data_4OC0 # _entry.id 4OC0 # _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 4OC0 RCSB RCSB084301 WWPDB D_1000084301 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4OC1 . unspecified PDB 4OC2 . unspecified PDB 4OC3 . unspecified PDB 4OC4 . unspecified PDB 4OC5 . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4OC0 _pdbx_database_status.recvd_initial_deposition_date 2014-01-08 _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.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Pavlicek, J.' 1 'Ptacek, J.' 2 'Cerny, J.' 3 'Byun, Y.' 4 'Skultetyova, L.' 5 'Pomper, M.' 6 'Lubkowski, J.' 7 'Barinka, C.' 8 # _citation.id primary _citation.title ;Structural characterization of P1'-diversified urea-based inhibitors of glutamate carboxypeptidase II. ; _citation.journal_abbrev Bioorg.Med.Chem.Lett. _citation.journal_volume 24 _citation.page_first 2340 _citation.page_last 2345 _citation.year 2014 _citation.journal_id_ASTM BMCLE8 _citation.country UK _citation.journal_id_ISSN 0960-894X _citation.journal_id_CSD 1127 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24731280 _citation.pdbx_database_id_DOI 10.1016/j.bmcl.2014.03.066 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Pavlicek, J.' 1 primary 'Ptacek, J.' 2 primary 'Cerny, J.' 3 primary 'Byun, Y.' 4 primary 'Skultetyova, L.' 5 primary 'Pomper, M.G.' 6 primary 'Lubkowski, J.' 7 primary 'Barinka, C.' 8 # _cell.entry_id 4OC0 _cell.length_a 101.376 _cell.length_b 129.938 _cell.length_c 158.575 _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 4OC0 _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~-[(1-carboxycyclopropyl)carbamoyl]-N~6~-(4-iodobenzoyl)-L-lysine' 503.288 1 ? ? ? ? 9 water nat water 18.015 450 ? ? ? ? # _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 'FOLH, FOLH1, GIG27, NAALAD1, PSM, PSMA' _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 ;Schneider's S2 cells ; _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type plasmid _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 4OC0 _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 4OC0 ARG A 1 ? UNP Q04609 ? ? 'EXPRESSION TAG' 42 1 1 4OC0 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 2R7 non-polymer . 'N~2~-[(1-carboxycyclopropyl)carbamoyl]-N~6~-(4-iodobenzoyl)-L-lysine' ? 'C18 H22 I N3 O6' 503.288 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 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 4OC0 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.27 _exptl_crystal.density_percent_sol 62.38 _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 _exptl_crystal_grow.pdbx_details ;33% (v/v) pentaerythritol propoxylate PO/OH 5/4, 1% (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 300 mm CCD' _diffrn_detector.pdbx_collection_date 2009-06-25 _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 _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 # _reflns.entry_id 4OC0 _reflns.observed_criterion_sigma_I -3 _reflns.observed_criterion_sigma_F -3 _reflns.d_resolution_low 30.0 _reflns.d_resolution_high 1.85 _reflns.number_obs 89273 _reflns.number_all 89273 _reflns.percent_possible_obs 99.9 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _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 # _reflns_shell.d_res_high 1.85 _reflns_shell.d_res_low 1.92 _reflns_shell.percent_possible_all 99.6 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 4OC0 _refine.ls_number_reflns_obs 87605 _refine.ls_number_reflns_all 87605 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F -3 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 28.47 _refine.ls_d_res_high 1.85 _refine.ls_percent_reflns_obs 99.25 _refine.ls_R_factor_obs 0.16101 _refine.ls_R_factor_all 0.16101 _refine.ls_R_factor_R_work 0.16069 _refine.ls_R_factor_R_free 0.18150 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 1.5 _refine.ls_number_reflns_R_free 1319 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.970 _refine.correlation_coeff_Fo_to_Fc_free 0.962 _refine.B_iso_mean 36.426 _refine.aniso_B[1][1] 0.00 _refine.aniso_B[2][2] 0.00 _refine.aniso_B[3][3] 0.00 _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 0.097 _refine.pdbx_overall_ESU_R_Free 0.092 _refine.overall_SU_ML 0.064 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 4.560 _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_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 5529 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 208 _refine_hist.number_atoms_solvent 450 _refine_hist.number_atoms_total 6187 _refine_hist.d_res_high 1.85 _refine_hist.d_res_low 28.47 # 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 0.019 0.022 ? 6237 ? 'X-RAY DIFFRACTION' r_bond_other_d ? ? ? ? ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.646 1.996 ? 8505 ? 'X-RAY DIFFRACTION' r_angle_other_deg ? ? ? ? ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 5.824 5.000 ? 757 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 36.034 23.924 ? 288 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 14.690 15.000 ? 1043 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 13.838 15.000 ? 35 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.202 0.200 ? 917 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.010 0.021 ? 4806 ? '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 0.966 1.500 ? 3622 ? 'X-RAY DIFFRACTION' r_mcbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcangle_it 1.669 2.000 ? 5911 ? 'X-RAY DIFFRACTION' r_mcangle_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_scbond_it 2.750 3.000 ? 2615 ? 'X-RAY DIFFRACTION' r_scbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_scangle_it 4.479 4.500 ? 2571 ? 'X-RAY DIFFRACTION' r_scangle_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_long_range_B_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_long_range_B_other ? ? ? ? ? '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 1.847 _refine_ls_shell.d_res_low 1.895 _refine_ls_shell.number_reflns_R_work 6155 _refine_ls_shell.R_factor_R_work 0.215 _refine_ls_shell.percent_reflns_obs 96.00 _refine_ls_shell.R_factor_R_free 0.197 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 93 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs 6248 _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 4OC0 _struct.title ;X-ray structure of of human glutamate carboxypeptidase II (GCPII) in a complex with CCIBzL, a urea-based inhibitor N~2~-[(1-carboxycyclopropyl)carbamoyl]-N~6~-(4-iodobenzoyl)-L-lysine ; _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 4OC0 _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 ? ? A ASN 35 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 76 A NAG 801 1_555 ? ? ? ? ? ? ? 1.419 ? covale2 covale ? ? L NAG . O4 ? ? ? 1_555 M BMA . C1 ? ? A NAG 811 A BMA 812 1_555 ? ? ? ? ? ? ? 1.431 ? covale3 covale ? ? A ASN 418 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 459 A NAG 807 1_555 ? ? ? ? ? ? ? 1.438 ? covale4 covale ? ? A ASN 435 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 476 A NAG 808 1_555 ? ? ? ? ? ? ? 1.439 ? covale5 covale ? ? K NAG . O4 ? ? ? 1_555 L NAG . C1 ? ? A NAG 810 A NAG 811 1_555 ? ? ? ? ? ? ? 1.442 ? covale6 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 801 A NAG 802 1_555 ? ? ? ? ? ? ? 1.444 ? covale7 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 808 A NAG 809 1_555 ? ? ? ? ? ? ? 1.446 ? covale8 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 804 A NAG 805 1_555 ? ? ? ? ? ? ? 1.446 ? covale9 covale ? ? A ASN 99 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 140 A NAG 804 1_555 ? ? ? ? ? ? ? 1.447 ? covale10 covale ? ? A ASN 80 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 121 A NAG 803 1_555 ? ? ? ? ? ? ? 1.447 ? covale11 covale ? ? M BMA . O3 ? ? ? 1_555 N MAN . C1 ? ? A BMA 812 A MAN 813 1_555 ? ? ? ? ? ? ? 1.451 ? covale12 covale ? ? A ASN 597 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 638 A NAG 810 1_555 ? ? ? ? ? ? ? 1.454 ? covale13 covale ? ? A ASN 154 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 195 A NAG 806 1_555 ? ? ? ? ? ? ? 1.456 ? metalc1 metalc ? ? P ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 815 A HOH 1347 1_555 ? ? ? ? ? ? ? 1.917 ? metalc2 metalc ? ? A ASP 346 OD1 ? ? ? 1_555 P ZN . ZN ? ? A ASP 387 A ZN 815 1_555 ? ? ? ? ? ? ? 1.961 ? metalc3 metalc ? ? A ASP 412 OD2 ? ? ? 1_555 P ZN . ZN ? ? A ASP 453 A ZN 815 1_555 ? ? ? ? ? ? ? 1.988 ? metalc4 metalc ? ? O ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 814 A HOH 1347 1_555 ? ? ? ? ? ? ? 1.990 ? metalc5 metalc ? ? A HIS 336 NE2 ? ? ? 1_555 P ZN . ZN ? ? A HIS 377 A ZN 815 1_555 ? ? ? ? ? ? ? 1.997 ? metalc6 metalc ? ? A HIS 512 NE2 ? ? ? 1_555 O ZN . ZN ? ? A HIS 553 A ZN 814 1_555 ? ? ? ? ? ? ? 2.043 ? metalc7 metalc ? ? A GLU 384 OE2 ? ? ? 1_555 O ZN . ZN ? ? A GLU 425 A ZN 814 1_555 ? ? ? ? ? ? ? 2.089 ? metalc8 metalc ? ? A ASP 346 OD2 ? ? ? 1_555 O ZN . ZN ? ? A ASP 387 A ZN 814 1_555 ? ? ? ? ? ? ? 2.116 ? metalc9 metalc ? ? A GLU 395 OE2 ? ? ? 1_555 Q CA . CA ? ? A GLU 436 A CA 816 1_555 ? ? ? ? ? ? ? 2.303 ? metalc10 metalc ? ? A TYR 231 O ? ? ? 1_555 Q CA . CA ? ? A TYR 272 A CA 816 1_555 ? ? ? ? ? ? ? 2.303 ? metalc11 metalc ? ? A THR 228 O ? ? ? 1_555 Q CA . CA ? ? A THR 269 A CA 816 1_555 ? ? ? ? ? ? ? 2.428 ? metalc12 metalc ? ? A GLU 392 OE2 ? ? ? 1_555 Q CA . CA ? ? A GLU 433 A CA 816 1_555 ? ? ? ? ? ? ? 2.437 ? metalc13 metalc ? ? A GLU 392 OE1 ? ? ? 1_555 Q CA . CA ? ? A GLU 433 A CA 816 1_555 ? ? ? ? ? ? ? 2.447 ? metalc14 metalc ? ? A GLU 384 OE1 ? ? ? 1_555 O ZN . ZN ? ? A GLU 425 A ZN 814 1_555 ? ? ? ? ? ? ? 2.451 ? metalc15 metalc ? ? A THR 228 OG1 ? ? ? 1_555 Q CA . CA ? ? A THR 269 A CA 816 1_555 ? ? ? ? ? ? ? 2.452 ? metalc16 metalc ? ? Q CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 816 A HOH 906 1_555 ? ? ? ? ? ? ? 2.479 ? # 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 10.44 2 GLY 289 A . ? GLY 330 A PRO 290 A ? PRO 331 A 1 -0.81 3 ASP 346 A . ? ASP 387 A PRO 347 A ? PRO 388 A 1 2.59 # 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 ALA A 652 ? N ALA A 693 O GLU A 662 ? O GLU A 703 # 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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 801' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 802' AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 803' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 804' AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 805' AC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 806' AC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 807' AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 808' AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 809' BC1 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 810' BC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 811' BC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE BMA A 812' BC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE MAN A 813' BC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ZN A 814' BC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE ZN A 815' BC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 816' BC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CL A 817' BC9 Software ? ? ? ? 18 'BINDING SITE FOR RESIDUE 2R7 A 818' # 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 4 ASN A 35 ? ASN A 76 . ? 1_555 ? 2 AC1 4 GLN A 58 ? GLN A 99 . ? 1_555 ? 3 AC1 4 NAG C . ? NAG A 802 . ? 1_555 ? 4 AC1 4 HOH T . ? HOH A 1131 . ? 1_555 ? 5 AC2 3 NAG B . ? NAG A 801 . ? 1_555 ? 6 AC2 3 HOH T . ? HOH A 1138 . ? 1_555 ? 7 AC2 3 HOH T . ? HOH A 1325 . ? 1_555 ? 8 AC3 4 ASN A 80 ? ASN A 121 . ? 1_555 ? 9 AC3 4 THR A 82 ? THR A 123 . ? 1_555 ? 10 AC3 4 HIS A 83 ? HIS A 124 . ? 1_555 ? 11 AC3 4 THR A 308 ? THR A 349 . ? 1_555 ? 12 AC4 5 TYR A 86 ? TYR A 127 . ? 1_555 ? 13 AC4 5 GLU A 96 ? GLU A 137 . ? 1_555 ? 14 AC4 5 ILE A 97 ? ILE A 138 . ? 1_555 ? 15 AC4 5 ASN A 99 ? ASN A 140 . ? 1_555 ? 16 AC4 5 NAG F . ? NAG A 805 . ? 1_555 ? 17 AC5 3 NAG E . ? NAG A 804 . ? 1_555 ? 18 AC5 3 HOH T . ? HOH A 1234 . ? 1_555 ? 19 AC5 3 HOH T . ? HOH A 1323 . ? 1_555 ? 20 AC6 2 ASN A 154 ? ASN A 195 . ? 1_555 ? 21 AC6 2 SER A 156 ? SER A 197 . ? 1_555 ? 22 AC7 6 TRP A 205 ? TRP A 246 . ? 1_555 ? 23 AC7 6 ASN A 418 ? ASN A 459 . ? 1_555 ? 24 AC7 6 PHE A 524 ? PHE A 565 . ? 1_555 ? 25 AC7 6 TYR A 525 ? TYR A 566 . ? 1_555 ? 26 AC7 6 HOH T . ? HOH A 977 . ? 1_555 ? 27 AC7 6 HOH T . ? HOH A 1151 . ? 1_555 ? 28 AC8 4 SER A 431 ? SER A 472 . ? 1_555 ? 29 AC8 4 ASN A 435 ? ASN A 476 . ? 1_555 ? 30 AC8 4 PRO A 553 ? PRO A 594 . ? 1_555 ? 31 AC8 4 NAG J . ? NAG A 809 . ? 1_555 ? 32 AC9 3 GLN A 610 ? GLN A 651 . ? 1_555 ? 33 AC9 3 NAG I . ? NAG A 808 . ? 1_555 ? 34 AC9 3 HOH T . ? HOH A 1335 . ? 1_555 ? 35 BC1 8 GLU A 235 ? GLU A 276 . ? 2_565 ? 36 BC1 8 SER A 590 ? SER A 631 . ? 1_555 ? 37 BC1 8 SER A 593 ? SER A 634 . ? 1_555 ? 38 BC1 8 ASN A 597 ? ASN A 638 . ? 1_555 ? 39 BC1 8 GLN A 699 ? GLN A 740 . ? 1_555 ? 40 BC1 8 NAG L . ? NAG A 811 . ? 1_555 ? 41 BC1 8 HOH T . ? HOH A 1023 . ? 1_555 ? 42 BC1 8 HOH T . ? HOH A 1207 . ? 1_555 ? 43 BC2 3 GLU A 235 ? GLU A 276 . ? 2_565 ? 44 BC2 3 NAG K . ? NAG A 810 . ? 1_555 ? 45 BC2 3 BMA M . ? BMA A 812 . ? 1_555 ? 46 BC3 7 HIS A 71 ? HIS A 112 . ? 2_565 ? 47 BC3 7 GLU A 235 ? GLU A 276 . ? 2_565 ? 48 BC3 7 ARG A 313 ? ARG A 354 . ? 2_565 ? 49 BC3 7 NAG L . ? NAG A 811 . ? 1_555 ? 50 BC3 7 MAN N . ? MAN A 813 . ? 1_555 ? 51 BC3 7 HOH T . ? HOH A 1326 . ? 1_555 ? 52 BC3 7 HOH T . ? HOH A 1327 . ? 1_555 ? 53 BC4 8 PHE A 194 ? PHE A 235 . ? 7_555 ? 54 BC4 8 LYS A 199 ? LYS A 240 . ? 7_555 ? 55 BC4 8 SER A 200 ? SER A 241 . ? 7_555 ? 56 BC4 8 GLU A 235 ? GLU A 276 . ? 2_565 ? 57 BC4 8 BMA M . ? BMA A 812 . ? 1_555 ? 58 BC4 8 HOH T . ? HOH A 1083 . ? 1_555 ? 59 BC4 8 HOH T . ? HOH A 1205 . ? 1_555 ? 60 BC4 8 HOH T . ? HOH A 1321 . ? 7_555 ? 61 BC5 6 ASP A 346 ? ASP A 387 . ? 1_555 ? 62 BC5 6 GLU A 384 ? GLU A 425 . ? 1_555 ? 63 BC5 6 HIS A 512 ? HIS A 553 . ? 1_555 ? 64 BC5 6 ZN P . ? ZN A 815 . ? 1_555 ? 65 BC5 6 2R7 S . ? 2R7 A 818 . ? 1_555 ? 66 BC5 6 HOH T . ? HOH A 1347 . ? 1_555 ? 67 BC6 7 HIS A 336 ? HIS A 377 . ? 1_555 ? 68 BC6 7 ASP A 346 ? ASP A 387 . ? 1_555 ? 69 BC6 7 GLU A 383 ? GLU A 424 . ? 1_555 ? 70 BC6 7 GLU A 384 ? GLU A 425 . ? 1_555 ? 71 BC6 7 ASP A 412 ? ASP A 453 . ? 1_555 ? 72 BC6 7 ZN O . ? ZN A 814 . ? 1_555 ? 73 BC6 7 HOH T . ? HOH A 1347 . ? 1_555 ? 74 BC7 5 THR A 228 ? THR A 269 . ? 1_555 ? 75 BC7 5 TYR A 231 ? TYR A 272 . ? 1_555 ? 76 BC7 5 GLU A 392 ? GLU A 433 . ? 1_555 ? 77 BC7 5 GLU A 395 ? GLU A 436 . ? 1_555 ? 78 BC7 5 HOH T . ? HOH A 906 . ? 1_555 ? 79 BC8 4 ASN A 410 ? ASN A 451 . ? 1_555 ? 80 BC8 4 ASP A 412 ? ASP A 453 . ? 1_555 ? 81 BC8 4 ARG A 493 ? ARG A 534 . ? 1_555 ? 82 BC8 4 ARG A 495 ? ARG A 536 . ? 1_555 ? 83 BC9 18 ARG A 169 ? ARG A 210 . ? 1_555 ? 84 BC9 18 GLU A 383 ? GLU A 424 . ? 1_555 ? 85 BC9 18 GLU A 384 ? GLU A 425 . ? 1_555 ? 86 BC9 18 SER A 413 ? SER A 454 . ? 1_555 ? 87 BC9 18 ARG A 422 ? ARG A 463 . ? 1_555 ? 88 BC9 18 ASP A 424 ? ASP A 465 . ? 1_555 ? 89 BC9 18 GLY A 477 ? GLY A 518 . ? 1_555 ? 90 BC9 18 ASN A 478 ? ASN A 519 . ? 1_555 ? 91 BC9 18 ARG A 493 ? ARG A 534 . ? 1_555 ? 92 BC9 18 ARG A 495 ? ARG A 536 . ? 1_555 ? 93 BC9 18 TYR A 511 ? TYR A 552 . ? 1_555 ? 94 BC9 18 HIS A 512 ? HIS A 553 . ? 1_555 ? 95 BC9 18 TYR A 659 ? TYR A 700 . ? 1_555 ? 96 BC9 18 ZN O . ? ZN A 814 . ? 1_555 ? 97 BC9 18 HOH T . ? HOH A 909 . ? 1_555 ? 98 BC9 18 HOH T . ? HOH A 1347 . ? 1_555 ? 99 BC9 18 HOH T . ? HOH A 1348 . ? 1_555 ? 100 BC9 18 HOH T . ? HOH A 1349 . ? 1_555 ? # _database_PDB_matrix.entry_id 4OC0 _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 4OC0 _atom_sites.fract_transf_matrix[1][1] 0.009864 _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] 0.007696 _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] 0.006306 _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 ? 16.550 45.264 82.553 1.00 67.24 ? 55 LYS A N 1 ATOM 2 C CA . LYS A 1 14 ? 16.048 46.451 81.801 1.00 65.97 ? 55 LYS A CA 1 ATOM 3 C C . LYS A 1 14 ? 15.738 46.154 80.335 1.00 63.65 ? 55 LYS A C 1 ATOM 4 O O . LYS A 1 14 ? 16.335 45.257 79.714 1.00 62.87 ? 55 LYS A O 1 ATOM 5 C CB . LYS A 1 14 ? 17.045 47.610 81.887 1.00 66.82 ? 55 LYS A CB 1 ATOM 6 C CG . LYS A 1 14 ? 16.377 48.971 82.046 1.00 69.52 ? 55 LYS A CG 1 ATOM 7 C CD . LYS A 1 14 ? 16.041 49.241 83.528 1.00 73.38 ? 55 LYS A CD 1 ATOM 8 C CE . LYS A 1 14 ? 14.911 50.258 83.693 1.00 74.92 ? 55 LYS A CE 1 ATOM 9 N NZ . LYS A 1 14 ? 15.040 51.445 82.776 1.00 75.96 ? 55 LYS A NZ 1 ATOM 10 N N . HIS A 1 15 ? 14.791 46.915 79.797 1.00 61.33 ? 56 HIS A N 1 ATOM 11 C CA . HIS A 1 15 ? 14.431 46.820 78.391 1.00 58.45 ? 56 HIS A CA 1 ATOM 12 C C . HIS A 1 15 ? 14.891 48.092 77.701 1.00 55.75 ? 56 HIS A C 1 ATOM 13 O O . HIS A 1 15 ? 14.179 49.109 77.717 1.00 56.41 ? 56 HIS A O 1 ATOM 14 C CB . HIS A 1 15 ? 12.923 46.618 78.236 1.00 58.86 ? 56 HIS A CB 1 ATOM 15 C CG . HIS A 1 15 ? 12.438 45.279 78.704 1.00 61.06 ? 56 HIS A CG 1 ATOM 16 N ND1 . HIS A 1 15 ? 11.358 45.132 79.554 1.00 63.28 ? 56 HIS A ND1 1 ATOM 17 C CD2 . HIS A 1 15 ? 12.892 44.026 78.447 1.00 61.38 ? 56 HIS A CD2 1 ATOM 18 C CE1 . HIS A 1 15 ? 11.165 43.846 79.794 1.00 65.82 ? 56 HIS A CE1 1 ATOM 19 N NE2 . HIS A 1 15 ? 12.079 43.154 79.132 1.00 64.72 ? 56 HIS A NE2 1 ATOM 20 N N . ASN A 1 16 ? 16.103 48.035 77.139 1.00 51.23 ? 57 ASN A N 1 ATOM 21 C CA . ASN A 1 16 ? 16.724 49.152 76.439 1.00 47.07 ? 57 ASN A CA 1 ATOM 22 C C . ASN A 1 16 ? 17.374 48.618 75.165 1.00 43.47 ? 57 ASN A C 1 ATOM 23 O O . ASN A 1 16 ? 17.192 47.445 74.832 1.00 40.55 ? 57 ASN A O 1 ATOM 24 C CB . ASN A 1 16 ? 17.779 49.827 77.317 1.00 47.88 ? 57 ASN A CB 1 ATOM 25 C CG . ASN A 1 16 ? 18.728 48.839 77.960 1.00 48.85 ? 57 ASN A CG 1 ATOM 26 O OD1 . ASN A 1 16 ? 18.865 47.678 77.535 1.00 45.12 ? 57 ASN A OD1 1 ATOM 27 N ND2 . ASN A 1 16 ? 19.386 49.289 79.033 1.00 49.69 ? 57 ASN A ND2 1 ATOM 28 N N . MET A 1 17 ? 18.136 49.456 74.467 1.00 40.95 ? 58 MET A N 1 ATOM 29 C CA . MET A 1 17 ? 18.642 48.986 73.179 1.00 39.77 ? 58 MET A CA 1 ATOM 30 C C . MET A 1 17 ? 19.656 47.861 73.368 1.00 39.26 ? 58 MET A C 1 ATOM 31 O O . MET A 1 17 ? 19.661 46.923 72.599 1.00 38.25 ? 58 MET A O 1 ATOM 32 C CB A MET A 1 17 ? 19.194 50.064 72.282 0.65 39.22 ? 58 MET A CB 1 ATOM 33 C CB B MET A 1 17 ? 19.278 50.153 72.393 0.35 39.25 ? 58 MET A CB 1 ATOM 34 C CG A MET A 1 17 ? 19.272 49.510 70.829 0.65 39.00 ? 58 MET A CG 1 ATOM 35 C CG B MET A 1 17 ? 19.379 49.945 70.848 0.35 39.61 ? 58 MET A CG 1 ATOM 36 S SD A MET A 1 17 ? 20.364 50.472 69.833 0.65 40.16 ? 58 MET A SD 1 ATOM 37 S SD B MET A 1 17 ? 19.558 51.493 69.896 0.35 41.15 ? 58 MET A SD 1 ATOM 38 C CE A MET A 1 17 ? 21.564 50.958 71.076 0.65 45.28 ? 58 MET A CE 1 ATOM 39 C CE B MET A 1 17 ? 21.178 52.021 70.417 0.35 38.64 ? 58 MET A CE 1 ATOM 40 N N . LYS A 1 18 ? 20.467 47.944 74.408 1.00 39.17 ? 59 LYS A N 1 ATOM 41 C CA . LYS A 1 18 ? 21.415 46.871 74.675 1.00 39.99 ? 59 LYS A CA 1 ATOM 42 C C . LYS A 1 18 ? 20.708 45.525 74.861 1.00 39.95 ? 59 LYS A C 1 ATOM 43 O O . LYS A 1 18 ? 21.178 44.530 74.346 1.00 39.63 ? 59 LYS A O 1 ATOM 44 C CB . LYS A 1 18 ? 22.306 47.207 75.889 1.00 41.09 ? 59 LYS A CB 1 ATOM 45 C CG . LYS A 1 18 ? 23.472 46.230 76.044 1.00 44.43 ? 59 LYS A CG 1 ATOM 46 C CD . LYS A 1 18 ? 24.600 46.884 76.908 1.00 52.74 ? 59 LYS A CD 1 ATOM 47 C CE . LYS A 1 18 ? 25.881 46.032 76.876 1.00 57.11 ? 59 LYS A CE 1 ATOM 48 N NZ . LYS A 1 18 ? 25.767 44.968 77.914 1.00 60.37 ? 59 LYS A NZ 1 ATOM 49 N N . ALA A 1 19 ? 19.585 45.488 75.599 1.00 40.57 ? 60 ALA A N 1 ATOM 50 C CA . ALA A 1 19 ? 18.817 44.228 75.748 1.00 40.52 ? 60 ALA A CA 1 ATOM 51 C C . ALA A 1 19 ? 18.373 43.674 74.369 1.00 38.69 ? 60 ALA A C 1 ATOM 52 O O . ALA A 1 19 ? 18.518 42.484 74.102 1.00 37.66 ? 60 ALA A O 1 ATOM 53 C CB . ALA A 1 19 ? 17.602 44.454 76.600 1.00 41.86 ? 60 ALA A CB 1 ATOM 54 N N . PHE A 1 20 ? 17.821 44.562 73.538 1.00 36.88 ? 61 PHE A N 1 ATOM 55 C CA . PHE A 1 20 ? 17.419 44.205 72.158 1.00 36.24 ? 61 PHE A CA 1 ATOM 56 C C . PHE A 1 20 ? 18.606 43.609 71.365 1.00 35.41 ? 61 PHE A C 1 ATOM 57 O O . PHE A 1 20 ? 18.533 42.501 70.779 1.00 34.64 ? 61 PHE A O 1 ATOM 58 C CB . PHE A 1 20 ? 16.841 45.418 71.421 1.00 34.35 ? 61 PHE A CB 1 ATOM 59 C CG . PHE A 1 20 ? 16.715 45.184 69.933 1.00 34.59 ? 61 PHE A CG 1 ATOM 60 C CD1 . PHE A 1 20 ? 15.740 44.308 69.430 1.00 32.75 ? 61 PHE A CD1 1 ATOM 61 C CD2 . PHE A 1 20 ? 17.608 45.769 69.072 1.00 32.60 ? 61 PHE A CD2 1 ATOM 62 C CE1 . PHE A 1 20 ? 15.665 44.048 68.035 1.00 34.02 ? 61 PHE A CE1 1 ATOM 63 C CE2 . PHE A 1 20 ? 17.542 45.516 67.682 1.00 34.78 ? 61 PHE A CE2 1 ATOM 64 C CZ . PHE A 1 20 ? 16.565 44.669 67.187 1.00 31.94 ? 61 PHE A CZ 1 ATOM 65 N N . LEU A 1 21 ? 19.691 44.361 71.337 1.00 35.11 ? 62 LEU A N 1 ATOM 66 C CA . LEU A 1 21 ? 20.872 43.967 70.582 1.00 35.53 ? 62 LEU A CA 1 ATOM 67 C C . LEU A 1 21 ? 21.518 42.652 71.052 1.00 37.71 ? 62 LEU A C 1 ATOM 68 O O . LEU A 1 21 ? 21.958 41.833 70.224 1.00 36.62 ? 62 LEU A O 1 ATOM 69 C CB . LEU A 1 21 ? 21.902 45.091 70.635 1.00 36.18 ? 62 LEU A CB 1 ATOM 70 C CG . LEU A 1 21 ? 21.515 46.383 69.904 1.00 35.28 ? 62 LEU A CG 1 ATOM 71 C CD1 . LEU A 1 21 ? 22.562 47.413 70.224 1.00 36.68 ? 62 LEU A CD1 1 ATOM 72 C CD2 . LEU A 1 21 ? 21.390 46.174 68.371 1.00 35.12 ? 62 LEU A CD2 1 ATOM 73 N N . ASP A 1 22 ? 21.571 42.457 72.360 1.00 40.16 ? 63 ASP A N 1 ATOM 74 C CA . ASP A 1 22 ? 22.191 41.235 72.934 1.00 42.57 ? 63 ASP A CA 1 ATOM 75 C C . ASP A 1 22 ? 21.375 39.993 72.627 1.00 41.99 ? 63 ASP A C 1 ATOM 76 O O . ASP A 1 22 ? 21.894 38.886 72.682 1.00 42.74 ? 63 ASP A O 1 ATOM 77 C CB . ASP A 1 22 ? 22.345 41.347 74.456 1.00 44.89 ? 63 ASP A CB 1 ATOM 78 C CG . ASP A 1 22 ? 23.456 42.304 74.878 1.00 48.93 ? 63 ASP A CG 1 ATOM 79 O OD1 . ASP A 1 22 ? 24.267 42.726 74.021 1.00 51.75 ? 63 ASP A OD1 1 ATOM 80 O OD2 . ASP A 1 22 ? 23.510 42.646 76.088 1.00 54.48 ? 63 ASP A OD2 1 ATOM 81 N N . GLU A 1 23 ? 20.097 40.169 72.314 1.00 40.67 ? 64 GLU A N 1 ATOM 82 C CA . GLU A 1 23 ? 19.236 39.032 72.085 1.00 40.05 ? 64 GLU A CA 1 ATOM 83 C C . GLU A 1 23 ? 19.461 38.476 70.673 1.00 38.23 ? 64 GLU A C 1 ATOM 84 O O . GLU A 1 23 ? 19.242 37.283 70.442 1.00 38.68 ? 64 GLU A O 1 ATOM 85 C CB . GLU A 1 23 ? 17.765 39.428 72.285 1.00 40.63 ? 64 GLU A CB 1 ATOM 86 C CG . GLU A 1 23 ? 16.707 38.297 72.058 1.00 42.46 ? 64 GLU A CG 1 ATOM 87 C CD . GLU A 1 23 ? 16.896 37.051 72.934 1.00 48.00 ? 64 GLU A CD 1 ATOM 88 O OE1 . GLU A 1 23 ? 17.215 37.178 74.129 1.00 49.29 ? 64 GLU A OE1 1 ATOM 89 O OE2 . GLU A 1 23 ? 16.725 35.915 72.427 1.00 47.98 ? 64 GLU A OE2 1 ATOM 90 N N . LEU A 1 24 ? 19.891 39.340 69.742 1.00 35.53 ? 65 LEU A N 1 ATOM 91 C CA . LEU A 1 24 ? 20.271 38.889 68.372 1.00 34.23 ? 65 LEU A CA 1 ATOM 92 C C . LEU A 1 24 ? 21.394 37.852 68.381 1.00 35.40 ? 65 LEU A C 1 ATOM 93 O O . LEU A 1 24 ? 22.405 38.106 69.005 1.00 34.70 ? 65 LEU A O 1 ATOM 94 C CB . LEU A 1 24 ? 20.692 40.088 67.509 1.00 33.05 ? 65 LEU A CB 1 ATOM 95 C CG . LEU A 1 24 ? 19.670 41.217 67.371 1.00 32.38 ? 65 LEU A CG 1 ATOM 96 C CD1 . LEU A 1 24 ? 20.365 42.464 66.835 1.00 32.46 ? 65 LEU A CD1 1 ATOM 97 C CD2 . LEU A 1 24 ? 18.537 40.787 66.429 1.00 31.44 ? 65 LEU A CD2 1 ATOM 98 N N . LYS A 1 25 ? 21.255 36.745 67.628 1.00 34.99 ? 66 LYS A N 1 ATOM 99 C CA . LYS A 1 25 ? 22.281 35.714 67.607 1.00 36.04 ? 66 LYS A CA 1 ATOM 100 C C . LYS A 1 25 ? 22.675 35.328 66.167 1.00 35.23 ? 66 LYS A C 1 ATOM 101 O O . LYS A 1 25 ? 21.802 35.057 65.334 1.00 32.25 ? 66 LYS A O 1 ATOM 102 C CB . LYS A 1 25 ? 21.773 34.453 68.338 1.00 37.74 ? 66 LYS A CB 1 ATOM 103 C CG . LYS A 1 25 ? 21.420 34.670 69.825 1.00 41.01 ? 66 LYS A CG 1 ATOM 104 C CD . LYS A 1 25 ? 22.673 34.924 70.638 1.00 48.23 ? 66 LYS A CD 1 ATOM 105 C CE . LYS A 1 25 ? 22.402 34.946 72.166 1.00 52.11 ? 66 LYS A CE 1 ATOM 106 N NZ . LYS A 1 25 ? 21.318 35.906 72.471 1.00 50.45 ? 66 LYS A NZ 1 ATOM 107 N N . ALA A 1 26 ? 23.979 35.286 65.902 1.00 34.93 ? 67 ALA A N 1 ATOM 108 C CA . ALA A 1 26 ? 24.493 34.832 64.611 1.00 34.48 ? 67 ALA A CA 1 ATOM 109 C C . ALA A 1 26 ? 23.936 33.441 64.239 1.00 35.33 ? 67 ALA A C 1 ATOM 110 O O . ALA A 1 26 ? 23.602 33.188 63.062 1.00 34.45 ? 67 ALA A O 1 ATOM 111 C CB . ALA A 1 26 ? 26.055 34.794 64.661 1.00 35.63 ? 67 ALA A CB 1 ATOM 112 N N A GLU A 1 27 ? 23.852 32.533 65.204 0.60 36.16 ? 68 GLU A N 1 ATOM 113 N N B GLU A 1 27 ? 23.849 32.561 65.241 0.40 35.75 ? 68 GLU A N 1 ATOM 114 C CA A GLU A 1 27 ? 23.453 31.156 64.893 0.60 37.25 ? 68 GLU A CA 1 ATOM 115 C CA B GLU A 1 27 ? 23.448 31.156 65.064 0.40 36.34 ? 68 GLU A CA 1 ATOM 116 C C A GLU A 1 27 ? 21.992 31.098 64.456 0.60 35.81 ? 68 GLU A C 1 ATOM 117 C C B GLU A 1 27 ? 21.998 31.035 64.591 0.40 35.45 ? 68 GLU A C 1 ATOM 118 O O A GLU A 1 27 ? 21.625 30.272 63.605 0.60 35.17 ? 68 GLU A O 1 ATOM 119 O O B GLU A 1 27 ? 21.655 30.113 63.844 0.40 35.19 ? 68 GLU A O 1 ATOM 120 C CB A GLU A 1 27 ? 23.721 30.206 66.069 0.60 39.11 ? 68 GLU A CB 1 ATOM 121 C CB B GLU A 1 27 ? 23.695 30.335 66.354 0.40 37.70 ? 68 GLU A CB 1 ATOM 122 C CG A GLU A 1 27 ? 23.254 28.770 65.836 0.60 43.13 ? 68 GLU A CG 1 ATOM 123 C CG B GLU A 1 27 ? 22.807 30.701 67.556 0.40 38.44 ? 68 GLU A CG 1 ATOM 124 C CD A GLU A 1 27 ? 24.057 28.044 64.765 0.60 48.91 ? 68 GLU A CD 1 ATOM 125 C CD B GLU A 1 27 ? 23.486 30.480 68.929 0.40 42.18 ? 68 GLU A CD 1 ATOM 126 O OE1 A GLU A 1 27 ? 25.296 27.978 64.890 0.60 49.63 ? 68 GLU A OE1 1 ATOM 127 O OE1 B GLU A 1 27 ? 24.146 29.438 69.126 0.40 45.83 ? 68 GLU A OE1 1 ATOM 128 O OE2 A GLU A 1 27 ? 23.440 27.535 63.798 0.60 51.52 ? 68 GLU A OE2 1 ATOM 129 O OE2 B GLU A 1 27 ? 23.349 31.343 69.815 0.40 40.85 ? 68 GLU A OE2 1 ATOM 130 N N . ASN A 1 28 ? 21.155 31.977 65.015 1.00 34.86 ? 69 ASN A N 1 ATOM 131 C CA . ASN A 1 28 ? 19.770 32.028 64.554 1.00 34.16 ? 69 ASN A CA 1 ATOM 132 C C . ASN A 1 28 ? 19.649 32.522 63.126 1.00 32.93 ? 69 ASN A C 1 ATOM 133 O O . ASN A 1 28 ? 18.843 32.005 62.356 1.00 32.50 ? 69 ASN A O 1 ATOM 134 C CB . ASN A 1 28 ? 18.924 32.936 65.443 1.00 34.43 ? 69 ASN A CB 1 ATOM 135 C CG . ASN A 1 28 ? 18.631 32.309 66.771 1.00 36.93 ? 69 ASN A CG 1 ATOM 136 O OD1 . ASN A 1 28 ? 18.612 31.079 66.898 1.00 37.93 ? 69 ASN A OD1 1 ATOM 137 N ND2 . ASN A 1 28 ? 18.426 33.148 67.783 1.00 36.63 ? 69 ASN A ND2 1 ATOM 138 N N . ILE A 1 29 ? 20.439 33.532 62.785 1.00 32.18 ? 70 ILE A N 1 ATOM 139 C CA . ILE A 1 29 ? 20.423 34.075 61.405 1.00 30.97 ? 70 ILE A CA 1 ATOM 140 C C . ILE A 1 29 ? 20.854 32.956 60.443 1.00 31.42 ? 70 ILE A C 1 ATOM 141 O O . ILE A 1 29 ? 20.264 32.776 59.380 1.00 30.70 ? 70 ILE A O 1 ATOM 142 C CB . ILE A 1 29 ? 21.366 35.304 61.280 1.00 31.19 ? 70 ILE A CB 1 ATOM 143 C CG1 . ILE A 1 29 ? 20.828 36.469 62.146 1.00 30.15 ? 70 ILE A CG1 1 ATOM 144 C CG2 . ILE A 1 29 ? 21.460 35.783 59.832 1.00 30.64 ? 70 ILE A CG2 1 ATOM 145 C CD1 . ILE A 1 29 ? 21.855 37.613 62.357 1.00 31.37 ? 70 ILE A CD1 1 ATOM 146 N N . LYS A 1 30 ? 21.851 32.168 60.859 1.00 30.74 ? 71 LYS A N 1 ATOM 147 C CA . LYS A 1 30 ? 22.358 31.056 60.037 1.00 31.57 ? 71 LYS A CA 1 ATOM 148 C C . LYS A 1 30 ? 21.251 30.027 59.839 1.00 32.26 ? 71 LYS A C 1 ATOM 149 O O . LYS A 1 30 ? 21.023 29.571 58.703 1.00 32.49 ? 71 LYS A O 1 ATOM 150 C CB . LYS A 1 30 ? 23.560 30.405 60.761 1.00 32.78 ? 71 LYS A CB 1 ATOM 151 C CG . LYS A 1 30 ? 24.146 29.205 60.063 1.00 35.06 ? 71 LYS A CG 1 ATOM 152 C CD . LYS A 1 30 ? 25.454 28.769 60.745 1.00 36.96 ? 71 LYS A CD 1 ATOM 153 C CE . LYS A 1 30 ? 25.939 27.498 60.123 1.00 41.32 ? 71 LYS A CE 1 ATOM 154 N NZ . LYS A 1 30 ? 27.136 26.960 60.870 1.00 42.49 ? 71 LYS A NZ 1 ATOM 155 N N . LYS A 1 31 ? 20.567 29.645 60.929 1.00 32.34 ? 72 LYS A N 1 ATOM 156 C CA A LYS A 1 31 ? 19.438 28.699 60.882 0.50 33.59 ? 72 LYS A CA 1 ATOM 157 C CA B LYS A 1 31 ? 19.488 28.661 60.798 0.50 33.06 ? 72 LYS A CA 1 ATOM 158 C C . LYS A 1 31 ? 18.364 29.185 59.881 1.00 31.86 ? 72 LYS A C 1 ATOM 159 O O . LYS A 1 31 ? 17.842 28.433 59.053 1.00 30.98 ? 72 LYS A O 1 ATOM 160 C CB A LYS A 1 31 ? 18.811 28.588 62.281 0.50 34.64 ? 72 LYS A CB 1 ATOM 161 C CB B LYS A 1 31 ? 18.929 28.246 62.155 0.50 33.89 ? 72 LYS A CB 1 ATOM 162 C CG A LYS A 1 31 ? 17.605 27.674 62.393 0.50 38.31 ? 72 LYS A CG 1 ATOM 163 C CG B LYS A 1 31 ? 19.886 27.407 62.949 0.50 36.04 ? 72 LYS A CG 1 ATOM 164 C CD A LYS A 1 31 ? 16.825 27.899 63.707 0.50 42.80 ? 72 LYS A CD 1 ATOM 165 C CD B LYS A 1 31 ? 19.508 27.319 64.397 0.50 37.03 ? 72 LYS A CD 1 ATOM 166 C CE A LYS A 1 31 ? 17.690 27.605 64.926 0.50 45.56 ? 72 LYS A CE 1 ATOM 167 C CE B LYS A 1 31 ? 20.466 26.352 65.098 0.50 41.63 ? 72 LYS A CE 1 ATOM 168 N NZ A LYS A 1 31 ? 16.872 27.560 66.187 0.50 48.99 ? 72 LYS A NZ 1 ATOM 169 N NZ B LYS A 1 31 ? 20.556 26.669 66.531 0.50 43.81 ? 72 LYS A NZ 1 ATOM 170 N N . PHE A 1 32 ? 18.028 30.459 59.981 1.00 30.24 ? 73 PHE A N 1 ATOM 171 C CA . PHE A 1 32 ? 16.990 31.010 59.126 1.00 29.47 ? 73 PHE A CA 1 ATOM 172 C C . PHE A 1 32 ? 17.409 31.070 57.643 1.00 29.30 ? 73 PHE A C 1 ATOM 173 O O . PHE A 1 32 ? 16.604 30.764 56.734 1.00 27.64 ? 73 PHE A O 1 ATOM 174 C CB . PHE A 1 32 ? 16.565 32.433 59.618 1.00 28.45 ? 73 PHE A CB 1 ATOM 175 C CG . PHE A 1 32 ? 15.989 32.450 61.011 1.00 29.43 ? 73 PHE A CG 1 ATOM 176 C CD1 . PHE A 1 32 ? 15.274 31.341 61.513 1.00 31.07 ? 73 PHE A CD1 1 ATOM 177 C CD2 . PHE A 1 32 ? 16.102 33.608 61.807 1.00 29.96 ? 73 PHE A CD2 1 ATOM 178 C CE1 . PHE A 1 32 ? 14.732 31.363 62.804 1.00 35.28 ? 73 PHE A CE1 1 ATOM 179 C CE2 . PHE A 1 32 ? 15.562 33.646 63.087 1.00 29.51 ? 73 PHE A CE2 1 ATOM 180 C CZ . PHE A 1 32 ? 14.865 32.532 63.587 1.00 33.29 ? 73 PHE A CZ 1 ATOM 181 N N . LEU A 1 33 ? 18.653 31.473 57.400 1.00 27.95 ? 74 LEU A N 1 ATOM 182 C CA . LEU A 1 33 ? 19.134 31.541 56.021 1.00 29.20 ? 74 LEU A CA 1 ATOM 183 C C . LEU A 1 33 ? 19.057 30.171 55.387 1.00 28.71 ? 74 LEU A C 1 ATOM 184 O O . LEU A 1 33 ? 18.597 30.043 54.249 1.00 29.18 ? 74 LEU A O 1 ATOM 185 C CB . LEU A 1 33 ? 20.576 32.058 55.940 1.00 28.49 ? 74 LEU A CB 1 ATOM 186 C CG . LEU A 1 33 ? 21.072 32.189 54.497 1.00 28.23 ? 74 LEU A CG 1 ATOM 187 C CD1 . LEU A 1 33 ? 20.304 33.277 53.745 1.00 25.72 ? 74 LEU A CD1 1 ATOM 188 C CD2 . LEU A 1 33 ? 22.541 32.588 54.563 1.00 32.07 ? 74 LEU A CD2 1 ATOM 189 N N . TYR A 1 34 ? 19.515 29.145 56.106 1.00 29.36 ? 75 TYR A N 1 ATOM 190 C CA . TYR A 1 34 ? 19.437 27.773 55.591 1.00 30.85 ? 75 TYR A CA 1 ATOM 191 C C . TYR A 1 34 ? 17.976 27.423 55.289 1.00 31.01 ? 75 TYR A C 1 ATOM 192 O O . TYR A 1 34 ? 17.646 26.888 54.229 1.00 30.88 ? 75 TYR A O 1 ATOM 193 C CB . TYR A 1 34 ? 20.036 26.780 56.624 1.00 32.00 ? 75 TYR A CB 1 ATOM 194 C CG . TYR A 1 34 ? 19.944 25.369 56.135 1.00 32.47 ? 75 TYR A CG 1 ATOM 195 C CD1 . TYR A 1 34 ? 20.917 24.878 55.268 1.00 33.49 ? 75 TYR A CD1 1 ATOM 196 C CD2 . TYR A 1 34 ? 18.866 24.548 56.471 1.00 36.24 ? 75 TYR A CD2 1 ATOM 197 C CE1 . TYR A 1 34 ? 20.864 23.574 54.783 1.00 35.99 ? 75 TYR A CE1 1 ATOM 198 C CE2 . TYR A 1 34 ? 18.781 23.198 55.956 1.00 39.32 ? 75 TYR A CE2 1 ATOM 199 C CZ . TYR A 1 34 ? 19.803 22.747 55.122 1.00 39.34 ? 75 TYR A CZ 1 ATOM 200 O OH . TYR A 1 34 ? 19.797 21.477 54.583 1.00 43.75 ? 75 TYR A OH 1 ATOM 201 N N . ASN A 1 35 ? 17.092 27.725 56.233 1.00 30.45 ? 76 ASN A N 1 ATOM 202 C CA . ASN A 1 35 ? 15.672 27.415 56.058 1.00 30.82 ? 76 ASN A CA 1 ATOM 203 C C . ASN A 1 35 ? 15.023 28.111 54.846 1.00 30.04 ? 76 ASN A C 1 ATOM 204 O O . ASN A 1 35 ? 14.091 27.547 54.220 1.00 30.11 ? 76 ASN A O 1 ATOM 205 C CB . ASN A 1 35 ? 14.934 27.841 57.318 1.00 32.05 ? 76 ASN A CB 1 ATOM 206 C CG . ASN A 1 35 ? 13.478 27.484 57.275 1.00 33.67 ? 76 ASN A CG 1 ATOM 207 O OD1 . ASN A 1 35 ? 12.637 28.299 56.908 1.00 31.92 ? 76 ASN A OD1 1 ATOM 208 N ND2 . ASN A 1 35 ? 13.181 26.262 57.622 1.00 36.21 ? 76 ASN A ND2 1 ATOM 209 N N . PHE A 1 36 ? 15.512 29.313 54.507 1.00 27.32 ? 77 PHE A N 1 ATOM 210 C CA . PHE A 1 36 ? 14.923 30.135 53.442 1.00 26.79 ? 77 PHE A CA 1 ATOM 211 C C . PHE A 1 36 ? 15.481 29.871 52.027 1.00 28.01 ? 77 PHE A C 1 ATOM 212 O O . PHE A 1 36 ? 15.023 30.497 51.052 1.00 27.06 ? 77 PHE A O 1 ATOM 213 C CB . PHE A 1 36 ? 15.122 31.648 53.714 1.00 25.16 ? 77 PHE A CB 1 ATOM 214 C CG . PHE A 1 36 ? 14.354 32.196 54.911 1.00 27.67 ? 77 PHE A CG 1 ATOM 215 C CD1 . PHE A 1 36 ? 13.381 31.441 55.573 1.00 29.65 ? 77 PHE A CD1 1 ATOM 216 C CD2 . PHE A 1 36 ? 14.618 33.514 55.356 1.00 27.72 ? 77 PHE A CD2 1 ATOM 217 C CE1 . PHE A 1 36 ? 12.696 32.003 56.728 1.00 28.72 ? 77 PHE A CE1 1 ATOM 218 C CE2 . PHE A 1 36 ? 13.934 34.092 56.448 1.00 27.79 ? 77 PHE A CE2 1 ATOM 219 C CZ . PHE A 1 36 ? 12.963 33.334 57.124 1.00 28.58 ? 77 PHE A CZ 1 ATOM 220 N N . THR A 1 37 ? 16.474 28.984 51.897 1.00 27.01 ? 78 THR A N 1 ATOM 221 C CA . THR A 1 37 ? 17.206 28.908 50.642 1.00 27.68 ? 78 THR A CA 1 ATOM 222 C C . THR A 1 37 ? 17.290 27.497 50.079 1.00 28.74 ? 78 THR A C 1 ATOM 223 O O . THR A 1 37 ? 18.121 27.241 49.214 1.00 28.22 ? 78 THR A O 1 ATOM 224 C CB . THR A 1 37 ? 18.660 29.400 50.826 1.00 26.55 ? 78 THR A CB 1 ATOM 225 O OG1 . THR A 1 37 ? 19.254 28.704 51.933 1.00 27.68 ? 78 THR A OG1 1 ATOM 226 C CG2 . THR A 1 37 ? 18.660 30.966 51.112 1.00 25.65 ? 78 THR A CG2 1 ATOM 227 N N . GLN A 1 38 ? 16.449 26.586 50.552 1.00 29.39 ? 79 GLN A N 1 ATOM 228 C CA . GLN A 1 38 ? 16.591 25.175 50.099 1.00 32.30 ? 79 GLN A CA 1 ATOM 229 C C . GLN A 1 38 ? 15.857 24.930 48.775 1.00 32.86 ? 79 GLN A C 1 ATOM 230 O O . GLN A 1 38 ? 16.114 23.950 48.096 1.00 33.42 ? 79 GLN A O 1 ATOM 231 C CB . GLN A 1 38 ? 16.060 24.199 51.176 1.00 33.68 ? 79 GLN A CB 1 ATOM 232 C CG . GLN A 1 38 ? 16.879 24.255 52.475 1.00 36.69 ? 79 GLN A CG 1 ATOM 233 C CD . GLN A 1 38 ? 18.363 24.179 52.140 1.00 41.74 ? 79 GLN A CD 1 ATOM 234 O OE1 . GLN A 1 38 ? 18.808 23.130 51.678 1.00 45.74 ? 79 GLN A OE1 1 ATOM 235 N NE2 . GLN A 1 38 ? 19.115 25.309 52.265 1.00 38.86 ? 79 GLN A NE2 1 ATOM 236 N N . ILE A 1 39 ? 14.895 25.794 48.454 1.00 32.23 ? 80 ILE A N 1 ATOM 237 C CA . ILE A 1 39 ? 14.120 25.646 47.211 1.00 32.83 ? 80 ILE A CA 1 ATOM 238 C C . ILE A 1 39 ? 13.901 27.048 46.625 1.00 30.33 ? 80 ILE A C 1 ATOM 239 O O . ILE A 1 39 ? 14.009 28.051 47.366 1.00 30.79 ? 80 ILE A O 1 ATOM 240 C CB . ILE A 1 39 ? 12.722 24.983 47.467 1.00 34.19 ? 80 ILE A CB 1 ATOM 241 C CG1 . ILE A 1 39 ? 11.844 25.889 48.322 1.00 35.09 ? 80 ILE A CG1 1 ATOM 242 C CG2 . ILE A 1 39 ? 12.847 23.525 48.011 1.00 36.74 ? 80 ILE A CG2 1 ATOM 243 C CD1 . ILE A 1 39 ? 10.429 25.377 48.468 1.00 39.18 ? 80 ILE A CD1 1 ATOM 244 N N . PRO A 1 40 ? 13.556 27.139 45.327 1.00 29.87 ? 81 PRO A N 1 ATOM 245 C CA . PRO A 1 40 ? 13.411 28.494 44.781 1.00 28.57 ? 81 PRO A CA 1 ATOM 246 C C . PRO A 1 40 ? 12.158 29.150 45.315 1.00 27.62 ? 81 PRO A C 1 ATOM 247 O O . PRO A 1 40 ? 11.158 28.455 45.598 1.00 28.67 ? 81 PRO A O 1 ATOM 248 C CB . PRO A 1 40 ? 13.318 28.260 43.266 1.00 29.44 ? 81 PRO A CB 1 ATOM 249 C CG . PRO A 1 40 ? 13.959 26.886 43.066 1.00 31.60 ? 81 PRO A CG 1 ATOM 250 C CD . PRO A 1 40 ? 13.542 26.106 44.268 1.00 31.04 ? 81 PRO A CD 1 ATOM 251 N N . HIS A 1 41 ? 12.180 30.469 45.417 1.00 26.24 ? 82 HIS A N 1 ATOM 252 C CA . HIS A 1 41 ? 10.978 31.204 45.885 1.00 26.98 ? 82 HIS A CA 1 ATOM 253 C C . HIS A 1 41 ? 10.610 32.313 44.883 1.00 25.72 ? 82 HIS A C 1 ATOM 254 O O . HIS A 1 41 ? 10.555 33.477 45.230 1.00 25.17 ? 82 HIS A O 1 ATOM 255 C CB . HIS A 1 41 ? 11.264 31.781 47.281 1.00 27.00 ? 82 HIS A CB 1 ATOM 256 C CG . HIS A 1 41 ? 11.399 30.716 48.325 1.00 28.65 ? 82 HIS A CG 1 ATOM 257 N ND1 . HIS A 1 41 ? 12.620 30.372 48.862 1.00 28.42 ? 82 HIS A ND1 1 ATOM 258 C CD2 . HIS A 1 41 ? 10.485 29.866 48.866 1.00 26.16 ? 82 HIS A CD2 1 ATOM 259 C CE1 . HIS A 1 41 ? 12.448 29.364 49.710 1.00 29.27 ? 82 HIS A CE1 1 ATOM 260 N NE2 . HIS A 1 41 ? 11.163 29.034 49.728 1.00 27.39 ? 82 HIS A NE2 1 ATOM 261 N N . LEU A 1 42 ? 10.464 31.944 43.614 1.00 25.69 ? 83 LEU A N 1 ATOM 262 C CA . LEU A 1 42 ? 10.160 32.898 42.566 1.00 25.38 ? 83 LEU A CA 1 ATOM 263 C C . LEU A 1 42 ? 8.794 33.557 42.768 1.00 24.74 ? 83 LEU A C 1 ATOM 264 O O . LEU A 1 42 ? 7.799 32.891 43.127 1.00 25.53 ? 83 LEU A O 1 ATOM 265 C CB . LEU A 1 42 ? 10.230 32.179 41.170 1.00 25.57 ? 83 LEU A CB 1 ATOM 266 C CG . LEU A 1 42 ? 10.018 33.083 39.938 1.00 26.90 ? 83 LEU A CG 1 ATOM 267 C CD1 . LEU A 1 42 ? 11.171 34.086 39.752 1.00 22.93 ? 83 LEU A CD1 1 ATOM 268 C CD2 . LEU A 1 42 ? 9.966 32.053 38.636 1.00 23.42 ? 83 LEU A CD2 1 ATOM 269 N N . ALA A 1 43 ? 8.724 34.875 42.552 1.00 23.48 ? 84 ALA A N 1 ATOM 270 C CA . ALA A 1 43 ? 7.427 35.565 42.729 1.00 24.23 ? 84 ALA A CA 1 ATOM 271 C C . ALA A 1 43 ? 6.308 34.905 41.941 1.00 25.99 ? 84 ALA A C 1 ATOM 272 O O . ALA A 1 43 ? 6.496 34.528 40.771 1.00 26.03 ? 84 ALA A O 1 ATOM 273 C CB . ALA A 1 43 ? 7.499 37.016 42.309 1.00 23.93 ? 84 ALA A CB 1 ATOM 274 N N . GLY A 1 44 ? 5.150 34.766 42.577 1.00 26.36 ? 85 GLY A N 1 ATOM 275 C CA . GLY A 1 44 ? 3.973 34.215 41.886 1.00 28.31 ? 85 GLY A CA 1 ATOM 276 C C . GLY A 1 44 ? 3.873 32.712 41.886 1.00 30.02 ? 85 GLY A C 1 ATOM 277 O O . GLY A 1 44 ? 2.873 32.156 41.423 1.00 32.49 ? 85 GLY A O 1 ATOM 278 N N . THR A 1 45 ? 4.860 32.036 42.445 1.00 29.09 ? 86 THR A N 1 ATOM 279 C CA . THR A 1 45 ? 4.839 30.593 42.505 1.00 29.16 ? 86 THR A CA 1 ATOM 280 C C . THR A 1 45 ? 4.274 30.052 43.820 1.00 29.18 ? 86 THR A C 1 ATOM 281 O O . THR A 1 45 ? 4.322 30.731 44.844 1.00 27.98 ? 86 THR A O 1 ATOM 282 C CB . THR A 1 45 ? 6.251 29.958 42.274 1.00 29.30 ? 86 THR A CB 1 ATOM 283 O OG1 . THR A 1 45 ? 7.132 30.277 43.378 1.00 29.24 ? 86 THR A OG1 1 ATOM 284 C CG2 . THR A 1 45 ? 6.868 30.411 40.969 1.00 29.91 ? 86 THR A CG2 1 ATOM 285 N N . GLU A 1 46 ? 3.815 28.794 43.802 1.00 29.66 ? 87 GLU A N 1 ATOM 286 C CA . GLU A 1 46 ? 3.336 28.150 45.032 1.00 32.48 ? 87 GLU A CA 1 ATOM 287 C C . GLU A 1 46 ? 4.374 28.102 46.204 1.00 31.15 ? 87 GLU A C 1 ATOM 288 O O . GLU A 1 46 ? 4.004 28.317 47.378 1.00 31.34 ? 87 GLU A O 1 ATOM 289 C CB . GLU A 1 46 ? 2.819 26.717 44.735 1.00 34.88 ? 87 GLU A CB 1 ATOM 290 C CG . GLU A 1 46 ? 2.313 25.990 46.008 1.00 43.52 ? 87 GLU A CG 1 ATOM 291 C CD . GLU A 1 46 ? 0.993 26.553 46.578 1.00 53.25 ? 87 GLU A CD 1 ATOM 292 O OE1 . GLU A 1 46 ? 0.627 26.183 47.738 1.00 57.44 ? 87 GLU A OE1 1 ATOM 293 O OE2 . GLU A 1 46 ? 0.301 27.351 45.880 1.00 55.89 ? 87 GLU A OE2 1 ATOM 294 N N A GLN A 1 47 ? 5.632 27.819 45.877 0.70 30.89 ? 88 GLN A N 1 ATOM 295 N N B GLN A 1 47 ? 5.634 27.821 45.874 0.30 30.68 ? 88 GLN A N 1 ATOM 296 C CA A GLN A 1 47 ? 6.721 27.802 46.861 0.70 31.53 ? 88 GLN A CA 1 ATOM 297 C CA B GLN A 1 47 ? 6.709 27.759 46.870 0.30 30.41 ? 88 GLN A CA 1 ATOM 298 C C A GLN A 1 47 ? 6.827 29.116 47.631 0.70 29.36 ? 88 GLN A C 1 ATOM 299 C C B GLN A 1 47 ? 6.928 29.097 47.596 0.30 29.30 ? 88 GLN A C 1 ATOM 300 O O A GLN A 1 47 ? 7.066 29.157 48.840 0.70 27.71 ? 88 GLN A O 1 ATOM 301 O O B GLN A 1 47 ? 7.314 29.125 48.767 0.30 28.65 ? 88 GLN A O 1 ATOM 302 C CB A GLN A 1 47 ? 8.056 27.513 46.168 0.70 31.44 ? 88 GLN A CB 1 ATOM 303 C CB B GLN A 1 47 ? 8.015 27.243 46.238 0.30 30.26 ? 88 GLN A CB 1 ATOM 304 C CG A GLN A 1 47 ? 8.122 26.133 45.509 0.70 36.36 ? 88 GLN A CG 1 ATOM 305 C CG B GLN A 1 47 ? 8.027 25.724 45.937 0.30 30.68 ? 88 GLN A CG 1 ATOM 306 C CD A GLN A 1 47 ? 7.725 26.129 44.020 0.70 39.89 ? 88 GLN A CD 1 ATOM 307 C CD B GLN A 1 47 ? 9.207 25.292 45.045 0.30 28.75 ? 88 GLN A CD 1 ATOM 308 O OE1 A GLN A 1 47 ? 6.767 26.789 43.586 0.70 34.88 ? 88 GLN A OE1 1 ATOM 309 O OE1 B GLN A 1 47 ? 9.634 24.127 45.060 0.30 31.36 ? 88 GLN A OE1 1 ATOM 310 N NE2 A GLN A 1 47 ? 8.467 25.348 43.235 0.70 44.12 ? 88 GLN A NE2 1 ATOM 311 N NE2 B GLN A 1 47 ? 9.713 26.219 44.247 0.30 23.78 ? 88 GLN A NE2 1 ATOM 312 N N . ASN A 1 48 ? 6.678 30.207 46.909 1.00 28.62 ? 89 ASN A N 1 ATOM 313 C CA . ASN A 1 48 ? 6.856 31.507 47.546 1.00 28.56 ? 89 ASN A CA 1 ATOM 314 C C . ASN A 1 48 ? 5.630 31.837 48.431 1.00 29.80 ? 89 ASN A C 1 ATOM 315 O O . ASN A 1 48 ? 5.759 32.473 49.493 1.00 27.91 ? 89 ASN A O 1 ATOM 316 C CB . ASN A 1 48 ? 7.106 32.588 46.512 1.00 28.54 ? 89 ASN A CB 1 ATOM 317 C CG . ASN A 1 48 ? 7.665 33.873 47.159 1.00 33.99 ? 89 ASN A CG 1 ATOM 318 O OD1 . ASN A 1 48 ? 8.376 33.817 48.203 1.00 34.65 ? 89 ASN A OD1 1 ATOM 319 N ND2 . ASN A 1 48 ? 7.403 34.989 46.548 1.00 31.26 ? 89 ASN A ND2 1 ATOM 320 N N . PHE A 1 49 ? 4.450 31.402 47.997 1.00 28.93 ? 90 PHE A N 1 ATOM 321 C CA . PHE A 1 49 ? 3.244 31.496 48.850 1.00 29.64 ? 90 PHE A CA 1 ATOM 322 C C . PHE A 1 49 ? 3.398 30.663 50.125 1.00 30.19 ? 90 PHE A C 1 ATOM 323 O O . PHE A 1 49 ? 3.103 31.155 51.220 1.00 28.71 ? 90 PHE A O 1 ATOM 324 C CB . PHE A 1 49 ? 1.975 31.118 48.058 1.00 30.66 ? 90 PHE A CB 1 ATOM 325 C CG . PHE A 1 49 ? 0.713 31.014 48.887 1.00 31.66 ? 90 PHE A CG 1 ATOM 326 C CD1 . PHE A 1 49 ? 0.193 32.111 49.570 1.00 32.42 ? 90 PHE A CD1 1 ATOM 327 C CD2 . PHE A 1 49 ? 0.026 29.797 48.962 1.00 39.44 ? 90 PHE A CD2 1 ATOM 328 C CE1 . PHE A 1 49 ? -1.012 32.011 50.303 1.00 34.32 ? 90 PHE A CE1 1 ATOM 329 C CE2 . PHE A 1 49 ? -1.185 29.674 49.710 1.00 42.75 ? 90 PHE A CE2 1 ATOM 330 C CZ . PHE A 1 49 ? -1.689 30.782 50.389 1.00 39.05 ? 90 PHE A CZ 1 ATOM 331 N N A GLN A 1 50 ? 3.885 29.423 50.009 0.60 29.85 ? 91 GLN A N 1 ATOM 332 N N B GLN A 1 50 ? 3.900 29.430 49.984 0.40 29.77 ? 91 GLN A N 1 ATOM 333 C CA A GLN A 1 50 ? 4.133 28.641 51.220 0.60 31.44 ? 91 GLN A CA 1 ATOM 334 C CA B GLN A 1 50 ? 4.199 28.574 51.138 0.40 30.90 ? 91 GLN A CA 1 ATOM 335 C C A GLN A 1 50 ? 5.117 29.313 52.165 0.60 30.63 ? 91 GLN A C 1 ATOM 336 C C B GLN A 1 50 ? 5.178 29.197 52.133 0.40 30.29 ? 91 GLN A C 1 ATOM 337 O O A GLN A 1 50 ? 4.879 29.341 53.374 0.60 29.61 ? 91 GLN A O 1 ATOM 338 O O B GLN A 1 50 ? 4.997 29.068 53.341 0.40 29.86 ? 91 GLN A O 1 ATOM 339 C CB A GLN A 1 50 ? 4.592 27.209 50.892 0.60 32.66 ? 91 GLN A CB 1 ATOM 340 C CB B GLN A 1 50 ? 4.711 27.199 50.677 0.40 31.53 ? 91 GLN A CB 1 ATOM 341 C CG A GLN A 1 50 ? 3.481 26.377 50.230 0.60 37.41 ? 91 GLN A CG 1 ATOM 342 C CG B GLN A 1 50 ? 3.579 26.314 50.153 0.40 34.35 ? 91 GLN A CG 1 ATOM 343 C CD A GLN A 1 50 ? 2.205 26.262 51.061 0.60 43.52 ? 91 GLN A CD 1 ATOM 344 C CD B GLN A 1 50 ? 4.070 25.110 49.361 0.40 35.86 ? 91 GLN A CD 1 ATOM 345 O OE1 A GLN A 1 50 ? 2.237 26.191 52.301 0.60 47.47 ? 91 GLN A OE1 1 ATOM 346 O OE1 B GLN A 1 50 ? 5.249 24.998 49.040 0.40 37.94 ? 91 GLN A OE1 1 ATOM 347 N NE2 A GLN A 1 50 ? 1.068 26.215 50.374 0.60 44.61 ? 91 GLN A NE2 1 ATOM 348 N NE2 B GLN A 1 50 ? 3.152 24.212 49.028 0.40 39.17 ? 91 GLN A NE2 1 ATOM 349 N N . LEU A 1 51 ? 6.205 29.879 51.627 1.00 28.76 ? 92 LEU A N 1 ATOM 350 C CA . LEU A 1 51 ? 7.148 30.594 52.518 1.00 28.92 ? 92 LEU A CA 1 ATOM 351 C C . LEU A 1 51 ? 6.445 31.787 53.196 1.00 27.79 ? 92 LEU A C 1 ATOM 352 O O . LEU A 1 51 ? 6.660 32.037 54.404 1.00 27.51 ? 92 LEU A O 1 ATOM 353 C CB . LEU A 1 51 ? 8.390 31.111 51.761 1.00 26.54 ? 92 LEU A CB 1 ATOM 354 C CG . LEU A 1 51 ? 9.508 31.715 52.608 1.00 28.92 ? 92 LEU A CG 1 ATOM 355 C CD1 . LEU A 1 51 ? 9.985 30.732 53.714 1.00 29.09 ? 92 LEU A CD1 1 ATOM 356 C CD2 . LEU A 1 51 ? 10.680 32.149 51.707 1.00 26.60 ? 92 LEU A CD2 1 ATOM 357 N N . ALA A 1 52 ? 5.615 32.527 52.440 1.00 27.03 ? 93 ALA A N 1 ATOM 358 C CA . ALA A 1 52 ? 4.857 33.650 53.045 1.00 27.47 ? 93 ALA A CA 1 ATOM 359 C C . ALA A 1 52 ? 4.034 33.159 54.218 1.00 28.16 ? 93 ALA A C 1 ATOM 360 O O . ALA A 1 52 ? 3.983 33.803 55.263 1.00 27.64 ? 93 ALA A O 1 ATOM 361 C CB . ALA A 1 52 ? 3.934 34.358 52.038 1.00 26.27 ? 93 ALA A CB 1 ATOM 362 N N . LYS A 1 53 ? 3.373 32.023 54.049 1.00 28.57 ? 94 LYS A N 1 ATOM 363 C CA A LYS A 1 53 ? 2.542 31.467 55.122 0.50 29.40 ? 94 LYS A CA 1 ATOM 364 C CA B LYS A 1 53 ? 2.539 31.490 55.126 0.50 29.51 ? 94 LYS A CA 1 ATOM 365 C C . LYS A 1 53 ? 3.375 31.055 56.338 1.00 30.23 ? 94 LYS A C 1 ATOM 366 O O . LYS A 1 53 ? 2.944 31.229 57.507 1.00 29.93 ? 94 LYS A O 1 ATOM 367 C CB A LYS A 1 53 ? 1.768 30.262 54.585 0.50 29.89 ? 94 LYS A CB 1 ATOM 368 C CB B LYS A 1 53 ? 1.701 30.325 54.595 0.50 30.23 ? 94 LYS A CB 1 ATOM 369 C CG A LYS A 1 53 ? 0.634 30.678 53.664 0.50 32.33 ? 94 LYS A CG 1 ATOM 370 C CG B LYS A 1 53 ? 0.548 30.795 53.695 0.50 32.92 ? 94 LYS A CG 1 ATOM 371 C CD A LYS A 1 53 ? -0.342 31.590 54.401 0.50 34.16 ? 94 LYS A CD 1 ATOM 372 C CD B LYS A 1 53 ? -0.505 29.698 53.534 0.50 37.47 ? 94 LYS A CD 1 ATOM 373 C CE A LYS A 1 53 ? -1.247 30.835 55.368 0.50 36.18 ? 94 LYS A CE 1 ATOM 374 C CE B LYS A 1 53 ? -0.041 28.651 52.546 0.50 39.31 ? 94 LYS A CE 1 ATOM 375 N NZ A LYS A 1 53 ? -2.497 31.626 55.685 0.50 37.17 ? 94 LYS A NZ 1 ATOM 376 N NZ B LYS A 1 53 ? -0.826 27.377 52.636 0.50 41.36 ? 94 LYS A NZ 1 ATOM 377 N N . GLN A 1 54 ? 4.559 30.480 56.067 1.00 29.55 ? 95 GLN A N 1 ATOM 378 C CA . GLN A 1 54 ? 5.489 30.093 57.148 1.00 30.66 ? 95 GLN A CA 1 ATOM 379 C C . GLN A 1 54 ? 5.928 31.323 57.917 1.00 29.79 ? 95 GLN A C 1 ATOM 380 O O . GLN A 1 54 ? 5.915 31.334 59.142 1.00 30.48 ? 95 GLN A O 1 ATOM 381 C CB . GLN A 1 54 ? 6.731 29.411 56.570 1.00 30.43 ? 95 GLN A CB 1 ATOM 382 C CG . GLN A 1 54 ? 7.739 29.100 57.669 1.00 33.27 ? 95 GLN A CG 1 ATOM 383 C CD . GLN A 1 54 ? 9.077 28.731 57.099 1.00 33.88 ? 95 GLN A CD 1 ATOM 384 O OE1 . GLN A 1 54 ? 9.148 28.019 56.084 1.00 32.16 ? 95 GLN A OE1 1 ATOM 385 N NE2 . GLN A 1 54 ? 10.147 29.224 57.715 1.00 34.23 ? 95 GLN A NE2 1 ATOM 386 N N . ILE A 1 55 ? 6.300 32.374 57.195 1.00 27.15 ? 96 ILE A N 1 ATOM 387 C CA . ILE A 1 55 ? 6.774 33.571 57.867 1.00 28.77 ? 96 ILE A CA 1 ATOM 388 C C . ILE A 1 55 ? 5.637 34.206 58.693 1.00 28.81 ? 96 ILE A C 1 ATOM 389 O O . ILE A 1 55 ? 5.837 34.637 59.854 1.00 28.63 ? 96 ILE A O 1 ATOM 390 C CB . ILE A 1 55 ? 7.301 34.636 56.846 1.00 28.17 ? 96 ILE A CB 1 ATOM 391 C CG1 A ILE A 1 55 ? 8.497 34.162 56.001 0.65 30.12 ? 96 ILE A CG1 1 ATOM 392 C CG1 B ILE A 1 55 ? 8.633 34.128 56.270 0.35 27.35 ? 96 ILE A CG1 1 ATOM 393 C CG2 . ILE A 1 55 ? 7.586 35.972 57.562 1.00 29.28 ? 96 ILE A CG2 1 ATOM 394 C CD1 A ILE A 1 55 ? 9.681 33.835 56.760 0.65 33.01 ? 96 ILE A CD1 1 ATOM 395 C CD1 B ILE A 1 55 ? 9.110 34.813 55.025 0.35 22.32 ? 96 ILE A CD1 1 ATOM 396 N N . GLN A 1 56 ? 4.452 34.283 58.104 1.00 28.06 ? 97 GLN A N 1 ATOM 397 C CA . GLN A 1 56 ? 3.322 34.769 58.894 1.00 29.02 ? 97 GLN A CA 1 ATOM 398 C C . GLN A 1 56 ? 3.134 33.970 60.189 1.00 30.02 ? 97 GLN A C 1 ATOM 399 O O . GLN A 1 56 ? 2.981 34.576 61.276 1.00 30.80 ? 97 GLN A O 1 ATOM 400 C CB . GLN A 1 56 ? 2.049 34.730 58.053 1.00 28.89 ? 97 GLN A CB 1 ATOM 401 C CG . GLN A 1 56 ? 0.767 35.023 58.843 1.00 32.30 ? 97 GLN A CG 1 ATOM 402 C CD . GLN A 1 56 ? -0.493 34.819 57.989 1.00 35.44 ? 97 GLN A CD 1 ATOM 403 O OE1 . GLN A 1 56 ? -0.543 33.928 57.120 1.00 35.76 ? 97 GLN A OE1 1 ATOM 404 N NE2 . GLN A 1 56 ? -1.509 35.629 58.246 1.00 34.11 ? 97 GLN A NE2 1 ATOM 405 N N . SER A 1 57 ? 3.119 32.640 60.107 1.00 30.15 ? 98 SER A N 1 ATOM 406 C CA . SER A 1 57 ? 2.985 31.806 61.324 1.00 32.71 ? 98 SER A CA 1 ATOM 407 C C . SER A 1 57 ? 4.079 32.075 62.368 1.00 32.19 ? 98 SER A C 1 ATOM 408 O O . SER A 1 57 ? 3.806 32.203 63.569 1.00 31.50 ? 98 SER A O 1 ATOM 409 C CB . SER A 1 57 ? 3.027 30.319 60.947 1.00 33.52 ? 98 SER A CB 1 ATOM 410 O OG A SER A 1 57 ? 2.820 29.507 62.081 0.50 36.13 ? 98 SER A OG 1 ATOM 411 O OG B SER A 1 57 ? 1.818 29.960 60.317 0.50 35.90 ? 98 SER A OG 1 ATOM 412 N N . GLN A 1 58 ? 5.326 32.117 61.903 1.00 31.66 ? 99 GLN A N 1 ATOM 413 C CA . GLN A 1 58 ? 6.458 32.343 62.798 1.00 32.16 ? 99 GLN A CA 1 ATOM 414 C C . GLN A 1 58 ? 6.435 33.729 63.421 1.00 32.30 ? 99 GLN A C 1 ATOM 415 O O . GLN A 1 58 ? 6.748 33.866 64.599 1.00 32.99 ? 99 GLN A O 1 ATOM 416 C CB . GLN A 1 58 ? 7.780 32.125 62.059 1.00 31.69 ? 99 GLN A CB 1 ATOM 417 C CG . GLN A 1 58 ? 7.936 30.643 61.729 1.00 35.90 ? 99 GLN A CG 1 ATOM 418 C CD . GLN A 1 58 ? 9.310 30.330 61.190 1.00 38.28 ? 99 GLN A CD 1 ATOM 419 O OE1 . GLN A 1 58 ? 9.695 30.837 60.168 1.00 35.60 ? 99 GLN A OE1 1 ATOM 420 N NE2 . GLN A 1 58 ? 10.036 29.481 61.885 1.00 41.61 ? 99 GLN A NE2 1 ATOM 421 N N . TRP A 1 59 ? 6.137 34.772 62.636 1.00 29.84 ? 100 TRP A N 1 ATOM 422 C CA . TRP A 1 59 ? 6.054 36.103 63.230 1.00 30.21 ? 100 TRP A CA 1 ATOM 423 C C . TRP A 1 59 ? 4.974 36.198 64.332 1.00 30.37 ? 100 TRP A C 1 ATOM 424 O O . TRP A 1 59 ? 5.157 36.915 65.336 1.00 31.75 ? 100 TRP A O 1 ATOM 425 C CB . TRP A 1 59 ? 5.805 37.170 62.155 1.00 28.10 ? 100 TRP A CB 1 ATOM 426 C CG . TRP A 1 59 ? 7.033 37.488 61.362 1.00 26.33 ? 100 TRP A CG 1 ATOM 427 C CD1 . TRP A 1 59 ? 8.249 36.827 61.394 1.00 27.14 ? 100 TRP A CD1 1 ATOM 428 C CD2 . TRP A 1 59 ? 7.148 38.480 60.333 1.00 25.48 ? 100 TRP A CD2 1 ATOM 429 N NE1 . TRP A 1 59 ? 9.110 37.380 60.476 1.00 27.80 ? 100 TRP A NE1 1 ATOM 430 C CE2 . TRP A 1 59 ? 8.473 38.390 59.810 1.00 25.56 ? 100 TRP A CE2 1 ATOM 431 C CE3 . TRP A 1 59 ? 6.266 39.437 59.809 1.00 26.30 ? 100 TRP A CE3 1 ATOM 432 C CZ2 . TRP A 1 59 ? 8.949 39.215 58.773 1.00 23.70 ? 100 TRP A CZ2 1 ATOM 433 C CZ3 . TRP A 1 59 ? 6.729 40.274 58.753 1.00 24.70 ? 100 TRP A CZ3 1 ATOM 434 C CH2 . TRP A 1 59 ? 8.066 40.172 58.265 1.00 25.97 ? 100 TRP A CH2 1 ATOM 435 N N . LYS A 1 60 ? 3.862 35.475 64.150 1.00 31.96 ? 101 LYS A N 1 ATOM 436 C CA . LYS A 1 60 ? 2.839 35.357 65.224 1.00 35.50 ? 101 LYS A CA 1 ATOM 437 C C . LYS A 1 60 ? 3.430 34.685 66.453 1.00 36.78 ? 101 LYS A C 1 ATOM 438 O O . LYS A 1 60 ? 3.292 35.206 67.562 1.00 37.92 ? 101 LYS A O 1 ATOM 439 C CB . LYS A 1 60 ? 1.619 34.558 64.758 1.00 36.38 ? 101 LYS A CB 1 ATOM 440 C CG . LYS A 1 60 ? 0.799 35.311 63.756 1.00 40.84 ? 101 LYS A CG 1 ATOM 441 C CD . LYS A 1 60 ? -0.345 34.460 63.186 1.00 50.80 ? 101 LYS A CD 1 ATOM 442 C CE . LYS A 1 60 ? -1.431 35.407 62.601 1.00 53.17 ? 101 LYS A CE 1 ATOM 443 N NZ . LYS A 1 60 ? -2.240 34.717 61.560 1.00 57.44 ? 101 LYS A NZ 1 ATOM 444 N N A GLU A 1 61 ? 4.091 33.543 66.278 0.40 36.60 ? 102 GLU A N 1 ATOM 445 N N B GLU A 1 61 ? 4.078 33.538 66.231 0.60 36.67 ? 102 GLU A N 1 ATOM 446 C CA A GLU A 1 61 ? 4.657 32.832 67.427 0.40 37.64 ? 102 GLU A CA 1 ATOM 447 C CA B GLU A 1 61 ? 4.726 32.759 67.284 0.60 38.09 ? 102 GLU A CA 1 ATOM 448 C C A GLU A 1 61 ? 5.830 33.596 68.059 0.40 37.25 ? 102 GLU A C 1 ATOM 449 C C B GLU A 1 61 ? 5.729 33.659 68.035 0.60 37.57 ? 102 GLU A C 1 ATOM 450 O O A GLU A 1 61 ? 6.083 33.461 69.261 0.40 37.54 ? 102 GLU A O 1 ATOM 451 O O B GLU A 1 61 ? 5.758 33.680 69.285 0.60 37.38 ? 102 GLU A O 1 ATOM 452 C CB A GLU A 1 61 ? 5.048 31.395 67.064 0.40 38.19 ? 102 GLU A CB 1 ATOM 453 C CB B GLU A 1 61 ? 5.454 31.535 66.687 0.60 38.47 ? 102 GLU A CB 1 ATOM 454 C CG A GLU A 1 61 ? 6.062 30.731 68.008 0.40 40.77 ? 102 GLU A CG 1 ATOM 455 C CG B GLU A 1 61 ? 4.571 30.420 66.059 0.60 42.20 ? 102 GLU A CG 1 ATOM 456 C CD A GLU A 1 61 ? 5.532 30.464 69.413 0.40 45.32 ? 102 GLU A CD 1 ATOM 457 C CD B GLU A 1 61 ? 5.350 29.427 65.147 0.60 46.94 ? 102 GLU A CD 1 ATOM 458 O OE1 A GLU A 1 61 ? 4.304 30.299 69.595 0.40 48.12 ? 102 GLU A OE1 1 ATOM 459 O OE1 B GLU A 1 61 ? 6.576 29.209 65.356 0.60 46.68 ? 102 GLU A OE1 1 ATOM 460 O OE2 A GLU A 1 61 ? 6.356 30.402 70.349 0.40 47.33 ? 102 GLU A OE2 1 ATOM 461 O OE2 B GLU A 1 61 ? 4.733 28.870 64.199 0.60 47.60 ? 102 GLU A OE2 1 ATOM 462 N N . PHE A 1 62 ? 6.509 34.431 67.270 1.00 35.15 ? 103 PHE A N 1 ATOM 463 C CA . PHE A 1 62 ? 7.557 35.324 67.832 1.00 35.47 ? 103 PHE A CA 1 ATOM 464 C C . PHE A 1 62 ? 6.984 36.421 68.739 1.00 35.21 ? 103 PHE A C 1 ATOM 465 O O . PHE A 1 62 ? 7.715 37.010 69.546 1.00 36.44 ? 103 PHE A O 1 ATOM 466 C CB . PHE A 1 62 ? 8.378 36.044 66.723 1.00 33.52 ? 103 PHE A CB 1 ATOM 467 C CG . PHE A 1 62 ? 9.309 35.124 65.931 1.00 33.33 ? 103 PHE A CG 1 ATOM 468 C CD1 . PHE A 1 62 ? 9.648 33.842 66.404 1.00 36.75 ? 103 PHE A CD1 1 ATOM 469 C CD2 . PHE A 1 62 ? 9.839 35.552 64.719 1.00 34.02 ? 103 PHE A CD2 1 ATOM 470 C CE1 . PHE A 1 62 ? 10.516 32.988 65.650 1.00 38.14 ? 103 PHE A CE1 1 ATOM 471 C CE2 . PHE A 1 62 ? 10.709 34.709 63.968 1.00 34.09 ? 103 PHE A CE2 1 ATOM 472 C CZ . PHE A 1 62 ? 11.041 33.441 64.429 1.00 36.66 ? 103 PHE A CZ 1 ATOM 473 N N . GLY A 1 63 ? 5.707 36.734 68.557 1.00 33.90 ? 104 GLY A N 1 ATOM 474 C CA . GLY A 1 63 ? 5.026 37.627 69.472 1.00 35.55 ? 104 GLY A CA 1 ATOM 475 C C . GLY A 1 63 ? 4.420 38.884 68.884 1.00 35.17 ? 104 GLY A C 1 ATOM 476 O O . GLY A 1 63 ? 3.940 39.738 69.655 1.00 36.38 ? 104 GLY A O 1 ATOM 477 N N . LEU A 1 64 ? 4.405 39.030 67.548 1.00 34.12 ? 105 LEU A N 1 ATOM 478 C CA . LEU A 1 64 ? 3.761 40.252 66.968 1.00 33.12 ? 105 LEU A CA 1 ATOM 479 C C . LEU A 1 64 ? 2.248 40.309 67.282 1.00 34.44 ? 105 LEU A C 1 ATOM 480 O O . LEU A 1 64 ? 1.607 39.265 67.497 1.00 36.35 ? 105 LEU A O 1 ATOM 481 C CB . LEU A 1 64 ? 4.019 40.370 65.451 1.00 31.77 ? 105 LEU A CB 1 ATOM 482 C CG . LEU A 1 64 ? 5.503 40.459 65.084 1.00 28.99 ? 105 LEU A CG 1 ATOM 483 C CD1 . LEU A 1 64 ? 5.654 40.812 63.592 1.00 29.28 ? 105 LEU A CD1 1 ATOM 484 C CD2 . LEU A 1 64 ? 6.233 41.532 65.957 1.00 29.89 ? 105 LEU A CD2 1 ATOM 485 N N . ASP A 1 65 ? 1.683 41.517 67.355 1.00 34.15 ? 106 ASP A N 1 ATOM 486 C CA . ASP A 1 65 ? 0.278 41.704 67.704 1.00 35.75 ? 106 ASP A CA 1 ATOM 487 C C . ASP A 1 65 ? -0.656 41.215 66.596 1.00 36.30 ? 106 ASP A C 1 ATOM 488 O O . ASP A 1 65 ? -1.713 40.653 66.862 1.00 36.84 ? 106 ASP A O 1 ATOM 489 C CB . ASP A 1 65 ? -0.001 43.192 68.010 1.00 35.59 ? 106 ASP A CB 1 ATOM 490 C CG . ASP A 1 65 ? 0.689 43.652 69.270 1.00 39.62 ? 106 ASP A CG 1 ATOM 491 O OD1 . ASP A 1 65 ? 0.436 43.007 70.308 1.00 35.98 ? 106 ASP A OD1 1 ATOM 492 O OD2 . ASP A 1 65 ? 1.503 44.603 69.242 1.00 36.20 ? 106 ASP A OD2 1 ATOM 493 N N . SER A 1 66 ? -0.259 41.432 65.350 1.00 33.30 ? 107 SER A N 1 ATOM 494 C CA . SER A 1 66 ? -1.081 41.032 64.204 1.00 33.06 ? 107 SER A CA 1 ATOM 495 C C . SER A 1 66 ? -0.118 40.734 63.058 1.00 31.92 ? 107 SER A C 1 ATOM 496 O O . SER A 1 66 ? 0.915 41.395 62.946 1.00 29.59 ? 107 SER A O 1 ATOM 497 C CB . SER A 1 66 ? -2.103 42.151 63.833 1.00 33.50 ? 107 SER A CB 1 ATOM 498 O OG A SER A 1 66 ? -1.472 43.258 63.204 0.50 30.70 ? 107 SER A OG 1 ATOM 499 O OG B SER A 1 66 ? -2.459 42.118 62.455 0.50 36.34 ? 107 SER A OG 1 ATOM 500 N N . VAL A 1 67 ? -0.423 39.717 62.258 1.00 29.96 ? 108 VAL A N 1 ATOM 501 C CA . VAL A 1 67 ? 0.431 39.426 61.120 1.00 30.42 ? 108 VAL A CA 1 ATOM 502 C C . VAL A 1 67 ? -0.545 38.974 60.016 1.00 30.82 ? 108 VAL A C 1 ATOM 503 O O . VAL A 1 67 ? -1.205 37.923 60.159 1.00 30.33 ? 108 VAL A O 1 ATOM 504 C CB . VAL A 1 67 ? 1.448 38.284 61.367 1.00 28.83 ? 108 VAL A CB 1 ATOM 505 C CG1 . VAL A 1 67 ? 2.391 38.205 60.092 1.00 28.56 ? 108 VAL A CG1 1 ATOM 506 C CG2 . VAL A 1 67 ? 2.266 38.514 62.672 1.00 31.02 ? 108 VAL A CG2 1 ATOM 507 N N . GLU A 1 68 ? -0.586 39.729 58.921 1.00 31.03 ? 109 GLU A N 1 ATOM 508 C CA . GLU A 1 68 ? -1.547 39.455 57.842 1.00 33.05 ? 109 GLU A CA 1 ATOM 509 C C . GLU A 1 68 ? -0.845 39.292 56.497 1.00 31.25 ? 109 GLU A C 1 ATOM 510 O O . GLU A 1 68 ? 0.243 39.842 56.322 1.00 30.52 ? 109 GLU A O 1 ATOM 511 C CB . GLU A 1 68 ? -2.540 40.625 57.733 1.00 34.55 ? 109 GLU A CB 1 ATOM 512 C CG . GLU A 1 68 ? -3.478 40.802 59.000 1.00 42.55 ? 109 GLU A CG 1 ATOM 513 C CD . GLU A 1 68 ? -4.371 39.570 59.304 1.00 53.47 ? 109 GLU A CD 1 ATOM 514 O OE1 . GLU A 1 68 ? -4.870 38.903 58.362 1.00 56.15 ? 109 GLU A OE1 1 ATOM 515 O OE2 . GLU A 1 68 ? -4.580 39.257 60.511 1.00 60.50 ? 109 GLU A OE2 1 ATOM 516 N N . LEU A 1 69 ? -1.466 38.586 55.549 1.00 29.75 ? 110 LEU A N 1 ATOM 517 C CA . LEU A 1 69 ? -0.985 38.637 54.147 1.00 30.37 ? 110 LEU A CA 1 ATOM 518 C C . LEU A 1 69 ? -1.771 39.708 53.384 1.00 30.69 ? 110 LEU A C 1 ATOM 519 O O . LEU A 1 69 ? -2.996 39.788 53.524 1.00 32.15 ? 110 LEU A O 1 ATOM 520 C CB . LEU A 1 69 ? -1.179 37.291 53.468 1.00 31.24 ? 110 LEU A CB 1 ATOM 521 C CG . LEU A 1 69 ? -0.515 36.083 54.097 1.00 34.47 ? 110 LEU A CG 1 ATOM 522 C CD1 . LEU A 1 69 ? -0.735 34.913 53.123 1.00 37.82 ? 110 LEU A CD1 1 ATOM 523 C CD2 . LEU A 1 69 ? 0.947 36.303 54.279 1.00 32.77 ? 110 LEU A CD2 1 ATOM 524 N N . ALA A 1 70 ? -1.081 40.590 52.683 1.00 28.29 ? 111 ALA A N 1 ATOM 525 C CA . ALA A 1 70 ? -1.767 41.548 51.826 1.00 27.46 ? 111 ALA A CA 1 ATOM 526 C C . ALA A 1 70 ? -1.460 41.062 50.408 1.00 27.94 ? 111 ALA A C 1 ATOM 527 O O . ALA A 1 70 ? -0.279 41.032 50.012 1.00 28.77 ? 111 ALA A O 1 ATOM 528 C CB . ALA A 1 70 ? -1.163 42.948 52.037 1.00 27.48 ? 111 ALA A CB 1 ATOM 529 N N . HIS A 1 71 ? -2.477 40.685 49.648 1.00 26.04 ? 112 HIS A N 1 ATOM 530 C CA . HIS A 1 71 ? -2.218 40.140 48.285 1.00 26.21 ? 112 HIS A CA 1 ATOM 531 C C . HIS A 1 71 ? -2.658 41.102 47.200 1.00 24.95 ? 112 HIS A C 1 ATOM 532 O O . HIS A 1 71 ? -3.529 41.954 47.457 1.00 24.33 ? 112 HIS A O 1 ATOM 533 C CB . HIS A 1 71 ? -2.908 38.770 48.092 1.00 26.16 ? 112 HIS A CB 1 ATOM 534 C CG . HIS A 1 71 ? -4.406 38.835 48.154 1.00 30.70 ? 112 HIS A CG 1 ATOM 535 N ND1 . HIS A 1 71 ? -5.104 38.718 49.338 1.00 35.45 ? 112 HIS A ND1 1 ATOM 536 C CD2 . HIS A 1 71 ? -5.336 39.042 47.185 1.00 34.66 ? 112 HIS A CD2 1 ATOM 537 C CE1 . HIS A 1 71 ? -6.407 38.817 49.095 1.00 37.93 ? 112 HIS A CE1 1 ATOM 538 N NE2 . HIS A 1 71 ? -6.574 39.026 47.799 1.00 36.53 ? 112 HIS A NE2 1 ATOM 539 N N . TYR A 1 72 ? -2.032 41.011 46.019 1.00 24.45 ? 113 TYR A N 1 ATOM 540 C CA . TYR A 1 72 ? -2.330 41.896 44.861 1.00 23.62 ? 113 TYR A CA 1 ATOM 541 C C . TYR A 1 72 ? -2.226 41.021 43.629 1.00 23.92 ? 113 TYR A C 1 ATOM 542 O O . TYR A 1 72 ? -1.466 40.037 43.640 1.00 24.18 ? 113 TYR A O 1 ATOM 543 C CB . TYR A 1 72 ? -1.356 43.104 44.728 1.00 22.83 ? 113 TYR A CB 1 ATOM 544 C CG . TYR A 1 72 ? -1.369 43.913 45.989 1.00 23.20 ? 113 TYR A CG 1 ATOM 545 C CD1 . TYR A 1 72 ? -2.400 44.835 46.227 1.00 24.91 ? 113 TYR A CD1 1 ATOM 546 C CD2 . TYR A 1 72 ? -0.466 43.629 47.005 1.00 24.24 ? 113 TYR A CD2 1 ATOM 547 C CE1 . TYR A 1 72 ? -2.479 45.555 47.460 1.00 25.08 ? 113 TYR A CE1 1 ATOM 548 C CE2 . TYR A 1 72 ? -0.557 44.286 48.234 1.00 24.36 ? 113 TYR A CE2 1 ATOM 549 C CZ . TYR A 1 72 ? -1.534 45.256 48.436 1.00 25.10 ? 113 TYR A CZ 1 ATOM 550 O OH . TYR A 1 72 ? -1.620 45.877 49.688 1.00 25.61 ? 113 TYR A OH 1 ATOM 551 N N . ASP A 1 73 ? -2.867 41.444 42.556 1.00 23.47 ? 114 ASP A N 1 ATOM 552 C CA . ASP A 1 73 ? -2.754 40.679 41.277 1.00 26.04 ? 114 ASP A CA 1 ATOM 553 C C . ASP A 1 73 ? -2.066 41.576 40.277 1.00 23.72 ? 114 ASP A C 1 ATOM 554 O O . ASP A 1 73 ? -2.671 42.541 39.809 1.00 24.50 ? 114 ASP A O 1 ATOM 555 C CB . ASP A 1 73 ? -4.137 40.260 40.765 1.00 27.16 ? 114 ASP A CB 1 ATOM 556 C CG . ASP A 1 73 ? -4.833 39.270 41.733 1.00 32.68 ? 114 ASP A CG 1 ATOM 557 O OD1 . ASP A 1 73 ? -4.190 38.261 42.103 1.00 30.37 ? 114 ASP A OD1 1 ATOM 558 O OD2 . ASP A 1 73 ? -5.979 39.540 42.140 1.00 35.69 ? 114 ASP A OD2 1 ATOM 559 N N . VAL A 1 74 ? -0.804 41.245 39.981 1.00 23.91 ? 115 VAL A N 1 ATOM 560 C CA . VAL A 1 74 ? 0.120 42.164 39.274 1.00 22.42 ? 115 VAL A CA 1 ATOM 561 C C . VAL A 1 74 ? 0.640 41.497 37.971 1.00 23.84 ? 115 VAL A C 1 ATOM 562 O O . VAL A 1 74 ? 0.623 40.266 37.863 1.00 25.39 ? 115 VAL A O 1 ATOM 563 C CB . VAL A 1 74 ? 1.304 42.656 40.165 1.00 22.61 ? 115 VAL A CB 1 ATOM 564 C CG1 . VAL A 1 74 ? 0.749 43.472 41.383 1.00 21.03 ? 115 VAL A CG1 1 ATOM 565 C CG2 . VAL A 1 74 ? 2.231 41.489 40.617 1.00 20.90 ? 115 VAL A CG2 1 ATOM 566 N N . LEU A 1 75 ? 1.129 42.318 37.047 1.00 22.27 ? 116 LEU A N 1 ATOM 567 C CA . LEU A 1 75 ? 1.743 41.723 35.839 1.00 22.56 ? 116 LEU A CA 1 ATOM 568 C C . LEU A 1 75 ? 3.112 41.124 36.164 1.00 22.65 ? 116 LEU A C 1 ATOM 569 O O . LEU A 1 75 ? 4.022 41.861 36.593 1.00 24.21 ? 116 LEU A O 1 ATOM 570 C CB . LEU A 1 75 ? 1.871 42.795 34.756 1.00 22.18 ? 116 LEU A CB 1 ATOM 571 C CG . LEU A 1 75 ? 2.204 42.164 33.355 1.00 25.38 ? 116 LEU A CG 1 ATOM 572 C CD1 . LEU A 1 75 ? 0.960 41.490 32.801 1.00 27.62 ? 116 LEU A CD1 1 ATOM 573 C CD2 . LEU A 1 75 ? 2.593 43.374 32.467 1.00 25.86 ? 116 LEU A CD2 1 ATOM 574 N N . LEU A 1 76 ? 3.287 39.824 35.921 1.00 23.29 ? 117 LEU A N 1 ATOM 575 C CA . LEU A 1 76 ? 4.613 39.179 36.055 1.00 24.26 ? 117 LEU A CA 1 ATOM 576 C C . LEU A 1 76 ? 4.991 38.643 34.656 1.00 25.22 ? 117 LEU A C 1 ATOM 577 O O . LEU A 1 76 ? 4.219 38.835 33.713 1.00 26.57 ? 117 LEU A O 1 ATOM 578 C CB . LEU A 1 76 ? 4.645 38.082 37.128 1.00 23.45 ? 117 LEU A CB 1 ATOM 579 C CG . LEU A 1 76 ? 4.328 38.567 38.573 1.00 23.57 ? 117 LEU A CG 1 ATOM 580 C CD1 . LEU A 1 76 ? 4.440 37.392 39.554 1.00 25.19 ? 117 LEU A CD1 1 ATOM 581 C CD2 . LEU A 1 76 ? 5.266 39.748 39.052 1.00 23.60 ? 117 LEU A CD2 1 ATOM 582 N N . SER A 1 77 ? 6.156 37.992 34.572 1.00 25.00 ? 118 SER A N 1 ATOM 583 C CA . SER A 1 77 ? 6.711 37.537 33.289 1.00 26.19 ? 118 SER A CA 1 ATOM 584 C C . SER A 1 77 ? 7.477 36.246 33.514 1.00 25.44 ? 118 SER A C 1 ATOM 585 O O . SER A 1 77 ? 8.269 36.159 34.446 1.00 25.63 ? 118 SER A O 1 ATOM 586 C CB . SER A 1 77 ? 7.648 38.634 32.736 1.00 26.65 ? 118 SER A CB 1 ATOM 587 O OG . SER A 1 77 ? 8.453 38.189 31.633 1.00 27.20 ? 118 SER A OG 1 ATOM 588 N N . TYR A 1 78 ? 7.281 35.250 32.642 1.00 26.52 ? 119 TYR A N 1 ATOM 589 C CA . TYR A 1 78 ? 7.930 33.986 32.810 1.00 26.99 ? 119 TYR A CA 1 ATOM 590 C C . TYR A 1 78 ? 8.261 33.405 31.452 1.00 28.95 ? 119 TYR A C 1 ATOM 591 O O . TYR A 1 78 ? 7.509 33.597 30.498 1.00 28.51 ? 119 TYR A O 1 ATOM 592 C CB . TYR A 1 78 ? 6.996 32.957 33.443 1.00 28.00 ? 119 TYR A CB 1 ATOM 593 C CG . TYR A 1 78 ? 6.468 33.345 34.818 1.00 28.69 ? 119 TYR A CG 1 ATOM 594 C CD1 . TYR A 1 78 ? 7.287 33.249 35.956 1.00 28.44 ? 119 TYR A CD1 1 ATOM 595 C CD2 . TYR A 1 78 ? 5.133 33.732 34.969 1.00 33.27 ? 119 TYR A CD2 1 ATOM 596 C CE1 . TYR A 1 78 ? 6.776 33.582 37.247 1.00 27.52 ? 119 TYR A CE1 1 ATOM 597 C CE2 . TYR A 1 78 ? 4.608 34.061 36.250 1.00 31.32 ? 119 TYR A CE2 1 ATOM 598 C CZ . TYR A 1 78 ? 5.435 33.952 37.370 1.00 31.31 ? 119 TYR A CZ 1 ATOM 599 O OH . TYR A 1 78 ? 4.936 34.228 38.627 1.00 29.57 ? 119 TYR A OH 1 ATOM 600 N N . PRO A 1 79 ? 9.345 32.649 31.394 1.00 29.48 ? 120 PRO A N 1 ATOM 601 C CA . PRO A 1 79 ? 9.617 31.961 30.124 1.00 31.09 ? 120 PRO A CA 1 ATOM 602 C C . PRO A 1 79 ? 8.554 30.894 29.853 1.00 34.10 ? 120 PRO A C 1 ATOM 603 O O . PRO A 1 79 ? 7.877 30.427 30.770 1.00 34.88 ? 120 PRO A O 1 ATOM 604 C CB . PRO A 1 79 ? 10.974 31.251 30.364 1.00 30.95 ? 120 PRO A CB 1 ATOM 605 C CG . PRO A 1 79 ? 11.569 31.846 31.574 1.00 30.51 ? 120 PRO A CG 1 ATOM 606 C CD . PRO A 1 79 ? 10.436 32.496 32.385 1.00 28.34 ? 120 PRO A CD 1 ATOM 607 N N . ASN A 1 80 ? 8.424 30.501 28.587 1.00 36.19 ? 121 ASN A N 1 ATOM 608 C CA . ASN A 1 80 ? 7.536 29.419 28.217 1.00 39.23 ? 121 ASN A CA 1 ATOM 609 C C . ASN A 1 80 ? 8.307 28.103 28.415 1.00 41.46 ? 121 ASN A C 1 ATOM 610 O O . ASN A 1 80 ? 9.320 27.842 27.720 1.00 40.97 ? 121 ASN A O 1 ATOM 611 C CB . ASN A 1 80 ? 7.116 29.601 26.774 1.00 39.22 ? 121 ASN A CB 1 ATOM 612 C CG . ASN A 1 80 ? 6.067 28.569 26.332 1.00 45.35 ? 121 ASN A CG 1 ATOM 613 O OD1 . ASN A 1 80 ? 6.117 27.407 26.722 1.00 47.84 ? 121 ASN A OD1 1 ATOM 614 N ND2 . ASN A 1 80 ? 5.122 28.997 25.534 1.00 51.82 ? 121 ASN A ND2 1 ATOM 615 N N . LYS A 1 81 ? 7.848 27.308 29.386 1.00 44.09 ? 122 LYS A N 1 ATOM 616 C CA . LYS A 1 81 ? 8.442 26.002 29.745 1.00 47.69 ? 122 LYS A CA 1 ATOM 617 C C . LYS A 1 81 ? 8.640 25.012 28.571 1.00 49.23 ? 122 LYS A C 1 ATOM 618 O O . LYS A 1 81 ? 9.589 24.212 28.563 1.00 50.13 ? 122 LYS A O 1 ATOM 619 C CB . LYS A 1 81 ? 7.603 25.329 30.851 1.00 49.31 ? 122 LYS A CB 1 ATOM 620 C CG . LYS A 1 81 ? 8.074 25.636 32.271 1.00 52.44 ? 122 LYS A CG 1 ATOM 621 C CD . LYS A 1 81 ? 8.047 24.365 33.159 1.00 60.98 ? 122 LYS A CD 1 ATOM 622 C CE . LYS A 1 81 ? 8.685 24.659 34.554 1.00 64.83 ? 122 LYS A CE 1 ATOM 623 N NZ . LYS A 1 81 ? 8.992 23.427 35.356 1.00 68.07 ? 122 LYS A NZ 1 ATOM 624 N N . THR A 1 82 ? 7.765 25.076 27.575 1.00 49.86 ? 123 THR A N 1 ATOM 625 C CA . THR A 1 82 ? 7.866 24.161 26.427 1.00 51.04 ? 123 THR A CA 1 ATOM 626 C C . THR A 1 82 ? 8.317 24.830 25.113 1.00 50.99 ? 123 THR A C 1 ATOM 627 O O . THR A 1 82 ? 8.204 24.248 24.037 1.00 52.12 ? 123 THR A O 1 ATOM 628 C CB . THR A 1 82 ? 6.528 23.409 26.202 1.00 52.12 ? 123 THR A CB 1 ATOM 629 O OG1 . THR A 1 82 ? 5.513 24.371 25.900 1.00 53.22 ? 123 THR A OG1 1 ATOM 630 C CG2 . THR A 1 82 ? 6.127 22.614 27.457 1.00 51.75 ? 123 THR A CG2 1 ATOM 631 N N . HIS A 1 83 ? 8.841 26.046 25.205 1.00 49.21 ? 124 HIS A N 1 ATOM 632 C CA . HIS A 1 83 ? 9.309 26.788 24.036 1.00 48.88 ? 124 HIS A CA 1 ATOM 633 C C . HIS A 1 83 ? 10.450 27.716 24.517 1.00 46.53 ? 124 HIS A C 1 ATOM 634 O O . HIS A 1 83 ? 10.252 28.931 24.644 1.00 44.26 ? 124 HIS A O 1 ATOM 635 C CB . HIS A 1 83 ? 8.138 27.603 23.493 1.00 49.74 ? 124 HIS A CB 1 ATOM 636 C CG . HIS A 1 83 ? 8.279 28.053 22.070 1.00 54.61 ? 124 HIS A CG 1 ATOM 637 N ND1 . HIS A 1 83 ? 7.510 29.073 21.544 1.00 58.50 ? 124 HIS A ND1 1 ATOM 638 C CD2 . HIS A 1 83 ? 9.055 27.606 21.052 1.00 61.20 ? 124 HIS A CD2 1 ATOM 639 C CE1 . HIS A 1 83 ? 7.810 29.236 20.265 1.00 61.22 ? 124 HIS A CE1 1 ATOM 640 N NE2 . HIS A 1 83 ? 8.750 28.364 19.944 1.00 63.23 ? 124 HIS A NE2 1 ATOM 641 N N . PRO A 1 84 ? 11.634 27.135 24.801 1.00 45.26 ? 125 PRO A N 1 ATOM 642 C CA . PRO A 1 84 ? 12.727 27.860 25.498 1.00 43.15 ? 125 PRO A CA 1 ATOM 643 C C . PRO A 1 84 ? 13.319 29.046 24.712 1.00 41.92 ? 125 PRO A C 1 ATOM 644 O O . PRO A 1 84 ? 13.337 29.045 23.472 1.00 42.00 ? 125 PRO A O 1 ATOM 645 C CB . PRO A 1 84 ? 13.794 26.771 25.737 1.00 44.62 ? 125 PRO A CB 1 ATOM 646 C CG . PRO A 1 84 ? 13.082 25.421 25.438 1.00 46.74 ? 125 PRO A CG 1 ATOM 647 C CD . PRO A 1 84 ? 12.010 25.745 24.456 1.00 46.62 ? 125 PRO A CD 1 ATOM 648 N N . ASN A 1 85 ? 13.756 30.066 25.448 1.00 37.80 ? 126 ASN A N 1 ATOM 649 C CA . ASN A 1 85 ? 14.433 31.231 24.887 1.00 37.23 ? 126 ASN A CA 1 ATOM 650 C C . ASN A 1 85 ? 15.870 30.854 24.574 1.00 37.16 ? 126 ASN A C 1 ATOM 651 O O . ASN A 1 85 ? 16.497 30.122 25.360 1.00 37.01 ? 126 ASN A O 1 ATOM 652 C CB . ASN A 1 85 ? 14.451 32.401 25.912 1.00 33.96 ? 126 ASN A CB 1 ATOM 653 C CG . ASN A 1 85 ? 13.042 32.857 26.287 1.00 35.97 ? 126 ASN A CG 1 ATOM 654 O OD1 . ASN A 1 85 ? 12.162 32.842 25.458 1.00 35.55 ? 126 ASN A OD1 1 ATOM 655 N ND2 . ASN A 1 85 ? 12.832 33.243 27.549 1.00 32.49 ? 126 ASN A ND2 1 ATOM 656 N N . TYR A 1 86 ? 16.360 31.300 23.417 1.00 37.35 ? 127 TYR A N 1 ATOM 657 C CA . TYR A 1 86 ? 17.785 31.129 23.074 1.00 38.25 ? 127 TYR A CA 1 ATOM 658 C C . TYR A 1 86 ? 18.177 32.080 21.966 1.00 38.31 ? 127 TYR A C 1 ATOM 659 O O . TYR A 1 86 ? 17.321 32.768 21.401 1.00 39.28 ? 127 TYR A O 1 ATOM 660 C CB . TYR A 1 86 ? 18.114 29.667 22.749 1.00 38.23 ? 127 TYR A CB 1 ATOM 661 C CG . TYR A 1 86 ? 17.598 29.182 21.419 1.00 41.58 ? 127 TYR A CG 1 ATOM 662 C CD1 . TYR A 1 86 ? 18.479 28.987 20.355 1.00 44.70 ? 127 TYR A CD1 1 ATOM 663 C CD2 . TYR A 1 86 ? 16.255 28.882 21.221 1.00 41.70 ? 127 TYR A CD2 1 ATOM 664 C CE1 . TYR A 1 86 ? 18.034 28.522 19.118 1.00 46.82 ? 127 TYR A CE1 1 ATOM 665 C CE2 . TYR A 1 86 ? 15.791 28.416 19.966 1.00 45.26 ? 127 TYR A CE2 1 ATOM 666 C CZ . TYR A 1 86 ? 16.692 28.245 18.930 1.00 48.25 ? 127 TYR A CZ 1 ATOM 667 O OH . TYR A 1 86 ? 16.262 27.788 17.694 1.00 49.03 ? 127 TYR A OH 1 ATOM 668 N N . ILE A 1 87 ? 19.479 32.169 21.710 1.00 38.42 ? 128 ILE A N 1 ATOM 669 C CA . ILE A 1 87 ? 20.015 33.026 20.672 1.00 37.88 ? 128 ILE A CA 1 ATOM 670 C C . ILE A 1 87 ? 20.863 32.116 19.768 1.00 39.21 ? 128 ILE A C 1 ATOM 671 O O . ILE A 1 87 ? 21.515 31.171 20.244 1.00 37.91 ? 128 ILE A O 1 ATOM 672 C CB . ILE A 1 87 ? 20.914 34.142 21.256 1.00 37.64 ? 128 ILE A CB 1 ATOM 673 C CG1 . ILE A 1 87 ? 20.087 35.144 22.120 1.00 35.91 ? 128 ILE A CG1 1 ATOM 674 C CG2 . ILE A 1 87 ? 21.674 34.874 20.159 1.00 38.94 ? 128 ILE A CG2 1 ATOM 675 C CD1 . ILE A 1 87 ? 20.958 35.899 23.109 1.00 38.45 ? 128 ILE A CD1 1 ATOM 676 N N . SER A 1 88 ? 20.852 32.424 18.478 1.00 40.94 ? 129 SER A N 1 ATOM 677 C CA . SER A 1 88 ? 21.634 31.691 17.481 1.00 43.24 ? 129 SER A CA 1 ATOM 678 C C . SER A 1 88 ? 22.546 32.586 16.650 1.00 44.49 ? 129 SER A C 1 ATOM 679 O O . SER A 1 88 ? 22.252 33.779 16.452 1.00 43.86 ? 129 SER A O 1 ATOM 680 C CB . SER A 1 88 ? 20.697 31.006 16.486 1.00 43.81 ? 129 SER A CB 1 ATOM 681 O OG . SER A 1 88 ? 19.935 30.011 17.111 1.00 46.77 ? 129 SER A OG 1 ATOM 682 N N . ILE A 1 89 ? 23.633 31.983 16.136 1.00 45.44 ? 130 ILE A N 1 ATOM 683 C CA . ILE A 1 89 ? 24.297 32.507 14.947 1.00 47.35 ? 130 ILE A CA 1 ATOM 684 C C . ILE A 1 89 ? 23.730 31.649 13.832 1.00 49.09 ? 130 ILE A C 1 ATOM 685 O O . ILE A 1 89 ? 23.661 30.420 13.947 1.00 47.95 ? 130 ILE A O 1 ATOM 686 C CB . ILE A 1 89 ? 25.836 32.410 14.976 1.00 48.08 ? 130 ILE A CB 1 ATOM 687 C CG1 . ILE A 1 89 ? 26.416 33.328 16.062 1.00 45.98 ? 130 ILE A CG1 1 ATOM 688 C CG2 . ILE A 1 89 ? 26.418 32.738 13.575 1.00 49.75 ? 130 ILE A CG2 1 ATOM 689 C CD1 . ILE A 1 89 ? 27.856 33.020 16.411 1.00 49.54 ? 130 ILE A CD1 1 ATOM 690 N N . ILE A 1 90 ? 23.294 32.325 12.781 1.00 51.68 ? 131 ILE A N 1 ATOM 691 C CA . ILE A 1 90 ? 22.570 31.693 11.695 1.00 55.65 ? 131 ILE A CA 1 ATOM 692 C C . ILE A 1 90 ? 23.344 31.986 10.394 1.00 58.07 ? 131 ILE A C 1 ATOM 693 O O . ILE A 1 90 ? 23.849 33.103 10.201 1.00 57.67 ? 131 ILE A O 1 ATOM 694 C CB . ILE A 1 90 ? 21.049 32.162 11.750 1.00 55.64 ? 131 ILE A CB 1 ATOM 695 C CG1 . ILE A 1 90 ? 20.115 31.135 11.117 1.00 58.76 ? 131 ILE A CG1 1 ATOM 696 C CG2 . ILE A 1 90 ? 20.832 33.592 11.204 1.00 56.55 ? 131 ILE A CG2 1 ATOM 697 C CD1 . ILE A 1 90 ? 18.661 31.342 11.538 1.00 60.99 ? 131 ILE A CD1 1 ATOM 698 N N . ASN A 1 91 ? 23.523 30.972 9.545 1.00 60.93 ? 132 ASN A N 1 ATOM 699 C CA . ASN A 1 91 ? 24.193 31.206 8.240 1.00 64.59 ? 132 ASN A CA 1 ATOM 700 C C . ASN A 1 91 ? 23.210 31.708 7.177 1.00 66.72 ? 132 ASN A C 1 ATOM 701 O O . ASN A 1 91 ? 22.004 31.815 7.448 1.00 66.04 ? 132 ASN A O 1 ATOM 702 C CB . ASN A 1 91 ? 25.015 29.987 7.758 1.00 65.47 ? 132 ASN A CB 1 ATOM 703 C CG . ASN A 1 91 ? 24.160 28.760 7.484 1.00 65.68 ? 132 ASN A CG 1 ATOM 704 O OD1 . ASN A 1 91 ? 22.974 28.870 7.158 1.00 65.71 ? 132 ASN A OD1 1 ATOM 705 N ND2 . ASN A 1 91 ? 24.763 27.577 7.619 1.00 63.53 ? 132 ASN A ND2 1 ATOM 706 N N . GLU A 1 92 ? 23.712 32.003 5.975 1.00 70.10 ? 133 GLU A N 1 ATOM 707 C CA . GLU A 1 92 ? 22.863 32.538 4.893 1.00 72.54 ? 133 GLU A CA 1 ATOM 708 C C . GLU A 1 92 ? 21.814 31.554 4.352 1.00 73.59 ? 133 GLU A C 1 ATOM 709 O O . GLU A 1 92 ? 20.857 31.970 3.706 1.00 74.59 ? 133 GLU A O 1 ATOM 710 C CB . GLU A 1 92 ? 23.722 33.060 3.748 1.00 74.36 ? 133 GLU A CB 1 ATOM 711 C CG . GLU A 1 92 ? 24.739 32.048 3.230 1.00 78.05 ? 133 GLU A CG 1 ATOM 712 C CD . GLU A 1 92 ? 25.718 32.664 2.248 1.00 82.34 ? 133 GLU A CD 1 ATOM 713 O OE1 . GLU A 1 92 ? 25.757 33.917 2.147 1.00 83.65 ? 133 GLU A OE1 1 ATOM 714 O OE2 . GLU A 1 92 ? 26.446 31.898 1.579 1.00 84.51 ? 133 GLU A OE2 1 ATOM 715 N N . ASP A 1 93 ? 22.010 30.259 4.602 1.00 74.13 ? 134 ASP A N 1 ATOM 716 C CA . ASP A 1 93 ? 20.986 29.238 4.339 1.00 74.85 ? 134 ASP A CA 1 ATOM 717 C C . ASP A 1 93 ? 19.875 29.288 5.384 1.00 73.01 ? 134 ASP A C 1 ATOM 718 O O . ASP A 1 93 ? 18.755 28.840 5.134 1.00 74.25 ? 134 ASP A O 1 ATOM 719 C CB . ASP A 1 93 ? 21.614 27.846 4.344 1.00 75.74 ? 134 ASP A CB 1 ATOM 720 C CG . ASP A 1 93 ? 22.624 27.665 3.234 1.00 79.64 ? 134 ASP A CG 1 ATOM 721 O OD1 . ASP A 1 93 ? 22.540 28.409 2.228 1.00 81.15 ? 134 ASP A OD1 1 ATOM 722 O OD2 . ASP A 1 93 ? 23.504 26.781 3.357 1.00 82.56 ? 134 ASP A OD2 1 ATOM 723 N N . GLY A 1 94 ? 20.187 29.830 6.558 1.00 70.53 ? 135 GLY A N 1 ATOM 724 C CA . GLY A 1 94 ? 19.250 29.830 7.662 1.00 67.31 ? 135 GLY A CA 1 ATOM 725 C C . GLY A 1 94 ? 19.454 28.654 8.609 1.00 65.11 ? 135 GLY A C 1 ATOM 726 O O . GLY A 1 94 ? 18.544 28.315 9.370 1.00 65.50 ? 135 GLY A O 1 ATOM 727 N N . ASN A 1 95 ? 20.630 28.026 8.565 1.00 63.54 ? 136 ASN A N 1 ATOM 728 C CA A ASN A 1 95 ? 20.975 27.007 9.552 0.50 61.57 ? 136 ASN A CA 1 ATOM 729 C CA B ASN A 1 95 ? 20.993 27.001 9.543 0.50 61.93 ? 136 ASN A CA 1 ATOM 730 C C . ASN A 1 95 ? 21.555 27.660 10.813 1.00 59.37 ? 136 ASN A C 1 ATOM 731 O O . ASN A 1 95 ? 22.398 28.566 10.732 1.00 58.72 ? 136 ASN A O 1 ATOM 732 C CB A ASN A 1 95 ? 21.959 25.989 8.985 0.50 62.58 ? 136 ASN A CB 1 ATOM 733 C CB B ASN A 1 95 ? 22.011 26.032 8.944 0.50 63.31 ? 136 ASN A CB 1 ATOM 734 C CG A ASN A 1 95 ? 21.531 25.442 7.636 0.50 63.46 ? 136 ASN A CG 1 ATOM 735 C CG B ASN A 1 95 ? 21.990 24.664 9.607 0.50 63.79 ? 136 ASN A CG 1 ATOM 736 O OD1 A ASN A 1 95 ? 20.347 25.407 7.301 0.50 62.44 ? 136 ASN A OD1 1 ATOM 737 O OD1 B ASN A 1 95 ? 21.790 24.541 10.819 0.50 63.33 ? 136 ASN A OD1 1 ATOM 738 N ND2 A ASN A 1 95 ? 22.502 25.023 6.854 0.50 62.67 ? 136 ASN A ND2 1 ATOM 739 N ND2 B ASN A 1 95 ? 22.203 23.623 8.807 0.50 64.92 ? 136 ASN A ND2 1 ATOM 740 N N . GLU A 1 96 ? 21.087 27.208 11.976 1.00 57.01 ? 137 GLU A N 1 ATOM 741 C CA . GLU A 1 96 ? 21.552 27.751 13.268 1.00 53.83 ? 137 GLU A CA 1 ATOM 742 C C . GLU A 1 96 ? 22.782 26.934 13.666 1.00 53.43 ? 137 GLU A C 1 ATOM 743 O O . GLU A 1 96 ? 22.674 25.768 14.054 1.00 52.99 ? 137 GLU A O 1 ATOM 744 C CB . GLU A 1 96 ? 20.428 27.710 14.320 1.00 52.43 ? 137 GLU A CB 1 ATOM 745 C CG . GLU A 1 96 ? 19.157 28.433 13.828 1.00 51.07 ? 137 GLU A CG 1 ATOM 746 C CD . GLU A 1 96 ? 18.052 28.605 14.879 1.00 51.96 ? 137 GLU A CD 1 ATOM 747 O OE1 . GLU A 1 96 ? 17.914 27.762 15.790 1.00 48.62 ? 137 GLU A OE1 1 ATOM 748 O OE2 . GLU A 1 96 ? 17.292 29.594 14.759 1.00 51.73 ? 137 GLU A OE2 1 ATOM 749 N N . ILE A 1 97 ? 23.955 27.555 13.515 1.00 52.66 ? 138 ILE A N 1 ATOM 750 C CA . ILE A 1 97 ? 25.254 26.863 13.665 1.00 52.40 ? 138 ILE A CA 1 ATOM 751 C C . ILE A 1 97 ? 25.830 26.961 15.079 1.00 50.33 ? 138 ILE A C 1 ATOM 752 O O . ILE A 1 97 ? 26.775 26.254 15.441 1.00 49.21 ? 138 ILE A O 1 ATOM 753 C CB . ILE A 1 97 ? 26.292 27.348 12.619 1.00 54.10 ? 138 ILE A CB 1 ATOM 754 C CG1 . ILE A 1 97 ? 26.607 28.846 12.805 1.00 54.01 ? 138 ILE A CG1 1 ATOM 755 C CG2 . ILE A 1 97 ? 25.800 27.005 11.209 1.00 55.67 ? 138 ILE A CG2 1 ATOM 756 C CD1 . ILE A 1 97 ? 27.798 29.375 11.932 1.00 55.87 ? 138 ILE A CD1 1 ATOM 757 N N . PHE A 1 98 ? 25.230 27.818 15.895 1.00 47.50 ? 139 PHE A N 1 ATOM 758 C CA . PHE A 1 98 ? 25.605 27.920 17.287 1.00 46.38 ? 139 PHE A CA 1 ATOM 759 C C . PHE A 1 98 ? 24.374 28.375 18.052 1.00 43.78 ? 139 PHE A C 1 ATOM 760 O O . PHE A 1 98 ? 23.676 29.271 17.587 1.00 42.94 ? 139 PHE A O 1 ATOM 761 C CB . PHE A 1 98 ? 26.709 28.953 17.519 1.00 46.26 ? 139 PHE A CB 1 ATOM 762 C CG . PHE A 1 98 ? 26.835 29.369 18.970 1.00 47.11 ? 139 PHE A CG 1 ATOM 763 C CD1 . PHE A 1 98 ? 27.487 28.535 19.895 1.00 48.56 ? 139 PHE A CD1 1 ATOM 764 C CD2 . PHE A 1 98 ? 26.293 30.567 19.411 1.00 47.14 ? 139 PHE A CD2 1 ATOM 765 C CE1 . PHE A 1 98 ? 27.591 28.899 21.239 1.00 48.29 ? 139 PHE A CE1 1 ATOM 766 C CE2 . PHE A 1 98 ? 26.379 30.939 20.775 1.00 46.01 ? 139 PHE A CE2 1 ATOM 767 C CZ . PHE A 1 98 ? 27.034 30.108 21.679 1.00 46.05 ? 139 PHE A CZ 1 ATOM 768 N N . ASN A 1 99 ? 24.119 27.725 19.185 1.00 43.48 ? 140 ASN A N 1 ATOM 769 C CA . ASN A 1 99 ? 23.012 28.087 20.093 1.00 43.27 ? 140 ASN A CA 1 ATOM 770 C C . ASN A 1 99 ? 23.499 28.368 21.485 1.00 41.30 ? 140 ASN A C 1 ATOM 771 O O . ASN A 1 99 ? 24.314 27.603 22.013 1.00 41.36 ? 140 ASN A O 1 ATOM 772 C CB . ASN A 1 99 ? 22.033 26.920 20.209 1.00 44.43 ? 140 ASN A CB 1 ATOM 773 C CG . ASN A 1 99 ? 21.267 26.646 18.903 1.00 49.58 ? 140 ASN A CG 1 ATOM 774 O OD1 . ASN A 1 99 ? 20.991 27.564 18.117 1.00 48.02 ? 140 ASN A OD1 1 ATOM 775 N ND2 . ASN A 1 99 ? 20.908 25.384 18.689 1.00 53.46 ? 140 ASN A ND2 1 ATOM 776 N N . THR A 1 100 ? 22.962 29.422 22.113 1.00 40.26 ? 141 THR A N 1 ATOM 777 C CA . THR A 1 100 ? 23.291 29.708 23.517 1.00 39.02 ? 141 THR A CA 1 ATOM 778 C C . THR A 1 100 ? 22.571 28.679 24.404 1.00 39.34 ? 141 THR A C 1 ATOM 779 O O . THR A 1 100 ? 21.640 28.005 23.957 1.00 39.07 ? 141 THR A O 1 ATOM 780 C CB . THR A 1 100 ? 22.907 31.151 23.921 1.00 37.68 ? 141 THR A CB 1 ATOM 781 O OG1 . THR A 1 100 ? 21.497 31.324 23.781 1.00 35.80 ? 141 THR A OG1 1 ATOM 782 C CG2 . THR A 1 100 ? 23.628 32.160 23.036 1.00 39.21 ? 141 THR A CG2 1 ATOM 783 N N . SER A 1 101 ? 22.987 28.584 25.660 1.00 39.24 ? 142 SER A N 1 ATOM 784 C CA A SER A 1 101 ? 22.509 27.538 26.546 0.50 39.55 ? 142 SER A CA 1 ATOM 785 C CA B SER A 1 101 ? 22.505 27.542 26.564 0.50 39.33 ? 142 SER A CA 1 ATOM 786 C C . SER A 1 101 ? 21.033 27.705 26.920 1.00 38.87 ? 142 SER A C 1 ATOM 787 O O . SER A 1 101 ? 20.499 28.832 26.943 1.00 39.04 ? 142 SER A O 1 ATOM 788 C CB A SER A 1 101 ? 23.403 27.486 27.793 0.50 40.01 ? 142 SER A CB 1 ATOM 789 C CB B SER A 1 101 ? 23.339 27.540 27.850 0.50 39.65 ? 142 SER A CB 1 ATOM 790 O OG A SER A 1 101 ? 22.984 26.472 28.679 0.50 40.63 ? 142 SER A OG 1 ATOM 791 O OG B SER A 1 101 ? 22.872 28.543 28.737 0.50 38.35 ? 142 SER A OG 1 ATOM 792 N N . LEU A 1 102 ? 20.374 26.594 27.222 1.00 39.17 ? 143 LEU A N 1 ATOM 793 C CA . LEU A 1 102 ? 18.958 26.643 27.630 1.00 39.60 ? 143 LEU A CA 1 ATOM 794 C C . LEU A 1 102 ? 18.822 26.756 29.162 1.00 38.93 ? 143 LEU A C 1 ATOM 795 O O . LEU A 1 102 ? 17.714 27.027 29.690 1.00 39.08 ? 143 LEU A O 1 ATOM 796 C CB . LEU A 1 102 ? 18.179 25.442 27.075 1.00 41.92 ? 143 LEU A CB 1 ATOM 797 C CG . LEU A 1 102 ? 18.213 25.269 25.550 1.00 43.81 ? 143 LEU A CG 1 ATOM 798 C CD1 . LEU A 1 102 ? 17.289 24.128 25.113 1.00 44.91 ? 143 LEU A CD1 1 ATOM 799 C CD2 . LEU A 1 102 ? 17.818 26.567 24.868 1.00 44.72 ? 143 LEU A CD2 1 ATOM 800 N N . PHE A 1 103 ? 19.947 26.632 29.879 1.00 37.75 ? 144 PHE A N 1 ATOM 801 C CA . PHE A 1 103 ? 19.919 26.724 31.357 1.00 36.84 ? 144 PHE A CA 1 ATOM 802 C C . PHE A 1 103 ? 21.328 26.828 31.912 1.00 36.30 ? 144 PHE A C 1 ATOM 803 O O . PHE A 1 103 ? 22.273 26.419 31.210 1.00 36.33 ? 144 PHE A O 1 ATOM 804 C CB . PHE A 1 103 ? 19.212 25.489 31.933 1.00 37.33 ? 144 PHE A CB 1 ATOM 805 C CG . PHE A 1 103 ? 19.893 24.183 31.603 1.00 40.36 ? 144 PHE A CG 1 ATOM 806 C CD1 . PHE A 1 103 ? 20.865 23.663 32.446 1.00 42.39 ? 144 PHE A CD1 1 ATOM 807 C CD2 . PHE A 1 103 ? 19.574 23.482 30.438 1.00 45.25 ? 144 PHE A CD2 1 ATOM 808 C CE1 . PHE A 1 103 ? 21.514 22.476 32.150 1.00 44.86 ? 144 PHE A CE1 1 ATOM 809 C CE2 . PHE A 1 103 ? 20.202 22.274 30.127 1.00 47.49 ? 144 PHE A CE2 1 ATOM 810 C CZ . PHE A 1 103 ? 21.180 21.768 30.985 1.00 50.55 ? 144 PHE A CZ 1 ATOM 811 N N . GLU A 1 104 ? 21.495 27.342 33.141 1.00 34.21 ? 145 GLU A N 1 ATOM 812 C CA . GLU A 1 104 ? 22.793 27.317 33.850 1.00 34.96 ? 145 GLU A CA 1 ATOM 813 C C . GLU A 1 104 ? 23.031 25.916 34.443 1.00 36.02 ? 145 GLU A C 1 ATOM 814 O O . GLU A 1 104 ? 22.121 25.359 35.057 1.00 36.31 ? 145 GLU A O 1 ATOM 815 C CB . GLU A 1 104 ? 22.847 28.308 35.034 1.00 33.75 ? 145 GLU A CB 1 ATOM 816 C CG . GLU A 1 104 ? 22.653 29.763 34.704 1.00 35.18 ? 145 GLU A CG 1 ATOM 817 C CD . GLU A 1 104 ? 22.516 30.626 35.997 1.00 36.09 ? 145 GLU A CD 1 ATOM 818 O OE1 . GLU A 1 104 ? 21.426 30.634 36.582 1.00 37.49 ? 145 GLU A OE1 1 ATOM 819 O OE2 . GLU A 1 104 ? 23.541 31.212 36.432 1.00 38.02 ? 145 GLU A OE2 1 ATOM 820 N N . PRO A 1 105 ? 24.249 25.358 34.298 1.00 37.39 ? 146 PRO A N 1 ATOM 821 C CA . PRO A 1 105 ? 24.531 24.059 34.962 1.00 38.29 ? 146 PRO A CA 1 ATOM 822 C C . PRO A 1 105 ? 24.220 24.199 36.463 1.00 37.50 ? 146 PRO A C 1 ATOM 823 O O . PRO A 1 105 ? 24.727 25.120 37.106 1.00 37.86 ? 146 PRO A O 1 ATOM 824 C CB . PRO A 1 105 ? 26.036 23.860 34.719 1.00 39.68 ? 146 PRO A CB 1 ATOM 825 C CG . PRO A 1 105 ? 26.348 24.720 33.495 1.00 40.34 ? 146 PRO A CG 1 ATOM 826 C CD . PRO A 1 105 ? 25.429 25.897 33.587 1.00 38.02 ? 146 PRO A CD 1 ATOM 827 N N . PRO A 1 106 ? 23.325 23.361 37.012 1.00 37.72 ? 147 PRO A N 1 ATOM 828 C CA . PRO A 1 106 ? 22.939 23.665 38.389 1.00 37.49 ? 147 PRO A CA 1 ATOM 829 C C . PRO A 1 106 ? 24.065 23.352 39.395 1.00 37.33 ? 147 PRO A C 1 ATOM 830 O O . PRO A 1 106 ? 24.911 22.488 39.117 1.00 39.05 ? 147 PRO A O 1 ATOM 831 C CB . PRO A 1 106 ? 21.704 22.776 38.616 1.00 38.01 ? 147 PRO A CB 1 ATOM 832 C CG . PRO A 1 106 ? 21.768 21.763 37.566 1.00 39.43 ? 147 PRO A CG 1 ATOM 833 C CD . PRO A 1 106 ? 22.417 22.380 36.394 1.00 38.62 ? 147 PRO A CD 1 ATOM 834 N N . PRO A 1 107 ? 24.069 24.038 40.555 1.00 36.30 ? 148 PRO A N 1 ATOM 835 C CA . PRO A 1 107 ? 25.171 23.816 41.505 1.00 36.55 ? 148 PRO A CA 1 ATOM 836 C C . PRO A 1 107 ? 25.116 22.396 42.115 1.00 36.88 ? 148 PRO A C 1 ATOM 837 O O . PRO A 1 107 ? 24.031 21.779 42.126 1.00 36.05 ? 148 PRO A O 1 ATOM 838 C CB . PRO A 1 107 ? 24.916 24.851 42.598 1.00 36.53 ? 148 PRO A CB 1 ATOM 839 C CG . PRO A 1 107 ? 23.505 25.295 42.446 1.00 35.42 ? 148 PRO A CG 1 ATOM 840 C CD . PRO A 1 107 ? 23.060 24.989 41.048 1.00 35.70 ? 148 PRO A CD 1 ATOM 841 N N . PRO A 1 108 ? 26.238 21.923 42.688 1.00 37.08 ? 149 PRO A N 1 ATOM 842 C CA . PRO A 1 108 ? 26.304 20.545 43.222 1.00 37.90 ? 149 PRO A CA 1 ATOM 843 C C . PRO A 1 108 ? 25.232 20.233 44.292 1.00 38.01 ? 149 PRO A C 1 ATOM 844 O O . PRO A 1 108 ? 25.071 20.994 45.265 1.00 36.40 ? 149 PRO A O 1 ATOM 845 C CB . PRO A 1 108 ? 27.699 20.496 43.846 1.00 38.94 ? 149 PRO A CB 1 ATOM 846 C CG . PRO A 1 108 ? 28.500 21.523 43.082 1.00 38.02 ? 149 PRO A CG 1 ATOM 847 C CD . PRO A 1 108 ? 27.539 22.622 42.770 1.00 37.40 ? 149 PRO A CD 1 ATOM 848 N N . GLY A 1 109 ? 24.507 19.129 44.123 1.00 38.71 ? 150 GLY A N 1 ATOM 849 C CA . GLY A 1 109 ? 23.527 18.743 45.128 1.00 40.61 ? 150 GLY A CA 1 ATOM 850 C C . GLY A 1 109 ? 22.127 19.309 44.891 1.00 42.25 ? 150 GLY A C 1 ATOM 851 O O . GLY A 1 109 ? 21.202 18.944 45.621 1.00 43.15 ? 150 GLY A O 1 ATOM 852 N N . TYR A 1 110 ? 22.004 20.195 43.895 1.00 42.61 ? 151 TYR A N 1 ATOM 853 C CA . TYR A 1 110 ? 20.733 20.834 43.476 1.00 45.06 ? 151 TYR A CA 1 ATOM 854 C C . TYR A 1 110 ? 20.434 20.542 42.016 1.00 48.51 ? 151 TYR A C 1 ATOM 855 O O . TYR A 1 110 ? 19.587 21.229 41.405 1.00 49.13 ? 151 TYR A O 1 ATOM 856 C CB . TYR A 1 110 ? 20.880 22.334 43.461 1.00 42.59 ? 151 TYR A CB 1 ATOM 857 C CG . TYR A 1 110 ? 21.145 23.001 44.771 1.00 39.53 ? 151 TYR A CG 1 ATOM 858 C CD1 . TYR A 1 110 ? 20.097 23.542 45.525 1.00 37.35 ? 151 TYR A CD1 1 ATOM 859 C CD2 . TYR A 1 110 ? 22.432 23.154 45.227 1.00 33.53 ? 151 TYR A CD2 1 ATOM 860 C CE1 . TYR A 1 110 ? 20.342 24.190 46.714 1.00 36.08 ? 151 TYR A CE1 1 ATOM 861 C CE2 . TYR A 1 110 ? 22.691 23.782 46.417 1.00 34.77 ? 151 TYR A CE2 1 ATOM 862 C CZ . TYR A 1 110 ? 21.629 24.311 47.151 1.00 34.28 ? 151 TYR A CZ 1 ATOM 863 O OH . TYR A 1 110 ? 21.913 24.918 48.325 1.00 33.61 ? 151 TYR A OH 1 ATOM 864 N N . GLU A 1 111 ? 21.196 19.643 41.410 1.00 51.61 ? 152 GLU A N 1 ATOM 865 C CA . GLU A 1 111 ? 20.935 19.251 40.023 1.00 55.69 ? 152 GLU A CA 1 ATOM 866 C C . GLU A 1 111 ? 19.534 18.564 39.877 1.00 57.21 ? 152 GLU A C 1 ATOM 867 O O . GLU A 1 111 ? 19.045 18.376 38.751 1.00 58.25 ? 152 GLU A O 1 ATOM 868 C CB . GLU A 1 111 ? 22.089 18.376 39.439 1.00 56.76 ? 152 GLU A CB 1 ATOM 869 C CG . GLU A 1 111 ? 23.563 18.883 39.723 1.00 60.14 ? 152 GLU A CG 1 ATOM 870 C CD . GLU A 1 111 ? 24.250 18.261 40.987 1.00 63.01 ? 152 GLU A CD 1 ATOM 871 O OE1 . GLU A 1 111 ? 23.560 17.810 41.926 1.00 62.79 ? 152 GLU A OE1 1 ATOM 872 O OE2 . GLU A 1 111 ? 25.503 18.234 41.042 1.00 65.60 ? 152 GLU A OE2 1 ATOM 873 N N . ASN A 1 112 ? 18.887 18.224 41.008 1.00 58.54 ? 153 ASN A N 1 ATOM 874 C CA . ASN A 1 112 ? 17.524 17.629 40.993 1.00 59.03 ? 153 ASN A CA 1 ATOM 875 C C . ASN A 1 112 ? 16.392 18.558 41.509 1.00 58.43 ? 153 ASN A C 1 ATOM 876 O O . ASN A 1 112 ? 15.231 18.178 41.579 1.00 58.48 ? 153 ASN A O 1 ATOM 877 C CB . ASN A 1 112 ? 17.503 16.269 41.709 1.00 60.24 ? 153 ASN A CB 1 ATOM 878 C CG . ASN A 1 112 ? 16.244 15.458 41.397 1.00 61.60 ? 153 ASN A CG 1 ATOM 879 O OD1 . ASN A 1 112 ? 16.029 15.011 40.264 1.00 63.34 ? 153 ASN A OD1 1 ATOM 880 N ND2 . ASN A 1 112 ? 15.407 15.269 42.411 1.00 63.15 ? 153 ASN A ND2 1 ATOM 881 N N . VAL A 1 113 ? 16.726 19.789 41.851 1.00 57.44 ? 154 VAL A N 1 ATOM 882 C CA . VAL A 1 113 ? 15.684 20.748 42.142 1.00 56.43 ? 154 VAL A CA 1 ATOM 883 C C . VAL A 1 113 ? 14.977 21.076 40.804 1.00 56.53 ? 154 VAL A C 1 ATOM 884 O O . VAL A 1 113 ? 15.617 21.255 39.767 1.00 57.45 ? 154 VAL A O 1 ATOM 885 C CB . VAL A 1 113 ? 16.237 21.996 42.887 1.00 56.05 ? 154 VAL A CB 1 ATOM 886 C CG1 . VAL A 1 113 ? 15.116 22.984 43.226 1.00 51.70 ? 154 VAL A CG1 1 ATOM 887 C CG2 . VAL A 1 113 ? 16.957 21.560 44.173 1.00 56.98 ? 154 VAL A CG2 1 ATOM 888 N N . SER A 1 114 ? 13.654 21.056 40.804 1.00 56.27 ? 155 SER A N 1 ATOM 889 C CA . SER A 1 114 ? 12.947 21.523 39.613 1.00 55.63 ? 155 SER A CA 1 ATOM 890 C C . SER A 1 114 ? 12.343 22.906 39.879 1.00 53.48 ? 155 SER A C 1 ATOM 891 O O . SER A 1 114 ? 12.442 23.480 41.021 1.00 52.30 ? 155 SER A O 1 ATOM 892 C CB . SER A 1 114 ? 11.910 20.496 39.077 1.00 57.36 ? 155 SER A CB 1 ATOM 893 O OG . SER A 1 114 ? 10.949 20.174 40.074 1.00 60.39 ? 155 SER A OG 1 ATOM 894 N N . ASP A 1 115 ? 11.764 23.466 38.824 1.00 50.58 ? 156 ASP A N 1 ATOM 895 C CA . ASP A 1 115 ? 11.221 24.779 38.933 1.00 47.52 ? 156 ASP A CA 1 ATOM 896 C C . ASP A 1 115 ? 12.391 25.750 39.107 1.00 43.19 ? 156 ASP A C 1 ATOM 897 O O . ASP A 1 115 ? 12.206 26.803 39.707 1.00 41.53 ? 156 ASP A O 1 ATOM 898 C CB . ASP A 1 115 ? 10.308 24.874 40.178 1.00 49.27 ? 156 ASP A CB 1 ATOM 899 C CG . ASP A 1 115 ? 8.809 24.723 39.861 1.00 54.87 ? 156 ASP A CG 1 ATOM 900 O OD1 . ASP A 1 115 ? 8.042 25.715 40.100 1.00 59.32 ? 156 ASP A OD1 1 ATOM 901 O OD2 . ASP A 1 115 ? 8.404 23.629 39.393 1.00 59.48 ? 156 ASP A OD2 1 ATOM 902 N N . ILE A 1 116 ? 13.601 25.409 38.633 1.00 38.42 ? 157 ILE A N 1 ATOM 903 C CA . ILE A 1 116 ? 14.600 26.482 38.516 1.00 35.27 ? 157 ILE A CA 1 ATOM 904 C C . ILE A 1 116 ? 14.279 27.236 37.231 1.00 33.89 ? 157 ILE A C 1 ATOM 905 O O . ILE A 1 116 ? 14.356 26.661 36.127 1.00 34.46 ? 157 ILE A O 1 ATOM 906 C CB . ILE A 1 116 ? 16.061 25.942 38.466 1.00 33.98 ? 157 ILE A CB 1 ATOM 907 C CG1 . ILE A 1 116 ? 16.453 25.385 39.820 1.00 33.35 ? 157 ILE A CG1 1 ATOM 908 C CG2 . ILE A 1 116 ? 17.025 27.078 38.130 1.00 31.44 ? 157 ILE A CG2 1 ATOM 909 C CD1 . ILE A 1 116 ? 17.843 24.692 39.841 1.00 33.63 ? 157 ILE A CD1 1 ATOM 910 N N . VAL A 1 117 ? 13.916 28.501 37.346 1.00 32.67 ? 158 VAL A N 1 ATOM 911 C CA . VAL A 1 117 ? 13.586 29.272 36.168 1.00 31.23 ? 158 VAL A CA 1 ATOM 912 C C . VAL A 1 117 ? 14.872 29.528 35.374 1.00 31.59 ? 158 VAL A C 1 ATOM 913 O O . VAL A 1 117 ? 15.830 30.054 35.925 1.00 31.05 ? 158 VAL A O 1 ATOM 914 C CB . VAL A 1 117 ? 12.872 30.642 36.528 1.00 29.56 ? 158 VAL A CB 1 ATOM 915 C CG1 . VAL A 1 117 ? 13.932 31.751 37.176 1.00 26.99 ? 158 VAL A CG1 1 ATOM 916 C CG2 . VAL A 1 117 ? 12.172 31.143 35.273 1.00 30.76 ? 158 VAL A CG2 1 ATOM 917 N N . PRO A 1 118 ? 14.895 29.169 34.072 1.00 31.87 ? 159 PRO A N 1 ATOM 918 C CA . PRO A 1 118 ? 16.087 29.450 33.247 1.00 32.29 ? 159 PRO A CA 1 ATOM 919 C C . PRO A 1 118 ? 16.340 30.952 33.107 1.00 30.66 ? 159 PRO A C 1 ATOM 920 O O . PRO A 1 118 ? 15.420 31.758 33.307 1.00 30.20 ? 159 PRO A O 1 ATOM 921 C CB . PRO A 1 118 ? 15.759 28.783 31.874 1.00 33.41 ? 159 PRO A CB 1 ATOM 922 C CG . PRO A 1 118 ? 14.241 28.734 31.835 1.00 34.98 ? 159 PRO A CG 1 ATOM 923 C CD . PRO A 1 118 ? 13.788 28.567 33.291 1.00 33.18 ? 159 PRO A CD 1 ATOM 924 N N . PRO A 1 119 ? 17.596 31.356 32.830 1.00 30.27 ? 160 PRO A N 1 ATOM 925 C CA . PRO A 1 119 ? 17.869 32.785 32.677 1.00 29.30 ? 160 PRO A CA 1 ATOM 926 C C . PRO A 1 119 ? 16.973 33.415 31.593 1.00 29.01 ? 160 PRO A C 1 ATOM 927 O O . PRO A 1 119 ? 16.789 32.855 30.503 1.00 28.14 ? 160 PRO A O 1 ATOM 928 C CB . PRO A 1 119 ? 19.339 32.815 32.246 1.00 29.65 ? 160 PRO A CB 1 ATOM 929 C CG . PRO A 1 119 ? 19.908 31.551 32.839 1.00 30.15 ? 160 PRO A CG 1 ATOM 930 C CD . PRO A 1 119 ? 18.809 30.534 32.626 1.00 31.29 ? 160 PRO A CD 1 ATOM 931 N N . PHE A 1 120 ? 16.458 34.588 31.894 1.00 27.74 ? 161 PHE A N 1 ATOM 932 C CA . PHE A 1 120 ? 15.620 35.343 30.954 1.00 27.98 ? 161 PHE A CA 1 ATOM 933 C C . PHE A 1 120 ? 15.610 36.755 31.437 1.00 26.61 ? 161 PHE A C 1 ATOM 934 O O . PHE A 1 120 ? 15.941 37.023 32.616 1.00 26.93 ? 161 PHE A O 1 ATOM 935 C CB . PHE A 1 120 ? 14.163 34.785 30.840 1.00 27.04 ? 161 PHE A CB 1 ATOM 936 C CG . PHE A 1 120 ? 13.243 35.101 32.052 1.00 27.97 ? 161 PHE A CG 1 ATOM 937 C CD1 . PHE A 1 120 ? 12.077 35.891 31.899 1.00 25.02 ? 161 PHE A CD1 1 ATOM 938 C CD2 . PHE A 1 120 ? 13.502 34.530 33.309 1.00 27.84 ? 161 PHE A CD2 1 ATOM 939 C CE1 . PHE A 1 120 ? 11.223 36.151 33.008 1.00 23.79 ? 161 PHE A CE1 1 ATOM 940 C CE2 . PHE A 1 120 ? 12.655 34.775 34.434 1.00 28.53 ? 161 PHE A CE2 1 ATOM 941 C CZ . PHE A 1 120 ? 11.517 35.619 34.277 1.00 26.36 ? 161 PHE A CZ 1 ATOM 942 N N . SER A 1 121 ? 15.213 37.657 30.541 1.00 26.46 ? 162 SER A N 1 ATOM 943 C CA . SER A 1 121 ? 15.008 39.052 30.929 1.00 25.52 ? 162 SER A CA 1 ATOM 944 C C . SER A 1 121 ? 13.516 39.286 31.141 1.00 26.00 ? 162 SER A C 1 ATOM 945 O O . SER A 1 121 ? 12.731 39.271 30.164 1.00 26.25 ? 162 SER A O 1 ATOM 946 C CB . SER A 1 121 ? 15.546 40.009 29.853 1.00 26.56 ? 162 SER A CB 1 ATOM 947 O OG . SER A 1 121 ? 16.969 39.853 29.662 1.00 27.28 ? 162 SER A OG 1 ATOM 948 N N . ALA A 1 122 ? 13.107 39.496 32.409 1.00 24.46 ? 163 ALA A N 1 ATOM 949 C CA . ALA A 1 122 ? 11.655 39.603 32.684 1.00 25.27 ? 163 ALA A CA 1 ATOM 950 C C . ALA A 1 122 ? 11.089 40.821 31.999 1.00 25.62 ? 163 ALA A C 1 ATOM 951 O O . ALA A 1 122 ? 11.688 41.912 32.046 1.00 24.86 ? 163 ALA A O 1 ATOM 952 C CB . ALA A 1 122 ? 11.363 39.660 34.210 1.00 23.12 ? 163 ALA A CB 1 ATOM 953 N N . PHE A 1 123 ? 9.939 40.584 31.366 1.00 26.28 ? 164 PHE A N 1 ATOM 954 C CA . PHE A 1 123 ? 9.127 41.558 30.623 1.00 27.01 ? 164 PHE A CA 1 ATOM 955 C C . PHE A 1 123 ? 9.566 41.783 29.170 1.00 27.97 ? 164 PHE A C 1 ATOM 956 O O . PHE A 1 123 ? 8.970 42.617 28.476 1.00 27.65 ? 164 PHE A O 1 ATOM 957 C CB . PHE A 1 123 ? 8.868 42.862 31.379 1.00 26.38 ? 164 PHE A CB 1 ATOM 958 C CG . PHE A 1 123 ? 8.203 42.659 32.727 1.00 25.48 ? 164 PHE A CG 1 ATOM 959 C CD1 . PHE A 1 123 ? 6.787 42.462 32.824 1.00 26.96 ? 164 PHE A CD1 1 ATOM 960 C CD2 . PHE A 1 123 ? 8.968 42.667 33.874 1.00 25.27 ? 164 PHE A CD2 1 ATOM 961 C CE1 . PHE A 1 123 ? 6.145 42.297 34.047 1.00 24.93 ? 164 PHE A CE1 1 ATOM 962 C CE2 . PHE A 1 123 ? 8.372 42.501 35.147 1.00 24.10 ? 164 PHE A CE2 1 ATOM 963 C CZ . PHE A 1 123 ? 6.931 42.318 35.244 1.00 23.41 ? 164 PHE A CZ 1 ATOM 964 N N . SER A 1 124 ? 10.572 41.040 28.705 1.00 26.59 ? 165 SER A N 1 ATOM 965 C CA . SER A 1 124 ? 10.916 41.120 27.283 1.00 29.23 ? 165 SER A CA 1 ATOM 966 C C . SER A 1 124 ? 9.658 40.787 26.468 1.00 29.69 ? 165 SER A C 1 ATOM 967 O O . SER A 1 124 ? 8.941 39.827 26.791 1.00 30.22 ? 165 SER A O 1 ATOM 968 C CB . SER A 1 124 ? 12.038 40.127 26.902 1.00 29.19 ? 165 SER A CB 1 ATOM 969 O OG . SER A 1 124 ? 12.218 40.111 25.465 1.00 30.07 ? 165 SER A OG 1 ATOM 970 N N . PRO A 1 125 ? 9.379 41.581 25.410 1.00 31.83 ? 166 PRO A N 1 ATOM 971 C CA . PRO A 1 125 ? 8.368 41.063 24.478 1.00 32.91 ? 166 PRO A CA 1 ATOM 972 C C . PRO A 1 125 ? 8.858 39.830 23.690 1.00 34.92 ? 166 PRO A C 1 ATOM 973 O O . PRO A 1 125 ? 10.070 39.521 23.679 1.00 33.25 ? 166 PRO A O 1 ATOM 974 C CB . PRO A 1 125 ? 8.174 42.230 23.508 1.00 34.47 ? 166 PRO A CB 1 ATOM 975 C CG . PRO A 1 125 ? 9.527 42.874 23.422 1.00 33.67 ? 166 PRO A CG 1 ATOM 976 C CD . PRO A 1 125 ? 10.037 42.797 24.878 1.00 32.39 ? 166 PRO A CD 1 ATOM 977 N N . GLN A 1 126 ? 7.924 39.141 23.034 1.00 35.16 ? 167 GLN A N 1 ATOM 978 C CA . GLN A 1 126 ? 8.267 38.017 22.179 1.00 36.60 ? 167 GLN A CA 1 ATOM 979 C C . GLN A 1 126 ? 8.798 38.517 20.848 1.00 37.94 ? 167 GLN A C 1 ATOM 980 O O . GLN A 1 126 ? 8.482 39.628 20.436 1.00 39.02 ? 167 GLN A O 1 ATOM 981 C CB . GLN A 1 126 ? 7.029 37.188 21.916 1.00 38.07 ? 167 GLN A CB 1 ATOM 982 C CG . GLN A 1 126 ? 6.346 36.739 23.209 1.00 39.79 ? 167 GLN A CG 1 ATOM 983 C CD . GLN A 1 126 ? 5.310 35.685 22.926 1.00 45.99 ? 167 GLN A CD 1 ATOM 984 O OE1 . GLN A 1 126 ? 5.008 35.433 21.782 1.00 51.39 ? 167 GLN A OE1 1 ATOM 985 N NE2 . GLN A 1 126 ? 4.798 35.038 23.956 1.00 46.00 ? 167 GLN A NE2 1 ATOM 986 N N . GLY A 1 127 ? 9.628 37.719 20.190 1.00 39.96 ? 168 GLY A N 1 ATOM 987 C CA . GLY A 1 127 ? 10.026 38.045 18.817 1.00 41.23 ? 168 GLY A CA 1 ATOM 988 C C . GLY A 1 127 ? 11.157 37.131 18.405 1.00 43.06 ? 168 GLY A C 1 ATOM 989 O O . GLY A 1 127 ? 11.772 36.457 19.247 1.00 42.46 ? 168 GLY A O 1 ATOM 990 N N . MET A 1 128 ? 11.416 37.089 17.101 1.00 44.75 ? 169 MET A N 1 ATOM 991 C CA . MET A 1 128 ? 12.566 36.382 16.599 1.00 45.76 ? 169 MET A CA 1 ATOM 992 C C . MET A 1 128 ? 13.392 37.284 15.688 1.00 45.91 ? 169 MET A C 1 ATOM 993 O O . MET A 1 128 ? 13.677 36.885 14.550 1.00 47.44 ? 169 MET A O 1 ATOM 994 C CB . MET A 1 128 ? 12.126 35.105 15.870 1.00 47.98 ? 169 MET A CB 1 ATOM 995 C CG . MET A 1 128 ? 11.335 34.131 16.734 1.00 53.14 ? 169 MET A CG 1 ATOM 996 S SD . MET A 1 128 ? 10.992 32.593 15.845 1.00 68.81 ? 169 MET A SD 1 ATOM 997 C CE . MET A 1 128 ? 9.525 31.990 16.696 1.00 66.45 ? 169 MET A CE 1 ATOM 998 N N . PRO A 1 129 ? 13.823 38.470 16.173 1.00 44.99 ? 170 PRO A N 1 ATOM 999 C CA . PRO A 1 129 ? 14.607 39.355 15.299 1.00 46.20 ? 170 PRO A CA 1 ATOM 1000 C C . PRO A 1 129 ? 15.957 38.736 14.899 1.00 48.05 ? 170 PRO A C 1 ATOM 1001 O O . PRO A 1 129 ? 16.555 37.976 15.679 1.00 46.23 ? 170 PRO A O 1 ATOM 1002 C CB . PRO A 1 129 ? 14.829 40.599 16.155 1.00 45.19 ? 170 PRO A CB 1 ATOM 1003 C CG . PRO A 1 129 ? 14.814 40.084 17.567 1.00 43.34 ? 170 PRO A CG 1 ATOM 1004 C CD . PRO A 1 129 ? 13.810 38.959 17.571 1.00 42.96 ? 170 PRO A CD 1 ATOM 1005 N N . GLU A 1 130 ? 16.402 39.062 13.680 1.00 49.72 ? 171 GLU A N 1 ATOM 1006 C CA . GLU A 1 130 ? 17.627 38.528 13.106 1.00 52.03 ? 171 GLU A CA 1 ATOM 1007 C C . GLU A 1 130 ? 18.387 39.696 12.481 1.00 52.62 ? 171 GLU A C 1 ATOM 1008 O O . GLU A 1 130 ? 17.788 40.512 11.779 1.00 54.32 ? 171 GLU A O 1 ATOM 1009 C CB . GLU A 1 130 ? 17.259 37.479 12.057 1.00 53.19 ? 171 GLU A CB 1 ATOM 1010 C CG . GLU A 1 130 ? 18.375 37.065 11.135 1.00 58.76 ? 171 GLU A CG 1 ATOM 1011 C CD . GLU A 1 130 ? 17.837 36.489 9.840 1.00 64.79 ? 171 GLU A CD 1 ATOM 1012 O OE1 . GLU A 1 130 ? 16.813 35.756 9.896 1.00 66.33 ? 171 GLU A OE1 1 ATOM 1013 O OE2 . GLU A 1 130 ? 18.435 36.788 8.780 1.00 67.65 ? 171 GLU A OE2 1 ATOM 1014 N N . GLY A 1 131 ? 19.685 39.814 12.753 1.00 51.84 ? 172 GLY A N 1 ATOM 1015 C CA . GLY A 1 131 ? 20.418 40.987 12.308 1.00 51.17 ? 172 GLY A CA 1 ATOM 1016 C C . GLY A 1 131 ? 21.907 40.931 12.563 1.00 50.83 ? 172 GLY A C 1 ATOM 1017 O O . GLY A 1 131 ? 22.449 39.908 12.981 1.00 50.49 ? 172 GLY A O 1 ATOM 1018 N N . ASP A 1 132 ? 22.565 42.049 12.304 1.00 50.43 ? 173 ASP A N 1 ATOM 1019 C CA . ASP A 1 132 ? 23.981 42.208 12.607 1.00 50.49 ? 173 ASP A CA 1 ATOM 1020 C C . ASP A 1 132 ? 24.163 42.772 14.013 1.00 48.40 ? 173 ASP A C 1 ATOM 1021 O O . ASP A 1 132 ? 23.374 43.608 14.459 1.00 47.09 ? 173 ASP A O 1 ATOM 1022 C CB . ASP A 1 132 ? 24.616 43.146 11.591 1.00 52.21 ? 173 ASP A CB 1 ATOM 1023 C CG . ASP A 1 132 ? 24.518 42.613 10.162 1.00 57.40 ? 173 ASP A CG 1 ATOM 1024 O OD1 . ASP A 1 132 ? 24.755 41.398 9.973 1.00 60.64 ? 173 ASP A OD1 1 ATOM 1025 O OD2 . ASP A 1 132 ? 24.215 43.415 9.242 1.00 59.97 ? 173 ASP A OD2 1 ATOM 1026 N N . LEU A 1 133 ? 25.214 42.312 14.690 1.00 47.08 ? 174 LEU A N 1 ATOM 1027 C CA . LEU A 1 133 ? 25.536 42.754 16.028 1.00 45.47 ? 174 LEU A CA 1 ATOM 1028 C C . LEU A 1 133 ? 26.294 44.082 16.037 1.00 45.55 ? 174 LEU A C 1 ATOM 1029 O O . LEU A 1 133 ? 27.152 44.334 15.196 1.00 46.71 ? 174 LEU A O 1 ATOM 1030 C CB . LEU A 1 133 ? 26.396 41.672 16.707 1.00 45.76 ? 174 LEU A CB 1 ATOM 1031 C CG A LEU A 1 133 ? 26.269 41.251 18.173 0.50 44.32 ? 174 LEU A CG 1 ATOM 1032 C CG B LEU A 1 133 ? 25.760 40.334 17.099 0.50 43.33 ? 174 LEU A CG 1 ATOM 1033 C CD1 A LEU A 1 133 ? 24.837 41.261 18.685 0.50 41.31 ? 174 LEU A CD1 1 ATOM 1034 C CD1 B LEU A 1 133 ? 26.804 39.410 17.703 0.50 40.66 ? 174 LEU A CD1 1 ATOM 1035 C CD2 A LEU A 1 133 ? 26.889 39.861 18.329 0.50 43.87 ? 174 LEU A CD2 1 ATOM 1036 C CD2 B LEU A 1 133 ? 24.615 40.533 18.077 0.50 40.40 ? 174 LEU A CD2 1 ATOM 1037 N N . VAL A 1 134 ? 25.983 44.927 17.016 1.00 44.08 ? 175 VAL A N 1 ATOM 1038 C CA . VAL A 1 134 ? 26.865 46.046 17.349 1.00 43.81 ? 175 VAL A CA 1 ATOM 1039 C C . VAL A 1 134 ? 27.150 45.942 18.848 1.00 42.70 ? 175 VAL A C 1 ATOM 1040 O O . VAL A 1 134 ? 26.224 45.700 19.650 1.00 40.73 ? 175 VAL A O 1 ATOM 1041 C CB . VAL A 1 134 ? 26.215 47.423 17.007 1.00 44.81 ? 175 VAL A CB 1 ATOM 1042 C CG1 . VAL A 1 134 ? 26.996 48.598 17.622 1.00 43.84 ? 175 VAL A CG1 1 ATOM 1043 C CG2 . VAL A 1 134 ? 26.127 47.593 15.510 1.00 44.25 ? 175 VAL A CG2 1 ATOM 1044 N N . TYR A 1 135 ? 28.418 46.115 19.213 1.00 41.81 ? 176 TYR A N 1 ATOM 1045 C CA . TYR A 1 135 ? 28.841 46.037 20.606 1.00 40.84 ? 176 TYR A CA 1 ATOM 1046 C C . TYR A 1 135 ? 28.859 47.441 21.173 1.00 40.73 ? 176 TYR A C 1 ATOM 1047 O O . TYR A 1 135 ? 29.485 48.343 20.594 1.00 40.95 ? 176 TYR A O 1 ATOM 1048 C CB . TYR A 1 135 ? 30.221 45.362 20.714 1.00 42.30 ? 176 TYR A CB 1 ATOM 1049 C CG . TYR A 1 135 ? 30.858 45.509 22.083 1.00 40.73 ? 176 TYR A CG 1 ATOM 1050 C CD1 . TYR A 1 135 ? 30.287 44.918 23.210 1.00 39.40 ? 176 TYR A CD1 1 ATOM 1051 C CD2 . TYR A 1 135 ? 32.053 46.234 22.241 1.00 42.31 ? 176 TYR A CD2 1 ATOM 1052 C CE1 . TYR A 1 135 ? 30.877 45.069 24.499 1.00 38.94 ? 176 TYR A CE1 1 ATOM 1053 C CE2 . TYR A 1 135 ? 32.640 46.397 23.516 1.00 40.28 ? 176 TYR A CE2 1 ATOM 1054 C CZ . TYR A 1 135 ? 32.060 45.798 24.628 1.00 37.46 ? 176 TYR A CZ 1 ATOM 1055 O OH . TYR A 1 135 ? 32.658 45.925 25.880 1.00 39.91 ? 176 TYR A OH 1 ATOM 1056 N N . VAL A 1 136 ? 28.157 47.629 22.295 1.00 38.90 ? 177 VAL A N 1 ATOM 1057 C CA . VAL A 1 136 ? 27.903 48.984 22.805 1.00 39.58 ? 177 VAL A CA 1 ATOM 1058 C C . VAL A 1 136 ? 28.466 49.181 24.210 1.00 38.83 ? 177 VAL A C 1 ATOM 1059 O O . VAL A 1 136 ? 27.987 50.045 24.995 1.00 37.56 ? 177 VAL A O 1 ATOM 1060 C CB . VAL A 1 136 ? 26.388 49.337 22.736 1.00 38.54 ? 177 VAL A CB 1 ATOM 1061 C CG1 . VAL A 1 136 ? 25.890 49.228 21.309 1.00 39.96 ? 177 VAL A CG1 1 ATOM 1062 C CG2 . VAL A 1 136 ? 25.561 48.398 23.619 1.00 39.33 ? 177 VAL A CG2 1 ATOM 1063 N N . ASN A 1 137 ? 29.493 48.388 24.530 1.00 38.45 ? 178 ASN A N 1 ATOM 1064 C CA . ASN A 1 137 ? 30.123 48.467 25.842 1.00 38.71 ? 178 ASN A CA 1 ATOM 1065 C C . ASN A 1 137 ? 29.066 48.225 26.952 1.00 36.83 ? 178 ASN A C 1 ATOM 1066 O O . ASN A 1 137 ? 28.363 47.195 26.899 1.00 35.65 ? 178 ASN A O 1 ATOM 1067 C CB . ASN A 1 137 ? 30.903 49.796 25.997 1.00 38.90 ? 178 ASN A CB 1 ATOM 1068 C CG . ASN A 1 137 ? 31.916 49.761 27.127 1.00 39.95 ? 178 ASN A CG 1 ATOM 1069 O OD1 . ASN A 1 137 ? 32.440 48.699 27.494 1.00 40.00 ? 178 ASN A OD1 1 ATOM 1070 N ND2 . ASN A 1 137 ? 32.249 50.941 27.648 1.00 40.36 ? 178 ASN A ND2 1 ATOM 1071 N N . TYR A 1 138 ? 28.943 49.133 27.936 1.00 35.65 ? 179 TYR A N 1 ATOM 1072 C CA . TYR A 1 138 ? 27.916 48.984 28.992 1.00 34.59 ? 179 TYR A CA 1 ATOM 1073 C C . TYR A 1 138 ? 26.523 49.523 28.613 1.00 34.06 ? 179 TYR A C 1 ATOM 1074 O O . TYR A 1 138 ? 25.575 49.510 29.435 1.00 33.30 ? 179 TYR A O 1 ATOM 1075 C CB . TYR A 1 138 ? 28.375 49.683 30.289 1.00 34.01 ? 179 TYR A CB 1 ATOM 1076 C CG . TYR A 1 138 ? 29.631 49.088 30.904 1.00 35.47 ? 179 TYR A CG 1 ATOM 1077 C CD1 . TYR A 1 138 ? 29.570 47.895 31.632 1.00 35.92 ? 179 TYR A CD1 1 ATOM 1078 C CD2 . TYR A 1 138 ? 30.871 49.757 30.812 1.00 35.93 ? 179 TYR A CD2 1 ATOM 1079 C CE1 . TYR A 1 138 ? 30.712 47.341 32.242 1.00 35.97 ? 179 TYR A CE1 1 ATOM 1080 C CE2 . TYR A 1 138 ? 32.021 49.216 31.421 1.00 38.61 ? 179 TYR A CE2 1 ATOM 1081 C CZ . TYR A 1 138 ? 31.928 48.013 32.143 1.00 37.92 ? 179 TYR A CZ 1 ATOM 1082 O OH . TYR A 1 138 ? 33.028 47.440 32.761 1.00 38.29 ? 179 TYR A OH 1 ATOM 1083 N N . ALA A 1 139 ? 26.399 49.995 27.372 1.00 35.32 ? 180 ALA A N 1 ATOM 1084 C CA . ALA A 1 139 ? 25.148 50.569 26.854 1.00 33.82 ? 180 ALA A CA 1 ATOM 1085 C C . ALA A 1 139 ? 24.697 51.768 27.706 1.00 33.75 ? 180 ALA A C 1 ATOM 1086 O O . ALA A 1 139 ? 23.481 52.029 27.859 1.00 31.54 ? 180 ALA A O 1 ATOM 1087 C CB . ALA A 1 139 ? 24.022 49.482 26.748 1.00 33.70 ? 180 ALA A CB 1 ATOM 1088 N N . ARG A 1 140 ? 25.676 52.505 28.250 1.00 33.92 ? 181 ARG A N 1 ATOM 1089 C CA . ARG A 1 140 ? 25.361 53.719 29.028 1.00 33.63 ? 181 ARG A CA 1 ATOM 1090 C C . ARG A 1 140 ? 25.037 54.845 28.059 1.00 34.01 ? 181 ARG A C 1 ATOM 1091 O O . ARG A 1 140 ? 25.349 54.764 26.864 1.00 34.67 ? 181 ARG A O 1 ATOM 1092 C CB . ARG A 1 140 ? 26.534 54.106 29.910 1.00 33.48 ? 181 ARG A CB 1 ATOM 1093 C CG . ARG A 1 140 ? 26.831 53.082 31.005 1.00 33.20 ? 181 ARG A CG 1 ATOM 1094 C CD . ARG A 1 140 ? 28.174 53.333 31.640 1.00 36.62 ? 181 ARG A CD 1 ATOM 1095 N NE . ARG A 1 140 ? 29.239 53.308 30.634 1.00 36.00 ? 181 ARG A NE 1 ATOM 1096 C CZ . ARG A 1 140 ? 30.535 53.481 30.876 1.00 38.43 ? 181 ARG A CZ 1 ATOM 1097 N NH1 . ARG A 1 140 ? 30.981 53.691 32.112 1.00 37.97 ? 181 ARG A NH1 1 ATOM 1098 N NH2 . ARG A 1 140 ? 31.387 53.446 29.864 1.00 36.67 ? 181 ARG A NH2 1 ATOM 1099 N N . THR A 1 141 ? 24.403 55.910 28.555 1.00 33.63 ? 182 THR A N 1 ATOM 1100 C CA . THR A 1 141 ? 24.169 57.088 27.717 1.00 34.82 ? 182 THR A CA 1 ATOM 1101 C C . THR A 1 141 ? 25.461 57.545 27.029 1.00 36.20 ? 182 THR A C 1 ATOM 1102 O O . THR A 1 141 ? 25.470 57.812 25.814 1.00 36.98 ? 182 THR A O 1 ATOM 1103 C CB . THR A 1 141 ? 23.573 58.234 28.556 1.00 35.55 ? 182 THR A CB 1 ATOM 1104 O OG1 . THR A 1 141 ? 22.327 57.775 29.072 1.00 33.52 ? 182 THR A OG1 1 ATOM 1105 C CG2 . THR A 1 141 ? 23.321 59.447 27.694 1.00 36.39 ? 182 THR A CG2 1 ATOM 1106 N N . GLU A 1 142 ? 26.566 57.611 27.774 1.00 36.58 ? 183 GLU A N 1 ATOM 1107 C CA . GLU A 1 142 ? 27.814 58.106 27.166 1.00 39.31 ? 183 GLU A CA 1 ATOM 1108 C C . GLU A 1 142 ? 28.398 57.108 26.157 1.00 39.37 ? 183 GLU A C 1 ATOM 1109 O O . GLU A 1 142 ? 29.079 57.522 25.221 1.00 39.63 ? 183 GLU A O 1 ATOM 1110 C CB . GLU A 1 142 ? 28.862 58.441 28.227 1.00 40.77 ? 183 GLU A CB 1 ATOM 1111 C CG . GLU A 1 142 ? 29.219 57.254 29.144 1.00 43.32 ? 183 GLU A CG 1 ATOM 1112 C CD . GLU A 1 142 ? 28.416 57.227 30.463 1.00 47.55 ? 183 GLU A CD 1 ATOM 1113 O OE1 . GLU A 1 142 ? 27.161 57.502 30.507 1.00 43.90 ? 183 GLU A OE1 1 ATOM 1114 O OE2 . GLU A 1 142 ? 29.063 56.893 31.476 1.00 47.64 ? 183 GLU A OE2 1 ATOM 1115 N N . ASP A 1 143 ? 28.130 55.803 26.336 1.00 38.71 ? 184 ASP A N 1 ATOM 1116 C CA . ASP A 1 143 ? 28.598 54.796 25.327 1.00 39.86 ? 184 ASP A CA 1 ATOM 1117 C C . ASP A 1 143 ? 27.859 55.007 23.989 1.00 39.96 ? 184 ASP A C 1 ATOM 1118 O O . ASP A 1 143 ? 28.461 54.946 22.930 1.00 40.34 ? 184 ASP A O 1 ATOM 1119 C CB . ASP A 1 143 ? 28.399 53.338 25.825 1.00 39.07 ? 184 ASP A CB 1 ATOM 1120 C CG . ASP A 1 143 ? 29.149 53.046 27.104 1.00 38.10 ? 184 ASP A CG 1 ATOM 1121 O OD1 . ASP A 1 143 ? 30.330 53.483 27.248 1.00 39.06 ? 184 ASP A OD1 1 ATOM 1122 O OD2 . ASP A 1 143 ? 28.566 52.360 27.977 1.00 36.58 ? 184 ASP A OD2 1 ATOM 1123 N N . PHE A 1 144 ? 26.554 55.264 24.052 1.00 39.51 ? 185 PHE A N 1 ATOM 1124 C CA . PHE A 1 144 ? 25.771 55.550 22.849 1.00 39.68 ? 185 PHE A CA 1 ATOM 1125 C C . PHE A 1 144 ? 26.152 56.880 22.198 1.00 41.70 ? 185 PHE A C 1 ATOM 1126 O O . PHE A 1 144 ? 26.152 56.983 20.953 1.00 42.21 ? 185 PHE A O 1 ATOM 1127 C CB . PHE A 1 144 ? 24.264 55.456 23.118 1.00 38.76 ? 185 PHE A CB 1 ATOM 1128 C CG . PHE A 1 144 ? 23.740 54.039 23.085 1.00 36.32 ? 185 PHE A CG 1 ATOM 1129 C CD1 . PHE A 1 144 ? 23.502 53.349 24.264 1.00 35.13 ? 185 PHE A CD1 1 ATOM 1130 C CD2 . PHE A 1 144 ? 23.541 53.380 21.858 1.00 37.20 ? 185 PHE A CD2 1 ATOM 1131 C CE1 . PHE A 1 144 ? 23.033 52.032 24.238 1.00 37.30 ? 185 PHE A CE1 1 ATOM 1132 C CE2 . PHE A 1 144 ? 23.092 52.041 21.808 1.00 36.05 ? 185 PHE A CE2 1 ATOM 1133 C CZ . PHE A 1 144 ? 22.832 51.368 23.008 1.00 36.02 ? 185 PHE A CZ 1 ATOM 1134 N N . PHE A 1 145 ? 26.508 57.881 23.014 1.00 41.94 ? 186 PHE A N 1 ATOM 1135 C CA . PHE A 1 145 ? 27.003 59.168 22.481 1.00 43.57 ? 186 PHE A CA 1 ATOM 1136 C C . PHE A 1 145 ? 28.292 58.931 21.679 1.00 46.02 ? 186 PHE A C 1 ATOM 1137 O O . PHE A 1 145 ? 28.434 59.438 20.561 1.00 47.05 ? 186 PHE A O 1 ATOM 1138 C CB . PHE A 1 145 ? 27.318 60.176 23.593 1.00 43.35 ? 186 PHE A CB 1 ATOM 1139 C CG . PHE A 1 145 ? 26.117 60.878 24.170 1.00 43.20 ? 186 PHE A CG 1 ATOM 1140 C CD1 . PHE A 1 145 ? 24.875 60.854 23.533 1.00 45.18 ? 186 PHE A CD1 1 ATOM 1141 C CD2 . PHE A 1 145 ? 26.241 61.590 25.366 1.00 44.27 ? 186 PHE A CD2 1 ATOM 1142 C CE1 . PHE A 1 145 ? 23.754 61.534 24.084 1.00 44.94 ? 186 PHE A CE1 1 ATOM 1143 C CE2 . PHE A 1 145 ? 25.122 62.273 25.932 1.00 40.22 ? 186 PHE A CE2 1 ATOM 1144 C CZ . PHE A 1 145 ? 23.888 62.240 25.281 1.00 42.00 ? 186 PHE A CZ 1 ATOM 1145 N N . LYS A 1 146 ? 29.217 58.168 22.267 1.00 47.10 ? 187 LYS A N 1 ATOM 1146 C CA . LYS A 1 146 ? 30.510 57.816 21.645 1.00 49.11 ? 187 LYS A CA 1 ATOM 1147 C C . LYS A 1 146 ? 30.332 57.086 20.306 1.00 50.40 ? 187 LYS A C 1 ATOM 1148 O O . LYS A 1 146 ? 30.980 57.434 19.313 1.00 51.53 ? 187 LYS A O 1 ATOM 1149 C CB . LYS A 1 146 ? 31.354 56.975 22.621 1.00 49.33 ? 187 LYS A CB 1 ATOM 1150 C CG . LYS A 1 146 ? 32.750 56.500 22.109 1.00 53.49 ? 187 LYS A CG 1 ATOM 1151 C CD . LYS A 1 146 ? 33.890 57.480 22.462 1.00 60.69 ? 187 LYS A CD 1 ATOM 1152 C CE . LYS A 1 146 ? 34.343 57.268 23.920 1.00 62.90 ? 187 LYS A CE 1 ATOM 1153 N NZ . LYS A 1 146 ? 35.023 58.463 24.509 1.00 65.86 ? 187 LYS A NZ 1 ATOM 1154 N N . LEU A 1 147 ? 29.462 56.077 20.289 1.00 50.17 ? 188 LEU A N 1 ATOM 1155 C CA . LEU A 1 147 ? 29.165 55.311 19.085 1.00 51.97 ? 188 LEU A CA 1 ATOM 1156 C C . LEU A 1 147 ? 28.620 56.190 17.992 1.00 52.96 ? 188 LEU A C 1 ATOM 1157 O O . LEU A 1 147 ? 29.144 56.200 16.869 1.00 52.58 ? 188 LEU A O 1 ATOM 1158 C CB . LEU A 1 147 ? 28.109 54.246 19.381 1.00 51.64 ? 188 LEU A CB 1 ATOM 1159 C CG . LEU A 1 147 ? 28.506 52.803 19.623 1.00 54.06 ? 188 LEU A CG 1 ATOM 1160 C CD1 . LEU A 1 147 ? 27.206 52.062 19.872 1.00 56.97 ? 188 LEU A CD1 1 ATOM 1161 C CD2 . LEU A 1 147 ? 29.200 52.226 18.443 1.00 55.15 ? 188 LEU A CD2 1 ATOM 1162 N N . GLU A 1 148 ? 27.583 56.947 18.342 1.00 52.09 ? 189 GLU A N 1 ATOM 1163 C CA . GLU A 1 148 ? 26.743 57.635 17.371 1.00 54.61 ? 189 GLU A CA 1 ATOM 1164 C C . GLU A 1 148 ? 27.341 58.982 16.940 1.00 55.66 ? 189 GLU A C 1 ATOM 1165 O O . GLU A 1 148 ? 27.402 59.286 15.738 1.00 57.33 ? 189 GLU A O 1 ATOM 1166 C CB . GLU A 1 148 ? 25.299 57.756 17.908 1.00 54.58 ? 189 GLU A CB 1 ATOM 1167 C CG . GLU A 1 148 ? 24.645 56.361 18.187 1.00 59.06 ? 189 GLU A CG 1 ATOM 1168 C CD . GLU A 1 148 ? 23.231 56.437 18.783 1.00 63.41 ? 189 GLU A CD 1 ATOM 1169 O OE1 . GLU A 1 148 ? 23.060 56.955 19.911 1.00 65.29 ? 189 GLU A OE1 1 ATOM 1170 O OE2 . GLU A 1 148 ? 22.281 55.969 18.111 1.00 66.46 ? 189 GLU A OE2 1 ATOM 1171 N N . ARG A 1 149 ? 27.837 59.748 17.911 1.00 55.02 ? 190 ARG A N 1 ATOM 1172 C CA . ARG A 1 149 ? 28.341 61.102 17.662 1.00 56.18 ? 190 ARG A CA 1 ATOM 1173 C C . ARG A 1 149 ? 29.808 61.119 17.230 1.00 58.19 ? 190 ARG A C 1 ATOM 1174 O O . ARG A 1 149 ? 30.180 61.887 16.339 1.00 59.70 ? 190 ARG A O 1 ATOM 1175 C CB . ARG A 1 149 ? 28.109 62.015 18.886 1.00 54.87 ? 190 ARG A CB 1 ATOM 1176 C CG . ARG A 1 149 ? 26.631 62.183 19.240 1.00 52.44 ? 190 ARG A CG 1 ATOM 1177 C CD . ARG A 1 149 ? 26.441 62.891 20.575 1.00 51.12 ? 190 ARG A CD 1 ATOM 1178 N NE . ARG A 1 149 ? 25.027 63.194 20.815 1.00 50.81 ? 190 ARG A NE 1 ATOM 1179 C CZ . ARG A 1 149 ? 24.589 64.015 21.776 1.00 50.88 ? 190 ARG A CZ 1 ATOM 1180 N NH1 . ARG A 1 149 ? 25.453 64.590 22.605 1.00 47.70 ? 190 ARG A NH1 1 ATOM 1181 N NH2 . ARG A 1 149 ? 23.290 64.252 21.915 1.00 48.65 ? 190 ARG A NH2 1 ATOM 1182 N N . ASP A 1 150 ? 30.633 60.269 17.848 1.00 58.40 ? 191 ASP A N 1 ATOM 1183 C CA . ASP A 1 150 ? 32.075 60.251 17.564 1.00 60.15 ? 191 ASP A CA 1 ATOM 1184 C C . ASP A 1 150 ? 32.482 59.222 16.507 1.00 60.37 ? 191 ASP A C 1 ATOM 1185 O O . ASP A 1 150 ? 33.273 59.524 15.618 1.00 61.09 ? 191 ASP A O 1 ATOM 1186 C CB . ASP A 1 150 ? 32.889 60.026 18.849 1.00 60.39 ? 191 ASP A CB 1 ATOM 1187 C CG . ASP A 1 150 ? 32.612 61.076 19.911 1.00 63.00 ? 191 ASP A CG 1 ATOM 1188 O OD1 . ASP A 1 150 ? 32.319 62.239 19.545 1.00 66.65 ? 191 ASP A OD1 1 ATOM 1189 O OD2 . ASP A 1 150 ? 32.673 60.734 21.116 1.00 65.94 ? 191 ASP A OD2 1 ATOM 1190 N N . MET A 1 151 ? 31.950 58.008 16.620 1.00 58.66 ? 192 MET A N 1 ATOM 1191 C CA . MET A 1 151 ? 32.332 56.918 15.725 1.00 59.36 ? 192 MET A CA 1 ATOM 1192 C C . MET A 1 151 ? 31.439 56.851 14.487 1.00 59.59 ? 192 MET A C 1 ATOM 1193 O O . MET A 1 151 ? 31.806 56.196 13.491 1.00 59.29 ? 192 MET A O 1 ATOM 1194 C CB . MET A 1 151 ? 32.330 55.572 16.460 1.00 58.52 ? 192 MET A CB 1 ATOM 1195 C CG . MET A 1 151 ? 33.362 55.455 17.579 1.00 58.91 ? 192 MET A CG 1 ATOM 1196 S SD . MET A 1 151 ? 33.206 53.856 18.399 1.00 59.33 ? 192 MET A SD 1 ATOM 1197 C CE . MET A 1 151 ? 34.308 52.885 17.343 1.00 58.98 ? 192 MET A CE 1 ATOM 1198 N N . LYS A 1 152 ? 30.293 57.538 14.561 1.00 57.98 ? 193 LYS A N 1 ATOM 1199 C CA . LYS A 1 152 ? 29.276 57.594 13.496 1.00 59.20 ? 193 LYS A CA 1 ATOM 1200 C C . LYS A 1 152 ? 28.764 56.216 13.110 1.00 59.06 ? 193 LYS A C 1 ATOM 1201 O O . LYS A 1 152 ? 28.573 55.916 11.919 1.00 60.08 ? 193 LYS A O 1 ATOM 1202 C CB . LYS A 1 152 ? 29.780 58.368 12.259 1.00 61.75 ? 193 LYS A CB 1 ATOM 1203 C CG . LYS A 1 152 ? 29.588 59.874 12.378 1.00 64.31 ? 193 LYS A CG 1 ATOM 1204 C CD . LYS A 1 152 ? 30.640 60.508 13.282 1.00 66.27 ? 193 LYS A CD 1 ATOM 1205 C CE . LYS A 1 152 ? 30.811 61.998 12.975 1.00 68.40 ? 193 LYS A CE 1 ATOM 1206 N NZ . LYS A 1 152 ? 29.633 62.780 13.453 1.00 67.28 ? 193 LYS A NZ 1 ATOM 1207 N N . ILE A 1 153 ? 28.574 55.374 14.124 1.00 57.43 ? 194 ILE A N 1 ATOM 1208 C CA . ILE A 1 153 ? 28.016 54.039 13.942 1.00 57.96 ? 194 ILE A CA 1 ATOM 1209 C C . ILE A 1 153 ? 26.522 54.101 14.222 1.00 57.58 ? 194 ILE A C 1 ATOM 1210 O O . ILE A 1 153 ? 26.093 54.615 15.259 1.00 56.79 ? 194 ILE A O 1 ATOM 1211 C CB . ILE A 1 153 ? 28.768 52.966 14.790 1.00 57.38 ? 194 ILE A CB 1 ATOM 1212 C CG1 . ILE A 1 153 ? 30.073 52.574 14.089 1.00 59.56 ? 194 ILE A CG1 1 ATOM 1213 C CG2 . ILE A 1 153 ? 27.925 51.694 14.951 1.00 56.93 ? 194 ILE A CG2 1 ATOM 1214 C CD1 . ILE A 1 153 ? 31.229 52.176 14.999 1.00 58.70 ? 194 ILE A CD1 1 ATOM 1215 N N . ASN A 1 154 ? 25.730 53.618 13.276 1.00 58.88 ? 195 ASN A N 1 ATOM 1216 C CA . ASN A 1 154 ? 24.276 53.698 13.363 1.00 59.64 ? 195 ASN A CA 1 ATOM 1217 C C . ASN A 1 154 ? 23.696 52.376 13.926 1.00 57.88 ? 195 ASN A C 1 ATOM 1218 O O . ASN A 1 154 ? 23.863 51.308 13.303 1.00 56.95 ? 195 ASN A O 1 ATOM 1219 C CB . ASN A 1 154 ? 23.713 54.056 11.972 1.00 62.33 ? 195 ASN A CB 1 ATOM 1220 C CG . ASN A 1 154 ? 22.213 54.327 11.978 1.00 67.64 ? 195 ASN A CG 1 ATOM 1221 O OD1 . ASN A 1 154 ? 21.574 54.350 13.035 1.00 67.87 ? 195 ASN A OD1 1 ATOM 1222 N ND2 . ASN A 1 154 ? 21.641 54.523 10.780 1.00 78.41 ? 195 ASN A ND2 1 ATOM 1223 N N . CYS A 1 155 ? 23.053 52.447 15.108 1.00 54.98 ? 196 CYS A N 1 ATOM 1224 C CA . CYS A 1 155 ? 22.438 51.254 15.723 1.00 54.07 ? 196 CYS A CA 1 ATOM 1225 C C . CYS A 1 155 ? 21.071 50.880 15.172 1.00 53.62 ? 196 CYS A C 1 ATOM 1226 O O . CYS A 1 155 ? 20.515 49.841 15.547 1.00 53.24 ? 196 CYS A O 1 ATOM 1227 C CB . CYS A 1 155 ? 22.352 51.357 17.256 1.00 52.56 ? 196 CYS A CB 1 ATOM 1228 S SG . CYS A 1 155 ? 23.950 51.221 18.016 1.00 54.62 ? 196 CYS A SG 1 ATOM 1229 N N . SER A 1 156 ? 20.527 51.702 14.282 1.00 53.94 ? 197 SER A N 1 ATOM 1230 C CA . SER A 1 156 ? 19.186 51.451 13.773 1.00 53.78 ? 197 SER A CA 1 ATOM 1231 C C . SER A 1 156 ? 19.072 50.105 13.051 1.00 53.47 ? 197 SER A C 1 ATOM 1232 O O . SER A 1 156 ? 19.858 49.802 12.153 1.00 55.03 ? 197 SER A O 1 ATOM 1233 C CB . SER A 1 156 ? 18.719 52.600 12.884 1.00 55.07 ? 197 SER A CB 1 ATOM 1234 O OG . SER A 1 156 ? 17.415 52.336 12.400 1.00 56.95 ? 197 SER A OG 1 ATOM 1235 N N . GLY A 1 157 ? 18.110 49.281 13.471 1.00 51.37 ? 198 GLY A N 1 ATOM 1236 C CA . GLY A 1 157 ? 17.904 47.962 12.853 1.00 50.30 ? 198 GLY A CA 1 ATOM 1237 C C . GLY A 1 157 ? 18.944 46.896 13.198 1.00 49.61 ? 198 GLY A C 1 ATOM 1238 O O . GLY A 1 157 ? 18.895 45.802 12.652 1.00 49.85 ? 198 GLY A O 1 ATOM 1239 N N . LYS A 1 158 ? 19.871 47.198 14.120 1.00 48.61 ? 199 LYS A N 1 ATOM 1240 C CA . LYS A 1 158 ? 20.904 46.227 14.550 1.00 47.54 ? 199 LYS A CA 1 ATOM 1241 C C . LYS A 1 158 ? 20.458 45.519 15.833 1.00 45.69 ? 199 LYS A C 1 ATOM 1242 O O . LYS A 1 158 ? 19.561 46.007 16.519 1.00 43.51 ? 199 LYS A O 1 ATOM 1243 C CB . LYS A 1 158 ? 22.219 46.943 14.864 1.00 47.99 ? 199 LYS A CB 1 ATOM 1244 C CG . LYS A 1 158 ? 22.667 47.954 13.819 1.00 51.58 ? 199 LYS A CG 1 ATOM 1245 C CD . LYS A 1 158 ? 22.872 47.336 12.475 1.00 56.41 ? 199 LYS A CD 1 ATOM 1246 C CE . LYS A 1 158 ? 23.255 48.421 11.483 1.00 59.32 ? 199 LYS A CE 1 ATOM 1247 N NZ . LYS A 1 158 ? 22.965 47.911 10.138 1.00 61.74 ? 199 LYS A NZ 1 ATOM 1248 N N . ILE A 1 159 ? 21.070 44.372 16.135 1.00 44.91 ? 200 ILE A N 1 ATOM 1249 C CA . ILE A 1 159 ? 20.988 43.772 17.487 1.00 43.76 ? 200 ILE A CA 1 ATOM 1250 C C . ILE A 1 159 ? 22.150 44.297 18.315 1.00 42.72 ? 200 ILE A C 1 ATOM 1251 O O . ILE A 1 159 ? 23.301 44.213 17.885 1.00 44.20 ? 200 ILE A O 1 ATOM 1252 C CB . ILE A 1 159 ? 21.007 42.236 17.430 1.00 43.66 ? 200 ILE A CB 1 ATOM 1253 C CG1 . ILE A 1 159 ? 19.761 41.771 16.673 1.00 45.56 ? 200 ILE A CG1 1 ATOM 1254 C CG2 . ILE A 1 159 ? 21.032 41.655 18.852 1.00 43.07 ? 200 ILE A CG2 1 ATOM 1255 C CD1 . ILE A 1 159 ? 19.710 40.308 16.364 1.00 46.79 ? 200 ILE A CD1 1 ATOM 1256 N N . VAL A 1 160 ? 21.869 44.863 19.479 1.00 40.65 ? 201 VAL A N 1 ATOM 1257 C CA . VAL A 1 160 ? 22.955 45.404 20.291 1.00 40.44 ? 201 VAL A CA 1 ATOM 1258 C C . VAL A 1 160 ? 23.412 44.309 21.282 1.00 39.30 ? 201 VAL A C 1 ATOM 1259 O O . VAL A 1 160 ? 22.570 43.590 21.850 1.00 38.39 ? 201 VAL A O 1 ATOM 1260 C CB . VAL A 1 160 ? 22.516 46.767 20.972 1.00 40.76 ? 201 VAL A CB 1 ATOM 1261 C CG1 A VAL A 1 160 ? 22.262 47.845 19.922 0.50 41.41 ? 201 VAL A CG1 1 ATOM 1262 C CG1 B VAL A 1 160 ? 22.914 46.852 22.441 0.50 37.43 ? 201 VAL A CG1 1 ATOM 1263 C CG2 A VAL A 1 160 ? 21.326 46.580 21.812 0.50 38.15 ? 201 VAL A CG2 1 ATOM 1264 C CG2 B VAL A 1 160 ? 22.992 47.958 20.146 0.50 42.19 ? 201 VAL A CG2 1 ATOM 1265 N N . ILE A 1 161 ? 24.723 44.166 21.481 1.00 38.67 ? 202 ILE A N 1 ATOM 1266 C CA . ILE A 1 161 ? 25.235 43.332 22.568 1.00 36.88 ? 202 ILE A CA 1 ATOM 1267 C C . ILE A 1 161 ? 25.976 44.221 23.552 1.00 36.99 ? 202 ILE A C 1 ATOM 1268 O O . ILE A 1 161 ? 26.826 45.031 23.174 1.00 37.53 ? 202 ILE A O 1 ATOM 1269 C CB . ILE A 1 161 ? 26.108 42.141 22.079 1.00 38.62 ? 202 ILE A CB 1 ATOM 1270 C CG1 . ILE A 1 161 ? 26.612 41.290 23.250 1.00 36.73 ? 202 ILE A CG1 1 ATOM 1271 C CG2 . ILE A 1 161 ? 27.286 42.610 21.188 1.00 38.85 ? 202 ILE A CG2 1 ATOM 1272 C CD1 . ILE A 1 161 ? 26.980 39.816 22.765 1.00 37.09 ? 202 ILE A CD1 1 ATOM 1273 N N . ALA A 1 162 ? 25.576 44.139 24.812 1.00 34.38 ? 203 ALA A N 1 ATOM 1274 C CA . ALA A 1 162 ? 26.128 45.003 25.820 1.00 34.11 ? 203 ALA A CA 1 ATOM 1275 C C . ALA A 1 162 ? 26.538 44.144 26.980 1.00 33.74 ? 203 ALA A C 1 ATOM 1276 O O . ALA A 1 162 ? 25.843 43.159 27.293 1.00 34.17 ? 203 ALA A O 1 ATOM 1277 C CB . ALA A 1 162 ? 25.048 46.019 26.290 1.00 32.79 ? 203 ALA A CB 1 ATOM 1278 N N . ARG A 1 163 ? 27.603 44.551 27.674 1.00 33.45 ? 204 ARG A N 1 ATOM 1279 C CA . ARG A 1 163 ? 27.933 43.928 28.934 1.00 33.46 ? 204 ARG A CA 1 ATOM 1280 C C . ARG A 1 163 ? 27.192 44.528 30.109 1.00 32.41 ? 204 ARG A C 1 ATOM 1281 O O . ARG A 1 163 ? 26.935 45.744 30.182 1.00 31.14 ? 204 ARG A O 1 ATOM 1282 C CB . ARG A 1 163 ? 29.453 43.875 29.197 1.00 35.73 ? 204 ARG A CB 1 ATOM 1283 C CG . ARG A 1 163 ? 30.181 45.195 28.991 1.00 37.25 ? 204 ARG A CG 1 ATOM 1284 C CD . ARG A 1 163 ? 31.646 45.000 29.406 1.00 41.47 ? 204 ARG A CD 1 ATOM 1285 N NE . ARG A 1 163 ? 32.457 46.192 29.094 1.00 41.62 ? 204 ARG A NE 1 ATOM 1286 C CZ . ARG A 1 163 ? 33.648 46.437 29.631 1.00 42.92 ? 204 ARG A CZ 1 ATOM 1287 N NH1 . ARG A 1 163 ? 34.149 45.603 30.539 1.00 41.79 ? 204 ARG A NH1 1 ATOM 1288 N NH2 . ARG A 1 163 ? 34.330 47.540 29.275 1.00 38.68 ? 204 ARG A NH2 1 ATOM 1289 N N . TYR A 1 164 ? 26.802 43.648 31.026 1.00 30.89 ? 205 TYR A N 1 ATOM 1290 C CA . TYR A 1 164 ? 26.181 44.083 32.262 1.00 31.13 ? 205 TYR A CA 1 ATOM 1291 C C . TYR A 1 164 ? 27.214 44.878 33.064 1.00 31.66 ? 205 TYR A C 1 ATOM 1292 O O . TYR A 1 164 ? 28.421 44.695 32.858 1.00 32.10 ? 205 TYR A O 1 ATOM 1293 C CB . TYR A 1 164 ? 25.855 42.848 33.039 1.00 29.29 ? 205 TYR A CB 1 ATOM 1294 C CG . TYR A 1 164 ? 24.493 42.225 32.837 1.00 29.79 ? 205 TYR A CG 1 ATOM 1295 C CD1 . TYR A 1 164 ? 24.378 40.853 32.568 1.00 28.15 ? 205 TYR A CD1 1 ATOM 1296 C CD2 . TYR A 1 164 ? 23.320 42.974 33.047 1.00 30.01 ? 205 TYR A CD2 1 ATOM 1297 C CE1 . TYR A 1 164 ? 23.125 40.218 32.507 1.00 27.52 ? 205 TYR A CE1 1 ATOM 1298 C CE2 . TYR A 1 164 ? 22.079 42.364 33.000 1.00 28.97 ? 205 TYR A CE2 1 ATOM 1299 C CZ . TYR A 1 164 ? 21.977 41.008 32.736 1.00 30.04 ? 205 TYR A CZ 1 ATOM 1300 O OH . TYR A 1 164 ? 20.723 40.418 32.731 1.00 28.57 ? 205 TYR A OH 1 ATOM 1301 N N . GLY A 1 165 ? 26.739 45.766 33.948 1.00 31.87 ? 206 GLY A N 1 ATOM 1302 C CA . GLY A 1 165 ? 27.596 46.454 34.919 1.00 32.28 ? 206 GLY A CA 1 ATOM 1303 C C . GLY A 1 165 ? 27.360 47.953 34.822 1.00 33.35 ? 206 GLY A C 1 ATOM 1304 O O . GLY A 1 165 ? 26.808 48.448 33.807 1.00 31.84 ? 206 GLY A O 1 ATOM 1305 N N . LYS A 1 166 ? 27.769 48.664 35.880 1.00 32.88 ? 207 LYS A N 1 ATOM 1306 C CA . LYS A 1 166 ? 27.804 50.143 35.904 1.00 33.78 ? 207 LYS A CA 1 ATOM 1307 C C . LYS A 1 166 ? 26.478 50.817 36.089 1.00 32.72 ? 207 LYS A C 1 ATOM 1308 O O . LYS A 1 166 ? 26.393 51.769 36.901 1.00 31.99 ? 207 LYS A O 1 ATOM 1309 C CB . LYS A 1 166 ? 28.474 50.776 34.674 1.00 34.67 ? 207 LYS A CB 1 ATOM 1310 C CG . LYS A 1 166 ? 29.883 50.234 34.364 1.00 38.94 ? 207 LYS A CG 1 ATOM 1311 C CD . LYS A 1 166 ? 30.852 50.609 35.470 1.00 45.57 ? 207 LYS A CD 1 ATOM 1312 C CE . LYS A 1 166 ? 32.272 50.295 35.012 1.00 48.52 ? 207 LYS A CE 1 ATOM 1313 N NZ . LYS A 1 166 ? 33.192 50.235 36.186 1.00 52.33 ? 207 LYS A NZ 1 ATOM 1314 N N . VAL A 1 167 ? 25.459 50.357 35.347 1.00 31.53 ? 208 VAL A N 1 ATOM 1315 C CA . VAL A 1 167 ? 24.114 50.942 35.455 1.00 29.75 ? 208 VAL A CA 1 ATOM 1316 C C . VAL A 1 167 ? 23.039 49.861 35.406 1.00 29.20 ? 208 VAL A C 1 ATOM 1317 O O . VAL A 1 167 ? 23.250 48.760 34.871 1.00 29.07 ? 208 VAL A O 1 ATOM 1318 C CB . VAL A 1 167 ? 23.823 52.032 34.327 1.00 29.46 ? 208 VAL A CB 1 ATOM 1319 C CG1 . VAL A 1 167 ? 24.949 53.132 34.273 1.00 29.76 ? 208 VAL A CG1 1 ATOM 1320 C CG2 . VAL A 1 167 ? 23.667 51.379 32.921 1.00 31.05 ? 208 VAL A CG2 1 ATOM 1321 N N . PHE A 1 168 ? 21.862 50.214 35.920 1.00 26.63 ? 209 PHE A N 1 ATOM 1322 C CA . PHE A 1 168 ? 20.713 49.315 35.869 1.00 27.32 ? 209 PHE A CA 1 ATOM 1323 C C . PHE A 1 168 ? 20.410 48.811 34.444 1.00 27.88 ? 209 PHE A C 1 ATOM 1324 O O . PHE A 1 168 ? 20.380 49.600 33.470 1.00 27.44 ? 209 PHE A O 1 ATOM 1325 C CB . PHE A 1 168 ? 19.469 50.042 36.446 1.00 25.50 ? 209 PHE A CB 1 ATOM 1326 C CG . PHE A 1 168 ? 18.183 49.257 36.308 1.00 28.01 ? 209 PHE A CG 1 ATOM 1327 C CD1 . PHE A 1 168 ? 18.062 48.002 36.923 1.00 26.74 ? 209 PHE A CD1 1 ATOM 1328 C CD2 . PHE A 1 168 ? 17.067 49.823 35.662 1.00 28.28 ? 209 PHE A CD2 1 ATOM 1329 C CE1 . PHE A 1 168 ? 16.896 47.275 36.813 1.00 28.41 ? 209 PHE A CE1 1 ATOM 1330 C CE2 . PHE A 1 168 ? 15.878 49.096 35.532 1.00 30.29 ? 209 PHE A CE2 1 ATOM 1331 C CZ . PHE A 1 168 ? 15.799 47.805 36.118 1.00 29.17 ? 209 PHE A CZ 1 ATOM 1332 N N . ARG A 1 169 ? 20.125 47.500 34.311 1.00 27.12 ? 210 ARG A N 1 ATOM 1333 C CA . ARG A 1 169 ? 19.951 46.932 32.940 1.00 27.13 ? 210 ARG A CA 1 ATOM 1334 C C . ARG A 1 169 ? 18.769 47.512 32.176 1.00 28.08 ? 210 ARG A C 1 ATOM 1335 O O . ARG A 1 169 ? 18.779 47.520 30.943 1.00 28.18 ? 210 ARG A O 1 ATOM 1336 C CB . ARG A 1 169 ? 19.836 45.396 33.005 1.00 26.87 ? 210 ARG A CB 1 ATOM 1337 C CG . ARG A 1 169 ? 18.587 44.921 33.715 1.00 25.69 ? 210 ARG A CG 1 ATOM 1338 C CD . ARG A 1 169 ? 18.590 43.343 33.947 1.00 25.79 ? 210 ARG A CD 1 ATOM 1339 N NE . ARG A 1 169 ? 19.336 42.954 35.171 1.00 25.33 ? 210 ARG A NE 1 ATOM 1340 C CZ . ARG A 1 169 ? 18.919 43.200 36.424 1.00 28.51 ? 210 ARG A CZ 1 ATOM 1341 N NH1 . ARG A 1 169 ? 17.748 43.789 36.626 1.00 25.87 ? 210 ARG A NH1 1 ATOM 1342 N NH2 . ARG A 1 169 ? 19.641 42.816 37.487 1.00 27.34 ? 210 ARG A NH2 1 ATOM 1343 N N . GLY A 1 170 ? 17.727 47.942 32.897 1.00 26.50 ? 211 GLY A N 1 ATOM 1344 C CA . GLY A 1 170 ? 16.585 48.621 32.268 1.00 28.54 ? 211 GLY A CA 1 ATOM 1345 C C . GLY A 1 170 ? 17.004 49.893 31.518 1.00 28.59 ? 211 GLY A C 1 ATOM 1346 O O . GLY A 1 170 ? 16.474 50.193 30.442 1.00 28.87 ? 211 GLY A O 1 ATOM 1347 N N . ASN A 1 171 ? 17.959 50.629 32.091 1.00 27.95 ? 212 ASN A N 1 ATOM 1348 C CA . ASN A 1 171 ? 18.477 51.829 31.413 1.00 29.25 ? 212 ASN A CA 1 ATOM 1349 C C . ASN A 1 171 ? 19.230 51.461 30.167 1.00 30.18 ? 212 ASN A C 1 ATOM 1350 O O . ASN A 1 171 ? 19.139 52.179 29.171 1.00 30.14 ? 212 ASN A O 1 ATOM 1351 C CB . ASN A 1 171 ? 19.381 52.632 32.331 1.00 28.73 ? 212 ASN A CB 1 ATOM 1352 C CG . ASN A 1 171 ? 18.605 53.319 33.445 1.00 32.49 ? 212 ASN A CG 1 ATOM 1353 O OD1 . ASN A 1 171 ? 18.591 52.821 34.582 1.00 31.36 ? 212 ASN A OD1 1 ATOM 1354 N ND2 . ASN A 1 171 ? 17.959 54.453 33.132 1.00 28.99 ? 212 ASN A ND2 1 ATOM 1355 N N . LYS A 1 172 ? 19.975 50.340 30.211 1.00 29.03 ? 213 LYS A N 1 ATOM 1356 C CA . LYS A 1 172 ? 20.650 49.864 28.972 1.00 29.23 ? 213 LYS A CA 1 ATOM 1357 C C . LYS A 1 172 ? 19.648 49.618 27.828 1.00 30.06 ? 213 LYS A C 1 ATOM 1358 O O . LYS A 1 172 ? 19.869 50.013 26.654 1.00 30.62 ? 213 LYS A O 1 ATOM 1359 C CB . LYS A 1 172 ? 21.432 48.562 29.226 1.00 28.56 ? 213 LYS A CB 1 ATOM 1360 C CG . LYS A 1 172 ? 22.459 48.610 30.365 1.00 29.06 ? 213 LYS A CG 1 ATOM 1361 C CD . LYS A 1 172 ? 23.099 47.237 30.546 1.00 28.97 ? 213 LYS A CD 1 ATOM 1362 C CE . LYS A 1 172 ? 23.932 47.157 31.812 1.00 28.90 ? 213 LYS A CE 1 ATOM 1363 N NZ . LYS A 1 172 ? 25.351 47.608 31.528 1.00 30.88 ? 213 LYS A NZ 1 ATOM 1364 N N . VAL A 1 173 ? 18.549 48.940 28.166 1.00 29.30 ? 214 VAL A N 1 ATOM 1365 C CA . VAL A 1 173 ? 17.563 48.560 27.186 1.00 28.83 ? 214 VAL A CA 1 ATOM 1366 C C . VAL A 1 173 ? 16.833 49.819 26.653 1.00 29.97 ? 214 VAL A C 1 ATOM 1367 O O . VAL A 1 173 ? 16.594 49.905 25.457 1.00 30.88 ? 214 VAL A O 1 ATOM 1368 C CB . VAL A 1 173 ? 16.542 47.530 27.789 1.00 30.44 ? 214 VAL A CB 1 ATOM 1369 C CG1 . VAL A 1 173 ? 15.376 47.304 26.830 1.00 28.25 ? 214 VAL A CG1 1 ATOM 1370 C CG2 . VAL A 1 173 ? 17.244 46.159 28.027 1.00 29.83 ? 214 VAL A CG2 1 ATOM 1371 N N . LYS A 1 174 ? 16.524 50.765 27.545 1.00 30.22 ? 215 LYS A N 1 ATOM 1372 C CA . LYS A 1 174 ? 15.895 52.031 27.126 1.00 31.54 ? 215 LYS A CA 1 ATOM 1373 C C . LYS A 1 174 ? 16.834 52.738 26.157 1.00 32.39 ? 215 LYS A C 1 ATOM 1374 O O . LYS A 1 174 ? 16.384 53.217 25.085 1.00 32.42 ? 215 LYS A O 1 ATOM 1375 C CB . LYS A 1 174 ? 15.617 52.919 28.330 1.00 31.71 ? 215 LYS A CB 1 ATOM 1376 C CG . LYS A 1 174 ? 15.057 54.319 27.967 1.00 35.78 ? 215 LYS A CG 1 ATOM 1377 C CD . LYS A 1 174 ? 14.667 55.051 29.286 1.00 41.21 ? 215 LYS A CD 1 ATOM 1378 C CE . LYS A 1 174 ? 14.270 56.502 29.040 1.00 48.53 ? 215 LYS A CE 1 ATOM 1379 N NZ . LYS A 1 174 ? 15.501 57.334 28.807 1.00 52.15 ? 215 LYS A NZ 1 ATOM 1380 N N . ASN A 1 175 ? 18.126 52.792 26.516 1.00 32.09 ? 216 ASN A N 1 ATOM 1381 C CA . ASN A 1 175 ? 19.143 53.453 25.634 1.00 32.86 ? 216 ASN A CA 1 ATOM 1382 C C . ASN A 1 175 ? 19.220 52.756 24.266 1.00 34.06 ? 216 ASN A C 1 ATOM 1383 O O . ASN A 1 175 ? 19.228 53.422 23.215 1.00 34.70 ? 216 ASN A O 1 ATOM 1384 C CB . ASN A 1 175 ? 20.527 53.512 26.320 1.00 31.40 ? 216 ASN A CB 1 ATOM 1385 C CG . ASN A 1 175 ? 20.527 54.385 27.575 1.00 36.15 ? 216 ASN A CG 1 ATOM 1386 O OD1 . ASN A 1 175 ? 19.598 55.151 27.781 1.00 36.50 ? 216 ASN A OD1 1 ATOM 1387 N ND2 . ASN A 1 175 ? 21.553 54.253 28.421 1.00 33.53 ? 216 ASN A ND2 1 ATOM 1388 N N . ALA A 1 176 ? 19.279 51.425 24.259 1.00 33.65 ? 217 ALA A N 1 ATOM 1389 C CA . ALA A 1 176 ? 19.311 50.654 22.972 1.00 35.55 ? 217 ALA A CA 1 ATOM 1390 C C . ALA A 1 176 ? 18.061 50.904 22.115 1.00 36.65 ? 217 ALA A C 1 ATOM 1391 O O . ALA A 1 176 ? 18.116 51.056 20.891 1.00 38.75 ? 217 ALA A O 1 ATOM 1392 C CB . ALA A 1 176 ? 19.468 49.146 23.265 1.00 34.61 ? 217 ALA A CB 1 ATOM 1393 N N . GLN A 1 177 ? 16.920 50.931 22.781 1.00 38.30 ? 218 GLN A N 1 ATOM 1394 C CA . GLN A 1 177 ? 15.637 51.152 22.119 1.00 40.44 ? 218 GLN A CA 1 ATOM 1395 C C . GLN A 1 177 ? 15.612 52.524 21.433 1.00 41.48 ? 218 GLN A C 1 ATOM 1396 O O . GLN A 1 177 ? 15.244 52.618 20.258 1.00 41.51 ? 218 GLN A O 1 ATOM 1397 C CB . GLN A 1 177 ? 14.522 51.046 23.170 1.00 40.45 ? 218 GLN A CB 1 ATOM 1398 C CG . GLN A 1 177 ? 13.198 50.574 22.651 1.00 45.45 ? 218 GLN A CG 1 ATOM 1399 C CD . GLN A 1 177 ? 12.180 50.380 23.797 1.00 47.32 ? 218 GLN A CD 1 ATOM 1400 O OE1 . GLN A 1 177 ? 12.229 49.382 24.535 1.00 46.32 ? 218 GLN A OE1 1 ATOM 1401 N NE2 . GLN A 1 177 ? 11.256 51.334 23.930 1.00 47.06 ? 218 GLN A NE2 1 ATOM 1402 N N . LEU A 1 178 ? 16.030 53.575 22.146 1.00 41.49 ? 219 LEU A N 1 ATOM 1403 C CA . LEU A 1 178 ? 16.048 54.922 21.563 1.00 43.26 ? 219 LEU A CA 1 ATOM 1404 C C . LEU A 1 178 ? 17.098 55.116 20.479 1.00 44.18 ? 219 LEU A C 1 ATOM 1405 O O . LEU A 1 178 ? 16.962 56.007 19.640 1.00 44.48 ? 219 LEU A O 1 ATOM 1406 C CB . LEU A 1 178 ? 16.165 56.008 22.631 1.00 43.62 ? 219 LEU A CB 1 ATOM 1407 C CG . LEU A 1 178 ? 15.039 56.035 23.682 1.00 46.39 ? 219 LEU A CG 1 ATOM 1408 C CD1 . LEU A 1 178 ? 15.228 57.221 24.643 1.00 48.76 ? 219 LEU A CD1 1 ATOM 1409 C CD2 . LEU A 1 178 ? 13.604 56.015 23.096 1.00 50.12 ? 219 LEU A CD2 1 ATOM 1410 N N . ALA A 1 179 ? 18.138 54.280 20.502 1.00 43.25 ? 220 ALA A N 1 ATOM 1411 C CA . ALA A 1 179 ? 19.098 54.191 19.413 1.00 44.07 ? 220 ALA A CA 1 ATOM 1412 C C . ALA A 1 179 ? 18.551 53.422 18.212 1.00 44.31 ? 220 ALA A C 1 ATOM 1413 O O . ALA A 1 179 ? 19.192 53.376 17.190 1.00 45.72 ? 220 ALA A O 1 ATOM 1414 C CB . ALA A 1 179 ? 20.364 53.552 19.903 1.00 43.96 ? 220 ALA A CB 1 ATOM 1415 N N . GLY A 1 180 ? 17.375 52.811 18.318 1.00 43.84 ? 221 GLY A N 1 ATOM 1416 C CA . GLY A 1 180 ? 16.813 52.117 17.144 1.00 43.06 ? 221 GLY A CA 1 ATOM 1417 C C . GLY A 1 180 ? 17.182 50.646 16.986 1.00 42.95 ? 221 GLY A C 1 ATOM 1418 O O . GLY A 1 180 ? 16.877 50.040 15.960 1.00 42.13 ? 221 GLY A O 1 ATOM 1419 N N . ALA A 1 181 ? 17.797 50.051 18.016 1.00 41.80 ? 222 ALA A N 1 ATOM 1420 C CA . ALA A 1 181 ? 18.125 48.608 18.028 1.00 41.60 ? 222 ALA A CA 1 ATOM 1421 C C . ALA A 1 181 ? 16.850 47.773 17.859 1.00 41.26 ? 222 ALA A C 1 ATOM 1422 O O . ALA A 1 181 ? 15.784 48.200 18.321 1.00 40.76 ? 222 ALA A O 1 ATOM 1423 C CB . ALA A 1 181 ? 18.811 48.230 19.372 1.00 40.08 ? 222 ALA A CB 1 ATOM 1424 N N . LYS A 1 182 ? 16.942 46.594 17.243 1.00 40.08 ? 223 LYS A N 1 ATOM 1425 C CA . LYS A 1 182 ? 15.782 45.711 17.206 1.00 40.33 ? 223 LYS A CA 1 ATOM 1426 C C . LYS A 1 182 ? 15.842 44.561 18.216 1.00 39.22 ? 223 LYS A C 1 ATOM 1427 O O . LYS A 1 182 ? 14.949 43.711 18.246 1.00 38.63 ? 223 LYS A O 1 ATOM 1428 C CB . LYS A 1 182 ? 15.509 45.167 15.806 1.00 42.66 ? 223 LYS A CB 1 ATOM 1429 C CG . LYS A 1 182 ? 16.535 44.236 15.275 1.00 46.16 ? 223 LYS A CG 1 ATOM 1430 C CD . LYS A 1 182 ? 16.046 43.728 13.922 1.00 48.69 ? 223 LYS A CD 1 ATOM 1431 C CE . LYS A 1 182 ? 17.177 43.331 13.053 1.00 52.89 ? 223 LYS A CE 1 ATOM 1432 N NZ . LYS A 1 182 ? 16.662 42.868 11.734 1.00 53.86 ? 223 LYS A NZ 1 ATOM 1433 N N . GLY A 1 183 ? 16.883 44.548 19.038 1.00 38.64 ? 224 GLY A N 1 ATOM 1434 C CA . GLY A 1 183 ? 17.071 43.495 20.035 1.00 38.03 ? 224 GLY A CA 1 ATOM 1435 C C . GLY A 1 183 ? 18.268 43.809 20.888 1.00 36.88 ? 224 GLY A C 1 ATOM 1436 O O . GLY A 1 183 ? 19.165 44.549 20.456 1.00 37.35 ? 224 GLY A O 1 ATOM 1437 N N . VAL A 1 184 ? 18.287 43.254 22.101 1.00 35.50 ? 225 VAL A N 1 ATOM 1438 C CA . VAL A 1 184 ? 19.395 43.446 23.024 1.00 34.69 ? 225 VAL A CA 1 ATOM 1439 C C . VAL A 1 184 ? 19.849 42.104 23.616 1.00 34.88 ? 225 VAL A C 1 ATOM 1440 O O . VAL A 1 184 ? 19.044 41.336 24.151 1.00 34.78 ? 225 VAL A O 1 ATOM 1441 C CB . VAL A 1 184 ? 19.044 44.359 24.181 1.00 33.05 ? 225 VAL A CB 1 ATOM 1442 C CG1 . VAL A 1 184 ? 20.266 44.569 25.088 1.00 31.72 ? 225 VAL A CG1 1 ATOM 1443 C CG2 . VAL A 1 184 ? 18.481 45.730 23.666 1.00 34.11 ? 225 VAL A CG2 1 ATOM 1444 N N . ILE A 1 185 ? 21.150 41.849 23.539 1.00 34.00 ? 226 ILE A N 1 ATOM 1445 C CA . ILE A 1 185 ? 21.752 40.714 24.228 1.00 32.30 ? 226 ILE A CA 1 ATOM 1446 C C . ILE A 1 185 ? 22.602 41.289 25.358 1.00 32.21 ? 226 ILE A C 1 ATOM 1447 O O . ILE A 1 185 ? 23.503 42.146 25.107 1.00 33.04 ? 226 ILE A O 1 ATOM 1448 C CB . ILE A 1 185 ? 22.622 39.867 23.258 1.00 34.40 ? 226 ILE A CB 1 ATOM 1449 C CG1 . ILE A 1 185 ? 21.742 39.310 22.129 1.00 33.91 ? 226 ILE A CG1 1 ATOM 1450 C CG2 . ILE A 1 185 ? 23.381 38.753 24.034 1.00 32.16 ? 226 ILE A CG2 1 ATOM 1451 C CD1 . ILE A 1 185 ? 22.563 38.794 20.918 1.00 33.65 ? 226 ILE A CD1 1 ATOM 1452 N N . LEU A 1 186 ? 22.322 40.845 26.591 1.00 29.13 ? 227 LEU A N 1 ATOM 1453 C CA . LEU A 1 186 ? 23.093 41.255 27.772 1.00 29.59 ? 227 LEU A CA 1 ATOM 1454 C C . LEU A 1 186 ? 24.013 40.101 28.201 1.00 29.86 ? 227 LEU A C 1 ATOM 1455 O O . LEU A 1 186 ? 23.587 38.929 28.143 1.00 30.62 ? 227 LEU A O 1 ATOM 1456 C CB . LEU A 1 186 ? 22.135 41.582 28.944 1.00 27.46 ? 227 LEU A CB 1 ATOM 1457 C CG . LEU A 1 186 ? 21.185 42.761 28.664 1.00 31.99 ? 227 LEU A CG 1 ATOM 1458 C CD1 . LEU A 1 186 ? 20.094 42.844 29.754 1.00 31.70 ? 227 LEU A CD1 1 ATOM 1459 C CD2 . LEU A 1 186 ? 21.999 44.055 28.602 1.00 33.66 ? 227 LEU A CD2 1 ATOM 1460 N N . TYR A 1 187 ? 25.269 40.397 28.561 1.00 29.08 ? 228 TYR A N 1 ATOM 1461 C CA . TYR A 1 187 ? 26.174 39.311 29.021 1.00 29.31 ? 228 TYR A CA 1 ATOM 1462 C C . TYR A 1 187 ? 27.045 39.777 30.177 1.00 29.74 ? 228 TYR A C 1 ATOM 1463 O O . TYR A 1 187 ? 27.296 40.977 30.327 1.00 30.63 ? 228 TYR A O 1 ATOM 1464 C CB . TYR A 1 187 ? 27.036 38.675 27.889 1.00 29.68 ? 228 TYR A CB 1 ATOM 1465 C CG . TYR A 1 187 ? 28.260 39.506 27.570 1.00 30.83 ? 228 TYR A CG 1 ATOM 1466 C CD1 . TYR A 1 187 ? 29.515 39.156 28.079 1.00 32.73 ? 228 TYR A CD1 1 ATOM 1467 C CD2 . TYR A 1 187 ? 28.160 40.641 26.776 1.00 32.01 ? 228 TYR A CD2 1 ATOM 1468 C CE1 . TYR A 1 187 ? 30.670 39.953 27.800 1.00 34.15 ? 228 TYR A CE1 1 ATOM 1469 C CE2 . TYR A 1 187 ? 29.289 41.446 26.498 1.00 34.92 ? 228 TYR A CE2 1 ATOM 1470 C CZ . TYR A 1 187 ? 30.529 41.096 27.025 1.00 35.85 ? 228 TYR A CZ 1 ATOM 1471 O OH . TYR A 1 187 ? 31.632 41.881 26.781 1.00 37.89 ? 228 TYR A OH 1 ATOM 1472 N N . SER A 1 188 ? 27.526 38.823 30.970 1.00 29.42 ? 229 SER A N 1 ATOM 1473 C CA . SER A 1 188 ? 28.446 39.132 32.064 1.00 29.25 ? 229 SER A CA 1 ATOM 1474 C C . SER A 1 188 ? 29.909 38.950 31.612 1.00 30.43 ? 229 SER A C 1 ATOM 1475 O O . SER A 1 188 ? 30.348 37.833 31.357 1.00 30.34 ? 229 SER A O 1 ATOM 1476 C CB . SER A 1 188 ? 28.117 38.210 33.247 1.00 29.12 ? 229 SER A CB 1 ATOM 1477 O OG . SER A 1 188 ? 26.771 38.419 33.652 1.00 30.24 ? 229 SER A OG 1 ATOM 1478 N N . ASP A 1 189 ? 30.653 40.052 31.518 1.00 30.86 ? 230 ASP A N 1 ATOM 1479 C CA . ASP A 1 189 ? 32.070 39.964 31.153 1.00 33.52 ? 230 ASP A CA 1 ATOM 1480 C C . ASP A 1 189 ? 32.892 39.632 32.401 1.00 34.69 ? 230 ASP A C 1 ATOM 1481 O O . ASP A 1 189 ? 32.650 40.206 33.473 1.00 35.09 ? 230 ASP A O 1 ATOM 1482 C CB . ASP A 1 189 ? 32.527 41.286 30.515 1.00 33.96 ? 230 ASP A CB 1 ATOM 1483 C CG . ASP A 1 189 ? 33.828 41.142 29.726 1.00 36.70 ? 230 ASP A CG 1 ATOM 1484 O OD1 . ASP A 1 189 ? 33.752 41.130 28.475 1.00 38.47 ? 230 ASP A OD1 1 ATOM 1485 O OD2 . ASP A 1 189 ? 34.902 40.957 30.352 1.00 37.83 ? 230 ASP A OD2 1 ATOM 1486 N N . PRO A 1 190 ? 33.885 38.720 32.281 1.00 36.55 ? 231 PRO A N 1 ATOM 1487 C CA . PRO A 1 190 ? 34.786 38.451 33.396 1.00 37.19 ? 231 PRO A CA 1 ATOM 1488 C C . PRO A 1 190 ? 35.464 39.715 33.927 1.00 38.01 ? 231 PRO A C 1 ATOM 1489 O O . PRO A 1 190 ? 35.847 39.744 35.084 1.00 37.83 ? 231 PRO A O 1 ATOM 1490 C CB . PRO A 1 190 ? 35.865 37.554 32.789 1.00 39.03 ? 231 PRO A CB 1 ATOM 1491 C CG . PRO A 1 190 ? 35.242 36.936 31.642 1.00 39.58 ? 231 PRO A CG 1 ATOM 1492 C CD . PRO A 1 190 ? 34.142 37.819 31.141 1.00 36.56 ? 231 PRO A CD 1 ATOM 1493 N N . ALA A 1 191 ? 35.596 40.763 33.120 1.00 38.55 ? 232 ALA A N 1 ATOM 1494 C CA . ALA A 1 191 ? 36.213 41.984 33.671 1.00 39.20 ? 232 ALA A CA 1 ATOM 1495 C C . ALA A 1 191 ? 35.412 42.512 34.889 1.00 38.70 ? 232 ALA A C 1 ATOM 1496 O O . ALA A 1 191 ? 35.992 42.988 35.888 1.00 37.94 ? 232 ALA A O 1 ATOM 1497 C CB . ALA A 1 191 ? 36.315 43.039 32.602 1.00 40.97 ? 232 ALA A CB 1 ATOM 1498 N N . ASP A 1 192 ? 34.082 42.391 34.806 1.00 37.49 ? 233 ASP A N 1 ATOM 1499 C CA . ASP A 1 192 ? 33.166 42.899 35.817 1.00 36.84 ? 233 ASP A CA 1 ATOM 1500 C C . ASP A 1 192 ? 32.721 41.840 36.830 1.00 36.78 ? 233 ASP A C 1 ATOM 1501 O O . ASP A 1 192 ? 32.319 42.191 37.965 1.00 38.65 ? 233 ASP A O 1 ATOM 1502 C CB . ASP A 1 192 ? 31.950 43.529 35.103 1.00 35.91 ? 233 ASP A CB 1 ATOM 1503 C CG . ASP A 1 192 ? 32.378 44.516 34.014 1.00 38.77 ? 233 ASP A CG 1 ATOM 1504 O OD1 . ASP A 1 192 ? 32.767 45.633 34.400 1.00 39.53 ? 233 ASP A OD1 1 ATOM 1505 O OD2 . ASP A 1 192 ? 32.396 44.171 32.792 1.00 36.73 ? 233 ASP A OD2 1 ATOM 1506 N N . TYR A 1 193 ? 32.744 40.561 36.456 1.00 34.79 ? 234 TYR A N 1 ATOM 1507 C CA . TYR A 1 193 ? 32.136 39.538 37.309 1.00 33.13 ? 234 TYR A CA 1 ATOM 1508 C C . TYR A 1 193 ? 33.063 38.401 37.663 1.00 34.35 ? 234 TYR A C 1 ATOM 1509 O O . TYR A 1 193 ? 32.606 37.328 38.056 1.00 33.97 ? 234 TYR A O 1 ATOM 1510 C CB . TYR A 1 193 ? 30.832 39.007 36.669 1.00 32.23 ? 234 TYR A CB 1 ATOM 1511 C CG . TYR A 1 193 ? 29.805 40.108 36.591 1.00 31.22 ? 234 TYR A CG 1 ATOM 1512 C CD1 . TYR A 1 193 ? 29.616 40.834 35.413 1.00 33.07 ? 234 TYR A CD1 1 ATOM 1513 C CD2 . TYR A 1 193 ? 29.047 40.444 37.710 1.00 31.48 ? 234 TYR A CD2 1 ATOM 1514 C CE1 . TYR A 1 193 ? 28.692 41.901 35.354 1.00 32.75 ? 234 TYR A CE1 1 ATOM 1515 C CE2 . TYR A 1 193 ? 28.140 41.504 37.675 1.00 32.22 ? 234 TYR A CE2 1 ATOM 1516 C CZ . TYR A 1 193 ? 27.970 42.230 36.499 1.00 33.00 ? 234 TYR A CZ 1 ATOM 1517 O OH . TYR A 1 193 ? 27.026 43.254 36.478 1.00 31.65 ? 234 TYR A OH 1 ATOM 1518 N N . PHE A 1 194 ? 34.374 38.603 37.496 1.00 35.43 ? 235 PHE A N 1 ATOM 1519 C CA . PHE A 1 194 ? 35.331 37.553 37.857 1.00 35.94 ? 235 PHE A CA 1 ATOM 1520 C C . PHE A 1 194 ? 36.494 38.295 38.512 1.00 38.07 ? 235 PHE A C 1 ATOM 1521 O O . PHE A 1 194 ? 37.275 38.933 37.812 1.00 38.70 ? 235 PHE A O 1 ATOM 1522 C CB . PHE A 1 194 ? 35.804 36.797 36.617 1.00 36.35 ? 235 PHE A CB 1 ATOM 1523 C CG . PHE A 1 194 ? 36.527 35.512 36.916 1.00 36.08 ? 235 PHE A CG 1 ATOM 1524 C CD1 . PHE A 1 194 ? 35.818 34.312 36.994 1.00 35.90 ? 235 PHE A CD1 1 ATOM 1525 C CD2 . PHE A 1 194 ? 37.918 35.498 37.148 1.00 37.74 ? 235 PHE A CD2 1 ATOM 1526 C CE1 . PHE A 1 194 ? 36.492 33.091 37.281 1.00 38.64 ? 235 PHE A CE1 1 ATOM 1527 C CE2 . PHE A 1 194 ? 38.594 34.291 37.435 1.00 38.82 ? 235 PHE A CE2 1 ATOM 1528 C CZ . PHE A 1 194 ? 37.874 33.087 37.503 1.00 38.32 ? 235 PHE A CZ 1 ATOM 1529 N N . ALA A 1 195 ? 36.581 38.254 39.836 1.00 38.71 ? 236 ALA A N 1 ATOM 1530 C CA . ALA A 1 195 ? 37.682 38.915 40.532 1.00 41.33 ? 236 ALA A CA 1 ATOM 1531 C C . ALA A 1 195 ? 38.969 38.106 40.319 1.00 43.74 ? 236 ALA A C 1 ATOM 1532 O O . ALA A 1 195 ? 38.951 36.876 40.438 1.00 43.10 ? 236 ALA A O 1 ATOM 1533 C CB . ALA A 1 195 ? 37.358 39.053 42.024 1.00 40.71 ? 236 ALA A CB 1 ATOM 1534 N N . PRO A 1 196 ? 40.088 38.784 39.976 1.00 46.39 ? 237 PRO A N 1 ATOM 1535 C CA . PRO A 1 196 ? 41.306 38.011 39.724 1.00 47.95 ? 237 PRO A CA 1 ATOM 1536 C C . PRO A 1 196 ? 41.721 37.238 40.989 1.00 48.02 ? 237 PRO A C 1 ATOM 1537 O O . PRO A 1 196 ? 41.560 37.746 42.103 1.00 47.83 ? 237 PRO A O 1 ATOM 1538 C CB . PRO A 1 196 ? 42.341 39.087 39.347 1.00 49.48 ? 237 PRO A CB 1 ATOM 1539 C CG . PRO A 1 196 ? 41.518 40.295 38.978 1.00 49.27 ? 237 PRO A CG 1 ATOM 1540 C CD . PRO A 1 196 ? 40.313 40.239 39.861 1.00 46.97 ? 237 PRO A CD 1 ATOM 1541 N N . GLY A 1 197 ? 42.168 36.001 40.814 1.00 48.22 ? 238 GLY A N 1 ATOM 1542 C CA . GLY A 1 197 ? 42.763 35.221 41.899 1.00 48.35 ? 238 GLY A CA 1 ATOM 1543 C C . GLY A 1 197 ? 41.782 34.438 42.754 1.00 47.76 ? 238 GLY A C 1 ATOM 1544 O O . GLY A 1 197 ? 42.182 33.782 43.721 1.00 48.09 ? 238 GLY A O 1 ATOM 1545 N N . VAL A 1 198 ? 40.492 34.495 42.406 1.00 43.88 ? 239 VAL A N 1 ATOM 1546 C CA . VAL A 1 198 ? 39.477 33.716 43.117 1.00 41.98 ? 239 VAL A CA 1 ATOM 1547 C C . VAL A 1 198 ? 38.859 32.715 42.147 1.00 41.08 ? 239 VAL A C 1 ATOM 1548 O O . VAL A 1 198 ? 38.758 32.982 40.961 1.00 40.98 ? 239 VAL A O 1 ATOM 1549 C CB . VAL A 1 198 ? 38.409 34.656 43.835 1.00 41.29 ? 239 VAL A CB 1 ATOM 1550 C CG1 A VAL A 1 198 ? 38.631 36.108 43.481 0.50 40.75 ? 239 VAL A CG1 1 ATOM 1551 C CG1 B VAL A 1 198 ? 37.201 33.861 44.347 0.50 38.89 ? 239 VAL A CG1 1 ATOM 1552 C CG2 A VAL A 1 198 ? 36.966 34.187 43.650 0.50 38.43 ? 239 VAL A CG2 1 ATOM 1553 C CG2 B VAL A 1 198 ? 39.055 35.475 44.951 0.50 40.10 ? 239 VAL A CG2 1 ATOM 1554 N N . LYS A 1 199 ? 38.484 31.556 42.666 1.00 41.12 ? 240 LYS A N 1 ATOM 1555 C CA A LYS A 1 199 ? 37.940 30.443 41.898 0.50 41.19 ? 240 LYS A CA 1 ATOM 1556 C CA B LYS A 1 199 ? 37.963 30.507 41.798 0.50 41.28 ? 240 LYS A CA 1 ATOM 1557 C C . LYS A 1 199 ? 36.452 30.641 41.598 1.00 40.34 ? 240 LYS A C 1 ATOM 1558 O O . LYS A 1 199 ? 35.767 31.303 42.373 1.00 38.85 ? 240 LYS A O 1 ATOM 1559 C CB A LYS A 1 199 ? 38.121 29.158 42.714 0.50 41.73 ? 240 LYS A CB 1 ATOM 1560 C CB B LYS A 1 199 ? 38.344 29.112 42.307 0.50 42.58 ? 240 LYS A CB 1 ATOM 1561 C CG A LYS A 1 199 ? 39.578 28.623 42.743 0.50 43.90 ? 240 LYS A CG 1 ATOM 1562 C CG B LYS A 1 199 ? 39.865 28.819 42.263 0.50 43.71 ? 240 LYS A CG 1 ATOM 1563 C CD A LYS A 1 199 ? 39.844 27.745 43.959 0.50 44.52 ? 240 LYS A CD 1 ATOM 1564 C CD B LYS A 1 199 ? 40.468 28.978 40.864 0.50 45.24 ? 240 LYS A CD 1 ATOM 1565 C CE A LYS A 1 199 ? 41.269 27.179 43.910 0.50 47.61 ? 240 LYS A CE 1 ATOM 1566 C CE B LYS A 1 199 ? 40.862 27.623 40.285 0.50 47.61 ? 240 LYS A CE 1 ATOM 1567 N NZ A LYS A 1 199 ? 41.775 26.926 45.276 0.50 49.63 ? 240 LYS A NZ 1 ATOM 1568 N NZ B LYS A 1 199 ? 42.078 27.704 39.407 0.50 48.54 ? 240 LYS A NZ 1 ATOM 1569 N N . SER A 1 200 ? 35.962 30.054 40.502 1.00 39.77 ? 241 SER A N 1 ATOM 1570 C CA . SER A 1 200 ? 34.524 30.019 40.180 1.00 39.43 ? 241 SER A CA 1 ATOM 1571 C C . SER A 1 200 ? 33.773 29.108 41.132 1.00 38.06 ? 241 SER A C 1 ATOM 1572 O O . SER A 1 200 ? 34.332 28.097 41.591 1.00 37.67 ? 241 SER A O 1 ATOM 1573 C CB . SER A 1 200 ? 34.356 29.340 38.804 1.00 42.15 ? 241 SER A CB 1 ATOM 1574 O OG . SER A 1 200 ? 34.862 30.131 37.763 1.00 46.83 ? 241 SER A OG 1 ATOM 1575 N N . TYR A 1 201 ? 32.487 29.397 41.341 1.00 36.72 ? 242 TYR A N 1 ATOM 1576 C CA . TYR A 1 201 ? 31.584 28.520 42.084 1.00 36.10 ? 242 TYR A CA 1 ATOM 1577 C C . TYR A 1 201 ? 31.576 27.125 41.449 1.00 37.72 ? 242 TYR A C 1 ATOM 1578 O O . TYR A 1 201 ? 31.529 27.036 40.215 1.00 36.62 ? 242 TYR A O 1 ATOM 1579 C CB . TYR A 1 201 ? 30.170 29.120 42.120 1.00 34.11 ? 242 TYR A CB 1 ATOM 1580 C CG . TYR A 1 201 ? 29.345 28.506 43.235 1.00 33.59 ? 242 TYR A CG 1 ATOM 1581 C CD1 . TYR A 1 201 ? 29.477 28.929 44.572 1.00 33.52 ? 242 TYR A CD1 1 ATOM 1582 C CD2 . TYR A 1 201 ? 28.478 27.435 42.956 1.00 34.82 ? 242 TYR A CD2 1 ATOM 1583 C CE1 . TYR A 1 201 ? 28.736 28.293 45.600 1.00 35.09 ? 242 TYR A CE1 1 ATOM 1584 C CE2 . TYR A 1 201 ? 27.724 26.814 43.961 1.00 35.39 ? 242 TYR A CE2 1 ATOM 1585 C CZ . TYR A 1 201 ? 27.852 27.255 45.282 1.00 38.07 ? 242 TYR A CZ 1 ATOM 1586 O OH . TYR A 1 201 ? 27.075 26.587 46.214 1.00 43.23 ? 242 TYR A OH 1 ATOM 1587 N N . PRO A 1 202 ? 31.611 26.040 42.268 1.00 38.89 ? 243 PRO A N 1 ATOM 1588 C CA . PRO A 1 202 ? 31.454 25.935 43.739 1.00 39.43 ? 243 PRO A CA 1 ATOM 1589 C C . PRO A 1 202 ? 32.727 26.041 44.600 1.00 40.37 ? 243 PRO A C 1 ATOM 1590 O O . PRO A 1 202 ? 32.650 25.830 45.816 1.00 42.53 ? 243 PRO A O 1 ATOM 1591 C CB . PRO A 1 202 ? 30.873 24.528 43.908 1.00 38.87 ? 243 PRO A CB 1 ATOM 1592 C CG . PRO A 1 202 ? 31.636 23.730 42.825 1.00 39.34 ? 243 PRO A CG 1 ATOM 1593 C CD . PRO A 1 202 ? 31.684 24.695 41.641 1.00 39.86 ? 243 PRO A CD 1 ATOM 1594 N N . ASP A 1 203 ? 33.849 26.392 44.003 1.00 39.94 ? 244 ASP A N 1 ATOM 1595 C CA . ASP A 1 203 ? 35.126 26.392 44.724 1.00 41.17 ? 244 ASP A CA 1 ATOM 1596 C C . ASP A 1 203 ? 35.571 27.774 45.152 1.00 39.81 ? 244 ASP A C 1 ATOM 1597 O O . ASP A 1 203 ? 36.589 27.911 45.820 1.00 39.61 ? 244 ASP A O 1 ATOM 1598 C CB . ASP A 1 203 ? 36.223 25.721 43.911 1.00 42.72 ? 244 ASP A CB 1 ATOM 1599 C CG . ASP A 1 203 ? 35.889 24.262 43.558 1.00 48.04 ? 244 ASP A CG 1 ATOM 1600 O OD1 . ASP A 1 203 ? 35.440 23.487 44.456 1.00 49.65 ? 244 ASP A OD1 1 ATOM 1601 O OD2 . ASP A 1 203 ? 36.073 23.914 42.367 1.00 51.54 ? 244 ASP A OD2 1 ATOM 1602 N N . GLY A 1 204 ? 34.779 28.791 44.794 1.00 38.19 ? 245 GLY A N 1 ATOM 1603 C CA . GLY A 1 204 ? 35.038 30.176 45.184 1.00 36.53 ? 245 GLY A CA 1 ATOM 1604 C C . GLY A 1 204 ? 33.789 30.978 44.816 1.00 36.46 ? 245 GLY A C 1 ATOM 1605 O O . GLY A 1 204 ? 32.783 30.401 44.403 1.00 36.01 ? 245 GLY A O 1 ATOM 1606 N N . TRP A 1 205 ? 33.856 32.295 44.958 1.00 34.40 ? 246 TRP A N 1 ATOM 1607 C CA . TRP A 1 205 ? 32.670 33.104 44.785 1.00 33.57 ? 246 TRP A CA 1 ATOM 1608 C C . TRP A 1 205 ? 32.576 33.795 43.435 1.00 33.17 ? 246 TRP A C 1 ATOM 1609 O O . TRP A 1 205 ? 31.751 34.706 43.256 1.00 32.68 ? 246 TRP A O 1 ATOM 1610 C CB . TRP A 1 205 ? 32.566 34.118 45.918 1.00 32.84 ? 246 TRP A CB 1 ATOM 1611 C CG . TRP A 1 205 ? 33.855 34.860 46.280 1.00 34.80 ? 246 TRP A CG 1 ATOM 1612 C CD1 . TRP A 1 205 ? 34.792 34.471 47.181 1.00 38.20 ? 246 TRP A CD1 1 ATOM 1613 C CD2 . TRP A 1 205 ? 34.268 36.141 45.794 1.00 37.62 ? 246 TRP A CD2 1 ATOM 1614 N NE1 . TRP A 1 205 ? 35.787 35.429 47.281 1.00 41.18 ? 246 TRP A NE1 1 ATOM 1615 C CE2 . TRP A 1 205 ? 35.490 36.466 46.443 1.00 38.29 ? 246 TRP A CE2 1 ATOM 1616 C CE3 . TRP A 1 205 ? 33.731 37.046 44.873 1.00 38.09 ? 246 TRP A CE3 1 ATOM 1617 C CZ2 . TRP A 1 205 ? 36.202 37.660 46.187 1.00 39.70 ? 246 TRP A CZ2 1 ATOM 1618 C CZ3 . TRP A 1 205 ? 34.451 38.267 44.618 1.00 39.94 ? 246 TRP A CZ3 1 ATOM 1619 C CH2 . TRP A 1 205 ? 35.670 38.549 45.286 1.00 39.77 ? 246 TRP A CH2 1 ATOM 1620 N N . ASN A 1 206 ? 33.402 33.368 42.472 1.00 32.62 ? 247 ASN A N 1 ATOM 1621 C CA . ASN A 1 206 ? 33.355 33.942 41.124 1.00 33.35 ? 247 ASN A CA 1 ATOM 1622 C C . ASN A 1 206 ? 32.295 33.324 40.221 1.00 32.74 ? 247 ASN A C 1 ATOM 1623 O O . ASN A 1 206 ? 31.865 32.197 40.468 1.00 32.07 ? 247 ASN A O 1 ATOM 1624 C CB . ASN A 1 206 ? 34.731 33.830 40.431 1.00 33.94 ? 247 ASN A CB 1 ATOM 1625 C CG . ASN A 1 206 ? 35.563 35.077 40.622 1.00 35.39 ? 247 ASN A CG 1 ATOM 1626 O OD1 . ASN A 1 206 ? 35.025 36.147 40.951 1.00 35.64 ? 247 ASN A OD1 1 ATOM 1627 N ND2 . ASN A 1 206 ? 36.885 34.959 40.410 1.00 32.12 ? 247 ASN A ND2 1 ATOM 1628 N N . LEU A 1 207 ? 31.890 34.081 39.188 1.00 31.39 ? 248 LEU A N 1 ATOM 1629 C CA . LEU A 1 207 ? 30.940 33.614 38.182 1.00 30.12 ? 248 LEU A CA 1 ATOM 1630 C C . LEU A 1 207 ? 31.591 32.669 37.182 1.00 31.93 ? 248 LEU A C 1 ATOM 1631 O O . LEU A 1 207 ? 32.583 33.039 36.567 1.00 33.72 ? 248 LEU A O 1 ATOM 1632 C CB . LEU A 1 207 ? 30.350 34.827 37.441 1.00 30.16 ? 248 LEU A CB 1 ATOM 1633 C CG . LEU A 1 207 ? 29.212 34.545 36.448 1.00 32.15 ? 248 LEU A CG 1 ATOM 1634 C CD1 . LEU A 1 207 ? 27.871 34.027 37.118 1.00 31.16 ? 248 LEU A CD1 1 ATOM 1635 C CD2 . LEU A 1 207 ? 28.993 35.814 35.620 1.00 33.95 ? 248 LEU A CD2 1 ATOM 1636 N N . PRO A 1 208 ? 31.068 31.429 37.058 1.00 32.31 ? 249 PRO A N 1 ATOM 1637 C CA . PRO A 1 208 ? 31.483 30.502 35.994 1.00 33.08 ? 249 PRO A CA 1 ATOM 1638 C C . PRO A 1 208 ? 30.993 30.950 34.615 1.00 33.13 ? 249 PRO A C 1 ATOM 1639 O O . PRO A 1 208 ? 30.041 31.726 34.513 1.00 32.66 ? 249 PRO A O 1 ATOM 1640 C CB . PRO A 1 208 ? 30.793 29.174 36.364 1.00 33.35 ? 249 PRO A CB 1 ATOM 1641 C CG . PRO A 1 208 ? 30.000 29.402 37.569 1.00 33.73 ? 249 PRO A CG 1 ATOM 1642 C CD . PRO A 1 208 ? 30.065 30.848 37.969 1.00 31.17 ? 249 PRO A CD 1 ATOM 1643 N N . GLY A 1 209 ? 31.619 30.425 33.560 1.00 34.43 ? 250 GLY A N 1 ATOM 1644 C CA . GLY A 1 209 ? 31.304 30.830 32.186 1.00 34.89 ? 250 GLY A CA 1 ATOM 1645 C C . GLY A 1 209 ? 29.876 30.521 31.755 1.00 35.08 ? 250 GLY A C 1 ATOM 1646 O O . GLY A 1 209 ? 29.381 31.122 30.785 1.00 33.81 ? 250 GLY A O 1 ATOM 1647 N N . GLY A 1 210 ? 29.250 29.563 32.446 1.00 34.23 ? 251 GLY A N 1 ATOM 1648 C CA . GLY A 1 210 ? 27.844 29.188 32.222 1.00 34.22 ? 251 GLY A CA 1 ATOM 1649 C C . GLY A 1 210 ? 26.858 29.937 33.110 1.00 33.80 ? 251 GLY A C 1 ATOM 1650 O O . GLY A 1 210 ? 25.640 29.801 32.947 1.00 32.51 ? 251 GLY A O 1 ATOM 1651 N N . GLY A 1 211 ? 27.358 30.755 34.047 1.00 32.32 ? 252 GLY A N 1 ATOM 1652 C CA . GLY A 1 211 ? 26.465 31.515 34.919 1.00 30.23 ? 252 GLY A CA 1 ATOM 1653 C C . GLY A 1 211 ? 25.817 32.684 34.174 1.00 29.80 ? 252 GLY A C 1 ATOM 1654 O O . GLY A 1 211 ? 26.426 33.258 33.253 1.00 29.99 ? 252 GLY A O 1 ATOM 1655 N N . VAL A 1 212 ? 24.595 33.024 34.557 1.00 28.07 ? 253 VAL A N 1 ATOM 1656 C CA . VAL A 1 212 ? 23.871 34.098 33.886 1.00 27.69 ? 253 VAL A CA 1 ATOM 1657 C C . VAL A 1 212 ? 23.120 34.941 34.895 1.00 28.09 ? 253 VAL A C 1 ATOM 1658 O O . VAL A 1 212 ? 22.472 34.422 35.811 1.00 28.19 ? 253 VAL A O 1 ATOM 1659 C CB . VAL A 1 212 ? 22.827 33.578 32.831 1.00 27.73 ? 253 VAL A CB 1 ATOM 1660 C CG1 . VAL A 1 212 ? 22.192 34.767 32.069 1.00 26.66 ? 253 VAL A CG1 1 ATOM 1661 C CG2 . VAL A 1 212 ? 23.455 32.568 31.817 1.00 28.93 ? 253 VAL A CG2 1 ATOM 1662 N N . GLN A 1 213 ? 23.163 36.246 34.697 1.00 26.35 ? 254 GLN A N 1 ATOM 1663 C CA . GLN A 1 213 ? 22.450 37.163 35.586 1.00 27.35 ? 254 GLN A CA 1 ATOM 1664 C C . GLN A 1 213 ? 21.019 37.369 35.059 1.00 27.06 ? 254 GLN A C 1 ATOM 1665 O O . GLN A 1 213 ? 20.836 37.951 33.970 1.00 26.74 ? 254 GLN A O 1 ATOM 1666 C CB . GLN A 1 213 ? 23.195 38.525 35.623 1.00 26.15 ? 254 GLN A CB 1 ATOM 1667 C CG . GLN A 1 213 ? 22.487 39.595 36.541 1.00 26.57 ? 254 GLN A CG 1 ATOM 1668 C CD . GLN A 1 213 ? 23.057 40.993 36.343 1.00 26.73 ? 254 GLN A CD 1 ATOM 1669 O OE1 . GLN A 1 213 ? 22.298 41.982 36.314 1.00 28.13 ? 254 GLN A OE1 1 ATOM 1670 N NE2 . GLN A 1 213 ? 24.390 41.092 36.237 1.00 25.65 ? 254 GLN A NE2 1 ATOM 1671 N N . ARG A 1 214 ? 20.024 36.921 35.839 1.00 26.15 ? 255 ARG A N 1 ATOM 1672 C CA . ARG A 1 214 ? 18.620 37.256 35.580 1.00 27.38 ? 255 ARG A CA 1 ATOM 1673 C C . ARG A 1 214 ? 18.322 38.710 35.934 1.00 26.62 ? 255 ARG A C 1 ATOM 1674 O O . ARG A 1 214 ? 19.104 39.371 36.651 1.00 25.61 ? 255 ARG A O 1 ATOM 1675 C CB . ARG A 1 214 ? 17.684 36.344 36.404 1.00 25.73 ? 255 ARG A CB 1 ATOM 1676 C CG . ARG A 1 214 ? 17.711 34.920 35.869 1.00 28.72 ? 255 ARG A CG 1 ATOM 1677 C CD . ARG A 1 214 ? 17.279 33.969 36.972 1.00 26.98 ? 255 ARG A CD 1 ATOM 1678 N NE . ARG A 1 214 ? 17.442 32.555 36.621 1.00 29.68 ? 255 ARG A NE 1 ATOM 1679 C CZ . ARG A 1 214 ? 18.606 31.916 36.598 1.00 32.00 ? 255 ARG A CZ 1 ATOM 1680 N NH1 . ARG A 1 214 ? 19.734 32.580 36.883 1.00 29.80 ? 255 ARG A NH1 1 ATOM 1681 N NH2 . ARG A 1 214 ? 18.644 30.612 36.290 1.00 28.53 ? 255 ARG A NH2 1 ATOM 1682 N N . GLY A 1 215 ? 17.183 39.208 35.460 1.00 25.80 ? 256 GLY A N 1 ATOM 1683 C CA . GLY A 1 215 ? 16.704 40.477 36.033 1.00 24.01 ? 256 GLY A CA 1 ATOM 1684 C C . GLY A 1 215 ? 15.708 41.168 35.139 1.00 24.76 ? 256 GLY A C 1 ATOM 1685 O O . GLY A 1 215 ? 15.741 41.009 33.908 1.00 24.92 ? 256 GLY A O 1 ATOM 1686 N N . ASN A 1 216 ? 14.811 41.947 35.739 1.00 23.23 ? 257 ASN A N 1 ATOM 1687 C CA . ASN A 1 216 ? 13.823 42.635 34.914 1.00 23.58 ? 257 ASN A CA 1 ATOM 1688 C C . ASN A 1 216 ? 14.463 43.807 34.160 1.00 24.37 ? 257 ASN A C 1 ATOM 1689 O O . ASN A 1 216 ? 15.470 44.350 34.594 1.00 24.14 ? 257 ASN A O 1 ATOM 1690 C CB . ASN A 1 216 ? 12.603 43.090 35.742 1.00 23.14 ? 257 ASN A CB 1 ATOM 1691 C CG . ASN A 1 216 ? 12.819 44.456 36.442 1.00 27.21 ? 257 ASN A CG 1 ATOM 1692 O OD1 . ASN A 1 216 ? 12.849 45.505 35.793 1.00 28.14 ? 257 ASN A OD1 1 ATOM 1693 N ND2 . ASN A 1 216 ? 12.954 44.443 37.761 1.00 29.09 ? 257 ASN A ND2 1 ATOM 1694 N N . ILE A 1 217 ? 13.843 44.173 33.041 1.00 24.37 ? 258 ILE A N 1 ATOM 1695 C CA . ILE A 1 217 ? 14.342 45.235 32.175 1.00 24.63 ? 258 ILE A CA 1 ATOM 1696 C C . ILE A 1 217 ? 13.293 46.337 32.011 1.00 26.31 ? 258 ILE A C 1 ATOM 1697 O O . ILE A 1 217 ? 13.215 47.000 30.974 1.00 26.19 ? 258 ILE A O 1 ATOM 1698 C CB . ILE A 1 217 ? 14.756 44.663 30.803 1.00 26.88 ? 258 ILE A CB 1 ATOM 1699 C CG1 . ILE A 1 217 ? 13.582 43.835 30.188 1.00 25.30 ? 258 ILE A CG1 1 ATOM 1700 C CG2 . ILE A 1 217 ? 16.134 43.883 30.934 1.00 25.34 ? 258 ILE A CG2 1 ATOM 1701 C CD1 . ILE A 1 217 ? 13.823 43.408 28.712 1.00 32.31 ? 258 ILE A CD1 1 ATOM 1702 N N . LEU A 1 218 ? 12.454 46.510 33.029 1.00 26.50 ? 259 LEU A N 1 ATOM 1703 C CA . LEU A 1 218 ? 11.413 47.543 32.992 1.00 27.46 ? 259 LEU A CA 1 ATOM 1704 C C . LEU A 1 218 ? 11.988 48.933 33.172 1.00 28.83 ? 259 LEU A C 1 ATOM 1705 O O . LEU A 1 218 ? 13.057 49.085 33.726 1.00 28.97 ? 259 LEU A O 1 ATOM 1706 C CB . LEU A 1 218 ? 10.417 47.348 34.158 1.00 26.64 ? 259 LEU A CB 1 ATOM 1707 C CG . LEU A 1 218 ? 9.548 46.086 34.034 1.00 27.34 ? 259 LEU A CG 1 ATOM 1708 C CD1 . LEU A 1 218 ? 8.757 45.919 35.342 1.00 29.82 ? 259 LEU A CD1 1 ATOM 1709 C CD2 . LEU A 1 218 ? 8.591 46.127 32.845 1.00 30.55 ? 259 LEU A CD2 1 ATOM 1710 N N . ASN A 1 219 ? 11.257 49.947 32.693 1.00 28.43 ? 260 ASN A N 1 ATOM 1711 C CA . ASN A 1 219 ? 11.540 51.329 33.105 1.00 28.18 ? 260 ASN A CA 1 ATOM 1712 C C . ASN A 1 219 ? 10.265 51.908 33.721 1.00 27.64 ? 260 ASN A C 1 ATOM 1713 O O . ASN A 1 219 ? 9.586 52.696 33.093 1.00 28.90 ? 260 ASN A O 1 ATOM 1714 C CB . ASN A 1 219 ? 11.993 52.147 31.886 1.00 29.88 ? 260 ASN A CB 1 ATOM 1715 C CG . ASN A 1 219 ? 13.454 51.854 31.545 1.00 34.30 ? 260 ASN A CG 1 ATOM 1716 O OD1 . ASN A 1 219 ? 14.358 52.484 32.097 1.00 39.02 ? 260 ASN A OD1 1 ATOM 1717 N ND2 . ASN A 1 219 ? 13.690 50.834 30.729 1.00 33.67 ? 260 ASN A ND2 1 ATOM 1718 N N . LEU A 1 220 ? 9.934 51.487 34.930 1.00 26.64 ? 261 LEU A N 1 ATOM 1719 C CA . LEU A 1 220 ? 8.670 51.897 35.558 1.00 25.89 ? 261 LEU A CA 1 ATOM 1720 C C . LEU A 1 220 ? 8.693 53.323 36.086 1.00 26.41 ? 261 LEU A C 1 ATOM 1721 O O . LEU A 1 220 ? 7.617 53.883 36.323 1.00 25.04 ? 261 LEU A O 1 ATOM 1722 C CB . LEU A 1 220 ? 8.411 50.991 36.774 1.00 26.42 ? 261 LEU A CB 1 ATOM 1723 C CG . LEU A 1 220 ? 8.005 49.554 36.388 1.00 26.63 ? 261 LEU A CG 1 ATOM 1724 C CD1 . LEU A 1 220 ? 7.876 48.674 37.666 1.00 26.84 ? 261 LEU A CD1 1 ATOM 1725 C CD2 . LEU A 1 220 ? 6.678 49.551 35.598 1.00 27.49 ? 261 LEU A CD2 1 ATOM 1726 N N . ASN A 1 221 ? 9.890 53.846 36.400 1.00 24.86 ? 262 ASN A N 1 ATOM 1727 C CA . ASN A 1 221 ? 9.985 55.181 37.072 1.00 25.49 ? 262 ASN A CA 1 ATOM 1728 C C . ASN A 1 221 ? 9.107 55.296 38.316 1.00 24.78 ? 262 ASN A C 1 ATOM 1729 O O . ASN A 1 221 ? 8.401 56.279 38.494 1.00 25.39 ? 262 ASN A O 1 ATOM 1730 C CB . ASN A 1 221 ? 9.641 56.287 36.053 1.00 25.02 ? 262 ASN A CB 1 ATOM 1731 C CG . ASN A 1 221 ? 10.702 56.368 34.964 1.00 30.61 ? 262 ASN A CG 1 ATOM 1732 O OD1 . ASN A 1 221 ? 11.880 56.152 35.241 1.00 33.74 ? 262 ASN A OD1 1 ATOM 1733 N ND2 . ASN A 1 221 ? 10.290 56.608 33.747 1.00 30.31 ? 262 ASN A ND2 1 ATOM 1734 N N . GLY A 1 222 ? 9.086 54.243 39.137 1.00 23.43 ? 263 GLY A N 1 ATOM 1735 C CA . GLY A 1 222 ? 8.339 54.277 40.356 1.00 23.83 ? 263 GLY A CA 1 ATOM 1736 C C . GLY A 1 222 ? 6.873 53.885 40.300 1.00 23.92 ? 263 GLY A C 1 ATOM 1737 O O . GLY A 1 222 ? 6.199 54.014 41.299 1.00 22.92 ? 263 GLY A O 1 ATOM 1738 N N . ALA A 1 223 ? 6.368 53.473 39.147 1.00 22.46 ? 264 ALA A N 1 ATOM 1739 C CA . ALA A 1 223 ? 4.935 53.222 38.997 1.00 23.73 ? 264 ALA A CA 1 ATOM 1740 C C . ALA A 1 223 ? 4.425 51.969 39.716 1.00 22.51 ? 264 ALA A C 1 ATOM 1741 O O . ALA A 1 223 ? 3.232 51.910 40.049 1.00 24.84 ? 264 ALA A O 1 ATOM 1742 C CB . ALA A 1 223 ? 4.520 53.158 37.485 1.00 23.05 ? 264 ALA A CB 1 ATOM 1743 N N . GLY A 1 224 ? 5.280 50.981 39.954 1.00 21.84 ? 265 GLY A N 1 ATOM 1744 C CA . GLY A 1 224 ? 4.750 49.716 40.524 1.00 22.79 ? 265 GLY A CA 1 ATOM 1745 C C . GLY A 1 224 ? 4.170 48.848 39.382 1.00 23.05 ? 265 GLY A C 1 ATOM 1746 O O . GLY A 1 224 ? 4.655 48.911 38.261 1.00 24.35 ? 265 GLY A O 1 ATOM 1747 N N . ASP A 1 225 ? 3.140 48.068 39.679 1.00 22.78 ? 266 ASP A N 1 ATOM 1748 C CA . ASP A 1 225 ? 2.503 47.181 38.650 1.00 23.46 ? 266 ASP A CA 1 ATOM 1749 C C . ASP A 1 225 ? 2.217 47.973 37.383 1.00 24.32 ? 266 ASP A C 1 ATOM 1750 O O . ASP A 1 225 ? 1.524 49.013 37.428 1.00 23.10 ? 266 ASP A O 1 ATOM 1751 C CB . ASP A 1 225 ? 1.218 46.625 39.240 1.00 23.77 ? 266 ASP A CB 1 ATOM 1752 C CG . ASP A 1 225 ? 0.347 45.945 38.202 1.00 25.39 ? 266 ASP A CG 1 ATOM 1753 O OD1 . ASP A 1 225 ? 0.877 45.181 37.364 1.00 25.25 ? 266 ASP A OD1 1 ATOM 1754 O OD2 . ASP A 1 225 ? -0.897 46.139 38.246 1.00 26.68 ? 266 ASP A OD2 1 ATOM 1755 N N . PRO A 1 226 ? 2.751 47.511 36.241 1.00 25.24 ? 267 PRO A N 1 ATOM 1756 C CA . PRO A 1 226 ? 2.574 48.216 34.996 1.00 26.65 ? 267 PRO A CA 1 ATOM 1757 C C . PRO A 1 226 ? 1.103 48.484 34.611 1.00 24.89 ? 267 PRO A C 1 ATOM 1758 O O . PRO A 1 226 ? 0.809 49.441 33.895 1.00 26.80 ? 267 PRO A O 1 ATOM 1759 C CB . PRO A 1 226 ? 3.148 47.222 33.965 1.00 26.45 ? 267 PRO A CB 1 ATOM 1760 C CG . PRO A 1 226 ? 4.190 46.464 34.690 1.00 27.69 ? 267 PRO A CG 1 ATOM 1761 C CD . PRO A 1 226 ? 3.693 46.362 36.111 1.00 25.08 ? 267 PRO A CD 1 ATOM 1762 N N . LEU A 1 227 ? 0.188 47.631 35.067 1.00 24.82 ? 268 LEU A N 1 ATOM 1763 C CA . LEU A 1 227 ? -1.223 47.800 34.674 1.00 24.29 ? 268 LEU A CA 1 ATOM 1764 C C . LEU A 1 227 ? -2.057 48.738 35.562 1.00 23.52 ? 268 LEU A C 1 ATOM 1765 O O . LEU A 1 227 ? -3.179 49.123 35.163 1.00 24.54 ? 268 LEU A O 1 ATOM 1766 C CB . LEU A 1 227 ? -1.872 46.395 34.626 1.00 23.65 ? 268 LEU A CB 1 ATOM 1767 C CG . LEU A 1 227 ? -1.149 45.429 33.681 1.00 25.12 ? 268 LEU A CG 1 ATOM 1768 C CD1 . LEU A 1 227 ? -2.018 44.175 33.548 1.00 28.63 ? 268 LEU A CD1 1 ATOM 1769 C CD2 . LEU A 1 227 ? -0.839 45.997 32.287 1.00 27.75 ? 268 LEU A CD2 1 ATOM 1770 N N . THR A 1 228 ? -1.550 49.118 36.746 1.00 23.06 ? 269 THR A N 1 ATOM 1771 C CA . THR A 1 228 ? -2.394 49.883 37.697 1.00 23.14 ? 269 THR A CA 1 ATOM 1772 C C . THR A 1 228 ? -1.689 51.091 38.337 1.00 22.69 ? 269 THR A C 1 ATOM 1773 O O . THR A 1 228 ? -1.721 51.275 39.559 1.00 22.14 ? 269 THR A O 1 ATOM 1774 C CB . THR A 1 228 ? -2.875 48.953 38.868 1.00 23.14 ? 269 THR A CB 1 ATOM 1775 O OG1 . THR A 1 228 ? -1.717 48.375 39.546 1.00 21.86 ? 269 THR A OG1 1 ATOM 1776 C CG2 . THR A 1 228 ? -3.773 47.797 38.312 1.00 21.56 ? 269 THR A CG2 1 ATOM 1777 N N . PRO A 1 229 ? -1.010 51.922 37.528 1.00 23.94 ? 270 PRO A N 1 ATOM 1778 C CA . PRO A 1 229 ? -0.236 53.021 38.168 1.00 22.56 ? 270 PRO A CA 1 ATOM 1779 C C . PRO A 1 229 ? -1.119 53.980 38.975 1.00 23.58 ? 270 PRO A C 1 ATOM 1780 O O . PRO A 1 229 ? -2.168 54.426 38.478 1.00 23.78 ? 270 PRO A O 1 ATOM 1781 C CB . PRO A 1 229 ? 0.386 53.759 36.974 1.00 23.40 ? 270 PRO A CB 1 ATOM 1782 C CG . PRO A 1 229 ? -0.618 53.467 35.820 1.00 24.58 ? 270 PRO A CG 1 ATOM 1783 C CD . PRO A 1 229 ? -1.007 52.008 36.048 1.00 24.54 ? 270 PRO A CD 1 ATOM 1784 N N . GLY A 1 230 ? -0.737 54.209 40.246 1.00 23.03 ? 271 GLY A N 1 ATOM 1785 C CA . GLY A 1 230 ? -1.457 55.141 41.143 1.00 22.81 ? 271 GLY A CA 1 ATOM 1786 C C . GLY A 1 230 ? -2.352 54.444 42.157 1.00 24.18 ? 271 GLY A C 1 ATOM 1787 O O . GLY A 1 230 ? -2.762 55.057 43.124 1.00 24.87 ? 271 GLY A O 1 ATOM 1788 N N . TYR A 1 231 ? -2.775 53.194 41.862 1.00 21.91 ? 272 TYR A N 1 ATOM 1789 C CA . TYR A 1 231 ? -3.810 52.545 42.655 1.00 22.56 ? 272 TYR A CA 1 ATOM 1790 C C . TYR A 1 231 ? -3.400 51.086 42.916 1.00 21.54 ? 272 TYR A C 1 ATOM 1791 O O . TYR A 1 231 ? -2.789 50.466 42.053 1.00 22.81 ? 272 TYR A O 1 ATOM 1792 C CB . TYR A 1 231 ? -5.181 52.620 41.930 1.00 22.21 ? 272 TYR A CB 1 ATOM 1793 C CG . TYR A 1 231 ? -5.468 54.061 41.539 1.00 23.65 ? 272 TYR A CG 1 ATOM 1794 C CD1 . TYR A 1 231 ? -6.048 54.950 42.451 1.00 22.89 ? 272 TYR A CD1 1 ATOM 1795 C CD2 . TYR A 1 231 ? -5.113 54.549 40.256 1.00 23.59 ? 272 TYR A CD2 1 ATOM 1796 C CE1 . TYR A 1 231 ? -6.296 56.277 42.079 1.00 22.34 ? 272 TYR A CE1 1 ATOM 1797 C CE2 . TYR A 1 231 ? -5.326 55.881 39.891 1.00 25.07 ? 272 TYR A CE2 1 ATOM 1798 C CZ . TYR A 1 231 ? -5.904 56.737 40.815 1.00 24.34 ? 272 TYR A CZ 1 ATOM 1799 O OH . TYR A 1 231 ? -6.117 58.061 40.471 1.00 23.36 ? 272 TYR A OH 1 ATOM 1800 N N . PRO A 1 232 ? -3.804 50.514 44.065 1.00 23.86 ? 273 PRO A N 1 ATOM 1801 C CA . PRO A 1 232 ? -3.420 49.139 44.325 1.00 23.63 ? 273 PRO A CA 1 ATOM 1802 C C . PRO A 1 232 ? -4.146 48.147 43.386 1.00 23.91 ? 273 PRO A C 1 ATOM 1803 O O . PRO A 1 232 ? -5.340 48.320 43.072 1.00 23.57 ? 273 PRO A O 1 ATOM 1804 C CB . PRO A 1 232 ? -3.857 48.881 45.770 1.00 23.23 ? 273 PRO A CB 1 ATOM 1805 C CG . PRO A 1 232 ? -5.088 49.864 45.979 1.00 24.99 ? 273 PRO A CG 1 ATOM 1806 C CD . PRO A 1 232 ? -4.623 51.112 45.135 1.00 23.70 ? 273 PRO A CD 1 ATOM 1807 N N . ALA A 1 233 ? -3.405 47.112 42.985 1.00 21.89 ? 274 ALA A N 1 ATOM 1808 C CA . ALA A 1 233 ? -3.921 46.036 42.128 1.00 23.26 ? 274 ALA A CA 1 ATOM 1809 C C . ALA A 1 233 ? -4.763 45.043 42.939 1.00 24.24 ? 274 ALA A C 1 ATOM 1810 O O . ALA A 1 233 ? -4.460 43.848 43.059 1.00 24.58 ? 274 ALA A O 1 ATOM 1811 C CB . ALA A 1 233 ? -2.744 45.324 41.437 1.00 24.27 ? 274 ALA A CB 1 ATOM 1812 N N . ASN A 1 234 ? -5.865 45.562 43.478 1.00 24.85 ? 275 ASN A N 1 ATOM 1813 C CA . ASN A 1 234 ? -6.751 44.776 44.320 1.00 27.51 ? 275 ASN A CA 1 ATOM 1814 C C . ASN A 1 234 ? -7.768 44.009 43.454 1.00 29.65 ? 275 ASN A C 1 ATOM 1815 O O . ASN A 1 234 ? -7.665 44.009 42.204 1.00 28.56 ? 275 ASN A O 1 ATOM 1816 C CB . ASN A 1 234 ? -7.443 45.697 45.337 1.00 28.27 ? 275 ASN A CB 1 ATOM 1817 C CG . ASN A 1 234 ? -8.295 46.786 44.682 1.00 28.79 ? 275 ASN A CG 1 ATOM 1818 O OD1 . ASN A 1 234 ? -8.813 46.648 43.549 1.00 32.39 ? 275 ASN A OD1 1 ATOM 1819 N ND2 . ASN A 1 234 ? -8.471 47.892 45.415 1.00 35.74 ? 275 ASN A ND2 1 ATOM 1820 N N . GLU A 1 235 ? -8.794 43.407 44.091 1.00 32.01 ? 276 GLU A N 1 ATOM 1821 C CA A GLU A 1 235 ? -9.674 42.521 43.327 0.50 33.59 ? 276 GLU A CA 1 ATOM 1822 C CA B GLU A 1 235 ? -9.791 42.545 43.423 0.50 34.23 ? 276 GLU A CA 1 ATOM 1823 C C . GLU A 1 235 ? -10.567 43.245 42.309 1.00 34.66 ? 276 GLU A C 1 ATOM 1824 O O . GLU A 1 235 ? -11.000 42.606 41.321 1.00 36.51 ? 276 GLU A O 1 ATOM 1825 C CB A GLU A 1 235 ? -10.539 41.612 44.244 0.50 35.01 ? 276 GLU A CB 1 ATOM 1826 C CB B GLU A 1 235 ? -10.853 42.021 44.446 0.50 35.86 ? 276 GLU A CB 1 ATOM 1827 C CG A GLU A 1 235 ? -9.827 40.392 44.783 0.50 37.87 ? 276 GLU A CG 1 ATOM 1828 C CG B GLU A 1 235 ? -11.474 43.180 45.289 0.50 40.09 ? 276 GLU A CG 1 ATOM 1829 C CD A GLU A 1 235 ? -9.927 39.187 43.878 0.50 41.12 ? 276 GLU A CD 1 ATOM 1830 C CD B GLU A 1 235 ? -13.005 43.159 45.562 0.50 45.51 ? 276 GLU A CD 1 ATOM 1831 O OE1 A GLU A 1 235 ? -10.484 39.250 42.749 0.50 44.36 ? 276 GLU A OE1 1 ATOM 1832 O OE1 B GLU A 1 235 ? -13.810 42.663 44.730 0.50 48.11 ? 276 GLU A OE1 1 ATOM 1833 O OE2 A GLU A 1 235 ? -9.456 38.140 44.311 0.50 43.24 ? 276 GLU A OE2 1 ATOM 1834 O OE2 B GLU A 1 235 ? -13.394 43.721 46.622 0.50 48.09 ? 276 GLU A OE2 1 ATOM 1835 N N . TYR A 1 236 ? -10.867 44.533 42.517 1.00 32.66 ? 277 TYR A N 1 ATOM 1836 C CA . TYR A 1 236 ? -11.760 45.224 41.579 1.00 33.51 ? 277 TYR A CA 1 ATOM 1837 C C . TYR A 1 236 ? -11.046 46.231 40.710 1.00 32.88 ? 277 TYR A C 1 ATOM 1838 O O . TYR A 1 236 ? -11.720 47.052 40.047 1.00 33.80 ? 277 TYR A O 1 ATOM 1839 C CB . TYR A 1 236 ? -12.941 45.917 42.313 1.00 32.67 ? 277 TYR A CB 1 ATOM 1840 C CG . TYR A 1 236 ? -12.480 46.843 43.394 1.00 32.29 ? 277 TYR A CG 1 ATOM 1841 C CD1 . TYR A 1 236 ? -12.271 48.210 43.130 1.00 35.16 ? 277 TYR A CD1 1 ATOM 1842 C CD2 . TYR A 1 236 ? -12.276 46.377 44.703 1.00 31.88 ? 277 TYR A CD2 1 ATOM 1843 C CE1 . TYR A 1 236 ? -11.820 49.083 44.131 1.00 34.19 ? 277 TYR A CE1 1 ATOM 1844 C CE2 . TYR A 1 236 ? -11.840 47.243 45.713 1.00 34.77 ? 277 TYR A CE2 1 ATOM 1845 C CZ . TYR A 1 236 ? -11.617 48.601 45.393 1.00 34.72 ? 277 TYR A CZ 1 ATOM 1846 O OH . TYR A 1 236 ? -11.195 49.454 46.374 1.00 37.59 ? 277 TYR A OH 1 ATOM 1847 N N . ALA A 1 237 ? -9.713 46.162 40.686 1.00 31.43 ? 278 ALA A N 1 ATOM 1848 C CA . ALA A 1 237 ? -8.898 47.150 39.986 1.00 32.86 ? 278 ALA A CA 1 ATOM 1849 C C . ALA A 1 237 ? -9.193 47.173 38.487 1.00 32.94 ? 278 ALA A C 1 ATOM 1850 O O . ALA A 1 237 ? -9.433 46.102 37.885 1.00 34.77 ? 278 ALA A O 1 ATOM 1851 C CB . ALA A 1 237 ? -7.408 46.817 40.183 1.00 32.59 ? 278 ALA A CB 1 ATOM 1852 N N . TYR A 1 238 ? -9.226 48.367 37.900 1.00 32.52 ? 279 TYR A N 1 ATOM 1853 C CA . TYR A 1 238 ? -9.359 48.479 36.441 1.00 34.48 ? 279 TYR A CA 1 ATOM 1854 C C . TYR A 1 238 ? -7.929 48.459 35.941 1.00 33.48 ? 279 TYR A C 1 ATOM 1855 O O . TYR A 1 238 ? -7.055 49.118 36.511 1.00 34.00 ? 279 TYR A O 1 ATOM 1856 C CB . TYR A 1 238 ? -10.068 49.783 35.960 1.00 36.36 ? 279 TYR A CB 1 ATOM 1857 C CG A TYR A 1 238 ? -10.393 49.773 34.469 0.50 33.71 ? 279 TYR A CG 1 ATOM 1858 C CG B TYR A 1 238 ? -9.383 50.428 34.711 0.50 36.78 ? 279 TYR A CG 1 ATOM 1859 C CD1 A TYR A 1 238 ? -11.420 48.990 33.954 0.50 34.01 ? 279 TYR A CD1 1 ATOM 1860 C CD1 B TYR A 1 238 ? -10.009 50.440 33.469 0.50 39.18 ? 279 TYR A CD1 1 ATOM 1861 C CD2 A TYR A 1 238 ? -9.628 50.525 33.584 0.50 33.92 ? 279 TYR A CD2 1 ATOM 1862 C CD2 B TYR A 1 238 ? -8.112 50.977 34.797 0.50 39.06 ? 279 TYR A CD2 1 ATOM 1863 C CE1 A TYR A 1 238 ? -11.689 48.969 32.587 0.50 36.44 ? 279 TYR A CE1 1 ATOM 1864 C CE1 B TYR A 1 238 ? -9.385 51.009 32.347 0.50 40.66 ? 279 TYR A CE1 1 ATOM 1865 C CE2 A TYR A 1 238 ? -9.897 50.512 32.222 0.50 36.04 ? 279 TYR A CE2 1 ATOM 1866 C CE2 B TYR A 1 238 ? -7.466 51.536 33.690 0.50 39.70 ? 279 TYR A CE2 1 ATOM 1867 C CZ A TYR A 1 238 ? -10.922 49.743 31.741 0.50 37.08 ? 279 TYR A CZ 1 ATOM 1868 C CZ B TYR A 1 238 ? -8.116 51.553 32.463 0.50 41.11 ? 279 TYR A CZ 1 ATOM 1869 O OH A TYR A 1 238 ? -11.151 49.739 30.391 0.50 41.92 ? 279 TYR A OH 1 ATOM 1870 O OH B TYR A 1 238 ? -7.488 52.116 31.359 0.50 43.24 ? 279 TYR A OH 1 ATOM 1871 N N . ARG A 1 239 ? -7.656 47.634 34.951 1.00 31.55 ? 280 ARG A N 1 ATOM 1872 C CA . ARG A 1 239 ? -6.287 47.498 34.466 1.00 31.43 ? 280 ARG A CA 1 ATOM 1873 C C . ARG A 1 239 ? -6.124 48.115 33.107 1.00 32.54 ? 280 ARG A C 1 ATOM 1874 O O . ARG A 1 239 ? -6.995 47.988 32.249 1.00 29.98 ? 280 ARG A O 1 ATOM 1875 C CB . ARG A 1 239 ? -5.919 46.009 34.378 1.00 32.72 ? 280 ARG A CB 1 ATOM 1876 C CG . ARG A 1 239 ? -5.777 45.419 35.735 1.00 33.28 ? 280 ARG A CG 1 ATOM 1877 C CD . ARG A 1 239 ? -5.319 43.944 35.727 1.00 35.38 ? 280 ARG A CD 1 ATOM 1878 N NE . ARG A 1 239 ? -5.018 43.677 37.134 1.00 40.59 ? 280 ARG A NE 1 ATOM 1879 C CZ . ARG A 1 239 ? -5.935 43.388 38.048 1.00 41.58 ? 280 ARG A CZ 1 ATOM 1880 N NH1 . ARG A 1 239 ? -7.202 43.242 37.648 1.00 43.90 ? 280 ARG A NH1 1 ATOM 1881 N NH2 . ARG A 1 239 ? -5.601 43.212 39.331 1.00 38.74 ? 280 ARG A NH2 1 ATOM 1882 N N . ARG A 1 240 ? -5.010 48.794 32.882 1.00 31.69 ? 281 ARG A N 1 ATOM 1883 C CA . ARG A 1 240 ? -4.681 49.184 31.505 1.00 33.86 ? 281 ARG A CA 1 ATOM 1884 C C . ARG A 1 240 ? -4.544 47.965 30.605 1.00 34.51 ? 281 ARG A C 1 ATOM 1885 O O . ARG A 1 240 ? -4.212 46.875 31.096 1.00 34.00 ? 281 ARG A O 1 ATOM 1886 C CB . ARG A 1 240 ? -3.356 49.908 31.506 1.00 32.89 ? 281 ARG A CB 1 ATOM 1887 C CG . ARG A 1 240 ? -3.462 51.216 32.190 1.00 34.30 ? 281 ARG A CG 1 ATOM 1888 C CD . ARG A 1 240 ? -2.168 51.942 32.067 1.00 37.04 ? 281 ARG A CD 1 ATOM 1889 N NE . ARG A 1 240 ? -2.348 53.293 32.566 1.00 36.76 ? 281 ARG A NE 1 ATOM 1890 C CZ . ARG A 1 240 ? -1.498 54.281 32.352 1.00 40.12 ? 281 ARG A CZ 1 ATOM 1891 N NH1 . ARG A 1 240 ? -0.438 54.093 31.598 1.00 39.07 ? 281 ARG A NH1 1 ATOM 1892 N NH2 . ARG A 1 240 ? -1.726 55.463 32.888 1.00 42.49 ? 281 ARG A NH2 1 ATOM 1893 N N . GLY A 1 241 ? -4.808 48.142 29.301 1.00 36.52 ? 282 GLY A N 1 ATOM 1894 C CA . GLY A 1 241 ? -4.447 47.116 28.324 1.00 38.93 ? 282 GLY A CA 1 ATOM 1895 C C . GLY A 1 241 ? -2.928 47.080 28.238 1.00 39.71 ? 282 GLY A C 1 ATOM 1896 O O . GLY A 1 241 ? -2.246 48.068 28.585 1.00 38.59 ? 282 GLY A O 1 ATOM 1897 N N . ILE A 1 242 ? -2.388 45.947 27.805 1.00 41.74 ? 283 ILE A N 1 ATOM 1898 C CA . ILE A 1 242 ? -0.928 45.787 27.639 1.00 43.11 ? 283 ILE A CA 1 ATOM 1899 C C . ILE A 1 242 ? -0.309 46.892 26.790 1.00 43.42 ? 283 ILE A C 1 ATOM 1900 O O . ILE A 1 242 ? 0.793 47.349 27.101 1.00 43.09 ? 283 ILE A O 1 ATOM 1901 C CB A ILE A 1 242 ? -0.583 44.370 27.093 0.65 44.06 ? 283 ILE A CB 1 ATOM 1902 C CB B ILE A 1 242 ? -0.509 44.383 27.084 0.35 43.41 ? 283 ILE A CB 1 ATOM 1903 C CG1 A ILE A 1 242 ? 0.798 43.922 27.557 0.65 44.64 ? 283 ILE A CG1 1 ATOM 1904 C CG1 B ILE A 1 242 ? -0.699 43.288 28.138 0.35 43.22 ? 283 ILE A CG1 1 ATOM 1905 C CG2 A ILE A 1 242 ? -0.774 44.271 25.557 0.65 46.11 ? 283 ILE A CG2 1 ATOM 1906 C CG2 B ILE A 1 242 ? 0.953 44.374 26.594 0.35 42.78 ? 283 ILE A CG2 1 ATOM 1907 C CD1 A ILE A 1 242 ? 0.874 43.693 29.070 0.65 42.92 ? 283 ILE A CD1 1 ATOM 1908 C CD1 B ILE A 1 242 ? 0.264 43.377 29.305 0.35 41.38 ? 283 ILE A CD1 1 ATOM 1909 N N . ALA A 1 243 ? -1.030 47.374 25.773 1.00 44.86 ? 284 ALA A N 1 ATOM 1910 C CA . ALA A 1 243 ? -0.492 48.431 24.918 1.00 45.55 ? 284 ALA A CA 1 ATOM 1911 C C . ALA A 1 243 ? -0.272 49.750 25.651 1.00 45.59 ? 284 ALA A C 1 ATOM 1912 O O . ALA A 1 243 ? 0.551 50.545 25.225 1.00 46.57 ? 284 ALA A O 1 ATOM 1913 C CB . ALA A 1 243 ? -1.370 48.638 23.635 1.00 47.25 ? 284 ALA A CB 1 ATOM 1914 N N . GLU A 1 244 ? -1.010 49.998 26.737 1.00 44.10 ? 285 GLU A N 1 ATOM 1915 C CA . GLU A 1 244 ? -0.870 51.243 27.490 1.00 43.82 ? 285 GLU A CA 1 ATOM 1916 C C . GLU A 1 244 ? -0.088 51.000 28.809 1.00 41.79 ? 285 GLU A C 1 ATOM 1917 O O . GLU A 1 244 ? 0.039 51.917 29.624 1.00 42.69 ? 285 GLU A O 1 ATOM 1918 C CB . GLU A 1 244 ? -2.254 51.868 27.794 1.00 45.00 ? 285 GLU A CB 1 ATOM 1919 C CG . GLU A 1 244 ? -2.948 52.591 26.613 1.00 50.22 ? 285 GLU A CG 1 ATOM 1920 C CD . GLU A 1 244 ? -3.587 51.632 25.595 1.00 59.95 ? 285 GLU A CD 1 ATOM 1921 O OE1 . GLU A 1 244 ? -4.059 50.527 25.981 1.00 62.20 ? 285 GLU A OE1 1 ATOM 1922 O OE2 . GLU A 1 244 ? -3.630 51.990 24.388 1.00 65.25 ? 285 GLU A OE2 1 ATOM 1923 N N . ALA A 1 245 ? 0.422 49.782 29.010 1.00 40.46 ? 286 ALA A N 1 ATOM 1924 C CA . ALA A 1 245 ? 1.133 49.426 30.249 1.00 39.06 ? 286 ALA A CA 1 ATOM 1925 C C . ALA A 1 245 ? 2.351 50.339 30.453 1.00 38.76 ? 286 ALA A C 1 ATOM 1926 O O . ALA A 1 245 ? 2.932 50.832 29.489 1.00 38.76 ? 286 ALA A O 1 ATOM 1927 C CB . ALA A 1 245 ? 1.553 48.003 30.239 1.00 38.32 ? 286 ALA A CB 1 ATOM 1928 N N . VAL A 1 246 ? 2.697 50.587 31.713 1.00 36.07 ? 287 VAL A N 1 ATOM 1929 C CA . VAL A 1 246 ? 3.853 51.436 32.030 1.00 35.50 ? 287 VAL A CA 1 ATOM 1930 C C . VAL A 1 246 ? 5.155 50.646 31.977 1.00 34.32 ? 287 VAL A C 1 ATOM 1931 O O . VAL A 1 246 ? 5.239 49.553 32.547 1.00 33.36 ? 287 VAL A O 1 ATOM 1932 C CB . VAL A 1 246 ? 3.702 52.071 33.433 1.00 34.70 ? 287 VAL A CB 1 ATOM 1933 C CG1 . VAL A 1 246 ? 4.966 52.926 33.802 1.00 34.73 ? 287 VAL A CG1 1 ATOM 1934 C CG2 . VAL A 1 246 ? 2.405 52.925 33.432 1.00 36.96 ? 287 VAL A CG2 1 ATOM 1935 N N . GLY A 1 247 ? 6.130 51.166 31.233 1.00 33.50 ? 288 GLY A N 1 ATOM 1936 C CA . GLY A 1 247 ? 7.522 50.721 31.404 1.00 33.05 ? 288 GLY A CA 1 ATOM 1937 C C . GLY A 1 247 ? 8.022 49.482 30.667 1.00 32.82 ? 288 GLY A C 1 ATOM 1938 O O . GLY A 1 247 ? 9.193 49.125 30.826 1.00 32.06 ? 288 GLY A O 1 ATOM 1939 N N . LEU A 1 248 ? 7.171 48.858 29.847 1.00 32.13 ? 289 LEU A N 1 ATOM 1940 C CA . LEU A 1 248 ? 7.564 47.640 29.127 1.00 32.39 ? 289 LEU A CA 1 ATOM 1941 C C . LEU A 1 248 ? 8.480 47.945 27.948 1.00 33.47 ? 289 LEU A C 1 ATOM 1942 O O . LEU A 1 248 ? 8.241 48.892 27.189 1.00 33.51 ? 289 LEU A O 1 ATOM 1943 C CB A LEU A 1 248 ? 6.338 46.865 28.627 0.65 32.46 ? 289 LEU A CB 1 ATOM 1944 C CB B LEU A 1 248 ? 6.345 46.871 28.614 0.35 32.60 ? 289 LEU A CB 1 ATOM 1945 C CG A LEU A 1 248 ? 5.208 46.592 29.626 0.65 33.56 ? 289 LEU A CG 1 ATOM 1946 C CG B LEU A 1 248 ? 5.669 45.857 29.532 0.35 33.04 ? 289 LEU A CG 1 ATOM 1947 C CD1 A LEU A 1 248 ? 4.053 45.900 28.921 0.65 33.78 ? 289 LEU A CD1 1 ATOM 1948 C CD1 B LEU A 1 248 ? 4.995 46.558 30.734 0.35 32.36 ? 289 LEU A CD1 1 ATOM 1949 C CD2 A LEU A 1 248 ? 5.727 45.715 30.782 0.65 32.15 ? 289 LEU A CD2 1 ATOM 1950 C CD2 B LEU A 1 248 ? 4.665 45.048 28.714 0.35 31.91 ? 289 LEU A CD2 1 ATOM 1951 N N . PRO A 1 249 ? 9.490 47.091 27.741 1.00 34.25 ? 290 PRO A N 1 ATOM 1952 C CA . PRO A 1 249 ? 10.358 47.278 26.576 1.00 34.88 ? 290 PRO A CA 1 ATOM 1953 C C . PRO A 1 249 ? 9.657 46.901 25.275 1.00 35.54 ? 290 PRO A C 1 ATOM 1954 O O . PRO A 1 249 ? 8.768 46.035 25.253 1.00 35.68 ? 290 PRO A O 1 ATOM 1955 C CB . PRO A 1 249 ? 11.542 46.330 26.858 1.00 36.00 ? 290 PRO A CB 1 ATOM 1956 C CG . PRO A 1 249 ? 10.971 45.257 27.755 1.00 35.21 ? 290 PRO A CG 1 ATOM 1957 C CD . PRO A 1 249 ? 9.843 45.908 28.550 1.00 34.56 ? 290 PRO A CD 1 ATOM 1958 N N . SER A 1 250 ? 10.082 47.523 24.186 1.00 35.96 ? 291 SER A N 1 ATOM 1959 C CA A SER A 1 250 ? 9.476 47.299 22.868 0.50 36.83 ? 291 SER A CA 1 ATOM 1960 C CA B SER A 1 250 ? 9.460 47.261 22.890 0.50 37.01 ? 291 SER A CA 1 ATOM 1961 C C . SER A 1 250 ? 10.286 46.330 22.002 1.00 37.07 ? 291 SER A C 1 ATOM 1962 O O . SER A 1 250 ? 9.858 45.951 20.911 1.00 37.85 ? 291 SER A O 1 ATOM 1963 C CB A SER A 1 250 ? 9.269 48.638 22.144 0.50 37.93 ? 291 SER A CB 1 ATOM 1964 C CB B SER A 1 250 ? 9.139 48.581 22.199 0.50 38.13 ? 291 SER A CB 1 ATOM 1965 O OG A SER A 1 250 ? 10.493 49.221 21.740 0.50 38.65 ? 291 SER A OG 1 ATOM 1966 O OG B SER A 1 250 ? 8.072 49.212 22.885 0.50 38.97 ? 291 SER A OG 1 ATOM 1967 N N . ILE A 1 251 ? 11.470 45.933 22.475 1.00 35.67 ? 292 ILE A N 1 ATOM 1968 C CA . ILE A 1 251 ? 12.344 45.011 21.686 1.00 35.77 ? 292 ILE A CA 1 ATOM 1969 C C . ILE A 1 251 ? 12.751 43.827 22.545 1.00 35.01 ? 292 ILE A C 1 ATOM 1970 O O . ILE A 1 251 ? 12.839 43.959 23.764 1.00 34.66 ? 292 ILE A O 1 ATOM 1971 C CB . ILE A 1 251 ? 13.610 45.725 21.111 1.00 36.09 ? 292 ILE A CB 1 ATOM 1972 C CG1 . ILE A 1 251 ? 14.410 46.410 22.214 1.00 34.78 ? 292 ILE A CG1 1 ATOM 1973 C CG2 . ILE A 1 251 ? 13.191 46.736 20.021 1.00 38.83 ? 292 ILE A CG2 1 ATOM 1974 C CD1 . ILE A 1 251 ? 15.742 47.091 21.707 1.00 39.70 ? 292 ILE A CD1 1 ATOM 1975 N N . PRO A 1 252 ? 12.947 42.654 21.940 1.00 35.48 ? 293 PRO A N 1 ATOM 1976 C CA . PRO A 1 252 ? 13.334 41.478 22.763 1.00 35.07 ? 293 PRO A CA 1 ATOM 1977 C C . PRO A 1 252 ? 14.736 41.598 23.373 1.00 33.90 ? 293 PRO A C 1 ATOM 1978 O O . PRO A 1 252 ? 15.645 42.224 22.764 1.00 33.82 ? 293 PRO A O 1 ATOM 1979 C CB . PRO A 1 252 ? 13.353 40.334 21.746 1.00 36.05 ? 293 PRO A CB 1 ATOM 1980 C CG . PRO A 1 252 ? 12.438 40.816 20.621 1.00 37.35 ? 293 PRO A CG 1 ATOM 1981 C CD . PRO A 1 252 ? 12.677 42.278 20.536 1.00 36.55 ? 293 PRO A CD 1 ATOM 1982 N N . VAL A 1 253 ? 14.898 40.975 24.544 1.00 32.32 ? 294 VAL A N 1 ATOM 1983 C CA . VAL A 1 253 ? 16.131 41.082 25.352 1.00 30.76 ? 294 VAL A CA 1 ATOM 1984 C C . VAL A 1 253 ? 16.386 39.713 25.991 1.00 30.45 ? 294 VAL A C 1 ATOM 1985 O O . VAL A 1 253 ? 15.450 39.042 26.444 1.00 29.58 ? 294 VAL A O 1 ATOM 1986 C CB . VAL A 1 253 ? 15.984 42.130 26.480 1.00 30.62 ? 294 VAL A CB 1 ATOM 1987 C CG1 . VAL A 1 253 ? 17.305 42.299 27.234 1.00 29.63 ? 294 VAL A CG1 1 ATOM 1988 C CG2 . VAL A 1 253 ? 15.530 43.512 25.905 1.00 29.98 ? 294 VAL A CG2 1 ATOM 1989 N N . HIS A 1 254 ? 17.651 39.293 26.045 1.00 30.29 ? 295 HIS A N 1 ATOM 1990 C CA . HIS A 1 254 ? 17.997 38.018 26.675 1.00 29.81 ? 295 HIS A CA 1 ATOM 1991 C C . HIS A 1 254 ? 19.423 38.101 27.258 1.00 30.14 ? 295 HIS A C 1 ATOM 1992 O O . HIS A 1 254 ? 20.308 38.704 26.618 1.00 31.71 ? 295 HIS A O 1 ATOM 1993 C CB . HIS A 1 254 ? 17.897 36.899 25.618 1.00 31.24 ? 295 HIS A CB 1 ATOM 1994 C CG . HIS A 1 254 ? 17.935 35.509 26.189 1.00 31.35 ? 295 HIS A CG 1 ATOM 1995 N ND1 . HIS A 1 254 ? 16.965 35.038 27.047 1.00 29.90 ? 295 HIS A ND1 1 ATOM 1996 C CD2 . HIS A 1 254 ? 18.840 34.504 26.047 1.00 32.06 ? 295 HIS A CD2 1 ATOM 1997 C CE1 . HIS A 1 254 ? 17.260 33.796 27.404 1.00 31.56 ? 295 HIS A CE1 1 ATOM 1998 N NE2 . HIS A 1 254 ? 18.396 33.449 26.820 1.00 32.20 ? 295 HIS A NE2 1 ATOM 1999 N N . PRO A 1 255 ? 19.646 37.529 28.458 1.00 28.92 ? 296 PRO A N 1 ATOM 2000 C CA . PRO A 1 255 ? 20.991 37.549 29.055 1.00 28.43 ? 296 PRO A CA 1 ATOM 2001 C C . PRO A 1 255 ? 21.699 36.198 28.858 1.00 29.06 ? 296 PRO A C 1 ATOM 2002 O O . PRO A 1 255 ? 21.052 35.129 28.840 1.00 28.90 ? 296 PRO A O 1 ATOM 2003 C CB . PRO A 1 255 ? 20.703 37.751 30.550 1.00 27.99 ? 296 PRO A CB 1 ATOM 2004 C CG . PRO A 1 255 ? 19.324 36.975 30.763 1.00 28.33 ? 296 PRO A CG 1 ATOM 2005 C CD . PRO A 1 255 ? 18.645 36.902 29.358 1.00 28.21 ? 296 PRO A CD 1 ATOM 2006 N N . ILE A 1 256 ? 23.020 36.256 28.753 1.00 29.99 ? 297 ILE A N 1 ATOM 2007 C CA . ILE A 1 256 ? 23.846 35.069 28.548 1.00 29.82 ? 297 ILE A CA 1 ATOM 2008 C C . ILE A 1 256 ? 25.129 35.175 29.385 1.00 30.39 ? 297 ILE A C 1 ATOM 2009 O O . ILE A 1 256 ? 25.494 36.278 29.866 1.00 29.48 ? 297 ILE A O 1 ATOM 2010 C CB . ILE A 1 256 ? 24.227 34.883 27.036 1.00 31.32 ? 297 ILE A CB 1 ATOM 2011 C CG1 . ILE A 1 256 ? 25.100 36.054 26.505 1.00 31.49 ? 297 ILE A CG1 1 ATOM 2012 C CG2 . ILE A 1 256 ? 22.962 34.592 26.161 1.00 30.24 ? 297 ILE A CG2 1 ATOM 2013 C CD1 . ILE A 1 256 ? 25.549 35.870 25.039 1.00 30.87 ? 297 ILE A CD1 1 ATOM 2014 N N . GLY A 1 257 ? 25.847 34.054 29.481 1.00 30.14 ? 298 GLY A N 1 ATOM 2015 C CA . GLY A 1 257 ? 27.087 33.990 30.224 1.00 30.03 ? 298 GLY A CA 1 ATOM 2016 C C . GLY A 1 257 ? 28.268 34.238 29.303 1.00 31.94 ? 298 GLY A C 1 ATOM 2017 O O . GLY A 1 257 ? 28.090 34.397 28.079 1.00 31.14 ? 298 GLY A O 1 ATOM 2018 N N . TYR A 1 258 ? 29.459 34.303 29.878 1.00 31.66 ? 299 TYR A N 1 ATOM 2019 C CA . TYR A 1 258 ? 30.618 34.669 29.072 1.00 34.58 ? 299 TYR A CA 1 ATOM 2020 C C . TYR A 1 258 ? 31.141 33.558 28.142 1.00 35.41 ? 299 TYR A C 1 ATOM 2021 O O . TYR A 1 258 ? 31.844 33.858 27.159 1.00 37.37 ? 299 TYR A O 1 ATOM 2022 C CB . TYR A 1 258 ? 31.735 35.328 29.891 1.00 33.85 ? 299 TYR A CB 1 ATOM 2023 C CG . TYR A 1 258 ? 32.312 34.569 31.056 1.00 32.48 ? 299 TYR A CG 1 ATOM 2024 C CD1 . TYR A 1 258 ? 31.871 34.840 32.372 1.00 32.46 ? 299 TYR A CD1 1 ATOM 2025 C CD2 . TYR A 1 258 ? 33.365 33.662 30.875 1.00 37.19 ? 299 TYR A CD2 1 ATOM 2026 C CE1 . TYR A 1 258 ? 32.426 34.171 33.475 1.00 32.96 ? 299 TYR A CE1 1 ATOM 2027 C CE2 . TYR A 1 258 ? 33.927 32.994 31.968 1.00 37.54 ? 299 TYR A CE2 1 ATOM 2028 C CZ . TYR A 1 258 ? 33.463 33.274 33.259 1.00 32.80 ? 299 TYR A CZ 1 ATOM 2029 O OH . TYR A 1 258 ? 34.006 32.628 34.353 1.00 33.07 ? 299 TYR A OH 1 ATOM 2030 N N . TYR A 1 259 ? 30.813 32.290 28.403 1.00 35.89 ? 300 TYR A N 1 ATOM 2031 C CA . TYR A 1 259 ? 31.154 31.267 27.391 1.00 37.68 ? 300 TYR A CA 1 ATOM 2032 C C . TYR A 1 259 ? 30.392 31.503 26.080 1.00 38.43 ? 300 TYR A C 1 ATOM 2033 O O . TYR A 1 259 ? 30.975 31.411 24.988 1.00 39.59 ? 300 TYR A O 1 ATOM 2034 C CB . TYR A 1 259 ? 30.852 29.842 27.858 1.00 37.86 ? 300 TYR A CB 1 ATOM 2035 C CG . TYR A 1 259 ? 31.768 29.300 28.924 1.00 39.79 ? 300 TYR A CG 1 ATOM 2036 C CD1 . TYR A 1 259 ? 33.080 29.803 29.091 1.00 41.54 ? 300 TYR A CD1 1 ATOM 2037 C CD2 . TYR A 1 259 ? 31.340 28.247 29.753 1.00 38.96 ? 300 TYR A CD2 1 ATOM 2038 C CE1 . TYR A 1 259 ? 33.926 29.274 30.055 1.00 44.25 ? 300 TYR A CE1 1 ATOM 2039 C CE2 . TYR A 1 259 ? 32.175 27.721 30.725 1.00 42.66 ? 300 TYR A CE2 1 ATOM 2040 C CZ . TYR A 1 259 ? 33.466 28.234 30.866 1.00 45.41 ? 300 TYR A CZ 1 ATOM 2041 O OH . TYR A 1 259 ? 34.282 27.718 31.840 1.00 46.92 ? 300 TYR A OH 1 ATOM 2042 N N . ASP A 1 260 ? 29.093 31.790 26.197 1.00 36.76 ? 301 ASP A N 1 ATOM 2043 C CA . ASP A 1 260 ? 28.253 32.081 25.031 1.00 38.52 ? 301 ASP A CA 1 ATOM 2044 C C . ASP A 1 260 ? 28.590 33.445 24.395 1.00 38.29 ? 301 ASP A C 1 ATOM 2045 O O . ASP A 1 260 ? 28.587 33.578 23.164 1.00 39.44 ? 301 ASP A O 1 ATOM 2046 C CB . ASP A 1 260 ? 26.760 32.032 25.400 1.00 37.06 ? 301 ASP A CB 1 ATOM 2047 C CG . ASP A 1 260 ? 26.242 30.601 25.615 1.00 38.18 ? 301 ASP A CG 1 ATOM 2048 O OD1 . ASP A 1 260 ? 26.880 29.624 25.157 1.00 40.86 ? 301 ASP A OD1 1 ATOM 2049 O OD2 . ASP A 1 260 ? 25.150 30.453 26.237 1.00 38.76 ? 301 ASP A OD2 1 ATOM 2050 N N . ALA A 1 261 ? 28.850 34.450 25.238 1.00 37.59 ? 302 ALA A N 1 ATOM 2051 C CA . ALA A 1 261 ? 29.269 35.781 24.763 1.00 37.12 ? 302 ALA A CA 1 ATOM 2052 C C . ALA A 1 261 ? 30.522 35.724 23.901 1.00 38.53 ? 302 ALA A C 1 ATOM 2053 O O . ALA A 1 261 ? 30.605 36.385 22.866 1.00 38.97 ? 302 ALA A O 1 ATOM 2054 C CB . ALA A 1 261 ? 29.493 36.724 25.942 1.00 36.18 ? 302 ALA A CB 1 ATOM 2055 N N . GLN A 1 262 ? 31.500 34.962 24.352 1.00 38.87 ? 303 GLN A N 1 ATOM 2056 C CA . GLN A 1 262 ? 32.728 34.733 23.592 1.00 41.72 ? 303 GLN A CA 1 ATOM 2057 C C . GLN A 1 262 ? 32.449 34.265 22.135 1.00 42.80 ? 303 GLN A C 1 ATOM 2058 O O . GLN A 1 262 ? 33.069 34.758 21.166 1.00 43.87 ? 303 GLN A O 1 ATOM 2059 C CB . GLN A 1 262 ? 33.568 33.730 24.365 1.00 41.74 ? 303 GLN A CB 1 ATOM 2060 C CG . GLN A 1 262 ? 34.750 33.154 23.586 1.00 48.12 ? 303 GLN A CG 1 ATOM 2061 C CD . GLN A 1 262 ? 36.088 33.627 24.082 1.00 52.23 ? 303 GLN A CD 1 ATOM 2062 O OE1 . GLN A 1 262 ? 37.044 33.709 23.306 1.00 59.76 ? 303 GLN A OE1 1 ATOM 2063 N NE2 . GLN A 1 262 ? 36.198 33.863 25.377 1.00 50.07 ? 303 GLN A NE2 1 ATOM 2064 N N . LYS A 1 263 ? 31.509 33.329 21.987 1.00 42.94 ? 304 LYS A N 1 ATOM 2065 C CA . LYS A 1 263 ? 31.143 32.801 20.689 1.00 44.32 ? 304 LYS A CA 1 ATOM 2066 C C . LYS A 1 263 ? 30.513 33.875 19.799 1.00 45.07 ? 304 LYS A C 1 ATOM 2067 O O . LYS A 1 263 ? 30.759 33.903 18.597 1.00 46.38 ? 304 LYS A O 1 ATOM 2068 C CB . LYS A 1 263 ? 30.222 31.593 20.836 1.00 44.68 ? 304 LYS A CB 1 ATOM 2069 C CG . LYS A 1 263 ? 30.804 30.454 21.675 1.00 46.52 ? 304 LYS A CG 1 ATOM 2070 C CD . LYS A 1 263 ? 32.026 29.787 21.023 1.00 52.81 ? 304 LYS A CD 1 ATOM 2071 C CE . LYS A 1 263 ? 31.626 29.077 19.759 1.00 56.70 ? 304 LYS A CE 1 ATOM 2072 N NZ . LYS A 1 263 ? 32.508 27.918 19.455 1.00 62.76 ? 304 LYS A NZ 1 ATOM 2073 N N . LEU A 1 264 ? 29.724 34.770 20.394 1.00 42.73 ? 305 LEU A N 1 ATOM 2074 C CA . LEU A 1 264 ? 29.107 35.864 19.645 1.00 43.75 ? 305 LEU A CA 1 ATOM 2075 C C . LEU A 1 264 ? 30.061 37.007 19.337 1.00 43.98 ? 305 LEU A C 1 ATOM 2076 O O . LEU A 1 264 ? 29.939 37.623 18.283 1.00 46.27 ? 305 LEU A O 1 ATOM 2077 C CB . LEU A 1 264 ? 27.849 36.423 20.363 1.00 41.76 ? 305 LEU A CB 1 ATOM 2078 C CG . LEU A 1 264 ? 26.720 35.424 20.648 1.00 43.09 ? 305 LEU A CG 1 ATOM 2079 C CD1 . LEU A 1 264 ? 25.528 36.055 21.440 1.00 42.80 ? 305 LEU A CD1 1 ATOM 2080 C CD2 . LEU A 1 264 ? 26.209 34.735 19.386 1.00 44.99 ? 305 LEU A CD2 1 ATOM 2081 N N . LEU A 1 265 ? 30.989 37.307 20.243 1.00 42.19 ? 306 LEU A N 1 ATOM 2082 C CA . LEU A 1 265 ? 31.862 38.455 20.056 1.00 42.24 ? 306 LEU A CA 1 ATOM 2083 C C . LEU A 1 265 ? 33.070 38.154 19.174 1.00 44.61 ? 306 LEU A C 1 ATOM 2084 O O . LEU A 1 265 ? 33.673 39.071 18.600 1.00 44.95 ? 306 LEU A O 1 ATOM 2085 C CB . LEU A 1 265 ? 32.364 38.943 21.378 1.00 40.28 ? 306 LEU A CB 1 ATOM 2086 C CG . LEU A 1 265 ? 31.269 39.503 22.315 1.00 40.79 ? 306 LEU A CG 1 ATOM 2087 C CD1 . LEU A 1 265 ? 31.878 39.663 23.691 1.00 42.37 ? 306 LEU A CD1 1 ATOM 2088 C CD2 . LEU A 1 265 ? 30.697 40.828 21.836 1.00 41.42 ? 306 LEU A CD2 1 ATOM 2089 N N . GLU A 1 266 ? 33.459 36.882 19.118 1.00 46.07 ? 307 GLU A N 1 ATOM 2090 C CA . GLU A 1 266 ? 34.772 36.550 18.541 1.00 48.06 ? 307 GLU A CA 1 ATOM 2091 C C . GLU A 1 266 ? 34.838 36.850 17.040 1.00 49.83 ? 307 GLU A C 1 ATOM 2092 O O . GLU A 1 266 ? 35.911 37.131 16.511 1.00 50.67 ? 307 GLU A O 1 ATOM 2093 C CB . GLU A 1 266 ? 35.200 35.119 18.870 1.00 48.92 ? 307 GLU A CB 1 ATOM 2094 C CG . GLU A 1 266 ? 34.324 34.055 18.253 1.00 51.41 ? 307 GLU A CG 1 ATOM 2095 C CD . GLU A 1 266 ? 34.709 32.644 18.681 1.00 56.76 ? 307 GLU A CD 1 ATOM 2096 O OE1 . GLU A 1 266 ? 35.661 32.476 19.486 1.00 59.26 ? 307 GLU A OE1 1 ATOM 2097 O OE2 . GLU A 1 266 ? 34.045 31.696 18.202 1.00 56.89 ? 307 GLU A OE2 1 ATOM 2098 N N . LYS A 1 267 ? 33.684 36.829 16.376 1.00 50.30 ? 308 LYS A N 1 ATOM 2099 C CA . LYS A 1 267 ? 33.615 37.076 14.932 1.00 51.92 ? 308 LYS A CA 1 ATOM 2100 C C . LYS A 1 267 ? 33.355 38.552 14.564 1.00 51.80 ? 308 LYS A C 1 ATOM 2101 O O . LYS A 1 267 ? 33.317 38.898 13.386 1.00 52.33 ? 308 LYS A O 1 ATOM 2102 C CB . LYS A 1 267 ? 32.539 36.179 14.316 1.00 52.27 ? 308 LYS A CB 1 ATOM 2103 C CG . LYS A 1 267 ? 32.927 34.720 14.264 1.00 55.11 ? 308 LYS A CG 1 ATOM 2104 C CD . LYS A 1 267 ? 31.739 33.815 13.972 1.00 54.99 ? 308 LYS A CD 1 ATOM 2105 C CE . LYS A 1 267 ? 32.227 32.429 13.552 1.00 57.74 ? 308 LYS A CE 1 ATOM 2106 N NZ . LYS A 1 267 ? 31.099 31.503 13.241 1.00 56.68 ? 308 LYS A NZ 1 ATOM 2107 N N . MET A 1 268 ? 33.187 39.419 15.566 1.00 50.53 ? 309 MET A N 1 ATOM 2108 C CA . MET A 1 268 ? 32.880 40.856 15.319 1.00 50.51 ? 309 MET A CA 1 ATOM 2109 C C . MET A 1 268 ? 33.914 41.656 14.469 1.00 52.07 ? 309 MET A C 1 ATOM 2110 O O . MET A 1 268 ? 35.107 41.618 14.735 1.00 51.96 ? 309 MET A O 1 ATOM 2111 C CB . MET A 1 268 ? 32.596 41.562 16.631 1.00 48.80 ? 309 MET A CB 1 ATOM 2112 C CG A MET A 1 268 ? 31.250 41.018 17.159 0.50 47.60 ? 309 MET A CG 1 ATOM 2113 C CG B MET A 1 268 ? 31.379 41.107 17.395 0.50 48.08 ? 309 MET A CG 1 ATOM 2114 S SD A MET A 1 268 ? 30.232 41.997 18.255 0.50 43.63 ? 309 MET A SD 1 ATOM 2115 S SD B MET A 1 268 ? 29.922 41.574 16.498 0.50 46.60 ? 309 MET A SD 1 ATOM 2116 C CE A MET A 1 268 ? 30.094 43.563 17.383 0.50 46.22 ? 309 MET A CE 1 ATOM 2117 C CE B MET A 1 268 ? 30.029 43.363 16.497 0.50 48.69 ? 309 MET A CE 1 ATOM 2118 N N . GLY A 1 269 ? 33.407 42.395 13.477 1.00 53.31 ? 310 GLY A N 1 ATOM 2119 C CA . GLY A 1 269 ? 34.223 43.195 12.549 1.00 55.98 ? 310 GLY A CA 1 ATOM 2120 C C . GLY A 1 269 ? 33.945 44.688 12.682 1.00 56.32 ? 310 GLY A C 1 ATOM 2121 O O . GLY A 1 269 ? 33.731 45.182 13.802 1.00 54.57 ? 310 GLY A O 1 ATOM 2122 N N . GLY A 1 270 ? 33.957 45.413 11.554 1.00 57.82 ? 311 GLY A N 1 ATOM 2123 C CA . GLY A 1 270 ? 33.740 46.869 11.587 1.00 57.97 ? 311 GLY A CA 1 ATOM 2124 C C . GLY A 1 270 ? 34.833 47.534 12.409 1.00 58.34 ? 311 GLY A C 1 ATOM 2125 O O . GLY A 1 270 ? 35.958 47.053 12.429 1.00 58.57 ? 311 GLY A O 1 ATOM 2126 N N . SER A 1 271 ? 34.500 48.607 13.123 1.00 57.51 ? 312 SER A N 1 ATOM 2127 C CA . SER A 1 271 ? 35.511 49.430 13.822 1.00 58.25 ? 312 SER A CA 1 ATOM 2128 C C . SER A 1 271 ? 36.151 48.779 15.052 1.00 57.15 ? 312 SER A C 1 ATOM 2129 O O . SER A 1 271 ? 35.493 48.045 15.782 1.00 55.36 ? 312 SER A O 1 ATOM 2130 C CB . SER A 1 271 ? 34.888 50.764 14.262 1.00 57.76 ? 312 SER A CB 1 ATOM 2131 O OG . SER A 1 271 ? 34.388 51.479 13.143 1.00 60.92 ? 312 SER A OG 1 ATOM 2132 N N . ALA A 1 272 ? 37.429 49.070 15.276 1.00 56.85 ? 313 ALA A N 1 ATOM 2133 C CA . ALA A 1 272 ? 38.104 48.769 16.540 1.00 56.05 ? 313 ALA A CA 1 ATOM 2134 C C . ALA A 1 272 ? 37.366 49.428 17.724 1.00 54.58 ? 313 ALA A C 1 ATOM 2135 O O . ALA A 1 272 ? 36.707 50.456 17.535 1.00 54.00 ? 313 ALA A O 1 ATOM 2136 C CB . ALA A 1 272 ? 39.556 49.281 16.482 1.00 57.22 ? 313 ALA A CB 1 ATOM 2137 N N . PRO A 1 273 ? 37.486 48.861 18.950 1.00 53.90 ? 314 PRO A N 1 ATOM 2138 C CA . PRO A 1 273 ? 36.914 49.599 20.109 1.00 52.62 ? 314 PRO A CA 1 ATOM 2139 C C . PRO A 1 273 ? 37.584 50.987 20.165 1.00 54.05 ? 314 PRO A C 1 ATOM 2140 O O . PRO A 1 273 ? 38.731 51.104 19.749 1.00 54.47 ? 314 PRO A O 1 ATOM 2141 C CB . PRO A 1 273 ? 37.295 48.743 21.321 1.00 51.09 ? 314 PRO A CB 1 ATOM 2142 C CG . PRO A 1 273 ? 38.441 47.850 20.836 1.00 52.77 ? 314 PRO A CG 1 ATOM 2143 C CD . PRO A 1 273 ? 38.267 47.671 19.354 1.00 53.65 ? 314 PRO A CD 1 ATOM 2144 N N . PRO A 1 274 ? 36.868 52.037 20.622 1.00 53.96 ? 315 PRO A N 1 ATOM 2145 C CA . PRO A 1 274 ? 37.498 53.379 20.534 1.00 55.55 ? 315 PRO A CA 1 ATOM 2146 C C . PRO A 1 274 ? 38.665 53.594 21.501 1.00 56.30 ? 315 PRO A C 1 ATOM 2147 O O . PRO A 1 274 ? 39.536 54.430 21.245 1.00 57.49 ? 315 PRO A O 1 ATOM 2148 C CB . PRO A 1 274 ? 36.338 54.341 20.860 1.00 54.11 ? 315 PRO A CB 1 ATOM 2149 C CG . PRO A 1 274 ? 35.342 53.488 21.644 1.00 52.51 ? 315 PRO A CG 1 ATOM 2150 C CD . PRO A 1 274 ? 35.446 52.121 20.998 1.00 52.56 ? 315 PRO A CD 1 ATOM 2151 N N . ASP A 1 275 ? 38.659 52.859 22.607 1.00 56.33 ? 316 ASP A N 1 ATOM 2152 C CA . ASP A 1 275 ? 39.733 52.907 23.608 1.00 57.21 ? 316 ASP A CA 1 ATOM 2153 C C . ASP A 1 275 ? 39.625 51.716 24.578 1.00 56.14 ? 316 ASP A C 1 ATOM 2154 O O . ASP A 1 275 ? 38.647 50.947 24.530 1.00 54.83 ? 316 ASP A O 1 ATOM 2155 C CB . ASP A 1 275 ? 39.767 54.276 24.349 1.00 57.59 ? 316 ASP A CB 1 ATOM 2156 C CG . ASP A 1 275 ? 38.520 54.536 25.204 1.00 57.81 ? 316 ASP A CG 1 ATOM 2157 O OD1 . ASP A 1 275 ? 38.259 53.751 26.132 1.00 60.27 ? 316 ASP A OD1 1 ATOM 2158 O OD2 . ASP A 1 275 ? 37.814 55.549 24.987 1.00 60.85 ? 316 ASP A OD2 1 ATOM 2159 N N . SER A 1 276 ? 40.613 51.588 25.466 1.00 55.73 ? 317 SER A N 1 ATOM 2160 C CA . SER A 1 276 ? 40.720 50.449 26.391 1.00 55.72 ? 317 SER A CA 1 ATOM 2161 C C . SER A 1 276 ? 39.543 50.292 27.390 1.00 53.26 ? 317 SER A C 1 ATOM 2162 O O . SER A 1 276 ? 39.317 49.189 27.907 1.00 53.59 ? 317 SER A O 1 ATOM 2163 C CB . SER A 1 276 ? 42.035 50.539 27.168 1.00 56.75 ? 317 SER A CB 1 ATOM 2164 O OG . SER A 1 276 ? 41.908 51.513 28.195 1.00 58.22 ? 317 SER A OG 1 ATOM 2165 N N . SER A 1 277 ? 38.808 51.372 27.678 1.00 51.72 ? 318 SER A N 1 ATOM 2166 C CA . SER A 1 277 ? 37.656 51.279 28.602 1.00 49.16 ? 318 SER A CA 1 ATOM 2167 C C . SER A 1 277 ? 36.478 50.491 28.008 1.00 48.43 ? 318 SER A C 1 ATOM 2168 O O . SER A 1 277 ? 35.483 50.222 28.712 1.00 47.34 ? 318 SER A O 1 ATOM 2169 C CB . SER A 1 277 ? 37.166 52.673 29.053 1.00 49.26 ? 318 SER A CB 1 ATOM 2170 O OG . SER A 1 277 ? 36.528 53.367 27.989 1.00 47.30 ? 318 SER A OG 1 ATOM 2171 N N . TRP A 1 278 ? 36.578 50.191 26.710 1.00 47.31 ? 319 TRP A N 1 ATOM 2172 C CA . TRP A 1 278 ? 35.595 49.412 25.966 1.00 46.28 ? 319 TRP A CA 1 ATOM 2173 C C . TRP A 1 278 ? 35.954 47.913 25.888 1.00 47.00 ? 319 TRP A C 1 ATOM 2174 O O . TRP A 1 278 ? 35.120 47.114 25.459 1.00 46.95 ? 319 TRP A O 1 ATOM 2175 C CB . TRP A 1 278 ? 35.418 49.989 24.546 1.00 46.36 ? 319 TRP A CB 1 ATOM 2176 C CG . TRP A 1 278 ? 34.442 51.158 24.490 1.00 44.69 ? 319 TRP A CG 1 ATOM 2177 C CD1 . TRP A 1 278 ? 34.548 52.362 25.163 1.00 43.57 ? 319 TRP A CD1 1 ATOM 2178 C CD2 . TRP A 1 278 ? 33.243 51.240 23.708 1.00 42.75 ? 319 TRP A CD2 1 ATOM 2179 N NE1 . TRP A 1 278 ? 33.457 53.163 24.878 1.00 43.88 ? 319 TRP A NE1 1 ATOM 2180 C CE2 . TRP A 1 278 ? 32.646 52.512 23.981 1.00 44.54 ? 319 TRP A CE2 1 ATOM 2181 C CE3 . TRP A 1 278 ? 32.598 50.360 22.819 1.00 43.54 ? 319 TRP A CE3 1 ATOM 2182 C CZ2 . TRP A 1 278 ? 31.420 52.920 23.401 1.00 42.51 ? 319 TRP A CZ2 1 ATOM 2183 C CZ3 . TRP A 1 278 ? 31.378 50.761 22.234 1.00 41.51 ? 319 TRP A CZ3 1 ATOM 2184 C CH2 . TRP A 1 278 ? 30.796 52.042 22.548 1.00 42.88 ? 319 TRP A CH2 1 ATOM 2185 N N . ARG A 1 279 ? 37.181 47.552 26.291 1.00 47.37 ? 320 ARG A N 1 ATOM 2186 C CA A ARG A 1 279 ? 37.669 46.165 26.269 0.50 47.81 ? 320 ARG A CA 1 ATOM 2187 C CA B ARG A 1 279 ? 37.632 46.161 26.267 0.50 47.85 ? 320 ARG A CA 1 ATOM 2188 C C . ARG A 1 279 ? 37.435 45.487 27.621 1.00 46.74 ? 320 ARG A C 1 ATOM 2189 O O . ARG A 1 279 ? 37.881 45.993 28.649 1.00 46.57 ? 320 ARG A O 1 ATOM 2190 C CB A ARG A 1 279 ? 39.180 46.116 25.958 0.50 49.52 ? 320 ARG A CB 1 ATOM 2191 C CB B ARG A 1 279 ? 39.109 46.077 25.874 0.50 49.63 ? 320 ARG A CB 1 ATOM 2192 C CG A ARG A 1 279 ? 39.609 46.542 24.551 0.50 51.59 ? 320 ARG A CG 1 ATOM 2193 C CG B ARG A 1 279 ? 39.385 46.243 24.394 0.50 52.00 ? 320 ARG A CG 1 ATOM 2194 C CD A ARG A 1 279 ? 41.066 46.104 24.228 0.50 55.53 ? 320 ARG A CD 1 ATOM 2195 C CD B ARG A 1 279 ? 40.867 46.014 24.094 0.50 56.29 ? 320 ARG A CD 1 ATOM 2196 N NE A ARG A 1 279 ? 41.296 44.700 24.565 0.50 55.80 ? 320 ARG A NE 1 ATOM 2197 N NE B ARG A 1 279 ? 41.686 47.099 24.621 0.50 57.76 ? 320 ARG A NE 1 ATOM 2198 C CZ A ARG A 1 279 ? 41.062 43.683 23.739 0.50 57.05 ? 320 ARG A CZ 1 ATOM 2199 C CZ B ARG A 1 279 ? 42.385 47.929 23.861 0.50 59.43 ? 320 ARG A CZ 1 ATOM 2200 N NH1 A ARG A 1 279 ? 40.613 43.917 22.514 0.50 58.68 ? 320 ARG A NH1 1 ATOM 2201 N NH1 B ARG A 1 279 ? 42.381 47.779 22.543 0.50 59.93 ? 320 ARG A NH1 1 ATOM 2202 N NH2 A ARG A 1 279 ? 41.271 42.434 24.133 0.50 54.72 ? 320 ARG A NH2 1 ATOM 2203 N NH2 B ARG A 1 279 ? 43.097 48.892 24.418 0.50 60.29 ? 320 ARG A NH2 1 ATOM 2204 N N . GLY A 1 280 ? 36.753 44.341 27.609 1.00 46.02 ? 321 GLY A N 1 ATOM 2205 C CA . GLY A 1 280 ? 36.617 43.473 28.786 1.00 43.94 ? 321 GLY A CA 1 ATOM 2206 C C . GLY A 1 280 ? 37.794 42.504 28.800 1.00 45.44 ? 321 GLY A C 1 ATOM 2207 O O . GLY A 1 280 ? 38.837 42.773 28.158 1.00 45.64 ? 321 GLY A O 1 ATOM 2208 N N . SER A 1 281 ? 37.623 41.371 29.487 1.00 44.22 ? 322 SER A N 1 ATOM 2209 C CA . SER A 1 281 ? 38.707 40.409 29.720 1.00 45.70 ? 322 SER A CA 1 ATOM 2210 C C . SER A 1 281 ? 38.681 39.180 28.822 1.00 45.34 ? 322 SER A C 1 ATOM 2211 O O . SER A 1 281 ? 39.551 38.333 28.924 1.00 47.02 ? 322 SER A O 1 ATOM 2212 C CB . SER A 1 281 ? 38.707 39.967 31.193 1.00 44.95 ? 322 SER A CB 1 ATOM 2213 O OG . SER A 1 281 ? 39.035 41.073 32.023 1.00 48.08 ? 322 SER A OG 1 ATOM 2214 N N . LEU A 1 282 ? 37.710 39.069 27.933 1.00 44.15 ? 323 LEU A N 1 ATOM 2215 C CA . LEU A 1 282 ? 37.690 37.913 27.031 1.00 44.10 ? 323 LEU A CA 1 ATOM 2216 C C . LEU A 1 282 ? 38.749 38.057 25.924 1.00 46.62 ? 323 LEU A C 1 ATOM 2217 O O . LEU A 1 282 ? 39.170 39.168 25.590 1.00 45.94 ? 323 LEU A O 1 ATOM 2218 C CB . LEU A 1 282 ? 36.302 37.714 26.396 1.00 43.15 ? 323 LEU A CB 1 ATOM 2219 C CG . LEU A 1 282 ? 35.102 37.516 27.345 1.00 40.22 ? 323 LEU A CG 1 ATOM 2220 C CD1 . LEU A 1 282 ? 33.762 37.551 26.553 1.00 35.87 ? 323 LEU A CD1 1 ATOM 2221 C CD2 . LEU A 1 282 ? 35.264 36.194 28.103 1.00 41.27 ? 323 LEU A CD2 1 ATOM 2222 N N . LYS A 1 283 ? 39.102 36.925 25.334 1.00 47.93 ? 324 LYS A N 1 ATOM 2223 C CA . LYS A 1 283 ? 40.082 36.866 24.270 1.00 51.28 ? 324 LYS A CA 1 ATOM 2224 C C . LYS A 1 283 ? 39.404 37.157 22.954 1.00 51.07 ? 324 LYS A C 1 ATOM 2225 O O . LYS A 1 283 ? 39.328 36.303 22.080 1.00 50.97 ? 324 LYS A O 1 ATOM 2226 C CB . LYS A 1 283 ? 40.743 35.481 24.248 1.00 53.55 ? 324 LYS A CB 1 ATOM 2227 C CG . LYS A 1 283 ? 41.482 35.167 25.541 1.00 57.76 ? 324 LYS A CG 1 ATOM 2228 C CD . LYS A 1 283 ? 42.643 36.151 25.740 1.00 64.86 ? 324 LYS A CD 1 ATOM 2229 C CE . LYS A 1 283 ? 42.668 36.718 27.165 1.00 66.05 ? 324 LYS A CE 1 ATOM 2230 N NZ . LYS A 1 283 ? 43.912 37.529 27.374 1.00 66.61 ? 324 LYS A NZ 1 ATOM 2231 N N . VAL A 1 284 ? 38.877 38.374 22.844 1.00 49.26 ? 325 VAL A N 1 ATOM 2232 C CA . VAL A 1 284 ? 38.238 38.833 21.624 1.00 49.42 ? 325 VAL A CA 1 ATOM 2233 C C . VAL A 1 284 ? 38.703 40.271 21.365 1.00 49.55 ? 325 VAL A C 1 ATOM 2234 O O . VAL A 1 284 ? 39.232 40.922 22.274 1.00 48.92 ? 325 VAL A O 1 ATOM 2235 C CB . VAL A 1 284 ? 36.669 38.747 21.709 1.00 47.54 ? 325 VAL A CB 1 ATOM 2236 C CG1 . VAL A 1 284 ? 36.195 37.290 21.898 1.00 48.23 ? 325 VAL A CG1 1 ATOM 2237 C CG2 . VAL A 1 284 ? 36.109 39.656 22.826 1.00 44.96 ? 325 VAL A CG2 1 ATOM 2238 N N . PRO A 1 285 ? 38.515 40.771 20.131 1.00 50.84 ? 326 PRO A N 1 ATOM 2239 C CA . PRO A 1 285 ? 39.001 42.134 19.857 1.00 51.26 ? 326 PRO A CA 1 ATOM 2240 C C . PRO A 1 285 ? 38.121 43.243 20.453 1.00 49.56 ? 326 PRO A C 1 ATOM 2241 O O . PRO A 1 285 ? 38.600 44.373 20.600 1.00 49.79 ? 326 PRO A O 1 ATOM 2242 C CB . PRO A 1 285 ? 39.005 42.216 18.319 1.00 52.61 ? 326 PRO A CB 1 ATOM 2243 C CG . PRO A 1 285 ? 38.012 41.131 17.866 1.00 54.00 ? 326 PRO A CG 1 ATOM 2244 C CD . PRO A 1 285 ? 38.124 40.041 18.901 1.00 51.99 ? 326 PRO A CD 1 ATOM 2245 N N . TYR A 1 286 ? 36.874 42.915 20.816 1.00 47.80 ? 327 TYR A N 1 ATOM 2246 C CA . TYR A 1 286 ? 35.881 43.912 21.249 1.00 46.52 ? 327 TYR A CA 1 ATOM 2247 C C . TYR A 1 286 ? 35.618 44.941 20.146 1.00 47.31 ? 327 TYR A C 1 ATOM 2248 O O . TYR A 1 286 ? 35.388 46.129 20.417 1.00 47.28 ? 327 TYR A O 1 ATOM 2249 C CB . TYR A 1 286 ? 36.258 44.566 22.587 1.00 45.42 ? 327 TYR A CB 1 ATOM 2250 C CG . TYR A 1 286 ? 36.135 43.600 23.734 1.00 43.84 ? 327 TYR A CG 1 ATOM 2251 C CD1 . TYR A 1 286 ? 34.892 43.398 24.368 1.00 42.32 ? 327 TYR A CD1 1 ATOM 2252 C CD2 . TYR A 1 286 ? 37.234 42.847 24.167 1.00 43.22 ? 327 TYR A CD2 1 ATOM 2253 C CE1 . TYR A 1 286 ? 34.757 42.486 25.427 1.00 41.68 ? 327 TYR A CE1 1 ATOM 2254 C CE2 . TYR A 1 286 ? 37.111 41.935 25.231 1.00 43.50 ? 327 TYR A CE2 1 ATOM 2255 C CZ . TYR A 1 286 ? 35.865 41.763 25.849 1.00 41.18 ? 327 TYR A CZ 1 ATOM 2256 O OH . TYR A 1 286 ? 35.711 40.885 26.899 1.00 41.61 ? 327 TYR A OH 1 ATOM 2257 N N . ASN A 1 287 ? 35.637 44.464 18.899 1.00 47.98 ? 328 ASN A N 1 ATOM 2258 C CA . ASN A 1 287 ? 35.247 45.293 17.766 1.00 48.48 ? 328 ASN A CA 1 ATOM 2259 C C . ASN A 1 287 ? 33.799 45.687 17.943 1.00 47.57 ? 328 ASN A C 1 ATOM 2260 O O . ASN A 1 287 ? 32.998 44.924 18.474 1.00 45.45 ? 328 ASN A O 1 ATOM 2261 C CB . ASN A 1 287 ? 35.422 44.551 16.453 1.00 48.75 ? 328 ASN A CB 1 ATOM 2262 C CG . ASN A 1 287 ? 36.887 44.440 16.028 1.00 51.10 ? 328 ASN A CG 1 ATOM 2263 O OD1 . ASN A 1 287 ? 37.751 45.235 16.438 1.00 50.59 ? 328 ASN A OD1 1 ATOM 2264 N ND2 . ASN A 1 287 ? 37.163 43.455 15.201 1.00 47.33 ? 328 ASN A ND2 1 ATOM 2265 N N . VAL A 1 288 ? 33.477 46.897 17.508 1.00 48.19 ? 329 VAL A N 1 ATOM 2266 C CA . VAL A 1 288 ? 32.151 47.451 17.742 1.00 47.28 ? 329 VAL A CA 1 ATOM 2267 C C . VAL A 1 288 ? 31.162 46.988 16.676 1.00 47.70 ? 329 VAL A C 1 ATOM 2268 O O . VAL A 1 288 ? 29.963 46.971 16.894 1.00 46.38 ? 329 VAL A O 1 ATOM 2269 C CB . VAL A 1 288 ? 32.246 48.970 17.808 1.00 47.07 ? 329 VAL A CB 1 ATOM 2270 C CG1 . VAL A 1 288 ? 30.879 49.592 17.764 1.00 49.42 ? 329 VAL A CG1 1 ATOM 2271 C CG2 . VAL A 1 288 ? 32.969 49.359 19.121 1.00 47.85 ? 329 VAL A CG2 1 ATOM 2272 N N . GLY A 1 289 ? 31.668 46.562 15.523 1.00 49.58 ? 330 GLY A N 1 ATOM 2273 C CA . GLY A 1 289 ? 30.773 46.183 14.434 1.00 51.17 ? 330 GLY A CA 1 ATOM 2274 C C . GLY A 1 289 ? 30.510 47.404 13.575 1.00 52.73 ? 330 GLY A C 1 ATOM 2275 O O . GLY A 1 289 ? 31.343 48.315 13.515 1.00 53.21 ? 330 GLY A O 1 ATOM 2276 N N . PRO A 1 290 ? 29.360 47.439 12.887 1.00 53.54 ? 331 PRO A N 1 ATOM 2277 C CA . PRO A 1 290 ? 28.307 46.425 12.841 1.00 53.02 ? 331 PRO A CA 1 ATOM 2278 C C . PRO A 1 290 ? 28.737 45.166 12.093 1.00 53.46 ? 331 PRO A C 1 ATOM 2279 O O . PRO A 1 290 ? 29.526 45.251 11.151 1.00 53.93 ? 331 PRO A O 1 ATOM 2280 C CB . PRO A 1 290 ? 27.196 47.126 12.054 1.00 53.60 ? 331 PRO A CB 1 ATOM 2281 C CG . PRO A 1 290 ? 27.964 48.010 11.077 1.00 56.28 ? 331 PRO A CG 1 ATOM 2282 C CD . PRO A 1 290 ? 29.174 48.481 11.853 1.00 55.29 ? 331 PRO A CD 1 ATOM 2283 N N . GLY A 1 291 ? 28.219 44.016 12.508 1.00 52.75 ? 332 GLY A N 1 ATOM 2284 C CA . GLY A 1 291 ? 28.411 42.769 11.740 1.00 53.32 ? 332 GLY A CA 1 ATOM 2285 C C . GLY A 1 291 ? 29.729 42.060 12.020 1.00 53.33 ? 332 GLY A C 1 ATOM 2286 O O . GLY A 1 291 ? 30.552 42.552 12.815 1.00 51.91 ? 332 GLY A O 1 ATOM 2287 N N . PHE A 1 292 ? 29.921 40.907 11.363 1.00 53.76 ? 333 PHE A N 1 ATOM 2288 C CA . PHE A 1 292 ? 31.106 40.056 11.547 1.00 54.71 ? 333 PHE A CA 1 ATOM 2289 C C . PHE A 1 292 ? 32.192 40.370 10.503 1.00 56.89 ? 333 PHE A C 1 ATOM 2290 O O . PHE A 1 292 ? 31.890 40.969 9.474 1.00 56.85 ? 333 PHE A O 1 ATOM 2291 C CB . PHE A 1 292 ? 30.727 38.567 11.436 1.00 54.37 ? 333 PHE A CB 1 ATOM 2292 C CG . PHE A 1 292 ? 29.822 38.063 12.552 1.00 53.08 ? 333 PHE A CG 1 ATOM 2293 C CD1 . PHE A 1 292 ? 28.840 37.118 12.282 1.00 53.59 ? 333 PHE A CD1 1 ATOM 2294 C CD2 . PHE A 1 292 ? 29.962 38.520 13.859 1.00 51.11 ? 333 PHE A CD2 1 ATOM 2295 C CE1 . PHE A 1 292 ? 27.999 36.634 13.291 1.00 50.95 ? 333 PHE A CE1 1 ATOM 2296 C CE2 . PHE A 1 292 ? 29.117 38.042 14.890 1.00 49.14 ? 333 PHE A CE2 1 ATOM 2297 C CZ . PHE A 1 292 ? 28.145 37.091 14.592 1.00 48.90 ? 333 PHE A CZ 1 ATOM 2298 N N . THR A 1 293 ? 33.434 39.960 10.762 1.00 58.57 ? 334 THR A N 1 ATOM 2299 C CA . THR A 1 293 ? 34.535 40.135 9.772 1.00 62.12 ? 334 THR A CA 1 ATOM 2300 C C . THR A 1 293 ? 34.347 39.334 8.479 1.00 64.30 ? 334 THR A C 1 ATOM 2301 O O . THR A 1 293 ? 33.638 38.318 8.451 1.00 64.02 ? 334 THR A O 1 ATOM 2302 C CB . THR A 1 293 ? 35.915 39.708 10.330 1.00 63.02 ? 334 THR A CB 1 ATOM 2303 O OG1 . THR A 1 293 ? 35.841 38.355 10.811 1.00 63.58 ? 334 THR A OG1 1 ATOM 2304 C CG2 . THR A 1 293 ? 36.380 40.638 11.440 1.00 61.52 ? 334 THR A CG2 1 ATOM 2305 N N . GLY A 1 294 ? 35.053 39.779 7.432 1.00 67.12 ? 335 GLY A N 1 ATOM 2306 C CA . GLY A 1 294 ? 35.013 39.207 6.087 1.00 69.77 ? 335 GLY A CA 1 ATOM 2307 C C . GLY A 1 294 ? 34.404 37.839 5.819 1.00 70.73 ? 335 GLY A C 1 ATOM 2308 O O . GLY A 1 294 ? 33.359 37.749 5.169 1.00 71.64 ? 335 GLY A O 1 ATOM 2309 N N . ASN A 1 295 ? 35.053 36.774 6.294 1.00 70.68 ? 336 ASN A N 1 ATOM 2310 C CA . ASN A 1 295 ? 34.613 35.401 5.998 1.00 71.44 ? 336 ASN A CA 1 ATOM 2311 C C . ASN A 1 295 ? 33.260 35.001 6.576 1.00 69.64 ? 336 ASN A C 1 ATOM 2312 O O . ASN A 1 295 ? 32.618 34.074 6.074 1.00 70.05 ? 336 ASN A O 1 ATOM 2313 C CB . ASN A 1 295 ? 35.682 34.378 6.413 1.00 72.47 ? 336 ASN A CB 1 ATOM 2314 C CG . ASN A 1 295 ? 36.943 34.494 5.585 1.00 75.72 ? 336 ASN A CG 1 ATOM 2315 O OD1 . ASN A 1 295 ? 37.044 33.938 4.486 1.00 79.85 ? 336 ASN A OD1 1 ATOM 2316 N ND2 . ASN A 1 295 ? 37.920 35.217 6.110 1.00 77.87 ? 336 ASN A ND2 1 ATOM 2317 N N . PHE A 1 296 ? 32.837 35.712 7.621 1.00 67.61 ? 337 PHE A N 1 ATOM 2318 C CA . PHE A 1 296 ? 31.591 35.418 8.316 1.00 65.77 ? 337 PHE A CA 1 ATOM 2319 C C . PHE A 1 296 ? 30.562 36.526 8.124 1.00 64.90 ? 337 PHE A C 1 ATOM 2320 O O . PHE A 1 296 ? 29.557 36.566 8.837 1.00 63.52 ? 337 PHE A O 1 ATOM 2321 C CB . PHE A 1 296 ? 31.860 35.225 9.808 1.00 64.06 ? 337 PHE A CB 1 ATOM 2322 C CG . PHE A 1 296 ? 32.925 34.225 10.103 1.00 65.26 ? 337 PHE A CG 1 ATOM 2323 C CD1 . PHE A 1 296 ? 34.173 34.641 10.565 1.00 65.68 ? 337 PHE A CD1 1 ATOM 2324 C CD2 . PHE A 1 296 ? 32.696 32.860 9.888 1.00 66.42 ? 337 PHE A CD2 1 ATOM 2325 C CE1 . PHE A 1 296 ? 35.170 33.718 10.838 1.00 66.24 ? 337 PHE A CE1 1 ATOM 2326 C CE2 . PHE A 1 296 ? 33.694 31.923 10.145 1.00 67.22 ? 337 PHE A CE2 1 ATOM 2327 C CZ . PHE A 1 296 ? 34.932 32.354 10.624 1.00 67.45 ? 337 PHE A CZ 1 ATOM 2328 N N . SER A 1 297 ? 30.798 37.414 7.156 1.00 65.58 ? 338 SER A N 1 ATOM 2329 C CA . SER A 1 297 ? 29.992 38.631 7.048 1.00 65.02 ? 338 SER A CA 1 ATOM 2330 C C . SER A 1 297 ? 28.554 38.350 6.618 1.00 64.10 ? 338 SER A C 1 ATOM 2331 O O . SER A 1 297 ? 27.679 39.208 6.790 1.00 63.98 ? 338 SER A O 1 ATOM 2332 C CB . SER A 1 297 ? 30.646 39.668 6.138 1.00 66.06 ? 338 SER A CB 1 ATOM 2333 O OG . SER A 1 297 ? 30.621 39.215 4.803 1.00 69.59 ? 338 SER A OG 1 ATOM 2334 N N . THR A 1 298 ? 28.311 37.140 6.119 1.00 63.38 ? 339 THR A N 1 ATOM 2335 C CA . THR A 1 298 ? 26.971 36.719 5.691 1.00 63.16 ? 339 THR A CA 1 ATOM 2336 C C . THR A 1 298 ? 26.160 36.032 6.794 1.00 61.39 ? 339 THR A C 1 ATOM 2337 O O . THR A 1 298 ? 24.951 35.803 6.648 1.00 61.83 ? 339 THR A O 1 ATOM 2338 C CB . THR A 1 298 ? 27.025 35.808 4.446 1.00 65.04 ? 339 THR A CB 1 ATOM 2339 O OG1 . THR A 1 298 ? 27.661 34.562 4.780 1.00 65.49 ? 339 THR A OG1 1 ATOM 2340 C CG2 . THR A 1 298 ? 27.795 36.497 3.321 1.00 67.00 ? 339 THR A CG2 1 ATOM 2341 N N . GLN A 1 299 ? 26.822 35.704 7.896 1.00 59.17 ? 340 GLN A N 1 ATOM 2342 C CA . GLN A 1 299 ? 26.127 35.132 9.039 1.00 56.49 ? 340 GLN A CA 1 ATOM 2343 C C . GLN A 1 299 ? 25.473 36.275 9.792 1.00 54.61 ? 340 GLN A C 1 ATOM 2344 O O . GLN A 1 299 ? 25.942 37.420 9.721 1.00 52.44 ? 340 GLN A O 1 ATOM 2345 C CB . GLN A 1 299 ? 27.087 34.333 9.927 1.00 55.38 ? 340 GLN A CB 1 ATOM 2346 C CG . GLN A 1 299 ? 27.784 33.170 9.170 1.00 59.33 ? 340 GLN A CG 1 ATOM 2347 C CD . GLN A 1 299 ? 28.844 32.439 9.991 1.00 58.65 ? 340 GLN A CD 1 ATOM 2348 O OE1 . GLN A 1 299 ? 29.235 32.875 11.071 1.00 58.64 ? 340 GLN A OE1 1 ATOM 2349 N NE2 . GLN A 1 299 ? 29.316 31.319 9.462 1.00 59.25 ? 340 GLN A NE2 1 ATOM 2350 N N . LYS A 1 300 ? 24.369 35.951 10.473 1.00 53.62 ? 341 LYS A N 1 ATOM 2351 C CA . LYS A 1 300 ? 23.626 36.890 11.295 1.00 51.92 ? 341 LYS A CA 1 ATOM 2352 C C . LYS A 1 300 ? 23.379 36.293 12.686 1.00 50.00 ? 341 LYS A C 1 ATOM 2353 O O . LYS A 1 300 ? 23.650 35.114 12.943 1.00 49.12 ? 341 LYS A O 1 ATOM 2354 C CB . LYS A 1 300 ? 22.254 37.230 10.676 1.00 52.74 ? 341 LYS A CB 1 ATOM 2355 C CG . LYS A 1 300 ? 22.250 37.663 9.233 1.00 56.54 ? 341 LYS A CG 1 ATOM 2356 C CD . LYS A 1 300 ? 22.468 39.149 9.066 1.00 59.79 ? 341 LYS A CD 1 ATOM 2357 C CE . LYS A 1 300 ? 23.124 39.405 7.692 1.00 66.89 ? 341 LYS A CE 1 ATOM 2358 N NZ . LYS A 1 300 ? 22.519 40.605 7.047 1.00 69.87 ? 341 LYS A NZ 1 ATOM 2359 N N . VAL A 1 301 ? 22.824 37.121 13.567 1.00 47.90 ? 342 VAL A N 1 ATOM 2360 C CA . VAL A 1 301 ? 22.443 36.667 14.897 1.00 45.77 ? 342 VAL A CA 1 ATOM 2361 C C . VAL A 1 301 ? 20.924 36.683 14.972 1.00 45.42 ? 342 VAL A C 1 ATOM 2362 O O . VAL A 1 301 ? 20.285 37.600 14.458 1.00 44.96 ? 342 VAL A O 1 ATOM 2363 C CB . VAL A 1 301 ? 23.093 37.530 15.991 1.00 45.83 ? 342 VAL A CB 1 ATOM 2364 C CG1 . VAL A 1 301 ? 22.523 37.201 17.336 1.00 42.11 ? 342 VAL A CG1 1 ATOM 2365 C CG2 . VAL A 1 301 ? 24.595 37.251 15.990 1.00 46.15 ? 342 VAL A CG2 1 ATOM 2366 N N . LYS A 1 302 ? 20.356 35.632 15.551 1.00 44.90 ? 343 LYS A N 1 ATOM 2367 C CA . LYS A 1 302 ? 18.915 35.514 15.652 1.00 44.35 ? 343 LYS A CA 1 ATOM 2368 C C . LYS A 1 302 ? 18.502 35.213 17.091 1.00 42.76 ? 343 LYS A C 1 ATOM 2369 O O . LYS A 1 302 ? 18.957 34.234 17.701 1.00 42.54 ? 343 LYS A O 1 ATOM 2370 C CB . LYS A 1 302 ? 18.376 34.423 14.721 1.00 45.45 ? 343 LYS A CB 1 ATOM 2371 C CG . LYS A 1 302 ? 16.846 34.328 14.702 1.00 46.12 ? 343 LYS A CG 1 ATOM 2372 C CD . LYS A 1 302 ? 16.416 33.221 13.764 1.00 49.79 ? 343 LYS A CD 1 ATOM 2373 C CE . LYS A 1 302 ? 14.907 33.182 13.585 1.00 51.68 ? 343 LYS A CE 1 ATOM 2374 N NZ . LYS A 1 302 ? 14.610 32.303 12.415 1.00 58.52 ? 343 LYS A NZ 1 ATOM 2375 N N . MET A 1 303 ? 17.616 36.042 17.607 1.00 41.53 ? 344 MET A N 1 ATOM 2376 C CA . MET A 1 303 ? 17.089 35.848 18.963 1.00 39.81 ? 344 MET A CA 1 ATOM 2377 C C . MET A 1 303 ? 15.791 35.040 18.836 1.00 40.60 ? 344 MET A C 1 ATOM 2378 O O . MET A 1 303 ? 15.135 35.077 17.778 1.00 41.07 ? 344 MET A O 1 ATOM 2379 C CB . MET A 1 303 ? 16.849 37.196 19.663 1.00 38.98 ? 344 MET A CB 1 ATOM 2380 C CG . MET A 1 303 ? 18.071 38.078 19.735 1.00 37.82 ? 344 MET A CG 1 ATOM 2381 S SD . MET A 1 303 ? 17.717 39.632 20.621 1.00 40.86 ? 344 MET A SD 1 ATOM 2382 C CE . MET A 1 303 ? 17.488 38.999 22.299 1.00 36.48 ? 344 MET A CE 1 ATOM 2383 N N . HIS A 1 304 ? 15.448 34.275 19.869 1.00 38.85 ? 345 HIS A N 1 ATOM 2384 C CA . HIS A 1 304 ? 14.192 33.536 19.899 1.00 39.02 ? 345 HIS A CA 1 ATOM 2385 C C . HIS A 1 304 ? 13.618 33.726 21.305 1.00 37.68 ? 345 HIS A C 1 ATOM 2386 O O . HIS A 1 304 ? 14.026 33.023 22.232 1.00 37.11 ? 345 HIS A O 1 ATOM 2387 C CB . HIS A 1 304 ? 14.409 32.048 19.716 1.00 39.48 ? 345 HIS A CB 1 ATOM 2388 C CG . HIS A 1 304 ? 15.190 31.674 18.487 1.00 43.16 ? 345 HIS A CG 1 ATOM 2389 N ND1 . HIS A 1 304 ? 16.568 31.691 18.456 1.00 45.85 ? 345 HIS A ND1 1 ATOM 2390 C CD2 . HIS A 1 304 ? 14.793 31.229 17.270 1.00 46.98 ? 345 HIS A CD2 1 ATOM 2391 C CE1 . HIS A 1 304 ? 16.992 31.295 17.268 1.00 46.58 ? 345 HIS A CE1 1 ATOM 2392 N NE2 . HIS A 1 304 ? 15.934 31.012 16.526 1.00 50.37 ? 345 HIS A NE2 1 ATOM 2393 N N . ILE A 1 305 ? 12.679 34.649 21.457 1.00 37.07 ? 346 ILE A N 1 ATOM 2394 C CA . ILE A 1 305 ? 12.150 34.991 22.788 1.00 35.96 ? 346 ILE A CA 1 ATOM 2395 C C . ILE A 1 305 ? 10.652 34.703 22.805 1.00 36.68 ? 346 ILE A C 1 ATOM 2396 O O . ILE A 1 305 ? 9.902 35.224 21.965 1.00 37.31 ? 346 ILE A O 1 ATOM 2397 C CB . ILE A 1 305 ? 12.442 36.468 23.183 1.00 36.33 ? 346 ILE A CB 1 ATOM 2398 C CG1 . ILE A 1 305 ? 13.945 36.809 23.056 1.00 36.12 ? 346 ILE A CG1 1 ATOM 2399 C CG2 . ILE A 1 305 ? 11.929 36.757 24.614 1.00 33.25 ? 346 ILE A CG2 1 ATOM 2400 C CD1 . ILE A 1 305 ? 14.903 35.862 23.834 1.00 38.97 ? 346 ILE A CD1 1 ATOM 2401 N N . HIS A 1 306 ? 10.227 33.859 23.748 1.00 36.42 ? 347 HIS A N 1 ATOM 2402 C CA . HIS A 1 306 ? 8.823 33.426 23.846 1.00 37.47 ? 347 HIS A CA 1 ATOM 2403 C C . HIS A 1 306 ? 8.175 33.567 25.228 1.00 35.47 ? 347 HIS A C 1 ATOM 2404 O O . HIS A 1 306 ? 7.107 32.952 25.503 1.00 34.22 ? 347 HIS A O 1 ATOM 2405 C CB . HIS A 1 306 ? 8.723 31.987 23.387 1.00 38.25 ? 347 HIS A CB 1 ATOM 2406 C CG . HIS A 1 306 ? 9.361 31.771 22.050 1.00 42.40 ? 347 HIS A CG 1 ATOM 2407 N ND1 . HIS A 1 306 ? 10.556 31.104 21.897 1.00 46.76 ? 347 HIS A ND1 1 ATOM 2408 C CD2 . HIS A 1 306 ? 9.021 32.231 20.820 1.00 45.96 ? 347 HIS A CD2 1 ATOM 2409 C CE1 . HIS A 1 306 ? 10.898 31.107 20.618 1.00 47.11 ? 347 HIS A CE1 1 ATOM 2410 N NE2 . HIS A 1 306 ? 9.987 31.788 19.944 1.00 50.88 ? 347 HIS A NE2 1 ATOM 2411 N N . SER A 1 307 ? 8.814 34.370 26.080 1.00 33.65 ? 348 SER A N 1 ATOM 2412 C CA . SER A 1 307 ? 8.292 34.665 27.416 1.00 31.32 ? 348 SER A CA 1 ATOM 2413 C C . SER A 1 307 ? 6.918 35.307 27.317 1.00 32.74 ? 348 SER A C 1 ATOM 2414 O O . SER A 1 307 ? 6.625 35.980 26.317 1.00 32.67 ? 348 SER A O 1 ATOM 2415 C CB . SER A 1 307 ? 9.244 35.638 28.136 1.00 29.65 ? 348 SER A CB 1 ATOM 2416 O OG . SER A 1 307 ? 10.507 35.003 28.235 1.00 32.18 ? 348 SER A OG 1 ATOM 2417 N N . THR A 1 308 ? 6.099 35.137 28.368 1.00 31.92 ? 349 THR A N 1 ATOM 2418 C CA . THR A 1 308 ? 4.746 35.733 28.389 1.00 33.18 ? 349 THR A CA 1 ATOM 2419 C C . THR A 1 308 ? 4.545 36.524 29.669 1.00 32.19 ? 349 THR A C 1 ATOM 2420 O O . THR A 1 308 ? 5.046 36.137 30.714 1.00 31.57 ? 349 THR A O 1 ATOM 2421 C CB . THR A 1 308 ? 3.661 34.664 28.311 1.00 34.74 ? 349 THR A CB 1 ATOM 2422 O OG1 . THR A 1 308 ? 3.775 33.789 29.439 1.00 39.85 ? 349 THR A OG1 1 ATOM 2423 C CG2 . THR A 1 308 ? 3.874 33.813 27.060 1.00 35.61 ? 349 THR A CG2 1 ATOM 2424 N N . ASN A 1 309 ? 3.837 37.634 29.541 1.00 31.04 ? 350 ASN A N 1 ATOM 2425 C CA . ASN A 1 309 ? 3.472 38.465 30.676 1.00 30.94 ? 350 ASN A CA 1 ATOM 2426 C C . ASN A 1 309 ? 2.119 37.962 31.155 1.00 32.17 ? 350 ASN A C 1 ATOM 2427 O O . ASN A 1 309 ? 1.234 37.709 30.346 1.00 33.69 ? 350 ASN A O 1 ATOM 2428 C CB . ASN A 1 309 ? 3.325 39.905 30.222 1.00 30.87 ? 350 ASN A CB 1 ATOM 2429 C CG . ASN A 1 309 ? 4.630 40.510 29.766 1.00 34.04 ? 350 ASN A CG 1 ATOM 2430 O OD1 . ASN A 1 309 ? 5.702 40.122 30.203 1.00 35.73 ? 350 ASN A OD1 1 ATOM 2431 N ND2 . ASN A 1 309 ? 4.537 41.439 28.831 1.00 38.62 ? 350 ASN A ND2 1 ATOM 2432 N N . GLU A 1 310 ? 1.944 37.789 32.455 1.00 30.79 ? 351 GLU A N 1 ATOM 2433 C CA . GLU A 1 310 ? 0.646 37.351 32.981 1.00 32.01 ? 351 GLU A CA 1 ATOM 2434 C C . GLU A 1 310 ? 0.361 37.894 34.355 1.00 29.63 ? 351 GLU A C 1 ATOM 2435 O O . GLU A 1 310 ? 1.262 37.989 35.207 1.00 27.85 ? 351 GLU A O 1 ATOM 2436 C CB . GLU A 1 310 ? 0.529 35.866 33.098 1.00 34.97 ? 351 GLU A CB 1 ATOM 2437 C CG . GLU A 1 310 ? 1.625 35.199 33.762 1.00 40.57 ? 351 GLU A CG 1 ATOM 2438 C CD . GLU A 1 310 ? 1.825 33.852 33.083 1.00 53.50 ? 351 GLU A CD 1 ATOM 2439 O OE1 . GLU A 1 310 ? 1.740 32.791 33.761 1.00 54.83 ? 351 GLU A OE1 1 ATOM 2440 O OE2 . GLU A 1 310 ? 2.010 33.876 31.837 1.00 60.83 ? 351 GLU A OE2 1 ATOM 2441 N N . VAL A 1 311 ? -0.910 38.207 34.553 1.00 29.43 ? 352 VAL A N 1 ATOM 2442 C CA . VAL A 1 311 ? -1.347 38.797 35.817 1.00 28.17 ? 352 VAL A CA 1 ATOM 2443 C C . VAL A 1 311 ? -1.373 37.640 36.830 1.00 27.84 ? 352 VAL A C 1 ATOM 2444 O O . VAL A 1 311 ? -1.991 36.590 36.591 1.00 27.66 ? 352 VAL A O 1 ATOM 2445 C CB . VAL A 1 311 ? -2.745 39.429 35.671 1.00 28.90 ? 352 VAL A CB 1 ATOM 2446 C CG1 . VAL A 1 311 ? -3.228 39.933 37.029 1.00 29.49 ? 352 VAL A CG1 1 ATOM 2447 C CG2 . VAL A 1 311 ? -2.665 40.611 34.699 1.00 30.81 ? 352 VAL A CG2 1 ATOM 2448 N N . THR A 1 312 ? -0.696 37.839 37.950 1.00 25.49 ? 353 THR A N 1 ATOM 2449 C CA . THR A 1 312 ? -0.403 36.748 38.876 1.00 25.81 ? 353 THR A CA 1 ATOM 2450 C C . THR A 1 312 ? -0.521 37.287 40.315 1.00 25.37 ? 353 THR A C 1 ATOM 2451 O O . THR A 1 312 ? -0.138 38.445 40.571 1.00 23.52 ? 353 THR A O 1 ATOM 2452 C CB . THR A 1 312 ? 1.021 36.256 38.650 1.00 26.66 ? 353 THR A CB 1 ATOM 2453 O OG1 . THR A 1 312 ? 1.178 35.894 37.248 1.00 29.73 ? 353 THR A OG1 1 ATOM 2454 C CG2 . THR A 1 312 ? 1.311 35.013 39.515 1.00 27.15 ? 353 THR A CG2 1 ATOM 2455 N N . ARG A 1 313 ? -0.986 36.446 41.243 1.00 23.82 ? 354 ARG A N 1 ATOM 2456 C CA . ARG A 1 313 ? -1.159 36.939 42.638 1.00 24.52 ? 354 ARG A CA 1 ATOM 2457 C C . ARG A 1 313 ? 0.187 36.914 43.394 1.00 23.83 ? 354 ARG A C 1 ATOM 2458 O O . ARG A 1 313 ? 0.985 35.947 43.258 1.00 25.09 ? 354 ARG A O 1 ATOM 2459 C CB . ARG A 1 313 ? -2.204 36.075 43.390 1.00 26.09 ? 354 ARG A CB 1 ATOM 2460 C CG . ARG A 1 313 ? -2.512 36.582 44.820 1.00 26.93 ? 354 ARG A CG 1 ATOM 2461 C CD . ARG A 1 313 ? -3.898 36.059 45.251 1.00 29.93 ? 354 ARG A CD 1 ATOM 2462 N NE . ARG A 1 313 ? -4.910 36.868 44.535 1.00 29.65 ? 354 ARG A NE 1 ATOM 2463 C CZ . ARG A 1 313 ? -6.215 36.794 44.726 1.00 34.69 ? 354 ARG A CZ 1 ATOM 2464 N NH1 . ARG A 1 313 ? -6.711 35.928 45.614 1.00 33.91 ? 354 ARG A NH1 1 ATOM 2465 N NH2 . ARG A 1 313 ? -7.021 37.614 44.031 1.00 33.84 ? 354 ARG A NH2 1 ATOM 2466 N N . ILE A 1 314 ? 0.412 37.958 44.190 1.00 22.99 ? 355 ILE A N 1 ATOM 2467 C CA . ILE A 1 314 ? 1.624 38.055 44.999 1.00 22.91 ? 355 ILE A CA 1 ATOM 2468 C C . ILE A 1 314 ? 1.168 38.314 46.437 1.00 23.67 ? 355 ILE A C 1 ATOM 2469 O O . ILE A 1 314 ? 0.040 38.794 46.621 1.00 23.54 ? 355 ILE A O 1 ATOM 2470 C CB . ILE A 1 314 ? 2.542 39.198 44.464 1.00 20.97 ? 355 ILE A CB 1 ATOM 2471 C CG1 . ILE A 1 314 ? 1.824 40.559 44.474 1.00 20.61 ? 355 ILE A CG1 1 ATOM 2472 C CG2 . ILE A 1 314 ? 3.067 38.783 43.034 1.00 20.81 ? 355 ILE A CG2 1 ATOM 2473 C CD1 . ILE A 1 314 ? 2.832 41.764 44.294 1.00 20.35 ? 355 ILE A CD1 1 ATOM 2474 N N . TYR A 1 315 ? 2.040 38.085 47.420 1.00 23.63 ? 356 TYR A N 1 ATOM 2475 C CA . TYR A 1 315 ? 1.600 38.173 48.817 1.00 24.20 ? 356 TYR A CA 1 ATOM 2476 C C . TYR A 1 315 ? 2.687 38.865 49.625 1.00 23.69 ? 356 TYR A C 1 ATOM 2477 O O . TYR A 1 315 ? 3.797 38.327 49.756 1.00 24.29 ? 356 TYR A O 1 ATOM 2478 C CB . TYR A 1 315 ? 1.481 36.743 49.398 1.00 24.50 ? 356 TYR A CB 1 ATOM 2479 C CG . TYR A 1 315 ? 0.440 35.892 48.706 1.00 24.84 ? 356 TYR A CG 1 ATOM 2480 C CD1 . TYR A 1 315 ? -0.876 35.887 49.151 1.00 26.61 ? 356 TYR A CD1 1 ATOM 2481 C CD2 . TYR A 1 315 ? 0.782 35.106 47.592 1.00 28.16 ? 356 TYR A CD2 1 ATOM 2482 C CE1 . TYR A 1 315 ? -1.865 35.091 48.516 1.00 27.29 ? 356 TYR A CE1 1 ATOM 2483 C CE2 . TYR A 1 315 ? -0.181 34.337 46.940 1.00 30.01 ? 356 TYR A CE2 1 ATOM 2484 C CZ . TYR A 1 315 ? -1.497 34.342 47.420 1.00 32.20 ? 356 TYR A CZ 1 ATOM 2485 O OH . TYR A 1 315 ? -2.424 33.603 46.761 1.00 32.70 ? 356 TYR A OH 1 ATOM 2486 N N . ASN A 1 316 ? 2.335 39.965 50.264 1.00 24.22 ? 357 ASN A N 1 ATOM 2487 C CA . ASN A 1 316 ? 3.228 40.562 51.267 1.00 24.06 ? 357 ASN A CA 1 ATOM 2488 C C . ASN A 1 316 ? 2.856 40.068 52.658 1.00 25.22 ? 357 ASN A C 1 ATOM 2489 O O . ASN A 1 316 ? 1.667 39.949 52.967 1.00 27.10 ? 357 ASN A O 1 ATOM 2490 C CB . ASN A 1 316 ? 3.111 42.097 51.294 1.00 23.05 ? 357 ASN A CB 1 ATOM 2491 C CG . ASN A 1 316 ? 3.434 42.744 49.964 1.00 24.63 ? 357 ASN A CG 1 ATOM 2492 O OD1 . ASN A 1 316 ? 4.321 42.320 49.233 1.00 22.71 ? 357 ASN A OD1 1 ATOM 2493 N ND2 . ASN A 1 316 ? 2.722 43.845 49.657 1.00 25.59 ? 357 ASN A ND2 1 ATOM 2494 N N . VAL A 1 317 ? 3.840 39.850 53.538 1.00 24.56 ? 358 VAL A N 1 ATOM 2495 C CA . VAL A 1 317 ? 3.509 39.576 54.943 1.00 23.78 ? 358 VAL A CA 1 ATOM 2496 C C . VAL A 1 317 ? 3.731 40.898 55.699 1.00 24.46 ? 358 VAL A C 1 ATOM 2497 O O . VAL A 1 317 ? 4.812 41.482 55.595 1.00 24.74 ? 358 VAL A O 1 ATOM 2498 C CB . VAL A 1 317 ? 4.385 38.457 55.561 1.00 25.37 ? 358 VAL A CB 1 ATOM 2499 C CG1 . VAL A 1 317 ? 3.815 38.095 56.960 1.00 24.71 ? 358 VAL A CG1 1 ATOM 2500 C CG2 . VAL A 1 317 ? 4.399 37.179 54.693 1.00 24.91 ? 358 VAL A CG2 1 ATOM 2501 N N . ILE A 1 318 ? 2.700 41.352 56.433 1.00 25.72 ? 359 ILE A N 1 ATOM 2502 C CA . ILE A 1 318 ? 2.745 42.614 57.185 1.00 26.33 ? 359 ILE A CA 1 ATOM 2503 C C . ILE A 1 318 ? 2.520 42.296 58.670 1.00 25.14 ? 359 ILE A C 1 ATOM 2504 O O . ILE A 1 318 ? 1.441 41.798 59.041 1.00 27.46 ? 359 ILE A O 1 ATOM 2505 C CB . ILE A 1 318 ? 1.646 43.614 56.698 1.00 25.96 ? 359 ILE A CB 1 ATOM 2506 C CG1 . ILE A 1 318 ? 1.679 43.764 55.155 1.00 26.76 ? 359 ILE A CG1 1 ATOM 2507 C CG2 . ILE A 1 318 ? 1.760 44.956 57.478 1.00 27.17 ? 359 ILE A CG2 1 ATOM 2508 C CD1 . ILE A 1 318 ? 2.992 44.390 54.675 1.00 26.17 ? 359 ILE A CD1 1 ATOM 2509 N N . GLY A 1 319 ? 3.550 42.534 59.485 1.00 25.54 ? 360 GLY A N 1 ATOM 2510 C CA . GLY A 1 319 ? 3.473 42.238 60.939 1.00 26.64 ? 360 GLY A CA 1 ATOM 2511 C C . GLY A 1 319 ? 3.448 43.551 61.700 1.00 26.96 ? 360 GLY A C 1 ATOM 2512 O O . GLY A 1 319 ? 4.093 44.497 61.280 1.00 26.57 ? 360 GLY A O 1 ATOM 2513 N N . THR A 1 320 ? 2.662 43.629 62.773 1.00 27.37 ? 361 THR A N 1 ATOM 2514 C CA . THR A 1 320 ? 2.508 44.873 63.549 1.00 28.86 ? 361 THR A CA 1 ATOM 2515 C C . THR A 1 320 ? 2.913 44.631 64.991 1.00 29.10 ? 361 THR A C 1 ATOM 2516 O O . THR A 1 320 ? 2.448 43.677 65.648 1.00 30.28 ? 361 THR A O 1 ATOM 2517 C CB . THR A 1 320 ? 1.029 45.349 63.536 1.00 30.51 ? 361 THR A CB 1 ATOM 2518 O OG1 . THR A 1 320 ? 0.683 45.592 62.167 1.00 29.18 ? 361 THR A OG1 1 ATOM 2519 C CG2 . THR A 1 320 ? 0.830 46.648 64.313 1.00 32.73 ? 361 THR A CG2 1 ATOM 2520 N N . LEU A 1 321 ? 3.751 45.533 65.501 1.00 28.70 ? 362 LEU A N 1 ATOM 2521 C CA . LEU A 1 321 ? 4.016 45.578 66.947 1.00 28.94 ? 362 LEU A CA 1 ATOM 2522 C C . LEU A 1 321 ? 3.529 46.926 67.430 1.00 28.55 ? 362 LEU A C 1 ATOM 2523 O O . LEU A 1 321 ? 4.193 47.932 67.197 1.00 28.11 ? 362 LEU A O 1 ATOM 2524 C CB . LEU A 1 321 ? 5.523 45.400 67.198 1.00 28.98 ? 362 LEU A CB 1 ATOM 2525 C CG . LEU A 1 321 ? 6.037 45.344 68.637 1.00 34.44 ? 362 LEU A CG 1 ATOM 2526 C CD1 . LEU A 1 321 ? 5.248 44.315 69.406 1.00 36.21 ? 362 LEU A CD1 1 ATOM 2527 C CD2 . LEU A 1 321 ? 7.531 45.004 68.660 1.00 33.50 ? 362 LEU A CD2 1 ATOM 2528 N N . ARG A 1 322 ? 2.370 46.950 68.104 1.00 28.28 ? 363 ARG A N 1 ATOM 2529 C CA . ARG A 1 322 ? 1.711 48.216 68.444 1.00 30.12 ? 363 ARG A CA 1 ATOM 2530 C C . ARG A 1 322 ? 2.509 49.036 69.498 1.00 29.95 ? 363 ARG A C 1 ATOM 2531 O O . ARG A 1 322 ? 3.000 48.496 70.482 1.00 30.58 ? 363 ARG A O 1 ATOM 2532 C CB . ARG A 1 322 ? 0.278 47.929 68.926 1.00 31.90 ? 363 ARG A CB 1 ATOM 2533 C CG . ARG A 1 322 ? -0.486 49.164 69.387 1.00 35.95 ? 363 ARG A CG 1 ATOM 2534 C CD . ARG A 1 322 ? -1.925 48.829 69.761 1.00 47.43 ? 363 ARG A CD 1 ATOM 2535 N NE . ARG A 1 322 ? -2.064 47.421 70.169 1.00 54.57 ? 363 ARG A NE 1 ATOM 2536 C CZ . ARG A 1 322 ? -1.970 46.951 71.413 1.00 58.00 ? 363 ARG A CZ 1 ATOM 2537 N NH1 . ARG A 1 322 ? -1.733 47.761 72.451 1.00 60.22 ? 363 ARG A NH1 1 ATOM 2538 N NH2 . ARG A 1 322 ? -2.116 45.647 71.612 1.00 58.20 ? 363 ARG A NH2 1 ATOM 2539 N N . GLY A 1 323 ? 2.677 50.330 69.219 1.00 28.95 ? 364 GLY A N 1 ATOM 2540 C CA . GLY A 1 323 ? 3.343 51.251 70.098 1.00 30.16 ? 364 GLY A CA 1 ATOM 2541 C C . GLY A 1 323 ? 2.559 51.502 71.399 1.00 31.47 ? 364 GLY A C 1 ATOM 2542 O O . GLY A 1 323 ? 1.325 51.593 71.403 1.00 32.60 ? 364 GLY A O 1 ATOM 2543 N N . ALA A 1 324 ? 3.302 51.611 72.479 1.00 33.18 ? 365 ALA A N 1 ATOM 2544 C CA . ALA A 1 324 ? 2.718 51.904 73.823 1.00 34.25 ? 365 ALA A CA 1 ATOM 2545 C C . ALA A 1 324 ? 2.213 53.320 73.977 1.00 35.35 ? 365 ALA A C 1 ATOM 2546 O O . ALA A 1 324 ? 1.227 53.543 74.705 1.00 36.40 ? 365 ALA A O 1 ATOM 2547 C CB . ALA A 1 324 ? 3.735 51.595 74.911 1.00 35.79 ? 365 ALA A CB 1 ATOM 2548 N N . VAL A 1 325 ? 2.879 54.294 73.342 1.00 33.18 ? 366 VAL A N 1 ATOM 2549 C CA . VAL A 1 325 ? 2.578 55.723 73.592 1.00 33.79 ? 366 VAL A CA 1 ATOM 2550 C C . VAL A 1 325 ? 2.099 56.445 72.326 1.00 32.83 ? 366 VAL A C 1 ATOM 2551 O O . VAL A 1 325 ? 1.141 57.233 72.358 1.00 32.94 ? 366 VAL A O 1 ATOM 2552 C CB . VAL A 1 325 ? 3.814 56.453 74.173 1.00 34.19 ? 366 VAL A CB 1 ATOM 2553 C CG1 . VAL A 1 325 ? 3.521 57.930 74.422 1.00 35.48 ? 366 VAL A CG1 1 ATOM 2554 C CG2 . VAL A 1 325 ? 4.239 55.807 75.451 1.00 37.14 ? 366 VAL A CG2 1 ATOM 2555 N N . GLU A 1 326 ? 2.748 56.149 71.189 1.00 30.98 ? 367 GLU A N 1 ATOM 2556 C CA . GLU A 1 326 ? 2.299 56.701 69.888 1.00 31.03 ? 367 GLU A CA 1 ATOM 2557 C C . GLU A 1 326 ? 2.017 55.593 68.896 1.00 28.96 ? 367 GLU A C 1 ATOM 2558 O O . GLU A 1 326 ? 2.795 55.403 67.965 1.00 27.67 ? 367 GLU A O 1 ATOM 2559 C CB . GLU A 1 326 ? 3.374 57.618 69.310 1.00 31.14 ? 367 GLU A CB 1 ATOM 2560 C CG . GLU A 1 326 ? 3.812 58.746 70.291 1.00 33.90 ? 367 GLU A CG 1 ATOM 2561 C CD . GLU A 1 326 ? 4.667 59.768 69.579 1.00 34.96 ? 367 GLU A CD 1 ATOM 2562 O OE1 . GLU A 1 326 ? 4.110 60.625 68.831 1.00 34.29 ? 367 GLU A OE1 1 ATOM 2563 O OE2 . GLU A 1 326 ? 5.902 59.710 69.764 1.00 38.95 ? 367 GLU A OE2 1 ATOM 2564 N N . PRO A 1 327 ? 0.914 54.855 69.078 1.00 29.69 ? 368 PRO A N 1 ATOM 2565 C CA . PRO A 1 327 ? 0.612 53.755 68.162 1.00 28.36 ? 368 PRO A CA 1 ATOM 2566 C C . PRO A 1 327 ? 0.282 54.235 66.748 1.00 28.18 ? 368 PRO A C 1 ATOM 2567 O O . PRO A 1 327 ? 0.408 53.460 65.810 1.00 27.01 ? 368 PRO A O 1 ATOM 2568 C CB . PRO A 1 327 ? -0.598 53.085 68.806 1.00 29.01 ? 368 PRO A CB 1 ATOM 2569 C CG . PRO A 1 327 ? -1.203 54.135 69.641 1.00 31.87 ? 368 PRO A CG 1 ATOM 2570 C CD . PRO A 1 327 ? -0.083 54.939 70.169 1.00 31.53 ? 368 PRO A CD 1 ATOM 2571 N N . ASP A 1 328 ? -0.064 55.526 66.603 1.00 28.62 ? 369 ASP A N 1 ATOM 2572 C CA . ASP A 1 328 ? -0.323 56.110 65.271 1.00 28.86 ? 369 ASP A CA 1 ATOM 2573 C C . ASP A 1 328 ? 0.937 56.708 64.600 1.00 27.13 ? 369 ASP A C 1 ATOM 2574 O O . ASP A 1 328 ? 0.832 57.539 63.716 1.00 26.29 ? 369 ASP A O 1 ATOM 2575 C CB . ASP A 1 328 ? -1.438 57.178 65.392 1.00 28.93 ? 369 ASP A CB 1 ATOM 2576 C CG . ASP A 1 328 ? -0.947 58.443 66.041 1.00 32.82 ? 369 ASP A CG 1 ATOM 2577 O OD1 . ASP A 1 328 ? 0.068 58.388 66.782 1.00 35.90 ? 369 ASP A OD1 1 ATOM 2578 O OD2 . ASP A 1 328 ? -1.558 59.521 65.779 1.00 35.76 ? 369 ASP A OD2 1 ATOM 2579 N N . ARG A 1 329 ? 2.133 56.236 64.967 1.00 26.73 ? 370 ARG A N 1 ATOM 2580 C CA . ARG A 1 329 ? 3.379 56.629 64.323 1.00 24.37 ? 370 ARG A CA 1 ATOM 2581 C C . ARG A 1 329 ? 4.096 55.337 63.986 1.00 25.61 ? 370 ARG A C 1 ATOM 2582 O O . ARG A 1 329 ? 4.188 54.463 64.849 1.00 25.03 ? 370 ARG A O 1 ATOM 2583 C CB . ARG A 1 329 ? 4.262 57.490 65.280 1.00 25.36 ? 370 ARG A CB 1 ATOM 2584 C CG . ARG A 1 329 ? 3.556 58.865 65.580 1.00 24.04 ? 370 ARG A CG 1 ATOM 2585 C CD . ARG A 1 329 ? 3.857 59.777 64.382 1.00 27.38 ? 370 ARG A CD 1 ATOM 2586 N NE . ARG A 1 329 ? 3.202 61.107 64.390 1.00 25.43 ? 370 ARG A NE 1 ATOM 2587 C CZ . ARG A 1 329 ? 1.981 61.383 63.928 1.00 27.00 ? 370 ARG A CZ 1 ATOM 2588 N NH1 . ARG A 1 329 ? 1.136 60.421 63.510 1.00 25.66 ? 370 ARG A NH1 1 ATOM 2589 N NH2 . ARG A 1 329 ? 1.571 62.665 63.936 1.00 27.55 ? 370 ARG A NH2 1 ATOM 2590 N N . TYR A 1 330 ? 4.512 55.202 62.719 1.00 24.40 ? 371 TYR A N 1 ATOM 2591 C CA . TYR A 1 330 ? 4.957 53.903 62.185 1.00 24.27 ? 371 TYR A CA 1 ATOM 2592 C C . TYR A 1 330 ? 6.387 53.962 61.808 1.00 23.93 ? 371 TYR A C 1 ATOM 2593 O O . TYR A 1 330 ? 6.815 54.801 60.971 1.00 24.87 ? 371 TYR A O 1 ATOM 2594 C CB . TYR A 1 330 ? 4.173 53.508 60.915 1.00 24.10 ? 371 TYR A CB 1 ATOM 2595 C CG . TYR A 1 330 ? 2.679 53.442 61.063 1.00 25.58 ? 371 TYR A CG 1 ATOM 2596 C CD1 . TYR A 1 330 ? 2.068 53.018 62.264 1.00 25.30 ? 371 TYR A CD1 1 ATOM 2597 C CD2 . TYR A 1 330 ? 1.861 53.756 59.977 1.00 24.39 ? 371 TYR A CD2 1 ATOM 2598 C CE1 . TYR A 1 330 ? 0.659 52.966 62.379 1.00 28.45 ? 371 TYR A CE1 1 ATOM 2599 C CE2 . TYR A 1 330 ? 0.492 53.671 60.059 1.00 25.38 ? 371 TYR A CE2 1 ATOM 2600 C CZ . TYR A 1 330 ? -0.113 53.286 61.254 1.00 27.59 ? 371 TYR A CZ 1 ATOM 2601 O OH . TYR A 1 330 ? -1.483 53.214 61.320 1.00 25.43 ? 371 TYR A OH 1 ATOM 2602 N N . VAL A 1 331 ? 7.149 53.023 62.372 1.00 24.22 ? 372 VAL A N 1 ATOM 2603 C CA . VAL A 1 331 ? 8.514 52.787 61.910 1.00 23.94 ? 372 VAL A CA 1 ATOM 2604 C C . VAL A 1 331 ? 8.490 51.453 61.159 1.00 23.84 ? 372 VAL A C 1 ATOM 2605 O O . VAL A 1 331 ? 8.044 50.431 61.697 1.00 24.07 ? 372 VAL A O 1 ATOM 2606 C CB . VAL A 1 331 ? 9.502 52.757 63.098 1.00 25.36 ? 372 VAL A CB 1 ATOM 2607 C CG1 . VAL A 1 331 ? 10.907 52.367 62.595 1.00 27.03 ? 372 VAL A CG1 1 ATOM 2608 C CG2 . VAL A 1 331 ? 9.549 54.153 63.792 1.00 24.96 ? 372 VAL A CG2 1 ATOM 2609 N N . ILE A 1 332 ? 8.991 51.462 59.925 1.00 21.99 ? 373 ILE A N 1 ATOM 2610 C CA . ILE A 1 332 ? 8.800 50.272 59.072 1.00 22.59 ? 373 ILE A CA 1 ATOM 2611 C C . ILE A 1 332 ? 10.153 49.636 58.774 1.00 21.64 ? 373 ILE A C 1 ATOM 2612 O O . ILE A 1 332 ? 11.105 50.305 58.321 1.00 22.46 ? 373 ILE A O 1 ATOM 2613 C CB . ILE A 1 332 ? 8.061 50.640 57.776 1.00 21.48 ? 373 ILE A CB 1 ATOM 2614 C CG1 . ILE A 1 332 ? 6.774 51.426 58.100 1.00 24.52 ? 373 ILE A CG1 1 ATOM 2615 C CG2 . ILE A 1 332 ? 7.859 49.350 56.848 1.00 22.24 ? 373 ILE A CG2 1 ATOM 2616 C CD1 . ILE A 1 332 ? 6.072 51.993 56.856 1.00 28.32 ? 373 ILE A CD1 1 ATOM 2617 N N . LEU A 1 333 ? 10.242 48.336 59.011 1.00 20.55 ? 374 LEU A N 1 ATOM 2618 C CA . LEU A 1 333 ? 11.404 47.548 58.586 1.00 21.21 ? 374 LEU A CA 1 ATOM 2619 C C . LEU A 1 333 ? 10.900 46.615 57.515 1.00 21.66 ? 374 LEU A C 1 ATOM 2620 O O . LEU A 1 333 ? 10.116 45.719 57.803 1.00 23.80 ? 374 LEU A O 1 ATOM 2621 C CB . LEU A 1 333 ? 11.997 46.734 59.742 1.00 22.01 ? 374 LEU A CB 1 ATOM 2622 C CG . LEU A 1 333 ? 13.123 45.735 59.416 1.00 22.88 ? 374 LEU A CG 1 ATOM 2623 C CD1 . LEU A 1 333 ? 14.343 46.529 58.825 1.00 22.58 ? 374 LEU A CD1 1 ATOM 2624 C CD2 . LEU A 1 333 ? 13.620 44.968 60.685 1.00 23.75 ? 374 LEU A CD2 1 ATOM 2625 N N . GLY A 1 334 ? 11.394 46.751 56.286 1.00 22.79 ? 375 GLY A N 1 ATOM 2626 C CA . GLY A 1 334 ? 10.825 45.922 55.212 1.00 22.67 ? 375 GLY A CA 1 ATOM 2627 C C . GLY A 1 334 ? 11.926 45.363 54.304 1.00 25.06 ? 375 GLY A C 1 ATOM 2628 O O . GLY A 1 334 ? 12.914 46.040 54.041 1.00 25.22 ? 375 GLY A O 1 ATOM 2629 N N . GLY A 1 335 ? 11.728 44.162 53.787 1.00 23.96 ? 376 GLY A N 1 ATOM 2630 C CA . GLY A 1 335 ? 12.678 43.688 52.719 1.00 24.25 ? 376 GLY A CA 1 ATOM 2631 C C . GLY A 1 335 ? 11.932 42.600 51.973 1.00 24.14 ? 376 GLY A C 1 ATOM 2632 O O . GLY A 1 335 ? 10.933 42.071 52.478 1.00 24.21 ? 376 GLY A O 1 ATOM 2633 N N . HIS A 1 336 ? 12.431 42.204 50.809 1.00 22.72 ? 377 HIS A N 1 ATOM 2634 C CA . HIS A 1 336 ? 11.647 41.254 50.013 1.00 22.02 ? 377 HIS A CA 1 ATOM 2635 C C . HIS A 1 336 ? 12.054 39.795 50.295 1.00 23.91 ? 377 HIS A C 1 ATOM 2636 O O . HIS A 1 336 ? 13.086 39.526 50.960 1.00 24.14 ? 377 HIS A O 1 ATOM 2637 C CB . HIS A 1 336 ? 11.760 41.632 48.521 1.00 21.97 ? 377 HIS A CB 1 ATOM 2638 C CG . HIS A 1 336 ? 13.081 41.305 47.859 1.00 20.15 ? 377 HIS A CG 1 ATOM 2639 N ND1 . HIS A 1 336 ? 13.213 40.221 47.010 1.00 23.02 ? 377 HIS A ND1 1 ATOM 2640 C CD2 . HIS A 1 336 ? 14.222 42.027 47.710 1.00 20.11 ? 377 HIS A CD2 1 ATOM 2641 C CE1 . HIS A 1 336 ? 14.415 40.223 46.446 1.00 21.71 ? 377 HIS A CE1 1 ATOM 2642 N NE2 . HIS A 1 336 ? 15.064 41.300 46.869 1.00 22.19 ? 377 HIS A NE2 1 ATOM 2643 N N . ARG A 1 337 ? 11.189 38.891 49.853 1.00 22.78 ? 378 ARG A N 1 ATOM 2644 C CA . ARG A 1 337 ? 11.254 37.475 50.142 1.00 23.78 ? 378 ARG A CA 1 ATOM 2645 C C . ARG A 1 337 ? 11.360 36.718 48.830 1.00 24.06 ? 378 ARG A C 1 ATOM 2646 O O . ARG A 1 337 ? 11.858 35.564 48.815 1.00 24.13 ? 378 ARG A O 1 ATOM 2647 C CB . ARG A 1 337 ? 9.914 37.074 50.772 1.00 23.94 ? 378 ARG A CB 1 ATOM 2648 C CG . ARG A 1 337 ? 9.790 35.596 51.136 1.00 25.42 ? 378 ARG A CG 1 ATOM 2649 C CD . ARG A 1 337 ? 8.377 35.272 51.645 1.00 26.01 ? 378 ARG A CD 1 ATOM 2650 N NE . ARG A 1 337 ? 7.335 35.325 50.560 1.00 26.59 ? 378 ARG A NE 1 ATOM 2651 C CZ . ARG A 1 337 ? 6.465 36.327 50.357 1.00 25.81 ? 378 ARG A CZ 1 ATOM 2652 N NH1 . ARG A 1 337 ? 6.398 37.371 51.176 1.00 23.55 ? 378 ARG A NH1 1 ATOM 2653 N NH2 . ARG A 1 337 ? 5.591 36.275 49.339 1.00 24.89 ? 378 ARG A NH2 1 ATOM 2654 N N . ASP A 1 338 ? 10.861 37.315 47.732 1.00 21.79 ? 379 ASP A N 1 ATOM 2655 C CA . ASP A 1 338 ? 10.873 36.573 46.434 1.00 22.57 ? 379 ASP A CA 1 ATOM 2656 C C . ASP A 1 338 ? 12.302 36.586 45.890 1.00 23.53 ? 379 ASP A C 1 ATOM 2657 O O . ASP A 1 338 ? 13.033 37.570 46.079 1.00 23.33 ? 379 ASP A O 1 ATOM 2658 C CB . ASP A 1 338 ? 9.966 37.239 45.416 1.00 21.60 ? 379 ASP A CB 1 ATOM 2659 C CG . ASP A 1 338 ? 10.451 38.646 45.040 1.00 24.35 ? 379 ASP A CG 1 ATOM 2660 O OD1 . ASP A 1 338 ? 10.476 39.528 45.931 1.00 23.44 ? 379 ASP A OD1 1 ATOM 2661 O OD2 . ASP A 1 338 ? 10.674 38.914 43.841 1.00 21.68 ? 379 ASP A OD2 1 ATOM 2662 N N . SER A 1 339 ? 12.719 35.514 45.211 1.00 24.66 ? 380 SER A N 1 ATOM 2663 C CA . SER A 1 339 ? 14.080 35.434 44.694 1.00 24.98 ? 380 SER A CA 1 ATOM 2664 C C . SER A 1 339 ? 14.027 34.930 43.250 1.00 26.32 ? 380 SER A C 1 ATOM 2665 O O . SER A 1 339 ? 13.010 34.348 42.833 1.00 26.34 ? 380 SER A O 1 ATOM 2666 C CB . SER A 1 339 ? 14.901 34.457 45.569 1.00 26.05 ? 380 SER A CB 1 ATOM 2667 O OG . SER A 1 339 ? 14.342 33.146 45.522 1.00 27.43 ? 380 SER A OG 1 ATOM 2668 N N . TRP A 1 340 ? 15.100 35.131 42.486 1.00 26.80 ? 381 TRP A N 1 ATOM 2669 C CA . TRP A 1 340 ? 15.178 34.519 41.163 1.00 27.04 ? 381 TRP A CA 1 ATOM 2670 C C . TRP A 1 340 ? 15.280 33.006 41.226 1.00 28.05 ? 381 TRP A C 1 ATOM 2671 O O . TRP A 1 340 ? 14.491 32.321 40.621 1.00 28.82 ? 381 TRP A O 1 ATOM 2672 C CB . TRP A 1 340 ? 16.311 35.134 40.316 1.00 25.71 ? 381 TRP A CB 1 ATOM 2673 C CG . TRP A 1 340 ? 15.878 36.481 39.803 1.00 24.51 ? 381 TRP A CG 1 ATOM 2674 C CD1 . TRP A 1 340 ? 16.443 37.707 40.089 1.00 24.64 ? 381 TRP A CD1 1 ATOM 2675 C CD2 . TRP A 1 340 ? 14.765 36.742 38.930 1.00 25.58 ? 381 TRP A CD2 1 ATOM 2676 N NE1 . TRP A 1 340 ? 15.740 38.727 39.433 1.00 26.71 ? 381 TRP A NE1 1 ATOM 2677 C CE2 . TRP A 1 340 ? 14.716 38.152 38.708 1.00 25.43 ? 381 TRP A CE2 1 ATOM 2678 C CE3 . TRP A 1 340 ? 13.823 35.910 38.271 1.00 27.11 ? 381 TRP A CE3 1 ATOM 2679 C CZ2 . TRP A 1 340 ? 13.731 38.754 37.884 1.00 24.39 ? 381 TRP A CZ2 1 ATOM 2680 C CZ3 . TRP A 1 340 ? 12.822 36.521 37.473 1.00 24.73 ? 381 TRP A CZ3 1 ATOM 2681 C CH2 . TRP A 1 340 ? 12.785 37.926 37.305 1.00 24.96 ? 381 TRP A CH2 1 ATOM 2682 N N . VAL A 1 341 ? 16.201 32.486 42.021 1.00 28.43 ? 382 VAL A N 1 ATOM 2683 C CA . VAL A 1 341 ? 16.264 31.053 42.301 1.00 28.59 ? 382 VAL A CA 1 ATOM 2684 C C . VAL A 1 341 ? 16.315 30.820 43.828 1.00 29.06 ? 382 VAL A C 1 ATOM 2685 O O . VAL A 1 341 ? 15.305 31.008 44.501 1.00 28.34 ? 382 VAL A O 1 ATOM 2686 C CB . VAL A 1 341 ? 17.416 30.353 41.533 1.00 29.46 ? 382 VAL A CB 1 ATOM 2687 C CG1 . VAL A 1 341 ? 17.173 28.823 41.556 1.00 29.50 ? 382 VAL A CG1 1 ATOM 2688 C CG2 . VAL A 1 341 ? 17.422 30.780 40.051 1.00 27.96 ? 382 VAL A CG2 1 ATOM 2689 N N . PHE A 1 342 ? 17.468 30.405 44.358 1.00 28.22 ? 383 PHE A N 1 ATOM 2690 C CA . PHE A 1 342 ? 17.578 30.128 45.791 1.00 27.96 ? 383 PHE A CA 1 ATOM 2691 C C . PHE A 1 342 ? 17.733 31.361 46.668 1.00 28.12 ? 383 PHE A C 1 ATOM 2692 O O . PHE A 1 342 ? 17.407 31.303 47.859 1.00 28.34 ? 383 PHE A O 1 ATOM 2693 C CB . PHE A 1 342 ? 18.734 29.134 46.050 1.00 26.60 ? 383 PHE A CB 1 ATOM 2694 C CG . PHE A 1 342 ? 18.563 27.872 45.272 1.00 28.29 ? 383 PHE A CG 1 ATOM 2695 C CD1 . PHE A 1 342 ? 17.550 26.974 45.622 1.00 28.06 ? 383 PHE A CD1 1 ATOM 2696 C CD2 . PHE A 1 342 ? 19.374 27.600 44.168 1.00 30.89 ? 383 PHE A CD2 1 ATOM 2697 C CE1 . PHE A 1 342 ? 17.354 25.786 44.878 1.00 28.74 ? 383 PHE A CE1 1 ATOM 2698 C CE2 . PHE A 1 342 ? 19.176 26.403 43.389 1.00 30.67 ? 383 PHE A CE2 1 ATOM 2699 C CZ . PHE A 1 342 ? 18.146 25.529 43.751 1.00 29.96 ? 383 PHE A CZ 1 ATOM 2700 N N . GLY A 1 343 ? 18.203 32.474 46.094 1.00 27.28 ? 384 GLY A N 1 ATOM 2701 C CA . GLY A 1 343 ? 18.215 33.740 46.915 1.00 26.83 ? 384 GLY A CA 1 ATOM 2702 C C . GLY A 1 343 ? 19.194 33.703 48.104 1.00 27.11 ? 384 GLY A C 1 ATOM 2703 O O . GLY A 1 343 ? 18.960 34.385 49.106 1.00 26.51 ? 384 GLY A O 1 ATOM 2704 N N . GLY A 1 344 ? 20.289 32.939 47.969 1.00 27.21 ? 385 GLY A N 1 ATOM 2705 C CA . GLY A 1 344 ? 21.277 32.756 49.069 1.00 26.98 ? 385 GLY A CA 1 ATOM 2706 C C . GLY A 1 344 ? 21.771 34.092 49.623 1.00 27.30 ? 385 GLY A C 1 ATOM 2707 O O . GLY A 1 344 ? 21.871 34.280 50.845 1.00 28.66 ? 385 GLY A O 1 ATOM 2708 N N . ILE A 1 345 ? 22.078 35.043 48.737 1.00 25.75 ? 386 ILE A N 1 ATOM 2709 C CA . ILE A 1 345 ? 22.340 36.389 49.227 1.00 25.74 ? 386 ILE A CA 1 ATOM 2710 C C . ILE A 1 345 ? 21.087 37.233 49.016 1.00 25.43 ? 386 ILE A C 1 ATOM 2711 O O . ILE A 1 345 ? 20.535 37.830 49.971 1.00 24.55 ? 386 ILE A O 1 ATOM 2712 C CB . ILE A 1 345 ? 23.580 37.010 48.530 1.00 25.06 ? 386 ILE A CB 1 ATOM 2713 C CG1 . ILE A 1 345 ? 24.850 36.282 49.030 1.00 29.11 ? 386 ILE A CG1 1 ATOM 2714 C CG2 . ILE A 1 345 ? 23.745 38.515 48.851 1.00 26.36 ? 386 ILE A CG2 1 ATOM 2715 C CD1 . ILE A 1 345 ? 26.126 36.746 48.356 1.00 31.86 ? 386 ILE A CD1 1 ATOM 2716 N N . ASP A 1 346 ? 20.664 37.325 47.771 1.00 25.09 ? 387 ASP A N 1 ATOM 2717 C CA . ASP A 1 346 ? 19.554 38.243 47.436 1.00 24.49 ? 387 ASP A CA 1 ATOM 2718 C C . ASP A 1 346 ? 18.246 37.431 47.289 1.00 24.65 ? 387 ASP A C 1 ATOM 2719 O O . ASP A 1 346 ? 18.069 36.714 46.290 1.00 25.70 ? 387 ASP A O 1 ATOM 2720 C CB . ASP A 1 346 ? 19.925 38.876 46.118 1.00 25.71 ? 387 ASP A CB 1 ATOM 2721 C CG . ASP A 1 346 ? 18.913 39.822 45.613 1.00 26.02 ? 387 ASP A CG 1 ATOM 2722 O OD1 . ASP A 1 346 ? 17.990 40.185 46.360 1.00 23.80 ? 387 ASP A OD1 1 ATOM 2723 O OD2 . ASP A 1 346 ? 19.059 40.171 44.419 1.00 29.09 ? 387 ASP A OD2 1 ATOM 2724 N N . PRO A 1 347 ? 17.294 37.588 48.222 1.00 23.71 ? 388 PRO A N 1 ATOM 2725 C CA . PRO A 1 347 ? 17.275 38.492 49.396 1.00 22.72 ? 388 PRO A CA 1 ATOM 2726 C C . PRO A 1 347 ? 17.428 37.774 50.743 1.00 23.98 ? 388 PRO A C 1 ATOM 2727 O O . PRO A 1 347 ? 17.295 38.435 51.794 1.00 24.27 ? 388 PRO A O 1 ATOM 2728 C CB . PRO A 1 347 ? 15.845 39.046 49.340 1.00 22.45 ? 388 PRO A CB 1 ATOM 2729 C CG . PRO A 1 347 ? 14.987 37.712 48.944 1.00 23.07 ? 388 PRO A CG 1 ATOM 2730 C CD . PRO A 1 347 ? 15.962 36.976 47.980 1.00 23.52 ? 388 PRO A CD 1 ATOM 2731 N N . GLN A 1 348 ? 17.629 36.456 50.753 1.00 23.49 ? 389 GLN A N 1 ATOM 2732 C CA . GLN A 1 348 ? 17.422 35.705 52.021 1.00 25.15 ? 389 GLN A CA 1 ATOM 2733 C C . GLN A 1 348 ? 18.429 36.079 53.096 1.00 25.39 ? 389 GLN A C 1 ATOM 2734 O O . GLN A 1 348 ? 18.124 35.956 54.268 1.00 26.43 ? 389 GLN A O 1 ATOM 2735 C CB . GLN A 1 348 ? 17.342 34.170 51.854 1.00 24.91 ? 389 GLN A CB 1 ATOM 2736 C CG . GLN A 1 348 ? 16.311 33.720 50.798 1.00 26.63 ? 389 GLN A CG 1 ATOM 2737 C CD . GLN A 1 348 ? 14.882 34.299 51.008 1.00 27.75 ? 389 GLN A CD 1 ATOM 2738 O OE1 . GLN A 1 348 ? 14.564 34.843 52.057 1.00 28.27 ? 389 GLN A OE1 1 ATOM 2739 N NE2 . GLN A 1 348 ? 14.007 34.092 50.016 1.00 25.51 ? 389 GLN A NE2 1 ATOM 2740 N N . SER A 1 349 ? 19.614 36.555 52.708 1.00 25.69 ? 390 SER A N 1 ATOM 2741 C CA A SER A 1 349 ? 20.581 37.048 53.707 0.50 25.83 ? 390 SER A CA 1 ATOM 2742 C CA B SER A 1 349 ? 20.592 37.069 53.666 0.50 27.24 ? 390 SER A CA 1 ATOM 2743 C C . SER A 1 349 ? 20.010 38.270 54.442 1.00 26.56 ? 390 SER A C 1 ATOM 2744 O O . SER A 1 349 ? 20.274 38.462 55.654 1.00 27.07 ? 390 SER A O 1 ATOM 2745 C CB A SER A 1 349 ? 21.959 37.342 53.081 0.50 26.00 ? 390 SER A CB 1 ATOM 2746 C CB B SER A 1 349 ? 21.864 37.447 52.902 0.50 27.53 ? 390 SER A CB 1 ATOM 2747 O OG A SER A 1 349 ? 21.946 38.507 52.272 0.50 19.54 ? 390 SER A OG 1 ATOM 2748 O OG B SER A 1 349 ? 22.634 38.369 53.621 0.50 30.24 ? 390 SER A OG 1 ATOM 2749 N N . GLY A 1 350 ? 19.206 39.070 53.747 1.00 25.62 ? 391 GLY A N 1 ATOM 2750 C CA . GLY A 1 350 ? 18.435 40.183 54.366 1.00 24.42 ? 391 GLY A CA 1 ATOM 2751 C C . GLY A 1 350 ? 17.213 39.681 55.142 1.00 25.59 ? 391 GLY A C 1 ATOM 2752 O O . GLY A 1 350 ? 17.003 40.045 56.318 1.00 24.83 ? 391 GLY A O 1 ATOM 2753 N N . ALA A 1 351 ? 16.414 38.808 54.513 1.00 25.00 ? 392 ALA A N 1 ATOM 2754 C CA . ALA A 1 351 ? 15.224 38.267 55.177 1.00 25.42 ? 392 ALA A CA 1 ATOM 2755 C C . ALA A 1 351 ? 15.494 37.488 56.475 1.00 26.04 ? 392 ALA A C 1 ATOM 2756 O O . ALA A 1 351 ? 14.732 37.604 57.433 1.00 24.61 ? 392 ALA A O 1 ATOM 2757 C CB . ALA A 1 351 ? 14.430 37.437 54.225 1.00 24.70 ? 392 ALA A CB 1 ATOM 2758 N N . ALA A 1 352 ? 16.601 36.735 56.510 1.00 25.67 ? 393 ALA A N 1 ATOM 2759 C CA . ALA A 1 352 ? 17.017 36.005 57.707 1.00 26.88 ? 393 ALA A CA 1 ATOM 2760 C C . ALA A 1 352 ? 17.337 36.986 58.842 1.00 28.09 ? 393 ALA A C 1 ATOM 2761 O O . ALA A 1 352 ? 17.031 36.737 60.031 1.00 27.38 ? 393 ALA A O 1 ATOM 2762 C CB . ALA A 1 352 ? 18.264 35.134 57.358 1.00 26.22 ? 393 ALA A CB 1 ATOM 2763 N N . VAL A 1 353 ? 17.930 38.121 58.479 1.00 27.22 ? 394 VAL A N 1 ATOM 2764 C CA . VAL A 1 353 ? 18.234 39.167 59.478 1.00 27.47 ? 394 VAL A CA 1 ATOM 2765 C C . VAL A 1 353 ? 16.924 39.800 60.013 1.00 27.65 ? 394 VAL A C 1 ATOM 2766 O O . VAL A 1 353 ? 16.764 40.059 61.227 1.00 26.17 ? 394 VAL A O 1 ATOM 2767 C CB . VAL A 1 353 ? 19.221 40.210 58.869 1.00 26.95 ? 394 VAL A CB 1 ATOM 2768 C CG1 . VAL A 1 353 ? 19.053 41.603 59.531 1.00 27.15 ? 394 VAL A CG1 1 ATOM 2769 C CG2 . VAL A 1 353 ? 20.699 39.695 58.972 1.00 27.07 ? 394 VAL A CG2 1 ATOM 2770 N N . VAL A 1 354 ? 15.986 40.077 59.092 1.00 25.29 ? 395 VAL A N 1 ATOM 2771 C CA . VAL A 1 354 ? 14.691 40.641 59.482 1.00 26.03 ? 395 VAL A CA 1 ATOM 2772 C C . VAL A 1 354 ? 13.994 39.645 60.458 1.00 26.61 ? 395 VAL A C 1 ATOM 2773 O O . VAL A 1 354 ? 13.461 40.042 61.498 1.00 25.33 ? 395 VAL A O 1 ATOM 2774 C CB . VAL A 1 354 ? 13.781 40.897 58.295 1.00 25.91 ? 395 VAL A CB 1 ATOM 2775 C CG1 . VAL A 1 354 ? 12.352 41.333 58.801 1.00 26.04 ? 395 VAL A CG1 1 ATOM 2776 C CG2 . VAL A 1 354 ? 14.372 42.047 57.390 1.00 26.00 ? 395 VAL A CG2 1 ATOM 2777 N N . HIS A 1 355 ? 14.045 38.355 60.130 1.00 26.98 ? 396 HIS A N 1 ATOM 2778 C CA . HIS A 1 355 ? 13.361 37.327 60.946 1.00 26.65 ? 396 HIS A CA 1 ATOM 2779 C C . HIS A 1 355 ? 13.976 37.339 62.358 1.00 29.05 ? 396 HIS A C 1 ATOM 2780 O O . HIS A 1 355 ? 13.255 37.260 63.372 1.00 29.67 ? 396 HIS A O 1 ATOM 2781 C CB . HIS A 1 355 ? 13.602 35.969 60.277 1.00 27.56 ? 396 HIS A CB 1 ATOM 2782 C CG . HIS A 1 355 ? 12.471 34.998 60.384 1.00 29.31 ? 396 HIS A CG 1 ATOM 2783 N ND1 . HIS A 1 355 ? 11.177 35.307 60.025 1.00 29.05 ? 396 HIS A ND1 1 ATOM 2784 C CD2 . HIS A 1 355 ? 12.459 33.695 60.771 1.00 32.03 ? 396 HIS A CD2 1 ATOM 2785 C CE1 . HIS A 1 355 ? 10.409 34.242 60.195 1.00 30.27 ? 396 HIS A CE1 1 ATOM 2786 N NE2 . HIS A 1 355 ? 11.164 33.250 60.648 1.00 31.23 ? 396 HIS A NE2 1 ATOM 2787 N N . GLU A 1 356 ? 15.295 37.452 62.452 1.00 27.77 ? 397 GLU A N 1 ATOM 2788 C CA . GLU A 1 356 ? 15.926 37.471 63.793 1.00 29.42 ? 397 GLU A CA 1 ATOM 2789 C C . GLU A 1 356 ? 15.629 38.764 64.554 1.00 29.16 ? 397 GLU A C 1 ATOM 2790 O O . GLU A 1 356 ? 15.462 38.753 65.773 1.00 30.66 ? 397 GLU A O 1 ATOM 2791 C CB . GLU A 1 356 ? 17.430 37.178 63.690 1.00 31.31 ? 397 GLU A CB 1 ATOM 2792 C CG . GLU A 1 356 ? 18.224 37.281 65.047 1.00 33.15 ? 397 GLU A CG 1 ATOM 2793 C CD . GLU A 1 356 ? 17.877 36.198 66.042 1.00 38.45 ? 397 GLU A CD 1 ATOM 2794 O OE1 . GLU A 1 356 ? 16.879 35.473 65.805 1.00 38.18 ? 397 GLU A OE1 1 ATOM 2795 O OE2 . GLU A 1 356 ? 18.638 36.034 67.046 1.00 35.75 ? 397 GLU A OE2 1 ATOM 2796 N N . ILE A 1 357 ? 15.526 39.881 63.826 1.00 29.11 ? 398 ILE A N 1 ATOM 2797 C CA . ILE A 1 357 ? 15.091 41.153 64.429 1.00 28.80 ? 398 ILE A CA 1 ATOM 2798 C C . ILE A 1 357 ? 13.675 41.051 65.003 1.00 29.28 ? 398 ILE A C 1 ATOM 2799 O O . ILE A 1 357 ? 13.421 41.443 66.152 1.00 28.67 ? 398 ILE A O 1 ATOM 2800 C CB . ILE A 1 357 ? 15.245 42.337 63.438 1.00 28.10 ? 398 ILE A CB 1 ATOM 2801 C CG1 . ILE A 1 357 ? 16.740 42.641 63.205 1.00 26.96 ? 398 ILE A CG1 1 ATOM 2802 C CG2 . ILE A 1 357 ? 14.462 43.609 63.956 1.00 27.05 ? 398 ILE A CG2 1 ATOM 2803 C CD1 . ILE A 1 357 ? 16.971 43.557 61.988 1.00 25.38 ? 398 ILE A CD1 1 ATOM 2804 N N . VAL A 1 358 ? 12.758 40.495 64.234 1.00 28.11 ? 399 VAL A N 1 ATOM 2805 C CA . VAL A 1 358 ? 11.381 40.279 64.730 1.00 30.02 ? 399 VAL A CA 1 ATOM 2806 C C . VAL A 1 358 ? 11.408 39.396 65.962 1.00 30.84 ? 399 VAL A C 1 ATOM 2807 O O . VAL A 1 358 ? 10.732 39.714 66.961 1.00 31.62 ? 399 VAL A O 1 ATOM 2808 C CB . VAL A 1 358 ? 10.448 39.626 63.669 1.00 29.53 ? 399 VAL A CB 1 ATOM 2809 C CG1 . VAL A 1 358 ? 9.067 39.290 64.297 1.00 31.25 ? 399 VAL A CG1 1 ATOM 2810 C CG2 . VAL A 1 358 ? 10.264 40.611 62.487 1.00 27.67 ? 399 VAL A CG2 1 ATOM 2811 N N . ARG A 1 359 ? 12.186 38.307 65.901 1.00 30.59 ? 400 ARG A N 1 ATOM 2812 C CA . ARG A 1 359 ? 12.309 37.396 67.042 1.00 32.21 ? 400 ARG A CA 1 ATOM 2813 C C . ARG A 1 359 ? 12.783 38.138 68.289 1.00 33.83 ? 400 ARG A C 1 ATOM 2814 O O . ARG A 1 359 ? 12.214 37.929 69.378 1.00 33.95 ? 400 ARG A O 1 ATOM 2815 C CB . ARG A 1 359 ? 13.241 36.195 66.749 1.00 31.58 ? 400 ARG A CB 1 ATOM 2816 C CG . ARG A 1 359 ? 13.046 35.065 67.796 1.00 34.93 ? 400 ARG A CG 1 ATOM 2817 C CD . ARG A 1 359 ? 14.227 34.064 67.771 1.00 34.78 ? 400 ARG A CD 1 ATOM 2818 N NE . ARG A 1 359 ? 15.474 34.759 68.109 1.00 37.77 ? 400 ARG A NE 1 ATOM 2819 C CZ . ARG A 1 359 ? 15.883 35.062 69.346 1.00 39.71 ? 400 ARG A CZ 1 ATOM 2820 N NH1 . ARG A 1 359 ? 17.024 35.724 69.506 1.00 36.98 ? 400 ARG A NH1 1 ATOM 2821 N NH2 . ARG A 1 359 ? 15.156 34.714 70.421 1.00 40.66 ? 400 ARG A NH2 1 ATOM 2822 N N . SER A 1 360 ? 13.807 38.992 68.147 1.00 33.77 ? 401 SER A N 1 ATOM 2823 C CA . SER A 1 360 ? 14.321 39.758 69.305 1.00 35.42 ? 401 SER A CA 1 ATOM 2824 C C . SER A 1 360 ? 13.316 40.765 69.859 1.00 35.62 ? 401 SER A C 1 ATOM 2825 O O . SER A 1 360 ? 13.143 40.844 71.088 1.00 36.70 ? 401 SER A O 1 ATOM 2826 C CB . SER A 1 360 ? 15.635 40.463 68.990 1.00 35.00 ? 401 SER A CB 1 ATOM 2827 O OG A SER A 1 360 ? 16.092 41.192 70.151 0.50 31.51 ? 401 SER A OG 1 ATOM 2828 O OG B SER A 1 360 ? 16.607 39.461 68.716 0.50 37.35 ? 401 SER A OG 1 ATOM 2829 N N . PHE A 1 361 ? 12.657 41.527 68.980 1.00 34.57 ? 402 PHE A N 1 ATOM 2830 C CA . PHE A 1 361 ? 11.624 42.467 69.459 1.00 34.31 ? 402 PHE A CA 1 ATOM 2831 C C . PHE A 1 361 ? 10.507 41.703 70.158 1.00 36.17 ? 402 PHE A C 1 ATOM 2832 O O . PHE A 1 361 ? 10.002 42.193 71.166 1.00 36.27 ? 402 PHE A O 1 ATOM 2833 C CB . PHE A 1 361 ? 11.015 43.310 68.335 1.00 32.41 ? 402 PHE A CB 1 ATOM 2834 C CG . PHE A 1 361 ? 11.807 44.538 67.977 1.00 31.59 ? 402 PHE A CG 1 ATOM 2835 C CD1 . PHE A 1 361 ? 11.971 45.569 68.893 1.00 33.09 ? 402 PHE A CD1 1 ATOM 2836 C CD2 . PHE A 1 361 ? 12.381 44.683 66.704 1.00 30.39 ? 402 PHE A CD2 1 ATOM 2837 C CE1 . PHE A 1 361 ? 12.695 46.739 68.565 1.00 31.08 ? 402 PHE A CE1 1 ATOM 2838 C CE2 . PHE A 1 361 ? 13.089 45.862 66.351 1.00 29.36 ? 402 PHE A CE2 1 ATOM 2839 C CZ . PHE A 1 361 ? 13.267 46.880 67.287 1.00 31.17 ? 402 PHE A CZ 1 ATOM 2840 N N . GLY A 1 362 ? 10.118 40.533 69.628 1.00 35.24 ? 403 GLY A N 1 ATOM 2841 C CA . GLY A 1 362 ? 9.061 39.722 70.218 1.00 37.70 ? 403 GLY A CA 1 ATOM 2842 C C . GLY A 1 362 ? 9.433 39.166 71.587 1.00 40.05 ? 403 GLY A C 1 ATOM 2843 O O . GLY A 1 362 ? 8.572 39.032 72.490 1.00 40.75 ? 403 GLY A O 1 ATOM 2844 N N . THR A 1 363 ? 10.709 38.844 71.770 1.00 40.84 ? 404 THR A N 1 ATOM 2845 C CA . THR A 1 363 ? 11.159 38.386 73.082 1.00 41.38 ? 404 THR A CA 1 ATOM 2846 C C . THR A 1 363 ? 10.943 39.454 74.158 1.00 42.29 ? 404 THR A C 1 ATOM 2847 O O . THR A 1 363 ? 10.479 39.132 75.244 1.00 42.85 ? 404 THR A O 1 ATOM 2848 C CB . THR A 1 363 ? 12.633 37.890 73.111 1.00 41.59 ? 404 THR A CB 1 ATOM 2849 O OG1 A THR A 1 363 ? 12.789 36.834 72.154 0.50 39.89 ? 404 THR A OG1 1 ATOM 2850 O OG1 B THR A 1 363 ? 13.540 39.005 73.055 0.50 41.60 ? 404 THR A OG1 1 ATOM 2851 C CG2 A THR A 1 363 ? 13.007 37.384 74.476 0.50 41.37 ? 404 THR A CG2 1 ATOM 2852 C CG2 B THR A 1 363 ? 12.917 36.893 72.004 0.50 40.38 ? 404 THR A CG2 1 ATOM 2853 N N . LEU A 1 364 ? 11.283 40.699 73.845 1.00 41.24 ? 405 LEU A N 1 ATOM 2854 C CA . LEU A 1 364 ? 11.090 41.813 74.750 1.00 41.46 ? 405 LEU A CA 1 ATOM 2855 C C . LEU A 1 364 ? 9.600 42.051 74.959 1.00 41.81 ? 405 LEU A C 1 ATOM 2856 O O . LEU A 1 364 ? 9.182 42.336 76.074 1.00 41.14 ? 405 LEU A O 1 ATOM 2857 C CB . LEU A 1 364 ? 11.731 43.118 74.208 1.00 41.69 ? 405 LEU A CB 1 ATOM 2858 C CG A LEU A 1 364 ? 13.203 43.105 73.771 0.50 41.88 ? 405 LEU A CG 1 ATOM 2859 C CG B LEU A 1 364 ? 13.212 43.405 74.506 0.50 41.66 ? 405 LEU A CG 1 ATOM 2860 C CD1 A LEU A 1 364 ? 13.567 44.456 73.167 0.50 41.69 ? 405 LEU A CD1 1 ATOM 2861 C CD1 B LEU A 1 364 ? 14.151 42.363 73.879 0.50 39.87 ? 405 LEU A CD1 1 ATOM 2862 C CD2 A LEU A 1 364 ? 14.120 42.760 74.944 0.50 44.98 ? 405 LEU A CD2 1 ATOM 2863 C CD2 B LEU A 1 364 ? 13.575 44.795 74.014 0.50 41.10 ? 405 LEU A CD2 1 ATOM 2864 N N . LYS A 1 365 ? 8.809 41.948 73.884 1.00 40.47 ? 406 LYS A N 1 ATOM 2865 C CA . LYS A 1 365 ? 7.365 42.076 74.001 1.00 41.28 ? 406 LYS A CA 1 ATOM 2866 C C . LYS A 1 365 ? 6.799 41.043 74.985 1.00 42.99 ? 406 LYS A C 1 ATOM 2867 O O . LYS A 1 365 ? 6.015 41.413 75.862 1.00 43.07 ? 406 LYS A O 1 ATOM 2868 C CB . LYS A 1 365 ? 6.621 41.991 72.654 1.00 41.41 ? 406 LYS A CB 1 ATOM 2869 C CG . LYS A 1 365 ? 5.180 42.453 72.828 1.00 45.90 ? 406 LYS A CG 1 ATOM 2870 C CD . LYS A 1 365 ? 4.215 41.871 71.838 1.00 53.19 ? 406 LYS A CD 1 ATOM 2871 C CE . LYS A 1 365 ? 3.079 41.135 72.555 1.00 57.64 ? 406 LYS A CE 1 ATOM 2872 N NZ . LYS A 1 365 ? 2.082 40.732 71.529 1.00 60.14 ? 406 LYS A NZ 1 ATOM 2873 N N . LYS A 1 366 ? 7.204 39.780 74.861 1.00 42.65 ? 407 LYS A N 1 ATOM 2874 C CA . LYS A 1 366 ? 6.729 38.736 75.794 1.00 45.23 ? 407 LYS A CA 1 ATOM 2875 C C . LYS A 1 366 ? 7.069 39.009 77.255 1.00 46.84 ? 407 LYS A C 1 ATOM 2876 O O . LYS A 1 366 ? 6.370 38.520 78.142 1.00 48.66 ? 407 LYS A O 1 ATOM 2877 C CB . LYS A 1 366 ? 7.162 37.340 75.363 1.00 45.48 ? 407 LYS A CB 1 ATOM 2878 C CG . LYS A 1 366 ? 6.442 36.881 74.099 1.00 48.07 ? 407 LYS A CG 1 ATOM 2879 C CD . LYS A 1 366 ? 7.050 35.619 73.518 1.00 50.93 ? 407 LYS A CD 1 ATOM 2880 C CE . LYS A 1 366 ? 6.297 35.239 72.260 1.00 50.65 ? 407 LYS A CE 1 ATOM 2881 N NZ . LYS A 1 366 ? 6.611 33.847 71.915 1.00 52.89 ? 407 LYS A NZ 1 ATOM 2882 N N . GLU A 1 367 ? 8.114 39.799 77.499 1.00 47.25 ? 408 GLU A N 1 ATOM 2883 C CA . GLU A 1 367 ? 8.517 40.231 78.856 1.00 49.79 ? 408 GLU A CA 1 ATOM 2884 C C . GLU A 1 367 ? 7.792 41.508 79.319 1.00 49.41 ? 408 GLU A C 1 ATOM 2885 O O . GLU A 1 367 ? 8.060 42.033 80.403 1.00 50.99 ? 408 GLU A O 1 ATOM 2886 C CB . GLU A 1 367 ? 10.042 40.437 78.918 1.00 50.36 ? 408 GLU A CB 1 ATOM 2887 C CG . GLU A 1 367 ? 10.874 39.141 78.947 1.00 56.79 ? 408 GLU A CG 1 ATOM 2888 C CD . GLU A 1 367 ? 12.326 39.321 78.457 1.00 64.84 ? 408 GLU A CD 1 ATOM 2889 O OE1 . GLU A 1 367 ? 12.976 38.289 78.118 1.00 67.91 ? 408 GLU A OE1 1 ATOM 2890 O OE2 . GLU A 1 367 ? 12.820 40.481 78.388 1.00 68.05 ? 408 GLU A OE2 1 ATOM 2891 N N . GLY A 1 368 ? 6.873 42.012 78.505 1.00 47.12 ? 409 GLY A N 1 ATOM 2892 C CA . GLY A 1 368 ? 6.027 43.142 78.904 1.00 46.62 ? 409 GLY A CA 1 ATOM 2893 C C . GLY A 1 368 ? 6.390 44.461 78.264 1.00 45.18 ? 409 GLY A C 1 ATOM 2894 O O . GLY A 1 368 ? 5.712 45.465 78.481 1.00 45.65 ? 409 GLY A O 1 ATOM 2895 N N . TRP A 1 369 ? 7.433 44.474 77.432 1.00 42.85 ? 410 TRP A N 1 ATOM 2896 C CA . TRP A 1 369 ? 7.882 45.730 76.852 1.00 41.22 ? 410 TRP A CA 1 ATOM 2897 C C . TRP A 1 369 ? 7.094 45.973 75.546 1.00 38.48 ? 410 TRP A C 1 ATOM 2898 O O . TRP A 1 369 ? 6.719 45.027 74.859 1.00 38.69 ? 410 TRP A O 1 ATOM 2899 C CB . TRP A 1 369 ? 9.388 45.663 76.590 1.00 41.37 ? 410 TRP A CB 1 ATOM 2900 C CG . TRP A 1 369 ? 9.998 46.779 75.731 1.00 42.18 ? 410 TRP A CG 1 ATOM 2901 C CD1 . TRP A 1 369 ? 10.558 47.969 76.178 1.00 43.46 ? 410 TRP A CD1 1 ATOM 2902 C CD2 . TRP A 1 369 ? 10.134 46.784 74.305 1.00 41.26 ? 410 TRP A CD2 1 ATOM 2903 N NE1 . TRP A 1 369 ? 11.023 48.698 75.106 1.00 41.96 ? 410 TRP A NE1 1 ATOM 2904 C CE2 . TRP A 1 369 ? 10.779 48.002 73.946 1.00 40.90 ? 410 TRP A CE2 1 ATOM 2905 C CE3 . TRP A 1 369 ? 9.750 45.887 73.281 1.00 40.55 ? 410 TRP A CE3 1 ATOM 2906 C CZ2 . TRP A 1 369 ? 11.068 48.332 72.608 1.00 37.59 ? 410 TRP A CZ2 1 ATOM 2907 C CZ3 . TRP A 1 369 ? 10.043 46.200 71.969 1.00 37.69 ? 410 TRP A CZ3 1 ATOM 2908 C CH2 . TRP A 1 369 ? 10.684 47.444 71.635 1.00 36.96 ? 410 TRP A CH2 1 ATOM 2909 N N . ARG A 1 370 ? 6.858 47.222 75.212 1.00 36.76 ? 411 ARG A N 1 ATOM 2910 C CA . ARG A 1 370 ? 6.426 47.592 73.841 1.00 35.58 ? 411 ARG A CA 1 ATOM 2911 C C . ARG A 1 370 ? 7.232 48.818 73.468 1.00 34.26 ? 411 ARG A C 1 ATOM 2912 O O . ARG A 1 370 ? 7.583 49.600 74.351 1.00 35.14 ? 411 ARG A O 1 ATOM 2913 C CB . ARG A 1 370 ? 4.956 48.021 73.828 1.00 36.34 ? 411 ARG A CB 1 ATOM 2914 C CG . ARG A 1 370 ? 3.942 46.910 73.843 1.00 38.51 ? 411 ARG A CG 1 ATOM 2915 C CD . ARG A 1 370 ? 2.478 47.444 73.735 1.00 38.35 ? 411 ARG A CD 1 ATOM 2916 N NE . ARG A 1 370 ? 1.626 46.253 73.720 1.00 39.00 ? 411 ARG A NE 1 ATOM 2917 C CZ . ARG A 1 370 ? 1.461 45.487 72.631 1.00 41.70 ? 411 ARG A CZ 1 ATOM 2918 N NH1 . ARG A 1 370 ? 2.011 45.866 71.473 1.00 35.52 ? 411 ARG A NH1 1 ATOM 2919 N NH2 . ARG A 1 370 ? 0.740 44.363 72.694 1.00 40.77 ? 411 ARG A NH2 1 ATOM 2920 N N . PRO A 1 371 ? 7.505 49.012 72.159 1.00 33.01 ? 412 PRO A N 1 ATOM 2921 C CA . PRO A 1 371 ? 8.163 50.218 71.703 1.00 31.77 ? 412 PRO A CA 1 ATOM 2922 C C . PRO A 1 371 ? 7.238 51.433 71.910 1.00 31.46 ? 412 PRO A C 1 ATOM 2923 O O . PRO A 1 371 ? 6.030 51.295 72.020 1.00 31.97 ? 412 PRO A O 1 ATOM 2924 C CB . PRO A 1 371 ? 8.371 49.961 70.174 1.00 31.44 ? 412 PRO A CB 1 ATOM 2925 C CG . PRO A 1 371 ? 7.233 49.012 69.771 1.00 30.55 ? 412 PRO A CG 1 ATOM 2926 C CD . PRO A 1 371 ? 7.075 48.126 71.054 1.00 30.91 ? 412 PRO A CD 1 ATOM 2927 N N . ARG A 1 372 ? 7.816 52.621 71.944 1.00 31.44 ? 413 ARG A N 1 ATOM 2928 C CA . ARG A 1 372 ? 7.019 53.852 72.084 1.00 31.58 ? 413 ARG A CA 1 ATOM 2929 C C . ARG A 1 372 ? 6.069 53.987 70.870 1.00 29.15 ? 413 ARG A C 1 ATOM 2930 O O . ARG A 1 372 ? 4.851 54.235 71.029 1.00 29.07 ? 413 ARG A O 1 ATOM 2931 C CB . ARG A 1 372 ? 7.948 55.052 72.157 1.00 30.66 ? 413 ARG A CB 1 ATOM 2932 C CG . ARG A 1 372 ? 7.230 56.399 72.251 1.00 34.60 ? 413 ARG A CG 1 ATOM 2933 C CD . ARG A 1 372 ? 8.187 57.564 72.176 1.00 32.53 ? 413 ARG A CD 1 ATOM 2934 N NE . ARG A 1 372 ? 7.395 58.801 72.146 1.00 36.55 ? 413 ARG A NE 1 ATOM 2935 C CZ . ARG A 1 372 ? 6.945 59.455 73.224 1.00 37.82 ? 413 ARG A CZ 1 ATOM 2936 N NH1 . ARG A 1 372 ? 7.222 59.012 74.429 1.00 34.63 ? 413 ARG A NH1 1 ATOM 2937 N NH2 . ARG A 1 372 ? 6.206 60.549 73.076 1.00 38.70 ? 413 ARG A NH2 1 ATOM 2938 N N . ARG A 1 373 ? 6.615 53.814 69.669 1.00 28.11 ? 414 ARG A N 1 ATOM 2939 C CA . ARG A 1 373 ? 5.841 53.944 68.418 1.00 26.93 ? 414 ARG A CA 1 ATOM 2940 C C . ARG A 1 373 ? 5.605 52.546 67.861 1.00 27.43 ? 414 ARG A C 1 ATOM 2941 O O . ARG A 1 373 ? 6.310 51.589 68.221 1.00 28.14 ? 414 ARG A O 1 ATOM 2942 C CB . ARG A 1 373 ? 6.692 54.697 67.367 1.00 25.04 ? 414 ARG A CB 1 ATOM 2943 C CG . ARG A 1 373 ? 7.093 56.135 67.873 1.00 26.79 ? 414 ARG A CG 1 ATOM 2944 C CD . ARG A 1 373 ? 7.856 57.038 66.830 1.00 27.15 ? 414 ARG A CD 1 ATOM 2945 N NE . ARG A 1 373 ? 8.095 58.310 67.509 1.00 27.10 ? 414 ARG A NE 1 ATOM 2946 C CZ . ARG A 1 373 ? 9.078 58.542 68.385 1.00 26.92 ? 414 ARG A CZ 1 ATOM 2947 N NH1 . ARG A 1 373 ? 10.073 57.668 68.534 1.00 25.28 ? 414 ARG A NH1 1 ATOM 2948 N NH2 . ARG A 1 373 ? 9.139 59.710 69.051 1.00 29.76 ? 414 ARG A NH2 1 ATOM 2949 N N . THR A 1 374 ? 4.648 52.434 66.964 1.00 26.44 ? 415 THR A N 1 ATOM 2950 C CA . THR A 1 374 ? 4.345 51.162 66.300 1.00 25.79 ? 415 THR A CA 1 ATOM 2951 C C . THR A 1 374 ? 5.497 50.827 65.334 1.00 24.65 ? 415 THR A C 1 ATOM 2952 O O . THR A 1 374 ? 6.005 51.708 64.611 1.00 24.38 ? 415 THR A O 1 ATOM 2953 C CB . THR A 1 374 ? 3.025 51.302 65.550 1.00 24.99 ? 415 THR A CB 1 ATOM 2954 O OG1 . THR A 1 374 ? 1.955 51.347 66.493 1.00 27.17 ? 415 THR A OG1 1 ATOM 2955 C CG2 . THR A 1 374 ? 2.772 50.130 64.530 1.00 23.84 ? 415 THR A CG2 1 ATOM 2956 N N . ILE A 1 375 ? 5.880 49.563 65.318 1.00 23.79 ? 416 ILE A N 1 ATOM 2957 C CA . ILE A 1 375 ? 6.814 49.063 64.355 1.00 22.93 ? 416 ILE A CA 1 ATOM 2958 C C . ILE A 1 375 ? 6.046 48.137 63.421 1.00 23.42 ? 416 ILE A C 1 ATOM 2959 O O . ILE A 1 375 ? 5.310 47.257 63.883 1.00 24.78 ? 416 ILE A O 1 ATOM 2960 C CB . ILE A 1 375 ? 8.010 48.256 65.002 1.00 22.86 ? 416 ILE A CB 1 ATOM 2961 C CG1 . ILE A 1 375 ? 8.753 49.149 66.004 1.00 25.16 ? 416 ILE A CG1 1 ATOM 2962 C CG2 . ILE A 1 375 ? 9.021 47.837 63.882 1.00 24.10 ? 416 ILE A CG2 1 ATOM 2963 C CD1 . ILE A 1 375 ? 9.810 48.334 66.853 1.00 24.96 ? 416 ILE A CD1 1 ATOM 2964 N N . LEU A 1 376 ? 6.193 48.367 62.107 1.00 23.29 ? 417 LEU A N 1 ATOM 2965 C CA A LEU A 1 376 ? 5.638 47.469 61.104 0.50 21.78 ? 417 LEU A CA 1 ATOM 2966 C CA B LEU A 1 376 ? 5.634 47.467 61.093 0.50 23.58 ? 417 LEU A CA 1 ATOM 2967 C C . LEU A 1 376 ? 6.790 46.700 60.464 1.00 23.27 ? 417 LEU A C 1 ATOM 2968 O O . LEU A 1 376 ? 7.884 47.292 60.147 1.00 24.68 ? 417 LEU A O 1 ATOM 2969 C CB A LEU A 1 376 ? 4.894 48.266 60.031 0.50 20.46 ? 417 LEU A CB 1 ATOM 2970 C CB B LEU A 1 376 ? 4.896 48.235 59.982 0.50 23.09 ? 417 LEU A CB 1 ATOM 2971 C CG A LEU A 1 376 ? 3.802 49.169 60.617 0.50 17.10 ? 417 LEU A CG 1 ATOM 2972 C CG B LEU A 1 376 ? 3.385 48.537 60.035 0.50 28.55 ? 417 LEU A CG 1 ATOM 2973 C CD1 A LEU A 1 376 ? 3.243 50.033 59.561 0.50 19.59 ? 417 LEU A CD1 1 ATOM 2974 C CD1 B LEU A 1 376 ? 2.844 48.887 61.422 0.50 29.74 ? 417 LEU A CD1 1 ATOM 2975 C CD2 A LEU A 1 376 ? 2.700 48.158 61.204 0.50 17.10 ? 417 LEU A CD2 1 ATOM 2976 C CD2 B LEU A 1 376 ? 2.990 49.614 58.992 0.50 26.96 ? 417 LEU A CD2 1 ATOM 2977 N N . PHE A 1 377 ? 6.573 45.401 60.280 1.00 23.04 ? 418 PHE A N 1 ATOM 2978 C CA . PHE A 1 377 ? 7.588 44.538 59.646 1.00 21.99 ? 418 PHE A CA 1 ATOM 2979 C C . PHE A 1 377 ? 6.983 44.023 58.337 1.00 23.33 ? 418 PHE A C 1 ATOM 2980 O O . PHE A 1 377 ? 5.833 43.564 58.326 1.00 25.31 ? 418 PHE A O 1 ATOM 2981 C CB . PHE A 1 377 ? 7.920 43.340 60.553 1.00 23.51 ? 418 PHE A CB 1 ATOM 2982 C CG . PHE A 1 377 ? 8.497 43.746 61.858 1.00 22.92 ? 418 PHE A CG 1 ATOM 2983 C CD1 . PHE A 1 377 ? 9.845 44.058 61.945 1.00 25.44 ? 418 PHE A CD1 1 ATOM 2984 C CD2 . PHE A 1 377 ? 7.676 43.906 63.010 1.00 27.44 ? 418 PHE A CD2 1 ATOM 2985 C CE1 . PHE A 1 377 ? 10.414 44.443 63.229 1.00 26.16 ? 418 PHE A CE1 1 ATOM 2986 C CE2 . PHE A 1 377 ? 8.214 44.301 64.232 1.00 29.24 ? 418 PHE A CE2 1 ATOM 2987 C CZ . PHE A 1 377 ? 9.602 44.539 64.350 1.00 27.05 ? 418 PHE A CZ 1 ATOM 2988 N N . ALA A 1 378 ? 7.775 44.019 57.266 1.00 22.36 ? 419 ALA A N 1 ATOM 2989 C CA . ALA A 1 378 ? 7.223 43.588 55.986 1.00 22.65 ? 419 ALA A CA 1 ATOM 2990 C C . ALA A 1 378 ? 8.177 42.626 55.280 1.00 23.34 ? 419 ALA A C 1 ATOM 2991 O O . ALA A 1 378 ? 9.409 42.849 55.242 1.00 24.46 ? 419 ALA A O 1 ATOM 2992 C CB . ALA A 1 378 ? 6.993 44.782 55.123 1.00 21.35 ? 419 ALA A CB 1 ATOM 2993 N N . SER A 1 379 ? 7.571 41.566 54.740 1.00 23.01 ? 420 SER A N 1 ATOM 2994 C CA . SER A 1 379 ? 8.220 40.649 53.828 1.00 22.71 ? 420 SER A CA 1 ATOM 2995 C C . SER A 1 379 ? 7.554 40.878 52.447 1.00 22.66 ? 420 SER A C 1 ATOM 2996 O O . SER A 1 379 ? 6.436 40.400 52.214 1.00 22.91 ? 420 SER A O 1 ATOM 2997 C CB . SER A 1 379 ? 7.929 39.237 54.326 1.00 24.05 ? 420 SER A CB 1 ATOM 2998 O OG . SER A 1 379 ? 8.421 38.240 53.427 1.00 23.32 ? 420 SER A OG 1 ATOM 2999 N N . TRP A 1 380 ? 8.214 41.647 51.575 1.00 22.24 ? 421 TRP A N 1 ATOM 3000 C CA . TRP A 1 380 ? 7.608 42.086 50.300 1.00 20.79 ? 421 TRP A CA 1 ATOM 3001 C C . TRP A 1 380 ? 7.739 40.977 49.246 1.00 22.71 ? 421 TRP A C 1 ATOM 3002 O O . TRP A 1 380 ? 8.714 40.184 49.257 1.00 21.63 ? 421 TRP A O 1 ATOM 3003 C CB . TRP A 1 380 ? 8.355 43.294 49.749 1.00 19.90 ? 421 TRP A CB 1 ATOM 3004 C CG . TRP A 1 380 ? 8.411 44.500 50.652 1.00 21.25 ? 421 TRP A CG 1 ATOM 3005 C CD1 . TRP A 1 380 ? 9.553 45.177 51.011 1.00 19.66 ? 421 TRP A CD1 1 ATOM 3006 C CD2 . TRP A 1 380 ? 7.288 45.232 51.225 1.00 19.86 ? 421 TRP A CD2 1 ATOM 3007 N NE1 . TRP A 1 380 ? 9.223 46.280 51.814 1.00 19.81 ? 421 TRP A NE1 1 ATOM 3008 C CE2 . TRP A 1 380 ? 7.842 46.330 51.947 1.00 19.53 ? 421 TRP A CE2 1 ATOM 3009 C CE3 . TRP A 1 380 ? 5.870 45.037 51.230 1.00 21.17 ? 421 TRP A CE3 1 ATOM 3010 C CZ2 . TRP A 1 380 ? 7.054 47.241 52.662 1.00 21.23 ? 421 TRP A CZ2 1 ATOM 3011 C CZ3 . TRP A 1 380 ? 5.056 45.977 51.926 1.00 22.38 ? 421 TRP A CZ3 1 ATOM 3012 C CH2 . TRP A 1 380 ? 5.662 47.055 52.658 1.00 20.86 ? 421 TRP A CH2 1 ATOM 3013 N N . ASP A 1 381 ? 6.735 40.913 48.361 1.00 21.35 ? 422 ASP A N 1 ATOM 3014 C CA . ASP A 1 381 ? 6.806 39.963 47.246 1.00 21.61 ? 422 ASP A CA 1 ATOM 3015 C C . ASP A 1 381 ? 7.119 40.736 45.973 1.00 21.80 ? 422 ASP A C 1 ATOM 3016 O O . ASP A 1 381 ? 6.929 41.967 45.937 1.00 23.74 ? 422 ASP A O 1 ATOM 3017 C CB . ASP A 1 381 ? 5.439 39.282 47.127 1.00 21.93 ? 422 ASP A CB 1 ATOM 3018 C CG . ASP A 1 381 ? 5.507 37.913 46.390 1.00 25.01 ? 422 ASP A CG 1 ATOM 3019 O OD1 . ASP A 1 381 ? 6.565 37.510 45.855 1.00 25.44 ? 422 ASP A OD1 1 ATOM 3020 O OD2 . ASP A 1 381 ? 4.491 37.215 46.414 1.00 23.53 ? 422 ASP A OD2 1 ATOM 3021 N N . ALA A 1 382 ? 7.586 40.011 44.939 1.00 21.58 ? 423 ALA A N 1 ATOM 3022 C CA . ALA A 1 382 ? 7.758 40.534 43.565 1.00 21.83 ? 423 ALA A CA 1 ATOM 3023 C C . ALA A 1 382 ? 8.636 41.757 43.476 1.00 20.45 ? 423 ALA A C 1 ATOM 3024 O O . ALA A 1 382 ? 8.473 42.590 42.586 1.00 20.96 ? 423 ALA A O 1 ATOM 3025 C CB . ALA A 1 382 ? 6.348 40.800 42.878 1.00 21.44 ? 423 ALA A CB 1 ATOM 3026 N N . GLU A 1 383 ? 9.594 41.864 44.383 1.00 20.90 ? 424 GLU A N 1 ATOM 3027 C CA . GLU A 1 383 ? 10.564 42.953 44.298 1.00 20.81 ? 424 GLU A CA 1 ATOM 3028 C C . GLU A 1 383 ? 11.370 42.770 43.019 1.00 20.96 ? 424 GLU A C 1 ATOM 3029 O O . GLU A 1 383 ? 11.701 43.755 42.324 1.00 21.62 ? 424 GLU A O 1 ATOM 3030 C CB . GLU A 1 383 ? 11.456 42.952 45.514 1.00 21.36 ? 424 GLU A CB 1 ATOM 3031 C CG . GLU A 1 383 ? 12.466 44.125 45.513 1.00 21.05 ? 424 GLU A CG 1 ATOM 3032 C CD . GLU A 1 383 ? 13.799 43.879 44.787 1.00 26.15 ? 424 GLU A CD 1 ATOM 3033 O OE1 . GLU A 1 383 ? 14.059 42.752 44.271 1.00 25.95 ? 424 GLU A OE1 1 ATOM 3034 O OE2 . GLU A 1 383 ? 14.575 44.884 44.720 1.00 27.44 ? 424 GLU A OE2 1 ATOM 3035 N N . GLU A 1 384 ? 11.669 41.518 42.687 1.00 21.77 ? 425 GLU A N 1 ATOM 3036 C CA . GLU A 1 384 ? 12.507 41.264 41.472 1.00 23.18 ? 425 GLU A CA 1 ATOM 3037 C C . GLU A 1 384 ? 11.833 41.649 40.168 1.00 23.08 ? 425 GLU A C 1 ATOM 3038 O O . GLU A 1 384 ? 12.514 41.812 39.136 1.00 22.94 ? 425 GLU A O 1 ATOM 3039 C CB . GLU A 1 384 ? 12.949 39.786 41.410 1.00 22.48 ? 425 GLU A CB 1 ATOM 3040 C CG . GLU A 1 384 ? 13.806 39.319 42.592 1.00 23.47 ? 425 GLU A CG 1 ATOM 3041 C CD . GLU A 1 384 ? 15.199 39.999 42.650 1.00 23.90 ? 425 GLU A CD 1 ATOM 3042 O OE1 . GLU A 1 384 ? 15.463 40.980 41.906 1.00 24.11 ? 425 GLU A OE1 1 ATOM 3043 O OE2 . GLU A 1 384 ? 16.033 39.599 43.469 1.00 25.35 ? 425 GLU A OE2 1 ATOM 3044 N N . PHE A 1 385 ? 10.505 41.813 40.180 1.00 22.67 ? 426 PHE A N 1 ATOM 3045 C CA . PHE A 1 385 ? 9.785 42.167 38.972 1.00 21.73 ? 426 PHE A CA 1 ATOM 3046 C C . PHE A 1 385 ? 9.397 43.635 38.943 1.00 23.04 ? 426 PHE A C 1 ATOM 3047 O O . PHE A 1 385 ? 8.518 44.020 38.180 1.00 22.69 ? 426 PHE A O 1 ATOM 3048 C CB . PHE A 1 385 ? 8.516 41.317 38.865 1.00 21.81 ? 426 PHE A CB 1 ATOM 3049 C CG . PHE A 1 385 ? 8.810 39.876 38.561 1.00 23.91 ? 426 PHE A CG 1 ATOM 3050 C CD1 . PHE A 1 385 ? 8.709 39.398 37.247 1.00 24.94 ? 426 PHE A CD1 1 ATOM 3051 C CD2 . PHE A 1 385 ? 9.187 39.000 39.590 1.00 23.30 ? 426 PHE A CD2 1 ATOM 3052 C CE1 . PHE A 1 385 ? 8.957 38.025 36.941 1.00 24.18 ? 426 PHE A CE1 1 ATOM 3053 C CE2 . PHE A 1 385 ? 9.466 37.640 39.331 1.00 22.79 ? 426 PHE A CE2 1 ATOM 3054 C CZ . PHE A 1 385 ? 9.347 37.132 37.979 1.00 24.37 ? 426 PHE A CZ 1 ATOM 3055 N N . GLY A 1 386 ? 10.059 44.442 39.784 1.00 22.06 ? 427 GLY A N 1 ATOM 3056 C CA . GLY A 1 386 ? 9.916 45.905 39.685 1.00 22.88 ? 427 GLY A CA 1 ATOM 3057 C C . GLY A 1 386 ? 9.352 46.552 40.954 1.00 21.82 ? 427 GLY A C 1 ATOM 3058 O O . GLY A 1 386 ? 8.614 47.557 40.877 1.00 22.40 ? 427 GLY A O 1 ATOM 3059 N N . LEU A 1 387 ? 9.735 46.002 42.095 1.00 19.68 ? 428 LEU A N 1 ATOM 3060 C CA . LEU A 1 387 ? 9.346 46.552 43.413 1.00 19.61 ? 428 LEU A CA 1 ATOM 3061 C C . LEU A 1 387 ? 7.798 46.495 43.540 1.00 20.47 ? 428 LEU A C 1 ATOM 3062 O O . LEU A 1 387 ? 7.179 47.384 44.101 1.00 21.08 ? 428 LEU A O 1 ATOM 3063 C CB . LEU A 1 387 ? 9.845 48.035 43.546 1.00 20.93 ? 428 LEU A CB 1 ATOM 3064 C CG . LEU A 1 387 ? 11.250 48.345 43.025 1.00 21.37 ? 428 LEU A CG 1 ATOM 3065 C CD1 . LEU A 1 387 ? 11.646 49.868 43.206 1.00 22.26 ? 428 LEU A CD1 1 ATOM 3066 C CD2 . LEU A 1 387 ? 12.245 47.432 43.705 1.00 22.09 ? 428 LEU A CD2 1 ATOM 3067 N N . LEU A 1 388 ? 7.176 45.440 43.019 1.00 19.81 ? 429 LEU A N 1 ATOM 3068 C CA . LEU A 1 388 ? 5.718 45.489 42.870 1.00 20.02 ? 429 LEU A CA 1 ATOM 3069 C C . LEU A 1 388 ? 4.993 45.368 44.202 1.00 21.05 ? 429 LEU A C 1 ATOM 3070 O O . LEU A 1 388 ? 4.005 46.031 44.419 1.00 21.91 ? 429 LEU A O 1 ATOM 3071 C CB . LEU A 1 388 ? 5.244 44.378 41.901 1.00 20.34 ? 429 LEU A CB 1 ATOM 3072 C CG . LEU A 1 388 ? 5.977 44.414 40.540 1.00 20.82 ? 429 LEU A CG 1 ATOM 3073 C CD1 . LEU A 1 388 ? 5.299 43.327 39.607 1.00 21.37 ? 429 LEU A CD1 1 ATOM 3074 C CD2 . LEU A 1 388 ? 5.905 45.758 39.791 1.00 22.92 ? 429 LEU A CD2 1 ATOM 3075 N N . GLY A 1 389 ? 5.449 44.469 45.055 1.00 21.00 ? 430 GLY A N 1 ATOM 3076 C CA . GLY A 1 389 ? 4.756 44.200 46.332 1.00 21.10 ? 430 GLY A CA 1 ATOM 3077 C C . GLY A 1 389 ? 4.808 45.413 47.255 1.00 20.87 ? 430 GLY A C 1 ATOM 3078 O O . GLY A 1 389 ? 3.762 45.800 47.809 1.00 21.53 ? 430 GLY A O 1 ATOM 3079 N N . SER A 1 390 ? 5.989 46.002 47.429 1.00 20.44 ? 431 SER A N 1 ATOM 3080 C CA . SER A 1 390 ? 6.076 47.184 48.315 1.00 20.51 ? 431 SER A CA 1 ATOM 3081 C C . SER A 1 390 ? 5.261 48.354 47.697 1.00 19.65 ? 431 SER A C 1 ATOM 3082 O O . SER A 1 390 ? 4.561 49.064 48.410 1.00 18.71 ? 431 SER A O 1 ATOM 3083 C CB . SER A 1 390 ? 7.527 47.631 48.477 1.00 20.35 ? 431 SER A CB 1 ATOM 3084 O OG . SER A 1 390 ? 8.157 47.936 47.212 1.00 21.20 ? 431 SER A OG 1 ATOM 3085 N N . THR A 1 391 ? 5.340 48.534 46.377 1.00 19.71 ? 432 THR A N 1 ATOM 3086 C CA . THR A 1 391 ? 4.676 49.675 45.727 1.00 19.07 ? 432 THR A CA 1 ATOM 3087 C C . THR A 1 391 ? 3.157 49.553 45.797 1.00 18.99 ? 432 THR A C 1 ATOM 3088 O O . THR A 1 391 ? 2.476 50.542 46.134 1.00 20.01 ? 432 THR A O 1 ATOM 3089 C CB . THR A 1 391 ? 5.170 49.872 44.251 1.00 21.26 ? 432 THR A CB 1 ATOM 3090 O OG1 . THR A 1 391 ? 6.597 50.030 44.322 1.00 20.90 ? 432 THR A OG1 1 ATOM 3091 C CG2 . THR A 1 391 ? 4.583 51.223 43.674 1.00 21.47 ? 432 THR A CG2 1 ATOM 3092 N N . GLU A 1 392 ? 2.613 48.365 45.483 1.00 18.88 ? 433 GLU A N 1 ATOM 3093 C CA . GLU A 1 392 ? 1.161 48.191 45.567 1.00 20.46 ? 433 GLU A CA 1 ATOM 3094 C C . GLU A 1 392 ? 0.666 48.429 47.015 1.00 20.20 ? 433 GLU A C 1 ATOM 3095 O O . GLU A 1 392 ? -0.370 49.043 47.214 1.00 19.91 ? 433 GLU A O 1 ATOM 3096 C CB . GLU A 1 392 ? 0.723 46.803 45.098 1.00 19.93 ? 433 GLU A CB 1 ATOM 3097 C CG . GLU A 1 392 ? 0.952 46.577 43.563 1.00 24.48 ? 433 GLU A CG 1 ATOM 3098 C CD . GLU A 1 392 ? 0.360 47.687 42.696 1.00 23.61 ? 433 GLU A CD 1 ATOM 3099 O OE1 . GLU A 1 392 ? -0.866 47.918 42.755 1.00 23.72 ? 433 GLU A OE1 1 ATOM 3100 O OE2 . GLU A 1 392 ? 1.093 48.384 41.965 1.00 23.56 ? 433 GLU A OE2 1 ATOM 3101 N N . TRP A 1 393 ? 1.370 47.894 48.009 1.00 19.54 ? 434 TRP A N 1 ATOM 3102 C CA . TRP A 1 393 ? 0.938 48.055 49.411 1.00 19.40 ? 434 TRP A CA 1 ATOM 3103 C C . TRP A 1 393 ? 1.019 49.545 49.784 1.00 20.44 ? 434 TRP A C 1 ATOM 3104 O O . TRP A 1 393 ? 0.128 50.063 50.454 1.00 20.34 ? 434 TRP A O 1 ATOM 3105 C CB . TRP A 1 393 ? 1.851 47.223 50.333 1.00 19.77 ? 434 TRP A CB 1 ATOM 3106 C CG . TRP A 1 393 ? 1.414 47.245 51.814 1.00 20.70 ? 434 TRP A CG 1 ATOM 3107 C CD1 . TRP A 1 393 ? 0.432 46.475 52.424 1.00 21.79 ? 434 TRP A CD1 1 ATOM 3108 C CD2 . TRP A 1 393 ? 1.923 48.120 52.800 1.00 21.48 ? 434 TRP A CD2 1 ATOM 3109 N NE1 . TRP A 1 393 ? 0.352 46.817 53.771 1.00 22.35 ? 434 TRP A NE1 1 ATOM 3110 C CE2 . TRP A 1 393 ? 1.280 47.797 54.029 1.00 23.47 ? 434 TRP A CE2 1 ATOM 3111 C CE3 . TRP A 1 393 ? 2.899 49.131 52.780 1.00 21.45 ? 434 TRP A CE3 1 ATOM 3112 C CZ2 . TRP A 1 393 ? 1.572 48.459 55.228 1.00 23.61 ? 434 TRP A CZ2 1 ATOM 3113 C CZ3 . TRP A 1 393 ? 3.227 49.787 54.012 1.00 23.83 ? 434 TRP A CZ3 1 ATOM 3114 C CH2 . TRP A 1 393 ? 2.545 49.446 55.204 1.00 23.56 ? 434 TRP A CH2 1 ATOM 3115 N N . ALA A 1 394 ? 2.077 50.235 49.346 1.00 20.08 ? 435 ALA A N 1 ATOM 3116 C CA . ALA A 1 394 ? 2.154 51.662 49.650 1.00 20.98 ? 435 ALA A CA 1 ATOM 3117 C C . ALA A 1 394 ? 1.065 52.470 48.935 1.00 20.89 ? 435 ALA A C 1 ATOM 3118 O O . ALA A 1 394 ? 0.565 53.452 49.483 1.00 20.34 ? 435 ALA A O 1 ATOM 3119 C CB . ALA A 1 394 ? 3.539 52.231 49.305 1.00 21.40 ? 435 ALA A CB 1 ATOM 3120 N N . GLU A 1 395 ? 0.720 52.087 47.706 1.00 20.65 ? 436 GLU A N 1 ATOM 3121 C CA . GLU A 1 395 ? -0.424 52.742 47.016 1.00 20.65 ? 436 GLU A CA 1 ATOM 3122 C C . GLU A 1 395 ? -1.730 52.499 47.777 1.00 21.60 ? 436 GLU A C 1 ATOM 3123 O O . GLU A 1 395 ? -2.571 53.413 47.913 1.00 20.40 ? 436 GLU A O 1 ATOM 3124 C CB . GLU A 1 395 ? -0.604 52.224 45.569 1.00 21.18 ? 436 GLU A CB 1 ATOM 3125 C CG . GLU A 1 395 ? 0.538 52.771 44.682 1.00 21.40 ? 436 GLU A CG 1 ATOM 3126 C CD . GLU A 1 395 ? 0.436 52.384 43.201 1.00 25.12 ? 436 GLU A CD 1 ATOM 3127 O OE1 . GLU A 1 395 ? 0.857 53.222 42.382 1.00 22.72 ? 436 GLU A OE1 1 ATOM 3128 O OE2 . GLU A 1 395 ? -0.066 51.272 42.923 1.00 23.75 ? 436 GLU A OE2 1 ATOM 3129 N N . GLU A 1 396 ? -1.932 51.271 48.245 1.00 19.58 ? 437 GLU A N 1 ATOM 3130 C CA . GLU A 1 396 ? -3.124 51.000 49.046 1.00 21.01 ? 437 GLU A CA 1 ATOM 3131 C C . GLU A 1 396 ? -3.168 51.857 50.336 1.00 21.95 ? 437 GLU A C 1 ATOM 3132 O O . GLU A 1 396 ? -4.259 52.368 50.713 1.00 22.19 ? 437 GLU A O 1 ATOM 3133 C CB . GLU A 1 396 ? -3.144 49.529 49.417 1.00 21.36 ? 437 GLU A CB 1 ATOM 3134 C CG . GLU A 1 396 ? -4.482 49.074 50.107 1.00 27.55 ? 437 GLU A CG 1 ATOM 3135 C CD . GLU A 1 396 ? -4.695 47.581 49.853 1.00 39.59 ? 437 GLU A CD 1 ATOM 3136 O OE1 . GLU A 1 396 ? -5.532 47.182 49.012 1.00 47.99 ? 437 GLU A OE1 1 ATOM 3137 O OE2 . GLU A 1 396 ? -3.959 46.818 50.437 1.00 36.58 ? 437 GLU A OE2 1 ATOM 3138 N N . ASN A 1 397 ? -2.013 51.967 50.986 1.00 21.69 ? 438 ASN A N 1 ATOM 3139 C CA . ASN A 1 397 ? -1.929 52.564 52.363 1.00 21.34 ? 438 ASN A CA 1 ATOM 3140 C C . ASN A 1 397 ? -1.349 53.983 52.398 1.00 21.70 ? 438 ASN A C 1 ATOM 3141 O O . ASN A 1 397 ? -1.004 54.507 53.473 1.00 20.81 ? 438 ASN A O 1 ATOM 3142 C CB . ASN A 1 397 ? -1.193 51.580 53.298 1.00 22.96 ? 438 ASN A CB 1 ATOM 3143 C CG . ASN A 1 397 ? -1.978 50.337 53.485 1.00 24.00 ? 438 ASN A CG 1 ATOM 3144 O OD1 . ASN A 1 397 ? -3.049 50.360 54.093 1.00 27.59 ? 438 ASN A OD1 1 ATOM 3145 N ND2 . ASN A 1 397 ? -1.513 49.243 52.912 1.00 25.24 ? 438 ASN A ND2 1 ATOM 3146 N N . SER A 1 398 ? -1.364 54.663 51.233 1.00 20.10 ? 439 SER A N 1 ATOM 3147 C CA . SER A 1 398 ? -0.604 55.909 51.114 1.00 21.12 ? 439 SER A CA 1 ATOM 3148 C C . SER A 1 398 ? -1.076 56.996 52.102 1.00 20.53 ? 439 SER A C 1 ATOM 3149 O O . SER A 1 398 ? -0.253 57.791 52.571 1.00 21.55 ? 439 SER A O 1 ATOM 3150 C CB . SER A 1 398 ? -0.702 56.465 49.662 1.00 21.58 ? 439 SER A CB 1 ATOM 3151 O OG . SER A 1 398 ? -2.043 56.787 49.369 1.00 22.56 ? 439 SER A OG 1 ATOM 3152 N N . ARG A 1 399 ? -2.383 57.067 52.350 1.00 20.51 ? 440 ARG A N 1 ATOM 3153 C CA . ARG A 1 399 ? -2.908 58.094 53.306 1.00 21.80 ? 440 ARG A CA 1 ATOM 3154 C C . ARG A 1 399 ? -2.401 57.831 54.736 1.00 23.25 ? 440 ARG A C 1 ATOM 3155 O O . ARG A 1 399 ? -2.072 58.766 55.481 1.00 22.94 ? 440 ARG A O 1 ATOM 3156 C CB . ARG A 1 399 ? -4.429 58.104 53.306 1.00 22.17 ? 440 ARG A CB 1 ATOM 3157 C CG . ARG A 1 399 ? -4.934 58.655 51.950 1.00 25.03 ? 440 ARG A CG 1 ATOM 3158 C CD . ARG A 1 399 ? -6.235 58.032 51.534 1.00 29.01 ? 440 ARG A CD 1 ATOM 3159 N NE . ARG A 1 399 ? -6.628 58.573 50.216 1.00 27.76 ? 440 ARG A NE 1 ATOM 3160 C CZ . ARG A 1 399 ? -6.191 58.158 49.034 1.00 29.70 ? 440 ARG A CZ 1 ATOM 3161 N NH1 . ARG A 1 399 ? -5.351 57.105 48.924 1.00 30.70 ? 440 ARG A NH1 1 ATOM 3162 N NH2 . ARG A 1 399 ? -6.615 58.789 47.945 1.00 25.92 ? 440 ARG A NH2 1 ATOM 3163 N N . LEU A 1 400 ? -2.402 56.568 55.137 1.00 23.03 ? 441 LEU A N 1 ATOM 3164 C CA . LEU A 1 400 ? -1.857 56.218 56.463 1.00 22.90 ? 441 LEU A CA 1 ATOM 3165 C C . LEU A 1 400 ? -0.345 56.532 56.522 1.00 23.48 ? 441 LEU A C 1 ATOM 3166 O O . LEU A 1 400 ? 0.169 57.113 57.486 1.00 23.23 ? 441 LEU A O 1 ATOM 3167 C CB . LEU A 1 400 ? -2.103 54.739 56.742 1.00 23.59 ? 441 LEU A CB 1 ATOM 3168 C CG . LEU A 1 400 ? -3.528 54.182 56.627 1.00 25.18 ? 441 LEU A CG 1 ATOM 3169 C CD1 . LEU A 1 400 ? -3.653 52.683 57.036 1.00 29.13 ? 441 LEU A CD1 1 ATOM 3170 C CD2 . LEU A 1 400 ? -4.506 55.033 57.456 1.00 27.86 ? 441 LEU A CD2 1 ATOM 3171 N N . LEU A 1 401 ? 0.365 56.189 55.472 1.00 21.47 ? 442 LEU A N 1 ATOM 3172 C CA . LEU A 1 401 ? 1.806 56.348 55.471 1.00 22.03 ? 442 LEU A CA 1 ATOM 3173 C C . LEU A 1 401 ? 2.204 57.802 55.440 1.00 22.51 ? 442 LEU A C 1 ATOM 3174 O O . LEU A 1 401 ? 3.166 58.217 56.096 1.00 25.43 ? 442 LEU A O 1 ATOM 3175 C CB . LEU A 1 401 ? 2.397 55.621 54.207 1.00 22.23 ? 442 LEU A CB 1 ATOM 3176 C CG . LEU A 1 401 ? 2.213 54.109 54.286 1.00 24.39 ? 442 LEU A CG 1 ATOM 3177 C CD1 . LEU A 1 401 ? 2.577 53.475 52.895 1.00 21.26 ? 442 LEU A CD1 1 ATOM 3178 C CD2 . LEU A 1 401 ? 3.093 53.450 55.433 1.00 28.35 ? 442 LEU A CD2 1 ATOM 3179 N N A GLN A 1 402 ? 1.480 58.571 54.624 0.50 22.76 ? 443 GLN A N 1 ATOM 3180 N N B GLN A 1 402 ? 1.532 58.617 54.657 0.50 21.75 ? 443 GLN A N 1 ATOM 3181 C CA A GLN A 1 402 ? 1.680 60.014 54.451 0.50 23.89 ? 443 GLN A CA 1 ATOM 3182 C CA B GLN A 1 402 ? 2.031 59.971 54.589 0.50 22.22 ? 443 GLN A CA 1 ATOM 3183 C C A GLN A 1 402 ? 1.650 60.707 55.818 0.50 23.96 ? 443 GLN A C 1 ATOM 3184 C C B GLN A 1 402 ? 1.636 60.805 55.825 0.50 22.91 ? 443 GLN A C 1 ATOM 3185 O O A GLN A 1 402 ? 2.539 61.498 56.165 0.50 23.79 ? 443 GLN A O 1 ATOM 3186 O O B GLN A 1 402 ? 2.267 61.831 56.079 0.50 23.04 ? 443 GLN A O 1 ATOM 3187 C CB A GLN A 1 402 ? 0.551 60.584 53.572 0.50 23.87 ? 443 GLN A CB 1 ATOM 3188 C CB B GLN A 1 402 ? 1.614 60.668 53.309 0.50 20.34 ? 443 GLN A CB 1 ATOM 3189 C CG A GLN A 1 402 ? 0.290 62.043 53.713 0.50 25.85 ? 443 GLN A CG 1 ATOM 3190 C CG B GLN A 1 402 ? 0.103 60.963 53.232 0.50 20.77 ? 443 GLN A CG 1 ATOM 3191 C CD A GLN A 1 402 ? 1.231 62.892 52.901 0.50 30.12 ? 443 GLN A CD 1 ATOM 3192 C CD B GLN A 1 402 ? -0.321 61.205 51.793 0.50 26.12 ? 443 GLN A CD 1 ATOM 3193 O OE1 A GLN A 1 402 ? 1.730 62.443 51.854 0.50 33.89 ? 443 GLN A OE1 1 ATOM 3194 O OE1 B GLN A 1 402 ? -1.502 61.484 51.511 0.50 27.79 ? 443 GLN A OE1 1 ATOM 3195 N NE2 A GLN A 1 402 ? 1.475 64.134 53.359 0.50 25.37 ? 443 GLN A NE2 1 ATOM 3196 N NE2 B GLN A 1 402 ? 0.638 61.078 50.867 0.50 23.99 ? 443 GLN A NE2 1 ATOM 3197 N N . GLU A 1 403 ? 0.622 60.375 56.592 1.00 22.92 ? 444 GLU A N 1 ATOM 3198 C CA . GLU A 1 403 ? 0.312 61.129 57.815 1.00 22.98 ? 444 GLU A CA 1 ATOM 3199 C C . GLU A 1 403 ? 0.951 60.500 59.073 1.00 22.81 ? 444 GLU A C 1 ATOM 3200 O O . GLU A 1 403 ? 1.081 61.193 60.073 1.00 23.23 ? 444 GLU A O 1 ATOM 3201 C CB . GLU A 1 403 ? -1.189 61.268 58.034 1.00 25.47 ? 444 GLU A CB 1 ATOM 3202 C CG . GLU A 1 403 ? -1.955 61.893 56.794 1.00 26.09 ? 444 GLU A CG 1 ATOM 3203 C CD . GLU A 1 403 ? -1.341 63.200 56.196 1.00 32.88 ? 444 GLU A CD 1 ATOM 3204 O OE1 . GLU A 1 403 ? -0.356 63.757 56.748 1.00 29.99 ? 444 GLU A OE1 1 ATOM 3205 O OE2 . GLU A 1 403 ? -1.863 63.683 55.142 1.00 31.45 ? 444 GLU A OE2 1 ATOM 3206 N N . ARG A 1 404 ? 1.390 59.255 58.977 1.00 21.22 ? 445 ARG A N 1 ATOM 3207 C CA . ARG A 1 404 ? 1.871 58.525 60.176 1.00 21.86 ? 445 ARG A CA 1 ATOM 3208 C C . ARG A 1 404 ? 3.268 57.932 60.056 1.00 23.12 ? 445 ARG A C 1 ATOM 3209 O O . ARG A 1 404 ? 3.793 57.472 61.055 1.00 24.16 ? 445 ARG A O 1 ATOM 3210 C CB . ARG A 1 404 ? 0.879 57.387 60.452 1.00 20.63 ? 445 ARG A CB 1 ATOM 3211 C CG . ARG A 1 404 ? -0.584 57.943 60.729 1.00 21.19 ? 445 ARG A CG 1 ATOM 3212 C CD . ARG A 1 404 ? -1.537 56.762 60.979 1.00 22.09 ? 445 ARG A CD 1 ATOM 3213 N NE . ARG A 1 404 ? -2.916 57.218 60.937 1.00 25.03 ? 445 ARG A NE 1 ATOM 3214 C CZ . ARG A 1 404 ? -3.950 56.401 60.919 1.00 23.59 ? 445 ARG A CZ 1 ATOM 3215 N NH1 . ARG A 1 404 ? -3.721 55.081 61.002 1.00 24.46 ? 445 ARG A NH1 1 ATOM 3216 N NH2 . ARG A 1 404 ? -5.172 56.909 60.840 1.00 23.92 ? 445 ARG A NH2 1 ATOM 3217 N N . GLY A 1 405 ? 3.842 57.925 58.848 1.00 23.57 ? 446 GLY A N 1 ATOM 3218 C CA . GLY A 1 405 ? 5.120 57.194 58.604 1.00 24.23 ? 446 GLY A CA 1 ATOM 3219 C C . GLY A 1 405 ? 6.310 58.016 59.085 1.00 23.67 ? 446 GLY A C 1 ATOM 3220 O O . GLY A 1 405 ? 6.606 59.132 58.571 1.00 25.07 ? 446 GLY A O 1 ATOM 3221 N N . VAL A 1 406 ? 6.994 57.483 60.079 1.00 22.54 ? 447 VAL A N 1 ATOM 3222 C CA . VAL A 1 406 ? 8.200 58.118 60.596 1.00 23.31 ? 447 VAL A CA 1 ATOM 3223 C C . VAL A 1 406 ? 9.429 57.822 59.740 1.00 22.79 ? 447 VAL A C 1 ATOM 3224 O O . VAL A 1 406 ? 10.183 58.730 59.360 1.00 22.86 ? 447 VAL A O 1 ATOM 3225 C CB . VAL A 1 406 ? 8.444 57.639 62.060 1.00 24.88 ? 447 VAL A CB 1 ATOM 3226 C CG1 . VAL A 1 406 ? 9.812 58.052 62.537 1.00 25.24 ? 447 VAL A CG1 1 ATOM 3227 C CG2 . VAL A 1 406 ? 7.263 58.226 62.928 1.00 26.78 ? 447 VAL A CG2 1 ATOM 3228 N N . ALA A 1 407 ? 9.642 56.542 59.448 1.00 22.77 ? 448 ALA A N 1 ATOM 3229 C CA . ALA A 1 407 ? 10.860 56.105 58.759 1.00 21.31 ? 448 ALA A CA 1 ATOM 3230 C C . ALA A 1 407 ? 10.654 54.721 58.191 1.00 22.13 ? 448 ALA A C 1 ATOM 3231 O O . ALA A 1 407 ? 9.805 53.929 58.664 1.00 23.31 ? 448 ALA A O 1 ATOM 3232 C CB . ALA A 1 407 ? 12.053 56.073 59.748 1.00 22.27 ? 448 ALA A CB 1 ATOM 3233 N N . TYR A 1 408 ? 11.451 54.436 57.158 1.00 22.36 ? 449 TYR A N 1 ATOM 3234 C CA . TYR A 1 408 ? 11.475 53.137 56.509 1.00 22.81 ? 449 TYR A CA 1 ATOM 3235 C C . TYR A 1 408 ? 12.929 52.695 56.427 1.00 22.31 ? 449 TYR A C 1 ATOM 3236 O O . TYR A 1 408 ? 13.795 53.415 55.914 1.00 23.74 ? 449 TYR A O 1 ATOM 3237 C CB . TYR A 1 408 ? 10.900 53.250 55.059 1.00 22.00 ? 449 TYR A CB 1 ATOM 3238 C CG . TYR A 1 408 ? 10.974 51.901 54.363 1.00 21.28 ? 449 TYR A CG 1 ATOM 3239 C CD1 . TYR A 1 408 ? 9.941 50.993 54.476 1.00 22.38 ? 449 TYR A CD1 1 ATOM 3240 C CD2 . TYR A 1 408 ? 12.062 51.564 53.620 1.00 21.91 ? 449 TYR A CD2 1 ATOM 3241 C CE1 . TYR A 1 408 ? 10.027 49.727 53.882 1.00 22.88 ? 449 TYR A CE1 1 ATOM 3242 C CE2 . TYR A 1 408 ? 12.187 50.288 52.978 1.00 22.95 ? 449 TYR A CE2 1 ATOM 3243 C CZ . TYR A 1 408 ? 11.147 49.403 53.101 1.00 26.31 ? 449 TYR A CZ 1 ATOM 3244 O OH . TYR A 1 408 ? 11.239 48.186 52.480 1.00 24.97 ? 449 TYR A OH 1 ATOM 3245 N N . ILE A 1 409 ? 13.210 51.507 56.941 1.00 21.80 ? 450 ILE A N 1 ATOM 3246 C CA . ILE A 1 409 ? 14.536 50.912 56.897 1.00 22.15 ? 450 ILE A CA 1 ATOM 3247 C C . ILE A 1 409 ? 14.411 49.673 55.998 1.00 23.03 ? 450 ILE A C 1 ATOM 3248 O O . ILE A 1 409 ? 13.571 48.789 56.229 1.00 23.01 ? 450 ILE A O 1 ATOM 3249 C CB . ILE A 1 409 ? 15.024 50.469 58.303 1.00 23.43 ? 450 ILE A CB 1 ATOM 3250 C CG1 . ILE A 1 409 ? 15.145 51.679 59.287 1.00 24.67 ? 450 ILE A CG1 1 ATOM 3251 C CG2 . ILE A 1 409 ? 16.382 49.725 58.217 1.00 23.54 ? 450 ILE A CG2 1 ATOM 3252 C CD1 . ILE A 1 409 ? 16.098 52.787 58.794 1.00 26.56 ? 450 ILE A CD1 1 ATOM 3253 N N . ASN A 1 410 ? 15.188 49.652 54.937 1.00 22.38 ? 451 ASN A N 1 ATOM 3254 C CA . ASN A 1 410 ? 15.108 48.520 53.969 1.00 23.41 ? 451 ASN A CA 1 ATOM 3255 C C . ASN A 1 410 ? 15.966 47.354 54.480 1.00 25.03 ? 451 ASN A C 1 ATOM 3256 O O . ASN A 1 410 ? 16.869 47.525 55.328 1.00 26.42 ? 451 ASN A O 1 ATOM 3257 C CB . ASN A 1 410 ? 15.661 48.961 52.606 1.00 22.58 ? 451 ASN A CB 1 ATOM 3258 C CG . ASN A 1 410 ? 15.085 48.154 51.471 1.00 25.96 ? 451 ASN A CG 1 ATOM 3259 O OD1 . ASN A 1 410 ? 13.865 47.990 51.374 1.00 27.29 ? 451 ASN A OD1 1 ATOM 3260 N ND2 . ASN A 1 410 ? 15.958 47.608 50.623 1.00 26.07 ? 451 ASN A ND2 1 ATOM 3261 N N . ALA A 1 411 ? 15.718 46.152 53.967 1.00 24.39 ? 452 ALA A N 1 ATOM 3262 C CA . ALA A 1 411 ? 16.491 45.000 54.443 1.00 25.15 ? 452 ALA A CA 1 ATOM 3263 C C . ALA A 1 411 ? 16.530 43.970 53.338 1.00 25.83 ? 452 ALA A C 1 ATOM 3264 O O . ALA A 1 411 ? 16.108 42.819 53.523 1.00 26.91 ? 452 ALA A O 1 ATOM 3265 C CB . ALA A 1 411 ? 15.820 44.398 55.706 1.00 26.39 ? 452 ALA A CB 1 ATOM 3266 N N . ASP A 1 412 ? 17.177 44.325 52.239 1.00 24.61 ? 453 ASP A N 1 ATOM 3267 C CA . ASP A 1 412 ? 17.480 43.295 51.240 1.00 25.98 ? 453 ASP A CA 1 ATOM 3268 C C . ASP A 1 412 ? 18.846 42.747 51.699 1.00 27.74 ? 453 ASP A C 1 ATOM 3269 O O . ASP A 1 412 ? 19.179 42.883 52.894 1.00 28.10 ? 453 ASP A O 1 ATOM 3270 C CB . ASP A 1 412 ? 17.485 43.929 49.844 1.00 24.59 ? 453 ASP A CB 1 ATOM 3271 C CG . ASP A 1 412 ? 17.450 42.888 48.699 1.00 25.87 ? 453 ASP A CG 1 ATOM 3272 O OD1 . ASP A 1 412 ? 17.612 41.694 48.965 1.00 29.48 ? 453 ASP A OD1 1 ATOM 3273 O OD2 . ASP A 1 412 ? 17.317 43.315 47.536 1.00 25.36 ? 453 ASP A OD2 1 ATOM 3274 N N A SER A 1 413 ? 19.597 42.135 50.786 0.80 27.28 ? 454 SER A N 1 ATOM 3275 N N B SER A 1 413 ? 19.619 42.160 50.780 0.20 26.83 ? 454 SER A N 1 ATOM 3276 C CA A SER A 1 413 ? 20.859 41.449 51.097 0.80 27.51 ? 454 SER A CA 1 ATOM 3277 C CA B SER A 1 413 ? 20.868 41.398 51.048 0.20 26.58 ? 454 SER A CA 1 ATOM 3278 C C A SER A 1 413 ? 21.659 42.136 52.215 0.80 28.10 ? 454 SER A C 1 ATOM 3279 C C B SER A 1 413 ? 21.879 41.977 52.056 0.20 27.14 ? 454 SER A C 1 ATOM 3280 O O A SER A 1 413 ? 21.901 43.366 52.190 0.80 27.22 ? 454 SER A O 1 ATOM 3281 O O B SER A 1 413 ? 22.587 42.932 51.742 0.20 26.51 ? 454 SER A O 1 ATOM 3282 C CB A SER A 1 413 ? 21.721 41.363 49.849 0.80 28.15 ? 454 SER A CB 1 ATOM 3283 C CB B SER A 1 413 ? 21.604 41.180 49.729 0.20 26.82 ? 454 SER A CB 1 ATOM 3284 O OG A SER A 1 413 ? 20.941 40.897 48.749 0.80 26.15 ? 454 SER A OG 1 ATOM 3285 O OG B SER A 1 413 ? 22.021 42.420 49.174 0.20 23.57 ? 454 SER A OG 1 ATOM 3286 N N . SER A 1 414 ? 21.985 41.347 53.227 1.00 27.03 ? 455 SER A N 1 ATOM 3287 C CA . SER A 1 414 ? 22.775 41.892 54.358 1.00 29.95 ? 455 SER A CA 1 ATOM 3288 C C . SER A 1 414 ? 24.270 41.965 54.015 1.00 31.00 ? 455 SER A C 1 ATOM 3289 O O . SER A 1 414 ? 24.991 42.767 54.581 1.00 32.06 ? 455 SER A O 1 ATOM 3290 C CB . SER A 1 414 ? 22.605 40.997 55.567 1.00 30.60 ? 455 SER A CB 1 ATOM 3291 O OG . SER A 1 414 ? 21.267 41.077 55.989 1.00 34.96 ? 455 SER A OG 1 ATOM 3292 N N . ILE A 1 415 ? 24.720 41.130 53.085 1.00 32.71 ? 456 ILE A N 1 ATOM 3293 C CA . ILE A 1 415 ? 26.128 41.080 52.676 1.00 34.50 ? 456 ILE A CA 1 ATOM 3294 C C . ILE A 1 415 ? 26.248 41.091 51.156 1.00 35.46 ? 456 ILE A C 1 ATOM 3295 O O . ILE A 1 415 ? 25.458 40.456 50.481 1.00 38.71 ? 456 ILE A O 1 ATOM 3296 C CB . ILE A 1 415 ? 26.825 39.831 53.241 1.00 35.10 ? 456 ILE A CB 1 ATOM 3297 C CG1 . ILE A 1 415 ? 25.978 38.569 52.980 1.00 36.51 ? 456 ILE A CG1 1 ATOM 3298 C CG2 . ILE A 1 415 ? 27.020 40.008 54.725 1.00 35.87 ? 456 ILE A CG2 1 ATOM 3299 C CD1 . ILE A 1 415 ? 26.776 37.324 52.783 1.00 44.46 ? 456 ILE A CD1 1 ATOM 3300 N N . GLU A 1 416 ? 27.188 41.832 50.602 1.00 34.44 ? 457 GLU A N 1 ATOM 3301 C CA . GLU A 1 416 ? 27.552 41.634 49.194 1.00 34.21 ? 457 GLU A CA 1 ATOM 3302 C C . GLU A 1 416 ? 29.063 41.567 49.158 1.00 34.16 ? 457 GLU A C 1 ATOM 3303 O O . GLU A 1 416 ? 29.689 41.619 48.098 1.00 34.61 ? 457 GLU A O 1 ATOM 3304 C CB . GLU A 1 416 ? 27.000 42.778 48.331 1.00 34.84 ? 457 GLU A CB 1 ATOM 3305 C CG . GLU A 1 416 ? 27.540 44.136 48.784 1.00 36.69 ? 457 GLU A CG 1 ATOM 3306 C CD . GLU A 1 416 ? 26.935 45.330 48.014 1.00 39.61 ? 457 GLU A CD 1 ATOM 3307 O OE1 . GLU A 1 416 ? 25.851 45.180 47.397 1.00 39.05 ? 457 GLU A OE1 1 ATOM 3308 O OE2 . GLU A 1 416 ? 27.571 46.410 48.044 1.00 40.15 ? 457 GLU A OE2 1 ATOM 3309 N N . GLY A 1 417 ? 29.649 41.453 50.349 1.00 33.82 ? 458 GLY A N 1 ATOM 3310 C CA . GLY A 1 417 ? 31.093 41.329 50.524 1.00 34.81 ? 458 GLY A CA 1 ATOM 3311 C C . GLY A 1 417 ? 31.380 41.285 52.013 1.00 34.95 ? 458 GLY A C 1 ATOM 3312 O O . GLY A 1 417 ? 30.450 41.267 52.829 1.00 34.82 ? 458 GLY A O 1 ATOM 3313 N N . ASN A 1 418 ? 32.642 41.295 52.382 1.00 34.67 ? 459 ASN A N 1 ATOM 3314 C CA . ASN A 1 418 ? 32.979 41.191 53.798 1.00 35.84 ? 459 ASN A CA 1 ATOM 3315 C C . ASN A 1 418 ? 34.035 42.176 54.233 1.00 35.34 ? 459 ASN A C 1 ATOM 3316 O O . ASN A 1 418 ? 34.747 41.946 55.202 1.00 37.51 ? 459 ASN A O 1 ATOM 3317 C CB . ASN A 1 418 ? 33.346 39.741 54.190 1.00 36.95 ? 459 ASN A CB 1 ATOM 3318 C CG . ASN A 1 418 ? 34.607 39.227 53.509 1.00 39.57 ? 459 ASN A CG 1 ATOM 3319 O OD1 . ASN A 1 418 ? 35.403 39.992 52.939 1.00 37.41 ? 459 ASN A OD1 1 ATOM 3320 N ND2 . ASN A 1 418 ? 34.810 37.909 53.579 1.00 53.50 ? 459 ASN A ND2 1 ATOM 3321 N N . TYR A 1 419 ? 34.103 43.314 53.551 1.00 34.40 ? 460 TYR A N 1 ATOM 3322 C CA . TYR A 1 419 ? 35.175 44.273 53.787 1.00 33.85 ? 460 TYR A CA 1 ATOM 3323 C C . TYR A 1 419 ? 34.748 45.333 54.808 1.00 34.45 ? 460 TYR A C 1 ATOM 3324 O O . TYR A 1 419 ? 35.448 45.553 55.800 1.00 34.16 ? 460 TYR A O 1 ATOM 3325 C CB . TYR A 1 419 ? 35.550 44.961 52.475 1.00 34.34 ? 460 TYR A CB 1 ATOM 3326 C CG . TYR A 1 419 ? 36.704 45.950 52.618 1.00 39.51 ? 460 TYR A CG 1 ATOM 3327 C CD1 . TYR A 1 419 ? 37.988 45.522 53.028 1.00 44.50 ? 460 TYR A CD1 1 ATOM 3328 C CD2 . TYR A 1 419 ? 36.525 47.289 52.310 1.00 43.76 ? 460 TYR A CD2 1 ATOM 3329 C CE1 . TYR A 1 419 ? 39.056 46.444 53.156 1.00 48.99 ? 460 TYR A CE1 1 ATOM 3330 C CE2 . TYR A 1 419 ? 37.577 48.216 52.438 1.00 45.46 ? 460 TYR A CE2 1 ATOM 3331 C CZ . TYR A 1 419 ? 38.822 47.791 52.837 1.00 50.79 ? 460 TYR A CZ 1 ATOM 3332 O OH . TYR A 1 419 ? 39.827 48.732 52.933 1.00 55.94 ? 460 TYR A OH 1 ATOM 3333 N N . THR A 1 420 ? 33.612 45.995 54.547 1.00 33.13 ? 461 THR A N 1 ATOM 3334 C CA . THR A 1 420 ? 33.181 47.075 55.454 1.00 33.11 ? 461 THR A CA 1 ATOM 3335 C C . THR A 1 420 ? 31.709 47.381 55.283 1.00 31.76 ? 461 THR A C 1 ATOM 3336 O O . THR A 1 420 ? 31.038 46.805 54.424 1.00 31.59 ? 461 THR A O 1 ATOM 3337 C CB . THR A 1 420 ? 34.032 48.377 55.307 1.00 34.42 ? 461 THR A CB 1 ATOM 3338 O OG1 . THR A 1 420 ? 33.811 49.219 56.450 1.00 33.81 ? 461 THR A OG1 1 ATOM 3339 C CG2 . THR A 1 420 ? 33.655 49.161 54.064 1.00 33.17 ? 461 THR A CG2 1 ATOM 3340 N N . LEU A 1 421 ? 31.206 48.255 56.151 1.00 30.78 ? 462 LEU A N 1 ATOM 3341 C CA . LEU A 1 421 ? 29.820 48.719 56.053 1.00 29.63 ? 462 LEU A CA 1 ATOM 3342 C C . LEU A 1 421 ? 29.586 49.655 54.879 1.00 29.51 ? 462 LEU A C 1 ATOM 3343 O O . LEU A 1 421 ? 30.492 50.404 54.492 1.00 29.52 ? 462 LEU A O 1 ATOM 3344 C CB . LEU A 1 421 ? 29.421 49.440 57.359 1.00 30.25 ? 462 LEU A CB 1 ATOM 3345 C CG . LEU A 1 421 ? 27.917 49.604 57.571 1.00 28.61 ? 462 LEU A CG 1 ATOM 3346 C CD1 . LEU A 1 421 ? 27.266 48.216 57.843 1.00 28.74 ? 462 LEU A CD1 1 ATOM 3347 C CD2 . LEU A 1 421 ? 27.830 50.530 58.817 1.00 30.45 ? 462 LEU A CD2 1 ATOM 3348 N N . ARG A 1 422 ? 28.382 49.593 54.327 1.00 27.85 ? 463 ARG A N 1 ATOM 3349 C CA . ARG A 1 422 ? 27.925 50.508 53.286 1.00 27.96 ? 463 ARG A CA 1 ATOM 3350 C C . ARG A 1 422 ? 26.564 51.002 53.757 1.00 28.29 ? 463 ARG A C 1 ATOM 3351 O O . ARG A 1 422 ? 25.687 50.203 54.115 1.00 28.45 ? 463 ARG A O 1 ATOM 3352 C CB . ARG A 1 422 ? 27.837 49.729 51.945 1.00 28.83 ? 463 ARG A CB 1 ATOM 3353 C CG . ARG A 1 422 ? 27.301 50.571 50.747 1.00 31.09 ? 463 ARG A CG 1 ATOM 3354 C CD . ARG A 1 422 ? 27.325 49.728 49.448 1.00 33.76 ? 463 ARG A CD 1 ATOM 3355 N NE . ARG A 1 422 ? 26.954 50.527 48.265 1.00 40.92 ? 463 ARG A NE 1 ATOM 3356 C CZ . ARG A 1 422 ? 26.882 50.072 47.001 1.00 42.36 ? 463 ARG A CZ 1 ATOM 3357 N NH1 . ARG A 1 422 ? 27.161 48.799 46.703 1.00 41.30 ? 463 ARG A NH1 1 ATOM 3358 N NH2 . ARG A 1 422 ? 26.524 50.900 46.009 1.00 42.94 ? 463 ARG A NH2 1 ATOM 3359 N N . VAL A 1 423 ? 26.369 52.320 53.744 1.00 27.36 ? 464 VAL A N 1 ATOM 3360 C CA . VAL A 1 423 ? 25.070 52.911 54.157 1.00 27.24 ? 464 VAL A CA 1 ATOM 3361 C C . VAL A 1 423 ? 24.632 53.940 53.102 1.00 27.76 ? 464 VAL A C 1 ATOM 3362 O O . VAL A 1 423 ? 25.429 54.765 52.657 1.00 28.62 ? 464 VAL A O 1 ATOM 3363 C CB . VAL A 1 423 ? 25.208 53.615 55.524 1.00 28.20 ? 464 VAL A CB 1 ATOM 3364 C CG1 . VAL A 1 423 ? 23.864 54.296 55.996 1.00 27.61 ? 464 VAL A CG1 1 ATOM 3365 C CG2 . VAL A 1 423 ? 25.715 52.642 56.603 1.00 28.85 ? 464 VAL A CG2 1 ATOM 3366 N N . ASP A 1 424 ? 23.359 53.898 52.745 1.00 25.31 ? 465 ASP A N 1 ATOM 3367 C CA . ASP A 1 424 ? 22.721 54.981 51.998 1.00 27.64 ? 465 ASP A CA 1 ATOM 3368 C C . ASP A 1 424 ? 21.508 55.413 52.813 1.00 25.96 ? 465 ASP A C 1 ATOM 3369 O O . ASP A 1 424 ? 20.704 54.581 53.177 1.00 26.39 ? 465 ASP A O 1 ATOM 3370 C CB . ASP A 1 424 ? 22.129 54.523 50.651 1.00 27.83 ? 465 ASP A CB 1 ATOM 3371 C CG . ASP A 1 424 ? 23.172 54.037 49.643 1.00 36.59 ? 465 ASP A CG 1 ATOM 3372 O OD1 . ASP A 1 424 ? 24.353 53.864 49.975 1.00 41.83 ? 465 ASP A OD1 1 ATOM 3373 O OD2 . ASP A 1 424 ? 22.750 53.787 48.482 1.00 45.58 ? 465 ASP A OD2 1 ATOM 3374 N N . CYS A 1 425 ? 21.294 56.708 52.982 1.00 25.59 ? 466 CYS A N 1 ATOM 3375 C CA . CYS A 1 425 ? 20.157 57.130 53.775 1.00 25.18 ? 466 CYS A CA 1 ATOM 3376 C C . CYS A 1 425 ? 19.892 58.599 53.576 1.00 25.62 ? 466 CYS A C 1 ATOM 3377 O O . CYS A 1 425 ? 20.690 59.279 52.988 1.00 28.87 ? 466 CYS A O 1 ATOM 3378 C CB . CYS A 1 425 ? 20.322 56.785 55.283 1.00 24.68 ? 466 CYS A CB 1 ATOM 3379 S SG . CYS A 1 425 ? 21.598 57.671 56.178 1.00 27.45 ? 466 CYS A SG 1 ATOM 3380 N N . THR A 1 426 ? 18.751 59.063 54.042 1.00 24.63 ? 467 THR A N 1 ATOM 3381 C CA . THR A 1 426 ? 18.498 60.500 54.096 1.00 23.62 ? 467 THR A CA 1 ATOM 3382 C C . THR A 1 426 ? 19.492 61.207 55.026 1.00 24.29 ? 467 THR A C 1 ATOM 3383 O O . THR A 1 426 ? 19.911 60.624 56.044 1.00 24.37 ? 467 THR A O 1 ATOM 3384 C CB . THR A 1 426 ? 17.054 60.743 54.573 1.00 23.68 ? 467 THR A CB 1 ATOM 3385 O OG1 . THR A 1 426 ? 16.870 62.135 54.817 1.00 24.28 ? 467 THR A OG1 1 ATOM 3386 C CG2 . THR A 1 426 ? 16.773 59.971 55.879 1.00 22.95 ? 467 THR A CG2 1 ATOM 3387 N N . PRO A 1 427 ? 19.880 62.466 54.722 1.00 24.40 ? 468 PRO A N 1 ATOM 3388 C CA . PRO A 1 427 ? 20.723 63.170 55.710 1.00 25.93 ? 468 PRO A CA 1 ATOM 3389 C C . PRO A 1 427 ? 20.090 63.204 57.136 1.00 25.99 ? 468 PRO A C 1 ATOM 3390 O O . PRO A 1 427 ? 20.819 63.382 58.093 1.00 26.86 ? 468 PRO A O 1 ATOM 3391 C CB . PRO A 1 427 ? 20.781 64.631 55.166 1.00 26.12 ? 468 PRO A CB 1 ATOM 3392 C CG . PRO A 1 427 ? 20.569 64.486 53.676 1.00 27.07 ? 468 PRO A CG 1 ATOM 3393 C CD . PRO A 1 427 ? 19.633 63.281 53.494 1.00 25.54 ? 468 PRO A CD 1 ATOM 3394 N N . LEU A 1 428 ? 18.751 63.077 57.238 1.00 25.65 ? 469 LEU A N 1 ATOM 3395 C CA . LEU A 1 428 ? 18.092 63.131 58.574 1.00 26.07 ? 469 LEU A CA 1 ATOM 3396 C C . LEU A 1 428 ? 18.571 62.008 59.492 1.00 26.24 ? 469 LEU A C 1 ATOM 3397 O O . LEU A 1 428 ? 18.452 62.113 60.706 1.00 28.22 ? 469 LEU A O 1 ATOM 3398 C CB . LEU A 1 428 ? 16.571 63.064 58.436 1.00 24.68 ? 469 LEU A CB 1 ATOM 3399 C CG . LEU A 1 428 ? 15.940 64.337 57.881 1.00 24.40 ? 469 LEU A CG 1 ATOM 3400 C CD1 . LEU A 1 428 ? 14.457 64.142 57.761 1.00 26.09 ? 469 LEU A CD1 1 ATOM 3401 C CD2 . LEU A 1 428 ? 16.288 65.574 58.764 1.00 24.87 ? 469 LEU A CD2 1 ATOM 3402 N N . MET A 1 429 ? 19.106 60.937 58.914 1.00 26.13 ? 470 MET A N 1 ATOM 3403 C CA . MET A 1 429 ? 19.577 59.814 59.725 1.00 25.93 ? 470 MET A CA 1 ATOM 3404 C C . MET A 1 429 ? 21.093 59.761 59.878 1.00 26.63 ? 470 MET A C 1 ATOM 3405 O O . MET A 1 429 ? 21.596 58.846 60.547 1.00 27.17 ? 470 MET A O 1 ATOM 3406 C CB . MET A 1 429 ? 19.068 58.478 59.122 1.00 26.69 ? 470 MET A CB 1 ATOM 3407 C CG . MET A 1 429 ? 17.544 58.208 59.310 1.00 28.51 ? 470 MET A CG 1 ATOM 3408 S SD . MET A 1 429 ? 17.236 56.673 58.368 1.00 37.48 ? 470 MET A SD 1 ATOM 3409 C CE . MET A 1 429 ? 15.453 56.751 58.230 1.00 35.02 ? 470 MET A CE 1 ATOM 3410 N N . TYR A 1 430 ? 21.837 60.734 59.341 1.00 25.41 ? 471 TYR A N 1 ATOM 3411 C CA . TYR A 1 430 ? 23.306 60.618 59.401 1.00 27.78 ? 471 TYR A CA 1 ATOM 3412 C C . TYR A 1 430 ? 23.797 60.536 60.855 1.00 29.42 ? 471 TYR A C 1 ATOM 3413 O O . TYR A 1 430 ? 24.670 59.718 61.200 1.00 29.76 ? 471 TYR A O 1 ATOM 3414 C CB . TYR A 1 430 ? 24.018 61.832 58.788 1.00 28.08 ? 471 TYR A CB 1 ATOM 3415 C CG . TYR A 1 430 ? 24.034 61.949 57.274 1.00 27.30 ? 471 TYR A CG 1 ATOM 3416 C CD1 . TYR A 1 430 ? 23.506 60.944 56.436 1.00 26.08 ? 471 TYR A CD1 1 ATOM 3417 C CD2 . TYR A 1 430 ? 24.510 63.124 56.693 1.00 30.20 ? 471 TYR A CD2 1 ATOM 3418 C CE1 . TYR A 1 430 ? 23.500 61.130 55.036 1.00 29.88 ? 471 TYR A CE1 1 ATOM 3419 C CE2 . TYR A 1 430 ? 24.498 63.313 55.338 1.00 32.08 ? 471 TYR A CE2 1 ATOM 3420 C CZ . TYR A 1 430 ? 24.012 62.322 54.515 1.00 34.03 ? 471 TYR A CZ 1 ATOM 3421 O OH . TYR A 1 430 ? 24.015 62.567 53.181 1.00 32.92 ? 471 TYR A OH 1 ATOM 3422 N N . SER A 1 431 ? 23.271 61.426 61.690 1.00 29.85 ? 472 SER A N 1 ATOM 3423 C CA . SER A 1 431 ? 23.716 61.470 63.108 1.00 29.48 ? 472 SER A CA 1 ATOM 3424 C C . SER A 1 431 ? 23.355 60.219 63.857 1.00 29.76 ? 472 SER A C 1 ATOM 3425 O O . SER A 1 431 ? 24.193 59.690 64.610 1.00 30.95 ? 472 SER A O 1 ATOM 3426 C CB . SER A 1 431 ? 23.109 62.702 63.790 1.00 32.24 ? 472 SER A CB 1 ATOM 3427 O OG A SER A 1 431 ? 23.693 63.872 63.193 0.50 33.25 ? 472 SER A OG 1 ATOM 3428 O OG B SER A 1 431 ? 23.601 62.814 65.118 0.50 28.67 ? 472 SER A OG 1 ATOM 3429 N N . LEU A 1 432 ? 22.145 59.709 63.609 1.00 29.11 ? 473 LEU A N 1 ATOM 3430 C CA . LEU A 1 432 ? 21.680 58.440 64.179 1.00 29.29 ? 473 LEU A CA 1 ATOM 3431 C C . LEU A 1 432 ? 22.666 57.310 63.800 1.00 29.40 ? 473 LEU A C 1 ATOM 3432 O O . LEU A 1 432 ? 23.107 56.516 64.655 1.00 28.57 ? 473 LEU A O 1 ATOM 3433 C CB . LEU A 1 432 ? 20.266 58.120 63.654 1.00 28.09 ? 473 LEU A CB 1 ATOM 3434 C CG . LEU A 1 432 ? 19.764 56.680 63.861 1.00 29.64 ? 473 LEU A CG 1 ATOM 3435 C CD1 . LEU A 1 432 ? 19.747 56.237 65.334 1.00 34.93 ? 473 LEU A CD1 1 ATOM 3436 C CD2 . LEU A 1 432 ? 18.431 56.480 63.237 1.00 33.78 ? 473 LEU A CD2 1 ATOM 3437 N N . VAL A 1 433 ? 22.990 57.200 62.510 1.00 29.14 ? 474 VAL A N 1 ATOM 3438 C CA . VAL A 1 433 ? 23.913 56.118 62.057 1.00 28.85 ? 474 VAL A CA 1 ATOM 3439 C C . VAL A 1 433 ? 25.294 56.292 62.699 1.00 29.68 ? 474 VAL A C 1 ATOM 3440 O O . VAL A 1 433 ? 25.902 55.312 63.184 1.00 30.54 ? 474 VAL A O 1 ATOM 3441 C CB . VAL A 1 433 ? 24.072 56.146 60.497 1.00 28.08 ? 474 VAL A CB 1 ATOM 3442 C CG1 . VAL A 1 433 ? 25.187 55.172 60.028 1.00 31.34 ? 474 VAL A CG1 1 ATOM 3443 C CG2 . VAL A 1 433 ? 22.737 55.789 59.832 1.00 30.24 ? 474 VAL A CG2 1 ATOM 3444 N N . HIS A 1 434 ? 25.836 57.508 62.672 1.00 29.39 ? 475 HIS A N 1 ATOM 3445 C CA . HIS A 1 434 ? 27.144 57.721 63.344 1.00 32.00 ? 475 HIS A CA 1 ATOM 3446 C C . HIS A 1 434 ? 27.092 57.285 64.800 1.00 32.84 ? 475 HIS A C 1 ATOM 3447 O O . HIS A 1 434 ? 27.991 56.573 65.258 1.00 32.98 ? 475 HIS A O 1 ATOM 3448 C CB . HIS A 1 434 ? 27.636 59.167 63.314 1.00 32.72 ? 475 HIS A CB 1 ATOM 3449 C CG . HIS A 1 434 ? 27.928 59.676 61.942 1.00 38.01 ? 475 HIS A CG 1 ATOM 3450 N ND1 . HIS A 1 434 ? 27.955 61.022 61.650 1.00 47.25 ? 475 HIS A ND1 1 ATOM 3451 C CD2 . HIS A 1 434 ? 28.144 59.033 60.772 1.00 40.06 ? 475 HIS A CD2 1 ATOM 3452 C CE1 . HIS A 1 434 ? 28.179 61.185 60.354 1.00 47.07 ? 475 HIS A CE1 1 ATOM 3453 N NE2 . HIS A 1 434 ? 28.311 59.996 59.803 1.00 42.43 ? 475 HIS A NE2 1 ATOM 3454 N N . ASN A 1 435 ? 26.057 57.723 65.527 1.00 32.49 ? 476 ASN A N 1 ATOM 3455 C CA . ASN A 1 435 ? 25.986 57.417 66.972 1.00 33.27 ? 476 ASN A CA 1 ATOM 3456 C C . ASN A 1 435 ? 25.847 55.941 67.260 1.00 32.52 ? 476 ASN A C 1 ATOM 3457 O O . ASN A 1 435 ? 26.532 55.403 68.160 1.00 33.33 ? 476 ASN A O 1 ATOM 3458 C CB . ASN A 1 435 ? 24.840 58.173 67.664 1.00 33.52 ? 476 ASN A CB 1 ATOM 3459 C CG . ASN A 1 435 ? 25.127 59.659 67.820 1.00 37.95 ? 476 ASN A CG 1 ATOM 3460 O OD1 . ASN A 1 435 ? 26.162 60.138 67.377 1.00 35.58 ? 476 ASN A OD1 1 ATOM 3461 N ND2 . ASN A 1 435 ? 24.203 60.387 68.437 1.00 39.22 ? 476 ASN A ND2 1 ATOM 3462 N N . LEU A 1 436 ? 24.992 55.276 66.485 1.00 31.92 ? 477 LEU A N 1 ATOM 3463 C CA . LEU A 1 436 ? 24.790 53.843 66.651 1.00 31.74 ? 477 LEU A CA 1 ATOM 3464 C C . LEU A 1 436 ? 26.062 53.045 66.341 1.00 31.22 ? 477 LEU A C 1 ATOM 3465 O O . LEU A 1 436 ? 26.459 52.182 67.137 1.00 31.59 ? 477 LEU A O 1 ATOM 3466 C CB . LEU A 1 436 ? 23.573 53.360 65.806 1.00 30.74 ? 477 LEU A CB 1 ATOM 3467 C CG . LEU A 1 436 ? 23.346 51.854 65.820 1.00 32.62 ? 477 LEU A CG 1 ATOM 3468 C CD1 . LEU A 1 436 ? 23.071 51.298 67.231 1.00 34.16 ? 477 LEU A CD1 1 ATOM 3469 C CD2 . LEU A 1 436 ? 22.247 51.431 64.814 1.00 31.21 ? 477 LEU A CD2 1 ATOM 3470 N N . THR A 1 437 ? 26.712 53.315 65.216 1.00 31.34 ? 478 THR A N 1 ATOM 3471 C CA . THR A 1 437 ? 27.946 52.547 64.861 1.00 32.09 ? 478 THR A CA 1 ATOM 3472 C C . THR A 1 437 ? 29.089 52.773 65.862 1.00 33.83 ? 478 THR A C 1 ATOM 3473 O O . THR A 1 437 ? 29.955 51.899 66.047 1.00 33.14 ? 478 THR A O 1 ATOM 3474 C CB . THR A 1 437 ? 28.403 52.800 63.400 1.00 31.58 ? 478 THR A CB 1 ATOM 3475 O OG1 . THR A 1 437 ? 28.706 54.194 63.195 1.00 30.99 ? 478 THR A OG1 1 ATOM 3476 C CG2 . THR A 1 437 ? 27.246 52.333 62.383 1.00 29.27 ? 478 THR A CG2 1 ATOM 3477 N N . LYS A 1 438 ? 29.115 53.926 66.527 1.00 35.38 ? 479 LYS A N 1 ATOM 3478 C CA . LYS A 1 438 ? 30.121 54.134 67.599 1.00 37.08 ? 479 LYS A CA 1 ATOM 3479 C C . LYS A 1 438 ? 29.863 53.246 68.813 1.00 38.22 ? 479 LYS A C 1 ATOM 3480 O O . LYS A 1 438 ? 30.766 53.012 69.604 1.00 39.48 ? 479 LYS A O 1 ATOM 3481 C CB . LYS A 1 438 ? 30.187 55.611 68.058 1.00 37.61 ? 479 LYS A CB 1 ATOM 3482 C CG . LYS A 1 438 ? 30.720 56.551 66.991 1.00 38.10 ? 479 LYS A CG 1 ATOM 3483 C CD . LYS A 1 438 ? 30.888 58.001 67.470 1.00 42.75 ? 479 LYS A CD 1 ATOM 3484 C CE . LYS A 1 438 ? 31.083 58.872 66.234 1.00 42.24 ? 479 LYS A CE 1 ATOM 3485 N NZ . LYS A 1 438 ? 31.005 60.342 66.480 1.00 45.50 ? 479 LYS A NZ 1 ATOM 3486 N N . GLU A 1 439 ? 28.644 52.754 68.981 1.00 38.03 ? 480 GLU A N 1 ATOM 3487 C CA . GLU A 1 439 ? 28.333 51.890 70.134 1.00 40.45 ? 480 GLU A CA 1 ATOM 3488 C C . GLU A 1 439 ? 28.363 50.414 69.794 1.00 39.78 ? 480 GLU A C 1 ATOM 3489 O O . GLU A 1 439 ? 28.178 49.601 70.682 1.00 40.76 ? 480 GLU A O 1 ATOM 3490 C CB . GLU A 1 439 ? 26.937 52.199 70.691 1.00 41.88 ? 480 GLU A CB 1 ATOM 3491 C CG . GLU A 1 439 ? 26.740 53.633 71.208 1.00 47.73 ? 480 GLU A CG 1 ATOM 3492 C CD . GLU A 1 439 ? 27.720 54.041 72.298 1.00 57.51 ? 480 GLU A CD 1 ATOM 3493 O OE1 . GLU A 1 439 ? 28.000 55.262 72.395 1.00 64.23 ? 480 GLU A OE1 1 ATOM 3494 O OE2 . GLU A 1 439 ? 28.207 53.171 73.067 1.00 60.44 ? 480 GLU A OE2 1 ATOM 3495 N N . LEU A 1 440 ? 28.531 50.072 68.509 1.00 37.49 ? 481 LEU A N 1 ATOM 3496 C CA . LEU A 1 440 ? 28.609 48.683 68.059 1.00 35.51 ? 481 LEU A CA 1 ATOM 3497 C C . LEU A 1 440 ? 30.059 48.188 67.891 1.00 36.86 ? 481 LEU A C 1 ATOM 3498 O O . LEU A 1 440 ? 30.945 48.950 67.507 1.00 37.47 ? 481 LEU A O 1 ATOM 3499 C CB . LEU A 1 440 ? 27.867 48.497 66.716 1.00 33.31 ? 481 LEU A CB 1 ATOM 3500 C CG . LEU A 1 440 ? 26.370 48.836 66.730 1.00 33.07 ? 481 LEU A CG 1 ATOM 3501 C CD1 . LEU A 1 440 ? 25.763 48.644 65.342 1.00 28.90 ? 481 LEU A CD1 1 ATOM 3502 C CD2 . LEU A 1 440 ? 25.651 47.957 67.767 1.00 32.04 ? 481 LEU A CD2 1 ATOM 3503 N N . LYS A 1 441 ? 30.267 46.902 68.127 1.00 37.14 ? 482 LYS A N 1 ATOM 3504 C CA A LYS A 1 441 ? 31.618 46.349 68.029 0.50 39.08 ? 482 LYS A CA 1 ATOM 3505 C CA B LYS A 1 441 ? 31.602 46.276 68.032 0.50 39.16 ? 482 LYS A CA 1 ATOM 3506 C C . LYS A 1 441 ? 31.944 46.055 66.561 1.00 38.61 ? 482 LYS A C 1 ATOM 3507 O O . LYS A 1 441 ? 31.073 45.631 65.781 1.00 38.47 ? 482 LYS A O 1 ATOM 3508 C CB A LYS A 1 441 ? 31.784 45.127 68.936 0.50 40.00 ? 482 LYS A CB 1 ATOM 3509 C CB B LYS A 1 441 ? 31.621 44.916 68.734 0.50 39.76 ? 482 LYS A CB 1 ATOM 3510 C CG A LYS A 1 441 ? 31.633 45.476 70.436 0.50 42.69 ? 482 LYS A CG 1 ATOM 3511 C CG B LYS A 1 441 ? 31.246 44.913 70.210 0.50 43.29 ? 482 LYS A CG 1 ATOM 3512 C CD A LYS A 1 441 ? 32.443 44.549 71.324 0.50 47.34 ? 482 LYS A CD 1 ATOM 3513 C CD B LYS A 1 441 ? 31.063 43.477 70.698 0.50 46.49 ? 482 LYS A CD 1 ATOM 3514 C CE A LYS A 1 441 ? 31.673 43.302 71.767 0.50 48.73 ? 482 LYS A CE 1 ATOM 3515 C CE B LYS A 1 441 ? 32.292 42.623 70.390 0.50 48.86 ? 482 LYS A CE 1 ATOM 3516 N NZ A LYS A 1 441 ? 30.571 43.618 72.715 0.50 50.03 ? 482 LYS A NZ 1 ATOM 3517 N NZ B LYS A 1 441 ? 32.161 41.181 70.800 0.50 51.82 ? 482 LYS A NZ 1 ATOM 3518 N N . SER A 1 442 ? 33.168 46.359 66.151 1.00 37.93 ? 483 SER A N 1 ATOM 3519 C CA . SER A 1 442 ? 33.531 46.027 64.767 1.00 38.06 ? 483 SER A CA 1 ATOM 3520 C C . SER A 1 442 ? 33.724 44.519 64.654 1.00 37.66 ? 483 SER A C 1 ATOM 3521 O O . SER A 1 442 ? 34.409 43.927 65.505 1.00 39.78 ? 483 SER A O 1 ATOM 3522 C CB . SER A 1 442 ? 34.829 46.704 64.314 1.00 38.05 ? 483 SER A CB 1 ATOM 3523 O OG . SER A 1 442 ? 35.178 46.165 63.026 1.00 38.19 ? 483 SER A OG 1 ATOM 3524 N N . PRO A 1 443 ? 33.191 43.885 63.590 1.00 37.54 ? 484 PRO A N 1 ATOM 3525 C CA . PRO A 1 443 ? 33.471 42.450 63.442 1.00 37.43 ? 484 PRO A CA 1 ATOM 3526 C C . PRO A 1 443 ? 34.757 42.171 62.627 1.00 38.51 ? 484 PRO A C 1 ATOM 3527 O O . PRO A 1 443 ? 35.079 41.007 62.389 1.00 38.19 ? 484 PRO A O 1 ATOM 3528 C CB . PRO A 1 443 ? 32.273 41.952 62.631 1.00 35.51 ? 484 PRO A CB 1 ATOM 3529 C CG . PRO A 1 443 ? 31.936 43.132 61.725 1.00 36.44 ? 484 PRO A CG 1 ATOM 3530 C CD . PRO A 1 443 ? 32.262 44.384 62.549 1.00 36.46 ? 484 PRO A CD 1 ATOM 3531 N N . ASP A 1 444 ? 35.443 43.222 62.172 1.00 38.10 ? 485 ASP A N 1 ATOM 3532 C CA . ASP A 1 444 ? 36.516 43.079 61.188 1.00 39.24 ? 485 ASP A CA 1 ATOM 3533 C C . ASP A 1 444 ? 37.795 42.570 61.848 1.00 41.17 ? 485 ASP A C 1 ATOM 3534 O O . ASP A 1 444 ? 38.119 42.965 62.981 1.00 40.41 ? 485 ASP A O 1 ATOM 3535 C CB . ASP A 1 444 ? 36.875 44.435 60.573 1.00 38.66 ? 485 ASP A CB 1 ATOM 3536 C CG . ASP A 1 444 ? 35.707 45.070 59.783 1.00 40.08 ? 485 ASP A CG 1 ATOM 3537 O OD1 . ASP A 1 444 ? 34.600 44.481 59.725 1.00 41.98 ? 485 ASP A OD1 1 ATOM 3538 O OD2 . ASP A 1 444 ? 35.904 46.163 59.217 1.00 39.91 ? 485 ASP A OD2 1 ATOM 3539 N N . GLU A 1 445 ? 38.535 41.756 61.109 1.00 42.32 ? 486 GLU A N 1 ATOM 3540 C CA A GLU A 1 445 ? 39.842 41.295 61.550 0.50 45.03 ? 486 GLU A CA 1 ATOM 3541 C CA B GLU A 1 445 ? 39.849 41.304 61.563 0.50 44.86 ? 486 GLU A CA 1 ATOM 3542 C C . GLU A 1 445 ? 40.777 42.512 61.675 1.00 45.36 ? 486 GLU A C 1 ATOM 3543 O O . GLU A 1 445 ? 40.809 43.369 60.792 1.00 45.43 ? 486 GLU A O 1 ATOM 3544 C CB A GLU A 1 445 ? 40.373 40.261 60.548 0.50 45.25 ? 486 GLU A CB 1 ATOM 3545 C CB B GLU A 1 445 ? 40.430 40.269 60.596 0.50 45.07 ? 486 GLU A CB 1 ATOM 3546 C CG A GLU A 1 445 ? 39.951 38.812 60.859 0.50 47.76 ? 486 GLU A CG 1 ATOM 3547 C CG B GLU A 1 445 ? 41.792 39.742 61.035 0.50 47.89 ? 486 GLU A CG 1 ATOM 3548 C CD A GLU A 1 445 ? 38.622 38.397 60.242 0.50 50.36 ? 486 GLU A CD 1 ATOM 3549 C CD B GLU A 1 445 ? 41.968 38.261 60.771 0.50 50.84 ? 486 GLU A CD 1 ATOM 3550 O OE1 A GLU A 1 445 ? 38.127 39.065 59.301 0.50 53.16 ? 486 GLU A OE1 1 ATOM 3551 O OE1 B GLU A 1 445 ? 42.652 37.592 61.578 0.50 52.46 ? 486 GLU A OE1 1 ATOM 3552 O OE2 A GLU A 1 445 ? 38.058 37.381 60.699 0.50 51.66 ? 486 GLU A OE2 1 ATOM 3553 O OE2 B GLU A 1 445 ? 41.411 37.765 59.768 0.50 51.17 ? 486 GLU A OE2 1 ATOM 3554 N N . GLY A 1 446 ? 41.506 42.607 62.781 1.00 47.72 ? 487 GLY A N 1 ATOM 3555 C CA . GLY A 1 446 ? 42.402 43.745 63.007 1.00 48.18 ? 487 GLY A CA 1 ATOM 3556 C C . GLY A 1 446 ? 41.742 44.889 63.759 1.00 49.16 ? 487 GLY A C 1 ATOM 3557 O O . GLY A 1 446 ? 42.423 45.843 64.127 1.00 50.89 ? 487 GLY A O 1 ATOM 3558 N N . PHE A 1 447 ? 40.430 44.812 63.992 1.00 46.85 ? 488 PHE A N 1 ATOM 3559 C CA . PHE A 1 447 ? 39.731 45.863 64.728 1.00 46.46 ? 488 PHE A CA 1 ATOM 3560 C C . PHE A 1 447 ? 39.004 45.297 65.930 1.00 47.02 ? 488 PHE A C 1 ATOM 3561 O O . PHE A 1 447 ? 37.992 45.865 66.360 1.00 46.17 ? 488 PHE A O 1 ATOM 3562 C CB . PHE A 1 447 ? 38.710 46.564 63.809 1.00 44.28 ? 488 PHE A CB 1 ATOM 3563 C CG . PHE A 1 447 ? 39.331 47.365 62.733 1.00 42.88 ? 488 PHE A CG 1 ATOM 3564 C CD1 . PHE A 1 447 ? 39.586 48.713 62.920 1.00 42.46 ? 488 PHE A CD1 1 ATOM 3565 C CD2 . PHE A 1 447 ? 39.681 46.770 61.521 1.00 42.35 ? 488 PHE A CD2 1 ATOM 3566 C CE1 . PHE A 1 447 ? 40.154 49.489 61.911 1.00 45.01 ? 488 PHE A CE1 1 ATOM 3567 C CE2 . PHE A 1 447 ? 40.269 47.531 60.508 1.00 44.82 ? 488 PHE A CE2 1 ATOM 3568 C CZ . PHE A 1 447 ? 40.506 48.893 60.701 1.00 45.60 ? 488 PHE A CZ 1 ATOM 3569 N N . GLU A 1 448 ? 39.470 44.161 66.453 1.00 48.28 ? 489 GLU A N 1 ATOM 3570 C CA . GLU A 1 448 ? 38.815 43.587 67.641 1.00 49.77 ? 489 GLU A CA 1 ATOM 3571 C C . GLU A 1 448 ? 38.890 44.582 68.810 1.00 49.89 ? 489 GLU A C 1 ATOM 3572 O O . GLU A 1 448 ? 39.919 45.217 69.044 1.00 51.14 ? 489 GLU A O 1 ATOM 3573 C CB . GLU A 1 448 ? 39.320 42.176 68.013 1.00 51.32 ? 489 GLU A CB 1 ATOM 3574 C CG . GLU A 1 448 ? 40.725 41.849 67.609 1.00 55.45 ? 489 GLU A CG 1 ATOM 3575 C CD . GLU A 1 448 ? 40.921 41.649 66.099 1.00 55.84 ? 489 GLU A CD 1 ATOM 3576 O OE1 . GLU A 1 448 ? 40.430 40.660 65.506 1.00 55.50 ? 489 GLU A OE1 1 ATOM 3577 O OE2 . GLU A 1 448 ? 41.625 42.490 65.513 1.00 57.96 ? 489 GLU A OE2 1 ATOM 3578 N N . GLY A 1 449 ? 37.772 44.775 69.495 1.00 48.90 ? 490 GLY A N 1 ATOM 3579 C CA . GLY A 1 449 ? 37.738 45.778 70.563 1.00 49.21 ? 490 GLY A CA 1 ATOM 3580 C C . GLY A 1 449 ? 37.561 47.207 70.072 1.00 48.41 ? 490 GLY A C 1 ATOM 3581 O O . GLY A 1 449 ? 37.513 48.149 70.877 1.00 49.95 ? 490 GLY A O 1 ATOM 3582 N N . LYS A 1 450 ? 37.475 47.397 68.762 1.00 45.49 ? 491 LYS A N 1 ATOM 3583 C CA . LYS A 1 450 ? 37.221 48.720 68.244 1.00 44.59 ? 491 LYS A CA 1 ATOM 3584 C C . LYS A 1 450 ? 35.767 48.788 67.793 1.00 41.83 ? 491 LYS A C 1 ATOM 3585 O O . LYS A 1 450 ? 35.119 47.759 67.593 1.00 41.73 ? 491 LYS A O 1 ATOM 3586 C CB . LYS A 1 450 ? 38.173 49.088 67.102 1.00 45.10 ? 491 LYS A CB 1 ATOM 3587 C CG . LYS A 1 450 ? 39.669 48.940 67.478 1.00 48.69 ? 491 LYS A CG 1 ATOM 3588 C CD . LYS A 1 450 ? 40.030 49.791 68.710 1.00 54.92 ? 491 LYS A CD 1 ATOM 3589 C CE . LYS A 1 450 ? 41.442 49.479 69.230 1.00 63.72 ? 491 LYS A CE 1 ATOM 3590 N NZ . LYS A 1 450 ? 42.455 49.661 68.154 1.00 66.94 ? 491 LYS A NZ 1 ATOM 3591 N N . SER A 1 451 ? 35.276 50.000 67.646 1.00 40.19 ? 492 SER A N 1 ATOM 3592 C CA . SER A 1 451 ? 33.890 50.223 67.246 1.00 38.69 ? 492 SER A CA 1 ATOM 3593 C C . SER A 1 451 ? 33.705 49.997 65.747 1.00 37.12 ? 492 SER A C 1 ATOM 3594 O O . SER A 1 451 ? 34.651 50.079 64.969 1.00 37.60 ? 492 SER A O 1 ATOM 3595 C CB . SER A 1 451 ? 33.473 51.634 67.622 1.00 38.52 ? 492 SER A CB 1 ATOM 3596 O OG . SER A 1 451 ? 33.996 52.606 66.728 1.00 38.97 ? 492 SER A OG 1 ATOM 3597 N N . LEU A 1 452 ? 32.468 49.723 65.345 1.00 35.26 ? 493 LEU A N 1 ATOM 3598 C CA . LEU A 1 452 ? 32.151 49.620 63.931 1.00 34.26 ? 493 LEU A CA 1 ATOM 3599 C C . LEU A 1 452 ? 32.408 50.976 63.258 1.00 33.89 ? 493 LEU A C 1 ATOM 3600 O O . LEU A 1 452 ? 32.870 51.010 62.123 1.00 33.15 ? 493 LEU A O 1 ATOM 3601 C CB . LEU A 1 452 ? 30.681 49.202 63.756 1.00 32.23 ? 493 LEU A CB 1 ATOM 3602 C CG . LEU A 1 452 ? 30.102 49.131 62.346 1.00 32.18 ? 493 LEU A CG 1 ATOM 3603 C CD1 . LEU A 1 452 ? 30.929 48.083 61.501 1.00 32.67 ? 493 LEU A CD1 1 ATOM 3604 C CD2 . LEU A 1 452 ? 28.649 48.733 62.461 1.00 28.77 ? 493 LEU A CD2 1 ATOM 3605 N N . TYR A 1 453 ? 32.106 52.081 63.954 1.00 34.54 ? 494 TYR A N 1 ATOM 3606 C CA . TYR A 1 453 ? 32.365 53.408 63.405 1.00 35.32 ? 494 TYR A CA 1 ATOM 3607 C C . TYR A 1 453 ? 33.848 53.553 63.027 1.00 35.72 ? 494 TYR A C 1 ATOM 3608 O O . TYR A 1 453 ? 34.170 54.099 61.971 1.00 35.79 ? 494 TYR A O 1 ATOM 3609 C CB . TYR A 1 453 ? 31.953 54.532 64.378 1.00 36.33 ? 494 TYR A CB 1 ATOM 3610 C CG . TYR A 1 453 ? 32.169 55.920 63.825 1.00 36.86 ? 494 TYR A CG 1 ATOM 3611 C CD1 . TYR A 1 453 ? 31.144 56.584 63.169 1.00 34.76 ? 494 TYR A CD1 1 ATOM 3612 C CD2 . TYR A 1 453 ? 33.402 56.585 63.996 1.00 40.02 ? 494 TYR A CD2 1 ATOM 3613 C CE1 . TYR A 1 453 ? 31.332 57.881 62.662 1.00 38.16 ? 494 TYR A CE1 1 ATOM 3614 C CE2 . TYR A 1 453 ? 33.595 57.882 63.491 1.00 39.93 ? 494 TYR A CE2 1 ATOM 3615 C CZ . TYR A 1 453 ? 32.558 58.504 62.821 1.00 37.99 ? 494 TYR A CZ 1 ATOM 3616 O OH . TYR A 1 453 ? 32.704 59.764 62.295 1.00 40.19 ? 494 TYR A OH 1 ATOM 3617 N N . GLU A 1 454 ? 34.735 53.089 63.888 1.00 35.90 ? 495 GLU A N 1 ATOM 3618 C CA . GLU A 1 454 ? 36.182 53.220 63.616 1.00 39.56 ? 495 GLU A CA 1 ATOM 3619 C C . GLU A 1 454 ? 36.647 52.393 62.388 1.00 38.49 ? 495 GLU A C 1 ATOM 3620 O O . GLU A 1 454 ? 37.318 52.929 61.505 1.00 39.30 ? 495 GLU A O 1 ATOM 3621 C CB . GLU A 1 454 ? 37.021 52.868 64.862 1.00 40.61 ? 495 GLU A CB 1 ATOM 3622 C CG . GLU A 1 454 ? 38.529 52.794 64.553 1.00 46.88 ? 495 GLU A CG 1 ATOM 3623 C CD . GLU A 1 454 ? 39.394 52.781 65.786 1.00 53.36 ? 495 GLU A CD 1 ATOM 3624 O OE1 . GLU A 1 454 ? 38.997 53.415 66.795 1.00 56.26 ? 495 GLU A OE1 1 ATOM 3625 O OE2 . GLU A 1 454 ? 40.472 52.148 65.726 1.00 55.19 ? 495 GLU A OE2 1 ATOM 3626 N N . SER A 1 455 ? 36.234 51.131 62.304 1.00 37.82 ? 496 SER A N 1 ATOM 3627 C CA . SER A 1 455 ? 36.607 50.297 61.148 1.00 38.05 ? 496 SER A CA 1 ATOM 3628 C C . SER A 1 455 ? 36.012 50.825 59.837 1.00 37.35 ? 496 SER A C 1 ATOM 3629 O O . SER A 1 455 ? 36.702 50.937 58.824 1.00 37.86 ? 496 SER A O 1 ATOM 3630 C CB . SER A 1 455 ? 36.272 48.812 61.374 1.00 37.90 ? 496 SER A CB 1 ATOM 3631 O OG . SER A 1 455 ? 34.895 48.564 61.512 1.00 38.20 ? 496 SER A OG 1 ATOM 3632 N N . TRP A 1 456 ? 34.734 51.177 59.873 1.00 35.58 ? 497 TRP A N 1 ATOM 3633 C CA . TRP A 1 456 ? 34.030 51.718 58.731 1.00 35.00 ? 497 TRP A CA 1 ATOM 3634 C C . TRP A 1 456 ? 34.656 53.037 58.248 1.00 36.46 ? 497 TRP A C 1 ATOM 3635 O O . TRP A 1 456 ? 34.873 53.237 57.041 1.00 35.09 ? 497 TRP A O 1 ATOM 3636 C CB . TRP A 1 456 ? 32.547 51.880 59.110 1.00 33.17 ? 497 TRP A CB 1 ATOM 3637 C CG . TRP A 1 456 ? 31.624 52.523 58.080 1.00 32.36 ? 497 TRP A CG 1 ATOM 3638 C CD1 . TRP A 1 456 ? 31.692 52.419 56.707 1.00 30.44 ? 497 TRP A CD1 1 ATOM 3639 C CD2 . TRP A 1 456 ? 30.483 53.304 58.364 1.00 31.78 ? 497 TRP A CD2 1 ATOM 3640 N NE1 . TRP A 1 456 ? 30.687 53.150 56.125 1.00 28.41 ? 497 TRP A NE1 1 ATOM 3641 C CE2 . TRP A 1 456 ? 29.913 53.694 57.122 1.00 33.77 ? 497 TRP A CE2 1 ATOM 3642 C CE3 . TRP A 1 456 ? 29.886 53.746 59.561 1.00 33.19 ? 497 TRP A CE3 1 ATOM 3643 C CZ2 . TRP A 1 456 ? 28.776 54.500 57.040 1.00 31.65 ? 497 TRP A CZ2 1 ATOM 3644 C CZ3 . TRP A 1 456 ? 28.741 54.534 59.480 1.00 34.29 ? 497 TRP A CZ3 1 ATOM 3645 C CH2 . TRP A 1 456 ? 28.204 54.912 58.222 1.00 34.05 ? 497 TRP A CH2 1 ATOM 3646 N N . THR A 1 457 ? 34.949 53.940 59.187 1.00 37.17 ? 498 THR A N 1 ATOM 3647 C CA . THR A 1 457 ? 35.549 55.202 58.821 1.00 38.41 ? 498 THR A CA 1 ATOM 3648 C C . THR A 1 457 ? 36.966 54.993 58.254 1.00 40.20 ? 498 THR A C 1 ATOM 3649 O O . THR A 1 457 ? 37.328 55.651 57.279 1.00 40.23 ? 498 THR A O 1 ATOM 3650 C CB . THR A 1 457 ? 35.567 56.179 60.028 1.00 39.67 ? 498 THR A CB 1 ATOM 3651 O OG1 A THR A 1 457 ? 34.208 56.512 60.363 1.00 38.07 ? 498 THR A OG1 1 ATOM 3652 C CG2 A THR A 1 457 ? 36.306 57.483 59.669 1.00 41.75 ? 498 THR A CG2 1 ATOM 3653 N N . LYS A 1 458 ? 37.751 54.093 58.847 1.00 41.25 ? 499 LYS A N 1 ATOM 3654 C CA . LYS A 1 458 ? 39.064 53.782 58.275 1.00 44.20 ? 499 LYS A CA 1 ATOM 3655 C C . LYS A 1 458 ? 38.952 53.236 56.843 1.00 43.53 ? 499 LYS A C 1 ATOM 3656 O O . LYS A 1 458 ? 39.671 53.681 55.951 1.00 43.83 ? 499 LYS A O 1 ATOM 3657 C CB . LYS A 1 458 ? 39.894 52.865 59.182 1.00 45.58 ? 499 LYS A CB 1 ATOM 3658 C CG . LYS A 1 458 ? 41.398 52.732 58.784 1.00 51.24 ? 499 LYS A CG 1 ATOM 3659 C CD . LYS A 1 458 ? 42.113 54.119 58.823 1.00 58.22 ? 499 LYS A CD 1 ATOM 3660 C CE . LYS A 1 458 ? 43.637 54.008 59.014 1.00 60.93 ? 499 LYS A CE 1 ATOM 3661 N NZ . LYS A 1 458 ? 44.208 53.021 58.053 1.00 63.06 ? 499 LYS A NZ 1 ATOM 3662 N N . LYS A 1 459 ? 38.016 52.323 56.604 1.00 42.28 ? 500 LYS A N 1 ATOM 3663 C CA . LYS A 1 459 ? 37.959 51.618 55.317 1.00 41.92 ? 500 LYS A CA 1 ATOM 3664 C C . LYS A 1 459 ? 37.209 52.352 54.233 1.00 41.88 ? 500 LYS A C 1 ATOM 3665 O O . LYS A 1 459 ? 37.431 52.097 53.045 1.00 41.73 ? 500 LYS A O 1 ATOM 3666 C CB . LYS A 1 459 ? 37.361 50.227 55.510 1.00 40.63 ? 500 LYS A CB 1 ATOM 3667 C CG . LYS A 1 459 ? 38.301 49.298 56.343 1.00 42.29 ? 500 LYS A CG 1 ATOM 3668 C CD . LYS A 1 459 ? 37.606 47.952 56.579 1.00 41.64 ? 500 LYS A CD 1 ATOM 3669 C CE . LYS A 1 459 ? 38.538 46.915 57.134 1.00 43.48 ? 500 LYS A CE 1 ATOM 3670 N NZ . LYS A 1 459 ? 37.812 45.616 57.234 1.00 44.04 ? 500 LYS A NZ 1 ATOM 3671 N N . SER A 1 460 ? 36.280 53.220 54.629 1.00 39.73 ? 501 SER A N 1 ATOM 3672 C CA . SER A 1 460 ? 35.447 53.921 53.682 1.00 40.09 ? 501 SER A CA 1 ATOM 3673 C C . SER A 1 460 ? 35.329 55.395 54.102 1.00 41.33 ? 501 SER A C 1 ATOM 3674 O O . SER A 1 460 ? 34.266 55.835 54.544 1.00 40.00 ? 501 SER A O 1 ATOM 3675 C CB . SER A 1 460 ? 34.075 53.279 53.660 1.00 38.29 ? 501 SER A CB 1 ATOM 3676 O OG . SER A 1 460 ? 33.362 53.713 52.529 1.00 40.08 ? 501 SER A OG 1 ATOM 3677 N N . PRO A 1 461 ? 36.445 56.157 54.000 1.00 43.23 ? 502 PRO A N 1 ATOM 3678 C CA . PRO A 1 461 ? 36.412 57.557 54.445 1.00 44.17 ? 502 PRO A CA 1 ATOM 3679 C C . PRO A 1 461 ? 35.481 58.417 53.596 1.00 45.36 ? 502 PRO A C 1 ATOM 3680 O O . PRO A 1 461 ? 35.354 58.234 52.382 1.00 44.18 ? 502 PRO A O 1 ATOM 3681 C CB . PRO A 1 461 ? 37.886 58.022 54.323 1.00 46.05 ? 502 PRO A CB 1 ATOM 3682 C CG . PRO A 1 461 ? 38.559 57.028 53.438 1.00 45.52 ? 502 PRO A CG 1 ATOM 3683 C CD . PRO A 1 461 ? 37.748 55.760 53.427 1.00 43.40 ? 502 PRO A CD 1 ATOM 3684 N N . SER A 1 462 ? 34.808 59.352 54.247 1.00 47.24 ? 503 SER A N 1 ATOM 3685 C CA . SER A 1 462 ? 34.060 60.362 53.532 1.00 50.19 ? 503 SER A CA 1 ATOM 3686 C C . SER A 1 462 ? 35.006 61.144 52.615 1.00 52.66 ? 503 SER A C 1 ATOM 3687 O O . SER A 1 462 ? 36.137 61.441 53.015 1.00 53.10 ? 503 SER A O 1 ATOM 3688 C CB . SER A 1 462 ? 33.431 61.319 54.543 1.00 50.11 ? 503 SER A CB 1 ATOM 3689 O OG . SER A 1 462 ? 33.068 62.503 53.896 1.00 51.98 ? 503 SER A OG 1 ATOM 3690 N N . PRO A 1 463 ? 34.559 61.465 51.388 1.00 54.61 ? 504 PRO A N 1 ATOM 3691 C CA . PRO A 1 463 ? 35.365 62.336 50.494 1.00 57.86 ? 504 PRO A CA 1 ATOM 3692 C C . PRO A 1 463 ? 35.547 63.775 51.034 1.00 60.48 ? 504 PRO A C 1 ATOM 3693 O O . PRO A 1 463 ? 36.585 64.399 50.804 1.00 61.96 ? 504 PRO A O 1 ATOM 3694 C CB . PRO A 1 463 ? 34.556 62.373 49.191 1.00 56.59 ? 504 PRO A CB 1 ATOM 3695 C CG . PRO A 1 463 ? 33.511 61.304 49.320 1.00 55.87 ? 504 PRO A CG 1 ATOM 3696 C CD . PRO A 1 463 ? 33.289 61.043 50.771 1.00 53.79 ? 504 PRO A CD 1 ATOM 3697 N N . GLU A 1 464 ? 34.551 64.281 51.763 1.00 62.25 ? 505 GLU A N 1 ATOM 3698 C CA . GLU A 1 464 ? 34.591 65.671 52.267 1.00 64.70 ? 505 GLU A CA 1 ATOM 3699 C C . GLU A 1 464 ? 35.089 65.878 53.707 1.00 65.44 ? 505 GLU A C 1 ATOM 3700 O O . GLU A 1 464 ? 35.629 66.943 54.017 1.00 66.65 ? 505 GLU A O 1 ATOM 3701 C CB . GLU A 1 464 ? 33.265 66.440 52.029 1.00 64.44 ? 505 GLU A CB 1 ATOM 3702 C CG . GLU A 1 464 ? 31.956 65.628 52.063 1.00 67.34 ? 505 GLU A CG 1 ATOM 3703 C CD . GLU A 1 464 ? 31.487 65.159 50.675 1.00 71.78 ? 505 GLU A CD 1 ATOM 3704 O OE1 . GLU A 1 464 ? 30.293 64.785 50.526 1.00 72.45 ? 505 GLU A OE1 1 ATOM 3705 O OE2 . GLU A 1 464 ? 32.310 65.151 49.727 1.00 74.31 ? 505 GLU A OE2 1 ATOM 3706 N N . PHE A 1 465 ? 34.927 64.885 54.580 1.00 65.06 ? 506 PHE A N 1 ATOM 3707 C CA . PHE A 1 465 ? 35.190 65.122 55.997 1.00 65.50 ? 506 PHE A CA 1 ATOM 3708 C C . PHE A 1 465 ? 36.151 64.137 56.617 1.00 65.44 ? 506 PHE A C 1 ATOM 3709 O O . PHE A 1 465 ? 35.937 62.922 56.606 1.00 64.77 ? 506 PHE A O 1 ATOM 3710 C CB . PHE A 1 465 ? 33.882 65.203 56.799 1.00 65.74 ? 506 PHE A CB 1 ATOM 3711 C CG . PHE A 1 465 ? 32.924 66.278 56.314 1.00 66.74 ? 506 PHE A CG 1 ATOM 3712 C CD1 . PHE A 1 465 ? 31.743 65.932 55.645 1.00 67.17 ? 506 PHE A CD1 1 ATOM 3713 C CD2 . PHE A 1 465 ? 33.200 67.639 56.536 1.00 69.43 ? 506 PHE A CD2 1 ATOM 3714 C CE1 . PHE A 1 465 ? 30.837 66.925 55.199 1.00 66.46 ? 506 PHE A CE1 1 ATOM 3715 C CE2 . PHE A 1 465 ? 32.315 68.637 56.091 1.00 70.08 ? 506 PHE A CE2 1 ATOM 3716 C CZ . PHE A 1 465 ? 31.124 68.273 55.419 1.00 69.10 ? 506 PHE A CZ 1 ATOM 3717 N N . SER A 1 466 ? 37.233 64.670 57.156 1.00 65.52 ? 507 SER A N 1 ATOM 3718 C CA . SER A 1 466 ? 38.250 63.821 57.754 1.00 64.74 ? 507 SER A CA 1 ATOM 3719 C C . SER A 1 466 ? 37.657 63.247 59.046 1.00 62.68 ? 507 SER A C 1 ATOM 3720 O O . SER A 1 466 ? 37.031 63.986 59.827 1.00 62.85 ? 507 SER A O 1 ATOM 3721 C CB . SER A 1 466 ? 39.534 64.622 58.021 1.00 66.59 ? 507 SER A CB 1 ATOM 3722 O OG . SER A 1 466 ? 40.626 63.748 58.302 1.00 69.28 ? 507 SER A OG 1 ATOM 3723 N N . GLY A 1 467 ? 37.802 61.937 59.241 1.00 59.42 ? 508 GLY A N 1 ATOM 3724 C CA . GLY A 1 467 ? 37.341 61.294 60.475 1.00 56.25 ? 508 GLY A CA 1 ATOM 3725 C C . GLY A 1 467 ? 35.864 60.895 60.489 1.00 52.01 ? 508 GLY A C 1 ATOM 3726 O O . GLY A 1 467 ? 35.312 60.555 61.553 1.00 50.70 ? 508 GLY A O 1 ATOM 3727 N N . MET A 1 468 ? 35.234 60.952 59.319 1.00 49.94 ? 509 MET A N 1 ATOM 3728 C CA . MET A 1 468 ? 33.846 60.485 59.128 1.00 47.47 ? 509 MET A CA 1 ATOM 3729 C C . MET A 1 468 ? 33.730 59.478 57.973 1.00 45.30 ? 509 MET A C 1 ATOM 3730 O O . MET A 1 468 ? 34.521 59.538 57.034 1.00 45.50 ? 509 MET A O 1 ATOM 3731 C CB . MET A 1 468 ? 32.950 61.655 58.795 1.00 47.20 ? 509 MET A CB 1 ATOM 3732 C CG . MET A 1 468 ? 33.223 62.867 59.685 1.00 52.15 ? 509 MET A CG 1 ATOM 3733 S SD . MET A 1 468 ? 31.668 63.522 60.156 1.00 60.95 ? 509 MET A SD 1 ATOM 3734 C CE . MET A 1 468 ? 30.877 63.787 58.572 1.00 60.41 ? 509 MET A CE 1 ATOM 3735 N N . PRO A 1 469 ? 32.716 58.579 58.016 1.00 42.39 ? 510 PRO A N 1 ATOM 3736 C CA . PRO A 1 469 ? 32.588 57.600 56.942 1.00 40.08 ? 510 PRO A CA 1 ATOM 3737 C C . PRO A 1 469 ? 31.743 58.098 55.796 1.00 37.69 ? 510 PRO A C 1 ATOM 3738 O O . PRO A 1 469 ? 30.945 59.053 55.933 1.00 36.99 ? 510 PRO A O 1 ATOM 3739 C CB . PRO A 1 469 ? 31.893 56.425 57.626 1.00 39.42 ? 510 PRO A CB 1 ATOM 3740 C CG . PRO A 1 469 ? 31.020 57.080 58.661 1.00 39.04 ? 510 PRO A CG 1 ATOM 3741 C CD . PRO A 1 469 ? 31.836 58.260 59.156 1.00 42.28 ? 510 PRO A CD 1 ATOM 3742 N N . ARG A 1 470 ? 31.884 57.436 54.661 1.00 36.88 ? 511 ARG A N 1 ATOM 3743 C CA . ARG A 1 470 ? 31.038 57.709 53.533 1.00 35.89 ? 511 ARG A CA 1 ATOM 3744 C C . ARG A 1 470 ? 29.606 57.188 53.782 1.00 35.45 ? 511 ARG A C 1 ATOM 3745 O O . ARG A 1 470 ? 29.394 56.040 54.203 1.00 33.40 ? 511 ARG A O 1 ATOM 3746 C CB . ARG A 1 470 ? 31.640 57.033 52.269 1.00 37.01 ? 511 ARG A CB 1 ATOM 3747 C CG . ARG A 1 470 ? 30.808 57.149 50.974 1.00 38.28 ? 511 ARG A CG 1 ATOM 3748 C CD . ARG A 1 470 ? 31.417 56.245 49.848 1.00 45.55 ? 511 ARG A CD 1 ATOM 3749 N NE . ARG A 1 470 ? 32.745 56.728 49.436 1.00 49.62 ? 511 ARG A NE 1 ATOM 3750 C CZ . ARG A 1 470 ? 32.945 57.713 48.548 1.00 53.42 ? 511 ARG A CZ 1 ATOM 3751 N NH1 . ARG A 1 470 ? 31.908 58.331 47.982 1.00 51.34 ? 511 ARG A NH1 1 ATOM 3752 N NH2 . ARG A 1 470 ? 34.174 58.103 48.234 1.00 52.46 ? 511 ARG A NH2 1 ATOM 3753 N N . ILE A 1 471 ? 28.631 58.041 53.490 1.00 34.75 ? 512 ILE A N 1 ATOM 3754 C CA . ILE A 1 471 ? 27.231 57.627 53.390 1.00 34.58 ? 512 ILE A CA 1 ATOM 3755 C C . ILE A 1 471 ? 26.685 58.163 52.079 1.00 35.14 ? 512 ILE A C 1 ATOM 3756 O O . ILE A 1 471 ? 26.777 59.373 51.820 1.00 35.58 ? 512 ILE A O 1 ATOM 3757 C CB . ILE A 1 471 ? 26.371 58.210 54.594 1.00 34.48 ? 512 ILE A CB 1 ATOM 3758 C CG1 . ILE A 1 471 ? 26.931 57.724 55.939 1.00 34.71 ? 512 ILE A CG1 1 ATOM 3759 C CG2 . ILE A 1 471 ? 24.852 57.842 54.395 1.00 31.98 ? 512 ILE A CG2 1 ATOM 3760 C CD1 . ILE A 1 471 ? 26.157 58.243 57.189 1.00 37.64 ? 512 ILE A CD1 1 ATOM 3761 N N . SER A 1 472 ? 26.090 57.296 51.259 1.00 34.88 ? 513 SER A N 1 ATOM 3762 C CA . SER A 1 472 ? 25.646 57.697 49.931 1.00 35.17 ? 513 SER A CA 1 ATOM 3763 C C . SER A 1 472 ? 24.181 58.118 49.893 1.00 34.65 ? 513 SER A C 1 ATOM 3764 O O . SER A 1 472 ? 23.443 57.895 50.848 1.00 32.37 ? 513 SER A O 1 ATOM 3765 C CB . SER A 1 472 ? 25.937 56.575 48.916 1.00 35.92 ? 513 SER A CB 1 ATOM 3766 O OG . SER A 1 472 ? 27.355 56.425 48.882 1.00 38.60 ? 513 SER A OG 1 ATOM 3767 N N A LYS A 1 473 ? 23.790 58.719 48.775 0.70 34.55 ? 514 LYS A N 1 ATOM 3768 N N B LYS A 1 473 ? 23.764 58.689 48.763 0.30 34.52 ? 514 LYS A N 1 ATOM 3769 C CA A LYS A 1 473 ? 22.411 59.107 48.515 0.70 34.14 ? 514 LYS A CA 1 ATOM 3770 C CA B LYS A 1 473 ? 22.378 59.116 48.566 0.30 34.23 ? 514 LYS A CA 1 ATOM 3771 C C A LYS A 1 473 ? 21.600 57.852 48.230 0.70 34.59 ? 514 LYS A C 1 ATOM 3772 C C B LYS A 1 473 ? 21.512 58.025 47.947 0.30 34.23 ? 514 LYS A C 1 ATOM 3773 O O A LYS A 1 473 ? 22.164 56.841 47.800 0.70 33.89 ? 514 LYS A O 1 ATOM 3774 O O B LYS A 1 473 ? 21.921 57.303 47.031 0.30 33.03 ? 514 LYS A O 1 ATOM 3775 C CB A LYS A 1 473 ? 22.369 60.031 47.285 0.70 33.21 ? 514 LYS A CB 1 ATOM 3776 C CB B LYS A 1 473 ? 22.308 60.363 47.688 0.30 34.37 ? 514 LYS A CB 1 ATOM 3777 C CG A LYS A 1 473 ? 23.283 61.272 47.449 0.70 33.52 ? 514 LYS A CG 1 ATOM 3778 C CG B LYS A 1 473 ? 22.900 60.176 46.318 0.30 34.44 ? 514 LYS A CG 1 ATOM 3779 C CD A LYS A 1 473 ? 23.042 62.327 46.386 0.70 36.26 ? 514 LYS A CD 1 ATOM 3780 C CD B LYS A 1 473 ? 22.717 61.427 45.476 0.30 35.42 ? 514 LYS A CD 1 ATOM 3781 C CE A LYS A 1 473 ? 23.679 61.992 45.057 0.70 36.85 ? 514 LYS A CE 1 ATOM 3782 C CE B LYS A 1 473 ? 23.203 62.681 46.189 0.30 35.85 ? 514 LYS A CE 1 ATOM 3783 N NZ A LYS A 1 473 ? 25.134 62.170 45.171 0.70 34.15 ? 514 LYS A NZ 1 ATOM 3784 N NZ B LYS A 1 473 ? 24.661 62.653 46.434 0.30 35.32 ? 514 LYS A NZ 1 ATOM 3785 N N . LEU A 1 474 ? 20.285 57.941 48.433 1.00 33.65 ? 515 LEU A N 1 ATOM 3786 C CA . LEU A 1 474 ? 19.350 56.921 47.956 1.00 34.45 ? 515 LEU A CA 1 ATOM 3787 C C . LEU A 1 474 ? 18.893 57.211 46.538 1.00 35.70 ? 515 LEU A C 1 ATOM 3788 O O . LEU A 1 474 ? 18.509 58.353 46.189 1.00 37.27 ? 515 LEU A O 1 ATOM 3789 C CB . LEU A 1 474 ? 18.089 56.896 48.836 1.00 32.90 ? 515 LEU A CB 1 ATOM 3790 C CG . LEU A 1 474 ? 18.279 56.439 50.289 1.00 32.13 ? 515 LEU A CG 1 ATOM 3791 C CD1 . LEU A 1 474 ? 17.019 56.850 51.092 1.00 31.54 ? 515 LEU A CD1 1 ATOM 3792 C CD2 . LEU A 1 474 ? 18.492 54.940 50.355 1.00 28.70 ? 515 LEU A CD2 1 ATOM 3793 N N . GLY A 1 475 ? 18.851 56.159 45.726 1.00 37.14 ? 516 GLY A N 1 ATOM 3794 C CA . GLY A 1 475 ? 18.220 56.258 44.413 1.00 35.79 ? 516 GLY A CA 1 ATOM 3795 C C . GLY A 1 475 ? 17.040 55.326 44.333 1.00 35.63 ? 516 GLY A C 1 ATOM 3796 O O . GLY A 1 475 ? 16.006 55.550 44.977 1.00 35.41 ? 516 GLY A O 1 ATOM 3797 N N . SER A 1 476 ? 17.148 54.287 43.491 1.00 34.66 ? 517 SER A N 1 ATOM 3798 C CA . SER A 1 476 ? 16.101 53.278 43.438 1.00 31.82 ? 517 SER A CA 1 ATOM 3799 C C . SER A 1 476 ? 16.725 51.891 43.247 1.00 30.77 ? 517 SER A C 1 ATOM 3800 O O . SER A 1 476 ? 17.878 51.679 43.599 1.00 30.52 ? 517 SER A O 1 ATOM 3801 C CB . SER A 1 476 ? 15.089 53.579 42.349 1.00 33.07 ? 517 SER A CB 1 ATOM 3802 O OG . SER A 1 476 ? 14.004 52.611 42.326 1.00 35.04 ? 517 SER A OG 1 ATOM 3803 N N . GLY A 1 477 ? 15.954 50.967 42.700 1.00 28.27 ? 518 GLY A N 1 ATOM 3804 C CA . GLY A 1 477 ? 16.418 49.590 42.563 1.00 28.48 ? 518 GLY A CA 1 ATOM 3805 C C . GLY A 1 477 ? 16.120 48.764 43.817 1.00 26.55 ? 518 GLY A C 1 ATOM 3806 O O . GLY A 1 477 ? 16.610 47.642 43.951 1.00 26.76 ? 518 GLY A O 1 ATOM 3807 N N . ASN A 1 478 ? 15.350 49.314 44.765 1.00 24.50 ? 519 ASN A N 1 ATOM 3808 C CA . ASN A 1 478 ? 14.919 48.483 45.911 1.00 23.45 ? 519 ASN A CA 1 ATOM 3809 C C . ASN A 1 478 ? 13.673 49.025 46.596 1.00 23.30 ? 519 ASN A C 1 ATOM 3810 O O . ASN A 1 478 ? 13.201 50.097 46.234 1.00 22.13 ? 519 ASN A O 1 ATOM 3811 C CB . ASN A 1 478 ? 16.071 48.202 46.915 1.00 24.61 ? 519 ASN A CB 1 ATOM 3812 C CG . ASN A 1 478 ? 16.064 46.747 47.388 1.00 25.77 ? 519 ASN A CG 1 ATOM 3813 O OD1 . ASN A 1 478 ? 15.079 46.264 47.990 1.00 26.37 ? 519 ASN A OD1 1 ATOM 3814 N ND2 . ASN A 1 478 ? 17.135 46.015 47.043 1.00 24.09 ? 519 ASN A ND2 1 ATOM 3815 N N . ASP A 1 479 ? 13.152 48.287 47.577 1.00 21.96 ? 520 ASP A N 1 ATOM 3816 C CA . ASP A 1 479 ? 11.795 48.515 48.036 1.00 20.79 ? 520 ASP A CA 1 ATOM 3817 C C . ASP A 1 479 ? 11.593 49.790 48.838 1.00 21.52 ? 520 ASP A C 1 ATOM 3818 O O . ASP A 1 479 ? 10.456 50.161 49.096 1.00 22.69 ? 520 ASP A O 1 ATOM 3819 C CB . ASP A 1 479 ? 11.322 47.316 48.887 1.00 21.45 ? 520 ASP A CB 1 ATOM 3820 C CG . ASP A 1 479 ? 10.949 46.084 48.002 1.00 21.86 ? 520 ASP A CG 1 ATOM 3821 O OD1 . ASP A 1 479 ? 10.183 46.277 47.033 1.00 23.88 ? 520 ASP A OD1 1 ATOM 3822 O OD2 . ASP A 1 479 ? 11.415 44.948 48.338 1.00 22.80 ? 520 ASP A OD2 1 ATOM 3823 N N . PHE A 1 480 ? 12.658 50.492 49.200 1.00 22.33 ? 521 PHE A N 1 ATOM 3824 C CA . PHE A 1 480 ? 12.473 51.809 49.820 1.00 22.45 ? 521 PHE A CA 1 ATOM 3825 C C . PHE A 1 480 ? 11.967 52.851 48.811 1.00 22.05 ? 521 PHE A C 1 ATOM 3826 O O . PHE A 1 480 ? 11.578 53.959 49.226 1.00 21.74 ? 521 PHE A O 1 ATOM 3827 C CB . PHE A 1 480 ? 13.814 52.298 50.416 1.00 23.03 ? 521 PHE A CB 1 ATOM 3828 C CG . PHE A 1 480 ? 14.860 52.508 49.369 1.00 23.02 ? 521 PHE A CG 1 ATOM 3829 C CD1 . PHE A 1 480 ? 14.917 53.719 48.634 1.00 25.74 ? 521 PHE A CD1 1 ATOM 3830 C CD2 . PHE A 1 480 ? 15.758 51.485 49.080 1.00 23.36 ? 521 PHE A CD2 1 ATOM 3831 C CE1 . PHE A 1 480 ? 15.864 53.859 47.594 1.00 25.53 ? 521 PHE A CE1 1 ATOM 3832 C CE2 . PHE A 1 480 ? 16.726 51.621 48.029 1.00 25.99 ? 521 PHE A CE2 1 ATOM 3833 C CZ . PHE A 1 480 ? 16.773 52.815 47.305 1.00 26.21 ? 521 PHE A CZ 1 ATOM 3834 N N . GLU A 1 481 ? 12.024 52.565 47.491 1.00 20.83 ? 522 GLU A N 1 ATOM 3835 C CA A GLU A 1 481 ? 11.785 53.608 46.496 0.50 20.95 ? 522 GLU A CA 1 ATOM 3836 C CA B GLU A 1 481 ? 11.733 53.613 46.460 0.50 21.51 ? 522 GLU A CA 1 ATOM 3837 C C . GLU A 1 481 ? 10.411 54.301 46.708 1.00 20.60 ? 522 GLU A C 1 ATOM 3838 O O . GLU A 1 481 ? 10.332 55.545 46.756 1.00 21.15 ? 522 GLU A O 1 ATOM 3839 C CB A GLU A 1 481 ? 11.947 53.027 45.064 0.50 21.09 ? 522 GLU A CB 1 ATOM 3840 C CB B GLU A 1 481 ? 11.686 53.095 44.987 0.50 22.17 ? 522 GLU A CB 1 ATOM 3841 C CG A GLU A 1 481 ? 11.889 54.091 43.961 0.50 22.60 ? 522 GLU A CG 1 ATOM 3842 C CG B GLU A 1 481 ? 11.391 54.292 43.946 0.50 25.38 ? 522 GLU A CG 1 ATOM 3843 C CD A GLU A 1 481 ? 11.400 53.518 42.607 0.50 21.85 ? 522 GLU A CD 1 ATOM 3844 C CD B GLU A 1 481 ? 9.891 54.692 43.751 0.50 30.25 ? 522 GLU A CD 1 ATOM 3845 O OE1 A GLU A 1 481 ? 10.268 53.049 42.497 0.50 28.40 ? 522 GLU A OE1 1 ATOM 3846 O OE1 B GLU A 1 481 ? 9.070 53.774 43.598 0.50 29.49 ? 522 GLU A OE1 1 ATOM 3847 O OE2 A GLU A 1 481 ? 12.144 53.525 41.655 0.50 21.82 ? 522 GLU A OE2 1 ATOM 3848 O OE2 B GLU A 1 481 ? 9.489 55.930 43.721 0.50 33.52 ? 522 GLU A OE2 1 ATOM 3849 N N . VAL A 1 482 ? 9.333 53.517 46.841 1.00 20.15 ? 523 VAL A N 1 ATOM 3850 C CA . VAL A 1 482 ? 8.003 54.167 46.936 1.00 20.40 ? 523 VAL A CA 1 ATOM 3851 C C . VAL A 1 482 ? 7.940 55.039 48.205 1.00 21.31 ? 523 VAL A C 1 ATOM 3852 O O . VAL A 1 482 ? 7.369 56.143 48.193 1.00 20.57 ? 523 VAL A O 1 ATOM 3853 C CB . VAL A 1 482 ? 6.828 53.148 46.887 1.00 21.73 ? 523 VAL A CB 1 ATOM 3854 C CG1 . VAL A 1 482 ? 6.830 52.187 48.166 1.00 20.35 ? 523 VAL A CG1 1 ATOM 3855 C CG2 . VAL A 1 482 ? 5.475 53.886 46.744 1.00 22.85 ? 523 VAL A CG2 1 ATOM 3856 N N . PHE A 1 483 ? 8.501 54.523 49.306 1.00 20.40 ? 524 PHE A N 1 ATOM 3857 C CA . PHE A 1 483 ? 8.410 55.266 50.591 1.00 20.27 ? 524 PHE A CA 1 ATOM 3858 C C . PHE A 1 483 ? 9.162 56.588 50.541 1.00 20.12 ? 524 PHE A C 1 ATOM 3859 O O . PHE A 1 483 ? 8.643 57.609 51.058 1.00 22.08 ? 524 PHE A O 1 ATOM 3860 C CB . PHE A 1 483 ? 8.964 54.386 51.726 1.00 20.68 ? 524 PHE A CB 1 ATOM 3861 C CG . PHE A 1 483 ? 8.163 53.118 51.866 1.00 21.89 ? 524 PHE A CG 1 ATOM 3862 C CD1 . PHE A 1 483 ? 6.945 53.134 52.550 1.00 27.06 ? 524 PHE A CD1 1 ATOM 3863 C CD2 . PHE A 1 483 ? 8.573 51.954 51.247 1.00 20.80 ? 524 PHE A CD2 1 ATOM 3864 C CE1 . PHE A 1 483 ? 6.142 51.964 52.633 1.00 27.67 ? 524 PHE A CE1 1 ATOM 3865 C CE2 . PHE A 1 483 ? 7.771 50.780 51.311 1.00 20.44 ? 524 PHE A CE2 1 ATOM 3866 C CZ . PHE A 1 483 ? 6.591 50.791 52.003 1.00 25.09 ? 524 PHE A CZ 1 ATOM 3867 N N . PHE A 1 484 ? 10.355 56.577 49.965 1.00 19.64 ? 525 PHE A N 1 ATOM 3868 C CA . PHE A 1 484 ? 11.216 57.794 49.967 1.00 20.02 ? 525 PHE A CA 1 ATOM 3869 C C . PHE A 1 484 ? 10.920 58.718 48.779 1.00 21.12 ? 525 PHE A C 1 ATOM 3870 O O . PHE A 1 484 ? 10.600 59.914 48.972 1.00 21.02 ? 525 PHE A O 1 ATOM 3871 C CB . PHE A 1 484 ? 12.692 57.354 49.916 1.00 21.01 ? 525 PHE A CB 1 ATOM 3872 C CG . PHE A 1 484 ? 13.652 58.486 50.093 1.00 21.74 ? 525 PHE A CG 1 ATOM 3873 C CD1 . PHE A 1 484 ? 13.620 59.224 51.285 1.00 23.41 ? 525 PHE A CD1 1 ATOM 3874 C CD2 . PHE A 1 484 ? 14.574 58.816 49.085 1.00 27.97 ? 525 PHE A CD2 1 ATOM 3875 C CE1 . PHE A 1 484 ? 14.538 60.281 51.528 1.00 27.85 ? 525 PHE A CE1 1 ATOM 3876 C CE2 . PHE A 1 484 ? 15.522 59.877 49.310 1.00 25.61 ? 525 PHE A CE2 1 ATOM 3877 C CZ . PHE A 1 484 ? 15.477 60.603 50.570 1.00 26.01 ? 525 PHE A CZ 1 ATOM 3878 N N . GLN A 1 485 ? 10.945 58.162 47.557 1.00 20.02 ? 526 GLN A N 1 ATOM 3879 C CA . GLN A 1 485 ? 10.860 59.009 46.326 1.00 21.13 ? 526 GLN A CA 1 ATOM 3880 C C . GLN A 1 485 ? 9.414 59.431 46.007 1.00 20.94 ? 526 GLN A C 1 ATOM 3881 O O . GLN A 1 485 ? 9.189 60.518 45.470 1.00 21.28 ? 526 GLN A O 1 ATOM 3882 C CB A GLN A 1 485 ? 11.422 58.176 45.118 0.65 20.98 ? 526 GLN A CB 1 ATOM 3883 C CB B GLN A 1 485 ? 11.518 58.344 45.113 0.35 21.75 ? 526 GLN A CB 1 ATOM 3884 C CG A GLN A 1 485 ? 12.864 57.615 45.253 0.65 23.27 ? 526 GLN A CG 1 ATOM 3885 C CG B GLN A 1 485 ? 13.000 58.609 45.031 0.35 25.77 ? 526 GLN A CG 1 ATOM 3886 C CD A GLN A 1 485 ? 13.923 58.742 45.328 0.65 21.55 ? 526 GLN A CD 1 ATOM 3887 C CD B GLN A 1 485 ? 13.781 57.512 45.711 0.35 28.20 ? 526 GLN A CD 1 ATOM 3888 O OE1 A GLN A 1 485 ? 13.568 59.900 45.286 0.65 22.17 ? 526 GLN A OE1 1 ATOM 3889 O OE1 B GLN A 1 485 ? 13.185 56.591 46.299 0.35 30.51 ? 526 GLN A OE1 1 ATOM 3890 N NE2 A GLN A 1 485 ? 15.201 58.379 45.403 0.65 23.28 ? 526 GLN A NE2 1 ATOM 3891 N NE2 B GLN A 1 485 ? 15.115 57.592 45.648 0.35 25.21 ? 526 GLN A NE2 1 ATOM 3892 N N . ARG A 1 486 ? 8.400 58.597 46.342 1.00 20.67 ? 527 ARG A N 1 ATOM 3893 C CA . ARG A 1 486 ? 7.025 59.007 46.082 1.00 21.29 ? 527 ARG A CA 1 ATOM 3894 C C . ARG A 1 486 ? 6.377 59.655 47.278 1.00 21.35 ? 527 ARG A C 1 ATOM 3895 O O . ARG A 1 486 ? 5.762 60.721 47.135 1.00 21.08 ? 527 ARG A O 1 ATOM 3896 C CB . ARG A 1 486 ? 6.130 57.790 45.574 1.00 20.06 ? 527 ARG A CB 1 ATOM 3897 C CG . ARG A 1 486 ? 4.840 58.310 45.020 1.00 21.26 ? 527 ARG A CG 1 ATOM 3898 C CD . ARG A 1 486 ? 3.750 57.161 44.902 1.00 21.07 ? 527 ARG A CD 1 ATOM 3899 N NE . ARG A 1 486 ? 4.137 56.144 43.912 1.00 19.58 ? 527 ARG A NE 1 ATOM 3900 C CZ . ARG A 1 486 ? 3.202 55.338 43.351 1.00 23.33 ? 527 ARG A CZ 1 ATOM 3901 N NH1 . ARG A 1 486 ? 1.901 55.545 43.600 1.00 21.12 ? 527 ARG A NH1 1 ATOM 3902 N NH2 . ARG A 1 486 ? 3.546 54.390 42.473 1.00 22.77 ? 527 ARG A NH2 1 ATOM 3903 N N . LEU A 1 487 ? 6.549 59.039 48.472 1.00 20.21 ? 528 LEU A N 1 ATOM 3904 C CA . LEU A 1 487 ? 5.812 59.492 49.651 1.00 19.93 ? 528 LEU A CA 1 ATOM 3905 C C . LEU A 1 487 ? 6.586 60.440 50.574 1.00 21.22 ? 528 LEU A C 1 ATOM 3906 O O . LEU A 1 487 ? 5.954 61.102 51.408 1.00 22.78 ? 528 LEU A O 1 ATOM 3907 C CB . LEU A 1 487 ? 5.305 58.296 50.492 1.00 19.65 ? 528 LEU A CB 1 ATOM 3908 C CG . LEU A 1 487 ? 4.359 57.365 49.679 1.00 21.42 ? 528 LEU A CG 1 ATOM 3909 C CD1 . LEU A 1 487 ? 3.915 56.166 50.562 1.00 22.48 ? 528 LEU A CD1 1 ATOM 3910 C CD2 . LEU A 1 487 ? 3.093 58.128 49.208 1.00 25.43 ? 528 LEU A CD2 1 ATOM 3911 N N . GLY A 1 488 ? 7.897 60.487 50.449 1.00 19.90 ? 529 GLY A N 1 ATOM 3912 C CA . GLY A 1 488 ? 8.731 61.424 51.267 1.00 20.25 ? 529 GLY A CA 1 ATOM 3913 C C . GLY A 1 488 ? 8.807 60.979 52.732 1.00 20.79 ? 529 GLY A C 1 ATOM 3914 O O . GLY A 1 488 ? 8.787 61.808 53.653 1.00 20.16 ? 529 GLY A O 1 ATOM 3915 N N . ILE A 1 489 ? 8.941 59.675 52.925 1.00 20.36 ? 530 ILE A N 1 ATOM 3916 C CA . ILE A 1 489 ? 9.252 59.128 54.274 1.00 20.05 ? 530 ILE A CA 1 ATOM 3917 C C . ILE A 1 489 ? 10.762 58.903 54.402 1.00 21.01 ? 530 ILE A C 1 ATOM 3918 O O . ILE A 1 489 ? 11.380 58.243 53.575 1.00 21.28 ? 530 ILE A O 1 ATOM 3919 C CB . ILE A 1 489 ? 8.462 57.821 54.478 1.00 19.58 ? 530 ILE A CB 1 ATOM 3920 C CG1 . ILE A 1 489 ? 6.963 58.160 54.450 1.00 22.31 ? 530 ILE A CG1 1 ATOM 3921 C CG2 . ILE A 1 489 ? 8.834 57.125 55.835 1.00 21.22 ? 530 ILE A CG2 1 ATOM 3922 C CD1 . ILE A 1 489 ? 6.103 56.854 54.217 1.00 23.95 ? 530 ILE A CD1 1 ATOM 3923 N N . ALA A 1 490 ? 11.363 59.437 55.470 1.00 21.05 ? 531 ALA A N 1 ATOM 3924 C CA . ALA A 1 490 ? 12.784 59.258 55.718 1.00 21.91 ? 531 ALA A CA 1 ATOM 3925 C C . ALA A 1 490 ? 13.177 57.797 55.633 1.00 22.16 ? 531 ALA A C 1 ATOM 3926 O O . ALA A 1 490 ? 12.582 56.953 56.334 1.00 23.06 ? 531 ALA A O 1 ATOM 3927 C CB . ALA A 1 490 ? 13.128 59.819 57.171 1.00 22.94 ? 531 ALA A CB 1 ATOM 3928 N N . SER A 1 491 ? 14.186 57.466 54.805 1.00 21.36 ? 532 SER A N 1 ATOM 3929 C CA . SER A 1 491 ? 14.499 56.068 54.576 1.00 21.57 ? 532 SER A CA 1 ATOM 3930 C C . SER A 1 491 ? 15.992 55.823 54.692 1.00 22.66 ? 532 SER A C 1 ATOM 3931 O O . SER A 1 491 ? 16.811 56.748 54.475 1.00 22.28 ? 532 SER A O 1 ATOM 3932 C CB . SER A 1 491 ? 14.012 55.660 53.153 1.00 23.60 ? 532 SER A CB 1 ATOM 3933 O OG . SER A 1 491 ? 12.602 55.702 53.076 1.00 23.31 ? 532 SER A OG 1 ATOM 3934 N N . GLY A 1 492 ? 16.365 54.575 54.966 1.00 22.53 ? 533 GLY A N 1 ATOM 3935 C CA . GLY A 1 492 ? 17.773 54.241 55.007 1.00 23.94 ? 533 GLY A CA 1 ATOM 3936 C C . GLY A 1 492 ? 18.009 52.767 54.705 1.00 24.15 ? 533 GLY A C 1 ATOM 3937 O O . GLY A 1 492 ? 17.067 51.950 54.729 1.00 24.17 ? 533 GLY A O 1 ATOM 3938 N N . ARG A 1 493 ? 19.265 52.440 54.472 1.00 23.20 ? 534 ARG A N 1 ATOM 3939 C CA . ARG A 1 493 ? 19.657 51.019 54.269 1.00 24.52 ? 534 ARG A CA 1 ATOM 3940 C C . ARG A 1 493 ? 21.126 50.856 54.605 1.00 25.47 ? 534 ARG A C 1 ATOM 3941 O O . ARG A 1 493 ? 21.886 51.827 54.588 1.00 25.67 ? 534 ARG A O 1 ATOM 3942 C CB . ARG A 1 493 ? 19.421 50.584 52.803 1.00 24.88 ? 534 ARG A CB 1 ATOM 3943 C CG . ARG A 1 493 ? 20.266 51.397 51.738 1.00 28.06 ? 534 ARG A CG 1 ATOM 3944 C CD . ARG A 1 493 ? 19.645 51.266 50.249 1.00 29.14 ? 534 ARG A CD 1 ATOM 3945 N NE . ARG A 1 493 ? 19.612 49.868 49.840 1.00 31.56 ? 534 ARG A NE 1 ATOM 3946 C CZ . ARG A 1 493 ? 19.734 49.432 48.583 1.00 33.63 ? 534 ARG A CZ 1 ATOM 3947 N NH1 . ARG A 1 493 ? 19.670 48.119 48.353 1.00 31.93 ? 534 ARG A NH1 1 ATOM 3948 N NH2 . ARG A 1 493 ? 19.915 50.302 47.578 1.00 30.51 ? 534 ARG A NH2 1 ATOM 3949 N N . ALA A 1 494 ? 21.508 49.623 54.951 1.00 25.50 ? 535 ALA A N 1 ATOM 3950 C CA . ALA A 1 494 ? 22.870 49.378 55.363 1.00 26.69 ? 535 ALA A CA 1 ATOM 3951 C C . ALA A 1 494 ? 23.163 47.919 55.083 1.00 26.10 ? 535 ALA A C 1 ATOM 3952 O O . ALA A 1 494 ? 22.310 47.050 55.349 1.00 25.93 ? 535 ALA A O 1 ATOM 3953 C CB . ALA A 1 494 ? 23.013 49.646 56.866 1.00 27.13 ? 535 ALA A CB 1 ATOM 3954 N N . ARG A 1 495 ? 24.383 47.641 54.637 1.00 25.81 ? 536 ARG A N 1 ATOM 3955 C CA . ARG A 1 495 ? 24.792 46.245 54.420 1.00 27.52 ? 536 ARG A CA 1 ATOM 3956 C C . ARG A 1 495 ? 26.298 46.161 54.479 1.00 27.93 ? 536 ARG A C 1 ATOM 3957 O O . ARG A 1 495 ? 26.960 47.196 54.456 1.00 29.43 ? 536 ARG A O 1 ATOM 3958 C CB . ARG A 1 495 ? 24.287 45.744 53.039 1.00 28.81 ? 536 ARG A CB 1 ATOM 3959 C CG . ARG A 1 495 ? 25.013 46.358 51.867 1.00 31.13 ? 536 ARG A CG 1 ATOM 3960 C CD . ARG A 1 495 ? 24.552 45.719 50.552 1.00 37.03 ? 536 ARG A CD 1 ATOM 3961 N NE . ARG A 1 495 ? 23.083 45.697 50.454 1.00 37.66 ? 536 ARG A NE 1 ATOM 3962 C CZ . ARG A 1 495 ? 22.404 45.298 49.376 1.00 39.44 ? 536 ARG A CZ 1 ATOM 3963 N NH1 . ARG A 1 495 ? 23.054 44.913 48.268 1.00 39.62 ? 536 ARG A NH1 1 ATOM 3964 N NH2 . ARG A 1 495 ? 21.075 45.276 49.408 1.00 35.96 ? 536 ARG A NH2 1 ATOM 3965 N N . TYR A 1 496 ? 26.845 44.946 54.552 1.00 27.15 ? 537 TYR A N 1 ATOM 3966 C CA . TYR A 1 496 ? 28.289 44.742 54.399 1.00 28.62 ? 537 TYR A CA 1 ATOM 3967 C C . TYR A 1 496 ? 28.639 44.617 52.908 1.00 29.28 ? 537 TYR A C 1 ATOM 3968 O O . TYR A 1 496 ? 27.879 44.026 52.121 1.00 30.64 ? 537 TYR A O 1 ATOM 3969 C CB . TYR A 1 496 ? 28.798 43.542 55.238 1.00 27.57 ? 537 TYR A CB 1 ATOM 3970 C CG . TYR A 1 496 ? 29.709 44.042 56.341 1.00 30.53 ? 537 TYR A CG 1 ATOM 3971 C CD1 . TYR A 1 496 ? 29.204 44.815 57.402 1.00 32.21 ? 537 TYR A CD1 1 ATOM 3972 C CD2 . TYR A 1 496 ? 31.083 43.831 56.270 1.00 29.58 ? 537 TYR A CD2 1 ATOM 3973 C CE1 . TYR A 1 496 ? 30.064 45.334 58.394 1.00 32.11 ? 537 TYR A CE1 1 ATOM 3974 C CE2 . TYR A 1 496 ? 31.946 44.331 57.268 1.00 31.84 ? 537 TYR A CE2 1 ATOM 3975 C CZ . TYR A 1 496 ? 31.412 45.059 58.324 1.00 33.45 ? 537 TYR A CZ 1 ATOM 3976 O OH . TYR A 1 496 ? 32.246 45.573 59.289 1.00 35.30 ? 537 TYR A OH 1 ATOM 3977 N N . THR A 1 497 ? 29.762 45.218 52.531 1.00 30.76 ? 538 THR A N 1 ATOM 3978 C CA . THR A 1 497 ? 30.127 45.329 51.122 1.00 32.07 ? 538 THR A CA 1 ATOM 3979 C C . THR A 1 497 ? 31.588 44.936 50.889 1.00 33.01 ? 538 THR A C 1 ATOM 3980 O O . THR A 1 497 ? 32.359 44.748 51.837 1.00 32.92 ? 538 THR A O 1 ATOM 3981 C CB . THR A 1 497 ? 29.875 46.770 50.568 1.00 31.90 ? 538 THR A CB 1 ATOM 3982 O OG1 . THR A 1 497 ? 29.972 46.724 49.145 1.00 34.82 ? 538 THR A OG1 1 ATOM 3983 C CG2 . THR A 1 497 ? 30.935 47.765 51.068 1.00 31.63 ? 538 THR A CG2 1 ATOM 3984 N N . LYS A 1 498 ? 31.953 44.844 49.609 1.00 35.56 ? 539 LYS A N 1 ATOM 3985 C CA . LYS A 1 498 ? 33.331 44.594 49.150 1.00 40.23 ? 539 LYS A CA 1 ATOM 3986 C C . LYS A 1 498 ? 34.170 45.877 49.084 1.00 43.33 ? 539 LYS A C 1 ATOM 3987 O O . LYS A 1 498 ? 33.668 46.964 49.347 1.00 42.14 ? 539 LYS A O 1 ATOM 3988 C CB . LYS A 1 498 ? 33.304 43.884 47.768 1.00 40.02 ? 539 LYS A CB 1 ATOM 3989 C CG A LYS A 1 498 ? 32.996 44.764 46.553 0.50 41.70 ? 539 LYS A CG 1 ATOM 3990 C CD A LYS A 1 498 ? 31.506 44.960 46.340 0.50 44.54 ? 539 LYS A CD 1 ATOM 3991 C CE A LYS A 1 498 ? 31.202 45.786 45.077 0.50 47.57 ? 539 LYS A CE 1 ATOM 3992 N NZ A LYS A 1 498 ? 30.653 44.960 43.941 0.50 47.34 ? 539 LYS A NZ 1 ATOM 3993 N N . ASN A 1 499 ? 35.457 45.740 48.762 1.00 48.40 ? 540 ASN A N 1 ATOM 3994 C CA . ASN A 1 499 ? 36.325 46.891 48.465 1.00 53.76 ? 540 ASN A CA 1 ATOM 3995 C C . ASN A 1 499 ? 36.031 47.576 47.093 1.00 56.64 ? 540 ASN A C 1 ATOM 3996 O O . ASN A 1 499 ? 36.025 48.809 46.989 1.00 58.95 ? 540 ASN A O 1 ATOM 3997 C CB . ASN A 1 499 ? 37.796 46.451 48.546 1.00 55.17 ? 540 ASN A CB 1 ATOM 3998 C CG . ASN A 1 499 ? 38.747 47.621 48.737 1.00 57.24 ? 540 ASN A CG 1 ATOM 3999 O OD1 . ASN A 1 499 ? 38.467 48.747 48.305 1.00 59.17 ? 540 ASN A OD1 1 ATOM 4000 N ND2 . ASN A 1 499 ? 39.878 47.364 49.397 1.00 59.49 ? 540 ASN A ND2 1 ATOM 4001 N N . TRP A 1 500 ? 35.738 46.759 46.080 1.00 59.56 ? 541 TRP A N 1 ATOM 4002 C CA . TRP A 1 500 ? 35.672 47.081 44.621 1.00 62.16 ? 541 TRP A CA 1 ATOM 4003 C C . TRP A 1 500 ? 34.878 48.324 44.112 1.00 62.76 ? 541 TRP A C 1 ATOM 4004 O O . TRP A 1 500 ? 33.782 48.165 43.533 1.00 62.04 ? 541 TRP A O 1 ATOM 4005 C CB . TRP A 1 500 ? 35.111 45.831 43.915 1.00 62.32 ? 541 TRP A CB 1 ATOM 4006 C CG . TRP A 1 500 ? 35.616 45.540 42.523 1.00 65.28 ? 541 TRP A CG 1 ATOM 4007 C CD1 . TRP A 1 500 ? 36.237 46.411 41.654 1.00 66.94 ? 541 TRP A CD1 1 ATOM 4008 C CD2 . TRP A 1 500 ? 35.492 44.285 41.818 1.00 67.10 ? 541 TRP A CD2 1 ATOM 4009 N NE1 . TRP A 1 500 ? 36.525 45.762 40.465 1.00 68.64 ? 541 TRP A NE1 1 ATOM 4010 C CE2 . TRP A 1 500 ? 36.078 44.463 40.538 1.00 67.85 ? 541 TRP A CE2 1 ATOM 4011 C CE3 . TRP A 1 500 ? 34.952 43.023 42.152 1.00 66.97 ? 541 TRP A CE3 1 ATOM 4012 C CZ2 . TRP A 1 500 ? 36.145 43.421 39.590 1.00 67.59 ? 541 TRP A CZ2 1 ATOM 4013 C CZ3 . TRP A 1 500 ? 35.019 41.987 41.205 1.00 67.35 ? 541 TRP A CZ3 1 ATOM 4014 C CH2 . TRP A 1 500 ? 35.611 42.199 39.942 1.00 65.46 ? 541 TRP A CH2 1 ATOM 4015 N N . GLU A 1 501 ? 35.461 49.528 44.242 1.00 64.51 ? 542 GLU A N 1 ATOM 4016 C CA . GLU A 1 501 ? 34.753 50.807 43.954 1.00 65.25 ? 542 GLU A CA 1 ATOM 4017 C C . GLU A 1 501 ? 34.095 50.947 42.573 1.00 64.47 ? 542 GLU A C 1 ATOM 4018 O O . GLU A 1 501 ? 32.942 51.402 42.482 1.00 64.26 ? 542 GLU A O 1 ATOM 4019 C CB . GLU A 1 501 ? 35.654 52.032 44.210 1.00 66.81 ? 542 GLU A CB 1 ATOM 4020 C CG . GLU A 1 501 ? 34.854 53.345 44.434 1.00 69.86 ? 542 GLU A CG 1 ATOM 4021 C CD . GLU A 1 501 ? 34.132 53.391 45.798 1.00 74.45 ? 542 GLU A CD 1 ATOM 4022 O OE1 . GLU A 1 501 ? 34.437 52.534 46.669 1.00 77.76 ? 542 GLU A OE1 1 ATOM 4023 O OE2 . GLU A 1 501 ? 33.266 54.283 46.008 1.00 74.41 ? 542 GLU A OE2 1 ATOM 4024 N N . THR A 1 502 ? 34.824 50.575 41.518 1.00 64.50 ? 543 THR A N 1 ATOM 4025 C CA . THR A 1 502 ? 34.289 50.579 40.138 1.00 63.68 ? 543 THR A CA 1 ATOM 4026 C C . THR A 1 502 ? 33.129 49.583 39.910 1.00 61.49 ? 543 THR A C 1 ATOM 4027 O O . THR A 1 502 ? 32.380 49.684 38.908 1.00 61.41 ? 543 THR A O 1 ATOM 4028 C CB . THR A 1 502 ? 35.402 50.304 39.073 1.00 65.10 ? 543 THR A CB 1 ATOM 4029 O OG1 . THR A 1 502 ? 36.206 49.171 39.471 1.00 66.76 ? 543 THR A OG1 1 ATOM 4030 C CG2 . THR A 1 502 ? 36.279 51.549 38.859 1.00 65.60 ? 543 THR A CG2 1 ATOM 4031 N N . ASN A 1 503 ? 33.002 48.611 40.811 1.00 58.78 ? 544 ASN A N 1 ATOM 4032 C CA . ASN A 1 503 ? 31.909 47.634 40.717 1.00 56.17 ? 544 ASN A CA 1 ATOM 4033 C C . ASN A 1 503 ? 30.676 47.947 41.604 1.00 53.28 ? 544 ASN A C 1 ATOM 4034 O O . ASN A 1 503 ? 29.832 47.071 41.794 1.00 51.53 ? 544 ASN A O 1 ATOM 4035 C CB . ASN A 1 503 ? 32.424 46.212 41.022 1.00 56.97 ? 544 ASN A CB 1 ATOM 4036 C CG . ASN A 1 503 ? 32.579 45.342 39.759 1.00 59.10 ? 544 ASN A CG 1 ATOM 4037 O OD1 . ASN A 1 503 ? 32.896 45.835 38.681 1.00 61.09 ? 544 ASN A OD1 1 ATOM 4038 N ND2 . ASN A 1 503 ? 32.346 44.040 39.907 1.00 60.34 ? 544 ASN A ND2 1 ATOM 4039 N N . LYS A 1 504 ? 30.572 49.164 42.146 1.00 50.77 ? 545 LYS A N 1 ATOM 4040 C CA . LYS A 1 504 ? 29.556 49.399 43.197 1.00 49.54 ? 545 LYS A CA 1 ATOM 4041 C C . LYS A 1 504 ? 28.067 49.321 42.733 1.00 46.69 ? 545 LYS A C 1 ATOM 4042 O O . LYS A 1 504 ? 27.148 49.121 43.563 1.00 45.77 ? 545 LYS A O 1 ATOM 4043 C CB . LYS A 1 504 ? 29.838 50.679 44.001 1.00 50.29 ? 545 LYS A CB 1 ATOM 4044 C CG . LYS A 1 504 ? 29.548 51.968 43.277 1.00 53.57 ? 545 LYS A CG 1 ATOM 4045 C CD . LYS A 1 504 ? 29.908 53.172 44.152 1.00 58.51 ? 545 LYS A CD 1 ATOM 4046 C CE . LYS A 1 504 ? 29.269 54.435 43.588 1.00 62.25 ? 545 LYS A CE 1 ATOM 4047 N NZ . LYS A 1 504 ? 30.029 54.938 42.392 1.00 64.47 ? 545 LYS A NZ 1 ATOM 4048 N N . PHE A 1 505 ? 27.838 49.465 41.429 1.00 43.80 ? 546 PHE A N 1 ATOM 4049 C CA . PHE A 1 505 ? 26.503 49.241 40.857 1.00 41.91 ? 546 PHE A CA 1 ATOM 4050 C C . PHE A 1 505 ? 26.416 47.940 40.035 1.00 41.88 ? 546 PHE A C 1 ATOM 4051 O O . PHE A 1 505 ? 25.373 47.657 39.430 1.00 41.33 ? 546 PHE A O 1 ATOM 4052 C CB . PHE A 1 505 ? 26.058 50.437 39.994 1.00 41.41 ? 546 PHE A CB 1 ATOM 4053 C CG . PHE A 1 505 ? 25.907 51.727 40.768 1.00 41.29 ? 546 PHE A CG 1 ATOM 4054 C CD1 . PHE A 1 505 ? 25.035 51.805 41.854 1.00 41.64 ? 546 PHE A CD1 1 ATOM 4055 C CD2 . PHE A 1 505 ? 26.638 52.871 40.399 1.00 42.64 ? 546 PHE A CD2 1 ATOM 4056 C CE1 . PHE A 1 505 ? 24.875 53.014 42.566 1.00 42.03 ? 546 PHE A CE1 1 ATOM 4057 C CE2 . PHE A 1 505 ? 26.492 54.081 41.094 1.00 41.47 ? 546 PHE A CE2 1 ATOM 4058 C CZ . PHE A 1 505 ? 25.617 54.143 42.192 1.00 42.64 ? 546 PHE A CZ 1 ATOM 4059 N N . SER A 1 506 ? 27.489 47.148 40.011 1.00 41.03 ? 547 SER A N 1 ATOM 4060 C CA . SER A 1 506 ? 27.482 45.969 39.115 1.00 41.41 ? 547 SER A CA 1 ATOM 4061 C C . SER A 1 506 ? 26.868 44.701 39.741 1.00 40.55 ? 547 SER A C 1 ATOM 4062 O O . SER A 1 506 ? 26.395 43.811 39.002 1.00 42.14 ? 547 SER A O 1 ATOM 4063 C CB . SER A 1 506 ? 28.878 45.723 38.518 1.00 42.42 ? 547 SER A CB 1 ATOM 4064 O OG . SER A 1 506 ? 29.279 46.913 37.827 1.00 43.11 ? 547 SER A OG 1 ATOM 4065 N N . GLY A 1 507 ? 26.832 44.654 41.085 1.00 38.90 ? 548 GLY A N 1 ATOM 4066 C CA . GLY A 1 507 ? 26.515 43.429 41.840 1.00 37.91 ? 548 GLY A CA 1 ATOM 4067 C C . GLY A 1 507 ? 27.777 42.576 42.039 1.00 37.14 ? 548 GLY A C 1 ATOM 4068 O O . GLY A 1 507 ? 28.800 42.754 41.338 1.00 39.26 ? 548 GLY A O 1 ATOM 4069 N N . TYR A 1 508 ? 27.722 41.685 43.025 1.00 34.03 ? 549 TYR A N 1 ATOM 4070 C CA . TYR A 1 508 ? 28.777 40.729 43.299 1.00 32.26 ? 549 TYR A CA 1 ATOM 4071 C C . TYR A 1 508 ? 28.735 39.692 42.167 1.00 30.14 ? 549 TYR A C 1 ATOM 4072 O O . TYR A 1 508 ? 27.765 39.651 41.384 1.00 30.89 ? 549 TYR A O 1 ATOM 4073 C CB . TYR A 1 508 ? 28.531 40.096 44.687 1.00 31.41 ? 549 TYR A CB 1 ATOM 4074 C CG . TYR A 1 508 ? 27.096 39.711 44.880 1.00 29.78 ? 549 TYR A CG 1 ATOM 4075 C CD1 . TYR A 1 508 ? 26.653 38.414 44.607 1.00 29.64 ? 549 TYR A CD1 1 ATOM 4076 C CD2 . TYR A 1 508 ? 26.156 40.671 45.367 1.00 31.37 ? 549 TYR A CD2 1 ATOM 4077 C CE1 . TYR A 1 508 ? 25.291 38.063 44.776 1.00 28.33 ? 549 TYR A CE1 1 ATOM 4078 C CE2 . TYR A 1 508 ? 24.841 40.337 45.532 1.00 30.01 ? 549 TYR A CE2 1 ATOM 4079 C CZ . TYR A 1 508 ? 24.417 39.041 45.239 1.00 26.36 ? 549 TYR A CZ 1 ATOM 4080 O OH . TYR A 1 508 ? 23.096 38.786 45.415 1.00 30.22 ? 549 TYR A OH 1 ATOM 4081 N N . PRO A 1 509 ? 29.768 38.849 42.046 1.00 29.21 ? 550 PRO A N 1 ATOM 4082 C CA . PRO A 1 509 ? 29.794 38.053 40.808 1.00 28.42 ? 550 PRO A CA 1 ATOM 4083 C C . PRO A 1 509 ? 28.601 37.146 40.573 1.00 28.00 ? 550 PRO A C 1 ATOM 4084 O O . PRO A 1 509 ? 28.189 36.976 39.414 1.00 27.72 ? 550 PRO A O 1 ATOM 4085 C CB . PRO A 1 509 ? 31.105 37.223 40.952 1.00 29.03 ? 550 PRO A CB 1 ATOM 4086 C CG . PRO A 1 509 ? 32.024 38.237 41.650 1.00 29.84 ? 550 PRO A CG 1 ATOM 4087 C CD . PRO A 1 509 ? 31.078 38.819 42.730 1.00 30.36 ? 550 PRO A CD 1 ATOM 4088 N N . LEU A 1 510 ? 28.064 36.538 41.626 1.00 26.02 ? 551 LEU A N 1 ATOM 4089 C CA . LEU A 1 510 ? 26.987 35.538 41.417 1.00 26.76 ? 551 LEU A CA 1 ATOM 4090 C C . LEU A 1 510 ? 25.587 36.127 41.510 1.00 26.99 ? 551 LEU A C 1 ATOM 4091 O O . LEU A 1 510 ? 24.569 35.377 41.598 1.00 28.17 ? 551 LEU A O 1 ATOM 4092 C CB . LEU A 1 510 ? 27.117 34.409 42.435 1.00 26.77 ? 551 LEU A CB 1 ATOM 4093 C CG . LEU A 1 510 ? 28.445 33.676 42.159 1.00 28.51 ? 551 LEU A CG 1 ATOM 4094 C CD1 . LEU A 1 510 ? 28.783 32.668 43.236 1.00 29.70 ? 551 LEU A CD1 1 ATOM 4095 C CD2 . LEU A 1 510 ? 28.452 32.995 40.731 1.00 26.46 ? 551 LEU A CD2 1 ATOM 4096 N N . TYR A 1 511 ? 25.531 37.458 41.494 1.00 25.03 ? 552 TYR A N 1 ATOM 4097 C CA . TYR A 1 511 ? 24.247 38.207 41.594 1.00 25.95 ? 552 TYR A CA 1 ATOM 4098 C C . TYR A 1 511 ? 23.216 37.722 40.575 1.00 24.83 ? 552 TYR A C 1 ATOM 4099 O O . TYR A 1 511 ? 23.499 37.676 39.354 1.00 26.61 ? 552 TYR A O 1 ATOM 4100 C CB . TYR A 1 511 ? 24.600 39.665 41.387 1.00 25.52 ? 552 TYR A CB 1 ATOM 4101 C CG . TYR A 1 511 ? 23.460 40.608 41.210 1.00 28.23 ? 552 TYR A CG 1 ATOM 4102 C CD1 . TYR A 1 511 ? 22.536 40.819 42.238 1.00 26.45 ? 552 TYR A CD1 1 ATOM 4103 C CD2 . TYR A 1 511 ? 23.287 41.270 39.995 1.00 28.67 ? 552 TYR A CD2 1 ATOM 4104 C CE1 . TYR A 1 511 ? 21.470 41.728 42.057 1.00 27.44 ? 552 TYR A CE1 1 ATOM 4105 C CE2 . TYR A 1 511 ? 22.229 42.191 39.810 1.00 28.60 ? 552 TYR A CE2 1 ATOM 4106 C CZ . TYR A 1 511 ? 21.340 42.383 40.823 1.00 27.60 ? 552 TYR A CZ 1 ATOM 4107 O OH . TYR A 1 511 ? 20.309 43.266 40.635 1.00 29.49 ? 552 TYR A OH 1 ATOM 4108 N N . HIS A 1 512 ? 22.047 37.306 41.074 1.00 24.79 ? 553 HIS A N 1 ATOM 4109 C CA . HIS A 1 512 ? 20.894 36.870 40.249 1.00 24.66 ? 553 HIS A CA 1 ATOM 4110 C C . HIS A 1 512 ? 21.162 35.616 39.410 1.00 26.63 ? 553 HIS A C 1 ATOM 4111 O O . HIS A 1 512 ? 20.430 35.327 38.420 1.00 26.15 ? 553 HIS A O 1 ATOM 4112 C CB . HIS A 1 512 ? 20.377 38.003 39.339 1.00 23.86 ? 553 HIS A CB 1 ATOM 4113 C CG . HIS A 1 512 ? 19.595 39.068 40.074 1.00 23.79 ? 553 HIS A CG 1 ATOM 4114 N ND1 . HIS A 1 512 ? 18.977 40.098 39.411 1.00 21.65 ? 553 HIS A ND1 1 ATOM 4115 C CD2 . HIS A 1 512 ? 19.317 39.248 41.392 1.00 22.84 ? 553 HIS A CD2 1 ATOM 4116 C CE1 . HIS A 1 512 ? 18.325 40.875 40.281 1.00 20.83 ? 553 HIS A CE1 1 ATOM 4117 N NE2 . HIS A 1 512 ? 18.504 40.361 41.483 1.00 21.72 ? 553 HIS A NE2 1 ATOM 4118 N N . SER A 1 513 ? 22.152 34.837 39.840 1.00 27.48 ? 554 SER A N 1 ATOM 4119 C CA . SER A 1 513 ? 22.460 33.593 39.177 1.00 26.57 ? 554 SER A CA 1 ATOM 4120 C C . SER A 1 513 ? 21.954 32.387 40.045 1.00 30.41 ? 554 SER A C 1 ATOM 4121 O O . SER A 1 513 ? 21.704 32.549 41.214 1.00 27.05 ? 554 SER A O 1 ATOM 4122 C CB . SER A 1 513 ? 23.977 33.466 38.934 1.00 26.94 ? 554 SER A CB 1 ATOM 4123 O OG A SER A 1 513 ? 24.682 33.159 40.125 0.50 23.62 ? 554 SER A OG 1 ATOM 4124 O OG B SER A 1 513 ? 24.345 32.096 38.776 0.50 29.82 ? 554 SER A OG 1 ATOM 4125 N N . VAL A 1 514 ? 21.889 31.184 39.434 1.00 27.63 ? 555 VAL A N 1 ATOM 4126 C CA . VAL A 1 514 ? 21.468 29.981 40.173 1.00 29.82 ? 555 VAL A CA 1 ATOM 4127 C C . VAL A 1 514 ? 22.485 29.662 41.304 1.00 29.34 ? 555 VAL A C 1 ATOM 4128 O O . VAL A 1 514 ? 22.175 28.899 42.235 1.00 30.87 ? 555 VAL A O 1 ATOM 4129 C CB . VAL A 1 514 ? 21.344 28.779 39.199 1.00 29.74 ? 555 VAL A CB 1 ATOM 4130 C CG1 . VAL A 1 514 ? 22.766 28.325 38.684 1.00 30.85 ? 555 VAL A CG1 1 ATOM 4131 C CG2 . VAL A 1 514 ? 20.654 27.590 39.858 1.00 28.89 ? 555 VAL A CG2 1 ATOM 4132 N N . TYR A 1 515 ? 23.679 30.250 41.243 1.00 28.22 ? 556 TYR A N 1 ATOM 4133 C CA . TYR A 1 515 ? 24.758 29.871 42.181 1.00 29.55 ? 556 TYR A CA 1 ATOM 4134 C C . TYR A 1 515 ? 24.692 30.607 43.511 1.00 29.81 ? 556 TYR A C 1 ATOM 4135 O O . TYR A 1 515 ? 25.512 30.295 44.402 1.00 30.45 ? 556 TYR A O 1 ATOM 4136 C CB . TYR A 1 515 ? 26.176 30.049 41.571 1.00 29.34 ? 556 TYR A CB 1 ATOM 4137 C CG . TYR A 1 515 ? 26.286 29.273 40.284 1.00 31.16 ? 556 TYR A CG 1 ATOM 4138 C CD1 . TYR A 1 515 ? 26.167 27.866 40.295 1.00 30.12 ? 556 TYR A CD1 1 ATOM 4139 C CD2 . TYR A 1 515 ? 26.446 29.921 39.060 1.00 29.15 ? 556 TYR A CD2 1 ATOM 4140 C CE1 . TYR A 1 515 ? 26.200 27.132 39.121 1.00 30.57 ? 556 TYR A CE1 1 ATOM 4141 C CE2 . TYR A 1 515 ? 26.505 29.178 37.869 1.00 30.00 ? 556 TYR A CE2 1 ATOM 4142 C CZ . TYR A 1 515 ? 26.378 27.795 37.912 1.00 32.30 ? 556 TYR A CZ 1 ATOM 4143 O OH . TYR A 1 515 ? 26.421 27.059 36.751 1.00 34.44 ? 556 TYR A OH 1 ATOM 4144 N N . GLU A 1 516 ? 23.763 31.572 43.647 1.00 27.98 ? 557 GLU A N 1 ATOM 4145 C CA . GLU A 1 516 ? 23.526 32.247 44.938 1.00 29.24 ? 557 GLU A CA 1 ATOM 4146 C C . GLU A 1 516 ? 22.829 31.314 45.889 1.00 28.45 ? 557 GLU A C 1 ATOM 4147 O O . GLU A 1 516 ? 21.607 31.223 45.846 1.00 30.03 ? 557 GLU A O 1 ATOM 4148 C CB . GLU A 1 516 ? 22.528 33.418 44.758 1.00 30.21 ? 557 GLU A CB 1 ATOM 4149 C CG . GLU A 1 516 ? 23.148 34.592 44.272 1.00 35.74 ? 557 GLU A CG 1 ATOM 4150 C CD . GLU A 1 516 ? 22.254 35.792 44.632 1.00 33.70 ? 557 GLU A CD 1 ATOM 4151 O OE1 . GLU A 1 516 ? 21.882 36.551 43.734 1.00 35.55 ? 557 GLU A OE1 1 ATOM 4152 O OE2 . GLU A 1 516 ? 21.864 35.871 45.814 1.00 36.48 ? 557 GLU A OE2 1 ATOM 4153 N N . THR A 1 517 ? 23.595 30.590 46.700 1.00 28.95 ? 558 THR A N 1 ATOM 4154 C CA . THR A 1 517 ? 23.058 29.522 47.547 1.00 28.56 ? 558 THR A CA 1 ATOM 4155 C C . THR A 1 517 ? 23.462 29.757 49.001 1.00 28.10 ? 558 THR A C 1 ATOM 4156 O O . THR A 1 517 ? 24.325 30.601 49.288 1.00 27.04 ? 558 THR A O 1 ATOM 4157 C CB . THR A 1 517 ? 23.681 28.145 47.154 1.00 29.54 ? 558 THR A CB 1 ATOM 4158 O OG1 . THR A 1 517 ? 25.109 28.245 47.226 1.00 32.00 ? 558 THR A OG1 1 ATOM 4159 C CG2 . THR A 1 517 ? 23.266 27.740 45.720 1.00 31.98 ? 558 THR A CG2 1 ATOM 4160 N N . TYR A 1 518 ? 22.884 28.969 49.912 1.00 27.45 ? 559 TYR A N 1 ATOM 4161 C CA . TYR A 1 518 ? 23.335 28.960 51.298 1.00 28.61 ? 559 TYR A CA 1 ATOM 4162 C C . TYR A 1 518 ? 24.856 28.647 51.365 1.00 29.38 ? 559 TYR A C 1 ATOM 4163 O O . TYR A 1 518 ? 25.596 29.291 52.122 1.00 29.68 ? 559 TYR A O 1 ATOM 4164 C CB . TYR A 1 518 ? 22.570 27.877 52.076 1.00 27.44 ? 559 TYR A CB 1 ATOM 4165 C CG . TYR A 1 518 ? 23.102 27.642 53.450 1.00 30.51 ? 559 TYR A CG 1 ATOM 4166 C CD1 . TYR A 1 518 ? 22.788 28.518 54.495 1.00 31.91 ? 559 TYR A CD1 1 ATOM 4167 C CD2 . TYR A 1 518 ? 23.950 26.548 53.712 1.00 33.28 ? 559 TYR A CD2 1 ATOM 4168 C CE1 . TYR A 1 518 ? 23.296 28.306 55.788 1.00 33.68 ? 559 TYR A CE1 1 ATOM 4169 C CE2 . TYR A 1 518 ? 24.476 26.340 54.999 1.00 36.50 ? 559 TYR A CE2 1 ATOM 4170 C CZ . TYR A 1 518 ? 24.130 27.225 56.029 1.00 36.05 ? 559 TYR A CZ 1 ATOM 4171 O OH . TYR A 1 518 ? 24.623 27.023 57.301 1.00 37.97 ? 559 TYR A OH 1 ATOM 4172 N N . GLU A 1 519 ? 25.305 27.673 50.577 1.00 28.50 ? 560 GLU A N 1 ATOM 4173 C CA . GLU A 1 519 ? 26.723 27.261 50.606 1.00 30.61 ? 560 GLU A CA 1 ATOM 4174 C C . GLU A 1 519 ? 27.649 28.401 50.210 1.00 30.13 ? 560 GLU A C 1 ATOM 4175 O O . GLU A 1 519 ? 28.731 28.555 50.806 1.00 31.05 ? 560 GLU A O 1 ATOM 4176 C CB . GLU A 1 519 ? 26.962 26.032 49.700 1.00 32.04 ? 560 GLU A CB 1 ATOM 4177 C CG . GLU A 1 519 ? 26.335 24.714 50.233 1.00 33.83 ? 560 GLU A CG 1 ATOM 4178 C CD . GLU A 1 519 ? 24.826 24.697 50.089 1.00 38.42 ? 560 GLU A CD 1 ATOM 4179 O OE1 . GLU A 1 519 ? 24.324 25.236 49.089 1.00 34.93 ? 560 GLU A OE1 1 ATOM 4180 O OE2 . GLU A 1 519 ? 24.140 24.132 50.971 1.00 40.19 ? 560 GLU A OE2 1 ATOM 4181 N N . LEU A 1 520 ? 27.230 29.218 49.242 1.00 27.59 ? 561 LEU A N 1 ATOM 4182 C CA . LEU A 1 520 ? 27.998 30.403 48.857 1.00 28.18 ? 561 LEU A CA 1 ATOM 4183 C C . LEU A 1 520 ? 28.259 31.289 50.072 1.00 29.16 ? 561 LEU A C 1 ATOM 4184 O O . LEU A 1 520 ? 29.401 31.752 50.300 1.00 29.56 ? 561 LEU A O 1 ATOM 4185 C CB . LEU A 1 520 ? 27.252 31.246 47.810 1.00 27.74 ? 561 LEU A CB 1 ATOM 4186 C CG . LEU A 1 520 ? 27.899 32.597 47.423 1.00 28.67 ? 561 LEU A CG 1 ATOM 4187 C CD1 . LEU A 1 520 ? 29.327 32.418 46.844 1.00 30.61 ? 561 LEU A CD1 1 ATOM 4188 C CD2 . LEU A 1 520 ? 26.941 33.359 46.462 1.00 30.51 ? 561 LEU A CD2 1 ATOM 4189 N N . VAL A 1 521 ? 27.203 31.555 50.831 1.00 29.10 ? 562 VAL A N 1 ATOM 4190 C CA . VAL A 1 521 ? 27.323 32.464 51.980 1.00 29.73 ? 562 VAL A CA 1 ATOM 4191 C C . VAL A 1 521 ? 28.165 31.800 53.088 1.00 31.23 ? 562 VAL A C 1 ATOM 4192 O O . VAL A 1 521 ? 29.140 32.382 53.592 1.00 31.69 ? 562 VAL A O 1 ATOM 4193 C CB . VAL A 1 521 ? 25.926 32.877 52.482 1.00 28.97 ? 562 VAL A CB 1 ATOM 4194 C CG1 . VAL A 1 521 ? 26.045 33.717 53.811 1.00 29.06 ? 562 VAL A CG1 1 ATOM 4195 C CG2 . VAL A 1 521 ? 25.211 33.687 51.410 1.00 30.49 ? 562 VAL A CG2 1 ATOM 4196 N N . GLU A 1 522 ? 27.798 30.573 53.457 1.00 31.50 ? 563 GLU A N 1 ATOM 4197 C CA . GLU A 1 522 ? 28.410 29.902 54.599 1.00 34.11 ? 563 GLU A CA 1 ATOM 4198 C C . GLU A 1 522 ? 29.887 29.545 54.358 1.00 34.78 ? 563 GLU A C 1 ATOM 4199 O O . GLU A 1 522 ? 30.723 29.636 55.276 1.00 35.70 ? 563 GLU A O 1 ATOM 4200 C CB . GLU A 1 522 ? 27.615 28.633 54.907 1.00 36.03 ? 563 GLU A CB 1 ATOM 4201 C CG . GLU A 1 522 ? 27.966 27.982 56.223 1.00 42.58 ? 563 GLU A CG 1 ATOM 4202 C CD . GLU A 1 522 ? 29.079 26.949 56.107 1.00 49.66 ? 563 GLU A CD 1 ATOM 4203 O OE1 . GLU A 1 522 ? 29.256 26.332 55.024 1.00 50.24 ? 563 GLU A OE1 1 ATOM 4204 O OE2 . GLU A 1 522 ? 29.795 26.761 57.126 1.00 54.96 ? 563 GLU A OE2 1 ATOM 4205 N N . LYS A 1 523 ? 30.236 29.200 53.118 1.00 33.12 ? 564 LYS A N 1 ATOM 4206 C CA . LYS A 1 523 ? 31.634 28.837 52.816 1.00 34.05 ? 564 LYS A CA 1 ATOM 4207 C C . LYS A 1 523 ? 32.515 30.054 52.528 1.00 34.96 ? 564 LYS A C 1 ATOM 4208 O O . LYS A 1 523 ? 33.686 30.058 52.917 1.00 36.13 ? 564 LYS A O 1 ATOM 4209 C CB . LYS A 1 523 ? 31.710 27.926 51.600 1.00 33.45 ? 564 LYS A CB 1 ATOM 4210 C CG . LYS A 1 523 ? 31.058 26.553 51.811 1.00 36.18 ? 564 LYS A CG 1 ATOM 4211 C CD . LYS A 1 523 ? 31.241 25.719 50.520 1.00 39.17 ? 564 LYS A CD 1 ATOM 4212 C CE . LYS A 1 523 ? 30.485 24.389 50.552 1.00 43.83 ? 564 LYS A CE 1 ATOM 4213 N NZ . LYS A 1 523 ? 30.926 23.584 51.690 1.00 49.16 ? 564 LYS A NZ 1 ATOM 4214 N N . PHE A 1 524 ? 31.996 31.021 51.771 1.00 32.45 ? 565 PHE A N 1 ATOM 4215 C CA . PHE A 1 524 ? 32.859 32.062 51.188 1.00 33.68 ? 565 PHE A CA 1 ATOM 4216 C C . PHE A 1 524 ? 32.632 33.473 51.664 1.00 33.99 ? 565 PHE A C 1 ATOM 4217 O O . PHE A 1 524 ? 33.541 34.291 51.518 1.00 35.91 ? 565 PHE A O 1 ATOM 4218 C CB . PHE A 1 524 ? 32.771 32.051 49.661 1.00 33.16 ? 565 PHE A CB 1 ATOM 4219 C CG . PHE A 1 524 ? 33.131 30.702 49.064 1.00 34.97 ? 565 PHE A CG 1 ATOM 4220 C CD1 . PHE A 1 524 ? 34.389 30.153 49.313 1.00 36.13 ? 565 PHE A CD1 1 ATOM 4221 C CD2 . PHE A 1 524 ? 32.206 29.977 48.310 1.00 32.34 ? 565 PHE A CD2 1 ATOM 4222 C CE1 . PHE A 1 524 ? 34.749 28.900 48.790 1.00 40.21 ? 565 PHE A CE1 1 ATOM 4223 C CE2 . PHE A 1 524 ? 32.544 28.704 47.770 1.00 35.24 ? 565 PHE A CE2 1 ATOM 4224 C CZ . PHE A 1 524 ? 33.804 28.156 48.021 1.00 37.79 ? 565 PHE A CZ 1 ATOM 4225 N N . TYR A 1 525 ? 31.435 33.785 52.153 1.00 32.72 ? 566 TYR A N 1 ATOM 4226 C CA . TYR A 1 525 ? 31.154 35.159 52.590 1.00 31.57 ? 566 TYR A CA 1 ATOM 4227 C C . TYR A 1 525 ? 31.263 35.355 54.104 1.00 32.21 ? 566 TYR A C 1 ATOM 4228 O O . TYR A 1 525 ? 31.906 36.329 54.593 1.00 33.26 ? 566 TYR A O 1 ATOM 4229 C CB . TYR A 1 525 ? 29.769 35.644 52.080 1.00 29.56 ? 566 TYR A CB 1 ATOM 4230 C CG . TYR A 1 525 ? 29.849 36.142 50.666 1.00 30.02 ? 566 TYR A CG 1 ATOM 4231 C CD1 . TYR A 1 525 ? 29.930 35.242 49.596 1.00 29.43 ? 566 TYR A CD1 1 ATOM 4232 C CD2 . TYR A 1 525 ? 29.888 37.513 50.384 1.00 31.33 ? 566 TYR A CD2 1 ATOM 4233 C CE1 . TYR A 1 525 ? 30.025 35.686 48.260 1.00 32.10 ? 566 TYR A CE1 1 ATOM 4234 C CE2 . TYR A 1 525 ? 29.987 37.979 49.057 1.00 34.27 ? 566 TYR A CE2 1 ATOM 4235 C CZ . TYR A 1 525 ? 30.054 37.048 48.001 1.00 34.92 ? 566 TYR A CZ 1 ATOM 4236 O OH . TYR A 1 525 ? 30.180 37.479 46.705 1.00 34.77 ? 566 TYR A OH 1 ATOM 4237 N N . ASP A 1 526 ? 30.591 34.494 54.864 1.00 31.84 ? 567 ASP A N 1 ATOM 4238 C CA . ASP A 1 526 ? 30.374 34.834 56.290 1.00 31.78 ? 567 ASP A CA 1 ATOM 4239 C C . ASP A 1 526 ? 30.213 33.577 57.098 1.00 32.47 ? 567 ASP A C 1 ATOM 4240 O O . ASP A 1 526 ? 29.146 33.346 57.650 1.00 32.37 ? 567 ASP A O 1 ATOM 4241 C CB . ASP A 1 526 ? 29.133 35.728 56.434 1.00 30.23 ? 567 ASP A CB 1 ATOM 4242 C CG . ASP A 1 526 ? 29.058 36.428 57.815 1.00 30.53 ? 567 ASP A CG 1 ATOM 4243 O OD1 . ASP A 1 526 ? 30.061 36.370 58.602 1.00 32.45 ? 567 ASP A OD1 1 ATOM 4244 O OD2 . ASP A 1 526 ? 27.997 36.988 58.108 1.00 30.42 ? 567 ASP A OD2 1 ATOM 4245 N N . PRO A 1 527 ? 31.275 32.747 57.182 1.00 34.62 ? 568 PRO A N 1 ATOM 4246 C CA . PRO A 1 527 ? 31.093 31.447 57.841 1.00 35.46 ? 568 PRO A CA 1 ATOM 4247 C C . PRO A 1 527 ? 30.635 31.496 59.309 1.00 36.61 ? 568 PRO A C 1 ATOM 4248 O O . PRO A 1 527 ? 29.905 30.589 59.738 1.00 37.14 ? 568 PRO A O 1 ATOM 4249 C CB . PRO A 1 527 ? 32.457 30.738 57.698 1.00 37.17 ? 568 PRO A CB 1 ATOM 4250 C CG . PRO A 1 527 ? 33.347 31.664 56.992 1.00 38.06 ? 568 PRO A CG 1 ATOM 4251 C CD . PRO A 1 527 ? 32.594 32.891 56.541 1.00 35.12 ? 568 PRO A CD 1 ATOM 4252 N N A MET A 1 528 ? 31.031 32.536 60.048 0.50 36.01 ? 569 MET A N 1 ATOM 4253 N N B MET A 1 528 ? 31.055 32.537 60.040 0.50 36.47 ? 569 MET A N 1 ATOM 4254 C CA A MET A 1 528 ? 30.645 32.692 61.464 0.50 36.26 ? 569 MET A CA 1 ATOM 4255 C CA B MET A 1 528 ? 30.697 32.742 61.457 0.50 37.19 ? 569 MET A CA 1 ATOM 4256 C C A MET A 1 528 ? 29.409 33.593 61.638 0.50 35.09 ? 569 MET A C 1 ATOM 4257 C C B MET A 1 528 ? 29.340 33.460 61.621 0.50 35.72 ? 569 MET A C 1 ATOM 4258 O O A MET A 1 528 ? 29.005 33.911 62.761 0.50 33.76 ? 569 MET A O 1 ATOM 4259 O O B MET A 1 528 ? 28.787 33.515 62.726 0.50 34.75 ? 569 MET A O 1 ATOM 4260 C CB A MET A 1 528 ? 31.815 33.254 62.264 0.50 37.61 ? 569 MET A CB 1 ATOM 4261 C CB B MET A 1 528 ? 31.792 33.556 62.169 0.50 38.68 ? 569 MET A CB 1 ATOM 4262 C CG A MET A 1 528 ? 33.110 32.427 62.134 0.50 39.72 ? 569 MET A CG 1 ATOM 4263 C CG B MET A 1 528 ? 33.211 32.906 62.176 0.50 43.12 ? 569 MET A CG 1 ATOM 4264 S SD A MET A 1 528 ? 32.802 30.736 62.619 0.50 43.69 ? 569 MET A SD 1 ATOM 4265 S SD B MET A 1 528 ? 34.383 33.742 63.292 0.50 51.04 ? 569 MET A SD 1 ATOM 4266 C CE A MET A 1 528 ? 32.433 30.930 64.356 0.50 42.45 ? 569 MET A CE 1 ATOM 4267 C CE B MET A 1 528 ? 35.435 34.654 62.151 0.50 49.32 ? 569 MET A CE 1 ATOM 4268 N N . PHE A 1 529 ? 28.817 34.004 60.515 1.00 33.28 ? 570 PHE A N 1 ATOM 4269 C CA . PHE A 1 529 ? 27.620 34.866 60.514 1.00 32.79 ? 570 PHE A CA 1 ATOM 4270 C C . PHE A 1 529 ? 27.810 36.146 61.311 1.00 32.45 ? 570 PHE A C 1 ATOM 4271 O O . PHE A 1 529 ? 26.859 36.756 61.775 1.00 32.48 ? 570 PHE A O 1 ATOM 4272 C CB . PHE A 1 529 ? 26.322 34.065 60.805 1.00 32.53 ? 570 PHE A CB 1 ATOM 4273 C CG . PHE A 1 529 ? 25.912 33.231 59.631 1.00 32.57 ? 570 PHE A CG 1 ATOM 4274 C CD1 . PHE A 1 529 ? 24.927 33.698 58.766 1.00 34.57 ? 570 PHE A CD1 1 ATOM 4275 C CD2 . PHE A 1 529 ? 26.598 32.024 59.331 1.00 35.50 ? 570 PHE A CD2 1 ATOM 4276 C CE1 . PHE A 1 529 ? 24.572 32.960 57.605 1.00 34.57 ? 570 PHE A CE1 1 ATOM 4277 C CE2 . PHE A 1 529 ? 26.257 31.268 58.161 1.00 35.75 ? 570 PHE A CE2 1 ATOM 4278 C CZ . PHE A 1 529 ? 25.264 31.757 57.311 1.00 33.47 ? 570 PHE A CZ 1 ATOM 4279 N N . LYS A 1 530 ? 29.075 36.549 61.440 1.00 33.15 ? 571 LYS A N 1 ATOM 4280 C CA . LYS A 1 530 ? 29.397 37.756 62.194 1.00 34.25 ? 571 LYS A CA 1 ATOM 4281 C C . LYS A 1 530 ? 29.093 39.021 61.415 1.00 31.56 ? 571 LYS A C 1 ATOM 4282 O O . LYS A 1 530 ? 28.754 40.032 62.017 1.00 30.88 ? 571 LYS A O 1 ATOM 4283 C CB . LYS A 1 530 ? 30.857 37.745 62.681 1.00 35.26 ? 571 LYS A CB 1 ATOM 4284 C CG . LYS A 1 530 ? 31.922 37.849 61.594 1.00 38.17 ? 571 LYS A CG 1 ATOM 4285 C CD . LYS A 1 530 ? 33.310 37.820 62.244 1.00 43.98 ? 571 LYS A CD 1 ATOM 4286 C CE . LYS A 1 530 ? 34.391 37.941 61.181 1.00 45.69 ? 571 LYS A CE 1 ATOM 4287 N NZ . LYS A 1 530 ? 35.739 38.239 61.768 1.00 50.35 ? 571 LYS A NZ 1 ATOM 4288 N N . TYR A 1 531 ? 29.207 38.985 60.085 1.00 30.99 ? 572 TYR A N 1 ATOM 4289 C CA . TYR A 1 531 ? 28.855 40.185 59.308 1.00 30.38 ? 572 TYR A CA 1 ATOM 4290 C C . TYR A 1 531 ? 27.344 40.332 59.261 1.00 29.58 ? 572 TYR A C 1 ATOM 4291 O O . TYR A 1 531 ? 26.827 41.453 59.397 1.00 30.16 ? 572 TYR A O 1 ATOM 4292 C CB . TYR A 1 531 ? 29.478 40.154 57.898 1.00 30.70 ? 572 TYR A CB 1 ATOM 4293 C CG . TYR A 1 531 ? 30.995 40.067 57.989 1.00 32.87 ? 572 TYR A CG 1 ATOM 4294 C CD1 . TYR A 1 531 ? 31.734 41.111 58.578 1.00 34.03 ? 572 TYR A CD1 1 ATOM 4295 C CD2 . TYR A 1 531 ? 31.679 38.947 57.524 1.00 34.98 ? 572 TYR A CD2 1 ATOM 4296 C CE1 . TYR A 1 531 ? 33.101 41.040 58.693 1.00 38.43 ? 572 TYR A CE1 1 ATOM 4297 C CE2 . TYR A 1 531 ? 33.060 38.870 57.645 1.00 36.88 ? 572 TYR A CE2 1 ATOM 4298 C CZ . TYR A 1 531 ? 33.757 39.918 58.205 1.00 39.25 ? 572 TYR A CZ 1 ATOM 4299 O OH . TYR A 1 531 ? 35.128 39.797 58.302 1.00 42.38 ? 572 TYR A OH 1 ATOM 4300 N N . HIS A 1 532 ? 26.636 39.214 59.102 1.00 29.03 ? 573 HIS A N 1 ATOM 4301 C CA . HIS A 1 532 ? 25.163 39.214 59.228 1.00 28.69 ? 573 HIS A CA 1 ATOM 4302 C C . HIS A 1 532 ? 24.740 39.807 60.584 1.00 27.86 ? 573 HIS A C 1 ATOM 4303 O O . HIS A 1 532 ? 23.845 40.628 60.642 1.00 27.05 ? 573 HIS A O 1 ATOM 4304 C CB . HIS A 1 532 ? 24.599 37.810 59.144 1.00 28.70 ? 573 HIS A CB 1 ATOM 4305 C CG . HIS A 1 532 ? 24.480 37.299 57.748 1.00 31.64 ? 573 HIS A CG 1 ATOM 4306 N ND1 . HIS A 1 532 ? 25.559 36.801 57.050 1.00 33.69 ? 573 HIS A ND1 1 ATOM 4307 C CD2 . HIS A 1 532 ? 23.414 37.223 56.917 1.00 33.37 ? 573 HIS A CD2 1 ATOM 4308 C CE1 . HIS A 1 532 ? 25.163 36.434 55.841 1.00 34.87 ? 573 HIS A CE1 1 ATOM 4309 N NE2 . HIS A 1 532 ? 23.860 36.653 55.745 1.00 35.09 ? 573 HIS A NE2 1 ATOM 4310 N N . LEU A 1 533 ? 25.362 39.352 61.662 1.00 29.06 ? 574 LEU A N 1 ATOM 4311 C CA . LEU A 1 533 ? 24.977 39.862 62.986 1.00 29.10 ? 574 LEU A CA 1 ATOM 4312 C C . LEU A 1 533 ? 25.213 41.357 63.124 1.00 29.24 ? 574 LEU A C 1 ATOM 4313 O O . LEU A 1 533 ? 24.343 42.078 63.649 1.00 28.65 ? 574 LEU A O 1 ATOM 4314 C CB . LEU A 1 533 ? 25.714 39.100 64.119 1.00 30.83 ? 574 LEU A CB 1 ATOM 4315 C CG . LEU A 1 533 ? 25.374 39.610 65.557 1.00 32.14 ? 574 LEU A CG 1 ATOM 4316 C CD1 . LEU A 1 533 ? 23.899 39.369 65.816 1.00 32.16 ? 574 LEU A CD1 1 ATOM 4317 C CD2 . LEU A 1 533 ? 26.245 38.789 66.531 1.00 32.36 ? 574 LEU A CD2 1 ATOM 4318 N N . THR A 1 534 ? 26.366 41.836 62.664 1.00 28.36 ? 575 THR A N 1 ATOM 4319 C CA . THR A 1 534 ? 26.629 43.281 62.654 1.00 28.74 ? 575 THR A CA 1 ATOM 4320 C C . THR A 1 534 ? 25.555 44.030 61.887 1.00 27.18 ? 575 THR A C 1 ATOM 4321 O O . THR A 1 534 ? 25.053 45.065 62.338 1.00 28.03 ? 575 THR A O 1 ATOM 4322 C CB . THR A 1 534 ? 28.039 43.585 62.077 1.00 28.70 ? 575 THR A CB 1 ATOM 4323 O OG1 . THR A 1 534 ? 29.018 43.034 62.971 1.00 31.25 ? 575 THR A OG1 1 ATOM 4324 C CG2 . THR A 1 534 ? 28.286 45.081 61.920 1.00 28.20 ? 575 THR A CG2 1 ATOM 4325 N N . VAL A 1 535 ? 25.163 43.518 60.726 1.00 27.17 ? 576 VAL A N 1 ATOM 4326 C CA . VAL A 1 535 ? 24.129 44.211 59.965 1.00 24.97 ? 576 VAL A CA 1 ATOM 4327 C C . VAL A 1 535 ? 22.772 44.149 60.677 1.00 25.03 ? 576 VAL A C 1 ATOM 4328 O O . VAL A 1 535 ? 22.019 45.124 60.624 1.00 26.78 ? 576 VAL A O 1 ATOM 4329 C CB . VAL A 1 535 ? 24.045 43.673 58.514 1.00 25.11 ? 576 VAL A CB 1 ATOM 4330 C CG1 . VAL A 1 535 ? 22.827 44.296 57.721 1.00 23.40 ? 576 VAL A CG1 1 ATOM 4331 C CG2 . VAL A 1 535 ? 25.369 43.997 57.765 1.00 25.38 ? 576 VAL A CG2 1 ATOM 4332 N N . ALA A 1 536 ? 22.443 43.036 61.314 1.00 25.33 ? 577 ALA A N 1 ATOM 4333 C CA . ALA A 1 536 ? 21.219 42.982 62.127 1.00 26.27 ? 577 ALA A CA 1 ATOM 4334 C C . ALA A 1 536 ? 21.238 44.009 63.265 1.00 27.23 ? 577 ALA A C 1 ATOM 4335 O O . ALA A 1 536 ? 20.220 44.641 63.558 1.00 26.29 ? 577 ALA A O 1 ATOM 4336 C CB . ALA A 1 536 ? 21.043 41.557 62.681 1.00 26.47 ? 577 ALA A CB 1 ATOM 4337 N N . GLN A 1 537 ? 22.397 44.180 63.896 1.00 27.88 ? 578 GLN A N 1 ATOM 4338 C CA . GLN A 1 537 ? 22.571 45.243 64.915 1.00 27.95 ? 578 GLN A CA 1 ATOM 4339 C C . GLN A 1 537 ? 22.408 46.657 64.366 1.00 28.45 ? 578 GLN A C 1 ATOM 4340 O O . GLN A 1 537 ? 21.827 47.525 65.048 1.00 28.60 ? 578 GLN A O 1 ATOM 4341 C CB . GLN A 1 537 ? 23.919 45.100 65.647 1.00 30.02 ? 578 GLN A CB 1 ATOM 4342 C CG . GLN A 1 537 ? 24.067 43.801 66.446 1.00 30.31 ? 578 GLN A CG 1 ATOM 4343 C CD . GLN A 1 537 ? 25.464 43.616 67.008 1.00 34.92 ? 578 GLN A CD 1 ATOM 4344 O OE1 . GLN A 1 537 ? 26.345 44.464 66.815 1.00 33.03 ? 578 GLN A OE1 1 ATOM 4345 N NE2 . GLN A 1 537 ? 25.680 42.490 67.699 1.00 35.17 ? 578 GLN A NE2 1 ATOM 4346 N N . VAL A 1 538 ? 22.923 46.922 63.163 1.00 26.75 ? 579 VAL A N 1 ATOM 4347 C CA . VAL A 1 538 ? 22.760 48.241 62.552 1.00 26.86 ? 579 VAL A CA 1 ATOM 4348 C C . VAL A 1 538 ? 21.284 48.465 62.165 1.00 25.77 ? 579 VAL A C 1 ATOM 4349 O O . VAL A 1 538 ? 20.668 49.491 62.511 1.00 26.30 ? 579 VAL A O 1 ATOM 4350 C CB . VAL A 1 538 ? 23.660 48.424 61.297 1.00 26.19 ? 579 VAL A CB 1 ATOM 4351 C CG1 . VAL A 1 538 ? 23.361 49.807 60.609 1.00 26.34 ? 579 VAL A CG1 1 ATOM 4352 C CG2 . VAL A 1 538 ? 25.139 48.360 61.678 1.00 28.47 ? 579 VAL A CG2 1 ATOM 4353 N N . ARG A 1 539 ? 20.709 47.529 61.413 1.00 26.01 ? 580 ARG A N 1 ATOM 4354 C CA . ARG A 1 539 ? 19.317 47.752 60.965 1.00 25.07 ? 580 ARG A CA 1 ATOM 4355 C C . ARG A 1 539 ? 18.356 47.746 62.153 1.00 26.36 ? 580 ARG A C 1 ATOM 4356 O O . ARG A 1 539 ? 17.447 48.607 62.280 1.00 26.17 ? 580 ARG A O 1 ATOM 4357 C CB . ARG A 1 539 ? 18.892 46.673 59.967 1.00 24.86 ? 580 ARG A CB 1 ATOM 4358 C CG . ARG A 1 539 ? 19.676 46.733 58.669 1.00 25.74 ? 580 ARG A CG 1 ATOM 4359 C CD . ARG A 1 539 ? 19.374 45.486 57.799 1.00 27.03 ? 580 ARG A CD 1 ATOM 4360 N NE . ARG A 1 539 ? 20.063 45.595 56.515 1.00 26.11 ? 580 ARG A NE 1 ATOM 4361 C CZ . ARG A 1 539 ? 19.997 44.676 55.552 1.00 27.11 ? 580 ARG A CZ 1 ATOM 4362 N NH1 . ARG A 1 539 ? 19.303 43.560 55.734 1.00 26.57 ? 580 ARG A NH1 1 ATOM 4363 N NH2 . ARG A 1 539 ? 20.620 44.886 54.403 1.00 24.88 ? 580 ARG A NH2 1 ATOM 4364 N N . GLY A 1 540 ? 18.504 46.724 62.982 1.00 26.26 ? 581 GLY A N 1 ATOM 4365 C CA . GLY A 1 540 ? 17.673 46.577 64.186 1.00 28.29 ? 581 GLY A CA 1 ATOM 4366 C C . GLY A 1 540 ? 17.845 47.749 65.147 1.00 27.92 ? 581 GLY A C 1 ATOM 4367 O O . GLY A 1 540 ? 16.836 48.297 65.685 1.00 28.02 ? 581 GLY A O 1 ATOM 4368 N N . GLY A 1 541 ? 19.097 48.149 65.365 1.00 28.12 ? 582 GLY A N 1 ATOM 4369 C CA . GLY A 1 541 ? 19.403 49.332 66.202 1.00 27.92 ? 582 GLY A CA 1 ATOM 4370 C C . GLY A 1 541 ? 18.758 50.619 65.699 1.00 27.38 ? 582 GLY A C 1 ATOM 4371 O O . GLY A 1 541 ? 18.262 51.446 66.522 1.00 27.79 ? 582 GLY A O 1 ATOM 4372 N N . MET A 1 542 ? 18.782 50.830 64.374 1.00 27.44 ? 583 MET A N 1 ATOM 4373 C CA A MET A 1 542 ? 18.145 52.012 63.806 0.50 26.08 ? 583 MET A CA 1 ATOM 4374 C CA B MET A 1 542 ? 18.145 52.000 63.777 0.50 27.29 ? 583 MET A CA 1 ATOM 4375 C C . MET A 1 542 ? 16.649 51.971 64.066 1.00 26.12 ? 583 MET A C 1 ATOM 4376 O O . MET A 1 542 ? 16.056 52.958 64.522 1.00 25.48 ? 583 MET A O 1 ATOM 4377 C CB A MET A 1 542 ? 18.434 52.143 62.304 0.50 25.19 ? 583 MET A CB 1 ATOM 4378 C CB B MET A 1 542 ? 18.398 52.037 62.259 0.50 27.23 ? 583 MET A CB 1 ATOM 4379 C CG A MET A 1 542 ? 19.848 52.607 62.046 0.50 24.97 ? 583 MET A CG 1 ATOM 4380 C CG B MET A 1 542 ? 19.878 52.138 61.923 0.50 32.49 ? 583 MET A CG 1 ATOM 4381 S SD A MET A 1 542 ? 20.256 52.586 60.288 0.50 21.36 ? 583 MET A SD 1 ATOM 4382 S SD B MET A 1 542 ? 20.481 53.814 62.045 0.50 43.45 ? 583 MET A SD 1 ATOM 4383 C CE A MET A 1 542 ? 19.521 54.106 59.705 0.50 23.63 ? 583 MET A CE 1 ATOM 4384 C CE B MET A 1 542 ? 19.571 54.504 60.654 0.50 38.42 ? 583 MET A CE 1 ATOM 4385 N N . VAL A 1 543 ? 16.033 50.819 63.789 1.00 26.26 ? 584 VAL A N 1 ATOM 4386 C CA . VAL A 1 543 ? 14.602 50.687 63.983 1.00 26.57 ? 584 VAL A CA 1 ATOM 4387 C C . VAL A 1 543 ? 14.276 50.911 65.480 1.00 26.87 ? 584 VAL A C 1 ATOM 4388 O O . VAL A 1 543 ? 13.309 51.626 65.796 1.00 26.29 ? 584 VAL A O 1 ATOM 4389 C CB . VAL A 1 543 ? 14.130 49.265 63.568 1.00 27.13 ? 584 VAL A CB 1 ATOM 4390 C CG1 . VAL A 1 543 ? 12.694 48.974 64.091 1.00 26.43 ? 584 VAL A CG1 1 ATOM 4391 C CG2 . VAL A 1 543 ? 14.218 49.061 62.044 1.00 26.00 ? 584 VAL A CG2 1 ATOM 4392 N N . PHE A 1 544 ? 15.084 50.331 66.392 1.00 27.12 ? 585 PHE A N 1 ATOM 4393 C CA . PHE A 1 544 ? 14.851 50.508 67.843 1.00 27.77 ? 585 PHE A CA 1 ATOM 4394 C C . PHE A 1 544 ? 14.892 51.995 68.225 1.00 28.22 ? 585 PHE A C 1 ATOM 4395 O O . PHE A 1 544 ? 13.986 52.487 68.925 1.00 29.29 ? 585 PHE A O 1 ATOM 4396 C CB . PHE A 1 544 ? 15.914 49.733 68.677 1.00 29.23 ? 585 PHE A CB 1 ATOM 4397 C CG . PHE A 1 544 ? 15.610 49.701 70.150 1.00 30.42 ? 585 PHE A CG 1 ATOM 4398 C CD1 . PHE A 1 544 ? 15.080 48.563 70.696 1.00 31.45 ? 585 PHE A CD1 1 ATOM 4399 C CD2 . PHE A 1 544 ? 15.822 50.823 70.964 1.00 32.18 ? 585 PHE A CD2 1 ATOM 4400 C CE1 . PHE A 1 544 ? 14.750 48.515 72.066 1.00 30.96 ? 585 PHE A CE1 1 ATOM 4401 C CE2 . PHE A 1 544 ? 15.504 50.795 72.337 1.00 31.41 ? 585 PHE A CE2 1 ATOM 4402 C CZ . PHE A 1 544 ? 14.981 49.632 72.874 1.00 31.16 ? 585 PHE A CZ 1 ATOM 4403 N N . GLU A 1 545 ? 15.912 52.718 67.777 1.00 27.31 ? 586 GLU A N 1 ATOM 4404 C CA . GLU A 1 545 ? 16.012 54.137 68.133 1.00 30.21 ? 586 GLU A CA 1 ATOM 4405 C C . GLU A 1 545 ? 14.859 54.965 67.531 1.00 28.02 ? 586 GLU A C 1 ATOM 4406 O O . GLU A 1 545 ? 14.302 55.842 68.193 1.00 28.61 ? 586 GLU A O 1 ATOM 4407 C CB . GLU A 1 545 ? 17.326 54.739 67.653 1.00 31.83 ? 586 GLU A CB 1 ATOM 4408 C CG . GLU A 1 545 ? 18.507 54.498 68.533 1.00 41.14 ? 586 GLU A CG 1 ATOM 4409 C CD . GLU A 1 545 ? 18.251 55.026 70.004 1.00 46.80 ? 586 GLU A CD 1 ATOM 4410 O OE1 . GLU A 1 545 ? 17.970 54.186 70.867 1.00 50.71 ? 586 GLU A OE1 1 ATOM 4411 O OE2 . GLU A 1 545 ? 18.248 56.255 70.263 1.00 52.40 ? 586 GLU A OE2 1 ATOM 4412 N N . LEU A 1 546 ? 14.471 54.646 66.299 1.00 27.11 ? 587 LEU A N 1 ATOM 4413 C CA . LEU A 1 546 ? 13.429 55.407 65.599 1.00 26.29 ? 587 LEU A CA 1 ATOM 4414 C C . LEU A 1 546 ? 12.111 55.151 66.312 1.00 27.65 ? 587 LEU A C 1 ATOM 4415 O O . LEU A 1 546 ? 11.266 56.064 66.443 1.00 27.96 ? 587 LEU A O 1 ATOM 4416 C CB . LEU A 1 546 ? 13.339 54.961 64.110 1.00 27.07 ? 587 LEU A CB 1 ATOM 4417 C CG . LEU A 1 546 ? 14.527 55.421 63.254 1.00 25.34 ? 587 LEU A CG 1 ATOM 4418 C CD1 . LEU A 1 546 ? 14.616 54.501 62.019 1.00 22.75 ? 587 LEU A CD1 1 ATOM 4419 C CD2 . LEU A 1 546 ? 14.295 56.893 62.808 1.00 28.18 ? 587 LEU A CD2 1 ATOM 4420 N N . ALA A 1 547 ? 11.931 53.922 66.815 1.00 26.22 ? 588 ALA A N 1 ATOM 4421 C CA . ALA A 1 547 ? 10.663 53.569 67.419 1.00 27.64 ? 588 ALA A CA 1 ATOM 4422 C C . ALA A 1 547 ? 10.591 53.916 68.903 1.00 28.39 ? 588 ALA A C 1 ATOM 4423 O O . ALA A 1 547 ? 9.495 53.916 69.441 1.00 29.90 ? 588 ALA A O 1 ATOM 4424 C CB . ALA A 1 547 ? 10.329 52.125 67.229 1.00 26.40 ? 588 ALA A CB 1 ATOM 4425 N N . ASN A 1 548 ? 11.734 54.166 69.536 1.00 28.99 ? 589 ASN A N 1 ATOM 4426 C CA . ASN A 1 548 ? 11.739 54.352 71.014 1.00 29.79 ? 589 ASN A CA 1 ATOM 4427 C C . ASN A 1 548 ? 12.251 55.673 71.554 1.00 32.10 ? 589 ASN A C 1 ATOM 4428 O O . ASN A 1 548 ? 11.910 56.042 72.704 1.00 32.28 ? 589 ASN A O 1 ATOM 4429 C CB . ASN A 1 548 ? 12.509 53.203 71.674 1.00 29.72 ? 589 ASN A CB 1 ATOM 4430 C CG A ASN A 1 548 ? 11.819 52.683 72.885 0.50 33.06 ? 589 ASN A CG 1 ATOM 4431 C CG B ASN A 1 548 ? 11.789 51.892 71.551 0.50 28.52 ? 589 ASN A CG 1 ATOM 4432 O OD1 A ASN A 1 548 ? 10.620 52.410 72.852 0.50 34.67 ? 589 ASN A OD1 1 ATOM 4433 O OD1 B ASN A 1 548 ? 12.154 51.037 70.741 0.50 31.30 ? 589 ASN A OD1 1 ATOM 4434 N ND2 A ASN A 1 548 ? 12.570 52.527 73.978 0.50 34.46 ? 589 ASN A ND2 1 ATOM 4435 N ND2 B ASN A 1 548 ? 10.723 51.742 72.300 0.50 25.87 ? 589 ASN A ND2 1 ATOM 4436 N N . SER A 1 549 ? 13.052 56.415 70.781 1.00 30.40 ? 590 SER A N 1 ATOM 4437 C CA A SER A 1 549 ? 13.588 57.688 71.270 0.50 30.67 ? 590 SER A CA 1 ATOM 4438 C CA B SER A 1 549 ? 13.578 57.681 71.301 0.50 31.69 ? 590 SER A CA 1 ATOM 4439 C C . SER A 1 549 ? 12.437 58.643 71.516 1.00 31.18 ? 590 SER A C 1 ATOM 4440 O O . SER A 1 549 ? 11.523 58.762 70.673 1.00 30.02 ? 590 SER A O 1 ATOM 4441 C CB A SER A 1 549 ? 14.524 58.319 70.231 0.50 30.93 ? 590 SER A CB 1 ATOM 4442 C CB B SER A 1 549 ? 14.565 58.323 70.333 0.50 32.27 ? 590 SER A CB 1 ATOM 4443 O OG A SER A 1 549 ? 15.227 59.415 70.786 0.50 28.53 ? 590 SER A OG 1 ATOM 4444 O OG B SER A 1 549 ? 15.617 57.431 70.056 0.50 35.32 ? 590 SER A OG 1 ATOM 4445 N N . ILE A 1 550 ? 12.502 59.365 72.613 1.00 30.37 ? 591 ILE A N 1 ATOM 4446 C CA . ILE A 1 550 ? 11.448 60.316 72.888 1.00 31.20 ? 591 ILE A CA 1 ATOM 4447 C C . ILE A 1 550 ? 11.371 61.400 71.842 1.00 29.15 ? 591 ILE A C 1 ATOM 4448 O O . ILE A 1 550 ? 10.285 61.701 71.318 1.00 28.81 ? 591 ILE A O 1 ATOM 4449 C CB . ILE A 1 550 ? 11.741 60.962 74.279 1.00 30.84 ? 591 ILE A CB 1 ATOM 4450 C CG1 . ILE A 1 550 ? 11.730 59.873 75.361 1.00 37.91 ? 591 ILE A CG1 1 ATOM 4451 C CG2 . ILE A 1 550 ? 10.758 62.049 74.568 1.00 34.83 ? 591 ILE A CG2 1 ATOM 4452 C CD1 . ILE A 1 550 ? 10.447 59.050 75.401 1.00 41.27 ? 591 ILE A CD1 1 ATOM 4453 N N . VAL A 1 551 ? 12.510 62.016 71.565 1.00 30.20 ? 592 VAL A N 1 ATOM 4454 C CA . VAL A 1 551 ? 12.588 62.937 70.431 1.00 30.01 ? 592 VAL A CA 1 ATOM 4455 C C . VAL A 1 551 ? 13.056 62.105 69.225 1.00 30.09 ? 592 VAL A C 1 ATOM 4456 O O . VAL A 1 551 ? 14.051 61.392 69.318 1.00 29.88 ? 592 VAL A O 1 ATOM 4457 C CB . VAL A 1 551 ? 13.540 64.092 70.714 1.00 31.23 ? 592 VAL A CB 1 ATOM 4458 C CG1 . VAL A 1 551 ? 13.667 65.007 69.466 1.00 32.48 ? 592 VAL A CG1 1 ATOM 4459 C CG2 . VAL A 1 551 ? 12.988 64.899 71.894 1.00 33.16 ? 592 VAL A CG2 1 ATOM 4460 N N . LEU A 1 552 ? 12.357 62.215 68.098 1.00 29.87 ? 593 LEU A N 1 ATOM 4461 C CA . LEU A 1 552 ? 12.797 61.485 66.855 1.00 28.91 ? 593 LEU A CA 1 ATOM 4462 C C . LEU A 1 552 ? 14.278 61.750 66.582 1.00 29.39 ? 593 LEU A C 1 ATOM 4463 O O . LEU A 1 552 ? 14.739 62.905 66.696 1.00 29.59 ? 593 LEU A O 1 ATOM 4464 C CB . LEU A 1 552 ? 11.900 61.843 65.647 1.00 28.63 ? 593 LEU A CB 1 ATOM 4465 C CG . LEU A 1 552 ? 10.523 61.202 65.629 1.00 30.59 ? 593 LEU A CG 1 ATOM 4466 C CD1 . LEU A 1 552 ? 9.713 61.794 64.471 1.00 29.87 ? 593 LEU A CD1 1 ATOM 4467 C CD2 . LEU A 1 552 ? 10.649 59.674 65.478 1.00 31.37 ? 593 LEU A CD2 1 ATOM 4468 N N . PRO A 1 553 ? 15.056 60.682 66.254 1.00 28.75 ? 594 PRO A N 1 ATOM 4469 C CA . PRO A 1 553 ? 16.504 60.836 66.157 1.00 30.21 ? 594 PRO A CA 1 ATOM 4470 C C . PRO A 1 553 ? 16.977 61.379 64.783 1.00 30.83 ? 594 PRO A C 1 ATOM 4471 O O . PRO A 1 553 ? 17.824 60.753 64.102 1.00 31.27 ? 594 PRO A O 1 ATOM 4472 C CB . PRO A 1 553 ? 17.029 59.395 66.404 1.00 30.65 ? 594 PRO A CB 1 ATOM 4473 C CG . PRO A 1 553 ? 15.965 58.539 65.719 1.00 28.32 ? 594 PRO A CG 1 ATOM 4474 C CD . PRO A 1 553 ? 14.637 59.282 66.098 1.00 28.47 ? 594 PRO A CD 1 ATOM 4475 N N . PHE A 1 554 ? 16.399 62.504 64.377 1.00 29.52 ? 595 PHE A N 1 ATOM 4476 C CA . PHE A 1 554 ? 16.709 63.154 63.080 1.00 29.10 ? 595 PHE A CA 1 ATOM 4477 C C . PHE A 1 554 ? 17.396 64.492 63.354 1.00 30.70 ? 595 PHE A C 1 ATOM 4478 O O . PHE A 1 554 ? 16.968 65.218 64.282 1.00 32.53 ? 595 PHE A O 1 ATOM 4479 C CB . PHE A 1 554 ? 15.398 63.502 62.352 1.00 26.69 ? 595 PHE A CB 1 ATOM 4480 C CG . PHE A 1 554 ? 14.612 62.318 61.846 1.00 26.28 ? 595 PHE A CG 1 ATOM 4481 C CD1 . PHE A 1 554 ? 15.223 61.095 61.575 1.00 25.47 ? 595 PHE A CD1 1 ATOM 4482 C CD2 . PHE A 1 554 ? 13.247 62.469 61.560 1.00 26.62 ? 595 PHE A CD2 1 ATOM 4483 C CE1 . PHE A 1 554 ? 14.469 60.004 61.035 1.00 26.53 ? 595 PHE A CE1 1 ATOM 4484 C CE2 . PHE A 1 554 ? 12.482 61.376 61.023 1.00 28.40 ? 595 PHE A CE2 1 ATOM 4485 C CZ . PHE A 1 554 ? 13.093 60.171 60.767 1.00 25.45 ? 595 PHE A CZ 1 ATOM 4486 N N . ASP A 1 555 ? 18.422 64.837 62.579 1.00 29.42 ? 596 ASP A N 1 ATOM 4487 C CA . ASP A 1 555 ? 19.081 66.124 62.747 1.00 29.88 ? 596 ASP A CA 1 ATOM 4488 C C . ASP A 1 555 ? 18.910 66.948 61.473 1.00 29.44 ? 596 ASP A C 1 ATOM 4489 O O . ASP A 1 555 ? 19.606 66.690 60.459 1.00 29.62 ? 596 ASP A O 1 ATOM 4490 C CB . ASP A 1 555 ? 20.565 65.968 63.045 1.00 30.19 ? 596 ASP A CB 1 ATOM 4491 C CG . ASP A 1 555 ? 21.182 67.270 63.554 1.00 34.57 ? 596 ASP A CG 1 ATOM 4492 O OD1 . ASP A 1 555 ? 20.589 68.377 63.364 1.00 33.95 ? 596 ASP A OD1 1 ATOM 4493 O OD2 . ASP A 1 555 ? 22.246 67.196 64.231 1.00 38.57 ? 596 ASP A OD2 1 ATOM 4494 N N . CYS A 1 556 ? 17.968 67.895 61.503 1.00 28.13 ? 597 CYS A N 1 ATOM 4495 C CA . CYS A 1 556 ? 17.746 68.753 60.326 1.00 29.07 ? 597 CYS A CA 1 ATOM 4496 C C . CYS A 1 556 ? 18.959 69.528 59.868 1.00 28.71 ? 597 CYS A C 1 ATOM 4497 O O . CYS A 1 556 ? 19.041 69.861 58.686 1.00 29.04 ? 597 CYS A O 1 ATOM 4498 C CB . CYS A 1 556 ? 16.569 69.715 60.560 1.00 29.43 ? 597 CYS A CB 1 ATOM 4499 S SG . CYS A 1 556 ? 16.843 70.810 62.031 1.00 35.34 ? 597 CYS A SG 1 ATOM 4500 N N . ARG A 1 557 ? 19.903 69.832 60.762 1.00 28.35 ? 598 ARG A N 1 ATOM 4501 C CA . ARG A 1 557 ? 21.119 70.577 60.364 1.00 29.80 ? 598 ARG A CA 1 ATOM 4502 C C . ARG A 1 557 ? 21.962 69.788 59.332 1.00 30.41 ? 598 ARG A C 1 ATOM 4503 O O . ARG A 1 557 ? 22.686 70.388 58.500 1.00 31.57 ? 598 ARG A O 1 ATOM 4504 C CB . ARG A 1 557 ? 21.979 70.903 61.595 1.00 29.85 ? 598 ARG A CB 1 ATOM 4505 C CG . ARG A 1 557 ? 21.259 71.906 62.524 1.00 30.67 ? 598 ARG A CG 1 ATOM 4506 C CD . ARG A 1 557 ? 21.997 72.033 63.908 1.00 30.84 ? 598 ARG A CD 1 ATOM 4507 N NE . ARG A 1 557 ? 22.115 70.715 64.544 1.00 35.87 ? 598 ARG A NE 1 ATOM 4508 C CZ . ARG A 1 557 ? 22.802 70.502 65.676 1.00 42.33 ? 598 ARG A CZ 1 ATOM 4509 N NH1 . ARG A 1 557 ? 23.382 71.519 66.276 1.00 39.76 ? 598 ARG A NH1 1 ATOM 4510 N NH2 . ARG A 1 557 ? 22.892 69.294 66.212 1.00 38.36 ? 598 ARG A NH2 1 ATOM 4511 N N . ASP A 1 558 ? 21.859 68.458 59.371 1.00 29.83 ? 599 ASP A N 1 ATOM 4512 C CA . ASP A 1 558 ? 22.609 67.624 58.418 1.00 29.51 ? 599 ASP A CA 1 ATOM 4513 C C . ASP A 1 558 ? 22.019 67.789 56.977 1.00 28.14 ? 599 ASP A C 1 ATOM 4514 O O . ASP A 1 558 ? 22.736 67.741 55.997 1.00 28.42 ? 599 ASP A O 1 ATOM 4515 C CB . ASP A 1 558 ? 22.604 66.140 58.835 1.00 28.82 ? 599 ASP A CB 1 ATOM 4516 C CG . ASP A 1 558 ? 23.569 65.865 60.017 1.00 35.29 ? 599 ASP A CG 1 ATOM 4517 O OD1 . ASP A 1 558 ? 24.617 66.515 60.079 1.00 42.87 ? 599 ASP A OD1 1 ATOM 4518 O OD2 . ASP A 1 558 ? 23.270 65.041 60.884 1.00 37.78 ? 599 ASP A OD2 1 ATOM 4519 N N . TYR A 1 559 ? 20.729 68.057 56.878 1.00 27.13 ? 600 TYR A N 1 ATOM 4520 C CA . TYR A 1 559 ? 20.147 68.321 55.563 1.00 26.70 ? 600 TYR A CA 1 ATOM 4521 C C . TYR A 1 559 ? 20.676 69.653 55.058 1.00 27.58 ? 600 TYR A C 1 ATOM 4522 O O . TYR A 1 559 ? 20.941 69.804 53.856 1.00 27.34 ? 600 TYR A O 1 ATOM 4523 C CB . TYR A 1 559 ? 18.617 68.380 55.621 1.00 25.32 ? 600 TYR A CB 1 ATOM 4524 C CG . TYR A 1 559 ? 17.953 67.410 54.623 1.00 25.58 ? 600 TYR A CG 1 ATOM 4525 C CD1 . TYR A 1 559 ? 18.285 67.449 53.271 1.00 26.86 ? 600 TYR A CD1 1 ATOM 4526 C CD2 . TYR A 1 559 ? 16.985 66.504 55.041 1.00 26.26 ? 600 TYR A CD2 1 ATOM 4527 C CE1 . TYR A 1 559 ? 17.660 66.576 52.349 1.00 25.08 ? 600 TYR A CE1 1 ATOM 4528 C CE2 . TYR A 1 559 ? 16.368 65.618 54.129 1.00 26.28 ? 600 TYR A CE2 1 ATOM 4529 C CZ . TYR A 1 559 ? 16.710 65.685 52.786 1.00 26.04 ? 600 TYR A CZ 1 ATOM 4530 O OH . TYR A 1 559 ? 16.094 64.823 51.902 1.00 27.23 ? 600 TYR A OH 1 ATOM 4531 N N . ALA A 1 560 ? 20.795 70.634 55.947 1.00 27.78 ? 601 ALA A N 1 ATOM 4532 C CA . ALA A 1 560 ? 21.242 71.964 55.519 1.00 28.19 ? 601 ALA A CA 1 ATOM 4533 C C . ALA A 1 560 ? 22.663 71.872 54.912 1.00 28.39 ? 601 ALA A C 1 ATOM 4534 O O . ALA A 1 560 ? 22.962 72.507 53.876 1.00 28.87 ? 601 ALA A O 1 ATOM 4535 C CB . ALA A 1 560 ? 21.225 72.964 56.697 1.00 27.79 ? 601 ALA A CB 1 ATOM 4536 N N . VAL A 1 561 ? 23.551 71.133 55.579 1.00 28.95 ? 602 VAL A N 1 ATOM 4537 C CA . VAL A 1 561 ? 24.893 70.878 55.061 1.00 29.52 ? 602 VAL A CA 1 ATOM 4538 C C . VAL A 1 561 ? 24.877 70.287 53.626 1.00 28.67 ? 602 VAL A C 1 ATOM 4539 O O . VAL A 1 561 ? 25.556 70.825 52.740 1.00 28.86 ? 602 VAL A O 1 ATOM 4540 C CB . VAL A 1 561 ? 25.739 69.952 56.001 1.00 30.09 ? 602 VAL A CB 1 ATOM 4541 C CG1 . VAL A 1 561 ? 27.155 69.665 55.360 1.00 34.48 ? 602 VAL A CG1 1 ATOM 4542 C CG2 . VAL A 1 561 ? 25.922 70.675 57.327 1.00 34.06 ? 602 VAL A CG2 1 ATOM 4543 N N . VAL A 1 562 ? 24.119 69.204 53.409 1.00 27.28 ? 603 VAL A N 1 ATOM 4544 C CA . VAL A 1 562 ? 24.134 68.569 52.076 1.00 28.26 ? 603 VAL A CA 1 ATOM 4545 C C . VAL A 1 562 ? 23.446 69.422 51.017 1.00 26.81 ? 603 VAL A C 1 ATOM 4546 O O . VAL A 1 562 ? 23.878 69.409 49.861 1.00 25.95 ? 603 VAL A O 1 ATOM 4547 C CB . VAL A 1 562 ? 23.621 67.109 52.032 1.00 27.88 ? 603 VAL A CB 1 ATOM 4548 C CG1 . VAL A 1 562 ? 24.386 66.225 53.051 1.00 30.85 ? 603 VAL A CG1 1 ATOM 4549 C CG2 . VAL A 1 562 ? 22.151 67.025 52.183 1.00 30.88 ? 603 VAL A CG2 1 ATOM 4550 N N . LEU A 1 563 ? 22.433 70.199 51.419 1.00 24.55 ? 604 LEU A N 1 ATOM 4551 C CA . LEU A 1 563 ? 21.726 71.027 50.426 1.00 25.65 ? 604 LEU A CA 1 ATOM 4552 C C . LEU A 1 563 ? 22.710 72.045 49.850 1.00 27.08 ? 604 LEU A C 1 ATOM 4553 O O . LEU A 1 563 ? 22.661 72.348 48.641 1.00 27.69 ? 604 LEU A O 1 ATOM 4554 C CB . LEU A 1 563 ? 20.523 71.757 51.055 1.00 24.59 ? 604 LEU A CB 1 ATOM 4555 C CG . LEU A 1 563 ? 19.312 70.816 51.288 1.00 24.21 ? 604 LEU A CG 1 ATOM 4556 C CD1 . LEU A 1 563 ? 18.240 71.536 52.158 1.00 27.66 ? 604 LEU A CD1 1 ATOM 4557 C CD2 . LEU A 1 563 ? 18.627 70.346 49.971 1.00 26.41 ? 604 LEU A CD2 1 ATOM 4558 N N . ARG A 1 564 ? 23.612 72.571 50.687 1.00 27.53 ? 605 ARG A N 1 ATOM 4559 C CA . ARG A 1 564 ? 24.641 73.506 50.157 1.00 29.00 ? 605 ARG A CA 1 ATOM 4560 C C . ARG A 1 564 ? 25.602 72.830 49.182 1.00 28.68 ? 605 ARG A C 1 ATOM 4561 O O . ARG A 1 564 ? 25.933 73.395 48.135 1.00 28.71 ? 605 ARG A O 1 ATOM 4562 C CB . ARG A 1 564 ? 25.426 74.191 51.302 1.00 30.01 ? 605 ARG A CB 1 ATOM 4563 C CG . ARG A 1 564 ? 26.564 75.124 50.818 1.00 35.08 ? 605 ARG A CG 1 ATOM 4564 C CD . ARG A 1 564 ? 26.001 76.240 49.879 1.00 39.49 ? 605 ARG A CD 1 ATOM 4565 N NE . ARG A 1 564 ? 27.121 77.057 49.427 1.00 44.79 ? 605 ARG A NE 1 ATOM 4566 C CZ . ARG A 1 564 ? 27.578 78.125 50.071 1.00 50.29 ? 605 ARG A CZ 1 ATOM 4567 N NH1 . ARG A 1 564 ? 27.006 78.538 51.212 1.00 48.36 ? 605 ARG A NH1 1 ATOM 4568 N NH2 . ARG A 1 564 ? 28.627 78.776 49.580 1.00 50.80 ? 605 ARG A NH2 1 ATOM 4569 N N A LYS A 1 565 ? 26.109 71.656 49.554 0.60 28.39 ? 606 LYS A N 1 ATOM 4570 N N B LYS A 1 565 ? 26.079 71.638 49.549 0.40 27.97 ? 606 LYS A N 1 ATOM 4571 C CA A LYS A 1 565 ? 26.926 70.840 48.671 0.60 28.97 ? 606 LYS A CA 1 ATOM 4572 C CA B LYS A 1 565 ? 26.916 70.813 48.683 0.40 27.89 ? 606 LYS A CA 1 ATOM 4573 C C A LYS A 1 565 ? 26.213 70.618 47.310 0.60 28.03 ? 606 LYS A C 1 ATOM 4574 C C B LYS A 1 565 ? 26.232 70.550 47.324 0.40 27.33 ? 606 LYS A C 1 ATOM 4575 O O A LYS A 1 565 ? 26.814 70.821 46.244 0.60 28.49 ? 606 LYS A O 1 ATOM 4576 O O B LYS A 1 565 ? 26.870 70.649 46.269 0.40 27.76 ? 606 LYS A O 1 ATOM 4577 C CB A LYS A 1 565 ? 27.194 69.481 49.356 0.60 29.53 ? 606 LYS A CB 1 ATOM 4578 C CB B LYS A 1 565 ? 27.207 69.466 49.377 0.40 28.07 ? 606 LYS A CB 1 ATOM 4579 C CG A LYS A 1 565 ? 28.157 68.563 48.626 0.60 32.23 ? 606 LYS A CG 1 ATOM 4580 C CG B LYS A 1 565 ? 27.786 69.593 50.783 0.40 27.37 ? 606 LYS A CG 1 ATOM 4581 C CD A LYS A 1 565 ? 28.483 67.305 49.482 0.60 35.71 ? 606 LYS A CD 1 ATOM 4582 C CD B LYS A 1 565 ? 29.254 69.206 50.833 0.40 33.31 ? 606 LYS A CD 1 ATOM 4583 C CE A LYS A 1 565 ? 27.245 66.399 49.612 0.60 36.14 ? 606 LYS A CE 1 ATOM 4584 C CE B LYS A 1 565 ? 29.890 69.460 52.199 0.40 30.21 ? 606 LYS A CE 1 ATOM 4585 N NZ A LYS A 1 565 ? 27.507 65.054 50.196 0.60 37.14 ? 606 LYS A NZ 1 ATOM 4586 N NZ B LYS A 1 565 ? 31.342 69.661 51.946 0.40 35.88 ? 606 LYS A NZ 1 ATOM 4587 N N . TYR A 1 566 ? 24.938 70.225 47.365 1.00 25.42 ? 607 TYR A N 1 ATOM 4588 C CA . TYR A 1 566 ? 24.174 69.883 46.132 1.00 25.53 ? 607 TYR A CA 1 ATOM 4589 C C . TYR A 1 566 ? 23.949 71.148 45.300 1.00 25.06 ? 607 TYR A C 1 ATOM 4590 O O . TYR A 1 566 ? 24.030 71.090 44.080 1.00 25.75 ? 607 TYR A O 1 ATOM 4591 C CB . TYR A 1 566 ? 22.815 69.282 46.429 1.00 23.99 ? 607 TYR A CB 1 ATOM 4592 C CG . TYR A 1 566 ? 22.863 67.954 47.197 1.00 24.54 ? 607 TYR A CG 1 ATOM 4593 C CD1 . TYR A 1 566 ? 24.029 67.160 47.198 1.00 26.09 ? 607 TYR A CD1 1 ATOM 4594 C CD2 . TYR A 1 566 ? 21.761 67.518 47.918 1.00 26.38 ? 607 TYR A CD2 1 ATOM 4595 C CE1 . TYR A 1 566 ? 24.074 65.952 47.932 1.00 26.91 ? 607 TYR A CE1 1 ATOM 4596 C CE2 . TYR A 1 566 ? 21.795 66.307 48.631 1.00 26.04 ? 607 TYR A CE2 1 ATOM 4597 C CZ . TYR A 1 566 ? 22.954 65.563 48.636 1.00 27.55 ? 607 TYR A CZ 1 ATOM 4598 O OH . TYR A 1 566 ? 22.972 64.396 49.329 1.00 29.65 ? 607 TYR A OH 1 ATOM 4599 N N . ALA A 1 567 ? 23.713 72.274 45.971 1.00 24.94 ? 608 ALA A N 1 ATOM 4600 C CA . ALA A 1 567 ? 23.559 73.526 45.241 1.00 26.45 ? 608 ALA A CA 1 ATOM 4601 C C . ALA A 1 567 ? 24.858 73.939 44.559 1.00 27.68 ? 608 ALA A C 1 ATOM 4602 O O . ALA A 1 567 ? 24.848 74.390 43.377 1.00 27.23 ? 608 ALA A O 1 ATOM 4603 C CB . ALA A 1 567 ? 23.113 74.631 46.170 1.00 27.17 ? 608 ALA A CB 1 ATOM 4604 N N . ASP A 1 568 ? 25.978 73.888 45.298 1.00 28.33 ? 609 ASP A N 1 ATOM 4605 C CA . ASP A 1 568 ? 27.291 74.167 44.686 1.00 30.78 ? 609 ASP A CA 1 ATOM 4606 C C . ASP A 1 568 ? 27.516 73.252 43.446 1.00 30.18 ? 609 ASP A C 1 ATOM 4607 O O . ASP A 1 568 ? 28.063 73.691 42.426 1.00 29.46 ? 609 ASP A O 1 ATOM 4608 C CB . ASP A 1 568 ? 28.443 73.854 45.657 1.00 30.81 ? 609 ASP A CB 1 ATOM 4609 C CG . ASP A 1 568 ? 28.567 74.826 46.808 1.00 37.10 ? 609 ASP A CG 1 ATOM 4610 O OD1 . ASP A 1 568 ? 28.089 75.962 46.744 1.00 41.21 ? 609 ASP A OD1 1 ATOM 4611 O OD2 . ASP A 1 568 ? 29.225 74.437 47.814 1.00 43.66 ? 609 ASP A OD2 1 ATOM 4612 N N . LYS A 1 569 ? 27.139 71.982 43.573 1.00 27.90 ? 610 LYS A N 1 ATOM 4613 C CA . LYS A 1 569 ? 27.391 71.016 42.523 1.00 29.19 ? 610 LYS A CA 1 ATOM 4614 C C . LYS A 1 569 ? 26.589 71.321 41.239 1.00 28.35 ? 610 LYS A C 1 ATOM 4615 O O . LYS A 1 569 ? 27.152 71.350 40.115 1.00 29.58 ? 610 LYS A O 1 ATOM 4616 C CB . LYS A 1 569 ? 27.057 69.594 43.022 1.00 28.65 ? 610 LYS A CB 1 ATOM 4617 C CG . LYS A 1 569 ? 27.417 68.552 42.007 1.00 33.92 ? 610 LYS A CG 1 ATOM 4618 C CD . LYS A 1 569 ? 26.847 67.242 42.458 1.00 40.23 ? 610 LYS A CD 1 ATOM 4619 C CE . LYS A 1 569 ? 27.562 66.055 41.837 1.00 47.15 ? 610 LYS A CE 1 ATOM 4620 N NZ . LYS A 1 569 ? 26.619 64.873 41.924 1.00 47.40 ? 610 LYS A NZ 1 ATOM 4621 N N . ILE A 1 570 ? 25.295 71.589 41.394 1.00 28.03 ? 611 ILE A N 1 ATOM 4622 C CA . ILE A 1 570 ? 24.429 71.866 40.231 1.00 27.36 ? 611 ILE A CA 1 ATOM 4623 C C . ILE A 1 570 ? 24.811 73.224 39.586 1.00 28.22 ? 611 ILE A C 1 ATOM 4624 O O . ILE A 1 570 ? 24.836 73.361 38.350 1.00 27.38 ? 611 ILE A O 1 ATOM 4625 C CB . ILE A 1 570 ? 22.937 71.785 40.585 1.00 27.09 ? 611 ILE A CB 1 ATOM 4626 C CG1 . ILE A 1 570 ? 22.102 71.768 39.293 1.00 28.54 ? 611 ILE A CG1 1 ATOM 4627 C CG2 . ILE A 1 570 ? 22.498 72.930 41.541 1.00 28.24 ? 611 ILE A CG2 1 ATOM 4628 C CD1 . ILE A 1 570 ? 22.206 70.394 38.574 1.00 26.38 ? 611 ILE A CD1 1 ATOM 4629 N N . TYR A 1 571 ? 25.148 74.202 40.429 1.00 27.27 ? 612 TYR A N 1 ATOM 4630 C CA . TYR A 1 571 ? 25.676 75.473 39.934 1.00 30.63 ? 612 TYR A CA 1 ATOM 4631 C C . TYR A 1 571 ? 26.930 75.233 39.067 1.00 30.94 ? 612 TYR A C 1 ATOM 4632 O O . TYR A 1 571 ? 27.087 75.818 37.962 1.00 31.11 ? 612 TYR A O 1 ATOM 4633 C CB . TYR A 1 571 ? 25.959 76.420 41.119 1.00 31.26 ? 612 TYR A CB 1 ATOM 4634 C CG . TYR A 1 571 ? 26.754 77.618 40.695 1.00 35.78 ? 612 TYR A CG 1 ATOM 4635 C CD1 . TYR A 1 571 ? 26.136 78.734 40.130 1.00 38.06 ? 612 TYR A CD1 1 ATOM 4636 C CD2 . TYR A 1 571 ? 28.141 77.606 40.823 1.00 41.95 ? 612 TYR A CD2 1 ATOM 4637 C CE1 . TYR A 1 571 ? 26.913 79.865 39.739 1.00 44.47 ? 612 TYR A CE1 1 ATOM 4638 C CE2 . TYR A 1 571 ? 28.926 78.699 40.424 1.00 47.27 ? 612 TYR A CE2 1 ATOM 4639 C CZ . TYR A 1 571 ? 28.301 79.808 39.877 1.00 48.52 ? 612 TYR A CZ 1 ATOM 4640 O OH . TYR A 1 571 ? 29.099 80.864 39.492 1.00 57.66 ? 612 TYR A OH 1 ATOM 4641 N N . SER A 1 572 ? 27.846 74.385 39.551 1.00 32.44 ? 613 SER A N 1 ATOM 4642 C CA . SER A 1 572 ? 29.079 74.103 38.797 1.00 33.70 ? 613 SER A CA 1 ATOM 4643 C C . SER A 1 572 ? 28.812 73.446 37.432 1.00 33.50 ? 613 SER A C 1 ATOM 4644 O O . SER A 1 572 ? 29.531 73.722 36.498 1.00 35.32 ? 613 SER A O 1 ATOM 4645 C CB . SER A 1 572 ? 30.089 73.264 39.599 1.00 34.42 ? 613 SER A CB 1 ATOM 4646 O OG A SER A 1 572 ? 30.571 73.992 40.721 0.50 36.19 ? 613 SER A OG 1 ATOM 4647 O OG B SER A 1 572 ? 29.586 71.986 39.863 0.50 35.02 ? 613 SER A OG 1 ATOM 4648 N N . ILE A 1 573 ? 27.806 72.566 37.347 1.00 32.37 ? 614 ILE A N 1 ATOM 4649 C CA . ILE A 1 573 ? 27.430 71.952 36.076 1.00 31.99 ? 614 ILE A CA 1 ATOM 4650 C C . ILE A 1 573 ? 26.919 72.997 35.095 1.00 33.41 ? 614 ILE A C 1 ATOM 4651 O O . ILE A 1 573 ? 27.332 73.024 33.939 1.00 32.85 ? 614 ILE A O 1 ATOM 4652 C CB . ILE A 1 573 ? 26.391 70.839 36.284 1.00 31.60 ? 614 ILE A CB 1 ATOM 4653 C CG1 . ILE A 1 573 ? 27.049 69.668 37.053 1.00 31.50 ? 614 ILE A CG1 1 ATOM 4654 C CG2 . ILE A 1 573 ? 25.794 70.354 34.909 1.00 31.53 ? 614 ILE A CG2 1 ATOM 4655 C CD1 . ILE A 1 573 ? 25.982 68.648 37.622 1.00 30.14 ? 614 ILE A CD1 1 ATOM 4656 N N . SER A 1 574 ? 26.053 73.881 35.581 1.00 31.26 ? 615 SER A N 1 ATOM 4657 C CA . SER A 1 574 ? 25.529 74.946 34.767 1.00 32.31 ? 615 SER A CA 1 ATOM 4658 C C . SER A 1 574 ? 26.606 75.870 34.277 1.00 33.72 ? 615 SER A C 1 ATOM 4659 O O . SER A 1 574 ? 26.571 76.305 33.116 1.00 33.01 ? 615 SER A O 1 ATOM 4660 C CB . SER A 1 574 ? 24.495 75.738 35.576 1.00 31.98 ? 615 SER A CB 1 ATOM 4661 O OG . SER A 1 574 ? 23.768 76.611 34.738 1.00 32.03 ? 615 SER A OG 1 ATOM 4662 N N . MET A 1 575 ? 27.571 76.162 35.154 1.00 33.97 ? 616 MET A N 1 ATOM 4663 C CA . MET A 1 575 ? 28.693 77.064 34.801 1.00 37.85 ? 616 MET A CA 1 ATOM 4664 C C . MET A 1 575 ? 29.685 76.507 33.766 1.00 39.04 ? 616 MET A C 1 ATOM 4665 O O . MET A 1 575 ? 30.630 77.189 33.372 1.00 39.73 ? 616 MET A O 1 ATOM 4666 C CB . MET A 1 575 ? 29.412 77.546 36.062 1.00 37.96 ? 616 MET A CB 1 ATOM 4667 C CG . MET A 1 575 ? 28.632 78.674 36.741 1.00 42.39 ? 616 MET A CG 1 ATOM 4668 S SD . MET A 1 575 ? 28.569 80.223 35.738 1.00 51.69 ? 616 MET A SD 1 ATOM 4669 C CE . MET A 1 575 ? 30.300 80.611 35.518 1.00 49.93 ? 616 MET A CE 1 ATOM 4670 N N . LYS A 1 576 ? 29.471 75.275 33.311 1.00 39.56 ? 617 LYS A N 1 ATOM 4671 C CA . LYS A 1 576 ? 30.170 74.831 32.091 1.00 40.53 ? 617 LYS A CA 1 ATOM 4672 C C . LYS A 1 576 ? 29.650 75.585 30.848 1.00 39.90 ? 617 LYS A C 1 ATOM 4673 O O . LYS A 1 576 ? 30.267 75.483 29.796 1.00 40.45 ? 617 LYS A O 1 ATOM 4674 C CB . LYS A 1 576 ? 30.012 73.324 31.853 1.00 41.85 ? 617 LYS A CB 1 ATOM 4675 C CG . LYS A 1 576 ? 30.572 72.393 32.955 1.00 46.47 ? 617 LYS A CG 1 ATOM 4676 C CD . LYS A 1 576 ? 30.595 70.882 32.487 1.00 53.43 ? 617 LYS A CD 1 ATOM 4677 C CE . LYS A 1 576 ? 29.340 70.045 32.868 1.00 54.22 ? 617 LYS A CE 1 ATOM 4678 N NZ . LYS A 1 576 ? 28.013 70.659 32.454 1.00 55.47 ? 617 LYS A NZ 1 ATOM 4679 N N . HIS A 1 577 ? 28.548 76.349 30.983 1.00 36.22 ? 618 HIS A N 1 ATOM 4680 C CA . HIS A 1 577 ? 27.908 77.095 29.865 1.00 35.61 ? 618 HIS A CA 1 ATOM 4681 C C . HIS A 1 577 ? 27.720 78.581 30.216 1.00 35.67 ? 618 HIS A C 1 ATOM 4682 O O . HIS A 1 577 ? 26.567 79.080 30.246 1.00 33.69 ? 618 HIS A O 1 ATOM 4683 C CB . HIS A 1 577 ? 26.519 76.520 29.559 1.00 34.54 ? 618 HIS A CB 1 ATOM 4684 C CG . HIS A 1 577 ? 26.488 75.022 29.472 1.00 36.15 ? 618 HIS A CG 1 ATOM 4685 N ND1 . HIS A 1 577 ? 26.761 74.342 28.308 1.00 40.39 ? 618 HIS A ND1 1 ATOM 4686 C CD2 . HIS A 1 577 ? 26.207 74.076 30.408 1.00 39.19 ? 618 HIS A CD2 1 ATOM 4687 C CE1 . HIS A 1 577 ? 26.672 73.038 28.528 1.00 41.49 ? 618 HIS A CE1 1 ATOM 4688 N NE2 . HIS A 1 577 ? 26.336 72.849 29.796 1.00 41.25 ? 618 HIS A NE2 1 ATOM 4689 N N . PRO A 1 578 ? 28.837 79.301 30.463 1.00 36.73 ? 619 PRO A N 1 ATOM 4690 C CA . PRO A 1 578 ? 28.709 80.658 30.972 1.00 37.12 ? 619 PRO A CA 1 ATOM 4691 C C . PRO A 1 578 ? 28.058 81.625 29.986 1.00 38.14 ? 619 PRO A C 1 ATOM 4692 O O . PRO A 1 578 ? 27.266 82.491 30.432 1.00 37.58 ? 619 PRO A O 1 ATOM 4693 C CB . PRO A 1 578 ? 30.152 81.079 31.275 1.00 39.23 ? 619 PRO A CB 1 ATOM 4694 C CG . PRO A 1 578 ? 31.023 80.193 30.343 1.00 39.92 ? 619 PRO A CG 1 ATOM 4695 C CD . PRO A 1 578 ? 30.240 78.871 30.343 1.00 37.68 ? 619 PRO A CD 1 ATOM 4696 N N . GLN A 1 579 ? 28.348 81.495 28.684 1.00 37.91 ? 620 GLN A N 1 ATOM 4697 C CA . GLN A 1 579 ? 27.700 82.364 27.709 1.00 39.17 ? 620 GLN A CA 1 ATOM 4698 C C . GLN A 1 579 ? 26.173 82.229 27.709 1.00 37.00 ? 620 GLN A C 1 ATOM 4699 O O . GLN A 1 579 ? 25.480 83.239 27.687 1.00 36.39 ? 620 GLN A O 1 ATOM 4700 C CB . GLN A 1 579 ? 28.301 82.230 26.288 1.00 42.03 ? 620 GLN A CB 1 ATOM 4701 C CG . GLN A 1 579 ? 27.894 83.364 25.331 1.00 48.86 ? 620 GLN A CG 1 ATOM 4702 C CD . GLN A 1 579 ? 27.910 84.799 25.954 1.00 54.54 ? 620 GLN A CD 1 ATOM 4703 O OE1 . GLN A 1 579 ? 26.835 85.387 26.200 1.00 54.97 ? 620 GLN A OE1 1 ATOM 4704 N NE2 . GLN A 1 579 ? 29.119 85.360 26.195 1.00 56.47 ? 620 GLN A NE2 1 ATOM 4705 N N . GLU A 1 580 ? 25.650 80.997 27.758 1.00 35.46 ? 621 GLU A N 1 ATOM 4706 C CA . GLU A 1 580 ? 24.194 80.803 27.820 1.00 34.45 ? 621 GLU A CA 1 ATOM 4707 C C . GLU A 1 580 ? 23.602 81.337 29.105 1.00 33.18 ? 621 GLU A C 1 ATOM 4708 O O . GLU A 1 580 ? 22.483 81.886 29.124 1.00 32.69 ? 621 GLU A O 1 ATOM 4709 C CB . GLU A 1 580 ? 23.879 79.314 27.672 1.00 35.61 ? 621 GLU A CB 1 ATOM 4710 C CG . GLU A 1 580 ? 24.207 78.778 26.271 1.00 39.72 ? 621 GLU A CG 1 ATOM 4711 C CD . GLU A 1 580 ? 25.675 78.582 25.966 1.00 46.63 ? 621 GLU A CD 1 ATOM 4712 O OE1 . GLU A 1 580 ? 26.549 78.562 26.859 1.00 48.39 ? 621 GLU A OE1 1 ATOM 4713 O OE2 . GLU A 1 580 ? 25.968 78.469 24.768 1.00 53.45 ? 621 GLU A OE2 1 ATOM 4714 N N . MET A 1 581 ? 24.328 81.172 30.209 1.00 32.18 ? 622 MET A N 1 ATOM 4715 C CA . MET A 1 581 ? 23.829 81.679 31.475 1.00 32.18 ? 622 MET A CA 1 ATOM 4716 C C . MET A 1 581 ? 23.715 83.207 31.422 1.00 33.35 ? 622 MET A C 1 ATOM 4717 O O . MET A 1 581 ? 22.776 83.763 31.982 1.00 33.58 ? 622 MET A O 1 ATOM 4718 C CB . MET A 1 581 ? 24.713 81.216 32.645 1.00 32.11 ? 622 MET A CB 1 ATOM 4719 C CG . MET A 1 581 ? 24.581 79.738 32.977 1.00 31.52 ? 622 MET A CG 1 ATOM 4720 S SD . MET A 1 581 ? 25.517 79.293 34.463 1.00 35.21 ? 622 MET A SD 1 ATOM 4721 C CE . MET A 1 581 ? 24.599 80.175 35.770 1.00 34.38 ? 622 MET A CE 1 ATOM 4722 N N . LYS A 1 582 ? 24.634 83.866 30.715 1.00 34.02 ? 623 LYS A N 1 ATOM 4723 C CA . LYS A 1 582 ? 24.567 85.334 30.540 1.00 36.90 ? 623 LYS A CA 1 ATOM 4724 C C . LYS A 1 582 ? 23.375 85.711 29.666 1.00 37.33 ? 623 LYS A C 1 ATOM 4725 O O . LYS A 1 582 ? 22.546 86.555 30.042 1.00 36.04 ? 623 LYS A O 1 ATOM 4726 C CB . LYS A 1 582 ? 25.852 85.853 29.911 1.00 38.35 ? 623 LYS A CB 1 ATOM 4727 C CG . LYS A 1 582 ? 27.008 85.793 30.839 1.00 39.42 ? 623 LYS A CG 1 ATOM 4728 C CD . LYS A 1 582 ? 28.275 86.260 30.158 1.00 47.67 ? 623 LYS A CD 1 ATOM 4729 C CE . LYS A 1 582 ? 29.380 86.144 31.176 1.00 51.43 ? 623 LYS A CE 1 ATOM 4730 N NZ . LYS A 1 582 ? 30.535 85.284 30.818 1.00 56.10 ? 623 LYS A NZ 1 ATOM 4731 N N . THR A 1 583 ? 23.282 85.037 28.516 1.00 38.15 ? 624 THR A N 1 ATOM 4732 C CA . THR A 1 583 ? 22.253 85.304 27.507 1.00 40.47 ? 624 THR A CA 1 ATOM 4733 C C . THR A 1 583 ? 20.844 85.123 28.016 1.00 38.18 ? 624 THR A C 1 ATOM 4734 O O . THR A 1 583 ? 19.970 85.955 27.753 1.00 38.09 ? 624 THR A O 1 ATOM 4735 C CB . THR A 1 583 ? 22.460 84.391 26.272 1.00 41.99 ? 624 THR A CB 1 ATOM 4736 O OG1 . THR A 1 583 ? 23.683 84.782 25.653 1.00 46.04 ? 624 THR A OG1 1 ATOM 4737 C CG2 . THR A 1 583 ? 21.326 84.579 25.237 1.00 44.25 ? 624 THR A CG2 1 ATOM 4738 N N . TYR A 1 584 ? 20.619 84.040 28.753 1.00 35.94 ? 625 TYR A N 1 ATOM 4739 C CA . TYR A 1 584 ? 19.288 83.746 29.258 1.00 34.96 ? 625 TYR A CA 1 ATOM 4740 C C . TYR A 1 584 ? 19.068 84.151 30.723 1.00 34.06 ? 625 TYR A C 1 ATOM 4741 O O . TYR A 1 584 ? 18.038 83.796 31.284 1.00 34.30 ? 625 TYR A O 1 ATOM 4742 C CB . TYR A 1 584 ? 18.914 82.261 29.001 1.00 33.62 ? 625 TYR A CB 1 ATOM 4743 C CG . TYR A 1 584 ? 19.026 81.930 27.528 1.00 36.08 ? 625 TYR A CG 1 ATOM 4744 C CD1 . TYR A 1 584 ? 18.154 82.517 26.596 1.00 40.22 ? 625 TYR A CD1 1 ATOM 4745 C CD2 . TYR A 1 584 ? 20.044 81.097 27.051 1.00 38.70 ? 625 TYR A CD2 1 ATOM 4746 C CE1 . TYR A 1 584 ? 18.303 82.285 25.209 1.00 43.31 ? 625 TYR A CE1 1 ATOM 4747 C CE2 . TYR A 1 584 ? 20.192 80.842 25.680 1.00 42.86 ? 625 TYR A CE2 1 ATOM 4748 C CZ . TYR A 1 584 ? 19.305 81.430 24.771 1.00 46.07 ? 625 TYR A CZ 1 ATOM 4749 O OH . TYR A 1 584 ? 19.468 81.211 23.423 1.00 48.64 ? 625 TYR A OH 1 ATOM 4750 N N . SER A 1 585 ? 20.026 84.897 31.301 1.00 33.94 ? 626 SER A N 1 ATOM 4751 C CA A SER A 1 585 ? 19.951 85.372 32.698 0.50 32.23 ? 626 SER A CA 1 ATOM 4752 C CA B SER A 1 585 ? 19.983 85.363 32.701 0.50 33.73 ? 626 SER A CA 1 ATOM 4753 C C . SER A 1 585 ? 19.612 84.246 33.665 1.00 31.92 ? 626 SER A C 1 ATOM 4754 O O . SER A 1 585 ? 18.602 84.312 34.393 1.00 31.57 ? 626 SER A O 1 ATOM 4755 C CB A SER A 1 585 ? 18.953 86.537 32.858 0.50 32.18 ? 626 SER A CB 1 ATOM 4756 C CB B SER A 1 585 ? 19.095 86.616 32.885 0.50 34.03 ? 626 SER A CB 1 ATOM 4757 O OG A SER A 1 585 ? 19.236 87.588 31.958 0.50 28.20 ? 626 SER A OG 1 ATOM 4758 O OG B SER A 1 585 ? 17.768 86.385 32.469 0.50 37.10 ? 626 SER A OG 1 ATOM 4759 N N . VAL A 1 586 ? 20.430 83.193 33.650 1.00 30.76 ? 627 VAL A N 1 ATOM 4760 C CA . VAL A 1 586 ? 20.174 82.023 34.456 1.00 30.73 ? 627 VAL A CA 1 ATOM 4761 C C . VAL A 1 586 ? 20.861 82.258 35.792 1.00 32.39 ? 627 VAL A C 1 ATOM 4762 O O . VAL A 1 586 ? 22.076 82.279 35.848 1.00 35.07 ? 627 VAL A O 1 ATOM 4763 C CB . VAL A 1 586 ? 20.772 80.755 33.775 1.00 30.32 ? 627 VAL A CB 1 ATOM 4764 C CG1 . VAL A 1 586 ? 20.428 79.467 34.605 1.00 27.77 ? 627 VAL A CG1 1 ATOM 4765 C CG2 . VAL A 1 586 ? 20.260 80.661 32.344 1.00 29.96 ? 627 VAL A CG2 1 ATOM 4766 N N . SER A 1 587 ? 20.079 82.511 36.833 1.00 32.89 ? 628 SER A N 1 ATOM 4767 C CA . SER A 1 587 ? 20.633 82.828 38.141 1.00 33.45 ? 628 SER A CA 1 ATOM 4768 C C . SER A 1 587 ? 20.287 81.707 39.117 1.00 31.45 ? 628 SER A C 1 ATOM 4769 O O . SER A 1 587 ? 19.158 81.236 39.163 1.00 30.98 ? 628 SER A O 1 ATOM 4770 C CB . SER A 1 587 ? 20.050 84.133 38.689 1.00 35.43 ? 628 SER A CB 1 ATOM 4771 O OG . SER A 1 587 ? 20.644 84.343 39.967 1.00 37.70 ? 628 SER A OG 1 ATOM 4772 N N . PHE A 1 588 ? 21.266 81.308 39.909 1.00 31.10 ? 629 PHE A N 1 ATOM 4773 C CA . PHE A 1 588 ? 21.018 80.365 41.014 1.00 29.56 ? 629 PHE A CA 1 ATOM 4774 C C . PHE A 1 588 ? 20.827 81.098 42.347 1.00 29.82 ? 629 PHE A C 1 ATOM 4775 O O . PHE A 1 588 ? 20.735 80.453 43.380 1.00 28.22 ? 629 PHE A O 1 ATOM 4776 C CB . PHE A 1 588 ? 22.173 79.344 41.105 1.00 29.54 ? 629 PHE A CB 1 ATOM 4777 C CG . PHE A 1 588 ? 22.084 78.267 40.060 1.00 28.83 ? 629 PHE A CG 1 ATOM 4778 C CD1 . PHE A 1 588 ? 21.545 77.024 40.378 1.00 26.58 ? 629 PHE A CD1 1 ATOM 4779 C CD2 . PHE A 1 588 ? 22.562 78.513 38.749 1.00 32.46 ? 629 PHE A CD2 1 ATOM 4780 C CE1 . PHE A 1 588 ? 21.468 76.003 39.413 1.00 28.09 ? 629 PHE A CE1 1 ATOM 4781 C CE2 . PHE A 1 588 ? 22.483 77.510 37.763 1.00 29.83 ? 629 PHE A CE2 1 ATOM 4782 C CZ . PHE A 1 588 ? 21.930 76.249 38.110 1.00 29.39 ? 629 PHE A CZ 1 ATOM 4783 N N . ASP A 1 589 ? 20.737 82.435 42.310 1.00 29.52 ? 630 ASP A N 1 ATOM 4784 C CA . ASP A 1 589 ? 20.632 83.213 43.563 1.00 31.72 ? 630 ASP A CA 1 ATOM 4785 C C . ASP A 1 589 ? 19.466 82.740 44.443 1.00 30.24 ? 630 ASP A C 1 ATOM 4786 O O . ASP A 1 589 ? 19.620 82.642 45.671 1.00 29.98 ? 630 ASP A O 1 ATOM 4787 C CB . ASP A 1 589 ? 20.508 84.700 43.299 1.00 32.02 ? 630 ASP A CB 1 ATOM 4788 C CG . ASP A 1 589 ? 21.837 85.318 42.743 1.00 40.32 ? 630 ASP A CG 1 ATOM 4789 O OD1 . ASP A 1 589 ? 22.838 84.587 42.582 1.00 43.54 ? 630 ASP A OD1 1 ATOM 4790 O OD2 . ASP A 1 589 ? 21.860 86.536 42.454 1.00 45.36 ? 630 ASP A OD2 1 ATOM 4791 N N . SER A 1 590 ? 18.311 82.457 43.840 1.00 28.79 ? 631 SER A N 1 ATOM 4792 C CA . SER A 1 590 ? 17.150 82.019 44.655 1.00 28.21 ? 631 SER A CA 1 ATOM 4793 C C . SER A 1 590 ? 17.419 80.710 45.383 1.00 26.90 ? 631 SER A C 1 ATOM 4794 O O . SER A 1 590 ? 17.025 80.526 46.554 1.00 26.03 ? 631 SER A O 1 ATOM 4795 C CB . SER A 1 590 ? 15.849 81.911 43.830 1.00 28.72 ? 631 SER A CB 1 ATOM 4796 O OG . SER A 1 590 ? 15.996 80.977 42.761 1.00 29.82 ? 631 SER A OG 1 ATOM 4797 N N . LEU A 1 591 ? 18.083 79.789 44.717 1.00 26.08 ? 632 LEU A N 1 ATOM 4798 C CA . LEU A 1 591 ? 18.341 78.516 45.325 1.00 25.62 ? 632 LEU A CA 1 ATOM 4799 C C . LEU A 1 591 ? 19.355 78.659 46.487 1.00 26.07 ? 632 LEU A C 1 ATOM 4800 O O . LEU A 1 591 ? 19.157 78.074 47.560 1.00 25.16 ? 632 LEU A O 1 ATOM 4801 C CB . LEU A 1 591 ? 18.822 77.496 44.281 1.00 25.99 ? 632 LEU A CB 1 ATOM 4802 C CG . LEU A 1 591 ? 19.176 76.078 44.803 1.00 25.18 ? 632 LEU A CG 1 ATOM 4803 C CD1 . LEU A 1 591 ? 17.936 75.427 45.407 1.00 24.10 ? 632 LEU A CD1 1 ATOM 4804 C CD2 . LEU A 1 591 ? 19.711 75.226 43.685 1.00 27.59 ? 632 LEU A CD2 1 ATOM 4805 N N . PHE A 1 592 ? 20.400 79.463 46.291 1.00 26.19 ? 633 PHE A N 1 ATOM 4806 C CA . PHE A 1 592 ? 21.356 79.653 47.402 1.00 27.55 ? 633 PHE A CA 1 ATOM 4807 C C . PHE A 1 592 ? 20.716 80.377 48.580 1.00 27.92 ? 633 PHE A C 1 ATOM 4808 O O . PHE A 1 592 ? 21.007 80.081 49.760 1.00 28.89 ? 633 PHE A O 1 ATOM 4809 C CB . PHE A 1 592 ? 22.607 80.371 46.899 1.00 28.80 ? 633 PHE A CB 1 ATOM 4810 C CG . PHE A 1 592 ? 23.540 79.436 46.141 1.00 31.60 ? 633 PHE A CG 1 ATOM 4811 C CD1 . PHE A 1 592 ? 24.341 78.528 46.836 1.00 32.67 ? 633 PHE A CD1 1 ATOM 4812 C CD2 . PHE A 1 592 ? 23.606 79.462 44.750 1.00 33.09 ? 633 PHE A CD2 1 ATOM 4813 C CE1 . PHE A 1 592 ? 25.214 77.634 46.161 1.00 33.39 ? 633 PHE A CE1 1 ATOM 4814 C CE2 . PHE A 1 592 ? 24.466 78.548 44.060 1.00 35.11 ? 633 PHE A CE2 1 ATOM 4815 C CZ . PHE A 1 592 ? 25.264 77.648 44.791 1.00 31.56 ? 633 PHE A CZ 1 ATOM 4816 N N . SER A 1 593 ? 19.850 81.335 48.257 1.00 27.48 ? 634 SER A N 1 ATOM 4817 C CA . SER A 1 593 ? 19.095 82.050 49.280 1.00 28.44 ? 634 SER A CA 1 ATOM 4818 C C . SER A 1 593 ? 18.234 81.081 50.067 1.00 26.86 ? 634 SER A C 1 ATOM 4819 O O . SER A 1 593 ? 18.220 81.134 51.302 1.00 27.09 ? 634 SER A O 1 ATOM 4820 C CB . SER A 1 593 ? 18.270 83.183 48.640 1.00 28.82 ? 634 SER A CB 1 ATOM 4821 O OG . SER A 1 593 ? 17.339 83.743 49.564 1.00 29.42 ? 634 SER A OG 1 ATOM 4822 N N . ALA A 1 594 ? 17.518 80.178 49.380 1.00 24.46 ? 635 ALA A N 1 ATOM 4823 C CA . ALA A 1 594 ? 16.706 79.204 50.065 1.00 24.44 ? 635 ALA A CA 1 ATOM 4824 C C . ALA A 1 594 ? 17.552 78.298 50.965 1.00 25.00 ? 635 ALA A C 1 ATOM 4825 O O . ALA A 1 594 ? 17.143 77.962 52.080 1.00 26.36 ? 635 ALA A O 1 ATOM 4826 C CB . ALA A 1 594 ? 15.857 78.349 49.046 1.00 22.30 ? 635 ALA A CB 1 ATOM 4827 N N . VAL A 1 595 ? 18.690 77.844 50.460 1.00 25.57 ? 636 VAL A N 1 ATOM 4828 C CA . VAL A 1 595 ? 19.559 76.943 51.254 1.00 26.23 ? 636 VAL A CA 1 ATOM 4829 C C . VAL A 1 595 ? 20.098 77.681 52.508 1.00 27.54 ? 636 VAL A C 1 ATOM 4830 O O . VAL A 1 595 ? 20.169 77.103 53.616 1.00 27.44 ? 636 VAL A O 1 ATOM 4831 C CB . VAL A 1 595 ? 20.674 76.392 50.392 1.00 26.53 ? 636 VAL A CB 1 ATOM 4832 C CG1 . VAL A 1 595 ? 21.757 75.700 51.254 1.00 28.22 ? 636 VAL A CG1 1 ATOM 4833 C CG2 . VAL A 1 595 ? 20.073 75.420 49.341 1.00 27.03 ? 636 VAL A CG2 1 ATOM 4834 N N . LYS A 1 596 ? 20.488 78.939 52.328 1.00 27.86 ? 637 LYS A N 1 ATOM 4835 C CA . LYS A 1 596 ? 20.958 79.809 53.460 1.00 29.49 ? 637 LYS A CA 1 ATOM 4836 C C . LYS A 1 596 ? 19.847 79.919 54.514 1.00 29.32 ? 637 LYS A C 1 ATOM 4837 O O . LYS A 1 596 ? 20.070 79.731 55.734 1.00 28.58 ? 637 LYS A O 1 ATOM 4838 C CB . LYS A 1 596 ? 21.300 81.213 52.927 1.00 31.12 ? 637 LYS A CB 1 ATOM 4839 C CG . LYS A 1 596 ? 21.723 82.251 54.039 1.00 37.47 ? 637 LYS A CG 1 ATOM 4840 C CD . LYS A 1 596 ? 22.127 83.620 53.411 1.00 41.97 ? 637 LYS A CD 1 ATOM 4841 C CE . LYS A 1 596 ? 22.590 84.611 54.501 1.00 49.94 ? 637 LYS A CE 1 ATOM 4842 N NZ . LYS A 1 596 ? 21.324 85.113 55.147 1.00 51.74 ? 637 LYS A NZ 1 ATOM 4843 N N . ASN A 1 597 ? 18.628 80.166 54.039 1.00 27.02 ? 638 ASN A N 1 ATOM 4844 C CA . ASN A 1 597 ? 17.476 80.248 54.925 1.00 28.60 ? 638 ASN A CA 1 ATOM 4845 C C . ASN A 1 597 ? 17.207 78.953 55.642 1.00 27.56 ? 638 ASN A C 1 ATOM 4846 O O . ASN A 1 597 ? 16.951 78.968 56.858 1.00 28.42 ? 638 ASN A O 1 ATOM 4847 C CB . ASN A 1 597 ? 16.204 80.648 54.170 1.00 27.20 ? 638 ASN A CB 1 ATOM 4848 C CG . ASN A 1 597 ? 16.212 82.091 53.773 1.00 29.54 ? 638 ASN A CG 1 ATOM 4849 O OD1 . ASN A 1 597 ? 17.087 82.870 54.194 1.00 28.70 ? 638 ASN A OD1 1 ATOM 4850 N ND2 . ASN A 1 597 ? 15.263 82.470 52.954 1.00 29.16 ? 638 ASN A ND2 1 ATOM 4851 N N . PHE A 1 598 ? 17.299 77.832 54.919 1.00 26.65 ? 639 PHE A N 1 ATOM 4852 C CA . PHE A 1 598 ? 17.100 76.545 55.528 1.00 26.32 ? 639 PHE A CA 1 ATOM 4853 C C . PHE A 1 598 ? 18.134 76.323 56.671 1.00 28.16 ? 639 PHE A C 1 ATOM 4854 O O . PHE A 1 598 ? 17.774 75.799 57.735 1.00 27.66 ? 639 PHE A O 1 ATOM 4855 C CB . PHE A 1 598 ? 17.245 75.435 54.491 1.00 25.47 ? 639 PHE A CB 1 ATOM 4856 C CG . PHE A 1 598 ? 16.834 74.073 54.991 1.00 25.98 ? 639 PHE A CG 1 ATOM 4857 C CD1 . PHE A 1 598 ? 15.631 73.503 54.570 1.00 24.96 ? 639 PHE A CD1 1 ATOM 4858 C CD2 . PHE A 1 598 ? 17.676 73.339 55.827 1.00 26.50 ? 639 PHE A CD2 1 ATOM 4859 C CE1 . PHE A 1 598 ? 15.237 72.236 55.011 1.00 28.89 ? 639 PHE A CE1 1 ATOM 4860 C CE2 . PHE A 1 598 ? 17.307 72.084 56.301 1.00 25.42 ? 639 PHE A CE2 1 ATOM 4861 C CZ . PHE A 1 598 ? 16.095 71.503 55.883 1.00 25.50 ? 639 PHE A CZ 1 ATOM 4862 N N . THR A 1 599 ? 19.392 76.661 56.403 1.00 28.08 ? 640 THR A N 1 ATOM 4863 C CA . THR A 1 599 ? 20.484 76.556 57.402 1.00 30.09 ? 640 THR A CA 1 ATOM 4864 C C . THR A 1 599 ? 20.166 77.342 58.685 1.00 30.86 ? 640 THR A C 1 ATOM 4865 O O . THR A 1 599 ? 20.271 76.804 59.811 1.00 30.46 ? 640 THR A O 1 ATOM 4866 C CB . THR A 1 599 ? 21.843 76.992 56.769 1.00 30.93 ? 640 THR A CB 1 ATOM 4867 O OG1 . THR A 1 599 ? 22.022 76.284 55.528 1.00 30.45 ? 640 THR A OG1 1 ATOM 4868 C CG2 . THR A 1 599 ? 23.060 76.667 57.716 1.00 32.64 ? 640 THR A CG2 1 ATOM 4869 N N . GLU A 1 600 ? 19.807 78.612 58.501 1.00 30.67 ? 641 GLU A N 1 ATOM 4870 C CA . GLU A 1 600 ? 19.443 79.484 59.622 1.00 33.17 ? 641 GLU A CA 1 ATOM 4871 C C . GLU A 1 600 ? 18.256 78.947 60.438 1.00 32.33 ? 641 GLU A C 1 ATOM 4872 O O . GLU A 1 600 ? 18.327 78.868 61.669 1.00 31.18 ? 641 GLU A O 1 ATOM 4873 C CB . GLU A 1 600 ? 19.214 80.912 59.118 1.00 33.76 ? 641 GLU A CB 1 ATOM 4874 C CG . GLU A 1 600 ? 20.549 81.516 58.643 1.00 43.60 ? 641 GLU A CG 1 ATOM 4875 C CD . GLU A 1 600 ? 20.415 82.901 57.964 1.00 51.19 ? 641 GLU A CD 1 ATOM 4876 O OE1 . GLU A 1 600 ? 21.458 83.451 57.532 1.00 54.01 ? 641 GLU A OE1 1 ATOM 4877 O OE2 . GLU A 1 600 ? 19.276 83.416 57.857 1.00 55.28 ? 641 GLU A OE2 1 ATOM 4878 N N . ILE A 1 601 ? 17.172 78.546 59.751 1.00 29.95 ? 642 ILE A N 1 ATOM 4879 C CA . ILE A 1 601 ? 15.964 78.100 60.427 1.00 30.04 ? 642 ILE A CA 1 ATOM 4880 C C . ILE A 1 601 ? 16.220 76.756 61.099 1.00 30.04 ? 642 ILE A C 1 ATOM 4881 O O . ILE A 1 601 ? 15.734 76.520 62.212 1.00 30.16 ? 642 ILE A O 1 ATOM 4882 C CB . ILE A 1 601 ? 14.734 78.053 59.438 1.00 27.93 ? 642 ILE A CB 1 ATOM 4883 C CG1 . ILE A 1 601 ? 14.335 79.464 59.049 1.00 29.33 ? 642 ILE A CG1 1 ATOM 4884 C CG2 . ILE A 1 601 ? 13.525 77.264 60.034 1.00 30.21 ? 642 ILE A CG2 1 ATOM 4885 C CD1 . ILE A 1 601 ? 13.386 79.474 57.808 1.00 29.42 ? 642 ILE A CD1 1 ATOM 4886 N N . ALA A 1 602 ? 16.950 75.872 60.421 1.00 29.10 ? 643 ALA A N 1 ATOM 4887 C CA . ALA A 1 602 ? 17.288 74.553 61.006 1.00 30.19 ? 643 ALA A CA 1 ATOM 4888 C C . ALA A 1 602 ? 18.102 74.755 62.310 1.00 31.43 ? 643 ALA A C 1 ATOM 4889 O O . ALA A 1 602 ? 17.897 74.037 63.307 1.00 30.27 ? 643 ALA A O 1 ATOM 4890 C CB . ALA A 1 602 ? 18.107 73.696 60.039 1.00 30.01 ? 643 ALA A CB 1 ATOM 4891 N N . SER A 1 603 ? 19.049 75.690 62.274 1.00 32.69 ? 644 SER A N 1 ATOM 4892 C CA . SER A 1 603 ? 19.862 75.987 63.454 1.00 36.07 ? 644 SER A CA 1 ATOM 4893 C C . SER A 1 603 ? 18.974 76.453 64.631 1.00 35.71 ? 644 SER A C 1 ATOM 4894 O O . SER A 1 603 ? 19.143 75.983 65.757 1.00 36.43 ? 644 SER A O 1 ATOM 4895 C CB . SER A 1 603 ? 20.951 77.019 63.108 1.00 37.50 ? 644 SER A CB 1 ATOM 4896 O OG . SER A 1 603 ? 21.725 77.364 64.257 1.00 46.66 ? 644 SER A OG 1 ATOM 4897 N N . LYS A 1 604 ? 18.032 77.354 64.369 1.00 33.32 ? 645 LYS A N 1 ATOM 4898 C CA . LYS A 1 604 ? 17.107 77.830 65.403 1.00 35.10 ? 645 LYS A CA 1 ATOM 4899 C C . LYS A 1 604 ? 16.190 76.720 65.887 1.00 33.79 ? 645 LYS A C 1 ATOM 4900 O O . LYS A 1 604 ? 15.947 76.599 67.088 1.00 32.18 ? 645 LYS A O 1 ATOM 4901 C CB . LYS A 1 604 ? 16.305 79.033 64.923 1.00 35.82 ? 645 LYS A CB 1 ATOM 4902 C CG . LYS A 1 604 ? 17.222 80.225 64.628 1.00 41.69 ? 645 LYS A CG 1 ATOM 4903 C CD . LYS A 1 604 ? 16.452 81.510 64.525 1.00 52.96 ? 645 LYS A CD 1 ATOM 4904 C CE . LYS A 1 604 ? 17.386 82.749 64.623 1.00 59.57 ? 645 LYS A CE 1 ATOM 4905 N NZ . LYS A 1 604 ? 17.357 83.513 63.311 1.00 62.64 ? 645 LYS A NZ 1 ATOM 4906 N N . PHE A 1 605 ? 15.700 75.892 64.958 1.00 30.67 ? 646 PHE A N 1 ATOM 4907 C CA . PHE A 1 605 ? 14.864 74.766 65.347 1.00 31.09 ? 646 PHE A CA 1 ATOM 4908 C C . PHE A 1 605 ? 15.627 73.790 66.274 1.00 32.26 ? 646 PHE A C 1 ATOM 4909 O O . PHE A 1 605 ? 15.062 73.292 67.264 1.00 33.41 ? 646 PHE A O 1 ATOM 4910 C CB . PHE A 1 605 ? 14.370 73.997 64.094 1.00 30.36 ? 646 PHE A CB 1 ATOM 4911 C CG . PHE A 1 605 ? 13.539 72.780 64.417 1.00 29.26 ? 646 PHE A CG 1 ATOM 4912 C CD1 . PHE A 1 605 ? 12.165 72.893 64.639 1.00 29.10 ? 646 PHE A CD1 1 ATOM 4913 C CD2 . PHE A 1 605 ? 14.135 71.530 64.530 1.00 31.91 ? 646 PHE A CD2 1 ATOM 4914 C CE1 . PHE A 1 605 ? 11.392 71.767 64.939 1.00 30.38 ? 646 PHE A CE1 1 ATOM 4915 C CE2 . PHE A 1 605 ? 13.372 70.392 64.849 1.00 31.28 ? 646 PHE A CE2 1 ATOM 4916 C CZ . PHE A 1 605 ? 12.007 70.502 65.042 1.00 30.15 ? 646 PHE A CZ 1 ATOM 4917 N N . SER A 1 606 ? 16.875 73.483 65.939 1.00 31.84 ? 647 SER A N 1 ATOM 4918 C CA . SER A 1 606 ? 17.671 72.569 66.748 1.00 34.02 ? 647 SER A CA 1 ATOM 4919 C C . SER A 1 606 ? 17.853 73.105 68.206 1.00 35.86 ? 647 SER A C 1 ATOM 4920 O O . SER A 1 606 ? 17.889 72.310 69.179 1.00 36.73 ? 647 SER A O 1 ATOM 4921 C CB . SER A 1 606 ? 19.051 72.405 66.128 1.00 33.46 ? 647 SER A CB 1 ATOM 4922 O OG A SER A 1 606 ? 18.968 71.882 64.819 0.50 32.96 ? 647 SER A OG 1 ATOM 4923 O OG B SER A 1 606 ? 19.769 71.346 66.746 0.50 34.90 ? 647 SER A OG 1 ATOM 4924 N N . GLU A 1 607 ? 18.031 74.415 68.323 1.00 36.97 ? 648 GLU A N 1 ATOM 4925 C CA . GLU A 1 607 ? 18.150 75.076 69.648 1.00 39.98 ? 648 GLU A CA 1 ATOM 4926 C C . GLU A 1 607 ? 16.866 74.882 70.456 1.00 39.92 ? 648 GLU A C 1 ATOM 4927 O O . GLU A 1 607 ? 16.920 74.483 71.632 1.00 38.41 ? 648 GLU A O 1 ATOM 4928 C CB . GLU A 1 607 ? 18.399 76.565 69.486 1.00 42.53 ? 648 GLU A CB 1 ATOM 4929 C CG . GLU A 1 607 ? 19.750 76.880 68.901 1.00 49.45 ? 648 GLU A CG 1 ATOM 4930 C CD . GLU A 1 607 ? 20.088 78.387 68.860 1.00 59.64 ? 648 GLU A CD 1 ATOM 4931 O OE1 . GLU A 1 607 ? 19.239 79.262 69.206 1.00 59.70 ? 648 GLU A OE1 1 ATOM 4932 O OE2 . GLU A 1 607 ? 21.250 78.685 68.478 1.00 65.42 ? 648 GLU A OE2 1 ATOM 4933 N N . ARG A 1 608 ? 15.708 75.110 69.808 1.00 36.88 ? 649 ARG A N 1 ATOM 4934 C CA . ARG A 1 608 ? 14.419 74.907 70.476 1.00 36.50 ? 649 ARG A CA 1 ATOM 4935 C C . ARG A 1 608 ? 14.227 73.465 70.846 1.00 36.20 ? 649 ARG A C 1 ATOM 4936 O O . ARG A 1 608 ? 13.701 73.175 71.911 1.00 36.25 ? 649 ARG A O 1 ATOM 4937 C CB . ARG A 1 608 ? 13.218 75.411 69.636 1.00 35.84 ? 649 ARG A CB 1 ATOM 4938 C CG . ARG A 1 608 ? 13.227 76.871 69.416 1.00 37.57 ? 649 ARG A CG 1 ATOM 4939 C CD . ARG A 1 608 ? 11.847 77.370 68.947 1.00 36.77 ? 649 ARG A CD 1 ATOM 4940 N NE . ARG A 1 608 ? 11.302 76.598 67.819 1.00 34.06 ? 649 ARG A NE 1 ATOM 4941 C CZ . ARG A 1 608 ? 11.624 76.812 66.542 1.00 36.06 ? 649 ARG A CZ 1 ATOM 4942 N NH1 . ARG A 1 608 ? 12.529 77.753 66.243 1.00 34.35 ? 649 ARG A NH1 1 ATOM 4943 N NH2 . ARG A 1 608 ? 11.044 76.083 65.575 1.00 31.75 ? 649 ARG A NH2 1 ATOM 4944 N N . LEU A 1 609 ? 14.695 72.547 70.000 1.00 36.10 ? 650 LEU A N 1 ATOM 4945 C CA . LEU A 1 609 ? 14.510 71.126 70.244 1.00 37.95 ? 650 LEU A CA 1 ATOM 4946 C C . LEU A 1 609 ? 15.337 70.686 71.446 1.00 41.03 ? 650 LEU A C 1 ATOM 4947 O O . LEU A 1 609 ? 14.977 69.753 72.157 1.00 40.73 ? 650 LEU A O 1 ATOM 4948 C CB . LEU A 1 609 ? 14.909 70.296 68.999 1.00 37.38 ? 650 LEU A CB 1 ATOM 4949 C CG . LEU A 1 609 ? 14.502 68.833 68.888 1.00 37.17 ? 650 LEU A CG 1 ATOM 4950 C CD1 . LEU A 1 609 ? 13.011 68.712 68.659 1.00 33.53 ? 650 LEU A CD1 1 ATOM 4951 C CD2 . LEU A 1 609 ? 15.342 68.114 67.734 1.00 36.46 ? 650 LEU A CD2 1 ATOM 4952 N N . GLN A 1 610 ? 16.441 71.371 71.675 1.00 43.82 ? 651 GLN A N 1 ATOM 4953 C CA . GLN A 1 610 ? 17.324 70.970 72.749 1.00 48.33 ? 651 GLN A CA 1 ATOM 4954 C C . GLN A 1 610 ? 16.845 71.576 74.074 1.00 49.60 ? 651 GLN A C 1 ATOM 4955 O O . GLN A 1 610 ? 17.030 70.962 75.123 1.00 52.17 ? 651 GLN A O 1 ATOM 4956 C CB A GLN A 1 610 ? 18.780 71.292 72.409 0.65 48.33 ? 651 GLN A CB 1 ATOM 4957 C CB B GLN A 1 610 ? 18.772 71.355 72.387 0.35 48.04 ? 651 GLN A CB 1 ATOM 4958 C CG A GLN A 1 610 ? 19.396 70.215 71.512 0.65 50.58 ? 651 GLN A CG 1 ATOM 4959 C CG B GLN A 1 610 ? 19.739 71.645 73.532 0.35 50.92 ? 651 GLN A CG 1 ATOM 4960 C CD A GLN A 1 610 ? 20.843 70.486 71.125 0.65 54.00 ? 651 GLN A CD 1 ATOM 4961 C CD B GLN A 1 610 ? 20.233 73.076 73.504 0.35 52.43 ? 651 GLN A CD 1 ATOM 4962 O OE1 A GLN A 1 610 ? 21.538 71.257 71.780 0.65 59.17 ? 651 GLN A OE1 1 ATOM 4963 O OE1 B GLN A 1 610 ? 19.497 73.991 73.127 0.35 50.12 ? 651 GLN A OE1 1 ATOM 4964 N NE2 A GLN A 1 610 ? 21.296 69.853 70.048 0.65 54.01 ? 651 GLN A NE2 1 ATOM 4965 N NE2 B GLN A 1 610 ? 21.494 73.276 73.889 0.35 52.93 ? 651 GLN A NE2 1 ATOM 4966 N N . ASP A 1 611 ? 16.131 72.700 73.966 1.00 51.31 ? 652 ASP A N 1 ATOM 4967 C CA . ASP A 1 611 ? 15.661 73.596 75.046 1.00 53.75 ? 652 ASP A CA 1 ATOM 4968 C C . ASP A 1 611 ? 14.203 73.551 75.548 1.00 53.48 ? 652 ASP A C 1 ATOM 4969 O O . ASP A 1 611 ? 13.868 74.353 76.406 1.00 54.18 ? 652 ASP A O 1 ATOM 4970 C CB . ASP A 1 611 ? 15.809 75.052 74.584 1.00 54.88 ? 652 ASP A CB 1 ATOM 4971 C CG . ASP A 1 611 ? 17.236 75.583 74.687 1.00 60.49 ? 652 ASP A CG 1 ATOM 4972 O OD1 . ASP A 1 611 ? 17.412 76.794 74.382 1.00 66.65 ? 652 ASP A OD1 1 ATOM 4973 O OD2 . ASP A 1 611 ? 18.160 74.823 75.067 1.00 65.13 ? 652 ASP A OD2 1 ATOM 4974 N N . PHE A 1 612 ? 13.313 72.713 75.009 1.00 52.48 ? 653 PHE A N 1 ATOM 4975 C CA . PHE A 1 612 ? 11.928 72.605 75.559 1.00 52.36 ? 653 PHE A CA 1 ATOM 4976 C C . PHE A 1 612 ? 11.794 71.476 76.628 1.00 54.68 ? 653 PHE A C 1 ATOM 4977 O O . PHE A 1 612 ? 10.725 71.332 77.339 1.00 57.22 ? 653 PHE A O 1 ATOM 4978 C CB . PHE A 1 612 ? 10.947 72.360 74.402 1.00 50.86 ? 653 PHE A CB 1 ATOM 4979 C CG . PHE A 1 612 ? 10.864 70.930 73.985 1.00 44.97 ? 653 PHE A CG 1 ATOM 4980 C CD1 . PHE A 1 612 ? 9.780 70.154 74.350 1.00 45.77 ? 653 PHE A CD1 1 ATOM 4981 C CD2 . PHE A 1 612 ? 11.868 70.359 73.227 1.00 46.28 ? 653 PHE A CD2 1 ATOM 4982 C CE1 . PHE A 1 612 ? 9.682 68.831 73.939 1.00 48.08 ? 653 PHE A CE1 1 ATOM 4983 C CE2 . PHE A 1 612 ? 11.803 69.029 72.816 1.00 46.95 ? 653 PHE A CE2 1 ATOM 4984 C CZ . PHE A 1 612 ? 10.705 68.259 73.164 1.00 47.85 ? 653 PHE A CZ 1 ATOM 4985 N N A SER A 1 615 ? 8.972 68.713 79.857 0.50 33.53 ? 656 SER A N 1 ATOM 4986 N N B SER A 1 615 ? 8.257 66.244 78.751 0.50 33.32 ? 656 SER A N 1 ATOM 4987 C CA A SER A 1 615 ? 7.744 68.154 80.385 0.50 34.19 ? 656 SER A CA 1 ATOM 4988 C CA B SER A 1 615 ? 7.089 65.742 79.533 0.50 33.52 ? 656 SER A CA 1 ATOM 4989 C C A SER A 1 615 ? 6.466 68.264 79.474 0.50 32.67 ? 656 SER A C 1 ATOM 4990 C C B SER A 1 615 ? 5.710 66.333 79.243 0.50 34.64 ? 656 SER A C 1 ATOM 4991 O O A SER A 1 615 ? 5.418 67.699 79.809 0.50 32.54 ? 656 SER A O 1 ATOM 4992 O O B SER A 1 615 ? 4.694 65.963 79.862 0.50 35.16 ? 656 SER A O 1 ATOM 4993 C CB A SER A 1 615 ? 7.461 68.829 81.710 0.50 33.12 ? 656 SER A CB 1 ATOM 4994 C CB B SER A 1 615 ? 7.374 65.831 81.042 0.50 34.77 ? 656 SER A CB 1 ATOM 4995 O OG A SER A 1 615 ? 6.966 70.122 81.483 0.50 34.31 ? 656 SER A OG 1 ATOM 4996 O OG B SER A 1 615 ? 7.693 64.549 81.471 0.50 31.53 ? 656 SER A OG 1 ATOM 4997 N N A ASN A 1 616 ? 6.541 68.984 78.352 0.50 31.87 ? 657 ASN A N 1 ATOM 4998 N N B ASN A 1 616 ? 5.650 67.283 78.339 0.50 34.31 ? 657 ASN A N 1 ATOM 4999 C CA A ASN A 1 616 ? 5.343 69.305 77.554 0.50 30.87 ? 657 ASN A CA 1 ATOM 5000 C CA B ASN A 1 616 ? 4.355 67.816 77.973 0.50 35.57 ? 657 ASN A CA 1 ATOM 5001 C C A ASN A 1 616 ? 5.190 68.388 76.349 0.50 29.83 ? 657 ASN A C 1 ATOM 5002 C C B ASN A 1 616 ? 3.936 67.076 76.699 0.50 33.85 ? 657 ASN A C 1 ATOM 5003 O O A ASN A 1 616 ? 5.994 68.457 75.407 0.50 28.51 ? 657 ASN A O 1 ATOM 5004 O O B ASN A 1 616 ? 4.537 67.279 75.650 0.50 33.47 ? 657 ASN A O 1 ATOM 5005 C CB A ASN A 1 616 ? 5.397 70.741 77.075 0.50 30.97 ? 657 ASN A CB 1 ATOM 5006 C CB B ASN A 1 616 ? 4.490 69.320 77.770 0.50 35.69 ? 657 ASN A CB 1 ATOM 5007 C CG A ASN A 1 616 ? 4.034 71.249 76.638 0.50 32.01 ? 657 ASN A CG 1 ATOM 5008 C CG B ASN A 1 616 ? 3.220 69.954 77.277 0.50 39.38 ? 657 ASN A CG 1 ATOM 5009 O OD1 A ASN A 1 616 ? 3.312 70.567 75.910 0.50 29.64 ? 657 ASN A OD1 1 ATOM 5010 O OD1 B ASN A 1 616 ? 2.472 69.350 76.498 0.50 42.12 ? 657 ASN A OD1 1 ATOM 5011 N ND2 A ASN A 1 616 ? 3.681 72.426 77.076 0.50 34.99 ? 657 ASN A ND2 1 ATOM 5012 N ND2 B ASN A 1 616 ? 2.986 71.193 77.681 0.50 39.31 ? 657 ASN A ND2 1 ATOM 5013 N N A PRO A 1 617 ? 4.184 67.493 76.383 0.50 29.85 ? 658 PRO A N 1 ATOM 5014 N N B PRO A 1 617 ? 2.938 66.169 76.788 0.50 33.68 ? 658 PRO A N 1 ATOM 5015 C CA A PRO A 1 617 ? 4.116 66.469 75.329 0.50 29.09 ? 658 PRO A CA 1 ATOM 5016 C CA B PRO A 1 617 ? 2.677 65.323 75.596 0.50 32.36 ? 658 PRO A CA 1 ATOM 5017 C C A PRO A 1 617 ? 3.550 67.010 74.025 0.50 28.06 ? 658 PRO A C 1 ATOM 5018 C C B PRO A 1 617 ? 2.286 66.049 74.288 0.50 31.83 ? 658 PRO A C 1 ATOM 5019 O O A PRO A 1 617 ? 3.747 66.384 72.985 0.50 27.34 ? 658 PRO A O 1 ATOM 5020 O O B PRO A 1 617 ? 2.735 65.623 73.223 0.50 30.81 ? 658 PRO A O 1 ATOM 5021 C CB A PRO A 1 617 ? 3.148 65.424 75.906 0.50 28.93 ? 658 PRO A CB 1 ATOM 5022 C CB B PRO A 1 617 ? 1.564 64.381 76.051 0.50 33.26 ? 658 PRO A CB 1 ATOM 5023 C CG A PRO A 1 617 ? 2.225 66.244 76.781 0.50 30.27 ? 658 PRO A CG 1 ATOM 5024 C CG B PRO A 1 617 ? 1.610 64.433 77.597 0.50 34.15 ? 658 PRO A CG 1 ATOM 5025 C CD A PRO A 1 617 ? 3.075 67.377 77.352 0.50 30.66 ? 658 PRO A CD 1 ATOM 5026 C CD B PRO A 1 617 ? 2.118 65.785 77.953 0.50 33.89 ? 658 PRO A CD 1 ATOM 5027 N N A ILE A 1 618 ? 2.818 68.123 74.101 0.50 29.01 ? 659 ILE A N 1 ATOM 5028 N N B ILE A 1 618 ? 1.474 67.105 74.325 0.50 32.20 ? 659 ILE A N 1 ATOM 5029 C CA A ILE A 1 618 ? 2.279 68.804 72.929 0.50 28.63 ? 659 ILE A CA 1 ATOM 5030 C CA B ILE A 1 618 ? 1.193 67.813 73.057 0.50 31.74 ? 659 ILE A CA 1 ATOM 5031 C C A ILE A 1 618 ? 3.401 69.468 72.131 0.50 27.79 ? 659 ILE A C 1 ATOM 5032 C C B ILE A 1 618 ? 2.403 68.549 72.522 0.50 30.78 ? 659 ILE A C 1 ATOM 5033 O O A ILE A 1 618 ? 3.448 69.389 70.903 0.50 25.87 ? 659 ILE A O 1 ATOM 5034 O O B ILE A 1 618 ? 2.705 68.460 71.345 0.50 30.43 ? 659 ILE A O 1 ATOM 5035 C CB A ILE A 1 618 ? 1.259 69.937 73.267 0.50 30.40 ? 659 ILE A CB 1 ATOM 5036 C CB B ILE A 1 618 ? -0.030 68.728 73.076 0.50 31.76 ? 659 ILE A CB 1 ATOM 5037 C CG1 A ILE A 1 618 ? 0.075 69.437 74.108 0.50 32.98 ? 659 ILE A CG1 1 ATOM 5038 C CG1 B ILE A 1 618 ? -1.251 67.856 73.215 0.50 34.53 ? 659 ILE A CG1 1 ATOM 5039 C CG2 A ILE A 1 618 ? 0.781 70.579 71.982 0.50 29.75 ? 659 ILE A CG2 1 ATOM 5040 C CG2 B ILE A 1 618 ? -0.144 69.491 71.769 0.50 31.24 ? 659 ILE A CG2 1 ATOM 5041 C CD1 A ILE A 1 618 ? -0.253 67.990 73.868 0.50 35.23 ? 659 ILE A CD1 1 ATOM 5042 C CD1 B ILE A 1 618 ? -0.995 66.477 72.684 0.50 33.56 ? 659 ILE A CD1 1 ATOM 5043 N N A VAL A 1 619 ? 4.285 70.162 72.835 0.50 27.46 ? 660 VAL A N 1 ATOM 5044 N N B VAL A 1 619 ? 3.107 69.276 73.370 0.50 30.70 ? 660 VAL A N 1 ATOM 5045 C CA A VAL A 1 619 ? 5.442 70.775 72.201 0.50 28.12 ? 660 VAL A CA 1 ATOM 5046 C CA B VAL A 1 619 ? 4.289 70.002 72.891 0.50 29.48 ? 660 VAL A CA 1 ATOM 5047 C C A VAL A 1 619 ? 6.372 69.688 71.658 0.50 27.66 ? 660 VAL A C 1 ATOM 5048 C C B VAL A 1 619 ? 5.323 69.036 72.263 0.50 29.22 ? 660 VAL A C 1 ATOM 5049 O O A VAL A 1 619 ? 6.918 69.823 70.571 0.50 26.18 ? 660 VAL A O 1 ATOM 5050 O O B VAL A 1 619 ? 5.847 69.298 71.165 0.50 27.91 ? 660 VAL A O 1 ATOM 5051 C CB A VAL A 1 619 ? 6.184 71.709 73.179 0.50 28.82 ? 660 VAL A CB 1 ATOM 5052 C CB B VAL A 1 619 ? 4.887 70.938 73.992 0.50 30.96 ? 660 VAL A CB 1 ATOM 5053 C CG1 A VAL A 1 619 ? 7.545 72.098 72.619 0.50 29.90 ? 660 VAL A CG1 1 ATOM 5054 C CG1 B VAL A 1 619 ? 6.249 71.518 73.569 0.50 29.01 ? 660 VAL A CG1 1 ATOM 5055 C CG2 A VAL A 1 619 ? 5.360 72.927 73.375 0.50 30.21 ? 660 VAL A CG2 1 ATOM 5056 C CG2 B VAL A 1 619 ? 3.896 72.067 74.319 0.50 32.56 ? 660 VAL A CG2 1 ATOM 5057 N N A LEU A 1 620 ? 6.541 68.611 72.425 0.50 27.81 ? 661 LEU A N 1 ATOM 5058 N N B LEU A 1 620 ? 5.595 67.913 72.923 0.50 29.05 ? 661 LEU A N 1 ATOM 5059 C CA A LEU A 1 620 ? 7.321 67.457 71.981 0.50 27.28 ? 661 LEU A CA 1 ATOM 5060 C CA B LEU A 1 620 ? 6.470 66.902 72.327 0.50 28.91 ? 661 LEU A CA 1 ATOM 5061 C C A LEU A 1 620 ? 6.779 66.888 70.661 0.50 26.99 ? 661 LEU A C 1 ATOM 5062 C C B LEU A 1 620 ? 5.858 66.420 70.989 0.50 27.98 ? 661 LEU A C 1 ATOM 5063 O O A LEU A 1 620 ? 7.518 66.723 69.685 0.50 24.21 ? 661 LEU A O 1 ATOM 5064 O O B LEU A 1 620 ? 6.556 66.138 70.015 0.50 25.54 ? 661 LEU A O 1 ATOM 5065 C CB A LEU A 1 620 ? 7.294 66.358 73.052 0.50 28.21 ? 661 LEU A CB 1 ATOM 5066 C CB B LEU A 1 620 ? 6.707 65.736 73.306 0.50 28.83 ? 661 LEU A CB 1 ATOM 5067 C CG A LEU A 1 620 ? 7.895 65.003 72.625 0.50 28.54 ? 661 LEU A CG 1 ATOM 5068 C CG B LEU A 1 620 ? 7.506 64.492 72.849 0.50 29.45 ? 661 LEU A CG 1 ATOM 5069 C CD1 A LEU A 1 620 ? 9.257 65.176 72.006 0.50 26.33 ? 661 LEU A CD1 1 ATOM 5070 C CD1 B LEU A 1 620 ? 8.945 64.823 72.442 0.50 26.45 ? 661 LEU A CD1 1 ATOM 5071 C CD2 A LEU A 1 620 ? 7.970 64.057 73.845 0.50 29.48 ? 661 LEU A CD2 1 ATOM 5072 C CD2 B LEU A 1 620 ? 7.461 63.445 73.992 0.50 25.93 ? 661 LEU A CD2 1 ATOM 5073 N N A ARG A 1 621 ? 5.489 66.567 70.663 0.50 26.66 ? 662 ARG A N 1 ATOM 5074 N N B ARG A 1 621 ? 4.547 66.307 70.934 0.50 28.36 ? 662 ARG A N 1 ATOM 5075 C CA A ARG A 1 621 ? 4.882 65.893 69.545 0.50 27.33 ? 662 ARG A CA 1 ATOM 5076 C CA B ARG A 1 621 ? 3.955 65.852 69.684 0.50 27.88 ? 662 ARG A CA 1 ATOM 5077 C C A ARG A 1 621 ? 4.728 66.893 68.428 0.50 27.63 ? 662 ARG A C 1 ATOM 5078 C C B ARG A 1 621 ? 4.243 66.816 68.491 0.50 28.58 ? 662 ARG A C 1 ATOM 5079 O O A ARG A 1 621 ? 4.931 66.549 67.281 0.50 26.58 ? 662 ARG A O 1 ATOM 5080 O O B ARG A 1 621 ? 4.410 66.357 67.365 0.50 27.15 ? 662 ARG A O 1 ATOM 5081 C CB A ARG A 1 621 ? 3.522 65.297 69.897 0.50 26.22 ? 662 ARG A CB 1 ATOM 5082 C CB B ARG A 1 621 ? 2.467 65.537 69.868 0.50 28.23 ? 662 ARG A CB 1 ATOM 5083 C CG A ARG A 1 621 ? 2.659 64.959 68.652 0.50 27.48 ? 662 ARG A CG 1 ATOM 5084 C CG B ARG A 1 621 ? 1.740 65.062 68.596 0.50 25.64 ? 662 ARG A CG 1 ATOM 5085 C CD A ARG A 1 621 ? 3.028 63.619 67.987 0.50 25.27 ? 662 ARG A CD 1 ATOM 5086 C CD B ARG A 1 621 ? 1.892 63.552 68.370 0.50 33.25 ? 662 ARG A CD 1 ATOM 5087 N NE A ARG A 1 621 ? 1.849 63.180 67.259 0.50 28.64 ? 662 ARG A NE 1 ATOM 5088 N NE B ARG A 1 621 ? 0.747 63.116 67.566 0.50 34.68 ? 662 ARG A NE 1 ATOM 5089 C CZ A ARG A 1 621 ? 1.261 62.003 67.383 0.50 28.15 ? 662 ARG A CZ 1 ATOM 5090 C CZ B ARG A 1 621 ? 0.412 61.864 67.312 0.50 33.75 ? 662 ARG A CZ 1 ATOM 5091 N NH1 A ARG A 1 621 ? 1.792 61.051 68.142 0.50 28.44 ? 662 ARG A NH1 1 ATOM 5092 N NH1 B ARG A 1 621 ? 1.152 60.847 67.759 0.50 33.50 ? 662 ARG A NH1 1 ATOM 5093 N NH2 A ARG A 1 621 ? 0.147 61.781 66.700 0.50 29.37 ? 662 ARG A NH2 1 ATOM 5094 N NH2 B ARG A 1 621 ? -0.666 61.647 66.578 0.50 34.37 ? 662 ARG A NH2 1 ATOM 5095 N N . MET A 1 622 ? 4.342 68.129 68.760 1.00 30.08 ? 663 MET A N 1 ATOM 5096 C CA . MET A 1 622 ? 4.464 69.194 67.724 1.00 30.42 ? 663 MET A CA 1 ATOM 5097 C C . MET A 1 622 ? 5.878 69.168 67.126 1.00 30.99 ? 663 MET A C 1 ATOM 5098 O O . MET A 1 622 ? 6.034 69.237 65.898 1.00 29.20 ? 663 MET A O 1 ATOM 5099 C CB A MET A 1 622 ? 4.240 70.606 68.299 0.50 30.89 ? 663 MET A CB 1 ATOM 5100 C CB B MET A 1 622 ? 3.991 70.563 68.261 0.50 31.07 ? 663 MET A CB 1 ATOM 5101 C CG A MET A 1 622 ? 4.896 71.749 67.479 0.50 29.71 ? 663 MET A CG 1 ATOM 5102 C CG B MET A 1 622 ? 2.521 70.484 68.752 0.50 30.22 ? 663 MET A CG 1 ATOM 5103 S SD A MET A 1 622 ? 4.535 73.416 68.146 0.50 30.82 ? 663 MET A SD 1 ATOM 5104 S SD B MET A 1 622 ? 1.567 71.953 69.283 0.50 33.43 ? 663 MET A SD 1 ATOM 5105 C CE A MET A 1 622 ? 2.935 73.079 68.832 0.50 33.91 ? 663 MET A CE 1 ATOM 5106 C CE B MET A 1 622 ? 2.404 72.412 70.851 0.50 26.63 ? 663 MET A CE 1 ATOM 5107 N N . MET A 1 623 ? 6.919 69.093 67.973 1.00 30.19 ? 664 MET A N 1 ATOM 5108 C CA . MET A 1 623 ? 8.278 69.085 67.450 1.00 30.72 ? 664 MET A CA 1 ATOM 5109 C C . MET A 1 623 ? 8.600 67.769 66.724 1.00 29.75 ? 664 MET A C 1 ATOM 5110 O O . MET A 1 623 ? 9.318 67.782 65.731 1.00 29.09 ? 664 MET A O 1 ATOM 5111 C CB A MET A 1 623 ? 9.271 69.173 68.644 0.50 31.99 ? 664 MET A CB 1 ATOM 5112 C CB B MET A 1 623 ? 9.350 69.504 68.482 0.50 31.25 ? 664 MET A CB 1 ATOM 5113 C CG A MET A 1 623 ? 9.018 70.325 69.607 0.50 36.17 ? 664 MET A CG 1 ATOM 5114 C CG B MET A 1 623 ? 9.301 71.009 68.757 0.50 31.98 ? 664 MET A CG 1 ATOM 5115 S SD A MET A 1 623 ? 9.130 71.857 68.694 0.50 41.05 ? 664 MET A SD 1 ATOM 5116 S SD B MET A 1 623 ? 10.673 71.739 69.683 0.50 31.99 ? 664 MET A SD 1 ATOM 5117 C CE A MET A 1 623 ? 10.920 72.100 68.715 0.50 39.90 ? 664 MET A CE 1 ATOM 5118 C CE B MET A 1 623 ? 11.742 72.149 68.315 0.50 27.60 ? 664 MET A CE 1 ATOM 5119 N N . ASN A 1 624 ? 8.115 66.642 67.253 1.00 28.93 ? 665 ASN A N 1 ATOM 5120 C CA . ASN A 1 624 ? 8.295 65.370 66.524 1.00 28.63 ? 665 ASN A CA 1 ATOM 5121 C C . ASN A 1 624 ? 7.584 65.397 65.148 1.00 27.07 ? 665 ASN A C 1 ATOM 5122 O O . ASN A 1 624 ? 8.094 64.833 64.222 1.00 26.00 ? 665 ASN A O 1 ATOM 5123 C CB . ASN A 1 624 ? 7.802 64.197 67.344 1.00 28.97 ? 665 ASN A CB 1 ATOM 5124 C CG . ASN A 1 624 ? 8.887 63.707 68.327 1.00 29.36 ? 665 ASN A CG 1 ATOM 5125 O OD1 . ASN A 1 624 ? 10.087 63.925 68.092 1.00 29.33 ? 665 ASN A OD1 1 ATOM 5126 N ND2 . ASN A 1 624 ? 8.472 63.078 69.424 1.00 29.14 ? 665 ASN A ND2 1 ATOM 5127 N N . ASP A 1 625 ? 6.406 66.009 65.089 1.00 27.20 ? 666 ASP A N 1 ATOM 5128 C CA . ASP A 1 625 ? 5.671 66.159 63.804 1.00 26.84 ? 666 ASP A CA 1 ATOM 5129 C C . ASP A 1 625 ? 6.501 67.024 62.832 1.00 26.43 ? 666 ASP A C 1 ATOM 5130 O O . ASP A 1 625 ? 6.603 66.678 61.667 1.00 26.52 ? 666 ASP A O 1 ATOM 5131 C CB . ASP A 1 625 ? 4.252 66.743 63.994 1.00 26.44 ? 666 ASP A CB 1 ATOM 5132 C CG . ASP A 1 625 ? 3.249 65.718 64.509 1.00 30.21 ? 666 ASP A CG 1 ATOM 5133 O OD1 . ASP A 1 625 ? 3.638 64.530 64.676 1.00 32.81 ? 666 ASP A OD1 1 ATOM 5134 O OD2 . ASP A 1 625 ? 2.081 66.121 64.758 1.00 33.43 ? 666 ASP A OD2 1 ATOM 5135 N N . GLN A 1 626 ? 7.125 68.109 63.314 1.00 25.58 ? 667 GLN A N 1 ATOM 5136 C CA . GLN A 1 626 ? 8.007 68.923 62.455 1.00 24.81 ? 667 GLN A CA 1 ATOM 5137 C C . GLN A 1 626 ? 9.148 68.090 61.950 1.00 24.29 ? 667 GLN A C 1 ATOM 5138 O O . GLN A 1 626 ? 9.499 68.139 60.769 1.00 25.50 ? 667 GLN A O 1 ATOM 5139 C CB . GLN A 1 626 ? 8.520 70.174 63.173 1.00 25.64 ? 667 GLN A CB 1 ATOM 5140 C CG . GLN A 1 626 ? 7.367 71.216 63.317 1.00 26.35 ? 667 GLN A CG 1 ATOM 5141 C CD . GLN A 1 626 ? 7.833 72.412 64.070 1.00 28.12 ? 667 GLN A CD 1 ATOM 5142 O OE1 . GLN A 1 626 ? 7.953 72.382 65.302 1.00 29.80 ? 667 GLN A OE1 1 ATOM 5143 N NE2 . GLN A 1 626 ? 8.101 73.501 63.339 1.00 27.10 ? 667 GLN A NE2 1 ATOM 5144 N N . LEU A 1 627 ? 9.723 67.255 62.812 1.00 25.39 ? 668 LEU A N 1 ATOM 5145 C CA . LEU A 1 627 ? 10.777 66.355 62.336 1.00 25.04 ? 668 LEU A CA 1 ATOM 5146 C C . LEU A 1 627 ? 10.308 65.298 61.334 1.00 24.84 ? 668 LEU A C 1 ATOM 5147 O O . LEU A 1 627 ? 10.966 65.053 60.319 1.00 24.92 ? 668 LEU A O 1 ATOM 5148 C CB . LEU A 1 627 ? 11.406 65.615 63.569 1.00 25.52 ? 668 LEU A CB 1 ATOM 5149 C CG . LEU A 1 627 ? 12.321 66.602 64.339 1.00 28.93 ? 668 LEU A CG 1 ATOM 5150 C CD1 . LEU A 1 627 ? 12.883 65.936 65.539 1.00 33.04 ? 668 LEU A CD1 1 ATOM 5151 C CD2 . LEU A 1 627 ? 13.476 67.126 63.411 1.00 29.70 ? 668 LEU A CD2 1 ATOM 5152 N N . MET A 1 628 ? 9.174 64.675 61.619 1.00 25.13 ? 669 MET A N 1 ATOM 5153 C CA . MET A 1 628 ? 8.654 63.626 60.729 1.00 26.34 ? 669 MET A CA 1 ATOM 5154 C C . MET A 1 628 ? 8.254 64.182 59.357 1.00 25.35 ? 669 MET A C 1 ATOM 5155 O O . MET A 1 628 ? 8.497 63.542 58.318 1.00 25.73 ? 669 MET A O 1 ATOM 5156 C CB . MET A 1 628 ? 7.413 63.010 61.391 1.00 27.52 ? 669 MET A CB 1 ATOM 5157 C CG . MET A 1 628 ? 6.686 61.987 60.504 1.00 33.19 ? 669 MET A CG 1 ATOM 5158 S SD . MET A 1 628 ? 5.317 61.168 61.352 1.00 34.20 ? 669 MET A SD 1 ATOM 5159 C CE . MET A 1 628 ? 4.060 62.423 61.146 1.00 31.18 ? 669 MET A CE 1 ATOM 5160 N N . PHE A 1 629 ? 7.623 65.350 59.366 1.00 24.07 ? 670 PHE A N 1 ATOM 5161 C CA . PHE A 1 629 ? 7.122 65.987 58.098 1.00 24.29 ? 670 PHE A CA 1 ATOM 5162 C C . PHE A 1 629 ? 8.186 66.745 57.316 1.00 23.73 ? 670 PHE A C 1 ATOM 5163 O O . PHE A 1 629 ? 7.896 67.247 56.203 1.00 25.45 ? 670 PHE A O 1 ATOM 5164 C CB . PHE A 1 629 ? 5.888 66.865 58.390 1.00 22.27 ? 670 PHE A CB 1 ATOM 5165 C CG . PHE A 1 629 ? 4.631 66.073 58.669 1.00 26.15 ? 670 PHE A CG 1 ATOM 5166 C CD1 . PHE A 1 629 ? 4.139 65.127 57.735 1.00 26.81 ? 670 PHE A CD1 1 ATOM 5167 C CD2 . PHE A 1 629 ? 3.899 66.311 59.851 1.00 28.29 ? 670 PHE A CD2 1 ATOM 5168 C CE1 . PHE A 1 629 ? 2.981 64.392 57.996 1.00 27.58 ? 670 PHE A CE1 1 ATOM 5169 C CE2 . PHE A 1 629 ? 2.725 65.607 60.125 1.00 32.19 ? 670 PHE A CE2 1 ATOM 5170 C CZ . PHE A 1 629 ? 2.257 64.641 59.212 1.00 30.77 ? 670 PHE A CZ 1 ATOM 5171 N N . LEU A 1 630 ? 9.430 66.803 57.838 1.00 24.11 ? 671 LEU A N 1 ATOM 5172 C CA . LEU A 1 630 ? 10.511 67.531 57.150 1.00 24.39 ? 671 LEU A CA 1 ATOM 5173 C C . LEU A 1 630 ? 10.877 66.818 55.827 1.00 23.81 ? 671 LEU A C 1 ATOM 5174 O O . LEU A 1 630 ? 10.934 67.456 54.781 1.00 22.67 ? 671 LEU A O 1 ATOM 5175 C CB . LEU A 1 630 ? 11.780 67.715 58.030 1.00 25.10 ? 671 LEU A CB 1 ATOM 5176 C CG . LEU A 1 630 ? 12.921 68.471 57.347 1.00 25.90 ? 671 LEU A CG 1 ATOM 5177 C CD1 . LEU A 1 630 ? 12.528 69.864 56.800 1.00 28.02 ? 671 LEU A CD1 1 ATOM 5178 C CD2 . LEU A 1 630 ? 14.078 68.604 58.398 1.00 28.09 ? 671 LEU A CD2 1 ATOM 5179 N N . GLU A 1 631 ? 11.097 65.503 55.874 1.00 22.27 ? 672 GLU A N 1 ATOM 5180 C CA . GLU A 1 631 ? 11.282 64.755 54.605 1.00 22.20 ? 672 GLU A CA 1 ATOM 5181 C C . GLU A 1 631 ? 10.067 64.932 53.685 1.00 20.69 ? 672 GLU A C 1 ATOM 5182 O O . GLU A 1 631 ? 10.215 65.063 52.426 1.00 22.33 ? 672 GLU A O 1 ATOM 5183 C CB . GLU A 1 631 ? 11.487 63.252 54.889 1.00 20.89 ? 672 GLU A CB 1 ATOM 5184 C CG . GLU A 1 631 ? 12.106 62.535 53.686 1.00 21.33 ? 672 GLU A CG 1 ATOM 5185 C CD . GLU A 1 631 ? 13.622 62.856 53.599 1.00 27.85 ? 672 GLU A CD 1 ATOM 5186 O OE1 . GLU A 1 631 ? 14.368 62.480 54.539 1.00 26.26 ? 672 GLU A OE1 1 ATOM 5187 O OE2 . GLU A 1 631 ? 14.055 63.494 52.590 1.00 26.10 ? 672 GLU A OE2 1 ATOM 5188 N N . ARG A 1 632 ? 8.859 64.947 54.273 1.00 21.44 ? 673 ARG A N 1 ATOM 5189 C CA . ARG A 1 632 ? 7.624 65.039 53.486 1.00 21.94 ? 673 ARG A CA 1 ATOM 5190 C C . ARG A 1 632 ? 7.589 66.383 52.724 1.00 21.78 ? 673 ARG A C 1 ATOM 5191 O O . ARG A 1 632 ? 7.026 66.505 51.641 1.00 22.50 ? 673 ARG A O 1 ATOM 5192 C CB . ARG A 1 632 ? 6.375 64.937 54.409 1.00 23.44 ? 673 ARG A CB 1 ATOM 5193 C CG . ARG A 1 632 ? 5.201 64.231 53.755 1.00 26.03 ? 673 ARG A CG 1 ATOM 5194 C CD . ARG A 1 632 ? 5.368 62.684 53.886 1.00 25.94 ? 673 ARG A CD 1 ATOM 5195 N NE . ARG A 1 632 ? 4.965 62.161 55.210 1.00 21.89 ? 673 ARG A NE 1 ATOM 5196 C CZ . ARG A 1 632 ? 5.774 61.611 56.121 1.00 22.40 ? 673 ARG A CZ 1 ATOM 5197 N NH1 . ARG A 1 632 ? 7.101 61.518 55.915 1.00 22.56 ? 673 ARG A NH1 1 ATOM 5198 N NH2 . ARG A 1 632 ? 5.231 61.208 57.267 1.00 25.67 ? 673 ARG A NH2 1 ATOM 5199 N N . ALA A 1 633 ? 8.211 67.398 53.313 1.00 21.72 ? 674 ALA A N 1 ATOM 5200 C CA . ALA A 1 633 ? 8.178 68.735 52.713 1.00 22.00 ? 674 ALA A CA 1 ATOM 5201 C C . ALA A 1 633 ? 8.931 68.827 51.384 1.00 22.63 ? 674 ALA A C 1 ATOM 5202 O O . ALA A 1 633 ? 8.714 69.764 50.602 1.00 22.59 ? 674 ALA A O 1 ATOM 5203 C CB . ALA A 1 633 ? 8.723 69.740 53.728 1.00 22.75 ? 674 ALA A CB 1 ATOM 5204 N N . PHE A 1 634 ? 9.833 67.878 51.129 1.00 21.42 ? 675 PHE A N 1 ATOM 5205 C CA . PHE A 1 634 ? 10.547 67.867 49.860 1.00 21.63 ? 675 PHE A CA 1 ATOM 5206 C C . PHE A 1 634 ? 9.773 67.267 48.679 1.00 21.61 ? 675 PHE A C 1 ATOM 5207 O O . PHE A 1 634 ? 10.271 67.325 47.567 1.00 22.51 ? 675 PHE A O 1 ATOM 5208 C CB . PHE A 1 634 ? 11.868 67.192 50.000 1.00 21.60 ? 675 PHE A CB 1 ATOM 5209 C CG . PHE A 1 634 ? 12.835 67.974 50.882 1.00 23.18 ? 675 PHE A CG 1 ATOM 5210 C CD1 . PHE A 1 634 ? 13.269 69.248 50.526 1.00 22.01 ? 675 PHE A CD1 1 ATOM 5211 C CD2 . PHE A 1 634 ? 13.271 67.416 52.062 1.00 25.22 ? 675 PHE A CD2 1 ATOM 5212 C CE1 . PHE A 1 634 ? 14.175 69.967 51.372 1.00 21.66 ? 675 PHE A CE1 1 ATOM 5213 C CE2 . PHE A 1 634 ? 14.185 68.117 52.902 1.00 25.97 ? 675 PHE A CE2 1 ATOM 5214 C CZ . PHE A 1 634 ? 14.617 69.390 52.542 1.00 24.82 ? 675 PHE A CZ 1 ATOM 5215 N N . ILE A 1 635 ? 8.558 66.782 48.926 1.00 21.81 ? 676 ILE A N 1 ATOM 5216 C CA . ILE A 1 635 ? 7.691 66.174 47.903 1.00 21.95 ? 676 ILE A CA 1 ATOM 5217 C C . ILE A 1 635 ? 6.996 67.296 47.150 1.00 22.76 ? 676 ILE A C 1 ATOM 5218 O O . ILE A 1 635 ? 6.400 68.196 47.775 1.00 24.84 ? 676 ILE A O 1 ATOM 5219 C CB . ILE A 1 635 ? 6.620 65.255 48.598 1.00 20.87 ? 676 ILE A CB 1 ATOM 5220 C CG1 . ILE A 1 635 ? 7.405 64.076 49.278 1.00 22.67 ? 676 ILE A CG1 1 ATOM 5221 C CG2 . ILE A 1 635 ? 5.518 64.785 47.611 1.00 20.37 ? 676 ILE A CG2 1 ATOM 5222 C CD1 . ILE A 1 635 ? 8.301 63.194 48.256 1.00 23.12 ? 676 ILE A CD1 1 ATOM 5223 N N . ASP A 1 636 ? 7.090 67.270 45.817 1.00 22.36 ? 677 ASP A N 1 ATOM 5224 C CA . ASP A 1 636 ? 6.260 68.124 44.961 1.00 22.29 ? 677 ASP A CA 1 ATOM 5225 C C . ASP A 1 636 ? 5.086 67.274 44.449 1.00 22.51 ? 677 ASP A C 1 ATOM 5226 O O . ASP A 1 636 ? 5.309 66.242 43.800 1.00 22.07 ? 677 ASP A O 1 ATOM 5227 C CB . ASP A 1 636 ? 7.104 68.561 43.762 1.00 22.51 ? 677 ASP A CB 1 ATOM 5228 C CG . ASP A 1 636 ? 6.415 69.622 42.920 1.00 25.38 ? 677 ASP A CG 1 ATOM 5229 O OD1 . ASP A 1 636 ? 5.157 69.673 42.899 1.00 24.48 ? 677 ASP A OD1 1 ATOM 5230 O OD2 . ASP A 1 636 ? 7.172 70.408 42.305 1.00 27.02 ? 677 ASP A OD2 1 ATOM 5231 N N . PRO A 1 637 ? 3.846 67.659 44.740 1.00 23.67 ? 678 PRO A N 1 ATOM 5232 C CA . PRO A 1 637 ? 2.696 66.821 44.348 1.00 26.78 ? 678 PRO A CA 1 ATOM 5233 C C . PRO A 1 637 ? 2.556 66.747 42.806 1.00 27.33 ? 678 PRO A C 1 ATOM 5234 O O . PRO A 1 637 ? 1.863 65.862 42.283 1.00 30.72 ? 678 PRO A O 1 ATOM 5235 C CB . PRO A 1 637 ? 1.461 67.559 44.977 1.00 26.59 ? 678 PRO A CB 1 ATOM 5236 C CG . PRO A 1 637 ? 1.898 68.925 45.259 1.00 27.48 ? 678 PRO A CG 1 ATOM 5237 C CD . PRO A 1 637 ? 3.453 68.924 45.403 1.00 25.29 ? 678 PRO A CD 1 ATOM 5238 N N . LEU A 1 638 ? 3.264 67.616 42.070 1.00 24.40 ? 679 LEU A N 1 ATOM 5239 C CA . LEU A 1 638 ? 3.199 67.547 40.593 1.00 24.84 ? 679 LEU A CA 1 ATOM 5240 C C . LEU A 1 638 ? 4.247 66.583 40.011 1.00 25.47 ? 679 LEU A C 1 ATOM 5241 O O . LEU A 1 638 ? 4.230 66.300 38.814 1.00 24.59 ? 679 LEU A O 1 ATOM 5242 C CB . LEU A 1 638 ? 3.325 68.958 39.972 1.00 24.87 ? 679 LEU A CB 1 ATOM 5243 C CG . LEU A 1 638 ? 2.196 69.939 40.371 1.00 26.23 ? 679 LEU A CG 1 ATOM 5244 C CD1 . LEU A 1 638 ? 2.408 71.332 39.751 1.00 29.14 ? 679 LEU A CD1 1 ATOM 5245 C CD2 . LEU A 1 638 ? 0.770 69.384 39.960 1.00 28.79 ? 679 LEU A CD2 1 ATOM 5246 N N . GLY A 1 639 ? 5.113 66.028 40.878 1.00 24.29 ? 680 GLY A N 1 ATOM 5247 C CA . GLY A 1 639 ? 6.164 65.098 40.420 1.00 24.68 ? 680 GLY A CA 1 ATOM 5248 C C . GLY A 1 639 ? 7.258 65.761 39.587 1.00 26.70 ? 680 GLY A C 1 ATOM 5249 O O . GLY A 1 639 ? 7.230 66.954 39.338 1.00 27.84 ? 680 GLY A O 1 ATOM 5250 N N . LEU A 1 640 ? 8.233 64.984 39.132 1.00 26.04 ? 681 LEU A N 1 ATOM 5251 C CA . LEU A 1 640 ? 9.227 65.482 38.180 1.00 27.81 ? 681 LEU A CA 1 ATOM 5252 C C . LEU A 1 640 ? 8.716 65.365 36.740 1.00 28.46 ? 681 LEU A C 1 ATOM 5253 O O . LEU A 1 640 ? 7.782 64.575 36.462 1.00 28.60 ? 681 LEU A O 1 ATOM 5254 C CB . LEU A 1 640 ? 10.585 64.718 38.399 1.00 27.05 ? 681 LEU A CB 1 ATOM 5255 C CG . LEU A 1 640 ? 11.199 65.060 39.775 1.00 27.71 ? 681 LEU A CG 1 ATOM 5256 C CD1 . LEU A 1 640 ? 12.202 63.998 40.187 1.00 33.51 ? 681 LEU A CD1 1 ATOM 5257 C CD2 . LEU A 1 640 ? 11.868 66.519 39.846 1.00 31.80 ? 681 LEU A CD2 1 ATOM 5258 N N . PRO A 1 641 ? 9.315 66.116 35.783 1.00 31.14 ? 682 PRO A N 1 ATOM 5259 C CA . PRO A 1 641 ? 8.846 66.090 34.382 1.00 32.56 ? 682 PRO A CA 1 ATOM 5260 C C . PRO A 1 641 ? 8.765 64.687 33.790 1.00 32.71 ? 682 PRO A C 1 ATOM 5261 O O . PRO A 1 641 ? 9.757 63.970 33.764 1.00 33.58 ? 682 PRO A O 1 ATOM 5262 C CB . PRO A 1 641 ? 9.920 66.949 33.633 1.00 34.12 ? 682 PRO A CB 1 ATOM 5263 C CG . PRO A 1 641 ? 10.242 67.961 34.652 1.00 33.63 ? 682 PRO A CG 1 ATOM 5264 C CD . PRO A 1 641 ? 10.328 67.182 35.973 1.00 31.87 ? 682 PRO A CD 1 ATOM 5265 N N . ASP A 1 642 ? 7.569 64.316 33.346 1.00 33.71 ? 683 ASP A N 1 ATOM 5266 C CA . ASP A 1 642 ? 7.254 62.992 32.793 1.00 34.52 ? 683 ASP A CA 1 ATOM 5267 C C . ASP A 1 642 ? 7.549 61.838 33.733 1.00 32.67 ? 683 ASP A C 1 ATOM 5268 O O . ASP A 1 642 ? 7.524 60.686 33.285 1.00 31.69 ? 683 ASP A O 1 ATOM 5269 C CB . ASP A 1 642 ? 7.981 62.722 31.482 1.00 37.88 ? 683 ASP A CB 1 ATOM 5270 C CG . ASP A 1 642 ? 7.707 63.793 30.455 1.00 44.20 ? 683 ASP A CG 1 ATOM 5271 O OD1 . ASP A 1 642 ? 6.508 64.060 30.203 1.00 47.13 ? 683 ASP A OD1 1 ATOM 5272 O OD2 . ASP A 1 642 ? 8.697 64.387 29.968 1.00 51.17 ? 683 ASP A OD2 1 ATOM 5273 N N . ARG A 1 643 ? 7.804 62.140 35.013 1.00 29.38 ? 684 ARG A N 1 ATOM 5274 C CA . ARG A 1 643 ? 7.975 61.076 36.024 1.00 26.84 ? 684 ARG A CA 1 ATOM 5275 C C . ARG A 1 643 ? 7.108 61.414 37.251 1.00 25.29 ? 684 ARG A C 1 ATOM 5276 O O . ARG A 1 643 ? 7.641 61.765 38.308 1.00 23.61 ? 684 ARG A O 1 ATOM 5277 C CB . ARG A 1 643 ? 9.462 60.879 36.396 1.00 27.25 ? 684 ARG A CB 1 ATOM 5278 C CG . ARG A 1 643 ? 10.330 60.422 35.135 1.00 26.84 ? 684 ARG A CG 1 ATOM 5279 C CD . ARG A 1 643 ? 11.779 59.998 35.490 1.00 31.78 ? 684 ARG A CD 1 ATOM 5280 N NE . ARG A 1 643 ? 12.531 61.096 36.151 1.00 27.74 ? 684 ARG A NE 1 ATOM 5281 C CZ . ARG A 1 643 ? 13.707 60.959 36.783 1.00 33.43 ? 684 ARG A CZ 1 ATOM 5282 N NH1 . ARG A 1 643 ? 14.319 59.756 36.886 1.00 28.45 ? 684 ARG A NH1 1 ATOM 5283 N NH2 . ARG A 1 643 ? 14.297 62.052 37.317 1.00 31.84 ? 684 ARG A NH2 1 ATOM 5284 N N . PRO A 1 644 ? 5.802 61.225 37.129 1.00 25.34 ? 685 PRO A N 1 ATOM 5285 C CA . PRO A 1 644 ? 4.877 61.670 38.187 1.00 25.70 ? 685 PRO A CA 1 ATOM 5286 C C . PRO A 1 644 ? 5.013 60.934 39.511 1.00 24.32 ? 685 PRO A C 1 ATOM 5287 O O . PRO A 1 644 ? 4.544 61.462 40.541 1.00 23.42 ? 685 PRO A O 1 ATOM 5288 C CB . PRO A 1 644 ? 3.483 61.412 37.564 1.00 27.15 ? 685 PRO A CB 1 ATOM 5289 C CG . PRO A 1 644 ? 3.732 60.316 36.490 1.00 28.22 ? 685 PRO A CG 1 ATOM 5290 C CD . PRO A 1 644 ? 5.078 60.697 35.936 1.00 26.16 ? 685 PRO A CD 1 ATOM 5291 N N . PHE A 1 645 ? 5.638 59.749 39.513 1.00 22.05 ? 686 PHE A N 1 ATOM 5292 C CA . PHE A 1 645 ? 5.799 59.003 40.744 1.00 21.60 ? 686 PHE A CA 1 ATOM 5293 C C . PHE A 1 645 ? 7.144 59.233 41.402 1.00 21.28 ? 686 PHE A C 1 ATOM 5294 O O . PHE A 1 645 ? 7.398 58.699 42.478 1.00 21.36 ? 686 PHE A O 1 ATOM 5295 C CB . PHE A 1 645 ? 5.504 57.489 40.548 1.00 22.10 ? 686 PHE A CB 1 ATOM 5296 C CG . PHE A 1 645 ? 4.116 57.255 40.048 1.00 22.63 ? 686 PHE A CG 1 ATOM 5297 C CD1 . PHE A 1 645 ? 3.012 57.611 40.852 1.00 23.85 ? 686 PHE A CD1 1 ATOM 5298 C CD2 . PHE A 1 645 ? 3.901 56.732 38.775 1.00 25.45 ? 686 PHE A CD2 1 ATOM 5299 C CE1 . PHE A 1 645 ? 1.735 57.436 40.357 1.00 23.45 ? 686 PHE A CE1 1 ATOM 5300 C CE2 . PHE A 1 645 ? 2.603 56.577 38.276 1.00 25.40 ? 686 PHE A CE2 1 ATOM 5301 C CZ . PHE A 1 645 ? 1.534 56.914 39.076 1.00 24.24 ? 686 PHE A CZ 1 ATOM 5302 N N . TYR A 1 646 ? 8.000 60.060 40.783 1.00 20.45 ? 687 TYR A N 1 ATOM 5303 C CA . TYR A 1 646 ? 9.192 60.506 41.507 1.00 21.46 ? 687 TYR A CA 1 ATOM 5304 C C . TYR A 1 646 ? 8.914 61.946 41.916 1.00 21.88 ? 687 TYR A C 1 ATOM 5305 O O . TYR A 1 646 ? 8.915 62.845 41.076 1.00 24.20 ? 687 TYR A O 1 ATOM 5306 C CB . TYR A 1 646 ? 10.446 60.481 40.591 1.00 23.22 ? 687 TYR A CB 1 ATOM 5307 C CG . TYR A 1 646 ? 10.930 59.062 40.296 1.00 21.98 ? 687 TYR A CG 1 ATOM 5308 C CD1 . TYR A 1 646 ? 10.719 58.007 41.229 1.00 23.76 ? 687 TYR A CD1 1 ATOM 5309 C CD2 . TYR A 1 646 ? 11.648 58.784 39.147 1.00 24.71 ? 687 TYR A CD2 1 ATOM 5310 C CE1 . TYR A 1 646 ? 11.150 56.682 40.950 1.00 24.38 ? 687 TYR A CE1 1 ATOM 5311 C CE2 . TYR A 1 646 ? 12.102 57.448 38.871 1.00 25.63 ? 687 TYR A CE2 1 ATOM 5312 C CZ . TYR A 1 646 ? 11.857 56.438 39.790 1.00 26.60 ? 687 TYR A CZ 1 ATOM 5313 O OH . TYR A 1 646 ? 12.335 55.165 39.526 1.00 27.76 ? 687 TYR A OH 1 ATOM 5314 N N . ARG A 1 647 ? 8.683 62.180 43.207 1.00 19.30 ? 688 ARG A N 1 ATOM 5315 C CA . ARG A 1 647 ? 8.113 63.491 43.619 1.00 19.58 ? 688 ARG A CA 1 ATOM 5316 C C . ARG A 1 647 ? 9.096 64.255 44.521 1.00 20.41 ? 688 ARG A C 1 ATOM 5317 O O . ARG A 1 647 ? 8.818 65.385 44.888 1.00 20.65 ? 688 ARG A O 1 ATOM 5318 C CB A ARG A 1 647 ? 6.817 63.258 44.378 0.65 19.41 ? 688 ARG A CB 1 ATOM 5319 C CB B ARG A 1 647 ? 6.865 63.230 44.452 0.35 20.30 ? 688 ARG A CB 1 ATOM 5320 C CG A ARG A 1 647 ? 5.799 62.528 43.456 0.65 17.42 ? 688 ARG A CG 1 ATOM 5321 C CG B ARG A 1 647 ? 5.909 62.241 43.799 0.35 24.01 ? 688 ARG A CG 1 ATOM 5322 C CD A ARG A 1 647 ? 4.383 62.680 43.963 0.65 18.32 ? 688 ARG A CD 1 ATOM 5323 C CD B ARG A 1 647 ? 4.653 62.912 43.350 0.35 30.90 ? 688 ARG A CD 1 ATOM 5324 N NE A ARG A 1 647 ? 4.230 62.249 45.322 0.65 14.59 ? 688 ARG A NE 1 ATOM 5325 N NE B ARG A 1 647 ? 3.554 62.013 43.641 0.35 33.93 ? 688 ARG A NE 1 ATOM 5326 C CZ A ARG A 1 647 ? 3.155 62.519 46.084 0.65 21.74 ? 688 ARG A CZ 1 ATOM 5327 C CZ B ARG A 1 647 ? 3.005 61.927 44.846 0.35 36.98 ? 688 ARG A CZ 1 ATOM 5328 N NH1 A ARG A 1 647 ? 3.163 62.100 47.366 0.65 15.43 ? 688 ARG A NH1 1 ATOM 5329 N NH1 B ARG A 1 647 ? 2.025 61.070 45.075 0.35 36.14 ? 688 ARG A NH1 1 ATOM 5330 N NH2 A ARG A 1 647 ? 2.091 63.211 45.573 0.65 17.01 ? 688 ARG A NH2 1 ATOM 5331 N NH2 B ARG A 1 647 ? 3.444 62.703 45.826 0.35 39.21 ? 688 ARG A NH2 1 ATOM 5332 N N . HIS A 1 648 ? 10.178 63.591 44.925 1.00 19.74 ? 689 HIS A N 1 ATOM 5333 C CA . HIS A 1 648 ? 11.116 64.212 45.920 1.00 20.24 ? 689 HIS A CA 1 ATOM 5334 C C . HIS A 1 648 ? 11.981 65.194 45.072 1.00 20.89 ? 689 HIS A C 1 ATOM 5335 O O . HIS A 1 648 ? 12.589 64.798 44.088 1.00 23.58 ? 689 HIS A O 1 ATOM 5336 C CB . HIS A 1 648 ? 12.042 63.168 46.530 1.00 20.90 ? 689 HIS A CB 1 ATOM 5337 C CG . HIS A 1 648 ? 12.708 63.605 47.812 1.00 22.51 ? 689 HIS A CG 1 ATOM 5338 N ND1 . HIS A 1 648 ? 13.663 64.593 47.882 1.00 20.47 ? 689 HIS A ND1 1 ATOM 5339 C CD2 . HIS A 1 648 ? 12.541 63.154 49.078 1.00 21.42 ? 689 HIS A CD2 1 ATOM 5340 C CE1 . HIS A 1 648 ? 14.068 64.737 49.141 1.00 24.14 ? 689 HIS A CE1 1 ATOM 5341 N NE2 . HIS A 1 648 ? 13.397 63.869 49.890 1.00 23.42 ? 689 HIS A NE2 1 ATOM 5342 N N . VAL A 1 649 ? 12.072 66.444 45.477 1.00 20.10 ? 690 VAL A N 1 ATOM 5343 C CA . VAL A 1 649 ? 12.736 67.458 44.651 1.00 21.08 ? 690 VAL A CA 1 ATOM 5344 C C . VAL A 1 649 ? 14.264 67.435 44.873 1.00 22.73 ? 690 VAL A C 1 ATOM 5345 O O . VAL A 1 649 ? 15.037 67.951 44.044 1.00 22.17 ? 690 VAL A O 1 ATOM 5346 C CB . VAL A 1 649 ? 12.100 68.861 45.003 1.00 22.76 ? 690 VAL A CB 1 ATOM 5347 C CG1 . VAL A 1 649 ? 12.884 70.058 44.371 1.00 22.33 ? 690 VAL A CG1 1 ATOM 5348 C CG2 . VAL A 1 649 ? 10.652 68.917 44.547 1.00 20.66 ? 690 VAL A CG2 1 ATOM 5349 N N . ILE A 1 650 ? 14.711 66.913 46.017 1.00 21.70 ? 691 ILE A N 1 ATOM 5350 C CA . ILE A 1 650 ? 16.155 66.894 46.258 1.00 22.93 ? 691 ILE A CA 1 ATOM 5351 C C . ILE A 1 650 ? 16.784 65.675 45.639 1.00 22.87 ? 691 ILE A C 1 ATOM 5352 O O . ILE A 1 650 ? 17.891 65.738 45.153 1.00 24.74 ? 691 ILE A O 1 ATOM 5353 C CB . ILE A 1 650 ? 16.487 66.933 47.791 1.00 22.60 ? 691 ILE A CB 1 ATOM 5354 C CG1 . ILE A 1 650 ? 15.710 68.059 48.459 1.00 22.73 ? 691 ILE A CG1 1 ATOM 5355 C CG2 . ILE A 1 650 ? 18.041 67.106 48.065 1.00 25.01 ? 691 ILE A CG2 1 ATOM 5356 C CD1 . ILE A 1 650 ? 15.838 69.484 47.787 1.00 23.70 ? 691 ILE A CD1 1 ATOM 5357 N N . TYR A 1 651 ? 16.095 64.536 45.705 1.00 23.39 ? 692 TYR A N 1 ATOM 5358 C CA . TYR A 1 651 ? 16.668 63.267 45.280 1.00 25.18 ? 692 TYR A CA 1 ATOM 5359 C C . TYR A 1 651 ? 15.744 62.595 44.253 1.00 26.71 ? 692 TYR A C 1 ATOM 5360 O O . TYR A 1 651 ? 14.548 62.605 44.413 1.00 29.45 ? 692 TYR A O 1 ATOM 5361 C CB . TYR A 1 651 ? 16.843 62.313 46.497 1.00 23.43 ? 692 TYR A CB 1 ATOM 5362 C CG . TYR A 1 651 ? 17.839 62.771 47.546 1.00 26.20 ? 692 TYR A CG 1 ATOM 5363 C CD1 . TYR A 1 651 ? 19.215 62.832 47.248 1.00 26.49 ? 692 TYR A CD1 1 ATOM 5364 C CD2 . TYR A 1 651 ? 17.416 63.086 48.856 1.00 26.70 ? 692 TYR A CD2 1 ATOM 5365 C CE1 . TYR A 1 651 ? 20.141 63.209 48.205 1.00 26.01 ? 692 TYR A CE1 1 ATOM 5366 C CE2 . TYR A 1 651 ? 18.347 63.479 49.834 1.00 25.11 ? 692 TYR A CE2 1 ATOM 5367 C CZ . TYR A 1 651 ? 19.683 63.522 49.501 1.00 27.40 ? 692 TYR A CZ 1 ATOM 5368 O OH . TYR A 1 651 ? 20.655 63.856 50.422 1.00 28.96 ? 692 TYR A OH 1 ATOM 5369 N N . ALA A 1 652 ? 16.303 61.994 43.217 1.00 27.97 ? 693 ALA A N 1 ATOM 5370 C CA . ALA A 1 652 ? 15.518 61.050 42.402 1.00 27.84 ? 693 ALA A CA 1 ATOM 5371 C C . ALA A 1 652 ? 16.515 60.044 41.861 1.00 28.17 ? 693 ALA A C 1 ATOM 5372 O O . ALA A 1 652 ? 17.737 60.316 41.791 1.00 28.37 ? 693 ALA A O 1 ATOM 5373 C CB . ALA A 1 652 ? 14.805 61.733 41.280 1.00 28.48 ? 693 ALA A CB 1 ATOM 5374 N N . PRO A 1 653 ? 16.028 58.872 41.490 1.00 27.96 ? 694 PRO A N 1 ATOM 5375 C CA . PRO A 1 653 ? 16.933 57.934 40.787 1.00 27.91 ? 694 PRO A CA 1 ATOM 5376 C C . PRO A 1 653 ? 17.404 58.600 39.520 1.00 28.60 ? 694 PRO A C 1 ATOM 5377 O O . PRO A 1 653 ? 16.640 59.360 38.882 1.00 28.08 ? 694 PRO A O 1 ATOM 5378 C CB . PRO A 1 653 ? 16.023 56.745 40.441 1.00 27.27 ? 694 PRO A CB 1 ATOM 5379 C CG . PRO A 1 653 ? 14.910 56.844 41.441 1.00 25.99 ? 694 PRO A CG 1 ATOM 5380 C CD . PRO A 1 653 ? 14.648 58.361 41.582 1.00 27.08 ? 694 PRO A CD 1 ATOM 5381 N N . SER A 1 654 ? 18.692 58.416 39.208 1.00 28.40 ? 695 SER A N 1 ATOM 5382 C CA . SER A 1 654 ? 19.267 59.001 38.013 1.00 28.85 ? 695 SER A CA 1 ATOM 5383 C C . SER A 1 654 ? 18.513 58.496 36.761 1.00 30.34 ? 695 SER A C 1 ATOM 5384 O O . SER A 1 654 ? 18.237 57.300 36.641 1.00 29.37 ? 695 SER A O 1 ATOM 5385 C CB . SER A 1 654 ? 20.756 58.592 37.885 1.00 28.95 ? 695 SER A CB 1 ATOM 5386 O OG . SER A 1 654 ? 21.208 58.935 36.584 1.00 29.70 ? 695 SER A OG 1 ATOM 5387 N N . SER A 1 655 ? 18.162 59.431 35.866 1.00 30.33 ? 696 SER A N 1 ATOM 5388 C CA A SER A 1 655 ? 17.544 59.074 34.589 0.50 29.41 ? 696 SER A CA 1 ATOM 5389 C CA B SER A 1 655 ? 17.600 59.149 34.552 0.50 32.08 ? 696 SER A CA 1 ATOM 5390 C C . SER A 1 655 ? 18.459 58.188 33.722 1.00 31.28 ? 696 SER A C 1 ATOM 5391 O O . SER A 1 655 ? 17.985 57.581 32.748 1.00 33.00 ? 696 SER A O 1 ATOM 5392 C CB A SER A 1 655 ? 17.146 60.339 33.810 0.50 28.74 ? 696 SER A CB 1 ATOM 5393 C CB B SER A 1 655 ? 17.492 60.470 33.781 0.50 31.97 ? 696 SER A CB 1 ATOM 5394 O OG A SER A 1 655 ? 16.129 61.050 34.489 0.50 17.24 ? 696 SER A OG 1 ATOM 5395 O OG B SER A 1 655 ? 16.576 60.330 32.732 0.50 37.02 ? 696 SER A OG 1 ATOM 5396 N N . HIS A 1 656 ? 19.731 58.082 34.068 1.00 32.01 ? 697 HIS A N 1 ATOM 5397 C CA . HIS A 1 656 ? 20.670 57.241 33.281 1.00 33.54 ? 697 HIS A CA 1 ATOM 5398 C C . HIS A 1 656 ? 21.027 55.965 33.993 1.00 33.65 ? 697 HIS A C 1 ATOM 5399 O O . HIS A 1 656 ? 21.698 55.108 33.426 1.00 33.57 ? 697 HIS A O 1 ATOM 5400 C CB . HIS A 1 656 ? 21.944 58.052 32.972 1.00 34.87 ? 697 HIS A CB 1 ATOM 5401 C CG . HIS A 1 656 ? 21.620 59.354 32.320 1.00 38.37 ? 697 HIS A CG 1 ATOM 5402 N ND1 . HIS A 1 656 ? 21.289 59.442 30.981 1.00 42.29 ? 697 HIS A ND1 1 ATOM 5403 C CD2 . HIS A 1 656 ? 21.412 60.585 32.841 1.00 44.06 ? 697 HIS A CD2 1 ATOM 5404 C CE1 . HIS A 1 656 ? 20.958 60.691 30.695 1.00 46.69 ? 697 HIS A CE1 1 ATOM 5405 N NE2 . HIS A 1 656 ? 21.033 61.407 31.805 1.00 44.45 ? 697 HIS A NE2 1 ATOM 5406 N N . ASN A 1 657 ? 20.616 55.849 35.260 1.00 31.51 ? 698 ASN A N 1 ATOM 5407 C CA . ASN A 1 657 ? 21.027 54.688 36.074 1.00 31.16 ? 698 ASN A CA 1 ATOM 5408 C C . ASN A 1 657 ? 20.134 54.676 37.290 1.00 30.29 ? 698 ASN A C 1 ATOM 5409 O O . ASN A 1 657 ? 20.440 55.323 38.281 1.00 30.29 ? 698 ASN A O 1 ATOM 5410 C CB . ASN A 1 657 ? 22.530 54.778 36.525 1.00 31.70 ? 698 ASN A CB 1 ATOM 5411 C CG . ASN A 1 657 ? 22.939 53.647 37.472 1.00 31.74 ? 698 ASN A CG 1 ATOM 5412 O OD1 . ASN A 1 657 ? 22.210 52.667 37.622 1.00 30.30 ? 698 ASN A OD1 1 ATOM 5413 N ND2 . ASN A 1 657 ? 24.110 53.775 38.116 1.00 28.26 ? 698 ASN A ND2 1 ATOM 5414 N N . LYS A 1 658 ? 19.065 53.884 37.244 1.00 29.91 ? 699 LYS A N 1 ATOM 5415 C CA . LYS A 1 658 ? 18.103 53.861 38.326 1.00 29.94 ? 699 LYS A CA 1 ATOM 5416 C C . LYS A 1 658 ? 18.712 53.555 39.711 1.00 29.13 ? 699 LYS A C 1 ATOM 5417 O O . LYS A 1 658 ? 18.167 53.987 40.722 1.00 27.31 ? 699 LYS A O 1 ATOM 5418 C CB . LYS A 1 658 ? 17.050 52.811 37.957 1.00 31.74 ? 699 LYS A CB 1 ATOM 5419 C CG . LYS A 1 658 ? 16.188 52.346 39.035 1.00 36.51 ? 699 LYS A CG 1 ATOM 5420 C CD . LYS A 1 658 ? 15.078 51.458 38.429 1.00 37.41 ? 699 LYS A CD 1 ATOM 5421 C CE . LYS A 1 658 ? 13.778 51.633 39.226 1.00 40.90 ? 699 LYS A CE 1 ATOM 5422 N NZ . LYS A 1 658 ? 12.665 50.782 38.717 1.00 43.60 ? 699 LYS A NZ 1 ATOM 5423 N N . TYR A 1 659 ? 19.814 52.803 39.755 1.00 28.17 ? 700 TYR A N 1 ATOM 5424 C CA . TYR A 1 659 ? 20.462 52.490 41.037 1.00 29.16 ? 700 TYR A CA 1 ATOM 5425 C C . TYR A 1 659 ? 21.089 53.711 41.755 1.00 29.74 ? 700 TYR A C 1 ATOM 5426 O O . TYR A 1 659 ? 21.225 53.680 42.967 1.00 30.26 ? 700 TYR A O 1 ATOM 5427 C CB . TYR A 1 659 ? 21.593 51.499 40.826 1.00 29.04 ? 700 TYR A CB 1 ATOM 5428 C CG . TYR A 1 659 ? 21.193 50.107 40.377 1.00 30.94 ? 700 TYR A CG 1 ATOM 5429 C CD1 . TYR A 1 659 ? 20.057 49.479 40.893 1.00 31.77 ? 700 TYR A CD1 1 ATOM 5430 C CD2 . TYR A 1 659 ? 22.003 49.401 39.457 1.00 31.31 ? 700 TYR A CD2 1 ATOM 5431 C CE1 . TYR A 1 659 ? 19.698 48.148 40.468 1.00 33.47 ? 700 TYR A CE1 1 ATOM 5432 C CE2 . TYR A 1 659 ? 21.688 48.075 39.041 1.00 33.11 ? 700 TYR A CE2 1 ATOM 5433 C CZ . TYR A 1 659 ? 20.545 47.469 39.567 1.00 34.37 ? 700 TYR A CZ 1 ATOM 5434 O OH . TYR A 1 659 ? 20.241 46.199 39.169 1.00 33.38 ? 700 TYR A OH 1 ATOM 5435 N N . ALA A 1 660 ? 21.538 54.714 40.986 1.00 29.30 ? 701 ALA A N 1 ATOM 5436 C CA . ALA A 1 660 ? 22.268 55.879 41.541 1.00 30.34 ? 701 ALA A CA 1 ATOM 5437 C C . ALA A 1 660 ? 21.273 56.983 41.980 1.00 31.00 ? 701 ALA A C 1 ATOM 5438 O O . ALA A 1 660 ? 20.338 57.284 41.246 1.00 31.10 ? 701 ALA A O 1 ATOM 5439 C CB . ALA A 1 660 ? 23.233 56.439 40.482 1.00 31.60 ? 701 ALA A CB 1 ATOM 5440 N N . GLY A 1 661 ? 21.488 57.612 43.140 1.00 30.38 ? 702 GLY A N 1 ATOM 5441 C CA . GLY A 1 661 ? 20.687 58.799 43.492 1.00 30.29 ? 702 GLY A CA 1 ATOM 5442 C C . GLY A 1 661 ? 21.241 59.991 42.722 1.00 30.70 ? 702 GLY A C 1 ATOM 5443 O O . GLY A 1 661 ? 22.459 60.054 42.514 1.00 32.08 ? 702 GLY A O 1 ATOM 5444 N N . GLU A 1 662 ? 20.379 60.899 42.244 1.00 29.26 ? 703 GLU A N 1 ATOM 5445 C CA . GLU A 1 662 ? 20.838 62.161 41.671 1.00 29.53 ? 703 GLU A CA 1 ATOM 5446 C C . GLU A 1 662 ? 20.319 63.300 42.559 1.00 28.20 ? 703 GLU A C 1 ATOM 5447 O O . GLU A 1 662 ? 19.157 63.222 42.925 1.00 28.03 ? 703 GLU A O 1 ATOM 5448 C CB . GLU A 1 662 ? 20.259 62.378 40.249 1.00 30.83 ? 703 GLU A CB 1 ATOM 5449 C CG . GLU A 1 662 ? 20.885 63.666 39.571 1.00 31.85 ? 703 GLU A CG 1 ATOM 5450 C CD . GLU A 1 662 ? 22.441 63.619 39.596 1.00 36.99 ? 703 GLU A CD 1 ATOM 5451 O OE1 . GLU A 1 662 ? 23.002 62.785 38.853 1.00 35.33 ? 703 GLU A OE1 1 ATOM 5452 O OE2 . GLU A 1 662 ? 23.096 64.364 40.388 1.00 37.75 ? 703 GLU A OE2 1 ATOM 5453 N N . SER A 1 663 ? 21.123 64.353 42.852 1.00 27.03 ? 704 SER A N 1 ATOM 5454 C CA A SER A 1 663 ? 20.608 65.487 43.624 0.50 24.33 ? 704 SER A CA 1 ATOM 5455 C CA B SER A 1 663 ? 20.530 65.460 43.601 0.50 26.07 ? 704 SER A CA 1 ATOM 5456 C C . SER A 1 663 ? 20.092 66.594 42.706 1.00 25.53 ? 704 SER A C 1 ATOM 5457 O O . SER A 1 663 ? 20.625 66.771 41.626 1.00 26.52 ? 704 SER A O 1 ATOM 5458 C CB A SER A 1 663 ? 21.648 66.030 44.604 0.50 25.43 ? 704 SER A CB 1 ATOM 5459 C CB B SER A 1 663 ? 21.415 65.966 44.712 0.50 26.70 ? 704 SER A CB 1 ATOM 5460 O OG A SER A 1 663 ? 22.917 66.232 43.985 0.50 19.27 ? 704 SER A OG 1 ATOM 5461 O OG B SER A 1 663 ? 21.902 64.877 45.450 0.50 31.66 ? 704 SER A OG 1 ATOM 5462 N N . PHE A 1 664 ? 19.099 67.365 43.196 1.00 23.71 ? 705 PHE A N 1 ATOM 5463 C CA . PHE A 1 664 ? 18.351 68.353 42.357 1.00 22.40 ? 705 PHE A CA 1 ATOM 5464 C C . PHE A 1 664 ? 18.105 67.802 40.957 1.00 22.12 ? 705 PHE A C 1 ATOM 5465 O O . PHE A 1 664 ? 18.515 68.390 39.954 1.00 21.92 ? 705 PHE A O 1 ATOM 5466 C CB . PHE A 1 664 ? 19.074 69.697 42.311 1.00 23.40 ? 705 PHE A CB 1 ATOM 5467 C CG . PHE A 1 664 ? 19.035 70.441 43.634 1.00 24.08 ? 705 PHE A CG 1 ATOM 5468 C CD1 . PHE A 1 664 ? 17.800 70.730 44.252 1.00 23.20 ? 705 PHE A CD1 1 ATOM 5469 C CD2 . PHE A 1 664 ? 20.228 70.839 44.259 1.00 23.75 ? 705 PHE A CD2 1 ATOM 5470 C CE1 . PHE A 1 664 ? 17.744 71.417 45.483 1.00 24.48 ? 705 PHE A CE1 1 ATOM 5471 C CE2 . PHE A 1 664 ? 20.204 71.504 45.480 1.00 25.07 ? 705 PHE A CE2 1 ATOM 5472 C CZ . PHE A 1 664 ? 18.947 71.834 46.090 1.00 24.61 ? 705 PHE A CZ 1 ATOM 5473 N N . PRO A 1 665 ? 17.397 66.658 40.884 1.00 22.29 ? 706 PRO A N 1 ATOM 5474 C CA . PRO A 1 665 ? 17.269 65.932 39.616 1.00 21.99 ? 706 PRO A CA 1 ATOM 5475 C C . PRO A 1 665 ? 16.520 66.722 38.579 1.00 21.98 ? 706 PRO A C 1 ATOM 5476 O O . PRO A 1 665 ? 16.780 66.543 37.398 1.00 23.54 ? 706 PRO A O 1 ATOM 5477 C CB . PRO A 1 665 ? 16.442 64.656 40.008 1.00 21.82 ? 706 PRO A CB 1 ATOM 5478 C CG . PRO A 1 665 ? 15.734 65.058 41.315 1.00 22.69 ? 706 PRO A CG 1 ATOM 5479 C CD . PRO A 1 665 ? 16.809 65.932 42.017 1.00 21.23 ? 706 PRO A CD 1 ATOM 5480 N N . GLY A 1 666 ? 15.591 67.615 38.984 1.00 20.85 ? 707 GLY A N 1 ATOM 5481 C CA . GLY A 1 666 ? 14.854 68.383 37.956 1.00 21.82 ? 707 GLY A CA 1 ATOM 5482 C C . GLY A 1 666 ? 15.822 69.313 37.197 1.00 22.46 ? 707 GLY A C 1 ATOM 5483 O O . GLY A 1 666 ? 15.763 69.445 35.928 1.00 22.79 ? 707 GLY A O 1 ATOM 5484 N N . ILE A 1 667 ? 16.714 69.967 37.957 1.00 22.00 ? 708 ILE A N 1 ATOM 5485 C CA . ILE A 1 667 ? 17.671 70.887 37.329 1.00 22.52 ? 708 ILE A CA 1 ATOM 5486 C C . ILE A 1 667 ? 18.718 70.057 36.573 1.00 23.29 ? 708 ILE A C 1 ATOM 5487 O O . ILE A 1 667 ? 19.122 70.412 35.455 1.00 24.67 ? 708 ILE A O 1 ATOM 5488 C CB . ILE A 1 667 ? 18.412 71.760 38.370 1.00 22.22 ? 708 ILE A CB 1 ATOM 5489 C CG1 . ILE A 1 667 ? 17.405 72.520 39.284 1.00 23.05 ? 708 ILE A CG1 1 ATOM 5490 C CG2 . ILE A 1 667 ? 19.310 72.812 37.642 1.00 24.43 ? 708 ILE A CG2 1 ATOM 5491 C CD1 . ILE A 1 667 ? 18.086 73.284 40.519 1.00 23.76 ? 708 ILE A CD1 1 ATOM 5492 N N . TYR A 1 668 ? 19.135 68.953 37.168 1.00 22.08 ? 709 TYR A N 1 ATOM 5493 C CA . TYR A 1 668 ? 20.198 68.129 36.523 1.00 24.74 ? 709 TYR A CA 1 ATOM 5494 C C . TYR A 1 668 ? 19.736 67.663 35.126 1.00 24.50 ? 709 TYR A C 1 ATOM 5495 O O . TYR A 1 668 ? 20.454 67.827 34.122 1.00 26.15 ? 709 TYR A O 1 ATOM 5496 C CB . TYR A 1 668 ? 20.561 66.936 37.406 1.00 24.46 ? 709 TYR A CB 1 ATOM 5497 C CG . TYR A 1 668 ? 21.662 66.103 36.754 1.00 26.00 ? 709 TYR A CG 1 ATOM 5498 C CD1 . TYR A 1 668 ? 22.995 66.309 37.064 1.00 30.62 ? 709 TYR A CD1 1 ATOM 5499 C CD2 . TYR A 1 668 ? 21.338 65.127 35.785 1.00 29.43 ? 709 TYR A CD2 1 ATOM 5500 C CE1 . TYR A 1 668 ? 24.055 65.544 36.425 1.00 31.76 ? 709 TYR A CE1 1 ATOM 5501 C CE2 . TYR A 1 668 ? 22.382 64.368 35.139 1.00 27.80 ? 709 TYR A CE2 1 ATOM 5502 C CZ . TYR A 1 668 ? 23.718 64.590 35.479 1.00 33.44 ? 709 TYR A CZ 1 ATOM 5503 O OH . TYR A 1 668 ? 24.736 63.847 34.865 1.00 31.19 ? 709 TYR A OH 1 ATOM 5504 N N . ASP A 1 669 ? 18.539 67.078 35.066 1.00 25.79 ? 710 ASP A N 1 ATOM 5505 C CA . ASP A 1 669 ? 17.992 66.637 33.784 1.00 26.45 ? 710 ASP A CA 1 ATOM 5506 C C . ASP A 1 669 ? 17.746 67.777 32.805 1.00 27.26 ? 710 ASP A C 1 ATOM 5507 O O . ASP A 1 669 ? 17.972 67.619 31.594 1.00 26.79 ? 710 ASP A O 1 ATOM 5508 C CB . ASP A 1 669 ? 16.717 65.819 34.008 1.00 25.15 ? 710 ASP A CB 1 ATOM 5509 C CG . ASP A 1 669 ? 17.014 64.427 34.512 1.00 29.84 ? 710 ASP A CG 1 ATOM 5510 O OD1 . ASP A 1 669 ? 18.192 63.963 34.434 1.00 30.20 ? 710 ASP A OD1 1 ATOM 5511 O OD2 . ASP A 1 669 ? 16.074 63.801 35.022 1.00 32.94 ? 710 ASP A OD2 1 ATOM 5512 N N . ALA A 1 670 ? 17.342 68.952 33.292 1.00 26.23 ? 711 ALA A N 1 ATOM 5513 C CA . ALA A 1 670 ? 17.194 70.110 32.370 1.00 26.80 ? 711 ALA A CA 1 ATOM 5514 C C . ALA A 1 670 ? 18.547 70.530 31.761 1.00 27.62 ? 711 ALA A C 1 ATOM 5515 O O . ALA A 1 670 ? 18.613 70.968 30.611 1.00 28.50 ? 711 ALA A O 1 ATOM 5516 C CB . ALA A 1 670 ? 16.537 71.319 33.123 1.00 26.55 ? 711 ALA A CB 1 ATOM 5517 N N . LEU A 1 671 ? 19.627 70.384 32.521 1.00 26.45 ? 712 LEU A N 1 ATOM 5518 C CA . LEU A 1 671 ? 20.989 70.755 32.009 1.00 27.92 ? 712 LEU A CA 1 ATOM 5519 C C . LEU A 1 671 ? 21.650 69.649 31.183 1.00 29.08 ? 712 LEU A C 1 ATOM 5520 O O . LEU A 1 671 ? 22.593 69.883 30.416 1.00 30.09 ? 712 LEU A O 1 ATOM 5521 C CB . LEU A 1 671 ? 21.894 71.060 33.201 1.00 28.17 ? 712 LEU A CB 1 ATOM 5522 C CG . LEU A 1 671 ? 21.618 72.421 33.868 1.00 29.02 ? 712 LEU A CG 1 ATOM 5523 C CD1 . LEU A 1 671 ? 22.354 72.418 35.226 1.00 28.04 ? 712 LEU A CD1 1 ATOM 5524 C CD2 . LEU A 1 671 ? 22.118 73.534 32.950 1.00 30.08 ? 712 LEU A CD2 1 ATOM 5525 N N . PHE A 1 672 ? 21.146 68.435 31.329 1.00 30.16 ? 713 PHE A N 1 ATOM 5526 C CA . PHE A 1 672 ? 21.894 67.294 30.726 1.00 31.68 ? 713 PHE A CA 1 ATOM 5527 C C . PHE A 1 672 ? 21.882 67.383 29.215 1.00 32.16 ? 713 PHE A C 1 ATOM 5528 O O . PHE A 1 672 ? 20.815 67.482 28.579 1.00 32.38 ? 713 PHE A O 1 ATOM 5529 C CB . PHE A 1 672 ? 21.340 65.914 31.184 1.00 31.03 ? 713 PHE A CB 1 ATOM 5530 C CG . PHE A 1 672 ? 22.191 64.760 30.688 1.00 34.13 ? 713 PHE A CG 1 ATOM 5531 C CD1 . PHE A 1 672 ? 23.373 64.419 31.363 1.00 36.62 ? 713 PHE A CD1 1 ATOM 5532 C CD2 . PHE A 1 672 ? 21.855 64.086 29.526 1.00 35.96 ? 713 PHE A CD2 1 ATOM 5533 C CE1 . PHE A 1 672 ? 24.211 63.381 30.871 1.00 39.55 ? 713 PHE A CE1 1 ATOM 5534 C CE2 . PHE A 1 672 ? 22.680 63.045 29.018 1.00 36.35 ? 713 PHE A CE2 1 ATOM 5535 C CZ . PHE A 1 672 ? 23.846 62.697 29.706 1.00 38.42 ? 713 PHE A CZ 1 ATOM 5536 N N . ASP A 1 673 ? 23.083 67.391 28.647 1.00 34.26 ? 714 ASP A N 1 ATOM 5537 C CA . ASP A 1 673 ? 23.274 67.412 27.176 1.00 36.45 ? 714 ASP A CA 1 ATOM 5538 C C . ASP A 1 673 ? 22.604 68.661 26.568 1.00 36.45 ? 714 ASP A C 1 ATOM 5539 O O . ASP A 1 673 ? 22.140 68.638 25.429 1.00 37.87 ? 714 ASP A O 1 ATOM 5540 C CB . ASP A 1 673 ? 22.688 66.100 26.567 1.00 37.42 ? 714 ASP A CB 1 ATOM 5541 C CG . ASP A 1 673 ? 23.149 65.856 25.103 1.00 40.42 ? 714 ASP A CG 1 ATOM 5542 O OD1 . ASP A 1 673 ? 24.293 66.202 24.744 1.00 40.47 ? 714 ASP A OD1 1 ATOM 5543 O OD2 . ASP A 1 673 ? 22.358 65.303 24.304 1.00 44.32 ? 714 ASP A OD2 1 ATOM 5544 N N . ILE A 1 674 ? 22.539 69.763 27.331 1.00 35.91 ? 715 ILE A N 1 ATOM 5545 C CA . ILE A 1 674 ? 21.744 70.922 26.899 1.00 34.78 ? 715 ILE A CA 1 ATOM 5546 C C . ILE A 1 674 ? 22.291 71.546 25.601 1.00 38.43 ? 715 ILE A C 1 ATOM 5547 O O . ILE A 1 674 ? 21.515 72.099 24.801 1.00 37.93 ? 715 ILE A O 1 ATOM 5548 C CB . ILE A 1 674 ? 21.603 71.984 28.025 1.00 34.24 ? 715 ILE A CB 1 ATOM 5549 C CG1 . ILE A 1 674 ? 20.580 73.036 27.621 1.00 33.36 ? 715 ILE A CG1 1 ATOM 5550 C CG2 . ILE A 1 674 ? 22.961 72.581 28.415 1.00 33.23 ? 715 ILE A CG2 1 ATOM 5551 C CD1 . ILE A 1 674 ? 20.035 73.829 28.768 1.00 33.15 ? 715 ILE A CD1 1 ATOM 5552 N N . GLU A 1 675 ? 23.610 71.440 25.412 1.00 40.43 ? 716 GLU A N 1 ATOM 5553 C CA . GLU A 1 675 ? 24.283 71.994 24.221 1.00 45.15 ? 716 GLU A CA 1 ATOM 5554 C C . GLU A 1 675 ? 23.876 71.330 22.899 1.00 46.90 ? 716 GLU A C 1 ATOM 5555 O O . GLU A 1 675 ? 24.232 71.836 21.821 1.00 47.61 ? 716 GLU A O 1 ATOM 5556 C CB . GLU A 1 675 ? 25.817 72.012 24.393 1.00 46.02 ? 716 GLU A CB 1 ATOM 5557 C CG . GLU A 1 675 ? 26.511 70.644 24.290 1.00 48.40 ? 716 GLU A CG 1 ATOM 5558 C CD . GLU A 1 675 ? 26.486 69.795 25.584 1.00 51.25 ? 716 GLU A CD 1 ATOM 5559 O OE1 . GLU A 1 675 ? 25.757 70.091 26.565 1.00 45.67 ? 716 GLU A OE1 1 ATOM 5560 O OE2 . GLU A 1 675 ? 27.232 68.792 25.615 1.00 55.65 ? 716 GLU A OE2 1 ATOM 5561 N N . SER A 1 676 ? 23.150 70.210 22.981 1.00 46.97 ? 717 SER A N 1 ATOM 5562 C CA A SER A 1 676 ? 22.659 69.504 21.796 0.50 48.21 ? 717 SER A CA 1 ATOM 5563 C CA B SER A 1 676 ? 22.662 69.512 21.790 0.50 49.00 ? 717 SER A CA 1 ATOM 5564 C C . SER A 1 676 ? 21.197 69.841 21.491 1.00 49.25 ? 717 SER A C 1 ATOM 5565 O O . SER A 1 676 ? 20.673 69.451 20.441 1.00 50.81 ? 717 SER A O 1 ATOM 5566 C CB A SER A 1 676 ? 22.840 67.983 21.941 0.50 47.48 ? 717 SER A CB 1 ATOM 5567 C CB B SER A 1 676 ? 22.825 67.994 21.934 0.50 48.41 ? 717 SER A CB 1 ATOM 5568 O OG A SER A 1 676 ? 24.177 67.656 22.260 0.50 44.07 ? 717 SER A OG 1 ATOM 5569 O OG B SER A 1 676 ? 21.616 67.430 22.410 0.50 48.21 ? 717 SER A OG 1 ATOM 5570 N N . LYS A 1 677 ? 20.537 70.578 22.390 1.00 48.61 ? 718 LYS A N 1 ATOM 5571 C CA . LYS A 1 677 ? 19.137 70.962 22.183 1.00 49.31 ? 718 LYS A CA 1 ATOM 5572 C C . LYS A 1 677 ? 18.997 71.973 21.056 1.00 50.73 ? 718 LYS A C 1 ATOM 5573 O O . LYS A 1 677 ? 19.804 72.909 20.925 1.00 51.51 ? 718 LYS A O 1 ATOM 5574 C CB . LYS A 1 677 ? 18.497 71.519 23.457 1.00 48.60 ? 718 LYS A CB 1 ATOM 5575 C CG . LYS A 1 677 ? 18.380 70.531 24.600 1.00 48.94 ? 718 LYS A CG 1 ATOM 5576 C CD . LYS A 1 677 ? 17.673 69.239 24.172 1.00 53.59 ? 718 LYS A CD 1 ATOM 5577 C CE . LYS A 1 677 ? 17.857 68.131 25.225 1.00 54.82 ? 718 LYS A CE 1 ATOM 5578 N NZ . LYS A 1 677 ? 17.231 68.507 26.542 1.00 52.65 ? 718 LYS A NZ 1 ATOM 5579 N N . VAL A 1 678 ? 17.966 71.800 20.241 1.00 51.48 ? 719 VAL A N 1 ATOM 5580 C CA . VAL A 1 678 ? 17.835 72.662 19.048 1.00 53.03 ? 719 VAL A CA 1 ATOM 5581 C C . VAL A 1 678 ? 17.284 74.059 19.341 1.00 52.54 ? 719 VAL A C 1 ATOM 5582 O O . VAL A 1 678 ? 17.567 74.986 18.605 1.00 54.01 ? 719 VAL A O 1 ATOM 5583 C CB . VAL A 1 678 ? 17.033 71.991 17.895 1.00 54.04 ? 719 VAL A CB 1 ATOM 5584 C CG1 . VAL A 1 678 ? 17.873 70.858 17.252 1.00 56.37 ? 719 VAL A CG1 1 ATOM 5585 C CG2 . VAL A 1 678 ? 15.657 71.499 18.367 1.00 52.99 ? 719 VAL A CG2 1 ATOM 5586 N N . ASP A 1 679 ? 16.512 74.202 20.417 1.00 50.35 ? 720 ASP A N 1 ATOM 5587 C CA . ASP A 1 679 ? 15.930 75.495 20.788 1.00 48.97 ? 720 ASP A CA 1 ATOM 5588 C C . ASP A 1 679 ? 16.524 75.841 22.157 1.00 46.47 ? 720 ASP A C 1 ATOM 5589 O O . ASP A 1 679 ? 15.931 75.504 23.174 1.00 43.57 ? 720 ASP A O 1 ATOM 5590 C CB . ASP A 1 679 ? 14.404 75.367 20.922 1.00 48.87 ? 720 ASP A CB 1 ATOM 5591 C CG . ASP A 1 679 ? 13.706 76.715 21.061 1.00 51.19 ? 720 ASP A CG 1 ATOM 5592 O OD1 . ASP A 1 679 ? 14.331 77.694 21.519 1.00 53.17 ? 720 ASP A OD1 1 ATOM 5593 O OD2 . ASP A 1 679 ? 12.507 76.804 20.714 1.00 57.37 ? 720 ASP A OD2 1 ATOM 5594 N N . PRO A 1 680 ? 17.698 76.498 22.177 1.00 45.43 ? 721 PRO A N 1 ATOM 5595 C CA . PRO A 1 680 ? 18.370 76.783 23.447 1.00 43.96 ? 721 PRO A CA 1 ATOM 5596 C C . PRO A 1 680 ? 17.561 77.725 24.350 1.00 42.85 ? 721 PRO A C 1 ATOM 5597 O O . PRO A 1 680 ? 17.651 77.634 25.576 1.00 39.75 ? 721 PRO A O 1 ATOM 5598 C CB . PRO A 1 680 ? 19.691 77.438 23.018 1.00 45.21 ? 721 PRO A CB 1 ATOM 5599 C CG . PRO A 1 680 ? 19.488 77.896 21.617 1.00 47.23 ? 721 PRO A CG 1 ATOM 5600 C CD . PRO A 1 680 ? 18.481 76.955 21.012 1.00 47.37 ? 721 PRO A CD 1 ATOM 5601 N N . SER A 1 681 ? 16.799 78.635 23.757 1.00 42.42 ? 722 SER A N 1 ATOM 5602 C CA . SER A 1 681 ? 15.915 79.492 24.548 1.00 42.52 ? 722 SER A CA 1 ATOM 5603 C C . SER A 1 681 ? 14.938 78.679 25.385 1.00 40.21 ? 722 SER A C 1 ATOM 5604 O O . SER A 1 681 ? 14.797 78.923 26.595 1.00 38.40 ? 722 SER A O 1 ATOM 5605 C CB . SER A 1 681 ? 15.142 80.448 23.640 1.00 43.78 ? 722 SER A CB 1 ATOM 5606 O OG . SER A 1 681 ? 14.382 81.316 24.446 1.00 47.87 ? 722 SER A OG 1 ATOM 5607 N N . LYS A 1 682 ? 14.265 77.709 24.752 1.00 38.67 ? 723 LYS A N 1 ATOM 5608 C CA A LYS A 1 682 ? 13.339 76.831 25.452 0.50 37.41 ? 723 LYS A CA 1 ATOM 5609 C CA B LYS A 1 682 ? 13.338 76.861 25.489 0.50 37.70 ? 723 LYS A CA 1 ATOM 5610 C C . LYS A 1 682 ? 14.060 75.980 26.505 1.00 36.00 ? 723 LYS A C 1 ATOM 5611 O O . LYS A 1 682 ? 13.570 75.808 27.623 1.00 33.98 ? 723 LYS A O 1 ATOM 5612 C CB A LYS A 1 682 ? 12.623 75.918 24.441 0.50 38.02 ? 723 LYS A CB 1 ATOM 5613 C CB B LYS A 1 682 ? 12.487 75.996 24.548 0.50 38.34 ? 723 LYS A CB 1 ATOM 5614 C CG A LYS A 1 682 ? 11.563 75.018 25.048 0.50 37.50 ? 723 LYS A CG 1 ATOM 5615 C CG B LYS A 1 682 ? 11.271 76.715 23.987 0.50 41.16 ? 723 LYS A CG 1 ATOM 5616 C CD A LYS A 1 682 ? 10.861 74.149 23.996 0.50 40.20 ? 723 LYS A CD 1 ATOM 5617 C CD B LYS A 1 682 ? 10.184 75.720 23.539 0.50 43.53 ? 723 LYS A CD 1 ATOM 5618 C CE A LYS A 1 682 ? 9.881 73.194 24.668 0.50 41.11 ? 723 LYS A CE 1 ATOM 5619 C CE B LYS A 1 682 ? 8.916 76.450 23.127 0.50 44.29 ? 723 LYS A CE 1 ATOM 5620 N NZ A LYS A 1 682 ? 9.290 72.280 23.657 0.50 44.30 ? 723 LYS A NZ 1 ATOM 5621 N NZ B LYS A 1 682 ? 9.225 77.465 22.081 0.50 46.25 ? 723 LYS A NZ 1 ATOM 5622 N N . ALA A 1 683 ? 15.211 75.422 26.119 1.00 34.61 ? 724 ALA A N 1 ATOM 5623 C CA . ALA A 1 683 ? 15.943 74.519 27.028 1.00 31.72 ? 724 ALA A CA 1 ATOM 5624 C C . ALA A 1 683 ? 16.398 75.286 28.284 1.00 30.55 ? 724 ALA A C 1 ATOM 5625 O O . ALA A 1 683 ? 16.244 74.783 29.386 1.00 28.44 ? 724 ALA A O 1 ATOM 5626 C CB . ALA A 1 683 ? 17.175 73.939 26.317 1.00 33.08 ? 724 ALA A CB 1 ATOM 5627 N N . TRP A 1 684 ? 17.003 76.473 28.091 1.00 29.81 ? 725 TRP A N 1 ATOM 5628 C CA . TRP A 1 684 ? 17.426 77.273 29.243 1.00 30.24 ? 725 TRP A CA 1 ATOM 5629 C C . TRP A 1 684 ? 16.252 77.825 30.077 1.00 29.55 ? 725 TRP A C 1 ATOM 5630 O O . TRP A 1 684 ? 16.361 77.932 31.286 1.00 29.09 ? 725 TRP A O 1 ATOM 5631 C CB . TRP A 1 684 ? 18.404 78.361 28.813 1.00 29.98 ? 725 TRP A CB 1 ATOM 5632 C CG . TRP A 1 684 ? 19.790 77.720 28.545 1.00 31.24 ? 725 TRP A CG 1 ATOM 5633 C CD1 . TRP A 1 684 ? 20.350 77.401 27.322 1.00 32.09 ? 725 TRP A CD1 1 ATOM 5634 C CD2 . TRP A 1 684 ? 20.739 77.299 29.540 1.00 30.90 ? 725 TRP A CD2 1 ATOM 5635 N NE1 . TRP A 1 684 ? 21.584 76.797 27.512 1.00 31.76 ? 725 TRP A NE1 1 ATOM 5636 C CE2 . TRP A 1 684 ? 21.851 76.737 28.854 1.00 30.43 ? 725 TRP A CE2 1 ATOM 5637 C CE3 . TRP A 1 684 ? 20.748 77.328 30.952 1.00 28.96 ? 725 TRP A CE3 1 ATOM 5638 C CZ2 . TRP A 1 684 ? 22.978 76.235 29.521 1.00 31.46 ? 725 TRP A CZ2 1 ATOM 5639 C CZ3 . TRP A 1 684 ? 21.881 76.837 31.616 1.00 29.98 ? 725 TRP A CZ3 1 ATOM 5640 C CH2 . TRP A 1 684 ? 22.967 76.277 30.892 1.00 30.18 ? 725 TRP A CH2 1 ATOM 5641 N N . GLY A 1 685 ? 15.144 78.168 29.420 1.00 30.56 ? 726 GLY A N 1 ATOM 5642 C CA . GLY A 1 685 ? 13.873 78.442 30.114 1.00 29.52 ? 726 GLY A CA 1 ATOM 5643 C C . GLY A 1 685 ? 13.508 77.334 31.069 1.00 29.38 ? 726 GLY A C 1 ATOM 5644 O O . GLY A 1 685 ? 13.094 77.592 32.216 1.00 28.33 ? 726 GLY A O 1 ATOM 5645 N N . GLU A 1 686 ? 13.651 76.084 30.614 1.00 28.84 ? 727 GLU A N 1 ATOM 5646 C CA . GLU A 1 686 ? 13.291 74.965 31.465 1.00 28.06 ? 727 GLU A CA 1 ATOM 5647 C C . GLU A 1 686 ? 14.288 74.799 32.641 1.00 27.05 ? 727 GLU A C 1 ATOM 5648 O O . GLU A 1 686 ? 13.892 74.438 33.742 1.00 25.61 ? 727 GLU A O 1 ATOM 5649 C CB . GLU A 1 686 ? 13.205 73.674 30.647 1.00 29.00 ? 727 GLU A CB 1 ATOM 5650 C CG A GLU A 1 686 ? 12.843 72.451 31.481 1.00 31.16 ? 727 GLU A CG 1 ATOM 5651 C CD A GLU A 1 686 ? 11.457 72.529 32.186 1.00 34.22 ? 727 GLU A CD 1 ATOM 5652 O OE1 A GLU A 1 686 ? 10.623 73.450 31.903 1.00 36.39 ? 727 GLU A OE1 1 ATOM 5653 O OE2 A GLU A 1 686 ? 11.236 71.634 33.030 1.00 35.63 ? 727 GLU A OE2 1 ATOM 5654 N N . VAL A 1 687 ? 15.574 75.099 32.409 1.00 26.32 ? 728 VAL A N 1 ATOM 5655 C CA . VAL A 1 687 ? 16.542 75.105 33.522 1.00 25.15 ? 728 VAL A CA 1 ATOM 5656 C C . VAL A 1 687 ? 16.072 76.132 34.588 1.00 25.38 ? 728 VAL A C 1 ATOM 5657 O O . VAL A 1 687 ? 16.028 75.841 35.778 1.00 23.56 ? 728 VAL A O 1 ATOM 5658 C CB . VAL A 1 687 ? 17.991 75.463 33.029 1.00 27.66 ? 728 VAL A CB 1 ATOM 5659 C CG1 . VAL A 1 687 ? 18.923 75.723 34.248 1.00 27.52 ? 728 VAL A CG1 1 ATOM 5660 C CG2 . VAL A 1 687 ? 18.548 74.336 32.036 1.00 25.14 ? 728 VAL A CG2 1 ATOM 5661 N N . LYS A 1 688 ? 15.734 77.329 34.134 1.00 25.41 ? 729 LYS A N 1 ATOM 5662 C CA . LYS A 1 688 ? 15.271 78.378 35.049 1.00 25.44 ? 729 LYS A CA 1 ATOM 5663 C C . LYS A 1 688 ? 14.004 77.962 35.803 1.00 25.45 ? 729 LYS A C 1 ATOM 5664 O O . LYS A 1 688 ? 13.862 78.247 37.007 1.00 24.77 ? 729 LYS A O 1 ATOM 5665 C CB B LYS A 1 688 ? 15.050 79.659 34.290 0.65 25.95 ? 729 LYS A CB 1 ATOM 5666 C CB C LYS A 1 688 ? 15.029 79.676 34.282 0.35 26.35 ? 729 LYS A CB 1 ATOM 5667 C CG B LYS A 1 688 ? 16.379 80.284 33.814 0.65 25.90 ? 729 LYS A CG 1 ATOM 5668 C CG C LYS A 1 688 ? 16.319 80.337 33.753 0.35 27.39 ? 729 LYS A CG 1 ATOM 5669 C CD B LYS A 1 688 ? 16.159 81.586 33.045 0.65 29.26 ? 729 LYS A CD 1 ATOM 5670 C CD C LYS A 1 688 ? 16.049 81.679 33.044 0.35 30.41 ? 729 LYS A CD 1 ATOM 5671 C CE B LYS A 1 688 ? 15.612 82.688 33.945 0.65 29.82 ? 729 LYS A CE 1 ATOM 5672 C CE C LYS A 1 688 ? 15.616 81.491 31.595 0.35 31.77 ? 729 LYS A CE 1 ATOM 5673 N NZ B LYS A 1 688 ? 15.627 83.944 33.145 0.65 34.98 ? 729 LYS A NZ 1 ATOM 5674 N NZ C LYS A 1 688 ? 15.297 82.780 30.900 0.35 35.17 ? 729 LYS A NZ 1 ATOM 5675 N N . ARG A 1 689 ? 13.075 77.297 35.102 1.00 24.19 ? 730 ARG A N 1 ATOM 5676 C CA . ARG A 1 689 ? 11.896 76.784 35.795 1.00 23.71 ? 730 ARG A CA 1 ATOM 5677 C C . ARG A 1 689 ? 12.239 75.811 36.894 1.00 22.73 ? 730 ARG A C 1 ATOM 5678 O O . ARG A 1 689 ? 11.705 75.911 38.014 1.00 22.47 ? 730 ARG A O 1 ATOM 5679 C CB . ARG A 1 689 ? 10.891 76.142 34.822 1.00 24.35 ? 730 ARG A CB 1 ATOM 5680 C CG . ARG A 1 689 ? 9.535 75.919 35.530 1.00 26.26 ? 730 ARG A CG 1 ATOM 5681 C CD . ARG A 1 689 ? 8.487 75.331 34.510 1.00 27.63 ? 730 ARG A CD 1 ATOM 5682 N NE . ARG A 1 689 ? 8.755 73.910 34.258 1.00 28.80 ? 730 ARG A NE 1 ATOM 5683 C CZ . ARG A 1 689 ? 8.306 72.897 35.005 1.00 33.66 ? 730 ARG A CZ 1 ATOM 5684 N NH1 . ARG A 1 689 ? 7.607 73.109 36.145 1.00 33.18 ? 730 ARG A NH1 1 ATOM 5685 N NH2 . ARG A 1 689 ? 8.605 71.651 34.645 1.00 34.64 ? 730 ARG A NH2 1 ATOM 5686 N N . GLN A 1 690 ? 13.159 74.872 36.627 1.00 21.67 ? 731 GLN A N 1 ATOM 5687 C CA . GLN A 1 690 ? 13.548 73.937 37.657 1.00 22.22 ? 731 GLN A CA 1 ATOM 5688 C C . GLN A 1 690 ? 14.319 74.589 38.819 1.00 22.31 ? 731 GLN A C 1 ATOM 5689 O O . GLN A 1 690 ? 14.222 74.080 39.957 1.00 21.42 ? 731 GLN A O 1 ATOM 5690 C CB . GLN A 1 690 ? 14.402 72.836 37.027 1.00 21.48 ? 731 GLN A CB 1 ATOM 5691 C CG . GLN A 1 690 ? 13.525 72.004 35.985 1.00 23.06 ? 731 GLN A CG 1 ATOM 5692 C CD . GLN A 1 690 ? 12.369 71.265 36.653 1.00 27.36 ? 731 GLN A CD 1 ATOM 5693 O OE1 . GLN A 1 690 ? 12.466 70.813 37.802 1.00 25.93 ? 731 GLN A OE1 1 ATOM 5694 N NE2 . GLN A 1 690 ? 11.263 71.157 35.946 1.00 30.59 ? 731 GLN A NE2 1 ATOM 5695 N N . ILE A 1 691 ? 15.079 75.655 38.522 1.00 22.29 ? 732 ILE A N 1 ATOM 5696 C CA . ILE A 1 691 ? 15.735 76.357 39.612 1.00 23.65 ? 732 ILE A CA 1 ATOM 5697 C C . ILE A 1 691 ? 14.676 76.953 40.553 1.00 23.58 ? 732 ILE A C 1 ATOM 5698 O O . ILE A 1 691 ? 14.818 76.833 41.758 1.00 24.15 ? 732 ILE A O 1 ATOM 5699 C CB . ILE A 1 691 ? 16.651 77.456 39.094 1.00 23.37 ? 732 ILE A CB 1 ATOM 5700 C CG1 . ILE A 1 691 ? 17.874 76.816 38.379 1.00 23.02 ? 732 ILE A CG1 1 ATOM 5701 C CG2 . ILE A 1 691 ? 17.112 78.408 40.252 1.00 24.45 ? 732 ILE A CG2 1 ATOM 5702 C CD1 . ILE A 1 691 ? 18.689 77.884 37.584 1.00 25.34 ? 732 ILE A CD1 1 ATOM 5703 N N . TYR A 1 692 ? 13.660 77.609 39.983 1.00 22.21 ? 733 TYR A N 1 ATOM 5704 C CA . TYR A 1 692 ? 12.531 78.140 40.790 1.00 23.79 ? 733 TYR A CA 1 ATOM 5705 C C . TYR A 1 692 ? 11.829 77.050 41.589 1.00 22.64 ? 733 TYR A C 1 ATOM 5706 O O . TYR A 1 692 ? 11.549 77.251 42.783 1.00 21.86 ? 733 TYR A O 1 ATOM 5707 C CB . TYR A 1 692 ? 11.556 78.766 39.824 1.00 24.57 ? 733 TYR A CB 1 ATOM 5708 C CG . TYR A 1 692 ? 10.094 79.029 40.208 1.00 28.91 ? 733 TYR A CG 1 ATOM 5709 C CD1 . TYR A 1 692 ? 9.754 79.765 41.363 1.00 31.91 ? 733 TYR A CD1 1 ATOM 5710 C CD2 . TYR A 1 692 ? 9.044 78.623 39.328 1.00 30.93 ? 733 TYR A CD2 1 ATOM 5711 C CE1 . TYR A 1 692 ? 8.394 80.066 41.648 1.00 30.39 ? 733 TYR A CE1 1 ATOM 5712 C CE2 . TYR A 1 692 ? 7.725 78.933 39.573 1.00 28.37 ? 733 TYR A CE2 1 ATOM 5713 C CZ . TYR A 1 692 ? 7.400 79.653 40.735 1.00 32.47 ? 733 TYR A CZ 1 ATOM 5714 O OH . TYR A 1 692 ? 6.063 79.998 40.994 1.00 32.10 ? 733 TYR A OH 1 ATOM 5715 N N . VAL A 1 693 ? 11.544 75.923 40.964 1.00 21.51 ? 734 VAL A N 1 ATOM 5716 C CA . VAL A 1 693 ? 10.871 74.838 41.727 1.00 21.90 ? 734 VAL A CA 1 ATOM 5717 C C . VAL A 1 693 ? 11.722 74.361 42.912 1.00 22.53 ? 734 VAL A C 1 ATOM 5718 O O . VAL A 1 693 ? 11.209 74.143 44.042 1.00 22.18 ? 734 VAL A O 1 ATOM 5719 C CB . VAL A 1 693 ? 10.480 73.643 40.789 1.00 22.77 ? 734 VAL A CB 1 ATOM 5720 C CG1 . VAL A 1 693 ? 9.922 72.455 41.626 1.00 23.56 ? 734 VAL A CG1 1 ATOM 5721 C CG2 . VAL A 1 693 ? 9.385 74.093 39.776 1.00 23.43 ? 734 VAL A CG2 1 ATOM 5722 N N . ALA A 1 694 ? 13.013 74.185 42.664 1.00 22.39 ? 735 ALA A N 1 ATOM 5723 C CA . ALA A 1 694 ? 13.907 73.721 43.722 1.00 22.44 ? 735 ALA A CA 1 ATOM 5724 C C . ALA A 1 694 ? 14.058 74.771 44.826 1.00 22.39 ? 735 ALA A C 1 ATOM 5725 O O . ALA A 1 694 ? 14.035 74.403 46.027 1.00 22.19 ? 735 ALA A O 1 ATOM 5726 C CB . ALA A 1 694 ? 15.271 73.336 43.146 1.00 24.34 ? 735 ALA A CB 1 ATOM 5727 N N . ALA A 1 695 ? 14.222 76.053 44.451 1.00 21.04 ? 736 ALA A N 1 ATOM 5728 C CA . ALA A 1 695 ? 14.392 77.111 45.463 1.00 22.57 ? 736 ALA A CA 1 ATOM 5729 C C . ALA A 1 695 ? 13.121 77.220 46.304 1.00 23.48 ? 736 ALA A C 1 ATOM 5730 O O . ALA A 1 695 ? 13.182 77.271 47.529 1.00 22.00 ? 736 ALA A O 1 ATOM 5731 C CB . ALA A 1 695 ? 14.703 78.442 44.815 1.00 22.10 ? 736 ALA A CB 1 ATOM 5732 N N . PHE A 1 696 ? 11.967 77.216 45.623 1.00 21.57 ? 737 PHE A N 1 ATOM 5733 C CA . PHE A 1 696 ? 10.684 77.262 46.333 1.00 22.95 ? 737 PHE A CA 1 ATOM 5734 C C . PHE A 1 696 ? 10.558 76.079 47.316 1.00 21.71 ? 737 PHE A C 1 ATOM 5735 O O . PHE A 1 696 ? 10.168 76.264 48.481 1.00 21.79 ? 737 PHE A O 1 ATOM 5736 C CB . PHE A 1 696 ? 9.502 77.258 45.366 1.00 22.32 ? 737 PHE A CB 1 ATOM 5737 C CG . PHE A 1 696 ? 8.196 76.897 46.049 1.00 23.63 ? 737 PHE A CG 1 ATOM 5738 C CD1 . PHE A 1 696 ? 7.637 77.794 46.974 1.00 24.50 ? 737 PHE A CD1 1 ATOM 5739 C CD2 . PHE A 1 696 ? 7.639 75.639 45.879 1.00 25.24 ? 737 PHE A CD2 1 ATOM 5740 C CE1 . PHE A 1 696 ? 6.460 77.411 47.699 1.00 26.62 ? 737 PHE A CE1 1 ATOM 5741 C CE2 . PHE A 1 696 ? 6.425 75.267 46.592 1.00 25.06 ? 737 PHE A CE2 1 ATOM 5742 C CZ . PHE A 1 696 ? 5.867 76.180 47.458 1.00 23.59 ? 737 PHE A CZ 1 ATOM 5743 N N . THR A 1 697 ? 10.895 74.883 46.871 1.00 20.33 ? 738 THR A N 1 ATOM 5744 C CA . THR A 1 697 ? 10.659 73.709 47.724 1.00 21.54 ? 738 THR A CA 1 ATOM 5745 C C . THR A 1 697 ? 11.588 73.713 48.929 1.00 22.21 ? 738 THR A C 1 ATOM 5746 O O . THR A 1 697 ? 11.179 73.350 50.055 1.00 22.53 ? 738 THR A O 1 ATOM 5747 C CB . THR A 1 697 ? 10.912 72.407 46.900 1.00 22.51 ? 738 THR A CB 1 ATOM 5748 O OG1 . THR A 1 697 ? 10.026 72.401 45.778 1.00 22.81 ? 738 THR A OG1 1 ATOM 5749 C CG2 . THR A 1 697 ? 10.659 71.153 47.750 1.00 20.63 ? 738 THR A CG2 1 ATOM 5750 N N . VAL A 1 698 ? 12.849 74.116 48.706 1.00 22.37 ? 739 VAL A N 1 ATOM 5751 C CA . VAL A 1 698 ? 13.821 74.221 49.846 1.00 22.59 ? 739 VAL A CA 1 ATOM 5752 C C . VAL A 1 698 ? 13.305 75.245 50.869 1.00 23.43 ? 739 VAL A C 1 ATOM 5753 O O . VAL A 1 698 ? 13.312 74.944 52.071 1.00 23.14 ? 739 VAL A O 1 ATOM 5754 C CB . VAL A 1 698 ? 15.239 74.522 49.363 1.00 22.81 ? 739 VAL A CB 1 ATOM 5755 C CG1 . VAL A 1 698 ? 16.219 74.917 50.560 1.00 22.20 ? 739 VAL A CG1 1 ATOM 5756 C CG2 . VAL A 1 698 ? 15.744 73.298 48.595 1.00 22.53 ? 739 VAL A CG2 1 ATOM 5757 N N . GLN A 1 699 ? 12.879 76.430 50.403 1.00 23.11 ? 740 GLN A N 1 ATOM 5758 C CA . GLN A 1 699 ? 12.307 77.430 51.306 1.00 24.15 ? 740 GLN A CA 1 ATOM 5759 C C . GLN A 1 699 ? 11.054 76.900 52.024 1.00 23.71 ? 740 GLN A C 1 ATOM 5760 O O . GLN A 1 699 ? 10.885 77.134 53.249 1.00 23.43 ? 740 GLN A O 1 ATOM 5761 C CB . GLN A 1 699 ? 11.958 78.711 50.555 1.00 25.05 ? 740 GLN A CB 1 ATOM 5762 C CG . GLN A 1 699 ? 11.386 79.836 51.458 1.00 27.29 ? 740 GLN A CG 1 ATOM 5763 C CD . GLN A 1 699 ? 12.452 80.430 52.385 1.00 26.61 ? 740 GLN A CD 1 ATOM 5764 O OE1 . GLN A 1 699 ? 13.671 80.381 52.112 1.00 28.59 ? 740 GLN A OE1 1 ATOM 5765 N NE2 . GLN A 1 699 ? 11.993 81.037 53.467 1.00 30.49 ? 740 GLN A NE2 1 ATOM 5766 N N . ALA A 1 700 ? 10.159 76.246 51.270 1.00 21.83 ? 741 ALA A N 1 ATOM 5767 C CA . ALA A 1 700 ? 8.944 75.671 51.872 1.00 21.86 ? 741 ALA A CA 1 ATOM 5768 C C . ALA A 1 700 ? 9.270 74.652 52.945 1.00 21.95 ? 741 ALA A C 1 ATOM 5769 O O . ALA A 1 700 ? 8.660 74.669 54.029 1.00 22.89 ? 741 ALA A O 1 ATOM 5770 C CB . ALA A 1 700 ? 8.018 75.037 50.791 1.00 21.00 ? 741 ALA A CB 1 ATOM 5771 N N . ALA A 1 701 ? 10.250 73.787 52.685 1.00 21.71 ? 742 ALA A N 1 ATOM 5772 C CA . ALA A 1 701 ? 10.688 72.803 53.688 1.00 23.38 ? 742 ALA A CA 1 ATOM 5773 C C . ALA A 1 701 ? 11.264 73.499 54.926 1.00 23.53 ? 742 ALA A C 1 ATOM 5774 O O . ALA A 1 701 ? 10.953 73.126 56.066 1.00 24.09 ? 742 ALA A O 1 ATOM 5775 C CB . ALA A 1 701 ? 11.736 71.837 53.100 1.00 21.10 ? 742 ALA A CB 1 ATOM 5776 N N . ALA A 1 702 ? 12.086 74.528 54.700 1.00 23.51 ? 743 ALA A N 1 ATOM 5777 C CA . ALA A 1 702 ? 12.663 75.291 55.817 1.00 24.34 ? 743 ALA A CA 1 ATOM 5778 C C . ALA A 1 702 ? 11.551 75.866 56.664 1.00 25.75 ? 743 ALA A C 1 ATOM 5779 O O . ALA A 1 702 ? 11.608 75.818 57.900 1.00 24.49 ? 743 ALA A O 1 ATOM 5780 C CB . ALA A 1 702 ? 13.500 76.467 55.269 1.00 23.61 ? 743 ALA A CB 1 ATOM 5781 N N . GLU A 1 703 ? 10.516 76.419 56.004 1.00 23.28 ? 744 GLU A N 1 ATOM 5782 C CA . GLU A 1 703 ? 9.432 77.058 56.735 1.00 24.75 ? 744 GLU A CA 1 ATOM 5783 C C . GLU A 1 703 ? 8.611 76.111 57.607 1.00 24.73 ? 744 GLU A C 1 ATOM 5784 O O . GLU A 1 703 ? 8.005 76.575 58.578 1.00 24.50 ? 744 GLU A O 1 ATOM 5785 C CB . GLU A 1 703 ? 8.512 77.915 55.815 1.00 25.21 ? 744 GLU A CB 1 ATOM 5786 C CG . GLU A 1 703 ? 9.235 79.173 55.403 1.00 28.94 ? 744 GLU A CG 1 ATOM 5787 C CD . GLU A 1 703 ? 8.496 80.057 54.412 1.00 35.20 ? 744 GLU A CD 1 ATOM 5788 O OE1 . GLU A 1 703 ? 7.349 79.735 53.987 1.00 38.30 ? 744 GLU A OE1 1 ATOM 5789 O OE2 . GLU A 1 703 ? 9.097 81.099 54.059 1.00 33.75 ? 744 GLU A OE2 1 ATOM 5790 N N . THR A 1 704 ? 8.652 74.804 57.311 1.00 23.21 ? 745 THR A N 1 ATOM 5791 C CA . THR A 1 704 ? 7.993 73.825 58.200 1.00 23.35 ? 745 THR A CA 1 ATOM 5792 C C . THR A 1 704 ? 8.704 73.711 59.568 1.00 24.45 ? 745 THR A C 1 ATOM 5793 O O . THR A 1 704 ? 8.114 73.216 60.514 1.00 24.51 ? 745 THR A O 1 ATOM 5794 C CB . THR A 1 704 ? 7.838 72.416 57.607 1.00 23.05 ? 745 THR A CB 1 ATOM 5795 O OG1 . THR A 1 704 ? 9.108 71.742 57.574 1.00 25.13 ? 745 THR A OG1 1 ATOM 5796 C CG2 . THR A 1 704 ? 7.173 72.468 56.144 1.00 21.76 ? 745 THR A CG2 1 ATOM 5797 N N . LEU A 1 705 ? 9.941 74.189 59.649 1.00 23.85 ? 746 LEU A N 1 ATOM 5798 C CA . LEU A 1 705 ? 10.728 74.149 60.892 1.00 25.25 ? 746 LEU A CA 1 ATOM 5799 C C . LEU A 1 705 ? 10.631 75.460 61.662 1.00 27.38 ? 746 LEU A C 1 ATOM 5800 O O . LEU A 1 705 ? 11.157 75.564 62.791 1.00 27.04 ? 746 LEU A O 1 ATOM 5801 C CB . LEU A 1 705 ? 12.198 73.858 60.582 1.00 24.50 ? 746 LEU A CB 1 ATOM 5802 C CG . LEU A 1 705 ? 12.421 72.535 59.867 1.00 27.06 ? 746 LEU A CG 1 ATOM 5803 C CD1 . LEU A 1 705 ? 13.944 72.391 59.568 1.00 28.06 ? 746 LEU A CD1 1 ATOM 5804 C CD2 . LEU A 1 705 ? 11.922 71.340 60.720 1.00 27.20 ? 746 LEU A CD2 1 ATOM 5805 N N . SER A 1 706 ? 10.018 76.491 61.057 1.00 27.99 ? 747 SER A N 1 ATOM 5806 C CA . SER A 1 706 ? 9.838 77.764 61.791 1.00 28.86 ? 747 SER A CA 1 ATOM 5807 C C . SER A 1 706 ? 8.882 77.556 62.968 1.00 29.78 ? 747 SER A C 1 ATOM 5808 O O . SER A 1 706 ? 8.115 76.584 62.989 1.00 28.71 ? 747 SER A O 1 ATOM 5809 C CB . SER A 1 706 ? 9.252 78.826 60.848 1.00 30.44 ? 747 SER A CB 1 ATOM 5810 O OG . SER A 1 706 ? 10.192 79.054 59.815 1.00 32.88 ? 747 SER A OG 1 ATOM 5811 N N . GLU A 1 707 ? 8.858 78.482 63.928 1.00 29.49 ? 748 GLU A N 1 ATOM 5812 C CA . GLU A 1 707 ? 7.769 78.423 64.929 1.00 32.53 ? 748 GLU A CA 1 ATOM 5813 C C . GLU A 1 707 ? 6.379 78.370 64.239 1.00 30.51 ? 748 GLU A C 1 ATOM 5814 O O . GLU A 1 707 ? 6.132 79.023 63.215 1.00 30.94 ? 748 GLU A O 1 ATOM 5815 C CB . GLU A 1 707 ? 7.882 79.582 65.942 1.00 33.98 ? 748 GLU A CB 1 ATOM 5816 C CG . GLU A 1 707 ? 9.219 79.448 66.683 1.00 38.49 ? 748 GLU A CG 1 ATOM 5817 C CD . GLU A 1 707 ? 9.318 80.286 67.919 1.00 50.17 ? 748 GLU A CD 1 ATOM 5818 O OE1 . GLU A 1 707 ? 9.635 81.490 67.781 1.00 52.36 ? 748 GLU A OE1 1 ATOM 5819 O OE2 . GLU A 1 707 ? 9.105 79.717 69.012 1.00 53.52 ? 748 GLU A OE2 1 ATOM 5820 N N . VAL A 1 708 ? 5.502 77.528 64.759 1.00 30.30 ? 749 VAL A N 1 ATOM 5821 C CA . VAL A 1 708 ? 4.270 77.177 64.006 1.00 29.08 ? 749 VAL A CA 1 ATOM 5822 C C . VAL A 1 708 ? 3.227 78.311 64.011 1.00 30.78 ? 749 VAL A C 1 ATOM 5823 O O . VAL A 1 708 ? 2.322 78.327 63.186 1.00 30.86 ? 749 VAL A O 1 ATOM 5824 C CB . VAL A 1 708 ? 3.659 75.857 64.537 1.00 28.24 ? 749 VAL A CB 1 ATOM 5825 C CG1 . VAL A 1 708 ? 4.694 74.696 64.436 1.00 29.88 ? 749 VAL A CG1 1 ATOM 5826 C CG2 . VAL A 1 708 ? 3.191 76.040 66.020 1.00 28.83 ? 749 VAL A CG2 1 ATOM 5827 N N . ALA A 1 709 ? 3.375 79.272 64.927 1.00 32.63 ? 750 ALA A N 1 ATOM 5828 C CA . ALA A 1 709 ? 2.403 80.382 65.084 1.00 35.83 ? 750 ALA A CA 1 ATOM 5829 C C . ALA A 1 709 ? 2.994 81.387 66.070 1.00 38.77 ? 750 ALA A C 1 ATOM 5830 O O . ALA A 1 709 ? 2.425 82.463 66.270 1.00 41.12 ? 750 ALA A O 1 ATOM 5831 C CB . ALA A 1 709 ? 1.073 79.872 65.621 1.00 35.90 ? 750 ALA A CB 1 ATOM 5832 O OXT . ALA A 1 709 ? 4.025 81.124 66.731 1.00 40.39 ? 750 ALA A OXT 1 HETATM 5833 C C1 . NAG B 2 . ? 11.830 25.832 57.676 1.00 38.18 ? 801 NAG A C1 1 HETATM 5834 C C2 . NAG B 2 . ? 11.576 24.405 57.222 1.00 43.85 ? 801 NAG A C2 1 HETATM 5835 C C3 . NAG B 2 . ? 10.090 24.094 57.423 1.00 47.31 ? 801 NAG A C3 1 HETATM 5836 C C4 . NAG B 2 . ? 9.624 24.336 58.835 1.00 45.58 ? 801 NAG A C4 1 HETATM 5837 C C5 . NAG B 2 . ? 10.017 25.749 59.206 1.00 43.27 ? 801 NAG A C5 1 HETATM 5838 C C6 . NAG B 2 . ? 9.592 26.118 60.639 1.00 45.44 ? 801 NAG A C6 1 HETATM 5839 C C7 . NAG B 2 . ? 12.982 23.799 55.326 1.00 52.42 ? 801 NAG A C7 1 HETATM 5840 C C8 . NAG B 2 . ? 13.129 23.804 53.830 1.00 50.97 ? 801 NAG A C8 1 HETATM 5841 N N2 . NAG B 2 . ? 11.849 24.338 55.803 1.00 47.34 ? 801 NAG A N2 1 HETATM 5842 O O3 . NAG B 2 . ? 9.814 22.759 57.106 1.00 49.11 ? 801 NAG A O3 1 HETATM 5843 O O4 . NAG B 2 . ? 8.212 24.271 58.764 1.00 50.14 ? 801 NAG A O4 1 HETATM 5844 O O5 . NAG B 2 . ? 11.414 25.972 59.029 1.00 37.74 ? 801 NAG A O5 1 HETATM 5845 O O6 . NAG B 2 . ? 10.243 25.243 61.531 1.00 46.35 ? 801 NAG A O6 1 HETATM 5846 O O7 . NAG B 2 . ? 13.883 23.348 56.053 1.00 54.39 ? 801 NAG A O7 1 HETATM 5847 C C1 . NAG C 2 . ? 7.660 23.385 59.761 1.00 56.06 ? 802 NAG A C1 1 HETATM 5848 C C2 . NAG C 2 . ? 6.182 23.724 60.022 1.00 57.01 ? 802 NAG A C2 1 HETATM 5849 C C3 . NAG C 2 . ? 5.506 22.674 60.924 1.00 60.64 ? 802 NAG A C3 1 HETATM 5850 C C4 . NAG C 2 . ? 5.933 21.222 60.637 1.00 62.95 ? 802 NAG A C4 1 HETATM 5851 C C5 . NAG C 2 . ? 7.460 21.140 60.410 1.00 62.72 ? 802 NAG A C5 1 HETATM 5852 C C6 . NAG C 2 . ? 7.978 19.748 60.052 1.00 62.03 ? 802 NAG A C6 1 HETATM 5853 C C7 . NAG C 2 . ? 5.546 26.149 59.960 1.00 52.82 ? 802 NAG A C7 1 HETATM 5854 C C8 . NAG C 2 . ? 5.391 26.043 58.480 1.00 47.99 ? 802 NAG A C8 1 HETATM 5855 N N2 . NAG C 2 . ? 5.939 25.041 60.623 1.00 53.62 ? 802 NAG A N2 1 HETATM 5856 O O3 . NAG C 2 . ? 4.110 22.822 60.744 1.00 61.18 ? 802 NAG A O3 1 HETATM 5857 O O4 . NAG C 2 . ? 5.524 20.398 61.721 1.00 66.69 ? 802 NAG A O4 1 HETATM 5858 O O5 . NAG C 2 . ? 7.771 22.032 59.346 1.00 59.96 ? 802 NAG A O5 1 HETATM 5859 O O6 . NAG C 2 . ? 7.410 19.408 58.802 1.00 61.17 ? 802 NAG A O6 1 HETATM 5860 O O7 . NAG C 2 . ? 5.330 27.244 60.534 1.00 53.08 ? 802 NAG A O7 1 HETATM 5861 C C1 . NAG D 2 . ? 4.169 27.980 25.145 1.00 50.89 ? 803 NAG A C1 1 HETATM 5862 C C2 . NAG D 2 . ? 2.768 28.544 24.951 1.00 56.60 ? 803 NAG A C2 1 HETATM 5863 C C3 . NAG D 2 . ? 1.781 27.592 24.256 1.00 59.11 ? 803 NAG A C3 1 HETATM 5864 C C4 . NAG D 2 . ? 2.446 26.651 23.222 1.00 61.31 ? 803 NAG A C4 1 HETATM 5865 C C5 . NAG D 2 . ? 3.802 26.123 23.736 1.00 61.01 ? 803 NAG A C5 1 HETATM 5866 C C6 . NAG D 2 . ? 4.516 25.105 22.810 1.00 62.46 ? 803 NAG A C6 1 HETATM 5867 C C7 . NAG D 2 . ? 2.025 30.269 26.480 1.00 57.51 ? 803 NAG A C7 1 HETATM 5868 C C8 . NAG D 2 . ? 2.094 31.242 25.335 1.00 55.76 ? 803 NAG A C8 1 HETATM 5869 N N2 . NAG D 2 . ? 2.334 28.990 26.265 1.00 55.53 ? 803 NAG A N2 1 HETATM 5870 O O3 . NAG D 2 . ? 0.843 28.433 23.616 1.00 59.91 ? 803 NAG A O3 1 HETATM 5871 O O4 . NAG D 2 . ? 1.576 25.570 22.857 1.00 63.71 ? 803 NAG A O4 1 HETATM 5872 O O5 . NAG D 2 . ? 4.644 27.236 24.042 1.00 56.28 ? 803 NAG A O5 1 HETATM 5873 O O6 . NAG D 2 . ? 4.975 25.629 21.566 1.00 64.61 ? 803 NAG A O6 1 HETATM 5874 O O7 . NAG D 2 . ? 1.667 30.657 27.587 1.00 59.69 ? 803 NAG A O7 1 HETATM 5875 C C1 . NAG E 2 . ? 20.147 25.038 17.508 1.00 45.35 ? 804 NAG A C1 1 HETATM 5876 C C2 . NAG E 2 . ? 20.769 23.824 16.775 1.00 50.62 ? 804 NAG A C2 1 HETATM 5877 C C3 . NAG E 2 . ? 19.939 23.448 15.548 1.00 53.13 ? 804 NAG A C3 1 HETATM 5878 C C4 . NAG E 2 . ? 18.432 23.408 15.838 1.00 53.24 ? 804 NAG A C4 1 HETATM 5879 C C5 . NAG E 2 . ? 17.928 24.598 16.725 1.00 50.27 ? 804 NAG A C5 1 HETATM 5880 C C6 . NAG E 2 . ? 16.487 24.442 17.230 1.00 46.97 ? 804 NAG A C6 1 HETATM 5881 C C7 . NAG E 2 . ? 23.214 23.591 16.897 1.00 51.92 ? 804 NAG A C7 1 HETATM 5882 C C8 . NAG E 2 . ? 24.551 24.006 16.350 1.00 51.60 ? 804 NAG A C8 1 HETATM 5883 N N2 . NAG E 2 . ? 22.130 24.126 16.335 1.00 49.94 ? 804 NAG A N2 1 HETATM 5884 O O3 . NAG E 2 . ? 20.409 22.186 15.096 1.00 53.90 ? 804 NAG A O3 1 HETATM 5885 O O4 . NAG E 2 . ? 17.800 23.436 14.572 1.00 59.75 ? 804 NAG A O4 1 HETATM 5886 O O5 . NAG E 2 . ? 18.776 24.783 17.844 1.00 47.17 ? 804 NAG A O5 1 HETATM 5887 O O6 . NAG E 2 . ? 16.356 23.275 18.005 1.00 47.21 ? 804 NAG A O6 1 HETATM 5888 O O7 . NAG E 2 . ? 23.164 22.789 17.820 1.00 53.36 ? 804 NAG A O7 1 HETATM 5889 C C1 . NAG F 2 . ? 16.765 22.430 14.481 1.00 65.26 ? 805 NAG A C1 1 HETATM 5890 C C2 . NAG F 2 . ? 15.795 22.872 13.383 1.00 67.44 ? 805 NAG A C2 1 HETATM 5891 C C3 . NAG F 2 . ? 14.743 21.786 13.110 1.00 70.31 ? 805 NAG A C3 1 HETATM 5892 C C4 . NAG F 2 . ? 15.372 20.395 12.965 1.00 71.25 ? 805 NAG A C4 1 HETATM 5893 C C5 . NAG F 2 . ? 16.251 20.097 14.193 1.00 71.01 ? 805 NAG A C5 1 HETATM 5894 C C6 . NAG F 2 . ? 16.922 18.725 14.109 1.00 72.30 ? 805 NAG A C6 1 HETATM 5895 C C7 . NAG F 2 . ? 15.532 25.339 13.359 1.00 66.31 ? 805 NAG A C7 1 HETATM 5896 C C8 . NAG F 2 . ? 14.738 26.513 13.871 1.00 65.85 ? 805 NAG A C8 1 HETATM 5897 N N2 . NAG F 2 . ? 15.142 24.122 13.768 1.00 66.51 ? 805 NAG A N2 1 HETATM 5898 O O3 . NAG F 2 . ? 14.015 22.110 11.943 1.00 70.47 ? 805 NAG A O3 1 HETATM 5899 O O4 . NAG F 2 . ? 14.341 19.437 12.758 1.00 73.19 ? 805 NAG A O4 1 HETATM 5900 O O5 . NAG F 2 . ? 17.260 21.101 14.311 1.00 67.89 ? 805 NAG A O5 1 HETATM 5901 O O6 . NAG F 2 . ? 17.987 18.789 13.179 1.00 73.98 ? 805 NAG A O6 1 HETATM 5902 O O7 . NAG F 2 . ? 16.495 25.539 12.617 1.00 64.80 ? 805 NAG A O7 1 HETATM 5903 C C1 . NAG G 2 . ? 20.225 54.780 10.559 1.00 66.96 ? 806 NAG A C1 1 HETATM 5904 C C2 . NAG G 2 . ? 19.971 56.261 10.263 1.00 73.76 ? 806 NAG A C2 1 HETATM 5905 C C3 . NAG G 2 . ? 18.473 56.446 10.080 1.00 74.46 ? 806 NAG A C3 1 HETATM 5906 C C4 . NAG G 2 . ? 17.982 55.595 8.907 1.00 74.65 ? 806 NAG A C4 1 HETATM 5907 C C5 . NAG G 2 . ? 18.314 54.108 9.091 1.00 73.63 ? 806 NAG A C5 1 HETATM 5908 C C6 . NAG G 2 . ? 18.070 53.408 7.742 1.00 74.09 ? 806 NAG A C6 1 HETATM 5909 C C7 . NAG G 2 . ? 21.609 57.867 11.259 1.00 78.10 ? 806 NAG A C7 1 HETATM 5910 C C8 . NAG G 2 . ? 21.898 58.751 12.439 1.00 77.38 ? 806 NAG A C8 1 HETATM 5911 N N2 . NAG G 2 . ? 20.459 57.172 11.301 1.00 76.03 ? 806 NAG A N2 1 HETATM 5912 O O3 . NAG G 2 . ? 18.223 57.811 9.843 1.00 75.30 ? 806 NAG A O3 1 HETATM 5913 O O4 . NAG G 2 . ? 16.591 55.774 8.714 1.00 76.38 ? 806 NAG A O4 1 HETATM 5914 O O5 . NAG G 2 . ? 19.659 53.910 9.558 1.00 70.71 ? 806 NAG A O5 1 HETATM 5915 O O6 . NAG G 2 . ? 18.419 52.039 7.752 1.00 75.50 ? 806 NAG A O6 1 HETATM 5916 O O7 . NAG G 2 . ? 22.429 57.818 10.333 1.00 78.82 ? 806 NAG A O7 1 HETATM 5917 C C1 . NAG H 2 . ? 35.992 37.345 52.985 1.00 47.19 ? 807 NAG A C1 1 HETATM 5918 C C2 . NAG H 2 . ? 36.172 37.393 51.458 1.00 49.48 ? 807 NAG A C2 1 HETATM 5919 C C3 . NAG H 2 . ? 37.420 36.588 51.046 1.00 54.41 ? 807 NAG A C3 1 HETATM 5920 C C4 . NAG H 2 . ? 38.659 37.183 51.723 1.00 59.05 ? 807 NAG A C4 1 HETATM 5921 C C5 . NAG H 2 . ? 38.388 37.298 53.241 1.00 59.63 ? 807 NAG A C5 1 HETATM 5922 C C6 . NAG H 2 . ? 39.547 37.953 54.025 1.00 62.69 ? 807 NAG A C6 1 HETATM 5923 C C7 . NAG H 2 . ? 34.416 37.670 49.836 1.00 40.00 ? 807 NAG A C7 1 HETATM 5924 C C8 . NAG H 2 . ? 33.242 37.071 49.146 1.00 38.96 ? 807 NAG A C8 1 HETATM 5925 N N2 . NAG H 2 . ? 34.993 36.921 50.756 1.00 42.90 ? 807 NAG A N2 1 HETATM 5926 O O3 . NAG H 2 . ? 37.602 36.648 49.654 1.00 55.37 ? 807 NAG A O3 1 HETATM 5927 O O4 . NAG H 2 . ? 39.843 36.424 51.396 1.00 63.49 ? 807 NAG A O4 1 HETATM 5928 O O5 . NAG H 2 . ? 37.154 37.974 53.525 1.00 54.17 ? 807 NAG A O5 1 HETATM 5929 O O6 . NAG H 2 . ? 40.058 39.117 53.377 1.00 63.93 ? 807 NAG A O6 1 HETATM 5930 O O7 . NAG H 2 . ? 34.789 38.791 49.515 1.00 37.96 ? 807 NAG A O7 1 HETATM 5931 C C1 . NAG I 2 . ? 24.420 61.794 68.644 1.00 35.34 ? 808 NAG A C1 1 HETATM 5932 C C2 . NAG I 2 . ? 23.040 62.425 68.825 1.00 35.36 ? 808 NAG A C2 1 HETATM 5933 C C3 . NAG I 2 . ? 23.262 63.879 69.193 1.00 36.58 ? 808 NAG A C3 1 HETATM 5934 C C4 . NAG I 2 . ? 24.228 63.996 70.390 1.00 37.63 ? 808 NAG A C4 1 HETATM 5935 C C5 . NAG I 2 . ? 25.565 63.325 70.066 1.00 37.35 ? 808 NAG A C5 1 HETATM 5936 C C6 . NAG I 2 . ? 26.580 63.378 71.244 1.00 39.36 ? 808 NAG A C6 1 HETATM 5937 C C7 . NAG I 2 . ? 21.065 61.810 67.475 1.00 42.59 ? 808 NAG A C7 1 HETATM 5938 C C8 . NAG I 2 . ? 20.544 61.185 68.722 1.00 40.15 ? 808 NAG A C8 1 HETATM 5939 N N2 . NAG I 2 . ? 22.251 62.390 67.573 1.00 35.46 ? 808 NAG A N2 1 HETATM 5940 O O3 . NAG I 2 . ? 22.006 64.365 69.586 1.00 34.46 ? 808 NAG A O3 1 HETATM 5941 O O4 . NAG I 2 . ? 24.442 65.384 70.538 1.00 40.79 ? 808 NAG A O4 1 HETATM 5942 O O5 . NAG I 2 . ? 25.218 61.968 69.838 1.00 36.76 ? 808 NAG A O5 1 HETATM 5943 O O6 . NAG I 2 . ? 25.949 62.701 72.316 1.00 40.63 ? 808 NAG A O6 1 HETATM 5944 O O7 . NAG I 2 . ? 20.371 61.806 66.396 1.00 44.59 ? 808 NAG A O7 1 HETATM 5945 C C1 . NAG J 2 . ? 24.188 65.751 71.913 1.00 42.76 ? 809 NAG A C1 1 HETATM 5946 C C2 . NAG J 2 . ? 24.809 67.136 72.034 1.00 45.27 ? 809 NAG A C2 1 HETATM 5947 C C3 . NAG J 2 . ? 24.585 67.730 73.423 1.00 48.70 ? 809 NAG A C3 1 HETATM 5948 C C4 . NAG J 2 . ? 23.085 67.694 73.738 1.00 49.00 ? 809 NAG A C4 1 HETATM 5949 C C5 . NAG J 2 . ? 22.487 66.273 73.549 1.00 48.03 ? 809 NAG A C5 1 HETATM 5950 C C6 . NAG J 2 . ? 20.964 66.292 73.754 1.00 48.64 ? 809 NAG A C6 1 HETATM 5951 C C7 . NAG J 2 . ? 26.766 67.552 70.592 1.00 49.78 ? 809 NAG A C7 1 HETATM 5952 C C8 . NAG J 2 . ? 25.903 68.220 69.568 1.00 47.48 ? 809 NAG A C8 1 HETATM 5953 N N2 . NAG J 2 . ? 26.226 67.068 71.715 1.00 46.49 ? 809 NAG A N2 1 HETATM 5954 O O3 . NAG J 2 . ? 25.076 69.052 73.390 1.00 46.62 ? 809 NAG A O3 1 HETATM 5955 O O4 . NAG J 2 . ? 22.850 68.140 75.073 1.00 51.54 ? 809 NAG A O4 1 HETATM 5956 O O5 . NAG J 2 . ? 22.810 65.733 72.255 1.00 44.30 ? 809 NAG A O5 1 HETATM 5957 O O6 . NAG J 2 . ? 20.365 67.217 72.844 1.00 51.19 ? 809 NAG A O6 1 HETATM 5958 O O7 . NAG J 2 . ? 27.980 67.473 70.355 1.00 56.10 ? 809 NAG A O7 1 HETATM 5959 C C1 . NAG K 2 . ? 15.173 83.857 52.527 1.00 29.39 ? 810 NAG A C1 1 HETATM 5960 C C2 . NAG K 2 . ? 14.138 83.972 51.372 1.00 28.09 ? 810 NAG A C2 1 HETATM 5961 C C3 . NAG K 2 . ? 13.966 85.477 51.068 1.00 34.41 ? 810 NAG A C3 1 HETATM 5962 C C4 . NAG K 2 . ? 13.572 86.269 52.328 1.00 37.21 ? 810 NAG A C4 1 HETATM 5963 C C5 . NAG K 2 . ? 14.517 85.953 53.496 1.00 38.69 ? 810 NAG A C5 1 HETATM 5964 C C6 . NAG K 2 . ? 13.840 86.517 54.744 1.00 42.61 ? 810 NAG A C6 1 HETATM 5965 C C7 . NAG K 2 . ? 13.768 82.519 49.433 1.00 30.90 ? 810 NAG A C7 1 HETATM 5966 C C8 . NAG K 2 . ? 14.368 81.788 48.274 1.00 27.84 ? 810 NAG A C8 1 HETATM 5967 N N2 . NAG K 2 . ? 14.614 83.279 50.176 1.00 28.41 ? 810 NAG A N2 1 HETATM 5968 O O3 . NAG K 2 . ? 13.002 85.642 50.059 1.00 32.34 ? 810 NAG A O3 1 HETATM 5969 O O4 . NAG K 2 . ? 13.686 87.671 52.102 1.00 43.90 ? 810 NAG A O4 1 HETATM 5970 O O5 . NAG K 2 . ? 14.597 84.536 53.638 1.00 32.72 ? 810 NAG A O5 1 HETATM 5971 O O6 . NAG K 2 . ? 14.779 86.707 55.779 1.00 51.62 ? 810 NAG A O6 1 HETATM 5972 O O7 . NAG K 2 . ? 12.578 82.379 49.727 1.00 29.07 ? 810 NAG A O7 1 HETATM 5973 C C1 . NAG L 2 . ? 12.529 88.179 51.407 1.00 43.96 ? 811 NAG A C1 1 HETATM 5974 C C2 . NAG L 2 . ? 12.046 89.494 52.018 1.00 47.18 ? 811 NAG A C2 1 HETATM 5975 C C3 . NAG L 2 . ? 11.006 90.210 51.153 1.00 48.84 ? 811 NAG A C3 1 HETATM 5976 C C4 . NAG L 2 . ? 11.604 90.399 49.756 1.00 49.21 ? 811 NAG A C4 1 HETATM 5977 C C5 . NAG L 2 . ? 11.913 88.970 49.292 1.00 49.80 ? 811 NAG A C5 1 HETATM 5978 C C6 . NAG L 2 . ? 12.300 88.914 47.831 1.00 52.50 ? 811 NAG A C6 1 HETATM 5979 C C7 . NAG L 2 . ? 12.184 89.773 54.421 1.00 53.09 ? 811 NAG A C7 1 HETATM 5980 C C8 . NAG L 2 . ? 13.510 90.468 54.237 1.00 52.73 ? 811 NAG A C8 1 HETATM 5981 N N2 . NAG L 2 . ? 11.509 89.319 53.350 1.00 49.65 ? 811 NAG A N2 1 HETATM 5982 O O3 . NAG L 2 . ? 10.713 91.425 51.816 1.00 48.14 ? 811 NAG A O3 1 HETATM 5983 O O4 . NAG L 2 . ? 10.715 90.924 48.783 1.00 49.13 ? 811 NAG A O4 1 HETATM 5984 O O5 . NAG L 2 . ? 12.947 88.431 50.084 1.00 44.52 ? 811 NAG A O5 1 HETATM 5985 O O6 . NAG L 2 . ? 13.679 89.146 47.753 1.00 59.07 ? 811 NAG A O6 1 HETATM 5986 O O7 . NAG L 2 . ? 11.735 89.610 55.556 1.00 57.80 ? 811 NAG A O7 1 HETATM 5987 C C1 . BMA M 3 . ? 10.643 92.353 48.778 1.00 49.93 ? 812 BMA A C1 1 HETATM 5988 C C2 . BMA M 3 . ? 10.371 92.796 47.341 1.00 50.83 ? 812 BMA A C2 1 HETATM 5989 C C3 . BMA M 3 . ? 10.050 94.288 47.254 1.00 51.83 ? 812 BMA A C3 1 HETATM 5990 C C4 . BMA M 3 . ? 8.968 94.692 48.258 1.00 52.01 ? 812 BMA A C4 1 HETATM 5991 C C5 . BMA M 3 . ? 9.320 94.160 49.641 1.00 53.10 ? 812 BMA A C5 1 HETATM 5992 C C6 . BMA M 3 . ? 8.221 94.438 50.651 1.00 51.66 ? 812 BMA A C6 1 HETATM 5993 O O2 . BMA M 3 . ? 9.268 92.003 46.849 1.00 51.03 ? 812 BMA A O2 1 HETATM 5994 O O3 . BMA M 3 . ? 9.604 94.502 45.918 1.00 51.38 ? 812 BMA A O3 1 HETATM 5995 O O4 . BMA M 3 . ? 8.802 96.096 48.321 1.00 54.48 ? 812 BMA A O4 1 HETATM 5996 O O5 . BMA M 3 . ? 9.528 92.737 49.571 1.00 51.43 ? 812 BMA A O5 1 HETATM 5997 O O6 . BMA M 3 . ? 8.624 93.817 51.877 1.00 50.22 ? 812 BMA A O6 1 HETATM 5998 C C1 . MAN N 4 . ? 10.313 95.610 45.305 1.00 54.70 ? 813 MAN A C1 1 HETATM 5999 C C2 . MAN N 4 . ? 9.511 96.037 44.059 1.00 54.83 ? 813 MAN A C2 1 HETATM 6000 C C3 . MAN N 4 . ? 9.605 94.965 42.956 1.00 57.05 ? 813 MAN A C3 1 HETATM 6001 C C4 . MAN N 4 . ? 11.042 94.502 42.701 1.00 57.83 ? 813 MAN A C4 1 HETATM 6002 C C5 . MAN N 4 . ? 11.713 94.156 44.039 1.00 57.30 ? 813 MAN A C5 1 HETATM 6003 C C6 . MAN N 4 . ? 13.140 93.581 43.930 1.00 59.19 ? 813 MAN A C6 1 HETATM 6004 O O2 . MAN N 4 . ? 9.983 97.287 43.613 1.00 54.12 ? 813 MAN A O2 1 HETATM 6005 O O3 . MAN N 4 . ? 9.005 95.329 41.726 1.00 58.14 ? 813 MAN A O3 1 HETATM 6006 O O4 . MAN N 4 . ? 11.009 93.366 41.838 1.00 61.28 ? 813 MAN A O4 1 HETATM 6007 O O5 . MAN N 4 . ? 11.642 95.258 44.941 1.00 53.70 ? 813 MAN A O5 1 HETATM 6008 O O6 . MAN N 4 . ? 13.969 94.488 43.218 1.00 61.94 ? 813 MAN A O6 1 HETATM 6009 ZN ZN . ZN O 5 . ? 17.558 40.997 43.178 1.00 27.52 ? 814 ZN A ZN 1 HETATM 6010 ZN ZN . ZN P 5 . ? 16.905 41.817 46.295 1.00 25.00 ? 815 ZN A ZN 1 HETATM 6011 CA CA . CA Q 6 . ? -0.725 49.839 41.245 1.00 21.94 ? 816 CA A CA 1 HETATM 6012 CL CL . CL R 7 . ? 19.037 46.944 51.452 1.00 29.99 ? 817 CL A CL 1 HETATM 6013 C CAP . 2R7 S 8 . ? 15.297 43.663 41.387 1.00 38.59 ? 818 2R7 A CAP 1 HETATM 6014 C CAQ . 2R7 S 8 . ? 14.750 45.058 41.155 1.00 36.34 ? 818 2R7 A CAQ 1 HETATM 6015 C CBB . 2R7 S 8 . ? 16.167 44.873 41.156 1.00 37.54 ? 818 2R7 A CBB 1 HETATM 6016 C CAV . 2R7 S 8 . ? 17.099 44.722 40.065 1.00 36.18 ? 818 2R7 A CAV 1 HETATM 6017 O OAF . 2R7 S 8 . ? 16.808 43.855 39.195 1.00 31.97 ? 818 2R7 A OAF 1 HETATM 6018 O OAB . 2R7 S 8 . ? 18.102 45.451 40.041 1.00 37.59 ? 818 2R7 A OAB 1 HETATM 6019 N NAT . 2R7 S 8 . ? 16.950 45.259 42.369 1.00 38.12 ? 818 2R7 A NAT 1 HETATM 6020 C CAW . 2R7 S 8 . ? 18.074 44.597 42.760 1.00 41.97 ? 818 2R7 A CAW 1 HETATM 6021 O OAC . 2R7 S 8 . ? 18.424 43.510 42.271 1.00 37.91 ? 818 2R7 A OAC 1 HETATM 6022 N N . 2R7 S 8 . ? 18.720 45.150 43.800 1.00 41.12 ? 818 2R7 A N 1 HETATM 6023 C CA . 2R7 S 8 . ? 19.971 44.707 44.371 1.00 42.71 ? 818 2R7 A CA 1 HETATM 6024 C C . 2R7 S 8 . ? 20.115 45.436 45.736 1.00 42.75 ? 818 2R7 A C 1 HETATM 6025 O OXT . 2R7 S 8 . ? 20.664 44.728 46.637 1.00 43.68 ? 818 2R7 A OXT 1 HETATM 6026 O O . 2R7 S 8 . ? 19.671 46.655 45.823 1.00 41.89 ? 818 2R7 A O 1 HETATM 6027 C CB . 2R7 S 8 . ? 20.999 45.315 43.335 1.00 43.27 ? 818 2R7 A CB 1 HETATM 6028 C CAM . 2R7 S 8 . ? 22.493 45.311 43.672 1.00 47.53 ? 818 2R7 A CAM 1 HETATM 6029 C CAL . 2R7 S 8 . ? 23.289 45.960 42.491 1.00 48.20 ? 818 2R7 A CAL 1 HETATM 6030 C CAN . 2R7 S 8 . ? 23.496 47.496 42.650 1.00 50.26 ? 818 2R7 A CAN 1 HETATM 6031 N NAR . 2R7 S 8 . ? 23.670 47.902 44.075 1.00 53.47 ? 818 2R7 A NAR 1 HETATM 6032 C CAX . 2R7 S 8 . ? 23.219 49.061 44.592 1.00 53.84 ? 818 2R7 A CAX 1 HETATM 6033 O OAD . 2R7 S 8 . ? 22.578 49.873 43.910 1.00 55.71 ? 818 2R7 A OAD 1 HETATM 6034 C CAZ . 2R7 S 8 . ? 23.359 49.283 46.142 1.00 51.62 ? 818 2R7 A CAZ 1 HETATM 6035 C CAJ . 2R7 S 8 . ? 23.368 50.589 46.686 1.00 52.42 ? 818 2R7 A CAJ 1 HETATM 6036 C CAH . 2R7 S 8 . ? 23.466 50.809 48.084 1.00 49.78 ? 818 2R7 A CAH 1 HETATM 6037 C CAY . 2R7 S 8 . ? 23.535 49.762 49.018 1.00 49.42 ? 818 2R7 A CAY 1 HETATM 6038 I IAG . 2R7 S 8 . ? 23.663 50.140 51.187 1.00 51.73 ? 818 2R7 A IAG 1 HETATM 6039 C CAI . 2R7 S 8 . ? 23.513 48.464 48.471 1.00 51.75 ? 818 2R7 A CAI 1 HETATM 6040 C CAK . 2R7 S 8 . ? 23.422 48.222 47.068 1.00 51.98 ? 818 2R7 A CAK 1 HETATM 6041 O O . HOH T 9 . ? 8.268 44.603 46.244 1.00 20.77 ? 901 HOH A O 1 HETATM 6042 O O . HOH T 9 . ? 6.879 58.266 37.285 1.00 24.65 ? 902 HOH A O 1 HETATM 6043 O O . HOH T 9 . ? 7.970 69.536 58.989 1.00 24.94 ? 903 HOH A O 1 HETATM 6044 O O . HOH T 9 . ? 13.751 44.620 49.708 1.00 25.37 ? 904 HOH A O 1 HETATM 6045 O O . HOH T 9 . ? 9.253 50.670 46.300 1.00 21.19 ? 905 HOH A O 1 HETATM 6046 O O . HOH T 9 . ? 1.122 50.432 39.702 1.00 24.12 ? 906 HOH A O 1 HETATM 6047 O O . HOH T 9 . ? 11.980 61.748 43.499 1.00 25.13 ? 907 HOH A O 1 HETATM 6048 O O . HOH T 9 . ? 13.664 29.710 39.909 1.00 30.73 ? 908 HOH A O 1 HETATM 6049 O O . HOH T 9 . ? 15.195 41.862 38.588 1.00 24.79 ? 909 HOH A O 1 HETATM 6050 O O . HOH T 9 . ? 9.678 60.807 57.510 1.00 23.79 ? 910 HOH A O 1 HETATM 6051 O O . HOH T 9 . ? 10.989 36.665 42.216 1.00 23.62 ? 911 HOH A O 1 HETATM 6052 O O . HOH T 9 . ? -5.465 59.601 59.627 1.00 23.52 ? 912 HOH A O 1 HETATM 6053 O O . HOH T 9 . ? 13.771 26.964 51.587 1.00 29.35 ? 913 HOH A O 1 HETATM 6054 O O . HOH T 9 . ? 7.467 71.685 45.081 1.00 26.18 ? 914 HOH A O 1 HETATM 6055 O O . HOH T 9 . ? 5.677 68.843 55.249 1.00 24.37 ? 915 HOH A O 1 HETATM 6056 O O . HOH T 9 . ? 16.881 37.038 43.870 1.00 25.63 ? 916 HOH A O 1 HETATM 6057 O O . HOH T 9 . ? -3.643 62.070 53.839 1.00 25.98 ? 917 HOH A O 1 HETATM 6058 O O . HOH T 9 . ? 29.515 36.141 44.255 1.00 26.52 ? 918 HOH A O 1 HETATM 6059 O O . HOH T 9 . ? 6.460 75.947 60.799 1.00 25.55 ? 919 HOH A O 1 HETATM 6060 O O . HOH T 9 . ? -3.535 60.014 61.728 1.00 25.83 ? 920 HOH A O 1 HETATM 6061 O O . HOH T 9 . ? 19.374 47.738 54.584 1.00 34.22 ? 921 HOH A O 1 HETATM 6062 O O . HOH T 9 . ? 3.954 70.381 64.305 1.00 29.26 ? 922 HOH A O 1 HETATM 6063 O O . HOH T 9 . ? 19.151 62.051 36.303 1.00 30.08 ? 923 HOH A O 1 HETATM 6064 O O . HOH T 9 . ? -6.966 51.474 51.371 1.00 29.03 ? 924 HOH A O 1 HETATM 6065 O O . HOH T 9 . ? 18.015 40.551 32.167 1.00 28.53 ? 925 HOH A O 1 HETATM 6066 O O . HOH T 9 . ? 20.113 61.473 62.798 1.00 28.31 ? 926 HOH A O 1 HETATM 6067 O O . HOH T 9 . ? -4.412 59.449 57.101 1.00 24.91 ? 927 HOH A O 1 HETATM 6068 O O . HOH T 9 . ? 3.513 71.940 43.330 1.00 26.26 ? 928 HOH A O 1 HETATM 6069 O O . HOH T 9 . ? 30.157 42.684 32.339 1.00 34.36 ? 929 HOH A O 1 HETATM 6070 O O . HOH T 9 . ? 24.057 46.083 34.668 1.00 29.09 ? 930 HOH A O 1 HETATM 6071 O O . HOH T 9 . ? 14.880 36.867 27.773 1.00 26.90 ? 931 HOH A O 1 HETATM 6072 O O . HOH T 9 . ? 18.546 33.429 43.381 1.00 31.06 ? 932 HOH A O 1 HETATM 6073 O O . HOH T 9 . ? 29.057 33.864 32.685 1.00 31.83 ? 933 HOH A O 1 HETATM 6074 O O . HOH T 9 . ? 5.992 75.373 54.004 1.00 28.35 ? 934 HOH A O 1 HETATM 6075 O O . HOH T 9 . ? 3.654 62.240 50.394 1.00 25.87 ? 935 HOH A O 1 HETATM 6076 O O . HOH T 9 . ? 14.771 32.038 48.040 1.00 27.26 ? 936 HOH A O 1 HETATM 6077 O O . HOH T 9 . ? 4.554 34.887 45.287 1.00 29.23 ? 937 HOH A O 1 HETATM 6078 O O . HOH T 9 . ? 0.330 56.827 45.548 1.00 28.75 ? 938 HOH A O 1 HETATM 6079 O O . HOH T 9 . ? -0.429 64.661 65.824 0.50 26.92 ? 939 HOH A O 1 HETATM 6080 O O . HOH T 9 . ? -0.333 43.403 60.512 1.00 30.75 ? 940 HOH A O 1 HETATM 6081 O O . HOH T 9 . ? 14.558 38.060 34.759 1.00 28.00 ? 941 HOH A O 1 HETATM 6082 O O . HOH T 9 . ? 22.083 87.922 32.215 1.00 38.11 ? 942 HOH A O 1 HETATM 6083 O O . HOH T 9 . ? 23.257 67.658 33.948 1.00 34.46 ? 943 HOH A O 1 HETATM 6084 O O . HOH T 9 . ? 23.308 68.714 42.871 1.00 31.33 ? 944 HOH A O 1 HETATM 6085 O O . HOH T 9 . ? 20.792 45.784 36.407 1.00 29.73 ? 945 HOH A O 1 HETATM 6086 O O . HOH T 9 . ? 24.630 37.286 32.418 1.00 30.94 ? 946 HOH A O 1 HETATM 6087 O O . HOH T 9 . ? 16.355 55.680 35.373 1.00 30.40 ? 947 HOH A O 1 HETATM 6088 O O . HOH T 9 . ? 25.873 37.094 38.058 1.00 30.11 ? 948 HOH A O 1 HETATM 6089 O O . HOH T 9 . ? 9.636 29.054 42.989 1.00 28.36 ? 949 HOH A O 1 HETATM 6090 O O . HOH T 9 . ? 27.654 31.071 28.684 1.00 34.67 ? 950 HOH A O 1 HETATM 6091 O O . HOH T 9 . ? 20.794 27.391 48.841 1.00 30.74 ? 951 HOH A O 1 HETATM 6092 O O . HOH T 9 . ? 10.256 30.979 26.497 1.00 35.43 ? 952 HOH A O 1 HETATM 6093 O O . HOH T 9 . ? 29.154 60.559 57.281 1.00 36.97 ? 953 HOH A O 1 HETATM 6094 O O . HOH T 9 . ? 16.980 61.916 38.180 1.00 33.47 ? 954 HOH A O 1 HETATM 6095 O O . HOH T 9 . ? 19.370 36.012 43.011 1.00 32.54 ? 955 HOH A O 1 HETATM 6096 O O . HOH T 9 . ? 20.180 31.102 43.490 1.00 31.48 ? 956 HOH A O 1 HETATM 6097 O O . HOH T 9 . ? 8.213 50.350 40.631 1.00 29.08 ? 957 HOH A O 1 HETATM 6098 O O . HOH T 9 . ? -2.471 44.080 37.501 1.00 25.68 ? 958 HOH A O 1 HETATM 6099 O O . HOH T 9 . ? 6.556 60.770 67.068 1.00 33.52 ? 959 HOH A O 1 HETATM 6100 O O . HOH T 9 . ? 5.199 64.710 36.838 1.00 28.96 ? 960 HOH A O 1 HETATM 6101 O O . HOH T 9 . ? 14.690 80.744 37.976 1.00 31.89 ? 961 HOH A O 1 HETATM 6102 O O . HOH T 9 . ? 6.875 55.215 43.537 1.00 30.67 ? 962 HOH A O 1 HETATM 6103 O O . HOH T 9 . ? 14.091 40.695 53.366 1.00 30.14 ? 963 HOH A O 1 HETATM 6104 O O . HOH T 9 . ? 11.164 27.366 54.297 1.00 31.18 ? 964 HOH A O 1 HETATM 6105 O O . HOH T 9 . ? 23.143 44.443 36.554 1.00 32.84 ? 965 HOH A O 1 HETATM 6106 O O . HOH T 9 . ? 4.307 66.951 51.355 1.00 27.79 ? 966 HOH A O 1 HETATM 6107 O O . HOH T 9 . ? 3.959 68.556 49.037 1.00 28.97 ? 967 HOH A O 1 HETATM 6108 O O . HOH T 9 . ? -4.497 55.038 51.651 1.00 28.12 ? 968 HOH A O 1 HETATM 6109 O O . HOH T 9 . ? 1.196 59.241 46.287 1.00 32.68 ? 969 HOH A O 1 HETATM 6110 O O . HOH T 9 . ? 2.669 32.988 45.241 1.00 31.96 ? 970 HOH A O 1 HETATM 6111 O O . HOH T 9 . ? -4.030 57.501 46.023 1.00 30.66 ? 971 HOH A O 1 HETATM 6112 O O . HOH T 9 . ? 11.164 63.397 58.096 1.00 33.66 ? 972 HOH A O 1 HETATM 6113 O O . HOH T 9 . ? 28.759 53.813 52.794 1.00 31.57 ? 973 HOH A O 1 HETATM 6114 O O . HOH T 9 . ? 13.734 71.341 40.344 1.00 25.74 ? 974 HOH A O 1 HETATM 6115 O O . HOH T 9 . ? 19.179 27.753 34.986 1.00 32.01 ? 975 HOH A O 1 HETATM 6116 O O . HOH T 9 . ? 13.310 77.711 63.460 1.00 37.02 ? 976 HOH A O 1 HETATM 6117 O O . HOH T 9 . ? 34.548 41.527 50.151 1.00 38.71 ? 977 HOH A O 1 HETATM 6118 O O . HOH T 9 . ? 26.550 39.039 36.254 1.00 31.21 ? 978 HOH A O 1 HETATM 6119 O O . HOH T 9 . ? -2.476 59.216 48.477 1.00 31.61 ? 979 HOH A O 1 HETATM 6120 O O . HOH T 9 . ? 8.862 74.545 66.502 1.00 31.21 ? 980 HOH A O 1 HETATM 6121 O O . HOH T 9 . ? 24.546 31.588 28.671 1.00 38.45 ? 981 HOH A O 1 HETATM 6122 O O . HOH T 9 . ? 5.668 62.640 64.885 1.00 35.76 ? 982 HOH A O 1 HETATM 6123 O O . HOH T 9 . ? 14.483 31.852 29.389 1.00 33.78 ? 983 HOH A O 1 HETATM 6124 O O . HOH T 9 . ? 12.139 34.946 53.556 1.00 30.30 ? 984 HOH A O 1 HETATM 6125 O O . HOH T 9 . ? 10.750 37.377 54.325 1.00 37.58 ? 985 HOH A O 1 HETATM 6126 O O . HOH T 9 . ? 21.333 63.514 60.869 1.00 28.99 ? 986 HOH A O 1 HETATM 6127 O O . HOH T 9 . ? 3.729 27.501 41.395 1.00 35.52 ? 987 HOH A O 1 HETATM 6128 O O . HOH T 9 . ? 19.507 53.505 45.167 1.00 49.86 ? 988 HOH A O 1 HETATM 6129 O O . HOH T 9 . ? 19.309 60.137 49.922 1.00 37.17 ? 989 HOH A O 1 HETATM 6130 O O . HOH T 9 . ? 20.526 53.177 47.444 1.00 36.62 ? 990 HOH A O 1 HETATM 6131 O O . HOH T 9 . ? 31.216 39.886 46.615 1.00 33.19 ? 991 HOH A O 1 HETATM 6132 O O . HOH T 9 . ? 5.343 77.975 54.367 1.00 33.27 ? 992 HOH A O 1 HETATM 6133 O O . HOH T 9 . ? 32.320 35.039 59.238 1.00 38.46 ? 993 HOH A O 1 HETATM 6134 O O . HOH T 9 . ? 21.882 61.624 36.765 1.00 38.75 ? 994 HOH A O 1 HETATM 6135 O O . HOH T 9 . ? 14.755 59.003 74.371 1.00 38.86 ? 995 HOH A O 1 HETATM 6136 O O . HOH T 9 . ? 29.538 70.255 45.989 1.00 37.20 ? 996 HOH A O 1 HETATM 6137 O O . HOH T 9 . ? -2.182 55.511 46.140 1.00 32.77 ? 997 HOH A O 1 HETATM 6138 O O . HOH T 9 . ? 24.017 40.578 69.369 1.00 39.39 ? 998 HOH A O 1 HETATM 6139 O O . HOH T 9 . ? 5.672 62.689 70.341 1.00 32.86 ? 999 HOH A O 1 HETATM 6140 O O . HOH T 9 . ? 16.876 68.156 64.233 1.00 35.30 ? 1000 HOH A O 1 HETATM 6141 O O . HOH T 9 . ? 25.192 32.871 67.886 1.00 41.15 ? 1001 HOH A O 1 HETATM 6142 O O . HOH T 9 . ? 15.094 61.809 72.994 1.00 35.58 ? 1002 HOH A O 1 HETATM 6143 O O . HOH T 9 . ? 0.270 31.302 58.190 1.00 37.83 ? 1003 HOH A O 1 HETATM 6144 O O . HOH T 9 . ? 18.621 55.312 30.392 1.00 43.16 ? 1004 HOH A O 1 HETATM 6145 O O . HOH T 9 . ? 9.066 68.971 40.739 1.00 27.96 ? 1005 HOH A O 1 HETATM 6146 O O . HOH T 9 . ? 12.234 36.942 28.509 1.00 29.39 ? 1006 HOH A O 1 HETATM 6147 O O . HOH T 9 . ? 0.554 33.289 43.241 1.00 31.80 ? 1007 HOH A O 1 HETATM 6148 O O . HOH T 9 . ? 1.105 63.311 42.862 1.00 38.82 ? 1008 HOH A O 1 HETATM 6149 O O . HOH T 9 . ? 33.988 47.862 58.898 1.00 40.64 ? 1009 HOH A O 1 HETATM 6150 O O . HOH T 9 . ? 17.198 81.616 37.052 1.00 35.99 ? 1010 HOH A O 1 HETATM 6151 O O . HOH T 9 . ? 15.068 68.924 41.439 1.00 36.70 ? 1011 HOH A O 1 HETATM 6152 O O . HOH T 9 . ? 16.562 26.163 34.535 1.00 36.70 ? 1012 HOH A O 1 HETATM 6153 O O . HOH T 9 . ? 23.398 55.193 31.318 1.00 36.70 ? 1013 HOH A O 1 HETATM 6154 O O . HOH T 9 . ? 17.529 82.481 41.063 1.00 44.96 ? 1014 HOH A O 1 HETATM 6155 O O . HOH T 9 . ? 24.065 75.076 54.534 1.00 38.10 ? 1015 HOH A O 1 HETATM 6156 O O . HOH T 9 . ? 23.130 67.434 40.479 1.00 39.19 ? 1016 HOH A O 1 HETATM 6157 O O . HOH T 9 . ? 8.091 51.704 42.923 1.00 32.52 ? 1017 HOH A O 1 HETATM 6158 O O . HOH T 9 . ? 29.962 27.076 33.521 1.00 38.50 ? 1018 HOH A O 1 HETATM 6159 O O . HOH T 9 . ? 6.322 38.715 26.236 1.00 37.94 ? 1019 HOH A O 1 HETATM 6160 O O . HOH T 9 . ? 18.861 68.910 65.597 1.00 39.78 ? 1020 HOH A O 1 HETATM 6161 O O . HOH T 9 . ? 21.753 74.489 60.517 1.00 37.15 ? 1021 HOH A O 1 HETATM 6162 O O . HOH T 9 . ? -2.046 33.881 40.504 1.00 35.94 ? 1022 HOH A O 1 HETATM 6163 O O . HOH T 9 . ? 13.417 82.748 55.605 1.00 35.86 ? 1023 HOH A O 1 HETATM 6164 O O . HOH T 9 . ? 25.771 35.497 68.159 1.00 40.49 ? 1024 HOH A O 1 HETATM 6165 O O . HOH T 9 . ? 23.854 73.134 59.213 1.00 35.82 ? 1025 HOH A O 1 HETATM 6166 O O . HOH T 9 . ? -1.354 61.517 62.083 1.00 33.05 ? 1026 HOH A O 1 HETATM 6167 O O . HOH T 9 . ? 10.125 35.998 69.861 1.00 38.57 ? 1027 HOH A O 1 HETATM 6168 O O . HOH T 9 . ? 14.078 57.532 35.097 1.00 34.62 ? 1028 HOH A O 1 HETATM 6169 O O . HOH T 9 . ? 13.700 29.456 28.385 1.00 31.42 ? 1029 HOH A O 1 HETATM 6170 O O . HOH T 9 . ? 36.825 42.485 65.286 1.00 45.33 ? 1030 HOH A O 1 HETATM 6171 O O . HOH T 9 . ? 10.885 28.814 40.377 1.00 33.66 ? 1031 HOH A O 1 HETATM 6172 O O . HOH T 9 . ? 11.815 40.815 55.279 1.00 31.09 ? 1032 HOH A O 1 HETATM 6173 O O . HOH T 9 . ? 19.205 63.472 32.107 1.00 44.64 ? 1033 HOH A O 1 HETATM 6174 O O . HOH T 9 . ? 12.657 53.182 36.046 1.00 34.98 ? 1034 HOH A O 1 HETATM 6175 O O . HOH T 9 . ? 23.452 56.714 45.008 1.00 42.08 ? 1035 HOH A O 1 HETATM 6176 O O . HOH T 9 . ? 21.915 61.088 51.541 1.00 35.35 ? 1036 HOH A O 1 HETATM 6177 O O . HOH T 9 . ? 25.922 27.280 24.119 1.00 44.57 ? 1037 HOH A O 1 HETATM 6178 O O . HOH T 9 . ? 25.676 56.005 37.518 1.00 36.59 ? 1038 HOH A O 1 HETATM 6179 O O . HOH T 9 . ? 20.327 31.370 26.075 1.00 39.77 ? 1039 HOH A O 1 HETATM 6180 O O . HOH T 9 . ? 31.058 52.409 52.677 1.00 40.01 ? 1040 HOH A O 1 HETATM 6181 O O . HOH T 9 . ? 6.532 76.354 67.267 1.00 40.09 ? 1041 HOH A O 1 HETATM 6182 O O . HOH T 9 . ? 10.642 55.516 75.022 1.00 40.38 ? 1042 HOH A O 1 HETATM 6183 O O . HOH T 9 . ? 21.366 32.407 28.535 1.00 36.46 ? 1043 HOH A O 1 HETATM 6184 O O . HOH T 9 . ? 25.329 70.390 30.993 1.00 38.90 ? 1044 HOH A O 1 HETATM 6185 O O . HOH T 9 . ? 18.920 69.466 28.294 1.00 36.59 ? 1045 HOH A O 1 HETATM 6186 O O . HOH T 9 . ? 23.539 78.965 50.419 1.00 37.33 ? 1046 HOH A O 1 HETATM 6187 O O . HOH T 9 . ? -9.632 46.021 34.006 1.00 40.89 ? 1047 HOH A O 1 HETATM 6188 O O . HOH T 9 . ? 29.261 40.299 64.857 1.00 40.79 ? 1048 HOH A O 1 HETATM 6189 O O . HOH T 9 . ? 11.811 27.849 28.986 1.00 41.38 ? 1049 HOH A O 1 HETATM 6190 O O . HOH T 9 . ? 25.276 63.452 49.904 1.00 36.07 ? 1050 HOH A O 1 HETATM 6191 O O . HOH T 9 . ? 16.363 29.059 28.022 1.00 38.71 ? 1051 HOH A O 1 HETATM 6192 O O . HOH T 9 . ? 13.802 79.835 67.849 1.00 43.29 ? 1052 HOH A O 1 HETATM 6193 O O . HOH T 9 . ? 5.174 31.719 29.940 1.00 48.83 ? 1053 HOH A O 1 HETATM 6194 O O . HOH T 9 . ? 14.256 81.227 40.507 1.00 43.69 ? 1054 HOH A O 1 HETATM 6195 O O . HOH T 9 . ? 10.205 80.950 63.591 1.00 41.37 ? 1055 HOH A O 1 HETATM 6196 O O . HOH T 9 . ? 4.228 63.393 72.613 1.00 36.06 ? 1056 HOH A O 1 HETATM 6197 O O . HOH T 9 . ? 21.756 84.038 46.934 1.00 42.14 ? 1057 HOH A O 1 HETATM 6198 O O . HOH T 9 . ? 27.925 54.297 50.474 1.00 47.35 ? 1058 HOH A O 1 HETATM 6199 O O . HOH T 9 . ? 20.908 50.423 75.961 1.00 46.11 ? 1059 HOH A O 1 HETATM 6200 O O . HOH T 9 . ? 7.673 38.626 29.192 1.00 36.14 ? 1060 HOH A O 1 HETATM 6201 O O . HOH T 9 . ? 38.307 34.535 26.449 1.00 50.17 ? 1061 HOH A O 1 HETATM 6202 O O . HOH T 9 . ? 4.643 62.027 74.986 1.00 35.09 ? 1062 HOH A O 1 HETATM 6203 O O . HOH T 9 . ? -1.662 32.285 44.558 1.00 45.32 ? 1063 HOH A O 1 HETATM 6204 O O . HOH T 9 . ? -12.791 47.505 37.392 1.00 37.86 ? 1064 HOH A O 1 HETATM 6205 O O . HOH T 9 . ? 29.559 50.088 39.064 1.00 47.51 ? 1065 HOH A O 1 HETATM 6206 O O . HOH T 9 . ? -10.001 43.711 47.061 1.00 40.11 ? 1066 HOH A O 1 HETATM 6207 O O . HOH T 9 . ? 30.031 25.271 47.319 1.00 51.01 ? 1067 HOH A O 1 HETATM 6208 O O . HOH T 9 . ? 29.474 54.342 34.849 1.00 41.29 ? 1068 HOH A O 1 HETATM 6209 O O . HOH T 9 . ? -0.749 58.070 43.131 1.00 28.28 ? 1069 HOH A O 1 HETATM 6210 O O . HOH T 9 . ? -2.882 38.410 63.035 1.00 40.84 ? 1070 HOH A O 1 HETATM 6211 O O . HOH T 9 . ? 11.617 38.303 56.422 1.00 39.28 ? 1071 HOH A O 1 HETATM 6212 O O . HOH T 9 . ? 25.634 66.986 29.867 1.00 43.12 ? 1072 HOH A O 1 HETATM 6213 O O . HOH T 9 . ? 16.734 69.086 20.513 1.00 57.45 ? 1073 HOH A O 1 HETATM 6214 O O . HOH T 9 . ? 11.977 63.681 35.196 1.00 40.67 ? 1074 HOH A O 1 HETATM 6215 O O . HOH T 9 . ? 25.107 65.797 40.215 1.00 48.52 ? 1075 HOH A O 1 HETATM 6216 O O . HOH T 9 . ? 32.047 55.251 26.337 1.00 47.97 ? 1076 HOH A O 1 HETATM 6217 O O . HOH T 9 . ? 18.184 31.005 29.045 1.00 37.08 ? 1077 HOH A O 1 HETATM 6218 O O . HOH T 9 . ? 29.006 26.044 36.094 1.00 39.05 ? 1078 HOH A O 1 HETATM 6219 O O . HOH T 9 . ? 16.602 79.532 21.018 1.00 51.65 ? 1079 HOH A O 1 HETATM 6220 O O . HOH T 9 . ? 20.028 25.669 36.650 1.00 37.72 ? 1080 HOH A O 1 HETATM 6221 O O . HOH T 9 . ? 28.117 45.231 68.850 1.00 38.48 ? 1081 HOH A O 1 HETATM 6222 O O . HOH T 9 . ? 17.922 52.329 74.958 1.00 43.03 ? 1082 HOH A O 1 HETATM 6223 O O . HOH T 9 . ? 12.956 93.560 40.289 1.00 53.50 ? 1083 HOH A O 1 HETATM 6224 O O . HOH T 9 . ? 0.532 33.440 36.498 1.00 47.46 ? 1084 HOH A O 1 HETATM 6225 O O . HOH T 9 . ? 25.875 25.470 20.024 1.00 50.49 ? 1085 HOH A O 1 HETATM 6226 O O . HOH T 9 . ? 35.155 50.987 31.402 1.00 54.99 ? 1086 HOH A O 1 HETATM 6227 O O . HOH T 9 . ? 20.840 30.141 29.868 1.00 41.22 ? 1087 HOH A O 1 HETATM 6228 O O . HOH T 9 . ? 24.655 29.481 30.266 1.00 37.91 ? 1088 HOH A O 1 HETATM 6229 O O . HOH T 9 . ? 26.548 40.133 13.346 1.00 47.91 ? 1089 HOH A O 1 HETATM 6230 O O . HOH T 9 . ? -2.701 32.908 55.653 0.50 32.73 ? 1090 HOH A O 1 HETATM 6231 O O . HOH T 9 . ? 24.019 82.318 42.358 1.00 48.79 ? 1091 HOH A O 1 HETATM 6232 O O . HOH T 9 . ? 29.275 78.993 27.299 1.00 51.82 ? 1092 HOH A O 1 HETATM 6233 O O . HOH T 9 . ? 10.582 27.124 51.527 1.00 37.03 ? 1093 HOH A O 1 HETATM 6234 O O . HOH T 9 . ? 5.288 40.285 23.032 1.00 40.24 ? 1094 HOH A O 1 HETATM 6235 O O . HOH T 9 . ? 36.025 42.950 57.522 1.00 44.53 ? 1095 HOH A O 1 HETATM 6236 O O . HOH T 9 . ? 36.948 52.394 68.485 1.00 48.55 ? 1096 HOH A O 1 HETATM 6237 O O . HOH T 9 . ? 9.920 69.869 38.438 1.00 38.39 ? 1097 HOH A O 1 HETATM 6238 O O . HOH T 9 . ? 22.907 65.338 66.020 1.00 42.92 ? 1098 HOH A O 1 HETATM 6239 O O . HOH T 9 . ? 27.315 57.014 70.261 1.00 44.22 ? 1099 HOH A O 1 HETATM 6240 O O . HOH T 9 . ? 6.962 75.815 37.499 1.00 35.72 ? 1100 HOH A O 1 HETATM 6241 O O . HOH T 9 . ? 34.866 41.350 19.469 1.00 58.95 ? 1101 HOH A O 1 HETATM 6242 O O . HOH T 9 . ? 39.853 43.878 58.283 1.00 44.79 ? 1102 HOH A O 1 HETATM 6243 O O . HOH T 9 . ? 28.033 72.094 52.820 1.00 44.31 ? 1103 HOH A O 1 HETATM 6244 O O . HOH T 9 . ? 5.182 31.393 24.412 1.00 41.43 ? 1104 HOH A O 1 HETATM 6245 O O . HOH T 9 . ? 26.509 60.291 30.813 1.00 52.19 ? 1105 HOH A O 1 HETATM 6246 O O . HOH T 9 . ? -1.643 45.893 55.610 1.00 37.81 ? 1106 HOH A O 1 HETATM 6247 O O . HOH T 9 . ? 1.550 30.994 64.663 1.00 47.26 ? 1107 HOH A O 1 HETATM 6248 O O . HOH T 9 . ? 21.737 25.209 23.713 1.00 46.78 ? 1108 HOH A O 1 HETATM 6249 O O . HOH T 9 . ? 24.149 61.440 34.764 1.00 46.06 ? 1109 HOH A O 1 HETATM 6250 O O . HOH T 9 . ? 11.006 76.625 28.415 1.00 45.85 ? 1110 HOH A O 1 HETATM 6251 O O . HOH T 9 . ? 26.260 23.431 45.791 1.00 47.56 ? 1111 HOH A O 1 HETATM 6252 O O . HOH T 9 . ? 20.818 44.082 11.351 1.00 50.83 ? 1112 HOH A O 1 HETATM 6253 O O . HOH T 9 . ? -3.881 37.359 56.451 1.00 39.82 ? 1113 HOH A O 1 HETATM 6254 O O . HOH T 9 . ? 16.349 67.345 72.323 1.00 60.73 ? 1114 HOH A O 1 HETATM 6255 O O . HOH T 9 . ? 11.730 48.795 29.522 1.00 36.37 ? 1115 HOH A O 1 HETATM 6256 O O . HOH T 9 . ? 5.474 66.029 33.568 1.00 49.80 ? 1116 HOH A O 1 HETATM 6257 O O . HOH T 9 . ? -2.909 37.805 32.439 1.00 39.61 ? 1117 HOH A O 1 HETATM 6258 O O . HOH T 9 . ? 24.252 77.831 52.846 1.00 45.75 ? 1118 HOH A O 1 HETATM 6259 O O . HOH T 9 . ? 20.693 74.422 23.509 1.00 50.68 ? 1119 HOH A O 1 HETATM 6260 O O . HOH T 9 . ? 10.408 51.685 39.730 1.00 29.62 ? 1120 HOH A O 1 HETATM 6261 O O . HOH T 9 . ? 30.768 83.903 28.408 1.00 53.55 ? 1121 HOH A O 1 HETATM 6262 O O . HOH T 9 . ? 0.373 62.938 48.063 1.00 45.48 ? 1122 HOH A O 1 HETATM 6263 O O . HOH T 9 . ? 26.532 66.030 26.125 1.00 48.42 ? 1123 HOH A O 1 HETATM 6264 O O . HOH T 9 . ? 31.679 46.840 36.728 1.00 48.84 ? 1124 HOH A O 1 HETATM 6265 O O . HOH T 9 . ? 28.359 63.975 23.028 1.00 59.32 ? 1125 HOH A O 1 HETATM 6266 O O . HOH T 9 . ? -4.315 53.127 37.057 1.00 35.50 ? 1126 HOH A O 1 HETATM 6267 O O . HOH T 9 . ? 28.757 44.336 65.523 1.00 45.54 ? 1127 HOH A O 1 HETATM 6268 O O . HOH T 9 . ? 8.373 82.328 51.814 1.00 44.01 ? 1128 HOH A O 1 HETATM 6269 O O . HOH T 9 . ? 33.044 29.840 24.483 1.00 49.36 ? 1129 HOH A O 1 HETATM 6270 O O . HOH T 9 . ? 15.015 52.844 34.682 1.00 42.13 ? 1130 HOH A O 1 HETATM 6271 O O . HOH T 9 . ? 15.300 24.577 58.472 1.00 43.05 ? 1131 HOH A O 1 HETATM 6272 O O . HOH T 9 . ? 4.266 43.512 75.895 1.00 57.22 ? 1132 HOH A O 1 HETATM 6273 O O . HOH T 9 . ? 9.297 52.079 75.045 1.00 46.47 ? 1133 HOH A O 1 HETATM 6274 O O . HOH T 9 . ? 18.871 65.832 27.907 1.00 51.65 ? 1134 HOH A O 1 HETATM 6275 O O . HOH T 9 . ? 17.918 32.196 70.545 1.00 44.36 ? 1135 HOH A O 1 HETATM 6276 O O . HOH T 9 . ? 14.145 50.364 18.849 1.00 43.73 ? 1136 HOH A O 1 HETATM 6277 O O . HOH T 9 . ? 17.802 65.029 30.394 1.00 44.72 ? 1137 HOH A O 1 HETATM 6278 O O . HOH T 9 . ? 3.387 27.343 57.309 1.00 55.53 ? 1138 HOH A O 1 HETATM 6279 O O . HOH T 9 . ? 26.005 24.783 57.580 1.00 47.73 ? 1139 HOH A O 1 HETATM 6280 O O . HOH T 9 . ? 3.710 27.216 54.649 1.00 39.51 ? 1140 HOH A O 1 HETATM 6281 O O . HOH T 9 . ? 14.904 81.498 28.249 1.00 46.14 ? 1141 HOH A O 1 HETATM 6282 O O . HOH T 9 . ? 23.788 45.439 39.132 1.00 41.87 ? 1142 HOH A O 1 HETATM 6283 O O . HOH T 9 . ? -4.363 53.800 34.362 1.00 43.42 ? 1143 HOH A O 1 HETATM 6284 O O . HOH T 9 . ? 21.688 75.135 66.750 1.00 50.65 ? 1144 HOH A O 1 HETATM 6285 O O . HOH T 9 . ? 34.592 32.652 27.430 1.00 58.09 ? 1145 HOH A O 1 HETATM 6286 O O . HOH T 9 . ? 21.254 88.306 44.071 1.00 48.58 ? 1146 HOH A O 1 HETATM 6287 O O . HOH T 9 . ? -4.398 36.879 51.273 1.00 52.24 ? 1147 HOH A O 1 HETATM 6288 O O . HOH T 9 . ? 33.851 28.847 34.179 1.00 49.62 ? 1148 HOH A O 1 HETATM 6289 O O . HOH T 9 . ? -5.929 41.444 44.218 1.00 43.98 ? 1149 HOH A O 1 HETATM 6290 O O . HOH T 9 . ? 13.861 65.206 35.896 1.00 45.59 ? 1150 HOH A O 1 HETATM 6291 O O . HOH T 9 . ? 33.901 40.166 47.618 1.00 42.25 ? 1151 HOH A O 1 HETATM 6292 O O . HOH T 9 . ? 31.542 31.731 17.235 1.00 51.56 ? 1152 HOH A O 1 HETATM 6293 O O . HOH T 9 . ? 30.584 59.814 25.362 1.00 54.47 ? 1153 HOH A O 1 HETATM 6294 O O . HOH T 9 . ? 5.372 53.092 77.653 1.00 56.19 ? 1154 HOH A O 1 HETATM 6295 O O . HOH T 9 . ? 12.556 43.715 17.094 1.00 43.15 ? 1155 HOH A O 1 HETATM 6296 O O . HOH T 9 . ? 26.498 69.236 28.937 1.00 48.97 ? 1156 HOH A O 1 HETATM 6297 O O . HOH T 9 . ? 36.492 43.111 49.309 1.00 47.93 ? 1157 HOH A O 1 HETATM 6298 O O . HOH T 9 . ? 13.620 28.020 16.997 1.00 56.90 ? 1158 HOH A O 1 HETATM 6299 O O . HOH T 9 . ? -3.208 46.944 53.022 1.00 39.50 ? 1159 HOH A O 1 HETATM 6300 O O . HOH T 9 . ? -7.370 48.102 47.904 1.00 46.96 ? 1160 HOH A O 1 HETATM 6301 O O . HOH T 9 . ? -0.703 32.272 60.691 1.00 46.56 ? 1161 HOH A O 1 HETATM 6302 O O . HOH T 9 . ? 20.078 56.015 22.901 1.00 47.97 ? 1162 HOH A O 1 HETATM 6303 O O . HOH T 9 . ? 32.875 42.857 20.067 1.00 56.24 ? 1163 HOH A O 1 HETATM 6304 O O . HOH T 9 . ? 21.405 23.889 51.197 1.00 47.30 ? 1164 HOH A O 1 HETATM 6305 O O . HOH T 9 . ? 16.751 63.572 68.698 1.00 55.33 ? 1165 HOH A O 1 HETATM 6306 O O . HOH T 9 . ? 29.236 28.022 59.424 1.00 51.21 ? 1166 HOH A O 1 HETATM 6307 O O . HOH T 9 . ? 27.165 20.236 39.801 1.00 48.47 ? 1167 HOH A O 1 HETATM 6308 O O . HOH T 9 . ? 5.307 81.498 53.915 1.00 44.81 ? 1168 HOH A O 1 HETATM 6309 O O . HOH T 9 . ? 8.552 29.203 33.153 1.00 45.26 ? 1169 HOH A O 1 HETATM 6310 O O . HOH T 9 . ? -1.254 51.360 72.375 1.00 44.02 ? 1170 HOH A O 1 HETATM 6311 O O . HOH T 9 . ? 6.211 68.420 37.070 1.00 41.39 ? 1171 HOH A O 1 HETATM 6312 O O . HOH T 9 . ? 12.254 27.609 21.448 1.00 45.53 ? 1172 HOH A O 1 HETATM 6313 O O . HOH T 9 . ? 29.202 28.135 25.071 1.00 56.13 ? 1173 HOH A O 1 HETATM 6314 O O . HOH T 9 . ? 38.777 55.145 62.156 1.00 55.10 ? 1174 HOH A O 1 HETATM 6315 O O . HOH T 9 . ? 12.957 71.704 79.904 1.00 52.17 ? 1175 HOH A O 1 HETATM 6316 O O . HOH T 9 . ? 11.590 81.108 60.926 1.00 48.68 ? 1176 HOH A O 1 HETATM 6317 O O . HOH T 9 . ? 1.520 36.950 68.588 1.00 45.81 ? 1177 HOH A O 1 HETATM 6318 O O . HOH T 9 . ? 4.662 70.985 80.731 1.00 57.87 ? 1178 HOH A O 1 HETATM 6319 O O . HOH T 9 . ? 13.006 32.944 70.804 1.00 46.50 ? 1179 HOH A O 1 HETATM 6320 O O . HOH T 9 . ? 14.731 73.159 23.497 1.00 61.03 ? 1180 HOH A O 1 HETATM 6321 O O . HOH T 9 . ? 18.997 40.630 75.970 1.00 47.42 ? 1181 HOH A O 1 HETATM 6322 O O . HOH T 9 . ? 20.036 45.728 78.934 1.00 56.43 ? 1182 HOH A O 1 HETATM 6323 O O . HOH T 9 . ? 5.900 56.266 35.681 1.00 38.25 ? 1183 HOH A O 1 HETATM 6324 O O . HOH T 9 . ? 23.441 60.276 39.757 1.00 55.08 ? 1184 HOH A O 1 HETATM 6325 O O . HOH T 9 . ? 30.624 71.540 43.402 1.00 46.90 ? 1185 HOH A O 1 HETATM 6326 O O . HOH T 9 . ? 8.651 74.739 75.384 1.00 48.60 ? 1186 HOH A O 1 HETATM 6327 O O . HOH T 9 . ? 3.095 38.421 26.935 1.00 47.49 ? 1187 HOH A O 1 HETATM 6328 O O . HOH T 9 . ? 17.491 61.928 69.503 1.00 59.66 ? 1188 HOH A O 1 HETATM 6329 O O . HOH T 9 . ? 26.961 31.072 63.711 1.00 59.27 ? 1189 HOH A O 1 HETATM 6330 O O . HOH T 9 . ? 25.114 85.920 42.313 1.00 49.14 ? 1190 HOH A O 1 HETATM 6331 O O . HOH T 9 . ? 21.986 80.672 22.685 1.00 53.22 ? 1191 HOH A O 1 HETATM 6332 O O . HOH T 9 . ? 40.947 45.102 19.963 1.00 55.57 ? 1192 HOH A O 1 HETATM 6333 O O . HOH T 9 . ? 28.194 53.601 37.103 1.00 38.96 ? 1193 HOH A O 1 HETATM 6334 O O . HOH T 9 . ? 24.935 22.973 53.216 1.00 56.70 ? 1194 HOH A O 1 HETATM 6335 O O . HOH T 9 . ? 25.323 66.494 56.709 1.00 45.36 ? 1195 HOH A O 1 HETATM 6336 O O . HOH T 9 . ? 15.401 25.753 29.725 1.00 50.41 ? 1196 HOH A O 1 HETATM 6337 O O . HOH T 9 . ? 31.266 61.366 23.302 1.00 55.54 ? 1197 HOH A O 1 HETATM 6338 O O . HOH T 9 . ? 35.815 50.208 35.706 1.00 66.28 ? 1198 HOH A O 1 HETATM 6339 O O . HOH T 9 . ? 7.671 57.788 33.588 1.00 48.17 ? 1199 HOH A O 1 HETATM 6340 O O . HOH T 9 . ? 6.657 42.866 27.171 1.00 45.05 ? 1200 HOH A O 1 HETATM 6341 O O . HOH T 9 . ? 35.138 43.928 68.243 1.00 52.24 ? 1201 HOH A O 1 HETATM 6342 O O . HOH T 9 . ? 12.185 29.197 18.989 1.00 51.84 ? 1202 HOH A O 1 HETATM 6343 O O . HOH T 9 . ? 27.166 28.399 28.275 1.00 57.41 ? 1203 HOH A O 1 HETATM 6344 O O . HOH T 9 . ? 15.795 54.850 72.221 1.00 56.16 ? 1204 HOH A O 1 HETATM 6345 O O . HOH T 9 . ? 6.213 95.443 42.087 1.00 54.03 ? 1205 HOH A O 1 HETATM 6346 O O . HOH T 9 . ? 9.462 74.842 69.376 1.00 57.52 ? 1206 HOH A O 1 HETATM 6347 O O . HOH T 9 . ? 10.368 83.952 50.979 1.00 44.69 ? 1207 HOH A O 1 HETATM 6348 O O . HOH T 9 . ? 30.106 75.797 43.088 1.00 55.34 ? 1208 HOH A O 1 HETATM 6349 O O . HOH T 9 . ? 0.898 64.117 38.393 1.00 52.61 ? 1209 HOH A O 1 HETATM 6350 O O . HOH T 9 . ? 25.274 65.056 44.450 1.00 48.70 ? 1210 HOH A O 1 HETATM 6351 O O . HOH T 9 . ? 25.240 56.716 32.306 1.00 49.42 ? 1211 HOH A O 1 HETATM 6352 O O . HOH T 9 . ? 32.448 84.412 32.277 1.00 60.79 ? 1212 HOH A O 1 HETATM 6353 O O . HOH T 9 . ? 39.469 57.489 57.741 1.00 50.52 ? 1213 HOH A O 1 HETATM 6354 O O . HOH T 9 . ? 9.135 54.276 30.949 1.00 48.08 ? 1214 HOH A O 1 HETATM 6355 O O . HOH T 9 . ? 6.159 44.889 25.345 1.00 52.88 ? 1215 HOH A O 1 HETATM 6356 O O . HOH T 9 . ? 5.230 63.700 76.712 1.00 48.74 ? 1216 HOH A O 1 HETATM 6357 O O . HOH T 9 . ? 17.288 25.690 59.513 1.00 38.98 ? 1217 HOH A O 1 HETATM 6358 O O . HOH T 9 . ? 0.111 29.707 44.775 1.00 58.19 ? 1218 HOH A O 1 HETATM 6359 O O . HOH T 9 . ? 2.623 63.320 40.414 1.00 40.97 ? 1219 HOH A O 1 HETATM 6360 O O . HOH T 9 . ? -4.008 43.953 27.141 1.00 58.16 ? 1220 HOH A O 1 HETATM 6361 O O . HOH T 9 . ? 21.444 24.116 26.534 1.00 49.30 ? 1221 HOH A O 1 HETATM 6362 O O . HOH T 9 . ? 14.418 61.772 32.991 1.00 57.81 ? 1222 HOH A O 1 HETATM 6363 O O . HOH T 9 . ? 29.397 72.829 49.805 1.00 51.17 ? 1223 HOH A O 1 HETATM 6364 O O . HOH T 9 . ? 22.210 83.564 49.693 1.00 47.47 ? 1224 HOH A O 1 HETATM 6365 O O . HOH T 9 . ? 24.260 81.986 24.220 1.00 61.55 ? 1225 HOH A O 1 HETATM 6366 O O . HOH T 9 . ? 29.574 30.466 14.727 1.00 66.52 ? 1226 HOH A O 1 HETATM 6367 O O . HOH T 9 . ? 23.996 83.545 45.574 1.00 51.52 ? 1227 HOH A O 1 HETATM 6368 O O . HOH T 9 . ? 24.813 68.151 62.913 1.00 62.23 ? 1228 HOH A O 1 HETATM 6369 O O . HOH T 9 . ? 30.747 71.983 47.561 1.00 53.15 ? 1229 HOH A O 1 HETATM 6370 O O . HOH T 9 . ? -5.281 44.500 30.825 1.00 47.28 ? 1230 HOH A O 1 HETATM 6371 O O . HOH T 9 . ? 27.001 64.709 35.247 1.00 55.35 ? 1231 HOH A O 1 HETATM 6372 O O . HOH T 9 . ? 17.750 64.790 66.944 1.00 49.68 ? 1232 HOH A O 1 HETATM 6373 O O . HOH T 9 . ? 27.414 63.212 63.112 1.00 57.49 ? 1233 HOH A O 1 HETATM 6374 O O . HOH T 9 . ? 19.325 25.020 12.302 1.00 59.00 ? 1234 HOH A O 1 HETATM 6375 O O . HOH T 9 . ? 33.996 53.145 32.075 1.00 51.58 ? 1235 HOH A O 1 HETATM 6376 O O . HOH T 9 . ? 1.370 59.983 43.498 1.00 36.17 ? 1236 HOH A O 1 HETATM 6377 O O . HOH T 9 . ? 3.042 64.960 50.764 1.00 36.86 ? 1237 HOH A O 1 HETATM 6378 O O . HOH T 9 . ? 15.292 24.848 32.337 1.00 48.12 ? 1238 HOH A O 1 HETATM 6379 O O . HOH T 9 . ? -1.846 63.565 48.674 1.00 39.62 ? 1239 HOH A O 1 HETATM 6380 O O . HOH T 9 . ? 29.085 25.782 31.385 1.00 48.54 ? 1240 HOH A O 1 HETATM 6381 O O . HOH T 9 . ? 26.693 64.833 28.830 1.00 55.86 ? 1241 HOH A O 1 HETATM 6382 O O . HOH T 9 . ? 25.434 68.047 32.530 1.00 46.07 ? 1242 HOH A O 1 HETATM 6383 O O . HOH T 9 . ? 29.683 67.630 45.449 1.00 53.23 ? 1243 HOH A O 1 HETATM 6384 O O . HOH T 9 . ? 29.546 61.774 27.030 1.00 62.15 ? 1244 HOH A O 1 HETATM 6385 O O . HOH T 9 . ? 27.436 66.127 46.191 1.00 48.51 ? 1245 HOH A O 1 HETATM 6386 O O . HOH T 9 . ? 17.838 22.116 48.635 1.00 49.56 ? 1246 HOH A O 1 HETATM 6387 O O . HOH T 9 . ? 34.769 35.567 58.340 1.00 53.47 ? 1247 HOH A O 1 HETATM 6388 O O . HOH T 9 . ? 24.479 79.453 55.145 1.00 48.43 ? 1248 HOH A O 1 HETATM 6389 O O . HOH T 9 . ? 21.537 56.562 25.215 1.00 47.76 ? 1249 HOH A O 1 HETATM 6390 O O . HOH T 9 . ? 28.252 35.970 67.552 1.00 50.87 ? 1250 HOH A O 1 HETATM 6391 O O . HOH T 9 . ? 29.641 37.806 66.257 1.00 50.91 ? 1251 HOH A O 1 HETATM 6392 O O . HOH T 9 . ? 13.797 80.465 62.860 1.00 49.88 ? 1252 HOH A O 1 HETATM 6393 O O . HOH T 9 . ? 11.874 73.507 81.387 1.00 58.91 ? 1253 HOH A O 1 HETATM 6394 O O . HOH T 9 . ? 35.308 49.154 33.208 1.00 53.26 ? 1254 HOH A O 1 HETATM 6395 O O . HOH T 9 . ? 37.969 41.494 36.871 1.00 50.59 ? 1255 HOH A O 1 HETATM 6396 O O . HOH T 9 . ? 31.125 51.734 49.820 1.00 54.33 ? 1256 HOH A O 1 HETATM 6397 O O . HOH T 9 . ? 14.927 69.989 81.771 1.00 56.77 ? 1257 HOH A O 1 HETATM 6398 O O . HOH T 9 . ? 5.096 50.031 28.047 1.00 44.96 ? 1258 HOH A O 1 HETATM 6399 O O . HOH T 9 . ? 25.697 71.916 60.656 1.00 59.65 ? 1259 HOH A O 1 HETATM 6400 O O . HOH T 9 . ? 23.661 74.536 65.372 1.00 49.28 ? 1260 HOH A O 1 HETATM 6401 O O . HOH T 9 . ? 41.857 39.357 20.488 0.50 52.94 ? 1261 HOH A O 1 HETATM 6402 O O . HOH T 9 . ? 16.369 84.646 40.634 1.00 52.44 ? 1262 HOH A O 1 HETATM 6403 O O . HOH T 9 . ? -5.433 34.026 47.446 1.00 44.70 ? 1263 HOH A O 1 HETATM 6404 O O . HOH T 9 . ? 12.701 50.314 27.299 1.00 43.96 ? 1264 HOH A O 1 HETATM 6405 O O . HOH T 9 . ? 7.745 26.379 54.676 1.00 52.55 ? 1265 HOH A O 1 HETATM 6406 O O . HOH T 9 . ? 18.622 57.928 29.804 1.00 55.77 ? 1266 HOH A O 1 HETATM 6407 O O . HOH T 9 . ? 20.916 79.359 65.654 1.00 56.89 ? 1267 HOH A O 1 HETATM 6408 O O . HOH T 9 . ? 1.219 31.845 67.369 1.00 51.09 ? 1268 HOH A O 1 HETATM 6409 O O . HOH T 9 . ? 15.914 82.556 57.523 1.00 59.48 ? 1269 HOH A O 1 HETATM 6410 O O . HOH T 9 . ? 37.279 56.660 63.825 1.00 54.40 ? 1270 HOH A O 1 HETATM 6411 O O . HOH T 9 . ? 12.597 28.447 60.584 1.00 56.98 ? 1271 HOH A O 1 HETATM 6412 O O . HOH T 9 . ? 11.266 41.361 17.353 1.00 55.31 ? 1272 HOH A O 1 HETATM 6413 O O . HOH T 9 . ? 24.010 58.235 37.063 1.00 52.74 ? 1273 HOH A O 1 HETATM 6414 O O . HOH T 9 . ? 21.524 72.998 68.687 1.00 63.39 ? 1274 HOH A O 1 HETATM 6415 O O . HOH T 9 . ? 32.780 27.529 56.322 1.00 54.44 ? 1275 HOH A O 1 HETATM 6416 O O . HOH T 9 . ? 25.881 74.562 58.318 1.00 51.55 ? 1276 HOH A O 1 HETATM 6417 O O . HOH T 9 . ? 30.074 42.041 66.424 1.00 54.02 ? 1277 HOH A O 1 HETATM 6418 O O . HOH T 9 . ? 28.799 64.340 25.695 1.00 53.06 ? 1278 HOH A O 1 HETATM 6419 O O . HOH T 9 . ? 40.126 56.786 60.131 1.00 57.47 ? 1279 HOH A O 1 HETATM 6420 O O . HOH T 9 . ? 7.312 81.534 62.504 1.00 57.23 ? 1280 HOH A O 1 HETATM 6421 O O . HOH T 9 . ? 28.698 56.665 34.155 1.00 57.04 ? 1281 HOH A O 1 HETATM 6422 O O . HOH T 9 . ? 26.405 74.889 55.397 1.00 55.13 ? 1282 HOH A O 1 HETATM 6423 O O . HOH T 9 . ? -9.370 45.771 48.383 1.00 47.37 ? 1283 HOH A O 1 HETATM 6424 O O . HOH T 9 . ? -3.653 46.635 24.745 1.00 51.84 ? 1284 HOH A O 1 HETATM 6425 O O . HOH T 9 . ? 40.599 45.620 16.918 1.00 58.22 ? 1285 HOH A O 1 HETATM 6426 O O . HOH T 9 . ? 24.452 81.421 50.385 1.00 59.47 ? 1286 HOH A O 1 HETATM 6427 O O . HOH T 9 . ? 14.147 54.745 37.415 1.00 46.10 ? 1287 HOH A O 1 HETATM 6428 O O . HOH T 9 . ? 22.603 55.029 69.766 1.00 66.00 ? 1288 HOH A O 1 HETATM 6429 O O . HOH T 9 . ? 33.640 26.847 35.898 1.00 50.79 ? 1289 HOH A O 1 HETATM 6430 O O . HOH T 9 . ? -10.342 43.516 38.374 1.00 50.99 ? 1290 HOH A O 1 HETATM 6431 O O . HOH T 9 . ? 14.037 72.095 25.680 1.00 61.44 ? 1291 HOH A O 1 HETATM 6432 O O . HOH T 9 . ? 1.636 66.421 37.019 1.00 56.61 ? 1292 HOH A O 1 HETATM 6433 O O . HOH T 9 . ? 31.860 73.911 44.002 1.00 63.71 ? 1293 HOH A O 1 HETATM 6434 O O . HOH T 9 . ? 34.314 54.974 67.950 1.00 62.19 ? 1294 HOH A O 1 HETATM 6435 O O . HOH T 9 . ? 28.564 41.988 68.681 1.00 53.18 ? 1295 HOH A O 1 HETATM 6436 O O . HOH T 9 . ? 16.904 20.715 51.885 1.00 53.25 ? 1296 HOH A O 1 HETATM 6437 O O . HOH T 9 . ? 4.228 78.893 68.446 1.00 56.38 ? 1297 HOH A O 1 HETATM 6438 O O . HOH T 9 . ? 32.628 41.765 67.256 1.00 57.61 ? 1298 HOH A O 1 HETATM 6439 O O . HOH T 9 . ? 25.211 42.908 71.643 1.00 63.17 ? 1299 HOH A O 1 HETATM 6440 O O . HOH T 9 . ? 14.078 68.604 75.279 1.00 48.74 ? 1300 HOH A O 1 HETATM 6441 O O . HOH T 9 . ? 32.016 74.461 36.406 1.00 48.38 ? 1301 HOH A O 1 HETATM 6442 O O . HOH T 9 . ? 31.176 61.444 63.892 1.00 52.26 ? 1302 HOH A O 1 HETATM 6443 O O . HOH T 9 . ? 10.059 47.199 80.145 1.00 64.86 ? 1303 HOH A O 1 HETATM 6444 O O . HOH T 9 . ? 30.469 25.870 38.298 1.00 55.67 ? 1304 HOH A O 1 HETATM 6445 O O . HOH T 9 . ? 18.379 23.832 35.995 1.00 46.86 ? 1305 HOH A O 1 HETATM 6446 O O . HOH T 9 . ? 36.196 39.621 64.927 1.00 66.63 ? 1306 HOH A O 1 HETATM 6447 O O . HOH T 9 . ? 35.653 33.824 54.729 1.00 56.95 ? 1307 HOH A O 1 HETATM 6448 O O . HOH T 9 . ? 17.451 66.210 70.261 1.00 61.91 ? 1308 HOH A O 1 HETATM 6449 O O . HOH T 9 . ? -7.051 39.918 37.676 1.00 59.24 ? 1309 HOH A O 1 HETATM 6450 O O . HOH T 9 . ? 12.196 25.200 35.169 1.00 61.89 ? 1310 HOH A O 1 HETATM 6451 O O . HOH T 9 . ? 38.986 38.960 64.612 1.00 59.42 ? 1311 HOH A O 1 HETATM 6452 O O . HOH T 9 . ? -3.466 32.570 42.460 1.00 58.92 ? 1312 HOH A O 1 HETATM 6453 O O . HOH T 9 . ? 5.927 53.446 30.002 1.00 44.77 ? 1313 HOH A O 1 HETATM 6454 O O . HOH T 9 . ? -0.027 60.468 48.263 1.00 46.35 ? 1314 HOH A O 1 HETATM 6455 O O . HOH T 9 . ? 9.859 75.843 30.778 1.00 48.01 ? 1315 HOH A O 1 HETATM 6456 O O . HOH T 9 . ? 8.090 56.416 75.569 1.00 38.02 ? 1316 HOH A O 1 HETATM 6457 O O . HOH T 9 . ? 6.809 53.807 75.376 1.00 41.82 ? 1317 HOH A O 1 HETATM 6458 O O . HOH T 9 . ? 11.404 52.267 28.139 1.00 54.75 ? 1318 HOH A O 1 HETATM 6459 O O . HOH T 9 . ? 29.788 60.890 52.441 1.00 49.35 ? 1319 HOH A O 1 HETATM 6460 O O . HOH T 9 . ? 2.993 34.336 70.620 1.00 62.31 ? 1320 HOH A O 1 HETATM 6461 O O . HOH T 9 . ? 36.392 31.482 33.994 1.00 56.86 ? 1321 HOH A O 1 HETATM 6462 O O . HOH T 9 . ? 36.725 46.624 31.598 1.00 53.76 ? 1322 HOH A O 1 HETATM 6463 O O . HOH T 9 . ? 13.031 23.236 15.378 1.00 74.22 ? 1323 HOH A O 1 HETATM 6464 O O . HOH T 9 . ? 20.067 80.687 62.883 1.00 57.30 ? 1324 HOH A O 1 HETATM 6465 O O . HOH T 9 . ? 3.596 18.757 61.133 1.00 66.66 ? 1325 HOH A O 1 HETATM 6466 O O . HOH T 9 . ? 8.929 93.519 54.280 1.00 56.05 ? 1326 HOH A O 1 HETATM 6467 O O . HOH T 9 . ? 6.652 93.513 53.243 1.00 54.43 ? 1327 HOH A O 1 HETATM 6468 O O . HOH T 9 . ? 3.917 64.038 34.510 1.00 55.27 ? 1328 HOH A O 1 HETATM 6469 O O . HOH T 9 . ? 39.792 42.293 14.327 1.00 63.46 ? 1329 HOH A O 1 HETATM 6470 O O . HOH T 9 . ? 26.036 56.786 34.700 1.00 58.53 ? 1330 HOH A O 1 HETATM 6471 O O . HOH T 9 . ? 15.194 71.722 21.678 1.00 57.38 ? 1331 HOH A O 1 HETATM 6472 O O . HOH T 9 . ? 0.138 63.699 61.448 1.00 49.18 ? 1332 HOH A O 1 HETATM 6473 O O . HOH T 9 . ? -7.463 41.551 40.830 1.00 45.03 ? 1333 HOH A O 1 HETATM 6474 O O . HOH T 9 . ? 23.105 78.374 22.688 1.00 58.89 ? 1334 HOH A O 1 HETATM 6475 O O . HOH T 9 . ? 18.545 68.144 74.677 1.00 53.00 ? 1335 HOH A O 1 HETATM 6476 O O . HOH T 9 . ? 35.162 55.946 51.082 1.00 58.56 ? 1336 HOH A O 1 HETATM 6477 O O . HOH T 9 . ? 30.970 41.521 40.397 1.00 41.51 ? 1337 HOH A O 1 HETATM 6478 O O . HOH T 9 . ? -5.445 50.593 28.451 1.00 55.57 ? 1338 HOH A O 1 HETATM 6479 O O . HOH T 9 . ? 2.711 52.757 26.719 1.00 66.06 ? 1339 HOH A O 1 HETATM 6480 O O . HOH T 9 . ? 8.678 50.560 25.100 1.00 55.07 ? 1340 HOH A O 1 HETATM 6481 O O . HOH T 9 . ? 26.145 53.032 48.498 1.00 49.03 ? 1341 HOH A O 1 HETATM 6482 O O . HOH T 9 . ? 26.005 59.102 46.405 1.00 50.30 ? 1342 HOH A O 1 HETATM 6483 O O . HOH T 9 . ? 13.881 68.054 34.608 1.00 30.39 ? 1343 HOH A O 1 HETATM 6484 O O . HOH T 9 . ? 12.843 69.509 32.542 1.00 39.71 ? 1344 HOH A O 1 HETATM 6485 O O . HOH T 9 . ? 16.218 72.055 29.510 1.00 31.42 ? 1345 HOH A O 1 HETATM 6486 O O . HOH T 9 . ? 23.018 75.664 25.363 1.00 45.11 ? 1346 HOH A O 1 HETATM 6487 O O . HOH T 9 . ? 16.908 42.373 44.460 1.00 25.97 ? 1347 HOH A O 1 HETATM 6488 O O . HOH T 9 . ? 19.529 49.203 44.918 1.00 41.59 ? 1348 HOH A O 1 HETATM 6489 O O . HOH T 9 . ? 21.751 42.084 46.325 1.00 46.56 ? 1349 HOH A O 1 HETATM 6490 O O . HOH T 9 . ? 11.947 49.936 36.449 1.00 32.37 ? 1350 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 ? 1.0884 0.8548 0.6115 0.2679 -0.0899 0.0346 55 LYS A N 2 C CA . LYS A 14 ? 1.0621 0.8411 0.6032 0.2581 -0.0872 0.0272 55 LYS A CA 3 C C . LYS A 14 ? 1.0165 0.8092 0.5925 0.2426 -0.0780 0.0287 55 LYS A C 4 O O . LYS A 14 ? 0.9998 0.7958 0.5932 0.2382 -0.0795 0.0308 55 LYS A O 5 C CB . LYS A 14 ? 1.0694 0.8535 0.6157 0.2603 -0.1059 0.0130 55 LYS A CB 6 C CG . LYS A 14 ? 1.1047 0.8915 0.6452 0.2598 -0.1046 0.0067 55 LYS A CG 7 C CD . LYS A 14 ? 1.1720 0.9435 0.6723 0.2749 -0.1060 0.0079 55 LYS A CD 8 C CE . LYS A 14 ? 1.1943 0.9666 0.6857 0.2741 -0.0968 0.0063 55 LYS A CE 9 N NZ . LYS A 14 ? 1.1938 0.9799 0.7124 0.2639 -0.1022 -0.0042 55 LYS A NZ 10 N N . HIS A 15 ? 0.9816 0.7819 0.5668 0.2348 -0.0688 0.0275 56 HIS A N 11 C CA . HIS A 15 ? 0.9301 0.7435 0.5469 0.2204 -0.0609 0.0277 56 HIS A CA 12 C C . HIS A 15 ? 0.8856 0.7109 0.5215 0.2139 -0.0704 0.0159 56 HIS A C 13 O O . HIS A 15 ? 0.8940 0.7220 0.5272 0.2123 -0.0670 0.0128 56 HIS A O 14 C CB . HIS A 15 ? 0.9363 0.7492 0.5509 0.2160 -0.0422 0.0364 56 HIS A CB 15 C CG . HIS A 15 ? 0.9717 0.7742 0.5738 0.2198 -0.0311 0.0489 56 HIS A CG 16 N ND1 . HIS A 15 ? 1.0106 0.8036 0.5900 0.2258 -0.0185 0.0573 56 HIS A ND1 17 C CD2 . HIS A 15 ? 0.9743 0.7740 0.5838 0.2187 -0.0304 0.0545 56 HIS A CD2 18 C CE1 . HIS A 15 ? 1.0473 0.8321 0.6211 0.2278 -0.0103 0.0680 56 HIS A CE1 19 N NE2 . HIS A 15 ? 1.0263 0.8146 0.6181 0.2237 -0.0175 0.0664 56 HIS A NE2 20 N N . ASN A 16 ? 0.8198 0.6518 0.4748 0.2108 -0.0823 0.0095 57 ASN A N 21 C CA . ASN A 16 ? 0.7564 0.5997 0.4321 0.2045 -0.0919 -0.0013 57 ASN A CA 22 C C . ASN A 16 ? 0.6970 0.5513 0.4034 0.1943 -0.0924 -0.0023 57 ASN A C 23 O O . ASN A 16 ? 0.6591 0.5119 0.3695 0.1920 -0.0845 0.0051 57 ASN A O 24 C CB . ASN A 16 ? 0.7718 0.6109 0.4366 0.2139 -0.1096 -0.0102 57 ASN A CB 25 C CG . ASN A 16 ? 0.7898 0.6212 0.4452 0.2227 -0.1182 -0.0083 57 ASN A CG 26 O OD1 . ASN A 16 ? 0.7395 0.5712 0.4034 0.2199 -0.1130 -0.0018 57 ASN A OD1 27 N ND2 . ASN A 16 ? 0.8091 0.6329 0.4459 0.2339 -0.1322 -0.0141 57 ASN A ND2 28 N N . MET A 17 ? 0.6545 0.5191 0.3821 0.1884 -0.1013 -0.0115 58 MET A N 29 C CA . MET A 17 ? 0.6264 0.5018 0.3827 0.1783 -0.0995 -0.0121 58 MET A CA 30 C C . MET A 17 ? 0.6202 0.4926 0.3788 0.1829 -0.1058 -0.0106 58 MET A C 31 O O . MET A 17 ? 0.6017 0.4775 0.3739 0.1773 -0.0991 -0.0062 58 MET A O 32 C CB A MET A 17 ? 0.6075 0.4950 0.3875 0.1702 -0.1055 -0.0209 58 MET A CB 33 C CB B MET A 17 ? 0.6085 0.4955 0.3873 0.1711 -0.1071 -0.0217 58 MET A CB 34 C CG A MET A 17 ? 0.5925 0.4904 0.3988 0.1588 -0.0981 -0.0191 58 MET A CG 35 C CG B MET A 17 ? 0.5992 0.4985 0.4069 0.1585 -0.1008 -0.0217 58 MET A CG 36 S SD A MET A 17 ? 0.5931 0.5043 0.4283 0.1509 -0.1069 -0.0289 58 MET A SD 37 S SD B MET A 17 ? 0.6076 0.5188 0.4369 0.1491 -0.1040 -0.0302 58 MET A SD 38 C CE A MET A 17 ? 0.6627 0.5686 0.4889 0.1620 -0.1252 -0.0366 58 MET A CE 39 C CE B MET A 17 ? 0.5728 0.4855 0.4098 0.1546 -0.1224 -0.0399 58 MET A CE 40 N N . LYS A 18 ? 0.6260 0.4915 0.3708 0.1934 -0.1187 -0.0142 59 LYS A N 41 C CA . LYS A 18 ? 0.6373 0.4990 0.3829 0.1989 -0.1253 -0.0126 59 LYS A CA 42 C C . LYS A 18 ? 0.6439 0.4968 0.3770 0.2010 -0.1134 -0.0010 59 LYS A C 43 O O . LYS A 18 ? 0.6348 0.4896 0.3811 0.1986 -0.1123 0.0015 59 LYS A O 44 C CB . LYS A 18 ? 0.6593 0.5134 0.3884 0.2113 -0.1418 -0.0183 59 LYS A CB 45 C CG . LYS A 18 ? 0.7002 0.5525 0.4354 0.2164 -0.1512 -0.0185 59 LYS A CG 46 C CD . LYS A 18 ? 0.8079 0.6580 0.5380 0.2258 -0.1709 -0.0281 59 LYS A CD 47 C CE . LYS A 18 ? 0.8583 0.7098 0.6017 0.2295 -0.1815 -0.0300 59 LYS A CE 48 N NZ . LYS A 18 ? 0.9140 0.7502 0.6295 0.2413 -0.1820 -0.0219 59 LYS A NZ 49 N N . ALA A 19 ? 0.6632 0.5064 0.3717 0.2055 -0.1044 0.0058 60 ALA A N 50 C CA . ALA A 19 ? 0.6688 0.5036 0.3672 0.2066 -0.0915 0.0175 60 ALA A CA 51 C C . ALA A 19 ? 0.6338 0.4780 0.3580 0.1938 -0.0801 0.0205 60 ALA A C 52 O O . ALA A 19 ? 0.6197 0.4613 0.3498 0.1930 -0.0762 0.0261 60 ALA A O 53 C CB . ALA A 19 ? 0.6977 0.5229 0.3698 0.2116 -0.0819 0.0239 60 ALA A CB 54 N N . PHE A 20 ? 0.6028 0.4573 0.3410 0.1844 -0.0753 0.0166 61 PHE A N 55 C CA . PHE A 20 ? 0.5833 0.4476 0.3460 0.1722 -0.0659 0.0179 61 PHE A CA 56 C C . PHE A 20 ? 0.5632 0.4342 0.3479 0.1688 -0.0725 0.0140 61 PHE A C 57 O O . PHE A 20 ? 0.5500 0.4210 0.3448 0.1651 -0.0661 0.0187 61 PHE A O 58 C CB . PHE A 20 ? 0.5523 0.4266 0.3260 0.1638 -0.0628 0.0130 61 PHE A CB 59 C CG . PHE A 20 ? 0.5430 0.4283 0.3428 0.1518 -0.0566 0.0121 61 PHE A CG 60 C CD1 . PHE A 20 ? 0.5189 0.4030 0.3223 0.1468 -0.0438 0.0195 61 PHE A CD1 61 C CD2 . PHE A 20 ? 0.5074 0.4034 0.3276 0.1462 -0.0638 0.0041 61 PHE A CD2 62 C CE1 . PHE A 20 ? 0.5241 0.4178 0.3507 0.1363 -0.0391 0.0181 61 PHE A CE1 63 C CE2 . PHE A 20 ? 0.5244 0.4299 0.3669 0.1359 -0.0581 0.0034 61 PHE A CE2 64 C CZ . PHE A 20 ? 0.4882 0.3923 0.3328 0.1313 -0.0462 0.0101 61 PHE A CZ 65 N N . LEU A 21 ? 0.5546 0.4314 0.3478 0.1699 -0.0852 0.0051 62 LEU A N 66 C CA . LEU A 21 ? 0.5497 0.4344 0.3656 0.1667 -0.0917 0.0003 62 LEU A CA 67 C C . LEU A 21 ? 0.5815 0.4584 0.3929 0.1737 -0.0950 0.0045 62 LEU A C 68 O O . LEU A 21 ? 0.5601 0.4416 0.3896 0.1692 -0.0928 0.0048 62 LEU A O 69 C CB . LEU A 21 ? 0.5525 0.4442 0.3777 0.1675 -0.1051 -0.0098 62 LEU A CB 70 C CG . LEU A 21 ? 0.5341 0.4355 0.3707 0.1590 -0.1027 -0.0149 62 LEU A CG 71 C CD1 . LEU A 21 ? 0.5484 0.4538 0.3913 0.1618 -0.1170 -0.0244 62 LEU A CD1 72 C CD2 . LEU A 21 ? 0.5202 0.4326 0.3813 0.1470 -0.0941 -0.0149 62 LEU A CD2 73 N N . ASP A 22 ? 0.6247 0.4894 0.4117 0.1850 -0.1002 0.0076 63 ASP A N 74 C CA . ASP A 22 ? 0.6606 0.5162 0.4404 0.1932 -0.1044 0.0121 63 ASP A CA 75 C C . ASP A 22 ? 0.6555 0.5053 0.4342 0.1903 -0.0908 0.0221 63 ASP A C 76 O O . ASP A 22 ? 0.6659 0.5108 0.4472 0.1937 -0.0923 0.0255 63 ASP A O 77 C CB . ASP A 22 ? 0.7043 0.5467 0.4546 0.2067 -0.1128 0.0138 63 ASP A CB 78 C CG . ASP A 22 ? 0.7533 0.5997 0.5059 0.2117 -0.1300 0.0032 63 ASP A CG 79 O OD1 . ASP A 22 ? 0.7760 0.6352 0.5551 0.2052 -0.1358 -0.0048 63 ASP A OD1 80 O OD2 . ASP A 22 ? 0.8352 0.6717 0.5628 0.2225 -0.1377 0.0029 63 ASP A OD2 81 N N . GLU A 23 ? 0.6397 0.4899 0.4154 0.1841 -0.0777 0.0268 64 GLU A N 82 C CA . GLU A 23 ? 0.6341 0.4783 0.4090 0.1814 -0.0647 0.0363 64 GLU A CA 83 C C . GLU A 23 ? 0.5983 0.4526 0.4016 0.1712 -0.0608 0.0339 64 GLU A C 84 O O . GLU A 23 ? 0.6044 0.4536 0.4115 0.1702 -0.0543 0.0400 64 GLU A O 85 C CB . GLU A 23 ? 0.6465 0.4879 0.4093 0.1787 -0.0523 0.0419 64 GLU A CB 86 C CG . GLU A 23 ? 0.6714 0.5068 0.4348 0.1751 -0.0376 0.0521 64 GLU A CG 87 C CD . GLU A 23 ? 0.7515 0.5722 0.4999 0.1839 -0.0368 0.0609 64 GLU A CD 88 O OE1 . GLU A 23 ? 0.7789 0.5898 0.5039 0.1949 -0.0429 0.0629 64 GLU A OE1 89 O OE2 . GLU A 23 ? 0.7483 0.5667 0.5079 0.1802 -0.0302 0.0660 64 GLU A OE2 90 N N . LEU A 24 ? 0.5532 0.4210 0.3756 0.1639 -0.0645 0.0251 65 LEU A N 91 C CA . LEU A 24 ? 0.5245 0.4024 0.3733 0.1550 -0.0620 0.0216 65 LEU A CA 92 C C . LEU A 24 ? 0.5374 0.4130 0.3943 0.1594 -0.0684 0.0210 65 LEU A C 93 O O . LEU A 24 ? 0.5300 0.4047 0.3837 0.1665 -0.0802 0.0170 65 LEU A O 94 C CB . LEU A 24 ? 0.4993 0.3913 0.3649 0.1479 -0.0660 0.0124 65 LEU A CB 95 C CG . LEU A 24 ? 0.4914 0.3869 0.3520 0.1430 -0.0607 0.0118 65 LEU A CG 96 C CD1 . LEU A 24 ? 0.4841 0.3910 0.3582 0.1389 -0.0680 0.0026 65 LEU A CD1 97 C CD2 . LEU A 24 ? 0.4760 0.3739 0.3445 0.1342 -0.0475 0.0161 65 LEU A CD2 98 N N . LYS A 25 ? 0.5283 0.4036 0.3975 0.1551 -0.0615 0.0241 66 LYS A N 99 C CA . LYS A 25 ? 0.5396 0.4123 0.4172 0.1595 -0.0670 0.0236 66 LYS A CA 100 C C . LYS A 25 ? 0.5170 0.4005 0.4209 0.1509 -0.0639 0.0186 66 LYS A C 101 O O . LYS A 25 ? 0.4763 0.3620 0.3871 0.1430 -0.0535 0.0206 66 LYS A O 102 C CB . LYS A 25 ? 0.5711 0.4286 0.4340 0.1653 -0.0619 0.0339 66 LYS A CB 103 C CG . LYS A 25 ? 0.6263 0.4712 0.4604 0.1752 -0.0643 0.0400 66 LYS A CG 104 C CD . LYS A 25 ? 0.7205 0.5636 0.5482 0.1851 -0.0794 0.0355 66 LYS A CD 105 C CE . LYS A 25 ? 0.7850 0.6134 0.5814 0.1967 -0.0824 0.0420 66 LYS A CE 106 N NZ . LYS A 25 ? 0.7687 0.5970 0.5509 0.1945 -0.0759 0.0436 66 LYS A NZ 107 N N . ALA A 26 ? 0.5063 0.3962 0.4247 0.1529 -0.0728 0.0120 67 ALA A N 108 C CA . ALA A 26 ? 0.4894 0.3887 0.4318 0.1464 -0.0701 0.0071 67 ALA A CA 109 C C . ALA A 26 ? 0.5019 0.3937 0.4464 0.1448 -0.0614 0.0130 67 ALA A C 110 O O . ALA A 26 ? 0.4840 0.3819 0.4427 0.1367 -0.0539 0.0110 67 ALA A O 111 C CB . ALA A 26 ? 0.4976 0.4025 0.4536 0.1513 -0.0816 0.0004 67 ALA A CB 112 N N A GLU A 27 ? 0.5216 0.3998 0.4523 0.1527 -0.0625 0.0201 68 GLU A N 113 N N B GLU A 27 ? 0.5167 0.3948 0.4468 0.1529 -0.0627 0.0202 68 GLU A N 114 C CA A GLU A 27 ? 0.5367 0.4071 0.4713 0.1518 -0.0553 0.0256 68 GLU A CA 115 C CA B GLU A 27 ? 0.5266 0.3955 0.4585 0.1529 -0.0558 0.0263 68 GLU A CA 116 C C A GLU A 27 ? 0.5201 0.3886 0.4516 0.1441 -0.0429 0.0303 68 GLU A C 117 C C B GLU A 27 ? 0.5167 0.3836 0.4463 0.1451 -0.0432 0.0311 68 GLU A C 118 O O A GLU A 27 ? 0.5082 0.3764 0.4516 0.1388 -0.0360 0.0309 68 GLU A O 119 O O B GLU A 27 ? 0.5103 0.3758 0.4509 0.1406 -0.0365 0.0324 68 GLU A O 120 C CB A GLU A 27 ? 0.5701 0.4255 0.4902 0.1624 -0.0594 0.0328 68 GLU A CB 121 C CB B GLU A 27 ? 0.5545 0.4083 0.4696 0.1641 -0.0605 0.0337 68 GLU A CB 122 C CG A GLU A 27 ? 0.6232 0.4686 0.5467 0.1617 -0.0517 0.0393 68 GLU A CG 123 C CG B GLU A 27 ? 0.5763 0.4193 0.4649 0.1689 -0.0582 0.0417 68 GLU A CG 124 C CD A GLU A 27 ? 0.6865 0.5383 0.6336 0.1587 -0.0528 0.0331 68 GLU A CD 125 C CD B GLU A 27 ? 0.6336 0.4654 0.5035 0.1818 -0.0681 0.0453 68 GLU A CD 126 O OE1 A GLU A 27 ? 0.6920 0.5471 0.6463 0.1642 -0.0624 0.0282 68 GLU A OE1 127 O OE1 B GLU A 27 ? 0.6812 0.5060 0.5540 0.1875 -0.0720 0.0475 68 GLU A OE1 128 O OE2 A GLU A 27 ? 0.7150 0.5686 0.6736 0.1511 -0.0440 0.0328 68 GLU A OE2 129 O OE2 B GLU A 27 ? 0.6237 0.4531 0.4753 0.1866 -0.0723 0.0459 68 GLU A OE2 130 N N . ASN A 28 ? 0.5136 0.3808 0.4301 0.1437 -0.0403 0.0333 69 ASN A N 131 C CA . ASN A 28 ? 0.5050 0.3720 0.4208 0.1361 -0.0289 0.0370 69 ASN A CA 132 C C . ASN A 28 ? 0.4787 0.3592 0.4130 0.1260 -0.0258 0.0297 69 ASN A C 133 O O . ASN A 28 ? 0.4706 0.3513 0.4130 0.1194 -0.0175 0.0311 69 ASN A O 134 C CB . ASN A 28 ? 0.5160 0.3797 0.4125 0.1381 -0.0268 0.0412 69 ASN A CB 135 C CG . ASN A 28 ? 0.5596 0.4080 0.4356 0.1470 -0.0257 0.0507 69 ASN A CG 136 O OD1 . ASN A 28 ? 0.5749 0.4141 0.4519 0.1493 -0.0227 0.0563 69 ASN A OD1 137 N ND2 . ASN A 28 ? 0.5633 0.4084 0.4198 0.1525 -0.0284 0.0526 69 ASN A ND2 138 N N . ILE A 29 ? 0.4634 0.3549 0.4043 0.1248 -0.0324 0.0219 70 ILE A N 139 C CA . ILE A 29 ? 0.4383 0.3426 0.3958 0.1156 -0.0296 0.0150 70 ILE A CA 140 C C . ILE A 29 ? 0.4381 0.3437 0.4120 0.1130 -0.0273 0.0125 70 ILE A C 141 O O . ILE A 29 ? 0.4244 0.3341 0.4077 0.1057 -0.0206 0.0107 70 ILE A O 142 C CB . ILE A 29 ? 0.4357 0.3508 0.3985 0.1156 -0.0375 0.0075 70 ILE A CB 143 C CG1 . ILE A 29 ? 0.4283 0.3421 0.3751 0.1175 -0.0394 0.0092 70 ILE A CG1 144 C CG2 . ILE A 29 ? 0.4190 0.3465 0.3986 0.1067 -0.0342 0.0009 70 ILE A CG2 145 C CD1 . ILE A 29 ? 0.4400 0.3615 0.3901 0.1196 -0.0493 0.0024 70 ILE A CD1 146 N N . LYS A 30 ? 0.4300 0.3313 0.4066 0.1197 -0.0330 0.0124 71 LYS A N 147 C CA . LYS A 30 ? 0.4352 0.3368 0.4272 0.1186 -0.0315 0.0097 71 LYS A CA 148 C C . LYS A 30 ? 0.4475 0.3401 0.4380 0.1156 -0.0227 0.0156 71 LYS A C 149 O O . LYS A 30 ? 0.4449 0.3413 0.4483 0.1095 -0.0177 0.0121 71 LYS A O 150 C CB . LYS A 30 ? 0.4519 0.3487 0.4448 0.1278 -0.0399 0.0097 71 LYS A CB 151 C CG . LYS A 30 ? 0.4759 0.3719 0.4840 0.1281 -0.0390 0.0072 71 LYS A CG 152 C CD . LYS A 30 ? 0.5000 0.3934 0.5108 0.1373 -0.0487 0.0060 71 LYS A CD 153 C CE . LYS A 30 ? 0.5513 0.4422 0.5762 0.1382 -0.0472 0.0042 71 LYS A CE 154 N NZ . LYS A 30 ? 0.5667 0.4536 0.5938 0.1480 -0.0569 0.0039 71 LYS A NZ 155 N N . LYS A 31 ? 0.4578 0.3381 0.4329 0.1201 -0.0207 0.0244 72 LYS A N 156 C CA A LYS A 31 ? 0.4772 0.3480 0.4509 0.1173 -0.0119 0.0311 72 LYS A CA 157 C CA B LYS A 31 ? 0.4698 0.3411 0.4450 0.1171 -0.0120 0.0305 72 LYS A CA 158 C C . LYS A 31 ? 0.4506 0.3287 0.4309 0.1074 -0.0046 0.0287 72 LYS A C 159 O O . LYS A 31 ? 0.4363 0.3134 0.4274 0.1022 0.0008 0.0279 72 LYS A O 160 C CB A LYS A 31 ? 0.5013 0.3596 0.4552 0.1234 -0.0102 0.0412 72 LYS A CB 161 C CB B LYS A 31 ? 0.4911 0.3482 0.4483 0.1235 -0.0101 0.0410 72 LYS A CB 162 C CG A LYS A 31 ? 0.5518 0.3997 0.5041 0.1208 -0.0005 0.0493 72 LYS A CG 163 C CG B LYS A 31 ? 0.5229 0.3706 0.4757 0.1329 -0.0165 0.0440 72 LYS A CG 164 C CD A LYS A 31 ? 0.6189 0.4568 0.5504 0.1257 0.0029 0.0591 72 LYS A CD 165 C CD B LYS A 31 ? 0.5470 0.3818 0.4780 0.1406 -0.0163 0.0538 72 LYS A CD 166 C CE A LYS A 31 ? 0.6621 0.4903 0.5786 0.1369 -0.0040 0.0634 72 LYS A CE 167 C CE B LYS A 31 ? 0.6099 0.4344 0.5372 0.1501 -0.0228 0.0570 72 LYS A CE 168 N NZ A LYS A 31 ? 0.7166 0.5326 0.6119 0.1421 0.0010 0.0742 72 LYS A NZ 169 N NZ B LYS A 31 ? 0.6484 0.4637 0.5524 0.1596 -0.0271 0.0633 72 LYS A NZ 170 N N . PHE A 32 ? 0.4301 0.3152 0.4037 0.1052 -0.0050 0.0272 73 PHE A N 171 C CA . PHE A 32 ? 0.4165 0.3081 0.3949 0.0966 0.0010 0.0254 73 PHE A CA 172 C C . PHE A 32 ? 0.4054 0.3076 0.4003 0.0903 0.0008 0.0165 73 PHE A C 173 O O . PHE A 32 ? 0.3812 0.2849 0.3839 0.0838 0.0064 0.0152 73 PHE A O 174 C CB . PHE A 32 ? 0.4059 0.3022 0.3727 0.0963 0.0001 0.0258 73 PHE A CB 175 C CG . PHE A 32 ? 0.4277 0.3138 0.3767 0.1022 0.0018 0.0343 73 PHE A CG 176 C CD1 . PHE A 32 ? 0.4537 0.3280 0.3989 0.1039 0.0080 0.0425 73 PHE A CD1 177 C CD2 . PHE A 32 ? 0.4382 0.3262 0.3740 0.1059 -0.0023 0.0342 73 PHE A CD2 178 C CE1 . PHE A 32 ? 0.5161 0.3806 0.4436 0.1097 0.0106 0.0509 73 PHE A CE1 179 C CE2 . PHE A 32 ? 0.4418 0.3200 0.3593 0.1119 -0.0004 0.0418 73 PHE A CE2 180 C CZ . PHE A 32 ? 0.4951 0.3617 0.4079 0.1139 0.0065 0.0505 73 PHE A CZ 181 N N . LEU A 33 ? 0.3841 0.2936 0.3843 0.0925 -0.0055 0.0104 74 LEU A N 182 C CA . LEU A 33 ? 0.3917 0.3111 0.4066 0.0872 -0.0050 0.0023 74 LEU A CA 183 C C . LEU A 33 ? 0.3840 0.2983 0.4086 0.0861 -0.0016 0.0017 74 LEU A C 184 O O . LEU A 33 ? 0.3858 0.3042 0.4185 0.0799 0.0025 -0.0023 74 LEU A O 185 C CB . LEU A 33 ? 0.3779 0.3054 0.3990 0.0903 -0.0119 -0.0035 74 LEU A CB 186 C CG . LEU A 33 ? 0.3664 0.3043 0.4018 0.0850 -0.0101 -0.0114 74 LEU A CG 187 C CD1 . LEU A 33 ? 0.3326 0.2780 0.3665 0.0778 -0.0065 -0.0134 74 LEU A CD1 188 C CD2 . LEU A 33 ? 0.4101 0.3552 0.4531 0.0888 -0.0166 -0.0164 74 LEU A CD2 189 N N . TYR A 34 ? 0.3956 0.3005 0.4193 0.0924 -0.0037 0.0053 75 TYR A N 190 C CA . TYR A 34 ? 0.4134 0.3119 0.4466 0.0919 -0.0007 0.0050 75 TYR A CA 191 C C . TYR A 34 ? 0.4172 0.3108 0.4500 0.0860 0.0065 0.0086 75 TYR A C 192 O O . TYR A 34 ? 0.4117 0.3066 0.4549 0.0811 0.0097 0.0042 75 TYR A O 193 C CB . TYR A 34 ? 0.4329 0.3201 0.4628 0.1003 -0.0042 0.0102 75 TYR A CB 194 C CG . TYR A 34 ? 0.4380 0.3176 0.4781 0.0999 -0.0012 0.0100 75 TYR A CG 195 C CD1 . TYR A 34 ? 0.4447 0.3291 0.4984 0.1004 -0.0034 0.0023 75 TYR A CD1 196 C CD2 . TYR A 34 ? 0.4904 0.3585 0.5278 0.0986 0.0043 0.0171 75 TYR A CD2 197 C CE1 . TYR A 34 ? 0.4755 0.3528 0.5391 0.1003 -0.0011 0.0013 75 TYR A CE1 198 C CE2 . TYR A 34 ? 0.5282 0.3888 0.5769 0.0979 0.0068 0.0163 75 TYR A CE2 199 C CZ . TYR A 34 ? 0.5227 0.3880 0.5839 0.0990 0.0036 0.0081 75 TYR A CZ 200 O OH . TYR A 34 ? 0.5772 0.4354 0.6496 0.0987 0.0054 0.0062 75 TYR A OH 201 N N . ASN A 35 ? 0.4160 0.3038 0.4369 0.0868 0.0090 0.0163 76 ASN A N 202 C CA . ASN A 35 ? 0.4219 0.3053 0.4438 0.0815 0.0161 0.0203 76 ASN A CA 203 C C . ASN A 35 ? 0.4063 0.3000 0.4348 0.0732 0.0185 0.0141 76 ASN A C 204 O O . ASN A 35 ? 0.4055 0.2969 0.4417 0.0681 0.0231 0.0138 76 ASN A O 205 C CB . ASN A 35 ? 0.4444 0.3218 0.4516 0.0842 0.0185 0.0293 76 ASN A CB 206 C CG . ASN A 35 ? 0.4658 0.3383 0.4751 0.0793 0.0263 0.0343 76 ASN A CG 207 O OD1 . ASN A 35 ? 0.4415 0.3205 0.4508 0.0740 0.0291 0.0331 76 ASN A OD1 208 N ND2 . ASN A 35 ? 0.5007 0.3618 0.5132 0.0808 0.0298 0.0399 76 ASN A ND2 209 N N . PHE A 36 ? 0.3691 0.2735 0.3952 0.0722 0.0152 0.0091 77 PHE A N 210 C CA . PHE A 36 ? 0.3581 0.2720 0.3879 0.0651 0.0171 0.0040 77 PHE A CA 211 C C . PHE A 36 ? 0.3674 0.2879 0.4087 0.0618 0.0163 -0.0047 77 PHE A C 212 O O . PHE A 36 ? 0.3522 0.2799 0.3957 0.0562 0.0177 -0.0091 77 PHE A O 213 C CB . PHE A 36 ? 0.3374 0.2595 0.3590 0.0652 0.0143 0.0032 77 PHE A CB 214 C CG . PHE A 36 ? 0.3748 0.2924 0.3839 0.0673 0.0157 0.0106 77 PHE A CG 215 C CD1 . PHE A 36 ? 0.4041 0.3120 0.4102 0.0680 0.0207 0.0179 77 PHE A CD1 216 C CD2 . PHE A 36 ? 0.3764 0.2997 0.3770 0.0687 0.0124 0.0100 77 PHE A CD2 217 C CE1 . PHE A 36 ? 0.3981 0.3019 0.3913 0.0707 0.0228 0.0249 77 PHE A CE1 218 C CE2 . PHE A 36 ? 0.3828 0.3021 0.3709 0.0712 0.0136 0.0161 77 PHE A CE2 219 C CZ . PHE A 36 ? 0.3974 0.3072 0.3813 0.0723 0.0192 0.0235 77 PHE A CZ 220 N N . THR A 37 ? 0.3535 0.2714 0.4012 0.0655 0.0142 -0.0074 78 THR A N 221 C CA . THR A 37 ? 0.3564 0.2817 0.4133 0.0635 0.0135 -0.0161 78 THR A CA 222 C C . THR A 37 ? 0.3687 0.2877 0.4353 0.0639 0.0149 -0.0190 78 THR A C 223 O O . THR A 37 ? 0.3583 0.2818 0.4322 0.0643 0.0140 -0.0260 78 THR A O 224 C CB . THR A 37 ? 0.3396 0.2714 0.3976 0.0680 0.0089 -0.0192 78 THR A CB 225 O OG1 . THR A 37 ? 0.3571 0.2810 0.4136 0.0749 0.0057 -0.0148 78 THR A OG1 226 C CG2 . THR A 37 ? 0.3280 0.2679 0.3784 0.0666 0.0071 -0.0185 78 THR A CG2 227 N N . GLN A 38 ? 0.3803 0.2888 0.4475 0.0638 0.0173 -0.0137 79 GLN A N 228 C CA . GLN A 38 ? 0.4163 0.3174 0.4935 0.0647 0.0180 -0.0164 79 GLN A CA 229 C C . GLN A 38 ? 0.4202 0.3236 0.5046 0.0585 0.0205 -0.0229 79 GLN A C 230 O O . GLN A 38 ? 0.4255 0.3254 0.5186 0.0588 0.0205 -0.0280 79 GLN A O 231 C CB . GLN A 38 ? 0.4385 0.3261 0.5148 0.0675 0.0197 -0.0076 79 GLN A CB 232 C CG . GLN A 38 ? 0.4808 0.3642 0.5490 0.0750 0.0164 -0.0015 79 GLN A CG 233 C CD . GLN A 38 ? 0.5412 0.4299 0.6145 0.0795 0.0117 -0.0079 79 GLN A CD 234 O OE1 . GLN A 38 ? 0.5902 0.4747 0.6731 0.0811 0.0114 -0.0115 79 GLN A OE1 235 N NE2 . GLN A 38 ? 0.5029 0.4016 0.5717 0.0810 0.0082 -0.0102 79 GLN A NE2 236 N N . ILE A 39 ? 0.4119 0.3204 0.4923 0.0532 0.0222 -0.0227 80 ILE A N 237 C CA . ILE A 39 ? 0.4168 0.3275 0.5027 0.0474 0.0235 -0.0290 80 ILE A CA 238 C C . ILE A 39 ? 0.3837 0.3055 0.4631 0.0438 0.0233 -0.0317 80 ILE A C 239 O O . ILE A 39 ? 0.3909 0.3166 0.4624 0.0448 0.0228 -0.0271 80 ILE A O 240 C CB . ILE A 39 ? 0.4354 0.3376 0.5260 0.0439 0.0262 -0.0245 80 ILE A CB 241 C CG1 . ILE A 39 ? 0.4488 0.3524 0.5319 0.0423 0.0282 -0.0169 80 ILE A CG1 242 C CG2 . ILE A 39 ? 0.4693 0.3591 0.5674 0.0471 0.0270 -0.0213 80 ILE A CG2 243 C CD1 . ILE A 39 ? 0.5005 0.3979 0.5900 0.0381 0.0315 -0.0129 80 ILE A CD1 244 N N . PRO A 40 ? 0.3756 0.3016 0.4575 0.0397 0.0234 -0.0390 81 PRO A N 245 C CA . PRO A 40 ? 0.3582 0.2941 0.4332 0.0367 0.0231 -0.0410 81 PRO A CA 246 C C . PRO A 40 ? 0.3475 0.2831 0.4186 0.0334 0.0241 -0.0351 81 PRO A C 247 O O . PRO A 40 ? 0.3613 0.2902 0.4376 0.0315 0.0254 -0.0322 81 PRO A O 248 C CB . PRO A 40 ? 0.3673 0.3060 0.4450 0.0339 0.0229 -0.0500 81 PRO A CB 249 C CG . PRO A 40 ? 0.3941 0.3264 0.4799 0.0371 0.0227 -0.0539 81 PRO A CG 250 C CD . PRO A 40 ? 0.3888 0.3116 0.4788 0.0387 0.0232 -0.0465 81 PRO A CD 251 N N . HIS A 41 ? 0.3301 0.2731 0.3936 0.0324 0.0236 -0.0337 82 HIS A N 252 C CA . HIS A 41 ? 0.3405 0.2842 0.4004 0.0295 0.0246 -0.0286 82 HIS A CA 253 C C . HIS A 41 ? 0.3231 0.2750 0.3789 0.0255 0.0237 -0.0327 82 HIS A C 254 O O . HIS A 41 ? 0.3167 0.2735 0.3660 0.0252 0.0233 -0.0300 82 HIS A O 255 C CB . HIS A 41 ? 0.3434 0.2861 0.3963 0.0331 0.0248 -0.0212 82 HIS A CB 256 C CG . HIS A 41 ? 0.3667 0.3000 0.4217 0.0370 0.0259 -0.0159 82 HIS A CG 257 N ND1 . HIS A 41 ? 0.3649 0.2962 0.4187 0.0424 0.0240 -0.0154 82 HIS A ND1 258 C CD2 . HIS A 41 ? 0.3365 0.2615 0.3957 0.0364 0.0288 -0.0109 82 HIS A CD2 259 C CE1 . HIS A 41 ? 0.3783 0.2998 0.4338 0.0452 0.0255 -0.0100 82 HIS A CE1 260 N NE2 . HIS A 41 ? 0.3547 0.2721 0.4137 0.0416 0.0288 -0.0070 82 HIS A NE2 261 N N . LEU A 42 ? 0.3213 0.2744 0.3804 0.0231 0.0229 -0.0397 83 LEU A N 262 C CA . LEU A 42 ? 0.3167 0.2766 0.3709 0.0199 0.0218 -0.0438 83 LEU A CA 263 C C . LEU A 42 ? 0.3086 0.2694 0.3619 0.0165 0.0216 -0.0403 83 LEU A C 264 O O . LEU A 42 ? 0.3180 0.2737 0.3780 0.0150 0.0223 -0.0380 83 LEU A O 265 C CB . LEU A 42 ? 0.3184 0.2777 0.3754 0.0188 0.0208 -0.0523 83 LEU A CB 266 C CG . LEU A 42 ? 0.3354 0.3009 0.3855 0.0163 0.0196 -0.0571 83 LEU A CG 267 C CD1 . LEU A 42 ? 0.2853 0.2577 0.3282 0.0179 0.0208 -0.0572 83 LEU A CD1 268 C CD2 . LEU A 42 ? 0.2915 0.2539 0.3444 0.0160 0.0183 -0.0661 83 LEU A CD2 269 N N . ALA A 43 ? 0.2929 0.2602 0.3389 0.0152 0.0208 -0.0397 84 ALA A N 270 C CA . ALA A 43 ? 0.3021 0.2707 0.3477 0.0123 0.0205 -0.0366 84 ALA A CA 271 C C . ALA A 43 ? 0.3228 0.2892 0.3754 0.0090 0.0191 -0.0403 84 ALA A C 272 O O . ALA A 43 ? 0.3232 0.2899 0.3758 0.0082 0.0171 -0.0472 84 ALA A O 273 C CB . ALA A 43 ? 0.2987 0.2743 0.3360 0.0112 0.0192 -0.0368 84 ALA A CB 274 N N . GLY A 44 ? 0.3262 0.2902 0.3849 0.0073 0.0200 -0.0361 85 GLY A N 275 C CA . GLY A 44 ? 0.3484 0.3108 0.4162 0.0038 0.0181 -0.0396 85 GLY A CA 276 C C . GLY A 44 ? 0.3688 0.3241 0.4474 0.0037 0.0187 -0.0415 85 GLY A C 277 O O . GLY A 44 ? 0.3975 0.3508 0.4859 0.0007 0.0169 -0.0443 85 GLY A O 278 N N . THR A 45 ? 0.3587 0.3097 0.4367 0.0069 0.0208 -0.0398 86 THR A N 279 C CA . THR A 45 ? 0.3587 0.3021 0.4472 0.0071 0.0215 -0.0412 86 THR A CA 280 C C . THR A 45 ? 0.3586 0.2959 0.4542 0.0075 0.0257 -0.0327 86 THR A C 281 O O . THR A 45 ? 0.3450 0.2835 0.4343 0.0092 0.0284 -0.0256 86 THR A O 282 C CB . THR A 45 ? 0.3623 0.3032 0.4477 0.0109 0.0213 -0.0448 86 THR A CB 283 O OG1 . THR A 45 ? 0.3636 0.3045 0.4429 0.0147 0.0237 -0.0385 86 THR A OG1 284 C CG2 . THR A 45 ? 0.3705 0.3170 0.4487 0.0109 0.0185 -0.0529 86 THR A CG2 285 N N . GLU A 46 ? 0.3629 0.2929 0.4710 0.0062 0.0263 -0.0334 87 GLU A N 286 C CA . GLU A 46 ? 0.3987 0.3216 0.5138 0.0067 0.0312 -0.0248 87 GLU A CA 287 C C . GLU A 46 ? 0.3860 0.3052 0.4920 0.0120 0.0343 -0.0179 87 GLU A C 288 O O . GLU A 46 ? 0.3901 0.3069 0.4936 0.0134 0.0385 -0.0092 87 GLU A O 289 C CB . GLU A 46 ? 0.4264 0.3412 0.5577 0.0044 0.0312 -0.0272 87 GLU A CB 290 C CG . GLU A 46 ? 0.5359 0.4425 0.6751 0.0048 0.0373 -0.0174 87 GLU A CG 291 C CD . GLU A 46 ? 0.6564 0.5657 0.8009 0.0017 0.0411 -0.0112 87 GLU A CD 292 O OE1 . GLU A 46 ? 0.7105 0.6139 0.8580 0.0027 0.0474 -0.0018 87 GLU A OE1 293 O OE2 . GLU A 46 ? 0.6869 0.6040 0.8326 -0.0014 0.0382 -0.0155 87 GLU A OE2 294 N N A GLN A 47 ? 0.3846 0.3033 0.4857 0.0153 0.0320 -0.0221 88 GLN A N 295 N N B GLN A 47 ? 0.3819 0.3006 0.4831 0.0153 0.0320 -0.0221 88 GLN A N 296 C CA A GLN A 47 ? 0.3963 0.3123 0.4892 0.0208 0.0333 -0.0170 88 GLN A CA 297 C CA B GLN A 47 ? 0.3821 0.2978 0.4754 0.0208 0.0333 -0.0169 88 GLN A CA 298 C C A GLN A 47 ? 0.3711 0.2926 0.4518 0.0226 0.0341 -0.0119 88 GLN A C 299 C C B GLN A 47 ? 0.3703 0.2919 0.4509 0.0228 0.0339 -0.0123 88 GLN A C 300 O O A GLN A 47 ? 0.3534 0.2710 0.4283 0.0263 0.0364 -0.0045 88 GLN A O 301 O O B GLN A 47 ? 0.3654 0.2832 0.4397 0.0269 0.0357 -0.0054 88 GLN A O 302 C CB A GLN A 47 ? 0.3954 0.3128 0.4861 0.0237 0.0301 -0.0239 88 GLN A CB 303 C CB B GLN A 47 ? 0.3806 0.2960 0.4732 0.0238 0.0304 -0.0234 88 GLN A CB 304 C CG A GLN A 47 ? 0.4563 0.3669 0.5581 0.0232 0.0292 -0.0292 88 GLN A CG 305 C CG B GLN A 47 ? 0.3849 0.2913 0.4892 0.0239 0.0304 -0.0262 88 GLN A CG 306 C CD A GLN A 47 ? 0.4983 0.4129 0.6042 0.0193 0.0261 -0.0390 88 GLN A CD 307 C CD B GLN A 47 ? 0.3601 0.2677 0.4645 0.0264 0.0274 -0.0347 88 GLN A CD 308 O OE1 A GLN A 47 ? 0.4332 0.3526 0.5392 0.0152 0.0253 -0.0402 88 GLN A OE1 309 O OE1 B GLN A 47 ? 0.3933 0.2933 0.5047 0.0286 0.0273 -0.0361 88 GLN A OE1 310 N NE2 A GLN A 47 ? 0.5515 0.4639 0.6606 0.0209 0.0241 -0.0464 88 GLN A NE2 311 N NE2 B GLN A 47 ? 0.2966 0.2134 0.3936 0.0261 0.0254 -0.0403 88 GLN A NE2 312 N N . ASN A 48 ? 0.3603 0.2906 0.4365 0.0201 0.0318 -0.0160 89 ASN A N 313 C CA . ASN A 48 ? 0.3613 0.2970 0.4265 0.0218 0.0319 -0.0123 89 ASN A CA 314 C C . ASN A 48 ? 0.3775 0.3115 0.4431 0.0206 0.0357 -0.0050 89 ASN A C 315 O O . ASN A 48 ? 0.3566 0.2904 0.4133 0.0237 0.0373 0.0007 89 ASN A O 316 C CB . ASN A 48 ? 0.3596 0.3045 0.4200 0.0197 0.0287 -0.0184 89 ASN A CB 317 C CG . ASN A 48 ? 0.4308 0.3806 0.4800 0.0222 0.0281 -0.0154 89 ASN A CG 318 O OD1 . ASN A 48 ? 0.4417 0.3885 0.4861 0.0267 0.0285 -0.0110 89 ASN A OD1 319 N ND2 . ASN A 48 ? 0.3951 0.3520 0.4405 0.0197 0.0265 -0.0179 89 ASN A ND2 320 N N . PHE A 49 ? 0.3633 0.2962 0.4396 0.0162 0.0371 -0.0058 90 PHE A N 321 C CA . PHE A 49 ? 0.3717 0.3025 0.4517 0.0150 0.0419 0.0012 90 PHE A CA 322 C C . PHE A 49 ? 0.3821 0.3035 0.4613 0.0188 0.0467 0.0095 90 PHE A C 323 O O . PHE A 49 ? 0.3661 0.2863 0.4381 0.0213 0.0506 0.0167 90 PHE A O 324 C CB . PHE A 49 ? 0.3793 0.3112 0.4740 0.0094 0.0418 -0.0018 90 PHE A CB 325 C CG . PHE A 49 ? 0.3902 0.3197 0.4927 0.0078 0.0476 0.0053 90 PHE A CG 326 C CD1 . PHE A 49 ? 0.4008 0.3346 0.4964 0.0087 0.0503 0.0101 90 PHE A CD1 327 C CD2 . PHE A 49 ? 0.4860 0.4088 0.6038 0.0054 0.0508 0.0072 90 PHE A CD2 328 C CE1 . PHE A 49 ? 0.4227 0.3548 0.5265 0.0073 0.0566 0.0166 90 PHE A CE1 329 C CE2 . PHE A 49 ? 0.5253 0.4462 0.6525 0.0036 0.0572 0.0143 90 PHE A CE2 330 C CZ . PHE A 49 ? 0.4793 0.4051 0.5991 0.0047 0.0604 0.0191 90 PHE A CZ 331 N N A GLN A 50 ? 0.3781 0.2924 0.4636 0.0198 0.0466 0.0086 91 GLN A N 332 N N B GLN A 50 ? 0.3770 0.2914 0.4624 0.0198 0.0464 0.0084 91 GLN A N 333 C CA A GLN A 50 ? 0.4023 0.3068 0.4854 0.0241 0.0508 0.0169 91 GLN A CA 334 C CA B GLN A 50 ? 0.3953 0.2997 0.4789 0.0240 0.0504 0.0163 91 GLN A CA 335 C C A GLN A 50 ? 0.3975 0.3021 0.4639 0.0303 0.0499 0.0207 91 GLN A C 336 C C B GLN A 50 ? 0.3933 0.2972 0.4603 0.0304 0.0498 0.0205 91 GLN A C 337 O O A GLN A 50 ? 0.3887 0.2880 0.4481 0.0337 0.0542 0.0292 91 GLN A O 338 O O B GLN A 50 ? 0.3920 0.2897 0.4528 0.0339 0.0541 0.0291 91 GLN A O 339 C CB A GLN A 50 ? 0.4173 0.3137 0.5098 0.0245 0.0501 0.0148 91 GLN A CB 340 C CB B GLN A 50 ? 0.4025 0.2997 0.4956 0.0242 0.0490 0.0131 91 GLN A CB 341 C CG A GLN A 50 ? 0.4724 0.3661 0.5829 0.0187 0.0516 0.0126 91 GLN A CG 342 C CG B GLN A 50 ? 0.4336 0.3272 0.5443 0.0188 0.0511 0.0119 91 GLN A CG 343 C CD A GLN A 50 ? 0.5488 0.4389 0.6659 0.0167 0.0586 0.0212 91 GLN A CD 344 C CD B GLN A 50 ? 0.4511 0.3393 0.5719 0.0182 0.0481 0.0056 91 GLN A CD 345 O OE1 A GLN A 50 ? 0.6032 0.4874 0.7129 0.0206 0.0638 0.0307 91 GLN A OE1 346 O OE1 B GLN A 50 ? 0.4793 0.3680 0.5942 0.0216 0.0443 0.0011 91 GLN A OE1 347 N NE2 A GLN A 50 ? 0.5566 0.4501 0.6880 0.0108 0.0588 0.0179 91 GLN A NE2 348 N NE2 B GLN A 50 ? 0.4893 0.3726 0.6264 0.0140 0.0497 0.0049 91 GLN A NE2 349 N N . LEU A 51 ? 0.3740 0.2846 0.4341 0.0318 0.0444 0.0145 92 LEU A N 350 C CA . LEU A 51 ? 0.3805 0.2918 0.4262 0.0376 0.0425 0.0174 92 LEU A CA 351 C C . LEU A 51 ? 0.3679 0.2830 0.4048 0.0378 0.0447 0.0216 92 LEU A C 352 O O . LEU A 51 ? 0.3695 0.2804 0.3950 0.0429 0.0461 0.0279 92 LEU A O 353 C CB . LEU A 51 ? 0.3491 0.2675 0.3918 0.0386 0.0366 0.0097 92 LEU A CB 354 C CG . LEU A 51 ? 0.3828 0.3019 0.4138 0.0445 0.0335 0.0115 92 LEU A CG 355 C CD1 . LEU A 51 ? 0.3897 0.2983 0.4173 0.0505 0.0344 0.0177 92 LEU A CD1 356 C CD2 . LEU A 51 ? 0.3505 0.2773 0.3827 0.0444 0.0284 0.0035 92 LEU A CD2 357 N N . ALA A 52 ? 0.3544 0.2768 0.3956 0.0327 0.0446 0.0181 93 ALA A N 358 C CA . ALA A 52 ? 0.3611 0.2872 0.3953 0.0327 0.0469 0.0219 93 ALA A CA 359 C C . ALA A 52 ? 0.3728 0.2911 0.4060 0.0348 0.0538 0.0310 93 ALA A C 360 O O . ALA A 52 ? 0.3705 0.2875 0.3919 0.0389 0.0558 0.0361 93 ALA A O 361 C CB . ALA A 52 ? 0.3409 0.2751 0.3822 0.0269 0.0461 0.0172 93 ALA A CB 362 N N . LYS A 53 ? 0.3756 0.2885 0.4213 0.0320 0.0577 0.0330 94 LYS A N 363 C CA A LYS A 53 ? 0.3884 0.2936 0.4350 0.0335 0.0655 0.0424 94 LYS A CA 364 C CA B LYS A 53 ? 0.3898 0.2950 0.4362 0.0335 0.0655 0.0424 94 LYS A CA 365 C C . LYS A 53 ? 0.4065 0.3025 0.4395 0.0409 0.0668 0.0491 94 LYS A C 366 O O . LYS A 53 ? 0.4074 0.2986 0.4310 0.0447 0.0725 0.0572 94 LYS A O 367 C CB A LYS A 53 ? 0.3898 0.2907 0.4550 0.0286 0.0688 0.0425 94 LYS A CB 368 C CB B LYS A 53 ? 0.3940 0.2954 0.4592 0.0285 0.0690 0.0426 94 LYS A CB 369 C CG A LYS A 53 ? 0.4136 0.3226 0.4922 0.0219 0.0686 0.0379 94 LYS A CG 370 C CG B LYS A 53 ? 0.4210 0.3306 0.4992 0.0219 0.0689 0.0381 94 LYS A CG 371 C CD A LYS A 53 ? 0.4370 0.3492 0.5117 0.0222 0.0740 0.0433 94 LYS A CD 372 C CD B LYS A 53 ? 0.4738 0.3786 0.5712 0.0174 0.0738 0.0405 94 LYS A CD 373 C CE A LYS A 53 ? 0.4630 0.3675 0.5441 0.0226 0.0836 0.0530 94 LYS A CE 374 C CE B LYS A 53 ? 0.4945 0.3963 0.6027 0.0149 0.0691 0.0339 94 LYS A CE 375 N NZ A LYS A 53 ? 0.4724 0.3824 0.5573 0.0208 0.0890 0.0561 94 LYS A NZ 376 N NZ B LYS A 53 ? 0.5171 0.4111 0.6432 0.0117 0.0741 0.0375 94 LYS A NZ 377 N N . GLN A 54 ? 0.3991 0.2924 0.4310 0.0433 0.0617 0.0456 95 GLN A N 378 C CA . GLN A 54 ? 0.4204 0.3052 0.4393 0.0509 0.0611 0.0510 95 GLN A CA 379 C C . GLN A 54 ? 0.4140 0.3022 0.4155 0.0558 0.0585 0.0519 95 GLN A C 380 O O . GLN A 54 ? 0.4294 0.3107 0.4180 0.0616 0.0615 0.0594 95 GLN A O 381 C CB . GLN A 54 ? 0.4166 0.3002 0.4392 0.0524 0.0549 0.0455 95 GLN A CB 382 C CG . GLN A 54 ? 0.4596 0.3352 0.4689 0.0606 0.0530 0.0504 95 GLN A CG 383 C CD . GLN A 54 ? 0.4659 0.3430 0.4783 0.0626 0.0459 0.0438 95 GLN A CD 384 O OE1 . GLN A 54 ? 0.4393 0.3173 0.4653 0.0586 0.0450 0.0385 95 GLN A OE1 385 N NE2 . GLN A 54 ? 0.4742 0.3518 0.4746 0.0688 0.0406 0.0435 95 GLN A NE2 386 N N . ILE A 55 ? 0.3772 0.2759 0.3781 0.0537 0.0529 0.0444 96 ILE A N 387 C CA . ILE A 55 ? 0.4018 0.3037 0.3877 0.0581 0.0496 0.0443 96 ILE A CA 388 C C . ILE A 55 ? 0.4049 0.3059 0.3836 0.0589 0.0558 0.0503 96 ILE A C 389 O O . ILE A 55 ? 0.4094 0.3061 0.3723 0.0653 0.0562 0.0549 96 ILE A O 390 C CB . ILE A 55 ? 0.3895 0.3028 0.3779 0.0547 0.0432 0.0352 96 ILE A CB 391 C CG1 A ILE A 55 ? 0.4112 0.3269 0.4062 0.0543 0.0375 0.0287 96 ILE A CG1 392 C CG1 B ILE A 55 ? 0.3774 0.2916 0.3699 0.0559 0.0373 0.0298 96 ILE A CG1 393 C CG2 . ILE A 55 ? 0.4071 0.3238 0.3816 0.0586 0.0401 0.0352 96 ILE A CG2 394 C CD1 A ILE A 55 ? 0.4520 0.3627 0.4393 0.0611 0.0336 0.0301 96 ILE A CD1 395 C CD1 B ILE A 55 ? 0.3082 0.2326 0.3070 0.0516 0.0327 0.0212 96 ILE A CD1 396 N N . GLN A 56 ? 0.3904 0.2953 0.3804 0.0528 0.0603 0.0500 97 GLN A N 397 C CA . GLN A 56 ? 0.4045 0.3084 0.3898 0.0535 0.0673 0.0560 97 GLN A CA 398 C C . GLN A 56 ? 0.4239 0.3162 0.4005 0.0592 0.0741 0.0660 97 GLN A C 399 O O . GLN A 56 ? 0.4399 0.3292 0.4010 0.0647 0.0768 0.0708 97 GLN A O 400 C CB . GLN A 56 ? 0.3953 0.3047 0.3976 0.0461 0.0713 0.0545 97 GLN A CB 401 C CG . GLN A 56 ? 0.4392 0.3473 0.4406 0.0465 0.0801 0.0614 97 GLN A CG 402 C CD . GLN A 56 ? 0.4705 0.3838 0.4921 0.0389 0.0837 0.0598 97 GLN A CD 403 O OE1 . GLN A 56 ? 0.4698 0.3827 0.5062 0.0343 0.0822 0.0567 97 GLN A OE1 404 N NE2 . GLN A 56 ? 0.4518 0.3698 0.4743 0.0381 0.0880 0.0615 97 GLN A NE2 405 N N . SER A 57 ? 0.4250 0.3099 0.4106 0.0582 0.0771 0.0694 98 SER A N 406 C CA . SER A 57 ? 0.4644 0.3369 0.4413 0.0637 0.0839 0.0797 98 SER A CA 407 C C . SER A 57 ? 0.4671 0.3337 0.4220 0.0729 0.0795 0.0821 98 SER A C 408 O O . SER A 57 ? 0.4658 0.3255 0.4054 0.0790 0.0847 0.0898 98 SER A O 409 C CB . SER A 57 ? 0.4724 0.3376 0.4633 0.0612 0.0860 0.0818 98 SER A CB 410 O OG A SER A 57 ? 0.5122 0.3648 0.4955 0.0662 0.0933 0.0925 98 SER A OG 411 O OG B SER A 57 ? 0.4953 0.3632 0.5053 0.0538 0.0918 0.0820 98 SER A OG 412 N N . GLN A 58 ? 0.4599 0.3291 0.4138 0.0743 0.0700 0.0754 99 GLN A N 413 C CA . GLN A 58 ? 0.4738 0.3383 0.4095 0.0829 0.0641 0.0764 99 GLN A CA 414 C C . GLN A 58 ? 0.4794 0.3481 0.3996 0.0866 0.0619 0.0751 99 GLN A C 415 O O . GLN A 58 ? 0.4968 0.3582 0.3984 0.0947 0.0616 0.0800 99 GLN A O 416 C CB . GLN A 58 ? 0.4648 0.3328 0.4063 0.0828 0.0545 0.0686 99 GLN A CB 417 C CG . GLN A 58 ? 0.5167 0.3774 0.4697 0.0816 0.0564 0.0708 99 GLN A CG 418 C CD . GLN A 58 ? 0.5447 0.4075 0.5019 0.0833 0.0476 0.0641 99 GLN A CD 419 O OE1 . GLN A 58 ? 0.5046 0.3774 0.4706 0.0789 0.0429 0.0555 99 GLN A OE1 420 N NE2 . GLN A 58 ? 0.5924 0.4452 0.5433 0.0898 0.0457 0.0685 99 GLN A NE2 421 N N . TRP A 59 ? 0.4422 0.3223 0.3691 0.0813 0.0596 0.0683 100 TRP A N 422 C CA . TRP A 59 ? 0.4503 0.3340 0.3634 0.0847 0.0577 0.0671 100 TRP A CA 423 C C . TRP A 59 ? 0.4583 0.3356 0.3600 0.0883 0.0672 0.0757 100 TRP A C 424 O O . TRP A 59 ? 0.4829 0.3572 0.3660 0.0953 0.0659 0.0773 100 TRP A O 425 C CB . TRP A 59 ? 0.4159 0.3122 0.3393 0.0779 0.0545 0.0590 100 TRP A CB 426 C CG . TRP A 59 ? 0.3899 0.2925 0.3179 0.0766 0.0448 0.0507 100 TRP A CG 427 C CD1 . TRP A 59 ? 0.4014 0.3007 0.3288 0.0799 0.0391 0.0491 100 TRP A CD1 428 C CD2 . TRP A 59 ? 0.3729 0.2865 0.3088 0.0712 0.0402 0.0429 100 TRP A CD2 429 N NE1 . TRP A 59 ? 0.4044 0.3124 0.3392 0.0769 0.0318 0.0408 100 TRP A NE1 430 C CE2 . TRP A 59 ? 0.3717 0.2882 0.3111 0.0716 0.0325 0.0371 100 TRP A CE2 431 C CE3 . TRP A 59 ? 0.3793 0.3002 0.3196 0.0664 0.0421 0.0405 100 TRP A CE3 432 C CZ2 . TRP A 59 ? 0.3423 0.2686 0.2893 0.0671 0.0273 0.0294 100 TRP A CZ2 433 C CZ3 . TRP A 59 ? 0.3536 0.2839 0.3008 0.0620 0.0362 0.0328 100 TRP A CZ3 434 C CH2 . TRP A 59 ? 0.3680 0.3008 0.3180 0.0624 0.0293 0.0276 100 TRP A CH2 435 N N . LYS A 60 ? 0.4752 0.3505 0.3884 0.0839 0.0768 0.0809 101 LYS A N 436 C CA . LYS A 60 ? 0.5255 0.3938 0.4295 0.0875 0.0876 0.0905 101 LYS A CA 437 C C . LYS A 60 ? 0.5524 0.4074 0.4375 0.0967 0.0888 0.0981 101 LYS A C 438 O O . LYS A 60 ? 0.5751 0.4251 0.4404 0.1039 0.0914 0.1024 101 LYS A O 439 C CB . LYS A 60 ? 0.5302 0.3985 0.4535 0.0806 0.0975 0.0948 101 LYS A CB 440 C CG . LYS A 60 ? 0.5774 0.4578 0.5165 0.0728 0.0975 0.0886 101 LYS A CG 441 C CD . LYS A 60 ? 0.6958 0.5769 0.6571 0.0656 0.1056 0.0917 101 LYS A CD 442 C CE . LYS A 60 ? 0.7185 0.6106 0.6910 0.0601 0.1076 0.0877 101 LYS A CE 443 N NZ . LYS A 60 ? 0.7628 0.6589 0.7606 0.0515 0.1099 0.0859 101 LYS A NZ 444 N N A GLU A 61 ? 0.5505 0.3992 0.4406 0.0971 0.0866 0.0997 102 GLU A N 445 N N B GLU A 61 ? 0.5511 0.4002 0.4420 0.0967 0.0866 0.0995 102 GLU A N 446 C CA A GLU A 61 ? 0.5743 0.4094 0.4464 0.1061 0.0873 0.1075 102 GLU A CA 447 C CA B GLU A 61 ? 0.5789 0.4147 0.4535 0.1053 0.0866 0.1067 102 GLU A CA 448 C C A GLU A 61 ? 0.5763 0.4107 0.4283 0.1144 0.0766 0.1033 102 GLU A C 449 C C B GLU A 61 ? 0.5799 0.4149 0.4325 0.1139 0.0772 0.1033 102 GLU A C 450 O O A GLU A 61 ? 0.5905 0.4144 0.4212 0.1236 0.0775 0.1097 102 GLU A O 451 O O B GLU A 61 ? 0.5881 0.4133 0.4186 0.1228 0.0797 0.1100 102 GLU A O 452 C CB A GLU A 61 ? 0.5797 0.4079 0.4635 0.1045 0.0875 0.1102 102 GLU A CB 453 C CB B GLU A 61 ? 0.5809 0.4127 0.4680 0.1034 0.0828 0.1059 102 GLU A CB 454 C CG A GLU A 61 ? 0.6222 0.4379 0.4887 0.1141 0.0835 0.1153 102 GLU A CG 455 C CG B GLU A 61 ? 0.6217 0.4513 0.5301 0.0960 0.0914 0.1098 102 GLU A CG 456 C CD A GLU A 61 ? 0.6911 0.4938 0.5370 0.1219 0.0925 0.1273 102 GLU A CD 457 C CD B GLU A 61 ? 0.6768 0.5057 0.6007 0.0927 0.0855 0.1052 102 GLU A CD 458 O OE1 A GLU A 61 ? 0.7255 0.5265 0.5760 0.1188 0.1047 0.1341 102 GLU A OE1 459 O OE1 B GLU A 61 ? 0.6775 0.5028 0.5931 0.0983 0.0772 0.1031 102 GLU A OE1 460 O OE2 A GLU A 61 ? 0.7264 0.5203 0.5513 0.1316 0.0875 0.1302 102 GLU A OE2 461 O OE2 B GLU A 61 ? 0.6771 0.5093 0.6223 0.0846 0.0888 0.1031 102 GLU A OE2 462 N N . PHE A 62 ? 0.5438 0.3891 0.4023 0.1113 0.0667 0.0928 103 PHE A N 463 C CA . PHE A 62 ? 0.5532 0.3993 0.3951 0.1184 0.0562 0.0878 103 PHE A CA 464 C C . PHE A 62 ? 0.5562 0.4017 0.3800 0.1232 0.0588 0.0894 103 PHE A C 465 O O . PHE A 62 ? 0.5788 0.4211 0.3843 0.1312 0.0515 0.0875 103 PHE A O 466 C CB . PHE A 62 ? 0.5198 0.3785 0.3750 0.1132 0.0459 0.0763 103 PHE A CB 467 C CG . PHE A 62 ? 0.5124 0.3719 0.3817 0.1107 0.0406 0.0729 103 PHE A CG 468 C CD1 . PHE A 62 ? 0.5605 0.4089 0.4269 0.1151 0.0420 0.0792 103 PHE A CD1 469 C CD2 . PHE A 62 ? 0.5121 0.3831 0.3972 0.1043 0.0345 0.0635 103 PHE A CD2 470 C CE1 . PHE A 62 ? 0.5731 0.4224 0.4534 0.1130 0.0371 0.0755 103 PHE A CE1 471 C CE2 . PHE A 62 ? 0.5084 0.3803 0.4065 0.1024 0.0302 0.0600 103 PHE A CE2 472 C CZ . PHE A 62 ? 0.5451 0.4065 0.4413 0.1067 0.0313 0.0656 103 PHE A CZ 473 N N . GLY A 63 ? 0.5362 0.3854 0.3662 0.1183 0.0684 0.0918 104 GLY A N 474 C CA . GLY A 63 ? 0.5633 0.4108 0.3764 0.1233 0.0731 0.0944 104 GLY A CA 475 C C . GLY A 63 ? 0.5520 0.4113 0.3730 0.1180 0.0727 0.0878 104 GLY A C 476 O O . GLY A 63 ? 0.5725 0.4307 0.3788 0.1227 0.0755 0.0888 104 GLY A O 477 N N . LEU A 64 ? 0.5278 0.3978 0.3707 0.1087 0.0696 0.0812 105 LEU A N 478 C CA . LEU A 64 ? 0.5091 0.3899 0.3594 0.1037 0.0693 0.0754 105 LEU A CA 479 C C . LEU A 64 ? 0.5252 0.4057 0.3776 0.1023 0.0820 0.0815 105 LEU A C 480 O O . LEU A 64 ? 0.5497 0.4245 0.4067 0.1014 0.0914 0.0893 105 LEU A O 481 C CB . LEU A 64 ? 0.4812 0.3727 0.3531 0.0944 0.0637 0.0677 105 LEU A CB 482 C CG . LEU A 64 ? 0.4455 0.3389 0.3170 0.0955 0.0519 0.0610 105 LEU A CG 483 C CD1 . LEU A 64 ? 0.4389 0.3436 0.3297 0.0866 0.0475 0.0533 105 LEU A CD1 484 C CD2 . LEU A 64 ? 0.4635 0.3555 0.3166 0.1030 0.0443 0.0577 105 LEU A CD2 485 N N . ASP A 65 ? 0.5206 0.4068 0.3700 0.1023 0.0824 0.0783 106 ASP A N 486 C CA . ASP A 65 ? 0.5400 0.4269 0.3914 0.1017 0.0941 0.0834 106 ASP A CA 487 C C . ASP A 65 ? 0.5358 0.4299 0.4133 0.0917 0.0995 0.0836 106 ASP A C 488 O O . ASP A 65 ? 0.5412 0.4330 0.4252 0.0905 0.1108 0.0905 106 ASP A O 489 C CB . ASP A 65 ? 0.5394 0.4311 0.3816 0.1045 0.0919 0.0786 106 ASP A CB 490 C CG . ASP A 65 ? 0.6023 0.4856 0.4174 0.1152 0.0881 0.0791 106 ASP A CG 491 O OD1 . ASP A 65 ? 0.5642 0.4376 0.3650 0.1217 0.0959 0.0873 106 ASP A OD1 492 O OD2 . ASP A 65 ? 0.5604 0.4464 0.3685 0.1174 0.0774 0.0716 106 ASP A OD2 493 N N . SER A 66 ? 0.4901 0.3926 0.3826 0.0848 0.0914 0.0759 107 SER A N 494 C CA . SER A 66 ? 0.4766 0.3862 0.3933 0.0756 0.0945 0.0746 107 SER A CA 495 C C . SER A 66 ? 0.4575 0.3710 0.3841 0.0707 0.0849 0.0678 107 SER A C 496 O O . SER A 66 ? 0.4301 0.3455 0.3484 0.0728 0.0757 0.0622 107 SER A O 497 C CB . SER A 66 ? 0.4767 0.3953 0.4009 0.0724 0.0964 0.0713 107 SER A CB 498 O OG A SER A 66 ? 0.4394 0.3649 0.3621 0.0711 0.0862 0.0629 107 SER A OG 499 O OG B SER A 66 ? 0.5026 0.4299 0.4479 0.0637 0.0933 0.0662 107 SER A OG 500 N N . VAL A 67 ? 0.4267 0.3409 0.3708 0.0646 0.0871 0.0684 108 VAL A N 501 C CA . VAL A 67 ? 0.4281 0.3461 0.3816 0.0602 0.0787 0.0617 108 VAL A CA 502 C C . VAL A 67 ? 0.4239 0.3474 0.3995 0.0518 0.0816 0.0600 108 VAL A C 503 O O . VAL A 67 ? 0.4161 0.3350 0.4013 0.0501 0.0887 0.0653 108 VAL A O 504 C CB . VAL A 67 ? 0.4118 0.3217 0.3615 0.0631 0.0766 0.0639 108 VAL A CB 505 C CG1 . VAL A 67 ? 0.4033 0.3190 0.3626 0.0586 0.0674 0.0554 108 VAL A CG1 506 C CG2 . VAL A 67 ? 0.4496 0.3519 0.3768 0.0725 0.0747 0.0673 108 VAL A CG2 507 N N . GLU A 68 ? 0.4209 0.3536 0.4045 0.0469 0.0757 0.0526 109 GLU A N 508 C CA . GLU A 68 ? 0.4379 0.3763 0.4413 0.0395 0.0770 0.0500 109 GLU A CA 509 C C . GLU A 68 ? 0.4110 0.3539 0.4222 0.0349 0.0688 0.0422 109 GLU A C 510 O O . GLU A 68 ? 0.4044 0.3489 0.4062 0.0369 0.0622 0.0381 109 GLU A O 511 C CB . GLU A 68 ? 0.4536 0.3994 0.4598 0.0380 0.0783 0.0486 109 GLU A CB 512 C CG . GLU A 68 ? 0.5578 0.5002 0.5587 0.0422 0.0881 0.0562 109 GLU A CG 513 C CD . GLU A 68 ? 0.6933 0.6311 0.7070 0.0403 0.0976 0.0630 109 GLU A CD 514 O OE1 . GLU A 68 ? 0.7200 0.6606 0.7528 0.0339 0.0972 0.0607 109 GLU A OE1 515 O OE2 . GLU A 68 ? 0.7878 0.7185 0.7922 0.0454 0.1058 0.0708 109 GLU A OE2 516 N N . LEU A 69 ? 0.3857 0.3307 0.4140 0.0290 0.0693 0.0399 110 LEU A N 517 C CA . LEU A 69 ? 0.3895 0.3398 0.4243 0.0246 0.0616 0.0318 110 LEU A CA 518 C C . LEU A 69 ? 0.3890 0.3480 0.4290 0.0210 0.0590 0.0275 110 LEU A C 519 O O . LEU A 69 ? 0.4037 0.3647 0.4530 0.0191 0.0635 0.0300 110 LEU A O 520 C CB . LEU A 69 ? 0.3967 0.3440 0.4461 0.0207 0.0623 0.0305 110 LEU A CB 521 C CG . LEU A 69 ? 0.4414 0.3795 0.4887 0.0237 0.0649 0.0347 110 LEU A CG 522 C CD1 . LEU A 69 ? 0.4788 0.4154 0.5425 0.0188 0.0638 0.0311 110 LEU A CD1 523 C CD2 . LEU A 69 ? 0.4250 0.3616 0.4584 0.0281 0.0598 0.0327 110 LEU A CD2 524 N N . ALA A 70 ? 0.3590 0.3230 0.3929 0.0206 0.0523 0.0219 111 ALA A N 525 C CA . ALA A 70 ? 0.3444 0.3158 0.3831 0.0171 0.0490 0.0178 111 ALA A CA 526 C C . ALA A 70 ? 0.3472 0.3210 0.3933 0.0128 0.0436 0.0113 111 ALA A C 527 O O . ALA A 70 ? 0.3602 0.3335 0.3995 0.0137 0.0397 0.0081 111 ALA A O 528 C CB . ALA A 70 ? 0.3480 0.3225 0.3735 0.0199 0.0453 0.0164 111 ALA A CB 529 N N . HIS A 71 ? 0.3177 0.2939 0.3776 0.0085 0.0434 0.0091 112 HIS A N 530 C CA . HIS A 71 ? 0.3175 0.2950 0.3834 0.0049 0.0380 0.0024 112 HIS A CA 531 C C . HIS A 71 ? 0.2991 0.2832 0.3656 0.0023 0.0325 -0.0025 112 HIS A C 532 O O . HIS A 71 ? 0.2894 0.2771 0.3577 0.0022 0.0334 -0.0007 112 HIS A O 533 C CB . HIS A 71 ? 0.3129 0.2867 0.3943 0.0021 0.0403 0.0024 112 HIS A CB 534 C CG . HIS A 71 ? 0.3647 0.3414 0.4601 -0.0006 0.0428 0.0040 112 HIS A CG 535 N ND1 . HIS A 71 ? 0.4242 0.3988 0.5236 0.0008 0.0504 0.0112 112 HIS A ND1 536 C CD2 . HIS A 71 ? 0.4096 0.3913 0.5159 -0.0043 0.0386 -0.0005 112 HIS A CD2 537 C CE1 . HIS A 71 ? 0.4494 0.4281 0.5635 -0.0022 0.0514 0.0109 112 HIS A CE1 538 N NE2 . HIS A 71 ? 0.4286 0.4118 0.5474 -0.0054 0.0437 0.0036 112 HIS A NE2 539 N N . TYR A 72 ? 0.2932 0.2785 0.3572 0.0007 0.0271 -0.0086 113 TYR A N 540 C CA . TYR A 72 ? 0.2815 0.2721 0.3438 -0.0012 0.0214 -0.0135 113 TYR A CA 541 C C . TYR A 72 ? 0.2840 0.2737 0.3512 -0.0037 0.0174 -0.0198 113 TYR A C 542 O O . TYR A 72 ? 0.2885 0.2741 0.3558 -0.0031 0.0185 -0.0209 113 TYR A O 543 C CB . TYR A 72 ? 0.2754 0.2685 0.3232 0.0006 0.0191 -0.0139 113 TYR A CB 544 C CG . TYR A 72 ? 0.2820 0.2751 0.3244 0.0036 0.0225 -0.0085 113 TYR A CG 545 C CD1 . TYR A 72 ? 0.3017 0.2982 0.3464 0.0034 0.0227 -0.0066 113 TYR A CD1 546 C CD2 . TYR A 72 ? 0.2985 0.2879 0.3346 0.0069 0.0257 -0.0051 113 TYR A CD2 547 C CE1 . TYR A 72 ? 0.3059 0.3018 0.3451 0.0066 0.0263 -0.0018 113 TYR A CE1 548 C CE2 . TYR A 72 ? 0.3022 0.2907 0.3326 0.0102 0.0287 -0.0003 113 TYR A CE2 549 C CZ . TYR A 72 ? 0.3101 0.3019 0.3416 0.0101 0.0291 0.0010 113 TYR A CZ 550 O OH . TYR A 72 ? 0.3192 0.3096 0.3442 0.0139 0.0324 0.0054 113 TYR A OH 551 N N . ASP A 73 ? 0.2763 0.2695 0.3457 -0.0059 0.0122 -0.0243 114 ASP A N 552 C CA . ASP A 73 ? 0.3085 0.3006 0.3802 -0.0077 0.0075 -0.0313 114 ASP A CA 553 C C . ASP A 73 ? 0.2828 0.2774 0.3408 -0.0070 0.0033 -0.0349 114 ASP A C 554 O O . ASP A 73 ? 0.2923 0.2905 0.3479 -0.0076 0.0000 -0.0354 114 ASP A O 555 C CB . ASP A 73 ? 0.3174 0.3106 0.4038 -0.0106 0.0041 -0.0344 114 ASP A CB 556 C CG . ASP A 73 ? 0.3829 0.3733 0.4852 -0.0117 0.0093 -0.0305 114 ASP A CG 557 O OD1 . ASP A 73 ? 0.3550 0.3402 0.4586 -0.0111 0.0124 -0.0297 114 ASP A OD1 558 O OD2 . ASP A 73 ? 0.4165 0.4096 0.5296 -0.0130 0.0105 -0.0279 114 ASP A OD2 559 N N . VAL A 74 ? 0.2887 0.2812 0.3383 -0.0056 0.0040 -0.0369 115 VAL A N 560 C CA . VAL A 74 ? 0.2738 0.2686 0.3095 -0.0045 0.0024 -0.0385 115 VAL A CA 561 C C . VAL A 74 ? 0.2936 0.2868 0.3253 -0.0046 -0.0004 -0.0454 115 VAL A C 562 O O . VAL A 74 ? 0.3119 0.3017 0.3508 -0.0050 -0.0003 -0.0485 115 VAL A O 563 C CB . VAL A 74 ? 0.2785 0.2735 0.3070 -0.0021 0.0064 -0.0341 115 VAL A CB 564 C CG1 . VAL A 74 ? 0.2576 0.2539 0.2875 -0.0014 0.0086 -0.0280 115 VAL A CG1 565 C CG2 . VAL A 74 ? 0.2573 0.2485 0.2883 -0.0006 0.0095 -0.0344 115 VAL A CG2 566 N N . LEU A 75 ? 0.2769 0.2721 0.2969 -0.0041 -0.0024 -0.0474 116 LEU A N 567 C CA . LEU A 75 ? 0.2833 0.2767 0.2970 -0.0035 -0.0040 -0.0538 116 LEU A CA 568 C C . LEU A 75 ? 0.2854 0.2774 0.2975 -0.0017 0.0004 -0.0538 116 LEU A C 569 O O . LEU A 75 ? 0.3064 0.3006 0.3128 -0.0006 0.0036 -0.0502 116 LEU A O 570 C CB . LEU A 75 ? 0.2822 0.2777 0.2828 -0.0032 -0.0066 -0.0551 116 LEU A CB 571 C CG . LEU A 75 ? 0.3260 0.3191 0.3190 -0.0022 -0.0090 -0.0625 116 LEU A CG 572 C CD1 . LEU A 75 ? 0.3528 0.3440 0.3526 -0.0033 -0.0153 -0.0676 116 LEU A CD1 573 C CD2 . LEU A 75 ? 0.3366 0.3315 0.3143 -0.0013 -0.0095 -0.0617 116 LEU A CD2 574 N N . LEU A 76 ? 0.2930 0.2813 0.3104 -0.0014 0.0004 -0.0582 117 LEU A N 575 C CA . LEU A 76 ? 0.3063 0.2931 0.3223 0.0007 0.0042 -0.0593 117 LEU A CA 576 C C . LEU A 76 ? 0.3210 0.3064 0.3308 0.0016 0.0025 -0.0671 117 LEU A C 577 O O . LEU A 76 ? 0.3395 0.3246 0.3452 0.0007 -0.0018 -0.0709 117 LEU A O 578 C CB . LEU A 76 ? 0.2934 0.2765 0.3209 0.0012 0.0065 -0.0572 117 LEU A CB 579 C CG . LEU A 76 ? 0.2933 0.2771 0.3250 0.0011 0.0089 -0.0494 117 LEU A CG 580 C CD1 . LEU A 76 ? 0.3124 0.2912 0.3535 0.0022 0.0116 -0.0471 117 LEU A CD1 581 C CD2 . LEU A 76 ? 0.2953 0.2830 0.3184 0.0027 0.0111 -0.0452 117 LEU A CD2 582 N N . SER A 77 ? 0.3189 0.3030 0.3278 0.0037 0.0057 -0.0694 118 SER A N 583 C CA . SER A 77 ? 0.3369 0.3198 0.3383 0.0054 0.0054 -0.0766 118 SER A CA 584 C C . SER A 77 ? 0.3262 0.3056 0.3346 0.0074 0.0078 -0.0798 118 SER A C 585 O O . SER A 77 ? 0.3268 0.3071 0.3398 0.0085 0.0114 -0.0758 118 SER A O 586 C CB . SER A 77 ? 0.3454 0.3327 0.3343 0.0065 0.0086 -0.0753 118 SER A CB 587 O OG . SER A 77 ? 0.3552 0.3416 0.3365 0.0089 0.0105 -0.0814 118 SER A OG 588 N N . TYR A 78 ? 0.3411 0.3163 0.3500 0.0082 0.0053 -0.0875 119 TYR A N 589 C CA . TYR A 78 ? 0.3460 0.3172 0.3622 0.0102 0.0070 -0.0909 119 TYR A CA 590 C C . TYR A 78 ? 0.3741 0.3429 0.3828 0.0124 0.0059 -0.1002 119 TYR A C 591 O O . TYR A 78 ? 0.3711 0.3390 0.3730 0.0117 0.0015 -0.1047 119 TYR A O 592 C CB . TYR A 78 ? 0.3559 0.3216 0.3863 0.0085 0.0042 -0.0910 119 TYR A CB 593 C CG . TYR A 78 ? 0.3617 0.3284 0.4000 0.0065 0.0054 -0.0820 119 TYR A CG 594 C CD1 . TYR A 78 ? 0.3573 0.3240 0.3992 0.0082 0.0097 -0.0763 119 TYR A CD1 595 C CD2 . TYR A 78 ? 0.4181 0.3854 0.4605 0.0034 0.0021 -0.0799 119 TYR A CD2 596 C CE1 . TYR A 78 ? 0.3438 0.3106 0.3911 0.0070 0.0110 -0.0681 119 TYR A CE1 597 C CE2 . TYR A 78 ? 0.3909 0.3588 0.4402 0.0020 0.0041 -0.0718 119 TYR A CE2 598 C CZ . TYR A 78 ? 0.3905 0.3577 0.4415 0.0039 0.0086 -0.0661 119 TYR A CZ 599 O OH . TYR A 78 ? 0.3667 0.3339 0.4227 0.0032 0.0107 -0.0583 119 TYR A OH 600 N N . PRO A 79 ? 0.3806 0.3480 0.3912 0.0153 0.0095 -0.1033 120 PRO A N 601 C CA . PRO A 79 ? 0.4044 0.3686 0.4082 0.0180 0.0085 -0.1129 120 PRO A CA 602 C C . PRO A 79 ? 0.4422 0.3995 0.4537 0.0169 0.0022 -0.1190 120 PRO A C 603 O O . PRO A 79 ? 0.4484 0.4031 0.4735 0.0145 0.0004 -0.1155 120 PRO A O 604 C CB . PRO A 79 ? 0.4013 0.3653 0.4094 0.0214 0.0138 -0.1144 120 PRO A CB 605 C CG . PRO A 79 ? 0.3924 0.3608 0.4060 0.0209 0.0176 -0.1055 120 PRO A CG 606 C CD . PRO A 79 ? 0.3635 0.3326 0.3806 0.0170 0.0144 -0.0986 120 PRO A CD 607 N N . ASN A 80 ? 0.4725 0.4269 0.4755 0.0188 -0.0008 -0.1282 121 ASN A N 608 C CA . ASN A 80 ? 0.5107 0.4581 0.5215 0.0182 -0.0073 -0.1357 121 ASN A CA 609 C C . ASN A 80 ? 0.5376 0.4799 0.5576 0.0208 -0.0049 -0.1400 121 ASN A C 610 O O . ASN A 80 ? 0.5343 0.4764 0.5458 0.0249 -0.0015 -0.1454 121 ASN A O 611 C CB . ASN A 80 ? 0.5160 0.4619 0.5120 0.0199 -0.0123 -0.1441 121 ASN A CB 612 C CG . ASN A 80 ? 0.5931 0.5320 0.5978 0.0190 -0.0207 -0.1527 121 ASN A CG 613 O OD1 . ASN A 80 ? 0.6217 0.5554 0.6404 0.0190 -0.0212 -0.1556 121 ASN A OD1 614 N ND2 . ASN A 80 ? 0.6776 0.6163 0.6748 0.0183 -0.0277 -0.1566 121 ASN A ND2 615 N N . LYS A 81 ? 0.5665 0.5046 0.6039 0.0187 -0.0061 -0.1371 122 LYS A N 616 C CA . LYS A 81 ? 0.6104 0.5424 0.6592 0.0208 -0.0045 -0.1400 122 LYS A CA 617 C C . LYS A 81 ? 0.6329 0.5589 0.6785 0.0241 -0.0075 -0.1525 122 LYS A C 618 O O . LYS A 81 ? 0.6444 0.5674 0.6929 0.0277 -0.0043 -0.1559 122 LYS A O 619 C CB . LYS A 81 ? 0.6262 0.5533 0.6937 0.0173 -0.0063 -0.1349 122 LYS A CB 620 C CG . LYS A 81 ? 0.6632 0.5928 0.7365 0.0169 -0.0008 -0.1236 122 LYS A CG 621 C CD . LYS A 81 ? 0.7685 0.6900 0.8584 0.0170 -0.0002 -0.1215 122 LYS A CD 622 C CE . LYS A 81 ? 0.8157 0.7392 0.9084 0.0179 0.0051 -0.1106 122 LYS A CE 623 N NZ . LYS A 81 ? 0.8551 0.7703 0.9607 0.0195 0.0065 -0.1085 122 LYS A NZ 624 N N . THR A 82 ? 0.6436 0.5678 0.6829 0.0234 -0.0140 -0.1597 123 THR A N 625 C CA . THR A 82 ? 0.6621 0.5799 0.6970 0.0268 -0.0179 -0.1725 123 THR A CA 626 C C . THR A 82 ? 0.6682 0.5891 0.6801 0.0307 -0.0173 -0.1785 123 THR A C 627 O O . THR A 82 ? 0.6866 0.6023 0.6912 0.0338 -0.0216 -0.1896 123 THR A O 628 C CB . THR A 82 ? 0.6740 0.5852 0.7210 0.0239 -0.0272 -0.1786 123 THR A CB 629 O OG1 . THR A 82 ? 0.6886 0.6038 0.7295 0.0210 -0.0321 -0.1768 123 THR A OG1 630 C CG2 . THR A 82 ? 0.6630 0.5699 0.7333 0.0204 -0.0267 -0.1726 123 THR A CG2 631 N N . HIS A 83 ? 0.6469 0.5756 0.6471 0.0308 -0.0117 -0.1713 124 HIS A N 632 C CA . HIS A 83 ? 0.6491 0.5808 0.6270 0.0343 -0.0096 -0.1750 124 HIS A CA 633 C C . HIS A 83 ? 0.6183 0.5580 0.5913 0.0349 0.0000 -0.1661 124 HIS A C 634 O O . HIS A 83 ? 0.5902 0.5356 0.5560 0.0327 0.0012 -0.1589 124 HIS A O 635 C CB . HIS A 83 ? 0.6629 0.5955 0.6315 0.0320 -0.0166 -0.1750 124 HIS A CB 636 C CG . HIS A 83 ? 0.7326 0.6646 0.6776 0.0362 -0.0175 -0.1817 124 HIS A CG 637 N ND1 . HIS A 83 ? 0.7855 0.7195 0.7176 0.0351 -0.0220 -0.1799 124 HIS A ND1 638 C CD2 . HIS A 83 ? 0.8217 0.7507 0.7529 0.0417 -0.0148 -0.1903 124 HIS A CD2 639 C CE1 . HIS A 83 ? 0.8279 0.7598 0.7383 0.0399 -0.0220 -0.1867 124 HIS A CE1 640 N NE2 . HIS A 83 ? 0.8548 0.7837 0.7639 0.0440 -0.0173 -0.1931 124 HIS A NE2 641 N N . PRO A 84 ? 0.6002 0.5404 0.5787 0.0379 0.0064 -0.1667 125 PRO A N 642 C CA . PRO A 84 ? 0.5706 0.5183 0.5505 0.0381 0.0148 -0.1581 125 PRO A CA 643 C C . PRO A 84 ? 0.5589 0.5129 0.5207 0.0397 0.0204 -0.1562 125 PRO A C 644 O O . PRO A 84 ? 0.5659 0.5179 0.5119 0.0428 0.0203 -0.1634 125 PRO A O 645 C CB . PRO A 84 ? 0.5867 0.5321 0.5765 0.0419 0.0190 -0.1619 125 PRO A CB 646 C CG . PRO A 84 ? 0.6143 0.5501 0.6113 0.0426 0.0121 -0.1710 125 PRO A CG 647 C CD . PRO A 84 ? 0.6179 0.5512 0.6023 0.0416 0.0056 -0.1763 125 PRO A CD 648 N N . ASN A 85 ? 0.5036 0.4648 0.4675 0.0375 0.0250 -0.1465 126 ASN A N 649 C CA . ASN A 85 ? 0.4990 0.4664 0.4491 0.0384 0.0314 -0.1431 126 ASN A CA 650 C C . ASN A 85 ? 0.4970 0.4672 0.4476 0.0428 0.0398 -0.1462 126 ASN A C 651 O O . ASN A 85 ? 0.4900 0.4603 0.4558 0.0438 0.0415 -0.1459 126 ASN A O 652 C CB . ASN A 85 ? 0.4536 0.4275 0.4092 0.0344 0.0330 -0.1317 126 ASN A CB 653 C CG . ASN A 85 ? 0.4795 0.4515 0.4356 0.0302 0.0254 -0.1280 126 ASN A CG 654 O OD1 . ASN A 85 ? 0.4786 0.4469 0.4250 0.0302 0.0202 -0.1326 126 ASN A OD1 655 N ND2 . ASN A 85 ? 0.4306 0.4052 0.3984 0.0269 0.0246 -0.1200 126 ASN A ND2 656 N N . TYR A 86 ? 0.5044 0.4762 0.4384 0.0458 0.0451 -0.1493 127 TYR A N 657 C CA . TYR A 86 ? 0.5142 0.4902 0.4486 0.0499 0.0548 -0.1514 127 TYR A CA 658 C C . TYR A 86 ? 0.5204 0.4995 0.4355 0.0517 0.0616 -0.1507 127 TYR A C 659 O O . TYR A 86 ? 0.5384 0.5154 0.4386 0.0503 0.0578 -0.1495 127 TYR A O 660 C CB . TYR A 86 ? 0.5142 0.4847 0.4534 0.0544 0.0543 -0.1615 127 TYR A CB 661 C CG . TYR A 86 ? 0.5647 0.5283 0.4865 0.0580 0.0515 -0.1716 127 TYR A CG 662 C CD1 . TYR A 86 ? 0.6082 0.5721 0.5178 0.0636 0.0592 -0.1779 127 TYR A CD1 663 C CD2 . TYR A 86 ? 0.5700 0.5265 0.4878 0.0561 0.0412 -0.1753 127 TYR A CD2 664 C CE1 . TYR A 86 ? 0.6433 0.6003 0.5351 0.0677 0.0563 -0.1878 127 TYR A CE1 665 C CE2 . TYR A 86 ? 0.6228 0.5725 0.5240 0.0599 0.0374 -0.1856 127 TYR A CE2 666 C CZ . TYR A 86 ? 0.6654 0.6150 0.5527 0.0659 0.0450 -0.1918 127 TYR A CZ 667 O OH . TYR A 86 ? 0.6837 0.6261 0.5528 0.0703 0.0412 -0.2024 127 TYR A OH 668 N N . ILE A 87 ? 0.5196 0.5042 0.4360 0.0547 0.0717 -0.1507 128 ILE A N 669 C CA . ILE A 87 ? 0.5174 0.5051 0.4167 0.0567 0.0803 -0.1494 128 ILE A CA 670 C C . ILE A 87 ? 0.5364 0.5226 0.4305 0.0632 0.0871 -0.1587 128 ILE A C 671 O O . ILE A 87 ? 0.5145 0.5014 0.4243 0.0653 0.0884 -0.1626 128 ILE A O 672 C CB . ILE A 87 ? 0.5082 0.5054 0.4164 0.0540 0.0881 -0.1395 128 ILE A CB 673 C CG1 . ILE A 87 ? 0.4847 0.4832 0.3965 0.0480 0.0817 -0.1304 128 ILE A CG1 674 C CG2 . ILE A 87 ? 0.5285 0.5291 0.4216 0.0566 0.0992 -0.1384 128 ILE A CG2 675 C CD1 . ILE A 87 ? 0.5085 0.5156 0.4367 0.0451 0.0865 -0.1221 128 ILE A CD1 676 N N . SER A 88 ? 0.5667 0.5504 0.4381 0.0666 0.0914 -0.1621 129 SER A N 677 C CA . SER A 88 ? 0.5995 0.5815 0.4619 0.0734 0.0989 -0.1709 129 SER A CA 678 C C . SER A 88 ? 0.6178 0.6052 0.4671 0.0757 0.1123 -0.1671 129 SER A C 679 O O . SER A 88 ? 0.6129 0.6020 0.4514 0.0728 0.1138 -0.1592 129 SER A O 680 C CB . SER A 88 ? 0.6165 0.5882 0.4596 0.0771 0.0914 -0.1811 129 SER A CB 681 O OG . SER A 88 ? 0.6516 0.6177 0.5076 0.0756 0.0802 -0.1861 129 SER A OG 682 N N . ILE A 89 ? 0.6288 0.6184 0.4793 0.0812 0.1222 -0.1727 130 ILE A N 683 C CA . ILE A 89 ? 0.6590 0.6501 0.4899 0.0856 0.1346 -0.1728 130 ILE A CA 684 C C . ILE A 89 ? 0.6919 0.6727 0.5004 0.0918 0.1306 -0.1845 130 ILE A C 685 O O . ILE A 89 ? 0.6763 0.6528 0.4926 0.0947 0.1254 -0.1940 130 ILE A O 686 C CB . ILE A 89 ? 0.6605 0.6606 0.5054 0.0883 0.1490 -0.1721 130 ILE A CB 687 C CG1 . ILE A 89 ? 0.6231 0.6335 0.4904 0.0822 0.1523 -0.1608 130 ILE A CG1 688 C CG2 . ILE A 89 ? 0.6896 0.6893 0.5111 0.0941 0.1622 -0.1740 130 ILE A CG2 689 C CD1 . ILE A 89 ? 0.6577 0.6774 0.5470 0.0843 0.1628 -0.1611 130 ILE A CD1 690 N N . ILE A 90 ? 0.7354 0.7119 0.5163 0.0938 0.1323 -0.1837 131 ILE A N 691 C CA . ILE A 90 ? 0.7975 0.7633 0.5536 0.0995 0.1263 -0.1943 131 ILE A CA 692 C C . ILE A 90 ? 0.8364 0.8017 0.5680 0.1064 0.1403 -0.1960 131 ILE A C 693 O O . ILE A 90 ? 0.8315 0.8023 0.5574 0.1049 0.1507 -0.1862 131 ILE A O 694 C CB . ILE A 90 ? 0.8030 0.7624 0.5485 0.0955 0.1115 -0.1922 131 ILE A CB 695 C CG1 . ILE A 90 ? 0.8504 0.7988 0.5830 0.0997 0.0995 -0.2052 131 ILE A CG1 696 C CG2 . ILE A 90 ? 0.8211 0.7813 0.5463 0.0942 0.1156 -0.1826 131 ILE A CG2 697 C CD1 . ILE A 90 ? 0.8797 0.8236 0.6138 0.0947 0.0836 -0.2037 131 ILE A CD1 698 N N . ASN A 91 ? 0.8790 0.8382 0.5979 0.1141 0.1415 -0.2084 132 ASN A N 699 C CA . ASN A 91 ? 0.9347 0.8922 0.6269 0.1216 0.1550 -0.2106 132 ASN A CA 700 C C . ASN A 91 ? 0.9768 0.9245 0.6336 0.1246 0.1491 -0.2119 132 ASN A C 701 O O . ASN A 91 ? 0.9705 0.9130 0.6254 0.1209 0.1339 -0.2119 132 ASN A O 702 C CB . ASN A 91 ? 0.9460 0.9021 0.6393 0.1294 0.1618 -0.2228 132 ASN A CB 703 C CG . ASN A 91 ? 0.9544 0.8994 0.6413 0.1333 0.1475 -0.2370 132 ASN A CG 704 O OD1 . ASN A 91 ? 0.9631 0.8998 0.6336 0.1326 0.1348 -0.2395 132 ASN A OD1 705 N ND2 . ASN A 91 ? 0.9226 0.8674 0.6237 0.1373 0.1494 -0.2467 132 ASN A ND2 706 N N . GLU A 92 ? 1.0298 0.9748 0.6589 0.1316 0.1609 -0.2130 133 GLU A N 707 C CA . GLU A 92 ? 1.0762 1.0114 0.6686 0.1355 0.1562 -0.2136 133 GLU A CA 708 C C . GLU A 92 ? 1.0987 1.0218 0.6754 0.1403 0.1400 -0.2280 133 GLU A C 709 O O . GLU A 92 ? 1.1224 1.0375 0.6740 0.1420 0.1309 -0.2287 133 GLU A O 710 C CB . GLU A 92 ? 1.1082 1.0431 0.6740 0.1423 0.1740 -0.2109 133 GLU A CB 711 C CG . GLU A 92 ? 1.1551 1.0904 0.7200 0.1503 0.1853 -0.2212 133 GLU A CG 712 C CD . GLU A 92 ? 1.2159 1.1531 0.7592 0.1561 0.2058 -0.2162 133 GLU A CD 713 O OE1 . GLU A 92 ? 1.2345 1.1743 0.7696 0.1527 0.2125 -0.2030 133 GLU A OE1 714 O OE2 . GLU A 92 ? 1.2467 1.1825 0.7815 0.1642 0.2155 -0.2253 133 GLU A OE2 715 N N . ASP A 93 ? 1.1009 1.0227 0.6929 0.1427 0.1363 -0.2396 134 ASP A N 716 C CA . ASP A 93 ? 1.1157 1.0268 0.7014 0.1456 0.1192 -0.2534 134 ASP A CA 717 C C . ASP A 93 ? 1.0851 0.9965 0.6924 0.1368 0.1026 -0.2502 134 ASP A C 718 O O . ASP A 93 ? 1.1062 1.0089 0.7059 0.1375 0.0868 -0.2583 134 ASP A O 719 C CB . ASP A 93 ? 1.1233 1.0329 0.7214 0.1505 0.1212 -0.2662 134 ASP A CB 720 C CG . ASP A 93 ? 1.1808 1.0891 0.7561 0.1603 0.1369 -0.2716 134 ASP A CG 721 O OD1 . ASP A 93 ? 1.2121 1.1163 0.7547 0.1649 0.1421 -0.2690 134 ASP A OD1 722 O OD2 . ASP A 93 ? 1.2121 1.1230 0.8016 0.1638 0.1442 -0.2783 134 ASP A OD2 723 N N . GLY A 94 ? 1.0412 0.9627 0.6759 0.1286 0.1061 -0.2384 135 GLY A N 724 C CA . GLY A 94 ? 0.9923 0.9149 0.6500 0.1204 0.0923 -0.2349 135 GLY A CA 725 C C . GLY A 94 ? 0.9537 0.8778 0.6422 0.1182 0.0883 -0.2406 135 GLY A C 726 O O . GLY A 94 ? 0.9537 0.8759 0.6588 0.1130 0.0752 -0.2413 135 GLY A O 727 N N . ASN A 95 ? 0.9300 0.8575 0.6265 0.1224 0.0996 -0.2445 136 ASN A N 728 C CA A ASN A 95 ? 0.8940 0.8238 0.6213 0.1203 0.0974 -0.2480 136 ASN A CA 729 C CA B ASN A 95 ? 0.8986 0.8285 0.6258 0.1204 0.0976 -0.2480 136 ASN A CA 730 C C . ASN A 95 ? 0.8535 0.7948 0.6074 0.1131 0.1033 -0.2346 136 ASN A C 731 O O . ASN A 95 ? 0.8435 0.7927 0.5947 0.1127 0.1161 -0.2259 136 ASN A O 732 C CB A ASN A 95 ? 0.9079 0.8361 0.6337 0.1283 0.1059 -0.2587 136 ASN A CB 733 C CB B ASN A 95 ? 0.9174 0.8458 0.6422 0.1285 0.1068 -0.2585 136 ASN A CB 734 C CG A ASN A 95 ? 0.9327 0.8496 0.6287 0.1366 0.1019 -0.2721 136 ASN A CG 735 C CG B ASN A 95 ? 0.9165 0.8416 0.6655 0.1286 0.0994 -0.2672 136 ASN A CG 736 O OD1 A ASN A 95 ? 0.9267 0.8355 0.6101 0.1360 0.0883 -0.2765 136 ASN A OD1 737 O OD1 B ASN A 95 ? 0.9007 0.8292 0.6762 0.1220 0.0939 -0.2614 136 ASN A OD1 738 N ND2 A ASN A 95 ? 0.9266 0.8432 0.6114 0.1446 0.1137 -0.2789 136 ASN A ND2 739 N ND2 B ASN A 95 ? 0.9366 0.8542 0.6758 0.1365 0.0995 -0.2810 136 ASN A ND2 740 N N . GLU A 96 ? 0.8150 0.7568 0.5942 0.1074 0.0938 -0.2330 137 GLU A N 741 C CA . GLU A 96 ? 0.7629 0.7145 0.5675 0.1008 0.0974 -0.2211 137 GLU A CA 742 C C . GLU A 96 ? 0.7499 0.7060 0.5739 0.1039 0.1057 -0.2244 137 GLU A C 743 O O . GLU A 96 ? 0.7413 0.6927 0.5794 0.1051 0.0995 -0.2318 137 GLU A O 744 C CB . GLU A 96 ? 0.7407 0.6902 0.5610 0.0937 0.0837 -0.2172 137 GLU A CB 745 C CG . GLU A 96 ? 0.7316 0.6762 0.5327 0.0915 0.0746 -0.2156 137 GLU A CG 746 C CD . GLU A 96 ? 0.7376 0.6819 0.5544 0.0841 0.0628 -0.2100 137 GLU A CD 747 O OE1 . GLU A 96 ? 0.6883 0.6314 0.5273 0.0817 0.0576 -0.2116 137 GLU A OE1 748 O OE2 . GLU A 96 ? 0.7382 0.6828 0.5442 0.0809 0.0588 -0.2039 137 GLU A OE2 749 N N . ILE A 97 ? 0.7370 0.7019 0.5618 0.1054 0.1199 -0.2189 138 ILE A N 750 C CA . ILE A 97 ? 0.7266 0.6967 0.5673 0.1097 0.1298 -0.2226 138 ILE A CA 751 C C . ILE A 97 ? 0.6873 0.6660 0.5591 0.1047 0.1303 -0.2144 138 ILE A C 752 O O . ILE A 97 ? 0.6657 0.6482 0.5555 0.1076 0.1352 -0.2175 138 ILE A O 753 C CB . ILE A 97 ? 0.7517 0.7267 0.5770 0.1152 0.1461 -0.2228 138 ILE A CB 754 C CG1 . ILE A 97 ? 0.7480 0.7320 0.5722 0.1103 0.1540 -0.2091 138 ILE A CG1 755 C CG2 . ILE A 97 ? 0.7855 0.7505 0.5791 0.1220 0.1453 -0.2330 138 ILE A CG2 756 C CD1 . ILE A 97 ? 0.7724 0.7630 0.5872 0.1149 0.1724 -0.2072 138 ILE A CD1 757 N N . PHE A 98 ? 0.6485 0.6300 0.5263 0.0974 0.1245 -0.2042 139 PHE A N 758 C CA . PHE A 98 ? 0.6230 0.6112 0.5280 0.0927 0.1228 -0.1967 139 PHE A CA 759 C C . PHE A 98 ? 0.5906 0.5756 0.4972 0.0859 0.1108 -0.1904 139 PHE A C 760 O O . PHE A 98 ? 0.5860 0.5698 0.4754 0.0835 0.1092 -0.1865 139 PHE A O 761 C CB . PHE A 98 ? 0.6146 0.6147 0.5281 0.0911 0.1346 -0.1876 139 PHE A CB 762 C CG . PHE A 98 ? 0.6155 0.6218 0.5526 0.0852 0.1304 -0.1784 139 PHE A CG 763 C CD1 . PHE A 98 ? 0.6249 0.6336 0.5863 0.0864 0.1289 -0.1800 139 PHE A CD1 764 C CD2 . PHE A 98 ? 0.6158 0.6248 0.5503 0.0790 0.1275 -0.1684 139 PHE A CD2 765 C CE1 . PHE A 98 ? 0.6133 0.6268 0.5944 0.0817 0.1245 -0.1718 139 PHE A CE1 766 C CE2 . PHE A 98 ? 0.5930 0.6069 0.5481 0.0741 0.1231 -0.1604 139 PHE A CE2 767 C CZ . PHE A 98 ? 0.5852 0.6014 0.5629 0.0755 0.1216 -0.1622 139 PHE A CZ 768 N N . ASN A 99 ? 0.5806 0.5639 0.5073 0.0833 0.1028 -0.1896 140 ASN A N 769 C CA . ASN A 99 ? 0.5769 0.5579 0.5089 0.0769 0.0922 -0.1830 140 ASN A CA 770 C C . ASN A 99 ? 0.5422 0.5299 0.4967 0.0732 0.0922 -0.1743 140 ASN A C 771 O O . ASN A 99 ? 0.5369 0.5263 0.5082 0.0758 0.0942 -0.1764 140 ASN A O 772 C CB . ASN A 99 ? 0.5942 0.5648 0.5288 0.0772 0.0811 -0.1905 140 ASN A CB 773 C CG . ASN A 99 ? 0.6698 0.6322 0.5817 0.0803 0.0776 -0.1997 140 ASN A CG 774 O OD1 . ASN A 99 ? 0.6563 0.6197 0.5485 0.0801 0.0798 -0.1977 140 ASN A OD1 775 N ND2 . ASN A 99 ? 0.7209 0.6747 0.6356 0.0833 0.0714 -0.2098 140 ASN A ND2 776 N N . THR A 100 ? 0.5279 0.5187 0.4827 0.0675 0.0890 -0.1648 141 THR A N 777 C CA . THR A 100 ? 0.5038 0.4999 0.4786 0.0640 0.0874 -0.1566 141 THR A CA 778 C C . THR A 100 ? 0.5064 0.4952 0.4930 0.0630 0.0776 -0.1583 141 THR A C 779 O O . THR A 100 ? 0.5083 0.4886 0.4874 0.0634 0.0714 -0.1643 141 THR A O 780 C CB . THR A 100 ? 0.4865 0.4874 0.4576 0.0585 0.0868 -0.1464 141 THR A CB 781 O OG1 . THR A 100 ? 0.4686 0.4630 0.4282 0.0555 0.0784 -0.1461 141 THR A OG1 782 C CG2 . THR A 100 ? 0.5074 0.5148 0.4675 0.0593 0.0970 -0.1441 141 THR A CG2 783 N N . SER A 101 ? 0.4981 0.4898 0.5028 0.0617 0.0760 -0.1528 142 SER A N 784 C CA A SER A 101 ? 0.5002 0.4851 0.5173 0.0615 0.0685 -0.1538 142 SER A CA 785 C CA B SER A 101 ? 0.4974 0.4823 0.5146 0.0615 0.0684 -0.1537 142 SER A CA 786 C C . SER A 101 ? 0.4950 0.4739 0.5076 0.0567 0.0598 -0.1505 142 SER A C 787 O O . SER A 101 ? 0.4989 0.4811 0.5033 0.0528 0.0591 -0.1446 142 SER A O 788 C CB A SER A 101 ? 0.4982 0.4879 0.5340 0.0620 0.0694 -0.1481 142 SER A CB 789 C CB B SER A 101 ? 0.4937 0.4833 0.5295 0.0616 0.0690 -0.1475 142 SER A CB 790 O OG A SER A 101 ? 0.5047 0.4871 0.5518 0.0622 0.0627 -0.1481 142 SER A OG 791 O OG B SER A 101 ? 0.4758 0.4685 0.5126 0.0568 0.0658 -0.1381 142 SER A OG 792 N N . LEU A 102 ? 0.4996 0.4698 0.5187 0.0570 0.0535 -0.1543 143 LEU A N 793 C CA . LEU A 102 ? 0.5073 0.4720 0.5253 0.0524 0.0455 -0.1513 143 LEU A CA 794 C C . LEU A 102 ? 0.4940 0.4593 0.5257 0.0495 0.0428 -0.1420 143 LEU A C 795 O O . LEU A 102 ? 0.4968 0.4594 0.5287 0.0453 0.0375 -0.1373 143 LEU A O 796 C CB . LEU A 102 ? 0.5401 0.4948 0.5578 0.0536 0.0399 -0.1603 143 LEU A CB 797 C CG . LEU A 102 ? 0.5699 0.5226 0.5720 0.0570 0.0415 -0.1704 143 LEU A CG 798 C CD1 . LEU A 102 ? 0.5871 0.5291 0.5902 0.0575 0.0340 -0.1793 143 LEU A CD1 799 C CD2 . LEU A 102 ? 0.5856 0.5430 0.5703 0.0548 0.0427 -0.1676 143 LEU A CD2 800 N N . PHE A 103 ? 0.4741 0.4434 0.5167 0.0520 0.0463 -0.1390 144 PHE A N 801 C CA . PHE A 103 ? 0.4587 0.4281 0.5128 0.0504 0.0436 -0.1304 144 PHE A CA 802 C C . PHE A 103 ? 0.4466 0.4223 0.5102 0.0537 0.0479 -0.1280 144 PHE A C 803 O O . PHE A 103 ? 0.4456 0.4237 0.5108 0.0578 0.0525 -0.1343 144 PHE A O 804 C CB . PHE A 103 ? 0.4654 0.4244 0.5284 0.0504 0.0382 -0.1314 144 PHE A CB 805 C CG . PHE A 103 ? 0.5028 0.4569 0.5735 0.0554 0.0392 -0.1391 144 PHE A CG 806 C CD1 . PHE A 103 ? 0.5244 0.4787 0.6075 0.0590 0.0403 -0.1367 144 PHE A CD1 807 C CD2 . PHE A 103 ? 0.5684 0.5173 0.6335 0.0569 0.0385 -0.1490 144 PHE A CD2 808 C CE1 . PHE A 103 ? 0.5546 0.5043 0.6453 0.0639 0.0412 -0.1438 144 PHE A CE1 809 C CE2 . PHE A 103 ? 0.5961 0.5400 0.6683 0.0618 0.0394 -0.1566 144 PHE A CE2 810 C CZ . PHE A 103 ? 0.6302 0.5746 0.7157 0.0653 0.0410 -0.1538 144 PHE A CZ 811 N N . GLU A 104 ? 0.4169 0.3954 0.4872 0.0525 0.0462 -0.1197 145 GLU A N 812 C CA . GLU A 104 ? 0.4210 0.4046 0.5028 0.0560 0.0483 -0.1175 145 GLU A CA 813 C C . GLU A 104 ? 0.4331 0.4090 0.5264 0.0600 0.0454 -0.1195 145 GLU A C 814 O O . GLU A 104 ? 0.4391 0.4067 0.5336 0.0585 0.0407 -0.1167 145 GLU A O 815 C CB . GLU A 104 ? 0.4033 0.3914 0.4876 0.0539 0.0461 -0.1083 145 GLU A CB 816 C CG . GLU A 104 ? 0.4220 0.4172 0.4972 0.0499 0.0482 -0.1048 145 GLU A CG 817 C CD . GLU A 104 ? 0.4319 0.4294 0.5096 0.0479 0.0447 -0.0961 145 GLU A CD 818 O OE1 . GLU A 104 ? 0.4529 0.4448 0.5266 0.0454 0.0405 -0.0920 145 GLU A OE1 819 O OE2 . GLU A 104 ? 0.4518 0.4564 0.5362 0.0493 0.0461 -0.0938 145 GLU A OE2 820 N N . PRO A 105 ? 0.4464 0.4251 0.5489 0.0650 0.0485 -0.1238 146 PRO A N 821 C CA . PRO A 105 ? 0.4565 0.4275 0.5706 0.0692 0.0454 -0.1248 146 PRO A CA 822 C C . PRO A 105 ? 0.4462 0.4139 0.5644 0.0682 0.0402 -0.1154 146 PRO A C 823 O O . PRO A 105 ? 0.4479 0.4228 0.5675 0.0679 0.0401 -0.1100 146 PRO A O 824 C CB . PRO A 105 ? 0.4686 0.4465 0.5926 0.0746 0.0498 -0.1291 146 PRO A CB 825 C CG . PRO A 105 ? 0.4767 0.4635 0.5922 0.0732 0.0565 -0.1332 146 PRO A CG 826 C CD . PRO A 105 ? 0.4506 0.4394 0.5545 0.0673 0.0552 -0.1272 146 PRO A CD 827 N N . PRO A 106 ? 0.4522 0.4090 0.5717 0.0675 0.0359 -0.1132 147 PRO A N 828 C CA . PRO A 106 ? 0.4500 0.4041 0.5702 0.0664 0.0320 -0.1035 147 PRO A CA 829 C C . PRO A 106 ? 0.4444 0.3991 0.5747 0.0718 0.0303 -0.1003 147 PRO A C 830 O O . PRO A 106 ? 0.4637 0.4172 0.6028 0.0766 0.0312 -0.1056 147 PRO A O 831 C CB . PRO A 106 ? 0.4607 0.4028 0.5806 0.0643 0.0291 -0.1022 147 PRO A CB 832 C CG . PRO A 106 ? 0.4791 0.4167 0.6021 0.0660 0.0303 -0.1115 147 PRO A CG 833 C CD . PRO A 106 ? 0.4673 0.4145 0.5853 0.0664 0.0346 -0.1183 147 PRO A CD 834 N N . PRO A 107 ? 0.4313 0.3876 0.5602 0.0716 0.0274 -0.0921 148 PRO A N 835 C CA . PRO A 107 ? 0.4311 0.3884 0.5688 0.0772 0.0247 -0.0894 148 PRO A CA 836 C C . PRO A 107 ? 0.4374 0.3824 0.5814 0.0815 0.0218 -0.0883 148 PRO A C 837 O O . PRO A 107 ? 0.4312 0.3665 0.5719 0.0790 0.0213 -0.0868 148 PRO A O 838 C CB . PRO A 107 ? 0.4322 0.3918 0.5639 0.0756 0.0217 -0.0810 148 PRO A CB 839 C CG . PRO A 107 ? 0.4228 0.3793 0.5437 0.0696 0.0224 -0.0780 148 PRO A CG 840 C CD . PRO A 107 ? 0.4268 0.3834 0.5459 0.0667 0.0261 -0.0854 148 PRO A CD 841 N N . PRO A 108 ? 0.4367 0.3818 0.5904 0.0877 0.0195 -0.0882 149 PRO A N 842 C CA . PRO A 108 ? 0.4488 0.3820 0.6092 0.0924 0.0167 -0.0872 149 PRO A CA 843 C C . PRO A 108 ? 0.4564 0.3777 0.6102 0.0911 0.0137 -0.0781 149 PRO A C 844 O O . PRO A 108 ? 0.4378 0.3603 0.5850 0.0908 0.0113 -0.0706 149 PRO A O 845 C CB . PRO A 108 ? 0.4573 0.3950 0.6273 0.0992 0.0137 -0.0870 149 PRO A CB 846 C CG . PRO A 108 ? 0.4396 0.3925 0.6124 0.0979 0.0171 -0.0923 149 PRO A CG 847 C CD . PRO A 108 ? 0.4345 0.3913 0.5949 0.0908 0.0194 -0.0899 149 PRO A CD 848 N N . GLY A 109 ? 0.4683 0.3781 0.6242 0.0905 0.0142 -0.0787 150 GLY A N 849 C CA . GLY A 109 ? 0.4978 0.3958 0.6492 0.0895 0.0124 -0.0696 150 GLY A CA 850 C C . GLY A 109 ? 0.5216 0.4193 0.6645 0.0820 0.0146 -0.0672 150 GLY A C 851 O O . GLY A 109 ? 0.5370 0.4250 0.6774 0.0805 0.0144 -0.0600 150 GLY A O 852 N N . TYR A 110 ? 0.5240 0.4321 0.6629 0.0778 0.0170 -0.0728 151 TYR A N 853 C CA . TYR A 110 ? 0.5571 0.4666 0.6884 0.0708 0.0187 -0.0720 151 TYR A CA 854 C C . TYR A 110 ? 0.5996 0.5107 0.7325 0.0679 0.0207 -0.0818 151 TYR A C 855 O O . TYR A 110 ? 0.6084 0.5234 0.7347 0.0626 0.0218 -0.0832 151 TYR A O 856 C CB . TYR A 110 ? 0.5245 0.4459 0.6476 0.0684 0.0193 -0.0704 151 TYR A CB 857 C CG . TYR A 110 ? 0.4868 0.4094 0.6055 0.0706 0.0170 -0.0619 151 TYR A CG 858 C CD1 . TYR A 110 ? 0.4628 0.3825 0.5735 0.0675 0.0168 -0.0542 151 TYR A CD1 859 C CD2 . TYR A 110 ? 0.4080 0.3352 0.5306 0.0760 0.0149 -0.0620 151 TYR A CD2 860 C CE1 . TYR A 110 ? 0.4483 0.3689 0.5533 0.0700 0.0145 -0.0470 151 TYR A CE1 861 C CE2 . TYR A 110 ? 0.4250 0.3530 0.5428 0.0785 0.0118 -0.0550 151 TYR A CE2 862 C CZ . TYR A 110 ? 0.4233 0.3478 0.5314 0.0755 0.0117 -0.0476 151 TYR A CZ 863 O OH . TYR A 110 ? 0.4166 0.3413 0.5189 0.0786 0.0084 -0.0412 151 TYR A OH 864 N N . GLU A 111 ? 0.6371 0.5462 0.7777 0.0718 0.0211 -0.0891 152 GLU A N 865 C CA . GLU A 111 ? 0.6885 0.5976 0.8297 0.0700 0.0227 -0.0992 152 GLU A CA 866 C C . GLU A 111 ? 0.7107 0.6095 0.8533 0.0656 0.0213 -0.0991 152 GLU A C 867 O O . GLU A 111 ? 0.7245 0.6229 0.8656 0.0632 0.0216 -0.1072 152 GLU A O 868 C CB . GLU A 111 ? 0.6993 0.6080 0.8490 0.0758 0.0236 -0.1075 152 GLU A CB 869 C CG . GLU A 111 ? 0.7379 0.6564 0.8906 0.0808 0.0247 -0.1073 152 GLU A CG 870 C CD . GLU A 111 ? 0.7734 0.6862 0.9344 0.0864 0.0215 -0.1011 152 GLU A CD 871 O OE1 . GLU A 111 ? 0.7740 0.6768 0.9348 0.0859 0.0188 -0.0937 152 GLU A OE1 872 O OE2 . GLU A 111 ? 0.8020 0.7205 0.9698 0.0917 0.0216 -0.1036 152 GLU A OE2 873 N N . ASN A 112 ? 0.7296 0.6199 0.8746 0.0648 0.0199 -0.0901 153 ASN A N 874 C CA . ASN A 112 ? 0.7378 0.6186 0.8863 0.0602 0.0191 -0.0887 153 ASN A CA 875 C C . ASN A 112 ? 0.7315 0.6150 0.8734 0.0547 0.0195 -0.0810 153 ASN A C 876 O O . ASN A 112 ? 0.7330 0.6099 0.8788 0.0506 0.0192 -0.0791 153 ASN A O 877 C CB . ASN A 112 ? 0.7541 0.6212 0.9133 0.0631 0.0180 -0.0853 153 ASN A CB 878 C CG . ASN A 112 ? 0.7723 0.6295 0.9388 0.0585 0.0173 -0.0868 153 ASN A CG 879 O OD1 . ASN A 112 ? 0.7935 0.6497 0.9635 0.0572 0.0161 -0.0970 153 ASN A OD1 880 N ND2 . ASN A 112 ? 0.7934 0.6432 0.9625 0.0562 0.0180 -0.0768 153 ASN A ND2 881 N N . VAL A 113 ? 0.7188 0.6120 0.8516 0.0546 0.0203 -0.0770 154 VAL A N 882 C CA . VAL A 113 ? 0.7071 0.6038 0.8332 0.0496 0.0208 -0.0715 154 VAL A CA 883 C C . VAL A 113 ? 0.7077 0.6087 0.8313 0.0449 0.0204 -0.0797 154 VAL A C 884 O O . VAL A 113 ? 0.7184 0.6252 0.8390 0.0461 0.0206 -0.0880 154 VAL A O 885 C CB . VAL A 113 ? 0.7024 0.6076 0.8195 0.0510 0.0213 -0.0654 154 VAL A CB 886 C CG1 . VAL A 113 ? 0.6485 0.5568 0.7588 0.0461 0.0219 -0.0597 154 VAL A CG1 887 C CG2 . VAL A 113 ? 0.7154 0.6152 0.8345 0.0564 0.0206 -0.0582 154 VAL A CG2 888 N N . SER A 114 ? 0.7049 0.6024 0.8304 0.0400 0.0198 -0.0777 155 SER A N 889 C CA . SER A 114 ? 0.6965 0.5988 0.8182 0.0359 0.0185 -0.0848 155 SER A CA 890 C C . SER A 114 ? 0.6696 0.5799 0.7825 0.0324 0.0191 -0.0794 155 SER A C 891 O O . SER A 114 ? 0.6551 0.5669 0.7650 0.0332 0.0206 -0.0702 155 SER A O 892 C CB . SER A 114 ? 0.7180 0.6117 0.8497 0.0328 0.0162 -0.0898 155 SER A CB 893 O OG . SER A 114 ? 0.7560 0.6432 0.8953 0.0301 0.0169 -0.0813 155 SER A OG 894 N N . ASP A 115 ? 0.6329 0.5481 0.7409 0.0292 0.0175 -0.0852 156 ASP A N 895 C CA . ASP A 115 ? 0.5943 0.5170 0.6941 0.0261 0.0177 -0.0810 156 ASP A CA 896 C C . ASP A 115 ? 0.5397 0.4706 0.6304 0.0290 0.0198 -0.0790 156 ASP A C 897 O O . ASP A 115 ? 0.5190 0.4549 0.6041 0.0278 0.0205 -0.0728 156 ASP A O 898 C CB . ASP A 115 ? 0.6161 0.5353 0.7203 0.0239 0.0187 -0.0711 156 ASP A CB 899 C CG . ASP A 115 ? 0.6858 0.6025 0.7963 0.0188 0.0168 -0.0720 156 ASP A CG 900 O OD1 . ASP A 115 ? 0.7419 0.6636 0.8483 0.0159 0.0170 -0.0677 156 ASP A OD1 901 O OD2 . ASP A 115 ? 0.7432 0.6530 0.8634 0.0179 0.0150 -0.0771 156 ASP A OD2 902 N N . ILE A 116 ? 0.4790 0.4114 0.5694 0.0329 0.0208 -0.0843 157 ILE A N 903 C CA . ILE A 116 ? 0.4384 0.3803 0.5211 0.0346 0.0227 -0.0838 157 ILE A CA 904 C C . ILE A 116 ? 0.4221 0.3698 0.4959 0.0320 0.0227 -0.0895 157 ILE A C 905 O O . ILE A 116 ? 0.4300 0.3760 0.5030 0.0328 0.0224 -0.0979 157 ILE A O 906 C CB . ILE A 116 ? 0.4205 0.3633 0.5071 0.0398 0.0244 -0.0871 157 ILE A CB 907 C CG1 . ILE A 116 ? 0.4119 0.3495 0.5054 0.0430 0.0238 -0.0805 157 ILE A CG1 908 C CG2 . ILE A 116 ? 0.3870 0.3403 0.4673 0.0408 0.0268 -0.0877 157 ILE A CG2 909 C CD1 . ILE A 116 ? 0.4134 0.3509 0.5132 0.0486 0.0247 -0.0839 157 ILE A CD1 910 N N . VAL A 117 ? 0.4070 0.3608 0.4734 0.0294 0.0228 -0.0852 158 VAL A N 911 C CA . VAL A 117 ? 0.3903 0.3489 0.4471 0.0272 0.0227 -0.0897 158 VAL A CA 912 C C . VAL A 117 ? 0.3946 0.3588 0.4466 0.0302 0.0261 -0.0944 158 VAL A C 913 O O . VAL A 117 ? 0.3857 0.3550 0.4388 0.0320 0.0285 -0.0907 158 VAL A O 914 C CB . VAL A 117 ? 0.3696 0.3332 0.4200 0.0237 0.0220 -0.0833 158 VAL A CB 915 C CG1 . VAL A 117 ? 0.3357 0.3068 0.3829 0.0252 0.0247 -0.0778 158 VAL A CG1 916 C CG2 . VAL A 117 ? 0.3871 0.3527 0.4288 0.0213 0.0203 -0.0882 158 VAL A CG2 917 N N . PRO A 118 ? 0.4001 0.3636 0.4471 0.0310 0.0264 -0.1028 159 PRO A N 918 C CA . PRO A 118 ? 0.4053 0.3744 0.4471 0.0339 0.0310 -0.1071 159 PRO A CA 919 C C . PRO A 118 ? 0.3847 0.3621 0.4179 0.0322 0.0335 -0.1027 159 PRO A C 920 O O . PRO A 118 ? 0.3802 0.3584 0.4086 0.0287 0.0310 -0.0983 159 PRO A O 921 C CB . PRO A 118 ? 0.4228 0.3879 0.4584 0.0350 0.0301 -0.1169 159 PRO A CB 922 C CG . PRO A 118 ? 0.4448 0.4050 0.4791 0.0311 0.0244 -0.1166 159 PRO A CG 923 C CD . PRO A 118 ? 0.4192 0.3768 0.4646 0.0292 0.0226 -0.1086 159 PRO A CD 924 N N . PRO A 119 ? 0.3779 0.3616 0.4105 0.0346 0.0386 -0.1034 160 PRO A N 925 C CA . PRO A 119 ? 0.3654 0.3565 0.3911 0.0327 0.0413 -0.0990 160 PRO A CA 926 C C . PRO A 119 ? 0.3666 0.3573 0.3782 0.0303 0.0405 -0.1010 160 PRO A C 927 O O . PRO A 119 ? 0.3589 0.3464 0.3636 0.0317 0.0408 -0.1080 160 PRO A O 928 C CB . PRO A 119 ? 0.3670 0.3640 0.3956 0.0360 0.0476 -0.1017 160 PRO A CB 929 C CG . PRO A 119 ? 0.3704 0.3638 0.4113 0.0396 0.0468 -0.1043 160 PRO A CG 930 C CD . PRO A 119 ? 0.3883 0.3727 0.4277 0.0391 0.0423 -0.1082 160 PRO A CD 931 N N . PHE A 120 ? 0.3510 0.3447 0.3580 0.0270 0.0393 -0.0949 161 PHE A N 932 C CA . PHE A 120 ? 0.3586 0.3522 0.3522 0.0249 0.0380 -0.0956 161 PHE A CA 933 C C . PHE A 120 ? 0.3403 0.3390 0.3317 0.0222 0.0387 -0.0880 161 PHE A C 934 O O . PHE A 120 ? 0.3405 0.3415 0.3411 0.0217 0.0384 -0.0827 161 PHE A O 935 C CB . PHE A 120 ? 0.3493 0.3363 0.3415 0.0231 0.0314 -0.0980 161 PHE A CB 936 C CG . PHE A 120 ? 0.3590 0.3451 0.3583 0.0200 0.0272 -0.0913 161 PHE A CG 937 C CD1 . PHE A 120 ? 0.3237 0.3098 0.3169 0.0170 0.0234 -0.0888 161 PHE A CD1 938 C CD2 . PHE A 120 ? 0.3539 0.3385 0.3654 0.0206 0.0270 -0.0878 161 PHE A CD2 939 C CE1 . PHE A 120 ? 0.3061 0.2914 0.3062 0.0145 0.0203 -0.0828 161 PHE A CE1 940 C CE2 . PHE A 120 ? 0.3612 0.3445 0.3780 0.0183 0.0240 -0.0815 161 PHE A CE2 941 C CZ . PHE A 120 ? 0.3353 0.3193 0.3466 0.0151 0.0210 -0.0791 161 PHE A CZ 942 N N . SER A 121 ? 0.3422 0.3421 0.3210 0.0209 0.0392 -0.0877 162 SER A N 943 C CA . SER A 121 ? 0.3299 0.3335 0.3060 0.0181 0.0391 -0.0806 162 SER A CA 944 C C . SER A 121 ? 0.3382 0.3383 0.3114 0.0155 0.0325 -0.0788 162 SER A C 945 O O . SER A 121 ? 0.3456 0.3428 0.3087 0.0153 0.0299 -0.0823 162 SER A O 946 C CB . SER A 121 ? 0.3458 0.3529 0.3104 0.0182 0.0442 -0.0801 162 SER A CB 947 O OG . SER A 121 ? 0.3520 0.3633 0.3211 0.0205 0.0512 -0.0815 162 SER A OG 948 N N . ALA A 122 ? 0.3157 0.3160 0.2975 0.0138 0.0298 -0.0736 163 ALA A N 949 C CA . ALA A 122 ? 0.3271 0.3244 0.3086 0.0115 0.0241 -0.0721 163 ALA A CA 950 C C . ALA A 122 ? 0.3347 0.3335 0.3052 0.0098 0.0229 -0.0700 163 ALA A C 951 O O . ALA A 122 ? 0.3248 0.3277 0.2920 0.0093 0.0259 -0.0658 163 ALA A O 952 C CB . ALA A 122 ? 0.2964 0.2936 0.2881 0.0106 0.0225 -0.0664 163 ALA A CB 953 N N . PHE A 123 ? 0.3456 0.3411 0.3115 0.0091 0.0181 -0.0732 164 PHE A N 954 C CA . PHE A 123 ? 0.3585 0.3541 0.3136 0.0079 0.0151 -0.0722 164 PHE A CA 955 C C . PHE A 123 ? 0.3759 0.3709 0.3160 0.0097 0.0172 -0.0759 164 PHE A C 956 O O . PHE A 123 ? 0.3755 0.3700 0.3049 0.0093 0.0147 -0.0748 164 PHE A O 957 C CB . PHE A 123 ? 0.3491 0.3478 0.3053 0.0058 0.0148 -0.0647 164 PHE A CB 958 C CG . PHE A 123 ? 0.3337 0.3321 0.3021 0.0044 0.0124 -0.0613 164 PHE A CG 959 C CD1 . PHE A 123 ? 0.3521 0.3483 0.3239 0.0030 0.0070 -0.0619 164 PHE A CD1 960 C CD2 . PHE A 123 ? 0.3278 0.3281 0.3041 0.0048 0.0155 -0.0575 164 PHE A CD2 961 C CE1 . PHE A 123 ? 0.3227 0.3187 0.3055 0.0019 0.0059 -0.0583 164 PHE A CE1 962 C CE2 . PHE A 123 ? 0.3102 0.3096 0.2957 0.0041 0.0139 -0.0539 164 PHE A CE2 963 C CZ . PHE A 123 ? 0.3011 0.2983 0.2898 0.0026 0.0096 -0.0540 164 PHE A CZ 964 N N . SER A 124 ? 0.3588 0.3535 0.2977 0.0122 0.0217 -0.0803 165 SER A N 965 C CA . SER A 124 ? 0.3979 0.3913 0.3213 0.0146 0.0241 -0.0845 165 SER A CA 966 C C . SER A 124 ? 0.4082 0.3965 0.3233 0.0150 0.0165 -0.0897 165 SER A C 967 O O . SER A 124 ? 0.4129 0.3983 0.3371 0.0145 0.0113 -0.0937 165 SER A O 968 C CB . SER A 124 ? 0.3971 0.3903 0.3216 0.0177 0.0295 -0.0899 165 SER A CB 969 O OG . SER A 124 ? 0.4146 0.4054 0.3222 0.0206 0.0315 -0.0948 165 SER A OG 970 N N . PRO A 125 ? 0.4413 0.4284 0.3397 0.0160 0.0156 -0.0895 166 PRO A N 971 C CA . PRO A 125 ? 0.4595 0.4414 0.3492 0.0175 0.0082 -0.0964 166 PRO A CA 972 C C . PRO A 125 ? 0.4878 0.4660 0.3729 0.0211 0.0093 -0.1055 166 PRO A C 973 O O . PRO A 125 ? 0.4657 0.4458 0.3516 0.0229 0.0172 -0.1061 166 PRO A O 974 C CB . PRO A 125 ? 0.4859 0.4670 0.3566 0.0186 0.0079 -0.0936 166 PRO A CB 975 C CG . PRO A 125 ? 0.4762 0.4608 0.3421 0.0193 0.0183 -0.0888 166 PRO A CG 976 C CD . PRO A 125 ? 0.4517 0.4411 0.3378 0.0164 0.0214 -0.0843 166 PRO A CD 977 N N . GLN A 126 ? 0.4939 0.4670 0.3750 0.0224 0.0014 -0.1130 167 GLN A N 978 C CA . GLN A 126 ? 0.5157 0.4843 0.3906 0.0263 0.0013 -0.1226 167 GLN A CA 979 C C . GLN A 126 ? 0.5412 0.5080 0.3923 0.0304 0.0051 -0.1246 167 GLN A C 980 O O . GLN A 126 ? 0.5589 0.5262 0.3975 0.0302 0.0044 -0.1197 167 GLN A O 981 C CB . GLN A 126 ? 0.5346 0.4981 0.4137 0.0262 -0.0094 -0.1302 167 GLN A CB 982 C CG . GLN A 126 ? 0.5481 0.5129 0.4508 0.0218 -0.0130 -0.1276 167 GLN A CG 983 C CD . GLN A 126 ? 0.6259 0.5854 0.5359 0.0218 -0.0224 -0.1361 167 GLN A CD 984 O OE1 . GLN A 126 ? 0.7001 0.6553 0.5969 0.0249 -0.0275 -0.1439 167 GLN A OE1 985 N NE2 . GLN A 126 ? 0.6190 0.5785 0.5500 0.0185 -0.0246 -0.1349 167 GLN A NE2 986 N N . GLY A 127 ? 0.5696 0.5342 0.4142 0.0344 0.0098 -0.1312 168 GLY A N 987 C CA . GLY A 127 ? 0.5949 0.5566 0.4147 0.0392 0.0132 -0.1342 168 GLY A CA 988 C C . GLY A 127 ? 0.6191 0.5799 0.4369 0.0432 0.0208 -0.1404 168 GLY A C 989 O O . GLY A 127 ? 0.6044 0.5682 0.4404 0.0420 0.0245 -0.1406 168 GLY A O 990 N N . MET A 128 ? 0.6495 0.6061 0.4446 0.0485 0.0231 -0.1458 169 MET A N 991 C CA . MET A 128 ? 0.6638 0.6201 0.4545 0.0530 0.0319 -0.1512 169 MET A CA 992 C C . MET A 128 ? 0.6723 0.6299 0.4420 0.0562 0.0425 -0.1470 169 MET A C 993 O O . MET A 128 ? 0.6998 0.6526 0.4501 0.0621 0.0451 -0.1540 169 MET A O 994 C CB . MET A 128 ? 0.6965 0.6452 0.4813 0.0573 0.0248 -0.1643 169 MET A CB 995 C CG . MET A 128 ? 0.7550 0.7019 0.5621 0.0540 0.0151 -0.1686 169 MET A CG 996 S SD . MET A 128 ? 0.9584 0.8959 0.7599 0.0593 0.0076 -0.1848 169 MET A SD 997 C CE . MET A 128 ? 0.9220 0.8568 0.7458 0.0540 -0.0066 -0.1869 169 MET A CE 998 N N . PRO A 129 ? 0.6575 0.6210 0.4308 0.0527 0.0491 -0.1357 170 PRO A N 999 C CA . PRO A 129 ? 0.6788 0.6432 0.4331 0.0555 0.0598 -0.1309 170 PRO A CA 1000 C C . PRO A 129 ? 0.7018 0.6684 0.4555 0.0596 0.0720 -0.1349 170 PRO A C 1001 O O . PRO A 129 ? 0.6704 0.6411 0.4450 0.0585 0.0743 -0.1371 170 PRO A O 1002 C CB . PRO A 129 ? 0.6601 0.6310 0.4257 0.0500 0.0638 -0.1186 170 PRO A CB 1003 C CG . PRO A 129 ? 0.6258 0.6014 0.4195 0.0455 0.0601 -0.1180 170 PRO A CG 1004 C CD . PRO A 129 ? 0.6219 0.5919 0.4183 0.0465 0.0486 -0.1273 170 PRO A CD 1005 N N . GLU A 130 ? 0.7320 0.6956 0.4615 0.0646 0.0797 -0.1355 171 GLU A N 1006 C CA . GLU A 130 ? 0.7620 0.7273 0.4875 0.0695 0.0921 -0.1396 171 GLU A CA 1007 C C . GLU A 130 ? 0.7734 0.7411 0.4846 0.0704 0.1051 -0.1307 171 GLU A C 1008 O O . GLU A 130 ? 0.8039 0.7666 0.4934 0.0714 0.1030 -0.1269 171 GLU A O 1009 C CB . GLU A 130 ? 0.7860 0.7426 0.4924 0.0763 0.0874 -0.1524 171 GLU A CB 1010 C CG . GLU A 130 ? 0.8609 0.8172 0.5544 0.0829 0.1004 -0.1570 171 GLU A CG 1011 C CD . GLU A 130 ? 0.9503 0.8964 0.6150 0.0903 0.0955 -0.1676 171 GLU A CD 1012 O OE1 . GLU A 130 ? 0.9715 0.9116 0.6371 0.0905 0.0812 -0.1759 171 GLU A OE1 1013 O OE2 . GLU A 130 ? 0.9951 0.9389 0.6363 0.0960 0.1059 -0.1675 171 GLU A OE2 1014 N N . GLY A 131 ? 0.7567 0.7320 0.4809 0.0699 0.1185 -0.1269 172 GLY A N 1015 C CA . GLY A 131 ? 0.7500 0.7285 0.4656 0.0695 0.1313 -0.1171 172 GLY A CA 1016 C C . GLY A 131 ? 0.7371 0.7245 0.4697 0.0695 0.1461 -0.1147 172 GLY A C 1017 O O . GLY A 131 ? 0.7261 0.7170 0.4752 0.0708 0.1470 -0.1215 172 GLY A O 1018 N N . ASP A 132 ? 0.7318 0.7229 0.4614 0.0680 0.1576 -0.1049 173 ASP A N 1019 C CA . ASP A 132 ? 0.7229 0.7236 0.4718 0.0669 0.1719 -0.1010 173 ASP A CA 1020 C C . ASP A 132 ? 0.6837 0.6924 0.4626 0.0594 0.1684 -0.0940 173 ASP A C 1021 O O . ASP A 132 ? 0.6679 0.6748 0.4464 0.0548 0.1605 -0.0876 173 ASP A O 1022 C CB . ASP A 132 ? 0.7506 0.7510 0.4819 0.0689 0.1869 -0.0937 173 ASP A CB 1023 C CG . ASP A 132 ? 0.8298 0.8220 0.5289 0.0773 0.1915 -0.1005 173 ASP A CG 1024 O OD1 . ASP A 132 ? 0.8709 0.8624 0.5708 0.0820 0.1912 -0.1113 173 ASP A OD1 1025 O OD2 . ASP A 132 ? 0.8733 0.8592 0.5460 0.0793 0.1953 -0.0951 173 ASP A OD2 1026 N N . LEU A 133 ? 0.6556 0.6730 0.4601 0.0586 0.1742 -0.0954 174 LEU A N 1027 C CA . LEU A 133 ? 0.6230 0.6482 0.4563 0.0524 0.1713 -0.0898 174 LEU A CA 1028 C C . LEU A 133 ? 0.6197 0.6509 0.4601 0.0487 0.1820 -0.0789 174 LEU A C 1029 O O . LEU A 133 ? 0.6357 0.6691 0.4699 0.0512 0.1962 -0.0770 174 LEU A O 1030 C CB . LEU A 133 ? 0.6164 0.6481 0.4739 0.0539 0.1727 -0.0962 174 LEU A CB 1031 C CG A LEU A 133 ? 0.5885 0.6238 0.4717 0.0503 0.1622 -0.0971 174 LEU A CG 1032 C CG B LEU A 133 ? 0.5863 0.6134 0.4465 0.0562 0.1611 -0.1060 174 LEU A CG 1033 C CD1 A LEU A 133 ? 0.5548 0.5832 0.4315 0.0475 0.1470 -0.0971 174 LEU A CD1 1034 C CD1 B LEU A 133 ? 0.5423 0.5761 0.4265 0.0579 0.1647 -0.1109 174 LEU A CD1 1035 C CD2 A LEU A 133 ? 0.5780 0.6152 0.4734 0.0546 0.1631 -0.1064 174 LEU A CD2 1036 C CD2 B LEU A 133 ? 0.5485 0.5725 0.4140 0.0513 0.1464 -0.1035 174 LEU A CD2 1037 N N . VAL A 134 ? 0.5956 0.6291 0.4498 0.0426 0.1755 -0.0720 175 VAL A N 1038 C CA . VAL A 134 ? 0.5844 0.6253 0.4548 0.0383 0.1843 -0.0628 175 VAL A CA 1039 C C . VAL A 134 ? 0.5578 0.6058 0.4587 0.0341 0.1771 -0.0627 175 VAL A C 1040 O O . VAL A 134 ? 0.5332 0.5779 0.4363 0.0324 0.1636 -0.0645 175 VAL A O 1041 C CB . VAL A 134 ? 0.6038 0.6397 0.4591 0.0350 0.1838 -0.0533 175 VAL A CB 1042 C CG1 . VAL A 134 ? 0.5819 0.6251 0.4587 0.0294 0.1898 -0.0441 175 VAL A CG1 1043 C CG2 . VAL A 134 ? 0.6088 0.6381 0.4343 0.0396 0.1927 -0.0524 175 VAL A CG2 1044 N N . TYR A 135 ? 0.5356 0.5930 0.4596 0.0329 0.1860 -0.0607 176 TYR A N 1045 C CA . TYR A 135 ? 0.5114 0.5758 0.4644 0.0297 0.1797 -0.0607 176 TYR A CA 1046 C C . TYR A 135 ? 0.5059 0.5727 0.4687 0.0237 0.1787 -0.0514 176 TYR A C 1047 O O . TYR A 135 ? 0.5077 0.5772 0.4710 0.0221 0.1898 -0.0452 176 TYR A O 1048 C CB . TYR A 135 ? 0.5196 0.5931 0.4941 0.0322 0.1885 -0.0648 176 TYR A CB 1049 C CG . TYR A 135 ? 0.4868 0.5684 0.4923 0.0289 0.1835 -0.0636 176 TYR A CG 1050 C CD1 . TYR A 135 ? 0.4680 0.5477 0.4812 0.0284 0.1697 -0.0669 176 TYR A CD1 1051 C CD2 . TYR A 135 ? 0.4963 0.5874 0.5236 0.0264 0.1928 -0.0590 176 TYR A CD2 1052 C CE1 . TYR A 135 ? 0.4510 0.5375 0.4910 0.0261 0.1644 -0.0658 176 TYR A CE1 1053 C CE2 . TYR A 135 ? 0.4588 0.5571 0.5146 0.0237 0.1869 -0.0583 176 TYR A CE2 1054 C CZ . TYR A 135 ? 0.4222 0.5180 0.4831 0.0239 0.1726 -0.0619 176 TYR A CZ 1055 O OH . TYR A 135 ? 0.4423 0.5446 0.5294 0.0221 0.1665 -0.0615 176 TYR A OH 1056 N N . VAL A 136 ? 0.4807 0.5461 0.4511 0.0205 0.1657 -0.0505 177 VAL A N 1057 C CA . VAL A 136 ? 0.4877 0.5531 0.4630 0.0152 0.1627 -0.0422 177 VAL A CA 1058 C C . VAL A 136 ? 0.4663 0.5388 0.4700 0.0121 0.1571 -0.0415 177 VAL A C 1059 O O . VAL A 136 ? 0.4491 0.5203 0.4575 0.0082 0.1495 -0.0370 177 VAL A O 1060 C CB . VAL A 136 ? 0.4847 0.5407 0.4387 0.0142 0.1525 -0.0404 177 VAL A CB 1061 C CG1 . VAL A 136 ? 0.5146 0.5635 0.4402 0.0176 0.1577 -0.0410 177 VAL A CG1 1062 C CG2 . VAL A 136 ? 0.4949 0.5482 0.4510 0.0152 0.1394 -0.0463 177 VAL A CG2 1063 N N . ASN A 137 ? 0.4529 0.5325 0.4753 0.0143 0.1605 -0.0463 178 ASN A N 1064 C CA . ASN A 137 ? 0.4450 0.5313 0.4943 0.0124 0.1548 -0.0465 178 ASN A CA 1065 C C . ASN A 137 ? 0.4238 0.5049 0.4706 0.0117 0.1396 -0.0479 178 ASN A C 1066 O O . ASN A 137 ? 0.4144 0.4904 0.4497 0.0148 0.1344 -0.0530 178 ASN A O 1067 C CB . ASN A 137 ? 0.4400 0.5322 0.5057 0.0078 0.1606 -0.0396 178 ASN A CB 1068 C CG . ASN A 137 ? 0.4401 0.5412 0.5364 0.0069 0.1574 -0.0412 178 ASN A CG 1069 O OD1 . ASN A 137 ? 0.4358 0.5408 0.5432 0.0104 0.1559 -0.0473 178 ASN A OD1 1070 N ND2 . ASN A 137 ? 0.4394 0.5437 0.5502 0.0023 0.1564 -0.0359 178 ASN A ND2 1071 N N . TYR A 138 ? 0.4049 0.4871 0.4625 0.0079 0.1329 -0.0436 179 TYR A N 1072 C CA . TYR A 138 ? 0.3943 0.4715 0.4485 0.0074 0.1195 -0.0442 179 TYR A CA 1073 C C . TYR A 138 ? 0.3978 0.4665 0.4296 0.0058 0.1151 -0.0409 179 TYR A C 1074 O O . TYR A 138 ? 0.3908 0.4552 0.4190 0.0051 0.1048 -0.0408 179 TYR A O 1075 C CB . TYR A 138 ? 0.3786 0.4602 0.4535 0.0048 0.1133 -0.0418 179 TYR A CB 1076 C CG . TYR A 138 ? 0.3865 0.4761 0.4849 0.0069 0.1141 -0.0457 179 TYR A CG 1077 C CD1 . TYR A 138 ? 0.3912 0.4800 0.4936 0.0106 0.1073 -0.0510 179 TYR A CD1 1078 C CD2 . TYR A 138 ? 0.3829 0.4808 0.5012 0.0050 0.1213 -0.0437 179 TYR A CD2 1079 C CE1 . TYR A 138 ? 0.3822 0.4780 0.5063 0.0130 0.1070 -0.0545 179 TYR A CE1 1080 C CE2 . TYR A 138 ? 0.4064 0.5122 0.5482 0.0071 0.1210 -0.0476 179 TYR A CE2 1081 C CZ . TYR A 138 ? 0.3974 0.5019 0.5414 0.0113 0.1135 -0.0530 179 TYR A CZ 1082 O OH . TYR A 138 ? 0.3923 0.5039 0.5587 0.0140 0.1123 -0.0570 179 TYR A OH 1083 N N . ALA A 139 ? 0.4197 0.4859 0.4362 0.0054 0.1231 -0.0381 180 ALA A N 1084 C CA . ALA A 139 ? 0.4107 0.4690 0.4054 0.0043 0.1196 -0.0349 180 ALA A CA 1085 C C . ALA A 139 ? 0.4082 0.4655 0.4085 0.0002 0.1129 -0.0292 180 ALA A C 1086 O O . ALA A 139 ? 0.3865 0.4375 0.3741 -0.0004 0.1052 -0.0279 180 ALA A O 1087 C CB . ALA A 139 ? 0.4164 0.4683 0.3958 0.0073 0.1121 -0.0404 180 ALA A CB 1088 N N . ARG A 140 ? 0.4018 0.4652 0.4218 -0.0023 0.1158 -0.0261 181 ARG A N 1089 C CA . ARG A 140 ? 0.3964 0.4586 0.4227 -0.0061 0.1100 -0.0211 181 ARG A CA 1090 C C . ARG A 140 ? 0.4071 0.4651 0.4201 -0.0084 0.1155 -0.0144 181 ARG A C 1091 O O . ARG A 140 ? 0.4190 0.4764 0.4217 -0.0073 0.1253 -0.0133 181 ARG A O 1092 C CB . ARG A 140 ? 0.3832 0.4531 0.4357 -0.0079 0.1104 -0.0208 181 ARG A CB 1093 C CG . ARG A 140 ? 0.3742 0.4475 0.4396 -0.0053 0.1034 -0.0267 181 ARG A CG 1094 C CD . ARG A 140 ? 0.4061 0.4877 0.4976 -0.0062 0.1051 -0.0273 181 ARG A CD 1095 N NE . ARG A 140 ? 0.3940 0.4813 0.4925 -0.0064 0.1179 -0.0268 181 ARG A NE 1096 C CZ . ARG A 140 ? 0.4139 0.5097 0.5364 -0.0072 0.1224 -0.0273 181 ARG A CZ 1097 N NH1 . ARG A 140 ? 0.4004 0.4999 0.5424 -0.0078 0.1141 -0.0289 181 ARG A NH1 1098 N NH2 . ARG A 140 ? 0.3886 0.4890 0.5154 -0.0071 0.1352 -0.0264 181 ARG A NH2 1099 N N . THR A 141 ? 0.4036 0.4580 0.4159 -0.0113 0.1095 -0.0100 182 THR A N 1100 C CA . THR A 141 ? 0.4237 0.4738 0.4255 -0.0136 0.1145 -0.0029 182 THR A CA 1101 C C . THR A 141 ? 0.4361 0.4909 0.4482 -0.0152 0.1275 0.0006 182 THR A C 1102 O O . THR A 141 ? 0.4521 0.5037 0.4493 -0.0147 0.1364 0.0045 182 THR A O 1103 C CB . THR A 141 ? 0.4324 0.4794 0.4387 -0.0167 0.1063 0.0010 182 THR A CB 1104 O OG1 . THR A 141 ? 0.4118 0.4543 0.4072 -0.0149 0.0958 -0.0020 182 THR A OG1 1105 C CG2 . THR A 141 ? 0.4483 0.4900 0.4440 -0.0190 0.1112 0.0086 182 THR A CG2 1106 N N . GLU A 142 ? 0.4299 0.4925 0.4674 -0.0169 0.1289 -0.0005 183 GLU A N 1107 C CA . GLU A 142 ? 0.4582 0.5262 0.5090 -0.0189 0.1416 0.0031 183 GLU A CA 1108 C C . GLU A 142 ? 0.4602 0.5312 0.5045 -0.0154 0.1524 0.0002 183 GLU A C 1109 O O . GLU A 142 ? 0.4630 0.5354 0.5072 -0.0162 0.1651 0.0046 183 GLU A O 1110 C CB . GLU A 142 ? 0.4637 0.5397 0.5454 -0.0215 0.1395 0.0020 183 GLU A CB 1111 C CG . GLU A 142 ? 0.4899 0.5717 0.5841 -0.0185 0.1330 -0.0060 183 GLU A CG 1112 C CD . GLU A 142 ? 0.5443 0.6230 0.6391 -0.0181 0.1179 -0.0088 183 GLU A CD 1113 O OE1 . GLU A 142 ? 0.5069 0.5778 0.5832 -0.0181 0.1114 -0.0070 183 GLU A OE1 1114 O OE2 . GLU A 142 ? 0.5371 0.6214 0.6513 -0.0175 0.1126 -0.0128 183 GLU A OE2 1115 N N . ASP A 143 ? 0.4534 0.5249 0.4922 -0.0113 0.1478 -0.0071 184 ASP A N 1116 C CA . ASP A 143 ? 0.4702 0.5435 0.5006 -0.0073 0.1576 -0.0108 184 ASP A CA 1117 C C . ASP A 143 ? 0.4841 0.5492 0.4849 -0.0056 0.1632 -0.0073 184 ASP A C 1118 O O . ASP A 143 ? 0.4908 0.5568 0.4851 -0.0041 0.1757 -0.0058 184 ASP A O 1119 C CB . ASP A 143 ? 0.4598 0.5342 0.4905 -0.0032 0.1506 -0.0195 184 ASP A CB 1120 C CG . ASP A 143 ? 0.4359 0.5178 0.4937 -0.0038 0.1451 -0.0230 184 ASP A CG 1121 O OD1 . ASP A 143 ? 0.4382 0.5278 0.5179 -0.0057 0.1516 -0.0213 184 ASP A OD1 1122 O OD2 . ASP A 143 ? 0.4174 0.4974 0.4751 -0.0022 0.1341 -0.0274 184 ASP A OD2 1123 N N . PHE A 144 ? 0.4871 0.5441 0.4699 -0.0057 0.1536 -0.0062 185 PHE A N 1124 C CA . PHE A 144 ? 0.5015 0.5500 0.4560 -0.0040 0.1568 -0.0029 185 PHE A CA 1125 C C . PHE A 144 ? 0.5285 0.5751 0.4809 -0.0070 0.1663 0.0065 185 PHE A C 1126 O O . PHE A 144 ? 0.5430 0.5852 0.4755 -0.0047 0.1755 0.0096 185 PHE A O 1127 C CB . PHE A 144 ? 0.4979 0.5388 0.4359 -0.0032 0.1435 -0.0045 185 PHE A CB 1128 C CG . PHE A 144 ? 0.4703 0.5100 0.3995 0.0009 0.1378 -0.0132 185 PHE A CG 1129 C CD1 . PHE A 144 ? 0.4498 0.4922 0.3926 0.0007 0.1280 -0.0184 185 PHE A CD1 1130 C CD2 . PHE A 144 ? 0.4902 0.5256 0.3976 0.0052 0.1428 -0.0162 185 PHE A CD2 1131 C CE1 . PHE A 144 ? 0.4801 0.5208 0.4162 0.0043 0.1232 -0.0261 185 PHE A CE1 1132 C CE2 . PHE A 144 ? 0.4784 0.5123 0.3790 0.0091 0.1374 -0.0248 185 PHE A CE2 1133 C CZ . PHE A 144 ? 0.4720 0.5086 0.3879 0.0084 0.1277 -0.0296 185 PHE A CZ 1134 N N . PHE A 145 ? 0.5237 0.5732 0.4963 -0.0118 0.1644 0.0111 186 PHE A N 1135 C CA . PHE A 145 ? 0.5439 0.5921 0.5193 -0.0152 0.1740 0.0205 186 PHE A CA 1136 C C . PHE A 145 ? 0.5706 0.6247 0.5531 -0.0144 0.1904 0.0217 186 PHE A C 1137 O O . PHE A 145 ? 0.5900 0.6398 0.5579 -0.0139 0.2016 0.0281 186 PHE A O 1138 C CB . PHE A 145 ? 0.5317 0.5832 0.5322 -0.0206 0.1689 0.0238 186 PHE A CB 1139 C CG . PHE A 145 ? 0.5349 0.5792 0.5273 -0.0221 0.1563 0.0258 186 PHE A CG 1140 C CD1 . PHE A 145 ? 0.5723 0.6075 0.5366 -0.0195 0.1518 0.0269 186 PHE A CD1 1141 C CD2 . PHE A 145 ? 0.5404 0.5872 0.5541 -0.0259 0.1486 0.0264 186 PHE A CD2 1142 C CE1 . PHE A 145 ? 0.5733 0.6024 0.5318 -0.0207 0.1403 0.0287 186 PHE A CE1 1143 C CE2 . PHE A 145 ? 0.4937 0.5339 0.5004 -0.0270 0.1372 0.0281 186 PHE A CE2 1144 C CZ . PHE A 145 ? 0.5281 0.5598 0.5077 -0.0244 0.1335 0.0294 186 PHE A CZ 1145 N N . LYS A 146 ? 0.5735 0.6372 0.5786 -0.0140 0.1917 0.0157 187 LYS A N 1146 C CA . LYS A 146 ? 0.5928 0.6639 0.6091 -0.0129 0.2069 0.0155 187 LYS A CA 1147 C C . LYS A 146 ? 0.6198 0.6866 0.6085 -0.0074 0.2160 0.0140 187 LYS A C 1148 O O . LYS A 146 ? 0.6356 0.7026 0.6196 -0.0070 0.2310 0.0192 187 LYS A O 1149 C CB . LYS A 146 ? 0.5828 0.6644 0.6269 -0.0125 0.2035 0.0079 187 LYS A CB 1150 C CG . LYS A 146 ? 0.6270 0.7180 0.6874 -0.0111 0.2184 0.0064 187 LYS A CG 1151 C CD . LYS A 146 ? 0.7050 0.8040 0.7967 -0.0163 0.2255 0.0117 187 LYS A CD 1152 C CE . LYS A 146 ? 0.7204 0.8272 0.8423 -0.0181 0.2140 0.0061 187 LYS A CE 1153 N NZ . LYS A 146 ? 0.7471 0.8585 0.8966 -0.0241 0.2145 0.0113 187 LYS A NZ 1154 N N . LEU A 147 ? 0.6242 0.6867 0.5950 -0.0032 0.2069 0.0068 188 LEU A N 1155 C CA . LEU A 147 ? 0.6579 0.7152 0.6012 0.0025 0.2128 0.0038 188 LEU A CA 1156 C C . LEU A 147 ? 0.6826 0.7305 0.5992 0.0029 0.2184 0.0118 188 LEU A C 1157 O O . LEU A 147 ? 0.6824 0.7291 0.5862 0.0057 0.2325 0.0146 188 LEU A O 1158 C CB . LEU A 147 ? 0.6598 0.7127 0.5894 0.0060 0.1991 -0.0047 188 LEU A CB 1159 C CG . LEU A 147 ? 0.6861 0.7441 0.6236 0.0098 0.1979 -0.0147 188 LEU A CG 1160 C CD1 . LEU A 147 ? 0.7306 0.7817 0.6522 0.0122 0.1835 -0.0208 188 LEU A CD1 1161 C CD2 . LEU A 147 ? 0.7034 0.7622 0.6299 0.0146 0.2120 -0.0169 188 LEU A CD2 1162 N N . GLU A 148 ? 0.6765 0.7176 0.5848 0.0004 0.2075 0.0157 189 GLU A N 1163 C CA . GLU A 148 ? 0.7220 0.7522 0.6008 0.0019 0.2084 0.0219 189 GLU A CA 1164 C C . GLU A 148 ? 0.7342 0.7632 0.6172 -0.0017 0.2202 0.0335 189 GLU A C 1165 O O . GLU A 148 ? 0.7648 0.7877 0.6256 0.0009 0.2309 0.0389 189 GLU A O 1166 C CB . GLU A 148 ? 0.7274 0.7509 0.5955 0.0015 0.1911 0.0202 189 GLU A CB 1167 C CG . GLU A 148 ? 0.7861 0.8098 0.6481 0.0054 0.1805 0.0090 189 GLU A CG 1168 C CD . GLU A 148 ? 0.8455 0.8636 0.7002 0.0048 0.1639 0.0072 189 GLU A CD 1169 O OE1 . GLU A 148 ? 0.8622 0.8830 0.7353 0.0006 0.1563 0.0088 189 GLU A OE1 1170 O OE2 . GLU A 148 ? 0.8945 0.9056 0.7250 0.0088 0.1585 0.0038 189 GLU A OE2 1171 N N . ARG A 149 ? 0.7148 0.7493 0.6264 -0.0076 0.2186 0.0370 190 ARG A N 1172 C CA . ARG A 149 ? 0.7273 0.7603 0.6467 -0.0120 0.2279 0.0481 190 ARG A CA 1173 C C . ARG A 149 ? 0.7443 0.7853 0.6810 -0.0131 0.2458 0.0509 190 ARG A C 1174 O O . ARG A 149 ? 0.7674 0.8045 0.6961 -0.0137 0.2590 0.0601 190 ARG A O 1175 C CB . ARG A 149 ? 0.7030 0.7371 0.6444 -0.0179 0.2169 0.0505 190 ARG A CB 1176 C CG . ARG A 149 ? 0.6809 0.7065 0.6049 -0.0171 0.2009 0.0492 190 ARG A CG 1177 C CD . ARG A 149 ? 0.6558 0.6837 0.6028 -0.0220 0.1895 0.0495 190 ARG A CD 1178 N NE . ARG A 149 ? 0.6602 0.6797 0.5903 -0.0212 0.1760 0.0495 190 ARG A NE 1179 C CZ . ARG A 149 ? 0.6575 0.6757 0.5998 -0.0248 0.1661 0.0512 190 ARG A CZ 1180 N NH1 . ARG A 149 ? 0.6057 0.6299 0.5767 -0.0294 0.1673 0.0526 190 ARG A NH1 1181 N NH2 . ARG A 149 ? 0.6371 0.6479 0.5635 -0.0235 0.1547 0.0512 190 ARG A NH2 1182 N N . ASP A 150 ? 0.7355 0.7874 0.6960 -0.0129 0.2465 0.0434 191 ASP A N 1183 C CA . ASP A 150 ? 0.7473 0.8085 0.7294 -0.0141 0.2628 0.0453 191 ASP A CA 1184 C C . ASP A 150 ? 0.7553 0.8177 0.7208 -0.0078 0.2748 0.0412 191 ASP A C 1185 O O . ASP A 150 ? 0.7643 0.8279 0.7286 -0.0073 0.2922 0.0471 191 ASP A O 1186 C CB . ASP A 150 ? 0.7334 0.8067 0.7545 -0.0176 0.2574 0.0398 191 ASP A CB 1187 C CG . ASP A 150 ? 0.7607 0.8331 0.7997 -0.0236 0.2463 0.0434 191 ASP A CG 1188 O OD1 . ASP A 150 ? 0.8116 0.8771 0.8435 -0.0267 0.2493 0.0526 191 ASP A OD1 1189 O OD2 . ASP A 150 ? 0.7892 0.8674 0.8485 -0.0249 0.2343 0.0368 191 ASP A OD2 1190 N N . MET A 151 ? 0.7378 0.7997 0.6912 -0.0029 0.2659 0.0312 192 MET A N 1191 C CA . MET A 151 ? 0.7510 0.8141 0.6902 0.0034 0.2756 0.0256 192 MET A CA 1192 C C . MET A 151 ? 0.7721 0.8229 0.6692 0.0087 0.2777 0.0273 192 MET A C 1193 O O . MET A 151 ? 0.7739 0.8240 0.6547 0.0144 0.2890 0.0248 192 MET A O 1194 C CB . MET A 151 ? 0.7349 0.8038 0.6847 0.0063 0.2657 0.0133 192 MET A CB 1195 C CG . MET A 151 ? 0.7221 0.8037 0.7124 0.0026 0.2648 0.0105 192 MET A CG 1196 S SD . MET A 151 ? 0.7235 0.8094 0.7214 0.0067 0.2521 -0.0030 192 MET A SD 1197 C CE . MET A 151 ? 0.7176 0.8093 0.7142 0.0127 0.2700 -0.0076 192 MET A CE 1198 N N . LYS A 152 ? 0.7605 0.8017 0.6407 0.0073 0.2667 0.0315 193 LYS A N 1199 C CA . LYS A 152 ? 0.7935 0.8220 0.6337 0.0121 0.2651 0.0334 193 LYS A CA 1200 C C . LYS A 152 ? 0.7992 0.8252 0.6194 0.0189 0.2593 0.0221 193 LYS A C 1201 O O . LYS A 152 ? 0.8245 0.8435 0.6145 0.0249 0.2659 0.0217 193 LYS A O 1202 C CB . LYS A 152 ? 0.8331 0.8566 0.6564 0.0135 0.2832 0.0437 193 LYS A CB 1203 C CG . LYS A 152 ? 0.8659 0.8845 0.6928 0.0079 0.2838 0.0559 193 LYS A CG 1204 C CD . LYS A 152 ? 0.8736 0.9028 0.7415 0.0006 0.2889 0.0599 193 LYS A CD 1205 C CE . LYS A 152 ? 0.9017 0.9257 0.7714 -0.0039 0.2972 0.0736 193 LYS A CE 1206 N NZ . LYS A 152 ? 0.8931 0.9085 0.7545 -0.0064 0.2815 0.0768 193 LYS A NZ 1207 N N . ILE A 153 ? 0.7710 0.8025 0.6083 0.0182 0.2470 0.0130 194 ILE A N 1208 C CA . ILE A 153 ? 0.7834 0.8125 0.6061 0.0238 0.2392 0.0018 194 ILE A CA 1209 C C . ILE A 153 ? 0.7867 0.8074 0.5935 0.0238 0.2215 0.0000 194 ILE A C 1210 O O . ILE A 153 ? 0.7709 0.7932 0.5937 0.0187 0.2110 0.0021 194 ILE A O 1211 C CB . ILE A 153 ? 0.7633 0.8031 0.6137 0.0238 0.2379 -0.0071 194 ILE A CB 1212 C CG1 . ILE A 153 ? 0.7869 0.8331 0.6429 0.0269 0.2560 -0.0079 194 ILE A CG1 1213 C CG2 . ILE A 153 ? 0.7623 0.7986 0.6019 0.0280 0.2249 -0.0183 194 ILE A CG2 1214 C CD1 . ILE A 153 ? 0.7592 0.8184 0.6527 0.0244 0.2593 -0.0112 194 ILE A CD1 1215 N N . ASN A 154 ? 0.8167 0.8284 0.5919 0.0295 0.2185 -0.0037 195 ASN A N 1216 C CA . ASN A 154 ? 0.8348 0.8380 0.5929 0.0300 0.2024 -0.0053 195 ASN A CA 1217 C C . ASN A 154 ? 0.8106 0.8151 0.5733 0.0320 0.1895 -0.0174 195 ASN A C 1218 O O . ASN A 154 ? 0.8028 0.8064 0.5543 0.0375 0.1923 -0.0255 195 ASN A O 1219 C CB . ASN A 154 ? 0.8852 0.8772 0.6059 0.0352 0.2057 -0.0018 195 ASN A CB 1220 C CG . ASN A 154 ? 0.9612 0.9442 0.6643 0.0357 0.1895 -0.0022 195 ASN A CG 1221 O OD1 . ASN A 154 ? 0.9579 0.9433 0.6774 0.0317 0.1766 -0.0040 195 ASN A OD1 1222 N ND2 . ASN A 154 ? 1.1124 1.0851 0.7817 0.0410 0.1901 -0.0005 195 ASN A ND2 1223 N N . CYS A 155 ? 0.7675 0.7742 0.5472 0.0277 0.1761 -0.0184 196 CYS A N 1224 C CA . CYS A 155 ? 0.7539 0.7612 0.5392 0.0291 0.1638 -0.0287 196 CYS A CA 1225 C C . CYS A 155 ? 0.7596 0.7575 0.5201 0.0326 0.1521 -0.0334 196 CYS A C 1226 O O . CYS A 155 ? 0.7538 0.7514 0.5175 0.0340 0.1424 -0.0421 196 CYS A O 1227 C CB . CYS A 155 ? 0.7231 0.7366 0.5371 0.0236 0.1550 -0.0284 196 CYS A CB 1228 S SG . CYS A 155 ? 0.7345 0.7600 0.5806 0.0210 0.1652 -0.0279 196 CYS A SG 1229 N N . SER A 156 ? 0.7743 0.7644 0.5107 0.0342 0.1528 -0.0277 197 SER A N 1230 C CA . SER A 156 ? 0.7827 0.7640 0.4965 0.0375 0.1404 -0.0319 197 SER A CA 1231 C C . SER A 156 ? 0.7847 0.7629 0.4839 0.0438 0.1390 -0.0432 197 SER A C 1232 O O . SER A 156 ? 0.8089 0.7863 0.4956 0.0481 0.1506 -0.0446 197 SER A O 1233 C CB . SER A 156 ? 0.8099 0.7829 0.4993 0.0388 0.1419 -0.0234 197 SER A CB 1234 O OG . SER A 156 ? 0.8434 0.8082 0.5120 0.0424 0.1289 -0.0281 197 SER A OG 1235 N N . GLY A 157 ? 0.7578 0.7342 0.4598 0.0442 0.1250 -0.0513 198 GLY A N 1236 C CA . GLY A 157 ? 0.7494 0.7222 0.4395 0.0498 0.1217 -0.0629 198 GLY A CA 1237 C C . GLY A 157 ? 0.7326 0.7121 0.4400 0.0507 0.1288 -0.0694 198 GLY A C 1238 O O . GLY A 157 ? 0.7398 0.7162 0.4378 0.0557 0.1274 -0.0791 198 GLY A O 1239 N N . LYS A 158 ? 0.7083 0.6968 0.4416 0.0461 0.1357 -0.0645 199 LYS A N 1240 C CA . LYS A 158 ? 0.6860 0.6815 0.4386 0.0468 0.1420 -0.0702 199 LYS A CA 1241 C C . LYS A 158 ? 0.6538 0.6525 0.4295 0.0436 0.1305 -0.0747 199 LYS A C 1242 O O . LYS A 158 ? 0.6250 0.6225 0.4057 0.0397 0.1203 -0.0714 199 LYS A O 1243 C CB . LYS A 158 ? 0.6832 0.6870 0.4530 0.0438 0.1557 -0.0624 199 LYS A CB 1244 C CG . LYS A 158 ? 0.7356 0.7369 0.4871 0.0452 0.1681 -0.0545 199 LYS A CG 1245 C CD . LYS A 158 ? 0.8071 0.8031 0.5328 0.0526 0.1755 -0.0599 199 LYS A CD 1246 C CE . LYS A 158 ? 0.8516 0.8442 0.5580 0.0538 0.1880 -0.0506 199 LYS A CE 1247 N NZ . LYS A 158 ? 0.8963 0.8802 0.5694 0.0617 0.1903 -0.0561 199 LYS A NZ 1248 N N . ILE A 159 ? 0.6383 0.6406 0.4273 0.0455 0.1323 -0.0822 200 ILE A N 1249 C CA . ILE A 159 ? 0.6136 0.6203 0.4284 0.0422 0.1245 -0.0846 200 ILE A CA 1250 C C . ILE A 159 ? 0.5894 0.6056 0.4280 0.0387 0.1325 -0.0785 200 ILE A C 1251 O O . ILE A 159 ? 0.6055 0.6262 0.4475 0.0408 0.1446 -0.0786 200 ILE A O 1252 C CB . ILE A 159 ? 0.6120 0.6169 0.4298 0.0462 0.1213 -0.0957 200 ILE A CB 1253 C CG1 . ILE A 159 ? 0.6465 0.6419 0.4425 0.0492 0.1115 -0.1020 200 ILE A CG1 1254 C CG2 . ILE A 159 ? 0.5942 0.6034 0.4387 0.0430 0.1146 -0.0969 200 ILE A CG2 1255 C CD1 . ILE A 159 ? 0.6638 0.6555 0.4584 0.0537 0.1084 -0.1136 200 ILE A CD1 1256 N N . VAL A 160 ? 0.5566 0.5759 0.4118 0.0336 0.1261 -0.0733 201 VAL A N 1257 C CA . VAL A 160 ? 0.5434 0.5714 0.4215 0.0303 0.1324 -0.0679 201 VAL A CA 1258 C C . VAL A 160 ? 0.5202 0.5526 0.4201 0.0309 0.1290 -0.0737 201 VAL A C 1259 O O . VAL A 160 ? 0.5094 0.5381 0.4110 0.0309 0.1184 -0.0778 201 VAL A O 1260 C CB . VAL A 160 ? 0.5456 0.5743 0.4287 0.0248 0.1282 -0.0588 201 VAL A CB 1261 C CG1 A VAL A 160 ? 0.5622 0.5865 0.4246 0.0248 0.1333 -0.0526 201 VAL A CG1 1262 C CG1 B VAL A 160 ? 0.4924 0.5274 0.4021 0.0212 0.1240 -0.0569 201 VAL A CG1 1263 C CG2 A VAL A 160 ? 0.5130 0.5381 0.3983 0.0229 0.1145 -0.0600 201 VAL A CG2 1264 C CG2 B VAL A 160 ? 0.5668 0.5957 0.4403 0.0239 0.1385 -0.0511 201 VAL A CG2 1265 N N . ILE A 161 ? 0.5041 0.5441 0.4208 0.0315 0.1378 -0.0737 202 ILE A N 1266 C CA . ILE A 161 ? 0.4722 0.5169 0.4118 0.0317 0.1341 -0.0775 202 ILE A CA 1267 C C . ILE A 161 ? 0.4639 0.5163 0.4252 0.0276 0.1355 -0.0709 202 ILE A C 1268 O O . ILE A 161 ? 0.4676 0.5251 0.4333 0.0264 0.1453 -0.0663 202 ILE A O 1269 C CB . ILE A 161 ? 0.4923 0.5391 0.4358 0.0369 0.1409 -0.0853 202 ILE A CB 1270 C CG1 . ILE A 161 ? 0.4590 0.5100 0.4263 0.0373 0.1362 -0.0887 202 ILE A CG1 1271 C CG2 . ILE A 161 ? 0.4934 0.5459 0.4367 0.0384 0.1561 -0.0832 202 ILE A CG2 1272 C CD1 . ILE A 161 ? 0.4644 0.5136 0.4310 0.0432 0.1386 -0.0984 202 ILE A CD1 1273 N N . ALA A 162 ? 0.4266 0.4792 0.4004 0.0253 0.1254 -0.0702 203 ALA A N 1274 C CA . ALA A 162 ? 0.4149 0.4735 0.4076 0.0216 0.1245 -0.0645 203 ALA A CA 1275 C C . ALA A 162 ? 0.4026 0.4644 0.4147 0.0229 0.1187 -0.0681 203 ALA A C 1276 O O . ALA A 162 ? 0.4111 0.4677 0.4192 0.0248 0.1114 -0.0726 203 ALA A O 1277 C CB . ALA A 162 ? 0.4019 0.4564 0.3875 0.0175 0.1165 -0.0586 203 ALA A CB 1278 N N . ARG A 163 ? 0.3894 0.4589 0.4226 0.0217 0.1211 -0.0659 204 ARG A N 1279 C CA . ARG A 163 ? 0.3827 0.4547 0.4338 0.0228 0.1139 -0.0681 204 ARG A CA 1280 C C . ARG A 163 ? 0.3695 0.4389 0.4228 0.0197 0.1035 -0.0640 204 ARG A C 1281 O O . ARG A 163 ? 0.3542 0.4239 0.4052 0.0160 0.1031 -0.0584 204 ARG A O 1282 C CB . ARG A 163 ? 0.4006 0.4821 0.4748 0.0240 0.1199 -0.0692 204 ARG A CB 1283 C CG . ARG A 163 ? 0.4146 0.5027 0.4979 0.0204 0.1268 -0.0636 204 ARG A CG 1284 C CD . ARG A 163 ? 0.4561 0.5540 0.5657 0.0218 0.1309 -0.0655 204 ARG A CD 1285 N NE . ARG A 163 ? 0.4518 0.5566 0.5727 0.0183 0.1391 -0.0605 204 ARG A NE 1286 C CZ . ARG A 163 ? 0.4565 0.5705 0.6035 0.0179 0.1410 -0.0606 204 ARG A CZ 1287 N NH1 . ARG A 163 ? 0.4358 0.5530 0.5989 0.0210 0.1344 -0.0652 204 ARG A NH1 1288 N NH2 . ARG A 163 ? 0.3973 0.5172 0.5550 0.0142 0.1490 -0.0558 204 ARG A NH2 1289 N N . TYR A 164 ? 0.3500 0.4162 0.4071 0.0216 0.0950 -0.0667 205 TYR A N 1290 C CA . TYR A 164 ? 0.3529 0.4167 0.4130 0.0196 0.0854 -0.0632 205 TYR A CA 1291 C C . TYR A 164 ? 0.3509 0.4219 0.4299 0.0183 0.0853 -0.0604 205 TYR A C 1292 O O . TYR A 164 ? 0.3494 0.4273 0.4426 0.0198 0.0911 -0.0625 205 TYR A O 1293 C CB . TYR A 164 ? 0.3301 0.3898 0.3929 0.0227 0.0786 -0.0668 205 TYR A CB 1294 C CG . TYR A 164 ? 0.3445 0.3957 0.3916 0.0229 0.0741 -0.0682 205 TYR A CG 1295 C CD1 . TYR A 164 ? 0.3256 0.3729 0.3710 0.0262 0.0738 -0.0738 205 TYR A CD1 1296 C CD2 . TYR A 164 ? 0.3523 0.3993 0.3886 0.0197 0.0692 -0.0641 205 TYR A CD2 1297 C CE1 . TYR A 164 ? 0.3239 0.3634 0.3581 0.0262 0.0687 -0.0754 205 TYR A CE1 1298 C CE2 . TYR A 164 ? 0.3452 0.3850 0.3706 0.0198 0.0643 -0.0655 205 TYR A CE2 1299 C CZ . TYR A 164 ? 0.3601 0.3963 0.3849 0.0228 0.0640 -0.0710 205 TYR A CZ 1300 O OH . TYR A 164 ? 0.3468 0.3758 0.3629 0.0225 0.0588 -0.0724 205 TYR A OH 1301 N N . GLY A 165 ? 0.3538 0.4235 0.4336 0.0157 0.0786 -0.0561 206 GLY A N 1302 C CA . GLY A 165 ? 0.3510 0.4264 0.4489 0.0149 0.0756 -0.0543 206 GLY A CA 1303 C C . GLY A 165 ? 0.3651 0.4410 0.4607 0.0104 0.0763 -0.0490 206 GLY A C 1304 O O . GLY A 165 ? 0.3515 0.4248 0.4332 0.0082 0.0814 -0.0466 206 GLY A O 1305 N N . LYS A 166 ? 0.3539 0.4326 0.4625 0.0094 0.0706 -0.0473 207 LYS A N 1306 C CA . LYS A 166 ? 0.3638 0.4439 0.4755 0.0052 0.0710 -0.0426 207 LYS A CA 1307 C C . LYS A 166 ? 0.3582 0.4311 0.4537 0.0031 0.0660 -0.0391 207 LYS A C 1308 O O . LYS A 166 ? 0.3474 0.4200 0.4481 0.0013 0.0604 -0.0367 207 LYS A O 1309 C CB . LYS A 166 ? 0.3726 0.4571 0.4873 0.0025 0.0823 -0.0405 207 LYS A CB 1310 C CG . LYS A 166 ? 0.4179 0.5108 0.5507 0.0043 0.0893 -0.0437 207 LYS A CG 1311 C CD . LYS A 166 ? 0.4920 0.5910 0.6485 0.0042 0.0839 -0.0447 207 LYS A CD 1312 C CE . LYS A 166 ? 0.5194 0.6278 0.6961 0.0052 0.0921 -0.0472 207 LYS A CE 1313 N NZ . LYS A 166 ? 0.5580 0.6721 0.7580 0.0069 0.0846 -0.0501 207 LYS A NZ 1314 N N . VAL A 167 ? 0.3511 0.4185 0.4282 0.0034 0.0676 -0.0391 208 VAL A N 1315 C CA . VAL A 167 ? 0.3358 0.3967 0.3978 0.0017 0.0628 -0.0359 208 VAL A CA 1316 C C . VAL A 167 ? 0.3352 0.3903 0.3837 0.0039 0.0595 -0.0384 208 VAL A C 1317 O O . VAL A 167 ? 0.3341 0.3893 0.3808 0.0063 0.0628 -0.0422 208 VAL A O 1318 C CB . VAL A 167 ? 0.3358 0.3954 0.3881 -0.0017 0.0688 -0.0316 208 VAL A CB 1319 C CG1 . VAL A 167 ? 0.3327 0.3979 0.4001 -0.0045 0.0734 -0.0286 208 VAL A CG1 1320 C CG2 . VAL A 167 ? 0.3608 0.4189 0.3998 -0.0005 0.0762 -0.0331 208 VAL A CG2 1321 N N . PHE A 168 ? 0.3074 0.3573 0.3469 0.0031 0.0532 -0.0363 209 PHE A N 1322 C CA . PHE A 168 ? 0.3219 0.3662 0.3497 0.0046 0.0500 -0.0380 209 PHE A CA 1323 C C . PHE A 168 ? 0.3335 0.3761 0.3495 0.0048 0.0553 -0.0401 209 PHE A C 1324 O O . PHE A 168 ? 0.3303 0.3731 0.3389 0.0029 0.0598 -0.0378 209 PHE A O 1325 C CB . PHE A 168 ? 0.3029 0.3428 0.3230 0.0031 0.0439 -0.0347 209 PHE A CB 1326 C CG . PHE A 168 ? 0.3401 0.3746 0.3494 0.0040 0.0408 -0.0361 209 PHE A CG 1327 C CD1 . PHE A 168 ? 0.3235 0.3563 0.3361 0.0066 0.0383 -0.0390 209 PHE A CD1 1328 C CD2 . PHE A 168 ? 0.3487 0.3798 0.3460 0.0021 0.0398 -0.0342 209 PHE A CD2 1329 C CE1 . PHE A 168 ? 0.3488 0.3767 0.3538 0.0070 0.0357 -0.0402 209 PHE A CE1 1330 C CE2 . PHE A 168 ? 0.3781 0.4049 0.3678 0.0028 0.0366 -0.0358 209 PHE A CE2 1331 C CZ . PHE A 168 ? 0.3630 0.3882 0.3572 0.0050 0.0347 -0.0389 209 PHE A CZ 1332 N N . ARG A 169 ? 0.3257 0.3658 0.3388 0.0073 0.0545 -0.0444 210 ARG A N 1333 C CA . ARG A 169 ? 0.3302 0.3684 0.3322 0.0081 0.0593 -0.0475 210 ARG A CA 1334 C C . ARG A 169 ? 0.3489 0.3827 0.3350 0.0064 0.0578 -0.0457 210 ARG A C 1335 O O . ARG A 169 ? 0.3542 0.3869 0.3295 0.0068 0.0625 -0.0469 210 ARG A O 1336 C CB . ARG A 169 ? 0.3273 0.3631 0.3305 0.0112 0.0578 -0.0530 210 ARG A CB 1337 C CG . ARG A 169 ? 0.3152 0.3456 0.3153 0.0111 0.0503 -0.0530 210 ARG A CG 1338 C CD . ARG A 169 ? 0.3159 0.3434 0.3203 0.0141 0.0488 -0.0580 210 ARG A CD 1339 N NE . ARG A 169 ? 0.3049 0.3343 0.3229 0.0159 0.0470 -0.0574 210 ARG A NE 1340 C CZ . ARG A 169 ? 0.3445 0.3723 0.3662 0.0156 0.0417 -0.0538 210 ARG A CZ 1341 N NH1 . ARG A 169 ? 0.3145 0.3393 0.3289 0.0134 0.0382 -0.0508 210 ARG A NH1 1342 N NH2 . ARG A 169 ? 0.3258 0.3548 0.3582 0.0180 0.0397 -0.0535 210 ARG A NH2 1343 N N . GLY A 170 ? 0.3306 0.3614 0.3146 0.0050 0.0512 -0.0430 211 GLY A N 1344 C CA . GLY A 170 ? 0.3622 0.3891 0.3329 0.0034 0.0489 -0.0408 211 GLY A CA 1345 C C . GLY A 170 ? 0.3641 0.3925 0.3297 0.0016 0.0537 -0.0366 211 GLY A C 1346 O O . GLY A 170 ? 0.3732 0.3985 0.3250 0.0015 0.0549 -0.0361 211 GLY A O 1347 N N . ASN A 171 ? 0.3508 0.3834 0.3278 0.0003 0.0561 -0.0336 212 ASN A N 1348 C CA . ASN A 171 ? 0.3675 0.4016 0.3423 -0.0017 0.0615 -0.0292 212 ASN A CA 1349 C C . ASN A 171 ? 0.3806 0.4160 0.3498 -0.0004 0.0702 -0.0308 212 ASN A C 1350 O O . ASN A 171 ? 0.3846 0.4180 0.3426 -0.0012 0.0745 -0.0277 212 ASN A O 1351 C CB . ASN A 171 ? 0.3541 0.3927 0.3448 -0.0034 0.0619 -0.0263 212 ASN A CB 1352 C CG . ASN A 171 ? 0.4016 0.4379 0.3948 -0.0046 0.0540 -0.0239 212 ASN A CG 1353 O OD1 . ASN A 171 ? 0.3842 0.4214 0.3856 -0.0033 0.0490 -0.0258 212 ASN A OD1 1354 N ND2 . ASN A 171 ? 0.3607 0.3940 0.3464 -0.0066 0.0529 -0.0195 212 ASN A ND2 1355 N N . LYS A 172 ? 0.3627 0.4011 0.3390 0.0018 0.0730 -0.0357 213 LYS A N 1356 C CA . LYS A 172 ? 0.3671 0.4065 0.3369 0.0037 0.0817 -0.0382 213 LYS A CA 1357 C C . LYS A 172 ? 0.3868 0.4199 0.3352 0.0052 0.0811 -0.0398 213 LYS A C 1358 O O . LYS A 172 ? 0.3984 0.4302 0.3346 0.0058 0.0878 -0.0382 213 LYS A O 1359 C CB . LYS A 172 ? 0.3539 0.3967 0.3342 0.0067 0.0836 -0.0441 213 LYS A CB 1360 C CG . LYS A 172 ? 0.3511 0.4001 0.3529 0.0062 0.0831 -0.0436 213 LYS A CG 1361 C CD . LYS A 172 ? 0.3464 0.3975 0.3567 0.0097 0.0841 -0.0497 213 LYS A CD 1362 C CE . LYS A 172 ? 0.3371 0.3932 0.3677 0.0099 0.0811 -0.0497 213 LYS A CE 1363 N NZ . LYS A 172 ? 0.3549 0.4187 0.3994 0.0095 0.0892 -0.0489 213 LYS A NZ 1364 N N . VAL A 173 ? 0.3801 0.4091 0.3240 0.0061 0.0729 -0.0430 214 VAL A N 1365 C CA . VAL A 173 ? 0.3820 0.4052 0.3080 0.0077 0.0704 -0.0458 214 VAL A CA 1366 C C . VAL A 173 ? 0.4020 0.4217 0.3150 0.0060 0.0690 -0.0403 214 VAL A C 1367 O O . VAL A 173 ? 0.4203 0.4363 0.3165 0.0077 0.0715 -0.0408 214 VAL A O 1368 C CB . VAL A 173 ? 0.4029 0.4228 0.3308 0.0085 0.0615 -0.0505 214 VAL A CB 1369 C CG1 . VAL A 173 ? 0.3828 0.3967 0.2936 0.0098 0.0572 -0.0533 214 VAL A CG1 1370 C CG2 . VAL A 173 ? 0.3915 0.4131 0.3288 0.0111 0.0635 -0.0565 214 VAL A CG2 1371 N N . LYS A 174 ? 0.4023 0.4229 0.3229 0.0031 0.0650 -0.0352 215 LYS A N 1372 C CA . LYS A 174 ? 0.4236 0.4408 0.3338 0.0015 0.0637 -0.0295 215 LYS A CA 1373 C C . LYS A 174 ? 0.4361 0.4541 0.3402 0.0013 0.0735 -0.0256 215 LYS A C 1374 O O . LYS A 174 ? 0.4440 0.4571 0.3305 0.0023 0.0748 -0.0234 215 LYS A O 1375 C CB . LYS A 174 ? 0.4214 0.4400 0.3432 -0.0013 0.0588 -0.0251 215 LYS A CB 1376 C CG . LYS A 174 ? 0.4770 0.4921 0.3902 -0.0030 0.0576 -0.0189 215 LYS A CG 1377 C CD . LYS A 174 ? 0.5414 0.5576 0.4667 -0.0052 0.0516 -0.0160 215 LYS A CD 1378 C CE . LYS A 174 ? 0.6371 0.6500 0.5568 -0.0070 0.0508 -0.0097 215 LYS A CE 1379 N NZ . LYS A 174 ? 0.6802 0.6954 0.6058 -0.0089 0.0587 -0.0052 215 LYS A NZ 1380 N N . ASN A 175 ? 0.4256 0.4494 0.3442 0.0004 0.0803 -0.0247 216 ASN A N 1381 C CA . ASN A 175 ? 0.4357 0.4610 0.3516 0.0000 0.0913 -0.0206 216 ASN A CA 1382 C C . ASN A 175 ? 0.4578 0.4802 0.3559 0.0037 0.0971 -0.0239 216 ASN A C 1383 O O . ASN A 175 ? 0.4723 0.4910 0.3551 0.0042 0.1027 -0.0198 216 ASN A O 1384 C CB . ASN A 175 ? 0.4073 0.4403 0.3452 -0.0015 0.0970 -0.0200 216 ASN A CB 1385 C CG . ASN A 175 ? 0.4615 0.4967 0.4154 -0.0049 0.0915 -0.0164 216 ASN A CG 1386 O OD1 . ASN A 175 ? 0.4694 0.5003 0.4170 -0.0063 0.0855 -0.0131 216 ASN A OD1 1387 N ND2 . ASN A 175 ? 0.4193 0.4609 0.3936 -0.0058 0.0929 -0.0176 216 ASN A ND2 1388 N N . ALA A 176 ? 0.4521 0.4754 0.3509 0.0065 0.0960 -0.0314 217 ALA A N 1389 C CA . ALA A 176 ? 0.4831 0.5031 0.3642 0.0107 0.1007 -0.0360 217 ALA A CA 1390 C C . ALA A 176 ? 0.5076 0.5195 0.3654 0.0123 0.0951 -0.0357 217 ALA A C 1391 O O . ALA A 176 ? 0.5419 0.5498 0.3806 0.0150 0.1005 -0.0350 217 ALA A O 1392 C CB . ALA A 176 ? 0.4685 0.4901 0.3565 0.0134 0.0985 -0.0446 217 ALA A CB 1393 N N . GLN A 177 ? 0.5287 0.5382 0.3882 0.0109 0.0840 -0.0363 218 GLN A N 1394 C CA . GLN A 177 ? 0.5644 0.5669 0.4052 0.0123 0.0767 -0.0365 218 GLN A CA 1395 C C . GLN A 177 ? 0.5828 0.5820 0.4109 0.0115 0.0806 -0.0284 218 GLN A C 1396 O O . GLN A 177 ? 0.5924 0.5857 0.3988 0.0146 0.0814 -0.0285 218 GLN A O 1397 C CB . GLN A 177 ? 0.5615 0.5636 0.4119 0.0103 0.0652 -0.0376 218 GLN A CB 1398 C CG . GLN A 177 ? 0.6310 0.6275 0.4682 0.0124 0.0560 -0.0422 218 GLN A CG 1399 C CD . GLN A 177 ? 0.6501 0.6474 0.5005 0.0102 0.0461 -0.0432 218 GLN A CD 1400 O OE1 . GLN A 177 ? 0.6323 0.6319 0.4956 0.0100 0.0440 -0.0478 218 GLN A OE1 1401 N NE2 . GLN A 177 ? 0.6487 0.6437 0.4957 0.0088 0.0403 -0.0388 218 GLN A NE2 1402 N N . LEU A 178 ? 0.5776 0.5800 0.4186 0.0077 0.0829 -0.0215 219 LEU A N 1403 C CA . LEU A 178 ? 0.6046 0.6033 0.4356 0.0066 0.0868 -0.0131 219 LEU A CA 1404 C C . LEU A 178 ? 0.6196 0.6180 0.4407 0.0083 0.0998 -0.0102 219 LEU A C 1405 O O . LEU A 178 ? 0.6305 0.6235 0.4359 0.0089 0.1033 -0.0040 219 LEU A O 1406 C CB . LEU A 178 ? 0.6025 0.6040 0.4507 0.0021 0.0851 -0.0070 219 LEU A CB 1407 C CG . LEU A 178 ? 0.6351 0.6362 0.4911 0.0007 0.0729 -0.0086 219 LEU A CG 1408 C CD1 . LEU A 178 ? 0.6595 0.6626 0.5304 -0.0032 0.0720 -0.0025 219 LEU A CD1 1409 C CD2 . LEU A 178 ? 0.6904 0.6850 0.5287 0.0029 0.0641 -0.0100 219 LEU A CD2 1410 N N . ALA A 179 ? 0.6030 0.6068 0.4333 0.0092 0.1072 -0.0144 220 ALA A N 1411 C CA . ALA A 179 ? 0.6169 0.6206 0.4370 0.0118 0.1201 -0.0133 220 ALA A CA 1412 C C . ALA A 179 ? 0.6307 0.6280 0.4248 0.0174 0.1192 -0.0187 220 ALA A C 1413 O O . ALA A 179 ? 0.6536 0.6493 0.4344 0.0204 0.1296 -0.0178 220 ALA A O 1414 C CB . ALA A 179 ? 0.6057 0.6180 0.4464 0.0112 0.1276 -0.0164 220 ALA A CB 1415 N N . GLY A 180 ? 0.6284 0.6218 0.4154 0.0190 0.1070 -0.0246 221 GLY A N 1416 C CA . GLY A 180 ? 0.6292 0.6158 0.3911 0.0245 0.1048 -0.0303 221 GLY A CA 1417 C C . GLY A 180 ? 0.6265 0.6150 0.3901 0.0279 0.1060 -0.0404 221 GLY A C 1418 O O . GLY A 180 ? 0.6250 0.6079 0.3677 0.0330 0.1054 -0.0459 221 GLY A O 1419 N N . ALA A 181 ? 0.6014 0.5973 0.3894 0.0256 0.1069 -0.0433 222 ALA A N 1420 C CA . ALA A 181 ? 0.5966 0.5943 0.3895 0.0286 0.1070 -0.0530 222 ALA A CA 1421 C C . ALA A 181 ? 0.5977 0.5894 0.3806 0.0309 0.0943 -0.0606 222 ALA A C 1422 O O . ALA A 181 ? 0.5917 0.5811 0.3757 0.0285 0.0842 -0.0586 222 ALA A O 1423 C CB . ALA A 181 ? 0.5649 0.5708 0.3872 0.0252 0.1073 -0.0536 222 ALA A CB 1424 N N . LYS A 182 ? 0.5861 0.5754 0.3611 0.0354 0.0946 -0.0697 223 LYS A N 1425 C CA . LYS A 182 ? 0.5926 0.5768 0.3629 0.0370 0.0821 -0.0777 223 LYS A CA 1426 C C . LYS A 182 ? 0.5700 0.5578 0.3624 0.0357 0.0778 -0.0838 223 LYS A C 1427 O O . LYS A 182 ? 0.5640 0.5478 0.3558 0.0368 0.0680 -0.0908 223 LYS A O 1428 C CB . LYS A 182 ? 0.6333 0.6101 0.3774 0.0432 0.0817 -0.0846 223 LYS A CB 1429 C CG . LYS A 182 ? 0.6780 0.6559 0.4199 0.0474 0.0909 -0.0910 223 LYS A CG 1430 C CD . LYS A 182 ? 0.7222 0.6915 0.4362 0.0539 0.0881 -0.0985 223 LYS A CD 1431 C CE . LYS A 182 ? 0.7790 0.7484 0.4821 0.0590 0.1011 -0.1016 223 LYS A CE 1432 N NZ . LYS A 182 ? 0.8042 0.7644 0.4777 0.0659 0.0977 -0.1093 223 LYS A NZ 1433 N N . GLY A 183 ? 0.5536 0.5485 0.3658 0.0335 0.0847 -0.0810 224 GLY A N 1434 C CA . GLY A 183 ? 0.5379 0.5359 0.3709 0.0326 0.0814 -0.0858 224 GLY A CA 1435 C C . GLY A 183 ? 0.5141 0.5201 0.3670 0.0302 0.0892 -0.0810 224 GLY A C 1436 O O . GLY A 183 ? 0.5198 0.5292 0.3700 0.0303 0.0992 -0.0762 224 GLY A O 1437 N N . VAL A 184 ? 0.4888 0.4978 0.3620 0.0282 0.0845 -0.0820 225 VAL A N 1438 C CA . VAL A 184 ? 0.4693 0.4858 0.3629 0.0264 0.0899 -0.0784 225 VAL A CA 1439 C C . VAL A 184 ? 0.4663 0.4842 0.3747 0.0284 0.0888 -0.0848 225 VAL A C 1440 O O . VAL A 184 ? 0.4649 0.4791 0.3772 0.0282 0.0802 -0.0884 225 VAL A O 1441 C CB . VAL A 184 ? 0.4438 0.4628 0.3490 0.0217 0.0849 -0.0713 225 VAL A CB 1442 C CG1 . VAL A 184 ? 0.4175 0.4441 0.3434 0.0203 0.0900 -0.0682 225 VAL A CG1 1443 C CG2 . VAL A 184 ? 0.4626 0.4794 0.3539 0.0196 0.0849 -0.0646 225 VAL A CG2 1444 N N . ILE A 185 ? 0.4503 0.4736 0.3678 0.0303 0.0976 -0.0860 226 ILE A N 1445 C CA . ILE A 185 ? 0.4224 0.4479 0.3568 0.0322 0.0970 -0.0909 226 ILE A CA 1446 C C . ILE A 185 ? 0.4120 0.4449 0.3669 0.0295 0.0988 -0.0852 226 ILE A C 1447 O O . ILE A 185 ? 0.4193 0.4581 0.3778 0.0286 0.1071 -0.0809 226 ILE A O 1448 C CB . ILE A 185 ? 0.4501 0.4761 0.3805 0.0372 0.1054 -0.0978 226 ILE A CB 1449 C CG1 . ILE A 185 ? 0.4540 0.4718 0.3625 0.0403 0.1025 -0.1041 226 ILE A CG1 1450 C CG2 . ILE A 185 ? 0.4143 0.4432 0.3645 0.0394 0.1051 -0.1022 226 ILE A CG2 1451 C CD1 . ILE A 185 ? 0.4542 0.4719 0.3524 0.0456 0.1124 -0.1101 226 ILE A CD1 1452 N N . LEU A 186 ? 0.3685 0.4011 0.3370 0.0284 0.0911 -0.0850 227 LEU A N 1453 C CA . LEU A 186 ? 0.3658 0.4047 0.3537 0.0267 0.0909 -0.0806 227 LEU A CA 1454 C C . LEU A 186 ? 0.3634 0.4048 0.3664 0.0302 0.0923 -0.0856 227 LEU A C 1455 O O . LEU A 186 ? 0.3754 0.4116 0.3763 0.0328 0.0886 -0.0913 227 LEU A O 1456 C CB . LEU A 186 ? 0.3386 0.3747 0.3299 0.0237 0.0811 -0.0765 227 LEU A CB 1457 C CG . LEU A 186 ? 0.4010 0.4348 0.3794 0.0202 0.0788 -0.0713 227 LEU A CG 1458 C CD1 . LEU A 186 ? 0.3977 0.4280 0.3786 0.0181 0.0692 -0.0687 227 LEU A CD1 1459 C CD2 . LEU A 186 ? 0.4188 0.4586 0.4015 0.0180 0.0848 -0.0655 227 LEU A CD2 1460 N N . TYR A 187 ? 0.3456 0.3948 0.3644 0.0306 0.0975 -0.0840 228 TYR A N 1461 C CA . TYR A 187 ? 0.3424 0.3942 0.3770 0.0343 0.0981 -0.0887 228 TYR A CA 1462 C C . TYR A 187 ? 0.3388 0.3974 0.3935 0.0334 0.0966 -0.0849 228 TYR A C 1463 O O . TYR A 187 ? 0.3475 0.4107 0.4055 0.0301 0.0984 -0.0795 228 TYR A O 1464 C CB . TYR A 187 ? 0.3467 0.4010 0.3799 0.0384 0.1079 -0.0946 228 TYR A CB 1465 C CG . TYR A 187 ? 0.3549 0.4185 0.3979 0.0378 0.1177 -0.0917 228 TYR A CG 1466 C CD1 . TYR A 187 ? 0.3692 0.4402 0.4339 0.0401 0.1207 -0.0934 228 TYR A CD1 1467 C CD2 . TYR A 187 ? 0.3732 0.4380 0.4049 0.0351 0.1239 -0.0872 228 TYR A CD2 1468 C CE1 . TYR A 187 ? 0.3801 0.4605 0.4568 0.0392 0.1302 -0.0907 228 TYR A CE1 1469 C CE2 . TYR A 187 ? 0.4036 0.4769 0.4460 0.0341 0.1337 -0.0838 228 TYR A CE2 1470 C CZ . TYR A 187 ? 0.4050 0.4864 0.4707 0.0360 0.1367 -0.0857 228 TYR A CZ 1471 O OH . TYR A 187 ? 0.4235 0.5138 0.5024 0.0347 0.1462 -0.0825 228 TYR A OH 1472 N N . SER A 188 ? 0.3300 0.3890 0.3985 0.0364 0.0929 -0.0879 229 SER A N 1473 C CA . SER A 188 ? 0.3192 0.3846 0.4074 0.0366 0.0906 -0.0854 229 SER A CA 1474 C C . SER A 188 ? 0.3263 0.4003 0.4296 0.0393 0.0992 -0.0886 229 SER A C 1475 O O . SER A 188 ? 0.3239 0.3974 0.4316 0.0436 0.1012 -0.0942 229 SER A O 1476 C CB . SER A 188 ? 0.3173 0.3776 0.4113 0.0388 0.0812 -0.0863 229 SER A CB 1477 O OG . SER A 188 ? 0.3382 0.3912 0.4194 0.0362 0.0745 -0.0831 229 SER A OG 1478 N N . ASP A 189 ? 0.3261 0.4080 0.4383 0.0368 0.1043 -0.0849 230 ASP A N 1479 C CA . ASP A 189 ? 0.3510 0.4422 0.4805 0.0390 0.1128 -0.0874 230 ASP A CA 1480 C C . ASP A 189 ? 0.3566 0.4524 0.5088 0.0412 0.1063 -0.0883 230 ASP A C 1481 O O . ASP A 189 ? 0.3605 0.4557 0.5170 0.0391 0.0978 -0.0844 230 ASP A O 1482 C CB . ASP A 189 ? 0.3538 0.4514 0.4850 0.0351 0.1215 -0.0828 230 ASP A CB 1483 C CG . ASP A 189 ? 0.3812 0.4876 0.5256 0.0374 0.1337 -0.0856 230 ASP A CG 1484 O OD1 . ASP A 189 ? 0.4085 0.5138 0.5391 0.0380 0.1435 -0.0866 230 ASP A OD1 1485 O OD2 . ASP A 189 ? 0.3850 0.4991 0.5531 0.0391 0.1332 -0.0872 230 ASP A OD2 1486 N N . PRO A 190 ? 0.3739 0.4742 0.5404 0.0459 0.1099 -0.0935 231 PRO A N 1487 C CA . PRO A 190 ? 0.3727 0.4781 0.5619 0.0485 0.1039 -0.0945 231 PRO A CA 1488 C C . PRO A 190 ? 0.3751 0.4889 0.5801 0.0450 0.1032 -0.0901 231 PRO A C 1489 O O . PRO A 190 ? 0.3676 0.4833 0.5865 0.0462 0.0945 -0.0896 231 PRO A O 1490 C CB . PRO A 190 ? 0.3898 0.5009 0.5921 0.0535 0.1116 -0.1006 231 PRO A CB 1491 C CG . PRO A 190 ? 0.4053 0.5103 0.5882 0.0547 0.1179 -0.1039 231 PRO A CG 1492 C CD . PRO A 190 ? 0.3760 0.4758 0.5372 0.0496 0.1187 -0.0993 231 PRO A CD 1493 N N . ALA A 191 ? 0.3812 0.4994 0.5839 0.0409 0.1119 -0.0870 232 ALA A N 1494 C CA . ALA A 191 ? 0.3814 0.5070 0.6008 0.0372 0.1106 -0.0829 232 ALA A CA 1495 C C . ALA A 191 ? 0.3789 0.4987 0.5928 0.0351 0.0976 -0.0792 232 ALA A C 1496 O O . ALA A 191 ? 0.3620 0.4863 0.5931 0.0349 0.0907 -0.0784 232 ALA A O 1497 C CB . ALA A 191 ? 0.4040 0.5333 0.6192 0.0328 0.1220 -0.0792 232 ALA A CB 1498 N N . ASP A 192 ? 0.3747 0.4845 0.5649 0.0339 0.0941 -0.0775 233 ASP A N 1499 C CA . ASP A 192 ? 0.3714 0.4751 0.5532 0.0319 0.0834 -0.0737 233 ASP A CA 1500 C C . ASP A 192 ? 0.3739 0.4708 0.5526 0.0361 0.0734 -0.0756 233 ASP A C 1501 O O . ASP A 192 ? 0.3991 0.4926 0.5769 0.0358 0.0638 -0.0730 233 ASP A O 1502 C CB . ASP A 192 ? 0.3694 0.4666 0.5283 0.0279 0.0860 -0.0700 233 ASP A CB 1503 C CG . ASP A 192 ? 0.4035 0.5062 0.5633 0.0242 0.0969 -0.0675 233 ASP A CG 1504 O OD1 . ASP A 192 ? 0.4080 0.5151 0.5786 0.0210 0.0959 -0.0640 233 ASP A OD1 1505 O OD2 . ASP A 192 ? 0.3806 0.4832 0.5314 0.0249 0.1064 -0.0691 233 ASP A OD2 1506 N N . TYR A 193 ? 0.3505 0.4446 0.5266 0.0401 0.0755 -0.0800 234 TYR A N 1507 C CA . TYR A 193 ? 0.3341 0.4199 0.5045 0.0435 0.0668 -0.0809 234 TYR A CA 1508 C C . TYR A 193 ? 0.3439 0.4317 0.5293 0.0493 0.0653 -0.0855 234 TYR A C 1509 O O . TYR A 193 ? 0.3434 0.4237 0.5233 0.0526 0.0607 -0.0869 234 TYR A O 1510 C CB . TYR A 193 ? 0.3332 0.4097 0.4818 0.0425 0.0680 -0.0812 234 TYR A CB 1511 C CG . TYR A 193 ? 0.3261 0.3996 0.4603 0.0374 0.0669 -0.0762 234 TYR A CG 1512 C CD1 . TYR A 193 ? 0.3519 0.4274 0.4772 0.0340 0.0748 -0.0753 234 TYR A CD1 1513 C CD2 . TYR A 193 ? 0.3327 0.4012 0.4619 0.0365 0.0580 -0.0723 234 TYR A CD2 1514 C CE1 . TYR A 193 ? 0.3528 0.4256 0.4657 0.0295 0.0733 -0.0705 234 TYR A CE1 1515 C CE2 . TYR A 193 ? 0.3468 0.4130 0.4643 0.0321 0.0568 -0.0680 234 TYR A CE2 1516 C CZ . TYR A 193 ? 0.3584 0.4268 0.4683 0.0286 0.0642 -0.0671 234 TYR A CZ 1517 O OH . TYR A 193 ? 0.3463 0.4117 0.4444 0.0246 0.0624 -0.0627 234 TYR A OH 1518 N N . PHE A 194 ? 0.3476 0.4455 0.5530 0.0506 0.0694 -0.0878 235 PHE A N 1519 C CA . PHE A 194 ? 0.3476 0.4482 0.5695 0.0565 0.0676 -0.0923 235 PHE A CA 1520 C C . PHE A 194 ? 0.3637 0.4743 0.6085 0.0567 0.0647 -0.0919 235 PHE A C 1521 O O . PHE A 194 ? 0.3645 0.4846 0.6214 0.0545 0.0729 -0.0926 235 PHE A O 1522 C CB . PHE A 194 ? 0.3512 0.4547 0.5751 0.0587 0.0782 -0.0974 235 PHE A CB 1523 C CG . PHE A 194 ? 0.3434 0.4469 0.5803 0.0653 0.0760 -0.1025 235 PHE A CG 1524 C CD1 . PHE A 194 ? 0.3485 0.4416 0.5738 0.0684 0.0726 -0.1045 235 PHE A CD1 1525 C CD2 . PHE A 194 ? 0.3525 0.4665 0.6147 0.0684 0.0770 -0.1052 235 PHE A CD2 1526 C CE1 . PHE A 194 ? 0.3794 0.4717 0.6170 0.0749 0.0703 -0.1091 235 PHE A CE1 1527 C CE2 . PHE A 194 ? 0.3621 0.4759 0.6369 0.0750 0.0745 -0.1099 235 PHE A CE2 1528 C CZ . PHE A 194 ? 0.3638 0.4664 0.6256 0.0783 0.0712 -0.1117 235 PHE A CZ 1529 N N . ALA A 195 ? 0.3708 0.4790 0.6210 0.0592 0.0532 -0.0907 236 ALA A N 1530 C CA . ALA A 195 ? 0.3934 0.5107 0.6660 0.0599 0.0485 -0.0911 236 ALA A CA 1531 C C . ALA A 195 ? 0.4138 0.5390 0.7089 0.0650 0.0515 -0.0965 236 ALA A C 1532 O O . ALA A 195 ? 0.4080 0.5282 0.7011 0.0701 0.0495 -0.0993 236 ALA A O 1533 C CB . ALA A 195 ? 0.3886 0.5000 0.6580 0.0620 0.0346 -0.0886 236 ALA A CB 1534 N N . PRO A 196 ? 0.4358 0.5734 0.7534 0.0635 0.0566 -0.0981 237 PRO A N 1535 C CA . PRO A 196 ? 0.4452 0.5910 0.7854 0.0684 0.0602 -0.1034 237 PRO A CA 1536 C C . PRO A 196 ? 0.4438 0.5870 0.7937 0.0751 0.0469 -0.1055 237 PRO A C 1537 O O . PRO A 196 ? 0.4425 0.5830 0.7918 0.0752 0.0355 -0.1030 237 PRO A O 1538 C CB . PRO A 196 ? 0.4522 0.6118 0.8159 0.0648 0.0665 -0.1036 237 PRO A CB 1539 C CG . PRO A 196 ? 0.4556 0.6126 0.8036 0.0575 0.0702 -0.0983 237 PRO A CG 1540 C CD . PRO A 196 ? 0.4382 0.5828 0.7634 0.0575 0.0590 -0.0951 237 PRO A CD 1541 N N . GLY A 197 ? 0.4443 0.5869 0.8007 0.0810 0.0482 -0.1098 238 GLY A N 1542 C CA . GLY A 197 ? 0.4422 0.5835 0.8112 0.0882 0.0366 -0.1121 238 GLY A CA 1543 C C . GLY A 197 ? 0.4469 0.5732 0.7946 0.0915 0.0269 -0.1095 238 GLY A C 1544 O O . GLY A 197 ? 0.4497 0.5730 0.8045 0.0978 0.0167 -0.1105 238 GLY A O 1545 N N . VAL A 198 ? 0.4095 0.5263 0.7314 0.0874 0.0301 -0.1059 239 VAL A N 1546 C CA . VAL A 198 ? 0.3969 0.4994 0.6988 0.0900 0.0227 -0.1031 239 VAL A CA 1547 C C . VAL A 198 ? 0.3917 0.4877 0.6812 0.0902 0.0309 -0.1051 239 VAL A C 1548 O O . VAL A 198 ? 0.3900 0.4902 0.6766 0.0864 0.0417 -0.1068 239 VAL A O 1549 C CB . VAL A 198 ? 0.3966 0.4925 0.6798 0.0856 0.0167 -0.0970 239 VAL A CB 1550 C CG1 A VAL A 198 ? 0.3846 0.4899 0.6737 0.0795 0.0205 -0.0958 239 VAL A CG1 1551 C CG1 B VAL A 198 ? 0.3784 0.4595 0.6394 0.0872 0.0123 -0.0935 239 VAL A CG1 1552 C CG2 A VAL A 198 ? 0.3731 0.4565 0.6307 0.0836 0.0184 -0.0937 239 VAL A CG2 1553 C CG2 B VAL A 198 ? 0.3758 0.4765 0.6711 0.0870 0.0064 -0.0959 239 VAL A CG2 1554 N N . LYS A 199 ? 0.3980 0.4834 0.6807 0.0950 0.0255 -0.1050 240 LYS A N 1555 C CA A LYS A 199 ? 0.4047 0.4825 0.6776 0.0962 0.0312 -0.1075 240 LYS A CA 1556 C CA B LYS A 199 ? 0.4055 0.4842 0.6787 0.0958 0.0321 -0.1078 240 LYS A CA 1557 C C . LYS A 199 ? 0.4053 0.4738 0.6535 0.0908 0.0332 -0.1038 240 LYS A C 1558 O O . LYS A 199 ? 0.3912 0.4557 0.6289 0.0882 0.0273 -0.0984 240 LYS A O 1559 C CB A LYS A 199 ? 0.4132 0.4824 0.6898 0.1035 0.0234 -0.1081 240 LYS A CB 1560 C CB B LYS A 199 ? 0.4217 0.4939 0.7020 0.1034 0.0268 -0.1101 240 LYS A CB 1561 C CG A LYS A 199 ? 0.4295 0.5071 0.7312 0.1100 0.0228 -0.1135 240 LYS A CG 1562 C CG B LYS A 199 ? 0.4238 0.5066 0.7304 0.1089 0.0272 -0.1154 240 LYS A CG 1563 C CD A LYS A 199 ? 0.4386 0.5083 0.7446 0.1173 0.0114 -0.1121 240 LYS A CD 1564 C CD B LYS A 199 ? 0.4362 0.5298 0.7526 0.1071 0.0402 -0.1210 240 LYS A CD 1565 C CE A LYS A 199 ? 0.4663 0.5445 0.7980 0.1239 0.0108 -0.1179 240 LYS A CE 1566 C CE B LYS A 199 ? 0.4650 0.5559 0.7879 0.1128 0.0443 -0.1271 240 LYS A CE 1567 N NZ A LYS A 199 ? 0.4904 0.5655 0.8297 0.1304 -0.0023 -0.1156 240 LYS A NZ 1568 N NZ B LYS A 199 ? 0.4653 0.5699 0.8091 0.1146 0.0538 -0.1331 240 LYS A NZ 1569 N N . SER A 200 ? 0.4021 0.4672 0.6417 0.0896 0.0410 -0.1070 241 SER A N 1570 C CA . SER A 200 ? 0.4083 0.4637 0.6259 0.0853 0.0421 -0.1045 241 SER A CA 1571 C C . SER A 200 ? 0.3981 0.4404 0.6077 0.0880 0.0341 -0.1013 241 SER A C 1572 O O . SER A 200 ? 0.3910 0.4299 0.6102 0.0940 0.0304 -0.1032 241 SER A O 1573 C CB . SER A 200 ? 0.4447 0.4989 0.6576 0.0852 0.0511 -0.1104 241 SER A CB 1574 O OG . SER A 200 ? 0.4995 0.5641 0.7154 0.0824 0.0602 -0.1128 241 SER A OG 1575 N N . TYR A 201 ? 0.3894 0.4241 0.5816 0.0838 0.0322 -0.0967 242 TYR A N 1576 C CA . TYR A 201 ? 0.3889 0.4105 0.5720 0.0854 0.0267 -0.0933 242 TYR A CA 1577 C C . TYR A 201 ? 0.4108 0.4259 0.5964 0.0887 0.0295 -0.0985 242 TYR A C 1578 O O . TYR A 201 ? 0.3965 0.4145 0.5803 0.0868 0.0367 -0.1039 242 TYR A O 1579 C CB . TYR A 201 ? 0.3714 0.3876 0.5368 0.0795 0.0265 -0.0885 242 TYR A CB 1580 C CG . TYR A 201 ? 0.3714 0.3755 0.5293 0.0812 0.0201 -0.0830 242 TYR A CG 1581 C CD1 . TYR A 201 ? 0.3712 0.3738 0.5284 0.0834 0.0131 -0.0773 242 TYR A CD1 1582 C CD2 . TYR A 201 ? 0.3924 0.3860 0.5443 0.0810 0.0212 -0.0837 242 TYR A CD2 1583 C CE1 . TYR A 201 ? 0.3978 0.3885 0.5471 0.0856 0.0082 -0.0717 242 TYR A CE1 1584 C CE2 . TYR A 201 ? 0.4054 0.3875 0.5515 0.0825 0.0164 -0.0780 242 TYR A CE2 1585 C CZ . TYR A 201 ? 0.4406 0.4212 0.5847 0.0848 0.0104 -0.0717 242 TYR A CZ 1586 O OH . TYR A 201 ? 0.5123 0.4808 0.6495 0.0865 0.0069 -0.0658 242 TYR A OH 1587 N N . PRO A 202 ? 0.4275 0.4334 0.6166 0.0937 0.0240 -0.0971 243 PRO A N 1588 C CA . PRO A 202 ? 0.4374 0.4363 0.6244 0.0966 0.0155 -0.0902 243 PRO A CA 1589 C C . PRO A 202 ? 0.4428 0.4472 0.6437 0.1025 0.0097 -0.0899 243 PRO A C 1590 O O . PRO A 202 ? 0.4734 0.4709 0.6716 0.1061 0.0022 -0.0846 243 PRO A O 1591 C CB . PRO A 202 ? 0.4358 0.4210 0.6200 0.0994 0.0140 -0.0898 243 PRO A CB 1592 C CG . PRO A 202 ? 0.4369 0.4254 0.6325 0.1022 0.0192 -0.0985 243 PRO A CG 1593 C CD . PRO A 202 ? 0.4405 0.4401 0.6337 0.0971 0.0265 -0.1027 243 PRO A CD 1594 N N . ASP A 203 ? 0.4285 0.4450 0.6438 0.1035 0.0130 -0.0953 244 ASP A N 1595 C CA . ASP A 203 ? 0.4367 0.4590 0.6684 0.1095 0.0073 -0.0962 244 ASP A CA 1596 C C . ASP A 203 ? 0.4148 0.4473 0.6504 0.1071 0.0045 -0.0942 244 ASP A C 1597 O O . ASP A 203 ? 0.4058 0.4437 0.6553 0.1117 -0.0013 -0.0949 244 ASP A O 1598 C CB . ASP A 203 ? 0.4482 0.4773 0.6977 0.1134 0.0121 -0.1038 244 ASP A CB 1599 C CG . ASP A 203 ? 0.5198 0.5380 0.7673 0.1168 0.0137 -0.1066 244 ASP A CG 1600 O OD1 . ASP A 203 ? 0.5462 0.5521 0.7880 0.1201 0.0072 -0.1022 244 ASP A OD1 1601 O OD2 . ASP A 203 ? 0.5617 0.5835 0.8130 0.1161 0.0218 -0.1130 244 ASP A OD2 1602 N N . GLY A 204 ? 0.3975 0.4321 0.6211 0.1002 0.0082 -0.0918 245 GLY A N 1603 C CA . GLY A 204 ? 0.3730 0.4160 0.5987 0.0972 0.0057 -0.0895 245 GLY A CA 1604 C C . GLY A 204 ? 0.3791 0.4194 0.5866 0.0899 0.0095 -0.0860 245 GLY A C 1605 O O . GLY A 204 ? 0.3805 0.4125 0.5752 0.0880 0.0127 -0.0851 245 GLY A O 1606 N N . TRP A 205 ? 0.3507 0.3980 0.5583 0.0861 0.0087 -0.0841 246 TRP A N 1607 C CA . TRP A 205 ? 0.3469 0.3911 0.5374 0.0799 0.0108 -0.0802 246 TRP A CA 1608 C C . TRP A 205 ? 0.3396 0.3912 0.5294 0.0740 0.0204 -0.0826 246 TRP A C 1609 O O . TRP A 205 ? 0.3374 0.3885 0.5155 0.0688 0.0219 -0.0795 246 TRP A O 1610 C CB . TRP A 205 ? 0.3388 0.3831 0.5258 0.0795 0.0031 -0.0758 246 TRP A CB 1611 C CG . TRP A 205 ? 0.3541 0.4090 0.5591 0.0813 -0.0007 -0.0780 246 TRP A CG 1612 C CD1 . TRP A 205 ? 0.3929 0.4486 0.6100 0.0877 -0.0086 -0.0792 246 TRP A CD1 1613 C CD2 . TRP A 205 ? 0.3837 0.4490 0.5964 0.0764 0.0026 -0.0790 246 TRP A CD2 1614 N NE1 . TRP A 205 ? 0.4215 0.4882 0.6548 0.0870 -0.0108 -0.0815 246 TRP A NE1 1615 C CE2 . TRP A 205 ? 0.3836 0.4563 0.6150 0.0800 -0.0037 -0.0812 246 TRP A CE2 1616 C CE3 . TRP A 205 ? 0.3907 0.4596 0.5969 0.0696 0.0100 -0.0781 246 TRP A CE3 1617 C CZ2 . TRP A 205 ? 0.3930 0.4768 0.6383 0.0764 -0.0023 -0.0826 246 TRP A CZ2 1618 C CZ3 . TRP A 205 ? 0.4063 0.4858 0.6251 0.0662 0.0118 -0.0789 246 TRP A CZ3 1619 C CH2 . TRP A 205 ? 0.3951 0.4819 0.6339 0.0694 0.0057 -0.0812 246 TRP A CH2 1620 N N . ASN A 206 ? 0.3265 0.3846 0.5281 0.0753 0.0271 -0.0880 247 ASN A N 1621 C CA . ASN A 206 ? 0.3344 0.3988 0.5337 0.0705 0.0371 -0.0902 247 ASN A CA 1622 C C . ASN A 206 ? 0.3346 0.3914 0.5179 0.0685 0.0422 -0.0914 247 ASN A C 1623 O O . ASN A 206 ? 0.3305 0.3784 0.5096 0.0715 0.0394 -0.0922 247 ASN A O 1624 C CB . ASN A 206 ? 0.3318 0.4070 0.5505 0.0727 0.0433 -0.0955 247 ASN A CB 1625 C CG . ASN A 206 ? 0.3420 0.4283 0.5743 0.0704 0.0434 -0.0944 247 ASN A CG 1626 O OD1 . ASN A 206 ? 0.3477 0.4338 0.5724 0.0661 0.0409 -0.0900 247 ASN A OD1 1627 N ND2 . ASN A 206 ? 0.2901 0.3862 0.5440 0.0733 0.0464 -0.0984 247 ASN A ND2 1628 N N . LEU A 207 ? 0.3193 0.3793 0.4939 0.0635 0.0492 -0.0915 248 LEU A N 1629 C CA . LEU A 207 ? 0.3102 0.3642 0.4698 0.0615 0.0540 -0.0935 248 LEU A CA 1630 C C . LEU A 207 ? 0.3306 0.3864 0.4960 0.0650 0.0608 -0.1003 248 LEU A C 1631 O O . LEU A 207 ? 0.3468 0.4119 0.5224 0.0655 0.0674 -0.1029 248 LEU A O 1632 C CB . LEU A 207 ? 0.3136 0.3705 0.4616 0.0556 0.0586 -0.0910 248 LEU A CB 1633 C CG . LEU A 207 ? 0.3470 0.3973 0.4771 0.0532 0.0619 -0.0925 248 LEU A CG 1634 C CD1 . LEU A 207 ? 0.3419 0.3811 0.4608 0.0524 0.0547 -0.0898 248 LEU A CD1 1635 C CD2 . LEU A 207 ? 0.3709 0.4261 0.4927 0.0484 0.0674 -0.0904 248 LEU A CD2 1636 N N . PRO A 208 ? 0.3402 0.3869 0.5004 0.0677 0.0593 -0.1034 249 PRO A N 1637 C CA . PRO A 208 ? 0.3493 0.3959 0.5116 0.0709 0.0657 -0.1106 249 PRO A CA 1638 C C . PRO A 208 ? 0.3542 0.4019 0.5024 0.0675 0.0735 -0.1130 249 PRO A C 1639 O O . PRO A 208 ? 0.3536 0.3991 0.4882 0.0627 0.0724 -0.1091 249 PRO A O 1640 C CB . PRO A 208 ? 0.3579 0.3925 0.5164 0.0736 0.0603 -0.1122 249 PRO A CB 1641 C CG . PRO A 208 ? 0.3665 0.3950 0.5201 0.0717 0.0521 -0.1053 249 PRO A CG 1642 C CD . PRO A 208 ? 0.3319 0.3676 0.4845 0.0679 0.0514 -0.0999 249 PRO A CD 1643 N N . GLY A 209 ? 0.3689 0.4196 0.5196 0.0705 0.0812 -0.1196 250 GLY A N 1644 C CA . GLY A 209 ? 0.3790 0.4309 0.5155 0.0684 0.0893 -0.1223 250 GLY A CA 1645 C C . GLY A 209 ? 0.3915 0.4328 0.5085 0.0661 0.0860 -0.1231 250 GLY A C 1646 O O . GLY A 209 ? 0.3803 0.4218 0.4824 0.0635 0.0905 -0.1235 250 GLY A O 1647 N N . GLY A 210 ? 0.3835 0.4157 0.5012 0.0674 0.0784 -0.1236 251 GLY A N 1648 C CA . GLY A 210 ? 0.3917 0.4137 0.4946 0.0650 0.0739 -0.1241 251 GLY A CA 1649 C C . GLY A 210 ? 0.3892 0.4085 0.4865 0.0602 0.0674 -0.1163 251 GLY A C 1650 O O . GLY A 210 ? 0.3789 0.3910 0.4650 0.0575 0.0639 -0.1160 251 GLY A O 1651 N N . GLY A 211 ? 0.3657 0.3910 0.4712 0.0591 0.0657 -0.1102 252 GLY A N 1652 C CA . GLY A 211 ? 0.3419 0.3648 0.4418 0.0550 0.0599 -0.1030 252 GLY A CA 1653 C C . GLY A 211 ? 0.3400 0.3656 0.4265 0.0502 0.0627 -0.1009 252 GLY A C 1654 O O . GLY A 211 ? 0.3408 0.3730 0.4255 0.0499 0.0697 -0.1028 252 GLY A O 1655 N N . VAL A 212 ? 0.3229 0.3433 0.4001 0.0466 0.0578 -0.0968 253 VAL A N 1656 C CA . VAL A 212 ? 0.3220 0.3439 0.3861 0.0423 0.0594 -0.0947 253 VAL A CA 1657 C C . VAL A 212 ? 0.3281 0.3490 0.3900 0.0389 0.0540 -0.0875 253 VAL A C 1658 O O . VAL A 212 ? 0.3308 0.3457 0.3943 0.0391 0.0484 -0.0852 253 VAL A O 1659 C CB . VAL A 212 ? 0.3291 0.3444 0.3798 0.0415 0.0594 -0.0993 253 VAL A CB 1660 C CG1 . VAL A 212 ? 0.3196 0.3369 0.3563 0.0377 0.0611 -0.0970 253 VAL A CG1 1661 C CG2 . VAL A 212 ? 0.3445 0.3589 0.3957 0.0456 0.0642 -0.1076 253 VAL A CG2 1662 N N . GLN A 213 ? 0.3057 0.3320 0.3634 0.0359 0.0560 -0.0839 254 GLN A N 1663 C CA . GLN A 213 ? 0.3195 0.3451 0.3744 0.0327 0.0512 -0.0774 254 GLN A CA 1664 C C . GLN A 213 ? 0.3222 0.3426 0.3633 0.0296 0.0493 -0.0769 254 GLN A C 1665 O O . GLN A 213 ? 0.3208 0.3429 0.3523 0.0279 0.0528 -0.0780 254 GLN A O 1666 C CB . GLN A 213 ? 0.3006 0.3342 0.3588 0.0309 0.0540 -0.0739 254 GLN A CB 1667 C CG . GLN A 213 ? 0.3071 0.3400 0.3622 0.0278 0.0489 -0.0676 254 GLN A CG 1668 C CD . GLN A 213 ? 0.3063 0.3461 0.3632 0.0253 0.0519 -0.0646 254 GLN A CD 1669 O OE1 . GLN A 213 ? 0.3270 0.3659 0.3758 0.0220 0.0505 -0.0609 254 GLN A OE1 1670 N NE2 . GLN A 213 ? 0.2864 0.3329 0.3552 0.0268 0.0559 -0.0661 254 GLN A NE2 1671 N N . ARG A 214 ? 0.3131 0.3272 0.3533 0.0290 0.0438 -0.0748 255 ARG A N 1672 C CA . ARG A 214 ? 0.3333 0.3435 0.3633 0.0258 0.0409 -0.0733 255 ARG A CA 1673 C C . ARG A 214 ? 0.3239 0.3377 0.3498 0.0228 0.0400 -0.0676 255 ARG A C 1674 O O . ARG A 214 ? 0.3076 0.3258 0.3397 0.0232 0.0402 -0.0643 255 ARG A O 1675 C CB . ARG A 214 ? 0.3139 0.3168 0.3468 0.0260 0.0361 -0.0722 255 ARG A CB 1676 C CG . ARG A 214 ? 0.3526 0.3504 0.3881 0.0284 0.0365 -0.0784 255 ARG A CG 1677 C CD . ARG A 214 ? 0.3303 0.3216 0.3732 0.0295 0.0329 -0.0762 255 ARG A CD 1678 N NE . ARG A 214 ? 0.3646 0.3505 0.4126 0.0321 0.0331 -0.0817 255 ARG A NE 1679 C CZ . ARG A 214 ? 0.3913 0.3783 0.4462 0.0359 0.0352 -0.0849 255 ARG A CZ 1680 N NH1 . ARG A 214 ? 0.3599 0.3540 0.4183 0.0375 0.0375 -0.0831 255 ARG A NH1 1681 N NH2 . ARG A 214 ? 0.3477 0.3289 0.4073 0.0383 0.0350 -0.0901 255 ARG A NH2 1682 N N . GLY A 215 ? 0.3174 0.3290 0.3337 0.0200 0.0383 -0.0666 256 GLY A N 1683 C CA . GLY A 215 ? 0.2951 0.3086 0.3086 0.0174 0.0362 -0.0608 256 GLY A CA 1684 C C . GLY A 215 ? 0.3086 0.3212 0.3109 0.0146 0.0355 -0.0605 256 GLY A C 1685 O O . GLY A 215 ? 0.3131 0.3254 0.3081 0.0148 0.0380 -0.0645 256 GLY A O 1686 N N . ASN A 216 ? 0.2902 0.3019 0.2903 0.0125 0.0321 -0.0560 257 ASN A N 1687 C CA . ASN A 216 ? 0.2984 0.3091 0.2883 0.0102 0.0307 -0.0557 257 ASN A CA 1688 C C . ASN A 216 ? 0.3091 0.3239 0.2929 0.0092 0.0344 -0.0541 257 ASN A C 1689 O O . ASN A 216 ? 0.3029 0.3218 0.2924 0.0094 0.0370 -0.0518 257 ASN A O 1690 C CB . ASN A 216 ? 0.2934 0.3021 0.2836 0.0085 0.0261 -0.0516 257 ASN A CB 1691 C CG . ASN A 216 ? 0.3437 0.3557 0.3342 0.0074 0.0259 -0.0461 257 ASN A CG 1692 O OD1 . ASN A 216 ? 0.3570 0.3709 0.3413 0.0059 0.0269 -0.0446 257 ASN A OD1 1693 N ND2 . ASN A 216 ? 0.3653 0.3771 0.3626 0.0083 0.0244 -0.0432 257 ASN A ND2 1694 N N . ILE A 217 ? 0.3133 0.3267 0.2859 0.0083 0.0343 -0.0552 258 ILE A N 1695 C CA . ILE A 217 ? 0.3183 0.3343 0.2832 0.0075 0.0383 -0.0533 258 ILE A CA 1696 C C . ILE A 217 ? 0.3428 0.3573 0.2996 0.0053 0.0348 -0.0495 258 ILE A C 1697 O O . ILE A 217 ? 0.3451 0.3590 0.2909 0.0049 0.0366 -0.0488 258 ILE A O 1698 C CB . ILE A 217 ? 0.3501 0.3652 0.3061 0.0094 0.0425 -0.0583 258 ILE A CB 1699 C CG1 . ILE A 217 ? 0.3344 0.3441 0.2828 0.0101 0.0376 -0.0632 258 ILE A CG1 1700 C CG2 . ILE A 217 ? 0.3263 0.3446 0.2917 0.0116 0.0479 -0.0613 258 ILE A CG2 1701 C CD1 . ILE A 217 ? 0.4280 0.4357 0.3638 0.0124 0.0408 -0.0686 258 ILE A CD1 1702 N N . LEU A 218 ? 0.3437 0.3572 0.3057 0.0042 0.0298 -0.0469 259 LEU A N 1703 C CA . LEU A 218 ? 0.3583 0.3705 0.3145 0.0024 0.0261 -0.0434 259 LEU A CA 1704 C C . LEU A 218 ? 0.3748 0.3897 0.3308 0.0011 0.0283 -0.0382 259 LEU A C 1705 O O . LEU A 218 ? 0.3730 0.3910 0.3367 0.0013 0.0314 -0.0370 259 LEU A O 1706 C CB . LEU A 218 ? 0.3459 0.3568 0.3092 0.0019 0.0212 -0.0418 259 LEU A CB 1707 C CG . LEU A 218 ? 0.3554 0.3630 0.3205 0.0025 0.0181 -0.0461 259 LEU A CG 1708 C CD1 . LEU A 218 ? 0.3842 0.3908 0.3579 0.0021 0.0151 -0.0435 259 LEU A CD1 1709 C CD2 . LEU A 218 ? 0.3999 0.4051 0.3555 0.0021 0.0149 -0.0489 259 LEU A CD2 1710 N N . ASN A 219 ? 0.3729 0.3863 0.3208 -0.0001 0.0263 -0.0354 260 ASN A N 1711 C CA . ASN A 219 ? 0.3686 0.3836 0.3182 -0.0016 0.0269 -0.0301 260 ASN A CA 1712 C C . ASN A 219 ? 0.3624 0.3755 0.3120 -0.0023 0.0211 -0.0277 260 ASN A C 1713 O O . ASN A 219 ? 0.3817 0.3929 0.3234 -0.0030 0.0191 -0.0257 260 ASN A O 1714 C CB . ASN A 219 ? 0.3936 0.4082 0.3334 -0.0022 0.0311 -0.0281 260 ASN A CB 1715 C CG . ASN A 219 ? 0.4473 0.4651 0.3906 -0.0017 0.0383 -0.0291 260 ASN A CG 1716 O OD1 . ASN A 219 ? 0.5030 0.5240 0.4553 -0.0028 0.0410 -0.0264 260 ASN A OD1 1717 N ND2 . ASN A 219 ? 0.4413 0.4585 0.3795 0.0000 0.0410 -0.0337 260 ASN A ND2 1718 N N . LEU A 220 ? 0.3468 0.3602 0.3049 -0.0019 0.0185 -0.0278 261 LEU A N 1719 C CA . LEU A 220 ? 0.3375 0.3494 0.2966 -0.0022 0.0136 -0.0260 261 LEU A CA 1720 C C . LEU A 220 ? 0.3437 0.3560 0.3035 -0.0030 0.0127 -0.0215 261 LEU A C 1721 O O . LEU A 220 ? 0.3272 0.3382 0.2858 -0.0032 0.0091 -0.0198 261 LEU A O 1722 C CB . LEU A 220 ? 0.3414 0.3532 0.3091 -0.0011 0.0124 -0.0269 261 LEU A CB 1723 C CG . LEU A 220 ? 0.3443 0.3545 0.3130 -0.0005 0.0120 -0.0312 261 LEU A CG 1724 C CD1 . LEU A 220 ? 0.3442 0.3536 0.3218 0.0006 0.0118 -0.0311 261 LEU A CD1 1725 C CD2 . LEU A 220 ? 0.3574 0.3658 0.3213 -0.0012 0.0082 -0.0326 261 LEU A CD2 1726 N N . ASN A 221 ? 0.3221 0.3365 0.2858 -0.0034 0.0157 -0.0200 262 ASN A N 1727 C CA . ASN A 221 ? 0.3292 0.3436 0.2955 -0.0040 0.0143 -0.0163 262 ASN A CA 1728 C C . ASN A 221 ? 0.3193 0.3327 0.2894 -0.0029 0.0102 -0.0155 262 ASN A C 1729 O O . ASN A 221 ? 0.3281 0.3401 0.2964 -0.0032 0.0076 -0.0132 262 ASN A O 1730 C CB . ASN A 221 ? 0.3265 0.3391 0.2849 -0.0055 0.0142 -0.0134 262 ASN A CB 1731 C CG . ASN A 221 ? 0.3982 0.4117 0.3531 -0.0065 0.0196 -0.0131 262 ASN A CG 1732 O OD1 . ASN A 221 ? 0.4345 0.4509 0.3964 -0.0066 0.0231 -0.0138 262 ASN A OD1 1733 N ND2 . ASN A 221 ? 0.3987 0.4099 0.3429 -0.0068 0.0203 -0.0123 262 ASN A ND2 1734 N N . GLY A 222 ? 0.3005 0.3142 0.2752 -0.0012 0.0100 -0.0174 263 GLY A N 1735 C CA . GLY A 222 ? 0.3051 0.3176 0.2826 0.0002 0.0073 -0.0164 263 GLY A CA 1736 C C . GLY A 222 ? 0.3072 0.3182 0.2832 0.0003 0.0054 -0.0165 263 GLY A C 1737 O O . GLY A 222 ? 0.2941 0.3042 0.2724 0.0017 0.0041 -0.0152 263 GLY A O 1738 N N . ALA A 223 ? 0.2901 0.3008 0.2625 -0.0008 0.0052 -0.0182 264 ALA A N 1739 C CA . ALA A 223 ? 0.3064 0.3162 0.2790 -0.0010 0.0025 -0.0186 264 ALA A CA 1740 C C . ALA A 223 ? 0.2890 0.2982 0.2680 0.0000 0.0031 -0.0200 264 ALA A C 1741 O O . ALA A 223 ? 0.3175 0.3264 0.2999 0.0000 0.0014 -0.0193 264 ALA A O 1742 C CB . ALA A 223 ? 0.3001 0.3093 0.2663 -0.0022 0.0009 -0.0206 264 ALA A CB 1743 N N . GLY A 224 ? 0.2798 0.2888 0.2612 0.0006 0.0055 -0.0215 265 GLY A N 1744 C CA . GLY A 224 ? 0.2904 0.2978 0.2777 0.0013 0.0062 -0.0225 265 GLY A CA 1745 C C . GLY A 224 ? 0.2938 0.3005 0.2814 0.0000 0.0049 -0.0263 265 GLY A C 1746 O O . GLY A 224 ? 0.3119 0.3190 0.2940 -0.0007 0.0047 -0.0288 265 GLY A O 1747 N N . ASP A 225 ? 0.2885 0.2940 0.2828 -0.0003 0.0041 -0.0268 266 ASP A N 1748 C CA . ASP A 225 ? 0.2968 0.3013 0.2931 -0.0016 0.0019 -0.0312 266 ASP A CA 1749 C C . ASP A 225 ? 0.3100 0.3154 0.2985 -0.0025 -0.0015 -0.0330 266 ASP A C 1750 O O . ASP A 225 ? 0.2945 0.3012 0.2816 -0.0028 -0.0037 -0.0306 266 ASP A O 1751 C CB . ASP A 225 ? 0.2976 0.3014 0.3039 -0.0022 0.0011 -0.0305 266 ASP A CB 1752 C CG . ASP A 225 ? 0.3171 0.3203 0.3272 -0.0038 -0.0026 -0.0352 266 ASP A CG 1753 O OD1 . ASP A 225 ? 0.3168 0.3183 0.3242 -0.0038 -0.0033 -0.0396 266 ASP A OD1 1754 O OD2 . ASP A 225 ? 0.3310 0.3353 0.3475 -0.0047 -0.0052 -0.0348 266 ASP A OD2 1755 N N . PRO A 226 ? 0.3240 0.3285 0.3065 -0.0025 -0.0019 -0.0371 267 PRO A N 1756 C CA . PRO A 226 ? 0.3451 0.3496 0.3178 -0.0027 -0.0049 -0.0386 267 PRO A CA 1757 C C . PRO A 226 ? 0.3221 0.3265 0.2968 -0.0034 -0.0106 -0.0395 267 PRO A C 1758 O O . PRO A 226 ? 0.3490 0.3535 0.3158 -0.0032 -0.0134 -0.0387 267 PRO A O 1759 C CB . PRO A 226 ? 0.3448 0.3474 0.3128 -0.0021 -0.0044 -0.0441 267 PRO A CB 1760 C CG . PRO A 226 ? 0.3588 0.3614 0.3319 -0.0015 0.0002 -0.0440 267 PRO A CG 1761 C CD . PRO A 226 ? 0.3221 0.3251 0.3057 -0.0018 0.0008 -0.0403 267 PRO A CD 1762 N N . LEU A 227 ? 0.3174 0.3217 0.3035 -0.0041 -0.0122 -0.0411 268 LEU A N 1763 C CA . LEU A 227 ? 0.3090 0.3140 0.2997 -0.0047 -0.0180 -0.0426 268 LEU A CA 1764 C C . LEU A 227 ? 0.2964 0.3038 0.2932 -0.0049 -0.0182 -0.0378 268 LEU A C 1765 O O . LEU A 227 ? 0.3078 0.3164 0.3079 -0.0051 -0.0233 -0.0387 268 LEU A O 1766 C CB . LEU A 227 ? 0.2975 0.3012 0.2996 -0.0057 -0.0198 -0.0471 268 LEU A CB 1767 C CG . LEU A 227 ? 0.3192 0.3199 0.3153 -0.0051 -0.0202 -0.0529 268 LEU A CG 1768 C CD1 . LEU A 227 ? 0.3600 0.3591 0.3687 -0.0063 -0.0237 -0.0578 268 LEU A CD1 1769 C CD2 . LEU A 227 ? 0.3581 0.3578 0.3384 -0.0038 -0.0236 -0.0558 268 LEU A CD2 1770 N N . THR A 228 ? 0.2898 0.2980 0.2884 -0.0044 -0.0133 -0.0332 269 THR A N 1771 C CA . THR A 228 ? 0.2879 0.2981 0.2929 -0.0041 -0.0130 -0.0292 269 THR A CA 1772 C C . THR A 228 ? 0.2844 0.2950 0.2827 -0.0029 -0.0105 -0.0248 269 THR A C 1773 O O . THR A 228 ? 0.2758 0.2869 0.2783 -0.0019 -0.0072 -0.0215 269 THR A O 1774 C CB . THR A 228 ? 0.2837 0.2940 0.3015 -0.0043 -0.0093 -0.0278 269 THR A CB 1775 O OG1 . THR A 228 ? 0.2689 0.2773 0.2843 -0.0035 -0.0044 -0.0265 269 THR A OG1 1776 C CG2 . THR A 228 ? 0.2602 0.2703 0.2885 -0.0059 -0.0121 -0.0321 269 THR A CG2 1777 N N . PRO A 229 ? 0.3040 0.3140 0.2914 -0.0028 -0.0118 -0.0246 270 PRO A N 1778 C CA . PRO A 229 ? 0.2882 0.2982 0.2709 -0.0020 -0.0094 -0.0208 270 PRO A CA 1779 C C . PRO A 229 ? 0.2992 0.3103 0.2861 -0.0010 -0.0105 -0.0177 270 PRO A C 1780 O O . PRO A 229 ? 0.3010 0.3128 0.2895 -0.0011 -0.0144 -0.0181 270 PRO A O 1781 C CB . PRO A 229 ? 0.3028 0.3117 0.2745 -0.0024 -0.0109 -0.0210 270 PRO A CB 1782 C CG . PRO A 229 ? 0.3184 0.3269 0.2886 -0.0027 -0.0160 -0.0241 270 PRO A CG 1783 C CD . PRO A 229 ? 0.3148 0.3237 0.2938 -0.0032 -0.0156 -0.0276 270 PRO A CD 1784 N N . GLY A 230 ? 0.2915 0.3026 0.2806 0.0002 -0.0071 -0.0152 271 GLY A N 1785 C CA . GLY A 230 ? 0.2876 0.2993 0.2797 0.0017 -0.0074 -0.0125 271 GLY A CA 1786 C C . GLY A 230 ? 0.3016 0.3142 0.3029 0.0027 -0.0048 -0.0118 271 GLY A C 1787 O O . GLY A 230 ? 0.3097 0.3225 0.3127 0.0047 -0.0035 -0.0096 271 GLY A O 1788 N N . TYR A 231 ? 0.2706 0.2836 0.2781 0.0014 -0.0043 -0.0138 272 TYR A N 1789 C CA . TYR A 231 ? 0.2749 0.2889 0.2931 0.0019 -0.0017 -0.0128 272 TYR A CA 1790 C C . TYR A 231 ? 0.2614 0.2737 0.2833 0.0012 0.0015 -0.0136 272 TYR A C 1791 O O . TYR A 231 ? 0.2787 0.2900 0.2979 -0.0001 0.0000 -0.0165 272 TYR A O 1792 C CB . TYR A 231 ? 0.2668 0.2835 0.2934 0.0006 -0.0057 -0.0146 272 TYR A CB 1793 C CG . TYR A 231 ? 0.2862 0.3040 0.3080 0.0015 -0.0097 -0.0139 272 TYR A CG 1794 C CD1 . TYR A 231 ? 0.2754 0.2942 0.2999 0.0036 -0.0081 -0.0112 272 TYR A CD1 1795 C CD2 . TYR A 231 ? 0.2886 0.3055 0.3021 0.0005 -0.0147 -0.0157 272 TYR A CD2 1796 C CE1 . TYR A 231 ? 0.2696 0.2888 0.2901 0.0045 -0.0120 -0.0106 272 TYR A CE1 1797 C CE2 . TYR A 231 ? 0.3090 0.3258 0.3175 0.0014 -0.0182 -0.0145 272 TYR A CE2 1798 C CZ . TYR A 231 ? 0.2981 0.3160 0.3106 0.0034 -0.0170 -0.0120 272 TYR A CZ 1799 O OH . TYR A 231 ? 0.2874 0.3046 0.2956 0.0044 -0.0207 -0.0107 272 TYR A OH 1800 N N . PRO A 232 ? 0.2889 0.3004 0.3171 0.0024 0.0063 -0.0109 273 PRO A N 1801 C CA . PRO A 232 ? 0.2856 0.2946 0.3174 0.0020 0.0094 -0.0111 273 PRO A CA 1802 C C . PRO A 232 ? 0.2856 0.2952 0.3275 -0.0008 0.0071 -0.0146 273 PRO A C 1803 O O . PRO A 232 ? 0.2775 0.2899 0.3282 -0.0020 0.0050 -0.0154 273 PRO A O 1804 C CB . PRO A 232 ? 0.2797 0.2873 0.3155 0.0043 0.0153 -0.0066 273 PRO A CB 1805 C CG . PRO A 232 ? 0.2992 0.3102 0.3400 0.0048 0.0150 -0.0053 273 PRO A CG 1806 C CD . PRO A 232 ? 0.2853 0.2978 0.3171 0.0046 0.0093 -0.0075 273 PRO A CD 1807 N N . ALA A 233 ? 0.2612 0.2682 0.3022 -0.0017 0.0072 -0.0170 274 ALA A N 1808 C CA . ALA A 233 ? 0.2757 0.2823 0.3258 -0.0042 0.0048 -0.0211 274 ALA A CA 1809 C C . ALA A 233 ? 0.2838 0.2891 0.3479 -0.0049 0.0090 -0.0188 274 ALA A C 1810 O O . ALA A 233 ? 0.2877 0.2896 0.3564 -0.0054 0.0112 -0.0194 274 ALA A O 1811 C CB . ALA A 233 ? 0.2916 0.2955 0.3350 -0.0044 0.0038 -0.0247 274 ALA A CB 1812 N N . ASN A 234 ? 0.2881 0.2962 0.3598 -0.0048 0.0105 -0.0161 275 ASN A N 1813 C CA . ASN A 234 ? 0.3173 0.3248 0.4031 -0.0054 0.0158 -0.0129 275 ASN A CA 1814 C C . ASN A 234 ? 0.3384 0.3475 0.4404 -0.0088 0.0121 -0.0172 275 ASN A C 1815 O O . ASN A 234 ? 0.3252 0.3351 0.4249 -0.0102 0.0050 -0.0230 275 ASN A O 1816 C CB . ASN A 234 ? 0.3257 0.3357 0.4127 -0.0033 0.0200 -0.0080 275 ASN A CB 1817 C CG . ASN A 234 ? 0.3295 0.3448 0.4193 -0.0039 0.0148 -0.0102 275 ASN A CG 1818 O OD1 . ASN A 234 ? 0.3722 0.3898 0.4686 -0.0063 0.0086 -0.0150 275 ASN A OD1 1819 N ND2 . ASN A 234 ? 0.4187 0.4357 0.5033 -0.0012 0.0171 -0.0069 275 ASN A ND2 1820 N N . GLU A 235 ? 0.3626 0.3723 0.4811 -0.0100 0.0166 -0.0145 276 GLU A N 1821 C CA A GLU A 235 ? 0.3765 0.3871 0.5125 -0.0136 0.0129 -0.0189 276 GLU A CA 1822 C CA B GLU A 235 ? 0.3840 0.3949 0.5214 -0.0136 0.0134 -0.0184 276 GLU A CA 1823 C C . GLU A 235 ? 0.3864 0.4025 0.5279 -0.0148 0.0048 -0.0238 276 GLU A C 1824 O O . GLU A 235 ? 0.4066 0.4229 0.5575 -0.0173 -0.0014 -0.0297 276 GLU A O 1825 C CB A GLU A 235 ? 0.3886 0.3982 0.5434 -0.0150 0.0202 -0.0146 276 GLU A CB 1826 C CB B GLU A 235 ? 0.3982 0.4099 0.5541 -0.0145 0.0211 -0.0133 276 GLU A CB 1827 C CG A GLU A 235 ? 0.4272 0.4300 0.5818 -0.0150 0.0255 -0.0121 276 GLU A CG 1828 C CG B GLU A 235 ? 0.4507 0.4668 0.6057 -0.0122 0.0254 -0.0084 276 GLU A CG 1829 C CD A GLU A 235 ? 0.4653 0.4655 0.6316 -0.0183 0.0209 -0.0180 276 GLU A CD 1830 C CD B GLU A 235 ? 0.5102 0.5314 0.6875 -0.0139 0.0281 -0.0070 276 GLU A CD 1831 O OE1 A GLU A 235 ? 0.5030 0.5063 0.6762 -0.0205 0.0128 -0.0247 276 GLU A OE1 1832 O OE1 B GLU A 235 ? 0.5364 0.5604 0.7309 -0.0173 0.0228 -0.0118 276 GLU A OE1 1833 O OE2 A GLU A 235 ? 0.4934 0.4877 0.6619 -0.0185 0.0251 -0.0159 276 GLU A OE2 1834 O OE2 B GLU A 235 ? 0.5424 0.5652 0.7196 -0.0115 0.0355 -0.0013 276 GLU A OE2 1835 N N . TYR A 236 ? 0.3616 0.3817 0.4976 -0.0129 0.0043 -0.0217 277 TYR A N 1836 C CA . TYR A 236 ? 0.3689 0.3939 0.5105 -0.0137 -0.0036 -0.0259 277 TYR A CA 1837 C C . TYR A 236 ? 0.3673 0.3920 0.4899 -0.0120 -0.0100 -0.0284 277 TYR A C 1838 O O . TYR A 236 ? 0.3773 0.4056 0.5011 -0.0117 -0.0163 -0.0307 277 TYR A O 1839 C CB . TYR A 236 ? 0.3523 0.3825 0.5065 -0.0129 -0.0002 -0.0223 277 TYR A CB 1840 C CG . TYR A 236 ? 0.3516 0.3814 0.4935 -0.0096 0.0062 -0.0163 277 TYR A CG 1841 C CD1 . TYR A 236 ? 0.3918 0.4233 0.5209 -0.0073 0.0022 -0.0165 277 TYR A CD1 1842 C CD2 . TYR A 236 ? 0.3472 0.3743 0.4898 -0.0084 0.0161 -0.0105 277 TYR A CD2 1843 C CE1 . TYR A 236 ? 0.3834 0.4140 0.5013 -0.0040 0.0076 -0.0118 277 TYR A CE1 1844 C CE2 . TYR A 236 ? 0.3883 0.4146 0.5183 -0.0047 0.0214 -0.0057 277 TYR A CE2 1845 C CZ . TYR A 236 ? 0.3909 0.4190 0.5090 -0.0027 0.0167 -0.0068 277 TYR A CZ 1846 O OH . TYR A 236 ? 0.4316 0.4585 0.5380 0.0009 0.0211 -0.0029 277 TYR A OH 1847 N N . ALA A 237 ? 0.3558 0.3764 0.4619 -0.0109 -0.0084 -0.0280 278 ALA A N 1848 C CA . ALA A 237 ? 0.3802 0.4002 0.4680 -0.0093 -0.0126 -0.0292 278 ALA A CA 1849 C C . ALA A 237 ? 0.3818 0.4022 0.4676 -0.0102 -0.0218 -0.0355 278 ALA A C 1850 O O . ALA A 237 ? 0.4028 0.4219 0.4963 -0.0120 -0.0249 -0.0402 278 ALA A O 1851 C CB . ALA A 237 ? 0.3828 0.3985 0.4569 -0.0084 -0.0090 -0.0282 278 ALA A CB 1852 N N . TYR A 238 ? 0.3793 0.4011 0.4551 -0.0088 -0.0265 -0.0356 279 TYR A N 1853 C CA . TYR A 238 ? 0.4065 0.4277 0.4758 -0.0088 -0.0353 -0.0411 279 TYR A CA 1854 C C . TYR A 238 ? 0.4013 0.4184 0.4521 -0.0080 -0.0340 -0.0417 279 TYR A C 1855 O O . TYR A 238 ? 0.4114 0.4278 0.4525 -0.0069 -0.0291 -0.0373 279 TYR A O 1856 C CB . TYR A 238 ? 0.4305 0.4542 0.4967 -0.0073 -0.0412 -0.0405 279 TYR A CB 1857 C CG A TYR A 238 ? 0.3991 0.4217 0.4597 -0.0069 -0.0511 -0.0463 279 TYR A CG 1858 C CG B TYR A 238 ? 0.4435 0.4641 0.4899 -0.0058 -0.0467 -0.0425 279 TYR A CG 1859 C CD1 A TYR A 238 ? 0.3976 0.4217 0.4726 -0.0080 -0.0574 -0.0518 279 TYR A CD1 1860 C CD1 B TYR A 238 ? 0.4747 0.4949 0.5191 -0.0052 -0.0560 -0.0475 279 TYR A CD1 1861 C CD2 A TYR A 238 ? 0.4097 0.4291 0.4500 -0.0051 -0.0539 -0.0464 279 TYR A CD2 1862 C CD2 B TYR A 238 ? 0.4787 0.4966 0.5088 -0.0049 -0.0423 -0.0394 279 TYR A CD2 1863 C CE1 A TYR A 238 ? 0.4312 0.4537 0.4994 -0.0070 -0.0672 -0.0576 279 TYR A CE1 1864 C CE1 B TYR A 238 ? 0.5011 0.5177 0.5258 -0.0034 -0.0601 -0.0487 279 TYR A CE1 1865 C CE2 A TYR A 238 ? 0.4397 0.4572 0.4723 -0.0040 -0.0628 -0.0514 279 TYR A CE2 1866 C CE2 B TYR A 238 ? 0.4936 0.5085 0.5062 -0.0037 -0.0458 -0.0404 279 TYR A CE2 1867 C CZ A TYR A 238 ? 0.4480 0.4669 0.4938 -0.0047 -0.0697 -0.0572 279 TYR A CZ 1868 C CZ B TYR A 238 ? 0.5130 0.5270 0.5220 -0.0028 -0.0544 -0.0448 279 TYR A CZ 1869 O OH A TYR A 238 ? 0.5133 0.5297 0.5495 -0.0030 -0.0791 -0.0626 279 TYR A OH 1870 O OH B TYR A 238 ? 0.5476 0.5578 0.5375 -0.0011 -0.0573 -0.0453 279 TYR A OH 1871 N N . ARG A 239 ? 0.3790 0.3935 0.4261 -0.0085 -0.0378 -0.0472 280 ARG A N 1872 C CA . ARG A 239 ? 0.3841 0.3951 0.4150 -0.0077 -0.0357 -0.0481 280 ARG A CA 1873 C C . ARG A 239 ? 0.4037 0.4131 0.4194 -0.0062 -0.0418 -0.0511 280 ARG A C 1874 O O . ARG A 239 ? 0.3705 0.3799 0.3885 -0.0060 -0.0495 -0.0556 280 ARG A O 1875 C CB . ARG A 239 ? 0.3995 0.4077 0.4358 -0.0087 -0.0342 -0.0523 280 ARG A CB 1876 C CG . ARG A 239 ? 0.4029 0.4113 0.4503 -0.0097 -0.0269 -0.0482 280 ARG A CG 1877 C CD . ARG A 239 ? 0.4289 0.4337 0.4816 -0.0105 -0.0249 -0.0516 280 ARG A CD 1878 N NE . ARG A 239 ? 0.4928 0.4973 0.5518 -0.0105 -0.0172 -0.0458 280 ARG A NE 1879 C CZ . ARG A 239 ? 0.4999 0.5056 0.5740 -0.0117 -0.0145 -0.0427 280 ARG A CZ 1880 N NH1 . ARG A 239 ? 0.5243 0.5322 0.6114 -0.0133 -0.0192 -0.0455 280 ARG A NH1 1881 N NH2 . ARG A 239 ? 0.4635 0.4682 0.5401 -0.0110 -0.0072 -0.0370 280 ARG A NH2 1882 N N . ARG A 240 ? 0.3988 0.4066 0.3986 -0.0050 -0.0387 -0.0485 281 ARG A N 1883 C CA . ARG A 240 ? 0.4326 0.4377 0.4159 -0.0034 -0.0431 -0.0513 281 ARG A CA 1884 C C . ARG A 240 ? 0.4426 0.4448 0.4236 -0.0032 -0.0461 -0.0585 281 ARG A C 1885 O O . ARG A 240 ? 0.4335 0.4353 0.4230 -0.0043 -0.0425 -0.0603 281 ARG A O 1886 C CB . ARG A 240 ? 0.4255 0.4293 0.3946 -0.0026 -0.0373 -0.0472 281 ARG A CB 1887 C CG . ARG A 240 ? 0.4428 0.4484 0.4120 -0.0025 -0.0357 -0.0410 281 ARG A CG 1888 C CD . ARG A 240 ? 0.4822 0.4864 0.4386 -0.0020 -0.0307 -0.0374 281 ARG A CD 1889 N NE . ARG A 240 ? 0.4786 0.4837 0.4343 -0.0018 -0.0305 -0.0321 281 ARG A NE 1890 C CZ . ARG A 240 ? 0.5250 0.5286 0.4704 -0.0014 -0.0278 -0.0283 281 ARG A CZ 1891 N NH1 . ARG A 240 ? 0.5160 0.5176 0.4506 -0.0012 -0.0248 -0.0291 281 ARG A NH1 1892 N NH2 . ARG A 240 ? 0.5545 0.5586 0.5012 -0.0012 -0.0280 -0.0238 281 ARG A NH2 1893 N N . GLY A 241 ? 0.4728 0.4727 0.4421 -0.0014 -0.0529 -0.0626 282 GLY A N 1894 C CA . GLY A 241 ? 0.5069 0.5030 0.4691 -0.0003 -0.0553 -0.0697 282 GLY A CA 1895 C C . GLY A 241 ? 0.5216 0.5160 0.4710 0.0004 -0.0473 -0.0679 282 GLY A C 1896 O O . GLY A 241 ? 0.5094 0.5048 0.4519 0.0005 -0.0421 -0.0617 282 GLY A O 1897 N N . ILE A 242 ? 0.5489 0.5406 0.4964 0.0010 -0.0463 -0.0736 283 ILE A N 1898 C CA . ILE A 242 ? 0.5703 0.5607 0.5069 0.0021 -0.0387 -0.0729 283 ILE A CA 1899 C C . ILE A 242 ? 0.5814 0.5704 0.4980 0.0041 -0.0371 -0.0699 283 ILE A C 1900 O O . ILE A 242 ? 0.5783 0.5684 0.4903 0.0040 -0.0295 -0.0654 283 ILE A O 1901 C CB A ILE A 242 ? 0.5833 0.5704 0.5201 0.0031 -0.0393 -0.0808 283 ILE A CB 1902 C CB B ILE A 242 ? 0.5754 0.5624 0.5115 0.0032 -0.0389 -0.0807 283 ILE A CB 1903 C CG1 A ILE A 242 ? 0.5907 0.5780 0.5271 0.0032 -0.0303 -0.0794 283 ILE A CG1 1904 C CG1 B ILE A 242 ? 0.5660 0.5539 0.5221 0.0009 -0.0371 -0.0817 283 ILE A CG1 1905 C CG2 A ILE A 242 ? 0.6163 0.5992 0.5362 0.0062 -0.0455 -0.0875 283 ILE A CG2 1906 C CG2 B ILE A 242 ? 0.5726 0.5583 0.4944 0.0051 -0.0317 -0.0807 283 ILE A CG2 1907 C CD1 A ILE A 242 ? 0.5623 0.5525 0.5160 0.0007 -0.0257 -0.0746 283 ILE A CD1 1908 C CD1 B ILE A 242 ? 0.5401 0.5303 0.5016 0.0000 -0.0283 -0.0756 283 ILE A CD1 1909 N N . ALA A 243 ? 0.6040 0.5907 0.5096 0.0060 -0.0443 -0.0720 284 ALA A N 1910 C CA . ALA A 243 ? 0.6203 0.6047 0.5057 0.0082 -0.0425 -0.0684 284 ALA A CA 1911 C C . ALA A 243 ? 0.6194 0.6064 0.5064 0.0067 -0.0383 -0.0595 284 ALA A C 1912 O O . ALA A 243 ? 0.6366 0.6222 0.5103 0.0077 -0.0335 -0.0553 284 ALA A O 1913 C CB . ALA A 243 ? 0.6477 0.6280 0.5193 0.0113 -0.0521 -0.0726 284 ALA A CB 1914 N N . GLU A 244 ? 0.5939 0.5844 0.4972 0.0045 -0.0400 -0.0567 285 GLU A N 1915 C CA . GLU A 244 ? 0.5889 0.5815 0.4945 0.0034 -0.0367 -0.0490 285 GLU A CA 1916 C C . GLU A 244 ? 0.5580 0.5540 0.4758 0.0012 -0.0291 -0.0460 285 GLU A C 1917 O O . GLU A 244 ? 0.5673 0.5652 0.4892 0.0002 -0.0265 -0.0403 285 GLU A O 1918 C CB . GLU A 244 ? 0.6006 0.5947 0.5144 0.0031 -0.0438 -0.0476 285 GLU A CB 1919 C CG . GLU A 244 ? 0.6723 0.6631 0.5727 0.0057 -0.0514 -0.0481 285 GLU A CG 1920 C CD . GLU A 244 ? 0.7976 0.7860 0.6941 0.0075 -0.0592 -0.0561 285 GLU A CD 1921 O OE1 . GLU A 244 ? 0.8207 0.8110 0.7316 0.0062 -0.0613 -0.0613 285 GLU A OE1 1922 O OE2 . GLU A 244 ? 0.8722 0.8561 0.7507 0.0105 -0.0634 -0.0574 285 GLU A OE2 1923 N N . ALA A 245 ? 0.5392 0.5354 0.4624 0.0009 -0.0261 -0.0500 286 ALA A N 1924 C CA . ALA A 245 ? 0.5170 0.5156 0.4513 -0.0005 -0.0199 -0.0476 286 ALA A CA 1925 C C . ALA A 245 ? 0.5150 0.5145 0.4430 -0.0005 -0.0134 -0.0424 286 ALA A C 1926 O O . ALA A 245 ? 0.5201 0.5179 0.4348 0.0004 -0.0118 -0.0419 286 ALA A O 1927 C CB . ALA A 245 ? 0.5064 0.5041 0.4454 -0.0003 -0.0181 -0.0527 286 ALA A CB 1928 N N . VAL A 246 ? 0.4769 0.4789 0.4146 -0.0016 -0.0099 -0.0385 287 VAL A N 1929 C CA . VAL A 246 ? 0.4702 0.4734 0.4049 -0.0019 -0.0046 -0.0341 287 VAL A CA 1930 C C . VAL A 246 ? 0.4551 0.4588 0.3900 -0.0014 0.0010 -0.0362 287 VAL A C 1931 O O . VAL A 246 ? 0.4400 0.4442 0.3833 -0.0013 0.0017 -0.0389 287 VAL A O 1932 C CB . VAL A 246 ? 0.4562 0.4614 0.4007 -0.0027 -0.0040 -0.0297 287 VAL A CB 1933 C CG1 . VAL A 246 ? 0.4566 0.4629 0.3997 -0.0030 0.0008 -0.0258 287 VAL A CG1 1934 C CG2 . VAL A 246 ? 0.4849 0.4897 0.4295 -0.0027 -0.0093 -0.0277 287 VAL A CG2 1935 N N . GLY A 247 ? 0.4478 0.4513 0.3736 -0.0011 0.0051 -0.0349 288 GLY A N 1936 C CA . GLY A 247 ? 0.4405 0.4460 0.3693 -0.0008 0.0114 -0.0355 288 GLY A CA 1937 C C . GLY A 247 ? 0.4389 0.4435 0.3646 0.0006 0.0136 -0.0412 288 GLY A C 1938 O O . GLY A 247 ? 0.4274 0.4339 0.3567 0.0011 0.0190 -0.0418 288 GLY A O 1939 N N . LEU A 248 ? 0.4331 0.4347 0.3526 0.0016 0.0094 -0.0457 289 LEU A N 1940 C CA . LEU A 248 ? 0.4381 0.4381 0.3544 0.0034 0.0108 -0.0521 289 LEU A CA 1941 C C . LEU A 248 ? 0.4565 0.4558 0.3591 0.0050 0.0160 -0.0525 289 LEU A C 1942 O O . LEU A 248 ? 0.4616 0.4593 0.3522 0.0053 0.0155 -0.0498 289 LEU A O 1943 C CB A LEU A 248 ? 0.4405 0.4372 0.3553 0.0040 0.0037 -0.0575 289 LEU A CB 1944 C CB B LEU A 248 ? 0.4424 0.4391 0.3570 0.0040 0.0037 -0.0575 289 LEU A CB 1945 C CG A LEU A 248 ? 0.4500 0.4471 0.3781 0.0023 -0.0014 -0.0569 289 LEU A CG 1946 C CG B LEU A 248 ? 0.4430 0.4396 0.3725 0.0030 0.0004 -0.0599 289 LEU A CG 1947 C CD1 A LEU A 248 ? 0.4541 0.4482 0.3809 0.0029 -0.0085 -0.0628 289 LEU A CD1 1948 C CD1 B LEU A 248 ? 0.4304 0.4292 0.3698 0.0010 -0.0013 -0.0542 289 LEU A CD1 1949 C CD2 A LEU A 248 ? 0.4270 0.4255 0.3690 0.0018 0.0018 -0.0569 289 LEU A CD2 1950 C CD2 B LEU A 248 ? 0.4308 0.4239 0.3578 0.0039 -0.0060 -0.0665 289 LEU A CD2 1951 N N . PRO A 249 ? 0.4657 0.4658 0.3696 0.0065 0.0212 -0.0561 290 PRO A N 1952 C CA . PRO A 249 ? 0.4783 0.4777 0.3691 0.0084 0.0273 -0.0570 290 PRO A CA 1953 C C . PRO A 249 ? 0.4937 0.4881 0.3684 0.0110 0.0234 -0.0621 290 PRO A C 1954 O O . PRO A 249 ? 0.4955 0.4874 0.3725 0.0115 0.0167 -0.0675 290 PRO A O 1955 C CB . PRO A 249 ? 0.4887 0.4907 0.3882 0.0096 0.0333 -0.0602 290 PRO A CB 1956 C CG . PRO A 249 ? 0.4747 0.4760 0.3870 0.0092 0.0281 -0.0636 290 PRO A CG 1957 C CD . PRO A 249 ? 0.4649 0.4661 0.3822 0.0067 0.0219 -0.0595 290 PRO A CD 1958 N N . SER A 250 ? 0.5050 0.4977 0.3636 0.0127 0.0276 -0.0606 291 SER A N 1959 C CA A SER A 250 ? 0.5240 0.5112 0.3638 0.0159 0.0239 -0.0652 291 SER A CA 1960 C CA B SER A 250 ? 0.5262 0.5134 0.3664 0.0159 0.0237 -0.0654 291 SER A CA 1961 C C . SER A 250 ? 0.5305 0.5161 0.3618 0.0195 0.0292 -0.0717 291 SER A C 1962 O O . SER A 250 ? 0.5474 0.5280 0.3627 0.0228 0.0260 -0.0770 291 SER A O 1963 C CB A SER A 250 ? 0.5441 0.5288 0.3680 0.0163 0.0245 -0.0591 291 SER A CB 1964 C CB B SER A 250 ? 0.5464 0.5310 0.3712 0.0162 0.0234 -0.0595 291 SER A CB 1965 O OG A SER A 250 ? 0.5547 0.5409 0.3727 0.0167 0.0350 -0.0546 291 SER A OG 1966 O OG B SER A 250 ? 0.5545 0.5395 0.3866 0.0137 0.0158 -0.0561 291 SER A OG 1967 N N . ILE A 251 ? 0.5077 0.4975 0.3497 0.0191 0.0371 -0.0716 292 ILE A N 1968 C CA . ILE A 251 ? 0.5115 0.5004 0.3469 0.0228 0.0433 -0.0778 292 ILE A CA 1969 C C . ILE A 251 ? 0.4950 0.4864 0.3487 0.0225 0.0434 -0.0824 292 ILE A C 1970 O O . ILE A 251 ? 0.4835 0.4788 0.3543 0.0194 0.0427 -0.0785 292 ILE A O 1971 C CB . ILE A 251 ? 0.5173 0.5087 0.3452 0.0239 0.0552 -0.0732 292 ILE A CB 1972 C CG1 . ILE A 251 ? 0.4924 0.4904 0.3383 0.0201 0.0603 -0.0661 292 ILE A CG1 1973 C CG2 . ILE A 251 ? 0.5610 0.5478 0.3665 0.0253 0.0554 -0.0693 292 ILE A CG2 1974 C CD1 . ILE A 251 ? 0.5547 0.5561 0.3975 0.0206 0.0727 -0.0615 292 ILE A CD1 1975 N N . PRO A 252 ? 0.5032 0.4919 0.3529 0.0260 0.0438 -0.0907 293 PRO A N 1976 C CA . PRO A 252 ? 0.4916 0.4818 0.3591 0.0259 0.0437 -0.0950 293 PRO A CA 1977 C C . PRO A 252 ? 0.4705 0.4670 0.3503 0.0255 0.0529 -0.0914 293 PRO A C 1978 O O . PRO A 252 ? 0.4712 0.4703 0.3435 0.0266 0.0616 -0.0887 293 PRO A O 1979 C CB . PRO A 252 ? 0.5089 0.4942 0.3664 0.0303 0.0430 -0.1049 293 PRO A CB 1980 C CG . PRO A 252 ? 0.5343 0.5143 0.3705 0.0320 0.0379 -0.1065 293 PRO A CG 1981 C CD . PRO A 252 ? 0.5256 0.5084 0.3544 0.0303 0.0426 -0.0973 293 PRO A CD 1982 N N . VAL A 253 ? 0.4435 0.4422 0.3421 0.0240 0.0511 -0.0914 294 VAL A N 1983 C CA . VAL A 253 ? 0.4167 0.4216 0.3301 0.0235 0.0576 -0.0879 294 VAL A CA 1984 C C . VAL A 253 ? 0.4085 0.4125 0.3358 0.0250 0.0559 -0.0931 294 VAL A C 1985 O O . VAL A 253 ? 0.3974 0.3972 0.3291 0.0243 0.0485 -0.0954 294 VAL A O 1986 C CB . VAL A 253 ? 0.4105 0.4190 0.3336 0.0195 0.0557 -0.0796 294 VAL A CB 1987 C CG1 . VAL A 253 ? 0.3910 0.4059 0.3288 0.0193 0.0618 -0.0765 294 VAL A CG1 1988 C CG2 . VAL A 253 ? 0.4070 0.4152 0.3168 0.0177 0.0560 -0.0741 294 VAL A CG2 1989 N N . HIS A 254 ? 0.4026 0.4103 0.3377 0.0273 0.0628 -0.0948 295 HIS A N 1990 C CA . HIS A 254 ? 0.3924 0.3991 0.3412 0.0291 0.0614 -0.0993 295 HIS A CA 1991 C C . HIS A 254 ? 0.3895 0.4031 0.3523 0.0301 0.0680 -0.0969 295 HIS A C 1992 O O . HIS A 254 ? 0.4092 0.4273 0.3683 0.0309 0.0759 -0.0958 295 HIS A O 1993 C CB . HIS A 254 ? 0.4151 0.4166 0.3552 0.0330 0.0615 -0.1086 295 HIS A CB 1994 C CG . HIS A 254 ? 0.4133 0.4114 0.3662 0.0348 0.0582 -0.1138 295 HIS A CG 1995 N ND1 . HIS A 254 ? 0.3937 0.3876 0.3546 0.0326 0.0502 -0.1129 295 HIS A ND1 1996 C CD2 . HIS A 254 ? 0.4201 0.4181 0.3797 0.0386 0.0621 -0.1194 295 HIS A CD2 1997 C CE1 . HIS A 254 ? 0.4122 0.4030 0.3838 0.0348 0.0493 -0.1175 295 HIS A CE1 1998 N NE2 . HIS A 254 ? 0.4196 0.4129 0.3908 0.0386 0.0561 -0.1217 295 HIS A NE2 1999 N N . PRO A 255 ? 0.3685 0.3827 0.3474 0.0300 0.0649 -0.0960 296 PRO A N 2000 C CA . PRO A 255 ? 0.3554 0.3759 0.3487 0.0314 0.0698 -0.0944 296 PRO A CA 2001 C C . PRO A 255 ? 0.3614 0.3808 0.3619 0.0358 0.0721 -0.1014 296 PRO A C 2002 O O . PRO A 255 ? 0.3620 0.3746 0.3615 0.0372 0.0674 -0.1062 296 PRO A O 2003 C CB . PRO A 255 ? 0.3459 0.3666 0.3507 0.0292 0.0636 -0.0889 296 PRO A CB 2004 C CG . PRO A 255 ? 0.3543 0.3669 0.3550 0.0285 0.0561 -0.0908 296 PRO A CG 2005 C CD . PRO A 255 ? 0.3595 0.3683 0.3440 0.0288 0.0566 -0.0957 296 PRO A CD 2006 N N . ILE A 256 ? 0.3682 0.3939 0.3772 0.0380 0.0792 -0.1020 297 ILE A N 2007 C CA . ILE A 256 ? 0.3633 0.3890 0.3804 0.0426 0.0823 -0.1087 297 ILE A CA 2008 C C . ILE A 256 ? 0.3616 0.3949 0.3978 0.0438 0.0851 -0.1062 297 ILE A C 2009 O O . ILE A 256 ? 0.3464 0.3856 0.3878 0.0411 0.0862 -0.1001 297 ILE A O 2010 C CB . ILE A 256 ? 0.3864 0.4123 0.3913 0.0457 0.0903 -0.1147 297 ILE A CB 2011 C CG1 . ILE A 256 ? 0.3863 0.4203 0.3896 0.0448 0.0997 -0.1106 297 ILE A CG1 2012 C CG2 . ILE A 256 ? 0.3819 0.3993 0.3676 0.0455 0.0861 -0.1188 297 ILE A CG2 2013 C CD1 . ILE A 256 ? 0.3827 0.4169 0.3731 0.0484 0.1090 -0.1160 297 ILE A CD1 2014 N N . GLY A 257 ? 0.3551 0.3882 0.4018 0.0482 0.0863 -0.1116 298 GLY A N 2015 C CA . GLY A 257 ? 0.3451 0.3851 0.4109 0.0502 0.0883 -0.1105 298 GLY A CA 2016 C C . GLY A 257 ? 0.3654 0.4133 0.4347 0.0524 0.0990 -0.1132 298 GLY A C 2017 O O . GLY A 257 ? 0.3604 0.4074 0.4152 0.0528 0.1051 -0.1159 298 GLY A O 2018 N N . TYR A 258 ? 0.3530 0.4087 0.4413 0.0541 0.1013 -0.1123 299 TYR A N 2019 C CA . TYR A 258 ? 0.3850 0.4494 0.4793 0.0556 0.1124 -0.1139 299 TYR A CA 2020 C C . TYR A 258 ? 0.3960 0.4596 0.4896 0.0612 0.1189 -0.1224 299 TYR A C 2021 O O . TYR A 258 ? 0.4196 0.4888 0.5115 0.0626 0.1297 -0.1242 299 TYR A O 2022 C CB . TYR A 258 ? 0.3652 0.4396 0.4811 0.0549 0.1134 -0.1100 299 TYR A CB 2023 C CG . TYR A 258 ? 0.3411 0.4166 0.4760 0.0581 0.1066 -0.1112 299 TYR A CG 2024 C CD1 . TYR A 258 ? 0.3404 0.4132 0.4794 0.0561 0.0962 -0.1063 299 TYR A CD1 2025 C CD2 . TYR A 258 ? 0.3947 0.4741 0.5440 0.0634 0.1108 -0.1171 299 TYR A CD2 2026 C CE1 . TYR A 258 ? 0.3413 0.4144 0.4964 0.0596 0.0897 -0.1070 299 TYR A CE1 2027 C CE2 . TYR A 258 ? 0.3930 0.4731 0.5599 0.0668 0.1040 -0.1179 299 TYR A CE2 2028 C CZ . TYR A 258 ? 0.3334 0.4102 0.5026 0.0649 0.0934 -0.1126 299 TYR A CZ 2029 O OH . TYR A 258 ? 0.3318 0.4084 0.5164 0.0687 0.0863 -0.1130 299 TYR A OH 2030 N N . TYR A 259 ? 0.4042 0.4605 0.4987 0.0646 0.1132 -0.1276 300 TYR A N 2031 C CA . TYR A 259 ? 0.4290 0.4830 0.5196 0.0699 0.1192 -0.1363 300 TYR A CA 2032 C C . TYR A 259 ? 0.4483 0.4974 0.5144 0.0692 0.1234 -0.1389 300 TYR A C 2033 O O . TYR A 259 ? 0.4639 0.5157 0.5244 0.0725 0.1333 -0.1434 300 TYR A O 2034 C CB . TYR A 259 ? 0.4325 0.4780 0.5278 0.0735 0.1118 -0.1416 300 TYR A CB 2035 C CG . TYR A 259 ? 0.4480 0.4972 0.5664 0.0765 0.1087 -0.1413 300 TYR A CG 2036 C CD1 . TYR A 259 ? 0.4605 0.5214 0.5962 0.0777 0.1148 -0.1398 300 TYR A CD1 2037 C CD2 . TYR A 259 ? 0.4387 0.4794 0.5623 0.0783 0.0996 -0.1426 300 TYR A CD2 2038 C CE1 . TYR A 259 ? 0.4867 0.5508 0.6437 0.0810 0.1110 -0.1401 300 TYR A CE1 2039 C CE2 . TYR A 259 ? 0.4780 0.5212 0.6214 0.0817 0.0963 -0.1421 300 TYR A CE2 2040 C CZ . TYR A 259 ? 0.5036 0.5585 0.6634 0.0832 0.1016 -0.1412 300 TYR A CZ 2041 O OH . TYR A 259 ? 0.5153 0.5725 0.6948 0.0870 0.0972 -0.1409 300 TYR A OH 2042 N N . ASP A 260 ? 0.4343 0.4762 0.4861 0.0654 0.1159 -0.1361 301 ASP A N 2043 C CA . ASP A 260 ? 0.4663 0.5030 0.4943 0.0646 0.1178 -0.1380 301 ASP A CA 2044 C C . ASP A 260 ? 0.4638 0.5072 0.4838 0.0621 0.1264 -0.1325 301 ASP A C 2045 O O . ASP A 260 ? 0.4844 0.5265 0.4877 0.0642 0.1336 -0.1355 301 ASP A O 2046 C CB . ASP A 260 ? 0.4542 0.4819 0.4718 0.0611 0.1068 -0.1364 301 ASP A CB 2047 C CG . ASP A 260 ? 0.4704 0.4892 0.4907 0.0638 0.0996 -0.1432 301 ASP A CG 2048 O OD1 . ASP A 260 ? 0.5035 0.5213 0.5277 0.0690 0.1033 -0.1507 301 ASP A OD1 2049 O OD2 . ASP A 260 ? 0.4804 0.4929 0.4992 0.0608 0.0903 -0.1410 301 ASP A OD2 2050 N N . ALA A 261 ? 0.4491 0.4987 0.4802 0.0579 0.1255 -0.1244 302 ALA A N 2051 C CA . ALA A 261 ? 0.4422 0.4984 0.4696 0.0551 0.1337 -0.1183 302 ALA A CA 2052 C C . ALA A 261 ? 0.4562 0.5195 0.4882 0.0588 0.1471 -0.1212 302 ALA A C 2053 O O . ALA A 261 ? 0.4661 0.5303 0.4839 0.0587 0.1560 -0.1197 302 ALA A O 2054 C CB . ALA A 261 ? 0.4232 0.4852 0.4663 0.0505 0.1298 -0.1103 302 ALA A CB 2055 N N . GLN A 262 ? 0.4522 0.5204 0.5042 0.0622 0.1489 -0.1251 303 GLN A N 2056 C CA . GLN A 262 ? 0.4835 0.5588 0.5428 0.0665 0.1617 -0.1289 303 GLN A CA 2057 C C . GLN A 262 ? 0.5069 0.5764 0.5427 0.0708 0.1688 -0.1352 303 GLN A C 2058 O O . GLN A 262 ? 0.5210 0.5950 0.5506 0.0722 0.1816 -0.1346 303 GLN A O 2059 C CB . GLN A 262 ? 0.4746 0.5535 0.5575 0.0703 0.1592 -0.1334 303 GLN A CB 2060 C CG . GLN A 262 ? 0.5506 0.6356 0.6418 0.0761 0.1714 -0.1396 303 GLN A CG 2061 C CD . GLN A 262 ? 0.5894 0.6873 0.7077 0.0758 0.1775 -0.1365 303 GLN A CD 2062 O OE1 . GLN A 262 ? 0.6805 0.7857 0.8042 0.0785 0.1905 -0.1385 303 GLN A OE1 2063 N NE2 . GLN A 262 ? 0.5551 0.6559 0.6913 0.0730 0.1682 -0.1323 303 GLN A NE2 2064 N N . LYS A 263 ? 0.5165 0.5756 0.5392 0.0729 0.1606 -0.1413 304 LYS A N 2065 C CA . LYS A 263 ? 0.5439 0.5962 0.5438 0.0773 0.1649 -0.1485 304 LYS A CA 2066 C C . LYS A 263 ? 0.5625 0.6121 0.5379 0.0748 0.1685 -0.1438 304 LYS A C 2067 O O . LYS A 263 ? 0.5848 0.6334 0.5437 0.0787 0.1782 -0.1469 304 LYS A O 2068 C CB . LYS A 263 ? 0.5540 0.5955 0.5480 0.0794 0.1536 -0.1559 304 LYS A CB 2069 C CG . LYS A 263 ? 0.5695 0.6119 0.5861 0.0824 0.1498 -0.1606 304 LYS A CG 2070 C CD . LYS A 263 ? 0.6450 0.6923 0.6690 0.0890 0.1609 -0.1676 304 LYS A CD 2071 C CE . LYS A 263 ? 0.7045 0.7434 0.7063 0.0942 0.1637 -0.1769 304 LYS A CE 2072 N NZ . LYS A 263 ? 0.7777 0.8174 0.7894 0.1014 0.1690 -0.1863 304 LYS A NZ 2073 N N . LEU A 264 ? 0.5340 0.5824 0.5071 0.0688 0.1610 -0.1361 305 LEU A N 2074 C CA . LEU A 264 ? 0.5550 0.6008 0.5063 0.0663 0.1636 -0.1307 305 LEU A CA 2075 C C . LEU A 264 ? 0.5534 0.6080 0.5093 0.0646 0.1763 -0.1233 305 LEU A C 2076 O O . LEU A 264 ? 0.5900 0.6425 0.5255 0.0654 0.1838 -0.1212 305 LEU A O 2077 C CB . LEU A 264 ? 0.5330 0.5738 0.4799 0.0607 0.1508 -0.1253 305 LEU A CB 2078 C CG . LEU A 264 ? 0.5546 0.5862 0.4964 0.0614 0.1379 -0.1314 305 LEU A CG 2079 C CD1 . LEU A 264 ? 0.5525 0.5807 0.4927 0.0556 0.1265 -0.1252 305 LEU A CD1 2080 C CD2 . LEU A 264 ? 0.5892 0.6125 0.5077 0.0663 0.1384 -0.1399 305 LEU A CD2 2081 N N . LEU A 265 ? 0.5187 0.5829 0.5011 0.0622 0.1786 -0.1193 306 LEU A N 2082 C CA . LEU A 265 ? 0.5139 0.5867 0.5042 0.0596 0.1899 -0.1118 306 LEU A CA 2083 C C . LEU A 265 ? 0.5406 0.6195 0.5346 0.0645 0.2055 -0.1153 306 LEU A C 2084 O O . LEU A 265 ? 0.5436 0.6276 0.5366 0.0633 0.2176 -0.1096 306 LEU A O 2085 C CB . LEU A 265 ? 0.4773 0.5579 0.4952 0.0552 0.1854 -0.1065 306 LEU A CB 2086 C CG . LEU A 265 ? 0.4861 0.5620 0.5016 0.0498 0.1717 -0.1014 306 LEU A CG 2087 C CD1 . LEU A 265 ? 0.4943 0.5774 0.5380 0.0472 0.1664 -0.0986 306 LEU A CD1 2088 C CD2 . LEU A 265 ? 0.5002 0.5737 0.4996 0.0456 0.1739 -0.0936 306 LEU A CD2 2089 N N . GLU A 266 ? 0.5572 0.6358 0.5573 0.0700 0.2057 -0.1244 307 GLU A N 2090 C CA . GLU A 266 ? 0.5760 0.6626 0.5872 0.0747 0.2202 -0.1278 307 GLU A CA 2091 C C . GLU A 266 ? 0.6078 0.6917 0.5936 0.0782 0.2338 -0.1282 307 GLU A C 2092 O O . GLU A 266 ? 0.6133 0.7051 0.6069 0.0801 0.2488 -0.1267 307 GLU A O 2093 C CB . GLU A 266 ? 0.5823 0.6691 0.6073 0.0801 0.2170 -0.1375 307 GLU A CB 2094 C CG . GLU A 266 ? 0.6253 0.7003 0.6276 0.0849 0.2112 -0.1465 307 GLU A CG 2095 C CD . GLU A 266 ? 0.6881 0.7625 0.7059 0.0899 0.2069 -0.1557 307 GLU A CD 2096 O OE1 . GLU A 266 ? 0.7075 0.7907 0.7534 0.0899 0.2080 -0.1550 307 GLU A OE1 2097 O OE2 . GLU A 266 ? 0.6984 0.7630 0.7001 0.0939 0.2019 -0.1638 307 GLU A OE2 2098 N N . LYS A 267 ? 0.6276 0.7002 0.5831 0.0790 0.2284 -0.1297 308 LYS A N 2099 C CA . LYS A 267 ? 0.6593 0.7272 0.5860 0.0831 0.2396 -0.1304 308 LYS A CA 2100 C C . LYS A 267 ? 0.6621 0.7298 0.5760 0.0784 0.2447 -0.1192 308 LYS A C 2101 O O . LYS A 267 ? 0.6785 0.7421 0.5676 0.0816 0.2545 -0.1180 308 LYS A O 2102 C CB . LYS A 267 ? 0.6769 0.7321 0.5768 0.0877 0.2306 -0.1393 308 LYS A CB 2103 C CG . LYS A 267 ? 0.7109 0.7651 0.6180 0.0940 0.2299 -0.1511 308 LYS A CG 2104 C CD . LYS A 267 ? 0.7203 0.7617 0.6071 0.0969 0.2170 -0.1599 308 LYS A CD 2105 C CE . LYS A 267 ? 0.7553 0.7947 0.6437 0.1047 0.2198 -0.1723 308 LYS A CE 2106 N NZ . LYS A 267 ? 0.7522 0.7788 0.6224 0.1076 0.2071 -0.1817 308 LYS A NZ 2107 N N . MET A 268 ? 0.6393 0.7109 0.5694 0.0712 0.2380 -0.1110 309 MET A N 2108 C CA . MET A 268 ? 0.6429 0.7135 0.5625 0.0662 0.2414 -0.1001 309 MET A CA 2109 C C . MET A 268 ? 0.6607 0.7375 0.5800 0.0669 0.2609 -0.0938 309 MET A C 2110 O O . MET A 268 ? 0.6473 0.7347 0.5921 0.0668 0.2705 -0.0933 309 MET A O 2111 C CB . MET A 268 ? 0.6133 0.6874 0.5532 0.0588 0.2305 -0.0935 309 MET A CB 2112 C CG A MET A 268 ? 0.6046 0.6697 0.5343 0.0581 0.2126 -0.0976 309 MET A CG 2113 C CG B MET A 268 ? 0.6081 0.6750 0.5438 0.0572 0.2123 -0.0967 309 MET A CG 2114 S SD A MET A 268 ? 0.5536 0.6163 0.4876 0.0505 0.1983 -0.0897 309 MET A SD 2115 S SD B MET A 268 ? 0.6061 0.6602 0.5042 0.0574 0.2066 -0.0949 309 MET A SD 2116 C CE A MET A 268 ? 0.5932 0.6540 0.5089 0.0476 0.2074 -0.0790 309 MET A CE 2117 C CE B MET A 268 ? 0.6314 0.6884 0.5298 0.0511 0.2125 -0.0812 309 MET A CE 2118 N N . GLY A 269 ? 0.6884 0.7580 0.5789 0.0674 0.2662 -0.0886 310 GLY A N 2119 C CA . GLY A 269 ? 0.7231 0.7961 0.6077 0.0683 0.2852 -0.0817 310 GLY A CA 2120 C C . GLY A 269 ? 0.7282 0.8004 0.6113 0.0616 0.2859 -0.0691 310 GLY A C 2121 O O . GLY A 269 ? 0.6980 0.7736 0.6014 0.0552 0.2756 -0.0652 310 GLY A O 2122 N N . GLY A 270 ? 0.7567 0.8242 0.6157 0.0633 0.2982 -0.0627 311 GLY A N 2123 C CA . GLY A 270 ? 0.7598 0.8257 0.6168 0.0573 0.3002 -0.0501 311 GLY A CA 2124 C C . GLY A 270 ? 0.7475 0.8261 0.6430 0.0511 0.3070 -0.0438 311 GLY A C 2125 O O . GLY A 270 ? 0.7402 0.8284 0.6566 0.0530 0.3176 -0.0471 311 GLY A O 2126 N N . SER A 271 ? 0.7332 0.8120 0.6396 0.0440 0.3001 -0.0356 312 SER A N 2127 C CA . SER A 271 ? 0.7272 0.8172 0.6689 0.0377 0.3067 -0.0287 312 SER A CA 2128 C C . SER A 271 ? 0.6975 0.7983 0.6756 0.0360 0.2995 -0.0351 312 SER A C 2129 O O . SER A 271 ? 0.6754 0.7737 0.6539 0.0367 0.2838 -0.0420 312 SER A O 2130 C CB . SER A 271 ? 0.7224 0.8082 0.6640 0.0308 0.2998 -0.0187 312 SER A CB 2131 O OG . SER A 271 ? 0.7763 0.8522 0.6862 0.0322 0.3072 -0.0114 312 SER A OG 2132 N N . ALA A 272 ? 0.6795 0.7921 0.6884 0.0338 0.3109 -0.0324 313 ALA A N 2133 C CA . ALA A 272 ? 0.6531 0.7765 0.7000 0.0311 0.3035 -0.0363 313 ALA A CA 2134 C C . ALA A 272 ? 0.6325 0.7534 0.6879 0.0249 0.2861 -0.0331 313 ALA A C 2135 O O . ALA A 272 ? 0.6321 0.7462 0.6732 0.0212 0.2846 -0.0253 313 ALA A O 2136 C CB . ALA A 272 ? 0.6532 0.7893 0.7315 0.0287 0.3194 -0.0320 313 ALA A CB 2137 N N . PRO A 273 ? 0.6145 0.7405 0.6928 0.0241 0.2731 -0.0390 314 PRO A N 2138 C CA . PRO A 273 ? 0.5955 0.7199 0.6839 0.0183 0.2582 -0.0354 314 PRO A CA 2139 C C . PRO A 273 ? 0.6055 0.7354 0.7127 0.0122 0.2663 -0.0259 314 PRO A C 2140 O O . PRO A 273 ? 0.6019 0.7405 0.7271 0.0123 0.2808 -0.0244 314 PRO A O 2141 C CB . PRO A 273 ? 0.5655 0.6965 0.6791 0.0194 0.2470 -0.0429 314 PRO A CB 2142 C CG . PRO A 273 ? 0.5794 0.7189 0.7066 0.0243 0.2592 -0.0486 314 PRO A CG 2143 C CD . PRO A 273 ? 0.6019 0.7359 0.7004 0.0284 0.2727 -0.0480 314 PRO A CD 2144 N N . PRO A 274 ? 0.6075 0.7319 0.7107 0.0070 0.2579 -0.0195 315 PRO A N 2145 C CA . PRO A 274 ? 0.6209 0.7492 0.7406 0.0012 0.2669 -0.0102 315 PRO A CA 2146 C C . PRO A 274 ? 0.6120 0.7530 0.7739 -0.0021 0.2663 -0.0113 315 PRO A C 2147 O O . PRO A 274 ? 0.6186 0.7657 0.7997 -0.0058 0.2779 -0.0052 315 PRO A O 2148 C CB . PRO A 274 ? 0.6111 0.7296 0.7152 -0.0028 0.2558 -0.0044 315 PRO A CB 2149 C CG . PRO A 274 ? 0.5960 0.7096 0.6893 -0.0003 0.2380 -0.0118 315 PRO A CG 2150 C CD . PRO A 274 ? 0.6008 0.7145 0.6815 0.0063 0.2426 -0.0196 315 PRO A CD 2151 N N . ASP A 275 ? 0.6065 0.7510 0.7826 -0.0007 0.2525 -0.0188 316 ASP A N 2152 C CA . ASP A 275 ? 0.6006 0.7568 0.8160 -0.0028 0.2492 -0.0214 316 ASP A CA 2153 C C . ASP A 275 ? 0.5844 0.7422 0.8061 0.0013 0.2353 -0.0309 316 ASP A C 2154 O O . ASP A 275 ? 0.5790 0.7285 0.7755 0.0048 0.2277 -0.0347 316 ASP A O 2155 C CB . ASP A 275 ? 0.5994 0.7563 0.8322 -0.0098 0.2434 -0.0150 316 ASP A CB 2156 C CG . ASP A 275 ? 0.6105 0.7579 0.8279 -0.0112 0.2254 -0.0151 316 ASP A CG 2157 O OD1 . ASP A 275 ? 0.6406 0.7882 0.8610 -0.0086 0.2121 -0.0218 316 ASP A OD1 2158 O OD2 . ASP A 275 ? 0.6562 0.7961 0.8594 -0.0149 0.2246 -0.0082 316 ASP A OD2 2159 N N . SER A 276 ? 0.5644 0.7327 0.8202 0.0007 0.2315 -0.0343 317 SER A N 2160 C CA . SER A 276 ? 0.5603 0.7311 0.8257 0.0051 0.2195 -0.0429 317 SER A CA 2161 C C . SER A 276 ? 0.5372 0.6988 0.7875 0.0051 0.2008 -0.0446 317 SER A C 2162 O O . SER A 276 ? 0.5430 0.7029 0.7902 0.0096 0.1921 -0.0510 317 SER A O 2163 C CB . SER A 276 ? 0.5553 0.7391 0.8616 0.0042 0.2186 -0.0454 317 SER A CB 2164 O OG . SER A 276 ? 0.5696 0.7532 0.8892 -0.0006 0.2070 -0.0425 317 SER A OG 2165 N N . SER A 277 ? 0.5226 0.6782 0.7643 0.0003 0.1949 -0.0387 318 SER A N 2166 C CA . SER A 277 ? 0.4979 0.6448 0.7248 0.0004 0.1783 -0.0399 318 SER A CA 2167 C C . SER A 277 ? 0.5034 0.6400 0.6965 0.0039 0.1768 -0.0417 318 SER A C 2168 O O . SER A 277 ? 0.4962 0.6257 0.6766 0.0045 0.1639 -0.0433 318 SER A O 2169 C CB . SER A 277 ? 0.5006 0.6436 0.7274 -0.0053 0.1727 -0.0334 318 SER A CB 2170 O OG . SER A 277 ? 0.4855 0.6218 0.6898 -0.0076 0.1811 -0.0270 318 SER A OG 2171 N N . TRP A 278 ? 0.4942 0.6300 0.6731 0.0059 0.1901 -0.0414 319 TRP A N 2172 C CA . TRP A 278 ? 0.4946 0.6213 0.6425 0.0096 0.1900 -0.0439 319 TRP A CA 2173 C C . TRP A 278 ? 0.5023 0.6312 0.6523 0.0157 0.1906 -0.0524 319 TRP A C 2174 O O . TRP A 278 ? 0.5119 0.6331 0.6389 0.0191 0.1879 -0.0561 319 TRP A O 2175 C CB . TRP A 278 ? 0.5038 0.6266 0.6310 0.0090 0.2036 -0.0387 319 TRP A CB 2176 C CG . TRP A 278 ? 0.4906 0.6056 0.6016 0.0046 0.1994 -0.0313 319 TRP A CG 2177 C CD1 . TRP A 278 ? 0.4710 0.5876 0.5967 -0.0008 0.1957 -0.0255 319 TRP A CD1 2178 C CD2 . TRP A 278 ? 0.4807 0.5848 0.5587 0.0055 0.1984 -0.0294 319 TRP A CD2 2179 N NE1 . TRP A 278 ? 0.4854 0.5927 0.5889 -0.0032 0.1922 -0.0200 319 TRP A NE1 2180 C CE2 . TRP A 278 ? 0.5060 0.6058 0.5803 0.0006 0.1937 -0.0221 319 TRP A CE2 2181 C CE3 . TRP A 278 ? 0.5017 0.5992 0.5532 0.0103 0.2000 -0.0335 319 TRP A CE3 2182 C CZ2 . TRP A 278 ? 0.4935 0.5827 0.5388 0.0004 0.1907 -0.0185 319 TRP A CZ2 2183 C CZ3 . TRP A 278 ? 0.4891 0.5762 0.5116 0.0101 0.1965 -0.0303 319 TRP A CZ3 2184 C CH2 . TRP A 278 ? 0.5086 0.5918 0.5287 0.0052 0.1918 -0.0227 319 TRP A CH2 2185 N N . ARG A 279 ? 0.4940 0.6332 0.6723 0.0172 0.1937 -0.0557 320 ARG A N 2186 C CA A ARG A 279 ? 0.4967 0.6388 0.6809 0.0231 0.1945 -0.0638 320 ARG A CA 2187 C CA B ARG A 279 ? 0.4976 0.6394 0.6810 0.0231 0.1943 -0.0638 320 ARG A CA 2188 C C . ARG A 279 ? 0.4803 0.6212 0.6742 0.0247 0.1785 -0.0681 320 ARG A C 2189 O O . ARG A 279 ? 0.4693 0.6152 0.6846 0.0223 0.1715 -0.0666 320 ARG A O 2190 C CB A ARG A 279 ? 0.5052 0.6598 0.7165 0.0243 0.2070 -0.0651 320 ARG A CB 2191 C CB B ARG A 279 ? 0.5077 0.6615 0.7164 0.0246 0.2073 -0.0652 320 ARG A CB 2192 C CG A ARG A 279 ? 0.5333 0.6900 0.7366 0.0242 0.2256 -0.0617 320 ARG A CG 2193 C CG B ARG A 279 ? 0.5419 0.6961 0.7374 0.0256 0.2251 -0.0631 320 ARG A CG 2194 C CD A ARG A 279 ? 0.5704 0.7395 0.8000 0.0272 0.2381 -0.0651 320 ARG A CD 2195 C CD B ARG A 279 ? 0.5829 0.7499 0.8060 0.0277 0.2380 -0.0654 320 ARG A CD 2196 N NE A ARG A 279 ? 0.5715 0.7417 0.8067 0.0333 0.2329 -0.0741 320 ARG A NE 2197 N NE B ARG A 279 ? 0.5888 0.7649 0.8410 0.0223 0.2399 -0.0602 320 ARG A NE 2198 C CZ A ARG A 279 ? 0.5952 0.7608 0.8113 0.0390 0.2382 -0.0796 320 ARG A CZ 2199 C CZ B ARG A 279 ? 0.6049 0.7869 0.8659 0.0195 0.2553 -0.0546 320 ARG A CZ 2200 N NH1 A ARG A 279 ? 0.6267 0.7865 0.8161 0.0396 0.2488 -0.0771 320 ARG A NH1 2201 N NH1 B ARG A 279 ? 0.6188 0.7982 0.8600 0.0221 0.2705 -0.0533 320 ARG A NH1 2202 N NH2 A ARG A 279 ? 0.5631 0.7294 0.7863 0.0444 0.2325 -0.0876 320 ARG A NH2 2203 N NH2 B ARG A 279 ? 0.6036 0.7936 0.8932 0.0143 0.2556 -0.0503 320 ARG A NH2 2204 N N . GLY A 280 ? 0.4788 0.6126 0.6570 0.0290 0.1728 -0.0734 321 GLY A N 2205 C CA . GLY A 280 ? 0.4502 0.5823 0.6370 0.0317 0.1595 -0.0778 321 GLY A CA 2206 C C . GLY A 280 ? 0.4596 0.5996 0.6673 0.0367 0.1639 -0.0840 321 GLY A C 2207 O O . GLY A 280 ? 0.4543 0.6033 0.6763 0.0368 0.1762 -0.0839 321 GLY A O 2208 N N . SER A 281 ? 0.4447 0.5811 0.6541 0.0409 0.1546 -0.0892 322 SER A N 2209 C CA . SER A 281 ? 0.4540 0.5973 0.6851 0.0461 0.1560 -0.0952 322 SER A CA 2210 C C . SER A 281 ? 0.4543 0.5941 0.6743 0.0516 0.1624 -0.1016 322 SER A C 2211 O O . SER A 281 ? 0.4681 0.6130 0.7051 0.0564 0.1642 -0.1070 322 SER A O 2212 C CB . SER A 281 ? 0.4407 0.5826 0.6845 0.0478 0.1410 -0.0964 322 SER A CB 2213 O OG . SER A 281 ? 0.4734 0.6206 0.7325 0.0436 0.1358 -0.0918 322 SER A OG 2214 N N . LEU A 282 ? 0.4514 0.5825 0.6437 0.0513 0.1655 -0.1017 323 LEU A N 2215 C CA . LEU A 282 ? 0.4557 0.5830 0.6368 0.0568 0.1715 -0.1087 323 LEU A CA 2216 C C . LEU A 282 ? 0.4824 0.6183 0.6704 0.0589 0.1883 -0.1102 323 LEU A C 2217 O O . LEU A 282 ? 0.4700 0.6122 0.6632 0.0550 0.1965 -0.1046 323 LEU A O 2218 C CB . LEU A 282 ? 0.4584 0.5734 0.6075 0.0563 0.1687 -0.1091 323 LEU A CB 2219 C CG . LEU A 282 ? 0.4276 0.5331 0.5672 0.0544 0.1535 -0.1076 323 LEU A CG 2220 C CD1 . LEU A 282 ? 0.3862 0.4811 0.4954 0.0531 0.1523 -0.1075 323 LEU A CD1 2221 C CD2 . LEU A 282 ? 0.4381 0.5411 0.5887 0.0591 0.1456 -0.1134 323 LEU A CD2 2222 N N . LYS A 283 ? 0.4996 0.6349 0.6865 0.0650 0.1935 -0.1176 324 LYS A N 2223 C CA . LYS A 283 ? 0.5377 0.6805 0.7299 0.0682 0.2099 -0.1202 324 LYS A CA 2224 C C . LYS A 283 ? 0.5477 0.6837 0.7090 0.0681 0.2189 -0.1193 324 LYS A C 2225 O O . LYS A 283 ? 0.5526 0.6842 0.6996 0.0734 0.2245 -0.1258 324 LYS A O 2226 C CB . LYS A 283 ? 0.5620 0.7065 0.7661 0.0755 0.2110 -0.1293 324 LYS A CB 2227 C CG . LYS A 283 ? 0.6027 0.7539 0.8378 0.0764 0.2019 -0.1302 324 LYS A CG 2228 C CD . LYS A 283 ? 0.6787 0.8442 0.9412 0.0735 0.2092 -0.1258 324 LYS A CD 2229 C CE . LYS A 283 ? 0.6871 0.8551 0.9674 0.0695 0.1955 -0.1213 324 LYS A CE 2230 N NZ . LYS A 283 ? 0.6791 0.8615 0.9903 0.0673 0.2019 -0.1186 324 LYS A NZ 2231 N N . VAL A 284 ? 0.5289 0.6633 0.6793 0.0622 0.2193 -0.1113 325 VAL A N 2232 C CA . VAL A 284 ? 0.5430 0.6709 0.6637 0.0618 0.2274 -0.1090 325 VAL A CA 2233 C C . VAL A 284 ? 0.5403 0.6749 0.6672 0.0566 0.2372 -0.0998 325 VAL A C 2234 O O . VAL A 284 ? 0.5216 0.6638 0.6733 0.0524 0.2338 -0.0955 325 VAL A O 2235 C CB . VAL A 284 ? 0.5329 0.6474 0.6261 0.0602 0.2147 -0.1087 325 VAL A CB 2236 C CG1 . VAL A 284 ? 0.5457 0.6531 0.6334 0.0652 0.2058 -0.1177 325 VAL A CG1 2237 C CG2 . VAL A 284 ? 0.4980 0.6120 0.5979 0.0536 0.2029 -0.1015 325 VAL A CG2 2238 N N . PRO A 285 ? 0.5653 0.6965 0.6696 0.0569 0.2491 -0.0969 326 PRO A N 2239 C CA . PRO A 285 ? 0.5664 0.7036 0.6775 0.0519 0.2594 -0.0876 326 PRO A CA 2240 C C . PRO A 285 ? 0.5486 0.6809 0.6535 0.0451 0.2492 -0.0797 326 PRO A C 2241 O O . PRO A 285 ? 0.5450 0.6831 0.6637 0.0401 0.2545 -0.0721 326 PRO A O 2242 C CB . PRO A 285 ? 0.5934 0.7267 0.6786 0.0555 0.2751 -0.0870 326 PRO A CB 2243 C CG . PRO A 285 ? 0.6245 0.7461 0.6810 0.0608 0.2677 -0.0951 326 PRO A CG 2244 C CD . PRO A 285 ? 0.5919 0.7155 0.6677 0.0629 0.2556 -0.1026 326 PRO A CD 2245 N N . TYR A 286 ? 0.5360 0.6581 0.6222 0.0449 0.2349 -0.0815 327 TYR A N 2246 C CA . TYR A 286 ? 0.5252 0.6413 0.6009 0.0392 0.2255 -0.0746 327 TYR A CA 2247 C C . TYR A 286 ? 0.5436 0.6559 0.5982 0.0373 0.2361 -0.0674 327 TYR A C 2248 O O . TYR A 286 ? 0.5425 0.6545 0.5990 0.0318 0.2345 -0.0594 327 TYR A O 2249 C CB . TYR A 286 ? 0.4996 0.6224 0.6035 0.0341 0.2175 -0.0706 327 TYR A CB 2250 C CG . TYR A 286 ? 0.4753 0.5981 0.5920 0.0360 0.2038 -0.0767 327 TYR A CG 2251 C CD1 . TYR A 286 ? 0.4638 0.5775 0.5665 0.0350 0.1892 -0.0772 327 TYR A CD1 2252 C CD2 . TYR A 286 ? 0.4562 0.5876 0.5983 0.0392 0.2057 -0.0819 327 TYR A CD2 2253 C CE1 . TYR A 286 ? 0.4525 0.5652 0.5657 0.0369 0.1773 -0.0821 327 TYR A CE1 2254 C CE2 . TYR A 286 ? 0.4566 0.5869 0.6091 0.0415 0.1929 -0.0870 327 TYR A CE2 2255 C CZ . TYR A 286 ? 0.4356 0.5562 0.5728 0.0402 0.1791 -0.0868 327 TYR A CZ 2256 O OH . TYR A 286 ? 0.4387 0.5573 0.5849 0.0424 0.1672 -0.0909 327 TYR A OH 2257 N N . ASN A 287 ? 0.5603 0.6689 0.5937 0.0424 0.2465 -0.0706 328 ASN A N 2258 C CA . ASN A 287 ? 0.5774 0.6799 0.5846 0.0420 0.2555 -0.0643 328 ASN A CA 2259 C C . ASN A 287 ? 0.5769 0.6686 0.5619 0.0395 0.2420 -0.0618 328 ASN A C 2260 O O . ASN A 287 ? 0.5532 0.6400 0.5335 0.0406 0.2284 -0.0676 328 ASN A O 2261 C CB . ASN A 287 ? 0.5892 0.6883 0.5746 0.0490 0.2671 -0.0696 328 ASN A CB 2262 C CG . ASN A 287 ? 0.6090 0.7188 0.6134 0.0514 0.2847 -0.0700 328 ASN A CG 2263 O OD1 . ASN A 287 ? 0.5909 0.7102 0.6212 0.0469 0.2912 -0.0637 328 ASN A OD1 2264 N ND2 . ASN A 287 ? 0.5657 0.6742 0.5582 0.0585 0.2923 -0.0776 328 ASN A ND2 2265 N N . VAL A 288 ? 0.5899 0.6782 0.5628 0.0359 0.2460 -0.0528 329 VAL A N 2266 C CA . VAL A 288 ? 0.5873 0.6664 0.5426 0.0330 0.2333 -0.0494 329 VAL A CA 2267 C C . VAL A 288 ? 0.6084 0.6763 0.5275 0.0379 0.2315 -0.0530 329 VAL A C 2268 O O . VAL A 288 ? 0.5991 0.6592 0.5039 0.0372 0.2185 -0.0539 329 VAL A O 2269 C CB . VAL A 288 ? 0.5827 0.6628 0.5427 0.0271 0.2373 -0.0382 329 VAL A CB 2270 C CG1 . VAL A 288 ? 0.6236 0.6933 0.5609 0.0252 0.2267 -0.0343 329 VAL A CG1 2271 C CG2 . VAL A 288 ? 0.5772 0.6671 0.5736 0.0220 0.2333 -0.0363 329 VAL A CG2 2272 N N . GLY A 289 ? 0.6373 0.7044 0.5420 0.0434 0.2445 -0.0557 330 GLY A N 2273 C CA . GLY A 289 ? 0.6732 0.7291 0.5418 0.0485 0.2430 -0.0593 330 GLY A CA 2274 C C . GLY A 289 ? 0.7019 0.7523 0.5491 0.0473 0.2504 -0.0495 330 GLY A C 2275 O O . GLY A 289 ? 0.7019 0.7579 0.5616 0.0441 0.2623 -0.0411 330 GLY A O 2276 N N . PRO A 290 ? 0.7266 0.7656 0.5419 0.0500 0.2435 -0.0503 331 PRO A N 2277 C CA . PRO A 290 ? 0.7277 0.7592 0.5272 0.0537 0.2295 -0.0600 331 PRO A CA 2278 C C . PRO A 290 ? 0.7370 0.7676 0.5267 0.0613 0.2355 -0.0704 331 PRO A C 2279 O O . PRO A 290 ? 0.7459 0.7775 0.5257 0.0652 0.2511 -0.0691 331 PRO A O 2280 C CB . PRO A 290 ? 0.7496 0.7699 0.5168 0.0547 0.2247 -0.0556 331 PRO A CB 2281 C CG . PRO A 290 ? 0.7876 0.8078 0.5429 0.0560 0.2426 -0.0469 331 PRO A CG 2282 C CD . PRO A 290 ? 0.7594 0.7917 0.5494 0.0507 0.2521 -0.0414 331 PRO A CD 2283 N N . GLY A 291 ? 0.7277 0.7562 0.5203 0.0633 0.2235 -0.0805 332 GLY A N 2284 C CA . GLY A 291 ? 0.7402 0.7655 0.5199 0.0710 0.2267 -0.0917 332 GLY A CA 2285 C C . GLY A 291 ? 0.7289 0.7641 0.5333 0.0728 0.2369 -0.0960 332 GLY A C 2286 O O . GLY A 291 ? 0.6982 0.7434 0.5308 0.0681 0.2418 -0.0902 332 GLY A O 2287 N N . PHE A 292 ? 0.7387 0.7710 0.5327 0.0800 0.2397 -0.1065 333 PHE A N 2288 C CA . PHE A 292 ? 0.7407 0.7814 0.5564 0.0831 0.2486 -0.1125 333 PHE A CA 2289 C C . PHE A 292 ? 0.7697 0.8143 0.5776 0.0874 0.2695 -0.1099 333 PHE A C 2290 O O . PHE A 292 ? 0.7810 0.8190 0.5600 0.0898 0.2759 -0.1059 333 PHE A O 2291 C CB . PHE A 292 ? 0.7401 0.7752 0.5503 0.0888 0.2400 -0.1261 333 PHE A CB 2292 C CG . PHE A 292 ? 0.7204 0.7527 0.5435 0.0849 0.2211 -0.1292 333 PHE A CG 2293 C CD1 . PHE A 292 ? 0.7355 0.7579 0.5427 0.0884 0.2092 -0.1388 333 PHE A CD1 2294 C CD2 . PHE A 292 ? 0.6837 0.7232 0.5350 0.0780 0.2156 -0.1228 333 PHE A CD2 2295 C CE1 . PHE A 292 ? 0.6987 0.7184 0.5184 0.0848 0.1928 -0.1413 333 PHE A CE1 2296 C CE2 . PHE A 292 ? 0.6562 0.6928 0.5181 0.0747 0.1990 -0.1254 333 PHE A CE2 2297 C CZ . PHE A 292 ? 0.6615 0.6883 0.5079 0.0781 0.1883 -0.1343 333 PHE A CZ 2298 N N . THR A 293 ? 0.7789 0.8340 0.6123 0.0887 0.2801 -0.1120 334 THR A N 2299 C CA . THR A 293 ? 0.8240 0.8836 0.6524 0.0933 0.3013 -0.1104 334 THR A CA 2300 C C . THR A 293 ? 0.8656 0.9163 0.6610 0.1028 0.3067 -0.1194 334 THR A C 2301 O O . THR A 293 ? 0.8683 0.9114 0.6528 0.1066 0.2944 -0.1299 334 THR A O 2302 C CB . THR A 293 ? 0.8187 0.8921 0.6837 0.0934 0.3108 -0.1125 334 THR A CB 2303 O OG1 . THR A 293 ? 0.8225 0.8953 0.6979 0.0970 0.3008 -0.1243 334 THR A OG1 2304 C CG2 . THR A 293 ? 0.7852 0.8688 0.6832 0.0848 0.3096 -0.1029 334 THR A CG2 2305 N N . GLY A 294 ? 0.9057 0.9576 0.6870 0.1068 0.3258 -0.1155 335 GLY A N 2306 C CA . GLY A 294 ? 0.9534 0.9969 0.7005 0.1164 0.3342 -0.1226 335 GLY A CA 2307 C C . GLY A 294 ? 0.9734 1.0083 0.7053 0.1233 0.3228 -0.1376 335 GLY A C 2308 O O . GLY A 294 ? 1.0002 1.0226 0.6990 0.1266 0.3140 -0.1410 335 GLY A O 2309 N N . ASN A 295 ? 0.9627 1.0039 0.7188 0.1258 0.3228 -0.1467 336 ASN A N 2310 C CA . ASN A 295 ? 0.9791 1.0121 0.7229 0.1329 0.3136 -0.1616 336 ASN A CA 2311 C C . ASN A 295 ? 0.9610 0.9849 0.6998 0.1298 0.2904 -0.1661 336 ASN A C 2312 O O . ASN A 295 ? 0.9761 0.9900 0.6954 0.1356 0.2820 -0.1774 336 ASN A O 2313 C CB . ASN A 295 ? 0.9793 1.0215 0.7526 0.1361 0.3194 -0.1696 336 ASN A CB 2314 C CG . ASN A 295 ? 1.0182 1.0675 0.7912 0.1418 0.3428 -0.1687 336 ASN A CG 2315 O OD1 . ASN A 295 ? 1.0812 1.1242 0.8282 0.1508 0.3509 -0.1765 336 ASN A OD1 2316 N ND2 . ASN A 295 ? 1.0311 1.0937 0.8336 0.1366 0.3540 -0.1592 336 ASN A ND2 2317 N N . PHE A 296 ? 0.9281 0.9556 0.6850 0.1207 0.2806 -0.1574 337 PHE A N 2318 C CA . PHE A 296 ? 0.9071 0.9276 0.6640 0.1168 0.2594 -0.1602 337 PHE A CA 2319 C C . PHE A 296 ? 0.9052 0.9193 0.6411 0.1125 0.2528 -0.1514 337 PHE A C 2320 O O . PHE A 296 ? 0.8877 0.8981 0.6276 0.1076 0.2364 -0.1508 337 PHE A O 2321 C CB . PHE A 296 ? 0.8696 0.8989 0.6655 0.1103 0.2516 -0.1581 337 PHE A CB 2322 C CG . PHE A 296 ? 0.8745 0.9108 0.6943 0.1142 0.2578 -0.1655 337 PHE A CG 2323 C CD1 . PHE A 296 ? 0.8660 0.9156 0.7137 0.1119 0.2701 -0.1595 337 PHE A CD1 2324 C CD2 . PHE A 296 ? 0.8929 0.9227 0.7081 0.1203 0.2514 -0.1787 337 PHE A CD2 2325 C CE1 . PHE A 296 ? 0.8631 0.9196 0.7340 0.1158 0.2754 -0.1664 337 PHE A CE1 2326 C CE2 . PHE A 296 ? 0.8934 0.9295 0.7309 0.1243 0.2571 -0.1857 337 PHE A CE2 2327 C CZ . PHE A 296 ? 0.8826 0.9322 0.7479 0.1222 0.2691 -0.1794 337 PHE A CZ 2328 N N . SER A 297 ? 0.9219 0.9344 0.6352 0.1146 0.2656 -0.1446 338 SER A N 2329 C CA . SER A 297 ? 0.9217 0.9296 0.6189 0.1100 0.2611 -0.1342 338 SER A CA 2330 C C . SER A 297 ? 0.9240 0.9186 0.5929 0.1123 0.2447 -0.1400 338 SER A C 2331 O O . SER A 297 ? 0.9265 0.9172 0.5871 0.1077 0.2360 -0.1328 338 SER A O 2332 C CB . SER A 297 ? 0.9400 0.9490 0.6210 0.1116 0.2797 -0.1244 338 SER A CB 2333 O OG . SER A 297 ? 0.9989 0.9994 0.6456 0.1210 0.2867 -0.1311 338 SER A OG 2334 N N . THR A 298 ? 0.9211 0.9092 0.5777 0.1192 0.2398 -0.1534 339 THR A N 2335 C CA . THR A 298 ? 0.9307 0.9063 0.5626 0.1220 0.2233 -0.1611 339 THR A CA 2336 C C . THR A 298 ? 0.9012 0.8762 0.5550 0.1171 0.2045 -0.1663 339 THR A C 2337 O O . THR A 298 ? 0.9145 0.8805 0.5539 0.1174 0.1891 -0.1711 339 THR A O 2338 C CB . THR A 298 ? 0.9671 0.9338 0.5700 0.1327 0.2268 -0.1735 339 THR A CB 2339 O OG1 . THR A 298 ? 0.9649 0.9354 0.5879 0.1356 0.2281 -0.1841 339 THR A OG1 2340 C CG2 . THR A 298 ? 1.0002 0.9666 0.5788 0.1381 0.2463 -0.1678 339 THR A CG2 2341 N N . GLN A 299 ? 0.8582 0.8429 0.5470 0.1127 0.2057 -0.1653 340 GLN A N 2342 C CA . GLN A 299 ? 0.8168 0.8015 0.5278 0.1077 0.1895 -0.1683 340 GLN A CA 2343 C C . GLN A 299 ? 0.7900 0.7768 0.5080 0.0994 0.1825 -0.1567 340 GLN A C 2344 O O . GLN A 299 ? 0.7610 0.7528 0.4783 0.0966 0.1923 -0.1459 340 GLN A O 2345 C CB . GLN A 299 ? 0.7890 0.7822 0.5330 0.1069 0.1931 -0.1716 340 GLN A CB 2346 C CG . GLN A 299 ? 0.8416 0.8328 0.5796 0.1157 0.2006 -0.1837 340 GLN A CG 2347 C CD . GLN A 299 ? 0.8190 0.8192 0.5899 0.1156 0.2055 -0.1863 340 GLN A CD 2348 O OE1 . GLN A 299 ? 0.8070 0.8160 0.6048 0.1094 0.2054 -0.1785 340 GLN A OE1 2349 N NE2 . GLN A 299 ? 0.8284 0.8260 0.5967 0.1230 0.2094 -0.1978 340 GLN A NE2 2350 N N . LYS A 300 ? 0.7767 0.7593 0.5012 0.0957 0.1656 -0.1592 341 LYS A N 2351 C CA . LYS A 300 ? 0.7519 0.7360 0.4848 0.0881 0.1571 -0.1497 341 LYS A CA 2352 C C . LYS A 300 ? 0.7163 0.7040 0.4792 0.0831 0.1467 -0.1509 341 LYS A C 2353 O O . LYS A 300 ? 0.7013 0.6887 0.4763 0.0857 0.1446 -0.1596 341 LYS A O 2354 C CB . LYS A 300 ? 0.7742 0.7484 0.4811 0.0888 0.1455 -0.1506 341 LYS A CB 2355 C CG . LYS A 300 ? 0.8361 0.8038 0.5082 0.0949 0.1525 -0.1509 341 LYS A CG 2356 C CD . LYS A 300 ? 0.8790 0.8494 0.5434 0.0918 0.1609 -0.1375 341 LYS A CD 2357 C CE . LYS A 300 ? 0.9795 0.9464 0.6154 0.0990 0.1755 -0.1372 341 LYS A CE 2358 N NZ . LYS A 300 ? 1.0276 0.9888 0.6384 0.0988 0.1751 -0.1284 341 LYS A NZ 2359 N N . VAL A 301 ? 0.6853 0.6755 0.4589 0.0762 0.1400 -0.1422 342 VAL A N 2360 C CA . VAL A 301 ? 0.6491 0.6416 0.4480 0.0715 0.1296 -0.1423 342 VAL A CA 2361 C C . VAL A 301 ? 0.6504 0.6352 0.4398 0.0693 0.1146 -0.1437 342 VAL A C 2362 O O . VAL A 301 ? 0.6517 0.6334 0.4232 0.0684 0.1127 -0.1389 342 VAL A O 2363 C CB . VAL A 301 ? 0.6390 0.6411 0.4609 0.0656 0.1340 -0.1318 342 VAL A CB 2364 C CG1 . VAL A 301 ? 0.5846 0.5876 0.4278 0.0609 0.1225 -0.1309 342 VAL A CG1 2365 C CG2 . VAL A 301 ? 0.6358 0.6458 0.4717 0.0681 0.1473 -0.1325 342 VAL A CG2 2366 N N . LYS A 302 ? 0.6410 0.6226 0.4424 0.0689 0.1043 -0.1505 343 LYS A N 2367 C CA . LYS A 302 ? 0.6380 0.6128 0.4340 0.0668 0.0901 -0.1527 343 LYS A CA 2368 C C . LYS A 302 ? 0.6085 0.5858 0.4304 0.0613 0.0820 -0.1500 343 LYS A C 2369 O O . LYS A 302 ? 0.5994 0.5779 0.4390 0.0619 0.0820 -0.1541 343 LYS A O 2370 C CB . LYS A 302 ? 0.6599 0.6257 0.4410 0.0724 0.0839 -0.1653 343 LYS A CB 2371 C CG . LYS A 302 ? 0.6727 0.6315 0.4480 0.0704 0.0688 -0.1682 343 LYS A CG 2372 C CD . LYS A 302 ? 0.7267 0.6765 0.4884 0.0762 0.0627 -0.1816 343 LYS A CD 2373 C CE . LYS A 302 ? 0.7551 0.6981 0.5101 0.0748 0.0476 -0.1851 343 LYS A CE 2374 N NZ . LYS A 302 ? 0.8510 0.7850 0.5872 0.0816 0.0427 -0.1983 343 LYS A NZ 2375 N N . MET A 303 ? 0.5923 0.5699 0.4156 0.0564 0.0752 -0.1430 344 MET A N 2376 C CA . MET A 303 ? 0.5625 0.5419 0.4079 0.0513 0.0675 -0.1398 344 MET A CA 2377 C C . MET A 303 ? 0.5759 0.5475 0.4190 0.0514 0.0549 -0.1471 344 MET A C 2378 O O . MET A 303 ? 0.5904 0.5562 0.4136 0.0542 0.0507 -0.1520 344 MET A O 2379 C CB . MET A 303 ? 0.5490 0.5332 0.3986 0.0460 0.0673 -0.1284 344 MET A CB 2380 C CG . MET A 303 ? 0.5309 0.5225 0.3834 0.0455 0.0790 -0.1213 344 MET A CG 2381 S SD . MET A 303 ? 0.5658 0.5620 0.4247 0.0392 0.0773 -0.1087 344 MET A SD 2382 C CE . MET A 303 ? 0.5006 0.4991 0.3861 0.0357 0.0702 -0.1078 344 MET A CE 2383 N N . HIS A 304 ? 0.5472 0.5183 0.4105 0.0489 0.0490 -0.1481 345 HIS A N 2384 C CA . HIS A 304 ? 0.5509 0.5152 0.4165 0.0480 0.0373 -0.1540 345 HIS A CA 2385 C C . HIS A 304 ? 0.5264 0.4933 0.4119 0.0423 0.0325 -0.1468 345 HIS A C 2386 O O . HIS A 304 ? 0.5127 0.4807 0.4164 0.0414 0.0335 -0.1463 345 HIS A O 2387 C CB . HIS A 304 ? 0.5562 0.5154 0.4282 0.0515 0.0357 -0.1644 345 HIS A CB 2388 C CG . HIS A 304 ? 0.6092 0.5661 0.4645 0.0579 0.0419 -0.1722 345 HIS A CG 2389 N ND1 . HIS A 304 ? 0.6408 0.6028 0.4983 0.0605 0.0536 -0.1709 345 HIS A ND1 2390 C CD2 . HIS A 304 ? 0.6660 0.6160 0.5028 0.0625 0.0382 -0.1819 345 HIS A CD2 2391 C CE1 . HIS A 304 ? 0.6568 0.6154 0.4974 0.0665 0.0577 -0.1790 345 HIS A CE1 2392 N NE2 . HIS A 304 ? 0.7120 0.6628 0.5387 0.0680 0.0484 -0.1859 345 HIS A NE2 2393 N N . ILE A 305 ? 0.5197 0.4873 0.4014 0.0388 0.0273 -0.1413 346 ILE A N 2394 C CA . ILE A 305 ? 0.4990 0.4695 0.3977 0.0337 0.0239 -0.1336 346 ILE A CA 2395 C C . ILE A 305 ? 0.5088 0.4746 0.4100 0.0316 0.0129 -0.1365 346 ILE A C 2396 O O . ILE A 305 ? 0.5224 0.4859 0.4091 0.0321 0.0081 -0.1382 346 ILE A O 2397 C CB . ILE A 305 ? 0.5025 0.4793 0.3984 0.0311 0.0285 -0.1232 346 ILE A CB 2398 C CG1 . ILE A 305 ? 0.4986 0.4806 0.3929 0.0331 0.0397 -0.1206 346 ILE A CG1 2399 C CG2 . ILE A 305 ? 0.4568 0.4363 0.3700 0.0265 0.0252 -0.1160 346 ILE A CG2 2400 C CD1 . ILE A 305 ? 0.5283 0.5123 0.4400 0.0341 0.0437 -0.1222 346 ILE A CD1 2401 N N . HIS A 306 ? 0.5000 0.4640 0.4198 0.0293 0.0090 -0.1371 347 HIS A N 2402 C CA . HIS A 306 ? 0.5124 0.4721 0.4391 0.0270 -0.0008 -0.1402 347 HIS A CA 2403 C C . HIS A 306 ? 0.4803 0.4421 0.4252 0.0223 -0.0029 -0.1326 347 HIS A C 2404 O O . HIS A 306 ? 0.4620 0.4202 0.4180 0.0201 -0.0099 -0.1351 347 HIS A O 2405 C CB . HIS A 306 ? 0.5231 0.4761 0.4540 0.0295 -0.0046 -0.1507 347 HIS A CB 2406 C CG . HIS A 306 ? 0.5827 0.5330 0.4950 0.0348 -0.0023 -0.1588 347 HIS A CG 2407 N ND1 . HIS A 306 ? 0.6380 0.5880 0.5505 0.0384 0.0047 -0.1625 347 HIS A ND1 2408 C CD2 . HIS A 306 ? 0.6355 0.5836 0.5272 0.0375 -0.0054 -0.1633 347 HIS A CD2 2409 C CE1 . HIS A 306 ? 0.6497 0.5973 0.5427 0.0431 0.0062 -0.1693 347 HIS A CE1 2410 N NE2 . HIS A 306 ? 0.7026 0.6486 0.5818 0.0428 0.0001 -0.1697 347 HIS A NE2 2411 N N . SER A 307 ? 0.4543 0.4218 0.4024 0.0209 0.0031 -0.1237 348 SER A N 2412 C CA . SER A 307 ? 0.4192 0.3890 0.3817 0.0170 0.0021 -0.1158 348 SER A CA 2413 C C . SER A 307 ? 0.4376 0.4074 0.3988 0.0143 -0.0046 -0.1142 348 SER A C 2414 O O . SER A 307 ? 0.4417 0.4116 0.3880 0.0153 -0.0071 -0.1162 348 SER A O 2415 C CB . SER A 307 ? 0.3961 0.3720 0.3582 0.0166 0.0090 -0.1074 348 SER A CB 2416 O OG . SER A 307 ? 0.4270 0.4034 0.3923 0.0193 0.0149 -0.1093 348 SER A OG 2417 N N . THR A 308 ? 0.4222 0.3919 0.3985 0.0111 -0.0073 -0.1101 349 THR A N 2418 C CA . THR A 308 ? 0.4373 0.4077 0.4155 0.0084 -0.0135 -0.1082 349 THR A CA 2419 C C . THR A 308 ? 0.4207 0.3953 0.4070 0.0058 -0.0108 -0.0985 349 THR A C 2420 O O . THR A 308 ? 0.4095 0.3843 0.4056 0.0054 -0.0065 -0.0945 349 THR A O 2421 C CB . THR A 308 ? 0.4545 0.4201 0.4452 0.0070 -0.0204 -0.1141 349 THR A CB 2422 O OG1 . THR A 308 ? 0.5141 0.4780 0.5217 0.0057 -0.0174 -0.1114 349 THR A OG1 2423 C CG2 . THR A 308 ? 0.4698 0.4305 0.4524 0.0101 -0.0237 -0.1248 349 THR A CG2 2424 N N . ASN A 309 ? 0.4068 0.3844 0.3879 0.0044 -0.0136 -0.0950 350 ASN A N 2425 C CA . ASN A 309 ? 0.4021 0.3834 0.3899 0.0022 -0.0119 -0.0865 350 ASN A CA 2426 C C . ASN A 309 ? 0.4132 0.3930 0.4159 -0.0002 -0.0168 -0.0869 350 ASN A C 2427 O O . ASN A 309 ? 0.4330 0.4110 0.4360 -0.0006 -0.0233 -0.0925 350 ASN A O 2428 C CB . ASN A 309 ? 0.4043 0.3889 0.3796 0.0022 -0.0129 -0.0831 350 ASN A CB 2429 C CG . ASN A 309 ? 0.4484 0.4346 0.4102 0.0042 -0.0073 -0.0817 350 ASN A CG 2430 O OD1 . ASN A 309 ? 0.4686 0.4555 0.4332 0.0052 -0.0018 -0.0809 350 ASN A OD1 2431 N ND2 . ASN A 309 ? 0.5110 0.4978 0.4585 0.0050 -0.0088 -0.0817 350 ASN A ND2 2432 N N . GLU A 310 ? 0.3913 0.3717 0.4066 -0.0018 -0.0136 -0.0811 351 GLU A N 2433 C CA . GLU A 310 ? 0.4019 0.3814 0.4328 -0.0043 -0.0168 -0.0805 351 GLU A CA 2434 C C . GLU A 310 ? 0.3683 0.3505 0.4067 -0.0056 -0.0127 -0.0717 351 GLU A C 2435 O O . GLU A 310 ? 0.3463 0.3288 0.3829 -0.0044 -0.0071 -0.0668 351 GLU A O 2436 C CB . GLU A 310 ? 0.4368 0.4113 0.4804 -0.0048 -0.0173 -0.0847 351 GLU A CB 2437 C CG . GLU A 310 ? 0.5081 0.4801 0.5532 -0.0033 -0.0114 -0.0827 351 GLU A CG 2438 C CD . GLU A 310 ? 0.6723 0.6387 0.7217 -0.0024 -0.0137 -0.0908 351 GLU A CD 2439 O OE1 . GLU A 310 ? 0.6861 0.6481 0.7489 -0.0031 -0.0120 -0.0901 351 GLU A OE1 2440 O OE2 . GLU A 310 ? 0.7688 0.7346 0.8076 -0.0009 -0.0173 -0.0980 351 GLU A OE2 2441 N N . VAL A 311 ? 0.3624 0.3463 0.4093 -0.0077 -0.0159 -0.0703 352 VAL A N 2442 C CA . VAL A 311 ? 0.3434 0.3299 0.3969 -0.0086 -0.0121 -0.0623 352 VAL A CA 2443 C C . VAL A 311 ? 0.3360 0.3187 0.4031 -0.0092 -0.0078 -0.0598 352 VAL A C 2444 O O . VAL A 311 ? 0.3307 0.3102 0.4100 -0.0108 -0.0101 -0.0637 352 VAL A O 2445 C CB . VAL A 311 ? 0.3493 0.3391 0.4095 -0.0104 -0.0166 -0.0619 352 VAL A CB 2446 C CG1 . VAL A 311 ? 0.3534 0.3456 0.4212 -0.0110 -0.0118 -0.0539 352 VAL A CG1 2447 C CG2 . VAL A 311 ? 0.3775 0.3701 0.4228 -0.0093 -0.0208 -0.0636 352 VAL A CG2 2448 N N . THR A 312 ? 0.3070 0.2896 0.3719 -0.0078 -0.0018 -0.0532 353 THR A N 2449 C CA . THR A 312 ? 0.3097 0.2876 0.3833 -0.0074 0.0026 -0.0504 353 THR A CA 2450 C C . THR A 312 ? 0.3035 0.2823 0.3779 -0.0065 0.0079 -0.0416 353 THR A C 2451 O O . THR A 312 ? 0.2823 0.2648 0.3464 -0.0051 0.0087 -0.0386 353 THR A O 2452 C CB . THR A 312 ? 0.3239 0.2993 0.3895 -0.0048 0.0042 -0.0528 353 THR A CB 2453 O OG1 . THR A 312 ? 0.3643 0.3390 0.4262 -0.0050 -0.0003 -0.0613 353 THR A OG1 2454 C CG2 . THR A 312 ? 0.3291 0.2985 0.4040 -0.0040 0.0080 -0.0504 353 THR A CG2 2455 N N . ARG A 313 ? 0.2813 0.2563 0.3673 -0.0070 0.0118 -0.0376 354 ARG A N 2456 C CA . ARG A 313 ? 0.2903 0.2655 0.3756 -0.0056 0.0172 -0.0291 354 ARG A CA 2457 C C . ARG A 313 ? 0.2859 0.2586 0.3609 -0.0019 0.0205 -0.0257 354 ARG A C 2458 O O . ARG A 313 ? 0.3031 0.2714 0.3788 -0.0007 0.0207 -0.0279 354 ARG A O 2459 C CB . ARG A 313 ? 0.3061 0.2778 0.4072 -0.0073 0.0211 -0.0251 354 ARG A CB 2460 C CG . ARG A 313 ? 0.3173 0.2890 0.4169 -0.0054 0.0274 -0.0163 354 ARG A CG 2461 C CD . ARG A 313 ? 0.3498 0.3207 0.4667 -0.0081 0.0309 -0.0131 354 ARG A CD 2462 N NE . ARG A 313 ? 0.3422 0.3198 0.4645 -0.0106 0.0266 -0.0165 354 ARG A NE 2463 C CZ . ARG A 313 ? 0.4003 0.3799 0.5379 -0.0131 0.0283 -0.0148 354 ARG A CZ 2464 N NH1 . ARG A 313 ? 0.3877 0.3631 0.5374 -0.0138 0.0351 -0.0094 354 ARG A NH1 2465 N NH2 . ARG A 313 ? 0.3862 0.3722 0.5273 -0.0148 0.0234 -0.0184 354 ARG A NH2 2466 N N . ILE A 314 ? 0.2773 0.2525 0.3436 0.0001 0.0224 -0.0208 355 ILE A N 2467 C CA . ILE A 314 ? 0.2801 0.2533 0.3371 0.0039 0.0246 -0.0176 355 ILE A CA 2468 C C . ILE A 314 ? 0.2905 0.2619 0.3468 0.0060 0.0293 -0.0099 355 ILE A C 2469 O O . ILE A 314 ? 0.2865 0.2603 0.3473 0.0044 0.0305 -0.0078 355 ILE A O 2470 C CB . ILE A 314 ? 0.2576 0.2359 0.3030 0.0049 0.0216 -0.0203 355 ILE A CB 2471 C CG1 . ILE A 314 ? 0.2527 0.2360 0.2944 0.0039 0.0205 -0.0187 355 ILE A CG1 2472 C CG2 . ILE A 314 ? 0.2554 0.2347 0.3005 0.0035 0.0182 -0.0277 355 ILE A CG2 2473 C CD1 . ILE A 314 ? 0.2519 0.2389 0.2821 0.0054 0.0186 -0.0194 355 ILE A CD1 2474 N N . TYR A 315 ? 0.2934 0.2609 0.3434 0.0099 0.0317 -0.0060 356 TYR A N 2475 C CA . TYR A 315 ? 0.3025 0.2667 0.3503 0.0126 0.0365 0.0014 356 TYR A CA 2476 C C . TYR A 315 ? 0.3005 0.2644 0.3350 0.0173 0.0358 0.0035 356 TYR A C 2477 O O . TYR A 315 ? 0.3102 0.2712 0.3414 0.0198 0.0346 0.0028 356 TYR A O 2478 C CB . TYR A 315 ? 0.3065 0.2629 0.3615 0.0134 0.0407 0.0051 356 TYR A CB 2479 C CG . TYR A 315 ? 0.3059 0.2614 0.3763 0.0089 0.0414 0.0029 356 TYR A CG 2480 C CD1 . TYR A 315 ? 0.3254 0.2809 0.4047 0.0070 0.0456 0.0071 356 TYR A CD1 2481 C CD2 . TYR A 315 ? 0.3461 0.3009 0.4229 0.0066 0.0376 -0.0036 356 TYR A CD2 2482 C CE1 . TYR A 315 ? 0.3285 0.2836 0.4248 0.0025 0.0458 0.0048 356 TYR A CE1 2483 C CE2 . TYR A 315 ? 0.3649 0.3187 0.4565 0.0025 0.0372 -0.0063 356 TYR A CE2 2484 C CZ . TYR A 315 ? 0.3891 0.3432 0.4910 0.0003 0.0411 -0.0021 356 TYR A CZ 2485 O OH . TYR A 315 ? 0.3902 0.3436 0.5084 -0.0038 0.0400 -0.0053 356 TYR A OH 2486 N N . ASN A 316 ? 0.3086 0.2750 0.3365 0.0188 0.0366 0.0064 357 ASN A N 2487 C CA . ASN A 316 ? 0.3113 0.2761 0.3268 0.0238 0.0360 0.0090 357 ASN A CA 2488 C C . ASN A 316 ? 0.3293 0.2874 0.3413 0.0278 0.0412 0.0161 357 ASN A C 2489 O O . ASN A 316 ? 0.3517 0.3091 0.3689 0.0265 0.0460 0.0197 357 ASN A O 2490 C CB . ASN A 316 ? 0.2989 0.2691 0.3078 0.0240 0.0336 0.0080 357 ASN A CB 2491 C CG . ASN A 316 ? 0.3162 0.2926 0.3269 0.0204 0.0289 0.0020 357 ASN A CG 2492 O OD1 . ASN A 316 ? 0.2913 0.2683 0.3032 0.0195 0.0265 -0.0017 357 ASN A OD1 2493 N ND2 . ASN A 316 ? 0.3271 0.3080 0.3372 0.0186 0.0279 0.0012 357 ASN A ND2 2494 N N . VAL A 317 ? 0.3256 0.2789 0.3284 0.0329 0.0406 0.0185 358 VAL A N 2495 C CA . VAL A 317 ? 0.3205 0.2670 0.3160 0.0378 0.0455 0.0257 358 VAL A CA 2496 C C . VAL A 317 ? 0.3327 0.2812 0.3153 0.0417 0.0435 0.0262 358 VAL A C 2497 O O . VAL A 317 ? 0.3374 0.2881 0.3142 0.0435 0.0377 0.0224 358 VAL A O 2498 C CB . VAL A 317 ? 0.3444 0.2830 0.3364 0.0420 0.0457 0.0286 358 VAL A CB 2499 C CG1 . VAL A 317 ? 0.3413 0.2719 0.3256 0.0468 0.0522 0.0371 358 VAL A CG1 2500 C CG2 . VAL A 317 ? 0.3348 0.2715 0.3400 0.0382 0.0463 0.0266 358 VAL A CG2 2501 N N . ILE A 318 ? 0.3502 0.2977 0.3293 0.0431 0.0484 0.0305 359 ILE A N 2502 C CA . ILE A 318 ? 0.3615 0.3103 0.3285 0.0470 0.0470 0.0308 359 ILE A CA 2503 C C . ILE A 318 ? 0.3530 0.2936 0.3082 0.0536 0.0523 0.0378 359 ILE A C 2504 O O . ILE A 318 ? 0.3821 0.3200 0.3412 0.0531 0.0601 0.0431 359 ILE A O 2505 C CB . ILE A 318 ? 0.3528 0.3083 0.3253 0.0433 0.0482 0.0291 359 ILE A CB 2506 C CG1 . ILE A 318 ? 0.3567 0.3191 0.3408 0.0368 0.0438 0.0230 359 ILE A CG1 2507 C CG2 . ILE A 318 ? 0.3721 0.3283 0.3318 0.0478 0.0461 0.0287 359 ILE A CG2 2508 C CD1 . ILE A 318 ? 0.3498 0.3151 0.3291 0.0371 0.0364 0.0178 359 ILE A CD1 2509 N N . GLY A 319 ? 0.3641 0.3006 0.3054 0.0597 0.0481 0.0379 360 GLY A N 2510 C CA . GLY A 319 ? 0.3859 0.3135 0.3125 0.0672 0.0523 0.0444 360 GLY A CA 2511 C C . GLY A 319 ? 0.3942 0.3226 0.3072 0.0719 0.0502 0.0433 360 GLY A C 2512 O O . GLY A 319 ? 0.3877 0.3213 0.3003 0.0710 0.0428 0.0371 360 GLY A O 2513 N N . THR A 320 ? 0.4046 0.3278 0.3072 0.0766 0.0570 0.0490 361 THR A N 2514 C CA . THR A 320 ? 0.4281 0.3513 0.3170 0.0816 0.0557 0.0477 361 THR A CA 2515 C C . THR A 320 ? 0.4414 0.3545 0.3097 0.0912 0.0567 0.0523 361 THR A C 2516 O O . THR A 320 ? 0.4602 0.3661 0.3241 0.0940 0.0647 0.0599 361 THR A O 2517 C CB . THR A 320 ? 0.4459 0.3727 0.3404 0.0793 0.0639 0.0500 361 THR A CB 2518 O OG1 . THR A 320 ? 0.4199 0.3559 0.3328 0.0709 0.0618 0.0454 361 THR A OG1 2519 C CG2 . THR A 320 ? 0.4786 0.4054 0.3594 0.0847 0.0628 0.0482 361 THR A CG2 2520 N N . LEU A 321 ? 0.4410 0.3532 0.2963 0.0964 0.0485 0.0478 362 LEU A N 2521 C CA . LEU A 321 ? 0.4547 0.3574 0.2874 0.1065 0.0487 0.0512 362 LEU A CA 2522 C C . LEU A 321 ? 0.4522 0.3566 0.2756 0.1097 0.0483 0.0482 362 LEU A C 2523 O O . LEU A 321 ? 0.4454 0.3539 0.2685 0.1095 0.0390 0.0410 362 LEU A O 2524 C CB . LEU A 321 ? 0.4588 0.3580 0.2842 0.1109 0.0379 0.0478 362 LEU A CB 2525 C CG . LEU A 321 ? 0.5395 0.4280 0.3408 0.1220 0.0353 0.0504 362 LEU A CG 2526 C CD1 . LEU A 321 ? 0.5681 0.4475 0.3602 0.1258 0.0466 0.0605 362 LEU A CD1 2527 C CD2 . LEU A 321 ? 0.5288 0.4155 0.3286 0.1249 0.0241 0.0467 362 LEU A CD2 2528 N N . ARG A 322 ? 0.4522 0.3534 0.2688 0.1125 0.0586 0.0538 363 ARG A N 2529 C CA . ARG A 322 ? 0.4767 0.3805 0.2872 0.1148 0.0597 0.0509 363 ARG A CA 2530 C C . ARG A 322 ? 0.4840 0.3818 0.2722 0.1242 0.0517 0.0470 363 ARG A C 2531 O O . ARG A 322 ? 0.5008 0.3893 0.2715 0.1320 0.0512 0.0504 363 ARG A O 2532 C CB . ARG A 322 ? 0.5000 0.4020 0.3099 0.1158 0.0738 0.0582 363 ARG A CB 2533 C CG . ARG A 322 ? 0.5530 0.4569 0.3558 0.1191 0.0764 0.0558 363 ARG A CG 2534 C CD . ARG A 322 ? 0.6976 0.6011 0.5034 0.1194 0.0911 0.0630 363 ARG A CD 2535 N NE . ARG A 322 ? 0.7910 0.6875 0.5949 0.1205 0.0996 0.0720 363 ARG A NE 2536 C CZ . ARG A 322 ? 0.8452 0.7308 0.6276 0.1295 0.1050 0.0784 363 ARG A CZ 2537 N NH1 . ARG A 322 ? 0.8831 0.7631 0.6419 0.1389 0.1027 0.0764 363 ARG A NH1 2538 N NH2 . ARG A 322 ? 0.8491 0.7288 0.6332 0.1292 0.1127 0.0868 363 ARG A NH2 2539 N N . GLY A 323 ? 0.4688 0.3719 0.2590 0.1232 0.0445 0.0394 364 GLY A N 2540 C CA . GLY A 323 ? 0.4917 0.3901 0.2639 0.1312 0.0362 0.0343 364 GLY A CA 2541 C C . GLY A 323 ? 0.5181 0.4088 0.2689 0.1405 0.0437 0.0381 364 GLY A C 2542 O O . GLY A 323 ? 0.5305 0.4232 0.2850 0.1391 0.0545 0.0418 364 GLY A O 2543 N N . ALA A 324 ? 0.5500 0.4318 0.2788 0.1501 0.0377 0.0367 365 ALA A N 2544 C CA . ALA A 324 ? 0.5748 0.4477 0.2786 0.1607 0.0436 0.0395 365 ALA A CA 2545 C C . ALA A 324 ? 0.5888 0.4646 0.2897 0.1625 0.0421 0.0332 365 ALA A C 2546 O O . ALA A 324 ? 0.6072 0.4795 0.2962 0.1678 0.0520 0.0366 365 ALA A O 2547 C CB . ALA A 324 ? 0.6059 0.4679 0.2858 0.1711 0.0360 0.0394 365 ALA A CB 2548 N N . VAL A 325 ? 0.5558 0.4377 0.2671 0.1586 0.0303 0.0241 366 VAL A N 2549 C CA . VAL A 325 ? 0.5647 0.4476 0.2713 0.1614 0.0267 0.0171 366 VAL A CA 2550 C C . VAL A 325 ? 0.5406 0.4347 0.2720 0.1511 0.0266 0.0136 366 VAL A C 2551 O O . VAL A 325 ? 0.5407 0.4372 0.2735 0.1514 0.0318 0.0125 366 VAL A O 2552 C CB . VAL A 325 ? 0.5757 0.4537 0.2694 0.1679 0.0115 0.0086 366 VAL A CB 2553 C CG1 . VAL A 325 ? 0.5932 0.4716 0.2829 0.1708 0.0072 0.0009 366 VAL A CG1 2554 C CG2 . VAL A 325 ? 0.6258 0.4920 0.2931 0.1790 0.0108 0.0118 366 VAL A CG2 2555 N N . GLU A 326 ? 0.5084 0.4093 0.2593 0.1422 0.0211 0.0121 367 GLU A N 2556 C CA . GLU A 326 ? 0.4978 0.4090 0.2719 0.1321 0.0214 0.0097 367 GLU A CA 2557 C C . GLU A 326 ? 0.4640 0.3808 0.2555 0.1237 0.0275 0.0153 367 GLU A C 2558 O O . GLU A 326 ? 0.4417 0.3631 0.2465 0.1173 0.0212 0.0129 367 GLU A O 2559 C CB . GLU A 326 ? 0.4954 0.4101 0.2777 0.1289 0.0080 0.0014 367 GLU A CB 2560 C CG . GLU A 326 ? 0.5378 0.4464 0.3039 0.1373 -0.0003 -0.0054 367 GLU A CG 2561 C CD . GLU A 326 ? 0.5453 0.4586 0.3243 0.1325 -0.0120 -0.0133 367 GLU A CD 2562 O OE1 . GLU A 326 ? 0.5307 0.4496 0.3224 0.1270 -0.0111 -0.0154 367 GLU A OE1 2563 O OE2 . GLU A 326 ? 0.5972 0.5083 0.3742 0.1342 -0.0220 -0.0171 367 GLU A OE2 2564 N N . PRO A 327 ? 0.4733 0.3894 0.2653 0.1236 0.0399 0.0225 368 PRO A N 2565 C CA . PRO A 327 ? 0.4492 0.3700 0.2583 0.1158 0.0455 0.0275 368 PRO A CA 2566 C C . PRO A 327 ? 0.4361 0.3670 0.2674 0.1060 0.0435 0.0241 368 PRO A C 2567 O O . PRO A 327 ? 0.4152 0.3502 0.2608 0.0991 0.0439 0.0256 368 PRO A O 2568 C CB . PRO A 327 ? 0.4600 0.3776 0.2647 0.1187 0.0594 0.0354 368 PRO A CB 2569 C CG . PRO A 327 ? 0.5012 0.4165 0.2932 0.1254 0.0618 0.0334 368 PRO A CG 2570 C CD . PRO A 327 ? 0.5033 0.4141 0.2804 0.1311 0.0498 0.0267 368 PRO A CD 2571 N N . ASP A 328 ? 0.4399 0.3742 0.2730 0.1059 0.0405 0.0192 369 ASP A N 2572 C CA . ASP A 328 ? 0.4337 0.3767 0.2859 0.0973 0.0375 0.0158 369 ASP A CA 2573 C C . ASP A 328 ? 0.4096 0.3548 0.2662 0.0941 0.0256 0.0096 369 ASP A C 2574 O O . ASP A 328 ? 0.3934 0.3441 0.2611 0.0890 0.0219 0.0060 369 ASP A O 2575 C CB . ASP A 328 ? 0.4333 0.3788 0.2871 0.0986 0.0411 0.0144 369 ASP A CB 2576 C CG . ASP A 328 ? 0.4879 0.4297 0.3295 0.1044 0.0337 0.0084 369 ASP A CG 2577 O OD1 . ASP A 328 ? 0.5336 0.4692 0.3612 0.1097 0.0279 0.0064 369 ASP A OD1 2578 O OD2 . ASP A 328 ? 0.5223 0.4673 0.3691 0.1036 0.0330 0.0052 369 ASP A OD2 2579 N N . ARG A 329 ? 0.4084 0.3495 0.2577 0.0967 0.0199 0.0086 370 ARG A N 2580 C CA . ARG A 329 ? 0.3754 0.3191 0.2311 0.0933 0.0096 0.0032 370 ARG A CA 2581 C C . ARG A 329 ? 0.3898 0.3335 0.2497 0.0910 0.0096 0.0059 370 ARG A C 2582 O O . ARG A 329 ? 0.3882 0.3258 0.2371 0.0963 0.0127 0.0098 370 ARG A O 2583 C CB . ARG A 329 ? 0.3943 0.3326 0.2365 0.1004 0.0007 -0.0020 370 ARG A CB 2584 C CG . ARG A 329 ? 0.3788 0.3169 0.2175 0.1028 0.0002 -0.0055 370 ARG A CG 2585 C CD . ARG A 329 ? 0.4135 0.3581 0.2684 0.0952 -0.0055 -0.0098 370 ARG A CD 2586 N NE . ARG A 329 ? 0.3884 0.3336 0.2441 0.0958 -0.0066 -0.0132 370 ARG A NE 2587 C CZ . ARG A 329 ? 0.4048 0.3537 0.2673 0.0931 -0.0001 -0.0110 370 ARG A CZ 2588 N NH1 . ARG A 329 ? 0.3847 0.3369 0.2533 0.0898 0.0086 -0.0053 370 ARG A NH1 2589 N NH2 . ARG A 329 ? 0.4114 0.3604 0.2749 0.0940 -0.0027 -0.0148 370 ARG A NH2 2590 N N . TYR A 330 ? 0.3672 0.3172 0.2426 0.0832 0.0071 0.0043 371 TYR A N 2591 C CA . TYR A 330 ? 0.3629 0.3139 0.2452 0.0799 0.0088 0.0069 371 TYR A CA 2592 C C . TYR A 330 ? 0.3567 0.3092 0.2432 0.0786 0.0002 0.0026 371 TYR A C 2593 O O . TYR A 330 ? 0.3638 0.3215 0.2597 0.0740 -0.0045 -0.0016 371 TYR A O 2594 C CB . TYR A 330 ? 0.3536 0.3108 0.2513 0.0718 0.0139 0.0087 371 TYR A CB 2595 C CG . TYR A 330 ? 0.3718 0.3294 0.2706 0.0716 0.0225 0.0127 371 TYR A CG 2596 C CD1 . TYR A 330 ? 0.3742 0.3257 0.2613 0.0779 0.0289 0.0173 371 TYR A CD1 2597 C CD2 . TYR A 330 ? 0.3502 0.3141 0.2621 0.0652 0.0244 0.0121 371 TYR A CD2 2598 C CE1 . TYR A 330 ? 0.4126 0.3653 0.3030 0.0774 0.0377 0.0211 371 TYR A CE1 2599 C CE2 . TYR A 330 ? 0.3611 0.3263 0.2767 0.0647 0.0319 0.0154 371 TYR A CE2 2600 C CZ . TYR A 330 ? 0.3941 0.3540 0.3000 0.0706 0.0388 0.0198 371 TYR A CZ 2601 O OH . TYR A 330 ? 0.3642 0.3260 0.2758 0.0699 0.0468 0.0232 371 TYR A OH 2602 N N . VAL A 331 ? 0.3637 0.3118 0.2444 0.0826 -0.0012 0.0041 372 VAL A N 2603 C CA . VAL A 331 ? 0.3570 0.3075 0.2449 0.0809 -0.0081 0.0006 372 VAL A CA 2604 C C . VAL A 331 ? 0.3522 0.3043 0.2491 0.0766 -0.0033 0.0039 372 VAL A C 2605 O O . VAL A 331 ? 0.3588 0.3059 0.2498 0.0795 0.0021 0.0090 372 VAL A O 2606 C CB . VAL A 331 ? 0.3812 0.3255 0.2567 0.0890 -0.0151 -0.0010 372 VAL A CB 2607 C CG1 . VAL A 331 ? 0.3981 0.3455 0.2835 0.0872 -0.0218 -0.0044 372 VAL A CG1 2608 C CG2 . VAL A 331 ? 0.3795 0.3220 0.2466 0.0932 -0.0210 -0.0056 372 VAL A CG2 2609 N N . ILE A 332 ? 0.3219 0.2806 0.2328 0.0700 -0.0051 0.0011 373 ILE A N 2610 C CA . ILE A 332 ? 0.3258 0.2863 0.2459 0.0655 -0.0001 0.0035 373 ILE A CA 2611 C C . ILE A 332 ? 0.3116 0.2732 0.2374 0.0655 -0.0047 0.0011 373 ILE A C 2612 O O . ILE A 332 ? 0.3184 0.2844 0.2504 0.0637 -0.0105 -0.0034 373 ILE A O 2613 C CB . ILE A 332 ? 0.3059 0.2729 0.2371 0.0579 0.0029 0.0026 373 ILE A CB 2614 C CG1 . ILE A 332 ? 0.3460 0.3126 0.2728 0.0583 0.0065 0.0043 373 ILE A CG1 2615 C CG2 . ILE A 332 ? 0.3119 0.2804 0.2526 0.0534 0.0075 0.0043 373 ILE A CG2 2616 C CD1 . ILE A 332 ? 0.3887 0.3615 0.3256 0.0515 0.0079 0.0029 373 ILE A CD1 2617 N N . LEU A 333 ? 0.2994 0.2569 0.2242 0.0674 -0.0019 0.0044 374 LEU A N 2618 C CA . LEU A 333 ? 0.3050 0.2637 0.2372 0.0670 -0.0050 0.0024 374 LEU A CA 2619 C C . LEU A 333 ? 0.3065 0.2675 0.2488 0.0613 0.0007 0.0037 374 LEU A C 2620 O O . LEU A 333 ? 0.3360 0.2923 0.2758 0.0621 0.0062 0.0083 374 LEU A O 2621 C CB . LEU A 333 ? 0.3207 0.2719 0.2436 0.0745 -0.0074 0.0048 374 LEU A CB 2622 C CG . LEU A 333 ? 0.3290 0.2805 0.2596 0.0750 -0.0102 0.0034 374 LEU A CG 2623 C CD1 . LEU A 333 ? 0.3194 0.2785 0.2599 0.0730 -0.0173 -0.0031 374 LEU A CD1 2624 C CD2 . LEU A 333 ? 0.3468 0.2896 0.2660 0.0835 -0.0130 0.0065 374 LEU A CD2 2625 N N . GLY A 334 ? 0.3149 0.2826 0.2685 0.0558 -0.0004 -0.0002 375 GLY A N 2626 C CA . GLY A 334 ? 0.3098 0.2794 0.2719 0.0506 0.0047 0.0003 375 GLY A CA 2627 C C . GLY A 334 ? 0.3357 0.3090 0.3075 0.0484 0.0028 -0.0034 375 GLY A C 2628 O O . GLY A 334 ? 0.3350 0.3128 0.3103 0.0481 -0.0015 -0.0072 375 GLY A O 2629 N N . GLY A 335 ? 0.3205 0.2921 0.2976 0.0468 0.0063 -0.0027 376 GLY A N 2630 C CA . GLY A 335 ? 0.3196 0.2955 0.3063 0.0442 0.0054 -0.0070 376 GLY A CA 2631 C C . GLY A 335 ? 0.3171 0.2913 0.3089 0.0410 0.0101 -0.0064 376 GLY A C 2632 O O . GLY A 335 ? 0.3206 0.2897 0.3096 0.0416 0.0135 -0.0023 376 GLY A O 2633 N N . HIS A 336 ? 0.2952 0.2732 0.2948 0.0379 0.0105 -0.0105 377 HIS A N 2634 C CA . HIS A 336 ? 0.2852 0.2615 0.2896 0.0346 0.0143 -0.0109 377 HIS A CA 2635 C C . HIS A 336 ? 0.3099 0.2805 0.3179 0.0374 0.0152 -0.0102 377 HIS A C 2636 O O . HIS A 336 ? 0.3136 0.2825 0.3209 0.0420 0.0126 -0.0100 377 HIS A O 2637 C CB . HIS A 336 ? 0.2810 0.2637 0.2899 0.0298 0.0145 -0.0159 377 HIS A CB 2638 C CG . HIS A 336 ? 0.2551 0.2410 0.2693 0.0303 0.0136 -0.0203 377 HIS A CG 2639 N ND1 . HIS A 336 ? 0.2900 0.2750 0.3097 0.0293 0.0154 -0.0235 377 HIS A ND1 2640 C CD2 . HIS A 336 ? 0.2523 0.2434 0.2682 0.0310 0.0115 -0.0227 377 HIS A CD2 2641 C CE1 . HIS A 336 ? 0.2706 0.2597 0.2943 0.0299 0.0149 -0.0274 377 HIS A CE1 2642 N NE2 . HIS A 336 ? 0.2758 0.2689 0.2981 0.0308 0.0127 -0.0268 377 HIS A NE2 2643 N N . ARG A 337 ? 0.2952 0.2626 0.3075 0.0350 0.0184 -0.0097 378 ARG A N 2644 C CA . ARG A 337 ? 0.3088 0.2693 0.3251 0.0371 0.0200 -0.0082 378 ARG A CA 2645 C C . ARG A 337 ? 0.3091 0.2711 0.3337 0.0338 0.0207 -0.0137 378 ARG A C 2646 O O . ARG A 337 ? 0.3099 0.2674 0.3394 0.0358 0.0210 -0.0146 378 ARG A O 2647 C CB . ARG A 337 ? 0.3132 0.2678 0.3285 0.0364 0.0238 -0.0026 378 ARG A CB 2648 C CG . ARG A 337 ? 0.3332 0.2794 0.3532 0.0382 0.0262 0.0001 378 ARG A CG 2649 C CD . ARG A 337 ? 0.3419 0.2832 0.3631 0.0366 0.0310 0.0057 378 ARG A CD 2650 N NE . ARG A 337 ? 0.3452 0.2904 0.3747 0.0305 0.0323 0.0023 378 ARG A NE 2651 C CZ . ARG A 337 ? 0.3340 0.2843 0.3621 0.0275 0.0327 0.0023 378 ARG A CZ 2652 N NH1 . ARG A 337 ? 0.3078 0.2598 0.3268 0.0299 0.0327 0.0056 378 ARG A NH1 2653 N NH2 . ARG A 337 ? 0.3187 0.2721 0.3548 0.0225 0.0328 -0.0011 378 ARG A NH2 2654 N N . ASP A 338 ? 0.2781 0.2456 0.3039 0.0291 0.0209 -0.0174 379 ASP A N 2655 C CA . ASP A 338 ? 0.2857 0.2538 0.3178 0.0264 0.0214 -0.0231 379 ASP A CA 2656 C C . ASP A 338 ? 0.2961 0.2683 0.3295 0.0281 0.0201 -0.0278 379 ASP A C 2657 O O . ASP A 338 ? 0.2930 0.2702 0.3230 0.0292 0.0187 -0.0277 379 ASP A O 2658 C CB . ASP A 338 ? 0.2723 0.2448 0.3037 0.0216 0.0213 -0.0258 379 ASP A CB 2659 C CG . ASP A 338 ? 0.3066 0.2862 0.3322 0.0208 0.0199 -0.0271 379 ASP A CG 2660 O OD1 . ASP A 338 ? 0.2962 0.2769 0.3172 0.0222 0.0192 -0.0231 379 ASP A OD1 2661 O OD2 . ASP A 338 ? 0.2715 0.2552 0.2967 0.0186 0.0197 -0.0318 379 ASP A OD2 2662 N N . SER A 339 ? 0.3092 0.2793 0.3483 0.0285 0.0207 -0.0320 380 SER A N 2663 C CA . SER A 339 ? 0.3111 0.2852 0.3527 0.0306 0.0203 -0.0366 380 SER A CA 2664 C C . SER A 339 ? 0.3268 0.3021 0.3710 0.0282 0.0217 -0.0432 380 SER A C 2665 O O . SER A 339 ? 0.3279 0.2993 0.3736 0.0258 0.0220 -0.0443 380 SER A O 2666 C CB . SER A 339 ? 0.3249 0.2939 0.3708 0.0355 0.0195 -0.0350 380 SER A CB 2667 O OG . SER A 339 ? 0.3433 0.3047 0.3939 0.0356 0.0206 -0.0351 380 SER A OG 2668 N N . TRP A 340 ? 0.3308 0.3115 0.3760 0.0290 0.0225 -0.0478 381 TRP A N 2669 C CA . TRP A 340 ? 0.3332 0.3142 0.3798 0.0280 0.0241 -0.0545 381 TRP A CA 2670 C C . TRP A 340 ? 0.3460 0.3200 0.3994 0.0304 0.0241 -0.0569 381 TRP A C 2671 O O . TRP A 340 ? 0.3568 0.3267 0.4113 0.0286 0.0239 -0.0600 381 TRP A O 2672 C CB . TRP A 340 ? 0.3143 0.3027 0.3599 0.0285 0.0262 -0.0585 381 TRP A CB 2673 C CG . TRP A 340 ? 0.2998 0.2934 0.3378 0.0250 0.0266 -0.0573 381 TRP A CG 2674 C CD1 . TRP A 340 ? 0.3001 0.2996 0.3365 0.0246 0.0268 -0.0545 381 TRP A CD1 2675 C CD2 . TRP A 340 ? 0.3158 0.3085 0.3474 0.0216 0.0263 -0.0589 381 TRP A CD2 2676 N NE1 . TRP A 340 ? 0.3280 0.3299 0.3568 0.0211 0.0271 -0.0538 381 TRP A NE1 2677 C CE2 . TRP A 340 ? 0.3142 0.3123 0.3396 0.0194 0.0266 -0.0565 381 TRP A CE2 2678 C CE3 . TRP A 340 ? 0.3370 0.3248 0.3679 0.0203 0.0252 -0.0625 381 TRP A CE3 2679 C CZ2 . TRP A 340 ? 0.3035 0.3018 0.3213 0.0163 0.0259 -0.0571 381 TRP A CZ2 2680 C CZ3 . TRP A 340 ? 0.3090 0.2976 0.3329 0.0171 0.0240 -0.0635 381 TRP A CZ3 2681 C CH2 . TRP A 340 ? 0.3124 0.3062 0.3296 0.0154 0.0243 -0.0606 381 TRP A CH2 2682 N N . VAL A 341 ? 0.3497 0.3220 0.4083 0.0345 0.0237 -0.0554 382 VAL A N 2683 C CA . VAL A 341 ? 0.3521 0.3166 0.4176 0.0372 0.0233 -0.0563 382 VAL A CA 2684 C C . VAL A 341 ? 0.3593 0.3186 0.4259 0.0403 0.0217 -0.0490 382 VAL A C 2685 O O . VAL A 341 ? 0.3526 0.3083 0.4159 0.0386 0.0214 -0.0436 382 VAL A O 2686 C CB . VAL A 341 ? 0.3607 0.3268 0.4318 0.0402 0.0246 -0.0631 382 VAL A CB 2687 C CG1 . VAL A 341 ? 0.3621 0.3188 0.4400 0.0419 0.0242 -0.0651 382 VAL A CG1 2688 C CG2 . VAL A 341 ? 0.3412 0.3128 0.4081 0.0376 0.0268 -0.0697 382 VAL A CG2 2689 N N . PHE A 342 ? 0.3474 0.3063 0.4183 0.0451 0.0206 -0.0489 383 PHE A N 2690 C CA . PHE A 342 ? 0.3462 0.2992 0.4165 0.0490 0.0185 -0.0421 383 PHE A CA 2691 C C . PHE A 342 ? 0.3491 0.3065 0.4127 0.0497 0.0166 -0.0374 383 PHE A C 2692 O O . PHE A 342 ? 0.3551 0.3069 0.4145 0.0521 0.0152 -0.0310 383 PHE A O 2693 C CB . PHE A 342 ? 0.3276 0.2776 0.4054 0.0546 0.0171 -0.0440 383 PHE A CB 2694 C CG . PHE A 342 ? 0.3486 0.2931 0.4331 0.0543 0.0188 -0.0487 383 PHE A CG 2695 C CD1 . PHE A 342 ? 0.3487 0.2830 0.4343 0.0533 0.0194 -0.0453 383 PHE A CD1 2696 C CD2 . PHE A 342 ? 0.3782 0.3273 0.4682 0.0550 0.0200 -0.0567 383 PHE A CD2 2697 C CE1 . PHE A 342 ? 0.3568 0.2854 0.4498 0.0529 0.0204 -0.0503 383 PHE A CE1 2698 C CE2 . PHE A 342 ? 0.3753 0.3187 0.4711 0.0549 0.0213 -0.0621 383 PHE A CE2 2699 C CZ . PHE A 342 ? 0.3692 0.3023 0.4666 0.0537 0.0210 -0.0590 383 PHE A CZ 2700 N N . GLY A 343 ? 0.3358 0.3025 0.3980 0.0478 0.0166 -0.0404 384 GLY A N 2701 C CA . GLY A 343 ? 0.3309 0.3014 0.3868 0.0480 0.0144 -0.0362 384 GLY A CA 2702 C C . GLY A 343 ? 0.3347 0.3038 0.3915 0.0539 0.0104 -0.0335 384 GLY A C 2703 O O . GLY A 343 ? 0.3297 0.2976 0.3797 0.0552 0.0079 -0.0289 384 GLY A O 2704 N N . GLY A 344 ? 0.3330 0.3025 0.3982 0.0576 0.0093 -0.0369 385 GLY A N 2705 C CA . GLY A 344 ? 0.3300 0.2977 0.3972 0.0639 0.0045 -0.0349 385 GLY A CA 2706 C C . GLY A 344 ? 0.3327 0.3069 0.3973 0.0645 0.0008 -0.0340 385 GLY A C 2707 O O . GLY A 344 ? 0.3532 0.3234 0.4122 0.0687 -0.0035 -0.0298 385 GLY A O 2708 N N . ILE A 345 ? 0.3088 0.2925 0.3769 0.0605 0.0026 -0.0380 386 ILE A N 2709 C CA . ILE A 345 ? 0.3077 0.2968 0.3732 0.0601 -0.0006 -0.0370 386 ILE A CA 2710 C C . ILE A 345 ? 0.3071 0.2959 0.3629 0.0550 0.0018 -0.0344 386 ILE A C 2711 O O . ILE A 345 ? 0.2999 0.2856 0.3471 0.0560 -0.0007 -0.0301 386 ILE A O 2712 C CB . ILE A 345 ? 0.2917 0.2914 0.3687 0.0593 -0.0005 -0.0422 386 ILE A CB 2713 C CG1 . ILE A 345 ? 0.3395 0.3396 0.4269 0.0653 -0.0046 -0.0443 386 ILE A CG1 2714 C CG2 . ILE A 345 ? 0.3068 0.3122 0.3823 0.0574 -0.0033 -0.0415 386 ILE A CG2 2715 C CD1 . ILE A 345 ? 0.3660 0.3768 0.4676 0.0648 -0.0039 -0.0495 386 ILE A CD1 2716 N N . ASP A 346 ? 0.3013 0.2936 0.3583 0.0500 0.0066 -0.0372 387 ASP A N 2717 C CA . ASP A 346 ? 0.2960 0.2893 0.3452 0.0451 0.0086 -0.0354 387 ASP A CA 2718 C C . ASP A 346 ? 0.3020 0.2882 0.3462 0.0433 0.0112 -0.0333 387 ASP A C 2719 O O . ASP A 346 ? 0.3144 0.3002 0.3619 0.0413 0.0143 -0.0367 387 ASP A O 2720 C CB . ASP A 346 ? 0.3075 0.3088 0.3605 0.0410 0.0118 -0.0397 387 ASP A CB 2721 C CG . ASP A 346 ? 0.3133 0.3160 0.3590 0.0362 0.0136 -0.0384 387 ASP A CG 2722 O OD1 . ASP A 346 ? 0.2888 0.2877 0.3275 0.0360 0.0119 -0.0343 387 ASP A OD1 2723 O OD2 . ASP A 346 ? 0.3501 0.3578 0.3972 0.0330 0.0169 -0.0415 387 ASP A OD2 2724 N N . PRO A 347 ? 0.2943 0.2752 0.3311 0.0438 0.0103 -0.0281 388 PRO A N 2725 C CA . PRO A 347 ? 0.2842 0.2645 0.3144 0.0462 0.0070 -0.0241 388 PRO A CA 2726 C C . PRO A 347 ? 0.3040 0.2765 0.3307 0.0522 0.0044 -0.0199 388 PRO A C 2727 O O . PRO A 347 ? 0.3108 0.2813 0.3298 0.0548 0.0016 -0.0165 388 PRO A O 2728 C CB . PRO A 347 ? 0.2835 0.2624 0.3068 0.0424 0.0093 -0.0212 388 PRO A CB 2729 C CG . PRO A 347 ? 0.2926 0.2654 0.3184 0.0410 0.0129 -0.0206 388 PRO A CG 2730 C CD . PRO A 347 ? 0.2947 0.2701 0.3289 0.0411 0.0134 -0.0262 388 PRO A CD 2731 N N . GLN A 348 ? 0.2981 0.2653 0.3290 0.0545 0.0053 -0.0198 389 GLN A N 2732 C CA . GLN A 348 ? 0.3243 0.2819 0.3494 0.0597 0.0041 -0.0141 389 GLN A CA 2733 C C . GLN A 348 ? 0.3285 0.2858 0.3503 0.0659 -0.0018 -0.0131 389 GLN A C 2734 O O . GLN A 348 ? 0.3473 0.2973 0.3597 0.0702 -0.0032 -0.0079 389 GLN A O 2735 C CB . GLN A 348 ? 0.3219 0.2723 0.3523 0.0610 0.0064 -0.0135 389 GLN A CB 2736 C CG . GLN A 348 ? 0.3425 0.2924 0.3769 0.0551 0.0114 -0.0151 389 GLN A CG 2737 C CD . GLN A 348 ? 0.3593 0.3079 0.3871 0.0514 0.0143 -0.0110 389 GLN A CD 2738 O OE1 . GLN A 348 ? 0.3695 0.3157 0.3888 0.0538 0.0136 -0.0060 389 GLN A OE1 2739 N NE2 . GLN A 348 ? 0.3290 0.2788 0.3612 0.0461 0.0175 -0.0134 389 GLN A NE2 2740 N N . SER A 349 ? 0.3272 0.2922 0.3566 0.0664 -0.0052 -0.0183 390 SER A N 2741 C CA A SER A 349 ? 0.3293 0.2950 0.3569 0.0720 -0.0120 -0.0182 390 SER A CA 2742 C CA B SER A 349 ? 0.3469 0.3129 0.3749 0.0718 -0.0120 -0.0184 390 SER A CA 2743 C C . SER A 349 ? 0.3422 0.3079 0.3590 0.0719 -0.0140 -0.0156 390 SER A C 2744 O O . SER A 349 ? 0.3528 0.3139 0.3615 0.0778 -0.0192 -0.0132 390 SER A O 2745 C CB A SER A 349 ? 0.3240 0.2989 0.3650 0.0720 -0.0149 -0.0245 390 SER A CB 2746 C CB B SER A 349 ? 0.3428 0.3188 0.3841 0.0708 -0.0141 -0.0249 390 SER A CB 2747 O OG A SER A 349 ? 0.2380 0.2218 0.2824 0.0664 -0.0132 -0.0277 390 SER A OG 2748 O OG B SER A 349 ? 0.3759 0.3554 0.4174 0.0739 -0.0205 -0.0260 390 SER A OG 2749 N N . GLY A 350 ? 0.3293 0.2993 0.3449 0.0659 -0.0102 -0.0162 391 GLY A N 2750 C CA . GLY A 350 ? 0.3177 0.2870 0.3229 0.0653 -0.0110 -0.0136 391 GLY A CA 2751 C C . GLY A 350 ? 0.3394 0.2996 0.3332 0.0670 -0.0076 -0.0072 391 GLY A C 2752 O O . GLY A 350 ? 0.3351 0.2903 0.3177 0.0717 -0.0101 -0.0037 391 GLY A O 2753 N N . ALA A 351 ? 0.3318 0.2893 0.3286 0.0636 -0.0017 -0.0057 392 ALA A N 2754 C CA . ALA A 351 ? 0.3425 0.2917 0.3313 0.0646 0.0025 0.0005 392 ALA A CA 2755 C C . ALA A 351 ? 0.3563 0.2959 0.3371 0.0720 0.0007 0.0056 392 ALA A C 2756 O O . ALA A 351 ? 0.3440 0.2774 0.3135 0.0747 0.0027 0.0111 392 ALA A O 2757 C CB . ALA A 351 ? 0.3312 0.2797 0.3274 0.0595 0.0081 0.0003 392 ALA A CB 2758 N N . ALA A 352 ? 0.3503 0.2886 0.3363 0.0757 -0.0028 0.0037 393 ALA A N 2759 C CA . ALA A 352 ? 0.3713 0.3002 0.3495 0.0835 -0.0057 0.0082 393 ALA A CA 2760 C C . ALA A 352 ? 0.3911 0.3191 0.3568 0.0890 -0.0114 0.0093 393 ALA A C 2761 O O . ALA A 352 ? 0.3898 0.3086 0.3419 0.0949 -0.0117 0.0152 393 ALA A O 2762 C CB . ALA A 352 ? 0.3592 0.2888 0.3480 0.0861 -0.0095 0.0046 393 ALA A CB 2763 N N . VAL A 353 ? 0.3757 0.3128 0.3457 0.0870 -0.0159 0.0035 394 VAL A N 2764 C CA . VAL A 353 ? 0.3824 0.3192 0.3418 0.0918 -0.0221 0.0032 394 VAL A CA 2765 C C . VAL A 353 ? 0.3904 0.3235 0.3366 0.0910 -0.0177 0.0077 394 VAL A C 2766 O O . VAL A 353 ? 0.3788 0.3053 0.3100 0.0974 -0.0201 0.0111 394 VAL A O 2767 C CB . VAL A 353 ? 0.3687 0.3164 0.3389 0.0892 -0.0278 -0.0041 394 VAL A CB 2768 C CG1 . VAL A 353 ? 0.3737 0.3228 0.3349 0.0905 -0.0319 -0.0051 394 VAL A CG1 2769 C CG2 . VAL A 353 ? 0.3666 0.3159 0.3460 0.0937 -0.0347 -0.0078 394 VAL A CG2 2770 N N . VAL A 354 ? 0.3571 0.2948 0.3088 0.0836 -0.0113 0.0074 395 VAL A N 2771 C CA . VAL A 354 ? 0.3705 0.3059 0.3126 0.0824 -0.0063 0.0113 395 VAL A CA 2772 C C . VAL A 354 ? 0.3852 0.3093 0.3164 0.0872 -0.0016 0.0192 395 VAL A C 2773 O O . VAL A 354 ? 0.3756 0.2943 0.2925 0.0916 -0.0006 0.0233 395 VAL A O 2774 C CB . VAL A 354 ? 0.3639 0.3054 0.3150 0.0740 -0.0005 0.0100 395 VAL A CB 2775 C CG1 . VAL A 354 ? 0.3696 0.3079 0.3116 0.0735 0.0050 0.0148 395 VAL A CG1 2776 C CG2 . VAL A 354 ? 0.3588 0.3106 0.3181 0.0696 -0.0045 0.0032 395 VAL A CG2 2777 N N . HIS A 355 ? 0.3890 0.3091 0.3270 0.0865 0.0014 0.0214 396 HIS A N 2778 C CA . HIS A 355 ? 0.3912 0.3003 0.3211 0.0902 0.0070 0.0294 396 HIS A CA 2779 C C . HIS A 355 ? 0.4297 0.3307 0.3432 0.1000 0.0019 0.0328 396 HIS A C 2780 O O . HIS A 355 ? 0.4452 0.3379 0.3442 0.1043 0.0060 0.0395 396 HIS A O 2781 C CB . HIS A 355 ? 0.3995 0.3061 0.3415 0.0881 0.0091 0.0297 396 HIS A CB 2782 C CG . HIS A 355 ? 0.4239 0.3229 0.3668 0.0863 0.0178 0.0364 396 HIS A CG 2783 N ND1 . HIS A 355 ? 0.4188 0.3203 0.3646 0.0807 0.0245 0.0381 396 HIS A ND1 2784 C CD2 . HIS A 355 ? 0.4615 0.3507 0.4046 0.0893 0.0206 0.0419 396 HIS A CD2 2785 C CE1 . HIS A 355 ? 0.4358 0.3297 0.3846 0.0800 0.0314 0.0442 396 HIS A CE1 2786 N NE2 . HIS A 355 ? 0.4512 0.3371 0.3980 0.0850 0.0293 0.0468 396 HIS A NE2 2787 N N . GLU A 356 ? 0.4122 0.3153 0.3274 0.1038 -0.0069 0.0281 397 GLU A N 2788 C CA . GLU A 356 ? 0.4411 0.3363 0.3403 0.1137 -0.0133 0.0305 397 GLU A CA 2789 C C . GLU A 356 ? 0.4423 0.3381 0.3274 0.1167 -0.0159 0.0298 397 GLU A C 2790 O O . GLU A 356 ? 0.4705 0.3572 0.3371 0.1244 -0.0167 0.0345 397 GLU A O 2791 C CB . GLU A 356 ? 0.4616 0.3592 0.3686 0.1173 -0.0227 0.0254 397 GLU A CB 2792 C CG . GLU A 356 ? 0.4927 0.3829 0.3838 0.1281 -0.0318 0.0266 397 GLU A CG 2793 C CD . GLU A 356 ? 0.5695 0.4455 0.4457 0.1352 -0.0286 0.0356 397 GLU A CD 2794 O OE1 . GLU A 356 ? 0.5672 0.4387 0.4445 0.1315 -0.0185 0.0416 397 GLU A OE1 2795 O OE2 . GLU A 356 ? 0.5417 0.4107 0.4059 0.1445 -0.0364 0.0367 397 GLU A OE2 2796 N N . ILE A 357 ? 0.4356 0.3416 0.3287 0.1107 -0.0169 0.0239 398 ILE A N 2797 C CA . ILE A 357 ? 0.4353 0.3422 0.3167 0.1125 -0.0185 0.0229 398 ILE A CA 2798 C C . ILE A 357 ? 0.4477 0.3480 0.3167 0.1132 -0.0090 0.0302 398 ILE A C 2799 O O . ILE A 357 ? 0.4483 0.3418 0.2990 0.1201 -0.0097 0.0330 398 ILE A O 2800 C CB . ILE A 357 ? 0.4182 0.3371 0.3123 0.1054 -0.0210 0.0155 398 ILE A CB 2801 C CG1 . ILE A 357 ? 0.3987 0.3232 0.3023 0.1066 -0.0311 0.0085 398 ILE A CG1 2802 C CG2 . ILE A 357 ? 0.4085 0.3276 0.2914 0.1061 -0.0203 0.0153 398 ILE A CG2 2803 C CD1 . ILE A 357 ? 0.3694 0.3057 0.2890 0.0985 -0.0319 0.0022 398 ILE A CD1 2804 N N . VAL A 358 ? 0.4290 0.3310 0.3079 0.1065 0.0000 0.0331 399 VAL A N 2805 C CA . VAL A 358 ? 0.4579 0.3540 0.3284 0.1067 0.0099 0.0405 399 VAL A CA 2806 C C . VAL A 358 ? 0.4779 0.3612 0.3324 0.1152 0.0118 0.0481 399 VAL A C 2807 O O . VAL A 358 ? 0.4954 0.3725 0.3332 0.1203 0.0159 0.0530 399 VAL A O 2808 C CB . VAL A 358 ? 0.4452 0.3448 0.3317 0.0980 0.0185 0.0423 399 VAL A CB 2809 C CG1 . VAL A 358 ? 0.4716 0.3646 0.3510 0.0988 0.0292 0.0506 399 VAL A CG1 2810 C CG2 . VAL A 358 ? 0.4134 0.3249 0.3129 0.0901 0.0171 0.0353 399 VAL A CG2 2811 N N . ARG A 359 ? 0.4748 0.3538 0.3334 0.1173 0.0092 0.0493 400 ARG A N 2812 C CA . ARG A 359 ? 0.5049 0.3707 0.3481 0.1258 0.0104 0.0570 400 ARG A CA 2813 C C . ARG A 359 ? 0.5344 0.3951 0.3559 0.1356 0.0036 0.0568 400 ARG A C 2814 O O . ARG A 359 ? 0.5457 0.3959 0.3482 0.1421 0.0085 0.0642 400 ARG A O 2815 C CB . ARG A 359 ? 0.4951 0.3576 0.3472 0.1270 0.0067 0.0572 400 ARG A CB 2816 C CG . ARG A 359 ? 0.5472 0.3947 0.3852 0.1344 0.0111 0.0673 400 ARG A CG 2817 C CD . ARG A 359 ? 0.5452 0.3883 0.3879 0.1384 0.0042 0.0667 400 ARG A CD 2818 N NE . ARG A 359 ? 0.5837 0.4302 0.4212 0.1441 -0.0086 0.0598 400 ARG A NE 2819 C CZ . ARG A 359 ? 0.6178 0.4566 0.4342 0.1542 -0.0147 0.0619 400 ARG A CZ 2820 N NH1 . ARG A 359 ? 0.5818 0.4252 0.3978 0.1582 -0.0271 0.0543 400 ARG A NH1 2821 N NH2 . ARG A 359 ? 0.6408 0.4671 0.4367 0.1604 -0.0083 0.0713 400 ARG A NH2 2822 N N . SER A 360 ? 0.5306 0.3980 0.3545 0.1367 -0.0075 0.0483 401 SER A N 2823 C CA . SER A 360 ? 0.5597 0.4223 0.3638 0.1461 -0.0158 0.0465 401 SER A CA 2824 C C . SER A 360 ? 0.5669 0.4288 0.3573 0.1472 -0.0111 0.0477 401 SER A C 2825 O O . SER A 360 ? 0.5916 0.4436 0.3592 0.1563 -0.0111 0.0519 401 SER A O 2826 C CB . SER A 360 ? 0.5487 0.4193 0.3617 0.1464 -0.0290 0.0367 401 SER A CB 2827 O OG A SER A 360 ? 0.5127 0.3781 0.3064 0.1558 -0.0378 0.0345 401 SER A OG 2828 O OG B SER A 360 ? 0.5756 0.4452 0.3983 0.1476 -0.0336 0.0363 401 SER A OG 2829 N N . PHE A 361 ? 0.5462 0.4180 0.3493 0.1386 -0.0070 0.0441 402 PHE A N 2830 C CA . PHE A 361 ? 0.5467 0.4181 0.3385 0.1395 -0.0018 0.0453 402 PHE A CA 2831 C C . PHE A 361 ? 0.5777 0.4394 0.3572 0.1425 0.0104 0.0557 402 PHE A C 2832 O O . PHE A 361 ? 0.5875 0.4431 0.3475 0.1491 0.0130 0.0585 402 PHE A O 2833 C CB . PHE A 361 ? 0.5131 0.3963 0.3219 0.1296 0.0012 0.0406 402 PHE A CB 2834 C CG . PHE A 361 ? 0.4982 0.3895 0.3126 0.1281 -0.0092 0.0311 402 PHE A CG 2835 C CD1 . PHE A 361 ? 0.5233 0.4117 0.3220 0.1348 -0.0152 0.0278 402 PHE A CD1 2836 C CD2 . PHE A 361 ? 0.4723 0.3739 0.3081 0.1200 -0.0128 0.0252 402 PHE A CD2 2837 C CE1 . PHE A 361 ? 0.4931 0.3888 0.2988 0.1330 -0.0249 0.0190 402 PHE A CE1 2838 C CE2 . PHE A 361 ? 0.4547 0.3637 0.2969 0.1182 -0.0215 0.0170 402 PHE A CE2 2839 C CZ . PHE A 361 ? 0.4833 0.3893 0.3114 0.1245 -0.0279 0.0139 402 PHE A CZ 2840 N N . GLY A 362 ? 0.5624 0.4227 0.3536 0.1379 0.0181 0.0612 403 GLY A N 2841 C CA . GLY A 362 ? 0.5993 0.4506 0.3823 0.1398 0.0305 0.0716 403 GLY A CA 2842 C C . GLY A 362 ? 0.6419 0.4791 0.4006 0.1514 0.0296 0.0782 403 GLY A C 2843 O O . GLY A 362 ? 0.6589 0.4877 0.4014 0.1563 0.0389 0.0862 403 GLY A O 2844 N N . THR A 363 ? 0.6539 0.4882 0.4094 0.1562 0.0186 0.0752 404 THR A N 2845 C CA . THR A 363 ? 0.6736 0.4941 0.4045 0.1682 0.0158 0.0808 404 THR A CA 2846 C C . THR A 363 ? 0.6944 0.5111 0.4010 0.1764 0.0137 0.0797 404 THR A C 2847 O O . THR A 363 ? 0.7130 0.5178 0.3972 0.1845 0.0198 0.0879 404 THR A O 2848 C CB . THR A 363 ? 0.6764 0.4949 0.4089 0.1727 0.0027 0.0770 404 THR A CB 2849 O OG1 A THR A 363 ? 0.6468 0.4679 0.4008 0.1658 0.0056 0.0783 404 THR A OG1 2850 O OG1 B THR A 363 ? 0.6738 0.4997 0.4069 0.1742 -0.0104 0.0664 404 THR A OG1 2851 C CG2 A THR A 363 ? 0.6875 0.4909 0.3934 0.1855 0.0000 0.0835 404 THR A CG2 2852 C CG2 B THR A 363 ? 0.6514 0.4743 0.4084 0.1649 0.0042 0.0768 404 THR A CG2 2853 N N . LEU A 364 ? 0.6765 0.5026 0.3875 0.1743 0.0054 0.0698 405 LEU A N 2854 C CA . LEU A 364 ? 0.6872 0.5105 0.3775 0.1814 0.0025 0.0671 405 LEU A CA 2855 C C . LEU A 364 ? 0.6938 0.5160 0.3785 0.1796 0.0172 0.0731 405 LEU A C 2856 O O . LEU A 364 ? 0.6964 0.5099 0.3567 0.1883 0.0206 0.0768 405 LEU A O 2857 C CB . LEU A 364 ? 0.6828 0.5174 0.3836 0.1779 -0.0090 0.0549 405 LEU A CB 2858 C CG A LEU A 364 ? 0.6795 0.5190 0.3925 0.1775 -0.0235 0.0470 405 LEU A CG 2859 C CG B LEU A 364 ? 0.6835 0.5178 0.3813 0.1837 -0.0258 0.0472 405 LEU A CG 2860 C CD1 A LEU A 364 ? 0.6692 0.5202 0.3947 0.1725 -0.0316 0.0363 405 LEU A CD1 2861 C CD1 B LEU A 364 ? 0.6549 0.4910 0.3691 0.1809 -0.0304 0.0472 405 LEU A CD1 2862 C CD2 A LEU A 364 ? 0.7296 0.5578 0.4213 0.1899 -0.0334 0.0478 405 LEU A CD2 2863 C CD2 B LEU A 364 ? 0.6694 0.5144 0.3778 0.1796 -0.0345 0.0362 405 LEU A CD2 2864 N N . LYS A 365 ? 0.6662 0.4976 0.3738 0.1685 0.0257 0.0737 406 LYS A N 2865 C CA . LYS A 365 ? 0.6769 0.5083 0.3833 0.1660 0.0400 0.0796 406 LYS A CA 2866 C C . LYS A 365 ? 0.7088 0.5266 0.3980 0.1727 0.0511 0.0918 406 LYS A C 2867 O O . LYS A 365 ? 0.7176 0.5299 0.3889 0.1785 0.0590 0.0962 406 LYS A O 2868 C CB . LYS A 365 ? 0.6652 0.5080 0.4001 0.1532 0.0467 0.0784 406 LYS A CB 2869 C CG . LYS A 365 ? 0.7218 0.5663 0.4557 0.1514 0.0592 0.0823 406 LYS A CG 2870 C CD . LYS A 365 ? 0.8040 0.6549 0.5619 0.1410 0.0692 0.0856 406 LYS A CD 2871 C CE . LYS A 365 ? 0.8653 0.7082 0.6165 0.1435 0.0846 0.0970 406 LYS A CE 2872 N NZ . LYS A 365 ? 0.8856 0.7363 0.6630 0.1328 0.0933 0.0986 406 LYS A NZ 2873 N N . LYS A 366 ? 0.7047 0.5169 0.3990 0.1724 0.0520 0.0972 407 LYS A N 2874 C CA . LYS A 366 ? 0.7473 0.5456 0.4256 0.1788 0.0625 0.1097 407 LYS A CA 2875 C C . LYS A 366 ? 0.7834 0.5691 0.4272 0.1928 0.0594 0.1126 407 LYS A C 2876 O O . LYS A 366 ? 0.8158 0.5906 0.4423 0.1987 0.0709 0.1230 407 LYS A O 2877 C CB . LYS A 366 ? 0.7477 0.5417 0.4386 0.1759 0.0630 0.1146 407 LYS A CB 2878 C CG . LYS A 366 ? 0.7671 0.5704 0.4886 0.1630 0.0707 0.1147 407 LYS A CG 2879 C CD . LYS A 366 ? 0.7993 0.5999 0.5356 0.1597 0.0683 0.1166 407 LYS A CD 2880 C CE . LYS A 366 ? 0.7830 0.5927 0.5486 0.1472 0.0752 0.1156 407 LYS A CE 2881 N NZ . LYS A 366 ? 0.8096 0.6133 0.5867 0.1452 0.0765 0.1201 407 LYS A NZ 2882 N N . GLU A 367 ? 0.7912 0.5784 0.4254 0.1981 0.0442 0.1034 408 GLU A N 2883 C CA . GLU A 367 ? 0.8382 0.6143 0.4391 0.2119 0.0384 0.1037 408 GLU A CA 2884 C C . GLU A 367 ? 0.8368 0.6154 0.4249 0.2147 0.0415 0.1000 408 GLU A C 2885 O O . GLU A 367 ? 0.8690 0.6391 0.4292 0.2260 0.0364 0.0986 408 GLU A O 2886 C CB . GLU A 367 ? 0.8464 0.6226 0.4444 0.2167 0.0192 0.0949 408 GLU A CB 2887 C CG . GLU A 367 ? 0.9296 0.6984 0.5294 0.2193 0.0150 0.0999 408 GLU A CG 2888 C CD . GLU A 367 ? 1.0253 0.8005 0.6375 0.2188 -0.0028 0.0894 408 GLU A CD 2889 O OE1 . GLU A 367 ? 1.0614 0.8346 0.6842 0.2177 -0.0059 0.0918 408 GLU A OE1 2890 O OE2 . GLU A 367 ? 1.0632 0.8458 0.6764 0.2191 -0.0137 0.0788 408 GLU A OE2 2891 N N . GLY A 368 ? 0.7975 0.5873 0.4055 0.2048 0.0495 0.0980 409 GLY A N 2892 C CA . GLY A 368 ? 0.7937 0.5858 0.3917 0.2069 0.0547 0.0954 409 GLY A CA 2893 C C . GLY A 368 ? 0.7675 0.5715 0.3775 0.2023 0.0435 0.0825 409 GLY A C 2894 O O . GLY A 368 ? 0.7742 0.5812 0.3788 0.2033 0.0469 0.0793 409 GLY A O 2895 N N . TRP A 369 ? 0.7297 0.5409 0.3575 0.1970 0.0309 0.0751 410 TRP A N 2896 C CA . TRP A 369 ? 0.7018 0.5236 0.3408 0.1929 0.0200 0.0632 410 TRP A CA 2897 C C . TRP A 369 ? 0.6531 0.4880 0.3208 0.1797 0.0271 0.0618 410 TRP A C 2898 O O . TRP A 369 ? 0.6496 0.4869 0.3335 0.1727 0.0348 0.0673 410 TRP A O 2899 C CB . TRP A 369 ? 0.7011 0.5246 0.3461 0.1936 0.0036 0.0561 410 TRP A CB 2900 C CG . TRP A 369 ? 0.7010 0.5367 0.3647 0.1870 -0.0075 0.0443 410 TRP A CG 2901 C CD1 . TRP A 369 ? 0.7200 0.5562 0.3747 0.1920 -0.0192 0.0351 410 TRP A CD1 2902 C CD2 . TRP A 369 ? 0.6752 0.5235 0.3689 0.1748 -0.0080 0.0406 410 TRP A CD2 2903 N NE1 . TRP A 369 ? 0.6891 0.5374 0.3676 0.1831 -0.0262 0.0267 410 TRP A NE1 2904 C CE2 . TRP A 369 ? 0.6654 0.5212 0.3671 0.1726 -0.0194 0.0300 410 TRP A CE2 2905 C CE3 . TRP A 369 ? 0.6575 0.5111 0.3719 0.1654 0.0002 0.0452 410 TRP A CE3 2906 C CZ2 . TRP A 369 ? 0.6104 0.4787 0.3391 0.1617 -0.0221 0.0246 410 TRP A CZ2 2907 C CZ3 . TRP A 369 ? 0.6088 0.4745 0.3487 0.1551 -0.0031 0.0393 410 TRP A CZ3 2908 C CH2 . TRP A 369 ? 0.5949 0.4679 0.3413 0.1533 -0.0138 0.0293 410 TRP A CH2 2909 N N . ARG A 370 ? 0.6268 0.4695 0.3002 0.1767 0.0238 0.0542 411 ARG A N 2910 C CA . ARG A 370 ? 0.5981 0.4540 0.2997 0.1642 0.0261 0.0505 411 ARG A CA 2911 C C . ARG A 370 ? 0.5771 0.4398 0.2846 0.1627 0.0126 0.0393 411 ARG A C 2912 O O . ARG A 370 ? 0.5959 0.4536 0.2853 0.1710 0.0056 0.0349 411 ARG A O 2913 C CB . ARG A 370 ? 0.6062 0.4649 0.3095 0.1617 0.0389 0.0539 411 ARG A CB 2914 C CG . ARG A 370 ? 0.6334 0.4892 0.3406 0.1595 0.0540 0.0645 411 ARG A CG 2915 C CD . ARG A 370 ? 0.6278 0.4883 0.3408 0.1563 0.0662 0.0668 411 ARG A CD 2916 N NE . ARG A 370 ? 0.6349 0.4925 0.3544 0.1537 0.0800 0.0771 411 ARG A NE 2917 C CZ . ARG A 370 ? 0.6589 0.5227 0.4028 0.1439 0.0824 0.0786 411 ARG A CZ 2918 N NH1 . ARG A 370 ? 0.5712 0.4446 0.3335 0.1361 0.0729 0.0707 411 ARG A NH1 2919 N NH2 . ARG A 370 ? 0.6464 0.5064 0.3960 0.1419 0.0944 0.0880 411 ARG A NH2 2920 N N . PRO A 371 ? 0.5492 0.4230 0.2818 0.1524 0.0091 0.0346 412 PRO A N 2921 C CA . PRO A 371 ? 0.5285 0.4092 0.2693 0.1498 -0.0019 0.0247 412 PRO A CA 2922 C C . PRO A 371 ? 0.5255 0.4080 0.2615 0.1504 0.0014 0.0220 412 PRO A C 2923 O O . PRO A 371 ? 0.5328 0.4148 0.2669 0.1497 0.0132 0.0276 412 PRO A O 2924 C CB . PRO A 371 ? 0.5115 0.4030 0.2799 0.1379 -0.0020 0.0229 412 PRO A CB 2925 C CG . PRO A 371 ? 0.4976 0.3896 0.2732 0.1331 0.0116 0.0311 412 PRO A CG 2926 C CD . PRO A 371 ? 0.5135 0.3932 0.2674 0.1427 0.0167 0.0388 412 PRO A CD 2927 N N . ARG A 372 ? 0.5245 0.4094 0.2604 0.1515 -0.0090 0.0134 413 ARG A N 2928 C CA . ARG A 372 ? 0.5268 0.4135 0.2596 0.1520 -0.0071 0.0099 413 ARG A CA 2929 C C . ARG A 372 ? 0.4856 0.3820 0.2399 0.1413 0.0011 0.0116 413 ARG A C 2930 O O . ARG A 372 ? 0.4853 0.3819 0.2370 0.1416 0.0108 0.0148 413 ARG A O 2931 C CB . ARG A 372 ? 0.5144 0.4025 0.2477 0.1537 -0.0210 -0.0001 413 ARG A CB 2932 C CG . ARG A 372 ? 0.5644 0.4542 0.2960 0.1541 -0.0205 -0.0047 413 ARG A CG 2933 C CD . ARG A 372 ? 0.5360 0.4275 0.2722 0.1542 -0.0345 -0.0147 413 ARG A CD 2934 N NE . ARG A 372 ? 0.5862 0.4794 0.3230 0.1538 -0.0329 -0.0185 413 ARG A NE 2935 C CZ . ARG A 372 ? 0.6113 0.4973 0.3282 0.1628 -0.0329 -0.0209 413 ARG A CZ 2936 N NH1 . ARG A 372 ? 0.5820 0.4582 0.2753 0.1733 -0.0347 -0.0198 413 ARG A NH1 2937 N NH2 . ARG A 372 ? 0.6206 0.5089 0.3408 0.1616 -0.0310 -0.0243 413 ARG A NH2 2938 N N . ARG A 373 ? 0.4627 0.3672 0.2380 0.1324 -0.0025 0.0095 414 ARG A N 2939 C CA . ARG A 373 ? 0.4380 0.3515 0.2335 0.1224 0.0034 0.0104 414 ARG A CA 2940 C C . ARG A 373 ? 0.4408 0.3556 0.2458 0.1177 0.0108 0.0170 414 ARG A C 2941 O O . ARG A 373 ? 0.4532 0.3632 0.2528 0.1208 0.0090 0.0195 414 ARG A O 2942 C CB . ARG A 373 ? 0.4058 0.3271 0.2182 0.1155 -0.0060 0.0033 414 ARG A CB 2943 C CG . ARG A 373 ? 0.4308 0.3507 0.2363 0.1197 -0.0151 -0.0041 414 ARG A CG 2944 C CD . ARG A 373 ? 0.4269 0.3543 0.2502 0.1126 -0.0236 -0.0107 414 ARG A CD 2945 N NE . ARG A 373 ? 0.4301 0.3543 0.2452 0.1176 -0.0312 -0.0171 414 ARG A NE 2946 C CZ . ARG A 373 ? 0.4331 0.3519 0.2378 0.1245 -0.0410 -0.0218 414 ARG A CZ 2947 N NH1 . ARG A 373 ? 0.4129 0.3303 0.2173 0.1262 -0.0455 -0.0213 414 ARG A NH1 2948 N NH2 . ARG A 373 ? 0.4730 0.3882 0.2695 0.1295 -0.0475 -0.0278 414 ARG A NH2 2949 N N . THR A 374 ? 0.4213 0.3423 0.2409 0.1103 0.0182 0.0193 415 THR A N 2950 C CA . THR A 374 ? 0.4087 0.3314 0.2399 0.1049 0.0249 0.0247 415 THR A CA 2951 C C . THR A 374 ? 0.3883 0.3156 0.2324 0.0996 0.0172 0.0209 415 THR A C 2952 O O . THR A 374 ? 0.3800 0.3133 0.2329 0.0956 0.0103 0.0148 415 THR A O 2953 C CB . THR A 374 ? 0.3920 0.3208 0.2365 0.0985 0.0331 0.0267 415 THR A CB 2954 O OG1 . THR A 374 ? 0.4247 0.3491 0.2585 0.1037 0.0421 0.0314 415 THR A OG1 2955 C CG2 . THR A 374 ? 0.3705 0.3031 0.2319 0.0909 0.0378 0.0300 415 THR A CG2 2956 N N . ILE A 375 ? 0.3781 0.3022 0.2236 0.0997 0.0190 0.0247 416 ILE A N 2957 C CA . ILE A 375 ? 0.3612 0.2897 0.2201 0.0945 0.0140 0.0219 416 ILE A CA 2958 C C . ILE A 375 ? 0.3616 0.2934 0.2348 0.0875 0.0218 0.0256 416 ILE A C 2959 O O . ILE A 375 ? 0.3816 0.3083 0.2514 0.0891 0.0298 0.0320 416 ILE A O 2960 C CB . ILE A 375 ? 0.3651 0.2873 0.2160 0.1003 0.0085 0.0224 416 ILE A CB 2961 C CG1 . ILE A 375 ? 0.4004 0.3188 0.2366 0.1080 -0.0001 0.0183 416 ILE A CG1 2962 C CG2 . ILE A 375 ? 0.3733 0.3016 0.2406 0.0945 0.0033 0.0186 416 ILE A CG2 2963 C CD1 . ILE A 375 ? 0.4040 0.3148 0.2294 0.1155 -0.0057 0.0196 416 ILE A CD1 2964 N N . LEU A 376 ? 0.3520 0.2918 0.2410 0.0797 0.0195 0.0215 417 LEU A N 2965 C CA A LEU A 376 ? 0.3271 0.2702 0.2303 0.0731 0.0249 0.0235 417 LEU A CA 2966 C CA B LEU A 376 ? 0.3498 0.2929 0.2531 0.0730 0.0249 0.0235 417 LEU A CA 2967 C C . LEU A 376 ? 0.3430 0.2872 0.2536 0.0711 0.0203 0.0211 417 LEU A C 2968 O O . LEU A 376 ? 0.3592 0.3068 0.2716 0.0708 0.0126 0.0157 417 LEU A O 2969 C CB A LEU A 376 ? 0.3039 0.2549 0.2184 0.0663 0.0257 0.0205 417 LEU A CB 2970 C CB B LEU A 376 ? 0.3369 0.2881 0.2520 0.0660 0.0257 0.0205 417 LEU A CB 2971 C CG A LEU A 376 ? 0.2634 0.2142 0.1720 0.0684 0.0295 0.0220 417 LEU A CG 2972 C CG B LEU A 376 ? 0.4049 0.3574 0.3223 0.0645 0.0329 0.0234 417 LEU A CG 2973 C CD1 A LEU A 376 ? 0.2889 0.2472 0.2082 0.0624 0.0285 0.0186 417 LEU A CD1 2974 C CD1 B LEU A 376 ? 0.4267 0.3735 0.3295 0.0717 0.0369 0.0271 417 LEU A CD1 2975 C CD2 A LEU A 376 ? 0.2652 0.2114 0.1728 0.0699 0.0396 0.0292 417 LEU A CD2 2976 C CD2 B LEU A 376 ? 0.3791 0.3394 0.3058 0.0590 0.0302 0.0190 417 LEU A CD2 2977 N N . PHE A 377 ? 0.3394 0.2806 0.2552 0.0697 0.0251 0.0248 418 PHE A N 2978 C CA . PHE A 377 ? 0.3234 0.2652 0.2469 0.0680 0.0216 0.0227 418 PHE A CA 2979 C C . PHE A 377 ? 0.3336 0.2804 0.2725 0.0602 0.0253 0.0216 418 PHE A C 2980 O O . PHE A 377 ? 0.3579 0.3032 0.3003 0.0582 0.0320 0.0255 418 PHE A O 2981 C CB . PHE A 377 ? 0.3480 0.2808 0.2644 0.0736 0.0234 0.0278 418 PHE A CB 2982 C CG . PHE A 377 ? 0.3479 0.2749 0.2477 0.0820 0.0193 0.0288 418 PHE A CG 2983 C CD1 . PHE A 377 ? 0.3800 0.3083 0.2783 0.0849 0.0102 0.0240 418 PHE A CD1 2984 C CD2 . PHE A 377 ? 0.4121 0.3326 0.2977 0.0874 0.0243 0.0343 418 PHE A CD2 2985 C CE1 . PHE A 377 ? 0.3966 0.3187 0.2784 0.0936 0.0050 0.0244 418 PHE A CE1 2986 C CE2 . PHE A 377 ? 0.4428 0.3572 0.3109 0.0959 0.0199 0.0348 418 PHE A CE2 2987 C CZ . PHE A 377 ? 0.4155 0.3305 0.2816 0.0992 0.0097 0.0297 418 PHE A CZ 2988 N N . ALA A 378 ? 0.3164 0.2686 0.2645 0.0563 0.0210 0.0164 419 ALA A N 2989 C CA . ALA A 378 ? 0.3144 0.2709 0.2752 0.0494 0.0237 0.0147 419 ALA A CA 2990 C C . ALA A 378 ? 0.3206 0.2774 0.2888 0.0481 0.0217 0.0119 419 ALA A C 2991 O O . ALA A 378 ? 0.3345 0.2930 0.3019 0.0500 0.0165 0.0086 419 ALA A O 2992 C CB . ALA A 378 ? 0.2943 0.2583 0.2586 0.0451 0.0215 0.0105 419 ALA A CB 2993 N N . SER A 379 ? 0.3143 0.2693 0.2907 0.0450 0.0258 0.0131 420 SER A N 2994 C CA . SER A 379 ? 0.3072 0.2631 0.2925 0.0426 0.0247 0.0097 420 SER A CA 2995 C C . SER A 379 ? 0.3016 0.2635 0.2957 0.0360 0.0254 0.0057 420 SER A C 2996 O O . SER A 379 ? 0.3034 0.2639 0.3030 0.0331 0.0292 0.0074 420 SER A O 2997 C CB . SER A 379 ? 0.3262 0.2740 0.3136 0.0445 0.0287 0.0142 420 SER A CB 2998 O OG . SER A 379 ? 0.3138 0.2615 0.3106 0.0422 0.0280 0.0107 420 SER A OG 2999 N N . TRP A 380 ? 0.2937 0.2620 0.2891 0.0338 0.0217 0.0006 421 TRP A N 3000 C CA . TRP A 380 ? 0.2718 0.2456 0.2725 0.0282 0.0217 -0.0029 421 TRP A CA 3001 C C . TRP A 380 ? 0.2934 0.2670 0.3022 0.0255 0.0223 -0.0065 421 TRP A C 3002 O O . TRP A 380 ? 0.2799 0.2514 0.2905 0.0276 0.0216 -0.0078 421 TRP A O 3003 C CB . TRP A 380 ? 0.2593 0.2393 0.2575 0.0272 0.0180 -0.0066 421 TRP A CB 3004 C CG . TRP A 380 ? 0.2786 0.2592 0.2694 0.0298 0.0162 -0.0046 421 TRP A CG 3005 C CD1 . TRP A 380 ? 0.2590 0.2413 0.2466 0.0323 0.0124 -0.0061 421 TRP A CD1 3006 C CD2 . TRP A 380 ? 0.2626 0.2426 0.2493 0.0300 0.0177 -0.0015 421 TRP A CD2 3007 N NE1 . TRP A 380 ? 0.2631 0.2452 0.2441 0.0343 0.0110 -0.0044 421 TRP A NE1 3008 C CE2 . TRP A 380 ? 0.2605 0.2412 0.2403 0.0331 0.0145 -0.0015 421 TRP A CE2 3009 C CE3 . TRP A 380 ? 0.2787 0.2577 0.2679 0.0282 0.0214 0.0010 421 TRP A CE3 3010 C CZ2 . TRP A 380 ? 0.2841 0.2641 0.2582 0.0346 0.0150 0.0006 421 TRP A CZ2 3011 C CZ3 . TRP A 380 ? 0.2955 0.2747 0.2800 0.0296 0.0224 0.0035 421 TRP A CZ3 3012 C CH2 . TRP A 380 ? 0.2790 0.2583 0.2551 0.0330 0.0193 0.0033 421 TRP A CH2 3013 N N . ASP A 381 ? 0.2739 0.2493 0.2878 0.0212 0.0233 -0.0082 422 ASP A N 3014 C CA . ASP A 381 ? 0.2750 0.2502 0.2959 0.0186 0.0231 -0.0127 422 ASP A CA 3015 C C . ASP A 381 ? 0.2758 0.2571 0.2951 0.0158 0.0206 -0.0178 422 ASP A C 3016 O O . ASP A 381 ? 0.3006 0.2858 0.3153 0.0150 0.0194 -0.0172 422 ASP A O 3017 C CB . ASP A 381 ? 0.2774 0.2499 0.3057 0.0159 0.0253 -0.0114 422 ASP A CB 3018 C CG . ASP A 381 ? 0.3148 0.2839 0.3513 0.0145 0.0254 -0.0151 422 ASP A CG 3019 O OD1 . ASP A 381 ? 0.3204 0.2896 0.3563 0.0155 0.0240 -0.0191 422 ASP A OD1 3020 O OD2 . ASP A 381 ? 0.2946 0.2605 0.3389 0.0125 0.0272 -0.0140 422 ASP A OD2 3021 N N . ALA A 382 ? 0.2718 0.2533 0.2945 0.0146 0.0200 -0.0228 423 ALA A N 3022 C CA . ALA A 382 ? 0.2742 0.2604 0.2948 0.0120 0.0184 -0.0278 423 ALA A CA 3023 C C . ALA A 382 ? 0.2571 0.2482 0.2718 0.0126 0.0175 -0.0278 423 ALA A C 3024 O O . ALA A 382 ? 0.2635 0.2582 0.2746 0.0104 0.0166 -0.0296 423 ALA A O 3025 C CB . ALA A 382 ? 0.2684 0.2556 0.2904 0.0085 0.0172 -0.0288 423 ALA A CB 3026 N N . GLU A 383 ? 0.2631 0.2539 0.2770 0.0158 0.0176 -0.0257 424 GLU A N 3027 C CA . GLU A 383 ? 0.2614 0.2569 0.2721 0.0162 0.0166 -0.0262 424 GLU A CA 3028 C C . GLU A 383 ? 0.2619 0.2606 0.2738 0.0150 0.0175 -0.0311 424 GLU A C 3029 O O . GLU A 383 ? 0.2699 0.2728 0.2787 0.0133 0.0176 -0.0321 424 GLU A O 3030 C CB . GLU A 383 ? 0.2687 0.2630 0.2798 0.0202 0.0156 -0.0239 424 GLU A CB 3031 C CG . GLU A 383 ? 0.2635 0.2627 0.2734 0.0205 0.0140 -0.0246 424 GLU A CG 3032 C CD . GLU A 383 ? 0.3252 0.3282 0.3400 0.0207 0.0147 -0.0285 424 GLU A CD 3033 O OE1 . GLU A 383 ? 0.3219 0.3236 0.3403 0.0212 0.0164 -0.0312 424 GLU A OE1 3034 O OE2 . GLU A 383 ? 0.3398 0.3472 0.3555 0.0204 0.0139 -0.0289 424 GLU A OE2 3035 N N . GLU A 384 ? 0.2716 0.2678 0.2876 0.0159 0.0187 -0.0340 425 GLU A N 3036 C CA . GLU A 384 ? 0.2882 0.2873 0.3049 0.0155 0.0202 -0.0391 425 GLU A CA 3037 C C . GLU A 384 ? 0.2882 0.2888 0.2997 0.0123 0.0205 -0.0418 425 GLU A C 3038 O O . GLU A 384 ? 0.2862 0.2898 0.2954 0.0120 0.0223 -0.0452 425 GLU A O 3039 C CB . GLU A 384 ? 0.2788 0.2743 0.3011 0.0176 0.0212 -0.0421 425 GLU A CB 3040 C CG . GLU A 384 ? 0.2903 0.2840 0.3173 0.0215 0.0207 -0.0398 425 GLU A CG 3041 C CD . GLU A 384 ? 0.2933 0.2927 0.3222 0.0231 0.0208 -0.0406 425 GLU A CD 3042 O OE1 . GLU A 384 ? 0.2950 0.2996 0.3214 0.0209 0.0219 -0.0418 425 GLU A OE1 3043 O OE2 . GLU A 384 ? 0.3103 0.3089 0.3437 0.0266 0.0197 -0.0398 425 GLU A OE2 3044 N N . PHE A 385 ? 0.2843 0.2829 0.2939 0.0104 0.0187 -0.0403 426 PHE A N 3045 C CA . PHE A 385 ? 0.2738 0.2734 0.2783 0.0079 0.0178 -0.0430 426 PHE A CA 3046 C C . PHE A 385 ? 0.2913 0.2939 0.2903 0.0063 0.0167 -0.0397 426 PHE A C 3047 O O . PHE A 385 ? 0.2882 0.2909 0.2830 0.0044 0.0149 -0.0407 426 PHE A O 3048 C CB . PHE A 385 ? 0.2750 0.2705 0.2830 0.0067 0.0158 -0.0443 426 PHE A CB 3049 C CG . PHE A 385 ? 0.3011 0.2930 0.3140 0.0078 0.0165 -0.0487 426 PHE A CG 3050 C CD1 . PHE A 385 ? 0.3154 0.3065 0.3255 0.0072 0.0156 -0.0548 426 PHE A CD1 3051 C CD2 . PHE A 385 ? 0.2922 0.2808 0.3120 0.0099 0.0177 -0.0467 426 PHE A CD2 3052 C CE1 . PHE A 385 ? 0.3055 0.2926 0.3205 0.0085 0.0159 -0.0596 426 PHE A CE1 3053 C CE2 . PHE A 385 ? 0.2853 0.2698 0.3105 0.0111 0.0182 -0.0507 426 PHE A CE2 3054 C CZ . PHE A 385 ? 0.3062 0.2900 0.3295 0.0103 0.0173 -0.0575 426 PHE A CZ 3055 N N . GLY A 386 ? 0.2780 0.2827 0.2774 0.0072 0.0172 -0.0362 427 GLY A N 3056 C CA . GLY A 386 ? 0.2890 0.2965 0.2836 0.0058 0.0164 -0.0336 427 GLY A CA 3057 C C . GLY A 386 ? 0.2755 0.2822 0.2711 0.0064 0.0146 -0.0291 427 GLY A C 3058 O O . GLY A 386 ? 0.2838 0.2913 0.2760 0.0051 0.0131 -0.0272 427 GLY A O 3059 N N . LEU A 387 ? 0.2477 0.2527 0.2474 0.0089 0.0149 -0.0277 428 LEU A N 3060 C CA . LEU A 387 ? 0.2474 0.2511 0.2466 0.0105 0.0136 -0.0236 428 LEU A CA 3061 C C . LEU A 387 ? 0.2589 0.2606 0.2580 0.0093 0.0132 -0.0219 428 LEU A C 3062 O O . LEU A 387 ? 0.2673 0.2692 0.2642 0.0095 0.0122 -0.0192 428 LEU A O 3063 C CB . LEU A 387 ? 0.2640 0.2708 0.2605 0.0102 0.0123 -0.0223 428 LEU A CB 3064 C CG . LEU A 387 ? 0.2678 0.2779 0.2660 0.0100 0.0130 -0.0243 428 LEU A CG 3065 C CD1 . LEU A 387 ? 0.2786 0.2912 0.2757 0.0093 0.0115 -0.0226 428 LEU A CD1 3066 C CD2 . LEU A 387 ? 0.2755 0.2850 0.2786 0.0130 0.0133 -0.0253 428 LEU A CD2 3067 N N . LEU A 388 ? 0.2502 0.2500 0.2526 0.0082 0.0138 -0.0238 429 LEU A N 3068 C CA . LEU A 388 ? 0.2524 0.2515 0.2565 0.0064 0.0130 -0.0231 429 LEU A CA 3069 C C . LEU A 388 ? 0.2654 0.2621 0.2722 0.0080 0.0144 -0.0187 429 LEU A C 3070 O O . LEU A 388 ? 0.2760 0.2735 0.2828 0.0073 0.0140 -0.0168 429 LEU A O 3071 C CB . LEU A 388 ? 0.2555 0.2532 0.2638 0.0046 0.0127 -0.0270 429 LEU A CB 3072 C CG . LEU A 388 ? 0.2626 0.2620 0.2663 0.0036 0.0119 -0.0317 429 LEU A CG 3073 C CD1 . LEU A 388 ? 0.2691 0.2664 0.2764 0.0022 0.0105 -0.0363 429 LEU A CD1 3074 C CD2 . LEU A 388 ? 0.2904 0.2931 0.2871 0.0023 0.0103 -0.0315 429 LEU A CD2 3075 N N . GLY A 389 ? 0.2652 0.2584 0.2740 0.0104 0.0164 -0.0172 430 GLY A N 3076 C CA . GLY A 389 ? 0.2671 0.2570 0.2774 0.0124 0.0187 -0.0125 430 GLY A CA 3077 C C . GLY A 389 ? 0.2660 0.2568 0.2699 0.0147 0.0182 -0.0094 430 GLY A C 3078 O O . GLY A 389 ? 0.2745 0.2649 0.2787 0.0150 0.0196 -0.0065 430 GLY A O 3079 N N . SER A 390 ? 0.2618 0.2539 0.2609 0.0165 0.0163 -0.0103 431 SER A N 3080 C CA . SER A 390 ? 0.2645 0.2570 0.2578 0.0189 0.0151 -0.0081 431 SER A CA 3081 C C . SER A 390 ? 0.2526 0.2486 0.2453 0.0162 0.0137 -0.0086 431 SER A C 3082 O O . SER A 390 ? 0.2417 0.2372 0.2318 0.0176 0.0140 -0.0062 431 SER A O 3083 C CB . SER A 390 ? 0.2630 0.2567 0.2536 0.0207 0.0124 -0.0097 431 SER A CB 3084 O OG . SER A 390 ? 0.2716 0.2694 0.2645 0.0175 0.0113 -0.0132 431 SER A OG 3085 N N . THR A 391 ? 0.2518 0.2508 0.2461 0.0127 0.0124 -0.0116 432 THR A N 3086 C CA . THR A 391 ? 0.2433 0.2451 0.2362 0.0106 0.0105 -0.0119 432 THR A CA 3087 C C . THR A 391 ? 0.2411 0.2426 0.2376 0.0097 0.0114 -0.0105 432 THR A C 3088 O O . THR A 391 ? 0.2542 0.2566 0.2493 0.0102 0.0107 -0.0089 432 THR A O 3089 C CB . THR A 391 ? 0.2704 0.2747 0.2624 0.0076 0.0091 -0.0151 432 THR A CB 3090 O OG1 . THR A 391 ? 0.2662 0.2713 0.2566 0.0086 0.0091 -0.0160 432 THR A OG1 3091 C CG2 . THR A 391 ? 0.2735 0.2798 0.2624 0.0060 0.0068 -0.0146 432 THR A CG2 3092 N N . GLU A 392 ? 0.2382 0.2386 0.2405 0.0084 0.0129 -0.0114 433 GLU A N 3093 C CA . GLU A 392 ? 0.2559 0.2566 0.2645 0.0074 0.0138 -0.0101 433 GLU A CA 3094 C C . GLU A 392 ? 0.2534 0.2524 0.2616 0.0104 0.0170 -0.0057 433 GLU A C 3095 O O . GLU A 392 ? 0.2484 0.2490 0.2590 0.0104 0.0174 -0.0043 433 GLU A O 3096 C CB . GLU A 392 ? 0.2470 0.2462 0.2636 0.0055 0.0148 -0.0119 433 GLU A CB 3097 C CG . GLU A 392 ? 0.3042 0.3050 0.3207 0.0028 0.0113 -0.0170 433 GLU A CG 3098 C CD . GLU A 392 ? 0.2930 0.2970 0.3068 0.0013 0.0076 -0.0183 433 GLU A CD 3099 O OE1 . GLU A 392 ? 0.2921 0.2975 0.3117 0.0005 0.0067 -0.0175 433 GLU A OE1 3100 O OE2 . GLU A 392 ? 0.2945 0.2997 0.3008 0.0009 0.0056 -0.0198 433 GLU A OE2 3101 N N . TRP A 393 ? 0.2473 0.2428 0.2523 0.0134 0.0195 -0.0036 434 TRP A N 3102 C CA . TRP A 393 ? 0.2473 0.2402 0.2495 0.0171 0.0229 0.0006 434 TRP A CA 3103 C C . TRP A 393 ? 0.2622 0.2567 0.2575 0.0189 0.0207 0.0008 434 TRP A C 3104 O O . TRP A 393 ? 0.2610 0.2555 0.2561 0.0206 0.0228 0.0031 434 TRP A O 3105 C CB . TRP A 393 ? 0.2550 0.2430 0.2528 0.0206 0.0248 0.0027 434 TRP A CB 3106 C CG . TRP A 393 ? 0.2698 0.2539 0.2627 0.0251 0.0290 0.0075 434 TRP A CG 3107 C CD1 . TRP A 393 ? 0.2831 0.2644 0.2804 0.0257 0.0347 0.0116 434 TRP A CD1 3108 C CD2 . TRP A 393 ? 0.2836 0.2661 0.2661 0.0296 0.0278 0.0086 434 TRP A CD2 3109 N NE1 . TRP A 393 ? 0.2943 0.2720 0.2827 0.0309 0.0377 0.0156 434 TRP A NE1 3110 C CE2 . TRP A 393 ? 0.3116 0.2898 0.2903 0.0335 0.0330 0.0135 434 TRP A CE2 3111 C CE3 . TRP A 393 ? 0.2850 0.2689 0.2611 0.0308 0.0227 0.0058 434 TRP A CE3 3112 C CZ2 . TRP A 393 ? 0.3183 0.2932 0.2852 0.0391 0.0329 0.0152 434 TRP A CZ2 3113 C CZ3 . TRP A 393 ? 0.3195 0.3003 0.2855 0.0362 0.0219 0.0072 434 TRP A CZ3 3114 C CH2 . TRP A 393 ? 0.3193 0.2956 0.2801 0.0405 0.0269 0.0116 434 TRP A CH2 3115 N N . ALA A 394 ? 0.2588 0.2546 0.2494 0.0186 0.0167 -0.0016 435 ALA A N 3116 C CA . ALA A 394 ? 0.2716 0.2685 0.2570 0.0201 0.0142 -0.0018 435 ALA A CA 3117 C C . ALA A 394 ? 0.2681 0.2682 0.2572 0.0176 0.0131 -0.0023 435 ALA A C 3118 O O . ALA A 394 ? 0.2620 0.2621 0.2487 0.0195 0.0128 -0.0013 435 ALA A O 3119 C CB . ALA A 394 ? 0.2778 0.2755 0.2596 0.0198 0.0105 -0.0042 435 ALA A CB 3120 N N . GLU A 395 ? 0.2625 0.2649 0.2568 0.0138 0.0120 -0.0042 436 GLU A N 3121 C CA . GLU A 395 ? 0.2603 0.2655 0.2586 0.0118 0.0103 -0.0046 436 GLU A CA 3122 C C . GLU A 395 ? 0.2703 0.2756 0.2746 0.0131 0.0138 -0.0022 436 GLU A C 3123 O O . GLU A 395 ? 0.2540 0.2611 0.2597 0.0139 0.0131 -0.0016 436 GLU A O 3124 C CB . GLU A 395 ? 0.2651 0.2721 0.2674 0.0080 0.0079 -0.0075 436 GLU A CB 3125 C CG . GLU A 395 ? 0.2700 0.2774 0.2657 0.0068 0.0050 -0.0095 436 GLU A CG 3126 C CD . GLU A 395 ? 0.3165 0.3251 0.3129 0.0038 0.0027 -0.0124 436 GLU A CD 3127 O OE1 . GLU A 395 ? 0.2876 0.2968 0.2787 0.0028 0.0003 -0.0131 436 GLU A OE1 3128 O OE2 . GLU A 395 ? 0.2973 0.3057 0.2993 0.0027 0.0033 -0.0139 436 GLU A OE2 3129 N N . GLU A 396 ? 0.2438 0.2474 0.2525 0.0134 0.0177 -0.0008 437 GLU A N 3130 C CA . GLU A 396 ? 0.2599 0.2635 0.2750 0.0147 0.0224 0.0021 437 GLU A CA 3131 C C . GLU A 396 ? 0.2747 0.2766 0.2825 0.0194 0.0249 0.0048 437 GLU A C 3132 O O . GLU A 396 ? 0.2757 0.2795 0.2877 0.0205 0.0271 0.0062 437 GLU A O 3133 C CB . GLU A 396 ? 0.2635 0.2643 0.2836 0.0145 0.0268 0.0038 437 GLU A CB 3134 C CG . GLU A 396 ? 0.3386 0.3396 0.3684 0.0150 0.0328 0.0073 437 GLU A CG 3135 C CD . GLU A 396 ? 0.4883 0.4876 0.5280 0.0125 0.0353 0.0077 437 GLU A CD 3136 O OE1 . GLU A 396 ? 0.5897 0.5919 0.6418 0.0088 0.0338 0.0055 437 GLU A OE1 3137 O OE2 . GLU A 396 ? 0.4534 0.4480 0.4884 0.0142 0.0379 0.0097 437 GLU A OE2 3138 N N . ASN A 397 ? 0.2759 0.2744 0.2736 0.0222 0.0243 0.0051 438 ASN A N 3139 C CA . ASN A 397 ? 0.2755 0.2710 0.2643 0.0276 0.0266 0.0074 438 ASN A CA 3140 C C . ASN A 397 ? 0.2823 0.2781 0.2638 0.0291 0.0217 0.0051 438 ASN A C 3141 O O . ASN A 397 ? 0.2750 0.2677 0.2478 0.0337 0.0219 0.0058 438 ASN A O 3142 C CB . ASN A 397 ? 0.2996 0.2901 0.2825 0.0307 0.0296 0.0098 438 ASN A CB 3143 C CG . ASN A 397 ? 0.3108 0.3000 0.3011 0.0299 0.0356 0.0130 438 ASN A CG 3144 O OD1 . ASN A 397 ? 0.3552 0.3445 0.3486 0.0314 0.0408 0.0160 438 ASN A OD1 3145 N ND2 . ASN A 397 ? 0.3252 0.3136 0.3201 0.0272 0.0352 0.0124 438 ASN A ND2 3146 N N . SER A 398 ? 0.2597 0.2590 0.2450 0.0254 0.0172 0.0025 439 SER A N 3147 C CA . SER A 398 ? 0.2745 0.2735 0.2541 0.0260 0.0123 0.0004 439 SER A CA 3148 C C . SER A 398 ? 0.2692 0.2666 0.2440 0.0302 0.0126 0.0009 439 SER A C 3149 O O . SER A 398 ? 0.2851 0.2802 0.2533 0.0325 0.0093 -0.0004 439 SER A O 3150 C CB . SER A 398 ? 0.2778 0.2801 0.2617 0.0215 0.0083 -0.0014 439 SER A CB 3151 O OG . SER A 398 ? 0.2875 0.2922 0.2774 0.0208 0.0089 -0.0008 439 SER A OG 3152 N N . ARG A 399 ? 0.2670 0.2659 0.2464 0.0311 0.0160 0.0025 440 ARG A N 3153 C CA . ARG A 399 ? 0.2853 0.2827 0.2602 0.0357 0.0169 0.0027 440 ARG A CA 3154 C C . ARG A 399 ? 0.3087 0.3012 0.2732 0.0413 0.0197 0.0039 440 ARG A C 3155 O O . ARG A 399 ? 0.3084 0.2981 0.2649 0.0454 0.0174 0.0024 440 ARG A O 3156 C CB . ARG A 399 ? 0.2860 0.2866 0.2695 0.0358 0.0210 0.0043 440 ARG A CB 3157 C CG . ARG A 399 ? 0.3180 0.3227 0.3099 0.0314 0.0165 0.0026 440 ARG A CG 3158 C CD . ARG A 399 ? 0.3629 0.3719 0.3672 0.0294 0.0196 0.0037 440 ARG A CD 3159 N NE . ARG A 399 ? 0.3440 0.3562 0.3546 0.0258 0.0140 0.0018 440 ARG A NE 3160 C CZ . ARG A 399 ? 0.3677 0.3808 0.3797 0.0216 0.0101 0.0003 440 ARG A CZ 3161 N NH1 . ARG A 399 ? 0.3817 0.3933 0.3911 0.0199 0.0112 0.0003 440 ARG A NH1 3162 N NH2 . ARG A 399 ? 0.3179 0.3333 0.3335 0.0194 0.0050 -0.0010 440 ARG A NH2 3163 N N . LEU A 400 ? 0.3064 0.2975 0.2708 0.0419 0.0244 0.0066 441 LEU A N 3164 C CA . LEU A 400 ? 0.3105 0.2961 0.2634 0.0476 0.0268 0.0082 441 LEU A CA 3165 C C . LEU A 400 ? 0.3211 0.3042 0.2667 0.0485 0.0201 0.0052 441 LEU A C 3166 O O . LEU A 400 ? 0.3227 0.3018 0.2579 0.0536 0.0178 0.0039 441 LEU A O 3167 C CB . LEU A 400 ? 0.3190 0.3030 0.2742 0.0475 0.0330 0.0121 441 LEU A CB 3168 C CG . LEU A 400 ? 0.3347 0.3215 0.3005 0.0457 0.0400 0.0153 441 LEU A CG 3169 C CD1 . LEU A 400 ? 0.3850 0.3688 0.3528 0.0459 0.0464 0.0197 441 LEU A CD1 3170 C CD2 . LEU A 400 ? 0.3696 0.3563 0.3325 0.0501 0.0440 0.0164 441 LEU A CD2 3171 N N . LEU A 401 ? 0.2929 0.2785 0.2442 0.0436 0.0167 0.0037 442 LEU A N 3172 C CA . LEU A 401 ? 0.3018 0.2859 0.2491 0.0440 0.0112 0.0011 442 LEU A CA 3173 C C . LEU A 401 ? 0.3086 0.2928 0.2538 0.0446 0.0055 -0.0021 442 LEU A C 3174 O O . LEU A 401 ? 0.3485 0.3299 0.2875 0.0478 0.0013 -0.0043 442 LEU A O 3175 C CB . LEU A 401 ? 0.3006 0.2880 0.2559 0.0383 0.0099 0.0002 442 LEU A CB 3176 C CG . LEU A 401 ? 0.3276 0.3139 0.2852 0.0380 0.0146 0.0029 442 LEU A CG 3177 C CD1 . LEU A 401 ? 0.2839 0.2737 0.2499 0.0323 0.0135 0.0013 442 LEU A CD1 3178 C CD2 . LEU A 401 ? 0.3823 0.3634 0.3313 0.0432 0.0147 0.0040 442 LEU A CD2 3179 N N A GLN A 402 ? 0.3086 0.2961 0.2598 0.0413 0.0050 -0.0027 443 GLN A N 3180 N N B GLN A 402 ? 0.2960 0.2833 0.2468 0.0414 0.0047 -0.0028 443 GLN A N 3181 C CA A GLN A 402 ? 0.3231 0.3104 0.2740 0.0412 0.0000 -0.0053 443 GLN A CA 3182 C CA B GLN A 402 ? 0.3027 0.2893 0.2523 0.0417 -0.0007 -0.0058 443 GLN A CA 3183 C C A GLN A 402 ? 0.3286 0.3114 0.2703 0.0477 -0.0009 -0.0066 443 GLN A C 3184 C C B GLN A 402 ? 0.3152 0.2980 0.2569 0.0477 -0.0011 -0.0067 443 GLN A C 3185 O O A GLN A 402 ? 0.3283 0.3088 0.2667 0.0494 -0.0063 -0.0096 443 GLN A O 3186 O O B GLN A 402 ? 0.3185 0.2992 0.2577 0.0492 -0.0064 -0.0098 443 GLN A O 3187 C CB A GLN A 402 ? 0.3195 0.3101 0.2772 0.0380 0.0008 -0.0046 443 GLN A CB 3188 C CB B GLN A 402 ? 0.2751 0.2653 0.2323 0.0366 -0.0024 -0.0061 443 GLN A CB 3189 C CG A GLN A 402 ? 0.3453 0.3347 0.3021 0.0395 -0.0025 -0.0064 443 GLN A CG 3190 C CG B GLN A 402 ? 0.2790 0.2707 0.2393 0.0370 0.0006 -0.0046 443 GLN A CG 3191 C CD A GLN A 402 ? 0.3985 0.3880 0.3578 0.0361 -0.0080 -0.0084 443 GLN A CD 3192 C CD B GLN A 402 ? 0.3430 0.3384 0.3109 0.0317 -0.0008 -0.0044 443 GLN A CD 3193 O OE1 A GLN A 402 ? 0.4440 0.4360 0.4075 0.0315 -0.0085 -0.0078 443 GLN A OE1 3194 O OE1 B GLN A 402 ? 0.3620 0.3594 0.3344 0.0314 0.0003 -0.0035 443 GLN A OE1 3195 N NE2 A GLN A 402 ? 0.3402 0.3267 0.2971 0.0384 -0.0121 -0.0106 443 GLN A NE2 3196 N NE2 B GLN A 402 ? 0.3151 0.3115 0.2846 0.0278 -0.0034 -0.0052 443 GLN A NE2 3197 N N . GLU A 403 ? 0.3170 0.2986 0.2551 0.0514 0.0045 -0.0043 444 GLU A N 3198 C CA . GLU A 403 ? 0.3223 0.2997 0.2510 0.0580 0.0046 -0.0055 444 GLU A CA 3199 C C . GLU A 403 ? 0.3259 0.2980 0.2425 0.0640 0.0052 -0.0051 444 GLU A C 3200 O O . GLU A 403 ? 0.3360 0.3038 0.2428 0.0699 0.0030 -0.0074 444 GLU A O 3201 C CB . GLU A 403 ? 0.3527 0.3315 0.2835 0.0596 0.0107 -0.0033 444 GLU A CB 3202 C CG . GLU A 403 ? 0.3548 0.3387 0.2978 0.0543 0.0095 -0.0036 444 GLU A CG 3203 C CD . GLU A 403 ? 0.4403 0.4239 0.3850 0.0523 0.0019 -0.0071 444 GLU A CD 3204 O OE1 . GLU A 403 ? 0.4072 0.3869 0.3453 0.0548 -0.0027 -0.0100 444 GLU A OE1 3205 O OE2 . GLU A 403 ? 0.4183 0.4052 0.3715 0.0481 0.0005 -0.0070 444 GLU A OE2 3206 N N . ARG A 404 ? 0.3056 0.2778 0.2228 0.0627 0.0073 -0.0027 445 ARG A N 3207 C CA . ARG A 404 ? 0.3196 0.2861 0.2246 0.0689 0.0086 -0.0013 445 ARG A CA 3208 C C . ARG A 404 ? 0.3360 0.3017 0.2407 0.0681 0.0035 -0.0027 445 ARG A C 3209 O O . ARG A 404 ? 0.3544 0.3150 0.2484 0.0737 0.0027 -0.0022 445 ARG A O 3210 C CB . ARG A 404 ? 0.3041 0.2703 0.2092 0.0695 0.0179 0.0041 445 ARG A CB 3211 C CG . ARG A 404 ? 0.3105 0.2779 0.2167 0.0712 0.0240 0.0057 445 ARG A CG 3212 C CD . ARG A 404 ? 0.3210 0.2884 0.2298 0.0713 0.0338 0.0115 445 ARG A CD 3213 N NE . ARG A 404 ? 0.3551 0.3257 0.2702 0.0711 0.0394 0.0128 445 ARG A NE 3214 C CZ . ARG A 404 ? 0.3336 0.3061 0.2563 0.0697 0.0479 0.0173 445 ARG A CZ 3215 N NH1 . ARG A 404 ? 0.3451 0.3156 0.2686 0.0687 0.0517 0.0212 445 ARG A NH1 3216 N NH2 . ARG A 404 ? 0.3339 0.3103 0.2643 0.0695 0.0523 0.0178 445 ARG A NH2 3217 N N . GLY A 405 ? 0.3364 0.3068 0.2523 0.0616 0.0003 -0.0042 446 GLY A N 3218 C CA . GLY A 405 ? 0.3439 0.3145 0.2620 0.0604 -0.0031 -0.0052 446 GLY A CA 3219 C C . GLY A 405 ? 0.3386 0.3073 0.2533 0.0632 -0.0114 -0.0098 446 GLY A C 3220 O O . GLY A 405 ? 0.3537 0.3247 0.2740 0.0605 -0.0159 -0.0131 446 GLY A O 3221 N N . VAL A 406 ? 0.3288 0.2928 0.2345 0.0689 -0.0137 -0.0100 447 VAL A N 3222 C CA . VAL A 406 ? 0.3400 0.3021 0.2433 0.0720 -0.0225 -0.0148 447 VAL A CA 3223 C C . VAL A 406 ? 0.3279 0.2945 0.2432 0.0674 -0.0265 -0.0169 447 VAL A C 3224 O O . VAL A 406 ? 0.3255 0.2946 0.2483 0.0650 -0.0323 -0.0210 447 VAL A O 3225 C CB . VAL A 406 ? 0.3676 0.3224 0.2552 0.0810 -0.0241 -0.0143 447 VAL A CB 3226 C CG1 . VAL A 406 ? 0.3730 0.3262 0.2597 0.0842 -0.0342 -0.0196 447 VAL A CG1 3227 C CG2 . VAL A 406 ? 0.3973 0.3477 0.2725 0.0861 -0.0202 -0.0132 447 VAL A CG2 3228 N N . ALA A 407 ? 0.3266 0.2941 0.2444 0.0662 -0.0230 -0.0141 448 ALA A N 3229 C CA . ALA A 407 ? 0.3033 0.2746 0.2315 0.0630 -0.0263 -0.0160 448 ALA A CA 3230 C C . ALA A 407 ? 0.3122 0.2847 0.2439 0.0605 -0.0203 -0.0124 448 ALA A C 3231 O O . ALA A 407 ? 0.3307 0.2996 0.2553 0.0629 -0.0149 -0.0082 448 ALA A O 3232 C CB . ALA A 407 ? 0.3180 0.2860 0.2419 0.0690 -0.0341 -0.0192 448 ALA A CB 3233 N N . TYR A 408 ? 0.3094 0.2871 0.2529 0.0556 -0.0210 -0.0140 449 TYR A N 3234 C CA . TYR A 408 ? 0.3130 0.2921 0.2614 0.0531 -0.0165 -0.0118 449 TYR A CA 3235 C C . TYR A 408 ? 0.3039 0.2848 0.2589 0.0539 -0.0209 -0.0145 449 TYR A C 3236 O O . TYR A 408 ? 0.3177 0.3030 0.2813 0.0513 -0.0248 -0.0181 449 TYR A O 3237 C CB . TYR A 408 ? 0.2981 0.2824 0.2553 0.0458 -0.0121 -0.0114 449 TYR A CB 3238 C CG . TYR A 408 ? 0.2868 0.2723 0.2492 0.0434 -0.0080 -0.0101 449 TYR A CG 3239 C CD1 . TYR A 408 ? 0.3028 0.2853 0.2621 0.0437 -0.0027 -0.0065 449 TYR A CD1 3240 C CD2 . TYR A 408 ? 0.2908 0.2800 0.2616 0.0412 -0.0094 -0.0126 449 TYR A CD2 3241 C CE1 . TYR A 408 ? 0.3073 0.2900 0.2718 0.0418 0.0004 -0.0057 449 TYR A CE1 3242 C CE2 . TYR A 408 ? 0.3021 0.2919 0.2776 0.0395 -0.0059 -0.0121 449 TYR A CE2 3243 C CZ . TYR A 408 ? 0.3470 0.3334 0.3192 0.0397 -0.0013 -0.0088 449 TYR A CZ 3244 O OH . TYR A 408 ? 0.3284 0.3147 0.3057 0.0381 0.0015 -0.0087 449 TYR A OH 3245 N N . ILE A 409 ? 0.2997 0.2770 0.2514 0.0577 -0.0203 -0.0127 450 ILE A N 3246 C CA . ILE A 409 ? 0.3014 0.2802 0.2599 0.0591 -0.0242 -0.0151 450 ILE A CA 3247 C C . ILE A 409 ? 0.3099 0.2903 0.2748 0.0556 -0.0185 -0.0134 450 ILE A C 3248 O O . ILE A 409 ? 0.3129 0.2890 0.2723 0.0567 -0.0137 -0.0094 450 ILE A O 3249 C CB . ILE A 409 ? 0.3231 0.2954 0.2717 0.0673 -0.0291 -0.0146 450 ILE A CB 3250 C CG1 . ILE A 409 ? 0.3423 0.3121 0.2828 0.0717 -0.0356 -0.0171 450 ILE A CG1 3251 C CG2 . ILE A 409 ? 0.3210 0.2951 0.2781 0.0690 -0.0333 -0.0170 450 ILE A CG2 3252 C CD1 . ILE A 409 ? 0.3602 0.3362 0.3127 0.0685 -0.0417 -0.0227 450 ILE A CD1 3253 N N . ASN A 410 ? 0.2956 0.2821 0.2724 0.0513 -0.0186 -0.0163 451 ASN A N 3254 C CA . ASN A 410 ? 0.3060 0.2941 0.2890 0.0481 -0.0134 -0.0156 451 ASN A CA 3255 C C . ASN A 410 ? 0.3270 0.3123 0.3115 0.0526 -0.0153 -0.0157 451 ASN A C 3256 O O . ASN A 410 ? 0.3453 0.3294 0.3289 0.0574 -0.0214 -0.0172 451 ASN A O 3257 C CB . ASN A 410 ? 0.2894 0.2849 0.2835 0.0423 -0.0122 -0.0189 451 ASN A CB 3258 C CG . ASN A 410 ? 0.3308 0.3276 0.3279 0.0381 -0.0062 -0.0183 451 ASN A CG 3259 O OD1 . ASN A 410 ? 0.3502 0.3444 0.3421 0.0366 -0.0028 -0.0157 451 ASN A OD1 3260 N ND2 . ASN A 410 ? 0.3280 0.3285 0.3337 0.0364 -0.0051 -0.0210 451 ASN A ND2 3261 N N . ALA A 411 ? 0.3185 0.3023 0.3057 0.0514 -0.0108 -0.0143 452 ALA A N 3262 C CA . ALA A 411 ? 0.3288 0.3092 0.3176 0.0560 -0.0125 -0.0141 452 ALA A CA 3263 C C . ALA A 411 ? 0.3339 0.3161 0.3311 0.0524 -0.0079 -0.0151 452 ALA A C 3264 O O . ALA A 411 ? 0.3501 0.3268 0.3454 0.0540 -0.0051 -0.0124 452 ALA A O 3265 C CB . ALA A 411 ? 0.3516 0.3229 0.3281 0.0615 -0.0121 -0.0090 452 ALA A CB 3266 N N . ASP A 412 ? 0.3129 0.3023 0.3198 0.0484 -0.0074 -0.0192 453 ASP A N 3267 C CA . ASP A 412 ? 0.3270 0.3181 0.3418 0.0464 -0.0039 -0.0213 453 ASP A CA 3268 C C . ASP A 412 ? 0.3469 0.3385 0.3683 0.0511 -0.0080 -0.0234 453 ASP A C 3269 O O . ASP A 412 ? 0.3543 0.3424 0.3710 0.0563 -0.0131 -0.0219 453 ASP A O 3270 C CB . ASP A 412 ? 0.3053 0.3034 0.3256 0.0404 -0.0007 -0.0244 453 ASP A CB 3271 C CG . ASP A 412 ? 0.3194 0.3183 0.3449 0.0380 0.0037 -0.0266 453 ASP A CG 3272 O OD1 . ASP A 412 ? 0.3660 0.3606 0.3932 0.0408 0.0040 -0.0263 453 ASP A OD1 3273 O OD2 . ASP A 412 ? 0.3108 0.3142 0.3382 0.0335 0.0067 -0.0287 453 ASP A OD2 3274 N N A SER A 413 ? 0.3365 0.3321 0.3679 0.0498 -0.0060 -0.0269 454 SER A N 3275 N N B SER A 413 ? 0.3306 0.3264 0.3623 0.0498 -0.0061 -0.0270 454 SER A N 3276 C CA A SER A 413 ? 0.3363 0.3327 0.3760 0.0543 -0.0093 -0.0292 454 SER A CA 3277 C CA B SER A 413 ? 0.3244 0.3208 0.3644 0.0543 -0.0091 -0.0293 454 SER A CA 3278 C C A SER A 413 ? 0.3437 0.3406 0.3834 0.0589 -0.0167 -0.0294 454 SER A C 3279 C C B SER A 413 ? 0.3303 0.3281 0.3727 0.0589 -0.0165 -0.0303 454 SER A C 3280 O O A SER A 413 ? 0.3302 0.3322 0.3718 0.0569 -0.0190 -0.0310 454 SER A O 3281 O O B SER A 413 ? 0.3172 0.3223 0.3674 0.0570 -0.0183 -0.0333 454 SER A O 3282 C CB A SER A 413 ? 0.3377 0.3418 0.3898 0.0514 -0.0062 -0.0340 454 SER A CB 3283 C CB B SER A 413 ? 0.3212 0.3247 0.3730 0.0511 -0.0053 -0.0339 454 SER A CB 3284 O OG A SER A 413 ? 0.3131 0.3167 0.3636 0.0471 0.0000 -0.0345 454 SER A OG 3285 O OG B SER A 413 ? 0.2758 0.2871 0.3324 0.0474 -0.0051 -0.0361 454 SER A OG 3286 N N . SER A 414 ? 0.3331 0.3239 0.3697 0.0652 -0.0208 -0.0278 455 SER A N 3287 C CA . SER A 414 ? 0.3705 0.3609 0.4062 0.0707 -0.0292 -0.0285 455 SER A CA 3288 C C . SER A 414 ? 0.3757 0.3741 0.4280 0.0716 -0.0329 -0.0338 455 SER A C 3289 O O . SER A 414 ? 0.3869 0.3883 0.4429 0.0738 -0.0395 -0.0361 455 SER A O 3290 C CB . SER A 414 ? 0.3856 0.3660 0.4108 0.0778 -0.0324 -0.0244 455 SER A CB 3291 O OG . SER A 414 ? 0.4479 0.4216 0.4586 0.0771 -0.0289 -0.0194 455 SER A OG 3292 N N . ILE A 415 ? 0.3927 0.3944 0.4555 0.0701 -0.0285 -0.0360 456 ILE A N 3293 C CA . ILE A 415 ? 0.4069 0.4166 0.4871 0.0710 -0.0307 -0.0411 456 ILE A CA 3294 C C . ILE A 415 ? 0.4134 0.4306 0.5033 0.0649 -0.0225 -0.0440 456 ILE A C 3295 O O . ILE A 415 ? 0.4574 0.4714 0.5419 0.0623 -0.0164 -0.0427 456 ILE A O 3296 C CB . ILE A 415 ? 0.4146 0.4202 0.4987 0.0778 -0.0345 -0.0414 456 ILE A CB 3297 C CG1 . ILE A 415 ? 0.4376 0.4353 0.5142 0.0779 -0.0289 -0.0382 456 ILE A CG1 3298 C CG2 . ILE A 415 ? 0.4291 0.4288 0.5051 0.0846 -0.0438 -0.0395 456 ILE A CG2 3299 C CD1 . ILE A 415 ? 0.5352 0.5321 0.6218 0.0817 -0.0290 -0.0403 456 ILE A CD1 3300 N N . GLU A 416 ? 0.3926 0.4193 0.4964 0.0625 -0.0223 -0.0478 457 GLU A N 3301 C CA . GLU A 416 ? 0.3841 0.4177 0.4980 0.0583 -0.0144 -0.0507 457 GLU A CA 3302 C C . GLU A 416 ? 0.3743 0.4159 0.5074 0.0609 -0.0168 -0.0551 457 GLU A C 3303 O O . GLU A 416 ? 0.3736 0.4228 0.5185 0.0580 -0.0108 -0.0582 457 GLU A O 3304 C CB . GLU A 416 ? 0.3918 0.4294 0.5025 0.0515 -0.0092 -0.0501 457 GLU A CB 3305 C CG . GLU A 416 ? 0.4113 0.4540 0.5285 0.0504 -0.0139 -0.0507 457 GLU A CG 3306 C CD . GLU A 416 ? 0.4487 0.4942 0.5619 0.0438 -0.0092 -0.0493 457 GLU A CD 3307 O OE1 . GLU A 416 ? 0.4468 0.4885 0.5481 0.0408 -0.0040 -0.0471 457 GLU A OE1 3308 O OE2 . GLU A 416 ? 0.4505 0.5016 0.5734 0.0419 -0.0112 -0.0505 457 GLU A OE2 3309 N N . GLY A 417 ? 0.3697 0.4092 0.5058 0.0667 -0.0259 -0.0554 458 GLY A N 3310 C CA . GLY A 417 ? 0.3735 0.4200 0.5289 0.0703 -0.0302 -0.0597 458 GLY A CA 3311 C C . GLY A 417 ? 0.3782 0.4195 0.5302 0.0772 -0.0418 -0.0591 458 GLY A C 3312 O O . GLY A 417 ? 0.3857 0.4176 0.5195 0.0791 -0.0450 -0.0550 458 GLY A O 3313 N N . ASN A 418 ? 0.3670 0.4142 0.5361 0.0810 -0.0482 -0.0630 459 ASN A N 3314 C CA . ASN A 418 ? 0.3848 0.4266 0.5501 0.0885 -0.0603 -0.0629 459 ASN A CA 3315 C C . ASN A 418 ? 0.3705 0.4202 0.5521 0.0894 -0.0686 -0.0673 459 ASN A C 3316 O O . ASN A 418 ? 0.3970 0.4452 0.5829 0.0963 -0.0791 -0.0693 459 ASN A O 3317 C CB . ASN A 418 ? 0.4006 0.4370 0.5663 0.0956 -0.0630 -0.0626 459 ASN A CB 3318 C CG . ASN A 418 ? 0.4226 0.4685 0.6123 0.0966 -0.0614 -0.0678 459 ASN A CG 3319 O OD1 . ASN A 418 ? 0.3852 0.4425 0.5936 0.0930 -0.0599 -0.0718 459 ASN A OD1 3320 N ND2 . ASN A 418 ? 0.6004 0.6416 0.7908 0.1017 -0.0614 -0.0675 459 ASN A ND2 3321 N N . TYR A 419 ? 0.3530 0.4105 0.5432 0.0826 -0.0644 -0.0687 460 TYR A N 3322 C CA . TYR A 419 ? 0.3365 0.4029 0.5467 0.0823 -0.0711 -0.0734 460 TYR A CA 3323 C C . TYR A 419 ? 0.3495 0.4109 0.5484 0.0833 -0.0801 -0.0728 460 TYR A C 3324 O O . TYR A 419 ? 0.3439 0.4052 0.5487 0.0888 -0.0921 -0.0761 460 TYR A O 3325 C CB . TYR A 419 ? 0.3334 0.4107 0.5606 0.0743 -0.0611 -0.0750 460 TYR A CB 3326 C CG . TYR A 419 ? 0.3874 0.4747 0.6390 0.0730 -0.0668 -0.0796 460 TYR A CG 3327 C CD1 . TYR A 419 ? 0.4414 0.5348 0.7143 0.0783 -0.0741 -0.0844 460 TYR A CD1 3328 C CD2 . TYR A 419 ? 0.4390 0.5297 0.6940 0.0667 -0.0648 -0.0793 460 TYR A CD2 3329 C CE1 . TYR A 419 ? 0.4867 0.5898 0.7847 0.0768 -0.0796 -0.0891 460 TYR A CE1 3330 C CE2 . TYR A 419 ? 0.4494 0.5490 0.7287 0.0651 -0.0699 -0.0836 460 TYR A CE2 3331 C CZ . TYR A 419 ? 0.5075 0.6136 0.8086 0.0699 -0.0771 -0.0885 460 TYR A CZ 3332 O OH . TYR A 419 ? 0.5611 0.6763 0.8879 0.0679 -0.0821 -0.0929 460 TYR A OH 3333 N N . THR A 420 ? 0.3395 0.3967 0.5224 0.0783 -0.0747 -0.0692 461 THR A N 3334 C CA . THR A 420 ? 0.3443 0.3970 0.5167 0.0790 -0.0825 -0.0690 461 THR A CA 3335 C C . THR A 420 ? 0.3369 0.3825 0.4870 0.0754 -0.0760 -0.0639 461 THR A C 3336 O O . THR A 420 ? 0.3372 0.3818 0.4811 0.0719 -0.0659 -0.0607 461 THR A O 3337 C CB . THR A 420 ? 0.3509 0.4127 0.5442 0.0752 -0.0864 -0.0736 461 THR A CB 3338 O OG1 . THR A 420 ? 0.3481 0.4044 0.5319 0.0785 -0.0973 -0.0749 461 THR A OG1 3339 C CG2 . THR A 420 ? 0.3315 0.3988 0.5297 0.0659 -0.0751 -0.0719 461 THR A CG2 3340 N N . LEU A 421 ? 0.3304 0.3706 0.4685 0.0769 -0.0826 -0.0636 462 LEU A N 3341 C CA . LEU A 421 ? 0.3243 0.3584 0.4429 0.0735 -0.0771 -0.0592 462 LEU A CA 3342 C C . LEU A 421 ? 0.3179 0.3585 0.4447 0.0647 -0.0689 -0.0589 462 LEU A C 3343 O O . LEU A 421 ? 0.3089 0.3576 0.4550 0.0615 -0.0702 -0.0624 462 LEU A O 3344 C CB . LEU A 421 ? 0.3395 0.3661 0.4435 0.0784 -0.0867 -0.0595 462 LEU A CB 3345 C CG . LEU A 421 ? 0.3294 0.3477 0.4100 0.0776 -0.0820 -0.0545 462 LEU A CG 3346 C CD1 . LEU A 421 ? 0.3386 0.3492 0.4040 0.0817 -0.0781 -0.0498 462 LEU A CD1 3347 C CD2 . LEU A 421 ? 0.3577 0.3706 0.4285 0.0824 -0.0924 -0.0566 462 LEU A CD2 3348 N N . ARG A 422 ? 0.3029 0.3397 0.4153 0.0610 -0.0606 -0.0545 463 ARG A N 3349 C CA . ARG A 422 ? 0.3021 0.3428 0.4171 0.0532 -0.0532 -0.0533 463 ARG A CA 3350 C C . ARG A 422 ? 0.3157 0.3485 0.4104 0.0532 -0.0532 -0.0498 463 ARG A C 3351 O O . ARG A 422 ? 0.3254 0.3512 0.4041 0.0560 -0.0514 -0.0465 463 ARG A O 3352 C CB . ARG A 422 ? 0.3106 0.3551 0.4295 0.0490 -0.0422 -0.0517 463 ARG A CB 3353 C CG . ARG A 422 ? 0.3381 0.3859 0.4572 0.0414 -0.0337 -0.0498 463 ARG A CG 3354 C CD . ARG A 422 ? 0.3697 0.4210 0.4918 0.0383 -0.0237 -0.0491 463 ARG A CD 3355 N NE . ARG A 422 ? 0.4592 0.5137 0.5816 0.0316 -0.0159 -0.0474 463 ARG A NE 3356 C CZ . ARG A 422 ? 0.4764 0.5336 0.5992 0.0284 -0.0068 -0.0468 463 ARG A CZ 3357 N NH1 . ARG A 422 ? 0.4623 0.5200 0.5867 0.0309 -0.0039 -0.0482 463 ARG A NH1 3358 N NH2 . ARG A 422 ? 0.4837 0.5428 0.6048 0.0229 -0.0006 -0.0449 463 ARG A NH2 3359 N N . VAL A 423 ? 0.3033 0.3370 0.3992 0.0499 -0.0548 -0.0504 464 VAL A N 3360 C CA . VAL A 423 ? 0.3100 0.3368 0.3878 0.0498 -0.0546 -0.0475 464 VAL A CA 3361 C C . VAL A 423 ? 0.3144 0.3445 0.3958 0.0423 -0.0484 -0.0461 464 VAL A C 3362 O O . VAL A 423 ? 0.3181 0.3541 0.4151 0.0387 -0.0491 -0.0484 464 VAL A O 3363 C CB . VAL A 423 ? 0.3255 0.3477 0.3980 0.0552 -0.0654 -0.0501 464 VAL A CB 3364 C CG1 . VAL A 423 ? 0.3266 0.3416 0.3806 0.0556 -0.0649 -0.0474 464 VAL A CG1 3365 C CG2 . VAL A 423 ? 0.3367 0.3548 0.4046 0.0633 -0.0724 -0.0513 464 VAL A CG2 3366 N N . ASP A 424 ? 0.2893 0.3155 0.3568 0.0403 -0.0427 -0.0422 465 ASP A N 3367 C CA . ASP A 424 ? 0.3188 0.3459 0.3854 0.0346 -0.0386 -0.0405 465 ASP A CA 3368 C C . ASP A 424 ? 0.3055 0.3253 0.3554 0.0371 -0.0410 -0.0386 465 ASP A C 3369 O O . ASP A 424 ? 0.3168 0.3319 0.3540 0.0400 -0.0392 -0.0362 465 ASP A O 3370 C CB . ASP A 424 ? 0.3213 0.3504 0.3857 0.0296 -0.0288 -0.0374 465 ASP A CB 3371 C CG . ASP A 424 ? 0.4251 0.4612 0.5038 0.0269 -0.0240 -0.0388 465 ASP A CG 3372 O OD1 . ASP A 424 ? 0.4858 0.5259 0.5775 0.0290 -0.0277 -0.0420 465 ASP A OD1 3373 O OD2 . ASP A 424 ? 0.5391 0.5768 0.6156 0.0230 -0.0163 -0.0369 465 ASP A OD2 3374 N N . CYS A 425 ? 0.3010 0.3199 0.3512 0.0355 -0.0440 -0.0393 466 CYS A N 3375 C CA . CYS A 425 ? 0.3033 0.3154 0.3379 0.0383 -0.0460 -0.0379 466 CYS A CA 3376 C C . CYS A 425 ? 0.3081 0.3200 0.3454 0.0350 -0.0474 -0.0385 466 CYS A C 3377 O O . CYS A 425 ? 0.3430 0.3595 0.3944 0.0310 -0.0478 -0.0400 466 CYS A O 3378 C CB . CYS A 425 ? 0.3017 0.3084 0.3276 0.0463 -0.0537 -0.0399 466 CYS A CB 3379 S SG . CYS A 425 ? 0.3330 0.3405 0.3693 0.0495 -0.0653 -0.0460 466 CYS A SG 3380 N N . THR A 426 ? 0.3015 0.3082 0.3258 0.0366 -0.0476 -0.0369 467 THR A N 3381 C CA . THR A 426 ? 0.2887 0.2938 0.3146 0.0348 -0.0505 -0.0380 467 THR A CA 3382 C C . THR A 426 ? 0.2952 0.2994 0.3282 0.0380 -0.0602 -0.0433 467 THR A C 3383 O O . THR A 426 ? 0.2983 0.3003 0.3270 0.0441 -0.0657 -0.0457 467 THR A O 3384 C CB . THR A 426 ? 0.2968 0.2961 0.3067 0.0372 -0.0491 -0.0358 467 THR A CB 3385 O OG1 . THR A 426 ? 0.3047 0.3016 0.3158 0.0368 -0.0532 -0.0377 467 THR A OG1 3386 C CG2 . THR A 426 ? 0.2937 0.2878 0.2902 0.0448 -0.0520 -0.0362 467 THR A CG2 3387 N N . PRO A 427 ? 0.2924 0.2979 0.3366 0.0344 -0.0628 -0.0452 468 PRO A N 3388 C CA . PRO A 427 ? 0.3102 0.3140 0.3609 0.0379 -0.0732 -0.0510 468 PRO A CA 3389 C C . PRO A 427 ? 0.3195 0.3156 0.3524 0.0459 -0.0795 -0.0532 468 PRO A C 3390 O O . PRO A 427 ? 0.3305 0.3247 0.3653 0.0507 -0.0887 -0.0583 468 PRO A O 3391 C CB . PRO A 427 ? 0.3088 0.3130 0.3704 0.0325 -0.0738 -0.0516 468 PRO A CB 3392 C CG . PRO A 427 ? 0.3175 0.3263 0.3845 0.0255 -0.0636 -0.0463 468 PRO A CG 3393 C CD . PRO A 427 ? 0.3035 0.3115 0.3551 0.0272 -0.0571 -0.0424 468 PRO A CD 3394 N N . LEU A 428 ? 0.3220 0.3139 0.3385 0.0473 -0.0745 -0.0496 469 LEU A N 3395 C CA . LEU A 428 ? 0.3358 0.3201 0.3345 0.0551 -0.0790 -0.0512 469 LEU A CA 3396 C C . LEU A 428 ? 0.3411 0.3235 0.3320 0.0619 -0.0826 -0.0522 469 LEU A C 3397 O O . LEU A 428 ? 0.3725 0.3487 0.3507 0.0692 -0.0887 -0.0548 469 LEU A O 3398 C CB . LEU A 428 ? 0.3238 0.3051 0.3085 0.0551 -0.0716 -0.0465 469 LEU A CB 3399 C CG . LEU A 428 ? 0.3193 0.3001 0.3075 0.0509 -0.0702 -0.0462 469 LEU A CG 3400 C CD1 . LEU A 428 ? 0.3457 0.3242 0.3213 0.0513 -0.0631 -0.0418 469 LEU A CD1 3401 C CD2 . LEU A 428 ? 0.3265 0.3028 0.3154 0.0544 -0.0797 -0.0522 469 LEU A CD2 3402 N N . MET A 429 ? 0.3360 0.3230 0.3338 0.0598 -0.0789 -0.0500 470 MET A N 3403 C CA . MET A 429 ? 0.3364 0.3213 0.3274 0.0662 -0.0821 -0.0504 470 MET A CA 3404 C C . MET A 429 ? 0.3389 0.3277 0.3452 0.0671 -0.0902 -0.0554 470 MET A C 3405 O O . MET A 429 ? 0.3478 0.3348 0.3496 0.0728 -0.0940 -0.0561 470 MET A O 3406 C CB . MET A 429 ? 0.3469 0.3332 0.3338 0.0645 -0.0727 -0.0447 470 MET A CB 3407 C CG . MET A 429 ? 0.3773 0.3586 0.3472 0.0658 -0.0656 -0.0398 470 MET A CG 3408 S SD . MET A 429 ? 0.4891 0.4735 0.4611 0.0622 -0.0558 -0.0344 470 MET A SD 3409 C CE . MET A 429 ? 0.4633 0.4444 0.4228 0.0609 -0.0475 -0.0294 470 MET A CE 3410 N N . TYR A 430 ? 0.3158 0.3094 0.3402 0.0621 -0.0933 -0.0589 471 TYR A N 3411 C CA . TYR A 430 ? 0.3381 0.3368 0.3804 0.0625 -0.1003 -0.0635 471 TYR A CA 3412 C C . TYR A 430 ? 0.3635 0.3566 0.3976 0.0717 -0.1124 -0.0686 471 TYR A C 3413 O O . TYR A 430 ? 0.3657 0.3605 0.4044 0.0755 -0.1170 -0.0703 471 TYR A O 3414 C CB . TYR A 430 ? 0.3331 0.3369 0.3967 0.0563 -0.1028 -0.0668 471 TYR A CB 3415 C CG . TYR A 430 ? 0.3164 0.3272 0.3936 0.0472 -0.0924 -0.0628 471 TYR A CG 3416 C CD1 . TYR A 430 ? 0.3021 0.3150 0.3736 0.0447 -0.0820 -0.0573 471 TYR A CD1 3417 C CD2 . TYR A 430 ? 0.3463 0.3604 0.4408 0.0413 -0.0931 -0.0645 471 TYR A CD2 3418 C CE1 . TYR A 430 ? 0.3450 0.3634 0.4269 0.0368 -0.0729 -0.0540 471 TYR A CE1 3419 C CE2 . TYR A 430 ? 0.3648 0.3842 0.4696 0.0335 -0.0836 -0.0605 471 TYR A CE2 3420 C CZ . TYR A 430 ? 0.3911 0.4126 0.4890 0.0315 -0.0737 -0.0554 471 TYR A CZ 3421 O OH . TYR A 430 ? 0.3727 0.3987 0.4792 0.0244 -0.0647 -0.0517 471 TYR A OH 3422 N N . SER A 431 ? 0.3751 0.3616 0.3974 0.0755 -0.1179 -0.0712 472 SER A N 3423 C CA . SER A 431 ? 0.3757 0.3560 0.3882 0.0850 -0.1303 -0.0768 472 SER A CA 3424 C C . SER A 431 ? 0.3879 0.3626 0.3801 0.0925 -0.1291 -0.0733 472 SER A C 3425 O O . SER A 431 ? 0.4037 0.3768 0.3951 0.0989 -0.1378 -0.0766 472 SER A O 3426 C CB . SER A 431 ? 0.4163 0.3900 0.4186 0.0876 -0.1355 -0.0803 472 SER A CB 3427 O OG A SER A 431 ? 0.4202 0.3986 0.4443 0.0811 -0.1387 -0.0844 472 SER A OG 3428 O OG B SER A 431 ? 0.3763 0.3438 0.3691 0.0969 -0.1482 -0.0865 472 SER A OG 3429 N N . LEU A 432 ? 0.3855 0.3575 0.3629 0.0916 -0.1183 -0.0666 473 LEU A N 3430 C CA . LEU A 432 ? 0.3957 0.3623 0.3548 0.0976 -0.1147 -0.0618 473 LEU A CA 3431 C C . LEU A 432 ? 0.3913 0.3628 0.3626 0.0971 -0.1150 -0.0611 473 LEU A C 3432 O O . LEU A 432 ? 0.3852 0.3523 0.3477 0.1047 -0.1206 -0.0615 473 LEU A O 3433 C CB . LEU A 432 ? 0.3844 0.3497 0.3330 0.0941 -0.1017 -0.0547 473 LEU A CB 3434 C CG . LEU A 432 ? 0.4095 0.3712 0.3454 0.0974 -0.0949 -0.0484 473 LEU A CG 3435 C CD1 . LEU A 432 ? 0.4867 0.4387 0.4014 0.1083 -0.1008 -0.0484 473 LEU A CD1 3436 C CD2 . LEU A 432 ? 0.4639 0.4255 0.3941 0.0928 -0.0829 -0.0423 473 LEU A CD2 3437 N N . VAL A 433 ? 0.3787 0.3590 0.3694 0.0886 -0.1087 -0.0598 474 VAL A N 3438 C CA . VAL A 433 ? 0.3691 0.3545 0.3724 0.0879 -0.1080 -0.0594 474 VAL A CA 3439 C C . VAL A 433 ? 0.3751 0.3624 0.3900 0.0925 -0.1209 -0.0661 474 VAL A C 3440 O O . VAL A 433 ? 0.3870 0.3728 0.4003 0.0981 -0.1251 -0.0663 474 VAL A O 3441 C CB . VAL A 433 ? 0.3498 0.3447 0.3724 0.0779 -0.0989 -0.0576 474 VAL A CB 3442 C CG1 . VAL A 433 ? 0.3837 0.3848 0.4222 0.0774 -0.0989 -0.0585 474 VAL A CG1 3443 C CG2 . VAL A 433 ? 0.3813 0.3745 0.3928 0.0739 -0.0869 -0.0512 474 VAL A CG2 3444 N N . HIS A 434 ? 0.3660 0.3565 0.3942 0.0900 -0.1275 -0.0717 475 HIS A N 3445 C CA . HIS A 434 ? 0.3943 0.3866 0.4350 0.0945 -0.1411 -0.0789 475 HIS A CA 3446 C C . HIS A 434 ? 0.4154 0.3979 0.4345 0.1059 -0.1505 -0.0804 475 HIS A C 3447 O O . HIS A 434 ? 0.4156 0.3985 0.4388 0.1113 -0.1579 -0.0827 475 HIS A O 3448 C CB . HIS A 434 ? 0.3971 0.3924 0.4535 0.0912 -0.1482 -0.0852 475 HIS A CB 3449 C CG . HIS A 434 ? 0.4530 0.4579 0.5330 0.0805 -0.1404 -0.0842 475 HIS A CG 3450 N ND1 . HIS A 434 ? 0.5657 0.5722 0.6571 0.0754 -0.1421 -0.0871 475 HIS A ND1 3451 C CD2 . HIS A 434 ? 0.4723 0.4846 0.5650 0.0743 -0.1301 -0.0802 475 HIS A CD2 3452 C CE1 . HIS A 434 ? 0.5546 0.5692 0.6643 0.0664 -0.1329 -0.0844 475 HIS A CE1 3453 N NE2 . HIS A 434 ? 0.4943 0.5127 0.6048 0.0658 -0.1256 -0.0804 475 HIS A NE2 3454 N N . ASN A 435 ? 0.4216 0.3952 0.4175 0.1100 -0.1504 -0.0792 476 ASN A N 3455 C CA . ASN A 435 ? 0.4426 0.4060 0.4153 0.1215 -0.1594 -0.0807 476 ASN A CA 3456 C C . ASN A 435 ? 0.4389 0.3981 0.3983 0.1267 -0.1553 -0.0748 476 ASN A C 3457 O O . ASN A 435 ? 0.4529 0.4076 0.4057 0.1353 -0.1652 -0.0772 476 ASN A O 3458 C CB . ASN A 435 ? 0.4563 0.4110 0.4061 0.1250 -0.1583 -0.0802 476 ASN A CB 3459 C CG . ASN A 435 ? 0.5091 0.4646 0.4681 0.1235 -0.1670 -0.0880 476 ASN A CG 3460 O OD1 . ASN A 435 ? 0.4684 0.4313 0.4521 0.1192 -0.1732 -0.0932 476 ASN A OD1 3461 N ND2 . ASN A 435 ? 0.5339 0.4820 0.4742 0.1269 -0.1669 -0.0886 476 ASN A ND2 3462 N N . LEU A 436 ? 0.4320 0.3925 0.3883 0.1215 -0.1414 -0.0673 477 LEU A N 3463 C CA . LEU A 436 ? 0.4346 0.3910 0.3800 0.1253 -0.1363 -0.0612 477 LEU A CA 3464 C C . LEU A 436 ? 0.4201 0.3822 0.3838 0.1257 -0.1410 -0.0633 477 LEU A C 3465 O O . LEU A 436 ? 0.4300 0.3864 0.3839 0.1339 -0.1467 -0.0625 477 LEU A O 3466 C CB . LEU A 436 ? 0.4233 0.3803 0.3641 0.1189 -0.1206 -0.0534 477 LEU A CB 3467 C CG . LEU A 436 ? 0.4511 0.4043 0.3841 0.1214 -0.1143 -0.0469 477 LEU A CG 3468 C CD1 . LEU A 436 ? 0.4831 0.4241 0.3904 0.1326 -0.1185 -0.0441 477 LEU A CD1 3469 C CD2 . LEU A 436 ? 0.4322 0.3876 0.3659 0.1138 -0.0997 -0.0405 477 LEU A CD2 3470 N N . THR A 437 ? 0.4091 0.3823 0.3990 0.1173 -0.1387 -0.0658 478 THR A N 3471 C CA . THR A 437 ? 0.4099 0.3897 0.4194 0.1175 -0.1423 -0.0680 478 THR A CA 3472 C C . THR A 437 ? 0.4310 0.4095 0.4448 0.1255 -0.1586 -0.0751 478 THR A C 3473 O O . THR A 437 ? 0.4194 0.3991 0.4404 0.1298 -0.1637 -0.0760 478 THR A O 3474 C CB . THR A 437 ? 0.3903 0.3824 0.4270 0.1070 -0.1351 -0.0690 478 THR A CB 3475 O OG1 . THR A 437 ? 0.3768 0.3738 0.4268 0.1024 -0.1393 -0.0742 478 THR A OG1 3476 C CG2 . THR A 437 ? 0.3631 0.3556 0.3934 0.1001 -0.1192 -0.0618 478 THR A CG2 3477 N N . LYS A 438 ? 0.4527 0.4286 0.4627 0.1278 -0.1676 -0.0804 479 LYS A N 3478 C CA . LYS A 438 ? 0.4747 0.4480 0.4859 0.1365 -0.1845 -0.0876 479 LYS A CA 3479 C C . LYS A 438 ? 0.5025 0.4637 0.4857 0.1482 -0.1896 -0.0847 479 LYS A C 3480 O O . LYS A 438 ? 0.5190 0.4779 0.5029 0.1562 -0.2028 -0.0893 479 LYS A O 3481 C CB . LYS A 438 ? 0.4812 0.4536 0.4942 0.1365 -0.1938 -0.0947 479 LYS A CB 3482 C CG . LYS A 438 ? 0.4732 0.4573 0.5170 0.1260 -0.1917 -0.0986 479 LYS A CG 3483 C CD . LYS A 438 ? 0.5311 0.5139 0.5793 0.1261 -0.2020 -0.1062 479 LYS A CD 3484 C CE . LYS A 438 ? 0.5121 0.5052 0.5874 0.1142 -0.1951 -0.1069 479 LYS A CE 3485 N NZ . LYS A 438 ? 0.5524 0.5439 0.6323 0.1123 -0.2017 -0.1128 479 LYS A NZ 3486 N N . GLU A 439 ? 0.5109 0.4641 0.4699 0.1495 -0.1792 -0.0769 480 GLU A N 3487 C CA . GLU A 439 ? 0.5551 0.4958 0.4860 0.1607 -0.1824 -0.0729 480 GLU A CA 3488 C C . GLU A 439 ? 0.5468 0.4868 0.4778 0.1612 -0.1751 -0.0660 480 GLU A C 3489 O O . GLU A 439 ? 0.5698 0.4994 0.4794 0.1702 -0.1771 -0.0619 480 GLU A O 3490 C CB . GLU A 439 ? 0.5860 0.5169 0.4883 0.1631 -0.1753 -0.0680 480 GLU A CB 3491 C CG . GLU A 439 ? 0.6626 0.5915 0.5591 0.1644 -0.1825 -0.0745 480 GLU A CG 3492 C CD . GLU A 439 ? 0.7891 0.7139 0.6819 0.1741 -0.2009 -0.0829 480 GLU A CD 3493 O OE1 . GLU A 439 ? 0.8706 0.7979 0.7719 0.1726 -0.2090 -0.0907 480 GLU A OE1 3494 O OE2 . GLU A 439 ? 0.8321 0.7505 0.7135 0.1833 -0.2080 -0.0820 480 GLU A OE2 3495 N N . LEU A 440 ? 0.5068 0.4569 0.4605 0.1517 -0.1659 -0.0645 481 LEU A N 3496 C CA . LEU A 440 ? 0.4807 0.4309 0.4376 0.1514 -0.1589 -0.0588 481 LEU A CA 3497 C C . LEU A 440 ? 0.4880 0.4449 0.4673 0.1534 -0.1677 -0.0637 481 LEU A C 3498 O O . LEU A 440 ? 0.4849 0.4515 0.4872 0.1498 -0.1740 -0.0709 481 LEU A O 3499 C CB . LEU A 440 ? 0.4474 0.4039 0.4141 0.1404 -0.1430 -0.0543 481 LEU A CB 3500 C CG . LEU A 440 ? 0.4526 0.4036 0.4001 0.1376 -0.1328 -0.0488 481 LEU A CG 3501 C CD1 . LEU A 440 ? 0.3934 0.3514 0.3530 0.1270 -0.1190 -0.0453 481 LEU A CD1 3502 C CD2 . LEU A 440 ? 0.4533 0.3909 0.3731 0.1463 -0.1310 -0.0420 481 LEU A CD2 3503 N N . LYS A 441 ? 0.4950 0.4470 0.4690 0.1588 -0.1673 -0.0596 482 LYS A N 3504 C CA A LYS A 441 ? 0.5108 0.4686 0.5054 0.1617 -0.1759 -0.0640 482 LYS A CA 3505 C CA B LYS A 441 ? 0.5121 0.4696 0.5062 0.1619 -0.1756 -0.0636 482 LYS A CA 3506 C C . LYS A 441 ? 0.4916 0.4619 0.5135 0.1516 -0.1658 -0.0643 482 LYS A C 3507 O O . LYS A 441 ? 0.4910 0.4612 0.5093 0.1454 -0.1520 -0.0586 482 LYS A O 3508 C CB A LYS A 441 ? 0.5317 0.4785 0.5096 0.1725 -0.1809 -0.0598 482 LYS A CB 3509 C CB B LYS A 441 ? 0.5286 0.4755 0.5066 0.1711 -0.1773 -0.0581 482 LYS A CB 3510 C CG A LYS A 441 ? 0.5788 0.5134 0.5295 0.1837 -0.1925 -0.0604 482 LYS A CG 3511 C CG B LYS A 441 ? 0.5886 0.5210 0.5353 0.1825 -0.1855 -0.0558 482 LYS A CG 3512 C CD A LYS A 441 ? 0.6424 0.5698 0.5865 0.1953 -0.2040 -0.0603 482 LYS A CD 3513 C CD B LYS A 441 ? 0.6381 0.5594 0.5686 0.1898 -0.1831 -0.0480 482 LYS A CD 3514 C CE A LYS A 441 ? 0.6727 0.5868 0.5920 0.2007 -0.1963 -0.0499 482 LYS A CE 3515 C CE B LYS A 441 ? 0.6591 0.5859 0.6114 0.1921 -0.1893 -0.0509 482 LYS A CE 3516 N NZ A LYS A 441 ? 0.7046 0.6059 0.5902 0.2059 -0.1939 -0.0449 482 LYS A NZ 3517 N NZ B LYS A 441 ? 0.7048 0.6206 0.6433 0.1991 -0.1869 -0.0432 482 LYS A NZ 3518 N N . SER A 442 ? 0.4701 0.4513 0.5195 0.1497 -0.1725 -0.0713 483 SER A N 3519 C CA . SER A 442 ? 0.4596 0.4524 0.5340 0.1410 -0.1624 -0.0716 483 SER A CA 3520 C C . SER A 442 ? 0.4559 0.4454 0.5296 0.1450 -0.1591 -0.0676 483 SER A C 3521 O O . SER A 442 ? 0.4851 0.4699 0.5563 0.1542 -0.1698 -0.0689 483 SER A O 3522 C CB . SER A 442 ? 0.4444 0.4504 0.5507 0.1378 -0.1690 -0.0797 483 SER A CB 3523 O OG . SER A 442 ? 0.4359 0.4517 0.5634 0.1309 -0.1582 -0.0791 483 SER A OG 3524 N N . PRO A 443 ? 0.4523 0.4442 0.5295 0.1383 -0.1450 -0.0632 484 PRO A N 3525 C CA . PRO A 443 ? 0.4512 0.4402 0.5305 0.1420 -0.1424 -0.0603 484 PRO A CA 3526 C C . PRO A 443 ? 0.4502 0.4518 0.5610 0.1399 -0.1433 -0.0660 484 PRO A C 3527 O O . PRO A 443 ? 0.4449 0.4454 0.5607 0.1426 -0.1410 -0.0645 484 PRO A O 3528 C CB . PRO A 443 ? 0.4312 0.4172 0.5007 0.1355 -0.1271 -0.0539 484 PRO A CB 3529 C CG . PRO A 443 ? 0.4369 0.4320 0.5155 0.1255 -0.1205 -0.0562 484 PRO A CG 3530 C CD . PRO A 443 ? 0.4374 0.4332 0.5145 0.1281 -0.1317 -0.0607 484 PRO A CD 3531 N N . ASP A 444 ? 0.4341 0.4474 0.5660 0.1348 -0.1458 -0.0722 485 ASP A N 3532 C CA . ASP A 444 ? 0.4338 0.4605 0.5967 0.1308 -0.1430 -0.0769 485 ASP A CA 3533 C C . ASP A 444 ? 0.4527 0.4815 0.6301 0.1393 -0.1560 -0.0816 485 ASP A C 3534 O O . ASP A 444 ? 0.4466 0.4709 0.6176 0.1463 -0.1698 -0.0843 485 ASP A O 3535 C CB . ASP A 444 ? 0.4163 0.4545 0.5981 0.1229 -0.1418 -0.0817 485 ASP A CB 3536 C CG . ASP A 444 ? 0.4380 0.4757 0.6089 0.1139 -0.1292 -0.0776 485 ASP A CG 3537 O OD1 . ASP A 444 ? 0.4722 0.5012 0.6216 0.1136 -0.1217 -0.0715 485 ASP A OD1 3538 O OD2 . ASP A 444 ? 0.4286 0.4745 0.6133 0.1071 -0.1270 -0.0804 485 ASP A OD2 3539 N N . GLU A 445 ? 0.4581 0.4941 0.6558 0.1388 -0.1517 -0.0833 486 GLU A N 3540 C CA A GLU A 445 ? 0.4845 0.5250 0.7015 0.1460 -0.1631 -0.0884 486 GLU A CA 3541 C CA B GLU A 445 ? 0.4824 0.5228 0.6993 0.1461 -0.1633 -0.0885 486 GLU A CA 3542 C C . GLU A 445 ? 0.4772 0.5287 0.7173 0.1442 -0.1722 -0.0960 486 GLU A C 3543 O O . GLU A 445 ? 0.4699 0.5312 0.7249 0.1351 -0.1644 -0.0978 486 GLU A O 3544 C CB A GLU A 445 ? 0.4787 0.5259 0.7144 0.1445 -0.1542 -0.0889 486 GLU A CB 3545 C CB B GLU A 445 ? 0.4762 0.5235 0.7125 0.1449 -0.1550 -0.0891 486 GLU A CB 3546 C CG A GLU A 445 ? 0.5203 0.5556 0.7387 0.1510 -0.1526 -0.0835 486 GLU A CG 3547 C CG B GLU A 445 ? 0.5031 0.5554 0.7610 0.1528 -0.1667 -0.0946 486 GLU A CG 3548 C CD A GLU A 445 ? 0.5623 0.5903 0.7606 0.1454 -0.1382 -0.0766 486 GLU A CD 3549 C CD B GLU A 445 ? 0.5412 0.5899 0.8003 0.1573 -0.1626 -0.0923 486 GLU A CD 3550 O OE1 A GLU A 445 ? 0.5948 0.6289 0.7960 0.1361 -0.1276 -0.0765 486 GLU A OE1 3551 O OE1 B GLU A 445 ? 0.5622 0.6070 0.8238 0.1669 -0.1744 -0.0937 486 GLU A OE1 3552 O OE2 A GLU A 445 ? 0.5891 0.6049 0.7688 0.1505 -0.1377 -0.0712 486 GLU A OE2 3553 O OE2 B GLU A 445 ? 0.5459 0.5951 0.8031 0.1515 -0.1482 -0.0892 486 GLU A OE2 3554 N N . GLY A 446 ? 0.5071 0.5563 0.7496 0.1529 -0.1889 -0.1002 487 GLY A N 3555 C CA . GLY A 446 ? 0.5022 0.5611 0.7674 0.1518 -0.1994 -0.1080 487 GLY A CA 3556 C C . GLY A 446 ? 0.5230 0.5752 0.7693 0.1515 -0.2059 -0.1083 487 GLY A C 3557 O O . GLY A 446 ? 0.5378 0.5957 0.8000 0.1516 -0.2167 -0.1150 487 GLY A O 3558 N N . PHE A 447 ? 0.5086 0.5488 0.7224 0.1512 -0.1995 -0.1015 488 PHE A N 3559 C CA . PHE A 447 ? 0.5127 0.5457 0.7066 0.1516 -0.2049 -0.1017 488 PHE A CA 3560 C C . PHE A 447 ? 0.5372 0.5536 0.6956 0.1614 -0.2110 -0.0971 488 PHE A C 3561 O O . PHE A 447 ? 0.5373 0.5453 0.6713 0.1610 -0.2093 -0.0941 488 PHE A O 3562 C CB . PHE A 447 ? 0.4863 0.5212 0.6747 0.1407 -0.1898 -0.0979 488 PHE A CB 3563 C CG . PHE A 447 ? 0.4533 0.5029 0.6729 0.1311 -0.1842 -0.1020 488 PHE A CG 3564 C CD1 . PHE A 447 ? 0.4431 0.4969 0.6732 0.1279 -0.1908 -0.1072 488 PHE A CD1 3565 C CD2 . PHE A 447 ? 0.4371 0.4960 0.6758 0.1254 -0.1721 -0.1008 488 PHE A CD2 3566 C CE1 . PHE A 447 ? 0.4613 0.5282 0.7207 0.1186 -0.1848 -0.1103 488 PHE A CE1 3567 C CE2 . PHE A 447 ? 0.4545 0.5268 0.7214 0.1166 -0.1658 -0.1041 488 PHE A CE2 3568 C CZ . PHE A 447 ? 0.4595 0.5358 0.7372 0.1131 -0.1719 -0.1085 488 PHE A CZ 3569 N N . GLU A 448 ? 0.5560 0.5673 0.7108 0.1703 -0.2172 -0.0959 489 GLU A N 3570 C CA . GLU A 448 ? 0.5921 0.5867 0.7120 0.1804 -0.2229 -0.0907 489 GLU A CA 3571 C C . GLU A 448 ? 0.5998 0.5888 0.7067 0.1866 -0.2381 -0.0955 489 GLU A C 3572 O O . GLU A 448 ? 0.6061 0.6027 0.7340 0.1883 -0.2509 -0.1040 489 GLU A O 3573 C CB . GLU A 448 ? 0.6144 0.6034 0.7322 0.1894 -0.2272 -0.0881 489 GLU A CB 3574 C CG . GLU A 448 ? 0.6511 0.6523 0.8033 0.1904 -0.2336 -0.0947 489 GLU A CG 3575 C CD . GLU A 448 ? 0.6426 0.6571 0.8217 0.1797 -0.2187 -0.0949 489 GLU A CD 3576 O OE1 . GLU A 448 ? 0.6413 0.6527 0.8146 0.1777 -0.2066 -0.0890 489 GLU A OE1 3577 O OE2 . GLU A 448 ? 0.6557 0.6839 0.8626 0.1735 -0.2194 -0.1014 489 GLU A OE2 3578 N N . GLY A 449 ? 0.6026 0.5789 0.6763 0.1895 -0.2360 -0.0904 490 GLY A N 3579 C CA . GLY A 449 ? 0.6133 0.5837 0.6724 0.1953 -0.2492 -0.0952 490 GLY A CA 3580 C C . GLY A 449 ? 0.5963 0.5749 0.6679 0.1861 -0.2470 -0.1001 490 GLY A C 3581 O O . GLY A 449 ? 0.6207 0.5950 0.6821 0.1899 -0.2576 -0.1050 490 GLY A O 3582 N N . LYS A 450 ? 0.5484 0.5383 0.6416 0.1743 -0.2336 -0.0992 491 LYS A N 3583 C CA . LYS A 450 ? 0.5312 0.5279 0.6348 0.1653 -0.2301 -0.1026 491 LYS A CA 3584 C C . LYS A 450 ? 0.5052 0.4965 0.5876 0.1593 -0.2141 -0.0947 491 LYS A C 3585 O O . LYS A 450 ? 0.5105 0.4963 0.5787 0.1599 -0.2042 -0.0871 491 LYS A O 3586 C CB . LYS A 450 ? 0.5189 0.5322 0.6623 0.1562 -0.2268 -0.1075 491 LYS A CB 3587 C CG . LYS A 450 ? 0.5536 0.5738 0.7225 0.1618 -0.2421 -0.1154 491 LYS A CG 3588 C CD . LYS A 450 ? 0.6364 0.6513 0.7988 0.1694 -0.2610 -0.1228 491 LYS A CD 3589 C CE . LYS A 450 ? 0.7390 0.7590 0.9231 0.1769 -0.2778 -0.1304 491 LYS A CE 3590 N NZ . LYS A 450 ? 0.7597 0.7969 0.9867 0.1685 -0.2739 -0.1347 491 LYS A NZ 3591 N N . SER A 451 ? 0.4843 0.4770 0.5658 0.1537 -0.2123 -0.0967 492 SER A N 3592 C CA . SER A 451 ? 0.4729 0.4611 0.5358 0.1481 -0.1984 -0.0901 492 SER A CA 3593 C C . SER A 451 ? 0.4439 0.4418 0.5246 0.1370 -0.1827 -0.0865 492 SER A C 3594 O O . SER A 451 ? 0.4364 0.4459 0.5461 0.1320 -0.1824 -0.0904 492 SER A O 3595 C CB . SER A 451 ? 0.4735 0.4597 0.5301 0.1466 -0.2029 -0.0940 492 SER A CB 3596 O OG . SER A 451 ? 0.4658 0.4638 0.5510 0.1372 -0.2014 -0.0988 492 SER A OG 3597 N N . LEU A 452 ? 0.4277 0.4209 0.4910 0.1332 -0.1696 -0.0793 493 LEU A N 3598 C CA . LEU A 452 ? 0.4079 0.4091 0.4846 0.1228 -0.1550 -0.0761 493 LEU A CA 3599 C C . LEU A 452 ? 0.3938 0.4041 0.4896 0.1145 -0.1544 -0.0806 493 LEU A C 3600 O O . LEU A 452 ? 0.3736 0.3942 0.4917 0.1071 -0.1472 -0.0813 493 LEU A O 3601 C CB . LEU A 452 ? 0.3926 0.3861 0.4456 0.1208 -0.1428 -0.0681 493 LEU A CB 3602 C CG . LEU A 452 ? 0.3871 0.3868 0.4485 0.1106 -0.1279 -0.0645 493 LEU A CG 3603 C CD1 . LEU A 452 ? 0.3846 0.3915 0.4653 0.1089 -0.1236 -0.0647 493 LEU A CD1 3604 C CD2 . LEU A 452 ? 0.3551 0.3459 0.3920 0.1106 -0.1189 -0.0573 493 LEU A CD2 3605 N N . TYR A 453 ? 0.4064 0.4126 0.4933 0.1161 -0.1614 -0.0836 494 TYR A N 3606 C CA . TYR A 453 ? 0.4077 0.4213 0.5128 0.1087 -0.1618 -0.0879 494 TYR A CA 3607 C C . TYR A 453 ? 0.3980 0.4229 0.5361 0.1067 -0.1679 -0.0941 494 TYR A C 3608 O O . TYR A 453 ? 0.3884 0.4229 0.5484 0.0979 -0.1611 -0.0949 494 TYR A O 3609 C CB . TYR A 453 ? 0.4276 0.4340 0.5187 0.1122 -0.1710 -0.0914 494 TYR A CB 3610 C CG . TYR A 453 ? 0.4259 0.4388 0.5358 0.1045 -0.1713 -0.0955 494 TYR A CG 3611 C CD1 . TYR A 453 ? 0.4017 0.4139 0.5051 0.0975 -0.1608 -0.0915 494 TYR A CD1 3612 C CD2 . TYR A 453 ? 0.4554 0.4748 0.5904 0.1044 -0.1827 -0.1034 494 TYR A CD2 3613 C CE1 . TYR A 453 ? 0.4374 0.4546 0.5577 0.0905 -0.1611 -0.0948 494 TYR A CE1 3614 C CE2 . TYR A 453 ? 0.4463 0.4711 0.5996 0.0970 -0.1827 -0.1068 494 TYR A CE2 3615 C CZ . TYR A 453 ? 0.4249 0.4483 0.5701 0.0902 -0.1716 -0.1022 494 TYR A CZ 3616 O OH . TYR A 453 ? 0.4457 0.4734 0.6080 0.0829 -0.1709 -0.1046 494 TYR A OH 3617 N N . GLU A 454 ? 0.3995 0.4232 0.5412 0.1150 -0.1806 -0.0985 495 GLU A N 3618 C CA . GLU A 454 ? 0.4309 0.4659 0.6060 0.1138 -0.1875 -0.1050 495 GLU A CA 3619 C C . GLU A 454 ? 0.4075 0.4524 0.6025 0.1081 -0.1757 -0.1023 495 GLU A C 3620 O O . GLU A 454 ? 0.4048 0.4609 0.6273 0.1008 -0.1716 -0.1048 495 GLU A O 3621 C CB . GLU A 454 ? 0.4459 0.4770 0.6198 0.1248 -0.2051 -0.1106 495 GLU A CB 3622 C CG . GLU A 454 ? 0.5092 0.5526 0.7194 0.1241 -0.2118 -0.1171 495 GLU A CG 3623 C CD . GLU A 454 ? 0.5915 0.6320 0.8039 0.1344 -0.2315 -0.1243 495 GLU A CD 3624 O OE1 . GLU A 454 ? 0.6378 0.6690 0.8308 0.1398 -0.2418 -0.1270 495 GLU A OE1 3625 O OE2 . GLU A 454 ? 0.6052 0.6527 0.8390 0.1372 -0.2368 -0.1276 495 GLU A OE2 3626 N N . SER A 455 ? 0.4053 0.4457 0.5858 0.1113 -0.1693 -0.0969 496 SER A N 3627 C CA . SER A 455 ? 0.3999 0.4487 0.5969 0.1066 -0.1579 -0.0946 496 SER A CA 3628 C C . SER A 455 ? 0.3877 0.4418 0.5896 0.0957 -0.1427 -0.0911 496 SER A C 3629 O O . SER A 455 ? 0.3822 0.4473 0.6087 0.0896 -0.1361 -0.0925 496 SER A O 3630 C CB . SER A 455 ? 0.4060 0.4477 0.5862 0.1127 -0.1550 -0.0898 496 SER A CB 3631 O OG . SER A 455 ? 0.4230 0.4542 0.5740 0.1127 -0.1479 -0.0831 496 SER A OG 3632 N N . TRP A 456 ? 0.3757 0.4220 0.5540 0.0936 -0.1372 -0.0864 497 TRP A N 3633 C CA . TRP A 456 ? 0.3670 0.4166 0.5460 0.0842 -0.1240 -0.0828 497 TRP A CA 3634 C C . TRP A 456 ? 0.3749 0.4332 0.5771 0.0776 -0.1250 -0.0869 497 TRP A C 3635 O O . TRP A 456 ? 0.3496 0.4161 0.5676 0.0700 -0.1145 -0.0856 497 TRP A O 3636 C CB . TRP A 456 ? 0.3574 0.3962 0.5064 0.0848 -0.1206 -0.0778 497 TRP A CB 3637 C CG . TRP A 456 ? 0.3479 0.3881 0.4933 0.0760 -0.1086 -0.0739 497 TRP A CG 3638 C CD1 . TRP A 456 ? 0.3170 0.3647 0.4748 0.0685 -0.0968 -0.0719 497 TRP A CD1 3639 C CD2 . TRP A 456 ? 0.3490 0.3824 0.4759 0.0748 -0.1075 -0.0714 497 TRP A CD2 3640 N NE1 . TRP A 456 ? 0.2950 0.3409 0.4434 0.0626 -0.0893 -0.0684 497 TRP A NE1 3641 C CE2 . TRP A 456 ? 0.3719 0.4092 0.5019 0.0662 -0.0956 -0.0681 497 TRP A CE2 3642 C CE3 . TRP A 456 ? 0.3765 0.4007 0.4840 0.0805 -0.1156 -0.0720 497 TRP A CE3 3643 C CZ2 . TRP A 456 ? 0.3513 0.3840 0.4671 0.0630 -0.0920 -0.0652 497 TRP A CZ2 3644 C CZ3 . TRP A 456 ? 0.3965 0.4162 0.4899 0.0773 -0.1111 -0.0692 497 TRP A CZ3 3645 C CH2 . TRP A 456 ? 0.3903 0.4144 0.4887 0.0685 -0.0997 -0.0659 497 TRP A CH2 3646 N N . THR A 457 ? 0.3841 0.4400 0.5881 0.0807 -0.1375 -0.0917 498 THR A N 3647 C CA . THR A 457 ? 0.3897 0.4530 0.6167 0.0746 -0.1394 -0.0957 498 THR A CA 3648 C C . THR A 457 ? 0.3970 0.4727 0.6577 0.0724 -0.1395 -0.0996 498 THR A C 3649 O O . THR A 457 ? 0.3877 0.4717 0.6688 0.0644 -0.1318 -0.0995 498 THR A O 3650 C CB . THR A 457 ? 0.4094 0.4666 0.6310 0.0791 -0.1542 -0.1010 498 THR A CB 3651 O OG1 A THR A 457 ? 0.4023 0.4492 0.5948 0.0798 -0.1514 -0.0970 498 THR A OG1 3652 C CG2 A THR A 457 ? 0.4240 0.4889 0.6733 0.0727 -0.1571 -0.1057 498 THR A CG2 3653 N N . LYS A 458 ? 0.4079 0.4848 0.6745 0.0796 -0.1477 -0.1028 499 LYS A N 3654 C CA . LYS A 458 ? 0.4302 0.5195 0.7294 0.0780 -0.1468 -0.1064 499 LYS A CA 3655 C C . LYS A 458 ? 0.4174 0.5132 0.7230 0.0713 -0.1291 -0.1014 499 LYS A C 3656 O O . LYS A 458 ? 0.4091 0.5154 0.7407 0.0649 -0.1226 -0.1026 499 LYS A O 3657 C CB . LYS A 458 ? 0.4463 0.5352 0.7500 0.0876 -0.1593 -0.1106 499 LYS A CB 3658 C CG . LYS A 458 ? 0.5006 0.6033 0.8427 0.0867 -0.1616 -0.1160 499 LYS A CG 3659 C CD . LYS A 458 ? 0.5778 0.6877 0.9466 0.0819 -0.1681 -0.1218 499 LYS A CD 3660 C CE . LYS A 458 ? 0.5963 0.7174 1.0011 0.0844 -0.1775 -0.1291 499 LYS A CE 3661 N NZ . LYS A 458 ? 0.6148 0.7452 1.0360 0.0828 -0.1659 -0.1271 499 LYS A NZ 3662 N N . LYS A 459 ? 0.4119 0.5010 0.6934 0.0726 -0.1211 -0.0958 500 LYS A N 3663 C CA . LYS A 459 ? 0.4040 0.4984 0.6901 0.0679 -0.1059 -0.0921 500 LYS A CA 3664 C C . LYS A 459 ? 0.4047 0.5001 0.6862 0.0589 -0.0929 -0.0877 500 LYS A C 3665 O O . LYS A 459 ? 0.3971 0.4994 0.6891 0.0539 -0.0807 -0.0859 500 LYS A O 3666 C CB . LYS A 459 ? 0.3974 0.4842 0.6620 0.0734 -0.1036 -0.0886 500 LYS A CB 3667 C CG . LYS A 459 ? 0.4153 0.5026 0.6885 0.0823 -0.1145 -0.0926 500 LYS A CG 3668 C CD . LYS A 459 ? 0.4179 0.4959 0.6681 0.0877 -0.1120 -0.0883 500 LYS A CD 3669 C CE . LYS A 459 ? 0.4377 0.5166 0.6977 0.0957 -0.1200 -0.0914 500 LYS A CE 3670 N NZ . LYS A 459 ? 0.4551 0.5246 0.6936 0.1000 -0.1158 -0.0865 500 LYS A NZ 3671 N N . SER A 460 ? 0.3857 0.4737 0.6499 0.0574 -0.0954 -0.0858 501 SER A N 3672 C CA . SER A 460 ? 0.3929 0.4803 0.6498 0.0497 -0.0842 -0.0813 501 SER A CA 3673 C C . SER A 460 ? 0.4080 0.4938 0.6682 0.0469 -0.0905 -0.0830 501 SER A C 3674 O O . SER A 460 ? 0.4015 0.4785 0.6399 0.0475 -0.0924 -0.0808 501 SER A O 3675 C CB . SER A 460 ? 0.3833 0.4612 0.6100 0.0511 -0.0789 -0.0760 501 SER A CB 3676 O OG . SER A 460 ? 0.4075 0.4861 0.6291 0.0438 -0.0669 -0.0716 501 SER A OG 3677 N N . PRO A 461 ? 0.4199 0.5141 0.7085 0.0440 -0.0941 -0.0873 502 PRO A N 3678 C CA . PRO A 461 ? 0.4306 0.5229 0.7246 0.0416 -0.1012 -0.0897 502 PRO A CA 3679 C C . PRO A 461 ? 0.4497 0.5393 0.7343 0.0342 -0.0908 -0.0843 502 PRO A C 3680 O O . PRO A 461 ? 0.4326 0.5263 0.7196 0.0287 -0.0774 -0.0799 502 PRO A O 3681 C CB . PRO A 461 ? 0.4385 0.5418 0.7692 0.0393 -0.1052 -0.0950 502 PRO A CB 3682 C CG . PRO A 461 ? 0.4243 0.5364 0.7688 0.0383 -0.0954 -0.0938 502 PRO A CG 3683 C CD . PRO A 461 ? 0.4083 0.5142 0.7263 0.0427 -0.0910 -0.0900 502 PRO A CD 3684 N N . SER A 462 ? 0.4800 0.5621 0.7526 0.0346 -0.0974 -0.0849 503 SER A N 3685 C CA . SER A 462 ? 0.5198 0.5995 0.7875 0.0277 -0.0897 -0.0807 503 SER A CA 3686 C C . SER A 462 ? 0.5381 0.6271 0.8357 0.0202 -0.0839 -0.0809 503 SER A C 3687 O O . SER A 462 ? 0.5333 0.6282 0.8558 0.0207 -0.0916 -0.0863 503 SER A O 3688 C CB . SER A 462 ? 0.5258 0.5968 0.7811 0.0302 -0.1002 -0.0831 503 SER A CB 3689 O OG . SER A 462 ? 0.5483 0.6186 0.8079 0.0233 -0.0949 -0.0805 503 SER A OG 3690 N N . PRO A 463 ? 0.5630 0.6533 0.8586 0.0133 -0.0704 -0.0749 504 PRO A N 3691 C CA . PRO A 463 ? 0.5928 0.6905 0.9150 0.0058 -0.0636 -0.0738 504 PRO A CA 3692 C C . PRO A 463 ? 0.6226 0.7178 0.9575 0.0033 -0.0722 -0.0768 504 PRO A C 3693 O O . PRO A 463 ? 0.6292 0.7314 0.9934 -0.0007 -0.0724 -0.0789 504 PRO A O 3694 C CB . PRO A 463 ? 0.5818 0.6780 0.8903 0.0005 -0.0483 -0.0661 504 PRO A CB 3695 C CG . PRO A 463 ? 0.5844 0.6746 0.8637 0.0051 -0.0468 -0.0639 504 PRO A CG 3696 C CD . PRO A 463 ? 0.5635 0.6479 0.8322 0.0125 -0.0609 -0.0687 504 PRO A CD 3697 N N . GLU A 464 ? 0.6553 0.7406 0.9693 0.0058 -0.0793 -0.0771 505 GLU A N 3698 C CA . GLU A 464 ? 0.6844 0.7659 1.0077 0.0037 -0.0875 -0.0801 505 GLU A CA 3699 C C . GLU A 464 ? 0.6926 0.7718 1.0219 0.0100 -0.1052 -0.0888 505 GLU A C 3700 O O . GLU A 464 ? 0.7014 0.7809 1.0501 0.0076 -0.1124 -0.0930 505 GLU A O 3701 C CB . GLU A 464 ? 0.6917 0.7638 0.9929 0.0013 -0.0836 -0.0753 505 GLU A CB 3702 C CG . GLU A 464 ? 0.7417 0.8073 1.0094 0.0053 -0.0797 -0.0713 505 GLU A CG 3703 C CD . GLU A 464 ? 0.7997 0.8677 1.0598 0.0006 -0.0640 -0.0636 505 GLU A CD 3704 O OE1 . GLU A 464 ? 0.8187 0.8808 1.0534 0.0021 -0.0599 -0.0597 505 GLU A OE1 3705 O OE2 . GLU A 464 ? 0.8227 0.8985 1.1021 -0.0043 -0.0556 -0.0617 505 GLU A OE2 3706 N N . PHE A 465 ? 0.6942 0.7705 1.0070 0.0181 -0.1125 -0.0916 506 PHE A N 3707 C CA . PHE A 465 ? 0.7017 0.7735 1.0133 0.0252 -0.1297 -0.0995 506 PHE A CA 3708 C C . PHE A 465 ? 0.6962 0.7730 1.0173 0.0314 -0.1379 -0.1046 506 PHE A C 3709 O O . PHE A 465 ? 0.6924 0.7692 0.9992 0.0356 -0.1342 -0.1021 506 PHE A O 3710 C CB . PHE A 465 ? 0.7201 0.7799 0.9978 0.0306 -0.1340 -0.0988 506 PHE A CB 3711 C CG . PHE A 465 ? 0.7375 0.7917 1.0066 0.0252 -0.1280 -0.0947 506 PHE A CG 3712 C CD1 . PHE A 465 ? 0.7516 0.8022 0.9981 0.0234 -0.1162 -0.0872 506 PHE A CD1 3713 C CD2 . PHE A 465 ? 0.7671 0.8195 1.0514 0.0221 -0.1347 -0.0986 506 PHE A CD2 3714 C CE1 . PHE A 465 ? 0.7470 0.7924 0.9855 0.0189 -0.1113 -0.0834 506 PHE A CE1 3715 C CE2 . PHE A 465 ? 0.7798 0.8265 1.0563 0.0175 -0.1294 -0.0947 506 PHE A CE2 3716 C CZ . PHE A 465 ? 0.7762 0.8195 1.0294 0.0160 -0.1177 -0.0869 506 PHE A CZ 3717 N N . SER A 466 ? 0.6872 0.7682 1.0339 0.0321 -0.1494 -0.1120 507 SER A N 3718 C CA . SER A 466 ? 0.6713 0.7577 1.0306 0.0382 -0.1587 -0.1175 507 SER A CA 3719 C C . SER A 466 ? 0.6587 0.7348 0.9878 0.0488 -0.1702 -0.1202 507 SER A C 3720 O O . SER A 466 ? 0.6692 0.7361 0.9824 0.0517 -0.1784 -0.1228 507 SER A O 3721 C CB . SER A 466 ? 0.6802 0.7737 1.0761 0.0362 -0.1691 -0.1252 507 SER A CB 3722 O OG . SER A 466 ? 0.7057 0.8070 1.1193 0.0407 -0.1752 -0.1296 507 SER A OG 3723 N N . GLY A 467 ? 0.6201 0.6972 0.9402 0.0546 -0.1700 -0.1192 508 GLY A N 3724 C CA . GLY A 467 ? 0.5925 0.6599 0.8847 0.0652 -0.1806 -0.1211 508 GLY A CA 3725 C C . GLY A 467 ? 0.5543 0.6118 0.8100 0.0669 -0.1722 -0.1141 508 GLY A C 3726 O O . GLY A 467 ? 0.5495 0.5974 0.7794 0.0753 -0.1800 -0.1151 508 GLY A O 3727 N N . MET A 468 ? 0.5279 0.5878 0.7817 0.0591 -0.1565 -0.1072 509 MET A N 3728 C CA . MET A 468 ? 0.5093 0.5617 0.7323 0.0596 -0.1469 -0.1001 509 MET A CA 3729 C C . MET A 468 ? 0.4797 0.5375 0.7039 0.0555 -0.1322 -0.0938 509 MET A C 3730 O O . MET A 468 ? 0.4709 0.5383 0.7194 0.0496 -0.1259 -0.0937 509 MET A O 3731 C CB . MET A 468 ? 0.5098 0.5579 0.7256 0.0541 -0.1423 -0.0977 509 MET A CB 3732 C CG . MET A 468 ? 0.5718 0.6161 0.7936 0.0561 -0.1558 -0.1047 509 MET A CG 3733 S SD . MET A 468 ? 0.6977 0.7299 0.8883 0.0579 -0.1549 -0.1021 509 MET A SD 3734 C CE . MET A 468 ? 0.6893 0.7249 0.8809 0.0475 -0.1365 -0.0934 509 MET A CE 3735 N N . PRO A 469 ? 0.4536 0.5051 0.6517 0.0585 -0.1262 -0.0886 510 PRO A N 3736 C CA . PRO A 469 ? 0.4227 0.4787 0.6214 0.0550 -0.1132 -0.0834 510 PRO A CA 3737 C C . PRO A 469 ? 0.3937 0.4502 0.5879 0.0470 -0.1002 -0.0779 510 PRO A C 3738 O O . PRO A 469 ? 0.3901 0.4414 0.5740 0.0451 -0.1007 -0.0768 510 PRO A O 3739 C CB . PRO A 469 ? 0.4254 0.4734 0.5988 0.0623 -0.1141 -0.0807 510 PRO A CB 3740 C CG . PRO A 469 ? 0.4311 0.4691 0.5831 0.0665 -0.1212 -0.0812 510 PRO A CG 3741 C CD . PRO A 469 ? 0.4656 0.5060 0.6348 0.0663 -0.1323 -0.0880 510 PRO A CD 3742 N N . ARG A 470 ? 0.3793 0.4416 0.5801 0.0428 -0.0888 -0.0745 511 ARG A N 3743 C CA . ARG A 470 ? 0.3692 0.4314 0.5628 0.0362 -0.0765 -0.0690 511 ARG A CA 3744 C C . ARG A 470 ? 0.3763 0.4295 0.5408 0.0389 -0.0736 -0.0647 511 ARG A C 3745 O O . ARG A 470 ? 0.3553 0.4053 0.5083 0.0441 -0.0743 -0.0639 511 ARG A O 3746 C CB . ARG A 470 ? 0.3760 0.4466 0.5835 0.0321 -0.0654 -0.0672 511 ARG A CB 3747 C CG . ARG A 470 ? 0.3950 0.4656 0.5938 0.0258 -0.0521 -0.0615 511 ARG A CG 3748 C CD . ARG A 470 ? 0.4811 0.5590 0.6903 0.0236 -0.0418 -0.0604 511 ARG A CD 3749 N NE . ARG A 470 ? 0.5201 0.6075 0.7575 0.0204 -0.0407 -0.0631 511 ARG A NE 3750 C CZ . ARG A 470 ? 0.5631 0.6545 0.8118 0.0137 -0.0336 -0.0610 511 ARG A CZ 3751 N NH1 . ARG A 470 ? 0.5437 0.6299 0.7771 0.0097 -0.0280 -0.0563 511 ARG A NH1 3752 N NH2 . ARG A 470 ? 0.5391 0.6392 0.8149 0.0110 -0.0323 -0.0633 511 ARG A NH2 3753 N N . ILE A 471 ? 0.3724 0.4216 0.5263 0.0352 -0.0700 -0.0617 512 ILE A N 3754 C CA . ILE A 471 ? 0.3803 0.4229 0.5106 0.0357 -0.0646 -0.0570 512 ILE A CA 3755 C C . ILE A 471 ? 0.3865 0.4312 0.5174 0.0283 -0.0542 -0.0529 512 ILE A C 3756 O O . ILE A 471 ? 0.3891 0.4347 0.5280 0.0242 -0.0546 -0.0531 512 ILE A O 3757 C CB . ILE A 471 ? 0.3879 0.4215 0.5005 0.0404 -0.0723 -0.0577 512 ILE A CB 3758 C CG1 . ILE A 471 ? 0.3928 0.4233 0.5027 0.0486 -0.0833 -0.0618 512 ILE A CG1 3759 C CG2 . ILE A 471 ? 0.3657 0.3933 0.4562 0.0402 -0.0654 -0.0524 512 ILE A CG2 3760 C CD1 . ILE A 471 ? 0.4392 0.4605 0.5303 0.0542 -0.0910 -0.0629 512 ILE A CD1 3761 N N . SER A 472 ? 0.3861 0.4309 0.5081 0.0267 -0.0452 -0.0492 513 SER A N 3762 C CA . SER A 472 ? 0.3891 0.4359 0.5110 0.0202 -0.0355 -0.0454 513 SER A CA 3763 C C . SER A 472 ? 0.3909 0.4312 0.4942 0.0193 -0.0336 -0.0419 513 SER A C 3764 O O . SER A 472 ? 0.3686 0.4029 0.4582 0.0238 -0.0383 -0.0419 513 SER A O 3765 C CB . SER A 472 ? 0.3961 0.4475 0.5209 0.0189 -0.0269 -0.0442 513 SER A CB 3766 O OG . SER A 472 ? 0.4209 0.4794 0.5662 0.0191 -0.0282 -0.0476 513 SER A OG 3767 N N A LYS A 473 ? 0.3893 0.4307 0.4926 0.0138 -0.0266 -0.0387 514 LYS A N 3768 N N B LYS A 473 ? 0.3891 0.4305 0.4920 0.0138 -0.0264 -0.0386 514 LYS A N 3769 C CA A LYS A 473 ? 0.3912 0.4273 0.4786 0.0124 -0.0240 -0.0352 514 LYS A CA 3770 C CA B LYS A 473 ? 0.3925 0.4283 0.4795 0.0126 -0.0243 -0.0352 514 LYS A CA 3771 C C A LYS A 473 ? 0.4018 0.4361 0.4761 0.0140 -0.0195 -0.0332 514 LYS A C 3772 C C B LYS A 473 ? 0.3972 0.4317 0.4715 0.0127 -0.0180 -0.0326 514 LYS A C 3773 O O A LYS A 473 ? 0.3904 0.4281 0.4692 0.0144 -0.0160 -0.0340 514 LYS A O 3774 O O B LYS A 473 ? 0.3793 0.4178 0.4577 0.0109 -0.0120 -0.0322 514 LYS A O 3775 C CB A LYS A 473 ? 0.3771 0.4151 0.4693 0.0062 -0.0177 -0.0322 514 LYS A CB 3776 C CB B LYS A 473 ? 0.3923 0.4289 0.4844 0.0069 -0.0208 -0.0328 514 LYS A CB 3777 C CG A LYS A 473 ? 0.3748 0.4151 0.4835 0.0037 -0.0213 -0.0338 514 LYS A CG 3778 C CG B LYS A 473 ? 0.3887 0.4307 0.4890 0.0024 -0.0120 -0.0309 514 LYS A CG 3779 C CD A LYS A 473 ? 0.4090 0.4489 0.5196 -0.0019 -0.0156 -0.0298 514 LYS A CD 3780 C CD B LYS A 473 ? 0.4005 0.4419 0.5033 -0.0027 -0.0082 -0.0275 514 LYS A CD 3781 C CE A LYS A 473 ? 0.4121 0.4575 0.5302 -0.0059 -0.0060 -0.0275 514 LYS A CE 3782 C CE B LYS A 473 ? 0.4023 0.4427 0.5167 -0.0035 -0.0148 -0.0293 514 LYS A CE 3783 N NZ A LYS A 473 ? 0.3687 0.4203 0.5085 -0.0070 -0.0067 -0.0302 514 LYS A NZ 3784 N NZ B LYS A 473 ? 0.3868 0.4332 0.5217 -0.0037 -0.0168 -0.0328 514 LYS A NZ 3785 N N . LEU A 474 ? 0.3967 0.4256 0.4561 0.0148 -0.0194 -0.0309 515 LEU A N 3786 C CA . LEU A 474 ? 0.4112 0.4382 0.4594 0.0150 -0.0144 -0.0287 515 LEU A CA 3787 C C . LEU A 474 ? 0.4272 0.4557 0.4735 0.0099 -0.0076 -0.0261 515 LEU A C 3788 O O . LEU A 474 ? 0.4477 0.4751 0.4930 0.0071 -0.0075 -0.0243 515 LEU A O 3789 C CB . LEU A 474 ? 0.3982 0.4191 0.4326 0.0182 -0.0172 -0.0273 515 LEU A CB 3790 C CG . LEU A 474 ? 0.3907 0.4083 0.4215 0.0243 -0.0232 -0.0291 515 LEU A CG 3791 C CD1 . LEU A 474 ? 0.3896 0.4013 0.4073 0.0269 -0.0251 -0.0274 515 LEU A CD1 3792 C CD2 . LEU A 474 ? 0.3476 0.3653 0.3773 0.0269 -0.0212 -0.0291 515 LEU A CD2 3793 N N . GLY A 475 ? 0.4455 0.4757 0.4898 0.0092 -0.0023 -0.0258 516 GLY A N 3794 C CA . GLY A 475 ? 0.4303 0.4606 0.4689 0.0055 0.0035 -0.0235 516 GLY A CA 3795 C C . GLY A 475 ? 0.4331 0.4600 0.4604 0.0068 0.0046 -0.0228 516 GLY A C 3796 O O . GLY A 475 ? 0.4341 0.4571 0.4540 0.0082 0.0017 -0.0215 516 GLY A O 3797 N N . SER A 476 ? 0.4206 0.4490 0.4470 0.0063 0.0091 -0.0237 517 SER A N 3798 C CA . SER A 476 ? 0.3885 0.4136 0.4065 0.0075 0.0098 -0.0235 517 SER A CA 3799 C C . SER A 476 ? 0.3736 0.4000 0.3953 0.0093 0.0121 -0.0261 517 SER A C 3800 O O . SER A 476 ? 0.3666 0.3959 0.3971 0.0108 0.0115 -0.0278 517 SER A O 3801 C CB . SER A 476 ? 0.4075 0.4313 0.4174 0.0046 0.0123 -0.0220 517 SER A CB 3802 O OG . SER A 476 ? 0.4355 0.4563 0.4392 0.0056 0.0124 -0.0222 517 SER A OG 3803 N N . GLY A 477 ? 0.3445 0.3688 0.3605 0.0091 0.0143 -0.0265 518 GLY A N 3804 C CA . GLY A 477 ? 0.3461 0.3705 0.3652 0.0110 0.0161 -0.0291 518 GLY A CA 3805 C C . GLY A 477 ? 0.3231 0.3436 0.3419 0.0147 0.0128 -0.0286 518 GLY A C 3806 O O . GLY A 477 ? 0.3248 0.3447 0.3473 0.0170 0.0135 -0.0304 518 GLY A O 3807 N N . ASN A 478 ? 0.2997 0.3171 0.3139 0.0157 0.0095 -0.0260 519 ASN A N 3808 C CA . ASN A 478 ? 0.2887 0.3015 0.3006 0.0193 0.0075 -0.0248 519 ASN A CA 3809 C C . ASN A 478 ? 0.2903 0.2996 0.2952 0.0196 0.0060 -0.0217 519 ASN A C 3810 O O . ASN A 478 ? 0.2759 0.2865 0.2783 0.0172 0.0057 -0.0209 519 ASN A O 3811 C CB . ASN A 478 ? 0.3017 0.3146 0.3187 0.0235 0.0043 -0.0257 519 ASN A CB 3812 C CG . ASN A 478 ? 0.3177 0.3265 0.3348 0.0268 0.0047 -0.0256 519 ASN A CG 3813 O OD1 . ASN A 478 ? 0.3290 0.3326 0.3402 0.0282 0.0049 -0.0229 519 ASN A OD1 3814 N ND2 . ASN A 478 ? 0.2932 0.3043 0.3177 0.0279 0.0055 -0.0283 519 ASN A ND2 3815 N N . ASP A 479 ? 0.2759 0.2805 0.2776 0.0228 0.0054 -0.0199 520 ASP A N 3816 C CA . ASP A 479 ? 0.2642 0.2656 0.2600 0.0228 0.0059 -0.0170 520 ASP A CA 3817 C C . ASP A 479 ? 0.2750 0.2760 0.2667 0.0241 0.0030 -0.0155 520 ASP A C 3818 O O . ASP A 479 ? 0.2917 0.2910 0.2792 0.0238 0.0037 -0.0134 520 ASP A O 3819 C CB . ASP A 479 ? 0.2748 0.2710 0.2689 0.0259 0.0072 -0.0147 520 ASP A CB 3820 C CG . ASP A 479 ? 0.2790 0.2744 0.2771 0.0237 0.0104 -0.0158 520 ASP A CG 3821 O OD1 . ASP A 479 ? 0.3038 0.3010 0.3024 0.0200 0.0117 -0.0168 520 ASP A OD1 3822 O OD2 . ASP A 479 ? 0.2911 0.2835 0.2916 0.0261 0.0110 -0.0159 520 ASP A OD2 3823 N N . PHE A 480 ? 0.2839 0.2868 0.2777 0.0255 -0.0002 -0.0170 521 PHE A N 3824 C CA . PHE A 480 ? 0.2866 0.2891 0.2770 0.0263 -0.0034 -0.0165 521 PHE A CA 3825 C C . PHE A 480 ? 0.2804 0.2857 0.2715 0.0218 -0.0024 -0.0165 521 PHE A C 3826 O O . PHE A 480 ? 0.2778 0.2822 0.2660 0.0221 -0.0046 -0.0158 521 PHE A O 3827 C CB . PHE A 480 ? 0.2923 0.2961 0.2866 0.0287 -0.0081 -0.0188 521 PHE A CB 3828 C CG . PHE A 480 ? 0.2872 0.2964 0.2909 0.0252 -0.0074 -0.0212 521 PHE A CG 3829 C CD1 . PHE A 480 ? 0.3197 0.3319 0.3264 0.0214 -0.0072 -0.0215 521 PHE A CD1 3830 C CD2 . PHE A 480 ? 0.2889 0.3000 0.2986 0.0259 -0.0062 -0.0228 521 PHE A CD2 3831 C CE1 . PHE A 480 ? 0.3126 0.3296 0.3277 0.0180 -0.0051 -0.0231 521 PHE A CE1 3832 C CE2 . PHE A 480 ? 0.3173 0.3338 0.3361 0.0227 -0.0042 -0.0250 521 PHE A CE2 3833 C CZ . PHE A 480 ? 0.3183 0.3378 0.3396 0.0188 -0.0033 -0.0249 521 PHE A CZ 3834 N N . GLU A 481 ? 0.2629 0.2712 0.2573 0.0179 0.0005 -0.0173 522 GLU A N 3835 C CA A GLU A 481 ? 0.2636 0.2741 0.2581 0.0140 0.0011 -0.0171 522 GLU A CA 3836 C CA B GLU A 481 ? 0.2707 0.2812 0.2651 0.0139 0.0012 -0.0171 522 GLU A CA 3837 C C . GLU A 481 ? 0.2617 0.2700 0.2508 0.0138 0.0004 -0.0150 522 GLU A C 3838 O O . GLU A 481 ? 0.2689 0.2772 0.2573 0.0130 -0.0016 -0.0145 522 GLU A O 3839 C CB A GLU A 481 ? 0.2640 0.2770 0.2602 0.0107 0.0047 -0.0183 522 GLU A CB 3840 C CB B GLU A 481 ? 0.2781 0.2908 0.2732 0.0104 0.0048 -0.0180 522 GLU A CB 3841 C CG A GLU A 481 ? 0.2828 0.2977 0.2780 0.0071 0.0056 -0.0177 522 GLU A CG 3842 C CG B GLU A 481 ? 0.3190 0.3331 0.3121 0.0069 0.0052 -0.0170 522 GLU A CG 3843 C CD A GLU A 481 ? 0.2742 0.2896 0.2661 0.0047 0.0087 -0.0184 522 GLU A CD 3844 C CD B GLU A 481 ? 0.3831 0.3952 0.3708 0.0060 0.0044 -0.0152 522 GLU A CD 3845 O OE1 A GLU A 481 ? 0.3590 0.3725 0.3475 0.0047 0.0084 -0.0181 522 GLU A OE1 3846 O OE1 B GLU A 481 ? 0.3744 0.3854 0.3605 0.0062 0.0054 -0.0155 522 GLU A OE1 3847 O OE2 A GLU A 481 ? 0.2727 0.2904 0.2658 0.0030 0.0113 -0.0194 522 GLU A OE2 3848 O OE2 B GLU A 481 ? 0.4254 0.4369 0.4113 0.0051 0.0026 -0.0137 522 GLU A OE2 3849 N N . VAL A 482 ? 0.2575 0.2639 0.2439 0.0144 0.0021 -0.0139 523 VAL A N 3850 C CA . VAL A 482 ? 0.2622 0.2674 0.2453 0.0140 0.0018 -0.0121 523 VAL A CA 3851 C C . VAL A 482 ? 0.2754 0.2784 0.2556 0.0174 -0.0006 -0.0112 523 VAL A C 3852 O O . VAL A 482 ? 0.2667 0.2695 0.2453 0.0169 -0.0021 -0.0106 523 VAL A O 3853 C CB . VAL A 482 ? 0.2794 0.2833 0.2626 0.0140 0.0043 -0.0111 523 VAL A CB 3854 C CG1 . VAL A 482 ? 0.2634 0.2640 0.2456 0.0179 0.0057 -0.0097 523 VAL A CG1 3855 C CG2 . VAL A 482 ? 0.2940 0.2980 0.2761 0.0131 0.0040 -0.0097 523 VAL A CG2 3856 N N . PHE A 483 ? 0.2652 0.2660 0.2439 0.0213 -0.0013 -0.0113 524 PHE A N 3857 C CA . PHE A 483 ? 0.2661 0.2639 0.2400 0.0254 -0.0040 -0.0109 524 PHE A CA 3858 C C . PHE A 483 ? 0.2632 0.2621 0.2389 0.0248 -0.0081 -0.0128 524 PHE A C 3859 O O . PHE A 483 ? 0.2898 0.2868 0.2623 0.0263 -0.0101 -0.0127 524 PHE A O 3860 C CB . PHE A 483 ? 0.2734 0.2681 0.2441 0.0302 -0.0045 -0.0107 524 PHE A CB 3861 C CG . PHE A 483 ? 0.2898 0.2825 0.2592 0.0309 0.0000 -0.0082 524 PHE A CG 3862 C CD1 . PHE A 483 ? 0.3578 0.3478 0.3225 0.0330 0.0026 -0.0055 524 PHE A CD1 3863 C CD2 . PHE A 483 ? 0.2743 0.2679 0.2481 0.0292 0.0019 -0.0086 524 PHE A CD2 3864 C CE1 . PHE A 483 ? 0.3658 0.3540 0.3314 0.0330 0.0073 -0.0028 524 PHE A CE1 3865 C CE2 . PHE A 483 ? 0.2703 0.2617 0.2445 0.0293 0.0060 -0.0063 524 PHE A CE2 3866 C CZ . PHE A 483 ? 0.3312 0.3199 0.3018 0.0311 0.0087 -0.0033 524 PHE A CZ 3867 N N . PHE A 484 ? 0.2543 0.2560 0.2360 0.0227 -0.0092 -0.0146 525 PHE A N 3868 C CA . PHE A 484 ? 0.2574 0.2600 0.2432 0.0219 -0.0130 -0.0164 525 PHE A CA 3869 C C . PHE A 484 ? 0.2697 0.2743 0.2583 0.0171 -0.0118 -0.0155 525 PHE A C 3870 O O . PHE A 484 ? 0.2692 0.2722 0.2570 0.0170 -0.0143 -0.0154 525 PHE A O 3871 C CB . PHE A 484 ? 0.2667 0.2719 0.2597 0.0219 -0.0144 -0.0187 525 PHE A CB 3872 C CG . PHE A 484 ? 0.2733 0.2796 0.2728 0.0214 -0.0187 -0.0208 525 PHE A CG 3873 C CD1 . PHE A 484 ? 0.2968 0.2996 0.2929 0.0253 -0.0240 -0.0223 525 PHE A CD1 3874 C CD2 . PHE A 484 ? 0.3477 0.3582 0.3568 0.0171 -0.0173 -0.0214 525 PHE A CD2 3875 C CE1 . PHE A 484 ? 0.3503 0.3537 0.3539 0.0249 -0.0290 -0.0250 525 PHE A CE1 3876 C CE2 . PHE A 484 ? 0.3146 0.3261 0.3321 0.0164 -0.0214 -0.0234 525 PHE A CE2 3877 C CZ . PHE A 484 ? 0.3217 0.3295 0.3368 0.0203 -0.0278 -0.0255 525 PHE A CZ 3878 N N . GLN A 485 ? 0.2542 0.2615 0.2447 0.0135 -0.0081 -0.0148 526 GLN A N 3879 C CA . GLN A 485 ? 0.2673 0.2760 0.2594 0.0092 -0.0067 -0.0136 526 GLN A CA 3880 C C . GLN A 485 ? 0.2674 0.2742 0.2539 0.0086 -0.0065 -0.0117 526 GLN A C 3881 O O . GLN A 485 ? 0.2719 0.2781 0.2583 0.0067 -0.0074 -0.0104 526 GLN A O 3882 C CB A GLN A 485 ? 0.2636 0.2754 0.2579 0.0064 -0.0026 -0.0139 526 GLN A CB 3883 C CB B GLN A 485 ? 0.2731 0.2850 0.2680 0.0062 -0.0029 -0.0139 526 GLN A CB 3884 C CG A GLN A 485 ? 0.2894 0.3040 0.2908 0.0069 -0.0021 -0.0160 526 GLN A CG 3885 C CG B GLN A 485 ? 0.3205 0.3351 0.3236 0.0053 -0.0029 -0.0153 526 GLN A CG 3886 C CD A GLN A 485 ? 0.2645 0.2805 0.2736 0.0056 -0.0040 -0.0165 526 GLN A CD 3887 C CD B GLN A 485 ? 0.3496 0.3655 0.3563 0.0080 -0.0033 -0.0175 526 GLN A CD 3888 O OE1 A GLN A 485 ? 0.2732 0.2876 0.2816 0.0044 -0.0056 -0.0152 526 GLN A OE1 3889 O OE1 B GLN A 485 ? 0.3810 0.3950 0.3831 0.0108 -0.0035 -0.0176 526 GLN A OE1 3890 N NE2 A GLN A 485 ? 0.2825 0.3018 0.3000 0.0058 -0.0037 -0.0185 526 GLN A NE2 3891 N NE2 B GLN A 485 ? 0.3076 0.3266 0.3233 0.0075 -0.0034 -0.0192 526 GLN A NE2 3892 N N . ARG A 486 ? 0.2655 0.2715 0.2484 0.0104 -0.0053 -0.0112 527 ARG A N 3893 C CA . ARG A 486 ? 0.2747 0.2796 0.2544 0.0100 -0.0053 -0.0096 527 ARG A CA 3894 C C . ARG A 486 ? 0.2770 0.2794 0.2546 0.0134 -0.0074 -0.0093 527 ARG A C 3895 O O . ARG A 486 ? 0.2742 0.2756 0.2511 0.0131 -0.0090 -0.0085 527 ARG A O 3896 C CB . ARG A 486 ? 0.2591 0.2649 0.2381 0.0093 -0.0027 -0.0094 527 ARG A CB 3897 C CG . ARG A 486 ? 0.2748 0.2804 0.2525 0.0082 -0.0034 -0.0082 527 ARG A CG 3898 C CD . ARG A 486 ? 0.2717 0.2780 0.2508 0.0083 -0.0016 -0.0082 527 ARG A CD 3899 N NE . ARG A 486 ? 0.2522 0.2597 0.2319 0.0060 -0.0001 -0.0097 527 ARG A NE 3900 C CZ . ARG A 486 ? 0.2989 0.3070 0.2804 0.0050 0.0002 -0.0104 527 ARG A CZ 3901 N NH1 . ARG A 486 ? 0.2700 0.2782 0.2539 0.0056 -0.0005 -0.0095 527 ARG A NH1 3902 N NH2 . ARG A 486 ? 0.2915 0.3002 0.2731 0.0034 0.0011 -0.0125 527 ARG A NH2 3903 N N . LEU A 487 ? 0.2637 0.2646 0.2396 0.0172 -0.0072 -0.0099 528 LEU A N 3904 C CA . LEU A 487 ? 0.2623 0.2605 0.2343 0.0212 -0.0081 -0.0095 528 LEU A CA 3905 C C . LEU A 487 ? 0.2800 0.2757 0.2504 0.0241 -0.0122 -0.0114 528 LEU A C 3906 O O . LEU A 487 ? 0.3019 0.2950 0.2685 0.0274 -0.0134 -0.0116 528 LEU A O 3907 C CB . LEU A 487 ? 0.2602 0.2570 0.2292 0.0244 -0.0050 -0.0084 528 LEU A CB 3908 C CG . LEU A 487 ? 0.2809 0.2797 0.2530 0.0217 -0.0013 -0.0069 528 LEU A CG 3909 C CD1 . LEU A 487 ? 0.2956 0.2925 0.2661 0.0246 0.0023 -0.0053 528 LEU A CD1 3910 C CD2 . LEU A 487 ? 0.3309 0.3308 0.3044 0.0204 -0.0013 -0.0060 528 LEU A CD2 3911 N N . GLY A 488 ? 0.2618 0.2584 0.2358 0.0231 -0.0144 -0.0131 529 GLY A N 3912 C CA . GLY A 488 ? 0.2667 0.2612 0.2414 0.0255 -0.0195 -0.0156 529 GLY A CA 3913 C C . GLY A 488 ? 0.2769 0.2681 0.2449 0.0316 -0.0212 -0.0169 529 GLY A C 3914 O O . GLY A 488 ? 0.2712 0.2591 0.2356 0.0353 -0.0250 -0.0188 529 GLY A O 3915 N N . ILE A 489 ? 0.2718 0.2634 0.2381 0.0329 -0.0185 -0.0158 530 ILE A N 3916 C CA . ILE A 489 ? 0.2715 0.2594 0.2308 0.0390 -0.0203 -0.0166 530 ILE A CA 3917 C C . ILE A 489 ? 0.2817 0.2707 0.2459 0.0395 -0.0245 -0.0193 530 ILE A C 3918 O O . ILE A 489 ? 0.2816 0.2742 0.2528 0.0361 -0.0228 -0.0191 530 ILE A O 3919 C CB . ILE A 489 ? 0.2674 0.2542 0.2221 0.0404 -0.0147 -0.0133 530 ILE A CB 3920 C CG1 . ILE A 489 ? 0.3032 0.2894 0.2549 0.0402 -0.0109 -0.0110 530 ILE A CG1 3921 C CG2 . ILE A 489 ? 0.2926 0.2747 0.2388 0.0470 -0.0160 -0.0132 530 ILE A CG2 3922 C CD1 . ILE A 489 ? 0.3237 0.3104 0.2758 0.0393 -0.0047 -0.0076 530 ILE A CD1 3923 N N . ALA A 490 ? 0.2843 0.2702 0.2452 0.0441 -0.0304 -0.0222 531 ALA A N 3924 C CA . ALA A 490 ? 0.2929 0.2799 0.2596 0.0453 -0.0355 -0.0253 531 ALA A CA 3925 C C . ALA A 490 ? 0.2956 0.2837 0.2627 0.0460 -0.0328 -0.0238 531 ALA A C 3926 O O . ALA A 490 ? 0.3115 0.2957 0.2690 0.0501 -0.0303 -0.0213 531 ALA A O 3927 C CB . ALA A 490 ? 0.3102 0.2920 0.2692 0.0523 -0.0428 -0.0287 531 ALA A CB 3928 N N . SER A 491 ? 0.2801 0.2730 0.2585 0.0424 -0.0328 -0.0250 532 SER A N 3929 C CA . SER A 491 ? 0.2819 0.2759 0.2617 0.0427 -0.0297 -0.0236 532 SER A CA 3930 C C . SER A 491 ? 0.2918 0.2884 0.2807 0.0438 -0.0343 -0.0269 532 SER A C 3931 O O . SER A 491 ? 0.2828 0.2826 0.2812 0.0419 -0.0383 -0.0299 532 SER A O 3932 C CB . SER A 491 ? 0.3046 0.3025 0.2894 0.0365 -0.0229 -0.0215 532 SER A CB 3933 O OG . SER A 491 ? 0.3041 0.2997 0.2815 0.0359 -0.0189 -0.0185 532 SER A OG 3934 N N . GLY A 492 ? 0.2908 0.2864 0.2787 0.0467 -0.0337 -0.0262 533 GLY A N 3935 C CA . GLY A 492 ? 0.3043 0.3030 0.3023 0.0479 -0.0379 -0.0293 533 GLY A CA 3936 C C . GLY A 492 ? 0.3062 0.3053 0.3060 0.0486 -0.0342 -0.0279 533 GLY A C 3937 O O . GLY A 492 ? 0.3104 0.3059 0.3018 0.0492 -0.0293 -0.0244 533 GLY A O 3938 N N . ARG A 493 ? 0.2888 0.2922 0.3003 0.0488 -0.0367 -0.0308 534 ARG A N 3939 C CA . ARG A 493 ? 0.3047 0.3081 0.3189 0.0503 -0.0342 -0.0301 534 ARG A CA 3940 C C . ARG A 493 ? 0.3119 0.3185 0.3373 0.0533 -0.0403 -0.0339 534 ARG A C 3941 O O . ARG A 493 ? 0.3099 0.3207 0.3449 0.0521 -0.0447 -0.0373 534 ARG A O 3942 C CB . ARG A 493 ? 0.3056 0.3135 0.3261 0.0442 -0.0263 -0.0293 534 ARG A CB 3943 C CG . ARG A 493 ? 0.3385 0.3543 0.3731 0.0389 -0.0251 -0.0321 534 ARG A CG 3944 C CD . ARG A 493 ? 0.3512 0.3698 0.3862 0.0328 -0.0168 -0.0306 534 ARG A CD 3945 N NE . ARG A 493 ? 0.3820 0.3999 0.4170 0.0336 -0.0128 -0.0303 534 ARG A NE 3946 C CZ . ARG A 493 ? 0.4055 0.4269 0.4451 0.0299 -0.0071 -0.0311 534 ARG A CZ 3947 N NH1 . ARG A 493 ? 0.3848 0.4045 0.4238 0.0313 -0.0044 -0.0313 534 ARG A NH1 3948 N NH2 . ARG A 493 ? 0.3629 0.3891 0.4071 0.0252 -0.0040 -0.0316 534 ARG A NH2 3949 N N . ALA A 494 ? 0.3132 0.3175 0.3381 0.0575 -0.0409 -0.0334 535 ALA A N 3950 C CA . ALA A 494 ? 0.3238 0.3307 0.3592 0.0613 -0.0474 -0.0371 535 ALA A CA 3951 C C . ALA A 494 ? 0.3156 0.3219 0.3539 0.0630 -0.0442 -0.0361 535 ALA A C 3952 O O . ALA A 494 ? 0.3196 0.3193 0.3462 0.0649 -0.0408 -0.0322 535 ALA A O 3953 C CB . ALA A 494 ? 0.3347 0.3355 0.3604 0.0686 -0.0566 -0.0378 535 ALA A CB 3954 N N . ARG A 495 ? 0.3045 0.3171 0.3589 0.0628 -0.0456 -0.0397 536 ARG A N 3955 C CA . ARG A 495 ? 0.3251 0.3370 0.3835 0.0652 -0.0435 -0.0395 536 ARG A CA 3956 C C . ARG A 495 ? 0.3224 0.3405 0.3981 0.0677 -0.0489 -0.0442 536 ARG A C 3957 O O . ARG A 495 ? 0.3360 0.3600 0.4222 0.0660 -0.0527 -0.0474 536 ARG A O 3958 C CB . ARG A 495 ? 0.3396 0.3543 0.4007 0.0593 -0.0334 -0.0385 536 ARG A CB 3959 C CG . ARG A 495 ? 0.3606 0.3850 0.4371 0.0538 -0.0298 -0.0418 536 ARG A CG 3960 C CD . ARG A 495 ? 0.4346 0.4606 0.5115 0.0493 -0.0205 -0.0412 536 ARG A CD 3961 N NE . ARG A 495 ? 0.4497 0.4698 0.5115 0.0471 -0.0168 -0.0374 536 ARG A NE 3962 C CZ . ARG A 495 ? 0.4730 0.4933 0.5322 0.0430 -0.0098 -0.0367 536 ARG A CZ 3963 N NH1 . ARG A 495 ? 0.4703 0.4959 0.5391 0.0408 -0.0050 -0.0396 536 ARG A NH1 3964 N NH2 . ARG A 495 ? 0.4347 0.4498 0.4818 0.0415 -0.0075 -0.0335 536 ARG A NH2 3965 N N . TYR A 496 ? 0.3114 0.3284 0.3914 0.0717 -0.0494 -0.0446 537 TYR A N 3966 C CA . TYR A 496 ? 0.3213 0.3455 0.4206 0.0736 -0.0531 -0.0493 537 TYR A CA 3967 C C . TYR A 496 ? 0.3220 0.3547 0.4355 0.0674 -0.0441 -0.0512 537 TYR A C 3968 O O . TYR A 496 ? 0.3422 0.3728 0.4492 0.0643 -0.0359 -0.0490 537 TYR A O 3969 C CB . TYR A 496 ? 0.3102 0.3290 0.4081 0.0816 -0.0588 -0.0491 537 TYR A CB 3970 C CG . TYR A 496 ? 0.3460 0.3653 0.4486 0.0874 -0.0708 -0.0522 537 TYR A CG 3971 C CD1 . TYR A 496 ? 0.3741 0.3873 0.4621 0.0903 -0.0774 -0.0510 537 TYR A CD1 3972 C CD2 . TYR A 496 ? 0.3248 0.3514 0.4477 0.0899 -0.0757 -0.0570 537 TYR A CD2 3973 C CE1 . TYR A 496 ? 0.3714 0.3850 0.4636 0.0959 -0.0895 -0.0548 537 TYR A CE1 3974 C CE2 . TYR A 496 ? 0.3512 0.3787 0.4800 0.0953 -0.0879 -0.0607 537 TYR A CE2 3975 C CZ . TYR A 496 ? 0.3792 0.3998 0.4918 0.0983 -0.0950 -0.0596 537 TYR A CZ 3976 O OH . TYR A 496 ? 0.4007 0.4218 0.5184 0.1039 -0.1078 -0.0639 537 TYR A OH 3977 N N . THR A 497 ? 0.3313 0.3735 0.4639 0.0657 -0.0454 -0.0554 538 THR A N 3978 C CA . THR A 497 ? 0.3407 0.3914 0.4862 0.0598 -0.0362 -0.0570 538 THR A CA 3979 C C . THR A 497 ? 0.3424 0.4015 0.5102 0.0619 -0.0375 -0.0615 538 THR A C 3980 O O . THR A 497 ? 0.3389 0.3980 0.5139 0.0676 -0.0467 -0.0638 538 THR A O 3981 C CB . THR A 497 ? 0.3365 0.3916 0.4839 0.0531 -0.0332 -0.0565 538 THR A CB 3982 O OG1 . THR A 497 ? 0.3692 0.4302 0.5233 0.0477 -0.0227 -0.0568 538 THR A OG1 3983 C CG2 . THR A 497 ? 0.3254 0.3867 0.4894 0.0535 -0.0405 -0.0600 538 THR A CG2 3984 N N . LYS A 498 ? 0.3687 0.4350 0.5474 0.0575 -0.0280 -0.0629 539 LYS A N 3985 C CA . LYS A 498 ? 0.4167 0.4929 0.6190 0.0583 -0.0265 -0.0673 539 LYS A CA 3986 C C . LYS A 498 ? 0.4469 0.5320 0.6673 0.0549 -0.0284 -0.0695 539 LYS A C 3987 O O . LYS A 498 ? 0.4346 0.5179 0.6486 0.0518 -0.0307 -0.0678 539 LYS A O 3988 C CB . LYS A 498 ? 0.4124 0.4916 0.6165 0.0555 -0.0145 -0.0677 539 LYS A CB 3989 C CG A LYS A 498 ? 0.4323 0.5161 0.6359 0.0481 -0.0046 -0.0664 539 LYS A CG 3990 C CD A LYS A 498 ? 0.4788 0.5544 0.6591 0.0449 -0.0018 -0.0622 539 LYS A CD 3991 C CE A LYS A 498 ? 0.5164 0.5959 0.6950 0.0382 0.0077 -0.0607 539 LYS A CE 3992 N NZ A LYS A 498 ? 0.5175 0.5948 0.6863 0.0369 0.0167 -0.0606 539 LYS A NZ 3993 N N . ASN A 499 ? 0.5000 0.5947 0.7441 0.0557 -0.0274 -0.0735 540 ASN A N 3994 C CA . ASN A 499 ? 0.5575 0.6621 0.8229 0.0515 -0.0267 -0.0755 540 ASN A CA 3995 C C . ASN A 499 ? 0.5925 0.7013 0.8579 0.0437 -0.0135 -0.0731 540 ASN A C 3996 O O . ASN A 499 ? 0.6195 0.7307 0.8896 0.0389 -0.0132 -0.0720 540 ASN A O 3997 C CB . ASN A 499 ? 0.5631 0.6772 0.8557 0.0550 -0.0293 -0.0805 540 ASN A CB 3998 C CG . ASN A 499 ? 0.5784 0.7014 0.8949 0.0523 -0.0334 -0.0833 540 ASN A CG 3999 O OD1 . ASN A 499 ? 0.6023 0.7268 0.9190 0.0460 -0.0292 -0.0812 540 ASN A OD1 4000 N ND2 . ASN A 499 ? 0.5980 0.7266 0.9355 0.0571 -0.0421 -0.0880 540 ASN A ND2 4001 N N . TRP A 500 ? 0.6319 0.7404 0.8904 0.0428 -0.0032 -0.0722 541 TRP A N 4002 C CA . TRP A 500 ? 0.6631 0.7761 0.9224 0.0370 0.0103 -0.0706 541 TRP A CA 4003 C C . TRP A 500 ? 0.6751 0.7860 0.9236 0.0304 0.0147 -0.0663 541 TRP A C 4004 O O . TRP A 500 ? 0.6749 0.7795 0.9027 0.0285 0.0198 -0.0634 541 TRP A O 4005 C CB . TRP A 500 ? 0.6714 0.7799 0.9163 0.0388 0.0172 -0.0705 541 TRP A CB 4006 C CG . TRP A 500 ? 0.7042 0.8193 0.9566 0.0367 0.0302 -0.0717 541 TRP A CG 4007 C CD1 . TRP A 500 ? 0.7181 0.8416 0.9836 0.0320 0.0389 -0.0711 541 TRP A CD1 4008 C CD2 . TRP A 500 ? 0.7300 0.8432 0.9759 0.0394 0.0365 -0.0736 541 TRP A CD2 4009 N NE1 . TRP A 500 ? 0.7382 0.8652 1.0046 0.0321 0.0505 -0.0725 541 TRP A NE1 4010 C CE2 . TRP A 500 ? 0.7342 0.8550 0.9888 0.0366 0.0489 -0.0745 541 TRP A CE2 4011 C CE3 . TRP A 500 ? 0.7350 0.8405 0.9689 0.0441 0.0330 -0.0747 541 TRP A CE3 4012 C CZ2 . TRP A 500 ? 0.7321 0.8529 0.9828 0.0387 0.0574 -0.0770 541 TRP A CZ2 4013 C CZ3 . TRP A 500 ? 0.7406 0.8460 0.9721 0.0457 0.0411 -0.0773 541 TRP A CZ3 4014 C CH2 . TRP A 500 ? 0.7115 0.8246 0.9509 0.0432 0.0530 -0.0787 541 TRP A CH2 4015 N N . GLU A 501 ? 0.6902 0.8066 0.9542 0.0270 0.0132 -0.0663 542 GLU A N 4016 C CA . GLU A 501 ? 0.7035 0.8170 0.9587 0.0212 0.0153 -0.0622 542 GLU A CA 4017 C C . GLU A 501 ? 0.6984 0.8107 0.9404 0.0167 0.0279 -0.0584 542 GLU A C 4018 O O . GLU A 501 ? 0.7047 0.8097 0.9270 0.0144 0.0278 -0.0549 542 GLU A O 4019 C CB . GLU A 501 ? 0.7133 0.8336 0.9913 0.0180 0.0125 -0.0631 542 GLU A CB 4020 C CG . GLU A 501 ? 0.7571 0.8720 1.0252 0.0139 0.0094 -0.0597 542 GLU A CG 4021 C CD . GLU A 501 ? 0.8226 0.9291 1.0767 0.0179 -0.0037 -0.0606 542 GLU A CD 4022 O OE1 . GLU A 501 ? 0.8645 0.9701 1.1199 0.0239 -0.0116 -0.0639 542 GLU A OE1 4023 O OE2 . GLU A 501 ? 0.8283 0.9288 1.0698 0.0154 -0.0061 -0.0579 542 GLU A OE2 4024 N N . THR A 502 ? 0.6930 0.8122 0.9454 0.0157 0.0386 -0.0593 543 THR A N 4025 C CA . THR A 502 ? 0.6876 0.8054 0.9263 0.0124 0.0510 -0.0562 543 THR A CA 4026 C C . THR A 502 ? 0.6711 0.7803 0.8847 0.0149 0.0512 -0.0559 543 THR A C 4027 O O . THR A 502 ? 0.6768 0.7824 0.8740 0.0123 0.0586 -0.0532 543 THR A O 4028 C CB . THR A 502 ? 0.6971 0.8241 0.9523 0.0117 0.0630 -0.0576 543 THR A CB 4029 O OG1 . THR A 502 ? 0.7122 0.8436 0.9806 0.0171 0.0604 -0.0627 543 THR A OG1 4030 C CG2 . THR A 502 ? 0.6937 0.8284 0.9704 0.0070 0.0671 -0.0558 543 THR A CG2 4031 N N . ASN A 503 ? 0.6388 0.7445 0.8499 0.0199 0.0431 -0.0586 544 ASN A N 4032 C CA . ASN A 503 ? 0.6157 0.7130 0.8054 0.0222 0.0425 -0.0584 544 ASN A CA 4033 C C . ASN A 503 ? 0.5878 0.6762 0.7604 0.0221 0.0340 -0.0556 544 ASN A C 4034 O O . ASN A 503 ? 0.5726 0.6542 0.7309 0.0245 0.0319 -0.0556 544 ASN A O 4035 C CB . ASN A 503 ? 0.6237 0.7214 0.8194 0.0278 0.0406 -0.0626 544 ASN A CB 4036 C CG . ASN A 503 ? 0.6509 0.7504 0.8440 0.0284 0.0511 -0.0647 544 ASN A CG 4037 O OD1 . ASN A 503 ? 0.6738 0.7780 0.8694 0.0252 0.0607 -0.0641 544 ASN A OD1 4038 N ND2 . ASN A 503 ? 0.6700 0.7649 0.8575 0.0327 0.0493 -0.0673 544 ASN A ND2 4039 N N . LYS A 504 ? 0.5552 0.6436 0.7301 0.0196 0.0294 -0.0534 545 LYS A N 4040 C CA . LYS A 504 ? 0.5469 0.6273 0.7079 0.0208 0.0205 -0.0516 545 LYS A CA 4041 C C . LYS A 504 ? 0.5208 0.5937 0.6593 0.0190 0.0231 -0.0484 545 LYS A C 4042 O O . LYS A 504 ? 0.5156 0.5816 0.6417 0.0210 0.0170 -0.0471 545 LYS A O 4043 C CB . LYS A 504 ? 0.5532 0.6350 0.7225 0.0194 0.0137 -0.0509 545 LYS A CB 4044 C CG . LYS A 504 ? 0.5949 0.6776 0.7629 0.0135 0.0186 -0.0477 545 LYS A CG 4045 C CD . LYS A 504 ? 0.6536 0.7373 0.8319 0.0125 0.0110 -0.0479 545 LYS A CD 4046 C CE . LYS A 504 ? 0.7039 0.7854 0.8759 0.0072 0.0145 -0.0439 545 LYS A CE 4047 N NZ . LYS A 504 ? 0.7256 0.8137 0.9102 0.0026 0.0246 -0.0425 545 LYS A NZ 4048 N N . PHE A 505 ? 0.4855 0.5597 0.6188 0.0155 0.0321 -0.0472 546 PHE A N 4049 C CA . PHE A 505 ? 0.4704 0.5380 0.5838 0.0142 0.0344 -0.0451 546 PHE A CA 4050 C C . PHE A 505 ? 0.4721 0.5388 0.5802 0.0160 0.0399 -0.0476 546 PHE A C 4051 O O . PHE A 505 ? 0.4718 0.5335 0.5648 0.0150 0.0420 -0.0467 546 PHE A O 4052 C CB . PHE A 505 ? 0.4661 0.5337 0.5732 0.0092 0.0392 -0.0415 546 PHE A CB 4053 C CG . PHE A 505 ? 0.4640 0.5308 0.5738 0.0073 0.0335 -0.0390 546 PHE A CG 4054 C CD1 . PHE A 505 ? 0.4732 0.5342 0.5745 0.0091 0.0254 -0.0382 546 PHE A CD1 4055 C CD2 . PHE A 505 ? 0.4758 0.5473 0.5970 0.0038 0.0366 -0.0375 546 PHE A CD2 4056 C CE1 . PHE A 505 ? 0.4780 0.5377 0.5810 0.0077 0.0200 -0.0365 546 PHE A CE1 4057 C CE2 . PHE A 505 ? 0.4604 0.5305 0.5847 0.0020 0.0310 -0.0357 546 PHE A CE2 4058 C CZ . PHE A 505 ? 0.4803 0.5445 0.5951 0.0042 0.0224 -0.0355 546 PHE A CZ 4059 N N . SER A 506 ? 0.4554 0.5267 0.5765 0.0189 0.0417 -0.0511 547 SER A N 4060 C CA . SER A 506 ? 0.4620 0.5325 0.5787 0.0207 0.0476 -0.0541 547 SER A CA 4061 C C . SER A 506 ? 0.4556 0.5194 0.5656 0.0245 0.0425 -0.0557 547 SER A C 4062 O O . SER A 506 ? 0.4796 0.5401 0.5812 0.0253 0.0461 -0.0576 547 SER A O 4063 C CB . SER A 506 ? 0.4665 0.5453 0.5997 0.0217 0.0542 -0.0572 547 SER A CB 4064 O OG . SER A 506 ? 0.4722 0.5561 0.6097 0.0176 0.0602 -0.0548 547 SER A OG 4065 N N . GLY A 507 ? 0.4344 0.4958 0.5475 0.0270 0.0341 -0.0547 548 GLY A N 4066 C CA . GLY A 507 ? 0.4249 0.4803 0.5349 0.0313 0.0294 -0.0557 548 GLY A CA 4067 C C . GLY A 507 ? 0.4087 0.4682 0.5340 0.0357 0.0292 -0.0594 548 GLY A C 4068 O O . GLY A 507 ? 0.4289 0.4961 0.5664 0.0351 0.0345 -0.0619 548 GLY A O 4069 N N . TYR A 508 ? 0.3710 0.4253 0.4963 0.0402 0.0231 -0.0596 549 TYR A N 4070 C CA . TYR A 508 ? 0.3436 0.4001 0.4820 0.0451 0.0218 -0.0630 549 TYR A CA 4071 C C . TYR A 508 ? 0.3175 0.3733 0.4544 0.0454 0.0289 -0.0663 549 TYR A C 4072 O O . TYR A 508 ? 0.3325 0.3845 0.4565 0.0424 0.0331 -0.0658 549 TYR A O 4073 C CB . TYR A 508 ? 0.3364 0.3855 0.4713 0.0499 0.0131 -0.0611 549 TYR A CB 4074 C CG . TYR A 508 ? 0.3247 0.3642 0.4423 0.0490 0.0125 -0.0578 549 TYR A CG 4075 C CD1 . TYR A 508 ? 0.3264 0.3597 0.4398 0.0508 0.0145 -0.0588 549 TYR A CD1 4076 C CD2 . TYR A 508 ? 0.3496 0.3861 0.4560 0.0462 0.0099 -0.0537 549 TYR A CD2 4077 C CE1 . TYR A 508 ? 0.3174 0.3420 0.4168 0.0495 0.0143 -0.0556 549 TYR A CE1 4078 C CE2 . TYR A 508 ? 0.3397 0.3683 0.4322 0.0453 0.0099 -0.0507 549 TYR A CE2 4079 C CZ . TYR A 508 ? 0.2963 0.3192 0.3859 0.0467 0.0121 -0.0515 549 TYR A CZ 4080 O OH . TYR A 508 ? 0.3516 0.3671 0.4294 0.0453 0.0122 -0.0484 549 TYR A OH 4081 N N . PRO A 509 ? 0.3002 0.3593 0.4503 0.0494 0.0302 -0.0703 550 PRO A N 4082 C CA . PRO A 509 ? 0.2906 0.3500 0.4392 0.0494 0.0381 -0.0742 550 PRO A CA 4083 C C . PRO A 509 ? 0.2935 0.3430 0.4273 0.0494 0.0381 -0.0742 550 PRO A C 4084 O O . PRO A 509 ? 0.2926 0.3416 0.4189 0.0473 0.0443 -0.0764 550 PRO A O 4085 C CB . PRO A 509 ? 0.2908 0.3548 0.4573 0.0547 0.0380 -0.0785 550 PRO A CB 4086 C CG . PRO A 509 ? 0.2938 0.3657 0.4744 0.0546 0.0342 -0.0773 550 PRO A CG 4087 C CD . PRO A 509 ? 0.3066 0.3718 0.4750 0.0533 0.0261 -0.0722 550 PRO A CD 4088 N N . LEU A 510 ? 0.2724 0.3140 0.4021 0.0520 0.0313 -0.0717 551 LEU A N 4089 C CA . LEU A 510 ? 0.2886 0.3207 0.4074 0.0521 0.0315 -0.0719 551 LEU A CA 4090 C C . LEU A 510 ? 0.2980 0.3251 0.4020 0.0478 0.0303 -0.0677 551 LEU A C 4091 O O . LEU A 510 ? 0.3185 0.3373 0.4145 0.0477 0.0291 -0.0668 551 LEU A O 4092 C CB . LEU A 510 ? 0.2897 0.3149 0.4125 0.0573 0.0260 -0.0712 551 LEU A CB 4093 C CG . LEU A 510 ? 0.3052 0.3350 0.4431 0.0619 0.0277 -0.0763 551 LEU A CG 4094 C CD1 . LEU A 510 ? 0.3204 0.3440 0.4639 0.0678 0.0216 -0.0753 551 LEU A CD1 4095 C CD2 . LEU A 510 ? 0.2791 0.3096 0.4166 0.0612 0.0353 -0.0821 551 LEU A CD2 4096 N N . TYR A 511 ? 0.2724 0.3046 0.3740 0.0443 0.0305 -0.0652 552 TYR A N 4097 C CA . TYR A 511 ? 0.2897 0.3182 0.3781 0.0403 0.0293 -0.0611 552 TYR A CA 4098 C C . TYR A 511 ? 0.2803 0.3044 0.3587 0.0378 0.0328 -0.0629 552 TYR A C 4099 O O . TYR A 511 ? 0.3018 0.3293 0.3798 0.0367 0.0383 -0.0668 552 TYR A O 4100 C CB . TYR A 511 ? 0.2814 0.3171 0.3712 0.0371 0.0305 -0.0596 552 TYR A CB 4101 C CG . TYR A 511 ? 0.3203 0.3541 0.3981 0.0327 0.0304 -0.0562 552 TYR A CG 4102 C CD1 . TYR A 511 ? 0.3020 0.3302 0.3728 0.0327 0.0252 -0.0521 552 TYR A CD1 4103 C CD2 . TYR A 511 ? 0.3263 0.3635 0.3992 0.0290 0.0358 -0.0570 552 TYR A CD2 4104 C CE1 . TYR A 511 ? 0.3182 0.3452 0.3790 0.0289 0.0251 -0.0492 552 TYR A CE1 4105 C CE2 . TYR A 511 ? 0.3297 0.3650 0.3917 0.0252 0.0352 -0.0538 552 TYR A CE2 4106 C CZ . TYR A 511 ? 0.3204 0.3509 0.3773 0.0252 0.0299 -0.0502 552 TYR A CZ 4107 O OH . TYR A 511 ? 0.3480 0.3770 0.3954 0.0218 0.0293 -0.0473 552 TYR A OH 4108 N N . HIS A 512 ? 0.2848 0.3013 0.3557 0.0373 0.0297 -0.0603 553 HIS A N 4109 C CA . HIS A 512 ? 0.2876 0.2992 0.3498 0.0347 0.0314 -0.0618 553 HIS A CA 4110 C C . HIS A 512 ? 0.3125 0.3217 0.3776 0.0367 0.0342 -0.0677 553 HIS A C 4111 O O . HIS A 512 ? 0.3094 0.3160 0.3678 0.0348 0.0361 -0.0708 553 HIS A O 4112 C CB . HIS A 512 ? 0.2791 0.2944 0.3328 0.0303 0.0339 -0.0615 553 HIS A CB 4113 C CG . HIS A 512 ? 0.2803 0.2951 0.3285 0.0279 0.0307 -0.0560 553 HIS A CG 4114 N ND1 . HIS A 512 ? 0.2551 0.2720 0.2954 0.0241 0.0319 -0.0548 553 HIS A ND1 4115 C CD2 . HIS A 512 ? 0.2689 0.2810 0.3177 0.0291 0.0264 -0.0515 553 HIS A CD2 4116 C CE1 . HIS A 512 ? 0.2461 0.2618 0.2833 0.0229 0.0285 -0.0501 553 HIS A CE1 4117 N NE2 . HIS A 512 ? 0.2568 0.2696 0.2985 0.0259 0.0253 -0.0481 553 HIS A NE2 4118 N N . SER A 513 ? 0.3198 0.3291 0.3949 0.0410 0.0338 -0.0694 554 SER A N 4119 C CA . SER A 513 ? 0.3080 0.3144 0.3871 0.0436 0.0360 -0.0751 554 SER A CA 4120 C C . SER A 513 ? 0.3590 0.3558 0.4406 0.0460 0.0320 -0.0735 554 SER A C 4121 O O . SER A 513 ? 0.3175 0.3114 0.3989 0.0467 0.0282 -0.0680 554 SER A O 4122 C CB . SER A 513 ? 0.3067 0.3199 0.3968 0.0470 0.0390 -0.0787 554 SER A CB 4123 O OG A SER A 513 ? 0.2617 0.2744 0.3613 0.0509 0.0348 -0.0764 554 SER A OG 4124 O OG B SER A 513 ? 0.3426 0.3514 0.4389 0.0510 0.0394 -0.0832 554 SER A OG 4125 N N . VAL A 514 ? 0.3247 0.3164 0.4086 0.0477 0.0333 -0.0786 555 VAL A N 4126 C CA . VAL A 514 ? 0.3544 0.3364 0.4420 0.0500 0.0301 -0.0771 555 VAL A CA 4127 C C . VAL A 514 ? 0.3454 0.3273 0.4418 0.0550 0.0274 -0.0743 555 VAL A C 4128 O O . VAL A 514 ? 0.3670 0.3407 0.4652 0.0573 0.0243 -0.0706 555 VAL A O 4129 C CB . VAL A 514 ? 0.3543 0.3313 0.4441 0.0511 0.0319 -0.0842 555 VAL A CB 4130 C CG1 . VAL A 514 ? 0.3640 0.3457 0.4624 0.0556 0.0349 -0.0902 555 VAL A CG1 4131 C CG2 . VAL A 514 ? 0.3461 0.3120 0.4394 0.0522 0.0289 -0.0823 555 VAL A CG2 4132 N N . TYR A 515 ? 0.3264 0.3170 0.4286 0.0569 0.0285 -0.0758 556 TYR A N 4133 C CA . TYR A 515 ? 0.3398 0.3308 0.4519 0.0623 0.0253 -0.0746 556 TYR A CA 4134 C C . TYR A 515 ? 0.3441 0.3348 0.4535 0.0630 0.0203 -0.0676 556 TYR A C 4135 O O . TYR A 515 ? 0.3502 0.3402 0.4664 0.0679 0.0164 -0.0662 556 TYR A O 4136 C CB . TYR A 515 ? 0.3304 0.3311 0.4532 0.0648 0.0284 -0.0799 556 TYR A CB 4137 C CG . TYR A 515 ? 0.3530 0.3535 0.4774 0.0651 0.0336 -0.0871 556 TYR A CG 4138 C CD1 . TYR A 515 ? 0.3416 0.3333 0.4695 0.0684 0.0326 -0.0898 556 TYR A CD1 4139 C CD2 . TYR A 515 ? 0.3262 0.3339 0.4474 0.0622 0.0396 -0.0911 556 TYR A CD2 4140 C CE1 . TYR A 515 ? 0.3474 0.3379 0.4758 0.0690 0.0368 -0.0971 556 TYR A CE1 4141 C CE2 . TYR A 515 ? 0.3375 0.3441 0.4580 0.0632 0.0443 -0.0982 556 TYR A CE2 4142 C CZ . TYR A 515 ? 0.3684 0.3664 0.4925 0.0666 0.0427 -0.1015 556 TYR A CZ 4143 O OH . TYR A 515 ? 0.3964 0.3927 0.5194 0.0678 0.0468 -0.1091 556 TYR A OH 4144 N N . GLU A 516 ? 0.3241 0.3154 0.4236 0.0585 0.0202 -0.0637 557 GLU A N 4145 C CA . GLU A 516 ? 0.3422 0.3317 0.4369 0.0593 0.0155 -0.0572 557 GLU A CA 4146 C C . GLU A 516 ? 0.3372 0.3155 0.4281 0.0618 0.0128 -0.0525 557 GLU A C 4147 O O . GLU A 516 ? 0.3614 0.3344 0.4450 0.0585 0.0142 -0.0499 557 GLU A O 4148 C CB . GLU A 516 ? 0.3571 0.3489 0.4418 0.0538 0.0166 -0.0545 557 GLU A CB 4149 C CG . GLU A 516 ? 0.4232 0.4247 0.5099 0.0517 0.0179 -0.0563 557 GLU A CG 4150 C CD . GLU A 516 ? 0.4003 0.4024 0.4774 0.0480 0.0167 -0.0518 557 GLU A CD 4151 O OE1 . GLU A 516 ? 0.4236 0.4300 0.4968 0.0436 0.0199 -0.0531 557 GLU A OE1 4152 O OE2 . GLU A 516 ? 0.4386 0.4358 0.5113 0.0499 0.0127 -0.0470 557 GLU A OE2 4153 N N . THR A 517 ? 0.3429 0.3175 0.4394 0.0676 0.0093 -0.0515 558 THR A N 4154 C CA . THR A 517 ? 0.3429 0.3056 0.4366 0.0707 0.0074 -0.0468 558 THR A CA 4155 C C . THR A 517 ? 0.3391 0.2988 0.4294 0.0759 0.0018 -0.0412 558 THR A C 4156 O O . THR A 517 ? 0.3224 0.2895 0.4152 0.0775 -0.0014 -0.0424 558 THR A O 4157 C CB . THR A 517 ? 0.3533 0.3119 0.4569 0.0745 0.0080 -0.0510 558 THR A CB 4158 O OG1 . THR A 517 ? 0.3791 0.3444 0.4923 0.0789 0.0056 -0.0544 558 THR A OG1 4159 C CG2 . THR A 517 ? 0.3830 0.3428 0.4891 0.0703 0.0132 -0.0573 558 THR A CG2 4160 N N . TYR A 518 ? 0.3366 0.2849 0.4214 0.0787 0.0005 -0.0354 559 TYR A N 4161 C CA . TYR A 518 ? 0.3543 0.2978 0.4346 0.0851 -0.0051 -0.0301 559 TYR A CA 4162 C C . TYR A 518 ? 0.3589 0.3066 0.4505 0.0908 -0.0096 -0.0344 559 TYR A C 4163 O O . TYR A 518 ? 0.3618 0.3130 0.4528 0.0946 -0.0152 -0.0337 559 TYR A O 4164 C CB . TYR A 518 ? 0.3461 0.2756 0.4205 0.0877 -0.0044 -0.0234 559 TYR A CB 4165 C CG . TYR A 518 ? 0.3892 0.3119 0.4581 0.0954 -0.0102 -0.0180 559 TYR A CG 4166 C CD1 . TYR A 518 ? 0.4116 0.3330 0.4678 0.0971 -0.0129 -0.0127 559 TYR A CD1 4167 C CD2 . TYR A 518 ? 0.4238 0.3409 0.4997 0.1016 -0.0133 -0.0185 559 TYR A CD2 4168 C CE1 . TYR A 518 ? 0.4387 0.3530 0.4877 0.1050 -0.0189 -0.0079 559 TYR A CE1 4169 C CE2 . TYR A 518 ? 0.4689 0.3791 0.5386 0.1095 -0.0195 -0.0134 559 TYR A CE2 4170 C CZ . TYR A 518 ? 0.4684 0.3772 0.5240 0.1111 -0.0223 -0.0081 559 TYR A CZ 4171 O OH . TYR A 518 ? 0.4980 0.3993 0.5453 0.1195 -0.0288 -0.0033 559 TYR A OH 4172 N N . GLU A 519 ? 0.3443 0.2916 0.4466 0.0916 -0.0073 -0.0392 560 GLU A N 4173 C CA . GLU A 519 ? 0.3657 0.3168 0.4804 0.0974 -0.0111 -0.0435 560 GLU A CA 4174 C C . GLU A 519 ? 0.3525 0.3177 0.4746 0.0961 -0.0122 -0.0484 560 GLU A C 4175 O O . GLU A 519 ? 0.3605 0.3293 0.4897 0.1014 -0.0181 -0.0494 560 GLU A O 4176 C CB . GLU A 519 ? 0.3813 0.3298 0.5063 0.0980 -0.0075 -0.0485 560 GLU A CB 4177 C CG . GLU A 519 ? 0.4101 0.3435 0.5316 0.1009 -0.0077 -0.0437 560 GLU A CG 4178 C CD . GLU A 519 ? 0.4737 0.4008 0.5853 0.0950 -0.0032 -0.0397 560 GLU A CD 4179 O OE1 . GLU A 519 ? 0.4274 0.3609 0.5385 0.0887 0.0010 -0.0437 560 GLU A OE1 4180 O OE2 . GLU A 519 ? 0.5022 0.4177 0.6068 0.0968 -0.0039 -0.0325 560 GLU A OE2 4181 N N . LEU A 520 ? 0.3181 0.2909 0.4391 0.0894 -0.0070 -0.0513 561 LEU A N 4182 C CA . LEU A 520 ? 0.3191 0.3047 0.4466 0.0873 -0.0071 -0.0550 561 LEU A CA 4183 C C . LEU A 520 ? 0.3327 0.3192 0.4559 0.0900 -0.0143 -0.0511 561 LEU A C 4184 O O . LEU A 520 ? 0.3317 0.3259 0.4655 0.0928 -0.0185 -0.0540 561 LEU A O 4185 C CB . LEU A 520 ? 0.3135 0.3047 0.4359 0.0796 -0.0008 -0.0565 561 LEU A CB 4186 C CG . LEU A 520 ? 0.3193 0.3228 0.4471 0.0767 -0.0002 -0.0590 561 LEU A CG 4187 C CD1 . LEU A 520 ? 0.3350 0.3477 0.4803 0.0792 0.0009 -0.0651 561 LEU A CD1 4188 C CD2 . LEU A 520 ? 0.3445 0.3507 0.4638 0.0694 0.0057 -0.0592 561 LEU A CD2 4189 N N . VAL A 521 ? 0.3394 0.3184 0.4477 0.0891 -0.0156 -0.0450 562 VAL A N 4190 C CA . VAL A 521 ? 0.3497 0.3287 0.4512 0.0916 -0.0222 -0.0416 562 VAL A CA 4191 C C . VAL A 521 ? 0.3696 0.3433 0.4735 0.1003 -0.0301 -0.0402 562 VAL A C 4192 O O . VAL A 521 ? 0.3714 0.3508 0.4817 0.1038 -0.0367 -0.0423 562 VAL A O 4193 C CB . VAL A 521 ? 0.3481 0.3201 0.4324 0.0888 -0.0206 -0.0355 562 VAL A CB 4194 C CG1 . VAL A 521 ? 0.3529 0.3231 0.4281 0.0929 -0.0280 -0.0320 562 VAL A CG1 4195 C CG2 . VAL A 521 ? 0.3656 0.3440 0.4487 0.0808 -0.0143 -0.0374 562 VAL A CG2 4196 N N . GLU A 522 ? 0.3784 0.3409 0.4777 0.1039 -0.0297 -0.0366 563 GLU A N 4197 C CA . GLU A 522 ? 0.4144 0.3693 0.5123 0.1126 -0.0372 -0.0337 563 GLU A CA 4198 C C . GLU A 522 ? 0.4145 0.3764 0.5306 0.1171 -0.0415 -0.0398 563 GLU A C 4199 O O . GLU A 522 ? 0.4256 0.3871 0.5436 0.1238 -0.0502 -0.0396 563 GLU A O 4200 C CB . GLU A 522 ? 0.4460 0.3869 0.5359 0.1146 -0.0343 -0.0280 563 GLU A CB 4201 C CG . GLU A 522 ? 0.5349 0.4651 0.6179 0.1236 -0.0415 -0.0228 563 GLU A CG 4202 C CD . GLU A 522 ? 0.6202 0.5495 0.7172 0.1296 -0.0451 -0.0262 563 GLU A CD 4203 O OE1 . GLU A 522 ? 0.6221 0.5548 0.7318 0.1267 -0.0399 -0.0311 563 GLU A OE1 4204 O OE2 . GLU A 522 ? 0.6893 0.6144 0.7843 0.1377 -0.0535 -0.0242 563 GLU A OE2 4205 N N . LYS A 523 ? 0.3865 0.3553 0.5163 0.1137 -0.0356 -0.0456 564 LYS A N 4206 C CA . LYS A 523 ? 0.3896 0.3658 0.5384 0.1179 -0.0384 -0.0517 564 LYS A CA 4207 C C . LYS A 523 ? 0.3922 0.3829 0.5528 0.1158 -0.0402 -0.0567 564 LYS A C 4208 O O . LYS A 523 ? 0.4010 0.3969 0.5748 0.1211 -0.0468 -0.0598 564 LYS A O 4209 C CB . LYS A 523 ? 0.3782 0.3556 0.5370 0.1159 -0.0309 -0.0563 564 LYS A CB 4210 C CG . LYS A 523 ? 0.4196 0.3828 0.5719 0.1185 -0.0296 -0.0526 564 LYS A CG 4211 C CD . LYS A 523 ? 0.4530 0.4185 0.6167 0.1167 -0.0226 -0.0589 564 LYS A CD 4212 C CE . LYS A 523 ? 0.5184 0.4698 0.6769 0.1179 -0.0205 -0.0559 564 LYS A CE 4213 N NZ . LYS A 523 ? 0.5892 0.5308 0.7476 0.1262 -0.0276 -0.0516 564 LYS A NZ 4214 N N . PHE A 524 ? 0.3591 0.3566 0.5170 0.1081 -0.0342 -0.0578 565 PHE A N 4215 C CA . PHE A 524 ? 0.3652 0.3771 0.5374 0.1051 -0.0333 -0.0630 565 PHE A CA 4216 C C . PHE A 524 ? 0.3698 0.3855 0.5359 0.1020 -0.0367 -0.0612 565 PHE A C 4217 O O . PHE A 524 ? 0.3859 0.4124 0.5660 0.1012 -0.0388 -0.0650 565 PHE A O 4218 C CB . PHE A 524 ? 0.3541 0.3729 0.5328 0.0990 -0.0226 -0.0672 565 PHE A CB 4219 C CG . PHE A 524 ? 0.3751 0.3914 0.5621 0.1021 -0.0190 -0.0706 565 PHE A CG 4220 C CD1 . PHE A 524 ? 0.3828 0.4029 0.5867 0.1085 -0.0234 -0.0742 565 PHE A CD1 4221 C CD2 . PHE A 524 ? 0.3469 0.3566 0.5253 0.0991 -0.0121 -0.0703 565 PHE A CD2 4222 C CE1 . PHE A 524 ? 0.4327 0.4502 0.6448 0.1119 -0.0203 -0.0776 565 PHE A CE1 4223 C CE2 . PHE A 524 ? 0.3819 0.3885 0.5682 0.1023 -0.0092 -0.0740 565 PHE A CE2 4224 C CZ . PHE A 524 ? 0.4076 0.4178 0.6103 0.1089 -0.0131 -0.0775 565 PHE A CZ 4225 N N . TYR A 525 ? 0.3628 0.3704 0.5098 0.0999 -0.0367 -0.0557 566 TYR A N 4226 C CA . TYR A 525 ? 0.3494 0.3601 0.4899 0.0971 -0.0397 -0.0543 566 TYR A CA 4227 C C . TYR A 525 ? 0.3626 0.3669 0.4943 0.1036 -0.0503 -0.0512 566 TYR A C 4228 O O . TYR A 525 ? 0.3721 0.3822 0.5094 0.1047 -0.0570 -0.0534 566 TYR A O 4229 C CB . TYR A 525 ? 0.3297 0.3376 0.4556 0.0901 -0.0326 -0.0510 566 TYR A CB 4230 C CG . TYR A 525 ? 0.3294 0.3470 0.4640 0.0832 -0.0243 -0.0549 566 TYR A CG 4231 C CD1 . TYR A 525 ? 0.3195 0.3382 0.4603 0.0819 -0.0173 -0.0578 566 TYR A CD1 4232 C CD2 . TYR A 525 ? 0.3428 0.3681 0.4793 0.0783 -0.0236 -0.0558 566 TYR A CD2 4233 C CE1 . TYR A 525 ? 0.3486 0.3756 0.4954 0.0761 -0.0093 -0.0613 566 TYR A CE1 4234 C CE2 . TYR A 525 ? 0.3749 0.4085 0.5185 0.0723 -0.0155 -0.0587 566 TYR A CE2 4235 C CZ . TYR A 525 ? 0.3815 0.4158 0.5293 0.0714 -0.0083 -0.0614 566 TYR A CZ 4236 O OH . TYR A 525 ? 0.3754 0.4172 0.5283 0.0663 -0.0002 -0.0642 566 TYR A OH 4237 N N . ASP A 526 ? 0.3670 0.3586 0.4840 0.1079 -0.0518 -0.0459 567 ASP A N 4238 C CA . ASP A 526 ? 0.3738 0.3576 0.4761 0.1134 -0.0603 -0.0417 567 ASP A CA 4239 C C . ASP A 526 ? 0.3898 0.3610 0.4828 0.1206 -0.0631 -0.0369 567 ASP A C 4240 O O . ASP A 526 ? 0.3980 0.3587 0.4731 0.1211 -0.0609 -0.0306 567 ASP A O 4241 C CB . ASP A 526 ? 0.3606 0.3416 0.4464 0.1086 -0.0568 -0.0378 567 ASP A CB 4242 C CG . ASP A 526 ? 0.3707 0.3465 0.4428 0.1138 -0.0658 -0.0353 567 ASP A CG 4243 O OD1 . ASP A 526 ? 0.3935 0.3692 0.4700 0.1209 -0.0756 -0.0373 567 ASP A OD1 4244 O OD2 . ASP A 526 ? 0.3758 0.3473 0.4326 0.1114 -0.0631 -0.0314 567 ASP A OD2 4245 N N . PRO A 527 ? 0.4126 0.3843 0.5183 0.1264 -0.0676 -0.0396 568 PRO A N 4246 C CA . PRO A 527 ? 0.4305 0.3890 0.5277 0.1330 -0.0693 -0.0346 568 PRO A CA 4247 C C . PRO A 527 ? 0.4561 0.4025 0.5321 0.1396 -0.0759 -0.0279 568 PRO A C 4248 O O . PRO A 527 ? 0.4714 0.4051 0.5345 0.1421 -0.0730 -0.0213 568 PRO A O 4249 C CB . PRO A 527 ? 0.4442 0.4072 0.5606 0.1385 -0.0745 -0.0396 568 PRO A CB 4250 C CG . PRO A 527 ? 0.4440 0.4227 0.5792 0.1347 -0.0751 -0.0471 568 PRO A CG 4251 C CD . PRO A 527 ? 0.4069 0.3912 0.5361 0.1264 -0.0697 -0.0471 568 PRO A CD 4252 N N A MET A 528 ? 0.4487 0.3985 0.5209 0.1423 -0.0843 -0.0295 569 MET A N 4253 N N B MET A 528 ? 0.4544 0.4043 0.5270 0.1423 -0.0843 -0.0297 569 MET A N 4254 C CA A MET A 528 ? 0.4630 0.4014 0.5133 0.1492 -0.0910 -0.0238 569 MET A CA 4255 C CA B MET A 528 ? 0.4742 0.4133 0.5253 0.1492 -0.0914 -0.0242 569 MET A CA 4256 C C A MET A 528 ? 0.4546 0.3907 0.4878 0.1443 -0.0858 -0.0201 569 MET A C 4257 C C B MET A 528 ? 0.4631 0.3982 0.4957 0.1443 -0.0851 -0.0195 569 MET A C 4258 O O A MET A 528 ? 0.4470 0.3746 0.4609 0.1494 -0.0903 -0.0158 569 MET A O 4259 O O B MET A 528 ? 0.4612 0.3857 0.4732 0.1495 -0.0879 -0.0138 569 MET A O 4260 C CB A MET A 528 ? 0.4772 0.4194 0.5324 0.1563 -0.1046 -0.0283 569 MET A CB 4261 C CB B MET A 528 ? 0.4895 0.4341 0.5457 0.1548 -0.1043 -0.0293 569 MET A CB 4262 C CG A MET A 528 ? 0.4965 0.4420 0.5706 0.1618 -0.1107 -0.0325 569 MET A CG 4263 C CG B MET A 528 ? 0.5381 0.4868 0.6134 0.1609 -0.1125 -0.0342 569 MET A CG 4264 S SD A MET A 528 ? 0.5558 0.4850 0.6189 0.1688 -0.1092 -0.0250 569 MET A SD 4265 S SD B MET A 528 ? 0.6362 0.5884 0.7145 0.1693 -0.1299 -0.0393 569 MET A SD 4266 C CE A MET A 528 ? 0.5548 0.4692 0.5887 0.1786 -0.1185 -0.0180 569 MET A CE 4267 C CE B MET A 528 ? 0.5966 0.5695 0.7077 0.1620 -0.1296 -0.0496 569 MET A CE 4268 N N . PHE A 529 ? 0.4269 0.3705 0.4669 0.1347 -0.0764 -0.0219 570 PHE A N 4269 C CA . PHE A 529 ? 0.4255 0.3682 0.4520 0.1292 -0.0709 -0.0190 570 PHE A CA 4270 C C . PHE A 529 ? 0.4230 0.3680 0.4420 0.1315 -0.0787 -0.0208 570 PHE A C 4271 O O . PHE A 529 ? 0.4301 0.3708 0.4331 0.1305 -0.0766 -0.0172 570 PHE A O 4272 C CB . PHE A 529 ? 0.4318 0.3621 0.4420 0.1291 -0.0632 -0.0107 570 PHE A CB 4273 C CG . PHE A 529 ? 0.4284 0.3600 0.4491 0.1229 -0.0539 -0.0109 570 PHE A CG 4274 C CD1 . PHE A 529 ? 0.4522 0.3881 0.4730 0.1143 -0.0454 -0.0111 570 PHE A CD1 4275 C CD2 . PHE A 529 ? 0.4624 0.3919 0.4943 0.1259 -0.0544 -0.0121 570 PHE A CD2 4276 C CE1 . PHE A 529 ? 0.4483 0.3859 0.4790 0.1086 -0.0375 -0.0124 570 PHE A CE1 4277 C CE2 . PHE A 529 ? 0.4616 0.3926 0.5039 0.1202 -0.0460 -0.0136 570 PHE A CE2 4278 C CZ . PHE A 529 ? 0.4317 0.3669 0.4731 0.1116 -0.0380 -0.0140 570 PHE A CZ 4279 N N . LYS A 530 ? 0.4249 0.3772 0.4572 0.1347 -0.0880 -0.0269 571 LYS A N 4280 C CA . LYS A 530 ? 0.4396 0.3944 0.4673 0.1373 -0.0970 -0.0299 571 LYS A CA 4281 C C . LYS A 530 ? 0.3998 0.3647 0.4345 0.1284 -0.0927 -0.0335 571 LYS A C 4282 O O . LYS A 530 ? 0.3951 0.3588 0.4193 0.1290 -0.0965 -0.0337 571 LYS A O 4283 C CB . LYS A 530 ? 0.4468 0.4055 0.4873 0.1441 -0.1096 -0.0355 571 LYS A CB 4284 C CG . LYS A 530 ? 0.4693 0.4422 0.5386 0.1395 -0.1089 -0.0426 571 LYS A CG 4285 C CD . LYS A 530 ? 0.5377 0.5138 0.6194 0.1472 -0.1224 -0.0477 571 LYS A CD 4286 C CE . LYS A 530 ? 0.5443 0.5352 0.6563 0.1427 -0.1210 -0.0547 571 LYS A CE 4287 N NZ . LYS A 530 ? 0.5962 0.5928 0.7239 0.1488 -0.1346 -0.0609 571 LYS A NZ 4288 N N . TYR A 531 ? 0.3838 0.3580 0.4354 0.1206 -0.0849 -0.0363 572 TYR A N 4289 C CA . TYR A 531 ? 0.3714 0.3543 0.4283 0.1123 -0.0802 -0.0388 572 TYR A CA 4290 C C . TYR A 531 ? 0.3694 0.3459 0.4085 0.1084 -0.0721 -0.0332 572 TYR A C 4291 O O . TYR A 531 ? 0.3784 0.3563 0.4110 0.1055 -0.0723 -0.0334 572 TYR A O 4292 C CB . TYR A 531 ? 0.3641 0.3588 0.4434 0.1057 -0.0741 -0.0434 572 TYR A CB 4293 C CG . TYR A 531 ? 0.3826 0.3845 0.4816 0.1096 -0.0820 -0.0491 572 TYR A CG 4294 C CD1 . TYR A 531 ? 0.3934 0.4002 0.4992 0.1115 -0.0916 -0.0533 572 TYR A CD1 4295 C CD2 . TYR A 531 ? 0.4045 0.4083 0.5161 0.1117 -0.0802 -0.0506 572 TYR A CD2 4296 C CE1 . TYR A 531 ? 0.4402 0.4539 0.5657 0.1152 -0.0993 -0.0587 572 TYR A CE1 4297 C CE2 . TYR A 531 ? 0.4198 0.4306 0.5507 0.1156 -0.0875 -0.0559 572 TYR A CE2 4298 C CZ . TYR A 531 ? 0.4456 0.4617 0.5839 0.1171 -0.0969 -0.0599 572 TYR A CZ 4299 O OH . TYR A 531 ? 0.4757 0.4992 0.6354 0.1210 -0.1043 -0.0654 572 TYR A OH 4300 N N . HIS A 532 ? 0.3673 0.3366 0.3992 0.1085 -0.0655 -0.0284 573 HIS A N 4301 C CA . HIS A 532 ? 0.3710 0.3331 0.3860 0.1059 -0.0583 -0.0224 573 HIS A CA 4302 C C . HIS A 532 ? 0.3693 0.3237 0.3653 0.1117 -0.0639 -0.0193 573 HIS A C 4303 O O . HIS A 532 ? 0.3622 0.3163 0.3491 0.1084 -0.0608 -0.0178 573 HIS A O 4304 C CB . HIS A 532 ? 0.3752 0.3290 0.3859 0.1070 -0.0524 -0.0174 573 HIS A CB 4305 C CG . HIS A 532 ? 0.4062 0.3656 0.4302 0.1002 -0.0444 -0.0196 573 HIS A CG 4306 N ND1 . HIS A 532 ? 0.4244 0.3901 0.4655 0.1002 -0.0454 -0.0246 573 HIS A ND1 4307 C CD2 . HIS A 532 ? 0.4285 0.3881 0.4510 0.0934 -0.0356 -0.0180 573 HIS A CD2 4308 C CE1 . HIS A 532 ? 0.4358 0.4050 0.4841 0.0940 -0.0373 -0.0259 573 HIS A CE1 4309 N NE2 . HIS A 532 ? 0.4436 0.4089 0.4807 0.0898 -0.0317 -0.0220 573 HIS A NE2 4310 N N . LEU A 533 ? 0.3890 0.3367 0.3783 0.1206 -0.0721 -0.0183 574 LEU A N 4311 C CA . LEU A 533 ? 0.3992 0.3385 0.3680 0.1271 -0.0774 -0.0154 574 LEU A CA 4312 C C . LEU A 533 ? 0.3982 0.3441 0.3686 0.1255 -0.0832 -0.0207 574 LEU A C 4313 O O . LEU A 533 ? 0.3972 0.3390 0.3523 0.1257 -0.0819 -0.0184 574 LEU A O 4314 C CB . LEU A 533 ? 0.4267 0.3573 0.3873 0.1378 -0.0864 -0.0138 574 LEU A CB 4315 C CG . LEU A 533 ? 0.4545 0.3753 0.3912 0.1459 -0.0927 -0.0110 574 LEU A CG 4316 C CD1 . LEU A 533 ? 0.4638 0.3758 0.3821 0.1446 -0.0822 -0.0029 574 LEU A CD1 4317 C CD2 . LEU A 533 ? 0.4621 0.3748 0.3925 0.1567 -0.1023 -0.0098 574 LEU A CD2 4318 N N . THR A 534 ? 0.3773 0.3332 0.3668 0.1239 -0.0893 -0.0277 575 THR A N 4319 C CA . THR A 534 ? 0.3781 0.3410 0.3728 0.1212 -0.0943 -0.0331 575 THR A CA 4320 C C . THR A 534 ? 0.3579 0.3240 0.3507 0.1127 -0.0849 -0.0316 575 THR A C 4321 O O . THR A 534 ? 0.3723 0.3370 0.3556 0.1126 -0.0869 -0.0321 575 THR A O 4322 C CB . THR A 534 ? 0.3654 0.3397 0.3853 0.1194 -0.1002 -0.0404 575 THR A CB 4323 O OG1 . THR A 534 ? 0.3986 0.3694 0.4191 0.1284 -0.1110 -0.0422 575 THR A OG1 4324 C CG2 . THR A 534 ? 0.3537 0.3355 0.3820 0.1153 -0.1041 -0.0457 575 THR A CG2 4325 N N . VAL A 535 ? 0.3536 0.3238 0.3550 0.1058 -0.0750 -0.0300 576 VAL A N 4326 C CA . VAL A 535 ? 0.3253 0.2984 0.3249 0.0980 -0.0667 -0.0287 576 VAL A CA 4327 C C . VAL A 535 ? 0.3364 0.2999 0.3146 0.1000 -0.0626 -0.0226 576 VAL A C 4328 O O . VAL A 535 ? 0.3601 0.3246 0.3328 0.0967 -0.0604 -0.0224 576 VAL A O 4329 C CB . VAL A 535 ? 0.3204 0.3000 0.3336 0.0906 -0.0577 -0.0290 576 VAL A CB 4330 C CG1 . VAL A 535 ? 0.2994 0.2809 0.3087 0.0830 -0.0492 -0.0270 576 VAL A CG1 4331 C CG2 . VAL A 535 ? 0.3130 0.3034 0.3479 0.0880 -0.0606 -0.0352 576 VAL A CG2 4332 N N . ALA A 536 ? 0.3469 0.3013 0.3140 0.1053 -0.0611 -0.0175 577 ALA A N 4333 C CA . ALA A 536 ? 0.3688 0.3136 0.3156 0.1081 -0.0570 -0.0113 577 ALA A CA 4334 C C . ALA A 536 ? 0.3868 0.3280 0.3198 0.1138 -0.0644 -0.0127 577 ALA A C 4335 O O . ALA A 536 ? 0.3797 0.3181 0.3009 0.1129 -0.0606 -0.0103 577 ALA A O 4336 C CB . ALA A 536 ? 0.3776 0.3124 0.3158 0.1135 -0.0546 -0.0053 577 ALA A CB 4337 N N . GLN A 537 ? 0.3944 0.3357 0.3292 0.1198 -0.0754 -0.0169 578 GLN A N 4338 C CA . GLN A 537 ? 0.3998 0.3384 0.3234 0.1253 -0.0843 -0.0200 578 GLN A CA 4339 C C . GLN A 537 ? 0.4008 0.3474 0.3325 0.1188 -0.0845 -0.0248 578 GLN A C 4340 O O . GLN A 537 ? 0.4086 0.3512 0.3266 0.1213 -0.0862 -0.0249 578 GLN A O 4341 C CB . GLN A 537 ? 0.4255 0.3630 0.3518 0.1331 -0.0972 -0.0244 578 GLN A CB 4342 C CG . GLN A 537 ? 0.4367 0.3640 0.3507 0.1415 -0.0987 -0.0193 578 GLN A CG 4343 C CD . GLN A 537 ? 0.4930 0.4205 0.4131 0.1487 -0.1120 -0.0242 578 GLN A CD 4344 O OE1 . GLN A 537 ? 0.4614 0.3972 0.3962 0.1473 -0.1202 -0.0317 578 GLN A OE1 4345 N NE2 . GLN A 537 ? 0.5027 0.4209 0.4124 0.1566 -0.1143 -0.0198 578 GLN A NE2 4346 N N . VAL A 538 ? 0.3687 0.3259 0.3218 0.1111 -0.0826 -0.0286 579 VAL A N 4347 C CA . VAL A 538 ? 0.3649 0.3292 0.3263 0.1045 -0.0820 -0.0323 579 VAL A CA 4348 C C . VAL A 538 ? 0.3549 0.3173 0.3069 0.0997 -0.0717 -0.0276 579 VAL A C 4349 O O . VAL A 538 ? 0.3649 0.3258 0.3086 0.0995 -0.0724 -0.0282 579 VAL A O 4350 C CB . VAL A 538 ? 0.3442 0.3201 0.3305 0.0973 -0.0811 -0.0367 579 VAL A CB 4351 C CG1 . VAL A 538 ? 0.3416 0.3238 0.3353 0.0901 -0.0791 -0.0392 579 VAL A CG1 4352 C CG2 . VAL A 538 ? 0.3679 0.3471 0.3667 0.1018 -0.0917 -0.0421 579 VAL A CG2 4353 N N . ARG A 539 ? 0.3570 0.3197 0.3114 0.0957 -0.0624 -0.0233 580 ARG A N 4354 C CA . ARG A 539 ? 0.3475 0.3093 0.2956 0.0907 -0.0531 -0.0194 580 ARG A CA 4355 C C . ARG A 539 ? 0.3741 0.3262 0.3011 0.0967 -0.0520 -0.0149 580 ARG A C 4356 O O . ARG A 539 ? 0.3743 0.3258 0.2941 0.0953 -0.0493 -0.0142 580 ARG A O 4357 C CB . ARG A 539 ? 0.3419 0.3054 0.2970 0.0857 -0.0443 -0.0162 580 ARG A CB 4358 C CG . ARG A 539 ? 0.3435 0.3166 0.3179 0.0794 -0.0435 -0.0204 580 ARG A CG 4359 C CD . ARG A 539 ? 0.3580 0.3312 0.3378 0.0760 -0.0360 -0.0179 580 ARG A CD 4360 N NE . ARG A 539 ? 0.3377 0.3200 0.3342 0.0702 -0.0343 -0.0219 580 ARG A NE 4361 C CZ . ARG A 539 ? 0.3473 0.3315 0.3509 0.0668 -0.0285 -0.0217 580 ARG A CZ 4362 N NH1 . ARG A 539 ? 0.3449 0.3224 0.3421 0.0683 -0.0244 -0.0176 580 ARG A NH1 4363 N NH2 . ARG A 539 ? 0.3120 0.3042 0.3290 0.0620 -0.0266 -0.0254 580 ARG A NH2 4364 N N . GLY A 540 ? 0.3788 0.3231 0.2958 0.1035 -0.0531 -0.0113 581 GLY A N 4365 C CA . GLY A 540 ? 0.4151 0.3492 0.3106 0.1103 -0.0513 -0.0063 581 GLY A CA 4366 C C . GLY A 540 ? 0.4150 0.3466 0.2992 0.1157 -0.0592 -0.0099 581 GLY A C 4367 O O . GLY A 540 ? 0.4223 0.3496 0.2925 0.1174 -0.0555 -0.0076 581 GLY A O 4368 N N . GLY A 541 ? 0.4144 0.3487 0.3050 0.1186 -0.0701 -0.0161 582 GLY A N 4369 C CA . GLY A 541 ? 0.4152 0.3477 0.2978 0.1234 -0.0795 -0.0212 582 GLY A CA 4370 C C . GLY A 541 ? 0.4053 0.3428 0.2921 0.1174 -0.0768 -0.0238 582 GLY A C 4371 O O . GLY A 541 ? 0.4169 0.3496 0.2892 0.1218 -0.0793 -0.0249 582 GLY A O 4372 N N . MET A 542 ? 0.3966 0.3435 0.3023 0.1079 -0.0723 -0.0250 583 MET A N 4373 C CA A MET A 542 ? 0.3765 0.3278 0.2866 0.1019 -0.0694 -0.0268 583 MET A CA 4374 C CA B MET A 542 ? 0.3916 0.3431 0.3021 0.1018 -0.0693 -0.0268 583 MET A CA 4375 C C . MET A 542 ? 0.3836 0.3298 0.2791 0.1023 -0.0605 -0.0213 583 MET A C 4376 O O . MET A 542 ? 0.3790 0.3230 0.2659 0.1039 -0.0613 -0.0226 583 MET A O 4377 C CB A MET A 542 ? 0.3547 0.3161 0.2861 0.0922 -0.0655 -0.0283 583 MET A CB 4378 C CB B MET A 542 ? 0.3806 0.3420 0.3121 0.0920 -0.0648 -0.0278 583 MET A CB 4379 C CG A MET A 542 ? 0.3444 0.3119 0.2922 0.0911 -0.0741 -0.0346 583 MET A CG 4380 C CG B MET A 542 ? 0.4394 0.4070 0.3879 0.0910 -0.0724 -0.0333 583 MET A CG 4381 S SD A MET A 542 ? 0.2872 0.2658 0.2583 0.0805 -0.0680 -0.0354 583 MET A SD 4382 S SD B MET A 542 ? 0.5742 0.5455 0.5310 0.0898 -0.0813 -0.0403 583 MET A SD 4383 C CE A MET A 542 ? 0.3141 0.2958 0.2877 0.0743 -0.0656 -0.0365 583 MET A CE 4384 C CE B MET A 542 ? 0.5057 0.4829 0.4709 0.0795 -0.0715 -0.0382 583 MET A CE 4385 N N . VAL A 543 ? 0.3865 0.3309 0.2800 0.1010 -0.0520 -0.0152 584 VAL A N 4386 C CA . VAL A 543 ? 0.3954 0.3358 0.2780 0.1008 -0.0427 -0.0097 584 VAL A CA 4387 C C . VAL A 543 ? 0.4098 0.3406 0.2704 0.1104 -0.0451 -0.0083 584 VAL A C 4388 O O . VAL A 543 ? 0.4059 0.3349 0.2578 0.1111 -0.0414 -0.0074 584 VAL A O 4389 C CB . VAL A 543 ? 0.4024 0.3412 0.2873 0.0987 -0.0342 -0.0036 584 VAL A CB 4390 C CG1 . VAL A 543 ? 0.3997 0.3326 0.2717 0.1004 -0.0249 0.0028 584 VAL A CG1 4391 C CG2 . VAL A 543 ? 0.3786 0.3263 0.2829 0.0893 -0.0305 -0.0049 584 VAL A CG2 4392 N N . PHE A 544 ? 0.4181 0.3428 0.2693 0.1183 -0.0515 -0.0083 585 PHE A N 4393 C CA . PHE A 544 ? 0.4375 0.3521 0.2653 0.1284 -0.0543 -0.0070 585 PHE A CA 4394 C C . PHE A 544 ? 0.4443 0.3598 0.2681 0.1302 -0.0611 -0.0135 585 PHE A C 4395 O O . PHE A 544 ? 0.4648 0.3751 0.2729 0.1343 -0.0575 -0.0119 585 PHE A O 4396 C CB . PHE A 544 ? 0.4608 0.3691 0.2804 0.1368 -0.0624 -0.0072 585 PHE A CB 4397 C CG . PHE A 544 ? 0.4887 0.3853 0.2817 0.1479 -0.0641 -0.0046 585 PHE A CG 4398 C CD1 . PHE A 544 ? 0.5091 0.3973 0.2884 0.1523 -0.0566 0.0037 585 PHE A CD1 4399 C CD2 . PHE A 544 ? 0.5159 0.4095 0.2971 0.1538 -0.0727 -0.0104 585 PHE A CD2 4400 C CE1 . PHE A 544 ? 0.5157 0.3922 0.2682 0.1631 -0.0568 0.0070 585 PHE A CE1 4401 C CE2 . PHE A 544 ? 0.5191 0.4011 0.2731 0.1649 -0.0738 -0.0081 585 PHE A CE2 4402 C CZ . PHE A 544 ? 0.5236 0.3972 0.2629 0.1695 -0.0656 0.0008 585 PHE A CZ 4403 N N . GLU A 545 ? 0.4258 0.3476 0.2641 0.1273 -0.0704 -0.0208 586 GLU A N 4404 C CA . GLU A 545 ? 0.4631 0.3852 0.2992 0.1289 -0.0776 -0.0274 586 GLU A CA 4405 C C . GLU A 545 ? 0.4332 0.3588 0.2726 0.1227 -0.0697 -0.0264 586 GLU A C 4406 O O . GLU A 545 ? 0.4460 0.3675 0.2734 0.1267 -0.0708 -0.0283 586 GLU A O 4407 C CB . GLU A 545 ? 0.4752 0.4041 0.3300 0.1257 -0.0883 -0.0349 586 GLU A CB 4408 C CG . GLU A 545 ? 0.5960 0.5209 0.4463 0.1337 -0.1004 -0.0391 586 GLU A CG 4409 C CD . GLU A 545 ? 0.6795 0.5939 0.5047 0.1446 -0.1067 -0.0413 586 GLU A CD 4410 O OE1 . GLU A 545 ? 0.7384 0.6442 0.5439 0.1523 -0.1047 -0.0365 586 GLU A OE1 4411 O OE2 . GLU A 545 ? 0.7507 0.6649 0.5751 0.1453 -0.1127 -0.0474 586 GLU A OE2 4412 N N . LEU A 546 ? 0.4141 0.3469 0.2689 0.1136 -0.0618 -0.0234 587 LEU A N 4413 C CA . LEU A 546 ? 0.4007 0.3375 0.2607 0.1074 -0.0551 -0.0226 587 LEU A CA 4414 C C . LEU A 546 ? 0.4257 0.3562 0.2685 0.1118 -0.0466 -0.0171 587 LEU A C 4415 O O . LEU A 546 ? 0.4312 0.3612 0.2697 0.1118 -0.0441 -0.0179 587 LEU A O 4416 C CB . LEU A 546 ? 0.4014 0.3466 0.2803 0.0974 -0.0489 -0.0204 587 LEU A CB 4417 C CG . LEU A 546 ? 0.3710 0.3234 0.2684 0.0921 -0.0555 -0.0257 587 LEU A CG 4418 C CD1 . LEU A 546 ? 0.3315 0.2900 0.2428 0.0850 -0.0492 -0.0228 587 LEU A CD1 4419 C CD2 . LEU A 546 ? 0.4035 0.3595 0.3077 0.0879 -0.0575 -0.0295 587 LEU A CD2 4420 N N . ALA A 547 ? 0.4126 0.3378 0.2457 0.1158 -0.0418 -0.0113 588 ALA A N 4421 C CA . ALA A 547 ? 0.4371 0.3568 0.2561 0.1193 -0.0320 -0.0051 588 ALA A CA 4422 C C . ALA A 547 ? 0.4576 0.3677 0.2531 0.1302 -0.0352 -0.0057 588 ALA A C 4423 O O . ALA A 547 ? 0.4822 0.3881 0.2657 0.1333 -0.0269 -0.0014 588 ALA A O 4424 C CB . ALA A 547 ? 0.4216 0.3396 0.2417 0.1180 -0.0238 0.0021 588 ALA A CB 4425 N N . ASN A 548 ? 0.4683 0.3752 0.2579 0.1360 -0.0468 -0.0109 589 ASN A N 4426 C CA . ASN A 548 ? 0.4903 0.3866 0.2546 0.1477 -0.0507 -0.0115 589 ASN A CA 4427 C C . ASN A 548 ? 0.5219 0.4167 0.2809 0.1521 -0.0620 -0.0204 589 ASN A C 4428 O O . ASN A 548 ? 0.5344 0.4208 0.2713 0.1614 -0.0632 -0.0212 589 ASN A O 4429 C CB . ASN A 548 ? 0.4950 0.3847 0.2492 0.1543 -0.0542 -0.0085 589 ASN A CB 4430 C CG A ASN A 548 ? 0.5498 0.4283 0.2779 0.1639 -0.0481 -0.0022 589 ASN A CG 4431 C CG B ASN A 548 ? 0.4814 0.3685 0.2335 0.1530 -0.0420 0.0012 589 ASN A CG 4432 O OD1 A ASN A 548 ? 0.5718 0.4493 0.2962 0.1623 -0.0354 0.0042 589 ASN A OD1 4433 O OD1 B ASN A 548 ? 0.5101 0.4016 0.2775 0.1472 -0.0403 0.0034 589 ASN A OD1 4434 N ND2 A ASN A 548 ? 0.5766 0.4463 0.2862 0.1743 -0.0569 -0.0039 589 ASN A ND2 4435 N ND2 B ASN A 548 ? 0.4559 0.3362 0.1905 0.1579 -0.0327 0.0070 589 ASN A ND2 4436 N N . SER A 549 ? 0.4913 0.3937 0.2697 0.1460 -0.0703 -0.0272 590 SER A N 4437 C CA A SER A 549 ? 0.4961 0.3970 0.2720 0.1497 -0.0818 -0.0361 590 SER A CA 4438 C CA B SER A 549 ? 0.5093 0.4100 0.2845 0.1499 -0.0818 -0.0361 590 SER A CA 4439 C C . SER A 549 ? 0.5062 0.4051 0.2734 0.1507 -0.0765 -0.0367 590 SER A C 4440 O O . SER A 549 ? 0.4862 0.3906 0.2636 0.1433 -0.0667 -0.0331 590 SER A O 4441 C CB A SER A 549 ? 0.4878 0.3980 0.2894 0.1412 -0.0892 -0.0422 590 SER A CB 4442 C CB B SER A 549 ? 0.5054 0.4149 0.3056 0.1421 -0.0899 -0.0424 590 SER A CB 4443 O OG A SER A 549 ? 0.4584 0.3664 0.2590 0.1453 -0.1019 -0.0510 590 SER A OG 4444 O OG B SER A 549 ? 0.5400 0.4522 0.3499 0.1410 -0.0942 -0.0420 590 SER A OG 4445 N N . ILE A 550 ? 0.5043 0.3956 0.2538 0.1598 -0.0834 -0.0418 591 ILE A N 4446 C CA . ILE A 550 ? 0.5183 0.4075 0.2596 0.1615 -0.0787 -0.0431 591 ILE A CA 4447 C C . ILE A 550 ? 0.4823 0.3797 0.2454 0.1522 -0.0802 -0.0474 591 ILE A C 4448 O O . ILE A 550 ? 0.4753 0.3760 0.2431 0.1476 -0.0706 -0.0442 591 ILE A O 4449 C CB . ILE A 550 ? 0.5248 0.4039 0.2430 0.1736 -0.0883 -0.0497 591 ILE A CB 4450 C CG1 . ILE A 550 ? 0.6258 0.4954 0.3190 0.1837 -0.0859 -0.0443 591 ILE A CG1 4451 C CG2 . ILE A 550 ? 0.5786 0.4554 0.2892 0.1758 -0.0847 -0.0524 591 ILE A CG2 4452 C CD1 . ILE A 550 ? 0.6720 0.5401 0.3560 0.1837 -0.0688 -0.0338 591 ILE A CD1 4453 N N . VAL A 551 ? 0.4901 0.3904 0.2667 0.1498 -0.0923 -0.0547 592 VAL A N 4454 C CA . VAL A 551 ? 0.4773 0.3856 0.2772 0.1399 -0.0934 -0.0578 592 VAL A CA 4455 C C . VAL A 551 ? 0.4687 0.3857 0.2887 0.1306 -0.0896 -0.0534 592 VAL A C 4456 O O . VAL A 551 ? 0.4648 0.3823 0.2879 0.1317 -0.0950 -0.0539 592 VAL A O 4457 C CB . VAL A 551 ? 0.4911 0.3980 0.2972 0.1415 -0.1076 -0.0677 592 VAL A CB 4458 C CG1 . VAL A 551 ? 0.4959 0.4109 0.3272 0.1308 -0.1080 -0.0698 592 VAL A CG1 4459 C CG2 . VAL A 551 ? 0.5257 0.4235 0.3105 0.1512 -0.1109 -0.0724 592 VAL A CG2 4460 N N . LEU A 552 ? 0.4592 0.3828 0.2926 0.1217 -0.0810 -0.0495 593 LEU A N 4461 C CA . LEU A 552 ? 0.4379 0.3698 0.2904 0.1127 -0.0773 -0.0459 593 LEU A CA 4462 C C . LEU A 552 ? 0.4378 0.3732 0.3054 0.1104 -0.0881 -0.0517 593 LEU A C 4463 O O . LEU A 552 ? 0.4385 0.3736 0.3121 0.1104 -0.0964 -0.0582 593 LEU A O 4464 C CB . LEU A 552 ? 0.4281 0.3663 0.2931 0.1038 -0.0687 -0.0425 593 LEU A CB 4465 C CG . LEU A 552 ? 0.4562 0.3934 0.3124 0.1040 -0.0568 -0.0356 593 LEU A CG 4466 C CD1 . LEU A 552 ? 0.4408 0.3840 0.3100 0.0959 -0.0511 -0.0339 593 LEU A CD1 4467 C CD2 . LEU A 552 ? 0.4661 0.4041 0.3216 0.1034 -0.0514 -0.0299 593 LEU A CD2 4468 N N . PRO A 553 ? 0.4263 0.3649 0.3009 0.1088 -0.0882 -0.0495 594 PRO A N 4469 C CA . PRO A 553 ? 0.4392 0.3810 0.3276 0.1080 -0.0986 -0.0551 594 PRO A CA 4470 C C . PRO A 553 ? 0.4357 0.3867 0.3490 0.0976 -0.0976 -0.0563 594 PRO A C 4471 O O . PRO A 553 ? 0.4345 0.3913 0.3622 0.0934 -0.0976 -0.0557 594 PRO A O 4472 C CB . PRO A 553 ? 0.4462 0.3872 0.3308 0.1114 -0.0980 -0.0517 594 PRO A CB 4473 C CG . PRO A 553 ? 0.4169 0.3597 0.2994 0.1070 -0.0845 -0.0436 594 PRO A CG 4474 C CD . PRO A 553 ? 0.4246 0.3632 0.2940 0.1088 -0.0794 -0.0423 594 PRO A CD 4475 N N . PHE A 554 ? 0.4173 0.3692 0.3349 0.0936 -0.0961 -0.0575 595 PHE A N 4476 C CA . PHE A 554 ? 0.4025 0.3618 0.3414 0.0839 -0.0943 -0.0578 595 PHE A CA 4477 C C . PHE A 554 ? 0.4201 0.3783 0.3681 0.0841 -0.1045 -0.0651 595 PHE A C 4478 O O . PHE A 554 ? 0.4495 0.4010 0.3851 0.0899 -0.1093 -0.0687 595 PHE A O 4479 C CB . PHE A 554 ? 0.3723 0.3325 0.3091 0.0792 -0.0847 -0.0532 595 PHE A CB 4480 C CG . PHE A 554 ? 0.3682 0.3303 0.3000 0.0773 -0.0742 -0.0461 595 PHE A CG 4481 C CD1 . PHE A 554 ? 0.3557 0.3207 0.2914 0.0765 -0.0723 -0.0439 595 PHE A CD1 4482 C CD2 . PHE A 554 ? 0.3749 0.3362 0.3002 0.0757 -0.0662 -0.0421 595 PHE A CD2 4483 C CE1 . PHE A 554 ? 0.3695 0.3361 0.3021 0.0742 -0.0626 -0.0377 595 PHE A CE1 4484 C CE2 . PHE A 554 ? 0.3974 0.3609 0.3205 0.0733 -0.0566 -0.0359 595 PHE A CE2 4485 C CZ . PHE A 554 ? 0.3582 0.3240 0.2848 0.0724 -0.0550 -0.0338 595 PHE A CZ 4486 N N . ASP A 555 ? 0.3946 0.3590 0.3641 0.0779 -0.1076 -0.0674 596 ASP A N 4487 C CA . ASP A 555 ? 0.3967 0.3604 0.3781 0.0769 -0.1168 -0.0740 596 ASP A CA 4488 C C . ASP A 555 ? 0.3841 0.3526 0.3817 0.0675 -0.1113 -0.0717 596 ASP A C 4489 O O . ASP A 555 ? 0.3782 0.3538 0.3931 0.0607 -0.1079 -0.0696 596 ASP A O 4490 C CB . ASP A 555 ? 0.3951 0.3616 0.3903 0.0782 -0.1266 -0.0795 596 ASP A CB 4491 C CG . ASP A 555 ? 0.4483 0.4122 0.4530 0.0794 -0.1382 -0.0875 596 ASP A CG 4492 O OD1 . ASP A 555 ? 0.4410 0.4022 0.4467 0.0768 -0.1375 -0.0884 596 ASP A OD1 4493 O OD2 . ASP A 555 ? 0.4970 0.4607 0.5076 0.0835 -0.1490 -0.0936 596 ASP A OD2 4494 N N . CYS A 556 ? 0.3711 0.3353 0.3624 0.0672 -0.1098 -0.0716 597 CYS A N 4495 C CA . CYS A 556 ? 0.3773 0.3447 0.3824 0.0588 -0.1050 -0.0690 597 CYS A CA 4496 C C . CYS A 556 ? 0.3639 0.3347 0.3920 0.0536 -0.1107 -0.0727 597 CYS A C 4497 O O . CYS A 556 ? 0.3622 0.3374 0.4036 0.0458 -0.1048 -0.0689 597 CYS A O 4498 C CB . CYS A 556 ? 0.3872 0.3487 0.3822 0.0605 -0.1040 -0.0691 597 CYS A CB 4499 S SG . CYS A 556 ? 0.4669 0.4198 0.4560 0.0685 -0.1175 -0.0787 597 CYS A SG 4500 N N . ARG A 557 ? 0.3582 0.3271 0.3916 0.0578 -0.1219 -0.0799 598 ARG A N 4501 C CA . ARG A 557 ? 0.3670 0.3397 0.4254 0.0526 -0.1276 -0.0838 598 ARG A CA 4502 C C . ARG A 557 ? 0.3662 0.3482 0.4410 0.0464 -0.1215 -0.0799 598 ARG A C 4503 O O . ARG A 557 ? 0.3721 0.3587 0.4687 0.0393 -0.1203 -0.0796 598 ARG A O 4504 C CB . ARG A 557 ? 0.3681 0.3372 0.4289 0.0592 -0.1418 -0.0930 598 ARG A CB 4505 C CG . ARG A 557 ? 0.3861 0.3458 0.4334 0.0648 -0.1484 -0.0979 598 ARG A CG 4506 C CD . ARG A 557 ? 0.3912 0.3460 0.4346 0.0735 -0.1633 -0.1075 598 ARG A CD 4507 N NE . ARG A 557 ? 0.4600 0.4149 0.4880 0.0801 -0.1637 -0.1065 598 ARG A NE 4508 C CZ . ARG A 557 ? 0.5447 0.4961 0.5672 0.0882 -0.1757 -0.1135 598 ARG A CZ 4509 N NH1 . ARG A 557 ? 0.5107 0.4583 0.5416 0.0905 -0.1882 -0.1223 598 ARG A NH1 4510 N NH2 . ARG A 557 ? 0.4994 0.4504 0.5075 0.0943 -0.1756 -0.1117 598 ARG A NH2 4511 N N . ASP A 558 ? 0.3614 0.3458 0.4261 0.0490 -0.1170 -0.0767 599 ASP A N 4512 C CA . ASP A 558 ? 0.3499 0.3427 0.4285 0.0439 -0.1109 -0.0733 599 ASP A CA 4513 C C . ASP A 558 ? 0.3301 0.3263 0.4125 0.0358 -0.0988 -0.0662 599 ASP A C 4514 O O . ASP A 558 ? 0.3259 0.3285 0.4252 0.0297 -0.0942 -0.0642 599 ASP A O 4515 C CB . ASP A 558 ? 0.3450 0.3386 0.4113 0.0492 -0.1094 -0.0717 599 ASP A CB 4516 C CG . ASP A 558 ? 0.4270 0.4191 0.4947 0.0563 -0.1214 -0.0785 599 ASP A CG 4517 O OD1 . ASP A 558 ? 0.5156 0.5106 0.6026 0.0546 -0.1289 -0.0837 599 ASP A OD1 4518 O OD2 . ASP A 558 ? 0.4657 0.4536 0.5158 0.0636 -0.1237 -0.0785 599 ASP A OD2 4519 N N . TYR A 559 ? 0.3241 0.3156 0.3911 0.0361 -0.0942 -0.0627 600 TYR A N 4520 C CA . TYR A 559 ? 0.3169 0.3108 0.3868 0.0291 -0.0844 -0.0566 600 TYR A CA 4521 C C . TYR A 559 ? 0.3221 0.3161 0.4096 0.0236 -0.0864 -0.0577 600 TYR A C 4522 O O . TYR A 559 ? 0.3139 0.3122 0.4126 0.0169 -0.0793 -0.0534 600 TYR A O 4523 C CB . TYR A 559 ? 0.3074 0.2962 0.3582 0.0311 -0.0800 -0.0531 600 TYR A CB 4524 C CG . TYR A 559 ? 0.3116 0.3040 0.3561 0.0280 -0.0695 -0.0466 600 TYR A CG 4525 C CD1 . TYR A 559 ? 0.3224 0.3198 0.3780 0.0210 -0.0628 -0.0428 600 TYR A CD1 4526 C CD2 . TYR A 559 ? 0.3266 0.3169 0.3541 0.0323 -0.0664 -0.0446 600 TYR A CD2 4527 C CE1 . TYR A 559 ? 0.3013 0.3013 0.3502 0.0186 -0.0541 -0.0376 600 TYR A CE1 4528 C CE2 . TYR A 559 ? 0.3274 0.3207 0.3504 0.0294 -0.0576 -0.0393 600 TYR A CE2 4529 C CZ . TYR A 559 ? 0.3192 0.3173 0.3526 0.0227 -0.0520 -0.0362 600 TYR A CZ 4530 O OH . TYR A 559 ? 0.3353 0.3358 0.3634 0.0204 -0.0443 -0.0319 600 TYR A OH 4531 N N . ALA A 560 ? 0.3256 0.3145 0.4152 0.0266 -0.0957 -0.0633 601 ALA A N 4532 C CA . ALA A 560 ? 0.3254 0.3133 0.4324 0.0214 -0.0980 -0.0644 601 ALA A CA 4533 C C . ALA A 560 ? 0.3174 0.3127 0.4485 0.0161 -0.0974 -0.0649 601 ALA A C 4534 O O . ALA A 560 ? 0.3178 0.3154 0.4635 0.0089 -0.0919 -0.0611 601 ALA A O 4535 C CB . ALA A 560 ? 0.3231 0.3038 0.4288 0.0262 -0.1095 -0.0717 601 ALA A CB 4536 N N . VAL A 561 ? 0.3216 0.3204 0.4576 0.0198 -0.1031 -0.0694 602 VAL A N 4537 C CA . VAL A 561 ? 0.3185 0.3253 0.4777 0.0156 -0.1022 -0.0701 602 VAL A CA 4538 C C . VAL A 561 ? 0.3045 0.3175 0.4670 0.0093 -0.0887 -0.0624 602 VAL A C 4539 O O . VAL A 561 ? 0.2991 0.3162 0.4809 0.0027 -0.0842 -0.0602 602 VAL A O 4540 C CB . VAL A 561 ? 0.3241 0.3339 0.4852 0.0216 -0.1103 -0.0758 602 VAL A CB 4541 C CG1 . VAL A 561 ? 0.3675 0.3869 0.5555 0.0169 -0.1084 -0.0764 602 VAL A CG1 4542 C CG2 . VAL A 561 ? 0.3768 0.3803 0.5370 0.0274 -0.1244 -0.0841 602 VAL A CG2 4543 N N . VAL A 562 ? 0.2929 0.3063 0.4371 0.0116 -0.0824 -0.0585 603 VAL A N 4544 C CA . VAL A 562 ? 0.3028 0.3218 0.4491 0.0064 -0.0704 -0.0522 603 VAL A CA 4545 C C . VAL A 562 ? 0.2858 0.3024 0.4304 0.0007 -0.0629 -0.0464 603 VAL A C 4546 O O . VAL A 562 ? 0.2701 0.2912 0.4246 -0.0048 -0.0545 -0.0421 603 VAL A O 4547 C CB . VAL A 562 ? 0.3030 0.3234 0.4329 0.0099 -0.0656 -0.0500 603 VAL A CB 4548 C CG1 . VAL A 562 ? 0.3392 0.3616 0.4712 0.0158 -0.0730 -0.0552 603 VAL A CG1 4549 C CG2 . VAL A 562 ? 0.3505 0.3648 0.4580 0.0124 -0.0635 -0.0471 603 VAL A CG2 4550 N N . LEU A 563 ? 0.2635 0.2728 0.3962 0.0024 -0.0661 -0.0463 604 LEU A N 4551 C CA . LEU A 563 ? 0.2793 0.2856 0.4097 -0.0024 -0.0596 -0.0406 604 LEU A CA 4552 C C . LEU A 563 ? 0.2892 0.2972 0.4422 -0.0085 -0.0589 -0.0400 604 LEU A C 4553 O O . LEU A 563 ? 0.2955 0.3045 0.4519 -0.0140 -0.0501 -0.0338 604 LEU A O 4554 C CB . LEU A 563 ? 0.2733 0.2716 0.3893 0.0009 -0.0641 -0.0414 604 LEU A CB 4555 C CG . LEU A 563 ? 0.2765 0.2732 0.3700 0.0054 -0.0614 -0.0396 604 LEU A CG 4556 C CD1 . LEU A 563 ? 0.3269 0.3160 0.4078 0.0099 -0.0669 -0.0418 604 LEU A CD1 4557 C CD2 . LEU A 563 ? 0.3061 0.3049 0.3922 0.0016 -0.0510 -0.0326 604 LEU A CD2 4558 N N . ARG A 564 ? 0.2896 0.2978 0.4584 -0.0075 -0.0678 -0.0462 605 ARG A N 4559 C CA . ARG A 564 ? 0.2992 0.3095 0.4930 -0.0137 -0.0669 -0.0457 605 ARG A CA 4560 C C . ARG A 564 ? 0.2876 0.3067 0.4952 -0.0182 -0.0579 -0.0423 605 ARG A C 4561 O O . ARG A 564 ? 0.2838 0.3042 0.5028 -0.0244 -0.0501 -0.0370 605 ARG A O 4562 C CB . ARG A 564 ? 0.3072 0.3160 0.5168 -0.0116 -0.0796 -0.0540 605 ARG A CB 4563 C CG . ARG A 564 ? 0.3607 0.3722 0.5999 -0.0183 -0.0791 -0.0540 605 ARG A CG 4564 C CD . ARG A 564 ? 0.4181 0.4241 0.6580 -0.0240 -0.0723 -0.0471 605 ARG A CD 4565 N NE . ARG A 564 ? 0.4746 0.4833 0.7436 -0.0305 -0.0709 -0.0465 605 ARG A NE 4566 C CZ . ARG A 564 ? 0.5399 0.5446 0.8261 -0.0314 -0.0803 -0.0518 605 ARG A CZ 4567 N NH1 . ARG A 564 ? 0.5213 0.5189 0.7971 -0.0257 -0.0920 -0.0585 605 ARG A NH1 4568 N NH2 . ARG A 564 ? 0.5358 0.5438 0.8505 -0.0379 -0.0777 -0.0507 605 ARG A NH2 4569 N N A LYS A 565 ? 0.2821 0.3071 0.4895 -0.0147 -0.0592 -0.0454 606 LYS A N 4570 N N B LYS A 565 ? 0.2770 0.3018 0.4837 -0.0146 -0.0591 -0.0453 606 LYS A N 4571 C CA A LYS A 565 ? 0.2832 0.3166 0.5009 -0.0177 -0.0503 -0.0427 606 LYS A CA 4572 C CA B LYS A 565 ? 0.2695 0.3030 0.4869 -0.0176 -0.0504 -0.0427 606 LYS A CA 4573 C C A LYS A 565 ? 0.2756 0.3088 0.4806 -0.0214 -0.0374 -0.0344 606 LYS A C 4574 C C B LYS A 565 ? 0.2667 0.3002 0.4715 -0.0212 -0.0374 -0.0345 606 LYS A C 4575 O O A LYS A 565 ? 0.2760 0.3131 0.4933 -0.0268 -0.0284 -0.0299 606 LYS A O 4576 O O B LYS A 565 ? 0.2665 0.3044 0.4836 -0.0264 -0.0283 -0.0303 606 LYS A O 4577 C CB A LYS A 565 ? 0.2909 0.3284 0.5027 -0.0119 -0.0541 -0.0469 606 LYS A CB 4578 C CB B LYS A 565 ? 0.2723 0.3099 0.4842 -0.0118 -0.0542 -0.0471 606 LYS A CB 4579 C CG A LYS A 565 ? 0.3178 0.3645 0.5422 -0.0139 -0.0465 -0.0457 606 LYS A CG 4580 C CG B LYS A 565 ? 0.2610 0.2978 0.4808 -0.0068 -0.0680 -0.0553 606 LYS A CG 4581 C CD A LYS A 565 ? 0.3622 0.4119 0.5825 -0.0074 -0.0524 -0.0507 606 LYS A CD 4582 C CD B LYS A 565 ? 0.3252 0.3707 0.5697 -0.0076 -0.0699 -0.0591 606 LYS A CD 4583 C CE A LYS A 565 ? 0.3787 0.4237 0.5707 -0.0031 -0.0504 -0.0484 606 LYS A CE 4584 C CE B LYS A 565 ? 0.2830 0.3275 0.5371 -0.0026 -0.0849 -0.0679 606 LYS A CE 4585 N NZ A LYS A 565 ? 0.3922 0.4398 0.5791 0.0024 -0.0533 -0.0514 606 LYS A NZ 4586 N NZ B LYS A 565 ? 0.3414 0.3943 0.6275 -0.0064 -0.0856 -0.0706 606 LYS A NZ 4587 N N . TYR A 566 ? 0.2523 0.2805 0.4328 -0.0182 -0.0368 -0.0324 607 TYR A N 4588 C CA . TYR A 566 ? 0.2586 0.2863 0.4249 -0.0206 -0.0260 -0.0254 607 TYR A CA 4589 C C . TYR A 566 ? 0.2529 0.2763 0.4230 -0.0259 -0.0216 -0.0200 607 TYR A C 4590 O O . TYR A 566 ? 0.2612 0.2863 0.4307 -0.0297 -0.0116 -0.0142 607 TYR A O 4591 C CB . TYR A 566 ? 0.2488 0.2721 0.3905 -0.0162 -0.0273 -0.0249 607 TYR A CB 4592 C CG . TYR A 566 ? 0.2572 0.2833 0.3919 -0.0108 -0.0306 -0.0290 607 TYR A CG 4593 C CD1 . TYR A 566 ? 0.2700 0.3031 0.4178 -0.0106 -0.0296 -0.0315 607 TYR A CD1 4594 C CD2 . TYR A 566 ? 0.2883 0.3098 0.4043 -0.0058 -0.0344 -0.0301 607 TYR A CD2 4595 C CE1 . TYR A 566 ? 0.2821 0.3169 0.4233 -0.0053 -0.0331 -0.0350 607 TYR A CE1 4596 C CE2 . TYR A 566 ? 0.2855 0.3087 0.3948 -0.0008 -0.0370 -0.0331 607 TYR A CE2 4597 C CZ . TYR A 566 ? 0.2985 0.3278 0.4202 -0.0006 -0.0366 -0.0355 607 TYR A CZ 4598 O OH . TYR A 566 ? 0.3272 0.3573 0.4420 0.0044 -0.0393 -0.0380 607 TYR A OH 4599 N N . ALA A 567 ? 0.2520 0.2695 0.4259 -0.0257 -0.0291 -0.0220 608 ALA A N 4600 C CA . ALA A 567 ? 0.2710 0.2837 0.4502 -0.0306 -0.0255 -0.0169 608 ALA A CA 4601 C C . ALA A 567 ? 0.2769 0.2944 0.4800 -0.0365 -0.0197 -0.0146 608 ALA A C 4602 O O . ALA A 567 ? 0.2715 0.2877 0.4754 -0.0412 -0.0102 -0.0073 608 ALA A O 4603 C CB . ALA A 567 ? 0.2822 0.2875 0.4624 -0.0289 -0.0353 -0.0204 608 ALA A CB 4604 N N . ASP A 568 ? 0.2768 0.2993 0.5003 -0.0362 -0.0254 -0.0206 609 ASP A N 4605 C CA . ASP A 568 ? 0.2972 0.3258 0.5464 -0.0417 -0.0194 -0.0189 609 ASP A CA 4606 C C . ASP A 568 ? 0.2892 0.3238 0.5335 -0.0437 -0.0060 -0.0131 609 ASP A C 4607 O O . ASP A 568 ? 0.2758 0.3120 0.5313 -0.0490 0.0038 -0.0073 609 ASP A O 4608 C CB . ASP A 568 ? 0.2884 0.3235 0.5586 -0.0400 -0.0277 -0.0270 609 ASP A CB 4609 C CG . ASP A 568 ? 0.3661 0.3963 0.6471 -0.0386 -0.0409 -0.0335 609 ASP A CG 4610 O OD1 . ASP A 568 ? 0.4207 0.4435 0.7015 -0.0409 -0.0425 -0.0314 609 ASP A OD1 4611 O OD2 . ASP A 568 ? 0.4446 0.4786 0.7353 -0.0350 -0.0504 -0.0413 609 ASP A OD2 4612 N N . LYS A 569 ? 0.2647 0.3021 0.4930 -0.0392 -0.0057 -0.0151 610 LYS A N 4613 C CA . LYS A 569 ? 0.2807 0.3238 0.5044 -0.0401 0.0055 -0.0113 610 LYS A CA 4614 C C . LYS A 569 ? 0.2772 0.3154 0.4843 -0.0428 0.0155 -0.0029 610 LYS A C 4615 O O . LYS A 569 ? 0.2897 0.3310 0.5028 -0.0467 0.0268 0.0023 610 LYS A O 4616 C CB . LYS A 569 ? 0.2776 0.3236 0.4870 -0.0344 0.0024 -0.0156 610 LYS A CB 4617 C CG . LYS A 569 ? 0.3434 0.3953 0.5500 -0.0349 0.0133 -0.0130 610 LYS A CG 4618 C CD . LYS A 569 ? 0.4287 0.4812 0.6186 -0.0294 0.0100 -0.0164 610 LYS A CD 4619 C CE . LYS A 569 ? 0.5125 0.5725 0.7062 -0.0288 0.0177 -0.0169 610 LYS A CE 4620 N NZ . LYS A 569 ? 0.5238 0.5817 0.6953 -0.0243 0.0168 -0.0179 610 LYS A NZ 4621 N N . ILE A 570 ? 0.2825 0.3131 0.4693 -0.0407 0.0116 -0.0016 611 ILE A N 4622 C CA . ILE A 570 ? 0.2815 0.3069 0.4509 -0.0424 0.0193 0.0058 611 ILE A CA 4623 C C . ILE A 570 ? 0.2897 0.3111 0.4713 -0.0479 0.0240 0.0118 611 ILE A C 4624 O O . ILE A 570 ? 0.2811 0.3014 0.4575 -0.0507 0.0346 0.0189 611 ILE A O 4625 C CB . ILE A 570 ? 0.2880 0.3068 0.4344 -0.0384 0.0134 0.0054 611 ILE A CB 4626 C CG1 . ILE A 570 ? 0.3139 0.3288 0.4416 -0.0394 0.0214 0.0124 611 ILE A CG1 4627 C CG2 . ILE A 570 ? 0.3035 0.3158 0.4537 -0.0378 0.0036 0.0031 611 ILE A CG2 4628 C CD1 . ILE A 570 ? 0.2880 0.3083 0.4059 -0.0380 0.0285 0.0125 611 ILE A CD1 4629 N N . TYR A 571 ? 0.2730 0.2920 0.4710 -0.0491 0.0163 0.0089 612 TYR A N 4630 C CA . TYR A 571 ? 0.3113 0.3268 0.5256 -0.0547 0.0203 0.0140 612 TYR A CA 4631 C C . TYR A 571 ? 0.3069 0.3299 0.5385 -0.0590 0.0319 0.0175 612 TYR A C 4632 O O . TYR A 571 ? 0.3096 0.3299 0.5423 -0.0632 0.0422 0.0257 612 TYR A O 4633 C CB . TYR A 571 ? 0.3144 0.3270 0.5462 -0.0550 0.0088 0.0083 612 TYR A CB 4634 C CG . TYR A 571 ? 0.3646 0.3753 0.6193 -0.0612 0.0128 0.0125 612 TYR A CG 4635 C CD1 . TYR A 571 ? 0.3986 0.3997 0.6478 -0.0638 0.0153 0.0193 612 TYR A CD1 4636 C CD2 . TYR A 571 ? 0.4309 0.4492 0.7136 -0.0645 0.0145 0.0100 612 TYR A CD2 4637 C CE1 . TYR A 571 ? 0.4730 0.4716 0.7450 -0.0699 0.0195 0.0238 612 TYR A CE1 4638 C CE2 . TYR A 571 ? 0.4908 0.5076 0.7975 -0.0707 0.0189 0.0142 612 TYR A CE2 4639 C CZ . TYR A 571 ? 0.5120 0.5187 0.8127 -0.0735 0.0217 0.0213 612 TYR A CZ 4640 O OH . TYR A 571 ? 0.6201 0.6250 0.9454 -0.0798 0.0264 0.0258 612 TYR A OH 4641 N N . SER A 572 ? 0.3183 0.3505 0.5635 -0.0578 0.0305 0.0115 613 SER A N 4642 C CA . SER A 572 ? 0.3255 0.3658 0.5891 -0.0614 0.0415 0.0141 613 SER A CA 4643 C C . SER A 572 ? 0.3288 0.3698 0.5741 -0.0615 0.0550 0.0209 613 SER A C 4644 O O . SER A 572 ? 0.3477 0.3910 0.6033 -0.0655 0.0666 0.0266 613 SER A O 4645 C CB . SER A 572 ? 0.3251 0.3754 0.6071 -0.0594 0.0367 0.0059 613 SER A CB 4646 O OG A SER A 572 ? 0.3406 0.3907 0.6435 -0.0600 0.0252 0.0000 613 SER A OG 4647 O OG B SER A 572 ? 0.3382 0.3908 0.6014 -0.0539 0.0340 0.0021 613 SER A OG 4648 N N . ILE A 573 ? 0.3240 0.3630 0.5429 -0.0569 0.0533 0.0198 614 ILE A N 4649 C CA . ILE A 573 ? 0.3259 0.3644 0.5249 -0.0563 0.0645 0.0254 614 ILE A CA 4650 C C . ILE A 573 ? 0.3502 0.3801 0.5393 -0.0594 0.0710 0.0345 614 ILE A C 4651 O O . ILE A 573 ? 0.3434 0.3739 0.5308 -0.0617 0.0835 0.0410 614 ILE A O 4652 C CB . ILE A 573 ? 0.3295 0.3670 0.5039 -0.0508 0.0596 0.0216 614 ILE A CB 4653 C CG1 . ILE A 573 ? 0.3223 0.3684 0.5062 -0.0477 0.0558 0.0138 614 ILE A CG1 4654 C CG2 . ILE A 573 ? 0.3375 0.3723 0.4883 -0.0500 0.0697 0.0274 614 ILE A CG2 4655 C CD1 . ILE A 573 ? 0.3126 0.3570 0.4754 -0.0422 0.0482 0.0092 614 ILE A CD1 4656 N N . SER A 574 ? 0.3277 0.3494 0.5107 -0.0592 0.0626 0.0352 615 SER A N 4657 C CA . SER A 574 ? 0.3469 0.3595 0.5212 -0.0617 0.0672 0.0437 615 SER A CA 4658 C C . SER A 574 ? 0.3571 0.3700 0.5538 -0.0675 0.0756 0.0494 615 SER A C 4659 O O . SER A 574 ? 0.3524 0.3607 0.5411 -0.0697 0.0862 0.0583 615 SER A O 4660 C CB . SER A 574 ? 0.3475 0.3520 0.5155 -0.0602 0.0553 0.0419 615 SER A CB 4661 O OG . SER A 574 ? 0.3558 0.3508 0.5104 -0.0614 0.0589 0.0501 615 SER A OG 4662 N N . MET A 575 ? 0.3492 0.3674 0.5740 -0.0698 0.0710 0.0443 616 MET A N 4663 C CA . MET A 575 ? 0.3890 0.4084 0.6406 -0.0759 0.0785 0.0490 616 MET A CA 4664 C C . MET A 575 ? 0.3991 0.4259 0.6580 -0.0782 0.0940 0.0534 616 MET A C 4665 O O . MET A 575 ? 0.3999 0.4283 0.6812 -0.0833 0.1022 0.0582 616 MET A O 4666 C CB . MET A 575 ? 0.3797 0.4024 0.6603 -0.0776 0.0678 0.0414 616 MET A CB 4667 C CG . MET A 575 ? 0.4398 0.4523 0.7184 -0.0777 0.0568 0.0407 616 MET A CG 4668 S SD . MET A 575 ? 0.5597 0.5614 0.8429 -0.0837 0.0657 0.0529 616 MET A SD 4669 C CE . MET A 575 ? 0.5215 0.5310 0.8443 -0.0906 0.0747 0.0547 616 MET A CE 4670 N N . LYS A 576 ? 0.4104 0.4416 0.6509 -0.0742 0.0983 0.0520 617 LYS A N 4671 C CA . LYS A 576 ? 0.4214 0.4571 0.6613 -0.0756 0.1147 0.0578 617 LYS A CA 4672 C C . LYS A 576 ? 0.4228 0.4486 0.6445 -0.0773 0.1249 0.0692 617 LYS A C 4673 O O . LYS A 576 ? 0.4289 0.4568 0.6510 -0.0790 0.1395 0.0755 617 LYS A O 4674 C CB . LYS A 576 ? 0.4418 0.4836 0.6647 -0.0705 0.1167 0.0531 617 LYS A CB 4675 C CG . LYS A 576 ? 0.4918 0.5435 0.7303 -0.0680 0.1081 0.0425 617 LYS A CG 4676 C CD . LYS A 576 ? 0.5828 0.6405 0.8066 -0.0635 0.1133 0.0393 617 LYS A CD 4677 C CE . LYS A 576 ? 0.6032 0.6570 0.7998 -0.0580 0.1037 0.0346 617 LYS A CE 4678 N NZ . LYS A 576 ? 0.6313 0.6738 0.8025 -0.0574 0.1013 0.0399 617 LYS A NZ 4679 N N . HIS A 577 ? 0.3849 0.4000 0.5912 -0.0766 0.1173 0.0718 618 HIS A N 4680 C CA . HIS A 577 ? 0.3874 0.3916 0.5738 -0.0774 0.1248 0.0826 618 HIS A CA 4681 C C . HIS A 577 ? 0.3873 0.3824 0.5854 -0.0812 0.1199 0.0868 618 HIS A C 4682 O O . HIS A 577 ? 0.3717 0.3572 0.5511 -0.0791 0.1127 0.0888 618 HIS A O 4683 C CB . HIS A 577 ? 0.3875 0.3860 0.5388 -0.0718 0.1197 0.0819 618 HIS A CB 4684 C CG . HIS A 577 ? 0.4093 0.4157 0.5486 -0.0674 0.1205 0.0756 618 HIS A CG 4685 N ND1 . HIS A 577 ? 0.4669 0.4752 0.5925 -0.0661 0.1331 0.0794 618 HIS A ND1 4686 C CD2 . HIS A 577 ? 0.4460 0.4581 0.5846 -0.0639 0.1104 0.0658 618 HIS A CD2 4687 C CE1 . HIS A 577 ? 0.4811 0.4961 0.5993 -0.0621 0.1304 0.0718 618 HIS A CE1 4688 N NE2 . HIS A 577 ? 0.4745 0.4919 0.6006 -0.0609 0.1168 0.0638 618 HIS A NE2 4689 N N . PRO A 578 ? 0.3891 0.3873 0.6191 -0.0868 0.1235 0.0882 619 PRO A N 4690 C CA . PRO A 578 ? 0.3918 0.3819 0.6364 -0.0903 0.1169 0.0903 619 PRO A CA 4691 C C . PRO A 578 ? 0.4148 0.3917 0.6425 -0.0915 0.1233 0.1021 619 PRO A C 4692 O O . PRO A 578 ? 0.4121 0.3796 0.6359 -0.0912 0.1136 0.1025 619 PRO A O 4693 C CB . PRO A 578 ? 0.4034 0.4005 0.6867 -0.0962 0.1214 0.0896 619 PRO A CB 4694 C CG . PRO A 578 ? 0.4085 0.4148 0.6931 -0.0966 0.1372 0.0928 619 PRO A CG 4695 C CD . PRO A 578 ? 0.3889 0.3983 0.6443 -0.0898 0.1330 0.0870 619 PRO A CD 4696 N N . GLN A 579 ? 0.4160 0.3916 0.6326 -0.0923 0.1389 0.1116 620 GLN A N 4697 C CA . GLN A 579 ? 0.4428 0.4051 0.6404 -0.0926 0.1449 0.1233 620 GLN A CA 4698 C C . GLN A 579 ? 0.4287 0.3830 0.5938 -0.0868 0.1346 0.1221 620 GLN A C 4699 O O . GLN A 579 ? 0.4267 0.3698 0.5861 -0.0872 0.1299 0.1269 620 GLN A O 4700 C CB . GLN A 579 ? 0.4819 0.4437 0.6712 -0.0939 0.1642 0.1341 620 GLN A CB 4701 C CG . GLN A 579 ? 0.5776 0.5248 0.7538 -0.0954 0.1715 0.1477 620 GLN A CG 4702 C CD . GLN A 579 ? 0.6448 0.5837 0.8436 -0.1003 0.1649 0.1504 620 GLN A CD 4703 O OE1 . GLN A 579 ? 0.6584 0.5872 0.8431 -0.0980 0.1542 0.1509 620 GLN A OE1 4704 N NE2 . GLN A 579 ? 0.6559 0.5991 0.8904 -0.1069 0.1711 0.1520 620 GLN A NE2 4705 N N . GLU A 580 ? 0.4139 0.3739 0.5593 -0.0816 0.1308 0.1154 621 GLU A N 4706 C CA . GLU A 580 ? 0.4126 0.3663 0.5299 -0.0761 0.1205 0.1133 621 GLU A CA 4707 C C . GLU A 580 ? 0.3940 0.3454 0.5211 -0.0757 0.1048 0.1063 621 GLU A C 4708 O O . GLU A 580 ? 0.3960 0.3381 0.5076 -0.0732 0.0974 0.1082 621 GLU A O 4709 C CB . GLU A 580 ? 0.4310 0.3923 0.5297 -0.0711 0.1200 0.1068 621 GLU A CB 4710 C CG . GLU A 580 ? 0.4887 0.4501 0.5702 -0.0700 0.1349 0.1137 621 GLU A CG 4711 C CD . GLU A 580 ? 0.5664 0.5360 0.6692 -0.0740 0.1482 0.1156 621 GLU A CD 4712 O OE1 . GLU A 580 ? 0.5761 0.5541 0.7082 -0.0772 0.1458 0.1098 621 GLU A OE1 4713 O OE2 . GLU A 580 ? 0.6579 0.6252 0.7476 -0.0736 0.1617 0.1233 621 GLU A OE2 4714 N N . MET A 581 ? 0.3701 0.3297 0.5226 -0.0776 0.0992 0.0979 622 MET A N 4715 C CA . MET A 581 ? 0.3679 0.3252 0.5295 -0.0768 0.0844 0.0907 622 MET A CA 4716 C C . MET A 581 ? 0.3832 0.3293 0.5544 -0.0802 0.0832 0.0973 622 MET A C 4717 O O . MET A 581 ? 0.3906 0.3298 0.5552 -0.0779 0.0726 0.0951 622 MET A O 4718 C CB . MET A 581 ? 0.3551 0.3230 0.5417 -0.0778 0.0785 0.0804 622 MET A CB 4719 C CG . MET A 581 ? 0.3481 0.3256 0.5239 -0.0733 0.0759 0.0725 622 MET A CG 4720 S SD . MET A 581 ? 0.3820 0.3701 0.5856 -0.0735 0.0666 0.0604 622 MET A SD 4721 C CE . MET A 581 ? 0.3739 0.3542 0.5781 -0.0713 0.0498 0.0545 622 MET A CE 4722 N N . LYS A 582 ? 0.3874 0.3314 0.5735 -0.0855 0.0947 0.1058 623 LYS A N 4723 C CA . LYS A 582 ? 0.4248 0.3570 0.6202 -0.0892 0.0950 0.1135 623 LYS A CA 4724 C C . LYS A 582 ? 0.4442 0.3645 0.6094 -0.0859 0.0960 0.1218 623 LYS A C 4725 O O . LYS A 582 ? 0.4322 0.3432 0.5938 -0.0846 0.0868 0.1221 623 LYS A O 4726 C CB . LYS A 582 ? 0.4352 0.3683 0.6535 -0.0958 0.1087 0.1213 623 LYS A CB 4727 C CG . LYS A 582 ? 0.4339 0.3769 0.6870 -0.0997 0.1059 0.1134 623 LYS A CG 4728 C CD . LYS A 582 ? 0.5297 0.4746 0.8069 -0.1063 0.1205 0.1215 623 LYS A CD 4729 C CE . LYS A 582 ? 0.5618 0.5174 0.8749 -0.1097 0.1155 0.1120 623 LYS A CE 4730 N NZ . LYS A 582 ? 0.6118 0.5805 0.9392 -0.1116 0.1268 0.1114 623 LYS A NZ 4731 N N . THR A 583 ? 0.4618 0.3828 0.6049 -0.0839 0.1066 0.1279 624 THR A N 4732 C CA . THR A 583 ? 0.5048 0.4149 0.6177 -0.0803 0.1088 0.1366 624 THR A CA 4733 C C . THR A 583 ? 0.4833 0.3902 0.5770 -0.0746 0.0948 0.1306 624 THR A C 4734 O O . THR A 583 ? 0.4899 0.3854 0.5718 -0.0730 0.0906 0.1360 624 THR A O 4735 C CB . THR A 583 ? 0.5301 0.4432 0.6218 -0.0783 0.1217 0.1418 624 THR A CB 4736 O OG1 . THR A 583 ? 0.5758 0.4895 0.6840 -0.0836 0.1364 0.1498 624 THR A OG1 4737 C CG2 . THR A 583 ? 0.5739 0.4756 0.6316 -0.0736 0.1222 0.1497 624 THR A CG2 4738 N N . TYR A 584 ? 0.4525 0.3693 0.5438 -0.0715 0.0877 0.1197 625 TYR A N 4739 C CA . TYR A 584 ? 0.4463 0.3615 0.5204 -0.0660 0.0753 0.1138 625 TYR A CA 4740 C C . TYR A 584 ? 0.4289 0.3451 0.5201 -0.0659 0.0623 0.1047 625 TYR A C 4741 O O . TYR A 584 ? 0.4357 0.3524 0.5151 -0.0613 0.0525 0.0986 625 TYR A O 4742 C CB . TYR A 584 ? 0.4331 0.3564 0.4878 -0.0616 0.0758 0.1086 625 TYR A CB 4743 C CG . TYR A 584 ? 0.4717 0.3923 0.5066 -0.0609 0.0878 0.1172 625 TYR A CG 4744 C CD1 . TYR A 584 ? 0.5354 0.4446 0.5482 -0.0584 0.0885 0.1257 625 TYR A CD1 4745 C CD2 . TYR A 584 ? 0.5010 0.4299 0.5394 -0.0624 0.0988 0.1172 625 TYR A CD2 4746 C CE1 . TYR A 584 ? 0.5823 0.4878 0.5754 -0.0573 0.0998 0.1341 625 TYR A CE1 4747 C CE2 . TYR A 584 ? 0.5611 0.4869 0.5805 -0.0613 0.1106 0.1253 625 TYR A CE2 4748 C CZ . TYR A 584 ? 0.6135 0.5274 0.6093 -0.0586 0.1108 0.1336 625 TYR A CZ 4749 O OH . TYR A 584 ? 0.6542 0.5641 0.6296 -0.0570 0.1224 0.1417 625 TYR A OH 4750 N N . SER A 585 ? 0.4180 0.3345 0.5368 -0.0708 0.0625 0.1039 626 SER A N 4751 C CA A SER A 585 ? 0.3904 0.3072 0.5267 -0.0707 0.0501 0.0950 626 SER A CA 4752 C CA B SER A 585 ? 0.4092 0.3263 0.5460 -0.0708 0.0503 0.0950 626 SER A CA 4753 C C . SER A 585 ? 0.3849 0.3112 0.5165 -0.0664 0.0418 0.0836 626 SER A C 4754 O O . SER A 585 ? 0.3842 0.3080 0.5073 -0.0622 0.0313 0.0782 626 SER A O 4755 C CB A SER A 585 ? 0.3957 0.3001 0.5266 -0.0691 0.0424 0.0977 626 SER A CB 4756 C CB B SER A 585 ? 0.4180 0.3225 0.5522 -0.0698 0.0428 0.0978 626 SER A CB 4757 O OG A SER A 585 ? 0.3474 0.2419 0.4819 -0.0729 0.0500 0.1090 626 SER A OG 4758 O OG B SER A 585 ? 0.4674 0.3674 0.5747 -0.0645 0.0395 0.0996 626 SER A OG 4759 N N . VAL A 586 ? 0.3649 0.3020 0.5016 -0.0671 0.0470 0.0801 627 VAL A N 4760 C CA . VAL A 586 ? 0.3635 0.3093 0.4946 -0.0631 0.0406 0.0704 627 VAL A CA 4761 C C . VAL A 586 ? 0.3751 0.3250 0.5304 -0.0642 0.0324 0.0617 627 VAL A C 4762 O O . VAL A 586 ? 0.4003 0.3554 0.5766 -0.0682 0.0368 0.0612 627 VAL A O 4763 C CB . VAL A 586 ? 0.3571 0.3121 0.4825 -0.0630 0.0500 0.0708 627 VAL A CB 4764 C CG1 . VAL A 586 ? 0.3244 0.2877 0.4428 -0.0585 0.0432 0.0609 627 VAL A CG1 4765 C CG2 . VAL A 586 ? 0.3619 0.3118 0.4646 -0.0622 0.0589 0.0799 627 VAL A CG2 4766 N N . SER A 587 ? 0.3834 0.3303 0.5359 -0.0606 0.0207 0.0552 628 SER A N 4767 C CA . SER A 587 ? 0.3830 0.3321 0.5559 -0.0608 0.0116 0.0465 628 SER A CA 4768 C C . SER A 587 ? 0.3580 0.3142 0.5226 -0.0556 0.0044 0.0371 628 SER A C 4769 O O . SER A 587 ? 0.3594 0.3142 0.5032 -0.0511 0.0016 0.0362 628 SER A O 4770 C CB . SER A 587 ? 0.4101 0.3489 0.5872 -0.0604 0.0032 0.0459 628 SER A CB 4771 O OG . SER A 587 ? 0.4316 0.3729 0.6275 -0.0601 -0.0059 0.0366 628 SER A OG 4772 N N . PHE A 588 ? 0.3455 0.3088 0.5271 -0.0561 0.0013 0.0303 629 PHE A N 4773 C CA . PHE A 588 ? 0.3262 0.2951 0.5019 -0.0509 -0.0067 0.0210 629 PHE A CA 4774 C C . PHE A 588 ? 0.3284 0.2927 0.5117 -0.0483 -0.0191 0.0134 629 PHE A C 4775 O O . PHE A 588 ? 0.3080 0.2760 0.4880 -0.0438 -0.0263 0.0056 629 PHE A O 4776 C CB . PHE A 588 ? 0.3185 0.2980 0.5058 -0.0518 -0.0032 0.0176 629 PHE A CB 4777 C CG . PHE A 588 ? 0.3126 0.2971 0.4857 -0.0518 0.0068 0.0223 629 PHE A CG 4778 C CD1 . PHE A 588 ? 0.2878 0.2768 0.4451 -0.0470 0.0048 0.0182 629 PHE A CD1 4779 C CD2 . PHE A 588 ? 0.3577 0.3419 0.5336 -0.0564 0.0186 0.0309 629 PHE A CD2 4780 C CE1 . PHE A 588 ? 0.3097 0.3030 0.4543 -0.0468 0.0136 0.0218 629 PHE A CE1 4781 C CE2 . PHE A 588 ? 0.3278 0.3161 0.4892 -0.0558 0.0278 0.0346 629 PHE A CE2 4782 C CZ . PHE A 588 ? 0.3258 0.3187 0.4719 -0.0509 0.0248 0.0296 629 PHE A CZ 4783 N N . ASP A 589 ? 0.3245 0.2803 0.5167 -0.0507 -0.0215 0.0158 630 ASP A N 4784 C CA . ASP A 589 ? 0.3512 0.3021 0.5519 -0.0482 -0.0336 0.0080 630 ASP A CA 4785 C C . ASP A 589 ? 0.3395 0.2893 0.5199 -0.0410 -0.0410 0.0022 630 ASP A C 4786 O O . ASP A 589 ? 0.3348 0.2855 0.5189 -0.0372 -0.0502 -0.0066 630 ASP A O 4787 C CB . ASP A 589 ? 0.3551 0.2958 0.5655 -0.0515 -0.0347 0.0120 630 ASP A CB 4788 C CG . ASP A 589 ? 0.4511 0.3927 0.6880 -0.0589 -0.0291 0.0160 630 ASP A CG 4789 O OD1 . ASP A 589 ? 0.4852 0.4359 0.7330 -0.0612 -0.0244 0.0153 630 ASP A OD1 4790 O OD2 . ASP A 589 ? 0.5143 0.4473 0.7616 -0.0623 -0.0291 0.0202 630 ASP A OD2 4791 N N . SER A 590 ? 0.3289 0.2764 0.4882 -0.0388 -0.0371 0.0072 631 SER A N 4792 C CA . SER A 590 ? 0.3280 0.2746 0.4692 -0.0321 -0.0432 0.0022 631 SER A CA 4793 C C . SER A 590 ? 0.3100 0.2650 0.4468 -0.0285 -0.0450 -0.0038 631 SER A C 4794 O O . SER A 590 ? 0.3010 0.2554 0.4323 -0.0232 -0.0527 -0.0110 631 SER A O 4795 C CB . SER A 590 ? 0.3422 0.2856 0.4635 -0.0305 -0.0389 0.0085 631 SER A CB 4796 O OG . SER A 590 ? 0.3566 0.3057 0.4705 -0.0327 -0.0298 0.0141 631 SER A OG 4797 N N . LEU A 591 ? 0.2967 0.2590 0.4351 -0.0311 -0.0378 -0.0011 632 LEU A N 4798 C CA . LEU A 591 ? 0.2898 0.2595 0.4240 -0.0278 -0.0391 -0.0062 632 LEU A CA 4799 C C . LEU A 591 ? 0.2893 0.2610 0.4399 -0.0267 -0.0472 -0.0143 632 LEU A C 4800 O O . LEU A 591 ? 0.2796 0.2528 0.4234 -0.0213 -0.0536 -0.0208 632 LEU A O 4801 C CB . LEU A 591 ? 0.2926 0.2695 0.4251 -0.0306 -0.0293 -0.0015 632 LEU A CB 4802 C CG . LEU A 591 ? 0.2809 0.2656 0.4100 -0.0275 -0.0298 -0.0063 632 LEU A CG 4803 C CD1 . LEU A 591 ? 0.2744 0.2577 0.3835 -0.0217 -0.0333 -0.0087 632 LEU A CD1 4804 C CD2 . LEU A 591 ? 0.3093 0.3003 0.4385 -0.0306 -0.0198 -0.0017 632 LEU A CD2 4805 N N . PHE A 592 ? 0.2838 0.2552 0.4560 -0.0315 -0.0473 -0.0139 633 PHE A N 4806 C CA . PHE A 592 ? 0.2949 0.2679 0.4839 -0.0303 -0.0564 -0.0224 633 PHE A CA 4807 C C . PHE A 592 ? 0.3038 0.2693 0.4876 -0.0253 -0.0675 -0.0290 633 PHE A C 4808 O O . PHE A 592 ? 0.3154 0.2821 0.5001 -0.0206 -0.0763 -0.0373 633 PHE A O 4809 C CB . PHE A 592 ? 0.3013 0.2758 0.5169 -0.0370 -0.0538 -0.0205 633 PHE A CB 4810 C CG . PHE A 592 ? 0.3308 0.3150 0.5546 -0.0404 -0.0449 -0.0173 633 PHE A CG 4811 C CD1 . PHE A 592 ? 0.3395 0.3313 0.5704 -0.0379 -0.0489 -0.0238 633 PHE A CD1 4812 C CD2 . PHE A 592 ? 0.3495 0.3346 0.5730 -0.0455 -0.0326 -0.0080 633 PHE A CD2 4813 C CE1 . PHE A 592 ? 0.3428 0.3438 0.5820 -0.0405 -0.0407 -0.0214 633 PHE A CE1 4814 C CE2 . PHE A 592 ? 0.3699 0.3641 0.6000 -0.0479 -0.0239 -0.0055 633 PHE A CE2 4815 C CZ . PHE A 592 ? 0.3193 0.3216 0.5581 -0.0455 -0.0281 -0.0125 633 PHE A CZ 4816 N N . SER A 593 ? 0.3028 0.2603 0.4809 -0.0259 -0.0671 -0.0254 634 SER A N 4817 C CA . SER A 593 ? 0.3197 0.2696 0.4910 -0.0208 -0.0765 -0.0312 634 SER A CA 4818 C C . SER A 593 ? 0.3063 0.2580 0.4561 -0.0135 -0.0790 -0.0350 634 SER A C 4819 O O . SER A 593 ? 0.3108 0.2603 0.4580 -0.0080 -0.0880 -0.0431 634 SER A O 4820 C CB . SER A 593 ? 0.3283 0.2696 0.4969 -0.0228 -0.0744 -0.0256 634 SER A CB 4821 O OG . SER A 593 ? 0.3416 0.2758 0.5001 -0.0169 -0.0822 -0.0308 634 SER A OG 4822 N N . ALA A 594 ? 0.2799 0.2352 0.4141 -0.0131 -0.0711 -0.0294 635 ALA A N 4823 C CA . ALA A 594 ? 0.2852 0.2424 0.4006 -0.0068 -0.0722 -0.0322 635 ALA A CA 4824 C C . ALA A 594 ? 0.2897 0.2523 0.4078 -0.0037 -0.0766 -0.0385 635 ALA A C 4825 O O . ALA A 594 ? 0.3110 0.2721 0.4182 0.0027 -0.0823 -0.0440 635 ALA A O 4826 C CB . ALA A 594 ? 0.2619 0.2225 0.3627 -0.0078 -0.0628 -0.0249 635 ALA A CB 4827 N N . VAL A 595 ? 0.2902 0.2592 0.4220 -0.0080 -0.0733 -0.0372 636 VAL A N 4828 C CA . VAL A 595 ? 0.2955 0.2699 0.4311 -0.0050 -0.0776 -0.0430 636 VAL A CA 4829 C C . VAL A 595 ? 0.3104 0.2807 0.4551 -0.0015 -0.0897 -0.0518 636 VAL A C 4830 O O . VAL A 595 ? 0.3116 0.2822 0.4486 0.0047 -0.0964 -0.0580 636 VAL A O 4831 C CB . VAL A 595 ? 0.2918 0.2740 0.4422 -0.0104 -0.0712 -0.0399 636 VAL A CB 4832 C CG1 . VAL A 595 ? 0.3083 0.2958 0.4681 -0.0076 -0.0775 -0.0466 636 VAL A CG1 4833 C CG2 . VAL A 595 ? 0.3012 0.2874 0.4382 -0.0119 -0.0605 -0.0328 636 VAL A CG2 4834 N N . LYS A 596 ? 0.3105 0.2766 0.4713 -0.0054 -0.0927 -0.0524 637 LYS A N 4835 C CA . LYS A 596 ? 0.3296 0.2906 0.5004 -0.0024 -0.1051 -0.0614 637 LYS A CA 4836 C C . LYS A 596 ? 0.3367 0.2909 0.4862 0.0056 -0.1111 -0.0660 637 LYS A C 4837 O O . LYS A 596 ? 0.3294 0.2821 0.4743 0.0120 -0.1204 -0.0741 637 LYS A O 4838 C CB . LYS A 596 ? 0.3453 0.3014 0.5354 -0.0085 -0.1057 -0.0598 637 LYS A CB 4839 C CG . LYS A 596 ? 0.4241 0.3737 0.6258 -0.0057 -0.1191 -0.0695 637 LYS A CG 4840 C CD . LYS A 596 ? 0.4753 0.4200 0.6990 -0.0127 -0.1189 -0.0671 637 LYS A CD 4841 C CE . LYS A 596 ? 0.5741 0.5123 0.8107 -0.0101 -0.1328 -0.0775 637 LYS A CE 4842 N NZ . LYS A 596 ? 0.6069 0.5360 0.8228 -0.0036 -0.1371 -0.0804 637 LYS A NZ 4843 N N . ASN A 597 ? 0.3135 0.2639 0.4492 0.0057 -0.1054 -0.0607 638 ASN A N 4844 C CA . ASN A 597 ? 0.3420 0.2867 0.4578 0.0132 -0.1091 -0.0641 638 ASN A CA 4845 C C . ASN A 597 ? 0.3334 0.2818 0.4320 0.0194 -0.1088 -0.0661 638 ASN A C 4846 O O . ASN A 597 ? 0.3492 0.2934 0.4370 0.0268 -0.1161 -0.0728 638 ASN A O 4847 C CB . ASN A 597 ? 0.3289 0.2701 0.4345 0.0119 -0.1023 -0.0575 638 ASN A CB 4848 C CG . ASN A 597 ? 0.3565 0.2910 0.4748 0.0081 -0.1045 -0.0566 638 ASN A CG 4849 O OD1 . ASN A 597 ? 0.3415 0.2730 0.4759 0.0069 -0.1119 -0.0620 638 ASN A OD1 4850 N ND2 . ASN A 597 ? 0.3546 0.2864 0.4668 0.0062 -0.0985 -0.0500 638 ASN A ND2 4851 N N . PHE A 598 ? 0.3203 0.2759 0.4162 0.0167 -0.1007 -0.0604 639 PHE A N 4852 C CA . PHE A 598 ? 0.3199 0.2789 0.4011 0.0220 -0.0998 -0.0615 639 PHE A CA 4853 C C . PHE A 598 ? 0.3416 0.3008 0.4275 0.0266 -0.1097 -0.0697 639 PHE A C 4854 O O . PHE A 598 ? 0.3413 0.2981 0.4114 0.0341 -0.1136 -0.0736 639 PHE A O 4855 C CB . PHE A 598 ? 0.3065 0.2731 0.3879 0.0177 -0.0902 -0.0548 639 PHE A CB 4856 C CG . PHE A 598 ? 0.3175 0.2868 0.3827 0.0228 -0.0879 -0.0546 639 PHE A CG 4857 C CD1 . PHE A 598 ? 0.3094 0.2791 0.3599 0.0234 -0.0805 -0.0494 639 PHE A CD1 4858 C CD2 . PHE A 598 ? 0.3231 0.2947 0.3891 0.0267 -0.0932 -0.0594 639 PHE A CD2 4859 C CE1 . PHE A 598 ? 0.3629 0.3347 0.3999 0.0277 -0.0779 -0.0488 639 PHE A CE1 4860 C CE2 . PHE A 598 ? 0.3137 0.2869 0.3649 0.0315 -0.0909 -0.0587 639 PHE A CE2 4861 C CZ . PHE A 598 ? 0.3194 0.2928 0.3564 0.0318 -0.0828 -0.0531 639 PHE A CZ 4862 N N . THR A 599 ? 0.3325 0.2947 0.4397 0.0220 -0.1131 -0.0717 640 THR A N 4863 C CA . THR A 599 ? 0.3548 0.3177 0.4705 0.0257 -0.1237 -0.0800 640 THR A CA 4864 C C . THR A 599 ? 0.3703 0.3245 0.4776 0.0329 -0.1348 -0.0882 640 THR A C 4865 O O . THR A 599 ? 0.3699 0.3223 0.4651 0.0406 -0.1417 -0.0939 640 THR A O 4866 C CB . THR A 599 ? 0.3544 0.3221 0.4987 0.0185 -0.1250 -0.0805 640 THR A CB 4867 O OG1 . THR A 599 ? 0.3440 0.3192 0.4934 0.0124 -0.1134 -0.0725 640 THR A OG1 4868 C CG2 . THR A 599 ? 0.3716 0.3419 0.5266 0.0223 -0.1359 -0.0889 640 THR A CG2 4869 N N . GLU A 600 ? 0.3679 0.3162 0.4811 0.0306 -0.1365 -0.0889 641 GLU A N 4870 C CA . GLU A 600 ? 0.4050 0.3444 0.5108 0.0372 -0.1466 -0.0969 641 GLU A CA 4871 C C . GLU A 600 ? 0.4051 0.3406 0.4824 0.0458 -0.1452 -0.0974 641 GLU A C 4872 O O . GLU A 600 ? 0.3958 0.3269 0.4618 0.0540 -0.1538 -0.1049 641 GLU A O 4873 C CB . GLU A 600 ? 0.4102 0.3440 0.5285 0.0325 -0.1472 -0.0964 641 GLU A CB 4874 C CG . GLU A 600 ? 0.5240 0.4604 0.6719 0.0252 -0.1510 -0.0980 641 GLU A CG 4875 C CD . GLU A 600 ? 0.6169 0.5479 0.7799 0.0192 -0.1502 -0.0957 641 GLU A CD 4876 O OE1 . GLU A 600 ? 0.6436 0.5764 0.8320 0.0128 -0.1522 -0.0962 641 GLU A OE1 4877 O OE2 . GLU A 600 ? 0.6750 0.6001 0.8252 0.0208 -0.1472 -0.0932 641 GLU A OE2 4878 N N . ILE A 601 ? 0.3784 0.3155 0.4441 0.0443 -0.1343 -0.0894 642 ILE A N 4879 C CA . ILE A 601 ? 0.3887 0.3225 0.4300 0.0517 -0.1315 -0.0891 642 ILE A CA 4880 C C . ILE A 601 ? 0.3918 0.3288 0.4205 0.0569 -0.1315 -0.0898 642 ILE A C 4881 O O . ILE A 601 ? 0.4011 0.3334 0.4112 0.0655 -0.1348 -0.0936 642 ILE A O 4882 C CB . ILE A 601 ? 0.3636 0.2988 0.3987 0.0480 -0.1201 -0.0804 642 ILE A CB 4883 C CG1 . ILE A 601 ? 0.3804 0.3100 0.4239 0.0452 -0.1217 -0.0807 642 ILE A CG1 4884 C CG2 . ILE A 601 ? 0.4006 0.3349 0.4123 0.0549 -0.1151 -0.0787 642 ILE A CG2 4885 C CD1 . ILE A 601 ? 0.3811 0.3130 0.4236 0.0400 -0.1112 -0.0715 642 ILE A CD1 4886 N N . ALA A 602 ? 0.3742 0.3189 0.4122 0.0521 -0.1275 -0.0858 643 ALA A N 4887 C CA . ALA A 602 ? 0.3905 0.3382 0.4183 0.0568 -0.1277 -0.0861 643 ALA A CA 4888 C C . ALA A 602 ? 0.4082 0.3515 0.4344 0.0640 -0.1408 -0.0956 643 ALA A C 4889 O O . ALA A 602 ? 0.4006 0.3411 0.4084 0.0721 -0.1432 -0.0977 643 ALA A O 4890 C CB . ALA A 602 ? 0.3807 0.3372 0.4222 0.0503 -0.1224 -0.0814 643 ALA A CB 4891 N N . SER A 603 ? 0.4178 0.3605 0.4636 0.0609 -0.1492 -0.1011 644 SER A N 4892 C CA . SER A 603 ? 0.4617 0.4002 0.5083 0.0674 -0.1631 -0.1110 644 SER A CA 4893 C C . SER A 603 ? 0.4680 0.3967 0.4919 0.0769 -0.1681 -0.1163 644 SER A C 4894 O O . SER A 603 ? 0.4834 0.4084 0.4921 0.0857 -0.1750 -0.1214 644 SER A O 4895 C CB . SER A 603 ? 0.4701 0.4096 0.5448 0.0614 -0.1707 -0.1158 644 SER A CB 4896 O OG . SER A 603 ? 0.5870 0.5221 0.6636 0.0678 -0.1855 -0.1264 644 SER A OG 4897 N N . LYS A 604 ? 0.4401 0.3644 0.4611 0.0756 -0.1645 -0.1150 645 LYS A N 4898 C CA . LYS A 604 ? 0.4727 0.3881 0.4726 0.0845 -0.1677 -0.1196 645 LYS A CA 4899 C C . LYS A 604 ? 0.4648 0.3800 0.4390 0.0910 -0.1600 -0.1151 645 LYS A C 4900 O O . LYS A 604 ? 0.4531 0.3619 0.4075 0.1008 -0.1650 -0.1202 645 LYS A O 4901 C CB . LYS A 604 ? 0.4816 0.3930 0.4863 0.0813 -0.1650 -0.1188 645 LYS A CB 4902 C CG . LYS A 604 ? 0.5482 0.4578 0.5778 0.0759 -0.1738 -0.1242 645 LYS A CG 4903 C CD . LYS A 604 ? 0.6928 0.5954 0.7238 0.0756 -0.1742 -0.1258 645 LYS A CD 4904 C CE . LYS A 604 ? 0.7706 0.6688 0.8237 0.0727 -0.1859 -0.1336 645 LYS A CE 4905 N NZ . LYS A 604 ? 0.8020 0.7019 0.8760 0.0623 -0.1798 -0.1271 645 LYS A NZ 4906 N N . PHE A 605 ? 0.4230 0.3448 0.3974 0.0857 -0.1479 -0.1056 646 PHE A N 4907 C CA . PHE A 605 ? 0.4354 0.3575 0.3882 0.0909 -0.1400 -0.1007 646 PHE A CA 4908 C C . PHE A 605 ? 0.4538 0.3752 0.3966 0.0975 -0.1457 -0.1037 646 PHE A C 4909 O O . PHE A 605 ? 0.4776 0.3941 0.3977 0.1064 -0.1450 -0.1043 646 PHE A O 4910 C CB . PHE A 605 ? 0.4218 0.3517 0.3800 0.0831 -0.1272 -0.0906 646 PHE A CB 4911 C CG . PHE A 605 ? 0.4139 0.3445 0.3531 0.0875 -0.1187 -0.0852 646 PHE A CG 4912 C CD1 . PHE A 605 ? 0.4178 0.3453 0.3426 0.0909 -0.1118 -0.0825 646 PHE A CD1 4913 C CD2 . PHE A 605 ? 0.4472 0.3813 0.3837 0.0884 -0.1177 -0.0830 646 PHE A CD2 4914 C CE1 . PHE A 605 ? 0.4389 0.3671 0.3480 0.0946 -0.1034 -0.0772 646 PHE A CE1 4915 C CE2 . PHE A 605 ? 0.4449 0.3789 0.3646 0.0924 -0.1097 -0.0777 646 PHE A CE2 4916 C CZ . PHE A 605 ? 0.4359 0.3671 0.3423 0.0952 -0.1024 -0.0746 646 PHE A CZ 4917 N N . SER A 606 ? 0.4413 0.3677 0.4007 0.0935 -0.1508 -0.1051 647 SER A N 4918 C CA . SER A 606 ? 0.4714 0.3976 0.4235 0.0996 -0.1570 -0.1079 647 SER A CA 4919 C C . SER A 606 ? 0.5029 0.4196 0.4401 0.1104 -0.1696 -0.1176 647 SER A C 4920 O O . SER A 606 ? 0.5217 0.4345 0.4393 0.1192 -0.1723 -0.1186 647 SER A O 4921 C CB . SER A 606 ? 0.4537 0.3870 0.4305 0.0933 -0.1618 -0.1092 647 SER A CB 4922 O OG A SER A 606 ? 0.4405 0.3820 0.4296 0.0842 -0.1506 -0.1010 647 SER A OG 4923 O OG B SER A 606 ? 0.4736 0.4078 0.4443 0.0986 -0.1663 -0.1105 647 SER A OG 4924 N N . GLU A 607 ? 0.5149 0.4278 0.4618 0.1097 -0.1775 -0.1245 648 GLU A N 4925 C CA . GLU A 607 ? 0.5609 0.4640 0.4941 0.1198 -0.1900 -0.1347 648 GLU A CA 4926 C C . GLU A 607 ? 0.5725 0.4686 0.4754 0.1287 -0.1840 -0.1330 648 GLU A C 4927 O O . GLU A 607 ? 0.5628 0.4524 0.4440 0.1392 -0.1896 -0.1371 648 GLU A O 4928 C CB . GLU A 607 ? 0.5885 0.4886 0.5388 0.1164 -0.1979 -0.1417 648 GLU A CB 4929 C CG . GLU A 607 ? 0.6641 0.5700 0.6447 0.1088 -0.2055 -0.1449 648 GLU A CG 4930 C CD . GLU A 607 ? 0.7885 0.6901 0.7873 0.1059 -0.2147 -0.1527 648 GLU A CD 4931 O OE1 . GLU A 607 ? 0.7952 0.6892 0.7837 0.1093 -0.2151 -0.1556 648 GLU A OE1 4932 O OE2 . GLU A 607 ? 0.8515 0.7574 0.8764 0.1001 -0.2217 -0.1560 648 GLU A OE2 4933 N N . ARG A 608 ? 0.5341 0.4316 0.4354 0.1247 -0.1721 -0.1266 649 ARG A N 4934 C CA . ARG A 608 ? 0.5399 0.4319 0.4151 0.1323 -0.1645 -0.1242 649 ARG A CA 4935 C C . ARG A 608 ? 0.5413 0.4346 0.3992 0.1367 -0.1578 -0.1179 649 ARG A C 4936 O O . ARG A 608 ? 0.5525 0.4390 0.3856 0.1467 -0.1571 -0.1191 649 ARG A O 4937 C CB . ARG A 608 ? 0.5292 0.4235 0.4089 0.1267 -0.1532 -0.1184 649 ARG A CB 4938 C CG . ARG A 608 ? 0.5479 0.4388 0.4407 0.1241 -0.1593 -0.1243 649 ARG A CG 4939 C CD . ARG A 608 ? 0.5388 0.4294 0.4287 0.1224 -0.1491 -0.1197 649 ARG A CD 4940 N NE . ARG A 608 ? 0.4995 0.3985 0.3961 0.1145 -0.1363 -0.1089 649 ARG A NE 4941 C CZ . ARG A 608 ? 0.5154 0.4207 0.4338 0.1040 -0.1339 -0.1047 649 ARG A CZ 4942 N NH1 . ARG A 608 ? 0.4879 0.3921 0.4247 0.0996 -0.1428 -0.1097 649 ARG A NH1 4943 N NH2 . ARG A 608 ? 0.4575 0.3697 0.3791 0.0980 -0.1226 -0.0954 649 ARG A NH2 4944 N N . LEU A 609 ? 0.5331 0.4346 0.4037 0.1295 -0.1529 -0.1115 650 LEU A N 4945 C CA . LEU A 609 ? 0.5608 0.4636 0.4172 0.1328 -0.1460 -0.1049 650 LEU A CA 4946 C C . LEU A 609 ? 0.6066 0.5035 0.4486 0.1425 -0.1567 -0.1105 650 LEU A C 4947 O O . LEU A 609 ? 0.6111 0.5043 0.4319 0.1497 -0.1526 -0.1068 650 LEU A O 4948 C CB . LEU A 609 ? 0.5440 0.4568 0.4193 0.1227 -0.1392 -0.0976 650 LEU A CB 4949 C CG . LEU A 609 ? 0.5439 0.4593 0.4091 0.1232 -0.1290 -0.0890 650 LEU A CG 4950 C CD1 . LEU A 609 ? 0.5011 0.4163 0.3564 0.1226 -0.1160 -0.0825 650 LEU A CD1 4951 C CD2 . LEU A 609 ? 0.5244 0.4493 0.4113 0.1139 -0.1268 -0.0850 650 LEU A CD2 4952 N N . GLN A 610 ? 0.6383 0.5341 0.4924 0.1429 -0.1706 -0.1193 651 GLN A N 4953 C CA . GLN A 610 ? 0.7009 0.5916 0.5435 0.1520 -0.1825 -0.1252 651 GLN A CA 4954 C C . GLN A 610 ? 0.7296 0.6087 0.5463 0.1640 -0.1887 -0.1321 651 GLN A C 4955 O O . GLN A 610 ? 0.7715 0.6442 0.5662 0.1743 -0.1933 -0.1337 651 GLN A O 4956 C CB A GLN A 610 ? 0.6908 0.5862 0.5592 0.1473 -0.1950 -0.1315 651 GLN A CB 4957 C CB B GLN A 610 ? 0.6869 0.5824 0.5560 0.1470 -0.1951 -0.1317 651 GLN A CB 4958 C CG A GLN A 610 ? 0.7106 0.6157 0.5951 0.1399 -0.1895 -0.1246 651 GLN A CG 4959 C CG B GLN A 610 ? 0.7276 0.6165 0.5906 0.1562 -0.2126 -0.1426 651 GLN A CG 4960 C CD A GLN A 610 ? 0.7428 0.6538 0.6550 0.1349 -0.2005 -0.1304 651 GLN A CD 4961 C CD B GLN A 610 ? 0.7413 0.6286 0.6222 0.1537 -0.2240 -0.1525 651 GLN A CD 4962 O OE1 A GLN A 610 ? 0.8082 0.7152 0.7247 0.1390 -0.2146 -0.1402 651 GLN A OE1 4963 O OE1 B GLN A 610 ? 0.7112 0.5973 0.5958 0.1499 -0.2193 -0.1524 651 GLN A OE1 4964 N NE2 A GLN A 610 ? 0.7332 0.6539 0.6651 0.1261 -0.1939 -0.1245 651 GLN A NE2 4965 N NE2 B GLN A 610 ? 0.7433 0.6306 0.6369 0.1556 -0.2394 -0.1611 651 GLN A NE2 4966 N N . ASP A 611 ? 0.7515 0.6280 0.5698 0.1628 -0.1871 -0.1351 652 ASP A N 4967 C CA . ASP A 611 ? 0.7925 0.6584 0.5911 0.1729 -0.1933 -0.1432 652 ASP A CA 4968 C C . ASP A 611 ? 0.7994 0.6599 0.5726 0.1793 -0.1815 -0.1390 652 ASP A C 4969 O O . ASP A 611 ? 0.8162 0.6681 0.5743 0.1876 -0.1868 -0.1464 652 ASP A O 4970 C CB . ASP A 611 ? 0.7999 0.6658 0.6192 0.1673 -0.1998 -0.1502 652 ASP A CB 4971 C CG . ASP A 611 ? 0.8645 0.7306 0.7029 0.1659 -0.2168 -0.1598 652 ASP A CG 4972 O OD1 . ASP A 611 ? 0.9371 0.8022 0.7929 0.1617 -0.2229 -0.1660 652 ASP A OD1 4973 O OD2 . ASP A 611 ? 0.9235 0.7905 0.7606 0.1690 -0.2240 -0.1613 652 ASP A OD2 4974 N N . PHE A 612 ? 0.7861 0.6516 0.5560 0.1756 -0.1657 -0.1279 653 PHE A N 4975 C CA . PHE A 612 ? 0.7941 0.6547 0.5405 0.1822 -0.1540 -0.1238 653 PHE A CA 4976 C C . PHE A 612 ? 0.8352 0.6897 0.5525 0.1929 -0.1508 -0.1202 653 PHE A C 4977 O O . PHE A 612 ? 0.8771 0.7261 0.5709 0.2008 -0.1416 -0.1173 653 PHE A O 4978 C CB . PHE A 612 ? 0.7678 0.6369 0.5275 0.1724 -0.1386 -0.1139 653 PHE A CB 4979 C CG . PHE A 612 ? 0.6915 0.5662 0.4508 0.1690 -0.1288 -0.1037 653 PHE A CG 4980 C CD1 . PHE A 612 ? 0.7081 0.5813 0.4495 0.1733 -0.1157 -0.0962 653 PHE A CD1 4981 C CD2 . PHE A 612 ? 0.6996 0.5812 0.4775 0.1614 -0.1324 -0.1017 653 PHE A CD2 4982 C CE1 . PHE A 612 ? 0.7354 0.6134 0.4779 0.1697 -0.1067 -0.0868 653 PHE A CE1 4983 C CE2 . PHE A 612 ? 0.7063 0.5928 0.4845 0.1582 -0.1236 -0.0927 653 PHE A CE2 4984 C CZ . PHE A 612 ? 0.7242 0.6087 0.4849 0.1622 -0.1109 -0.0852 653 PHE A CZ 4985 N N A SER A 615 ? 0.6092 0.4409 0.2236 0.2271 -0.1152 -0.0996 656 SER A N 4986 N N B SER A 615 ? 0.5992 0.4421 0.2247 0.2157 -0.0904 -0.0763 656 SER A N 4987 C CA A SER A 615 ? 0.6257 0.4539 0.2194 0.2329 -0.0991 -0.0914 656 SER A CA 4988 C CA B SER A 615 ? 0.6116 0.4487 0.2131 0.2235 -0.0759 -0.0692 656 SER A CA 4989 C C A SER A 615 ? 0.5981 0.4349 0.2081 0.2241 -0.0832 -0.0844 656 SER A C 4990 C C B SER A 615 ? 0.6232 0.4638 0.2292 0.2211 -0.0631 -0.0669 656 SER A C 4991 O O A SER A 615 ? 0.6013 0.4367 0.1983 0.2276 -0.0685 -0.0766 656 SER A O 4992 O O B SER A 615 ? 0.6369 0.4735 0.2252 0.2273 -0.0501 -0.0610 656 SER A O 4993 C CB A SER A 615 ? 0.6260 0.4422 0.1899 0.2471 -0.1026 -0.0986 656 SER A CB 4994 C CB B SER A 615 ? 0.6432 0.4669 0.2107 0.2390 -0.0824 -0.0740 656 SER A CB 4995 O OG A SER A 615 ? 0.6377 0.4550 0.2107 0.2454 -0.1040 -0.1056 656 SER A OG 4996 O OG B SER A 615 ? 0.6082 0.4278 0.1620 0.2431 -0.0795 -0.0665 656 SER A OG 4997 N N A ASN A 616 ? 0.5758 0.4210 0.2139 0.2132 -0.0861 -0.0871 657 ASN A N 4998 N N B ASN A 616 ? 0.6090 0.4565 0.2381 0.2127 -0.0667 -0.0716 657 ASN A N 4999 C CA A ASN A 616 ? 0.5560 0.4083 0.2086 0.2062 -0.0737 -0.0824 657 ASN A CA 5000 C CA B ASN A 616 ? 0.6213 0.4728 0.2571 0.2099 -0.0551 -0.0693 657 ASN A CA 5001 C C A ASN A 616 ? 0.5321 0.3949 0.2061 0.1943 -0.0652 -0.0729 657 ASN A C 5002 C C B ASN A 616 ? 0.5879 0.4505 0.2477 0.1974 -0.0454 -0.0602 657 ASN A C 5003 O O A ASN A 616 ? 0.5062 0.3752 0.2019 0.1852 -0.0723 -0.0742 657 ASN A O 5004 O O B ASN A 616 ? 0.5729 0.4426 0.2559 0.1875 -0.0517 -0.0618 657 ASN A O 5005 C CB A ASN A 616 ? 0.5513 0.4053 0.2198 0.2022 -0.0817 -0.0909 657 ASN A CB 5006 C CB B ASN A 616 ? 0.6196 0.4712 0.2653 0.2088 -0.0650 -0.0796 657 ASN A CB 5007 C CG A ASN A 616 ? 0.5608 0.4188 0.2364 0.1995 -0.0698 -0.0879 657 ASN A CG 5008 C CG B ASN A 616 ? 0.6614 0.5176 0.3171 0.2052 -0.0546 -0.0778 657 ASN A CG 5009 O OD1 A ASN A 616 ? 0.5247 0.3902 0.2110 0.1927 -0.0578 -0.0788 657 ASN A OD1 5010 O OD1 B ASN A 616 ? 0.6890 0.5531 0.3580 0.1979 -0.0428 -0.0692 657 ASN A OD1 5011 N ND2 A ASN A 616 ? 0.6019 0.4551 0.2723 0.2047 -0.0735 -0.0956 657 ASN A ND2 5012 N ND2 B ASN A 616 ? 0.6635 0.5153 0.3148 0.2102 -0.0597 -0.0863 657 ASN A ND2 5013 N N A PRO A 617 ? 0.5338 0.3983 0.2019 0.1946 -0.0500 -0.0633 658 PRO A N 5014 N N B PRO A 617 ? 0.5871 0.4510 0.2415 0.1979 -0.0299 -0.0505 658 PRO A N 5015 C CA A PRO A 617 ? 0.5152 0.3884 0.2015 0.1843 -0.0428 -0.0546 658 PRO A CA 5016 C CA B PRO A 617 ? 0.5597 0.4334 0.2364 0.1863 -0.0223 -0.0424 658 PRO A CA 5017 C C A PRO A 617 ? 0.4903 0.3732 0.2027 0.1732 -0.0392 -0.0535 658 PRO A C 5018 C C B PRO A 617 ? 0.5406 0.4242 0.2447 0.1753 -0.0222 -0.0437 658 PRO A C 5019 O O A PRO A 617 ? 0.4725 0.3630 0.2030 0.1637 -0.0372 -0.0488 658 PRO A O 5020 O O B PRO A 617 ? 0.5188 0.4094 0.2422 0.1656 -0.0240 -0.0413 658 PRO A O 5021 C CB A PRO A 617 ? 0.5192 0.3899 0.1901 0.1891 -0.0277 -0.0452 658 PRO A CB 5022 C CB B PRO A 617 ? 0.5752 0.4476 0.2410 0.1898 -0.0058 -0.0328 658 PRO A CB 5023 C CG A PRO A 617 ? 0.5435 0.4086 0.1978 0.1981 -0.0229 -0.0483 658 PRO A CG 5024 C CG B PRO A 617 ? 0.6012 0.4616 0.2345 0.2042 -0.0061 -0.0348 658 PRO A CG 5025 C CD A PRO A 617 ? 0.5534 0.4120 0.1992 0.2041 -0.0384 -0.0601 658 PRO A CD 5026 C CD B PRO A 617 ? 0.6009 0.4572 0.2292 0.2088 -0.0192 -0.0464 658 PRO A CD 5027 N N A ILE A 618 ? 0.5022 0.3845 0.2154 0.1750 -0.0382 -0.0578 659 ILE A N 5028 N N B ILE A 618 ? 0.5445 0.4284 0.2502 0.1768 -0.0200 -0.0474 659 ILE A N 5029 C CA A ILE A 618 ? 0.4869 0.3772 0.2233 0.1656 -0.0363 -0.0577 659 ILE A CA 5030 C CA B ILE A 618 ? 0.5275 0.4199 0.2586 0.1665 -0.0212 -0.0486 659 ILE A CA 5031 C C A ILE A 618 ? 0.4695 0.3625 0.2235 0.1585 -0.0493 -0.0634 659 ILE A C 5032 C C B ILE A 618 ? 0.5111 0.4042 0.2542 0.1619 -0.0359 -0.0558 659 ILE A C 5033 O O A ILE A 618 ? 0.4357 0.3365 0.2106 0.1482 -0.0482 -0.0603 659 ILE A O 5034 O O B ILE A 618 ? 0.4972 0.3976 0.2610 0.1518 -0.0375 -0.0539 659 ILE A O 5035 C CB A ILE A 618 ? 0.5114 0.3995 0.2441 0.1702 -0.0331 -0.0616 659 ILE A CB 5036 C CB B ILE A 618 ? 0.5266 0.4201 0.2600 0.1683 -0.0148 -0.0500 659 ILE A CB 5037 C CG1 A ILE A 618 ? 0.5506 0.4360 0.2664 0.1779 -0.0193 -0.0565 659 ILE A CG1 5038 C CG1 B ILE A 618 ? 0.5617 0.4580 0.2924 0.1693 0.0010 -0.0413 659 ILE A CG1 5039 C CG2 A ILE A 618 ? 0.4923 0.3884 0.2496 0.1603 -0.0321 -0.0609 659 ILE A CG2 5040 C CG2 B ILE A 618 ? 0.5091 0.4101 0.2676 0.1582 -0.0184 -0.0516 659 ILE A CG2 5041 C CD1 A ILE A 618 ? 0.5772 0.4668 0.2946 0.1745 -0.0084 -0.0462 659 ILE A CD1 5042 C CD1 B ILE A 618 ? 0.5456 0.4461 0.2832 0.1631 0.0055 -0.0333 659 ILE A CD1 5043 N N A VAL A 619 ? 0.4704 0.3567 0.2160 0.1642 -0.0615 -0.0719 660 VAL A N 5044 N N B VAL A 619 ? 0.5167 0.4022 0.2473 0.1692 -0.0466 -0.0641 660 VAL A N 5045 C CA A VAL A 619 ? 0.4724 0.3608 0.2349 0.1580 -0.0741 -0.0776 660 VAL A CA 5046 C CA B VAL A 619 ? 0.4966 0.3828 0.2407 0.1646 -0.0608 -0.0712 660 VAL A CA 5047 C C A VAL A 619 ? 0.4622 0.3553 0.2334 0.1523 -0.0756 -0.0733 660 VAL A C 5048 C C B VAL A 619 ? 0.4882 0.3790 0.2429 0.1580 -0.0642 -0.0677 660 VAL A C 5049 O O A VAL A 619 ? 0.4342 0.3337 0.2264 0.1428 -0.0787 -0.0729 660 VAL A O 5050 O O B VAL A 619 ? 0.4622 0.3594 0.2385 0.1485 -0.0683 -0.0682 660 VAL A O 5051 C CB A VAL A 619 ? 0.4879 0.3674 0.2395 0.1662 -0.0874 -0.0883 660 VAL A CB 5052 C CB B VAL A 619 ? 0.5236 0.4001 0.2524 0.1742 -0.0728 -0.0816 660 VAL A CB 5053 C CG1 A VAL A 619 ? 0.4949 0.3767 0.2645 0.1600 -0.1004 -0.0934 660 VAL A CG1 5054 C CG1 B VAL A 619 ? 0.4936 0.3709 0.2375 0.1695 -0.0878 -0.0886 660 VAL A CG1 5055 C CG2 A VAL A 619 ? 0.5071 0.3834 0.2571 0.1692 -0.0868 -0.0931 660 VAL A CG2 5056 C CG2 B VAL A 619 ? 0.5465 0.4198 0.2708 0.1787 -0.0700 -0.0859 660 VAL A CG2 5057 N N A LEU A 620 ? 0.4709 0.3604 0.2253 0.1584 -0.0731 -0.0699 661 LEU A N 5058 N N B LEU A 620 ? 0.4920 0.3796 0.2319 0.1630 -0.0618 -0.0638 661 LEU A N 5059 C CA A LEU A 620 ? 0.4606 0.3541 0.2217 0.1539 -0.0734 -0.0653 661 LEU A CA 5060 C CA B LEU A 620 ? 0.4853 0.3774 0.2354 0.1571 -0.0637 -0.0600 661 LEU A CA 5061 C C A LEU A 620 ? 0.4474 0.3504 0.2273 0.1431 -0.0635 -0.0575 661 LEU A C 5062 C C B LEU A 620 ? 0.4637 0.3655 0.2338 0.1461 -0.0540 -0.0526 661 LEU A C 5063 O O A LEU A 620 ? 0.4042 0.3133 0.2023 0.1348 -0.0670 -0.0571 661 LEU A O 5064 O O B LEU A 620 ? 0.4249 0.3329 0.2125 0.1378 -0.0570 -0.0517 661 LEU A O 5065 C CB A LEU A 620 ? 0.4822 0.3693 0.2202 0.1629 -0.0697 -0.0614 661 LEU A CB 5066 C CB B LEU A 620 ? 0.4932 0.3793 0.2226 0.1651 -0.0616 -0.0562 661 LEU A CB 5067 C CG A LEU A 620 ? 0.4832 0.3740 0.2270 0.1588 -0.0677 -0.0551 661 LEU A CG 5068 C CG B LEU A 620 ? 0.4975 0.3870 0.2342 0.1607 -0.0620 -0.0512 661 LEU A CG 5069 C CD1 A LEU A 620 ? 0.4480 0.3429 0.2094 0.1531 -0.0794 -0.0600 661 LEU A CD1 5070 C CD1 B LEU A 620 ? 0.4540 0.3461 0.2049 0.1569 -0.0760 -0.0577 661 LEU A CD1 5071 C CD2 A LEU A 620 ? 0.5063 0.3887 0.2248 0.1693 -0.0660 -0.0521 661 LEU A CD2 5072 C CD2 B LEU A 620 ? 0.4638 0.3453 0.1760 0.1705 -0.0583 -0.0467 661 LEU A CD2 5073 N N A ARG A 621 ? 0.4445 0.3486 0.2196 0.1436 -0.0512 -0.0516 662 ARG A N 5074 N N B ARG A 621 ? 0.4688 0.3721 0.2366 0.1462 -0.0423 -0.0476 662 ARG A N 5075 C CA A ARG A 621 ? 0.4452 0.3574 0.2355 0.1347 -0.0417 -0.0442 662 ARG A CA 5076 C CA B ARG A 621 ? 0.4536 0.3657 0.2400 0.1362 -0.0342 -0.0413 662 ARG A CA 5077 C C A ARG A 621 ? 0.4406 0.3586 0.2506 0.1266 -0.0440 -0.0466 662 ARG A C 5078 C C B ARG A 621 ? 0.4533 0.3714 0.2612 0.1273 -0.0401 -0.0449 662 ARG A C 5079 O O A ARG A 621 ? 0.4195 0.3442 0.2460 0.1177 -0.0428 -0.0435 662 ARG A O 5080 O O B ARG A 621 ? 0.4275 0.3524 0.2514 0.1186 -0.0382 -0.0413 662 ARG A O 5081 C CB A ARG A 621 ? 0.4344 0.3461 0.2157 0.1377 -0.0281 -0.0375 662 ARG A CB 5082 C CB B ARG A 621 ? 0.4592 0.3723 0.2409 0.1381 -0.0207 -0.0354 662 ARG A CB 5083 C CG A ARG A 621 ? 0.4412 0.3617 0.2412 0.1282 -0.0193 -0.0316 662 ARG A CG 5084 C CG B ARG A 621 ? 0.4170 0.3391 0.2181 0.1282 -0.0127 -0.0294 662 ARG A CG 5085 C CD A ARG A 621 ? 0.4089 0.3338 0.2171 0.1223 -0.0160 -0.0257 662 ARG A CD 5086 C CD B ARG A 621 ? 0.5122 0.4362 0.3146 0.1254 -0.0070 -0.0224 662 ARG A CD 5087 N NE A ARG A 621 ? 0.4462 0.3769 0.2650 0.1170 -0.0053 -0.0197 662 ARG A NE 5088 N NE B ARG A 621 ? 0.5239 0.4546 0.3392 0.1194 0.0031 -0.0166 662 ARG A NE 5089 C CZ A ARG A 621 ? 0.4406 0.3718 0.2571 0.1171 0.0041 -0.0129 662 ARG A CZ 5090 C CZ B ARG A 621 ? 0.5101 0.4431 0.3290 0.1165 0.0110 -0.0099 662 ARG A CZ 5091 N NH1 A ARG A 621 ? 0.4502 0.3761 0.2540 0.1219 0.0048 -0.0102 662 ARG A NH1 5092 N NH1 B ARG A 621 ? 0.5110 0.4402 0.3215 0.1189 0.0103 -0.0074 662 ARG A NH1 5093 N NH2 A ARG A 621 ? 0.4502 0.3871 0.2785 0.1122 0.0126 -0.0087 662 ARG A NH2 5094 N NH2 B ARG A 621 ? 0.5116 0.4506 0.3436 0.1112 0.0189 -0.0059 662 ARG A NH2 5095 N N . MET A 622 ? 0.4735 0.3882 0.2809 0.1299 -0.0472 -0.0519 663 MET A N 5096 C CA . MET A 622 ? 0.4702 0.3890 0.2964 0.1223 -0.0520 -0.0549 663 MET A CA 5097 C C . MET A 622 ? 0.4724 0.3936 0.3112 0.1166 -0.0612 -0.0574 663 MET A C 5098 O O . MET A 622 ? 0.4417 0.3693 0.2983 0.1076 -0.0605 -0.0551 663 MET A O 5099 C CB A MET A 622 ? 0.4796 0.3928 0.3013 0.1275 -0.0577 -0.0622 663 MET A CB 5100 C CB B MET A 622 ? 0.4817 0.3954 0.3032 0.1275 -0.0556 -0.0612 663 MET A CB 5101 C CG A MET A 622 ? 0.4581 0.3728 0.2976 0.1210 -0.0667 -0.0670 663 MET A CG 5102 C CG B MET A 622 ? 0.4747 0.3875 0.2859 0.1326 -0.0446 -0.0579 663 MET A CG 5103 S SD A MET A 622 ? 0.4762 0.3834 0.3113 0.1272 -0.0732 -0.0757 663 MET A SD 5104 S SD B MET A 622 ? 0.5186 0.4267 0.3249 0.1388 -0.0448 -0.0638 663 MET A SD 5105 C CE A MET A 622 ? 0.5211 0.4271 0.3402 0.1344 -0.0606 -0.0718 663 MET A CE 5106 C CE B MET A 622 ? 0.4438 0.3405 0.2276 0.1507 -0.0549 -0.0729 663 MET A CE 5107 N N . MET A 623 ? 0.4669 0.3832 0.2971 0.1221 -0.0699 -0.0623 664 MET A N 5108 C CA . MET A 623 ? 0.4680 0.3871 0.3119 0.1170 -0.0786 -0.0651 664 MET A CA 5109 C C . MET A 623 ? 0.4514 0.3766 0.3024 0.1114 -0.0733 -0.0585 664 MET A C 5110 O O . MET A 623 ? 0.4354 0.3662 0.3037 0.1036 -0.0757 -0.0582 664 MET A O 5111 C CB A MET A 623 ? 0.4904 0.4026 0.3223 0.1253 -0.0896 -0.0719 664 MET A CB 5112 C CB B MET A 623 ? 0.4795 0.3920 0.3156 0.1240 -0.0912 -0.0733 664 MET A CB 5113 C CG A MET A 623 ? 0.5499 0.4542 0.3702 0.1331 -0.0957 -0.0795 664 MET A CG 5114 C CG B MET A 623 ? 0.4895 0.3976 0.3277 0.1260 -0.0987 -0.0809 664 MET A CG 5115 S SD A MET A 623 ? 0.6037 0.5102 0.4457 0.1256 -0.1012 -0.0841 664 MET A SD 5116 S SD B MET A 623 ? 0.4924 0.3939 0.3289 0.1318 -0.1158 -0.0922 664 MET A SD 5117 C CE A MET A 623 ? 0.5848 0.4914 0.4398 0.1236 -0.1159 -0.0911 664 MET A CE 5118 C CE B MET A 623 ? 0.4239 0.3333 0.2915 0.1195 -0.1207 -0.0926 664 MET A CE 5119 N N . ASN A 624 ? 0.4459 0.3697 0.2834 0.1157 -0.0661 -0.0534 665 ASN A N 5120 C CA . ASN A 624 ? 0.4378 0.3671 0.2826 0.1102 -0.0604 -0.0470 665 ASN A CA 5121 C C . ASN A 624 ? 0.4103 0.3470 0.2710 0.1008 -0.0530 -0.0424 665 ASN A C 5122 O O . ASN A 624 ? 0.3909 0.3330 0.2638 0.0942 -0.0522 -0.0401 665 ASN A O 5123 C CB . ASN A 624 ? 0.4491 0.3745 0.2770 0.1165 -0.0534 -0.0419 665 ASN A CB 5124 C CG . ASN A 624 ? 0.4599 0.3797 0.2760 0.1236 -0.0614 -0.0448 665 ASN A CG 5125 O OD1 . ASN A 624 ? 0.4556 0.3771 0.2815 0.1215 -0.0709 -0.0493 665 ASN A OD1 5126 N ND2 . ASN A 624 ? 0.4662 0.3793 0.2617 0.1322 -0.0575 -0.0421 665 ASN A ND2 5127 N N . ASP A 625 ? 0.4126 0.3491 0.2716 0.1010 -0.0477 -0.0414 666 ASP A N 5128 C CA . ASP A 625 ? 0.4010 0.3441 0.2746 0.0928 -0.0420 -0.0377 666 ASP A CA 5129 C C . ASP A 625 ? 0.3894 0.3356 0.2789 0.0860 -0.0489 -0.0409 666 ASP A C 5130 O O . ASP A 625 ? 0.3846 0.3366 0.2864 0.0785 -0.0462 -0.0376 666 ASP A O 5131 C CB . ASP A 625 ? 0.3977 0.3398 0.2672 0.0952 -0.0359 -0.0366 666 ASP A CB 5132 C CG . ASP A 625 ? 0.4487 0.3905 0.3086 0.0988 -0.0258 -0.0310 666 ASP A CG 5133 O OD1 . ASP A 625 ? 0.4828 0.4246 0.3389 0.0992 -0.0233 -0.0277 666 ASP A OD1 5134 O OD2 . ASP A 625 ? 0.4907 0.4320 0.3475 0.1014 -0.0201 -0.0300 666 ASP A OD2 5135 N N . GLN A 626 ? 0.3801 0.3222 0.2695 0.0887 -0.0577 -0.0473 667 GLN A N 5136 C CA . GLN A 626 ? 0.3642 0.3088 0.2697 0.0822 -0.0641 -0.0501 667 GLN A CA 5137 C C . GLN A 626 ? 0.3533 0.3022 0.2673 0.0780 -0.0658 -0.0490 667 GLN A C 5138 O O . GLN A 626 ? 0.3622 0.3162 0.2904 0.0703 -0.0645 -0.0469 667 GLN A O 5139 C CB . GLN A 626 ? 0.3769 0.3157 0.2815 0.0862 -0.0738 -0.0576 667 GLN A CB 5140 C CG . GLN A 626 ? 0.3881 0.3236 0.2891 0.0884 -0.0719 -0.0587 667 GLN A CG 5141 C CD . GLN A 626 ? 0.4132 0.3423 0.3127 0.0929 -0.0816 -0.0667 667 GLN A CD 5142 O OE1 . GLN A 626 ? 0.4413 0.3646 0.3261 0.1014 -0.0855 -0.0711 667 GLN A OE1 5143 N NE2 . GLN A 626 ? 0.3953 0.3247 0.3095 0.0875 -0.0857 -0.0686 667 GLN A NE2 5144 N N . LEU A 627 ? 0.3710 0.3176 0.2758 0.0833 -0.0681 -0.0500 668 LEU A N 5145 C CA . LEU A 627 ? 0.3623 0.3133 0.2755 0.0797 -0.0692 -0.0488 668 LEU A CA 5146 C C . LEU A 627 ? 0.3564 0.3130 0.2742 0.0741 -0.0598 -0.0420 668 LEU A C 5147 O O . LEU A 627 ? 0.3512 0.3132 0.2824 0.0676 -0.0594 -0.0408 668 LEU A O 5148 C CB . LEU A 627 ? 0.3742 0.3206 0.2746 0.0878 -0.0738 -0.0510 668 LEU A CB 5149 C CG . LEU A 627 ? 0.4187 0.3608 0.3194 0.0920 -0.0859 -0.0591 668 LEU A CG 5150 C CD1 . LEU A 627 ? 0.4771 0.4142 0.3639 0.1005 -0.0912 -0.0614 668 LEU A CD1 5151 C CD2 . LEU A 627 ? 0.4193 0.3669 0.3423 0.0845 -0.0913 -0.0618 668 LEU A CD2 5152 N N . MET A 628 ? 0.3640 0.3193 0.2713 0.0767 -0.0523 -0.0377 669 MET A N 5153 C CA . MET A 628 ? 0.3762 0.3364 0.2881 0.0718 -0.0439 -0.0318 669 MET A CA 5154 C C . MET A 628 ? 0.3577 0.3229 0.2824 0.0638 -0.0411 -0.0302 669 MET A C 5155 O O . MET A 628 ? 0.3580 0.3281 0.2915 0.0580 -0.0381 -0.0275 669 MET A O 5156 C CB . MET A 628 ? 0.3963 0.3536 0.2956 0.0764 -0.0364 -0.0279 669 MET A CB 5157 C CG . MET A 628 ? 0.4648 0.4267 0.3696 0.0713 -0.0278 -0.0221 669 MET A CG 5158 S SD . MET A 628 ? 0.4826 0.4413 0.3753 0.0765 -0.0185 -0.0171 669 MET A SD 5159 C CE . MET A 628 ? 0.4434 0.4031 0.3382 0.0759 -0.0163 -0.0179 669 MET A CE 5160 N N . PHE A 629 ? 0.3420 0.3056 0.2669 0.0641 -0.0423 -0.0318 670 PHE A N 5161 C CA . PHE A 629 ? 0.3400 0.3073 0.2755 0.0573 -0.0400 -0.0299 670 PHE A CA 5162 C C . PHE A 629 ? 0.3281 0.2973 0.2759 0.0521 -0.0453 -0.0321 670 PHE A C 5163 O O . PHE A 629 ? 0.3464 0.3182 0.3023 0.0465 -0.0434 -0.0300 670 PHE A O 5164 C CB . PHE A 629 ? 0.3167 0.2815 0.2479 0.0599 -0.0384 -0.0300 670 PHE A CB 5165 C CG . PHE A 629 ? 0.3679 0.3334 0.2922 0.0624 -0.0306 -0.0261 670 PHE A CG 5166 C CD1 . PHE A 629 ? 0.3728 0.3432 0.3026 0.0575 -0.0246 -0.0215 670 PHE A CD1 5167 C CD2 . PHE A 629 ? 0.4003 0.3612 0.3131 0.0697 -0.0291 -0.0273 670 PHE A CD2 5168 C CE1 . PHE A 629 ? 0.3836 0.3547 0.3094 0.0595 -0.0174 -0.0180 670 PHE A CE1 5169 C CE2 . PHE A 629 ? 0.4510 0.4129 0.3591 0.0718 -0.0211 -0.0233 670 PHE A CE2 5170 C CZ . PHE A 629 ? 0.4289 0.3959 0.3443 0.0666 -0.0153 -0.0186 670 PHE A CZ 5171 N N . LEU A 630 ? 0.3328 0.3007 0.2826 0.0538 -0.0516 -0.0360 671 LEU A N 5172 C CA . LEU A 630 ? 0.3310 0.3009 0.2946 0.0487 -0.0562 -0.0381 671 LEU A CA 5173 C C . LEU A 630 ? 0.3185 0.2946 0.2915 0.0418 -0.0511 -0.0341 671 LEU A C 5174 O O . LEU A 630 ? 0.3004 0.2785 0.2823 0.0362 -0.0499 -0.0325 671 LEU A O 5175 C CB . LEU A 630 ? 0.3400 0.3078 0.3058 0.0522 -0.0646 -0.0437 671 LEU A CB 5176 C CG . LEU A 630 ? 0.3436 0.3139 0.3263 0.0467 -0.0690 -0.0458 671 LEU A CG 5177 C CD1 . LEU A 630 ? 0.3690 0.3373 0.3583 0.0431 -0.0699 -0.0459 671 LEU A CD1 5178 C CD2 . LEU A 630 ? 0.3716 0.3395 0.3562 0.0512 -0.0784 -0.0522 671 LEU A CD2 5179 N N . GLU A 631 ? 0.2992 0.2777 0.2693 0.0426 -0.0480 -0.0324 672 GLU A N 5180 C CA . GLU A 631 ? 0.2941 0.2780 0.2712 0.0367 -0.0425 -0.0289 672 GLU A CA 5181 C C . GLU A 631 ? 0.2750 0.2600 0.2508 0.0332 -0.0370 -0.0250 672 GLU A C 5182 O O . GLU A 631 ? 0.2923 0.2806 0.2754 0.0275 -0.0344 -0.0228 672 GLU A O 5183 C CB . GLU A 631 ? 0.2785 0.2638 0.2513 0.0389 -0.0398 -0.0276 672 GLU A CB 5184 C CG . GLU A 631 ? 0.2793 0.2700 0.2612 0.0334 -0.0360 -0.0258 672 GLU A CG 5185 C CD . GLU A 631 ? 0.3572 0.3503 0.3505 0.0319 -0.0406 -0.0290 672 GLU A CD 5186 O OE1 . GLU A 631 ? 0.3378 0.3297 0.3303 0.0362 -0.0453 -0.0319 672 GLU A OE1 5187 O OE2 . GLU A 631 ? 0.3307 0.3268 0.3340 0.0264 -0.0395 -0.0285 672 GLU A OE2 5188 N N . ARG A 632 ? 0.2886 0.2708 0.2553 0.0369 -0.0352 -0.0240 673 ARG A N 5189 C CA . ARG A 632 ? 0.2946 0.2781 0.2608 0.0343 -0.0305 -0.0206 673 ARG A CA 5190 C C . ARG A 632 ? 0.2907 0.2736 0.2631 0.0307 -0.0328 -0.0207 673 ARG A C 5191 O O . ARG A 632 ? 0.2983 0.2832 0.2734 0.0267 -0.0299 -0.0178 673 ARG A O 5192 C CB . ARG A 632 ? 0.3176 0.2984 0.2746 0.0395 -0.0283 -0.0200 673 ARG A CB 5193 C CG . ARG A 632 ? 0.3495 0.3330 0.3064 0.0374 -0.0222 -0.0162 673 ARG A CG 5194 C CD . ARG A 632 ? 0.3485 0.3336 0.3034 0.0379 -0.0183 -0.0145 673 ARG A CD 5195 N NE . ARG A 632 ? 0.3013 0.2831 0.2473 0.0440 -0.0165 -0.0143 673 ARG A NE 5196 C CZ . ARG A 632 ? 0.3104 0.2896 0.2508 0.0480 -0.0182 -0.0154 673 ARG A CZ 5197 N NH1 . ARG A 632 ? 0.3107 0.2909 0.2553 0.0466 -0.0224 -0.0176 673 ARG A NH1 5198 N NH2 . ARG A 632 ? 0.3563 0.3318 0.2870 0.0539 -0.0157 -0.0144 673 ARG A NH2 5199 N N . ALA A 633 ? 0.2902 0.2699 0.2648 0.0323 -0.0384 -0.0241 674 ALA A N 5200 C CA . ALA A 633 ? 0.2924 0.2704 0.2732 0.0293 -0.0408 -0.0240 674 ALA A CA 5201 C C . ALA A 633 ? 0.2962 0.2773 0.2863 0.0227 -0.0391 -0.0216 674 ALA A C 5202 O O . ALA A 633 ? 0.2947 0.2746 0.2890 0.0194 -0.0392 -0.0197 674 ALA A O 5203 C CB . ALA A 633 ? 0.3030 0.2763 0.2849 0.0328 -0.0477 -0.0289 674 ALA A CB 5204 N N . PHE A 634 ? 0.2785 0.2634 0.2718 0.0209 -0.0374 -0.0215 675 PHE A N 5205 C CA . PHE A 634 ? 0.2774 0.2656 0.2787 0.0151 -0.0346 -0.0190 675 PHE A CA 5206 C C . PHE A 634 ? 0.2776 0.2683 0.2752 0.0121 -0.0289 -0.0148 675 PHE A C 5207 O O . PHE A 634 ? 0.2868 0.2795 0.2889 0.0077 -0.0261 -0.0126 675 PHE A O 5208 C CB . PHE A 634 ? 0.2738 0.2652 0.2814 0.0145 -0.0351 -0.0210 675 PHE A CB 5209 C CG . PHE A 634 ? 0.2921 0.2816 0.3070 0.0162 -0.0417 -0.0253 675 PHE A CG 5210 C CD1 . PHE A 634 ? 0.2747 0.2623 0.2989 0.0130 -0.0442 -0.0255 675 PHE A CD1 5211 C CD2 . PHE A 634 ? 0.3190 0.3079 0.3311 0.0211 -0.0458 -0.0291 675 PHE A CD2 5212 C CE1 . PHE A 634 ? 0.2682 0.2538 0.3006 0.0146 -0.0512 -0.0302 675 PHE A CE1 5213 C CE2 . PHE A 634 ? 0.3270 0.3138 0.3457 0.0232 -0.0531 -0.0339 675 PHE A CE2 5214 C CZ . PHE A 634 ? 0.3093 0.2948 0.3389 0.0197 -0.0559 -0.0347 675 PHE A CZ 5215 N N . ILE A 635 ? 0.2829 0.2731 0.2726 0.0147 -0.0273 -0.0140 676 ILE A N 5216 C CA . ILE A 635 ? 0.2851 0.2774 0.2714 0.0124 -0.0229 -0.0108 676 ILE A CA 5217 C C . ILE A 635 ? 0.2960 0.2861 0.2825 0.0105 -0.0237 -0.0085 676 ILE A C 5218 O O . ILE A 635 ? 0.3238 0.3105 0.3093 0.0130 -0.0267 -0.0093 676 ILE A O 5219 C CB . ILE A 635 ? 0.2733 0.2660 0.2534 0.0161 -0.0212 -0.0110 676 ILE A CB 5220 C CG1 . ILE A 635 ? 0.2958 0.2900 0.2754 0.0180 -0.0203 -0.0127 676 ILE A CG1 5221 C CG2 . ILE A 635 ? 0.2671 0.2616 0.2452 0.0141 -0.0180 -0.0084 676 ILE A CG2 5222 C CD1 . ILE A 635 ? 0.2989 0.2969 0.2825 0.0142 -0.0174 -0.0120 676 ILE A CD1 5223 N N . ASP A 636 ? 0.2903 0.2816 0.2774 0.0065 -0.0212 -0.0056 677 ASP A N 5224 C CA . ASP A 636 ? 0.2909 0.2799 0.2760 0.0050 -0.0217 -0.0027 677 ASP A CA 5225 C C . ASP A 636 ? 0.2947 0.2858 0.2747 0.0055 -0.0198 -0.0016 677 ASP A C 5226 O O . ASP A 636 ? 0.2887 0.2827 0.2671 0.0039 -0.0168 -0.0014 677 ASP A O 5227 C CB . ASP A 636 ? 0.2929 0.2816 0.2805 0.0006 -0.0198 0.0000 677 ASP A CB 5228 C CG . ASP A 636 ? 0.3313 0.3161 0.3166 -0.0005 -0.0209 0.0036 677 ASP A CG 5229 O OD1 . ASP A 636 ? 0.3216 0.3056 0.3027 0.0015 -0.0224 0.0040 677 ASP A OD1 5230 O OD2 . ASP A 636 ? 0.3518 0.3344 0.3403 -0.0034 -0.0201 0.0060 677 ASP A OD2 5231 N N . PRO A 637 ? 0.3104 0.3002 0.2886 0.0079 -0.0216 -0.0015 678 PRO A N 5232 C CA . PRO A 637 ? 0.3497 0.3420 0.3255 0.0085 -0.0202 -0.0010 678 PRO A CA 5233 C C . PRO A 637 ? 0.3575 0.3501 0.3305 0.0053 -0.0197 0.0014 678 PRO A C 5234 O O . PRO A 637 ? 0.4002 0.3952 0.3715 0.0050 -0.0188 0.0012 678 PRO A O 5235 C CB . PRO A 637 ? 0.3477 0.3383 0.3241 0.0118 -0.0225 -0.0012 678 PRO A CB 5236 C CG . PRO A 637 ? 0.3599 0.3464 0.3378 0.0122 -0.0255 -0.0011 678 PRO A CG 5237 C CD . PRO A 637 ? 0.3317 0.3176 0.3114 0.0102 -0.0250 -0.0020 678 PRO A CD 5238 N N . LEU A 638 ? 0.3216 0.3115 0.2939 0.0029 -0.0201 0.0036 679 LEU A N 5239 C CA . LEU A 638 ? 0.3290 0.3184 0.2962 0.0005 -0.0192 0.0063 679 LEU A CA 5240 C C . LEU A 638 ? 0.3366 0.3286 0.3023 -0.0018 -0.0152 0.0058 679 LEU A C 5241 O O . LEU A 638 ? 0.3274 0.3192 0.2875 -0.0033 -0.0138 0.0074 679 LEU A O 5242 C CB . LEU A 638 ? 0.3314 0.3159 0.2976 -0.0006 -0.0209 0.0099 679 LEU A CB 5243 C CG . LEU A 638 ? 0.3492 0.3307 0.3165 0.0019 -0.0252 0.0104 679 LEU A CG 5244 C CD1 . LEU A 638 ? 0.3882 0.3639 0.3548 0.0007 -0.0269 0.0143 679 LEU A CD1 5245 C CD2 . LEU A 638 ? 0.3819 0.3654 0.3464 0.0037 -0.0272 0.0099 679 LEU A CD2 5246 N N . GLY A 639 ? 0.3194 0.3136 0.2897 -0.0015 -0.0134 0.0034 680 GLY A N 5247 C CA . GLY A 639 ? 0.3233 0.3204 0.2938 -0.0033 -0.0095 0.0026 680 GLY A CA 5248 C C . GLY A 639 ? 0.3492 0.3450 0.3203 -0.0062 -0.0070 0.0052 680 GLY A C 5249 O O . GLY A 639 ? 0.3646 0.3569 0.3359 -0.0071 -0.0082 0.0080 680 GLY A O 5250 N N . LEU A 640 ? 0.3396 0.3382 0.3115 -0.0077 -0.0029 0.0044 681 LEU A N 5251 C CA . LEU A 640 ? 0.3621 0.3601 0.3342 -0.0105 0.0010 0.0073 681 LEU A CA 5252 C C . LEU A 640 ? 0.3746 0.3707 0.3358 -0.0112 0.0030 0.0098 681 LEU A C 5253 O O . LEU A 640 ? 0.3784 0.3750 0.3332 -0.0097 0.0014 0.0081 681 LEU A O 5254 C CB . LEU A 640 ? 0.3487 0.3510 0.3279 -0.0114 0.0049 0.0050 681 LEU A CB 5255 C CG . LEU A 640 ? 0.3532 0.3565 0.3431 -0.0105 0.0019 0.0027 681 LEU A CG 5256 C CD1 . LEU A 640 ? 0.4231 0.4309 0.4190 -0.0100 0.0039 -0.0005 681 LEU A CD1 5257 C CD2 . LEU A 640 ? 0.4032 0.4040 0.4007 -0.0127 0.0012 0.0051 681 LEU A CD2 5258 N N . PRO A 641 ? 0.4103 0.4039 0.3689 -0.0134 0.0066 0.0140 682 PRO A N 5259 C CA . PRO A 641 ? 0.4335 0.4242 0.3793 -0.0134 0.0082 0.0168 682 PRO A CA 5260 C C . PRO A 641 ? 0.4366 0.4302 0.3758 -0.0123 0.0103 0.0134 682 PRO A C 5261 O O . PRO A 641 ? 0.4453 0.4424 0.3882 -0.0131 0.0149 0.0116 682 PRO A O 5262 C CB . PRO A 641 ? 0.4537 0.4422 0.4002 -0.0160 0.0140 0.0217 682 PRO A CB 5263 C CG . PRO A 641 ? 0.4439 0.4314 0.4024 -0.0171 0.0115 0.0224 682 PRO A CG 5264 C CD . PRO A 641 ? 0.4170 0.4093 0.3843 -0.0157 0.0086 0.0167 682 PRO A CD 5265 N N . ASP A 642 ? 0.4527 0.4448 0.3832 -0.0105 0.0063 0.0124 683 ASP A N 5266 C CA . ASP A 642 ? 0.4643 0.4584 0.3887 -0.0092 0.0066 0.0085 683 ASP A CA 5267 C C . ASP A 642 ? 0.4364 0.4352 0.3696 -0.0088 0.0071 0.0037 683 ASP A C 5268 O O . ASP A 642 ? 0.4246 0.4249 0.3543 -0.0081 0.0082 0.0003 683 ASP A O 5269 C CB . ASP A 642 ? 0.5106 0.5035 0.4251 -0.0096 0.0122 0.0097 683 ASP A CB 5270 C CG . ASP A 642 ? 0.5962 0.5834 0.4995 -0.0096 0.0122 0.0150 683 ASP A CG 5271 O OD1 . ASP A 642 ? 0.6365 0.6207 0.5334 -0.0079 0.0061 0.0153 683 ASP A OD1 5272 O OD2 . ASP A 642 ? 0.6854 0.6713 0.5875 -0.0111 0.0183 0.0190 683 ASP A OD2 5273 N N . ARG A 643 ? 0.3906 0.3910 0.3345 -0.0090 0.0060 0.0034 684 ARG A N 5274 C CA . ARG A 643 ? 0.3548 0.3589 0.3061 -0.0080 0.0058 -0.0005 684 ARG A CA 5275 C C . ARG A 643 ? 0.3335 0.3372 0.2900 -0.0065 0.0012 -0.0009 684 ARG A C 5276 O O . ARG A 643 ? 0.3096 0.3140 0.2732 -0.0062 0.0008 -0.0010 684 ARG A O 5277 C CB . ARG A 643 ? 0.3565 0.3634 0.3154 -0.0089 0.0101 -0.0012 684 ARG A CB 5278 C CG . ARG A 643 ? 0.3526 0.3604 0.3066 -0.0100 0.0160 -0.0011 684 ARG A CG 5279 C CD . ARG A 643 ? 0.4107 0.4226 0.3742 -0.0106 0.0204 -0.0026 684 ARG A CD 5280 N NE . ARG A 643 ? 0.3562 0.3685 0.3293 -0.0121 0.0203 -0.0004 684 ARG A NE 5281 C CZ . ARG A 643 ? 0.4232 0.4391 0.4077 -0.0124 0.0220 -0.0019 684 ARG A CZ 5282 N NH1 . ARG A 643 ? 0.3578 0.3772 0.3458 -0.0112 0.0243 -0.0054 684 ARG A NH1 5283 N NH2 . ARG A 643 ? 0.4001 0.4159 0.3936 -0.0138 0.0210 0.0000 684 ARG A NH2 5284 N N . PRO A 644 ? 0.3356 0.3384 0.2888 -0.0054 -0.0022 -0.0014 685 PRO A N 5285 C CA . PRO A 644 ? 0.3389 0.3412 0.2964 -0.0038 -0.0059 -0.0013 685 PRO A CA 5286 C C . PRO A 644 ? 0.3184 0.3228 0.2825 -0.0022 -0.0054 -0.0036 685 PRO A C 5287 O O . PRO A 644 ? 0.3062 0.3098 0.2736 -0.0006 -0.0074 -0.0033 685 PRO A O 5288 C CB . PRO A 644 ? 0.3587 0.3604 0.3123 -0.0030 -0.0091 -0.0019 685 PRO A CB 5289 C CG . PRO A 644 ? 0.3738 0.3763 0.3221 -0.0038 -0.0073 -0.0040 685 PRO A CG 5290 C CD . PRO A 644 ? 0.3489 0.3508 0.2940 -0.0053 -0.0032 -0.0023 685 PRO A CD 5291 N N . PHE A 645 ? 0.2886 0.2950 0.2540 -0.0024 -0.0026 -0.0059 686 PHE A N 5292 C CA . PHE A 645 ? 0.2808 0.2884 0.2513 -0.0005 -0.0021 -0.0075 686 PHE A CA 5293 C C . PHE A 645 ? 0.2752 0.2834 0.2497 -0.0003 -0.0009 -0.0078 686 PHE A C 5294 O O . PHE A 645 ? 0.2751 0.2837 0.2528 0.0016 -0.0010 -0.0090 686 PHE A O 5295 C CB . PHE A 645 ? 0.2865 0.2953 0.2575 -0.0003 -0.0007 -0.0099 686 PHE A CB 5296 C CG . PHE A 645 ? 0.2939 0.3023 0.2634 -0.0004 -0.0027 -0.0102 686 PHE A CG 5297 C CD1 . PHE A 645 ? 0.3085 0.3165 0.2809 0.0010 -0.0047 -0.0092 686 PHE A CD1 5298 C CD2 . PHE A 645 ? 0.3310 0.3394 0.2964 -0.0017 -0.0030 -0.0118 686 PHE A CD2 5299 C CE1 . PHE A 645 ? 0.3031 0.3115 0.2763 0.0008 -0.0069 -0.0097 686 PHE A CE1 5300 C CE2 . PHE A 645 ? 0.3307 0.3388 0.2956 -0.0017 -0.0060 -0.0126 686 PHE A CE2 5301 C CZ . PHE A 645 ? 0.3142 0.3227 0.2841 -0.0006 -0.0080 -0.0115 686 PHE A CZ 5302 N N . TYR A 646 ? 0.2646 0.2728 0.2393 -0.0022 0.0000 -0.0065 687 TYR A N 5303 C CA . TYR A 646 ? 0.2751 0.2841 0.2560 -0.0021 0.0000 -0.0068 687 TYR A CA 5304 C C . TYR A 646 ? 0.2811 0.2874 0.2628 -0.0020 -0.0030 -0.0050 687 TYR A C 5305 O O . TYR A 646 ? 0.3115 0.3163 0.2916 -0.0041 -0.0026 -0.0026 687 TYR A O 5306 C CB . TYR A 646 ? 0.2959 0.3069 0.2791 -0.0045 0.0038 -0.0066 687 TYR A CB 5307 C CG . TYR A 646 ? 0.2792 0.2928 0.2628 -0.0040 0.0069 -0.0091 687 TYR A CG 5308 C CD1 . TYR A 646 ? 0.3011 0.3151 0.2864 -0.0015 0.0057 -0.0113 687 TYR A CD1 5309 C CD2 . TYR A 646 ? 0.3137 0.3289 0.2962 -0.0058 0.0114 -0.0090 687 TYR A CD2 5310 C CE1 . TYR A 646 ? 0.3080 0.3238 0.2943 -0.0010 0.0083 -0.0137 687 TYR A CE1 5311 C CE2 . TYR A 646 ? 0.3243 0.3417 0.3075 -0.0051 0.0142 -0.0119 687 TYR A CE2 5312 C CZ . TYR A 646 ? 0.3358 0.3534 0.3214 -0.0027 0.0123 -0.0142 687 TYR A CZ 5313 O OH . TYR A 646 ? 0.3495 0.3687 0.3365 -0.0019 0.0149 -0.0170 687 TYR A OH 5314 N N . ARG A 647 ? 0.2480 0.2532 0.2319 0.0006 -0.0061 -0.0062 688 ARG A N 5315 C CA . ARG A 647 ? 0.2527 0.2547 0.2363 0.0013 -0.0095 -0.0050 688 ARG A CA 5316 C C . ARG A 647 ? 0.2616 0.2627 0.2512 0.0021 -0.0120 -0.0064 688 ARG A C 5317 O O . ARG A 647 ? 0.2652 0.2633 0.2557 0.0027 -0.0151 -0.0060 688 ARG A O 5318 C CB A ARG A 647 ? 0.2520 0.2530 0.2323 0.0044 -0.0111 -0.0055 688 ARG A CB 5319 C CB B ARG A 647 ? 0.2632 0.2642 0.2436 0.0045 -0.0111 -0.0057 688 ARG A CB 5320 C CG A ARG A 647 ? 0.2277 0.2299 0.2041 0.0034 -0.0094 -0.0046 688 ARG A CG 5321 C CG B ARG A 647 ? 0.3109 0.3135 0.2879 0.0041 -0.0091 -0.0052 688 ARG A CG 5322 C CD A ARG A 647 ? 0.2399 0.2411 0.2150 0.0056 -0.0110 -0.0043 688 ARG A CD 5323 C CD B ARG A 647 ? 0.3994 0.4005 0.3739 0.0041 -0.0109 -0.0036 688 ARG A CD 5324 N NE A ARG A 647 ? 0.1924 0.1934 0.1683 0.0090 -0.0108 -0.0057 688 ARG A NE 5325 N NE B ARG A 647 ? 0.4374 0.4398 0.4117 0.0056 -0.0102 -0.0043 688 ARG A NE 5326 C CZ A ARG A 647 ? 0.2834 0.2835 0.2590 0.0118 -0.0115 -0.0055 688 ARG A CZ 5327 C CZ B ARG A 647 ? 0.4758 0.4777 0.4513 0.0088 -0.0104 -0.0049 688 ARG A CZ 5328 N NH1 A ARG A 647 ? 0.2041 0.2034 0.1788 0.0153 -0.0106 -0.0064 688 ARG A NH1 5329 N NH1 B ARG A 647 ? 0.4644 0.4677 0.4411 0.0098 -0.0089 -0.0051 688 ARG A NH1 5330 N NH2 A ARG A 647 ? 0.2236 0.2233 0.1993 0.0115 -0.0130 -0.0043 688 ARG A NH2 5331 N NH2 B ARG A 647 ? 0.5047 0.5046 0.4803 0.0109 -0.0119 -0.0054 688 ARG A NH2 5332 N N . HIS A 648 ? 0.2508 0.2543 0.2449 0.0025 -0.0114 -0.0085 689 HIS A N 5333 C CA . HIS A 648 ? 0.2551 0.2578 0.2558 0.0039 -0.0151 -0.0108 689 HIS A CA 5334 C C . HIS A 648 ? 0.2609 0.2639 0.2688 -0.0001 -0.0141 -0.0092 689 HIS A C 5335 O O . HIS A 648 ? 0.2933 0.2991 0.3035 -0.0030 -0.0098 -0.0079 689 HIS A O 5336 C CB . HIS A 648 ? 0.2616 0.2670 0.2656 0.0057 -0.0151 -0.0134 689 HIS A CB 5337 C CG . HIS A 648 ? 0.2810 0.2849 0.2891 0.0089 -0.0204 -0.0166 689 HIS A CG 5338 N ND1 . HIS A 648 ? 0.2521 0.2560 0.2695 0.0073 -0.0233 -0.0179 689 HIS A ND1 5339 C CD2 . HIS A 648 ? 0.2693 0.2714 0.2730 0.0138 -0.0236 -0.0188 689 HIS A CD2 5340 C CE1 . HIS A 648 ? 0.2987 0.3010 0.3175 0.0112 -0.0289 -0.0214 689 HIS A CE1 5341 N NE2 . HIS A 648 ? 0.2931 0.2940 0.3025 0.0155 -0.0291 -0.0219 689 HIS A NE2 5342 N N . VAL A 649 ? 0.2506 0.2505 0.2625 -0.0002 -0.0178 -0.0094 690 VAL A N 5343 C CA . VAL A 649 ? 0.2609 0.2601 0.2799 -0.0043 -0.0164 -0.0070 690 VAL A CA 5344 C C . VAL A 649 ? 0.2765 0.2788 0.3081 -0.0058 -0.0166 -0.0091 690 VAL A C 5345 O O . VAL A 649 ? 0.2665 0.2699 0.3059 -0.0098 -0.0133 -0.0068 690 VAL A O 5346 C CB . VAL A 649 ? 0.2840 0.2777 0.3029 -0.0038 -0.0207 -0.0064 690 VAL A CB 5347 C CG1 . VAL A 649 ? 0.2760 0.2678 0.3045 -0.0079 -0.0201 -0.0039 690 VAL A CG1 5348 C CG2 . VAL A 649 ? 0.2617 0.2531 0.2701 -0.0029 -0.0200 -0.0038 690 VAL A CG2 5349 N N . ILE A 650 ? 0.2621 0.2658 0.2965 -0.0024 -0.0205 -0.0134 691 ILE A N 5350 C CA . ILE A 650 ? 0.2721 0.2792 0.3199 -0.0034 -0.0216 -0.0159 691 ILE A CA 5351 C C . ILE A 650 ? 0.2689 0.2814 0.3185 -0.0044 -0.0163 -0.0157 691 ILE A C 5352 O O . ILE A 650 ? 0.2874 0.3037 0.3486 -0.0072 -0.0136 -0.0156 691 ILE A O 5353 C CB . ILE A 650 ? 0.2674 0.2732 0.3178 0.0011 -0.0294 -0.0212 691 ILE A CB 5354 C CG1 . ILE A 650 ? 0.2724 0.2723 0.3186 0.0030 -0.0346 -0.0220 691 ILE A CG1 5355 C CG2 . ILE A 650 ? 0.2912 0.3006 0.3585 0.0000 -0.0322 -0.0244 691 ILE A CG2 5356 C CD1 . ILE A 650 ? 0.2830 0.2802 0.3373 -0.0013 -0.0344 -0.0197 691 ILE A CD1 5357 N N . TYR A 651 ? 0.2788 0.2918 0.3181 -0.0019 -0.0147 -0.0158 692 TYR A N 5358 C CA . TYR A 651 ? 0.2995 0.3170 0.3401 -0.0019 -0.0105 -0.0164 692 TYR A CA 5359 C C . TYR A 651 ? 0.3225 0.3398 0.3523 -0.0030 -0.0052 -0.0136 692 TYR A C 5360 O O . TYR A 651 ? 0.3616 0.3756 0.3817 -0.0016 -0.0064 -0.0126 692 TYR A O 5361 C CB . TYR A 651 ? 0.2776 0.2954 0.3170 0.0029 -0.0147 -0.0200 692 TYR A CB 5362 C CG . TYR A 651 ? 0.3092 0.3274 0.3588 0.0049 -0.0210 -0.0237 692 TYR A CG 5363 C CD1 . TYR A 651 ? 0.3062 0.3292 0.3709 0.0028 -0.0203 -0.0252 692 TYR A CD1 5364 C CD2 . TYR A 651 ? 0.3187 0.3327 0.3630 0.0094 -0.0278 -0.0261 692 TYR A CD2 5365 C CE1 . TYR A 651 ? 0.2963 0.3201 0.3718 0.0048 -0.0271 -0.0292 692 TYR A CE1 5366 C CE2 . TYR A 651 ? 0.2958 0.3097 0.3485 0.0119 -0.0348 -0.0302 692 TYR A CE2 5367 C CZ . TYR A 651 ? 0.3177 0.3367 0.3864 0.0095 -0.0348 -0.0319 692 TYR A CZ 5368 O OH . TYR A 651 ? 0.3339 0.3534 0.4129 0.0118 -0.0423 -0.0365 692 TYR A OH 5369 N N . ALA A 652 ? 0.3367 0.3574 0.3685 -0.0053 0.0005 -0.0128 693 ALA A N 5370 C CA . ALA A 652 ? 0.3385 0.3591 0.3599 -0.0052 0.0044 -0.0118 693 ALA A CA 5371 C C . ALA A 652 ? 0.3395 0.3646 0.3660 -0.0056 0.0091 -0.0133 693 ALA A C 5372 O O . ALA A 652 ? 0.3371 0.3657 0.3751 -0.0070 0.0106 -0.0140 693 ALA A O 5373 C CB . ALA A 652 ? 0.3498 0.3680 0.3640 -0.0079 0.0072 -0.0081 693 ALA A CB 5374 N N . PRO A 653 ? 0.3392 0.3644 0.3587 -0.0044 0.0112 -0.0142 694 PRO A N 5375 C CA . PRO A 653 ? 0.3360 0.3651 0.3594 -0.0047 0.0164 -0.0158 694 PRO A CA 5376 C C . PRO A 653 ? 0.3440 0.3745 0.3680 -0.0082 0.0222 -0.0133 694 PRO A C 5377 O O . PRO A 653 ? 0.3412 0.3685 0.3571 -0.0099 0.0227 -0.0102 694 PRO A O 5378 C CB . PRO A 653 ? 0.3317 0.3591 0.3452 -0.0032 0.0173 -0.0169 694 PRO A CB 5379 C CG . PRO A 653 ? 0.3184 0.3421 0.3269 -0.0013 0.0120 -0.0165 694 PRO A CG 5380 C CD . PRO A 653 ? 0.3327 0.3546 0.3413 -0.0029 0.0096 -0.0139 694 PRO A CD 5381 N N . SER A 654 ? 0.3364 0.3715 0.3709 -0.0090 0.0264 -0.0144 695 SER A N 5382 C CA . SER A 654 ? 0.3411 0.3778 0.3770 -0.0121 0.0333 -0.0116 695 SER A CA 5383 C C . SER A 654 ? 0.3659 0.4002 0.3865 -0.0122 0.0378 -0.0105 695 SER A C 5384 O O . SER A 654 ? 0.3554 0.3898 0.3707 -0.0100 0.0380 -0.0135 695 SER A O 5385 C CB . SER A 654 ? 0.3355 0.3785 0.3859 -0.0123 0.0380 -0.0136 695 SER A CB 5386 O OG . SER A 654 ? 0.3450 0.3893 0.3941 -0.0149 0.0466 -0.0107 695 SER A OG 5387 N N . SER A 655 ? 0.3692 0.4005 0.3825 -0.0144 0.0406 -0.0062 696 SER A N 5388 C CA A SER A 655 ? 0.3635 0.3922 0.3615 -0.0142 0.0446 -0.0051 696 SER A CA 5389 C CA B SER A 655 ? 0.3973 0.4260 0.3956 -0.0144 0.0449 -0.0048 696 SER A CA 5390 C C . SER A 655 ? 0.3859 0.4182 0.3844 -0.0136 0.0523 -0.0071 696 SER A C 5391 O O . SER A 655 ? 0.4128 0.4430 0.3981 -0.0124 0.0549 -0.0079 696 SER A O 5392 C CB A SER A 655 ? 0.3590 0.3834 0.3493 -0.0164 0.0463 0.0003 696 SER A CB 5393 C CB B SER A 655 ? 0.3986 0.4240 0.3922 -0.0170 0.0478 0.0008 696 SER A CB 5394 O OG A SER A 655 ? 0.2155 0.2360 0.2033 -0.0164 0.0391 0.0016 696 SER A OG 5395 O OG B SER A 655 ? 0.4697 0.4908 0.4459 -0.0161 0.0487 0.0021 696 SER A OG 5396 N N . HIS A 656 ? 0.3882 0.4259 0.4020 -0.0141 0.0555 -0.0083 697 HIS A N 5397 C CA . HIS A 656 ? 0.4055 0.4473 0.4215 -0.0132 0.0634 -0.0105 697 HIS A CA 5398 C C . HIS A 656 ? 0.4032 0.4484 0.4267 -0.0104 0.0609 -0.0160 697 HIS A C 5399 O O . HIS A 656 ? 0.4006 0.4490 0.4258 -0.0090 0.0666 -0.0187 697 HIS A O 5400 C CB . HIS A 656 ? 0.4164 0.4625 0.4459 -0.0159 0.0706 -0.0075 697 HIS A CB 5401 C CG . HIS A 656 ? 0.4643 0.5063 0.4872 -0.0187 0.0732 -0.0013 697 HIS A CG 5402 N ND1 . HIS A 656 ? 0.5206 0.5590 0.5271 -0.0186 0.0796 0.0017 697 HIS A ND1 5403 C CD2 . HIS A 656 ? 0.5355 0.5750 0.5635 -0.0211 0.0692 0.0022 697 HIS A CD2 5404 C CE1 . HIS A 656 ? 0.5790 0.6131 0.5817 -0.0210 0.0799 0.0075 697 HIS A CE1 5405 N NE2 . HIS A 656 ? 0.5459 0.5807 0.5621 -0.0228 0.0737 0.0079 697 HIS A NE2 5406 N N . ASN A 657 ? 0.3749 0.4192 0.4029 -0.0093 0.0527 -0.0176 698 ASN A N 5407 C CA . ASN A 657 ? 0.3670 0.4139 0.4030 -0.0063 0.0499 -0.0222 698 ASN A CA 5408 C C . ASN A 657 ? 0.3579 0.4013 0.3917 -0.0050 0.0411 -0.0226 698 ASN A C 5409 O O . ASN A 657 ? 0.3546 0.3988 0.3973 -0.0051 0.0366 -0.0220 698 ASN A O 5410 C CB . ASN A 657 ? 0.3651 0.4186 0.4205 -0.0064 0.0518 -0.0236 698 ASN A CB 5411 C CG . ASN A 657 ? 0.3623 0.4177 0.4257 -0.0028 0.0476 -0.0281 698 ASN A CG 5412 O OD1 . ASN A 657 ? 0.3482 0.4002 0.4028 -0.0005 0.0451 -0.0300 698 ASN A OD1 5413 N ND2 . ASN A 657 ? 0.3107 0.3714 0.3916 -0.0023 0.0466 -0.0296 698 ASN A ND2 5414 N N . LYS A 658 ? 0.3582 0.3976 0.3807 -0.0034 0.0387 -0.0238 699 LYS A N 5415 C CA . LYS A 658 ? 0.3607 0.3965 0.3801 -0.0021 0.0316 -0.0236 699 LYS A CA 5416 C C . LYS A 658 ? 0.3464 0.3837 0.3765 0.0003 0.0271 -0.0253 699 LYS A C 5417 O O . LYS A 658 ? 0.3246 0.3592 0.3536 0.0012 0.0216 -0.0243 699 LYS A O 5418 C CB . LYS A 658 ? 0.3883 0.4205 0.3972 -0.0008 0.0311 -0.0253 699 LYS A CB 5419 C CG . LYS A 658 ? 0.4502 0.4793 0.4577 0.0010 0.0256 -0.0256 699 LYS A CG 5420 C CD . LYS A 658 ? 0.4657 0.4915 0.4640 0.0014 0.0256 -0.0270 699 LYS A CD 5421 C CE . LYS A 658 ? 0.5124 0.5346 0.5068 0.0018 0.0207 -0.0252 699 LYS A CE 5422 N NZ . LYS A 658 ? 0.5496 0.5689 0.5379 0.0018 0.0201 -0.0267 699 LYS A NZ 5423 N N . TYR A 659 ? 0.3299 0.3710 0.3694 0.0018 0.0292 -0.0281 700 TYR A N 5424 C CA . TYR A 659 ? 0.3387 0.3810 0.3880 0.0048 0.0243 -0.0299 700 TYR A CA 5425 C C . TYR A 659 ? 0.3423 0.3866 0.4011 0.0039 0.0207 -0.0289 700 TYR A C 5426 O O . TYR A 659 ? 0.3480 0.3913 0.4103 0.0066 0.0145 -0.0300 700 TYR A O 5427 C CB . TYR A 659 ? 0.3325 0.3791 0.3915 0.0067 0.0274 -0.0332 700 TYR A CB 5428 C CG . TYR A 659 ? 0.3595 0.4038 0.4120 0.0086 0.0297 -0.0354 700 TYR A CG 5429 C CD1 . TYR A 659 ? 0.3750 0.4137 0.4182 0.0101 0.0260 -0.0349 700 TYR A CD1 5430 C CD2 . TYR A 659 ? 0.3615 0.4095 0.4187 0.0090 0.0357 -0.0381 700 TYR A CD2 5431 C CE1 . TYR A 659 ? 0.3988 0.4350 0.4378 0.0117 0.0279 -0.0373 700 TYR A CE1 5432 C CE2 . TYR A 659 ? 0.3867 0.4323 0.4388 0.0110 0.0375 -0.0408 700 TYR A CE2 5433 C CZ . TYR A 659 ? 0.4076 0.4471 0.4511 0.0122 0.0332 -0.0404 700 TYR A CZ 5434 O OH . TYR A 659 ? 0.3971 0.4338 0.4372 0.0139 0.0346 -0.0433 700 TYR A OH 5435 N N . ALA A 660 ? 0.3343 0.3813 0.3976 0.0003 0.0246 -0.0271 701 ALA A N 5436 C CA . ALA A 660 ? 0.3427 0.3920 0.4180 -0.0010 0.0217 -0.0266 701 ALA A CA 5437 C C . ALA A 660 ? 0.3553 0.3996 0.4228 -0.0021 0.0171 -0.0239 701 ALA A C 5438 O O . ALA A 660 ? 0.3614 0.4025 0.4175 -0.0040 0.0197 -0.0212 701 ALA A O 5439 C CB . ALA A 660 ? 0.3537 0.4080 0.4389 -0.0045 0.0290 -0.0253 701 ALA A CB 5440 N N . GLY A 661 ? 0.3457 0.3891 0.4193 -0.0007 0.0101 -0.0250 702 GLY A N 5441 C CA . GLY A 661 ? 0.3478 0.3868 0.4160 -0.0019 0.0063 -0.0229 702 GLY A CA 5442 C C . GLY A 661 ? 0.3496 0.3904 0.4263 -0.0064 0.0099 -0.0205 702 GLY A C 5443 O O . GLY A 661 ? 0.3605 0.4065 0.4519 -0.0078 0.0123 -0.0216 702 GLY A O 5444 N N . GLU A 662 ? 0.3355 0.3722 0.4038 -0.0088 0.0108 -0.0170 703 GLU A N 5445 C CA . GLU A 662 ? 0.3361 0.3731 0.4125 -0.0129 0.0135 -0.0141 703 GLU A CA 5446 C C . GLU A 662 ? 0.3209 0.3532 0.3972 -0.0125 0.0062 -0.0140 703 GLU A C 5447 O O . GLU A 662 ? 0.3246 0.3525 0.3879 -0.0104 0.0030 -0.0137 703 GLU A O 5448 C CB . GLU A 662 ? 0.3569 0.3919 0.4224 -0.0157 0.0207 -0.0095 703 GLU A CB 5449 C CG . GLU A 662 ? 0.3667 0.4017 0.4415 -0.0201 0.0249 -0.0055 703 GLU A CG 5450 C CD . GLU A 662 ? 0.4229 0.4646 0.5177 -0.0217 0.0281 -0.0072 703 GLU A CD 5451 O OE1 . GLU A 662 ? 0.4001 0.4461 0.4960 -0.0217 0.0351 -0.0075 703 GLU A OE1 5452 O OE2 . GLU A 662 ? 0.4271 0.4698 0.5372 -0.0225 0.0233 -0.0089 703 GLU A OE2 5453 N N . SER A 663 ? 0.3011 0.3341 0.3918 -0.0147 0.0040 -0.0143 704 SER A N 5454 C CA A SER A 663 ? 0.2687 0.2965 0.3590 -0.0143 -0.0028 -0.0146 704 SER A CA 5455 C CA B SER A 663 ? 0.2912 0.3188 0.3804 -0.0142 -0.0027 -0.0144 704 SER A CA 5456 C C . SER A 663 ? 0.2864 0.3102 0.3731 -0.0181 0.0008 -0.0094 704 SER A C 5457 O O . SER A 663 ? 0.2967 0.3226 0.3881 -0.0217 0.0082 -0.0059 704 SER A O 5458 C CB A SER A 663 ? 0.2763 0.3059 0.3839 -0.0138 -0.0093 -0.0187 704 SER A CB 5459 C CB B SER A 663 ? 0.2938 0.3225 0.3981 -0.0131 -0.0100 -0.0188 704 SER A CB 5460 O OG A SER A 663 ? 0.1905 0.2256 0.3159 -0.0176 -0.0045 -0.0181 704 SER A OG 5461 O OG B SER A 663 ? 0.3547 0.3869 0.4610 -0.0092 -0.0131 -0.0231 704 SER A OG 5462 N N . PHE A 664 ? 0.2680 0.2858 0.3469 -0.0169 -0.0042 -0.0089 705 PHE A N 5463 C CA . PHE A 664 ? 0.2553 0.2680 0.3276 -0.0196 -0.0016 -0.0037 705 PHE A CA 5464 C C . PHE A 664 ? 0.2545 0.2684 0.3174 -0.0214 0.0067 0.0006 705 PHE A C 5465 O O . PHE A 664 ? 0.2511 0.2644 0.3171 -0.0251 0.0126 0.0050 705 PHE A O 5466 C CB . PHE A 664 ? 0.2637 0.2746 0.3507 -0.0232 -0.0023 -0.0022 705 PHE A CB 5467 C CG . PHE A 664 ? 0.2713 0.2790 0.3645 -0.0209 -0.0118 -0.0066 705 PHE A CG 5468 C CD1 . PHE A 664 ? 0.2661 0.2684 0.3468 -0.0175 -0.0171 -0.0075 705 PHE A CD1 5469 C CD2 . PHE A 664 ? 0.2600 0.2702 0.3719 -0.0219 -0.0155 -0.0102 705 PHE A CD2 5470 C CE1 . PHE A 664 ? 0.2821 0.2809 0.3669 -0.0148 -0.0258 -0.0120 705 PHE A CE1 5471 C CE2 . PHE A 664 ? 0.2763 0.2831 0.3930 -0.0194 -0.0250 -0.0151 705 PHE A CE2 5472 C CZ . PHE A 664 ? 0.2774 0.2780 0.3795 -0.0157 -0.0300 -0.0159 705 PHE A CZ 5473 N N . PRO A 665 ? 0.2605 0.2753 0.3109 -0.0187 0.0073 -0.0006 706 PRO A N 5474 C CA . PRO A 665 ? 0.2592 0.2755 0.3007 -0.0197 0.0146 0.0019 706 PRO A CA 5475 C C . PRO A 665 ? 0.2640 0.2754 0.2955 -0.0216 0.0173 0.0072 706 PRO A C 5476 O O . PRO A 665 ? 0.2851 0.2971 0.3122 -0.0234 0.0242 0.0104 706 PRO A O 5477 C CB . PRO A 665 ? 0.2603 0.2774 0.2912 -0.0160 0.0123 -0.0012 706 PRO A CB 5478 C CG . PRO A 665 ? 0.2726 0.2865 0.3028 -0.0133 0.0044 -0.0034 706 PRO A CG 5479 C CD . PRO A 665 ? 0.2488 0.2635 0.2941 -0.0143 0.0015 -0.0048 706 PRO A CD 5480 N N . GLY A 666 ? 0.2528 0.2590 0.2802 -0.0209 0.0120 0.0084 707 GLY A N 5481 C CA . GLY A 666 ? 0.2702 0.2711 0.2876 -0.0223 0.0141 0.0138 707 GLY A CA 5482 C C . GLY A 666 ? 0.2759 0.2757 0.3015 -0.0263 0.0197 0.0185 707 GLY A C 5483 O O . GLY A 666 ? 0.2837 0.2814 0.3007 -0.0278 0.0258 0.0235 707 GLY A O 5484 N N . ILE A 667 ? 0.2643 0.2652 0.3063 -0.0279 0.0177 0.0171 708 ILE A N 5485 C CA . ILE A 667 ? 0.2676 0.2674 0.3205 -0.0322 0.0231 0.0216 708 ILE A CA 5486 C C . ILE A 667 ? 0.2739 0.2799 0.3309 -0.0337 0.0319 0.0221 708 ILE A C 5487 O O . ILE A 667 ? 0.2923 0.2971 0.3480 -0.0364 0.0400 0.0277 708 ILE A O 5488 C CB . ILE A 667 ? 0.2573 0.2572 0.3295 -0.0336 0.0181 0.0190 708 ILE A CB 5489 C CG1 . ILE A 667 ? 0.2710 0.2650 0.3394 -0.0312 0.0089 0.0171 708 ILE A CG1 5490 C CG2 . ILE A 667 ? 0.2818 0.2799 0.3665 -0.0386 0.0242 0.0246 708 ILE A CG2 5491 C CD1 . ILE A 667 ? 0.2743 0.2679 0.3606 -0.0315 0.0018 0.0126 708 ILE A CD1 5492 N N . TYR A 668 ? 0.2551 0.2673 0.3164 -0.0316 0.0305 0.0166 709 TYR A N 5493 C CA . TYR A 668 ? 0.2848 0.3034 0.3518 -0.0327 0.0387 0.0163 709 TYR A CA 5494 C C . TYR A 668 ? 0.2882 0.3050 0.3375 -0.0325 0.0462 0.0203 709 TYR A C 5495 O O . TYR A 668 ? 0.3081 0.3259 0.3593 -0.0348 0.0554 0.0244 709 TYR A O 5496 C CB . TYR A 668 ? 0.2776 0.3021 0.3498 -0.0297 0.0350 0.0095 709 TYR A CB 5497 C CG . TYR A 668 ? 0.2924 0.3236 0.3717 -0.0305 0.0433 0.0089 709 TYR A CG 5498 C CD1 . TYR A 668 ? 0.3419 0.3786 0.4426 -0.0325 0.0452 0.0075 709 TYR A CD1 5499 C CD2 . TYR A 668 ? 0.3406 0.3724 0.4052 -0.0290 0.0492 0.0095 709 TYR A CD2 5500 C CE1 . TYR A 668 ? 0.3515 0.3951 0.4602 -0.0330 0.0537 0.0069 709 TYR A CE1 5501 C CE2 . TYR A 668 ? 0.3158 0.3536 0.3868 -0.0294 0.0576 0.0087 709 TYR A CE2 5502 C CZ . TYR A 668 ? 0.3779 0.4217 0.4710 -0.0313 0.0600 0.0075 709 TYR A CZ 5503 O OH . TYR A 668 ? 0.3446 0.3949 0.4452 -0.0314 0.0685 0.0065 709 TYR A OH 5504 N N . ASP A 669 ? 0.3111 0.3252 0.3434 -0.0294 0.0424 0.0190 710 ASP A N 5505 C CA . ASP A 669 ? 0.3262 0.3379 0.3406 -0.0286 0.0477 0.0218 710 ASP A CA 5506 C C . ASP A 669 ? 0.3412 0.3465 0.3480 -0.0306 0.0516 0.0292 710 ASP A C 5507 O O . ASP A 669 ? 0.3387 0.3430 0.3359 -0.0310 0.0595 0.0328 710 ASP A O 5508 C CB . ASP A 669 ? 0.3150 0.3251 0.3152 -0.0251 0.0416 0.0184 710 ASP A CB 5509 C CG . ASP A 669 ? 0.3715 0.3872 0.3749 -0.0229 0.0410 0.0124 710 ASP A CG 5510 O OD1 . ASP A 669 ? 0.3709 0.3919 0.3846 -0.0237 0.0462 0.0109 710 ASP A OD1 5511 O OD2 . ASP A 669 ? 0.4132 0.4282 0.4100 -0.0203 0.0353 0.0092 710 ASP A OD2 5512 N N . ALA A 670 ? 0.3284 0.3289 0.3393 -0.0318 0.0465 0.0316 711 ALA A N 5513 C CA . ALA A 670 ? 0.3398 0.3334 0.3448 -0.0339 0.0504 0.0393 711 ALA A CA 5514 C C . ALA A 670 ? 0.3457 0.3412 0.3624 -0.0376 0.0604 0.0437 711 ALA A C 5515 O O . ALA A 670 ? 0.3614 0.3525 0.3687 -0.0386 0.0677 0.0503 711 ALA A O 5516 C CB . ALA A 670 ? 0.3371 0.3250 0.3466 -0.0343 0.0424 0.0405 711 ALA A CB 5517 N N . LEU A 671 ? 0.3220 0.3239 0.3591 -0.0393 0.0610 0.0400 712 LEU A N 5518 C CA . LEU A 671 ? 0.3345 0.3396 0.3868 -0.0431 0.0709 0.0438 712 LEU A CA 5519 C C . LEU A 671 ? 0.3486 0.3595 0.3967 -0.0422 0.0803 0.0430 712 LEU A C 5520 O O . LEU A 671 ? 0.3586 0.3712 0.4133 -0.0447 0.0909 0.0475 712 LEU A O 5521 C CB . LEU A 671 ? 0.3273 0.3375 0.4054 -0.0452 0.0665 0.0394 712 LEU A CB 5522 C CG . LEU A 671 ? 0.3370 0.3412 0.4241 -0.0472 0.0596 0.0411 712 LEU A CG 5523 C CD1 . LEU A 671 ? 0.3155 0.3251 0.4248 -0.0475 0.0524 0.0341 712 LEU A CD1 5524 C CD2 . LEU A 671 ? 0.3503 0.3498 0.4428 -0.0515 0.0682 0.0497 712 LEU A CD2 5525 N N . PHE A 672 ? 0.3650 0.3786 0.4022 -0.0385 0.0769 0.0375 713 PHE A N 5526 C CA . PHE A 672 ? 0.3823 0.4023 0.4188 -0.0373 0.0851 0.0351 713 PHE A CA 5527 C C . PHE A 672 ? 0.3952 0.4113 0.4151 -0.0372 0.0955 0.0413 713 PHE A C 5528 O O . PHE A 672 ? 0.4076 0.4168 0.4060 -0.0352 0.0935 0.0439 713 PHE A O 5529 C CB . PHE A 672 ? 0.3758 0.3988 0.4041 -0.0332 0.0792 0.0277 713 PHE A CB 5530 C CG . PHE A 672 ? 0.4123 0.4418 0.4427 -0.0319 0.0868 0.0246 713 PHE A CG 5531 C CD1 . PHE A 672 ? 0.4338 0.4712 0.4862 -0.0327 0.0882 0.0209 713 PHE A CD1 5532 C CD2 . PHE A 672 ? 0.4425 0.4699 0.4535 -0.0295 0.0927 0.0254 713 PHE A CD2 5533 C CE1 . PHE A 672 ? 0.4678 0.5114 0.5234 -0.0313 0.0958 0.0180 713 PHE A CE1 5534 C CE2 . PHE A 672 ? 0.4450 0.4782 0.4579 -0.0280 0.1004 0.0223 713 PHE A CE2 5535 C CZ . PHE A 672 ? 0.4609 0.5022 0.4965 -0.0289 0.1021 0.0187 713 PHE A CZ 5536 N N . ASP A 673 ? 0.4169 0.4373 0.4473 -0.0392 0.1066 0.0438 714 ASP A N 5537 C CA . ASP A 673 ? 0.4508 0.4681 0.4659 -0.0387 0.1187 0.0499 714 ASP A CA 5538 C C . ASP A 673 ? 0.4584 0.4656 0.4608 -0.0401 0.1192 0.0584 714 ASP A C 5539 O O . ASP A 673 ? 0.4859 0.4872 0.4657 -0.0379 0.1243 0.0628 714 ASP A O 5540 C CB . ASP A 673 ? 0.4703 0.4876 0.4636 -0.0339 0.1187 0.0453 714 ASP A CB 5541 C CG . ASP A 673 ? 0.5136 0.5295 0.4924 -0.0325 0.1322 0.0495 714 ASP A CG 5542 O OD1 . ASP A 673 ? 0.5086 0.5282 0.5006 -0.0350 0.1433 0.0534 714 ASP A OD1 5543 O OD2 . ASP A 673 ? 0.5728 0.5840 0.5269 -0.0286 0.1317 0.0487 714 ASP A OD2 5544 N N . ILE A 674 ? 0.4477 0.4523 0.4642 -0.0432 0.1135 0.0607 715 ILE A N 5545 C CA . ILE A 674 ? 0.4408 0.4351 0.4453 -0.0440 0.1117 0.0681 715 ILE A CA 5546 C C . ILE A 674 ? 0.4909 0.4805 0.4885 -0.0456 0.1253 0.0778 715 ILE A C 5547 O O . ILE A 674 ? 0.4946 0.4747 0.4716 -0.0441 0.1258 0.0841 715 ILE A O 5548 C CB . ILE A 674 ? 0.4288 0.4210 0.4510 -0.0469 0.1027 0.0679 715 ILE A CB 5549 C CG1 . ILE A 674 ? 0.4263 0.4075 0.4338 -0.0465 0.0991 0.0745 715 ILE A CG1 5550 C CG2 . ILE A 674 ? 0.4049 0.4019 0.4557 -0.0517 0.1083 0.0694 715 ILE A CG2 5551 C CD1 . ILE A 674 ? 0.4210 0.3993 0.4392 -0.0474 0.0875 0.0722 715 ILE A CD1 5552 N N . GLU A 675 ? 0.5084 0.5045 0.5232 -0.0483 0.1362 0.0790 716 GLU A N 5553 C CA . GLU A 675 ? 0.5706 0.5632 0.5815 -0.0500 0.1511 0.0886 716 GLU A CA 5554 C C . GLU A 675 ? 0.6044 0.5929 0.5845 -0.0454 0.1583 0.0910 716 GLU A C 5555 O O . GLU A 675 ? 0.6182 0.6016 0.5889 -0.0458 0.1704 0.0998 716 GLU A O 5556 C CB . GLU A 675 ? 0.5689 0.5707 0.6087 -0.0541 0.1613 0.0888 716 GLU A CB 5557 C CG . GLU A 675 ? 0.5946 0.6067 0.6375 -0.0517 0.1666 0.0818 716 GLU A CG 5558 C CD . GLU A 675 ? 0.6234 0.6436 0.6802 -0.0505 0.1545 0.0706 716 GLU A CD 5559 O OE1 . GLU A 675 ? 0.5526 0.5704 0.6120 -0.0506 0.1411 0.0672 716 GLU A OE1 5560 O OE2 . GLU A 675 ? 0.6733 0.7024 0.7384 -0.0491 0.1589 0.0653 716 GLU A OE2 5561 N N . SER A 676 ? 0.6098 0.6001 0.5745 -0.0408 0.1510 0.0833 717 SER A N 5562 C CA A SER A 676 ? 0.6369 0.6231 0.5717 -0.0358 0.1554 0.0838 717 SER A CA 5563 C CA B SER A 676 ? 0.6469 0.6330 0.5816 -0.0358 0.1555 0.0839 717 SER A CA 5564 C C . SER A 676 ? 0.6618 0.6377 0.5717 -0.0326 0.1455 0.0857 717 SER A C 5565 O O . SER A 676 ? 0.6924 0.6628 0.5754 -0.0283 0.1479 0.0870 717 SER A O 5566 C CB A SER A 676 ? 0.6253 0.6197 0.5590 -0.0325 0.1545 0.0739 717 SER A CB 5567 C CB B SER A 676 ? 0.6373 0.6315 0.5706 -0.0325 0.1544 0.0740 717 SER A CB 5568 O OG A SER A 676 ? 0.5708 0.5750 0.5285 -0.0350 0.1628 0.0718 717 SER A OG 5569 O OG B SER A 676 ? 0.6391 0.6315 0.5610 -0.0294 0.1406 0.0675 717 SER A OG 5570 N N . LYS A 677 ? 0.6516 0.6249 0.5704 -0.0345 0.1344 0.0855 718 LYS A N 5571 C CA . LYS A 677 ? 0.6703 0.6345 0.5687 -0.0316 0.1244 0.0872 718 LYS A CA 5572 C C . LYS A 677 ? 0.6976 0.6509 0.5789 -0.0313 0.1312 0.0983 718 LYS A C 5573 O O . LYS A 677 ? 0.7039 0.6553 0.5976 -0.0352 0.1398 0.1059 718 LYS A O 5574 C CB . LYS A 677 ? 0.6564 0.6206 0.5695 -0.0335 0.1115 0.0841 718 LYS A CB 5575 C CG . LYS A 677 ? 0.6536 0.6267 0.5790 -0.0329 0.1032 0.0735 718 LYS A CG 5576 C CD . LYS A 677 ? 0.7186 0.6929 0.6247 -0.0281 0.0998 0.0673 718 LYS A CD 5577 C CE . LYS A 677 ? 0.7263 0.7100 0.6465 -0.0278 0.0947 0.0575 718 LYS A CE 5578 N NZ . LYS A 677 ? 0.6944 0.6787 0.6271 -0.0288 0.0832 0.0542 718 LYS A NZ 5579 N N . VAL A 678 ? 0.7189 0.6647 0.5723 -0.0264 0.1270 0.0993 719 VAL A N 5580 C CA . VAL A 678 ? 0.7491 0.6837 0.5821 -0.0250 0.1339 0.1102 719 VAL A CA 5581 C C . VAL A 678 ? 0.7443 0.6703 0.5814 -0.0271 0.1281 0.1173 719 VAL A C 5582 O O . VAL A 678 ? 0.7679 0.6856 0.5983 -0.0279 0.1360 0.1277 719 VAL A O 5583 C CB . VAL A 678 ? 0.7752 0.7039 0.5742 -0.0183 0.1324 0.1093 719 VAL A CB 5584 C CG1 . VAL A 678 ? 0.8050 0.7395 0.5973 -0.0163 0.1432 0.1056 719 VAL A CG1 5585 C CG2 . VAL A 678 ? 0.7645 0.6930 0.5558 -0.0151 0.1160 0.1014 719 VAL A CG2 5586 N N . ASP A 679 ? 0.7123 0.6402 0.5606 -0.0277 0.1146 0.1117 720 ASP A N 5587 C CA . ASP A 679 ? 0.6957 0.6157 0.5490 -0.0293 0.1080 0.1172 720 ASP A CA 5588 C C . ASP A 679 ? 0.6510 0.5779 0.5365 -0.0344 0.1052 0.1133 720 ASP A C 5589 O O . ASP A 679 ? 0.6100 0.5415 0.5038 -0.0339 0.0942 0.1053 720 ASP A O 5590 C CB . ASP A 679 ? 0.7007 0.6168 0.5390 -0.0248 0.0937 0.1132 720 ASP A CB 5591 C CG . ASP A 679 ? 0.7333 0.6396 0.5719 -0.0252 0.0873 0.1197 720 ASP A CG 5592 O OD1 . ASP A 679 ? 0.7528 0.6573 0.6101 -0.0297 0.0907 0.1244 720 ASP A OD1 5593 O OD2 . ASP A 679 ? 0.8195 0.7197 0.6403 -0.0208 0.0784 0.1197 720 ASP A OD2 5594 N N . PRO A 680 ? 0.6315 0.5592 0.5351 -0.0393 0.1153 0.1189 721 PRO A N 5595 C CA . PRO A 680 ? 0.6002 0.5348 0.5351 -0.0440 0.1125 0.1145 721 PRO A CA 5596 C C . PRO A 680 ? 0.5851 0.5147 0.5283 -0.0447 0.1002 0.1137 721 PRO A C 5597 O O . PRO A 680 ? 0.5374 0.4730 0.4997 -0.0462 0.0928 0.1063 721 PRO A O 5598 C CB . PRO A 680 ? 0.6112 0.5454 0.5610 -0.0489 0.1264 0.1224 721 PRO A CB 5599 C CG . PRO A 680 ? 0.6483 0.5720 0.5740 -0.0469 0.1351 0.1332 721 PRO A CG 5600 C CD . PRO A 680 ? 0.6604 0.5828 0.5565 -0.0404 0.1300 0.1293 721 PRO A CD 5601 N N . SER A 681 ? 0.5883 0.5064 0.5168 -0.0432 0.0982 0.1213 722 SER A N 5602 C CA . SER A 681 ? 0.5894 0.5023 0.5237 -0.0429 0.0862 0.1202 722 SER A CA 5603 C C . SER A 681 ? 0.5593 0.4779 0.4905 -0.0394 0.0739 0.1097 722 SER A C 5604 O O . SER A 681 ? 0.5296 0.4513 0.4779 -0.0406 0.0658 0.1039 722 SER A O 5605 C CB . SER A 681 ? 0.6161 0.5156 0.5315 -0.0407 0.0857 0.1299 722 SER A CB 5606 O OG . SER A 681 ? 0.6667 0.5615 0.5904 -0.0406 0.0747 0.1286 722 SER A OG 5607 N N . LYS A 682 ? 0.5466 0.4664 0.4561 -0.0349 0.0725 0.1071 723 LYS A N 5608 C CA A LYS A 682 ? 0.5298 0.4552 0.4363 -0.0316 0.0619 0.0975 723 LYS A CA 5609 C CA B LYS A 682 ? 0.5332 0.4586 0.4404 -0.0317 0.0617 0.0975 723 LYS A CA 5610 C C . LYS A 682 ? 0.5017 0.4386 0.4272 -0.0336 0.0618 0.0888 723 LYS A C 5611 O O . LYS A 682 ? 0.4718 0.4125 0.4067 -0.0330 0.0528 0.0820 723 LYS A O 5612 C CB A LYS A 682 ? 0.5465 0.4708 0.4272 -0.0268 0.0615 0.0966 723 LYS A CB 5613 C CB B LYS A 682 ? 0.5504 0.4744 0.4319 -0.0267 0.0600 0.0963 723 LYS A CB 5614 C CG A LYS A 682 ? 0.5394 0.4687 0.4167 -0.0235 0.0508 0.0875 723 LYS A CG 5615 C CG B LYS A 682 ? 0.5952 0.5091 0.4595 -0.0232 0.0531 0.1011 723 LYS A CG 5616 C CD A LYS A 682 ? 0.5822 0.5099 0.4351 -0.0188 0.0498 0.0862 723 LYS A CD 5617 C CD B LYS A 682 ? 0.6312 0.5463 0.4763 -0.0180 0.0463 0.0958 723 LYS A CD 5618 C CE A LYS A 682 ? 0.5916 0.5252 0.4450 -0.0162 0.0398 0.0768 723 LYS A CE 5619 C CE B LYS A 682 ? 0.6484 0.5545 0.4798 -0.0143 0.0376 0.0995 723 LYS A CE 5620 N NZ A LYS A 682 ? 0.6395 0.5720 0.4713 -0.0120 0.0385 0.0747 723 LYS A NZ 5621 N NZ B LYS A 682 ? 0.6810 0.5760 0.5002 -0.0142 0.0440 0.1108 723 LYS A NZ 5622 N N . ALA A 683 ? 0.4809 0.4230 0.4109 -0.0356 0.0721 0.0892 724 ALA A N 5623 C CA . ALA A 683 ? 0.4350 0.3880 0.3820 -0.0370 0.0721 0.0810 724 ALA A CA 5624 C C . ALA A 683 ? 0.4112 0.3661 0.3833 -0.0404 0.0676 0.0789 724 ALA A C 5625 O O . ALA A 683 ? 0.3793 0.3400 0.3609 -0.0396 0.0604 0.0711 724 ALA A O 5626 C CB . ALA A 683 ? 0.4498 0.4077 0.3990 -0.0386 0.0848 0.0827 724 ALA A CB 5627 N N . TRP A 684 ? 0.4000 0.3497 0.3827 -0.0441 0.0724 0.0860 725 TRP A N 5628 C CA . TRP A 684 ? 0.3972 0.3477 0.4039 -0.0473 0.0674 0.0836 725 TRP A CA 5629 C C . TRP A 684 ? 0.3907 0.3364 0.3953 -0.0450 0.0549 0.0806 725 TRP A C 5630 O O . TRP A 684 ? 0.3787 0.3278 0.3988 -0.0454 0.0479 0.0743 725 TRP A O 5631 C CB . TRP A 684 ? 0.3907 0.3370 0.4113 -0.0522 0.0759 0.0917 725 TRP A CB 5632 C CG . TRP A 684 ? 0.3996 0.3545 0.4328 -0.0550 0.0867 0.0913 725 TRP A CG 5633 C CD1 . TRP A 684 ? 0.4135 0.3685 0.4372 -0.0554 0.0995 0.0974 725 TRP A CD1 5634 C CD2 . TRP A 684 ? 0.3840 0.3487 0.4411 -0.0571 0.0852 0.0839 725 TRP A CD2 5635 N NE1 . TRP A 684 ? 0.4001 0.3650 0.4417 -0.0578 0.1064 0.0941 725 TRP A NE1 5636 C CE2 . TRP A 684 ? 0.3742 0.3451 0.4369 -0.0589 0.0975 0.0860 725 TRP A CE2 5637 C CE3 . TRP A 684 ? 0.3526 0.3212 0.4263 -0.0571 0.0745 0.0757 725 TRP A CE3 5638 C CZ2 . TRP A 684 ? 0.3760 0.3572 0.4619 -0.0610 0.0991 0.0801 725 TRP A CZ2 5639 C CZ3 . TRP A 684 ? 0.3551 0.3334 0.4505 -0.0591 0.0757 0.0699 725 TRP A CZ3 5640 C CH2 . TRP A 684 ? 0.3534 0.3381 0.4551 -0.0610 0.0876 0.0722 725 TRP A CH2 5641 N N . GLY A 685 ? 0.4126 0.3505 0.3980 -0.0421 0.0520 0.0849 726 GLY A N 5642 C CA . GLY A 685 ? 0.4020 0.3367 0.3827 -0.0388 0.0404 0.0812 726 GLY A CA 5643 C C . GLY A 685 ? 0.3969 0.3402 0.3793 -0.0362 0.0341 0.0713 726 GLY A C 5644 O O . GLY A 685 ? 0.3803 0.3243 0.3717 -0.0352 0.0259 0.0660 726 GLY A O 5645 N N . GLU A 686 ? 0.3911 0.3404 0.3643 -0.0349 0.0381 0.0687 727 GLU A N 5646 C CA . GLU A 686 ? 0.3784 0.3352 0.3526 -0.0324 0.0327 0.0599 727 GLU A CA 5647 C C . GLU A 686 ? 0.3563 0.3198 0.3516 -0.0346 0.0320 0.0544 727 GLU A C 5648 O O . GLU A 686 ? 0.3353 0.3021 0.3354 -0.0326 0.0249 0.0479 727 GLU A O 5649 C CB . GLU A 686 ? 0.3938 0.3547 0.3534 -0.0304 0.0369 0.0584 727 GLU A CB 5650 C CG A GLU A 686 ? 0.4182 0.3863 0.3791 -0.0280 0.0319 0.0499 727 GLU A CG 5651 C CD A GLU A 686 ? 0.4590 0.4252 0.4157 -0.0249 0.0219 0.0465 727 GLU A CD 5652 O OE1 A GLU A 686 ? 0.4909 0.4503 0.4412 -0.0239 0.0182 0.0505 727 GLU A OE1 5653 O OE2 A GLU A 686 ? 0.4738 0.4456 0.4341 -0.0233 0.0183 0.0400 727 GLU A OE2 5654 N N . VAL A 687 ? 0.3421 0.3074 0.3504 -0.0384 0.0393 0.0571 728 VAL A N 5655 C CA . VAL A 687 ? 0.3182 0.2891 0.3482 -0.0404 0.0374 0.0520 728 VAL A CA 5656 C C . VAL A 687 ? 0.3196 0.2860 0.3586 -0.0401 0.0281 0.0499 728 VAL A C 5657 O O . VAL A 687 ? 0.2928 0.2627 0.3393 -0.0384 0.0212 0.0428 728 VAL A O 5658 C CB . VAL A 687 ? 0.3441 0.3171 0.3894 -0.0450 0.0469 0.0561 728 VAL A CB 5659 C CG1 . VAL A 687 ? 0.3325 0.3102 0.4027 -0.0471 0.0428 0.0506 728 VAL A CG1 5660 C CG2 . VAL A 687 ? 0.3132 0.2918 0.3502 -0.0448 0.0569 0.0571 728 VAL A CG2 5661 N N . LYS A 688 ? 0.3234 0.2812 0.3607 -0.0414 0.0281 0.0561 729 LYS A N 5662 C CA . LYS A 688 ? 0.3229 0.2753 0.3681 -0.0409 0.0196 0.0543 729 LYS A CA 5663 C C . LYS A 688 ? 0.3264 0.2791 0.3611 -0.0359 0.0108 0.0486 729 LYS A C 5664 O O . LYS A 688 ? 0.3148 0.2677 0.3583 -0.0345 0.0034 0.0429 729 LYS A O 5665 C CB B LYS A 688 ? 0.3333 0.2758 0.3766 -0.0428 0.0217 0.0627 729 LYS A CB 5666 C CB C LYS A 688 ? 0.3385 0.2808 0.3815 -0.0427 0.0216 0.0627 729 LYS A CB 5667 C CG B LYS A 688 ? 0.3277 0.2693 0.3868 -0.0482 0.0299 0.0680 729 LYS A CG 5668 C CG C LYS A 688 ? 0.3472 0.2881 0.4052 -0.0482 0.0300 0.0686 729 LYS A CG 5669 C CD B LYS A 688 ? 0.3747 0.3053 0.4317 -0.0502 0.0325 0.0773 729 LYS A CD 5670 C CD C LYS A 688 ? 0.3899 0.3195 0.4460 -0.0499 0.0319 0.0776 729 LYS A CD 5671 C CE B LYS A 688 ? 0.3812 0.3050 0.4466 -0.0494 0.0228 0.0750 729 LYS A CE 5672 C CE C LYS A 688 ? 0.4158 0.3410 0.4502 -0.0488 0.0391 0.0859 729 LYS A CE 5673 N NZ B LYS A 688 ? 0.4499 0.3628 0.5161 -0.0520 0.0266 0.0848 729 LYS A NZ 5674 N NZ C LYS A 688 ? 0.4641 0.3773 0.4946 -0.0499 0.0406 0.0953 729 LYS A NZ 5675 N N . ARG A 689 ? 0.3167 0.2694 0.3329 -0.0332 0.0116 0.0501 730 ARG A N 5676 C CA . ARG A 689 ? 0.3129 0.2670 0.3210 -0.0287 0.0042 0.0448 730 ARG A CA 5677 C C . ARG A 689 ? 0.2955 0.2574 0.3104 -0.0274 0.0018 0.0369 730 ARG A C 5678 O O . ARG A 689 ? 0.2913 0.2532 0.3091 -0.0247 -0.0050 0.0319 730 ARG A O 5679 C CB . ARG A 689 ? 0.3275 0.2809 0.3164 -0.0262 0.0053 0.0471 730 ARG A CB 5680 C CG . ARG A 689 ? 0.3536 0.3072 0.3368 -0.0219 -0.0026 0.0426 730 ARG A CG 5681 C CD . ARG A 689 ? 0.3770 0.3298 0.3427 -0.0195 -0.0026 0.0447 730 ARG A CD 5682 N NE . ARG A 689 ? 0.3912 0.3509 0.3520 -0.0192 0.0009 0.0415 730 ARG A NE 5683 C CZ . ARG A 689 ? 0.4507 0.4160 0.4120 -0.0170 -0.0020 0.0353 730 ARG A CZ 5684 N NH1 . ARG A 689 ? 0.4427 0.4084 0.4093 -0.0147 -0.0081 0.0315 730 ARG A NH1 5685 N NH2 . ARG A 689 ? 0.4629 0.4334 0.4198 -0.0170 0.0015 0.0330 730 ARG A NH2 5686 N N . GLN A 690 ? 0.2791 0.2474 0.2967 -0.0289 0.0074 0.0358 731 GLN A N 5687 C CA . GLN A 690 ? 0.2816 0.2567 0.3057 -0.0274 0.0050 0.0287 731 GLN A CA 5688 C C . GLN A 690 ? 0.2769 0.2523 0.3184 -0.0282 0.0005 0.0249 731 GLN A C 5689 O O . GLN A 690 ? 0.2637 0.2422 0.3076 -0.0253 -0.0047 0.0186 731 GLN A O 5690 C CB . GLN A 690 ? 0.2702 0.2517 0.2941 -0.0287 0.0121 0.0286 731 GLN A CB 5691 C CG . GLN A 690 ? 0.2965 0.2778 0.3016 -0.0269 0.0150 0.0306 731 GLN A CG 5692 C CD . GLN A 690 ? 0.3532 0.3358 0.3502 -0.0229 0.0089 0.0260 731 GLN A CD 5693 O OE1 . GLN A 690 ? 0.3318 0.3179 0.3354 -0.0212 0.0050 0.0206 731 GLN A OE1 5694 N NE2 . GLN A 690 ? 0.3998 0.3794 0.3829 -0.0212 0.0079 0.0281 731 GLN A NE2 5695 N N . ILE A 691 ? 0.2739 0.2459 0.3269 -0.0320 0.0027 0.0286 732 ILE A N 5696 C CA . ILE A 691 ? 0.2857 0.2571 0.3557 -0.0327 -0.0027 0.0244 732 ILE A CA 5697 C C . ILE A 691 ? 0.2880 0.2542 0.3536 -0.0289 -0.0115 0.0210 732 ILE A C 5698 O O . ILE A 691 ? 0.2928 0.2607 0.3641 -0.0264 -0.0177 0.0145 732 ILE A O 5699 C CB . ILE A 691 ? 0.2784 0.2464 0.3629 -0.0376 0.0010 0.0292 732 ILE A CB 5700 C CG1 . ILE A 691 ? 0.2693 0.2438 0.3616 -0.0411 0.0100 0.0313 732 ILE A CG1 5701 C CG2 . ILE A 691 ? 0.2872 0.2526 0.3891 -0.0381 -0.0066 0.0244 732 ILE A CG2 5702 C CD1 . ILE A 691 ? 0.2957 0.2664 0.4007 -0.0465 0.0165 0.0382 732 ILE A CD1 5703 N N . TYR A 692 ? 0.2762 0.2360 0.3317 -0.0282 -0.0119 0.0255 733 TYR A N 5704 C CA . TYR A 692 ? 0.2994 0.2546 0.3498 -0.0242 -0.0195 0.0225 733 TYR A CA 5705 C C . TYR A 692 ? 0.2862 0.2462 0.3278 -0.0195 -0.0227 0.0169 733 TYR A C 5706 O O . TYR A 692 ? 0.2758 0.2350 0.3198 -0.0162 -0.0289 0.0114 733 TYR A O 5707 C CB . TYR A 692 ? 0.3150 0.2638 0.3548 -0.0241 -0.0183 0.0289 733 TYR A CB 5708 C CG . TYR A 692 ? 0.3743 0.3195 0.4044 -0.0195 -0.0241 0.0275 733 TYR A CG 5709 C CD1 . TYR A 692 ? 0.4115 0.3533 0.4475 -0.0167 -0.0311 0.0227 733 TYR A CD1 5710 C CD2 . TYR A 692 ? 0.4049 0.3498 0.4203 -0.0179 -0.0225 0.0311 733 TYR A CD2 5711 C CE1 . TYR A 692 ? 0.3960 0.3346 0.4238 -0.0124 -0.0355 0.0217 733 TYR A CE1 5712 C CE2 . TYR A 692 ? 0.3757 0.3176 0.3844 -0.0140 -0.0274 0.0303 733 TYR A CE2 5713 C CZ . TYR A 692 ? 0.4264 0.3654 0.4416 -0.0113 -0.0335 0.0258 733 TYR A CZ 5714 O OH . TYR A 692 ? 0.4246 0.3608 0.4340 -0.0071 -0.0380 0.0248 733 TYR A OH 5715 N N . VAL A 693 ? 0.2737 0.2384 0.3051 -0.0191 -0.0183 0.0182 734 VAL A N 5716 C CA . VAL A 693 ? 0.2796 0.2487 0.3037 -0.0149 -0.0208 0.0132 734 VAL A CA 5717 C C . VAL A 693 ? 0.2834 0.2565 0.3161 -0.0137 -0.0234 0.0071 734 VAL A C 5718 O O . VAL A 693 ? 0.2797 0.2530 0.3098 -0.0094 -0.0282 0.0023 734 VAL A O 5719 C CB . VAL A 693 ? 0.2930 0.2662 0.3058 -0.0150 -0.0157 0.0153 734 VAL A CB 5720 C CG1 . VAL A 693 ? 0.3031 0.2809 0.3109 -0.0112 -0.0177 0.0104 734 VAL A CG1 5721 C CG2 . VAL A 693 ? 0.3064 0.2751 0.3086 -0.0148 -0.0153 0.0203 734 VAL A CG2 5722 N N . ALA A 694 ? 0.2772 0.2536 0.3199 -0.0169 -0.0202 0.0073 735 ALA A N 5723 C CA . ALA A 694 ? 0.2734 0.2538 0.3251 -0.0156 -0.0233 0.0014 735 ALA A CA 5724 C C . ALA A 694 ? 0.2714 0.2474 0.3316 -0.0140 -0.0308 -0.0026 735 ALA A C 5725 O O . ALA A 694 ? 0.2690 0.2459 0.3282 -0.0098 -0.0361 -0.0084 735 ALA A O 5726 C CB . ALA A 694 ? 0.2922 0.2776 0.3547 -0.0195 -0.0181 0.0025 735 ALA A CB 5727 N N . ALA A 695 ? 0.2536 0.2242 0.3214 -0.0169 -0.0315 0.0002 736 ALA A N 5728 C CA . ALA A 695 ? 0.2717 0.2374 0.3485 -0.0155 -0.0391 -0.0042 736 ALA A CA 5729 C C . ALA A 695 ? 0.2883 0.2505 0.3531 -0.0099 -0.0442 -0.0073 736 ALA A C 5730 O O . ALA A 695 ? 0.2696 0.2309 0.3354 -0.0058 -0.0505 -0.0137 736 ALA A O 5731 C CB . ALA A 695 ? 0.2642 0.2241 0.3512 -0.0199 -0.0383 0.0000 736 ALA A CB 5732 N N . PHE A 696 ? 0.2687 0.2289 0.3218 -0.0092 -0.0414 -0.0029 737 PHE A N 5733 C CA . PHE A 696 ? 0.2905 0.2482 0.3331 -0.0039 -0.0451 -0.0054 737 PHE A CA 5734 C C . PHE A 696 ? 0.2754 0.2379 0.3113 0.0004 -0.0462 -0.0104 737 PHE A C 5735 O O . PHE A 696 ? 0.2781 0.2384 0.3112 0.0053 -0.0511 -0.0153 737 PHE A O 5736 C CB . PHE A 696 ? 0.2864 0.2428 0.3187 -0.0040 -0.0417 0.0000 737 PHE A CB 5737 C CG . PHE A 696 ? 0.3064 0.2629 0.3285 0.0013 -0.0438 -0.0026 737 PHE A CG 5738 C CD1 . PHE A 696 ? 0.3188 0.2703 0.3415 0.0052 -0.0492 -0.0062 737 PHE A CD1 5739 C CD2 . PHE A 696 ? 0.3279 0.2898 0.3413 0.0026 -0.0403 -0.0021 737 PHE A CD2 5740 C CE1 . PHE A 696 ? 0.3484 0.3007 0.3623 0.0106 -0.0503 -0.0088 737 PHE A CE1 5741 C CE2 . PHE A 696 ? 0.3280 0.2906 0.3336 0.0076 -0.0416 -0.0045 737 PHE A CE2 5742 C CZ . PHE A 696 ? 0.3107 0.2686 0.3168 0.0114 -0.0462 -0.0075 737 PHE A CZ 5743 N N . THR A 697 ? 0.2568 0.2253 0.2901 -0.0009 -0.0414 -0.0090 738 THR A N 5744 C CA . THR A 697 ? 0.2732 0.2455 0.2993 0.0032 -0.0418 -0.0126 738 THR A CA 5745 C C . THR A 697 ? 0.2798 0.2522 0.3120 0.0058 -0.0471 -0.0186 738 THR A C 5746 O O . THR A 697 ? 0.2864 0.2580 0.3115 0.0111 -0.0503 -0.0226 738 THR A O 5747 C CB . THR A 697 ? 0.2845 0.2629 0.3077 0.0009 -0.0356 -0.0099 738 THR A CB 5748 O OG1 . THR A 697 ? 0.2906 0.2686 0.3072 -0.0008 -0.0317 -0.0050 738 THR A OG1 5749 C CG2 . THR A 697 ? 0.2620 0.2436 0.2782 0.0051 -0.0357 -0.0130 738 THR A CG2 5750 N N . VAL A 698 ? 0.2770 0.2503 0.3224 0.0021 -0.0481 -0.0191 739 VAL A N 5751 C CA . VAL A 698 ? 0.2773 0.2504 0.3305 0.0045 -0.0546 -0.0255 739 VAL A CA 5752 C C . VAL A 698 ? 0.2909 0.2573 0.3419 0.0088 -0.0618 -0.0299 739 VAL A C 5753 O O . VAL A 698 ? 0.2893 0.2547 0.3349 0.0143 -0.0667 -0.0353 739 VAL A O 5754 C CB . VAL A 698 ? 0.2734 0.2492 0.3438 -0.0005 -0.0542 -0.0253 739 VAL A CB 5755 C CG1 . VAL A 698 ? 0.2625 0.2372 0.3436 0.0019 -0.0631 -0.0327 739 VAL A CG1 5756 C CG2 . VAL A 698 ? 0.2675 0.2504 0.3381 -0.0030 -0.0474 -0.0224 739 VAL A CG2 5757 N N . GLN A 699 ? 0.2874 0.2487 0.3418 0.0066 -0.0623 -0.0276 740 GLN A N 5758 C CA . GLN A 699 ? 0.3036 0.2581 0.3556 0.0109 -0.0688 -0.0319 740 GLN A CA 5759 C C . GLN A 699 ? 0.3038 0.2576 0.3393 0.0173 -0.0684 -0.0333 740 GLN A C 5760 O O . GLN A 699 ? 0.3030 0.2533 0.3336 0.0231 -0.0741 -0.0392 740 GLN A O 5761 C CB . GLN A 699 ? 0.3150 0.2639 0.3728 0.0075 -0.0685 -0.0283 740 GLN A CB 5762 C CG . GLN A 699 ? 0.3463 0.2875 0.4030 0.0120 -0.0755 -0.0331 740 GLN A CG 5763 C CD . GLN A 699 ? 0.3348 0.2732 0.4027 0.0130 -0.0836 -0.0403 740 GLN A CD 5764 O OE1 . GLN A 699 ? 0.3545 0.2957 0.4360 0.0086 -0.0841 -0.0405 740 GLN A OE1 5765 N NE2 . GLN A 699 ? 0.3876 0.3202 0.4507 0.0189 -0.0903 -0.0465 740 GLN A NE2 5766 N N . ALA A 700 ? 0.2817 0.2386 0.3090 0.0163 -0.0620 -0.0281 741 ALA A N 5767 C CA . ALA A 700 ? 0.2865 0.2436 0.3003 0.0218 -0.0605 -0.0288 741 ALA A CA 5768 C C . ALA A 700 ? 0.2890 0.2484 0.2964 0.0264 -0.0616 -0.0327 741 ALA A C 5769 O O . ALA A 700 ? 0.3048 0.2614 0.3034 0.0326 -0.0639 -0.0363 741 ALA A O 5770 C CB . ALA A 700 ? 0.2763 0.2369 0.2847 0.0194 -0.0537 -0.0227 741 ALA A CB 5771 N N . ALA A 701 ? 0.2830 0.2471 0.2946 0.0238 -0.0601 -0.0322 742 ALA A N 5772 C CA . ALA A 701 ? 0.3054 0.2713 0.3116 0.0282 -0.0617 -0.0357 742 ALA A CA 5773 C C . ALA A 701 ? 0.3085 0.2697 0.3158 0.0328 -0.0702 -0.0426 742 ALA A C 5774 O O . ALA A 701 ? 0.3199 0.2789 0.3162 0.0394 -0.0725 -0.0460 742 ALA A O 5775 C CB . ALA A 701 ? 0.2723 0.2441 0.2851 0.0243 -0.0590 -0.0341 742 ALA A CB 5776 N N . ALA A 702 ? 0.3045 0.2637 0.3249 0.0295 -0.0748 -0.0446 743 ALA A N 5777 C CA . ALA A 702 ? 0.3158 0.2700 0.3390 0.0336 -0.0840 -0.0519 743 ALA A CA 5778 C C . ALA A 702 ? 0.3397 0.2878 0.3507 0.0399 -0.0863 -0.0547 743 ALA A C 5779 O O . ALA A 702 ? 0.3278 0.2724 0.3302 0.0468 -0.0917 -0.0604 743 ALA A O 5780 C CB . ALA A 702 ? 0.3011 0.2534 0.3423 0.0281 -0.0878 -0.0528 743 ALA A CB 5781 N N . GLU A 703 ? 0.3095 0.2560 0.3189 0.0381 -0.0821 -0.0507 744 GLU A N 5782 C CA . GLU A 703 ? 0.3332 0.2741 0.3328 0.0440 -0.0838 -0.0533 744 GLU A CA 5783 C C . GLU A 703 ? 0.3383 0.2800 0.3213 0.0508 -0.0805 -0.0538 744 GLU A C 5784 O O . GLU A 703 ? 0.3401 0.2768 0.3140 0.0574 -0.0832 -0.0580 744 GLU A O 5785 C CB . GLU A 703 ? 0.3385 0.2776 0.3417 0.0408 -0.0806 -0.0490 744 GLU A CB 5786 C CG . GLU A 703 ? 0.3823 0.3170 0.4000 0.0366 -0.0857 -0.0502 744 GLU A CG 5787 C CD . GLU A 703 ? 0.4610 0.3931 0.4831 0.0330 -0.0831 -0.0453 744 GLU A CD 5788 O OE1 . GLU A 703 ? 0.5023 0.4362 0.5166 0.0339 -0.0778 -0.0411 744 GLU A OE1 5789 O OE2 . GLU A 703 ? 0.4399 0.3678 0.4743 0.0294 -0.0869 -0.0457 744 GLU A OE2 5790 N N . THR A 704 ? 0.3183 0.2659 0.2976 0.0494 -0.0749 -0.0499 745 THR A N 5791 C CA . THR A 704 ? 0.3250 0.2729 0.2892 0.0557 -0.0716 -0.0500 745 THR A CA 5792 C C . THR A 704 ? 0.3428 0.2867 0.2995 0.0625 -0.0782 -0.0564 745 THR A C 5793 O O . THR A 704 ? 0.3490 0.2908 0.2914 0.0693 -0.0765 -0.0573 745 THR A O 5794 C CB . THR A 704 ? 0.3197 0.2740 0.2820 0.0529 -0.0642 -0.0444 745 THR A CB 5795 O OG1 . THR A 704 ? 0.3435 0.3005 0.3106 0.0510 -0.0665 -0.0453 745 THR A OG1 5796 C CG2 . THR A 704 ? 0.2997 0.2579 0.2689 0.0462 -0.0583 -0.0383 745 THR A CG2 5797 N N . LEU A 705 ? 0.3322 0.2751 0.2988 0.0608 -0.0858 -0.0606 746 LEU A N 5798 C CA . LEU A 705 ? 0.3532 0.2921 0.3140 0.0672 -0.0939 -0.0674 746 LEU A CA 5799 C C . LEU A 705 ? 0.3832 0.3146 0.3425 0.0718 -0.1016 -0.0744 746 LEU A C 5800 O O . LEU A 705 ? 0.3827 0.3094 0.3350 0.0783 -0.1094 -0.0811 746 LEU A O 5801 C CB . LEU A 705 ? 0.3379 0.2805 0.3122 0.0631 -0.0985 -0.0689 746 LEU A CB 5802 C CG . LEU A 705 ? 0.3674 0.3172 0.3434 0.0591 -0.0915 -0.0629 746 LEU A CG 5803 C CD1 . LEU A 705 ? 0.3736 0.3272 0.3653 0.0551 -0.0964 -0.0651 746 LEU A CD1 5804 C CD2 . LEU A 705 ? 0.3754 0.3245 0.3335 0.0658 -0.0882 -0.0618 746 LEU A CD2 5805 N N . SER A 706 ? 0.3893 0.3188 0.3553 0.0686 -0.1004 -0.0733 747 SER A N 5806 C CA . SER A 706 ? 0.4035 0.3251 0.3680 0.0733 -0.1077 -0.0801 747 SER A CA 5807 C C . SER A 706 ? 0.4234 0.3407 0.3672 0.0831 -0.1063 -0.0828 747 SER A C 5808 O O . SER A 706 ? 0.4123 0.3329 0.3454 0.0848 -0.0979 -0.0778 747 SER A O 5809 C CB . SER A 706 ? 0.4203 0.3406 0.3955 0.0681 -0.1056 -0.0773 747 SER A CB 5810 O OG . SER A 706 ? 0.4440 0.3676 0.4375 0.0595 -0.1066 -0.0746 747 SER A OG 5811 N N . GLU A 707 ? 0.4242 0.3338 0.3624 0.0896 -0.1137 -0.0906 748 GLU A N 5812 C CA . GLU A 707 ? 0.4707 0.3760 0.3892 0.0989 -0.1106 -0.0925 748 GLU A CA 5813 C C . GLU A 707 ? 0.4443 0.3529 0.3621 0.0968 -0.0999 -0.0856 748 GLU A C 5814 O O . GLU A 707 ? 0.4446 0.3548 0.3760 0.0903 -0.0986 -0.0825 748 GLU A O 5815 C CB . GLU A 707 ? 0.4939 0.3898 0.4073 0.1060 -0.1202 -0.1024 748 GLU A CB 5816 C CG . GLU A 707 ? 0.5521 0.4452 0.4649 0.1089 -0.1310 -0.1093 748 GLU A CG 5817 C CD . GLU A 707 ? 0.7069 0.5904 0.6090 0.1182 -0.1407 -0.1198 748 GLU A CD 5818 O OE1 . GLU A 707 ? 0.7318 0.6109 0.6466 0.1162 -0.1483 -0.1253 748 GLU A OE1 5819 O OE2 . GLU A 707 ? 0.7574 0.6375 0.6383 0.1275 -0.1406 -0.1224 748 GLU A OE2 5820 N N . VAL A 708 ? 0.4462 0.3561 0.3489 0.1020 -0.0922 -0.0826 749 VAL A N 5821 C CA . VAL A 708 ? 0.4284 0.3436 0.3328 0.0989 -0.0816 -0.0752 749 VAL A CA 5822 C C . VAL A 708 ? 0.4506 0.3623 0.3563 0.1015 -0.0808 -0.0771 749 VAL A C 5823 O O . VAL A 708 ? 0.4482 0.3640 0.3603 0.0977 -0.0745 -0.0717 749 VAL A O 5824 C CB . VAL A 708 ? 0.4215 0.3396 0.3117 0.1032 -0.0729 -0.0709 749 VAL A CB 5825 C CG1 . VAL A 708 ? 0.4411 0.3627 0.3314 0.1003 -0.0737 -0.0686 749 VAL A CG1 5826 C CG2 . VAL A 708 ? 0.4377 0.3490 0.3087 0.1146 -0.0732 -0.0762 749 VAL A CG2 5827 N N . ALA A 709 ? 0.4786 0.3824 0.3786 0.1080 -0.0879 -0.0851 750 ALA A N 5828 C CA . ALA A 709 ? 0.5206 0.4200 0.4206 0.1118 -0.0877 -0.0881 750 ALA A CA 5829 C C . ALA A 709 ? 0.5626 0.4526 0.4577 0.1181 -0.0982 -0.0983 750 ALA A C 5830 O O . ALA A 709 ? 0.5938 0.4786 0.4900 0.1216 -0.1004 -0.1025 750 ALA A O 5831 C CB . ALA A 709 ? 0.5252 0.4263 0.4123 0.1181 -0.0778 -0.0855 750 ALA A CB 5832 O OXT . ALA A 709 ? 0.5859 0.4731 0.4754 0.1206 -0.1050 -0.1029 750 ALA A OXT 6009 ZN ZN . ZN O . ? 0.3334 0.3418 0.3703 0.0265 0.0200 -0.0413 814 ZN A ZN 6010 ZN ZN . ZN P . ? 0.3061 0.3074 0.3363 0.0315 0.0117 -0.0315 815 ZN A ZN 6011 CA CA . CA Q . ? 0.2724 0.2810 0.2802 -0.0005 0.0004 -0.0195 816 CA A CA 6012 CL CL . CL R . ? 0.3708 0.3755 0.3930 0.0439 -0.0137 -0.0267 817 CL A CL 6041 O O . HOH T . ? 0.2642 0.2571 0.2676 0.0166 0.0156 -0.0167 901 HOH A O 6042 O O . HOH T . ? 0.3236 0.3316 0.2811 -0.0048 0.0033 -0.0085 902 HOH A O 6043 O O . HOH T . ? 0.3495 0.3069 0.2910 0.0610 -0.0579 -0.0423 903 HOH A O 6044 O O . HOH T . ? 0.3232 0.3147 0.3260 0.0339 0.0057 -0.0170 904 HOH A O 6045 O O . HOH T . ? 0.2699 0.2748 0.2601 0.0145 0.0070 -0.0153 905 HOH A O 6046 O O . HOH T . ? 0.3051 0.3135 0.2977 -0.0011 -0.0011 -0.0224 906 HOH A O 6047 O O . HOH T . ? 0.3148 0.3254 0.3145 -0.0009 -0.0035 -0.0095 907 HOH A O 6048 O O . HOH T . ? 0.3817 0.3374 0.4482 0.0289 0.0229 -0.0676 908 HOH A O 6049 O O . HOH T . ? 0.3054 0.3162 0.3202 0.0150 0.0277 -0.0489 909 HOH A O 6050 O O . HOH T . ? 0.3292 0.3052 0.2693 0.0541 -0.0327 -0.0231 910 HOH A O 6051 O O . HOH T . ? 0.2947 0.2735 0.3289 0.0183 0.0208 -0.0414 911 HOH A O 6052 O O . HOH T . ? 0.3238 0.3067 0.2629 0.0666 0.0398 0.0087 912 HOH A O 6053 O O . HOH T . ? 0.3857 0.2858 0.4436 0.0578 0.0245 -0.0007 913 HOH A O 6054 O O . HOH T . ? 0.3393 0.3174 0.3378 0.0022 -0.0290 -0.0013 914 HOH A O 6055 O O . HOH T . ? 0.3324 0.3030 0.2903 0.0440 -0.0396 -0.0268 915 HOH A O 6056 O O . HOH T . ? 0.3130 0.3034 0.3572 0.0327 0.0200 -0.0428 916 HOH A O 6057 O O . HOH T . ? 0.3408 0.3362 0.3100 0.0420 0.0084 -0.0020 917 HOH A O 6058 O O . HOH T . ? 0.2728 0.3136 0.4209 0.0619 0.0159 -0.0693 918 HOH A O 6059 O O . HOH T . ? 0.3656 0.2970 0.3082 0.0737 -0.0804 -0.0627 919 HOH A O 6060 O O . HOH T . ? 0.3688 0.3381 0.2744 0.0787 0.0343 0.0056 920 HOH A O 6061 O O . HOH T . ? 0.4329 0.4278 0.4396 0.0566 -0.0282 -0.0252 921 HOH A O 6062 O O . HOH T . ? 0.4343 0.3687 0.3088 0.0989 -0.0499 -0.0501 922 HOH A O 6063 O O . HOH T . ? 0.3600 0.3907 0.3921 -0.0197 0.0404 0.0000 923 HOH A O 6064 O O . HOH T . ? 0.3533 0.3610 0.3885 0.0200 0.0378 0.0110 924 HOH A O 6065 O O . HOH T . ? 0.3571 0.3756 0.3513 0.0189 0.0502 -0.0719 925 HOH A O 6066 O O . HOH T . ? 0.3782 0.3484 0.3489 0.0834 -0.1071 -0.0632 926 HOH A O 6067 O O . HOH T . ? 0.3339 0.3232 0.2891 0.0537 0.0280 0.0054 927 HOH A O 6068 O O . HOH T . ? 0.3466 0.3223 0.3285 0.0052 -0.0296 0.0054 928 HOH A O 6069 O O . HOH T . ? 0.3695 0.4543 0.4816 0.0276 0.0995 -0.0726 929 HOH A O 6070 O O . HOH T . ? 0.3318 0.3878 0.3854 0.0132 0.0655 -0.0519 930 HOH A O 6071 O O . HOH T . ? 0.3580 0.3517 0.3123 0.0249 0.0404 -0.1015 931 HOH A O 6072 O O . HOH T . ? 0.3787 0.3595 0.4418 0.0411 0.0217 -0.0520 932 HOH A O 6073 O O . HOH T . ? 0.3505 0.4010 0.4577 0.0536 0.0826 -0.1056 933 HOH A O 6074 O O . HOH T . ? 0.3792 0.3321 0.3658 0.0375 -0.0596 -0.0333 934 HOH A O 6075 O O . HOH T . ? 0.3401 0.3343 0.3084 0.0249 -0.0117 -0.0089 935 HOH A O 6076 O O . HOH T . ? 0.3459 0.2941 0.3957 0.0444 0.0190 -0.0242 936 HOH A O 6077 O O . HOH T . ? 0.3641 0.3227 0.4238 0.0104 0.0266 -0.0208 937 HOH A O 6078 O O . HOH T . ? 0.3662 0.3735 0.3524 0.0103 -0.0004 -0.0062 938 HOH A O 6079 O O . HOH T . ? 0.4127 0.3540 0.2561 0.1088 0.0031 -0.0191 939 HOH A O 6080 O O . HOH T . ? 0.4275 0.3663 0.3743 0.0584 0.0696 0.0487 940 HOH A O 6081 O O . HOH T . ? 0.3523 0.3524 0.3592 0.0175 0.0313 -0.0708 941 HOH A O 6082 O O . HOH T . ? 0.4511 0.3559 0.6410 -0.0849 0.0629 0.1093 942 HOH A O 6083 O O . HOH T . ? 0.3968 0.4275 0.4848 -0.0393 0.0683 0.0237 943 HOH A O 6084 O O . HOH T . ? 0.3392 0.3699 0.4811 -0.0266 0.0005 -0.0109 944 HOH A O 6085 O O . HOH T . ? 0.3522 0.3924 0.3848 0.0123 0.0473 -0.0481 945 HOH A O 6086 O O . HOH T . ? 0.3616 0.3998 0.4141 0.0358 0.0718 -0.0881 946 HOH A O 6087 O O . HOH T . ? 0.3787 0.4075 0.3687 -0.0075 0.0379 -0.0162 947 HOH A O 6088 O O . HOH T . ? 0.3360 0.3752 0.4327 0.0410 0.0480 -0.0754 948 HOH A O 6089 O O . HOH T . ? 0.3537 0.2912 0.4324 0.0219 0.0230 -0.0454 949 HOH A O 6090 O O . HOH T . ? 0.4071 0.4380 0.4722 0.0613 0.0937 -0.1297 950 HOH A O 6091 O O . HOH T . ? 0.3828 0.3179 0.4672 0.0717 0.0088 -0.0350 951 HOH A O 6092 O O . HOH T . ? 0.4719 0.4294 0.4447 0.0263 0.0067 -0.1374 952 HOH A O 6093 O O . HOH T . ? 0.4064 0.4414 0.5568 0.0489 -0.1093 -0.0770 953 HOH A O 6094 O O . HOH T . ? 0.4089 0.4331 0.4295 -0.0152 0.0248 -0.0032 954 HOH A O 6095 O O . HOH T . ? 0.3937 0.3901 0.4524 0.0378 0.0222 -0.0515 955 HOH A O 6096 O O . HOH T . ? 0.3808 0.3552 0.4599 0.0496 0.0213 -0.0575 956 HOH A O 6097 O O . HOH T . ? 0.3698 0.3804 0.3545 0.0028 0.0105 -0.0227 957 HOH A O 6098 O O . HOH T . ? 0.3125 0.3144 0.3485 -0.0075 -0.0099 -0.0423 958 HOH A O 6099 O O . HOH T . ? 0.5079 0.4360 0.3295 0.1143 -0.0294 -0.0228 959 HOH A O 6100 O O . HOH T . ? 0.3852 0.3796 0.3353 -0.0061 -0.0074 0.0071 960 HOH A O 6101 O O . HOH T . ? 0.3987 0.3408 0.4722 -0.0388 -0.0030 0.0436 961 HOH A O 6102 O O . HOH T . ? 0.3916 0.4007 0.3727 0.0053 0.0025 -0.0125 962 HOH A O 6103 O O . HOH T . ? 0.3956 0.3611 0.3884 0.0520 0.0052 -0.0055 963 HOH A O 6104 O O . HOH T . ? 0.4199 0.3051 0.4596 0.0585 0.0349 0.0226 964 HOH A O 6105 O O . HOH T . ? 0.3813 0.4294 0.4370 0.0175 0.0525 -0.0543 965 HOH A O 6106 O O . HOH T . ? 0.3673 0.3514 0.3369 0.0285 -0.0258 -0.0143 966 HOH A O 6107 O O . HOH T . ? 0.3796 0.3635 0.3574 0.0205 -0.0275 -0.0102 967 HOH A O 6108 O O . HOH T . ? 0.3546 0.3588 0.3551 0.0264 0.0243 0.0058 968 HOH A O 6109 O O . HOH T . ? 0.4191 0.4237 0.3988 0.0127 -0.0043 -0.0054 969 HOH A O 6110 O O . HOH T . ? 0.3938 0.3434 0.4770 0.0057 0.0293 -0.0200 970 HOH A O 6111 O O . HOH T . ? 0.3828 0.3952 0.3869 0.0126 0.0000 -0.0039 971 HOH A O 6112 O O . HOH T . ? 0.4526 0.4258 0.4005 0.0555 -0.0483 -0.0329 972 HOH A O 6113 O O . HOH T . ? 0.3356 0.3866 0.4771 0.0429 -0.0572 -0.0576 973 HOH A O 6114 O O . HOH T . ? 0.3198 0.3088 0.3492 -0.0202 -0.0034 0.0120 974 HOH A O 6115 O O . HOH T . ? 0.3925 0.3620 0.4618 0.0449 0.0360 -0.1060 975 HOH A O 6116 O O . HOH T . ? 0.5034 0.4217 0.4814 0.0778 -0.1335 -0.0973 976 HOH A O 6117 O O . HOH T . ? 0.3962 0.4667 0.6079 0.0742 -0.0351 -0.0713 977 HOH A O 6118 O O . HOH T . ? 0.3468 0.3986 0.4403 0.0353 0.0601 -0.0752 978 HOH A O 6119 O O . HOH T . ? 0.4020 0.4080 0.3908 0.0200 0.0016 -0.0024 979 HOH A O 6120 O O . HOH T . ? 0.4632 0.3746 0.3479 0.1088 -0.1048 -0.0869 980 HOH A O 6121 O O . HOH T . ? 0.4699 0.4855 0.5054 0.0530 0.0795 -0.1251 981 HOH A O 6122 O O . HOH T . ? 0.5217 0.4622 0.3747 0.0994 -0.0289 -0.0260 982 HOH A O 6123 O O . HOH T . ? 0.4376 0.4129 0.4330 0.0296 0.0303 -0.1171 983 HOH A O 6124 O O . HOH T . ? 0.4030 0.3385 0.4097 0.0533 0.0205 0.0065 984 HOH A O 6125 O O . HOH T . ? 0.4979 0.4399 0.4897 0.0515 0.0217 0.0102 985 HOH A O 6126 O O . HOH T . ? 0.3676 0.3504 0.3835 0.0672 -0.1088 -0.0681 986 HOH A O 6127 O O . HOH T . ? 0.4343 0.3619 0.5532 0.0030 0.0183 -0.0517 987 HOH A O 6128 O O . HOH T . ? 0.6049 0.6380 0.6514 0.0122 0.0033 -0.0286 988 HOH A O 6129 O O . HOH T . ? 0.4467 0.4673 0.4982 0.0169 -0.0300 -0.0316 989 HOH A O 6130 O O . HOH T . ? 0.4354 0.4668 0.4890 0.0200 -0.0076 -0.0317 990 HOH A O 6131 O O . HOH T . ? 0.3450 0.4026 0.5133 0.0608 -0.0014 -0.0654 991 HOH A O 6132 O O . HOH T . ? 0.4435 0.3846 0.4360 0.0406 -0.0679 -0.0378 992 HOH A O 6133 O O . HOH T . ? 0.4617 0.4387 0.5609 0.1342 -0.0898 -0.0427 993 HOH A O 6134 O O . HOH T . ? 0.4545 0.4974 0.5203 -0.0210 0.0464 -0.0039 994 HOH A O 6135 O O . HOH T . ? 0.6224 0.5020 0.3518 0.1764 -0.1090 -0.0513 995 HOH A O 6136 O O . HOH T . ? 0.3649 0.4190 0.6294 -0.0307 -0.0247 -0.0343 996 HOH A O 6137 O O . HOH T . ? 0.4120 0.4216 0.4115 0.0111 0.0038 -0.0048 997 HOH A O 6138 O O . HOH T . ? 0.5815 0.4711 0.4437 0.1693 -0.1033 -0.0008 998 HOH A O 6139 O O . HOH T . ? 0.5229 0.4310 0.2946 0.1397 -0.0340 -0.0318 999 HOH A O 6140 O O . HOH T . ? 0.4813 0.4289 0.4310 0.0865 -0.1196 -0.0785 1000 HOH A O 6141 O O . HOH T . ? 0.6006 0.4638 0.4990 0.1754 -0.0850 0.0226 1001 HOH A O 6142 O O . HOH T . ? 0.5636 0.4561 0.3321 0.1624 -0.1199 -0.0666 1002 HOH A O 6143 O O . HOH T . ? 0.5031 0.3938 0.5401 0.0395 0.0886 0.0679 1003 HOH A O 6144 O O . HOH T . ? 0.5470 0.5787 0.5141 -0.0081 0.0681 -0.0146 1004 HOH A O 6145 O O . HOH T . ? 0.3612 0.3502 0.3507 -0.0089 -0.0106 0.0080 1005 HOH A O 6146 O O . HOH T . ? 0.3906 0.3779 0.3480 0.0195 0.0260 -0.0988 1006 HOH A O 6147 O O . HOH T . ? 0.3845 0.3410 0.4825 -0.0026 0.0225 -0.0302 1007 HOH A O 6148 O O . HOH T . ? 0.5001 0.5012 0.4737 0.0064 -0.0149 -0.0020 1008 HOH A O 6149 O O . HOH T . ? 0.4481 0.4884 0.6076 0.0971 -0.1176 -0.0755 1009 HOH A O 6150 O O . HOH T . ? 0.4400 0.3826 0.5449 -0.0493 0.0100 0.0516 1010 HOH A O 6151 O O . HOH T . ? 0.4520 0.4533 0.4890 -0.0173 -0.0025 0.0031 1011 HOH A O 6152 O O . HOH T . ? 0.4578 0.4092 0.5275 0.0402 0.0279 -0.1112 1012 HOH A O 6153 O O . HOH T . ? 0.4377 0.4919 0.4646 -0.0100 0.0863 -0.0167 1013 HOH A O 6154 O O . HOH T . ? 0.5420 0.4854 0.6806 -0.0440 -0.0185 0.0267 1014 HOH A O 6155 O O . HOH T . ? 0.4258 0.4167 0.6051 0.0053 -0.1073 -0.0702 1015 HOH A O 6156 O O . HOH T . ? 0.4431 0.4778 0.5682 -0.0293 0.0197 -0.0030 1016 HOH A O 6157 O O . HOH T . ? 0.4131 0.4227 0.3997 0.0058 0.0079 -0.0176 1017 HOH A O 6158 O O . HOH T . ? 0.4336 0.4557 0.5735 0.0770 0.0712 -0.1297 1018 HOH A O 6159 O O . HOH T . ? 0.5117 0.4890 0.4407 0.0132 -0.0057 -0.1034 1019 HOH A O 6160 O O . HOH T . ? 0.5362 0.4796 0.4954 0.0939 -0.1429 -0.0930 1020 HOH A O 6161 O O . HOH T . ? 0.4517 0.4144 0.5454 0.0463 -0.1454 -0.0964 1021 HOH A O 6162 O O . HOH T . ? 0.4285 0.3944 0.5426 -0.0112 0.0089 -0.0453 1022 HOH A O 6163 O O . HOH T . ? 0.4538 0.3749 0.5335 0.0248 -0.1112 -0.0644 1023 HOH A O 6164 O O . HOH T . ? 0.5871 0.4664 0.4850 0.1741 -0.0980 0.0097 1024 HOH A O 6165 O O . HOH T . ? 0.4173 0.3975 0.5459 0.0369 -0.1397 -0.0925 1025 HOH A O 6166 O O . HOH T . ? 0.4672 0.4300 0.3586 0.0822 0.0171 -0.0036 1026 HOH A O 6167 O O . HOH T . ? 0.6106 0.4448 0.4099 0.1405 0.0336 0.0842 1027 HOH A O 6168 O O . HOH T . ? 0.4405 0.4609 0.4137 -0.0094 0.0306 -0.0098 1028 HOH A O 6169 O O . HOH T . ? 0.4109 0.3722 0.4106 0.0328 0.0234 -0.1331 1029 HOH A O 6170 O O . HOH T . ? 0.5379 0.5339 0.6505 0.1619 -0.1820 -0.0762 1030 HOH A O 6171 O O . HOH T . ? 0.4198 0.3637 0.4951 0.0225 0.0204 -0.0633 1031 HOH A O 6172 O O . HOH T . ? 0.4178 0.3713 0.3919 0.0557 0.0112 0.0060 1032 HOH A O 6173 O O . HOH T . ? 0.5567 0.5794 0.5601 -0.0249 0.0633 0.0153 1033 HOH A O 6174 O O . HOH T . ? 0.4456 0.4654 0.4179 -0.0030 0.0248 -0.0225 1034 HOH A O 6175 O O . HOH T . ? 0.4844 0.5336 0.5808 0.0056 0.0006 -0.0323 1035 HOH A O 6176 O O . HOH T . ? 0.4131 0.4375 0.4924 0.0209 -0.0458 -0.0411 1036 HOH A O 6177 O O . HOH T . ? 0.5602 0.5600 0.5732 0.0756 0.0963 -0.1684 1037 HOH A O 6178 O O . HOH T . ? 0.4060 0.4740 0.5099 -0.0090 0.0540 -0.0247 1038 HOH A O 6179 O O . HOH T . ? 0.5124 0.5047 0.4937 0.0482 0.0651 -0.1357 1039 HOH A O 6180 O O . HOH T . ? 0.4277 0.4905 0.6017 0.0473 -0.0602 -0.0637 1040 HOH A O 6181 O O . HOH T . ? 0.5839 0.4858 0.4535 0.1183 -0.0997 -0.0912 1041 HOH A O 6182 O O . HOH T . ? 0.6608 0.5271 0.3461 0.1808 -0.0532 -0.0130 1042 HOH A O 6183 O O . HOH T . ? 0.4576 0.4609 0.4665 0.0443 0.0657 -0.1202 1043 HOH A O 6184 O O . HOH T . ? 0.4484 0.4741 0.5555 -0.0516 0.1009 0.0469 1044 HOH A O 6185 O O . HOH T . ? 0.4731 0.4656 0.4514 -0.0355 0.0840 0.0534 1045 HOH A O 6186 O O . HOH T . ? 0.4067 0.3880 0.6235 -0.0219 -0.0814 -0.0460 1046 HOH A O 6187 O O . HOH T . ? 0.4877 0.5036 0.5622 -0.0112 -0.0490 -0.0576 1047 HOH A O 6188 O O . HOH T . ? 0.5368 0.4833 0.5297 0.1486 -0.1188 -0.0324 1048 HOH A O 6189 O O . HOH T . ? 0.5352 0.4838 0.5531 0.0292 0.0121 -0.1368 1049 HOH A O 6190 O O . HOH T . ? 0.3959 0.4361 0.5383 0.0070 -0.0447 -0.0449 1050 HOH A O 6191 O O . HOH T . ? 0.5006 0.4682 0.5018 0.0405 0.0362 -0.1371 1051 HOH A O 6192 O O . HOH T . ? 0.6042 0.4934 0.5471 0.1085 -0.1696 -0.1312 1052 HOH A O 6193 O O . HOH T . ? 0.6260 0.5828 0.6463 0.0086 -0.0117 -0.1162 1053 HOH A O 6194 O O . HOH T . ? 0.5444 0.4857 0.6298 -0.0333 -0.0199 0.0292 1054 HOH A O 6195 O O . HOH T . ? 0.5675 0.4684 0.5359 0.0837 -0.1311 -0.1010 1055 HOH A O 6196 O O . HOH T . ? 0.5817 0.4755 0.3129 0.1587 -0.0263 -0.0329 1056 HOH A O 6197 O O . HOH T . ? 0.4731 0.4225 0.7053 -0.0418 -0.0631 -0.0175 1057 HOH A O 6198 O O . HOH T . ? 0.5341 0.5898 0.6751 0.0311 -0.0382 -0.0519 1058 HOH A O 6199 O O . HOH T . ? 0.7231 0.5834 0.4453 0.2053 -0.1406 -0.0304 1059 HOH A O 6200 O O . HOH T . ? 0.4769 0.4609 0.4352 0.0101 0.0051 -0.0902 1060 HOH A O 6201 O O . HOH T . ? 0.5333 0.6547 0.7181 0.0726 0.1730 -0.1286 1061 HOH A O 6202 O O . HOH T . ? 0.5912 0.4671 0.2749 0.1786 -0.0245 -0.0285 1062 HOH A O 6203 O O . HOH T . ? 0.5487 0.4996 0.6737 -0.0067 0.0297 -0.0208 1063 HOH A O 6204 O O . HOH T . ? 0.4274 0.4587 0.5524 -0.0124 -0.0372 -0.0426 1064 HOH A O 6205 O O . HOH T . ? 0.5214 0.6094 0.6743 0.0101 0.0520 -0.0474 1065 HOH A O 6206 O O . HOH T . ? 0.4618 0.4717 0.5903 -0.0060 0.0354 0.0003 1066 HOH A O 6207 O O . HOH T . ? 0.6004 0.5715 0.7662 0.1031 -0.0027 -0.0700 1067 HOH A O 6208 O O . HOH T . ? 0.4459 0.5366 0.5863 -0.0081 0.0856 -0.0296 1068 HOH A O 6209 O O . HOH T . ? 0.3598 0.3690 0.3454 0.0061 -0.0070 -0.0070 1069 HOH A O 6210 O O . HOH T . ? 0.5606 0.4688 0.5223 0.0619 0.1102 0.0833 1070 HOH A O 6211 O O . HOH T . ? 0.5278 0.4649 0.4997 0.0621 0.0163 0.0149 1071 HOH A O 6212 O O . HOH T . ? 0.5059 0.5440 0.5882 -0.0430 0.1118 0.0372 1072 HOH A O 6213 O O . HOH T . ? 0.7973 0.7527 0.6326 -0.0186 0.1123 0.0788 1073 HOH A O 6214 O O . HOH T . ? 0.5249 0.5294 0.4910 -0.0150 0.0197 0.0086 1074 HOH A O 6215 O O . HOH T . ? 0.5495 0.5983 0.6955 -0.0287 0.0272 -0.0076 1075 HOH A O 6216 O O . HOH T . ? 0.5402 0.6384 0.6437 -0.0117 0.1723 -0.0108 1076 HOH A O 6217 O O . HOH T . ? 0.4731 0.4571 0.4783 0.0397 0.0468 -0.1232 1077 HOH A O 6218 O O . HOH T . ? 0.4434 0.4495 0.5905 0.0780 0.0540 -0.1198 1078 HOH A O 6219 O O . HOH T . ? 0.7267 0.6245 0.6110 -0.0395 0.1144 0.1426 1079 HOH A O 6220 O O . HOH T . ? 0.4613 0.4195 0.5524 0.0517 0.0329 -0.1039 1080 HOH A O 6221 O O . HOH T . ? 0.5353 0.4654 0.4615 0.1647 -0.1497 -0.0419 1081 HOH A O 6222 O O . HOH T . ? 0.6816 0.5495 0.4037 0.1897 -0.1132 -0.0270 1082 HOH A O 6224 O O . HOH T . ? 0.5854 0.5504 0.6674 -0.0068 -0.0046 -0.0716 1084 HOH A O 6225 O O . HOH T . ? 0.6567 0.6408 0.6209 0.0915 0.1070 -0.2002 1085 HOH A O 6226 O O . HOH T . ? 0.5857 0.7148 0.7890 0.0013 0.1370 -0.0434 1086 HOH A O 6227 O O . HOH T . ? 0.5155 0.5067 0.5439 0.0468 0.0559 -0.1243 1087 HOH A O 6228 O O . HOH T . ? 0.4583 0.4648 0.5171 0.0573 0.0703 -0.1280 1088 HOH A O 6229 O O . HOH T . ? 0.6690 0.6861 0.4650 0.0717 0.1887 -0.1138 1089 HOH A O 6230 O O . HOH T . ? 0.4160 0.3340 0.4935 0.0213 0.0871 0.0538 1090 HOH A O 6231 O O . HOH T . ? 0.5448 0.5153 0.7935 -0.0605 -0.0159 0.0123 1091 HOH A O 6232 O O . HOH T . ? 0.5927 0.5862 0.7899 -0.0873 0.1600 0.1098 1092 HOH A O 6233 O O . HOH T . ? 0.4828 0.3792 0.5448 0.0466 0.0340 0.0065 1093 HOH A O 6234 O O . HOH T . ? 0.5588 0.5304 0.4398 0.0187 -0.0154 -0.1098 1094 HOH A O 6235 O O . HOH T . ? 0.4844 0.5312 0.6762 0.1079 -0.1065 -0.0750 1095 HOH A O 6236 O O . HOH T . ? 0.5756 0.5777 0.6911 0.1550 -0.2412 -0.1163 1096 HOH A O 6237 O O . HOH T . ? 0.4956 0.4811 0.4817 -0.0147 -0.0032 0.0164 1097 HOH A O 6238 O O . HOH T . ? 0.5625 0.5203 0.5479 0.0995 -0.1591 -0.0960 1098 HOH A O 6239 O O . HOH T . ? 0.5992 0.5434 0.5373 0.1498 -0.1931 -0.0918 1099 HOH A O 6240 O O . HOH T . ? 0.4741 0.4286 0.4544 -0.0133 -0.0179 0.0328 1100 HOH A O 6241 O O . HOH T . ? 0.7043 0.8042 0.7313 0.0530 0.2267 -0.0925 1101 HOH A O 6242 O O . HOH T . ? 0.4552 0.5277 0.7186 0.1157 -0.1334 -0.0932 1102 HOH A O 6243 O O . HOH T . ? 0.4742 0.4990 0.7100 -0.0038 -0.0933 -0.0678 1103 HOH A O 6244 O O . HOH T . ? 0.5545 0.5018 0.5177 0.0200 -0.0266 -0.1514 1104 HOH A O 6245 O O . HOH T . ? 0.6138 0.6768 0.6923 -0.0256 0.1070 0.0044 1105 HOH A O 6246 O O . HOH T . ? 0.4913 0.4627 0.4825 0.0351 0.0526 0.0266 1106 HOH A O 6247 O O . HOH T . ? 0.6673 0.5140 0.6143 0.0775 0.1081 0.1084 1107 HOH A O 6248 O O . HOH T . ? 0.6063 0.5723 0.5986 0.0710 0.0659 -0.1818 1108 HOH A O 6249 O O . HOH T . ? 0.5384 0.5911 0.6205 -0.0247 0.0675 -0.0007 1109 HOH A O 6250 O O . HOH T . ? 0.6284 0.5607 0.5530 -0.0273 0.0323 0.0791 1110 HOH A O 6251 O O . HOH T . ? 0.5731 0.5175 0.7162 0.0906 0.0090 -0.0684 1111 HOH A O 6252 O O . HOH T . ? 0.7547 0.7333 0.4432 0.0662 0.1486 -0.0921 1112 HOH A O 6253 O O . HOH T . ? 0.5073 0.4474 0.5581 0.0260 0.0865 0.0517 1113 HOH A O 6254 O O . HOH T . ? 0.8640 0.7611 0.6820 0.1521 -0.1541 -0.1001 1114 HOH A O 6255 O O . HOH T . ? 0.4832 0.4927 0.4059 0.0032 0.0327 -0.0441 1115 HOH A O 6256 O O . HOH T . ? 0.6598 0.6452 0.5869 -0.0083 -0.0041 0.0162 1116 HOH A O 6257 O O . HOH T . ? 0.4897 0.4725 0.5426 -0.0095 -0.0321 -0.0841 1117 HOH A O 6258 O O . HOH T . ? 0.5137 0.4983 0.7262 -0.0096 -0.1008 -0.0629 1118 HOH A O 6259 O O . HOH T . ? 0.6700 0.6288 0.6265 -0.0457 0.1298 0.1031 1119 HOH A O 6260 O O . HOH T . ? 0.3756 0.3907 0.3590 0.0015 0.0136 -0.0226 1120 HOH A O 6261 O O . HOH T . ? 0.5907 0.5638 0.8801 -0.1087 0.1572 0.1259 1121 HOH A O 6262 O O . HOH T . ? 0.5843 0.5832 0.5603 0.0196 -0.0103 -0.0050 1122 HOH A O 6263 O O . HOH T . ? 0.5853 0.6224 0.6318 -0.0400 0.1479 0.0479 1123 HOH A O 6264 O O . HOH T . ? 0.5289 0.6289 0.6978 0.0182 0.0744 -0.0587 1124 HOH A O 6265 O O . HOH T . ? 0.7283 0.7737 0.7518 -0.0330 0.1860 0.0488 1125 HOH A O 6266 O O . HOH T . ? 0.4450 0.4586 0.4450 -0.0026 -0.0228 -0.0247 1126 HOH A O 6267 O O . HOH T . ? 0.5965 0.5524 0.5812 0.1426 -0.1297 -0.0433 1127 HOH A O 6268 O O . HOH T . ? 0.5679 0.4921 0.6122 0.0203 -0.0807 -0.0335 1128 HOH A O 6269 O O . HOH T . ? 0.5772 0.6365 0.6618 0.0835 0.1455 -0.1556 1129 HOH A O 6270 O O . HOH T . ? 0.5330 0.5583 0.5091 -0.0032 0.0362 -0.0245 1130 HOH A O 6271 O O . HOH T . ? 0.5923 0.4392 0.6042 0.0944 0.0212 0.0420 1131 HOH A O 6272 O O . HOH T . ? 0.8932 0.7170 0.5637 0.1757 0.0689 0.0905 1132 HOH A O 6273 O O . HOH T . ? 0.7433 0.6018 0.4205 0.1797 -0.0235 0.0136 1133 HOH A O 6274 O O . HOH T . ? 0.6656 0.6705 0.6262 -0.0278 0.0855 0.0376 1134 HOH A O 6275 O O . HOH T . ? 0.6879 0.5018 0.4955 0.1726 -0.0264 0.0715 1135 HOH A O 6276 O O . HOH T . ? 0.6321 0.6174 0.4120 0.0231 0.0722 -0.0456 1136 HOH A O 6277 O O . HOH T . ? 0.5715 0.5810 0.5466 -0.0258 0.0656 0.0260 1137 HOH A O 6278 O O . HOH T . ? 0.7313 0.5975 0.7810 0.0440 0.0771 0.0634 1138 HOH A O 6279 O O . HOH T . ? 0.6211 0.5100 0.6823 0.1308 -0.0343 -0.0032 1139 HOH A O 6280 O O . HOH T . ? 0.5163 0.3957 0.5889 0.0342 0.0661 0.0436 1140 HOH A O 6281 O O . HOH T . ? 0.6186 0.5301 0.6043 -0.0461 0.0556 0.1065 1141 HOH A O 6282 O O . HOH T . ? 0.4890 0.5396 0.5621 0.0187 0.0410 -0.0497 1142 HOH A O 6283 O O . HOH T . ? 0.5529 0.5633 0.5334 -0.0020 -0.0330 -0.0289 1143 HOH A O 6284 O O . HOH T . ? 0.6562 0.5857 0.6824 0.0906 -0.1954 -0.1326 1144 HOH A O 6285 O O . HOH T . ? 0.6623 0.7469 0.7979 0.0721 0.1401 -0.1324 1145 HOH A O 6286 O O . HOH T . ? 0.5564 0.4748 0.8146 -0.0586 -0.0485 0.0096 1146 HOH A O 6287 O O . HOH T . ? 0.6431 0.6024 0.7393 0.0057 0.0623 0.0230 1147 HOH A O 6288 O O . HOH T . ? 0.5471 0.6043 0.7339 0.0818 0.0816 -0.1271 1148 HOH A O 6289 O O . HOH T . ? 0.5249 0.5216 0.6244 -0.0082 0.0197 -0.0154 1149 HOH A O 6290 O O . HOH T . ? 0.5797 0.5856 0.5670 -0.0188 0.0227 0.0115 1150 HOH A O 6291 O O . HOH T . ? 0.4420 0.5139 0.6492 0.0681 -0.0122 -0.0718 1151 HOH A O 6292 O O . HOH T . ? 0.6549 0.6981 0.6058 0.0923 0.1870 -0.1667 1152 HOH A O 6293 O O . HOH T . ? 0.6369 0.7153 0.7174 -0.0254 0.1768 0.0170 1153 HOH A O 6294 O O . HOH T . ? 0.8918 0.7325 0.5105 0.1988 0.0128 0.0269 1154 HOH A O 6295 O O . HOH T . ? 0.6349 0.6061 0.3983 0.0397 0.0483 -0.0970 1155 HOH A O 6296 O O . HOH T . ? 0.5768 0.6090 0.6745 -0.0508 0.1251 0.0516 1156 HOH A O 6297 O O . HOH T . ? 0.4915 0.5842 0.7451 0.0685 -0.0325 -0.0778 1157 HOH A O 6298 O O . HOH T . ? 0.7921 0.7238 0.6459 0.0667 0.0192 -0.2077 1158 HOH A O 6299 O O . HOH T . ? 0.4997 0.4858 0.5152 0.0238 0.0460 0.0180 1159 HOH A O 6300 O O . HOH T . ? 0.5685 0.5792 0.6364 0.0053 0.0291 0.0021 1160 HOH A O 6301 O O . HOH T . ? 0.6247 0.5087 0.6355 0.0493 0.1029 0.0842 1161 HOH A O 6302 O O . HOH T . ? 0.6390 0.6576 0.5261 -0.0013 0.1138 -0.0036 1162 HOH A O 6303 O O . HOH T . ? 0.6813 0.7696 0.6856 0.0442 0.2092 -0.0817 1163 HOH A O 6304 O O . HOH T . ? 0.6017 0.5033 0.6920 0.0879 0.0037 -0.0226 1164 HOH A O 6305 O O . HOH T . ? 0.7708 0.6964 0.6349 0.1249 -0.1229 -0.0729 1165 HOH A O 6306 O O . HOH T . ? 0.6559 0.5711 0.7184 0.1447 -0.0640 -0.0141 1166 HOH A O 6307 O O . HOH T . ? 0.5760 0.5229 0.7427 0.0914 0.0286 -0.1113 1167 HOH A O 6308 O O . HOH T . ? 0.5889 0.5136 0.6001 0.0386 -0.0793 -0.0406 1168 HOH A O 6309 O O . HOH T . ? 0.5734 0.5234 0.6228 0.0149 0.0060 -0.1054 1169 HOH A O 6310 O O . HOH T . ? 0.6780 0.5681 0.4264 0.1433 0.0816 0.0540 1170 HOH A O 6311 O O . HOH T . ? 0.5436 0.5280 0.5009 -0.0088 -0.0089 0.0162 1171 HOH A O 6312 O O . HOH T . ? 0.6209 0.5588 0.5502 0.0482 0.0089 -0.1847 1172 HOH A O 6313 O O . HOH T . ? 0.6854 0.7105 0.7367 0.0793 0.1143 -0.1606 1173 HOH A O 6314 O O . HOH T . ? 0.5890 0.6540 0.8505 0.0985 -0.1924 -0.1187 1174 HOH A O 6315 O O . HOH T . ? 0.8321 0.6603 0.4895 0.2249 -0.1783 -0.1392 1175 HOH A O 6316 O O . HOH T . ? 0.6428 0.5543 0.6523 0.0624 -0.1263 -0.0895 1176 HOH A O 6317 O O . HOH T . ? 0.6785 0.5332 0.5288 0.1070 0.1036 0.1059 1177 HOH A O 6318 O O . HOH T . ? 0.9290 0.7542 0.5154 0.2394 -0.0807 -0.0999 1178 HOH A O 6319 O O . HOH T . ? 0.7222 0.5312 0.5131 0.1576 0.0171 0.0916 1179 HOH A O 6320 O O . HOH T . ? 0.8333 0.7752 0.7102 -0.0270 0.0822 0.0886 1180 HOH A O 6321 O O . HOH T . ? 0.7643 0.5801 0.4572 0.2128 -0.0798 0.0390 1181 HOH A O 6322 O O . HOH T . ? 0.8981 0.7106 0.5353 0.2380 -0.1234 0.0063 1182 HOH A O 6323 O O . HOH T . ? 0.4988 0.5064 0.4479 -0.0043 0.0027 -0.0140 1183 HOH A O 6324 O O . HOH T . ? 0.6479 0.7000 0.7446 -0.0148 0.0316 -0.0161 1184 HOH A O 6325 O O . HOH T . ? 0.4766 0.5356 0.7696 -0.0450 0.0001 -0.0205 1185 HOH A O 6326 O O . HOH T . ? 0.7507 0.6072 0.4888 0.1841 -0.1329 -0.1233 1186 HOH A O 6327 O O . HOH T . ? 0.6257 0.6006 0.5779 0.0076 -0.0234 -0.1047 1187 HOH A O 6328 O O . HOH T . ? 0.8311 0.7531 0.6823 0.1329 -0.1259 -0.0701 1188 HOH A O 6329 O O . HOH T . ? 0.7926 0.6857 0.7736 0.1558 -0.0757 0.0052 1189 HOH A O 6330 O O . HOH T . ? 0.5373 0.4892 0.8403 -0.0728 -0.0204 0.0174 1190 HOH A O 6331 O O . HOH T . ? 0.7000 0.6220 0.7000 -0.0636 0.1491 0.1466 1191 HOH A O 6332 O O . HOH T . ? 0.5976 0.7562 0.7573 0.0393 0.2822 -0.0675 1192 HOH A O 6333 O O . HOH T . ? 0.4218 0.5046 0.5537 -0.0033 0.0639 -0.0339 1193 HOH A O 6334 O O . HOH T . ? 0.7192 0.6168 0.8183 0.1108 -0.0130 -0.0214 1194 HOH A O 6335 O O . HOH T . ? 0.5281 0.5409 0.6544 0.0337 -0.1052 -0.0725 1195 HOH A O 6336 O O . HOH T . ? 0.6435 0.5910 0.6808 0.0410 0.0253 -0.1418 1196 HOH A O 6337 O O . HOH T . ? 0.6556 0.7292 0.7253 -0.0290 0.2028 0.0329 1197 HOH A O 6338 O O . HOH T . ? 0.7129 0.8463 0.9591 0.0072 0.0969 -0.0538 1198 HOH A O 6339 O O . HOH T . ? 0.6301 0.6356 0.5645 -0.0063 0.0097 -0.0092 1199 HOH A O 6340 O O . HOH T . ? 0.6021 0.5909 0.5183 0.0090 0.0015 -0.0796 1200 HOH A O 6341 O O . HOH T . ? 0.6587 0.6257 0.7002 0.1768 -0.1996 -0.0724 1201 HOH A O 6342 O O . HOH T . ? 0.7171 0.6557 0.5967 0.0540 0.0108 -0.1895 1202 HOH A O 6343 O O . HOH T . ? 0.7001 0.7153 0.7657 0.0686 0.0881 -0.1439 1203 HOH A O 6344 O O . HOH T . ? 0.8251 0.7176 0.5911 0.1611 -0.0929 -0.0310 1204 HOH A O 6346 O O . HOH T . ? 0.8138 0.7087 0.6627 0.1303 -0.1203 -0.1019 1206 HOH A O 6347 O O . HOH T . ? 0.5687 0.4862 0.6428 0.0100 -0.0851 -0.0318 1207 HOH A O 6348 O O . HOH T . ? 0.5828 0.6210 0.8988 -0.0577 -0.0030 -0.0111 1208 HOH A O 6349 O O . HOH T . ? 0.6813 0.6785 0.6387 0.0004 -0.0191 0.0024 1209 HOH A O 6350 O O . HOH T . ? 0.5489 0.5969 0.7043 -0.0163 -0.0050 -0.0249 1210 HOH A O 6351 O O . HOH T . ? 0.5837 0.6470 0.6468 -0.0147 0.0888 -0.0129 1211 HOH A O 6352 O O . HOH T . ? 0.6456 0.6374 1.0264 -0.1145 0.1202 0.0944 1212 HOH A O 6353 O O . HOH T . ? 0.4943 0.5922 0.8329 0.0611 -0.1498 -0.1124 1213 HOH A O 6354 O O . HOH T . ? 0.6337 0.6402 0.5527 -0.0034 0.0196 -0.0216 1214 HOH A O 6355 O O . HOH T . ? 0.7124 0.6991 0.5974 0.0109 -0.0011 -0.0760 1215 HOH A O 6356 O O . HOH T . ? 0.7790 0.6411 0.4316 0.1953 -0.0405 -0.0431 1216 HOH A O 6357 O O . HOH T . ? 0.5439 0.3967 0.5402 0.1060 0.0078 0.0390 1217 HOH A O 6358 O O . HOH T . ? 0.7157 0.6502 0.8450 -0.0029 0.0316 -0.0223 1218 HOH A O 6359 O O . HOH T . ? 0.5303 0.5303 0.4959 0.0008 -0.0135 -0.0002 1219 HOH A O 6360 O O . HOH T . ? 0.7515 0.7403 0.7177 0.0004 -0.0592 -0.0874 1220 HOH A O 6361 O O . HOH T . ? 0.6271 0.5878 0.6579 0.0668 0.0554 -0.1711 1221 HOH A O 6362 O O . HOH T . ? 0.7405 0.7524 0.7034 -0.0162 0.0380 0.0067 1222 HOH A O 6363 O O . HOH T . ? 0.5429 0.5801 0.8210 -0.0224 -0.0675 -0.0542 1223 HOH A O 6364 O O . HOH T . ? 0.5391 0.4907 0.7737 -0.0308 -0.0861 -0.0392 1224 HOH A O 6365 O O . HOH T . ? 0.7774 0.7089 0.8522 -0.0771 0.1543 0.1458 1225 HOH A O 6366 O O . HOH T . ? 0.8751 0.8920 0.7603 0.1024 0.1796 -0.1859 1226 HOH A O 6367 O O . HOH T . ? 0.5759 0.5385 0.8430 -0.0529 -0.0486 -0.0105 1227 HOH A O 6368 O O . HOH T . ? 0.7715 0.7502 0.8427 0.0703 -0.1577 -0.1005 1228 HOH A O 6369 O O . HOH T . ? 0.5549 0.6075 0.8570 -0.0319 -0.0438 -0.0444 1229 HOH A O 6370 O O . HOH T . ? 0.5948 0.5944 0.6070 -0.0063 -0.0486 -0.0712 1230 HOH A O 6371 O O . HOH T . ? 0.6330 0.6935 0.7764 -0.0362 0.0736 0.0064 1231 HOH A O 6372 O O . HOH T . ? 0.6811 0.6192 0.5870 0.1096 -0.1265 -0.0773 1232 HOH A O 6373 O O . HOH T . ? 0.7035 0.6982 0.7825 0.0806 -0.1579 -0.0961 1233 HOH A O 6374 O O . HOH T . ? 0.8410 0.7652 0.6352 0.1072 0.0670 -0.2518 1234 HOH A O 6375 O O . HOH T . ? 0.5481 0.6688 0.7426 -0.0064 0.1272 -0.0341 1235 HOH A O 6376 O O . HOH T . ? 0.4637 0.4695 0.4410 0.0065 -0.0082 -0.0055 1236 HOH A O 6377 O O . HOH T . ? 0.4810 0.4706 0.4490 0.0272 -0.0178 -0.0104 1237 HOH A O 6378 O O . HOH T . ? 0.6078 0.5490 0.6716 0.0395 0.0232 -0.1286 1238 HOH A O 6379 O O . HOH T . ? 0.5084 0.5082 0.4884 0.0236 -0.0092 -0.0042 1239 HOH A O 6380 O O . HOH T . ? 0.5706 0.5821 0.6913 0.0791 0.0769 -0.1434 1240 HOH A O 6381 O O . HOH T . ? 0.6651 0.7141 0.7431 -0.0385 0.1257 0.0313 1241 HOH A O 6382 O O . HOH T . ? 0.5335 0.5718 0.6451 -0.0450 0.0889 0.0303 1242 HOH A O 6383 O O . HOH T . ? 0.5701 0.6337 0.8187 -0.0253 -0.0155 -0.0344 1243 HOH A O 6384 O O . HOH T . ? 0.7328 0.8038 0.8247 -0.0322 0.1568 0.0223 1244 HOH A O 6385 O O . HOH T . ? 0.5305 0.5843 0.7285 -0.0158 -0.0204 -0.0346 1245 HOH A O 6386 O O . HOH T . ? 0.6302 0.5189 0.7337 0.0692 0.0171 -0.0289 1246 HOH A O 6387 O O . HOH T . ? 0.6283 0.6291 0.7741 0.1340 -0.0968 -0.0563 1247 HOH A O 6388 O O . HOH T . ? 0.5494 0.5213 0.7692 -0.0013 -0.1268 -0.0804 1248 HOH A O 6389 O O . HOH T . ? 0.6155 0.6470 0.5520 -0.0076 0.1125 -0.0024 1249 HOH A O 6390 O O . HOH T . ? 0.7002 0.5980 0.6346 0.1758 -0.1167 -0.0061 1250 HOH A O 6391 O O . HOH T . ? 0.6785 0.6037 0.6520 0.1656 -0.1246 -0.0229 1251 HOH A O 6392 O O . HOH T . ? 0.6587 0.5687 0.6676 0.0706 -0.1447 -0.1044 1252 HOH A O 6393 O O . HOH T . ? 0.9337 0.7456 0.5588 0.2412 -0.1828 -0.1533 1253 HOH A O 6394 O O . HOH T . ? 0.5594 0.6892 0.7751 0.0089 0.1186 -0.0536 1254 HOH A O 6395 O O . HOH T . ? 0.5057 0.6404 0.7759 0.0442 0.0854 -0.0869 1255 HOH A O 6396 O O . HOH T . ? 0.6018 0.6754 0.7869 0.0368 -0.0353 -0.0599 1256 HOH A O 6397 O O . HOH T . ? 0.9067 0.7222 0.5279 0.2442 -0.1999 -0.1432 1257 HOH A O 6398 O O . HOH T . ? 0.6049 0.6007 0.5026 0.0027 -0.0018 -0.0459 1258 HOH A O 6399 O O . HOH T . ? 0.7147 0.6997 0.8520 0.0460 -0.1563 -0.1031 1259 HOH A O 6400 O O . HOH T . ? 0.6185 0.5641 0.6895 0.0777 -0.1949 -0.1298 1260 HOH A O 6401 O O . HOH T . ? 0.5583 0.7182 0.7350 0.0659 0.2682 -0.1082 1261 HOH A O 6402 O O . HOH T . ? 0.6436 0.5687 0.7799 -0.0445 -0.0224 0.0341 1262 HOH A O 6403 O O . HOH T . ? 0.5309 0.4903 0.6769 -0.0095 0.0472 0.0016 1263 HOH A O 6404 O O . HOH T . ? 0.5880 0.5960 0.4861 0.0041 0.0428 -0.0395 1264 HOH A O 6405 O O . HOH T . ? 0.6896 0.5629 0.7441 0.0485 0.0508 0.0355 1265 HOH A O 6406 O O . HOH T . ? 0.7092 0.7368 0.6727 -0.0129 0.0718 -0.0028 1266 HOH A O 6407 O O . HOH T . ? 0.7267 0.6444 0.7905 0.0770 -0.2000 -0.1395 1267 HOH A O 6408 O O . HOH T . ? 0.7355 0.5686 0.6371 0.0939 0.1188 0.1235 1268 HOH A O 6409 O O . HOH T . ? 0.7469 0.6690 0.8440 0.0291 -0.1299 -0.0815 1269 HOH A O 6410 O O . HOH T . ? 0.6012 0.6463 0.8193 0.1046 -0.2059 -0.1209 1270 HOH A O 6411 O O . HOH T . ? 0.7798 0.6367 0.7481 0.0921 0.0307 0.0550 1271 HOH A O 6412 O O . HOH T . ? 0.7864 0.7520 0.5630 0.0414 0.0313 -0.1150 1272 HOH A O 6413 O O . HOH T . ? 0.6203 0.6781 0.7052 -0.0144 0.0520 -0.0159 1273 HOH A O 6414 O O . HOH T . ? 0.8352 0.7588 0.8145 0.1098 -0.1997 -0.1333 1274 HOH A O 6415 O O . HOH T . ? 0.6598 0.6126 0.7960 0.1420 -0.0640 -0.0411 1275 HOH A O 6416 O O . HOH T . ? 0.5962 0.5837 0.7785 0.0250 -0.1450 -0.0965 1276 HOH A O 6417 O O . HOH T . ? 0.7074 0.6536 0.6915 0.1574 -0.1398 -0.0404 1277 HOH A O 6418 O O . HOH T . ? 0.6294 0.6848 0.7016 -0.0383 0.1659 0.0409 1278 HOH A O 6419 O O . HOH T . ? 0.5892 0.6782 0.9161 0.0792 -0.1799 -0.1222 1279 HOH A O 6420 O O . HOH T . ? 0.7706 0.6721 0.7315 0.0830 -0.1139 -0.0901 1280 HOH A O 6421 O O . HOH T . ? 0.6509 0.7351 0.7810 -0.0154 0.0890 -0.0193 1281 HOH A O 6422 O O . HOH T . ? 0.6269 0.6260 0.8416 0.0060 -0.1209 -0.0812 1282 HOH A O 6423 O O . HOH T . ? 0.5619 0.5727 0.6652 0.0010 0.0390 0.0057 1283 HOH A O 6424 O O . HOH T . ? 0.6899 0.6744 0.6051 0.0073 -0.0655 -0.0835 1284 HOH A O 6425 O O . HOH T . ? 0.6551 0.8020 0.7548 0.0445 0.3141 -0.0609 1285 HOH A O 6426 O O . HOH T . ? 0.6775 0.6498 0.9322 -0.0297 -0.0885 -0.0481 1286 HOH A O 6427 O O . HOH T . ? 0.5802 0.6039 0.5674 -0.0041 0.0248 -0.0187 1287 HOH A O 6428 O O . HOH T . ? 0.9021 0.8299 0.7758 0.1461 -0.1424 -0.0601 1288 HOH A O 6429 O O . HOH T . ? 0.5636 0.6052 0.7607 0.0891 0.0666 -0.1270 1289 HOH A O 6430 O O . HOH T . ? 0.5980 0.6148 0.7244 -0.0165 -0.0214 -0.0434 1290 HOH A O 6431 O O . HOH T . ? 0.8269 0.7811 0.7263 -0.0267 0.0660 0.0727 1291 HOH A O 6432 O O . HOH T . ? 0.7379 0.7270 0.6861 -0.0012 -0.0205 0.0094 1292 HOH A O 6433 O O . HOH T . ? 0.6746 0.7313 1.0146 -0.0529 -0.0082 -0.0229 1293 HOH A O 6434 O O . HOH T . ? 0.7605 0.7551 0.8471 0.1403 -0.2230 -0.1120 1294 HOH A O 6435 O O . HOH T . ? 0.7243 0.6446 0.6515 0.1716 -0.1426 -0.0303 1295 HOH A O 6436 O O . HOH T . ? 0.6904 0.5493 0.7836 0.0777 0.0189 -0.0029 1296 HOH A O 6437 O O . HOH T . ? 0.7997 0.6878 0.6545 0.1324 -0.0989 -0.1016 1297 HOH A O 6438 O O . HOH T . ? 0.7429 0.6946 0.7511 0.1700 -0.1652 -0.0513 1298 HOH A O 6439 O O . HOH T . ? 0.8930 0.7780 0.7291 0.1864 -0.1332 -0.0140 1299 HOH A O 6440 O O . HOH T . ? 0.7444 0.6152 0.4922 0.1794 -0.1529 -0.1074 1300 HOH A O 6441 O O . HOH T . ? 0.4894 0.5450 0.8035 -0.0739 0.0758 0.0271 1301 HOH A O 6442 O O . HOH T . ? 0.6170 0.6263 0.7421 0.0897 -0.1821 -0.1086 1302 HOH A O 6443 O O . HOH T . ? 1.0353 0.8310 0.5978 0.2288 -0.0132 0.0503 1303 HOH A O 6444 O O . HOH T . ? 0.6450 0.6543 0.8158 0.0848 0.0451 -0.1129 1304 HOH A O 6445 O O . HOH T . ? 0.5816 0.5228 0.6760 0.0498 0.0285 -0.1111 1305 HOH A O 6446 O O . HOH T . ? 0.8175 0.7995 0.9143 0.1672 -0.1678 -0.0638 1306 HOH A O 6447 O O . HOH T . ? 0.6510 0.6710 0.8415 0.1229 -0.0702 -0.0653 1307 HOH A O 6448 O O . HOH T . ? 0.8595 0.7743 0.7184 0.1349 -0.1477 -0.0923 1308 HOH A O 6449 O O . HOH T . ? 0.7137 0.7124 0.8245 -0.0168 -0.0167 -0.0521 1309 HOH A O 6450 O O . HOH T . ? 0.7793 0.7122 0.8600 0.0281 0.0156 -0.1066 1310 HOH A O 6451 O O . HOH T . ? 0.7021 0.7023 0.8531 0.1739 -0.1835 -0.0763 1311 HOH A O 6452 O O . HOH T . ? 0.7126 0.6715 0.8546 -0.0138 0.0189 -0.0337 1312 HOH A O 6453 O O . HOH T . ? 0.5975 0.5981 0.5051 -0.0013 0.0042 -0.0278 1313 HOH A O 6454 O O . HOH T . ? 0.5935 0.5955 0.5721 0.0193 -0.0040 -0.0043 1314 HOH A O 6455 O O . HOH T . ? 0.6471 0.5894 0.5877 -0.0242 0.0165 0.0637 1315 HOH A O 6456 O O . HOH T . ? 0.6376 0.5010 0.3058 0.1836 -0.0320 -0.0076 1316 HOH A O 6457 O O . HOH T . ? 0.6867 0.5473 0.3547 0.1800 -0.0060 0.0138 1317 HOH A O 6458 O O . HOH T . ? 0.7247 0.7311 0.6242 0.0006 0.0350 -0.0304 1318 HOH A O 6459 O O . HOH T . ? 0.5409 0.5990 0.7351 0.0222 -0.0694 -0.0641 1319 HOH A O 6460 O O . HOH T . ? 0.9096 0.7306 0.7272 0.1241 0.1062 0.1248 1320 HOH A O 6461 O O . HOH T . ? 0.6169 0.7066 0.8369 0.0783 0.0946 -0.1227 1321 HOH A O 6462 O O . HOH T . ? 0.5605 0.6988 0.7831 0.0188 0.1375 -0.0644 1322 HOH A O 6464 O O . HOH T . ? 0.7200 0.6426 0.8143 0.0562 -0.1790 -0.1231 1324 HOH A O 6468 O O . HOH T . ? 0.7253 0.7172 0.6574 -0.0054 -0.0095 0.0076 1328 HOH A O 6469 O O . HOH T . ? 0.7524 0.8803 0.7785 0.0681 0.3235 -0.0862 1329 HOH A O 6470 O O . HOH T . ? 0.6870 0.7561 0.7807 -0.0141 0.0751 -0.0176 1330 HOH A O 6471 O O . HOH T . ? 0.7968 0.7394 0.6439 -0.0223 0.0947 0.0885 1331 HOH A O 6472 O O . HOH T . ? 0.6707 0.6324 0.5654 0.0798 -0.0002 -0.0137 1332 HOH A O 6473 O O . HOH T . ? 0.5315 0.5352 0.6443 -0.0142 0.0000 -0.0326 1333 HOH A O 6474 O O . HOH T . ? 0.7634 0.7067 0.7674 -0.0616 0.1576 0.1340 1334 HOH A O 6475 O O . HOH T . ? 0.7759 0.6587 0.5788 0.1717 -0.1913 -0.1221 1335 HOH A O 6476 O O . HOH T . ? 0.6174 0.7148 0.8926 0.0303 -0.0600 -0.0748 1336 HOH A O 6477 O O . HOH T . ? 0.4446 0.5233 0.6094 0.0400 0.0431 -0.0699 1337 HOH A O 6478 O O . HOH T . ? 0.7203 0.7197 0.6712 0.0015 -0.0597 -0.0563 1338 HOH A O 6479 O O . HOH T . ? 0.8811 0.8712 0.7576 0.0041 -0.0160 -0.0385 1339 HOH A O 6480 O O . HOH T . ? 0.7465 0.7396 0.6060 0.0075 0.0205 -0.0444 1340 HOH A O 6481 O O . HOH T . ? 0.5644 0.6167 0.6817 0.0259 -0.0195 -0.0449 1341 HOH A O 6482 O O . HOH T . ? 0.5715 0.6284 0.7110 0.0038 -0.0121 -0.0379 1342 HOH A O 6483 O O . HOH T . ? 0.3914 0.3867 0.3764 -0.0235 0.0260 0.0237 1343 HOH A O 6484 O O . HOH T . ? 0.5210 0.5043 0.4834 -0.0242 0.0292 0.0350 1344 HOH A O 6485 O O . HOH T . ? 0.4159 0.3905 0.3872 -0.0350 0.0604 0.0585 1345 HOH A O 6486 O O . HOH T . ? 0.5718 0.5425 0.5996 -0.0576 0.1336 0.1019 1346 HOH A O 6487 O O . HOH T . ? 0.3160 0.3237 0.3470 0.0262 0.0159 -0.0355 1347 HOH A O 6488 O O . HOH T . ? 0.5024 0.5321 0.5456 0.0191 0.0087 -0.0326 1348 HOH A O 6489 O O . HOH T . ? 0.5629 0.5814 0.6248 0.0387 0.0075 -0.0409 1349 HOH A O 6490 O O . HOH T . ? 0.4123 0.4295 0.3881 0.0006 0.0229 -0.0309 1350 HOH A O # 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 418 A ASN 459 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 435 A ASN 476 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 99 A ASN 140 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 80 A ASN 121 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 597 A ASN 638 ? 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)' 12070 ? 1 MORE -123 ? 1 'SSA (A^2)' 49010 ? # 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 129.9380000000 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 1347 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 OD1 ? A ASP 346 ? A ASP 387 ? 1_555 105.8 ? 2 O ? T HOH . ? A HOH 1347 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 OD2 ? A ASP 412 ? A ASP 453 ? 1_555 112.2 ? 3 OD1 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 OD2 ? A ASP 412 ? A ASP 453 ? 1_555 119.5 ? 4 O ? T HOH . ? A HOH 1347 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 NE2 ? A HIS 336 ? A HIS 377 ? 1_555 110.6 ? 5 OD1 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 NE2 ? A HIS 336 ? A HIS 377 ? 1_555 106.6 ? 6 OD2 ? A ASP 412 ? A ASP 453 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 NE2 ? A HIS 336 ? A HIS 377 ? 1_555 101.9 ? 7 O ? T HOH . ? A HOH 1347 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 154.3 ? 8 O ? T HOH . ? A HOH 1347 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 97.7 ? 9 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 104.2 ? 10 O ? T HOH . ? A HOH 1347 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 97.1 ? 11 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 92.1 ? 12 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 100.1 ? 13 O ? T HOH . ? A HOH 1347 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 93.4 ? 14 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 87.9 ? 15 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 56.2 ? 16 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 155.3 ? 17 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? A TYR 231 ? A TYR 272 ? 1_555 80.3 ? 18 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 104.8 ? 19 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 73.4 ? 20 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 86.7 ? 21 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 136.7 ? 22 O ? A THR 228 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 149.8 ? 23 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 93.2 ? 24 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 86.9 ? 25 O ? A THR 228 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 150.3 ? 26 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 52.6 ? 27 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 172.8 ? 28 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 92.5 ? 29 O ? A THR 228 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 72.9 ? 30 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 98.6 ? 31 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 86.3 ? 32 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 95.2 ? 33 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 145.2 ? 34 O ? A THR 228 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 74.5 ? 35 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 76.8 ? 36 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 127.9 ? 37 OG1 ? A THR 228 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 90.7 ? # _pdbx_audit_revision_history.ordinal 1 _pdbx_audit_revision_history.data_content_type 'Structure model' _pdbx_audit_revision_history.major_revision 1 _pdbx_audit_revision_history.minor_revision 0 _pdbx_audit_revision_history.revision_date 2014-05-21 # _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_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 17.7609 _pdbx_refine_tls.origin_y 49.6117 _pdbx_refine_tls.origin_z 44.6974 _pdbx_refine_tls.T[1][1] 0.0286 _pdbx_refine_tls.T[2][2] 0.0534 _pdbx_refine_tls.T[3][3] 0.0581 _pdbx_refine_tls.T[1][2] 0.0167 _pdbx_refine_tls.T[1][3] 0.0094 _pdbx_refine_tls.T[2][3] -0.0295 _pdbx_refine_tls.L[1][1] 0.7437 _pdbx_refine_tls.L[2][2] 1.1203 _pdbx_refine_tls.L[3][3] 0.3690 _pdbx_refine_tls.L[1][2] -0.3554 _pdbx_refine_tls.L[1][3] 0.0676 _pdbx_refine_tls.L[2][3] 0.0990 _pdbx_refine_tls.S[1][1] -0.0663 _pdbx_refine_tls.S[1][2] 0.0547 _pdbx_refine_tls.S[1][3] -0.0364 _pdbx_refine_tls.S[2][1] 0.0019 _pdbx_refine_tls.S[2][2] 0.0782 _pdbx_refine_tls.S[2][3] -0.2069 _pdbx_refine_tls.S[3][1] 0.0368 _pdbx_refine_tls.S[3][2] 0.0894 _pdbx_refine_tls.S[3][3] -0.0119 # _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 MAR345dtb 'data collection' . ? 1 REFMAC refinement 5.5.0109 ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 REFMAC phasing 5.5.0109 ? 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 O A HOH 1165 ? ? O A HOH 1188 ? ? 1.97 2 1 NH1 A ARG 688 ? B O A HOH 1236 ? ? 2.02 3 1 OG A SER 517 ? ? OE2 A GLU 522 ? A 2.18 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 SER _pdbx_validate_symm_contact.auth_seq_id_1 656 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 B _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 1216 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 4_566 _pdbx_validate_symm_contact.dist 2.09 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CB _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 VAL _pdbx_validate_rmsd_bond.auth_seq_id_1 158 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 CG1 _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 VAL _pdbx_validate_rmsd_bond.auth_seq_id_2 158 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.665 _pdbx_validate_rmsd_bond.bond_target_value 1.524 _pdbx_validate_rmsd_bond.bond_deviation 0.141 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.021 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 HIS A 124 ? ? -150.92 73.74 2 1 PHE A 164 ? ? 84.21 3.49 3 1 ASN A 178 ? ? 57.28 -126.64 4 1 LYS A 207 ? ? 76.87 -45.70 5 1 VAL A 382 ? ? -128.48 -108.20 6 1 ALA A 452 ? ? -153.27 65.19 7 1 ASP A 453 ? ? -88.70 -157.90 8 1 ASP A 453 ? ? -88.70 -156.32 9 1 SER A 454 ? A -34.91 125.68 10 1 SER A 454 ? B -43.68 108.78 11 1 SER A 517 ? ? -142.03 -155.85 12 1 TRP A 541 ? ? -48.71 78.11 13 1 ASP A 567 ? ? -153.51 64.83 14 1 ASP A 683 ? ? 57.36 12.53 15 1 ASN A 698 ? ? -165.87 96.45 16 1 PHE A 705 ? ? 38.51 59.53 # 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~-[(1-carboxycyclopropyl)carbamoyl]-N~6~-(4-iodobenzoyl)-L-lysine' 2R7 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 1 801 1755 NAG NAG A . C 2 NAG 2 802 1756 NAG NAG A . D 2 NAG 1 803 1757 NAG NAG A . E 2 NAG 1 804 1758 NAG NAG A . F 2 NAG 2 805 1767 NAG NAG A . G 2 NAG 1 806 1759 NAG NAG A . H 2 NAG 1 807 1760 NAG NAG A . I 2 NAG 1 808 1761 NAG NAG A . J 2 NAG 2 809 1762 NAG NAG A . K 2 NAG 1 810 1763 NAG NAG A . L 2 NAG 2 811 1764 NAG NAG A . M 3 BMA 3 812 1765 BMA BMA A . N 4 MAN 4 813 1766 MAN MAN A . O 5 ZN 1 814 1751 ZN ZN A . P 5 ZN 1 815 1752 ZN ZN A . Q 6 CA 1 816 1753 CA CA A . R 7 CL 1 817 1754 CL CL A . S 8 2R7 1 818 1 2R7 DRG A . T 9 HOH 1 901 1768 HOH HOH A . T 9 HOH 2 902 1769 HOH HOH A . T 9 HOH 3 903 1770 HOH HOH A . T 9 HOH 4 904 1771 HOH HOH A . T 9 HOH 5 905 1772 HOH HOH A . T 9 HOH 6 906 1773 HOH HOH A . T 9 HOH 7 907 1774 HOH HOH A . T 9 HOH 8 908 1775 HOH HOH A . T 9 HOH 9 909 1776 HOH HOH A . T 9 HOH 10 910 1777 HOH HOH A . T 9 HOH 11 911 1778 HOH HOH A . T 9 HOH 12 912 1779 HOH HOH A . T 9 HOH 13 913 1780 HOH HOH A . T 9 HOH 14 914 1781 HOH HOH A . T 9 HOH 15 915 1782 HOH HOH A . T 9 HOH 16 916 1783 HOH HOH A . T 9 HOH 17 917 1784 HOH HOH A . T 9 HOH 18 918 1785 HOH HOH A . T 9 HOH 19 919 1786 HOH HOH A . T 9 HOH 20 920 1787 HOH HOH A . T 9 HOH 21 921 1788 HOH HOH A . T 9 HOH 22 922 1789 HOH HOH A . T 9 HOH 23 923 1790 HOH HOH A . T 9 HOH 24 924 1791 HOH HOH A . T 9 HOH 25 925 1792 HOH HOH A . T 9 HOH 26 926 1793 HOH HOH A . T 9 HOH 27 927 1794 HOH HOH A . T 9 HOH 28 928 1795 HOH HOH A . T 9 HOH 29 929 1796 HOH HOH A . T 9 HOH 30 930 1797 HOH HOH A . T 9 HOH 31 931 1798 HOH HOH A . T 9 HOH 32 932 1799 HOH HOH A . T 9 HOH 33 933 1800 HOH HOH A . T 9 HOH 34 934 1801 HOH HOH A . T 9 HOH 35 935 1802 HOH HOH A . T 9 HOH 36 936 1803 HOH HOH A . T 9 HOH 37 937 1804 HOH HOH A . T 9 HOH 38 938 1805 HOH HOH A . T 9 HOH 39 939 1806 HOH HOH A . T 9 HOH 40 940 1807 HOH HOH A . T 9 HOH 41 941 1808 HOH HOH A . T 9 HOH 42 942 1809 HOH HOH A . T 9 HOH 43 943 1810 HOH HOH A . T 9 HOH 44 944 1811 HOH HOH A . T 9 HOH 45 945 1812 HOH HOH A . T 9 HOH 46 946 1813 HOH HOH A . T 9 HOH 47 947 1814 HOH HOH A . T 9 HOH 48 948 1815 HOH HOH A . T 9 HOH 49 949 1816 HOH HOH A . T 9 HOH 50 950 1817 HOH HOH A . T 9 HOH 51 951 1818 HOH HOH A . T 9 HOH 52 952 1819 HOH HOH A . T 9 HOH 53 953 1820 HOH HOH A . T 9 HOH 54 954 1821 HOH HOH A . T 9 HOH 55 955 1822 HOH HOH A . T 9 HOH 56 956 1823 HOH HOH A . T 9 HOH 57 957 1824 HOH HOH A . T 9 HOH 58 958 1825 HOH HOH A . T 9 HOH 59 959 1826 HOH HOH A . T 9 HOH 60 960 1827 HOH HOH A . T 9 HOH 61 961 1828 HOH HOH A . T 9 HOH 62 962 1829 HOH HOH A . T 9 HOH 63 963 1830 HOH HOH A . T 9 HOH 64 964 1831 HOH HOH A . T 9 HOH 65 965 1832 HOH HOH A . T 9 HOH 66 966 1834 HOH HOH A . T 9 HOH 67 967 1835 HOH HOH A . T 9 HOH 68 968 1836 HOH HOH A . T 9 HOH 69 969 1837 HOH HOH A . T 9 HOH 70 970 1838 HOH HOH A . T 9 HOH 71 971 1839 HOH HOH A . T 9 HOH 72 972 1840 HOH HOH A . T 9 HOH 73 973 1841 HOH HOH A . T 9 HOH 74 974 1842 HOH HOH A . T 9 HOH 75 975 1843 HOH HOH A . T 9 HOH 76 976 1844 HOH HOH A . T 9 HOH 77 977 1845 HOH HOH A . T 9 HOH 78 978 1846 HOH HOH A . T 9 HOH 79 979 1847 HOH HOH A . T 9 HOH 80 980 1848 HOH HOH A . T 9 HOH 81 981 1849 HOH HOH A . T 9 HOH 82 982 1850 HOH HOH A . T 9 HOH 83 983 1851 HOH HOH A . T 9 HOH 84 984 1852 HOH HOH A . T 9 HOH 85 985 1853 HOH HOH A . T 9 HOH 86 986 1854 HOH HOH A . T 9 HOH 87 987 1855 HOH HOH A . T 9 HOH 88 988 1856 HOH HOH A . T 9 HOH 89 989 1857 HOH HOH A . T 9 HOH 90 990 1858 HOH HOH A . T 9 HOH 91 991 1859 HOH HOH A . T 9 HOH 92 992 1860 HOH HOH A . T 9 HOH 93 993 1861 HOH HOH A . T 9 HOH 94 994 1862 HOH HOH A . T 9 HOH 95 995 1864 HOH HOH A . T 9 HOH 96 996 1865 HOH HOH A . T 9 HOH 97 997 1866 HOH HOH A . T 9 HOH 98 998 1867 HOH HOH A . T 9 HOH 99 999 1868 HOH HOH A . T 9 HOH 100 1000 1869 HOH HOH A . T 9 HOH 101 1001 1870 HOH HOH A . T 9 HOH 102 1002 1872 HOH HOH A . T 9 HOH 103 1003 1873 HOH HOH A . T 9 HOH 104 1004 1874 HOH HOH A . T 9 HOH 105 1005 1875 HOH HOH A . T 9 HOH 106 1006 1876 HOH HOH A . T 9 HOH 107 1007 1877 HOH HOH A . T 9 HOH 108 1008 1878 HOH HOH A . T 9 HOH 109 1009 1879 HOH HOH A . T 9 HOH 110 1010 1880 HOH HOH A . T 9 HOH 111 1011 1881 HOH HOH A . T 9 HOH 112 1012 1882 HOH HOH A . T 9 HOH 113 1013 1883 HOH HOH A . T 9 HOH 114 1014 1884 HOH HOH A . T 9 HOH 115 1015 1885 HOH HOH A . T 9 HOH 116 1016 1886 HOH HOH A . T 9 HOH 117 1017 1887 HOH HOH A . T 9 HOH 118 1018 1888 HOH HOH A . T 9 HOH 119 1019 1889 HOH HOH A . T 9 HOH 120 1020 1890 HOH HOH A . T 9 HOH 121 1021 1892 HOH HOH A . T 9 HOH 122 1022 1893 HOH HOH A . T 9 HOH 123 1023 1894 HOH HOH A . T 9 HOH 124 1024 1895 HOH HOH A . T 9 HOH 125 1025 1896 HOH HOH A . T 9 HOH 126 1026 1897 HOH HOH A . T 9 HOH 127 1027 1898 HOH HOH A . T 9 HOH 128 1028 1899 HOH HOH A . T 9 HOH 129 1029 1900 HOH HOH A . T 9 HOH 130 1030 1901 HOH HOH A . T 9 HOH 131 1031 1902 HOH HOH A . T 9 HOH 132 1032 1903 HOH HOH A . T 9 HOH 133 1033 1904 HOH HOH A . T 9 HOH 134 1034 1905 HOH HOH A . T 9 HOH 135 1035 1906 HOH HOH A . T 9 HOH 136 1036 1907 HOH HOH A . T 9 HOH 137 1037 1908 HOH HOH A . T 9 HOH 138 1038 1909 HOH HOH A . T 9 HOH 139 1039 1910 HOH HOH A . T 9 HOH 140 1040 1911 HOH HOH A . T 9 HOH 141 1041 1912 HOH HOH A . T 9 HOH 142 1042 1913 HOH HOH A . T 9 HOH 143 1043 1914 HOH HOH A . T 9 HOH 144 1044 1915 HOH HOH A . T 9 HOH 145 1045 1916 HOH HOH A . T 9 HOH 146 1046 1917 HOH HOH A . T 9 HOH 147 1047 1918 HOH HOH A . T 9 HOH 148 1048 1919 HOH HOH A . T 9 HOH 149 1049 1920 HOH HOH A . T 9 HOH 150 1050 1921 HOH HOH A . T 9 HOH 151 1051 1922 HOH HOH A . T 9 HOH 152 1052 1923 HOH HOH A . T 9 HOH 153 1053 1924 HOH HOH A . T 9 HOH 154 1054 1925 HOH HOH A . T 9 HOH 155 1055 1926 HOH HOH A . T 9 HOH 156 1056 1927 HOH HOH A . T 9 HOH 157 1057 1929 HOH HOH A . T 9 HOH 158 1058 1931 HOH HOH A . T 9 HOH 159 1059 1932 HOH HOH A . T 9 HOH 160 1060 1933 HOH HOH A . T 9 HOH 161 1061 1934 HOH HOH A . T 9 HOH 162 1062 1935 HOH HOH A . T 9 HOH 163 1063 1936 HOH HOH A . T 9 HOH 164 1064 1937 HOH HOH A . T 9 HOH 165 1065 1938 HOH HOH A . T 9 HOH 166 1066 1940 HOH HOH A . T 9 HOH 167 1067 1941 HOH HOH A . T 9 HOH 168 1068 1942 HOH HOH A . T 9 HOH 169 1069 1944 HOH HOH A . T 9 HOH 170 1070 1946 HOH HOH A . T 9 HOH 171 1071 1947 HOH HOH A . T 9 HOH 172 1072 1948 HOH HOH A . T 9 HOH 173 1073 1949 HOH HOH A . T 9 HOH 174 1074 1950 HOH HOH A . T 9 HOH 175 1075 1951 HOH HOH A . T 9 HOH 176 1076 1952 HOH HOH A . T 9 HOH 177 1077 1953 HOH HOH A . T 9 HOH 178 1078 1954 HOH HOH A . T 9 HOH 179 1079 1955 HOH HOH A . T 9 HOH 180 1080 1956 HOH HOH A . T 9 HOH 181 1081 1957 HOH HOH A . T 9 HOH 182 1082 1958 HOH HOH A . T 9 HOH 183 1083 1959 HOH HOH A . T 9 HOH 184 1084 1960 HOH HOH A . T 9 HOH 185 1085 1962 HOH HOH A . T 9 HOH 186 1086 1963 HOH HOH A . T 9 HOH 187 1087 1964 HOH HOH A . T 9 HOH 188 1088 1966 HOH HOH A . T 9 HOH 189 1089 1967 HOH HOH A . T 9 HOH 190 1090 1968 HOH HOH A . T 9 HOH 191 1091 1969 HOH HOH A . T 9 HOH 192 1092 1970 HOH HOH A . T 9 HOH 193 1093 1971 HOH HOH A . T 9 HOH 194 1094 1972 HOH HOH A . T 9 HOH 195 1095 1973 HOH HOH A . T 9 HOH 196 1096 1974 HOH HOH A . T 9 HOH 197 1097 1975 HOH HOH A . T 9 HOH 198 1098 1976 HOH HOH A . T 9 HOH 199 1099 1977 HOH HOH A . T 9 HOH 200 1100 1978 HOH HOH A . T 9 HOH 201 1101 1979 HOH HOH A . T 9 HOH 202 1102 1980 HOH HOH A . T 9 HOH 203 1103 1982 HOH HOH A . T 9 HOH 204 1104 1984 HOH HOH A . T 9 HOH 205 1105 1987 HOH HOH A . T 9 HOH 206 1106 1989 HOH HOH A . T 9 HOH 207 1107 1990 HOH HOH A . T 9 HOH 208 1108 1991 HOH HOH A . T 9 HOH 209 1109 1993 HOH HOH A . T 9 HOH 210 1110 1994 HOH HOH A . T 9 HOH 211 1111 1995 HOH HOH A . T 9 HOH 212 1112 1996 HOH HOH A . T 9 HOH 213 1113 1997 HOH HOH A . T 9 HOH 214 1114 1998 HOH HOH A . T 9 HOH 215 1115 1999 HOH HOH A . T 9 HOH 216 1116 2000 HOH HOH A . T 9 HOH 217 1117 2001 HOH HOH A . T 9 HOH 218 1118 2002 HOH HOH A . T 9 HOH 219 1119 2003 HOH HOH A . T 9 HOH 220 1120 2004 HOH HOH A . T 9 HOH 221 1121 2005 HOH HOH A . T 9 HOH 222 1122 2006 HOH HOH A . T 9 HOH 223 1123 2007 HOH HOH A . T 9 HOH 224 1124 2009 HOH HOH A . T 9 HOH 225 1125 2010 HOH HOH A . T 9 HOH 226 1126 2011 HOH HOH A . T 9 HOH 227 1127 2012 HOH HOH A . T 9 HOH 228 1128 2013 HOH HOH A . T 9 HOH 229 1129 2014 HOH HOH A . T 9 HOH 230 1130 2015 HOH HOH A . T 9 HOH 231 1131 2016 HOH HOH A . T 9 HOH 232 1132 2017 HOH HOH A . T 9 HOH 233 1133 2018 HOH HOH A . T 9 HOH 234 1134 2019 HOH HOH A . T 9 HOH 235 1135 2020 HOH HOH A . T 9 HOH 236 1136 2021 HOH HOH A . T 9 HOH 237 1137 2025 HOH HOH A . T 9 HOH 238 1138 2026 HOH HOH A . T 9 HOH 239 1139 2029 HOH HOH A . T 9 HOH 240 1140 2031 HOH HOH A . T 9 HOH 241 1141 2032 HOH HOH A . T 9 HOH 242 1142 2033 HOH HOH A . T 9 HOH 243 1143 2034 HOH HOH A . T 9 HOH 244 1144 2035 HOH HOH A . T 9 HOH 245 1145 2036 HOH HOH A . T 9 HOH 246 1146 2038 HOH HOH A . T 9 HOH 247 1147 2039 HOH HOH A . T 9 HOH 248 1148 2040 HOH HOH A . T 9 HOH 249 1149 2041 HOH HOH A . T 9 HOH 250 1150 2043 HOH HOH A . T 9 HOH 251 1151 2044 HOH HOH A . T 9 HOH 252 1152 2046 HOH HOH A . T 9 HOH 253 1153 2047 HOH HOH A . T 9 HOH 254 1154 2048 HOH HOH A . T 9 HOH 255 1155 2049 HOH HOH A . T 9 HOH 256 1156 2050 HOH HOH A . T 9 HOH 257 1157 2052 HOH HOH A . T 9 HOH 258 1158 2054 HOH HOH A . T 9 HOH 259 1159 2055 HOH HOH A . T 9 HOH 260 1160 2056 HOH HOH A . T 9 HOH 261 1161 2059 HOH HOH A . T 9 HOH 262 1162 2062 HOH HOH A . T 9 HOH 263 1163 2063 HOH HOH A . T 9 HOH 264 1164 2064 HOH HOH A . T 9 HOH 265 1165 2065 HOH HOH A . T 9 HOH 266 1166 2067 HOH HOH A . T 9 HOH 267 1167 2068 HOH HOH A . T 9 HOH 268 1168 2071 HOH HOH A . T 9 HOH 269 1169 2072 HOH HOH A . T 9 HOH 270 1170 2073 HOH HOH A . T 9 HOH 271 1171 2078 HOH HOH A . T 9 HOH 272 1172 2079 HOH HOH A . T 9 HOH 273 1173 2080 HOH HOH A . T 9 HOH 274 1174 2081 HOH HOH A . T 9 HOH 275 1175 2082 HOH HOH A . T 9 HOH 276 1176 2083 HOH HOH A . T 9 HOH 277 1177 2084 HOH HOH A . T 9 HOH 278 1178 2086 HOH HOH A . T 9 HOH 279 1179 2088 HOH HOH A . T 9 HOH 280 1180 2090 HOH HOH A . T 9 HOH 281 1181 2091 HOH HOH A . T 9 HOH 282 1182 2092 HOH HOH A . T 9 HOH 283 1183 2093 HOH HOH A . T 9 HOH 284 1184 2096 HOH HOH A . T 9 HOH 285 1185 2097 HOH HOH A . T 9 HOH 286 1186 2098 HOH HOH A . T 9 HOH 287 1187 2100 HOH HOH A . T 9 HOH 288 1188 2102 HOH HOH A . T 9 HOH 289 1189 2105 HOH HOH A . T 9 HOH 290 1190 2106 HOH HOH A . T 9 HOH 291 1191 2109 HOH HOH A . T 9 HOH 292 1192 2110 HOH HOH A . T 9 HOH 293 1193 2113 HOH HOH A . T 9 HOH 294 1194 2117 HOH HOH A . T 9 HOH 295 1195 2118 HOH HOH A . T 9 HOH 296 1196 2119 HOH HOH A . T 9 HOH 297 1197 2120 HOH HOH A . T 9 HOH 298 1198 2121 HOH HOH A . T 9 HOH 299 1199 2122 HOH HOH A . T 9 HOH 300 1200 2124 HOH HOH A . T 9 HOH 301 1201 2125 HOH HOH A . T 9 HOH 302 1202 2128 HOH HOH A . T 9 HOH 303 1203 2129 HOH HOH A . T 9 HOH 304 1204 2130 HOH HOH A . T 9 HOH 305 1205 2131 HOH HOH A . T 9 HOH 306 1206 2132 HOH HOH A . T 9 HOH 307 1207 2133 HOH HOH A . T 9 HOH 308 1208 2135 HOH HOH A . T 9 HOH 309 1209 2136 HOH HOH A . T 9 HOH 310 1210 2137 HOH HOH A . T 9 HOH 311 1211 2138 HOH HOH A . T 9 HOH 312 1212 2139 HOH HOH A . T 9 HOH 313 1213 2140 HOH HOH A . T 9 HOH 314 1214 2142 HOH HOH A . T 9 HOH 315 1215 2144 HOH HOH A . T 9 HOH 316 1216 2145 HOH HOH A . T 9 HOH 317 1217 2146 HOH HOH A . T 9 HOH 318 1218 2147 HOH HOH A . T 9 HOH 319 1219 2148 HOH HOH A . T 9 HOH 320 1220 2151 HOH HOH A . T 9 HOH 321 1221 2152 HOH HOH A . T 9 HOH 322 1222 2154 HOH HOH A . T 9 HOH 323 1223 2156 HOH HOH A . T 9 HOH 324 1224 2158 HOH HOH A . T 9 HOH 325 1225 2160 HOH HOH A . T 9 HOH 326 1226 2161 HOH HOH A . T 9 HOH 327 1227 2163 HOH HOH A . T 9 HOH 328 1228 2169 HOH HOH A . T 9 HOH 329 1229 2171 HOH HOH A . T 9 HOH 330 1230 2172 HOH HOH A . T 9 HOH 331 1231 2173 HOH HOH A . T 9 HOH 332 1232 2174 HOH HOH A . T 9 HOH 333 1233 2175 HOH HOH A . T 9 HOH 334 1234 2178 HOH HOH A . T 9 HOH 335 1235 2179 HOH HOH A . T 9 HOH 336 1236 2182 HOH HOH A . T 9 HOH 337 1237 2183 HOH HOH A . T 9 HOH 338 1238 2187 HOH HOH A . T 9 HOH 339 1239 2188 HOH HOH A . T 9 HOH 340 1240 2189 HOH HOH A . T 9 HOH 341 1241 2190 HOH HOH A . T 9 HOH 342 1242 2191 HOH HOH A . T 9 HOH 343 1243 2193 HOH HOH A . T 9 HOH 344 1244 2194 HOH HOH A . T 9 HOH 345 1245 2195 HOH HOH A . T 9 HOH 346 1246 2196 HOH HOH A . T 9 HOH 347 1247 2197 HOH HOH A . T 9 HOH 348 1248 2198 HOH HOH A . T 9 HOH 349 1249 2200 HOH HOH A . T 9 HOH 350 1250 2202 HOH HOH A . T 9 HOH 351 1251 2203 HOH HOH A . T 9 HOH 352 1252 2204 HOH HOH A . T 9 HOH 353 1253 2205 HOH HOH A . T 9 HOH 354 1254 2206 HOH HOH A . T 9 HOH 355 1255 2207 HOH HOH A . T 9 HOH 356 1256 2209 HOH HOH A . T 9 HOH 357 1257 2210 HOH HOH A . T 9 HOH 358 1258 2211 HOH HOH A . T 9 HOH 359 1259 2212 HOH HOH A . T 9 HOH 360 1260 2213 HOH HOH A . T 9 HOH 361 1261 2215 HOH HOH A . T 9 HOH 362 1262 2217 HOH HOH A . T 9 HOH 363 1263 2222 HOH HOH A . T 9 HOH 364 1264 2223 HOH HOH A . T 9 HOH 365 1265 2227 HOH HOH A . T 9 HOH 366 1266 2229 HOH HOH A . T 9 HOH 367 1267 2230 HOH HOH A . T 9 HOH 368 1268 2233 HOH HOH A . T 9 HOH 369 1269 2235 HOH HOH A . T 9 HOH 370 1270 2236 HOH HOH A . T 9 HOH 371 1271 2241 HOH HOH A . T 9 HOH 372 1272 2242 HOH HOH A . T 9 HOH 373 1273 2243 HOH HOH A . T 9 HOH 374 1274 2245 HOH HOH A . T 9 HOH 375 1275 2246 HOH HOH A . T 9 HOH 376 1276 2249 HOH HOH A . T 9 HOH 377 1277 2252 HOH HOH A . T 9 HOH 378 1278 2254 HOH HOH A . T 9 HOH 379 1279 2256 HOH HOH A . T 9 HOH 380 1280 2257 HOH HOH A . T 9 HOH 381 1281 2259 HOH HOH A . T 9 HOH 382 1282 2260 HOH HOH A . T 9 HOH 383 1283 2261 HOH HOH A . T 9 HOH 384 1284 2264 HOH HOH A . T 9 HOH 385 1285 2265 HOH HOH A . T 9 HOH 386 1286 2266 HOH HOH A . T 9 HOH 387 1287 2268 HOH HOH A . T 9 HOH 388 1288 2270 HOH HOH A . T 9 HOH 389 1289 2271 HOH HOH A . T 9 HOH 390 1290 2272 HOH HOH A . T 9 HOH 391 1291 2275 HOH HOH A . T 9 HOH 392 1292 2276 HOH HOH A . T 9 HOH 393 1293 2278 HOH HOH A . T 9 HOH 394 1294 2279 HOH HOH A . T 9 HOH 395 1295 2284 HOH HOH A . T 9 HOH 396 1296 2285 HOH HOH A . T 9 HOH 397 1297 2287 HOH HOH A . T 9 HOH 398 1298 2289 HOH HOH A . T 9 HOH 399 1299 2290 HOH HOH A . T 9 HOH 400 1300 2296 HOH HOH A . T 9 HOH 401 1301 2301 HOH HOH A . T 9 HOH 402 1302 2304 HOH HOH A . T 9 HOH 403 1303 2305 HOH HOH A . T 9 HOH 404 1304 2310 HOH HOH A . T 9 HOH 405 1305 2311 HOH HOH A . T 9 HOH 406 1306 2314 HOH HOH A . T 9 HOH 407 1307 2316 HOH HOH A . T 9 HOH 408 1308 2319 HOH HOH A . T 9 HOH 409 1309 2325 HOH HOH A . T 9 HOH 410 1310 2327 HOH HOH A . T 9 HOH 411 1311 2333 HOH HOH A . T 9 HOH 412 1312 2337 HOH HOH A . T 9 HOH 413 1313 2349 HOH HOH A . T 9 HOH 414 1314 2350 HOH HOH A . T 9 HOH 415 1315 2351 HOH HOH A . T 9 HOH 416 1316 2353 HOH HOH A . T 9 HOH 417 1317 2354 HOH HOH A . T 9 HOH 418 1318 2356 HOH HOH A . T 9 HOH 419 1319 2357 HOH HOH A . T 9 HOH 420 1320 2358 HOH HOH A . T 9 HOH 421 1321 2362 HOH HOH A . T 9 HOH 422 1322 2366 HOH HOH A . T 9 HOH 423 1323 2367 HOH HOH A . T 9 HOH 424 1324 2373 HOH HOH A . T 9 HOH 425 1325 2374 HOH HOH A . T 9 HOH 426 1326 2375 HOH HOH A . T 9 HOH 427 1327 2376 HOH HOH A . T 9 HOH 428 1328 2378 HOH HOH A . T 9 HOH 429 1329 2389 HOH HOH A . T 9 HOH 430 1330 2403 HOH HOH A . T 9 HOH 431 1331 2405 HOH HOH A . T 9 HOH 432 1332 2409 HOH HOH A . T 9 HOH 433 1333 2415 HOH HOH A . T 9 HOH 434 1334 2416 HOH HOH A . T 9 HOH 435 1335 2432 HOH HOH A . T 9 HOH 436 1336 2433 HOH HOH A . T 9 HOH 437 1337 2434 HOH HOH A . T 9 HOH 438 1338 2435 HOH HOH A . T 9 HOH 439 1339 2436 HOH HOH A . T 9 HOH 440 1340 2437 HOH HOH A . T 9 HOH 441 1341 2438 HOH HOH A . T 9 HOH 442 1342 2439 HOH HOH A . T 9 HOH 443 1343 2441 HOH HOH A . T 9 HOH 444 1344 2442 HOH HOH A . T 9 HOH 445 1345 2443 HOH HOH A . T 9 HOH 446 1346 2444 HOH HOH A . T 9 HOH 447 1347 2445 HOH HOH A . T 9 HOH 448 1348 2446 HOH HOH A . T 9 HOH 449 1349 2447 HOH HOH A . T 9 HOH 450 1350 2448 HOH HOH A . #