0.0367 72 LYS A CG 163 C CD . LYS A 31 ? 0.5791 0.4413 0.5051 0.1210 -0.0171 0.0455 72 LYS A CD 164 C CE . LYS A 31 ? 0.6571 0.5094 0.5773 0.1300 -0.0240 0.0481 72 LYS A CE 165 N NZ . LYS A 31 ? 0.7074 0.5478 0.6052 0.1365 -0.0240 0.0559 72 LYS A NZ 166 N N . PHE A 32 ? 0.3466 0.2580 0.3151 0.0911 -0.0071 0.0227 73 PHE A N 167 C CA . PHE A 32 ? 0.3336 0.2517 0.3070 0.0835 -0.0014 0.0211 73 PHE A CA 168 C C . PHE A 32 ? 0.3172 0.2451 0.3057 0.0786 -0.0017 0.0138 73 PHE A C 169 O O . PHE A 32 ? 0.3161 0.2459 0.3115 0.0728 0.0034 0.0127 73 PHE A O 170 C CB . PHE A 32 ? 0.3265 0.2494 0.2910 0.0833 -0.0023 0.0212 73 PHE A CB 171 C CG . PHE A 32 ? 0.3561 0.2694 0.3044 0.0879 -0.0008 0.0283 73 PHE A CG 172 C CD1 . PHE A 32 ? 0.4056 0.3079 0.3492 0.0889 0.0049 0.0351 73 PHE A CD1 173 C CD2 . PHE A 32 ? 0.3443 0.2591 0.2816 0.0911 -0.0044 0.0282 73 PHE A CD2 174 C CE1 . PHE A 32 ? 0.4474 0.3403 0.3749 0.0935 0.0071 0.0421 73 PHE A CE1 175 C CE2 . PHE A 32 ? 0.3922 0.2979 0.3130 0.0959 -0.0028 0.0345 73 PHE A CE2 176 C CZ . PHE A 32 ? 0.4328 0.3275 0.3480 0.0971 0.0035 0.0417 73 PHE A CZ 177 N N . LEU A 33 ? 0.3045 0.2388 0.2982 0.0809 -0.0076 0.0087 74 LEU A N 178 C CA . LEU A 33 ? 0.2942 0.2378 0.3015 0.0767 -0.0072 0.0019 74 LEU A CA 179 C C . LEU A 33 ? 0.3033 0.2420 0.3183 0.0756 -0.0041 0.0015 74 LEU A C 180 O O . LEU A 33 ? 0.2985 0.2409 0.3204 0.0702 -0.0002 -0.0016 74 LEU A O 181 C CB . LEU A 33 ? 0.3025 0.2533 0.3158 0.0798 -0.0136 -0.0031 74 LEU A CB 182 C CG . LEU A 33 ? 0.2691 0.2295 0.2957 0.0753 -0.0118 -0.0098 74 LEU A CG 183 C CD1 . LEU A 33 ? 0.2597 0.2276 0.2862 0.0689 -0.0084 -0.0116 74 LEU A CD1 184 C CD2 . LEU A 33 ? 0.3123 0.2794 0.3475 0.0787 -0.0173 -0.0146 74 LEU A CD2 185 N N . TYR A 34 ? 0.3161 0.2458 0.3294 0.0811 -0.0061 0.0045 75 TYR A N 186 C CA . TYR A 34 ? 0.3207 0.2442 0.3411 0.0803 -0.0031 0.0044 75 TYR A CA 187 C C . TYR A 34 ? 0.3294 0.2489 0.3490 0.0747 0.0036 0.0073 75 TYR A C 188 O O . TYR A 34 ? 0.3341 0.2554 0.3628 0.0703 0.0066 0.0036 75 TYR A O 189 C CB . TYR A 34 ? 0.3320 0.2447 0.3484 0.0876 -0.0063 0.0087 75 TYR A CB 190 C CG . TYR A 34 ? 0.3466 0.2522 0.3708 0.0872 -0.0037 0.0086 75 TYR A CG 191 C CD1 . TYR A 34 ? 0.3606 0.2701 0.3965 0.0883 -0.0059 0.0023 75 TYR A CD1 192 C CD2 . TYR A 34 ? 0.4088 0.3043 0.4297 0.0853 0.0016 0.0142 75 TYR A CD2 193 C CE1 . TYR A 34 ? 0.3954 0.2981 0.4386 0.0882 -0.0037 0.0015 75 TYR A CE1 194 C CE2 . TYR A 34 ? 0.4548 0.3431 0.4839 0.0847 0.0038 0.0137 75 TYR A CE2 195 C CZ . TYR A 34 ? 0.4707 0.3625 0.5104 0.0863 0.0009 0.0072 75 TYR A CZ 196 O OH . TYR A 34 ? 0.5099 0.3946 0.5579 0.0861 0.0028 0.0060 75 TYR A OH 197 N N . ASN A 35 ? 0.3253 0.2401 0.3345 0.0749 0.0059 0.0135 76 ASN A N 198 C CA . ASN A 35 ? 0.3376 0.2485 0.3470 0.0699 0.0124 0.0169 76 ASN A CA 199 C C . ASN A 35 ? 0.3166 0.2374 0.3329 0.0628 0.0147 0.0117 76 ASN A C 200 O O . ASN A 35 ? 0.3257 0.2447 0.3481 0.0580 0.0190 0.0116 76 ASN A O 201 C CB . ASN A 35 ? 0.3492 0.2542 0.3455 0.0721 0.0145 0.0244 76 ASN A CB 202 C CG . ASN A 35 ? 0.3679 0.2693 0.3654 0.0672 0.0217 0.0285 76 ASN A CG 203 O OD1 . ASN A 35 ? 0.3753 0.2834 0.3737 0.0626 0.0242 0.0272 76 ASN A OD1 204 N ND2 . ASN A 35 ? 0.4024 0.2927 0.4008 0.0682 0.0252 0.0335 76 ASN A ND2 205 N N . PHE A 36 ? 0.2993 0.2302 0.3150 0.0621 0.0117 0.0075 77 PHE A N 206 C CA . PHE A 36 ? 0.2905 0.2303 0.3106 0.0559 0.0137 0.0034 77 PHE A CA 207 C C . PHE A 36 ? 0.2842 0.2298 0.3144 0.0534 0.0129 -0.0039 77 PHE A C 208 O O . PHE A 36 ? 0.2780 0.2306 0.3111 0.0486 0.0142 -0.0076 77 PHE A O 209 C CB . PHE A 36 ? 0.2793 0.2270 0.2935 0.0562 0.0111 0.0025 77 PHE A CB 210 C CG . PHE A 36 ? 0.2904 0.2342 0.2936 0.0580 0.0123 0.0086 77 PHE A CG 211 C CD1 . PHE A 36 ? 0.3176 0.2522 0.3168 0.0584 0.0167 0.0148 77 PHE A CD1 212 C CD2 . PHE A 36 ? 0.2965 0.2455 0.2933 0.0596 0.0091 0.0079 77 PHE A CD2 213 C CE1 . PHE A 36 ? 0.3237 0.2546 0.3117 0.0605 0.0186 0.0205 77 PHE A CE1 214 C CE2 . PHE A 36 ? 0.3059 0.2513 0.2916 0.0616 0.0102 0.0130 77 PHE A CE2 215 C CZ . PHE A 36 ? 0.3273 0.2638 0.3081 0.0622 0.0152 0.0193 77 PHE A CZ 216 N N . THR A 37 ? 0.2831 0.2260 0.3182 0.0569 0.0107 -0.0061 78 THR A N 217 C CA . THR A 37 ? 0.2795 0.2290 0.3233 0.0554 0.0100 -0.0134 78 THR A CA 218 C C . THR A 37 ? 0.2915 0.2350 0.3427 0.0555 0.0114 -0.0158 78 THR A C 219 O O . THR A 37 ? 0.2971 0.2445 0.3550 0.0560 0.0107 -0.0216 78 THR A O 220 C CB . THR A 37 ? 0.2706 0.2257 0.3158 0.0597 0.0057 -0.0160 78 THR A CB 221 O OG1 . THR A 37 ? 0.2829 0.2303 0.3260 0.0657 0.0028 -0.0123 78 THR A OG1 222 C CG2 . THR A 37 ? 0.2593 0.2217 0.2989 0.0588 0.0040 -0.0153 78 THR A CG2 223 N N . GLN A 38 ? 0.2995 0.2334 0.3500 0.0552 0.0137 -0.0113 79 GLN A N 224 C CA . GLN A 38 ? 0.3303 0.2571 0.3882 0.0555 0.0148 -0.0132 79 GLN A CA 225 C C . GLN A 38 ? 0.3296 0.2589 0.3938 0.0499 0.0171 -0.0188 79 GLN A C 226 O O . GLN A 38 ? 0.3470 0.2728 0.4180 0.0503 0.0172 -0.0231 79 GLN A O 227 C CB . GLN A 38 ? 0.3488 0.2632 0.4039 0.0574 0.0165 -0.0058 79 GLN A CB 228 C CG . GLN A 38 ? 0.3727 0.2828 0.4207 0.0642 0.0134 -0.0008 79 GLN A CG 229 C CD . GLN A 38 ? 0.4228 0.3366 0.4756 0.0688 0.0090 -0.0058 79 GLN A CD 230 O OE1 . GLN A 38 ? 0.4671 0.3763 0.5272 0.0702 0.0089 -0.0085 79 GLN A OE1 231 N NE2 . GLN A 38 ? 0.4174 0.3398 0.4674 0.0708 0.0055 -0.0076 79 GLN A NE2 232 N N . ILE A 39 ? 0.3264 0.2605 0.3880 0.0451 0.0188 -0.0185 80 ILE A N 233 C CA . ILE A 39 ? 0.3290 0.2658 0.3954 0.0397 0.0202 -0.0238 80 ILE A CA 234 C C . ILE A 39 ? 0.3003 0.2475 0.3627 0.0368 0.0198 -0.0262 80 ILE A C 235 O O . ILE A 39 ? 0.3065 0.2573 0.3628 0.0381 0.0191 -0.0224 80 ILE A O 236 C CB . ILE A 39 ? 0.3409 0.2708 0.4102 0.0361 0.0229 -0.0203 80 ILE A CB 237 C CG1 . ILE A 39 ? 0.3524 0.2844 0.4159 0.0346 0.0245 -0.0142 80 ILE A CG1 238 C CG2 . ILE A 39 ? 0.3884 0.3065 0.4624 0.0386 0.0237 -0.0174 80 ILE A CG2 239 C CD1 . ILE A 39 ? 0.4051 0.3317 0.4732 0.0306 0.0276 -0.0110 80 ILE A CD1 240 N N . PRO A 40 ? 0.2919 0.2433 0.3570 0.0333 0.0199 -0.0325 81 PRO A N 241 C CA . PRO A 40 ? 0.2865 0.2470 0.3471 0.0307 0.0196 -0.0342 81 PRO A CA 242 C C . PRO A 40 ? 0.2778 0.2388 0.3353 0.0277 0.0205 -0.0293 81 PRO A C 243 O O . PRO A 40 ? 0.2993 0.2544 0.3603 0.0258 0.0220 -0.0267 81 PRO A O 244 C CB . PRO A 40 ? 0.2918 0.2544 0.3552 0.0279 0.0196 -0.0416 81 PRO A CB 245 C CG . PRO A 40 ? 0.3027 0.2593 0.3717 0.0308 0.0196 -0.0449 81 PRO A CG 246 C CD . PRO A 40 ? 0.3106 0.2586 0.3818 0.0322 0.0201 -0.0385 81 PRO A CD 247 N N . HIS A 41 ? 0.2512 0.2192 0.3033 0.0272 0.0199 -0.0282 82 HIS A N 248 C CA . HIS A 41 ? 0.2558 0.2252 0.3050 0.0245 0.0208 -0.0242 82 HIS A CA 249 C C . HIS A 41 ? 0.2364 0.2137 0.2832 0.0212 0.0199 -0.0276 82 HIS A C 250 O O . HIS A 41 ? 0.2457 0.2276 0.2876 0.0211 0.0195 -0.0253 82 HIS A O 251 C CB . HIS A 41 ? 0.2753 0.2437 0.3187 0.0277 0.0209 -0.0179 82 HIS A CB 252 C CG . HIS A 41 ? 0.2693 0.2290 0.3134 0.0310 0.0220 -0.0135 82 HIS A CG 253 N ND1 . HIS A 41 ? 0.2858 0.2433 0.3282 0.0359 0.0201 -0.0131 82 HIS A ND1 254 C CD2 . HIS A 41 ? 0.2665 0.2186 0.3133 0.0302 0.0247 -0.0096 82 HIS A CD2 255 C CE1 . HIS A 41 ? 0.2838 0.2323 0.3265 0.0382 0.0214 -0.0087 82 HIS A CE1 256 N NE2 . HIS A 41 ? 0.2977 0.2426 0.3431 0.0347 0.0245 -0.0063 82 HIS A NE2 257 N N . LEU A 42 ? 0.2438 0.2220 0.2936 0.0188 0.0194 -0.0332 83 LEU A N 258 C CA . LEU A 42 ? 0.2439 0.2284 0.2904 0.0161 0.0183 -0.0367 83 LEU A CA 259 C C . LEU A 42 ? 0.2298 0.2157 0.2761 0.0132 0.0183 -0.0337 83 LEU A C 260 O O . LEU A 42 ? 0.2488 0.2305 0.3002 0.0116 0.0191 -0.0317 83 LEU A O 261 C CB . LEU A 42 ? 0.2433 0.2269 0.2920 0.0148 0.0176 -0.0436 83 LEU A CB 262 C CG . LEU A 42 ? 0.2311 0.2203 0.2746 0.0127 0.0164 -0.0476 83 LEU A CG 263 C CD1 . LEU A 42 ? 0.2505 0.2451 0.2887 0.0145 0.0172 -0.0481 83 LEU A CD1 264 C CD2 . LEU A 42 ? 0.2464 0.2322 0.2919 0.0119 0.0155 -0.0547 83 LEU A CD2 265 N N . ALA A 43 ? 0.2253 0.2172 0.2663 0.0124 0.0175 -0.0332 84 ALA A N 266 C CA . ALA A 43 ? 0.2217 0.2156 0.2628 0.0098 0.0172 -0.0308 84 ALA A CA 267 C C . ALA A 43 ? 0.2245 0.2170 0.2712 0.0065 0.0161 -0.0341 84 ALA A C 268 O O . ALA A 43 ? 0.2321 0.2245 0.2788 0.0057 0.0145 -0.0397 84 ALA A O 269 C CB . ALA A 43 ? 0.2176 0.2179 0.2524 0.0094 0.0160 -0.0310 84 ALA A CB 270 N N . GLY A 44 ? 0.2348 0.2259 0.2869 0.0048 0.0171 -0.0308 85 GLY A N 271 C CA . GLY A 44 ? 0.2593 0.2495 0.3187 0.0014 0.0156 -0.0338 85 GLY A CA 272 C C . GLY A 44 ? 0.2844 0.2680 0.3520 0.0009 0.0164 -0.0351 85 GLY A C 273 O O . GLY A 44 ? 0.3028 0.2851 0.3785 -0.0021 0.0150 -0.0376 85 GLY A O 274 N N . THR A 45 ? 0.2640 0.2431 0.3304 0.0037 0.0183 -0.0336 86 THR A N 275 C CA . THR A 45 ? 0.2691 0.2409 0.3432 0.0035 0.0191 -0.0347 86 THR A CA 276 C C . THR A 45 ? 0.2800 0.2467 0.3589 0.0038 0.0229 -0.0276 86 THR A C 277 O O . THR A 45 ? 0.2760 0.2441 0.3499 0.0055 0.0252 -0.0219 86 THR A O 278 C CB . THR A 45 ? 0.2733 0.2421 0.3441 0.0067 0.0188 -0.0377 86 THR A CB 279 O OG1 . THR A 45 ? 0.2823 0.2509 0.3479 0.0105 0.0207 -0.0326 86 THR A OG1 280 C CG2 . THR A 45 ? 0.2870 0.2606 0.3522 0.0068 0.0161 -0.0444 86 THR A CG2 281 N N . GLU A 46 ? 0.2949 0.2551 0.3833 0.0022 0.0239 -0.0281 87 GLU A N 282 C CA . GLU A 46 ? 0.3103 0.2644 0.4039 0.0022 0.0283 -0.0211 87 GLU A CA 283 C C . GLU A 46 ? 0.3044 0.2546 0.3898 0.0071 0.0307 -0.0154 87 GLU A C 284 O O . GLU A 46 ? 0.3095 0.2579 0.3925 0.0083 0.0344 -0.0084 87 GLU A O 285 C CB . GLU A 46 ? 0.3467 0.2935 0.4525 -0.0003 0.0286 -0.0231 87 GLU A CB 286 C CG . GLU A 46 ? 0.4215 0.3611 0.5331 -0.0003 0.0340 -0.0153 87 GLU A CG 287 C CD . GLU A 46 ? 0.5363 0.4790 0.6527 -0.0031 0.0374 -0.0104 87 GLU A CD 288 O OE1 . GLU A 46 ? 0.5781 0.5151 0.6965 -0.0024 0.0430 -0.0030 87 GLU A OE1 289 O OE2 . GLU A 46 ? 0.5751 0.5257 0.6932 -0.0056 0.0350 -0.0137 87 GLU A OE2 290 N N A GLN A 47 ? 0.2993 0.2483 0.3804 0.0101 0.0286 -0.0188 88 GLN A N 291 N N B GLN A 47 ? 0.3115 0.2604 0.3924 0.0103 0.0287 -0.0185 88 GLN A N 292 C CA A GLN A 47 ? 0.2947 0.2406 0.3686 0.0152 0.0294 -0.0149 88 GLN A CA 293 C CA B GLN A 47 ? 0.3170 0.2621 0.3910 0.0152 0.0300 -0.0135 88 GLN A CA 294 C C A GLN A 47 ? 0.2833 0.2342 0.3479 0.0171 0.0299 -0.0105 88 GLN A C 295 C C B GLN A 47 ? 0.2997 0.2507 0.3637 0.0174 0.0299 -0.0103 88 GLN A C 296 O O A GLN A 47 ? 0.2830 0.2297 0.3428 0.0202 0.0321 -0.0042 88 GLN A O 297 O O B GLN A 47 ? 0.2967 0.2441 0.3548 0.0210 0.0315 -0.0046 88 GLN A O 298 C CB A GLN A 47 ? 0.2889 0.2358 0.3608 0.0177 0.0264 -0.0207 88 GLN A CB 299 C CB B GLN A 47 ? 0.3313 0.2734 0.4051 0.0182 0.0279 -0.0176 88 GLN A CB 300 C CG A GLN A 47 ? 0.3146 0.2543 0.3947 0.0173 0.0260 -0.0245 88 GLN A CG 301 C CG B GLN A 47 ? 0.3862 0.3194 0.4692 0.0174 0.0287 -0.0188 88 GLN A CG 302 C CD A GLN A 47 ? 0.3576 0.2994 0.4440 0.0129 0.0242 -0.0313 88 GLN A CD 303 C CD B GLN A 47 ? 0.4641 0.3887 0.5507 0.0173 0.0328 -0.0110 88 GLN A CD 304 O OE1 A GLN A 47 ? 0.2876 0.2365 0.3716 0.0104 0.0227 -0.0339 88 GLN A OE1 305 O OE1 B GLN A 47 ? 0.5135 0.4331 0.6100 0.0139 0.0342 -0.0114 88 GLN A OE1 306 N NE2 A GLN A 47 ? 0.3831 0.3179 0.4773 0.0122 0.0238 -0.0346 88 GLN A NE2 307 N NE2 B GLN A 47 ? 0.4827 0.4054 0.5612 0.0209 0.0348 -0.0039 88 GLN A NE2 308 N N . ASN A 48 ? 0.2770 0.2363 0.3386 0.0154 0.0278 -0.0139 89 ASN A N 309 C CA A ASN A 48 ? 0.2704 0.2346 0.3236 0.0171 0.0278 -0.0106 89 ASN A CA 310 C CA B ASN A 48 ? 0.2870 0.2517 0.3404 0.0169 0.0277 -0.0110 89 ASN A CA 311 C C . ASN A 48 ? 0.2984 0.2619 0.3522 0.0158 0.0312 -0.0050 89 ASN A C 312 O O . ASN A 48 ? 0.3139 0.2771 0.3600 0.0188 0.0325 -0.0001 89 ASN A O 313 C CB A ASN A 48 ? 0.2604 0.2331 0.3104 0.0158 0.0248 -0.0157 89 ASN A CB 314 C CB B ASN A 48 ? 0.2843 0.2573 0.3355 0.0150 0.0247 -0.0164 89 ASN A CB 315 C CG A ASN A 48 ? 0.2238 0.2006 0.2652 0.0184 0.0240 -0.0132 89 ASN A CG 316 C CG B ASN A 48 ? 0.3102 0.2886 0.3543 0.0158 0.0244 -0.0138 89 ASN A CG 317 O OD1 A ASN A 48 ? 0.1883 0.1620 0.2255 0.0224 0.0242 -0.0099 89 ASN A OD1 318 O OD1 B ASN A 48 ? 0.3562 0.3346 0.4003 0.0150 0.0265 -0.0097 89 ASN A OD1 319 N ND2 A ASN A 48 ? 0.2157 0.1993 0.2547 0.0164 0.0227 -0.0149 89 ASN A ND2 320 N ND2 B ASN A 48 ? 0.3380 0.3210 0.3768 0.0174 0.0221 -0.0161 89 ASN A ND2 321 N N . PHE A 49 ? 0.2820 0.2449 0.3449 0.0117 0.0328 -0.0055 90 PHE A N 322 C CA . PHE A 49 ? 0.2921 0.2539 0.3580 0.0103 0.0370 0.0000 90 PHE A CA 323 C C . PHE A 49 ? 0.3008 0.2537 0.3649 0.0133 0.0414 0.0068 90 PHE A C 324 O O . PHE A 49 ? 0.2942 0.2457 0.3523 0.0154 0.0448 0.0128 90 PHE A O 325 C CB . PHE A 49 ? 0.2931 0.2563 0.3719 0.0050 0.0372 -0.0028 90 PHE A CB 326 C CG . PHE A 49 ? 0.3227 0.2847 0.4080 0.0032 0.0424 0.0028 90 PHE A CG 327 C CD1 . PHE A 49 ? 0.3245 0.2902 0.4040 0.0046 0.0450 0.0071 90 PHE A CD1 328 C CD2 . PHE A 49 ? 0.4151 0.3725 0.5135 -0.0001 0.0448 0.0033 90 PHE A CD2 329 C CE1 . PHE A 49 ? 0.3441 0.3092 0.4304 0.0029 0.0504 0.0120 90 PHE A CE1 330 C CE2 . PHE A 49 ? 0.4728 0.4295 0.5792 -0.0021 0.0503 0.0085 90 PHE A CE2 331 C CZ . PHE A 49 ? 0.4223 0.3830 0.5224 -0.0005 0.0534 0.0129 90 PHE A CZ 332 N N A GLN A 50 ? 0.3023 0.2483 0.3702 0.0139 0.0411 0.0060 91 GLN A N 333 N N B GLN A 50 ? 0.3013 0.2474 0.3692 0.0139 0.0411 0.0059 91 GLN A N 334 C CA A GLN A 50 ? 0.3221 0.2586 0.3869 0.0173 0.0449 0.0128 91 GLN A CA 335 C CA B GLN A 50 ? 0.3171 0.2536 0.3821 0.0173 0.0447 0.0125 91 GLN A CA 336 C C A GLN A 50 ? 0.3118 0.2477 0.3625 0.0232 0.0440 0.0163 91 GLN A C 337 C C B GLN A 50 ? 0.3109 0.2465 0.3618 0.0232 0.0439 0.0161 91 GLN A C 338 O O A GLN A 50 ? 0.3141 0.2447 0.3584 0.0259 0.0479 0.0233 91 GLN A O 339 O O B GLN A 50 ? 0.3174 0.2474 0.3623 0.0259 0.0479 0.0232 91 GLN A O 340 C CB A GLN A 50 ? 0.3308 0.2597 0.4025 0.0173 0.0444 0.0112 91 GLN A CB 341 C CB B GLN A 50 ? 0.3225 0.2519 0.3943 0.0173 0.0437 0.0101 91 GLN A CB 342 C CG A GLN A 50 ? 0.3752 0.3022 0.4616 0.0118 0.0461 0.0092 91 GLN A CG 343 C CG B GLN A 50 ? 0.3513 0.2783 0.4375 0.0120 0.0458 0.0088 91 GLN A CG 344 C CD A GLN A 50 ? 0.4358 0.3596 0.5273 0.0097 0.0525 0.0162 91 GLN A CD 345 C CD B GLN A 50 ? 0.3714 0.2925 0.4652 0.0114 0.0436 0.0044 91 GLN A CD 346 O OE1 A GLN A 50 ? 0.4824 0.4097 0.5853 0.0048 0.0534 0.0143 91 GLN A OE1 347 O OE1 B GLN A 50 ? 0.3941 0.3161 0.4839 0.0139 0.0396 -0.0004 91 GLN A OE1 348 N NE2 A GLN A 50 ? 0.4440 0.3611 0.5275 0.0136 0.0570 0.0243 91 GLN A NE2 349 N NE2 B GLN A 50 ? 0.4251 0.3401 0.5309 0.0080 0.0465 0.0057 91 GLN A NE2 350 N N . LEU A 51 ? 0.2989 0.2400 0.3447 0.0250 0.0389 0.0113 92 LEU A N 351 C CA . LEU A 51 ? 0.2931 0.2345 0.3270 0.0303 0.0370 0.0137 92 LEU A CA 352 C C . LEU A 51 ? 0.2836 0.2289 0.3107 0.0305 0.0389 0.0170 92 LEU A C 353 O O . LEU A 51 ? 0.2885 0.2296 0.3057 0.0349 0.0401 0.0222 92 LEU A O 354 C CB . LEU A 51 ? 0.2762 0.2233 0.3087 0.0317 0.0316 0.0075 92 LEU A CB 355 C CG . LEU A 51 ? 0.2923 0.2396 0.3146 0.0371 0.0288 0.0093 92 LEU A CG 356 C CD1 . LEU A 51 ? 0.3242 0.2611 0.3417 0.0424 0.0296 0.0147 92 LEU A CD1 357 C CD2 . LEU A 51 ? 0.2839 0.2378 0.3078 0.0376 0.0242 0.0028 92 LEU A CD2 358 N N . ALA A 52 ? 0.2650 0.2175 0.2969 0.0262 0.0390 0.0141 93 ALA A N 359 C CA . ALA A 52 ? 0.2725 0.2286 0.2993 0.0263 0.0411 0.0171 93 ALA A CA 360 C C . ALA A 52 ? 0.2847 0.2336 0.3097 0.0277 0.0473 0.0246 93 ALA A C 361 O O . ALA A 52 ? 0.2864 0.2338 0.3010 0.0313 0.0491 0.0288 93 ALA A O 362 C CB . ALA A 52 ? 0.2763 0.2404 0.3106 0.0212 0.0405 0.0131 93 ALA A CB 363 N N . LYS A 53 ? 0.2887 0.2328 0.3236 0.0248 0.0509 0.0262 94 LYS A N 364 C CA . LYS A 53 ? 0.3089 0.2459 0.3431 0.0257 0.0580 0.0338 94 LYS A CA 365 C C . LYS A 53 ? 0.3148 0.2425 0.3364 0.0319 0.0590 0.0394 94 LYS A C 366 O O . LYS A 53 ? 0.3264 0.2495 0.3395 0.0350 0.0639 0.0459 94 LYS A O 367 C CB . LYS A 53 ? 0.3193 0.2532 0.3690 0.0207 0.0615 0.0341 94 LYS A CB 368 C CG . LYS A 53 ? 0.3478 0.2904 0.4090 0.0152 0.0615 0.0302 94 LYS A CG 369 C CD . LYS A 53 ? 0.4633 0.4026 0.5407 0.0104 0.0651 0.0307 94 LYS A CD 370 C CE . LYS A 53 ? 0.4994 0.4374 0.5839 0.0083 0.0599 0.0244 94 LYS A CE 371 N NZ . LYS A 53 ? 0.5697 0.5039 0.6709 0.0036 0.0624 0.0241 94 LYS A NZ 372 N N . GLN A 54 ? 0.3125 0.2375 0.3325 0.0342 0.0542 0.0366 95 GLN A N 373 C CA . GLN A 54 ? 0.3328 0.2491 0.3408 0.0408 0.0536 0.0413 95 GLN A CA 374 C C . GLN A 54 ? 0.3349 0.2540 0.3284 0.0454 0.0512 0.0422 95 GLN A C 375 O O . GLN A 54 ? 0.3571 0.2692 0.3388 0.0502 0.0539 0.0483 95 GLN A O 376 C CB . GLN A 54 ? 0.3246 0.2392 0.3356 0.0422 0.0481 0.0369 95 GLN A CB 377 C CG . GLN A 54 ? 0.3465 0.2529 0.3452 0.0495 0.0461 0.0411 95 GLN A CG 378 C CD . GLN A 54 ? 0.3555 0.2631 0.3568 0.0516 0.0396 0.0357 95 GLN A CD 379 O OE1 . GLN A 54 ? 0.3544 0.2627 0.3672 0.0483 0.0390 0.0315 95 GLN A OE1 380 N NE2 . GLN A 54 ? 0.3684 0.2761 0.3595 0.0572 0.0348 0.0356 95 GLN A NE2 381 N N . ILE A 55 ? 0.3220 0.2509 0.3162 0.0441 0.0462 0.0359 96 ILE A N 382 C CA . ILE A 55 ? 0.3207 0.2527 0.3028 0.0481 0.0431 0.0358 96 ILE A CA 383 C C . ILE A 55 ? 0.3195 0.2507 0.2955 0.0485 0.0487 0.0407 96 ILE A C 384 O O . ILE A 55 ? 0.3283 0.2549 0.2904 0.0539 0.0491 0.0445 96 ILE A O 385 C CB . ILE A 55 ? 0.3102 0.2529 0.2962 0.0456 0.0374 0.0284 96 ILE A CB 386 C CG1 A ILE A 55 ? 0.3385 0.2822 0.3296 0.0460 0.0323 0.0236 96 ILE A CG1 387 C CG1 B ILE A 55 ? 0.3052 0.2478 0.2941 0.0472 0.0320 0.0243 96 ILE A CG1 388 C CG2 . ILE A 55 ? 0.3228 0.2688 0.2977 0.0490 0.0347 0.0282 96 ILE A CG2 389 C CD1 A ILE A 55 ? 0.3571 0.2956 0.3400 0.0521 0.0287 0.0250 96 ILE A CD1 390 C CD1 B ILE A 55 ? 0.2526 0.2047 0.2487 0.0437 0.0280 0.0170 96 ILE A CD1 391 N N . GLN A 56 ? 0.3135 0.2488 0.3000 0.0430 0.0531 0.0403 97 GLN A N 392 C CA . GLN A 56 ? 0.3168 0.2519 0.2999 0.0431 0.0593 0.0449 97 GLN A CA 393 C C . GLN A 56 ? 0.3455 0.2692 0.3194 0.0475 0.0653 0.0531 97 GLN A C 394 O O . GLN A 56 ? 0.3612 0.2822 0.3222 0.0519 0.0680 0.0570 97 GLN A O 395 C CB . GLN A 56 ? 0.3170 0.2575 0.3157 0.0365 0.0631 0.0435 97 GLN A CB 396 C CG . GLN A 56 ? 0.3340 0.2742 0.3321 0.0363 0.0709 0.0487 97 GLN A CG 397 C CD . GLN A 56 ? 0.3631 0.3088 0.3789 0.0297 0.0742 0.0472 97 GLN A CD 398 O OE1 . GLN A 56 ? 0.3745 0.3199 0.4026 0.0256 0.0730 0.0447 97 GLN A OE1 399 N NE2 . GLN A 56 ? 0.3393 0.2900 0.3568 0.0288 0.0779 0.0482 97 GLN A NE2 400 N N . SER A 57 ? 0.3500 0.2666 0.3298 0.0466 0.0675 0.0557 98 SER A N 401 C CA . SER A 57 ? 0.3725 0.2772 0.3437 0.0507 0.0738 0.0643 98 SER A CA 402 C C . SER A 57 ? 0.3756 0.2740 0.3275 0.0587 0.0698 0.0664 98 SER A C 403 O O . SER A 57 ? 0.3902 0.2816 0.3282 0.0635 0.0743 0.0727 98 SER A O 404 C CB . SER A 57 ? 0.3751 0.2732 0.3574 0.0480 0.0760 0.0660 98 SER A CB 405 O OG A SER A 57 ? 0.3690 0.2549 0.3429 0.0518 0.0823 0.0747 98 SER A OG 406 O OG B SER A 57 ? 0.4147 0.3157 0.4128 0.0415 0.0821 0.0666 98 SER A OG 407 N N . GLN A 58 ? 0.3609 0.2618 0.3121 0.0603 0.0611 0.0610 99 GLN A N 408 C CA . GLN A 58 ? 0.3794 0.2749 0.3146 0.0679 0.0558 0.0620 99 GLN A CA 409 C C . GLN A 58 ? 0.3727 0.2720 0.2953 0.0713 0.0538 0.0611 99 GLN A C 410 O O . GLN A 58 ? 0.3894 0.2811 0.2953 0.0781 0.0535 0.0652 99 GLN A O 411 C CB . GLN A 58 ? 0.3692 0.2677 0.3097 0.0684 0.0472 0.0560 99 GLN A CB 412 C CG . GLN A 58 ? 0.4039 0.2952 0.3530 0.0673 0.0489 0.0579 99 GLN A CG 413 C CD . GLN A 58 ? 0.4500 0.3432 0.4032 0.0690 0.0408 0.0524 99 GLN A CD 414 O OE1 . GLN A 58 ? 0.4291 0.3323 0.3909 0.0656 0.0366 0.0452 99 GLN A OE1 415 N NE2 . GLN A 58 ? 0.5497 0.4331 0.4965 0.0745 0.0389 0.0560 99 GLN A NE2 416 N N . TRP A 59 ? 0.3498 0.2602 0.2795 0.0670 0.0520 0.0555 100 TRP A N 417 C CA . TRP A 59 ? 0.3501 0.2637 0.2686 0.0700 0.0505 0.0545 100 TRP A CA 418 C C . TRP A 59 ? 0.3789 0.2865 0.2875 0.0725 0.0591 0.0614 100 TRP A C 419 O O . TRP A 59 ? 0.3901 0.2945 0.2827 0.0782 0.0582 0.0628 100 TRP A O 420 C CB . TRP A 59 ? 0.3300 0.2560 0.2591 0.0646 0.0479 0.0478 100 TRP A CB 421 C CG . TRP A 59 ? 0.3043 0.2361 0.2382 0.0639 0.0392 0.0411 100 TRP A CG 422 C CD1 . TRP A 59 ? 0.3226 0.2508 0.2550 0.0670 0.0340 0.0400 100 TRP A CD1 423 C CD2 . TRP A 59 ? 0.2968 0.2392 0.2388 0.0597 0.0353 0.0346 100 TRP A CD2 424 N NE1 . TRP A 59 ? 0.3257 0.2620 0.2651 0.0651 0.0273 0.0332 100 TRP A NE1 425 C CE2 . TRP A 59 ? 0.2877 0.2324 0.2325 0.0605 0.0282 0.0300 100 TRP A CE2 426 C CE3 . TRP A 59 ? 0.3072 0.2570 0.2541 0.0557 0.0371 0.0325 100 TRP A CE3 427 C CZ2 . TRP A 59 ? 0.2876 0.2418 0.2401 0.0571 0.0235 0.0236 100 TRP A CZ2 428 C CZ3 . TRP A 59 ? 0.2855 0.2442 0.2392 0.0524 0.0319 0.0263 100 TRP A CZ3 429 C CH2 . TRP A 59 ? 0.2774 0.2380 0.2335 0.0530 0.0255 0.0220 100 TRP A CH2 430 N N . LYS A 60 ? 0.3838 0.2898 0.3020 0.0683 0.0675 0.0655 101 LYS A N 431 C CA A LYS A 60 ? 0.4202 0.3198 0.3305 0.0705 0.0773 0.0730 101 LYS A CA 432 C CA B LYS A 60 ? 0.4161 0.3158 0.3263 0.0705 0.0772 0.0729 101 LYS A CA 433 C C . LYS A 60 ? 0.4354 0.3215 0.3275 0.0781 0.0784 0.0796 101 LYS A C 434 O O . LYS A 60 ? 0.4610 0.3419 0.3358 0.0839 0.0813 0.0833 101 LYS A O 435 C CB A LYS A 60 ? 0.4241 0.3243 0.3511 0.0640 0.0859 0.0761 101 LYS A CB 436 C CB B LYS A 60 ? 0.4168 0.3177 0.3442 0.0639 0.0857 0.0758 101 LYS A CB 437 C CG A LYS A 60 ? 0.4506 0.3612 0.3892 0.0588 0.0891 0.0732 101 LYS A CG 438 C CG B LYS A 60 ? 0.4179 0.3314 0.3620 0.0569 0.0850 0.0699 101 LYS A CG 439 C CD A LYS A 60 ? 0.4875 0.3989 0.4443 0.0525 0.0970 0.0760 101 LYS A CD 440 C CD B LYS A 60 ? 0.4400 0.3546 0.4035 0.0502 0.0909 0.0713 101 LYS A CD 441 C CE A LYS A 60 ? 0.4904 0.4146 0.4635 0.0462 0.0956 0.0699 101 LYS A CE 442 C CE B LYS A 60 ? 0.4517 0.3773 0.4288 0.0447 0.0926 0.0676 101 LYS A CE 443 N NZ A LYS A 60 ? 0.5203 0.4474 0.4963 0.0454 0.1040 0.0731 101 LYS A NZ 444 N NZ B LYS A 60 ? 0.4800 0.4053 0.4748 0.0391 0.0999 0.0705 101 LYS A NZ 445 N N A GLU A 61 ? 0.4370 0.3170 0.3318 0.0786 0.0760 0.0809 102 GLU A N 446 N N B GLU A 61 ? 0.4390 0.3192 0.3344 0.0784 0.0759 0.0807 102 GLU A N 447 C CA A GLU A 61 ? 0.4576 0.3239 0.3353 0.0861 0.0768 0.0876 102 GLU A CA 448 C CA B GLU A 61 ? 0.4655 0.3322 0.3450 0.0856 0.0759 0.0870 102 GLU A CA 449 C C A GLU A 61 ? 0.4593 0.3244 0.3199 0.0935 0.0672 0.0844 102 GLU A C 450 C C B GLU A 61 ? 0.4645 0.3301 0.3254 0.0932 0.0677 0.0844 102 GLU A C 451 O O A GLU A 61 ? 0.4732 0.3276 0.3144 0.1010 0.0678 0.0898 102 GLU A O 452 O O B GLU A 61 ? 0.4738 0.3294 0.3148 0.1004 0.0697 0.0900 102 GLU A O 453 C CB A GLU A 61 ? 0.4643 0.3240 0.3508 0.0846 0.0768 0.0899 102 GLU A CB 454 C CB B GLU A 61 ? 0.4726 0.3355 0.3616 0.0844 0.0721 0.0863 102 GLU A CB 455 C CG A GLU A 61 ? 0.5137 0.3609 0.3837 0.0928 0.0729 0.0942 102 GLU A CG 456 C CG B GLU A 61 ? 0.5250 0.3877 0.4332 0.0771 0.0790 0.0883 102 GLU A CG 457 C CD A GLU A 61 ? 0.6147 0.4486 0.4677 0.0982 0.0816 0.1045 102 GLU A CD 458 C CD B GLU A 61 ? 0.5799 0.4415 0.5000 0.0751 0.0735 0.0849 102 GLU A CD 459 O OE1 A GLU A 61 ? 0.6531 0.4858 0.5117 0.0943 0.0925 0.1095 102 GLU A OE1 460 O OE1 B GLU A 61 ? 0.5808 0.4373 0.4922 0.0807 0.0667 0.0844 102 GLU A OE1 461 O OE2 A GLU A 61 ? 0.6390 0.4633 0.4728 0.1065 0.0776 0.1075 102 GLU A OE2 462 O OE2 B GLU A 61 ? 0.5812 0.4470 0.5198 0.0681 0.0758 0.0824 102 GLU A OE2 463 N N . PHE A 62 ? 0.4328 0.3086 0.3001 0.0914 0.0585 0.0759 103 PHE A N 464 C CA . PHE A 62 ? 0.4398 0.3158 0.2931 0.0977 0.0493 0.0720 103 PHE A CA 465 C C . PHE A 62 ? 0.4518 0.3272 0.2900 0.1015 0.0518 0.0731 103 PHE A C 466 O O . PHE A 62 ? 0.4884 0.3603 0.3109 0.1083 0.0455 0.0719 103 PHE A O 467 C CB . PHE A 62 ? 0.4115 0.2995 0.2775 0.0941 0.0400 0.0626 103 PHE A CB 468 C CG . PHE A 62 ? 0.4136 0.3021 0.2912 0.0925 0.0350 0.0600 103 PHE A CG 469 C CD1 . PHE A 62 ? 0.4464 0.3243 0.3201 0.0961 0.0357 0.0651 103 PHE A CD1 470 C CD2 . PHE A 62 ? 0.4035 0.3032 0.2959 0.0875 0.0298 0.0524 103 PHE A CD2 471 C CE1 . PHE A 62 ? 0.4731 0.3521 0.3587 0.0947 0.0309 0.0619 103 PHE A CE1 472 C CE2 . PHE A 62 ? 0.4016 0.3025 0.3051 0.0861 0.0255 0.0493 103 PHE A CE2 473 C CZ . PHE A 62 ? 0.4192 0.3102 0.3198 0.0896 0.0260 0.0538 103 PHE A CZ 474 N N . GLY A 63 ? 0.4442 0.3235 0.2880 0.0972 0.0606 0.0750 104 GLY A N 475 C CA . GLY A 63 ? 0.4599 0.3371 0.2889 0.1012 0.0650 0.0771 104 GLY A CA 476 C C . GLY A 63 ? 0.4439 0.3327 0.2818 0.0967 0.0652 0.0717 104 GLY A C 477 O O . GLY A 63 ? 0.4626 0.3505 0.2892 0.1001 0.0683 0.0725 104 GLY A O 478 N N . LEU A 64 ? 0.4164 0.3159 0.2738 0.0895 0.0619 0.0661 105 LEU A N 479 C CA . LEU A 64 ? 0.4072 0.3172 0.2724 0.0855 0.0621 0.0613 105 LEU A CA 480 C C . LEU A 64 ? 0.4141 0.3244 0.2818 0.0836 0.0733 0.0659 105 LEU A C 481 O O . LEU A 64 ? 0.4402 0.3457 0.3124 0.0819 0.0816 0.0719 105 LEU A O 482 C CB . LEU A 64 ? 0.3849 0.3053 0.2698 0.0781 0.0571 0.0551 105 LEU A CB 483 C CG . LEU A 64 ? 0.3742 0.2968 0.2593 0.0793 0.0463 0.0495 105 LEU A CG 484 C CD1 . LEU A 64 ? 0.3502 0.2839 0.2531 0.0721 0.0428 0.0433 105 LEU A CD1 485 C CD2 . LEU A 64 ? 0.3828 0.3042 0.2529 0.0854 0.0396 0.0466 105 LEU A CD2 486 N N . ASP A 65 ? 0.4145 0.3304 0.2804 0.0838 0.0739 0.0631 106 ASP A N 487 C CA . ASP A 65 ? 0.4394 0.3561 0.3076 0.0827 0.0847 0.0671 106 ASP A CA 488 C C . ASP A 65 ? 0.4450 0.3693 0.3364 0.0743 0.0895 0.0670 106 ASP A C 489 O O . ASP A 65 ? 0.4635 0.3858 0.3602 0.0728 0.0997 0.0725 106 ASP A O 490 C CB . ASP A 65 ? 0.4248 0.3461 0.2863 0.0852 0.0831 0.0632 106 ASP A CB 491 C CG . ASP A 65 ? 0.4780 0.3907 0.3155 0.0941 0.0799 0.0637 106 ASP A CG 492 O OD1 . ASP A 65 ? 0.5001 0.4028 0.3237 0.0991 0.0868 0.0704 106 ASP A OD1 493 O OD2 . ASP A 65 ? 0.4468 0.3621 0.2791 0.0961 0.0705 0.0577 106 ASP A OD2 494 N N . SER A 66 ? 0.4136 0.3466 0.3188 0.0690 0.0822 0.0607 107 SER A N 495 C CA . SER A 66 ? 0.3909 0.3309 0.3174 0.0612 0.0849 0.0596 107 SER A CA 496 C C . SER A 66 ? 0.3666 0.3102 0.3017 0.0576 0.0761 0.0543 107 SER A C 497 O O . SER A 66 ? 0.3335 0.2787 0.2619 0.0598 0.0679 0.0499 107 SER A O 498 C CB . SER A 66 ? 0.3955 0.3447 0.3304 0.0585 0.0869 0.0568 107 SER A CB 499 O OG A SER A 66 ? 0.3741 0.3296 0.3079 0.0583 0.0782 0.0501 107 SER A OG 500 O OG B SER A 66 ? 0.4123 0.3701 0.3662 0.0514 0.0841 0.0525 107 SER A OG 501 N N . VAL A 67 ? 0.3351 0.2799 0.2853 0.0523 0.0780 0.0547 108 VAL A N 502 C CA . VAL A 67 ? 0.3286 0.2775 0.2876 0.0487 0.0702 0.0491 108 VAL A CA 503 C C . VAL A 67 ? 0.3312 0.2857 0.3094 0.0416 0.0728 0.0476 108 VAL A C 504 O O . VAL A 67 ? 0.3402 0.2906 0.3259 0.0397 0.0791 0.0519 108 VAL A O 505 C CB . VAL A 67 ? 0.3371 0.2778 0.2913 0.0511 0.0681 0.0511 108 VAL A CB 506 C CG1 . VAL A 67 ? 0.3267 0.2725 0.2884 0.0483 0.0598 0.0445 108 VAL A CG1 507 C CG2 . VAL A 67 ? 0.3483 0.2812 0.2823 0.0591 0.0664 0.0539 108 VAL A CG2 508 N N . GLU A 68 ? 0.3258 0.2894 0.3120 0.0379 0.0677 0.0416 109 GLU A N 509 C CA . GLU A 68 ? 0.3318 0.3016 0.3357 0.0315 0.0688 0.0392 109 GLU A CA 510 C C . GLU A 68 ? 0.3189 0.2928 0.3295 0.0281 0.0615 0.0331 109 GLU A C 511 O O . GLU A 68 ? 0.3175 0.2922 0.3203 0.0301 0.0555 0.0299 109 GLU A O 512 C CB . GLU A 68 ? 0.3598 0.3371 0.3676 0.0303 0.0700 0.0378 109 GLU A CB 513 C CG . GLU A 68 ? 0.4457 0.4196 0.4479 0.0337 0.0785 0.0437 109 GLU A CG 514 C CD . GLU A 68 ? 0.5734 0.5425 0.5844 0.0319 0.0872 0.0494 109 GLU A CD 515 O OE1 . GLU A 68 ? 0.5720 0.5444 0.6000 0.0263 0.0874 0.0477 109 GLU A OE1 516 O OE2 . GLU A 68 ? 0.6515 0.6130 0.6523 0.0361 0.0939 0.0556 109 GLU A OE2 517 N N . LEU A 69 ? 0.2992 0.2757 0.3247 0.0229 0.0620 0.0312 110 LEU A N 518 C CA . LEU A 69 ? 0.3000 0.2813 0.3313 0.0196 0.0551 0.0246 110 LEU A CA 519 C C . LEU A 69 ? 0.2999 0.2899 0.3370 0.0168 0.0529 0.0211 110 LEU A C 520 O O . LEU A 69 ? 0.3193 0.3117 0.3643 0.0151 0.0571 0.0230 110 LEU A O 521 C CB . LEU A 69 ? 0.3025 0.2813 0.3457 0.0158 0.0556 0.0236 110 LEU A CB 522 C CG . LEU A 69 ? 0.3423 0.3120 0.3823 0.0180 0.0578 0.0270 110 LEU A CG 523 C CD1 . LEU A 69 ? 0.3829 0.3514 0.4365 0.0136 0.0569 0.0241 110 LEU A CD1 524 C CD2 . LEU A 69 ? 0.3518 0.3198 0.3798 0.0220 0.0529 0.0254 110 LEU A CD2 525 N N . ALA A 70 ? 0.2731 0.2675 0.3064 0.0165 0.0465 0.0162 111 ALA A N 526 C CA . ALA A 70 ? 0.2569 0.2588 0.2951 0.0140 0.0434 0.0125 111 ALA A CA 527 C C . ALA A 70 ? 0.2519 0.2559 0.2963 0.0104 0.0385 0.0073 111 ALA A C 528 O O . ALA A 70 ? 0.2777 0.2806 0.3161 0.0114 0.0349 0.0048 111 ALA A O 529 C CB . ALA A 70 ? 0.2785 0.2831 0.3062 0.0168 0.0403 0.0115 111 ALA A CB 530 N N . HIS A 71 ? 0.2349 0.2419 0.2917 0.0065 0.0384 0.0054 112 HIS A N 531 C CA . HIS A 71 ? 0.2319 0.2400 0.2939 0.0034 0.0336 0.0000 112 HIS A CA 532 C C . HIS A 71 ? 0.2082 0.2230 0.2720 0.0014 0.0286 -0.0042 112 HIS A C 533 O O . HIS A 71 ? 0.2244 0.2431 0.2912 0.0013 0.0294 -0.0030 112 HIS A O 534 C CB . HIS A 71 ? 0.2460 0.2512 0.3207 0.0004 0.0357 -0.0001 112 HIS A CB 535 C CG . HIS A 71 ? 0.2834 0.2919 0.3707 -0.0022 0.0381 0.0009 112 HIS A CG 536 N ND1 . HIS A 71 ? 0.3368 0.3434 0.4281 -0.0015 0.0450 0.0067 112 HIS A ND1 537 C CD2 . HIS A 71 ? 0.2930 0.3067 0.3904 -0.0055 0.0344 -0.0031 112 HIS A CD2 538 C CE1 . HIS A 71 ? 0.3501 0.3612 0.4550 -0.0044 0.0459 0.0061 112 HIS A CE1 539 N NE2 . HIS A 71 ? 0.3340 0.3495 0.4431 -0.0068 0.0390 0.0000 112 HIS A NE2 540 N N . TYR A 72 ? 0.2246 0.2400 0.2865 0.0002 0.0238 -0.0091 113 TYR A N 541 C CA . TYR A 72 ? 0.2092 0.2296 0.2705 -0.0014 0.0185 -0.0133 113 TYR A CA 542 C C . TYR A 72 ? 0.2138 0.2331 0.2788 -0.0037 0.0149 -0.0184 113 TYR A C 543 O O . TYR A 72 ? 0.2284 0.2434 0.2929 -0.0034 0.0160 -0.0190 113 TYR A O 544 C CB . TYR A 72 ? 0.1987 0.2207 0.2477 0.0009 0.0164 -0.0136 113 TYR A CB 545 C CG . TYR A 72 ? 0.2016 0.2236 0.2459 0.0037 0.0196 -0.0090 113 TYR A CG 546 C CD1 . TYR A 72 ? 0.2133 0.2390 0.2601 0.0038 0.0198 -0.0078 113 TYR A CD1 547 C CD2 . TYR A 72 ? 0.2372 0.2552 0.2755 0.0065 0.0224 -0.0062 113 TYR A CD2 548 C CE1 . TYR A 72 ? 0.2423 0.2676 0.2845 0.0067 0.0230 -0.0039 113 TYR A CE1 549 C CE2 . TYR A 72 ? 0.2436 0.2609 0.2768 0.0094 0.0250 -0.0024 113 TYR A CE2 550 C CZ . TYR A 72 ? 0.2511 0.2719 0.2860 0.0095 0.0256 -0.0013 113 TYR A CZ 551 O OH . TYR A 72 ? 0.2608 0.2803 0.2897 0.0129 0.0286 0.0022 113 TYR A OH 552 N N . ASP A 73 ? 0.2068 0.2296 0.2743 -0.0055 0.0102 -0.0223 114 ASP A N 553 C CA . ASP A 73 ? 0.2224 0.2439 0.2914 -0.0073 0.0060 -0.0280 114 ASP A CA 554 C C . ASP A 73 ? 0.2201 0.2434 0.2777 -0.0064 0.0021 -0.0308 114 ASP A C 555 O O . ASP A 73 ? 0.2158 0.2427 0.2717 -0.0066 -0.0011 -0.0314 114 ASP A O 556 C CB . ASP A 73 ? 0.2270 0.2504 0.3091 -0.0102 0.0032 -0.0306 114 ASP A CB 557 C CG . ASP A 73 ? 0.3030 0.3244 0.3977 -0.0115 0.0080 -0.0274 114 ASP A CG 558 O OD1 . ASP A 73 ? 0.3022 0.3185 0.3968 -0.0112 0.0109 -0.0266 114 ASP A OD1 559 O OD2 . ASP A 73 ? 0.3323 0.3570 0.4369 -0.0127 0.0091 -0.0256 114 ASP A OD2 560 N N . VAL A 74 ? 0.2075 0.2280 0.2572 -0.0052 0.0027 -0.0323 115 VAL A N 561 C CA . VAL A 74 ? 0.2105 0.2323 0.2486 -0.0040 0.0008 -0.0337 115 VAL A CA 562 C C . VAL A 74 ? 0.2249 0.2445 0.2591 -0.0044 -0.0016 -0.0391 115 VAL A C 563 O O . VAL A 74 ? 0.2335 0.2499 0.2728 -0.0049 -0.0011 -0.0414 115 VAL A O 564 C CB . VAL A 74 ? 0.2101 0.2316 0.2417 -0.0016 0.0043 -0.0301 115 VAL A CB 565 C CG1 . VAL A 74 ? 0.2049 0.2281 0.2384 -0.0007 0.0064 -0.0252 115 VAL A CG1 566 C CG2 . VAL A 74 ? 0.1937 0.2113 0.2266 -0.0006 0.0071 -0.0302 115 VAL A CG2 567 N N . LEU A 75 ? 0.2228 0.2436 0.2471 -0.0037 -0.0036 -0.0409 116 LEU A N 568 C CA . LEU A 75 ? 0.2198 0.2382 0.2385 -0.0036 -0.0051 -0.0461 116 LEU A CA 569 C C . LEU A 75 ? 0.2271 0.2435 0.2436 -0.0021 -0.0011 -0.0459 116 LEU A C 570 O O . LEU A 75 ? 0.2422 0.2602 0.2539 -0.0008 0.0015 -0.0430 116 LEU A O 571 C CB . LEU A 75 ? 0.2148 0.2345 0.2225 -0.0031 -0.0077 -0.0474 116 LEU A CB 572 C CG . LEU A 75 ? 0.2473 0.2642 0.2484 -0.0028 -0.0099 -0.0532 116 LEU A CG 573 C CD1 . LEU A 75 ? 0.2565 0.2722 0.2635 -0.0042 -0.0153 -0.0574 116 LEU A CD1 574 C CD2 . LEU A 75 ? 0.2889 0.3063 0.2768 -0.0018 -0.0106 -0.0532 116 LEU A CD2 575 N N . LEU A 76 ? 0.2231 0.2360 0.2437 -0.0022 -0.0008 -0.0494 117 LEU A N 576 C CA . LEU A 76 ? 0.2241 0.2348 0.2429 -0.0005 0.0025 -0.0502 117 LEU A CA 577 C C . LEU A 76 ? 0.2440 0.2525 0.2573 -0.0001 0.0011 -0.0564 117 LEU A C 578 O O . LEU A 76 ? 0.2745 0.2830 0.2844 -0.0010 -0.0028 -0.0596 117 LEU A O 579 C CB . LEU A 76 ? 0.2234 0.2309 0.2514 -0.0002 0.0046 -0.0485 117 LEU A CB 580 C CG . LEU A 76 ? 0.2228 0.2316 0.2549 0.0000 0.0067 -0.0422 117 LEU A CG 581 C CD1 . LEU A 76 ? 0.2403 0.2446 0.2795 0.0008 0.0093 -0.0403 117 LEU A CD1 582 C CD2 . LEU A 76 ? 0.2391 0.2511 0.2646 0.0018 0.0083 -0.0387 117 LEU A CD2 583 N N . SER A 77 ? 0.2402 0.2471 0.2518 0.0017 0.0040 -0.0582 118 SER A N 584 C CA . SER A 77 ? 0.2566 0.2613 0.2616 0.0027 0.0036 -0.0642 118 SER A CA 585 C C . SER A 77 ? 0.2658 0.2669 0.2762 0.0041 0.0058 -0.0667 118 SER A C 586 O O . SER A 77 ? 0.2667 0.2684 0.2809 0.0054 0.0090 -0.0634 118 SER A O 587 C CB . SER A 77 ? 0.2759 0.2836 0.2707 0.0039 0.0062 -0.0634 118 SER A CB 588 O OG . SER A 77 ? 0.2944 0.3000 0.2825 0.0055 0.0078 -0.0686 118 SER A OG 589 N N . TYR A 78 ? 0.2599 0.2568 0.2704 0.0041 0.0038 -0.0727 119 TYR A N 590 C CA . TYR A 78 ? 0.2657 0.2585 0.2815 0.0057 0.0056 -0.0756 119 TYR A CA 591 C C . TYR A 78 ? 0.2810 0.2707 0.2901 0.0071 0.0049 -0.0831 119 TYR A C 592 O O . TYR A 78 ? 0.3058 0.2945 0.3089 0.0062 0.0010 -0.0869 119 TYR A O 593 C CB . TYR A 78 ? 0.2782 0.2669 0.3054 0.0039 0.0034 -0.0754 119 TYR A CB 594 C CG . TYR A 78 ? 0.2720 0.2625 0.3063 0.0027 0.0045 -0.0682 119 TYR A CG 595 C CD1 . TYR A 78 ? 0.2914 0.2820 0.3283 0.0045 0.0082 -0.0635 119 TYR A CD1 596 C CD2 . TYR A 78 ? 0.3148 0.3067 0.3532 0.0000 0.0017 -0.0664 119 TYR A CD2 597 C CE1 . TYR A 78 ? 0.2717 0.2632 0.3135 0.0039 0.0093 -0.0569 119 TYR A CE1 598 C CE2 . TYR A 78 ? 0.3229 0.3162 0.3674 -0.0009 0.0034 -0.0599 119 TYR A CE2 599 C CZ . TYR A 78 ? 0.3148 0.3073 0.3602 0.0012 0.0072 -0.0552 119 TYR A CZ 600 O OH . TYR A 78 ? 0.2930 0.2861 0.3428 0.0008 0.0091 -0.0489 119 TYR A OH 601 N N . PRO A 79 ? 0.2847 0.2724 0.2947 0.0096 0.0083 -0.0855 120 PRO A N 602 C CA . PRO A 79 ? 0.3137 0.2973 0.3180 0.0111 0.0074 -0.0934 120 PRO A CA 603 C C . PRO A 79 ? 0.3406 0.3185 0.3506 0.0096 0.0023 -0.0981 120 PRO A C 604 O O . PRO A 79 ? 0.3308 0.3073 0.3519 0.0075 0.0006 -0.0952 120 PRO A O 605 C CB . PRO A 79 ? 0.3204 0.3029 0.3276 0.0143 0.0122 -0.0948 120 PRO A CB 606 C CG . PRO A 79 ? 0.3037 0.2908 0.3163 0.0144 0.0152 -0.0875 120 PRO A CG 607 C CD . PRO A 79 ? 0.2854 0.2740 0.3014 0.0114 0.0123 -0.0819 120 PRO A CD 608 N N . ASN A 80 ? 0.3572 0.3316 0.3595 0.0108 0.0001 -0.1057 121 ASN A N 609 C CA . ASN A 80 ? 0.3964 0.3648 0.4044 0.0097 -0.0053 -0.1115 121 ASN A CA 610 C C . ASN A 80 ? 0.4186 0.3818 0.4333 0.0117 -0.0029 -0.1150 121 ASN A C 611 O O . ASN A 80 ? 0.4148 0.3770 0.4224 0.0150 0.0003 -0.1189 121 ASN A O 612 C CB . ASN A 80 ? 0.3992 0.3658 0.3948 0.0104 -0.0098 -0.1184 121 ASN A CB 613 C CG . ASN A 80 ? 0.4457 0.4064 0.4480 0.0089 -0.0166 -0.1250 121 ASN A CG 614 O OD1 . ASN A 80 ? 0.4960 0.4523 0.5100 0.0085 -0.0165 -0.1267 121 ASN A OD1 615 N ND2 . ASN A 80 ? 0.4942 0.4547 0.4898 0.0082 -0.0227 -0.1286 121 ASN A ND2 616 N N . LYS A 81 ? 0.4488 0.4087 0.4776 0.0099 -0.0040 -0.1130 122 LYS A N 617 C CA . LYS A 81 ? 0.4957 0.4499 0.5325 0.0117 -0.0019 -0.1151 122 LYS A CA 618 C C . LYS A 81 ? 0.5115 0.4593 0.5446 0.0138 -0.0043 -0.1252 122 LYS A C 619 O O . LYS A 81 ? 0.5343 0.4786 0.5689 0.0168 -0.0013 -0.1282 122 LYS A O 620 C CB . LYS A 81 ? 0.5023 0.4533 0.5544 0.0090 -0.0029 -0.1106 122 LYS A CB 621 C CG . LYS A 81 ? 0.5584 0.5133 0.6145 0.0090 0.0013 -0.1008 122 LYS A CG 622 C CD . LYS A 81 ? 0.6414 0.5928 0.7109 0.0061 0.0006 -0.0959 122 LYS A CD 623 C CE . LYS A 81 ? 0.6962 0.6386 0.7754 0.0065 -0.0001 -0.0998 122 LYS A CE 624 N NZ . LYS A 81 ? 0.7349 0.6746 0.8127 0.0108 0.0034 -0.1006 122 LYS A NZ 625 N N . THR A 82 ? 0.5182 0.4646 0.5460 0.0124 -0.0099 -0.1308 123 THR A N 626 C CA . THR A 82 ? 0.5287 0.4685 0.5513 0.0146 -0.0129 -0.1411 123 THR A CA 627 C C . THR A 82 ? 0.5285 0.4700 0.5320 0.0177 -0.0124 -0.1460 123 THR A C 628 O O . THR A 82 ? 0.5391 0.4751 0.5354 0.0198 -0.0154 -0.1549 123 THR A O 629 C CB . THR A 82 ? 0.5432 0.4777 0.5753 0.0115 -0.0206 -0.1460 123 THR A CB 630 O OG1 . THR A 82 ? 0.5560 0.4948 0.5846 0.0088 -0.0252 -0.1444 123 THR A OG1 631 C CG2 . THR A 82 ? 0.5574 0.4889 0.6085 0.0087 -0.0198 -0.1412 123 THR A CG2 632 N N . HIS A 83 ? 0.4954 0.4439 0.4903 0.0181 -0.0083 -0.1401 124 HIS A N 633 C CA . HIS A 83 ? 0.5011 0.4512 0.4776 0.0208 -0.0066 -0.1431 124 HIS A CA 634 C C . HIS A 83 ? 0.4791 0.4359 0.4523 0.0222 0.0014 -0.1363 124 HIS A C 635 O O . HIS A 83 ? 0.4696 0.4319 0.4377 0.0207 0.0022 -0.1305 124 HIS A O 636 C CB . HIS A 83 ? 0.5147 0.4661 0.4831 0.0189 -0.0127 -0.1432 124 HIS A CB 637 C CG . HIS A 83 ? 0.5715 0.5213 0.5197 0.0220 -0.0131 -0.1485 124 HIS A CG 638 N ND1 . HIS A 83 ? 0.6317 0.5825 0.5694 0.0212 -0.0183 -0.1485 124 HIS A ND1 639 C CD2 . HIS A 83 ? 0.6435 0.5905 0.5795 0.0263 -0.0087 -0.1538 124 HIS A CD2 640 C CE1 . HIS A 83 ? 0.6631 0.6109 0.5818 0.0249 -0.0173 -0.1535 124 HIS A CE1 641 N NE2 . HIS A 83 ? 0.6840 0.6296 0.6012 0.0280 -0.0111 -0.1568 124 HIS A NE2 642 N N . PRO A 84 ? 0.4648 0.4211 0.4420 0.0250 0.0071 -0.1372 125 PRO A N 643 C CA . PRO A 84 ? 0.4432 0.4065 0.4226 0.0255 0.0137 -0.1299 125 PRO A CA 644 C C . PRO A 84 ? 0.4372 0.4050 0.4021 0.0271 0.0185 -0.1289 125 PRO A C 645 O O . PRO A 84 ? 0.4444 0.4094 0.3956 0.0293 0.0188 -0.1348 125 PRO A O 646 C CB . PRO A 84 ? 0.4615 0.4227 0.4507 0.0283 0.0176 -0.1316 125 PRO A CB 647 C CG . PRO A 84 ? 0.4824 0.4355 0.4701 0.0301 0.0146 -0.1409 125 PRO A CG 648 C CD . PRO A 84 ? 0.4867 0.4364 0.4686 0.0276 0.0073 -0.1443 125 PRO A CD 649 N N . ASN A 85 ? 0.3989 0.3735 0.3669 0.0260 0.0223 -0.1212 126 ASN A N 650 C CA . ASN A 85 ? 0.3943 0.3739 0.3516 0.0270 0.0276 -0.1187 126 ASN A CA 651 C C . ASN A 85 ? 0.3888 0.3696 0.3466 0.0307 0.0351 -0.1214 126 ASN A C 652 O O . ASN A 85 ? 0.3997 0.3808 0.3701 0.0318 0.0366 -0.1212 126 ASN A O 653 C CB . ASN A 85 ? 0.3612 0.3474 0.3242 0.0243 0.0285 -0.1098 126 ASN A CB 654 C CG . ASN A 85 ? 0.3931 0.3788 0.3568 0.0208 0.0219 -0.1066 126 ASN A CG 655 O OD1 . ASN A 85 ? 0.3809 0.3631 0.3360 0.0203 0.0173 -0.1102 126 ASN A OD1 656 N ND2 . ASN A 85 ? 0.3554 0.3447 0.3294 0.0187 0.0212 -0.1000 126 ASN A ND2 657 N N . TYR A 86 ? 0.3946 0.3756 0.3385 0.0328 0.0397 -0.1241 127 TYR A N 658 C CA . TYR A 86 ? 0.3928 0.3765 0.3379 0.0363 0.0482 -0.1259 127 TYR A CA 659 C C . TYR A 86 ? 0.4004 0.3857 0.3295 0.0375 0.0539 -0.1258 127 TYR A C 660 O O . TYR A 86 ? 0.4089 0.3917 0.3246 0.0363 0.0506 -0.1254 127 TYR A O 661 C CB . TYR A 86 ? 0.4095 0.3875 0.3574 0.0398 0.0484 -0.1342 127 TYR A CB 662 C CG . TYR A 86 ? 0.4353 0.4059 0.3673 0.0419 0.0462 -0.1423 127 TYR A CG 663 C CD1 . TYR A 86 ? 0.4608 0.4299 0.3825 0.0462 0.0529 -0.1479 127 TYR A CD1 664 C CD2 . TYR A 86 ? 0.4490 0.4142 0.3768 0.0398 0.0374 -0.1447 127 TYR A CD2 665 C CE1 . TYR A 86 ? 0.4981 0.4597 0.4037 0.0488 0.0505 -0.1559 127 TYR A CE1 666 C CE2 . TYR A 86 ? 0.4893 0.4474 0.4024 0.0421 0.0343 -0.1528 127 TYR A CE2 667 C CZ . TYR A 86 ? 0.5223 0.4784 0.4236 0.0467 0.0408 -0.1584 127 TYR A CZ 668 O OH . TYR A 86 ? 0.5602 0.5086 0.4454 0.0493 0.0373 -0.1667 127 TYR A OH 669 N N . ILE A 87 ? 0.3995 0.3888 0.3304 0.0400 0.0627 -0.1259 128 ILE A N 670 C CA . ILE A 87 ? 0.4108 0.4013 0.3270 0.0414 0.0699 -0.1256 128 ILE A CA 671 C C . ILE A 87 ? 0.4272 0.4147 0.3389 0.0463 0.0760 -0.1333 128 ILE A C 672 O O . ILE A 87 ? 0.4162 0.4045 0.3416 0.0482 0.0773 -0.1362 128 ILE A O 673 C CB . ILE A 87 ? 0.4011 0.4002 0.3256 0.0398 0.0765 -0.1181 128 ILE A CB 674 C CG1 . ILE A 87 ? 0.3880 0.3897 0.3171 0.0353 0.0704 -0.1108 128 ILE A CG1 675 C CG2 . ILE A 87 ? 0.4311 0.4312 0.3418 0.0414 0.0855 -0.1176 128 ILE A CG2 676 C CD1 . ILE A 87 ? 0.4004 0.4103 0.3440 0.0336 0.0740 -0.1044 128 ILE A CD1 677 N N . SER A 88 ? 0.4525 0.4362 0.3446 0.0486 0.0797 -0.1365 129 SER A N 678 C CA . SER A 88 ? 0.4752 0.4560 0.3600 0.0537 0.0870 -0.1437 129 SER A CA 679 C C . SER A 88 ? 0.4873 0.4713 0.3612 0.0554 0.0982 -0.1412 129 SER A C 680 O O . SER A 88 ? 0.4858 0.4711 0.3504 0.0531 0.0992 -0.1351 129 SER A O 681 C CB . SER A 88 ? 0.4872 0.4579 0.3551 0.0563 0.0811 -0.1521 129 SER A CB 682 O OG . SER A 88 ? 0.5464 0.5134 0.4248 0.0548 0.0712 -0.1550 129 SER A OG 683 N N . ILE A 89 ? 0.4947 0.4792 0.3693 0.0598 0.1071 -0.1461 130 ILE A N 684 C CA . ILE A 89 ? 0.5163 0.5002 0.3740 0.0628 0.1177 -0.1466 130 ILE A CA 685 C C . ILE A 89 ? 0.5479 0.5213 0.3857 0.0672 0.1146 -0.1560 130 ILE A C 686 O O . ILE A 89 ? 0.5291 0.4988 0.3733 0.0696 0.1109 -0.1634 130 ILE A O 687 C CB . ILE A 89 ? 0.5039 0.4950 0.3742 0.0652 0.1301 -0.1464 130 ILE A CB 688 C CG1 . ILE A 89 ? 0.4912 0.4926 0.3813 0.0608 0.1324 -0.1374 130 ILE A CG1 689 C CG2 . ILE A 89 ? 0.5372 0.5255 0.3869 0.0691 0.1416 -0.1484 130 ILE A CG2 690 C CD1 . ILE A 89 ? 0.5108 0.5204 0.4193 0.0631 0.1428 -0.1381 130 ILE A CD1 691 N N . ILE A 90 ? 0.5899 0.5580 0.4036 0.0681 0.1152 -0.1554 131 ILE A N 692 C CA A ILE A 90 ? 0.6335 0.5909 0.4250 0.0723 0.1112 -0.1641 131 ILE A CA 693 C CA B ILE A 90 ? 0.6334 0.5909 0.4247 0.0724 0.1114 -0.1642 131 ILE A CA 694 C C . ILE A 90 ? 0.6705 0.6253 0.4414 0.0774 0.1235 -0.1660 131 ILE A C 695 O O . ILE A 90 ? 0.6744 0.6332 0.4400 0.0762 0.1320 -0.1585 131 ILE A O 696 C CB A ILE A 90 ? 0.6345 0.5865 0.4144 0.0695 0.0985 -0.1627 131 ILE A CB 697 C CB B ILE A 90 ? 0.6389 0.5902 0.4163 0.0700 0.0990 -0.1633 131 ILE A CB 698 C CG1 A ILE A 90 ? 0.6560 0.5974 0.4209 0.0730 0.0898 -0.1731 131 ILE A CG1 699 C CG1 B ILE A 90 ? 0.6385 0.5936 0.4101 0.0665 0.1009 -0.1531 131 ILE A CG1 700 C CG2 A ILE A 90 ? 0.6495 0.6021 0.4133 0.0681 0.1020 -0.1548 131 ILE A CG2 701 C CG2 B ILE A 90 ? 0.6206 0.5718 0.4155 0.0665 0.0866 -0.1648 131 ILE A CG2 702 C CD1 A ILE A 90 ? 0.6401 0.5773 0.3990 0.0699 0.0761 -0.1722 131 ILE A CD1 703 C CD1 B ILE A 90 ? 0.6701 0.6173 0.4186 0.0668 0.0925 -0.1536 131 ILE A CD1 704 N N . ASN A 91 ? 0.7109 0.6587 0.4705 0.0830 0.1251 -0.1760 132 ASN A N 705 C CA . ASN A 91 ? 0.7667 0.7105 0.5033 0.0885 0.1369 -0.1783 132 ASN A CA 706 C C . ASN A 91 ? 0.8091 0.7432 0.5148 0.0902 0.1315 -0.1792 132 ASN A C 707 O O . ASN A 91 ? 0.8060 0.7368 0.5098 0.0871 0.1182 -0.1787 132 ASN A O 708 C CB . ASN A 91 ? 0.7850 0.7265 0.5224 0.0946 0.1438 -0.1881 132 ASN A CB 709 C CG . ASN A 91 ? 0.7898 0.7214 0.5209 0.0975 0.1322 -0.1993 132 ASN A CG 710 O OD1 . ASN A 91 ? 0.8123 0.7369 0.5302 0.0964 0.1204 -0.2011 132 ASN A OD1 711 N ND2 . ASN A 91 ? 0.7675 0.6987 0.5096 0.1012 0.1352 -0.2070 132 ASN A ND2 712 N N . GLU A 92 ? 0.8627 0.7922 0.5443 0.0952 0.1419 -0.1803 133 GLU A N 713 C CA . GLU A 92 ? 0.9099 0.8295 0.5597 0.0976 0.1375 -0.1807 133 GLU A CA 714 C C . GLU A 92 ? 0.9313 0.8401 0.5678 0.1006 0.1235 -0.1917 133 GLU A C 715 O O . GLU A 92 ? 0.9502 0.8516 0.5661 0.1012 0.1146 -0.1919 133 GLU A O 716 C CB . GLU A 92 ? 0.9347 0.8509 0.5610 0.1029 0.1529 -0.1797 133 GLU A CB 717 C CG . GLU A 92 ? 0.9734 0.8883 0.5995 0.1089 0.1625 -0.1887 133 GLU A CG 718 C CD . GLU A 92 ? 1.0229 0.9348 0.6259 0.1143 0.1790 -0.1873 133 GLU A CD 719 O OE1 . GLU A 92 ? 1.0265 0.9428 0.6274 0.1117 0.1880 -0.1767 133 GLU A OE1 720 O OE2 . GLU A 92 ? 1.0518 0.9567 0.6390 0.1212 0.1833 -0.1968 133 GLU A OE2 721 N N . ASP A 93 ? 0.9355 0.8435 0.5850 0.1026 0.1211 -0.2007 134 ASP A N 722 C CA . ASP A 93 ? 0.9540 0.8525 0.5960 0.1050 0.1074 -0.2117 134 ASP A CA 723 C C . ASP A 93 ? 0.9293 0.8302 0.5914 0.0986 0.0923 -0.2099 134 ASP A C 724 O O . ASP A 93 ? 0.9458 0.8393 0.6040 0.0993 0.0794 -0.2178 134 ASP A O 725 C CB . ASP A 93 ? 0.9649 0.8605 0.6123 0.1100 0.1114 -0.2224 134 ASP A CB 726 C CG . ASP A 93 ? 1.0072 0.8991 0.6323 0.1172 0.1260 -0.2257 134 ASP A CG 727 O OD1 . ASP A 93 ? 1.0442 0.9304 0.6411 0.1198 0.1285 -0.2236 134 ASP A OD1 728 O OD2 . ASP A 93 ? 1.0087 0.9031 0.6443 0.1204 0.1351 -0.2303 134 ASP A OD2 729 N N . GLY A 94 ? 0.8902 0.8014 0.5742 0.0925 0.0941 -0.1997 135 GLY A N 730 C CA . GLY A 94 ? 0.8586 0.7730 0.5624 0.0865 0.0816 -0.1969 135 GLY A CA 731 C C . GLY A 94 ? 0.8264 0.7438 0.5571 0.0849 0.0791 -0.2007 135 GLY A C 732 O O . GLY A 94 ? 0.8265 0.7440 0.5717 0.0809 0.0679 -0.2009 135 GLY A O 733 N N . ASN A 95 ? 0.8045 0.7244 0.5425 0.0882 0.0896 -0.2036 136 ASN A N 734 C CA . ASN A 95 ? 0.7659 0.6893 0.5305 0.0870 0.0882 -0.2060 136 ASN A CA 735 C C . ASN A 95 ? 0.7136 0.6486 0.5014 0.0820 0.0927 -0.1952 136 ASN A C 736 O O . ASN A 95 ? 0.7015 0.6430 0.4880 0.0820 0.1036 -0.1889 136 ASN A O 737 C CB . ASN A 95 ? 0.7789 0.6994 0.5422 0.0932 0.0965 -0.2146 136 ASN A CB 738 C CG . ASN A 95 ? 0.8482 0.7564 0.5883 0.0987 0.0917 -0.2263 136 ASN A CG 739 O OD1 . ASN A 95 ? 0.8931 0.7946 0.6284 0.0973 0.0787 -0.2305 136 ASN A OD1 740 N ND2 . ASN A 95 ? 0.8665 0.7718 0.5926 0.1051 0.1023 -0.2319 136 ASN A ND2 741 N N . GLU A 96 ? 0.6720 0.6094 0.4810 0.0776 0.0842 -0.1932 137 GLU A N 742 C CA . GLU A 96 ? 0.6286 0.5762 0.4598 0.0732 0.0871 -0.1837 137 GLU A CA 743 C C . GLU A 96 ? 0.6137 0.5651 0.4613 0.0762 0.0949 -0.1864 137 GLU A C 744 O O . GLU A 96 ? 0.6236 0.5714 0.4829 0.0773 0.0900 -0.1921 137 GLU A O 745 C CB . GLU A 96 ? 0.6035 0.5514 0.4486 0.0679 0.0751 -0.1803 137 GLU A CB 746 C CG . GLU A 96 ? 0.6061 0.5507 0.4354 0.0653 0.0674 -0.1780 137 GLU A CG 747 C CD . GLU A 96 ? 0.6057 0.5516 0.4484 0.0598 0.0568 -0.1737 137 GLU A CD 748 O OE1 . GLU A 96 ? 0.5988 0.5450 0.4602 0.0584 0.0531 -0.1746 137 GLU A OE1 749 O OE2 . GLU A 96 ? 0.6183 0.5645 0.4520 0.0572 0.0524 -0.1692 137 GLU A OE2 750 N N . ILE A 97 ? 0.6014 0.5597 0.4499 0.0777 0.1070 -0.1826 138 ILE A N 751 C CA . ILE A 97 ? 0.5919 0.5543 0.4549 0.0814 0.1157 -0.1857 138 ILE A CA 752 C C . ILE A 97 ? 0.5619 0.5336 0.4522 0.0783 0.1160 -0.1792 138 ILE A C 753 O O . ILE A 97 ? 0.5611 0.5357 0.4666 0.0812 0.1204 -0.1821 138 ILE A O 754 C CB . ILE A 97 ? 0.6146 0.5791 0.4648 0.0858 0.1298 -0.1869 138 ILE A CB 755 C CG1 . ILE A 97 ? 0.6066 0.5792 0.4563 0.0822 0.1366 -0.1765 138 ILE A CG1 756 C CG2 . ILE A 97 ? 0.6443 0.5979 0.4668 0.0904 0.1293 -0.1953 138 ILE A CG2 757 C CD1 . ILE A 97 ? 0.6480 0.6245 0.4911 0.0860 0.1525 -0.1763 138 ILE A CD1 758 N N . PHE A 98 ? 0.5342 0.5102 0.4306 0.0728 0.1109 -0.1707 139 PHE A N 759 C CA . PHE A 98 ? 0.5018 0.4852 0.4223 0.0700 0.1091 -0.1650 139 PHE A CA 760 C C . PHE A 98 ? 0.4754 0.4575 0.3972 0.0646 0.0984 -0.1595 139 PHE A C 761 O O . PHE A 98 ? 0.4687 0.4494 0.3756 0.0623 0.0964 -0.1566 139 PHE A O 762 C CB . PHE A 98 ? 0.5019 0.4958 0.4311 0.0692 0.1190 -0.1583 139 PHE A CB 763 C CG . PHE A 98 ? 0.5011 0.5023 0.4506 0.0651 0.1149 -0.1507 139 PHE A CG 764 C CD1 . PHE A 98 ? 0.4985 0.5027 0.4689 0.0665 0.1136 -0.1516 139 PHE A CD1 765 C CD2 . PHE A 98 ? 0.4953 0.4995 0.4421 0.0601 0.1120 -0.1427 139 PHE A CD2 766 C CE1 . PHE A 98 ? 0.4988 0.5089 0.4861 0.0631 0.1091 -0.1445 139 PHE A CE1 767 C CE2 . PHE A 98 ? 0.4857 0.4960 0.4498 0.0567 0.1078 -0.1360 139 PHE A CE2 768 C CZ . PHE A 98 ? 0.4750 0.4881 0.4587 0.0582 0.1064 -0.1370 139 PHE A CZ 769 N N . ASN A 99 ? 0.4565 0.4387 0.3955 0.0630 0.0916 -0.1584 140 ASN A N 770 C CA . ASN A 99 ? 0.4517 0.4336 0.3947 0.0579 0.0822 -0.1528 140 ASN A CA 771 C C . ASN A 99 ? 0.4369 0.4259 0.3998 0.0557 0.0817 -0.1458 140 ASN A C 772 O O . ASN A 99 ? 0.4337 0.4242 0.4112 0.0582 0.0834 -0.1476 140 ASN A O 773 C CB . ASN A 99 ? 0.4642 0.4372 0.4079 0.0579 0.0730 -0.1583 140 ASN A CB 774 C CG . ASN A 99 ? 0.5092 0.4740 0.4326 0.0596 0.0704 -0.1655 140 ASN A CG 775 O OD1 . ASN A 99 ? 0.5138 0.4790 0.4208 0.0591 0.0724 -0.1641 140 ASN A OD1 776 N ND2 . ASN A 99 ? 0.5530 0.5098 0.4776 0.0617 0.0656 -0.1735 140 ASN A ND2 777 N N . THR A 100 ? 0.4136 0.4065 0.3770 0.0513 0.0787 -0.1381 141 THR A N 778 C CA . THR A 100 ? 0.4031 0.4017 0.3838 0.0492 0.0766 -0.1315 141 THR A CA 779 C C . THR A 100 ? 0.4016 0.3947 0.3913 0.0485 0.0683 -0.1325 141 THR A C 780 O O . THR A 100 ? 0.4179 0.4034 0.4002 0.0485 0.0634 -0.1373 141 THR A O 781 C CB . THR A 100 ? 0.3885 0.3925 0.3669 0.0449 0.0757 -0.1233 141 THR A CB 782 O OG1 . THR A 100 ? 0.3965 0.3953 0.3644 0.0420 0.0686 -0.1226 141 THR A OG1 783 C CG2 . THR A 100 ? 0.4073 0.4161 0.3776 0.0454 0.0845 -0.1219 141 THR A CG2 784 N N . SER A 101 ? 0.3880 0.3848 0.3936 0.0482 0.0668 -0.1280 142 SER A N 785 C CA . SER A 101 ? 0.3934 0.3849 0.4090 0.0482 0.0604 -0.1282 142 SER A CA 786 C C . SER A 101 ? 0.3919 0.3792 0.4031 0.0440 0.0529 -0.1252 142 SER A C 787 O O . SER A 101 ? 0.3998 0.3906 0.4049 0.0407 0.0520 -0.1203 142 SER A O 788 C CB . SER A 101 ? 0.4013 0.3981 0.4328 0.0489 0.0607 -0.1229 142 SER A CB 789 O OG A SER A 101 ? 0.3533 0.3542 0.3851 0.0450 0.0578 -0.1154 142 SER A OG 790 O OG B SER A 101 ? 0.4076 0.3988 0.4488 0.0500 0.0558 -0.1232 142 SER A OG 791 N N . LEU A 102 ? 0.4011 0.3811 0.4169 0.0440 0.0477 -0.1278 143 LEU A N 792 C CA . LEU A 102 ? 0.4070 0.3833 0.4216 0.0400 0.0409 -0.1249 143 LEU A CA 793 C C . LEU A 102 ? 0.3958 0.3736 0.4221 0.0382 0.0382 -0.1173 143 LEU A C 794 O O . LEU A 102 ? 0.4052 0.3816 0.4314 0.0347 0.0336 -0.1134 143 LEU A O 795 C CB . LEU A 102 ? 0.4305 0.3976 0.4430 0.0402 0.0365 -0.1318 143 LEU A CB 796 C CG . LEU A 102 ? 0.4686 0.4328 0.4672 0.0422 0.0381 -0.1400 143 LEU A CG 797 C CD1 . LEU A 102 ? 0.5352 0.4898 0.5336 0.0424 0.0326 -0.1472 143 LEU A CD1 798 C CD2 . LEU A 102 ? 0.4910 0.4589 0.4754 0.0399 0.0382 -0.1378 143 LEU A CD2 799 N N . PHE A 103 ? 0.3868 0.3677 0.4230 0.0410 0.0409 -0.1152 144 PHE A N 800 C CA . PHE A 103 ? 0.3820 0.3639 0.4278 0.0402 0.0383 -0.1081 144 PHE A CA 801 C C . PHE A 103 ? 0.3704 0.3576 0.4248 0.0436 0.0417 -0.1065 144 PHE A C 802 O O . PHE A 103 ? 0.3813 0.3698 0.4372 0.0470 0.0459 -0.1117 144 PHE A O 803 C CB . PHE A 103 ? 0.3893 0.3623 0.4414 0.0399 0.0338 -0.1084 144 PHE A CB 804 C CG . PHE A 103 ? 0.4340 0.4017 0.4918 0.0440 0.0350 -0.1145 144 PHE A CG 805 C CD1 . PHE A 103 ? 0.4381 0.4060 0.5062 0.0476 0.0360 -0.1126 144 PHE A CD1 806 C CD2 . PHE A 103 ? 0.4956 0.4574 0.5483 0.0445 0.0346 -0.1224 144 PHE A CD2 807 C CE1 . PHE A 103 ? 0.4758 0.4388 0.5499 0.0517 0.0371 -0.1182 144 PHE A CE1 808 C CE2 . PHE A 103 ? 0.5303 0.4868 0.5885 0.0485 0.0357 -0.1283 144 PHE A CE2 809 C CZ . PHE A 103 ? 0.5196 0.4768 0.5888 0.0521 0.0371 -0.1261 144 PHE A CZ 810 N N . GLU A 104 ? 0.3420 0.3326 0.4024 0.0432 0.0400 -0.0997 145 GLU A N 811 C CA . GLU A 104 ? 0.3435 0.3386 0.4141 0.0468 0.0417 -0.0982 145 GLU A CA 812 C C . GLU A 104 ? 0.3495 0.3376 0.4288 0.0503 0.0394 -0.0996 145 GLU A C 813 O O . GLU A 104 ? 0.3583 0.3394 0.4379 0.0490 0.0355 -0.0970 145 GLU A O 814 C CB . GLU A 104 ? 0.3417 0.3414 0.4150 0.0455 0.0392 -0.0907 145 GLU A CB 815 C CG . GLU A 104 ? 0.3368 0.3437 0.4041 0.0424 0.0411 -0.0883 145 GLU A CG 816 C CD . GLU A 104 ? 0.3184 0.3284 0.3885 0.0415 0.0377 -0.0812 145 GLU A CD 817 O OE1 . GLU A 104 ? 0.3189 0.3248 0.3850 0.0392 0.0341 -0.0774 145 GLU A OE1 818 O OE2 . GLU A 104 ? 0.3163 0.3325 0.3935 0.0433 0.0387 -0.0799 145 GLU A OE2 819 N N . PRO A 105 ? 0.3568 0.3467 0.4439 0.0548 0.0422 -0.1033 146 PRO A N 820 C CA . PRO A 105 ? 0.3636 0.3466 0.4597 0.0586 0.0397 -0.1038 146 PRO A CA 821 C C . PRO A 105 ? 0.3634 0.3443 0.4631 0.0584 0.0349 -0.0960 146 PRO A C 822 O O . PRO A 105 ? 0.3694 0.3572 0.4712 0.0585 0.0344 -0.0918 146 PRO A O 823 C CB . PRO A 105 ? 0.3808 0.3693 0.4858 0.0634 0.0435 -0.1078 146 PRO A CB 824 C CG . PRO A 105 ? 0.3798 0.3753 0.4777 0.0618 0.0494 -0.1117 146 PRO A CG 825 C CD . PRO A 105 ? 0.3743 0.3727 0.4636 0.0566 0.0478 -0.1063 146 PRO A CD 826 N N . PRO A 106 ? 0.3618 0.3333 0.4614 0.0577 0.0314 -0.0939 147 PRO A N 827 C CA . PRO A 106 ? 0.3689 0.3386 0.4693 0.0573 0.0277 -0.0860 147 PRO A CA 828 C C . PRO A 106 ? 0.3716 0.3416 0.4807 0.0627 0.0260 -0.0837 147 PRO A C 829 O O . PRO A 106 ? 0.3951 0.3633 0.5112 0.0668 0.0270 -0.0883 147 PRO A O 830 C CB . PRO A 106 ? 0.3801 0.3391 0.4788 0.0552 0.0255 -0.0844 147 PRO A CB 831 C CG . PRO A 106 ? 0.3924 0.3467 0.4927 0.0560 0.0270 -0.0921 147 PRO A CG 832 C CD . PRO A 106 ? 0.3888 0.3515 0.4861 0.0563 0.0308 -0.0980 147 PRO A CD 833 N N . PRO A 107 ? 0.3750 0.3471 0.4834 0.0629 0.0231 -0.0770 148 PRO A N 834 C CA . PRO A 107 ? 0.3758 0.3483 0.4918 0.0684 0.0205 -0.0750 148 PRO A CA 835 C C . PRO A 107 ? 0.3746 0.3359 0.4946 0.0721 0.0180 -0.0736 148 PRO A C 836 O O . PRO A 107 ? 0.3743 0.3269 0.4903 0.0698 0.0178 -0.0719 148 PRO A O 837 C CB . PRO A 107 ? 0.3630 0.3390 0.4747 0.0674 0.0175 -0.0683 148 PRO A CB 838 C CG . PRO A 107 ? 0.3756 0.3491 0.4779 0.0620 0.0181 -0.0653 148 PRO A CG 839 C CD . PRO A 107 ? 0.3850 0.3588 0.4853 0.0587 0.0219 -0.0714 148 PRO A CD 840 N N . PRO A 108 ? 0.3719 0.3331 0.5002 0.0780 0.0159 -0.0739 149 PRO A N 841 C CA . PRO A 108 ? 0.3817 0.3318 0.5141 0.0823 0.0134 -0.0724 149 PRO A CA 842 C C . PRO A 108 ? 0.3852 0.3252 0.5103 0.0808 0.0109 -0.0647 149 PRO A C 843 O O . PRO A 108 ? 0.3816 0.3234 0.5013 0.0805 0.0086 -0.0587 149 PRO A O 844 C CB . PRO A 108 ? 0.3888 0.3427 0.5297 0.0888 0.0102 -0.0722 149 PRO A CB 845 C CG . PRO A 108 ? 0.3723 0.3402 0.5172 0.0876 0.0130 -0.0768 149 PRO A CG 846 C CD . PRO A 108 ? 0.3759 0.3478 0.5111 0.0810 0.0155 -0.0756 149 PRO A CD 847 N N . GLY A 109 ? 0.4049 0.3342 0.5301 0.0798 0.0118 -0.0650 150 GLY A N 848 C CA . GLY A 109 ? 0.4235 0.3425 0.5434 0.0785 0.0104 -0.0575 150 GLY A CA 849 C C . GLY A 109 ? 0.4463 0.3662 0.5591 0.0715 0.0127 -0.0559 150 GLY A C 850 O O . GLY A 109 ? 0.4651 0.3765 0.5748 0.0696 0.0126 -0.0503 150 GLY A O 851 N N . TYR A 110 ? 0.4492 0.3789 0.5600 0.0679 0.0147 -0.0607 151 TYR A N 852 C CA . TYR A 110 ? 0.4699 0.4018 0.5745 0.0614 0.0164 -0.0602 151 TYR A CA 853 C C . TYR A 110 ? 0.5017 0.4343 0.6077 0.0585 0.0186 -0.0682 151 TYR A C 854 O O . TYR A 110 ? 0.5131 0.4491 0.6141 0.0535 0.0196 -0.0694 151 TYR A O 855 C CB . TYR A 110 ? 0.4453 0.3884 0.5446 0.0596 0.0166 -0.0591 151 TYR A CB 856 C CG . TYR A 110 ? 0.4097 0.3538 0.5055 0.0617 0.0141 -0.0519 151 TYR A CG 857 C CD1 . TYR A 110 ? 0.3755 0.3177 0.4644 0.0586 0.0140 -0.0457 151 TYR A CD1 858 C CD2 . TYR A 110 ? 0.3469 0.2946 0.4463 0.0669 0.0118 -0.0517 151 TYR A CD2 859 C CE1 . TYR A 110 ? 0.3559 0.2988 0.4400 0.0609 0.0117 -0.0395 151 TYR A CE1 860 C CE2 . TYR A 110 ? 0.3382 0.2867 0.4337 0.0692 0.0088 -0.0459 151 TYR A CE2 861 C CZ . TYR A 110 ? 0.3430 0.2890 0.4300 0.0662 0.0088 -0.0398 151 TYR A CZ 862 O OH . TYR A 110 ? 0.3308 0.2770 0.4128 0.0690 0.0058 -0.0345 151 TYR A OH 863 N N . GLU A 111 ? 0.5339 0.4637 0.6461 0.0619 0.0191 -0.0741 152 GLU A N 864 C CA . GLU A 111 ? 0.5673 0.4967 0.6797 0.0599 0.0210 -0.0824 152 GLU A CA 865 C C . GLU A 111 ? 0.5929 0.5134 0.7047 0.0555 0.0202 -0.0823 152 GLU A C 866 O O . GLU A 111 ? 0.6115 0.5319 0.7217 0.0530 0.0209 -0.0890 152 GLU A O 867 C CB . GLU A 111 ? 0.5742 0.5026 0.6935 0.0651 0.0220 -0.0891 152 GLU A CB 868 C CG . GLU A 111 ? 0.5741 0.5104 0.6975 0.0701 0.0222 -0.0883 152 GLU A CG 869 C CD . GLU A 111 ? 0.5948 0.5249 0.7241 0.0752 0.0190 -0.0829 152 GLU A CD 870 O OE1 . GLU A 111 ? 0.5776 0.4990 0.7051 0.0742 0.0169 -0.0768 152 GLU A OE1 871 O OE2 . GLU A 111 ? 0.5956 0.5297 0.7315 0.0804 0.0186 -0.0846 152 GLU A OE2 872 N N . ASN A 112 ? 0.6121 0.5253 0.7250 0.0547 0.0189 -0.0749 153 ASN A N 873 C CA . ASN A 112 ? 0.6251 0.5302 0.7396 0.0501 0.0185 -0.0740 153 ASN A CA 874 C C . ASN A 112 ? 0.6228 0.5307 0.7324 0.0454 0.0186 -0.0674 153 ASN A C 875 O O . ASN A 112 ? 0.6347 0.5367 0.7468 0.0415 0.0186 -0.0655 153 ASN A O 876 C CB . ASN A 112 ? 0.6441 0.5363 0.7659 0.0525 0.0178 -0.0712 153 ASN A CB 877 C CG . ASN A 112 ? 0.6666 0.5501 0.7929 0.0478 0.0176 -0.0727 153 ASN A CG 878 O OD1 . ASN A 112 ? 0.6870 0.5706 0.8148 0.0457 0.0170 -0.0809 153 ASN A OD1 879 N ND2 . ASN A 112 ? 0.6911 0.5670 0.8199 0.0462 0.0180 -0.0647 153 ASN A ND2 880 N N . VAL A 113 ? 0.6078 0.5248 0.7113 0.0457 0.0189 -0.0642 154 VAL A N 881 C CA . VAL A 113 ? 0.5918 0.5127 0.6902 0.0415 0.0192 -0.0592 154 VAL A CA 882 C C . VAL A 113 ? 0.5919 0.5168 0.6884 0.0367 0.0191 -0.0652 154 VAL A C 883 O O . VAL A 113 ? 0.6016 0.5316 0.6960 0.0373 0.0193 -0.0722 154 VAL A O 884 C CB . VAL A 113 ? 0.5849 0.5139 0.6773 0.0433 0.0190 -0.0545 154 VAL A CB 885 C CG1 . VAL A 113 ? 0.5559 0.4887 0.6428 0.0389 0.0195 -0.0498 154 VAL A CG1 886 C CG2 . VAL A 113 ? 0.6057 0.5294 0.6992 0.0484 0.0181 -0.0486 154 VAL A CG2 887 N N . SER A 114 ? 0.5820 0.5043 0.6796 0.0322 0.0189 -0.0625 155 SER A N 888 C CA . SER A 114 ? 0.5697 0.4955 0.6657 0.0277 0.0180 -0.0676 155 SER A CA 889 C C . SER A 114 ? 0.5435 0.4785 0.6324 0.0255 0.0182 -0.0641 155 SER A C 890 O O . SER A 114 ? 0.5350 0.4723 0.6210 0.0268 0.0192 -0.0571 155 SER A O 891 C CB . SER A 114 ? 0.5892 0.5072 0.6928 0.0238 0.0172 -0.0675 155 SER A CB 892 O OG A SER A 114 ? 0.5845 0.5008 0.6895 0.0220 0.0186 -0.0588 155 SER A OG 893 O OG B SER A 114 ? 0.5933 0.5101 0.6985 0.0221 0.0151 -0.0765 155 SER A OG 894 N N . ASP A 115 ? 0.5037 0.4433 0.5892 0.0224 0.0170 -0.0691 156 ASP A N 895 C CA . ASP A 115 ? 0.4636 0.4111 0.5429 0.0200 0.0168 -0.0664 156 ASP A CA 896 C C . ASP A 115 ? 0.4084 0.3632 0.4812 0.0228 0.0181 -0.0645 156 ASP A C 897 O O . ASP A 115 ? 0.3937 0.3532 0.4628 0.0219 0.0184 -0.0593 156 ASP A O 898 C CB . ASP A 115 ? 0.4869 0.4326 0.5693 0.0174 0.0173 -0.0589 156 ASP A CB 899 C CG . ASP A 115 ? 0.5524 0.4918 0.6431 0.0138 0.0163 -0.0603 156 ASP A CG 900 O OD1 . ASP A 115 ? 0.6340 0.5721 0.7264 0.0124 0.0140 -0.0678 156 ASP A OD1 901 O OD2 . ASP A 115 ? 0.6340 0.5695 0.7297 0.0126 0.0178 -0.0539 156 ASP A OD2 902 N N . ILE A 116 ? 0.3532 0.3091 0.4254 0.0262 0.0190 -0.0688 157 ILE A N 903 C CA . ILE A 116 ? 0.3114 0.2756 0.3783 0.0279 0.0202 -0.0684 157 ILE A CA 904 C C . ILE A 116 ? 0.3045 0.2737 0.3648 0.0254 0.0202 -0.0733 157 ILE A C 905 O O . ILE A 116 ? 0.2999 0.2668 0.3594 0.0255 0.0201 -0.0801 157 ILE A O 906 C CB . ILE A 116 ? 0.2935 0.2578 0.3637 0.0326 0.0216 -0.0712 157 ILE A CB 907 C CG1 . ILE A 116 ? 0.3058 0.2649 0.3815 0.0357 0.0209 -0.0660 157 ILE A CG1 908 C CG2 . ILE A 116 ? 0.2906 0.2641 0.3567 0.0337 0.0233 -0.0722 157 ILE A CG2 909 C CD1 . ILE A 116 ? 0.3102 0.2680 0.3911 0.0408 0.0216 -0.0690 157 ILE A CD1 910 N N . VAL A 117 ? 0.2879 0.2631 0.3427 0.0233 0.0200 -0.0700 158 VAL A N 911 C CA . VAL A 117 ? 0.2867 0.2661 0.3342 0.0211 0.0198 -0.0739 158 VAL A CA 912 C C . VAL A 117 ? 0.2901 0.2732 0.3341 0.0238 0.0227 -0.0782 158 VAL A C 913 O O . VAL A 117 ? 0.2801 0.2672 0.3261 0.0260 0.0246 -0.0758 158 VAL A O 914 C CB . VAL A 117 ? 0.2730 0.2575 0.3158 0.0184 0.0189 -0.0689 158 VAL A CB 915 C CG1 . VAL A 117 ? 0.2649 0.2558 0.3056 0.0201 0.0208 -0.0651 158 VAL A CG1 916 C CG2 . VAL A 117 ? 0.3084 0.2946 0.3444 0.0158 0.0175 -0.0726 158 VAL A CG2 917 N N . PRO A 118 ? 0.2919 0.2736 0.3314 0.0238 0.0230 -0.0850 159 PRO A N 918 C CA . PRO A 118 ? 0.3067 0.2923 0.3425 0.0264 0.0269 -0.0888 159 PRO A CA 919 C C . PRO A 118 ? 0.2926 0.2858 0.3222 0.0253 0.0288 -0.0856 159 PRO A C 920 O O . PRO A 118 ? 0.2953 0.2900 0.3208 0.0223 0.0266 -0.0821 159 PRO A O 921 C CB . PRO A 118 ? 0.3211 0.3027 0.3507 0.0264 0.0264 -0.0964 159 PRO A CB 922 C CG . PRO A 118 ? 0.3411 0.3194 0.3690 0.0228 0.0217 -0.0960 159 PRO A CG 923 C CD . PRO A 118 ? 0.3137 0.2905 0.3509 0.0216 0.0200 -0.0894 159 PRO A CD 924 N N . PRO A 119 ? 0.2884 0.2864 0.3178 0.0276 0.0331 -0.0867 160 PRO A N 925 C CA . PRO A 119 ? 0.2868 0.2915 0.3112 0.0262 0.0352 -0.0835 160 PRO A CA 926 C C . PRO A 119 ? 0.2757 0.2799 0.2883 0.0238 0.0345 -0.0850 160 PRO A C 927 O O . PRO A 119 ? 0.2907 0.2911 0.2974 0.0244 0.0346 -0.0907 160 PRO A O 928 C CB . PRO A 119 ? 0.2829 0.2918 0.3101 0.0292 0.0406 -0.0862 160 PRO A CB 929 C CG . PRO A 119 ? 0.3114 0.3168 0.3488 0.0324 0.0401 -0.0881 160 PRO A CG 930 C CD . PRO A 119 ? 0.2963 0.2938 0.3317 0.0314 0.0362 -0.0905 160 PRO A CD 931 N N . PHE A 120 ? 0.2758 0.2833 0.2851 0.0212 0.0331 -0.0800 161 PHE A N 932 C CA . PHE A 120 ? 0.2722 0.2796 0.2704 0.0190 0.0319 -0.0804 161 PHE A CA 933 C C . PHE A 120 ? 0.2601 0.2724 0.2571 0.0172 0.0322 -0.0745 161 PHE A C 934 O O . PHE A 120 ? 0.2523 0.2672 0.2573 0.0173 0.0318 -0.0703 161 PHE A O 935 C CB . PHE A 120 ? 0.2713 0.2734 0.2679 0.0172 0.0264 -0.0821 161 PHE A CB 936 C CG . PHE A 120 ? 0.2542 0.2567 0.2568 0.0150 0.0228 -0.0766 161 PHE A CG 937 C CD1 . PHE A 120 ? 0.2483 0.2514 0.2460 0.0124 0.0194 -0.0748 161 PHE A CD1 938 C CD2 . PHE A 120 ? 0.2774 0.2793 0.2903 0.0158 0.0227 -0.0735 161 PHE A CD2 939 C CE1 . PHE A 120 ? 0.2438 0.2473 0.2473 0.0105 0.0166 -0.0699 161 PHE A CE1 940 C CE2 . PHE A 120 ? 0.2537 0.2554 0.2708 0.0140 0.0200 -0.0683 161 PHE A CE2 941 C CZ . PHE A 120 ? 0.2626 0.2654 0.2753 0.0113 0.0173 -0.0665 161 PHE A CZ 942 N N . SER A 121 ? 0.2560 0.2692 0.2426 0.0158 0.0324 -0.0742 162 SER A N 943 C CA . SER A 121 ? 0.2542 0.2712 0.2390 0.0139 0.0321 -0.0687 162 SER A CA 944 C C . SER A 121 ? 0.2573 0.2721 0.2396 0.0117 0.0265 -0.0670 162 SER A C 945 O O . SER A 121 ? 0.2688 0.2809 0.2425 0.0111 0.0243 -0.0697 162 SER A O 946 C CB . SER A 121 ? 0.2789 0.2978 0.2538 0.0138 0.0363 -0.0688 162 SER A CB 947 O OG . SER A 121 ? 0.2697 0.2915 0.2488 0.0158 0.0423 -0.0702 162 SER A OG 948 N N . ALA A 122 ? 0.2545 0.2706 0.2442 0.0107 0.0241 -0.0627 163 ALA A N 949 C CA . ALA A 122 ? 0.2459 0.2601 0.2350 0.0087 0.0193 -0.0613 163 ALA A CA 950 C C . ALA A 122 ? 0.2602 0.2759 0.2401 0.0073 0.0181 -0.0597 163 ALA A C 951 O O . ALA A 122 ? 0.2465 0.2654 0.2241 0.0072 0.0204 -0.0564 163 ALA A O 952 C CB . ALA A 122 ? 0.2411 0.2564 0.2389 0.0084 0.0180 -0.0564 163 ALA A CB 953 N N . PHE A 123 ? 0.2499 0.2628 0.2257 0.0063 0.0139 -0.0621 164 PHE A N 954 C CA . PHE A 123 ? 0.2552 0.2681 0.2220 0.0053 0.0110 -0.0614 164 PHE A CA 955 C C . PHE A 123 ? 0.2769 0.2882 0.2312 0.0065 0.0131 -0.0644 164 PHE A C 956 O O . PHE A 123 ? 0.3046 0.3154 0.2498 0.0061 0.0111 -0.0634 164 PHE A O 957 C CB . PHE A 123 ? 0.2539 0.2703 0.2220 0.0041 0.0107 -0.0554 164 PHE A CB 958 C CG . PHE A 123 ? 0.2425 0.2599 0.2212 0.0032 0.0087 -0.0526 164 PHE A CG 959 C CD1 . PHE A 123 ? 0.2553 0.2715 0.2370 0.0020 0.0041 -0.0531 164 PHE A CD1 960 C CD2 . PHE A 123 ? 0.2419 0.2611 0.2276 0.0039 0.0114 -0.0495 164 PHE A CD2 961 C CE1 . PHE A 123 ? 0.2435 0.2605 0.2348 0.0012 0.0033 -0.0500 164 PHE A CE1 962 C CE2 . PHE A 123 ? 0.2407 0.2600 0.2341 0.0035 0.0100 -0.0466 164 PHE A CE2 963 C CZ . PHE A 123 ? 0.2385 0.2567 0.2347 0.0021 0.0064 -0.0465 164 PHE A CZ 964 N N . SER A 124 ? 0.2882 0.2983 0.2415 0.0083 0.0170 -0.0681 165 SER A N 965 C CA . SER A 124 ? 0.2983 0.3058 0.2380 0.0098 0.0190 -0.0717 165 SER A CA 966 C C . SER A 124 ? 0.3299 0.3332 0.2622 0.0098 0.0125 -0.0756 165 SER A C 967 O O . SER A 124 ? 0.3361 0.3375 0.2760 0.0091 0.0081 -0.0785 165 SER A O 968 C CB . SER A 124 ? 0.3101 0.3162 0.2506 0.0121 0.0234 -0.0765 165 SER A CB 969 O OG . SER A 124 ? 0.3233 0.3265 0.2492 0.0139 0.0257 -0.0799 165 SER A OG 970 N N . PRO A 125 ? 0.3409 0.3423 0.2587 0.0105 0.0118 -0.0757 166 PRO A N 971 C CA . PRO A 125 ? 0.3679 0.3645 0.2776 0.0113 0.0055 -0.0810 166 PRO A CA 972 C C . PRO A 125 ? 0.3788 0.3712 0.2843 0.0136 0.0067 -0.0883 166 PRO A C 973 O O . PRO A 125 ? 0.3647 0.3579 0.2710 0.0150 0.0135 -0.0890 166 PRO A O 974 C CB . PRO A 125 ? 0.3882 0.3833 0.2813 0.0123 0.0054 -0.0789 166 PRO A CB 975 C CG . PRO A 125 ? 0.3681 0.3655 0.2584 0.0128 0.0142 -0.0750 166 PRO A CG 976 C CD . PRO A 125 ? 0.3496 0.3522 0.2576 0.0109 0.0166 -0.0716 166 PRO A CD 977 N N . GLN A 126 ? 0.3909 0.3789 0.2926 0.0142 0.0000 -0.0940 167 GLN A N 978 C CA . GLN A 126 ? 0.4085 0.3913 0.3041 0.0167 0.0000 -0.1019 167 GLN A CA 979 C C . GLN A 126 ? 0.4330 0.4125 0.3080 0.0198 0.0032 -0.1037 167 GLN A C 980 O O . GLN A 126 ? 0.4500 0.4294 0.3139 0.0199 0.0020 -0.1002 167 GLN A O 981 C CB . GLN A 126 ? 0.4129 0.3920 0.3120 0.0161 -0.0092 -0.1076 167 GLN A CB 982 C CG . GLN A 126 ? 0.4428 0.4244 0.3628 0.0130 -0.0120 -0.1060 167 GLN A CG 983 C CD . GLN A 126 ? 0.5349 0.5126 0.4603 0.0122 -0.0205 -0.1122 167 GLN A CD 984 O OE1 . GLN A 126 ? 0.6030 0.5766 0.5167 0.0139 -0.0257 -0.1177 167 GLN A OE1 985 N NE2 . GLN A 126 ? 0.5464 0.5253 0.4898 0.0095 -0.0221 -0.1112 167 GLN A NE2 986 N N . GLY A 127 ? 0.4468 0.4233 0.3164 0.0226 0.0077 -0.1090 168 GLY A N 987 C CA . GLY A 127 ? 0.4725 0.4445 0.3209 0.0262 0.0105 -0.1119 168 GLY A CA 988 C C . GLY A 127 ? 0.4810 0.4510 0.3271 0.0291 0.0175 -0.1170 168 GLY A C 989 O O . GLY A 127 ? 0.4613 0.4343 0.3229 0.0284 0.0208 -0.1172 168 GLY A O 990 N N . MET A 128 ? 0.4987 0.4633 0.3246 0.0329 0.0196 -0.1212 169 MET A N 991 C CA . MET A 128 ? 0.5201 0.4827 0.3411 0.0364 0.0274 -0.1260 169 MET A CA 992 C C . MET A 128 ? 0.5252 0.4870 0.3280 0.0390 0.0364 -0.1232 169 MET A C 993 O O . MET A 128 ? 0.5548 0.5105 0.3398 0.0433 0.0387 -0.1291 169 MET A O 994 C CB . MET A 128 ? 0.5481 0.5033 0.3630 0.0392 0.0212 -0.1363 169 MET A CB 995 C CG . MET A 128 ? 0.5916 0.5472 0.4266 0.0367 0.0144 -0.1394 169 MET A CG 996 S SD . MET A 128 ? 0.7923 0.7388 0.6209 0.0402 0.0084 -0.1522 169 MET A SD 997 C CE . MET A 128 ? 0.7363 0.6832 0.5878 0.0358 -0.0020 -0.1533 169 MET A CE 998 N N . PRO A 129 ? 0.5157 0.4831 0.3222 0.0366 0.0419 -0.1144 170 PRO A N 999 C CA . PRO A 129 ? 0.5392 0.5059 0.3298 0.0386 0.0510 -0.1107 170 PRO A CA 1000 C C . PRO A 129 ? 0.5583 0.5251 0.3476 0.0418 0.0615 -0.1145 170 PRO A C 1001 O O . PRO A 129 ? 0.5332 0.5045 0.3408 0.0411 0.0640 -0.1161 170 PRO A O 1002 C CB . PRO A 129 ? 0.5235 0.4972 0.3258 0.0346 0.0544 -0.1010 170 PRO A CB 1003 C CG . PRO A 129 ? 0.5013 0.4806 0.3275 0.0316 0.0506 -0.1007 170 PRO A CG 1004 C CD . PRO A 129 ? 0.4872 0.4619 0.3140 0.0322 0.0406 -0.1076 170 PRO A CD 1005 N N . GLU A 130 ? 0.5862 0.5478 0.3537 0.0457 0.0675 -0.1161 171 GLU A N 1006 C CA A GLU A 130 ? 0.6074 0.5692 0.3721 0.0491 0.0788 -0.1193 171 GLU A CA 1007 C CA B GLU A 130 ? 0.6092 0.5705 0.3723 0.0494 0.0788 -0.1197 171 GLU A CA 1008 C C . GLU A 130 ? 0.6216 0.5845 0.3751 0.0495 0.0899 -0.1123 171 GLU A C 1009 O O . GLU A 130 ? 0.6472 0.6051 0.3817 0.0501 0.0882 -0.1090 171 GLU A O 1010 C CB A GLU A 130 ? 0.6305 0.5837 0.3782 0.0542 0.0763 -0.1294 171 GLU A CB 1011 C CB B GLU A 130 ? 0.6372 0.5890 0.3786 0.0548 0.0768 -0.1288 171 GLU A CB 1012 C CG A GLU A 130 ? 0.6619 0.6144 0.4041 0.0586 0.0884 -0.1336 171 GLU A CG 1013 C CG B GLU A 130 ? 0.6513 0.5990 0.3976 0.0554 0.0654 -0.1375 171 GLU A CG 1014 C CD A GLU A 130 ? 0.6969 0.6396 0.4187 0.0641 0.0856 -0.1437 171 GLU A CD 1015 C CD B GLU A 130 ? 0.6882 0.6256 0.4100 0.0607 0.0618 -0.1463 171 GLU A CD 1016 O OE1 A GLU A 130 ? 0.7160 0.6547 0.4401 0.0641 0.0739 -0.1500 171 GLU A OE1 1017 O OE1 B GLU A 130 ? 0.7165 0.6500 0.4187 0.0650 0.0707 -0.1473 171 GLU A OE1 1018 O OE2 A GLU A 130 ? 0.7175 0.6566 0.4213 0.0686 0.0952 -0.1454 171 GLU A OE2 1019 O OE2 B GLU A 130 ? 0.7002 0.6331 0.4224 0.0606 0.0499 -0.1525 171 GLU A OE2 1020 N N . GLY A 131 ? 0.6045 0.5740 0.3705 0.0491 0.1012 -0.1098 172 GLY A N 1021 C CA . GLY A 131 ? 0.6055 0.5764 0.3634 0.0490 0.1124 -0.1028 172 GLY A CA 1022 C C . GLY A 131 ? 0.5964 0.5748 0.3696 0.0490 0.1253 -0.1012 172 GLY A C 1023 O O . GLY A 131 ? 0.5951 0.5770 0.3829 0.0502 0.1263 -0.1065 172 GLY A O 1024 N N . ASP A 132 ? 0.5861 0.5669 0.3565 0.0477 0.1349 -0.0937 173 ASP A N 1025 C CA . ASP A 132 ? 0.5794 0.5680 0.3657 0.0471 0.1478 -0.0912 173 ASP A CA 1026 C C . ASP A 132 ? 0.5389 0.5366 0.3511 0.0417 0.1446 -0.0854 173 ASP A C 1027 O O . ASP A 132 ? 0.5213 0.5182 0.3326 0.0384 0.1374 -0.0801 173 ASP A O 1028 C CB . ASP A 132 ? 0.6120 0.5982 0.3823 0.0483 0.1605 -0.0859 173 ASP A CB 1029 C CG . ASP A 132 ? 0.6811 0.6581 0.4239 0.0544 0.1654 -0.0916 173 ASP A CG 1030 O OD1 . ASP A 132 ? 0.7402 0.7170 0.4851 0.0581 0.1670 -0.0999 173 ASP A OD1 1031 O OD2 . ASP A 132 ? 0.7289 0.6984 0.4475 0.0558 0.1676 -0.0879 173 ASP A OD2 1032 N N . LEU A 133 ? 0.5155 0.5214 0.3501 0.0413 0.1501 -0.0866 174 LEU A N 1033 C CA . LEU A 133 ? 0.4935 0.5080 0.3535 0.0369 0.1470 -0.0821 174 LEU A CA 1034 C C . LEU A 133 ? 0.4848 0.5042 0.3509 0.0338 0.1561 -0.0739 174 LEU A C 1035 O O . LEU A 133 ? 0.5095 0.5291 0.3698 0.0355 0.1685 -0.0728 174 LEU A O 1036 C CB . LEU A 133 ? 0.4807 0.5016 0.3622 0.0384 0.1484 -0.0873 174 LEU A CB 1037 C CG A LEU A 133 ? 0.4543 0.4803 0.3578 0.0364 0.1390 -0.0880 174 LEU A CG 1038 C CG B LEU A 133 ? 0.4627 0.4805 0.3464 0.0404 0.1384 -0.0945 174 LEU A CG 1039 C CD1 A LEU A 133 ? 0.4396 0.4604 0.3367 0.0346 0.1255 -0.0879 174 LEU A CD1 1040 C CD1 B LEU A 133 ? 0.4486 0.4727 0.3532 0.0423 0.1422 -0.0987 174 LEU A CD1 1041 C CD2 A LEU A 133 ? 0.4443 0.4723 0.3588 0.0400 0.1408 -0.0953 174 LEU A CD2 1042 C CD2 B LEU A 133 ? 0.4397 0.4565 0.3281 0.0369 0.1252 -0.0921 174 LEU A CD2 1043 N N . VAL A 134 ? 0.4705 0.4933 0.3481 0.0294 0.1499 -0.0682 175 VAL A N 1044 C CA . VAL A 134 ? 0.4534 0.4827 0.3452 0.0259 0.1572 -0.0613 175 VAL A CA 1045 C C . VAL A 134 ? 0.4349 0.4725 0.3535 0.0233 0.1512 -0.0611 175 VAL A C 1046 O O . VAL A 134 ? 0.4099 0.4462 0.3306 0.0222 0.1395 -0.0619 175 VAL A O 1047 C CB . VAL A 134 ? 0.4697 0.4943 0.3481 0.0231 0.1563 -0.0538 175 VAL A CB 1048 C CG1 . VAL A 134 ? 0.4539 0.4851 0.3496 0.0190 0.1626 -0.0470 175 VAL A CG1 1049 C CG2 . VAL A 134 ? 0.4841 0.5000 0.3346 0.0264 0.1634 -0.0536 175 VAL A CG2 1050 N N . TYR A 135 ? 0.4118 0.4577 0.3504 0.0224 0.1590 -0.0602 176 TYR A N 1051 C CA . TYR A 135 ? 0.3888 0.4427 0.3530 0.0204 0.1535 -0.0600 176 TYR A CA 1052 C C . TYR A 135 ? 0.3810 0.4379 0.3539 0.0157 0.1527 -0.0527 176 TYR A C 1053 O O . TYR A 135 ? 0.3867 0.4448 0.3594 0.0140 0.1622 -0.0483 176 TYR A O 1054 C CB . TYR A 135 ? 0.3914 0.4531 0.3746 0.0226 0.1609 -0.0641 176 TYR A CB 1055 C CG . TYR A 135 ? 0.3653 0.4358 0.3756 0.0205 0.1568 -0.0630 176 TYR A CG 1056 C CD1 . TYR A 135 ? 0.3450 0.4154 0.3624 0.0206 0.1446 -0.0650 176 TYR A CD1 1057 C CD2 . TYR A 135 ? 0.3830 0.4616 0.4119 0.0186 0.1649 -0.0601 176 TYR A CD2 1058 C CE1 . TYR A 135 ? 0.3326 0.4103 0.3732 0.0192 0.1400 -0.0640 176 TYR A CE1 1059 C CE2 . TYR A 135 ? 0.3597 0.4462 0.4135 0.0170 0.1599 -0.0597 176 TYR A CE2 1060 C CZ . TYR A 135 ? 0.3348 0.4206 0.3933 0.0175 0.1473 -0.0617 176 TYR A CZ 1061 O OH . TYR A 135 ? 0.3333 0.4261 0.4145 0.0165 0.1420 -0.0613 176 TYR A OH 1062 N N . VAL A 136 ? 0.3632 0.4209 0.3437 0.0136 0.1415 -0.0515 177 VAL A N 1063 C CA . VAL A 136 ? 0.3661 0.4243 0.3504 0.0094 0.1383 -0.0450 177 VAL A CA 1064 C C . VAL A 136 ? 0.3405 0.4064 0.3493 0.0074 0.1332 -0.0444 177 VAL A C 1065 O O . VAL A 136 ? 0.3346 0.4003 0.3467 0.0045 0.1271 -0.0405 177 VAL A O 1066 C CB . VAL A 136 ? 0.3664 0.4167 0.3322 0.0087 0.1292 -0.0431 177 VAL A CB 1067 C CG1 . VAL A 136 ? 0.4074 0.4500 0.3485 0.0107 0.1338 -0.0433 177 VAL A CG1 1068 C CG2 . VAL A 136 ? 0.3915 0.4410 0.3597 0.0101 0.1180 -0.0473 177 VAL A CG2 1069 N N . ASN A 137 ? 0.3318 0.4042 0.3574 0.0093 0.1361 -0.0485 178 ASN A N 1070 C CA . ASN A 137 ? 0.3211 0.4008 0.3703 0.0083 0.1311 -0.0487 178 ASN A CA 1071 C C . ASN A 137 ? 0.3140 0.3904 0.3604 0.0083 0.1180 -0.0491 178 ASN A C 1072 O O . ASN A 137 ? 0.3135 0.3855 0.3497 0.0108 0.1138 -0.0525 178 ASN A O 1073 C CB . ASN A 137 ? 0.3121 0.3965 0.3741 0.0043 0.1356 -0.0436 178 ASN A CB 1074 C CG . ASN A 137 ? 0.3230 0.4166 0.4120 0.0040 0.1337 -0.0452 178 ASN A CG 1075 O OD1 . ASN A 137 ? 0.3051 0.4023 0.4040 0.0072 0.1322 -0.0500 178 ASN A OD1 1076 N ND2 . ASN A 137 ? 0.3224 0.4193 0.4237 0.0003 0.1335 -0.0412 178 ASN A ND2 1077 N N . TYR A 138 ? 0.2807 0.3589 0.3356 0.0055 0.1121 -0.0456 179 TYR A N 1078 C CA . TYR A 138 ? 0.2723 0.3474 0.3243 0.0056 0.1005 -0.0455 179 TYR A CA 1079 C C . TYR A 138 ? 0.2728 0.3405 0.3053 0.0042 0.0969 -0.0425 179 TYR A C 1080 O O . TYR A 138 ? 0.2668 0.3319 0.2966 0.0039 0.0879 -0.0419 179 TYR A O 1081 C CB . TYR A 138 ? 0.2683 0.3483 0.3375 0.0039 0.0951 -0.0436 179 TYR A CB 1082 C CG . TYR A 138 ? 0.2661 0.3535 0.3560 0.0058 0.0956 -0.0470 179 TYR A CG 1083 C CD1 . TYR A 138 ? 0.2730 0.3603 0.3667 0.0092 0.0895 -0.0508 179 TYR A CD1 1084 C CD2 . TYR A 138 ? 0.2749 0.3691 0.3814 0.0042 0.1020 -0.0462 179 TYR A CD2 1085 C CE1 . TYR A 138 ? 0.2687 0.3627 0.3821 0.0114 0.0893 -0.0539 179 TYR A CE1 1086 C CE2 . TYR A 138 ? 0.2882 0.3898 0.4154 0.0062 0.1018 -0.0496 179 TYR A CE2 1087 C CZ . TYR A 138 ? 0.2759 0.3772 0.4059 0.0100 0.0950 -0.0534 179 TYR A CZ 1088 O OH . TYR A 138 ? 0.3035 0.4116 0.4535 0.0124 0.0939 -0.0567 179 TYR A OH 1089 N N . ALA A 139 ? 0.2865 0.3507 0.3053 0.0034 0.1038 -0.0405 180 ALA A N 1090 C CA . ALA A 139 ? 0.2946 0.3515 0.2942 0.0024 0.1006 -0.0376 180 ALA A CA 1091 C C . ALA A 139 ? 0.2961 0.3528 0.2996 -0.0006 0.0948 -0.0329 180 ALA A C 1092 O O . ALA A 139 ? 0.2934 0.3452 0.2858 -0.0010 0.0882 -0.0314 180 ALA A O 1093 C CB . ALA A 139 ? 0.3068 0.3586 0.2938 0.0049 0.0940 -0.0415 180 ALA A CB 1094 N N . ARG A 140 ? 0.2851 0.3474 0.3054 -0.0027 0.0971 -0.0310 181 ARG A N 1095 C CA . ARG A 140 ? 0.2763 0.3382 0.3011 -0.0055 0.0921 -0.0268 181 ARG A CA 1096 C C . ARG A 140 ? 0.2922 0.3494 0.3051 -0.0078 0.0970 -0.0217 181 ARG A C 1097 O O . ARG A 140 ? 0.3049 0.3602 0.3089 -0.0074 0.1056 -0.0209 181 ARG A O 1098 C CB . ARG A 140 ? 0.2719 0.3411 0.3192 -0.0068 0.0926 -0.0270 181 ARG A CB 1099 C CG . ARG A 140 ? 0.2803 0.3536 0.3396 -0.0043 0.0863 -0.0314 181 ARG A CG 1100 C CD . ARG A 140 ? 0.2821 0.3629 0.3635 -0.0050 0.0881 -0.0324 181 ARG A CD 1101 N NE . ARG A 140 ? 0.2908 0.3754 0.3778 -0.0054 0.0992 -0.0327 181 ARG A NE 1102 C CZ . ARG A 140 ? 0.3224 0.4144 0.4300 -0.0061 0.1031 -0.0337 181 ARG A CZ 1103 N NH1 . ARG A 140 ? 0.3210 0.4174 0.4452 -0.0063 0.0958 -0.0349 181 ARG A NH1 1104 N NH2 . ARG A 140 ? 0.3195 0.4148 0.4315 -0.0064 0.1142 -0.0339 181 ARG A NH2 1105 N N . THR A 141 ? 0.2774 0.3321 0.2897 -0.0099 0.0918 -0.0180 182 THR A N 1106 C CA . THR A 141 ? 0.2997 0.3494 0.3015 -0.0121 0.0961 -0.0126 182 THR A CA 1107 C C . THR A 141 ? 0.3180 0.3706 0.3281 -0.0139 0.1073 -0.0103 182 THR A C 1108 O O . THR A 141 ? 0.3432 0.3914 0.3399 -0.0139 0.1149 -0.0075 182 THR A O 1109 C CB . THR A 141 ? 0.3031 0.3510 0.3086 -0.0142 0.0890 -0.0093 182 THR A CB 1110 O OG1 . THR A 141 ? 0.3132 0.3582 0.3100 -0.0124 0.0799 -0.0111 182 THR A OG1 1111 C CG2 . THR A 141 ? 0.3238 0.3660 0.3198 -0.0165 0.0935 -0.0033 182 THR A CG2 1112 N N . GLU A 142 ? 0.3133 0.3733 0.3453 -0.0151 0.1087 -0.0118 183 GLU A N 1113 C CA . GLU A 142 ? 0.3346 0.3982 0.3775 -0.0172 0.1197 -0.0096 183 GLU A CA 1114 C C . GLU A 142 ? 0.3396 0.4048 0.3776 -0.0147 0.1289 -0.0123 183 GLU A C 1115 O O . GLU A 142 ? 0.3542 0.4196 0.3925 -0.0159 0.1400 -0.0095 183 GLU A O 1116 C CB . GLU A 142 ? 0.3409 0.4125 0.4104 -0.0192 0.1180 -0.0109 183 GLU A CB 1117 C CG . GLU A 142 ? 0.3578 0.4355 0.4389 -0.0163 0.1121 -0.0171 183 GLU A CG 1118 C CD . GLU A 142 ? 0.4086 0.4850 0.4900 -0.0154 0.0992 -0.0187 183 GLU A CD 1119 O OE1 . GLU A 142 ? 0.3890 0.4588 0.4542 -0.0153 0.0937 -0.0167 183 GLU A OE1 1120 O OE2 . GLU A 142 ? 0.4288 0.5110 0.5267 -0.0144 0.0945 -0.0222 183 GLU A OE2 1121 N N . ASP A 143 ? 0.3300 0.3958 0.3634 -0.0112 0.1248 -0.0176 184 ASP A N 1122 C CA . ASP A 143 ? 0.3368 0.4035 0.3645 -0.0083 0.1333 -0.0208 184 ASP A CA 1123 C C . ASP A 143 ? 0.3526 0.4107 0.3547 -0.0074 0.1381 -0.0181 184 ASP A C 1124 O O . ASP A 143 ? 0.3658 0.4233 0.3622 -0.0067 0.1493 -0.0173 184 ASP A O 1125 C CB . ASP A 143 ? 0.3348 0.4031 0.3634 -0.0047 0.1269 -0.0273 184 ASP A CB 1126 C CG . ASP A 143 ? 0.3137 0.3901 0.3661 -0.0047 0.1227 -0.0302 184 ASP A CG 1127 O OD1 . ASP A 143 ? 0.3246 0.4074 0.3951 -0.0064 0.1287 -0.0294 184 ASP A OD1 1128 O OD2 . ASP A 143 ? 0.3046 0.3808 0.3581 -0.0029 0.1133 -0.0332 184 ASP A OD2 1129 N N . PHE A 144 ? 0.3589 0.4102 0.3453 -0.0074 0.1298 -0.0165 185 PHE A N 1130 C CA . PHE A 144 ? 0.3689 0.4115 0.3303 -0.0063 0.1329 -0.0138 185 PHE A CA 1131 C C . PHE A 144 ? 0.3969 0.4366 0.3558 -0.0091 0.1408 -0.0067 185 PHE A C 1132 O O . PHE A 144 ? 0.4158 0.4499 0.3576 -0.0079 0.1489 -0.0043 185 PHE A O 1133 C CB . PHE A 144 ? 0.3607 0.3972 0.3073 -0.0051 0.1214 -0.0145 185 PHE A CB 1134 C CG . PHE A 144 ? 0.3601 0.3963 0.3010 -0.0017 0.1165 -0.0210 185 PHE A CG 1135 C CD1 . PHE A 144 ? 0.3654 0.4056 0.3186 -0.0014 0.1078 -0.0247 185 PHE A CD1 1136 C CD2 . PHE A 144 ? 0.3908 0.4222 0.3135 0.0015 0.1208 -0.0236 185 PHE A CD2 1137 C CE1 . PHE A 144 ? 0.3738 0.4131 0.3225 0.0015 0.1035 -0.0304 185 PHE A CE1 1138 C CE2 . PHE A 144 ? 0.3786 0.4091 0.2967 0.0046 0.1159 -0.0301 185 PHE A CE2 1139 C CZ . PHE A 144 ? 0.3876 0.4222 0.3196 0.0044 0.1074 -0.0334 185 PHE A CZ 1140 N N . PHE A 145 ? 0.3938 0.4368 0.3695 -0.0128 0.1390 -0.0033 186 PHE A N 1141 C CA . PHE A 145 ? 0.4184 0.4589 0.3953 -0.0160 0.1473 0.0036 186 PHE A CA 1142 C C . PHE A 145 ? 0.4414 0.4858 0.4244 -0.0159 0.1615 0.0037 186 PHE A C 1143 O O . PHE A 145 ? 0.4671 0.5061 0.4371 -0.0161 0.1715 0.0086 186 PHE A O 1144 C CB . PHE A 145 ? 0.4034 0.4478 0.4011 -0.0200 0.1430 0.0061 186 PHE A CB 1145 C CG . PHE A 145 ? 0.4077 0.4466 0.3979 -0.0208 0.1321 0.0084 186 PHE A CG 1146 C CD1 . PHE A 145 ? 0.4326 0.4630 0.3986 -0.0187 0.1280 0.0099 186 PHE A CD1 1147 C CD2 . PHE A 145 ? 0.3934 0.4357 0.4016 -0.0235 0.1258 0.0088 186 PHE A CD2 1148 C CE1 . PHE A 145 ? 0.4402 0.4662 0.4014 -0.0193 0.1180 0.0118 186 PHE A CE1 1149 C CE2 . PHE A 145 ? 0.3784 0.4159 0.3806 -0.0240 0.1161 0.0107 186 PHE A CE2 1150 C CZ . PHE A 145 ? 0.3903 0.4199 0.3696 -0.0219 0.1125 0.0123 186 PHE A CZ 1151 N N . LYS A 146 ? 0.4366 0.4902 0.4395 -0.0153 0.1627 -0.0014 187 LYS A N 1152 C CA . LYS A 146 ? 0.4451 0.5039 0.4572 -0.0150 0.1761 -0.0021 187 LYS A CA 1153 C C . LYS A 146 ? 0.4711 0.5239 0.4589 -0.0110 0.1836 -0.0031 187 LYS A C 1154 O O . LYS A 146 ? 0.4781 0.5288 0.4599 -0.0113 0.1966 0.0008 187 LYS A O 1155 C CB . LYS A 146 ? 0.4383 0.5078 0.4753 -0.0142 0.1738 -0.0083 187 LYS A CB 1156 C CG . LYS A 146 ? 0.4698 0.5465 0.5205 -0.0134 0.1870 -0.0102 187 LYS A CG 1157 C CD . LYS A 146 ? 0.5510 0.6331 0.6235 -0.0179 0.1956 -0.0057 187 LYS A CD 1158 C CE . LYS A 146 ? 0.5837 0.6736 0.6836 -0.0204 0.1859 -0.0078 187 LYS A CE 1159 N NZ . LYS A 146 ? 0.6452 0.7409 0.7689 -0.0250 0.1934 -0.0041 187 LYS A NZ 1160 N N . LEU A 147 ? 0.4710 0.5206 0.4443 -0.0073 0.1756 -0.0082 188 LEU A N 1161 C CA . LEU A 147 ? 0.5056 0.5489 0.4547 -0.0031 0.1807 -0.0103 188 LEU A CA 1162 C C . LEU A 147 ? 0.5280 0.5611 0.4524 -0.0031 0.1852 -0.0041 188 LEU A C 1163 O O . LEU A 147 ? 0.5362 0.5662 0.4490 -0.0014 0.1973 -0.0024 188 LEU A O 1164 C CB . LEU A 147 ? 0.5068 0.5475 0.4455 0.0003 0.1690 -0.0167 188 LEU A CB 1165 C CG . LEU A 147 ? 0.5266 0.5738 0.4778 0.0029 0.1678 -0.0243 188 LEU A CG 1166 C CD1 . LEU A 147 ? 0.5721 0.6161 0.5159 0.0047 0.1540 -0.0287 188 LEU A CD1 1167 C CD2 . LEU A 147 ? 0.5595 0.6057 0.5012 0.0065 0.1792 -0.0272 188 LEU A CD2 1168 N N A GLU A 148 ? 0.5214 0.5492 0.4383 -0.0047 0.1758 -0.0005 189 GLU A N 1169 N N B GLU A 148 ? 0.5254 0.5526 0.4403 -0.0044 0.1755 -0.0007 189 GLU A N 1170 C CA A GLU A 148 ? 0.5467 0.5636 0.4376 -0.0038 0.1768 0.0047 189 GLU A CA 1171 C CA B GLU A 148 ? 0.5518 0.5682 0.4414 -0.0038 0.1777 0.0051 189 GLU A CA 1172 C C A GLU A 148 ? 0.5582 0.5726 0.4515 -0.0073 0.1865 0.0134 189 GLU A C 1173 C C B GLU A 148 ? 0.5598 0.5754 0.4553 -0.0073 0.1888 0.0132 189 GLU A C 1174 O O A GLU A 148 ? 0.5805 0.5869 0.4529 -0.0058 0.1946 0.0179 189 GLU A O 1175 O O B GLU A 148 ? 0.5780 0.5877 0.4573 -0.0059 0.1998 0.0171 189 GLU A O 1176 C CB A GLU A 148 ? 0.5398 0.5521 0.4212 -0.0034 0.1617 0.0040 189 GLU A CB 1177 C CB B GLU A 148 ? 0.5515 0.5622 0.4303 -0.0039 0.1636 0.0061 189 GLU A CB 1178 C CG A GLU A 148 ? 0.5605 0.5737 0.4370 0.0001 0.1532 -0.0043 189 GLU A CG 1179 C CG B GLU A 148 ? 0.5999 0.5986 0.4492 -0.0018 0.1645 0.0109 189 GLU A CG 1180 C CD A GLU A 148 ? 0.5708 0.5812 0.4427 0.0001 0.1385 -0.0054 189 GLU A CD 1181 C CD B GLU A 148 ? 0.6395 0.6329 0.4820 -0.0027 0.1521 0.0137 189 GLU A CD 1182 O OE1 A GLU A 148 ? 0.5933 0.6073 0.4805 -0.0029 0.1323 -0.0035 189 GLU A OE1 1183 O OE1 B GLU A 148 ? 0.6429 0.6382 0.4997 -0.0066 0.1500 0.0181 189 GLU A OE1 1184 O OE2 A GLU A 148 ? 0.6118 0.6163 0.4648 0.0034 0.1330 -0.0084 189 GLU A OE2 1185 O OE2 B GLU A 148 ? 0.6547 0.6420 0.4778 0.0006 0.1443 0.0112 189 GLU A OE2 1186 N N . ARG A 149 ? 0.5445 0.5654 0.4629 -0.0118 0.1859 0.0158 190 ARG A N 1187 C CA . ARG A 149 ? 0.5626 0.5813 0.4870 -0.0159 0.1939 0.0240 190 ARG A CA 1188 C C . ARG A 149 ? 0.5749 0.5995 0.5139 -0.0173 0.2095 0.0255 190 ARG A C 1189 O O . ARG A 149 ? 0.6027 0.6220 0.5338 -0.0185 0.2211 0.0324 190 ARG A O 1190 C CB . ARG A 149 ? 0.5371 0.5588 0.4807 -0.0201 0.1845 0.0259 190 ARG A CB 1191 C CG . ARG A 149 ? 0.5341 0.5496 0.4636 -0.0189 0.1702 0.0255 190 ARG A CG 1192 C CD . ARG A 149 ? 0.4935 0.5126 0.4428 -0.0225 0.1609 0.0262 190 ARG A CD 1193 N NE . ARG A 149 ? 0.5093 0.5220 0.4445 -0.0213 0.1489 0.0268 190 ARG A NE 1194 C CZ . ARG A 149 ? 0.4839 0.4969 0.4298 -0.0237 0.1403 0.0281 190 ARG A CZ 1195 N NH1 . ARG A 149 ? 0.4484 0.4675 0.4185 -0.0274 0.1417 0.0286 190 ARG A NH1 1196 N NH2 . ARG A 149 ? 0.5001 0.5075 0.4329 -0.0222 0.1301 0.0285 190 ARG A NH2 1197 N N . ASP A 150 ? 0.5721 0.6073 0.5327 -0.0171 0.2102 0.0193 191 ASP A N 1198 C CA . ASP A 150 ? 0.5852 0.6275 0.5636 -0.0186 0.2247 0.0201 191 ASP A CA 1199 C C . ASP A 150 ? 0.5949 0.6368 0.5599 -0.0140 0.2353 0.0168 191 ASP A C 1200 O O . ASP A 150 ? 0.6035 0.6443 0.5659 -0.0142 0.2505 0.0209 191 ASP A O 1201 C CB . ASP A 150 ? 0.5719 0.6266 0.5847 -0.0212 0.2206 0.0158 191 ASP A CB 1202 C CG . ASP A 150 ? 0.6198 0.6749 0.6460 -0.0254 0.2099 0.0184 191 ASP A CG 1203 O OD1 . ASP A 150 ? 0.6952 0.7427 0.7123 -0.0279 0.2111 0.0254 191 ASP A OD1 1204 O OD2 . ASP A 150 ? 0.6438 0.7063 0.6892 -0.0258 0.2002 0.0133 191 ASP A OD2 1205 N N . MET A 151 ? 0.5828 0.6253 0.5395 -0.0097 0.2275 0.0092 192 MET A N 1206 C CA . MET A 151 ? 0.5964 0.6392 0.5427 -0.0050 0.2362 0.0045 192 MET A CA 1207 C C . MET A 151 ? 0.6155 0.6459 0.5254 -0.0010 0.2376 0.0059 192 MET A C 1208 O O . MET A 151 ? 0.6302 0.6585 0.5265 0.0032 0.2465 0.0030 192 MET A O 1209 C CB . MET A 151 ? 0.5754 0.6249 0.5324 -0.0022 0.2272 -0.0049 192 MET A CB 1210 C CG . MET A 151 ? 0.5784 0.6404 0.5705 -0.0049 0.2262 -0.0074 192 MET A CG 1211 S SD . MET A 151 ? 0.5879 0.6554 0.5878 -0.0009 0.2159 -0.0177 192 MET A SD 1212 C CE . MET A 151 ? 0.5938 0.6647 0.5931 0.0034 0.2316 -0.0219 192 MET A CE 1213 N N . LYS A 152 ? 0.6114 0.6335 0.5058 -0.0020 0.2284 0.0100 193 LYS A N 1214 C CA . LYS A 152 ? 0.6434 0.6529 0.5028 0.0017 0.2274 0.0119 193 LYS A CA 1215 C C . LYS A 152 ? 0.6476 0.6549 0.4909 0.0072 0.2216 0.0034 193 LYS A C 1216 O O . LYS A 152 ? 0.6742 0.6735 0.4915 0.0116 0.2273 0.0029 193 LYS A O 1217 C CB . LYS A 152 ? 0.6735 0.6768 0.5183 0.0022 0.2441 0.0190 193 LYS A CB 1218 C CG . LYS A 152 ? 0.7223 0.7175 0.5583 -0.0009 0.2447 0.0289 193 LYS A CG 1219 C CD . LYS A 152 ? 0.7363 0.7387 0.6029 -0.0074 0.2438 0.0330 193 LYS A CD 1220 C CE . LYS A 152 ? 0.7743 0.7678 0.6319 -0.0102 0.2489 0.0436 193 LYS A CE 1221 N NZ . LYS A 152 ? 0.7844 0.7803 0.6608 -0.0151 0.2385 0.0462 193 LYS A NZ 1222 N N . ILE A 153 ? 0.6167 0.6305 0.4753 0.0072 0.2105 -0.0034 194 ILE A N 1223 C CA . ILE A 153 ? 0.6303 0.6421 0.4764 0.0120 0.2039 -0.0118 194 ILE A CA 1224 C C . ILE A 153 ? 0.6221 0.6276 0.4549 0.0123 0.1883 -0.0125 194 ILE A C 1225 O O . ILE A 153 ? 0.6102 0.6189 0.4571 0.0088 0.1792 -0.0107 194 ILE A O 1226 C CB . ILE A 153 ? 0.6175 0.6398 0.4875 0.0125 0.2032 -0.0192 194 ILE A CB 1227 C CG1 . ILE A 153 ? 0.6463 0.6728 0.5221 0.0141 0.2196 -0.0198 194 ILE A CG1 1228 C CG2 . ILE A 153 ? 0.6280 0.6476 0.4879 0.0165 0.1928 -0.0276 194 ILE A CG2 1229 C CD1 . ILE A 153 ? 0.6607 0.6992 0.5664 0.0134 0.2215 -0.0247 194 ILE A CD1 1230 N N . ASN A 154 ? 0.6416 0.6382 0.4473 0.0167 0.1853 -0.0154 195 ASN A N 1231 C CA . ASN A 154 ? 0.6468 0.6369 0.4385 0.0174 0.1710 -0.0160 195 ASN A CA 1232 C C . ASN A 154 ? 0.6267 0.6193 0.4224 0.0196 0.1605 -0.0251 195 ASN A C 1233 O O . ASN A 154 ? 0.6221 0.6127 0.4077 0.0237 0.1634 -0.0313 195 ASN A O 1234 C CB . ASN A 154 ? 0.6946 0.6726 0.4533 0.0209 0.1734 -0.0130 195 ASN A CB 1235 C CG . ASN A 154 ? 0.7372 0.7082 0.4812 0.0217 0.1590 -0.0127 195 ASN A CG 1236 O OD1 . ASN A 154 ? 0.7374 0.7126 0.4953 0.0196 0.1473 -0.0150 195 ASN A OD1 1237 N ND2 . ASN A 154 ? 0.8385 0.7985 0.5537 0.0250 0.1598 -0.0098 195 ASN A ND2 1238 N N . CYS A 155 ? 0.5872 0.5838 0.3977 0.0169 0.1487 -0.0260 196 CYS A N 1239 C CA . CYS A 155 ? 0.5839 0.5825 0.3994 0.0186 0.1388 -0.0339 196 CYS A CA 1240 C C . CYS A 155 ? 0.5921 0.5823 0.3864 0.0214 0.1285 -0.0371 196 CYS A C 1241 O O . CYS A 155 ? 0.5811 0.5722 0.3793 0.0226 0.1199 -0.0436 196 CYS A O 1242 C CB . CYS A 155 ? 0.5441 0.5505 0.3850 0.0149 0.1310 -0.0337 196 CYS A CB 1243 S SG . CYS A 155 ? 0.5786 0.5959 0.4477 0.0124 0.1404 -0.0328 196 CYS A SG 1244 N N . SER A 156 ? 0.6052 0.5872 0.3778 0.0224 0.1286 -0.0327 197 SER A N 1245 C CA . SER A 156 ? 0.6184 0.5927 0.3719 0.0251 0.1176 -0.0357 197 SER A CA 1246 C C . SER A 156 ? 0.6253 0.5960 0.3660 0.0298 0.1169 -0.0444 197 SER A C 1247 O O . SER A 156 ? 0.6359 0.6037 0.3645 0.0328 0.1274 -0.0456 197 SER A O 1248 C CB . SER A 156 ? 0.6474 0.6131 0.3796 0.0258 0.1176 -0.0289 197 SER A CB 1249 O OG . SER A 156 ? 0.6974 0.6552 0.4087 0.0295 0.1077 -0.0328 197 SER A OG 1250 N N . GLY A 157 ? 0.6072 0.5778 0.3511 0.0303 0.1049 -0.0505 198 GLY A N 1251 C CA . GLY A 157 ? 0.6095 0.5765 0.3436 0.0345 0.1021 -0.0595 198 GLY A CA 1252 C C . GLY A 157 ? 0.5916 0.5648 0.3417 0.0349 0.1084 -0.0648 198 GLY A C 1253 O O . GLY A 157 ? 0.6102 0.5800 0.3525 0.0386 0.1074 -0.0725 198 GLY A O 1254 N N . LYS A 158 ? 0.5628 0.5446 0.3353 0.0315 0.1143 -0.0610 199 LYS A N 1255 C CA . LYS A 158 ? 0.5434 0.5317 0.3331 0.0320 0.1204 -0.0655 199 LYS A CA 1256 C C . LYS A 158 ? 0.5122 0.5060 0.3234 0.0298 0.1108 -0.0684 199 LYS A C 1257 O O . LYS A 158 ? 0.4980 0.4925 0.3144 0.0269 0.1019 -0.0653 199 LYS A O 1258 C CB . LYS A 158 ? 0.5411 0.5358 0.3434 0.0300 0.1329 -0.0598 199 LYS A CB 1259 C CG . LYS A 158 ? 0.5928 0.5823 0.3755 0.0315 0.1438 -0.0551 199 LYS A CG 1260 C CD . LYS A 158 ? 0.6483 0.6345 0.4179 0.0365 0.1523 -0.0610 199 LYS A CD 1261 C CE . LYS A 158 ? 0.7052 0.6865 0.4563 0.0382 0.1652 -0.0557 199 LYS A CE 1262 N NZ . LYS A 158 ? 0.7545 0.7241 0.4739 0.0418 0.1609 -0.0562 199 LYS A NZ 1263 N N . ILE A 159 ? 0.4986 0.4958 0.3213 0.0314 0.1127 -0.0744 200 ILE A N 1264 C CA . ILE A 159 ? 0.4779 0.4806 0.3227 0.0293 0.1058 -0.0762 200 ILE A CA 1265 C C . ILE A 159 ? 0.4623 0.4738 0.3277 0.0270 0.1129 -0.0718 200 ILE A C 1266 O O . ILE A 159 ? 0.4668 0.4812 0.3353 0.0285 0.1233 -0.0725 200 ILE A O 1267 C CB . ILE A 159 ? 0.4870 0.4879 0.3338 0.0325 0.1031 -0.0849 200 ILE A CB 1268 C CG1 . ILE A 159 ? 0.5134 0.5057 0.3418 0.0343 0.0941 -0.0895 200 ILE A CG1 1269 C CG2 . ILE A 159 ? 0.4852 0.4919 0.3557 0.0306 0.0978 -0.0858 200 ILE A CG2 1270 C CD1 . ILE A 159 ? 0.5484 0.5372 0.3752 0.0378 0.0922 -0.0986 200 ILE A CD1 1271 N N . VAL A 160 ? 0.4316 0.4475 0.3114 0.0233 0.1072 -0.0674 201 VAL A N 1272 C CA . VAL A 160 ? 0.4253 0.4494 0.3249 0.0211 0.1128 -0.0635 201 VAL A CA 1273 C C . VAL A 160 ? 0.4038 0.4328 0.3227 0.0218 0.1096 -0.0678 201 VAL A C 1274 O O . VAL A 160 ? 0.3874 0.4141 0.3075 0.0220 0.1004 -0.0706 201 VAL A O 1275 C CB . VAL A 160 ? 0.4323 0.4579 0.3358 0.0170 0.1094 -0.0561 201 VAL A CB 1276 C CG1 A VAL A 160 ? 0.4370 0.4568 0.3205 0.0168 0.1132 -0.0517 201 VAL A CG1 1277 C CG1 B VAL A 160 ? 0.3856 0.4185 0.3124 0.0146 0.1061 -0.0544 201 VAL A CG1 1278 C CG2 A VAL A 160 ? 0.3957 0.4205 0.3032 0.0156 0.0977 -0.0562 201 VAL A CG2 1279 C CG2 B VAL A 160 ? 0.4533 0.4774 0.3470 0.0162 0.1186 -0.0507 201 VAL A CG2 1280 N N . ILE A 161 ? 0.3778 0.4133 0.3115 0.0223 0.1173 -0.0682 202 ILE A N 1281 C CA . ILE A 161 ? 0.3533 0.3941 0.3072 0.0229 0.1142 -0.0711 202 ILE A CA 1282 C C . ILE A 161 ? 0.3414 0.3899 0.3144 0.0200 0.1153 -0.0661 202 ILE A C 1283 O O . ILE A 161 ? 0.3450 0.3974 0.3220 0.0188 0.1238 -0.0629 202 ILE A O 1284 C CB . ILE A 161 ? 0.3614 0.4030 0.3182 0.0271 0.1204 -0.0777 202 ILE A CB 1285 C CG1 . ILE A 161 ? 0.3449 0.3915 0.3227 0.0280 0.1165 -0.0803 202 ILE A CG1 1286 C CG2 . ILE A 161 ? 0.3659 0.4104 0.3209 0.0280 0.1336 -0.0767 202 ILE A CG2 1287 C CD1 . ILE A 161 ? 0.3765 0.4210 0.3544 0.0326 0.1189 -0.0879 202 ILE A CD1 1288 N N . ALA A 162 ? 0.3243 0.3745 0.3082 0.0187 0.1064 -0.0652 203 ALA A N 1289 C CA . ALA A 162 ? 0.3199 0.3763 0.3202 0.0161 0.1049 -0.0608 203 ALA A CA 1290 C C . ALA A 162 ? 0.3064 0.3668 0.3242 0.0176 0.1000 -0.0634 203 ALA A C 1291 O O . ALA A 162 ? 0.3134 0.3701 0.3282 0.0193 0.0940 -0.0665 203 ALA A O 1292 C CB . ALA A 162 ? 0.3098 0.3630 0.3030 0.0130 0.0977 -0.0560 203 ALA A CB 1293 N N . ARG A 163 ? 0.3049 0.3726 0.3410 0.0170 0.1023 -0.0621 204 ARG A N 1294 C CA . ARG A 163 ? 0.2868 0.3579 0.3387 0.0185 0.0962 -0.0638 204 ARG A CA 1295 C C . ARG A 163 ? 0.2714 0.3413 0.3246 0.0164 0.0869 -0.0601 204 ARG A C 1296 O O . ARG A 163 ? 0.2706 0.3409 0.3213 0.0133 0.0867 -0.0557 204 ARG A O 1297 C CB . ARG A 163 ? 0.2913 0.3707 0.3635 0.0195 0.1011 -0.0649 204 ARG A CB 1298 C CG . ARG A 163 ? 0.3007 0.3853 0.3801 0.0164 0.1070 -0.0610 204 ARG A CG 1299 C CD . ARG A 163 ? 0.3250 0.4184 0.4279 0.0177 0.1097 -0.0630 204 ARG A CD 1300 N NE . ARG A 163 ? 0.3201 0.4192 0.4326 0.0147 0.1170 -0.0599 204 ARG A NE 1301 C CZ . ARG A 163 ? 0.3337 0.4412 0.4687 0.0148 0.1189 -0.0607 204 ARG A CZ 1302 N NH1 . ARG A 163 ? 0.3126 0.4237 0.4617 0.0180 0.1132 -0.0643 204 ARG A NH1 1303 N NH2 . ARG A 163 ? 0.3013 0.4137 0.4455 0.0116 0.1262 -0.0577 204 ARG A NH2 1304 N N . TYR A 164 ? 0.2481 0.3160 0.3043 0.0183 0.0796 -0.0618 205 TYR A N 1305 C CA . TYR A 164 ? 0.2513 0.3185 0.3104 0.0171 0.0712 -0.0587 205 TYR A CA 1306 C C . TYR A 164 ? 0.2413 0.3151 0.3164 0.0164 0.0710 -0.0568 205 TYR A C 1307 O O . TYR A 164 ? 0.2478 0.3273 0.3358 0.0176 0.0756 -0.0589 205 TYR A O 1308 C CB . TYR A 164 ? 0.2379 0.3019 0.2992 0.0200 0.0653 -0.0611 205 TYR A CB 1309 C CG . TYR A 164 ? 0.2453 0.3019 0.2928 0.0199 0.0615 -0.0617 205 TYR A CG 1310 C CD1 . TYR A 164 ? 0.2370 0.2899 0.2831 0.0226 0.0612 -0.0660 205 TYR A CD1 1311 C CD2 . TYR A 164 ? 0.2414 0.2949 0.2794 0.0173 0.0574 -0.0582 205 TYR A CD2 1312 C CE1 . TYR A 164 ? 0.2487 0.2950 0.2848 0.0223 0.0570 -0.0666 205 TYR A CE1 1313 C CE2 . TYR A 164 ? 0.2536 0.3011 0.2818 0.0172 0.0534 -0.0588 205 TYR A CE2 1314 C CZ . TYR A 164 ? 0.2551 0.2992 0.2829 0.0195 0.0531 -0.0630 205 TYR A CZ 1315 O OH . TYR A 164 ? 0.2661 0.3044 0.2864 0.0191 0.0488 -0.0636 205 TYR A OH 1316 N N . GLY A 165 ? 0.2396 0.3130 0.3149 0.0145 0.0652 -0.0533 206 GLY A N 1317 C CA . GLY A 165 ? 0.2355 0.3145 0.3261 0.0140 0.0628 -0.0520 206 GLY A CA 1318 C C . GLY A 165 ? 0.2447 0.3239 0.3325 0.0102 0.0630 -0.0479 206 GLY A C 1319 O O . GLY A 165 ? 0.2533 0.3294 0.3288 0.0080 0.0671 -0.0460 206 GLY A O 1320 N N . LYS A 166 ? 0.2328 0.3154 0.3322 0.0097 0.0584 -0.0467 207 LYS A N 1321 C CA . LYS A 166 ? 0.2381 0.3216 0.3391 0.0061 0.0585 -0.0432 207 LYS A CA 1322 C C . LYS A 166 ? 0.2359 0.3135 0.3225 0.0044 0.0543 -0.0400 207 LYS A C 1323 O O . LYS A 166 ? 0.2396 0.3174 0.3302 0.0032 0.0494 -0.0381 207 LYS A O 1324 C CB . LYS A 166 ? 0.2410 0.3275 0.3448 0.0034 0.0682 -0.0420 207 LYS A CB 1325 C CG . LYS A 166 ? 0.2737 0.3672 0.3937 0.0048 0.0742 -0.0452 207 LYS A CG 1326 C CD . LYS A 166 ? 0.3335 0.4328 0.4730 0.0053 0.0692 -0.0464 207 LYS A CD 1327 C CE . LYS A 166 ? 0.3562 0.4633 0.5136 0.0062 0.0762 -0.0493 207 LYS A CE 1328 N NZ . LYS A 166 ? 0.4129 0.5259 0.5906 0.0075 0.0696 -0.0514 207 LYS A NZ 1329 N N . VAL A 167 ? 0.2355 0.3079 0.3062 0.0045 0.0557 -0.0396 208 VAL A N 1330 C CA . VAL A 167 ? 0.2287 0.2957 0.2862 0.0030 0.0516 -0.0366 208 VAL A CA 1331 C C . VAL A 167 ? 0.2165 0.2788 0.2631 0.0049 0.0486 -0.0380 208 VAL A C 1332 O O . VAL A 167 ? 0.2281 0.2903 0.2738 0.0067 0.0515 -0.0411 208 VAL A O 1333 C CB . VAL A 167 ? 0.2429 0.3079 0.2914 -0.0001 0.0568 -0.0334 208 VAL A CB 1334 C CG1 . VAL A 167 ? 0.2110 0.2804 0.2718 -0.0025 0.0606 -0.0316 208 VAL A CG1 1335 C CG2 . VAL A 167 ? 0.2798 0.3425 0.3171 0.0004 0.0634 -0.0347 208 VAL A CG2 1336 N N . PHE A 168 ? 0.2070 0.2654 0.2455 0.0044 0.0433 -0.0360 209 PHE A N 1337 C CA . PHE A 168 ? 0.2040 0.2579 0.2329 0.0056 0.0405 -0.0370 209 PHE A CA 1338 C C . PHE A 168 ? 0.2163 0.2678 0.2353 0.0053 0.0451 -0.0386 209 PHE A C 1339 O O . PHE A 168 ? 0.2347 0.2856 0.2472 0.0036 0.0491 -0.0371 209 PHE A O 1340 C CB . PHE A 168 ? 0.1960 0.2467 0.2182 0.0045 0.0354 -0.0340 209 PHE A CB 1341 C CG . PHE A 168 ? 0.2149 0.2613 0.2280 0.0051 0.0328 -0.0346 209 PHE A CG 1342 C CD1 . PHE A 168 ? 0.2359 0.2811 0.2517 0.0073 0.0308 -0.0367 209 PHE A CD1 1343 C CD2 . PHE A 168 ? 0.2394 0.2827 0.2420 0.0035 0.0321 -0.0330 209 PHE A CD2 1344 C CE1 . PHE A 168 ? 0.2639 0.3051 0.2731 0.0075 0.0284 -0.0373 209 PHE A CE1 1345 C CE2 . PHE A 168 ? 0.2619 0.3018 0.2580 0.0039 0.0291 -0.0339 209 PHE A CE2 1346 C CZ . PHE A 168 ? 0.2618 0.3006 0.2618 0.0057 0.0276 -0.0362 209 PHE A CZ 1347 N N . ARG A 169 ? 0.2111 0.2606 0.2283 0.0073 0.0446 -0.0418 210 ARG A N 1348 C CA . ARG A 169 ? 0.2350 0.2820 0.2428 0.0076 0.0486 -0.0444 210 ARG A CA 1349 C C . ARG A 169 ? 0.2486 0.2914 0.2424 0.0059 0.0472 -0.0427 210 ARG A C 1350 O O . ARG A 169 ? 0.2533 0.2943 0.2380 0.0059 0.0512 -0.0438 210 ARG A O 1351 C CB . ARG A 169 ? 0.2405 0.2855 0.2496 0.0101 0.0475 -0.0486 210 ARG A CB 1352 C CG . ARG A 169 ? 0.2448 0.2858 0.2510 0.0101 0.0410 -0.0481 210 ARG A CG 1353 C CD . ARG A 169 ? 0.2502 0.2888 0.2599 0.0125 0.0400 -0.0518 210 ARG A CD 1354 N NE . ARG A 169 ? 0.2200 0.2608 0.2414 0.0144 0.0385 -0.0513 210 ARG A NE 1355 C CZ . ARG A 169 ? 0.2547 0.2950 0.2793 0.0145 0.0338 -0.0483 210 ARG A CZ 1356 N NH1 . ARG A 169 ? 0.2380 0.2762 0.2564 0.0127 0.0307 -0.0455 210 ARG A NH1 1357 N NH2 . ARG A 169 ? 0.2377 0.2794 0.2716 0.0168 0.0323 -0.0481 210 ARG A NH2 1358 N N . GLY A 170 ? 0.2446 0.2857 0.2366 0.0050 0.0415 -0.0402 211 GLY A N 1359 C CA . GLY A 170 ? 0.2655 0.3032 0.2458 0.0036 0.0397 -0.0385 211 GLY A CA 1360 C C . GLY A 170 ? 0.2588 0.2970 0.2347 0.0020 0.0437 -0.0355 211 GLY A C 1361 O O . GLY A 170 ? 0.2668 0.3016 0.2308 0.0017 0.0445 -0.0350 211 GLY A O 1362 N N . ASN A 171 ? 0.2507 0.2927 0.2363 0.0012 0.0458 -0.0333 212 ASN A N 1363 C CA . ASN A 171 ? 0.2589 0.3013 0.2421 -0.0006 0.0506 -0.0303 212 ASN A CA 1364 C C . ASN A 171 ? 0.2761 0.3182 0.2538 -0.0001 0.0581 -0.0319 212 ASN A C 1365 O O . ASN A 171 ? 0.2962 0.3352 0.2632 -0.0009 0.0616 -0.0296 212 ASN A O 1366 C CB . ASN A 171 ? 0.2587 0.3053 0.2551 -0.0018 0.0511 -0.0282 212 ASN A CB 1367 C CG . ASN A 171 ? 0.2871 0.3329 0.2857 -0.0024 0.0443 -0.0260 212 ASN A CG 1368 O OD1 . ASN A 171 ? 0.2641 0.3113 0.2694 -0.0011 0.0399 -0.0273 212 ASN A OD1 1369 N ND2 . ASN A 171 ? 0.2780 0.3209 0.2696 -0.0040 0.0434 -0.0225 212 ASN A ND2 1370 N N . LYS A 172 ? 0.2541 0.2987 0.2382 0.0017 0.0607 -0.0358 213 LYS A N 1371 C CA . LYS A 172 ? 0.2730 0.3172 0.2516 0.0029 0.0682 -0.0382 213 LYS A CA 1372 C C . LYS A 172 ? 0.2910 0.3290 0.2513 0.0038 0.0675 -0.0393 213 LYS A C 1373 O O . LYS A 172 ? 0.2999 0.3355 0.2495 0.0039 0.0732 -0.0384 213 LYS A O 1374 C CB . LYS A 172 ? 0.2555 0.3027 0.2437 0.0053 0.0696 -0.0430 213 LYS A CB 1375 C CG . LYS A 172 ? 0.2627 0.3161 0.2698 0.0052 0.0693 -0.0426 213 LYS A CG 1376 C CD . LYS A 172 ? 0.2671 0.3226 0.2826 0.0081 0.0700 -0.0474 213 LYS A CD 1377 C CE . LYS A 172 ? 0.2630 0.3240 0.2964 0.0087 0.0679 -0.0475 213 LYS A CE 1378 N NZ . LYS A 172 ? 0.2544 0.3212 0.2988 0.0083 0.0753 -0.0476 213 LYS A NZ 1379 N N . VAL A 173 ? 0.2852 0.3204 0.2419 0.0045 0.0602 -0.0412 214 VAL A N 1380 C CA . VAL A 173 ? 0.2932 0.3228 0.2346 0.0055 0.0579 -0.0433 214 VAL A CA 1381 C C . VAL A 173 ? 0.3058 0.3320 0.2356 0.0042 0.0567 -0.0390 214 VAL A C 1382 O O . VAL A 173 ? 0.3224 0.3443 0.2375 0.0052 0.0590 -0.0394 214 VAL A O 1383 C CB . VAL A 173 ? 0.2950 0.3230 0.2387 0.0063 0.0505 -0.0464 214 VAL A CB 1384 C CG1 . VAL A 173 ? 0.3099 0.3323 0.2389 0.0070 0.0467 -0.0486 214 VAL A CG1 1385 C CG2 . VAL A 173 ? 0.2963 0.3261 0.2488 0.0082 0.0522 -0.0511 214 VAL A CG2 1386 N N . LYS A 174 ? 0.2990 0.3268 0.2351 0.0022 0.0532 -0.0349 215 LYS A N 1387 C CA A LYS A 174 ? 0.3215 0.3462 0.2485 0.0010 0.0520 -0.0303 215 LYS A CA 1388 C CA B LYS A 174 ? 0.3227 0.3472 0.2491 0.0010 0.0519 -0.0304 215 LYS A CA 1389 C C . LYS A 174 ? 0.3339 0.3574 0.2545 0.0006 0.0603 -0.0278 215 LYS A C 1390 O O . LYS A 174 ? 0.3481 0.3664 0.2532 0.0012 0.0612 -0.0261 215 LYS A O 1391 C CB A LYS A 174 ? 0.3158 0.3429 0.2530 -0.0009 0.0480 -0.0267 215 LYS A CB 1392 C CB B LYS A 174 ? 0.3176 0.3440 0.2530 -0.0007 0.0473 -0.0268 215 LYS A CB 1393 C CG A LYS A 174 ? 0.3452 0.3694 0.2757 -0.0023 0.0483 -0.0215 215 LYS A CG 1394 C CG B LYS A 174 ? 0.3497 0.3722 0.2757 -0.0017 0.0452 -0.0224 215 LYS A CG 1395 C CD A LYS A 174 ? 0.3839 0.4091 0.3216 -0.0035 0.0425 -0.0189 215 LYS A CD 1396 C CD B LYS A 174 ? 0.4099 0.4345 0.3459 -0.0032 0.0408 -0.0194 215 LYS A CD 1397 C CE A LYS A 174 ? 0.4200 0.4417 0.3511 -0.0047 0.0429 -0.0139 215 LYS A CE 1398 C CE B LYS A 174 ? 0.4288 0.4584 0.3796 -0.0043 0.0442 -0.0189 215 LYS A CE 1399 N NZ A LYS A 174 ? 0.4252 0.4492 0.3648 -0.0066 0.0487 -0.0111 215 LYS A NZ 1400 N NZ B LYS A 174 ? 0.4866 0.5173 0.4455 -0.0056 0.0405 -0.0159 215 LYS A NZ 1401 N N . ASN A 175 ? 0.3234 0.3517 0.2562 -0.0002 0.0665 -0.0273 216 ASN A N 1402 C CA . ASN A 175 ? 0.3279 0.3560 0.2575 -0.0008 0.0757 -0.0247 216 ASN A CA 1403 C C . ASN A 175 ? 0.3463 0.3704 0.2604 0.0016 0.0808 -0.0274 216 ASN A C 1404 O O . ASN A 175 ? 0.3671 0.3867 0.2679 0.0017 0.0854 -0.0243 216 ASN A O 1405 C CB . ASN A 175 ? 0.3158 0.3508 0.2641 -0.0020 0.0810 -0.0247 216 ASN A CB 1406 C CG . ASN A 175 ? 0.3430 0.3812 0.3052 -0.0044 0.0762 -0.0218 216 ASN A CG 1407 O OD1 . ASN A 175 ? 0.3674 0.4024 0.3244 -0.0054 0.0710 -0.0187 216 ASN A OD1 1408 N ND2 . ASN A 175 ? 0.3118 0.3562 0.2916 -0.0049 0.0778 -0.0230 216 ASN A ND2 1409 N N . ALA A 176 ? 0.3434 0.3685 0.2588 0.0038 0.0798 -0.0332 217 ALA A N 1410 C CA . ALA A 176 ? 0.3627 0.3838 0.2635 0.0067 0.0841 -0.0369 217 ALA A CA 1411 C C . ALA A 176 ? 0.3889 0.4023 0.2695 0.0078 0.0787 -0.0365 217 ALA A C 1412 O O . ALA A 176 ? 0.4230 0.4314 0.2867 0.0095 0.0834 -0.0361 217 ALA A O 1413 C CB . ALA A 176 ? 0.3570 0.3801 0.2647 0.0088 0.0824 -0.0435 217 ALA A CB 1414 N N . GLN A 177 ? 0.3981 0.4108 0.2804 0.0070 0.0691 -0.0365 218 GLN A N 1415 C CA . GLN A 177 ? 0.4372 0.4435 0.3032 0.0082 0.0627 -0.0366 218 GLN A CA 1416 C C . GLN A 177 ? 0.4499 0.4521 0.3036 0.0076 0.0659 -0.0304 218 GLN A C 1417 O O . GLN A 177 ? 0.4646 0.4602 0.2990 0.0098 0.0664 -0.0306 218 GLN A O 1418 C CB . GLN A 177 ? 0.4384 0.4463 0.3130 0.0070 0.0527 -0.0370 218 GLN A CB 1419 C CG . GLN A 177 ? 0.5293 0.5324 0.3926 0.0085 0.0446 -0.0400 218 GLN A CG 1420 C CD . GLN A 177 ? 0.5821 0.5880 0.4577 0.0072 0.0363 -0.0406 218 GLN A CD 1421 O OE1 . GLN A 177 ? 0.5777 0.5869 0.4657 0.0069 0.0354 -0.0437 218 GLN A OE1 1422 N NE2 . GLN A 177 ? 0.6099 0.6141 0.4821 0.0065 0.0306 -0.0374 218 GLN A NE2 1423 N N . LEU A 178 ? 0.4451 0.4505 0.3095 0.0049 0.0682 -0.0251 219 LEU A N 1424 C CA . LEU A 178 ? 0.4748 0.4759 0.3297 0.0040 0.0713 -0.0186 219 LEU A CA 1425 C C . LEU A 178 ? 0.4849 0.4838 0.3309 0.0047 0.0826 -0.0168 219 LEU A C 1426 O O . LEU A 178 ? 0.5052 0.4980 0.3368 0.0051 0.0856 -0.0120 219 LEU A O 1427 C CB . LEU A 178 ? 0.4655 0.4702 0.3354 0.0007 0.0699 -0.0139 219 LEU A CB 1428 C CG . LEU A 178 ? 0.5209 0.5264 0.3962 0.0002 0.0591 -0.0144 219 LEU A CG 1429 C CD1 . LEU A 178 ? 0.5430 0.5519 0.4328 -0.0026 0.0587 -0.0102 219 LEU A CD1 1430 C CD2 . LEU A 178 ? 0.5735 0.5724 0.4321 0.0020 0.0522 -0.0138 219 LEU A CD2 1431 N N . ALA A 179 ? 0.4543 0.4576 0.3083 0.0053 0.0890 -0.0205 220 ALA A N 1432 C CA . ALA A 179 ? 0.4732 0.4748 0.3188 0.0066 0.1006 -0.0196 220 ALA A CA 1433 C C . ALA A 179 ? 0.4872 0.4820 0.3104 0.0107 0.1003 -0.0238 220 ALA A C 1434 O O . ALA A 179 ? 0.5102 0.5020 0.3218 0.0127 0.1097 -0.0235 220 ALA A O 1435 C CB . ALA A 179 ? 0.4577 0.4672 0.3218 0.0059 0.1074 -0.0224 220 ALA A CB 1436 N N . GLY A 180 ? 0.4892 0.4813 0.3062 0.0122 0.0896 -0.0278 221 GLY A N 1437 C CA . GLY A 180 ? 0.5014 0.4864 0.2970 0.0163 0.0876 -0.0324 221 GLY A CA 1438 C C . GLY A 180 ? 0.4958 0.4828 0.2945 0.0186 0.0882 -0.0406 221 GLY A C 1439 O O . GLY A 180 ? 0.5134 0.4945 0.2947 0.0222 0.0875 -0.0451 221 GLY A O 1440 N N . ALA A 181 ? 0.4744 0.4691 0.2950 0.0168 0.0888 -0.0428 222 ALA A N 1441 C CA . ALA A 181 ? 0.4622 0.4587 0.2876 0.0190 0.0892 -0.0504 222 ALA A CA 1442 C C . ALA A 181 ? 0.4641 0.4560 0.2811 0.0209 0.0785 -0.0562 222 ALA A C 1443 O O . ALA A 181 ? 0.4615 0.4522 0.2786 0.0195 0.0695 -0.0544 222 ALA A O 1444 C CB . ALA A 181 ? 0.4351 0.4402 0.2860 0.0168 0.0899 -0.0510 222 ALA A CB 1445 N N . LYS A 182 ? 0.4668 0.4557 0.2766 0.0242 0.0793 -0.0633 223 LYS A N 1446 C CA . LYS A 182 ? 0.4704 0.4556 0.2764 0.0255 0.0684 -0.0693 223 LYS A CA 1447 C C . LYS A 182 ? 0.4512 0.4410 0.2765 0.0246 0.0649 -0.0739 223 LYS A C 1448 O O . LYS A 182 ? 0.4430 0.4301 0.2682 0.0253 0.0565 -0.0790 223 LYS A O 1449 C CB . LYS A 182 ? 0.5190 0.4959 0.3016 0.0298 0.0677 -0.0746 223 LYS A CB 1450 C CG . LYS A 182 ? 0.5383 0.5146 0.3179 0.0329 0.0758 -0.0800 223 LYS A CG 1451 C CD . LYS A 182 ? 0.6209 0.5877 0.3739 0.0375 0.0746 -0.0849 223 LYS A CD 1452 C CE . LYS A 182 ? 0.6545 0.6203 0.4039 0.0411 0.0828 -0.0908 223 LYS A CE 1453 N NZ . LYS A 182 ? 0.7018 0.6578 0.4232 0.0462 0.0827 -0.0957 223 LYS A NZ 1454 N N . GLY A 183 ? 0.4304 0.4269 0.2729 0.0232 0.0711 -0.0720 224 GLY A N 1455 C CA . GLY A 183 ? 0.4170 0.4176 0.2783 0.0225 0.0680 -0.0753 224 GLY A CA 1456 C C . GLY A 183 ? 0.3924 0.4005 0.2711 0.0210 0.0748 -0.0718 224 GLY A C 1457 O O . GLY A 183 ? 0.4002 0.4100 0.2762 0.0209 0.0833 -0.0684 224 GLY A O 1458 N N . VAL A 184 ? 0.3596 0.3718 0.2562 0.0198 0.0711 -0.0724 225 VAL A N 1459 C CA . VAL A 184 ? 0.3472 0.3665 0.2614 0.0187 0.0760 -0.0695 225 VAL A CA 1460 C C . VAL A 184 ? 0.3455 0.3665 0.2724 0.0204 0.0751 -0.0745 225 VAL A C 1461 O O . VAL A 184 ? 0.3482 0.3668 0.2781 0.0203 0.0676 -0.0769 225 VAL A O 1462 C CB . VAL A 184 ? 0.3366 0.3595 0.2611 0.0154 0.0713 -0.0637 225 VAL A CB 1463 C CG1 . VAL A 184 ? 0.3239 0.3539 0.2663 0.0146 0.0757 -0.0615 225 VAL A CG1 1464 C CG2 . VAL A 184 ? 0.3697 0.3903 0.2820 0.0137 0.0713 -0.0586 225 VAL A CG2 1465 N N . ILE A 185 ? 0.3430 0.3680 0.2782 0.0219 0.0827 -0.0758 226 ILE A N 1466 C CA . ILE A 185 ? 0.3280 0.3553 0.2776 0.0238 0.0822 -0.0798 226 ILE A CA 1467 C C . ILE A 185 ? 0.3122 0.3470 0.2798 0.0223 0.0837 -0.0756 226 ILE A C 1468 O O . ILE A 185 ? 0.3237 0.3628 0.2942 0.0216 0.0907 -0.0729 226 ILE A O 1469 C CB . ILE A 185 ? 0.3477 0.3739 0.2932 0.0274 0.0896 -0.0855 226 ILE A CB 1470 C CG1 . ILE A 185 ? 0.3681 0.3861 0.2939 0.0292 0.0873 -0.0902 226 ILE A CG1 1471 C CG2 . ILE A 185 ? 0.3447 0.3737 0.3068 0.0296 0.0896 -0.0893 226 ILE A CG2 1472 C CD1 . ILE A 185 ? 0.3684 0.3842 0.2858 0.0333 0.0955 -0.0960 226 ILE A CD1 1473 N N . LEU A 186 ? 0.2934 0.3293 0.2728 0.0218 0.0771 -0.0750 227 LEU A N 1474 C CA . LEU A 186 ? 0.2827 0.3249 0.2789 0.0208 0.0767 -0.0715 227 LEU A CA 1475 C C . LEU A 186 ? 0.2747 0.3191 0.2839 0.0240 0.0780 -0.0756 227 LEU A C 1476 O O . LEU A 186 ? 0.2932 0.3330 0.3004 0.0259 0.0748 -0.0797 227 LEU A O 1477 C CB . LEU A 186 ? 0.2533 0.2945 0.2520 0.0187 0.0681 -0.0679 227 LEU A CB 1478 C CG . LEU A 186 ? 0.3018 0.3410 0.2895 0.0158 0.0659 -0.0636 227 LEU A CG 1479 C CD1 . LEU A 186 ? 0.3128 0.3501 0.3020 0.0144 0.0574 -0.0612 227 LEU A CD1 1480 C CD2 . LEU A 186 ? 0.3531 0.3973 0.3452 0.0140 0.0705 -0.0593 227 LEU A CD2 1481 N N . TYR A 187 ? 0.2665 0.3176 0.2893 0.0246 0.0825 -0.0748 228 TYR A N 1482 C CA . TYR A 187 ? 0.2635 0.3167 0.2997 0.0280 0.0830 -0.0787 228 TYR A CA 1483 C C . TYR A 187 ? 0.2737 0.3339 0.3278 0.0278 0.0815 -0.0759 228 TYR A C 1484 O O . TYR A 187 ? 0.2663 0.3306 0.3233 0.0251 0.0828 -0.0718 228 TYR A O 1485 C CB . TYR A 187 ? 0.2654 0.3195 0.3005 0.0309 0.0917 -0.0838 228 TYR A CB 1486 C CG . TYR A 187 ? 0.2607 0.3225 0.3051 0.0305 0.1001 -0.0822 228 TYR A CG 1487 C CD1 . TYR A 187 ? 0.2705 0.3389 0.3343 0.0326 0.1020 -0.0837 228 TYR A CD1 1488 C CD2 . TYR A 187 ? 0.2644 0.3267 0.2991 0.0279 0.1058 -0.0790 228 TYR A CD2 1489 C CE1 . TYR A 187 ? 0.2740 0.3503 0.3488 0.0319 0.1101 -0.0823 228 TYR A CE1 1490 C CE2 . TYR A 187 ? 0.2777 0.3471 0.3224 0.0270 0.1140 -0.0769 228 TYR A CE2 1491 C CZ . TYR A 187 ? 0.2939 0.3705 0.3593 0.0289 0.1160 -0.0787 228 TYR A CZ 1492 O OH . TYR A 187 ? 0.3198 0.4037 0.3968 0.0277 0.1238 -0.0768 228 TYR A OH 1493 N N . SER A 188 ? 0.2612 0.3221 0.3271 0.0308 0.0786 -0.0783 229 SER A N 1494 C CA . SER A 188 ? 0.2521 0.3191 0.3352 0.0315 0.0760 -0.0765 229 SER A CA 1495 C C . SER A 188 ? 0.2536 0.3276 0.3503 0.0337 0.0833 -0.0795 229 SER A C 1496 O O . SER A 188 ? 0.2669 0.3401 0.3675 0.0373 0.0854 -0.0841 229 SER A O 1497 C CB . SER A 188 ? 0.2350 0.2980 0.3222 0.0338 0.0680 -0.0768 229 SER A CB 1498 O OG . SER A 188 ? 0.2674 0.3251 0.3441 0.0314 0.0618 -0.0734 229 SER A OG 1499 N N . ASP A 189 ? 0.2377 0.3186 0.3425 0.0317 0.0876 -0.0771 230 ASP A N 1500 C CA . ASP A 189 ? 0.2592 0.3476 0.3789 0.0335 0.0952 -0.0798 230 ASP A CA 1501 C C . ASP A 189 ? 0.2501 0.3433 0.3891 0.0360 0.0892 -0.0805 230 ASP A C 1502 O O . ASP A 189 ? 0.2422 0.3355 0.3844 0.0347 0.0816 -0.0772 230 ASP A O 1503 C CB . ASP A 189 ? 0.2558 0.3495 0.3776 0.0299 0.1021 -0.0766 230 ASP A CB 1504 C CG . ASP A 189 ? 0.2745 0.3751 0.4079 0.0314 0.1128 -0.0794 230 ASP A CG 1505 O OD1 . ASP A 189 ? 0.3002 0.3986 0.4215 0.0313 0.1216 -0.0802 230 ASP A OD1 1506 O OD2 . ASP A 189 ? 0.2678 0.3756 0.4220 0.0332 0.1125 -0.0810 230 ASP A OD2 1507 N N . PRO A 190 ? 0.2635 0.3605 0.4156 0.0400 0.0924 -0.0849 231 PRO A N 1508 C CA . PRO A 190 ? 0.2671 0.3688 0.4380 0.0428 0.0862 -0.0855 231 PRO A CA 1509 C C . PRO A 190 ? 0.2758 0.3857 0.4612 0.0402 0.0855 -0.0827 231 PRO A C 1510 O O . PRO A 190 ? 0.2641 0.3760 0.4605 0.0417 0.0774 -0.0821 231 PRO A O 1511 C CB . PRO A 190 ? 0.2759 0.3810 0.4585 0.0473 0.0917 -0.0910 231 PRO A CB 1512 C CG . PRO A 190 ? 0.3220 0.4228 0.4897 0.0473 0.1001 -0.0935 231 PRO A CG 1513 C CD . PRO A 190 ? 0.2655 0.3610 0.4134 0.0428 0.1003 -0.0897 231 PRO A CD 1514 N N . ALA A 191 ? 0.2713 0.3851 0.4560 0.0364 0.0934 -0.0809 232 ALA A N 1515 C CA . ALA A 191 ? 0.2711 0.3918 0.4696 0.0333 0.0919 -0.0779 232 ALA A CA 1516 C C . ALA A 191 ? 0.2705 0.3870 0.4634 0.0318 0.0808 -0.0744 232 ALA A C 1517 O O . ALA A 191 ? 0.2625 0.3838 0.4698 0.0318 0.0749 -0.0737 232 ALA A O 1518 C CB . ALA A 191 ? 0.2819 0.4050 0.4766 0.0290 0.1019 -0.0754 232 ALA A CB 1519 N N . ASP A 192 ? 0.2551 0.3629 0.4274 0.0308 0.0778 -0.0724 233 ASP A N 1520 C CA . ASP A 192 ? 0.2568 0.3601 0.4212 0.0292 0.0687 -0.0688 233 ASP A CA 1521 C C . ASP A 192 ? 0.2628 0.3606 0.4241 0.0331 0.0600 -0.0697 233 ASP A C 1522 O O . ASP A 192 ? 0.2695 0.3650 0.4293 0.0331 0.0517 -0.0673 233 ASP A O 1523 C CB . ASP A 192 ? 0.2705 0.3678 0.4148 0.0255 0.0713 -0.0658 233 ASP A CB 1524 C CG . ASP A 192 ? 0.2668 0.3679 0.4116 0.0220 0.0806 -0.0643 233 ASP A CG 1525 O OD1 . ASP A 192 ? 0.3058 0.4108 0.4588 0.0192 0.0795 -0.0616 233 ASP A OD1 1526 O OD2 . ASP A 192 ? 0.3027 0.4029 0.4403 0.0222 0.0888 -0.0659 233 ASP A OD2 1527 N N . TYR A 193 ? 0.2425 0.3375 0.4018 0.0364 0.0620 -0.0730 234 TYR A N 1528 C CA . TYR A 193 ? 0.2370 0.3250 0.3911 0.0397 0.0546 -0.0733 234 TYR A CA 1529 C C . TYR A 193 ? 0.2493 0.3391 0.4168 0.0450 0.0530 -0.0770 234 TYR A C 1530 O O . TYR A 193 ? 0.2425 0.3258 0.4053 0.0480 0.0490 -0.0777 234 TYR A O 1531 C CB . TYR A 193 ? 0.2525 0.3321 0.3876 0.0385 0.0559 -0.0730 234 TYR A CB 1532 C CG . TYR A 193 ? 0.2343 0.3113 0.3565 0.0340 0.0548 -0.0689 234 TYR A CG 1533 C CD1 . TYR A 193 ? 0.2337 0.3121 0.3487 0.0306 0.0617 -0.0684 234 TYR A CD1 1534 C CD2 . TYR A 193 ? 0.2293 0.3028 0.3471 0.0335 0.0471 -0.0654 234 TYR A CD2 1535 C CE1 . TYR A 193 ? 0.2570 0.3332 0.3610 0.0267 0.0604 -0.0645 234 TYR A CE1 1536 C CE2 . TYR A 193 ? 0.2497 0.3213 0.3568 0.0296 0.0461 -0.0617 234 TYR A CE2 1537 C CZ . TYR A 193 ? 0.2713 0.3443 0.3720 0.0262 0.0526 -0.0614 234 TYR A CZ 1538 O OH . TYR A 193 ? 0.2370 0.3079 0.3277 0.0228 0.0513 -0.0578 234 TYR A OH 1539 N N . PHE A 194 ? 0.2522 0.3508 0.4374 0.0462 0.0565 -0.0794 235 PHE A N 1540 C CA . PHE A 194 ? 0.2665 0.3675 0.4662 0.0515 0.0549 -0.0832 235 PHE A CA 1541 C C . PHE A 194 ? 0.2760 0.3864 0.4962 0.0522 0.0523 -0.0836 235 PHE A C 1542 O O . PHE A 194 ? 0.2977 0.4163 0.5295 0.0506 0.0596 -0.0852 235 PHE A O 1543 C CB . PHE A 194 ? 0.2655 0.3679 0.4670 0.0531 0.0643 -0.0877 235 PHE A CB 1544 C CG . PHE A 194 ? 0.2639 0.3663 0.4770 0.0591 0.0623 -0.0916 235 PHE A CG 1545 C CD1 . PHE A 194 ? 0.2848 0.3779 0.4877 0.0619 0.0596 -0.0928 235 PHE A CD1 1546 C CD2 . PHE A 194 ? 0.2901 0.4017 0.5254 0.0620 0.0628 -0.0943 235 PHE A CD2 1547 C CE1 . PHE A 194 ? 0.3045 0.3967 0.5180 0.0676 0.0573 -0.0962 235 PHE A CE1 1548 C CE2 . PHE A 194 ? 0.2915 0.4029 0.5378 0.0679 0.0604 -0.0979 235 PHE A CE2 1549 C CZ . PHE A 194 ? 0.3047 0.4061 0.5397 0.0708 0.0578 -0.0989 235 PHE A CZ 1550 N N . ALA A 195 ? 0.2780 0.3870 0.5022 0.0546 0.0421 -0.0822 236 ALA A N 1551 C CA . ALA A 195 ? 0.3013 0.4190 0.5456 0.0557 0.0379 -0.0832 236 ALA A CA 1552 C C . ALA A 195 ? 0.3239 0.4482 0.5879 0.0602 0.0404 -0.0880 236 ALA A C 1553 O O . ALA A 195 ? 0.3176 0.4372 0.5796 0.0647 0.0388 -0.0898 236 ALA A O 1554 C CB . ALA A 195 ? 0.2962 0.4095 0.5375 0.0580 0.0258 -0.0809 236 ALA A CB 1555 N N . PRO A 196 ? 0.3395 0.4747 0.6234 0.0590 0.0447 -0.0900 237 PRO A N 1556 C CA . PRO A 196 ? 0.3528 0.4956 0.6580 0.0634 0.0473 -0.0947 237 PRO A CA 1557 C C . PRO A 196 ? 0.3435 0.4840 0.6560 0.0698 0.0356 -0.0961 237 PRO A C 1558 O O . PRO A 196 ? 0.3462 0.4846 0.6572 0.0702 0.0254 -0.0939 237 PRO A O 1559 C CB . PRO A 196 ? 0.3630 0.5177 0.6886 0.0601 0.0516 -0.0955 237 PRO A CB 1560 C CG . PRO A 196 ? 0.3688 0.5208 0.6789 0.0533 0.0567 -0.0913 237 PRO A CG 1561 C CD . PRO A 196 ? 0.3494 0.4903 0.6371 0.0532 0.0483 -0.0879 237 PRO A CD 1562 N N . GLY A 197 ? 0.3492 0.4889 0.6675 0.0750 0.0372 -0.0996 238 GLY A N 1563 C CA . GLY A 197 ? 0.3484 0.4867 0.6766 0.0819 0.0270 -0.1013 238 GLY A CA 1564 C C . GLY A 197 ? 0.3556 0.4809 0.6644 0.0847 0.0184 -0.0981 238 GLY A C 1565 O O . GLY A 197 ? 0.3795 0.5022 0.6940 0.0906 0.0094 -0.0987 238 GLY A O 1566 N N . VAL A 198 ? 0.3113 0.4281 0.5975 0.0807 0.0214 -0.0948 239 VAL A N 1567 C CA . VAL A 198 ? 0.2986 0.4027 0.5663 0.0828 0.0151 -0.0915 239 VAL A CA 1568 C C . VAL A 198 ? 0.2981 0.3957 0.5552 0.0828 0.0224 -0.0929 239 VAL A C 1569 O O . VAL A 198 ? 0.3022 0.4031 0.5577 0.0794 0.0320 -0.0948 239 VAL A O 1570 C CB . VAL A 198 ? 0.3026 0.4015 0.5535 0.0786 0.0102 -0.0862 239 VAL A CB 1571 C CG1 A VAL A 198 ? 0.3183 0.4248 0.5715 0.0725 0.0158 -0.0858 239 VAL A CG1 1572 C CG1 B VAL A 198 ? 0.2829 0.3689 0.5152 0.0806 0.0049 -0.0825 239 VAL A CG1 1573 C CG2 A VAL A 198 ? 0.2813 0.3681 0.5100 0.0776 0.0104 -0.0829 239 VAL A CG2 1574 C CG2 B VAL A 198 ? 0.2902 0.3957 0.5528 0.0791 0.0025 -0.0858 239 VAL A CG2 1575 N N . LYS A 199 ? 0.2991 0.3871 0.5497 0.0872 0.0175 -0.0923 240 LYS A N 1576 C CA . LYS A 199 ? 0.3101 0.3908 0.5519 0.0878 0.0229 -0.0941 240 LYS A CA 1577 C C . LYS A 199 ? 0.3023 0.3749 0.5222 0.0827 0.0249 -0.0905 240 LYS A C 1578 O O . LYS A 199 ? 0.3086 0.3785 0.5193 0.0803 0.0198 -0.0859 240 LYS A O 1579 C CB . LYS A 199 ? 0.3230 0.3960 0.5672 0.0945 0.0163 -0.0942 240 LYS A CB 1580 C CG . LYS A 199 ? 0.3516 0.4320 0.6184 0.1005 0.0156 -0.0991 240 LYS A CG 1581 C CD . LYS A 199 ? 0.4265 0.5145 0.7027 0.0996 0.0267 -0.1047 240 LYS A CD 1582 C CE . LYS A 199 ? 0.4720 0.5681 0.7723 0.1057 0.0263 -0.1096 240 LYS A CE 1583 N NZ . LYS A 199 ? 0.4997 0.6039 0.8100 0.1051 0.0381 -0.1152 240 LYS A NZ 1584 N N . SER A 200 ? 0.3012 0.3701 0.5134 0.0812 0.0320 -0.0930 241 SER A N 1585 C CA A SER A 200 ? 0.2980 0.3584 0.4906 0.0769 0.0335 -0.0905 241 SER A CA 1586 C CA B SER A 200 ? 0.2974 0.3583 0.4902 0.0767 0.0329 -0.0901 241 SER A CA 1587 C C . SER A 200 ? 0.2922 0.3412 0.4767 0.0793 0.0266 -0.0874 241 SER A C 1588 O O . SER A 200 ? 0.3033 0.3491 0.4959 0.0849 0.0233 -0.0888 241 SER A O 1589 C CB A SER A 200 ? 0.3142 0.3727 0.5018 0.0759 0.0419 -0.0951 241 SER A CB 1590 C CB B SER A 200 ? 0.3096 0.3706 0.4957 0.0738 0.0422 -0.0938 241 SER A CB 1591 O OG A SER A 200 ? 0.3285 0.3963 0.5217 0.0740 0.0500 -0.0982 241 SER A OG 1592 O OG B SER A 200 ? 0.3480 0.4072 0.5405 0.0781 0.0455 -0.0990 241 SER A OG 1593 N N . TYR A 201 ? 0.2829 0.3254 0.4519 0.0754 0.0252 -0.0833 242 TYR A N 1594 C CA . TYR A 201 ? 0.2925 0.3236 0.4527 0.0768 0.0204 -0.0799 242 TYR A CA 1595 C C . TYR A 201 ? 0.3138 0.3386 0.4759 0.0796 0.0231 -0.0840 242 TYR A C 1596 O O . TYR A 201 ? 0.3267 0.3536 0.4877 0.0777 0.0296 -0.0886 242 TYR A O 1597 C CB . TYR A 201 ? 0.2851 0.3118 0.4297 0.0713 0.0206 -0.0759 242 TYR A CB 1598 C CG . TYR A 201 ? 0.2982 0.3149 0.4359 0.0730 0.0148 -0.0709 242 TYR A CG 1599 C CD1 . TYR A 201 ? 0.3242 0.3410 0.4627 0.0755 0.0085 -0.0666 242 TYR A CD1 1600 C CD2 . TYR A 201 ? 0.3404 0.3471 0.4718 0.0728 0.0157 -0.0707 242 TYR A CD2 1601 C CE1 . TYR A 201 ? 0.3459 0.3531 0.4775 0.0777 0.0039 -0.0618 242 TYR A CE1 1602 C CE2 . TYR A 201 ? 0.3519 0.3492 0.4780 0.0744 0.0112 -0.0657 242 TYR A CE2 1603 C CZ . TYR A 201 ? 0.3680 0.3655 0.4934 0.0769 0.0057 -0.0610 242 TYR A CZ 1604 O OH . TYR A 201 ? 0.4409 0.4285 0.5601 0.0791 0.0018 -0.0557 242 TYR A OH 1605 N N . PRO A 202 ? 0.3286 0.3452 0.4929 0.0843 0.0182 -0.0825 243 PRO A N 1606 C CA . PRO A 202 ? 0.3367 0.3475 0.4986 0.0871 0.0105 -0.0767 243 PRO A CA 1607 C C . PRO A 202 ? 0.3540 0.3698 0.5283 0.0927 0.0051 -0.0767 243 PRO A C 1608 O O . PRO A 202 ? 0.3732 0.3830 0.5444 0.0960 -0.0017 -0.0721 243 PRO A O 1609 C CB . PRO A 202 ? 0.3447 0.3428 0.5023 0.0892 0.0096 -0.0759 243 PRO A CB 1610 C CG . PRO A 202 ? 0.3419 0.3422 0.5097 0.0917 0.0142 -0.0831 243 PRO A CG 1611 C CD . PRO A 202 ? 0.3420 0.3518 0.5083 0.0868 0.0208 -0.0868 243 PRO A CD 1612 N N . ASP A 203 ? 0.3482 0.3745 0.5359 0.0938 0.0080 -0.0817 244 ASP A N 1613 C CA . ASP A 203 ? 0.3619 0.3937 0.5646 0.0995 0.0028 -0.0828 244 ASP A CA 1614 C C . ASP A 203 ? 0.3403 0.3814 0.5467 0.0976 -0.0001 -0.0813 244 ASP A C 1615 O O . ASP A 203 ? 0.3472 0.3931 0.5655 0.1020 -0.0059 -0.0819 244 ASP A O 1616 C CB . ASP A 203 ? 0.3787 0.4159 0.5967 0.1028 0.0075 -0.0895 244 ASP A CB 1617 C CG . ASP A 203 ? 0.4487 0.4754 0.6628 0.1051 0.0096 -0.0913 244 ASP A CG 1618 O OD1 . ASP A 203 ? 0.4931 0.5091 0.7027 0.1086 0.0038 -0.0878 244 ASP A OD1 1619 O OD2 . ASP A 203 ? 0.5459 0.5740 0.7598 0.1030 0.0173 -0.0960 244 ASP A OD2 1620 N N . GLY A 204 ? 0.3279 0.3710 0.5240 0.0913 0.0031 -0.0792 245 GLY A N 1621 C CA . GLY A 204 ? 0.2941 0.3449 0.4924 0.0888 0.0005 -0.0776 245 GLY A CA 1622 C C . GLY A 204 ? 0.2935 0.3424 0.4764 0.0822 0.0040 -0.0746 245 GLY A C 1623 O O . GLY A 204 ? 0.3136 0.3548 0.4847 0.0801 0.0071 -0.0735 245 GLY A O 1624 N N . TRP A 205 ? 0.2703 0.3260 0.4542 0.0790 0.0032 -0.0734 246 TRP A N 1625 C CA . TRP A 205 ? 0.2607 0.3141 0.4297 0.0732 0.0052 -0.0700 246 TRP A CA 1626 C C . TRP A 205 ? 0.2566 0.3161 0.4251 0.0677 0.0138 -0.0723 246 TRP A C 1627 O O . TRP A 205 ? 0.2521 0.3110 0.4099 0.0629 0.0153 -0.0697 246 TRP A O 1628 C CB . TRP A 205 ? 0.2628 0.3166 0.4283 0.0731 -0.0019 -0.0662 246 TRP A CB 1629 C CG . TRP A 205 ? 0.2886 0.3521 0.4700 0.0748 -0.0055 -0.0685 246 TRP A CG 1630 C CD1 . TRP A 205 ? 0.3250 0.3894 0.5168 0.0806 -0.0127 -0.0696 246 TRP A CD1 1631 C CD2 . TRP A 205 ? 0.2790 0.3522 0.4680 0.0705 -0.0023 -0.0700 246 TRP A CD2 1632 N NE1 . TRP A 205 ? 0.3401 0.4148 0.5467 0.0802 -0.0146 -0.0721 246 TRP A NE1 1633 C CE2 . TRP A 205 ? 0.3042 0.3842 0.5096 0.0738 -0.0079 -0.0722 246 TRP A CE2 1634 C CE3 . TRP A 205 ? 0.3253 0.4016 0.5090 0.0642 0.0046 -0.0696 246 TRP A CE3 1635 C CZ2 . TRP A 205 ? 0.3087 0.3989 0.5267 0.0706 -0.0065 -0.0740 246 TRP A CZ2 1636 C CZ3 . TRP A 205 ? 0.3529 0.4386 0.5477 0.0613 0.0064 -0.0709 246 TRP A CZ3 1637 C CH2 . TRP A 205 ? 0.3206 0.4133 0.5330 0.0643 0.0010 -0.0731 246 TRP A CH2 1638 N N . ASN A 206 ? 0.2555 0.3203 0.4345 0.0686 0.0197 -0.0770 247 ASN A N 1639 C CA . ASN A 206 ? 0.2514 0.3213 0.4289 0.0640 0.0287 -0.0792 247 ASN A CA 1640 C C . ASN A 206 ? 0.2600 0.3226 0.4232 0.0620 0.0333 -0.0798 247 ASN A C 1641 O O . ASN A 206 ? 0.2563 0.3109 0.4152 0.0646 0.0308 -0.0799 247 ASN A O 1642 C CB . ASN A 206 ? 0.2495 0.3287 0.4442 0.0659 0.0342 -0.0841 247 ASN A CB 1643 C CG . ASN A 206 ? 0.2410 0.3304 0.4482 0.0641 0.0339 -0.0837 247 ASN A CG 1644 O OD1 . ASN A 206 ? 0.2586 0.3483 0.4596 0.0605 0.0313 -0.0801 247 ASN A OD1 1645 N ND2 . ASN A 206 ? 0.2432 0.3412 0.4697 0.0669 0.0364 -0.0875 247 ASN A ND2 1646 N N . LEU A 207 ? 0.2508 0.3159 0.4069 0.0573 0.0396 -0.0802 248 LEU A N 1647 C CA . LEU A 207 ? 0.2404 0.2994 0.3832 0.0553 0.0438 -0.0815 248 LEU A CA 1648 C C . LEU A 207 ? 0.2513 0.3113 0.3996 0.0580 0.0499 -0.0873 248 LEU A C 1649 O O . LEU A 207 ? 0.2653 0.3332 0.4225 0.0582 0.0558 -0.0899 248 LEU A O 1650 C CB . LEU A 207 ? 0.2388 0.3003 0.3718 0.0499 0.0478 -0.0797 248 LEU A CB 1651 C CG . LEU A 207 ? 0.2643 0.3198 0.3819 0.0472 0.0512 -0.0808 248 LEU A CG 1652 C CD1 . LEU A 207 ? 0.2550 0.3018 0.3629 0.0466 0.0451 -0.0779 248 LEU A CD1 1653 C CD2 . LEU A 207 ? 0.2770 0.3365 0.3874 0.0427 0.0558 -0.0793 248 LEU A CD2 1654 N N . PRO A 208 ? 0.2574 0.3092 0.4003 0.0600 0.0491 -0.0893 249 PRO A N 1655 C CA . PRO A 208 ? 0.2538 0.3054 0.3994 0.0625 0.0553 -0.0954 249 PRO A CA 1656 C C . PRO A 208 ? 0.2587 0.3102 0.3920 0.0590 0.0621 -0.0975 249 PRO A C 1657 O O . PRO A 208 ? 0.2612 0.3110 0.3827 0.0546 0.0611 -0.0941 249 PRO A O 1658 C CB . PRO A 208 ? 0.2877 0.3292 0.4307 0.0654 0.0511 -0.0966 249 PRO A CB 1659 C CG . PRO A 208 ? 0.2684 0.3042 0.4044 0.0636 0.0445 -0.0912 249 PRO A CG 1660 C CD . PRO A 208 ? 0.2636 0.3057 0.3987 0.0603 0.0427 -0.0864 249 PRO A CD 1661 N N . GLY A 209 ? 0.2829 0.3357 0.4184 0.0613 0.0689 -0.1031 250 GLY A N 1662 C CA . GLY A 209 ? 0.2965 0.3498 0.4201 0.0588 0.0761 -0.1053 250 GLY A CA 1663 C C . GLY A 209 ? 0.2908 0.3347 0.3970 0.0564 0.0736 -0.1057 250 GLY A C 1664 O O . GLY A 209 ? 0.3002 0.3436 0.3938 0.0537 0.0775 -0.1061 250 GLY A O 1665 N N . GLY A 210 ? 0.2867 0.3229 0.3929 0.0578 0.0673 -0.1057 251 GLY A N 1666 C CA . GLY A 210 ? 0.2830 0.3103 0.3756 0.0553 0.0636 -0.1056 251 GLY A CA 1667 C C . GLY A 210 ? 0.2861 0.3122 0.3740 0.0514 0.0577 -0.0990 251 GLY A C 1668 O O . GLY A 210 ? 0.2817 0.3014 0.3595 0.0489 0.0547 -0.0985 251 GLY A O 1669 N N . GLY A 211 ? 0.2763 0.3083 0.3717 0.0510 0.0557 -0.0942 252 GLY A N 1670 C CA . GLY A 211 ? 0.2546 0.2852 0.3445 0.0475 0.0505 -0.0881 252 GLY A CA 1671 C C . GLY A 211 ? 0.2515 0.2846 0.3304 0.0431 0.0530 -0.0866 252 GLY A C 1672 O O . GLY A 211 ? 0.2622 0.3007 0.3404 0.0427 0.0589 -0.0884 252 GLY A O 1673 N N . VAL A 212 ? 0.2558 0.2850 0.3265 0.0400 0.0487 -0.0829 253 VAL A N 1674 C CA . VAL A 212 ? 0.2476 0.2781 0.3073 0.0361 0.0499 -0.0812 253 VAL A CA 1675 C C . VAL A 212 ? 0.2423 0.2726 0.3002 0.0335 0.0448 -0.0751 253 VAL A C 1676 O O . VAL A 212 ? 0.2612 0.2869 0.3204 0.0340 0.0401 -0.0730 253 VAL A O 1677 C CB . VAL A 212 ? 0.2495 0.2736 0.2976 0.0349 0.0502 -0.0848 253 VAL A CB 1678 C CG1 . VAL A 212 ? 0.2806 0.3066 0.3171 0.0315 0.0519 -0.0834 253 VAL A CG1 1679 C CG2 . VAL A 212 ? 0.2683 0.2908 0.3174 0.0382 0.0546 -0.0916 253 VAL A CG2 1680 N N . GLN A 213 ? 0.2321 0.2672 0.2866 0.0309 0.0462 -0.0724 254 GLN A N 1681 C CA . GLN A 213 ? 0.2204 0.2559 0.2727 0.0285 0.0419 -0.0670 254 GLN A CA 1682 C C . GLN A 213 ? 0.2295 0.2608 0.2699 0.0255 0.0405 -0.0663 254 GLN A C 1683 O O . GLN A 213 ? 0.2503 0.2826 0.2829 0.0238 0.0436 -0.0676 254 GLN A O 1684 C CB . GLN A 213 ? 0.2162 0.2588 0.2719 0.0272 0.0442 -0.0648 254 GLN A CB 1685 C CG . GLN A 213 ? 0.2128 0.2559 0.2658 0.0249 0.0399 -0.0596 254 GLN A CG 1686 C CD . GLN A 213 ? 0.2348 0.2838 0.2898 0.0229 0.0424 -0.0577 254 GLN A CD 1687 O OE1 . GLN A 213 ? 0.2318 0.2804 0.2800 0.0202 0.0411 -0.0546 254 GLN A OE1 1688 N NE2 . GLN A 213 ? 0.2294 0.2839 0.2948 0.0243 0.0457 -0.0593 254 GLN A NE2 1689 N N . ARG A 214 ? 0.2298 0.2562 0.2689 0.0251 0.0359 -0.0644 255 ARG A N 1690 C CA . ARG A 214 ? 0.2363 0.2596 0.2665 0.0220 0.0336 -0.0630 255 ARG A CA 1691 C C . ARG A 214 ? 0.2315 0.2586 0.2588 0.0198 0.0325 -0.0584 255 ARG A C 1692 O O . ARG A 214 ? 0.2262 0.2573 0.2589 0.0205 0.0326 -0.0560 255 ARG A O 1693 C CB . ARG A 214 ? 0.2284 0.2460 0.2606 0.0222 0.0295 -0.0616 255 ARG A CB 1694 C CG . ARG A 214 ? 0.2357 0.2481 0.2696 0.0238 0.0300 -0.0665 255 ARG A CG 1695 C CD . ARG A 214 ? 0.2314 0.2384 0.2712 0.0250 0.0271 -0.0644 255 ARG A CD 1696 N NE . ARG A 214 ? 0.2574 0.2592 0.3007 0.0269 0.0276 -0.0690 255 ARG A NE 1697 C CZ . ARG A 214 ? 0.2713 0.2740 0.3205 0.0304 0.0297 -0.0716 255 ARG A CZ 1698 N NH1 . ARG A 214 ? 0.2710 0.2798 0.3235 0.0320 0.0313 -0.0702 255 ARG A NH1 1699 N NH2 . ARG A 214 ? 0.2690 0.2662 0.3214 0.0323 0.0300 -0.0759 255 ARG A NH2 1700 N N . GLY A 215 ? 0.2289 0.2543 0.2481 0.0172 0.0310 -0.0574 256 GLY A N 1701 C CA . GLY A 215 ? 0.2304 0.2581 0.2472 0.0152 0.0291 -0.0528 256 GLY A CA 1702 C C . GLY A 215 ? 0.2488 0.2758 0.2562 0.0127 0.0286 -0.0527 256 GLY A C 1703 O O . GLY A 215 ? 0.2381 0.2643 0.2396 0.0126 0.0309 -0.0560 256 GLY A O 1704 N N . ASN A 216 ? 0.2304 0.2576 0.2359 0.0111 0.0257 -0.0489 257 ASN A N 1705 C CA . ASN A 216 ? 0.2389 0.2654 0.2358 0.0090 0.0245 -0.0487 257 ASN A CA 1706 C C . ASN A 216 ? 0.2312 0.2606 0.2232 0.0082 0.0274 -0.0477 257 ASN A C 1707 O O . ASN A 216 ? 0.2306 0.2634 0.2274 0.0087 0.0297 -0.0461 257 ASN A O 1708 C CB . ASN A 216 ? 0.2359 0.2615 0.2331 0.0077 0.0205 -0.0452 257 ASN A CB 1709 C CG . ASN A 216 ? 0.2604 0.2891 0.2582 0.0073 0.0202 -0.0410 257 ASN A CG 1710 O OD1 . ASN A 216 ? 0.2738 0.3040 0.2664 0.0061 0.0209 -0.0399 257 ASN A OD1 1711 N ND2 . ASN A 216 ? 0.2753 0.3042 0.2788 0.0083 0.0188 -0.0384 257 ASN A ND2 1712 N N . ILE A 217 ? 0.2480 0.2757 0.2304 0.0071 0.0272 -0.0486 258 ILE A N 1713 C CA . ILE A 217 ? 0.2508 0.2799 0.2266 0.0064 0.0306 -0.0474 258 ILE A CA 1714 C C . ILE A 217 ? 0.2651 0.2934 0.2342 0.0047 0.0275 -0.0442 258 ILE A C 1715 O O . ILE A 217 ? 0.2880 0.3153 0.2479 0.0042 0.0291 -0.0436 258 ILE A O 1716 C CB . ILE A 217 ? 0.2589 0.2861 0.2270 0.0075 0.0344 -0.0516 258 ILE A CB 1717 C CG1 . ILE A 217 ? 0.2666 0.2893 0.2287 0.0078 0.0304 -0.0553 258 ILE A CG1 1718 C CG2 . ILE A 217 ? 0.2772 0.3066 0.2532 0.0094 0.0389 -0.0542 258 ILE A CG2 1719 C CD1 . ILE A 217 ? 0.3283 0.3480 0.2785 0.0091 0.0332 -0.0594 258 ILE A CD1 1720 N N . LEU A 218 ? 0.2756 0.3039 0.2489 0.0042 0.0233 -0.0420 259 LEU A N 1721 C CA . LEU A 218 ? 0.3006 0.3283 0.2692 0.0029 0.0199 -0.0391 259 LEU A CA 1722 C C . LEU A 218 ? 0.3088 0.3387 0.2776 0.0021 0.0215 -0.0352 259 LEU A C 1723 O O . LEU A 218 ? 0.3343 0.3668 0.3101 0.0024 0.0237 -0.0342 259 LEU A O 1724 C CB . LEU A 218 ? 0.3003 0.3279 0.2751 0.0027 0.0157 -0.0378 259 LEU A CB 1725 C CG . LEU A 218 ? 0.3278 0.3530 0.3041 0.0028 0.0130 -0.0409 259 LEU A CG 1726 C CD1 . LEU A 218 ? 0.3713 0.3968 0.3552 0.0026 0.0106 -0.0385 259 LEU A CD1 1727 C CD2 . LEU A 218 ? 0.3615 0.3846 0.3299 0.0022 0.0102 -0.0428 259 LEU A CD2 1728 N N . ASN A 219 ? 0.3149 0.3435 0.2766 0.0012 0.0197 -0.0330 260 ASN A N 1729 C CA A ASN A 219 ? 0.3113 0.3411 0.2739 0.0002 0.0203 -0.0290 260 ASN A CA 1730 C CA B ASN A 219 ? 0.3216 0.3513 0.2835 0.0002 0.0204 -0.0290 260 ASN A CA 1731 C C . ASN A 219 ? 0.3044 0.3334 0.2665 -0.0001 0.0153 -0.0268 260 ASN A C 1732 O O . ASN A 219 ? 0.3242 0.3512 0.2790 -0.0005 0.0135 -0.0253 260 ASN A O 1733 C CB A ASN A 219 ? 0.3289 0.3575 0.2832 -0.0004 0.0241 -0.0278 260 ASN A CB 1734 C CB B ASN A 219 ? 0.3419 0.3696 0.2938 -0.0003 0.0235 -0.0282 260 ASN A CB 1735 C CG A ASN A 219 ? 0.3338 0.3642 0.2911 -0.0001 0.0303 -0.0293 260 ASN A CG 1736 C CG B ASN A 219 ? 0.3898 0.4177 0.3414 -0.0015 0.0243 -0.0238 260 ASN A CG 1737 O OD1 A ASN A 219 ? 0.3815 0.4149 0.3469 -0.0007 0.0327 -0.0277 260 ASN A OD1 1738 O OD1 B ASN A 219 ? 0.4280 0.4582 0.3883 -0.0019 0.0238 -0.0221 260 ASN A OD1 1739 N ND2 A ASN A 219 ? 0.3124 0.3412 0.2635 0.0008 0.0327 -0.0326 260 ASN A ND2 1740 N ND2 B ASN A 219 ? 0.4264 0.4511 0.3674 -0.0019 0.0254 -0.0219 260 ASN A ND2 1741 N N . LEU A 220 ? 0.2865 0.3169 0.2563 0.0005 0.0131 -0.0266 261 LEU A N 1742 C CA . LEU A 220 ? 0.2750 0.3048 0.2456 0.0005 0.0089 -0.0251 261 LEU A CA 1743 C C . LEU A 220 ? 0.2786 0.3091 0.2500 0.0003 0.0081 -0.0216 261 LEU A C 1744 O O . LEU A 220 ? 0.2532 0.2831 0.2237 0.0004 0.0049 -0.0201 261 LEU A O 1745 C CB . LEU A 220 ? 0.2895 0.3201 0.2678 0.0014 0.0079 -0.0257 261 LEU A CB 1746 C CG . LEU A 220 ? 0.2949 0.3242 0.2742 0.0015 0.0078 -0.0291 261 LEU A CG 1747 C CD1 . LEU A 220 ? 0.3080 0.3374 0.2951 0.0024 0.0079 -0.0288 261 LEU A CD1 1748 C CD2 . LEU A 220 ? 0.3061 0.3341 0.2819 0.0008 0.0044 -0.0303 261 LEU A CD2 1749 N N . ASN A 221 ? 0.2497 0.2813 0.2236 0.0001 0.0107 -0.0205 262 ASN A N 1750 C CA . ASN A 221 ? 0.2513 0.2831 0.2270 -0.0001 0.0097 -0.0177 262 ASN A CA 1751 C C . ASN A 221 ? 0.2403 0.2722 0.2193 0.0011 0.0064 -0.0168 262 ASN A C 1752 O O . ASN A 221 ? 0.2492 0.2802 0.2267 0.0011 0.0042 -0.0148 262 ASN A O 1753 C CB . ASN A 221 ? 0.2583 0.2880 0.2273 -0.0013 0.0097 -0.0155 262 ASN A CB 1754 C CG . ASN A 221 ? 0.2859 0.3154 0.2519 -0.0024 0.0142 -0.0156 262 ASN A CG 1755 O OD1 . ASN A 221 ? 0.2992 0.3308 0.2711 -0.0025 0.0172 -0.0164 262 ASN A OD1 1756 N ND2 . ASN A 221 ? 0.3324 0.3590 0.2890 -0.0029 0.0148 -0.0147 262 ASN A ND2 1757 N N . GLY A 222 ? 0.2215 0.2541 0.2045 0.0023 0.0063 -0.0181 263 GLY A N 1758 C CA . GLY A 222 ? 0.2176 0.2502 0.2037 0.0038 0.0043 -0.0170 263 GLY A CA 1759 C C . GLY A 222 ? 0.2034 0.2355 0.1888 0.0039 0.0026 -0.0169 263 GLY A C 1760 O O . GLY A 222 ? 0.2180 0.2500 0.2057 0.0052 0.0017 -0.0157 263 GLY A O 1761 N N . ALA A 223 ? 0.1990 0.2307 0.1818 0.0027 0.0023 -0.0184 264 ALA A N 1762 C CA . ALA A 223 ? 0.1976 0.2293 0.1813 0.0026 -0.0001 -0.0185 264 ALA A CA 1763 C C . ALA A 223 ? 0.2116 0.2434 0.2011 0.0031 0.0006 -0.0193 264 ALA A C 1764 O O . ALA A 223 ? 0.2486 0.2811 0.2417 0.0033 -0.0008 -0.0187 264 ALA A O 1765 C CB . ALA A 223 ? 0.2194 0.2502 0.1980 0.0014 -0.0018 -0.0202 264 ALA A CB 1766 N N . GLY A 224 ? 0.2228 0.2541 0.2141 0.0034 0.0027 -0.0205 265 GLY A N 1767 C CA . GLY A 224 ? 0.2154 0.2459 0.2120 0.0037 0.0035 -0.0212 265 GLY A CA 1768 C C . GLY A 224 ? 0.2167 0.2465 0.2140 0.0022 0.0023 -0.0242 265 GLY A C 1769 O O . GLY A 224 ? 0.2396 0.2691 0.2321 0.0015 0.0018 -0.0265 265 GLY A O 1770 N N . ASP A 225 ? 0.2012 0.2307 0.2045 0.0017 0.0018 -0.0245 266 ASP A N 1771 C CA . ASP A 225 ? 0.2198 0.2485 0.2249 0.0002 -0.0002 -0.0281 266 ASP A CA 1772 C C . ASP A 225 ? 0.2400 0.2694 0.2386 -0.0004 -0.0035 -0.0297 266 ASP A C 1773 O O . ASP A 225 ? 0.2379 0.2688 0.2356 -0.0003 -0.0055 -0.0279 266 ASP A O 1774 C CB . ASP A 225 ? 0.2390 0.2682 0.2532 -0.0005 -0.0008 -0.0274 266 ASP A CB 1775 C CG . ASP A 225 ? 0.2515 0.2804 0.2689 -0.0021 -0.0042 -0.0313 266 ASP A CG 1776 O OD1 . ASP A 225 ? 0.2480 0.2748 0.2627 -0.0025 -0.0048 -0.0349 266 ASP A OD1 1777 O OD2 . ASP A 225 ? 0.2320 0.2629 0.2553 -0.0029 -0.0064 -0.0310 266 ASP A OD2 1778 N N . PRO A 226 ? 0.2624 0.2901 0.2560 -0.0008 -0.0042 -0.0332 267 PRO A N 1779 C CA . PRO A 226 ? 0.2773 0.3046 0.2625 -0.0009 -0.0070 -0.0344 267 PRO A CA 1780 C C . PRO A 226 ? 0.2603 0.2884 0.2476 -0.0014 -0.0121 -0.0351 267 PRO A C 1781 O O . PRO A 226 ? 0.2811 0.3089 0.2614 -0.0009 -0.0148 -0.0346 267 PRO A O 1782 C CB . PRO A 226 ? 0.2964 0.3212 0.2765 -0.0008 -0.0065 -0.0387 267 PRO A CB 1783 C CG . PRO A 226 ? 0.3032 0.3277 0.2877 -0.0004 -0.0023 -0.0386 267 PRO A CG 1784 C CD . PRO A 226 ? 0.2662 0.2920 0.2601 -0.0005 -0.0016 -0.0356 267 PRO A CD 1785 N N . LEU A 227 ? 0.2383 0.2672 0.2358 -0.0022 -0.0132 -0.0362 268 LEU A N 1786 C CA . LEU A 227 ? 0.2473 0.2776 0.2496 -0.0027 -0.0183 -0.0376 268 LEU A CA 1787 C C . LEU A 227 ? 0.2188 0.2522 0.2270 -0.0024 -0.0185 -0.0338 268 LEU A C 1788 O O . LEU A 227 ? 0.2258 0.2610 0.2375 -0.0024 -0.0230 -0.0347 268 LEU A O 1789 C CB . LEU A 227 ? 0.2320 0.2617 0.2438 -0.0041 -0.0199 -0.0413 268 LEU A CB 1790 C CG . LEU A 227 ? 0.2684 0.2945 0.2747 -0.0041 -0.0202 -0.0458 268 LEU A CG 1791 C CD1 . LEU A 227 ? 0.2938 0.3192 0.3112 -0.0056 -0.0225 -0.0495 268 LEU A CD1 1792 C CD2 . LEU A 227 ? 0.3067 0.3311 0.3000 -0.0031 -0.0240 -0.0484 268 LEU A CD2 1793 N N . THR A 228 ? 0.2140 0.2481 0.2233 -0.0017 -0.0140 -0.0299 269 THR A N 1794 C CA . THR A 228 ? 0.2120 0.2488 0.2273 -0.0010 -0.0135 -0.0267 269 THR A CA 1795 C C . THR A 228 ? 0.2151 0.2518 0.2242 0.0005 -0.0112 -0.0233 269 THR A C 1796 O O . THR A 228 ? 0.2023 0.2398 0.2150 0.0015 -0.0081 -0.0206 269 THR A O 1797 C CB . THR A 228 ? 0.1975 0.2350 0.2238 -0.0014 -0.0098 -0.0256 269 THR A CB 1798 O OG1 . THR A 228 ? 0.1930 0.2281 0.2163 -0.0009 -0.0055 -0.0245 269 THR A OG1 1799 C CG2 . THR A 228 ? 0.2198 0.2578 0.2557 -0.0033 -0.0124 -0.0291 269 THR A CG2 1800 N N . PRO A 229 ? 0.2227 0.2580 0.2222 0.0008 -0.0128 -0.0232 270 PRO A N 1801 C CA . PRO A 229 ? 0.2171 0.2520 0.2122 0.0019 -0.0107 -0.0202 270 PRO A CA 1802 C C . PRO A 229 ? 0.2186 0.2552 0.2176 0.0032 -0.0114 -0.0178 270 PRO A C 1803 O O . PRO A 229 ? 0.2383 0.2761 0.2392 0.0033 -0.0149 -0.0181 270 PRO A O 1804 C CB . PRO A 229 ? 0.2358 0.2687 0.2208 0.0017 -0.0122 -0.0205 270 PRO A CB 1805 C CG . PRO A 229 ? 0.2374 0.2700 0.2214 0.0012 -0.0168 -0.0232 270 PRO A CG 1806 C CD . PRO A 229 ? 0.2491 0.2828 0.2412 0.0003 -0.0163 -0.0258 270 PRO A CD 1807 N N . GLY A 230 ? 0.2205 0.2571 0.2209 0.0043 -0.0081 -0.0156 271 GLY A N 1808 C CA . GLY A 230 ? 0.2170 0.2549 0.2206 0.0060 -0.0080 -0.0135 271 GLY A CA 1809 C C . GLY A 230 ? 0.2265 0.2661 0.2383 0.0067 -0.0055 -0.0129 271 GLY A C 1810 O O . GLY A 230 ? 0.2375 0.2777 0.2510 0.0086 -0.0041 -0.0110 271 GLY A O 1811 N N . TYR A 231 ? 0.2129 0.2533 0.2306 0.0052 -0.0051 -0.0144 272 TYR A N 1812 C CA . TYR A 231 ? 0.2014 0.2436 0.2288 0.0054 -0.0025 -0.0135 272 TYR A CA 1813 C C . TYR A 231 ? 0.1898 0.2303 0.2202 0.0042 0.0004 -0.0140 272 TYR A C 1814 O O . TYR A 231 ? 0.2009 0.2399 0.2285 0.0028 -0.0011 -0.0163 272 TYR A O 1815 C CB . TYR A 231 ? 0.1977 0.2431 0.2332 0.0043 -0.0063 -0.0152 272 TYR A CB 1816 C CG . TYR A 231 ? 0.2158 0.2622 0.2476 0.0056 -0.0098 -0.0148 272 TYR A CG 1817 C CD1 . TYR A 231 ? 0.2192 0.2670 0.2536 0.0078 -0.0080 -0.0126 272 TYR A CD1 1818 C CD2 . TYR A 231 ? 0.2332 0.2783 0.2578 0.0051 -0.0145 -0.0163 272 TYR A CD2 1819 C CE1 . TYR A 231 ? 0.2063 0.2542 0.2372 0.0093 -0.0113 -0.0121 272 TYR A CE1 1820 C CE2 . TYR A 231 ? 0.2278 0.2726 0.2480 0.0064 -0.0174 -0.0154 272 TYR A CE2 1821 C CZ . TYR A 231 ? 0.2164 0.2626 0.2403 0.0085 -0.0161 -0.0134 272 TYR A CZ 1822 O OH . TYR A 231 ? 0.2229 0.2684 0.2429 0.0100 -0.0194 -0.0125 272 TYR A OH 1823 N N . PRO A 232 ? 0.1989 0.2392 0.2348 0.0050 0.0049 -0.0117 273 PRO A N 1824 C CA . PRO A 232 ? 0.1953 0.2331 0.2338 0.0041 0.0077 -0.0118 273 PRO A CA 1825 C C . PRO A 232 ? 0.2024 0.2412 0.2498 0.0013 0.0056 -0.0147 273 PRO A C 1826 O O . PRO A 232 ? 0.1951 0.2372 0.2509 0.0003 0.0039 -0.0155 273 PRO A O 1827 C CB . PRO A 232 ? 0.1972 0.2340 0.2386 0.0060 0.0133 -0.0080 273 PRO A CB 1828 C CG . PRO A 232 ? 0.2134 0.2541 0.2596 0.0068 0.0131 -0.0071 273 PRO A CG 1829 C CD . PRO A 232 ? 0.2112 0.2529 0.2502 0.0071 0.0080 -0.0089 273 PRO A CD 1830 N N . ALA A 233 ? 0.1974 0.2334 0.2436 0.0002 0.0057 -0.0164 274 ALA A N 1831 C CA . ALA A 233 ? 0.2014 0.2373 0.2550 -0.0024 0.0033 -0.0199 274 ALA A CA 1832 C C . ALA A 233 ? 0.2196 0.2550 0.2853 -0.0034 0.0073 -0.0182 274 ALA A C 1833 O O . ALA A 233 ? 0.2311 0.2630 0.2996 -0.0043 0.0093 -0.0185 274 ALA A O 1834 C CB . ALA A 233 ? 0.2215 0.2539 0.2679 -0.0026 0.0024 -0.0226 274 ALA A CB 1835 N N . ASN A 234 ? 0.2175 0.2561 0.2904 -0.0032 0.0089 -0.0160 275 ASN A N 1836 C CA . ASN A 234 ? 0.2417 0.2804 0.3269 -0.0042 0.0138 -0.0135 275 ASN A CA 1837 C C . ASN A 234 ? 0.2599 0.3008 0.3592 -0.0075 0.0104 -0.0172 275 ASN A C 1838 O O . ASN A 234 ? 0.2582 0.2993 0.3554 -0.0087 0.0042 -0.0219 275 ASN A O 1839 C CB . ASN A 234 ? 0.2602 0.3014 0.3467 -0.0020 0.0179 -0.0095 275 ASN A CB 1840 C CG . ASN A 234 ? 0.2530 0.2996 0.3425 -0.0020 0.0133 -0.0114 275 ASN A CG 1841 O OD1 . ASN A 234 ? 0.2699 0.3189 0.3654 -0.0040 0.0078 -0.0153 275 ASN A OD1 1842 N ND2 . ASN A 234 ? 0.2968 0.3450 0.3821 0.0008 0.0155 -0.0087 275 ASN A ND2 1843 N N . GLU A 235 ? 0.2782 0.3203 0.3917 -0.0089 0.0146 -0.0152 276 GLU A N 1844 C CA A GLU A 235 ? 0.2989 0.3426 0.4279 -0.0123 0.0115 -0.0188 276 GLU A CA 1845 C CA B GLU A 235 ? 0.3076 0.3517 0.4376 -0.0123 0.0121 -0.0184 276 GLU A CA 1846 C C . GLU A 235 ? 0.3036 0.3529 0.4378 -0.0130 0.0042 -0.0230 276 GLU A C 1847 O O . GLU A 235 ? 0.3447 0.3943 0.4862 -0.0154 -0.0015 -0.0280 276 GLU A O 1848 C CB A GLU A 235 ? 0.3144 0.3585 0.4594 -0.0139 0.0183 -0.0153 276 GLU A CB 1849 C CB B GLU A 235 ? 0.3227 0.3685 0.4684 -0.0133 0.0192 -0.0143 276 GLU A CB 1850 C CG A GLU A 235 ? 0.3321 0.3698 0.4768 -0.0145 0.0234 -0.0129 276 GLU A CG 1851 C CG B GLU A 235 ? 0.3701 0.4190 0.5127 -0.0104 0.0239 -0.0098 276 GLU A CG 1852 C CD A GLU A 235 ? 0.3208 0.3558 0.4727 -0.0177 0.0190 -0.0179 276 GLU A CD 1853 C CD B GLU A 235 ? 0.4067 0.4614 0.5676 -0.0115 0.0272 -0.0085 276 GLU A CD 1854 O OE1 A GLU A 235 ? 0.3747 0.4131 0.5348 -0.0198 0.0121 -0.0233 276 GLU A OE1 1855 O OE1 B GLU A 235 ? 0.4480 0.5059 0.6252 -0.0147 0.0237 -0.0119 276 GLU A OE1 1856 O OE2 A GLU A 235 ? 0.3234 0.3525 0.4729 -0.0177 0.0222 -0.0164 276 GLU A OE2 1857 O OE2 B GLU A 235 ? 0.4343 0.4904 0.5931 -0.0089 0.0333 -0.0041 276 GLU A OE2 1858 N N . TYR A 236 ? 0.2737 0.3268 0.4042 -0.0108 0.0038 -0.0214 277 TYR A N 1859 C CA . TYR A 236 ? 0.2881 0.3462 0.4239 -0.0111 -0.0034 -0.0249 277 TYR A CA 1860 C C . TYR A 236 ? 0.2896 0.3469 0.4092 -0.0091 -0.0093 -0.0268 277 TYR A C 1861 O O . TYR A 236 ? 0.3043 0.3651 0.4253 -0.0084 -0.0151 -0.0289 277 TYR A O 1862 C CB . TYR A 236 ? 0.2788 0.3425 0.4269 -0.0104 -0.0001 -0.0222 277 TYR A CB 1863 C CG . TYR A 236 ? 0.2765 0.3396 0.4140 -0.0071 0.0054 -0.0175 277 TYR A CG 1864 C CD1 . TYR A 236 ? 0.2940 0.3582 0.4207 -0.0045 0.0014 -0.0178 277 TYR A CD1 1865 C CD2 . TYR A 236 ? 0.2737 0.3342 0.4108 -0.0062 0.0144 -0.0126 277 TYR A CD2 1866 C CE1 . TYR A 236 ? 0.3138 0.3770 0.4307 -0.0014 0.0060 -0.0139 277 TYR A CE1 1867 C CE2 . TYR A 236 ? 0.3026 0.3618 0.4285 -0.0028 0.0189 -0.0088 277 TYR A CE2 1868 C CZ . TYR A 236 ? 0.3063 0.3671 0.4227 -0.0005 0.0143 -0.0098 277 TYR A CZ 1869 O OH . TYR A 236 ? 0.3657 0.4249 0.4715 0.0029 0.0182 -0.0066 277 TYR A OH 1870 N N . ALA A 237 ? 0.2844 0.3369 0.3892 -0.0082 -0.0080 -0.0262 278 ALA A N 1871 C CA . ALA A 237 ? 0.3014 0.3526 0.3907 -0.0064 -0.0120 -0.0271 278 ALA A CA 1872 C C . ALA A 237 ? 0.3119 0.3636 0.4003 -0.0073 -0.0203 -0.0323 278 ALA A C 1873 O O . ALA A 237 ? 0.3281 0.3790 0.4236 -0.0094 -0.0228 -0.0360 278 ALA A O 1874 C CB . ALA A 237 ? 0.3063 0.3526 0.3828 -0.0058 -0.0089 -0.0261 278 ALA A CB 1875 N N . TYR A 238 ? 0.3187 0.3715 0.3990 -0.0055 -0.0248 -0.0325 279 TYR A N 1876 C CA . TYR A 238 ? 0.3316 0.3833 0.4058 -0.0055 -0.0327 -0.0369 279 TYR A CA 1877 C C . TYR A 238 ? 0.3164 0.3632 0.3738 -0.0049 -0.0316 -0.0372 279 TYR A C 1878 O O . TYR A 238 ? 0.3472 0.3926 0.3960 -0.0037 -0.0270 -0.0336 279 TYR A O 1879 C CB . TYR A 238 ? 0.3617 0.4163 0.4349 -0.0037 -0.0383 -0.0369 279 TYR A CB 1880 C CG A TYR A 238 ? 0.3391 0.3927 0.4088 -0.0036 -0.0474 -0.0418 279 TYR A CG 1881 C CG B TYR A 238 ? 0.3879 0.4387 0.4435 -0.0022 -0.0435 -0.0383 279 TYR A CG 1882 C CD1 A TYR A 238 ? 0.3761 0.4319 0.4594 -0.0052 -0.0522 -0.0463 279 TYR A CD1 1883 C CD1 B TYR A 238 ? 0.4339 0.4844 0.4880 -0.0017 -0.0520 -0.0425 279 TYR A CD1 1884 C CD2 A TYR A 238 ? 0.3831 0.4330 0.4356 -0.0017 -0.0510 -0.0421 279 TYR A CD2 1885 C CD2 B TYR A 238 ? 0.4245 0.4717 0.4653 -0.0011 -0.0398 -0.0356 279 TYR A CD2 1886 C CE1 A TYR A 238 ? 0.4063 0.4606 0.4853 -0.0046 -0.0612 -0.0513 279 TYR A CE1 1887 C CE1 B TYR A 238 ? 0.4535 0.4996 0.4901 0.0000 -0.0559 -0.0433 279 TYR A CE1 1888 C CE2 A TYR A 238 ? 0.3818 0.4299 0.4289 -0.0011 -0.0593 -0.0465 279 TYR A CE2 1889 C CE2 B TYR A 238 ? 0.4541 0.4975 0.4794 0.0000 -0.0433 -0.0363 279 TYR A CE2 1890 C CZ A TYR A 238 ? 0.4086 0.4588 0.4685 -0.0023 -0.0647 -0.0513 279 TYR A CZ 1891 C CZ B TYR A 238 ? 0.4733 0.5160 0.4958 0.0007 -0.0511 -0.0400 279 TYR A CZ 1892 O OH A TYR A 238 ? 0.4499 0.4978 0.5033 -0.0013 -0.0736 -0.0561 279 TYR A OH 1893 O OH B TYR A 238 ? 0.4991 0.5374 0.5048 0.0022 -0.0540 -0.0402 279 TYR A OH 1894 N N . ARG A 239 ? 0.2918 0.3358 0.3457 -0.0058 -0.0352 -0.0417 280 ARG A N 1895 C CA . ARG A 239 ? 0.2917 0.3313 0.3308 -0.0052 -0.0336 -0.0423 280 ARG A CA 1896 C C . ARG A 239 ? 0.3225 0.3599 0.3485 -0.0039 -0.0394 -0.0447 280 ARG A C 1897 O O . ARG A 239 ? 0.3190 0.3568 0.3474 -0.0039 -0.0462 -0.0486 280 ARG A O 1898 C CB A ARG A 239 ? 0.2956 0.3324 0.3385 -0.0068 -0.0322 -0.0456 280 ARG A CB 1899 C CB B ARG A 239 ? 0.2872 0.3241 0.3299 -0.0068 -0.0323 -0.0456 280 ARG A CB 1900 C CG A ARG A 239 ? 0.2826 0.3185 0.3296 -0.0073 -0.0245 -0.0423 280 ARG A CG 1901 C CG B ARG A 239 ? 0.2608 0.2983 0.3137 -0.0078 -0.0258 -0.0424 280 ARG A CG 1902 C CD A ARG A 239 ? 0.3130 0.3518 0.3757 -0.0085 -0.0213 -0.0395 280 ARG A CD 1903 C CD B ARG A 239 ? 0.1931 0.2270 0.2480 -0.0089 -0.0238 -0.0450 280 ARG A CD 1904 N NE A ARG A 239 ? 0.2838 0.3205 0.3481 -0.0084 -0.0143 -0.0361 280 ARG A NE 1905 N NE B ARG A 239 ? 0.2185 0.2520 0.2793 -0.0091 -0.0170 -0.0407 280 ARG A NE 1906 C CZ A ARG A 239 ? 0.2854 0.3230 0.3613 -0.0092 -0.0100 -0.0333 280 ARG A CZ 1907 C CZ B ARG A 239 ? 0.1933 0.2287 0.2675 -0.0103 -0.0145 -0.0385 280 ARG A CZ 1908 N NH1 A ARG A 239 ? 0.3095 0.3508 0.3983 -0.0105 -0.0117 -0.0337 280 ARG A NH1 1909 N NH1 B ARG A 239 ? 0.2143 0.2529 0.3004 -0.0118 -0.0184 -0.0405 280 ARG A NH1 1910 N NH2 A ARG A 239 ? 0.2213 0.2562 0.2964 -0.0086 -0.0040 -0.0299 280 ARG A NH2 1911 N NH2 B ARG A 239 ? 0.2373 0.2712 0.3134 -0.0099 -0.0080 -0.0343 280 ARG A NH2 1912 N N . ARG A 240 ? 0.3157 0.3506 0.3276 -0.0027 -0.0367 -0.0426 281 ARG A N 1913 C CA . ARG A 240 ? 0.3585 0.3899 0.3558 -0.0014 -0.0409 -0.0449 281 ARG A CA 1914 C C . ARG A 240 ? 0.3786 0.4071 0.3740 -0.0019 -0.0435 -0.0506 281 ARG A C 1915 O O . ARG A 240 ? 0.3745 0.4024 0.3760 -0.0032 -0.0400 -0.0521 281 ARG A O 1916 C CB . ARG A 240 ? 0.3539 0.3829 0.3383 -0.0005 -0.0360 -0.0417 281 ARG A CB 1917 C CG . ARG A 240 ? 0.3705 0.4015 0.3553 0.0003 -0.0344 -0.0367 281 ARG A CG 1918 C CD . ARG A 240 ? 0.3846 0.4130 0.3574 0.0009 -0.0303 -0.0338 281 ARG A CD 1919 N NE . ARG A 240 ? 0.3992 0.4287 0.3719 0.0018 -0.0301 -0.0295 281 ARG A NE 1920 C CZ . ARG A 240 ? 0.4560 0.4833 0.4196 0.0023 -0.0278 -0.0265 281 ARG A CZ 1921 N NH1 . ARG A 240 ? 0.4646 0.4890 0.4185 0.0021 -0.0251 -0.0270 281 ARG A NH1 1922 N NH2 . ARG A 240 ? 0.4802 0.5082 0.4450 0.0031 -0.0279 -0.0229 281 ARG A NH2 1923 N N . GLY A 241 ? 0.4149 0.4410 0.4012 -0.0006 -0.0500 -0.0539 282 GLY A N 1924 C CA . GLY A 241 ? 0.4540 0.4759 0.4330 -0.0002 -0.0526 -0.0596 282 GLY A CA 1925 C C . GLY A 241 ? 0.4734 0.4923 0.4406 0.0003 -0.0457 -0.0583 282 GLY A C 1926 O O . GLY A 241 ? 0.4711 0.4902 0.4315 0.0009 -0.0413 -0.0535 282 GLY A O 1927 N N . ILE A 242 ? 0.5030 0.5191 0.4690 0.0001 -0.0447 -0.0629 283 ILE A N 1928 C CA . ILE A 242 ? 0.5206 0.5341 0.4767 0.0007 -0.0381 -0.0623 283 ILE A CA 1929 C C . ILE A 242 ? 0.5307 0.5416 0.4690 0.0027 -0.0368 -0.0602 283 ILE A C 1930 O O . ILE A 242 ? 0.5357 0.5469 0.4698 0.0028 -0.0301 -0.0566 283 ILE A O 1931 C CB A ILE A 242 ? 0.5282 0.5385 0.4851 0.0007 -0.0381 -0.0685 283 ILE A CB 1932 C CB B ILE A 242 ? 0.5266 0.5367 0.4826 0.0008 -0.0382 -0.0685 283 ILE A CB 1933 C CG1 A ILE A 242 ? 0.5307 0.5400 0.4839 0.0011 -0.0302 -0.0674 283 ILE A CG1 1934 C CG1 B ILE A 242 ? 0.5205 0.5325 0.4936 -0.0013 -0.0356 -0.0686 283 ILE A CG1 1935 C CG2 A ILE A 242 ? 0.5479 0.5539 0.4935 0.0025 -0.0449 -0.0746 283 ILE A CG2 1936 C CG2 B ILE A 242 ? 0.5368 0.5438 0.4793 0.0024 -0.0324 -0.0689 283 ILE A CG2 1937 C CD1 A ILE A 242 ? 0.5062 0.5186 0.4730 -0.0005 -0.0251 -0.0636 283 ILE A CD1 1938 C CD1 B ILE A 242 ? 0.5003 0.5141 0.4763 -0.0017 -0.0276 -0.0636 283 ILE A CD1 1939 N N . ALA A 243 ? 0.5474 0.5558 0.4756 0.0044 -0.0432 -0.0621 284 ALA A N 1940 C CA . ALA A 243 ? 0.5641 0.5689 0.4742 0.0065 -0.0418 -0.0594 284 ALA A CA 1941 C C . ALA A 243 ? 0.5580 0.5653 0.4693 0.0060 -0.0384 -0.0523 284 ALA A C 1942 O O . ALA A 243 ? 0.5645 0.5693 0.4635 0.0070 -0.0347 -0.0490 284 ALA A O 1943 C CB . ALA A 243 ? 0.5853 0.5861 0.4836 0.0088 -0.0503 -0.0629 284 ALA A CB 1944 N N . GLU A 244 ? 0.5371 0.5491 0.4633 0.0045 -0.0395 -0.0500 285 GLU A N 1945 C CA . GLU A 244 ? 0.5292 0.5434 0.4576 0.0042 -0.0367 -0.0438 285 GLU A CA 1946 C C . GLU A 244 ? 0.5047 0.5222 0.4433 0.0025 -0.0298 -0.0413 285 GLU A C 1947 O O . GLU A 244 ? 0.5111 0.5305 0.4528 0.0022 -0.0274 -0.0367 285 GLU A O 1948 C CB . GLU A 244 ? 0.5373 0.5541 0.4737 0.0044 -0.0430 -0.0428 285 GLU A CB 1949 C CG . GLU A 244 ? 0.5962 0.6095 0.5207 0.0067 -0.0498 -0.0433 285 GLU A CG 1950 C CD . GLU A 244 ? 0.6994 0.7104 0.6207 0.0076 -0.0565 -0.0498 285 GLU A CD 1951 O OE1 . GLU A 244 ? 0.7107 0.7247 0.6457 0.0062 -0.0589 -0.0537 285 GLU A OE1 1952 O OE2 . GLU A 244 ? 0.7580 0.7637 0.6625 0.0099 -0.0595 -0.0511 285 GLU A OE2 1953 N N . ALA A 245 ? 0.4855 0.5031 0.4286 0.0017 -0.0270 -0.0444 286 ALA A N 1954 C CA . ALA A 245 ? 0.4747 0.4949 0.4272 0.0006 -0.0212 -0.0422 286 ALA A CA 1955 C C . ALA A 245 ? 0.4770 0.4970 0.4234 0.0009 -0.0158 -0.0382 286 ALA A C 1956 O O . ALA A 245 ? 0.4938 0.5111 0.4283 0.0017 -0.0147 -0.0379 286 ALA A O 1957 C CB . ALA A 245 ? 0.4619 0.4813 0.4188 0.0001 -0.0193 -0.0461 286 ALA A CB 1958 N N . VAL A 246 ? 0.4458 0.4685 0.4005 0.0003 -0.0125 -0.0351 287 VAL A N 1959 C CA . VAL A 246 ? 0.4394 0.4625 0.3910 0.0003 -0.0079 -0.0316 287 VAL A CA 1960 C C . VAL A 246 ? 0.4372 0.4600 0.3885 0.0003 -0.0030 -0.0333 287 VAL A C 1961 O O . VAL A 246 ? 0.4342 0.4578 0.3929 0.0002 -0.0021 -0.0353 287 VAL A O 1962 C CB . VAL A 246 ? 0.4290 0.4548 0.3894 0.0001 -0.0072 -0.0281 287 VAL A CB 1963 C CG1 . VAL A 246 ? 0.4249 0.4510 0.3837 0.0001 -0.0030 -0.0252 287 VAL A CG1 1964 C CG2 . VAL A 246 ? 0.4479 0.4742 0.4092 0.0005 -0.0118 -0.0265 287 VAL A CG2 1965 N N . GLY A 247 ? 0.4372 0.4586 0.3803 0.0006 0.0005 -0.0324 288 GLY A N 1966 C CA . GLY A 247 ? 0.4158 0.4382 0.3609 0.0006 0.0061 -0.0330 288 GLY A CA 1967 C C . GLY A 247 ? 0.4166 0.4375 0.3588 0.0013 0.0083 -0.0375 288 GLY A C 1968 O O . GLY A 247 ? 0.3990 0.4212 0.3446 0.0016 0.0129 -0.0381 288 GLY A O 1969 N N . LEU A 248 ? 0.4082 0.4264 0.3448 0.0018 0.0046 -0.0409 289 LEU A N 1970 C CA . LEU A 248 ? 0.4054 0.4215 0.3389 0.0028 0.0058 -0.0461 289 LEU A CA 1971 C C . LEU A 248 ? 0.4178 0.4318 0.3393 0.0039 0.0102 -0.0467 289 LEU A C 1972 O O . LEU A 248 ? 0.4320 0.4437 0.3427 0.0042 0.0094 -0.0448 289 LEU A O 1973 C CB A LEU A 248 ? 0.4057 0.4193 0.3377 0.0030 -0.0004 -0.0503 289 LEU A CB 1974 C CB B LEU A 248 ? 0.4090 0.4227 0.3415 0.0030 -0.0003 -0.0503 289 LEU A CB 1975 C CG A LEU A 248 ? 0.4072 0.4227 0.3514 0.0019 -0.0047 -0.0500 289 LEU A CG 1976 C CG B LEU A 248 ? 0.4081 0.4229 0.3538 0.0022 -0.0024 -0.0523 289 LEU A CG 1977 C CD1 A LEU A 248 ? 0.4317 0.4448 0.3746 0.0020 -0.0110 -0.0545 289 LEU A CD1 1978 C CD1 B LEU A 248 ? 0.4113 0.4296 0.3675 0.0011 -0.0026 -0.0476 289 LEU A CD1 1979 C CD2 A LEU A 248 ? 0.4353 0.4523 0.3909 0.0015 -0.0015 -0.0503 289 LEU A CD2 1980 C CD2 B LEU A 248 ? 0.4161 0.4283 0.3609 0.0022 -0.0086 -0.0571 289 LEU A CD2 1981 N N . PRO A 249 ? 0.4214 0.4354 0.3441 0.0047 0.0150 -0.0494 290 PRO A N 1982 C CA . PRO A 249 ? 0.4288 0.4408 0.3402 0.0060 0.0203 -0.0502 290 PRO A CA 1983 C C . PRO A 249 ? 0.4365 0.4433 0.3338 0.0076 0.0171 -0.0543 290 PRO A C 1984 O O . PRO A 249 ? 0.4411 0.4464 0.3405 0.0078 0.0112 -0.0583 290 PRO A O 1985 C CB . PRO A 249 ? 0.4397 0.4537 0.3587 0.0067 0.0256 -0.0529 290 PRO A CB 1986 C CG . PRO A 249 ? 0.4208 0.4355 0.3511 0.0064 0.0213 -0.0552 290 PRO A CG 1987 C CD . PRO A 249 ? 0.4191 0.4351 0.3540 0.0047 0.0162 -0.0515 290 PRO A CD 1988 N N . SER A 250 ? 0.4404 0.4443 0.3235 0.0089 0.0210 -0.0536 291 SER A N 1989 C CA A SER A 250 ? 0.4508 0.4490 0.3177 0.0111 0.0176 -0.0573 291 SER A CA 1990 C CA B SER A 250 ? 0.4538 0.4520 0.3206 0.0111 0.0176 -0.0573 291 SER A CA 1991 C C . SER A 250 ? 0.4530 0.4484 0.3120 0.0135 0.0224 -0.0625 291 SER A C 1992 O O . SER A 250 ? 0.4622 0.4522 0.3067 0.0158 0.0197 -0.0667 291 SER A O 1993 C CB A SER A 250 ? 0.4780 0.4731 0.3310 0.0115 0.0176 -0.0526 291 SER A CB 1994 C CB B SER A 250 ? 0.4812 0.4764 0.3342 0.0115 0.0179 -0.0525 291 SER A CB 1995 O OG A SER A 250 ? 0.4877 0.4832 0.3364 0.0115 0.0268 -0.0489 291 SER A OG 1996 O OG B SER A 250 ? 0.4935 0.4916 0.3549 0.0094 0.0152 -0.0472 291 SER A OG 1997 N N . ILE A 251 ? 0.4208 0.4198 0.2892 0.0132 0.0294 -0.0626 292 ILE A N 1998 C CA . ILE A 251 ? 0.4109 0.4078 0.2736 0.0157 0.0348 -0.0677 292 ILE A CA 1999 C C . ILE A 251 ? 0.3865 0.3865 0.2652 0.0154 0.0351 -0.0712 292 ILE A C 2000 O O . ILE A 251 ? 0.3679 0.3724 0.2613 0.0133 0.0343 -0.0680 292 ILE A O 2001 C CB . ILE A 251 ? 0.4183 0.4160 0.2747 0.0164 0.0451 -0.0644 292 ILE A CB 2002 C CG1 . ILE A 251 ? 0.3929 0.3973 0.2655 0.0138 0.0493 -0.0590 292 ILE A CG1 2003 C CG2 . ILE A 251 ? 0.4635 0.4562 0.3007 0.0173 0.0453 -0.0614 292 ILE A CG2 2004 C CD1 . ILE A 251 ? 0.4290 0.4350 0.2989 0.0139 0.0599 -0.0555 292 ILE A CD1 2005 N N . PRO A 252 ? 0.3902 0.3871 0.2655 0.0178 0.0357 -0.0779 293 PRO A N 2006 C CA . PRO A 252 ? 0.3674 0.3664 0.2579 0.0178 0.0359 -0.0812 293 PRO A CA 2007 C C . PRO A 252 ? 0.3565 0.3609 0.2581 0.0177 0.0438 -0.0785 293 PRO A C 2008 O O . PRO A 252 ? 0.3560 0.3616 0.2516 0.0185 0.0512 -0.0767 293 PRO A O 2009 C CB . PRO A 252 ? 0.3862 0.3796 0.2674 0.0209 0.0357 -0.0892 293 PRO A CB 2010 C CG . PRO A 252 ? 0.4327 0.4209 0.2954 0.0218 0.0311 -0.0903 293 PRO A CG 2011 C CD . PRO A 252 ? 0.4046 0.3950 0.2614 0.0208 0.0351 -0.0831 293 PRO A CD 2012 N N . VAL A 253 ? 0.3226 0.3301 0.2406 0.0168 0.0422 -0.0782 294 VAL A N 2013 C CA . VAL A 253 ? 0.3100 0.3228 0.2404 0.0168 0.0480 -0.0758 294 VAL A CA 2014 C C . VAL A 253 ? 0.2942 0.3068 0.2366 0.0181 0.0469 -0.0797 294 VAL A C 2015 O O . VAL A 253 ? 0.3094 0.3192 0.2552 0.0175 0.0406 -0.0813 294 VAL A O 2016 C CB . VAL A 253 ? 0.3042 0.3213 0.2431 0.0141 0.0459 -0.0692 294 VAL A CB 2017 C CG1 . VAL A 253 ? 0.2918 0.3146 0.2442 0.0143 0.0509 -0.0670 294 VAL A CG1 2018 C CG2 . VAL A 253 ? 0.3213 0.3378 0.2489 0.0127 0.0461 -0.0649 294 VAL A CG2 2019 N N . HIS A 254 ? 0.3039 0.3193 0.2532 0.0200 0.0529 -0.0813 295 HIS A N 2020 C CA . HIS A 254 ? 0.2864 0.3012 0.2472 0.0216 0.0517 -0.0846 295 HIS A CA 2021 C C . HIS A 254 ? 0.2921 0.3127 0.2651 0.0228 0.0575 -0.0832 295 HIS A C 2022 O O . HIS A 254 ? 0.3088 0.3324 0.2789 0.0235 0.0642 -0.0827 295 HIS A O 2023 C CB . HIS A 254 ? 0.3125 0.3216 0.2655 0.0243 0.0522 -0.0922 295 HIS A CB 2024 C CG . HIS A 254 ? 0.3080 0.3146 0.2717 0.0257 0.0495 -0.0960 295 HIS A CG 2025 N ND1 . HIS A 254 ? 0.3184 0.3222 0.2881 0.0241 0.0426 -0.0952 295 HIS A ND1 2026 C CD2 . HIS A 254 ? 0.3163 0.3223 0.2858 0.0288 0.0531 -0.1005 295 HIS A CD2 2027 C CE1 . HIS A 254 ? 0.3330 0.3341 0.3115 0.0259 0.0420 -0.0986 295 HIS A CE1 2028 N NE2 . HIS A 254 ? 0.3304 0.3327 0.3089 0.0289 0.0480 -0.1021 295 HIS A NE2 2029 N N . PRO A 255 ? 0.2724 0.2943 0.2592 0.0233 0.0548 -0.0824 296 PRO A N 2030 C CA . PRO A 255 ? 0.2596 0.2871 0.2592 0.0248 0.0588 -0.0813 296 PRO A CA 2031 C C . PRO A 255 ? 0.2785 0.3042 0.2838 0.0284 0.0611 -0.0870 296 PRO A C 2032 O O . PRO A 255 ? 0.2913 0.3112 0.2951 0.0293 0.0574 -0.0907 296 PRO A O 2033 C CB . PRO A 255 ? 0.2576 0.2863 0.2668 0.0235 0.0532 -0.0767 296 PRO A CB 2034 C CG . PRO A 255 ? 0.2711 0.2933 0.2763 0.0228 0.0470 -0.0780 296 PRO A CG 2035 C CD . PRO A 255 ? 0.2628 0.2813 0.2537 0.0222 0.0477 -0.0814 296 PRO A CD 2036 N N . ILE A 256 ? 0.2788 0.3097 0.2919 0.0303 0.0672 -0.0879 297 ILE A N 2037 C CA . ILE A 256 ? 0.2723 0.3026 0.2923 0.0342 0.0704 -0.0933 297 ILE A CA 2038 C C . ILE A 256 ? 0.2781 0.3154 0.3150 0.0358 0.0727 -0.0917 297 ILE A C 2039 O O . ILE A 256 ? 0.2708 0.3138 0.3128 0.0338 0.0730 -0.0868 297 ILE A O 2040 C CB . ILE A 256 ? 0.2954 0.3244 0.3050 0.0362 0.0775 -0.0985 297 ILE A CB 2041 C CG1 . ILE A 256 ? 0.3020 0.3375 0.3109 0.0353 0.0854 -0.0957 297 ILE A CG1 2042 C CG2 . ILE A 256 ? 0.3085 0.3300 0.3012 0.0353 0.0741 -0.1011 297 ILE A CG2 2043 C CD1 . ILE A 256 ? 0.3194 0.3535 0.3175 0.0377 0.0936 -0.1003 297 ILE A CD1 2044 N N . GLY A 257 ? 0.2664 0.3030 0.3120 0.0396 0.0737 -0.0960 298 GLY A N 2045 C CA . GLY A 257 ? 0.2793 0.3220 0.3419 0.0419 0.0749 -0.0954 298 GLY A CA 2046 C C . GLY A 257 ? 0.2881 0.3369 0.3544 0.0435 0.0842 -0.0981 298 GLY A C 2047 O O . GLY A 257 ? 0.3028 0.3501 0.3568 0.0430 0.0897 -0.1001 298 GLY A O 2048 N N . TYR A 258 ? 0.2834 0.3391 0.3664 0.0454 0.0861 -0.0978 299 TYR A N 2049 C CA . TYR A 258 ? 0.2960 0.3585 0.3842 0.0464 0.0958 -0.0998 299 TYR A CA 2050 C C . TYR A 258 ? 0.3155 0.3763 0.4035 0.0508 0.1019 -0.1067 299 TYR A C 2051 O O . TYR A 258 ? 0.3424 0.4071 0.4292 0.0515 0.1113 -0.1085 299 TYR A O 2052 C CB . TYR A 258 ? 0.2890 0.3611 0.3963 0.0463 0.0967 -0.0970 299 TYR A CB 2053 C CG . TYR A 258 ? 0.2708 0.3447 0.3948 0.0497 0.0907 -0.0978 299 TYR A CG 2054 C CD1 . TYR A 258 ? 0.2680 0.3408 0.3953 0.0485 0.0816 -0.0935 299 TYR A CD1 2055 C CD2 . TYR A 258 ? 0.2970 0.3737 0.4336 0.0543 0.0944 -0.1028 299 TYR A CD2 2056 C CE1 . TYR A 258 ? 0.2854 0.3590 0.4265 0.0520 0.0757 -0.0940 299 TYR A CE1 2057 C CE2 . TYR A 258 ? 0.2880 0.3662 0.4400 0.0578 0.0884 -0.1033 299 TYR A CE2 2058 C CZ . TYR A 258 ? 0.2781 0.3545 0.4316 0.0566 0.0789 -0.0987 299 TYR A CZ 2059 O OH . TYR A 258 ? 0.3017 0.3786 0.4687 0.0605 0.0728 -0.0990 299 TYR A OH 2060 N N . TYR A 259 ? 0.3125 0.3671 0.4012 0.0538 0.0973 -0.1104 300 TYR A N 2061 C CA . TYR A 259 ? 0.3288 0.3801 0.4140 0.0578 0.1028 -0.1176 300 TYR A CA 2062 C C . TYR A 259 ? 0.3450 0.3910 0.4089 0.0563 0.1066 -0.1195 300 TYR A C 2063 O O . TYR A 259 ? 0.3668 0.4143 0.4258 0.0583 0.1156 -0.1230 300 TYR A O 2064 C CB . TYR A 259 ? 0.3275 0.3717 0.4164 0.0611 0.0966 -0.1213 300 TYR A CB 2065 C CG . TYR A 259 ? 0.3238 0.3718 0.4326 0.0643 0.0937 -0.1210 300 TYR A CG 2066 C CD1 . TYR A 259 ? 0.3551 0.4134 0.4797 0.0657 0.0988 -0.1204 300 TYR A CD1 2067 C CD2 . TYR A 259 ? 0.3418 0.3829 0.4544 0.0663 0.0860 -0.1216 300 TYR A CD2 2068 C CE1 . TYR A 259 ? 0.3726 0.4342 0.5156 0.0692 0.0952 -0.1206 300 TYR A CE1 2069 C CE2 . TYR A 259 ? 0.3617 0.4054 0.4917 0.0700 0.0830 -0.1214 300 TYR A CE2 2070 C CZ . TYR A 259 ? 0.3928 0.4468 0.5376 0.0716 0.0872 -0.1211 300 TYR A CZ 2071 O OH . TYR A 259 ? 0.3934 0.4501 0.5557 0.0756 0.0834 -0.1212 300 TYR A OH 2072 N N . ASP A 260 ? 0.3321 0.3722 0.3834 0.0530 0.0999 -0.1168 301 ASP A N 2073 C CA . ASP A 260 ? 0.3561 0.3909 0.3869 0.0516 0.1018 -0.1182 301 ASP A CA 2074 C C . ASP A 260 ? 0.3603 0.4004 0.3848 0.0492 0.1090 -0.1143 301 ASP A C 2075 O O . ASP A 260 ? 0.3848 0.4226 0.3953 0.0503 0.1154 -0.1170 301 ASP A O 2076 C CB . ASP A 260 ? 0.3479 0.3758 0.3693 0.0485 0.0922 -0.1162 301 ASP A CB 2077 C CG . ASP A 260 ? 0.3586 0.3785 0.3803 0.0508 0.0866 -0.1215 301 ASP A CG 2078 O OD1 . ASP A 260 ? 0.4231 0.4410 0.4468 0.0549 0.0904 -0.1278 301 ASP A OD1 2079 O OD2 . ASP A 260 ? 0.3674 0.3827 0.3879 0.0484 0.0785 -0.1193 301 ASP A OD2 2080 N N . ALA A 261 ? 0.3417 0.3883 0.3760 0.0462 0.1078 -0.1080 302 ALA A N 2081 C CA . ALA A 261 ? 0.3453 0.3970 0.3760 0.0437 0.1149 -0.1038 302 ALA A CA 2082 C C . ALA A 261 ? 0.3684 0.4249 0.4032 0.0465 0.1267 -0.1068 302 ALA A C 2083 O O . ALA A 261 ? 0.3764 0.4325 0.3989 0.0459 0.1342 -0.1058 302 ALA A O 2084 C CB . ALA A 261 ? 0.3403 0.3983 0.3839 0.0403 0.1113 -0.0972 302 ALA A CB 2085 N N . GLN A 262 ? 0.3458 0.4069 0.3983 0.0498 0.1283 -0.1100 303 GLN A N 2086 C CA . GLN A 262 ? 0.3719 0.4383 0.4315 0.0530 0.1396 -0.1134 303 GLN A CA 2087 C C . GLN A 262 ? 0.3887 0.4482 0.4276 0.0556 0.1459 -0.1184 303 GLN A C 2088 O O . GLN A 262 ? 0.3995 0.4615 0.4330 0.0563 0.1568 -0.1185 303 GLN A O 2089 C CB . GLN A 262 ? 0.3676 0.4372 0.4466 0.0570 0.1377 -0.1176 303 GLN A CB 2090 C CG . GLN A 262 ? 0.4590 0.5343 0.5476 0.0610 0.1489 -0.1220 303 GLN A CG 2091 C CD . GLN A 262 ? 0.5096 0.5962 0.6211 0.0598 0.1518 -0.1185 303 GLN A CD 2092 O OE1 . GLN A 262 ? 0.6025 0.6947 0.7152 0.0575 0.1603 -0.1154 303 GLN A OE1 2093 N NE2 . GLN A 262 ? 0.4872 0.5769 0.6170 0.0612 0.1441 -0.1187 303 GLN A NE2 2094 N N . LYS A 263 ? 0.4020 0.4523 0.4289 0.0570 0.1389 -0.1226 304 LYS A N 2095 C CA A LYS A 263 ? 0.4224 0.4653 0.4296 0.0601 0.1432 -0.1285 304 LYS A CA 2096 C CA B LYS A 263 ? 0.4215 0.4643 0.4287 0.0601 0.1433 -0.1285 304 LYS A CA 2097 C C . LYS A 263 ? 0.4346 0.4741 0.4203 0.0574 0.1459 -0.1250 304 LYS A C 2098 O O . LYS A 263 ? 0.4629 0.4996 0.4337 0.0599 0.1543 -0.1278 304 LYS A O 2099 C CB A LYS A 263 ? 0.4263 0.4603 0.4284 0.0620 0.1340 -0.1340 304 LYS A CB 2100 C CB B LYS A 263 ? 0.4243 0.4582 0.4264 0.0621 0.1342 -0.1341 304 LYS A CB 2101 C CG A LYS A 263 ? 0.4362 0.4719 0.4580 0.0653 0.1314 -0.1377 304 LYS A CG 2102 C CG B LYS A 263 ? 0.4338 0.4694 0.4545 0.0660 0.1332 -0.1387 304 LYS A CG 2103 C CD A LYS A 263 ? 0.4919 0.5285 0.5162 0.0709 0.1410 -0.1448 304 LYS A CD 2104 C CD B LYS A 263 ? 0.4741 0.5110 0.4948 0.0713 0.1441 -0.1452 304 LYS A CD 2105 C CE A LYS A 263 ? 0.5174 0.5459 0.5174 0.0730 0.1448 -0.1501 304 LYS A CE 2106 C CE B LYS A 263 ? 0.4746 0.5150 0.5169 0.0752 0.1438 -0.1489 304 LYS A CE 2107 N NZ A LYS A 263 ? 0.5633 0.5895 0.5641 0.0791 0.1511 -0.1587 304 LYS A NZ 2108 N NZ B LYS A 263 ? 0.5124 0.5538 0.5545 0.0807 0.1547 -0.1558 304 LYS A NZ 2109 N N . LEU A 264 ? 0.4139 0.4533 0.3975 0.0527 0.1389 -0.1186 305 LEU A N 2110 C CA . LEU A 264 ? 0.4361 0.4725 0.4007 0.0500 0.1408 -0.1143 305 LEU A CA 2111 C C . LEU A 264 ? 0.4460 0.4896 0.4147 0.0486 0.1520 -0.1091 305 LEU A C 2112 O O . LEU A 264 ? 0.4799 0.5201 0.4306 0.0486 0.1583 -0.1076 305 LEU A O 2113 C CB . LEU A 264 ? 0.4085 0.4422 0.3697 0.0457 0.1296 -0.1094 305 LEU A CB 2114 C CG . LEU A 264 ? 0.4266 0.4526 0.3820 0.0463 0.1187 -0.1137 305 LEU A CG 2115 C CD1 . LEU A 264 ? 0.4226 0.4475 0.3775 0.0419 0.1089 -0.1083 305 LEU A CD1 2116 C CD2 . LEU A 264 ? 0.4301 0.4473 0.3635 0.0492 0.1194 -0.1196 305 LEU A CD2 2117 N N . LEU A 265 ? 0.4185 0.4714 0.4106 0.0474 0.1542 -0.1064 306 LEU A N 2118 C CA . LEU A 265 ? 0.4118 0.4720 0.4114 0.0452 0.1638 -0.1010 306 LEU A CA 2119 C C . LEU A 265 ? 0.4241 0.4885 0.4283 0.0489 0.1773 -0.1045 306 LEU A C 2120 O O . LEU A 265 ? 0.4303 0.4983 0.4338 0.0475 0.1878 -0.1006 306 LEU A O 2121 C CB . LEU A 265 ? 0.3816 0.4502 0.4052 0.0422 0.1593 -0.0968 306 LEU A CB 2122 C CG . LEU A 265 ? 0.3867 0.4524 0.4075 0.0382 0.1472 -0.0922 306 LEU A CG 2123 C CD1 . LEU A 265 ? 0.3956 0.4690 0.4404 0.0366 0.1423 -0.0898 306 LEU A CD1 2124 C CD2 . LEU A 265 ? 0.4065 0.4696 0.4124 0.0345 0.1492 -0.0862 306 LEU A CD2 2125 N N . GLU A 266 ? 0.4295 0.4936 0.4400 0.0534 0.1775 -0.1116 307 GLU A N 2126 C CA . GLU A 266 ? 0.4443 0.5140 0.4638 0.0572 0.1906 -0.1152 307 GLU A CA 2127 C C . GLU A 266 ? 0.4794 0.5448 0.4771 0.0591 0.2027 -0.1158 307 GLU A C 2128 O O . GLU A 266 ? 0.4780 0.5494 0.4833 0.0604 0.2159 -0.1154 307 GLU A O 2129 C CB . GLU A 266 ? 0.4467 0.5164 0.4772 0.0622 0.1881 -0.1230 307 GLU A CB 2130 C CG . GLU A 266 ? 0.4877 0.5462 0.4971 0.0657 0.1841 -0.1295 307 GLU A CG 2131 C CD . GLU A 266 ? 0.5615 0.6191 0.5832 0.0700 0.1796 -0.1366 307 GLU A CD 2132 O OE1 . GLU A 266 ? 0.6059 0.6718 0.6525 0.0706 0.1794 -0.1362 307 GLU A OE1 2133 O OE2 . GLU A 266 ? 0.5807 0.6290 0.5872 0.0731 0.1762 -0.1428 307 GLU A OE2 2134 N N . LYS A 267 ? 0.4969 0.5516 0.4677 0.0595 0.1984 -0.1169 308 LYS A N 2135 C CA . LYS A 267 ? 0.5265 0.5752 0.4727 0.0620 0.2086 -0.1177 308 LYS A CA 2136 C C . LYS A 267 ? 0.5304 0.5782 0.4650 0.0577 0.2123 -0.1090 308 LYS A C 2137 O O . LYS A 267 ? 0.5523 0.5945 0.4650 0.0596 0.2208 -0.1085 308 LYS A O 2138 C CB . LYS A 267 ? 0.5485 0.5853 0.4704 0.0654 0.2015 -0.1242 308 LYS A CB 2139 C CG . LYS A 267 ? 0.5832 0.6182 0.5097 0.0710 0.2016 -0.1338 308 LYS A CG 2140 C CD . LYS A 267 ? 0.6115 0.6349 0.5182 0.0730 0.1908 -0.1399 308 LYS A CD 2141 C CE . LYS A 267 ? 0.6648 0.6851 0.5736 0.0790 0.1923 -0.1500 308 LYS A CE 2142 N NZ . LYS A 267 ? 0.6922 0.7010 0.5837 0.0806 0.1811 -0.1563 308 LYS A NZ 2143 N N . MET A 268 ? 0.5026 0.5555 0.4513 0.0523 0.2061 -0.1024 309 MET A N 2144 C CA . MET A 268 ? 0.5133 0.5648 0.4519 0.0481 0.2086 -0.0939 309 MET A CA 2145 C C . MET A 268 ? 0.5296 0.5851 0.4689 0.0480 0.2253 -0.0898 309 MET A C 2146 O O . MET A 268 ? 0.5172 0.5822 0.4790 0.0484 0.2337 -0.0904 309 MET A O 2147 C CB . MET A 268 ? 0.4924 0.5481 0.4463 0.0426 0.1982 -0.0883 309 MET A CB 2148 C CG A MET A 268 ? 0.4905 0.5380 0.4305 0.0424 0.1836 -0.0903 309 MET A CG 2149 C CG B MET A 268 ? 0.5210 0.5715 0.4702 0.0420 0.1826 -0.0905 309 MET A CG 2150 S SD A MET A 268 ? 0.4422 0.4912 0.3910 0.0366 0.1705 -0.0838 309 MET A SD 2151 S SD B MET A 268 ? 0.5742 0.6136 0.4927 0.0406 0.1774 -0.0870 309 MET A SD 2152 C CE A MET A 268 ? 0.4828 0.5291 0.4164 0.0333 0.1772 -0.0753 309 MET A CE 2153 C CE B MET A 268 ? 0.5540 0.5979 0.4785 0.0351 0.1824 -0.0764 309 MET A CE 2154 N N . GLY A 269 ? 0.5476 0.5956 0.4620 0.0476 0.2299 -0.0856 310 GLY A N 2155 C CA . GLY A 269 ? 0.5721 0.6217 0.4825 0.0476 0.2463 -0.0809 310 GLY A CA 2156 C C . GLY A 269 ? 0.5786 0.6270 0.4850 0.0423 0.2465 -0.0711 310 GLY A C 2157 O O . GLY A 269 ? 0.5580 0.6105 0.4801 0.0376 0.2369 -0.0675 310 GLY A O 2158 N N . GLY A 270 ? 0.6026 0.6447 0.4874 0.0432 0.2573 -0.0666 311 GLY A N 2159 C CA . GLY A 270 ? 0.6092 0.6494 0.4900 0.0383 0.2588 -0.0568 311 GLY A CA 2160 C C . GLY A 270 ? 0.5966 0.6487 0.5098 0.0335 0.2653 -0.0519 311 GLY A C 2161 O O . GLY A 270 ? 0.5946 0.6547 0.5253 0.0349 0.2763 -0.0543 311 GLY A O 2162 N N . SER A 271 ? 0.5791 0.6325 0.5013 0.0280 0.2581 -0.0456 312 SER A N 2163 C CA . SER A 271 ? 0.5717 0.6350 0.5228 0.0229 0.2634 -0.0402 312 SER A CA 2164 C C . SER A 271 ? 0.5511 0.6260 0.5351 0.0220 0.2570 -0.0450 312 SER A C 2165 O O . SER A 271 ? 0.5392 0.6135 0.5245 0.0231 0.2432 -0.0499 312 SER A O 2166 C CB . SER A 271 ? 0.5728 0.6320 0.5198 0.0177 0.2570 -0.0321 312 SER A CB 2167 O OG A SER A 271 ? 0.5783 0.6455 0.5503 0.0128 0.2638 -0.0264 312 SER A OG 2168 O OG B SER A 271 ? 0.5810 0.6292 0.4980 0.0187 0.2630 -0.0269 312 SER A OG 2169 N N . ALA A 272 ? 0.5428 0.6282 0.5537 0.0201 0.2669 -0.0437 313 ALA A N 2170 C CA . ALA A 272 ? 0.5181 0.6149 0.5621 0.0188 0.2603 -0.0472 313 ALA A CA 2171 C C . ALA A 272 ? 0.5015 0.5985 0.5540 0.0141 0.2455 -0.0438 313 ALA A C 2172 O O . ALA A 272 ? 0.5047 0.5953 0.5435 0.0109 0.2440 -0.0375 313 ALA A O 2173 C CB . ALA A 272 ? 0.5221 0.6300 0.5933 0.0173 0.2745 -0.0457 313 ALA A CB 2174 N N . PRO A 273 ? 0.4766 0.5803 0.5504 0.0141 0.2344 -0.0480 314 PRO A N 2175 C CA . PRO A 273 ? 0.4680 0.5725 0.5510 0.0099 0.2214 -0.0449 314 PRO A CA 2176 C C . PRO A 273 ? 0.4710 0.5803 0.5701 0.0046 0.2285 -0.0382 314 PRO A C 2177 O O . PRO A 273 ? 0.4653 0.5820 0.5814 0.0044 0.2410 -0.0381 314 PRO A O 2178 C CB . PRO A 273 ? 0.4448 0.5570 0.5504 0.0117 0.2121 -0.0508 314 PRO A CB 2179 C CG . PRO A 273 ? 0.4500 0.5690 0.5683 0.0153 0.2236 -0.0555 314 PRO A CG 2180 C CD . PRO A 273 ? 0.4724 0.5835 0.5638 0.0180 0.2341 -0.0555 314 PRO A CD 2181 N N . PRO A 274 ? 0.4700 0.5750 0.5642 0.0005 0.2214 -0.0327 315 PRO A N 2182 C CA . PRO A 274 ? 0.4820 0.5896 0.5888 -0.0046 0.2290 -0.0259 315 PRO A CA 2183 C C . PRO A 274 ? 0.4796 0.5996 0.6230 -0.0071 0.2282 -0.0273 315 PRO A C 2184 O O . PRO A 274 ? 0.4824 0.6071 0.6419 -0.0107 0.2381 -0.0233 315 PRO A O 2185 C CB . PRO A 274 ? 0.4771 0.5762 0.5680 -0.0076 0.2195 -0.0208 315 PRO A CB 2186 C CG . PRO A 274 ? 0.4640 0.5605 0.5472 -0.0048 0.2039 -0.0259 315 PRO A CG 2187 C CD . PRO A 274 ? 0.4601 0.5560 0.5335 0.0005 0.2083 -0.0319 315 PRO A CD 2188 N N . ASP A 275 ? 0.4706 0.5955 0.6272 -0.0051 0.2166 -0.0331 316 ASP A N 2189 C CA . ASP A 275 ? 0.4643 0.6007 0.6551 -0.0066 0.2137 -0.0354 316 ASP A CA 2190 C C . ASP A 275 ? 0.4531 0.5922 0.6499 -0.0025 0.2016 -0.0423 316 ASP A C 2191 O O . ASP A 275 ? 0.4496 0.5814 0.6246 0.0008 0.1958 -0.0447 316 ASP A O 2192 C CB . ASP A 275 ? 0.4636 0.6007 0.6667 -0.0122 0.2080 -0.0305 316 ASP A CB 2193 C CG . ASP A 275 ? 0.4833 0.6132 0.6719 -0.0126 0.1924 -0.0299 316 ASP A CG 2194 O OD1 . ASP A 275 ? 0.5214 0.6535 0.7157 -0.0099 0.1810 -0.0349 316 ASP A OD1 2195 O OD2 . ASP A 275 ? 0.5172 0.6391 0.6892 -0.0153 0.1916 -0.0245 316 ASP A OD2 2196 N N . SER A 276 ? 0.4404 0.5895 0.6667 -0.0026 0.1973 -0.0454 317 SER A N 2197 C CA . SER A 276 ? 0.4455 0.5979 0.6799 0.0019 0.1873 -0.0519 317 SER A CA 2198 C C . SER A 276 ? 0.4268 0.5723 0.6480 0.0025 0.1711 -0.0522 317 SER A C 2199 O O . SER A 276 ? 0.4369 0.5815 0.6556 0.0067 0.1636 -0.0569 317 SER A O 2200 C CB . SER A 276 ? 0.4429 0.6077 0.7127 0.0018 0.1866 -0.0549 317 SER A CB 2201 O OG . SER A 276 ? 0.4712 0.6378 0.7538 -0.0023 0.1776 -0.0524 317 SER A OG 2202 N N . SER A 277 ? 0.4105 0.5511 0.6237 -0.0016 0.1659 -0.0473 318 SER A N 2203 C CA . SER A 277 ? 0.3837 0.5178 0.5842 -0.0011 0.1515 -0.0472 318 SER A CA 2204 C C . SER A 277 ? 0.3776 0.5022 0.5491 0.0016 0.1505 -0.0479 318 SER A C 2205 O O . SER A 277 ? 0.3776 0.4967 0.5378 0.0025 0.1395 -0.0484 318 SER A O 2206 C CB . SER A 277 ? 0.3899 0.5211 0.5893 -0.0060 0.1469 -0.0419 318 SER A CB 2207 O OG . SER A 277 ? 0.3989 0.5226 0.5772 -0.0083 0.1542 -0.0369 318 SER A OG 2208 N N . TRP A 278 ? 0.3637 0.4862 0.5234 0.0028 0.1621 -0.0479 319 TRP A N 2209 C CA . TRP A 278 ? 0.3595 0.4733 0.4926 0.0057 0.1619 -0.0495 319 TRP A CA 2210 C C . TRP A 278 ? 0.3551 0.4710 0.4916 0.0109 0.1621 -0.0562 319 TRP A C 2211 O O . TRP A 278 ? 0.3520 0.4609 0.4695 0.0137 0.1596 -0.0587 319 TRP A O 2212 C CB . TRP A 278 ? 0.3761 0.4846 0.4905 0.0046 0.1737 -0.0458 319 TRP A CB 2213 C CG . TRP A 278 ? 0.3605 0.4624 0.4610 0.0009 0.1703 -0.0398 319 TRP A CG 2214 C CD1 . TRP A 278 ? 0.3647 0.4690 0.4778 -0.0035 0.1671 -0.0354 319 TRP A CD1 2215 C CD2 . TRP A 278 ? 0.3472 0.4388 0.4191 0.0013 0.1690 -0.0377 319 TRP A CD2 2216 N NE1 . TRP A 278 ? 0.3679 0.4638 0.4617 -0.0057 0.1642 -0.0305 319 TRP A NE1 2217 C CE2 . TRP A 278 ? 0.3767 0.4650 0.4452 -0.0028 0.1652 -0.0317 319 TRP A CE2 2218 C CE3 . TRP A 278 ? 0.3597 0.4444 0.4088 0.0050 0.1701 -0.0406 319 TRP A CE3 2219 C CZ2 . TRP A 278 ? 0.3803 0.4588 0.4236 -0.0032 0.1623 -0.0284 319 TRP A CZ2 2220 C CZ3 . TRP A 278 ? 0.3751 0.4502 0.3992 0.0045 0.1669 -0.0375 319 TRP A CZ3 2221 C CH2 . TRP A 278 ? 0.3795 0.4518 0.4012 0.0005 0.1629 -0.0313 319 TRP A CH2 2222 N N . ARG A 279 ? 0.3490 0.4743 0.5102 0.0122 0.1653 -0.0592 320 ARG A N 2223 C CA . ARG A 279 ? 0.3561 0.4836 0.5223 0.0174 0.1655 -0.0656 320 ARG A CA 2224 C C . ARG A 279 ? 0.3395 0.4679 0.5155 0.0195 0.1518 -0.0686 320 ARG A C 2225 O O . ARG A 279 ? 0.3349 0.4690 0.5297 0.0179 0.1458 -0.0676 320 ARG A O 2226 C CB . ARG A 279 ? 0.3535 0.4906 0.5407 0.0185 0.1774 -0.0677 320 ARG A CB 2227 C CG . ARG A 279 ? 0.4343 0.5687 0.6072 0.0188 0.1923 -0.0666 320 ARG A CG 2228 C CD . ARG A 279 ? 0.5208 0.6649 0.7147 0.0206 0.2047 -0.0694 320 ARG A CD 2229 N NE . ARG A 279 ? 0.6382 0.7876 0.8441 0.0160 0.2142 -0.0640 320 ARG A NE 2230 C CZ . ARG A 279 ? 0.6602 0.8193 0.8952 0.0133 0.2126 -0.0631 320 ARG A CZ 2231 N NH1 . ARG A 279 ? 0.6658 0.8305 0.9200 0.0152 0.2015 -0.0672 320 ARG A NH1 2232 N NH2 . ARG A 279 ? 0.6665 0.8293 0.9113 0.0087 0.2219 -0.0581 320 ARG A NH2 2233 N N . GLY A 280 ? 0.3403 0.4624 0.5027 0.0231 0.1468 -0.0721 321 GLY A N 2234 C CA . GLY A 280 ? 0.3240 0.4463 0.4949 0.0262 0.1356 -0.0754 321 GLY A CA 2235 C C . GLY A 280 ? 0.3265 0.4557 0.5164 0.0306 0.1393 -0.0807 321 GLY A C 2236 O O . GLY A 280 ? 0.3306 0.4674 0.5345 0.0303 0.1496 -0.0812 321 GLY A O 2237 N N . SER A 281 ? 0.3167 0.4433 0.5080 0.0346 0.1314 -0.0844 322 SER A N 2238 C CA . SER A 281 ? 0.3440 0.4769 0.5553 0.0393 0.1323 -0.0894 322 SER A CA 2239 C C . SER A 281 ? 0.3447 0.4735 0.5470 0.0438 0.1377 -0.0946 322 SER A C 2240 O O . SER A 281 ? 0.3565 0.4897 0.5742 0.0481 0.1388 -0.0991 322 SER A O 2241 C CB . SER A 281 ? 0.3477 0.4810 0.5702 0.0413 0.1189 -0.0898 322 SER A CB 2242 O OG . SER A 281 ? 0.3770 0.5154 0.6115 0.0379 0.1143 -0.0862 322 SER A OG 2243 N N . LEU A 282 ? 0.3385 0.4587 0.5163 0.0430 0.1406 -0.0943 323 LEU A N 2244 C CA . LEU A 282 ? 0.3415 0.4571 0.5094 0.0473 0.1461 -0.0997 323 LEU A CA 2245 C C . LEU A 282 ? 0.3657 0.4878 0.5407 0.0485 0.1606 -0.1018 323 LEU A C 2246 O O . LEU A 282 ? 0.3592 0.4866 0.5389 0.0450 0.1677 -0.0979 323 LEU A O 2247 C CB . LEU A 282 ? 0.3441 0.4486 0.4836 0.0461 0.1446 -0.0992 323 LEU A CB 2248 C CG . LEU A 282 ? 0.3481 0.4452 0.4786 0.0451 0.1313 -0.0976 323 LEU A CG 2249 C CD1 . LEU A 282 ? 0.3308 0.4182 0.4347 0.0433 0.1306 -0.0967 323 LEU A CD1 2250 C CD2 . LEU A 282 ? 0.3548 0.4499 0.4937 0.0498 0.1254 -0.1023 323 LEU A CD2 2251 N N . LYS A 283 ? 0.3801 0.5006 0.5539 0.0535 0.1653 -0.1078 324 LYS A N 2252 C CA . LYS A 283 ? 0.4189 0.5448 0.5981 0.0556 0.1798 -0.1106 324 LYS A CA 2253 C C . LYS A 283 ? 0.4312 0.5496 0.5834 0.0548 0.1882 -0.1100 324 LYS A C 2254 O O . LYS A 283 ? 0.4446 0.5585 0.5857 0.0590 0.1939 -0.1153 324 LYS A O 2255 C CB . LYS A 283 ? 0.4380 0.5661 0.6302 0.0620 0.1809 -0.1177 324 LYS A CB 2256 C CG . LYS A 283 ? 0.4852 0.6206 0.7041 0.0632 0.1722 -0.1180 324 LYS A CG 2257 C CD . LYS A 283 ? 0.5618 0.7093 0.8032 0.0601 0.1769 -0.1145 324 LYS A CD 2258 C CE . LYS A 283 ? 0.5964 0.7482 0.8561 0.0591 0.1639 -0.1124 324 LYS A CE 2259 N NZ . LYS A 283 ? 0.5967 0.7607 0.8812 0.0565 0.1684 -0.1101 324 LYS A NZ 2260 N N . VAL A 284 ? 0.4177 0.5343 0.5590 0.0496 0.1880 -0.1037 325 VAL A N 2261 C CA . VAL A 284 ? 0.4331 0.5430 0.5492 0.0484 0.1960 -0.1017 325 VAL A CA 2262 C C . VAL A 284 ? 0.4312 0.5470 0.5534 0.0436 0.2039 -0.0950 325 VAL A C 2263 O O . VAL A 284 ? 0.4212 0.5443 0.5642 0.0405 0.1997 -0.0917 325 VAL A O 2264 C CB . VAL A 284 ? 0.4282 0.5268 0.5192 0.0468 0.1857 -0.1004 325 VAL A CB 2265 C CG1 . VAL A 284 ? 0.4549 0.5470 0.5399 0.0510 0.1781 -0.1068 325 VAL A CG1 2266 C CG2 . VAL A 284 ? 0.4054 0.5050 0.5020 0.0418 0.1752 -0.0943 325 VAL A CG2 2267 N N . PRO A 285 ? 0.4458 0.5574 0.5492 0.0430 0.2149 -0.0928 326 PRO A N 2268 C CA . PRO A 285 ? 0.4463 0.5624 0.5546 0.0384 0.2235 -0.0859 326 PRO A CA 2269 C C . PRO A 285 ? 0.4292 0.5418 0.5308 0.0329 0.2145 -0.0792 326 PRO A C 2270 O O . PRO A 285 ? 0.4245 0.5420 0.5371 0.0287 0.2189 -0.0736 326 PRO A O 2271 C CB . PRO A 285 ? 0.4731 0.5835 0.5586 0.0404 0.2372 -0.0858 326 PRO A CB 2272 C CG . PRO A 285 ? 0.5055 0.6051 0.5661 0.0446 0.2309 -0.0914 326 PRO A CG 2273 C CD . PRO A 285 ? 0.4720 0.5744 0.5491 0.0470 0.2200 -0.0969 326 PRO A CD 2274 N N . TYR A 286 ? 0.4112 0.5153 0.4960 0.0331 0.2022 -0.0800 327 TYR A N 2275 C CA . TYR A 286 ? 0.3987 0.4980 0.4731 0.0285 0.1935 -0.0741 327 TYR A CA 2276 C C . TYR A 286 ? 0.4180 0.5123 0.4735 0.0262 0.2023 -0.0686 327 TYR A C 2277 O O . TYR A 286 ? 0.4167 0.5112 0.4736 0.0217 0.2006 -0.0623 327 TYR A O 2278 C CB . TYR A 286 ? 0.3820 0.4888 0.4806 0.0250 0.1864 -0.0710 327 TYR A CB 2279 C CG . TYR A 286 ? 0.3529 0.4611 0.4625 0.0273 0.1744 -0.0753 327 TYR A CG 2280 C CD1 . TYR A 286 ? 0.3479 0.4488 0.4446 0.0267 0.1618 -0.0749 327 TYR A CD1 2281 C CD2 . TYR A 286 ? 0.3461 0.4623 0.4785 0.0303 0.1759 -0.0797 327 TYR A CD2 2282 C CE1 . TYR A 286 ? 0.3399 0.4412 0.4458 0.0289 0.1515 -0.0782 327 TYR A CE1 2283 C CE2 . TYR A 286 ? 0.3404 0.4568 0.4819 0.0327 0.1648 -0.0832 327 TYR A CE2 2284 C CZ . TYR A 286 ? 0.3561 0.4648 0.4836 0.0321 0.1531 -0.0823 327 TYR A CZ 2285 O OH . TYR A 286 ? 0.3286 0.4368 0.4643 0.0345 0.1426 -0.0851 327 TYR A OH 2286 N N . ASN A 287 ? 0.4388 0.5282 0.4762 0.0297 0.2118 -0.0711 328 ASN A N 2287 C CA . ASN A 287 ? 0.4603 0.5426 0.4742 0.0287 0.2196 -0.0664 328 ASN A CA 2288 C C . ASN A 287 ? 0.4566 0.5299 0.4504 0.0268 0.2080 -0.0637 328 ASN A C 2289 O O . ASN A 287 ? 0.4439 0.5137 0.4332 0.0281 0.1962 -0.0676 328 ASN A O 2290 C CB . ASN A 287 ? 0.4693 0.5468 0.4648 0.0339 0.2300 -0.0710 328 ASN A CB 2291 C CG . ASN A 287 ? 0.4954 0.5816 0.5084 0.0357 0.2450 -0.0725 328 ASN A CG 2292 O OD1 . ASN A 287 ? 0.4982 0.5933 0.5340 0.0322 0.2506 -0.0683 328 ASN A OD1 2293 N ND2 . ASN A 287 ? 0.4944 0.5779 0.4974 0.0412 0.2515 -0.0788 328 ASN A ND2 2294 N N . VAL A 288 ? 0.4719 0.5415 0.4544 0.0236 0.2114 -0.0567 329 VAL A N 2295 C CA . VAL A 288 ? 0.4674 0.5296 0.4346 0.0213 0.2002 -0.0533 329 VAL A CA 2296 C C . VAL A 288 ? 0.4897 0.5408 0.4253 0.0249 0.1987 -0.0558 329 VAL A C 2297 O O . VAL A 288 ? 0.4737 0.5185 0.3965 0.0244 0.1874 -0.0557 329 VAL A O 2298 C CB . VAL A 288 ? 0.4802 0.5434 0.4514 0.0163 0.2034 -0.0447 329 VAL A CB 2299 C CG1 . VAL A 288 ? 0.4992 0.5531 0.4489 0.0149 0.1947 -0.0410 329 VAL A CG1 2300 C CG2 . VAL A 288 ? 0.4527 0.5258 0.4550 0.0126 0.1986 -0.0434 329 VAL A CG2 2301 N N . GLY A 289 ? 0.5110 0.5596 0.4345 0.0287 0.2101 -0.0585 330 GLY A N 2302 C CA . GLY A 289 ? 0.5475 0.5850 0.4396 0.0327 0.2095 -0.0612 330 GLY A CA 2303 C C . GLY A 289 ? 0.5705 0.6013 0.4422 0.0313 0.2156 -0.0537 330 GLY A C 2304 O O . GLY A 289 ? 0.5681 0.6031 0.4497 0.0285 0.2257 -0.0475 330 GLY A O 2305 N N . PRO A 290 ? 0.5940 0.6139 0.4376 0.0333 0.2093 -0.0541 331 PRO A N 2306 C CA . PRO A 290 ? 0.5983 0.6123 0.4292 0.0364 0.1972 -0.0613 331 PRO A CA 2307 C C . PRO A 290 ? 0.6049 0.6172 0.4283 0.0421 0.2026 -0.0699 331 PRO A C 2308 O O . PRO A 290 ? 0.6186 0.6300 0.4336 0.0449 0.2166 -0.0696 331 PRO A O 2309 C CB . PRO A 290 ? 0.6181 0.6212 0.4202 0.0370 0.1926 -0.0578 331 PRO A CB 2310 C CG . PRO A 290 ? 0.6593 0.6602 0.4506 0.0371 0.2076 -0.0511 331 PRO A CG 2311 C CD . PRO A 290 ? 0.6251 0.6374 0.4472 0.0326 0.2144 -0.0467 331 PRO A CD 2312 N N . GLY A 291 ? 0.5916 0.6030 0.4179 0.0440 0.1920 -0.0773 332 GLY A N 2313 C CA . GLY A 291 ? 0.6069 0.6145 0.4232 0.0497 0.1947 -0.0863 332 GLY A CA 2314 C C . GLY A 291 ? 0.5949 0.6110 0.4322 0.0515 0.2045 -0.0901 332 GLY A C 2315 O O . GLY A 291 ? 0.5705 0.5964 0.4327 0.0481 0.2086 -0.0860 332 GLY A O 2316 N N . PHE A 292 ? 0.6129 0.6250 0.4402 0.0571 0.2078 -0.0983 333 PHE A N 2317 C CA . PHE A 292 ? 0.6003 0.6197 0.4470 0.0597 0.2154 -0.1035 333 PHE A CA 2318 C C . PHE A 292 ? 0.6265 0.6472 0.4667 0.0627 0.2337 -0.1025 333 PHE A C 2319 O O . PHE A 292 ? 0.6337 0.6469 0.4483 0.0642 0.2396 -0.0997 333 PHE A O 2320 C CB . PHE A 292 ? 0.6088 0.6232 0.4509 0.0643 0.2080 -0.1139 333 PHE A CB 2321 C CG . PHE A 292 ? 0.5972 0.6114 0.4503 0.0616 0.1915 -0.1156 333 PHE A CG 2322 C CD1 . PHE A 292 ? 0.6138 0.6190 0.4522 0.0643 0.1814 -0.1227 333 PHE A CD1 2323 C CD2 . PHE A 292 ? 0.5923 0.6147 0.4699 0.0567 0.1862 -0.1104 333 PHE A CD2 2324 C CE1 . PHE A 292 ? 0.6183 0.6229 0.4667 0.0620 0.1673 -0.1241 333 PHE A CE1 2325 C CE2 . PHE A 292 ? 0.5721 0.5937 0.4583 0.0547 0.1719 -0.1119 333 PHE A CE2 2326 C CZ . PHE A 292 ? 0.5673 0.5799 0.4392 0.0572 0.1629 -0.1184 333 PHE A CZ 2327 N N . THR A 293 ? 0.6268 0.6568 0.4900 0.0639 0.2426 -0.1048 334 THR A N 2328 C CA . THR A 293 ? 0.6691 0.7014 0.5292 0.0671 0.2611 -0.1045 334 THR A CA 2329 C C . THR A 293 ? 0.7152 0.7372 0.5460 0.0740 0.2661 -0.1116 334 THR A C 2330 O O . THR A 293 ? 0.7221 0.7370 0.5416 0.0770 0.2554 -0.1191 334 THR A O 2331 C CB . THR A 293 ? 0.6644 0.7095 0.5576 0.0676 0.2688 -0.1069 334 THR A CB 2332 O OG1 . THR A 293 ? 0.6737 0.7185 0.5747 0.0712 0.2606 -0.1161 334 THR A OG1 2333 C CG2 . THR A 293 ? 0.6411 0.6966 0.5629 0.0611 0.2660 -0.0999 334 THR A CG2 2334 N N . GLY A 294 ? 0.7407 0.7618 0.5599 0.0766 0.2829 -0.1093 335 GLY A N 2335 C CA . GLY A 294 ? 0.7931 0.8037 0.5807 0.0834 0.2902 -0.1147 335 GLY A CA 2336 C C . GLY A 294 ? 0.8102 0.8133 0.5851 0.0892 0.2814 -0.1263 335 GLY A C 2337 O O . GLY A 294 ? 0.8406 0.8317 0.5858 0.0918 0.2744 -0.1290 335 GLY A O 2338 N N . ASN A 295 ? 0.7987 0.8084 0.5962 0.0913 0.2814 -0.1333 336 ASN A N 2339 C CA . ASN A 295 ? 0.8169 0.8195 0.6050 0.0968 0.2735 -0.1447 336 ASN A CA 2340 C C . ASN A 295 ? 0.7980 0.7934 0.5787 0.0946 0.2535 -0.1469 336 ASN A C 2341 O O . ASN A 295 ? 0.8139 0.7992 0.5749 0.0989 0.2466 -0.1551 336 ASN A O 2342 C CB . ASN A 295 ? 0.8177 0.8293 0.6350 0.0991 0.2767 -0.1509 336 ASN A CB 2343 C CG . ASN A 295 ? 0.8722 0.8894 0.6940 0.1031 0.2968 -0.1516 336 ASN A CG 2344 O OD1 . ASN A 295 ? 0.9413 0.9538 0.7404 0.1052 0.3090 -0.1486 336 ASN A OD1 2345 N ND2 . ASN A 295 ? 0.9145 0.9416 0.7655 0.1045 0.3006 -0.1556 336 ASN A ND2 2346 N N . PHE A 296 ? 0.7544 0.7550 0.5511 0.0879 0.2444 -0.1398 337 PHE A N 2347 C CA . PHE A 296 ? 0.7309 0.7266 0.5257 0.0853 0.2260 -0.1414 337 PHE A CA 2348 C C . PHE A 296 ? 0.7319 0.7219 0.5075 0.0817 0.2202 -0.1342 337 PHE A C 2349 O O . PHE A 296 ? 0.7073 0.6954 0.4852 0.0782 0.2057 -0.1331 337 PHE A O 2350 C CB . PHE A 296 ? 0.7006 0.7061 0.5291 0.0809 0.2185 -0.1397 337 PHE A CB 2351 C CG . PHE A 296 ? 0.6940 0.7068 0.5450 0.0840 0.2253 -0.1450 337 PHE A CG 2352 C CD1 . PHE A 296 ? 0.6903 0.7149 0.5651 0.0821 0.2356 -0.1401 337 PHE A CD1 2353 C CD2 . PHE A 296 ? 0.7183 0.7259 0.5671 0.0891 0.2212 -0.1553 337 PHE A CD2 2354 C CE1 . PHE A 296 ? 0.6770 0.7088 0.5737 0.0853 0.2415 -0.1451 337 PHE A CE1 2355 C CE2 . PHE A 296 ? 0.7059 0.7200 0.5759 0.0924 0.2274 -0.1603 337 PHE A CE2 2356 C CZ . PHE A 296 ? 0.6992 0.7257 0.5932 0.0906 0.2374 -0.1552 337 PHE A CZ 2357 N N . SER A 297 ? 0.7509 0.7379 0.5073 0.0829 0.2317 -0.1293 338 SER A N 2358 C CA . SER A 297 ? 0.7529 0.7352 0.4927 0.0794 0.2283 -0.1209 338 SER A CA 2359 C C . SER A 297 ? 0.7527 0.7239 0.4699 0.0806 0.2131 -0.1249 338 SER A C 2360 O O . SER A 297 ? 0.7512 0.7202 0.4627 0.0767 0.2049 -0.1186 338 SER A O 2361 C CB . SER A 297 ? 0.7793 0.7585 0.4995 0.0817 0.2445 -0.1158 338 SER A CB 2362 O OG . SER A 297 ? 0.8231 0.7910 0.5121 0.0886 0.2468 -0.1226 338 SER A OG 2363 N N . THR A 298 ? 0.7514 0.7159 0.4571 0.0860 0.2090 -0.1354 339 THR A N 2364 C CA . THR A 298 ? 0.7639 0.7176 0.4486 0.0877 0.1943 -0.1407 339 THR A CA 2365 C C . THR A 298 ? 0.7348 0.6906 0.4389 0.0844 0.1783 -0.1444 339 THR A C 2366 O O . THR A 298 ? 0.7481 0.6963 0.4396 0.0846 0.1649 -0.1480 339 THR A O 2367 C CB . THR A 298 ? 0.7889 0.7320 0.4466 0.0956 0.1973 -0.1506 339 THR A CB 2368 O OG1 . THR A 298 ? 0.7989 0.7457 0.4727 0.0986 0.2011 -0.1589 339 THR A OG1 2369 C CG2 . THR A 298 ? 0.8426 0.7813 0.4754 0.0992 0.2125 -0.1464 339 THR A CG2 2370 N N . GLN A 299 ? 0.6964 0.6624 0.4314 0.0815 0.1796 -0.1436 340 GLN A N 2371 C CA . GLN A 299 ? 0.6574 0.6260 0.4126 0.0778 0.1655 -0.1451 340 GLN A CA 2372 C C . GLN A 299 ? 0.6416 0.6136 0.4026 0.0715 0.1587 -0.1356 340 GLN A C 2373 O O . GLN A 299 ? 0.6353 0.6107 0.3942 0.0693 0.1665 -0.1274 340 GLN A O 2374 C CB . GLN A 299 ? 0.6335 0.6110 0.4179 0.0776 0.1693 -0.1474 340 GLN A CB 2375 C CG . GLN A 299 ? 0.6733 0.6473 0.4531 0.0842 0.1755 -0.1575 340 GLN A CG 2376 C CD . GLN A 299 ? 0.6629 0.6459 0.4713 0.0848 0.1809 -0.1595 340 GLN A CD 2377 O OE1 . GLN A 299 ? 0.6487 0.6410 0.4810 0.0804 0.1799 -0.1535 340 GLN A OE1 2378 N NE2 . GLN A 299 ? 0.6503 0.6303 0.4558 0.0907 0.1861 -0.1685 340 GLN A NE2 2379 N N . LYS A 300 ? 0.6165 0.5870 0.3843 0.0687 0.1442 -0.1369 341 LYS A N 2380 C CA . LYS A 300 ? 0.5972 0.5704 0.3712 0.0630 0.1365 -0.1289 341 LYS A CA 2381 C C . LYS A 300 ? 0.5705 0.5494 0.3709 0.0596 0.1280 -0.1294 341 LYS A C 2382 O O . LYS A 300 ? 0.5538 0.5330 0.3650 0.0618 0.1273 -0.1360 341 LYS A O 2383 C CB . LYS A 300 ? 0.6134 0.5774 0.3648 0.0633 0.1259 -0.1297 341 LYS A CB 2384 C CG . LYS A 300 ? 0.6623 0.6179 0.3823 0.0676 0.1317 -0.1303 341 LYS A CG 2385 C CD . LYS A 300 ? 0.7252 0.6830 0.4391 0.0652 0.1392 -0.1198 341 LYS A CD 2386 C CE . LYS A 300 ? 0.8010 0.7510 0.4853 0.0701 0.1486 -0.1200 341 LYS A CE 2387 N NZ . LYS A 300 ? 0.8342 0.7900 0.5240 0.0699 0.1656 -0.1139 341 LYS A NZ 2388 N N . VAL A 301 ? 0.5399 0.5226 0.3498 0.0545 0.1218 -0.1222 342 VAL A N 2389 C CA . VAL A 301 ? 0.5172 0.5035 0.3482 0.0513 0.1123 -0.1221 342 VAL A CA 2390 C C . VAL A 301 ? 0.5133 0.4938 0.3354 0.0495 0.0993 -0.1227 342 VAL A C 2391 O O . VAL A 301 ? 0.5278 0.5055 0.3352 0.0484 0.0974 -0.1185 342 VAL A O 2392 C CB . VAL A 301 ? 0.4957 0.4919 0.3476 0.0471 0.1154 -0.1139 342 VAL A CB 2393 C CG1 . VAL A 301 ? 0.4946 0.4931 0.3636 0.0437 0.1047 -0.1125 342 VAL A CG1 2394 C CG2 . VAL A 301 ? 0.5030 0.5056 0.3687 0.0492 0.1268 -0.1150 342 VAL A CG2 2395 N N . LYS A 302 ? 0.5050 0.4835 0.3366 0.0493 0.0904 -0.1278 343 LYS A N 2396 C CA . LYS A 302 ? 0.5007 0.4742 0.3271 0.0475 0.0781 -0.1288 343 LYS A CA 2397 C C . LYS A 302 ? 0.4915 0.4696 0.3406 0.0436 0.0712 -0.1262 343 LYS A C 2398 O O . LYS A 302 ? 0.4797 0.4596 0.3443 0.0443 0.0720 -0.1292 343 LYS A O 2399 C CB . LYS A 302 ? 0.5340 0.4984 0.3460 0.0514 0.0731 -0.1387 343 LYS A CB 2400 C CG . LYS A 302 ? 0.5102 0.4697 0.3190 0.0495 0.0596 -0.1408 343 LYS A CG 2401 C CD . LYS A 302 ? 0.5860 0.5362 0.3802 0.0538 0.0554 -0.1514 343 LYS A CD 2402 C CE . LYS A 302 ? 0.6261 0.5712 0.4147 0.0523 0.0420 -0.1540 343 LYS A CE 2403 N NZ . LYS A 302 ? 0.6852 0.6207 0.4537 0.0572 0.0386 -0.1639 343 LYS A NZ 2404 N N . MET A 303 ? 0.4684 0.4477 0.3189 0.0398 0.0646 -0.1206 344 MET A N 2405 C CA . MET A 303 ? 0.4561 0.4388 0.3259 0.0363 0.0579 -0.1179 344 MET A CA 2406 C C . MET A 303 ? 0.4649 0.4415 0.3326 0.0360 0.0472 -0.1232 344 MET A C 2407 O O . MET A 303 ? 0.4834 0.4544 0.3342 0.0373 0.0431 -0.1266 344 MET A O 2408 C CB . MET A 303 ? 0.4351 0.4232 0.3093 0.0325 0.0572 -0.1089 344 MET A CB 2409 C CG . MET A 303 ? 0.4417 0.4356 0.3184 0.0323 0.0674 -0.1034 344 MET A CG 2410 S SD . MET A 303 ? 0.4353 0.4346 0.3177 0.0278 0.0655 -0.0934 344 MET A SD 2411 C CE . MET A 303 ? 0.3861 0.3896 0.2920 0.0255 0.0598 -0.0922 344 MET A CE 2412 N N . HIS A 304 ? 0.4414 0.4189 0.3264 0.0342 0.0424 -0.1239 345 HIS A N 2413 C CA . HIS A 304 ? 0.4433 0.4157 0.3298 0.0331 0.0323 -0.1281 345 HIS A CA 2414 C C . HIS A 304 ? 0.4144 0.3910 0.3182 0.0290 0.0282 -0.1220 345 HIS A C 2415 O O . HIS A 304 ? 0.4123 0.3905 0.3314 0.0286 0.0293 -0.1215 345 HIS A O 2416 C CB . HIS A 304 ? 0.4572 0.4240 0.3474 0.0357 0.0310 -0.1368 345 HIS A CB 2417 C CG . HIS A 304 ? 0.5056 0.4691 0.3822 0.0404 0.0374 -0.1428 345 HIS A CG 2418 N ND1 . HIS A 304 ? 0.5327 0.5005 0.4128 0.0425 0.0475 -0.1414 345 HIS A ND1 2419 C CD2 . HIS A 304 ? 0.5267 0.4830 0.3866 0.0437 0.0353 -0.1507 345 HIS A CD2 2420 C CE1 . HIS A 304 ? 0.5452 0.5087 0.4111 0.0468 0.0521 -0.1477 345 HIS A CE1 2421 N NE2 . HIS A 304 ? 0.5780 0.5342 0.4305 0.0478 0.0448 -0.1535 345 HIS A NE2 2422 N N . ILE A 305 ? 0.4020 0.3800 0.3027 0.0263 0.0234 -0.1175 346 ILE A N 2423 C CA . ILE A 305 ? 0.3881 0.3705 0.3039 0.0226 0.0203 -0.1111 346 ILE A CA 2424 C C . ILE A 305 ? 0.4036 0.3828 0.3209 0.0206 0.0109 -0.1131 346 ILE A C 2425 O O . ILE A 305 ? 0.4227 0.3996 0.3273 0.0209 0.0068 -0.1145 346 ILE A O 2426 C CB . ILE A 305 ? 0.3849 0.3731 0.2991 0.0211 0.0240 -0.1030 346 ILE A CB 2427 C CG1 . ILE A 305 ? 0.4106 0.4021 0.3228 0.0230 0.0336 -0.1016 346 ILE A CG1 2428 C CG2 . ILE A 305 ? 0.3594 0.3517 0.2888 0.0179 0.0213 -0.0971 346 ILE A CG2 2429 C CD1 . ILE A 305 ? 0.4323 0.4261 0.3597 0.0240 0.0375 -0.1024 346 ILE A CD1 2430 N N . HIS A 306 ? 0.3853 0.3641 0.3182 0.0188 0.0076 -0.1132 347 HIS A N 2431 C CA . HIS A 306 ? 0.3940 0.3698 0.3318 0.0167 -0.0009 -0.1157 347 HIS A CA 2432 C C . HIS A 306 ? 0.3763 0.3556 0.3302 0.0133 -0.0028 -0.1096 347 HIS A C 2433 O O . HIS A 306 ? 0.3820 0.3591 0.3450 0.0112 -0.0087 -0.1114 347 HIS A O 2434 C CB . HIS A 306 ? 0.4018 0.3711 0.3418 0.0182 -0.0037 -0.1243 347 HIS A CB 2435 C CG . HIS A 306 ? 0.4692 0.4345 0.3925 0.0222 -0.0015 -0.1309 347 HIS A CG 2436 N ND1 . HIS A 306 ? 0.5277 0.4916 0.4506 0.0251 0.0049 -0.1340 347 HIS A ND1 2437 C CD2 . HIS A 306 ? 0.5125 0.4748 0.4183 0.0239 -0.0045 -0.1346 347 HIS A CD2 2438 C CE1 . HIS A 306 ? 0.5478 0.5079 0.4536 0.0285 0.0061 -0.1397 347 HIS A CE1 2439 N NE2 . HIS A 306 ? 0.5822 0.5410 0.4767 0.0279 0.0004 -0.1400 347 HIS A NE2 2440 N N . SER A 307 ? 0.3508 0.3354 0.3079 0.0127 0.0022 -0.1025 348 SER A N 2441 C CA . SER A 307 ? 0.3348 0.3228 0.3047 0.0100 0.0013 -0.0961 348 SER A CA 2442 C C . SER A 307 ? 0.3473 0.3361 0.3166 0.0077 -0.0048 -0.0947 348 SER A C 2443 O O . SER A 307 ? 0.3581 0.3466 0.3153 0.0083 -0.0072 -0.0964 348 SER A O 2444 C CB . SER A 307 ? 0.3287 0.3220 0.2994 0.0103 0.0070 -0.0894 348 SER A CB 2445 O OG . SER A 307 ? 0.3325 0.3255 0.3048 0.0127 0.0123 -0.0912 348 SER A OG 2446 N N . THR A 308 ? 0.3303 0.3204 0.3127 0.0053 -0.0069 -0.0912 349 THR A N 2447 C CA . THR A 308 ? 0.3334 0.3252 0.3179 0.0031 -0.0124 -0.0898 349 THR A CA 2448 C C . THR A 308 ? 0.3182 0.3147 0.3098 0.0015 -0.0103 -0.0820 349 THR A C 2449 O O . THR A 308 ? 0.3249 0.3220 0.3244 0.0015 -0.0064 -0.0785 349 THR A O 2450 C CB . THR A 308 ? 0.3562 0.3445 0.3507 0.0013 -0.0182 -0.0944 349 THR A CB 2451 O OG1 . THR A 308 ? 0.4139 0.4009 0.4225 0.0002 -0.0157 -0.0924 349 THR A OG1 2452 C CG2 . THR A 308 ? 0.3680 0.3509 0.3544 0.0032 -0.0211 -0.1030 349 THR A CG2 2453 N N . ASN A 309 ? 0.3132 0.3127 0.3011 0.0006 -0.0132 -0.0795 350 ASN A N 2454 C CA . ASN A 309 ? 0.3063 0.3100 0.3007 -0.0008 -0.0119 -0.0726 350 ASN A CA 2455 C C . ASN A 309 ? 0.3137 0.3174 0.3208 -0.0030 -0.0159 -0.0729 350 ASN A C 2456 O O . ASN A 309 ? 0.3439 0.3462 0.3512 -0.0037 -0.0216 -0.0774 350 ASN A O 2457 C CB . ASN A 309 ? 0.3129 0.3196 0.2975 -0.0004 -0.0129 -0.0697 350 ASN A CB 2458 C CG . ASN A 309 ? 0.3532 0.3602 0.3262 0.0015 -0.0083 -0.0688 350 ASN A CG 2459 O OD1 . ASN A 309 ? 0.3799 0.3870 0.3552 0.0023 -0.0034 -0.0680 350 ASN A OD1 2460 N ND2 . ASN A 309 ? 0.3887 0.3956 0.3493 0.0022 -0.0098 -0.0689 350 ASN A ND2 2461 N N . GLU A 310 ? 0.3042 0.3093 0.3220 -0.0041 -0.0130 -0.0680 351 GLU A N 2462 C CA . GLU A 310 ? 0.3163 0.3210 0.3482 -0.0064 -0.0151 -0.0678 351 GLU A CA 2463 C C . GLU A 310 ? 0.2866 0.2950 0.3245 -0.0070 -0.0121 -0.0606 351 GLU A C 2464 O O . GLU A 310 ? 0.2767 0.2852 0.3131 -0.0058 -0.0072 -0.0565 351 GLU A O 2465 C CB . GLU A 310 ? 0.3383 0.3383 0.3790 -0.0067 -0.0131 -0.0697 351 GLU A CB 2466 C CG A GLU A 310 ? 0.3781 0.3736 0.4128 -0.0054 -0.0143 -0.0765 351 GLU A CG 2467 C CG B GLU A 310 ? 0.3823 0.3815 0.4390 -0.0096 -0.0151 -0.0695 351 GLU A CG 2468 C CD A GLU A 310 ? 0.4453 0.4357 0.4915 -0.0063 -0.0143 -0.0792 351 GLU A CD 2469 C CD B GLU A 310 ? 0.4557 0.4501 0.5232 -0.0102 -0.0115 -0.0685 351 GLU A CD 2470 O OE1 A GLU A 310 ? 0.5063 0.4935 0.5545 -0.0070 -0.0191 -0.0859 351 GLU A OE1 2471 O OE1 B GLU A 310 ? 0.4680 0.4585 0.5426 -0.0115 -0.0145 -0.0737 351 GLU A OE1 2472 O OE2 A GLU A 310 ? 0.4406 0.4298 0.4940 -0.0063 -0.0099 -0.0747 351 GLU A OE2 2473 O OE2 B GLU A 310 ? 0.4185 0.4127 0.4877 -0.0093 -0.0061 -0.0625 351 GLU A OE2 2474 N N . VAL A 311 ? 0.2769 0.2881 0.3221 -0.0087 -0.0149 -0.0595 352 VAL A N 2475 C CA . VAL A 311 ? 0.2608 0.2750 0.3128 -0.0092 -0.0114 -0.0530 352 VAL A CA 2476 C C . VAL A 311 ? 0.2573 0.2683 0.3204 -0.0101 -0.0074 -0.0509 352 VAL A C 2477 O O . VAL A 311 ? 0.2709 0.2793 0.3441 -0.0120 -0.0092 -0.0541 352 VAL A O 2478 C CB . VAL A 311 ? 0.2553 0.2735 0.3136 -0.0106 -0.0151 -0.0526 352 VAL A CB 2479 C CG1 . VAL A 311 ? 0.2701 0.2910 0.3356 -0.0108 -0.0108 -0.0462 352 VAL A CG1 2480 C CG2 . VAL A 311 ? 0.2933 0.3139 0.3394 -0.0093 -0.0190 -0.0536 352 VAL A CG2 2481 N N . THR A 312 ? 0.2393 0.2500 0.3002 -0.0085 -0.0022 -0.0455 353 THR A N 2482 C CA . THR A 312 ? 0.2352 0.2417 0.3026 -0.0083 0.0020 -0.0430 353 THR A CA 2483 C C . THR A 312 ? 0.2117 0.2195 0.2801 -0.0073 0.0067 -0.0359 353 THR A C 2484 O O . THR A 312 ? 0.2083 0.2193 0.2687 -0.0057 0.0071 -0.0334 353 THR A O 2485 C CB . THR A 312 ? 0.2539 0.2570 0.3139 -0.0062 0.0033 -0.0450 353 THR A CB 2486 O OG1 . THR A 312 ? 0.2915 0.2936 0.3482 -0.0067 -0.0008 -0.0519 353 THR A OG1 2487 C CG2 . THR A 312 ? 0.2525 0.2501 0.3191 -0.0057 0.0068 -0.0431 353 THR A CG2 2488 N N . ARG A 313 ? 0.2278 0.2326 0.3057 -0.0081 0.0101 -0.0326 354 ARG A N 2489 C CA . ARG A 313 ? 0.2179 0.2229 0.2957 -0.0066 0.0151 -0.0257 354 ARG A CA 2490 C C . ARG A 313 ? 0.2317 0.2337 0.3000 -0.0032 0.0178 -0.0229 354 ARG A C 2491 O O . ARG A 313 ? 0.2405 0.2382 0.3085 -0.0024 0.0180 -0.0245 354 ARG A O 2492 C CB . ARG A 313 ? 0.2369 0.2394 0.3278 -0.0086 0.0186 -0.0227 354 ARG A CB 2493 C CG . ARG A 313 ? 0.2512 0.2541 0.3410 -0.0069 0.0241 -0.0157 354 ARG A CG 2494 C CD . ARG A 313 ? 0.2689 0.2721 0.3733 -0.0096 0.0273 -0.0133 354 ARG A CD 2495 N NE . ARG A 313 ? 0.2836 0.2936 0.3939 -0.0117 0.0233 -0.0165 354 ARG A NE 2496 C CZ . ARG A 313 ? 0.3062 0.3191 0.4300 -0.0140 0.0250 -0.0152 354 ARG A CZ 2497 N NH1 . ARG A 313 ? 0.3006 0.3099 0.4333 -0.0148 0.0314 -0.0106 354 ARG A NH1 2498 N NH2 . ARG A 313 ? 0.3097 0.3288 0.4381 -0.0154 0.0206 -0.0184 354 ARG A NH2 2499 N N . ILE A 314 ? 0.2073 0.2116 0.2687 -0.0010 0.0194 -0.0188 355 ILE A N 2500 C CA . ILE A 314 ? 0.2099 0.2119 0.2628 0.0025 0.0213 -0.0160 355 ILE A CA 2501 C C . ILE A 314 ? 0.2204 0.2211 0.2725 0.0043 0.0255 -0.0097 355 ILE A C 2502 O O . ILE A 314 ? 0.2162 0.2195 0.2728 0.0029 0.0267 -0.0081 355 ILE A O 2503 C CB . ILE A 314 ? 0.2013 0.2073 0.2448 0.0039 0.0185 -0.0181 355 ILE A CB 2504 C CG1 . ILE A 314 ? 0.1901 0.2011 0.2313 0.0033 0.0173 -0.0171 355 ILE A CG1 2505 C CG2 . ILE A 314 ? 0.2040 0.2105 0.2472 0.0025 0.0153 -0.0240 355 ILE A CG2 2506 C CD1 . ILE A 314 ? 0.2070 0.2208 0.2387 0.0051 0.0156 -0.0174 355 ILE A CD1 2507 N N . TYR A 315 ? 0.2133 0.2098 0.2593 0.0077 0.0275 -0.0064 356 TYR A N 2508 C CA . TYR A 315 ? 0.2116 0.2051 0.2555 0.0099 0.0320 -0.0003 356 TYR A CA 2509 C C . TYR A 315 ? 0.2205 0.2133 0.2530 0.0142 0.0312 0.0015 356 TYR A C 2510 O O . TYR A 315 ? 0.2332 0.2229 0.2623 0.0164 0.0300 0.0009 356 TYR A O 2511 C CB . TYR A 315 ? 0.2217 0.2080 0.2708 0.0101 0.0357 0.0027 356 TYR A CB 2512 C CG . TYR A 315 ? 0.2295 0.2156 0.2918 0.0057 0.0366 0.0009 356 TYR A CG 2513 C CD1 . TYR A 315 ? 0.2554 0.2424 0.3254 0.0038 0.0405 0.0042 356 TYR A CD1 2514 C CD2 . TYR A 315 ? 0.2395 0.2249 0.3069 0.0036 0.0332 -0.0045 356 TYR A CD2 2515 C CE1 . TYR A 315 ? 0.2596 0.2466 0.3437 -0.0004 0.0408 0.0022 356 TYR A CE1 2516 C CE2 . TYR A 315 ? 0.2680 0.2528 0.3480 -0.0004 0.0331 -0.0068 356 TYR A CE2 2517 C CZ . TYR A 315 ? 0.2770 0.2630 0.3657 -0.0025 0.0366 -0.0035 356 TYR A CZ 2518 O OH . TYR A 315 ? 0.3004 0.2862 0.4033 -0.0066 0.0359 -0.0063 356 TYR A OH 2519 N N . ASN A 316 ? 0.2156 0.2106 0.2428 0.0158 0.0320 0.0039 357 ASN A N 2520 C CA . ASN A 316 ? 0.2229 0.2162 0.2393 0.0203 0.0313 0.0060 357 ASN A CA 2521 C C . ASN A 316 ? 0.2332 0.2203 0.2459 0.0234 0.0362 0.0119 357 ASN A C 2522 O O . ASN A 316 ? 0.2761 0.2630 0.2935 0.0220 0.0404 0.0146 357 ASN A O 2523 C CB . ASN A 316 ? 0.2233 0.2217 0.2348 0.0209 0.0294 0.0051 357 ASN A CB 2524 C CG . ASN A 316 ? 0.2268 0.2310 0.2405 0.0181 0.0250 0.0001 357 ASN A CG 2525 O OD1 . ASN A 316 ? 0.2073 0.2116 0.2220 0.0174 0.0228 -0.0029 357 ASN A OD1 2526 N ND2 . ASN A 316 ? 0.2460 0.2546 0.2596 0.0169 0.0241 -0.0005 357 ASN A ND2 2527 N N . VAL A 317 ? 0.2299 0.2120 0.2340 0.0278 0.0355 0.0139 358 VAL A N 2528 C CA . VAL A 317 ? 0.2367 0.2124 0.2340 0.0315 0.0402 0.0200 358 VAL A CA 2529 C C . VAL A 317 ? 0.2506 0.2279 0.2371 0.0351 0.0386 0.0204 358 VAL A C 2530 O O . VAL A 317 ? 0.2484 0.2277 0.2303 0.0369 0.0333 0.0174 358 VAL A O 2531 C CB . VAL A 317 ? 0.2527 0.2205 0.2455 0.0351 0.0403 0.0226 358 VAL A CB 2532 C CG1 . VAL A 317 ? 0.2683 0.2286 0.2533 0.0388 0.0460 0.0295 358 VAL A CG1 2533 C CG2 . VAL A 317 ? 0.2715 0.2377 0.2749 0.0318 0.0406 0.0210 358 VAL A CG2 2534 N N . ILE A 318 ? 0.2563 0.2327 0.2398 0.0363 0.0432 0.0241 359 ILE A N 2535 C CA . ILE A 318 ? 0.2546 0.2323 0.2280 0.0398 0.0418 0.0240 359 ILE A CA 2536 C C . ILE A 318 ? 0.2625 0.2324 0.2249 0.0450 0.0466 0.0298 359 ILE A C 2537 O O . ILE A 318 ? 0.2899 0.2578 0.2555 0.0442 0.0536 0.0339 359 ILE A O 2538 C CB . ILE A 318 ? 0.2550 0.2395 0.2343 0.0368 0.0431 0.0225 359 ILE A CB 2539 C CG1 . ILE A 318 ? 0.2710 0.2623 0.2605 0.0316 0.0389 0.0174 359 ILE A CG1 2540 C CG2 . ILE A 318 ? 0.2678 0.2529 0.2365 0.0407 0.0414 0.0220 359 ILE A CG2 2541 C CD1 . ILE A 318 ? 0.2846 0.2783 0.2701 0.0323 0.0321 0.0131 359 ILE A CD1 2542 N N . GLY A 319 ? 0.2776 0.2431 0.2276 0.0502 0.0429 0.0299 360 GLY A N 2543 C CA . GLY A 319 ? 0.2977 0.2546 0.2340 0.0562 0.0467 0.0354 360 GLY A CA 2544 C C . GLY A 319 ? 0.2958 0.2534 0.2209 0.0602 0.0451 0.0344 360 GLY A C 2545 O O . GLY A 319 ? 0.3160 0.2782 0.2407 0.0601 0.0387 0.0294 360 GLY A O 2546 N N . THR A 320 ? 0.3089 0.2614 0.2248 0.0638 0.0515 0.0391 361 THR A N 2547 C CA . THR A 320 ? 0.3231 0.2757 0.2276 0.0681 0.0504 0.0379 361 THR A CA 2548 C C . THR A 320 ? 0.3540 0.2964 0.2397 0.0758 0.0513 0.0417 361 THR A C 2549 O O . THR A 320 ? 0.3626 0.2982 0.2443 0.0775 0.0584 0.0478 361 THR A O 2550 C CB . THR A 320 ? 0.3487 0.3049 0.2585 0.0660 0.0579 0.0396 361 THR A CB 2551 O OG1 . THR A 320 ? 0.3514 0.3168 0.2781 0.0592 0.0561 0.0357 361 THR A OG1 2552 C CG2 . THR A 320 ? 0.3721 0.3283 0.2708 0.0704 0.0569 0.0379 361 THR A CG2 2553 N N . LEU A 321 ? 0.3441 0.2851 0.2183 0.0805 0.0443 0.0383 362 LEU A N 2554 C CA . LEU A 321 ? 0.3745 0.3057 0.2281 0.0887 0.0444 0.0411 362 LEU A CA 2555 C C . LEU A 321 ? 0.3748 0.3078 0.2210 0.0913 0.0445 0.0386 362 LEU A C 2556 O O . LEU A 321 ? 0.3689 0.3057 0.2150 0.0916 0.0365 0.0327 362 LEU A O 2557 C CB . LEU A 321 ? 0.3829 0.3105 0.2299 0.0925 0.0346 0.0385 362 LEU A CB 2558 C CG . LEU A 321 ? 0.4490 0.3659 0.2738 0.1017 0.0326 0.0408 362 LEU A CG 2559 C CD1 . LEU A 321 ? 0.4986 0.4065 0.3134 0.1048 0.0427 0.0490 362 LEU A CD1 2560 C CD2 . LEU A 321 ? 0.4566 0.3711 0.2793 0.1044 0.0227 0.0381 362 LEU A CD2 2561 N N . ARG A 322 ? 0.3645 0.2948 0.2055 0.0930 0.0538 0.0429 363 ARG A N 2562 C CA . ARG A 322 ? 0.3879 0.3207 0.2243 0.0950 0.0554 0.0405 363 ARG A CA 2563 C C . ARG A 322 ? 0.3959 0.3225 0.2128 0.1027 0.0485 0.0374 363 ARG A C 2564 O O . ARG A 322 ? 0.4205 0.3374 0.2206 0.1091 0.0483 0.0406 363 ARG A O 2565 C CB . ARG A 322 ? 0.3939 0.3243 0.2284 0.0959 0.0680 0.0466 363 ARG A CB 2566 C CG . ARG A 322 ? 0.4596 0.3918 0.2884 0.0988 0.0709 0.0445 363 ARG A CG 2567 C CD . ARG A 322 ? 0.5838 0.5156 0.4152 0.0986 0.0841 0.0502 363 ARG A CD 2568 N NE . ARG A 322 ? 0.6879 0.6137 0.5187 0.0984 0.0914 0.0574 363 ARG A NE 2569 C CZ . ARG A 322 ? 0.7287 0.6434 0.5405 0.1051 0.0958 0.0627 363 ARG A CZ 2570 N NH1 . ARG A 322 ? 0.7692 0.6771 0.5593 0.1131 0.0936 0.0615 363 ARG A NH1 2571 N NH2 . ARG A 322 ? 0.7489 0.6585 0.5630 0.1038 0.1023 0.0694 363 ARG A NH2 2572 N N . GLY A 323 ? 0.3818 0.3135 0.2006 0.1023 0.0425 0.0312 364 GLY A N 2573 C CA . GLY A 323 ? 0.4013 0.3276 0.2031 0.1094 0.0356 0.0273 364 GLY A CA 2574 C C . GLY A 323 ? 0.4177 0.3363 0.2008 0.1166 0.0426 0.0304 364 GLY A C 2575 O O . GLY A 323 ? 0.4391 0.3597 0.2258 0.1153 0.0525 0.0335 364 GLY A O 2576 N N . ALA A 324 ? 0.4450 0.3546 0.2081 0.1245 0.0372 0.0293 365 ALA A N 2577 C CA . ALA A 324 ? 0.4668 0.3676 0.2085 0.1326 0.0433 0.0319 365 ALA A CA 2578 C C . ALA A 324 ? 0.4796 0.3830 0.2188 0.1342 0.0428 0.0268 365 ALA A C 2579 O O . ALA A 324 ? 0.5041 0.4034 0.2318 0.1388 0.0517 0.0294 365 ALA A O 2580 C CB . ALA A 324 ? 0.4891 0.3790 0.2094 0.1408 0.0366 0.0319 365 ALA A CB 2581 N N . VAL A 325 ? 0.4605 0.3698 0.2089 0.1315 0.0326 0.0194 366 VAL A N 2582 C CA . VAL A 325 ? 0.4790 0.3893 0.2234 0.1340 0.0299 0.0136 366 VAL A CA 2583 C C . VAL A 325 ? 0.4527 0.3744 0.2196 0.1259 0.0299 0.0106 366 VAL A C 2584 O O . VAL A 325 ? 0.4453 0.3696 0.2143 0.1260 0.0351 0.0097 366 VAL A O 2585 C CB . VAL A 325 ? 0.5022 0.4072 0.2344 0.1394 0.0168 0.0070 366 VAL A CB 2586 C CG1 . VAL A 325 ? 0.5162 0.4221 0.2460 0.1415 0.0135 0.0005 366 VAL A CG1 2587 C CG2 . VAL A 325 ? 0.5479 0.4408 0.2555 0.1485 0.0163 0.0098 366 VAL A CG2 2588 N N . GLU A 326 ? 0.4067 0.3351 0.1903 0.1190 0.0242 0.0091 367 GLU A N 2589 C CA . GLU A 326 ? 0.4058 0.3446 0.2104 0.1111 0.0240 0.0069 367 GLU A CA 2590 C C . GLU A 326 ? 0.3611 0.3058 0.1819 0.1039 0.0289 0.0114 367 GLU A C 2591 O O . GLU A 326 ? 0.3479 0.2975 0.1810 0.0986 0.0231 0.0094 367 GLU A O 2592 C CB . GLU A 326 ? 0.3958 0.3377 0.2068 0.1090 0.0123 0.0001 367 GLU A CB 2593 C CG . GLU A 326 ? 0.4463 0.3823 0.2430 0.1157 0.0060 -0.0054 367 GLU A CG 2594 C CD . GLU A 326 ? 0.4721 0.4122 0.2792 0.1122 -0.0046 -0.0118 367 GLU A CD 2595 O OE1 . GLU A 326 ? 0.4803 0.4259 0.2985 0.1082 -0.0043 -0.0141 367 GLU A OE1 2596 O OE2 . GLU A 326 ? 0.5039 0.4416 0.3083 0.1137 -0.0132 -0.0146 367 GLU A OE2 2597 N N . PRO A 327 ? 0.3740 0.3181 0.1953 0.1037 0.0399 0.0172 368 PRO A N 2598 C CA . PRO A 327 ? 0.3624 0.3114 0.1989 0.0972 0.0443 0.0211 368 PRO A CA 2599 C C . PRO A 327 ? 0.3420 0.3012 0.1986 0.0896 0.0424 0.0182 368 PRO A C 2600 O O . PRO A 327 ? 0.3463 0.3096 0.2155 0.0839 0.0429 0.0197 368 PRO A O 2601 C CB . PRO A 327 ? 0.3860 0.3320 0.2189 0.0992 0.0567 0.0274 368 PRO A CB 2602 C CG . PRO A 327 ? 0.4054 0.3491 0.2277 0.1045 0.0594 0.0257 368 PRO A CG 2603 C CD . PRO A 327 ? 0.4002 0.3388 0.2081 0.1097 0.0490 0.0205 368 PRO A CD 2604 N N . ASP A 328 ? 0.3405 0.3030 0.1990 0.0897 0.0399 0.0141 369 ASP A N 2605 C CA . ASP A 328 ? 0.3357 0.3069 0.2116 0.0830 0.0374 0.0114 369 ASP A CA 2606 C C . ASP A 328 ? 0.3126 0.2858 0.1919 0.0807 0.0271 0.0065 369 ASP A C 2607 O O . ASP A 328 ? 0.3000 0.2785 0.1888 0.0771 0.0238 0.0033 369 ASP A O 2608 C CB . ASP A 328 ? 0.3385 0.3124 0.2164 0.0842 0.0408 0.0100 369 ASP A CB 2609 C CG . ASP A 328 ? 0.4118 0.3816 0.2780 0.0894 0.0350 0.0053 369 ASP A CG 2610 O OD1 . ASP A 328 ? 0.4324 0.3954 0.2846 0.0942 0.0305 0.0039 369 ASP A OD1 2611 O OD2 . ASP A 328 ? 0.4331 0.4061 0.3040 0.0892 0.0348 0.0026 369 ASP A OD2 2612 N N . ARG A 329 ? 0.3238 0.2925 0.1955 0.0830 0.0219 0.0058 370 ARG A N 2613 C CA . ARG A 329 ? 0.3019 0.2730 0.1790 0.0803 0.0127 0.0015 370 ARG A CA 2614 C C . ARG A 329 ? 0.3055 0.2767 0.1866 0.0780 0.0123 0.0037 370 ARG A C 2615 O O . ARG A 329 ? 0.3096 0.2748 0.1809 0.0821 0.0147 0.0069 370 ARG A O 2616 C CB . ARG A 329 ? 0.3059 0.2716 0.1709 0.0860 0.0052 -0.0027 370 ARG A CB 2617 C CG . ARG A 329 ? 0.3088 0.2742 0.1705 0.0882 0.0050 -0.0058 370 ARG A CG 2618 C CD . ARG A 329 ? 0.3136 0.2857 0.1899 0.0822 0.0004 -0.0092 370 ARG A CD 2619 N NE . ARG A 329 ? 0.3128 0.2852 0.1889 0.0834 0.0000 -0.0121 370 ARG A NE 2620 C CZ . ARG A 329 ? 0.3207 0.2970 0.2034 0.0813 0.0058 -0.0105 370 ARG A CZ 2621 N NH1 . ARG A 329 ? 0.3028 0.2826 0.1917 0.0786 0.0132 -0.0060 370 ARG A NH1 2622 N NH2 . ARG A 329 ? 0.3312 0.3077 0.2150 0.0822 0.0039 -0.0137 370 ARG A NH2 2623 N N . TYR A 330 ? 0.2701 0.2475 0.1650 0.0718 0.0098 0.0023 371 TYR A N 2624 C CA . TYR A 330 ? 0.2737 0.2519 0.1743 0.0691 0.0105 0.0044 371 TYR A CA 2625 C C . TYR A 330 ? 0.2788 0.2581 0.1826 0.0682 0.0027 0.0009 371 TYR A C 2626 O O . TYR A 330 ? 0.2890 0.2731 0.2007 0.0648 -0.0016 -0.0028 371 TYR A O 2627 C CB . TYR A 330 ? 0.2525 0.2371 0.1673 0.0624 0.0146 0.0057 371 TYR A CB 2628 C CG . TYR A 330 ? 0.2680 0.2534 0.1843 0.0621 0.0224 0.0089 371 TYR A CG 2629 C CD1 . TYR A 330 ? 0.3136 0.2933 0.2197 0.0670 0.0281 0.0126 371 TYR A CD1 2630 C CD2 . TYR A 330 ? 0.2607 0.2525 0.1890 0.0570 0.0240 0.0083 371 TYR A CD2 2631 C CE1 . TYR A 330 ? 0.3094 0.2906 0.2189 0.0664 0.0359 0.0155 371 TYR A CE1 2632 C CE2 . TYR A 330 ? 0.2641 0.2575 0.1962 0.0565 0.0308 0.0109 371 TYR A CE2 2633 C CZ . TYR A 330 ? 0.3014 0.2899 0.2251 0.0610 0.0370 0.0145 371 TYR A CZ 2634 O OH . TYR A 330 ? 0.2970 0.2880 0.2266 0.0602 0.0442 0.0170 371 TYR A OH 2635 N N . VAL A 331 ? 0.2674 0.2424 0.1660 0.0712 0.0012 0.0022 372 VAL A N 2636 C CA . VAL A 331 ? 0.2628 0.2395 0.1668 0.0702 -0.0055 -0.0007 372 VAL A CA 2637 C C . VAL A 331 ? 0.2653 0.2438 0.1775 0.0664 -0.0015 0.0021 372 VAL A C 2638 O O . VAL A 331 ? 0.2845 0.2584 0.1916 0.0685 0.0034 0.0063 372 VAL A O 2639 C CB . VAL A 331 ? 0.2903 0.2605 0.1823 0.0770 -0.0113 -0.0019 372 VAL A CB 2640 C CG1 . VAL A 331 ? 0.2796 0.2522 0.1795 0.0758 -0.0175 -0.0045 372 VAL A CG1 2641 C CG2 . VAL A 331 ? 0.2916 0.2602 0.1767 0.0802 -0.0161 -0.0057 372 VAL A CG2 2642 N N . ILE A 332 ? 0.2385 0.2231 0.1632 0.0611 -0.0032 -0.0003 373 ILE A N 2643 C CA . ILE A 332 ? 0.2443 0.2307 0.1771 0.0573 0.0009 0.0017 373 ILE A CA 2644 C C . ILE A 332 ? 0.2398 0.2268 0.1771 0.0575 -0.0035 -0.0002 373 ILE A C 2645 O O . ILE A 332 ? 0.2643 0.2552 0.2067 0.0562 -0.0086 -0.0041 373 ILE A O 2646 C CB . ILE A 332 ? 0.2228 0.2159 0.1661 0.0511 0.0032 0.0006 373 ILE A CB 2647 C CG1 . ILE A 332 ? 0.2700 0.2630 0.2099 0.0514 0.0070 0.0022 373 ILE A CG1 2648 C CG2 . ILE A 332 ? 0.2598 0.2542 0.2111 0.0473 0.0070 0.0022 373 ILE A CG2 2649 C CD1 . ILE A 332 ? 0.3345 0.3339 0.2842 0.0457 0.0082 0.0008 373 ILE A CD1 2650 N N . LEU A 333 ? 0.2407 0.2239 0.1770 0.0589 -0.0013 0.0025 374 LEU A N 2651 C CA . LEU A 333 ? 0.2295 0.2137 0.1723 0.0586 -0.0046 0.0007 374 LEU A CA 2652 C C . LEU A 333 ? 0.2501 0.2366 0.2018 0.0537 0.0004 0.0019 374 LEU A C 2653 O O . LEU A 333 ? 0.2563 0.2387 0.2058 0.0540 0.0054 0.0058 374 LEU A O 2654 C CB . LEU A 333 ? 0.2677 0.2444 0.2014 0.0648 -0.0066 0.0030 374 LEU A CB 2655 C CG . LEU A 333 ? 0.2513 0.2284 0.1918 0.0652 -0.0097 0.0016 374 LEU A CG 2656 C CD1 . LEU A 333 ? 0.2706 0.2537 0.2188 0.0644 -0.0163 -0.0038 374 LEU A CD1 2657 C CD2 . LEU A 333 ? 0.2927 0.2608 0.2221 0.0723 -0.0116 0.0048 374 LEU A CD2 2658 N N . GLY A 334 ? 0.2495 0.2421 0.2113 0.0494 -0.0008 -0.0015 375 GLY A N 2659 C CA . GLY A 334 ? 0.2407 0.2354 0.2104 0.0449 0.0034 -0.0012 375 GLY A CA 2660 C C . GLY A 334 ? 0.2541 0.2517 0.2319 0.0433 0.0015 -0.0043 375 GLY A C 2661 O O . GLY A 334 ? 0.2619 0.2632 0.2428 0.0433 -0.0024 -0.0075 375 GLY A O 2662 N N . GLY A 335 ? 0.2472 0.2433 0.2294 0.0416 0.0046 -0.0035 376 GLY A N 2663 C CA . GLY A 335 ? 0.2537 0.2533 0.2443 0.0397 0.0036 -0.0071 376 GLY A CA 2664 C C . GLY A 335 ? 0.2410 0.2392 0.2359 0.0368 0.0076 -0.0065 376 GLY A C 2665 O O . GLY A 335 ? 0.2617 0.2556 0.2539 0.0370 0.0108 -0.0030 376 GLY A O 2666 N N . HIS A 336 ? 0.2250 0.2265 0.2268 0.0342 0.0078 -0.0100 377 HIS A N 2667 C CA . HIS A 336 ? 0.2071 0.2071 0.2130 0.0312 0.0111 -0.0102 377 HIS A CA 2668 C C . HIS A 336 ? 0.2292 0.2238 0.2376 0.0333 0.0119 -0.0094 377 HIS A C 2669 O O . HIS A 336 ? 0.2485 0.2411 0.2562 0.0372 0.0095 -0.0094 377 HIS A O 2670 C CB . HIS A 336 ? 0.1981 0.2037 0.2086 0.0271 0.0113 -0.0144 377 HIS A CB 2671 C CG . HIS A 336 ? 0.1928 0.2009 0.2078 0.0276 0.0102 -0.0181 377 HIS A CG 2672 N ND1 . HIS A 336 ? 0.2083 0.2153 0.2279 0.0264 0.0118 -0.0206 377 HIS A ND1 2673 C CD2 . HIS A 336 ? 0.2061 0.2184 0.2228 0.0285 0.0082 -0.0203 377 HIS A CD2 2674 C CE1 . HIS A 336 ? 0.2013 0.2116 0.2245 0.0271 0.0112 -0.0240 377 HIS A CE1 2675 N NE2 . HIS A 336 ? 0.2041 0.2178 0.2262 0.0282 0.0091 -0.0237 377 HIS A NE2 2676 N N . ARG A 337 ? 0.2202 0.2122 0.2321 0.0308 0.0148 -0.0091 378 ARG A N 2677 C CA . ARG A 337 ? 0.2352 0.2208 0.2500 0.0323 0.0163 -0.0078 378 ARG A CA 2678 C C . ARG A 337 ? 0.2392 0.2261 0.2612 0.0294 0.0169 -0.0123 378 ARG A C 2679 O O . ARG A 337 ? 0.2394 0.2222 0.2648 0.0310 0.0169 -0.0131 378 ARG A O 2680 C CB . ARG A 337 ? 0.2520 0.2328 0.2656 0.0314 0.0198 -0.0031 378 ARG A CB 2681 C CG . ARG A 337 ? 0.2664 0.2392 0.2828 0.0327 0.0220 -0.0006 378 ARG A CG 2682 C CD . ARG A 337 ? 0.2777 0.2466 0.2949 0.0310 0.0264 0.0039 378 ARG A CD 2683 N NE . ARG A 337 ? 0.2516 0.2246 0.2762 0.0256 0.0276 0.0012 378 ARG A NE 2684 C CZ . ARG A 337 ? 0.2582 0.2362 0.2823 0.0232 0.0282 0.0012 378 ARG A CZ 2685 N NH1 . ARG A 337 ? 0.2507 0.2303 0.2673 0.0254 0.0282 0.0039 378 ARG A NH1 2686 N NH2 . ARG A 337 ? 0.2578 0.2391 0.2893 0.0187 0.0283 -0.0018 378 ARG A NH2 2687 N N . ASP A 338 ? 0.2281 0.2200 0.2518 0.0254 0.0171 -0.0154 379 ASP A N 2688 C CA . ASP A 338 ? 0.2207 0.2133 0.2497 0.0229 0.0174 -0.0202 379 ASP A CA 2689 C C . ASP A 338 ? 0.2267 0.2221 0.2569 0.0248 0.0161 -0.0239 379 ASP A C 2690 O O . ASP A 338 ? 0.2318 0.2315 0.2595 0.0260 0.0147 -0.0239 379 ASP A O 2691 C CB . ASP A 338 ? 0.2088 0.2059 0.2378 0.0187 0.0174 -0.0225 379 ASP A CB 2692 C CG . ASP A 338 ? 0.2243 0.2277 0.2491 0.0184 0.0160 -0.0235 379 ASP A CG 2693 O OD1 . ASP A 338 ? 0.2176 0.2219 0.2386 0.0199 0.0154 -0.0203 379 ASP A OD1 2694 O OD2 . ASP A 338 ? 0.2178 0.2245 0.2427 0.0166 0.0157 -0.0275 379 ASP A OD2 2695 N N . SER A 339 ? 0.2243 0.2175 0.2590 0.0249 0.0167 -0.0274 380 SER A N 2696 C CA . SER A 339 ? 0.2270 0.2231 0.2640 0.0269 0.0161 -0.0311 380 SER A CA 2697 C C . SER A 339 ? 0.2429 0.2399 0.2821 0.0245 0.0174 -0.0366 380 SER A C 2698 O O . SER A 339 ? 0.2454 0.2394 0.2854 0.0221 0.0179 -0.0373 380 SER A O 2699 C CB . SER A 339 ? 0.2524 0.2436 0.2924 0.0311 0.0154 -0.0297 380 SER A CB 2700 O OG . SER A 339 ? 0.2717 0.2558 0.3147 0.0308 0.0166 -0.0294 380 SER A OG 2701 N N . TRP A 340 ? 0.2297 0.2309 0.2703 0.0254 0.0180 -0.0405 381 TRP A N 2702 C CA . TRP A 340 ? 0.2352 0.2362 0.2767 0.0241 0.0195 -0.0459 381 TRP A CA 2703 C C . TRP A 340 ? 0.2608 0.2555 0.3073 0.0259 0.0197 -0.0477 381 TRP A C 2704 O O . TRP A 340 ? 0.2581 0.2493 0.3052 0.0240 0.0198 -0.0504 381 TRP A O 2705 C CB . TRP A 340 ? 0.2375 0.2446 0.2788 0.0246 0.0212 -0.0495 381 TRP A CB 2706 C CG . TRP A 340 ? 0.2301 0.2421 0.2657 0.0218 0.0214 -0.0487 381 TRP A CG 2707 C CD1 . TRP A 340 ? 0.2294 0.2466 0.2641 0.0217 0.0213 -0.0465 381 TRP A CD1 2708 C CD2 . TRP A 340 ? 0.2122 0.2236 0.2425 0.0186 0.0212 -0.0499 381 TRP A CD2 2709 N NE1 . TRP A 340 ? 0.2198 0.2394 0.2485 0.0187 0.0215 -0.0460 381 TRP A NE1 2710 C CE2 . TRP A 340 ? 0.2242 0.2403 0.2498 0.0169 0.0212 -0.0481 381 TRP A CE2 2711 C CE3 . TRP A 340 ? 0.2502 0.2573 0.2797 0.0171 0.0205 -0.0527 381 TRP A CE3 2712 C CZ2 . TRP A 340 ? 0.2231 0.2397 0.2427 0.0141 0.0206 -0.0486 381 TRP A CZ2 2713 C CZ3 . TRP A 340 ? 0.2264 0.2344 0.2503 0.0141 0.0194 -0.0536 381 TRP A CZ3 2714 C CH2 . TRP A 340 ? 0.2187 0.2313 0.2375 0.0129 0.0194 -0.0513 381 TRP A CH2 2715 N N . VAL A 341 ? 0.2455 0.2384 0.2961 0.0297 0.0192 -0.0463 382 VAL A N 2716 C CA . VAL A 341 ? 0.2443 0.2299 0.2998 0.0319 0.0192 -0.0472 382 VAL A CA 2717 C C . VAL A 341 ? 0.2535 0.2347 0.3094 0.0347 0.0176 -0.0412 382 VAL A C 2718 O O . VAL A 341 ? 0.2482 0.2265 0.3012 0.0332 0.0175 -0.0367 382 VAL A O 2719 C CB . VAL A 341 ? 0.2514 0.2379 0.3116 0.0345 0.0203 -0.0529 382 VAL A CB 2720 C CG1 . VAL A 341 ? 0.2798 0.2577 0.3446 0.0357 0.0202 -0.0542 382 VAL A CG1 2721 C CG2 . VAL A 341 ? 0.2840 0.2751 0.3414 0.0320 0.0224 -0.0584 382 VAL A CG2 2722 N N . PHE A 342 ? 0.2455 0.2260 0.3048 0.0392 0.0165 -0.0410 383 PHE A N 2723 C CA . PHE A 342 ? 0.2527 0.2276 0.3109 0.0426 0.0147 -0.0353 383 PHE A CA 2724 C C . PHE A 342 ? 0.2680 0.2469 0.3211 0.0436 0.0127 -0.0315 383 PHE A C 2725 O O . PHE A 342 ? 0.2817 0.2556 0.3308 0.0458 0.0115 -0.0262 383 PHE A O 2726 C CB . PHE A 342 ? 0.2580 0.2294 0.3219 0.0476 0.0133 -0.0366 383 PHE A CB 2727 C CG . PHE A 342 ? 0.2901 0.2561 0.3590 0.0472 0.0150 -0.0404 383 PHE A CG 2728 C CD1 . PHE A 342 ? 0.2879 0.2450 0.3567 0.0459 0.0159 -0.0375 383 PHE A CD1 2729 C CD2 . PHE A 342 ? 0.3063 0.2764 0.3803 0.0477 0.0162 -0.0471 383 PHE A CD2 2730 C CE1 . PHE A 342 ? 0.3149 0.2666 0.3891 0.0452 0.0171 -0.0417 383 PHE A CE1 2731 C CE2 . PHE A 342 ? 0.2813 0.2459 0.3595 0.0475 0.0176 -0.0514 383 PHE A CE2 2732 C CZ . PHE A 342 ? 0.3015 0.2571 0.3798 0.0460 0.0177 -0.0489 383 PHE A CZ 2733 N N . GLY A 343 ? 0.2555 0.2429 0.3084 0.0422 0.0126 -0.0341 384 GLY A N 2734 C CA . GLY A 343 ? 0.2590 0.2503 0.3074 0.0428 0.0104 -0.0310 384 GLY A CA 2735 C C . GLY A 343 ? 0.2580 0.2477 0.3067 0.0481 0.0066 -0.0286 384 GLY A C 2736 O O . GLY A 343 ? 0.2576 0.2467 0.3004 0.0493 0.0045 -0.0248 384 GLY A O 2737 N N . GLY A 344 ? 0.2528 0.2425 0.3085 0.0516 0.0055 -0.0314 385 GLY A N 2738 C CA . GLY A 344 ? 0.2590 0.2471 0.3162 0.0572 0.0011 -0.0298 385 GLY A CA 2739 C C . GLY A 344 ? 0.2522 0.2459 0.3073 0.0580 -0.0022 -0.0291 385 GLY A C 2740 O O . GLY A 344 ? 0.2793 0.2691 0.3292 0.0618 -0.0062 -0.0255 385 GLY A O 2741 N N . ILE A 345 ? 0.2415 0.2438 0.3004 0.0545 -0.0008 -0.0326 386 ILE A N 2742 C CA . ILE A 345 ? 0.2286 0.2363 0.2861 0.0542 -0.0036 -0.0321 386 ILE A CA 2743 C C . ILE A 345 ? 0.2339 0.2419 0.2832 0.0496 -0.0012 -0.0299 386 ILE A C 2744 O O . ILE A 345 ? 0.2345 0.2400 0.2764 0.0506 -0.0035 -0.0264 386 ILE A O 2745 C CB . ILE A 345 ? 0.2161 0.2331 0.2842 0.0537 -0.0037 -0.0368 386 ILE A CB 2746 C CG1 . ILE A 345 ? 0.2464 0.2633 0.3230 0.0592 -0.0074 -0.0385 386 ILE A CG1 2747 C CG2 . ILE A 345 ? 0.2398 0.2623 0.3069 0.0520 -0.0059 -0.0365 386 ILE A CG2 2748 C CD1 . ILE A 345 ? 0.2791 0.3052 0.3689 0.0588 -0.0065 -0.0434 386 ILE A CD1 2749 N N . ASP A 346 ? 0.2337 0.2445 0.2841 0.0451 0.0031 -0.0322 387 ASP A N 2750 C CA . ASP A 346 ? 0.2182 0.2305 0.2624 0.0407 0.0050 -0.0309 387 ASP A CA 2751 C C . ASP A 346 ? 0.2251 0.2313 0.2646 0.0388 0.0076 -0.0289 387 ASP A C 2752 O O . ASP A 346 ? 0.2281 0.2338 0.2705 0.0370 0.0103 -0.0316 387 ASP A O 2753 C CB . ASP A 346 ? 0.2104 0.2299 0.2588 0.0372 0.0078 -0.0348 387 ASP A CB 2754 C CG . ASP A 346 ? 0.2128 0.2340 0.2554 0.0330 0.0093 -0.0338 387 ASP A CG 2755 O OD1 . ASP A 346 ? 0.2149 0.2327 0.2512 0.0328 0.0082 -0.0303 387 ASP A OD1 2756 O OD2 . ASP A 346 ? 0.2316 0.2575 0.2757 0.0302 0.0120 -0.0364 387 ASP A OD2 2757 N N . PRO A 347 ? 0.2177 0.2192 0.2507 0.0394 0.0069 -0.0244 388 PRO A N 2758 C CA . PRO A 347 ? 0.2030 0.2043 0.2302 0.0414 0.0040 -0.0212 388 PRO A CA 2759 C C . PRO A 347 ? 0.2284 0.2226 0.2520 0.0465 0.0017 -0.0176 388 PRO A C 2760 O O . PRO A 347 ? 0.2370 0.2297 0.2540 0.0488 -0.0006 -0.0148 388 PRO A O 2761 C CB . PRO A 347 ? 0.2082 0.2086 0.2298 0.0380 0.0064 -0.0186 388 PRO A CB 2762 C CG . PRO A 347 ? 0.2233 0.2186 0.2467 0.0366 0.0095 -0.0181 388 PRO A CG 2763 C CD . PRO A 347 ? 0.2219 0.2187 0.2523 0.0367 0.0098 -0.0226 388 PRO A CD 2764 N N . GLN A 348 ? 0.2361 0.2253 0.2628 0.0485 0.0024 -0.0174 389 GLN A N 2765 C CA . GLN A 348 ? 0.2544 0.2350 0.2749 0.0527 0.0014 -0.0125 389 GLN A CA 2766 C C . GLN A 348 ? 0.2645 0.2444 0.2822 0.0583 -0.0040 -0.0117 389 GLN A C 2767 O O . GLN A 348 ? 0.2660 0.2391 0.2751 0.0621 -0.0052 -0.0072 389 GLN A O 2768 C CB . GLN A 348 ? 0.2696 0.2436 0.2939 0.0537 0.0034 -0.0119 389 GLN A CB 2769 C CG . GLN A 348 ? 0.2568 0.2303 0.2844 0.0484 0.0081 -0.0130 389 GLN A CG 2770 C CD . GLN A 348 ? 0.2527 0.2254 0.2748 0.0451 0.0108 -0.0095 389 GLN A CD 2771 O OE1 . GLN A 348 ? 0.2753 0.2460 0.2899 0.0471 0.0103 -0.0053 389 GLN A OE1 2772 N NE2 . GLN A 348 ? 0.2580 0.2322 0.2840 0.0403 0.0137 -0.0115 389 GLN A NE2 2773 N N . SER A 349 ? 0.2449 0.2316 0.2698 0.0590 -0.0071 -0.0161 390 SER A N 2774 C CA . SER A 349 ? 0.2660 0.2529 0.2889 0.0642 -0.0132 -0.0160 390 SER A CA 2775 C C . SER A 349 ? 0.2613 0.2483 0.2748 0.0641 -0.0149 -0.0138 390 SER A C 2776 O O . SER A 349 ? 0.2790 0.2619 0.2853 0.0691 -0.0195 -0.0117 390 SER A O 2777 C CB . SER A 349 ? 0.2753 0.2702 0.3101 0.0646 -0.0161 -0.0214 390 SER A CB 2778 O OG . SER A 349 ? 0.2841 0.2872 0.3226 0.0599 -0.0146 -0.0242 390 SER A OG 2779 N N . GLY A 350 ? 0.2463 0.2375 0.2592 0.0588 -0.0113 -0.0143 391 GLY A N 2780 C CA . GLY A 350 ? 0.2405 0.2315 0.2446 0.0583 -0.0118 -0.0122 391 GLY A CA 2781 C C . GLY A 350 ? 0.2618 0.2446 0.2557 0.0595 -0.0086 -0.0067 391 GLY A C 2782 O O . GLY A 350 ? 0.2661 0.2448 0.2503 0.0630 -0.0107 -0.0040 391 GLY A O 2783 N N . ALA A 351 ? 0.2402 0.2206 0.2366 0.0565 -0.0035 -0.0053 392 ALA A N 2784 C CA . ALA A 351 ? 0.2646 0.2379 0.2536 0.0568 0.0005 -0.0001 392 ALA A CA 2785 C C . ALA A 351 ? 0.2738 0.2379 0.2548 0.0630 -0.0011 0.0042 392 ALA A C 2786 O O . ALA A 351 ? 0.2802 0.2385 0.2513 0.0649 0.0010 0.0090 392 ALA A O 2787 C CB . ALA A 351 ? 0.2683 0.2410 0.2638 0.0522 0.0056 -0.0001 392 ALA A CB 2788 N N . ALA A 352 ? 0.2816 0.2443 0.2668 0.0664 -0.0048 0.0026 393 ALA A N 2789 C CA . ALA A 352 ? 0.2863 0.2400 0.2636 0.0730 -0.0074 0.0065 393 ALA A CA 2790 C C . ALA A 352 ? 0.3083 0.2610 0.2749 0.0776 -0.0123 0.0074 393 ALA A C 2791 O O . ALA A 352 ? 0.3070 0.2509 0.2614 0.0826 -0.0126 0.0122 393 ALA A O 2792 C CB . ALA A 352 ? 0.2993 0.2528 0.2851 0.0759 -0.0112 0.0036 393 ALA A CB 2793 N N . VAL A 353 ? 0.2836 0.2448 0.2547 0.0762 -0.0162 0.0025 394 VAL A N 2794 C CA . VAL A 353 ? 0.2883 0.2493 0.2504 0.0801 -0.0215 0.0021 394 VAL A CA 2795 C C . VAL A 353 ? 0.2969 0.2549 0.2478 0.0791 -0.0172 0.0059 394 VAL A C 2796 O O . VAL A 353 ? 0.3062 0.2577 0.2437 0.0844 -0.0192 0.0089 394 VAL A O 2797 C CB . VAL A 353 ? 0.2797 0.2509 0.2521 0.0779 -0.0262 -0.0042 394 VAL A CB 2798 C CG1 . VAL A 353 ? 0.2899 0.2625 0.2549 0.0793 -0.0301 -0.0052 394 VAL A CG1 2799 C CG2 . VAL A 353 ? 0.2668 0.2395 0.2478 0.0816 -0.0322 -0.0074 394 VAL A CG2 2800 N N . VAL A 354 ? 0.2799 0.2424 0.2360 0.0727 -0.0114 0.0056 395 VAL A N 2801 C CA . VAL A 354 ? 0.2933 0.2538 0.2409 0.0715 -0.0068 0.0090 395 VAL A CA 2802 C C . VAL A 354 ? 0.2964 0.2465 0.2341 0.0752 -0.0027 0.0155 395 VAL A C 2803 O O . VAL A 354 ? 0.3072 0.2521 0.2322 0.0787 -0.0016 0.0190 395 VAL A O 2804 C CB . VAL A 354 ? 0.2828 0.2494 0.2391 0.0643 -0.0015 0.0078 395 VAL A CB 2805 C CG1 . VAL A 354 ? 0.2728 0.2368 0.2210 0.0638 0.0036 0.0118 395 VAL A CG1 2806 C CG2 . VAL A 354 ? 0.2886 0.2648 0.2528 0.0609 -0.0050 0.0021 395 VAL A CG2 2807 N N . HIS A 355 ? 0.3038 0.2502 0.2469 0.0746 -0.0003 0.0172 396 HIS A N 2808 C CA . HIS A 355 ? 0.3095 0.2454 0.2445 0.0775 0.0045 0.0240 396 HIS A CA 2809 C C . HIS A 355 ? 0.3434 0.2713 0.2635 0.0856 0.0002 0.0269 396 HIS A C 2810 O O . HIS A 355 ? 0.3572 0.2777 0.2643 0.0886 0.0041 0.0324 396 HIS A O 2811 C CB . HIS A 355 ? 0.3224 0.2559 0.2676 0.0756 0.0065 0.0243 396 HIS A CB 2812 C CG . HIS A 355 ? 0.3301 0.2567 0.2750 0.0736 0.0143 0.0300 396 HIS A CG 2813 N ND1 . HIS A 355 ? 0.3385 0.2679 0.2859 0.0687 0.0205 0.0313 396 HIS A ND1 2814 C CD2 . HIS A 355 ? 0.3787 0.2959 0.3228 0.0757 0.0170 0.0346 396 HIS A CD2 2815 C CE1 . HIS A 355 ? 0.3570 0.2795 0.3059 0.0675 0.0267 0.0363 396 HIS A CE1 2816 N NE2 . HIS A 355 ? 0.3872 0.3020 0.3342 0.0715 0.0249 0.0384 396 HIS A NE2 2817 N N . GLU A 356 ? 0.3356 0.2651 0.2569 0.0893 -0.0078 0.0231 397 GLU A N 2818 C CA . GLU A 356 ? 0.3690 0.2907 0.2758 0.0976 -0.0135 0.0252 397 GLU A CA 2819 C C . GLU A 356 ? 0.3634 0.2858 0.2586 0.0999 -0.0156 0.0245 397 GLU A C 2820 O O . GLU A 356 ? 0.3918 0.3054 0.2704 0.1062 -0.0166 0.0283 397 GLU A O 2821 C CB . GLU A 356 ? 0.3830 0.3069 0.2967 0.1008 -0.0221 0.0209 397 GLU A CB 2822 C CG . GLU A 356 ? 0.3744 0.2907 0.2742 0.1100 -0.0301 0.0220 397 GLU A CG 2823 C CD . GLU A 356 ? 0.4599 0.3626 0.3456 0.1157 -0.0274 0.0295 397 GLU A CD 2824 O OE1 . GLU A 356 ? 0.4522 0.3507 0.3380 0.1124 -0.0184 0.0346 397 GLU A OE1 2825 O OE2 . GLU A 356 ? 0.4620 0.3578 0.3364 0.1236 -0.0344 0.0305 397 GLU A OE2 2826 N N . ILE A 357 ? 0.3388 0.2710 0.2419 0.0949 -0.0161 0.0197 398 ILE A N 2827 C CA . ILE A 357 ? 0.3359 0.2689 0.2290 0.0963 -0.0172 0.0188 398 ILE A CA 2828 C C . ILE A 357 ? 0.3505 0.2775 0.2326 0.0964 -0.0087 0.0248 398 ILE A C 2829 O O . ILE A 357 ? 0.3639 0.2843 0.2297 0.1021 -0.0092 0.0272 398 ILE A O 2830 C CB . ILE A 357 ? 0.3110 0.2554 0.2162 0.0905 -0.0192 0.0126 398 ILE A CB 2831 C CG1 . ILE A 357 ? 0.3186 0.2680 0.2317 0.0921 -0.0285 0.0068 398 ILE A CG1 2832 C CG2 . ILE A 357 ? 0.3172 0.2621 0.2131 0.0910 -0.0183 0.0124 398 ILE A CG2 2833 C CD1 . ILE A 357 ? 0.3073 0.2681 0.2358 0.0855 -0.0293 0.0012 398 ILE A CD1 2834 N N . VAL A 358 ? 0.3357 0.2646 0.2267 0.0906 -0.0007 0.0272 399 VAL A N 2835 C CA . VAL A 358 ? 0.3656 0.2891 0.2490 0.0903 0.0084 0.0333 399 VAL A CA 2836 C C . VAL A 358 ? 0.3811 0.2919 0.2490 0.0974 0.0100 0.0398 399 VAL A C 2837 O O . VAL A 358 ? 0.4022 0.3069 0.2552 0.1014 0.0136 0.0437 399 VAL A O 2838 C CB . VAL A 358 ? 0.3496 0.2770 0.2473 0.0829 0.0157 0.0345 399 VAL A CB 2839 C CG1 . VAL A 358 ? 0.3618 0.2837 0.2534 0.0828 0.0253 0.0410 399 VAL A CG1 2840 C CG2 . VAL A 358 ? 0.3447 0.2842 0.2556 0.0762 0.0144 0.0284 399 VAL A CG2 2841 N N . ARG A 359 ? 0.3805 0.2868 0.2512 0.0992 0.0076 0.0410 400 ARG A N 2842 C CA . ARG A 359 ? 0.4046 0.2980 0.2605 0.1063 0.0086 0.0475 400 ARG A CA 2843 C C . ARG A 359 ? 0.4325 0.3207 0.2693 0.1144 0.0024 0.0473 400 ARG A C 2844 O O . ARG A 359 ? 0.4555 0.3335 0.2747 0.1197 0.0067 0.0534 400 ARG A O 2845 C CB . ARG A 359 ? 0.3896 0.2799 0.2527 0.1074 0.0048 0.0476 400 ARG A CB 2846 C CG . ARG A 359 ? 0.4240 0.2998 0.2741 0.1131 0.0087 0.0560 400 ARG A CG 2847 C CD . ARG A 359 ? 0.4459 0.3174 0.2997 0.1167 0.0021 0.0554 400 ARG A CD 2848 N NE . ARG A 359 ? 0.4708 0.3454 0.3209 0.1218 -0.0093 0.0498 400 ARG A NE 2849 C CZ . ARG A 359 ? 0.5223 0.3894 0.3539 0.1302 -0.0148 0.0515 400 ARG A CZ 2850 N NH1 . ARG A 359 ? 0.5088 0.3801 0.3406 0.1339 -0.0258 0.0453 400 ARG A NH1 2851 N NH2 . ARG A 359 ? 0.5393 0.3944 0.3521 0.1350 -0.0093 0.0591 400 ARG A NH2 2852 N N . SER A 360 ? 0.4276 0.3223 0.2675 0.1155 -0.0073 0.0402 401 SER A N 2853 C CA . SER A 360 ? 0.4617 0.3518 0.2847 0.1232 -0.0147 0.0387 401 SER A CA 2854 C C . SER A 360 ? 0.4640 0.3534 0.2754 0.1238 -0.0102 0.0396 401 SER A C 2855 O O . SER A 360 ? 0.4812 0.3607 0.2721 0.1311 -0.0100 0.0432 401 SER A O 2856 C CB . SER A 360 ? 0.4602 0.3575 0.2916 0.1241 -0.0266 0.0307 401 SER A CB 2857 O OG A SER A 360 ? 0.4294 0.3216 0.2438 0.1317 -0.0340 0.0289 401 SER A OG 2858 O OG B SER A 360 ? 0.4767 0.3734 0.3173 0.1248 -0.0304 0.0304 401 SER A OG 2859 N N . PHE A 361 ? 0.4473 0.3465 0.2706 0.1167 -0.0063 0.0365 402 PHE A N 2860 C CA . PHE A 361 ? 0.4506 0.3494 0.2643 0.1172 -0.0014 0.0374 402 PHE A CA 2861 C C . PHE A 361 ? 0.4855 0.3752 0.2879 0.1192 0.0094 0.0459 402 PHE A C 2862 O O . PHE A 361 ? 0.4955 0.3785 0.2801 0.1247 0.0119 0.0485 402 PHE A O 2863 C CB . PHE A 361 ? 0.4170 0.3279 0.2470 0.1089 0.0013 0.0332 402 PHE A CB 2864 C CG . PHE A 361 ? 0.4141 0.3326 0.2497 0.1080 -0.0078 0.0254 402 PHE A CG 2865 C CD1 . PHE A 361 ? 0.4310 0.3466 0.2528 0.1135 -0.0128 0.0228 402 PHE A CD1 2866 C CD2 . PHE A 361 ? 0.3797 0.3082 0.2343 0.1016 -0.0109 0.0206 402 PHE A CD2 2867 C CE1 . PHE A 361 ? 0.4144 0.3368 0.2425 0.1124 -0.0211 0.0156 402 PHE A CE1 2868 C CE2 . PHE A 361 ? 0.3713 0.3068 0.2319 0.1004 -0.0186 0.0137 402 PHE A CE2 2869 C CZ . PHE A 361 ? 0.4107 0.3431 0.2588 0.1057 -0.0239 0.0112 402 PHE A CZ 2870 N N . GLY A 362 ? 0.4725 0.3612 0.2850 0.1151 0.0158 0.0502 403 GLY A N 2871 C CA . GLY A 362 ? 0.4953 0.3752 0.2998 0.1162 0.0268 0.0588 403 GLY A CA 2872 C C . GLY A 362 ? 0.5264 0.3923 0.3084 0.1258 0.0256 0.0642 403 GLY A C 2873 O O . GLY A 362 ? 0.5526 0.4103 0.3200 0.1293 0.0338 0.0706 403 GLY A O 2874 N N . THR A 363 ? 0.5381 0.4010 0.3164 0.1304 0.0154 0.0617 404 THR A N 2875 C CA . THR A 363 ? 0.5612 0.4103 0.3169 0.1402 0.0127 0.0665 404 THR A CA 2876 C C . THR A 363 ? 0.5785 0.4237 0.3135 0.1467 0.0112 0.0656 404 THR A C 2877 O O . THR A 363 ? 0.6138 0.4470 0.3278 0.1532 0.0165 0.0722 404 THR A O 2878 C CB . THR A 363 ? 0.5689 0.4160 0.3260 0.1444 0.0008 0.0634 404 THR A CB 2879 O OG1 A THR A 363 ? 0.5609 0.4097 0.3350 0.1392 0.0036 0.0652 404 THR A OG1 2880 O OG1 B THR A 363 ? 0.5683 0.4222 0.3262 0.1462 -0.0107 0.0549 404 THR A OG1 2881 C CG2 A THR A 363 ? 0.5681 0.4008 0.3004 0.1551 -0.0029 0.0681 404 THR A CG2 2882 C CG2 B THR A 363 ? 0.5557 0.4081 0.3346 0.1379 0.0017 0.0629 404 THR A CG2 2883 N N . LEU A 364 ? 0.5521 0.4068 0.2928 0.1449 0.0043 0.0574 405 LEU A N 2884 C CA . LEU A 364 ? 0.5645 0.4164 0.2874 0.1504 0.0024 0.0552 405 LEU A CA 2885 C C . LEU A 364 ? 0.5668 0.4171 0.2845 0.1486 0.0159 0.0604 405 LEU A C 2886 O O . LEU A 364 ? 0.5680 0.4089 0.2636 0.1557 0.0194 0.0640 405 LEU A O 2887 C CB . LEU A 364 ? 0.5606 0.4236 0.2939 0.1477 -0.0073 0.0453 405 LEU A CB 2888 C CG A LEU A 364 ? 0.5634 0.4297 0.3038 0.1493 -0.0212 0.0388 405 LEU A CG 2889 C CG B LEU A 364 ? 0.5688 0.4309 0.2986 0.1531 -0.0221 0.0392 405 LEU A CG 2890 C CD1 A LEU A 364 ? 0.5571 0.4348 0.3100 0.1451 -0.0278 0.0299 405 LEU A CD1 2891 C CD1 B LEU A 364 ? 0.5555 0.4189 0.2984 0.1515 -0.0266 0.0395 405 LEU A CD1 2892 C CD2 A LEU A 364 ? 0.5940 0.4482 0.3117 0.1603 -0.0294 0.0397 405 LEU A CD2 2893 C CD2 B LEU A 364 ? 0.5650 0.4375 0.3050 0.1500 -0.0297 0.0300 405 LEU A CD2 2894 N N . LYS A 365 ? 0.5408 0.4003 0.2787 0.1395 0.0234 0.0607 406 LYS A N 2895 C CA . LYS A 365 ? 0.5559 0.4153 0.2929 0.1370 0.0365 0.0655 406 LYS A CA 2896 C C . LYS A 365 ? 0.5893 0.4354 0.3104 0.1420 0.0462 0.0755 406 LYS A C 2897 O O . LYS A 365 ? 0.6024 0.4434 0.3090 0.1457 0.0543 0.0793 406 LYS A O 2898 C CB . LYS A 365 ? 0.5492 0.4205 0.3122 0.1264 0.0419 0.0642 406 LYS A CB 2899 C CG . LYS A 365 ? 0.5753 0.4470 0.3394 0.1238 0.0553 0.0691 406 LYS A CG 2900 C CD . LYS A 365 ? 0.6416 0.5256 0.4305 0.1140 0.0588 0.0665 406 LYS A CD 2901 C CE . LYS A 365 ? 0.6635 0.5472 0.4554 0.1116 0.0724 0.0722 406 LYS A CE 2902 N NZ . LYS A 365 ? 0.6981 0.5729 0.4884 0.1121 0.0809 0.0808 406 LYS A NZ 2903 N N . LYS A 366 ? 0.5906 0.4309 0.3141 0.1422 0.0458 0.0799 407 LYS A N 2904 C CA . LYS A 366 ? 0.6290 0.4557 0.3378 0.1468 0.0554 0.0902 407 LYS A CA 2905 C C . LYS A 366 ? 0.6673 0.4813 0.3454 0.1581 0.0529 0.0927 407 LYS A C 2906 O O . LYS A 366 ? 0.6936 0.4964 0.3555 0.1625 0.0631 0.1013 407 LYS A O 2907 C CB . LYS A 366 ? 0.6321 0.4550 0.3511 0.1445 0.0552 0.0940 407 LYS A CB 2908 C CG . LYS A 366 ? 0.6404 0.4728 0.3864 0.1337 0.0621 0.0941 407 LYS A CG 2909 C CD . LYS A 366 ? 0.6782 0.5079 0.4358 0.1314 0.0596 0.0958 407 LYS A CD 2910 C CE . LYS A 366 ? 0.6565 0.4952 0.4402 0.1209 0.0656 0.0950 407 LYS A CE 2911 N NZ . LYS A 366 ? 0.7086 0.5431 0.5022 0.1192 0.0643 0.0972 407 LYS A NZ 2912 N N . GLU A 367 ? 0.6743 0.4895 0.3444 0.1629 0.0396 0.0854 408 GLU A N 2913 C CA . GLU A 367 ? 0.7184 0.5221 0.3587 0.1742 0.0350 0.0860 408 GLU A CA 2914 C C . GLU A 367 ? 0.7170 0.5228 0.3465 0.1763 0.0385 0.0830 408 GLU A C 2915 O O . GLU A 367 ? 0.7474 0.5440 0.3515 0.1857 0.0345 0.0823 408 GLU A O 2916 C CB . GLU A 367 ? 0.7259 0.5293 0.3627 0.1790 0.0179 0.0791 408 GLU A CB 2917 C CG . GLU A 367 ? 0.7952 0.5950 0.4390 0.1791 0.0131 0.0817 408 GLU A CG 2918 C CD . GLU A 367 ? 0.8773 0.6773 0.5185 0.1844 -0.0041 0.0746 408 GLU A CD 2919 O OE1 . GLU A 367 ? 0.9483 0.7370 0.5755 0.1918 -0.0089 0.0784 408 GLU A OE1 2920 O OE2 . GLU A 367 ? 0.9161 0.7274 0.5698 0.1812 -0.0127 0.0653 408 GLU A OE2 2921 N N . GLY A 368 ? 0.6901 0.5072 0.3380 0.1680 0.0456 0.0810 409 GLY A N 2922 C CA . GLY A 368 ? 0.6859 0.5053 0.3258 0.1695 0.0503 0.0786 409 GLY A CA 2923 C C . GLY A 368 ? 0.6611 0.4922 0.3122 0.1663 0.0406 0.0679 409 GLY A C 2924 O O . GLY A 368 ? 0.6627 0.4958 0.3078 0.1678 0.0432 0.0650 409 GLY A O 2925 N N . TRP A 369 ? 0.6189 0.4577 0.2869 0.1620 0.0297 0.0621 410 TRP A N 2926 C CA . TRP A 369 ? 0.5919 0.4412 0.2709 0.1589 0.0202 0.0523 410 TRP A CA 2927 C C . TRP A 369 ? 0.5502 0.4126 0.2547 0.1483 0.0266 0.0510 410 TRP A C 2928 O O . TRP A 369 ? 0.5492 0.4140 0.2674 0.1425 0.0339 0.0558 410 TRP A O 2929 C CB . TRP A 369 ? 0.5948 0.4462 0.2802 0.1595 0.0058 0.0468 410 TRP A CB 2930 C CG . TRP A 369 ? 0.5939 0.4573 0.2962 0.1546 -0.0038 0.0372 410 TRP A CG 2931 C CD1 . TRP A 369 ? 0.6178 0.4813 0.3121 0.1588 -0.0136 0.0299 410 TRP A CD1 2932 C CD2 . TRP A 369 ? 0.5658 0.4419 0.2949 0.1448 -0.0045 0.0339 410 TRP A CD2 2933 N NE1 . TRP A 369 ? 0.5717 0.4470 0.2870 0.1520 -0.0200 0.0228 410 TRP A NE1 2934 C CE2 . TRP A 369 ? 0.5683 0.4515 0.3045 0.1435 -0.0143 0.0253 410 TRP A CE2 2935 C CE3 . TRP A 369 ? 0.5624 0.4439 0.3098 0.1371 0.0022 0.0374 410 TRP A CE3 2936 C CZ2 . TRP A 369 ? 0.5096 0.4050 0.2696 0.1350 -0.0171 0.0206 410 TRP A CZ2 2937 C CZ3 . TRP A 369 ? 0.4971 0.3907 0.2674 0.1290 -0.0010 0.0323 410 TRP A CZ3 2938 C CH2 . TRP A 369 ? 0.4930 0.3934 0.2689 0.1280 -0.0102 0.0242 410 TRP A CH2 2939 N N . ARG A 370 ? 0.5220 0.3919 0.2320 0.1462 0.0238 0.0446 411 ARG A N 2940 C CA . ARG A 370 ? 0.4925 0.3759 0.2282 0.1361 0.0256 0.0413 411 ARG A CA 2941 C C . ARG A 370 ? 0.4665 0.3565 0.2078 0.1352 0.0141 0.0322 411 ARG A C 2942 O O . ARG A 370 ? 0.4847 0.3696 0.2101 0.1419 0.0082 0.0286 411 ARG A O 2943 C CB . ARG A 370 ? 0.5088 0.3953 0.2474 0.1334 0.0373 0.0439 411 ARG A CB 2944 C CG . ARG A 370 ? 0.5231 0.4067 0.2648 0.1312 0.0502 0.0525 411 ARG A CG 2945 C CD . ARG A 370 ? 0.5443 0.4324 0.2909 0.1287 0.0613 0.0541 411 ARG A CD 2946 N NE . ARG A 370 ? 0.5670 0.4527 0.3195 0.1259 0.0730 0.0622 411 ARG A NE 2947 C CZ . ARG A 370 ? 0.5129 0.4053 0.2870 0.1177 0.0748 0.0633 411 ARG A CZ 2948 N NH1 . ARG A 370 ? 0.4415 0.3440 0.2334 0.1114 0.0666 0.0569 411 ARG A NH1 2949 N NH2 . ARG A 370 ? 0.5426 0.4312 0.3204 0.1160 0.0853 0.0708 411 ARG A NH2 2950 N N . PRO A 371 ? 0.4401 0.3410 0.2038 0.1270 0.0111 0.0284 412 PRO A N 2951 C CA . PRO A 371 ? 0.4249 0.3325 0.1961 0.1252 0.0014 0.0203 412 PRO A CA 2952 C C . PRO A 371 ? 0.4086 0.3183 0.1768 0.1255 0.0048 0.0180 412 PRO A C 2953 O O . PRO A 371 ? 0.4298 0.3392 0.1967 0.1246 0.0154 0.0224 412 PRO A O 2954 C CB . PRO A 371 ? 0.4104 0.3288 0.2062 0.1159 0.0007 0.0186 412 PRO A CB 2955 C CG . PRO A 371 ? 0.4065 0.3255 0.2087 0.1118 0.0124 0.0253 412 PRO A CG 2956 C CD . PRO A 371 ? 0.4252 0.3322 0.2077 0.1191 0.0176 0.0318 412 PRO A CD 2957 N N . ARG A 372 ? 0.4003 0.3123 0.1684 0.1265 -0.0040 0.0110 413 ARG A N 2958 C CA . ARG A 372 ? 0.4125 0.3265 0.1786 0.1268 -0.0017 0.0081 413 ARG A CA 2959 C C . ARG A 372 ? 0.3941 0.3179 0.1797 0.1182 0.0054 0.0091 413 ARG A C 2960 O O . ARG A 372 ? 0.4076 0.3318 0.1917 0.1181 0.0144 0.0118 413 ARG A O 2961 C CB . ARG A 372 ? 0.4147 0.3296 0.1804 0.1286 -0.0135 -0.0001 413 ARG A CB 2962 C CG . ARG A 372 ? 0.4443 0.3607 0.2083 0.1290 -0.0120 -0.0037 413 ARG A CG 2963 C CD . ARG A 372 ? 0.4771 0.3952 0.2446 0.1293 -0.0239 -0.0119 413 ARG A CD 2964 N NE . ARG A 372 ? 0.5141 0.4341 0.2826 0.1289 -0.0219 -0.0150 413 ARG A NE 2965 C CZ . ARG A 372 ? 0.5697 0.4826 0.3207 0.1361 -0.0213 -0.0169 413 ARG A CZ 2966 N NH1 . ARG A 372 ? 0.5095 0.4124 0.2391 0.1446 -0.0230 -0.0161 413 ARG A NH1 2967 N NH2 . ARG A 372 ? 0.5221 0.4374 0.2765 0.1351 -0.0193 -0.0199 413 ARG A NH2 2968 N N . ARG A 373 ? 0.3563 0.2878 0.1600 0.1114 0.0014 0.0071 414 ARG A N 2969 C CA . ARG A 373 ? 0.3376 0.2784 0.1599 0.1032 0.0066 0.0077 414 ARG A CA 2970 C C . ARG A 373 ? 0.3506 0.2929 0.1815 0.0992 0.0126 0.0131 414 ARG A C 2971 O O . ARG A 373 ? 0.3514 0.2890 0.1774 0.1015 0.0107 0.0152 414 ARG A O 2972 C CB . ARG A 373 ? 0.3276 0.2760 0.1645 0.0980 -0.0015 0.0018 414 ARG A CB 2973 C CG . ARG A 373 ? 0.3497 0.2964 0.1801 0.1016 -0.0093 -0.0043 414 ARG A CG 2974 C CD . ARG A 373 ? 0.3503 0.3043 0.1965 0.0959 -0.0165 -0.0097 414 ARG A CD 2975 N NE . ARG A 373 ? 0.3387 0.2895 0.1772 0.1001 -0.0226 -0.0148 414 ARG A NE 2976 C CZ . ARG A 373 ? 0.3535 0.2987 0.1819 0.1057 -0.0309 -0.0185 414 ARG A CZ 2977 N NH1 . ARG A 373 ? 0.3425 0.2856 0.1690 0.1075 -0.0349 -0.0178 414 ARG A NH1 2978 N NH2 . ARG A 373 ? 0.3638 0.3053 0.1841 0.1099 -0.0356 -0.0232 414 ARG A NH2 2979 N N . THR A 374 ? 0.3233 0.2717 0.1671 0.0933 0.0194 0.0150 415 THR A N 2980 C CA . THR A 374 ? 0.3239 0.2746 0.1786 0.0885 0.0245 0.0192 415 THR A CA 2981 C C . THR A 374 ? 0.3135 0.2685 0.1794 0.0843 0.0176 0.0162 415 THR A C 2982 O O . THR A 374 ? 0.3085 0.2693 0.1826 0.0811 0.0118 0.0113 415 THR A O 2983 C CB . THR A 374 ? 0.3085 0.2656 0.1758 0.0830 0.0321 0.0207 415 THR A CB 2984 O OG1 . THR A 374 ? 0.3245 0.2771 0.1819 0.0873 0.0401 0.0245 415 THR A OG1 2985 C CG2 . THR A 374 ? 0.3043 0.2648 0.1856 0.0771 0.0361 0.0237 415 THR A CG2 2986 N N . ILE A 375 ? 0.2921 0.2437 0.1583 0.0844 0.0189 0.0195 416 ILE A N 2987 C CA . ILE A 375 ? 0.2919 0.2478 0.1702 0.0802 0.0142 0.0173 416 ILE A CA 2988 C C . ILE A 375 ? 0.2866 0.2460 0.1777 0.0743 0.0207 0.0201 416 ILE A C 2989 O O . ILE A 375 ? 0.3152 0.2701 0.2033 0.0752 0.0278 0.0254 416 ILE A O 2990 C CB . ILE A 375 ? 0.2928 0.2425 0.1635 0.0850 0.0089 0.0177 416 ILE A CB 2991 C CG1 . ILE A 375 ? 0.3363 0.2820 0.1937 0.0914 0.0016 0.0144 416 ILE A CG1 2992 C CG2 . ILE A 375 ? 0.2963 0.2517 0.1815 0.0802 0.0047 0.0149 416 ILE A CG2 2993 C CD1 . ILE A 375 ? 0.3403 0.2782 0.1872 0.0977 -0.0035 0.0156 416 ILE A CD1 2994 N N . LEU A 376 ? 0.2717 0.2391 0.1771 0.0681 0.0184 0.0166 417 LEU A N 2995 C CA . LEU A 376 ? 0.2810 0.2518 0.1991 0.0624 0.0231 0.0183 417 LEU A CA 2996 C C . LEU A 376 ? 0.2787 0.2502 0.2026 0.0610 0.0186 0.0163 417 LEU A C 2997 O O . LEU A 376 ? 0.2840 0.2587 0.2097 0.0610 0.0119 0.0120 417 LEU A O 2998 C CB . LEU A 376 ? 0.2651 0.2440 0.1941 0.0569 0.0236 0.0155 417 LEU A CB 2999 C CG . LEU A 376 ? 0.3021 0.2814 0.2270 0.0583 0.0274 0.0166 417 LEU A CG 3000 C CD1 . LEU A 376 ? 0.2916 0.2788 0.2283 0.0528 0.0273 0.0139 417 LEU A CD1 3001 C CD2 . LEU A 376 ? 0.3151 0.2897 0.2365 0.0601 0.0358 0.0222 417 LEU A CD2 3002 N N . PHE A 377 ? 0.2583 0.2272 0.1866 0.0596 0.0225 0.0193 418 PHE A N 3003 C CA . PHE A 377 ? 0.2543 0.2236 0.1889 0.0583 0.0191 0.0176 418 PHE A CA 3004 C C . PHE A 377 ? 0.2527 0.2269 0.2011 0.0518 0.0223 0.0168 418 PHE A C 3005 O O . PHE A 377 ? 0.2610 0.2344 0.2124 0.0498 0.0283 0.0198 418 PHE A O 3006 C CB . PHE A 377 ? 0.2654 0.2260 0.1928 0.0628 0.0205 0.0219 418 PHE A CB 3007 C CG . PHE A 377 ? 0.2902 0.2447 0.2026 0.0699 0.0171 0.0230 418 PHE A CG 3008 C CD1 . PHE A 377 ? 0.3137 0.2686 0.2241 0.0729 0.0089 0.0192 418 PHE A CD1 3009 C CD2 . PHE A 377 ? 0.3356 0.2841 0.2358 0.0738 0.0220 0.0275 418 PHE A CD2 3010 C CE1 . PHE A 377 ? 0.3259 0.2745 0.2215 0.0800 0.0047 0.0198 418 PHE A CE1 3011 C CE2 . PHE A 377 ? 0.3614 0.3035 0.2457 0.0810 0.0184 0.0281 418 PHE A CE2 3012 C CZ . PHE A 377 ? 0.3383 0.2803 0.2201 0.0841 0.0094 0.0242 418 PHE A CZ 3013 N N . ALA A 378 ? 0.2599 0.2392 0.2167 0.0486 0.0184 0.0124 419 ALA A N 3014 C CA . ALA A 378 ? 0.2364 0.2200 0.2045 0.0428 0.0208 0.0110 419 ALA A CA 3015 C C . ALA A 378 ? 0.2393 0.2227 0.2134 0.0419 0.0187 0.0089 419 ALA A C 3016 O O . ALA A 378 ? 0.2579 0.2424 0.2311 0.0437 0.0140 0.0062 419 ALA A O 3017 C CB . ALA A 378 ? 0.2454 0.2365 0.2179 0.0392 0.0187 0.0073 419 ALA A CB 3018 N N . SER A 379 ? 0.2323 0.2144 0.2134 0.0389 0.0223 0.0099 420 SER A N 3019 C CA . SER A 379 ? 0.2209 0.2034 0.2094 0.0370 0.0211 0.0071 420 SER A CA 3020 C C . SER A 379 ? 0.2167 0.2053 0.2136 0.0314 0.0217 0.0036 420 SER A C 3021 O O . SER A 379 ? 0.2280 0.2160 0.2297 0.0286 0.0251 0.0050 420 SER A O 3022 C CB . SER A 379 ? 0.2371 0.2121 0.2264 0.0382 0.0247 0.0110 420 SER A CB 3023 O OG . SER A 379 ? 0.2409 0.2158 0.2382 0.0363 0.0238 0.0080 420 SER A OG 3024 N N . TRP A 380 ? 0.2085 0.2027 0.2069 0.0299 0.0182 -0.0006 421 TRP A N 3025 C CA . TRP A 380 ? 0.1971 0.1967 0.2010 0.0252 0.0183 -0.0037 421 TRP A CA 3026 C C . TRP A 380 ? 0.2206 0.2198 0.2313 0.0227 0.0187 -0.0065 421 TRP A C 3027 O O . TRP A 380 ? 0.2250 0.2220 0.2367 0.0243 0.0179 -0.0077 421 TRP A O 3028 C CB . TRP A 380 ? 0.1963 0.2013 0.1986 0.0246 0.0149 -0.0068 421 TRP A CB 3029 C CG . TRP A 380 ? 0.1987 0.2045 0.1946 0.0270 0.0134 -0.0053 421 TRP A CG 3030 C CD1 . TRP A 380 ? 0.2072 0.2139 0.2001 0.0294 0.0101 -0.0065 421 TRP A CD1 3031 C CD2 . TRP A 380 ? 0.1912 0.1970 0.1839 0.0272 0.0149 -0.0028 421 TRP A CD2 3032 N NE1 . TRP A 380 ? 0.1929 0.1998 0.1803 0.0311 0.0091 -0.0052 421 TRP A NE1 3033 C CE2 . TRP A 380 ? 0.2026 0.2087 0.1893 0.0300 0.0122 -0.0029 421 TRP A CE2 3034 C CE3 . TRP A 380 ? 0.2058 0.2113 0.2011 0.0254 0.0183 -0.0008 421 TRP A CE3 3035 C CZ2 . TRP A 380 ? 0.2174 0.2234 0.1995 0.0312 0.0129 -0.0011 421 TRP A CZ2 3036 C CZ3 . TRP A 380 ? 0.2128 0.2188 0.2043 0.0265 0.0194 0.0012 421 TRP A CZ3 3037 C CH2 . TRP A 380 ? 0.2213 0.2272 0.2056 0.0297 0.0168 0.0011 421 TRP A CH2 3038 N N . ASP A 381 ? 0.2067 0.2083 0.2220 0.0189 0.0195 -0.0081 422 ASP A N 3039 C CA . ASP A 381 ? 0.1955 0.1968 0.2167 0.0164 0.0193 -0.0118 422 ASP A CA 3040 C C . ASP A 381 ? 0.2046 0.2113 0.2250 0.0142 0.0169 -0.0161 422 ASP A C 3041 O O . ASP A 381 ? 0.2123 0.2228 0.2293 0.0137 0.0157 -0.0158 422 ASP A O 3042 C CB . ASP A 381 ? 0.2070 0.2064 0.2346 0.0137 0.0214 -0.0107 422 ASP A CB 3043 C CG . ASP A 381 ? 0.2225 0.2185 0.2564 0.0122 0.0216 -0.0137 422 ASP A CG 3044 O OD1 . ASP A 381 ? 0.2340 0.2298 0.2672 0.0130 0.0201 -0.0170 422 ASP A OD1 3045 O OD2 . ASP A 381 ? 0.2253 0.2189 0.2658 0.0102 0.0234 -0.0127 422 ASP A OD2 3046 N N . ALA A 382 ? 0.1964 0.2028 0.2198 0.0130 0.0164 -0.0200 423 ALA A N 3047 C CA . ALA A 382 ? 0.1998 0.2102 0.2220 0.0109 0.0148 -0.0243 423 ALA A CA 3048 C C . ALA A 382 ? 0.1842 0.1986 0.2015 0.0119 0.0139 -0.0244 423 ALA A C 3049 O O . ALA A 382 ? 0.1933 0.2110 0.2079 0.0100 0.0129 -0.0261 423 ALA A O 3050 C CB . ALA A 382 ? 0.1988 0.2106 0.2227 0.0078 0.0139 -0.0252 423 ALA A CB 3051 N N . GLU A 383 ? 0.1870 0.2008 0.2034 0.0148 0.0139 -0.0228 424 GLU A N 3052 C CA . GLU A 383 ? 0.2007 0.2185 0.2145 0.0154 0.0128 -0.0235 424 GLU A CA 3053 C C . GLU A 383 ? 0.1938 0.2138 0.2087 0.0142 0.0135 -0.0275 424 GLU A C 3054 O O . GLU A 383 ? 0.1977 0.2212 0.2103 0.0129 0.0134 -0.0286 424 GLU A O 3055 C CB . GLU A 383 ? 0.1769 0.1934 0.1907 0.0190 0.0119 -0.0216 424 GLU A CB 3056 C CG . GLU A 383 ? 0.1967 0.2172 0.2097 0.0196 0.0103 -0.0223 424 GLU A CG 3057 C CD . GLU A 383 ? 0.2249 0.2482 0.2420 0.0196 0.0109 -0.0257 424 GLU A CD 3058 O OE1 . GLU A 383 ? 0.2153 0.2373 0.2354 0.0197 0.0124 -0.0279 424 GLU A OE1 3059 O OE2 . GLU A 383 ? 0.2325 0.2595 0.2505 0.0195 0.0101 -0.0263 424 GLU A OE2 3060 N N . GLU A 384 ? 0.1940 0.2115 0.2121 0.0147 0.0145 -0.0299 425 GLU A N 3061 C CA . GLU A 384 ? 0.2066 0.2260 0.2254 0.0143 0.0157 -0.0340 425 GLU A CA 3062 C C . GLU A 384 ? 0.1955 0.2162 0.2103 0.0115 0.0159 -0.0363 425 GLU A C 3063 O O . GLU A 384 ? 0.2214 0.2441 0.2343 0.0111 0.0173 -0.0392 425 GLU A O 3064 C CB . GLU A 384 ? 0.1961 0.2119 0.2192 0.0160 0.0166 -0.0362 425 GLU A CB 3065 C CG . GLU A 384 ? 0.2184 0.2327 0.2452 0.0195 0.0161 -0.0344 425 GLU A CG 3066 C CD . GLU A 384 ? 0.2030 0.2219 0.2319 0.0212 0.0161 -0.0354 425 GLU A CD 3067 O OE1 . GLU A 384 ? 0.2100 0.2333 0.2372 0.0194 0.0170 -0.0366 425 GLU A OE1 3068 O OE2 . GLU A 384 ? 0.2193 0.2373 0.2518 0.0244 0.0150 -0.0347 425 GLU A OE2 3069 N N . PHE A 385 ? 0.1993 0.2188 0.2127 0.0097 0.0145 -0.0350 426 PHE A N 3070 C CA . PHE A 385 ? 0.1982 0.2185 0.2075 0.0074 0.0136 -0.0373 426 PHE A CA 3071 C C . PHE A 385 ? 0.2160 0.2393 0.2210 0.0064 0.0126 -0.0348 426 PHE A C 3072 O O . PHE A 385 ? 0.2357 0.2592 0.2373 0.0047 0.0110 -0.0357 426 PHE A O 3073 C CB . PHE A 385 ? 0.2062 0.2234 0.2184 0.0061 0.0121 -0.0382 426 PHE A CB 3074 C CG . PHE A 385 ? 0.2062 0.2198 0.2221 0.0066 0.0128 -0.0416 426 PHE A CG 3075 C CD1 . PHE A 385 ? 0.2242 0.2369 0.2374 0.0058 0.0120 -0.0466 426 PHE A CD1 3076 C CD2 . PHE A 385 ? 0.2192 0.2298 0.2407 0.0084 0.0140 -0.0400 426 PHE A CD2 3077 C CE1 . PHE A 385 ? 0.2310 0.2398 0.2476 0.0065 0.0125 -0.0506 426 PHE A CE1 3078 C CE2 . PHE A 385 ? 0.2453 0.2519 0.2706 0.0090 0.0145 -0.0434 426 PHE A CE2 3079 C CZ . PHE A 385 ? 0.2493 0.2550 0.2725 0.0080 0.0137 -0.0489 426 PHE A CZ 3080 N N . GLY A 386 ? 0.2108 0.2360 0.2160 0.0075 0.0130 -0.0321 427 GLY A N 3081 C CA . GLY A 386 ? 0.2075 0.2351 0.2088 0.0066 0.0120 -0.0300 427 GLY A CA 3082 C C . GLY A 386 ? 0.2006 0.2282 0.2030 0.0074 0.0107 -0.0264 427 GLY A C 3083 O O . GLY A 386 ? 0.2074 0.2361 0.2072 0.0065 0.0094 -0.0248 427 GLY A O 3084 N N . LEU A 387 ? 0.1843 0.2106 0.1898 0.0095 0.0111 -0.0250 428 LEU A N 3085 C CA . LEU A 387 ? 0.1862 0.2118 0.1912 0.0111 0.0101 -0.0217 428 LEU A CA 3086 C C . LEU A 387 ? 0.1857 0.2103 0.1910 0.0100 0.0100 -0.0202 428 LEU A C 3087 O O . LEU A 387 ? 0.1876 0.2128 0.1913 0.0103 0.0093 -0.0179 428 LEU A O 3088 C CB . LEU A 387 ? 0.2022 0.2302 0.2047 0.0112 0.0089 -0.0207 428 LEU A CB 3089 C CG . LEU A 387 ? 0.1849 0.2153 0.1888 0.0111 0.0094 -0.0226 428 LEU A CG 3090 C CD1 . LEU A 387 ? 0.1852 0.2174 0.1878 0.0109 0.0080 -0.0213 428 LEU A CD1 3091 C CD2 . LEU A 387 ? 0.1810 0.2105 0.1887 0.0136 0.0096 -0.0233 428 LEU A CD2 3092 N N . LEU A 388 ? 0.1868 0.2098 0.1950 0.0087 0.0106 -0.0217 429 LEU A N 3093 C CA . LEU A 388 ? 0.1838 0.2070 0.1941 0.0070 0.0100 -0.0211 429 LEU A CA 3094 C C . LEU A 388 ? 0.1879 0.2095 0.2004 0.0084 0.0115 -0.0174 429 LEU A C 3095 O O . LEU A 388 ? 0.2083 0.2313 0.2212 0.0079 0.0111 -0.0159 429 LEU A O 3096 C CB . LEU A 388 ? 0.1957 0.2176 0.2093 0.0052 0.0096 -0.0243 429 LEU A CB 3097 C CG . LEU A 388 ? 0.2063 0.2292 0.2159 0.0043 0.0087 -0.0281 429 LEU A CG 3098 C CD1 . LEU A 388 ? 0.2163 0.2373 0.2291 0.0027 0.0076 -0.0318 429 LEU A CD1 3099 C CD2 . LEU A 388 ? 0.2173 0.2429 0.2214 0.0034 0.0070 -0.0281 429 LEU A CD2 3100 N N . GLY A 389 ? 0.1882 0.2065 0.2019 0.0103 0.0133 -0.0159 430 GLY A N 3101 C CA . GLY A 389 ? 0.1851 0.2008 0.1998 0.0119 0.0156 -0.0119 430 GLY A CA 3102 C C . GLY A 389 ? 0.1871 0.2038 0.1964 0.0142 0.0152 -0.0095 430 GLY A C 3103 O O . GLY A 389 ? 0.1984 0.2155 0.2082 0.0144 0.0166 -0.0071 430 GLY A O 3104 N N . SER A 390 ? 0.1803 0.1977 0.1852 0.0158 0.0134 -0.0102 431 SER A N 3105 C CA . SER A 390 ? 0.1788 0.1966 0.1786 0.0182 0.0125 -0.0085 431 SER A CA 3106 C C . SER A 390 ? 0.1769 0.1981 0.1768 0.0162 0.0113 -0.0091 431 SER A C 3107 O O . SER A 390 ? 0.1820 0.2032 0.1798 0.0175 0.0117 -0.0072 431 SER A O 3108 C CB . SER A 390 ? 0.1711 0.1893 0.1684 0.0199 0.0101 -0.0100 431 SER A CB 3109 O OG . SER A 390 ? 0.1922 0.2137 0.1914 0.0174 0.0088 -0.0130 431 SER A OG 3110 N N . THR A 391 ? 0.1709 0.1948 0.1725 0.0134 0.0099 -0.0117 432 THR A N 3111 C CA . THR A 391 ? 0.1771 0.2036 0.1779 0.0119 0.0083 -0.0120 432 THR A CA 3112 C C . THR A 391 ? 0.1758 0.2029 0.1803 0.0110 0.0092 -0.0110 432 THR A C 3113 O O . THR A 391 ? 0.1760 0.2044 0.1797 0.0116 0.0087 -0.0097 432 THR A O 3114 C CB . THR A 391 ? 0.1780 0.2064 0.1781 0.0094 0.0067 -0.0148 432 THR A CB 3115 O OG1 . THR A 391 ? 0.1956 0.2239 0.1938 0.0102 0.0066 -0.0157 432 THR A OG1 3116 C CG2 . THR A 391 ? 0.2045 0.2347 0.2024 0.0083 0.0047 -0.0146 432 THR A CG2 3117 N N . GLU A 392 ? 0.1718 0.1982 0.1815 0.0096 0.0105 -0.0115 433 GLU A N 3118 C CA . GLU A 392 ? 0.1783 0.2058 0.1939 0.0086 0.0115 -0.0105 433 GLU A CA 3119 C C . GLU A 392 ? 0.1769 0.2032 0.1922 0.0111 0.0146 -0.0069 433 GLU A C 3120 O O . GLU A 392 ? 0.1861 0.2145 0.2039 0.0112 0.0150 -0.0059 433 GLU A O 3121 C CB . GLU A 392 ? 0.1920 0.2184 0.2146 0.0065 0.0123 -0.0120 433 GLU A CB 3122 C CG . GLU A 392 ? 0.2006 0.2281 0.2227 0.0042 0.0090 -0.0161 433 GLU A CG 3123 C CD . GLU A 392 ? 0.2081 0.2387 0.2286 0.0032 0.0056 -0.0173 433 GLU A CD 3124 O OE1 . GLU A 392 ? 0.1973 0.2298 0.2232 0.0027 0.0052 -0.0165 433 GLU A OE1 3125 O OE2 . GLU A 392 ? 0.2100 0.2411 0.2243 0.0031 0.0036 -0.0188 433 GLU A OE2 3126 N N . TRP A 393 ? 0.1866 0.2093 0.1983 0.0135 0.0168 -0.0051 434 TRP A N 3127 C CA . TRP A 393 ? 0.1826 0.2033 0.1917 0.0166 0.0200 -0.0015 434 TRP A CA 3128 C C . TRP A 393 ? 0.2001 0.2222 0.2034 0.0186 0.0182 -0.0014 434 TRP A C 3129 O O . TRP A 393 ? 0.2089 0.2314 0.2125 0.0200 0.0204 0.0004 434 TRP A O 3130 C CB . TRP A 393 ? 0.2136 0.2294 0.2185 0.0191 0.0218 0.0003 434 TRP A CB 3131 C CG . TRP A 393 ? 0.1850 0.1974 0.1854 0.0227 0.0256 0.0042 434 TRP A CG 3132 C CD1 . TRP A 393 ? 0.2168 0.2270 0.2210 0.0229 0.0308 0.0076 434 TRP A CD1 3133 C CD2 . TRP A 393 ? 0.2288 0.2392 0.2196 0.0268 0.0247 0.0052 434 TRP A CD2 3134 N NE1 . TRP A 393 ? 0.2388 0.2454 0.2348 0.0273 0.0336 0.0109 434 TRP A NE1 3135 C CE2 . TRP A 393 ? 0.2385 0.2451 0.2260 0.0298 0.0295 0.0091 434 TRP A CE2 3136 C CE3 . TRP A 393 ? 0.2197 0.2310 0.2049 0.0283 0.0202 0.0029 434 TRP A CE3 3137 C CZ2 . TRP A 393 ? 0.2618 0.2650 0.2386 0.0347 0.0297 0.0107 434 TRP A CZ2 3138 C CZ3 . TRP A 393 ? 0.2476 0.2557 0.2237 0.0328 0.0198 0.0041 434 TRP A CZ3 3139 C CH2 . TRP A 393 ? 0.2538 0.2578 0.2251 0.0362 0.0244 0.0078 434 TRP A CH2 3140 N N . ALA A 394 ? 0.1954 0.2181 0.1944 0.0186 0.0146 -0.0035 435 ALA A N 3141 C CA . ALA A 394 ? 0.1846 0.2083 0.1792 0.0201 0.0125 -0.0038 435 ALA A CA 3142 C C . ALA A 394 ? 0.1809 0.2079 0.1794 0.0183 0.0116 -0.0043 435 ALA A C 3143 O O . ALA A 394 ? 0.1987 0.2260 0.1955 0.0201 0.0116 -0.0035 435 ALA A O 3144 C CB . ALA A 394 ? 0.2018 0.2255 0.1928 0.0201 0.0091 -0.0058 435 ALA A CB 3145 N N . GLU A 395 ? 0.1839 0.2132 0.1875 0.0150 0.0104 -0.0059 436 GLU A N 3146 C CA . GLU A 395 ? 0.1677 0.2001 0.1754 0.0136 0.0089 -0.0064 436 GLU A CA 3147 C C . GLU A 395 ? 0.1972 0.2305 0.2104 0.0147 0.0122 -0.0045 436 GLU A C 3148 O O . GLU A 395 ? 0.2070 0.2423 0.2218 0.0156 0.0117 -0.0041 436 GLU A O 3149 C CB . GLU A 395 ? 0.1878 0.2219 0.1990 0.0104 0.0065 -0.0088 436 GLU A CB 3150 C CG . GLU A 395 ? 0.1917 0.2253 0.1969 0.0095 0.0037 -0.0105 436 GLU A CG 3151 C CD . GLU A 395 ? 0.2284 0.2630 0.2345 0.0068 0.0013 -0.0130 436 GLU A CD 3152 O OE1 . GLU A 395 ? 0.2144 0.2491 0.2158 0.0062 -0.0011 -0.0137 436 GLU A OE1 3153 O OE2 . GLU A 395 ? 0.2231 0.2580 0.2344 0.0056 0.0017 -0.0141 436 GLU A OE2 3154 N N . GLU A 396 ? 0.1906 0.2225 0.2075 0.0145 0.0158 -0.0032 437 GLU A N 3155 C CA . GLU A 396 ? 0.1940 0.2266 0.2170 0.0154 0.0201 -0.0008 437 GLU A CA 3156 C C . GLU A 396 ? 0.1969 0.2279 0.2134 0.0194 0.0226 0.0014 437 GLU A C 3157 O O . GLU A 396 ? 0.2027 0.2359 0.2234 0.0204 0.0248 0.0024 437 GLU A O 3158 C CB . GLU A 396 ? 0.2118 0.2417 0.2383 0.0147 0.0240 0.0007 437 GLU A CB 3159 C CG . GLU A 396 ? 0.2553 0.2861 0.2904 0.0148 0.0294 0.0034 437 GLU A CG 3160 C CD . GLU A 396 ? 0.3728 0.4023 0.4164 0.0119 0.0312 0.0035 437 GLU A CD 3161 O OE1 . GLU A 396 ? 0.3628 0.3878 0.4019 0.0130 0.0333 0.0051 437 GLU A OE1 3162 O OE2 . GLU A 396 ? 0.5026 0.5355 0.5572 0.0087 0.0297 0.0015 437 GLU A OE2 3163 N N . ASN A 397 ? 0.1837 0.2110 0.1907 0.0218 0.0221 0.0018 438 ASN A N 3164 C CA . ASN A 397 ? 0.1916 0.2160 0.1911 0.0263 0.0246 0.0037 438 ASN A CA 3165 C C . ASN A 397 ? 0.1936 0.2179 0.1864 0.0280 0.0203 0.0018 438 ASN A C 3166 O O . ASN A 397 ? 0.2057 0.2268 0.1905 0.0318 0.0207 0.0024 438 ASN A O 3167 C CB . ASN A 397 ? 0.2034 0.2227 0.1967 0.0285 0.0270 0.0057 438 ASN A CB 3168 C CG . ASN A 397 ? 0.2322 0.2506 0.2318 0.0274 0.0323 0.0084 438 ASN A CG 3169 O OD1 . ASN A 397 ? 0.2850 0.3038 0.2875 0.0286 0.0372 0.0108 438 ASN A OD1 3170 N ND2 . ASN A 397 ? 0.2295 0.2469 0.2327 0.0249 0.0317 0.0079 438 ASN A ND2 3171 N N . SER A 398 ? 0.1935 0.2209 0.1895 0.0252 0.0160 -0.0005 439 SER A N 3172 C CA . SER A 398 ? 0.1970 0.2237 0.1876 0.0262 0.0119 -0.0022 439 SER A CA 3173 C C . SER A 398 ? 0.2093 0.2346 0.1958 0.0300 0.0126 -0.0018 439 SER A C 3174 O O . SER A 398 ? 0.2214 0.2441 0.2013 0.0321 0.0100 -0.0029 439 SER A O 3175 C CB . SER A 398 ? 0.2071 0.2368 0.2017 0.0227 0.0080 -0.0039 439 SER A CB 3176 O OG . SER A 398 ? 0.2216 0.2543 0.2225 0.0222 0.0087 -0.0036 439 SER A OG 3177 N N . ARG A 399 ? 0.1963 0.2235 0.1873 0.0308 0.0159 -0.0005 440 ARG A N 3178 C CA . ARG A 399 ? 0.1977 0.2236 0.1848 0.0348 0.0170 -0.0004 440 ARG A CA 3179 C C . ARG A 399 ? 0.2103 0.2314 0.1880 0.0391 0.0198 0.0007 440 ARG A C 3180 O O . ARG A 399 ? 0.2253 0.2434 0.1956 0.0426 0.0181 -0.0005 440 ARG A O 3181 C CB . ARG A 399 ? 0.2096 0.2391 0.2049 0.0349 0.0207 0.0007 440 ARG A CB 3182 C CG . ARG A 399 ? 0.2435 0.2772 0.2466 0.0318 0.0165 -0.0009 440 ARG A CG 3183 C CD . ARG A 399 ? 0.2856 0.3240 0.3005 0.0301 0.0192 0.0000 440 ARG A CD 3184 N NE . ARG A 399 ? 0.2449 0.2867 0.2659 0.0273 0.0139 -0.0018 440 ARG A NE 3185 C CZ . ARG A 399 ? 0.2740 0.3165 0.2962 0.0238 0.0102 -0.0029 440 ARG A CZ 3186 N NH1 . ARG A 399 ? 0.2752 0.3160 0.2951 0.0219 0.0112 -0.0027 440 ARG A NH1 3187 N NH2 . ARG A 399 ? 0.2595 0.3043 0.2853 0.0223 0.0055 -0.0043 440 ARG A NH2 3188 N N . LEU A 400 ? 0.2093 0.2290 0.1869 0.0391 0.0238 0.0030 441 LEU A N 3189 C CA . LEU A 400 ? 0.2197 0.2339 0.1866 0.0436 0.0261 0.0044 441 LEU A CA 3190 C C . LEU A 400 ? 0.2367 0.2479 0.1964 0.0444 0.0203 0.0021 441 LEU A C 3191 O O . LEU A 400 ? 0.2476 0.2546 0.1976 0.0487 0.0188 0.0013 441 LEU A O 3192 C CB . LEU A 400 ? 0.2311 0.2437 0.1994 0.0433 0.0315 0.0077 441 LEU A CB 3193 C CG . LEU A 400 ? 0.2705 0.2867 0.2494 0.0412 0.0372 0.0099 441 LEU A CG 3194 C CD1 . LEU A 400 ? 0.3194 0.3328 0.2995 0.0408 0.0424 0.0134 441 LEU A CD1 3195 C CD2 . LEU A 400 ? 0.2946 0.3113 0.2724 0.0448 0.0415 0.0108 441 LEU A CD2 3196 N N . LEU A 401 ? 0.2179 0.2313 0.1826 0.0404 0.0169 0.0009 442 LEU A N 3197 C CA . LEU A 401 ? 0.2361 0.2475 0.1964 0.0408 0.0120 -0.0012 442 LEU A CA 3198 C C . LEU A 401 ? 0.2456 0.2570 0.2038 0.0415 0.0072 -0.0040 442 LEU A C 3199 O O . LEU A 401 ? 0.2783 0.2863 0.2301 0.0443 0.0038 -0.0056 442 LEU A O 3200 C CB . LEU A 401 ? 0.2237 0.2380 0.1909 0.0361 0.0105 -0.0019 442 LEU A CB 3201 C CG . LEU A 401 ? 0.2277 0.2411 0.1971 0.0354 0.0143 0.0004 442 LEU A CG 3202 C CD1 . LEU A 401 ? 0.2370 0.2536 0.2139 0.0307 0.0129 -0.0010 442 LEU A CD1 3203 C CD2 . LEU A 401 ? 0.2779 0.2863 0.2395 0.0392 0.0139 0.0012 442 LEU A CD2 3204 N N A GLN A 402 ? 0.2430 0.2576 0.2068 0.0391 0.0067 -0.0046 443 GLN A N 3205 N N B GLN A 402 ? 0.2391 0.2535 0.2025 0.0392 0.0063 -0.0047 443 GLN A N 3206 C CA A GLN A 402 ? 0.2472 0.2616 0.2103 0.0395 0.0027 -0.0068 443 GLN A CA 3207 C CA B GLN A 402 ? 0.2393 0.2527 0.2007 0.0399 0.0017 -0.0073 443 GLN A CA 3208 C C A GLN A 402 ? 0.2462 0.2561 0.2007 0.0449 0.0023 -0.0077 443 GLN A C 3209 C C B GLN A 402 ? 0.2412 0.2511 0.1957 0.0450 0.0020 -0.0079 443 GLN A C 3210 O O A GLN A 402 ? 0.2284 0.2356 0.1790 0.0464 -0.0023 -0.0102 443 GLN A O 3211 O O B GLN A 402 ? 0.2356 0.2432 0.1871 0.0464 -0.0023 -0.0104 443 GLN A O 3212 C CB A GLN A 402 ? 0.2510 0.2689 0.2206 0.0373 0.0034 -0.0064 443 GLN A CB 3213 C CB B GLN A 402 ? 0.2176 0.2345 0.1859 0.0359 -0.0001 -0.0078 443 GLN A CB 3214 C CG A GLN A 402 ? 0.2564 0.2730 0.2247 0.0390 0.0006 -0.0080 443 GLN A CG 3215 C CG B GLN A 402 ? 0.2041 0.2232 0.1761 0.0362 0.0027 -0.0065 443 GLN A CG 3216 C CD A GLN A 402 ? 0.3117 0.3281 0.2816 0.0362 -0.0042 -0.0096 443 GLN A CD 3217 C CD B GLN A 402 ? 0.2413 0.2638 0.2200 0.0321 0.0009 -0.0066 443 GLN A CD 3218 O OE1 A GLN A 402 ? 0.3358 0.3545 0.3096 0.0323 -0.0049 -0.0091 443 GLN A OE1 3219 O OE1 B GLN A 402 ? 0.2375 0.2606 0.2174 0.0290 -0.0015 -0.0072 443 GLN A OE1 3220 N NE2 A GLN A 402 ? 0.2630 0.2765 0.2302 0.0382 -0.0075 -0.0114 443 GLN A NE2 3221 N NE2 B GLN A 402 ? 0.2632 0.2880 0.2463 0.0324 0.0021 -0.0060 443 GLN A NE2 3222 N N . GLU A 403 ? 0.2451 0.2541 0.1968 0.0479 0.0073 -0.0058 444 GLU A N 3223 C CA . GLU A 403 ? 0.2484 0.2536 0.1921 0.0532 0.0079 -0.0067 444 GLU A CA 3224 C C . GLU A 403 ? 0.2508 0.2507 0.1835 0.0577 0.0086 -0.0063 444 GLU A C 3225 O O . GLU A 403 ? 0.2651 0.2606 0.1886 0.0627 0.0073 -0.0081 444 GLU A O 3226 C CB . GLU A 403 ? 0.2649 0.2720 0.2113 0.0547 0.0136 -0.0050 444 GLU A CB 3227 C CG . GLU A 403 ? 0.2825 0.2948 0.2399 0.0507 0.0122 -0.0055 444 GLU A CG 3228 C CD . GLU A 403 ? 0.3511 0.3625 0.3088 0.0497 0.0057 -0.0085 444 GLU A CD 3229 O OE1 . GLU A 403 ? 0.3251 0.3322 0.2757 0.0521 0.0020 -0.0108 444 GLU A OE1 3230 O OE2 . GLU A 403 ? 0.3541 0.3689 0.3195 0.0466 0.0042 -0.0085 444 GLU A OE2 3231 N N . ARG A 404 ? 0.2352 0.2350 0.1683 0.0563 0.0099 -0.0043 445 ARG A N 3232 C CA . ARG A 404 ? 0.2396 0.2338 0.1617 0.0611 0.0111 -0.0031 445 ARG A CA 3233 C C . ARG A 404 ? 0.2602 0.2532 0.1814 0.0604 0.0065 -0.0040 445 ARG A C 3234 O O . ARG A 404 ? 0.2770 0.2648 0.1885 0.0647 0.0059 -0.0034 445 ARG A O 3235 C CB . ARG A 404 ? 0.2378 0.2316 0.1598 0.0617 0.0191 0.0015 445 ARG A CB 3236 C CG . ARG A 404 ? 0.2547 0.2501 0.1785 0.0630 0.0249 0.0027 445 ARG A CG 3237 C CD . ARG A 404 ? 0.2558 0.2515 0.1825 0.0627 0.0334 0.0074 445 ARG A CD 3238 N NE . ARG A 404 ? 0.2590 0.2583 0.1921 0.0626 0.0386 0.0083 445 ARG A NE 3239 C CZ . ARG A 404 ? 0.2499 0.2514 0.1903 0.0612 0.0461 0.0119 445 ARG A CZ 3240 N NH1 . ARG A 404 ? 0.2559 0.2558 0.1976 0.0596 0.0491 0.0151 445 ARG A NH1 3241 N NH2 . ARG A 404 ? 0.2533 0.2588 0.2010 0.0612 0.0502 0.0121 445 ARG A NH2 3242 N N . GLY A 405 ? 0.2456 0.2430 0.1765 0.0552 0.0034 -0.0054 446 GLY A N 3243 C CA . GLY A 405 ? 0.2485 0.2458 0.1811 0.0540 -0.0001 -0.0062 446 GLY A CA 3244 C C . GLY A 405 ? 0.2493 0.2440 0.1776 0.0566 -0.0071 -0.0099 446 GLY A C 3245 O O . GLY A 405 ? 0.2763 0.2732 0.2094 0.0545 -0.0111 -0.0128 446 GLY A O 3246 N N . VAL A 406 ? 0.2609 0.2510 0.1810 0.0610 -0.0089 -0.0098 447 VAL A N 3247 C CA . VAL A 406 ? 0.2642 0.2520 0.1813 0.0637 -0.0165 -0.0138 447 VAL A CA 3248 C C . VAL A 406 ? 0.2495 0.2413 0.1768 0.0599 -0.0203 -0.0155 447 VAL A C 3249 O O . VAL A 406 ? 0.2512 0.2451 0.1845 0.0580 -0.0253 -0.0190 447 VAL A O 3250 C CB . VAL A 406 ? 0.3001 0.2810 0.2035 0.0706 -0.0176 -0.0131 447 VAL A CB 3251 C CG1 . VAL A 406 ? 0.3234 0.3020 0.2245 0.0735 -0.0263 -0.0174 447 VAL A CG1 3252 C CG2 . VAL A 406 ? 0.3370 0.3138 0.2297 0.0748 -0.0140 -0.0122 447 VAL A CG2 3253 N N . ALA A 407 ? 0.2547 0.2472 0.1844 0.0588 -0.0179 -0.0132 448 ALA A N 3254 C CA . ALA A 407 ? 0.2317 0.2277 0.1705 0.0561 -0.0210 -0.0149 448 ALA A CA 3255 C C . ALA A 407 ? 0.2369 0.2343 0.1795 0.0539 -0.0163 -0.0119 448 ALA A C 3256 O O . ALA A 407 ? 0.2593 0.2533 0.1957 0.0558 -0.0117 -0.0084 448 ALA A O 3257 C CB . ALA A 407 ? 0.2599 0.2525 0.1944 0.0609 -0.0277 -0.0174 448 ALA A CB 3258 N N . TYR A 408 ? 0.2279 0.2298 0.1807 0.0498 -0.0172 -0.0133 449 TYR A N 3259 C CA . TYR A 408 ? 0.2157 0.2189 0.1731 0.0477 -0.0136 -0.0115 449 TYR A CA 3260 C C . TYR A 408 ? 0.2302 0.2346 0.1928 0.0485 -0.0179 -0.0139 449 TYR A C 3261 O O . TYR A 408 ? 0.2328 0.2410 0.2026 0.0465 -0.0213 -0.0170 449 TYR A O 3262 C CB . TYR A 408 ? 0.1996 0.2079 0.1651 0.0418 -0.0099 -0.0113 449 TYR A CB 3263 C CG . TYR A 408 ? 0.2067 0.2160 0.1771 0.0397 -0.0069 -0.0102 449 TYR A CG 3264 C CD1 . TYR A 408 ? 0.2196 0.2267 0.1878 0.0397 -0.0023 -0.0072 449 TYR A CD1 3265 C CD2 . TYR A 408 ? 0.2261 0.2386 0.2039 0.0378 -0.0085 -0.0125 449 TYR A CD2 3266 C CE1 . TYR A 408 ? 0.2338 0.2410 0.2067 0.0380 0.0002 -0.0065 449 TYR A CE1 3267 C CE2 . TYR A 408 ? 0.2130 0.2260 0.1950 0.0363 -0.0057 -0.0121 449 TYR A CE2 3268 C CZ . TYR A 408 ? 0.2344 0.2446 0.2138 0.0364 -0.0017 -0.0092 449 TYR A CZ 3269 O OH . TYR A 408 ? 0.2420 0.2520 0.2259 0.0349 0.0006 -0.0091 449 TYR A OH 3270 N N . ILE A 409 ? 0.2313 0.2324 0.1912 0.0514 -0.0175 -0.0122 450 ILE A N 3271 C CA . ILE A 409 ? 0.2171 0.2193 0.1828 0.0526 -0.0212 -0.0143 450 ILE A CA 3272 C C . ILE A 409 ? 0.2219 0.2255 0.1934 0.0497 -0.0166 -0.0128 450 ILE A C 3273 O O . ILE A 409 ? 0.2243 0.2240 0.1910 0.0506 -0.0126 -0.0094 450 ILE A O 3274 C CB . ILE A 409 ? 0.2298 0.2256 0.1860 0.0595 -0.0255 -0.0136 450 ILE A CB 3275 C CG1 . ILE A 409 ? 0.2749 0.2685 0.2240 0.0629 -0.0306 -0.0157 450 ILE A CG1 3276 C CG2 . ILE A 409 ? 0.2463 0.2433 0.2095 0.0611 -0.0296 -0.0157 450 ILE A CG2 3277 C CD1 . ILE A 409 ? 0.2859 0.2851 0.2450 0.0601 -0.0354 -0.0203 450 ILE A CD1 3278 N N . ASN A 410 ? 0.2134 0.2225 0.1954 0.0463 -0.0168 -0.0154 451 ASN A N 3279 C CA . ASN A 410 ? 0.2152 0.2254 0.2025 0.0437 -0.0127 -0.0148 451 ASN A CA 3280 C C . ASN A 410 ? 0.2424 0.2498 0.2308 0.0475 -0.0146 -0.0148 451 ASN A C 3281 O O . ASN A 410 ? 0.2779 0.2843 0.2656 0.0515 -0.0200 -0.0162 451 ASN A O 3282 C CB . ASN A 410 ? 0.2142 0.2310 0.2114 0.0389 -0.0117 -0.0177 451 ASN A CB 3283 C CG . ASN A 410 ? 0.2411 0.2590 0.2412 0.0353 -0.0066 -0.0171 451 ASN A CG 3284 O OD1 . ASN A 410 ? 0.2765 0.2926 0.2725 0.0339 -0.0035 -0.0149 451 ASN A OD1 3285 N ND2 . ASN A 410 ? 0.2423 0.2633 0.2501 0.0339 -0.0058 -0.0195 451 ASN A ND2 3286 N N . ALA A 411 ? 0.2334 0.2392 0.2237 0.0465 -0.0108 -0.0134 452 ALA A N 3287 C CA . ALA A 411 ? 0.2531 0.2556 0.2447 0.0502 -0.0125 -0.0131 452 ALA A CA 3288 C C . ALA A 411 ? 0.2582 0.2620 0.2571 0.0474 -0.0087 -0.0139 452 ALA A C 3289 O O . ALA A 411 ? 0.2629 0.2616 0.2596 0.0484 -0.0061 -0.0113 452 ALA A O 3290 C CB . ALA A 411 ? 0.2729 0.2671 0.2532 0.0548 -0.0122 -0.0087 452 ALA A CB 3291 N N . ASP A 412 ? 0.2581 0.2684 0.2657 0.0440 -0.0083 -0.0175 453 ASP A N 3292 C CA . ASP A 412 ? 0.2423 0.2541 0.2572 0.0422 -0.0055 -0.0193 453 ASP A CA 3293 C C . ASP A 412 ? 0.2636 0.2754 0.2838 0.0464 -0.0092 -0.0211 453 ASP A C 3294 O O . ASP A 412 ? 0.2713 0.2796 0.2871 0.0509 -0.0135 -0.0197 453 ASP A O 3295 C CB . ASP A 412 ? 0.2263 0.2444 0.2465 0.0371 -0.0026 -0.0221 453 ASP A CB 3296 C CG . ASP A 412 ? 0.2429 0.2611 0.2674 0.0350 0.0012 -0.0237 453 ASP A CG 3297 O OD1 . ASP A 412 ? 0.2710 0.2849 0.2961 0.0374 0.0014 -0.0230 453 ASP A OD1 3298 O OD2 . ASP A 412 ? 0.2153 0.2377 0.2425 0.0313 0.0037 -0.0259 453 ASP A OD2 3299 N N A SER A 413 ? 0.2446 0.2599 0.2738 0.0453 -0.0077 -0.0241 454 SER A N 3300 N N B SER A 413 ? 0.2547 0.2699 0.2838 0.0453 -0.0076 -0.0241 454 SER A N 3301 C CA A SER A 413 ? 0.2584 0.2739 0.2945 0.0492 -0.0106 -0.0261 454 SER A CA 3302 C CA B SER A 413 ? 0.2614 0.2764 0.2970 0.0493 -0.0106 -0.0259 454 SER A CA 3303 C C A SER A 413 ? 0.2615 0.2775 0.2976 0.0533 -0.0171 -0.0264 454 SER A C 3304 C C B SER A 413 ? 0.2645 0.2805 0.3009 0.0533 -0.0170 -0.0265 454 SER A C 3305 O O A SER A 413 ? 0.2670 0.2877 0.3050 0.0517 -0.0190 -0.0279 454 SER A O 3306 O O B SER A 413 ? 0.2633 0.2847 0.3031 0.0515 -0.0186 -0.0284 454 SER A O 3307 C CB A SER A 413 ? 0.2592 0.2816 0.3062 0.0465 -0.0079 -0.0303 454 SER A CB 3308 C CB B SER A 413 ? 0.2578 0.2787 0.3043 0.0470 -0.0078 -0.0300 454 SER A CB 3309 O OG A SER A 413 ? 0.2292 0.2510 0.2751 0.0428 -0.0025 -0.0306 454 SER A OG 3310 O OG B SER A 413 ? 0.2475 0.2756 0.2989 0.0442 -0.0077 -0.0322 454 SER A OG 3311 N N . SER A 414 ? 0.2704 0.2808 0.3035 0.0588 -0.0209 -0.0248 455 SER A N 3312 C CA . SER A 414 ? 0.2871 0.2972 0.3194 0.0635 -0.0281 -0.0256 455 SER A CA 3313 C C . SER A 414 ? 0.2865 0.3036 0.3334 0.0645 -0.0314 -0.0302 455 SER A C 3314 O O . SER A 414 ? 0.2885 0.3080 0.3384 0.0668 -0.0375 -0.0322 455 SER A O 3315 C CB . SER A 414 ? 0.3094 0.3102 0.3322 0.0696 -0.0312 -0.0220 455 SER A CB 3316 O OG . SER A 414 ? 0.3590 0.3539 0.3687 0.0688 -0.0281 -0.0176 455 SER A OG 3317 N N . ILE A 415 ? 0.2918 0.3119 0.3481 0.0630 -0.0276 -0.0322 456 ILE A N 3318 C CA . ILE A 415 ? 0.3170 0.3438 0.3883 0.0644 -0.0300 -0.0366 456 ILE A CA 3319 C C . ILE A 415 ? 0.3203 0.3536 0.4006 0.0592 -0.0230 -0.0393 456 ILE A C 3320 O O . ILE A 415 ? 0.3652 0.3958 0.4409 0.0566 -0.0174 -0.0381 456 ILE A O 3321 C CB . ILE A 415 ? 0.3126 0.3349 0.3864 0.0705 -0.0337 -0.0365 456 ILE A CB 3322 C CG1 . ILE A 415 ? 0.3495 0.3648 0.4170 0.0703 -0.0285 -0.0338 456 ILE A CG1 3323 C CG2 . ILE A 415 ? 0.3463 0.3624 0.4109 0.0764 -0.0416 -0.0343 456 ILE A CG2 3324 C CD1 . ILE A 415 ? 0.4372 0.4521 0.5141 0.0731 -0.0280 -0.0358 456 ILE A CD1 3325 N N . GLU A 416 ? 0.2872 0.3290 0.3803 0.0575 -0.0231 -0.0429 457 GLU A N 3326 C CA . GLU A 416 ? 0.2871 0.3349 0.3895 0.0539 -0.0163 -0.0456 457 GLU A CA 3327 C C . GLU A 416 ? 0.2808 0.3355 0.4001 0.0564 -0.0187 -0.0496 457 GLU A C 3328 O O . GLU A 416 ? 0.2781 0.3395 0.4083 0.0540 -0.0135 -0.0525 457 GLU A O 3329 C CB . GLU A 416 ? 0.2823 0.3337 0.3822 0.0479 -0.0115 -0.0453 457 GLU A CB 3330 C CG . GLU A 416 ? 0.2928 0.3487 0.3974 0.0469 -0.0156 -0.0459 457 GLU A CG 3331 C CD . GLU A 416 ? 0.3237 0.3822 0.4251 0.0411 -0.0111 -0.0450 457 GLU A CD 3332 O OE1 . GLU A 416 ? 0.3315 0.3873 0.4238 0.0381 -0.0059 -0.0433 457 GLU A OE1 3333 O OE2 . GLU A 416 ? 0.3239 0.3870 0.4328 0.0397 -0.0131 -0.0462 457 GLU A OE2 3334 N N . GLY A 417 ? 0.2783 0.3312 0.3997 0.0617 -0.0268 -0.0497 458 GLY A N 3335 C CA . GLY A 417 ? 0.2830 0.3420 0.4212 0.0650 -0.0311 -0.0536 458 GLY A CA 3336 C C . GLY A 417 ? 0.2914 0.3457 0.4259 0.0711 -0.0412 -0.0528 458 GLY A C 3337 O O . GLY A 417 ? 0.2948 0.3408 0.4129 0.0726 -0.0438 -0.0490 458 GLY A O 3338 N N . ASN A 418 ? 0.2776 0.3371 0.4270 0.0747 -0.0470 -0.0563 459 ASN A N 3339 C CA . ASN A 418 ? 0.2997 0.3546 0.4457 0.0814 -0.0577 -0.0561 459 ASN A CA 3340 C C . ASN A 418 ? 0.2851 0.3472 0.4446 0.0820 -0.0649 -0.0600 459 ASN A C 3341 O O . ASN A 418 ? 0.3181 0.3796 0.4825 0.0880 -0.0744 -0.0619 459 ASN A O 3342 C CB . ASN A 418 ? 0.3164 0.3674 0.4653 0.0875 -0.0600 -0.0562 459 ASN A CB 3343 C CG . ASN A 418 ? 0.3487 0.4093 0.5202 0.0880 -0.0588 -0.0612 459 ASN A CG 3344 O OD1 . ASN A 418 ? 0.3542 0.4248 0.5409 0.0844 -0.0572 -0.0646 459 ASN A OD1 3345 N ND2 . ASN A 418 ? 0.4721 0.5295 0.6466 0.0928 -0.0593 -0.0614 459 ASN A ND2 3346 N N . TYR A 419 ? 0.2646 0.3336 0.4309 0.0758 -0.0609 -0.0614 460 TYR A N 3347 C CA . TYR A 419 ? 0.2673 0.3445 0.4507 0.0753 -0.0665 -0.0656 460 TYR A CA 3348 C C . TYR A 419 ? 0.2643 0.3374 0.4375 0.0758 -0.0740 -0.0651 460 TYR A C 3349 O O . TYR A 419 ? 0.2739 0.3467 0.4512 0.0807 -0.0846 -0.0676 460 TYR A O 3350 C CB . TYR A 419 ? 0.2599 0.3470 0.4591 0.0685 -0.0577 -0.0676 460 TYR A CB 3351 C CG . TYR A 419 ? 0.3040 0.4001 0.5233 0.0671 -0.0622 -0.0718 460 TYR A CG 3352 C CD1 . TYR A 419 ? 0.3568 0.4588 0.5952 0.0713 -0.0685 -0.0761 460 TYR A CD1 3353 C CD2 . TYR A 419 ? 0.3657 0.4643 0.5860 0.0614 -0.0600 -0.0715 460 TYR A CD2 3354 C CE1 . TYR A 419 ? 0.4135 0.5242 0.6728 0.0698 -0.0728 -0.0802 460 TYR A CE1 3355 C CE2 . TYR A 419 ? 0.3847 0.4914 0.6253 0.0597 -0.0640 -0.0755 460 TYR A CE2 3356 C CZ . TYR A 419 ? 0.4139 0.5268 0.6740 0.0637 -0.0702 -0.0798 460 TYR A CZ 3357 O OH . TYR A 419 ? 0.4692 0.5905 0.7513 0.0618 -0.0743 -0.0840 460 TYR A OH 3358 N N . THR A 420 ? 0.2577 0.3274 0.4173 0.0712 -0.0689 -0.0619 461 THR A N 3359 C CA . THR A 420 ? 0.2569 0.3227 0.4068 0.0718 -0.0755 -0.0617 461 THR A CA 3360 C C . THR A 420 ? 0.2367 0.2961 0.3672 0.0684 -0.0694 -0.0572 461 THR A C 3361 O O . THR A 420 ? 0.2357 0.2940 0.3611 0.0655 -0.0606 -0.0544 461 THR A O 3362 C CB . THR A 420 ? 0.2663 0.3403 0.4339 0.0686 -0.0789 -0.0660 461 THR A CB 3363 O OG1 . THR A 420 ? 0.2719 0.3410 0.4303 0.0711 -0.0879 -0.0668 461 THR A OG1 3364 C CG2 . THR A 420 ? 0.2520 0.3311 0.4246 0.0605 -0.0689 -0.0650 461 THR A CG2 3365 N N . LEU A 421 ? 0.2409 0.2960 0.3610 0.0692 -0.0745 -0.0568 462 LEU A N 3366 C CA . LEU A 421 ? 0.2363 0.2858 0.3390 0.0662 -0.0694 -0.0527 462 LEU A CA 3367 C C . LEU A 421 ? 0.2417 0.2971 0.3516 0.0585 -0.0617 -0.0527 462 LEU A C 3368 O O . LEU A 421 ? 0.2432 0.3061 0.3699 0.0555 -0.0624 -0.0561 462 LEU A O 3369 C CB . LEU A 421 ? 0.2372 0.2803 0.3270 0.0701 -0.0776 -0.0529 462 LEU A CB 3370 C CG . LEU A 421 ? 0.2512 0.2868 0.3206 0.0692 -0.0731 -0.0483 462 LEU A CG 3371 C CD1 . LEU A 421 ? 0.2815 0.3100 0.3379 0.0729 -0.0702 -0.0441 462 LEU A CD1 3372 C CD2 . LEU A 421 ? 0.2767 0.3074 0.3364 0.0728 -0.0814 -0.0497 462 LEU A CD2 3373 N N . ARG A 422 ? 0.2272 0.2790 0.3245 0.0553 -0.0544 -0.0489 463 ARG A N 3374 C CA . ARG A 422 ? 0.2323 0.2877 0.3320 0.0486 -0.0475 -0.0481 463 ARG A CA 3375 C C . ARG A 422 ? 0.2412 0.2899 0.3235 0.0484 -0.0475 -0.0450 463 ARG A C 3376 O O . ARG A 422 ? 0.2566 0.2989 0.3253 0.0513 -0.0470 -0.0422 463 ARG A O 3377 C CB . ARG A 422 ? 0.2203 0.2785 0.3228 0.0451 -0.0381 -0.0467 463 ARG A CB 3378 C CG . ARG A 422 ? 0.2506 0.3132 0.3574 0.0385 -0.0310 -0.0463 463 ARG A CG 3379 C CD . ARG A 422 ? 0.2647 0.3293 0.3727 0.0360 -0.0224 -0.0455 463 ARG A CD 3380 N NE . ARG A 422 ? 0.3020 0.3693 0.4105 0.0303 -0.0157 -0.0444 463 ARG A NE 3381 C CZ . ARG A 422 ? 0.2905 0.3600 0.3999 0.0275 -0.0080 -0.0441 463 ARG A CZ 3382 N NH1 . ARG A 422 ? 0.2912 0.3607 0.4021 0.0297 -0.0056 -0.0451 463 ARG A NH1 3383 N NH2 . ARG A 422 ? 0.3088 0.3799 0.4172 0.0226 -0.0025 -0.0428 463 ARG A NH2 3384 N N . VAL A 423 ? 0.2321 0.2820 0.3153 0.0452 -0.0481 -0.0456 464 VAL A N 3385 C CA . VAL A 423 ? 0.2416 0.2854 0.3092 0.0452 -0.0480 -0.0430 464 VAL A CA 3386 C C . VAL A 423 ? 0.2425 0.2891 0.3127 0.0390 -0.0427 -0.0421 464 VAL A C 3387 O O . VAL A 423 ? 0.2421 0.2938 0.3253 0.0359 -0.0431 -0.0444 464 VAL A O 3388 C CB . VAL A 423 ? 0.2503 0.2901 0.3129 0.0497 -0.0572 -0.0450 464 VAL A CB 3389 C CG1 . VAL A 423 ? 0.2546 0.2885 0.3018 0.0499 -0.0566 -0.0427 464 VAL A CG1 3390 C CG2 . VAL A 423 ? 0.2768 0.3131 0.3358 0.0566 -0.0635 -0.0459 464 VAL A CG2 3391 N N . ASP A 424 ? 0.2345 0.2775 0.2927 0.0373 -0.0378 -0.0387 465 ASP A N 3392 C CA . ASP A 424 ? 0.2406 0.2846 0.2981 0.0324 -0.0339 -0.0374 465 ASP A CA 3393 C C . ASP A 424 ? 0.2305 0.2683 0.2736 0.0346 -0.0359 -0.0356 465 ASP A C 3394 O O . ASP A 424 ? 0.2360 0.2697 0.2686 0.0371 -0.0345 -0.0333 465 ASP A O 3395 C CB . ASP A 424 ? 0.2385 0.2841 0.2943 0.0284 -0.0256 -0.0350 465 ASP A CB 3396 C CG . ASP A 424 ? 0.2945 0.3463 0.3636 0.0256 -0.0215 -0.0365 465 ASP A CG 3397 O OD1 . ASP A 424 ? 0.3466 0.4021 0.4275 0.0268 -0.0246 -0.0393 465 ASP A OD1 3398 O OD2 . ASP A 424 ? 0.3591 0.4121 0.4265 0.0224 -0.0150 -0.0349 465 ASP A OD2 3399 N N . CYS A 425 ? 0.2285 0.2653 0.2711 0.0334 -0.0383 -0.0364 466 CYS A N 3400 C CA . CYS A 425 ? 0.2323 0.2632 0.2610 0.0358 -0.0396 -0.0348 466 CYS A CA 3401 C C . CYS A 425 ? 0.2420 0.2727 0.2725 0.0332 -0.0408 -0.0355 466 CYS A C 3402 O O . CYS A 425 ? 0.2797 0.3141 0.3219 0.0300 -0.0416 -0.0374 466 CYS A O 3403 C CB . CYS A 425 ? 0.2492 0.2752 0.2698 0.0423 -0.0461 -0.0360 466 CYS A CB 3404 S SG . CYS A 425 ? 0.2657 0.2924 0.2949 0.0449 -0.0560 -0.0414 466 CYS A SG 3405 N N . THR A 426 ? 0.2260 0.2521 0.2450 0.0346 -0.0406 -0.0340 467 THR A N 3406 C CA . THR A 426 ? 0.2230 0.2477 0.2427 0.0330 -0.0426 -0.0350 467 THR A CA 3407 C C . THR A 426 ? 0.2235 0.2470 0.2478 0.0357 -0.0507 -0.0394 467 THR A C 3408 O O . THR A 426 ? 0.2221 0.2436 0.2427 0.0406 -0.0555 -0.0411 467 THR A O 3409 C CB . THR A 426 ? 0.2191 0.2390 0.2254 0.0351 -0.0411 -0.0328 467 THR A CB 3410 O OG1 . THR A 426 ? 0.2355 0.2532 0.2421 0.0346 -0.0441 -0.0344 467 THR A OG1 3411 C CG2 . THR A 426 ? 0.2533 0.2686 0.2480 0.0413 -0.0436 -0.0328 467 THR A CG2 3412 N N . PRO A 427 ? 0.2138 0.2382 0.2464 0.0326 -0.0526 -0.0412 468 PRO A N 3413 C CA . PRO A 427 ? 0.2335 0.2561 0.2707 0.0353 -0.0613 -0.0460 468 PRO A CA 3414 C C . PRO A 427 ? 0.2404 0.2564 0.2625 0.0418 -0.0662 -0.0473 468 PRO A C 3415 O O . PRO A 427 ? 0.2536 0.2678 0.2766 0.0457 -0.0740 -0.0514 468 PRO A O 3416 C CB . PRO A 427 ? 0.2540 0.2767 0.2991 0.0308 -0.0611 -0.0466 468 PRO A CB 3417 C CG . PRO A 427 ? 0.2472 0.2743 0.2981 0.0252 -0.0528 -0.0427 468 PRO A CG 3418 C CD . PRO A 427 ? 0.2154 0.2421 0.2546 0.0267 -0.0475 -0.0391 468 PRO A CD 3419 N N . LEU A 428 ? 0.2392 0.2516 0.2478 0.0431 -0.0618 -0.0441 469 LEU A N 3420 C CA . LEU A 428 ? 0.2611 0.2669 0.2546 0.0495 -0.0655 -0.0451 469 LEU A CA 3421 C C . LEU A 428 ? 0.2596 0.2636 0.2467 0.0549 -0.0686 -0.0456 469 LEU A C 3422 O O . LEU A 428 ? 0.2905 0.2888 0.2663 0.0609 -0.0736 -0.0475 469 LEU A O 3423 C CB . LEU A 428 ? 0.2646 0.2679 0.2466 0.0497 -0.0590 -0.0411 469 LEU A CB 3424 C CG . LEU A 428 ? 0.2606 0.2636 0.2451 0.0463 -0.0573 -0.0408 469 LEU A CG 3425 C CD1 . LEU A 428 ? 0.2904 0.2917 0.2646 0.0470 -0.0510 -0.0370 469 LEU A CD1 3426 C CD2 . LEU A 428 ? 0.2870 0.2857 0.2709 0.0490 -0.0647 -0.0456 469 LEU A CD2 3427 N N . MET A 429 ? 0.2502 0.2585 0.2440 0.0532 -0.0660 -0.0440 470 MET A N 3428 C CA A MET A 429 ? 0.2569 0.2635 0.2458 0.0582 -0.0686 -0.0439 470 MET A CA 3429 C CA B MET A 429 ? 0.2643 0.2704 0.2525 0.0586 -0.0693 -0.0442 470 MET A CA 3430 C C . MET A 429 ? 0.2653 0.2750 0.2664 0.0592 -0.0761 -0.0483 470 MET A C 3431 O O . MET A 429 ? 0.2695 0.2776 0.2672 0.0638 -0.0796 -0.0487 470 MET A O 3432 C CB A MET A 429 ? 0.2507 0.2596 0.2391 0.0562 -0.0609 -0.0393 470 MET A CB 3433 C CB B MET A 429 ? 0.2741 0.2804 0.2567 0.0583 -0.0619 -0.0393 470 MET A CB 3434 C CG A MET A 429 ? 0.2427 0.2479 0.2181 0.0568 -0.0544 -0.0350 470 MET A CG 3435 C CG B MET A 429 ? 0.2791 0.2805 0.2470 0.0601 -0.0571 -0.0359 470 MET A CG 3436 S SD A MET A 429 ? 0.2276 0.2345 0.2030 0.0552 -0.0469 -0.0305 470 MET A SD 3437 S SD B MET A 429 ? 0.3451 0.3452 0.3059 0.0606 -0.0494 -0.0303 470 MET A SD 3438 C CE A MET A 429 ? 0.2082 0.2119 0.1722 0.0546 -0.0397 -0.0261 470 MET A CE 3439 C CE B MET A 429 ? 0.3475 0.3547 0.3206 0.0525 -0.0423 -0.0285 470 MET A CE 3440 N N . TYR A 430 ? 0.2562 0.2703 0.2724 0.0550 -0.0786 -0.0515 471 TYR A N 3441 C CA . TYR A 430 ? 0.2659 0.2842 0.2969 0.0554 -0.0852 -0.0557 471 TYR A CA 3442 C C . TYR A 430 ? 0.2764 0.2895 0.2997 0.0629 -0.0953 -0.0596 471 TYR A C 3443 O O . TYR A 430 ? 0.2835 0.2980 0.3108 0.0660 -0.0995 -0.0609 471 TYR A O 3444 C CB . TYR A 430 ? 0.2503 0.2728 0.2979 0.0502 -0.0870 -0.0588 471 TYR A CB 3445 C CG . TYR A 430 ? 0.2342 0.2627 0.2932 0.0427 -0.0781 -0.0558 471 TYR A CG 3446 C CD1 . TYR A 430 ? 0.2311 0.2620 0.2874 0.0408 -0.0698 -0.0514 471 TYR A CD1 3447 C CD2 . TYR A 430 ? 0.2509 0.2822 0.3239 0.0377 -0.0784 -0.0576 471 TYR A CD2 3448 C CE1 . TYR A 430 ? 0.2565 0.2922 0.3218 0.0342 -0.0618 -0.0488 471 TYR A CE1 3449 C CE2 . TYR A 430 ? 0.2835 0.3195 0.3658 0.0312 -0.0703 -0.0546 471 TYR A CE2 3450 C CZ . TYR A 430 ? 0.2876 0.3258 0.3655 0.0297 -0.0622 -0.0504 471 TYR A CZ 3451 O OH . TYR A 430 ? 0.3034 0.3456 0.3890 0.0237 -0.0543 -0.0476 471 TYR A OH 3452 N N . SER A 431 ? 0.2802 0.2870 0.2918 0.0661 -0.0996 -0.0615 472 SER A N 3453 C CA . SER A 431 ? 0.2931 0.2942 0.2962 0.0737 -0.1102 -0.0659 472 SER A CA 3454 C C . SER A 431 ? 0.3052 0.3011 0.2913 0.0800 -0.1094 -0.0626 472 SER A C 3455 O O . SER A 431 ? 0.3035 0.2976 0.2883 0.0854 -0.1173 -0.0653 472 SER A O 3456 C CB . SER A 431 ? 0.3188 0.3139 0.3126 0.0757 -0.1142 -0.0688 472 SER A CB 3457 O OG A SER A 431 ? 0.3496 0.3491 0.3618 0.0705 -0.1174 -0.0728 472 SER A OG 3458 O OG B SER A 431 ? 0.2816 0.2702 0.2645 0.0835 -0.1245 -0.0733 472 SER A OG 3459 N N . LEU A 432 ? 0.3011 0.2948 0.2755 0.0792 -0.1000 -0.0569 473 LEU A N 3460 C CA . LEU A 432 ? 0.3191 0.3079 0.2786 0.0842 -0.0972 -0.0526 473 LEU A CA 3461 C C . LEU A 432 ? 0.3019 0.2951 0.2722 0.0841 -0.0982 -0.0522 473 LEU A C 3462 O O . LEU A 432 ? 0.3193 0.3083 0.2822 0.0903 -0.1034 -0.0524 473 LEU A O 3463 C CB . LEU A 432 ? 0.3139 0.3018 0.2650 0.0815 -0.0859 -0.0466 473 LEU A CB 3464 C CG . LEU A 432 ? 0.3246 0.3087 0.2644 0.0845 -0.0806 -0.0411 473 LEU A CG 3465 C CD1 . LEU A 432 ? 0.3888 0.3639 0.3105 0.0934 -0.0861 -0.0413 473 LEU A CD1 3466 C CD2 . LEU A 432 ? 0.3825 0.3666 0.3173 0.0809 -0.0702 -0.0362 473 LEU A CD2 3467 N N . VAL A 433 ? 0.2937 0.2950 0.2812 0.0772 -0.0931 -0.0516 474 VAL A N 3468 C CA . VAL A 433 ? 0.2946 0.3007 0.2937 0.0767 -0.0931 -0.0514 474 VAL A CA 3469 C C . VAL A 433 ? 0.3036 0.3113 0.3123 0.0803 -0.1041 -0.0570 474 VAL A C 3470 O O . VAL A 433 ? 0.3052 0.3116 0.3129 0.0851 -0.1079 -0.0569 474 VAL A O 3471 C CB . VAL A 433 ? 0.2735 0.2880 0.2889 0.0686 -0.0853 -0.0502 474 VAL A CB 3472 C CG1 . VAL A 433 ? 0.3252 0.3452 0.3545 0.0682 -0.0854 -0.0509 474 VAL A CG1 3473 C CG2 . VAL A 433 ? 0.3139 0.3267 0.3198 0.0657 -0.0752 -0.0448 474 VAL A CG2 3474 N N . HIS A 434 ? 0.2981 0.3084 0.3169 0.0784 -0.1097 -0.0619 475 HIS A N 3475 C CA . HIS A 434 ? 0.3246 0.3366 0.3542 0.0819 -0.1213 -0.0679 475 HIS A CA 3476 C C . HIS A 434 ? 0.3303 0.3333 0.3412 0.0913 -0.1297 -0.0689 475 HIS A C 3477 O O . HIS A 434 ? 0.3380 0.3412 0.3520 0.0959 -0.1361 -0.0705 475 HIS A O 3478 C CB . HIS A 434 ? 0.3202 0.3351 0.3622 0.0785 -0.1264 -0.0732 475 HIS A CB 3479 C CG . HIS A 434 ? 0.3638 0.3873 0.4255 0.0697 -0.1191 -0.0724 475 HIS A CG 3480 N ND1 . HIS A 434 ? 0.4554 0.4799 0.5239 0.0649 -0.1186 -0.0742 475 HIS A ND1 3481 C CD2 . HIS A 434 ? 0.3816 0.4121 0.4556 0.0649 -0.1112 -0.0697 475 HIS A CD2 3482 C CE1 . HIS A 434 ? 0.4289 0.4608 0.5133 0.0576 -0.1109 -0.0724 475 HIS A CE1 3483 N NE2 . HIS A 434 ? 0.3605 0.3963 0.4487 0.0576 -0.1065 -0.0700 475 HIS A NE2 3484 N N . ASN A 435 ? 0.3247 0.3197 0.3157 0.0944 -0.1294 -0.0678 476 ASN A N 3485 C CA . ASN A 435 ? 0.3509 0.3362 0.3216 0.1039 -0.1371 -0.0686 476 ASN A CA 3486 C C . ASN A 435 ? 0.3579 0.3394 0.3176 0.1081 -0.1337 -0.0633 476 ASN A C 3487 O O . ASN A 435 ? 0.3759 0.3526 0.3284 0.1155 -0.1421 -0.0648 476 ASN A O 3488 C CB . ASN A 435 ? 0.3644 0.3417 0.3150 0.1063 -0.1355 -0.0679 476 ASN A CB 3489 C CG . ASN A 435 ? 0.3942 0.3724 0.3519 0.1048 -0.1422 -0.0743 476 ASN A CG 3490 O OD1 . ASN A 435 ? 0.3991 0.3840 0.3777 0.1012 -0.1477 -0.0790 476 ASN A OD1 3491 N ND2 . ASN A 435 ? 0.3836 0.3548 0.3243 0.1075 -0.1415 -0.0744 476 ASN A ND2 3492 N N . LEU A 436 ? 0.3429 0.3257 0.3008 0.1039 -0.1218 -0.0571 477 LEU A N 3493 C CA . LEU A 436 ? 0.3395 0.3180 0.2874 0.1076 -0.1179 -0.0518 477 LEU A CA 3494 C C . LEU A 436 ? 0.3254 0.3091 0.2891 0.1083 -0.1228 -0.0538 477 LEU A C 3495 O O . LEU A 436 ? 0.3401 0.3183 0.2952 0.1150 -0.1275 -0.0528 477 LEU A O 3496 C CB . LEU A 436 ? 0.3363 0.3162 0.2823 0.1019 -0.1043 -0.0455 477 LEU A CB 3497 C CG . LEU A 436 ? 0.3737 0.3500 0.3132 0.1042 -0.0992 -0.0399 477 LEU A CG 3498 C CD1 . LEU A 436 ? 0.3833 0.3481 0.3001 0.1132 -0.1032 -0.0377 477 LEU A CD1 3499 C CD2 . LEU A 436 ? 0.3588 0.3369 0.2984 0.0982 -0.0868 -0.0347 477 LEU A CD2 3500 N N . THR A 437 ? 0.3115 0.3055 0.2981 0.1014 -0.1209 -0.0563 478 THR A N 3501 C CA . THR A 437 ? 0.3070 0.3069 0.3107 0.1018 -0.1243 -0.0583 478 THR A CA 3502 C C . THR A 437 ? 0.3337 0.3326 0.3412 0.1082 -0.1383 -0.0641 478 THR A C 3503 O O . THR A 437 ? 0.3360 0.3362 0.3506 0.1117 -0.1428 -0.0649 478 THR A O 3504 C CB . THR A 437 ? 0.3021 0.3135 0.3297 0.0931 -0.1181 -0.0595 478 THR A CB 3505 O OG1 . THR A 437 ? 0.2916 0.3077 0.3306 0.0891 -0.1213 -0.0641 478 THR A OG1 3506 C CG2 . THR A 437 ? 0.3077 0.3196 0.3308 0.0874 -0.1045 -0.0536 478 THR A CG2 3507 N N . LYS A 438 ? 0.3355 0.3316 0.3380 0.1102 -0.1458 -0.0684 479 LYS A N 3508 C CA . LYS A 438 ? 0.3682 0.3620 0.3719 0.1171 -0.1605 -0.0744 479 LYS A CA 3509 C C . LYS A 438 ? 0.4008 0.3834 0.3808 0.1269 -0.1654 -0.0717 479 LYS A C 3510 O O . LYS A 438 ? 0.4102 0.3909 0.3915 0.1336 -0.1775 -0.0758 479 LYS A O 3511 C CB . LYS A 438 ? 0.3781 0.3709 0.3819 0.1166 -0.1674 -0.0801 479 LYS A CB 3512 C CG . LYS A 438 ? 0.3870 0.3909 0.4176 0.1078 -0.1655 -0.0838 479 LYS A CG 3513 C CD . LYS A 438 ? 0.4251 0.4271 0.4559 0.1073 -0.1722 -0.0893 479 LYS A CD 3514 C CE . LYS A 438 ? 0.4454 0.4576 0.5021 0.0979 -0.1683 -0.0915 479 LYS A CE 3515 N NZ . LYS A 438 ? 0.4683 0.4782 0.5257 0.0963 -0.1733 -0.0963 479 LYS A NZ 3516 N N . GLU A 439 ? 0.4198 0.3948 0.3789 0.1280 -0.1564 -0.0650 480 GLU A N 3517 C CA A GLU A 439 ? 0.4468 0.4100 0.3811 0.1371 -0.1589 -0.0611 480 GLU A CA 3518 C CA B GLU A 439 ? 0.4555 0.4186 0.3898 0.1371 -0.1589 -0.0611 480 GLU A CA 3519 C C . GLU A 439 ? 0.4472 0.4095 0.3818 0.1378 -0.1529 -0.0553 480 GLU A C 3520 O O . GLU A 439 ? 0.4863 0.4387 0.4024 0.1454 -0.1551 -0.0517 480 GLU A O 3521 C CB A GLU A 439 ? 0.4602 0.4147 0.3704 0.1384 -0.1524 -0.0571 480 GLU A CB 3522 C CB B GLU A 439 ? 0.4742 0.4283 0.3838 0.1387 -0.1529 -0.0573 480 GLU A CB 3523 C CG A GLU A 439 ? 0.4791 0.4332 0.3869 0.1380 -0.1575 -0.0626 480 GLU A CG 3524 C CG B GLU A 439 ? 0.5579 0.4983 0.4391 0.1491 -0.1566 -0.0540 480 GLU A CG 3525 C CD A GLU A 439 ? 0.5355 0.4843 0.4366 0.1463 -0.1729 -0.0691 480 GLU A CD 3526 C CD B GLU A 439 ? 0.6232 0.5579 0.4909 0.1493 -0.1444 -0.0448 480 GLU A CD 3527 O OE1 A GLU A 439 ? 0.5833 0.5332 0.4878 0.1454 -0.1789 -0.0751 480 GLU A OE1 3528 O OE1 B GLU A 439 ? 0.6560 0.5924 0.5225 0.1434 -0.1330 -0.0412 480 GLU A OE1 3529 O OE2 A GLU A 439 ? 0.5647 0.5078 0.4569 0.1538 -0.1795 -0.0683 480 GLU A OE2 3530 O OE2 B GLU A 439 ? 0.6709 0.5993 0.5299 0.1552 -0.1465 -0.0414 480 GLU A OE2 3531 N N . LEU A 440 ? 0.4031 0.3751 0.3580 0.1302 -0.1453 -0.0544 481 LEU A N 3532 C CA . LEU A 440 ? 0.3886 0.3602 0.3462 0.1306 -0.1400 -0.0497 481 LEU A CA 3533 C C . LEU A 440 ? 0.3997 0.3777 0.3771 0.1325 -0.1481 -0.0541 481 LEU A C 3534 O O . LEU A 440 ? 0.4112 0.3983 0.4085 0.1294 -0.1534 -0.0603 481 LEU A O 3535 C CB . LEU A 440 ? 0.3603 0.3378 0.3266 0.1216 -0.1260 -0.0458 481 LEU A CB 3536 C CG . LEU A 440 ? 0.3661 0.3391 0.3168 0.1187 -0.1169 -0.0414 481 LEU A CG 3537 C CD1 . LEU A 440 ? 0.3418 0.3219 0.3043 0.1098 -0.1051 -0.0389 481 LEU A CD1 3538 C CD2 . LEU A 440 ? 0.3947 0.3553 0.3210 0.1254 -0.1148 -0.0353 481 LEU A CD2 3539 N N . LYS A 441 ? 0.4010 0.3743 0.3740 0.1373 -0.1483 -0.0505 482 LYS A N 3540 C CA A LYS A 441 ? 0.4189 0.3973 0.4096 0.1401 -0.1556 -0.0540 482 LYS A CA 3541 C CA B LYS A 441 ? 0.4190 0.3975 0.4100 0.1400 -0.1557 -0.0541 482 LYS A CA 3542 C C . LYS A 441 ? 0.3972 0.3875 0.4124 0.1318 -0.1471 -0.0548 482 LYS A C 3543 O O . LYS A 441 ? 0.4070 0.3971 0.4191 0.1266 -0.1350 -0.0499 482 LYS A O 3544 C CB A LYS A 441 ? 0.4370 0.4053 0.4136 0.1480 -0.1574 -0.0491 482 LYS A CB 3545 C CB B LYS A 441 ? 0.4395 0.4077 0.4160 0.1484 -0.1587 -0.0497 482 LYS A CB 3546 C CG A LYS A 441 ? 0.4797 0.4340 0.4275 0.1569 -0.1637 -0.0465 482 LYS A CG 3547 C CG B LYS A 441 ? 0.4817 0.4383 0.4354 0.1583 -0.1696 -0.0498 482 LYS A CG 3548 C CD A LYS A 441 ? 0.5239 0.4684 0.4600 0.1642 -0.1647 -0.0411 482 LYS A CD 3549 C CD B LYS A 441 ? 0.5311 0.4774 0.4718 0.1669 -0.1728 -0.0451 482 LYS A CD 3550 C CE A LYS A 441 ? 0.5671 0.4965 0.4725 0.1737 -0.1700 -0.0376 482 LYS A CE 3551 C CE B LYS A 441 ? 0.5639 0.5176 0.5277 0.1676 -0.1771 -0.0480 482 LYS A CE 3552 N NZ A LYS A 441 ? 0.6324 0.5616 0.5342 0.1782 -0.1830 -0.0444 482 LYS A NZ 3553 N NZ B LYS A 441 ? 0.6094 0.5525 0.5607 0.1778 -0.1843 -0.0448 482 LYS A NZ 3554 N N . SER A 442 ? 0.3844 0.3850 0.4239 0.1303 -0.1529 -0.0610 483 SER A N 3555 C CA . SER A 442 ? 0.3778 0.3891 0.4399 0.1235 -0.1447 -0.0616 483 SER A CA 3556 C C . SER A 442 ? 0.3748 0.3828 0.4364 0.1274 -0.1424 -0.0582 483 SER A C 3557 O O . SER A 442 ? 0.3814 0.3841 0.4390 0.1356 -0.1521 -0.0589 483 SER A O 3558 C CB . SER A 442 ? 0.3679 0.3914 0.4578 0.1212 -0.1509 -0.0689 483 SER A CB 3559 O OG . SER A 442 ? 0.3614 0.3944 0.4711 0.1153 -0.1417 -0.0690 483 SER A OG 3560 N N . PRO A 443 ? 0.3545 0.3652 0.4206 0.1218 -0.1304 -0.0549 484 PRO A N 3561 C CA . PRO A 443 ? 0.3707 0.3782 0.4379 0.1252 -0.1283 -0.0522 484 PRO A CA 3562 C C . PRO A 443 ? 0.3701 0.3889 0.4646 0.1240 -0.1295 -0.0572 484 PRO A C 3563 O O . PRO A 443 ? 0.3758 0.3935 0.4749 0.1264 -0.1275 -0.0559 484 PRO A O 3564 C CB . PRO A 443 ? 0.3558 0.3608 0.4150 0.1193 -0.1147 -0.0469 484 PRO A CB 3565 C CG . PRO A 443 ? 0.3429 0.3569 0.4111 0.1108 -0.1090 -0.0493 484 PRO A CG 3566 C CD . PRO A 443 ? 0.3492 0.3635 0.4151 0.1130 -0.1186 -0.0529 484 PRO A CD 3567 N N . ASP A 444 ? 0.3622 0.3918 0.4753 0.1200 -0.1321 -0.0629 485 ASP A N 3568 C CA . ASP A 444 ? 0.3548 0.3967 0.4955 0.1169 -0.1299 -0.0673 485 ASP A CA 3569 C C . ASP A 444 ? 0.3678 0.4117 0.5215 0.1244 -0.1414 -0.0714 485 ASP A C 3570 O O . ASP A 444 ? 0.3722 0.4121 0.5200 0.1302 -0.1535 -0.0734 485 ASP A O 3571 C CB . ASP A 444 ? 0.3386 0.3912 0.4959 0.1100 -0.1286 -0.0717 485 ASP A CB 3572 C CG . ASP A 444 ? 0.3426 0.3950 0.4908 0.1020 -0.1172 -0.0683 485 ASP A CG 3573 O OD1 . ASP A 444 ? 0.3854 0.4301 0.5156 0.1015 -0.1103 -0.0630 485 ASP A OD1 3574 O OD2 . ASP A 444 ? 0.3484 0.4083 0.5086 0.0962 -0.1153 -0.0711 485 ASP A OD2 3575 N N . GLU A 445 ? 0.3711 0.4213 0.5426 0.1243 -0.1379 -0.0729 486 GLU A N 3576 C CA A GLU A 445 ? 0.3892 0.4440 0.5785 0.1307 -0.1483 -0.0776 486 GLU A CA 3577 C CA B GLU A 445 ? 0.3842 0.4394 0.5742 0.1305 -0.1480 -0.0777 486 GLU A CA 3578 C C . GLU A 445 ? 0.3803 0.4450 0.5888 0.1292 -0.1564 -0.0842 486 GLU A C 3579 O O . GLU A 445 ? 0.3801 0.4538 0.6017 0.1213 -0.1497 -0.0862 486 GLU A O 3580 C CB A GLU A 445 ? 0.3857 0.4475 0.5937 0.1296 -0.1410 -0.0786 486 GLU A CB 3581 C CB B GLU A 445 ? 0.3766 0.4395 0.5861 0.1287 -0.1401 -0.0788 486 GLU A CB 3582 C CG A GLU A 445 ? 0.4300 0.4818 0.6230 0.1328 -0.1356 -0.0732 486 GLU A CG 3583 C CG B GLU A 445 ? 0.3964 0.4668 0.6300 0.1342 -0.1491 -0.0844 486 GLU A CG 3584 C CD A GLU A 445 ? 0.4696 0.5279 0.6830 0.1339 -0.1319 -0.0757 486 GLU A CD 3585 C CD B GLU A 445 ? 0.4156 0.4973 0.6736 0.1304 -0.1395 -0.0870 486 GLU A CD 3586 O OE1 A GLU A 445 ? 0.4851 0.5485 0.7157 0.1393 -0.1411 -0.0801 486 GLU A OE1 3587 O OE1 B GLU A 445 ? 0.4397 0.5232 0.6954 0.1234 -0.1261 -0.0847 486 GLU A OE1 3588 O OE2 A GLU A 445 ? 0.5014 0.5600 0.7142 0.1295 -0.1200 -0.0736 486 GLU A OE2 3589 O OE2 B GLU A 445 ? 0.4251 0.5139 0.7048 0.1346 -0.1455 -0.0916 486 GLU A OE2 3590 N N . GLY A 446 ? 0.4029 0.4653 0.6125 0.1368 -0.1711 -0.0875 487 GLY A N 3591 C CA . GLY A 446 ? 0.4037 0.4751 0.6328 0.1357 -0.1802 -0.0944 487 GLY A CA 3592 C C . GLY A 446 ? 0.4195 0.4851 0.6319 0.1351 -0.1856 -0.0946 487 GLY A C 3593 O O . GLY A 446 ? 0.4355 0.5062 0.6610 0.1354 -0.1954 -0.1005 487 GLY A O 3594 N N . PHE A 447 ? 0.4043 0.4591 0.5886 0.1341 -0.1793 -0.0885 488 PHE A N 3595 C CA . PHE A 447 ? 0.4073 0.4555 0.5734 0.1339 -0.1834 -0.0883 488 PHE A CA 3596 C C . PHE A 447 ? 0.4362 0.4690 0.5711 0.1423 -0.1890 -0.0838 488 PHE A C 3597 O O . PHE A 447 ? 0.4283 0.4531 0.5411 0.1417 -0.1872 -0.0810 488 PHE A O 3598 C CB . PHE A 447 ? 0.3906 0.4405 0.5518 0.1244 -0.1696 -0.0850 488 PHE A CB 3599 C CG . PHE A 447 ? 0.3692 0.4328 0.5577 0.1162 -0.1643 -0.0889 488 PHE A CG 3600 C CD1 . PHE A 447 ? 0.3729 0.4405 0.5698 0.1129 -0.1692 -0.0933 488 PHE A CD1 3601 C CD2 . PHE A 447 ? 0.3666 0.4386 0.5729 0.1119 -0.1544 -0.0884 488 PHE A CD2 3602 C CE1 . PHE A 447 ? 0.3681 0.4478 0.5907 0.1050 -0.1637 -0.0964 488 PHE A CE1 3603 C CE2 . PHE A 447 ? 0.3678 0.4522 0.5986 0.1043 -0.1484 -0.0916 488 PHE A CE2 3604 C CZ . PHE A 447 ? 0.3757 0.4638 0.6149 0.1008 -0.1531 -0.0954 488 PHE A CZ 3605 N N . GLU A 448 ? 0.4539 0.4822 0.5865 0.1502 -0.1954 -0.0831 489 GLU A N 3606 C CA . GLU A 448 ? 0.4934 0.5062 0.5959 0.1589 -0.2011 -0.0786 489 GLU A CA 3607 C C . GLU A 448 ? 0.4962 0.5038 0.5867 0.1636 -0.2140 -0.0824 489 GLU A C 3608 O O . GLU A 448 ? 0.5145 0.5292 0.6229 0.1652 -0.2254 -0.0898 489 GLU A O 3609 C CB . GLU A 448 ? 0.5068 0.5142 0.6076 0.1672 -0.2057 -0.0764 489 GLU A CB 3610 C CG . GLU A 448 ? 0.5549 0.5736 0.6863 0.1681 -0.2100 -0.0815 489 GLU A CG 3611 C CD . GLU A 448 ? 0.5026 0.5337 0.6573 0.1588 -0.1965 -0.0820 489 GLU A CD 3612 O OE1 . GLU A 448 ? 0.5264 0.5552 0.6781 0.1573 -0.1861 -0.0773 489 GLU A OE1 3613 O OE2 . GLU A 448 ? 0.5247 0.5680 0.7022 0.1535 -0.1970 -0.0877 489 GLU A OE2 3614 N N . GLY A 449 ? 0.4986 0.4945 0.5597 0.1654 -0.2116 -0.0777 490 GLY A N 3615 C CA . GLY A 449 ? 0.4999 0.4900 0.5471 0.1698 -0.2227 -0.0814 490 GLY A CA 3616 C C . GLY A 449 ? 0.4711 0.4686 0.5277 0.1616 -0.2196 -0.0854 490 GLY A C 3617 O O . GLY A 449 ? 0.4991 0.4923 0.5455 0.1644 -0.2283 -0.0891 490 GLY A O 3618 N N . LYS A 450 ? 0.4276 0.4357 0.5032 0.1517 -0.2076 -0.0848 491 LYS A N 3619 C CA A LYS A 450 ? 0.4120 0.4272 0.4978 0.1433 -0.2035 -0.0878 491 LYS A CA 3620 C CA B LYS A 450 ? 0.4127 0.4275 0.4978 0.1436 -0.2037 -0.0878 491 LYS A CA 3621 C C . LYS A 450 ? 0.3945 0.4043 0.4613 0.1383 -0.1896 -0.0811 491 LYS A C 3622 O O . LYS A 450 ? 0.3974 0.4019 0.4518 0.1391 -0.1813 -0.0746 491 LYS A O 3623 C CB A LYS A 450 ? 0.3929 0.4234 0.5128 0.1356 -0.1990 -0.0915 491 LYS A CB 3624 C CB B LYS A 450 ? 0.3956 0.4258 0.5154 0.1362 -0.2005 -0.0922 491 LYS A CB 3625 C CG A LYS A 450 ? 0.4047 0.4427 0.5488 0.1397 -0.2119 -0.0986 491 LYS A CG 3626 C CG B LYS A 450 ? 0.4073 0.4438 0.5487 0.1412 -0.2141 -0.0989 491 LYS A CG 3627 C CD A LYS A 450 ? 0.4250 0.4635 0.5734 0.1412 -0.2248 -0.1057 491 LYS A CD 3628 C CD B LYS A 450 ? 0.4405 0.4715 0.5738 0.1476 -0.2301 -0.1045 491 LYS A CD 3629 C CE A LYS A 450 ? 0.4594 0.5072 0.6363 0.1441 -0.2374 -0.1134 491 LYS A CE 3630 C CE B LYS A 450 ? 0.4751 0.5124 0.6309 0.1529 -0.2450 -0.1119 491 LYS A CE 3631 N NZ A LYS A 450 ? 0.4564 0.5192 0.6662 0.1357 -0.2285 -0.1150 491 LYS A NZ 3632 N NZ B LYS A 450 ? 0.5093 0.5386 0.6521 0.1631 -0.2523 -0.1097 491 LYS A NZ 3633 N N . SER A 451 ? 0.3929 0.4044 0.4591 0.1331 -0.1874 -0.0828 492 SER A N 3634 C CA . SER A 451 ? 0.3748 0.3820 0.4245 0.1282 -0.1748 -0.0770 492 SER A CA 3635 C C . SER A 451 ? 0.3524 0.3687 0.4185 0.1193 -0.1614 -0.0743 492 SER A C 3636 O O . SER A 451 ? 0.3344 0.3615 0.4259 0.1153 -0.1615 -0.0781 492 SER A O 3637 C CB . SER A 451 ? 0.3908 0.3966 0.4351 0.1259 -0.1774 -0.0801 492 SER A CB 3638 O OG . SER A 451 ? 0.3900 0.4072 0.4597 0.1179 -0.1756 -0.0844 492 SER A OG 3639 N N . LEU A 452 ? 0.3420 0.3539 0.3933 0.1161 -0.1498 -0.0681 493 LEU A N 3640 C CA . LEU A 452 ? 0.3303 0.3499 0.3941 0.1074 -0.1371 -0.0658 493 LEU A CA 3641 C C . LEU A 452 ? 0.3290 0.3570 0.4088 0.1003 -0.1362 -0.0699 493 LEU A C 3642 O O . LEU A 452 ? 0.3073 0.3449 0.4071 0.0941 -0.1302 -0.0709 493 LEU A O 3643 C CB . LEU A 452 ? 0.3209 0.3334 0.3642 0.1056 -0.1264 -0.0588 493 LEU A CB 3644 C CG . LEU A 452 ? 0.3097 0.3282 0.3611 0.0971 -0.1134 -0.0560 493 LEU A CG 3645 C CD1 . LEU A 452 ? 0.2988 0.3242 0.3682 0.0956 -0.1100 -0.0566 493 LEU A CD1 3646 C CD2 . LEU A 452 ? 0.3041 0.3144 0.3344 0.0968 -0.1050 -0.0495 493 LEU A CD2 3647 N N . TYR A 453 ? 0.3278 0.3519 0.3987 0.1012 -0.1417 -0.0721 494 TYR A N 3648 C CA . TYR A 453 ? 0.3252 0.3563 0.4117 0.0947 -0.1413 -0.0759 494 TYR A CA 3649 C C . TYR A 453 ? 0.3161 0.3576 0.4311 0.0932 -0.1468 -0.0815 494 TYR A C 3650 O O . TYR A 453 ? 0.3157 0.3659 0.4495 0.0858 -0.1408 -0.0825 494 TYR A O 3651 C CB . TYR A 453 ? 0.3378 0.3625 0.4117 0.0973 -0.1489 -0.0786 494 TYR A CB 3652 C CG . TYR A 453 ? 0.3374 0.3682 0.4271 0.0905 -0.1487 -0.0824 494 TYR A CG 3653 C CD1 . TYR A 453 ? 0.3214 0.3519 0.4060 0.0843 -0.1389 -0.0791 494 TYR A CD1 3654 C CD2 . TYR A 453 ? 0.3531 0.3897 0.4633 0.0904 -0.1585 -0.0893 494 TYR A CD2 3655 C CE1 . TYR A 453 ? 0.3355 0.3706 0.4340 0.0783 -0.1387 -0.0821 494 TYR A CE1 3656 C CE2 . TYR A 453 ? 0.3376 0.3791 0.4629 0.0840 -0.1580 -0.0924 494 TYR A CE2 3657 C CZ . TYR A 453 ? 0.3515 0.3919 0.4702 0.0780 -0.1480 -0.0886 494 TYR A CZ 3658 O OH . TYR A 453 ? 0.3575 0.4018 0.4905 0.0718 -0.1471 -0.0911 494 TYR A OH 3659 N N . GLU A 454 ? 0.3202 0.3605 0.4381 0.1003 -0.1583 -0.0852 495 GLU A N 3660 C CA A GLU A 454 ? 0.3340 0.3843 0.4802 0.0997 -0.1649 -0.0911 495 GLU A CA 3661 C CA B GLU A 454 ? 0.3299 0.3802 0.4760 0.0998 -0.1649 -0.0911 495 GLU A CA 3662 C C . GLU A 454 ? 0.3181 0.3776 0.4826 0.0951 -0.1548 -0.0892 495 GLU A C 3663 O O . GLU A 454 ? 0.3131 0.3827 0.5014 0.0889 -0.1515 -0.0919 495 GLU A O 3664 C CB A GLU A 454 ? 0.3534 0.4000 0.4978 0.1092 -0.1802 -0.0954 495 GLU A CB 3665 C CB B GLU A 454 ? 0.3464 0.3927 0.4901 0.1093 -0.1799 -0.0951 495 GLU A CB 3666 C CG A GLU A 454 ? 0.3779 0.4354 0.5526 0.1092 -0.1860 -0.1008 495 GLU A CG 3667 C CG B GLU A 454 ? 0.3539 0.4107 0.5280 0.1089 -0.1888 -0.1024 495 GLU A CG 3668 C CD A GLU A 454 ? 0.4319 0.4900 0.6161 0.1141 -0.2027 -0.1086 495 GLU A CD 3669 C CD B GLU A 454 ? 0.3838 0.4370 0.5562 0.1188 -0.2039 -0.1063 495 GLU A CD 3670 O OE1 A GLU A 454 ? 0.4511 0.5002 0.6164 0.1183 -0.2107 -0.1101 495 GLU A OE1 3671 O OE1 B GLU A 454 ? 0.4182 0.4606 0.5675 0.1255 -0.2125 -0.1067 495 GLU A OE1 3672 O OE2 A GLU A 454 ? 0.4381 0.5060 0.6496 0.1138 -0.2080 -0.1136 495 GLU A OE2 3673 O OE2 B GLU A 454 ? 0.3685 0.4295 0.5623 0.1203 -0.2072 -0.1091 495 GLU A OE2 3674 N N . SER A 455 ? 0.3224 0.3778 0.4752 0.0978 -0.1494 -0.0844 496 SER A N 3675 C CA . SER A 455 ? 0.3179 0.3810 0.4864 0.0942 -0.1400 -0.0829 496 SER A CA 3676 C C . SER A 455 ? 0.3132 0.3811 0.4858 0.0849 -0.1265 -0.0802 496 SER A C 3677 O O . SER A 455 ? 0.3088 0.3865 0.5027 0.0798 -0.1206 -0.0817 496 SER A O 3678 C CB . SER A 455 ? 0.3319 0.3888 0.4872 0.0995 -0.1378 -0.0786 496 SER A CB 3679 O OG . SER A 455 ? 0.3335 0.3802 0.4624 0.0999 -0.1320 -0.0727 496 SER A OG 3680 N N . TRP A 456 ? 0.3020 0.3626 0.4536 0.0831 -0.1215 -0.0760 497 TRP A N 3681 C CA . TRP A 456 ? 0.2967 0.3604 0.4493 0.0750 -0.1098 -0.0732 497 TRP A CA 3682 C C . TRP A 456 ? 0.2992 0.3708 0.4715 0.0692 -0.1103 -0.0770 497 TRP A C 3683 O O . TRP A 456 ? 0.2808 0.3595 0.4663 0.0628 -0.1010 -0.0763 497 TRP A O 3684 C CB . TRP A 456 ? 0.2929 0.3470 0.4198 0.0752 -0.1067 -0.0686 497 TRP A CB 3685 C CG . TRP A 456 ? 0.2988 0.3544 0.4232 0.0677 -0.0960 -0.0656 497 TRP A CG 3686 C CD1 . TRP A 456 ? 0.2798 0.3421 0.4157 0.0615 -0.0860 -0.0643 497 TRP A CD1 3687 C CD2 . TRP A 456 ? 0.2830 0.3325 0.3909 0.0663 -0.0944 -0.0632 497 TRP A CD2 3688 N NE1 . TRP A 456 ? 0.2573 0.3179 0.3845 0.0564 -0.0788 -0.0612 497 TRP A NE1 3689 C CE2 . TRP A 456 ? 0.2785 0.3316 0.3895 0.0591 -0.0839 -0.0606 497 TRP A CE2 3690 C CE3 . TRP A 456 ? 0.3064 0.3476 0.3969 0.0709 -0.1010 -0.0632 497 TRP A CE3 3691 C CZ2 . TRP A 456 ? 0.3001 0.3489 0.3982 0.0562 -0.0801 -0.0580 497 TRP A CZ2 3692 C CZ3 . TRP A 456 ? 0.3077 0.3450 0.3858 0.0680 -0.0965 -0.0607 497 TRP A CZ3 3693 C CH2 . TRP A 456 ? 0.3108 0.3521 0.3935 0.0606 -0.0864 -0.0581 497 TRP A CH2 3694 N N . THR A 457 ? 0.2939 0.3637 0.4673 0.0716 -0.1209 -0.0811 498 THR A N 3695 C CA . THR A 457 ? 0.3128 0.3891 0.5051 0.0661 -0.1221 -0.0848 498 THR A CA 3696 C C . THR A 457 ? 0.3135 0.4012 0.5355 0.0641 -0.1220 -0.0885 498 THR A C 3697 O O . THR A 457 ? 0.3081 0.4031 0.5472 0.0570 -0.1150 -0.0888 498 THR A O 3698 C CB . THR A 457 ? 0.3321 0.4030 0.5186 0.0696 -0.1344 -0.0889 498 THR A CB 3699 O OG1 A THR A 457 ? 0.3273 0.3888 0.4882 0.0702 -0.1317 -0.0851 498 THR A OG1 3700 C CG2 A THR A 457 ? 0.3672 0.4447 0.5755 0.0638 -0.1360 -0.0931 498 THR A CG2 3701 N N . LYS A 458 ? 0.3201 0.4091 0.5474 0.0702 -0.1286 -0.0908 499 LYS A N 3702 C CA A LYS A 458 ? 0.3242 0.4243 0.5802 0.0691 -0.1289 -0.0946 499 LYS A CA 3703 C CA B LYS A 458 ? 0.3216 0.4216 0.5775 0.0692 -0.1289 -0.0946 499 LYS A CA 3704 C C . LYS A 458 ? 0.3151 0.4210 0.5780 0.0638 -0.1140 -0.0909 499 LYS A C 3705 O O . LYS A 458 ? 0.3180 0.4335 0.6040 0.0584 -0.1084 -0.0926 499 LYS A O 3706 C CB A LYS A 458 ? 0.3348 0.4341 0.5934 0.0778 -0.1402 -0.0978 499 LYS A CB 3707 C CB B LYS A 458 ? 0.3317 0.4307 0.5895 0.0779 -0.1398 -0.0975 499 LYS A CB 3708 C CG A LYS A 458 ? 0.3593 0.4704 0.6506 0.0777 -0.1440 -0.1033 499 LYS A CG 3709 C CG B LYS A 458 ? 0.3389 0.4497 0.6270 0.0776 -0.1403 -0.1015 499 LYS A CG 3710 C CD A LYS A 458 ? 0.3879 0.4968 0.6800 0.0871 -0.1587 -0.1072 499 LYS A CD 3711 C CD B LYS A 458 ? 0.3642 0.4828 0.6777 0.0750 -0.1477 -0.1078 499 LYS A CD 3712 C CE A LYS A 458 ? 0.3965 0.5149 0.7189 0.0876 -0.1693 -0.1149 499 LYS A CE 3713 C CE B LYS A 458 ? 0.3548 0.4856 0.7002 0.0752 -0.1486 -0.1120 499 LYS A CE 3714 N NZ A LYS A 458 ? 0.4154 0.5452 0.7648 0.0871 -0.1653 -0.1168 499 LYS A NZ 3715 N NZ B LYS A 458 ? 0.3732 0.5124 0.7456 0.0708 -0.1531 -0.1174 499 LYS A NZ 3716 N N . LYS A 459 ? 0.3013 0.4009 0.5436 0.0650 -0.1072 -0.0858 500 LYS A N 3717 C CA . LYS A 459 ? 0.2940 0.3979 0.5404 0.0613 -0.0940 -0.0828 500 LYS A CA 3718 C C . LYS A 459 ? 0.3086 0.4131 0.5507 0.0535 -0.0824 -0.0793 500 LYS A C 3719 O O . LYS A 459 ? 0.3118 0.4221 0.5630 0.0494 -0.0718 -0.0781 500 LYS A O 3720 C CB . LYS A 459 ? 0.3027 0.3995 0.5308 0.0663 -0.0927 -0.0795 500 LYS A CB 3721 C CG . LYS A 459 ? 0.3003 0.3979 0.5365 0.0739 -0.1021 -0.0826 500 LYS A CG 3722 C CD . LYS A 459 ? 0.3255 0.4147 0.5427 0.0788 -0.1003 -0.0787 500 LYS A CD 3723 C CE . LYS A 459 ? 0.3588 0.4491 0.5854 0.0860 -0.1083 -0.0814 500 LYS A CE 3724 N NZ . LYS A 459 ? 0.3455 0.4270 0.5545 0.0907 -0.1063 -0.0773 500 LYS A NZ 3725 N N . SER A 460 ? 0.2945 0.3925 0.5213 0.0521 -0.0844 -0.0776 501 SER A N 3726 C CA . SER A 460 ? 0.3019 0.3989 0.5216 0.0454 -0.0744 -0.0738 501 SER A CA 3727 C C . SER A 460 ? 0.3199 0.4155 0.5411 0.0427 -0.0793 -0.0753 501 SER A C 3728 O O . SER A 460 ? 0.3199 0.4078 0.5221 0.0431 -0.0807 -0.0731 501 SER A O 3729 C CB . SER A 460 ? 0.2994 0.3880 0.4936 0.0466 -0.0697 -0.0689 501 SER A CB 3730 O OG . SER A 460 ? 0.3416 0.4302 0.5305 0.0405 -0.0593 -0.0653 501 SER A OG 3731 N N . PRO A 461 ? 0.3283 0.4315 0.5734 0.0400 -0.0820 -0.0793 502 PRO A N 3732 C CA . PRO A 461 ? 0.3490 0.4510 0.5987 0.0376 -0.0877 -0.0815 502 PRO A CA 3733 C C . PRO A 461 ? 0.3651 0.4644 0.6061 0.0313 -0.0785 -0.0772 502 PRO A C 3734 O O . PRO A 461 ? 0.3565 0.4589 0.5994 0.0268 -0.0670 -0.0738 502 PRO A O 3735 C CB . PRO A 461 ? 0.3489 0.4610 0.6299 0.0353 -0.0903 -0.0864 502 PRO A CB 3736 C CG . PRO A 461 ? 0.3417 0.4610 0.6339 0.0350 -0.0823 -0.0855 502 PRO A CG 3737 C CD . PRO A 461 ? 0.3279 0.4410 0.5979 0.0398 -0.0808 -0.0824 502 PRO A CD 3738 N N . SER A 462 ? 0.3904 0.4832 0.6209 0.0315 -0.0841 -0.0776 503 SER A N 3739 C CA . SER A 462 ? 0.4353 0.5254 0.6605 0.0257 -0.0776 -0.0744 503 SER A CA 3740 C C . SER A 462 ? 0.4523 0.5503 0.7023 0.0192 -0.0724 -0.0753 503 SER A C 3741 O O . SER A 462 ? 0.4625 0.5657 0.7334 0.0195 -0.0792 -0.0802 503 SER A O 3742 C CB . SER A 462 ? 0.4357 0.5183 0.6501 0.0278 -0.0866 -0.0763 503 SER A CB 3743 O OG . SER A 462 ? 0.4858 0.5666 0.6995 0.0220 -0.0811 -0.0738 503 SER A OG 3744 N N . PRO A 463 ? 0.4766 0.5753 0.7247 0.0135 -0.0605 -0.0705 504 PRO A N 3745 C CA . PRO A 463 ? 0.5042 0.6089 0.7731 0.0068 -0.0539 -0.0701 504 PRO A CA 3746 C C . PRO A 463 ? 0.5388 0.6402 0.8140 0.0043 -0.0601 -0.0720 504 PRO A C 3747 O O . PRO A 463 ? 0.5446 0.6515 0.8432 0.0001 -0.0596 -0.0740 504 PRO A O 3748 C CB . PRO A 463 ? 0.4960 0.5992 0.7531 0.0028 -0.0406 -0.0639 504 PRO A CB 3749 C CG . PRO A 463 ? 0.4874 0.5826 0.7169 0.0067 -0.0420 -0.0613 504 PRO A CG 3750 C CD . PRO A 463 ? 0.4754 0.5694 0.7013 0.0135 -0.0524 -0.0652 504 PRO A CD 3751 N N . GLU A 464 ? 0.5707 0.6635 0.8261 0.0070 -0.0660 -0.0718 505 GLU A N 3752 C CA . GLU A 464 ? 0.6033 0.6914 0.8611 0.0054 -0.0725 -0.0739 505 GLU A CA 3753 C C . GLU A 464 ? 0.6135 0.7017 0.8811 0.0098 -0.0870 -0.0812 505 GLU A C 3754 O O . GLU A 464 ? 0.6182 0.7085 0.9050 0.0066 -0.0912 -0.0846 505 GLU A O 3755 C CB . GLU A 464 ? 0.6115 0.6900 0.8434 0.0065 -0.0717 -0.0705 505 GLU A CB 3756 C CG . GLU A 464 ? 0.6578 0.7350 0.8743 0.0043 -0.0598 -0.0638 505 GLU A CG 3757 C CD . GLU A 464 ? 0.7242 0.8033 0.9500 -0.0030 -0.0495 -0.0597 505 GLU A CD 3758 O OE1 . GLU A 464 ? 0.7509 0.8302 0.9916 -0.0066 -0.0516 -0.0613 505 GLU A OE1 3759 O OE2 . GLU A 464 ? 0.7514 0.8312 0.9689 -0.0049 -0.0395 -0.0550 505 GLU A OE2 3760 N N . PHE A 465 ? 0.6181 0.7036 0.8727 0.0170 -0.0948 -0.0834 506 PHE A N 3761 C CA . PHE A 465 ? 0.6275 0.7104 0.8847 0.0221 -0.1094 -0.0901 506 PHE A CA 3762 C C . PHE A 465 ? 0.6203 0.7077 0.8855 0.0277 -0.1170 -0.0942 506 PHE A C 3763 O O . PHE A 465 ? 0.6190 0.7067 0.8731 0.0312 -0.1138 -0.0916 506 PHE A O 3764 C CB . PHE A 465 ? 0.6455 0.7176 0.8758 0.0268 -0.1148 -0.0898 506 PHE A CB 3765 C CG . PHE A 465 ? 0.6694 0.7364 0.8883 0.0223 -0.1070 -0.0851 506 PHE A CG 3766 C CD1 . PHE A 465 ? 0.6797 0.7438 0.8790 0.0222 -0.0976 -0.0789 506 PHE A CD1 3767 C CD2 . PHE A 465 ? 0.6969 0.7617 0.9253 0.0182 -0.1093 -0.0870 506 PHE A CD2 3768 C CE1 . PHE A 465 ? 0.6945 0.7540 0.8836 0.0184 -0.0910 -0.0747 506 PHE A CE1 3769 C CE2 . PHE A 465 ? 0.7140 0.7737 0.9318 0.0145 -0.1023 -0.0825 506 PHE A CE2 3770 C CZ . PHE A 465 ? 0.7050 0.7622 0.9029 0.0147 -0.0933 -0.0763 506 PHE A CZ 3771 N N . SER A 466 ? 0.6089 0.6996 0.8936 0.0286 -0.1276 -0.1008 507 SER A N 3772 C CA . SER A 466 ? 0.5906 0.6857 0.8854 0.0342 -0.1369 -0.1056 507 SER A CA 3773 C C . SER A 466 ? 0.5744 0.6606 0.8425 0.0431 -0.1457 -0.1064 507 SER A C 3774 O O . SER A 466 ? 0.5855 0.6628 0.8358 0.0456 -0.1511 -0.1073 507 SER A O 3775 C CB . SER A 466 ? 0.6024 0.7024 0.9245 0.0331 -0.1476 -0.1131 507 SER A CB 3776 O OG . SER A 466 ? 0.6176 0.7292 0.9682 0.0299 -0.1436 -0.1142 507 SER A OG 3777 N N . GLY A 467 ? 0.5345 0.6228 0.7996 0.0481 -0.1466 -0.1059 508 GLY A N 3778 C CA . GLY A 467 ? 0.5051 0.5851 0.7467 0.0571 -0.1553 -0.1066 508 GLY A CA 3779 C C . GLY A 467 ? 0.4637 0.5348 0.6748 0.0582 -0.1477 -0.1001 508 GLY A C 3780 O O . GLY A 467 ? 0.4675 0.5299 0.6562 0.0652 -0.1540 -0.1001 508 GLY A O 3781 N N . MET A 468 ? 0.4334 0.5068 0.6444 0.0515 -0.1342 -0.0948 509 MET A N 3782 C CA A MET A 468 ? 0.4176 0.4845 0.6036 0.0514 -0.1252 -0.0883 509 MET A CA 3783 C CA B MET A 468 ? 0.4209 0.4877 0.6067 0.0520 -0.1258 -0.0884 509 MET A CA 3784 C C . MET A 468 ? 0.3987 0.4703 0.5866 0.0490 -0.1137 -0.0835 509 MET A C 3785 O O . MET A 468 ? 0.3842 0.4644 0.5930 0.0442 -0.1085 -0.0839 509 MET A O 3786 C CB A MET A 468 ? 0.4136 0.4778 0.5955 0.0455 -0.1193 -0.0860 509 MET A CB 3787 C CB B MET A 468 ? 0.4181 0.4803 0.5949 0.0478 -0.1217 -0.0864 509 MET A CB 3788 C CG A MET A 468 ? 0.4318 0.4921 0.6160 0.0461 -0.1289 -0.0909 509 MET A CG 3789 C CG B MET A 468 ? 0.4570 0.5093 0.6127 0.0536 -0.1300 -0.0880 509 MET A CG 3790 S SD A MET A 468 ? 0.4594 0.5087 0.6176 0.0559 -0.1405 -0.0935 509 MET A SD 3791 S SD B MET A 468 ? 0.4665 0.5151 0.6215 0.0488 -0.1293 -0.0887 509 MET A SD 3792 C CE A MET A 468 ? 0.4271 0.4697 0.5576 0.0559 -0.1293 -0.0857 509 MET A CE 3793 C CE B MET A 468 ? 0.4667 0.5198 0.6255 0.0404 -0.1130 -0.0817 509 MET A CE 3794 N N . PRO A 469 ? 0.3774 0.4432 0.5435 0.0519 -0.1092 -0.0788 510 PRO A N 3795 C CA . PRO A 469 ? 0.3554 0.4249 0.5223 0.0493 -0.0982 -0.0746 510 PRO A CA 3796 C C . PRO A 469 ? 0.3296 0.3995 0.4927 0.0424 -0.0866 -0.0700 510 PRO A C 3797 O O . PRO A 469 ? 0.3299 0.3954 0.4842 0.0405 -0.0865 -0.0691 510 PRO A O 3798 C CB . PRO A 469 ? 0.3592 0.4214 0.5046 0.0557 -0.0997 -0.0719 510 PRO A CB 3799 C CG . PRO A 469 ? 0.3744 0.4277 0.5007 0.0586 -0.1050 -0.0718 510 PRO A CG 3800 C CD . PRO A 469 ? 0.3857 0.4414 0.5265 0.0582 -0.1142 -0.0777 510 PRO A CD 3801 N N . ARG A 470 ? 0.3061 0.3808 0.4745 0.0392 -0.0769 -0.0673 511 ARG A N 3802 C CA . ARG A 470 ? 0.2930 0.3675 0.4559 0.0335 -0.0661 -0.0629 511 ARG A CA 3803 C C . ARG A 470 ? 0.2863 0.3530 0.4247 0.0356 -0.0633 -0.0587 511 ARG A C 3804 O O . ARG A 470 ? 0.2800 0.3440 0.4093 0.0399 -0.0640 -0.0577 511 ARG A O 3805 C CB . ARG A 470 ? 0.3051 0.3869 0.4807 0.0302 -0.0571 -0.0619 511 ARG A CB 3806 C CG . ARG A 470 ? 0.3158 0.3975 0.4852 0.0247 -0.0458 -0.0575 511 ARG A CG 3807 C CD . ARG A 470 ? 0.3849 0.4728 0.5640 0.0230 -0.0375 -0.0570 511 ARG A CD 3808 N NE . ARG A 470 ? 0.4155 0.5114 0.6183 0.0203 -0.0367 -0.0599 511 ARG A NE 3809 C CZ . ARG A 470 ? 0.4704 0.5698 0.6824 0.0144 -0.0297 -0.0585 511 ARG A CZ 3810 N NH1 . ARG A 470 ? 0.4858 0.5807 0.6840 0.0109 -0.0235 -0.0544 511 ARG A NH1 3811 N NH2 . ARG A 470 ? 0.4710 0.5779 0.7062 0.0120 -0.0288 -0.0612 511 ARG A NH2 3812 N N . ILE A 471 ? 0.2660 0.3290 0.3947 0.0325 -0.0601 -0.0562 512 ILE A N 3813 C CA . ILE A 471 ? 0.2728 0.3299 0.3817 0.0331 -0.0554 -0.0519 512 ILE A CA 3814 C C . ILE A 471 ? 0.2779 0.3367 0.3873 0.0268 -0.0464 -0.0488 512 ILE A C 3815 O O . ILE A 471 ? 0.3026 0.3624 0.4190 0.0232 -0.0466 -0.0494 512 ILE A O 3816 C CB . ILE A 471 ? 0.2600 0.3095 0.3535 0.0368 -0.0616 -0.0520 512 ILE A CB 3817 C CG1 . ILE A 471 ? 0.3065 0.3530 0.3967 0.0438 -0.0711 -0.0550 512 ILE A CG1 3818 C CG2 . ILE A 471 ? 0.2560 0.3005 0.3314 0.0363 -0.0553 -0.0473 512 ILE A CG2 3819 C CD1 . ILE A 471 ? 0.3213 0.3597 0.3946 0.0484 -0.0773 -0.0554 512 ILE A CD1 3820 N N . SER A 472 ? 0.2652 0.3239 0.3674 0.0255 -0.0390 -0.0455 513 SER A N 3821 C CA . SER A 472 ? 0.2657 0.3262 0.3686 0.0200 -0.0307 -0.0429 513 SER A CA 3822 C C . SER A 472 ? 0.2728 0.3276 0.3597 0.0193 -0.0288 -0.0396 513 SER A C 3823 O O . SER A 472 ? 0.2607 0.3106 0.3362 0.0231 -0.0328 -0.0393 513 SER A O 3824 C CB . SER A 472 ? 0.2744 0.3387 0.3808 0.0188 -0.0237 -0.0420 513 SER A CB 3825 O OG . SER A 472 ? 0.2969 0.3674 0.4211 0.0189 -0.0249 -0.0452 513 SER A OG 3826 N N A LYS A 473 ? 0.2746 0.3302 0.3611 0.0147 -0.0225 -0.0372 514 LYS A N 3827 N N B LYS A 473 ? 0.2704 0.3259 0.3565 0.0147 -0.0223 -0.0371 514 LYS A N 3828 C CA A LYS A 473 ? 0.2716 0.3224 0.3445 0.0136 -0.0204 -0.0341 514 LYS A CA 3829 C CA B LYS A 473 ? 0.2686 0.3195 0.3413 0.0136 -0.0204 -0.0340 514 LYS A CA 3830 C C A LYS A 473 ? 0.2870 0.3364 0.3494 0.0149 -0.0166 -0.0321 514 LYS A C 3831 C C B LYS A 473 ? 0.2731 0.3227 0.3355 0.0135 -0.0151 -0.0314 514 LYS A C 3832 O O A LYS A 473 ? 0.2920 0.3443 0.3583 0.0150 -0.0136 -0.0326 514 LYS A O 3833 O O B LYS A 473 ? 0.2413 0.2939 0.3068 0.0117 -0.0097 -0.0311 514 LYS A O 3834 C CB A LYS A 473 ? 0.2719 0.3239 0.3485 0.0084 -0.0153 -0.0321 514 LYS A CB 3835 C CB B LYS A 473 ? 0.2763 0.3273 0.3530 0.0091 -0.0178 -0.0327 514 LYS A CB 3836 C CG A LYS A 473 ? 0.2533 0.3066 0.3423 0.0065 -0.0185 -0.0339 514 LYS A CG 3837 C CG B LYS A 473 ? 0.2717 0.3265 0.3546 0.0049 -0.0103 -0.0312 514 LYS A CG 3838 C CD A LYS A 473 ? 0.2685 0.3214 0.3597 0.0015 -0.0133 -0.0312 514 LYS A CD 3839 C CD B LYS A 473 ? 0.2773 0.3310 0.3630 0.0007 -0.0077 -0.0292 514 LYS A CD 3840 C CE A LYS A 473 ? 0.2863 0.3436 0.3840 -0.0018 -0.0054 -0.0298 514 LYS A CE 3841 C CE B LYS A 473 ? 0.2880 0.3417 0.3843 0.0004 -0.0134 -0.0315 514 LYS A CE 3842 N NZ A LYS A 473 ? 0.2811 0.3440 0.3973 -0.0028 -0.0058 -0.0326 514 LYS A NZ 3843 N NZ B LYS A 473 ? 0.3068 0.3664 0.4211 -0.0013 -0.0123 -0.0337 514 LYS A NZ 3844 N N . LEU A 474 ? 0.2812 0.3262 0.3314 0.0155 -0.0166 -0.0299 515 LEU A N 3845 C CA . LEU A 474 ? 0.2913 0.3348 0.3324 0.0157 -0.0125 -0.0278 515 LEU A CA 3846 C C . LEU A 474 ? 0.3148 0.3591 0.3538 0.0115 -0.0068 -0.0257 515 LEU A C 3847 O O . LEU A 474 ? 0.3424 0.3852 0.3792 0.0094 -0.0066 -0.0243 515 LEU A O 3848 C CB . LEU A 474 ? 0.2895 0.3280 0.3192 0.0187 -0.0151 -0.0264 515 LEU A CB 3849 C CG . LEU A 474 ? 0.2609 0.2969 0.2879 0.0238 -0.0201 -0.0276 515 LEU A CG 3850 C CD1 . LEU A 474 ? 0.2656 0.2967 0.2813 0.0262 -0.0218 -0.0261 515 LEU A CD1 3851 C CD2 . LEU A 474 ? 0.2517 0.2877 0.2781 0.0259 -0.0187 -0.0275 515 LEU A CD2 3852 N N . GLY A 475 ? 0.3250 0.3707 0.3631 0.0107 -0.0025 -0.0255 516 GLY A N 3853 C CA . GLY A 475 ? 0.3099 0.3552 0.3428 0.0077 0.0022 -0.0237 516 GLY A CA 3854 C C . GLY A 475 ? 0.2922 0.3351 0.3166 0.0090 0.0030 -0.0229 516 GLY A C 3855 O O . GLY A 475 ? 0.2909 0.3309 0.3092 0.0104 0.0006 -0.0217 516 GLY A O 3856 N N . SER A 476 ? 0.2953 0.3393 0.3195 0.0083 0.0067 -0.0237 517 SER A N 3857 C CA . SER A 476 ? 0.2789 0.3206 0.2972 0.0094 0.0071 -0.0234 517 SER A CA 3858 C C . SER A 476 ? 0.2573 0.3001 0.2800 0.0111 0.0084 -0.0255 517 SER A C 3859 O O . SER A 476 ? 0.2989 0.3440 0.3291 0.0124 0.0077 -0.0271 517 SER A O 3860 C CB . SER A 476 ? 0.3064 0.3470 0.3181 0.0070 0.0095 -0.0224 517 SER A CB 3861 O OG . SER A 476 ? 0.3702 0.4089 0.3778 0.0077 0.0099 -0.0227 517 SER A OG 3862 N N . GLY A 477 ? 0.2287 0.2697 0.2473 0.0111 0.0101 -0.0258 518 GLY A N 3863 C CA . GLY A 477 ? 0.2311 0.2723 0.2532 0.0127 0.0115 -0.0278 518 GLY A CA 3864 C C . GLY A 477 ? 0.2167 0.2545 0.2377 0.0156 0.0089 -0.0270 518 GLY A C 3865 O O . GLY A 477 ? 0.2295 0.2664 0.2532 0.0173 0.0096 -0.0284 518 GLY A O 3866 N N . ASN A 478 ? 0.1959 0.2315 0.2129 0.0166 0.0062 -0.0247 519 ASN A N 3867 C CA . ASN A 478 ? 0.1993 0.2311 0.2140 0.0196 0.0046 -0.0233 519 ASN A CA 3868 C C . ASN A 478 ? 0.2055 0.2349 0.2142 0.0198 0.0036 -0.0207 519 ASN A C 3869 O O . ASN A 478 ? 0.1940 0.2248 0.2008 0.0177 0.0034 -0.0203 519 ASN A O 3870 C CB . ASN A 478 ? 0.1952 0.2268 0.2137 0.0233 0.0018 -0.0239 519 ASN A CB 3871 C CG . ASN A 478 ? 0.2254 0.2534 0.2439 0.0258 0.0022 -0.0236 519 ASN A CG 3872 O OD1 . ASN A 478 ? 0.2445 0.2682 0.2578 0.0269 0.0025 -0.0211 519 ASN A OD1 3873 N ND2 . ASN A 478 ? 0.2105 0.2401 0.2353 0.0267 0.0027 -0.0259 519 ASN A ND2 3874 N N . ASP A 479 ? 0.1957 0.2213 0.2015 0.0223 0.0032 -0.0188 520 ASP A N 3875 C CA . ASP A 479 ? 0.1963 0.2195 0.1971 0.0222 0.0039 -0.0163 520 ASP A CA 3876 C C . ASP A 479 ? 0.1957 0.2188 0.1926 0.0234 0.0016 -0.0151 520 ASP A C 3877 O O . ASP A 479 ? 0.2076 0.2297 0.2013 0.0231 0.0025 -0.0134 520 ASP A O 3878 C CB . ASP A 479 ? 0.1984 0.2171 0.1975 0.0246 0.0051 -0.0141 520 ASP A CB 3879 C CG . ASP A 479 ? 0.2320 0.2500 0.2346 0.0225 0.0077 -0.0150 520 ASP A CG 3880 O OD1 . ASP A 479 ? 0.2252 0.2453 0.2290 0.0192 0.0089 -0.0160 520 ASP A OD1 3881 O OD2 . ASP A 479 ? 0.2228 0.2379 0.2271 0.0244 0.0082 -0.0149 520 ASP A OD2 3882 N N . PHE A 480 ? 0.1960 0.2204 0.1943 0.0247 -0.0013 -0.0165 521 PHE A N 3883 C CA . PHE A 480 ? 0.2126 0.2367 0.2077 0.0256 -0.0038 -0.0161 521 PHE A CA 3884 C C . PHE A 480 ? 0.2054 0.2321 0.2013 0.0219 -0.0029 -0.0163 521 PHE A C 3885 O O . PHE A 480 ? 0.2033 0.2293 0.1966 0.0224 -0.0046 -0.0159 521 PHE A O 3886 C CB . PHE A 480 ? 0.2206 0.2455 0.2188 0.0277 -0.0078 -0.0182 521 PHE A CB 3887 C CG . PHE A 480 ? 0.2030 0.2325 0.2094 0.0247 -0.0074 -0.0205 521 PHE A CG 3888 C CD1 . PHE A 480 ? 0.2149 0.2469 0.2235 0.0215 -0.0072 -0.0210 521 PHE A CD1 3889 C CD2 . PHE A 480 ? 0.2598 0.2907 0.2714 0.0251 -0.0064 -0.0219 521 PHE A CD2 3890 C CE1 . PHE A 480 ? 0.2410 0.2769 0.2568 0.0187 -0.0055 -0.0226 521 PHE A CE1 3891 C CE2 . PHE A 480 ? 0.2501 0.2854 0.2693 0.0224 -0.0049 -0.0239 521 PHE A CE2 3892 C CZ . PHE A 480 ? 0.2580 0.2956 0.2788 0.0192 -0.0040 -0.0240 521 PHE A CZ 3893 N N . GLU A 481 ? 0.1869 0.2161 0.1860 0.0186 -0.0006 -0.0171 522 GLU A N 3894 C CA . GLU A 481 ? 0.2014 0.2326 0.2007 0.0155 -0.0001 -0.0172 522 GLU A CA 3895 C C . GLU A 481 ? 0.1950 0.2247 0.1899 0.0154 -0.0005 -0.0154 522 GLU A C 3896 O O . GLU A 481 ? 0.1978 0.2276 0.1918 0.0149 -0.0021 -0.0152 522 GLU A O 3897 C CB . GLU A 481 ? 0.2128 0.2456 0.2134 0.0126 0.0027 -0.0182 522 GLU A CB 3898 C CG . GLU A 481 ? 0.2260 0.2602 0.2257 0.0096 0.0034 -0.0180 522 GLU A CG 3899 C CD . GLU A 481 ? 0.3531 0.3877 0.3507 0.0075 0.0058 -0.0186 522 GLU A CD 3900 O OE1 . GLU A 481 ? 0.4178 0.4512 0.4128 0.0075 0.0055 -0.0182 522 GLU A OE1 3901 O OE2 . GLU A 481 ? 0.3518 0.3878 0.3504 0.0060 0.0079 -0.0198 522 GLU A OE2 3902 N N . VAL A 482 ? 0.1803 0.2088 0.1734 0.0158 0.0010 -0.0143 523 VAL A N 3903 C CA . VAL A 482 ? 0.1980 0.2260 0.1885 0.0157 0.0008 -0.0128 523 VAL A CA 3904 C C . VAL A 482 ? 0.2009 0.2270 0.1885 0.0187 -0.0009 -0.0120 523 VAL A C 3905 O O . VAL A 482 ? 0.2072 0.2332 0.1934 0.0186 -0.0020 -0.0116 523 VAL A O 3906 C CB . VAL A 482 ? 0.2115 0.2391 0.2028 0.0154 0.0030 -0.0119 523 VAL A CB 3907 C CG1 . VAL A 482 ? 0.2049 0.2297 0.1954 0.0183 0.0044 -0.0106 523 VAL A CG1 3908 C CG2 . VAL A 482 ? 0.2052 0.2334 0.1961 0.0147 0.0028 -0.0108 523 VAL A CG2 3909 N N . PHE A 483 ? 0.1869 0.2110 0.1730 0.0218 -0.0015 -0.0120 524 PHE A N 3910 C CA . PHE A 483 ? 0.1908 0.2123 0.1724 0.0253 -0.0034 -0.0116 524 PHE A CA 3911 C C . PHE A 483 ? 0.1950 0.2171 0.1776 0.0250 -0.0068 -0.0133 524 PHE A C 3912 O O . PHE A 483 ? 0.2122 0.2328 0.1919 0.0263 -0.0082 -0.0132 524 PHE A O 3913 C CB . PHE A 483 ? 0.1958 0.2144 0.1745 0.0290 -0.0037 -0.0112 524 PHE A CB 3914 C CG . PHE A 483 ? 0.2138 0.2309 0.1918 0.0294 0.0000 -0.0090 524 PHE A CG 3915 C CD1 . PHE A 483 ? 0.2329 0.2481 0.2072 0.0310 0.0026 -0.0067 524 PHE A CD1 3916 C CD2 . PHE A 483 ? 0.2192 0.2369 0.2011 0.0279 0.0014 -0.0093 524 PHE A CD2 3917 C CE1 . PHE A 483 ? 0.2780 0.2919 0.2533 0.0309 0.0067 -0.0044 524 PHE A CE1 3918 C CE2 . PHE A 483 ? 0.2039 0.2199 0.1863 0.0279 0.0049 -0.0073 524 PHE A CE2 3919 C CZ . PHE A 483 ? 0.2499 0.2640 0.2294 0.0292 0.0076 -0.0047 524 PHE A CZ 3920 N N . PHE A 484 ? 0.1964 0.2205 0.1837 0.0231 -0.0079 -0.0149 525 PHE A N 3921 C CA . PHE A 484 ? 0.1912 0.2158 0.1813 0.0226 -0.0111 -0.0166 525 PHE A CA 3922 C C . PHE A 484 ? 0.1946 0.2207 0.1868 0.0188 -0.0101 -0.0161 525 PHE A C 3923 O O . PHE A 484 ? 0.1953 0.2199 0.1862 0.0191 -0.0119 -0.0160 525 PHE A O 3924 C CB . PHE A 484 ? 0.1990 0.2255 0.1950 0.0225 -0.0124 -0.0186 525 PHE A CB 3925 C CG . PHE A 484 ? 0.1905 0.2174 0.1909 0.0222 -0.0160 -0.0205 525 PHE A CG 3926 C CD1 . PHE A 484 ? 0.2010 0.2247 0.1977 0.0256 -0.0203 -0.0217 525 PHE A CD1 3927 C CD2 . PHE A 484 ? 0.2250 0.2550 0.2331 0.0186 -0.0151 -0.0214 525 PHE A CD2 3928 C CE1 . PHE A 484 ? 0.2400 0.2637 0.2420 0.0254 -0.0244 -0.0241 525 PHE A CE1 3929 C CE2 . PHE A 484 ? 0.2494 0.2797 0.2636 0.0180 -0.0185 -0.0232 525 PHE A CE2 3930 C CZ . PHE A 484 ? 0.2351 0.2623 0.2466 0.0213 -0.0235 -0.0248 525 PHE A CZ 3931 N N . GLN A 485 ? 0.1920 0.2205 0.1866 0.0157 -0.0072 -0.0157 526 GLN A N 3932 C CA . GLN A 485 ? 0.1937 0.2230 0.1891 0.0124 -0.0063 -0.0149 526 GLN A CA 3933 C C . GLN A 485 ? 0.1861 0.2141 0.1771 0.0121 -0.0061 -0.0132 526 GLN A C 3934 O O . GLN A 485 ? 0.2065 0.2337 0.1970 0.0107 -0.0068 -0.0124 526 GLN A O 3935 C CB A GLN A 485 ? 0.2025 0.2342 0.2001 0.0097 -0.0031 -0.0152 526 GLN A CB 3936 C CB B GLN A 485 ? 0.2067 0.2384 0.2049 0.0096 -0.0034 -0.0153 526 GLN A CB 3937 C CG A GLN A 485 ? 0.1873 0.2210 0.1907 0.0098 -0.0026 -0.0171 526 GLN A CG 3938 C CG B GLN A 485 ? 0.2446 0.2781 0.2494 0.0088 -0.0035 -0.0168 526 GLN A CG 3939 C CD A GLN A 485 ? 0.1634 0.1978 0.1724 0.0090 -0.0042 -0.0179 526 GLN A CD 3940 C CD B GLN A 485 ? 0.2488 0.2835 0.2569 0.0108 -0.0037 -0.0185 526 GLN A CD 3941 O OE1 A GLN A 485 ? 0.1767 0.2096 0.1847 0.0081 -0.0054 -0.0169 526 GLN A OE1 3942 O OE1 B GLN A 485 ? 0.2807 0.3143 0.2855 0.0130 -0.0039 -0.0183 526 GLN A OE1 3943 N NE2 A GLN A 485 ? 0.1943 0.2311 0.2102 0.0092 -0.0043 -0.0197 526 GLN A NE2 3944 N NE2 B GLN A 485 ? 0.2417 0.2789 0.2571 0.0101 -0.0036 -0.0201 526 GLN A NE2 3945 N N . ARG A 486 ? 0.1745 0.2025 0.1633 0.0135 -0.0050 -0.0126 527 ARG A N 3946 C CA . ARG A 486 ? 0.1831 0.2106 0.1697 0.0135 -0.0050 -0.0113 527 ARG A CA 3947 C C . ARG A 486 ? 0.2061 0.2318 0.1908 0.0165 -0.0063 -0.0110 527 ARG A C 3948 O O . ARG A 486 ? 0.1969 0.2218 0.1808 0.0166 -0.0076 -0.0104 527 ARG A O 3949 C CB . ARG A 486 ? 0.1937 0.2225 0.1806 0.0128 -0.0029 -0.0110 527 ARG A CB 3950 C CG . ARG A 486 ? 0.1811 0.2103 0.1675 0.0119 -0.0036 -0.0101 527 ARG A CG 3951 C CD . ARG A 486 ? 0.2164 0.2468 0.2049 0.0117 -0.0022 -0.0099 527 ARG A CD 3952 N NE . ARG A 486 ? 0.2042 0.2355 0.1934 0.0096 -0.0012 -0.0112 527 ARG A NE 3953 C CZ . ARG A 486 ? 0.2011 0.2334 0.1926 0.0086 -0.0010 -0.0117 527 ARG A CZ 3954 N NH1 . ARG A 486 ? 0.2188 0.2520 0.2129 0.0092 -0.0016 -0.0109 527 ARG A NH1 3955 N NH2 . ARG A 486 ? 0.2044 0.2369 0.1961 0.0070 -0.0003 -0.0133 527 ARG A NH2 3956 N N . LEU A 487 ? 0.1888 0.2133 0.1720 0.0194 -0.0060 -0.0112 528 LEU A N 3957 C CA . LEU A 487 ? 0.1928 0.2151 0.1726 0.0229 -0.0064 -0.0108 528 LEU A CA 3958 C C . LEU A 487 ? 0.1998 0.2196 0.1775 0.0253 -0.0096 -0.0124 528 LEU A C 3959 O O . LEU A 487 ? 0.2329 0.2506 0.2071 0.0282 -0.0102 -0.0124 528 LEU A O 3960 C CB . LEU A 487 ? 0.1945 0.2162 0.1725 0.0252 -0.0036 -0.0097 528 LEU A CB 3961 C CG . LEU A 487 ? 0.2124 0.2363 0.1938 0.0229 -0.0006 -0.0084 528 LEU A CG 3962 C CD1 . LEU A 487 ? 0.2433 0.2658 0.2236 0.0251 0.0027 -0.0069 528 LEU A CD1 3963 C CD2 . LEU A 487 ? 0.2500 0.2754 0.2331 0.0221 -0.0007 -0.0078 528 LEU A CD2 3964 N N . GLY A 488 ? 0.1918 0.2118 0.1718 0.0244 -0.0116 -0.0139 529 GLY A N 3965 C CA . GLY A 488 ? 0.1947 0.2125 0.1743 0.0264 -0.0155 -0.0159 529 GLY A CA 3966 C C . GLY A 488 ? 0.1932 0.2081 0.1671 0.0313 -0.0167 -0.0167 529 GLY A C 3967 O O . GLY A 488 ? 0.2013 0.2131 0.1714 0.0343 -0.0196 -0.0182 529 GLY A O 3968 N N . ILE A 489 ? 0.1948 0.2101 0.1676 0.0322 -0.0148 -0.0158 530 ILE A N 3969 C CA . ILE A 489 ? 0.1928 0.2046 0.1592 0.0371 -0.0161 -0.0162 530 ILE A CA 3970 C C . ILE A 489 ? 0.1997 0.2120 0.1698 0.0374 -0.0199 -0.0185 530 ILE A C 3971 O O . ILE A 489 ? 0.2117 0.2273 0.1882 0.0343 -0.0186 -0.0183 530 ILE A O 3972 C CB . ILE A 489 ? 0.1944 0.2057 0.1578 0.0380 -0.0114 -0.0133 530 ILE A CB 3973 C CG1 . ILE A 489 ? 0.2264 0.2376 0.1878 0.0380 -0.0079 -0.0114 530 ILE A CG1 3974 C CG2 . ILE A 489 ? 0.2227 0.2295 0.1784 0.0433 -0.0124 -0.0130 530 ILE A CG2 3975 C CD1 . ILE A 489 ? 0.2312 0.2431 0.1933 0.0373 -0.0026 -0.0085 530 ILE A CD1 3976 N N . ALA A 490 ? 0.2147 0.2239 0.1811 0.0412 -0.0247 -0.0208 531 ALA A N 3977 C CA . ALA A 490 ? 0.2109 0.2206 0.1816 0.0421 -0.0294 -0.0235 531 ALA A CA 3978 C C . ALA A 490 ? 0.2345 0.2453 0.2063 0.0425 -0.0273 -0.0220 531 ALA A C 3979 O O . ALA A 490 ? 0.2341 0.2418 0.1983 0.0455 -0.0249 -0.0197 531 ALA A O 3980 C CB . ALA A 490 ? 0.2350 0.2398 0.1981 0.0478 -0.0349 -0.0259 531 ALA A CB 3981 N N . SER A 491 ? 0.1995 0.2144 0.1809 0.0395 -0.0276 -0.0232 532 SER A N 3982 C CA . SER A 491 ? 0.2122 0.2282 0.1956 0.0394 -0.0251 -0.0220 532 SER A CA 3983 C C . SER A 491 ? 0.2263 0.2443 0.2172 0.0404 -0.0294 -0.0248 532 SER A C 3984 O O . SER A 491 ? 0.2315 0.2520 0.2297 0.0389 -0.0328 -0.0275 532 SER A O 3985 C CB . SER A 491 ? 0.2164 0.2361 0.2047 0.0344 -0.0196 -0.0204 532 SER A CB 3986 O OG . SER A 491 ? 0.2185 0.2366 0.2009 0.0339 -0.0161 -0.0179 532 SER A OG 3987 N N . GLY A 492 ? 0.2161 0.2330 0.2061 0.0429 -0.0292 -0.0241 533 GLY A N 3988 C CA . GLY A 492 ? 0.2236 0.2432 0.2226 0.0438 -0.0330 -0.0269 533 GLY A CA 3989 C C . GLY A 492 ? 0.2386 0.2583 0.2390 0.0444 -0.0300 -0.0255 533 GLY A C 3990 O O . GLY A 492 ? 0.2456 0.2620 0.2388 0.0450 -0.0260 -0.0223 533 GLY A O 3991 N N . ARG A 493 ? 0.2292 0.2524 0.2397 0.0445 -0.0323 -0.0279 534 ARG A N 3992 C CA . ARG A 493 ? 0.2387 0.2622 0.2524 0.0454 -0.0302 -0.0274 534 ARG A CA 3993 C C . ARG A 493 ? 0.2361 0.2621 0.2590 0.0482 -0.0359 -0.0307 534 ARG A C 3994 O O . ARG A 493 ? 0.2270 0.2566 0.2577 0.0472 -0.0396 -0.0337 534 ARG A O 3995 C CB . ARG A 493 ? 0.2431 0.2707 0.2627 0.0402 -0.0237 -0.0270 534 ARG A CB 3996 C CG . ARG A 493 ? 0.2379 0.2719 0.2687 0.0361 -0.0230 -0.0295 534 ARG A CG 3997 C CD . ARG A 493 ? 0.2401 0.2771 0.2735 0.0310 -0.0161 -0.0288 534 ARG A CD 3998 N NE . ARG A 493 ? 0.2693 0.3056 0.3029 0.0316 -0.0128 -0.0284 534 ARG A NE 3999 C CZ . ARG A 493 ? 0.2785 0.3176 0.3157 0.0284 -0.0078 -0.0290 534 ARG A CZ 4000 N NH1 . ARG A 493 ? 0.2693 0.3067 0.3061 0.0295 -0.0056 -0.0290 534 ARG A NH1 4001 N NH2 . ARG A 493 ? 0.2835 0.3261 0.3236 0.0243 -0.0049 -0.0295 534 ARG A NH2 4002 N N . ALA A 494 ? 0.2367 0.2603 0.2590 0.0518 -0.0368 -0.0302 535 ALA A N 4003 C CA . ALA A 494 ? 0.2311 0.2570 0.2626 0.0551 -0.0426 -0.0334 535 ALA A CA 4004 C C . ALA A 494 ? 0.2539 0.2788 0.2879 0.0569 -0.0404 -0.0325 535 ALA A C 4005 O O . ALA A 494 ? 0.2469 0.2661 0.2710 0.0582 -0.0372 -0.0290 535 ALA A O 4006 C CB . ALA A 494 ? 0.2400 0.2606 0.2630 0.0611 -0.0506 -0.0339 535 ALA A CB 4007 N N . ARG A 495 ? 0.2312 0.2618 0.2794 0.0567 -0.0416 -0.0357 536 ARG A N 4008 C CA . ARG A 495 ? 0.2371 0.2668 0.2891 0.0591 -0.0403 -0.0355 536 ARG A CA 4009 C C . ARG A 495 ? 0.2276 0.2626 0.2944 0.0615 -0.0454 -0.0396 536 ARG A C 4010 O O . ARG A 495 ? 0.2238 0.2639 0.2993 0.0604 -0.0490 -0.0426 536 ARG A O 4011 C CB . ARG A 495 ? 0.2408 0.2728 0.2958 0.0543 -0.0318 -0.0348 536 ARG A CB 4012 C CG . ARG A 495 ? 0.2539 0.2944 0.3215 0.0493 -0.0284 -0.0377 536 ARG A CG 4013 C CD . ARG A 495 ? 0.2989 0.3405 0.3676 0.0459 -0.0205 -0.0373 536 ARG A CD 4014 N NE . ARG A 495 ? 0.3197 0.3569 0.3761 0.0432 -0.0167 -0.0341 536 ARG A NE 4015 C CZ . ARG A 495 ? 0.3038 0.3416 0.3591 0.0395 -0.0105 -0.0338 536 ARG A CZ 4016 N NH1 . ARG A 495 ? 0.3025 0.3447 0.3666 0.0380 -0.0068 -0.0364 536 ARG A NH1 4017 N NH2 . ARG A 495 ? 0.2981 0.3320 0.3432 0.0376 -0.0081 -0.0310 536 ARG A NH2 4018 N N . TYR A 496 ? 0.2385 0.2723 0.3091 0.0648 -0.0458 -0.0398 537 TYR A N 4019 C CA . TYR A 496 ? 0.2432 0.2833 0.3305 0.0668 -0.0497 -0.0440 537 TYR A CA 4020 C C . TYR A 496 ? 0.2481 0.2956 0.3480 0.0617 -0.0419 -0.0459 537 TYR A C 4021 O O . TYR A 496 ? 0.2468 0.2922 0.3412 0.0591 -0.0349 -0.0439 537 TYR A O 4022 C CB . TYR A 496 ? 0.2402 0.2755 0.3267 0.0738 -0.0551 -0.0438 537 TYR A CB 4023 C CG . TYR A 496 ? 0.2590 0.2950 0.3496 0.0787 -0.0654 -0.0465 537 TYR A CG 4024 C CD1 . TYR A 496 ? 0.2804 0.3109 0.3578 0.0811 -0.0710 -0.0453 537 TYR A CD1 4025 C CD2 . TYR A 496 ? 0.2419 0.2845 0.3504 0.0810 -0.0699 -0.0509 537 TYR A CD2 4026 C CE1 . TYR A 496 ? 0.2876 0.3183 0.3681 0.0860 -0.0816 -0.0484 537 TYR A CE1 4027 C CE2 . TYR A 496 ? 0.2811 0.3246 0.3945 0.0857 -0.0807 -0.0540 537 TYR A CE2 4028 C CZ . TYR A 496 ? 0.2764 0.3136 0.3750 0.0882 -0.0867 -0.0528 537 TYR A CZ 4029 O OH . TYR A 496 ? 0.3221 0.3596 0.4245 0.0929 -0.0979 -0.0564 537 TYR A OH 4030 N N . THR A 497 ? 0.2458 0.3018 0.3625 0.0603 -0.0432 -0.0498 538 THR A N 4031 C CA . THR A 497 ? 0.2399 0.3033 0.3685 0.0554 -0.0352 -0.0516 538 THR A CA 4032 C C . THR A 497 ? 0.2533 0.3241 0.4016 0.0575 -0.0367 -0.0558 538 THR A C 4033 O O . THR A 497 ? 0.2567 0.3270 0.4100 0.0626 -0.0446 -0.0574 538 THR A O 4034 C CB . THR A 497 ? 0.2519 0.3194 0.3821 0.0494 -0.0319 -0.0515 538 THR A CB 4035 O OG1 . THR A 497 ? 0.2663 0.3387 0.4026 0.0448 -0.0227 -0.0520 538 THR A OG1 4036 C CG2 . THR A 497 ? 0.2355 0.3080 0.3780 0.0498 -0.0385 -0.0545 538 THR A CG2 4037 N N . LYS A 498 ? 0.2618 0.3388 0.4200 0.0535 -0.0285 -0.0573 539 LYS A N 4038 C CA . LYS A 498 ? 0.2958 0.3813 0.4746 0.0545 -0.0275 -0.0613 539 LYS A CA 4039 C C . LYS A 498 ? 0.3200 0.4136 0.5142 0.0515 -0.0286 -0.0637 539 LYS A C 4040 O O . LYS A 498 ? 0.3236 0.4160 0.5123 0.0485 -0.0301 -0.0623 539 LYS A O 4041 C CB . LYS A 498 ? 0.3045 0.3920 0.4853 0.0522 -0.0172 -0.0618 539 LYS A CB 4042 C CG A LYS A 498 ? 0.3167 0.4076 0.4959 0.0456 -0.0083 -0.0609 539 LYS A CG 4043 C CD A LYS A 498 ? 0.3525 0.4356 0.5111 0.0431 -0.0057 -0.0570 539 LYS A CD 4044 C CE A LYS A 498 ? 0.3980 0.4837 0.5539 0.0371 0.0030 -0.0561 539 LYS A CE 4045 N NZ A LYS A 498 ? 0.3743 0.4574 0.5223 0.0362 0.0104 -0.0560 539 LYS A NZ 4046 N N . ASN A 499 ? 0.3518 0.4537 0.5668 0.0526 -0.0282 -0.0675 540 ASN A N 4047 C CA . ASN A 499 ? 0.3914 0.5025 0.6251 0.0489 -0.0267 -0.0699 540 ASN A CA 4048 C C . ASN A 499 ? 0.4074 0.5235 0.6468 0.0445 -0.0140 -0.0699 540 ASN A C 4049 O O . ASN A 499 ? 0.4026 0.5249 0.6574 0.0462 -0.0106 -0.0728 540 ASN A O 4050 C CB . ASN A 499 ? 0.3909 0.5083 0.6457 0.0534 -0.0342 -0.0744 540 ASN A CB 4051 C CG . ASN A 499 ? 0.4203 0.5473 0.6968 0.0497 -0.0342 -0.0772 540 ASN A CG 4052 O OD1 . ASN A 499 ? 0.4483 0.5760 0.7228 0.0440 -0.0296 -0.0754 540 ASN A OD1 4053 N ND2 . ASN A 499 ? 0.4531 0.5874 0.7516 0.0530 -0.0395 -0.0815 540 ASN A ND2 4054 N N . TRP A 500 ? 0.4275 0.5406 0.6538 0.0395 -0.0070 -0.0667 541 TRP A N 4055 C CA . TRP A 500 ? 0.4540 0.5709 0.6828 0.0354 0.0051 -0.0664 541 TRP A CA 4056 C C . TRP A 500 ? 0.4714 0.5863 0.6903 0.0296 0.0095 -0.0630 541 TRP A C 4057 O O . TRP A 500 ? 0.4671 0.5758 0.6676 0.0280 0.0134 -0.0602 541 TRP A O 4058 C CB . TRP A 500 ? 0.4593 0.5717 0.6766 0.0376 0.0101 -0.0661 541 TRP A CB 4059 C CG . TRP A 500 ? 0.4664 0.5837 0.6901 0.0355 0.0216 -0.0675 541 TRP A CG 4060 C CD1 . TRP A 500 ? 0.4707 0.5950 0.7055 0.0313 0.0293 -0.0678 541 TRP A CD1 4061 C CD2 . TRP A 500 ? 0.4804 0.5952 0.6983 0.0378 0.0270 -0.0688 541 TRP A CD2 4062 N NE1 . TRP A 500 ? 0.4916 0.6179 0.7271 0.0311 0.0394 -0.0691 541 TRP A NE1 4063 C CE2 . TRP A 500 ? 0.4742 0.5948 0.6994 0.0351 0.0378 -0.0701 541 TRP A CE2 4064 C CE3 . TRP A 500 ? 0.4911 0.5989 0.6983 0.0418 0.0238 -0.0689 541 TRP A CE3 4065 C CZ2 . TRP A 500 ? 0.4759 0.5955 0.6976 0.0367 0.0451 -0.0721 541 TRP A CZ2 4066 C CZ3 . TRP A 500 ? 0.4998 0.6067 0.7049 0.0430 0.0308 -0.0709 541 TRP A CZ3 4067 C CH2 . TRP A 500 ? 0.4577 0.5705 0.6697 0.0406 0.0412 -0.0727 541 TRP A CH2 4068 N N . GLU A 501 ? 0.4884 0.6084 0.7202 0.0266 0.0085 -0.0635 542 GLU A N 4069 C CA . GLU A 501 ? 0.5064 0.6234 0.7294 0.0217 0.0100 -0.0603 542 GLU A CA 4070 C C . GLU A 501 ? 0.5002 0.6153 0.7118 0.0176 0.0209 -0.0573 542 GLU A C 4071 O O . GLU A 501 ? 0.5091 0.6177 0.7030 0.0157 0.0210 -0.0540 542 GLU A O 4072 C CB . GLU A 501 ? 0.5236 0.6466 0.7653 0.0190 0.0073 -0.0616 542 GLU A CB 4073 C CG . GLU A 501 ? 0.5920 0.7120 0.8333 0.0215 -0.0053 -0.0628 542 GLU A CG 4074 C CD . GLU A 501 ? 0.6705 0.7821 0.8912 0.0200 -0.0078 -0.0594 542 GLU A CD 4075 O OE1 . GLU A 501 ? 0.7154 0.8226 0.9201 0.0179 -0.0012 -0.0560 542 GLU A OE1 4076 O OE2 . GLU A 501 ? 0.7054 0.8147 0.9261 0.0210 -0.0168 -0.0603 542 GLU A OE2 4077 N N . THR A 502 ? 0.4937 0.6144 0.7150 0.0166 0.0300 -0.0585 543 THR A N 4078 C CA . THR A 502 ? 0.4845 0.6034 0.6949 0.0133 0.0408 -0.0561 543 THR A CA 4079 C C . THR A 502 ? 0.4644 0.5758 0.6538 0.0154 0.0413 -0.0552 543 THR A C 4080 O O . THR A 502 ? 0.4768 0.5850 0.6530 0.0130 0.0484 -0.0531 543 THR A O 4081 C CB . THR A 502 ? 0.4908 0.6174 0.7167 0.0126 0.0509 -0.0580 543 THR A CB 4082 O OG1 . THR A 502 ? 0.4992 0.6291 0.7346 0.0175 0.0488 -0.0620 543 THR A OG1 4083 C CG2 . THR A 502 ? 0.4983 0.6320 0.7444 0.0090 0.0528 -0.0579 543 THR A CG2 4084 N N . ASN A 503 ? 0.4338 0.5422 0.6201 0.0198 0.0337 -0.0566 544 ASN A N 4085 C CA A ASN A 503 ? 0.4170 0.5181 0.5856 0.0218 0.0335 -0.0559 544 ASN A CA 4086 C CA B ASN A 503 ? 0.4216 0.5228 0.5901 0.0216 0.0336 -0.0558 544 ASN A CA 4087 C C . ASN A 503 ? 0.4048 0.4988 0.5588 0.0221 0.0260 -0.0532 544 ASN A C 4088 O O . ASN A 503 ? 0.4031 0.4912 0.5450 0.0243 0.0241 -0.0527 544 ASN A O 4089 C CB A ASN A 503 ? 0.4171 0.5190 0.5919 0.0267 0.0320 -0.0592 544 ASN A CB 4090 C CB B ASN A 503 ? 0.4274 0.5294 0.6017 0.0264 0.0329 -0.0591 544 ASN A CB 4091 C CG A ASN A 503 ? 0.4171 0.5188 0.5879 0.0268 0.0409 -0.0608 544 ASN A CG 4092 C CG B ASN A 503 ? 0.4427 0.5494 0.6240 0.0260 0.0427 -0.0615 544 ASN A CG 4093 O OD1 A ASN A 503 ? 0.3972 0.5021 0.5693 0.0238 0.0494 -0.0606 544 ASN A OD1 4094 O OD1 B ASN A 503 ? 0.4796 0.5931 0.6739 0.0237 0.0480 -0.0620 544 ASN A OD1 4095 N ND2 A ASN A 503 ? 0.3876 0.4849 0.5529 0.0305 0.0390 -0.0623 544 ASN A ND2 4096 N ND2 B ASN A 503 ? 0.4305 0.5332 0.6032 0.0283 0.0454 -0.0629 544 ASN A ND2 4097 N N . LYS A 504 ? 0.3743 0.4686 0.5296 0.0199 0.0221 -0.0515 545 LYS A N 4098 C CA . LYS A 504 ? 0.3608 0.4487 0.5036 0.0209 0.0147 -0.0494 545 LYS A CA 4099 C C . LYS A 504 ? 0.3372 0.4185 0.4608 0.0193 0.0173 -0.0464 545 LYS A C 4100 O O . LYS A 504 ? 0.3297 0.4055 0.4428 0.0210 0.0120 -0.0449 545 LYS A O 4101 C CB . LYS A 504 ? 0.3749 0.4642 0.5234 0.0193 0.0097 -0.0488 545 LYS A CB 4102 C CG . LYS A 504 ? 0.4200 0.5095 0.5656 0.0141 0.0149 -0.0464 545 LYS A CG 4103 C CD . LYS A 504 ? 0.4863 0.5773 0.6403 0.0126 0.0098 -0.0464 545 LYS A CD 4104 C CE . LYS A 504 ? 0.5281 0.6209 0.6850 0.0072 0.0167 -0.0442 545 LYS A CE 4105 N NZ . LYS A 504 ? 0.5981 0.6894 0.7571 0.0052 0.0117 -0.0433 545 LYS A NZ 4106 N N . PHE A 505 ? 0.2995 0.3812 0.4186 0.0162 0.0251 -0.0457 546 PHE A N 4107 C CA . PHE A 505 ? 0.2812 0.3568 0.3829 0.0149 0.0271 -0.0435 546 PHE A CA 4108 C C . PHE A 505 ? 0.2903 0.3647 0.3879 0.0162 0.0319 -0.0454 546 PHE A C 4109 O O . PHE A 505 ? 0.2975 0.3677 0.3826 0.0150 0.0340 -0.0444 546 PHE A O 4110 C CB . PHE A 505 ? 0.2863 0.3614 0.3819 0.0106 0.0311 -0.0409 546 PHE A CB 4111 C CG . PHE A 505 ? 0.2831 0.3579 0.3805 0.0092 0.0261 -0.0389 546 PHE A CG 4112 C CD1 . PHE A 505 ? 0.3196 0.3901 0.4101 0.0110 0.0191 -0.0379 546 PHE A CD1 4113 C CD2 . PHE A 505 ? 0.3375 0.4159 0.4436 0.0060 0.0290 -0.0382 546 PHE A CD2 4114 C CE1 . PHE A 505 ? 0.3252 0.3950 0.4168 0.0101 0.0145 -0.0367 546 PHE A CE1 4115 C CE2 . PHE A 505 ? 0.3132 0.3907 0.4213 0.0047 0.0241 -0.0368 546 PHE A CE2 4116 C CZ . PHE A 505 ? 0.3269 0.4001 0.4275 0.0070 0.0166 -0.0363 546 PHE A CZ 4117 N N . SER A 506 ? 0.2841 0.3622 0.3929 0.0188 0.0332 -0.0485 547 SER A N 4118 C CA . SER A 506 ? 0.2871 0.3639 0.3921 0.0199 0.0384 -0.0507 547 SER A CA 4119 C C . SER A 506 ? 0.2875 0.3591 0.3875 0.0233 0.0340 -0.0515 547 SER A C 4120 O O . SER A 506 ? 0.3155 0.3837 0.4084 0.0237 0.0370 -0.0529 547 SER A O 4121 C CB . SER A 506 ? 0.2832 0.3667 0.4025 0.0207 0.0441 -0.0538 547 SER A CB 4122 O OG . SER A 506 ? 0.3000 0.3877 0.4234 0.0171 0.0492 -0.0524 547 SER A OG 4123 N N . GLY A 507 ? 0.2730 0.3431 0.3756 0.0258 0.0267 -0.0505 548 GLY A N 4124 C CA . GLY A 507 ? 0.2855 0.3505 0.3849 0.0294 0.0229 -0.0509 548 GLY A CA 4125 C C . GLY A 507 ? 0.2857 0.3539 0.3983 0.0334 0.0224 -0.0540 548 GLY A C 4126 O O . GLY A 507 ? 0.3119 0.3863 0.4351 0.0329 0.0269 -0.0565 548 GLY A O 4127 N N . TYR A 508 ? 0.2602 0.3241 0.3725 0.0374 0.0168 -0.0536 549 TYR A N 4128 C CA . TYR A 508 ? 0.2408 0.3062 0.3643 0.0419 0.0154 -0.0564 549 TYR A CA 4129 C C . TYR A 508 ? 0.2281 0.2923 0.3508 0.0420 0.0218 -0.0592 549 TYR A C 4130 O O . TYR A 508 ? 0.2282 0.2889 0.3397 0.0390 0.0256 -0.0587 549 TYR A O 4131 C CB . TYR A 508 ? 0.2382 0.2974 0.3581 0.0462 0.0078 -0.0544 549 TYR A CB 4132 C CG . TYR A 508 ? 0.2538 0.3046 0.3584 0.0452 0.0075 -0.0512 549 TYR A CG 4133 C CD1 . TYR A 508 ? 0.2493 0.2942 0.3500 0.0467 0.0092 -0.0516 549 TYR A CD1 4134 C CD2 . TYR A 508 ? 0.2621 0.3109 0.3571 0.0426 0.0057 -0.0478 549 TYR A CD2 4135 C CE1 . TYR A 508 ? 0.2580 0.2956 0.3462 0.0452 0.0092 -0.0486 549 TYR A CE1 4136 C CE2 . TYR A 508 ? 0.2636 0.3057 0.3464 0.0415 0.0060 -0.0450 549 TYR A CE2 4137 C CZ . TYR A 508 ? 0.2411 0.2778 0.3210 0.0426 0.0077 -0.0453 549 TYR A CZ 4138 O OH . TYR A 508 ? 0.2787 0.3092 0.3481 0.0410 0.0082 -0.0425 549 TYR A OH 4139 N N . PRO A 509 ? 0.2230 0.2900 0.3574 0.0455 0.0227 -0.0626 550 PRO A N 4140 C CA . PRO A 509 ? 0.2214 0.2883 0.3555 0.0453 0.0298 -0.0661 550 PRO A CA 4141 C C . PRO A 509 ? 0.2271 0.2850 0.3479 0.0451 0.0300 -0.0655 550 PRO A C 4142 O O . PRO A 509 ? 0.2375 0.2943 0.3519 0.0430 0.0355 -0.0674 550 PRO A O 4143 C CB . PRO A 509 ? 0.2271 0.2977 0.3769 0.0501 0.0292 -0.0696 550 PRO A CB 4144 C CG . PRO A 509 ? 0.2255 0.3032 0.3870 0.0503 0.0252 -0.0688 550 PRO A CG 4145 C CD . PRO A 509 ? 0.2267 0.2993 0.3769 0.0490 0.0187 -0.0643 550 PRO A CD 4146 N N . LEU A 510 ? 0.2109 0.2622 0.3274 0.0473 0.0241 -0.0630 551 LEU A N 4147 C CA . LEU A 510 ? 0.2237 0.2663 0.3302 0.0472 0.0243 -0.0625 551 LEU A CA 4148 C C . LEU A 510 ? 0.2186 0.2575 0.3123 0.0433 0.0233 -0.0588 551 LEU A C 4149 O O . LEU A 510 ? 0.2429 0.2745 0.3294 0.0430 0.0225 -0.0578 551 LEU A O 4150 C CB . LEU A 510 ? 0.2091 0.2459 0.3189 0.0520 0.0195 -0.0617 551 LEU A CB 4151 C CG . LEU A 510 ? 0.2229 0.2632 0.3459 0.0561 0.0209 -0.0661 551 LEU A CG 4152 C CD1 . LEU A 510 ? 0.2636 0.2979 0.3897 0.0613 0.0155 -0.0648 551 LEU A CD1 4153 C CD2 . LEU A 510 ? 0.2232 0.2632 0.3453 0.0551 0.0276 -0.0707 551 LEU A CD2 4154 N N . TYR A 511 ? 0.2141 0.2577 0.3060 0.0403 0.0236 -0.0571 552 TYR A N 4155 C CA . TYR A 511 ? 0.2134 0.2542 0.2938 0.0367 0.0227 -0.0537 552 TYR A CA 4156 C C . TYR A 511 ? 0.2004 0.2369 0.2722 0.0343 0.0259 -0.0550 552 TYR A C 4157 O O . TYR A 511 ? 0.2266 0.2654 0.2978 0.0329 0.0306 -0.0583 552 TYR A O 4158 C CB . TYR A 511 ? 0.1993 0.2466 0.2812 0.0340 0.0237 -0.0528 552 TYR A CB 4159 C CG . TYR A 511 ? 0.2046 0.2505 0.2759 0.0300 0.0238 -0.0500 552 TYR A CG 4160 C CD1 . TYR A 511 ? 0.2205 0.2622 0.2855 0.0301 0.0193 -0.0462 552 TYR A CD1 4161 C CD2 . TYR A 511 ? 0.2308 0.2797 0.2987 0.0267 0.0285 -0.0509 552 TYR A CD2 4162 C CE1 . TYR A 511 ? 0.2027 0.2437 0.2592 0.0266 0.0195 -0.0439 552 TYR A CE1 4163 C CE2 . TYR A 511 ? 0.2209 0.2686 0.2797 0.0234 0.0282 -0.0483 552 TYR A CE2 4164 C CZ . TYR A 511 ? 0.2109 0.2548 0.2646 0.0234 0.0236 -0.0451 552 TYR A CZ 4165 O OH . TYR A 511 ? 0.2315 0.2744 0.2770 0.0204 0.0233 -0.0427 552 TYR A OH 4166 N N . HIS A 512 ? 0.2240 0.2542 0.2891 0.0338 0.0233 -0.0524 553 HIS A N 4167 C CA . HIS A 512 ? 0.2228 0.2487 0.2802 0.0312 0.0250 -0.0534 553 HIS A CA 4168 C C . HIS A 512 ? 0.2359 0.2589 0.2956 0.0326 0.0275 -0.0581 553 HIS A C 4169 O O . HIS A 512 ? 0.2294 0.2499 0.2832 0.0305 0.0293 -0.0606 553 HIS A O 4170 C CB . HIS A 512 ? 0.2205 0.2497 0.2711 0.0273 0.0270 -0.0532 553 HIS A CB 4171 C CG . HIS A 512 ? 0.1999 0.2295 0.2460 0.0254 0.0241 -0.0487 553 HIS A CG 4172 N ND1 . HIS A 512 ? 0.1838 0.2153 0.2234 0.0221 0.0252 -0.0479 553 HIS A ND1 4173 C CD2 . HIS A 512 ? 0.2129 0.2409 0.2594 0.0267 0.0204 -0.0449 553 HIS A CD2 4174 C CE1 . HIS A 512 ? 0.2026 0.2339 0.2396 0.0212 0.0223 -0.0440 553 HIS A CE1 4175 N NE2 . HIS A 512 ? 0.1952 0.2242 0.2357 0.0240 0.0195 -0.0421 553 HIS A NE2 4176 N N . SER A 513 ? 0.2318 0.2547 0.2998 0.0364 0.0271 -0.0595 554 SER A N 4177 C CA . SER A 513 ? 0.2135 0.2328 0.2848 0.0386 0.0290 -0.0640 554 SER A CA 4178 C C . SER A 513 ? 0.2639 0.2750 0.3364 0.0407 0.0257 -0.0622 554 SER A C 4179 O O . SER A 513 ? 0.2458 0.2550 0.3180 0.0416 0.0223 -0.0576 554 SER A O 4180 C CB . SER A 513 ? 0.2136 0.2385 0.2949 0.0419 0.0313 -0.0672 554 SER A CB 4181 O OG A SER A 513 ? 0.2451 0.2699 0.3341 0.0455 0.0275 -0.0650 554 SER A OG 4182 O OG B SER A 513 ? 0.2135 0.2344 0.2999 0.0452 0.0321 -0.0710 554 SER A OG 4183 N N . VAL A 514 ? 0.2316 0.2377 0.3055 0.0418 0.0270 -0.0662 555 VAL A N 4184 C CA . VAL A 514 ? 0.2554 0.2530 0.3316 0.0439 0.0245 -0.0647 555 VAL A CA 4185 C C . VAL A 514 ? 0.2611 0.2588 0.3447 0.0487 0.0220 -0.0626 555 VAL A C 4186 O O . VAL A 514 ? 0.2872 0.2777 0.3716 0.0508 0.0193 -0.0593 555 VAL A O 4187 C CB . VAL A 514 ? 0.2607 0.2532 0.3382 0.0443 0.0264 -0.0703 555 VAL A CB 4188 C CG1 . VAL A 514 ? 0.2557 0.2516 0.3409 0.0484 0.0289 -0.0753 555 VAL A CG1 4189 C CG2 . VAL A 514 ? 0.2760 0.2587 0.3553 0.0453 0.0240 -0.0682 555 VAL A CG2 4190 N N . TYR A 515 ? 0.2385 0.2438 0.3280 0.0506 0.0229 -0.0644 556 TYR A N 4191 C CA . TYR A 515 ? 0.2646 0.2703 0.3626 0.0557 0.0200 -0.0635 556 TYR A CA 4192 C C . TYR A 515 ? 0.2668 0.2728 0.3623 0.0565 0.0154 -0.0578 556 TYR A C 4193 O O . TYR A 515 ? 0.2870 0.2921 0.3880 0.0611 0.0116 -0.0564 556 TYR A O 4194 C CB . TYR A 515 ? 0.2526 0.2666 0.3605 0.0579 0.0227 -0.0684 556 TYR A CB 4195 C CG . TYR A 515 ? 0.2667 0.2795 0.3757 0.0578 0.0275 -0.0743 556 TYR A CG 4196 C CD1 . TYR A 515 ? 0.2615 0.2660 0.3725 0.0606 0.0267 -0.0762 556 TYR A CD1 4197 C CD2 . TYR A 515 ? 0.2825 0.3014 0.3895 0.0552 0.0328 -0.0779 556 TYR A CD2 4198 C CE1 . TYR A 515 ? 0.2684 0.2711 0.3796 0.0607 0.0309 -0.0822 556 TYR A CE1 4199 C CE2 . TYR A 515 ? 0.2778 0.2948 0.3839 0.0556 0.0372 -0.0837 556 TYR A CE2 4200 C CZ . TYR A 515 ? 0.2648 0.2739 0.3730 0.0584 0.0360 -0.0861 556 TYR A CZ 4201 O OH . TYR A 515 ? 0.2988 0.3055 0.4056 0.0590 0.0399 -0.0923 556 TYR A OH 4202 N N . GLU A 516 ? 0.2570 0.2638 0.3442 0.0525 0.0152 -0.0545 557 GLU A N 4203 C CA . GLU A 516 ? 0.2726 0.2790 0.3566 0.0538 0.0108 -0.0493 557 GLU A CA 4204 C C . GLU A 516 ? 0.2736 0.2699 0.3520 0.0553 0.0086 -0.0447 557 GLU A C 4205 O O . GLU A 516 ? 0.2777 0.2699 0.3492 0.0521 0.0100 -0.0423 557 GLU A O 4206 C CB . GLU A 516 ? 0.3130 0.3255 0.3924 0.0501 0.0110 -0.0479 557 GLU A CB 4207 C CG . GLU A 516 ? 0.3168 0.3291 0.3887 0.0452 0.0138 -0.0474 557 GLU A CG 4208 C CD . GLU A 516 ? 0.3446 0.3611 0.4119 0.0431 0.0120 -0.0443 557 GLU A CD 4209 O OE1 . GLU A 516 ? 0.3326 0.3549 0.3992 0.0400 0.0142 -0.0457 557 GLU A OE1 4210 O OE2 . GLU A 516 ? 0.3133 0.3264 0.3770 0.0450 0.0085 -0.0402 557 GLU A OE2 4211 N N . THR A 517 ? 0.2660 0.2582 0.3486 0.0605 0.0056 -0.0438 558 THR A N 4212 C CA . THR A 517 ? 0.2693 0.2510 0.3481 0.0629 0.0041 -0.0396 558 THR A CA 4213 C C . THR A 517 ? 0.2697 0.2488 0.3454 0.0676 -0.0011 -0.0350 558 THR A C 4214 O O . THR A 517 ? 0.2617 0.2474 0.3406 0.0695 -0.0042 -0.0362 558 THR A O 4215 C CB . THR A 517 ? 0.2813 0.2583 0.3674 0.0659 0.0048 -0.0428 558 THR A CB 4216 O OG1 . THR A 517 ? 0.3120 0.2943 0.4070 0.0704 0.0023 -0.0457 558 THR A OG1 4217 C CG2 . THR A 517 ? 0.3001 0.2783 0.3884 0.0620 0.0096 -0.0480 558 THR A CG2 4218 N N . TYR A 518 ? 0.2825 0.2514 0.3523 0.0699 -0.0021 -0.0299 559 TYR A N 4219 C CA . TYR A 518 ? 0.2877 0.2519 0.3532 0.0756 -0.0072 -0.0255 559 TYR A CA 4220 C C . TYR A 518 ? 0.2915 0.2589 0.3666 0.0810 -0.0114 -0.0291 559 TYR A C 4221 O O . TYR A 518 ? 0.3000 0.2704 0.3750 0.0846 -0.0166 -0.0285 559 TYR A O 4222 C CB . TYR A 518 ? 0.2936 0.2451 0.3524 0.0775 -0.0065 -0.0197 559 TYR A CB 4223 C CG . TYR A 518 ? 0.2931 0.2382 0.3465 0.0843 -0.0118 -0.0152 559 TYR A CG 4224 C CD1 . TYR A 518 ? 0.3317 0.2758 0.3743 0.0856 -0.0142 -0.0108 559 TYR A CD1 4225 C CD2 . TYR A 518 ? 0.3587 0.2982 0.4172 0.0899 -0.0146 -0.0154 559 TYR A CD2 4226 C CE1 . TYR A 518 ? 0.3456 0.2829 0.3811 0.0926 -0.0196 -0.0066 559 TYR A CE1 4227 C CE2 . TYR A 518 ? 0.3889 0.3218 0.4412 0.0968 -0.0203 -0.0111 559 TYR A CE2 4228 C CZ . TYR A 518 ? 0.3889 0.3207 0.4292 0.0981 -0.0227 -0.0068 559 TYR A CZ 4229 O OH . TYR A 518 ? 0.4028 0.3274 0.4352 0.1054 -0.0286 -0.0026 559 TYR A OH 4230 N N . GLU A 519 ? 0.3039 0.2709 0.3882 0.0816 -0.0093 -0.0332 560 GLU A N 4231 C CA . GLU A 519 ? 0.3032 0.2731 0.3982 0.0871 -0.0130 -0.0366 560 GLU A CA 4232 C C . GLU A 519 ? 0.2928 0.2755 0.3956 0.0864 -0.0142 -0.0411 560 GLU A C 4233 O O . GLU A 519 ? 0.3061 0.2919 0.4152 0.0912 -0.0196 -0.0420 560 GLU A O 4234 C CB . GLU A 519 ? 0.3180 0.2848 0.4212 0.0878 -0.0098 -0.0406 560 GLU A CB 4235 C CG . GLU A 519 ? 0.3444 0.2975 0.4428 0.0900 -0.0099 -0.0362 560 GLU A CG 4236 C CD . GLU A 519 ? 0.3714 0.3192 0.4610 0.0842 -0.0053 -0.0331 560 GLU A CD 4237 O OE1 . GLU A 519 ? 0.3663 0.3203 0.4568 0.0787 -0.0013 -0.0368 560 GLU A OE1 4238 O OE2 . GLU A 519 ? 0.4026 0.3400 0.4850 0.0854 -0.0057 -0.0270 560 GLU A OE2 4239 N N . LEU A 520 ? 0.2731 0.2630 0.3760 0.0804 -0.0094 -0.0438 561 LEU A N 4240 C CA . LEU A 520 ? 0.2584 0.2599 0.3680 0.0788 -0.0098 -0.0471 561 LEU A CA 4241 C C . LEU A 520 ? 0.2718 0.2744 0.3778 0.0813 -0.0163 -0.0439 561 LEU A C 4242 O O . LEU A 520 ? 0.2678 0.2772 0.3835 0.0841 -0.0202 -0.0466 561 LEU A O 4243 C CB . LEU A 520 ? 0.2643 0.2712 0.3706 0.0719 -0.0039 -0.0487 561 LEU A CB 4244 C CG . LEU A 520 ? 0.2437 0.2616 0.3557 0.0698 -0.0039 -0.0511 561 LEU A CG 4245 C CD1 . LEU A 520 ? 0.2653 0.2910 0.3930 0.0723 -0.0030 -0.0564 561 LEU A CD1 4246 C CD2 . LEU A 520 ? 0.2695 0.2907 0.3754 0.0632 0.0015 -0.0514 561 LEU A CD2 4247 N N . VAL A 521 ? 0.2701 0.2661 0.3626 0.0803 -0.0173 -0.0386 562 VAL A N 4248 C CA . VAL A 521 ? 0.2762 0.2726 0.3630 0.0826 -0.0232 -0.0359 562 VAL A CA 4249 C C . VAL A 521 ? 0.2935 0.2846 0.3814 0.0903 -0.0303 -0.0345 562 VAL A C 4250 O O . VAL A 521 ? 0.3014 0.2976 0.3947 0.0936 -0.0365 -0.0363 562 VAL A O 4251 C CB . VAL A 521 ? 0.2790 0.2693 0.3505 0.0801 -0.0218 -0.0305 562 VAL A CB 4252 C CG1 . VAL A 521 ? 0.2906 0.2801 0.3549 0.0834 -0.0283 -0.0280 562 VAL A CG1 4253 C CG2 . VAL A 521 ? 0.2890 0.2853 0.3600 0.0728 -0.0159 -0.0322 562 VAL A CG2 4254 N N . GLU A 522 ? 0.3000 0.2809 0.3832 0.0933 -0.0298 -0.0313 563 GLU A N 4255 C CA . GLU A 522 ? 0.3358 0.3092 0.4168 0.1010 -0.0366 -0.0286 563 GLU A CA 4256 C C . GLU A 522 ? 0.3397 0.3192 0.4367 0.1053 -0.0406 -0.0339 563 GLU A C 4257 O O . GLU A 522 ? 0.3527 0.3316 0.4510 0.1114 -0.0486 -0.0336 563 GLU A O 4258 C CB . GLU A 522 ? 0.3631 0.3235 0.4360 0.1025 -0.0338 -0.0237 563 GLU A CB 4259 C CG . GLU A 522 ? 0.4243 0.3741 0.4900 0.1105 -0.0403 -0.0190 563 GLU A CG 4260 C CD . GLU A 522 ? 0.5155 0.4650 0.5936 0.1162 -0.0442 -0.0222 563 GLU A CD 4261 O OE1 . GLU A 522 ? 0.5029 0.4562 0.5928 0.1138 -0.0398 -0.0267 563 GLU A OE1 4262 O OE2 . GLU A 522 ? 0.5405 0.4857 0.6160 0.1234 -0.0519 -0.0204 563 GLU A OE2 4263 N N . LYS A 523 ? 0.3267 0.3122 0.4361 0.1026 -0.0355 -0.0389 564 LYS A N 4264 C CA . LYS A 523 ? 0.3241 0.3163 0.4503 0.1066 -0.0383 -0.0441 564 LYS A CA 4265 C C . LYS A 523 ? 0.3263 0.3318 0.4638 0.1050 -0.0402 -0.0486 564 LYS A C 4266 O O . LYS A 523 ? 0.3526 0.3625 0.5011 0.1100 -0.0465 -0.0512 564 LYS A O 4267 C CB . LYS A 523 ? 0.3092 0.3021 0.4443 0.1050 -0.0317 -0.0480 564 LYS A CB 4268 C CG . LYS A 523 ? 0.3359 0.3158 0.4643 0.1072 -0.0304 -0.0447 564 LYS A CG 4269 C CD . LYS A 523 ? 0.3742 0.3555 0.5118 0.1052 -0.0238 -0.0497 564 LYS A CD 4270 C CE . LYS A 523 ? 0.4685 0.4366 0.6000 0.1061 -0.0217 -0.0469 564 LYS A CE 4271 N NZ . LYS A 523 ? 0.5362 0.4947 0.6655 0.1133 -0.0281 -0.0426 564 LYS A NZ 4272 N N . PHE A 524 ? 0.3076 0.3195 0.4436 0.0982 -0.0346 -0.0498 565 PHE A N 4273 C CA . PHE A 524 ? 0.3035 0.3282 0.4526 0.0957 -0.0340 -0.0544 565 PHE A CA 4274 C C . PHE A 524 ? 0.3072 0.3358 0.4513 0.0930 -0.0370 -0.0530 565 PHE A C 4275 O O . PHE A 524 ? 0.3361 0.3743 0.4927 0.0927 -0.0392 -0.0565 565 PHE A O 4276 C CB . PHE A 524 ? 0.2934 0.3244 0.4492 0.0904 -0.0247 -0.0582 565 PHE A CB 4277 C CG . PHE A 524 ? 0.3058 0.3342 0.4689 0.0934 -0.0217 -0.0610 565 PHE A CG 4278 C CD1 . PHE A 524 ? 0.3155 0.3475 0.4937 0.0993 -0.0258 -0.0643 565 PHE A CD1 4279 C CD2 . PHE A 524 ? 0.2951 0.3172 0.4505 0.0906 -0.0154 -0.0605 565 PHE A CD2 4280 C CE1 . PHE A 524 ? 0.3348 0.3642 0.5201 0.1023 -0.0230 -0.0670 565 PHE A CE1 4281 C CE2 . PHE A 524 ? 0.3163 0.3352 0.4784 0.0936 -0.0129 -0.0635 565 PHE A CE2 4282 C CZ . PHE A 524 ? 0.3334 0.3558 0.5102 0.0995 -0.0165 -0.0667 565 PHE A CZ 4283 N N . TYR A 525 ? 0.2933 0.3150 0.4204 0.0908 -0.0367 -0.0483 566 TYR A N 4284 C CA . TYR A 525 ? 0.2825 0.3079 0.4050 0.0882 -0.0392 -0.0474 566 TYR A CA 4285 C C . TYR A 525 ? 0.2936 0.3134 0.4080 0.0937 -0.0485 -0.0447 566 TYR A C 4286 O O . TYR A 525 ? 0.3033 0.3288 0.4233 0.0946 -0.0542 -0.0469 566 TYR A O 4287 C CB . TYR A 525 ? 0.2605 0.2837 0.3705 0.0818 -0.0327 -0.0446 566 TYR A CB 4288 C CG . TYR A 525 ? 0.2635 0.2954 0.3817 0.0757 -0.0253 -0.0482 566 TYR A CG 4289 C CD1 . TYR A 525 ? 0.2695 0.3017 0.3926 0.0744 -0.0190 -0.0504 566 TYR A CD1 4290 C CD2 . TYR A 525 ? 0.2929 0.3322 0.4137 0.0715 -0.0246 -0.0493 566 TYR A CD2 4291 C CE1 . TYR A 525 ? 0.2708 0.3102 0.3997 0.0695 -0.0121 -0.0536 566 TYR A CE1 4292 C CE2 . TYR A 525 ? 0.2660 0.3125 0.3933 0.0662 -0.0174 -0.0520 566 TYR A CE2 4293 C CZ . TYR A 525 ? 0.2789 0.3253 0.4096 0.0654 -0.0112 -0.0541 566 TYR A CZ 4294 O OH . TYR A 525 ? 0.2689 0.3218 0.4043 0.0608 -0.0041 -0.0567 566 TYR A OH 4295 N N . ASP A 526 ? 0.2834 0.2916 0.3841 0.0974 -0.0500 -0.0399 567 ASP A N 4296 C CA . ASP A 526 ? 0.2977 0.2989 0.3853 0.1021 -0.0574 -0.0363 567 ASP A CA 4297 C C . ASP A 526 ? 0.3188 0.3077 0.3969 0.1084 -0.0599 -0.0318 567 ASP A C 4298 O O . ASP A 526 ? 0.3280 0.3074 0.3898 0.1086 -0.0580 -0.0263 567 ASP A O 4299 C CB . ASP A 526 ? 0.2780 0.2773 0.3516 0.0975 -0.0541 -0.0331 567 ASP A CB 4300 C CG . ASP A 526 ? 0.3011 0.2957 0.3625 0.1018 -0.0619 -0.0309 567 ASP A CG 4301 O OD1 . ASP A 526 ? 0.3375 0.3315 0.4021 0.1081 -0.0706 -0.0324 567 ASP A OD1 4302 O OD2 . ASP A 526 ? 0.3121 0.3033 0.3606 0.0993 -0.0592 -0.0277 567 ASP A OD2 4303 N N . PRO A 527 ? 0.3334 0.3224 0.4221 0.1137 -0.0641 -0.0341 568 PRO A N 4304 C CA . PRO A 527 ? 0.3526 0.3292 0.4329 0.1194 -0.0657 -0.0296 568 PRO A CA 4305 C C . PRO A 527 ? 0.3711 0.3367 0.4322 0.1247 -0.0714 -0.0238 568 PRO A C 4306 O O . PRO A 527 ? 0.3936 0.3473 0.4426 0.1269 -0.0691 -0.0181 568 PRO A O 4307 C CB . PRO A 527 ? 0.3638 0.3440 0.4605 0.1250 -0.0712 -0.0339 568 PRO A CB 4308 C CG . PRO A 527 ? 0.3683 0.3633 0.4831 0.1212 -0.0705 -0.0406 568 PRO A CG 4309 C CD . PRO A 527 ? 0.3292 0.3296 0.4390 0.1143 -0.0666 -0.0406 568 PRO A CD 4310 N N A MET A 528 ? 0.3650 0.3342 0.4234 0.1268 -0.0786 -0.0254 569 MET A N 4311 N N B MET A 528 ? 0.3702 0.3394 0.4288 0.1268 -0.0787 -0.0254 569 MET A N 4312 C CA A MET A 528 ? 0.3859 0.3449 0.4249 0.1324 -0.0846 -0.0206 569 MET A CA 4313 C CA B MET A 528 ? 0.3953 0.3545 0.4344 0.1324 -0.0847 -0.0207 569 MET A CA 4314 C C A MET A 528 ? 0.3727 0.3300 0.3971 0.1275 -0.0795 -0.0174 569 MET A C 4315 C C B MET A 528 ? 0.3789 0.3355 0.4028 0.1275 -0.0790 -0.0170 569 MET A C 4316 O O A MET A 528 ? 0.3768 0.3258 0.3835 0.1316 -0.0831 -0.0134 569 MET A O 4317 O O B MET A 528 ? 0.3857 0.3328 0.3911 0.1315 -0.0817 -0.0123 569 MET A O 4318 C CB A MET A 528 ? 0.3972 0.3599 0.4410 0.1385 -0.0967 -0.0246 569 MET A CB 4319 C CB B MET A 528 ? 0.4106 0.3744 0.4543 0.1377 -0.0964 -0.0249 569 MET A CB 4320 C CG A MET A 528 ? 0.4380 0.4029 0.4973 0.1439 -0.1024 -0.0279 569 MET A CG 4321 C CG B MET A 528 ? 0.4716 0.4380 0.5305 0.1436 -0.1036 -0.0286 569 MET A CG 4322 S SD A MET A 528 ? 0.5005 0.4492 0.5477 0.1506 -0.1020 -0.0210 569 MET A SD 4323 S SD B MET A 528 ? 0.5717 0.5467 0.6415 0.1483 -0.1173 -0.0351 569 MET A SD 4324 C CE A MET A 528 ? 0.4979 0.4335 0.5186 0.1582 -0.1100 -0.0153 569 MET A CE 4325 C CE B MET A 528 ? 0.5723 0.5333 0.6146 0.1562 -0.1262 -0.0301 569 MET A CE 4326 N N . PHE A 529 ? 0.3552 0.3201 0.3866 0.1192 -0.0713 -0.0193 570 PHE A N 4327 C CA . PHE A 529 ? 0.3376 0.3017 0.3573 0.1142 -0.0661 -0.0167 570 PHE A CA 4328 C C . PHE A 529 ? 0.3408 0.3068 0.3534 0.1163 -0.0730 -0.0180 570 PHE A C 4329 O O . PHE A 529 ? 0.3440 0.3060 0.3423 0.1149 -0.0707 -0.0148 570 PHE A O 4330 C CB . PHE A 529 ? 0.3526 0.3051 0.3572 0.1139 -0.0595 -0.0095 570 PHE A CB 4331 C CG . PHE A 529 ? 0.3461 0.2999 0.3596 0.1085 -0.0511 -0.0097 570 PHE A CG 4332 C CD1 . PHE A 529 ? 0.3541 0.3123 0.3683 0.1008 -0.0433 -0.0099 570 PHE A CD1 4333 C CD2 . PHE A 529 ? 0.3611 0.3122 0.3832 0.1114 -0.0515 -0.0103 570 PHE A CD2 4334 C CE1 . PHE A 529 ? 0.3413 0.3010 0.3640 0.0960 -0.0364 -0.0110 570 PHE A CE1 4335 C CE2 . PHE A 529 ? 0.3572 0.3095 0.3879 0.1065 -0.0442 -0.0115 570 PHE A CE2 4336 C CZ . PHE A 529 ? 0.3312 0.2878 0.3617 0.0988 -0.0368 -0.0118 570 PHE A CZ 4337 N N . LYS A 530 ? 0.3367 0.3092 0.3607 0.1193 -0.0814 -0.0232 571 LYS A N 4338 C CA . LYS A 530 ? 0.3460 0.3206 0.3659 0.1215 -0.0892 -0.0257 571 LYS A CA 4339 C C . LYS A 530 ? 0.3230 0.3074 0.3500 0.1137 -0.0850 -0.0289 571 LYS A C 4340 O O . LYS A 530 ? 0.3266 0.3099 0.3441 0.1139 -0.0879 -0.0289 571 LYS A O 4341 C CB . LYS A 530 ? 0.3602 0.3384 0.3914 0.1276 -0.1005 -0.0305 571 LYS A CB 4342 C CG . LYS A 530 ? 0.3586 0.3499 0.4150 0.1238 -0.0998 -0.0367 571 LYS A CG 4343 C CD . LYS A 530 ? 0.3740 0.3683 0.4417 0.1306 -0.1118 -0.0412 571 LYS A CD 4344 C CE . LYS A 530 ? 0.3940 0.4021 0.4884 0.1267 -0.1105 -0.0474 571 LYS A CE 4345 N NZ . LYS A 530 ? 0.4120 0.4246 0.5194 0.1328 -0.1232 -0.0526 571 LYS A NZ 4346 N N . TYR A 531 ? 0.3103 0.3036 0.3531 0.1073 -0.0785 -0.0316 572 TYR A N 4347 C CA . TYR A 531 ? 0.3001 0.3016 0.3481 0.1000 -0.0740 -0.0339 572 TYR A CA 4348 C C . TYR A 531 ? 0.3004 0.2963 0.3327 0.0963 -0.0666 -0.0290 572 TYR A C 4349 O O . TYR A 531 ? 0.3112 0.3089 0.3385 0.0935 -0.0664 -0.0293 572 TYR A O 4350 C CB . TYR A 531 ? 0.2772 0.2897 0.3453 0.0945 -0.0689 -0.0381 572 TYR A CB 4351 C CG . TYR A 531 ? 0.3005 0.3193 0.3857 0.0982 -0.0758 -0.0430 572 TYR A CG 4352 C CD1 . TYR A 531 ? 0.3253 0.3489 0.4170 0.0997 -0.0840 -0.0468 572 TYR A CD1 4353 C CD2 . TYR A 531 ? 0.3350 0.3547 0.4305 0.1004 -0.0746 -0.0441 572 TYR A CD2 4354 C CE1 . TYR A 531 ? 0.3427 0.3725 0.4515 0.1032 -0.0909 -0.0515 572 TYR A CE1 4355 C CE2 . TYR A 531 ? 0.3466 0.3723 0.4587 0.1043 -0.0813 -0.0487 572 TYR A CE2 4356 C CZ . TYR A 531 ? 0.3261 0.3573 0.4454 0.1054 -0.0892 -0.0523 572 TYR A CZ 4357 O OH . TYR A 531 ? 0.3891 0.4268 0.5269 0.1092 -0.0961 -0.0571 572 TYR A OH 4358 N N . HIS A 532 ? 0.2889 0.2781 0.3146 0.0964 -0.0608 -0.0247 573 HIS A N 4359 C CA . HIS A 532 ? 0.2951 0.2781 0.3063 0.0937 -0.0542 -0.0197 573 HIS A CA 4360 C C . HIS A 532 ? 0.3011 0.2769 0.2952 0.0984 -0.0590 -0.0169 573 HIS A C 4361 O O . HIS A 532 ? 0.2953 0.2708 0.2813 0.0953 -0.0557 -0.0155 573 HIS A O 4362 C CB . HIS A 532 ? 0.3007 0.2759 0.3075 0.0944 -0.0489 -0.0154 573 HIS A CB 4363 C CG . HIS A 532 ? 0.3007 0.2811 0.3195 0.0887 -0.0420 -0.0173 573 HIS A CG 4364 N ND1 . HIS A 532 ? 0.2879 0.2739 0.3218 0.0890 -0.0431 -0.0215 573 HIS A ND1 4365 C CD2 . HIS A 532 ? 0.3085 0.2886 0.3259 0.0830 -0.0340 -0.0156 573 HIS A CD2 4366 C CE1 . HIS A 532 ? 0.3149 0.3035 0.3551 0.0839 -0.0360 -0.0225 573 HIS A CE1 4367 N NE2 . HIS A 532 ? 0.3248 0.3097 0.3551 0.0803 -0.0308 -0.0190 573 HIS A NE2 4368 N N . LEU A 533 ? 0.3193 0.2889 0.3074 0.1060 -0.0666 -0.0162 574 LEU A N 4369 C CA . LEU A 533 ? 0.3294 0.2910 0.2990 0.1113 -0.0709 -0.0135 574 LEU A CA 4370 C C . LEU A 533 ? 0.3250 0.2929 0.2964 0.1097 -0.0755 -0.0180 574 LEU A C 4371 O O . LEU A 533 ? 0.3265 0.2907 0.2845 0.1096 -0.0740 -0.0160 574 LEU A O 4372 C CB . LEU A 533 ? 0.3469 0.3003 0.3092 0.1205 -0.0793 -0.0122 574 LEU A CB 4373 C CG . LEU A 533 ? 0.3606 0.3049 0.3017 0.1268 -0.0843 -0.0097 574 LEU A CG 4374 C CD1 . LEU A 533 ? 0.3882 0.3242 0.3124 0.1254 -0.0750 -0.0028 574 LEU A CD1 4375 C CD2 . LEU A 533 ? 0.3988 0.3350 0.3332 0.1361 -0.0931 -0.0086 574 LEU A CD2 4376 N N . THR A 534 ? 0.3189 0.2962 0.3074 0.1086 -0.0809 -0.0240 575 THR A N 4377 C CA . THR A 534 ? 0.3050 0.2890 0.2985 0.1062 -0.0851 -0.0287 575 THR A CA 4378 C C . THR A 534 ? 0.2942 0.2816 0.2866 0.0987 -0.0766 -0.0277 575 THR A C 4379 O O . THR A 534 ? 0.2987 0.2848 0.2825 0.0986 -0.0781 -0.0280 575 THR A O 4380 C CB . THR A 534 ? 0.3057 0.3000 0.3213 0.1051 -0.0904 -0.0351 575 THR A CB 4381 O OG1 . THR A 534 ? 0.3256 0.3162 0.3407 0.1131 -0.1003 -0.0365 575 THR A OG1 4382 C CG2 . THR A 534 ? 0.3116 0.3132 0.3348 0.1014 -0.0936 -0.0397 575 THR A CG2 4383 N N . VAL A 535 ? 0.2736 0.2652 0.2745 0.0930 -0.0682 -0.0266 576 VAL A N 4384 C CA . VAL A 535 ? 0.2573 0.2517 0.2567 0.0861 -0.0602 -0.0253 576 VAL A CA 4385 C C . VAL A 535 ? 0.2739 0.2595 0.2542 0.0877 -0.0567 -0.0201 576 VAL A C 4386 O O . VAL A 535 ? 0.2917 0.2781 0.2668 0.0849 -0.0546 -0.0199 576 VAL A O 4387 C CB . VAL A 535 ? 0.2561 0.2562 0.2677 0.0802 -0.0526 -0.0257 576 VAL A CB 4388 C CG1 . VAL A 535 ? 0.2401 0.2421 0.2483 0.0737 -0.0451 -0.0241 576 VAL A CG1 4389 C CG2 . VAL A 535 ? 0.2634 0.2731 0.2937 0.0784 -0.0555 -0.0312 576 VAL A CG2 4390 N N . ALA A 536 ? 0.2793 0.2561 0.2493 0.0923 -0.0560 -0.0157 577 ALA A N 4391 C CA . ALA A 536 ? 0.2971 0.2652 0.2490 0.0943 -0.0522 -0.0104 577 ALA A CA 4392 C C . ALA A 536 ? 0.3090 0.2738 0.2489 0.0987 -0.0582 -0.0115 577 ALA A C 4393 O O . ALA A 536 ? 0.3076 0.2699 0.2372 0.0977 -0.0544 -0.0093 577 ALA A O 4394 C CB . ALA A 536 ? 0.3134 0.2719 0.2567 0.0988 -0.0502 -0.0052 577 ALA A CB 4395 N N . GLN A 537 ? 0.3174 0.2821 0.2587 0.1039 -0.0679 -0.0150 578 GLN A N 4396 C CA . GLN A 537 ? 0.3203 0.2820 0.2509 0.1084 -0.0751 -0.0172 578 GLN A CA 4397 C C . GLN A 537 ? 0.3167 0.2861 0.2547 0.1028 -0.0747 -0.0213 578 GLN A C 4398 O O . GLN A 537 ? 0.3279 0.2938 0.2539 0.1044 -0.0757 -0.0213 578 GLN A O 4399 C CB . GLN A 537 ? 0.3365 0.2968 0.2687 0.1153 -0.0868 -0.0209 578 GLN A CB 4400 C CG . GLN A 537 ? 0.3451 0.2958 0.2666 0.1220 -0.0881 -0.0165 578 GLN A CG 4401 C CD . GLN A 537 ? 0.4197 0.3702 0.3459 0.1285 -0.1000 -0.0204 578 GLN A CD 4402 O OE1 . GLN A 537 ? 0.4052 0.3638 0.3453 0.1272 -0.1068 -0.0268 578 GLN A OE1 4403 N NE2 . GLN A 537 ? 0.4314 0.3724 0.3466 0.1355 -0.1024 -0.0164 578 GLN A NE2 4404 N N . VAL A 538 ? 0.2962 0.2756 0.2533 0.0966 -0.0734 -0.0247 579 VAL A N 4405 C CA . VAL A 538 ? 0.2938 0.2801 0.2586 0.0909 -0.0724 -0.0280 579 VAL A CA 4406 C C . VAL A 538 ? 0.2897 0.2745 0.2466 0.0868 -0.0632 -0.0240 579 VAL A C 4407 O O . VAL A 538 ? 0.2930 0.2764 0.2424 0.0868 -0.0637 -0.0245 579 VAL A O 4408 C CB . VAL A 538 ? 0.2825 0.2793 0.2690 0.0853 -0.0717 -0.0318 579 VAL A CB 4409 C CG1 . VAL A 538 ? 0.2789 0.2816 0.2718 0.0791 -0.0693 -0.0340 579 VAL A CG1 4410 C CG2 . VAL A 538 ? 0.2918 0.2913 0.2884 0.0893 -0.0816 -0.0366 579 VAL A CG2 4411 N N . ARG A 539 ? 0.2784 0.2638 0.2380 0.0833 -0.0552 -0.0205 580 ARG A N 4412 C CA . ARG A 539 ? 0.2804 0.2652 0.2348 0.0791 -0.0469 -0.0172 580 ARG A CA 4413 C C . ARG A 539 ? 0.3064 0.2823 0.2423 0.0838 -0.0458 -0.0133 580 ARG A C 4414 O O . ARG A 539 ? 0.2923 0.2680 0.2225 0.0824 -0.0432 -0.0128 580 ARG A O 4415 C CB . ARG A 539 ? 0.2745 0.2609 0.2353 0.0749 -0.0395 -0.0145 580 ARG A CB 4416 C CG . ARG A 539 ? 0.2604 0.2556 0.2383 0.0698 -0.0390 -0.0183 580 ARG A CG 4417 C CD . ARG A 539 ? 0.2764 0.2719 0.2592 0.0669 -0.0327 -0.0162 580 ARG A CD 4418 N NE . ARG A 539 ? 0.2695 0.2732 0.2672 0.0624 -0.0316 -0.0199 580 ARG A NE 4419 C CZ . ARG A 539 ? 0.2642 0.2695 0.2685 0.0597 -0.0270 -0.0198 580 ARG A CZ 4420 N NH1 . ARG A 539 ? 0.2897 0.2890 0.2882 0.0609 -0.0234 -0.0162 580 ARG A NH1 4421 N NH2 . ARG A 539 ? 0.2628 0.2755 0.2793 0.0558 -0.0256 -0.0232 580 ARG A NH2 4422 N N . GLY A 540 ? 0.3022 0.2705 0.2285 0.0897 -0.0473 -0.0103 581 GLY A N 4423 C CA . GLY A 540 ? 0.3232 0.2821 0.2305 0.0948 -0.0452 -0.0059 581 GLY A CA 4424 C C . GLY A 540 ? 0.3318 0.2881 0.2290 0.0993 -0.0519 -0.0089 581 GLY A C 4425 O O . GLY A 540 ? 0.3290 0.2813 0.2140 0.1007 -0.0484 -0.0069 581 GLY A O 4426 N N . GLY A 541 ? 0.3218 0.2804 0.2245 0.1019 -0.0615 -0.0140 582 GLY A N 4427 C CA . GLY A 541 ? 0.3257 0.2821 0.2202 0.1061 -0.0692 -0.0180 582 GLY A CA 4428 C C . GLY A 541 ? 0.3282 0.2897 0.2268 0.1009 -0.0665 -0.0203 582 GLY A C 4429 O O . GLY A 541 ? 0.3335 0.2905 0.2196 0.1041 -0.0679 -0.0210 582 GLY A O 4430 N N . MET A 542 ? 0.2980 0.2684 0.2136 0.0932 -0.0627 -0.0215 583 MET A N 4431 C CA A MET A 542 ? 0.2925 0.2674 0.2124 0.0881 -0.0597 -0.0231 583 MET A CA 4432 C CA B MET A 542 ? 0.3046 0.2798 0.2250 0.0879 -0.0595 -0.0230 583 MET A CA 4433 C C . MET A 542 ? 0.3037 0.2742 0.2112 0.0882 -0.0516 -0.0184 583 MET A C 4434 O O . MET A 542 ? 0.3063 0.2748 0.2062 0.0894 -0.0520 -0.0194 583 MET A O 4435 C CB A MET A 542 ? 0.2736 0.2581 0.2126 0.0802 -0.0566 -0.0246 583 MET A CB 4436 C CB B MET A 542 ? 0.2966 0.2810 0.2355 0.0800 -0.0559 -0.0242 583 MET A CB 4437 C CG A MET A 542 ? 0.2707 0.2607 0.2236 0.0794 -0.0642 -0.0300 583 MET A CG 4438 C CG B MET A 542 ? 0.3441 0.3344 0.2981 0.0791 -0.0626 -0.0290 583 MET A CG 4439 S SD A MET A 542 ? 0.2290 0.2294 0.2028 0.0709 -0.0595 -0.0312 583 MET A SD 4440 S SD B MET A 542 ? 0.4803 0.4730 0.4390 0.0786 -0.0701 -0.0348 583 MET A SD 4441 C CE A MET A 542 ? 0.2350 0.2381 0.2103 0.0658 -0.0569 -0.0322 583 MET A CE 4442 C CE B MET A 542 ? 0.4230 0.4217 0.3899 0.0701 -0.0619 -0.0336 583 MET A CE 4443 N N . VAL A 543 ? 0.2952 0.2639 0.2009 0.0872 -0.0444 -0.0133 584 VAL A N 4444 C CA . VAL A 543 ? 0.3033 0.2682 0.1993 0.0870 -0.0360 -0.0085 584 VAL A CA 4445 C C . VAL A 543 ? 0.3193 0.2751 0.1958 0.0948 -0.0380 -0.0073 584 VAL A C 4446 O O . VAL A 543 ? 0.3196 0.2739 0.1888 0.0952 -0.0345 -0.0066 584 VAL A O 4447 C CB . VAL A 543 ? 0.2942 0.2581 0.1930 0.0850 -0.0290 -0.0035 584 VAL A CB 4448 C CG1 . VAL A 543 ? 0.3128 0.2715 0.2011 0.0859 -0.0205 0.0019 584 VAL A CG1 4449 C CG2 . VAL A 543 ? 0.2774 0.2501 0.1939 0.0772 -0.0263 -0.0051 584 VAL A CG2 4450 N N . PHE A 544 ? 0.3335 0.2832 0.2016 0.1011 -0.0437 -0.0071 585 PHE A N 4451 C CA . PHE A 544 ? 0.3461 0.2863 0.1937 0.1093 -0.0462 -0.0062 585 PHE A CA 4452 C C . PHE A 544 ? 0.3552 0.2959 0.1986 0.1108 -0.0514 -0.0114 585 PHE A C 4453 O O . PHE A 544 ? 0.3717 0.3075 0.2014 0.1139 -0.0476 -0.0098 585 PHE A O 4454 C CB . PHE A 544 ? 0.3554 0.2894 0.1956 0.1161 -0.0537 -0.0063 585 PHE A CB 4455 C CG . PHE A 544 ? 0.3943 0.3168 0.2105 0.1251 -0.0549 -0.0039 585 PHE A CG 4456 C CD1 . PHE A 544 ? 0.4100 0.3243 0.2138 0.1285 -0.0482 0.0033 585 PHE A CD1 4457 C CD2 . PHE A 544 ? 0.4292 0.3487 0.2351 0.1298 -0.0620 -0.0086 585 PHE A CD2 4458 C CE1 . PHE A 544 ? 0.4630 0.3660 0.2429 0.1370 -0.0481 0.0062 585 PHE A CE1 4459 C CE2 . PHE A 544 ? 0.4278 0.3362 0.2096 0.1385 -0.0626 -0.0065 585 PHE A CE2 4460 C CZ . PHE A 544 ? 0.4731 0.3731 0.2415 0.1421 -0.0552 0.0012 585 PHE A CZ 4461 N N . GLU A 545 ? 0.3519 0.2987 0.2079 0.1084 -0.0594 -0.0175 586 GLU A N 4462 C CA A GLU A 545 ? 0.3673 0.3146 0.2216 0.1095 -0.0653 -0.0230 586 GLU A CA 4463 C CA B GLU A 545 ? 0.3632 0.3101 0.2166 0.1098 -0.0652 -0.0229 586 GLU A CA 4464 C C . GLU A 545 ? 0.3528 0.3036 0.2103 0.1045 -0.0582 -0.0223 586 GLU A C 4465 O O . GLU A 545 ? 0.3565 0.3035 0.2034 0.1076 -0.0584 -0.0237 586 GLU A O 4466 C CB A GLU A 545 ? 0.3691 0.3228 0.2397 0.1070 -0.0746 -0.0293 586 GLU A CB 4467 C CB B GLU A 545 ? 0.3657 0.3179 0.2334 0.1083 -0.0754 -0.0294 586 GLU A CB 4468 C CG A GLU A 545 ? 0.4129 0.3626 0.2795 0.1134 -0.0845 -0.0318 586 GLU A CG 4469 C CG B GLU A 545 ? 0.3787 0.3289 0.2423 0.1113 -0.0837 -0.0355 586 GLU A CG 4470 C CD A GLU A 545 ? 0.4918 0.4320 0.3380 0.1221 -0.0909 -0.0339 586 GLU A CD 4471 C CD B GLU A 545 ? 0.4384 0.3782 0.2807 0.1212 -0.0900 -0.0366 586 GLU A CD 4472 O OE1 A GLU A 545 ? 0.5383 0.4697 0.3663 0.1285 -0.0890 -0.0297 586 GLU A OE1 4473 O OE1 B GLU A 545 ? 0.4385 0.3721 0.2681 0.1259 -0.0874 -0.0318 586 GLU A OE1 4474 O OE2 A GLU A 545 ? 0.5508 0.4916 0.3985 0.1227 -0.0975 -0.0398 586 GLU A OE2 4475 O OE2 B GLU A 545 ? 0.4878 0.4251 0.3258 0.1245 -0.0980 -0.0423 586 GLU A OE2 4476 N N . LEU A 546 ? 0.3205 0.2787 0.1927 0.0970 -0.0520 -0.0203 587 LEU A N 4477 C CA . LEU A 546 ? 0.3098 0.2717 0.1861 0.0922 -0.0455 -0.0195 587 LEU A CA 4478 C C . LEU A 546 ? 0.3315 0.2875 0.1931 0.0955 -0.0377 -0.0147 587 LEU A C 4479 O O . LEU A 546 ? 0.3386 0.2945 0.1968 0.0954 -0.0351 -0.0154 587 LEU A O 4480 C CB . LEU A 546 ? 0.3162 0.2862 0.2095 0.0842 -0.0406 -0.0179 587 LEU A CB 4481 C CG . LEU A 546 ? 0.2808 0.2575 0.1898 0.0800 -0.0466 -0.0226 587 LEU A CG 4482 C CD1 . LEU A 546 ? 0.2686 0.2512 0.1907 0.0743 -0.0422 -0.0205 587 LEU A CD1 4483 C CD2 . LEU A 546 ? 0.3250 0.3049 0.2392 0.0766 -0.0476 -0.0257 587 LEU A CD2 4484 N N . ALA A 547 ? 0.3333 0.2845 0.1869 0.0985 -0.0336 -0.0098 588 ALA A N 4485 C CA . ALA A 547 ? 0.3540 0.2999 0.1953 0.1012 -0.0248 -0.0046 588 ALA A CA 4486 C C . ALA A 547 ? 0.3725 0.3090 0.1927 0.1101 -0.0275 -0.0050 588 ALA A C 4487 O O . ALA A 547 ? 0.3908 0.3233 0.2006 0.1125 -0.0201 -0.0016 588 ALA A O 4488 C CB . ALA A 547 ? 0.3592 0.3037 0.2019 0.0999 -0.0181 0.0014 588 ALA A CB 4489 N N . ASN A 548 ? 0.3751 0.3081 0.1895 0.1149 -0.0377 -0.0094 589 ASN A N 4490 C CA . ASN A 548 ? 0.3909 0.3136 0.1827 0.1243 -0.0406 -0.0095 589 ASN A CA 4491 C C . ASN A 548 ? 0.4102 0.3311 0.1966 0.1279 -0.0498 -0.0166 589 ASN A C 4492 O O . ASN A 548 ? 0.4544 0.3670 0.2212 0.1353 -0.0502 -0.0170 589 ASN A O 4493 C CB . ASN A 548 ? 0.3943 0.3103 0.1770 0.1295 -0.0439 -0.0068 589 ASN A CB 4494 C CG A ASN A 548 ? 0.4226 0.3274 0.1816 0.1374 -0.0388 -0.0017 589 ASN A CG 4495 C CG B ASN A 548 ? 0.4204 0.3340 0.2009 0.1283 -0.0329 0.0014 589 ASN A CG 4496 O OD1 A ASN A 548 ? 0.4383 0.3419 0.1936 0.1362 -0.0276 0.0037 589 ASN A OD1 4497 O OD1 B ASN A 548 ? 0.4364 0.3437 0.2026 0.1319 -0.0251 0.0060 589 ASN A OD1 4498 N ND2 A ASN A 548 ? 0.4884 0.3846 0.2312 0.1458 -0.0470 -0.0031 589 ASN A ND2 4499 N ND2 B ASN A 548 ? 0.4207 0.3395 0.2167 0.1229 -0.0318 0.0032 589 ASN A ND2 4500 N N . SER A 549 ? 0.3888 0.3171 0.1920 0.1231 -0.0569 -0.0223 590 SER A N 4501 C CA A SER A 549 ? 0.3920 0.3187 0.1924 0.1261 -0.0666 -0.0297 590 SER A CA 4502 C CA B SER A 549 ? 0.4065 0.3331 0.2068 0.1261 -0.0664 -0.0296 590 SER A CA 4503 C C . SER A 549 ? 0.4022 0.3271 0.1951 0.1268 -0.0613 -0.0302 590 SER A C 4504 O O . SER A 549 ? 0.4018 0.3319 0.2032 0.1213 -0.0526 -0.0271 590 SER A O 4505 C CB A SER A 549 ? 0.3819 0.3174 0.2044 0.1196 -0.0736 -0.0349 590 SER A CB 4506 C CB B SER A 549 ? 0.3986 0.3341 0.2209 0.1196 -0.0733 -0.0347 590 SER A CB 4507 O OG A SER A 549 ? 0.3505 0.2841 0.1717 0.1225 -0.0837 -0.0422 590 SER A OG 4508 O OG B SER A 549 ? 0.4479 0.3839 0.2750 0.1208 -0.0799 -0.0356 590 SER A OG 4509 N N . ILE A 550 ? 0.4077 0.3250 0.1844 0.1342 -0.0668 -0.0342 591 ILE A N 4510 C CA A ILE A 550 ? 0.4155 0.3308 0.1848 0.1355 -0.0619 -0.0352 591 ILE A CA 4511 C CA B ILE A 550 ? 0.4120 0.3272 0.1812 0.1356 -0.0620 -0.0353 591 ILE A CA 4512 C C . ILE A 550 ? 0.4018 0.3254 0.1906 0.1280 -0.0629 -0.0389 591 ILE A C 4513 O O . ILE A 550 ? 0.4025 0.3296 0.1961 0.1243 -0.0544 -0.0363 591 ILE A O 4514 C CB A ILE A 550 ? 0.4325 0.3375 0.1798 0.1453 -0.0683 -0.0397 591 ILE A CB 4515 C CB B ILE A 550 ? 0.4248 0.3300 0.1731 0.1451 -0.0693 -0.0404 591 ILE A CB 4516 C CG1 A ILE A 550 ? 0.4785 0.3747 0.2055 0.1528 -0.0662 -0.0349 591 ILE A CG1 4517 C CG1 B ILE A 550 ? 0.4668 0.3625 0.1923 0.1532 -0.0656 -0.0354 591 ILE A CG1 4518 C CG2 A ILE A 550 ? 0.4528 0.3556 0.1926 0.1470 -0.0623 -0.0407 591 ILE A CG2 4519 C CG2 B ILE A 550 ? 0.4372 0.3412 0.1813 0.1460 -0.0659 -0.0431 591 ILE A CG2 4520 C CD1 A ILE A 550 ? 0.4874 0.3835 0.2105 0.1514 -0.0518 -0.0262 591 ILE A CD1 4521 C CD1 B ILE A 550 ? 0.4450 0.3311 0.1518 0.1625 -0.0767 -0.0408 591 ILE A CD1 4522 N N . VAL A 551 ? 0.4111 0.3376 0.2114 0.1258 -0.0734 -0.0448 592 VAL A N 4523 C CA . VAL A 551 ? 0.4021 0.3364 0.2222 0.1181 -0.0741 -0.0475 592 VAL A CA 4524 C C . VAL A 551 ? 0.3751 0.3177 0.2131 0.1107 -0.0717 -0.0442 592 VAL A C 4525 O O . VAL A 551 ? 0.3956 0.3381 0.2350 0.1120 -0.0765 -0.0443 592 VAL A O 4526 C CB . VAL A 551 ? 0.4106 0.3435 0.2349 0.1193 -0.0860 -0.0557 592 VAL A CB 4527 C CG1 . VAL A 551 ? 0.4348 0.3754 0.2805 0.1109 -0.0865 -0.0578 592 VAL A CG1 4528 C CG2 . VAL A 551 ? 0.4576 0.3814 0.2628 0.1272 -0.0885 -0.0595 592 VAL A CG2 4529 N N . LEU A 552 ? 0.3638 0.3134 0.2151 0.1034 -0.0647 -0.0414 593 LEU A N 4530 C CA . LEU A 552 ? 0.3440 0.3012 0.2114 0.0966 -0.0621 -0.0385 593 LEU A CA 4531 C C . LEU A 552 ? 0.3364 0.2966 0.2160 0.0948 -0.0717 -0.0435 593 LEU A C 4532 O O . LEU A 552 ? 0.3619 0.3217 0.2458 0.0947 -0.0784 -0.0489 593 LEU A O 4533 C CB . LEU A 552 ? 0.3223 0.2858 0.2014 0.0894 -0.0549 -0.0361 593 LEU A CB 4534 C CG . LEU A 552 ? 0.3603 0.3232 0.2327 0.0896 -0.0445 -0.0303 593 LEU A CG 4535 C CD1 . LEU A 552 ? 0.3373 0.3065 0.2221 0.0829 -0.0394 -0.0290 593 LEU A CD1 4536 C CD2 . LEU A 552 ? 0.3821 0.3457 0.2544 0.0891 -0.0405 -0.0255 593 LEU A CD2 4537 N N . PRO A 553 ? 0.3292 0.2923 0.2153 0.0934 -0.0725 -0.0419 594 PRO A N 4538 C CA . PRO A 553 ? 0.3465 0.3126 0.2444 0.0926 -0.0817 -0.0466 594 PRO A CA 4539 C C . PRO A 553 ? 0.3383 0.3132 0.2578 0.0839 -0.0805 -0.0476 594 PRO A C 4540 O O . PRO A 553 ? 0.3497 0.3301 0.2814 0.0805 -0.0800 -0.0467 594 PRO A O 4541 C CB . PRO A 553 ? 0.3457 0.3107 0.2403 0.0955 -0.0819 -0.0438 594 PRO A CB 4542 C CG . PRO A 553 ? 0.3543 0.3210 0.2476 0.0923 -0.0706 -0.0371 594 PRO A CG 4543 C CD . PRO A 553 ? 0.3302 0.2931 0.2121 0.0938 -0.0656 -0.0359 594 PRO A CD 4544 N N . PHE A 554 ? 0.3241 0.2999 0.2472 0.0809 -0.0793 -0.0490 595 PHE A N 4545 C CA . PHE A 554 ? 0.3148 0.2975 0.2558 0.0730 -0.0775 -0.0494 595 PHE A CA 4546 C C . PHE A 554 ? 0.3386 0.3202 0.2862 0.0730 -0.0857 -0.0554 595 PHE A C 4547 O O . PHE A 554 ? 0.3623 0.3375 0.2983 0.0778 -0.0893 -0.0582 595 PHE A O 4548 C CB . PHE A 554 ? 0.2981 0.2817 0.2373 0.0696 -0.0692 -0.0456 595 PHE A CB 4549 C CG . PHE A 554 ? 0.2898 0.2756 0.2261 0.0680 -0.0604 -0.0398 595 PHE A CG 4550 C CD1 . PHE A 554 ? 0.3082 0.2966 0.2484 0.0673 -0.0593 -0.0379 595 PHE A CD1 4551 C CD2 . PHE A 554 ? 0.3109 0.2962 0.2423 0.0668 -0.0535 -0.0365 595 PHE A CD2 4552 C CE1 . PHE A 554 ? 0.2838 0.2739 0.2222 0.0654 -0.0513 -0.0328 595 PHE A CE1 4553 C CE2 . PHE A 554 ? 0.3270 0.3144 0.2571 0.0651 -0.0457 -0.0314 595 PHE A CE2 4554 C CZ . PHE A 554 ? 0.2855 0.2749 0.2189 0.0644 -0.0447 -0.0296 595 PHE A CZ 4555 N N . ASP A 555 ? 0.3133 0.3004 0.2789 0.0680 -0.0887 -0.0577 596 ASP A N 4556 C CA . ASP A 555 ? 0.3107 0.2970 0.2853 0.0671 -0.0963 -0.0634 596 ASP A CA 4557 C C . ASP A 555 ? 0.3152 0.3057 0.3032 0.0595 -0.0915 -0.0619 596 ASP A C 4558 O O . ASP A 555 ? 0.3082 0.3053 0.3111 0.0538 -0.0886 -0.0603 596 ASP A O 4559 C CB . ASP A 555 ? 0.3147 0.3033 0.3005 0.0681 -0.1052 -0.0682 596 ASP A CB 4560 C CG . ASP A 555 ? 0.3468 0.3326 0.3389 0.0688 -0.1145 -0.0749 596 ASP A CG 4561 O OD1 . ASP A 555 ? 0.3448 0.3283 0.3370 0.0667 -0.1132 -0.0755 596 ASP A OD1 4562 O OD2 . ASP A 555 ? 0.3714 0.3567 0.3678 0.0722 -0.1239 -0.0799 596 ASP A OD2 4563 N N . CYS A 556 ? 0.3018 0.2884 0.2838 0.0596 -0.0901 -0.0619 597 CYS A N 4564 C CA . CYS A 556 ? 0.3016 0.2911 0.2948 0.0528 -0.0857 -0.0599 597 CYS A CA 4565 C C . CYS A 556 ? 0.2918 0.2842 0.3037 0.0483 -0.0905 -0.0634 597 CYS A C 4566 O O . CYS A 556 ? 0.2886 0.2848 0.3122 0.0419 -0.0858 -0.0608 597 CYS A O 4567 C CB . CYS A 556 ? 0.3018 0.2859 0.2858 0.0545 -0.0844 -0.0600 597 CYS A CB 4568 S SG . CYS A 556 ? 0.3786 0.3546 0.3564 0.0606 -0.0951 -0.0677 597 CYS A SG 4569 N N . ARG A 557 ? 0.2858 0.2763 0.3014 0.0514 -0.0999 -0.0693 598 ARG A N 4570 C CA . ARG A 557 ? 0.2856 0.2792 0.3213 0.0468 -0.1044 -0.0728 598 ARG A CA 4571 C C . ARG A 557 ? 0.2900 0.2920 0.3406 0.0416 -0.0999 -0.0699 598 ARG A C 4572 O O . ARG A 557 ? 0.2970 0.3028 0.3652 0.0358 -0.0990 -0.0702 598 ARG A O 4573 C CB . ARG A 557 ? 0.3005 0.2907 0.3374 0.0518 -0.1163 -0.0802 598 ARG A CB 4574 C CG . ARG A 557 ? 0.2952 0.2768 0.3188 0.0566 -0.1211 -0.0838 598 ARG A CG 4575 C CD . ARG A 557 ? 0.3182 0.2954 0.3388 0.0630 -0.1335 -0.0915 598 ARG A CD 4576 N NE . ARG A 557 ? 0.3497 0.3270 0.3583 0.0686 -0.1347 -0.0906 598 ARG A NE 4577 C CZ . ARG A 557 ? 0.4079 0.3814 0.4105 0.0753 -0.1450 -0.0963 598 ARG A CZ 4578 N NH1 . ARG A 557 ? 0.4215 0.3910 0.4289 0.0770 -0.1552 -0.1036 598 ARG A NH1 4579 N NH2 . ARG A 557 ? 0.4099 0.3830 0.4011 0.0804 -0.1453 -0.0946 598 ARG A NH2 4580 N N . ASP A 558 ? 0.2749 0.2794 0.3185 0.0439 -0.0966 -0.0672 599 ASP A N 4581 C CA . ASP A 558 ? 0.2729 0.2850 0.3292 0.0396 -0.0918 -0.0646 599 ASP A CA 4582 C C . ASP A 558 ? 0.2623 0.2772 0.3220 0.0333 -0.0818 -0.0592 599 ASP A C 4583 O O . ASP A 558 ? 0.2655 0.2863 0.3399 0.0281 -0.0780 -0.0579 599 ASP A O 4584 C CB . ASP A 558 ? 0.2687 0.2816 0.3156 0.0441 -0.0911 -0.0632 599 ASP A CB 4585 C CG . ASP A 558 ? 0.3549 0.3666 0.4034 0.0497 -0.1016 -0.0687 599 ASP A CG 4586 O OD1 . ASP A 558 ? 0.4612 0.4748 0.5246 0.0482 -0.1082 -0.0735 599 ASP A OD1 4587 O OD2 . ASP A 558 ? 0.3627 0.3710 0.3973 0.0557 -0.1037 -0.0684 599 ASP A OD2 4588 N N . TYR A 559 ? 0.2510 0.2619 0.2975 0.0339 -0.0776 -0.0561 600 TYR A N 4589 C CA . TYR A 559 ? 0.2361 0.2490 0.2853 0.0282 -0.0693 -0.0512 600 TYR A CA 4590 C C . TYR A 559 ? 0.2457 0.2582 0.3085 0.0236 -0.0709 -0.0527 600 TYR A C 4591 O O . TYR A 559 ? 0.2343 0.2505 0.3071 0.0180 -0.0653 -0.0497 600 TYR A O 4592 C CB . TYR A 559 ? 0.2407 0.2494 0.2741 0.0301 -0.0654 -0.0480 600 TYR A CB 4593 C CG . TYR A 559 ? 0.2380 0.2501 0.2674 0.0278 -0.0570 -0.0427 600 TYR A CG 4594 C CD1 . TYR A 559 ? 0.2437 0.2601 0.2829 0.0220 -0.0516 -0.0400 600 TYR A CD1 4595 C CD2 . TYR A 559 ? 0.2584 0.2690 0.2745 0.0315 -0.0545 -0.0407 600 TYR A CD2 4596 C CE1 . TYR A 559 ? 0.2636 0.2827 0.2986 0.0201 -0.0446 -0.0358 600 TYR A CE1 4597 C CE2 . TYR A 559 ? 0.2472 0.2609 0.2608 0.0292 -0.0474 -0.0364 600 TYR A CE2 4598 C CZ . TYR A 559 ? 0.2632 0.2810 0.2861 0.0236 -0.0429 -0.0343 600 TYR A CZ 4599 O OH . TYR A 559 ? 0.2555 0.2757 0.2750 0.0218 -0.0366 -0.0306 600 TYR A OH 4600 N N . ALA A 560 ? 0.2412 0.2489 0.3044 0.0260 -0.0784 -0.0573 601 ALA A N 4601 C CA . ALA A 560 ? 0.2437 0.2504 0.3208 0.0215 -0.0801 -0.0587 601 ALA A CA 4602 C C . ALA A 560 ? 0.2482 0.2612 0.3455 0.0168 -0.0798 -0.0595 601 ALA A C 4603 O O . ALA A 560 ? 0.2501 0.2648 0.3587 0.0108 -0.0748 -0.0568 601 ALA A O 4604 C CB . ALA A 560 ? 0.2479 0.2480 0.3223 0.0255 -0.0894 -0.0645 601 ALA A CB 4605 N N . VAL A 561 ? 0.2536 0.2701 0.3555 0.0196 -0.0847 -0.0631 602 VAL A N 4606 C CA . VAL A 561 ? 0.2537 0.2771 0.3755 0.0159 -0.0845 -0.0643 602 VAL A CA 4607 C C . VAL A 561 ? 0.2476 0.2764 0.3733 0.0108 -0.0735 -0.0584 602 VAL A C 4608 O O . VAL A 561 ? 0.2628 0.2946 0.4039 0.0051 -0.0695 -0.0571 602 VAL A O 4609 C CB . VAL A 561 ? 0.2702 0.2962 0.3934 0.0209 -0.0915 -0.0687 602 VAL A CB 4610 C CG1 . VAL A 561 ? 0.3006 0.3351 0.4462 0.0170 -0.0904 -0.0698 602 VAL A CG1 4611 C CG2 . VAL A 561 ? 0.3227 0.3431 0.4443 0.0251 -0.1028 -0.0751 602 VAL A CG2 4612 N N . VAL A 562 ? 0.2285 0.2578 0.3400 0.0129 -0.0684 -0.0548 603 VAL A N 4613 C CA . VAL A 562 ? 0.2258 0.2599 0.3397 0.0087 -0.0585 -0.0498 603 VAL A CA 4614 C C . VAL A 562 ? 0.2241 0.2557 0.3364 0.0040 -0.0520 -0.0453 603 VAL A C 4615 O O . VAL A 562 ? 0.2205 0.2559 0.3413 -0.0008 -0.0451 -0.0422 603 VAL A O 4616 C CB . VAL A 562 ? 0.2395 0.2753 0.3412 0.0117 -0.0549 -0.0475 603 VAL A CB 4617 C CG1 . VAL A 562 ? 0.2613 0.2992 0.3654 0.0166 -0.0615 -0.0518 603 VAL A CG1 4618 C CG2 . VAL A 562 ? 0.2714 0.3020 0.3543 0.0142 -0.0531 -0.0448 603 VAL A CG2 4619 N N . LEU A 563 ? 0.2094 0.2347 0.3112 0.0055 -0.0543 -0.0449 604 LEU A N 4620 C CA . LEU A 563 ? 0.2170 0.2393 0.3162 0.0016 -0.0486 -0.0404 604 LEU A CA 4621 C C . LEU A 563 ? 0.2165 0.2396 0.3335 -0.0037 -0.0478 -0.0405 604 LEU A C 4622 O O . LEU A 563 ? 0.2334 0.2568 0.3529 -0.0083 -0.0405 -0.0358 604 LEU A O 4623 C CB . LEU A 563 ? 0.2075 0.2228 0.2936 0.0046 -0.0518 -0.0405 604 LEU A CB 4624 C CG . LEU A 563 ? 0.2152 0.2295 0.2837 0.0087 -0.0499 -0.0386 604 LEU A CG 4625 C CD1 . LEU A 563 ? 0.2448 0.2528 0.3030 0.0125 -0.0541 -0.0401 604 LEU A CD1 4626 C CD2 . LEU A 563 ? 0.2319 0.2483 0.2955 0.0056 -0.0412 -0.0328 604 LEU A CD2 4627 N N . ARG A 564 ? 0.2255 0.2487 0.3550 -0.0032 -0.0552 -0.0458 605 ARG A N 4628 C CA . ARG A 564 ? 0.2242 0.2485 0.3732 -0.0086 -0.0543 -0.0461 605 ARG A CA 4629 C C . ARG A 564 ? 0.2149 0.2470 0.3762 -0.0124 -0.0472 -0.0439 605 ARG A C 4630 O O . ARG A 564 ? 0.2124 0.2449 0.3822 -0.0177 -0.0402 -0.0399 605 ARG A O 4631 C CB . ARG A 564 ? 0.2281 0.2510 0.3888 -0.0070 -0.0648 -0.0530 605 ARG A CB 4632 C CG . ARG A 564 ? 0.2674 0.2922 0.4514 -0.0129 -0.0641 -0.0537 605 ARG A CG 4633 C CD . ARG A 564 ? 0.3120 0.3312 0.4959 -0.0177 -0.0581 -0.0485 605 ARG A CD 4634 N NE . ARG A 564 ? 0.3628 0.3838 0.5700 -0.0236 -0.0566 -0.0487 605 ARG A NE 4635 C CZ . ARG A 564 ? 0.4276 0.4448 0.6474 -0.0246 -0.0641 -0.0532 605 ARG A CZ 4636 N NH1 . ARG A 564 ? 0.4153 0.4266 0.6253 -0.0196 -0.0737 -0.0582 605 ARG A NH1 4637 N NH2 . ARG A 564 ? 0.4610 0.4803 0.7037 -0.0304 -0.0619 -0.0531 605 ARG A NH2 4638 N N A LYS A 565 ? 0.2133 0.2509 0.3752 -0.0094 -0.0487 -0.0463 606 LYS A N 4639 N N B LYS A 565 ? 0.2108 0.2484 0.3725 -0.0095 -0.0483 -0.0461 606 LYS A N 4640 C CA A LYS A 565 ? 0.2202 0.2651 0.3912 -0.0120 -0.0415 -0.0444 606 LYS A CA 4641 C CA B LYS A 565 ? 0.2091 0.2541 0.3817 -0.0126 -0.0410 -0.0441 606 LYS A CA 4642 C C A LYS A 565 ? 0.2148 0.2592 0.3763 -0.0151 -0.0307 -0.0376 606 LYS A C 4643 C C B LYS A 565 ? 0.2074 0.2520 0.3689 -0.0151 -0.0303 -0.0375 606 LYS A C 4644 O O A LYS A 565 ? 0.2066 0.2540 0.3789 -0.0198 -0.0232 -0.0347 606 LYS A O 4645 O O B LYS A 565 ? 0.2046 0.2528 0.3760 -0.0195 -0.0225 -0.0346 606 LYS A O 4646 C CB A LYS A 565 ? 0.2340 0.2830 0.4009 -0.0070 -0.0450 -0.0474 606 LYS A CB 4647 C CB B LYS A 565 ? 0.2145 0.2651 0.3896 -0.0085 -0.0449 -0.0480 606 LYS A CB 4648 C CG A LYS A 565 ? 0.2634 0.3204 0.4420 -0.0088 -0.0389 -0.0467 606 LYS A CG 4649 C CG B LYS A 565 ? 0.2116 0.2615 0.3933 -0.0047 -0.0566 -0.0546 606 LYS A CG 4650 C CD A LYS A 565 ? 0.3254 0.3857 0.5013 -0.0033 -0.0439 -0.0502 606 LYS A CD 4651 C CD B LYS A 565 ? 0.2916 0.3486 0.4851 -0.0025 -0.0597 -0.0584 606 LYS A CD 4652 C CE A LYS A 565 ? 0.3318 0.3879 0.4846 0.0007 -0.0431 -0.0479 606 LYS A CE 4653 C CE B LYS A 565 ? 0.2888 0.3460 0.4656 0.0026 -0.0590 -0.0574 606 LYS A CE 4654 N NZ A LYS A 565 ? 0.3608 0.4202 0.5113 0.0051 -0.0448 -0.0496 606 LYS A NZ 4655 N NZ B LYS A 565 ? 0.3059 0.3569 0.4663 0.0089 -0.0678 -0.0600 606 LYS A NZ 4656 N N . TYR A 566 ? 0.2054 0.2457 0.3470 -0.0122 -0.0300 -0.0353 607 TYR A N 4657 C CA . TYR A 566 ? 0.1987 0.2382 0.3292 -0.0142 -0.0210 -0.0296 607 TYR A CA 4658 C C . TYR A 566 ? 0.1998 0.2347 0.3323 -0.0187 -0.0170 -0.0256 607 TYR A C 4659 O O . TYR A 566 ? 0.2059 0.2418 0.3383 -0.0221 -0.0086 -0.0211 607 TYR A O 4660 C CB . TYR A 566 ? 0.1986 0.2348 0.3092 -0.0102 -0.0221 -0.0285 607 TYR A CB 4661 C CG . TYR A 566 ? 0.1945 0.2340 0.3008 -0.0057 -0.0252 -0.0314 607 TYR A CG 4662 C CD1 . TYR A 566 ? 0.1885 0.2340 0.3061 -0.0057 -0.0246 -0.0337 607 TYR A CD1 4663 C CD2 . TYR A 566 ? 0.2124 0.2484 0.3035 -0.0012 -0.0286 -0.0318 607 TYR A CD2 4664 C CE1 . TYR A 566 ? 0.2084 0.2560 0.3214 -0.0012 -0.0278 -0.0361 607 TYR A CE1 4665 C CE2 . TYR A 566 ? 0.2130 0.2509 0.2992 0.0029 -0.0309 -0.0338 607 TYR A CE2 4666 C CZ . TYR A 566 ? 0.2597 0.3031 0.3567 0.0030 -0.0307 -0.0359 607 TYR A CZ 4667 O OH . TYR A 566 ? 0.2752 0.3198 0.3674 0.0074 -0.0334 -0.0377 607 TYR A OH 4668 N N . ALA A 567 ? 0.1987 0.2285 0.3333 -0.0185 -0.0229 -0.0272 608 ALA A N 4669 C CA . ALA A 567 ? 0.2152 0.2398 0.3524 -0.0226 -0.0196 -0.0233 608 ALA A CA 4670 C C . ALA A 567 ? 0.2233 0.2515 0.3800 -0.0279 -0.0146 -0.0223 608 ALA A C 4671 O O . ALA A 567 ? 0.2429 0.2692 0.3997 -0.0318 -0.0067 -0.0169 608 ALA A O 4672 C CB . ALA A 567 ? 0.2207 0.2387 0.3574 -0.0209 -0.0276 -0.0261 608 ALA A CB 4673 N N . ASP A 568 ? 0.2271 0.2602 0.4009 -0.0279 -0.0193 -0.0274 609 ASP A N 4674 C CA . ASP A 568 ? 0.2361 0.2740 0.4313 -0.0329 -0.0143 -0.0269 609 ASP A CA 4675 C C . ASP A 568 ? 0.2264 0.2693 0.4190 -0.0348 -0.0032 -0.0225 609 ASP A C 4676 O O . ASP A 568 ? 0.2200 0.2631 0.4207 -0.0395 0.0052 -0.0182 609 ASP A O 4677 C CB . ASP A 568 ? 0.2459 0.2898 0.4588 -0.0315 -0.0220 -0.0339 609 ASP A CB 4678 C CG . ASP A 568 ? 0.3135 0.3528 0.5342 -0.0308 -0.0324 -0.0389 609 ASP A CG 4679 O OD1 . ASP A 568 ? 0.3586 0.3909 0.5772 -0.0329 -0.0324 -0.0367 609 ASP A OD1 4680 O OD2 . ASP A 568 ? 0.3837 0.4264 0.6135 -0.0279 -0.0411 -0.0454 609 ASP A OD2 4681 N N . LYS A 569 ? 0.2095 0.2555 0.3900 -0.0309 -0.0031 -0.0234 610 LYS A N 4682 C CA . LYS A 569 ? 0.2243 0.2750 0.4024 -0.0318 0.0063 -0.0204 610 LYS A CA 4683 C C . LYS A 569 ? 0.2167 0.2619 0.3800 -0.0340 0.0144 -0.0137 610 LYS A C 4684 O O . LYS A 569 ? 0.2348 0.2817 0.4021 -0.0373 0.0238 -0.0099 610 LYS A O 4685 C CB . LYS A 569 ? 0.2258 0.2797 0.3933 -0.0268 0.0034 -0.0232 610 LYS A CB 4686 C CG . LYS A 569 ? 0.2690 0.3272 0.4328 -0.0273 0.0124 -0.0209 610 LYS A CG 4687 C CD . LYS A 569 ? 0.3270 0.3873 0.4808 -0.0223 0.0087 -0.0237 610 LYS A CD 4688 C CE . LYS A 569 ? 0.3952 0.4621 0.5540 -0.0222 0.0152 -0.0242 610 LYS A CE 4689 N NZ . LYS A 569 ? 0.4432 0.5098 0.5876 -0.0177 0.0129 -0.0255 610 LYS A NZ 4690 N N . ILE A 570 ? 0.2136 0.2522 0.3597 -0.0317 0.0106 -0.0123 611 ILE A N 4691 C CA . ILE A 570 ? 0.2170 0.2502 0.3481 -0.0330 0.0172 -0.0061 611 ILE A CA 4692 C C . ILE A 570 ? 0.2177 0.2462 0.3571 -0.0379 0.0216 -0.0018 611 ILE A C 4693 O O . ILE A 570 ? 0.2233 0.2500 0.3577 -0.0404 0.0306 0.0037 611 ILE A O 4694 C CB . ILE A 570 ? 0.2258 0.2539 0.3374 -0.0292 0.0122 -0.0058 611 ILE A CB 4695 C CG1 . ILE A 570 ? 0.2635 0.2874 0.3592 -0.0298 0.0186 -0.0001 611 ILE A CG1 4696 C CG2 . ILE A 570 ? 0.2437 0.2662 0.3566 -0.0284 0.0045 -0.0073 611 ILE A CG2 4697 C CD1 . ILE A 570 ? 0.2814 0.3099 0.3710 -0.0293 0.0250 0.0006 611 ILE A CD1 4698 N N . TYR A 571 ? 0.2207 0.2472 0.3731 -0.0391 0.0157 -0.0042 612 TYR A N 4699 C CA . TYR A 571 ? 0.2511 0.2735 0.4149 -0.0440 0.0195 -0.0007 612 TYR A CA 4700 C C . TYR A 571 ? 0.2456 0.2737 0.4241 -0.0482 0.0292 0.0014 612 TYR A C 4701 O O . TYR A 571 ? 0.2445 0.2690 0.4230 -0.0519 0.0379 0.0075 612 TYR A O 4702 C CB . TYR A 571 ? 0.2434 0.2639 0.4215 -0.0443 0.0100 -0.0055 612 TYR A CB 4703 C CG . TYR A 571 ? 0.3065 0.3239 0.5016 -0.0499 0.0138 -0.0027 612 TYR A CG 4704 C CD1 . TYR A 571 ? 0.3506 0.3586 0.5383 -0.0519 0.0165 0.0029 612 TYR A CD1 4705 C CD2 . TYR A 571 ? 0.3599 0.3838 0.5791 -0.0532 0.0151 -0.0054 612 TYR A CD2 4706 C CE1 . TYR A 571 ? 0.4166 0.4211 0.6207 -0.0573 0.0205 0.0060 612 TYR A CE1 4707 C CE2 . TYR A 571 ? 0.4049 0.4262 0.6418 -0.0589 0.0193 -0.0026 612 TYR A CE2 4708 C CZ . TYR A 571 ? 0.4424 0.4537 0.6710 -0.0609 0.0222 0.0033 612 TYR A CZ 4709 O OH . TYR A 571 ? 0.5569 0.5651 0.8037 -0.0667 0.0268 0.0064 612 TYR A OH 4710 N N . SER A 572 ? 0.2413 0.2783 0.4321 -0.0472 0.0280 -0.0035 613 SER A N 4711 C CA . SER A 572 ? 0.2588 0.3023 0.4662 -0.0509 0.0369 -0.0023 613 SER A CA 4712 C C . SER A 572 ? 0.2630 0.3064 0.4557 -0.0510 0.0481 0.0032 613 SER A C 4713 O O . SER A 572 ? 0.2824 0.3268 0.4831 -0.0549 0.0583 0.0073 613 SER A O 4714 C CB . SER A 572 ? 0.2556 0.3087 0.4795 -0.0491 0.0321 -0.0092 613 SER A CB 4715 O OG A SER A 572 ? 0.2796 0.3325 0.5204 -0.0501 0.0232 -0.0137 613 SER A OG 4716 O OG B SER A 572 ? 0.2935 0.3504 0.5045 -0.0449 0.0323 -0.0108 613 SER A OG 4717 N N . ILE A 573 ? 0.2606 0.3026 0.4319 -0.0468 0.0464 0.0030 614 ILE A N 4718 C CA . ILE A 573 ? 0.2563 0.2970 0.4115 -0.0465 0.0557 0.0077 614 ILE A CA 4719 C C . ILE A 573 ? 0.2739 0.3057 0.4195 -0.0492 0.0614 0.0149 614 ILE A C 4720 O O . ILE A 573 ? 0.2822 0.3132 0.4258 -0.0516 0.0722 0.0198 614 ILE A O 4721 C CB . ILE A 573 ? 0.2586 0.2990 0.3936 -0.0414 0.0512 0.0056 614 ILE A CB 4722 C CG1 . ILE A 573 ? 0.2529 0.3020 0.3969 -0.0388 0.0483 -0.0004 614 ILE A CG1 4723 C CG2 . ILE A 573 ? 0.2904 0.3269 0.4056 -0.0409 0.0591 0.0106 614 ILE A CG2 4724 C CD1 . ILE A 573 ? 0.2553 0.3040 0.3830 -0.0339 0.0421 -0.0032 614 ILE A CD1 4725 N N . SER A 574 ? 0.2603 0.2850 0.3999 -0.0487 0.0544 0.0157 615 SER A N 4726 C CA . SER A 574 ? 0.2718 0.2871 0.4020 -0.0508 0.0585 0.0226 615 SER A CA 4727 C C . SER A 574 ? 0.2920 0.3065 0.4397 -0.0563 0.0662 0.0263 615 SER A C 4728 O O . SER A 574 ? 0.2972 0.3062 0.4375 -0.0585 0.0753 0.0333 615 SER A O 4729 C CB . SER A 574 ? 0.2776 0.2862 0.4012 -0.0489 0.0486 0.0217 615 SER A CB 4730 O OG . SER A 574 ? 0.3006 0.2997 0.4117 -0.0499 0.0519 0.0284 615 SER A OG 4731 N N . MET A 575 ? 0.2764 0.2962 0.4475 -0.0583 0.0624 0.0218 616 MET A N 4732 C CA . MET A 575 ? 0.3085 0.3281 0.5005 -0.0640 0.0688 0.0246 616 MET A CA 4733 C C . MET A 575 ? 0.3245 0.3494 0.5232 -0.0666 0.0820 0.0279 616 MET A C 4734 O O . MET A 575 ? 0.3396 0.3643 0.5554 -0.0715 0.0893 0.0313 616 MET A O 4735 C CB . MET A 575 ? 0.3074 0.3309 0.5232 -0.0653 0.0600 0.0182 616 MET A CB 4736 C CG . MET A 575 ? 0.3553 0.3701 0.5682 -0.0650 0.0508 0.0178 616 MET A CG 4737 S SD . MET A 575 ? 0.4931 0.4961 0.7053 -0.0700 0.0586 0.0272 616 MET A SD 4738 C CE . MET A 575 ? 0.4321 0.4406 0.6768 -0.0767 0.0664 0.0277 616 MET A CE 4739 N N . LYS A 576 ? 0.3388 0.3680 0.5241 -0.0633 0.0856 0.0271 617 LYS A N 4740 C CA . LYS A 576 ? 0.3546 0.3866 0.5400 -0.0651 0.0994 0.0312 617 LYS A CA 4741 C C . LYS A 576 ? 0.3543 0.3759 0.5226 -0.0667 0.1083 0.0403 617 LYS A C 4742 O O . LYS A 576 ? 0.3573 0.3794 0.5268 -0.0689 0.1209 0.0450 617 LYS A O 4743 C CB . LYS A 576 ? 0.3769 0.4153 0.5512 -0.0608 0.1008 0.0278 617 LYS A CB 4744 C CG . LYS A 576 ? 0.4225 0.4707 0.6110 -0.0585 0.0926 0.0193 617 LYS A CG 4745 C CD . LYS A 576 ? 0.5424 0.5996 0.7605 -0.0618 0.0968 0.0168 617 LYS A CD 4746 C CE . LYS A 576 ? 0.5765 0.6427 0.8070 -0.0587 0.0873 0.0082 617 LYS A CE 4747 N NZ . LYS A 576 ? 0.6281 0.7033 0.8891 -0.0618 0.0903 0.0054 617 LYS A NZ 4748 N N . HIS A 577 ? 0.3227 0.3347 0.4763 -0.0655 0.1019 0.0429 618 HIS A N 4749 C CA . HIS A 577 ? 0.3329 0.3337 0.4675 -0.0661 0.1083 0.0515 618 HIS A CA 4750 C C . HIS A 577 ? 0.3411 0.3333 0.4832 -0.0692 0.1048 0.0550 618 HIS A C 4751 O O . HIS A 577 ? 0.3383 0.3221 0.4642 -0.0669 0.0985 0.0569 618 HIS A O 4752 C CB . HIS A 577 ? 0.3363 0.3327 0.4426 -0.0608 0.1031 0.0515 618 HIS A CB 4753 C CG . HIS A 577 ? 0.3781 0.3825 0.4773 -0.0572 0.1033 0.0465 618 HIS A CG 4754 N ND1 . HIS A 577 ? 0.4136 0.4183 0.5005 -0.0563 0.1135 0.0494 618 HIS A ND1 4755 C CD2 . HIS A 577 ? 0.4070 0.4185 0.5090 -0.0541 0.0946 0.0390 618 HIS A CD2 4756 C CE1 . HIS A 577 ? 0.4078 0.4197 0.4913 -0.0530 0.1109 0.0436 618 HIS A CE1 4757 N NE2 . HIS A 577 ? 0.4202 0.4363 0.5130 -0.0517 0.0996 0.0375 618 HIS A NE2 4758 N N . PRO A 578 ? 0.3402 0.3345 0.5078 -0.0744 0.1085 0.0555 619 PRO A N 4759 C CA . PRO A 578 ? 0.3436 0.3301 0.5204 -0.0772 0.1034 0.0573 619 PRO A CA 4760 C C . PRO A 578 ? 0.3615 0.3346 0.5205 -0.0778 0.1088 0.0668 619 PRO A C 4761 O O . PRO A 578 ? 0.3640 0.3290 0.5183 -0.0770 0.1008 0.0674 619 PRO A O 4762 C CB . PRO A 578 ? 0.3561 0.3481 0.5647 -0.0829 0.1081 0.0564 619 PRO A CB 4763 C CG . PRO A 578 ? 0.3634 0.3641 0.5756 -0.0835 0.1199 0.0571 619 PRO A CG 4764 C CD . PRO A 578 ? 0.3406 0.3452 0.5318 -0.0776 0.1157 0.0531 619 PRO A CD 4765 N N . GLN A 579 ? 0.3676 0.3379 0.5162 -0.0788 0.1219 0.0740 620 GLN A N 4766 C CA A GLN A 579 ? 0.3816 0.3382 0.5122 -0.0791 0.1267 0.0835 620 GLN A CA 4767 C CA B GLN A 579 ? 0.3906 0.3475 0.5197 -0.0789 0.1274 0.0837 620 GLN A CA 4768 C C . GLN A 579 ? 0.3787 0.3292 0.4822 -0.0732 0.1173 0.0830 620 GLN A C 4769 O O . GLN A 579 ? 0.3871 0.3268 0.4823 -0.0729 0.1136 0.0873 620 GLN A O 4770 C CB A GLN A 579 ? 0.4031 0.3570 0.5262 -0.0809 0.1430 0.0916 620 GLN A CB 4771 C CB B GLN A 579 ? 0.4110 0.3672 0.5285 -0.0793 0.1426 0.0901 620 GLN A CB 4772 C CG A GLN A 579 ? 0.4328 0.3715 0.5407 -0.0820 0.1495 0.1026 620 GLN A CG 4773 C CG B GLN A 579 ? 0.4836 0.4259 0.5757 -0.0780 0.1488 0.1002 620 GLN A CG 4774 C CD A GLN A 579 ? 0.4413 0.3725 0.5657 -0.0861 0.1452 0.1049 620 GLN A CD 4775 C CD B GLN A 579 ? 0.5727 0.5136 0.6590 -0.0797 0.1658 0.1074 620 GLN A CD 4776 O OE1 A GLN A 579 ? 0.4802 0.4129 0.6294 -0.0919 0.1517 0.1067 620 GLN A OE1 4777 O OE1 B GLN A 579 ? 0.6083 0.5596 0.7085 -0.0813 0.1731 0.1044 620 GLN A OE1 4778 N NE2 A GLN A 579 ? 0.3655 0.2883 0.4765 -0.0830 0.1346 0.1050 620 GLN A NE2 4779 N NE2 B GLN A 579 ? 0.6027 0.5305 0.6683 -0.0790 0.1722 0.1170 620 GLN A NE2 4780 N N . GLU A 580 ? 0.3605 0.3178 0.4516 -0.0687 0.1131 0.0776 621 GLU A N 4781 C CA . GLU A 580 ? 0.3495 0.3018 0.4172 -0.0634 0.1042 0.0768 621 GLU A CA 4782 C C . GLU A 580 ? 0.3358 0.2876 0.4120 -0.0624 0.0910 0.0716 621 GLU A C 4783 O O . GLU A 580 ? 0.3492 0.2931 0.4112 -0.0596 0.0844 0.0733 621 GLU A O 4784 C CB . GLU A 580 ? 0.3689 0.3286 0.4227 -0.0590 0.1033 0.0722 621 GLU A CB 4785 C CG . GLU A 580 ? 0.4270 0.3848 0.4649 -0.0585 0.1154 0.0776 621 GLU A CG 4786 C CD . GLU A 580 ? 0.4901 0.4539 0.5451 -0.0626 0.1275 0.0788 621 GLU A CD 4787 O OE1 . GLU A 580 ? 0.4962 0.4695 0.5751 -0.0650 0.1260 0.0732 621 GLU A OE1 4788 O OE2 . GLU A 580 ? 0.5920 0.5506 0.6362 -0.0634 0.1391 0.0857 621 GLU A OE2 4789 N N . MET A 581 ? 0.3130 0.2732 0.4114 -0.0642 0.0865 0.0647 622 MET A N 4790 C CA . MET A 581 ? 0.3070 0.2662 0.4128 -0.0629 0.0741 0.0594 622 MET A CA 4791 C C . MET A 581 ? 0.3236 0.2715 0.4341 -0.0657 0.0737 0.0646 622 MET A C 4792 O O . MET A 581 ? 0.3241 0.2666 0.4290 -0.0632 0.0646 0.0632 622 MET A O 4793 C CB . MET A 581 ? 0.2985 0.2682 0.4265 -0.0640 0.0691 0.0510 622 MET A CB 4794 C CG . MET A 581 ? 0.2991 0.2787 0.4209 -0.0603 0.0671 0.0452 622 MET A CG 4795 S SD . MET A 581 ? 0.3140 0.3047 0.4609 -0.0607 0.0597 0.0354 622 MET A SD 4796 C CE . MET A 581 ? 0.2856 0.2709 0.4331 -0.0583 0.0454 0.0307 622 MET A CE 4797 N N . LYS A 582 ? 0.3352 0.2796 0.4561 -0.0708 0.0839 0.0708 623 LYS A N 4798 C CA . LYS A 582 ? 0.3599 0.2925 0.4850 -0.0738 0.0850 0.0771 623 LYS A CA 4799 C C . LYS A 582 ? 0.3812 0.3024 0.4792 -0.0703 0.0855 0.0841 623 LYS A C 4800 O O . LYS A 582 ? 0.3836 0.2963 0.4770 -0.0687 0.0779 0.0849 623 LYS A O 4801 C CB . LYS A 582 ? 0.3703 0.3021 0.5131 -0.0802 0.0973 0.0827 623 LYS A CB 4802 C CG . LYS A 582 ? 0.3498 0.2917 0.5222 -0.0839 0.0956 0.0757 623 LYS A CG 4803 C CD . LYS A 582 ? 0.4234 0.3654 0.6158 -0.0904 0.1081 0.0811 623 LYS A CD 4804 C CE . LYS A 582 ? 0.4700 0.4239 0.6913 -0.0930 0.1041 0.0725 623 LYS A CE 4805 N NZ . LYS A 582 ? 0.5449 0.5047 0.7861 -0.0983 0.1167 0.0754 623 LYS A NZ 4806 N N . THR A 583 ? 0.3843 0.3057 0.4643 -0.0687 0.0938 0.0887 624 THR A N 4807 C CA . THR A 583 ? 0.4240 0.3346 0.4774 -0.0654 0.0954 0.0959 624 THR A CA 4808 C C . THR A 583 ? 0.4104 0.3195 0.4494 -0.0598 0.0829 0.0919 624 THR A C 4809 O O . THR A 583 ? 0.4214 0.3197 0.4490 -0.0578 0.0791 0.0963 624 THR A O 4810 C CB . THR A 583 ? 0.4370 0.3496 0.4738 -0.0642 0.1058 0.0997 624 THR A CB 4811 O OG1 . THR A 583 ? 0.4771 0.3886 0.5256 -0.0693 0.1189 0.1055 624 THR A OG1 4812 C CG2 . THR A 583 ? 0.4996 0.4015 0.5065 -0.0596 0.1054 0.1060 624 THR A CG2 4813 N N . TYR A 584 ? 0.3855 0.3053 0.4257 -0.0570 0.0767 0.0834 625 TYR A N 4814 C CA . TYR A 584 ? 0.3740 0.2940 0.4013 -0.0516 0.0657 0.0791 625 TYR A CA 4815 C C . TYR A 584 ? 0.3596 0.2820 0.4015 -0.0511 0.0550 0.0721 625 TYR A C 4816 O O . TYR A 584 ? 0.3651 0.2891 0.3985 -0.0467 0.0464 0.0678 625 TYR A O 4817 C CB . TYR A 584 ? 0.3751 0.3034 0.3893 -0.0481 0.0655 0.0752 625 TYR A CB 4818 C CG . TYR A 584 ? 0.4002 0.3247 0.3976 -0.0478 0.0753 0.0818 625 TYR A CG 4819 C CD1 . TYR A 584 ? 0.4561 0.3696 0.4332 -0.0453 0.0754 0.0885 625 TYR A CD1 4820 C CD2 . TYR A 584 ? 0.4380 0.3693 0.4395 -0.0499 0.0845 0.0814 625 TYR A CD2 4821 C CE1 . TYR A 584 ? 0.4909 0.3997 0.4507 -0.0448 0.0845 0.0949 625 TYR A CE1 4822 C CE2 . TYR A 584 ? 0.4789 0.4062 0.4638 -0.0494 0.0941 0.0874 625 TYR A CE2 4823 C CZ . TYR A 584 ? 0.5204 0.4362 0.4837 -0.0467 0.0939 0.0941 625 TYR A CZ 4824 O OH . TYR A 584 ? 0.5674 0.4780 0.5126 -0.0458 0.1033 0.1001 625 TYR A OH 4825 N N . SER A 585 ? 0.3473 0.2695 0.4108 -0.0556 0.0558 0.0712 626 SER A N 4826 C CA . SER A 585 ? 0.3455 0.2685 0.4229 -0.0551 0.0457 0.0645 626 SER A CA 4827 C C . SER A 585 ? 0.3263 0.2601 0.4034 -0.0514 0.0384 0.0555 626 SER A C 4828 O O . SER A 585 ? 0.3398 0.2730 0.4111 -0.0473 0.0293 0.0513 626 SER A O 4829 C CB A SER A 585 ? 0.3530 0.2647 0.4217 -0.0527 0.0396 0.0674 626 SER A CB 4830 C CB B SER A 585 ? 0.3580 0.2699 0.4268 -0.0527 0.0395 0.0672 626 SER A CB 4831 O OG A SER A 585 ? 0.3521 0.2533 0.4233 -0.0564 0.0460 0.0756 626 SER A OG 4832 O OG B SER A 585 ? 0.3965 0.3092 0.4782 -0.0520 0.0302 0.0603 626 SER A OG 4833 N N . VAL A 586 ? 0.3114 0.2549 0.3944 -0.0527 0.0429 0.0528 627 VAL A N 4834 C CA . VAL A 586 ? 0.3008 0.2542 0.3824 -0.0492 0.0373 0.0452 627 VAL A CA 4835 C C . VAL A 586 ? 0.3073 0.2653 0.4095 -0.0503 0.0309 0.0381 627 VAL A C 4836 O O . VAL A 586 ? 0.3267 0.2887 0.4469 -0.0544 0.0348 0.0373 627 VAL A O 4837 C CB . VAL A 586 ? 0.2969 0.2582 0.3752 -0.0496 0.0450 0.0455 627 VAL A CB 4838 C CG1 . VAL A 586 ? 0.2869 0.2577 0.3636 -0.0459 0.0391 0.0379 627 VAL A CG1 4839 C CG2 . VAL A 586 ? 0.3156 0.2712 0.3737 -0.0487 0.0519 0.0528 627 VAL A CG2 4840 N N . SER A 587 ? 0.3186 0.2750 0.4183 -0.0468 0.0211 0.0333 628 SER A N 4841 C CA . SER A 587 ? 0.3136 0.2731 0.4303 -0.0470 0.0136 0.0260 628 SER A CA 4842 C C . SER A 587 ? 0.2885 0.2557 0.4006 -0.0424 0.0073 0.0190 628 SER A C 4843 O O . SER A 587 ? 0.2921 0.2587 0.3875 -0.0380 0.0045 0.0188 628 SER A O 4844 C CB . SER A 587 ? 0.3448 0.2950 0.4630 -0.0462 0.0070 0.0256 628 SER A CB 4845 O OG . SER A 587 ? 0.3962 0.3491 0.5304 -0.0463 -0.0002 0.0182 628 SER A OG 4846 N N . PHE A 588 ? 0.2837 0.2579 0.4110 -0.0433 0.0048 0.0132 629 PHE A N 4847 C CA . PHE A 588 ? 0.2687 0.2492 0.3925 -0.0388 -0.0020 0.0064 629 PHE A CA 4848 C C . PHE A 588 ? 0.2650 0.2420 0.3943 -0.0364 -0.0121 0.0005 629 PHE A C 4849 O O . PHE A 588 ? 0.2530 0.2342 0.3806 -0.0325 -0.0183 -0.0055 629 PHE A O 4850 C CB . PHE A 588 ? 0.2554 0.2458 0.3907 -0.0401 0.0007 0.0033 629 PHE A CB 4851 C CG . PHE A 588 ? 0.2519 0.2465 0.3771 -0.0402 0.0088 0.0071 629 PHE A CG 4852 C CD1 . PHE A 588 ? 0.2545 0.2542 0.3685 -0.0360 0.0069 0.0044 629 PHE A CD1 4853 C CD2 . PHE A 588 ? 0.2835 0.2764 0.4100 -0.0443 0.0187 0.0136 629 PHE A CD2 4854 C CE1 . PHE A 588 ? 0.2664 0.2694 0.3709 -0.0360 0.0140 0.0074 629 PHE A CE1 4855 C CE2 . PHE A 588 ? 0.2731 0.2694 0.3890 -0.0439 0.0259 0.0166 629 PHE A CE2 4856 C CZ . PHE A 588 ? 0.2686 0.2700 0.3736 -0.0397 0.0231 0.0132 629 PHE A CZ 4857 N N . ASP A 589 ? 0.2795 0.2484 0.4144 -0.0385 -0.0135 0.0023 630 ASP A N 4858 C CA . ASP A 589 ? 0.2924 0.2570 0.4332 -0.0363 -0.0232 -0.0038 630 ASP A CA 4859 C C . ASP A 589 ? 0.2743 0.2388 0.3993 -0.0297 -0.0297 -0.0078 630 ASP A C 4860 O O . ASP A 589 ? 0.2727 0.2387 0.4012 -0.0265 -0.0375 -0.0150 630 ASP A O 4861 C CB . ASP A 589 ? 0.3134 0.2678 0.4603 -0.0392 -0.0234 -0.0006 630 ASP A CB 4862 C CG . ASP A 589 ? 0.3887 0.3431 0.5566 -0.0458 -0.0189 0.0013 630 ASP A CG 4863 O OD1 . ASP A 589 ? 0.4047 0.3674 0.5838 -0.0482 -0.0158 -0.0001 630 ASP A OD1 4864 O OD2 . ASP A 589 ? 0.4450 0.3907 0.6189 -0.0486 -0.0184 0.0045 630 ASP A OD2 4865 N N . SER A 590 ? 0.2681 0.2310 0.3760 -0.0273 -0.0267 -0.0035 631 SER A N 4866 C CA . SER A 590 ? 0.2502 0.2133 0.3448 -0.0213 -0.0321 -0.0070 631 SER A CA 4867 C C . SER A 590 ? 0.2393 0.2109 0.3322 -0.0186 -0.0338 -0.0117 631 SER A C 4868 O O . SER A 590 ? 0.2337 0.2053 0.3220 -0.0140 -0.0400 -0.0169 631 SER A O 4869 C CB . SER A 590 ? 0.2703 0.2306 0.3485 -0.0193 -0.0290 -0.0018 631 SER A CB 4870 O OG . SER A 590 ? 0.2996 0.2649 0.3730 -0.0213 -0.0218 0.0026 631 SER A OG 4871 N N . LEU A 591 ? 0.2357 0.2138 0.3314 -0.0211 -0.0282 -0.0098 632 LEU A N 4872 C CA . LEU A 591 ? 0.2277 0.2133 0.3214 -0.0184 -0.0296 -0.0137 632 LEU A CA 4873 C C . LEU A 591 ? 0.2337 0.2213 0.3408 -0.0179 -0.0361 -0.0204 632 LEU A C 4874 O O . LEU A 591 ? 0.2195 0.2090 0.3218 -0.0134 -0.0416 -0.0252 632 LEU A O 4875 C CB . LEU A 591 ? 0.2400 0.2318 0.3337 -0.0210 -0.0218 -0.0101 632 LEU A CB 4876 C CG . LEU A 591 ? 0.2357 0.2351 0.3287 -0.0185 -0.0229 -0.0140 632 LEU A CG 4877 C CD1 . LEU A 591 ? 0.2250 0.2242 0.3024 -0.0132 -0.0259 -0.0153 632 LEU A CD1 4878 C CD2 . LEU A 591 ? 0.2402 0.2446 0.3338 -0.0213 -0.0147 -0.0103 632 LEU A CD2 4879 N N . PHE A 592 ? 0.2263 0.2130 0.3500 -0.0223 -0.0358 -0.0206 633 PHE A N 4880 C CA . PHE A 592 ? 0.2407 0.2290 0.3780 -0.0217 -0.0432 -0.0275 633 PHE A CA 4881 C C . PHE A 592 ? 0.2479 0.2297 0.3797 -0.0173 -0.0520 -0.0324 633 PHE A C 4882 O O . PHE A 592 ? 0.2700 0.2533 0.4026 -0.0135 -0.0594 -0.0389 633 PHE A O 4883 C CB . PHE A 592 ? 0.2448 0.2335 0.4029 -0.0278 -0.0407 -0.0265 633 PHE A CB 4884 C CG . PHE A 592 ? 0.2588 0.2558 0.4253 -0.0309 -0.0338 -0.0245 633 PHE A CG 4885 C CD1 . PHE A 592 ? 0.2629 0.2673 0.4360 -0.0289 -0.0376 -0.0298 633 PHE A CD1 4886 C CD2 . PHE A 592 ? 0.3133 0.3105 0.4801 -0.0353 -0.0237 -0.0174 633 PHE A CD2 4887 C CE1 . PHE A 592 ? 0.2694 0.2819 0.4504 -0.0313 -0.0311 -0.0282 633 PHE A CE1 4888 C CE2 . PHE A 592 ? 0.3100 0.3151 0.4841 -0.0378 -0.0168 -0.0159 633 PHE A CE2 4889 C CZ . PHE A 592 ? 0.2810 0.2939 0.4625 -0.0357 -0.0206 -0.0215 633 PHE A CZ 4890 N N . SER A 593 ? 0.2417 0.2159 0.3668 -0.0173 -0.0514 -0.0293 634 SER A N 4891 C CA . SER A 593 ? 0.2642 0.2318 0.3825 -0.0126 -0.0590 -0.0338 634 SER A CA 4892 C C . SER A 593 ? 0.2540 0.2242 0.3563 -0.0062 -0.0615 -0.0365 634 SER A C 4893 O O . SER A 593 ? 0.2531 0.2216 0.3527 -0.0016 -0.0688 -0.0428 634 SER A O 4894 C CB . SER A 593 ? 0.2772 0.2366 0.3909 -0.0136 -0.0570 -0.0293 634 SER A CB 4895 O OG . SER A 593 ? 0.3036 0.2569 0.4102 -0.0086 -0.0638 -0.0337 634 SER A OG 4896 N N . ALA A 594 ? 0.2311 0.2048 0.3221 -0.0057 -0.0552 -0.0316 635 ALA A N 4897 C CA . ALA A 594 ? 0.2266 0.2031 0.3036 -0.0002 -0.0564 -0.0334 635 ALA A CA 4898 C C . ALA A 594 ? 0.2318 0.2135 0.3118 0.0020 -0.0602 -0.0384 635 ALA A C 4899 O O . ALA A 594 ? 0.2494 0.2300 0.3212 0.0074 -0.0652 -0.0428 635 ALA A O 4900 C CB . ALA A 594 ? 0.2313 0.2108 0.2978 -0.0007 -0.0492 -0.0274 635 ALA A CB 4901 N N . VAL A 595 ? 0.2240 0.2110 0.3162 -0.0020 -0.0579 -0.0379 636 VAL A N 4902 C CA . VAL A 595 ? 0.2232 0.2155 0.3200 0.0000 -0.0617 -0.0425 636 VAL A CA 4903 C C . VAL A 595 ? 0.2413 0.2298 0.3443 0.0026 -0.0714 -0.0497 636 VAL A C 4904 O O . VAL A 595 ? 0.2408 0.2299 0.3377 0.0078 -0.0771 -0.0544 636 VAL A O 4905 C CB . VAL A 595 ? 0.2252 0.2241 0.3355 -0.0051 -0.0566 -0.0403 636 VAL A CB 4906 C CG1 . VAL A 595 ? 0.2494 0.2534 0.3675 -0.0031 -0.0617 -0.0456 636 VAL A CG1 4907 C CG2 . VAL A 595 ? 0.2279 0.2305 0.3287 -0.0062 -0.0479 -0.0343 636 VAL A CG2 4908 N N . LYS A 596 ? 0.2520 0.2359 0.3663 -0.0007 -0.0735 -0.0505 637 LYS A N 4909 C CA . LYS A 596 ? 0.2641 0.2433 0.3846 0.0016 -0.0833 -0.0577 637 LYS A CA 4910 C C . LYS A 596 ? 0.2669 0.2404 0.3696 0.0086 -0.0880 -0.0609 637 LYS A C 4911 O O . LYS A 596 ? 0.2653 0.2378 0.3642 0.0137 -0.0957 -0.0672 637 LYS A O 4912 C CB . LYS A 596 ? 0.2772 0.2514 0.4122 -0.0036 -0.0835 -0.0570 637 LYS A CB 4913 C CG . LYS A 596 ? 0.3512 0.3188 0.4920 -0.0011 -0.0940 -0.0647 637 LYS A CG 4914 C CD . LYS A 596 ? 0.4177 0.3812 0.5766 -0.0074 -0.0937 -0.0637 637 LYS A CD 4915 C CE . LYS A 596 ? 0.4662 0.4229 0.6325 -0.0052 -0.1047 -0.0721 637 LYS A CE 4916 N NZ . LYS A 596 ? 0.5331 0.4815 0.6819 0.0003 -0.1076 -0.0735 637 LYS A NZ 4917 N N . ASN A 597 ? 0.2470 0.2172 0.3378 0.0094 -0.0831 -0.0563 638 ASN A N 4918 C CA . ASN A 597 ? 0.2700 0.2355 0.3446 0.0159 -0.0861 -0.0587 638 ASN A CA 4919 C C . ASN A 597 ? 0.2696 0.2393 0.3316 0.0210 -0.0862 -0.0599 638 ASN A C 4920 O O . ASN A 597 ? 0.2907 0.2569 0.3434 0.0271 -0.0920 -0.0651 638 ASN A O 4921 C CB . ASN A 597 ? 0.2528 0.2151 0.3193 0.0153 -0.0804 -0.0532 638 ASN A CB 4922 C CG . ASN A 597 ? 0.2821 0.2377 0.3575 0.0121 -0.0817 -0.0527 638 ASN A CG 4923 O OD1 . ASN A 597 ? 0.3010 0.2534 0.3887 0.0106 -0.0875 -0.0573 638 ASN A OD1 4924 N ND2 . ASN A 597 ? 0.2862 0.2393 0.3562 0.0111 -0.0765 -0.0472 638 ASN A ND2 4925 N N . PHE A 598 ? 0.2422 0.2186 0.3035 0.0188 -0.0799 -0.0554 639 PHE A N 4926 C CA . PHE A 598 ? 0.2412 0.2212 0.2916 0.0233 -0.0795 -0.0559 639 PHE A CA 4927 C C . PHE A 598 ? 0.2559 0.2361 0.3101 0.0264 -0.0877 -0.0624 639 PHE A C 4928 O O . PHE A 598 ? 0.2680 0.2461 0.3096 0.0328 -0.0913 -0.0655 639 PHE A O 4929 C CB . PHE A 598 ? 0.2289 0.2160 0.2810 0.0196 -0.0718 -0.0503 639 PHE A CB 4930 C CG . PHE A 598 ? 0.2327 0.2229 0.2733 0.0238 -0.0702 -0.0498 639 PHE A CG 4931 C CD1 . PHE A 598 ? 0.2505 0.2414 0.2799 0.0247 -0.0641 -0.0453 639 PHE A CD1 4932 C CD2 . PHE A 598 ? 0.2408 0.2332 0.2825 0.0266 -0.0748 -0.0536 639 PHE A CD2 4933 C CE1 . PHE A 598 ? 0.2847 0.2780 0.3044 0.0282 -0.0624 -0.0446 639 PHE A CE1 4934 C CE2 . PHE A 598 ? 0.2590 0.2533 0.2901 0.0304 -0.0731 -0.0526 639 PHE A CE2 4935 C CZ . PHE A 598 ? 0.2834 0.2780 0.3033 0.0312 -0.0667 -0.0481 639 PHE A CZ 4936 N N . THR A 599 ? 0.2505 0.2329 0.3220 0.0222 -0.0906 -0.0645 640 THR A N 4937 C CA . THR A 599 ? 0.2781 0.2612 0.3563 0.0248 -0.0993 -0.0711 640 THR A CA 4938 C C . THR A 599 ? 0.2993 0.2747 0.3695 0.0305 -0.1080 -0.0775 640 THR A C 4939 O O . THR A 599 ? 0.2992 0.2733 0.3602 0.0367 -0.1140 -0.0819 640 THR A O 4940 C CB . THR A 599 ? 0.2644 0.2515 0.3655 0.0185 -0.1002 -0.0720 640 THR A CB 4941 O OG1 . THR A 599 ? 0.2662 0.2601 0.3729 0.0136 -0.0912 -0.0658 640 THR A OG1 4942 C CG2 . THR A 599 ? 0.3059 0.2951 0.4162 0.0210 -0.1097 -0.0790 640 THR A CG2 4943 N N . GLU A 600 ? 0.2895 0.2590 0.3621 0.0290 -0.1088 -0.0780 641 GLU A N 4944 C CA A GLU A 600 ? 0.3150 0.2764 0.3808 0.0343 -0.1171 -0.0847 641 GLU A CA 4945 C CA B GLU A 600 ? 0.3235 0.2847 0.3890 0.0343 -0.1171 -0.0847 641 GLU A CA 4946 C C . GLU A 600 ? 0.3202 0.2785 0.3630 0.0417 -0.1157 -0.0844 641 GLU A C 4947 O O . GLU A 600 ? 0.3280 0.2823 0.3608 0.0482 -0.1227 -0.0901 641 GLU A O 4948 C CB A GLU A 600 ? 0.3195 0.2752 0.3944 0.0306 -0.1176 -0.0849 641 GLU A CB 4949 C CB B GLU A 600 ? 0.3317 0.2868 0.4046 0.0311 -0.1174 -0.0848 641 GLU A CB 4950 C CG A GLU A 600 ? 0.3494 0.3069 0.4479 0.0242 -0.1208 -0.0868 641 GLU A CG 4951 C CG B GLU A 600 ? 0.4066 0.3578 0.4661 0.0326 -0.1112 -0.0803 641 GLU A CG 4952 C CD A GLU A 600 ? 0.3953 0.3469 0.5040 0.0197 -0.1202 -0.0858 641 GLU A CD 4953 C CD B GLU A 600 ? 0.4645 0.4071 0.5110 0.0396 -0.1167 -0.0858 641 GLU A CD 4954 O OE1 A GLU A 600 ? 0.4236 0.3768 0.5524 0.0136 -0.1208 -0.0858 641 GLU A OE1 4955 O OE1 B GLU A 600 ? 0.4681 0.4057 0.5127 0.0391 -0.1143 -0.0840 641 GLU A OE1 4956 O OE2 A GLU A 600 ? 0.4286 0.3740 0.5261 0.0223 -0.1190 -0.0849 641 GLU A OE2 4957 O OE2 B GLU A 600 ? 0.5135 0.4539 0.5508 0.0458 -0.1232 -0.0917 641 GLU A OE2 4958 N N . ILE A 601 ? 0.2988 0.2589 0.3333 0.0407 -0.1067 -0.0778 642 ILE A N 4959 C CA . ILE A 601 ? 0.3072 0.2646 0.3220 0.0471 -0.1042 -0.0770 642 ILE A CA 4960 C C . ILE A 601 ? 0.3107 0.2712 0.3161 0.0513 -0.1047 -0.0774 642 ILE A C 4961 O O . ILE A 601 ? 0.3284 0.2847 0.3185 0.0583 -0.1073 -0.0803 642 ILE A O 4962 C CB . ILE A 601 ? 0.3015 0.2604 0.3120 0.0446 -0.0947 -0.0699 642 ILE A CB 4963 C CG1 . ILE A 601 ? 0.2839 0.2375 0.3005 0.0424 -0.0956 -0.0704 642 ILE A CG1 4964 C CG2 . ILE A 601 ? 0.3515 0.3094 0.3438 0.0508 -0.0910 -0.0686 642 ILE A CG2 4965 C CD1 . ILE A 601 ? 0.3116 0.2673 0.3281 0.0387 -0.0871 -0.0631 642 ILE A CD1 4966 N N . ALA A 602 ? 0.3019 0.2694 0.3162 0.0472 -0.1020 -0.0744 643 ALA A N 4967 C CA . ALA A 602 ? 0.3065 0.2769 0.3133 0.0510 -0.1027 -0.0745 643 ALA A CA 4968 C C . ALA A 602 ? 0.3274 0.2938 0.3320 0.0564 -0.1134 -0.0821 643 ALA A C 4969 O O . ALA A 602 ? 0.3352 0.2991 0.3247 0.0630 -0.1154 -0.0834 643 ALA A O 4970 C CB . ALA A 602 ? 0.3103 0.2889 0.3294 0.0455 -0.0985 -0.0707 643 ALA A CB 4971 N N . SER A 603 ? 0.3235 0.2889 0.3431 0.0537 -0.1204 -0.0869 644 SER A N 4972 C CA A SER A 603 ? 0.3391 0.3003 0.3577 0.0588 -0.1320 -0.0950 644 SER A CA 4973 C CA B SER A 603 ? 0.3468 0.3080 0.3654 0.0588 -0.1320 -0.0950 644 SER A CA 4974 C C . SER A 603 ? 0.3607 0.3130 0.3595 0.0666 -0.1355 -0.0988 644 SER A C 4975 O O . SER A 603 ? 0.3805 0.3292 0.3664 0.0738 -0.1417 -0.1028 644 SER A O 4976 C CB A SER A 603 ? 0.3450 0.3064 0.3850 0.0541 -0.1388 -0.0998 644 SER A CB 4977 C CB B SER A 603 ? 0.3522 0.3138 0.3924 0.0538 -0.1383 -0.0994 644 SER A CB 4978 O OG A SER A 603 ? 0.3679 0.3260 0.4078 0.0591 -0.1508 -0.1080 644 SER A OG 4979 O OG B SER A 603 ? 0.4017 0.3714 0.4588 0.0490 -0.1376 -0.0980 644 SER A OG 4980 N N . LYS A 604 ? 0.3542 0.3026 0.3500 0.0657 -0.1317 -0.0975 645 LYS A N 4981 C CA . LYS A 604 ? 0.3767 0.3168 0.3542 0.0731 -0.1340 -0.1011 645 LYS A CA 4982 C C . LYS A 604 ? 0.3673 0.3073 0.3243 0.0787 -0.1276 -0.0970 645 LYS A C 4983 O O . LYS A 604 ? 0.3814 0.3155 0.3215 0.0865 -0.1315 -0.1007 645 LYS A O 4984 C CB . LYS A 604 ? 0.3909 0.3270 0.3722 0.0706 -0.1316 -0.1008 645 LYS A CB 4985 C CG A LYS A 604 ? 0.4263 0.3606 0.4272 0.0657 -0.1386 -0.1054 645 LYS A CG 4986 C CG B LYS A 604 ? 0.4163 0.3492 0.4148 0.0671 -0.1398 -0.1066 645 LYS A CG 4987 C CD A LYS A 604 ? 0.4819 0.4108 0.4848 0.0644 -0.1370 -0.1055 645 LYS A CD 4988 C CD B LYS A 604 ? 0.4650 0.3908 0.4567 0.0739 -0.1517 -0.1162 645 LYS A CD 4989 C CE A LYS A 604 ? 0.5414 0.4656 0.5604 0.0617 -0.1461 -0.1120 645 LYS A CE 4990 C CE B LYS A 604 ? 0.5075 0.4309 0.5191 0.0699 -0.1608 -0.1224 645 LYS A CE 4991 N NZ A LYS A 604 ? 0.5459 0.4727 0.5838 0.0527 -0.1412 -0.1070 645 LYS A NZ 4992 N NZ B LYS A 604 ? 0.5618 0.4785 0.5666 0.0769 -0.1734 -0.1323 645 LYS A NZ 4993 N N . PHE A 605 ? 0.3345 0.2809 0.2930 0.0747 -0.1177 -0.0892 646 PHE A N 4994 C CA . PHE A 605 ? 0.3442 0.2911 0.2859 0.0792 -0.1115 -0.0850 646 PHE A CA 4995 C C . PHE A 605 ? 0.3557 0.3019 0.2893 0.0842 -0.1167 -0.0873 646 PHE A C 4996 O O . PHE A 605 ? 0.3864 0.3276 0.3009 0.0916 -0.1163 -0.0877 646 PHE A O 4997 C CB . PHE A 605 ? 0.3334 0.2878 0.2814 0.0731 -0.1011 -0.0769 646 PHE A CB 4998 C CG . PHE A 605 ? 0.3378 0.2931 0.2712 0.0768 -0.0942 -0.0723 646 PHE A CG 4999 C CD1 . PHE A 605 ? 0.3476 0.3004 0.2697 0.0797 -0.0879 -0.0698 646 PHE A CD1 5000 C CD2 . PHE A 605 ? 0.3644 0.3230 0.2965 0.0774 -0.0940 -0.0704 646 PHE A CD2 5001 C CE1 . PHE A 605 ? 0.3691 0.3228 0.2792 0.0828 -0.0810 -0.0653 646 PHE A CE1 5002 C CE2 . PHE A 605 ? 0.3936 0.3524 0.3127 0.0807 -0.0874 -0.0658 646 PHE A CE2 5003 C CZ . PHE A 605 ? 0.3549 0.3113 0.2634 0.0831 -0.0807 -0.0631 646 PHE A CZ 5004 N N . SER A 606 ? 0.3490 0.2997 0.2968 0.0807 -0.1215 -0.0887 647 SER A N 5005 C CA . SER A 606 ? 0.3768 0.3269 0.3187 0.0855 -0.1275 -0.0911 647 SER A CA 5006 C C . SER A 606 ? 0.4057 0.3469 0.3341 0.0938 -0.1376 -0.0987 647 SER A C 5007 O O . SER A 606 ? 0.4172 0.3546 0.3292 0.1007 -0.1397 -0.0992 647 SER A O 5008 C CB . SER A 606 ? 0.3704 0.3271 0.3330 0.0802 -0.1321 -0.0925 647 SER A CB 5009 O OG A SER A 606 ? 0.3625 0.3269 0.3361 0.0731 -0.1228 -0.0859 647 SER A OG 5010 O OG B SER A 606 ? 0.3991 0.3567 0.3568 0.0843 -0.1359 -0.0931 647 SER A OG 5011 N N . GLU A 607 ? 0.4070 0.3445 0.3423 0.0930 -0.1437 -0.1045 648 GLU A N 5012 C CA A GLU A 607 ? 0.4395 0.3678 0.3619 0.1008 -0.1536 -0.1125 648 GLU A CA 5013 C CA B GLU A 607 ? 0.4366 0.3649 0.3590 0.1008 -0.1536 -0.1125 648 GLU A CA 5014 C C . GLU A 607 ? 0.4522 0.3740 0.3492 0.1082 -0.1479 -0.1106 648 GLU A C 5015 O O . GLU A 607 ? 0.4695 0.3849 0.3476 0.1167 -0.1526 -0.1137 648 GLU A O 5016 C CB A GLU A 607 ? 0.4505 0.3757 0.3860 0.0978 -0.1598 -0.1185 648 GLU A CB 5017 C CB B GLU A 607 ? 0.4471 0.3726 0.3834 0.0978 -0.1603 -0.1187 648 GLU A CB 5018 C CG A GLU A 607 ? 0.4717 0.4023 0.4328 0.0912 -0.1664 -0.1215 648 GLU A CG 5019 C CG B GLU A 607 ? 0.4786 0.3942 0.4026 0.1058 -0.1718 -0.1281 648 GLU A CG 5020 C CD A GLU A 607 ? 0.5174 0.4439 0.4914 0.0884 -0.1726 -0.1275 648 GLU A CD 5021 C CD B GLU A 607 ? 0.5404 0.4529 0.4804 0.1027 -0.1800 -0.1352 648 GLU A CD 5022 O OE1 A GLU A 607 ? 0.5525 0.4747 0.5213 0.0883 -0.1682 -0.1266 648 GLU A OE1 5023 O OE1 B GLU A 607 ? 0.5593 0.4754 0.5161 0.0949 -0.1750 -0.1322 648 GLU A OE1 5024 O OE2 A GLU A 607 ? 0.5859 0.5134 0.5763 0.0862 -0.1822 -0.1333 648 GLU A OE2 5025 O OE2 B GLU A 607 ? 0.5634 0.4692 0.4983 0.1084 -0.1920 -0.1441 648 GLU A OE2 5026 N N . ARG A 608 ? 0.4239 0.3473 0.3200 0.1053 -0.1374 -0.1052 649 ARG A N 5027 C CA . ARG A 608 ? 0.4409 0.3589 0.3150 0.1120 -0.1311 -0.1032 649 ARG A CA 5028 C C . ARG A 608 ? 0.4495 0.3687 0.3101 0.1157 -0.1262 -0.0981 649 ARG A C 5029 O O . ARG A 608 ? 0.4736 0.3862 0.3132 0.1235 -0.1249 -0.0985 649 ARG A O 5030 C CB . ARG A 608 ? 0.4280 0.3484 0.3059 0.1080 -0.1209 -0.0984 649 ARG A CB 5031 C CG . ARG A 608 ? 0.4488 0.3663 0.3373 0.1055 -0.1251 -0.1031 649 ARG A CG 5032 C CD . ARG A 608 ? 0.4382 0.3554 0.3240 0.1049 -0.1161 -0.0994 649 ARG A CD 5033 N NE . ARG A 608 ? 0.4068 0.3324 0.3004 0.0987 -0.1058 -0.0907 649 ARG A NE 5034 C CZ . ARG A 608 ? 0.4153 0.3467 0.3276 0.0902 -0.1043 -0.0877 649 ARG A CZ 5035 N NH1 . ARG A 608 ? 0.4010 0.3313 0.3273 0.0866 -0.1119 -0.0921 649 ARG A NH1 5036 N NH2 . ARG A 608 ? 0.3908 0.3291 0.3078 0.0855 -0.0953 -0.0802 649 ARG A NH2 5037 N N . LEU A 609 ? 0.4385 0.3655 0.3108 0.1100 -0.1228 -0.0929 650 LEU A N 5038 C CA . LEU A 609 ? 0.4674 0.3955 0.3286 0.1127 -0.1173 -0.0874 650 LEU A CA 5039 C C . LEU A 609 ? 0.5164 0.4384 0.3643 0.1205 -0.1266 -0.0918 650 LEU A C 5040 O O . LEU A 609 ? 0.5224 0.4406 0.3522 0.1265 -0.1230 -0.0886 650 LEU A O 5041 C CB . LEU A 609 ? 0.4715 0.4094 0.3505 0.1046 -0.1127 -0.0819 650 LEU A CB 5042 C CG . LEU A 609 ? 0.4784 0.4190 0.3504 0.1049 -0.1041 -0.0745 650 LEU A CG 5043 C CD1 . LEU A 609 ? 0.4559 0.3963 0.3195 0.1050 -0.0928 -0.0691 650 LEU A CD1 5044 C CD2 . LEU A 609 ? 0.4747 0.4243 0.3659 0.0974 -0.1028 -0.0715 650 LEU A CD2 5045 N N . GLN A 610 ? 0.5433 0.4648 0.4013 0.1202 -0.1383 -0.0988 651 GLN A N 5046 C CA A GLN A 610 ? 0.5915 0.5076 0.4387 0.1275 -0.1487 -0.1036 651 GLN A CA 5047 C CA B GLN A 610 ? 0.5909 0.5071 0.4388 0.1274 -0.1491 -0.1039 651 GLN A CA 5048 C C . GLN A 610 ? 0.6170 0.5221 0.4419 0.1368 -0.1534 -0.1091 651 GLN A C 5049 O O . GLN A 610 ? 0.6524 0.5508 0.4582 0.1451 -0.1580 -0.1106 651 GLN A O 5050 C CB A GLN A 610 ? 0.5859 0.5063 0.4540 0.1237 -0.1600 -0.1092 651 GLN A CB 5051 C CB B GLN A 610 ? 0.5885 0.5086 0.4577 0.1235 -0.1607 -0.1101 651 GLN A CB 5052 C CG A GLN A 610 ? 0.6003 0.5308 0.4866 0.1167 -0.1560 -0.1040 651 GLN A CG 5053 C CG B GLN A 610 ? 0.6194 0.5348 0.4938 0.1241 -0.1699 -0.1187 651 GLN A CG 5054 C CD A GLN A 610 ? 0.6076 0.5418 0.5122 0.1149 -0.1676 -0.1097 651 GLN A CD 5055 C CD B GLN A 610 ? 0.6665 0.5879 0.5680 0.1175 -0.1782 -0.1233 651 GLN A CD 5056 O OE1 A GLN A 610 ? 0.6705 0.5990 0.5682 0.1213 -0.1794 -0.1167 651 GLN A OE1 5057 O OE1 B GLN A 610 ? 0.6625 0.5922 0.5796 0.1121 -0.1763 -0.1198 651 GLN A OE1 5058 N NE2 A GLN A 610 ? 0.6164 0.5602 0.5443 0.1063 -0.1642 -0.1071 651 GLN A NE2 5059 N NE2 B GLN A 610 ? 0.6812 0.5983 0.5891 0.1178 -0.1873 -0.1313 651 GLN A NE2 5060 N N . ASP A 611 ? 0.6342 0.5370 0.4608 0.1356 -0.1518 -0.1118 652 ASP A N 5061 C CA . ASP A 611 ? 0.6769 0.5694 0.4860 0.1435 -0.1566 -0.1185 652 ASP A CA 5062 C C . ASP A 611 ? 0.6723 0.5602 0.4613 0.1483 -0.1456 -0.1144 652 ASP A C 5063 O O . ASP A 611 ? 0.6994 0.5785 0.4723 0.1555 -0.1487 -0.1198 652 ASP A O 5064 C CB . ASP A 611 ? 0.6871 0.5797 0.5127 0.1388 -0.1614 -0.1243 652 ASP A CB 5065 C CG . ASP A 611 ? 0.7548 0.6467 0.5942 0.1379 -0.1763 -0.1329 652 ASP A CG 5066 O OD1 . ASP A 611 ? 0.8252 0.7174 0.6632 0.1406 -0.1837 -0.1347 652 ASP A OD1 5067 O OD2 . ASP A 611 ? 0.8353 0.7262 0.6881 0.1343 -0.1806 -0.1379 652 ASP A OD2 5068 N N . PHE A 612 ? 0.6552 0.5490 0.4463 0.1442 -0.1326 -0.1055 653 PHE A N 5069 C CA . PHE A 612 ? 0.6539 0.5443 0.4297 0.1482 -0.1220 -0.1021 653 PHE A CA 5070 C C . PHE A 612 ? 0.6807 0.5628 0.4287 0.1583 -0.1200 -0.1011 653 PHE A C 5071 O O . PHE A 612 ? 0.7182 0.5944 0.4505 0.1640 -0.1147 -0.1018 653 PHE A O 5072 C CB . PHE A 612 ? 0.6192 0.5182 0.4066 0.1408 -0.1089 -0.0934 653 PHE A CB 5073 C CG . PHE A 612 ? 0.5928 0.4954 0.3759 0.1403 -0.1015 -0.0855 653 PHE A CG 5074 C CD1 . PHE A 612 ? 0.5444 0.4439 0.3100 0.1453 -0.0913 -0.0803 653 PHE A CD1 5075 C CD2 . PHE A 612 ? 0.5687 0.4781 0.3667 0.1343 -0.1038 -0.0831 653 PHE A CD2 5076 C CE1 . PHE A 612 ? 0.6231 0.5257 0.3865 0.1441 -0.0839 -0.0728 653 PHE A CE1 5077 C CE2 . PHE A 612 ? 0.6104 0.5230 0.4058 0.1334 -0.0968 -0.0758 653 PHE A CE2 5078 C CZ . PHE A 612 ? 0.6250 0.5341 0.4034 0.1381 -0.0870 -0.0706 653 PHE A CZ 5079 N N A SER A 615 ? 0.5144 0.3727 0.1686 0.1876 -0.0870 -0.0811 656 SER A N 5080 N N B SER A 615 ? 0.4916 0.3590 0.1511 0.1806 -0.0641 -0.0604 656 SER A N 5081 C CA A SER A 615 ? 0.5341 0.3888 0.1709 0.1923 -0.0730 -0.0740 656 SER A CA 5082 C CA B SER A 615 ? 0.5012 0.3632 0.1416 0.1863 -0.0511 -0.0539 656 SER A CA 5083 C C A SER A 615 ? 0.5025 0.3657 0.1542 0.1856 -0.0592 -0.0684 656 SER A C 5084 C C B SER A 615 ? 0.5120 0.3779 0.1582 0.1842 -0.0403 -0.0530 656 SER A C 5085 O O A SER A 615 ? 0.5168 0.3783 0.1575 0.1887 -0.0463 -0.0622 656 SER A O 5086 O O B SER A 615 ? 0.5336 0.3955 0.1654 0.1891 -0.0289 -0.0487 656 SER A O 5087 C CB A SER A 615 ? 0.5329 0.3754 0.1422 0.2037 -0.0747 -0.0793 656 SER A CB 5088 C CB B SER A 615 ? 0.5171 0.3652 0.1261 0.1987 -0.0562 -0.0571 656 SER A CB 5089 O OG A SER A 615 ? 0.5485 0.3914 0.1646 0.2031 -0.0772 -0.0862 656 SER A OG 5090 O OG B SER A 615 ? 0.5604 0.4040 0.1618 0.2034 -0.0603 -0.0652 656 SER A OG 5091 N N A ASN A 616 ? 0.4827 0.3544 0.1586 0.1772 -0.0617 -0.0707 657 ASN A N 5092 N N B ASN A 616 ? 0.4955 0.3687 0.1625 0.1775 -0.0442 -0.0572 657 ASN A N 5093 C CA A ASN A 616 ? 0.4723 0.3512 0.1616 0.1718 -0.0508 -0.0670 657 ASN A CA 5094 C CA B ASN A 616 ? 0.5142 0.3922 0.1900 0.1747 -0.0347 -0.0561 657 ASN A CA 5095 C C A ASN A 616 ? 0.4532 0.3426 0.1624 0.1623 -0.0446 -0.0595 657 ASN A C 5096 C C B ASN A 616 ? 0.4914 0.3807 0.1896 0.1647 -0.0269 -0.0489 657 ASN A C 5097 O O A ASN A 616 ? 0.4204 0.3160 0.1481 0.1551 -0.0513 -0.0607 657 ASN A O 5098 O O B ASN A 616 ? 0.4727 0.3693 0.1912 0.1569 -0.0324 -0.0504 657 ASN A O 5099 C CB A ASN A 616 ? 0.4683 0.3487 0.1697 0.1693 -0.0568 -0.0741 657 ASN A CB 5100 C CB B ASN A 616 ? 0.5120 0.3899 0.1957 0.1739 -0.0438 -0.0650 657 ASN A CB 5101 C CG A ASN A 616 ? 0.4587 0.3446 0.1699 0.1661 -0.0460 -0.0711 657 ASN A CG 5102 C CG B ASN A 616 ? 0.5317 0.4145 0.2258 0.1713 -0.0355 -0.0645 657 ASN A CG 5103 O OD1 A ASN A 616 ? 0.4242 0.3173 0.1452 0.1610 -0.0364 -0.0637 657 ASN A OD1 5104 O OD1 B ASN A 616 ? 0.5526 0.4434 0.2599 0.1654 -0.0257 -0.0579 657 ASN A OD1 5105 N ND2 A ASN A 616 ? 0.5039 0.3861 0.2127 0.1694 -0.0479 -0.0771 657 ASN A ND2 5106 N ND2 B ASN A 616 ? 0.5303 0.4084 0.2201 0.1753 -0.0404 -0.0720 657 ASN A ND2 5107 N N A PRO A 617 ? 0.4458 0.3368 0.1509 0.1625 -0.0318 -0.0516 658 PRO A N 5108 N N B PRO A 617 ? 0.4987 0.3892 0.1931 0.1651 -0.0138 -0.0411 658 PRO A N 5109 C CA A PRO A 617 ? 0.4268 0.3266 0.1489 0.1542 -0.0267 -0.0447 658 PRO A CA 5110 C CA B PRO A 617 ? 0.4712 0.3717 0.1861 0.1559 -0.0074 -0.0347 658 PRO A CA 5111 C C A PRO A 617 ? 0.3986 0.3083 0.1440 0.1455 -0.0239 -0.0443 658 PRO A C 5112 C C B PRO A 617 ? 0.4480 0.3583 0.1870 0.1475 -0.0081 -0.0364 658 PRO A C 5113 O O A PRO A 617 ? 0.3754 0.2926 0.1373 0.1379 -0.0231 -0.0406 658 PRO A O 5114 O O B PRO A 617 ? 0.4216 0.3390 0.1777 0.1397 -0.0100 -0.0342 658 PRO A O 5115 C CB A PRO A 617 ? 0.4266 0.3242 0.1369 0.1576 -0.0134 -0.0371 658 PRO A CB 5116 C CB B PRO A 617 ? 0.4848 0.3841 0.1914 0.1586 0.0073 -0.0272 658 PRO A CB 5117 C CG A PRO A 617 ? 0.4519 0.3440 0.1482 0.1647 -0.0084 -0.0397 658 PRO A CG 5118 C CG B PRO A 617 ? 0.5217 0.4087 0.1994 0.1698 0.0072 -0.0285 658 PRO A CG 5119 C CD A PRO A 617 ? 0.4797 0.3643 0.1649 0.1703 -0.0215 -0.0488 658 PRO A CD 5120 C CD B PRO A 617 ? 0.5143 0.3969 0.1862 0.1737 -0.0041 -0.0379 658 PRO A CD 5121 N N A ILE A 618 ? 0.4144 0.3236 0.1604 0.1472 -0.0221 -0.0476 659 ILE A N 5122 N N B ILE A 618 ? 0.4477 0.3581 0.1881 0.1490 -0.0065 -0.0399 659 ILE A N 5123 C CA A ILE A 618 ? 0.4052 0.3228 0.1720 0.1398 -0.0200 -0.0474 659 ILE A CA 5124 C CA B ILE A 618 ? 0.4361 0.3555 0.1992 0.1410 -0.0069 -0.0406 659 ILE A CA 5125 C C A ILE A 618 ? 0.3815 0.3015 0.1620 0.1346 -0.0316 -0.0523 659 ILE A C 5126 C C B ILE A 618 ? 0.4159 0.3362 0.1888 0.1372 -0.0198 -0.0466 659 ILE A C 5127 O O A ILE A 618 ? 0.3607 0.2885 0.1594 0.1266 -0.0313 -0.0500 659 ILE A O 5128 O O B ILE A 618 ? 0.4062 0.3339 0.1978 0.1292 -0.0218 -0.0454 659 ILE A O 5129 C CB A ILE A 618 ? 0.4269 0.3428 0.1908 0.1436 -0.0154 -0.0501 659 ILE A CB 5130 C CB B ILE A 618 ? 0.4408 0.3615 0.2060 0.1429 0.0001 -0.0414 659 ILE A CB 5131 C CG1 A ILE A 618 ? 0.4602 0.3723 0.2081 0.1505 -0.0039 -0.0463 659 ILE A CG1 5132 C CG1 B ILE A 618 ? 0.4692 0.3925 0.2328 0.1436 0.0139 -0.0341 659 ILE A CG1 5133 C CG2 A ILE A 618 ? 0.4163 0.3409 0.2017 0.1362 -0.0129 -0.0488 659 ILE A CG2 5134 C CG2 B ILE A 618 ? 0.4474 0.3757 0.2342 0.1354 -0.0028 -0.0429 659 ILE A CG2 5135 C CD1 A ILE A 618 ? 0.4969 0.4138 0.2489 0.1472 0.0059 -0.0378 659 ILE A CD1 5136 C CD1 B ILE A 618 ? 0.4605 0.3875 0.2299 0.1386 0.0166 -0.0278 659 ILE A CD1 5137 N N A VAL A 619 ? 0.3879 0.3010 0.1593 0.1392 -0.0417 -0.0593 660 VAL A N 5138 N N B VAL A 619 ? 0.4213 0.3337 0.1817 0.1431 -0.0287 -0.0532 660 VAL A N 5139 C CA A VAL A 619 ? 0.3852 0.3002 0.1702 0.1344 -0.0528 -0.0641 660 VAL A CA 5140 C CA B VAL A 619 ? 0.3985 0.3117 0.1696 0.1393 -0.0410 -0.0588 660 VAL A CA 5141 C C A VAL A 619 ? 0.3656 0.2855 0.1595 0.1292 -0.0551 -0.0607 660 VAL A C 5142 C C B VAL A 619 ? 0.3785 0.2963 0.1590 0.1337 -0.0447 -0.0559 660 VAL A C 5143 O O A VAL A 619 ? 0.3576 0.2841 0.1701 0.1215 -0.0580 -0.0605 660 VAL A O 5144 O O B VAL A 619 ? 0.3664 0.2905 0.1655 0.1262 -0.0487 -0.0564 660 VAL A O 5145 C CB A VAL A 619 ? 0.3943 0.3005 0.1682 0.1408 -0.0638 -0.0727 660 VAL A CB 5146 C CB B VAL A 619 ? 0.4233 0.3270 0.1799 0.1467 -0.0507 -0.0670 660 VAL A CB 5147 C CG1 A VAL A 619 ? 0.4041 0.3127 0.1931 0.1355 -0.0752 -0.0770 660 VAL A CG1 5148 C CG1 B VAL A 619 ? 0.4131 0.3180 0.1826 0.1423 -0.0637 -0.0725 660 VAL A CG1 5149 C CG2 A VAL A 619 ? 0.4276 0.3298 0.1972 0.1445 -0.0625 -0.0770 660 VAL A CG2 5150 C CG2 B VAL A 619 ? 0.4330 0.3330 0.1841 0.1511 -0.0478 -0.0707 660 VAL A CG2 5151 N N A LEU A 620 ? 0.3683 0.2846 0.1483 0.1337 -0.0534 -0.0579 661 LEU A N 5152 N N B LEU A 620 ? 0.3681 0.2829 0.1365 0.1373 -0.0422 -0.0521 661 LEU A N 5153 C CA A LEU A 620 ? 0.3460 0.2661 0.1322 0.1300 -0.0549 -0.0543 661 LEU A CA 5154 C CA B LEU A 620 ? 0.3642 0.2832 0.1412 0.1326 -0.0448 -0.0491 661 LEU A CA 5155 C C A LEU A 620 ? 0.3452 0.2747 0.1484 0.1216 -0.0466 -0.0481 661 LEU A C 5156 C C B LEU A 620 ? 0.3490 0.2778 0.1447 0.1238 -0.0374 -0.0435 661 LEU A C 5157 O O A LEU A 620 ? 0.3235 0.2590 0.1427 0.1149 -0.0501 -0.0480 661 LEU A O 5158 O O B LEU A 620 ? 0.3365 0.2712 0.1475 0.1172 -0.0409 -0.0430 661 LEU A O 5159 C CB A LEU A 620 ? 0.3770 0.2904 0.1431 0.1373 -0.0529 -0.0515 661 LEU A CB 5160 C CB B LEU A 620 ? 0.3669 0.2802 0.1264 0.1385 -0.0422 -0.0453 661 LEU A CB 5161 C CG A LEU A 620 ? 0.3723 0.2889 0.1429 0.1344 -0.0517 -0.0463 661 LEU A CG 5162 C CG B LEU A 620 ? 0.4072 0.3242 0.1746 0.1344 -0.0439 -0.0416 661 LEU A CG 5163 C CD1 A LEU A 620 ? 0.3891 0.3104 0.1757 0.1291 -0.0615 -0.0496 661 LEU A CD1 5164 C CD1 B LEU A 620 ? 0.3987 0.3171 0.1757 0.1322 -0.0567 -0.0475 661 LEU A CD1 5165 C CD2 A LEU A 620 ? 0.3874 0.2953 0.1354 0.1428 -0.0504 -0.0437 661 LEU A CD2 5166 C CD2 B LEU A 620 ? 0.4118 0.3215 0.1595 0.1414 -0.0406 -0.0375 661 LEU A CD2 5167 N N A ARG A 621 ? 0.3429 0.2736 0.1429 0.1222 -0.0358 -0.0432 662 ARG A N 5168 N N B ARG A 621 ? 0.3573 0.2876 0.1516 0.1241 -0.0269 -0.0392 662 ARG A N 5169 C CA A ARG A 621 ? 0.3455 0.2846 0.1604 0.1149 -0.0282 -0.0374 662 ARG A CA 5170 C CA B ARG A 621 ? 0.3535 0.2930 0.1658 0.1160 -0.0205 -0.0346 662 ARG A CA 5171 C C A ARG A 621 ? 0.3417 0.2865 0.1734 0.1087 -0.0304 -0.0396 662 ARG A C 5172 C C B ARG A 621 ? 0.3519 0.2972 0.1824 0.1092 -0.0256 -0.0376 662 ARG A C 5173 O O A ARG A 621 ? 0.3040 0.2554 0.1506 0.1016 -0.0305 -0.0375 662 ARG A O 5174 O O B ARG A 621 ? 0.3294 0.2815 0.1742 0.1022 -0.0246 -0.0348 662 ARG A O 5175 C CB A ARG A 621 ? 0.3484 0.2876 0.1573 0.1170 -0.0162 -0.0320 662 ARG A CB 5176 C CB B ARG A 621 ? 0.3580 0.2984 0.1669 0.1177 -0.0086 -0.0298 662 ARG A CB 5177 C CG A ARG A 621 ? 0.3465 0.2945 0.1728 0.1095 -0.0094 -0.0275 662 ARG A CG 5178 C CG B ARG A 621 ? 0.3386 0.2881 0.1654 0.1100 -0.0025 -0.0252 662 ARG A CG 5179 C CD A ARG A 621 ? 0.3198 0.2716 0.1522 0.1052 -0.0069 -0.0226 662 ARG A CD 5180 C CD B ARG A 621 ? 0.4402 0.3922 0.2700 0.1069 0.0018 -0.0196 662 ARG A CD 5181 N NE A ARG A 621 ? 0.3826 0.3401 0.2245 0.1013 0.0024 -0.0179 662 ARG A NE 5182 N NE B ARG A 621 ? 0.4499 0.4090 0.2928 0.1018 0.0101 -0.0152 662 ARG A NE 5183 C CZ A ARG A 621 ? 0.3361 0.2945 0.1777 0.1007 0.0102 -0.0122 662 ARG A CZ 5184 C CZ B ARG A 621 ? 0.4330 0.3943 0.2791 0.0996 0.0169 -0.0096 662 ARG A CZ 5185 N NH1 A ARG A 621 ? 0.3684 0.3221 0.2002 0.1035 0.0103 -0.0098 662 ARG A NH1 5186 N NH1 B ARG A 621 ? 0.4563 0.4132 0.2935 0.1018 0.0169 -0.0072 662 ARG A NH1 5187 N NH2 A ARG A 621 ? 0.3888 0.3528 0.2408 0.0972 0.0178 -0.0090 662 ARG A NH2 5188 N NH2 B ARG A 621 ? 0.4449 0.4128 0.3040 0.0952 0.0234 -0.0067 662 ARG A NH2 5189 N N . MET A 622 ? 0.3677 0.3097 0.1969 0.1114 -0.0315 -0.0435 663 MET A N 5190 C CA . MET A 622 ? 0.3742 0.3201 0.2191 0.1057 -0.0360 -0.0464 663 MET A CA 5191 C C . MET A 622 ? 0.3763 0.3245 0.2317 0.1008 -0.0444 -0.0484 663 MET A C 5192 O O . MET A 622 ? 0.3483 0.3026 0.2190 0.0937 -0.0443 -0.0467 663 MET A O 5193 C CB A MET A 622 ? 0.3835 0.3236 0.2228 0.1103 -0.0404 -0.0525 663 MET A CB 5194 C CB B MET A 622 ? 0.3872 0.3280 0.2268 0.1102 -0.0382 -0.0515 663 MET A CB 5195 C CG A MET A 622 ? 0.3780 0.3200 0.2325 0.1049 -0.0474 -0.0562 663 MET A CG 5196 C CG B MET A 622 ? 0.3854 0.3256 0.2171 0.1145 -0.0282 -0.0487 663 MET A CG 5197 S SD A MET A 622 ? 0.3632 0.2979 0.2116 0.1105 -0.0515 -0.0630 663 MET A SD 5198 S SD B MET A 622 ? 0.4241 0.3600 0.2521 0.1195 -0.0276 -0.0535 663 MET A SD 5199 C CE A MET A 622 ? 0.4416 0.3764 0.2797 0.1155 -0.0395 -0.0590 663 MET A CE 5200 C CE B MET A 622 ? 0.3244 0.2488 0.1307 0.1290 -0.0351 -0.0604 663 MET A CE 5201 N N . MET A 623 ? 0.3596 0.3028 0.2067 0.1048 -0.0519 -0.0523 664 MET A N 5202 C CA . MET A 623 ? 0.3539 0.2997 0.2124 0.1004 -0.0595 -0.0544 664 MET A CA 5203 C C . MET A 623 ? 0.3406 0.2925 0.2063 0.0958 -0.0559 -0.0492 664 MET A C 5204 O O . MET A 623 ? 0.3519 0.3091 0.2325 0.0895 -0.0584 -0.0491 664 MET A O 5205 C CB A MET A 623 ? 0.3820 0.3208 0.2287 0.1070 -0.0685 -0.0599 664 MET A CB 5206 C CB B MET A 623 ? 0.3679 0.3073 0.2189 0.1056 -0.0702 -0.0611 664 MET A CB 5207 C CG A MET A 623 ? 0.4254 0.3564 0.2592 0.1138 -0.0715 -0.0651 664 MET A CG 5208 C CG B MET A 623 ? 0.3299 0.2652 0.1819 0.1071 -0.0757 -0.0672 664 MET A CG 5209 S SD A MET A 623 ? 0.4689 0.4013 0.3191 0.1088 -0.0771 -0.0701 664 MET A SD 5210 S SD B MET A 623 ? 0.3804 0.3089 0.2280 0.1119 -0.0899 -0.0761 664 MET A SD 5211 C CE A MET A 623 ? 0.4209 0.3484 0.2715 0.1113 -0.0915 -0.0783 664 MET A CE 5212 C CE B MET A 623 ? 0.3086 0.2439 0.1823 0.1022 -0.0951 -0.0776 664 MET A CE 5213 N N . ASN A 624 ? 0.3588 0.3093 0.2137 0.0992 -0.0497 -0.0448 665 ASN A N 5214 C CA . ASN A 624 ? 0.3336 0.2891 0.1949 0.0950 -0.0456 -0.0397 665 ASN A CA 5215 C C . ASN A 624 ? 0.3249 0.2878 0.2004 0.0878 -0.0394 -0.0362 665 ASN A C 5216 O O . ASN A 624 ? 0.3161 0.2842 0.2029 0.0823 -0.0394 -0.0345 665 ASN A O 5217 C CB . ASN A 624 ? 0.3601 0.3119 0.2073 0.1000 -0.0398 -0.0355 665 ASN A CB 5218 C CG . ASN A 624 ? 0.3660 0.3121 0.2024 0.1055 -0.0469 -0.0377 665 ASN A CG 5219 O OD1 . ASN A 624 ? 0.3739 0.3216 0.2184 0.1036 -0.0552 -0.0413 665 ASN A OD1 5220 N ND2 . ASN A 624 ? 0.3804 0.3200 0.1993 0.1122 -0.0434 -0.0353 665 ASN A ND2 5221 N N . ASP A 625 ? 0.3183 0.2811 0.1926 0.0883 -0.0346 -0.0354 666 ASP A N 5222 C CA . ASP A 625 ? 0.3137 0.2833 0.2017 0.0817 -0.0299 -0.0326 666 ASP A CA 5223 C C . ASP A 625 ? 0.3101 0.2826 0.2111 0.0763 -0.0360 -0.0354 666 ASP A C 5224 O O . ASP A 625 ? 0.2932 0.2713 0.2057 0.0701 -0.0342 -0.0329 666 ASP A O 5225 C CB . ASP A 625 ? 0.3132 0.2821 0.1981 0.0839 -0.0243 -0.0317 666 ASP A CB 5226 C CG . ASP A 625 ? 0.3539 0.3227 0.2316 0.0867 -0.0154 -0.0271 666 ASP A CG 5227 O OD1 . ASP A 625 ? 0.3796 0.3484 0.2544 0.0867 -0.0136 -0.0242 666 ASP A OD1 5228 O OD2 . ASP A 625 ? 0.3819 0.3509 0.2584 0.0886 -0.0101 -0.0262 666 ASP A OD2 5229 N N . GLN A 626 ? 0.2908 0.2590 0.1902 0.0786 -0.0431 -0.0406 667 GLN A N 5230 C CA . GLN A 626 ? 0.2889 0.2595 0.2015 0.0732 -0.0485 -0.0430 667 GLN A CA 5231 C C . GLN A 626 ? 0.2843 0.2588 0.2046 0.0694 -0.0506 -0.0422 667 GLN A C 5232 O O . GLN A 626 ? 0.2955 0.2748 0.2282 0.0632 -0.0501 -0.0408 667 GLN A O 5233 C CB . GLN A 626 ? 0.2914 0.2561 0.2016 0.0765 -0.0563 -0.0492 667 GLN A CB 5234 C CG . GLN A 626 ? 0.3106 0.2725 0.2175 0.0787 -0.0540 -0.0500 667 GLN A CG 5235 C CD . GLN A 626 ? 0.3228 0.2784 0.2268 0.0822 -0.0615 -0.0564 667 GLN A CD 5236 O OE1 . GLN A 626 ? 0.3548 0.3047 0.2458 0.0889 -0.0646 -0.0599 667 GLN A OE1 5237 N NE2 . GLN A 626 ? 0.3122 0.2680 0.2280 0.0779 -0.0649 -0.0582 667 GLN A NE2 5238 N N . LEU A 627 ? 0.2992 0.2715 0.2117 0.0734 -0.0527 -0.0428 668 LEU A N 5239 C CA . LEU A 627 ? 0.2974 0.2736 0.2174 0.0704 -0.0544 -0.0420 668 LEU A CA 5240 C C . LEU A 627 ? 0.2841 0.2658 0.2095 0.0658 -0.0469 -0.0365 668 LEU A C 5241 O O . LEU A 627 ? 0.2980 0.2848 0.2353 0.0604 -0.0471 -0.0358 668 LEU A O 5242 C CB . LEU A 627 ? 0.3153 0.2870 0.2245 0.0765 -0.0586 -0.0437 668 LEU A CB 5243 C CG . LEU A 627 ? 0.3711 0.3383 0.2789 0.0800 -0.0684 -0.0503 668 LEU A CG 5244 C CD1 . LEU A 627 ? 0.4070 0.3686 0.3006 0.0873 -0.0727 -0.0519 668 LEU A CD1 5245 C CD2 . LEU A 627 ? 0.3594 0.3312 0.2849 0.0743 -0.0739 -0.0531 668 LEU A CD2 5246 N N . MET A 628 ? 0.2987 0.2795 0.2160 0.0679 -0.0404 -0.0329 669 MET A N 5247 C CA . MET A 628 ? 0.2982 0.2838 0.2202 0.0641 -0.0335 -0.0281 669 MET A CA 5248 C C . MET A 628 ? 0.2779 0.2684 0.2112 0.0579 -0.0313 -0.0269 669 MET A C 5249 O O . MET A 628 ? 0.2848 0.2800 0.2261 0.0531 -0.0289 -0.0247 669 MET A O 5250 C CB . MET A 628 ? 0.3141 0.2974 0.2263 0.0677 -0.0269 -0.0246 669 MET A CB 5251 C CG . MET A 628 ? 0.3507 0.3388 0.2690 0.0635 -0.0199 -0.0199 669 MET A CG 5252 S SD . MET A 628 ? 0.4051 0.3906 0.3137 0.0676 -0.0116 -0.0157 669 MET A SD 5253 C CE . MET A 628 ? 0.3680 0.3546 0.2786 0.0676 -0.0092 -0.0165 669 MET A CE 5254 N N . PHE A 629 ? 0.2589 0.2479 0.1920 0.0583 -0.0320 -0.0284 670 PHE A N 5255 C CA . PHE A 629 ? 0.2597 0.2525 0.2023 0.0530 -0.0300 -0.0269 670 PHE A CA 5256 C C . PHE A 629 ? 0.2574 0.2514 0.2094 0.0489 -0.0348 -0.0290 670 PHE A C 5257 O O . PHE A 629 ? 0.2561 0.2525 0.2151 0.0445 -0.0335 -0.0276 670 PHE A O 5258 C CB . PHE A 629 ? 0.2612 0.2521 0.2003 0.0554 -0.0281 -0.0269 670 PHE A CB 5259 C CG . PHE A 629 ? 0.2726 0.2645 0.2069 0.0575 -0.0214 -0.0236 670 PHE A CG 5260 C CD1 . PHE A 629 ? 0.2995 0.2963 0.2395 0.0536 -0.0166 -0.0199 670 PHE A CD1 5261 C CD2 . PHE A 629 ? 0.3156 0.3034 0.2401 0.0634 -0.0196 -0.0244 670 PHE A CD2 5262 C CE1 . PHE A 629 ? 0.3299 0.3277 0.2673 0.0554 -0.0104 -0.0170 670 PHE A CE1 5263 C CE2 . PHE A 629 ? 0.3497 0.3386 0.2711 0.0653 -0.0127 -0.0212 670 PHE A CE2 5264 C CZ . PHE A 629 ? 0.3388 0.3329 0.2675 0.0610 -0.0081 -0.0175 670 PHE A CZ 5265 N N . LEU A 630 ? 0.2611 0.2536 0.2141 0.0499 -0.0401 -0.0322 671 LEU A N 5266 C CA . LEU A 630 ? 0.2484 0.2423 0.2122 0.0457 -0.0441 -0.0341 671 LEU A CA 5267 C C . LEU A 630 ? 0.2369 0.2365 0.2092 0.0401 -0.0404 -0.0311 671 LEU A C 5268 O O . LEU A 630 ? 0.2438 0.2450 0.2235 0.0356 -0.0395 -0.0300 671 LEU A O 5269 C CB . LEU A 630 ? 0.2649 0.2562 0.2287 0.0486 -0.0511 -0.0387 671 LEU A CB 5270 C CG . LEU A 630 ? 0.2610 0.2543 0.2381 0.0440 -0.0548 -0.0407 671 LEU A CG 5271 C CD1 . LEU A 630 ? 0.2867 0.2780 0.2688 0.0413 -0.0555 -0.0411 671 LEU A CD1 5272 C CD2 . LEU A 630 ? 0.2887 0.2793 0.2659 0.0477 -0.0628 -0.0459 671 LEU A CD2 5273 N N . GLU A 631 ? 0.2306 0.2325 0.2013 0.0406 -0.0381 -0.0296 672 GLU A N 5274 C CA . GLU A 631 ? 0.2249 0.2317 0.2026 0.0357 -0.0342 -0.0270 672 GLU A CA 5275 C C . GLU A 631 ? 0.2019 0.2100 0.1791 0.0331 -0.0294 -0.0238 672 GLU A C 5276 O O . GLU A 631 ? 0.2176 0.2285 0.2011 0.0284 -0.0275 -0.0222 672 GLU A O 5277 C CB . GLU A 631 ? 0.2326 0.2409 0.2076 0.0372 -0.0321 -0.0258 672 GLU A CB 5278 C CG . GLU A 631 ? 0.2157 0.2289 0.1990 0.0324 -0.0293 -0.0244 672 GLU A CG 5279 C CD . GLU A 631 ? 0.2617 0.2765 0.2537 0.0311 -0.0332 -0.0272 672 GLU A CD 5280 O OE1 . GLU A 631 ? 0.2519 0.2656 0.2427 0.0346 -0.0369 -0.0293 672 GLU A OE1 5281 O OE2 . GLU A 631 ? 0.2601 0.2773 0.2604 0.0268 -0.0325 -0.0272 672 GLU A OE2 5282 N N . ARG A 632 ? 0.2126 0.2188 0.1827 0.0361 -0.0275 -0.0227 673 ARG A N 5283 C CA . ARG A 632 ? 0.2103 0.2180 0.1807 0.0343 -0.0238 -0.0201 673 ARG A CA 5284 C C . ARG A 632 ? 0.2160 0.2230 0.1909 0.0316 -0.0256 -0.0203 673 ARG A C 5285 O O . ARG A 632 ? 0.2222 0.2311 0.1997 0.0285 -0.0233 -0.0180 673 ARG A O 5286 C CB . ARG A 632 ? 0.2444 0.2501 0.2074 0.0387 -0.0215 -0.0194 673 ARG A CB 5287 C CG . ARG A 632 ? 0.2301 0.2389 0.1945 0.0370 -0.0166 -0.0163 673 ARG A CG 5288 C CD . ARG A 632 ? 0.2490 0.2593 0.2121 0.0372 -0.0136 -0.0148 673 ARG A CD 5289 N NE . ARG A 632 ? 0.2178 0.2253 0.1733 0.0421 -0.0115 -0.0143 673 ARG A NE 5290 C CZ . ARG A 632 ? 0.2407 0.2456 0.1912 0.0450 -0.0129 -0.0151 673 ARG A CZ 5291 N NH1 . ARG A 632 ? 0.2455 0.2507 0.1989 0.0438 -0.0169 -0.0169 673 ARG A NH1 5292 N NH2 . ARG A 632 ? 0.2710 0.2727 0.2135 0.0496 -0.0103 -0.0139 673 ARG A NH2 5293 N N . ALA A 633 ? 0.2070 0.2106 0.1826 0.0330 -0.0300 -0.0232 674 ALA A N 5294 C CA . ALA A 633 ? 0.2061 0.2079 0.1860 0.0307 -0.0318 -0.0232 674 ALA A CA 5295 C C . ALA A 633 ? 0.1989 0.2032 0.1862 0.0253 -0.0307 -0.0215 674 ALA A C 5296 O O . ALA A 633 ? 0.2289 0.2316 0.2191 0.0229 -0.0309 -0.0203 674 ALA A O 5297 C CB . ALA A 633 ? 0.2327 0.2298 0.2124 0.0334 -0.0372 -0.0272 674 ALA A CB 5298 N N . PHE A 634 ? 0.2037 0.2111 0.1941 0.0235 -0.0297 -0.0216 675 PHE A N 5299 C CA . PHE A 634 ? 0.1938 0.2037 0.1909 0.0185 -0.0277 -0.0198 675 PHE A CA 5300 C C . PHE A 634 ? 0.2061 0.2184 0.2010 0.0163 -0.0233 -0.0166 675 PHE A C 5301 O O . PHE A 634 ? 0.2085 0.2222 0.2069 0.0125 -0.0212 -0.0148 675 PHE A O 5302 C CB . PHE A 634 ? 0.2008 0.2133 0.2033 0.0177 -0.0285 -0.0217 675 PHE A CB 5303 C CG . PHE A 634 ? 0.2156 0.2259 0.2225 0.0192 -0.0337 -0.0252 675 PHE A CG 5304 C CD1 . PHE A 634 ? 0.2212 0.2294 0.2349 0.0165 -0.0356 -0.0257 675 PHE A CD1 5305 C CD2 . PHE A 634 ? 0.2536 0.2636 0.2582 0.0231 -0.0370 -0.0282 675 PHE A CD2 5306 C CE1 . PHE A 634 ? 0.2440 0.2500 0.2633 0.0176 -0.0412 -0.0297 675 PHE A CE1 5307 C CE2 . PHE A 634 ? 0.2615 0.2692 0.2705 0.0246 -0.0430 -0.0322 675 PHE A CE2 5308 C CZ . PHE A 634 ? 0.2521 0.2581 0.2691 0.0217 -0.0451 -0.0331 675 PHE A CZ 5309 N N . ILE A 635 ? 0.2037 0.2163 0.1929 0.0187 -0.0220 -0.0156 676 ILE A N 5310 C CA . ILE A 635 ? 0.1985 0.2132 0.1859 0.0168 -0.0186 -0.0130 676 ILE A CA 5311 C C . ILE A 635 ? 0.2060 0.2186 0.1931 0.0156 -0.0192 -0.0112 676 ILE A C 5312 O O . ILE A 635 ? 0.2458 0.2555 0.2318 0.0180 -0.0215 -0.0118 676 ILE A O 5313 C CB . ILE A 635 ? 0.2034 0.2193 0.1868 0.0198 -0.0171 -0.0129 676 ILE A CB 5314 C CG1 . ILE A 635 ? 0.2203 0.2378 0.2035 0.0208 -0.0161 -0.0139 676 ILE A CG1 5315 C CG2 . ILE A 635 ? 0.2097 0.2278 0.1925 0.0182 -0.0147 -0.0106 676 ILE A CG2 5316 C CD1 . ILE A 635 ? 0.2447 0.2652 0.2313 0.0173 -0.0140 -0.0134 676 ILE A CD1 5317 N N . ASP A 636 ? 0.1960 0.2096 0.1833 0.0124 -0.0174 -0.0090 677 ASP A N 5318 C CA . ASP A 636 ? 0.2148 0.2261 0.2004 0.0116 -0.0180 -0.0068 677 ASP A CA 5319 C C . ASP A 636 ? 0.2181 0.2318 0.2008 0.0120 -0.0168 -0.0057 677 ASP A C 5320 O O . ASP A 636 ? 0.2197 0.2360 0.2017 0.0104 -0.0146 -0.0055 677 ASP A O 5321 C CB . ASP A 636 ? 0.2194 0.2294 0.2061 0.0079 -0.0167 -0.0048 677 ASP A CB 5322 C CG . ASP A 636 ? 0.2433 0.2496 0.2275 0.0072 -0.0177 -0.0021 677 ASP A CG 5323 O OD1 . ASP A 636 ? 0.2421 0.2483 0.2234 0.0091 -0.0190 -0.0015 677 ASP A OD1 5324 O OD2 . ASP A 636 ? 0.2600 0.2634 0.2458 0.0047 -0.0171 -0.0004 677 ASP A OD2 5325 N N . PRO A 637 ? 0.2425 0.2556 0.2243 0.0143 -0.0182 -0.0054 678 PRO A N 5326 C CA . PRO A 637 ? 0.2780 0.2941 0.2591 0.0149 -0.0173 -0.0049 678 PRO A CA 5327 C C . PRO A 637 ? 0.2922 0.3082 0.2710 0.0123 -0.0174 -0.0031 678 PRO A C 5328 O O . PRO A 637 ? 0.3395 0.3581 0.3180 0.0121 -0.0171 -0.0031 678 PRO A O 5329 C CB . PRO A 637 ? 0.2777 0.2929 0.2597 0.0180 -0.0190 -0.0050 678 PRO A CB 5330 C CG . PRO A 637 ? 0.3039 0.3145 0.2857 0.0185 -0.0212 -0.0050 678 PRO A CG 5331 C CD . PRO A 637 ? 0.2514 0.2612 0.2337 0.0169 -0.0206 -0.0060 678 PRO A CD 5332 N N . LEU A 638 ? 0.2404 0.2531 0.2174 0.0104 -0.0178 -0.0015 679 LEU A N 5333 C CA . LEU A 638 ? 0.2469 0.2589 0.2196 0.0083 -0.0175 0.0004 679 LEU A CA 5334 C C . LEU A 638 ? 0.2654 0.2791 0.2368 0.0059 -0.0143 0.0000 679 LEU A C 5335 O O . LEU A 638 ? 0.2757 0.2889 0.2423 0.0045 -0.0136 0.0011 679 LEU A O 5336 C CB . LEU A 638 ? 0.2467 0.2534 0.2169 0.0077 -0.0189 0.0031 679 LEU A CB 5337 C CG . LEU A 638 ? 0.2764 0.2809 0.2478 0.0104 -0.0224 0.0035 679 LEU A CG 5338 C CD1 . LEU A 638 ? 0.2973 0.2956 0.2661 0.0097 -0.0237 0.0066 679 LEU A CD1 5339 C CD2 . LEU A 638 ? 0.3075 0.3149 0.2780 0.0121 -0.0243 0.0032 679 LEU A CD2 5340 N N . GLY A 639 ? 0.2432 0.2588 0.2184 0.0057 -0.0126 -0.0018 680 GLY A N 5341 C CA . GLY A 639 ? 0.2446 0.2623 0.2202 0.0037 -0.0095 -0.0026 680 GLY A CA 5342 C C . GLY A 639 ? 0.2594 0.2748 0.2343 0.0012 -0.0074 -0.0009 680 GLY A C 5343 O O . GLY A 639 ? 0.2843 0.2960 0.2580 0.0007 -0.0084 0.0013 680 GLY A O 5344 N N . LEU A 640 ? 0.2553 0.2727 0.2313 -0.0005 -0.0041 -0.0016 681 LEU A N 5345 C CA . LEU A 640 ? 0.2690 0.2847 0.2446 -0.0030 -0.0009 0.0002 681 LEU A CA 5346 C C . LEU A 640 ? 0.2889 0.3025 0.2555 -0.0037 0.0006 0.0022 681 LEU A C 5347 O O . LEU A 640 ? 0.2906 0.3053 0.2528 -0.0025 -0.0009 0.0012 681 LEU A O 5348 C CB . LEU A 640 ? 0.2651 0.2845 0.2467 -0.0040 0.0022 -0.0018 681 LEU A CB 5349 C CG . LEU A 640 ? 0.2720 0.2926 0.2619 -0.0031 0.0000 -0.0037 681 LEU A CG 5350 C CD1 . LEU A 640 ? 0.3127 0.3374 0.3084 -0.0032 0.0019 -0.0063 681 LEU A CD1 5351 C CD2 . LEU A 640 ? 0.3264 0.3441 0.3212 -0.0048 -0.0004 -0.0022 681 LEU A CD2 5352 N N . PRO A 641 ? 0.3183 0.3287 0.2820 -0.0057 0.0036 0.0052 682 PRO A N 5353 C CA . PRO A 641 ? 0.3367 0.3440 0.2897 -0.0058 0.0049 0.0073 682 PRO A CA 5354 C C . PRO A 641 ? 0.3363 0.3461 0.2845 -0.0053 0.0063 0.0049 682 PRO A C 5355 O O . PRO A 641 ? 0.3502 0.3629 0.3016 -0.0063 0.0103 0.0032 682 PRO A O 5356 C CB . PRO A 641 ? 0.3536 0.3575 0.3060 -0.0083 0.0098 0.0108 682 PRO A CB 5357 C CG . PRO A 641 ? 0.3520 0.3555 0.3140 -0.0090 0.0082 0.0111 682 PRO A CG 5358 C CD . PRO A 641 ? 0.3368 0.3458 0.3069 -0.0077 0.0059 0.0067 682 PRO A CD 5359 N N . ASP A 642 ? 0.3396 0.3484 0.2809 -0.0037 0.0027 0.0044 683 ASP A N 5360 C CA . ASP A 642 ? 0.3519 0.3624 0.2885 -0.0030 0.0028 0.0016 683 ASP A CA 5361 C C . ASP A 642 ? 0.3241 0.3397 0.2688 -0.0028 0.0034 -0.0021 683 ASP A C 5362 O O . ASP A 642 ? 0.3264 0.3433 0.2684 -0.0025 0.0042 -0.0047 683 ASP A O 5363 C CB . ASP A 642 ? 0.3924 0.4003 0.3198 -0.0038 0.0073 0.0026 683 ASP A CB 5364 C CG . ASP A 642 ? 0.4793 0.4811 0.3965 -0.0035 0.0067 0.0067 683 ASP A CG 5365 O OD1 . ASP A 642 ? 0.5290 0.5286 0.4407 -0.0017 0.0014 0.0069 683 ASP A OD1 5366 O OD2 . ASP A 642 ? 0.5521 0.5513 0.4676 -0.0051 0.0117 0.0099 683 ASP A OD2 5367 N N . ARG A 643 ? 0.2892 0.3071 0.2430 -0.0027 0.0026 -0.0025 684 ARG A N 5368 C CA . ARG A 643 ? 0.2725 0.2944 0.2334 -0.0020 0.0027 -0.0055 684 ARG A CA 5369 C C . ARG A 643 ? 0.2498 0.2725 0.2153 -0.0004 -0.0011 -0.0056 684 ARG A C 5370 O O . ARG A 643 ? 0.2494 0.2729 0.2208 0.0001 -0.0013 -0.0058 684 ARG A O 5371 C CB . ARG A 643 ? 0.2794 0.3034 0.2464 -0.0031 0.0065 -0.0063 684 ARG A CB 5372 C CG . ARG A 643 ? 0.2685 0.2921 0.2310 -0.0044 0.0111 -0.0064 684 ARG A CG 5373 C CD . ARG A 643 ? 0.2781 0.3051 0.2489 -0.0050 0.0149 -0.0080 684 ARG A CD 5374 N NE . ARG A 643 ? 0.2916 0.3185 0.2691 -0.0062 0.0152 -0.0063 684 ARG A NE 5375 C CZ . ARG A 643 ? 0.2849 0.3149 0.2721 -0.0066 0.0168 -0.0076 684 ARG A CZ 5376 N NH1 . ARG A 643 ? 0.2832 0.3165 0.2743 -0.0059 0.0185 -0.0104 684 ARG A NH1 5377 N NH2 . ARG A 643 ? 0.2761 0.3056 0.2697 -0.0077 0.0163 -0.0062 684 ARG A NH2 5378 N N . PRO A 644 ? 0.2487 0.2710 0.2117 0.0007 -0.0042 -0.0058 685 PRO A N 5379 C CA . PRO A 644 ? 0.2466 0.2695 0.2137 0.0024 -0.0072 -0.0056 685 PRO A CA 5380 C C . PRO A 644 ? 0.2287 0.2543 0.2020 0.0036 -0.0065 -0.0072 685 PRO A C 5381 O O . PRO A 644 ? 0.2447 0.2702 0.2208 0.0052 -0.0079 -0.0069 685 PRO A O 5382 C CB . PRO A 644 ? 0.2622 0.2852 0.2268 0.0032 -0.0103 -0.0059 685 PRO A CB 5383 C CG . PRO A 644 ? 0.2595 0.2827 0.2198 0.0022 -0.0091 -0.0075 685 PRO A CG 5384 C CD . PRO A 644 ? 0.2652 0.2867 0.2219 0.0006 -0.0053 -0.0065 685 PRO A CD 5385 N N . PHE A 645 ? 0.2095 0.2368 0.1843 0.0031 -0.0042 -0.0090 686 PHE A N 5386 C CA . PHE A 645 ? 0.2104 0.2394 0.1900 0.0045 -0.0035 -0.0101 686 PHE A CA 5387 C C . PHE A 645 ? 0.2108 0.2399 0.1932 0.0047 -0.0023 -0.0104 686 PHE A C 5388 O O . PHE A 645 ? 0.2216 0.2514 0.2068 0.0063 -0.0022 -0.0113 686 PHE A O 5389 C CB . PHE A 645 ? 0.2221 0.2525 0.2027 0.0043 -0.0023 -0.0119 686 PHE A CB 5390 C CG . PHE A 645 ? 0.2093 0.2400 0.1895 0.0043 -0.0043 -0.0121 686 PHE A CG 5391 C CD1 . PHE A 645 ? 0.2155 0.2467 0.1986 0.0058 -0.0057 -0.0112 686 PHE A CD1 5392 C CD2 . PHE A 645 ? 0.2384 0.2687 0.2152 0.0030 -0.0049 -0.0134 686 PHE A CD2 5393 C CE1 . PHE A 645 ? 0.2058 0.2381 0.1906 0.0057 -0.0077 -0.0116 686 PHE A CE1 5394 C CE2 . PHE A 645 ? 0.2546 0.2854 0.2318 0.0031 -0.0077 -0.0140 686 PHE A CE2 5395 C CZ . PHE A 645 ? 0.2355 0.2676 0.2177 0.0043 -0.0091 -0.0131 686 PHE A CZ 5396 N N A TYR A 646 ? 0.1974 0.2256 0.1790 0.0031 -0.0015 -0.0097 687 TYR A N 5397 N N B TYR A 646 ? 0.1987 0.2269 0.1804 0.0031 -0.0015 -0.0097 687 TYR A N 5398 C CA A TYR A 646 ? 0.1969 0.2254 0.1830 0.0032 -0.0013 -0.0101 687 TYR A CA 5399 C CA B TYR A 646 ? 0.1991 0.2275 0.1853 0.0032 -0.0013 -0.0101 687 TYR A CA 5400 C C A TYR A 646 ? 0.1987 0.2247 0.1844 0.0036 -0.0038 -0.0087 687 TYR A C 5401 C C B TYR A 646 ? 0.2023 0.2284 0.1885 0.0035 -0.0037 -0.0087 687 TYR A C 5402 O O A TYR A 646 ? 0.2182 0.2422 0.2015 0.0021 -0.0037 -0.0069 687 TYR A O 5403 O O B TYR A 646 ? 0.2227 0.2470 0.2074 0.0018 -0.0033 -0.0070 687 TYR A O 5404 C CB A TYR A 646 ? 0.2060 0.2354 0.1936 0.0010 0.0018 -0.0102 687 TYR A CB 5405 C CB B TYR A 646 ? 0.2081 0.2376 0.1959 0.0010 0.0019 -0.0103 687 TYR A CB 5406 C CG A TYR A 646 ? 0.1909 0.2225 0.1794 0.0010 0.0043 -0.0122 687 TYR A CG 5407 C CG B TYR A 646 ? 0.1961 0.2278 0.1848 0.0009 0.0044 -0.0122 687 TYR A CG 5408 C CD1 A TYR A 646 ? 0.2103 0.2429 0.2005 0.0030 0.0033 -0.0136 687 TYR A CD1 5409 C CD1 B TYR A 646 ? 0.2208 0.2535 0.2112 0.0029 0.0035 -0.0137 687 TYR A CD1 5410 C CD2 A TYR A 646 ? 0.2223 0.2546 0.2098 -0.0007 0.0078 -0.0125 687 TYR A CD2 5411 C CD2 B TYR A 646 ? 0.2241 0.2564 0.2119 -0.0009 0.0080 -0.0124 687 TYR A CD2 5412 C CE1 A TYR A 646 ? 0.2314 0.2654 0.2231 0.0032 0.0053 -0.0154 687 TYR A CE1 5413 C CE1 B TYR A 646 ? 0.2375 0.2716 0.2292 0.0030 0.0056 -0.0155 687 TYR A CE1 5414 C CE2 A TYR A 646 ? 0.2150 0.2491 0.2036 -0.0004 0.0100 -0.0146 687 TYR A CE2 5415 C CE2 B TYR A 646 ? 0.2314 0.2656 0.2202 -0.0006 0.0103 -0.0146 687 TYR A CE2 5416 C CZ A TYR A 646 ? 0.2326 0.2675 0.2237 0.0015 0.0085 -0.0162 687 TYR A CZ 5417 C CZ B TYR A 646 ? 0.2492 0.2842 0.2404 0.0013 0.0088 -0.0162 687 TYR A CZ 5418 O OH A TYR A 646 ? 0.2446 0.2806 0.2371 0.0020 0.0105 -0.0183 687 TYR A OH 5419 O OH B TYR A 646 ? 0.2510 0.2872 0.2435 0.0017 0.0110 -0.0183 687 TYR A OH 5420 N N . ARG A 647 ? 0.1808 0.2064 0.1684 0.0060 -0.0060 -0.0094 688 ARG A N 5421 C CA . ARG A 647 ? 0.1760 0.1990 0.1630 0.0070 -0.0086 -0.0086 688 ARG A CA 5422 C C . ARG A 647 ? 0.1802 0.2020 0.1712 0.0077 -0.0105 -0.0098 688 ARG A C 5423 O O . ARG A 647 ? 0.1996 0.2187 0.1906 0.0084 -0.0128 -0.0095 688 ARG A O 5424 C CB A ARG A 647 ? 0.1775 0.2004 0.1624 0.0097 -0.0099 -0.0086 688 ARG A CB 5425 C CB B ARG A 647 ? 0.1868 0.2098 0.1717 0.0098 -0.0097 -0.0087 688 ARG A CB 5426 C CG A ARG A 647 ? 0.1593 0.1836 0.1419 0.0088 -0.0088 -0.0077 688 ARG A CG 5427 C CG B ARG A 647 ? 0.2093 0.2342 0.1925 0.0091 -0.0082 -0.0083 688 ARG A CG 5428 C CD A ARG A 647 ? 0.1240 0.1485 0.1063 0.0109 -0.0099 -0.0074 688 ARG A CD 5429 C CD B ARG A 647 ? 0.2733 0.2986 0.2564 0.0114 -0.0089 -0.0081 688 ARG A CD 5430 N NE A ARG A 647 ? 0.1336 0.1584 0.1170 0.0138 -0.0094 -0.0083 688 ARG A NE 5431 N NE B ARG A 647 ? 0.3042 0.3309 0.2868 0.0103 -0.0086 -0.0077 688 ARG A NE 5432 C CZ A ARG A 647 ? 0.1792 0.2037 0.1627 0.0163 -0.0098 -0.0080 688 ARG A CZ 5433 C CZ B ARG A 647 ? 0.3693 0.3954 0.3504 0.0097 -0.0104 -0.0067 688 ARG A CZ 5434 N NH1 A ARG A 647 ? 0.1610 0.1850 0.1439 0.0191 -0.0087 -0.0086 688 ARG A NH1 5435 N NH1 B ARG A 647 ? 0.3375 0.3650 0.3185 0.0090 -0.0110 -0.0068 688 ARG A NH1 5436 N NH2 A ARG A 647 ? 0.1925 0.2170 0.1764 0.0163 -0.0111 -0.0071 688 ARG A NH2 5437 N NH2 B ARG A 647 ? 0.4067 0.4301 0.3865 0.0100 -0.0121 -0.0056 688 ARG A NH2 5438 N N . HIS A 648 ? 0.1807 0.2043 0.1757 0.0076 -0.0100 -0.0115 689 HIS A N 5439 C CA . HIS A 648 ? 0.1850 0.2077 0.1846 0.0086 -0.0128 -0.0134 689 HIS A CA 5440 C C . HIS A 648 ? 0.1968 0.2189 0.2012 0.0052 -0.0119 -0.0124 689 HIS A C 5441 O O . HIS A 648 ? 0.2107 0.2346 0.2165 0.0025 -0.0084 -0.0113 689 HIS A O 5442 C CB . HIS A 648 ? 0.1990 0.2241 0.2015 0.0100 -0.0128 -0.0154 689 HIS A CB 5443 C CG . HIS A 648 ? 0.1855 0.2093 0.1907 0.0126 -0.0170 -0.0179 689 HIS A CG 5444 N ND1 . HIS A 648 ? 0.1956 0.2189 0.2076 0.0112 -0.0194 -0.0193 689 HIS A ND1 5445 C CD2 . HIS A 648 ? 0.1921 0.2147 0.1937 0.0166 -0.0194 -0.0194 689 HIS A CD2 5446 C CE1 . HIS A 648 ? 0.2190 0.2409 0.2316 0.0145 -0.0238 -0.0221 689 HIS A CE1 5447 N NE2 . HIS A 648 ? 0.2093 0.2305 0.2147 0.0180 -0.0238 -0.0220 689 HIS A NE2 5448 N N . VAL A 649 ? 0.1854 0.2044 0.1921 0.0054 -0.0148 -0.0128 690 VAL A N 5449 C CA . VAL A 649 ? 0.1816 0.1991 0.1933 0.0019 -0.0137 -0.0113 690 VAL A CA 5450 C C . VAL A 649 ? 0.1971 0.2170 0.2189 0.0004 -0.0138 -0.0133 690 VAL A C 5451 O O . VAL A 649 ? 0.2111 0.2312 0.2385 -0.0031 -0.0109 -0.0118 690 VAL A O 5452 C CB . VAL A 649 ? 0.1874 0.2000 0.1979 0.0027 -0.0169 -0.0107 690 VAL A CB 5453 C CG1 . VAL A 649 ? 0.2222 0.2321 0.2390 -0.0008 -0.0162 -0.0091 690 VAL A CG1 5454 C CG2 . VAL A 649 ? 0.2130 0.2240 0.2152 0.0039 -0.0164 -0.0084 690 VAL A CG2 5455 N N . ILE A 650 ? 0.1865 0.2082 0.2109 0.0031 -0.0169 -0.0166 691 ILE A N 5456 C CA . ILE A 650 ? 0.1953 0.2195 0.2307 0.0019 -0.0179 -0.0190 691 ILE A CA 5457 C C . ILE A 650 ? 0.1926 0.2216 0.2307 0.0009 -0.0139 -0.0189 691 ILE A C 5458 O O . ILE A 650 ? 0.2021 0.2340 0.2500 -0.0016 -0.0118 -0.0193 691 ILE A O 5459 C CB . ILE A 650 ? 0.1967 0.2201 0.2338 0.0057 -0.0242 -0.0230 691 ILE A CB 5460 C CG1 . ILE A 650 ? 0.2099 0.2282 0.2423 0.0078 -0.0284 -0.0237 691 ILE A CG1 5461 C CG2 . ILE A 650 ? 0.2118 0.2379 0.2627 0.0042 -0.0262 -0.0257 691 ILE A CG2 5462 C CD1 . ILE A 650 ? 0.2461 0.2613 0.2837 0.0044 -0.0281 -0.0222 691 ILE A CD1 5463 N N . TYR A 651 ? 0.1996 0.2296 0.2299 0.0030 -0.0125 -0.0185 692 TYR A N 5464 C CA . TYR A 651 ? 0.2022 0.2362 0.2346 0.0026 -0.0091 -0.0190 692 TYR A CA 5465 C C . TYR A 651 ? 0.2172 0.2510 0.2413 0.0018 -0.0050 -0.0167 692 TYR A C 5466 O O . TYR A 651 ? 0.2384 0.2697 0.2544 0.0032 -0.0061 -0.0156 692 TYR A O 5467 C CB . TYR A 651 ? 0.2074 0.2422 0.2391 0.0067 -0.0126 -0.0215 692 TYR A CB 5468 C CG . TYR A 651 ? 0.1854 0.2205 0.2248 0.0083 -0.0178 -0.0246 692 TYR A CG 5469 C CD1 . TYR A 651 ? 0.2093 0.2482 0.2612 0.0063 -0.0172 -0.0263 692 TYR A CD1 5470 C CD2 . TYR A 651 ? 0.2156 0.2473 0.2502 0.0121 -0.0233 -0.0263 692 TYR A CD2 5471 C CE1 . TYR A 651 ? 0.2116 0.2511 0.2720 0.0078 -0.0228 -0.0296 692 TYR A CE1 5472 C CE2 . TYR A 651 ? 0.2302 0.2617 0.2712 0.0140 -0.0289 -0.0296 692 TYR A CE2 5473 C CZ . TYR A 651 ? 0.2286 0.2642 0.2829 0.0118 -0.0290 -0.0314 692 TYR A CZ 5474 O OH . TYR A 651 ? 0.2301 0.2661 0.2927 0.0136 -0.0354 -0.0353 692 TYR A OH 5475 N N . ALA A 652 ? 0.2002 0.2366 0.2262 -0.0002 -0.0003 -0.0163 693 ALA A N 5476 C CA . ALA A 652 ? 0.2056 0.2421 0.2236 -0.0001 0.0027 -0.0153 693 ALA A CA 5477 C C . ALA A 652 ? 0.2170 0.2570 0.2396 -0.0007 0.0064 -0.0167 693 ALA A C 5478 O O . ALA A 652 ? 0.2217 0.2643 0.2535 -0.0018 0.0077 -0.0177 693 ALA A O 5479 C CB . ALA A 652 ? 0.2127 0.2466 0.2241 -0.0024 0.0052 -0.0124 693 ALA A CB 5480 N N . PRO A 653 ? 0.2042 0.2444 0.2213 0.0001 0.0082 -0.0171 694 PRO A N 5481 C CA . PRO A 653 ? 0.2115 0.2548 0.2325 -0.0004 0.0123 -0.0186 694 PRO A CA 5482 C C . PRO A 653 ? 0.2080 0.2516 0.2293 -0.0035 0.0173 -0.0170 694 PRO A C 5483 O O . PRO A 653 ? 0.2294 0.2700 0.2433 -0.0048 0.0181 -0.0146 694 PRO A O 5484 C CB . PRO A 653 ? 0.2081 0.2501 0.2214 0.0007 0.0130 -0.0190 694 PRO A CB 5485 C CG . PRO A 653 ? 0.2049 0.2445 0.2142 0.0026 0.0086 -0.0183 694 PRO A CG 5486 C CD . PRO A 653 ? 0.2222 0.2601 0.2309 0.0015 0.0067 -0.0164 694 PRO A CD 5487 N N . SER A 654 ? 0.2044 0.2516 0.2345 -0.0044 0.0208 -0.0182 695 SER A N 5488 C CA . SER A 654 ? 0.2181 0.2657 0.2490 -0.0072 0.0268 -0.0165 695 SER A CA 5489 C C . SER A 654 ? 0.2384 0.2834 0.2569 -0.0075 0.0304 -0.0154 695 SER A C 5490 O O . SER A 654 ? 0.2379 0.2832 0.2524 -0.0058 0.0306 -0.0175 695 SER A O 5491 C CB . SER A 654 ? 0.2229 0.2755 0.2659 -0.0075 0.0307 -0.0186 695 SER A CB 5492 O OG . SER A 654 ? 0.2498 0.3028 0.2930 -0.0101 0.0378 -0.0166 695 SER A OG 5493 N N . SER A 655 ? 0.2337 0.2755 0.2457 -0.0095 0.0331 -0.0122 696 SER A N 5494 C CA . SER A 655 ? 0.2614 0.3002 0.2602 -0.0095 0.0361 -0.0112 696 SER A CA 5495 C C . SER A 655 ? 0.2562 0.2973 0.2556 -0.0094 0.0427 -0.0130 696 SER A C 5496 O O . SER A 655 ? 0.2953 0.3339 0.2834 -0.0087 0.0449 -0.0133 696 SER A O 5497 C CB . SER A 655 ? 0.2612 0.2954 0.2527 -0.0113 0.0376 -0.0069 696 SER A CB 5498 O OG A SER A 655 ? 0.1927 0.2242 0.1817 -0.0108 0.0315 -0.0056 696 SER A OG 5499 O OG B SER A 655 ? 0.3603 0.3956 0.3590 -0.0137 0.0431 -0.0049 696 SER A OG 5500 N N . HIS A 656 ? 0.2581 0.3039 0.2705 -0.0099 0.0455 -0.0144 697 HIS A N 5501 C CA . HIS A 656 ? 0.2711 0.3200 0.2865 -0.0095 0.0523 -0.0164 697 HIS A CA 5502 C C . HIS A 656 ? 0.2731 0.3255 0.2955 -0.0071 0.0500 -0.0207 697 HIS A C 5503 O O . HIS A 656 ? 0.2781 0.3329 0.3027 -0.0062 0.0547 -0.0231 697 HIS A O 5504 C CB . HIS A 656 ? 0.2864 0.3381 0.3125 -0.0120 0.0584 -0.0146 697 HIS A CB 5505 C CG . HIS A 656 ? 0.3000 0.3471 0.3190 -0.0144 0.0606 -0.0098 697 HIS A CG 5506 N ND1 . HIS A 656 ? 0.3505 0.3935 0.3558 -0.0147 0.0664 -0.0075 697 HIS A ND1 5507 C CD2 . HIS A 656 ? 0.3457 0.3907 0.3678 -0.0162 0.0573 -0.0069 697 HIS A CD2 5508 C CE1 . HIS A 656 ? 0.3935 0.4321 0.3942 -0.0166 0.0666 -0.0029 697 HIS A CE1 5509 N NE2 . HIS A 656 ? 0.3509 0.3907 0.3620 -0.0176 0.0612 -0.0026 697 HIS A NE2 5510 N N . ASN A 657 ? 0.2400 0.2926 0.2660 -0.0058 0.0430 -0.0216 698 ASN A N 5511 C CA . ASN A 657 ? 0.2307 0.2862 0.2639 -0.0033 0.0405 -0.0251 698 ASN A CA 5512 C C . ASN A 657 ? 0.2245 0.2780 0.2561 -0.0017 0.0330 -0.0250 698 ASN A C 5513 O O . ASN A 657 ? 0.2318 0.2864 0.2706 -0.0016 0.0293 -0.0246 698 ASN A O 5514 C CB . ASN A 657 ? 0.2350 0.2961 0.2847 -0.0033 0.0421 -0.0266 698 ASN A CB 5515 C CG . ASN A 657 ? 0.2269 0.2903 0.2839 -0.0001 0.0386 -0.0300 698 ASN A CG 5516 O OD1 . ASN A 657 ? 0.2295 0.2903 0.2792 0.0019 0.0364 -0.0312 698 ASN A OD1 5517 N ND2 . ASN A 657 ? 0.2223 0.2905 0.2941 0.0004 0.0378 -0.0316 698 ASN A ND2 5518 N N . LYS A 658 ? 0.2431 0.2936 0.2658 -0.0004 0.0310 -0.0257 699 LYS A N 5519 C CA A LYS A 658 ? 0.2436 0.2919 0.2640 0.0011 0.0249 -0.0251 699 LYS A CA 5520 C CA B LYS A 658 ? 0.2494 0.2976 0.2697 0.0012 0.0249 -0.0253 699 LYS A CA 5521 C C . LYS A 658 ? 0.2398 0.2899 0.2692 0.0033 0.0212 -0.0264 699 LYS A C 5522 O O . LYS A 658 ? 0.2488 0.2973 0.2771 0.0044 0.0166 -0.0254 699 LYS A O 5523 C CB A LYS A 658 ? 0.2549 0.3002 0.2666 0.0019 0.0243 -0.0259 699 LYS A CB 5524 C CB B LYS A 658 ? 0.2588 0.3045 0.2718 0.0025 0.0244 -0.0267 699 LYS A CB 5525 C CG A LYS A 658 ? 0.2883 0.3314 0.2975 0.0033 0.0194 -0.0251 699 LYS A CG 5526 C CG B LYS A 658 ? 0.3301 0.3726 0.3322 0.0011 0.0246 -0.0254 699 LYS A CG 5527 C CD A LYS A 658 ? 0.3140 0.3547 0.3170 0.0037 0.0194 -0.0263 699 LYS A CD 5528 C CD B LYS A 658 ? 0.3777 0.4179 0.3767 0.0017 0.0198 -0.0241 699 LYS A CD 5529 C CE A LYS A 658 ? 0.3433 0.3815 0.3413 0.0036 0.0158 -0.0244 699 LYS A CE 5530 C CE B LYS A 658 ? 0.4195 0.4569 0.4093 0.0010 0.0190 -0.0237 699 LYS A CE 5531 N NZ A LYS A 658 ? 0.4037 0.4399 0.3981 0.0038 0.0154 -0.0259 699 LYS A NZ 5532 N NZ B LYS A 658 ? 0.4481 0.4842 0.4379 0.0021 0.0151 -0.0234 699 LYS A NZ 5533 N N . TYR A 659 ? 0.2272 0.2807 0.2654 0.0044 0.0231 -0.0288 700 TYR A N 5534 C CA . TYR A 659 ? 0.2231 0.2781 0.2694 0.0071 0.0188 -0.0301 700 TYR A CA 5535 C C . TYR A 659 ? 0.2339 0.2907 0.2876 0.0065 0.0159 -0.0296 700 TYR A C 5536 O O . TYR A 659 ? 0.2500 0.3067 0.3076 0.0091 0.0108 -0.0305 700 TYR A O 5537 C CB . TYR A 659 ? 0.2237 0.2821 0.2787 0.0087 0.0212 -0.0330 700 TYR A CB 5538 C CG . TYR A 659 ? 0.2299 0.2861 0.2796 0.0101 0.0232 -0.0344 700 TYR A CG 5539 C CD1 . TYR A 659 ? 0.2471 0.2989 0.2887 0.0113 0.0203 -0.0336 700 TYR A CD1 5540 C CD2 . TYR A 659 ? 0.2433 0.3020 0.2972 0.0102 0.0283 -0.0369 700 TYR A CD2 5541 C CE1 . TYR A 659 ? 0.2644 0.3138 0.3025 0.0123 0.0219 -0.0352 700 TYR A CE1 5542 C CE2 . TYR A 659 ? 0.2556 0.3119 0.3049 0.0116 0.0298 -0.0387 700 TYR A CE2 5543 C CZ . TYR A 659 ? 0.2626 0.3142 0.3046 0.0126 0.0262 -0.0379 700 TYR A CZ 5544 O OH . TYR A 659 ? 0.2673 0.3161 0.3060 0.0137 0.0274 -0.0399 700 TYR A OH 5545 N N . ALA A 660 ? 0.2161 0.2744 0.2724 0.0034 0.0191 -0.0284 701 ALA A N 5546 C CA . ALA A 660 ? 0.2246 0.2848 0.2902 0.0025 0.0165 -0.0284 701 ALA A CA 5547 C C . ALA A 660 ? 0.2414 0.2975 0.2996 0.0015 0.0132 -0.0260 701 ALA A C 5548 O O . ALA A 660 ? 0.2572 0.3104 0.3055 0.0000 0.0155 -0.0237 701 ALA A O 5549 C CB . ALA A 660 ? 0.2316 0.2954 0.3052 -0.0007 0.0226 -0.0280 701 ALA A CB 5550 N N . GLY A 661 ? 0.2231 0.2789 0.2862 0.0026 0.0076 -0.0267 702 GLY A N 5551 C CA . GLY A 661 ? 0.2330 0.2849 0.2901 0.0017 0.0048 -0.0247 702 GLY A CA 5552 C C . GLY A 661 ? 0.2268 0.2799 0.2912 -0.0020 0.0075 -0.0235 702 GLY A C 5553 O O . GLY A 661 ? 0.2489 0.3062 0.3259 -0.0032 0.0093 -0.0250 702 GLY A O 5554 N N . GLU A 662 ? 0.2039 0.2531 0.2611 -0.0038 0.0081 -0.0208 703 GLU A N 5555 C CA . GLU A 662 ? 0.2072 0.2560 0.2701 -0.0074 0.0105 -0.0189 703 GLU A CA 5556 C C . GLU A 662 ? 0.2060 0.2509 0.2677 -0.0068 0.0046 -0.0187 703 GLU A C 5557 O O . GLU A 662 ? 0.2273 0.2689 0.2787 -0.0046 0.0016 -0.0183 703 GLU A O 5558 C CB . GLU A 662 ? 0.2145 0.2612 0.2687 -0.0098 0.0169 -0.0154 703 GLU A CB 5559 C CG . GLU A 662 ? 0.2402 0.2859 0.3005 -0.0136 0.0205 -0.0128 703 GLU A CG 5560 C CD . GLU A 662 ? 0.2873 0.3384 0.3643 -0.0151 0.0230 -0.0147 703 GLU A CD 5561 O OE1 . GLU A 662 ? 0.2868 0.3413 0.3657 -0.0156 0.0291 -0.0149 703 GLU A OE1 5562 O OE2 . GLU A 662 ? 0.3124 0.3646 0.4015 -0.0155 0.0186 -0.0164 703 GLU A OE2 5563 N N . SER A 663 ? 0.2045 0.2497 0.2771 -0.0087 0.0032 -0.0192 704 SER A N 5564 C CA A SER A 663 ? 0.1875 0.2284 0.2592 -0.0082 -0.0025 -0.0194 704 SER A CA 5565 C CA B SER A 663 ? 0.2136 0.2543 0.2846 -0.0081 -0.0025 -0.0193 704 SER A CA 5566 C C . SER A 663 ? 0.2047 0.2414 0.2721 -0.0112 0.0008 -0.0154 704 SER A C 5567 O O . SER A 663 ? 0.2054 0.2430 0.2756 -0.0145 0.0072 -0.0128 704 SER A O 5568 C CB A SER A 663 ? 0.1888 0.2315 0.2750 -0.0081 -0.0075 -0.0229 704 SER A CB 5569 C CB B SER A 663 ? 0.2196 0.2619 0.3043 -0.0078 -0.0078 -0.0229 704 SER A CB 5570 O OG A SER A 663 ? 0.1163 0.1632 0.2170 -0.0117 -0.0032 -0.0229 704 SER A OG 5571 O OG B SER A 663 ? 0.3097 0.3572 0.4024 -0.0062 -0.0086 -0.0259 704 SER A OG 5572 N N . PHE A 664 ? 0.1972 0.2288 0.2576 -0.0099 -0.0035 -0.0148 705 PHE A N 5573 C CA . PHE A 664 ? 0.1991 0.2258 0.2538 -0.0122 -0.0012 -0.0107 705 PHE A CA 5574 C C . PHE A 664 ? 0.2086 0.2359 0.2556 -0.0138 0.0057 -0.0073 705 PHE A C 5575 O O . PHE A 664 ? 0.2081 0.2336 0.2563 -0.0169 0.0106 -0.0040 705 PHE A O 5576 C CB . PHE A 664 ? 0.1969 0.2215 0.2631 -0.0154 -0.0014 -0.0101 705 PHE A CB 5577 C CG . PHE A 664 ? 0.1962 0.2181 0.2663 -0.0134 -0.0091 -0.0133 705 PHE A CG 5578 C CD1 . PHE A 664 ? 0.1926 0.2102 0.2517 -0.0103 -0.0131 -0.0134 705 PHE A CD1 5579 C CD2 . PHE A 664 ? 0.2165 0.2403 0.3013 -0.0143 -0.0123 -0.0167 705 PHE A CD2 5580 C CE1 . PHE A 664 ? 0.2035 0.2182 0.2644 -0.0077 -0.0201 -0.0169 705 PHE A CE1 5581 C CE2 . PHE A 664 ? 0.2159 0.2367 0.3030 -0.0119 -0.0201 -0.0204 705 PHE A CE2 5582 C CZ . PHE A 664 ? 0.2084 0.2243 0.2827 -0.0085 -0.0238 -0.0204 705 PHE A CZ 5583 N N . PRO A 665 ? 0.1958 0.2244 0.2337 -0.0114 0.0059 -0.0080 706 PRO A N 5584 C CA . PRO A 665 ? 0.2070 0.2364 0.2376 -0.0124 0.0117 -0.0058 706 PRO A CA 5585 C C . PRO A 665 ? 0.2088 0.2331 0.2305 -0.0140 0.0141 -0.0015 706 PRO A C 5586 O O . PRO A 665 ? 0.2303 0.2545 0.2486 -0.0157 0.0199 0.0007 706 PRO A O 5587 C CB . PRO A 665 ? 0.1955 0.2263 0.2184 -0.0092 0.0095 -0.0078 706 PRO A CB 5588 C CG . PRO A 665 ? 0.2229 0.2517 0.2451 -0.0065 0.0029 -0.0093 706 PRO A CG 5589 C CD . PRO A 665 ? 0.1947 0.2243 0.2292 -0.0075 0.0008 -0.0109 706 PRO A CD 5590 N N . GLY A 666 ? 0.2167 0.2366 0.2340 -0.0130 0.0098 -0.0004 707 GLY A N 5591 C CA . GLY A 666 ? 0.2188 0.2336 0.2269 -0.0140 0.0116 0.0039 707 GLY A CA 5592 C C . GLY A 666 ? 0.2255 0.2380 0.2394 -0.0175 0.0161 0.0071 707 GLY A C 5593 O O . GLY A 666 ? 0.2331 0.2428 0.2398 -0.0190 0.0212 0.0108 707 GLY A O 5594 N N . ILE A 667 ? 0.2018 0.2151 0.2288 -0.0189 0.0146 0.0056 708 ILE A N 5595 C CA . ILE A 667 ? 0.2173 0.2288 0.2524 -0.0228 0.0195 0.0086 708 ILE A CA 5596 C C . ILE A 667 ? 0.2242 0.2405 0.2632 -0.0246 0.0269 0.0087 708 ILE A C 5597 O O . ILE A 667 ? 0.2433 0.2574 0.2801 -0.0270 0.0337 0.0129 708 ILE A O 5598 C CB . ILE A 667 ? 0.1919 0.2032 0.2418 -0.0240 0.0156 0.0064 708 ILE A CB 5599 C CG1 . ILE A 667 ? 0.2361 0.2431 0.2821 -0.0215 0.0081 0.0052 708 ILE A CG1 5600 C CG2 . ILE A 667 ? 0.2304 0.2384 0.2879 -0.0283 0.0210 0.0106 708 ILE A CG2 5601 C CD1 . ILE A 667 ? 0.2419 0.2488 0.3019 -0.0219 0.0028 0.0015 708 ILE A CD1 5602 N N . TYR A 668 ? 0.2265 0.2491 0.2707 -0.0230 0.0257 0.0043 709 TYR A N 5603 C CA . TYR A 668 ? 0.2441 0.2719 0.2937 -0.0242 0.0322 0.0037 709 TYR A CA 5604 C C . TYR A 668 ? 0.2349 0.2603 0.2697 -0.0242 0.0382 0.0070 709 TYR A C 5605 O O . TYR A 668 ? 0.2418 0.2671 0.2778 -0.0264 0.0460 0.0096 709 TYR A O 5606 C CB . TYR A 668 ? 0.2119 0.2458 0.2667 -0.0217 0.0289 -0.0015 709 TYR A CB 5607 C CG . TYR A 668 ? 0.2325 0.2718 0.2942 -0.0228 0.0358 -0.0024 709 TYR A CG 5608 C CD1 . TYR A 668 ? 0.2479 0.2920 0.3278 -0.0247 0.0373 -0.0041 709 TYR A CD1 5609 C CD2 . TYR A 668 ? 0.2512 0.2907 0.3016 -0.0218 0.0408 -0.0016 709 TYR A CD2 5610 C CE1 . TYR A 668 ? 0.2512 0.3007 0.3388 -0.0256 0.0443 -0.0049 709 TYR A CE1 5611 C CE2 . TYR A 668 ? 0.2559 0.3000 0.3122 -0.0226 0.0477 -0.0025 709 TYR A CE2 5612 C CZ . TYR A 668 ? 0.2848 0.3341 0.3599 -0.0244 0.0496 -0.0041 709 TYR A CZ 5613 O OH . TYR A 668 ? 0.2890 0.3434 0.3708 -0.0248 0.0568 -0.0051 709 TYR A OH 5614 N N . ASP A 669 ? 0.2491 0.2724 0.2701 -0.0214 0.0348 0.0066 710 ASP A N 5615 C CA . ASP A 669 ? 0.2581 0.2789 0.2646 -0.0209 0.0393 0.0089 710 ASP A CA 5616 C C . ASP A 669 ? 0.2699 0.2838 0.2686 -0.0227 0.0429 0.0146 710 ASP A C 5617 O O . ASP A 669 ? 0.2956 0.3076 0.2861 -0.0234 0.0496 0.0173 710 ASP A O 5618 C CB . ASP A 669 ? 0.2654 0.2857 0.2608 -0.0177 0.0341 0.0068 710 ASP A CB 5619 C CG . ASP A 669 ? 0.3110 0.3372 0.3106 -0.0160 0.0335 0.0021 710 ASP A CG 5620 O OD1 . ASP A 669 ? 0.2993 0.3298 0.3081 -0.0169 0.0377 0.0005 710 ASP A OD1 5621 O OD2 . ASP A 669 ? 0.3295 0.3558 0.3236 -0.0136 0.0288 0.0000 710 ASP A OD2 5622 N N . ALA A 670 ? 0.2442 0.2539 0.2451 -0.0233 0.0386 0.0166 711 ALA A N 5623 C CA . ALA A 670 ? 0.2613 0.2636 0.2556 -0.0250 0.0419 0.0225 711 ALA A CA 5624 C C . ALA A 670 ? 0.2723 0.2749 0.2753 -0.0287 0.0507 0.0254 711 ALA A C 5625 O O . ALA A 670 ? 0.2844 0.2817 0.2785 -0.0298 0.0569 0.0306 711 ALA A O 5626 C CB . ALA A 670 ? 0.2771 0.2747 0.2741 -0.0250 0.0355 0.0237 711 ALA A CB 5627 N N . LEU A 671 ? 0.2629 0.2718 0.2835 -0.0303 0.0513 0.0222 712 LEU A N 5628 C CA . LEU A 671 ? 0.2590 0.2696 0.2919 -0.0340 0.0596 0.0243 712 LEU A CA 5629 C C . LEU A 671 ? 0.2668 0.2821 0.2979 -0.0339 0.0678 0.0236 712 LEU A C 5630 O O . LEU A 671 ? 0.2988 0.3144 0.3355 -0.0365 0.0765 0.0266 712 LEU A O 5631 C CB . LEU A 671 ? 0.2686 0.2842 0.3230 -0.0357 0.0558 0.0205 712 LEU A CB 5632 C CG . LEU A 671 ? 0.2547 0.2647 0.3143 -0.0370 0.0506 0.0221 712 LEU A CG 5633 C CD1 . LEU A 671 ? 0.2629 0.2784 0.3415 -0.0373 0.0444 0.0165 712 LEU A CD1 5634 C CD2 . LEU A 671 ? 0.2686 0.2732 0.3313 -0.0410 0.0585 0.0285 712 LEU A CD2 5635 N N . PHE A 672 ? 0.2622 0.2811 0.2860 -0.0306 0.0649 0.0195 713 PHE A N 5636 C CA . PHE A 672 ? 0.2811 0.3052 0.3060 -0.0302 0.0717 0.0174 713 PHE A CA 5637 C C . PHE A 672 ? 0.2960 0.3152 0.3065 -0.0306 0.0807 0.0222 713 PHE A C 5638 O O . PHE A 672 ? 0.3209 0.3337 0.3128 -0.0287 0.0788 0.0246 713 PHE A O 5639 C CB . PHE A 672 ? 0.2760 0.3037 0.2949 -0.0265 0.0664 0.0122 713 PHE A CB 5640 C CG . PHE A 672 ? 0.3010 0.3341 0.3227 -0.0258 0.0729 0.0095 713 PHE A CG 5641 C CD1 . PHE A 672 ? 0.3183 0.3589 0.3593 -0.0266 0.0739 0.0061 713 PHE A CD1 5642 C CD2 . PHE A 672 ? 0.3265 0.3569 0.3321 -0.0243 0.0780 0.0104 713 PHE A CD2 5643 C CE1 . PHE A 672 ? 0.3528 0.3985 0.3974 -0.0258 0.0802 0.0036 713 PHE A CE1 5644 C CE2 . PHE A 672 ? 0.3539 0.3890 0.3620 -0.0234 0.0846 0.0077 713 PHE A CE2 5645 C CZ . PHE A 672 ? 0.3539 0.3966 0.3818 -0.0242 0.0859 0.0044 713 PHE A CZ 5646 N N . ASP A 673 ? 0.3145 0.3366 0.3337 -0.0328 0.0905 0.0236 714 ASP A N 5647 C CA . ASP A 673 ? 0.3526 0.3700 0.3578 -0.0329 0.1006 0.0282 714 ASP A CA 5648 C C . ASP A 673 ? 0.3813 0.3887 0.3736 -0.0338 0.1009 0.0350 714 ASP A C 5649 O O . ASP A 673 ? 0.4002 0.4013 0.3727 -0.0322 0.1050 0.0384 714 ASP A O 5650 C CB . ASP A 673 ? 0.3568 0.3744 0.3452 -0.0290 0.1007 0.0250 714 ASP A CB 5651 C CG . ASP A 673 ? 0.4042 0.4187 0.3801 -0.0286 0.1122 0.0282 714 ASP A CG 5652 O OD1 . ASP A 673 ? 0.4310 0.4481 0.4185 -0.0313 0.1220 0.0305 714 ASP A OD1 5653 O OD2 . ASP A 673 ? 0.4485 0.4579 0.4030 -0.0255 0.1114 0.0282 714 ASP A OD2 5654 N N . ILE A 674 ? 0.3651 0.3705 0.3681 -0.0362 0.0963 0.0368 715 ILE A N 5655 C CA . ILE A 674 ? 0.3710 0.3664 0.3617 -0.0365 0.0949 0.0429 715 ILE A CA 5656 C C . ILE A 674 ? 0.4079 0.3972 0.3919 -0.0386 0.1066 0.0501 715 ILE A C 5657 O O . ILE A 674 ? 0.4107 0.3906 0.3765 -0.0374 0.1070 0.0554 715 ILE A O 5658 C CB . ILE A 674 ? 0.3606 0.3547 0.3646 -0.0383 0.0870 0.0427 715 ILE A CB 5659 C CG1 . ILE A 674 ? 0.3543 0.3379 0.3440 -0.0377 0.0838 0.0482 715 ILE A CG1 5660 C CG2 . ILE A 674 ? 0.3520 0.3502 0.3798 -0.0427 0.0915 0.0429 715 ILE A CG2 5661 C CD1 . ILE A 674 ? 0.3383 0.3209 0.3376 -0.0380 0.0742 0.0464 715 ILE A CD1 5662 N N . GLU A 675 ? 0.4164 0.4110 0.4148 -0.0413 0.1161 0.0503 716 GLU A N 5663 C CA . GLU A 675 ? 0.4697 0.4591 0.4633 -0.0434 0.1289 0.0573 716 GLU A CA 5664 C C . GLU A 675 ? 0.4951 0.4795 0.4625 -0.0398 0.1344 0.0594 716 GLU A C 5665 O O . GLU A 675 ? 0.5216 0.4989 0.4781 -0.0405 0.1443 0.0662 716 GLU A O 5666 C CB . GLU A 675 ? 0.4644 0.4618 0.4821 -0.0472 0.1380 0.0566 716 GLU A CB 5667 C CG . GLU A 675 ? 0.4878 0.4946 0.5095 -0.0453 0.1421 0.0508 716 GLU A CG 5668 C CD . GLU A 675 ? 0.5172 0.5334 0.5540 -0.0442 0.1319 0.0424 716 GLU A CD 5669 O OE1 . GLU A 675 ? 0.4626 0.4778 0.5017 -0.0437 0.1204 0.0402 716 GLU A OE1 5670 O OE2 . GLU A 675 ? 0.5720 0.5965 0.6180 -0.0434 0.1357 0.0379 716 GLU A OE2 5671 N N . SER A 676 ? 0.4994 0.4867 0.4562 -0.0358 0.1280 0.0536 717 SER A N 5672 C CA . SER A 676 ? 0.5314 0.5140 0.4629 -0.0318 0.1308 0.0540 717 SER A CA 5673 C C . SER A 676 ? 0.5530 0.5268 0.4633 -0.0287 0.1220 0.0559 717 SER A C 5674 O O . SER A 676 ? 0.5817 0.5502 0.4697 -0.0252 0.1234 0.0566 717 SER A O 5675 C CB . SER A 676 ? 0.5260 0.5168 0.4591 -0.0292 0.1297 0.0462 717 SER A CB 5676 O OG . SER A 676 ? 0.5390 0.5378 0.4915 -0.0317 0.1385 0.0448 717 SER A OG 5677 N N . LYS A 677 ? 0.5355 0.5074 0.4523 -0.0297 0.1129 0.0566 718 LYS A N 5678 C CA . LYS A 677 ? 0.5556 0.5197 0.4540 -0.0266 0.1042 0.0582 718 LYS A CA 5679 C C . LYS A 677 ? 0.5873 0.5397 0.4691 -0.0265 0.1100 0.0669 718 LYS A C 5680 O O . LYS A 677 ? 0.5966 0.5462 0.4874 -0.0301 0.1173 0.0725 718 LYS A O 5681 C CB . LYS A 677 ? 0.5371 0.5028 0.4474 -0.0272 0.0930 0.0561 718 LYS A CB 5682 C CG . LYS A 677 ? 0.5483 0.5242 0.4722 -0.0267 0.0866 0.0479 718 LYS A CG 5683 C CD . LYS A 677 ? 0.5966 0.5743 0.5065 -0.0227 0.0827 0.0432 718 LYS A CD 5684 C CE . LYS A 677 ? 0.6059 0.5934 0.5302 -0.0224 0.0775 0.0357 718 LYS A CE 5685 N NZ . LYS A 677 ? 0.5979 0.5865 0.5305 -0.0222 0.0673 0.0338 718 LYS A NZ 5686 N N . VAL A 678 ? 0.6087 0.5539 0.4664 -0.0223 0.1064 0.0681 719 VAL A N 5687 C CA . VAL A 678 ? 0.6374 0.5706 0.4758 -0.0214 0.1122 0.0766 719 VAL A CA 5688 C C . VAL A 678 ? 0.6343 0.5598 0.4747 -0.0226 0.1074 0.0824 719 VAL A C 5689 O O . VAL A 678 ? 0.6590 0.5751 0.4909 -0.0235 0.1143 0.0905 719 VAL A O 5690 C CB . VAL A 678 ? 0.6597 0.5868 0.4699 -0.0160 0.1098 0.0761 719 VAL A CB 5691 C CG1 . VAL A 678 ? 0.6851 0.6165 0.4899 -0.0149 0.1186 0.0726 719 VAL A CG1 5692 C CG2 . VAL A 678 ? 0.6633 0.5922 0.4698 -0.0128 0.0952 0.0703 719 VAL A CG2 5693 N N . ASP A 679 ? 0.6023 0.5314 0.4532 -0.0225 0.0960 0.0783 720 ASP A N 5694 C CA . ASP A 679 ? 0.5906 0.5129 0.4444 -0.0231 0.0902 0.0826 720 ASP A CA 5695 C C . ASP A 679 ? 0.5534 0.4830 0.4347 -0.0273 0.0882 0.0796 720 ASP A C 5696 O O . ASP A 679 ? 0.5353 0.4711 0.4254 -0.0263 0.0787 0.0734 720 ASP A O 5697 C CB . ASP A 679 ? 0.5920 0.5119 0.4335 -0.0186 0.0776 0.0800 720 ASP A CB 5698 C CG . ASP A 679 ? 0.6291 0.5405 0.4698 -0.0183 0.0718 0.0850 720 ASP A CG 5699 O OD1 . ASP A 679 ? 0.6545 0.5628 0.5075 -0.0220 0.0760 0.0893 720 ASP A OD1 5700 O OD2 . ASP A 679 ? 0.7006 0.6081 0.5289 -0.0143 0.0627 0.0844 720 ASP A OD2 5701 N N . PRO A 680 ? 0.5391 0.4678 0.4338 -0.0318 0.0971 0.0837 721 PRO A N 5702 C CA . PRO A 680 ? 0.5132 0.4492 0.4347 -0.0357 0.0952 0.0801 721 PRO A CA 5703 C C . PRO A 680 ? 0.4964 0.4290 0.4236 -0.0352 0.0845 0.0796 721 PRO A C 5704 O O . PRO A 680 ? 0.4625 0.4022 0.4065 -0.0361 0.0783 0.0737 721 PRO A O 5705 C CB . PRO A 680 ? 0.5268 0.4604 0.4593 -0.0404 0.1072 0.0860 721 PRO A CB 5706 C CG . PRO A 680 ? 0.5606 0.4867 0.4713 -0.0389 0.1170 0.0925 721 PRO A CG 5707 C CD . PRO A 680 ? 0.5696 0.4902 0.4554 -0.0333 0.1092 0.0922 721 PRO A CD 5708 N N . SER A 681 ? 0.5047 0.4261 0.4174 -0.0335 0.0824 0.0857 722 SER A N 5709 C CA . SER A 681 ? 0.5031 0.4206 0.4196 -0.0324 0.0721 0.0852 722 SER A CA 5710 C C . SER A 681 ? 0.4753 0.4001 0.3917 -0.0289 0.0615 0.0773 722 SER A C 5711 O O . SER A 681 ? 0.4442 0.3732 0.3753 -0.0295 0.0549 0.0728 722 SER A O 5712 C CB . SER A 681 ? 0.5367 0.4410 0.4353 -0.0301 0.0711 0.0929 722 SER A CB 5713 O OG . SER A 681 ? 0.5781 0.4790 0.4836 -0.0294 0.0619 0.0922 722 SER A OG 5714 N N . LYS A 682 ? 0.4560 0.3821 0.3557 -0.0252 0.0599 0.0756 723 LYS A N 5715 C CA A LYS A 682 ? 0.4466 0.3795 0.3456 -0.0220 0.0508 0.0685 723 LYS A CA 5716 C CA B LYS A 682 ? 0.4505 0.3833 0.3501 -0.0221 0.0505 0.0685 723 LYS A CA 5717 C C . LYS A 682 ? 0.4171 0.3614 0.3339 -0.0239 0.0508 0.0615 723 LYS A C 5718 O O . LYS A 682 ? 0.4026 0.3518 0.3284 -0.0229 0.0432 0.0564 723 LYS A O 5719 C CB A LYS A 682 ? 0.4637 0.3954 0.3421 -0.0182 0.0504 0.0681 723 LYS A CB 5720 C CB B LYS A 682 ? 0.4697 0.4007 0.3482 -0.0179 0.0484 0.0681 723 LYS A CB 5721 C CG A LYS A 682 ? 0.4565 0.3941 0.3334 -0.0149 0.0408 0.0614 723 LYS A CG 5722 C CG B LYS A 682 ? 0.5102 0.4327 0.3751 -0.0142 0.0411 0.0714 723 LYS A CG 5723 C CD A LYS A 682 ? 0.5095 0.4454 0.3667 -0.0113 0.0400 0.0607 723 LYS A CD 5724 C CD B LYS A 682 ? 0.5519 0.4729 0.3966 -0.0099 0.0380 0.0702 723 LYS A CD 5725 C CE A LYS A 682 ? 0.5161 0.4579 0.3737 -0.0083 0.0305 0.0543 723 LYS A CE 5726 C CE B LYS A 682 ? 0.5789 0.4899 0.4088 -0.0063 0.0318 0.0749 723 LYS A CE 5727 N NZ A LYS A 682 ? 0.5623 0.5028 0.4022 -0.0051 0.0294 0.0527 723 LYS A NZ 5728 N NZ B LYS A 682 ? 0.6241 0.5312 0.4319 -0.0024 0.0309 0.0754 723 LYS A NZ 5729 N N . ALA A 683 ? 0.4021 0.3505 0.3235 -0.0264 0.0597 0.0615 724 ALA A N 5730 C CA . ALA A 683 ? 0.3733 0.3326 0.3106 -0.0278 0.0601 0.0549 724 ALA A CA 5731 C C . ALA A 683 ? 0.3459 0.3077 0.3042 -0.0305 0.0569 0.0531 724 ALA A C 5732 O O . ALA A 683 ? 0.3246 0.2931 0.2925 -0.0296 0.0508 0.0471 724 ALA A O 5733 C CB . ALA A 683 ? 0.3911 0.3532 0.3297 -0.0298 0.0710 0.0561 724 ALA A CB 5734 N N . TRP A 684 ? 0.3393 0.2951 0.3038 -0.0336 0.0610 0.0584 725 TRP A N 5735 C CA . TRP A 684 ? 0.3330 0.2902 0.3173 -0.0362 0.0573 0.0564 725 TRP A CA 5736 C C . TRP A 684 ? 0.3348 0.2888 0.3168 -0.0334 0.0468 0.0545 725 TRP A C 5737 O O . TRP A 684 ? 0.3123 0.2703 0.3079 -0.0335 0.0408 0.0495 725 TRP A O 5738 C CB . TRP A 684 ? 0.3387 0.2906 0.3324 -0.0407 0.0649 0.0622 725 TRP A CB 5739 C CG . TRP A 684 ? 0.3339 0.2929 0.3387 -0.0437 0.0740 0.0614 725 TRP A CG 5740 C CD1 . TRP A 684 ? 0.3698 0.3275 0.3658 -0.0445 0.0846 0.0657 725 TRP A CD1 5741 C CD2 . TRP A 684 ? 0.3131 0.2816 0.3394 -0.0458 0.0732 0.0554 725 TRP A CD2 5742 N NE1 . TRP A 684 ? 0.3781 0.3444 0.3903 -0.0472 0.0909 0.0630 725 TRP A NE1 5743 C CE2 . TRP A 684 ? 0.3262 0.2994 0.3572 -0.0480 0.0836 0.0566 725 TRP A CE2 5744 C CE3 . TRP A 684 ? 0.3150 0.2884 0.3565 -0.0457 0.0644 0.0491 725 TRP A CE3 5745 C CZ2 . TRP A 684 ? 0.3151 0.2980 0.3670 -0.0502 0.0853 0.0517 725 TRP A CZ2 5746 C CZ3 . TRP A 684 ? 0.3081 0.2906 0.3690 -0.0478 0.0656 0.0442 725 TRP A CZ3 5747 C CH2 . TRP A 684 ? 0.3003 0.2877 0.3669 -0.0500 0.0758 0.0455 725 TRP A CH2 5748 N N . GLY A 685 ? 0.3428 0.2898 0.3076 -0.0304 0.0441 0.0580 726 GLY A N 5749 C CA . GLY A 685 ? 0.3378 0.2830 0.3000 -0.0271 0.0342 0.0556 726 GLY A CA 5750 C C . GLY A 685 ? 0.3233 0.2777 0.2892 -0.0247 0.0283 0.0480 726 GLY A C 5751 O O . GLY A 685 ? 0.3220 0.2779 0.2955 -0.0234 0.0215 0.0442 726 GLY A O 5752 N N . GLU A 686 ? 0.3124 0.2725 0.2722 -0.0239 0.0312 0.0459 727 GLU A N 5753 C CA A GLU A 686 ? 0.2914 0.2597 0.2543 -0.0217 0.0264 0.0393 727 GLU A CA 5754 C CA B GLU A 686 ? 0.3090 0.2775 0.2718 -0.0218 0.0269 0.0393 727 GLU A CA 5755 C C . GLU A 686 ? 0.2740 0.2489 0.2548 -0.0238 0.0266 0.0348 727 GLU A C 5756 O O . GLU A 686 ? 0.2768 0.2560 0.2627 -0.0219 0.0207 0.0299 727 GLU A O 5757 C CB A GLU A 686 ? 0.3018 0.2733 0.2530 -0.0201 0.0290 0.0381 727 GLU A CB 5758 C CB B GLU A 686 ? 0.3223 0.2941 0.2745 -0.0208 0.0308 0.0386 727 GLU A CB 5759 C CG A GLU A 686 ? 0.2491 0.2289 0.2041 -0.0182 0.0249 0.0316 727 GLU A CG 5760 C CG B GLU A 686 ? 0.3936 0.3603 0.3279 -0.0176 0.0277 0.0408 727 GLU A CG 5761 C CD A GLU A 686 ? 0.2554 0.2352 0.2080 -0.0150 0.0165 0.0292 727 GLU A CD 5762 C CD B GLU A 686 ? 0.4534 0.4193 0.3878 -0.0148 0.0187 0.0388 727 GLU A CD 5763 O OE1 A GLU A 686 ? 0.3140 0.2876 0.2610 -0.0137 0.0131 0.0322 727 GLU A OE1 5764 O OE1 B GLU A 686 ? 0.4650 0.4374 0.4076 -0.0138 0.0147 0.0336 727 GLU A OE1 5765 O OE2 A GLU A 686 ? 0.2720 0.2580 0.2289 -0.0136 0.0136 0.0244 727 GLU A OE2 5766 O OE2 B GLU A 686 ? 0.4910 0.4498 0.4174 -0.0133 0.0159 0.0427 727 GLU A OE2 5767 N N . VAL A 687 ? 0.2801 0.2556 0.2706 -0.0275 0.0331 0.0366 728 VAL A N 5768 C CA . VAL A 687 ? 0.2615 0.2425 0.2706 -0.0294 0.0318 0.0323 728 VAL A CA 5769 C C . VAL A 687 ? 0.2618 0.2392 0.2775 -0.0287 0.0243 0.0308 728 VAL A C 5770 O O . VAL A 687 ? 0.2395 0.2213 0.2625 -0.0272 0.0187 0.0254 728 VAL A O 5771 C CB . VAL A 687 ? 0.2669 0.2485 0.2877 -0.0339 0.0400 0.0349 728 VAL A CB 5772 C CG1 . VAL A 687 ? 0.2783 0.2650 0.3204 -0.0358 0.0370 0.0301 728 VAL A CG1 5773 C CG2 . VAL A 687 ? 0.2661 0.2519 0.2809 -0.0341 0.0479 0.0356 728 VAL A CG2 5774 N N . LYS A 688 ? 0.2728 0.2417 0.2851 -0.0295 0.0245 0.0357 729 LYS A N 5775 C CA . LYS A 688 ? 0.2685 0.2330 0.2864 -0.0286 0.0175 0.0343 729 LYS A CA 5776 C C . LYS A 688 ? 0.2745 0.2407 0.2847 -0.0239 0.0100 0.0304 729 LYS A C 5777 O O . LYS A 688 ? 0.2611 0.2286 0.2786 -0.0224 0.0041 0.0259 729 LYS A O 5778 C CB B LYS A 688 ? 0.2780 0.2322 0.2916 -0.0299 0.0191 0.0408 729 LYS A CB 5779 C CB C LYS A 688 ? 0.2844 0.2386 0.2987 -0.0300 0.0192 0.0408 729 LYS A CB 5780 C CG B LYS A 688 ? 0.2842 0.2361 0.3091 -0.0350 0.0265 0.0447 729 LYS A CG 5781 C CG C LYS A 688 ? 0.2945 0.2467 0.3198 -0.0351 0.0267 0.0446 729 LYS A CG 5782 C CD B LYS A 688 ? 0.3073 0.2479 0.3272 -0.0365 0.0292 0.0522 729 LYS A CD 5783 C CD C LYS A 688 ? 0.3245 0.2656 0.3475 -0.0367 0.0283 0.0512 729 LYS A CD 5784 C CE B LYS A 688 ? 0.3132 0.2474 0.3385 -0.0355 0.0217 0.0512 729 LYS A CE 5785 C CE C LYS A 688 ? 0.3586 0.2938 0.3615 -0.0348 0.0317 0.0575 729 LYS A CE 5786 N NZ B LYS A 688 ? 0.3640 0.2870 0.3890 -0.0380 0.0255 0.0587 729 LYS A NZ 5787 N NZ C LYS A 688 ? 0.3856 0.3094 0.3866 -0.0367 0.0348 0.0650 729 LYS A NZ 5788 N N . ARG A 689 ? 0.2557 0.2220 0.2515 -0.0214 0.0102 0.0320 730 ARG A N 5789 C CA . ARG A 689 ? 0.2486 0.2176 0.2391 -0.0173 0.0039 0.0282 730 ARG A CA 5790 C C . ARG A 689 ? 0.2398 0.2169 0.2378 -0.0163 0.0017 0.0219 730 ARG A C 5791 O O . ARG A 689 ? 0.2303 0.2085 0.2310 -0.0137 -0.0039 0.0182 730 ARG A O 5792 C CB . ARG A 689 ? 0.2634 0.2319 0.2387 -0.0151 0.0044 0.0304 730 ARG A CB 5793 C CG . ARG A 689 ? 0.2910 0.2610 0.2626 -0.0109 -0.0024 0.0273 730 ARG A CG 5794 C CD . ARG A 689 ? 0.3358 0.3052 0.2939 -0.0087 -0.0031 0.0290 730 ARG A CD 5795 N NE . ARG A 689 ? 0.3556 0.3313 0.3109 -0.0088 -0.0004 0.0266 730 ARG A NE 5796 C CZ . ARG A 689 ? 0.3962 0.3782 0.3538 -0.0070 -0.0031 0.0220 730 ARG A CZ 5797 N NH1 . ARG A 689 ? 0.3996 0.3828 0.3623 -0.0047 -0.0080 0.0193 730 ARG A NH1 5798 N NH2 . ARG A 689 ? 0.4119 0.3988 0.3670 -0.0073 -0.0005 0.0200 730 ARG A NH2 5799 N N . GLN A 690 ? 0.2337 0.2162 0.2346 -0.0181 0.0064 0.0209 731 GLN A N 5800 C CA . GLN A 690 ? 0.2316 0.2215 0.2397 -0.0171 0.0046 0.0154 731 GLN A CA 5801 C C . GLN A 690 ? 0.2332 0.2235 0.2551 -0.0179 0.0013 0.0122 731 GLN A C 5802 O O . GLN A 690 ? 0.2181 0.2119 0.2426 -0.0154 -0.0032 0.0074 731 GLN A O 5803 C CB . GLN A 690 ? 0.2422 0.2374 0.2507 -0.0187 0.0104 0.0151 731 GLN A CB 5804 C CG . GLN A 690 ? 0.2397 0.2346 0.2338 -0.0171 0.0123 0.0170 731 GLN A CG 5805 C CD . GLN A 690 ? 0.2753 0.2727 0.2642 -0.0135 0.0070 0.0137 731 GLN A CD 5806 O OE1 . GLN A 690 ? 0.2601 0.2616 0.2554 -0.0121 0.0039 0.0096 731 GLN A OE1 5807 N NE2 . GLN A 690 ? 0.3528 0.3474 0.3303 -0.0117 0.0056 0.0157 731 GLN A NE2 5808 N N . ILE A 691 ? 0.2218 0.2081 0.2518 -0.0212 0.0034 0.0146 732 ILE A N 5809 C CA . ILE A 691 ? 0.2234 0.2092 0.2666 -0.0217 -0.0011 0.0110 732 ILE A CA 5810 C C . ILE A 691 ? 0.2299 0.2118 0.2688 -0.0181 -0.0081 0.0088 732 ILE A C 5811 O O . ILE A 691 ? 0.2500 0.2340 0.2935 -0.0158 -0.0133 0.0036 732 ILE A O 5812 C CB . ILE A 691 ? 0.2266 0.2080 0.2801 -0.0262 0.0025 0.0143 732 ILE A CB 5813 C CG1 . ILE A 691 ? 0.2349 0.2215 0.2952 -0.0297 0.0099 0.0156 732 ILE A CG1 5814 C CG2 . ILE A 691 ? 0.2450 0.2245 0.3120 -0.0266 -0.0034 0.0104 732 ILE A CG2 5815 C CD1 . ILE A 691 ? 0.2473 0.2291 0.3164 -0.0345 0.0155 0.0205 732 ILE A CD1 5816 N N . TYR A 692 ? 0.2278 0.2038 0.2573 -0.0171 -0.0084 0.0127 733 TYR A N 5817 C CA . TYR A 692 ? 0.2493 0.2217 0.2744 -0.0132 -0.0146 0.0107 733 TYR A CA 5818 C C . TYR A 692 ? 0.2343 0.2124 0.2541 -0.0091 -0.0175 0.0066 733 TYR A C 5819 O O . TYR A 692 ? 0.2306 0.2084 0.2525 -0.0062 -0.0224 0.0024 733 TYR A O 5820 C CB . TYR A 692 ? 0.2456 0.2117 0.2613 -0.0126 -0.0139 0.0159 733 TYR A CB 5821 C CG . TYR A 692 ? 0.3015 0.2653 0.3095 -0.0081 -0.0187 0.0151 733 TYR A CG 5822 C CD1 . TYR A 692 ? 0.3325 0.2936 0.3448 -0.0056 -0.0241 0.0115 733 TYR A CD1 5823 C CD2 . TYR A 692 ? 0.3313 0.2948 0.3279 -0.0064 -0.0179 0.0183 733 TYR A CD2 5824 C CE1 . TYR A 692 ? 0.3370 0.2957 0.3429 -0.0013 -0.0279 0.0111 733 TYR A CE1 5825 C CE2 . TYR A 692 ? 0.3191 0.2807 0.3105 -0.0025 -0.0221 0.0179 733 TYR A CE2 5826 C CZ . TYR A 692 ? 0.3508 0.3101 0.3472 0.0000 -0.0268 0.0144 733 TYR A CZ 5827 O OH . TYR A 692 ? 0.3761 0.3335 0.3680 0.0042 -0.0305 0.0140 733 TYR A OH 5828 N N . VAL A 693 ? 0.2178 0.2003 0.2303 -0.0088 -0.0143 0.0077 734 VAL A N 5829 C CA . VAL A 693 ? 0.2132 0.2007 0.2216 -0.0052 -0.0166 0.0041 734 VAL A CA 5830 C C . VAL A 693 ? 0.2150 0.2065 0.2312 -0.0046 -0.0185 -0.0008 734 VAL A C 5831 O O . VAL A 693 ? 0.2310 0.2234 0.2457 -0.0010 -0.0224 -0.0043 734 VAL A O 5832 C CB . VAL A 693 ? 0.2242 0.2156 0.2249 -0.0055 -0.0127 0.0060 734 VAL A CB 5833 C CG1 . VAL A 693 ? 0.2372 0.2340 0.2359 -0.0025 -0.0143 0.0022 734 VAL A CG1 5834 C CG2 . VAL A 693 ? 0.2665 0.2535 0.2580 -0.0047 -0.0129 0.0099 734 VAL A CG2 5835 N N . ALA A 694 ? 0.2053 0.1991 0.2296 -0.0078 -0.0159 -0.0010 735 ALA A N 5836 C CA . ALA A 694 ? 0.2091 0.2068 0.2412 -0.0070 -0.0183 -0.0057 735 ALA A CA 5837 C C . ALA A 694 ? 0.1954 0.1892 0.2333 -0.0056 -0.0241 -0.0090 735 ALA A C 5838 O O . ALA A 694 ? 0.2004 0.1957 0.2380 -0.0021 -0.0285 -0.0134 735 ALA A O 5839 C CB . ALA A 694 ? 0.2108 0.2123 0.2524 -0.0108 -0.0142 -0.0053 735 ALA A CB 5840 N N . ALA A 695 ? 0.1959 0.1843 0.2387 -0.0080 -0.0243 -0.0070 736 ALA A N 5841 C CA . ALA A 695 ? 0.2137 0.1975 0.2623 -0.0067 -0.0302 -0.0106 736 ALA A CA 5842 C C . ALA A 695 ? 0.2197 0.2011 0.2588 -0.0016 -0.0344 -0.0126 736 ALA A C 5843 O O . ALA A 695 ? 0.2131 0.1939 0.2529 0.0018 -0.0395 -0.0177 736 ALA A O 5844 C CB . ALA A 695 ? 0.2177 0.1952 0.2729 -0.0104 -0.0292 -0.0073 736 ALA A CB 5845 N N . PHE A 696 ? 0.2152 0.1952 0.2449 -0.0006 -0.0321 -0.0089 737 PHE A N 5846 C CA . PHE A 696 ? 0.2309 0.2094 0.2525 0.0043 -0.0351 -0.0106 737 PHE A CA 5847 C C . PHE A 696 ? 0.2194 0.2031 0.2372 0.0077 -0.0360 -0.0142 737 PHE A C 5848 O O . PHE A 696 ? 0.2219 0.2040 0.2372 0.0118 -0.0398 -0.0179 737 PHE A O 5849 C CB . PHE A 696 ? 0.2278 0.2053 0.2415 0.0046 -0.0326 -0.0061 737 PHE A CB 5850 C CG . PHE A 696 ? 0.2373 0.2158 0.2437 0.0095 -0.0343 -0.0077 737 PHE A CG 5851 C CD1 . PHE A 696 ? 0.2584 0.2326 0.2646 0.0131 -0.0385 -0.0107 737 PHE A CD1 5852 C CD2 . PHE A 696 ? 0.2616 0.2456 0.2625 0.0105 -0.0318 -0.0071 737 PHE A CD2 5853 C CE1 . PHE A 696 ? 0.2856 0.2615 0.2857 0.0179 -0.0391 -0.0123 737 PHE A CE1 5854 C CE2 . PHE A 696 ? 0.2457 0.2313 0.2414 0.0149 -0.0327 -0.0085 737 PHE A CE2 5855 C CZ . PHE A 696 ? 0.2402 0.2217 0.2357 0.0185 -0.0361 -0.0111 737 PHE A CZ 5856 N N . THR A 697 ? 0.2020 0.1912 0.2189 0.0062 -0.0325 -0.0131 738 THR A N 5857 C CA . THR A 697 ? 0.1961 0.1898 0.2086 0.0094 -0.0327 -0.0156 738 THR A CA 5858 C C . THR A 697 ? 0.2111 0.2046 0.2282 0.0112 -0.0370 -0.0204 738 THR A C 5859 O O . THR A 697 ? 0.2160 0.2092 0.2278 0.0157 -0.0395 -0.0234 738 THR A O 5860 C CB . THR A 697 ? 0.2025 0.2016 0.2137 0.0073 -0.0280 -0.0134 738 THR A CB 5861 O OG1 . THR A 697 ? 0.2126 0.2111 0.2185 0.0062 -0.0252 -0.0094 738 THR A OG1 5862 C CG2 . THR A 697 ? 0.2200 0.2226 0.2263 0.0109 -0.0283 -0.0156 738 THR A CG2 5863 N N . VAL A 698 ? 0.1960 0.1897 0.2231 0.0079 -0.0378 -0.0213 739 VAL A N 5864 C CA . VAL A 698 ? 0.2127 0.2061 0.2452 0.0098 -0.0431 -0.0265 739 VAL A CA 5865 C C . VAL A 698 ? 0.2292 0.2167 0.2588 0.0135 -0.0485 -0.0298 739 VAL A C 5866 O O . VAL A 698 ? 0.2217 0.2085 0.2470 0.0181 -0.0527 -0.0341 739 VAL A O 5867 C CB . VAL A 698 ? 0.2073 0.2023 0.2533 0.0053 -0.0429 -0.0269 739 VAL A CB 5868 C CG1 . VAL A 698 ? 0.2251 0.2190 0.2784 0.0071 -0.0498 -0.0328 739 VAL A CG1 5869 C CG2 . VAL A 698 ? 0.2109 0.2125 0.2590 0.0029 -0.0377 -0.0247 739 VAL A CG2 5870 N N . GLN A 699 ? 0.2310 0.2136 0.2621 0.0120 -0.0485 -0.0281 740 GLN A N 5871 C CA . GLN A 699 ? 0.2360 0.2125 0.2643 0.0158 -0.0536 -0.0315 740 GLN A CA 5872 C C . GLN A 699 ? 0.2318 0.2082 0.2475 0.0214 -0.0533 -0.0322 740 GLN A C 5873 O O . GLN A 699 ? 0.2345 0.2080 0.2457 0.0261 -0.0575 -0.0367 740 GLN A O 5874 C CB . GLN A 699 ? 0.2468 0.2176 0.2789 0.0132 -0.0533 -0.0289 740 GLN A CB 5875 C CG . GLN A 699 ? 0.2398 0.2038 0.2694 0.0173 -0.0584 -0.0326 740 GLN A CG 5876 C CD . GLN A 699 ? 0.2657 0.2266 0.3030 0.0177 -0.0647 -0.0385 740 GLN A CD 5877 O OE1 . GLN A 699 ? 0.2830 0.2461 0.3313 0.0136 -0.0652 -0.0389 740 GLN A OE1 5878 N NE2 . GLN A 699 ? 0.3035 0.2594 0.3358 0.0228 -0.0698 -0.0434 740 GLN A NE2 5879 N N . ALA A 700 ? 0.2234 0.2031 0.2336 0.0209 -0.0482 -0.0279 741 ALA A N 5880 C CA . ALA A 700 ? 0.2302 0.2106 0.2305 0.0257 -0.0470 -0.0281 741 ALA A CA 5881 C C . ALA A 700 ? 0.2313 0.2143 0.2269 0.0291 -0.0478 -0.0311 741 ALA A C 5882 O O . ALA A 700 ? 0.2442 0.2249 0.2325 0.0343 -0.0493 -0.0336 741 ALA A O 5883 C CB . ALA A 700 ? 0.2336 0.2176 0.2310 0.0239 -0.0418 -0.0231 741 ALA A CB 5884 N N . ALA A 701 ? 0.2207 0.2079 0.2201 0.0266 -0.0469 -0.0308 742 ALA A N 5885 C CA . ALA A 701 ? 0.2290 0.2180 0.2245 0.0299 -0.0484 -0.0335 742 ALA A CA 5886 C C . ALA A 701 ? 0.2366 0.2210 0.2321 0.0334 -0.0551 -0.0390 742 ALA A C 5887 O O . ALA A 701 ? 0.2465 0.2290 0.2329 0.0389 -0.0568 -0.0415 742 ALA A O 5888 C CB . ALA A 701 ? 0.2123 0.2065 0.2145 0.0262 -0.0467 -0.0324 742 ALA A CB 5889 N N . ALA A 702 ? 0.2332 0.2153 0.2383 0.0305 -0.0587 -0.0408 743 ALA A N 5890 C CA . ALA A 702 ? 0.2530 0.2301 0.2589 0.0337 -0.0660 -0.0468 743 ALA A CA 5891 C C . ALA A 702 ? 0.2689 0.2407 0.2641 0.0393 -0.0674 -0.0488 743 ALA A C 5892 O O . ALA A 702 ? 0.2693 0.2379 0.2570 0.0448 -0.0716 -0.0533 743 ALA A O 5893 C CB . ALA A 702 ? 0.2527 0.2276 0.2719 0.0292 -0.0691 -0.0479 743 ALA A CB 5894 N N . GLU A 703 ? 0.2485 0.2189 0.2424 0.0384 -0.0638 -0.0456 744 GLU A N 5895 C CA . GLU A 703 ? 0.2704 0.2360 0.2558 0.0436 -0.0648 -0.0476 744 GLU A CA 5896 C C . GLU A 703 ? 0.2620 0.2289 0.2347 0.0491 -0.0619 -0.0476 744 GLU A C 5897 O O . GLU A 703 ? 0.2797 0.2421 0.2443 0.0546 -0.0633 -0.0506 744 GLU A O 5898 C CB . GLU A 703 ? 0.2833 0.2475 0.2714 0.0414 -0.0619 -0.0441 744 GLU A CB 5899 C CG . GLU A 703 ? 0.2911 0.2510 0.2900 0.0375 -0.0657 -0.0451 744 GLU A CG 5900 C CD . GLU A 703 ? 0.3862 0.3435 0.3882 0.0352 -0.0636 -0.0414 744 GLU A CD 5901 O OE1 . GLU A 703 ? 0.4005 0.3598 0.3969 0.0366 -0.0594 -0.0380 744 GLU A OE1 5902 O OE2 . GLU A 703 ? 0.3896 0.3423 0.4001 0.0322 -0.0665 -0.0419 744 GLU A OE2 5903 N N . THR A 704 ? 0.2434 0.2159 0.2144 0.0478 -0.0577 -0.0443 745 THR A N 5904 C CA . THR A 704 ? 0.2556 0.2289 0.2152 0.0529 -0.0547 -0.0440 745 THR A CA 5905 C C . THR A 704 ? 0.2701 0.2396 0.2226 0.0580 -0.0599 -0.0489 745 THR A C 5906 O O . THR A 704 ? 0.2971 0.2648 0.2380 0.0635 -0.0581 -0.0494 745 THR A O 5907 C CB . THR A 704 ? 0.2334 0.2130 0.1932 0.0503 -0.0490 -0.0393 745 THR A CB 5908 O OG1 . THR A 704 ? 0.2465 0.2283 0.2107 0.0482 -0.0514 -0.0401 745 THR A OG1 5909 C CG2 . THR A 704 ? 0.2446 0.2279 0.2113 0.0451 -0.0447 -0.0347 745 THR A CG2 5910 N N . LEU A 705 ? 0.2624 0.2306 0.2223 0.0562 -0.0662 -0.0525 746 LEU A N 5911 C CA . LEU A 705 ? 0.2697 0.2338 0.2240 0.0610 -0.0730 -0.0581 746 LEU A CA 5912 C C . LEU A 705 ? 0.2895 0.2463 0.2408 0.0648 -0.0789 -0.0637 746 LEU A C 5913 O O . LEU A 705 ? 0.3090 0.2613 0.2533 0.0699 -0.0850 -0.0689 746 LEU A O 5914 C CB . LEU A 705 ? 0.2636 0.2308 0.2285 0.0574 -0.0774 -0.0595 746 LEU A CB 5915 C CG . LEU A 705 ? 0.2848 0.2588 0.2526 0.0542 -0.0721 -0.0547 746 LEU A CG 5916 C CD1 . LEU A 705 ? 0.2849 0.2618 0.2651 0.0507 -0.0768 -0.0568 746 LEU A CD1 5917 C CD2 . LEU A 705 ? 0.3024 0.2759 0.2561 0.0596 -0.0695 -0.0534 746 LEU A CD2 5918 N N . SER A 706 ? 0.2930 0.2480 0.2494 0.0627 -0.0776 -0.0630 747 SER A N 5919 C CA . SER A 706 ? 0.3057 0.2531 0.2588 0.0667 -0.0828 -0.0684 747 SER A CA 5920 C C . SER A 706 ? 0.3202 0.2639 0.2562 0.0748 -0.0811 -0.0703 747 SER A C 5921 O O . SER A 706 ? 0.3139 0.2611 0.2424 0.0763 -0.0743 -0.0660 747 SER A O 5922 C CB . SER A 706 ? 0.3326 0.2791 0.2939 0.0629 -0.0806 -0.0661 747 SER A CB 5923 O OG . SER A 706 ? 0.3579 0.3066 0.3341 0.0558 -0.0822 -0.0646 747 SER A OG 5924 N N . GLU A 707 ? 0.3297 0.2659 0.2595 0.0801 -0.0867 -0.0765 748 GLU A N 5925 C CA . GLU A 707 ? 0.3738 0.3060 0.2874 0.0877 -0.0836 -0.0779 748 GLU A CA 5926 C C . GLU A 707 ? 0.3471 0.2829 0.2619 0.0865 -0.0747 -0.0722 748 GLU A C 5927 O O . GLU A 707 ? 0.3659 0.3034 0.2923 0.0815 -0.0737 -0.0700 748 GLU A O 5928 C CB . GLU A 707 ? 0.4009 0.3242 0.3090 0.0932 -0.0906 -0.0856 748 GLU A CB 5929 C CG . GLU A 707 ? 0.4665 0.3867 0.3720 0.0953 -0.0997 -0.0913 748 GLU A CG 5930 C CD . GLU A 707 ? 0.6231 0.5339 0.5172 0.1029 -0.1068 -0.0995 748 GLU A CD 5931 O OE1 . GLU A 707 ? 0.6624 0.5686 0.5651 0.1016 -0.1132 -0.1044 748 GLU A OE1 5932 O OE2 . GLU A 707 ? 0.6978 0.6053 0.5740 0.1103 -0.1061 -0.1011 748 GLU A OE2 5933 N N . VAL A 708 ? 0.3593 0.2964 0.2624 0.0909 -0.0682 -0.0697 749 VAL A N 5934 C CA . VAL A 708 ? 0.3566 0.2994 0.2630 0.0888 -0.0594 -0.0636 749 VAL A CA 5935 C C . VAL A 708 ? 0.3796 0.3193 0.2865 0.0913 -0.0579 -0.0651 749 VAL A C 5936 O O . VAL A 708 ? 0.3798 0.3238 0.2933 0.0888 -0.0526 -0.0608 749 VAL A O 5937 C CB . VAL A 708 ? 0.3561 0.3021 0.2525 0.0917 -0.0521 -0.0598 749 VAL A CB 5938 C CG1 . VAL A 708 ? 0.3641 0.3131 0.2607 0.0892 -0.0535 -0.0581 749 VAL A CG1 5939 C CG2 . VAL A 708 ? 0.3749 0.3145 0.2545 0.1009 -0.0508 -0.0635 749 VAL A CG2 5940 N N . ALA A 709 ? 0.3877 0.3197 0.2882 0.0966 -0.0632 -0.0715 750 ALA A N 5941 C CA . ALA A 709 ? 0.4196 0.3473 0.3202 0.0999 -0.0629 -0.0742 750 ALA A CA 5942 C C . ALA A 709 ? 0.4707 0.3891 0.3661 0.1044 -0.0714 -0.0824 750 ALA A C 5943 C CB . ALA A 709 ? 0.4251 0.3543 0.3165 0.1055 -0.0544 -0.0722 750 ALA A CB 5944 O OXT . ALA A 709 ? 0.4789 0.3946 0.3664 0.1069 -0.0760 -0.0859 750 ALA A OXT # 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 ARG 1 42 ? ? ? A . n A 1 2 SER 2 43 ? ? ? A . n A 1 3 LYS 3 44 ? ? ? A . n A 1 4 SER 4 45 ? ? ? A . n A 1 5 SER 5 46 ? ? ? A . n A 1 6 ASN 6 47 ? ? ? A . n A 1 7 GLU 7 48 ? ? ? A . n A 1 8 ALA 8 49 ? ? ? A . n A 1 9 THR 9 50 ? ? ? A . n A 1 10 ASN 10 51 ? ? ? A . n A 1 11 ILE 11 52 ? ? ? A . n A 1 12 THR 12 53 ? ? ? A . n A 1 13 PRO 13 54 ? ? ? A . n A 1 14 LYS 14 55 55 LYS LYS A . n A 1 15 HIS 15 56 56 HIS HIS A . n A 1 16 ASN 16 57 57 ASN ASN A . n A 1 17 MET 17 58 58 MET MET A . n A 1 18 LYS 18 59 59 LYS LYS A . n A 1 19 ALA 19 60 60 ALA ALA A . n A 1 20 PHE 20 61 61 PHE PHE A . n A 1 21 LEU 21 62 62 LEU LEU A . n A 1 22 ASP 22 63 63 ASP ASP A . n A 1 23 GLU 23 64 64 GLU GLU A . n A 1 24 LEU 24 65 65 LEU LEU A . n A 1 25 LYS 25 66 66 LYS LYS A . n A 1 26 ALA 26 67 67 ALA ALA A . n A 1 27 GLU 27 68 68 GLU GLU A . n A 1 28 ASN 28 69 69 ASN ASN A . n A 1 29 ILE 29 70 70 ILE ILE A . n A 1 30 LYS 30 71 71 LYS LYS A . n A 1 31 LYS 31 72 72 LYS LYS A . n A 1 32 PHE 32 73 73 PHE PHE A . n A 1 33 LEU 33 74 74 LEU LEU A . n A 1 34 TYR 34 75 75 TYR TYR A . n A 1 35 ASN 35 76 76 ASN ASN A . n A 1 36 PHE 36 77 77 PHE PHE A . n A 1 37 THR 37 78 78 THR THR A . n A 1 38 GLN 38 79 79 GLN GLN A . n A 1 39 ILE 39 80 80 ILE ILE A . n A 1 40 PRO 40 81 81 PRO PRO A . n A 1 41 HIS 41 82 82 HIS HIS A . n A 1 42 LEU 42 83 83 LEU LEU A . n A 1 43 ALA 43 84 84 ALA ALA A . n A 1 44 GLY 44 85 85 GLY GLY A . n A 1 45 THR 45 86 86 THR THR A . n A 1 46 GLU 46 87 87 GLU GLU A . n A 1 47 GLN 47 88 88 GLN GLN A . n A 1 48 ASN 48 89 89 ASN ASN A . n A 1 49 PHE 49 90 90 PHE PHE A . n A 1 50 GLN 50 91 91 GLN GLN A . n A 1 51 LEU 51 92 92 LEU LEU A . n A 1 52 ALA 52 93 93 ALA ALA A . n A 1 53 LYS 53 94 94 LYS LYS A . n A 1 54 GLN 54 95 95 GLN GLN A . n A 1 55 ILE 55 96 96 ILE ILE A . n A 1 56 GLN 56 97 97 GLN GLN A . n A 1 57 SER 57 98 98 SER SER A . n A 1 58 GLN 58 99 99 GLN GLN A . n A 1 59 TRP 59 100 100 TRP TRP A . n A 1 60 LYS 60 101 101 LYS LYS A . n A 1 61 GLU 61 102 102 GLU GLU A . n A 1 62 PHE 62 103 103 PHE PHE A . n A 1 63 GLY 63 104 104 GLY GLY A . n A 1 64 LEU 64 105 105 LEU LEU A . n A 1 65 ASP 65 106 106 ASP ASP A . n A 1 66 SER 66 107 107 SER SER A . n A 1 67 VAL 67 108 108 VAL VAL A . n A 1 68 GLU 68 109 109 GLU GLU A . n A 1 69 LEU 69 110 110 LEU LEU A . n A 1 70 ALA 70 111 111 ALA ALA A . n A 1 71 HIS 71 112 112 HIS HIS A . n A 1 72 TYR 72 113 113 TYR TYR A . n A 1 73 ASP 73 114 114 ASP ASP A . n A 1 74 VAL 74 115 115 VAL VAL A . n A 1 75 LEU 75 116 116 LEU LEU A . n A 1 76 LEU 76 117 117 LEU LEU A . n A 1 77 SER 77 118 118 SER SER A . n A 1 78 TYR 78 119 119 TYR TYR A . n A 1 79 PRO 79 120 120 PRO PRO A . n A 1 80 ASN 80 121 121 ASN ASN A . n A 1 81 LYS 81 122 122 LYS LYS A . n A 1 82 THR 82 123 123 THR THR A . n A 1 83 HIS 83 124 124 HIS HIS A . n A 1 84 PRO 84 125 125 PRO PRO A . n A 1 85 ASN 85 126 126 ASN ASN A . n A 1 86 TYR 86 127 127 TYR TYR A . n A 1 87 ILE 87 128 128 ILE ILE A . n A 1 88 SER 88 129 129 SER SER A . n A 1 89 ILE 89 130 130 ILE ILE A . n A 1 90 ILE 90 131 131 ILE ILE A . n A 1 91 ASN 91 132 132 ASN ASN A . n A 1 92 GLU 92 133 133 GLU GLU A . n A 1 93 ASP 93 134 134 ASP ASP A . n A 1 94 GLY 94 135 135 GLY GLY A . n A 1 95 ASN 95 136 136 ASN ASN A . n A 1 96 GLU 96 137 137 GLU GLU A . n A 1 97 ILE 97 138 138 ILE ILE A . n A 1 98 PHE 98 139 139 PHE PHE A . n A 1 99 ASN 99 140 140 ASN ASN A . n A 1 100 THR 100 141 141 THR THR A . n A 1 101 SER 101 142 142 SER SER A . n A 1 102 LEU 102 143 143 LEU LEU A . n A 1 103 PHE 103 144 144 PHE PHE A . n A 1 104 GLU 104 145 145 GLU GLU A . n A 1 105 PRO 105 146 146 PRO PRO A . n A 1 106 PRO 106 147 147 PRO PRO A . n A 1 107 PRO 107 148 148 PRO PRO A . n A 1 108 PRO 108 149 149 PRO PRO A . n A 1 109 GLY 109 150 150 GLY GLY A . n A 1 110 TYR 110 151 151 TYR TYR A . n A 1 111 GLU 111 152 152 GLU GLU A . n A 1 112 ASN 112 153 153 ASN ASN A . n A 1 113 VAL 113 154 154 VAL VAL A . n A 1 114 SER 114 155 155 SER SER A . n A 1 115 ASP 115 156 156 ASP ASP A . n A 1 116 ILE 116 157 157 ILE ILE A . n A 1 117 VAL 117 158 158 VAL VAL A . n A 1 118 PRO 118 159 159 PRO PRO A . n A 1 119 PRO 119 160 160 PRO PRO A . n A 1 120 PHE 120 161 161 PHE PHE A . n A 1 121 SER 121 162 162 SER SER A . n A 1 122 ALA 122 163 163 ALA ALA A . n A 1 123 PHE 123 164 164 PHE PHE A . n A 1 124 SER 124 165 165 SER SER A . n A 1 125 PRO 125 166 166 PRO PRO A . n A 1 126 GLN 126 167 167 GLN GLN A . n A 1 127 GLY 127 168 168 GLY GLY A . n A 1 128 MET 128 169 169 MET MET A . n A 1 129 PRO 129 170 170 PRO PRO A . n A 1 130 GLU 130 171 171 GLU GLU A . n A 1 131 GLY 131 172 172 GLY GLY A . n A 1 132 ASP 132 173 173 ASP ASP A . n A 1 133 LEU 133 174 174 LEU LEU A . n A 1 134 VAL 134 175 175 VAL VAL A . n A 1 135 TYR 135 176 176 TYR TYR A . n A 1 136 VAL 136 177 177 VAL VAL A . n A 1 137 ASN 137 178 178 ASN ASN A . n A 1 138 TYR 138 179 179 TYR TYR A . n A 1 139 ALA 139 180 180 ALA ALA A . n A 1 140 ARG 140 181 181 ARG ARG A . n A 1 141 THR 141 182 182 THR THR A . n A 1 142 GLU 142 183 183 GLU GLU A . n A 1 143 ASP 143 184 184 ASP ASP A . n A 1 144 PHE 144 185 185 PHE PHE A . n A 1 145 PHE 145 186 186 PHE PHE A . n A 1 146 LYS 146 187 187 LYS LYS A . n A 1 147 LEU 147 188 188 LEU LEU A . n A 1 148 GLU 148 189 189 GLU GLU A . n A 1 149 ARG 149 190 190 ARG ARG A . n A 1 150 ASP 150 191 191 ASP ASP A . n A 1 151 MET 151 192 192 MET MET A . n A 1 152 LYS 152 193 193 LYS LYS A . n A 1 153 ILE 153 194 194 ILE ILE A . n A 1 154 ASN 154 195 195 ASN ASN A . n A 1 155 CYS 155 196 196 CYS CYS A . n A 1 156 SER 156 197 197 SER SER A . n A 1 157 GLY 157 198 198 GLY GLY A . n A 1 158 LYS 158 199 199 LYS LYS A . n A 1 159 ILE 159 200 200 ILE ILE A . n A 1 160 VAL 160 201 201 VAL VAL A . n A 1 161 ILE 161 202 202 ILE ILE A . n A 1 162 ALA 162 203 203 ALA ALA A . n A 1 163 ARG 163 204 204 ARG ARG A . n A 1 164 TYR 164 205 205 TYR TYR A . n A 1 165 GLY 165 206 206 GLY GLY A . n A 1 166 LYS 166 207 207 LYS LYS A . n A 1 167 VAL 167 208 208 VAL VAL A . n A 1 168 PHE 168 209 209 PHE PHE A . n A 1 169 ARG 169 210 210 ARG ARG A . n A 1 170 GLY 170 211 211 GLY GLY A . n A 1 171 ASN 171 212 212 ASN ASN A . n A 1 172 LYS 172 213 213 LYS LYS A . n A 1 173 VAL 173 214 214 VAL VAL A . n A 1 174 LYS 174 215 215 LYS LYS A . n A 1 175 ASN 175 216 216 ASN ASN A . n A 1 176 ALA 176 217 217 ALA ALA A . n A 1 177 GLN 177 218 218 GLN GLN A . n A 1 178 LEU 178 219 219 LEU LEU A . n A 1 179 ALA 179 220 220 ALA ALA A . n A 1 180 GLY 180 221 221 GLY GLY A . n A 1 181 ALA 181 222 222 ALA ALA A . n A 1 182 LYS 182 223 223 LYS LYS A . n A 1 183 GLY 183 224 224 GLY GLY A . n A 1 184 VAL 184 225 225 VAL VAL A . n A 1 185 ILE 185 226 226 ILE ILE A . n A 1 186 LEU 186 227 227 LEU LEU A . n A 1 187 TYR 187 228 228 TYR TYR A . n A 1 188 SER 188 229 229 SER SER A . n A 1 189 ASP 189 230 230 ASP ASP A . n A 1 190 PRO 190 231 231 PRO PRO A . n A 1 191 ALA 191 232 232 ALA ALA A . n A 1 192 ASP 192 233 233 ASP ASP A . n A 1 193 TYR 193 234 234 TYR TYR A . n A 1 194 PHE 194 235 235 PHE PHE A . n A 1 195 ALA 195 236 236 ALA ALA A . n A 1 196 PRO 196 237 237 PRO PRO A . n A 1 197 GLY 197 238 238 GLY GLY A . n A 1 198 VAL 198 239 239 VAL VAL A . n A 1 199 LYS 199 240 240 LYS LYS A . n A 1 200 SER 200 241 241 SER SER A . n A 1 201 TYR 201 242 242 TYR TYR A . n A 1 202 PRO 202 243 243 PRO PRO A . n A 1 203 ASP 203 244 244 ASP ASP A . n A 1 204 GLY 204 245 245 GLY GLY A . n A 1 205 TRP 205 246 246 TRP TRP A . n A 1 206 ASN 206 247 247 ASN ASN A . n A 1 207 LEU 207 248 248 LEU LEU A . n A 1 208 PRO 208 249 249 PRO PRO A . n A 1 209 GLY 209 250 250 GLY GLY A . n A 1 210 GLY 210 251 251 GLY GLY A . n A 1 211 GLY 211 252 252 GLY GLY A . n A 1 212 VAL 212 253 253 VAL VAL A . n A 1 213 GLN 213 254 254 GLN GLN A . n A 1 214 ARG 214 255 255 ARG ARG A . n A 1 215 GLY 215 256 256 GLY GLY A . n A 1 216 ASN 216 257 257 ASN ASN A . n A 1 217 ILE 217 258 258 ILE ILE A . n A 1 218 LEU 218 259 259 LEU LEU A . n A 1 219 ASN 219 260 260 ASN ASN A . n A 1 220 LEU 220 261 261 LEU LEU A . n A 1 221 ASN 221 262 262 ASN ASN A . n A 1 222 GLY 222 263 263 GLY GLY A . n A 1 223 ALA 223 264 264 ALA ALA A . n A 1 224 GLY 224 265 265 GLY GLY A . n A 1 225 ASP 225 266 266 ASP ASP A . n A 1 226 PRO 226 267 267 PRO PRO A . n A 1 227 LEU 227 268 268 LEU LEU A . n A 1 228 THR 228 269 269 THR THR A . n A 1 229 PRO 229 270 270 PRO PRO A . n A 1 230 GLY 230 271 271 GLY GLY A . n A 1 231 TYR 231 272 272 TYR TYR A . n A 1 232 PRO 232 273 273 PRO PRO A . n A 1 233 ALA 233 274 274 ALA ALA A . n A 1 234 ASN 234 275 275 ASN ASN A . n A 1 235 GLU 235 276 276 GLU GLU A . n A 1 236 TYR 236 277 277 TYR TYR A . n A 1 237 ALA 237 278 278 ALA ALA A . n A 1 238 TYR 238 279 279 TYR TYR A . n A 1 239 ARG 239 280 280 ARG ARG A . n A 1 240 ARG 240 281 281 ARG ARG A . n A 1 241 GLY 241 282 282 GLY GLY A . n A 1 242 ILE 242 283 283 ILE ILE A . n A 1 243 ALA 243 284 284 ALA ALA A . n A 1 244 GLU 244 285 285 GLU GLU A . n A 1 245 ALA 245 286 286 ALA ALA A . n A 1 246 VAL 246 287 287 VAL VAL A . n A 1 247 GLY 247 288 288 GLY GLY A . n A 1 248 LEU 248 289 289 LEU LEU A . n A 1 249 PRO 249 290 290 PRO PRO A . n A 1 250 SER 250 291 291 SER SER A . n A 1 251 ILE 251 292 292 ILE ILE A . n A 1 252 PRO 252 293 293 PRO PRO A . n A 1 253 VAL 253 294 294 VAL VAL A . n A 1 254 HIS 254 295 295 HIS HIS A . n A 1 255 PRO 255 296 296 PRO PRO A . n A 1 256 ILE 256 297 297 ILE ILE A . n A 1 257 GLY 257 298 298 GLY GLY A . n A 1 258 TYR 258 299 299 TYR TYR A . n A 1 259 TYR 259 300 300 TYR TYR A . n A 1 260 ASP 260 301 301 ASP ASP A . n A 1 261 ALA 261 302 302 ALA ALA A . n A 1 262 GLN 262 303 303 GLN GLN A . n A 1 263 LYS 263 304 304 LYS LYS A . n A 1 264 LEU 264 305 305 LEU LEU A . n A 1 265 LEU 265 306 306 LEU LEU A . n A 1 266 GLU 266 307 307 GLU GLU A . n A 1 267 LYS 267 308 308 LYS LYS A . n A 1 268 MET 268 309 309 MET MET A . n A 1 269 GLY 269 310 310 GLY GLY A . n A 1 270 GLY 270 311 311 GLY GLY A . n A 1 271 SER 271 312 312 SER SER A . n A 1 272 ALA 272 313 313 ALA ALA A . n A 1 273 PRO 273 314 314 PRO PRO A . n A 1 274 PRO 274 315 315 PRO PRO A . n A 1 275 ASP 275 316 316 ASP ASP A . n A 1 276 SER 276 317 317 SER SER A . n A 1 277 SER 277 318 318 SER SER A . n A 1 278 TRP 278 319 319 TRP TRP A . n A 1 279 ARG 279 320 320 ARG ARG A . n A 1 280 GLY 280 321 321 GLY GLY A . n A 1 281 SER 281 322 322 SER SER A . n A 1 282 LEU 282 323 323 LEU LEU A . n A 1 283 LYS 283 324 324 LYS LYS A . n A 1 284 VAL 284 325 325 VAL VAL A . n A 1 285 PRO 285 326 326 PRO PRO A . n A 1 286 TYR 286 327 327 TYR TYR A . n A 1 287 ASN 287 328 328 ASN ASN A . n A 1 288 VAL 288 329 329 VAL VAL A . n A 1 289 GLY 289 330 330 GLY GLY A . n A 1 290 PRO 290 331 331 PRO PRO A . n A 1 291 GLY 291 332 332 GLY GLY A . n A 1 292 PHE 292 333 333 PHE PHE A . n A 1 293 THR 293 334 334 THR THR A . n A 1 294 GLY 294 335 335 GLY GLY A . n A 1 295 ASN 295 336 336 ASN ASN A . n A 1 296 PHE 296 337 337 PHE PHE A . n A 1 297 SER 297 338 338 SER SER A . n A 1 298 THR 298 339 339 THR THR A . n A 1 299 GLN 299 340 340 GLN GLN A . n A 1 300 LYS 300 341 341 LYS LYS A . n A 1 301 VAL 301 342 342 VAL VAL A . n A 1 302 LYS 302 343 343 LYS LYS A . n A 1 303 MET 303 344 344 MET MET A . n A 1 304 HIS 304 345 345 HIS HIS A . n A 1 305 ILE 305 346 346 ILE ILE A . n A 1 306 HIS 306 347 347 HIS HIS A . n A 1 307 SER 307 348 348 SER SER A . n A 1 308 THR 308 349 349 THR THR A . n A 1 309 ASN 309 350 350 ASN ASN A . n A 1 310 GLU 310 351 351 GLU GLU A . n A 1 311 VAL 311 352 352 VAL VAL A . n A 1 312 THR 312 353 353 THR THR A . n A 1 313 ARG 313 354 354 ARG ARG A . n A 1 314 ILE 314 355 355 ILE ILE A . n A 1 315 TYR 315 356 356 TYR TYR A . n A 1 316 ASN 316 357 357 ASN ASN A . n A 1 317 VAL 317 358 358 VAL VAL A . n A 1 318 ILE 318 359 359 ILE ILE A . n A 1 319 GLY 319 360 360 GLY GLY A . n A 1 320 THR 320 361 361 THR THR A . n A 1 321 LEU 321 362 362 LEU LEU A . n A 1 322 ARG 322 363 363 ARG ARG A . n A 1 323 GLY 323 364 364 GLY GLY A . n A 1 324 ALA 324 365 365 ALA ALA A . n A 1 325 VAL 325 366 366 VAL VAL A . n A 1 326 GLU 326 367 367 GLU GLU A . n A 1 327 PRO 327 368 368 PRO PRO A . n A 1 328 ASP 328 369 369 ASP ASP A . n A 1 329 ARG 329 370 370 ARG ARG A . n A 1 330 TYR 330 371 371 TYR TYR A . n A 1 331 VAL 331 372 372 VAL VAL A . n A 1 332 ILE 332 373 373 ILE ILE A . n A 1 333 LEU 333 374 374 LEU LEU A . n A 1 334 GLY 334 375 375 GLY GLY A . n A 1 335 GLY 335 376 376 GLY GLY A . n A 1 336 HIS 336 377 377 HIS HIS A . n A 1 337 ARG 337 378 378 ARG ARG A . n A 1 338 ASP 338 379 379 ASP ASP A . n A 1 339 SER 339 380 380 SER SER A . n A 1 340 TRP 340 381 381 TRP TRP A . n A 1 341 VAL 341 382 382 VAL VAL A . n A 1 342 PHE 342 383 383 PHE PHE A . n A 1 343 GLY 343 384 384 GLY GLY A . n A 1 344 GLY 344 385 385 GLY GLY A . n A 1 345 ILE 345 386 386 ILE ILE A . n A 1 346 ASP 346 387 387 ASP ASP A . n A 1 347 PRO 347 388 388 PRO PRO A . n A 1 348 GLN 348 389 389 GLN GLN A . n A 1 349 SER 349 390 390 SER SER A . n A 1 350 GLY 350 391 391 GLY GLY A . n A 1 351 ALA 351 392 392 ALA ALA A . n A 1 352 ALA 352 393 393 ALA ALA A . n A 1 353 VAL 353 394 394 VAL VAL A . n A 1 354 VAL 354 395 395 VAL VAL A . n A 1 355 HIS 355 396 396 HIS HIS A . n A 1 356 GLU 356 397 397 GLU GLU A . n A 1 357 ILE 357 398 398 ILE ILE A . n A 1 358 VAL 358 399 399 VAL VAL A . n A 1 359 ARG 359 400 400 ARG ARG A . n A 1 360 SER 360 401 401 SER SER A . n A 1 361 PHE 361 402 402 PHE PHE A . n A 1 362 GLY 362 403 403 GLY GLY A . n A 1 363 THR 363 404 404 THR THR A . n A 1 364 LEU 364 405 405 LEU LEU A . n A 1 365 LYS 365 406 406 LYS LYS A . n A 1 366 LYS 366 407 407 LYS LYS A . n A 1 367 GLU 367 408 408 GLU GLU A . n A 1 368 GLY 368 409 409 GLY GLY A . n A 1 369 TRP 369 410 410 TRP TRP A . n A 1 370 ARG 370 411 411 ARG ARG A . n A 1 371 PRO 371 412 412 PRO PRO A . n A 1 372 ARG 372 413 413 ARG ARG A . n A 1 373 ARG 373 414 414 ARG ARG A . n A 1 374 THR 374 415 415 THR THR A . n A 1 375 ILE 375 416 416 ILE ILE A . n A 1 376 LEU 376 417 417 LEU LEU A . n A 1 377 PHE 377 418 418 PHE PHE A . n A 1 378 ALA 378 419 419 ALA ALA A . n A 1 379 SER 379 420 420 SER SER A . n A 1 380 TRP 380 421 421 TRP TRP A . n A 1 381 ASP 381 422 422 ASP ASP A . n A 1 382 ALA 382 423 423 ALA ALA A . n A 1 383 GLU 383 424 424 GLU GLU A . n A 1 384 GLU 384 425 425 GLU GLU A . n A 1 385 PHE 385 426 426 PHE PHE A . n A 1 386 GLY 386 427 427 GLY GLY A . n A 1 387 LEU 387 428 428 LEU LEU A . n A 1 388 LEU 388 429 429 LEU LEU A . n A 1 389 GLY 389 430 430 GLY GLY A . n A 1 390 SER 390 431 431 SER SER A . n A 1 391 THR 391 432 432 THR THR A . n A 1 392 GLU 392 433 433 GLU GLU A . n A 1 393 TRP 393 434 434 TRP TRP A . n A 1 394 ALA 394 435 435 ALA ALA A . n A 1 395 GLU 395 436 436 GLU GLU A . n A 1 396 GLU 396 437 437 GLU GLU A . n A 1 397 ASN 397 438 438 ASN ASN A . n A 1 398 SER 398 439 439 SER SER A . n A 1 399 ARG 399 440 440 ARG ARG A . n A 1 400 LEU 400 441 441 LEU LEU A . n A 1 401 LEU 401 442 442 LEU LEU A . n A 1 402 GLN 402 443 443 GLN GLN A . n A 1 403 GLU 403 444 444 GLU GLU A . n A 1 404 ARG 404 445 445 ARG ARG A . n A 1 405 GLY 405 446 446 GLY GLY A . n A 1 406 VAL 406 447 447 VAL VAL A . n A 1 407 ALA 407 448 448 ALA ALA A . n A 1 408 TYR 408 449 449 TYR TYR A . n A 1 409 ILE 409 450 450 ILE ILE A . n A 1 410 ASN 410 451 451 ASN ASN A . n A 1 411 ALA 411 452 452 ALA ALA A . n A 1 412 ASP 412 453 453 ASP ASP A . n A 1 413 SER 413 454 454 SER SER A . n A 1 414 SER 414 455 455 SER SER A . n A 1 415 ILE 415 456 456 ILE ILE A . n A 1 416 GLU 416 457 457 GLU GLU A . n A 1 417 GLY 417 458 458 GLY GLY A . n A 1 418 ASN 418 459 459 ASN ASN A . n A 1 419 TYR 419 460 460 TYR TYR A . n A 1 420 THR 420 461 461 THR THR A . n A 1 421 LEU 421 462 462 LEU LEU A . n A 1 422 ARG 422 463 463 ARG ARG A . n A 1 423 VAL 423 464 464 VAL VAL A . n A 1 424 ASP 424 465 465 ASP ASP A . n A 1 425 CYS 425 466 466 CYS CYS A . n A 1 426 THR 426 467 467 THR THR A . n A 1 427 PRO 427 468 468 PRO PRO A . n A 1 428 LEU 428 469 469 LEU LEU A . n A 1 429 MET 429 470 470 MET MET A . n A 1 430 TYR 430 471 471 TYR TYR A . n A 1 431 SER 431 472 472 SER SER A . n A 1 432 LEU 432 473 473 LEU LEU A . n A 1 433 VAL 433 474 474 VAL VAL A . n A 1 434 HIS 434 475 475 HIS HIS A . n A 1 435 ASN 435 476 476 ASN ASN A . n A 1 436 LEU 436 477 477 LEU LEU A . n A 1 437 THR 437 478 478 THR THR A . n A 1 438 LYS 438 479 479 LYS LYS A . n A 1 439 GLU 439 480 480 GLU GLU A . n A 1 440 LEU 440 481 481 LEU LEU A . n A 1 441 LYS 441 482 482 LYS LYS A . n A 1 442 SER 442 483 483 SER SER A . n A 1 443 PRO 443 484 484 PRO PRO A . n A 1 444 ASP 444 485 485 ASP ASP A . n A 1 445 GLU 445 486 486 GLU GLU A . n A 1 446 GLY 446 487 487 GLY GLY A . n A 1 447 PHE 447 488 488 PHE PHE A . n A 1 448 GLU 448 489 489 GLU GLU A . n A 1 449 GLY 449 490 490 GLY GLY A . n A 1 450 LYS 450 491 491 LYS LYS A . n A 1 451 SER 451 492 492 SER SER A . n A 1 452 LEU 452 493 493 LEU LEU A . n A 1 453 TYR 453 494 494 TYR TYR A . n A 1 454 GLU 454 495 495 GLU GLU A . n A 1 455 SER 455 496 496 SER SER A . n A 1 456 TRP 456 497 497 TRP TRP A . n A 1 457 THR 457 498 498 THR THR A . n A 1 458 LYS 458 499 499 LYS LYS A . n A 1 459 LYS 459 500 500 LYS LYS A . n A 1 460 SER 460 501 501 SER SER A . n A 1 461 PRO 461 502 502 PRO PRO A . n A 1 462 SER 462 503 503 SER SER A . n A 1 463 PRO 463 504 504 PRO PRO A . n A 1 464 GLU 464 505 505 GLU GLU A . n A 1 465 PHE 465 506 506 PHE PHE A . n A 1 466 SER 466 507 507 SER SER A . n A 1 467 GLY 467 508 508 GLY GLY A . n A 1 468 MET 468 509 509 MET MET A . n A 1 469 PRO 469 510 510 PRO PRO A . n A 1 470 ARG 470 511 511 ARG ARG A . n A 1 471 ILE 471 512 512 ILE ILE A . n A 1 472 SER 472 513 513 SER SER A . n A 1 473 LYS 473 514 514 LYS LYS A . n A 1 474 LEU 474 515 515 LEU LEU A . n A 1 475 GLY 475 516 516 GLY GLY A . n A 1 476 SER 476 517 517 SER SER A . n A 1 477 GLY 477 518 518 GLY GLY A . n A 1 478 ASN 478 519 519 ASN ASN A . n A 1 479 ASP 479 520 520 ASP ASP A . n A 1 480 PHE 480 521 521 PHE PHE A . n A 1 481 GLU 481 522 522 GLU GLU A . n A 1 482 VAL 482 523 523 VAL VAL A . n A 1 483 PHE 483 524 524 PHE PHE A . n A 1 484 PHE 484 525 525 PHE PHE A . n A 1 485 GLN 485 526 526 GLN GLN A . n A 1 486 ARG 486 527 527 ARG ARG A . n A 1 487 LEU 487 528 528 LEU LEU A . n A 1 488 GLY 488 529 529 GLY GLY A . n A 1 489 ILE 489 530 530 ILE ILE A . n A 1 490 ALA 490 531 531 ALA ALA A . n A 1 491 SER 491 532 532 SER SER A . n A 1 492 GLY 492 533 533 GLY GLY A . n A 1 493 ARG 493 534 534 ARG ARG A . n A 1 494 ALA 494 535 535 ALA ALA A . n A 1 495 ARG 495 536 536 ARG ARG A . n A 1 496 TYR 496 537 537 TYR TYR A . n A 1 497 THR 497 538 538 THR THR A . n A 1 498 LYS 498 539 539 LYS LYS A . n A 1 499 ASN 499 540 540 ASN ASN A . n A 1 500 TRP 500 541 541 TRP TRP A . n A 1 501 GLU 501 542 542 GLU GLU A . n A 1 502 THR 502 543 543 THR THR A . n A 1 503 ASN 503 544 544 ASN ASN A . n A 1 504 LYS 504 545 545 LYS LYS A . n A 1 505 PHE 505 546 546 PHE PHE A . n A 1 506 SER 506 547 547 SER SER A . n A 1 507 GLY 507 548 548 GLY GLY A . n A 1 508 TYR 508 549 549 TYR TYR A . n A 1 509 PRO 509 550 550 PRO PRO A . n A 1 510 LEU 510 551 551 LEU LEU A . n A 1 511 TYR 511 552 552 TYR TYR A . n A 1 512 HIS 512 553 553 HIS HIS A . n A 1 513 SER 513 554 554 SER SER A . n A 1 514 VAL 514 555 555 VAL VAL A . n A 1 515 TYR 515 556 556 TYR TYR A . n A 1 516 GLU 516 557 557 GLU GLU A . n A 1 517 THR 517 558 558 THR THR A . n A 1 518 TYR 518 559 559 TYR TYR A . n A 1 519 GLU 519 560 560 GLU GLU A . n A 1 520 LEU 520 561 561 LEU LEU A . n A 1 521 VAL 521 562 562 VAL VAL A . n A 1 522 GLU 522 563 563 GLU GLU A . n A 1 523 LYS 523 564 564 LYS LYS A . n A 1 524 PHE 524 565 565 PHE PHE A . n A 1 525 TYR 525 566 566 TYR TYR A . n A 1 526 ASP 526 567 567 ASP ASP A . n A 1 527 PRO 527 568 568 PRO PRO A . n A 1 528 MET 528 569 569 MET MET A . n A 1 529 PHE 529 570 570 PHE PHE A . n A 1 530 LYS 530 571 571 LYS LYS A . n A 1 531 TYR 531 572 572 TYR TYR A . n A 1 532 HIS 532 573 573 HIS HIS A . n A 1 533 LEU 533 574 574 LEU LEU A . n A 1 534 THR 534 575 575 THR THR A . n A 1 535 VAL 535 576 576 VAL VAL A . n A 1 536 ALA 536 577 577 ALA ALA A . n A 1 537 GLN 537 578 578 GLN GLN A . n A 1 538 VAL 538 579 579 VAL VAL A . n A 1 539 ARG 539 580 580 ARG ARG A . n A 1 540 GLY 540 581 581 GLY GLY A . n A 1 541 GLY 541 582 582 GLY GLY A . n A 1 542 MET 542 583 583 MET MET A . n A 1 543 VAL 543 584 584 VAL VAL A . n A 1 544 PHE 544 585 585 PHE PHE A . n A 1 545 GLU 545 586 586 GLU GLU A . n A 1 546 LEU 546 587 587 LEU LEU A . n A 1 547 ALA 547 588 588 ALA ALA A . n A 1 548 ASN 548 589 589 ASN ASN A . n A 1 549 SER 549 590 590 SER SER A . n A 1 550 ILE 550 591 591 ILE ILE A . n A 1 551 VAL 551 592 592 VAL VAL A . n A 1 552 LEU 552 593 593 LEU LEU A . n A 1 553 PRO 553 594 594 PRO PRO A . n A 1 554 PHE 554 595 595 PHE PHE A . n A 1 555 ASP 555 596 596 ASP ASP A . n A 1 556 CYS 556 597 597 CYS CYS A . n A 1 557 ARG 557 598 598 ARG ARG A . n A 1 558 ASP 558 599 599 ASP ASP A . n A 1 559 TYR 559 600 600 TYR TYR A . n A 1 560 ALA 560 601 601 ALA ALA A . n A 1 561 VAL 561 602 602 VAL VAL A . n A 1 562 VAL 562 603 603 VAL VAL A . n A 1 563 LEU 563 604 604 LEU LEU A . n A 1 564 ARG 564 605 605 ARG ARG A . n A 1 565 LYS 565 606 606 LYS LYS A . n A 1 566 TYR 566 607 607 TYR TYR A . n A 1 567 ALA 567 608 608 ALA ALA A . n A 1 568 ASP 568 609 609 ASP ASP A . n A 1 569 LYS 569 610 610 LYS LYS A . n A 1 570 ILE 570 611 611 ILE ILE A . n A 1 571 TYR 571 612 612 TYR TYR A . n A 1 572 SER 572 613 613 SER SER A . n A 1 573 ILE 573 614 614 ILE ILE A . n A 1 574 SER 574 615 615 SER SER A . n A 1 575 MET 575 616 616 MET MET A . n A 1 576 LYS 576 617 617 LYS LYS A . n A 1 577 HIS 577 618 618 HIS HIS A . n A 1 578 PRO 578 619 619 PRO PRO A . n A 1 579 GLN 579 620 620 GLN GLN A . n A 1 580 GLU 580 621 621 GLU GLU A . n A 1 581 MET 581 622 622 MET MET A . n A 1 582 LYS 582 623 623 LYS LYS A . n A 1 583 THR 583 624 624 THR THR A . n A 1 584 TYR 584 625 625 TYR TYR A . n A 1 585 SER 585 626 626 SER SER A . n A 1 586 VAL 586 627 627 VAL VAL A . n A 1 587 SER 587 628 628 SER SER A . n A 1 588 PHE 588 629 629 PHE PHE A . n A 1 589 ASP 589 630 630 ASP ASP A . n A 1 590 SER 590 631 631 SER SER A . n A 1 591 LEU 591 632 632 LEU LEU A . n A 1 592 PHE 592 633 633 PHE PHE A . n A 1 593 SER 593 634 634 SER SER A . n A 1 594 ALA 594 635 635 ALA ALA A . n A 1 595 VAL 595 636 636 VAL VAL A . n A 1 596 LYS 596 637 637 LYS LYS A . n A 1 597 ASN 597 638 638 ASN ASN A . n A 1 598 PHE 598 639 639 PHE PHE A . n A 1 599 THR 599 640 640 THR THR A . n A 1 600 GLU 600 641 641 GLU GLU A . n A 1 601 ILE 601 642 642 ILE ILE A . n A 1 602 ALA 602 643 643 ALA ALA A . n A 1 603 SER 603 644 644 SER SER A . n A 1 604 LYS 604 645 645 LYS LYS A . n A 1 605 PHE 605 646 646 PHE PHE A . n A 1 606 SER 606 647 647 SER SER A . n A 1 607 GLU 607 648 648 GLU GLU A . n A 1 608 ARG 608 649 649 ARG ARG A . n A 1 609 LEU 609 650 650 LEU LEU A . n A 1 610 GLN 610 651 651 GLN GLN A . n A 1 611 ASP 611 652 652 ASP ASP A . n A 1 612 PHE 612 653 653 PHE PHE A . n A 1 613 ASP 613 654 ? ? ? A . n A 1 614 LYS 614 655 ? ? ? A . n A 1 615 SER 615 656 656 SER SER A . n A 1 616 ASN 616 657 657 ASN ASN A . n A 1 617 PRO 617 658 658 PRO PRO A . n A 1 618 ILE 618 659 659 ILE ILE A . n A 1 619 VAL 619 660 660 VAL VAL A . n A 1 620 LEU 620 661 661 LEU LEU A . n A 1 621 ARG 621 662 662 ARG ARG A . n A 1 622 MET 622 663 663 MET MET A . n A 1 623 MET 623 664 664 MET MET A . n A 1 624 ASN 624 665 665 ASN ASN A . n A 1 625 ASP 625 666 666 ASP ASP A . n A 1 626 GLN 626 667 667 GLN GLN A . n A 1 627 LEU 627 668 668 LEU LEU A . n A 1 628 MET 628 669 669 MET MET A . n A 1 629 PHE 629 670 670 PHE PHE A . n A 1 630 LEU 630 671 671 LEU LEU A . n A 1 631 GLU 631 672 672 GLU GLU A . n A 1 632 ARG 632 673 673 ARG ARG A . n A 1 633 ALA 633 674 674 ALA ALA A . n A 1 634 PHE 634 675 675 PHE PHE A . n A 1 635 ILE 635 676 676 ILE ILE A . n A 1 636 ASP 636 677 677 ASP ASP A . n A 1 637 PRO 637 678 678 PRO PRO A . n A 1 638 LEU 638 679 679 LEU LEU A . n A 1 639 GLY 639 680 680 GLY GLY A . n A 1 640 LEU 640 681 681 LEU LEU A . n A 1 641 PRO 641 682 682 PRO PRO A . n A 1 642 ASP 642 683 683 ASP ASP A . n A 1 643 ARG 643 684 684 ARG ARG A . n A 1 644 PRO 644 685 685 PRO PRO A . n A 1 645 PHE 645 686 686 PHE PHE A . n A 1 646 TYR 646 687 687 TYR TYR A . n A 1 647 ARG 647 688 688 ARG ARG A . n A 1 648 HIS 648 689 689 HIS HIS A . n A 1 649 VAL 649 690 690 VAL VAL A . n A 1 650 ILE 650 691 691 ILE ILE A . n A 1 651 TYR 651 692 692 TYR TYR A . n A 1 652 ALA 652 693 693 ALA ALA A . n A 1 653 PRO 653 694 694 PRO PRO A . n A 1 654 SER 654 695 695 SER SER A . n A 1 655 SER 655 696 696 SER SER A . n A 1 656 HIS 656 697 697 HIS HIS A . n A 1 657 ASN 657 698 698 ASN ASN A . n A 1 658 LYS 658 699 699 LYS LYS A . n A 1 659 TYR 659 700 700 TYR TYR A . n A 1 660 ALA 660 701 701 ALA ALA A . n A 1 661 GLY 661 702 702 GLY GLY A . n A 1 662 GLU 662 703 703 GLU GLU A . n A 1 663 SER 663 704 704 SER SER A . n A 1 664 PHE 664 705 705 PHE PHE A . n A 1 665 PRO 665 706 706 PRO PRO A . n A 1 666 GLY 666 707 707 GLY GLY A . n A 1 667 ILE 667 708 708 ILE ILE A . n A 1 668 TYR 668 709 709 TYR TYR A . n A 1 669 ASP 669 710 710 ASP ASP A . n A 1 670 ALA 670 711 711 ALA ALA A . n A 1 671 LEU 671 712 712 LEU LEU A . n A 1 672 PHE 672 713 713 PHE PHE A . n A 1 673 ASP 673 714 714 ASP ASP A . n A 1 674 ILE 674 715 715 ILE ILE A . n A 1 675 GLU 675 716 716 GLU GLU A . n A 1 676 SER 676 717 717 SER SER A . n A 1 677 LYS 677 718 718 LYS LYS A . n A 1 678 VAL 678 719 719 VAL VAL A . n A 1 679 ASP 679 720 720 ASP ASP A . n A 1 680 PRO 680 721 721 PRO PRO A . n A 1 681 SER 681 722 722 SER SER A . n A 1 682 LYS 682 723 723 LYS LYS A . n A 1 683 ALA 683 724 724 ALA ALA A . n A 1 684 TRP 684 725 725 TRP TRP A . n A 1 685 GLY 685 726 726 GLY GLY A . n A 1 686 GLU 686 727 727 GLU GLU A . n A 1 687 VAL 687 728 728 VAL VAL A . n A 1 688 LYS 688 729 729 LYS LYS A . n A 1 689 ARG 689 730 730 ARG ARG A . n A 1 690 GLN 690 731 731 GLN GLN A . n A 1 691 ILE 691 732 732 ILE ILE A . n A 1 692 TYR 692 733 733 TYR TYR A . n A 1 693 VAL 693 734 734 VAL VAL A . n A 1 694 ALA 694 735 735 ALA ALA A . n A 1 695 ALA 695 736 736 ALA ALA A . n A 1 696 PHE 696 737 737 PHE PHE A . n A 1 697 THR 697 738 738 THR THR A . n A 1 698 VAL 698 739 739 VAL VAL A . n A 1 699 GLN 699 740 740 GLN GLN A . n A 1 700 ALA 700 741 741 ALA ALA A . n A 1 701 ALA 701 742 742 ALA ALA A . n A 1 702 ALA 702 743 743 ALA ALA A . n A 1 703 GLU 703 744 744 GLU GLU A . n A 1 704 THR 704 745 745 THR THR A . n A 1 705 LEU 705 746 746 LEU LEU A . n A 1 706 SER 706 747 747 SER SER A . n A 1 707 GLU 707 748 748 GLU GLU A . n A 1 708 VAL 708 749 749 VAL VAL A . n A 1 709 ALA 709 750 750 ALA ALA A . n # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 35 A ASN 76 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 597 A ASN 638 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 418 A ASN 459 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 435 A ASN 476 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 80 A ASN 121 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 99 A ASN 140 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 154 A ASN 195 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 12000 ? 1 MORE -119 ? 1 'SSA (A^2)' 49220 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_565 -x,-y+1,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 130.4310000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? T HOH . ? A HOH 2476 ? 1_555 ZN ? P ZN . ? A ZN 1752 ? 1_555 OD2 ? A ASP 412 ? A ASP 453 ? 1_555 112.1 ? 2 O ? T HOH . ? A HOH 2476 ? 1_555 ZN ? P ZN . ? A ZN 1752 ? 1_555 OD1 ? A ASP 346 ? A ASP 387 ? 1_555 105.6 ? 3 OD2 ? A ASP 412 ? A ASP 453 ? 1_555 ZN ? P ZN . ? A ZN 1752 ? 1_555 OD1 ? A ASP 346 ? A ASP 387 ? 1_555 118.1 ? 4 O ? T HOH . ? A HOH 2476 ? 1_555 ZN ? P ZN . ? A ZN 1752 ? 1_555 NE2 ? A HIS 336 ? A HIS 377 ? 1_555 109.4 ? 5 OD2 ? A ASP 412 ? A ASP 453 ? 1_555 ZN ? P ZN . ? A ZN 1752 ? 1_555 NE2 ? A HIS 336 ? A HIS 377 ? 1_555 103.1 ? 6 OD1 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? P ZN . ? A ZN 1752 ? 1_555 NE2 ? A HIS 336 ? A HIS 377 ? 1_555 108.5 ? 7 O ? T HOH . ? A HOH 2476 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 162.8 ? 8 O ? T HOH . ? A HOH 2476 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 95.6 ? 9 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 92.2 ? 10 O ? T HOH . ? A HOH 2476 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 92.7 ? 11 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 100.7 ? 12 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 101.5 ? 13 O ? T HOH . ? A HOH 2476 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 91.9 ? 14 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 86.7 ? 15 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 156.7 ? 16 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 56.1 ? 17 O ? T HOH . ? A HOH 2476 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OAD ? S JRG . ? A JRG 1 ? 1_555 77.2 ? 18 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OAD ? S JRG . ? A JRG 1 ? 1_555 85.9 ? 19 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OAD ? S JRG . ? A JRG 1 ? 1_555 106.0 ? 20 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OAD ? S JRG . ? A JRG 1 ? 1_555 151.5 ? 21 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? O ZN . ? A ZN 1751 ? 1_555 OAD ? S JRG . ? A JRG 1 ? 1_555 97.2 ? 22 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 79.6 ? 23 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 74.9 ? 24 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 104.3 ? 25 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 O ? T HOH . ? A HOH 1773 ? 1_555 146.1 ? 26 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 O ? T HOH . ? A HOH 1773 ? 1_555 96.2 ? 27 O ? A THR 228 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 O ? T HOH . ? A HOH 1773 ? 1_555 73.7 ? 28 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 135.8 ? 29 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 88.5 ? 30 O ? A THR 228 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 149.0 ? 31 O ? T HOH . ? A HOH 1773 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 77.0 ? 32 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 93.1 ? 33 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 172.7 ? 34 O ? A THR 228 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 73.1 ? 35 O ? T HOH . ? A HOH 1773 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 89.7 ? 36 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 97.1 ? 37 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 85.7 ? 38 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 90.7 ? 39 O ? A THR 228 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 152.5 ? 40 O ? T HOH . ? A HOH 1773 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 128.1 ? 41 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 51.8 ? 42 OG1 ? A THR 228 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 1753 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 89.0 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2011-10-05 2 'Structure model' 1 1 2011-11-16 # _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_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 17.7540 _pdbx_refine_tls.origin_y 49.8909 _pdbx_refine_tls.origin_z 44.8708 _pdbx_refine_tls.T[1][1] 0.0182 _pdbx_refine_tls.T[2][2] 0.0599 _pdbx_refine_tls.T[3][3] 0.0476 _pdbx_refine_tls.T[1][2] 0.0170 _pdbx_refine_tls.T[1][3] 0.0061 _pdbx_refine_tls.T[2][3] -0.0279 _pdbx_refine_tls.L[1][1] 0.5964 _pdbx_refine_tls.L[2][2] 0.9950 _pdbx_refine_tls.L[3][3] 0.3556 _pdbx_refine_tls.L[1][2] -0.2758 _pdbx_refine_tls.L[1][3] 0.0415 _pdbx_refine_tls.L[2][3] 0.1021 _pdbx_refine_tls.S[1][1] -0.0566 _pdbx_refine_tls.S[1][2] 0.0363 _pdbx_refine_tls.S[1][3] -0.0369 _pdbx_refine_tls.S[2][1] 0.0052 _pdbx_refine_tls.S[2][2] 0.0702 _pdbx_refine_tls.S[2][3] -0.1750 _pdbx_refine_tls.S[3][1] 0.0320 _pdbx_refine_tls.S[3][2] 0.0708 _pdbx_refine_tls.S[3][3] -0.0137 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id A _pdbx_refine_tls_group.beg_auth_seq_id 55 _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id A _pdbx_refine_tls_group.end_auth_seq_id 750 _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal SERGUI 'data collection' . ? 1 REFMAC refinement . ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 REFMAC phasing . ? 5 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 NH2 A ARG 688 ? B O A HOH 1878 ? ? 1.99 2 1 OH A TYR 242 ? ? O A HOH 2468 ? ? 2.03 3 1 NZ A LYS 699 ? A O A HOH 2045 ? ? 2.08 4 1 CG A GLU 276 ? B O A HOH 1940 ? ? 2.09 5 1 CZ A ARG 688 ? B O A HOH 1878 ? ? 2.15 6 1 O A HOH 2093 ? ? O A HOH 2492 ? ? 2.17 7 1 NH2 A ARG 688 ? B O A HOH 2148 ? ? 2.18 # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A SER 656 ? B 1_555 O A HOH 2145 ? ? 4_566 2.05 2 1 OG A SER 656 ? B 1_555 O A HOH 2145 ? ? 4_566 2.10 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 PHE A 164 ? ? 80.74 8.63 2 1 ASN A 178 ? ? 57.61 -126.19 3 1 LYS A 207 ? ? 70.30 -44.65 4 1 VAL A 382 ? ? -131.04 -108.12 5 1 ASP A 453 ? ? -85.07 -157.80 6 1 ASP A 453 ? ? -85.07 -158.60 7 1 SER A 454 ? A -36.67 125.04 8 1 SER A 517 ? ? -130.66 -156.64 9 1 TRP A 541 ? ? -154.20 76.37 10 1 ASP A 567 ? ? -154.06 65.18 11 1 ASP A 683 ? ? 56.94 15.30 12 1 ASN A 698 ? ? -168.24 99.08 # _pdbx_unobs_or_zero_occ_atoms.id 1 _pdbx_unobs_or_zero_occ_atoms.PDB_model_num 1 _pdbx_unobs_or_zero_occ_atoms.polymer_flag Y _pdbx_unobs_or_zero_occ_atoms.occupancy_flag 1 _pdbx_unobs_or_zero_occ_atoms.auth_asym_id A _pdbx_unobs_or_zero_occ_atoms.auth_comp_id ALA _pdbx_unobs_or_zero_occ_atoms.auth_seq_id 750 _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code ? _pdbx_unobs_or_zero_occ_atoms.auth_atom_id O _pdbx_unobs_or_zero_occ_atoms.label_alt_id ? _pdbx_unobs_or_zero_occ_atoms.label_asym_id A _pdbx_unobs_or_zero_occ_atoms.label_comp_id ALA _pdbx_unobs_or_zero_occ_atoms.label_seq_id 709 _pdbx_unobs_or_zero_occ_atoms.label_atom_id O # 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 ARG 42 ? A ARG 1 2 1 Y 1 A SER 43 ? A SER 2 3 1 Y 1 A LYS 44 ? A LYS 3 4 1 Y 1 A SER 45 ? A SER 4 5 1 Y 1 A SER 46 ? A SER 5 6 1 Y 1 A ASN 47 ? A ASN 6 7 1 Y 1 A GLU 48 ? A GLU 7 8 1 Y 1 A ALA 49 ? A ALA 8 9 1 Y 1 A THR 50 ? A THR 9 10 1 Y 1 A ASN 51 ? A ASN 10 11 1 Y 1 A ILE 52 ? A ILE 11 12 1 Y 1 A THR 53 ? A THR 12 13 1 Y 1 A PRO 54 ? A PRO 13 14 1 Y 1 A ASP 654 ? A ASP 613 15 1 Y 1 A LYS 655 ? A LYS 614 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 ALPHA-D-MANNOSE MAN 5 'ZINC ION' ZN 6 'CALCIUM ION' CA 7 'CHLORIDE ION' CL 8 'N~2~-{[(1S)-1-carboxy-3-(methylsulfanyl)propyl]carbamoyl}-N~6~-(4-iodobenzoyl)-L-lysine' JRG 9 water HOH # 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 B 2 NAG 1 1755 1755 NAG NAG A . C 2 NAG 2 1756 1756 NAG NAG A . D 2 NAG 1 1757 1757 NAG NAG A . E 2 NAG 1 1758 1758 NAG NAG A . F 2 NAG 2 1767 1767 NAG NAG A . G 2 NAG 1 1759 1759 NAG NAG A . H 2 NAG 1 1760 1760 NAG NAG A . I 2 NAG 1 1761 1761 NAG NAG A . J 2 NAG 2 1762 1762 NAG NAG A . K 2 NAG 1 1763 1763 NAG NAG A . L 2 NAG 2 1764 1764 NAG NAG A . M 3 BMA 3 1765 1765 BMA BMA A . N 4 MAN 4 1766 1766 MAN MAN A . O 5 ZN 1 1751 1751 ZN ZN A . P 5 ZN 1 1752 1752 ZN ZN A . Q 6 CA 1 1753 1753 CA CA A . R 7 CL 1 1754 1754 CL CL A . S 8 JRG 1 1 1 JRG JRG A . T 9 HOH 1 1768 1768 HOH HOH A . T 9 HOH 2 1769 1769 HOH HOH A . T 9 HOH 3 1770 1770 HOH HOH A . T 9 HOH 4 1771 1771 HOH HOH A . T 9 HOH 5 1772 1772 HOH HOH A . T 9 HOH 6 1773 1773 HOH HOH A . T 9 HOH 7 1774 1774 HOH HOH A . T 9 HOH 8 1775 1775 HOH HOH A . T 9 HOH 9 1776 1776 HOH HOH A . T 9 HOH 10 1777 1777 HOH HOH A . T 9 HOH 11 1778 1778 HOH HOH A . T 9 HOH 12 1779 1779 HOH HOH A . T 9 HOH 13 1780 1780 HOH HOH A . T 9 HOH 14 1781 1781 HOH HOH A . T 9 HOH 15 1782 1782 HOH HOH A . T 9 HOH 16 1783 1783 HOH HOH A . T 9 HOH 17 1784 1784 HOH HOH A . T 9 HOH 18 1785 1785 HOH HOH A . T 9 HOH 19 1786 1786 HOH HOH A . T 9 HOH 20 1787 1787 HOH HOH A . T 9 HOH 21 1788 1788 HOH HOH A . T 9 HOH 22 1789 1789 HOH HOH A . T 9 HOH 23 1790 1790 HOH HOH A . T 9 HOH 24 1791 1791 HOH HOH A . T 9 HOH 25 1792 1792 HOH HOH A . T 9 HOH 26 1793 1793 HOH HOH A . T 9 HOH 27 1794 1794 HOH HOH A . T 9 HOH 28 1795 1795 HOH HOH A . T 9 HOH 29 1796 1796 HOH HOH A . T 9 HOH 30 1797 1797 HOH HOH A . T 9 HOH 31 1798 1798 HOH HOH A . T 9 HOH 32 1799 1799 HOH HOH A . T 9 HOH 33 1800 1800 HOH HOH A . T 9 HOH 34 1801 1801 HOH HOH A . T 9 HOH 35 1802 1802 HOH HOH A . T 9 HOH 36 1803 1803 HOH HOH A . T 9 HOH 37 1804 1804 HOH HOH A . T 9 HOH 38 1805 1805 HOH HOH A . T 9 HOH 39 1806 1806 HOH HOH A . T 9 HOH 40 1807 1807 HOH HOH A . T 9 HOH 41 1808 1808 HOH HOH A . T 9 HOH 42 1809 1809 HOH HOH A . T 9 HOH 43 1810 1810 HOH HOH A . T 9 HOH 44 1811 1811 HOH HOH A . T 9 HOH 45 1812 1812 HOH HOH A . T 9 HOH 46 1813 1813 HOH HOH A . T 9 HOH 47 1814 1814 HOH HOH A . T 9 HOH 48 1815 1815 HOH HOH A . T 9 HOH 49 1816 1816 HOH HOH A . T 9 HOH 50 1817 1817 HOH HOH A . T 9 HOH 51 1818 1818 HOH HOH A . T 9 HOH 52 1819 1819 HOH HOH A . T 9 HOH 53 1820 1820 HOH HOH A . T 9 HOH 54 1821 1821 HOH HOH A . T 9 HOH 55 1822 1822 HOH HOH A . T 9 HOH 56 1823 1823 HOH HOH A . T 9 HOH 57 1824 1824 HOH HOH A . T 9 HOH 58 1825 1825 HOH HOH A . T 9 HOH 59 1826 1826 HOH HOH A . T 9 HOH 60 1827 1827 HOH HOH A . T 9 HOH 61 1828 1828 HOH HOH A . T 9 HOH 62 1829 1829 HOH HOH A . T 9 HOH 63 1830 1830 HOH HOH A . T 9 HOH 64 1831 1831 HOH HOH A . T 9 HOH 65 1832 1832 HOH HOH A . T 9 HOH 66 1833 1833 HOH HOH A . T 9 HOH 67 1834 1834 HOH HOH A . T 9 HOH 68 1835 1835 HOH HOH A . T 9 HOH 69 1836 1836 HOH HOH A . T 9 HOH 70 1838 1838 HOH HOH A . T 9 HOH 71 1839 1839 HOH HOH A . T 9 HOH 72 1840 1840 HOH HOH A . T 9 HOH 73 1841 1841 HOH HOH A . T 9 HOH 74 1842 1842 HOH HOH A . T 9 HOH 75 1843 1843 HOH HOH A . T 9 HOH 76 1844 1844 HOH HOH A . T 9 HOH 77 1845 1845 HOH HOH A . T 9 HOH 78 1846 1846 HOH HOH A . T 9 HOH 79 1847 1847 HOH HOH A . T 9 HOH 80 1848 1848 HOH HOH A . T 9 HOH 81 1849 1849 HOH HOH A . T 9 HOH 82 1850 1850 HOH HOH A . T 9 HOH 83 1851 1851 HOH HOH A . T 9 HOH 84 1852 1852 HOH HOH A . T 9 HOH 85 1853 1853 HOH HOH A . T 9 HOH 86 1854 1854 HOH HOH A . T 9 HOH 87 1855 1855 HOH HOH A . T 9 HOH 88 1857 1857 HOH HOH A . T 9 HOH 89 1858 1858 HOH HOH A . T 9 HOH 90 1859 1859 HOH HOH A . T 9 HOH 91 1860 1860 HOH HOH A . T 9 HOH 92 1861 1861 HOH HOH A . T 9 HOH 93 1862 1862 HOH HOH A . T 9 HOH 94 1863 1863 HOH HOH A . T 9 HOH 95 1864 1864 HOH HOH A . T 9 HOH 96 1865 1865 HOH HOH A . T 9 HOH 97 1866 1866 HOH HOH A . T 9 HOH 98 1867 1867 HOH HOH A . T 9 HOH 99 1868 1868 HOH HOH A . T 9 HOH 100 1869 1869 HOH HOH A . T 9 HOH 101 1870 1870 HOH HOH A . T 9 HOH 102 1871 1871 HOH HOH A . T 9 HOH 103 1872 1872 HOH HOH A . T 9 HOH 104 1873 1873 HOH HOH A . T 9 HOH 105 1874 1874 HOH HOH A . T 9 HOH 106 1875 1875 HOH HOH A . T 9 HOH 107 1876 1876 HOH HOH A . T 9 HOH 108 1877 1877 HOH HOH A . T 9 HOH 109 1878 1878 HOH HOH A . T 9 HOH 110 1879 1879 HOH HOH A . T 9 HOH 111 1880 1880 HOH HOH A . T 9 HOH 112 1881 1881 HOH HOH A . T 9 HOH 113 1882 1882 HOH HOH A . T 9 HOH 114 1883 1883 HOH HOH A . T 9 HOH 115 1884 1884 HOH HOH A . T 9 HOH 116 1885 1885 HOH HOH A . T 9 HOH 117 1886 1886 HOH HOH A . T 9 HOH 118 1887 1887 HOH HOH A . T 9 HOH 119 1888 1888 HOH HOH A . T 9 HOH 120 1889 1889 HOH HOH A . T 9 HOH 121 1890 1890 HOH HOH A . T 9 HOH 122 1891 1891 HOH HOH A . T 9 HOH 123 1892 1892 HOH HOH A . T 9 HOH 124 1893 1893 HOH HOH A . T 9 HOH 125 1894 1894 HOH HOH A . T 9 HOH 126 1895 1895 HOH HOH A . T 9 HOH 127 1896 1896 HOH HOH A . T 9 HOH 128 1897 1897 HOH HOH A . T 9 HOH 129 1898 1898 HOH HOH A . T 9 HOH 130 1899 1899 HOH HOH A . T 9 HOH 131 1900 1900 HOH HOH A . T 9 HOH 132 1901 1901 HOH HOH A . T 9 HOH 133 1902 1902 HOH HOH A . T 9 HOH 134 1903 1903 HOH HOH A . T 9 HOH 135 1904 1904 HOH HOH A . T 9 HOH 136 1905 1905 HOH HOH A . T 9 HOH 137 1906 1906 HOH HOH A . T 9 HOH 138 1907 1907 HOH HOH A . T 9 HOH 139 1908 1908 HOH HOH A . T 9 HOH 140 1909 1909 HOH HOH A . T 9 HOH 141 1910 1910 HOH HOH A . T 9 HOH 142 1911 1911 HOH HOH A . T 9 HOH 143 1912 1912 HOH HOH A . T 9 HOH 144 1913 1913 HOH HOH A . T 9 HOH 145 1914 1914 HOH HOH A . T 9 HOH 146 1915 1915 HOH HOH A . T 9 HOH 147 1916 1916 HOH HOH A . T 9 HOH 148 1917 1917 HOH HOH A . T 9 HOH 149 1918 1918 HOH HOH A . T 9 HOH 150 1919 1919 HOH HOH A . T 9 HOH 151 1920 1920 HOH HOH A . T 9 HOH 152 1921 1921 HOH HOH A . T 9 HOH 153 1922 1922 HOH HOH A . T 9 HOH 154 1923 1923 HOH HOH A . T 9 HOH 155 1924 1924 HOH HOH A . T 9 HOH 156 1925 1925 HOH HOH A . T 9 HOH 157 1926 1926 HOH HOH A . T 9 HOH 158 1927 1927 HOH HOH A . T 9 HOH 159 1928 1928 HOH HOH A . T 9 HOH 160 1929 1929 HOH HOH A . T 9 HOH 161 1930 1930 HOH HOH A . T 9 HOH 162 1932 1932 HOH HOH A . T 9 HOH 163 1933 1933 HOH HOH A . T 9 HOH 164 1934 1934 HOH HOH A . T 9 HOH 165 1935 1935 HOH HOH A . T 9 HOH 166 1936 1936 HOH HOH A . T 9 HOH 167 1937 1937 HOH HOH A . T 9 HOH 168 1940 1940 HOH HOH A . T 9 HOH 169 1941 1941 HOH HOH A . T 9 HOH 170 1942 1942 HOH HOH A . T 9 HOH 171 1944 1944 HOH HOH A . T 9 HOH 172 1946 1946 HOH HOH A . T 9 HOH 173 1947 1947 HOH HOH A . T 9 HOH 174 1948 1948 HOH HOH A . T 9 HOH 175 1949 1949 HOH HOH A . T 9 HOH 176 1950 1950 HOH HOH A . T 9 HOH 177 1951 1951 HOH HOH A . T 9 HOH 178 1952 1952 HOH HOH A . T 9 HOH 179 1953 1953 HOH HOH A . T 9 HOH 180 1954 1954 HOH HOH A . T 9 HOH 181 1955 1955 HOH HOH A . T 9 HOH 182 1956 1956 HOH HOH A . T 9 HOH 183 1957 1957 HOH HOH A . T 9 HOH 184 1958 1958 HOH HOH A . T 9 HOH 185 1959 1959 HOH HOH A . T 9 HOH 186 1962 1962 HOH HOH A . T 9 HOH 187 1963 1963 HOH HOH A . T 9 HOH 188 1964 1964 HOH HOH A . T 9 HOH 189 1965 1965 HOH HOH A . T 9 HOH 190 1966 1966 HOH HOH A . T 9 HOH 191 1967 1967 HOH HOH A . T 9 HOH 192 1968 1968 HOH HOH A . T 9 HOH 193 1969 1969 HOH HOH A . T 9 HOH 194 1970 1970 HOH HOH A . T 9 HOH 195 1971 1971 HOH HOH A . T 9 HOH 196 1972 1972 HOH HOH A . T 9 HOH 197 1973 1973 HOH HOH A . T 9 HOH 198 1974 1974 HOH HOH A . T 9 HOH 199 1975 1975 HOH HOH A . T 9 HOH 200 1976 1976 HOH HOH A . T 9 HOH 201 1977 1977 HOH HOH A . T 9 HOH 202 1978 1978 HOH HOH A . T 9 HOH 203 1979 1979 HOH HOH A . T 9 HOH 204 1980 1980 HOH HOH A . T 9 HOH 205 1981 1981 HOH HOH A . T 9 HOH 206 1982 1982 HOH HOH A . T 9 HOH 207 1984 1984 HOH HOH A . T 9 HOH 208 1987 1987 HOH HOH A . T 9 HOH 209 1989 1989 HOH HOH A . T 9 HOH 210 1990 1990 HOH HOH A . T 9 HOH 211 1991 1991 HOH HOH A . T 9 HOH 212 1992 1992 HOH HOH A . T 9 HOH 213 1993 1993 HOH HOH A . T 9 HOH 214 1994 1994 HOH HOH A . T 9 HOH 215 1995 1995 HOH HOH A . T 9 HOH 216 1996 1996 HOH HOH A . T 9 HOH 217 1997 1997 HOH HOH A . T 9 HOH 218 1998 1998 HOH HOH A . T 9 HOH 219 2000 2000 HOH HOH A . T 9 HOH 220 2001 2001 HOH HOH A . T 9 HOH 221 2002 2002 HOH HOH A . T 9 HOH 222 2003 2003 HOH HOH A . T 9 HOH 223 2004 2004 HOH HOH A . T 9 HOH 224 2005 2005 HOH HOH A . T 9 HOH 225 2007 2007 HOH HOH A . T 9 HOH 226 2008 2008 HOH HOH A . T 9 HOH 227 2009 2009 HOH HOH A . T 9 HOH 228 2010 2010 HOH HOH A . T 9 HOH 229 2011 2011 HOH HOH A . T 9 HOH 230 2012 2012 HOH HOH A . T 9 HOH 231 2013 2013 HOH HOH A . T 9 HOH 232 2014 2014 HOH HOH A . T 9 HOH 233 2016 2016 HOH HOH A . T 9 HOH 234 2017 2017 HOH HOH A . T 9 HOH 235 2018 2018 HOH HOH A . T 9 HOH 236 2019 2019 HOH HOH A . T 9 HOH 237 2020 2020 HOH HOH A . T 9 HOH 238 2021 2021 HOH HOH A . T 9 HOH 239 2024 2024 HOH HOH A . T 9 HOH 240 2025 2025 HOH HOH A . T 9 HOH 241 2026 2026 HOH HOH A . T 9 HOH 242 2027 2027 HOH HOH A . T 9 HOH 243 2029 2029 HOH HOH A . T 9 HOH 244 2031 2031 HOH HOH A . T 9 HOH 245 2032 2032 HOH HOH A . T 9 HOH 246 2033 2033 HOH HOH A . T 9 HOH 247 2034 2034 HOH HOH A . T 9 HOH 248 2035 2035 HOH HOH A . T 9 HOH 249 2036 2036 HOH HOH A . T 9 HOH 250 2038 2038 HOH HOH A . T 9 HOH 251 2039 2039 HOH HOH A . T 9 HOH 252 2040 2040 HOH HOH A . T 9 HOH 253 2041 2041 HOH HOH A . T 9 HOH 254 2042 2042 HOH HOH A . T 9 HOH 255 2043 2043 HOH HOH A . T 9 HOH 256 2044 2044 HOH HOH A . T 9 HOH 257 2045 2045 HOH HOH A . T 9 HOH 258 2046 2046 HOH HOH A . T 9 HOH 259 2047 2047 HOH HOH A . T 9 HOH 260 2048 2048 HOH HOH A . T 9 HOH 261 2049 2049 HOH HOH A . T 9 HOH 262 2050 2050 HOH HOH A . T 9 HOH 263 2051 2051 HOH HOH A . T 9 HOH 264 2052 2052 HOH HOH A . T 9 HOH 265 2053 2053 HOH HOH A . T 9 HOH 266 2054 2054 HOH HOH A . T 9 HOH 267 2055 2055 HOH HOH A . T 9 HOH 268 2056 2056 HOH HOH A . T 9 HOH 269 2057 2057 HOH HOH A . T 9 HOH 270 2059 2059 HOH HOH A . T 9 HOH 271 2060 2060 HOH HOH A . T 9 HOH 272 2061 2061 HOH HOH A . T 9 HOH 273 2062 2062 HOH HOH A . T 9 HOH 274 2063 2063 HOH HOH A . T 9 HOH 275 2064 2064 HOH HOH A . T 9 HOH 276 2065 2065 HOH HOH A . T 9 HOH 277 2067 2067 HOH HOH A . T 9 HOH 278 2068 2068 HOH HOH A . T 9 HOH 279 2069 2069 HOH HOH A . T 9 HOH 280 2071 2071 HOH HOH A . T 9 HOH 281 2072 2072 HOH HOH A . T 9 HOH 282 2073 2073 HOH HOH A . T 9 HOH 283 2074 2074 HOH HOH A . T 9 HOH 284 2075 2075 HOH HOH A . T 9 HOH 285 2076 2076 HOH HOH A . T 9 HOH 286 2077 2077 HOH HOH A . T 9 HOH 287 2078 2078 HOH HOH A . T 9 HOH 288 2079 2079 HOH HOH A . T 9 HOH 289 2080 2080 HOH HOH A . T 9 HOH 290 2081 2081 HOH HOH A . T 9 HOH 291 2082 2082 HOH HOH A . T 9 HOH 292 2083 2083 HOH HOH A . T 9 HOH 293 2084 2084 HOH HOH A . T 9 HOH 294 2085 2085 HOH HOH A . T 9 HOH 295 2088 2088 HOH HOH A . T 9 HOH 296 2089 2089 HOH HOH A . T 9 HOH 297 2090 2090 HOH HOH A . T 9 HOH 298 2091 2091 HOH HOH A . T 9 HOH 299 2092 2092 HOH HOH A . T 9 HOH 300 2093 2093 HOH HOH A . T 9 HOH 301 2096 2096 HOH HOH A . T 9 HOH 302 2097 2097 HOH HOH A . T 9 HOH 303 2098 2098 HOH HOH A . T 9 HOH 304 2100 2100 HOH HOH A . T 9 HOH 305 2101 2101 HOH HOH A . T 9 HOH 306 2102 2102 HOH HOH A . T 9 HOH 307 2103 2103 HOH HOH A . T 9 HOH 308 2105 2105 HOH HOH A . T 9 HOH 309 2106 2106 HOH HOH A . T 9 HOH 310 2108 2108 HOH HOH A . T 9 HOH 311 2109 2109 HOH HOH A . T 9 HOH 312 2110 2110 HOH HOH A . T 9 HOH 313 2111 2111 HOH HOH A . T 9 HOH 314 2113 2113 HOH HOH A . T 9 HOH 315 2115 2115 HOH HOH A . T 9 HOH 316 2117 2117 HOH HOH A . T 9 HOH 317 2118 2118 HOH HOH A . T 9 HOH 318 2119 2119 HOH HOH A . T 9 HOH 319 2120 2120 HOH HOH A . T 9 HOH 320 2122 2122 HOH HOH A . T 9 HOH 321 2123 2123 HOH HOH A . T 9 HOH 322 2124 2124 HOH HOH A . T 9 HOH 323 2125 2125 HOH HOH A . T 9 HOH 324 2126 2126 HOH HOH A . T 9 HOH 325 2127 2127 HOH HOH A . T 9 HOH 326 2128 2128 HOH HOH A . T 9 HOH 327 2129 2129 HOH HOH A . T 9 HOH 328 2130 2130 HOH HOH A . T 9 HOH 329 2131 2131 HOH HOH A . T 9 HOH 330 2132 2132 HOH HOH A . T 9 HOH 331 2133 2133 HOH HOH A . T 9 HOH 332 2134 2134 HOH HOH A . T 9 HOH 333 2135 2135 HOH HOH A . T 9 HOH 334 2136 2136 HOH HOH A . T 9 HOH 335 2137 2137 HOH HOH A . T 9 HOH 336 2138 2138 HOH HOH A . T 9 HOH 337 2139 2139 HOH HOH A . T 9 HOH 338 2140 2140 HOH HOH A . T 9 HOH 339 2142 2142 HOH HOH A . T 9 HOH 340 2143 2143 HOH HOH A . T 9 HOH 341 2144 2144 HOH HOH A . T 9 HOH 342 2145 2145 HOH HOH A . T 9 HOH 343 2146 2146 HOH HOH A . T 9 HOH 344 2147 2147 HOH HOH A . T 9 HOH 345 2148 2148 HOH HOH A . T 9 HOH 346 2151 2151 HOH HOH A . T 9 HOH 347 2152 2152 HOH HOH A . T 9 HOH 348 2153 2153 HOH HOH A . T 9 HOH 349 2155 2155 HOH HOH A . T 9 HOH 350 2156 2156 HOH HOH A . T 9 HOH 351 2158 2158 HOH HOH A . T 9 HOH 352 2159 2159 HOH HOH A . T 9 HOH 353 2160 2160 HOH HOH A . T 9 HOH 354 2161 2161 HOH HOH A . T 9 HOH 355 2162 2162 HOH HOH A . T 9 HOH 356 2163 2163 HOH HOH A . T 9 HOH 357 2164 2164 HOH HOH A . T 9 HOH 358 2167 2167 HOH HOH A . T 9 HOH 359 2169 2169 HOH HOH A . T 9 HOH 360 2170 2170 HOH HOH A . T 9 HOH 361 2171 2171 HOH HOH A . T 9 HOH 362 2172 2172 HOH HOH A . T 9 HOH 363 2173 2173 HOH HOH A . T 9 HOH 364 2174 2174 HOH HOH A . T 9 HOH 365 2175 2175 HOH HOH A . T 9 HOH 366 2179 2179 HOH HOH A . T 9 HOH 367 2180 2180 HOH HOH A . T 9 HOH 368 2181 2181 HOH HOH A . T 9 HOH 369 2183 2183 HOH HOH A . T 9 HOH 370 2184 2184 HOH HOH A . T 9 HOH 371 2185 2185 HOH HOH A . T 9 HOH 372 2186 2186 HOH HOH A . T 9 HOH 373 2187 2187 HOH HOH A . T 9 HOH 374 2188 2188 HOH HOH A . T 9 HOH 375 2189 2189 HOH HOH A . T 9 HOH 376 2190 2190 HOH HOH A . T 9 HOH 377 2191 2191 HOH HOH A . T 9 HOH 378 2192 2192 HOH HOH A . T 9 HOH 379 2193 2193 HOH HOH A . T 9 HOH 380 2195 2195 HOH HOH A . T 9 HOH 381 2197 2197 HOH HOH A . T 9 HOH 382 2198 2198 HOH HOH A . T 9 HOH 383 2200 2200 HOH HOH A . T 9 HOH 384 2201 2201 HOH HOH A . T 9 HOH 385 2202 2202 HOH HOH A . T 9 HOH 386 2203 2203 HOH HOH A . T 9 HOH 387 2204 2204 HOH HOH A . T 9 HOH 388 2205 2205 HOH HOH A . T 9 HOH 389 2206 2206 HOH HOH A . T 9 HOH 390 2207 2207 HOH HOH A . T 9 HOH 391 2208 2208 HOH HOH A . T 9 HOH 392 2210 2210 HOH HOH A . T 9 HOH 393 2212 2212 HOH HOH A . T 9 HOH 394 2213 2213 HOH HOH A . T 9 HOH 395 2214 2214 HOH HOH A . T 9 HOH 396 2216 2216 HOH HOH A . T 9 HOH 397 2217 2217 HOH HOH A . T 9 HOH 398 2218 2218 HOH HOH A . T 9 HOH 399 2219 2219 HOH HOH A . T 9 HOH 400 2220 2220 HOH HOH A . T 9 HOH 401 2221 2221 HOH HOH A . T 9 HOH 402 2222 2222 HOH HOH A . T 9 HOH 403 2223 2223 HOH HOH A . T 9 HOH 404 2225 2225 HOH HOH A . T 9 HOH 405 2227 2227 HOH HOH A . T 9 HOH 406 2229 2229 HOH HOH A . T 9 HOH 407 2230 2230 HOH HOH A . T 9 HOH 408 2231 2231 HOH HOH A . T 9 HOH 409 2232 2232 HOH HOH A . T 9 HOH 410 2233 2233 HOH HOH A . T 9 HOH 411 2234 2234 HOH HOH A . T 9 HOH 412 2235 2235 HOH HOH A . T 9 HOH 413 2236 2236 HOH HOH A . T 9 HOH 414 2238 2238 HOH HOH A . T 9 HOH 415 2241 2241 HOH HOH A . T 9 HOH 416 2242 2242 HOH HOH A . T 9 HOH 417 2244 2244 HOH HOH A . T 9 HOH 418 2245 2245 HOH HOH A . T 9 HOH 419 2246 2246 HOH HOH A . T 9 HOH 420 2247 2247 HOH HOH A . T 9 HOH 421 2249 2249 HOH HOH A . T 9 HOH 422 2250 2250 HOH HOH A . T 9 HOH 423 2251 2251 HOH HOH A . T 9 HOH 424 2252 2252 HOH HOH A . T 9 HOH 425 2253 2253 HOH HOH A . T 9 HOH 426 2254 2254 HOH HOH A . T 9 HOH 427 2256 2256 HOH HOH A . T 9 HOH 428 2257 2257 HOH HOH A . T 9 HOH 429 2258 2258 HOH HOH A . T 9 HOH 430 2259 2259 HOH HOH A . T 9 HOH 431 2260 2260 HOH HOH A . T 9 HOH 432 2261 2261 HOH HOH A . T 9 HOH 433 2264 2264 HOH HOH A . T 9 HOH 434 2265 2265 HOH HOH A . T 9 HOH 435 2266 2266 HOH HOH A . T 9 HOH 436 2271 2271 HOH HOH A . T 9 HOH 437 2273 2273 HOH HOH A . T 9 HOH 438 2274 2274 HOH HOH A . T 9 HOH 439 2275 2275 HOH HOH A . T 9 HOH 440 2276 2276 HOH HOH A . T 9 HOH 441 2277 2277 HOH HOH A . T 9 HOH 442 2278 2278 HOH HOH A . T 9 HOH 443 2279 2279 HOH HOH A . T 9 HOH 444 2281 2281 HOH HOH A . T 9 HOH 445 2282 2282 HOH HOH A . T 9 HOH 446 2284 2284 HOH HOH A . T 9 HOH 447 2285 2285 HOH HOH A . T 9 HOH 448 2286 2286 HOH HOH A . T 9 HOH 449 2287 2287 HOH HOH A . T 9 HOH 450 2288 2288 HOH HOH A . T 9 HOH 451 2289 2289 HOH HOH A . T 9 HOH 452 2290 2290 HOH HOH A . T 9 HOH 453 2291 2291 HOH HOH A . T 9 HOH 454 2292 2292 HOH HOH A . T 9 HOH 455 2294 2294 HOH HOH A . T 9 HOH 456 2296 2296 HOH HOH A . T 9 HOH 457 2298 2298 HOH HOH A . T 9 HOH 458 2299 2299 HOH HOH A . T 9 HOH 459 2301 2301 HOH HOH A . T 9 HOH 460 2302 2302 HOH HOH A . T 9 HOH 461 2303 2303 HOH HOH A . T 9 HOH 462 2304 2304 HOH HOH A . T 9 HOH 463 2305 2305 HOH HOH A . T 9 HOH 464 2307 2307 HOH HOH A . T 9 HOH 465 2310 2310 HOH HOH A . T 9 HOH 466 2311 2311 HOH HOH A . T 9 HOH 467 2316 2316 HOH HOH A . T 9 HOH 468 2317 2317 HOH HOH A . T 9 HOH 469 2319 2319 HOH HOH A . T 9 HOH 470 2322 2322 HOH HOH A . T 9 HOH 471 2325 2325 HOH HOH A . T 9 HOH 472 2329 2329 HOH HOH A . T 9 HOH 473 2331 2331 HOH HOH A . T 9 HOH 474 2333 2333 HOH HOH A . T 9 HOH 475 2334 2334 HOH HOH A . T 9 HOH 476 2337 2337 HOH HOH A . T 9 HOH 477 2340 2340 HOH HOH A . T 9 HOH 478 2348 2348 HOH HOH A . T 9 HOH 479 2349 2349 HOH HOH A . T 9 HOH 480 2350 2350 HOH HOH A . T 9 HOH 481 2353 2353 HOH HOH A . T 9 HOH 482 2354 2354 HOH HOH A . T 9 HOH 483 2356 2356 HOH HOH A . T 9 HOH 484 2357 2357 HOH HOH A . T 9 HOH 485 2362 2362 HOH HOH A . T 9 HOH 486 2363 2363 HOH HOH A . T 9 HOH 487 2365 2365 HOH HOH A . T 9 HOH 488 2366 2366 HOH HOH A . T 9 HOH 489 2369 2369 HOH HOH A . T 9 HOH 490 2375 2375 HOH HOH A . T 9 HOH 491 2376 2376 HOH HOH A . T 9 HOH 492 2377 2377 HOH HOH A . T 9 HOH 493 2378 2378 HOH HOH A . T 9 HOH 494 2387 2387 HOH HOH A . T 9 HOH 495 2388 2388 HOH HOH A . T 9 HOH 496 2389 2389 HOH HOH A . T 9 HOH 497 2398 2398 HOH HOH A . T 9 HOH 498 2403 2403 HOH HOH A . T 9 HOH 499 2410 2410 HOH HOH A . T 9 HOH 500 2415 2415 HOH HOH A . T 9 HOH 501 2416 2416 HOH HOH A . T 9 HOH 502 2418 2418 HOH HOH A . T 9 HOH 503 2430 2430 HOH HOH A . T 9 HOH 504 2432 2432 HOH HOH A . T 9 HOH 505 2433 2433 HOH HOH A . T 9 HOH 506 2434 2434 HOH HOH A . T 9 HOH 507 2435 2435 HOH HOH A . T 9 HOH 508 2436 2436 HOH HOH A . T 9 HOH 509 2437 2437 HOH HOH A . T 9 HOH 510 2438 2438 HOH HOH A . T 9 HOH 511 2439 2439 HOH HOH A . T 9 HOH 512 2440 2440 HOH HOH A . T 9 HOH 513 2441 2441 HOH HOH A . T 9 HOH 514 2442 2442 HOH HOH A . T 9 HOH 515 2443 2443 HOH HOH A . T 9 HOH 516 2444 2444 HOH HOH A . T 9 HOH 517 2445 2445 HOH HOH A . T 9 HOH 518 2446 2446 HOH HOH A . T 9 HOH 519 2447 2447 HOH HOH A . T 9 HOH 520 2448 2448 HOH HOH A . T 9 HOH 521 2449 2449 HOH HOH A . T 9 HOH 522 2450 2450 HOH HOH A . T 9 HOH 523 2451 2451 HOH HOH A . T 9 HOH 524 2452 2452 HOH HOH A . T 9 HOH 525 2453 2453 HOH HOH A . T 9 HOH 526 2454 2454 HOH HOH A . T 9 HOH 527 2455 2455 HOH HOH A . T 9 HOH 528 2456 2456 HOH HOH A . T 9 HOH 529 2457 2457 HOH HOH A . T 9 HOH 530 2458 2458 HOH HOH A . T 9 HOH 531 2459 2459 HOH HOH A . T 9 HOH 532 2460 2460 HOH HOH A . T 9 HOH 533 2461 2461 HOH HOH A . T 9 HOH 534 2462 2462 HOH HOH A . T 9 HOH 535 2463 2463 HOH HOH A . T 9 HOH 536 2464 2464 HOH HOH A . T 9 HOH 537 2465 2465 HOH HOH A . T 9 HOH 538 2466 2466 HOH HOH A . T 9 HOH 539 2467 2467 HOH HOH A . T 9 HOH 540 2468 2468 HOH HOH A . T 9 HOH 541 2469 2469 HOH HOH A . T 9 HOH 542 2470 2470 HOH HOH A . T 9 HOH 543 2471 2471 HOH HOH A . T 9 HOH 544 2472 2472 HOH HOH A . T 9 HOH 545 2473 2473 HOH HOH A . T 9 HOH 546 2474 2474 HOH HOH A . T 9 HOH 547 2475 2475 HOH HOH A . T 9 HOH 548 2476 2476 HOH HOH A . T 9 HOH 549 2477 2477 HOH HOH A . T 9 HOH 550 2478 2478 HOH HOH A . T 9 HOH 551 2479 2479 HOH HOH A . T 9 HOH 552 2480 2480 HOH HOH A . T 9 HOH 553 2481 2481 HOH HOH A . T 9 HOH 554 2482 2482 HOH HOH A . T 9 HOH 555 2483 2483 HOH HOH A . T 9 HOH 556 2484 2484 HOH HOH A . T 9 HOH 557 2485 2485 HOH HOH A . T 9 HOH 558 2486 2486 HOH HOH A . T 9 HOH 559 2487 2487 HOH HOH A . T 9 HOH 560 2488 2488 HOH HOH A . T 9 HOH 561 2489 2489 HOH HOH A . T 9 HOH 562 2490 2490 HOH HOH A . T 9 HOH 563 2491 2491 HOH HOH A . T 9 HOH 564 2492 2492 HOH HOH A . T 9 HOH 565 2493 2493 HOH HOH A . T 9 HOH 566 2494 2494 HOH HOH A . T 9 HOH 567 2495 2495 HOH HOH A . T 9 HOH 568 2496 2496 HOH HOH A . T 9 HOH 569 2497 2497 HOH HOH A . T 9 HOH 570 2498 2498 HOH HOH A . T 9 HOH 571 2499 2499 HOH HOH A . T 9 HOH 572 2500 2500 HOH HOH A . T 9 HOH 573 2501 2501 HOH HOH A . T 9 HOH 574 2502 2502 HOH HOH A . T 9 HOH 575 2503 2503 HOH HOH A . T 9 HOH 576 2504 2504 HOH HOH A . T 9 HOH 577 2505 2505 HOH HOH A . T 9 HOH 578 2506 2506 HOH HOH A . T 9 HOH 579 2507 2507 HOH HOH A . T 9 HOH 580 2508 2508 HOH HOH A . T 9 HOH 581 2509 2509 HOH HOH A . T 9 HOH 582 2510 2510 HOH HOH A . T 9 HOH 583 2511 2511 HOH HOH A . T 9 HOH 584 2512 2512 HOH HOH A . #