data_3SJG # _entry.id 3SJG # _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 3SJG RCSB RCSB066276 WWPDB D_1000066276 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3SJE . unspecified PDB 3SJF . unspecified PDB 3SJX . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3SJG _pdbx_database_status.recvd_initial_deposition_date 2011-06-21 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Plechanovova, A.' 1 'Byun, Y.' 2 'Alquicer, G.' 3 'Skultetyova, L.' 4 'Mlcochova, P.' 5 'Nemcova, A.' 6 'Kim, H.' 7 'Navratil, M.' 8 'Mease, R.' 9 'Lubkowski, J.' 10 'Pomper, M.' 11 'Konvalinka, J.' 12 'Rulisek, L.' 13 'Barinka, C.' 14 # _citation.id primary _citation.title 'Novel Substrate-Based Inhibitors of Human Glutamate Carboxypeptidase II with Enhanced Lipophilicity.' _citation.journal_abbrev J.Med.Chem. _citation.journal_volume 54 _citation.page_first 7535 _citation.page_last 7546 _citation.year 2011 _citation.journal_id_ASTM JMCMAR _citation.country US _citation.journal_id_ISSN 0022-2623 _citation.journal_id_CSD 0151 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 21923190 _citation.pdbx_database_id_DOI 10.1021/jm200807m # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Plechanovova, A.' 1 primary 'Byun, Y.' 2 primary 'Alquicer, G.' 3 primary 'Skultetyova, L.' 4 primary 'Mlcochova, P.' 5 primary 'Nemcova, A.' 6 primary 'Kim, H.J.' 7 primary 'Navratil, M.' 8 primary 'Mease, R.' 9 primary 'Lubkowski, J.' 10 primary 'Pomper, M.' 11 primary 'Konvalinka, J.' 12 primary 'Rulisek, L.' 13 primary 'Barinka, C.' 14 # _cell.entry_id 3SJG _cell.length_a 102.266 _cell.length_b 129.993 _cell.length_c 159.121 _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 3SJG _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' 79800.992 1 3.4.17.21 E424A ? ? 2 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 3 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 4 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 11 ? ? ? ? 6 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 7 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 8 non-polymer syn '(2S)-2-[(N-acetyl-L-alpha-aspartyl)amino]nonanoic acid' 330.377 1 ? ? ? ? 9 water nat water 18.015 520 ? ? ? ? # _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 LRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAAEFGLLGSTEWAEENSRL LQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDF EVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYA VVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGL PDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_seq_one_letter_code_can ;RSKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPN KTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIV IARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRR GIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGT LRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAAEFGLLGSTEWAEENSRL 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 ALA 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 ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ;Schneider's S2 cells ; _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code FOLH1_HUMAN _struct_ref.pdbx_db_accession Q04609 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;KSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKT HPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIA RYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGI AEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLR GAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQ ERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEV FFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVV LRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPD RPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _struct_ref.pdbx_align_begin 44 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3SJG _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 3SJG ARG A 1 ? UNP Q04609 ? ? 'EXPRESSION TAG' 42 1 1 3SJG SER A 2 ? UNP Q04609 ? ? 'EXPRESSION TAG' 43 2 1 3SJG ALA A 383 ? UNP Q04609 GLU 424 'ENGINEERED MUTATION' 424 3 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 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 SDR peptide-like . '(2S)-2-[(N-acetyl-L-alpha-aspartyl)amino]nonanoic acid' ? 'C15 H26 N2 O6' 330.377 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 3SJG _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.31 _exptl_crystal.density_percent_sol 62.88 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8.0 _exptl_crystal_grow.pdbx_details ;33% (v/v) pentaerythritol propoxylate PO/OH 5/4, 0.5 % (w/v) PEG 3350, 100 mM Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K ; _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MARMOSAIC 225 mm CCD' _diffrn_detector.pdbx_collection_date 2006-06-11 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Si 111, Rosenbaum-Rock double-crystal monochromator' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.00 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 22-ID' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 22-ID _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.00 # _reflns.entry_id 3SJG _reflns.observed_criterion_sigma_I -3 _reflns.observed_criterion_sigma_F -3 _reflns.d_resolution_low 30.0 _reflns.d_resolution_high 1.65 _reflns.number_obs 126870 _reflns.number_all ? _reflns.percent_possible_obs 99.9 _reflns.pdbx_Rmerge_I_obs 0.11 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 19.9 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 6.7 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _refine.entry_id 3SJG _refine.ls_number_reflns_obs 120461 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 28.05 _refine.ls_d_res_high 1.65 _refine.ls_percent_reflns_obs 99.13 _refine.ls_R_factor_obs 0.16708 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.16623 _refine.ls_R_factor_R_free 0.18315 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 6380 _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 0.966 _refine.B_iso_mean 31.865 _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 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'FOURIER SYNTHESIS' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R_Free 0.072 _refine.overall_SU_ML 0.045 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 2.924 _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_overall_ESU_R ? _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 5538 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 202 _refine_hist.number_atoms_solvent 520 _refine_hist.number_atoms_total 6260 _refine_hist.d_res_high 1.65 _refine_hist.d_res_low 28.05 # 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 0.017 0.022 ? 6208 ? 'X-RAY DIFFRACTION' r_bond_other_d ? ? ? ? ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.684 1.993 ? 8440 ? 'X-RAY DIFFRACTION' r_angle_other_deg ? ? ? ? ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 6.023 5.000 ? 734 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 36.680 23.897 ? 290 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 14.280 15.000 ? 1030 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 13.938 15.000 ? 35 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.119 0.200 ? 911 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.010 0.021 ? 4754 ? '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 0.926 1.500 ? 3608 ? 'X-RAY DIFFRACTION' r_mcbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcangle_it 1.555 2.000 ? 5876 ? 'X-RAY DIFFRACTION' r_scbond_it 2.368 3.000 ? 2600 ? 'X-RAY DIFFRACTION' r_scangle_it 3.738 4.500 ? 2554 ? 'X-RAY DIFFRACTION' r_rigid_bond_restr ? ? ? ? ? 'X-RAY DIFFRACTION' r_sphericity_free ? ? ? ? ? 'X-RAY DIFFRACTION' r_sphericity_bonded ? ? ? ? ? 'X-RAY DIFFRACTION' # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.65 _refine_ls_shell.d_res_low 1.688 _refine_ls_shell.number_reflns_R_work 8131 _refine_ls_shell.R_factor_R_work 0.225 _refine_ls_shell.percent_reflns_obs 91.58 _refine_ls_shell.R_factor_R_free 0.246 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 453 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 3SJG _struct.title 'Human glutamate carboxypeptidase II (E424A inactive mutant ) in complex with N-acetyl-aspartyl-aminooctanoic acid' _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 3SJG _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 3 ? E N N 4 ? F N N 5 ? G N N 5 ? H N N 5 ? I N N 5 ? J N N 5 ? K N N 5 ? L N N 5 ? M N N 5 ? N N N 5 ? 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 ? GLU A 439 ? MET A 470 GLU A 480 1 ? 11 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 ? PHE A 524 ? THR A 558 PHE A 565 1 ? 8 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 ? PHE A 634 ? ASN A 657 PHE A 675 1 ? 19 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 435 ND2 ? ? ? 1_555 M NAG . C1 ? ? A ASN 476 A NAG 1761 1_555 ? ? ? ? ? ? ? 1.434 ? covale2 covale ? ? A ASN 597 ND2 ? ? ? 1_555 O NAG . C1 ? ? A ASN 638 A NAG 1763 1_555 ? ? ? ? ? ? ? 1.434 ? covale3 covale ? ? O NAG . O4 ? ? ? 1_555 P NAG . C1 ? ? A NAG 1763 A NAG 1764 1_555 ? ? ? ? ? ? ? 1.438 ? covale4 covale ? ? M NAG . O4 ? ? ? 1_555 N NAG . C1 ? ? A NAG 1761 A NAG 1762 1_555 ? ? ? ? ? ? ? 1.441 ? covale5 covale ? ? A ASN 35 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 76 A NAG 1755 1_555 ? ? ? ? ? ? ? 1.442 ? covale6 covale ? ? A ASN 99 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 140 A NAG 1758 1_555 ? ? ? ? ? ? ? 1.443 ? covale7 covale ? ? A ASN 418 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 459 A NAG 1760 1_555 ? ? ? ? ? ? ? 1.448 ? covale8 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 1755 A NAG 1756 1_555 ? ? ? ? ? ? ? 1.449 ? covale9 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 1758 A NAG 1767 1_555 ? ? ? ? ? ? ? 1.450 ? covale10 covale ? ? A ASN 80 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 121 A NAG 1757 1_555 ? ? ? ? ? ? ? 1.451 ? covale11 covale ? ? A ASN 154 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 195 A NAG 1759 1_555 ? ? ? ? ? ? ? 1.454 ? metalc1 metalc ? ? C ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 1752 A HOH 2271 1_555 ? ? ? ? ? ? ? 1.964 ? metalc2 metalc ? ? B ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 1751 A HOH 2271 1_555 ? ? ? ? ? ? ? 1.972 ? metalc3 metalc ? ? A ASP 412 OD2 ? ? ? 1_555 C ZN . ZN ? ? A ASP 453 A ZN 1752 1_555 ? ? ? ? ? ? ? 1.977 ? metalc4 metalc ? ? A ASP 346 OD1 ? ? ? 1_555 C ZN . ZN ? ? A ASP 387 A ZN 1752 1_555 ? ? ? ? ? ? ? 1.988 ? metalc5 metalc ? ? A HIS 336 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 377 A ZN 1752 1_555 ? ? ? ? ? ? ? 2.001 ? metalc6 metalc ? ? A HIS 512 NE2 ? ? ? 1_555 B ZN . ZN ? ? A HIS 553 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.018 ? metalc7 metalc ? ? A ASP 346 OD2 ? ? ? 1_555 B ZN . ZN ? ? A ASP 387 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.061 ? metalc8 metalc ? ? A GLU 384 OE2 ? ? ? 1_555 B ZN . ZN ? ? A GLU 425 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.076 ? metalc9 metalc ? ? A GLU 395 OE2 ? ? ? 1_555 D CA . CA ? ? A GLU 436 A CA 1753 1_555 ? ? ? ? ? ? ? 2.304 ? metalc10 metalc ? ? A TYR 231 O ? ? ? 1_555 D CA . CA ? ? A TYR 272 A CA 1753 1_555 ? ? ? ? ? ? ? 2.332 ? metalc11 metalc ? ? D CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 1753 A HOH 1805 1_555 ? ? ? ? ? ? ? 2.421 ? metalc12 metalc ? ? A THR 228 O ? ? ? 1_555 D CA . CA ? ? A THR 269 A CA 1753 1_555 ? ? ? ? ? ? ? 2.429 ? metalc13 metalc ? ? A GLU 384 OE1 ? ? ? 1_555 B ZN . ZN ? ? A GLU 425 A ZN 1751 1_555 ? ? ? ? ? ? ? 2.440 ? metalc14 metalc ? ? A THR 228 OG1 ? ? ? 1_555 D CA . CA ? ? A THR 269 A CA 1753 1_555 ? ? ? ? ? ? ? 2.480 ? metalc15 metalc ? ? A GLU 392 OE1 ? ? ? 1_555 D CA . CA ? ? A GLU 433 A CA 1753 1_555 ? ? ? ? ? ? ? 2.486 ? metalc16 metalc ? ? A GLU 392 OE2 ? ? ? 1_555 D CA . CA ? ? A GLU 433 A CA 1753 1_555 ? ? ? ? ? ? ? 2.490 ? covale12 covale ? ? P NAG . O4 ? ? ? 1_555 Q BMA . C1 ? ? A NAG 1764 A BMA 1765 1_555 ? ? ? ? ? ? ? 1.423 ? covale13 covale ? ? Q BMA . O3 ? ? ? 1_555 R MAN . C1 ? ? A BMA 1765 A MAN 1766 1_555 ? ? ? ? ? ? ? 1.448 ? metalc17 metalc ? ? B ZN . ZN ? ? ? 1_555 S SDR . OAF ? ? A ZN 1751 A SDR 1 1_555 ? ? ? ? ? ? ? 2.541 ? # 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 10.76 2 GLY 289 A . ? GLY 330 A PRO 290 A ? PRO 331 A 1 0.80 3 ASP 346 A . ? ASP 387 A PRO 347 A ? PRO 388 A 1 6.47 # 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 SER A 491 ? THR A 497 ? SER A 532 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 PHE A 98 ? O PHE A 139 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 HIS A 254 ? O HIS A 295 E 1 2 N SER A 654 ? N SER A 695 O ALA A 660 ? O ALA A 701 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ZN A 1751' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE ZN A 1752' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 1753' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CL A 1754' AC5 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 1755' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 1756' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 1757' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 1758' AC9 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 1767' BC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 1759' BC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 1760' BC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 1761' BC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 1762' BC5 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 1763' BC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 1764' BC7 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE BMA A 1765' BC8 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE MAN A 1766' BC9 Software ? ? ? ? 25 'BINDING SITE FOR RESIDUE SDR A 1' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 SDR S . ? SDR A 1 . ? 1_555 ? 2 AC1 6 ASP A 346 ? ASP A 387 . ? 1_555 ? 3 AC1 6 GLU A 384 ? GLU A 425 . ? 1_555 ? 4 AC1 6 HIS A 512 ? HIS A 553 . ? 1_555 ? 5 AC1 6 ZN C . ? ZN A 1752 . ? 1_555 ? 6 AC1 6 HOH T . ? HOH A 2271 . ? 1_555 ? 7 AC2 7 SDR S . ? SDR A 1 . ? 1_555 ? 8 AC2 7 HIS A 336 ? HIS A 377 . ? 1_555 ? 9 AC2 7 ASP A 346 ? ASP A 387 . ? 1_555 ? 10 AC2 7 GLU A 384 ? GLU A 425 . ? 1_555 ? 11 AC2 7 ASP A 412 ? ASP A 453 . ? 1_555 ? 12 AC2 7 ZN B . ? ZN A 1751 . ? 1_555 ? 13 AC2 7 HOH T . ? HOH A 2271 . ? 1_555 ? 14 AC3 5 THR A 228 ? THR A 269 . ? 1_555 ? 15 AC3 5 TYR A 231 ? TYR A 272 . ? 1_555 ? 16 AC3 5 GLU A 392 ? GLU A 433 . ? 1_555 ? 17 AC3 5 GLU A 395 ? GLU A 436 . ? 1_555 ? 18 AC3 5 HOH T . ? HOH A 1805 . ? 1_555 ? 19 AC4 4 ASN A 410 ? ASN A 451 . ? 1_555 ? 20 AC4 4 ASP A 412 ? ASP A 453 . ? 1_555 ? 21 AC4 4 ARG A 493 ? ARG A 534 . ? 1_555 ? 22 AC4 4 ARG A 495 ? ARG A 536 . ? 1_555 ? 23 AC5 7 ASN A 35 ? ASN A 76 . ? 1_555 ? 24 AC5 7 GLN A 54 ? GLN A 95 . ? 1_555 ? 25 AC5 7 GLN A 58 ? GLN A 99 . ? 1_555 ? 26 AC5 7 NAG G . ? NAG A 1756 . ? 1_555 ? 27 AC5 7 HOH T . ? HOH A 2031 . ? 1_555 ? 28 AC5 7 HOH T . ? HOH A 2058 . ? 1_555 ? 29 AC5 7 HOH T . ? HOH A 2241 . ? 1_555 ? 30 AC6 3 NAG F . ? NAG A 1755 . ? 1_555 ? 31 AC6 3 HOH T . ? HOH A 2038 . ? 1_555 ? 32 AC6 3 HOH T . ? HOH A 2241 . ? 1_555 ? 33 AC7 4 ASN A 80 ? ASN A 121 . ? 1_555 ? 34 AC7 4 THR A 82 ? THR A 123 . ? 1_555 ? 35 AC7 4 HIS A 83 ? HIS A 124 . ? 1_555 ? 36 AC7 4 THR A 308 ? THR A 349 . ? 1_555 ? 37 AC8 5 TYR A 86 ? TYR A 127 . ? 1_555 ? 38 AC8 5 GLU A 96 ? GLU A 137 . ? 1_555 ? 39 AC8 5 ILE A 97 ? ILE A 138 . ? 1_555 ? 40 AC8 5 ASN A 99 ? ASN A 140 . ? 1_555 ? 41 AC8 5 NAG J . ? NAG A 1767 . ? 1_555 ? 42 AC9 1 NAG I . ? NAG A 1758 . ? 1_555 ? 43 BC1 2 ASN A 154 ? ASN A 195 . ? 1_555 ? 44 BC1 2 SER A 156 ? SER A 197 . ? 1_555 ? 45 BC2 9 TRP A 205 ? TRP A 246 . ? 1_555 ? 46 BC2 9 ASN A 418 ? ASN A 459 . ? 1_555 ? 47 BC2 9 PHE A 524 ? PHE A 565 . ? 1_555 ? 48 BC2 9 TYR A 525 ? TYR A 566 . ? 1_555 ? 49 BC2 9 HOH T . ? HOH A 1875 . ? 1_555 ? 50 BC2 9 HOH T . ? HOH A 2049 . ? 1_555 ? 51 BC2 9 HOH T . ? HOH A 2091 . ? 1_555 ? 52 BC2 9 HOH T . ? HOH A 2137 . ? 1_555 ? 53 BC2 9 HOH T . ? HOH A 2222 . ? 1_555 ? 54 BC3 5 SER A 431 ? SER A 472 . ? 1_555 ? 55 BC3 5 ASN A 435 ? ASN A 476 . ? 1_555 ? 56 BC3 5 NAG N . ? NAG A 1762 . ? 1_555 ? 57 BC3 5 HOH T . ? HOH A 2055 . ? 1_555 ? 58 BC3 5 HOH T . ? HOH A 2297 . ? 1_555 ? 59 BC4 3 NAG M . ? NAG A 1761 . ? 1_555 ? 60 BC4 3 HOH T . ? HOH A 2268 . ? 1_555 ? 61 BC4 3 HOH T . ? HOH A 2290 . ? 1_555 ? 62 BC5 9 TYR A 236 ? TYR A 277 . ? 2_565 ? 63 BC5 9 SER A 590 ? SER A 631 . ? 1_555 ? 64 BC5 9 SER A 593 ? SER A 634 . ? 1_555 ? 65 BC5 9 ASN A 597 ? ASN A 638 . ? 1_555 ? 66 BC5 9 GLN A 699 ? GLN A 740 . ? 1_555 ? 67 BC5 9 NAG P . ? NAG A 1764 . ? 1_555 ? 68 BC5 9 HOH T . ? HOH A 1924 . ? 1_555 ? 69 BC5 9 HOH T . ? HOH A 1954 . ? 2_565 ? 70 BC5 9 HOH T . ? HOH A 2119 . ? 1_555 ? 71 BC6 3 GLU A 235 ? GLU A 276 . ? 2_565 ? 72 BC6 3 NAG O . ? NAG A 1763 . ? 1_555 ? 73 BC6 3 BMA Q . ? BMA A 1765 . ? 1_555 ? 74 BC7 7 HIS A 71 ? HIS A 112 . ? 2_565 ? 75 BC7 7 GLU A 235 ? GLU A 276 . ? 2_565 ? 76 BC7 7 LYS A 283 ? LYS A 324 . ? 7_555 ? 77 BC7 7 ARG A 313 ? ARG A 354 . ? 2_565 ? 78 BC7 7 NAG P . ? NAG A 1764 . ? 1_555 ? 79 BC7 7 MAN R . ? MAN A 1766 . ? 1_555 ? 80 BC7 7 HOH T . ? HOH A 2266 . ? 1_555 ? 81 BC8 8 PHE A 194 ? PHE A 235 . ? 7_555 ? 82 BC8 8 LYS A 199 ? LYS A 240 . ? 7_555 ? 83 BC8 8 SER A 200 ? SER A 241 . ? 7_555 ? 84 BC8 8 GLU A 235 ? GLU A 276 . ? 2_565 ? 85 BC8 8 BMA Q . ? BMA A 1765 . ? 1_555 ? 86 BC8 8 HOH T . ? HOH A 1983 . ? 1_555 ? 87 BC8 8 HOH T . ? HOH A 2117 . ? 1_555 ? 88 BC8 8 HOH T . ? HOH A 2120 . ? 7_555 ? 89 BC9 25 PHE A 168 ? PHE A 209 . ? 1_555 ? 90 BC9 25 ARG A 169 ? ARG A 210 . ? 1_555 ? 91 BC9 25 ASN A 216 ? ASN A 257 . ? 1_555 ? 92 BC9 25 ASP A 346 ? ASP A 387 . ? 1_555 ? 93 BC9 25 ALA A 383 ? ALA A 424 . ? 1_555 ? 94 BC9 25 GLU A 384 ? GLU A 425 . ? 1_555 ? 95 BC9 25 GLY A 386 ? GLY A 427 . ? 1_555 ? 96 BC9 25 ASP A 412 ? ASP A 453 . ? 1_555 ? 97 BC9 25 SER A 413 ? SER A 454 . ? 1_555 ? 98 BC9 25 SER A 476 ? SER A 517 . ? 1_555 ? 99 BC9 25 GLY A 477 ? GLY A 518 . ? 1_555 ? 100 BC9 25 ASN A 478 ? ASN A 519 . ? 1_555 ? 101 BC9 25 ARG A 493 ? ARG A 534 . ? 1_555 ? 102 BC9 25 ARG A 495 ? ARG A 536 . ? 1_555 ? 103 BC9 25 TYR A 511 ? TYR A 552 . ? 1_555 ? 104 BC9 25 HIS A 512 ? HIS A 553 . ? 1_555 ? 105 BC9 25 LYS A 658 ? LYS A 699 . ? 1_555 ? 106 BC9 25 TYR A 659 ? TYR A 700 . ? 1_555 ? 107 BC9 25 ZN B . ? ZN A 1751 . ? 1_555 ? 108 BC9 25 ZN C . ? ZN A 1752 . ? 1_555 ? 109 BC9 25 HOH T . ? HOH A 1808 . ? 1_555 ? 110 BC9 25 HOH T . ? HOH A 1964 . ? 1_555 ? 111 BC9 25 HOH T . ? HOH A 2271 . ? 1_555 ? 112 BC9 25 HOH T . ? HOH A 2274 . ? 1_555 ? 113 BC9 25 HOH T . ? HOH A 2285 . ? 1_555 ? # _database_PDB_matrix.entry_id 3SJG _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 3SJG _atom_sites.fract_transf_matrix[1][1] 0.009778 _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] 0.007693 _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] 0.006285 _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 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 ? 16.698 45.503 82.680 1.00 60.34 ? 55 LYS A N 1 ATOM 2 C CA . LYS A 1 14 ? 16.233 46.635 81.831 1.00 58.82 ? 55 LYS A CA 1 ATOM 3 C C . LYS A 1 14 ? 15.843 46.166 80.432 1.00 56.36 ? 55 LYS A C 1 ATOM 4 O O . LYS A 1 14 ? 16.440 45.236 79.883 1.00 56.18 ? 55 LYS A O 1 ATOM 5 C CB . LYS A 1 14 ? 17.302 47.738 81.733 1.00 59.58 ? 55 LYS A CB 1 ATOM 6 C CG . LYS A 1 14 ? 17.036 48.991 82.590 1.00 62.49 ? 55 LYS A CG 1 ATOM 7 C CD . LYS A 1 14 ? 17.241 50.249 81.714 1.00 64.16 ? 55 LYS A CD 1 ATOM 8 C CE . LYS A 1 14 ? 16.092 51.243 81.847 1.00 64.38 ? 55 LYS A CE 1 ATOM 9 N NZ . LYS A 1 14 ? 15.769 51.890 80.535 1.00 63.99 ? 55 LYS A NZ 1 ATOM 10 N N . HIS A 1 15 ? 14.817 46.804 79.880 1.00 54.15 ? 56 HIS A N 1 ATOM 11 C CA . HIS A 1 15 ? 14.465 46.634 78.475 1.00 51.04 ? 56 HIS A CA 1 ATOM 12 C C . HIS A 1 15 ? 14.923 47.879 77.751 1.00 48.32 ? 56 HIS A C 1 ATOM 13 O O . HIS A 1 15 ? 14.175 48.857 77.644 1.00 49.66 ? 56 HIS A O 1 ATOM 14 C CB . HIS A 1 15 ? 12.960 46.475 78.303 1.00 51.29 ? 56 HIS A CB 1 ATOM 15 C CG . HIS A 1 15 ? 12.420 45.167 78.792 1.00 53.86 ? 56 HIS A CG 1 ATOM 16 N ND1 . HIS A 1 15 ? 11.287 45.082 79.576 1.00 55.76 ? 56 HIS A ND1 1 ATOM 17 C CD2 . HIS A 1 15 ? 12.855 43.897 78.612 1.00 54.68 ? 56 HIS A CD2 1 ATOM 18 C CE1 . HIS A 1 15 ? 11.045 43.812 79.852 1.00 57.91 ? 56 HIS A CE1 1 ATOM 19 N NE2 . HIS A 1 15 ? 11.982 43.074 79.278 1.00 57.28 ? 56 HIS A NE2 1 ATOM 20 N N . ASN A 1 16 ? 16.156 47.862 77.268 1.00 43.85 ? 57 ASN A N 1 ATOM 21 C CA . ASN A 1 16 ? 16.707 49.028 76.609 1.00 40.52 ? 57 ASN A CA 1 ATOM 22 C C . ASN A 1 16 ? 17.314 48.546 75.318 1.00 37.12 ? 57 ASN A C 1 ATOM 23 O O . ASN A 1 16 ? 17.170 47.349 74.971 1.00 35.10 ? 57 ASN A O 1 ATOM 24 C CB . ASN A 1 16 ? 17.762 49.722 77.465 1.00 40.16 ? 57 ASN A CB 1 ATOM 25 C CG . ASN A 1 16 ? 18.726 48.752 78.105 1.00 41.82 ? 57 ASN A CG 1 ATOM 26 O OD1 . ASN A 1 16 ? 18.888 47.613 77.660 1.00 41.30 ? 57 ASN A OD1 1 ATOM 27 N ND2 . ASN A 1 16 ? 19.353 49.190 79.208 1.00 41.29 ? 57 ASN A ND2 1 ATOM 28 N N . MET A 1 17 ? 17.982 49.446 74.601 1.00 35.57 ? 58 MET A N 1 ATOM 29 C CA . MET A 1 17 ? 18.522 48.985 73.319 1.00 34.58 ? 58 MET A CA 1 ATOM 30 C C . MET A 1 17 ? 19.542 47.863 73.510 1.00 34.26 ? 58 MET A C 1 ATOM 31 O O . MET A 1 17 ? 19.570 46.916 72.706 1.00 34.28 ? 58 MET A O 1 ATOM 32 C CB . MET A 1 17 ? 19.153 50.066 72.466 1.00 33.49 ? 58 MET A CB 1 ATOM 33 C CG . MET A 1 17 ? 19.299 49.507 70.982 1.00 37.00 ? 58 MET A CG 1 ATOM 34 S SD . MET A 1 17 ? 20.259 50.618 70.007 1.00 43.52 ? 58 MET A SD 1 ATOM 35 C CE . MET A 1 17 ? 19.279 52.015 70.111 1.00 42.50 ? 58 MET A CE 1 ATOM 36 N N . LYS A 1 18 ? 20.363 47.936 74.553 1.00 35.36 ? 59 LYS A N 1 ATOM 37 C CA . LYS A 1 18 ? 21.363 46.919 74.754 1.00 35.85 ? 59 LYS A CA 1 ATOM 38 C C . LYS A 1 18 ? 20.727 45.532 74.934 1.00 35.43 ? 59 LYS A C 1 ATOM 39 O O . LYS A 1 18 ? 21.259 44.550 74.422 1.00 36.17 ? 59 LYS A O 1 ATOM 40 C CB . LYS A 1 18 ? 22.270 47.256 75.963 1.00 37.65 ? 59 LYS A CB 1 ATOM 41 C CG . LYS A 1 18 ? 23.406 46.257 76.126 1.00 41.49 ? 59 LYS A CG 1 ATOM 42 C CD . LYS A 1 18 ? 24.392 46.767 77.203 1.00 47.90 ? 59 LYS A CD 1 ATOM 43 C CE . LYS A 1 18 ? 25.659 45.899 77.320 1.00 54.71 ? 59 LYS A CE 1 ATOM 44 N NZ . LYS A 1 18 ? 25.388 44.568 77.948 1.00 56.57 ? 59 LYS A NZ 1 ATOM 45 N N . ALA A 1 19 ? 19.576 45.463 75.608 1.00 35.45 ? 60 ALA A N 1 ATOM 46 C CA . ALA A 1 19 ? 18.848 44.191 75.788 1.00 36.57 ? 60 ALA A CA 1 ATOM 47 C C . ALA A 1 19 ? 18.365 43.628 74.439 1.00 34.41 ? 60 ALA A C 1 ATOM 48 O O . ALA A 1 19 ? 18.488 42.441 74.174 1.00 34.82 ? 60 ALA A O 1 ATOM 49 C CB . ALA A 1 19 ? 17.666 44.369 76.725 1.00 37.84 ? 60 ALA A CB 1 ATOM 50 N N . PHE A 1 20 ? 17.822 44.511 73.617 1.00 32.69 ? 61 PHE A N 1 ATOM 51 C CA . PHE A 1 20 ? 17.390 44.136 72.278 1.00 31.62 ? 61 PHE A CA 1 ATOM 52 C C . PHE A 1 20 ? 18.575 43.607 71.475 1.00 31.58 ? 61 PHE A C 1 ATOM 53 O O . PHE A 1 20 ? 18.479 42.536 70.837 1.00 31.45 ? 61 PHE A O 1 ATOM 54 C CB . PHE A 1 20 ? 16.747 45.324 71.556 1.00 29.19 ? 61 PHE A CB 1 ATOM 55 C CG . PHE A 1 20 ? 16.663 45.104 70.067 1.00 29.28 ? 61 PHE A CG 1 ATOM 56 C CD1 . PHE A 1 20 ? 15.696 44.246 69.536 1.00 28.14 ? 61 PHE A CD1 1 ATOM 57 C CD2 . PHE A 1 20 ? 17.604 45.687 69.243 1.00 28.21 ? 61 PHE A CD2 1 ATOM 58 C CE1 . PHE A 1 20 ? 15.663 43.995 68.120 1.00 27.82 ? 61 PHE A CE1 1 ATOM 59 C CE2 . PHE A 1 20 ? 17.569 45.465 67.856 1.00 27.80 ? 61 PHE A CE2 1 ATOM 60 C CZ . PHE A 1 20 ? 16.602 44.628 67.313 1.00 28.98 ? 61 PHE A CZ 1 ATOM 61 N N . LEU A 1 21 ? 19.685 44.353 71.497 1.00 30.93 ? 62 LEU A N 1 ATOM 62 C CA . LEU A 1 21 ? 20.828 43.979 70.658 1.00 31.66 ? 62 LEU A CA 1 ATOM 63 C C . LEU A 1 21 ? 21.470 42.678 71.124 1.00 32.77 ? 62 LEU A C 1 ATOM 64 O O . LEU A 1 21 ? 21.909 41.867 70.310 1.00 33.42 ? 62 LEU A O 1 ATOM 65 C CB . LEU A 1 21 ? 21.885 45.079 70.663 1.00 32.54 ? 62 LEU A CB 1 ATOM 66 C CG . LEU A 1 21 ? 21.520 46.394 69.989 1.00 30.14 ? 62 LEU A CG 1 ATOM 67 C CD1 . LEU A 1 21 ? 22.551 47.463 70.346 1.00 34.45 ? 62 LEU A CD1 1 ATOM 68 C CD2 . LEU A 1 21 ? 21.387 46.234 68.454 1.00 30.18 ? 62 LEU A CD2 1 ATOM 69 N N . ASP A 1 22 ? 21.526 42.489 72.442 1.00 33.82 ? 63 ASP A N 1 ATOM 70 C CA . ASP A 1 22 ? 22.189 41.305 72.980 1.00 35.68 ? 63 ASP A CA 1 ATOM 71 C C . ASP A 1 22 ? 21.418 40.030 72.674 1.00 35.72 ? 63 ASP A C 1 ATOM 72 O O . ASP A 1 22 ? 22.003 38.941 72.661 1.00 36.35 ? 63 ASP A O 1 ATOM 73 C CB . ASP A 1 22 ? 22.352 41.438 74.499 1.00 37.63 ? 63 ASP A CB 1 ATOM 74 C CG . ASP A 1 22 ? 23.500 42.351 74.885 1.00 40.61 ? 63 ASP A CG 1 ATOM 75 O OD1 . ASP A 1 22 ? 24.330 42.683 74.010 1.00 43.30 ? 63 ASP A OD1 1 ATOM 76 O OD2 . ASP A 1 22 ? 23.564 42.732 76.082 1.00 44.18 ? 63 ASP A OD2 1 ATOM 77 N N . GLU A 1 23 ? 20.120 40.160 72.424 1.00 34.87 ? 64 GLU A N 1 ATOM 78 C CA . GLU A 1 23 ? 19.296 38.986 72.179 1.00 35.02 ? 64 GLU A CA 1 ATOM 79 C C . GLU A 1 23 ? 19.511 38.436 70.754 1.00 33.58 ? 64 GLU A C 1 ATOM 80 O O . GLU A 1 23 ? 19.256 37.252 70.531 1.00 33.96 ? 64 GLU A O 1 ATOM 81 C CB . GLU A 1 23 ? 17.822 39.300 72.454 1.00 35.20 ? 64 GLU A CB 1 ATOM 82 C CG . GLU A 1 23 ? 16.799 38.186 72.190 1.00 37.80 ? 64 GLU A CG 1 ATOM 83 C CD . GLU A 1 23 ? 16.960 36.951 73.061 1.00 43.40 ? 64 GLU A CD 1 ATOM 84 O OE1 . GLU A 1 23 ? 17.245 37.088 74.278 1.00 44.43 ? 64 GLU A OE1 1 ATOM 85 O OE2 . GLU A 1 23 ? 16.803 35.820 72.542 1.00 40.92 ? 64 GLU A OE2 1 ATOM 86 N N . LEU A 1 24 ? 19.967 39.295 69.827 1.00 32.15 ? 65 LEU A N 1 ATOM 87 C CA . LEU A 1 24 ? 20.277 38.884 68.427 1.00 31.00 ? 65 LEU A CA 1 ATOM 88 C C . LEU A 1 24 ? 21.420 37.885 68.397 1.00 31.82 ? 65 LEU A C 1 ATOM 89 O O . LEU A 1 24 ? 22.428 38.117 69.061 1.00 33.01 ? 65 LEU A O 1 ATOM 90 C CB . LEU A 1 24 ? 20.711 40.106 67.617 1.00 29.89 ? 65 LEU A CB 1 ATOM 91 C CG . LEU A 1 24 ? 19.717 41.261 67.509 1.00 28.90 ? 65 LEU A CG 1 ATOM 92 C CD1 . LEU A 1 24 ? 20.429 42.502 66.897 1.00 28.03 ? 65 LEU A CD1 1 ATOM 93 C CD2 . LEU A 1 24 ? 18.497 40.821 66.660 1.00 25.69 ? 65 LEU A CD2 1 ATOM 94 N N . LYS A 1 25 ? 21.288 36.806 67.611 1.00 30.35 ? 66 LYS A N 1 ATOM 95 C CA . LYS A 1 25 ? 22.311 35.745 67.598 1.00 31.80 ? 66 LYS A CA 1 ATOM 96 C C . LYS A 1 25 ? 22.674 35.375 66.177 1.00 30.93 ? 66 LYS A C 1 ATOM 97 O O . LYS A 1 25 ? 21.784 35.115 65.353 1.00 29.76 ? 66 LYS A O 1 ATOM 98 C CB . LYS A 1 25 ? 21.794 34.476 68.300 1.00 33.22 ? 66 LYS A CB 1 ATOM 99 C CG . LYS A 1 25 ? 21.392 34.652 69.807 1.00 36.29 ? 66 LYS A CG 1 ATOM 100 C CD . LYS A 1 25 ? 22.591 34.998 70.664 1.00 44.80 ? 66 LYS A CD 1 ATOM 101 C CE . LYS A 1 25 ? 22.306 34.885 72.177 1.00 47.28 ? 66 LYS A CE 1 ATOM 102 N NZ . LYS A 1 25 ? 21.408 35.973 72.609 1.00 45.51 ? 66 LYS A NZ 1 ATOM 103 N N . ALA A 1 26 ? 23.980 35.290 65.920 1.00 30.90 ? 67 ALA A N 1 ATOM 104 C CA . ALA A 1 26 ? 24.499 34.900 64.605 1.00 30.58 ? 67 ALA A CA 1 ATOM 105 C C . ALA A 1 26 ? 23.974 33.524 64.230 1.00 30.21 ? 67 ALA A C 1 ATOM 106 O O . ALA A 1 26 ? 23.651 33.280 63.069 1.00 28.20 ? 67 ALA A O 1 ATOM 107 C CB . ALA A 1 26 ? 26.027 34.922 64.614 1.00 30.57 ? 67 ALA A CB 1 ATOM 108 N N . GLU A 1 27 ? 23.913 32.617 65.204 1.00 31.19 ? 68 GLU A N 1 ATOM 109 C CA . GLU A 1 27 ? 23.454 31.235 64.941 1.00 32.03 ? 68 GLU A CA 1 ATOM 110 C C . GLU A 1 27 ? 22.010 31.135 64.459 1.00 30.75 ? 68 GLU A C 1 ATOM 111 O O . GLU A 1 27 ? 21.684 30.253 63.654 1.00 31.19 ? 68 GLU A O 1 ATOM 112 C CB . GLU A 1 27 ? 23.671 30.321 66.177 1.00 33.85 ? 68 GLU A CB 1 ATOM 113 C CG A GLU A 1 27 ? 23.435 28.833 65.870 0.50 34.84 ? 68 GLU A CG 1 ATOM 114 C CG B GLU A 1 27 ? 22.705 30.647 67.360 0.50 36.55 ? 68 GLU A CG 1 ATOM 115 C CD A GLU A 1 27 ? 24.444 28.228 64.891 0.50 38.12 ? 68 GLU A CD 1 ATOM 116 C CD B GLU A 1 27 ? 23.145 30.154 68.741 0.50 43.32 ? 68 GLU A CD 1 ATOM 117 O OE1 A GLU A 1 27 ? 25.614 28.667 64.832 0.50 38.33 ? 68 GLU A OE1 1 ATOM 118 O OE1 B GLU A 1 27 ? 23.414 31.015 69.620 0.50 43.92 ? 68 GLU A OE1 1 ATOM 119 O OE2 A GLU A 1 27 ? 24.064 27.281 64.180 0.50 41.95 ? 68 GLU A OE2 1 ATOM 120 O OE2 B GLU A 1 27 ? 23.196 28.920 68.955 0.50 47.00 ? 68 GLU A OE2 1 ATOM 121 N N . ASN A 1 28 ? 21.145 32.027 64.956 1.00 29.52 ? 69 ASN A N 1 ATOM 122 C CA . ASN A 1 28 ? 19.743 32.068 64.531 1.00 29.23 ? 69 ASN A CA 1 ATOM 123 C C . ASN A 1 28 ? 19.644 32.562 63.123 1.00 28.56 ? 69 ASN A C 1 ATOM 124 O O . ASN A 1 28 ? 18.860 32.013 62.318 1.00 28.53 ? 69 ASN A O 1 ATOM 125 C CB . ASN A 1 28 ? 18.910 32.967 65.462 1.00 30.15 ? 69 ASN A CB 1 ATOM 126 C CG . ASN A 1 28 ? 18.656 32.321 66.828 1.00 32.59 ? 69 ASN A CG 1 ATOM 127 O OD1 . ASN A 1 28 ? 18.630 31.100 66.964 1.00 36.55 ? 69 ASN A OD1 1 ATOM 128 N ND2 . ASN A 1 28 ? 18.501 33.147 67.839 1.00 31.99 ? 69 ASN A ND2 1 ATOM 129 N N . ILE A 1 29 ? 20.424 33.596 62.809 1.00 27.01 ? 70 ILE A N 1 ATOM 130 C CA . ILE A 1 29 ? 20.440 34.147 61.450 1.00 26.35 ? 70 ILE A CA 1 ATOM 131 C C . ILE A 1 29 ? 20.884 33.048 60.472 1.00 26.46 ? 70 ILE A C 1 ATOM 132 O O . ILE A 1 29 ? 20.272 32.885 59.396 1.00 26.96 ? 70 ILE A O 1 ATOM 133 C CB . ILE A 1 29 ? 21.355 35.374 61.330 1.00 25.94 ? 70 ILE A CB 1 ATOM 134 C CG1 . ILE A 1 29 ? 20.843 36.495 62.268 1.00 26.45 ? 70 ILE A CG1 1 ATOM 135 C CG2 . ILE A 1 29 ? 21.360 35.918 59.868 1.00 26.32 ? 70 ILE A CG2 1 ATOM 136 C CD1 . ILE A 1 29 ? 21.829 37.664 62.385 1.00 28.71 ? 70 ILE A CD1 1 ATOM 137 N N . LYS A 1 30 ? 21.907 32.283 60.856 1.00 26.46 ? 71 LYS A N 1 ATOM 138 C CA . LYS A 1 30 ? 22.381 31.158 60.025 1.00 26.89 ? 71 LYS A CA 1 ATOM 139 C C . LYS A 1 30 ? 21.276 30.125 59.775 1.00 27.96 ? 71 LYS A C 1 ATOM 140 O O . LYS A 1 30 ? 21.058 29.691 58.634 1.00 28.06 ? 71 LYS A O 1 ATOM 141 C CB . LYS A 1 30 ? 23.574 30.479 60.735 1.00 27.81 ? 71 LYS A CB 1 ATOM 142 C CG . LYS A 1 30 ? 24.203 29.352 59.931 1.00 28.32 ? 71 LYS A CG 1 ATOM 143 C CD . LYS A 1 30 ? 25.385 28.802 60.771 1.00 31.09 ? 71 LYS A CD 1 ATOM 144 C CE . LYS A 1 30 ? 26.110 27.736 60.025 1.00 35.59 ? 71 LYS A CE 1 ATOM 145 N NZ . LYS A 1 30 ? 27.254 27.170 60.841 1.00 36.00 ? 71 LYS A NZ 1 ATOM 146 N N . LYS A 1 31 ? 20.613 29.703 60.853 1.00 28.53 ? 72 LYS A N 1 ATOM 147 C CA . LYS A 1 31 ? 19.506 28.747 60.777 1.00 29.48 ? 72 LYS A CA 1 ATOM 148 C C . LYS A 1 31 ? 18.369 29.238 59.880 1.00 27.66 ? 72 LYS A C 1 ATOM 149 O O . LYS A 1 31 ? 17.837 28.489 59.070 1.00 27.38 ? 72 LYS A O 1 ATOM 150 C CB . LYS A 1 31 ? 18.976 28.422 62.180 1.00 30.72 ? 72 LYS A CB 1 ATOM 151 C CG . LYS A 1 31 ? 19.917 27.546 62.956 1.00 37.87 ? 72 LYS A CG 1 ATOM 152 C CD . LYS A 1 31 ? 19.481 27.417 64.413 1.00 43.69 ? 72 LYS A CD 1 ATOM 153 C CE . LYS A 1 31 ? 20.461 26.511 65.154 1.00 48.99 ? 72 LYS A CE 1 ATOM 154 N NZ . LYS A 1 31 ? 20.041 26.311 66.569 1.00 51.95 ? 72 LYS A NZ 1 ATOM 155 N N . PHE A 1 32 ? 18.028 30.510 60.013 1.00 26.71 ? 73 PHE A N 1 ATOM 156 C CA . PHE A 1 32 ? 16.970 31.060 59.189 1.00 25.28 ? 73 PHE A CA 1 ATOM 157 C C . PHE A 1 32 ? 17.397 31.128 57.741 1.00 25.23 ? 73 PHE A C 1 ATOM 158 O O . PHE A 1 32 ? 16.598 30.809 56.826 1.00 25.79 ? 73 PHE A O 1 ATOM 159 C CB . PHE A 1 32 ? 16.542 32.465 59.698 1.00 25.16 ? 73 PHE A CB 1 ATOM 160 C CG . PHE A 1 32 ? 15.977 32.467 61.090 1.00 26.25 ? 73 PHE A CG 1 ATOM 161 C CD1 . PHE A 1 32 ? 15.247 31.382 61.591 1.00 28.81 ? 73 PHE A CD1 1 ATOM 162 C CD2 . PHE A 1 32 ? 16.144 33.603 61.883 1.00 25.52 ? 73 PHE A CD2 1 ATOM 163 C CE1 . PHE A 1 32 ? 14.741 31.406 62.884 1.00 31.35 ? 73 PHE A CE1 1 ATOM 164 C CE2 . PHE A 1 32 ? 15.621 33.668 63.186 1.00 29.72 ? 73 PHE A CE2 1 ATOM 165 C CZ . PHE A 1 32 ? 14.911 32.584 63.690 1.00 30.74 ? 73 PHE A CZ 1 ATOM 166 N N . LEU A 1 33 ? 18.648 31.523 57.503 1.00 24.54 ? 74 LEU A N 1 ATOM 167 C CA . LEU A 1 33 ? 19.095 31.608 56.105 1.00 24.68 ? 74 LEU A CA 1 ATOM 168 C C . LEU A 1 33 ? 19.043 30.227 55.486 1.00 25.05 ? 74 LEU A C 1 ATOM 169 O O . LEU A 1 33 ? 18.554 30.092 54.362 1.00 24.63 ? 74 LEU A O 1 ATOM 170 C CB . LEU A 1 33 ? 20.513 32.159 55.980 1.00 24.81 ? 74 LEU A CB 1 ATOM 171 C CG . LEU A 1 33 ? 20.994 32.269 54.523 1.00 24.95 ? 74 LEU A CG 1 ATOM 172 C CD1 . LEU A 1 33 ? 20.201 33.340 53.762 1.00 24.38 ? 74 LEU A CD1 1 ATOM 173 C CD2 . LEU A 1 33 ? 22.469 32.580 54.528 1.00 26.85 ? 74 LEU A CD2 1 ATOM 174 N N . TYR A 1 34 ? 19.552 29.197 56.181 1.00 25.15 ? 75 TYR A N 1 ATOM 175 C CA . TYR A 1 34 ? 19.422 27.841 55.643 1.00 26.05 ? 75 TYR A CA 1 ATOM 176 C C . TYR A 1 34 ? 17.941 27.511 55.331 1.00 26.54 ? 75 TYR A C 1 ATOM 177 O O . TYR A 1 34 ? 17.612 27.005 54.277 1.00 26.81 ? 75 TYR A O 1 ATOM 178 C CB . TYR A 1 34 ? 20.036 26.826 56.638 1.00 26.35 ? 75 TYR A CB 1 ATOM 179 C CG . TYR A 1 34 ? 19.955 25.437 56.138 1.00 28.25 ? 75 TYR A CG 1 ATOM 180 C CD1 . TYR A 1 34 ? 20.986 24.910 55.358 1.00 28.93 ? 75 TYR A CD1 1 ATOM 181 C CD2 . TYR A 1 34 ? 18.839 24.656 56.411 1.00 31.38 ? 75 TYR A CD2 1 ATOM 182 C CE1 . TYR A 1 34 ? 20.930 23.594 54.890 1.00 30.83 ? 75 TYR A CE1 1 ATOM 183 C CE2 . TYR A 1 34 ? 18.763 23.308 55.931 1.00 34.50 ? 75 TYR A CE2 1 ATOM 184 C CZ . TYR A 1 34 ? 19.809 22.816 55.177 1.00 35.94 ? 75 TYR A CZ 1 ATOM 185 O OH . TYR A 1 34 ? 19.773 21.520 54.688 1.00 39.07 ? 75 TYR A OH 1 ATOM 186 N N . ASN A 1 35 ? 17.050 27.824 56.257 1.00 25.55 ? 76 ASN A N 1 ATOM 187 C CA . ASN A 1 35 ? 15.633 27.491 56.088 1.00 26.19 ? 76 ASN A CA 1 ATOM 188 C C . ASN A 1 35 ? 14.968 28.166 54.885 1.00 25.38 ? 76 ASN A C 1 ATOM 189 O O . ASN A 1 35 ? 14.067 27.574 54.253 1.00 26.07 ? 76 ASN A O 1 ATOM 190 C CB . ASN A 1 35 ? 14.901 27.891 57.359 1.00 26.48 ? 76 ASN A CB 1 ATOM 191 C CG . ASN A 1 35 ? 13.437 27.569 57.321 1.00 28.47 ? 76 ASN A CG 1 ATOM 192 O OD1 . ASN A 1 35 ? 12.598 28.398 56.935 1.00 29.60 ? 76 ASN A OD1 1 ATOM 193 N ND2 . ASN A 1 35 ? 13.112 26.348 57.724 1.00 31.51 ? 76 ASN A ND2 1 ATOM 194 N N . PHE A 1 36 ? 15.432 29.374 54.540 1.00 24.04 ? 77 PHE A N 1 ATOM 195 C CA . PHE A 1 36 ? 14.801 30.159 53.496 1.00 23.73 ? 77 PHE A CA 1 ATOM 196 C C . PHE A 1 36 ? 15.379 29.879 52.102 1.00 23.04 ? 77 PHE A C 1 ATOM 197 O O . PHE A 1 36 ? 14.934 30.486 51.126 1.00 23.79 ? 77 PHE A O 1 ATOM 198 C CB . PHE A 1 36 ? 14.979 31.690 53.754 1.00 24.17 ? 77 PHE A CB 1 ATOM 199 C CG . PHE A 1 36 ? 14.271 32.224 54.982 1.00 24.11 ? 77 PHE A CG 1 ATOM 200 C CD1 . PHE A 1 36 ? 13.319 31.468 55.662 1.00 24.66 ? 77 PHE A CD1 1 ATOM 201 C CD2 . PHE A 1 36 ? 14.570 33.512 55.430 1.00 23.79 ? 77 PHE A CD2 1 ATOM 202 C CE1 . PHE A 1 36 ? 12.668 31.987 56.839 1.00 24.48 ? 77 PHE A CE1 1 ATOM 203 C CE2 . PHE A 1 36 ? 13.899 34.093 56.573 1.00 24.15 ? 77 PHE A CE2 1 ATOM 204 C CZ . PHE A 1 36 ? 12.943 33.328 57.262 1.00 23.73 ? 77 PHE A CZ 1 ATOM 205 N N . THR A 1 37 ? 16.410 29.025 52.007 1.00 23.84 ? 78 THR A N 1 ATOM 206 C CA . THR A 1 37 ? 17.127 28.931 50.752 1.00 24.04 ? 78 THR A CA 1 ATOM 207 C C . THR A 1 37 ? 17.254 27.511 50.179 1.00 24.88 ? 78 THR A C 1 ATOM 208 O O . THR A 1 37 ? 18.082 27.291 49.324 1.00 25.04 ? 78 THR A O 1 ATOM 209 C CB . THR A 1 37 ? 18.573 29.483 50.920 1.00 24.63 ? 78 THR A CB 1 ATOM 210 O OG1 . THR A 1 37 ? 19.219 28.763 51.994 1.00 24.53 ? 78 THR A OG1 1 ATOM 211 C CG2 . THR A 1 37 ? 18.529 31.020 51.239 1.00 22.51 ? 78 THR A CG2 1 ATOM 212 N N . GLN A 1 38 ? 16.435 26.574 50.657 1.00 25.22 ? 79 GLN A N 1 ATOM 213 C CA . GLN A 1 38 ? 16.533 25.176 50.203 1.00 27.66 ? 79 GLN A CA 1 ATOM 214 C C . GLN A 1 38 ? 15.819 24.938 48.883 1.00 27.52 ? 79 GLN A C 1 ATOM 215 O O . GLN A 1 38 ? 16.126 23.967 48.190 1.00 28.94 ? 79 GLN A O 1 ATOM 216 C CB . GLN A 1 38 ? 15.977 24.223 51.286 1.00 28.41 ? 79 GLN A CB 1 ATOM 217 C CG . GLN A 1 38 ? 16.806 24.302 52.557 1.00 30.37 ? 79 GLN A CG 1 ATOM 218 C CD . GLN A 1 38 ? 18.287 24.142 52.242 1.00 31.91 ? 79 GLN A CD 1 ATOM 219 O OE1 . GLN A 1 38 ? 18.713 23.061 51.813 1.00 36.03 ? 79 GLN A OE1 1 ATOM 220 N NE2 . GLN A 1 38 ? 19.079 25.222 52.420 1.00 31.52 ? 79 GLN A NE2 1 ATOM 221 N N . ILE A 1 39 ? 14.819 25.768 48.584 1.00 26.84 ? 80 ILE A N 1 ATOM 222 C CA . ILE A 1 39 ? 14.070 25.664 47.318 1.00 27.75 ? 80 ILE A CA 1 ATOM 223 C C . ILE A 1 39 ? 13.880 27.061 46.737 1.00 26.04 ? 80 ILE A C 1 ATOM 224 O O . ILE A 1 39 ? 13.987 28.047 47.478 1.00 26.05 ? 80 ILE A O 1 ATOM 225 C CB . ILE A 1 39 ? 12.662 25.008 47.517 1.00 28.71 ? 80 ILE A CB 1 ATOM 226 C CG1 . ILE A 1 39 ? 11.775 25.884 48.407 1.00 29.47 ? 80 ILE A CG1 1 ATOM 227 C CG2 . ILE A 1 39 ? 12.795 23.540 47.979 1.00 31.13 ? 80 ILE A CG2 1 ATOM 228 C CD1 . ILE A 1 39 ? 10.335 25.360 48.556 1.00 32.80 ? 80 ILE A CD1 1 ATOM 229 N N . PRO A 1 40 ? 13.608 27.165 45.423 1.00 26.04 ? 81 PRO A N 1 ATOM 230 C CA . PRO A 1 40 ? 13.335 28.505 44.865 1.00 24.84 ? 81 PRO A CA 1 ATOM 231 C C . PRO A 1 40 ? 12.073 29.156 45.444 1.00 24.74 ? 81 PRO A C 1 ATOM 232 O O . PRO A 1 40 ? 11.090 28.444 45.791 1.00 25.41 ? 81 PRO A O 1 ATOM 233 C CB . PRO A 1 40 ? 13.157 28.228 43.361 1.00 26.40 ? 81 PRO A CB 1 ATOM 234 C CG . PRO A 1 40 ? 13.896 26.863 43.118 1.00 28.39 ? 81 PRO A CG 1 ATOM 235 C CD . PRO A 1 40 ? 13.599 26.100 44.396 1.00 25.79 ? 81 PRO A CD 1 ATOM 236 N N . HIS A 1 41 ? 12.095 30.494 45.557 1.00 22.34 ? 82 HIS A N 1 ATOM 237 C CA . HIS A 1 41 ? 10.907 31.249 45.999 1.00 22.26 ? 82 HIS A CA 1 ATOM 238 C C . HIS A 1 41 ? 10.565 32.365 45.001 1.00 21.52 ? 82 HIS A C 1 ATOM 239 O O . HIS A 1 41 ? 10.470 33.531 45.363 1.00 21.91 ? 82 HIS A O 1 ATOM 240 C CB . HIS A 1 41 ? 11.127 31.808 47.429 1.00 23.13 ? 82 HIS A CB 1 ATOM 241 C CG . HIS A 1 41 ? 11.291 30.734 48.459 1.00 23.20 ? 82 HIS A CG 1 ATOM 242 N ND1 . HIS A 1 41 ? 12.515 30.403 49.001 1.00 25.29 ? 82 HIS A ND1 1 ATOM 243 C CD2 . HIS A 1 41 ? 10.400 29.839 48.961 1.00 24.35 ? 82 HIS A CD2 1 ATOM 244 C CE1 . HIS A 1 41 ? 12.356 29.397 49.851 1.00 25.24 ? 82 HIS A CE1 1 ATOM 245 N NE2 . HIS A 1 41 ? 11.083 29.033 49.842 1.00 25.59 ? 82 HIS A NE2 1 ATOM 246 N N . LEU A 1 42 ? 10.399 31.990 43.736 1.00 21.87 ? 83 LEU A N 1 ATOM 247 C CA . LEU A 1 42 ? 10.069 32.965 42.707 1.00 21.48 ? 83 LEU A CA 1 ATOM 248 C C . LEU A 1 42 ? 8.714 33.591 42.964 1.00 21.35 ? 83 LEU A C 1 ATOM 249 O O . LEU A 1 42 ? 7.741 32.891 43.338 1.00 23.28 ? 83 LEU A O 1 ATOM 250 C CB . LEU A 1 42 ? 10.069 32.224 41.339 1.00 21.02 ? 83 LEU A CB 1 ATOM 251 C CG . LEU A 1 42 ? 9.882 33.166 40.134 1.00 21.00 ? 83 LEU A CG 1 ATOM 252 C CD1 . LEU A 1 42 ? 11.072 34.073 39.873 1.00 21.68 ? 83 LEU A CD1 1 ATOM 253 C CD2 . LEU A 1 42 ? 9.805 32.132 38.855 1.00 23.01 ? 83 LEU A CD2 1 ATOM 254 N N . ALA A 1 43 ? 8.616 34.903 42.775 1.00 20.90 ? 84 ALA A N 1 ATOM 255 C CA . ALA A 1 43 ? 7.333 35.587 42.976 1.00 20.93 ? 84 ALA A CA 1 ATOM 256 C C . ALA A 1 43 ? 6.220 34.948 42.146 1.00 22.26 ? 84 ALA A C 1 ATOM 257 O O . ALA A 1 43 ? 6.440 34.559 40.980 1.00 22.07 ? 84 ALA A O 1 ATOM 258 C CB . ALA A 1 43 ? 7.455 37.064 42.598 1.00 20.68 ? 84 ALA A CB 1 ATOM 259 N N . GLY A 1 44 ? 5.057 34.805 42.778 1.00 22.48 ? 85 GLY A N 1 ATOM 260 C CA . GLY A 1 44 ? 3.847 34.271 42.132 1.00 24.56 ? 85 GLY A CA 1 ATOM 261 C C . GLY A 1 44 ? 3.766 32.763 42.100 1.00 25.85 ? 85 GLY A C 1 ATOM 262 O O . GLY A 1 44 ? 2.801 32.207 41.548 1.00 27.82 ? 85 GLY A O 1 ATOM 263 N N . THR A 1 45 ? 4.779 32.085 42.639 1.00 24.06 ? 86 THR A N 1 ATOM 264 C CA . THR A 1 45 ? 4.752 30.611 42.659 1.00 25.20 ? 86 THR A CA 1 ATOM 265 C C . THR A 1 45 ? 4.250 30.067 44.001 1.00 25.99 ? 86 THR A C 1 ATOM 266 O O . THR A 1 45 ? 4.281 30.746 45.017 1.00 26.24 ? 86 THR A O 1 ATOM 267 C CB . THR A 1 45 ? 6.157 29.996 42.378 1.00 25.86 ? 86 THR A CB 1 ATOM 268 O OG1 . THR A 1 45 ? 7.049 30.310 43.472 1.00 25.65 ? 86 THR A OG1 1 ATOM 269 C CG2 . THR A 1 45 ? 6.740 30.491 41.076 1.00 26.95 ? 86 THR A CG2 1 ATOM 270 N N . GLU A 1 46 ? 3.784 28.802 43.999 1.00 27.31 ? 87 GLU A N 1 ATOM 271 C CA . GLU A 1 46 ? 3.236 28.208 45.218 1.00 28.78 ? 87 GLU A CA 1 ATOM 272 C C . GLU A 1 46 ? 4.278 28.170 46.359 1.00 28.31 ? 87 GLU A C 1 ATOM 273 O O . GLU A 1 46 ? 3.926 28.388 47.520 1.00 28.50 ? 87 GLU A O 1 ATOM 274 C CB . GLU A 1 46 ? 2.717 26.785 44.922 1.00 32.01 ? 87 GLU A CB 1 ATOM 275 C CG . GLU A 1 46 ? 2.197 26.046 46.180 1.00 35.56 ? 87 GLU A CG 1 ATOM 276 C CD . GLU A 1 46 ? 0.885 26.629 46.732 1.00 44.82 ? 87 GLU A CD 1 ATOM 277 O OE1 . GLU A 1 46 ? 0.531 26.307 47.900 1.00 48.79 ? 87 GLU A OE1 1 ATOM 278 O OE2 . GLU A 1 46 ? 0.199 27.414 46.027 1.00 46.34 ? 87 GLU A OE2 1 ATOM 279 N N . GLN A 1 47 ? 5.539 27.896 46.014 1.00 27.93 ? 88 GLN A N 1 ATOM 280 C CA A GLN A 1 47 ? 6.597 27.825 47.008 0.60 27.93 ? 88 GLN A CA 1 ATOM 281 C CA B GLN A 1 47 ? 6.658 27.846 46.966 0.40 27.49 ? 88 GLN A CA 1 ATOM 282 C C . GLN A 1 47 ? 6.794 29.164 47.741 1.00 26.09 ? 88 GLN A C 1 ATOM 283 O O . GLN A 1 47 ? 7.057 29.198 48.969 1.00 25.95 ? 88 GLN A O 1 ATOM 284 C CB A GLN A 1 47 ? 7.892 27.347 46.345 0.60 28.77 ? 88 GLN A CB 1 ATOM 285 C CB B GLN A 1 47 ? 7.972 27.551 46.211 0.40 27.65 ? 88 GLN A CB 1 ATOM 286 C CG A GLN A 1 47 ? 7.784 25.912 45.790 0.60 32.10 ? 88 GLN A CG 1 ATOM 287 C CG B GLN A 1 47 ? 8.111 26.095 45.720 0.40 29.77 ? 88 GLN A CG 1 ATOM 288 C CD A GLN A 1 47 ? 7.073 25.801 44.427 0.60 35.04 ? 88 GLN A CD 1 ATOM 289 C CD B GLN A 1 47 ? 8.826 25.967 44.376 0.40 29.58 ? 88 GLN A CD 1 ATOM 290 O OE1 A GLN A 1 47 ? 6.837 26.790 43.715 0.60 29.44 ? 88 GLN A OE1 1 ATOM 291 O OE1 B GLN A 1 47 ? 9.922 26.494 44.175 0.40 26.83 ? 88 GLN A OE1 1 ATOM 292 N NE2 A GLN A 1 47 ? 6.746 24.566 44.057 0.60 37.44 ? 88 GLN A NE2 1 ATOM 293 N NE2 B GLN A 1 47 ? 8.199 25.252 43.450 0.40 31.68 ? 88 GLN A NE2 1 ATOM 294 N N . ASN A 1 48 ? 6.615 30.268 47.039 1.00 24.95 ? 89 ASN A N 1 ATOM 295 C CA . ASN A 1 48 ? 6.733 31.571 47.710 1.00 25.59 ? 89 ASN A CA 1 ATOM 296 C C . ASN A 1 48 ? 5.512 31.917 48.583 1.00 26.43 ? 89 ASN A C 1 ATOM 297 O O . ASN A 1 48 ? 5.663 32.585 49.620 1.00 27.36 ? 89 ASN A O 1 ATOM 298 C CB . ASN A 1 48 ? 7.061 32.673 46.711 1.00 24.50 ? 89 ASN A CB 1 ATOM 299 C CG . ASN A 1 48 ? 7.661 33.901 47.399 1.00 27.68 ? 89 ASN A CG 1 ATOM 300 O OD1 . ASN A 1 48 ? 8.398 33.781 48.387 1.00 25.87 ? 89 ASN A OD1 1 ATOM 301 N ND2 . ASN A 1 48 ? 7.388 35.061 46.863 1.00 26.00 ? 89 ASN A ND2 1 ATOM 302 N N . PHE A 1 49 ? 4.313 31.441 48.195 1.00 26.08 ? 90 PHE A N 1 ATOM 303 C CA . PHE A 1 49 ? 3.113 31.582 49.031 1.00 26.42 ? 90 PHE A CA 1 ATOM 304 C C . PHE A 1 49 ? 3.298 30.735 50.291 1.00 26.00 ? 90 PHE A C 1 ATOM 305 O O . PHE A 1 49 ? 3.039 31.215 51.410 1.00 25.47 ? 90 PHE A O 1 ATOM 306 C CB A PHE A 1 49 ? 1.890 31.101 48.219 0.65 27.18 ? 90 PHE A CB 1 ATOM 307 C CB B PHE A 1 49 ? 1.871 31.152 48.241 0.35 26.71 ? 90 PHE A CB 1 ATOM 308 C CG A PHE A 1 49 ? 0.560 31.174 48.943 0.65 29.28 ? 90 PHE A CG 1 ATOM 309 C CG B PHE A 1 49 ? 0.628 30.979 49.074 0.35 27.49 ? 90 PHE A CG 1 ATOM 310 C CD1 A PHE A 1 49 ? 0.277 32.160 49.889 0.65 29.42 ? 90 PHE A CD1 1 ATOM 311 C CD1 B PHE A 1 49 ? 0.039 32.059 49.721 0.35 27.20 ? 90 PHE A CD1 1 ATOM 312 C CD2 A PHE A 1 49 ? -0.453 30.287 48.587 0.65 32.42 ? 90 PHE A CD2 1 ATOM 313 C CD2 B PHE A 1 49 ? 0.017 29.740 49.154 0.35 29.29 ? 90 PHE A CD2 1 ATOM 314 C CE1 A PHE A 1 49 ? -0.990 32.226 50.507 0.65 30.22 ? 90 PHE A CE1 1 ATOM 315 C CE1 B PHE A 1 49 ? -1.122 31.898 50.461 0.35 27.40 ? 90 PHE A CE1 1 ATOM 316 C CE2 A PHE A 1 49 ? -1.717 30.347 49.202 0.65 33.41 ? 90 PHE A CE2 1 ATOM 317 C CE2 B PHE A 1 49 ? -1.142 29.576 49.878 0.35 29.65 ? 90 PHE A CE2 1 ATOM 318 C CZ A PHE A 1 49 ? -1.975 31.305 50.165 0.65 33.48 ? 90 PHE A CZ 1 ATOM 319 C CZ B PHE A 1 49 ? -1.713 30.653 50.540 0.35 29.28 ? 90 PHE A CZ 1 ATOM 320 N N . GLN A 1 50 ? 3.810 29.504 50.133 1.00 26.33 ? 91 GLN A N 1 ATOM 321 C CA A GLN A 1 50 ? 4.036 28.674 51.325 0.50 27.58 ? 91 GLN A CA 1 ATOM 322 C CA B GLN A 1 50 ? 4.078 28.646 51.293 0.50 27.68 ? 91 GLN A CA 1 ATOM 323 C C . GLN A 1 50 ? 5.039 29.331 52.280 1.00 26.77 ? 91 GLN A C 1 ATOM 324 O O . GLN A 1 50 ? 4.830 29.307 53.486 1.00 27.71 ? 91 GLN A O 1 ATOM 325 C CB A GLN A 1 50 ? 4.421 27.228 50.971 0.50 28.58 ? 91 GLN A CB 1 ATOM 326 C CB B GLN A 1 50 ? 4.564 27.257 50.827 0.50 28.57 ? 91 GLN A CB 1 ATOM 327 C CG A GLN A 1 50 ? 3.277 26.419 50.336 0.50 32.27 ? 91 GLN A CG 1 ATOM 328 C CG B GLN A 1 50 ? 3.436 26.487 50.114 0.50 32.89 ? 91 GLN A CG 1 ATOM 329 C CD A GLN A 1 50 ? 2.014 26.348 51.191 0.50 34.94 ? 91 GLN A CD 1 ATOM 330 C CD B GLN A 1 50 ? 3.867 25.188 49.446 0.50 36.02 ? 91 GLN A CD 1 ATOM 331 O OE1 A GLN A 1 50 ? 0.902 26.316 50.659 0.50 38.31 ? 91 GLN A OE1 1 ATOM 332 O OE1 B GLN A 1 50 ? 5.019 25.024 49.034 0.50 39.42 ? 91 GLN A OE1 1 ATOM 333 N NE2 A GLN A 1 50 ? 2.176 26.308 52.517 0.50 35.17 ? 91 GLN A NE2 1 ATOM 334 N NE2 B GLN A 1 50 ? 2.921 24.259 49.313 0.50 39.93 ? 91 GLN A NE2 1 ATOM 335 N N . LEU A 1 51 ? 6.091 29.970 51.743 1.00 24.94 ? 92 LEU A N 1 ATOM 336 C CA . LEU A 1 51 ? 7.037 30.661 52.628 1.00 24.98 ? 92 LEU A CA 1 ATOM 337 C C . LEU A 1 51 ? 6.366 31.843 53.319 1.00 23.48 ? 92 LEU A C 1 ATOM 338 O O . LEU A 1 51 ? 6.619 32.086 54.512 1.00 25.16 ? 92 LEU A O 1 ATOM 339 C CB . LEU A 1 51 ? 8.312 31.108 51.875 1.00 23.09 ? 92 LEU A CB 1 ATOM 340 C CG . LEU A 1 51 ? 9.422 31.747 52.701 1.00 23.73 ? 92 LEU A CG 1 ATOM 341 C CD1 . LEU A 1 51 ? 9.956 30.822 53.870 1.00 26.23 ? 92 LEU A CD1 1 ATOM 342 C CD2 . LEU A 1 51 ? 10.566 32.196 51.790 1.00 22.72 ? 92 LEU A CD2 1 ATOM 343 N N . ALA A 1 52 ? 5.538 32.589 52.586 1.00 23.07 ? 93 ALA A N 1 ATOM 344 C CA . ALA A 1 52 ? 4.790 33.683 53.225 1.00 23.10 ? 93 ALA A CA 1 ATOM 345 C C . ALA A 1 52 ? 3.968 33.195 54.418 1.00 23.75 ? 93 ALA A C 1 ATOM 346 O O . ALA A 1 52 ? 3.960 33.826 55.498 1.00 24.86 ? 93 ALA A O 1 ATOM 347 C CB . ALA A 1 52 ? 3.871 34.368 52.201 1.00 23.42 ? 93 ALA A CB 1 ATOM 348 N N . LYS A 1 53 ? 3.273 32.079 54.235 1.00 24.33 ? 94 LYS A N 1 ATOM 349 C CA . LYS A 1 53 ? 2.475 31.512 55.338 1.00 25.67 ? 94 LYS A CA 1 ATOM 350 C C . LYS A 1 53 ? 3.343 31.081 56.508 1.00 26.05 ? 94 LYS A C 1 ATOM 351 O O . LYS A 1 53 ? 2.967 31.258 57.671 1.00 27.08 ? 94 LYS A O 1 ATOM 352 C CB . LYS A 1 53 ? 1.597 30.364 54.798 1.00 27.67 ? 94 LYS A CB 1 ATOM 353 C CG . LYS A 1 53 ? 0.477 30.928 53.875 1.00 29.77 ? 94 LYS A CG 1 ATOM 354 C CD . LYS A 1 53 ? -0.576 29.878 53.542 1.00 40.14 ? 94 LYS A CD 1 ATOM 355 C CE . LYS A 1 53 ? 0.015 28.875 52.590 1.00 42.50 ? 94 LYS A CE 1 ATOM 356 N NZ . LYS A 1 53 ? -0.925 27.783 52.198 1.00 48.76 ? 94 LYS A NZ 1 ATOM 357 N N . GLN A 1 54 ? 4.527 30.534 56.213 1.00 26.06 ? 95 GLN A N 1 ATOM 358 C CA . GLN A 1 54 ? 5.464 30.136 57.282 1.00 26.69 ? 95 GLN A CA 1 ATOM 359 C C . GLN A 1 54 ? 5.915 31.354 58.089 1.00 26.46 ? 95 GLN A C 1 ATOM 360 O O . GLN A 1 54 ? 5.855 31.350 59.331 1.00 27.56 ? 95 GLN A O 1 ATOM 361 C CB . GLN A 1 54 ? 6.685 29.446 56.664 1.00 26.17 ? 95 GLN A CB 1 ATOM 362 C CG . GLN A 1 54 ? 7.690 29.045 57.748 1.00 27.41 ? 95 GLN A CG 1 ATOM 363 C CD . GLN A 1 54 ? 9.043 28.731 57.158 1.00 27.45 ? 95 GLN A CD 1 ATOM 364 O OE1 . GLN A 1 54 ? 9.145 27.991 56.164 1.00 28.44 ? 95 GLN A OE1 1 ATOM 365 N NE2 . GLN A 1 54 ? 10.087 29.285 57.756 1.00 27.56 ? 95 GLN A NE2 1 ATOM 366 N N . ILE A 1 55 ? 6.344 32.405 57.382 1.00 25.46 ? 96 ILE A N 1 ATOM 367 C CA . ILE A 1 55 ? 6.787 33.642 58.032 1.00 25.30 ? 96 ILE A CA 1 ATOM 368 C C . ILE A 1 55 ? 5.645 34.256 58.848 1.00 25.31 ? 96 ILE A C 1 ATOM 369 O O . ILE A 1 55 ? 5.846 34.672 60.009 1.00 25.44 ? 96 ILE A O 1 ATOM 370 C CB . ILE A 1 55 ? 7.318 34.652 56.976 1.00 24.71 ? 96 ILE A CB 1 ATOM 371 C CG1 A ILE A 1 55 ? 8.450 34.104 56.128 0.65 28.00 ? 96 ILE A CG1 1 ATOM 372 C CG1 B ILE A 1 55 ? 8.655 34.095 56.472 0.35 24.64 ? 96 ILE A CG1 1 ATOM 373 C CG2 . ILE A 1 55 ? 7.641 36.025 57.627 1.00 24.32 ? 96 ILE A CG2 1 ATOM 374 C CD1 A ILE A 1 55 ? 9.646 33.819 56.878 0.65 28.17 ? 96 ILE A CD1 1 ATOM 375 C CD1 B ILE A 1 55 ? 9.240 34.736 55.224 0.35 19.42 ? 96 ILE A CD1 1 ATOM 376 N N . GLN A 1 56 ? 4.452 34.293 58.263 1.00 24.97 ? 97 GLN A N 1 ATOM 377 C CA . GLN A 1 56 ? 3.288 34.787 59.024 1.00 25.99 ? 97 GLN A CA 1 ATOM 378 C C . GLN A 1 56 ? 3.123 33.999 60.323 1.00 27.16 ? 97 GLN A C 1 ATOM 379 O O . GLN A 1 56 ? 2.981 34.604 61.381 1.00 27.84 ? 97 GLN A O 1 ATOM 380 C CB . GLN A 1 56 ? 2.025 34.703 58.176 1.00 26.60 ? 97 GLN A CB 1 ATOM 381 C CG . GLN A 1 56 ? 0.717 35.077 58.928 1.00 28.63 ? 97 GLN A CG 1 ATOM 382 C CD . GLN A 1 56 ? -0.528 34.850 58.101 1.00 30.99 ? 97 GLN A CD 1 ATOM 383 O OE1 . GLN A 1 56 ? -0.599 33.955 57.236 1.00 30.01 ? 97 GLN A OE1 1 ATOM 384 N NE2 . GLN A 1 56 ? -1.535 35.677 58.357 1.00 29.13 ? 97 GLN A NE2 1 ATOM 385 N N . SER A 1 57 ? 3.155 32.673 60.244 1.00 28.41 ? 98 SER A N 1 ATOM 386 C CA . SER A 1 57 ? 2.969 31.866 61.445 1.00 29.12 ? 98 SER A CA 1 ATOM 387 C C . SER A 1 57 ? 4.092 32.110 62.479 1.00 28.59 ? 98 SER A C 1 ATOM 388 O O . SER A 1 57 ? 3.850 32.203 63.698 1.00 29.70 ? 98 SER A O 1 ATOM 389 C CB . SER A 1 57 ? 2.962 30.391 61.046 1.00 29.80 ? 98 SER A CB 1 ATOM 390 O OG A SER A 1 57 ? 2.789 29.601 62.193 0.50 29.63 ? 98 SER A OG 1 ATOM 391 O OG B SER A 1 57 ? 1.688 30.051 60.532 0.50 33.58 ? 98 SER A OG 1 ATOM 392 N N . GLN A 1 58 ? 5.329 32.181 61.990 1.00 27.41 ? 99 GLN A N 1 ATOM 393 C CA . GLN A 1 58 ? 6.463 32.395 62.875 1.00 27.68 ? 99 GLN A CA 1 ATOM 394 C C . GLN A 1 58 ? 6.460 33.773 63.531 1.00 26.97 ? 99 GLN A C 1 ATOM 395 O O . GLN A 1 58 ? 6.741 33.866 64.724 1.00 28.16 ? 99 GLN A O 1 ATOM 396 C CB . GLN A 1 58 ? 7.791 32.122 62.172 1.00 27.52 ? 99 GLN A CB 1 ATOM 397 C CG . GLN A 1 58 ? 7.998 30.642 61.921 1.00 29.56 ? 99 GLN A CG 1 ATOM 398 C CD . GLN A 1 58 ? 9.339 30.390 61.233 1.00 31.15 ? 99 GLN A CD 1 ATOM 399 O OE1 . GLN A 1 58 ? 9.594 30.913 60.164 1.00 32.07 ? 99 GLN A OE1 1 ATOM 400 N NE2 . GLN A 1 58 ? 10.197 29.609 61.873 1.00 39.50 ? 99 GLN A NE2 1 ATOM 401 N N . TRP A 1 59 ? 6.126 34.829 62.776 1.00 26.48 ? 100 TRP A N 1 ATOM 402 C CA . TRP A 1 59 ? 6.061 36.153 63.390 1.00 26.03 ? 100 TRP A CA 1 ATOM 403 C C . TRP A 1 59 ? 4.996 36.217 64.463 1.00 27.41 ? 100 TRP A C 1 ATOM 404 O O . TRP A 1 59 ? 5.174 36.907 65.453 1.00 28.97 ? 100 TRP A O 1 ATOM 405 C CB . TRP A 1 59 ? 5.799 37.226 62.324 1.00 24.21 ? 100 TRP A CB 1 ATOM 406 C CG . TRP A 1 59 ? 7.002 37.511 61.519 1.00 24.85 ? 100 TRP A CG 1 ATOM 407 C CD1 . TRP A 1 59 ? 8.225 36.874 61.562 1.00 25.71 ? 100 TRP A CD1 1 ATOM 408 C CD2 . TRP A 1 59 ? 7.096 38.485 60.474 1.00 23.82 ? 100 TRP A CD2 1 ATOM 409 N NE1 . TRP A 1 59 ? 9.083 37.443 60.638 1.00 24.44 ? 100 TRP A NE1 1 ATOM 410 C CE2 . TRP A 1 59 ? 8.414 38.432 59.961 1.00 22.58 ? 100 TRP A CE2 1 ATOM 411 C CE3 . TRP A 1 59 ? 6.188 39.426 59.944 1.00 22.37 ? 100 TRP A CE3 1 ATOM 412 C CZ2 . TRP A 1 59 ? 8.868 39.274 58.894 1.00 22.50 ? 100 TRP A CZ2 1 ATOM 413 C CZ3 . TRP A 1 59 ? 6.621 40.259 58.901 1.00 23.37 ? 100 TRP A CZ3 1 ATOM 414 C CH2 . TRP A 1 59 ? 7.952 40.181 58.387 1.00 22.64 ? 100 TRP A CH2 1 ATOM 415 N N . LYS A 1 60 ? 3.913 35.477 64.271 1.00 28.07 ? 101 LYS A N 1 ATOM 416 C CA . LYS A 1 60 ? 2.879 35.358 65.340 1.00 30.41 ? 101 LYS A CA 1 ATOM 417 C C . LYS A 1 60 ? 3.454 34.682 66.594 1.00 31.57 ? 101 LYS A C 1 ATOM 418 O O . LYS A 1 60 ? 3.267 35.201 67.724 1.00 33.16 ? 101 LYS A O 1 ATOM 419 C CB . LYS A 1 60 ? 1.638 34.595 64.851 1.00 30.95 ? 101 LYS A CB 1 ATOM 420 C CG . LYS A 1 60 ? 0.894 35.299 63.765 1.00 35.41 ? 101 LYS A CG 1 ATOM 421 C CD . LYS A 1 60 ? -0.389 34.571 63.395 1.00 43.86 ? 101 LYS A CD 1 ATOM 422 C CE . LYS A 1 60 ? -1.277 35.503 62.553 1.00 45.13 ? 101 LYS A CE 1 ATOM 423 N NZ . LYS A 1 60 ? -2.719 35.211 62.722 1.00 51.64 ? 101 LYS A NZ 1 ATOM 424 N N . GLU A 1 61 ? 4.137 33.547 66.402 1.00 31.74 ? 102 GLU A N 1 ATOM 425 C CA . GLU A 1 61 ? 4.757 32.781 67.507 1.00 33.56 ? 102 GLU A CA 1 ATOM 426 C C . GLU A 1 61 ? 5.788 33.687 68.201 1.00 32.54 ? 102 GLU A C 1 ATOM 427 O O . GLU A 1 61 ? 5.931 33.656 69.426 1.00 33.12 ? 102 GLU A O 1 ATOM 428 C CB . GLU A 1 61 ? 5.463 31.504 67.002 1.00 35.00 ? 102 GLU A CB 1 ATOM 429 C CG A GLU A 1 61 ? 4.754 30.531 66.006 0.50 37.33 ? 102 GLU A CG 1 ATOM 430 C CG B GLU A 1 61 ? 6.114 30.672 68.100 0.50 37.51 ? 102 GLU A CG 1 ATOM 431 C CD A GLU A 1 61 ? 5.723 29.589 65.169 0.50 40.36 ? 102 GLU A CD 1 ATOM 432 C CD B GLU A 1 61 ? 6.404 29.263 67.643 0.50 43.22 ? 102 GLU A CD 1 ATOM 433 O OE1 A GLU A 1 61 ? 6.927 29.407 65.506 0.50 39.25 ? 102 GLU A OE1 1 ATOM 434 O OE1 B GLU A 1 61 ? 5.936 28.887 66.540 0.50 45.84 ? 102 GLU A OE1 1 ATOM 435 O OE2 A GLU A 1 61 ? 5.273 29.018 64.136 0.50 40.40 ? 102 GLU A OE2 1 ATOM 436 O OE2 B GLU A 1 61 ? 7.090 28.528 68.387 0.50 46.76 ? 102 GLU A OE2 1 ATOM 437 N N . PHE A 1 62 ? 6.510 34.501 67.417 1.00 30.03 ? 103 PHE A N 1 ATOM 438 C CA . PHE A 1 62 ? 7.564 35.364 67.973 1.00 30.30 ? 103 PHE A CA 1 ATOM 439 C C . PHE A 1 62 ? 6.992 36.450 68.889 1.00 31.18 ? 103 PHE A C 1 ATOM 440 O O . PHE A 1 62 ? 7.712 37.012 69.703 1.00 32.84 ? 103 PHE A O 1 ATOM 441 C CB . PHE A 1 62 ? 8.387 36.057 66.855 1.00 28.95 ? 103 PHE A CB 1 ATOM 442 C CG . PHE A 1 62 ? 9.318 35.129 66.079 1.00 28.44 ? 103 PHE A CG 1 ATOM 443 C CD1 . PHE A 1 62 ? 9.657 33.840 66.535 1.00 33.28 ? 103 PHE A CD1 1 ATOM 444 C CD2 . PHE A 1 62 ? 9.856 35.577 64.867 1.00 28.33 ? 103 PHE A CD2 1 ATOM 445 C CE1 . PHE A 1 62 ? 10.512 33.005 65.767 1.00 34.35 ? 103 PHE A CE1 1 ATOM 446 C CE2 . PHE A 1 62 ? 10.727 34.743 64.104 1.00 28.65 ? 103 PHE A CE2 1 ATOM 447 C CZ . PHE A 1 62 ? 11.048 33.477 64.535 1.00 31.13 ? 103 PHE A CZ 1 ATOM 448 N N . GLY A 1 63 ? 5.719 36.774 68.712 1.00 30.38 ? 104 GLY A N 1 ATOM 449 C CA . GLY A 1 63 ? 5.034 37.674 69.639 1.00 30.74 ? 104 GLY A CA 1 ATOM 450 C C . GLY A 1 63 ? 4.360 38.904 69.064 1.00 30.22 ? 104 GLY A C 1 ATOM 451 O O . GLY A 1 63 ? 3.806 39.704 69.807 1.00 30.81 ? 104 GLY A O 1 ATOM 452 N N . LEU A 1 64 ? 4.388 39.090 67.744 1.00 28.23 ? 105 LEU A N 1 ATOM 453 C CA . LEU A 1 64 ? 3.727 40.278 67.182 1.00 28.01 ? 105 LEU A CA 1 ATOM 454 C C . LEU A 1 64 ? 2.238 40.309 67.439 1.00 28.87 ? 105 LEU A C 1 ATOM 455 O O . LEU A 1 64 ? 1.570 39.257 67.560 1.00 30.97 ? 105 LEU A O 1 ATOM 456 C CB . LEU A 1 64 ? 4.010 40.373 65.664 1.00 26.24 ? 105 LEU A CB 1 ATOM 457 C CG . LEU A 1 64 ? 5.489 40.488 65.309 1.00 26.80 ? 105 LEU A CG 1 ATOM 458 C CD1 . LEU A 1 64 ? 5.566 40.850 63.807 1.00 26.17 ? 105 LEU A CD1 1 ATOM 459 C CD2 . LEU A 1 64 ? 6.196 41.591 66.100 1.00 26.56 ? 105 LEU A CD2 1 ATOM 460 N N . ASP A 1 65 ? 1.700 41.521 67.536 1.00 28.89 ? 106 ASP A N 1 ATOM 461 C CA . ASP A 1 65 ? 0.289 41.705 67.904 1.00 31.01 ? 106 ASP A CA 1 ATOM 462 C C . ASP A 1 65 ? -0.660 41.219 66.808 1.00 31.69 ? 106 ASP A C 1 ATOM 463 O O . ASP A 1 65 ? -1.718 40.641 67.097 1.00 32.96 ? 106 ASP A O 1 ATOM 464 C CB . ASP A 1 65 ? 0.022 43.184 68.184 1.00 29.43 ? 106 ASP A CB 1 ATOM 465 C CG . ASP A 1 65 ? 0.704 43.654 69.447 1.00 31.76 ? 106 ASP A CG 1 ATOM 466 O OD1 . ASP A 1 65 ? 0.439 43.020 70.499 1.00 33.99 ? 106 ASP A OD1 1 ATOM 467 O OD2 . ASP A 1 65 ? 1.534 44.593 69.399 1.00 30.51 ? 106 ASP A OD2 1 ATOM 468 N N . SER A 1 66 ? -0.294 41.490 65.556 1.00 29.60 ? 107 SER A N 1 ATOM 469 C CA . SER A 1 66 ? -1.101 41.044 64.438 1.00 28.67 ? 107 SER A CA 1 ATOM 470 C C . SER A 1 66 ? -0.126 40.714 63.298 1.00 26.77 ? 107 SER A C 1 ATOM 471 O O . SER A 1 66 ? 0.908 41.371 63.146 1.00 25.11 ? 107 SER A O 1 ATOM 472 C CB . SER A 1 66 ? -2.114 42.162 64.049 1.00 28.85 ? 107 SER A CB 1 ATOM 473 O OG A SER A 1 66 ? -1.510 43.323 63.505 0.50 26.40 ? 107 SER A OG 1 ATOM 474 O OG B SER A 1 66 ? -2.282 42.323 62.657 0.50 31.13 ? 107 SER A OG 1 ATOM 475 N N . VAL A 1 67 ? -0.466 39.701 62.518 1.00 26.51 ? 108 VAL A N 1 ATOM 476 C CA . VAL A 1 67 ? 0.352 39.387 61.324 1.00 25.73 ? 108 VAL A CA 1 ATOM 477 C C . VAL A 1 67 ? -0.582 38.946 60.205 1.00 26.64 ? 108 VAL A C 1 ATOM 478 O O . VAL A 1 67 ? -1.256 37.893 60.327 1.00 28.68 ? 108 VAL A O 1 ATOM 479 C CB . VAL A 1 67 ? 1.419 38.277 61.544 1.00 26.25 ? 108 VAL A CB 1 ATOM 480 C CG1 . VAL A 1 67 ? 2.353 38.288 60.332 1.00 25.24 ? 108 VAL A CG1 1 ATOM 481 C CG2 . VAL A 1 67 ? 2.257 38.521 62.819 1.00 26.57 ? 108 VAL A CG2 1 ATOM 482 N N . GLU A 1 68 ? -0.622 39.731 59.131 1.00 25.77 ? 109 GLU A N 1 ATOM 483 C CA . GLU A 1 68 ? -1.576 39.468 58.086 1.00 27.29 ? 109 GLU A CA 1 ATOM 484 C C . GLU A 1 68 ? -0.888 39.319 56.745 1.00 26.06 ? 109 GLU A C 1 ATOM 485 O O . GLU A 1 68 ? 0.220 39.823 56.543 1.00 27.15 ? 109 GLU A O 1 ATOM 486 C CB . GLU A 1 68 ? -2.567 40.640 57.962 1.00 29.19 ? 109 GLU A CB 1 ATOM 487 C CG . GLU A 1 68 ? -3.458 40.831 59.234 1.00 35.15 ? 109 GLU A CG 1 ATOM 488 C CD . GLU A 1 68 ? -4.319 39.612 59.575 1.00 45.61 ? 109 GLU A CD 1 ATOM 489 O OE1 . GLU A 1 68 ? -4.840 38.941 58.644 1.00 48.59 ? 109 GLU A OE1 1 ATOM 490 O OE2 . GLU A 1 68 ? -4.497 39.328 60.796 1.00 50.26 ? 109 GLU A OE2 1 ATOM 491 N N . LEU A 1 69 ? -1.556 38.635 55.825 1.00 25.36 ? 110 LEU A N 1 ATOM 492 C CA . LEU A 1 69 ? -1.095 38.697 54.426 1.00 24.56 ? 110 LEU A CA 1 ATOM 493 C C . LEU A 1 69 ? -1.872 39.766 53.668 1.00 25.14 ? 110 LEU A C 1 ATOM 494 O O . LEU A 1 69 ? -3.113 39.842 53.799 1.00 27.54 ? 110 LEU A O 1 ATOM 495 C CB . LEU A 1 69 ? -1.281 37.365 53.718 1.00 26.17 ? 110 LEU A CB 1 ATOM 496 C CG . LEU A 1 69 ? -0.600 36.133 54.310 1.00 27.16 ? 110 LEU A CG 1 ATOM 497 C CD1 . LEU A 1 69 ? -0.824 34.979 53.345 1.00 32.70 ? 110 LEU A CD1 1 ATOM 498 C CD2 . LEU A 1 69 ? 0.881 36.343 54.511 1.00 28.06 ? 110 LEU A CD2 1 ATOM 499 N N . ALA A 1 70 ? -1.161 40.580 52.890 1.00 23.32 ? 111 ALA A N 1 ATOM 500 C CA . ALA A 1 70 ? -1.790 41.587 52.058 1.00 22.62 ? 111 ALA A CA 1 ATOM 501 C C . ALA A 1 70 ? -1.494 41.121 50.639 1.00 22.67 ? 111 ALA A C 1 ATOM 502 O O . ALA A 1 70 ? -0.303 41.101 50.230 1.00 25.20 ? 111 ALA A O 1 ATOM 503 C CB . ALA A 1 70 ? -1.175 42.975 52.304 1.00 23.69 ? 111 ALA A CB 1 ATOM 504 N N . HIS A 1 71 ? -2.544 40.765 49.899 1.00 23.43 ? 112 HIS A N 1 ATOM 505 C CA . HIS A 1 71 ? -2.295 40.221 48.546 1.00 23.03 ? 112 HIS A CA 1 ATOM 506 C C . HIS A 1 71 ? -2.773 41.181 47.459 1.00 21.97 ? 112 HIS A C 1 ATOM 507 O O . HIS A 1 71 ? -3.641 42.017 47.698 1.00 23.50 ? 112 HIS A O 1 ATOM 508 C CB . HIS A 1 71 ? -2.944 38.847 48.357 1.00 24.11 ? 112 HIS A CB 1 ATOM 509 C CG . HIS A 1 71 ? -4.437 38.878 48.385 1.00 27.41 ? 112 HIS A CG 1 ATOM 510 N ND1 . HIS A 1 71 ? -5.172 38.657 49.538 1.00 32.35 ? 112 HIS A ND1 1 ATOM 511 C CD2 . HIS A 1 71 ? -5.340 39.097 47.401 1.00 28.87 ? 112 HIS A CD2 1 ATOM 512 C CE1 . HIS A 1 71 ? -6.462 38.742 49.259 1.00 33.00 ? 112 HIS A CE1 1 ATOM 513 N NE2 . HIS A 1 71 ? -6.593 38.991 47.965 1.00 33.28 ? 112 HIS A NE2 1 ATOM 514 N N . TYR A 1 72 ? -2.193 41.045 46.256 1.00 21.53 ? 113 TYR A N 1 ATOM 515 C CA . TYR A 1 72 ? -2.487 41.900 45.104 1.00 21.56 ? 113 TYR A CA 1 ATOM 516 C C . TYR A 1 72 ? -2.347 41.032 43.893 1.00 21.64 ? 113 TYR A C 1 ATOM 517 O O . TYR A 1 72 ? -1.624 40.037 43.940 1.00 22.60 ? 113 TYR A O 1 ATOM 518 C CB . TYR A 1 72 ? -1.457 43.083 44.968 1.00 20.19 ? 113 TYR A CB 1 ATOM 519 C CG . TYR A 1 72 ? -1.443 43.901 46.247 1.00 19.17 ? 113 TYR A CG 1 ATOM 520 C CD1 . TYR A 1 72 ? -2.393 44.880 46.459 1.00 18.26 ? 113 TYR A CD1 1 ATOM 521 C CD2 . TYR A 1 72 ? -0.555 43.590 47.267 1.00 22.30 ? 113 TYR A CD2 1 ATOM 522 C CE1 . TYR A 1 72 ? -2.440 45.574 47.674 1.00 22.88 ? 113 TYR A CE1 1 ATOM 523 C CE2 . TYR A 1 72 ? -0.571 44.271 48.449 1.00 22.50 ? 113 TYR A CE2 1 ATOM 524 C CZ . TYR A 1 72 ? -1.529 45.236 48.655 1.00 22.77 ? 113 TYR A CZ 1 ATOM 525 O OH . TYR A 1 72 ? -1.561 45.909 49.889 1.00 23.83 ? 113 TYR A OH 1 ATOM 526 N N . ASP A 1 73 ? -2.981 41.427 42.799 1.00 21.60 ? 114 ASP A N 1 ATOM 527 C CA . ASP A 1 73 ? -2.860 40.664 41.546 1.00 21.94 ? 114 ASP A CA 1 ATOM 528 C C . ASP A 1 73 ? -2.193 41.581 40.552 1.00 21.34 ? 114 ASP A C 1 ATOM 529 O O . ASP A 1 73 ? -2.811 42.534 40.067 1.00 20.76 ? 114 ASP A O 1 ATOM 530 C CB . ASP A 1 73 ? -4.264 40.232 41.033 1.00 24.08 ? 114 ASP A CB 1 ATOM 531 C CG . ASP A 1 73 ? -4.951 39.294 42.001 1.00 27.67 ? 114 ASP A CG 1 ATOM 532 O OD1 . ASP A 1 73 ? -4.325 38.282 42.344 1.00 28.73 ? 114 ASP A OD1 1 ATOM 533 O OD2 . ASP A 1 73 ? -6.094 39.575 42.404 1.00 32.58 ? 114 ASP A OD2 1 ATOM 534 N N . VAL A 1 74 ? -0.927 41.264 40.240 1.00 20.57 ? 115 VAL A N 1 ATOM 535 C CA . VAL A 1 74 ? -0.059 42.161 39.469 1.00 20.13 ? 115 VAL A CA 1 ATOM 536 C C . VAL A 1 74 ? 0.495 41.471 38.242 1.00 21.22 ? 115 VAL A C 1 ATOM 537 O O . VAL A 1 74 ? 0.596 40.225 38.221 1.00 21.84 ? 115 VAL A O 1 ATOM 538 C CB . VAL A 1 74 ? 1.136 42.671 40.343 1.00 19.69 ? 115 VAL A CB 1 ATOM 539 C CG1 . VAL A 1 74 ? 0.564 43.422 41.568 1.00 18.92 ? 115 VAL A CG1 1 ATOM 540 C CG2 . VAL A 1 74 ? 2.116 41.532 40.775 1.00 19.27 ? 115 VAL A CG2 1 ATOM 541 N N . LEU A 1 75 ? 0.965 42.277 37.286 1.00 21.10 ? 116 LEU A N 1 ATOM 542 C CA . LEU A 1 75 ? 1.565 41.685 36.089 1.00 20.95 ? 116 LEU A CA 1 ATOM 543 C C . LEU A 1 75 ? 2.966 41.109 36.411 1.00 20.67 ? 116 LEU A C 1 ATOM 544 O O . LEU A 1 75 ? 3.862 41.860 36.852 1.00 21.98 ? 116 LEU A O 1 ATOM 545 C CB . LEU A 1 75 ? 1.674 42.761 35.008 1.00 20.32 ? 116 LEU A CB 1 ATOM 546 C CG . LEU A 1 75 ? 2.007 42.173 33.627 1.00 22.31 ? 116 LEU A CG 1 ATOM 547 C CD1 . LEU A 1 75 ? 0.760 41.430 33.112 1.00 24.58 ? 116 LEU A CD1 1 ATOM 548 C CD2 . LEU A 1 75 ? 2.383 43.304 32.673 1.00 24.73 ? 116 LEU A CD2 1 ATOM 549 N N . LEU A 1 76 ? 3.133 39.802 36.166 1.00 21.65 ? 117 LEU A N 1 ATOM 550 C CA . LEU A 1 76 ? 4.463 39.139 36.296 1.00 21.66 ? 117 LEU A CA 1 ATOM 551 C C . LEU A 1 76 ? 4.856 38.592 34.922 1.00 22.95 ? 117 LEU A C 1 ATOM 552 O O . LEU A 1 76 ? 4.106 38.736 33.978 1.00 24.08 ? 117 LEU A O 1 ATOM 553 C CB . LEU A 1 76 ? 4.449 38.051 37.374 1.00 21.35 ? 117 LEU A CB 1 ATOM 554 C CG . LEU A 1 76 ? 4.122 38.502 38.809 1.00 21.98 ? 117 LEU A CG 1 ATOM 555 C CD1 . LEU A 1 76 ? 4.337 37.304 39.793 1.00 21.01 ? 117 LEU A CD1 1 ATOM 556 C CD2 . LEU A 1 76 ? 5.061 39.691 39.238 1.00 22.22 ? 117 LEU A CD2 1 ATOM 557 N N . SER A 1 77 ? 6.043 38.020 34.812 1.00 22.52 ? 118 SER A N 1 ATOM 558 C CA . SER A 1 77 ? 6.566 37.559 33.506 1.00 23.69 ? 118 SER A CA 1 ATOM 559 C C . SER A 1 77 ? 7.318 36.268 33.731 1.00 24.87 ? 118 SER A C 1 ATOM 560 O O . SER A 1 77 ? 8.113 36.150 34.680 1.00 24.07 ? 118 SER A O 1 ATOM 561 C CB . SER A 1 77 ? 7.505 38.639 32.912 1.00 25.22 ? 118 SER A CB 1 ATOM 562 O OG . SER A 1 77 ? 8.297 38.134 31.827 1.00 26.06 ? 118 SER A OG 1 ATOM 563 N N . TYR A 1 78 ? 7.077 35.271 32.876 1.00 25.22 ? 119 TYR A N 1 ATOM 564 C CA . TYR A 1 78 ? 7.770 34.001 33.042 1.00 25.33 ? 119 TYR A CA 1 ATOM 565 C C . TYR A 1 78 ? 8.105 33.405 31.698 1.00 26.46 ? 119 TYR A C 1 ATOM 566 O O . TYR A 1 78 ? 7.328 33.546 30.755 1.00 28.30 ? 119 TYR A O 1 ATOM 567 C CB . TYR A 1 78 ? 6.846 32.981 33.695 1.00 24.90 ? 119 TYR A CB 1 ATOM 568 C CG . TYR A 1 78 ? 6.333 33.328 35.061 1.00 25.96 ? 119 TYR A CG 1 ATOM 569 C CD1 . TYR A 1 78 ? 7.165 33.265 36.169 1.00 25.55 ? 119 TYR A CD1 1 ATOM 570 C CD2 . TYR A 1 78 ? 4.998 33.691 35.225 1.00 27.60 ? 119 TYR A CD2 1 ATOM 571 C CE1 . TYR A 1 78 ? 6.670 33.602 37.458 1.00 24.54 ? 119 TYR A CE1 1 ATOM 572 C CE2 . TYR A 1 78 ? 4.486 33.994 36.494 1.00 29.04 ? 119 TYR A CE2 1 ATOM 573 C CZ . TYR A 1 78 ? 5.339 33.911 37.591 1.00 27.22 ? 119 TYR A CZ 1 ATOM 574 O OH . TYR A 1 78 ? 4.829 34.185 38.845 1.00 26.50 ? 119 TYR A OH 1 ATOM 575 N N . PRO A 1 79 ? 9.214 32.662 31.626 1.00 27.67 ? 120 PRO A N 1 ATOM 576 C CA . PRO A 1 79 ? 9.428 31.919 30.368 1.00 27.96 ? 120 PRO A CA 1 ATOM 577 C C . PRO A 1 79 ? 8.357 30.867 30.132 1.00 30.98 ? 120 PRO A C 1 ATOM 578 O O . PRO A 1 79 ? 7.670 30.395 31.062 1.00 30.28 ? 120 PRO A O 1 ATOM 579 C CB . PRO A 1 79 ? 10.789 31.204 30.587 1.00 29.62 ? 120 PRO A CB 1 ATOM 580 C CG . PRO A 1 79 ? 11.419 31.910 31.766 1.00 27.72 ? 120 PRO A CG 1 ATOM 581 C CD . PRO A 1 79 ? 10.274 32.400 32.616 1.00 25.87 ? 120 PRO A CD 1 ATOM 582 N N . ASN A 1 80 ? 8.231 30.472 28.862 1.00 31.68 ? 121 ASN A N 1 ATOM 583 C CA . ASN A 1 80 ? 7.347 29.376 28.513 1.00 36.12 ? 121 ASN A CA 1 ATOM 584 C C . ASN A 1 80 ? 8.095 28.048 28.744 1.00 37.41 ? 121 ASN A C 1 ATOM 585 O O . ASN A 1 80 ? 9.150 27.822 28.151 1.00 37.68 ? 121 ASN A O 1 ATOM 586 C CB . ASN A 1 80 ? 6.945 29.540 27.056 1.00 36.43 ? 121 ASN A CB 1 ATOM 587 C CG . ASN A 1 80 ? 5.918 28.518 26.606 1.00 40.67 ? 121 ASN A CG 1 ATOM 588 O OD1 . ASN A 1 80 ? 5.935 27.374 27.042 1.00 43.20 ? 121 ASN A OD1 1 ATOM 589 N ND2 . ASN A 1 80 ? 5.019 28.932 25.740 1.00 45.79 ? 121 ASN A ND2 1 ATOM 590 N N . LYS A 1 81 ? 7.570 27.213 29.643 1.00 39.67 ? 122 LYS A N 1 ATOM 591 C CA . LYS A 1 81 ? 8.179 25.910 29.997 1.00 42.30 ? 122 LYS A CA 1 ATOM 592 C C . LYS A 1 81 ? 8.363 24.943 28.832 1.00 43.69 ? 122 LYS A C 1 ATOM 593 O O . LYS A 1 81 ? 9.283 24.114 28.848 1.00 44.21 ? 122 LYS A O 1 ATOM 594 C CB . LYS A 1 81 ? 7.368 25.208 31.087 1.00 43.09 ? 122 LYS A CB 1 ATOM 595 C CG . LYS A 1 81 ? 7.659 25.719 32.484 1.00 46.42 ? 122 LYS A CG 1 ATOM 596 C CD . LYS A 1 81 ? 6.543 25.336 33.462 1.00 51.85 ? 122 LYS A CD 1 ATOM 597 C CE . LYS A 1 81 ? 6.517 26.294 34.657 1.00 54.81 ? 122 LYS A CE 1 ATOM 598 N NZ . LYS A 1 81 ? 5.144 26.402 35.253 1.00 58.13 ? 122 LYS A NZ 1 ATOM 599 N N . THR A 1 82 ? 7.511 25.056 27.820 1.00 44.66 ? 123 THR A N 1 ATOM 600 C CA . THR A 1 82 ? 7.578 24.129 26.679 1.00 46.59 ? 123 THR A CA 1 ATOM 601 C C . THR A 1 82 ? 8.099 24.760 25.365 1.00 46.85 ? 123 THR A C 1 ATOM 602 O O . THR A 1 82 ? 8.093 24.140 24.302 1.00 47.95 ? 123 THR A O 1 ATOM 603 C CB . THR A 1 82 ? 6.221 23.383 26.474 1.00 47.90 ? 123 THR A CB 1 ATOM 604 O OG1 . THR A 1 82 ? 5.216 24.306 26.032 1.00 49.26 ? 123 THR A OG1 1 ATOM 605 C CG2 . THR A 1 82 ? 5.756 22.730 27.788 1.00 47.45 ? 123 THR A CG2 1 ATOM 606 N N . HIS A 1 83 ? 8.602 25.978 25.460 1.00 45.59 ? 124 HIS A N 1 ATOM 607 C CA . HIS A 1 83 ? 9.075 26.735 24.320 1.00 45.59 ? 124 HIS A CA 1 ATOM 608 C C . HIS A 1 83 ? 10.189 27.660 24.843 1.00 43.32 ? 124 HIS A C 1 ATOM 609 O O . HIS A 1 83 ? 9.976 28.853 24.987 1.00 42.09 ? 124 HIS A O 1 ATOM 610 C CB . HIS A 1 83 ? 7.913 27.558 23.777 1.00 46.66 ? 124 HIS A CB 1 ATOM 611 C CG . HIS A 1 83 ? 8.094 28.037 22.370 1.00 51.89 ? 124 HIS A CG 1 ATOM 612 N ND1 . HIS A 1 83 ? 9.028 27.502 21.509 1.00 57.61 ? 124 HIS A ND1 1 ATOM 613 C CD2 . HIS A 1 83 ? 7.423 28.978 21.661 1.00 55.11 ? 124 HIS A CD2 1 ATOM 614 C CE1 . HIS A 1 83 ? 8.939 28.104 20.334 1.00 58.94 ? 124 HIS A CE1 1 ATOM 615 N NE2 . HIS A 1 83 ? 7.974 29.006 20.400 1.00 58.43 ? 124 HIS A NE2 1 ATOM 616 N N . PRO A 1 84 ? 11.372 27.089 25.128 1.00 42.04 ? 125 PRO A N 1 ATOM 617 C CA . PRO A 1 84 ? 12.441 27.819 25.827 1.00 40.54 ? 125 PRO A CA 1 ATOM 618 C C . PRO A 1 84 ? 13.084 28.950 25.030 1.00 39.72 ? 125 PRO A C 1 ATOM 619 O O . PRO A 1 84 ? 13.121 28.930 23.789 1.00 40.30 ? 125 PRO A O 1 ATOM 620 C CB . PRO A 1 84 ? 13.456 26.722 26.177 1.00 41.71 ? 125 PRO A CB 1 ATOM 621 C CG . PRO A 1 84 ? 13.163 25.617 25.201 1.00 42.32 ? 125 PRO A CG 1 ATOM 622 C CD . PRO A 1 84 ? 11.696 25.656 24.981 1.00 43.03 ? 125 PRO A CD 1 ATOM 623 N N . ASN A 1 85 ? 13.551 29.954 25.771 1.00 35.93 ? 126 ASN A N 1 ATOM 624 C CA . ASN A 1 85 ? 14.250 31.115 25.196 1.00 35.33 ? 126 ASN A CA 1 ATOM 625 C C . ASN A 1 85 ? 15.679 30.756 24.832 1.00 35.54 ? 126 ASN A C 1 ATOM 626 O O . ASN A 1 85 ? 16.347 30.058 25.609 1.00 35.48 ? 126 ASN A O 1 ATOM 627 C CB . ASN A 1 85 ? 14.259 32.288 26.210 1.00 32.30 ? 126 ASN A CB 1 ATOM 628 C CG . ASN A 1 85 ? 12.866 32.774 26.544 1.00 34.15 ? 126 ASN A CG 1 ATOM 629 O OD1 . ASN A 1 85 ? 11.979 32.813 25.692 1.00 33.50 ? 126 ASN A OD1 1 ATOM 630 N ND2 . ASN A 1 85 ? 12.658 33.159 27.807 1.00 30.73 ? 126 ASN A ND2 1 ATOM 631 N N . TYR A 1 86 ? 16.131 31.160 23.634 1.00 37.17 ? 127 TYR A N 1 ATOM 632 C CA . TYR A 1 86 ? 17.569 31.026 23.298 1.00 37.74 ? 127 TYR A CA 1 ATOM 633 C C . TYR A 1 86 ? 18.006 31.958 22.173 1.00 38.37 ? 127 TYR A C 1 ATOM 634 O O . TYR A 1 86 ? 17.166 32.610 21.543 1.00 37.24 ? 127 TYR A O 1 ATOM 635 C CB . TYR A 1 86 ? 17.956 29.577 22.988 1.00 39.31 ? 127 TYR A CB 1 ATOM 636 C CG . TYR A 1 86 ? 17.417 29.063 21.673 1.00 40.80 ? 127 TYR A CG 1 ATOM 637 C CD1 . TYR A 1 86 ? 18.259 28.881 20.571 1.00 42.58 ? 127 TYR A CD1 1 ATOM 638 C CD2 . TYR A 1 86 ? 16.066 28.759 21.526 1.00 41.88 ? 127 TYR A CD2 1 ATOM 639 C CE1 . TYR A 1 86 ? 17.763 28.394 19.364 1.00 43.96 ? 127 TYR A CE1 1 ATOM 640 C CE2 . TYR A 1 86 ? 15.561 28.287 20.315 1.00 43.48 ? 127 TYR A CE2 1 ATOM 641 C CZ . TYR A 1 86 ? 16.418 28.105 19.247 1.00 45.14 ? 127 TYR A CZ 1 ATOM 642 O OH . TYR A 1 86 ? 15.905 27.638 18.063 1.00 45.60 ? 127 TYR A OH 1 ATOM 643 N N . ILE A 1 87 ? 19.326 32.051 21.965 1.00 37.78 ? 128 ILE A N 1 ATOM 644 C CA . ILE A 1 87 ? 19.878 32.904 20.919 1.00 36.90 ? 128 ILE A CA 1 ATOM 645 C C . ILE A 1 87 ? 20.679 31.979 20.020 1.00 38.51 ? 128 ILE A C 1 ATOM 646 O O . ILE A 1 87 ? 21.305 31.019 20.500 1.00 37.36 ? 128 ILE A O 1 ATOM 647 C CB . ILE A 1 87 ? 20.781 34.052 21.482 1.00 36.70 ? 128 ILE A CB 1 ATOM 648 C CG1 . ILE A 1 87 ? 19.952 34.987 22.404 1.00 34.84 ? 128 ILE A CG1 1 ATOM 649 C CG2 . ILE A 1 87 ? 21.419 34.871 20.335 1.00 39.11 ? 128 ILE A CG2 1 ATOM 650 C CD1 . ILE A 1 87 ? 20.799 35.770 23.400 1.00 37.04 ? 128 ILE A CD1 1 ATOM 651 N N . SER A 1 88 ? 20.618 32.263 18.724 1.00 39.73 ? 129 SER A N 1 ATOM 652 C CA . SER A 1 88 ? 21.428 31.534 17.740 1.00 41.21 ? 129 SER A CA 1 ATOM 653 C C . SER A 1 88 ? 22.326 32.420 16.900 1.00 42.15 ? 129 SER A C 1 ATOM 654 O O . SER A 1 88 ? 22.027 33.588 16.652 1.00 41.36 ? 129 SER A O 1 ATOM 655 C CB . SER A 1 88 ? 20.533 30.747 16.773 1.00 42.90 ? 129 SER A CB 1 ATOM 656 O OG . SER A 1 88 ? 19.831 29.720 17.451 1.00 45.41 ? 129 SER A OG 1 ATOM 657 N N . ILE A 1 89 ? 23.423 31.831 16.416 1.00 43.82 ? 130 ILE A N 1 ATOM 658 C CA . ILE A 1 89 ? 24.059 32.348 15.205 1.00 45.48 ? 130 ILE A CA 1 ATOM 659 C C . ILE A 1 89 ? 23.460 31.527 14.067 1.00 47.70 ? 130 ILE A C 1 ATOM 660 O O . ILE A 1 89 ? 23.405 30.291 14.127 1.00 46.39 ? 130 ILE A O 1 ATOM 661 C CB . ILE A 1 89 ? 25.604 32.254 15.211 1.00 45.87 ? 130 ILE A CB 1 ATOM 662 C CG1 . ILE A 1 89 ? 26.217 33.193 16.262 1.00 46.34 ? 130 ILE A CG1 1 ATOM 663 C CG2 . ILE A 1 89 ? 26.171 32.527 13.772 1.00 47.04 ? 130 ILE A CG2 1 ATOM 664 C CD1 . ILE A 1 89 ? 27.721 33.013 16.439 1.00 49.80 ? 130 ILE A CD1 1 ATOM 665 N N . ILE A 1 90 ? 22.960 32.245 13.068 1.00 49.92 ? 131 ILE A N 1 ATOM 666 C CA . ILE A 1 90 ? 22.277 31.625 11.930 1.00 53.64 ? 131 ILE A CA 1 ATOM 667 C C . ILE A 1 90 ? 23.058 31.904 10.635 1.00 56.25 ? 131 ILE A C 1 ATOM 668 O O . ILE A 1 90 ? 23.457 33.044 10.364 1.00 56.41 ? 131 ILE A O 1 ATOM 669 C CB . ILE A 1 90 ? 20.764 32.075 11.903 1.00 53.69 ? 131 ILE A CB 1 ATOM 670 C CG1 . ILE A 1 90 ? 19.897 31.095 11.104 1.00 56.00 ? 131 ILE A CG1 1 ATOM 671 C CG2 . ILE A 1 90 ? 20.603 33.554 11.485 1.00 54.15 ? 131 ILE A CG2 1 ATOM 672 C CD1 . ILE A 1 90 ? 18.381 31.365 11.238 1.00 56.45 ? 131 ILE A CD1 1 ATOM 673 N N . ASN A 1 91 ? 23.323 30.850 9.870 1.00 58.62 ? 132 ASN A N 1 ATOM 674 C CA . ASN A 1 91 ? 24.006 31.010 8.574 1.00 62.18 ? 132 ASN A CA 1 ATOM 675 C C . ASN A 1 91 ? 23.019 31.381 7.462 1.00 64.07 ? 132 ASN A C 1 ATOM 676 O O . ASN A 1 91 ? 21.810 31.439 7.690 1.00 63.39 ? 132 ASN A O 1 ATOM 677 C CB . ASN A 1 91 ? 24.883 29.786 8.223 1.00 63.25 ? 132 ASN A CB 1 ATOM 678 C CG . ASN A 1 91 ? 24.074 28.558 7.789 1.00 64.10 ? 132 ASN A CG 1 ATOM 679 O OD1 . ASN A 1 91 ? 22.893 28.653 7.443 1.00 64.51 ? 132 ASN A OD1 1 ATOM 680 N ND2 . ASN A 1 91 ? 24.725 27.391 7.810 1.00 63.47 ? 132 ASN A ND2 1 ATOM 681 N N . GLU A 1 92 ? 23.528 31.615 6.257 1.00 67.13 ? 133 GLU A N 1 ATOM 682 C CA . GLU A 1 92 ? 22.688 32.080 5.154 1.00 69.77 ? 133 GLU A CA 1 ATOM 683 C C . GLU A 1 92 ? 21.584 31.086 4.734 1.00 70.58 ? 133 GLU A C 1 ATOM 684 O O . GLU A 1 92 ? 20.568 31.484 4.154 1.00 71.28 ? 133 GLU A O 1 ATOM 685 C CB . GLU A 1 92 ? 23.579 32.406 3.965 1.00 71.64 ? 133 GLU A CB 1 ATOM 686 C CG . GLU A 1 92 ? 23.035 33.460 3.027 1.00 74.54 ? 133 GLU A CG 1 ATOM 687 C CD . GLU A 1 92 ? 23.933 33.624 1.814 1.00 78.52 ? 133 GLU A CD 1 ATOM 688 O OE1 . GLU A 1 92 ? 25.167 33.743 2.011 1.00 80.12 ? 133 GLU A OE1 1 ATOM 689 O OE2 . GLU A 1 92 ? 23.413 33.617 0.674 1.00 80.74 ? 133 GLU A OE2 1 ATOM 690 N N . ASP A 1 93 ? 21.790 29.804 5.037 1.00 70.94 ? 134 ASP A N 1 ATOM 691 C CA . ASP A 1 93 ? 20.823 28.748 4.719 1.00 71.76 ? 134 ASP A CA 1 ATOM 692 C C . ASP A 1 93 ? 19.688 28.640 5.742 1.00 70.21 ? 134 ASP A C 1 ATOM 693 O O . ASP A 1 93 ? 18.765 27.844 5.569 1.00 71.22 ? 134 ASP A O 1 ATOM 694 C CB . ASP A 1 93 ? 21.542 27.399 4.584 1.00 72.81 ? 134 ASP A CB 1 ATOM 695 C CG . ASP A 1 93 ? 22.527 27.373 3.421 1.00 75.76 ? 134 ASP A CG 1 ATOM 696 O OD1 . ASP A 1 93 ? 22.375 28.195 2.489 1.00 78.00 ? 134 ASP A OD1 1 ATOM 697 O OD2 . ASP A 1 93 ? 23.454 26.529 3.431 1.00 77.72 ? 134 ASP A OD2 1 ATOM 698 N N . GLY A 1 94 ? 19.760 29.438 6.804 1.00 67.81 ? 135 GLY A N 1 ATOM 699 C CA . GLY A 1 94 ? 18.785 29.373 7.885 1.00 65.56 ? 135 GLY A CA 1 ATOM 700 C C . GLY A 1 94 ? 19.097 28.282 8.896 1.00 63.82 ? 135 GLY A C 1 ATOM 701 O O . GLY A 1 94 ? 18.230 27.906 9.699 1.00 63.98 ? 135 GLY A O 1 ATOM 702 N N . ASN A 1 95 ? 20.331 27.777 8.866 1.00 62.65 ? 136 ASN A N 1 ATOM 703 C CA . ASN A 1 95 ? 20.788 26.800 9.849 1.00 60.49 ? 136 ASN A CA 1 ATOM 704 C C . ASN A 1 95 ? 21.294 27.532 11.074 1.00 57.18 ? 136 ASN A C 1 ATOM 705 O O . ASN A 1 95 ? 22.087 28.476 10.961 1.00 55.99 ? 136 ASN A O 1 ATOM 706 C CB . ASN A 1 95 ? 21.913 25.919 9.304 1.00 62.00 ? 136 ASN A CB 1 ATOM 707 C CG . ASN A 1 95 ? 21.534 25.191 8.026 1.00 65.16 ? 136 ASN A CG 1 ATOM 708 O OD1 . ASN A 1 95 ? 22.368 25.002 7.141 1.00 67.82 ? 136 ASN A OD1 1 ATOM 709 N ND2 . ASN A 1 95 ? 20.278 24.772 7.926 1.00 68.13 ? 136 ASN A ND2 1 ATOM 710 N N . GLU A 1 96 ? 20.824 27.100 12.239 1.00 55.44 ? 137 GLU A N 1 ATOM 711 C CA . GLU A 1 96 ? 21.296 27.654 13.506 1.00 51.81 ? 137 GLU A CA 1 ATOM 712 C C . GLU A 1 96 ? 22.507 26.834 13.929 1.00 51.80 ? 137 GLU A C 1 ATOM 713 O O . GLU A 1 96 ? 22.372 25.690 14.384 1.00 51.95 ? 137 GLU A O 1 ATOM 714 C CB . GLU A 1 96 ? 20.180 27.629 14.560 1.00 50.61 ? 137 GLU A CB 1 ATOM 715 C CG . GLU A 1 96 ? 18.907 28.289 14.064 1.00 49.50 ? 137 GLU A CG 1 ATOM 716 C CD . GLU A 1 96 ? 17.854 28.528 15.138 1.00 48.63 ? 137 GLU A CD 1 ATOM 717 O OE1 . GLU A 1 96 ? 17.732 27.711 16.074 1.00 47.60 ? 137 GLU A OE1 1 ATOM 718 O OE2 . GLU A 1 96 ? 17.116 29.524 14.996 1.00 48.76 ? 137 GLU A OE2 1 ATOM 719 N N . ILE A 1 97 ? 23.694 27.411 13.728 1.00 51.39 ? 138 ILE A N 1 ATOM 720 C CA . ILE A 1 97 ? 24.970 26.681 13.883 1.00 51.74 ? 138 ILE A CA 1 ATOM 721 C C . ILE A 1 97 ? 25.546 26.769 15.301 1.00 49.85 ? 138 ILE A C 1 ATOM 722 O O . ILE A 1 97 ? 26.473 26.026 15.654 1.00 50.28 ? 138 ILE A O 1 ATOM 723 C CB . ILE A 1 97 ? 26.053 27.116 12.833 1.00 52.78 ? 138 ILE A CB 1 ATOM 724 C CG1 . ILE A 1 97 ? 26.393 28.616 12.962 1.00 53.24 ? 138 ILE A CG1 1 ATOM 725 C CG2 . ILE A 1 97 ? 25.612 26.741 11.415 1.00 53.98 ? 138 ILE A CG2 1 ATOM 726 C CD1 . ILE A 1 97 ? 27.600 29.083 12.106 1.00 54.15 ? 138 ILE A CD1 1 ATOM 727 N N . PHE A 1 98 ? 24.994 27.671 16.108 1.00 47.86 ? 139 PHE A N 1 ATOM 728 C CA . PHE A 1 98 ? 25.361 27.771 17.503 1.00 45.87 ? 139 PHE A CA 1 ATOM 729 C C . PHE A 1 98 ? 24.132 28.231 18.260 1.00 43.65 ? 139 PHE A C 1 ATOM 730 O O . PHE A 1 98 ? 23.417 29.128 17.795 1.00 42.42 ? 139 PHE A O 1 ATOM 731 C CB . PHE A 1 98 ? 26.501 28.773 17.722 1.00 45.71 ? 139 PHE A CB 1 ATOM 732 C CG . PHE A 1 98 ? 26.654 29.192 19.157 1.00 45.46 ? 139 PHE A CG 1 ATOM 733 C CD1 . PHE A 1 98 ? 27.279 28.347 20.073 1.00 46.36 ? 139 PHE A CD1 1 ATOM 734 C CD2 . PHE A 1 98 ? 26.135 30.410 19.606 1.00 45.39 ? 139 PHE A CD2 1 ATOM 735 C CE1 . PHE A 1 98 ? 27.396 28.713 21.423 1.00 46.75 ? 139 PHE A CE1 1 ATOM 736 C CE2 . PHE A 1 98 ? 26.250 30.790 20.961 1.00 43.59 ? 139 PHE A CE2 1 ATOM 737 C CZ . PHE A 1 98 ? 26.878 29.933 21.862 1.00 44.09 ? 139 PHE A CZ 1 ATOM 738 N N . ASN A 1 99 ? 23.888 27.600 19.405 1.00 42.99 ? 140 ASN A N 1 ATOM 739 C CA . ASN A 1 99 ? 22.833 28.022 20.326 1.00 41.10 ? 140 ASN A CA 1 ATOM 740 C C . ASN A 1 99 ? 23.332 28.288 21.735 1.00 40.04 ? 140 ASN A C 1 ATOM 741 O O . ASN A 1 99 ? 24.119 27.512 22.291 1.00 39.36 ? 140 ASN A O 1 ATOM 742 C CB . ASN A 1 99 ? 21.751 26.953 20.459 1.00 41.94 ? 140 ASN A CB 1 ATOM 743 C CG . ASN A 1 99 ? 21.045 26.638 19.147 1.00 43.72 ? 140 ASN A CG 1 ATOM 744 O OD1 . ASN A 1 99 ? 20.850 27.508 18.286 1.00 44.19 ? 140 ASN A OD1 1 ATOM 745 N ND2 . ASN A 1 99 ? 20.650 25.385 19.006 1.00 48.61 ? 140 ASN A ND2 1 ATOM 746 N N . THR A 1 100 ? 22.812 29.356 22.329 1.00 38.31 ? 141 THR A N 1 ATOM 747 C CA . THR A 1 100 ? 23.087 29.640 23.742 1.00 37.34 ? 141 THR A CA 1 ATOM 748 C C . THR A 1 100 ? 22.389 28.607 24.631 1.00 37.02 ? 141 THR A C 1 ATOM 749 O O . THR A 1 100 ? 21.465 27.924 24.173 1.00 36.97 ? 141 THR A O 1 ATOM 750 C CB . THR A 1 100 ? 22.698 31.074 24.101 1.00 36.80 ? 141 THR A CB 1 ATOM 751 O OG1 . THR A 1 100 ? 21.290 31.262 23.899 1.00 37.09 ? 141 THR A OG1 1 ATOM 752 C CG2 . THR A 1 100 ? 23.468 32.057 23.219 1.00 36.50 ? 141 THR A CG2 1 ATOM 753 N N . SER A 1 101 ? 22.807 28.510 25.896 1.00 36.31 ? 142 SER A N 1 ATOM 754 C CA . SER A 1 101 ? 22.326 27.481 26.820 1.00 35.75 ? 142 SER A CA 1 ATOM 755 C C . SER A 1 101 ? 20.825 27.606 27.138 1.00 35.49 ? 142 SER A C 1 ATOM 756 O O . SER A 1 101 ? 20.244 28.708 27.075 1.00 36.25 ? 142 SER A O 1 ATOM 757 C CB . SER A 1 101 ? 23.135 27.544 28.127 1.00 36.58 ? 142 SER A CB 1 ATOM 758 O OG A SER A 1 101 ? 22.686 28.584 28.991 0.50 30.24 ? 142 SER A OG 1 ATOM 759 O OG B SER A 1 101 ? 23.016 26.345 28.867 0.50 39.35 ? 142 SER A OG 1 ATOM 760 N N . LEU A 1 102 ? 20.198 26.490 27.492 1.00 35.83 ? 143 LEU A N 1 ATOM 761 C CA . LEU A 1 102 ? 18.796 26.551 27.920 1.00 35.79 ? 143 LEU A CA 1 ATOM 762 C C . LEU A 1 102 ? 18.665 26.654 29.431 1.00 35.15 ? 143 LEU A C 1 ATOM 763 O O . LEU A 1 102 ? 17.568 26.909 29.924 1.00 34.88 ? 143 LEU A O 1 ATOM 764 C CB . LEU A 1 102 ? 17.999 25.362 27.382 1.00 37.69 ? 143 LEU A CB 1 ATOM 765 C CG . LEU A 1 102 ? 18.042 25.239 25.843 1.00 38.32 ? 143 LEU A CG 1 ATOM 766 C CD1 . LEU A 1 102 ? 17.421 23.934 25.399 1.00 45.12 ? 143 LEU A CD1 1 ATOM 767 C CD2 . LEU A 1 102 ? 17.357 26.455 25.191 1.00 38.95 ? 143 LEU A CD2 1 ATOM 768 N N . PHE A 1 103 ? 19.778 26.523 30.152 1.00 34.45 ? 144 PHE A N 1 ATOM 769 C CA . PHE A 1 103 ? 19.781 26.644 31.624 1.00 34.05 ? 144 PHE A CA 1 ATOM 770 C C . PHE A 1 103 ? 21.233 26.733 32.098 1.00 33.25 ? 144 PHE A C 1 ATOM 771 O O . PHE A 1 103 ? 22.149 26.352 31.358 1.00 34.68 ? 144 PHE A O 1 ATOM 772 C CB . PHE A 1 103 ? 19.053 25.441 32.259 1.00 35.96 ? 144 PHE A CB 1 ATOM 773 C CG . PHE A 1 103 ? 19.651 24.100 31.882 1.00 36.77 ? 144 PHE A CG 1 ATOM 774 C CD1 . PHE A 1 103 ? 20.645 23.524 32.681 1.00 40.47 ? 144 PHE A CD1 1 ATOM 775 C CD2 . PHE A 1 103 ? 19.266 23.431 30.719 1.00 42.72 ? 144 PHE A CD2 1 ATOM 776 C CE1 . PHE A 1 103 ? 21.246 22.315 32.353 1.00 44.38 ? 144 PHE A CE1 1 ATOM 777 C CE2 . PHE A 1 103 ? 19.864 22.200 30.366 1.00 45.02 ? 144 PHE A CE2 1 ATOM 778 C CZ . PHE A 1 103 ? 20.854 21.635 31.191 1.00 44.31 ? 144 PHE A CZ 1 ATOM 779 N N . GLU A 1 104 ? 21.446 27.241 33.318 1.00 31.05 ? 145 GLU A N 1 ATOM 780 C CA . GLU A 1 104 ? 22.756 27.234 33.976 1.00 30.47 ? 145 GLU A CA 1 ATOM 781 C C . GLU A 1 104 ? 22.995 25.848 34.561 1.00 31.56 ? 145 GLU A C 1 ATOM 782 O O . GLU A 1 104 ? 22.101 25.269 35.180 1.00 31.36 ? 145 GLU A O 1 ATOM 783 C CB . GLU A 1 104 ? 22.766 28.207 35.164 1.00 30.72 ? 145 GLU A CB 1 ATOM 784 C CG . GLU A 1 104 ? 22.636 29.660 34.819 1.00 27.05 ? 145 GLU A CG 1 ATOM 785 C CD . GLU A 1 104 ? 22.492 30.488 36.100 1.00 30.03 ? 145 GLU A CD 1 ATOM 786 O OE1 . GLU A 1 104 ? 21.404 30.470 36.668 1.00 30.37 ? 145 GLU A OE1 1 ATOM 787 O OE2 . GLU A 1 104 ? 23.501 31.085 36.529 1.00 31.09 ? 145 GLU A OE2 1 ATOM 788 N N . PRO A 1 105 ? 24.214 25.311 34.399 1.00 32.13 ? 146 PRO A N 1 ATOM 789 C CA . PRO A 1 105 ? 24.540 24.055 35.079 1.00 32.49 ? 146 PRO A CA 1 ATOM 790 C C . PRO A 1 105 ? 24.260 24.173 36.579 1.00 32.03 ? 146 PRO A C 1 ATOM 791 O O . PRO A 1 105 ? 24.764 25.108 37.236 1.00 32.93 ? 146 PRO A O 1 ATOM 792 C CB . PRO A 1 105 ? 26.047 23.901 34.821 1.00 33.73 ? 146 PRO A CB 1 ATOM 793 C CG . PRO A 1 105 ? 26.294 24.725 33.593 1.00 34.94 ? 146 PRO A CG 1 ATOM 794 C CD . PRO A 1 105 ? 25.343 25.863 33.629 1.00 33.57 ? 146 PRO A CD 1 ATOM 795 N N . PRO A 1 106 ? 23.412 23.298 37.130 1.00 32.08 ? 147 PRO A N 1 ATOM 796 C CA . PRO A 1 106 ? 23.063 23.577 38.524 1.00 32.01 ? 147 PRO A CA 1 ATOM 797 C C . PRO A 1 106 ? 24.195 23.277 39.474 1.00 33.38 ? 147 PRO A C 1 ATOM 798 O O . PRO A 1 106 ? 25.036 22.439 39.150 1.00 34.65 ? 147 PRO A O 1 ATOM 799 C CB . PRO A 1 106 ? 21.862 22.660 38.795 1.00 33.20 ? 147 PRO A CB 1 ATOM 800 C CG . PRO A 1 106 ? 21.794 21.722 37.654 1.00 33.90 ? 147 PRO A CG 1 ATOM 801 C CD . PRO A 1 106 ? 22.505 22.327 36.495 1.00 33.32 ? 147 PRO A CD 1 ATOM 802 N N . PRO A 1 107 ? 24.202 23.951 40.649 1.00 33.70 ? 148 PRO A N 1 ATOM 803 C CA . PRO A 1 107 ? 25.285 23.680 41.588 1.00 34.50 ? 148 PRO A CA 1 ATOM 804 C C . PRO A 1 107 ? 25.238 22.270 42.213 1.00 34.04 ? 148 PRO A C 1 ATOM 805 O O . PRO A 1 107 ? 24.172 21.638 42.251 1.00 33.03 ? 148 PRO A O 1 ATOM 806 C CB . PRO A 1 107 ? 25.069 24.746 42.677 1.00 33.65 ? 148 PRO A CB 1 ATOM 807 C CG . PRO A 1 107 ? 23.678 25.190 42.583 1.00 33.89 ? 148 PRO A CG 1 ATOM 808 C CD . PRO A 1 107 ? 23.184 24.857 41.184 1.00 34.19 ? 148 PRO A CD 1 ATOM 809 N N . PRO A 1 108 ? 26.380 21.813 42.764 1.00 34.20 ? 149 PRO A N 1 ATOM 810 C CA . PRO A 1 108 ? 26.463 20.473 43.350 1.00 35.31 ? 149 PRO A CA 1 ATOM 811 C C . PRO A 1 108 ? 25.391 20.211 44.405 1.00 34.44 ? 149 PRO A C 1 ATOM 812 O O . PRO A 1 108 ? 25.237 20.994 45.349 1.00 34.20 ? 149 PRO A O 1 ATOM 813 C CB . PRO A 1 108 ? 27.847 20.457 43.994 1.00 36.24 ? 149 PRO A CB 1 ATOM 814 C CG . PRO A 1 108 ? 28.657 21.463 43.160 1.00 35.92 ? 149 PRO A CG 1 ATOM 815 C CD . PRO A 1 108 ? 27.686 22.510 42.741 1.00 34.54 ? 149 PRO A CD 1 ATOM 816 N N . GLY A 1 109 ? 24.673 19.096 44.250 1.00 35.64 ? 150 GLY A N 1 ATOM 817 C CA . GLY A 1 109 ? 23.664 18.729 45.231 1.00 37.24 ? 150 GLY A CA 1 ATOM 818 C C . GLY A 1 109 ? 22.265 19.266 44.915 1.00 39.28 ? 150 GLY A C 1 ATOM 819 O O . GLY A 1 109 ? 21.303 18.854 45.563 1.00 40.40 ? 150 GLY A O 1 ATOM 820 N N . TYR A 1 110 ? 22.174 20.138 43.906 1.00 39.59 ? 151 TYR A N 1 ATOM 821 C CA . TYR A 1 110 ? 20.905 20.786 43.471 1.00 41.49 ? 151 TYR A CA 1 ATOM 822 C C . TYR A 1 110 ? 20.584 20.463 42.027 1.00 44.77 ? 151 TYR A C 1 ATOM 823 O O . TYR A 1 110 ? 19.757 21.149 41.399 1.00 45.66 ? 151 TYR A O 1 ATOM 824 C CB . TYR A 1 110 ? 21.078 22.292 43.440 1.00 39.70 ? 151 TYR A CB 1 ATOM 825 C CG . TYR A 1 110 ? 21.290 22.967 44.744 1.00 35.50 ? 151 TYR A CG 1 ATOM 826 C CD1 . TYR A 1 110 ? 20.213 23.512 45.443 1.00 34.07 ? 151 TYR A CD1 1 ATOM 827 C CD2 . TYR A 1 110 ? 22.573 23.138 45.249 1.00 32.20 ? 151 TYR A CD2 1 ATOM 828 C CE1 . TYR A 1 110 ? 20.400 24.150 46.647 1.00 32.17 ? 151 TYR A CE1 1 ATOM 829 C CE2 . TYR A 1 110 ? 22.778 23.778 46.433 1.00 29.36 ? 151 TYR A CE2 1 ATOM 830 C CZ . TYR A 1 110 ? 21.692 24.303 47.116 1.00 30.34 ? 151 TYR A CZ 1 ATOM 831 O OH . TYR A 1 110 ? 21.904 24.934 48.272 1.00 27.86 ? 151 TYR A OH 1 ATOM 832 N N . GLU A 1 111 ? 21.292 19.498 41.457 1.00 47.46 ? 152 GLU A N 1 ATOM 833 C CA . GLU A 1 111 ? 21.095 19.145 40.058 1.00 50.59 ? 152 GLU A CA 1 ATOM 834 C C . GLU A 1 111 ? 19.731 18.441 39.830 1.00 52.03 ? 152 GLU A C 1 ATOM 835 O O . GLU A 1 111 ? 19.315 18.238 38.675 1.00 53.36 ? 152 GLU A O 1 ATOM 836 C CB . GLU A 1 111 ? 22.280 18.305 39.513 1.00 51.70 ? 152 GLU A CB 1 ATOM 837 C CG . GLU A 1 111 ? 23.695 18.872 39.818 1.00 52.51 ? 152 GLU A CG 1 ATOM 838 C CD . GLU A 1 111 ? 24.365 18.280 41.070 1.00 53.91 ? 152 GLU A CD 1 ATOM 839 O OE1 . GLU A 1 111 ? 25.603 18.270 41.113 1.00 54.28 ? 152 GLU A OE1 1 ATOM 840 O OE2 . GLU A 1 111 ? 23.687 17.841 42.014 1.00 53.97 ? 152 GLU A OE2 1 ATOM 841 N N . ASN A 1 112 ? 19.046 18.097 40.928 1.00 52.89 ? 153 ASN A N 1 ATOM 842 C CA . ASN A 1 112 ? 17.703 17.493 40.881 1.00 53.51 ? 153 ASN A CA 1 ATOM 843 C C . ASN A 1 112 ? 16.585 18.360 41.503 1.00 53.10 ? 153 ASN A C 1 ATOM 844 O O . ASN A 1 112 ? 15.432 17.931 41.636 1.00 53.65 ? 153 ASN A O 1 ATOM 845 C CB . ASN A 1 112 ? 17.711 16.101 41.520 1.00 54.95 ? 153 ASN A CB 1 ATOM 846 C CG . ASN A 1 112 ? 16.522 15.257 41.088 1.00 56.08 ? 153 ASN A CG 1 ATOM 847 O OD1 . ASN A 1 112 ? 16.398 14.890 39.917 1.00 57.62 ? 153 ASN A OD1 1 ATOM 848 N ND2 . ASN A 1 112 ? 15.640 14.949 42.035 1.00 57.65 ? 153 ASN A ND2 1 ATOM 849 N N . VAL A 1 113 ? 16.923 19.588 41.875 1.00 51.58 ? 154 VAL A N 1 ATOM 850 C CA . VAL A 1 113 ? 15.905 20.548 42.285 1.00 49.74 ? 154 VAL A CA 1 ATOM 851 C C . VAL A 1 113 ? 15.071 20.938 41.028 1.00 49.17 ? 154 VAL A C 1 ATOM 852 O O . VAL A 1 113 ? 15.625 21.228 39.956 1.00 50.25 ? 154 VAL A O 1 ATOM 853 C CB . VAL A 1 113 ? 16.529 21.743 43.082 1.00 49.57 ? 154 VAL A CB 1 ATOM 854 C CG1 . VAL A 1 113 ? 15.468 22.824 43.417 1.00 47.13 ? 154 VAL A CG1 1 ATOM 855 C CG2 . VAL A 1 113 ? 17.177 21.219 44.388 1.00 50.31 ? 154 VAL A CG2 1 ATOM 856 N N A SER A 1 114 ? 13.756 20.917 41.241 0.50 47.50 ? 155 SER A N 1 ATOM 857 N N B SER A 1 114 ? 13.746 20.897 41.079 0.50 48.67 ? 155 SER A N 1 ATOM 858 C CA A SER A 1 114 ? 12.769 21.302 40.249 0.50 45.65 ? 155 SER A CA 1 ATOM 859 C CA B SER A 1 114 ? 13.007 20.927 39.788 0.50 48.02 ? 155 SER A CA 1 ATOM 860 C C A SER A 1 114 ? 12.444 22.785 40.333 0.50 43.16 ? 155 SER A C 1 ATOM 861 C C B SER A 1 114 ? 12.598 22.302 39.190 0.50 46.32 ? 155 SER A C 1 ATOM 862 O O A SER A 1 114 ? 12.681 23.450 41.364 0.50 41.49 ? 155 SER A O 1 ATOM 863 O O B SER A 1 114 ? 12.809 22.555 37.990 0.50 47.17 ? 155 SER A O 1 ATOM 864 C CB A SER A 1 114 ? 11.475 20.493 40.429 0.50 46.59 ? 155 SER A CB 1 ATOM 865 C CB B SER A 1 114 ? 11.814 19.953 39.817 0.50 48.74 ? 155 SER A CB 1 ATOM 866 O OG A SER A 1 114 ? 10.608 20.670 39.315 0.50 47.57 ? 155 SER A OG 1 ATOM 867 O OG B SER A 1 114 ? 11.427 19.610 38.499 0.50 50.81 ? 155 SER A OG 1 ATOM 868 N N A ASP A 1 115 ? 11.893 23.290 39.233 0.50 40.98 ? 156 ASP A N 1 ATOM 869 N N B ASP A 1 115 ? 12.009 23.162 40.021 0.50 43.44 ? 156 ASP A N 1 ATOM 870 C CA A ASP A 1 115 ? 11.337 24.623 39.212 0.50 38.85 ? 156 ASP A CA 1 ATOM 871 C CA B ASP A 1 115 ? 11.460 24.457 39.595 0.50 40.27 ? 156 ASP A CA 1 ATOM 872 C C A ASP A 1 115 ? 12.406 25.700 39.378 0.50 36.30 ? 156 ASP A C 1 ATOM 873 C C B ASP A 1 115 ? 12.480 25.611 39.585 0.50 37.21 ? 156 ASP A C 1 ATOM 874 O O A ASP A 1 115 ? 12.116 26.774 39.906 0.50 35.48 ? 156 ASP A O 1 ATOM 875 O O B ASP A 1 115 ? 12.208 26.670 40.151 0.50 36.22 ? 156 ASP A O 1 ATOM 876 C CB A ASP A 1 115 ? 10.287 24.765 40.316 0.50 39.65 ? 156 ASP A CB 1 ATOM 877 C CB B ASP A 1 115 ? 10.298 24.858 40.520 0.50 40.77 ? 156 ASP A CB 1 ATOM 878 C CG A ASP A 1 115 ? 8.984 24.033 39.996 0.50 42.07 ? 156 ASP A CG 1 ATOM 879 C CG B ASP A 1 115 ? 9.113 23.893 40.446 0.50 42.27 ? 156 ASP A CG 1 ATOM 880 O OD1 A ASP A 1 115 ? 9.008 23.019 39.249 0.50 45.61 ? 156 ASP A OD1 1 ATOM 881 O OD1 B ASP A 1 115 ? 8.483 23.779 39.362 0.50 44.53 ? 156 ASP A OD1 1 ATOM 882 O OD2 A ASP A 1 115 ? 7.930 24.481 40.507 0.50 44.09 ? 156 ASP A OD2 1 ATOM 883 O OD2 B ASP A 1 115 ? 8.796 23.267 41.484 0.50 43.68 ? 156 ASP A OD2 1 ATOM 884 N N . ILE A 1 116 ? 13.636 25.416 38.950 1.00 35.22 ? 157 ILE A N 1 ATOM 885 C CA . ILE A 1 116 ? 14.610 26.498 38.774 1.00 31.27 ? 157 ILE A CA 1 ATOM 886 C C . ILE A 1 116 ? 14.253 27.205 37.465 1.00 30.54 ? 157 ILE A C 1 ATOM 887 O O . ILE A 1 116 ? 14.298 26.582 36.391 1.00 30.14 ? 157 ILE A O 1 ATOM 888 C CB . ILE A 1 116 ? 16.055 25.951 38.714 1.00 30.41 ? 157 ILE A CB 1 ATOM 889 C CG1 . ILE A 1 116 ? 16.411 25.349 40.077 1.00 28.18 ? 157 ILE A CG1 1 ATOM 890 C CG2 . ILE A 1 116 ? 17.023 27.064 38.317 1.00 28.00 ? 157 ILE A CG2 1 ATOM 891 C CD1 . ILE A 1 116 ? 17.775 24.535 40.116 1.00 27.02 ? 157 ILE A CD1 1 ATOM 892 N N . VAL A 1 117 ? 13.849 28.476 37.549 1.00 29.27 ? 158 VAL A N 1 ATOM 893 C CA . VAL A 1 117 ? 13.490 29.232 36.361 1.00 28.63 ? 158 VAL A CA 1 ATOM 894 C C . VAL A 1 117 ? 14.765 29.471 35.581 1.00 28.68 ? 158 VAL A C 1 ATOM 895 O O . VAL A 1 117 ? 15.738 29.947 36.130 1.00 27.66 ? 158 VAL A O 1 ATOM 896 C CB . VAL A 1 117 ? 12.766 30.616 36.713 1.00 28.22 ? 158 VAL A CB 1 ATOM 897 C CG1 . VAL A 1 117 ? 13.777 31.755 37.241 1.00 27.62 ? 158 VAL A CG1 1 ATOM 898 C CG2 . VAL A 1 117 ? 11.958 31.062 35.493 1.00 29.37 ? 158 VAL A CG2 1 ATOM 899 N N . PRO A 1 118 ? 14.773 29.144 34.283 1.00 28.33 ? 159 PRO A N 1 ATOM 900 C CA . PRO A 1 118 ? 16.000 29.391 33.531 1.00 29.88 ? 159 PRO A CA 1 ATOM 901 C C . PRO A 1 118 ? 16.258 30.880 33.367 1.00 27.96 ? 159 PRO A C 1 ATOM 902 O O . PRO A 1 118 ? 15.327 31.698 33.530 1.00 28.16 ? 159 PRO A O 1 ATOM 903 C CB . PRO A 1 118 ? 15.728 28.725 32.153 1.00 30.93 ? 159 PRO A CB 1 ATOM 904 C CG . PRO A 1 118 ? 14.256 28.686 32.024 1.00 31.80 ? 159 PRO A CG 1 ATOM 905 C CD . PRO A 1 118 ? 13.701 28.554 33.452 1.00 30.41 ? 159 PRO A CD 1 ATOM 906 N N . PRO A 1 119 ? 17.504 31.257 33.059 1.00 27.68 ? 160 PRO A N 1 ATOM 907 C CA . PRO A 1 119 ? 17.761 32.689 32.866 1.00 26.75 ? 160 PRO A CA 1 ATOM 908 C C . PRO A 1 119 ? 16.844 33.332 31.797 1.00 26.29 ? 160 PRO A C 1 ATOM 909 O O . PRO A 1 119 ? 16.629 32.765 30.715 1.00 26.21 ? 160 PRO A O 1 ATOM 910 C CB . PRO A 1 119 ? 19.208 32.703 32.418 1.00 27.08 ? 160 PRO A CB 1 ATOM 911 C CG . PRO A 1 119 ? 19.801 31.476 33.071 1.00 28.22 ? 160 PRO A CG 1 ATOM 912 C CD . PRO A 1 119 ? 18.732 30.440 32.918 1.00 27.82 ? 160 PRO A CD 1 ATOM 913 N N . PHE A 1 120 ? 16.278 34.483 32.136 1.00 24.54 ? 161 PHE A N 1 ATOM 914 C CA . PHE A 1 120 ? 15.482 35.266 31.219 1.00 24.51 ? 161 PHE A CA 1 ATOM 915 C C . PHE A 1 120 ? 15.484 36.706 31.698 1.00 24.72 ? 161 PHE A C 1 ATOM 916 O O . PHE A 1 120 ? 15.840 36.944 32.870 1.00 23.21 ? 161 PHE A O 1 ATOM 917 C CB . PHE A 1 120 ? 14.042 34.708 31.121 1.00 24.67 ? 161 PHE A CB 1 ATOM 918 C CG . PHE A 1 120 ? 13.149 35.009 32.341 1.00 24.85 ? 161 PHE A CG 1 ATOM 919 C CD1 . PHE A 1 120 ? 12.012 35.837 32.213 1.00 24.61 ? 161 PHE A CD1 1 ATOM 920 C CD2 . PHE A 1 120 ? 13.402 34.409 33.565 1.00 26.52 ? 161 PHE A CD2 1 ATOM 921 C CE1 . PHE A 1 120 ? 11.165 36.078 33.314 1.00 26.07 ? 161 PHE A CE1 1 ATOM 922 C CE2 . PHE A 1 120 ? 12.576 34.662 34.689 1.00 25.90 ? 161 PHE A CE2 1 ATOM 923 C CZ . PHE A 1 120 ? 11.436 35.522 34.547 1.00 24.59 ? 161 PHE A CZ 1 ATOM 924 N N . SER A 1 121 ? 15.039 37.623 30.815 1.00 25.43 ? 162 SER A N 1 ATOM 925 C CA . SER A 1 121 ? 14.869 39.040 31.176 1.00 24.60 ? 162 SER A CA 1 ATOM 926 C C . SER A 1 121 ? 13.381 39.257 31.406 1.00 23.75 ? 162 SER A C 1 ATOM 927 O O . SER A 1 121 ? 12.605 39.194 30.471 1.00 25.31 ? 162 SER A O 1 ATOM 928 C CB . SER A 1 121 ? 15.402 39.935 30.038 1.00 26.19 ? 162 SER A CB 1 ATOM 929 O OG . SER A 1 121 ? 16.811 39.721 29.919 1.00 25.11 ? 162 SER A OG 1 ATOM 930 N N . ALA A 1 122 ? 12.980 39.466 32.648 1.00 23.91 ? 163 ALA A N 1 ATOM 931 C CA . ALA A 1 122 ? 11.540 39.578 32.916 1.00 23.78 ? 163 ALA A CA 1 ATOM 932 C C . ALA A 1 122 ? 10.975 40.812 32.228 1.00 24.81 ? 163 ALA A C 1 ATOM 933 O O . ALA A 1 122 ? 11.538 41.901 32.329 1.00 23.10 ? 163 ALA A O 1 ATOM 934 C CB . ALA A 1 122 ? 11.315 39.675 34.430 1.00 22.77 ? 163 ALA A CB 1 ATOM 935 N N . PHE A 1 123 ? 9.821 40.577 31.590 1.00 24.69 ? 164 PHE A N 1 ATOM 936 C CA . PHE A 1 123 ? 8.967 41.531 30.865 1.00 24.85 ? 164 PHE A CA 1 ATOM 937 C C . PHE A 1 123 ? 9.459 41.752 29.434 1.00 26.41 ? 164 PHE A C 1 ATOM 938 O O . PHE A 1 123 ? 8.926 42.613 28.749 1.00 27.93 ? 164 PHE A O 1 ATOM 939 C CB . PHE A 1 123 ? 8.708 42.832 31.606 1.00 23.95 ? 164 PHE A CB 1 ATOM 940 C CG . PHE A 1 123 ? 8.020 42.631 32.952 1.00 23.03 ? 164 PHE A CG 1 ATOM 941 C CD1 . PHE A 1 123 ? 6.631 42.414 33.026 1.00 23.63 ? 164 PHE A CD1 1 ATOM 942 C CD2 . PHE A 1 123 ? 8.758 42.656 34.128 1.00 22.05 ? 164 PHE A CD2 1 ATOM 943 C CE1 . PHE A 1 123 ? 5.998 42.285 34.271 1.00 24.55 ? 164 PHE A CE1 1 ATOM 944 C CE2 . PHE A 1 123 ? 8.125 42.509 35.376 1.00 22.84 ? 164 PHE A CE2 1 ATOM 945 C CZ . PHE A 1 123 ? 6.752 42.313 35.451 1.00 22.29 ? 164 PHE A CZ 1 ATOM 946 N N . SER A 1 124 ? 10.473 41.005 29.004 1.00 26.03 ? 165 SER A N 1 ATOM 947 C CA . SER A 1 124 ? 10.771 41.024 27.556 1.00 27.71 ? 165 SER A CA 1 ATOM 948 C C . SER A 1 124 ? 9.496 40.684 26.767 1.00 29.03 ? 165 SER A C 1 ATOM 949 O O . SER A 1 124 ? 8.735 39.756 27.114 1.00 29.58 ? 165 SER A O 1 ATOM 950 C CB . SER A 1 124 ? 11.887 40.041 27.166 1.00 28.30 ? 165 SER A CB 1 ATOM 951 O OG . SER A 1 124 ? 12.063 40.064 25.739 1.00 30.67 ? 165 SER A OG 1 ATOM 952 N N . PRO A 1 125 ? 9.262 41.423 25.663 1.00 30.98 ? 166 PRO A N 1 ATOM 953 C CA . PRO A 1 125 ? 8.237 40.952 24.754 1.00 32.62 ? 166 PRO A CA 1 ATOM 954 C C . PRO A 1 125 ? 8.724 39.730 23.991 1.00 34.02 ? 166 PRO A C 1 ATOM 955 O O . PRO A 1 125 ? 9.935 39.427 23.983 1.00 33.75 ? 166 PRO A O 1 ATOM 956 C CB . PRO A 1 125 ? 8.068 42.125 23.791 1.00 33.60 ? 166 PRO A CB 1 ATOM 957 C CG . PRO A 1 125 ? 9.420 42.788 23.773 1.00 32.12 ? 166 PRO A CG 1 ATOM 958 C CD . PRO A 1 125 ? 9.903 42.664 25.200 1.00 31.07 ? 166 PRO A CD 1 ATOM 959 N N . GLN A 1 126 ? 7.776 39.032 23.371 1.00 34.95 ? 167 GLN A N 1 ATOM 960 C CA . GLN A 1 126 ? 8.065 37.956 22.438 1.00 36.87 ? 167 GLN A CA 1 ATOM 961 C C . GLN A 1 126 ? 8.571 38.481 21.101 1.00 37.96 ? 167 GLN A C 1 ATOM 962 O O . GLN A 1 126 ? 8.243 39.603 20.684 1.00 38.56 ? 167 GLN A O 1 ATOM 963 C CB . GLN A 1 126 ? 6.824 37.088 22.235 1.00 37.40 ? 167 GLN A CB 1 ATOM 964 C CG . GLN A 1 126 ? 6.209 36.573 23.566 1.00 39.96 ? 167 GLN A CG 1 ATOM 965 C CD . GLN A 1 126 ? 4.976 35.716 23.341 1.00 45.94 ? 167 GLN A CD 1 ATOM 966 O OE1 . GLN A 1 126 ? 4.532 35.552 22.212 1.00 48.09 ? 167 GLN A OE1 1 ATOM 967 N NE2 . GLN A 1 126 ? 4.416 35.169 24.418 1.00 44.49 ? 167 GLN A NE2 1 ATOM 968 N N . GLY A 1 127 ? 9.422 37.685 20.476 1.00 38.66 ? 168 GLY A N 1 ATOM 969 C CA . GLY A 1 127 ? 9.875 37.939 19.108 1.00 39.60 ? 168 GLY A CA 1 ATOM 970 C C . GLY A 1 127 ? 11.017 37.039 18.708 1.00 40.55 ? 168 GLY A C 1 ATOM 971 O O . GLY A 1 127 ? 11.603 36.334 19.539 1.00 39.46 ? 168 GLY A O 1 ATOM 972 N N . MET A 1 128 ? 11.310 37.050 17.406 1.00 42.06 ? 169 MET A N 1 ATOM 973 C CA . MET A 1 128 ? 12.423 36.287 16.838 1.00 43.43 ? 169 MET A CA 1 ATOM 974 C C . MET A 1 128 ? 13.254 37.139 15.876 1.00 43.39 ? 169 MET A C 1 ATOM 975 O O . MET A 1 128 ? 13.558 36.700 14.751 1.00 44.69 ? 169 MET A O 1 ATOM 976 C CB . MET A 1 128 ? 11.887 35.036 16.153 1.00 45.29 ? 169 MET A CB 1 ATOM 977 C CG . MET A 1 128 ? 11.386 33.981 17.140 1.00 49.56 ? 169 MET A CG 1 ATOM 978 S SD . MET A 1 128 ? 10.766 32.536 16.282 1.00 62.90 ? 169 MET A SD 1 ATOM 979 C CE . MET A 1 128 ? 11.010 31.293 17.535 1.00 60.46 ? 169 MET A CE 1 ATOM 980 N N . PRO A 1 129 ? 13.638 38.356 16.306 1.00 43.27 ? 170 PRO A N 1 ATOM 981 C CA . PRO A 1 129 ? 14.424 39.264 15.479 1.00 44.48 ? 170 PRO A CA 1 ATOM 982 C C . PRO A 1 129 ? 15.747 38.618 15.066 1.00 46.83 ? 170 PRO A C 1 ATOM 983 O O . PRO A 1 129 ? 16.400 37.960 15.882 1.00 45.36 ? 170 PRO A O 1 ATOM 984 C CB . PRO A 1 129 ? 14.687 40.458 16.399 1.00 43.82 ? 170 PRO A CB 1 ATOM 985 C CG . PRO A 1 129 ? 14.562 39.902 17.799 1.00 41.18 ? 170 PRO A CG 1 ATOM 986 C CD . PRO A 1 129 ? 13.476 38.871 17.684 1.00 41.10 ? 170 PRO A CD 1 ATOM 987 N N . GLU A 1 130 ? 16.111 38.773 13.796 1.00 49.30 ? 171 GLU A N 1 ATOM 988 C CA . GLU A 1 130 ? 17.448 38.393 13.340 1.00 52.38 ? 171 GLU A CA 1 ATOM 989 C C . GLU A 1 130 ? 18.124 39.572 12.663 1.00 53.32 ? 171 GLU A C 1 ATOM 990 O O . GLU A 1 130 ? 17.470 40.353 11.959 1.00 54.94 ? 171 GLU A O 1 ATOM 991 C CB . GLU A 1 130 ? 17.449 37.147 12.445 1.00 53.76 ? 171 GLU A CB 1 ATOM 992 C CG . GLU A 1 130 ? 16.468 37.134 11.311 1.00 58.00 ? 171 GLU A CG 1 ATOM 993 C CD . GLU A 1 130 ? 16.778 36.029 10.303 1.00 64.30 ? 171 GLU A CD 1 ATOM 994 O OE1 . GLU A 1 130 ? 16.180 34.932 10.422 1.00 66.63 ? 171 GLU A OE1 1 ATOM 995 O OE2 . GLU A 1 130 ? 17.630 36.250 9.404 1.00 65.97 ? 171 GLU A OE2 1 ATOM 996 N N . GLY A 1 131 ? 19.422 39.723 12.909 1.00 53.01 ? 172 GLY A N 1 ATOM 997 C CA . GLY A 1 131 ? 20.173 40.825 12.334 1.00 53.13 ? 172 GLY A CA 1 ATOM 998 C C . GLY A 1 131 ? 21.632 40.799 12.719 1.00 52.44 ? 172 GLY A C 1 ATOM 999 O O . GLY A 1 131 ? 22.155 39.782 13.179 1.00 52.62 ? 172 GLY A O 1 ATOM 1000 N N . ASP A 1 132 ? 22.284 41.938 12.534 1.00 51.80 ? 173 ASP A N 1 ATOM 1001 C CA . ASP A 1 132 ? 23.716 42.051 12.764 1.00 50.91 ? 173 ASP A CA 1 ATOM 1002 C C . ASP A 1 132 ? 23.961 42.658 14.121 1.00 48.15 ? 173 ASP A C 1 ATOM 1003 O O . ASP A 1 132 ? 23.192 43.515 14.562 1.00 46.62 ? 173 ASP A O 1 ATOM 1004 C CB . ASP A 1 132 ? 24.341 42.933 11.696 1.00 52.31 ? 173 ASP A CB 1 ATOM 1005 C CG . ASP A 1 132 ? 24.159 42.373 10.291 1.00 55.10 ? 173 ASP A CG 1 ATOM 1006 O OD1 . ASP A 1 132 ? 24.196 41.133 10.136 1.00 57.02 ? 173 ASP A OD1 1 ATOM 1007 O OD2 . ASP A 1 132 ? 23.977 43.183 9.349 1.00 57.23 ? 173 ASP A OD2 1 ATOM 1008 N N . LEU A 1 133 ? 25.037 42.237 14.772 1.00 46.26 ? 174 LEU A N 1 ATOM 1009 C CA . LEU A 1 133 ? 25.336 42.718 16.114 1.00 44.02 ? 174 LEU A CA 1 ATOM 1010 C C . LEU A 1 133 ? 26.093 44.053 16.119 1.00 43.85 ? 174 LEU A C 1 ATOM 1011 O O . LEU A 1 133 ? 26.954 44.295 15.263 1.00 45.11 ? 174 LEU A O 1 ATOM 1012 C CB . LEU A 1 133 ? 26.177 41.649 16.815 1.00 44.15 ? 174 LEU A CB 1 ATOM 1013 C CG A LEU A 1 133 ? 26.001 41.156 18.250 0.50 42.95 ? 174 LEU A CG 1 ATOM 1014 C CG B LEU A 1 133 ? 25.568 40.289 17.174 0.50 41.70 ? 174 LEU A CG 1 ATOM 1015 C CD1 A LEU A 1 133 ? 24.540 41.086 18.691 0.50 42.09 ? 174 LEU A CD1 1 ATOM 1016 C CD1 B LEU A 1 133 ? 26.629 39.393 17.830 0.50 40.89 ? 174 LEU A CD1 1 ATOM 1017 C CD2 A LEU A 1 133 ? 26.676 39.790 18.395 0.50 42.68 ? 174 LEU A CD2 1 ATOM 1018 C CD2 B LEU A 1 133 ? 24.324 40.427 18.069 0.50 37.67 ? 174 LEU A CD2 1 ATOM 1019 N N . VAL A 1 134 ? 25.777 44.914 17.085 1.00 42.61 ? 175 VAL A N 1 ATOM 1020 C CA . VAL A 1 134 ? 26.643 46.036 17.454 1.00 42.40 ? 175 VAL A CA 1 ATOM 1021 C C . VAL A 1 134 ? 26.954 45.890 18.946 1.00 41.70 ? 175 VAL A C 1 ATOM 1022 O O . VAL A 1 134 ? 26.048 45.642 19.758 1.00 40.85 ? 175 VAL A O 1 ATOM 1023 C CB . VAL A 1 134 ? 25.963 47.406 17.174 1.00 43.00 ? 175 VAL A CB 1 ATOM 1024 C CG1 . VAL A 1 134 ? 26.779 48.588 17.735 1.00 42.42 ? 175 VAL A CG1 1 ATOM 1025 C CG2 . VAL A 1 134 ? 25.739 47.580 15.692 1.00 42.97 ? 175 VAL A CG2 1 ATOM 1026 N N . TYR A 1 135 ? 28.226 46.018 19.297 1.00 40.73 ? 176 TYR A N 1 ATOM 1027 C CA . TYR A 1 135 ? 28.636 45.913 20.681 1.00 40.07 ? 176 TYR A CA 1 ATOM 1028 C C . TYR A 1 135 ? 28.677 47.336 21.263 1.00 39.69 ? 176 TYR A C 1 ATOM 1029 O O . TYR A 1 135 ? 29.337 48.226 20.678 1.00 39.92 ? 176 TYR A O 1 ATOM 1030 C CB . TYR A 1 135 ? 29.990 45.177 20.765 1.00 39.87 ? 176 TYR A CB 1 ATOM 1031 C CG . TYR A 1 135 ? 30.661 45.363 22.090 1.00 40.12 ? 176 TYR A CG 1 ATOM 1032 C CD1 . TYR A 1 135 ? 30.148 44.764 23.226 1.00 36.55 ? 176 TYR A CD1 1 ATOM 1033 C CD2 . TYR A 1 135 ? 31.814 46.122 22.205 1.00 41.02 ? 176 TYR A CD2 1 ATOM 1034 C CE1 . TYR A 1 135 ? 30.758 44.943 24.481 1.00 39.28 ? 176 TYR A CE1 1 ATOM 1035 C CE2 . TYR A 1 135 ? 32.428 46.303 23.437 1.00 40.14 ? 176 TYR A CE2 1 ATOM 1036 C CZ . TYR A 1 135 ? 31.894 45.709 24.566 1.00 37.06 ? 176 TYR A CZ 1 ATOM 1037 O OH . TYR A 1 135 ? 32.521 45.898 25.770 1.00 38.75 ? 176 TYR A OH 1 ATOM 1038 N N . VAL A 1 136 ? 27.955 47.544 22.374 1.00 37.85 ? 177 VAL A N 1 ATOM 1039 C CA . VAL A 1 136 ? 27.673 48.883 22.896 1.00 37.96 ? 177 VAL A CA 1 ATOM 1040 C C . VAL A 1 136 ? 28.275 49.127 24.269 1.00 36.93 ? 177 VAL A C 1 ATOM 1041 O O . VAL A 1 136 ? 27.830 50.014 25.017 1.00 36.69 ? 177 VAL A O 1 ATOM 1042 C CB . VAL A 1 136 ? 26.163 49.156 22.925 1.00 36.91 ? 177 VAL A CB 1 ATOM 1043 C CG1 . VAL A 1 136 ? 25.604 49.081 21.523 1.00 38.58 ? 177 VAL A CG1 1 ATOM 1044 C CG2 . VAL A 1 136 ? 25.460 48.135 23.815 1.00 37.94 ? 177 VAL A CG2 1 ATOM 1045 N N . ASN A 1 137 ? 29.321 48.365 24.585 1.00 37.57 ? 178 ASN A N 1 ATOM 1046 C CA . ASN A 1 137 ? 29.959 48.467 25.883 1.00 37.87 ? 178 ASN A CA 1 ATOM 1047 C C . ASN A 1 137 ? 28.889 48.220 26.952 1.00 36.60 ? 178 ASN A C 1 ATOM 1048 O O . ASN A 1 137 ? 28.211 47.194 26.883 1.00 36.15 ? 178 ASN A O 1 ATOM 1049 C CB . ASN A 1 137 ? 30.698 49.818 26.029 1.00 39.09 ? 178 ASN A CB 1 ATOM 1050 C CG . ASN A 1 137 ? 31.769 49.796 27.113 1.00 39.68 ? 178 ASN A CG 1 ATOM 1051 O OD1 . ASN A 1 137 ? 32.273 48.731 27.491 1.00 38.13 ? 178 ASN A OD1 1 ATOM 1052 N ND2 . ASN A 1 137 ? 32.124 50.979 27.621 1.00 39.79 ? 178 ASN A ND2 1 ATOM 1053 N N . TYR A 1 138 ? 28.720 49.153 27.902 1.00 35.71 ? 179 TYR A N 1 ATOM 1054 C CA . TYR A 1 138 ? 27.756 48.994 28.987 1.00 34.28 ? 179 TYR A CA 1 ATOM 1055 C C . TYR A 1 138 ? 26.362 49.492 28.631 1.00 33.61 ? 179 TYR A C 1 ATOM 1056 O O . TYR A 1 138 ? 25.458 49.499 29.499 1.00 32.37 ? 179 TYR A O 1 ATOM 1057 C CB . TYR A 1 138 ? 28.234 49.732 30.250 1.00 34.49 ? 179 TYR A CB 1 ATOM 1058 C CG . TYR A 1 138 ? 29.462 49.126 30.887 1.00 34.80 ? 179 TYR A CG 1 ATOM 1059 C CD1 . TYR A 1 138 ? 29.382 47.931 31.617 1.00 34.09 ? 179 TYR A CD1 1 ATOM 1060 C CD2 . TYR A 1 138 ? 30.713 49.763 30.777 1.00 36.28 ? 179 TYR A CD2 1 ATOM 1061 C CE1 . TYR A 1 138 ? 30.553 47.364 32.204 1.00 36.14 ? 179 TYR A CE1 1 ATOM 1062 C CE2 . TYR A 1 138 ? 31.864 49.216 31.362 1.00 39.20 ? 179 TYR A CE2 1 ATOM 1063 C CZ . TYR A 1 138 ? 31.777 48.039 32.090 1.00 37.43 ? 179 TYR A CZ 1 ATOM 1064 O OH . TYR A 1 138 ? 32.928 47.533 32.673 1.00 38.40 ? 179 TYR A OH 1 ATOM 1065 N N . ALA A 1 139 ? 26.165 49.895 27.376 1.00 33.95 ? 180 ALA A N 1 ATOM 1066 C CA . ALA A 1 139 ? 24.898 50.499 26.942 1.00 34.53 ? 180 ALA A CA 1 ATOM 1067 C C . ALA A 1 139 ? 24.469 51.719 27.789 1.00 34.38 ? 180 ALA A C 1 ATOM 1068 O O . ALA A 1 139 ? 23.253 51.988 27.969 1.00 32.80 ? 180 ALA A O 1 ATOM 1069 C CB . ALA A 1 139 ? 23.775 49.403 26.906 1.00 34.72 ? 180 ALA A CB 1 ATOM 1070 N N . ARG A 1 140 ? 25.461 52.441 28.331 1.00 34.22 ? 181 ARG A N 1 ATOM 1071 C CA . ARG A 1 140 ? 25.193 53.674 29.093 1.00 33.96 ? 181 ARG A CA 1 ATOM 1072 C C . ARG A 1 140 ? 24.857 54.831 28.152 1.00 33.90 ? 181 ARG A C 1 ATOM 1073 O O . ARG A 1 140 ? 25.098 54.774 26.944 1.00 33.62 ? 181 ARG A O 1 ATOM 1074 C CB . ARG A 1 140 ? 26.418 54.039 29.930 1.00 33.75 ? 181 ARG A CB 1 ATOM 1075 C CG . ARG A 1 140 ? 26.693 53.072 31.091 1.00 35.03 ? 181 ARG A CG 1 ATOM 1076 C CD . ARG A 1 140 ? 28.059 53.305 31.686 1.00 36.65 ? 181 ARG A CD 1 ATOM 1077 N NE . ARG A 1 140 ? 29.113 53.210 30.666 1.00 36.39 ? 181 ARG A NE 1 ATOM 1078 C CZ . ARG A 1 140 ? 30.413 53.396 30.881 1.00 40.68 ? 181 ARG A CZ 1 ATOM 1079 N NH1 . ARG A 1 140 ? 30.872 53.649 32.103 1.00 40.24 ? 181 ARG A NH1 1 ATOM 1080 N NH2 . ARG A 1 140 ? 31.263 53.298 29.869 1.00 40.90 ? 181 ARG A NH2 1 ATOM 1081 N N . THR A 1 141 ? 24.277 55.895 28.705 1.00 33.59 ? 182 THR A N 1 ATOM 1082 C CA . THR A 1 141 ? 24.003 57.071 27.889 1.00 33.64 ? 182 THR A CA 1 ATOM 1083 C C . THR A 1 141 ? 25.266 57.525 27.171 1.00 35.03 ? 182 THR A C 1 ATOM 1084 O O . THR A 1 141 ? 25.265 57.749 25.939 1.00 36.25 ? 182 THR A O 1 ATOM 1085 C CB . THR A 1 141 ? 23.424 58.205 28.772 1.00 33.24 ? 182 THR A CB 1 ATOM 1086 O OG1 . THR A 1 141 ? 22.150 57.779 29.266 1.00 33.46 ? 182 THR A OG1 1 ATOM 1087 C CG2 . THR A 1 141 ? 23.265 59.488 27.968 1.00 33.89 ? 182 THR A CG2 1 ATOM 1088 N N . GLU A 1 142 ? 26.370 57.599 27.916 1.00 35.43 ? 183 GLU A N 1 ATOM 1089 C CA . GLU A 1 142 ? 27.631 58.046 27.318 1.00 37.51 ? 183 GLU A CA 1 ATOM 1090 C C . GLU A 1 142 ? 28.176 57.077 26.260 1.00 37.89 ? 183 GLU A C 1 ATOM 1091 O O . GLU A 1 142 ? 28.857 57.503 25.344 1.00 38.88 ? 183 GLU A O 1 ATOM 1092 C CB . GLU A 1 142 ? 28.697 58.314 28.381 1.00 38.24 ? 183 GLU A CB 1 ATOM 1093 C CG . GLU A 1 142 ? 29.057 57.118 29.237 1.00 40.05 ? 183 GLU A CG 1 ATOM 1094 C CD . GLU A 1 142 ? 28.318 57.102 30.570 1.00 42.64 ? 183 GLU A CD 1 ATOM 1095 O OE1 . GLU A 1 142 ? 27.105 57.492 30.639 1.00 40.94 ? 183 GLU A OE1 1 ATOM 1096 O OE2 . GLU A 1 142 ? 28.966 56.687 31.558 1.00 42.21 ? 183 GLU A OE2 1 ATOM 1097 N N . ASP A 1 143 ? 27.873 55.783 26.398 1.00 37.59 ? 184 ASP A N 1 ATOM 1098 C CA . ASP A 1 143 ? 28.334 54.779 25.395 1.00 38.22 ? 184 ASP A CA 1 ATOM 1099 C C . ASP A 1 143 ? 27.607 54.967 24.061 1.00 38.37 ? 184 ASP A C 1 ATOM 1100 O O . ASP A 1 143 ? 28.201 54.858 22.986 1.00 40.06 ? 184 ASP A O 1 ATOM 1101 C CB . ASP A 1 143 ? 28.118 53.342 25.923 1.00 37.61 ? 184 ASP A CB 1 ATOM 1102 C CG . ASP A 1 143 ? 28.965 53.037 27.141 1.00 36.80 ? 184 ASP A CG 1 ATOM 1103 O OD1 . ASP A 1 143 ? 30.169 53.426 27.183 1.00 37.65 ? 184 ASP A OD1 1 ATOM 1104 O OD2 . ASP A 1 143 ? 28.437 52.362 28.053 1.00 34.74 ? 184 ASP A OD2 1 ATOM 1105 N N . PHE A 1 144 ? 26.312 55.272 24.138 1.00 38.11 ? 185 PHE A N 1 ATOM 1106 C CA . PHE A 1 144 ? 25.527 55.545 22.932 1.00 37.83 ? 185 PHE A CA 1 ATOM 1107 C C . PHE A 1 144 ? 25.864 56.884 22.303 1.00 39.53 ? 185 PHE A C 1 ATOM 1108 O O . PHE A 1 144 ? 25.893 56.986 21.065 1.00 39.61 ? 185 PHE A O 1 ATOM 1109 C CB . PHE A 1 144 ? 24.031 55.428 23.217 1.00 36.87 ? 185 PHE A CB 1 ATOM 1110 C CG . PHE A 1 144 ? 23.550 54.003 23.233 1.00 34.99 ? 185 PHE A CG 1 ATOM 1111 C CD1 . PHE A 1 144 ? 23.304 53.368 24.436 1.00 35.40 ? 185 PHE A CD1 1 ATOM 1112 C CD2 . PHE A 1 144 ? 23.399 53.281 22.025 1.00 36.54 ? 185 PHE A CD2 1 ATOM 1113 C CE1 . PHE A 1 144 ? 22.849 52.041 24.465 1.00 35.71 ? 185 PHE A CE1 1 ATOM 1114 C CE2 . PHE A 1 144 ? 22.966 51.945 22.034 1.00 35.50 ? 185 PHE A CE2 1 ATOM 1115 C CZ . PHE A 1 144 ? 22.682 51.315 23.284 1.00 34.19 ? 185 PHE A CZ 1 ATOM 1116 N N . PHE A 1 145 ? 26.138 57.904 23.136 1.00 39.18 ? 186 PHE A N 1 ATOM 1117 C CA . PHE A 1 145 ? 26.734 59.168 22.609 1.00 41.09 ? 186 PHE A CA 1 ATOM 1118 C C . PHE A 1 145 ? 28.003 58.895 21.813 1.00 43.01 ? 186 PHE A C 1 ATOM 1119 O O . PHE A 1 145 ? 28.155 59.429 20.716 1.00 43.85 ? 186 PHE A O 1 ATOM 1120 C CB . PHE A 1 145 ? 27.101 60.198 23.700 1.00 40.78 ? 186 PHE A CB 1 ATOM 1121 C CG . PHE A 1 145 ? 25.909 60.914 24.338 1.00 40.42 ? 186 PHE A CG 1 ATOM 1122 C CD1 . PHE A 1 145 ? 24.674 60.995 23.689 1.00 41.42 ? 186 PHE A CD1 1 ATOM 1123 C CD2 . PHE A 1 145 ? 26.055 61.561 25.581 1.00 40.33 ? 186 PHE A CD2 1 ATOM 1124 C CE1 . PHE A 1 145 ? 23.581 61.669 24.276 1.00 41.76 ? 186 PHE A CE1 1 ATOM 1125 C CE2 . PHE A 1 145 ? 24.964 62.242 26.189 1.00 37.29 ? 186 PHE A CE2 1 ATOM 1126 C CZ . PHE A 1 145 ? 23.726 62.299 25.545 1.00 38.32 ? 186 PHE A CZ 1 ATOM 1127 N N . LYS A 1 146 ? 28.921 58.105 22.390 1.00 43.59 ? 187 LYS A N 1 ATOM 1128 C CA . LYS A 1 146 ? 30.206 57.757 21.730 1.00 45.55 ? 187 LYS A CA 1 ATOM 1129 C C . LYS A 1 146 ? 29.998 57.050 20.387 1.00 46.92 ? 187 LYS A C 1 ATOM 1130 O O . LYS A 1 146 ? 30.570 57.434 19.371 1.00 46.72 ? 187 LYS A O 1 ATOM 1131 C CB . LYS A 1 146 ? 31.092 56.905 22.661 1.00 45.46 ? 187 LYS A CB 1 ATOM 1132 C CG . LYS A 1 146 ? 32.387 56.334 22.014 1.00 49.23 ? 187 LYS A CG 1 ATOM 1133 C CD . LYS A 1 146 ? 33.361 57.426 21.561 1.00 54.03 ? 187 LYS A CD 1 ATOM 1134 C CE . LYS A 1 146 ? 34.606 57.490 22.440 1.00 57.43 ? 187 LYS A CE 1 ATOM 1135 N NZ . LYS A 1 146 ? 34.304 57.770 23.876 1.00 58.94 ? 187 LYS A NZ 1 ATOM 1136 N N . LEU A 1 147 ? 29.160 56.028 20.390 1.00 46.70 ? 188 LEU A N 1 ATOM 1137 C CA . LEU A 1 147 ? 28.805 55.305 19.177 1.00 48.60 ? 188 LEU A CA 1 ATOM 1138 C C . LEU A 1 147 ? 28.267 56.203 18.086 1.00 49.68 ? 188 LEU A C 1 ATOM 1139 O O . LEU A 1 147 ? 28.762 56.179 16.945 1.00 50.44 ? 188 LEU A O 1 ATOM 1140 C CB . LEU A 1 147 ? 27.717 54.291 19.537 1.00 48.33 ? 188 LEU A CB 1 ATOM 1141 C CG . LEU A 1 147 ? 28.247 52.968 20.047 1.00 49.14 ? 188 LEU A CG 1 ATOM 1142 C CD1 . LEU A 1 147 ? 27.126 52.195 20.707 1.00 49.54 ? 188 LEU A CD1 1 ATOM 1143 C CD2 . LEU A 1 147 ? 28.852 52.210 18.861 1.00 48.40 ? 188 LEU A CD2 1 ATOM 1144 N N . GLU A 1 148 ? 27.264 57.006 18.449 1.00 49.45 ? 189 GLU A N 1 ATOM 1145 C CA . GLU A 1 148 ? 26.488 57.747 17.470 1.00 51.45 ? 189 GLU A CA 1 ATOM 1146 C C . GLU A 1 148 ? 27.143 59.058 17.036 1.00 52.72 ? 189 GLU A C 1 ATOM 1147 O O . GLU A 1 148 ? 27.296 59.315 15.824 1.00 53.10 ? 189 GLU A O 1 ATOM 1148 C CB . GLU A 1 148 ? 25.040 57.912 17.947 1.00 51.81 ? 189 GLU A CB 1 ATOM 1149 C CG . GLU A 1 148 ? 24.229 56.614 17.702 1.00 55.78 ? 189 GLU A CG 1 ATOM 1150 C CD . GLU A 1 148 ? 23.159 56.333 18.748 1.00 59.67 ? 189 GLU A CD 1 ATOM 1151 O OE1 . GLU A 1 148 ? 23.521 55.828 19.836 1.00 59.93 ? 189 GLU A OE1 1 ATOM 1152 O OE2 . GLU A 1 148 ? 21.959 56.582 18.463 1.00 61.52 ? 189 GLU A OE2 1 ATOM 1153 N N . ARG A 1 149 ? 27.571 59.859 18.012 1.00 51.52 ? 190 ARG A N 1 ATOM 1154 C CA . ARG A 1 149 ? 28.133 61.190 17.733 1.00 52.48 ? 190 ARG A CA 1 ATOM 1155 C C . ARG A 1 149 ? 29.602 61.161 17.299 1.00 53.66 ? 190 ARG A C 1 ATOM 1156 O O . ARG A 1 149 ? 29.996 61.913 16.388 1.00 54.90 ? 190 ARG A O 1 ATOM 1157 C CB . ARG A 1 149 ? 27.943 62.124 18.943 1.00 50.90 ? 190 ARG A CB 1 ATOM 1158 C CG . ARG A 1 149 ? 26.501 62.333 19.342 1.00 47.93 ? 190 ARG A CG 1 ATOM 1159 C CD . ARG A 1 149 ? 26.394 62.967 20.720 1.00 44.21 ? 190 ARG A CD 1 ATOM 1160 N NE . ARG A 1 149 ? 25.004 63.315 21.008 1.00 44.20 ? 190 ARG A NE 1 ATOM 1161 C CZ . ARG A 1 149 ? 24.617 64.054 22.050 1.00 43.66 ? 190 ARG A CZ 1 ATOM 1162 N NH1 . ARG A 1 149 ? 25.527 64.514 22.894 1.00 41.76 ? 190 ARG A NH1 1 ATOM 1163 N NH2 . ARG A 1 149 ? 23.325 64.316 22.255 1.00 41.99 ? 190 ARG A NH2 1 ATOM 1164 N N . ASP A 1 150 ? 30.411 60.313 17.938 1.00 53.67 ? 191 ASP A N 1 ATOM 1165 C CA . ASP A 1 150 ? 31.855 60.253 17.627 1.00 56.09 ? 191 ASP A CA 1 ATOM 1166 C C . ASP A 1 150 ? 32.218 59.200 16.581 1.00 56.54 ? 191 ASP A C 1 ATOM 1167 O O . ASP A 1 150 ? 32.970 59.478 15.644 1.00 58.31 ? 191 ASP A O 1 ATOM 1168 C CB . ASP A 1 150 ? 32.689 60.054 18.900 1.00 55.75 ? 191 ASP A CB 1 ATOM 1169 C CG . ASP A 1 150 ? 32.415 61.122 19.947 1.00 58.46 ? 191 ASP A CG 1 ATOM 1170 O OD1 . ASP A 1 150 ? 32.233 62.301 19.554 1.00 62.09 ? 191 ASP A OD1 1 ATOM 1171 O OD2 . ASP A 1 150 ? 32.378 60.789 21.158 1.00 58.00 ? 191 ASP A OD2 1 ATOM 1172 N N . MET A 1 151 ? 31.686 57.994 16.739 1.00 55.71 ? 192 MET A N 1 ATOM 1173 C CA . MET A 1 151 ? 32.038 56.897 15.827 1.00 56.64 ? 192 MET A CA 1 ATOM 1174 C C . MET A 1 151 ? 31.140 56.824 14.592 1.00 57.01 ? 192 MET A C 1 ATOM 1175 O O . MET A 1 151 ? 31.445 56.081 13.648 1.00 57.24 ? 192 MET A O 1 ATOM 1176 C CB . MET A 1 151 ? 32.027 55.550 16.565 1.00 55.45 ? 192 MET A CB 1 ATOM 1177 C CG . MET A 1 151 ? 33.038 55.453 17.686 1.00 55.99 ? 192 MET A CG 1 ATOM 1178 S SD . MET A 1 151 ? 32.968 53.867 18.540 1.00 56.42 ? 192 MET A SD 1 ATOM 1179 C CE . MET A 1 151 ? 33.945 52.847 17.427 1.00 56.36 ? 192 MET A CE 1 ATOM 1180 N N . LYS A 1 152 ? 30.043 57.586 14.605 1.00 56.50 ? 193 LYS A N 1 ATOM 1181 C CA . LYS A 1 152 ? 29.041 57.555 13.530 1.00 57.45 ? 193 LYS A CA 1 ATOM 1182 C C . LYS A 1 152 ? 28.596 56.125 13.227 1.00 57.04 ? 193 LYS A C 1 ATOM 1183 O O . LYS A 1 152 ? 28.605 55.682 12.066 1.00 57.22 ? 193 LYS A O 1 ATOM 1184 C CB . LYS A 1 152 ? 29.558 58.256 12.251 1.00 59.71 ? 193 LYS A CB 1 ATOM 1185 C CG . LYS A 1 152 ? 29.097 59.706 12.080 1.00 62.89 ? 193 LYS A CG 1 ATOM 1186 C CD . LYS A 1 152 ? 29.657 60.643 13.149 1.00 65.06 ? 193 LYS A CD 1 ATOM 1187 C CE . LYS A 1 152 ? 29.590 62.094 12.686 1.00 67.67 ? 193 LYS A CE 1 ATOM 1188 N NZ . LYS A 1 152 ? 29.238 63.003 13.811 1.00 67.94 ? 193 LYS A NZ 1 ATOM 1189 N N . ILE A 1 153 ? 28.249 55.392 14.290 1.00 55.02 ? 194 ILE A N 1 ATOM 1190 C CA . ILE A 1 153 ? 27.717 54.040 14.147 1.00 55.40 ? 194 ILE A CA 1 ATOM 1191 C C . ILE A 1 153 ? 26.227 54.093 14.438 1.00 54.53 ? 194 ILE A C 1 ATOM 1192 O O . ILE A 1 153 ? 25.796 54.695 15.431 1.00 53.54 ? 194 ILE A O 1 ATOM 1193 C CB . ILE A 1 153 ? 28.515 52.982 14.976 1.00 55.06 ? 194 ILE A CB 1 ATOM 1194 C CG1 . ILE A 1 153 ? 29.812 52.625 14.221 1.00 58.12 ? 194 ILE A CG1 1 ATOM 1195 C CG2 . ILE A 1 153 ? 27.695 51.688 15.201 1.00 54.25 ? 194 ILE A CG2 1 ATOM 1196 C CD1 . ILE A 1 153 ? 31.000 52.244 15.108 1.00 58.81 ? 194 ILE A CD1 1 ATOM 1197 N N . ASN A 1 154 ? 25.448 53.523 13.523 1.00 55.51 ? 195 ASN A N 1 ATOM 1198 C CA . ASN A 1 154 ? 23.990 53.597 13.589 1.00 55.40 ? 195 ASN A CA 1 ATOM 1199 C C . ASN A 1 154 ? 23.414 52.275 14.110 1.00 53.49 ? 195 ASN A C 1 ATOM 1200 O O . ASN A 1 154 ? 23.575 51.217 13.473 1.00 53.55 ? 195 ASN A O 1 ATOM 1201 C CB . ASN A 1 154 ? 23.421 53.968 12.207 1.00 57.71 ? 195 ASN A CB 1 ATOM 1202 C CG . ASN A 1 154 ? 21.896 54.154 12.208 1.00 61.43 ? 195 ASN A CG 1 ATOM 1203 O OD1 . ASN A 1 154 ? 21.234 54.129 13.264 1.00 60.35 ? 195 ASN A OD1 1 ATOM 1204 N ND2 . ASN A 1 154 ? 21.334 54.340 10.998 1.00 69.51 ? 195 ASN A ND2 1 ATOM 1205 N N . CYS A 1 155 ? 22.769 52.340 15.278 1.00 50.54 ? 196 CYS A N 1 ATOM 1206 C CA . CYS A 1 155 ? 22.193 51.148 15.889 1.00 49.11 ? 196 CYS A CA 1 ATOM 1207 C C . CYS A 1 155 ? 20.851 50.730 15.327 1.00 48.81 ? 196 CYS A C 1 ATOM 1208 O O . CYS A 1 155 ? 20.352 49.660 15.682 1.00 48.08 ? 196 CYS A O 1 ATOM 1209 C CB . CYS A 1 155 ? 22.080 51.301 17.411 1.00 47.74 ? 196 CYS A CB 1 ATOM 1210 S SG . CYS A 1 155 ? 23.670 51.153 18.161 1.00 48.56 ? 196 CYS A SG 1 ATOM 1211 N N . SER A 1 156 ? 20.266 51.544 14.448 1.00 49.08 ? 197 SER A N 1 ATOM 1212 C CA . SER A 1 156 ? 18.908 51.258 13.984 1.00 49.51 ? 197 SER A CA 1 ATOM 1213 C C . SER A 1 156 ? 18.786 49.928 13.217 1.00 49.54 ? 197 SER A C 1 ATOM 1214 O O . SER A 1 156 ? 19.508 49.680 12.246 1.00 51.19 ? 197 SER A O 1 ATOM 1215 C CB . SER A 1 156 ? 18.306 52.459 13.232 1.00 50.14 ? 197 SER A CB 1 ATOM 1216 O OG . SER A 1 156 ? 17.365 52.055 12.245 1.00 53.17 ? 197 SER A OG 1 ATOM 1217 N N . GLY A 1 157 ? 17.883 49.069 13.689 1.00 48.46 ? 198 GLY A N 1 ATOM 1218 C CA . GLY A 1 157 ? 17.630 47.768 13.053 1.00 47.51 ? 198 GLY A CA 1 ATOM 1219 C C . GLY A 1 157 ? 18.683 46.723 13.397 1.00 46.84 ? 198 GLY A C 1 ATOM 1220 O O . GLY A 1 157 ? 18.681 45.629 12.822 1.00 47.04 ? 198 GLY A O 1 ATOM 1221 N N . LYS A 1 158 ? 19.587 47.053 14.325 1.00 45.15 ? 199 LYS A N 1 ATOM 1222 C CA . LYS A 1 158 ? 20.648 46.112 14.719 1.00 44.97 ? 199 LYS A CA 1 ATOM 1223 C C . LYS A 1 158 ? 20.274 45.407 16.020 1.00 43.57 ? 199 LYS A C 1 ATOM 1224 O O . LYS A 1 158 ? 19.449 45.916 16.795 1.00 41.95 ? 199 LYS A O 1 ATOM 1225 C CB . LYS A 1 158 ? 21.998 46.823 14.912 1.00 44.99 ? 199 LYS A CB 1 ATOM 1226 C CG . LYS A 1 158 ? 22.459 47.720 13.755 1.00 48.39 ? 199 LYS A CG 1 ATOM 1227 C CD . LYS A 1 158 ? 22.585 46.948 12.471 1.00 51.01 ? 199 LYS A CD 1 ATOM 1228 C CE . LYS A 1 158 ? 22.945 47.891 11.324 1.00 55.02 ? 199 LYS A CE 1 ATOM 1229 N NZ . LYS A 1 158 ? 22.324 47.394 10.081 1.00 56.13 ? 199 LYS A NZ 1 ATOM 1230 N N . ILE A 1 159 ? 20.883 44.252 16.273 1.00 43.23 ? 200 ILE A N 1 ATOM 1231 C CA . ILE A 1 159 ? 20.792 43.658 17.621 1.00 42.31 ? 200 ILE A CA 1 ATOM 1232 C C . ILE A 1 159 ? 21.989 44.152 18.429 1.00 41.50 ? 200 ILE A C 1 ATOM 1233 O O . ILE A 1 159 ? 23.150 44.028 17.999 1.00 42.38 ? 200 ILE A O 1 ATOM 1234 C CB . ILE A 1 159 ? 20.743 42.129 17.575 1.00 42.98 ? 200 ILE A CB 1 ATOM 1235 C CG1 . ILE A 1 159 ? 19.452 41.674 16.879 1.00 43.91 ? 200 ILE A CG1 1 ATOM 1236 C CG2 . ILE A 1 159 ? 20.788 41.572 19.013 1.00 41.96 ? 200 ILE A CG2 1 ATOM 1237 C CD1 . ILE A 1 159 ? 19.407 40.187 16.556 1.00 43.89 ? 200 ILE A CD1 1 ATOM 1238 N N . VAL A 1 160 ? 21.723 44.756 19.574 1.00 39.61 ? 201 VAL A N 1 ATOM 1239 C CA . VAL A 1 160 ? 22.809 45.272 20.375 1.00 38.98 ? 201 VAL A CA 1 ATOM 1240 C C . VAL A 1 160 ? 23.228 44.217 21.414 1.00 38.91 ? 201 VAL A C 1 ATOM 1241 O O . VAL A 1 160 ? 22.371 43.533 21.992 1.00 37.37 ? 201 VAL A O 1 ATOM 1242 C CB . VAL A 1 160 ? 22.450 46.692 20.974 1.00 39.32 ? 201 VAL A CB 1 ATOM 1243 C CG1 A VAL A 1 160 ? 22.246 47.721 19.857 0.50 39.12 ? 201 VAL A CG1 1 ATOM 1244 C CG1 B VAL A 1 160 ? 22.727 46.809 22.473 0.50 37.42 ? 201 VAL A CG1 1 ATOM 1245 C CG2 A VAL A 1 160 ? 21.236 46.634 21.860 0.50 35.88 ? 201 VAL A CG2 1 ATOM 1246 C CG2 B VAL A 1 160 ? 23.090 47.801 20.140 0.50 39.99 ? 201 VAL A CG2 1 ATOM 1247 N N . ILE A 1 161 ? 24.534 44.031 21.566 1.00 37.59 ? 202 ILE A N 1 ATOM 1248 C CA . ILE A 1 161 ? 25.042 43.235 22.660 1.00 35.76 ? 202 ILE A CA 1 ATOM 1249 C C . ILE A 1 161 ? 25.749 44.153 23.644 1.00 35.81 ? 202 ILE A C 1 ATOM 1250 O O . ILE A 1 161 ? 26.590 44.978 23.274 1.00 35.72 ? 202 ILE A O 1 ATOM 1251 C CB . ILE A 1 161 ? 25.925 42.046 22.174 1.00 36.79 ? 202 ILE A CB 1 ATOM 1252 C CG1 . ILE A 1 161 ? 26.377 41.183 23.370 1.00 35.66 ? 202 ILE A CG1 1 ATOM 1253 C CG2 . ILE A 1 161 ? 27.083 42.523 21.201 1.00 35.19 ? 202 ILE A CG2 1 ATOM 1254 C CD1 . ILE A 1 161 ? 26.785 39.736 22.928 1.00 37.71 ? 202 ILE A CD1 1 ATOM 1255 N N . ALA A 1 162 ? 25.359 44.043 24.908 1.00 32.91 ? 203 ALA A N 1 ATOM 1256 C CA . ALA A 1 162 ? 25.900 44.912 25.905 1.00 33.07 ? 203 ALA A CA 1 ATOM 1257 C C . ALA A 1 162 ? 26.365 44.065 27.046 1.00 32.57 ? 203 ALA A C 1 ATOM 1258 O O . ALA A 1 162 ? 25.712 43.074 27.387 1.00 33.83 ? 203 ALA A O 1 ATOM 1259 C CB . ALA A 1 162 ? 24.807 45.923 26.397 1.00 31.20 ? 203 ALA A CB 1 ATOM 1260 N N . ARG A 1 163 ? 27.443 44.498 27.686 1.00 33.93 ? 204 ARG A N 1 ATOM 1261 C CA . ARG A 1 163 ? 27.827 43.910 28.958 1.00 33.62 ? 204 ARG A CA 1 ATOM 1262 C C . ARG A 1 163 ? 27.098 44.506 30.130 1.00 32.86 ? 204 ARG A C 1 ATOM 1263 O O . ARG A 1 163 ? 26.894 45.733 30.224 1.00 31.88 ? 204 ARG A O 1 ATOM 1264 C CB . ARG A 1 163 ? 29.340 43.927 29.183 1.00 35.21 ? 204 ARG A CB 1 ATOM 1265 C CG . ARG A 1 163 ? 30.033 45.237 28.973 1.00 36.01 ? 204 ARG A CG 1 ATOM 1266 C CD . ARG A 1 163 ? 31.486 45.063 29.396 1.00 40.73 ? 204 ARG A CD 1 ATOM 1267 N NE . ARG A 1 163 ? 32.318 46.209 29.058 1.00 40.89 ? 204 ARG A NE 1 ATOM 1268 C CZ . ARG A 1 163 ? 33.535 46.407 29.558 1.00 44.31 ? 204 ARG A CZ 1 ATOM 1269 N NH1 . ARG A 1 163 ? 34.034 45.566 30.467 1.00 39.65 ? 204 ARG A NH1 1 ATOM 1270 N NH2 . ARG A 1 163 ? 34.232 47.475 29.180 1.00 40.87 ? 204 ARG A NH2 1 ATOM 1271 N N . TYR A 1 164 ? 26.669 43.620 31.023 1.00 30.83 ? 205 TYR A N 1 ATOM 1272 C CA . TYR A 1 164 ? 26.107 44.063 32.289 1.00 30.27 ? 205 TYR A CA 1 ATOM 1273 C C . TYR A 1 164 ? 27.133 44.878 33.077 1.00 30.85 ? 205 TYR A C 1 ATOM 1274 O O . TYR A 1 164 ? 28.356 44.672 32.963 1.00 31.69 ? 205 TYR A O 1 ATOM 1275 C CB . TYR A 1 164 ? 25.779 42.834 33.107 1.00 29.05 ? 205 TYR A CB 1 ATOM 1276 C CG . TYR A 1 164 ? 24.429 42.188 32.937 1.00 28.09 ? 205 TYR A CG 1 ATOM 1277 C CD1 . TYR A 1 164 ? 24.312 40.813 32.671 1.00 26.44 ? 205 TYR A CD1 1 ATOM 1278 C CD2 . TYR A 1 164 ? 23.267 42.928 33.144 1.00 25.12 ? 205 TYR A CD2 1 ATOM 1279 C CE1 . TYR A 1 164 ? 23.043 40.192 32.633 1.00 24.61 ? 205 TYR A CE1 1 ATOM 1280 C CE2 . TYR A 1 164 ? 22.029 42.336 33.102 1.00 26.56 ? 205 TYR A CE2 1 ATOM 1281 C CZ . TYR A 1 164 ? 21.903 40.987 32.853 1.00 25.71 ? 205 TYR A CZ 1 ATOM 1282 O OH . TYR A 1 164 ? 20.645 40.443 32.855 1.00 26.16 ? 205 TYR A OH 1 ATOM 1283 N N . GLY A 1 165 ? 26.648 45.802 33.899 1.00 30.08 ? 206 GLY A N 1 ATOM 1284 C CA . GLY A 1 165 ? 27.532 46.523 34.840 1.00 31.71 ? 206 GLY A CA 1 ATOM 1285 C C . GLY A 1 165 ? 27.253 48.016 34.810 1.00 32.44 ? 206 GLY A C 1 ATOM 1286 O O . GLY A 1 165 ? 26.650 48.513 33.843 1.00 31.85 ? 206 GLY A O 1 ATOM 1287 N N . LYS A 1 166 ? 27.707 48.709 35.862 1.00 32.80 ? 207 LYS A N 1 ATOM 1288 C CA . LYS A 1 166 ? 27.734 50.198 35.908 1.00 32.64 ? 207 LYS A CA 1 ATOM 1289 C C . LYS A 1 166 ? 26.391 50.843 36.147 1.00 32.03 ? 207 LYS A C 1 ATOM 1290 O O . LYS A 1 166 ? 26.289 51.777 36.973 1.00 31.70 ? 207 LYS A O 1 ATOM 1291 C CB . LYS A 1 166 ? 28.341 50.832 34.635 1.00 33.23 ? 207 LYS A CB 1 ATOM 1292 C CG . LYS A 1 166 ? 29.780 50.349 34.259 1.00 36.53 ? 207 LYS A CG 1 ATOM 1293 C CD . LYS A 1 166 ? 30.783 50.574 35.387 1.00 39.65 ? 207 LYS A CD 1 ATOM 1294 C CE . LYS A 1 166 ? 32.214 50.376 34.842 1.00 43.36 ? 207 LYS A CE 1 ATOM 1295 N NZ . LYS A 1 166 ? 33.229 50.491 35.923 1.00 46.73 ? 207 LYS A NZ 1 ATOM 1296 N N . VAL A 1 167 ? 25.365 50.397 35.417 1.00 30.90 ? 208 VAL A N 1 ATOM 1297 C CA . VAL A 1 167 ? 23.996 50.982 35.577 1.00 28.71 ? 208 VAL A CA 1 ATOM 1298 C C . VAL A 1 167 ? 22.930 49.891 35.533 1.00 28.78 ? 208 VAL A C 1 ATOM 1299 O O . VAL A 1 167 ? 23.166 48.782 35.019 1.00 28.75 ? 208 VAL A O 1 ATOM 1300 C CB . VAL A 1 167 ? 23.680 52.084 34.477 1.00 29.07 ? 208 VAL A CB 1 ATOM 1301 C CG1 . VAL A 1 167 ? 24.806 53.158 34.404 1.00 29.48 ? 208 VAL A CG1 1 ATOM 1302 C CG2 . VAL A 1 167 ? 23.530 51.467 33.087 1.00 29.13 ? 208 VAL A CG2 1 ATOM 1303 N N . PHE A 1 168 ? 21.728 50.233 35.994 1.00 26.21 ? 209 PHE A N 1 ATOM 1304 C CA . PHE A 1 168 ? 20.602 49.314 35.965 1.00 26.00 ? 209 PHE A CA 1 ATOM 1305 C C . PHE A 1 168 ? 20.319 48.822 34.540 1.00 26.48 ? 209 PHE A C 1 ATOM 1306 O O . PHE A 1 168 ? 20.328 49.585 33.574 1.00 27.61 ? 209 PHE A O 1 ATOM 1307 C CB . PHE A 1 168 ? 19.362 50.051 36.506 1.00 25.23 ? 209 PHE A CB 1 ATOM 1308 C CG . PHE A 1 168 ? 18.073 49.242 36.411 1.00 26.37 ? 209 PHE A CG 1 ATOM 1309 C CD1 . PHE A 1 168 ? 17.979 47.979 36.998 1.00 26.26 ? 209 PHE A CD1 1 ATOM 1310 C CD2 . PHE A 1 168 ? 16.950 49.780 35.733 1.00 29.04 ? 209 PHE A CD2 1 ATOM 1311 C CE1 . PHE A 1 168 ? 16.767 47.235 36.928 1.00 29.46 ? 209 PHE A CE1 1 ATOM 1312 C CE2 . PHE A 1 168 ? 15.720 49.046 35.652 1.00 30.90 ? 209 PHE A CE2 1 ATOM 1313 C CZ . PHE A 1 168 ? 15.657 47.747 36.236 1.00 28.26 ? 209 PHE A CZ 1 ATOM 1314 N N . ARG A 1 169 ? 20.049 47.511 34.391 1.00 26.59 ? 210 ARG A N 1 ATOM 1315 C CA . ARG A 1 169 ? 19.843 46.937 33.034 1.00 26.53 ? 210 ARG A CA 1 ATOM 1316 C C . ARG A 1 169 ? 18.635 47.473 32.281 1.00 27.06 ? 210 ARG A C 1 ATOM 1317 O O . ARG A 1 169 ? 18.607 47.464 31.064 1.00 27.92 ? 210 ARG A O 1 ATOM 1318 C CB . ARG A 1 169 ? 19.733 45.398 33.116 1.00 26.23 ? 210 ARG A CB 1 ATOM 1319 C CG . ARG A 1 169 ? 18.448 44.936 33.911 1.00 24.06 ? 210 ARG A CG 1 ATOM 1320 C CD . ARG A 1 169 ? 18.476 43.382 34.110 1.00 26.49 ? 210 ARG A CD 1 ATOM 1321 N NE . ARG A 1 169 ? 19.289 42.966 35.266 1.00 23.77 ? 210 ARG A NE 1 ATOM 1322 C CZ . ARG A 1 169 ? 18.929 43.148 36.545 1.00 24.36 ? 210 ARG A CZ 1 ATOM 1323 N NH1 . ARG A 1 169 ? 17.783 43.739 36.844 1.00 23.95 ? 210 ARG A NH1 1 ATOM 1324 N NH2 . ARG A 1 169 ? 19.723 42.762 37.553 1.00 24.07 ? 210 ARG A NH2 1 ATOM 1325 N N . GLY A 1 170 ? 17.618 47.925 33.012 1.00 26.62 ? 211 GLY A N 1 ATOM 1326 C CA . GLY A 1 170 ? 16.470 48.559 32.375 1.00 28.55 ? 211 GLY A CA 1 ATOM 1327 C C . GLY A 1 170 ? 16.861 49.863 31.674 1.00 28.70 ? 211 GLY A C 1 ATOM 1328 O O . GLY A 1 170 ? 16.289 50.161 30.635 1.00 29.22 ? 211 GLY A O 1 ATOM 1329 N N . ASN A 1 171 ? 17.790 50.632 32.263 1.00 28.62 ? 212 ASN A N 1 ATOM 1330 C CA . ASN A 1 171 ? 18.331 51.813 31.564 1.00 29.20 ? 212 ASN A CA 1 ATOM 1331 C C . ASN A 1 171 ? 19.073 51.430 30.316 1.00 30.23 ? 212 ASN A C 1 ATOM 1332 O O . ASN A 1 171 ? 18.950 52.124 29.284 1.00 31.71 ? 212 ASN A O 1 ATOM 1333 C CB . ASN A 1 171 ? 19.250 52.638 32.446 1.00 28.94 ? 212 ASN A CB 1 ATOM 1334 C CG . ASN A 1 171 ? 18.494 53.305 33.576 1.00 29.22 ? 212 ASN A CG 1 ATOM 1335 O OD1 . ASN A 1 171 ? 18.470 52.806 34.723 1.00 29.72 ? 212 ASN A OD1 1 ATOM 1336 N ND2 . ASN A 1 171 ? 17.869 54.442 33.271 1.00 30.45 ? 212 ASN A ND2 1 ATOM 1337 N N . LYS A 1 172 ? 19.835 50.321 30.365 1.00 29.69 ? 213 LYS A N 1 ATOM 1338 C CA . LYS A 1 172 ? 20.486 49.837 29.119 1.00 30.73 ? 213 LYS A CA 1 ATOM 1339 C C . LYS A 1 172 ? 19.493 49.569 27.999 1.00 30.75 ? 213 LYS A C 1 ATOM 1340 O O . LYS A 1 172 ? 19.749 49.902 26.817 1.00 31.17 ? 213 LYS A O 1 ATOM 1341 C CB . LYS A 1 172 ? 21.320 48.542 29.348 1.00 29.48 ? 213 LYS A CB 1 ATOM 1342 C CG . LYS A 1 172 ? 22.244 48.578 30.551 1.00 29.58 ? 213 LYS A CG 1 ATOM 1343 C CD . LYS A 1 172 ? 23.005 47.231 30.696 1.00 29.72 ? 213 LYS A CD 1 ATOM 1344 C CE . LYS A 1 172 ? 23.929 47.258 31.888 1.00 29.92 ? 213 LYS A CE 1 ATOM 1345 N NZ . LYS A 1 172 ? 25.365 47.592 31.521 1.00 30.91 ? 213 LYS A NZ 1 ATOM 1346 N N . VAL A 1 173 ? 18.385 48.905 28.345 1.00 30.09 ? 214 VAL A N 1 ATOM 1347 C CA . VAL A 1 173 ? 17.391 48.500 27.354 1.00 29.38 ? 214 VAL A CA 1 ATOM 1348 C C . VAL A 1 173 ? 16.645 49.765 26.839 1.00 29.94 ? 214 VAL A C 1 ATOM 1349 O O . VAL A 1 173 ? 16.360 49.858 25.663 1.00 31.02 ? 214 VAL A O 1 ATOM 1350 C CB . VAL A 1 173 ? 16.385 47.435 27.943 1.00 29.88 ? 214 VAL A CB 1 ATOM 1351 C CG1 . VAL A 1 173 ? 15.199 47.182 26.976 1.00 30.65 ? 214 VAL A CG1 1 ATOM 1352 C CG2 . VAL A 1 173 ? 17.110 46.113 28.202 1.00 29.02 ? 214 VAL A CG2 1 ATOM 1353 N N . LYS A 1 174 ? 16.339 50.715 27.726 1.00 29.31 ? 215 LYS A N 1 ATOM 1354 C CA . LYS A 1 174 ? 15.709 51.975 27.313 1.00 30.94 ? 215 LYS A CA 1 ATOM 1355 C C . LYS A 1 174 ? 16.641 52.673 26.318 1.00 31.88 ? 215 LYS A C 1 ATOM 1356 O O . LYS A 1 174 ? 16.191 53.094 25.242 1.00 33.39 ? 215 LYS A O 1 ATOM 1357 C CB . LYS A 1 174 ? 15.428 52.879 28.509 1.00 30.82 ? 215 LYS A CB 1 ATOM 1358 C CG . LYS A 1 174 ? 14.899 54.242 28.075 1.00 33.70 ? 215 LYS A CG 1 ATOM 1359 C CD . LYS A 1 174 ? 14.391 55.056 29.242 1.00 38.32 ? 215 LYS A CD 1 ATOM 1360 C CE . LYS A 1 174 ? 14.065 56.491 28.801 1.00 42.65 ? 215 LYS A CE 1 ATOM 1361 N NZ . LYS A 1 174 ? 15.328 57.286 28.879 1.00 44.40 ? 215 LYS A NZ 1 ATOM 1362 N N . ASN A 1 175 ? 17.941 52.732 26.657 1.00 32.50 ? 216 ASN A N 1 ATOM 1363 C CA . ASN A 1 175 ? 18.924 53.432 25.816 1.00 31.77 ? 216 ASN A CA 1 ATOM 1364 C C . ASN A 1 175 ? 19.025 52.737 24.466 1.00 32.36 ? 216 ASN A C 1 ATOM 1365 O O . ASN A 1 175 ? 19.094 53.423 23.448 1.00 34.33 ? 216 ASN A O 1 ATOM 1366 C CB . ASN A 1 175 ? 20.313 53.492 26.468 1.00 31.13 ? 216 ASN A CB 1 ATOM 1367 C CG . ASN A 1 175 ? 20.312 54.280 27.779 1.00 33.09 ? 216 ASN A CG 1 ATOM 1368 O OD1 . ASN A 1 175 ? 19.383 55.055 28.060 1.00 34.82 ? 216 ASN A OD1 1 ATOM 1369 N ND2 . ASN A 1 175 ? 21.380 54.117 28.572 1.00 33.05 ? 216 ASN A ND2 1 ATOM 1370 N N . ALA A 1 176 ? 19.033 51.400 24.465 1.00 32.79 ? 217 ALA A N 1 ATOM 1371 C CA . ALA A 1 176 ? 19.052 50.611 23.203 1.00 34.30 ? 217 ALA A CA 1 ATOM 1372 C C . ALA A 1 176 ? 17.817 50.869 22.366 1.00 35.91 ? 217 ALA A C 1 ATOM 1373 O O . ALA A 1 176 ? 17.908 51.023 21.152 1.00 38.03 ? 217 ALA A O 1 ATOM 1374 C CB . ALA A 1 176 ? 19.215 49.096 23.472 1.00 33.71 ? 217 ALA A CB 1 ATOM 1375 N N . GLN A 1 177 ? 16.655 50.924 23.009 1.00 36.67 ? 218 GLN A N 1 ATOM 1376 C CA . GLN A 1 177 ? 15.401 51.148 22.278 1.00 38.48 ? 218 GLN A CA 1 ATOM 1377 C C . GLN A 1 177 ? 15.418 52.465 21.527 1.00 39.44 ? 218 GLN A C 1 ATOM 1378 O O . GLN A 1 177 ? 15.029 52.541 20.358 1.00 38.40 ? 218 GLN A O 1 ATOM 1379 C CB . GLN A 1 177 ? 14.214 51.156 23.254 1.00 39.04 ? 218 GLN A CB 1 ATOM 1380 C CG . GLN A 1 177 ? 13.767 49.772 23.586 1.00 42.89 ? 218 GLN A CG 1 ATOM 1381 C CD . GLN A 1 177 ? 12.439 49.699 24.358 1.00 47.03 ? 218 GLN A CD 1 ATOM 1382 O OE1 . GLN A 1 177 ? 12.155 48.681 24.969 1.00 48.75 ? 218 GLN A OE1 1 ATOM 1383 N NE2 . GLN A 1 177 ? 11.617 50.748 24.284 1.00 50.26 ? 218 GLN A NE2 1 ATOM 1384 N N . LEU A 1 178 ? 15.849 53.510 22.236 1.00 39.22 ? 219 LEU A N 1 ATOM 1385 C CA . LEU A 1 178 ? 15.859 54.865 21.686 1.00 40.35 ? 219 LEU A CA 1 ATOM 1386 C C . LEU A 1 178 ? 16.949 55.054 20.648 1.00 41.13 ? 219 LEU A C 1 ATOM 1387 O O . LEU A 1 178 ? 16.832 55.914 19.762 1.00 42.33 ? 219 LEU A O 1 ATOM 1388 C CB . LEU A 1 178 ? 15.941 55.905 22.817 1.00 40.23 ? 219 LEU A CB 1 ATOM 1389 C CG . LEU A 1 178 ? 14.646 55.939 23.650 1.00 42.06 ? 219 LEU A CG 1 ATOM 1390 C CD1 . LEU A 1 178 ? 14.790 56.793 24.911 1.00 45.86 ? 219 LEU A CD1 1 ATOM 1391 C CD2 . LEU A 1 178 ? 13.386 56.350 22.859 1.00 46.70 ? 219 LEU A CD2 1 ATOM 1392 N N . ALA A 1 179 ? 17.997 54.230 20.718 1.00 40.46 ? 220 ALA A N 1 ATOM 1393 C CA . ALA A 1 179 ? 18.972 54.129 19.614 1.00 41.00 ? 220 ALA A CA 1 ATOM 1394 C C . ALA A 1 179 ? 18.436 53.376 18.400 1.00 41.90 ? 220 ALA A C 1 ATOM 1395 O O . ALA A 1 179 ? 19.124 53.298 17.385 1.00 42.31 ? 220 ALA A O 1 ATOM 1396 C CB . ALA A 1 179 ? 20.260 53.473 20.098 1.00 40.48 ? 220 ALA A CB 1 ATOM 1397 N N . GLY A 1 180 ? 17.233 52.807 18.483 1.00 40.74 ? 221 GLY A N 1 ATOM 1398 C CA . GLY A 1 180 ? 16.696 52.117 17.294 1.00 40.78 ? 221 GLY A CA 1 ATOM 1399 C C . GLY A 1 180 ? 16.937 50.623 17.190 1.00 40.90 ? 221 GLY A C 1 ATOM 1400 O O . GLY A 1 180 ? 16.590 50.014 16.172 1.00 41.14 ? 221 GLY A O 1 ATOM 1401 N N . ALA A 1 181 ? 17.485 50.008 18.253 1.00 39.81 ? 222 ALA A N 1 ATOM 1402 C CA . ALA A 1 181 ? 17.853 48.571 18.214 1.00 40.42 ? 222 ALA A CA 1 ATOM 1403 C C . ALA A 1 181 ? 16.607 47.707 18.056 1.00 40.01 ? 222 ALA A C 1 ATOM 1404 O O . ALA A 1 181 ? 15.522 48.112 18.509 1.00 39.49 ? 222 ALA A O 1 ATOM 1405 C CB . ALA A 1 181 ? 18.620 48.177 19.502 1.00 39.30 ? 222 ALA A CB 1 ATOM 1406 N N . LYS A 1 182 ? 16.729 46.535 17.423 1.00 39.15 ? 223 LYS A N 1 ATOM 1407 C CA . LYS A 1 182 ? 15.583 45.624 17.430 1.00 39.78 ? 223 LYS A CA 1 ATOM 1408 C C . LYS A 1 182 ? 15.660 44.481 18.464 1.00 39.21 ? 223 LYS A C 1 ATOM 1409 O O . LYS A 1 182 ? 14.782 43.610 18.504 1.00 38.97 ? 223 LYS A O 1 ATOM 1410 C CB . LYS A 1 182 ? 15.268 45.074 16.049 1.00 42.00 ? 223 LYS A CB 1 ATOM 1411 C CG . LYS A 1 182 ? 16.219 44.052 15.507 1.00 44.33 ? 223 LYS A CG 1 ATOM 1412 C CD . LYS A 1 182 ? 15.807 43.727 14.085 1.00 48.28 ? 223 LYS A CD 1 ATOM 1413 C CE . LYS A 1 182 ? 16.926 43.095 13.356 1.00 51.05 ? 223 LYS A CE 1 ATOM 1414 N NZ . LYS A 1 182 ? 16.585 42.958 11.916 1.00 53.91 ? 223 LYS A NZ 1 ATOM 1415 N N . GLY A 1 183 ? 16.721 44.471 19.263 1.00 37.74 ? 224 GLY A N 1 ATOM 1416 C CA . GLY A 1 183 ? 16.927 43.384 20.230 1.00 37.31 ? 224 GLY A CA 1 ATOM 1417 C C . GLY A 1 183 ? 18.122 43.726 21.091 1.00 36.31 ? 224 GLY A C 1 ATOM 1418 O O . GLY A 1 183 ? 19.008 44.470 20.639 1.00 36.76 ? 224 GLY A O 1 ATOM 1419 N N . VAL A 1 184 ? 18.156 43.196 22.321 1.00 34.54 ? 225 VAL A N 1 ATOM 1420 C CA . VAL A 1 184 ? 19.280 43.392 23.211 1.00 33.41 ? 225 VAL A CA 1 ATOM 1421 C C . VAL A 1 184 ? 19.710 42.040 23.796 1.00 34.24 ? 225 VAL A C 1 ATOM 1422 O O . VAL A 1 184 ? 18.889 41.279 24.318 1.00 32.72 ? 225 VAL A O 1 ATOM 1423 C CB . VAL A 1 184 ? 18.951 44.289 24.417 1.00 32.50 ? 225 VAL A CB 1 ATOM 1424 C CG1 . VAL A 1 184 ? 20.211 44.532 25.238 1.00 30.45 ? 225 VAL A CG1 1 ATOM 1425 C CG2 . VAL A 1 184 ? 18.353 45.619 23.945 1.00 33.64 ? 225 VAL A CG2 1 ATOM 1426 N N . ILE A 1 185 ? 21.007 41.766 23.699 1.00 33.01 ? 226 ILE A N 1 ATOM 1427 C CA . ILE A 1 185 ? 21.593 40.617 24.376 1.00 32.23 ? 226 ILE A CA 1 ATOM 1428 C C . ILE A 1 185 ? 22.451 41.170 25.487 1.00 31.53 ? 226 ILE A C 1 ATOM 1429 O O . ILE A 1 185 ? 23.307 42.022 25.236 1.00 32.37 ? 226 ILE A O 1 ATOM 1430 C CB . ILE A 1 185 ? 22.440 39.784 23.372 1.00 33.00 ? 226 ILE A CB 1 ATOM 1431 C CG1 . ILE A 1 185 ? 21.529 39.166 22.304 1.00 33.35 ? 226 ILE A CG1 1 ATOM 1432 C CG2 . ILE A 1 185 ? 23.243 38.694 24.101 1.00 33.47 ? 226 ILE A CG2 1 ATOM 1433 C CD1 . ILE A 1 185 ? 22.281 38.670 21.071 1.00 32.52 ? 226 ILE A CD1 1 ATOM 1434 N N . LEU A 1 186 ? 22.185 40.736 26.722 1.00 29.71 ? 227 LEU A N 1 ATOM 1435 C CA . LEU A 1 186 ? 22.947 41.152 27.909 1.00 29.28 ? 227 LEU A CA 1 ATOM 1436 C C . LEU A 1 186 ? 23.835 39.984 28.325 1.00 28.93 ? 227 LEU A C 1 ATOM 1437 O O . LEU A 1 186 ? 23.387 38.842 28.260 1.00 29.37 ? 227 LEU A O 1 ATOM 1438 C CB . LEU A 1 186 ? 21.998 41.500 29.054 1.00 27.11 ? 227 LEU A CB 1 ATOM 1439 C CG . LEU A 1 186 ? 21.049 42.654 28.728 1.00 27.90 ? 227 LEU A CG 1 ATOM 1440 C CD1 . LEU A 1 186 ? 19.922 42.671 29.795 1.00 27.70 ? 227 LEU A CD1 1 ATOM 1441 C CD2 . LEU A 1 186 ? 21.787 43.983 28.720 1.00 30.80 ? 227 LEU A CD2 1 ATOM 1442 N N . TYR A 1 187 ? 25.088 40.270 28.690 1.00 29.11 ? 228 TYR A N 1 ATOM 1443 C CA . TYR A 1 187 ? 25.998 39.209 29.116 1.00 29.57 ? 228 TYR A CA 1 ATOM 1444 C C . TYR A 1 187 ? 26.897 39.699 30.221 1.00 30.28 ? 228 TYR A C 1 ATOM 1445 O O . TYR A 1 187 ? 27.134 40.901 30.362 1.00 29.72 ? 228 TYR A O 1 ATOM 1446 C CB . TYR A 1 187 ? 26.828 38.625 27.925 1.00 30.23 ? 228 TYR A CB 1 ATOM 1447 C CG . TYR A 1 187 ? 28.079 39.442 27.603 1.00 31.46 ? 228 TYR A CG 1 ATOM 1448 C CD1 . TYR A 1 187 ? 29.310 39.108 28.164 1.00 32.04 ? 228 TYR A CD1 1 ATOM 1449 C CD2 . TYR A 1 187 ? 27.996 40.594 26.803 1.00 33.09 ? 228 TYR A CD2 1 ATOM 1450 C CE1 . TYR A 1 187 ? 30.454 39.866 27.907 1.00 32.76 ? 228 TYR A CE1 1 ATOM 1451 C CE2 . TYR A 1 187 ? 29.156 41.382 26.530 1.00 32.66 ? 228 TYR A CE2 1 ATOM 1452 C CZ . TYR A 1 187 ? 30.359 41.005 27.099 1.00 34.77 ? 228 TYR A CZ 1 ATOM 1453 O OH . TYR A 1 187 ? 31.492 41.763 26.881 1.00 36.73 ? 228 TYR A OH 1 ATOM 1454 N N . SER A 1 188 ? 27.415 38.758 31.006 1.00 29.87 ? 229 SER A N 1 ATOM 1455 C CA . SER A 1 188 ? 28.317 39.077 32.096 1.00 29.18 ? 229 SER A CA 1 ATOM 1456 C C . SER A 1 188 ? 29.773 38.934 31.664 1.00 29.60 ? 229 SER A C 1 ATOM 1457 O O . SER A 1 188 ? 30.221 37.825 31.387 1.00 29.76 ? 229 SER A O 1 ATOM 1458 C CB . SER A 1 188 ? 27.993 38.161 33.290 1.00 28.41 ? 229 SER A CB 1 ATOM 1459 O OG . SER A 1 188 ? 26.673 38.435 33.779 1.00 29.02 ? 229 SER A OG 1 ATOM 1460 N N . ASP A 1 189 ? 30.504 40.047 31.587 1.00 29.91 ? 230 ASP A N 1 ATOM 1461 C CA . ASP A 1 189 ? 31.920 39.970 31.167 1.00 31.85 ? 230 ASP A CA 1 ATOM 1462 C C . ASP A 1 189 ? 32.780 39.629 32.390 1.00 32.34 ? 230 ASP A C 1 ATOM 1463 O O . ASP A 1 189 ? 32.550 40.141 33.485 1.00 32.40 ? 230 ASP A O 1 ATOM 1464 C CB . ASP A 1 189 ? 32.383 41.277 30.509 1.00 32.05 ? 230 ASP A CB 1 ATOM 1465 C CG . ASP A 1 189 ? 33.673 41.108 29.702 1.00 34.20 ? 230 ASP A CG 1 ATOM 1466 O OD1 . ASP A 1 189 ? 33.590 41.053 28.452 1.00 34.94 ? 230 ASP A OD1 1 ATOM 1467 O OD2 . ASP A 1 189 ? 34.752 40.970 30.325 1.00 35.73 ? 230 ASP A OD2 1 ATOM 1468 N N . PRO A 1 190 ? 33.792 38.755 32.219 1.00 33.51 ? 231 PRO A N 1 ATOM 1469 C CA . PRO A 1 190 ? 34.642 38.480 33.372 1.00 34.07 ? 231 PRO A CA 1 ATOM 1470 C C . PRO A 1 190 ? 35.336 39.725 33.928 1.00 35.80 ? 231 PRO A C 1 ATOM 1471 O O . PRO A 1 190 ? 35.672 39.766 35.113 1.00 35.70 ? 231 PRO A O 1 ATOM 1472 C CB . PRO A 1 190 ? 35.700 37.524 32.806 1.00 35.91 ? 231 PRO A CB 1 ATOM 1473 C CG . PRO A 1 190 ? 35.028 36.858 31.679 1.00 36.61 ? 231 PRO A CG 1 ATOM 1474 C CD . PRO A 1 190 ? 34.048 37.838 31.095 1.00 32.95 ? 231 PRO A CD 1 ATOM 1475 N N . ALA A 1 191 ? 35.526 40.741 33.094 1.00 36.13 ? 232 ALA A N 1 ATOM 1476 C CA . ALA A 1 191 ? 36.112 42.005 33.572 1.00 37.77 ? 232 ALA A CA 1 ATOM 1477 C C . ALA A 1 191 ? 35.320 42.587 34.764 1.00 36.99 ? 232 ALA A C 1 ATOM 1478 O O . ALA A 1 191 ? 35.888 43.120 35.742 1.00 37.24 ? 232 ALA A O 1 ATOM 1479 C CB . ALA A 1 191 ? 36.210 43.011 32.410 1.00 38.74 ? 232 ALA A CB 1 ATOM 1480 N N . ASP A 1 192 ? 34.006 42.381 34.725 1.00 36.11 ? 233 ASP A N 1 ATOM 1481 C CA . ASP A 1 192 ? 33.079 42.922 35.720 1.00 35.93 ? 233 ASP A CA 1 ATOM 1482 C C . ASP A 1 192 ? 32.606 41.888 36.747 1.00 35.32 ? 233 ASP A C 1 ATOM 1483 O O . ASP A 1 192 ? 32.147 42.247 37.856 1.00 35.83 ? 233 ASP A O 1 ATOM 1484 C CB . ASP A 1 192 ? 31.887 43.460 34.950 1.00 35.37 ? 233 ASP A CB 1 ATOM 1485 C CG . ASP A 1 192 ? 32.305 44.476 33.900 1.00 35.40 ? 233 ASP A CG 1 ATOM 1486 O OD1 . ASP A 1 192 ? 32.653 45.602 34.324 1.00 37.72 ? 233 ASP A OD1 1 ATOM 1487 O OD2 . ASP A 1 192 ? 32.309 44.167 32.675 1.00 35.36 ? 233 ASP A OD2 1 ATOM 1488 N N . TYR A 1 193 ? 32.686 40.603 36.408 1.00 33.80 ? 234 TYR A N 1 ATOM 1489 C CA . TYR A 1 193 ? 32.126 39.566 37.296 1.00 32.47 ? 234 TYR A CA 1 ATOM 1490 C C . TYR A 1 193 ? 33.070 38.422 37.639 1.00 34.05 ? 234 TYR A C 1 ATOM 1491 O O . TYR A 1 193 ? 32.646 37.359 38.109 1.00 33.31 ? 234 TYR A O 1 ATOM 1492 C CB . TYR A 1 193 ? 30.799 39.030 36.718 1.00 31.50 ? 234 TYR A CB 1 ATOM 1493 C CG . TYR A 1 193 ? 29.756 40.107 36.618 1.00 30.90 ? 234 TYR A CG 1 ATOM 1494 C CD1 . TYR A 1 193 ? 29.581 40.833 35.449 1.00 30.00 ? 234 TYR A CD1 1 ATOM 1495 C CD2 . TYR A 1 193 ? 28.974 40.439 37.719 1.00 28.46 ? 234 TYR A CD2 1 ATOM 1496 C CE1 . TYR A 1 193 ? 28.631 41.868 35.362 1.00 30.28 ? 234 TYR A CE1 1 ATOM 1497 C CE2 . TYR A 1 193 ? 28.035 41.477 37.654 1.00 31.56 ? 234 TYR A CE2 1 ATOM 1498 C CZ . TYR A 1 193 ? 27.867 42.179 36.480 1.00 30.57 ? 234 TYR A CZ 1 ATOM 1499 O OH . TYR A 1 193 ? 26.941 43.181 36.420 1.00 29.73 ? 234 TYR A OH 1 ATOM 1500 N N . PHE A 1 194 ? 34.362 38.613 37.380 1.00 34.28 ? 235 PHE A N 1 ATOM 1501 C CA . PHE A 1 194 ? 35.304 37.594 37.752 1.00 35.82 ? 235 PHE A CA 1 ATOM 1502 C C . PHE A 1 194 ? 36.466 38.320 38.420 1.00 37.24 ? 235 PHE A C 1 ATOM 1503 O O . PHE A 1 194 ? 37.280 38.927 37.733 1.00 38.81 ? 235 PHE A O 1 ATOM 1504 C CB . PHE A 1 194 ? 35.763 36.819 36.526 1.00 36.93 ? 235 PHE A CB 1 ATOM 1505 C CG . PHE A 1 194 ? 36.500 35.564 36.861 1.00 37.50 ? 235 PHE A CG 1 ATOM 1506 C CD1 . PHE A 1 194 ? 35.813 34.356 36.978 1.00 38.43 ? 235 PHE A CD1 1 ATOM 1507 C CD2 . PHE A 1 194 ? 37.885 35.582 37.056 1.00 39.57 ? 235 PHE A CD2 1 ATOM 1508 C CE1 . PHE A 1 194 ? 36.502 33.175 37.294 1.00 39.18 ? 235 PHE A CE1 1 ATOM 1509 C CE2 . PHE A 1 194 ? 38.573 34.421 37.376 1.00 41.34 ? 235 PHE A CE2 1 ATOM 1510 C CZ . PHE A 1 194 ? 37.884 33.211 37.496 1.00 42.33 ? 235 PHE A CZ 1 ATOM 1511 N N . ALA A 1 195 ? 36.485 38.295 39.748 1.00 36.30 ? 236 ALA A N 1 ATOM 1512 C CA . ALA A 1 195 ? 37.558 38.900 40.525 1.00 38.52 ? 236 ALA A CA 1 ATOM 1513 C C . ALA A 1 195 ? 38.864 38.109 40.358 1.00 39.99 ? 236 ALA A C 1 ATOM 1514 O O . ALA A 1 195 ? 38.859 36.885 40.439 1.00 39.59 ? 236 ALA A O 1 ATOM 1515 C CB . ALA A 1 195 ? 37.159 38.965 41.978 1.00 37.90 ? 236 ALA A CB 1 ATOM 1516 N N . PRO A 1 196 ? 39.983 38.811 40.087 1.00 41.79 ? 237 PRO A N 1 ATOM 1517 C CA . PRO A 1 196 ? 41.296 38.168 39.944 1.00 43.27 ? 237 PRO A CA 1 ATOM 1518 C C . PRO A 1 196 ? 41.670 37.289 41.136 1.00 42.87 ? 237 PRO A C 1 ATOM 1519 O O . PRO A 1 196 ? 41.473 37.690 42.300 1.00 43.59 ? 237 PRO A O 1 ATOM 1520 C CB . PRO A 1 196 ? 42.271 39.361 39.864 1.00 44.50 ? 237 PRO A CB 1 ATOM 1521 C CG . PRO A 1 196 ? 41.444 40.509 39.411 1.00 44.03 ? 237 PRO A CG 1 ATOM 1522 C CD . PRO A 1 196 ? 40.019 40.255 39.781 1.00 42.09 ? 237 PRO A CD 1 ATOM 1523 N N . GLY A 1 197 ? 42.171 36.092 40.841 1.00 43.58 ? 238 GLY A N 1 ATOM 1524 C CA . GLY A 1 197 ? 42.726 35.205 41.864 1.00 43.49 ? 238 GLY A CA 1 ATOM 1525 C C . GLY A 1 197 ? 41.724 34.478 42.738 1.00 42.93 ? 238 GLY A C 1 ATOM 1526 O O . GLY A 1 197 ? 42.121 33.853 43.729 1.00 45.17 ? 238 GLY A O 1 ATOM 1527 N N . VAL A 1 198 ? 40.434 34.531 42.373 1.00 39.06 ? 239 VAL A N 1 ATOM 1528 C CA . VAL A 1 198 ? 39.392 33.772 43.083 1.00 36.64 ? 239 VAL A CA 1 ATOM 1529 C C . VAL A 1 198 ? 38.794 32.689 42.168 1.00 36.02 ? 239 VAL A C 1 ATOM 1530 O O . VAL A 1 198 ? 38.661 32.864 40.957 1.00 36.58 ? 239 VAL A O 1 ATOM 1531 C CB . VAL A 1 198 ? 38.313 34.754 43.781 1.00 35.29 ? 239 VAL A CB 1 ATOM 1532 C CG1 A VAL A 1 198 ? 38.579 36.192 43.406 0.50 36.41 ? 239 VAL A CG1 1 ATOM 1533 C CG1 B VAL A 1 198 ? 37.187 33.976 44.477 0.50 32.71 ? 239 VAL A CG1 1 ATOM 1534 C CG2 A VAL A 1 198 ? 36.873 34.321 43.572 0.50 34.00 ? 239 VAL A CG2 1 ATOM 1535 C CG2 B VAL A 1 198 ? 38.984 35.735 44.757 0.50 34.77 ? 239 VAL A CG2 1 ATOM 1536 N N . LYS A 1 199 ? 38.486 31.543 42.755 1.00 35.78 ? 240 LYS A N 1 ATOM 1537 C CA . LYS A 1 199 ? 37.916 30.429 42.013 1.00 36.83 ? 240 LYS A CA 1 ATOM 1538 C C . LYS A 1 199 ? 36.428 30.630 41.678 1.00 35.90 ? 240 LYS A C 1 ATOM 1539 O O . LYS A 1 199 ? 35.697 31.275 42.441 1.00 34.89 ? 240 LYS A O 1 ATOM 1540 C CB . LYS A 1 199 ? 38.089 29.145 42.831 1.00 37.81 ? 240 LYS A CB 1 ATOM 1541 C CG . LYS A 1 199 ? 39.583 28.692 42.997 1.00 40.68 ? 240 LYS A CG 1 ATOM 1542 C CD . LYS A 1 199 ? 40.226 28.556 41.645 1.00 45.54 ? 240 LYS A CD 1 ATOM 1543 C CE . LYS A 1 199 ? 41.600 27.879 41.747 1.00 51.15 ? 240 LYS A CE 1 ATOM 1544 N NZ . LYS A 1 199 ? 42.230 27.790 40.389 1.00 53.16 ? 240 LYS A NZ 1 ATOM 1545 N N . SER A 1 200 ? 35.999 30.081 40.538 1.00 36.50 ? 241 SER A N 1 ATOM 1546 C CA . SER A 1 200 ? 34.563 30.054 40.204 1.00 35.52 ? 241 SER A CA 1 ATOM 1547 C C . SER A 1 200 ? 33.792 29.153 41.152 1.00 33.88 ? 241 SER A C 1 ATOM 1548 O O . SER A 1 200 ? 34.328 28.147 41.637 1.00 34.41 ? 241 SER A O 1 ATOM 1549 C CB . SER A 1 200 ? 34.344 29.425 38.817 1.00 38.59 ? 241 SER A CB 1 ATOM 1550 O OG . SER A 1 200 ? 34.963 30.129 37.779 1.00 44.55 ? 241 SER A OG 1 ATOM 1551 N N . TYR A 1 201 ? 32.503 29.462 41.340 1.00 32.14 ? 242 TYR A N 1 ATOM 1552 C CA . TYR A 1 201 ? 31.605 28.599 42.098 1.00 31.11 ? 242 TYR A CA 1 ATOM 1553 C C . TYR A 1 201 ? 31.606 27.181 41.471 1.00 32.58 ? 242 TYR A C 1 ATOM 1554 O O . TYR A 1 201 ? 31.540 27.065 40.245 1.00 32.10 ? 242 TYR A O 1 ATOM 1555 C CB . TYR A 1 201 ? 30.172 29.177 42.120 1.00 30.27 ? 242 TYR A CB 1 ATOM 1556 C CG . TYR A 1 201 ? 29.421 28.609 43.271 1.00 28.45 ? 242 TYR A CG 1 ATOM 1557 C CD1 . TYR A 1 201 ? 29.658 29.073 44.571 1.00 29.94 ? 242 TYR A CD1 1 ATOM 1558 C CD2 . TYR A 1 201 ? 28.527 27.544 43.085 1.00 30.68 ? 242 TYR A CD2 1 ATOM 1559 C CE1 . TYR A 1 201 ? 29.012 28.505 45.647 1.00 31.97 ? 242 TYR A CE1 1 ATOM 1560 C CE2 . TYR A 1 201 ? 27.879 26.958 44.164 1.00 30.35 ? 242 TYR A CE2 1 ATOM 1561 C CZ . TYR A 1 201 ? 28.127 27.459 45.439 1.00 31.25 ? 242 TYR A CZ 1 ATOM 1562 O OH . TYR A 1 201 ? 27.493 26.876 46.489 1.00 38.09 ? 242 TYR A OH 1 ATOM 1563 N N . PRO A 1 202 ? 31.656 26.104 42.296 1.00 33.32 ? 243 PRO A N 1 ATOM 1564 C CA . PRO A 1 202 ? 31.504 26.015 43.750 1.00 34.39 ? 243 PRO A CA 1 ATOM 1565 C C . PRO A 1 202 ? 32.771 26.126 44.602 1.00 35.97 ? 243 PRO A C 1 ATOM 1566 O O . PRO A 1 202 ? 32.683 25.934 45.833 1.00 37.33 ? 243 PRO A O 1 ATOM 1567 C CB . PRO A 1 202 ? 30.864 24.635 43.935 1.00 34.59 ? 243 PRO A CB 1 ATOM 1568 C CG . PRO A 1 202 ? 31.514 23.814 42.846 1.00 35.50 ? 243 PRO A CG 1 ATOM 1569 C CD . PRO A 1 202 ? 31.621 24.759 41.665 1.00 34.97 ? 243 PRO A CD 1 ATOM 1570 N N . ASP A 1 203 ? 33.908 26.450 43.983 1.00 36.31 ? 244 ASP A N 1 ATOM 1571 C CA . ASP A 1 203 ? 35.196 26.430 44.680 1.00 37.91 ? 244 ASP A CA 1 ATOM 1572 C C . ASP A 1 203 ? 35.630 27.795 45.154 1.00 36.57 ? 244 ASP A C 1 ATOM 1573 O O . ASP A 1 203 ? 36.582 27.914 45.913 1.00 36.83 ? 244 ASP A O 1 ATOM 1574 C CB . ASP A 1 203 ? 36.262 25.752 43.824 1.00 39.51 ? 244 ASP A CB 1 ATOM 1575 C CG . ASP A 1 203 ? 35.865 24.311 43.461 1.00 43.84 ? 244 ASP A CG 1 ATOM 1576 O OD1 . ASP A 1 203 ? 35.471 23.532 44.375 1.00 43.48 ? 244 ASP A OD1 1 ATOM 1577 O OD2 . ASP A 1 203 ? 35.878 23.991 42.259 1.00 49.00 ? 244 ASP A OD2 1 ATOM 1578 N N . GLY A 1 204 ? 34.861 28.817 44.758 1.00 35.34 ? 245 GLY A N 1 ATOM 1579 C CA . GLY A 1 204 ? 35.067 30.167 45.238 1.00 33.12 ? 245 GLY A CA 1 ATOM 1580 C C . GLY A 1 204 ? 33.806 30.933 44.887 1.00 32.07 ? 245 GLY A C 1 ATOM 1581 O O . GLY A 1 204 ? 32.788 30.327 44.472 1.00 32.84 ? 245 GLY A O 1 ATOM 1582 N N . TRP A 1 205 ? 33.876 32.245 45.024 1.00 30.30 ? 246 TRP A N 1 ATOM 1583 C CA . TRP A 1 205 ? 32.676 33.084 44.845 1.00 28.79 ? 246 TRP A CA 1 ATOM 1584 C C . TRP A 1 205 ? 32.554 33.788 43.488 1.00 28.90 ? 246 TRP A C 1 ATOM 1585 O O . TRP A 1 205 ? 31.684 34.665 43.310 1.00 28.44 ? 246 TRP A O 1 ATOM 1586 C CB . TRP A 1 205 ? 32.536 34.094 46.000 1.00 28.64 ? 246 TRP A CB 1 ATOM 1587 C CG . TRP A 1 205 ? 33.790 34.873 46.336 1.00 30.72 ? 246 TRP A CG 1 ATOM 1588 C CD1 . TRP A 1 205 ? 34.769 34.507 47.227 1.00 32.76 ? 246 TRP A CD1 1 ATOM 1589 C CD2 . TRP A 1 205 ? 34.183 36.159 45.819 1.00 30.59 ? 246 TRP A CD2 1 ATOM 1590 N NE1 . TRP A 1 205 ? 35.738 35.479 47.279 1.00 35.04 ? 246 TRP A NE1 1 ATOM 1591 C CE2 . TRP A 1 205 ? 35.399 36.506 46.441 1.00 33.15 ? 246 TRP A CE2 1 ATOM 1592 C CE3 . TRP A 1 205 ? 33.616 37.050 44.893 1.00 34.41 ? 246 TRP A CE3 1 ATOM 1593 C CZ2 . TRP A 1 205 ? 36.080 37.700 46.161 1.00 35.19 ? 246 TRP A CZ2 1 ATOM 1594 C CZ3 . TRP A 1 205 ? 34.283 38.255 44.616 1.00 35.59 ? 246 TRP A CZ3 1 ATOM 1595 C CH2 . TRP A 1 205 ? 35.516 38.563 45.256 1.00 34.98 ? 246 TRP A CH2 1 ATOM 1596 N N . ASN A 1 206 ? 33.382 33.385 42.514 1.00 28.62 ? 247 ASN A N 1 ATOM 1597 C CA . ASN A 1 206 ? 33.329 33.954 41.149 1.00 29.09 ? 247 ASN A CA 1 ATOM 1598 C C . ASN A 1 206 ? 32.289 33.341 40.249 1.00 29.07 ? 247 ASN A C 1 ATOM 1599 O O . ASN A 1 206 ? 31.821 32.233 40.507 1.00 29.66 ? 247 ASN A O 1 ATOM 1600 C CB . ASN A 1 206 ? 34.693 33.846 40.444 1.00 30.09 ? 247 ASN A CB 1 ATOM 1601 C CG . ASN A 1 206 ? 35.491 35.122 40.557 1.00 31.77 ? 247 ASN A CG 1 ATOM 1602 O OD1 . ASN A 1 206 ? 34.935 36.185 40.913 1.00 33.85 ? 247 ASN A OD1 1 ATOM 1603 N ND2 . ASN A 1 206 ? 36.800 35.041 40.268 1.00 32.44 ? 247 ASN A ND2 1 ATOM 1604 N N . LEU A 1 207 ? 31.931 34.071 39.190 1.00 28.60 ? 248 LEU A N 1 ATOM 1605 C CA . LEU A 1 207 ? 30.933 33.619 38.248 1.00 28.53 ? 248 LEU A CA 1 ATOM 1606 C C . LEU A 1 207 ? 31.576 32.657 37.235 1.00 28.99 ? 248 LEU A C 1 ATOM 1607 O O . LEU A 1 207 ? 32.591 33.003 36.615 1.00 30.84 ? 248 LEU A O 1 ATOM 1608 C CB . LEU A 1 207 ? 30.357 34.813 37.502 1.00 27.41 ? 248 LEU A CB 1 ATOM 1609 C CG . LEU A 1 207 ? 29.231 34.555 36.498 1.00 31.05 ? 248 LEU A CG 1 ATOM 1610 C CD1 . LEU A 1 207 ? 27.994 34.112 37.209 1.00 28.81 ? 248 LEU A CD1 1 ATOM 1611 C CD2 . LEU A 1 207 ? 28.970 35.807 35.641 1.00 32.59 ? 248 LEU A CD2 1 ATOM 1612 N N . PRO A 1 208 ? 31.028 31.426 37.121 1.00 28.80 ? 249 PRO A N 1 ATOM 1613 C CA . PRO A 1 208 ? 31.481 30.550 36.042 1.00 29.62 ? 249 PRO A CA 1 ATOM 1614 C C . PRO A 1 208 ? 30.959 30.975 34.679 1.00 28.99 ? 249 PRO A C 1 ATOM 1615 O O . PRO A 1 208 ? 29.994 31.726 34.581 1.00 29.36 ? 249 PRO A O 1 ATOM 1616 C CB . PRO A 1 208 ? 30.874 29.172 36.398 1.00 31.57 ? 249 PRO A CB 1 ATOM 1617 C CG . PRO A 1 208 ? 30.075 29.340 37.569 1.00 29.37 ? 249 PRO A CG 1 ATOM 1618 C CD . PRO A 1 208 ? 30.005 30.782 37.963 1.00 29.29 ? 249 PRO A CD 1 ATOM 1619 N N . GLY A 1 209 ? 31.574 30.441 33.627 1.00 30.03 ? 250 GLY A N 1 ATOM 1620 C CA . GLY A 1 209 ? 31.210 30.872 32.291 1.00 31.70 ? 250 GLY A CA 1 ATOM 1621 C C . GLY A 1 209 ? 29.814 30.492 31.860 1.00 30.82 ? 250 GLY A C 1 ATOM 1622 O O . GLY A 1 209 ? 29.285 31.067 30.901 1.00 31.90 ? 250 GLY A O 1 ATOM 1623 N N . GLY A 1 210 ? 29.233 29.510 32.537 1.00 30.09 ? 251 GLY A N 1 ATOM 1624 C CA . GLY A 1 210 ? 27.814 29.154 32.347 1.00 29.39 ? 251 GLY A CA 1 ATOM 1625 C C . GLY A 1 210 ? 26.801 29.904 33.222 1.00 28.34 ? 251 GLY A C 1 ATOM 1626 O O . GLY A 1 210 ? 25.603 29.734 33.044 1.00 28.29 ? 251 GLY A O 1 ATOM 1627 N N . GLY A 1 211 ? 27.279 30.730 34.161 1.00 27.59 ? 252 GLY A N 1 ATOM 1628 C CA . GLY A 1 211 ? 26.390 31.510 35.032 1.00 26.10 ? 252 GLY A CA 1 ATOM 1629 C C . GLY A 1 211 ? 25.737 32.665 34.282 1.00 25.81 ? 252 GLY A C 1 ATOM 1630 O O . GLY A 1 211 ? 26.331 33.236 33.330 1.00 27.77 ? 252 GLY A O 1 ATOM 1631 N N . VAL A 1 212 ? 24.537 33.025 34.720 1.00 25.75 ? 253 VAL A N 1 ATOM 1632 C CA . VAL A 1 212 ? 23.787 34.078 34.050 1.00 25.61 ? 253 VAL A CA 1 ATOM 1633 C C . VAL A 1 212 ? 23.047 34.893 35.064 1.00 25.53 ? 253 VAL A C 1 ATOM 1634 O O . VAL A 1 212 ? 22.442 34.352 36.006 1.00 25.53 ? 253 VAL A O 1 ATOM 1635 C CB . VAL A 1 212 ? 22.747 33.494 33.003 1.00 24.13 ? 253 VAL A CB 1 ATOM 1636 C CG1 . VAL A 1 212 ? 22.085 34.622 32.209 1.00 25.74 ? 253 VAL A CG1 1 ATOM 1637 C CG2 . VAL A 1 212 ? 23.385 32.444 32.013 1.00 25.41 ? 253 VAL A CG2 1 ATOM 1638 N N . GLN A 1 213 ? 23.086 36.211 34.859 1.00 24.68 ? 254 GLN A N 1 ATOM 1639 C CA . GLN A 1 213 ? 22.344 37.140 35.738 1.00 23.84 ? 254 GLN A CA 1 ATOM 1640 C C . GLN A 1 213 ? 20.941 37.351 35.217 1.00 24.65 ? 254 GLN A C 1 ATOM 1641 O O . GLN A 1 213 ? 20.756 37.921 34.122 1.00 25.64 ? 254 GLN A O 1 ATOM 1642 C CB . GLN A 1 213 ? 23.123 38.472 35.787 1.00 24.36 ? 254 GLN A CB 1 ATOM 1643 C CG . GLN A 1 213 ? 22.415 39.573 36.616 1.00 23.45 ? 254 GLN A CG 1 ATOM 1644 C CD . GLN A 1 213 ? 23.042 40.961 36.397 1.00 24.84 ? 254 GLN A CD 1 ATOM 1645 O OE1 . GLN A 1 213 ? 22.333 41.953 36.374 1.00 25.70 ? 254 GLN A OE1 1 ATOM 1646 N NE2 . GLN A 1 213 ? 24.364 41.024 36.247 1.00 25.06 ? 254 GLN A NE2 1 ATOM 1647 N N . ARG A 1 214 ? 19.954 36.853 35.966 1.00 23.04 ? 255 ARG A N 1 ATOM 1648 C CA . ARG A 1 214 ? 18.556 37.216 35.705 1.00 24.33 ? 255 ARG A CA 1 ATOM 1649 C C . ARG A 1 214 ? 18.283 38.681 36.082 1.00 23.63 ? 255 ARG A C 1 ATOM 1650 O O . ARG A 1 214 ? 19.093 39.340 36.726 1.00 22.65 ? 255 ARG A O 1 ATOM 1651 C CB . ARG A 1 214 ? 17.643 36.306 36.529 1.00 23.79 ? 255 ARG A CB 1 ATOM 1652 C CG . ARG A 1 214 ? 17.634 34.847 36.015 1.00 25.15 ? 255 ARG A CG 1 ATOM 1653 C CD . ARG A 1 214 ? 17.223 33.904 37.169 1.00 26.10 ? 255 ARG A CD 1 ATOM 1654 N NE . ARG A 1 214 ? 17.370 32.501 36.788 1.00 27.84 ? 255 ARG A NE 1 ATOM 1655 C CZ . ARG A 1 214 ? 18.534 31.861 36.758 1.00 28.27 ? 255 ARG A CZ 1 ATOM 1656 N NH1 . ARG A 1 214 ? 19.675 32.514 37.031 1.00 25.90 ? 255 ARG A NH1 1 ATOM 1657 N NH2 . ARG A 1 214 ? 18.580 30.572 36.388 1.00 27.99 ? 255 ARG A NH2 1 ATOM 1658 N N . GLY A 1 215 ? 17.121 39.184 35.681 1.00 23.05 ? 256 GLY A N 1 ATOM 1659 C CA . GLY A 1 215 ? 16.673 40.491 36.210 1.00 22.03 ? 256 GLY A CA 1 ATOM 1660 C C . GLY A 1 215 ? 15.635 41.161 35.334 1.00 22.97 ? 256 GLY A C 1 ATOM 1661 O O . GLY A 1 215 ? 15.642 41.008 34.101 1.00 22.81 ? 256 GLY A O 1 ATOM 1662 N N A ASN A 1 216 ? 14.727 41.908 35.950 0.70 23.11 ? 257 ASN A N 1 ATOM 1663 N N B ASN A 1 216 ? 14.811 41.958 36.003 0.30 22.79 ? 257 ASN A N 1 ATOM 1664 C CA A ASN A 1 216 ? 13.732 42.575 35.107 0.70 22.72 ? 257 ASN A CA 1 ATOM 1665 C CA B ASN A 1 216 ? 13.796 42.840 35.436 0.30 22.91 ? 257 ASN A CA 1 ATOM 1666 C C A ASN A 1 216 ? 14.386 43.739 34.392 0.70 22.75 ? 257 ASN A C 1 ATOM 1667 C C B ASN A 1 216 ? 14.385 43.870 34.456 0.30 23.15 ? 257 ASN A C 1 ATOM 1668 O O A ASN A 1 216 ? 15.408 44.292 34.825 0.70 22.58 ? 257 ASN A O 1 ATOM 1669 O O B ASN A 1 216 ? 15.423 44.459 34.770 0.30 23.10 ? 257 ASN A O 1 ATOM 1670 C CB A ASN A 1 216 ? 12.503 43.036 35.894 0.70 22.23 ? 257 ASN A CB 1 ATOM 1671 C CB B ASN A 1 216 ? 13.226 43.549 36.659 0.30 22.58 ? 257 ASN A CB 1 ATOM 1672 C CG A ASN A 1 216 ? 12.709 44.362 36.607 0.70 23.36 ? 257 ASN A CG 1 ATOM 1673 C CG B ASN A 1 216 ? 12.111 44.480 36.348 0.30 22.19 ? 257 ASN A CG 1 ATOM 1674 O OD1 A ASN A 1 216 ? 12.675 45.439 36.006 0.70 23.04 ? 257 ASN A OD1 1 ATOM 1675 O OD1 B ASN A 1 216 ? 11.478 44.373 35.326 0.30 22.76 ? 257 ASN A OD1 1 ATOM 1676 N ND2 A ASN A 1 216 ? 12.862 44.290 37.933 0.70 26.03 ? 257 ASN A ND2 1 ATOM 1677 N ND2 B ASN A 1 216 ? 11.857 45.414 37.266 0.30 25.15 ? 257 ASN A ND2 1 ATOM 1678 N N . ILE A 1 217 ? 13.768 44.081 33.279 1.00 23.65 ? 258 ILE A N 1 ATOM 1679 C CA . ILE A 1 217 ? 14.202 45.184 32.439 1.00 25.15 ? 258 ILE A CA 1 ATOM 1680 C C . ILE A 1 217 ? 13.111 46.255 32.280 1.00 26.29 ? 258 ILE A C 1 ATOM 1681 O O . ILE A 1 217 ? 13.117 46.996 31.314 1.00 27.59 ? 258 ILE A O 1 ATOM 1682 C CB . ILE A 1 217 ? 14.596 44.663 31.054 1.00 25.22 ? 258 ILE A CB 1 ATOM 1683 C CG1 . ILE A 1 217 ? 13.514 43.695 30.547 1.00 24.35 ? 258 ILE A CG1 1 ATOM 1684 C CG2 . ILE A 1 217 ? 15.907 43.888 31.165 1.00 27.20 ? 258 ILE A CG2 1 ATOM 1685 C CD1 . ILE A 1 217 ? 13.574 43.382 28.993 1.00 31.43 ? 258 ILE A CD1 1 ATOM 1686 N N . LEU A 1 218 ? 12.174 46.322 33.222 1.00 27.25 ? 259 LEU A N 1 ATOM 1687 C CA . LEU A 1 218 ? 11.148 47.382 33.197 1.00 28.91 ? 259 LEU A CA 1 ATOM 1688 C C . LEU A 1 218 ? 11.743 48.789 33.353 1.00 29.80 ? 259 LEU A C 1 ATOM 1689 O O . LEU A 1 218 ? 12.805 48.989 33.946 1.00 30.91 ? 259 LEU A O 1 ATOM 1690 C CB . LEU A 1 218 ? 10.190 47.172 34.366 1.00 30.26 ? 259 LEU A CB 1 ATOM 1691 C CG . LEU A 1 218 ? 9.219 46.010 34.216 1.00 30.69 ? 259 LEU A CG 1 ATOM 1692 C CD1 . LEU A 1 218 ? 8.315 45.964 35.469 1.00 35.00 ? 259 LEU A CD1 1 ATOM 1693 C CD2 . LEU A 1 218 ? 8.367 46.076 33.027 1.00 35.72 ? 259 LEU A CD2 1 ATOM 1694 N N . ASN A 1 219 ? 11.054 49.781 32.812 1.00 29.73 ? 260 ASN A N 1 ATOM 1695 C CA . ASN A 1 219 ? 11.344 51.184 33.194 1.00 31.89 ? 260 ASN A CA 1 ATOM 1696 C C . ASN A 1 219 ? 10.092 51.803 33.786 1.00 30.05 ? 260 ASN A C 1 ATOM 1697 O O . ASN A 1 219 ? 9.384 52.571 33.120 1.00 32.88 ? 260 ASN A O 1 ATOM 1698 C CB . ASN A 1 219 ? 11.786 51.966 31.951 1.00 33.62 ? 260 ASN A CB 1 ATOM 1699 C CG . ASN A 1 219 ? 13.240 51.763 31.633 1.00 39.12 ? 260 ASN A CG 1 ATOM 1700 O OD1 . ASN A 1 219 ? 14.127 52.440 32.194 1.00 44.12 ? 260 ASN A OD1 1 ATOM 1701 N ND2 . ASN A 1 219 ? 13.510 50.822 30.724 1.00 41.41 ? 260 ASN A ND2 1 ATOM 1702 N N . LEU A 1 220 ? 9.773 51.433 35.020 1.00 28.21 ? 261 LEU A N 1 ATOM 1703 C CA . LEU A 1 220 ? 8.517 51.863 35.654 1.00 27.69 ? 261 LEU A CA 1 ATOM 1704 C C . LEU A 1 220 ? 8.556 53.269 36.258 1.00 27.58 ? 261 LEU A C 1 ATOM 1705 O O . LEU A 1 220 ? 7.485 53.851 36.508 1.00 25.96 ? 261 LEU A O 1 ATOM 1706 C CB . LEU A 1 220 ? 8.200 50.913 36.836 1.00 28.63 ? 261 LEU A CB 1 ATOM 1707 C CG . LEU A 1 220 ? 7.823 49.465 36.483 1.00 29.14 ? 261 LEU A CG 1 ATOM 1708 C CD1 . LEU A 1 220 ? 7.754 48.584 37.815 1.00 27.57 ? 261 LEU A CD1 1 ATOM 1709 C CD2 . LEU A 1 220 ? 6.481 49.487 35.728 1.00 29.20 ? 261 LEU A CD2 1 ATOM 1710 N N . ASN A 1 221 ? 9.746 53.806 36.487 1.00 26.76 ? 262 ASN A N 1 ATOM 1711 C CA . ASN A 1 221 ? 9.837 55.144 37.198 1.00 25.32 ? 262 ASN A CA 1 ATOM 1712 C C . ASN A 1 221 ? 8.940 55.253 38.424 1.00 24.10 ? 262 ASN A C 1 ATOM 1713 O O . ASN A 1 221 ? 8.257 56.271 38.663 1.00 23.25 ? 262 ASN A O 1 ATOM 1714 C CB . ASN A 1 221 ? 9.583 56.324 36.269 1.00 25.47 ? 262 ASN A CB 1 ATOM 1715 C CG . ASN A 1 221 ? 10.657 56.435 35.217 1.00 28.87 ? 262 ASN A CG 1 ATOM 1716 O OD1 . ASN A 1 221 ? 11.821 56.165 35.500 1.00 29.42 ? 262 ASN A OD1 1 ATOM 1717 N ND2 . ASN A 1 221 ? 10.271 56.810 34.000 1.00 29.78 ? 262 ASN A ND2 1 ATOM 1718 N N . GLY A 1 222 ? 8.959 54.184 39.206 1.00 21.69 ? 263 GLY A N 1 ATOM 1719 C CA . GLY A 1 222 ? 8.289 54.197 40.493 1.00 20.71 ? 263 GLY A CA 1 ATOM 1720 C C . GLY A 1 222 ? 6.824 53.865 40.470 1.00 19.51 ? 263 GLY A C 1 ATOM 1721 O O . GLY A 1 222 ? 6.182 53.965 41.500 1.00 21.10 ? 263 GLY A O 1 ATOM 1722 N N . ALA A 1 223 ? 6.303 53.413 39.341 1.00 18.43 ? 264 ALA A N 1 ATOM 1723 C CA . ALA A 1 223 ? 4.837 53.209 39.263 1.00 18.50 ? 264 ALA A CA 1 ATOM 1724 C C . ALA A 1 223 ? 4.299 51.951 39.968 1.00 19.11 ? 264 ALA A C 1 ATOM 1725 O O . ALA A 1 223 ? 3.112 51.921 40.313 1.00 22.08 ? 264 ALA A O 1 ATOM 1726 C CB . ALA A 1 223 ? 4.373 53.165 37.743 1.00 19.48 ? 264 ALA A CB 1 ATOM 1727 N N . GLY A 1 224 ? 5.130 50.942 40.157 1.00 18.75 ? 265 GLY A N 1 ATOM 1728 C CA . GLY A 1 224 ? 4.644 49.661 40.718 1.00 19.03 ? 265 GLY A CA 1 ATOM 1729 C C . GLY A 1 224 ? 4.062 48.769 39.617 1.00 18.83 ? 265 GLY A C 1 ATOM 1730 O O . GLY A 1 224 ? 4.534 48.772 38.481 1.00 21.52 ? 265 GLY A O 1 ATOM 1731 N N . ASP A 1 225 ? 2.983 48.067 39.926 1.00 18.55 ? 266 ASP A N 1 ATOM 1732 C CA . ASP A 1 225 ? 2.377 47.185 38.906 1.00 19.85 ? 266 ASP A CA 1 ATOM 1733 C C . ASP A 1 225 ? 2.111 47.962 37.638 1.00 20.86 ? 266 ASP A C 1 ATOM 1734 O O . ASP A 1 225 ? 1.395 48.977 37.653 1.00 21.64 ? 266 ASP A O 1 ATOM 1735 C CB . ASP A 1 225 ? 1.089 46.613 39.503 1.00 20.53 ? 266 ASP A CB 1 ATOM 1736 C CG . ASP A 1 225 ? 0.200 45.938 38.450 1.00 21.63 ? 266 ASP A CG 1 ATOM 1737 O OD1 . ASP A 1 225 ? 0.732 45.167 37.638 1.00 22.12 ? 266 ASP A OD1 1 ATOM 1738 O OD2 . ASP A 1 225 ? -1.021 46.224 38.438 1.00 21.67 ? 266 ASP A OD2 1 ATOM 1739 N N . PRO A 1 226 ? 2.586 47.449 36.495 1.00 22.41 ? 267 PRO A N 1 ATOM 1740 C CA . PRO A 1 226 ? 2.398 48.199 35.276 1.00 23.16 ? 267 PRO A CA 1 ATOM 1741 C C . PRO A 1 226 ? 0.940 48.461 34.855 1.00 22.24 ? 267 PRO A C 1 ATOM 1742 O O . PRO A 1 226 ? 0.662 49.430 34.141 1.00 23.83 ? 267 PRO A O 1 ATOM 1743 C CB . PRO A 1 226 ? 3.022 47.271 34.206 1.00 23.47 ? 267 PRO A CB 1 ATOM 1744 C CG . PRO A 1 226 ? 3.964 46.423 34.904 1.00 25.76 ? 267 PRO A CG 1 ATOM 1745 C CD . PRO A 1 226 ? 3.520 46.319 36.346 1.00 23.66 ? 267 PRO A CD 1 ATOM 1746 N N . LEU A 1 227 ? 0.006 47.649 35.344 1.00 21.77 ? 268 LEU A N 1 ATOM 1747 C CA . LEU A 1 227 ? -1.384 47.811 34.942 1.00 22.39 ? 268 LEU A CA 1 ATOM 1748 C C . LEU A 1 227 ? -2.245 48.754 35.825 1.00 20.46 ? 268 LEU A C 1 ATOM 1749 O O . LEU A 1 227 ? -3.350 49.117 35.419 1.00 21.50 ? 268 LEU A O 1 ATOM 1750 C CB . LEU A 1 227 ? -2.049 46.427 34.877 1.00 21.35 ? 268 LEU A CB 1 ATOM 1751 C CG . LEU A 1 227 ? -1.340 45.412 33.963 1.00 23.25 ? 268 LEU A CG 1 ATOM 1752 C CD1 . LEU A 1 227 ? -2.182 44.153 33.903 1.00 25.68 ? 268 LEU A CD1 1 ATOM 1753 C CD2 . LEU A 1 227 ? -1.216 45.953 32.560 1.00 26.83 ? 268 LEU A CD2 1 ATOM 1754 N N . THR A 1 228 ? -1.742 49.148 36.995 1.00 18.82 ? 269 THR A N 1 ATOM 1755 C CA . THR A 1 228 ? -2.553 49.914 37.942 1.00 19.43 ? 269 THR A CA 1 ATOM 1756 C C . THR A 1 228 ? -1.786 51.090 38.582 1.00 17.74 ? 269 THR A C 1 ATOM 1757 O O . THR A 1 228 ? -1.827 51.289 39.813 1.00 18.54 ? 269 THR A O 1 ATOM 1758 C CB . THR A 1 228 ? -2.975 48.977 39.119 1.00 18.44 ? 269 THR A CB 1 ATOM 1759 O OG1 . THR A 1 228 ? -1.808 48.379 39.754 1.00 18.68 ? 269 THR A OG1 1 ATOM 1760 C CG2 . THR A 1 228 ? -3.954 47.874 38.612 1.00 21.00 ? 269 THR A CG2 1 ATOM 1761 N N . PRO A 1 229 ? -1.103 51.921 37.787 1.00 18.72 ? 270 PRO A N 1 ATOM 1762 C CA . PRO A 1 229 ? -0.366 53.047 38.375 1.00 19.08 ? 270 PRO A CA 1 ATOM 1763 C C . PRO A 1 229 ? -1.230 53.997 39.185 1.00 19.29 ? 270 PRO A C 1 ATOM 1764 O O . PRO A 1 229 ? -2.283 54.464 38.706 1.00 20.93 ? 270 PRO A O 1 ATOM 1765 C CB . PRO A 1 229 ? 0.269 53.753 37.151 1.00 20.19 ? 270 PRO A CB 1 ATOM 1766 C CG . PRO A 1 229 ? -0.696 53.366 35.969 1.00 20.70 ? 270 PRO A CG 1 ATOM 1767 C CD . PRO A 1 229 ? -1.131 51.953 36.304 1.00 20.02 ? 270 PRO A CD 1 ATOM 1768 N N . GLY A 1 230 ? -0.824 54.213 40.441 1.00 19.03 ? 271 GLY A N 1 ATOM 1769 C CA . GLY A 1 230 ? -1.566 55.112 41.330 1.00 19.02 ? 271 GLY A CA 1 ATOM 1770 C C . GLY A 1 230 ? -2.436 54.439 42.390 1.00 19.52 ? 271 GLY A C 1 ATOM 1771 O O . GLY A 1 230 ? -2.830 55.081 43.382 1.00 20.79 ? 271 GLY A O 1 ATOM 1772 N N . TYR A 1 231 ? -2.830 53.191 42.130 1.00 18.97 ? 272 TYR A N 1 ATOM 1773 C CA . TYR A 1 231 ? -3.885 52.544 42.920 1.00 19.60 ? 272 TYR A CA 1 ATOM 1774 C C . TYR A 1 231 ? -3.525 51.086 43.167 1.00 18.38 ? 272 TYR A C 1 ATOM 1775 O O . TYR A 1 231 ? -2.905 50.434 42.318 1.00 19.56 ? 272 TYR A O 1 ATOM 1776 C CB . TYR A 1 231 ? -5.253 52.628 42.180 1.00 19.22 ? 272 TYR A CB 1 ATOM 1777 C CG . TYR A 1 231 ? -5.562 54.059 41.774 1.00 20.18 ? 272 TYR A CG 1 ATOM 1778 C CD1 . TYR A 1 231 ? -6.107 54.962 42.700 1.00 20.06 ? 272 TYR A CD1 1 ATOM 1779 C CD2 . TYR A 1 231 ? -5.191 54.556 40.520 1.00 19.43 ? 272 TYR A CD2 1 ATOM 1780 C CE1 . TYR A 1 231 ? -6.315 56.279 42.353 1.00 20.41 ? 272 TYR A CE1 1 ATOM 1781 C CE2 . TYR A 1 231 ? -5.382 55.871 40.149 1.00 19.75 ? 272 TYR A CE2 1 ATOM 1782 C CZ . TYR A 1 231 ? -5.966 56.734 41.077 1.00 20.62 ? 272 TYR A CZ 1 ATOM 1783 O OH . TYR A 1 231 ? -6.167 58.038 40.740 1.00 21.46 ? 272 TYR A OH 1 ATOM 1784 N N . PRO A 1 232 ? -3.938 50.538 44.297 1.00 19.28 ? 273 PRO A N 1 ATOM 1785 C CA . PRO A 1 232 ? -3.539 49.145 44.572 1.00 18.82 ? 273 PRO A CA 1 ATOM 1786 C C . PRO A 1 232 ? -4.263 48.156 43.658 1.00 19.78 ? 273 PRO A C 1 ATOM 1787 O O . PRO A 1 232 ? -5.462 48.333 43.350 1.00 19.70 ? 273 PRO A O 1 ATOM 1788 C CB . PRO A 1 232 ? -3.954 48.934 46.066 1.00 19.79 ? 273 PRO A CB 1 ATOM 1789 C CG . PRO A 1 232 ? -5.119 49.940 46.266 1.00 20.42 ? 273 PRO A CG 1 ATOM 1790 C CD . PRO A 1 232 ? -4.720 51.155 45.406 1.00 20.66 ? 273 PRO A CD 1 ATOM 1791 N N . ALA A 1 233 ? -3.526 47.111 43.255 1.00 19.35 ? 274 ALA A N 1 ATOM 1792 C CA . ALA A 1 233 ? -4.033 46.064 42.354 1.00 20.01 ? 274 ALA A CA 1 ATOM 1793 C C . ALA A 1 233 ? -4.868 45.064 43.163 1.00 21.46 ? 274 ALA A C 1 ATOM 1794 O O . ALA A 1 233 ? -4.484 43.894 43.325 1.00 23.09 ? 274 ALA A O 1 ATOM 1795 C CB . ALA A 1 233 ? -2.834 45.360 41.696 1.00 21.65 ? 274 ALA A CB 1 ATOM 1796 N N . ASN A 1 234 ? -5.970 45.576 43.684 1.00 21.98 ? 275 ASN A N 1 ATOM 1797 C CA . ASN A 1 234 ? -6.890 44.775 44.515 1.00 23.94 ? 275 ASN A CA 1 ATOM 1798 C C . ASN A 1 234 ? -7.895 44.011 43.677 1.00 25.55 ? 275 ASN A C 1 ATOM 1799 O O . ASN A 1 234 ? -7.766 43.961 42.457 1.00 24.30 ? 275 ASN A O 1 ATOM 1800 C CB . ASN A 1 234 ? -7.533 45.687 45.567 1.00 25.44 ? 275 ASN A CB 1 ATOM 1801 C CG . ASN A 1 234 ? -8.373 46.808 44.958 1.00 23.68 ? 275 ASN A CG 1 ATOM 1802 O OD1 . ASN A 1 234 ? -8.855 46.709 43.831 1.00 26.14 ? 275 ASN A OD1 1 ATOM 1803 N ND2 . ASN A 1 234 ? -8.523 47.929 45.709 1.00 26.14 ? 275 ASN A ND2 1 ATOM 1804 N N . GLU A 1 235 ? -8.933 43.439 44.334 1.00 27.46 ? 276 GLU A N 1 ATOM 1805 C CA A GLU A 1 235 ? -9.805 42.518 43.596 0.70 30.44 ? 276 GLU A CA 1 ATOM 1806 C CA B GLU A 1 235 ? -9.931 42.552 43.694 0.30 29.99 ? 276 GLU A CA 1 ATOM 1807 C C . GLU A 1 235 ? -10.739 43.232 42.622 1.00 30.82 ? 276 GLU A C 1 ATOM 1808 O O . GLU A 1 235 ? -11.210 42.596 41.645 1.00 33.86 ? 276 GLU A O 1 ATOM 1809 C CB A GLU A 1 235 ? -10.601 41.604 44.557 0.70 32.48 ? 276 GLU A CB 1 ATOM 1810 C CB B GLU A 1 235 ? -10.962 42.052 44.722 0.30 30.94 ? 276 GLU A CB 1 ATOM 1811 C CG A GLU A 1 235 ? -9.798 40.409 45.017 0.70 36.53 ? 276 GLU A CG 1 ATOM 1812 C CG B GLU A 1 235 ? -10.779 40.633 45.144 0.30 33.20 ? 276 GLU A CG 1 ATOM 1813 C CD A GLU A 1 235 ? -10.034 39.175 44.173 0.70 39.30 ? 276 GLU A CD 1 ATOM 1814 C CD B GLU A 1 235 ? -9.820 40.530 46.304 0.30 33.54 ? 276 GLU A CD 1 ATOM 1815 O OE1 A GLU A 1 235 ? -10.696 39.224 43.098 0.70 45.02 ? 276 GLU A OE1 1 ATOM 1816 O OE1 B GLU A 1 235 ? -9.643 41.538 47.017 0.30 36.12 ? 276 GLU A OE1 1 ATOM 1817 O OE2 A GLU A 1 235 ? -9.576 38.122 44.596 0.70 43.96 ? 276 GLU A OE2 1 ATOM 1818 O OE2 B GLU A 1 235 ? -9.252 39.446 46.504 0.30 32.60 ? 276 GLU A OE2 1 ATOM 1819 N N . TYR A 1 236 ? -10.998 44.518 42.839 1.00 28.83 ? 277 TYR A N 1 ATOM 1820 C CA . TYR A 1 236 ? -11.899 45.243 41.920 1.00 28.87 ? 277 TYR A CA 1 ATOM 1821 C C . TYR A 1 236 ? -11.192 46.233 41.026 1.00 29.16 ? 277 TYR A C 1 ATOM 1822 O O . TYR A 1 236 ? -11.838 47.058 40.357 1.00 29.03 ? 277 TYR A O 1 ATOM 1823 C CB . TYR A 1 236 ? -13.063 45.909 42.676 1.00 30.17 ? 277 TYR A CB 1 ATOM 1824 C CG . TYR A 1 236 ? -12.594 46.843 43.729 1.00 28.41 ? 277 TYR A CG 1 ATOM 1825 C CD1 . TYR A 1 236 ? -12.375 48.187 43.420 1.00 28.32 ? 277 TYR A CD1 1 ATOM 1826 C CD2 . TYR A 1 236 ? -12.375 46.394 45.043 1.00 27.47 ? 277 TYR A CD2 1 ATOM 1827 C CE1 . TYR A 1 236 ? -11.902 49.090 44.395 1.00 30.59 ? 277 TYR A CE1 1 ATOM 1828 C CE2 . TYR A 1 236 ? -11.897 47.278 46.024 1.00 29.83 ? 277 TYR A CE2 1 ATOM 1829 C CZ . TYR A 1 236 ? -11.669 48.634 45.662 1.00 29.81 ? 277 TYR A CZ 1 ATOM 1830 O OH . TYR A 1 236 ? -11.221 49.559 46.582 1.00 32.51 ? 277 TYR A OH 1 ATOM 1831 N N . ALA A 1 237 ? -9.859 46.118 40.975 1.00 27.99 ? 278 ALA A N 1 ATOM 1832 C CA . ALA A 1 237 ? -9.055 47.059 40.236 1.00 27.59 ? 278 ALA A CA 1 ATOM 1833 C C . ALA A 1 237 ? -9.424 47.052 38.783 1.00 29.11 ? 278 ALA A C 1 ATOM 1834 O O . ALA A 1 237 ? -9.748 45.973 38.228 1.00 30.50 ? 278 ALA A O 1 ATOM 1835 C CB . ALA A 1 237 ? -7.556 46.697 40.373 1.00 27.50 ? 278 ALA A CB 1 ATOM 1836 N N . TYR A 1 238 ? -9.430 48.252 38.192 1.00 28.56 ? 279 TYR A N 1 ATOM 1837 C CA . TYR A 1 238 ? -9.557 48.374 36.746 1.00 30.29 ? 279 TYR A CA 1 ATOM 1838 C C . TYR A 1 238 ? -8.128 48.431 36.186 1.00 29.40 ? 279 TYR A C 1 ATOM 1839 O O . TYR A 1 238 ? -7.264 49.153 36.665 1.00 32.34 ? 279 TYR A O 1 ATOM 1840 C CB . TYR A 1 238 ? -10.452 49.572 36.282 1.00 31.70 ? 279 TYR A CB 1 ATOM 1841 C CG A TYR A 1 238 ? -10.700 49.576 34.782 0.50 28.76 ? 279 TYR A CG 1 ATOM 1842 C CG B TYR A 1 238 ? -9.956 50.153 34.956 0.50 35.39 ? 279 TYR A CG 1 ATOM 1843 C CD1 A TYR A 1 238 ? -11.694 48.791 34.210 0.50 28.49 ? 279 TYR A CD1 1 ATOM 1844 C CD1 B TYR A 1 238 ? -10.642 49.950 33.766 0.50 37.74 ? 279 TYR A CD1 1 ATOM 1845 C CD2 A TYR A 1 238 ? -9.910 50.368 33.938 0.50 29.47 ? 279 TYR A CD2 1 ATOM 1846 C CD2 B TYR A 1 238 ? -8.755 50.845 34.903 0.50 36.35 ? 279 TYR A CD2 1 ATOM 1847 C CE1 A TYR A 1 238 ? -11.898 48.789 32.837 0.50 32.34 ? 279 TYR A CE1 1 ATOM 1848 C CE1 B TYR A 1 238 ? -10.143 50.465 32.564 0.50 40.27 ? 279 TYR A CE1 1 ATOM 1849 C CE2 A TYR A 1 238 ? -10.103 50.362 32.575 0.50 31.03 ? 279 TYR A CE2 1 ATOM 1850 C CE2 B TYR A 1 238 ? -8.256 51.338 33.731 0.50 40.34 ? 279 TYR A CE2 1 ATOM 1851 C CZ A TYR A 1 238 ? -11.101 49.580 32.033 0.50 31.43 ? 279 TYR A CZ 1 ATOM 1852 C CZ B TYR A 1 238 ? -8.944 51.167 32.570 0.50 40.65 ? 279 TYR A CZ 1 ATOM 1853 O OH A TYR A 1 238 ? -11.292 49.576 30.681 0.50 36.11 ? 279 TYR A OH 1 ATOM 1854 O OH B TYR A 1 238 ? -8.387 51.707 31.424 0.50 44.04 ? 279 TYR A OH 1 ATOM 1855 N N . ARG A 1 239 ? -7.850 47.572 35.237 1.00 28.70 ? 280 ARG A N 1 ATOM 1856 C CA . ARG A 1 239 ? -6.491 47.422 34.732 1.00 28.60 ? 280 ARG A CA 1 ATOM 1857 C C . ARG A 1 239 ? -6.282 48.049 33.363 1.00 30.42 ? 280 ARG A C 1 ATOM 1858 O O . ARG A 1 239 ? -7.118 47.858 32.454 1.00 31.29 ? 280 ARG A O 1 ATOM 1859 C CB A ARG A 1 239 ? -6.096 45.937 34.794 0.65 28.78 ? 280 ARG A CB 1 ATOM 1860 C CB B ARG A 1 239 ? -6.170 45.933 34.582 0.35 28.30 ? 280 ARG A CB 1 ATOM 1861 C CG A ARG A 1 239 ? -6.082 45.471 36.273 0.65 27.79 ? 280 ARG A CG 1 ATOM 1862 C CG B ARG A 1 239 ? -5.568 45.326 35.811 0.35 25.49 ? 280 ARG A CG 1 ATOM 1863 C CD A ARG A 1 239 ? -5.735 44.012 36.508 0.65 29.17 ? 280 ARG A CD 1 ATOM 1864 C CD B ARG A 1 239 ? -5.423 43.846 35.699 0.35 22.24 ? 280 ARG A CD 1 ATOM 1865 N NE A ARG A 1 239 ? -5.350 43.805 37.918 0.65 28.03 ? 280 ARG A NE 1 ATOM 1866 N NE B ARG A 1 239 ? -5.130 43.375 37.034 0.35 21.44 ? 280 ARG A NE 1 ATOM 1867 C CZ A ARG A 1 239 ? -6.150 43.610 38.961 0.65 26.35 ? 280 ARG A CZ 1 ATOM 1868 C CZ B ARG A 1 239 ? -6.056 43.071 37.933 0.35 20.51 ? 280 ARG A CZ 1 ATOM 1869 N NH1 A ARG A 1 239 ? -7.465 43.563 38.823 0.65 32.62 ? 280 ARG A NH1 1 ATOM 1870 N NH1 B ARG A 1 239 ? -7.362 43.113 37.609 0.35 16.58 ? 280 ARG A NH1 1 ATOM 1871 N NH2 A ARG A 1 239 ? -5.622 43.431 40.168 0.65 23.44 ? 280 ARG A NH2 1 ATOM 1872 N NH2 B ARG A 1 239 ? -5.673 42.698 39.143 0.35 20.70 ? 280 ARG A NH2 1 ATOM 1873 N N . ARG A 1 240 ? -5.175 48.776 33.185 1.00 29.63 ? 281 ARG A N 1 ATOM 1874 C CA . ARG A 1 240 ? -4.797 49.093 31.802 1.00 32.55 ? 281 ARG A CA 1 ATOM 1875 C C . ARG A 1 240 ? -4.698 47.852 30.939 1.00 34.34 ? 281 ARG A C 1 ATOM 1876 O O . ARG A 1 240 ? -4.287 46.771 31.395 1.00 32.94 ? 281 ARG A O 1 ATOM 1877 C CB . ARG A 1 240 ? -3.451 49.809 31.735 1.00 31.73 ? 281 ARG A CB 1 ATOM 1878 C CG . ARG A 1 240 ? -3.536 51.116 32.490 1.00 33.38 ? 281 ARG A CG 1 ATOM 1879 C CD . ARG A 1 240 ? -2.284 51.910 32.343 1.00 33.56 ? 281 ARG A CD 1 ATOM 1880 N NE . ARG A 1 240 ? -2.522 53.260 32.837 1.00 34.79 ? 281 ARG A NE 1 ATOM 1881 C CZ . ARG A 1 240 ? -1.667 54.261 32.684 1.00 39.16 ? 281 ARG A CZ 1 ATOM 1882 N NH1 . ARG A 1 240 ? -0.528 54.058 32.053 1.00 40.99 ? 281 ARG A NH1 1 ATOM 1883 N NH2 . ARG A 1 240 ? -1.943 55.459 33.176 1.00 42.88 ? 281 ARG A NH2 1 ATOM 1884 N N . GLY A 1 241 ? -5.070 48.024 29.668 1.00 36.57 ? 282 GLY A N 1 ATOM 1885 C CA . GLY A 1 241 ? -4.748 47.034 28.646 1.00 40.59 ? 282 GLY A CA 1 ATOM 1886 C C . GLY A 1 241 ? -3.233 46.960 28.531 1.00 41.65 ? 282 GLY A C 1 ATOM 1887 O O . GLY A 1 241 ? -2.528 47.926 28.867 1.00 41.67 ? 282 GLY A O 1 ATOM 1888 N N . ILE A 1 242 ? -2.714 45.817 28.087 1.00 43.88 ? 283 ILE A N 1 ATOM 1889 C CA . ILE A 1 242 ? -1.256 45.659 27.934 1.00 44.55 ? 283 ILE A CA 1 ATOM 1890 C C . ILE A 1 242 ? -0.624 46.780 27.071 1.00 45.11 ? 283 ILE A C 1 ATOM 1891 O O . ILE A 1 242 ? 0.463 47.260 27.384 1.00 44.45 ? 283 ILE A O 1 ATOM 1892 C CB A ILE A 1 242 ? -0.882 44.237 27.392 0.65 45.22 ? 283 ILE A CB 1 ATOM 1893 C CB B ILE A 1 242 ? -0.860 44.245 27.404 0.35 45.06 ? 283 ILE A CB 1 ATOM 1894 C CG1 A ILE A 1 242 ? 0.527 43.828 27.829 0.65 44.83 ? 283 ILE A CG1 1 ATOM 1895 C CG1 B ILE A 1 242 ? -1.201 43.170 28.439 0.35 44.71 ? 283 ILE A CG1 1 ATOM 1896 C CG2 A ILE A 1 242 ? -1.052 44.149 25.869 0.65 46.68 ? 283 ILE A CG2 1 ATOM 1897 C CG2 B ILE A 1 242 ? 0.635 44.173 27.053 0.35 45.19 ? 283 ILE A CG2 1 ATOM 1898 C CD1 A ILE A 1 242 ? 0.641 43.562 29.295 0.65 41.98 ? 283 ILE A CD1 1 ATOM 1899 C CD1 B ILE A 1 242 ? -0.450 43.334 29.756 0.35 43.18 ? 283 ILE A CD1 1 ATOM 1900 N N . ALA A 1 243 ? -1.318 47.225 26.025 1.00 46.65 ? 284 ALA A N 1 ATOM 1901 C CA . ALA A 1 243 ? -0.766 48.272 25.148 1.00 47.44 ? 284 ALA A CA 1 ATOM 1902 C C . ALA A 1 243 ? -0.523 49.621 25.846 1.00 47.20 ? 284 ALA A C 1 ATOM 1903 O O . ALA A 1 243 ? 0.301 50.420 25.384 1.00 47.38 ? 284 ALA A O 1 ATOM 1904 C CB . ALA A 1 243 ? -1.645 48.453 23.914 1.00 48.62 ? 284 ALA A CB 1 ATOM 1905 N N . GLU A 1 244 ? -1.214 49.855 26.971 1.00 46.04 ? 285 GLU A N 1 ATOM 1906 C CA . GLU A 1 244 ? -1.094 51.115 27.711 1.00 45.44 ? 285 GLU A CA 1 ATOM 1907 C C . GLU A 1 244 ? -0.326 50.924 29.028 1.00 43.79 ? 285 GLU A C 1 ATOM 1908 O O . GLU A 1 244 ? -0.218 51.864 29.839 1.00 43.98 ? 285 GLU A O 1 ATOM 1909 C CB . GLU A 1 244 ? -2.480 51.734 27.976 1.00 45.91 ? 285 GLU A CB 1 ATOM 1910 C CG . GLU A 1 244 ? -3.166 52.322 26.720 1.00 49.88 ? 285 GLU A CG 1 ATOM 1911 C CD . GLU A 1 244 ? -3.734 51.259 25.781 1.00 55.79 ? 285 GLU A CD 1 ATOM 1912 O OE1 . GLU A 1 244 ? -4.189 50.194 26.258 1.00 56.06 ? 285 GLU A OE1 1 ATOM 1913 O OE2 . GLU A 1 244 ? -3.728 51.490 24.547 1.00 59.80 ? 285 GLU A OE2 1 ATOM 1914 N N . ALA A 1 245 ? 0.225 49.725 29.219 1.00 42.32 ? 286 ALA A N 1 ATOM 1915 C CA . ALA A 1 245 ? 0.888 49.405 30.476 1.00 40.67 ? 286 ALA A CA 1 ATOM 1916 C C . ALA A 1 245 ? 2.104 50.310 30.658 1.00 40.67 ? 286 ALA A C 1 ATOM 1917 O O . ALA A 1 245 ? 2.639 50.898 29.698 1.00 39.41 ? 286 ALA A O 1 ATOM 1918 C CB . ALA A 1 245 ? 1.269 47.940 30.548 1.00 40.55 ? 286 ALA A CB 1 ATOM 1919 N N . VAL A 1 246 ? 2.504 50.455 31.916 1.00 38.39 ? 287 VAL A N 1 ATOM 1920 C CA . VAL A 1 246 ? 3.628 51.304 32.231 1.00 38.71 ? 287 VAL A CA 1 ATOM 1921 C C . VAL A 1 246 ? 4.917 50.513 32.196 1.00 37.72 ? 287 VAL A C 1 ATOM 1922 O O . VAL A 1 246 ? 5.018 49.440 32.816 1.00 37.51 ? 287 VAL A O 1 ATOM 1923 C CB . VAL A 1 246 ? 3.477 51.974 33.621 1.00 37.49 ? 287 VAL A CB 1 ATOM 1924 C CG1 . VAL A 1 246 ? 4.751 52.839 33.946 1.00 38.06 ? 287 VAL A CG1 1 ATOM 1925 C CG2 . VAL A 1 246 ? 2.231 52.837 33.628 1.00 40.53 ? 287 VAL A CG2 1 ATOM 1926 N N . GLY A 1 247 ? 5.878 51.022 31.434 1.00 36.97 ? 288 GLY A N 1 ATOM 1927 C CA . GLY A 1 247 ? 7.269 50.575 31.582 1.00 36.17 ? 288 GLY A CA 1 ATOM 1928 C C . GLY A 1 247 ? 7.749 49.393 30.764 1.00 36.12 ? 288 GLY A C 1 ATOM 1929 O O . GLY A 1 247 ? 8.932 48.981 30.920 1.00 36.18 ? 288 GLY A O 1 ATOM 1930 N N . LEU A 1 248 ? 6.875 48.843 29.917 1.00 35.72 ? 289 LEU A N 1 ATOM 1931 C CA . LEU A 1 248 ? 7.209 47.583 29.231 1.00 35.79 ? 289 LEU A CA 1 ATOM 1932 C C . LEU A 1 248 ? 8.149 47.815 28.058 1.00 35.94 ? 289 LEU A C 1 ATOM 1933 O O . LEU A 1 248 ? 7.932 48.723 27.249 1.00 36.82 ? 289 LEU A O 1 ATOM 1934 C CB A LEU A 1 248 ? 5.962 46.830 28.738 0.65 35.87 ? 289 LEU A CB 1 ATOM 1935 C CB B LEU A 1 248 ? 5.955 46.833 28.760 0.35 36.01 ? 289 LEU A CB 1 ATOM 1936 C CG A LEU A 1 248 ? 4.851 46.435 29.726 0.65 36.56 ? 289 LEU A CG 1 ATOM 1937 C CG B LEU A 1 248 ? 5.350 45.778 29.697 0.35 36.43 ? 289 LEU A CG 1 ATOM 1938 C CD1 A LEU A 1 248 ? 3.785 45.635 29.015 0.65 37.32 ? 289 LEU A CD1 1 ATOM 1939 C CD1 B LEU A 1 248 ? 4.762 46.405 30.973 0.35 35.63 ? 289 LEU A CD1 1 ATOM 1940 C CD2 A LEU A 1 248 ? 5.392 45.648 30.943 0.65 36.87 ? 289 LEU A CD2 1 ATOM 1941 C CD2 B LEU A 1 248 ? 4.299 44.961 28.965 0.35 37.43 ? 289 LEU A CD2 1 ATOM 1942 N N . PRO A 1 249 ? 9.191 46.978 27.954 1.00 36.11 ? 290 PRO A N 1 ATOM 1943 C CA . PRO A 1 249 ? 10.132 47.152 26.842 1.00 36.03 ? 290 PRO A CA 1 ATOM 1944 C C . PRO A 1 249 ? 9.470 46.763 25.539 1.00 36.74 ? 290 PRO A C 1 ATOM 1945 O O . PRO A 1 249 ? 8.586 45.914 25.523 1.00 35.67 ? 290 PRO A O 1 ATOM 1946 C CB . PRO A 1 249 ? 11.268 46.163 27.146 1.00 37.23 ? 290 PRO A CB 1 ATOM 1947 C CG . PRO A 1 249 ? 10.818 45.333 28.281 1.00 37.21 ? 290 PRO A CG 1 ATOM 1948 C CD . PRO A 1 249 ? 9.639 45.976 28.943 1.00 35.94 ? 290 PRO A CD 1 ATOM 1949 N N . SER A 1 250 ? 9.934 47.361 24.451 1.00 36.75 ? 291 SER A N 1 ATOM 1950 C CA . SER A 1 250 ? 9.316 47.168 23.138 1.00 38.19 ? 291 SER A CA 1 ATOM 1951 C C . SER A 1 250 ? 10.128 46.243 22.226 1.00 37.56 ? 291 SER A C 1 ATOM 1952 O O . SER A 1 250 ? 9.724 45.952 21.082 1.00 37.80 ? 291 SER A O 1 ATOM 1953 C CB . SER A 1 250 ? 9.126 48.532 22.468 1.00 40.23 ? 291 SER A CB 1 ATOM 1954 O OG . SER A 1 250 ? 10.393 49.153 22.226 1.00 44.52 ? 291 SER A OG 1 ATOM 1955 N N . ILE A 1 251 ? 11.296 45.810 22.713 1.00 35.41 ? 292 ILE A N 1 ATOM 1956 C CA . ILE A 1 251 ? 12.191 44.945 21.895 1.00 34.94 ? 292 ILE A CA 1 ATOM 1957 C C . ILE A 1 251 ? 12.592 43.728 22.743 1.00 34.25 ? 292 ILE A C 1 ATOM 1958 O O . ILE A 1 251 ? 12.713 43.867 23.957 1.00 32.02 ? 292 ILE A O 1 ATOM 1959 C CB . ILE A 1 251 ? 13.442 45.706 21.323 1.00 34.95 ? 292 ILE A CB 1 ATOM 1960 C CG1 . ILE A 1 251 ? 14.294 46.365 22.410 1.00 33.88 ? 292 ILE A CG1 1 ATOM 1961 C CG2 . ILE A 1 251 ? 13.007 46.744 20.278 1.00 37.98 ? 292 ILE A CG2 1 ATOM 1962 C CD1 . ILE A 1 251 ? 15.586 47.034 21.862 1.00 34.54 ? 292 ILE A CD1 1 ATOM 1963 N N . PRO A 1 252 ? 12.749 42.543 22.132 1.00 33.91 ? 293 PRO A N 1 ATOM 1964 C CA . PRO A 1 252 ? 13.193 41.355 22.917 1.00 33.94 ? 293 PRO A CA 1 ATOM 1965 C C . PRO A 1 252 ? 14.585 41.481 23.555 1.00 33.51 ? 293 PRO A C 1 ATOM 1966 O O . PRO A 1 252 ? 15.486 42.101 22.973 1.00 33.60 ? 293 PRO A O 1 ATOM 1967 C CB . PRO A 1 252 ? 13.231 40.245 21.877 1.00 35.18 ? 293 PRO A CB 1 ATOM 1968 C CG . PRO A 1 252 ? 12.288 40.744 20.762 1.00 36.58 ? 293 PRO A CG 1 ATOM 1969 C CD . PRO A 1 252 ? 12.566 42.200 20.701 1.00 34.91 ? 293 PRO A CD 1 ATOM 1970 N N . VAL A 1 253 ? 14.748 40.890 24.749 1.00 30.93 ? 294 VAL A N 1 ATOM 1971 C CA . VAL A 1 253 ? 15.969 41.014 25.537 1.00 28.86 ? 294 VAL A CA 1 ATOM 1972 C C . VAL A 1 253 ? 16.234 39.652 26.180 1.00 28.53 ? 294 VAL A C 1 ATOM 1973 O O . VAL A 1 253 ? 15.286 38.970 26.592 1.00 28.34 ? 294 VAL A O 1 ATOM 1974 C CB . VAL A 1 253 ? 15.807 42.051 26.644 1.00 28.57 ? 294 VAL A CB 1 ATOM 1975 C CG1 . VAL A 1 253 ? 17.114 42.228 27.422 1.00 28.39 ? 294 VAL A CG1 1 ATOM 1976 C CG2 . VAL A 1 253 ? 15.321 43.396 26.069 1.00 27.45 ? 294 VAL A CG2 1 ATOM 1977 N N . HIS A 1 254 ? 17.510 39.230 26.237 1.00 28.68 ? 295 HIS A N 1 ATOM 1978 C CA . HIS A 1 254 ? 17.824 37.956 26.893 1.00 27.85 ? 295 HIS A CA 1 ATOM 1979 C C . HIS A 1 254 ? 19.243 38.012 27.458 1.00 27.73 ? 295 HIS A C 1 ATOM 1980 O O . HIS A 1 254 ? 20.122 38.616 26.814 1.00 29.77 ? 295 HIS A O 1 ATOM 1981 C CB . HIS A 1 254 ? 17.700 36.815 25.851 1.00 29.51 ? 295 HIS A CB 1 ATOM 1982 C CG . HIS A 1 254 ? 17.733 35.438 26.441 1.00 28.45 ? 295 HIS A CG 1 ATOM 1983 N ND1 . HIS A 1 254 ? 16.744 34.970 27.287 1.00 28.01 ? 295 HIS A ND1 1 ATOM 1984 C CD2 . HIS A 1 254 ? 18.630 34.428 26.310 1.00 29.95 ? 295 HIS A CD2 1 ATOM 1985 C CE1 . HIS A 1 254 ? 17.035 33.738 27.660 1.00 28.92 ? 295 HIS A CE1 1 ATOM 1986 N NE2 . HIS A 1 254 ? 18.159 33.370 27.060 1.00 28.78 ? 295 HIS A NE2 1 ATOM 1987 N N . PRO A 1 255 ? 19.469 37.446 28.672 1.00 26.82 ? 296 PRO A N 1 ATOM 1988 C CA . PRO A 1 255 ? 20.808 37.474 29.263 1.00 26.28 ? 296 PRO A CA 1 ATOM 1989 C C . PRO A 1 255 ? 21.531 36.131 29.016 1.00 27.61 ? 296 PRO A C 1 ATOM 1990 O O . PRO A 1 255 ? 20.882 35.059 28.972 1.00 27.71 ? 296 PRO A O 1 ATOM 1991 C CB . PRO A 1 255 ? 20.507 37.669 30.776 1.00 25.39 ? 296 PRO A CB 1 ATOM 1992 C CG . PRO A 1 255 ? 19.201 36.846 30.969 1.00 26.01 ? 296 PRO A CG 1 ATOM 1993 C CD . PRO A 1 255 ? 18.475 36.869 29.606 1.00 25.93 ? 296 PRO A CD 1 ATOM 1994 N N . ILE A 1 256 ? 22.854 36.207 28.884 1.00 28.00 ? 297 ILE A N 1 ATOM 1995 C CA . ILE A 1 256 ? 23.703 35.017 28.689 1.00 28.35 ? 297 ILE A CA 1 ATOM 1996 C C . ILE A 1 256 ? 24.976 35.130 29.527 1.00 29.03 ? 297 ILE A C 1 ATOM 1997 O O . ILE A 1 256 ? 25.339 36.229 29.999 1.00 29.52 ? 297 ILE A O 1 ATOM 1998 C CB . ILE A 1 256 ? 24.079 34.813 27.174 1.00 30.12 ? 297 ILE A CB 1 ATOM 1999 C CG1 . ILE A 1 256 ? 24.918 35.994 26.661 1.00 30.67 ? 297 ILE A CG1 1 ATOM 2000 C CG2 . ILE A 1 256 ? 22.807 34.540 26.328 1.00 30.65 ? 297 ILE A CG2 1 ATOM 2001 C CD1 . ILE A 1 256 ? 25.404 35.807 25.207 1.00 31.66 ? 297 ILE A CD1 1 ATOM 2002 N N . GLY A 1 257 ? 25.667 34.002 29.687 1.00 28.63 ? 298 GLY A N 1 ATOM 2003 C CA . GLY A 1 257 ? 26.952 33.979 30.355 1.00 29.37 ? 298 GLY A CA 1 ATOM 2004 C C . GLY A 1 257 ? 28.116 34.203 29.412 1.00 30.83 ? 298 GLY A C 1 ATOM 2005 O O . GLY A 1 257 ? 27.942 34.367 28.181 1.00 31.02 ? 298 GLY A O 1 ATOM 2006 N N . TYR A 1 258 ? 29.320 34.220 29.982 1.00 30.62 ? 299 TYR A N 1 ATOM 2007 C CA . TYR A 1 258 ? 30.479 34.578 29.167 1.00 32.07 ? 299 TYR A CA 1 ATOM 2008 C C . TYR A 1 258 ? 30.984 33.485 28.238 1.00 33.49 ? 299 TYR A C 1 ATOM 2009 O O . TYR A 1 258 ? 31.535 33.811 27.197 1.00 34.62 ? 299 TYR A O 1 ATOM 2010 C CB . TYR A 1 258 ? 31.618 35.258 29.947 1.00 33.21 ? 299 TYR A CB 1 ATOM 2011 C CG . TYR A 1 258 ? 32.237 34.523 31.125 1.00 31.28 ? 299 TYR A CG 1 ATOM 2012 C CD1 . TYR A 1 258 ? 31.839 34.812 32.423 1.00 31.30 ? 299 TYR A CD1 1 ATOM 2013 C CD2 . TYR A 1 258 ? 33.303 33.627 30.939 1.00 34.15 ? 299 TYR A CD2 1 ATOM 2014 C CE1 . TYR A 1 258 ? 32.424 34.208 33.528 1.00 32.64 ? 299 TYR A CE1 1 ATOM 2015 C CE2 . TYR A 1 258 ? 33.901 33.001 32.040 1.00 33.68 ? 299 TYR A CE2 1 ATOM 2016 C CZ . TYR A 1 258 ? 33.453 33.298 33.332 1.00 30.77 ? 299 TYR A CZ 1 ATOM 2017 O OH . TYR A 1 258 ? 34.040 32.651 34.402 1.00 31.61 ? 299 TYR A OH 1 ATOM 2018 N N . TYR A 1 259 ? 30.745 32.213 28.551 1.00 32.66 ? 300 TYR A N 1 ATOM 2019 C CA . TYR A 1 259 ? 31.056 31.189 27.531 1.00 34.47 ? 300 TYR A CA 1 ATOM 2020 C C . TYR A 1 259 ? 30.239 31.435 26.243 1.00 35.07 ? 300 TYR A C 1 ATOM 2021 O O . TYR A 1 259 ? 30.777 31.405 25.140 1.00 36.03 ? 300 TYR A O 1 ATOM 2022 C CB . TYR A 1 259 ? 30.800 29.761 28.036 1.00 34.85 ? 300 TYR A CB 1 ATOM 2023 C CG . TYR A 1 259 ? 31.748 29.232 29.087 1.00 35.47 ? 300 TYR A CG 1 ATOM 2024 C CD1 . TYR A 1 259 ? 33.034 29.781 29.272 1.00 39.99 ? 300 TYR A CD1 1 ATOM 2025 C CD2 . TYR A 1 259 ? 31.384 28.128 29.869 1.00 38.60 ? 300 TYR A CD2 1 ATOM 2026 C CE1 . TYR A 1 259 ? 33.900 29.269 30.236 1.00 40.01 ? 300 TYR A CE1 1 ATOM 2027 C CE2 . TYR A 1 259 ? 32.262 27.600 30.827 1.00 39.80 ? 300 TYR A CE2 1 ATOM 2028 C CZ . TYR A 1 259 ? 33.510 28.177 31.004 1.00 40.81 ? 300 TYR A CZ 1 ATOM 2029 O OH . TYR A 1 259 ? 34.371 27.636 31.950 1.00 41.37 ? 300 TYR A OH 1 ATOM 2030 N N . ASP A 1 260 ? 28.941 31.692 26.393 1.00 34.03 ? 301 ASP A N 1 ATOM 2031 C CA . ASP A 1 260 ? 28.084 31.978 25.247 1.00 35.16 ? 301 ASP A CA 1 ATOM 2032 C C . ASP A 1 260 ? 28.380 33.324 24.590 1.00 35.29 ? 301 ASP A C 1 ATOM 2033 O O . ASP A 1 260 ? 28.371 33.419 23.366 1.00 36.03 ? 301 ASP A O 1 ATOM 2034 C CB . ASP A 1 260 ? 26.615 31.913 25.631 1.00 34.24 ? 301 ASP A CB 1 ATOM 2035 C CG . ASP A 1 260 ? 26.132 30.489 25.865 1.00 36.10 ? 301 ASP A CG 1 ATOM 2036 O OD1 . ASP A 1 260 ? 26.781 29.544 25.366 1.00 40.19 ? 301 ASP A OD1 1 ATOM 2037 O OD2 . ASP A 1 260 ? 25.069 30.323 26.528 1.00 35.66 ? 301 ASP A OD2 1 ATOM 2038 N N . ALA A 1 261 ? 28.659 34.347 25.394 1.00 34.15 ? 302 ALA A N 1 ATOM 2039 C CA . ALA A 1 261 ? 29.039 35.671 24.851 1.00 35.35 ? 302 ALA A CA 1 ATOM 2040 C C . ALA A 1 261 ? 30.275 35.574 23.955 1.00 36.67 ? 302 ALA A C 1 ATOM 2041 O O . ALA A 1 261 ? 30.335 36.225 22.894 1.00 38.47 ? 302 ALA A O 1 ATOM 2042 C CB . ALA A 1 261 ? 29.310 36.661 25.964 1.00 33.99 ? 302 ALA A CB 1 ATOM 2043 N N . GLN A 1 262 ? 31.272 34.805 24.402 1.00 36.91 ? 303 GLN A N 1 ATOM 2044 C CA . GLN A 1 262 ? 32.512 34.581 23.646 1.00 39.49 ? 303 GLN A CA 1 ATOM 2045 C C . GLN A 1 262 ? 32.206 34.110 22.222 1.00 40.97 ? 303 GLN A C 1 ATOM 2046 O O . GLN A 1 262 ? 32.793 34.611 21.255 1.00 41.56 ? 303 GLN A O 1 ATOM 2047 C CB . GLN A 1 262 ? 33.363 33.530 24.365 1.00 39.63 ? 303 GLN A CB 1 ATOM 2048 C CG . GLN A 1 262 ? 34.726 33.204 23.699 1.00 44.28 ? 303 GLN A CG 1 ATOM 2049 C CD . GLN A 1 262 ? 35.838 33.814 24.513 1.00 48.48 ? 303 GLN A CD 1 ATOM 2050 O OE1 . GLN A 1 262 ? 36.367 34.875 24.171 1.00 55.23 ? 303 GLN A OE1 1 ATOM 2051 N NE2 . GLN A 1 262 ? 36.151 33.189 25.639 1.00 47.74 ? 303 GLN A NE2 1 ATOM 2052 N N . LYS A 1 263 ? 31.277 33.158 22.100 1.00 41.19 ? 304 LYS A N 1 ATOM 2053 C CA . LYS A 1 263 ? 30.900 32.623 20.796 1.00 42.10 ? 304 LYS A CA 1 ATOM 2054 C C . LYS A 1 263 ? 30.233 33.689 19.933 1.00 42.46 ? 304 LYS A C 1 ATOM 2055 O O . LYS A 1 263 ? 30.332 33.654 18.710 1.00 44.32 ? 304 LYS A O 1 ATOM 2056 C CB . LYS A 1 263 ? 29.943 31.450 20.965 1.00 42.14 ? 304 LYS A CB 1 ATOM 2057 C CG . LYS A 1 263 ? 30.568 30.242 21.616 1.00 44.09 ? 304 LYS A CG 1 ATOM 2058 C CD . LYS A 1 263 ? 31.332 29.400 20.592 1.00 49.19 ? 304 LYS A CD 1 ATOM 2059 C CE . LYS A 1 263 ? 32.466 28.695 21.288 1.00 55.02 ? 304 LYS A CE 1 ATOM 2060 N NZ . LYS A 1 263 ? 33.473 29.691 21.785 1.00 57.27 ? 304 LYS A NZ 1 ATOM 2061 N N . LEU A 1 264 ? 29.546 34.632 20.566 1.00 40.49 ? 305 LEU A N 1 ATOM 2062 C CA . LEU A 1 264 ? 28.887 35.704 19.827 1.00 41.21 ? 305 LEU A CA 1 ATOM 2063 C C . LEU A 1 264 ? 29.832 36.847 19.452 1.00 42.03 ? 305 LEU A C 1 ATOM 2064 O O . LEU A 1 264 ? 29.687 37.437 18.379 1.00 44.38 ? 305 LEU A O 1 ATOM 2065 C CB . LEU A 1 264 ? 27.689 36.258 20.633 1.00 38.89 ? 305 LEU A CB 1 ATOM 2066 C CG . LEU A 1 264 ? 26.518 35.280 20.835 1.00 38.70 ? 305 LEU A CG 1 ATOM 2067 C CD1 . LEU A 1 264 ? 25.397 35.950 21.633 1.00 36.27 ? 305 LEU A CD1 1 ATOM 2068 C CD2 . LEU A 1 264 ? 25.940 34.780 19.529 1.00 41.65 ? 305 LEU A CD2 1 ATOM 2069 N N . LEU A 1 265 ? 30.782 37.173 20.325 1.00 41.05 ? 306 LEU A N 1 ATOM 2070 C CA . LEU A 1 265 ? 31.660 38.324 20.089 1.00 41.13 ? 306 LEU A CA 1 ATOM 2071 C C . LEU A 1 265 ? 32.848 38.002 19.186 1.00 43.54 ? 306 LEU A C 1 ATOM 2072 O O . LEU A 1 265 ? 33.424 38.914 18.571 1.00 44.14 ? 306 LEU A O 1 ATOM 2073 C CB . LEU A 1 265 ? 32.205 38.862 21.392 1.00 40.05 ? 306 LEU A CB 1 ATOM 2074 C CG . LEU A 1 265 ? 31.123 39.360 22.367 1.00 37.55 ? 306 LEU A CG 1 ATOM 2075 C CD1 . LEU A 1 265 ? 31.698 39.718 23.751 1.00 38.94 ? 306 LEU A CD1 1 ATOM 2076 C CD2 . LEU A 1 265 ? 30.404 40.568 21.779 1.00 38.59 ? 306 LEU A CD2 1 ATOM 2077 N N . GLU A 1 266 ? 33.232 36.730 19.134 1.00 44.75 ? 307 GLU A N 1 ATOM 2078 C CA . GLU A 1 266 ? 34.525 36.383 18.536 1.00 47.01 ? 307 GLU A CA 1 ATOM 2079 C C . GLU A 1 266 ? 34.611 36.677 17.037 1.00 49.11 ? 307 GLU A C 1 ATOM 2080 O O . GLU A 1 266 ? 35.705 36.893 16.503 1.00 50.43 ? 307 GLU A O 1 ATOM 2081 C CB . GLU A 1 266 ? 34.934 34.947 18.867 1.00 46.58 ? 307 GLU A CB 1 ATOM 2082 C CG . GLU A 1 266 ? 34.093 33.886 18.219 1.00 48.58 ? 307 GLU A CG 1 ATOM 2083 C CD . GLU A 1 266 ? 34.426 32.510 18.742 1.00 53.05 ? 307 GLU A CD 1 ATOM 2084 O OE1 . GLU A 1 266 ? 35.297 32.417 19.645 1.00 55.77 ? 307 GLU A OE1 1 ATOM 2085 O OE2 . GLU A 1 266 ? 33.826 31.524 18.247 1.00 53.48 ? 307 GLU A OE2 1 ATOM 2086 N N . LYS A 1 267 ? 33.462 36.701 16.367 1.00 49.78 ? 308 LYS A N 1 ATOM 2087 C CA . LYS A 1 267 ? 33.428 36.959 14.929 1.00 51.29 ? 308 LYS A CA 1 ATOM 2088 C C . LYS A 1 267 ? 33.179 38.436 14.619 1.00 51.51 ? 308 LYS A C 1 ATOM 2089 O O . LYS A 1 267 ? 33.182 38.840 13.460 1.00 51.28 ? 308 LYS A O 1 ATOM 2090 C CB . LYS A 1 267 ? 32.368 36.079 14.256 1.00 51.93 ? 308 LYS A CB 1 ATOM 2091 C CG . LYS A 1 267 ? 32.770 34.615 14.151 1.00 53.27 ? 308 LYS A CG 1 ATOM 2092 C CD . LYS A 1 267 ? 31.561 33.704 13.996 1.00 53.68 ? 308 LYS A CD 1 ATOM 2093 C CE . LYS A 1 267 ? 32.011 32.272 13.688 1.00 56.05 ? 308 LYS A CE 1 ATOM 2094 N NZ . LYS A 1 267 ? 30.856 31.366 13.409 1.00 57.27 ? 308 LYS A NZ 1 ATOM 2095 N N . MET A 1 268 ? 32.969 39.255 15.652 1.00 49.93 ? 309 MET A N 1 ATOM 2096 C CA . MET A 1 268 ? 32.646 40.672 15.415 1.00 50.71 ? 309 MET A CA 1 ATOM 2097 C C . MET A 1 268 ? 33.657 41.461 14.545 1.00 52.68 ? 309 MET A C 1 ATOM 2098 O O . MET A 1 268 ? 34.876 41.380 14.748 1.00 53.05 ? 309 MET A O 1 ATOM 2099 C CB . MET A 1 268 ? 32.313 41.389 16.722 1.00 49.22 ? 309 MET A CB 1 ATOM 2100 C CG A MET A 1 268 ? 30.949 40.872 17.218 0.50 47.73 ? 309 MET A CG 1 ATOM 2101 C CG B MET A 1 268 ? 31.110 40.874 17.455 0.50 49.32 ? 309 MET A CG 1 ATOM 2102 S SD A MET A 1 268 ? 29.963 41.877 18.326 0.50 43.90 ? 309 MET A SD 1 ATOM 2103 S SD B MET A 1 268 ? 29.675 41.577 16.689 0.50 50.38 ? 309 MET A SD 1 ATOM 2104 C CE A MET A 1 268 ? 29.648 43.355 17.354 0.50 44.73 ? 309 MET A CE 1 ATOM 2105 C CE B MET A 1 268 ? 30.010 43.335 16.850 0.50 51.25 ? 309 MET A CE 1 ATOM 2106 N N . GLY A 1 269 ? 33.120 42.200 13.568 1.00 53.62 ? 310 GLY A N 1 ATOM 2107 C CA . GLY A 1 269 ? 33.924 43.009 12.639 1.00 55.16 ? 310 GLY A CA 1 ATOM 2108 C C . GLY A 1 269 ? 33.669 44.503 12.741 1.00 55.72 ? 310 GLY A C 1 ATOM 2109 O O . GLY A 1 269 ? 33.438 45.036 13.844 1.00 54.18 ? 310 GLY A O 1 ATOM 2110 N N . GLY A 1 270 ? 33.713 45.192 11.596 1.00 57.28 ? 311 GLY A N 1 ATOM 2111 C CA . GLY A 1 270 ? 33.483 46.637 11.585 1.00 57.62 ? 311 GLY A CA 1 ATOM 2112 C C . GLY A 1 270 ? 34.571 47.364 12.353 1.00 58.42 ? 311 GLY A C 1 ATOM 2113 O O . GLY A 1 270 ? 35.738 46.966 12.322 1.00 59.78 ? 311 GLY A O 1 ATOM 2114 N N . SER A 1 271 ? 34.185 48.423 13.051 1.00 58.31 ? 312 SER A N 1 ATOM 2115 C CA . SER A 1 271 ? 35.126 49.298 13.746 1.00 59.49 ? 312 SER A CA 1 ATOM 2116 C C . SER A 1 271 ? 35.743 48.684 15.017 1.00 58.39 ? 312 SER A C 1 ATOM 2117 O O . SER A 1 271 ? 35.101 47.920 15.727 1.00 57.34 ? 312 SER A O 1 ATOM 2118 C CB . SER A 1 271 ? 34.420 50.623 14.076 1.00 59.50 ? 312 SER A CB 1 ATOM 2119 O OG . SER A 1 271 ? 35.318 51.590 14.606 1.00 62.81 ? 312 SER A OG 1 ATOM 2120 N N . ALA A 1 272 ? 37.000 49.019 15.288 1.00 59.11 ? 313 ALA A N 1 ATOM 2121 C CA . ALA A 1 272 ? 37.660 48.632 16.539 1.00 57.87 ? 313 ALA A CA 1 ATOM 2122 C C . ALA A 1 272 ? 37.017 49.346 17.739 1.00 56.45 ? 313 ALA A C 1 ATOM 2123 O O . ALA A 1 272 ? 36.333 50.357 17.554 1.00 56.02 ? 313 ALA A O 1 ATOM 2124 C CB . ALA A 1 272 ? 39.169 48.954 16.456 1.00 59.27 ? 313 ALA A CB 1 ATOM 2125 N N . PRO A 1 273 ? 37.225 48.823 18.969 1.00 55.02 ? 314 PRO A N 1 ATOM 2126 C CA . PRO A 1 273 ? 36.771 49.584 20.144 1.00 54.03 ? 314 PRO A CA 1 ATOM 2127 C C . PRO A 1 273 ? 37.482 50.944 20.198 1.00 54.56 ? 314 PRO A C 1 ATOM 2128 O O . PRO A 1 273 ? 38.667 51.028 19.861 1.00 55.67 ? 314 PRO A O 1 ATOM 2129 C CB . PRO A 1 273 ? 37.177 48.697 21.330 1.00 53.02 ? 314 PRO A CB 1 ATOM 2130 C CG . PRO A 1 273 ? 38.301 47.822 20.781 1.00 54.33 ? 314 PRO A CG 1 ATOM 2131 C CD . PRO A 1 273 ? 37.922 47.576 19.349 1.00 55.40 ? 314 PRO A CD 1 ATOM 2132 N N . PRO A 1 274 ? 36.764 52.010 20.600 1.00 54.16 ? 315 PRO A N 1 ATOM 2133 C CA . PRO A 1 274 ? 37.357 53.355 20.541 1.00 55.19 ? 315 PRO A CA 1 ATOM 2134 C C . PRO A 1 274 ? 38.553 53.534 21.479 1.00 55.98 ? 315 PRO A C 1 ATOM 2135 O O . PRO A 1 274 ? 39.415 54.374 21.227 1.00 56.80 ? 315 PRO A O 1 ATOM 2136 C CB . PRO A 1 274 ? 36.197 54.272 20.950 1.00 53.23 ? 315 PRO A CB 1 ATOM 2137 C CG . PRO A 1 274 ? 35.274 53.371 21.771 1.00 51.68 ? 315 PRO A CG 1 ATOM 2138 C CD . PRO A 1 274 ? 35.365 52.043 21.071 1.00 52.22 ? 315 PRO A CD 1 ATOM 2139 N N . ASP A 1 275 ? 38.593 52.736 22.542 1.00 55.88 ? 316 ASP A N 1 ATOM 2140 C CA . ASP A 1 275 ? 39.641 52.791 23.569 1.00 56.69 ? 316 ASP A CA 1 ATOM 2141 C C . ASP A 1 275 ? 39.514 51.594 24.524 1.00 56.05 ? 316 ASP A C 1 ATOM 2142 O O . ASP A 1 275 ? 38.544 50.818 24.443 1.00 54.30 ? 316 ASP A O 1 ATOM 2143 C CB . ASP A 1 275 ? 39.602 54.132 24.346 1.00 56.89 ? 316 ASP A CB 1 ATOM 2144 C CG . ASP A 1 275 ? 38.318 54.322 25.157 1.00 56.79 ? 316 ASP A CG 1 ATOM 2145 O OD1 . ASP A 1 275 ? 37.958 53.407 25.920 1.00 59.10 ? 316 ASP A OD1 1 ATOM 2146 O OD2 . ASP A 1 275 ? 37.678 55.390 25.054 1.00 57.34 ? 316 ASP A OD2 1 ATOM 2147 N N . SER A 1 276 ? 40.465 51.480 25.452 1.00 55.90 ? 317 SER A N 1 ATOM 2148 C CA . SER A 1 276 ? 40.530 50.333 26.362 1.00 55.84 ? 317 SER A CA 1 ATOM 2149 C C . SER A 1 276 ? 39.367 50.218 27.376 1.00 53.44 ? 317 SER A C 1 ATOM 2150 O O . SER A 1 276 ? 39.173 49.139 27.953 1.00 53.22 ? 317 SER A O 1 ATOM 2151 C CB . SER A 1 276 ? 41.891 50.279 27.076 1.00 57.08 ? 317 SER A CB 1 ATOM 2152 O OG . SER A 1 276 ? 41.989 51.295 28.061 1.00 58.85 ? 317 SER A OG 1 ATOM 2153 N N . SER A 1 277 ? 38.608 51.302 27.602 1.00 52.02 ? 318 SER A N 1 ATOM 2154 C CA . SER A 1 277 ? 37.431 51.260 28.504 1.00 48.84 ? 318 SER A CA 1 ATOM 2155 C C . SER A 1 277 ? 36.237 50.507 27.890 1.00 47.42 ? 318 SER A C 1 ATOM 2156 O O . SER A 1 277 ? 35.239 50.201 28.586 1.00 46.06 ? 318 SER A O 1 ATOM 2157 C CB . SER A 1 277 ? 36.980 52.666 28.938 1.00 49.16 ? 318 SER A CB 1 ATOM 2158 O OG . SER A 1 277 ? 36.357 53.373 27.874 1.00 48.78 ? 318 SER A OG 1 ATOM 2159 N N . TRP A 1 278 ? 36.343 50.241 26.592 1.00 45.98 ? 319 TRP A N 1 ATOM 2160 C CA . TRP A 1 278 ? 35.383 49.434 25.847 1.00 44.32 ? 319 TRP A CA 1 ATOM 2161 C C . TRP A 1 278 ? 35.759 47.940 25.776 1.00 44.45 ? 319 TRP A C 1 ATOM 2162 O O . TRP A 1 278 ? 34.943 47.121 25.353 1.00 43.89 ? 319 TRP A O 1 ATOM 2163 C CB . TRP A 1 278 ? 35.195 50.003 24.436 1.00 44.77 ? 319 TRP A CB 1 ATOM 2164 C CG . TRP A 1 278 ? 34.226 51.154 24.420 1.00 44.46 ? 319 TRP A CG 1 ATOM 2165 C CD1 . TRP A 1 278 ? 34.322 52.330 25.140 1.00 41.98 ? 319 TRP A CD1 1 ATOM 2166 C CD2 . TRP A 1 278 ? 33.007 51.243 23.670 1.00 44.22 ? 319 TRP A CD2 1 ATOM 2167 N NE1 . TRP A 1 278 ? 33.243 53.137 24.872 1.00 43.87 ? 319 TRP A NE1 1 ATOM 2168 C CE2 . TRP A 1 278 ? 32.408 52.495 23.991 1.00 44.23 ? 319 TRP A CE2 1 ATOM 2169 C CE3 . TRP A 1 278 ? 32.353 50.388 22.767 1.00 43.22 ? 319 TRP A CE3 1 ATOM 2170 C CZ2 . TRP A 1 278 ? 31.189 52.906 23.444 1.00 42.95 ? 319 TRP A CZ2 1 ATOM 2171 C CZ3 . TRP A 1 278 ? 31.141 50.803 22.215 1.00 43.08 ? 319 TRP A CZ3 1 ATOM 2172 C CH2 . TRP A 1 278 ? 30.570 52.050 22.561 1.00 44.24 ? 319 TRP A CH2 1 ATOM 2173 N N . ARG A 1 279 ? 36.990 47.593 26.168 1.00 44.53 ? 320 ARG A N 1 ATOM 2174 C CA . ARG A 1 279 ? 37.435 46.191 26.143 1.00 44.64 ? 320 ARG A CA 1 ATOM 2175 C C . ARG A 1 279 ? 37.219 45.486 27.465 1.00 43.23 ? 320 ARG A C 1 ATOM 2176 O O . ARG A 1 279 ? 37.679 45.958 28.507 1.00 44.28 ? 320 ARG A O 1 ATOM 2177 C CB . ARG A 1 279 ? 38.925 46.083 25.787 1.00 45.87 ? 320 ARG A CB 1 ATOM 2178 C CG . ARG A 1 279 ? 39.237 46.333 24.341 1.00 49.73 ? 320 ARG A CG 1 ATOM 2179 C CD . ARG A 1 279 ? 40.689 45.942 24.059 1.00 56.52 ? 320 ARG A CD 1 ATOM 2180 N NE . ARG A 1 279 ? 41.092 46.351 22.724 1.00 63.62 ? 320 ARG A NE 1 ATOM 2181 C CZ . ARG A 1 279 ? 41.655 47.522 22.421 1.00 66.84 ? 320 ARG A CZ 1 ATOM 2182 N NH1 . ARG A 1 279 ? 41.891 48.437 23.369 1.00 65.85 ? 320 ARG A NH1 1 ATOM 2183 N NH2 . ARG A 1 279 ? 41.980 47.778 21.155 1.00 67.63 ? 320 ARG A NH2 1 ATOM 2184 N N . GLY A 1 280 ? 36.521 44.353 27.436 1.00 43.19 ? 321 GLY A N 1 ATOM 2185 C CA . GLY A 1 280 ? 36.434 43.482 28.619 1.00 41.33 ? 321 GLY A CA 1 ATOM 2186 C C . GLY A 1 280 ? 37.610 42.507 28.648 1.00 42.53 ? 321 GLY A C 1 ATOM 2187 O O . GLY A 1 280 ? 38.662 42.764 28.023 1.00 43.33 ? 321 GLY A O 1 ATOM 2188 N N . SER A 1 281 ? 37.444 41.384 29.354 1.00 41.53 ? 322 SER A N 1 ATOM 2189 C CA . SER A 1 281 ? 38.554 40.449 29.606 1.00 43.33 ? 322 SER A CA 1 ATOM 2190 C C . SER A 1 281 ? 38.570 39.226 28.700 1.00 42.62 ? 322 SER A C 1 ATOM 2191 O O . SER A 1 281 ? 39.451 38.373 28.826 1.00 44.23 ? 322 SER A O 1 ATOM 2192 C CB . SER A 1 281 ? 38.526 39.990 31.073 1.00 43.05 ? 322 SER A CB 1 ATOM 2193 O OG . SER A 1 281 ? 38.856 41.078 31.929 1.00 47.02 ? 322 SER A OG 1 ATOM 2194 N N . LEU A 1 282 ? 37.599 39.110 27.802 1.00 41.66 ? 323 LEU A N 1 ATOM 2195 C CA . LEU A 1 282 ? 37.543 37.918 26.955 1.00 40.95 ? 323 LEU A CA 1 ATOM 2196 C C . LEU A 1 282 ? 38.592 38.033 25.862 1.00 43.31 ? 323 LEU A C 1 ATOM 2197 O O . LEU A 1 282 ? 39.030 39.137 25.512 1.00 43.17 ? 323 LEU A O 1 ATOM 2198 C CB . LEU A 1 282 ? 36.162 37.707 26.335 1.00 40.67 ? 323 LEU A CB 1 ATOM 2199 C CG . LEU A 1 282 ? 35.015 37.417 27.324 1.00 37.57 ? 323 LEU A CG 1 ATOM 2200 C CD1 . LEU A 1 282 ? 33.648 37.566 26.605 1.00 36.81 ? 323 LEU A CD1 1 ATOM 2201 C CD2 . LEU A 1 282 ? 35.187 36.016 27.930 1.00 39.73 ? 323 LEU A CD2 1 ATOM 2202 N N . LYS A 1 283 ? 38.970 36.885 25.333 1.00 44.11 ? 324 LYS A N 1 ATOM 2203 C CA . LYS A 1 283 ? 39.983 36.847 24.280 1.00 47.03 ? 324 LYS A CA 1 ATOM 2204 C C . LYS A 1 283 ? 39.290 37.050 22.925 1.00 47.15 ? 324 LYS A C 1 ATOM 2205 O O . LYS A 1 283 ? 39.245 36.160 22.073 1.00 48.58 ? 324 LYS A O 1 ATOM 2206 C CB . LYS A 1 283 ? 40.861 35.584 24.404 1.00 48.09 ? 324 LYS A CB 1 ATOM 2207 C CG A LYS A 1 283 ? 41.343 35.342 25.856 0.50 49.08 ? 324 LYS A CG 1 ATOM 2208 C CG B LYS A 1 283 ? 41.564 35.452 25.769 0.50 49.39 ? 324 LYS A CG 1 ATOM 2209 C CD A LYS A 1 283 ? 42.356 34.193 26.031 0.50 50.58 ? 324 LYS A CD 1 ATOM 2210 C CD B LYS A 1 283 ? 42.634 36.531 26.002 0.50 50.34 ? 324 LYS A CD 1 ATOM 2211 C CE A LYS A 1 283 ? 42.770 34.104 27.510 0.50 51.26 ? 324 LYS A CE 1 ATOM 2212 C CE B LYS A 1 283 ? 42.862 36.775 27.489 0.50 50.09 ? 324 LYS A CE 1 ATOM 2213 N NZ A LYS A 1 283 ? 43.484 32.858 27.905 0.50 51.65 ? 324 LYS A NZ 1 ATOM 2214 N NZ B LYS A 1 283 ? 43.892 37.828 27.723 0.50 49.45 ? 324 LYS A NZ 1 ATOM 2215 N N . VAL A 1 284 ? 38.721 38.247 22.780 1.00 46.40 ? 325 VAL A N 1 ATOM 2216 C CA . VAL A 1 284 ? 38.075 38.712 21.557 1.00 47.10 ? 325 VAL A CA 1 ATOM 2217 C C . VAL A 1 284 ? 38.507 40.164 21.323 1.00 46.94 ? 325 VAL A C 1 ATOM 2218 O O . VAL A 1 284 ? 39.012 40.823 22.252 1.00 45.54 ? 325 VAL A O 1 ATOM 2219 C CB . VAL A 1 284 ? 36.516 38.624 21.609 1.00 46.39 ? 325 VAL A CB 1 ATOM 2220 C CG1 . VAL A 1 284 ? 36.037 37.179 21.752 1.00 48.00 ? 325 VAL A CG1 1 ATOM 2221 C CG2 . VAL A 1 284 ? 35.918 39.520 22.716 1.00 44.73 ? 325 VAL A CG2 1 ATOM 2222 N N . PRO A 1 285 ? 38.306 40.673 20.088 1.00 47.71 ? 326 PRO A N 1 ATOM 2223 C CA . PRO A 1 285 ? 38.761 42.037 19.797 1.00 48.31 ? 326 PRO A CA 1 ATOM 2224 C C . PRO A 1 285 ? 37.908 43.157 20.425 1.00 46.79 ? 326 PRO A C 1 ATOM 2225 O O . PRO A 1 285 ? 38.397 44.278 20.593 1.00 46.26 ? 326 PRO A O 1 ATOM 2226 C CB . PRO A 1 285 ? 38.750 42.116 18.258 1.00 50.04 ? 326 PRO A CB 1 ATOM 2227 C CG . PRO A 1 285 ? 37.921 40.931 17.782 1.00 50.97 ? 326 PRO A CG 1 ATOM 2228 C CD . PRO A 1 285 ? 37.814 39.944 18.896 1.00 48.49 ? 326 PRO A CD 1 ATOM 2229 N N . TYR A 1 286 ? 36.668 42.830 20.795 1.00 45.06 ? 327 TYR A N 1 ATOM 2230 C CA . TYR A 1 286 ? 35.664 43.827 21.269 1.00 44.29 ? 327 TYR A CA 1 ATOM 2231 C C . TYR A 1 286 ? 35.386 44.876 20.191 1.00 45.28 ? 327 TYR A C 1 ATOM 2232 O O . TYR A 1 286 ? 35.198 46.075 20.476 1.00 45.52 ? 327 TYR A O 1 ATOM 2233 C CB . TYR A 1 286 ? 36.059 44.469 22.597 1.00 43.75 ? 327 TYR A CB 1 ATOM 2234 C CG . TYR A 1 286 ? 35.938 43.507 23.743 1.00 42.19 ? 327 TYR A CG 1 ATOM 2235 C CD1 . TYR A 1 286 ? 34.712 43.301 24.368 1.00 39.00 ? 327 TYR A CD1 1 ATOM 2236 C CD2 . TYR A 1 286 ? 37.039 42.770 24.178 1.00 43.40 ? 327 TYR A CD2 1 ATOM 2237 C CE1 . TYR A 1 286 ? 34.598 42.408 25.413 1.00 40.20 ? 327 TYR A CE1 1 ATOM 2238 C CE2 . TYR A 1 286 ? 36.938 41.870 25.215 1.00 41.77 ? 327 TYR A CE2 1 ATOM 2239 C CZ . TYR A 1 286 ? 35.713 41.679 25.820 1.00 40.79 ? 327 TYR A CZ 1 ATOM 2240 O OH . TYR A 1 286 ? 35.602 40.791 26.858 1.00 40.50 ? 327 TYR A OH 1 ATOM 2241 N N . ASN A 1 287 ? 35.347 44.393 18.957 1.00 46.13 ? 328 ASN A N 1 ATOM 2242 C CA . ASN A 1 287 ? 34.998 45.205 17.817 1.00 47.83 ? 328 ASN A CA 1 ATOM 2243 C C . ASN A 1 287 ? 33.564 45.613 17.972 1.00 46.67 ? 328 ASN A C 1 ATOM 2244 O O . ASN A 1 287 ? 32.731 44.847 18.458 1.00 45.41 ? 328 ASN A O 1 ATOM 2245 C CB . ASN A 1 287 ? 35.176 44.432 16.510 1.00 48.06 ? 328 ASN A CB 1 ATOM 2246 C CG . ASN A 1 287 ? 36.642 44.306 16.081 1.00 51.07 ? 328 ASN A CG 1 ATOM 2247 O OD1 . ASN A 1 287 ? 37.502 45.092 16.500 1.00 52.35 ? 328 ASN A OD1 1 ATOM 2248 N ND2 . ASN A 1 287 ? 36.929 43.309 15.240 1.00 48.37 ? 328 ASN A ND2 1 ATOM 2249 N N . VAL A 1 288 ? 33.277 46.835 17.551 1.00 47.99 ? 329 VAL A N 1 ATOM 2250 C CA . VAL A 1 288 ? 31.959 47.409 17.778 1.00 47.32 ? 329 VAL A CA 1 ATOM 2251 C C . VAL A 1 288 ? 30.939 46.965 16.716 1.00 47.88 ? 329 VAL A C 1 ATOM 2252 O O . VAL A 1 288 ? 29.729 47.012 16.945 1.00 47.05 ? 329 VAL A O 1 ATOM 2253 C CB . VAL A 1 288 ? 32.065 48.951 17.910 1.00 47.59 ? 329 VAL A CB 1 ATOM 2254 C CG1 . VAL A 1 288 ? 30.693 49.611 17.831 1.00 47.58 ? 329 VAL A CG1 1 ATOM 2255 C CG2 . VAL A 1 288 ? 32.752 49.306 19.247 1.00 47.17 ? 329 VAL A CG2 1 ATOM 2256 N N . GLY A 1 289 ? 31.426 46.501 15.574 1.00 49.61 ? 330 GLY A N 1 ATOM 2257 C CA . GLY A 1 289 ? 30.544 46.129 14.476 1.00 51.04 ? 330 GLY A CA 1 ATOM 2258 C C . GLY A 1 289 ? 30.259 47.326 13.578 1.00 52.41 ? 330 GLY A C 1 ATOM 2259 O O . GLY A 1 289 ? 31.082 48.250 13.494 1.00 53.13 ? 330 GLY A O 1 ATOM 2260 N N . PRO A 1 290 ? 29.101 47.324 12.890 1.00 52.87 ? 331 PRO A N 1 ATOM 2261 C CA . PRO A 1 290 ? 28.060 46.290 12.921 1.00 52.48 ? 331 PRO A CA 1 ATOM 2262 C C . PRO A 1 290 ? 28.490 45.026 12.156 1.00 52.96 ? 331 PRO A C 1 ATOM 2263 O O . PRO A 1 290 ? 29.284 45.103 11.204 1.00 54.79 ? 331 PRO A O 1 ATOM 2264 C CB . PRO A 1 290 ? 26.898 46.973 12.190 1.00 52.59 ? 331 PRO A CB 1 ATOM 2265 C CG . PRO A 1 290 ? 27.641 47.753 11.065 1.00 55.13 ? 331 PRO A CG 1 ATOM 2266 C CD . PRO A 1 290 ? 28.855 48.313 11.810 1.00 54.63 ? 331 PRO A CD 1 ATOM 2267 N N . GLY A 1 291 ? 27.970 43.879 12.583 1.00 52.14 ? 332 GLY A N 1 ATOM 2268 C CA . GLY A 1 291 ? 28.152 42.603 11.884 1.00 53.02 ? 332 GLY A CA 1 ATOM 2269 C C . GLY A 1 291 ? 29.487 41.904 12.112 1.00 53.72 ? 332 GLY A C 1 ATOM 2270 O O . GLY A 1 291 ? 30.330 42.377 12.898 1.00 53.01 ? 332 GLY A O 1 ATOM 2271 N N . PHE A 1 292 ? 29.668 40.778 11.415 1.00 54.51 ? 333 PHE A N 1 ATOM 2272 C CA . PHE A 1 292 ? 30.839 39.899 11.561 1.00 54.66 ? 333 PHE A CA 1 ATOM 2273 C C . PHE A 1 292 ? 31.913 40.183 10.486 1.00 57.09 ? 333 PHE A C 1 ATOM 2274 O O . PHE A 1 292 ? 31.620 40.817 9.469 1.00 57.86 ? 333 PHE A O 1 ATOM 2275 C CB . PHE A 1 292 ? 30.420 38.413 11.477 1.00 53.98 ? 333 PHE A CB 1 ATOM 2276 C CG . PHE A 1 292 ? 29.544 37.925 12.631 1.00 53.15 ? 333 PHE A CG 1 ATOM 2277 C CD1 . PHE A 1 292 ? 28.582 36.931 12.412 1.00 52.36 ? 333 PHE A CD1 1 ATOM 2278 C CD2 . PHE A 1 292 ? 29.696 38.429 13.915 1.00 51.45 ? 333 PHE A CD2 1 ATOM 2279 C CE1 . PHE A 1 292 ? 27.772 36.456 13.447 1.00 53.66 ? 333 PHE A CE1 1 ATOM 2280 C CE2 . PHE A 1 292 ? 28.874 37.955 14.971 1.00 51.06 ? 333 PHE A CE2 1 ATOM 2281 C CZ . PHE A 1 292 ? 27.920 36.961 14.718 1.00 49.03 ? 333 PHE A CZ 1 ATOM 2282 N N . THR A 1 293 ? 33.138 39.701 10.719 1.00 57.91 ? 334 THR A N 1 ATOM 2283 C CA . THR A 1 293 ? 34.245 39.815 9.733 1.00 61.05 ? 334 THR A CA 1 ATOM 2284 C C . THR A 1 293 ? 34.025 38.982 8.470 1.00 63.09 ? 334 THR A C 1 ATOM 2285 O O . THR A 1 293 ? 33.360 37.948 8.509 1.00 62.94 ? 334 THR A O 1 ATOM 2286 C CB . THR A 1 293 ? 35.603 39.370 10.327 1.00 61.26 ? 334 THR A CB 1 ATOM 2287 O OG1 . THR A 1 293 ? 35.523 37.993 10.730 1.00 61.22 ? 334 THR A OG1 1 ATOM 2288 C CG2 . THR A 1 293 ? 35.992 40.230 11.517 1.00 61.89 ? 334 THR A CG2 1 ATOM 2289 N N . GLY A 1 294 ? 34.666 39.416 7.379 1.00 65.38 ? 335 GLY A N 1 ATOM 2290 C CA . GLY A 1 294 ? 34.532 38.841 6.034 1.00 67.57 ? 335 GLY A CA 1 ATOM 2291 C C . GLY A 1 294 ? 34.068 37.414 5.770 1.00 68.62 ? 335 GLY A C 1 ATOM 2292 O O . GLY A 1 294 ? 33.157 37.204 4.959 1.00 69.72 ? 335 GLY A O 1 ATOM 2293 N N . ASN A 1 295 ? 34.712 36.428 6.397 1.00 68.48 ? 336 ASN A N 1 ATOM 2294 C CA . ASN A 1 295 ? 34.336 35.015 6.211 1.00 69.12 ? 336 ASN A CA 1 ATOM 2295 C C . ASN A 1 295 ? 32.923 34.673 6.694 1.00 67.45 ? 336 ASN A C 1 ATOM 2296 O O . ASN A 1 295 ? 32.260 33.803 6.131 1.00 68.61 ? 336 ASN A O 1 ATOM 2297 C CB . ASN A 1 295 ? 35.344 34.090 6.910 1.00 69.57 ? 336 ASN A CB 1 ATOM 2298 C CG . ASN A 1 295 ? 36.651 33.940 6.138 1.00 73.21 ? 336 ASN A CG 1 ATOM 2299 O OD1 . ASN A 1 295 ? 36.902 34.645 5.152 1.00 76.65 ? 336 ASN A OD1 1 ATOM 2300 N ND2 . ASN A 1 295 ? 37.491 33.003 6.583 1.00 75.74 ? 336 ASN A ND2 1 ATOM 2301 N N . PHE A 1 296 ? 32.479 35.367 7.738 1.00 65.07 ? 337 PHE A N 1 ATOM 2302 C CA . PHE A 1 296 ? 31.189 35.098 8.358 1.00 62.84 ? 337 PHE A CA 1 ATOM 2303 C C . PHE A 1 296 ? 30.250 36.288 8.181 1.00 62.00 ? 337 PHE A C 1 ATOM 2304 O O . PHE A 1 296 ? 29.319 36.477 8.965 1.00 60.20 ? 337 PHE A O 1 ATOM 2305 C CB . PHE A 1 296 ? 31.375 34.803 9.853 1.00 61.48 ? 337 PHE A CB 1 ATOM 2306 C CG . PHE A 1 296 ? 32.617 34.012 10.171 1.00 61.66 ? 337 PHE A CG 1 ATOM 2307 C CD1 . PHE A 1 296 ? 33.784 34.662 10.585 1.00 62.23 ? 337 PHE A CD1 1 ATOM 2308 C CD2 . PHE A 1 296 ? 32.624 32.619 10.055 1.00 61.85 ? 337 PHE A CD2 1 ATOM 2309 C CE1 . PHE A 1 296 ? 34.942 33.937 10.877 1.00 62.66 ? 337 PHE A CE1 1 ATOM 2310 C CE2 . PHE A 1 296 ? 33.771 31.883 10.353 1.00 62.05 ? 337 PHE A CE2 1 ATOM 2311 C CZ . PHE A 1 296 ? 34.933 32.542 10.764 1.00 62.24 ? 337 PHE A CZ 1 ATOM 2312 N N . SER A 1 297 ? 30.497 37.086 7.148 1.00 62.43 ? 338 SER A N 1 ATOM 2313 C CA . SER A 1 297 ? 29.748 38.315 6.908 1.00 62.07 ? 338 SER A CA 1 ATOM 2314 C C . SER A 1 297 ? 28.277 38.046 6.616 1.00 61.12 ? 338 SER A C 1 ATOM 2315 O O . SER A 1 297 ? 27.434 38.942 6.791 1.00 60.89 ? 338 SER A O 1 ATOM 2316 C CB . SER A 1 297 ? 30.369 39.107 5.751 1.00 63.67 ? 338 SER A CB 1 ATOM 2317 O OG . SER A 1 297 ? 30.152 38.442 4.524 1.00 66.57 ? 338 SER A OG 1 ATOM 2318 N N . THR A 1 298 ? 27.977 36.814 6.203 1.00 60.97 ? 339 THR A N 1 ATOM 2319 C CA . THR A 1 298 ? 26.623 36.423 5.801 1.00 60.76 ? 339 THR A CA 1 ATOM 2320 C C . THR A 1 298 ? 25.824 35.751 6.921 1.00 59.49 ? 339 THR A C 1 ATOM 2321 O O . THR A 1 298 ? 24.622 35.498 6.773 1.00 59.63 ? 339 THR A O 1 ATOM 2322 C CB . THR A 1 298 ? 26.637 35.522 4.560 1.00 62.21 ? 339 THR A CB 1 ATOM 2323 O OG1 . THR A 1 298 ? 27.608 34.480 4.738 1.00 62.83 ? 339 THR A OG1 1 ATOM 2324 C CG2 . THR A 1 298 ? 26.988 36.347 3.315 1.00 63.31 ? 339 THR A CG2 1 ATOM 2325 N N . GLN A 1 299 ? 26.496 35.475 8.038 1.00 58.11 ? 340 GLN A N 1 ATOM 2326 C CA . GLN A 1 299 ? 25.827 35.010 9.262 1.00 55.98 ? 340 GLN A CA 1 ATOM 2327 C C . GLN A 1 299 ? 25.152 36.163 9.998 1.00 54.37 ? 340 GLN A C 1 ATOM 2328 O O . GLN A 1 299 ? 25.573 37.326 9.893 1.00 53.71 ? 340 GLN A O 1 ATOM 2329 C CB . GLN A 1 299 ? 26.814 34.231 10.150 1.00 55.40 ? 340 GLN A CB 1 ATOM 2330 C CG . GLN A 1 299 ? 27.399 32.981 9.414 1.00 57.82 ? 340 GLN A CG 1 ATOM 2331 C CD . GLN A 1 299 ? 28.493 32.211 10.179 1.00 59.45 ? 340 GLN A CD 1 ATOM 2332 O OE1 . GLN A 1 299 ? 28.923 32.601 11.265 1.00 59.16 ? 340 GLN A OE1 1 ATOM 2333 N NE2 . GLN A 1 299 ? 28.945 31.104 9.590 1.00 60.61 ? 340 GLN A NE2 1 ATOM 2334 N N . LYS A 1 300 ? 24.081 35.830 10.719 1.00 52.41 ? 341 LYS A N 1 ATOM 2335 C CA . LYS A 1 300 ? 23.342 36.792 11.525 1.00 50.37 ? 341 LYS A CA 1 ATOM 2336 C C . LYS A 1 300 ? 23.183 36.215 12.923 1.00 48.15 ? 341 LYS A C 1 ATOM 2337 O O . LYS A 1 300 ? 23.515 35.052 13.183 1.00 47.51 ? 341 LYS A O 1 ATOM 2338 C CB . LYS A 1 300 ? 21.937 37.059 10.959 1.00 50.55 ? 341 LYS A CB 1 ATOM 2339 C CG . LYS A 1 300 ? 21.834 37.261 9.467 1.00 54.57 ? 341 LYS A CG 1 ATOM 2340 C CD . LYS A 1 300 ? 22.233 38.655 9.058 1.00 58.19 ? 341 LYS A CD 1 ATOM 2341 C CE . LYS A 1 300 ? 22.769 38.586 7.620 1.00 61.79 ? 341 LYS A CE 1 ATOM 2342 N NZ . LYS A 1 300 ? 22.465 39.852 6.919 1.00 67.17 ? 341 LYS A NZ 1 ATOM 2343 N N . VAL A 1 301 ? 22.675 37.048 13.821 1.00 45.89 ? 342 VAL A N 1 ATOM 2344 C CA . VAL A 1 301 ? 22.276 36.572 15.133 1.00 44.09 ? 342 VAL A CA 1 ATOM 2345 C C . VAL A 1 301 ? 20.749 36.561 15.174 1.00 43.24 ? 342 VAL A C 1 ATOM 2346 O O . VAL A 1 301 ? 20.123 37.505 14.705 1.00 43.38 ? 342 VAL A O 1 ATOM 2347 C CB . VAL A 1 301 ? 22.859 37.467 16.251 1.00 43.11 ? 342 VAL A CB 1 ATOM 2348 C CG1 . VAL A 1 301 ? 22.170 37.181 17.575 1.00 40.99 ? 342 VAL A CG1 1 ATOM 2349 C CG2 . VAL A 1 301 ? 24.378 37.235 16.337 1.00 45.05 ? 342 VAL A CG2 1 ATOM 2350 N N . LYS A 1 302 ? 20.162 35.497 15.725 1.00 42.94 ? 343 LYS A N 1 ATOM 2351 C CA . LYS A 1 302 ? 18.710 35.394 15.881 1.00 42.97 ? 343 LYS A CA 1 ATOM 2352 C C . LYS A 1 302 ? 18.283 35.106 17.339 1.00 41.57 ? 343 LYS A C 1 ATOM 2353 O O . LYS A 1 302 ? 18.729 34.125 17.946 1.00 40.27 ? 343 LYS A O 1 ATOM 2354 C CB . LYS A 1 302 ? 18.180 34.281 14.997 1.00 44.69 ? 343 LYS A CB 1 ATOM 2355 C CG . LYS A 1 302 ? 16.683 34.008 15.088 1.00 45.03 ? 343 LYS A CG 1 ATOM 2356 C CD . LYS A 1 302 ? 16.360 32.961 14.019 1.00 51.29 ? 343 LYS A CD 1 ATOM 2357 C CE . LYS A 1 302 ? 14.934 32.455 14.099 1.00 55.59 ? 343 LYS A CE 1 ATOM 2358 N NZ . LYS A 1 302 ? 13.956 33.465 13.605 1.00 59.92 ? 343 LYS A NZ 1 ATOM 2359 N N . MET A 1 303 ? 17.392 35.940 17.862 1.00 41.11 ? 344 MET A N 1 ATOM 2360 C CA . MET A 1 303 ? 16.830 35.717 19.202 1.00 40.29 ? 344 MET A CA 1 ATOM 2361 C C . MET A 1 303 ? 15.543 34.893 19.089 1.00 40.98 ? 344 MET A C 1 ATOM 2362 O O . MET A 1 303 ? 14.848 34.952 18.071 1.00 40.90 ? 344 MET A O 1 ATOM 2363 C CB . MET A 1 303 ? 16.542 37.047 19.901 1.00 39.48 ? 344 MET A CB 1 ATOM 2364 C CG . MET A 1 303 ? 17.730 37.990 19.941 1.00 38.89 ? 344 MET A CG 1 ATOM 2365 S SD . MET A 1 303 ? 17.490 39.549 20.801 1.00 36.63 ? 344 MET A SD 1 ATOM 2366 C CE . MET A 1 303 ? 17.242 38.919 22.487 1.00 33.96 ? 344 MET A CE 1 ATOM 2367 N N . HIS A 1 304 ? 15.228 34.123 20.127 1.00 39.60 ? 345 HIS A N 1 ATOM 2368 C CA . HIS A 1 304 ? 13.953 33.413 20.205 1.00 39.22 ? 345 HIS A CA 1 ATOM 2369 C C . HIS A 1 304 ? 13.420 33.629 21.603 1.00 37.70 ? 345 HIS A C 1 ATOM 2370 O O . HIS A 1 304 ? 13.856 32.936 22.518 1.00 37.60 ? 345 HIS A O 1 ATOM 2371 C CB . HIS A 1 304 ? 14.124 31.920 20.057 1.00 40.21 ? 345 HIS A CB 1 ATOM 2372 C CG . HIS A 1 304 ? 14.984 31.518 18.903 1.00 42.47 ? 345 HIS A CG 1 ATOM 2373 N ND1 . HIS A 1 304 ? 16.356 31.630 18.944 1.00 44.37 ? 345 HIS A ND1 1 ATOM 2374 C CD2 . HIS A 1 304 ? 14.681 31.004 17.686 1.00 43.70 ? 345 HIS A CD2 1 ATOM 2375 C CE1 . HIS A 1 304 ? 16.865 31.216 17.798 1.00 43.66 ? 345 HIS A CE1 1 ATOM 2376 N NE2 . HIS A 1 304 ? 15.870 30.824 17.019 1.00 47.60 ? 345 HIS A NE2 1 ATOM 2377 N N . ILE A 1 305 ? 12.459 34.530 21.742 1.00 37.38 ? 346 ILE A N 1 ATOM 2378 C CA . ILE A 1 305 ? 11.946 34.900 23.089 1.00 36.13 ? 346 ILE A CA 1 ATOM 2379 C C . ILE A 1 305 ? 10.449 34.632 23.097 1.00 36.94 ? 346 ILE A C 1 ATOM 2380 O O . ILE A 1 305 ? 9.700 35.166 22.249 1.00 38.04 ? 346 ILE A O 1 ATOM 2381 C CB . ILE A 1 305 ? 12.241 36.381 23.456 1.00 35.88 ? 346 ILE A CB 1 ATOM 2382 C CG1 . ILE A 1 305 ? 13.741 36.709 23.307 1.00 36.65 ? 346 ILE A CG1 1 ATOM 2383 C CG2 . ILE A 1 305 ? 11.721 36.694 24.896 1.00 33.82 ? 346 ILE A CG2 1 ATOM 2384 C CD1 . ILE A 1 305 ? 14.708 35.854 24.181 1.00 37.13 ? 346 ILE A CD1 1 ATOM 2385 N N . HIS A 1 306 ? 10.007 33.808 24.045 1.00 36.11 ? 347 HIS A N 1 ATOM 2386 C CA . HIS A 1 306 ? 8.604 33.387 24.118 1.00 35.86 ? 347 HIS A CA 1 ATOM 2387 C C . HIS A 1 306 ? 7.970 33.538 25.505 1.00 33.68 ? 347 HIS A C 1 ATOM 2388 O O . HIS A 1 306 ? 6.918 32.933 25.792 1.00 33.57 ? 347 HIS A O 1 ATOM 2389 C CB . HIS A 1 306 ? 8.493 31.938 23.708 1.00 37.00 ? 347 HIS A CB 1 ATOM 2390 C CG . HIS A 1 306 ? 9.187 31.628 22.413 1.00 40.70 ? 347 HIS A CG 1 ATOM 2391 N ND1 . HIS A 1 306 ? 8.744 32.108 21.197 1.00 46.59 ? 347 HIS A ND1 1 ATOM 2392 C CD2 . HIS A 1 306 ? 10.304 30.911 22.153 1.00 42.60 ? 347 HIS A CD2 1 ATOM 2393 C CE1 . HIS A 1 306 ? 9.550 31.682 20.241 1.00 45.57 ? 347 HIS A CE1 1 ATOM 2394 N NE2 . HIS A 1 306 ? 10.497 30.943 20.793 1.00 45.91 ? 347 HIS A NE2 1 ATOM 2395 N N . SER A 1 307 ? 8.617 34.334 26.356 1.00 31.68 ? 348 SER A N 1 ATOM 2396 C CA . SER A 1 307 ? 8.108 34.566 27.699 1.00 30.27 ? 348 SER A CA 1 ATOM 2397 C C . SER A 1 307 ? 6.736 35.224 27.611 1.00 31.21 ? 348 SER A C 1 ATOM 2398 O O . SER A 1 307 ? 6.435 35.881 26.622 1.00 32.24 ? 348 SER A O 1 ATOM 2399 C CB . SER A 1 307 ? 9.058 35.509 28.442 1.00 28.79 ? 348 SER A CB 1 ATOM 2400 O OG . SER A 1 307 ? 10.380 34.952 28.457 1.00 29.50 ? 348 SER A OG 1 ATOM 2401 N N . THR A 1 308 ? 5.934 35.089 28.671 1.00 30.92 ? 349 THR A N 1 ATOM 2402 C CA . THR A 1 308 ? 4.602 35.663 28.659 1.00 30.24 ? 349 THR A CA 1 ATOM 2403 C C . THR A 1 308 ? 4.392 36.470 29.908 1.00 30.04 ? 349 THR A C 1 ATOM 2404 O O . THR A 1 308 ? 4.911 36.113 30.969 1.00 29.66 ? 349 THR A O 1 ATOM 2405 C CB . THR A 1 308 ? 3.515 34.595 28.677 1.00 32.22 ? 349 THR A CB 1 ATOM 2406 O OG1 . THR A 1 308 ? 3.724 33.742 29.808 1.00 36.51 ? 349 THR A OG1 1 ATOM 2407 C CG2 . THR A 1 308 ? 3.561 33.748 27.411 1.00 32.06 ? 349 THR A CG2 1 ATOM 2408 N N . ASN A 1 309 ? 3.644 37.545 29.767 1.00 28.31 ? 350 ASN A N 1 ATOM 2409 C CA . ASN A 1 309 ? 3.266 38.345 30.938 1.00 28.38 ? 350 ASN A CA 1 ATOM 2410 C C . ASN A 1 309 ? 1.906 37.867 31.416 1.00 28.82 ? 350 ASN A C 1 ATOM 2411 O O . ASN A 1 309 ? 1.020 37.601 30.617 1.00 31.05 ? 350 ASN A O 1 ATOM 2412 C CB . ASN A 1 309 ? 3.154 39.823 30.560 1.00 28.70 ? 350 ASN A CB 1 ATOM 2413 C CG . ASN A 1 309 ? 4.460 40.388 30.065 1.00 30.61 ? 350 ASN A CG 1 ATOM 2414 O OD1 . ASN A 1 309 ? 5.535 39.959 30.480 1.00 30.35 ? 350 ASN A OD1 1 ATOM 2415 N ND2 . ASN A 1 309 ? 4.375 41.340 29.140 1.00 35.36 ? 350 ASN A ND2 1 ATOM 2416 N N . GLU A 1 310 ? 1.722 37.769 32.724 1.00 27.84 ? 351 GLU A N 1 ATOM 2417 C CA . GLU A 1 310 ? 0.543 37.098 33.296 1.00 28.61 ? 351 GLU A CA 1 ATOM 2418 C C . GLU A 1 310 ? 0.191 37.793 34.613 1.00 26.48 ? 351 GLU A C 1 ATOM 2419 O O . GLU A 1 310 ? 1.052 37.930 35.478 1.00 25.45 ? 351 GLU A O 1 ATOM 2420 C CB . GLU A 1 310 ? 0.906 35.623 33.643 1.00 30.50 ? 351 GLU A CB 1 ATOM 2421 C CG A GLU A 1 310 ? 1.026 34.647 32.448 0.50 34.07 ? 351 GLU A CG 1 ATOM 2422 C CG B GLU A 1 310 ? 1.604 34.806 32.522 0.50 34.62 ? 351 GLU A CG 1 ATOM 2423 C CD A GLU A 1 310 ? 1.151 33.182 32.881 0.50 36.55 ? 351 GLU A CD 1 ATOM 2424 C CD B GLU A 1 310 ? 0.628 34.157 31.543 0.50 39.63 ? 351 GLU A CD 1 ATOM 2425 O OE1 A GLU A 1 310 ? 0.651 32.309 32.138 0.50 40.26 ? 351 GLU A OE1 1 ATOM 2426 O OE1 B GLU A 1 310 ? 1.089 33.672 30.481 0.50 42.81 ? 351 GLU A OE1 1 ATOM 2427 O OE2 A GLU A 1 310 ? 1.742 32.890 33.951 0.50 36.62 ? 351 GLU A OE2 1 ATOM 2428 O OE2 B GLU A 1 310 ? -0.591 34.103 31.829 0.50 41.91 ? 351 GLU A OE2 1 ATOM 2429 N N . VAL A 1 311 ? -1.065 38.199 34.773 1.00 25.58 ? 352 VAL A N 1 ATOM 2430 C CA . VAL A 1 311 ? -1.492 38.742 36.076 1.00 24.62 ? 352 VAL A CA 1 ATOM 2431 C C . VAL A 1 311 ? -1.551 37.592 37.077 1.00 24.70 ? 352 VAL A C 1 ATOM 2432 O O . VAL A 1 311 ? -2.228 36.555 36.834 1.00 25.97 ? 352 VAL A O 1 ATOM 2433 C CB . VAL A 1 311 ? -2.854 39.433 35.971 1.00 24.01 ? 352 VAL A CB 1 ATOM 2434 C CG1 . VAL A 1 311 ? -3.334 39.859 37.363 1.00 25.32 ? 352 VAL A CG1 1 ATOM 2435 C CG2 . VAL A 1 311 ? -2.774 40.656 35.032 1.00 25.14 ? 352 VAL A CG2 1 ATOM 2436 N N . THR A 1 312 ? -0.876 37.795 38.222 1.00 22.63 ? 353 THR A N 1 ATOM 2437 C CA . THR A 1 312 ? -0.536 36.722 39.172 1.00 22.52 ? 353 THR A CA 1 ATOM 2438 C C . THR A 1 312 ? -0.674 37.287 40.600 1.00 21.81 ? 353 THR A C 1 ATOM 2439 O O . THR A 1 312 ? -0.303 38.450 40.839 1.00 21.60 ? 353 THR A O 1 ATOM 2440 C CB . THR A 1 312 ? 0.904 36.231 38.911 1.00 24.02 ? 353 THR A CB 1 ATOM 2441 O OG1 . THR A 1 312 ? 1.038 35.893 37.509 1.00 27.32 ? 353 THR A OG1 1 ATOM 2442 C CG2 . THR A 1 312 ? 1.232 35.002 39.718 1.00 24.61 ? 353 THR A CG2 1 ATOM 2443 N N . ARG A 1 313 ? -1.153 36.463 41.532 1.00 22.68 ? 354 ARG A N 1 ATOM 2444 C CA . ARG A 1 313 ? -1.324 36.915 42.918 1.00 22.54 ? 354 ARG A CA 1 ATOM 2445 C C . ARG A 1 313 ? 0.034 36.900 43.631 1.00 22.35 ? 354 ARG A C 1 ATOM 2446 O O . ARG A 1 313 ? 0.815 35.927 43.509 1.00 23.86 ? 354 ARG A O 1 ATOM 2447 C CB . ARG A 1 313 ? -2.351 36.020 43.679 1.00 23.95 ? 354 ARG A CB 1 ATOM 2448 C CG . ARG A 1 313 ? -2.691 36.569 45.093 1.00 23.79 ? 354 ARG A CG 1 ATOM 2449 C CD . ARG A 1 313 ? -4.101 36.094 45.485 1.00 27.70 ? 354 ARG A CD 1 ATOM 2450 N NE . ARG A 1 313 ? -5.079 36.871 44.727 1.00 28.15 ? 354 ARG A NE 1 ATOM 2451 C CZ . ARG A 1 313 ? -6.381 36.848 44.960 1.00 32.23 ? 354 ARG A CZ 1 ATOM 2452 N NH1 . ARG A 1 313 ? -6.844 36.053 45.918 1.00 32.16 ? 354 ARG A NH1 1 ATOM 2453 N NH2 . ARG A 1 313 ? -7.199 37.638 44.267 1.00 33.16 ? 354 ARG A NH2 1 ATOM 2454 N N . ILE A 1 314 ? 0.272 37.951 44.414 1.00 20.48 ? 355 ILE A N 1 ATOM 2455 C CA . ILE A 1 314 ? 1.482 38.056 45.234 1.00 20.94 ? 355 ILE A CA 1 ATOM 2456 C C . ILE A 1 314 ? 1.026 38.344 46.657 1.00 21.73 ? 355 ILE A C 1 ATOM 2457 O O . ILE A 1 314 ? -0.076 38.810 46.852 1.00 22.01 ? 355 ILE A O 1 ATOM 2458 C CB . ILE A 1 314 ? 2.418 39.172 44.729 1.00 19.63 ? 355 ILE A CB 1 ATOM 2459 C CG1 . ILE A 1 314 ? 1.713 40.531 44.695 1.00 18.69 ? 355 ILE A CG1 1 ATOM 2460 C CG2 . ILE A 1 314 ? 2.856 38.789 43.313 1.00 20.02 ? 355 ILE A CG2 1 ATOM 2461 C CD1 . ILE A 1 314 ? 2.722 41.742 44.577 1.00 19.19 ? 355 ILE A CD1 1 ATOM 2462 N N . TYR A 1 315 ? 1.915 38.106 47.615 1.00 21.28 ? 356 TYR A N 1 ATOM 2463 C CA . TYR A 1 315 ? 1.540 38.170 49.030 1.00 21.39 ? 356 TYR A CA 1 ATOM 2464 C C . TYR A 1 315 ? 2.629 38.864 49.823 1.00 20.13 ? 356 TYR A C 1 ATOM 2465 O O . TYR A 1 315 ? 3.749 38.333 49.958 1.00 21.05 ? 356 TYR A O 1 ATOM 2466 C CB . TYR A 1 315 ? 1.402 36.756 49.605 1.00 21.91 ? 356 TYR A CB 1 ATOM 2467 C CG . TYR A 1 315 ? 0.337 35.918 48.942 1.00 23.81 ? 356 TYR A CG 1 ATOM 2468 C CD1 . TYR A 1 315 ? -0.964 35.914 49.411 1.00 23.84 ? 356 TYR A CD1 1 ATOM 2469 C CD2 . TYR A 1 315 ? 0.653 35.185 47.805 1.00 24.18 ? 356 TYR A CD2 1 ATOM 2470 C CE1 . TYR A 1 315 ? -1.929 35.133 48.787 1.00 25.15 ? 356 TYR A CE1 1 ATOM 2471 C CE2 . TYR A 1 315 ? -0.323 34.380 47.168 1.00 25.26 ? 356 TYR A CE2 1 ATOM 2472 C CZ . TYR A 1 315 ? -1.592 34.405 47.664 1.00 24.55 ? 356 TYR A CZ 1 ATOM 2473 O OH . TYR A 1 315 ? -2.587 33.644 47.040 1.00 29.11 ? 356 TYR A OH 1 ATOM 2474 N N . ASN A 1 316 ? 2.279 39.962 50.487 1.00 20.29 ? 357 ASN A N 1 ATOM 2475 C CA . ASN A 1 316 ? 3.192 40.570 51.474 1.00 20.08 ? 357 ASN A CA 1 ATOM 2476 C C . ASN A 1 316 ? 2.811 40.081 52.852 1.00 20.86 ? 357 ASN A C 1 ATOM 2477 O O . ASN A 1 316 ? 1.622 39.928 53.143 1.00 24.14 ? 357 ASN A O 1 ATOM 2478 C CB . ASN A 1 316 ? 3.015 42.097 51.508 1.00 19.33 ? 357 ASN A CB 1 ATOM 2479 C CG . ASN A 1 316 ? 3.384 42.791 50.214 1.00 20.72 ? 357 ASN A CG 1 ATOM 2480 O OD1 . ASN A 1 316 ? 4.240 42.359 49.461 1.00 19.89 ? 357 ASN A OD1 1 ATOM 2481 N ND2 . ASN A 1 316 ? 2.716 43.939 49.968 1.00 21.88 ? 357 ASN A ND2 1 ATOM 2482 N N . VAL A 1 317 ? 3.788 39.840 53.712 1.00 19.97 ? 358 VAL A N 1 ATOM 2483 C CA . VAL A 1 317 ? 3.436 39.583 55.127 1.00 20.96 ? 358 VAL A CA 1 ATOM 2484 C C . VAL A 1 317 ? 3.645 40.903 55.892 1.00 21.06 ? 358 VAL A C 1 ATOM 2485 O O . VAL A 1 317 ? 4.688 41.527 55.748 1.00 21.15 ? 358 VAL A O 1 ATOM 2486 C CB . VAL A 1 317 ? 4.338 38.485 55.742 1.00 21.82 ? 358 VAL A CB 1 ATOM 2487 C CG1 . VAL A 1 317 ? 3.802 38.103 57.164 1.00 22.97 ? 358 VAL A CG1 1 ATOM 2488 C CG2 . VAL A 1 317 ? 4.409 37.257 54.852 1.00 23.24 ? 358 VAL A CG2 1 ATOM 2489 N N . ILE A 1 318 ? 2.646 41.316 56.685 1.00 21.71 ? 359 ILE A N 1 ATOM 2490 C CA . ILE A 1 318 ? 2.709 42.592 57.411 1.00 21.00 ? 359 ILE A CA 1 ATOM 2491 C C . ILE A 1 318 ? 2.467 42.317 58.891 1.00 21.37 ? 359 ILE A C 1 ATOM 2492 O O . ILE A 1 318 ? 1.392 41.856 59.250 1.00 22.92 ? 359 ILE A O 1 ATOM 2493 C CB . ILE A 1 318 ? 1.631 43.600 56.872 1.00 20.57 ? 359 ILE A CB 1 ATOM 2494 C CG1 . ILE A 1 318 ? 1.715 43.781 55.327 1.00 20.99 ? 359 ILE A CG1 1 ATOM 2495 C CG2 . ILE A 1 318 ? 1.767 44.961 57.625 1.00 22.77 ? 359 ILE A CG2 1 ATOM 2496 C CD1 . ILE A 1 318 ? 3.031 44.443 54.836 1.00 23.71 ? 359 ILE A CD1 1 ATOM 2497 N N . GLY A 1 319 ? 3.503 42.529 59.691 1.00 21.74 ? 360 GLY A N 1 ATOM 2498 C CA . GLY A 1 319 ? 3.421 42.265 61.171 1.00 22.60 ? 360 GLY A CA 1 ATOM 2499 C C . GLY A 1 319 ? 3.406 43.582 61.911 1.00 22.76 ? 360 GLY A C 1 ATOM 2500 O O . GLY A 1 319 ? 4.066 44.523 61.509 1.00 24.17 ? 360 GLY A O 1 ATOM 2501 N N . THR A 1 320 ? 2.616 43.662 62.980 1.00 23.52 ? 361 THR A N 1 ATOM 2502 C CA . THR A 1 320 ? 2.487 44.928 63.732 1.00 24.64 ? 361 THR A CA 1 ATOM 2503 C C . THR A 1 320 ? 2.879 44.669 65.176 1.00 25.60 ? 361 THR A C 1 ATOM 2504 O O . THR A 1 320 ? 2.435 43.711 65.784 1.00 26.20 ? 361 THR A O 1 ATOM 2505 C CB . THR A 1 320 ? 1.025 45.415 63.693 1.00 26.51 ? 361 THR A CB 1 ATOM 2506 O OG1 . THR A 1 320 ? 0.624 45.631 62.337 1.00 26.74 ? 361 THR A OG1 1 ATOM 2507 C CG2 . THR A 1 320 ? 0.813 46.720 64.426 1.00 27.94 ? 361 THR A CG2 1 ATOM 2508 N N . LEU A 1 321 ? 3.711 45.544 65.705 1.00 25.32 ? 362 LEU A N 1 ATOM 2509 C CA . LEU A 1 321 ? 4.010 45.589 67.146 1.00 26.37 ? 362 LEU A CA 1 ATOM 2510 C C . LEU A 1 321 ? 3.544 46.976 67.594 1.00 25.97 ? 362 LEU A C 1 ATOM 2511 O O . LEU A 1 321 ? 4.228 47.980 67.352 1.00 25.43 ? 362 LEU A O 1 ATOM 2512 C CB . LEU A 1 321 ? 5.521 45.410 67.345 1.00 26.46 ? 362 LEU A CB 1 ATOM 2513 C CG . LEU A 1 321 ? 6.010 45.449 68.815 1.00 30.85 ? 362 LEU A CG 1 ATOM 2514 C CD1 . LEU A 1 321 ? 5.172 44.575 69.731 1.00 34.49 ? 362 LEU A CD1 1 ATOM 2515 C CD2 . LEU A 1 321 ? 7.459 45.051 68.862 1.00 31.45 ? 362 LEU A CD2 1 ATOM 2516 N N . ARG A 1 322 ? 2.355 47.004 68.177 1.00 26.45 ? 363 ARG A N 1 ATOM 2517 C CA A ARG A 1 322 ? 1.705 48.267 68.576 0.60 26.78 ? 363 ARG A CA 1 ATOM 2518 C CA B ARG A 1 322 ? 1.675 48.247 68.631 0.40 27.41 ? 363 ARG A CA 1 ATOM 2519 C C . ARG A 1 322 ? 2.493 49.082 69.631 1.00 27.76 ? 363 ARG A C 1 ATOM 2520 O O . ARG A 1 322 ? 2.957 48.554 70.649 1.00 28.38 ? 363 ARG A O 1 ATOM 2521 C CB A ARG A 1 322 ? 0.306 47.954 69.097 0.60 27.56 ? 363 ARG A CB 1 ATOM 2522 C CB B ARG A 1 322 ? 0.337 47.902 69.308 0.40 28.54 ? 363 ARG A CB 1 ATOM 2523 C CG A ARG A 1 322 ? -0.490 49.152 69.524 0.60 27.28 ? 363 ARG A CG 1 ATOM 2524 C CG B ARG A 1 322 ? -0.664 47.150 68.457 0.40 30.52 ? 363 ARG A CG 1 ATOM 2525 C CD A ARG A 1 322 ? -1.820 48.703 70.049 0.60 31.42 ? 363 ARG A CD 1 ATOM 2526 C CD B ARG A 1 322 ? -2.039 47.123 69.131 0.40 37.83 ? 363 ARG A CD 1 ATOM 2527 N NE A ARG A 1 322 ? -1.654 48.113 71.377 0.60 37.87 ? 363 ARG A NE 1 ATOM 2528 N NE B ARG A 1 322 ? -2.436 45.802 69.588 0.40 41.05 ? 363 ARG A NE 1 ATOM 2529 C CZ A ARG A 1 322 ? -1.912 46.851 71.707 0.60 41.40 ? 363 ARG A CZ 1 ATOM 2530 C CZ B ARG A 1 322 ? -3.170 44.954 68.878 0.40 41.81 ? 363 ARG A CZ 1 ATOM 2531 N NH1 A ARG A 1 322 ? -2.374 45.990 70.808 0.60 42.09 ? 363 ARG A NH1 1 ATOM 2532 N NH1 B ARG A 1 322 ? -3.502 43.771 69.382 0.40 42.90 ? 363 ARG A NH1 1 ATOM 2533 N NH2 A ARG A 1 322 ? -1.736 46.463 72.960 0.60 42.35 ? 363 ARG A NH2 1 ATOM 2534 N NH2 B ARG A 1 322 ? -3.570 45.286 67.667 0.40 42.29 ? 363 ARG A NH2 1 ATOM 2535 N N . GLY A 1 323 ? 2.639 50.386 69.364 1.00 26.69 ? 364 GLY A N 1 ATOM 2536 C CA . GLY A 1 323 ? 3.351 51.296 70.255 1.00 26.79 ? 364 GLY A CA 1 ATOM 2537 C C . GLY A 1 323 ? 2.541 51.508 71.535 1.00 28.17 ? 364 GLY A C 1 ATOM 2538 O O . GLY A 1 323 ? 1.298 51.526 71.524 1.00 28.68 ? 364 GLY A O 1 ATOM 2539 N N . ALA A 1 324 ? 3.264 51.667 72.628 1.00 28.21 ? 365 ALA A N 1 ATOM 2540 C CA . ALA A 1 324 ? 2.640 51.955 73.930 1.00 30.05 ? 365 ALA A CA 1 ATOM 2541 C C . ALA A 1 324 ? 2.157 53.384 74.117 1.00 30.73 ? 365 ALA A C 1 ATOM 2542 O O . ALA A 1 324 ? 1.247 53.632 74.948 1.00 33.08 ? 365 ALA A O 1 ATOM 2543 C CB . ALA A 1 324 ? 3.614 51.614 75.015 1.00 29.56 ? 365 ALA A CB 1 ATOM 2544 N N . VAL A 1 325 ? 2.800 54.342 73.444 1.00 29.39 ? 366 VAL A N 1 ATOM 2545 C CA . VAL A 1 325 ? 2.541 55.760 73.720 1.00 30.77 ? 366 VAL A CA 1 ATOM 2546 C C . VAL A 1 325 ? 2.057 56.475 72.462 1.00 29.60 ? 366 VAL A C 1 ATOM 2547 O O . VAL A 1 325 ? 1.066 57.247 72.488 1.00 29.16 ? 366 VAL A O 1 ATOM 2548 C CB . VAL A 1 325 ? 3.791 56.460 74.310 1.00 32.64 ? 366 VAL A CB 1 ATOM 2549 C CG1 . VAL A 1 325 ? 3.532 57.951 74.543 1.00 32.13 ? 366 VAL A CG1 1 ATOM 2550 C CG2 . VAL A 1 325 ? 4.195 55.809 75.640 1.00 34.48 ? 366 VAL A CG2 1 ATOM 2551 N N . GLU A 1 326 ? 2.729 56.171 71.351 1.00 27.16 ? 367 GLU A N 1 ATOM 2552 C CA . GLU A 1 326 ? 2.348 56.755 70.046 1.00 26.89 ? 367 GLU A CA 1 ATOM 2553 C C . GLU A 1 326 ? 2.042 55.655 69.049 1.00 24.05 ? 367 GLU A C 1 ATOM 2554 O O . GLU A 1 326 ? 2.815 55.472 68.082 1.00 23.73 ? 367 GLU A O 1 ATOM 2555 C CB . GLU A 1 326 ? 3.439 57.670 69.505 1.00 27.36 ? 367 GLU A CB 1 ATOM 2556 C CG . GLU A 1 326 ? 3.772 58.845 70.447 1.00 29.71 ? 367 GLU A CG 1 ATOM 2557 C CD . GLU A 1 326 ? 4.725 59.815 69.772 1.00 29.95 ? 367 GLU A CD 1 ATOM 2558 O OE1 . GLU A 1 326 ? 4.228 60.714 69.058 1.00 30.62 ? 367 GLU A OE1 1 ATOM 2559 O OE2 . GLU A 1 326 ? 5.954 59.728 70.021 1.00 32.24 ? 367 GLU A OE2 1 ATOM 2560 N N . PRO A 1 327 ? 0.910 54.950 69.225 1.00 24.96 ? 368 PRO A N 1 ATOM 2561 C CA . PRO A 1 327 ? 0.616 53.837 68.315 1.00 24.60 ? 368 PRO A CA 1 ATOM 2562 C C . PRO A 1 327 ? 0.278 54.302 66.914 1.00 24.08 ? 368 PRO A C 1 ATOM 2563 O O . PRO A 1 327 ? 0.328 53.483 65.998 1.00 23.71 ? 368 PRO A O 1 ATOM 2564 C CB . PRO A 1 327 ? -0.587 53.156 68.957 1.00 26.84 ? 368 PRO A CB 1 ATOM 2565 C CG . PRO A 1 327 ? -1.230 54.207 69.765 1.00 28.02 ? 368 PRO A CG 1 ATOM 2566 C CD . PRO A 1 327 ? -0.084 55.000 70.336 1.00 26.76 ? 368 PRO A CD 1 ATOM 2567 N N . ASP A 1 328 ? -0.022 55.584 66.760 1.00 23.11 ? 369 ASP A N 1 ATOM 2568 C CA . ASP A 1 328 ? -0.273 56.123 65.433 1.00 23.42 ? 369 ASP A CA 1 ATOM 2569 C C . ASP A 1 328 ? 0.967 56.717 64.822 1.00 22.29 ? 369 ASP A C 1 ATOM 2570 O O . ASP A 1 328 ? 0.848 57.583 63.903 1.00 21.62 ? 369 ASP A O 1 ATOM 2571 C CB . ASP A 1 328 ? -1.357 57.205 65.518 1.00 24.30 ? 369 ASP A CB 1 ATOM 2572 C CG . ASP A 1 328 ? -0.866 58.450 66.261 1.00 26.68 ? 369 ASP A CG 1 ATOM 2573 O OD1 . ASP A 1 328 ? 0.084 58.425 67.083 1.00 28.65 ? 369 ASP A OD1 1 ATOM 2574 O OD2 . ASP A 1 328 ? -1.465 59.541 66.043 1.00 30.07 ? 369 ASP A OD2 1 ATOM 2575 N N . ARG A 1 329 ? 2.151 56.225 65.196 1.00 22.23 ? 370 ARG A N 1 ATOM 2576 C CA . ARG A 1 329 ? 3.369 56.614 64.498 1.00 20.78 ? 370 ARG A CA 1 ATOM 2577 C C . ARG A 1 329 ? 4.050 55.317 64.135 1.00 21.40 ? 370 ARG A C 1 ATOM 2578 O O . ARG A 1 329 ? 4.191 54.426 64.979 1.00 22.29 ? 370 ARG A O 1 ATOM 2579 C CB . ARG A 1 329 ? 4.250 57.464 65.425 1.00 21.22 ? 370 ARG A CB 1 ATOM 2580 C CG . ARG A 1 329 ? 3.606 58.857 65.720 1.00 20.17 ? 370 ARG A CG 1 ATOM 2581 C CD . ARG A 1 329 ? 3.833 59.741 64.501 1.00 23.48 ? 370 ARG A CD 1 ATOM 2582 N NE . ARG A 1 329 ? 3.198 61.065 64.619 1.00 22.40 ? 370 ARG A NE 1 ATOM 2583 C CZ . ARG A 1 329 ? 1.960 61.374 64.189 1.00 20.69 ? 370 ARG A CZ 1 ATOM 2584 N NH1 . ARG A 1 329 ? 1.077 60.454 63.749 1.00 20.87 ? 370 ARG A NH1 1 ATOM 2585 N NH2 . ARG A 1 329 ? 1.571 62.653 64.202 1.00 22.45 ? 370 ARG A NH2 1 ATOM 2586 N N . TYR A 1 330 ? 4.407 55.189 62.851 1.00 19.89 ? 371 TYR A N 1 ATOM 2587 C CA . TYR A 1 330 ? 4.921 53.915 62.342 1.00 19.90 ? 371 TYR A CA 1 ATOM 2588 C C . TYR A 1 330 ? 6.377 54.000 61.970 1.00 20.67 ? 371 TYR A C 1 ATOM 2589 O O . TYR A 1 330 ? 6.812 54.862 61.166 1.00 21.03 ? 371 TYR A O 1 ATOM 2590 C CB . TYR A 1 330 ? 4.165 53.513 61.048 1.00 18.80 ? 371 TYR A CB 1 ATOM 2591 C CG . TYR A 1 330 ? 2.668 53.464 61.187 1.00 19.22 ? 371 TYR A CG 1 ATOM 2592 C CD1 . TYR A 1 330 ? 2.053 53.105 62.391 1.00 22.03 ? 371 TYR A CD1 1 ATOM 2593 C CD2 . TYR A 1 330 ? 1.844 53.745 60.093 1.00 19.74 ? 371 TYR A CD2 1 ATOM 2594 C CE1 . TYR A 1 330 ? 0.646 53.054 62.508 1.00 22.93 ? 371 TYR A CE1 1 ATOM 2595 C CE2 . TYR A 1 330 ? 0.458 53.692 60.194 1.00 20.91 ? 371 TYR A CE2 1 ATOM 2596 C CZ . TYR A 1 330 ? -0.149 53.319 61.383 1.00 22.08 ? 371 TYR A CZ 1 ATOM 2597 O OH . TYR A 1 330 ? -1.519 53.284 61.462 1.00 23.13 ? 371 TYR A OH 1 ATOM 2598 N N . VAL A 1 331 ? 7.142 53.056 62.498 1.00 20.13 ? 372 VAL A N 1 ATOM 2599 C CA . VAL A 1 331 ? 8.534 52.833 62.072 1.00 20.05 ? 372 VAL A CA 1 ATOM 2600 C C . VAL A 1 331 ? 8.497 51.486 61.343 1.00 19.78 ? 372 VAL A C 1 ATOM 2601 O O . VAL A 1 331 ? 8.042 50.488 61.898 1.00 21.12 ? 372 VAL A O 1 ATOM 2602 C CB . VAL A 1 331 ? 9.468 52.758 63.287 1.00 22.98 ? 372 VAL A CB 1 ATOM 2603 C CG1 . VAL A 1 331 ? 10.858 52.401 62.830 1.00 21.51 ? 372 VAL A CG1 1 ATOM 2604 C CG2 . VAL A 1 331 ? 9.521 54.129 63.989 1.00 22.20 ? 372 VAL A CG2 1 ATOM 2605 N N . ILE A 1 332 ? 8.951 51.469 60.088 1.00 18.52 ? 373 ILE A N 1 ATOM 2606 C CA . ILE A 1 332 ? 8.767 50.278 59.251 1.00 19.48 ? 373 ILE A CA 1 ATOM 2607 C C . ILE A 1 332 ? 10.113 49.647 58.956 1.00 19.50 ? 373 ILE A C 1 ATOM 2608 O O . ILE A 1 332 ? 11.039 50.333 58.534 1.00 20.54 ? 373 ILE A O 1 ATOM 2609 C CB . ILE A 1 332 ? 8.065 50.683 57.917 1.00 18.19 ? 373 ILE A CB 1 ATOM 2610 C CG1 . ILE A 1 332 ? 6.728 51.379 58.217 1.00 21.09 ? 373 ILE A CG1 1 ATOM 2611 C CG2 . ILE A 1 332 ? 7.830 49.426 57.002 1.00 20.10 ? 373 ILE A CG2 1 ATOM 2612 C CD1 . ILE A 1 332 ? 6.114 52.020 56.949 1.00 25.29 ? 373 ILE A CD1 1 ATOM 2613 N N . LEU A 1 333 ? 10.242 48.346 59.187 1.00 19.03 ? 374 LEU A N 1 ATOM 2614 C CA . LEU A 1 333 ? 11.419 47.557 58.718 1.00 18.05 ? 374 LEU A CA 1 ATOM 2615 C C . LEU A 1 333 ? 10.904 46.613 57.664 1.00 19.04 ? 374 LEU A C 1 ATOM 2616 O O . LEU A 1 333 ? 10.092 45.736 57.976 1.00 20.20 ? 374 LEU A O 1 ATOM 2617 C CB . LEU A 1 333 ? 11.979 46.763 59.897 1.00 20.12 ? 374 LEU A CB 1 ATOM 2618 C CG . LEU A 1 333 ? 13.130 45.801 59.548 1.00 20.13 ? 374 LEU A CG 1 ATOM 2619 C CD1 . LEU A 1 333 ? 14.366 46.558 59.055 1.00 23.22 ? 374 LEU A CD1 1 ATOM 2620 C CD2 . LEU A 1 333 ? 13.479 44.982 60.838 1.00 23.04 ? 374 LEU A CD2 1 ATOM 2621 N N . GLY A 1 334 ? 11.394 46.765 56.445 1.00 19.48 ? 375 GLY A N 1 ATOM 2622 C CA . GLY A 1 334 ? 10.801 45.961 55.333 1.00 18.54 ? 375 GLY A CA 1 ATOM 2623 C C . GLY A 1 334 ? 11.891 45.420 54.428 1.00 20.19 ? 375 GLY A C 1 ATOM 2624 O O . GLY A 1 334 ? 12.875 46.096 54.148 1.00 20.70 ? 375 GLY A O 1 ATOM 2625 N N . GLY A 1 335 ? 11.657 44.233 53.894 1.00 19.86 ? 376 GLY A N 1 ATOM 2626 C CA . GLY A 1 335 ? 12.566 43.726 52.874 1.00 19.65 ? 376 GLY A CA 1 ATOM 2627 C C . GLY A 1 335 ? 11.823 42.653 52.101 1.00 19.73 ? 376 GLY A C 1 ATOM 2628 O O . GLY A 1 335 ? 10.832 42.111 52.587 1.00 21.20 ? 376 GLY A O 1 ATOM 2629 N N . HIS A 1 336 ? 12.354 42.278 50.934 1.00 19.13 ? 377 HIS A N 1 ATOM 2630 C CA . HIS A 1 336 ? 11.593 41.305 50.140 1.00 19.16 ? 377 HIS A CA 1 ATOM 2631 C C . HIS A 1 336 ? 11.976 39.853 50.433 1.00 19.79 ? 377 HIS A C 1 ATOM 2632 O O . HIS A 1 336 ? 13.031 39.571 51.053 1.00 21.61 ? 377 HIS A O 1 ATOM 2633 C CB . HIS A 1 336 ? 11.676 41.667 48.624 1.00 19.01 ? 377 HIS A CB 1 ATOM 2634 C CG . HIS A 1 336 ? 12.981 41.341 47.937 1.00 19.08 ? 377 HIS A CG 1 ATOM 2635 N ND1 . HIS A 1 336 ? 13.105 40.261 47.077 1.00 19.52 ? 377 HIS A ND1 1 ATOM 2636 C CD2 . HIS A 1 336 ? 14.116 42.064 47.784 1.00 17.50 ? 377 HIS A CD2 1 ATOM 2637 C CE1 . HIS A 1 336 ? 14.292 40.291 46.494 1.00 21.29 ? 377 HIS A CE1 1 ATOM 2638 N NE2 . HIS A 1 336 ? 14.935 41.369 46.909 1.00 20.06 ? 377 HIS A NE2 1 ATOM 2639 N N . ARG A 1 337 ? 11.083 38.976 49.972 1.00 19.72 ? 378 ARG A N 1 ATOM 2640 C CA . ARG A 1 337 ? 11.124 37.527 50.226 1.00 20.01 ? 378 ARG A CA 1 ATOM 2641 C C . ARG A 1 337 ? 11.285 36.771 48.930 1.00 20.46 ? 378 ARG A C 1 ATOM 2642 O O . ARG A 1 337 ? 11.892 35.691 48.935 1.00 20.74 ? 378 ARG A O 1 ATOM 2643 C CB . ARG A 1 337 ? 9.799 37.117 50.854 1.00 21.63 ? 378 ARG A CB 1 ATOM 2644 C CG . ARG A 1 337 ? 9.745 35.656 51.265 1.00 22.73 ? 378 ARG A CG 1 ATOM 2645 C CD . ARG A 1 337 ? 8.337 35.333 51.820 1.00 24.22 ? 378 ARG A CD 1 ATOM 2646 N NE . ARG A 1 337 ? 7.307 35.361 50.755 1.00 22.81 ? 378 ARG A NE 1 ATOM 2647 C CZ . ARG A 1 337 ? 6.424 36.337 50.552 1.00 21.68 ? 378 ARG A CZ 1 ATOM 2648 N NH1 . ARG A 1 337 ? 6.338 37.415 51.364 1.00 20.84 ? 378 ARG A NH1 1 ATOM 2649 N NH2 . ARG A 1 337 ? 5.594 36.245 49.533 1.00 22.39 ? 378 ARG A NH2 1 ATOM 2650 N N . ASP A 1 338 ? 10.755 37.323 47.832 1.00 19.58 ? 379 ASP A N 1 ATOM 2651 C CA . ASP A 1 338 ? 10.834 36.633 46.518 1.00 19.32 ? 379 ASP A CA 1 ATOM 2652 C C . ASP A 1 338 ? 12.270 36.638 46.027 1.00 20.09 ? 379 ASP A C 1 ATOM 2653 O O . ASP A 1 338 ? 13.004 37.619 46.224 1.00 20.77 ? 379 ASP A O 1 ATOM 2654 C CB . ASP A 1 338 ? 9.893 37.318 45.525 1.00 19.01 ? 379 ASP A CB 1 ATOM 2655 C CG . ASP A 1 338 ? 10.362 38.711 45.160 1.00 19.47 ? 379 ASP A CG 1 ATOM 2656 O OD1 . ASP A 1 338 ? 10.414 39.588 46.061 1.00 19.26 ? 379 ASP A OD1 1 ATOM 2657 O OD2 . ASP A 1 338 ? 10.607 38.950 43.959 1.00 18.98 ? 379 ASP A OD2 1 ATOM 2658 N N . SER A 1 339 ? 12.671 35.565 45.337 1.00 20.68 ? 380 SER A N 1 ATOM 2659 C CA . SER A 1 339 ? 14.036 35.438 44.826 1.00 21.24 ? 380 SER A CA 1 ATOM 2660 C C . SER A 1 339 ? 13.965 34.974 43.385 1.00 21.67 ? 380 SER A C 1 ATOM 2661 O O . SER A 1 339 ? 12.914 34.460 42.929 1.00 22.88 ? 380 SER A O 1 ATOM 2662 C CB . SER A 1 339 ? 14.837 34.428 45.672 1.00 22.11 ? 380 SER A CB 1 ATOM 2663 O OG . SER A 1 339 ? 14.199 33.158 45.676 1.00 22.99 ? 380 SER A OG 1 ATOM 2664 N N . TRP A 1 340 ? 15.075 35.089 42.669 1.00 21.52 ? 381 TRP A N 1 ATOM 2665 C CA . TRP A 1 340 ? 15.103 34.575 41.306 1.00 21.44 ? 381 TRP A CA 1 ATOM 2666 C C . TRP A 1 340 ? 15.219 33.065 41.375 1.00 23.24 ? 381 TRP A C 1 ATOM 2667 O O . TRP A 1 340 ? 14.472 32.371 40.708 1.00 22.88 ? 381 TRP A O 1 ATOM 2668 C CB . TRP A 1 340 ? 16.248 35.186 40.450 1.00 23.18 ? 381 TRP A CB 1 ATOM 2669 C CG . TRP A 1 340 ? 15.805 36.531 39.940 1.00 22.61 ? 381 TRP A CG 1 ATOM 2670 C CD1 . TRP A 1 340 ? 16.367 37.772 40.233 1.00 23.02 ? 381 TRP A CD1 1 ATOM 2671 C CD2 . TRP A 1 340 ? 14.692 36.789 39.090 1.00 21.38 ? 381 TRP A CD2 1 ATOM 2672 N NE1 . TRP A 1 340 ? 15.660 38.767 39.598 1.00 23.70 ? 381 TRP A NE1 1 ATOM 2673 C CE2 . TRP A 1 340 ? 14.633 38.201 38.886 1.00 22.34 ? 381 TRP A CE2 1 ATOM 2674 C CE3 . TRP A 1 340 ? 13.731 35.958 38.459 1.00 23.04 ? 381 TRP A CE3 1 ATOM 2675 C CZ2 . TRP A 1 340 ? 13.640 38.803 38.107 1.00 22.87 ? 381 TRP A CZ2 1 ATOM 2676 C CZ3 . TRP A 1 340 ? 12.719 36.565 37.683 1.00 21.50 ? 381 TRP A CZ3 1 ATOM 2677 C CH2 . TRP A 1 340 ? 12.683 37.973 37.532 1.00 22.51 ? 381 TRP A CH2 1 ATOM 2678 N N . VAL A 1 341 ? 16.110 32.554 42.214 1.00 23.04 ? 382 VAL A N 1 ATOM 2679 C CA . VAL A 1 341 ? 16.215 31.105 42.419 1.00 23.63 ? 382 VAL A CA 1 ATOM 2680 C C . VAL A 1 341 ? 16.266 30.858 43.934 1.00 23.42 ? 382 VAL A C 1 ATOM 2681 O O . VAL A 1 341 ? 15.259 31.020 44.600 1.00 22.83 ? 382 VAL A O 1 ATOM 2682 C CB . VAL A 1 341 ? 17.358 30.425 41.609 1.00 24.72 ? 382 VAL A CB 1 ATOM 2683 C CG1 . VAL A 1 341 ? 17.149 28.889 41.645 1.00 25.87 ? 382 VAL A CG1 1 ATOM 2684 C CG2 . VAL A 1 341 ? 17.306 30.790 40.104 1.00 27.05 ? 382 VAL A CG2 1 ATOM 2685 N N . PHE A 1 342 ? 17.420 30.473 44.480 1.00 22.59 ? 383 PHE A N 1 ATOM 2686 C CA . PHE A 1 342 ? 17.492 30.167 45.904 1.00 23.28 ? 383 PHE A CA 1 ATOM 2687 C C . PHE A 1 342 ? 17.639 31.376 46.776 1.00 23.69 ? 383 PHE A C 1 ATOM 2688 O O . PHE A 1 342 ? 17.295 31.308 47.959 1.00 25.08 ? 383 PHE A O 1 ATOM 2689 C CB . PHE A 1 342 ? 18.626 29.165 46.199 1.00 23.76 ? 383 PHE A CB 1 ATOM 2690 C CG . PHE A 1 342 ? 18.477 27.892 45.412 1.00 24.79 ? 383 PHE A CG 1 ATOM 2691 C CD1 . PHE A 1 342 ? 17.464 26.972 45.725 1.00 25.91 ? 383 PHE A CD1 1 ATOM 2692 C CD2 . PHE A 1 342 ? 19.295 27.675 44.281 1.00 26.90 ? 383 PHE A CD2 1 ATOM 2693 C CE1 . PHE A 1 342 ? 17.321 25.771 44.935 1.00 26.80 ? 383 PHE A CE1 1 ATOM 2694 C CE2 . PHE A 1 342 ? 19.155 26.473 43.489 1.00 24.66 ? 383 PHE A CE2 1 ATOM 2695 C CZ . PHE A 1 342 ? 18.161 25.576 43.830 1.00 26.27 ? 383 PHE A CZ 1 ATOM 2696 N N . GLY A 1 343 ? 18.110 32.483 46.201 1.00 23.02 ? 384 GLY A N 1 ATOM 2697 C CA . GLY A 1 343 ? 18.188 33.760 46.976 1.00 22.43 ? 384 GLY A CA 1 ATOM 2698 C C . GLY A 1 343 ? 19.140 33.732 48.164 1.00 22.83 ? 384 GLY A C 1 ATOM 2699 O O . GLY A 1 343 ? 18.913 34.439 49.180 1.00 22.48 ? 384 GLY A O 1 ATOM 2700 N N . GLY A 1 344 ? 20.236 32.983 48.030 1.00 23.78 ? 385 GLY A N 1 ATOM 2701 C CA . GLY A 1 344 ? 21.185 32.817 49.135 1.00 24.01 ? 385 GLY A CA 1 ATOM 2702 C C . GLY A 1 344 ? 21.700 34.141 49.670 1.00 23.44 ? 385 GLY A C 1 ATOM 2703 O O . GLY A 1 344 ? 21.836 34.306 50.893 1.00 24.28 ? 385 GLY A O 1 ATOM 2704 N N . ILE A 1 345 ? 21.985 35.098 48.782 1.00 22.39 ? 386 ILE A N 1 ATOM 2705 C CA . ILE A 1 345 ? 22.270 36.441 49.251 1.00 22.13 ? 386 ILE A CA 1 ATOM 2706 C C . ILE A 1 345 ? 20.982 37.291 49.030 1.00 21.84 ? 386 ILE A C 1 ATOM 2707 O O . ILE A 1 345 ? 20.468 37.885 49.958 1.00 22.13 ? 386 ILE A O 1 ATOM 2708 C CB . ILE A 1 345 ? 23.490 37.054 48.511 1.00 21.42 ? 386 ILE A CB 1 ATOM 2709 C CG1 . ILE A 1 345 ? 24.759 36.320 48.998 1.00 25.51 ? 386 ILE A CG1 1 ATOM 2710 C CG2 . ILE A 1 345 ? 23.606 38.547 48.813 1.00 22.93 ? 386 ILE A CG2 1 ATOM 2711 C CD1 . ILE A 1 345 ? 26.020 36.718 48.236 1.00 27.30 ? 386 ILE A CD1 1 ATOM 2712 N N . ASP A 1 346 ? 20.501 37.340 47.796 1.00 21.51 ? 387 ASP A N 1 ATOM 2713 C CA . ASP A 1 346 ? 19.411 38.301 47.486 1.00 20.94 ? 387 ASP A CA 1 ATOM 2714 C C . ASP A 1 346 ? 18.074 37.516 47.369 1.00 20.95 ? 387 ASP A C 1 ATOM 2715 O O . ASP A 1 346 ? 17.901 36.812 46.367 1.00 21.21 ? 387 ASP A O 1 ATOM 2716 C CB . ASP A 1 346 ? 19.768 38.879 46.109 1.00 22.10 ? 387 ASP A CB 1 ATOM 2717 C CG . ASP A 1 346 ? 18.821 39.893 45.649 1.00 22.47 ? 387 ASP A CG 1 ATOM 2718 O OD1 . ASP A 1 346 ? 17.920 40.248 46.419 1.00 20.43 ? 387 ASP A OD1 1 ATOM 2719 O OD2 . ASP A 1 346 ? 18.965 40.299 44.468 1.00 20.93 ? 387 ASP A OD2 1 ATOM 2720 N N . PRO A 1 347 ? 17.151 37.627 48.320 1.00 20.21 ? 388 PRO A N 1 ATOM 2721 C CA . PRO A 1 347 ? 17.152 38.535 49.485 1.00 19.55 ? 388 PRO A CA 1 ATOM 2722 C C . PRO A 1 347 ? 17.313 37.825 50.810 1.00 21.33 ? 388 PRO A C 1 ATOM 2723 O O . PRO A 1 347 ? 17.203 38.482 51.851 1.00 21.48 ? 388 PRO A O 1 ATOM 2724 C CB . PRO A 1 347 ? 15.708 39.096 49.448 1.00 19.34 ? 388 PRO A CB 1 ATOM 2725 C CG . PRO A 1 347 ? 14.894 37.812 49.092 1.00 19.89 ? 388 PRO A CG 1 ATOM 2726 C CD . PRO A 1 347 ? 15.778 37.052 48.124 1.00 20.23 ? 388 PRO A CD 1 ATOM 2727 N N . GLN A 1 348 ? 17.534 36.508 50.825 1.00 22.16 ? 389 GLN A N 1 ATOM 2728 C CA . GLN A 1 348 ? 17.372 35.807 52.098 1.00 22.34 ? 389 GLN A CA 1 ATOM 2729 C C . GLN A 1 348 ? 18.423 36.158 53.156 1.00 22.77 ? 389 GLN A C 1 ATOM 2730 O O . GLN A 1 348 ? 18.127 36.027 54.347 1.00 22.93 ? 389 GLN A O 1 ATOM 2731 C CB . GLN A 1 348 ? 17.301 34.286 51.932 1.00 22.66 ? 389 GLN A CB 1 ATOM 2732 C CG . GLN A 1 348 ? 16.220 33.795 50.923 1.00 22.28 ? 389 GLN A CG 1 ATOM 2733 C CD . GLN A 1 348 ? 14.785 34.368 51.141 1.00 21.19 ? 389 GLN A CD 1 ATOM 2734 O OE1 . GLN A 1 348 ? 14.455 34.991 52.161 1.00 23.75 ? 389 GLN A OE1 1 ATOM 2735 N NE2 . GLN A 1 348 ? 13.915 34.139 50.133 1.00 23.18 ? 389 GLN A NE2 1 ATOM 2736 N N . SER A 1 349 ? 19.580 36.670 52.750 1.00 22.43 ? 390 SER A N 1 ATOM 2737 C CA A SER A 1 349 ? 20.539 37.161 53.753 0.50 23.74 ? 390 SER A CA 1 ATOM 2738 C CA B SER A 1 349 ? 20.565 37.211 53.692 0.50 24.05 ? 390 SER A CA 1 ATOM 2739 C C . SER A 1 349 ? 19.937 38.362 54.483 1.00 23.11 ? 390 SER A C 1 ATOM 2740 O O . SER A 1 349 ? 20.259 38.591 55.666 1.00 24.26 ? 390 SER A O 1 ATOM 2741 C CB A SER A 1 349 ? 21.916 37.491 53.145 0.50 24.20 ? 390 SER A CB 1 ATOM 2742 C CB B SER A 1 349 ? 21.801 37.680 52.908 0.50 24.40 ? 390 SER A CB 1 ATOM 2743 O OG A SER A 1 349 ? 21.864 38.628 52.311 0.50 22.55 ? 390 SER A OG 1 ATOM 2744 O OG B SER A 1 349 ? 22.505 38.700 53.568 0.50 25.18 ? 390 SER A OG 1 ATOM 2745 N N . GLY A 1 350 ? 19.059 39.108 53.818 1.00 21.85 ? 391 GLY A N 1 ATOM 2746 C CA . GLY A 1 350 ? 18.324 40.220 54.507 1.00 20.90 ? 391 GLY A CA 1 ATOM 2747 C C . GLY A 1 350 ? 17.134 39.681 55.283 1.00 20.94 ? 391 GLY A C 1 ATOM 2748 O O . GLY A 1 350 ? 16.914 40.086 56.438 1.00 21.57 ? 391 GLY A O 1 ATOM 2749 N N . ALA A 1 351 ? 16.343 38.804 54.667 1.00 20.56 ? 392 ALA A N 1 ATOM 2750 C CA . ALA A 1 351 ? 15.129 38.276 55.297 1.00 21.53 ? 392 ALA A CA 1 ATOM 2751 C C . ALA A 1 351 ? 15.424 37.499 56.595 1.00 22.04 ? 392 ALA A C 1 ATOM 2752 O O . ALA A 1 351 ? 14.652 37.586 57.558 1.00 22.42 ? 392 ALA A O 1 ATOM 2753 C CB . ALA A 1 351 ? 14.303 37.446 54.314 1.00 21.73 ? 392 ALA A CB 1 ATOM 2754 N N . ALA A 1 352 ? 16.567 36.816 56.622 1.00 22.19 ? 393 ALA A N 1 ATOM 2755 C CA . ALA A 1 352 ? 16.977 36.070 57.808 1.00 22.61 ? 393 ALA A CA 1 ATOM 2756 C C . ALA A 1 352 ? 17.281 37.040 58.922 1.00 23.55 ? 393 ALA A C 1 ATOM 2757 O O . ALA A 1 352 ? 17.011 36.754 60.097 1.00 23.91 ? 393 ALA A O 1 ATOM 2758 C CB . ALA A 1 352 ? 18.252 35.216 57.483 1.00 24.08 ? 393 ALA A CB 1 ATOM 2759 N N . VAL A 1 353 ? 17.861 38.183 58.556 1.00 23.23 ? 394 VAL A N 1 ATOM 2760 C CA . VAL A 1 353 ? 18.186 39.230 59.576 1.00 23.57 ? 394 VAL A CA 1 ATOM 2761 C C . VAL A 1 353 ? 16.881 39.867 60.118 1.00 23.36 ? 394 VAL A C 1 ATOM 2762 O O . VAL A 1 353 ? 16.727 40.087 61.370 1.00 23.33 ? 394 VAL A O 1 ATOM 2763 C CB . VAL A 1 353 ? 19.158 40.275 58.969 1.00 23.34 ? 394 VAL A CB 1 ATOM 2764 C CG1 . VAL A 1 353 ? 19.052 41.650 59.694 1.00 24.21 ? 394 VAL A CG1 1 ATOM 2765 C CG2 . VAL A 1 353 ? 20.628 39.704 59.010 1.00 23.48 ? 394 VAL A CG2 1 ATOM 2766 N N . VAL A 1 354 ? 15.927 40.146 59.207 1.00 22.85 ? 395 VAL A N 1 ATOM 2767 C CA . VAL A 1 354 ? 14.617 40.652 59.641 1.00 22.31 ? 395 VAL A CA 1 ATOM 2768 C C . VAL A 1 354 ? 13.959 39.651 60.598 1.00 23.49 ? 395 VAL A C 1 ATOM 2769 O O . VAL A 1 354 ? 13.435 40.037 61.630 1.00 23.06 ? 395 VAL A O 1 ATOM 2770 C CB . VAL A 1 354 ? 13.671 40.900 58.462 1.00 21.96 ? 395 VAL A CB 1 ATOM 2771 C CG1 . VAL A 1 354 ? 12.261 41.360 59.025 1.00 23.33 ? 395 VAL A CG1 1 ATOM 2772 C CG2 . VAL A 1 354 ? 14.235 42.017 57.578 1.00 23.09 ? 395 VAL A CG2 1 ATOM 2773 N N . HIS A 1 355 ? 14.051 38.362 60.272 1.00 23.60 ? 396 HIS A N 1 ATOM 2774 C CA . HIS A 1 355 ? 13.406 37.331 61.063 1.00 23.66 ? 396 HIS A CA 1 ATOM 2775 C C . HIS A 1 355 ? 13.974 37.344 62.489 1.00 25.15 ? 396 HIS A C 1 ATOM 2776 O O . HIS A 1 355 ? 13.213 37.311 63.473 1.00 26.52 ? 396 HIS A O 1 ATOM 2777 C CB . HIS A 1 355 ? 13.611 35.975 60.379 1.00 24.85 ? 396 HIS A CB 1 ATOM 2778 C CG . HIS A 1 355 ? 12.451 35.036 60.506 1.00 25.00 ? 396 HIS A CG 1 ATOM 2779 N ND1 . HIS A 1 355 ? 11.160 35.393 60.169 1.00 25.72 ? 396 HIS A ND1 1 ATOM 2780 C CD2 . HIS A 1 355 ? 12.404 33.720 60.849 1.00 27.94 ? 396 HIS A CD2 1 ATOM 2781 C CE1 . HIS A 1 355 ? 10.364 34.346 60.307 1.00 27.36 ? 396 HIS A CE1 1 ATOM 2782 N NE2 . HIS A 1 355 ? 11.092 33.317 60.724 1.00 26.80 ? 396 HIS A NE2 1 ATOM 2783 N N . GLU A 1 356 ? 15.295 37.449 62.605 1.00 24.62 ? 397 GLU A N 1 ATOM 2784 C CA . GLU A 1 356 ? 15.947 37.470 63.935 1.00 25.41 ? 397 GLU A CA 1 ATOM 2785 C C . GLU A 1 356 ? 15.639 38.764 64.666 1.00 26.16 ? 397 GLU A C 1 ATOM 2786 O O . GLU A 1 356 ? 15.494 38.771 65.894 1.00 27.41 ? 397 GLU A O 1 ATOM 2787 C CB . GLU A 1 356 ? 17.458 37.256 63.758 1.00 26.44 ? 397 GLU A CB 1 ATOM 2788 C CG . GLU A 1 356 ? 18.277 37.278 65.076 1.00 26.56 ? 397 GLU A CG 1 ATOM 2789 C CD . GLU A 1 356 ? 17.896 36.197 66.066 1.00 31.58 ? 397 GLU A CD 1 ATOM 2790 O OE1 . GLU A 1 356 ? 16.905 35.445 65.848 1.00 31.31 ? 397 GLU A OE1 1 ATOM 2791 O OE2 . GLU A 1 356 ? 18.643 36.081 67.068 1.00 31.55 ? 397 GLU A OE2 1 ATOM 2792 N N . ILE A 1 357 ? 15.504 39.876 63.923 1.00 24.57 ? 398 ILE A N 1 ATOM 2793 C CA . ILE A 1 357 ? 15.089 41.157 64.574 1.00 24.31 ? 398 ILE A CA 1 ATOM 2794 C C . ILE A 1 357 ? 13.676 41.073 65.167 1.00 25.23 ? 398 ILE A C 1 ATOM 2795 O O . ILE A 1 357 ? 13.429 41.466 66.321 1.00 25.08 ? 398 ILE A O 1 ATOM 2796 C CB . ILE A 1 357 ? 15.225 42.352 63.582 1.00 22.99 ? 398 ILE A CB 1 ATOM 2797 C CG1 . ILE A 1 357 ? 16.725 42.646 63.358 1.00 23.30 ? 398 ILE A CG1 1 ATOM 2798 C CG2 . ILE A 1 357 ? 14.441 43.561 64.094 1.00 22.51 ? 398 ILE A CG2 1 ATOM 2799 C CD1 . ILE A 1 357 ? 17.006 43.526 62.136 1.00 24.04 ? 398 ILE A CD1 1 ATOM 2800 N N . VAL A 1 358 ? 12.750 40.508 64.395 1.00 24.78 ? 399 VAL A N 1 ATOM 2801 C CA . VAL A 1 358 ? 11.370 40.288 64.897 1.00 26.04 ? 399 VAL A CA 1 ATOM 2802 C C . VAL A 1 358 ? 11.384 39.389 66.141 1.00 26.22 ? 399 VAL A C 1 ATOM 2803 O O . VAL A 1 358 ? 10.733 39.725 67.166 1.00 28.52 ? 399 VAL A O 1 ATOM 2804 C CB . VAL A 1 358 ? 10.437 39.648 63.844 1.00 25.15 ? 399 VAL A CB 1 ATOM 2805 C CG1 . VAL A 1 358 ? 9.015 39.353 64.457 1.00 26.68 ? 399 VAL A CG1 1 ATOM 2806 C CG2 . VAL A 1 358 ? 10.267 40.566 62.620 1.00 25.99 ? 399 VAL A CG2 1 ATOM 2807 N N . ARG A 1 359 ? 12.118 38.269 66.064 1.00 26.07 ? 400 ARG A N 1 ATOM 2808 C CA . ARG A 1 359 ? 12.238 37.366 67.225 1.00 27.20 ? 400 ARG A CA 1 ATOM 2809 C C . ARG A 1 359 ? 12.753 38.110 68.456 1.00 28.42 ? 400 ARG A C 1 ATOM 2810 O O . ARG A 1 359 ? 12.208 37.914 69.557 1.00 29.72 ? 400 ARG A O 1 ATOM 2811 C CB . ARG A 1 359 ? 13.155 36.175 66.901 1.00 27.30 ? 400 ARG A CB 1 ATOM 2812 C CG . ARG A 1 359 ? 13.042 35.032 67.946 1.00 28.22 ? 400 ARG A CG 1 ATOM 2813 C CD . ARG A 1 359 ? 14.253 34.021 67.829 1.00 31.13 ? 400 ARG A CD 1 ATOM 2814 N NE . ARG A 1 359 ? 15.508 34.712 68.118 1.00 31.82 ? 400 ARG A NE 1 ATOM 2815 C CZ . ARG A 1 359 ? 15.939 35.033 69.341 1.00 33.85 ? 400 ARG A CZ 1 ATOM 2816 N NH1 . ARG A 1 359 ? 17.084 35.690 69.475 1.00 33.92 ? 400 ARG A NH1 1 ATOM 2817 N NH2 . ARG A 1 359 ? 15.246 34.693 70.440 1.00 33.32 ? 400 ARG A NH2 1 ATOM 2818 N N . SER A 1 360 ? 13.765 38.968 68.286 1.00 28.36 ? 401 SER A N 1 ATOM 2819 C CA . SER A 1 360 ? 14.324 39.709 69.431 1.00 30.26 ? 401 SER A CA 1 ATOM 2820 C C . SER A 1 360 ? 13.331 40.720 69.983 1.00 30.20 ? 401 SER A C 1 ATOM 2821 O O . SER A 1 360 ? 13.120 40.791 71.211 1.00 31.23 ? 401 SER A O 1 ATOM 2822 C CB . SER A 1 360 ? 15.619 40.438 69.082 1.00 29.80 ? 401 SER A CB 1 ATOM 2823 O OG A SER A 1 360 ? 16.109 41.125 70.260 0.50 27.23 ? 401 SER A OG 1 ATOM 2824 O OG B SER A 1 360 ? 16.616 39.477 68.784 0.50 33.64 ? 401 SER A OG 1 ATOM 2825 N N . PHE A 1 361 ? 12.684 41.495 69.098 1.00 28.96 ? 402 PHE A N 1 ATOM 2826 C CA . PHE A 1 361 ? 11.678 42.421 69.612 1.00 29.23 ? 402 PHE A CA 1 ATOM 2827 C C . PHE A 1 361 ? 10.581 41.665 70.320 1.00 31.89 ? 402 PHE A C 1 ATOM 2828 O O . PHE A 1 361 ? 10.061 42.139 71.331 1.00 32.30 ? 402 PHE A O 1 ATOM 2829 C CB . PHE A 1 361 ? 11.051 43.289 68.485 1.00 27.89 ? 402 PHE A CB 1 ATOM 2830 C CG . PHE A 1 361 ? 11.854 44.498 68.129 1.00 26.22 ? 402 PHE A CG 1 ATOM 2831 C CD1 . PHE A 1 361 ? 12.027 45.550 69.045 1.00 28.55 ? 402 PHE A CD1 1 ATOM 2832 C CD2 . PHE A 1 361 ? 12.375 44.657 66.846 1.00 27.55 ? 402 PHE A CD2 1 ATOM 2833 C CE1 . PHE A 1 361 ? 12.775 46.674 68.718 1.00 28.32 ? 402 PHE A CE1 1 ATOM 2834 C CE2 . PHE A 1 361 ? 13.114 45.815 66.497 1.00 26.95 ? 402 PHE A CE2 1 ATOM 2835 C CZ . PHE A 1 361 ? 13.305 46.831 67.435 1.00 28.49 ? 402 PHE A CZ 1 ATOM 2836 N N . GLY A 1 362 ? 10.216 40.497 69.793 1.00 31.23 ? 403 GLY A N 1 ATOM 2837 C CA . GLY A 1 362 ? 9.151 39.697 70.386 1.00 32.36 ? 403 GLY A CA 1 ATOM 2838 C C . GLY A 1 362 ? 9.507 39.163 71.771 1.00 34.51 ? 403 GLY A C 1 ATOM 2839 O O . GLY A 1 362 ? 8.638 39.016 72.626 1.00 36.41 ? 403 GLY A O 1 ATOM 2840 N N . THR A 1 363 ? 10.783 38.861 71.987 1.00 34.99 ? 404 THR A N 1 ATOM 2841 C CA . THR A 1 363 ? 11.274 38.410 73.310 1.00 35.71 ? 404 THR A CA 1 ATOM 2842 C C . THR A 1 363 ? 11.069 39.500 74.367 1.00 36.68 ? 404 THR A C 1 ATOM 2843 O O . THR A 1 363 ? 10.635 39.219 75.511 1.00 37.77 ? 404 THR A O 1 ATOM 2844 C CB . THR A 1 363 ? 12.771 37.944 73.273 1.00 36.09 ? 404 THR A CB 1 ATOM 2845 O OG1 A THR A 1 363 ? 12.892 36.788 72.429 0.50 36.42 ? 404 THR A OG1 1 ATOM 2846 O OG1 B THR A 1 363 ? 13.659 39.076 73.249 0.50 35.26 ? 404 THR A OG1 1 ATOM 2847 C CG2 A THR A 1 363 ? 13.265 37.593 74.641 0.50 35.97 ? 404 THR A CG2 1 ATOM 2848 C CG2 B THR A 1 363 ? 13.045 37.033 72.090 0.50 35.80 ? 404 THR A CG2 1 ATOM 2849 N N . LEU A 1 364 ? 11.362 40.737 73.993 1.00 35.83 ? 405 LEU A N 1 ATOM 2850 C CA . LEU A 1 364 ? 11.120 41.866 74.893 1.00 35.87 ? 405 LEU A CA 1 ATOM 2851 C C . LEU A 1 364 ? 9.618 42.031 75.131 1.00 36.27 ? 405 LEU A C 1 ATOM 2852 O O . LEU A 1 364 ? 9.184 42.253 76.262 1.00 35.20 ? 405 LEU A O 1 ATOM 2853 C CB . LEU A 1 364 ? 11.709 43.176 74.310 1.00 36.01 ? 405 LEU A CB 1 ATOM 2854 C CG A LEU A 1 364 ? 13.220 43.228 74.077 0.50 36.13 ? 405 LEU A CG 1 ATOM 2855 C CG B LEU A 1 364 ? 13.177 43.475 74.663 0.50 35.88 ? 405 LEU A CG 1 ATOM 2856 C CD1 A LEU A 1 364 ? 13.581 44.518 73.362 0.50 36.69 ? 405 LEU A CD1 1 ATOM 2857 C CD1 B LEU A 1 364 ? 14.173 42.474 74.054 0.50 34.00 ? 405 LEU A CD1 1 ATOM 2858 C CD2 A LEU A 1 364 ? 13.985 43.082 75.397 0.50 39.06 ? 405 LEU A CD2 1 ATOM 2859 C CD2 B LEU A 1 364 ? 13.545 44.898 74.274 0.50 36.80 ? 405 LEU A CD2 1 ATOM 2860 N N . LYS A 1 365 ? 8.821 41.922 74.074 1.00 34.35 ? 406 LYS A N 1 ATOM 2861 C CA . LYS A 1 365 ? 7.371 42.072 74.185 1.00 35.60 ? 406 LYS A CA 1 ATOM 2862 C C . LYS A 1 365 ? 6.797 41.032 75.124 1.00 38.07 ? 406 LYS A C 1 ATOM 2863 O O . LYS A 1 365 ? 5.917 41.354 75.945 1.00 38.50 ? 406 LYS A O 1 ATOM 2864 C CB . LYS A 1 365 ? 6.686 41.963 72.801 1.00 35.51 ? 406 LYS A CB 1 ATOM 2865 C CG . LYS A 1 365 ? 5.172 42.143 72.919 1.00 38.01 ? 406 LYS A CG 1 ATOM 2866 C CD . LYS A 1 365 ? 4.476 42.089 71.598 1.00 45.54 ? 406 LYS A CD 1 ATOM 2867 C CE . LYS A 1 365 ? 2.970 42.057 71.804 1.00 46.46 ? 406 LYS A CE 1 ATOM 2868 N NZ . LYS A 1 365 ? 2.516 40.710 72.225 1.00 49.99 ? 406 LYS A NZ 1 ATOM 2869 N N . LYS A 1 366 ? 7.307 39.799 75.049 1.00 37.73 ? 407 LYS A N 1 ATOM 2870 C CA . LYS A 1 366 ? 6.812 38.740 75.958 1.00 40.08 ? 407 LYS A CA 1 ATOM 2871 C C . LYS A 1 366 ? 7.111 39.013 77.427 1.00 42.25 ? 407 LYS A C 1 ATOM 2872 O O . LYS A 1 366 ? 6.406 38.511 78.312 1.00 44.18 ? 407 LYS A O 1 ATOM 2873 C CB . LYS A 1 366 ? 7.275 37.357 75.519 1.00 40.40 ? 407 LYS A CB 1 ATOM 2874 C CG . LYS A 1 366 ? 6.570 36.921 74.238 1.00 43.19 ? 407 LYS A CG 1 ATOM 2875 C CD . LYS A 1 366 ? 7.046 35.573 73.757 1.00 46.18 ? 407 LYS A CD 1 ATOM 2876 C CE . LYS A 1 366 ? 6.291 35.185 72.501 1.00 44.36 ? 407 LYS A CE 1 ATOM 2877 N NZ . LYS A 1 366 ? 6.764 33.870 72.048 1.00 50.17 ? 407 LYS A NZ 1 ATOM 2878 N N . GLU A 1 367 ? 8.129 39.826 77.685 1.00 42.05 ? 408 GLU A N 1 ATOM 2879 C CA . GLU A 1 367 ? 8.486 40.231 79.050 1.00 44.22 ? 408 GLU A CA 1 ATOM 2880 C C . GLU A 1 367 ? 7.750 41.483 79.540 1.00 43.94 ? 408 GLU A C 1 ATOM 2881 O O . GLU A 1 367 ? 7.989 41.956 80.661 1.00 45.30 ? 408 GLU A O 1 ATOM 2882 C CB . GLU A 1 367 ? 9.996 40.420 79.161 1.00 44.97 ? 408 GLU A CB 1 ATOM 2883 C CG . GLU A 1 367 ? 10.796 39.136 78.964 1.00 50.95 ? 408 GLU A CG 1 ATOM 2884 C CD . GLU A 1 367 ? 12.305 39.342 79.075 1.00 57.40 ? 408 GLU A CD 1 ATOM 2885 O OE1 . GLU A 1 367 ? 12.958 38.542 79.779 1.00 61.21 ? 408 GLU A OE1 1 ATOM 2886 O OE2 . GLU A 1 367 ? 12.846 40.298 78.464 1.00 60.62 ? 408 GLU A OE2 1 ATOM 2887 N N . GLY A 1 368 ? 6.860 42.018 78.701 1.00 41.70 ? 409 GLY A N 1 ATOM 2888 C CA . GLY A 1 368 ? 6.013 43.163 79.035 1.00 41.61 ? 409 GLY A CA 1 ATOM 2889 C C . GLY A 1 368 ? 6.410 44.490 78.445 1.00 40.45 ? 409 GLY A C 1 ATOM 2890 O O . GLY A 1 368 ? 5.814 45.535 78.775 1.00 41.04 ? 409 GLY A O 1 ATOM 2891 N N . TRP A 1 369 ? 7.414 44.476 77.569 1.00 38.32 ? 410 TRP A N 1 ATOM 2892 C CA . TRP A 1 369 ? 7.883 45.713 76.984 1.00 37.05 ? 410 TRP A CA 1 ATOM 2893 C C . TRP A 1 369 ? 7.066 45.983 75.730 1.00 35.35 ? 410 TRP A C 1 ATOM 2894 O O . TRP A 1 369 ? 6.612 45.049 75.044 1.00 36.21 ? 410 TRP A O 1 ATOM 2895 C CB . TRP A 1 369 ? 9.359 45.577 76.616 1.00 37.50 ? 410 TRP A CB 1 ATOM 2896 C CG . TRP A 1 369 ? 9.976 46.713 75.826 1.00 37.11 ? 410 TRP A CG 1 ATOM 2897 C CD1 . TRP A 1 369 ? 10.512 47.867 76.320 1.00 37.24 ? 410 TRP A CD1 1 ATOM 2898 C CD2 . TRP A 1 369 ? 10.108 46.790 74.395 1.00 35.02 ? 410 TRP A CD2 1 ATOM 2899 N NE1 . TRP A 1 369 ? 11.003 48.645 75.278 1.00 35.93 ? 410 TRP A NE1 1 ATOM 2900 C CE2 . TRP A 1 369 ? 10.764 48.003 74.095 1.00 33.91 ? 410 TRP A CE2 1 ATOM 2901 C CE3 . TRP A 1 369 ? 9.751 45.935 73.341 1.00 34.27 ? 410 TRP A CE3 1 ATOM 2902 C CZ2 . TRP A 1 369 ? 11.078 48.381 72.773 1.00 30.86 ? 410 TRP A CZ2 1 ATOM 2903 C CZ3 . TRP A 1 369 ? 10.057 46.305 72.044 1.00 33.56 ? 410 TRP A CZ3 1 ATOM 2904 C CH2 . TRP A 1 369 ? 10.706 47.534 71.773 1.00 31.67 ? 410 TRP A CH2 1 ATOM 2905 N N . ARG A 1 370 ? 6.878 47.256 75.438 1.00 33.57 ? 411 ARG A N 1 ATOM 2906 C CA . ARG A 1 370 ? 6.447 47.658 74.082 1.00 31.70 ? 411 ARG A CA 1 ATOM 2907 C C . ARG A 1 370 ? 7.260 48.874 73.691 1.00 30.33 ? 411 ARG A C 1 ATOM 2908 O O . ARG A 1 370 ? 7.637 49.692 74.530 1.00 30.17 ? 411 ARG A O 1 ATOM 2909 C CB . ARG A 1 370 ? 4.983 48.106 74.068 1.00 33.47 ? 411 ARG A CB 1 ATOM 2910 C CG . ARG A 1 370 ? 3.957 47.017 74.146 1.00 35.38 ? 411 ARG A CG 1 ATOM 2911 C CD . ARG A 1 370 ? 2.515 47.561 73.971 1.00 34.74 ? 411 ARG A CD 1 ATOM 2912 N NE . ARG A 1 370 ? 1.679 46.387 73.910 1.00 35.24 ? 411 ARG A NE 1 ATOM 2913 C CZ . ARG A 1 370 ? 1.519 45.629 72.816 1.00 33.56 ? 411 ARG A CZ 1 ATOM 2914 N NH1 . ARG A 1 370 ? 2.037 45.983 71.622 1.00 30.02 ? 411 ARG A NH1 1 ATOM 2915 N NH2 . ARG A 1 370 ? 0.783 44.531 72.912 1.00 34.75 ? 411 ARG A NH2 1 ATOM 2916 N N . PRO A 1 371 ? 7.476 49.050 72.389 1.00 27.48 ? 412 PRO A N 1 ATOM 2917 C CA . PRO A 1 371 ? 8.154 50.238 71.925 1.00 26.92 ? 412 PRO A CA 1 ATOM 2918 C C . PRO A 1 371 ? 7.219 51.442 72.100 1.00 26.55 ? 412 PRO A C 1 ATOM 2919 O O . PRO A 1 371 ? 6.007 51.286 72.192 1.00 27.98 ? 412 PRO A O 1 ATOM 2920 C CB . PRO A 1 371 ? 8.366 49.960 70.402 1.00 26.57 ? 412 PRO A CB 1 ATOM 2921 C CG . PRO A 1 371 ? 7.254 49.021 70.060 1.00 26.93 ? 412 PRO A CG 1 ATOM 2922 C CD . PRO A 1 371 ? 7.012 48.169 71.310 1.00 26.86 ? 412 PRO A CD 1 ATOM 2923 N N . ARG A 1 372 ? 7.790 52.627 72.130 1.00 25.24 ? 413 ARG A N 1 ATOM 2924 C CA . ARG A 1 372 ? 6.987 53.845 72.259 1.00 25.54 ? 413 ARG A CA 1 ATOM 2925 C C . ARG A 1 372 ? 6.032 54.012 71.050 1.00 25.79 ? 413 ARG A C 1 ATOM 2926 O O . ARG A 1 372 ? 4.831 54.206 71.213 1.00 25.01 ? 413 ARG A O 1 ATOM 2927 C CB . ARG A 1 372 ? 7.922 55.046 72.321 1.00 26.50 ? 413 ARG A CB 1 ATOM 2928 C CG . ARG A 1 372 ? 7.142 56.384 72.413 1.00 29.18 ? 413 ARG A CG 1 ATOM 2929 C CD . ARG A 1 372 ? 8.081 57.555 72.376 1.00 31.41 ? 413 ARG A CD 1 ATOM 2930 N NE . ARG A 1 372 ? 7.367 58.832 72.322 1.00 29.74 ? 413 ARG A NE 1 ATOM 2931 C CZ . ARG A 1 372 ? 6.938 59.505 73.382 1.00 33.66 ? 413 ARG A CZ 1 ATOM 2932 N NH1 . ARG A 1 372 ? 7.103 58.999 74.610 1.00 33.48 ? 413 ARG A NH1 1 ATOM 2933 N NH2 . ARG A 1 372 ? 6.322 60.664 73.200 1.00 32.40 ? 413 ARG A NH2 1 ATOM 2934 N N . ARG A 1 373 ? 6.618 53.882 69.864 1.00 24.09 ? 414 ARG A N 1 ATOM 2935 C CA . ARG A 1 373 ? 5.847 53.983 68.583 1.00 23.05 ? 414 ARG A CA 1 ATOM 2936 C C . ARG A 1 373 ? 5.599 52.580 68.038 1.00 24.20 ? 414 ARG A C 1 ATOM 2937 O O . ARG A 1 373 ? 6.306 51.622 68.375 1.00 24.47 ? 414 ARG A O 1 ATOM 2938 C CB . ARG A 1 373 ? 6.642 54.790 67.550 1.00 23.02 ? 414 ARG A CB 1 ATOM 2939 C CG . ARG A 1 373 ? 7.090 56.178 68.079 1.00 22.58 ? 414 ARG A CG 1 ATOM 2940 C CD . ARG A 1 373 ? 7.827 57.084 67.032 1.00 23.59 ? 414 ARG A CD 1 ATOM 2941 N NE . ARG A 1 373 ? 8.079 58.343 67.728 1.00 23.16 ? 414 ARG A NE 1 ATOM 2942 C CZ . ARG A 1 373 ? 9.040 58.562 68.618 1.00 23.78 ? 414 ARG A CZ 1 ATOM 2943 N NH1 . ARG A 1 373 ? 9.991 57.666 68.832 1.00 23.58 ? 414 ARG A NH1 1 ATOM 2944 N NH2 . ARG A 1 373 ? 9.059 59.722 69.292 1.00 25.70 ? 414 ARG A NH2 1 ATOM 2945 N N . THR A 1 374 ? 4.624 52.466 67.140 1.00 22.77 ? 415 THR A N 1 ATOM 2946 C CA . THR A 1 374 ? 4.342 51.212 66.449 1.00 22.15 ? 415 THR A CA 1 ATOM 2947 C C . THR A 1 374 ? 5.472 50.838 65.490 1.00 21.94 ? 415 THR A C 1 ATOM 2948 O O . THR A 1 374 ? 5.984 51.704 64.746 1.00 21.75 ? 415 THR A O 1 ATOM 2949 C CB . THR A 1 374 ? 3.009 51.339 65.689 1.00 22.24 ? 415 THR A CB 1 ATOM 2950 O OG1 . THR A 1 374 ? 1.940 51.361 66.641 1.00 23.08 ? 415 THR A OG1 1 ATOM 2951 C CG2 . THR A 1 374 ? 2.782 50.149 64.704 1.00 23.18 ? 415 THR A CG2 1 ATOM 2952 N N . ILE A 1 375 ? 5.850 49.555 65.512 1.00 21.29 ? 416 ILE A N 1 ATOM 2953 C CA . ILE A 1 375 ? 6.785 49.021 64.521 1.00 20.68 ? 416 ILE A CA 1 ATOM 2954 C C . ILE A 1 375 ? 6.025 48.114 63.581 1.00 20.71 ? 416 ILE A C 1 ATOM 2955 O O . ILE A 1 375 ? 5.261 47.241 64.027 1.00 22.44 ? 416 ILE A O 1 ATOM 2956 C CB . ILE A 1 375 ? 7.980 48.261 65.181 1.00 21.27 ? 416 ILE A CB 1 ATOM 2957 C CG1 . ILE A 1 375 ? 8.714 49.175 66.163 1.00 22.88 ? 416 ILE A CG1 1 ATOM 2958 C CG2 . ILE A 1 375 ? 8.946 47.826 64.067 1.00 21.56 ? 416 ILE A CG2 1 ATOM 2959 C CD1 . ILE A 1 375 ? 9.750 48.402 67.021 1.00 24.24 ? 416 ILE A CD1 1 ATOM 2960 N N . LEU A 1 376 ? 6.188 48.354 62.268 1.00 20.40 ? 417 LEU A N 1 ATOM 2961 C CA . LEU A 1 376 ? 5.609 47.477 61.257 1.00 20.35 ? 417 LEU A CA 1 ATOM 2962 C C . LEU A 1 376 ? 6.765 46.717 60.618 1.00 21.03 ? 417 LEU A C 1 ATOM 2963 O O . LEU A 1 376 ? 7.818 47.302 60.334 1.00 22.11 ? 417 LEU A O 1 ATOM 2964 C CB . LEU A 1 376 ? 4.903 48.302 60.168 1.00 19.72 ? 417 LEU A CB 1 ATOM 2965 C CG . LEU A 1 376 ? 3.730 49.173 60.689 1.00 20.92 ? 417 LEU A CG 1 ATOM 2966 C CD1 . LEU A 1 376 ? 3.062 49.905 59.499 1.00 22.77 ? 417 LEU A CD1 1 ATOM 2967 C CD2 . LEU A 1 376 ? 2.720 48.324 61.475 1.00 23.98 ? 417 LEU A CD2 1 ATOM 2968 N N . PHE A 1 377 ? 6.560 45.416 60.417 1.00 20.08 ? 418 PHE A N 1 ATOM 2969 C CA . PHE A 1 377 ? 7.578 44.565 59.802 1.00 19.78 ? 418 PHE A CA 1 ATOM 2970 C C . PHE A 1 377 ? 6.988 44.034 58.509 1.00 20.27 ? 418 PHE A C 1 ATOM 2971 O O . PHE A 1 377 ? 5.807 43.621 58.503 1.00 21.31 ? 418 PHE A O 1 ATOM 2972 C CB . PHE A 1 377 ? 7.914 43.387 60.715 1.00 21.23 ? 418 PHE A CB 1 ATOM 2973 C CG . PHE A 1 377 ? 8.498 43.792 62.007 1.00 22.36 ? 418 PHE A CG 1 ATOM 2974 C CD1 . PHE A 1 377 ? 9.870 44.052 62.103 1.00 24.22 ? 418 PHE A CD1 1 ATOM 2975 C CD2 . PHE A 1 377 ? 7.674 43.912 63.147 1.00 25.05 ? 418 PHE A CD2 1 ATOM 2976 C CE1 . PHE A 1 377 ? 10.446 44.433 63.334 1.00 24.00 ? 418 PHE A CE1 1 ATOM 2977 C CE2 . PHE A 1 377 ? 8.251 44.299 64.382 1.00 25.04 ? 418 PHE A CE2 1 ATOM 2978 C CZ . PHE A 1 377 ? 9.645 44.548 64.475 1.00 24.73 ? 418 PHE A CZ 1 ATOM 2979 N N . ALA A 1 378 ? 7.751 44.077 57.412 1.00 19.93 ? 419 ALA A N 1 ATOM 2980 C CA . ALA A 1 378 ? 7.179 43.646 56.123 1.00 19.09 ? 419 ALA A CA 1 ATOM 2981 C C . ALA A 1 378 ? 8.094 42.668 55.425 1.00 19.65 ? 419 ALA A C 1 ATOM 2982 O O . ALA A 1 378 ? 9.301 42.865 55.380 1.00 20.13 ? 419 ALA A O 1 ATOM 2983 C CB . ALA A 1 378 ? 6.883 44.852 55.213 1.00 19.35 ? 419 ALA A CB 1 ATOM 2984 N N . SER A 1 379 ? 7.465 41.625 54.877 1.00 18.57 ? 420 SER A N 1 ATOM 2985 C CA . SER A 1 379 ? 8.100 40.648 53.990 1.00 18.89 ? 420 SER A CA 1 ATOM 2986 C C . SER A 1 379 ? 7.447 40.912 52.612 1.00 18.98 ? 420 SER A C 1 ATOM 2987 O O . SER A 1 379 ? 6.323 40.462 52.341 1.00 20.07 ? 420 SER A O 1 ATOM 2988 C CB . SER A 1 379 ? 7.787 39.235 54.469 1.00 20.61 ? 420 SER A CB 1 ATOM 2989 O OG . SER A 1 379 ? 8.313 38.268 53.531 1.00 20.94 ? 420 SER A OG 1 ATOM 2990 N N . TRP A 1 380 ? 8.144 41.642 51.761 1.00 18.91 ? 421 TRP A N 1 ATOM 2991 C CA . TRP A 1 380 ? 7.535 42.077 50.481 1.00 18.53 ? 421 TRP A CA 1 ATOM 2992 C C . TRP A 1 380 ? 7.640 41.002 49.417 1.00 20.32 ? 421 TRP A C 1 ATOM 2993 O O . TRP A 1 380 ? 8.632 40.266 49.376 1.00 20.87 ? 421 TRP A O 1 ATOM 2994 C CB . TRP A 1 380 ? 8.294 43.257 49.904 1.00 18.91 ? 421 TRP A CB 1 ATOM 2995 C CG . TRP A 1 380 ? 8.392 44.506 50.783 1.00 18.30 ? 421 TRP A CG 1 ATOM 2996 C CD1 . TRP A 1 380 ? 9.534 45.177 51.086 1.00 17.72 ? 421 TRP A CD1 1 ATOM 2997 C CD2 . TRP A 1 380 ? 7.305 45.244 51.374 1.00 17.00 ? 421 TRP A CD2 1 ATOM 2998 N NE1 . TRP A 1 380 ? 9.238 46.297 51.880 1.00 16.80 ? 421 TRP A NE1 1 ATOM 2999 C CE2 . TRP A 1 380 ? 7.868 46.353 52.047 1.00 16.47 ? 421 TRP A CE2 1 ATOM 3000 C CE3 . TRP A 1 380 ? 5.909 45.071 51.387 1.00 17.55 ? 421 TRP A CE3 1 ATOM 3001 C CZ2 . TRP A 1 380 ? 7.061 47.302 52.774 1.00 19.26 ? 421 TRP A CZ2 1 ATOM 3002 C CZ3 . TRP A 1 380 ? 5.109 46.000 52.100 1.00 18.44 ? 421 TRP A CZ3 1 ATOM 3003 C CH2 . TRP A 1 380 ? 5.720 47.111 52.786 1.00 18.88 ? 421 TRP A CH2 1 ATOM 3004 N N . ASP A 1 381 ? 6.641 40.969 48.537 1.00 19.66 ? 422 ASP A N 1 ATOM 3005 C CA . ASP A 1 381 ? 6.701 40.025 47.405 1.00 18.29 ? 422 ASP A CA 1 ATOM 3006 C C . ASP A 1 381 ? 7.015 40.782 46.131 1.00 19.56 ? 422 ASP A C 1 ATOM 3007 O O . ASP A 1 381 ? 6.893 42.011 46.049 1.00 19.46 ? 422 ASP A O 1 ATOM 3008 C CB . ASP A 1 381 ? 5.328 39.300 47.263 1.00 19.72 ? 422 ASP A CB 1 ATOM 3009 C CG . ASP A 1 381 ? 5.416 37.944 46.572 1.00 19.69 ? 422 ASP A CG 1 ATOM 3010 O OD1 . ASP A 1 381 ? 6.449 37.544 45.960 1.00 20.66 ? 422 ASP A OD1 1 ATOM 3011 O OD2 . ASP A 1 381 ? 4.389 37.204 46.648 1.00 21.37 ? 422 ASP A OD2 1 ATOM 3012 N N . ALA A 1 382 ? 7.403 40.022 45.120 1.00 18.35 ? 423 ALA A N 1 ATOM 3013 C CA . ALA A 1 382 ? 7.612 40.519 43.763 1.00 19.75 ? 423 ALA A CA 1 ATOM 3014 C C . ALA A 1 382 ? 8.526 41.739 43.658 1.00 18.42 ? 423 ALA A C 1 ATOM 3015 O O . ALA A 1 382 ? 8.391 42.558 42.729 1.00 19.22 ? 423 ALA A O 1 ATOM 3016 C CB . ALA A 1 382 ? 6.249 40.722 43.022 1.00 18.83 ? 423 ALA A CB 1 ATOM 3017 N N . ALA A 1 383 ? 9.521 41.854 44.545 1.00 18.65 ? 424 ALA A N 1 ATOM 3018 C CA . ALA A 1 383 ? 10.450 42.950 44.372 1.00 18.54 ? 424 ALA A CA 1 ATOM 3019 C C . ALA A 1 383 ? 11.256 42.748 43.122 1.00 18.93 ? 424 ALA A C 1 ATOM 3020 O O . ALA A 1 383 ? 11.630 43.764 42.459 1.00 19.13 ? 424 ALA A O 1 ATOM 3021 C CB . ALA A 1 383 ? 11.373 43.040 45.574 1.00 19.27 ? 424 ALA A CB 1 ATOM 3022 N N . GLU A 1 384 ? 11.552 41.478 42.787 1.00 18.90 ? 425 GLU A N 1 ATOM 3023 C CA . GLU A 1 384 ? 12.404 41.253 41.628 1.00 19.75 ? 425 GLU A CA 1 ATOM 3024 C C . GLU A 1 384 ? 11.724 41.629 40.330 1.00 19.55 ? 425 GLU A C 1 ATOM 3025 O O . GLU A 1 384 ? 12.377 41.775 39.300 1.00 20.45 ? 425 GLU A O 1 ATOM 3026 C CB . GLU A 1 384 ? 12.866 39.796 41.570 1.00 19.73 ? 425 GLU A CB 1 ATOM 3027 C CG . GLU A 1 384 ? 13.812 39.338 42.716 1.00 19.96 ? 425 GLU A CG 1 ATOM 3028 C CD . GLU A 1 384 ? 15.173 40.028 42.752 1.00 20.01 ? 425 GLU A CD 1 ATOM 3029 O OE1 . GLU A 1 384 ? 15.388 41.005 42.018 1.00 22.39 ? 425 GLU A OE1 1 ATOM 3030 O OE2 . GLU A 1 384 ? 16.041 39.629 43.564 1.00 20.37 ? 425 GLU A OE2 1 ATOM 3031 N N . PHE A 1 385 ? 10.407 41.810 40.367 1.00 19.69 ? 426 PHE A N 1 ATOM 3032 C CA . PHE A 1 385 ? 9.661 42.171 39.157 1.00 19.41 ? 426 PHE A CA 1 ATOM 3033 C C . PHE A 1 385 ? 9.270 43.634 39.143 1.00 19.12 ? 426 PHE A C 1 ATOM 3034 O O . PHE A 1 385 ? 8.368 44.021 38.375 1.00 20.70 ? 426 PHE A O 1 ATOM 3035 C CB . PHE A 1 385 ? 8.378 41.304 39.130 1.00 19.35 ? 426 PHE A CB 1 ATOM 3036 C CG . PHE A 1 385 ? 8.651 39.869 38.804 1.00 21.00 ? 426 PHE A CG 1 ATOM 3037 C CD1 . PHE A 1 385 ? 8.561 39.464 37.481 1.00 20.29 ? 426 PHE A CD1 1 ATOM 3038 C CD2 . PHE A 1 385 ? 9.029 38.918 39.810 1.00 20.92 ? 426 PHE A CD2 1 ATOM 3039 C CE1 . PHE A 1 385 ? 8.818 38.092 37.079 1.00 20.96 ? 426 PHE A CE1 1 ATOM 3040 C CE2 . PHE A 1 385 ? 9.295 37.541 39.465 1.00 21.12 ? 426 PHE A CE2 1 ATOM 3041 C CZ . PHE A 1 385 ? 9.202 37.117 38.076 1.00 22.17 ? 426 PHE A CZ 1 ATOM 3042 N N . GLY A 1 386 ? 9.963 44.469 39.956 1.00 19.02 ? 427 GLY A N 1 ATOM 3043 C CA . GLY A 1 386 ? 9.735 45.904 39.878 1.00 19.36 ? 427 GLY A CA 1 ATOM 3044 C C . GLY A 1 386 ? 9.235 46.508 41.176 1.00 17.44 ? 427 GLY A C 1 ATOM 3045 O O . GLY A 1 386 ? 8.500 47.512 41.160 1.00 18.39 ? 427 GLY A O 1 ATOM 3046 N N . LEU A 1 387 ? 9.645 45.940 42.300 1.00 17.17 ? 428 LEU A N 1 ATOM 3047 C CA . LEU A 1 387 ? 9.239 46.482 43.615 1.00 17.64 ? 428 LEU A CA 1 ATOM 3048 C C . LEU A 1 387 ? 7.698 46.452 43.775 1.00 17.99 ? 428 LEU A C 1 ATOM 3049 O O . LEU A 1 387 ? 7.090 47.327 44.358 1.00 17.65 ? 428 LEU A O 1 ATOM 3050 C CB . LEU A 1 387 ? 9.772 47.943 43.828 1.00 18.45 ? 428 LEU A CB 1 ATOM 3051 C CG . LEU A 1 387 ? 11.252 48.111 43.428 1.00 18.42 ? 428 LEU A CG 1 ATOM 3052 C CD1 . LEU A 1 387 ? 11.626 49.611 43.586 1.00 18.89 ? 428 LEU A CD1 1 ATOM 3053 C CD2 . LEU A 1 387 ? 12.193 47.212 44.225 1.00 19.46 ? 428 LEU A CD2 1 ATOM 3054 N N . LEU A 1 388 ? 7.073 45.399 43.230 1.00 17.43 ? 429 LEU A N 1 ATOM 3055 C CA . LEU A 1 388 ? 5.619 45.428 43.078 1.00 16.98 ? 429 LEU A CA 1 ATOM 3056 C C . LEU A 1 388 ? 4.886 45.323 44.407 1.00 17.11 ? 429 LEU A C 1 ATOM 3057 O O . LEU A 1 388 ? 3.904 46.047 44.618 1.00 18.23 ? 429 LEU A O 1 ATOM 3058 C CB . LEU A 1 388 ? 5.162 44.323 42.107 1.00 17.47 ? 429 LEU A CB 1 ATOM 3059 C CG . LEU A 1 388 ? 5.857 44.403 40.729 1.00 18.45 ? 429 LEU A CG 1 ATOM 3060 C CD1 . LEU A 1 388 ? 5.206 43.322 39.854 1.00 20.15 ? 429 LEU A CD1 1 ATOM 3061 C CD2 . LEU A 1 388 ? 5.689 45.759 40.017 1.00 21.33 ? 429 LEU A CD2 1 ATOM 3062 N N . GLY A 1 389 ? 5.352 44.459 45.288 1.00 18.39 ? 430 GLY A N 1 ATOM 3063 C CA . GLY A 1 389 ? 4.682 44.244 46.590 1.00 17.64 ? 430 GLY A CA 1 ATOM 3064 C C . GLY A 1 389 ? 4.728 45.470 47.489 1.00 17.98 ? 430 GLY A C 1 ATOM 3065 O O . GLY A 1 389 ? 3.679 45.866 48.087 1.00 18.06 ? 430 GLY A O 1 ATOM 3066 N N . SER A 1 390 ? 5.912 46.067 47.626 1.00 16.92 ? 431 SER A N 1 ATOM 3067 C CA . SER A 1 390 ? 6.015 47.249 48.485 1.00 16.66 ? 431 SER A CA 1 ATOM 3068 C C . SER A 1 390 ? 5.187 48.388 47.873 1.00 17.01 ? 431 SER A C 1 ATOM 3069 O O . SER A 1 390 ? 4.501 49.146 48.582 1.00 17.02 ? 431 SER A O 1 ATOM 3070 C CB . SER A 1 390 ? 7.488 47.621 48.665 1.00 16.75 ? 431 SER A CB 1 ATOM 3071 O OG . SER A 1 390 ? 8.109 47.991 47.421 1.00 18.22 ? 431 SER A OG 1 ATOM 3072 N N . THR A 1 391 ? 5.272 48.516 46.550 1.00 17.00 ? 432 THR A N 1 ATOM 3073 C CA . THR A 1 391 ? 4.626 49.650 45.929 1.00 16.39 ? 432 THR A CA 1 ATOM 3074 C C . THR A 1 391 ? 3.108 49.543 45.982 1.00 16.40 ? 432 THR A C 1 ATOM 3075 O O . THR A 1 391 ? 2.436 50.557 46.332 1.00 16.45 ? 432 THR A O 1 ATOM 3076 C CB . THR A 1 391 ? 5.107 49.842 44.473 1.00 16.25 ? 432 THR A CB 1 ATOM 3077 O OG1 . THR A 1 391 ? 6.531 50.031 44.460 1.00 17.36 ? 432 THR A OG1 1 ATOM 3078 C CG2 . THR A 1 391 ? 4.446 51.143 43.927 1.00 18.84 ? 432 THR A CG2 1 ATOM 3079 N N . GLU A 1 392 ? 2.553 48.342 45.744 1.00 16.97 ? 433 GLU A N 1 ATOM 3080 C CA . GLU A 1 392 ? 1.083 48.203 45.802 1.00 16.38 ? 433 GLU A CA 1 ATOM 3081 C C . GLU A 1 392 ? 0.597 48.440 47.234 1.00 16.40 ? 433 GLU A C 1 ATOM 3082 O O . GLU A 1 392 ? -0.439 49.069 47.424 1.00 17.10 ? 433 GLU A O 1 ATOM 3083 C CB . GLU A 1 392 ? 0.612 46.824 45.332 1.00 17.43 ? 433 GLU A CB 1 ATOM 3084 C CG . GLU A 1 392 ? 0.909 46.612 43.814 1.00 18.44 ? 433 GLU A CG 1 ATOM 3085 C CD . GLU A 1 392 ? 0.306 47.699 42.975 1.00 19.96 ? 433 GLU A CD 1 ATOM 3086 O OE1 . GLU A 1 392 ? -0.918 47.944 43.076 1.00 18.85 ? 433 GLU A OE1 1 ATOM 3087 O OE2 . GLU A 1 392 ? 1.039 48.339 42.196 1.00 18.84 ? 433 GLU A OE2 1 ATOM 3088 N N . TRP A 1 393 ? 1.332 47.928 48.216 1.00 16.94 ? 434 TRP A N 1 ATOM 3089 C CA . TRP A 1 393 ? 0.915 48.143 49.610 1.00 17.65 ? 434 TRP A CA 1 ATOM 3090 C C . TRP A 1 393 ? 0.983 49.616 49.991 1.00 18.29 ? 434 TRP A C 1 ATOM 3091 O O . TRP A 1 393 ? 0.085 50.115 50.674 1.00 18.48 ? 434 TRP A O 1 ATOM 3092 C CB . TRP A 1 393 ? 1.802 47.285 50.497 1.00 17.85 ? 434 TRP A CB 1 ATOM 3093 C CG . TRP A 1 393 ? 1.404 47.324 51.977 1.00 17.12 ? 434 TRP A CG 1 ATOM 3094 C CD1 . TRP A 1 393 ? 0.449 46.531 52.605 1.00 19.60 ? 434 TRP A CD1 1 ATOM 3095 C CD2 . TRP A 1 393 ? 1.964 48.179 52.991 1.00 18.63 ? 434 TRP A CD2 1 ATOM 3096 N NE1 . TRP A 1 393 ? 0.392 46.855 53.954 1.00 20.72 ? 434 TRP A NE1 1 ATOM 3097 C CE2 . TRP A 1 393 ? 1.311 47.849 54.208 1.00 18.82 ? 434 TRP A CE2 1 ATOM 3098 C CE3 . TRP A 1 393 ? 2.972 49.166 52.983 1.00 18.51 ? 434 TRP A CE3 1 ATOM 3099 C CZ2 . TRP A 1 393 ? 1.610 48.489 55.426 1.00 20.85 ? 434 TRP A CZ2 1 ATOM 3100 C CZ3 . TRP A 1 393 ? 3.287 49.822 54.216 1.00 19.39 ? 434 TRP A CZ3 1 ATOM 3101 C CH2 . TRP A 1 393 ? 2.590 49.455 55.421 1.00 19.99 ? 434 TRP A CH2 1 ATOM 3102 N N . ALA A 1 394 ? 2.037 50.303 49.545 1.00 17.15 ? 435 ALA A N 1 ATOM 3103 C CA . ALA A 1 394 ? 2.127 51.734 49.835 1.00 17.05 ? 435 ALA A CA 1 ATOM 3104 C C . ALA A 1 394 ? 1.022 52.489 49.121 1.00 17.76 ? 435 ALA A C 1 ATOM 3105 O O . ALA A 1 394 ? 0.486 53.455 49.661 1.00 17.16 ? 435 ALA A O 1 ATOM 3106 C CB . ALA A 1 394 ? 3.537 52.262 49.420 1.00 17.70 ? 435 ALA A CB 1 ATOM 3107 N N . GLU A 1 395 ? 0.680 52.073 47.893 1.00 17.31 ? 436 GLU A N 1 ATOM 3108 C CA . GLU A 1 395 ? -0.478 52.716 47.236 1.00 16.96 ? 436 GLU A CA 1 ATOM 3109 C C . GLU A 1 395 ? -1.790 52.505 48.019 1.00 17.63 ? 436 GLU A C 1 ATOM 3110 O O . GLU A 1 395 ? -2.616 53.436 48.111 1.00 18.86 ? 436 GLU A O 1 ATOM 3111 C CB . GLU A 1 395 ? -0.669 52.202 45.799 1.00 17.65 ? 436 GLU A CB 1 ATOM 3112 C CG . GLU A 1 395 ? 0.503 52.778 44.891 1.00 17.05 ? 436 GLU A CG 1 ATOM 3113 C CD . GLU A 1 395 ? 0.371 52.394 43.443 1.00 19.91 ? 436 GLU A CD 1 ATOM 3114 O OE1 . GLU A 1 395 ? 0.760 53.227 42.614 1.00 18.41 ? 436 GLU A OE1 1 ATOM 3115 O OE2 . GLU A 1 395 ? -0.152 51.295 43.153 1.00 20.39 ? 436 GLU A OE2 1 ATOM 3116 N N . GLU A 1 396 ? -1.967 51.309 48.566 1.00 18.40 ? 437 GLU A N 1 ATOM 3117 C CA . GLU A 1 396 ? -3.202 51.024 49.306 1.00 18.59 ? 437 GLU A CA 1 ATOM 3118 C C . GLU A 1 396 ? -3.256 51.892 50.572 1.00 19.09 ? 437 GLU A C 1 ATOM 3119 O O . GLU A 1 396 ? -4.310 52.422 50.915 1.00 18.97 ? 437 GLU A O 1 ATOM 3120 C CB . GLU A 1 396 ? -3.176 49.564 49.729 1.00 20.92 ? 437 GLU A CB 1 ATOM 3121 C CG . GLU A 1 396 ? -4.530 49.104 50.344 1.00 23.46 ? 437 GLU A CG 1 ATOM 3122 C CD . GLU A 1 396 ? -4.692 47.611 50.010 1.00 32.48 ? 437 GLU A CD 1 ATOM 3123 O OE1 . GLU A 1 396 ? -5.510 47.211 49.168 1.00 43.11 ? 437 GLU A OE1 1 ATOM 3124 O OE2 . GLU A 1 396 ? -3.896 46.864 50.505 1.00 31.02 ? 437 GLU A OE2 1 ATOM 3125 N N . ASN A 1 397 ? -2.103 52.025 51.202 1.00 16.76 ? 438 ASN A N 1 ATOM 3126 C CA . ASN A 1 397 ? -2.026 52.641 52.552 1.00 17.32 ? 438 ASN A CA 1 ATOM 3127 C C . ASN A 1 397 ? -1.404 54.012 52.556 1.00 17.81 ? 438 ASN A C 1 ATOM 3128 O O . ASN A 1 397 ? -1.039 54.529 53.610 1.00 18.12 ? 438 ASN A O 1 ATOM 3129 C CB . ASN A 1 397 ? -1.244 51.671 53.471 1.00 17.71 ? 438 ASN A CB 1 ATOM 3130 C CG . ASN A 1 397 ? -2.015 50.393 53.685 1.00 20.46 ? 438 ASN A CG 1 ATOM 3131 O OD1 . ASN A 1 397 ? -3.085 50.411 54.329 1.00 24.32 ? 438 ASN A OD1 1 ATOM 3132 N ND2 . ASN A 1 397 ? -1.537 49.267 53.103 1.00 20.27 ? 438 ASN A ND2 1 ATOM 3133 N N . SER A 1 398 ? -1.392 54.671 51.399 1.00 16.89 ? 439 SER A N 1 ATOM 3134 C CA . SER A 1 398 ? -0.664 55.944 51.289 1.00 17.40 ? 439 SER A CA 1 ATOM 3135 C C . SER A 1 398 ? -1.131 57.018 52.274 1.00 16.82 ? 439 SER A C 1 ATOM 3136 O O . SER A 1 398 ? -0.298 57.797 52.754 1.00 18.08 ? 439 SER A O 1 ATOM 3137 C CB . SER A 1 398 ? -0.818 56.517 49.830 1.00 17.31 ? 439 SER A CB 1 ATOM 3138 O OG . SER A 1 398 ? -2.180 56.789 49.548 1.00 19.67 ? 439 SER A OG 1 ATOM 3139 N N . ARG A 1 399 ? -2.428 57.084 52.577 1.00 17.35 ? 440 ARG A N 1 ATOM 3140 C CA . ARG A 1 399 ? -2.893 58.114 53.516 1.00 17.34 ? 440 ARG A CA 1 ATOM 3141 C C . ARG A 1 399 ? -2.397 57.861 54.935 1.00 18.19 ? 440 ARG A C 1 ATOM 3142 O O . ARG A 1 399 ? -2.024 58.831 55.660 1.00 19.04 ? 440 ARG A O 1 ATOM 3143 C CB . ARG A 1 399 ? -4.414 58.189 53.501 1.00 17.71 ? 440 ARG A CB 1 ATOM 3144 C CG . ARG A 1 399 ? -4.946 58.705 52.128 1.00 20.12 ? 440 ARG A CG 1 ATOM 3145 C CD . ARG A 1 399 ? -6.262 58.054 51.693 1.00 24.07 ? 440 ARG A CD 1 ATOM 3146 N NE . ARG A 1 399 ? -6.654 58.576 50.378 1.00 21.49 ? 440 ARG A NE 1 ATOM 3147 C CZ . ARG A 1 399 ? -6.227 58.141 49.206 1.00 22.74 ? 440 ARG A CZ 1 ATOM 3148 N NH1 . ARG A 1 399 ? -5.386 57.059 49.107 1.00 25.10 ? 440 ARG A NH1 1 ATOM 3149 N NH2 . ARG A 1 399 ? -6.664 58.794 48.130 1.00 21.99 ? 440 ARG A NH2 1 ATOM 3150 N N . LEU A 1 400 ? -2.405 56.581 55.347 1.00 17.96 ? 441 LEU A N 1 ATOM 3151 C CA . LEU A 1 400 ? -1.889 56.261 56.664 1.00 18.94 ? 441 LEU A CA 1 ATOM 3152 C C . LEU A 1 400 ? -0.381 56.553 56.723 1.00 19.30 ? 441 LEU A C 1 ATOM 3153 O O . LEU A 1 400 ? 0.135 57.100 57.695 1.00 19.50 ? 441 LEU A O 1 ATOM 3154 C CB . LEU A 1 400 ? -2.117 54.779 56.971 1.00 19.30 ? 441 LEU A CB 1 ATOM 3155 C CG . LEU A 1 400 ? -3.556 54.280 56.787 1.00 21.58 ? 441 LEU A CG 1 ATOM 3156 C CD1 . LEU A 1 400 ? -3.592 52.827 57.233 1.00 25.44 ? 441 LEU A CD1 1 ATOM 3157 C CD2 . LEU A 1 400 ? -4.601 55.112 57.570 1.00 23.55 ? 441 LEU A CD2 1 ATOM 3158 N N . LEU A 1 401 ? 0.334 56.215 55.643 1.00 18.38 ? 442 LEU A N 1 ATOM 3159 C CA . LEU A 1 401 ? 1.789 56.348 55.664 1.00 18.89 ? 442 LEU A CA 1 ATOM 3160 C C . LEU A 1 401 ? 2.216 57.807 55.610 1.00 19.53 ? 442 LEU A C 1 ATOM 3161 O O . LEU A 1 401 ? 3.164 58.187 56.285 1.00 21.82 ? 442 LEU A O 1 ATOM 3162 C CB . LEU A 1 401 ? 2.392 55.622 54.422 1.00 17.28 ? 442 LEU A CB 1 ATOM 3163 C CG . LEU A 1 401 ? 2.218 54.120 54.482 1.00 20.44 ? 442 LEU A CG 1 ATOM 3164 C CD1 . LEU A 1 401 ? 2.563 53.475 53.096 1.00 20.17 ? 442 LEU A CD1 1 ATOM 3165 C CD2 . LEU A 1 401 ? 3.147 53.444 55.501 1.00 21.40 ? 442 LEU A CD2 1 ATOM 3166 N N A GLN A 1 402 ? 1.562 58.637 54.833 0.50 18.47 ? 443 GLN A N 1 ATOM 3167 N N B GLN A 1 402 ? 1.479 58.599 54.808 0.50 19.84 ? 443 GLN A N 1 ATOM 3168 C CA A GLN A 1 402 ? 2.085 59.979 54.768 0.50 17.93 ? 443 GLN A CA 1 ATOM 3169 C CA B GLN A 1 402 ? 1.658 60.064 54.637 0.50 20.25 ? 443 GLN A CA 1 ATOM 3170 C C A GLN A 1 402 ? 1.666 60.820 56.009 0.50 18.85 ? 443 GLN A C 1 ATOM 3171 C C B GLN A 1 402 ? 1.637 60.760 55.986 0.50 20.36 ? 443 GLN A C 1 ATOM 3172 O O A GLN A 1 402 ? 2.350 61.806 56.314 0.50 18.51 ? 443 GLN A O 1 ATOM 3173 O O B GLN A 1 402 ? 2.539 61.529 56.343 0.50 19.53 ? 443 GLN A O 1 ATOM 3174 C CB A GLN A 1 402 ? 1.696 60.637 53.451 0.50 15.45 ? 443 GLN A CB 1 ATOM 3175 C CB B GLN A 1 402 ? 0.518 60.656 53.759 0.50 20.83 ? 443 GLN A CB 1 ATOM 3176 C CG A GLN A 1 402 ? 0.203 60.916 53.356 0.50 15.40 ? 443 GLN A CG 1 ATOM 3177 C CG B GLN A 1 402 ? 0.295 62.114 53.914 0.50 19.83 ? 443 GLN A CG 1 ATOM 3178 C CD A GLN A 1 402 ? -0.152 61.211 51.930 0.50 18.76 ? 443 GLN A CD 1 ATOM 3179 C CD B GLN A 1 402 ? 1.219 62.903 53.081 0.50 23.84 ? 443 GLN A CD 1 ATOM 3180 O OE1 A GLN A 1 402 ? 0.704 61.100 51.025 0.50 18.90 ? 443 GLN A OE1 1 ATOM 3181 O OE1 B GLN A 1 402 ? 1.711 62.379 52.060 0.50 25.13 ? 443 GLN A OE1 1 ATOM 3182 N NE2 A GLN A 1 402 ? -1.416 61.538 51.691 0.50 20.43 ? 443 GLN A NE2 1 ATOM 3183 N NE2 B GLN A 1 402 ? 1.487 64.163 53.493 0.50 15.17 ? 443 GLN A NE2 1 ATOM 3184 N N . GLU A 1 403 ? 0.627 60.400 56.763 1.00 19.04 ? 444 GLU A N 1 ATOM 3185 C CA . GLU A 1 403 ? 0.314 61.153 57.962 1.00 18.82 ? 444 GLU A CA 1 ATOM 3186 C C . GLU A 1 403 ? 0.935 60.541 59.207 1.00 19.29 ? 444 GLU A C 1 ATOM 3187 O O . GLU A 1 403 ? 1.055 61.282 60.209 1.00 19.03 ? 444 GLU A O 1 ATOM 3188 C CB . GLU A 1 403 ? -1.203 61.330 58.142 1.00 20.90 ? 444 GLU A CB 1 ATOM 3189 C CG . GLU A 1 403 ? -1.894 61.928 56.901 1.00 21.67 ? 444 GLU A CG 1 ATOM 3190 C CD . GLU A 1 403 ? -1.298 63.246 56.413 1.00 27.02 ? 444 GLU A CD 1 ATOM 3191 O OE1 . GLU A 1 403 ? -0.314 63.784 56.993 1.00 22.17 ? 444 GLU A OE1 1 ATOM 3192 O OE2 . GLU A 1 403 ? -1.814 63.738 55.374 1.00 26.20 ? 444 GLU A OE2 1 ATOM 3193 N N . ARG A 1 404 ? 1.420 59.298 59.117 1.00 19.13 ? 445 ARG A N 1 ATOM 3194 C CA . ARG A 1 404 ? 1.864 58.571 60.340 1.00 18.56 ? 445 ARG A CA 1 ATOM 3195 C C . ARG A 1 404 ? 3.249 57.968 60.204 1.00 20.38 ? 445 ARG A C 1 ATOM 3196 O O . ARG A 1 404 ? 3.815 57.503 61.202 1.00 20.76 ? 445 ARG A O 1 ATOM 3197 C CB . ARG A 1 404 ? 0.892 57.454 60.673 1.00 19.68 ? 445 ARG A CB 1 ATOM 3198 C CG . ARG A 1 404 ? -0.569 57.977 60.935 1.00 20.66 ? 445 ARG A CG 1 ATOM 3199 C CD . ARG A 1 404 ? -1.494 56.807 61.199 1.00 20.15 ? 445 ARG A CD 1 ATOM 3200 N NE . ARG A 1 404 ? -2.875 57.271 61.177 1.00 19.30 ? 445 ARG A NE 1 ATOM 3201 C CZ . ARG A 1 404 ? -3.944 56.453 61.149 1.00 18.99 ? 445 ARG A CZ 1 ATOM 3202 N NH1 . ARG A 1 404 ? -3.755 55.124 61.152 1.00 20.90 ? 445 ARG A NH1 1 ATOM 3203 N NH2 . ARG A 1 404 ? -5.160 56.985 61.034 1.00 19.96 ? 445 ARG A NH2 1 ATOM 3204 N N . GLY A 1 405 ? 3.818 58.003 59.007 1.00 18.96 ? 446 GLY A N 1 ATOM 3205 C CA . GLY A 1 405 ? 5.082 57.284 58.728 1.00 19.54 ? 446 GLY A CA 1 ATOM 3206 C C . GLY A 1 405 ? 6.282 58.057 59.257 1.00 19.11 ? 446 GLY A C 1 ATOM 3207 O O . GLY A 1 405 ? 6.647 59.130 58.743 1.00 20.39 ? 446 GLY A O 1 ATOM 3208 N N . VAL A 1 406 ? 6.931 57.489 60.247 1.00 20.03 ? 447 VAL A N 1 ATOM 3209 C CA . VAL A 1 406 ? 8.162 58.116 60.797 1.00 19.37 ? 447 VAL A CA 1 ATOM 3210 C C . VAL A 1 406 ? 9.401 57.803 59.937 1.00 19.81 ? 447 VAL A C 1 ATOM 3211 O O . VAL A 1 406 ? 10.167 58.693 59.553 1.00 19.30 ? 447 VAL A O 1 ATOM 3212 C CB . VAL A 1 406 ? 8.403 57.612 62.222 1.00 21.01 ? 447 VAL A CB 1 ATOM 3213 C CG1 . VAL A 1 406 ? 9.768 58.048 62.722 1.00 22.54 ? 447 VAL A CG1 1 ATOM 3214 C CG2 . VAL A 1 406 ? 7.269 58.218 63.059 1.00 22.86 ? 447 VAL A CG2 1 ATOM 3215 N N . ALA A 1 407 ? 9.587 56.534 59.631 1.00 19.18 ? 448 ALA A N 1 ATOM 3216 C CA . ALA A 1 407 ? 10.813 56.101 58.942 1.00 18.49 ? 448 ALA A CA 1 ATOM 3217 C C . ALA A 1 407 ? 10.602 54.725 58.359 1.00 19.66 ? 448 ALA A C 1 ATOM 3218 O O . ALA A 1 407 ? 9.745 53.952 58.844 1.00 20.35 ? 448 ALA A O 1 ATOM 3219 C CB . ALA A 1 407 ? 12.014 56.038 59.933 1.00 20.34 ? 448 ALA A CB 1 ATOM 3220 N N . TYR A 1 408 ? 11.370 54.472 57.300 1.00 18.68 ? 449 TYR A N 1 ATOM 3221 C CA . TYR A 1 408 ? 11.451 53.154 56.666 1.00 18.50 ? 449 TYR A CA 1 ATOM 3222 C C . TYR A 1 408 ? 12.911 52.749 56.619 1.00 19.26 ? 449 TYR A C 1 ATOM 3223 O O . TYR A 1 408 ? 13.789 53.482 56.078 1.00 19.35 ? 449 TYR A O 1 ATOM 3224 C CB . TYR A 1 408 ? 10.853 53.222 55.209 1.00 18.03 ? 449 TYR A CB 1 ATOM 3225 C CG . TYR A 1 408 ? 10.966 51.910 54.510 1.00 18.04 ? 449 TYR A CG 1 ATOM 3226 C CD1 . TYR A 1 408 ? 9.963 50.937 54.648 1.00 18.63 ? 449 TYR A CD1 1 ATOM 3227 C CD2 . TYR A 1 408 ? 12.062 51.640 53.702 1.00 21.11 ? 449 TYR A CD2 1 ATOM 3228 C CE1 . TYR A 1 408 ? 10.063 49.702 54.024 1.00 20.74 ? 449 TYR A CE1 1 ATOM 3229 C CE2 . TYR A 1 408 ? 12.198 50.379 53.048 1.00 19.61 ? 449 TYR A CE2 1 ATOM 3230 C CZ . TYR A 1 408 ? 11.192 49.446 53.227 1.00 20.39 ? 449 TYR A CZ 1 ATOM 3231 O OH . TYR A 1 408 ? 11.332 48.231 52.567 1.00 20.15 ? 449 TYR A OH 1 ATOM 3232 N N . ILE A 1 409 ? 13.162 51.563 57.149 1.00 18.44 ? 450 ILE A N 1 ATOM 3233 C CA . ILE A 1 409 ? 14.471 50.927 57.059 1.00 18.09 ? 450 ILE A CA 1 ATOM 3234 C C . ILE A 1 409 ? 14.348 49.691 56.174 1.00 18.15 ? 450 ILE A C 1 ATOM 3235 O O . ILE A 1 409 ? 13.526 48.792 56.454 1.00 19.12 ? 450 ILE A O 1 ATOM 3236 C CB . ILE A 1 409 ? 14.968 50.497 58.484 1.00 19.31 ? 450 ILE A CB 1 ATOM 3237 C CG1 . ILE A 1 409 ? 15.052 51.728 59.429 1.00 21.22 ? 450 ILE A CG1 1 ATOM 3238 C CG2 . ILE A 1 409 ? 16.358 49.800 58.416 1.00 20.91 ? 450 ILE A CG2 1 ATOM 3239 C CD1 . ILE A 1 409 ? 15.969 52.874 58.916 1.00 22.57 ? 450 ILE A CD1 1 ATOM 3240 N N . ASN A 1 410 ? 15.138 49.653 55.089 1.00 18.08 ? 451 ASN A N 1 ATOM 3241 C CA . ASN A 1 410 ? 15.086 48.529 54.172 1.00 19.19 ? 451 ASN A CA 1 ATOM 3242 C C . ASN A 1 410 ? 15.897 47.346 54.696 1.00 20.28 ? 451 ASN A C 1 ATOM 3243 O O . ASN A 1 410 ? 16.743 47.480 55.607 1.00 22.25 ? 451 ASN A O 1 ATOM 3244 C CB . ASN A 1 410 ? 15.667 48.972 52.827 1.00 18.81 ? 451 ASN A CB 1 ATOM 3245 C CG . ASN A 1 410 ? 15.113 48.162 51.652 1.00 20.03 ? 451 ASN A CG 1 ATOM 3246 O OD1 . ASN A 1 410 ? 13.897 48.000 51.489 1.00 21.35 ? 451 ASN A OD1 1 ATOM 3247 N ND2 . ASN A 1 410 ? 16.031 47.608 50.839 1.00 21.07 ? 451 ASN A ND2 1 ATOM 3248 N N . ALA A 1 411 ? 15.626 46.167 54.136 1.00 19.35 ? 452 ALA A N 1 ATOM 3249 C CA . ALA A 1 411 ? 16.364 44.964 54.596 1.00 20.79 ? 452 ALA A CA 1 ATOM 3250 C C . ALA A 1 411 ? 16.396 43.946 53.475 1.00 21.11 ? 452 ALA A C 1 ATOM 3251 O O . ALA A 1 411 ? 15.928 42.791 53.628 1.00 21.84 ? 452 ALA A O 1 ATOM 3252 C CB . ALA A 1 411 ? 15.649 44.393 55.831 1.00 22.55 ? 452 ALA A CB 1 ATOM 3253 N N . ASP A 1 412 ? 16.935 44.367 52.328 1.00 21.65 ? 453 ASP A N 1 ATOM 3254 C CA . ASP A 1 412 ? 17.355 43.390 51.338 1.00 21.10 ? 453 ASP A CA 1 ATOM 3255 C C . ASP A 1 412 ? 18.718 42.819 51.810 1.00 22.32 ? 453 ASP A C 1 ATOM 3256 O O . ASP A 1 412 ? 19.036 42.897 53.008 1.00 22.15 ? 453 ASP A O 1 ATOM 3257 C CB . ASP A 1 412 ? 17.374 43.986 49.918 1.00 20.11 ? 453 ASP A CB 1 ATOM 3258 C CG . ASP A 1 412 ? 17.303 42.930 48.801 1.00 23.82 ? 453 ASP A CG 1 ATOM 3259 O OD1 . ASP A 1 412 ? 17.462 41.745 49.050 1.00 23.92 ? 453 ASP A OD1 1 ATOM 3260 O OD2 . ASP A 1 412 ? 17.146 43.361 47.657 1.00 21.19 ? 453 ASP A OD2 1 ATOM 3261 N N . SER A 1 413 ? 19.486 42.217 50.914 1.00 21.36 ? 454 SER A N 1 ATOM 3262 C CA A SER A 1 413 ? 20.712 41.488 51.274 0.70 22.45 ? 454 SER A CA 1 ATOM 3263 C CA B SER A 1 413 ? 20.711 41.487 51.276 0.30 22.89 ? 454 SER A CA 1 ATOM 3264 C C . SER A 1 413 ? 21.557 42.171 52.363 1.00 23.23 ? 454 SER A C 1 ATOM 3265 O O . SER A 1 413 ? 21.861 43.364 52.277 1.00 23.26 ? 454 SER A O 1 ATOM 3266 C CB A SER A 1 413 ? 21.555 41.289 50.053 0.70 23.45 ? 454 SER A CB 1 ATOM 3267 C CB B SER A 1 413 ? 21.558 41.214 50.041 0.30 23.46 ? 454 SER A CB 1 ATOM 3268 O OG A SER A 1 413 ? 20.776 40.714 49.032 0.70 20.79 ? 454 SER A OG 1 ATOM 3269 O OG B SER A 1 413 ? 22.080 42.409 49.486 0.30 24.24 ? 454 SER A OG 1 ATOM 3270 N N . SER A 1 414 ? 21.902 41.401 53.388 1.00 23.44 ? 455 SER A N 1 ATOM 3271 C CA . SER A 1 414 ? 22.765 41.949 54.455 1.00 25.43 ? 455 SER A CA 1 ATOM 3272 C C . SER A 1 414 ? 24.225 42.056 54.036 1.00 24.85 ? 455 SER A C 1 ATOM 3273 O O . SER A 1 414 ? 24.986 42.803 54.666 1.00 25.83 ? 455 SER A O 1 ATOM 3274 C CB . SER A 1 414 ? 22.645 41.113 55.715 1.00 26.04 ? 455 SER A CB 1 ATOM 3275 O OG . SER A 1 414 ? 21.307 41.144 56.134 1.00 27.98 ? 455 SER A OG 1 ATOM 3276 N N . ILE A 1 415 ? 24.630 41.316 53.011 1.00 25.86 ? 456 ILE A N 1 ATOM 3277 C CA . ILE A 1 415 ? 26.023 41.305 52.566 1.00 28.25 ? 456 ILE A CA 1 ATOM 3278 C C . ILE A 1 415 ? 26.104 41.381 51.052 1.00 29.10 ? 456 ILE A C 1 ATOM 3279 O O . ILE A 1 415 ? 25.254 40.830 50.353 1.00 31.26 ? 456 ILE A O 1 ATOM 3280 C CB . ILE A 1 415 ? 26.760 40.004 53.040 1.00 28.18 ? 456 ILE A CB 1 ATOM 3281 C CG1 . ILE A 1 415 ? 25.910 38.735 52.698 1.00 30.64 ? 456 ILE A CG1 1 ATOM 3282 C CG2 . ILE A 1 415 ? 27.033 40.097 54.525 1.00 32.21 ? 456 ILE A CG2 1 ATOM 3283 C CD1 . ILE A 1 415 ? 26.713 37.443 52.429 1.00 33.27 ? 456 ILE A CD1 1 ATOM 3284 N N . GLU A 1 416 ? 27.109 42.067 50.540 1.00 28.61 ? 457 GLU A N 1 ATOM 3285 C CA . GLU A 1 416 ? 27.461 41.938 49.121 1.00 29.64 ? 457 GLU A CA 1 ATOM 3286 C C . GLU A 1 416 ? 28.990 41.857 49.049 1.00 29.96 ? 457 GLU A C 1 ATOM 3287 O O . GLU A 1 416 ? 29.594 41.963 47.970 1.00 31.44 ? 457 GLU A O 1 ATOM 3288 C CB . GLU A 1 416 ? 26.898 43.115 48.320 1.00 29.55 ? 457 GLU A CB 1 ATOM 3289 C CG . GLU A 1 416 ? 27.456 44.502 48.737 1.00 31.06 ? 457 GLU A CG 1 ATOM 3290 C CD . GLU A 1 416 ? 26.706 45.694 48.113 1.00 30.39 ? 457 GLU A CD 1 ATOM 3291 O OE1 . GLU A 1 416 ? 25.604 45.516 47.485 1.00 30.25 ? 457 GLU A OE1 1 ATOM 3292 O OE2 . GLU A 1 416 ? 27.202 46.843 48.270 1.00 30.14 ? 457 GLU A OE2 1 ATOM 3293 N N . GLY A 1 417 ? 29.602 41.676 50.219 1.00 30.45 ? 458 GLY A N 1 ATOM 3294 C CA . GLY A 1 417 ? 31.050 41.622 50.401 1.00 30.51 ? 458 GLY A CA 1 ATOM 3295 C C . GLY A 1 417 ? 31.321 41.458 51.892 1.00 31.76 ? 458 GLY A C 1 ATOM 3296 O O . GLY A 1 417 ? 30.373 41.344 52.684 1.00 31.99 ? 458 GLY A O 1 ATOM 3297 N N . ASN A 1 418 ? 32.590 41.426 52.280 1.00 30.83 ? 459 ASN A N 1 ATOM 3298 C CA . ASN A 1 418 ? 32.946 41.253 53.690 1.00 31.68 ? 459 ASN A CA 1 ATOM 3299 C C . ASN A 1 418 ? 33.981 42.295 54.163 1.00 31.06 ? 459 ASN A C 1 ATOM 3300 O O . ASN A 1 418 ? 34.727 42.055 55.115 1.00 33.03 ? 459 ASN A O 1 ATOM 3301 C CB . ASN A 1 418 ? 33.451 39.801 53.925 1.00 32.75 ? 459 ASN A CB 1 ATOM 3302 C CG . ASN A 1 418 ? 34.761 39.493 53.197 1.00 35.41 ? 459 ASN A CG 1 ATOM 3303 O OD1 . ASN A 1 418 ? 35.353 40.355 52.547 1.00 38.09 ? 459 ASN A OD1 1 ATOM 3304 N ND2 . ASN A 1 418 ? 35.241 38.249 53.329 1.00 42.62 ? 459 ASN A ND2 1 ATOM 3305 N N . TYR A 1 419 ? 34.032 43.441 53.483 1.00 30.82 ? 460 TYR A N 1 ATOM 3306 C CA . TYR A 1 419 ? 35.091 44.426 53.704 1.00 31.08 ? 460 TYR A CA 1 ATOM 3307 C C . TYR A 1 419 ? 34.675 45.449 54.750 1.00 30.98 ? 460 TYR A C 1 ATOM 3308 O O . TYR A 1 419 ? 35.352 45.639 55.757 1.00 31.83 ? 460 TYR A O 1 ATOM 3309 C CB . TYR A 1 419 ? 35.454 45.122 52.385 1.00 31.63 ? 460 TYR A CB 1 ATOM 3310 C CG . TYR A 1 419 ? 36.538 46.145 52.536 1.00 35.60 ? 460 TYR A CG 1 ATOM 3311 C CD1 . TYR A 1 419 ? 37.833 45.762 52.948 1.00 39.75 ? 460 TYR A CD1 1 ATOM 3312 C CD2 . TYR A 1 419 ? 36.294 47.483 52.257 1.00 40.17 ? 460 TYR A CD2 1 ATOM 3313 C CE1 . TYR A 1 419 ? 38.852 46.705 53.093 1.00 43.64 ? 460 TYR A CE1 1 ATOM 3314 C CE2 . TYR A 1 419 ? 37.315 48.438 52.404 1.00 42.90 ? 460 TYR A CE2 1 ATOM 3315 C CZ . TYR A 1 419 ? 38.572 48.043 52.806 1.00 44.93 ? 460 TYR A CZ 1 ATOM 3316 O OH . TYR A 1 419 ? 39.561 48.996 52.943 1.00 49.70 ? 460 TYR A OH 1 ATOM 3317 N N . THR A 1 420 ? 33.569 46.128 54.512 1.00 29.26 ? 461 THR A N 1 ATOM 3318 C CA . THR A 1 420 ? 33.164 47.156 55.498 1.00 29.51 ? 461 THR A CA 1 ATOM 3319 C C . THR A 1 420 ? 31.680 47.438 55.410 1.00 28.03 ? 461 THR A C 1 ATOM 3320 O O . THR A 1 420 ? 30.965 46.902 54.546 1.00 27.50 ? 461 THR A O 1 ATOM 3321 C CB . THR A 1 420 ? 33.985 48.476 55.358 1.00 30.70 ? 461 THR A CB 1 ATOM 3322 O OG1 . THR A 1 420 ? 33.805 49.317 56.516 1.00 32.71 ? 461 THR A OG1 1 ATOM 3323 C CG2 . THR A 1 420 ? 33.596 49.243 54.118 1.00 30.38 ? 461 THR A CG2 1 ATOM 3324 N N . LEU A 1 421 ? 31.204 48.316 56.283 1.00 27.17 ? 462 LEU A N 1 ATOM 3325 C CA . LEU A 1 421 ? 29.790 48.733 56.225 1.00 26.10 ? 462 LEU A CA 1 ATOM 3326 C C . LEU A 1 421 ? 29.474 49.672 55.056 1.00 25.98 ? 462 LEU A C 1 ATOM 3327 O O . LEU A 1 421 ? 30.335 50.476 54.650 1.00 27.40 ? 462 LEU A O 1 ATOM 3328 C CB . LEU A 1 421 ? 29.443 49.471 57.531 1.00 26.24 ? 462 LEU A CB 1 ATOM 3329 C CG . LEU A 1 421 ? 27.950 49.698 57.789 1.00 25.30 ? 462 LEU A CG 1 ATOM 3330 C CD1 . LEU A 1 421 ? 27.201 48.376 57.980 1.00 28.10 ? 462 LEU A CD1 1 ATOM 3331 C CD2 . LEU A 1 421 ? 27.818 50.573 59.046 1.00 27.89 ? 462 LEU A CD2 1 ATOM 3332 N N . ARG A 1 422 ? 28.254 49.558 54.525 1.00 24.21 ? 463 ARG A N 1 ATOM 3333 C CA . ARG A 1 422 ? 27.737 50.480 53.535 1.00 25.23 ? 463 ARG A CA 1 ATOM 3334 C C . ARG A 1 422 ? 26.419 50.989 54.086 1.00 24.76 ? 463 ARG A C 1 ATOM 3335 O O . ARG A 1 422 ? 25.573 50.199 54.503 1.00 24.89 ? 463 ARG A O 1 ATOM 3336 C CB . ARG A 1 422 ? 27.468 49.744 52.204 1.00 25.79 ? 463 ARG A CB 1 ATOM 3337 C CG . ARG A 1 422 ? 26.695 50.611 51.211 1.00 29.92 ? 463 ARG A CG 1 ATOM 3338 C CD . ARG A 1 422 ? 26.401 49.871 49.912 1.00 32.54 ? 463 ARG A CD 1 ATOM 3339 N NE . ARG A 1 422 ? 25.310 50.554 49.199 1.00 33.51 ? 463 ARG A NE 1 ATOM 3340 C CZ . ARG A 1 422 ? 24.712 50.071 48.117 1.00 35.95 ? 463 ARG A CZ 1 ATOM 3341 N NH1 . ARG A 1 422 ? 25.090 48.896 47.610 1.00 35.38 ? 463 ARG A NH1 1 ATOM 3342 N NH2 . ARG A 1 422 ? 23.726 50.764 47.546 1.00 34.46 ? 463 ARG A NH2 1 ATOM 3343 N N . VAL A 1 423 ? 26.234 52.309 54.082 1.00 24.50 ? 464 VAL A N 1 ATOM 3344 C CA . VAL A 1 423 ? 24.957 52.914 54.504 1.00 22.70 ? 464 VAL A CA 1 ATOM 3345 C C . VAL A 1 423 ? 24.532 53.933 53.475 1.00 23.14 ? 464 VAL A C 1 ATOM 3346 O O . VAL A 1 423 ? 25.351 54.744 53.049 1.00 24.07 ? 464 VAL A O 1 ATOM 3347 C CB . VAL A 1 423 ? 25.097 53.647 55.863 1.00 23.55 ? 464 VAL A CB 1 ATOM 3348 C CG1 . VAL A 1 423 ? 23.761 54.301 56.207 1.00 23.61 ? 464 VAL A CG1 1 ATOM 3349 C CG2 . VAL A 1 423 ? 25.477 52.656 56.942 1.00 26.24 ? 464 VAL A CG2 1 ATOM 3350 N N . ASP A 1 424 ? 23.289 53.843 53.018 1.00 22.19 ? 465 ASP A N 1 ATOM 3351 C CA . ASP A 1 424 ? 22.711 54.873 52.135 1.00 23.12 ? 465 ASP A CA 1 ATOM 3352 C C . ASP A 1 424 ? 21.478 55.341 52.899 1.00 22.64 ? 465 ASP A C 1 ATOM 3353 O O . ASP A 1 424 ? 20.622 54.527 53.259 1.00 21.87 ? 465 ASP A O 1 ATOM 3354 C CB . ASP A 1 424 ? 22.222 54.336 50.758 1.00 22.71 ? 465 ASP A CB 1 ATOM 3355 C CG . ASP A 1 424 ? 23.260 53.526 49.960 1.00 27.65 ? 465 ASP A CG 1 ATOM 3356 O OD1 . ASP A 1 424 ? 24.402 53.309 50.380 1.00 27.44 ? 465 ASP A OD1 1 ATOM 3357 O OD2 . ASP A 1 424 ? 22.856 53.059 48.829 1.00 31.42 ? 465 ASP A OD2 1 ATOM 3358 N N . CYS A 1 425 ? 21.315 56.646 53.106 1.00 22.70 ? 466 CYS A N 1 ATOM 3359 C CA . CYS A 1 425 ? 20.133 57.109 53.865 1.00 21.18 ? 466 CYS A CA 1 ATOM 3360 C C . CYS A 1 425 ? 19.940 58.586 53.712 1.00 21.72 ? 466 CYS A C 1 ATOM 3361 O O . CYS A 1 425 ? 20.811 59.294 53.221 1.00 25.06 ? 466 CYS A O 1 ATOM 3362 C CB . CYS A 1 425 ? 20.240 56.768 55.388 1.00 21.59 ? 466 CYS A CB 1 ATOM 3363 S SG . CYS A 1 425 ? 21.561 57.643 56.277 1.00 24.30 ? 466 CYS A SG 1 ATOM 3364 N N . THR A 1 426 ? 18.778 59.063 54.140 1.00 20.67 ? 467 THR A N 1 ATOM 3365 C CA . THR A 1 426 ? 18.530 60.488 54.237 1.00 20.30 ? 467 THR A CA 1 ATOM 3366 C C . THR A 1 426 ? 19.498 61.176 55.214 1.00 22.23 ? 467 THR A C 1 ATOM 3367 O O . THR A 1 426 ? 19.864 60.591 56.225 1.00 21.58 ? 467 THR A O 1 ATOM 3368 C CB . THR A 1 426 ? 17.075 60.721 54.678 1.00 19.35 ? 467 THR A CB 1 ATOM 3369 O OG1 . THR A 1 426 ? 16.873 62.123 54.923 1.00 20.34 ? 467 THR A OG1 1 ATOM 3370 C CG2 . THR A 1 426 ? 16.712 59.961 56.008 1.00 20.45 ? 467 THR A CG2 1 ATOM 3371 N N . PRO A 1 427 ? 19.887 62.421 54.916 1.00 21.36 ? 468 PRO A N 1 ATOM 3372 C CA . PRO A 1 427 ? 20.674 63.213 55.890 1.00 22.36 ? 468 PRO A CA 1 ATOM 3373 C C . PRO A 1 427 ? 20.036 63.204 57.282 1.00 22.24 ? 468 PRO A C 1 ATOM 3374 O O . PRO A 1 427 ? 20.782 63.344 58.257 1.00 23.70 ? 468 PRO A O 1 ATOM 3375 C CB . PRO A 1 427 ? 20.658 64.643 55.314 1.00 24.90 ? 468 PRO A CB 1 ATOM 3376 C CG . PRO A 1 427 ? 20.543 64.383 53.828 1.00 22.84 ? 468 PRO A CG 1 ATOM 3377 C CD . PRO A 1 427 ? 19.558 63.199 53.695 1.00 22.14 ? 468 PRO A CD 1 ATOM 3378 N N . LEU A 1 428 ? 18.689 63.093 57.367 1.00 21.30 ? 469 LEU A N 1 ATOM 3379 C CA . LEU A 1 428 ? 18.052 63.130 58.720 1.00 22.69 ? 469 LEU A CA 1 ATOM 3380 C C . LEU A 1 428 ? 18.507 62.002 59.606 1.00 22.78 ? 469 LEU A C 1 ATOM 3381 O O . LEU A 1 428 ? 18.371 62.099 60.831 1.00 25.51 ? 469 LEU A O 1 ATOM 3382 C CB . LEU A 1 428 ? 16.532 63.035 58.607 1.00 20.91 ? 469 LEU A CB 1 ATOM 3383 C CG . LEU A 1 428 ? 15.965 64.306 58.030 1.00 21.58 ? 469 LEU A CG 1 ATOM 3384 C CD1 . LEU A 1 428 ? 14.467 64.131 57.949 1.00 23.11 ? 469 LEU A CD1 1 ATOM 3385 C CD2 . LEU A 1 428 ? 16.361 65.595 58.861 1.00 22.82 ? 469 LEU A CD2 1 ATOM 3386 N N . MET A 1 429 ? 19.063 60.943 59.020 1.00 23.09 ? 470 MET A N 1 ATOM 3387 C CA A MET A 1 429 ? 19.533 59.767 59.795 0.70 22.76 ? 470 MET A CA 1 ATOM 3388 C CA B MET A 1 429 ? 19.522 59.850 59.876 0.30 23.12 ? 470 MET A CA 1 ATOM 3389 C C . MET A 1 429 ? 21.036 59.708 60.008 1.00 23.80 ? 470 MET A C 1 ATOM 3390 O O . MET A 1 429 ? 21.516 58.779 60.652 1.00 23.75 ? 470 MET A O 1 ATOM 3391 C CB A MET A 1 429 ? 19.113 58.456 59.105 0.70 23.24 ? 470 MET A CB 1 ATOM 3392 C CB B MET A 1 429 ? 18.849 58.538 59.484 0.30 23.28 ? 470 MET A CB 1 ATOM 3393 C CG A MET A 1 429 ? 17.633 58.151 59.218 0.70 21.28 ? 470 MET A CG 1 ATOM 3394 C CG B MET A 1 429 ? 17.411 58.493 59.935 0.30 22.62 ? 470 MET A CG 1 ATOM 3395 S SD A MET A 1 429 ? 17.236 56.564 58.465 0.70 23.18 ? 470 MET A SD 1 ATOM 3396 S SD B MET A 1 429 ? 16.589 56.919 59.717 0.30 24.15 ? 470 MET A SD 1 ATOM 3397 C CE A MET A 1 429 ? 15.443 56.656 58.484 0.70 24.24 ? 470 MET A CE 1 ATOM 3398 C CE B MET A 1 429 ? 16.132 57.000 57.984 0.30 23.34 ? 470 MET A CE 1 ATOM 3399 N N . TYR A 1 430 ? 21.790 60.674 59.477 1.00 23.88 ? 471 TYR A N 1 ATOM 3400 C CA . TYR A 1 430 ? 23.242 60.613 59.623 1.00 24.07 ? 471 TYR A CA 1 ATOM 3401 C C . TYR A 1 430 ? 23.688 60.520 61.078 1.00 25.74 ? 471 TYR A C 1 ATOM 3402 O O . TYR A 1 430 ? 24.571 59.709 61.424 1.00 26.58 ? 471 TYR A O 1 ATOM 3403 C CB . TYR A 1 430 ? 23.925 61.836 59.018 1.00 24.64 ? 471 TYR A CB 1 ATOM 3404 C CG . TYR A 1 430 ? 23.948 61.959 57.500 1.00 23.93 ? 471 TYR A CG 1 ATOM 3405 C CD1 . TYR A 1 430 ? 23.450 60.954 56.663 1.00 23.93 ? 471 TYR A CD1 1 ATOM 3406 C CD2 . TYR A 1 430 ? 24.484 63.109 56.916 1.00 26.22 ? 471 TYR A CD2 1 ATOM 3407 C CE1 . TYR A 1 430 ? 23.496 61.141 55.253 1.00 25.20 ? 471 TYR A CE1 1 ATOM 3408 C CE2 . TYR A 1 430 ? 24.517 63.285 55.551 1.00 27.49 ? 471 TYR A CE2 1 ATOM 3409 C CZ . TYR A 1 430 ? 24.050 62.305 54.739 1.00 27.52 ? 471 TYR A CZ 1 ATOM 3410 O OH . TYR A 1 430 ? 24.107 62.527 53.372 1.00 30.11 ? 471 TYR A OH 1 ATOM 3411 N N . SER A 1 431 ? 23.121 61.373 61.930 1.00 24.74 ? 472 SER A N 1 ATOM 3412 C CA . SER A 1 431 ? 23.626 61.420 63.336 1.00 25.87 ? 472 SER A CA 1 ATOM 3413 C C . SER A 1 431 ? 23.225 60.154 64.066 1.00 25.97 ? 472 SER A C 1 ATOM 3414 O O . SER A 1 431 ? 24.014 59.648 64.885 1.00 26.40 ? 472 SER A O 1 ATOM 3415 C CB . SER A 1 431 ? 23.073 62.670 64.012 1.00 26.76 ? 472 SER A CB 1 ATOM 3416 O OG A SER A 1 431 ? 23.731 63.796 63.411 0.50 29.26 ? 472 SER A OG 1 ATOM 3417 O OG B SER A 1 431 ? 23.473 62.806 65.387 0.50 23.45 ? 472 SER A OG 1 ATOM 3418 N N . LEU A 1 432 ? 22.032 59.645 63.771 1.00 25.90 ? 473 LEU A N 1 ATOM 3419 C CA . LEU A 1 432 ? 21.573 58.375 64.349 1.00 26.61 ? 473 LEU A CA 1 ATOM 3420 C C . LEU A 1 432 ? 22.586 57.280 63.997 1.00 26.54 ? 473 LEU A C 1 ATOM 3421 O O . LEU A 1 432 ? 22.997 56.495 64.842 1.00 27.80 ? 473 LEU A O 1 ATOM 3422 C CB . LEU A 1 432 ? 20.194 58.005 63.817 1.00 26.27 ? 473 LEU A CB 1 ATOM 3423 C CG . LEU A 1 432 ? 19.680 56.575 64.023 1.00 26.90 ? 473 LEU A CG 1 ATOM 3424 C CD1 . LEU A 1 432 ? 19.571 56.187 65.504 1.00 30.93 ? 473 LEU A CD1 1 ATOM 3425 C CD2 . LEU A 1 432 ? 18.375 56.434 63.232 1.00 31.08 ? 473 LEU A CD2 1 ATOM 3426 N N . VAL A 1 433 ? 22.949 57.211 62.722 1.00 25.67 ? 474 VAL A N 1 ATOM 3427 C CA . VAL A 1 433 ? 23.879 56.137 62.278 1.00 26.20 ? 474 VAL A CA 1 ATOM 3428 C C . VAL A 1 433 ? 25.243 56.283 62.872 1.00 27.68 ? 474 VAL A C 1 ATOM 3429 O O . VAL A 1 433 ? 25.820 55.272 63.316 1.00 28.30 ? 474 VAL A O 1 ATOM 3430 C CB . VAL A 1 433 ? 23.972 56.159 60.749 1.00 25.01 ? 474 VAL A CB 1 ATOM 3431 C CG1 . VAL A 1 433 ? 25.063 55.185 60.265 1.00 29.27 ? 474 VAL A CG1 1 ATOM 3432 C CG2 . VAL A 1 433 ? 22.620 55.733 60.161 1.00 26.61 ? 474 VAL A CG2 1 ATOM 3433 N N . HIS A 1 434 ? 25.775 57.510 62.927 1.00 27.94 ? 475 HIS A N 1 ATOM 3434 C CA . HIS A 1 434 ? 27.081 57.739 63.552 1.00 29.62 ? 475 HIS A CA 1 ATOM 3435 C C . HIS A 1 434 ? 27.025 57.284 65.018 1.00 29.85 ? 475 HIS A C 1 ATOM 3436 O O . HIS A 1 434 ? 27.883 56.507 65.456 1.00 32.05 ? 475 HIS A O 1 ATOM 3437 C CB . HIS A 1 434 ? 27.498 59.218 63.503 1.00 29.46 ? 475 HIS A CB 1 ATOM 3438 C CG . HIS A 1 434 ? 27.730 59.745 62.118 1.00 33.73 ? 475 HIS A CG 1 ATOM 3439 N ND1 . HIS A 1 434 ? 27.566 61.078 61.798 1.00 40.10 ? 475 HIS A ND1 1 ATOM 3440 C CD2 . HIS A 1 434 ? 28.026 59.113 60.961 1.00 36.06 ? 475 HIS A CD2 1 ATOM 3441 C CE1 . HIS A 1 434 ? 27.822 61.247 60.513 1.00 41.13 ? 475 HIS A CE1 1 ATOM 3442 N NE2 . HIS A 1 434 ? 28.121 60.074 59.990 1.00 34.84 ? 475 HIS A NE2 1 ATOM 3443 N N . ASN A 1 435 ? 25.991 57.721 65.742 1.00 28.38 ? 476 ASN A N 1 ATOM 3444 C CA . ASN A 1 435 ? 25.925 57.421 67.187 1.00 30.33 ? 476 ASN A CA 1 ATOM 3445 C C . ASN A 1 435 ? 25.767 55.953 67.443 1.00 30.58 ? 476 ASN A C 1 ATOM 3446 O O . ASN A 1 435 ? 26.385 55.405 68.371 1.00 31.99 ? 476 ASN A O 1 ATOM 3447 C CB . ASN A 1 435 ? 24.784 58.182 67.868 1.00 30.56 ? 476 ASN A CB 1 ATOM 3448 C CG . ASN A 1 435 ? 25.060 59.657 67.990 1.00 33.50 ? 476 ASN A CG 1 ATOM 3449 O OD1 . ASN A 1 435 ? 26.089 60.162 67.533 1.00 33.34 ? 476 ASN A OD1 1 ATOM 3450 N ND2 . ASN A 1 435 ? 24.121 60.369 68.629 1.00 31.62 ? 476 ASN A ND2 1 ATOM 3451 N N . LEU A 1 436 ? 24.979 55.286 66.613 1.00 29.70 ? 477 LEU A N 1 ATOM 3452 C CA . LEU A 1 436 ? 24.741 53.865 66.813 1.00 28.37 ? 477 LEU A CA 1 ATOM 3453 C C . LEU A 1 436 ? 26.011 53.098 66.515 1.00 28.31 ? 477 LEU A C 1 ATOM 3454 O O . LEU A 1 436 ? 26.379 52.213 67.274 1.00 28.97 ? 477 LEU A O 1 ATOM 3455 C CB . LEU A 1 436 ? 23.574 53.391 65.890 1.00 26.76 ? 477 LEU A CB 1 ATOM 3456 C CG . LEU A 1 436 ? 23.333 51.886 65.929 1.00 29.36 ? 477 LEU A CG 1 ATOM 3457 C CD1 . LEU A 1 436 ? 23.083 51.396 67.361 1.00 30.46 ? 477 LEU A CD1 1 ATOM 3458 C CD2 . LEU A 1 436 ? 22.186 51.483 64.955 1.00 28.08 ? 477 LEU A CD2 1 ATOM 3459 N N . THR A 1 437 ? 26.670 53.404 65.397 1.00 29.01 ? 478 THR A N 1 ATOM 3460 C CA . THR A 1 437 ? 27.879 52.631 65.038 1.00 28.33 ? 478 THR A CA 1 ATOM 3461 C C . THR A 1 437 ? 29.041 52.838 66.005 1.00 30.77 ? 478 THR A C 1 ATOM 3462 O O . THR A 1 437 ? 29.915 51.976 66.107 1.00 30.98 ? 478 THR A O 1 ATOM 3463 C CB . THR A 1 437 ? 28.336 52.841 63.581 1.00 28.56 ? 478 THR A CB 1 ATOM 3464 O OG1 . THR A 1 437 ? 28.655 54.213 63.356 1.00 27.94 ? 478 THR A OG1 1 ATOM 3465 C CG2 . THR A 1 437 ? 27.229 52.370 62.585 1.00 25.90 ? 478 THR A CG2 1 ATOM 3466 N N . LYS A 1 438 ? 29.032 53.950 66.734 1.00 31.72 ? 479 LYS A N 1 ATOM 3467 C CA . LYS A 1 438 ? 30.053 54.182 67.754 1.00 33.86 ? 479 LYS A CA 1 ATOM 3468 C C . LYS A 1 438 ? 29.844 53.258 68.953 1.00 34.68 ? 479 LYS A C 1 ATOM 3469 O O . LYS A 1 438 ? 30.781 53.036 69.757 1.00 35.92 ? 479 LYS A O 1 ATOM 3470 C CB . LYS A 1 438 ? 30.043 55.662 68.177 1.00 34.83 ? 479 LYS A CB 1 ATOM 3471 C CG . LYS A 1 438 ? 30.704 56.628 67.148 1.00 35.23 ? 479 LYS A CG 1 ATOM 3472 C CD . LYS A 1 438 ? 30.513 58.102 67.516 1.00 39.70 ? 479 LYS A CD 1 ATOM 3473 C CE . LYS A 1 438 ? 30.998 59.010 66.382 1.00 39.73 ? 479 LYS A CE 1 ATOM 3474 N NZ . LYS A 1 438 ? 30.991 60.475 66.761 1.00 40.20 ? 479 LYS A NZ 1 ATOM 3475 N N . GLU A 1 439 ? 28.629 52.726 69.084 1.00 34.26 ? 480 GLU A N 1 ATOM 3476 C CA . GLU A 1 439 ? 28.280 51.845 70.212 1.00 36.11 ? 480 GLU A CA 1 ATOM 3477 C C . GLU A 1 439 ? 28.291 50.359 69.880 1.00 35.28 ? 480 GLU A C 1 ATOM 3478 O O . GLU A 1 439 ? 28.096 49.517 70.766 1.00 37.15 ? 480 GLU A O 1 ATOM 3479 C CB . GLU A 1 439 ? 26.891 52.188 70.757 1.00 36.85 ? 480 GLU A CB 1 ATOM 3480 C CG . GLU A 1 439 ? 26.743 53.612 71.274 1.00 44.21 ? 480 GLU A CG 1 ATOM 3481 C CD . GLU A 1 439 ? 27.734 53.994 72.369 1.00 50.35 ? 480 GLU A CD 1 ATOM 3482 O OE1 . GLU A 1 439 ? 28.164 53.117 73.180 1.00 53.60 ? 480 GLU A OE1 1 ATOM 3483 O OE2 . GLU A 1 439 ? 28.081 55.203 72.423 1.00 55.11 ? 480 GLU A OE2 1 ATOM 3484 N N . LEU A 1 440 ? 28.521 50.028 68.615 1.00 33.12 ? 481 LEU A N 1 ATOM 3485 C CA . LEU A 1 440 ? 28.570 48.635 68.193 1.00 31.94 ? 481 LEU A CA 1 ATOM 3486 C C . LEU A 1 440 ? 30.004 48.177 68.010 1.00 33.70 ? 481 LEU A C 1 ATOM 3487 O O . LEU A 1 440 ? 30.880 48.992 67.704 1.00 34.77 ? 481 LEU A O 1 ATOM 3488 C CB . LEU A 1 440 ? 27.815 48.469 66.863 1.00 30.58 ? 481 LEU A CB 1 ATOM 3489 C CG . LEU A 1 440 ? 26.336 48.838 66.909 1.00 30.02 ? 481 LEU A CG 1 ATOM 3490 C CD1 . LEU A 1 440 ? 25.717 48.669 65.503 1.00 27.45 ? 481 LEU A CD1 1 ATOM 3491 C CD2 . LEU A 1 440 ? 25.569 47.986 67.894 1.00 32.15 ? 481 LEU A CD2 1 ATOM 3492 N N . LYS A 1 441 ? 30.225 46.885 68.224 1.00 33.54 ? 482 LYS A N 1 ATOM 3493 C CA . LYS A 1 441 ? 31.563 46.296 68.059 1.00 35.81 ? 482 LYS A CA 1 ATOM 3494 C C . LYS A 1 441 ? 31.883 46.076 66.589 1.00 35.08 ? 482 LYS A C 1 ATOM 3495 O O . LYS A 1 441 ? 31.004 45.660 65.809 1.00 35.35 ? 482 LYS A O 1 ATOM 3496 C CB . LYS A 1 441 ? 31.683 44.986 68.833 1.00 37.05 ? 482 LYS A CB 1 ATOM 3497 C CG . LYS A 1 441 ? 31.390 45.087 70.324 1.00 41.21 ? 482 LYS A CG 1 ATOM 3498 C CD . LYS A 1 441 ? 31.829 43.794 71.021 1.00 48.55 ? 482 LYS A CD 1 ATOM 3499 C CE . LYS A 1 441 ? 30.888 43.370 72.164 1.00 53.38 ? 482 LYS A CE 1 ATOM 3500 N NZ . LYS A 1 441 ? 31.038 44.178 73.407 1.00 58.09 ? 482 LYS A NZ 1 ATOM 3501 N N . SER A 1 442 ? 33.106 46.388 66.173 1.00 35.27 ? 483 SER A N 1 ATOM 3502 C CA . SER A 1 442 ? 33.509 46.035 64.797 1.00 35.22 ? 483 SER A CA 1 ATOM 3503 C C . SER A 1 442 ? 33.723 44.537 64.700 1.00 34.49 ? 483 SER A C 1 ATOM 3504 O O . SER A 1 442 ? 34.393 43.955 65.575 1.00 35.68 ? 483 SER A O 1 ATOM 3505 C CB . SER A 1 442 ? 34.802 46.745 64.370 1.00 35.64 ? 483 SER A CB 1 ATOM 3506 O OG . SER A 1 442 ? 35.170 46.346 63.051 1.00 36.91 ? 483 SER A OG 1 ATOM 3507 N N . PRO A 1 443 ? 33.208 43.898 63.632 1.00 33.49 ? 484 PRO A N 1 ATOM 3508 C CA . PRO A 1 443 ? 33.440 42.468 63.402 1.00 34.18 ? 484 PRO A CA 1 ATOM 3509 C C . PRO A 1 443 ? 34.725 42.211 62.603 1.00 34.80 ? 484 PRO A C 1 ATOM 3510 O O . PRO A 1 443 ? 35.053 41.050 62.332 1.00 35.97 ? 484 PRO A O 1 ATOM 3511 C CB . PRO A 1 443 ? 32.237 42.055 62.531 1.00 32.78 ? 484 PRO A CB 1 ATOM 3512 C CG . PRO A 1 443 ? 31.932 43.305 61.689 1.00 31.71 ? 484 PRO A CG 1 ATOM 3513 C CD . PRO A 1 443 ? 32.343 44.516 62.593 1.00 32.67 ? 484 PRO A CD 1 ATOM 3514 N N . ASP A 1 444 ? 35.411 43.281 62.186 1.00 35.40 ? 485 ASP A N 1 ATOM 3515 C CA . ASP A 1 444 ? 36.492 43.167 61.189 1.00 35.74 ? 485 ASP A CA 1 ATOM 3516 C C . ASP A 1 444 ? 37.784 42.670 61.829 1.00 37.75 ? 485 ASP A C 1 ATOM 3517 O O . ASP A 1 444 ? 38.100 43.041 62.962 1.00 38.19 ? 485 ASP A O 1 ATOM 3518 C CB . ASP A 1 444 ? 36.813 44.526 60.545 1.00 35.03 ? 485 ASP A CB 1 ATOM 3519 C CG . ASP A 1 444 ? 35.635 45.149 59.796 1.00 35.67 ? 485 ASP A CG 1 ATOM 3520 O OD1 . ASP A 1 444 ? 34.513 44.598 59.774 1.00 38.09 ? 485 ASP A OD1 1 ATOM 3521 O OD2 . ASP A 1 444 ? 35.863 46.228 59.228 1.00 34.96 ? 485 ASP A OD2 1 ATOM 3522 N N . GLU A 1 445 ? 38.527 41.862 61.079 1.00 39.04 ? 486 GLU A N 1 ATOM 3523 C CA . GLU A 1 445 ? 39.905 41.485 61.453 1.00 42.12 ? 486 GLU A CA 1 ATOM 3524 C C . GLU A 1 445 ? 40.781 42.718 61.624 1.00 41.84 ? 486 GLU A C 1 ATOM 3525 O O . GLU A 1 445 ? 40.793 43.599 60.767 1.00 41.93 ? 486 GLU A O 1 ATOM 3526 C CB . GLU A 1 445 ? 40.550 40.618 60.367 1.00 43.16 ? 486 GLU A CB 1 ATOM 3527 C CG . GLU A 1 445 ? 39.620 39.750 59.553 1.00 49.18 ? 486 GLU A CG 1 ATOM 3528 C CD . GLU A 1 445 ? 38.971 38.635 60.355 1.00 56.42 ? 486 GLU A CD 1 ATOM 3529 O OE1 . GLU A 1 445 ? 39.575 38.222 61.381 1.00 59.97 ? 486 GLU A OE1 1 ATOM 3530 O OE2 . GLU A 1 445 ? 37.869 38.170 59.941 1.00 58.10 ? 486 GLU A OE2 1 ATOM 3531 N N . GLY A 1 446 ? 41.514 42.780 62.723 1.00 43.46 ? 487 GLY A N 1 ATOM 3532 C CA . GLY A 1 446 ? 42.411 43.908 62.972 1.00 43.88 ? 487 GLY A CA 1 ATOM 3533 C C . GLY A 1 446 ? 41.738 45.020 63.736 1.00 44.07 ? 487 GLY A C 1 ATOM 3534 O O . GLY A 1 446 ? 42.390 45.985 64.136 1.00 45.43 ? 487 GLY A O 1 ATOM 3535 N N . PHE A 1 447 ? 40.413 44.918 63.908 1.00 41.51 ? 488 PHE A N 1 ATOM 3536 C CA . PHE A 1 447 ? 39.683 45.909 64.670 1.00 41.50 ? 488 PHE A CA 1 ATOM 3537 C C . PHE A 1 447 ? 38.991 45.331 65.896 1.00 42.06 ? 488 PHE A C 1 ATOM 3538 O O . PHE A 1 447 ? 38.007 45.899 66.366 1.00 42.32 ? 488 PHE A O 1 ATOM 3539 C CB . PHE A 1 447 ? 38.650 46.599 63.752 1.00 39.44 ? 488 PHE A CB 1 ATOM 3540 C CG . PHE A 1 447 ? 39.269 47.452 62.709 1.00 39.94 ? 488 PHE A CG 1 ATOM 3541 C CD1 . PHE A 1 447 ? 39.505 48.793 62.946 1.00 40.01 ? 488 PHE A CD1 1 ATOM 3542 C CD2 . PHE A 1 447 ? 39.648 46.905 61.480 1.00 42.37 ? 488 PHE A CD2 1 ATOM 3543 C CE1 . PHE A 1 447 ? 40.084 49.607 61.965 1.00 42.22 ? 488 PHE A CE1 1 ATOM 3544 C CE2 . PHE A 1 447 ? 40.228 47.703 60.492 1.00 41.12 ? 488 PHE A CE2 1 ATOM 3545 C CZ . PHE A 1 447 ? 40.446 49.049 60.733 1.00 43.65 ? 488 PHE A CZ 1 ATOM 3546 N N . GLU A 1 448 ? 39.479 44.209 66.418 1.00 43.85 ? 489 GLU A N 1 ATOM 3547 C CA . GLU A 1 448 ? 38.862 43.638 67.614 1.00 45.77 ? 489 GLU A CA 1 ATOM 3548 C C . GLU A 1 448 ? 38.969 44.632 68.773 1.00 46.64 ? 489 GLU A C 1 ATOM 3549 O O . GLU A 1 448 ? 39.999 45.284 68.962 1.00 48.61 ? 489 GLU A O 1 ATOM 3550 C CB . GLU A 1 448 ? 39.412 42.233 67.993 1.00 46.73 ? 489 GLU A CB 1 ATOM 3551 C CG . GLU A 1 448 ? 40.784 41.850 67.501 1.00 52.55 ? 489 GLU A CG 1 ATOM 3552 C CD . GLU A 1 448 ? 40.926 41.756 65.991 1.00 50.92 ? 489 GLU A CD 1 ATOM 3553 O OE1 . GLU A 1 448 ? 40.432 40.800 65.337 1.00 50.88 ? 489 GLU A OE1 1 ATOM 3554 O OE2 . GLU A 1 448 ? 41.625 42.644 65.477 1.00 52.53 ? 489 GLU A OE2 1 ATOM 3555 N N . GLY A 1 449 ? 37.883 44.779 69.518 1.00 46.31 ? 490 GLY A N 1 ATOM 3556 C CA . GLY A 1 449 ? 37.829 45.762 70.607 1.00 46.55 ? 490 GLY A CA 1 ATOM 3557 C C . GLY A 1 449 ? 37.596 47.199 70.168 1.00 45.88 ? 490 GLY A C 1 ATOM 3558 O O . GLY A 1 449 ? 37.553 48.104 71.004 1.00 47.76 ? 490 GLY A O 1 ATOM 3559 N N . LYS A 1 450 ? 37.476 47.424 68.859 1.00 43.17 ? 491 LYS A N 1 ATOM 3560 C CA . LYS A 1 450 ? 37.222 48.742 68.315 1.00 42.35 ? 491 LYS A CA 1 ATOM 3561 C C . LYS A 1 450 ? 35.762 48.832 67.879 1.00 39.53 ? 491 LYS A C 1 ATOM 3562 O O . LYS A 1 450 ? 35.105 47.811 67.653 1.00 39.31 ? 491 LYS A O 1 ATOM 3563 C CB . LYS A 1 450 ? 38.129 49.042 67.119 1.00 42.33 ? 491 LYS A CB 1 ATOM 3564 C CG . LYS A 1 450 ? 39.631 48.985 67.422 1.00 46.07 ? 491 LYS A CG 1 ATOM 3565 C CD . LYS A 1 450 ? 40.011 50.059 68.451 1.00 50.07 ? 491 LYS A CD 1 ATOM 3566 C CE . LYS A 1 450 ? 41.520 50.056 68.759 1.00 54.98 ? 491 LYS A CE 1 ATOM 3567 N NZ . LYS A 1 450 ? 42.313 50.071 67.495 1.00 57.81 ? 491 LYS A NZ 1 ATOM 3568 N N . SER A 1 451 ? 35.270 50.054 67.775 1.00 38.93 ? 492 SER A N 1 ATOM 3569 C CA . SER A 1 451 ? 33.869 50.284 67.347 1.00 35.99 ? 492 SER A CA 1 ATOM 3570 C C . SER A 1 451 ? 33.682 50.042 65.847 1.00 34.95 ? 492 SER A C 1 ATOM 3571 O O . SER A 1 451 ? 34.614 50.153 65.058 1.00 34.39 ? 492 SER A O 1 ATOM 3572 C CB . SER A 1 451 ? 33.418 51.706 67.694 1.00 37.16 ? 492 SER A CB 1 ATOM 3573 O OG . SER A 1 451 ? 33.933 52.631 66.753 1.00 37.93 ? 492 SER A OG 1 ATOM 3574 N N . LEU A 1 452 ? 32.450 49.742 65.452 1.00 32.46 ? 493 LEU A N 1 ATOM 3575 C CA . LEU A 1 452 ? 32.102 49.645 64.036 1.00 31.75 ? 493 LEU A CA 1 ATOM 3576 C C . LEU A 1 452 ? 32.322 51.009 63.374 1.00 31.86 ? 493 LEU A C 1 ATOM 3577 O O . LEU A 1 452 ? 32.758 51.071 62.229 1.00 30.54 ? 493 LEU A O 1 ATOM 3578 C CB . LEU A 1 452 ? 30.633 49.217 63.893 1.00 30.13 ? 493 LEU A CB 1 ATOM 3579 C CG . LEU A 1 452 ? 29.990 49.100 62.504 1.00 30.46 ? 493 LEU A CG 1 ATOM 3580 C CD1 . LEU A 1 452 ? 30.853 48.131 61.606 1.00 30.28 ? 493 LEU A CD1 1 ATOM 3581 C CD2 . LEU A 1 452 ? 28.562 48.601 62.626 1.00 30.26 ? 493 LEU A CD2 1 ATOM 3582 N N . TYR A 1 453 ? 32.014 52.113 64.087 1.00 31.99 ? 494 TYR A N 1 ATOM 3583 C CA . TYR A 1 453 ? 32.280 53.429 63.518 1.00 33.40 ? 494 TYR A CA 1 ATOM 3584 C C . TYR A 1 453 ? 33.760 53.576 63.128 1.00 34.59 ? 494 TYR A C 1 ATOM 3585 O O . TYR A 1 453 ? 34.075 54.158 62.082 1.00 34.68 ? 494 TYR A O 1 ATOM 3586 C CB . TYR A 1 453 ? 31.898 54.549 64.492 1.00 34.04 ? 494 TYR A CB 1 ATOM 3587 C CG . TYR A 1 453 ? 32.101 55.943 63.937 1.00 32.77 ? 494 TYR A CG 1 ATOM 3588 C CD1 . TYR A 1 453 ? 31.084 56.596 63.258 1.00 33.40 ? 494 TYR A CD1 1 ATOM 3589 C CD2 . TYR A 1 453 ? 33.305 56.632 64.147 1.00 35.37 ? 494 TYR A CD2 1 ATOM 3590 C CE1 . TYR A 1 453 ? 31.255 57.895 62.747 1.00 34.68 ? 494 TYR A CE1 1 ATOM 3591 C CE2 . TYR A 1 453 ? 33.486 57.936 63.648 1.00 36.41 ? 494 TYR A CE2 1 ATOM 3592 C CZ . TYR A 1 453 ? 32.465 58.562 62.973 1.00 35.26 ? 494 TYR A CZ 1 ATOM 3593 O OH . TYR A 1 453 ? 32.632 59.829 62.475 1.00 37.16 ? 494 TYR A OH 1 ATOM 3594 N N . GLU A 1 454 ? 34.646 53.108 63.996 1.00 35.30 ? 495 GLU A N 1 ATOM 3595 C CA . GLU A 1 454 ? 36.094 53.236 63.743 1.00 37.39 ? 495 GLU A CA 1 ATOM 3596 C C . GLU A 1 454 ? 36.537 52.473 62.483 1.00 37.18 ? 495 GLU A C 1 ATOM 3597 O O . GLU A 1 454 ? 37.187 53.056 61.601 1.00 37.37 ? 495 GLU A O 1 ATOM 3598 C CB . GLU A 1 454 ? 36.949 52.805 64.944 1.00 39.27 ? 495 GLU A CB 1 ATOM 3599 C CG . GLU A 1 454 ? 38.417 53.062 64.673 1.00 43.57 ? 495 GLU A CG 1 ATOM 3600 C CD . GLU A 1 454 ? 39.292 52.873 65.892 1.00 48.14 ? 495 GLU A CD 1 ATOM 3601 O OE1 . GLU A 1 454 ? 38.854 53.259 67.001 1.00 49.36 ? 495 GLU A OE1 1 ATOM 3602 O OE2 . GLU A 1 454 ? 40.425 52.369 65.727 1.00 51.74 ? 495 GLU A OE2 1 ATOM 3603 N N . SER A 1 455 ? 36.113 51.212 62.366 1.00 36.26 ? 496 SER A N 1 ATOM 3604 C CA . SER A 1 455 ? 36.486 50.412 61.183 1.00 36.48 ? 496 SER A CA 1 ATOM 3605 C C . SER A 1 455 ? 35.861 50.925 59.896 1.00 35.95 ? 496 SER A C 1 ATOM 3606 O O . SER A 1 455 ? 36.522 51.026 58.857 1.00 36.85 ? 496 SER A O 1 ATOM 3607 C CB . SER A 1 455 ? 36.227 48.909 61.383 1.00 36.36 ? 496 SER A CB 1 ATOM 3608 O OG . SER A 1 455 ? 34.862 48.599 61.524 1.00 34.47 ? 496 SER A OG 1 ATOM 3609 N N . TRP A 1 456 ? 34.584 51.273 59.975 1.00 33.71 ? 497 TRP A N 1 ATOM 3610 C CA . TRP A 1 456 ? 33.879 51.814 58.833 1.00 33.52 ? 497 TRP A CA 1 ATOM 3611 C C . TRP A 1 456 ? 34.526 53.120 58.341 1.00 34.23 ? 497 TRP A C 1 ATOM 3612 O O . TRP A 1 456 ? 34.742 53.306 57.133 1.00 33.19 ? 497 TRP A O 1 ATOM 3613 C CB . TRP A 1 456 ? 32.406 51.993 59.221 1.00 31.14 ? 497 TRP A CB 1 ATOM 3614 C CG . TRP A 1 456 ? 31.501 52.631 58.208 1.00 31.62 ? 497 TRP A CG 1 ATOM 3615 C CD1 . TRP A 1 456 ? 31.573 52.543 56.846 1.00 30.23 ? 497 TRP A CD1 1 ATOM 3616 C CD2 . TRP A 1 456 ? 30.355 53.417 58.504 1.00 31.38 ? 497 TRP A CD2 1 ATOM 3617 N NE1 . TRP A 1 456 ? 30.544 53.259 56.277 1.00 29.91 ? 497 TRP A NE1 1 ATOM 3618 C CE2 . TRP A 1 456 ? 29.776 53.804 57.269 1.00 30.18 ? 497 TRP A CE2 1 ATOM 3619 C CE3 . TRP A 1 456 ? 29.758 53.857 59.704 1.00 29.58 ? 497 TRP A CE3 1 ATOM 3620 C CZ2 . TRP A 1 456 ? 28.634 54.613 57.194 1.00 29.91 ? 497 TRP A CZ2 1 ATOM 3621 C CZ3 . TRP A 1 456 ? 28.625 54.660 59.625 1.00 30.06 ? 497 TRP A CZ3 1 ATOM 3622 C CH2 . TRP A 1 456 ? 28.073 55.030 58.375 1.00 29.14 ? 497 TRP A CH2 1 ATOM 3623 N N . THR A 1 457 ? 34.829 54.031 59.270 1.00 35.17 ? 498 THR A N 1 ATOM 3624 C CA . THR A 1 457 ? 35.383 55.317 58.873 1.00 36.97 ? 498 THR A CA 1 ATOM 3625 C C . THR A 1 457 ? 36.790 55.160 58.279 1.00 38.69 ? 498 THR A C 1 ATOM 3626 O O . THR A 1 457 ? 37.142 55.851 57.310 1.00 39.26 ? 498 THR A O 1 ATOM 3627 C CB . THR A 1 457 ? 35.377 56.306 60.061 1.00 37.87 ? 498 THR A CB 1 ATOM 3628 O OG1 . THR A 1 457 ? 34.020 56.543 60.446 1.00 35.56 ? 498 THR A OG1 1 ATOM 3629 C CG2 . THR A 1 457 ? 35.992 57.665 59.661 1.00 40.41 ? 498 THR A CG2 1 ATOM 3630 N N . LYS A 1 458 ? 37.557 54.231 58.821 1.00 39.54 ? 499 LYS A N 1 ATOM 3631 C CA . LYS A 1 458 ? 38.884 53.970 58.290 1.00 41.75 ? 499 LYS A CA 1 ATOM 3632 C C . LYS A 1 458 ? 38.802 53.398 56.870 1.00 41.05 ? 499 LYS A C 1 ATOM 3633 O O . LYS A 1 458 ? 39.495 53.881 55.979 1.00 42.44 ? 499 LYS A O 1 ATOM 3634 C CB . LYS A 1 458 ? 39.686 53.076 59.221 1.00 42.80 ? 499 LYS A CB 1 ATOM 3635 C CG . LYS A 1 458 ? 41.192 53.199 58.992 1.00 47.65 ? 499 LYS A CG 1 ATOM 3636 C CD . LYS A 1 458 ? 41.919 51.910 59.305 1.00 53.88 ? 499 LYS A CD 1 ATOM 3637 C CE . LYS A 1 458 ? 43.451 52.111 59.325 1.00 57.51 ? 499 LYS A CE 1 ATOM 3638 N NZ . LYS A 1 458 ? 43.906 53.320 58.536 1.00 59.16 ? 499 LYS A NZ 1 ATOM 3639 N N . LYS A 1 459 ? 37.912 52.431 56.652 1.00 39.52 ? 500 LYS A N 1 ATOM 3640 C CA . LYS A 1 459 ? 37.804 51.722 55.357 1.00 38.74 ? 500 LYS A CA 1 ATOM 3641 C C . LYS A 1 459 ? 37.048 52.464 54.268 1.00 38.14 ? 500 LYS A C 1 ATOM 3642 O O . LYS A 1 459 ? 37.240 52.194 53.074 1.00 38.03 ? 500 LYS A O 1 ATOM 3643 C CB . LYS A 1 459 ? 37.173 50.351 55.564 1.00 37.92 ? 500 LYS A CB 1 ATOM 3644 C CG . LYS A 1 459 ? 38.127 49.359 56.264 1.00 39.19 ? 500 LYS A CG 1 ATOM 3645 C CD . LYS A 1 459 ? 37.487 47.975 56.396 1.00 37.24 ? 500 LYS A CD 1 ATOM 3646 C CE . LYS A 1 459 ? 38.454 46.964 56.946 1.00 37.83 ? 500 LYS A CE 1 ATOM 3647 N NZ . LYS A 1 459 ? 37.766 45.676 57.294 1.00 38.15 ? 500 LYS A NZ 1 ATOM 3648 N N . SER A 1 460 ? 36.164 53.371 54.676 1.00 37.24 ? 501 SER A N 1 ATOM 3649 C CA . SER A 1 460 ? 35.277 54.052 53.748 1.00 37.42 ? 501 SER A CA 1 ATOM 3650 C C . SER A 1 460 ? 35.141 55.531 54.132 1.00 38.31 ? 501 SER A C 1 ATOM 3651 O O . SER A 1 460 ? 34.091 55.979 54.604 1.00 36.38 ? 501 SER A O 1 ATOM 3652 C CB . SER A 1 460 ? 33.917 53.330 53.732 1.00 35.24 ? 501 SER A CB 1 ATOM 3653 O OG . SER A 1 460 ? 33.088 53.803 52.688 1.00 39.15 ? 501 SER A OG 1 ATOM 3654 N N . PRO A 1 461 ? 36.232 56.298 53.973 1.00 40.85 ? 502 PRO A N 1 ATOM 3655 C CA . PRO A 1 461 ? 36.202 57.709 54.380 1.00 42.51 ? 502 PRO A CA 1 ATOM 3656 C C . PRO A 1 461 ? 35.288 58.529 53.493 1.00 43.80 ? 502 PRO A C 1 ATOM 3657 O O . PRO A 1 461 ? 35.191 58.255 52.286 1.00 42.24 ? 502 PRO A O 1 ATOM 3658 C CB . PRO A 1 461 ? 37.672 58.154 54.232 1.00 43.19 ? 502 PRO A CB 1 ATOM 3659 C CG . PRO A 1 461 ? 38.304 57.126 53.304 1.00 44.21 ? 502 PRO A CG 1 ATOM 3660 C CD . PRO A 1 461 ? 37.573 55.850 53.539 1.00 41.27 ? 502 PRO A CD 1 ATOM 3661 N N . SER A 1 462 ? 34.578 59.505 54.076 1.00 46.29 ? 503 SER A N 1 ATOM 3662 C CA A SER A 1 462 ? 33.731 60.398 53.268 0.70 48.15 ? 503 SER A CA 1 ATOM 3663 C CA B SER A 1 462 ? 33.736 60.389 53.280 0.30 47.83 ? 503 SER A CA 1 ATOM 3664 C C . SER A 1 462 ? 34.648 61.318 52.488 1.00 50.14 ? 503 SER A C 1 ATOM 3665 O O . SER A 1 462 ? 35.693 61.719 52.994 1.00 52.03 ? 503 SER A O 1 ATOM 3666 C CB A SER A 1 462 ? 32.772 61.246 54.125 0.70 47.91 ? 503 SER A CB 1 ATOM 3667 C CB B SER A 1 462 ? 32.798 61.199 54.175 0.30 47.42 ? 503 SER A CB 1 ATOM 3668 O OG A SER A 1 462 ? 31.870 62.014 53.308 0.70 47.95 ? 503 SER A OG 1 ATOM 3669 O OG B SER A 1 462 ? 33.499 62.207 54.876 0.30 47.43 ? 503 SER A OG 1 ATOM 3670 N N . PRO A 1 463 ? 34.277 61.634 51.240 1.00 52.25 ? 504 PRO A N 1 ATOM 3671 C CA . PRO A 1 463 ? 35.120 62.579 50.494 1.00 55.77 ? 504 PRO A CA 1 ATOM 3672 C C . PRO A 1 463 ? 35.350 63.951 51.182 1.00 58.49 ? 504 PRO A C 1 ATOM 3673 O O . PRO A 1 463 ? 36.473 64.463 51.170 1.00 59.93 ? 504 PRO A O 1 ATOM 3674 C CB . PRO A 1 463 ? 34.343 62.755 49.191 1.00 54.90 ? 504 PRO A CB 1 ATOM 3675 C CG . PRO A 1 463 ? 33.743 61.439 48.979 1.00 54.35 ? 504 PRO A CG 1 ATOM 3676 C CD . PRO A 1 463 ? 33.310 60.974 50.355 1.00 51.27 ? 504 PRO A CD 1 ATOM 3677 N N . GLU A 1 464 ? 34.304 64.525 51.785 1.00 60.38 ? 505 GLU A N 1 ATOM 3678 C CA . GLU A 1 464 ? 34.372 65.914 52.313 1.00 62.49 ? 505 GLU A CA 1 ATOM 3679 C C . GLU A 1 464 ? 34.906 66.132 53.753 1.00 63.65 ? 505 GLU A C 1 ATOM 3680 O O . GLU A 1 464 ? 35.348 67.243 54.078 1.00 65.23 ? 505 GLU A O 1 ATOM 3681 C CB . GLU A 1 464 ? 33.035 66.676 52.109 1.00 61.93 ? 505 GLU A CB 1 ATOM 3682 C CG . GLU A 1 464 ? 31.780 65.834 52.234 1.00 62.94 ? 505 GLU A CG 1 ATOM 3683 C CD . GLU A 1 464 ? 31.360 65.144 50.933 1.00 64.44 ? 505 GLU A CD 1 ATOM 3684 O OE1 . GLU A 1 464 ? 30.228 64.608 50.875 1.00 62.47 ? 505 GLU A OE1 1 ATOM 3685 O OE2 . GLU A 1 464 ? 32.157 65.127 49.972 1.00 66.45 ? 505 GLU A OE2 1 ATOM 3686 N N . PHE A 1 465 ? 34.879 65.105 54.607 1.00 63.45 ? 506 PHE A N 1 ATOM 3687 C CA . PHE A 1 465 ? 35.100 65.343 56.034 1.00 63.80 ? 506 PHE A CA 1 ATOM 3688 C C . PHE A 1 465 ? 36.192 64.513 56.689 1.00 63.74 ? 506 PHE A C 1 ATOM 3689 O O . PHE A 1 465 ? 36.427 63.357 56.338 1.00 63.83 ? 506 PHE A O 1 ATOM 3690 C CB . PHE A 1 465 ? 33.794 65.154 56.811 1.00 63.75 ? 506 PHE A CB 1 ATOM 3691 C CG . PHE A 1 465 ? 32.626 65.960 56.284 1.00 64.31 ? 506 PHE A CG 1 ATOM 3692 C CD1 . PHE A 1 465 ? 31.572 65.322 55.624 1.00 63.37 ? 506 PHE A CD1 1 ATOM 3693 C CD2 . PHE A 1 465 ? 32.560 67.348 56.479 1.00 66.85 ? 506 PHE A CD2 1 ATOM 3694 C CE1 . PHE A 1 465 ? 30.469 66.051 55.146 1.00 64.24 ? 506 PHE A CE1 1 ATOM 3695 C CE2 . PHE A 1 465 ? 31.464 68.089 55.995 1.00 66.69 ? 506 PHE A CE2 1 ATOM 3696 C CZ . PHE A 1 465 ? 30.416 67.431 55.329 1.00 64.79 ? 506 PHE A CZ 1 ATOM 3697 N N . SER A 1 466 ? 36.853 65.098 57.672 1.00 64.02 ? 507 SER A N 1 ATOM 3698 C CA . SER A 1 466 ? 37.908 64.367 58.374 1.00 63.72 ? 507 SER A CA 1 ATOM 3699 C C . SER A 1 466 ? 37.296 63.500 59.469 1.00 61.86 ? 507 SER A C 1 ATOM 3700 O O . SER A 1 466 ? 36.443 63.966 60.233 1.00 61.93 ? 507 SER A O 1 ATOM 3701 C CB . SER A 1 466 ? 38.973 65.310 58.956 1.00 65.22 ? 507 SER A CB 1 ATOM 3702 O OG . SER A 1 466 ? 40.059 64.555 59.474 1.00 66.88 ? 507 SER A OG 1 ATOM 3703 N N . GLY A 1 467 ? 37.727 62.241 59.526 1.00 59.96 ? 508 GLY A N 1 ATOM 3704 C CA . GLY A 1 467 ? 37.259 61.305 60.551 1.00 56.82 ? 508 GLY A CA 1 ATOM 3705 C C . GLY A 1 467 ? 35.762 60.983 60.473 1.00 52.86 ? 508 GLY A C 1 ATOM 3706 O O . GLY A 1 467 ? 35.184 60.554 61.486 1.00 51.83 ? 508 GLY A O 1 ATOM 3707 N N . MET A 1 468 ? 35.164 61.207 59.294 1.00 50.75 ? 509 MET A N 1 ATOM 3708 C CA . MET A 1 468 ? 33.739 60.827 58.960 1.00 48.05 ? 509 MET A CA 1 ATOM 3709 C C . MET A 1 468 ? 33.587 59.723 57.883 1.00 45.82 ? 509 MET A C 1 ATOM 3710 O O . MET A 1 468 ? 34.299 59.731 56.866 1.00 46.24 ? 509 MET A O 1 ATOM 3711 C CB . MET A 1 468 ? 32.905 61.993 58.437 1.00 48.76 ? 509 MET A CB 1 ATOM 3712 C CG . MET A 1 468 ? 32.911 63.264 59.242 1.00 52.03 ? 509 MET A CG 1 ATOM 3713 S SD . MET A 1 468 ? 32.185 63.052 60.848 1.00 54.28 ? 509 MET A SD 1 ATOM 3714 C CE . MET A 1 468 ? 30.485 63.377 60.433 1.00 52.83 ? 509 MET A CE 1 ATOM 3715 N N . PRO A 1 469 ? 32.608 58.807 58.065 1.00 42.01 ? 510 PRO A N 1 ATOM 3716 C CA . PRO A 1 469 ? 32.414 57.758 57.058 1.00 39.81 ? 510 PRO A CA 1 ATOM 3717 C C . PRO A 1 469 ? 31.570 58.188 55.863 1.00 37.63 ? 510 PRO A C 1 ATOM 3718 O O . PRO A 1 469 ? 30.724 59.084 55.966 1.00 37.13 ? 510 PRO A O 1 ATOM 3719 C CB . PRO A 1 469 ? 31.673 56.665 57.842 1.00 39.00 ? 510 PRO A CB 1 ATOM 3720 C CG . PRO A 1 469 ? 30.856 57.417 58.851 1.00 38.59 ? 510 PRO A CG 1 ATOM 3721 C CD . PRO A 1 469 ? 31.745 58.604 59.242 1.00 41.60 ? 510 PRO A CD 1 ATOM 3722 N N . ARG A 1 470 ? 31.767 57.520 54.729 1.00 35.78 ? 511 ARG A N 1 ATOM 3723 C CA . ARG A 1 470 ? 30.914 57.725 53.568 1.00 33.79 ? 511 ARG A CA 1 ATOM 3724 C C . ARG A 1 470 ? 29.486 57.211 53.816 1.00 32.52 ? 511 ARG A C 1 ATOM 3725 O O . ARG A 1 470 ? 29.296 56.087 54.257 1.00 31.89 ? 511 ARG A O 1 ATOM 3726 C CB . ARG A 1 470 ? 31.507 56.980 52.357 1.00 34.70 ? 511 ARG A CB 1 ATOM 3727 C CG . ARG A 1 470 ? 30.738 57.152 51.053 1.00 36.32 ? 511 ARG A CG 1 ATOM 3728 C CD . ARG A 1 470 ? 31.329 56.193 50.024 1.00 43.67 ? 511 ARG A CD 1 ATOM 3729 N NE . ARG A 1 470 ? 32.666 56.640 49.642 1.00 49.62 ? 511 ARG A NE 1 ATOM 3730 C CZ . ARG A 1 470 ? 32.915 57.483 48.633 1.00 55.46 ? 511 ARG A CZ 1 ATOM 3731 N NH1 . ARG A 1 470 ? 31.903 57.955 47.904 1.00 55.09 ? 511 ARG A NH1 1 ATOM 3732 N NH2 . ARG A 1 470 ? 34.174 57.856 48.344 1.00 54.75 ? 511 ARG A NH2 1 ATOM 3733 N N . ILE A 1 471 ? 28.503 58.060 53.550 1.00 30.35 ? 512 ILE A N 1 ATOM 3734 C CA . ILE A 1 471 ? 27.086 57.649 53.415 1.00 29.22 ? 512 ILE A CA 1 ATOM 3735 C C . ILE A 1 471 ? 26.527 58.056 52.042 1.00 29.17 ? 512 ILE A C 1 ATOM 3736 O O . ILE A 1 471 ? 26.607 59.250 51.693 1.00 30.70 ? 512 ILE A O 1 ATOM 3737 C CB . ILE A 1 471 ? 26.198 58.257 54.599 1.00 28.46 ? 512 ILE A CB 1 ATOM 3738 C CG1 . ILE A 1 471 ? 26.698 57.726 55.942 1.00 31.92 ? 512 ILE A CG1 1 ATOM 3739 C CG2 . ILE A 1 471 ? 24.690 57.960 54.336 1.00 28.91 ? 512 ILE A CG2 1 ATOM 3740 C CD1 . ILE A 1 471 ? 26.005 58.354 57.193 1.00 32.23 ? 512 ILE A CD1 1 ATOM 3741 N N . SER A 1 472 ? 25.930 57.131 51.272 1.00 28.81 ? 513 SER A N 1 ATOM 3742 C CA . SER A 1 472 ? 25.465 57.446 49.922 1.00 29.52 ? 513 SER A CA 1 ATOM 3743 C C . SER A 1 472 ? 24.024 57.936 49.931 1.00 28.27 ? 513 SER A C 1 ATOM 3744 O O . SER A 1 472 ? 23.313 57.795 50.937 1.00 27.64 ? 513 SER A O 1 ATOM 3745 C CB . SER A 1 472 ? 25.593 56.241 48.959 1.00 29.72 ? 513 SER A CB 1 ATOM 3746 O OG . SER A 1 472 ? 26.974 55.932 48.796 1.00 33.32 ? 513 SER A OG 1 ATOM 3747 N N . LYS A 1 473 ? 23.613 58.445 48.783 1.00 28.45 ? 514 LYS A N 1 ATOM 3748 C CA . LYS A 1 473 ? 22.247 58.913 48.538 1.00 28.02 ? 514 LYS A CA 1 ATOM 3749 C C . LYS A 1 473 ? 21.347 57.745 48.166 1.00 28.98 ? 514 LYS A C 1 ATOM 3750 O O . LYS A 1 473 ? 21.828 56.732 47.587 1.00 30.29 ? 514 LYS A O 1 ATOM 3751 C CB . LYS A 1 473 ? 22.297 59.861 47.346 1.00 28.28 ? 514 LYS A CB 1 ATOM 3752 C CG . LYS A 1 473 ? 23.259 61.037 47.562 1.00 30.08 ? 514 LYS A CG 1 ATOM 3753 C CD . LYS A 1 473 ? 23.043 62.094 46.520 1.00 32.58 ? 514 LYS A CD 1 ATOM 3754 C CE . LYS A 1 473 ? 23.706 61.758 45.205 1.00 37.97 ? 514 LYS A CE 1 ATOM 3755 N NZ . LYS A 1 473 ? 25.151 62.123 45.310 1.00 39.55 ? 514 LYS A NZ 1 ATOM 3756 N N . LEU A 1 474 ? 20.034 57.903 48.367 1.00 28.05 ? 515 LEU A N 1 ATOM 3757 C CA . LEU A 1 474 ? 19.063 56.906 47.899 1.00 26.85 ? 515 LEU A CA 1 ATOM 3758 C C . LEU A 1 474 ? 18.516 57.211 46.502 1.00 27.02 ? 515 LEU A C 1 ATOM 3759 O O . LEU A 1 474 ? 18.042 58.323 46.228 1.00 27.45 ? 515 LEU A O 1 ATOM 3760 C CB . LEU A 1 474 ? 17.872 56.866 48.874 1.00 25.51 ? 515 LEU A CB 1 ATOM 3761 C CG . LEU A 1 474 ? 18.145 56.328 50.285 1.00 25.94 ? 515 LEU A CG 1 ATOM 3762 C CD1 . LEU A 1 474 ? 16.909 56.664 51.184 1.00 26.49 ? 515 LEU A CD1 1 ATOM 3763 C CD2 . LEU A 1 474 ? 18.413 54.805 50.330 1.00 25.29 ? 515 LEU A CD2 1 ATOM 3764 N N . GLY A 1 475 ? 18.551 56.201 45.629 1.00 27.26 ? 516 GLY A N 1 ATOM 3765 C CA . GLY A 1 475 ? 17.892 56.279 44.331 1.00 26.51 ? 516 GLY A CA 1 ATOM 3766 C C . GLY A 1 475 ? 16.741 55.295 44.276 1.00 25.74 ? 516 GLY A C 1 ATOM 3767 O O . GLY A 1 475 ? 15.755 55.471 44.963 1.00 25.62 ? 516 GLY A O 1 ATOM 3768 N N . SER A 1 476 ? 16.857 54.247 43.441 1.00 24.42 ? 517 SER A N 1 ATOM 3769 C CA . SER A 1 476 ? 15.855 53.195 43.408 1.00 24.92 ? 517 SER A CA 1 ATOM 3770 C C . SER A 1 476 ? 16.575 51.859 43.420 1.00 24.13 ? 517 SER A C 1 ATOM 3771 O O . SER A 1 476 ? 17.762 51.756 43.854 1.00 24.56 ? 517 SER A O 1 ATOM 3772 C CB . SER A 1 476 ? 15.002 53.292 42.136 1.00 27.35 ? 517 SER A CB 1 ATOM 3773 O OG . SER A 1 476 ? 13.889 52.355 42.240 1.00 30.18 ? 517 SER A OG 1 ATOM 3774 N N . GLY A 1 477 ? 15.898 50.834 42.915 1.00 22.24 ? 518 GLY A N 1 ATOM 3775 C CA . GLY A 1 477 ? 16.503 49.526 42.835 1.00 23.59 ? 518 GLY A CA 1 ATOM 3776 C C . GLY A 1 477 ? 16.108 48.687 44.046 1.00 21.71 ? 518 GLY A C 1 ATOM 3777 O O . GLY A 1 477 ? 16.508 47.524 44.120 1.00 24.36 ? 518 GLY A O 1 ATOM 3778 N N . ASN A 1 478 ? 15.422 49.284 45.047 1.00 19.76 ? 519 ASN A N 1 ATOM 3779 C CA . ASN A 1 478 ? 15.021 48.485 46.190 1.00 18.49 ? 519 ASN A CA 1 ATOM 3780 C C . ASN A 1 478 ? 13.787 49.060 46.858 1.00 17.83 ? 519 ASN A C 1 ATOM 3781 O O . ASN A 1 478 ? 13.307 50.134 46.449 1.00 17.38 ? 519 ASN A O 1 ATOM 3782 C CB . ASN A 1 478 ? 16.202 48.282 47.177 1.00 19.24 ? 519 ASN A CB 1 ATOM 3783 C CG . ASN A 1 478 ? 16.290 46.861 47.645 1.00 21.84 ? 519 ASN A CG 1 ATOM 3784 O OD1 . ASN A 1 478 ? 15.352 46.325 48.277 1.00 22.07 ? 519 ASN A OD1 1 ATOM 3785 N ND2 . ASN A 1 478 ? 17.374 46.190 47.208 1.00 21.15 ? 519 ASN A ND2 1 ATOM 3786 N N . ASP A 1 479 ? 13.253 48.333 47.857 1.00 17.20 ? 520 ASP A N 1 ATOM 3787 C CA . ASP A 1 479 ? 11.861 48.565 48.291 1.00 17.66 ? 520 ASP A CA 1 ATOM 3788 C C . ASP A 1 479 ? 11.653 49.846 49.108 1.00 17.59 ? 520 ASP A C 1 ATOM 3789 O O . ASP A 1 479 ? 10.538 50.187 49.377 1.00 18.98 ? 520 ASP A O 1 ATOM 3790 C CB . ASP A 1 479 ? 11.321 47.350 49.064 1.00 17.52 ? 520 ASP A CB 1 ATOM 3791 C CG . ASP A 1 479 ? 11.031 46.168 48.137 1.00 19.79 ? 520 ASP A CG 1 ATOM 3792 O OD1 . ASP A 1 479 ? 10.195 46.343 47.232 1.00 19.52 ? 520 ASP A OD1 1 ATOM 3793 O OD2 . ASP A 1 479 ? 11.683 45.108 48.304 1.00 21.42 ? 520 ASP A OD2 1 ATOM 3794 N N . PHE A 1 480 ? 12.715 50.575 49.420 1.00 19.24 ? 521 PHE A N 1 ATOM 3795 C CA . PHE A 1 480 ? 12.547 51.919 49.992 1.00 18.71 ? 521 PHE A CA 1 ATOM 3796 C C . PHE A 1 480 ? 12.034 52.935 48.967 1.00 19.44 ? 521 PHE A C 1 ATOM 3797 O O . PHE A 1 480 ? 11.638 54.027 49.368 1.00 19.60 ? 521 PHE A O 1 ATOM 3798 C CB . PHE A 1 480 ? 13.907 52.446 50.554 1.00 20.15 ? 521 PHE A CB 1 ATOM 3799 C CG . PHE A 1 480 ? 14.995 52.521 49.489 1.00 18.82 ? 521 PHE A CG 1 ATOM 3800 C CD1 . PHE A 1 480 ? 14.998 53.601 48.563 1.00 21.79 ? 521 PHE A CD1 1 ATOM 3801 C CD2 . PHE A 1 480 ? 15.939 51.498 49.367 1.00 22.08 ? 521 PHE A CD2 1 ATOM 3802 C CE1 . PHE A 1 480 ? 15.983 53.607 47.547 1.00 21.20 ? 521 PHE A CE1 1 ATOM 3803 C CE2 . PHE A 1 480 ? 16.955 51.542 48.363 1.00 24.15 ? 521 PHE A CE2 1 ATOM 3804 C CZ . PHE A 1 480 ? 16.917 52.600 47.440 1.00 23.13 ? 521 PHE A CZ 1 ATOM 3805 N N . GLU A 1 481 ? 12.039 52.591 47.669 1.00 17.85 ? 522 GLU A N 1 ATOM 3806 C CA . GLU A 1 481 ? 11.768 53.584 46.634 1.00 18.17 ? 522 GLU A CA 1 ATOM 3807 C C . GLU A 1 481 ? 10.406 54.282 46.847 1.00 17.74 ? 522 GLU A C 1 ATOM 3808 O O . GLU A 1 481 ? 10.327 55.528 46.847 1.00 18.32 ? 522 GLU A O 1 ATOM 3809 C CB . GLU A 1 481 ? 11.791 52.924 45.243 1.00 19.74 ? 522 GLU A CB 1 ATOM 3810 C CG . GLU A 1 481 ? 11.647 53.975 44.072 1.00 22.49 ? 522 GLU A CG 1 ATOM 3811 C CD . GLU A 1 481 ? 11.205 53.294 42.711 1.00 30.08 ? 522 GLU A CD 1 ATOM 3812 O OE1 . GLU A 1 481 ? 10.152 52.608 42.631 1.00 34.34 ? 522 GLU A OE1 1 ATOM 3813 O OE2 . GLU A 1 481 ? 11.869 53.419 41.715 1.00 32.40 ? 522 GLU A OE2 1 ATOM 3814 N N . VAL A 1 482 ? 9.315 53.512 47.037 1.00 17.18 ? 523 VAL A N 1 ATOM 3815 C CA . VAL A 1 482 ? 8.025 54.195 47.139 1.00 17.29 ? 523 VAL A CA 1 ATOM 3816 C C . VAL A 1 482 ? 7.933 55.037 48.408 1.00 17.74 ? 523 VAL A C 1 ATOM 3817 O O . VAL A 1 482 ? 7.379 56.125 48.389 1.00 17.71 ? 523 VAL A O 1 ATOM 3818 C CB . VAL A 1 482 ? 6.836 53.181 47.060 1.00 18.37 ? 523 VAL A CB 1 ATOM 3819 C CG1 . VAL A 1 482 ? 6.819 52.211 48.309 1.00 18.00 ? 523 VAL A CG1 1 ATOM 3820 C CG2 . VAL A 1 482 ? 5.502 53.906 46.845 1.00 19.74 ? 523 VAL A CG2 1 ATOM 3821 N N . PHE A 1 483 ? 8.512 54.522 49.487 1.00 16.56 ? 524 PHE A N 1 ATOM 3822 C CA . PHE A 1 483 ? 8.422 55.283 50.739 1.00 16.75 ? 524 PHE A CA 1 ATOM 3823 C C . PHE A 1 483 ? 9.167 56.595 50.687 1.00 17.48 ? 524 PHE A C 1 ATOM 3824 O O . PHE A 1 483 ? 8.650 57.614 51.204 1.00 18.27 ? 524 PHE A O 1 ATOM 3825 C CB . PHE A 1 483 ? 8.971 54.394 51.875 1.00 17.22 ? 524 PHE A CB 1 ATOM 3826 C CG . PHE A 1 483 ? 8.154 53.140 52.017 1.00 19.08 ? 524 PHE A CG 1 ATOM 3827 C CD1 . PHE A 1 483 ? 6.907 53.174 52.615 1.00 22.37 ? 524 PHE A CD1 1 ATOM 3828 C CD2 . PHE A 1 483 ? 8.623 51.939 51.477 1.00 19.73 ? 524 PHE A CD2 1 ATOM 3829 C CE1 . PHE A 1 483 ? 6.112 51.988 52.671 1.00 23.74 ? 524 PHE A CE1 1 ATOM 3830 C CE2 . PHE A 1 483 ? 7.860 50.760 51.516 1.00 19.39 ? 524 PHE A CE2 1 ATOM 3831 C CZ . PHE A 1 483 ? 6.621 50.770 52.136 1.00 22.01 ? 524 PHE A CZ 1 ATOM 3832 N N . PHE A 1 484 ? 10.354 56.578 50.095 1.00 17.99 ? 525 PHE A N 1 ATOM 3833 C CA . PHE A 1 484 ? 11.223 57.767 50.063 1.00 17.42 ? 525 PHE A CA 1 ATOM 3834 C C . PHE A 1 484 ? 10.922 58.686 48.879 1.00 17.67 ? 525 PHE A C 1 ATOM 3835 O O . PHE A 1 484 ? 10.639 59.898 49.068 1.00 18.24 ? 525 PHE A O 1 ATOM 3836 C CB . PHE A 1 484 ? 12.685 57.315 49.996 1.00 17.67 ? 525 PHE A CB 1 ATOM 3837 C CG . PHE A 1 484 ? 13.652 58.431 50.257 1.00 18.03 ? 525 PHE A CG 1 ATOM 3838 C CD1 . PHE A 1 484 ? 13.593 59.115 51.468 1.00 17.35 ? 525 PHE A CD1 1 ATOM 3839 C CD2 . PHE A 1 484 ? 14.527 58.843 49.276 1.00 20.76 ? 525 PHE A CD2 1 ATOM 3840 C CE1 . PHE A 1 484 ? 14.494 60.171 51.736 1.00 21.07 ? 525 PHE A CE1 1 ATOM 3841 C CE2 . PHE A 1 484 ? 15.467 59.885 49.542 1.00 20.95 ? 525 PHE A CE2 1 ATOM 3842 C CZ . PHE A 1 484 ? 15.411 60.552 50.784 1.00 21.80 ? 525 PHE A CZ 1 ATOM 3843 N N . GLN A 1 485 ? 10.943 58.123 47.674 1.00 17.06 ? 526 GLN A N 1 ATOM 3844 C CA . GLN A 1 485 ? 10.839 58.956 46.469 1.00 17.73 ? 526 GLN A CA 1 ATOM 3845 C C . GLN A 1 485 ? 9.383 59.392 46.163 1.00 17.25 ? 526 GLN A C 1 ATOM 3846 O O . GLN A 1 485 ? 9.184 60.489 45.608 1.00 18.74 ? 526 GLN A O 1 ATOM 3847 C CB . GLN A 1 485 ? 11.389 58.211 45.198 1.00 19.01 ? 526 GLN A CB 1 ATOM 3848 C CG . GLN A 1 485 ? 12.794 57.611 45.334 1.00 20.69 ? 526 GLN A CG 1 ATOM 3849 C CD . GLN A 1 485 ? 13.862 58.660 45.470 1.00 20.08 ? 526 GLN A CD 1 ATOM 3850 O OE1 . GLN A 1 485 ? 13.557 59.868 45.394 1.00 22.01 ? 526 GLN A OE1 1 ATOM 3851 N NE2 . GLN A 1 485 ? 15.112 58.233 45.643 1.00 21.01 ? 526 GLN A NE2 1 ATOM 3852 N N . ARG A 1 486 ? 8.383 58.545 46.506 1.00 16.63 ? 527 ARG A N 1 ATOM 3853 C CA . ARG A 1 486 ? 6.996 58.955 46.256 1.00 16.73 ? 527 ARG A CA 1 ATOM 3854 C C . ARG A 1 486 ? 6.399 59.618 47.448 1.00 17.43 ? 527 ARG A C 1 ATOM 3855 O O . ARG A 1 486 ? 5.773 60.685 47.298 1.00 17.48 ? 527 ARG A O 1 ATOM 3856 C CB . ARG A 1 486 ? 6.095 57.772 45.823 1.00 17.13 ? 527 ARG A CB 1 ATOM 3857 C CG . ARG A 1 486 ? 4.806 58.284 45.167 1.00 16.01 ? 527 ARG A CG 1 ATOM 3858 C CD . ARG A 1 486 ? 3.706 57.212 45.004 1.00 17.96 ? 527 ARG A CD 1 ATOM 3859 N NE . ARG A 1 486 ? 4.098 56.144 44.058 1.00 16.72 ? 527 ARG A NE 1 ATOM 3860 C CZ . ARG A 1 486 ? 3.196 55.328 43.499 1.00 17.18 ? 527 ARG A CZ 1 ATOM 3861 N NH1 . ARG A 1 486 ? 1.893 55.498 43.739 1.00 18.33 ? 527 ARG A NH1 1 ATOM 3862 N NH2 . ARG A 1 486 ? 3.588 54.345 42.687 1.00 17.51 ? 527 ARG A NH2 1 ATOM 3863 N N . LEU A 1 487 ? 6.528 58.990 48.636 1.00 16.87 ? 528 LEU A N 1 ATOM 3864 C CA . LEU A 1 487 ? 5.813 59.496 49.774 1.00 17.26 ? 528 LEU A CA 1 ATOM 3865 C C . LEU A 1 487 ? 6.614 60.452 50.678 1.00 17.41 ? 528 LEU A C 1 ATOM 3866 O O . LEU A 1 487 ? 5.985 61.125 51.520 1.00 19.17 ? 528 LEU A O 1 ATOM 3867 C CB . LEU A 1 487 ? 5.312 58.320 50.631 1.00 15.71 ? 528 LEU A CB 1 ATOM 3868 C CG . LEU A 1 487 ? 4.362 57.365 49.860 1.00 17.39 ? 528 LEU A CG 1 ATOM 3869 C CD1 . LEU A 1 487 ? 3.883 56.254 50.797 1.00 20.95 ? 528 LEU A CD1 1 ATOM 3870 C CD2 . LEU A 1 487 ? 3.104 58.134 49.319 1.00 21.10 ? 528 LEU A CD2 1 ATOM 3871 N N . GLY A 1 488 ? 7.940 60.462 50.590 1.00 16.98 ? 529 GLY A N 1 ATOM 3872 C CA . GLY A 1 488 ? 8.725 61.419 51.393 1.00 16.78 ? 529 GLY A CA 1 ATOM 3873 C C . GLY A 1 488 ? 8.827 60.996 52.868 1.00 16.87 ? 529 GLY A C 1 ATOM 3874 O O . GLY A 1 488 ? 8.808 61.856 53.750 1.00 17.59 ? 529 GLY A O 1 ATOM 3875 N N . ILE A 1 489 ? 8.973 59.687 53.089 1.00 17.62 ? 530 ILE A N 1 ATOM 3876 C CA . ILE A 1 489 ? 9.196 59.160 54.478 1.00 16.44 ? 530 ILE A CA 1 ATOM 3877 C C . ILE A 1 489 ? 10.706 58.934 54.598 1.00 16.99 ? 530 ILE A C 1 ATOM 3878 O O . ILE A 1 489 ? 11.310 58.270 53.758 1.00 17.86 ? 530 ILE A O 1 ATOM 3879 C CB . ILE A 1 489 ? 8.398 57.865 54.655 1.00 16.87 ? 530 ILE A CB 1 ATOM 3880 C CG1 . ILE A 1 489 ? 6.906 58.185 54.636 1.00 18.07 ? 530 ILE A CG1 1 ATOM 3881 C CG2 . ILE A 1 489 ? 8.799 57.144 56.011 1.00 17.98 ? 530 ILE A CG2 1 ATOM 3882 C CD1 . ILE A 1 489 ? 6.067 56.894 54.411 1.00 19.43 ? 530 ILE A CD1 1 ATOM 3883 N N . ALA A 1 490 ? 11.324 59.487 55.659 1.00 17.48 ? 531 ALA A N 1 ATOM 3884 C CA . ALA A 1 490 ? 12.748 59.298 55.897 1.00 17.56 ? 531 ALA A CA 1 ATOM 3885 C C . ALA A 1 490 ? 13.108 57.818 55.822 1.00 18.95 ? 531 ALA A C 1 ATOM 3886 O O . ALA A 1 490 ? 12.485 56.979 56.483 1.00 18.47 ? 531 ALA A O 1 ATOM 3887 C CB . ALA A 1 490 ? 13.028 59.827 57.363 1.00 18.49 ? 531 ALA A CB 1 ATOM 3888 N N . SER A 1 491 ? 14.108 57.500 55.011 1.00 17.78 ? 532 SER A N 1 ATOM 3889 C CA . SER A 1 491 ? 14.447 56.096 54.771 1.00 18.56 ? 532 SER A CA 1 ATOM 3890 C C . SER A 1 491 ? 15.947 55.867 54.838 1.00 19.48 ? 532 SER A C 1 ATOM 3891 O O . SER A 1 491 ? 16.780 56.790 54.615 1.00 20.62 ? 532 SER A O 1 ATOM 3892 C CB . SER A 1 491 ? 13.959 55.692 53.347 1.00 17.79 ? 532 SER A CB 1 ATOM 3893 O OG . SER A 1 491 ? 12.534 55.755 53.241 1.00 18.95 ? 532 SER A OG 1 ATOM 3894 N N . GLY A 1 492 ? 16.300 54.609 55.101 1.00 19.65 ? 533 GLY A N 1 ATOM 3895 C CA . GLY A 1 492 ? 17.711 54.206 55.177 1.00 20.12 ? 533 GLY A CA 1 ATOM 3896 C C . GLY A 1 492 ? 17.911 52.736 54.857 1.00 19.75 ? 533 GLY A C 1 ATOM 3897 O O . GLY A 1 492 ? 16.981 51.932 54.925 1.00 20.22 ? 533 GLY A O 1 ATOM 3898 N N . ARG A 1 493 ? 19.154 52.403 54.573 1.00 20.50 ? 534 ARG A N 1 ATOM 3899 C CA . ARG A 1 493 ? 19.566 51.007 54.353 1.00 21.70 ? 534 ARG A CA 1 ATOM 3900 C C . ARG A 1 493 ? 21.013 50.844 54.793 1.00 22.63 ? 534 ARG A C 1 ATOM 3901 O O . ARG A 1 493 ? 21.810 51.815 54.780 1.00 22.34 ? 534 ARG A O 1 ATOM 3902 C CB . ARG A 1 493 ? 19.390 50.619 52.881 1.00 21.26 ? 534 ARG A CB 1 ATOM 3903 C CG . ARG A 1 493 ? 20.352 51.331 51.970 1.00 24.55 ? 534 ARG A CG 1 ATOM 3904 C CD . ARG A 1 493 ? 20.048 51.108 50.472 1.00 27.85 ? 534 ARG A CD 1 ATOM 3905 N NE . ARG A 1 493 ? 20.004 49.677 50.133 1.00 30.70 ? 534 ARG A NE 1 ATOM 3906 C CZ . ARG A 1 493 ? 20.061 49.218 48.887 1.00 30.37 ? 534 ARG A CZ 1 ATOM 3907 N NH1 . ARG A 1 493 ? 19.929 47.922 48.673 1.00 26.38 ? 534 ARG A NH1 1 ATOM 3908 N NH2 . ARG A 1 493 ? 20.196 50.073 47.861 1.00 31.11 ? 534 ARG A NH2 1 ATOM 3909 N N . ALA A 1 494 ? 21.349 49.617 55.200 1.00 21.78 ? 535 ALA A N 1 ATOM 3910 C CA . ALA A 1 494 ? 22.734 49.319 55.596 1.00 22.53 ? 535 ALA A CA 1 ATOM 3911 C C . ALA A 1 494 ? 23.054 47.875 55.263 1.00 23.34 ? 535 ALA A C 1 ATOM 3912 O O . ALA A 1 494 ? 22.200 47.001 55.407 1.00 23.24 ? 535 ALA A O 1 ATOM 3913 C CB . ALA A 1 494 ? 22.904 49.565 57.122 1.00 23.11 ? 535 ALA A CB 1 ATOM 3914 N N . ARG A 1 495 ? 24.279 47.614 54.825 1.00 22.99 ? 536 ARG A N 1 ATOM 3915 C CA . ARG A 1 495 ? 24.691 46.222 54.539 1.00 22.84 ? 536 ARG A CA 1 ATOM 3916 C C . ARG A 1 495 ? 26.197 46.178 54.588 1.00 24.00 ? 536 ARG A C 1 ATOM 3917 O O . ARG A 1 495 ? 26.861 47.223 54.538 1.00 24.72 ? 536 ARG A O 1 ATOM 3918 C CB . ARG A 1 495 ? 24.208 45.730 53.144 1.00 23.98 ? 536 ARG A CB 1 ATOM 3919 C CG . ARG A 1 495 ? 24.672 46.602 51.964 1.00 24.57 ? 536 ARG A CG 1 ATOM 3920 C CD . ARG A 1 495 ? 24.433 45.861 50.641 1.00 29.00 ? 536 ARG A CD 1 ATOM 3921 N NE . ARG A 1 495 ? 23.014 45.453 50.532 1.00 29.43 ? 536 ARG A NE 1 ATOM 3922 C CZ . ARG A 1 495 ? 22.303 45.408 49.400 1.00 30.20 ? 536 ARG A CZ 1 ATOM 3923 N NH1 . ARG A 1 495 ? 21.039 45.022 49.453 1.00 29.37 ? 536 ARG A NH1 1 ATOM 3924 N NH2 . ARG A 1 495 ? 22.838 45.720 48.209 1.00 30.68 ? 536 ARG A NH2 1 ATOM 3925 N N . TYR A 1 496 ? 26.736 44.966 54.613 1.00 24.33 ? 537 TYR A N 1 ATOM 3926 C CA . TYR A 1 496 ? 28.186 44.828 54.477 1.00 25.62 ? 537 TYR A CA 1 ATOM 3927 C C . TYR A 1 496 ? 28.525 44.767 52.978 1.00 26.72 ? 537 TYR A C 1 ATOM 3928 O O . TYR A 1 496 ? 27.735 44.243 52.185 1.00 26.93 ? 537 TYR A O 1 ATOM 3929 C CB . TYR A 1 496 ? 28.798 43.631 55.275 1.00 26.10 ? 537 TYR A CB 1 ATOM 3930 C CG . TYR A 1 496 ? 29.743 44.123 56.358 1.00 27.44 ? 537 TYR A CG 1 ATOM 3931 C CD1 . TYR A 1 496 ? 29.245 44.825 57.440 1.00 26.49 ? 537 TYR A CD1 1 ATOM 3932 C CD2 . TYR A 1 496 ? 31.129 43.916 56.284 1.00 26.91 ? 537 TYR A CD2 1 ATOM 3933 C CE1 . TYR A 1 496 ? 30.090 45.318 58.450 1.00 28.81 ? 537 TYR A CE1 1 ATOM 3934 C CE2 . TYR A 1 496 ? 31.984 44.412 57.300 1.00 28.85 ? 537 TYR A CE2 1 ATOM 3935 C CZ . TYR A 1 496 ? 31.444 45.115 58.351 1.00 30.29 ? 537 TYR A CZ 1 ATOM 3936 O OH . TYR A 1 496 ? 32.262 45.623 59.342 1.00 31.33 ? 537 TYR A OH 1 ATOM 3937 N N . THR A 1 497 ? 29.649 45.380 52.615 1.00 27.50 ? 538 THR A N 1 ATOM 3938 C CA . THR A 1 497 ? 29.991 45.530 51.190 1.00 28.43 ? 538 THR A CA 1 ATOM 3939 C C . THR A 1 497 ? 31.459 45.168 50.893 1.00 30.70 ? 538 THR A C 1 ATOM 3940 O O . THR A 1 497 ? 32.245 44.946 51.814 1.00 29.37 ? 538 THR A O 1 ATOM 3941 C CB . THR A 1 497 ? 29.680 46.977 50.704 1.00 28.75 ? 538 THR A CB 1 ATOM 3942 O OG1 . THR A 1 497 ? 29.741 47.014 49.274 1.00 30.99 ? 538 THR A OG1 1 ATOM 3943 C CG2 . THR A 1 497 ? 30.667 47.985 51.287 1.00 29.21 ? 538 THR A CG2 1 ATOM 3944 N N . LYS A 1 498 ? 31.785 45.138 49.598 1.00 32.11 ? 539 LYS A N 1 ATOM 3945 C CA . LYS A 1 498 ? 33.144 44.902 49.087 1.00 36.44 ? 539 LYS A CA 1 ATOM 3946 C C . LYS A 1 498 ? 34.014 46.164 49.104 1.00 38.74 ? 539 LYS A C 1 ATOM 3947 O O . LYS A 1 498 ? 33.581 47.221 49.548 1.00 37.96 ? 539 LYS A O 1 ATOM 3948 C CB . LYS A 1 498 ? 33.037 44.387 47.639 1.00 36.07 ? 539 LYS A CB 1 ATOM 3949 C CG . LYS A 1 498 ? 32.285 45.333 46.665 1.00 40.00 ? 539 LYS A CG 1 ATOM 3950 C CD . LYS A 1 498 ? 31.751 44.600 45.416 1.00 45.91 ? 539 LYS A CD 1 ATOM 3951 C CE . LYS A 1 498 ? 31.252 45.572 44.332 1.00 46.41 ? 539 LYS A CE 1 ATOM 3952 N NZ . LYS A 1 498 ? 30.257 44.906 43.404 1.00 46.96 ? 539 LYS A NZ 1 ATOM 3953 N N . ASN A 1 499 ? 35.241 46.046 48.601 1.00 42.55 ? 540 ASN A N 1 ATOM 3954 C CA . ASN A 1 499 ? 36.100 47.222 48.369 1.00 46.53 ? 540 ASN A CA 1 ATOM 3955 C C . ASN A 1 499 ? 35.852 47.880 46.968 1.00 49.28 ? 540 ASN A C 1 ATOM 3956 O O . ASN A 1 499 ? 35.768 49.113 46.857 1.00 50.39 ? 540 ASN A O 1 ATOM 3957 C CB . ASN A 1 499 ? 37.558 46.831 48.615 1.00 47.52 ? 540 ASN A CB 1 ATOM 3958 C CG . ASN A 1 499 ? 38.490 48.034 48.826 1.00 48.04 ? 540 ASN A CG 1 ATOM 3959 O OD1 . ASN A 1 499 ? 38.173 49.172 48.490 1.00 46.57 ? 540 ASN A OD1 1 ATOM 3960 N ND2 . ASN A 1 499 ? 39.665 47.759 49.379 1.00 50.01 ? 540 ASN A ND2 1 ATOM 3961 N N . TRP A 1 500 ? 35.634 47.044 45.944 1.00 51.56 ? 541 TRP A N 1 ATOM 3962 C CA . TRP A 1 500 ? 35.582 47.363 44.481 1.00 53.32 ? 541 TRP A CA 1 ATOM 3963 C C . TRP A 1 500 ? 34.722 48.572 43.951 1.00 53.80 ? 541 TRP A C 1 ATOM 3964 O O . TRP A 1 500 ? 33.626 48.365 43.387 1.00 52.50 ? 541 TRP A O 1 ATOM 3965 C CB . TRP A 1 500 ? 35.111 46.077 43.775 1.00 53.54 ? 541 TRP A CB 1 ATOM 3966 C CG . TRP A 1 500 ? 35.639 45.820 42.401 1.00 56.56 ? 541 TRP A CG 1 ATOM 3967 C CD1 . TRP A 1 500 ? 36.293 46.705 41.571 1.00 58.38 ? 541 TRP A CD1 1 ATOM 3968 C CD2 . TRP A 1 500 ? 35.533 44.581 41.667 1.00 58.44 ? 541 TRP A CD2 1 ATOM 3969 N NE1 . TRP A 1 500 ? 36.603 46.085 40.378 1.00 59.97 ? 541 TRP A NE1 1 ATOM 3970 C CE2 . TRP A 1 500 ? 36.148 44.787 40.407 1.00 59.58 ? 541 TRP A CE2 1 ATOM 3971 C CE3 . TRP A 1 500 ? 34.973 43.317 41.955 1.00 58.81 ? 541 TRP A CE3 1 ATOM 3972 C CZ2 . TRP A 1 500 ? 36.239 43.764 39.433 1.00 60.07 ? 541 TRP A CZ2 1 ATOM 3973 C CZ3 . TRP A 1 500 ? 35.051 42.305 40.982 1.00 58.59 ? 541 TRP A CZ3 1 ATOM 3974 C CH2 . TRP A 1 500 ? 35.681 42.540 39.739 1.00 59.33 ? 541 TRP A CH2 1 ATOM 3975 N N . GLU A 1 501 ? 35.245 49.801 44.069 1.00 54.80 ? 542 GLU A N 1 ATOM 3976 C CA . GLU A 1 501 ? 34.484 51.041 43.747 1.00 55.10 ? 542 GLU A CA 1 ATOM 3977 C C . GLU A 1 501 ? 33.846 51.136 42.341 1.00 55.17 ? 542 GLU A C 1 ATOM 3978 O O . GLU A 1 501 ? 32.684 51.555 42.216 1.00 55.07 ? 542 GLU A O 1 ATOM 3979 C CB . GLU A 1 501 ? 35.336 52.296 44.018 1.00 56.01 ? 542 GLU A CB 1 ATOM 3980 N N . THR A 1 502 ? 34.591 50.764 41.292 1.00 55.69 ? 543 THR A N 1 ATOM 3981 C CA . THR A 1 502 ? 34.056 50.811 39.906 1.00 55.39 ? 543 THR A CA 1 ATOM 3982 C C . THR A 1 502 ? 32.997 49.720 39.632 1.00 54.05 ? 543 THR A C 1 ATOM 3983 O O . THR A 1 502 ? 32.278 49.764 38.612 1.00 53.46 ? 543 THR A O 1 ATOM 3984 C CB . THR A 1 502 ? 35.177 50.781 38.811 1.00 56.49 ? 543 THR A CB 1 ATOM 3985 O OG1 . THR A 1 502 ? 35.988 49.604 38.972 1.00 58.35 ? 543 THR A OG1 1 ATOM 3986 C CG2 . THR A 1 502 ? 36.052 52.052 38.881 1.00 57.51 ? 543 THR A CG2 1 ATOM 3987 N N . ASN A 1 503 ? 32.910 48.749 40.543 1.00 52.83 ? 544 ASN A N 1 ATOM 3988 C CA . ASN A 1 503 ? 31.859 47.727 40.486 1.00 51.25 ? 544 ASN A CA 1 ATOM 3989 C C . ASN A 1 503 ? 30.650 48.022 41.382 1.00 49.54 ? 544 ASN A C 1 ATOM 3990 O O . ASN A 1 503 ? 29.782 47.160 41.543 1.00 48.64 ? 544 ASN A O 1 ATOM 3991 C CB . ASN A 1 503 ? 32.428 46.338 40.824 1.00 51.62 ? 544 ASN A CB 1 ATOM 3992 C CG . ASN A 1 503 ? 32.648 45.484 39.587 1.00 53.48 ? 544 ASN A CG 1 ATOM 3993 O OD1 . ASN A 1 503 ? 33.066 45.981 38.538 1.00 56.87 ? 544 ASN A OD1 1 ATOM 3994 N ND2 . ASN A 1 503 ? 32.362 44.198 39.702 1.00 52.22 ? 544 ASN A ND2 1 ATOM 3995 N N . LYS A 1 504 ? 30.596 49.226 41.956 1.00 48.27 ? 545 LYS A N 1 ATOM 3996 C CA . LYS A 1 504 ? 29.572 49.552 42.962 1.00 46.91 ? 545 LYS A CA 1 ATOM 3997 C C . LYS A 1 504 ? 28.120 49.221 42.518 1.00 45.47 ? 545 LYS A C 1 ATOM 3998 O O . LYS A 1 504 ? 27.319 48.687 43.317 1.00 45.44 ? 545 LYS A O 1 ATOM 3999 C CB . LYS A 1 504 ? 29.666 51.020 43.412 1.00 47.55 ? 545 LYS A CB 1 ATOM 4000 C CG . LYS A 1 504 ? 28.598 51.375 44.440 1.00 48.93 ? 545 LYS A CG 1 ATOM 4001 C CD . LYS A 1 504 ? 28.632 52.822 44.892 1.00 52.96 ? 545 LYS A CD 1 ATOM 4002 C CE . LYS A 1 504 ? 27.415 53.103 45.792 1.00 54.04 ? 545 LYS A CE 1 ATOM 4003 N NZ . LYS A 1 504 ? 27.250 54.558 46.011 1.00 54.99 ? 545 LYS A NZ 1 ATOM 4004 N N . PHE A 1 505 ? 27.789 49.542 41.268 1.00 43.82 ? 546 PHE A N 1 ATOM 4005 C CA . PHE A 1 505 ? 26.422 49.318 40.734 1.00 42.58 ? 546 PHE A CA 1 ATOM 4006 C C . PHE A 1 505 ? 26.326 48.067 39.844 1.00 42.14 ? 546 PHE A C 1 ATOM 4007 O O . PHE A 1 505 ? 25.326 47.878 39.113 1.00 41.72 ? 546 PHE A O 1 ATOM 4008 C CB . PHE A 1 505 ? 25.936 50.538 39.929 1.00 42.00 ? 546 PHE A CB 1 ATOM 4009 C CG . PHE A 1 505 ? 25.872 51.820 40.724 1.00 42.82 ? 546 PHE A CG 1 ATOM 4010 C CD1 . PHE A 1 505 ? 26.660 52.928 40.359 1.00 44.64 ? 546 PHE A CD1 1 ATOM 4011 C CD2 . PHE A 1 505 ? 25.027 51.925 41.829 1.00 42.11 ? 546 PHE A CD2 1 ATOM 4012 C CE1 . PHE A 1 505 ? 26.602 54.115 41.099 1.00 45.08 ? 546 PHE A CE1 1 ATOM 4013 C CE2 . PHE A 1 505 ? 24.956 53.111 42.574 1.00 42.77 ? 546 PHE A CE2 1 ATOM 4014 C CZ . PHE A 1 505 ? 25.745 54.198 42.211 1.00 44.25 ? 546 PHE A CZ 1 ATOM 4015 N N . SER A 1 506 ? 27.361 47.228 39.894 1.00 41.15 ? 547 SER A N 1 ATOM 4016 C CA . SER A 1 506 ? 27.397 46.056 39.017 1.00 40.35 ? 547 SER A CA 1 ATOM 4017 C C . SER A 1 506 ? 26.880 44.762 39.669 1.00 40.04 ? 547 SER A C 1 ATOM 4018 O O . SER A 1 506 ? 26.539 43.816 38.953 1.00 40.02 ? 547 SER A O 1 ATOM 4019 C CB . SER A 1 506 ? 28.785 45.883 38.368 1.00 40.93 ? 547 SER A CB 1 ATOM 4020 O OG A SER A 1 506 ? 29.169 47.071 37.705 0.50 36.96 ? 547 SER A OG 1 ATOM 4021 O OG B SER A 1 506 ? 29.700 45.173 39.194 0.50 43.44 ? 547 SER A OG 1 ATOM 4022 N N . GLY A 1 507 ? 26.761 44.734 41.007 1.00 38.67 ? 548 GLY A N 1 ATOM 4023 C CA . GLY A 1 507 ? 26.497 43.467 41.714 1.00 37.92 ? 548 GLY A CA 1 ATOM 4024 C C . GLY A 1 507 ? 27.775 42.636 41.951 1.00 37.27 ? 548 GLY A C 1 ATOM 4025 O O . GLY A 1 507 ? 28.810 42.834 41.283 1.00 40.72 ? 548 GLY A O 1 ATOM 4026 N N . TYR A 1 508 ? 27.695 41.739 42.940 1.00 33.72 ? 549 TYR A N 1 ATOM 4027 C CA . TYR A 1 508 ? 28.727 40.759 43.294 1.00 31.16 ? 549 TYR A CA 1 ATOM 4028 C C . TYR A 1 508 ? 28.683 39.685 42.191 1.00 29.16 ? 549 TYR A C 1 ATOM 4029 O O . TYR A 1 508 ? 27.745 39.652 41.403 1.00 28.32 ? 549 TYR A O 1 ATOM 4030 C CB . TYR A 1 508 ? 28.423 40.164 44.687 1.00 30.80 ? 549 TYR A CB 1 ATOM 4031 C CG . TYR A 1 508 ? 26.980 39.812 44.867 1.00 27.16 ? 549 TYR A CG 1 ATOM 4032 C CD1 . TYR A 1 508 ? 26.517 38.498 44.651 1.00 25.88 ? 549 TYR A CD1 1 ATOM 4033 C CD2 . TYR A 1 508 ? 26.049 40.787 45.267 1.00 26.88 ? 549 TYR A CD2 1 ATOM 4034 C CE1 . TYR A 1 508 ? 25.141 38.170 44.788 1.00 24.11 ? 549 TYR A CE1 1 ATOM 4035 C CE2 . TYR A 1 508 ? 24.685 40.471 45.398 1.00 26.32 ? 549 TYR A CE2 1 ATOM 4036 C CZ . TYR A 1 508 ? 24.253 39.180 45.166 1.00 24.22 ? 549 TYR A CZ 1 ATOM 4037 O OH . TYR A 1 508 ? 22.923 38.919 45.316 1.00 24.84 ? 549 TYR A OH 1 ATOM 4038 N N . PRO A 1 509 ? 29.714 38.826 42.081 1.00 27.75 ? 550 PRO A N 1 ATOM 4039 C CA . PRO A 1 509 ? 29.760 38.053 40.837 1.00 26.60 ? 550 PRO A CA 1 ATOM 4040 C C . PRO A 1 509 ? 28.607 37.107 40.589 1.00 26.19 ? 550 PRO A C 1 ATOM 4041 O O . PRO A 1 509 ? 28.221 36.924 39.426 1.00 26.30 ? 550 PRO A O 1 ATOM 4042 C CB . PRO A 1 509 ? 31.052 37.246 40.987 1.00 27.05 ? 550 PRO A CB 1 ATOM 4043 C CG . PRO A 1 509 ? 31.963 38.252 41.713 1.00 26.92 ? 550 PRO A CG 1 ATOM 4044 C CD . PRO A 1 509 ? 31.022 38.824 42.777 1.00 28.89 ? 550 PRO A CD 1 ATOM 4045 N N . LEU A 1 510 ? 28.033 36.525 41.647 1.00 23.92 ? 551 LEU A N 1 ATOM 4046 C CA . LEU A 1 510 ? 27.004 35.490 41.448 1.00 23.89 ? 551 LEU A CA 1 ATOM 4047 C C . LEU A 1 510 ? 25.581 36.081 41.516 1.00 23.16 ? 551 LEU A C 1 ATOM 4048 O O . LEU A 1 510 ? 24.566 35.347 41.641 1.00 23.98 ? 551 LEU A O 1 ATOM 4049 C CB . LEU A 1 510 ? 27.164 34.398 42.506 1.00 23.82 ? 551 LEU A CB 1 ATOM 4050 C CG . LEU A 1 510 ? 28.499 33.680 42.215 1.00 24.26 ? 551 LEU A CG 1 ATOM 4051 C CD1 . LEU A 1 510 ? 28.695 32.644 43.289 1.00 24.41 ? 551 LEU A CD1 1 ATOM 4052 C CD2 . LEU A 1 510 ? 28.437 33.019 40.835 1.00 23.56 ? 551 LEU A CD2 1 ATOM 4053 N N . TYR A 1 511 ? 25.518 37.412 41.505 1.00 23.59 ? 552 TYR A N 1 ATOM 4054 C CA . TYR A 1 511 ? 24.224 38.141 41.571 1.00 22.88 ? 552 TYR A CA 1 ATOM 4055 C C . TYR A 1 511 ? 23.178 37.612 40.591 1.00 22.51 ? 552 TYR A C 1 ATOM 4056 O O . TYR A 1 511 ? 23.398 37.557 39.355 1.00 23.71 ? 552 TYR A O 1 ATOM 4057 C CB . TYR A 1 511 ? 24.546 39.600 41.301 1.00 22.59 ? 552 TYR A CB 1 ATOM 4058 C CG . TYR A 1 511 ? 23.383 40.548 41.162 1.00 22.35 ? 552 TYR A CG 1 ATOM 4059 C CD1 . TYR A 1 511 ? 22.445 40.689 42.154 1.00 24.39 ? 552 TYR A CD1 1 ATOM 4060 C CD2 . TYR A 1 511 ? 23.274 41.321 40.000 1.00 22.74 ? 552 TYR A CD2 1 ATOM 4061 C CE1 . TYR A 1 511 ? 21.394 41.622 42.000 1.00 23.22 ? 552 TYR A CE1 1 ATOM 4062 C CE2 . TYR A 1 511 ? 22.257 42.257 39.875 1.00 23.72 ? 552 TYR A CE2 1 ATOM 4063 C CZ . TYR A 1 511 ? 21.345 42.367 40.823 1.00 23.36 ? 552 TYR A CZ 1 ATOM 4064 O OH . TYR A 1 511 ? 20.312 43.293 40.610 1.00 25.16 ? 552 TYR A OH 1 ATOM 4065 N N . HIS A 1 512 ? 22.035 37.205 41.145 1.00 22.43 ? 553 HIS A N 1 ATOM 4066 C CA . HIS A 1 512 ? 20.827 36.781 40.374 1.00 22.36 ? 553 HIS A CA 1 ATOM 4067 C C . HIS A 1 512 ? 21.095 35.514 39.526 1.00 23.07 ? 553 HIS A C 1 ATOM 4068 O O . HIS A 1 512 ? 20.347 35.201 38.572 1.00 22.53 ? 553 HIS A O 1 ATOM 4069 C CB . HIS A 1 512 ? 20.282 37.934 39.474 1.00 22.25 ? 553 HIS A CB 1 ATOM 4070 C CG . HIS A 1 512 ? 19.502 39.014 40.206 1.00 21.84 ? 553 HIS A CG 1 ATOM 4071 N ND1 . HIS A 1 512 ? 18.921 40.068 39.530 1.00 21.17 ? 553 HIS A ND1 1 ATOM 4072 C CD2 . HIS A 1 512 ? 19.241 39.220 41.516 1.00 21.76 ? 553 HIS A CD2 1 ATOM 4073 C CE1 . HIS A 1 512 ? 18.289 40.860 40.395 1.00 21.64 ? 553 HIS A CE1 1 ATOM 4074 N NE2 . HIS A 1 512 ? 18.440 40.352 41.604 1.00 20.24 ? 553 HIS A NE2 1 ATOM 4075 N N . SER A 1 513 ? 22.111 34.764 39.928 1.00 23.95 ? 554 SER A N 1 ATOM 4076 C CA . SER A 1 513 ? 22.437 33.468 39.295 1.00 23.36 ? 554 SER A CA 1 ATOM 4077 C C . SER A 1 513 ? 21.935 32.287 40.188 1.00 26.25 ? 554 SER A C 1 ATOM 4078 O O . SER A 1 513 ? 21.611 32.483 41.341 1.00 24.51 ? 554 SER A O 1 ATOM 4079 C CB . SER A 1 513 ? 23.948 33.345 39.088 1.00 23.76 ? 554 SER A CB 1 ATOM 4080 O OG A SER A 1 513 ? 24.661 33.072 40.289 0.50 22.43 ? 554 SER A OG 1 ATOM 4081 O OG B SER A 1 513 ? 24.341 31.984 38.932 0.50 26.54 ? 554 SER A OG 1 ATOM 4082 N N . VAL A 1 514 ? 21.842 31.111 39.587 1.00 23.95 ? 555 VAL A N 1 ATOM 4083 C CA . VAL A 1 514 ? 21.443 29.904 40.313 1.00 24.95 ? 555 VAL A CA 1 ATOM 4084 C C . VAL A 1 514 ? 22.470 29.589 41.440 1.00 25.93 ? 555 VAL A C 1 ATOM 4085 O O . VAL A 1 514 ? 22.149 28.819 42.383 1.00 28.22 ? 555 VAL A O 1 ATOM 4086 C CB . VAL A 1 514 ? 21.311 28.700 39.359 1.00 24.93 ? 555 VAL A CB 1 ATOM 4087 C CG1 . VAL A 1 514 ? 22.712 28.186 38.898 1.00 26.06 ? 555 VAL A CG1 1 ATOM 4088 C CG2 . VAL A 1 514 ? 20.629 27.544 40.061 1.00 26.34 ? 555 VAL A CG2 1 ATOM 4089 N N . TYR A 1 515 ? 23.681 30.164 41.339 1.00 25.28 ? 556 TYR A N 1 ATOM 4090 C CA . TYR A 1 515 ? 24.801 29.845 42.248 1.00 26.27 ? 556 TYR A CA 1 ATOM 4091 C C . TYR A 1 515 ? 24.688 30.598 43.551 1.00 27.19 ? 556 TYR A C 1 ATOM 4092 O O . TYR A 1 515 ? 25.448 30.336 44.492 1.00 28.48 ? 556 TYR A O 1 ATOM 4093 C CB . TYR A 1 515 ? 26.199 30.034 41.589 1.00 26.59 ? 556 TYR A CB 1 ATOM 4094 C CG . TYR A 1 515 ? 26.301 29.236 40.321 1.00 26.85 ? 556 TYR A CG 1 ATOM 4095 C CD1 . TYR A 1 515 ? 26.219 27.837 40.346 1.00 26.89 ? 556 TYR A CD1 1 ATOM 4096 C CD2 . TYR A 1 515 ? 26.420 29.867 39.095 1.00 27.68 ? 556 TYR A CD2 1 ATOM 4097 C CE1 . TYR A 1 515 ? 26.248 27.086 39.165 1.00 26.48 ? 556 TYR A CE1 1 ATOM 4098 C CE2 . TYR A 1 515 ? 26.475 29.121 37.909 1.00 26.72 ? 556 TYR A CE2 1 ATOM 4099 C CZ . TYR A 1 515 ? 26.386 27.748 37.952 1.00 27.65 ? 556 TYR A CZ 1 ATOM 4100 O OH . TYR A 1 515 ? 26.385 27.015 36.788 1.00 31.03 ? 556 TYR A OH 1 ATOM 4101 N N . GLU A 1 516 ? 23.737 31.519 43.630 1.00 25.36 ? 557 GLU A N 1 ATOM 4102 C CA . GLU A 1 516 ? 23.539 32.275 44.857 1.00 25.80 ? 557 GLU A CA 1 ATOM 4103 C C . GLU A 1 516 ? 22.814 31.382 45.888 1.00 25.46 ? 557 GLU A C 1 ATOM 4104 O O . GLU A 1 516 ? 21.590 31.312 45.928 1.00 25.18 ? 557 GLU A O 1 ATOM 4105 C CB . GLU A 1 516 ? 22.691 33.511 44.523 1.00 26.72 ? 557 GLU A CB 1 ATOM 4106 C CG . GLU A 1 516 ? 23.255 34.740 45.051 1.00 31.79 ? 557 GLU A CG 1 ATOM 4107 C CD . GLU A 1 516 ? 22.187 35.811 45.073 1.00 23.89 ? 557 GLU A CD 1 ATOM 4108 O OE1 . GLU A 1 516 ? 22.103 36.597 44.108 1.00 30.30 ? 557 GLU A OE1 1 ATOM 4109 O OE2 . GLU A 1 516 ? 21.347 35.688 45.943 1.00 29.80 ? 557 GLU A OE2 1 ATOM 4110 N N . THR A 1 517 ? 23.585 30.676 46.711 1.00 25.10 ? 558 THR A N 1 ATOM 4111 C CA . THR A 1 517 ? 23.034 29.663 47.583 1.00 24.89 ? 558 THR A CA 1 ATOM 4112 C C . THR A 1 517 ? 23.449 29.896 49.027 1.00 24.27 ? 558 THR A C 1 ATOM 4113 O O . THR A 1 517 ? 24.339 30.690 49.311 1.00 23.65 ? 558 THR A O 1 ATOM 4114 C CB . THR A 1 517 ? 23.582 28.273 47.209 1.00 26.76 ? 558 THR A CB 1 ATOM 4115 O OG1 . THR A 1 517 ? 25.020 28.292 47.227 1.00 27.50 ? 558 THR A OG1 1 ATOM 4116 C CG2 . THR A 1 517 ? 23.088 27.822 45.794 1.00 24.90 ? 558 THR A CG2 1 ATOM 4117 N N . TYR A 1 518 ? 22.872 29.093 49.910 1.00 24.70 ? 559 TYR A N 1 ATOM 4118 C CA . TYR A 1 518 ? 23.309 29.062 51.295 1.00 25.56 ? 559 TYR A CA 1 ATOM 4119 C C . TYR A 1 518 ? 24.812 28.756 51.388 1.00 25.94 ? 559 TYR A C 1 ATOM 4120 O O . TYR A 1 518 ? 25.513 29.404 52.162 1.00 26.24 ? 559 TYR A O 1 ATOM 4121 C CB . TYR A 1 518 ? 22.527 27.999 52.057 1.00 25.54 ? 559 TYR A CB 1 ATOM 4122 C CG . TYR A 1 518 ? 23.081 27.742 53.433 1.00 25.38 ? 559 TYR A CG 1 ATOM 4123 C CD1 . TYR A 1 518 ? 22.739 28.579 54.493 1.00 26.68 ? 559 TYR A CD1 1 ATOM 4124 C CD2 . TYR A 1 518 ? 23.972 26.676 53.672 1.00 28.04 ? 559 TYR A CD2 1 ATOM 4125 C CE1 . TYR A 1 518 ? 23.228 28.348 55.770 1.00 28.79 ? 559 TYR A CE1 1 ATOM 4126 C CE2 . TYR A 1 518 ? 24.475 26.448 54.954 1.00 30.16 ? 559 TYR A CE2 1 ATOM 4127 C CZ . TYR A 1 518 ? 24.101 27.305 55.991 1.00 31.08 ? 559 TYR A CZ 1 ATOM 4128 O OH . TYR A 1 518 ? 24.585 27.113 57.280 1.00 33.00 ? 559 TYR A OH 1 ATOM 4129 N N . GLU A 1 519 ? 25.284 27.822 50.558 1.00 26.63 ? 560 GLU A N 1 ATOM 4130 C CA . GLU A 1 519 ? 26.703 27.438 50.598 1.00 27.81 ? 560 GLU A CA 1 ATOM 4131 C C . GLU A 1 519 ? 27.605 28.582 50.222 1.00 27.44 ? 560 GLU A C 1 ATOM 4132 O O . GLU A 1 519 ? 28.691 28.738 50.785 1.00 28.16 ? 560 GLU A O 1 ATOM 4133 C CB . GLU A 1 519 ? 26.978 26.225 49.693 1.00 28.38 ? 560 GLU A CB 1 ATOM 4134 C CG . GLU A 1 519 ? 26.405 24.952 50.266 1.00 31.29 ? 560 GLU A CG 1 ATOM 4135 C CD . GLU A 1 519 ? 24.910 24.874 50.056 1.00 29.94 ? 560 GLU A CD 1 ATOM 4136 O OE1 . GLU A 1 519 ? 24.409 25.396 49.043 1.00 30.13 ? 560 GLU A OE1 1 ATOM 4137 O OE2 . GLU A 1 519 ? 24.227 24.289 50.909 1.00 34.35 ? 560 GLU A OE2 1 ATOM 4138 N N . LEU A 1 520 ? 27.175 29.390 49.266 1.00 26.36 ? 561 LEU A N 1 ATOM 4139 C CA . LEU A 1 520 ? 27.953 30.552 48.881 1.00 26.20 ? 561 LEU A CA 1 ATOM 4140 C C . LEU A 1 520 ? 28.241 31.451 50.076 1.00 26.68 ? 561 LEU A C 1 ATOM 4141 O O . LEU A 1 520 ? 29.366 31.922 50.254 1.00 27.42 ? 561 LEU A O 1 ATOM 4142 C CB . LEU A 1 520 ? 27.187 31.349 47.820 1.00 25.57 ? 561 LEU A CB 1 ATOM 4143 C CG . LEU A 1 520 ? 27.878 32.660 47.444 1.00 25.24 ? 561 LEU A CG 1 ATOM 4144 C CD1 . LEU A 1 520 ? 29.326 32.462 46.931 1.00 25.09 ? 561 LEU A CD1 1 ATOM 4145 C CD2 . LEU A 1 520 ? 27.006 33.415 46.413 1.00 27.49 ? 561 LEU A CD2 1 ATOM 4146 N N . VAL A 1 521 ? 27.201 31.707 50.867 1.00 25.81 ? 562 VAL A N 1 ATOM 4147 C CA . VAL A 1 521 ? 27.324 32.565 52.036 1.00 25.30 ? 562 VAL A CA 1 ATOM 4148 C C . VAL A 1 521 ? 28.128 31.884 53.146 1.00 27.67 ? 562 VAL A C 1 ATOM 4149 O O . VAL A 1 521 ? 29.085 32.473 53.699 1.00 28.34 ? 562 VAL A O 1 ATOM 4150 C CB . VAL A 1 521 ? 25.939 32.970 52.563 1.00 25.63 ? 562 VAL A CB 1 ATOM 4151 C CG1 . VAL A 1 521 ? 26.098 33.829 53.851 1.00 26.94 ? 562 VAL A CG1 1 ATOM 4152 C CG2 . VAL A 1 521 ? 25.191 33.758 51.478 1.00 24.81 ? 562 VAL A CG2 1 ATOM 4153 N N . GLU A 1 522 ? 27.754 30.649 53.474 1.00 27.74 ? 563 GLU A N 1 ATOM 4154 C CA . GLU A 1 522 ? 28.365 29.966 54.612 1.00 30.02 ? 563 GLU A CA 1 ATOM 4155 C C . GLU A 1 522 ? 29.830 29.634 54.340 1.00 30.05 ? 563 GLU A C 1 ATOM 4156 O O . GLU A 1 522 ? 30.644 29.669 55.265 1.00 31.36 ? 563 GLU A O 1 ATOM 4157 C CB . GLU A 1 522 ? 27.582 28.702 54.945 1.00 31.13 ? 563 GLU A CB 1 ATOM 4158 C CG . GLU A 1 522 ? 28.007 28.018 56.266 1.00 35.26 ? 563 GLU A CG 1 ATOM 4159 C CD . GLU A 1 522 ? 29.133 27.031 56.096 1.00 41.39 ? 563 GLU A CD 1 ATOM 4160 O OE1 . GLU A 1 522 ? 29.333 26.507 54.972 1.00 44.27 ? 563 GLU A OE1 1 ATOM 4161 O OE2 . GLU A 1 522 ? 29.838 26.791 57.110 1.00 43.95 ? 563 GLU A OE2 1 ATOM 4162 N N . LYS A 1 523 ? 30.186 29.340 53.086 1.00 28.83 ? 564 LYS A N 1 ATOM 4163 C CA . LYS A 1 523 ? 31.582 28.980 52.780 1.00 29.23 ? 564 LYS A CA 1 ATOM 4164 C C . LYS A 1 523 ? 32.480 30.186 52.517 1.00 29.77 ? 564 LYS A C 1 ATOM 4165 O O . LYS A 1 523 ? 33.658 30.194 52.935 1.00 32.95 ? 564 LYS A O 1 ATOM 4166 C CB . LYS A 1 523 ? 31.644 28.053 51.565 1.00 28.80 ? 564 LYS A CB 1 ATOM 4167 C CG . LYS A 1 523 ? 31.049 26.680 51.846 1.00 31.63 ? 564 LYS A CG 1 ATOM 4168 C CD . LYS A 1 523 ? 31.156 25.788 50.588 1.00 34.97 ? 564 LYS A CD 1 ATOM 4169 C CE . LYS A 1 523 ? 30.432 24.423 50.757 1.00 38.88 ? 564 LYS A CE 1 ATOM 4170 N NZ . LYS A 1 523 ? 31.077 23.658 51.852 1.00 43.10 ? 564 LYS A NZ 1 ATOM 4171 N N . PHE A 1 524 ? 31.945 31.180 51.817 1.00 29.21 ? 565 PHE A N 1 ATOM 4172 C CA . PHE A 1 524 ? 32.803 32.186 51.208 1.00 30.09 ? 565 PHE A CA 1 ATOM 4173 C C . PHE A 1 524 ? 32.565 33.583 51.736 1.00 30.34 ? 565 PHE A C 1 ATOM 4174 O O . PHE A 1 524 ? 33.515 34.334 51.864 1.00 33.62 ? 565 PHE A O 1 ATOM 4175 C CB . PHE A 1 524 ? 32.728 32.147 49.665 1.00 29.43 ? 565 PHE A CB 1 ATOM 4176 C CG . PHE A 1 524 ? 33.122 30.815 49.086 1.00 30.45 ? 565 PHE A CG 1 ATOM 4177 C CD1 . PHE A 1 524 ? 34.405 30.318 49.315 1.00 34.07 ? 565 PHE A CD1 1 ATOM 4178 C CD2 . PHE A 1 524 ? 32.213 30.063 48.345 1.00 31.73 ? 565 PHE A CD2 1 ATOM 4179 C CE1 . PHE A 1 524 ? 34.783 29.093 48.793 1.00 33.74 ? 565 PHE A CE1 1 ATOM 4180 C CE2 . PHE A 1 524 ? 32.578 28.814 47.787 1.00 31.32 ? 565 PHE A CE2 1 ATOM 4181 C CZ . PHE A 1 524 ? 33.860 28.320 48.042 1.00 32.31 ? 565 PHE A CZ 1 ATOM 4182 N N . TYR A 1 525 ? 31.325 33.962 52.032 1.00 28.65 ? 566 TYR A N 1 ATOM 4183 C CA . TYR A 1 525 ? 31.110 35.332 52.472 1.00 28.51 ? 566 TYR A CA 1 ATOM 4184 C C . TYR A 1 525 ? 31.185 35.541 53.985 1.00 28.83 ? 566 TYR A C 1 ATOM 4185 O O . TYR A 1 525 ? 31.801 36.521 54.460 1.00 29.67 ? 566 TYR A O 1 ATOM 4186 C CB . TYR A 1 525 ? 29.743 35.848 51.948 1.00 27.15 ? 566 TYR A CB 1 ATOM 4187 C CG . TYR A 1 525 ? 29.829 36.333 50.533 1.00 28.85 ? 566 TYR A CG 1 ATOM 4188 C CD1 . TYR A 1 525 ? 29.830 35.428 49.468 1.00 27.75 ? 566 TYR A CD1 1 ATOM 4189 C CD2 . TYR A 1 525 ? 29.895 37.716 50.247 1.00 29.22 ? 566 TYR A CD2 1 ATOM 4190 C CE1 . TYR A 1 525 ? 29.897 35.867 48.152 1.00 28.20 ? 566 TYR A CE1 1 ATOM 4191 C CE2 . TYR A 1 525 ? 29.976 38.161 48.947 1.00 28.33 ? 566 TYR A CE2 1 ATOM 4192 C CZ . TYR A 1 525 ? 29.985 37.231 47.913 1.00 29.40 ? 566 TYR A CZ 1 ATOM 4193 O OH . TYR A 1 525 ? 30.108 37.715 46.658 1.00 30.14 ? 566 TYR A OH 1 ATOM 4194 N N . ASP A 1 526 ? 30.540 34.667 54.759 1.00 27.45 ? 567 ASP A N 1 ATOM 4195 C CA . ASP A 1 526 ? 30.376 34.968 56.193 1.00 27.77 ? 567 ASP A CA 1 ATOM 4196 C C . ASP A 1 526 ? 30.218 33.706 57.025 1.00 29.06 ? 567 ASP A C 1 ATOM 4197 O O . ASP A 1 526 ? 29.180 33.448 57.591 1.00 29.23 ? 567 ASP A O 1 ATOM 4198 C CB . ASP A 1 526 ? 29.162 35.920 56.356 1.00 25.43 ? 567 ASP A CB 1 ATOM 4199 C CG . ASP A 1 526 ? 29.058 36.567 57.759 1.00 27.30 ? 567 ASP A CG 1 ATOM 4200 O OD1 . ASP A 1 526 ? 30.018 36.558 58.540 1.00 31.25 ? 567 ASP A OD1 1 ATOM 4201 O OD2 . ASP A 1 526 ? 27.981 37.108 58.028 1.00 28.01 ? 567 ASP A OD2 1 ATOM 4202 N N . PRO A 1 527 ? 31.293 32.895 57.127 1.00 30.46 ? 568 PRO A N 1 ATOM 4203 C CA . PRO A 1 527 ? 31.178 31.603 57.796 1.00 31.78 ? 568 PRO A CA 1 ATOM 4204 C C . PRO A 1 527 ? 30.699 31.652 59.234 1.00 32.19 ? 568 PRO A C 1 ATOM 4205 O O . PRO A 1 527 ? 30.005 30.727 59.682 1.00 33.48 ? 568 PRO A O 1 ATOM 4206 C CB . PRO A 1 527 ? 32.614 31.039 57.732 1.00 32.26 ? 568 PRO A CB 1 ATOM 4207 C CG . PRO A 1 527 ? 33.196 31.693 56.520 1.00 33.81 ? 568 PRO A CG 1 ATOM 4208 C CD . PRO A 1 527 ? 32.552 33.048 56.393 1.00 32.19 ? 568 PRO A CD 1 ATOM 4209 N N . MET A 1 528 ? 31.054 32.715 59.942 1.00 31.49 ? 569 MET A N 1 ATOM 4210 C CA . MET A 1 528 ? 30.689 32.854 61.359 1.00 33.19 ? 569 MET A CA 1 ATOM 4211 C C . MET A 1 528 ? 29.394 33.631 61.550 1.00 31.51 ? 569 MET A C 1 ATOM 4212 O O . MET A 1 528 ? 28.917 33.811 62.683 1.00 31.86 ? 569 MET A O 1 ATOM 4213 C CB . MET A 1 528 ? 31.836 33.499 62.146 1.00 35.87 ? 569 MET A CB 1 ATOM 4214 C CG . MET A 1 528 ? 33.110 32.648 62.163 1.00 40.83 ? 569 MET A CG 1 ATOM 4215 S SD . MET A 1 528 ? 32.794 30.980 62.817 1.00 51.79 ? 569 MET A SD 1 ATOM 4216 C CE . MET A 1 528 ? 32.387 31.299 64.540 1.00 50.22 ? 569 MET A CE 1 ATOM 4217 N N . PHE A 1 529 ? 28.835 34.085 60.435 1.00 28.85 ? 570 PHE A N 1 ATOM 4218 C CA . PHE A 1 529 ? 27.644 34.965 60.466 1.00 27.69 ? 570 PHE A CA 1 ATOM 4219 C C . PHE A 1 529 ? 27.824 36.217 61.298 1.00 28.23 ? 570 PHE A C 1 ATOM 4220 O O . PHE A 1 529 ? 26.836 36.854 61.709 1.00 27.70 ? 570 PHE A O 1 ATOM 4221 C CB . PHE A 1 529 ? 26.363 34.154 60.776 1.00 28.03 ? 570 PHE A CB 1 ATOM 4222 C CG . PHE A 1 529 ? 25.947 33.315 59.609 1.00 28.57 ? 570 PHE A CG 1 ATOM 4223 C CD1 . PHE A 1 529 ? 24.976 33.784 58.731 1.00 28.40 ? 570 PHE A CD1 1 ATOM 4224 C CD2 . PHE A 1 529 ? 26.609 32.125 59.330 1.00 30.19 ? 570 PHE A CD2 1 ATOM 4225 C CE1 . PHE A 1 529 ? 24.648 33.033 57.569 1.00 28.05 ? 570 PHE A CE1 1 ATOM 4226 C CE2 . PHE A 1 529 ? 26.284 31.366 58.199 1.00 30.08 ? 570 PHE A CE2 1 ATOM 4227 C CZ . PHE A 1 529 ? 25.282 31.835 57.335 1.00 27.25 ? 570 PHE A CZ 1 ATOM 4228 N N . LYS A 1 530 ? 29.082 36.646 61.429 1.00 28.08 ? 571 LYS A N 1 ATOM 4229 C CA . LYS A 1 530 ? 29.389 37.866 62.201 1.00 29.35 ? 571 LYS A CA 1 ATOM 4230 C C . LYS A 1 530 ? 29.030 39.134 61.445 1.00 28.70 ? 571 LYS A C 1 ATOM 4231 O O . LYS A 1 530 ? 28.619 40.103 62.051 1.00 27.96 ? 571 LYS A O 1 ATOM 4232 C CB . LYS A 1 530 ? 30.854 37.933 62.656 1.00 30.27 ? 571 LYS A CB 1 ATOM 4233 C CG . LYS A 1 530 ? 31.877 37.993 61.542 1.00 32.14 ? 571 LYS A CG 1 ATOM 4234 C CD . LYS A 1 530 ? 33.286 38.029 62.153 1.00 34.51 ? 571 LYS A CD 1 ATOM 4235 C CE . LYS A 1 530 ? 34.344 38.151 61.078 1.00 38.64 ? 571 LYS A CE 1 ATOM 4236 N NZ . LYS A 1 530 ? 35.708 38.401 61.678 1.00 39.36 ? 571 LYS A NZ 1 ATOM 4237 N N . TYR A 1 531 ? 29.201 39.143 60.125 1.00 27.79 ? 572 TYR A N 1 ATOM 4238 C CA . TYR A 1 531 ? 28.802 40.312 59.346 1.00 28.08 ? 572 TYR A CA 1 ATOM 4239 C C . TYR A 1 531 ? 27.292 40.429 59.333 1.00 26.89 ? 572 TYR A C 1 ATOM 4240 O O . TYR A 1 531 ? 26.763 41.534 59.467 1.00 27.37 ? 572 TYR A O 1 ATOM 4241 C CB . TYR A 1 531 ? 29.390 40.259 57.917 1.00 28.38 ? 572 TYR A CB 1 ATOM 4242 C CG . TYR A 1 531 ? 30.891 40.192 57.956 1.00 29.06 ? 572 TYR A CG 1 ATOM 4243 C CD1 . TYR A 1 531 ? 31.642 41.182 58.632 1.00 30.09 ? 572 TYR A CD1 1 ATOM 4244 C CD2 . TYR A 1 531 ? 31.567 39.127 57.374 1.00 31.30 ? 572 TYR A CD2 1 ATOM 4245 C CE1 . TYR A 1 531 ? 33.021 41.112 58.691 1.00 34.18 ? 572 TYR A CE1 1 ATOM 4246 C CE2 . TYR A 1 531 ? 32.927 39.056 57.436 1.00 33.56 ? 572 TYR A CE2 1 ATOM 4247 C CZ . TYR A 1 531 ? 33.645 40.042 58.088 1.00 35.15 ? 572 TYR A CZ 1 ATOM 4248 O OH . TYR A 1 531 ? 35.018 39.906 58.115 1.00 39.09 ? 572 TYR A OH 1 ATOM 4249 N N . HIS A 1 532 ? 26.590 39.298 59.206 1.00 25.76 ? 573 HIS A N 1 ATOM 4250 C CA . HIS A 1 532 ? 25.117 39.291 59.307 1.00 25.14 ? 573 HIS A CA 1 ATOM 4251 C C . HIS A 1 532 ? 24.684 39.818 60.682 1.00 24.30 ? 573 HIS A C 1 ATOM 4252 O O . HIS A 1 532 ? 23.770 40.636 60.751 1.00 24.26 ? 573 HIS A O 1 ATOM 4253 C CB . HIS A 1 532 ? 24.564 37.893 59.126 1.00 25.17 ? 573 HIS A CB 1 ATOM 4254 C CG . HIS A 1 532 ? 24.442 37.469 57.695 1.00 26.92 ? 573 HIS A CG 1 ATOM 4255 N ND1 . HIS A 1 532 ? 25.515 37.022 56.955 1.00 26.35 ? 573 HIS A ND1 1 ATOM 4256 C CD2 . HIS A 1 532 ? 23.370 37.440 56.872 1.00 28.83 ? 573 HIS A CD2 1 ATOM 4257 C CE1 . HIS A 1 532 ? 25.104 36.719 55.729 1.00 28.81 ? 573 HIS A CE1 1 ATOM 4258 N NE2 . HIS A 1 532 ? 23.806 36.969 55.656 1.00 30.62 ? 573 HIS A NE2 1 ATOM 4259 N N . LEU A 1 533 ? 25.318 39.341 61.751 1.00 25.57 ? 574 LEU A N 1 ATOM 4260 C CA . LEU A 1 533 ? 24.950 39.845 63.068 1.00 25.74 ? 574 LEU A CA 1 ATOM 4261 C C . LEU A 1 533 ? 25.172 41.357 63.178 1.00 26.49 ? 574 LEU A C 1 ATOM 4262 O O . LEU A 1 533 ? 24.295 42.080 63.697 1.00 25.27 ? 574 LEU A O 1 ATOM 4263 C CB . LEU A 1 533 ? 25.713 39.089 64.164 1.00 26.73 ? 574 LEU A CB 1 ATOM 4264 C CG . LEU A 1 533 ? 25.416 39.662 65.550 1.00 26.86 ? 574 LEU A CG 1 ATOM 4265 C CD1 . LEU A 1 533 ? 23.937 39.438 65.886 1.00 30.52 ? 574 LEU A CD1 1 ATOM 4266 C CD2 . LEU A 1 533 ? 26.363 38.886 66.493 1.00 28.68 ? 574 LEU A CD2 1 ATOM 4267 N N . THR A 1 534 ? 26.322 41.846 62.714 1.00 26.19 ? 575 THR A N 1 ATOM 4268 C CA . THR A 1 534 ? 26.596 43.310 62.721 1.00 25.70 ? 575 THR A CA 1 ATOM 4269 C C . THR A 1 534 ? 25.521 44.097 61.978 1.00 24.98 ? 575 THR A C 1 ATOM 4270 O O . THR A 1 534 ? 25.014 45.102 62.468 1.00 24.66 ? 575 THR A O 1 ATOM 4271 C CB . THR A 1 534 ? 28.031 43.613 62.167 1.00 27.03 ? 575 THR A CB 1 ATOM 4272 O OG1 . THR A 1 534 ? 29.019 43.103 63.088 1.00 28.48 ? 575 THR A OG1 1 ATOM 4273 C CG2 . THR A 1 534 ? 28.267 45.119 61.995 1.00 27.98 ? 575 THR A CG2 1 ATOM 4274 N N . VAL A 1 535 ? 25.146 43.612 60.791 1.00 23.44 ? 576 VAL A N 1 ATOM 4275 C CA . VAL A 1 535 ? 24.057 44.244 60.039 1.00 23.38 ? 576 VAL A CA 1 ATOM 4276 C C . VAL A 1 535 ? 22.721 44.190 60.769 1.00 23.26 ? 576 VAL A C 1 ATOM 4277 O O . VAL A 1 535 ? 21.947 45.180 60.726 1.00 22.85 ? 576 VAL A O 1 ATOM 4278 C CB . VAL A 1 535 ? 23.997 43.706 58.609 1.00 22.88 ? 576 VAL A CB 1 ATOM 4279 C CG1 . VAL A 1 535 ? 22.743 44.313 57.840 1.00 22.57 ? 576 VAL A CG1 1 ATOM 4280 C CG2 . VAL A 1 535 ? 25.284 44.089 57.908 1.00 24.89 ? 576 VAL A CG2 1 ATOM 4281 N N . ALA A 1 536 ? 22.442 43.075 61.432 1.00 23.91 ? 577 ALA A N 1 ATOM 4282 C CA . ALA A 1 536 ? 21.237 43.000 62.276 1.00 23.97 ? 577 ALA A CA 1 ATOM 4283 C C . ALA A 1 536 ? 21.243 44.045 63.411 1.00 24.14 ? 577 ALA A C 1 ATOM 4284 O O . ALA A 1 536 ? 20.209 44.649 63.706 1.00 23.90 ? 577 ALA A O 1 ATOM 4285 C CB . ALA A 1 536 ? 21.059 41.618 62.840 1.00 24.04 ? 577 ALA A CB 1 ATOM 4286 N N . GLN A 1 537 ? 22.399 44.209 64.034 1.00 26.00 ? 578 GLN A N 1 ATOM 4287 C CA . GLN A 1 537 ? 22.574 45.260 65.046 1.00 25.15 ? 578 GLN A CA 1 ATOM 4288 C C . GLN A 1 537 ? 22.336 46.680 64.501 1.00 25.37 ? 578 GLN A C 1 ATOM 4289 O O . GLN A 1 537 ? 21.730 47.539 65.184 1.00 24.86 ? 578 GLN A O 1 ATOM 4290 C CB . GLN A 1 537 ? 23.953 45.145 65.697 1.00 26.53 ? 578 GLN A CB 1 ATOM 4291 C CG . GLN A 1 537 ? 24.096 43.824 66.476 1.00 25.89 ? 578 GLN A CG 1 ATOM 4292 C CD . GLN A 1 537 ? 25.482 43.647 67.063 1.00 31.28 ? 578 GLN A CD 1 ATOM 4293 O OE1 . GLN A 1 537 ? 26.366 44.455 66.802 1.00 31.14 ? 578 GLN A OE1 1 ATOM 4294 N NE2 . GLN A 1 537 ? 25.684 42.561 67.825 1.00 31.20 ? 578 GLN A NE2 1 ATOM 4295 N N . VAL A 1 538 ? 22.853 46.954 63.302 1.00 24.64 ? 579 VAL A N 1 ATOM 4296 C CA . VAL A 1 538 ? 22.676 48.301 62.718 1.00 24.72 ? 579 VAL A CA 1 ATOM 4297 C C . VAL A 1 538 ? 21.218 48.508 62.329 1.00 24.03 ? 579 VAL A C 1 ATOM 4298 O O . VAL A 1 538 ? 20.584 49.503 62.716 1.00 23.29 ? 579 VAL A O 1 ATOM 4299 C CB . VAL A 1 538 ? 23.600 48.485 61.461 1.00 24.41 ? 579 VAL A CB 1 ATOM 4300 C CG1 . VAL A 1 538 ? 23.305 49.810 60.782 1.00 24.26 ? 579 VAL A CG1 1 ATOM 4301 C CG2 . VAL A 1 538 ? 25.081 48.404 61.869 1.00 26.12 ? 579 VAL A CG2 1 ATOM 4302 N N . ARG A 1 539 ? 20.645 47.583 61.565 1.00 23.04 ? 580 ARG A N 1 ATOM 4303 C CA . ARG A 1 539 ? 19.256 47.789 61.137 1.00 21.72 ? 580 ARG A CA 1 ATOM 4304 C C . ARG A 1 539 ? 18.303 47.768 62.328 1.00 23.41 ? 580 ARG A C 1 ATOM 4305 O O . ARG A 1 539 ? 17.400 48.620 62.445 1.00 22.36 ? 580 ARG A O 1 ATOM 4306 C CB . ARG A 1 539 ? 18.809 46.700 60.172 1.00 21.82 ? 580 ARG A CB 1 ATOM 4307 C CG . ARG A 1 539 ? 19.574 46.746 58.838 1.00 20.70 ? 580 ARG A CG 1 ATOM 4308 C CD . ARG A 1 539 ? 19.183 45.514 58.015 1.00 22.26 ? 580 ARG A CD 1 ATOM 4309 N NE . ARG A 1 539 ? 19.872 45.577 56.731 1.00 22.45 ? 580 ARG A NE 1 ATOM 4310 C CZ . ARG A 1 539 ? 19.873 44.614 55.805 1.00 23.83 ? 580 ARG A CZ 1 ATOM 4311 N NH1 . ARG A 1 539 ? 19.203 43.479 56.011 1.00 26.01 ? 580 ARG A NH1 1 ATOM 4312 N NH2 . ARG A 1 539 ? 20.506 44.821 54.659 1.00 21.68 ? 580 ARG A NH2 1 ATOM 4313 N N . GLY A 1 540 ? 18.486 46.780 63.190 1.00 24.02 ? 581 GLY A N 1 ATOM 4314 C CA . GLY A 1 540 ? 17.641 46.648 64.393 1.00 24.50 ? 581 GLY A CA 1 ATOM 4315 C C . GLY A 1 540 ? 17.818 47.796 65.362 1.00 24.77 ? 581 GLY A C 1 ATOM 4316 O O . GLY A 1 540 ? 16.820 48.322 65.905 1.00 24.31 ? 581 GLY A O 1 ATOM 4317 N N . GLY A 1 541 ? 19.052 48.247 65.527 1.00 24.78 ? 582 GLY A N 1 ATOM 4318 C CA . GLY A 1 541 ? 19.326 49.391 66.404 1.00 24.68 ? 582 GLY A CA 1 ATOM 4319 C C . GLY A 1 541 ? 18.681 50.673 65.895 1.00 24.72 ? 582 GLY A C 1 ATOM 4320 O O . GLY A 1 541 ? 18.155 51.472 66.682 1.00 24.48 ? 582 GLY A O 1 ATOM 4321 N N . MET A 1 542 ? 18.732 50.874 64.568 1.00 23.29 ? 583 MET A N 1 ATOM 4322 C CA . MET A 1 542 ? 18.107 52.045 63.964 1.00 22.88 ? 583 MET A CA 1 ATOM 4323 C C . MET A 1 542 ? 16.619 51.994 64.229 1.00 22.52 ? 583 MET A C 1 ATOM 4324 O O . MET A 1 542 ? 16.040 52.997 64.649 1.00 22.41 ? 583 MET A O 1 ATOM 4325 C CB . MET A 1 542 ? 18.410 52.146 62.447 1.00 22.56 ? 583 MET A CB 1 ATOM 4326 C CG . MET A 1 542 ? 19.848 52.547 62.206 1.00 24.29 ? 583 MET A CG 1 ATOM 4327 S SD . MET A 1 542 ? 20.239 52.533 60.440 1.00 28.18 ? 583 MET A SD 1 ATOM 4328 C CE . MET A 1 542 ? 19.465 54.075 59.915 1.00 26.78 ? 583 MET A CE 1 ATOM 4329 N N . VAL A 1 543 ? 15.994 50.831 64.005 1.00 21.55 ? 584 VAL A N 1 ATOM 4330 C CA . VAL A 1 543 ? 14.571 50.679 64.259 1.00 21.91 ? 584 VAL A CA 1 ATOM 4331 C C . VAL A 1 543 ? 14.241 50.939 65.717 1.00 23.13 ? 584 VAL A C 1 ATOM 4332 O O . VAL A 1 543 ? 13.286 51.678 66.007 1.00 22.37 ? 584 VAL A O 1 ATOM 4333 C CB . VAL A 1 543 ? 14.066 49.267 63.808 1.00 24.05 ? 584 VAL A CB 1 ATOM 4334 C CG1 . VAL A 1 543 ? 12.610 48.982 64.256 1.00 22.66 ? 584 VAL A CG1 1 ATOM 4335 C CG2 . VAL A 1 543 ? 14.169 49.135 62.262 1.00 23.11 ? 584 VAL A CG2 1 ATOM 4336 N N . PHE A 1 544 ? 15.042 50.352 66.600 1.00 23.39 ? 585 PHE A N 1 ATOM 4337 C CA . PHE A 1 544 ? 14.838 50.546 68.041 1.00 24.10 ? 585 PHE A CA 1 ATOM 4338 C C . PHE A 1 544 ? 14.835 52.020 68.404 1.00 25.06 ? 585 PHE A C 1 ATOM 4339 O O . PHE A 1 544 ? 13.894 52.483 69.095 1.00 25.48 ? 585 PHE A O 1 ATOM 4340 C CB . PHE A 1 544 ? 15.922 49.798 68.857 1.00 25.36 ? 585 PHE A CB 1 ATOM 4341 C CG . PHE A 1 544 ? 15.606 49.746 70.334 1.00 27.24 ? 585 PHE A CG 1 ATOM 4342 C CD1 . PHE A 1 544 ? 15.042 48.602 70.881 1.00 28.54 ? 585 PHE A CD1 1 ATOM 4343 C CD2 . PHE A 1 544 ? 15.842 50.843 71.145 1.00 30.33 ? 585 PHE A CD2 1 ATOM 4344 C CE1 . PHE A 1 544 ? 14.687 48.563 72.236 1.00 32.38 ? 585 PHE A CE1 1 ATOM 4345 C CE2 . PHE A 1 544 ? 15.519 50.801 72.508 1.00 28.22 ? 585 PHE A CE2 1 ATOM 4346 C CZ . PHE A 1 544 ? 14.925 49.667 73.034 1.00 30.82 ? 585 PHE A CZ 1 ATOM 4347 N N . GLU A 1 545 ? 15.823 52.774 67.941 1.00 25.28 ? 586 GLU A N 1 ATOM 4348 C CA . GLU A 1 545 ? 15.955 54.200 68.328 1.00 25.83 ? 586 GLU A CA 1 ATOM 4349 C C . GLU A 1 545 ? 14.817 55.021 67.711 1.00 23.95 ? 586 GLU A C 1 ATOM 4350 O O . GLU A 1 545 ? 14.215 55.854 68.347 1.00 24.58 ? 586 GLU A O 1 ATOM 4351 C CB . GLU A 1 545 ? 17.289 54.788 67.844 1.00 27.69 ? 586 GLU A CB 1 ATOM 4352 C CG . GLU A 1 545 ? 18.444 54.561 68.708 1.00 34.97 ? 586 GLU A CG 1 ATOM 4353 C CD . GLU A 1 545 ? 18.167 55.123 70.149 1.00 37.59 ? 586 GLU A CD 1 ATOM 4354 O OE1 . GLU A 1 545 ? 17.816 54.301 70.994 1.00 44.37 ? 586 GLU A OE1 1 ATOM 4355 O OE2 . GLU A 1 545 ? 18.203 56.352 70.389 1.00 45.61 ? 586 GLU A OE2 1 ATOM 4356 N N . LEU A 1 546 ? 14.500 54.743 66.450 1.00 23.09 ? 587 LEU A N 1 ATOM 4357 C CA . LEU A 1 546 ? 13.411 55.457 65.798 1.00 21.79 ? 587 LEU A CA 1 ATOM 4358 C C . LEU A 1 546 ? 12.084 55.180 66.496 1.00 22.24 ? 587 LEU A C 1 ATOM 4359 O O . LEU A 1 546 ? 11.244 56.090 66.611 1.00 23.38 ? 587 LEU A O 1 ATOM 4360 C CB . LEU A 1 546 ? 13.360 55.050 64.287 1.00 21.49 ? 587 LEU A CB 1 ATOM 4361 C CG . LEU A 1 546 ? 14.534 55.550 63.459 1.00 22.30 ? 587 LEU A CG 1 ATOM 4362 C CD1 . LEU A 1 546 ? 14.718 54.669 62.189 1.00 21.60 ? 587 LEU A CD1 1 ATOM 4363 C CD2 . LEU A 1 546 ? 14.235 57.015 63.045 1.00 25.38 ? 587 LEU A CD2 1 ATOM 4364 N N . ALA A 1 547 ? 11.891 53.951 67.007 1.00 22.98 ? 588 ALA A N 1 ATOM 4365 C CA . ALA A 1 547 ? 10.579 53.584 67.594 1.00 24.17 ? 588 ALA A CA 1 ATOM 4366 C C . ALA A 1 547 ? 10.518 53.933 69.085 1.00 24.64 ? 588 ALA A C 1 ATOM 4367 O O . ALA A 1 547 ? 9.418 53.986 69.636 1.00 25.71 ? 588 ALA A O 1 ATOM 4368 C CB . ALA A 1 547 ? 10.244 52.108 67.373 1.00 23.72 ? 588 ALA A CB 1 ATOM 4369 N N . ASN A 1 548 ? 11.662 54.196 69.700 1.00 25.37 ? 589 ASN A N 1 ATOM 4370 C CA . ASN A 1 548 ? 11.672 54.366 71.169 1.00 26.05 ? 589 ASN A CA 1 ATOM 4371 C C . ASN A 1 548 ? 12.192 55.669 71.716 1.00 27.34 ? 589 ASN A C 1 ATOM 4372 O O . ASN A 1 548 ? 11.877 56.009 72.867 1.00 29.14 ? 589 ASN A O 1 ATOM 4373 C CB . ASN A 1 548 ? 12.432 53.194 71.785 1.00 26.26 ? 589 ASN A CB 1 ATOM 4374 C CG A ASN A 1 548 ? 11.793 52.695 73.060 0.50 27.31 ? 589 ASN A CG 1 ATOM 4375 C CG B ASN A 1 548 ? 11.625 51.924 71.714 0.50 28.09 ? 589 ASN A CG 1 ATOM 4376 O OD1 A ASN A 1 548 ? 10.604 52.385 73.083 0.50 28.08 ? 589 ASN A OD1 1 ATOM 4377 O OD1 B ASN A 1 548 ? 10.659 51.742 72.464 0.50 30.41 ? 589 ASN A OD1 1 ATOM 4378 N ND2 A ASN A 1 548 ? 12.590 52.587 74.129 0.50 32.40 ? 589 ASN A ND2 1 ATOM 4379 N ND2 B ASN A 1 548 ? 12.002 51.039 70.807 0.50 29.21 ? 589 ASN A ND2 1 ATOM 4380 N N . SER A 1 549 ? 12.983 56.407 70.943 1.00 26.40 ? 590 SER A N 1 ATOM 4381 C CA . SER A 1 549 ? 13.514 57.680 71.443 1.00 26.52 ? 590 SER A CA 1 ATOM 4382 C C . SER A 1 549 ? 12.380 58.665 71.696 1.00 26.02 ? 590 SER A C 1 ATOM 4383 O O . SER A 1 549 ? 11.460 58.768 70.892 1.00 26.41 ? 590 SER A O 1 ATOM 4384 C CB . SER A 1 549 ? 14.501 58.284 70.426 1.00 27.83 ? 590 SER A CB 1 ATOM 4385 O OG . SER A 1 549 ? 15.111 59.480 70.952 1.00 30.88 ? 590 SER A OG 1 ATOM 4386 N N . ILE A 1 550 ? 12.446 59.379 72.809 1.00 25.38 ? 591 ILE A N 1 ATOM 4387 C CA . ILE A 1 550 ? 11.405 60.340 73.095 1.00 25.68 ? 591 ILE A CA 1 ATOM 4388 C C . ILE A 1 550 ? 11.319 61.385 72.013 1.00 25.65 ? 591 ILE A C 1 ATOM 4389 O O . ILE A 1 550 ? 10.225 61.654 71.515 1.00 26.67 ? 591 ILE A O 1 ATOM 4390 C CB . ILE A 1 550 ? 11.650 60.961 74.495 1.00 26.03 ? 591 ILE A CB 1 ATOM 4391 C CG1 A ILE A 1 550 ? 11.505 59.865 75.528 0.50 28.56 ? 591 ILE A CG1 1 ATOM 4392 C CG1 B ILE A 1 550 ? 11.567 59.836 75.524 0.50 28.99 ? 591 ILE A CG1 1 ATOM 4393 C CG2 A ILE A 1 550 ? 10.694 62.096 74.732 0.50 28.52 ? 591 ILE A CG2 1 ATOM 4394 C CG2 B ILE A 1 550 ? 10.646 62.040 74.761 0.50 28.75 ? 591 ILE A CG2 1 ATOM 4395 C CD1 A ILE A 1 550 ? 11.824 60.350 76.889 0.50 27.98 ? 591 ILE A CD1 1 ATOM 4396 C CD1 B ILE A 1 550 ? 10.307 58.986 75.415 0.50 28.69 ? 591 ILE A CD1 1 ATOM 4397 N N . VAL A 1 551 ? 12.461 61.988 71.699 1.00 26.92 ? 592 VAL A N 1 ATOM 4398 C CA . VAL A 1 551 ? 12.517 62.927 70.579 1.00 26.42 ? 592 VAL A CA 1 ATOM 4399 C C . VAL A 1 551 ? 12.986 62.091 69.393 1.00 25.31 ? 592 VAL A C 1 ATOM 4400 O O . VAL A 1 551 ? 13.962 61.361 69.519 1.00 26.70 ? 592 VAL A O 1 ATOM 4401 C CB . VAL A 1 551 ? 13.494 64.049 70.837 1.00 28.13 ? 592 VAL A CB 1 ATOM 4402 C CG1 . VAL A 1 551 ? 13.606 64.993 69.650 1.00 29.32 ? 592 VAL A CG1 1 ATOM 4403 C CG2 . VAL A 1 551 ? 12.995 64.904 72.039 1.00 30.13 ? 592 VAL A CG2 1 ATOM 4404 N N . LEU A 1 552 ? 12.346 62.249 68.237 1.00 25.96 ? 593 LEU A N 1 ATOM 4405 C CA . LEU A 1 552 ? 12.797 61.479 67.074 1.00 24.94 ? 593 LEU A CA 1 ATOM 4406 C C . LEU A 1 552 ? 14.282 61.754 66.797 1.00 25.46 ? 593 LEU A C 1 ATOM 4407 O O . LEU A 1 552 ? 14.751 62.905 66.870 1.00 26.35 ? 593 LEU A O 1 ATOM 4408 C CB . LEU A 1 552 ? 11.904 61.779 65.824 1.00 23.66 ? 593 LEU A CB 1 ATOM 4409 C CG . LEU A 1 552 ? 10.492 61.184 65.849 1.00 24.83 ? 593 LEU A CG 1 ATOM 4410 C CD1 . LEU A 1 552 ? 9.651 61.773 64.678 1.00 23.90 ? 593 LEU A CD1 1 ATOM 4411 C CD2 . LEU A 1 552 ? 10.614 59.626 65.801 1.00 28.71 ? 593 LEU A CD2 1 ATOM 4412 N N . PRO A 1 553 ? 15.051 60.697 66.448 1.00 24.62 ? 594 PRO A N 1 ATOM 4413 C CA . PRO A 1 553 ? 16.481 60.882 66.298 1.00 26.17 ? 594 PRO A CA 1 ATOM 4414 C C . PRO A 1 553 ? 16.883 61.365 64.893 1.00 25.59 ? 594 PRO A C 1 ATOM 4415 O O . PRO A 1 553 ? 17.645 60.676 64.173 1.00 25.05 ? 594 PRO A O 1 ATOM 4416 C CB . PRO A 1 553 ? 17.049 59.471 66.551 1.00 25.92 ? 594 PRO A CB 1 ATOM 4417 C CG . PRO A 1 553 ? 15.931 58.519 66.055 1.00 26.81 ? 594 PRO A CG 1 ATOM 4418 C CD . PRO A 1 553 ? 14.632 59.287 66.362 1.00 25.36 ? 594 PRO A CD 1 ATOM 4419 N N . PHE A 1 554 ? 16.347 62.515 64.527 1.00 25.03 ? 595 PHE A N 1 ATOM 4420 C CA . PHE A 1 554 ? 16.626 63.162 63.219 1.00 25.18 ? 595 PHE A CA 1 ATOM 4421 C C . PHE A 1 554 ? 17.309 64.476 63.537 1.00 26.94 ? 595 PHE A C 1 ATOM 4422 O O . PHE A 1 554 ? 16.865 65.201 64.463 1.00 28.37 ? 595 PHE A O 1 ATOM 4423 C CB . PHE A 1 554 ? 15.324 63.510 62.519 1.00 24.07 ? 595 PHE A CB 1 ATOM 4424 C CG . PHE A 1 554 ? 14.532 62.324 62.027 1.00 22.77 ? 595 PHE A CG 1 ATOM 4425 C CD1 . PHE A 1 554 ? 15.154 61.114 61.712 1.00 23.78 ? 595 PHE A CD1 1 ATOM 4426 C CD2 . PHE A 1 554 ? 13.169 62.465 61.758 1.00 23.17 ? 595 PHE A CD2 1 ATOM 4427 C CE1 . PHE A 1 554 ? 14.372 60.025 61.205 1.00 23.78 ? 595 PHE A CE1 1 ATOM 4428 C CE2 . PHE A 1 554 ? 12.387 61.364 61.271 1.00 23.01 ? 595 PHE A CE2 1 ATOM 4429 C CZ . PHE A 1 554 ? 13.009 60.162 60.993 1.00 23.51 ? 595 PHE A CZ 1 ATOM 4430 N N . ASP A 1 555 ? 18.379 64.808 62.805 1.00 25.52 ? 596 ASP A N 1 ATOM 4431 C CA . ASP A 1 555 ? 19.044 66.105 62.963 1.00 24.80 ? 596 ASP A CA 1 ATOM 4432 C C . ASP A 1 555 ? 18.867 66.929 61.682 1.00 25.22 ? 596 ASP A C 1 ATOM 4433 O O . ASP A 1 555 ? 19.564 66.668 60.654 1.00 24.14 ? 596 ASP A O 1 ATOM 4434 C CB . ASP A 1 555 ? 20.543 65.950 63.313 1.00 26.65 ? 596 ASP A CB 1 ATOM 4435 C CG . ASP A 1 555 ? 21.159 67.255 63.783 1.00 28.54 ? 596 ASP A CG 1 ATOM 4436 O OD1 . ASP A 1 555 ? 20.610 68.350 63.560 1.00 29.80 ? 596 ASP A OD1 1 ATOM 4437 O OD2 . ASP A 1 555 ? 22.200 67.208 64.482 1.00 32.40 ? 596 ASP A OD2 1 ATOM 4438 N N . CYS A 1 556 ? 17.937 67.890 61.744 1.00 24.77 ? 597 CYS A N 1 ATOM 4439 C CA . CYS A 1 556 ? 17.709 68.745 60.570 1.00 24.71 ? 597 CYS A CA 1 ATOM 4440 C C . CYS A 1 556 ? 18.954 69.509 60.115 1.00 24.96 ? 597 CYS A C 1 ATOM 4441 O O . CYS A 1 556 ? 19.051 69.870 58.934 1.00 25.23 ? 597 CYS A O 1 ATOM 4442 C CB . CYS A 1 556 ? 16.556 69.712 60.811 1.00 23.58 ? 597 CYS A CB 1 ATOM 4443 S SG . CYS A 1 556 ? 16.840 70.816 62.236 1.00 29.37 ? 597 CYS A SG 1 ATOM 4444 N N . ARG A 1 557 ? 19.924 69.792 60.998 1.00 24.23 ? 598 ARG A N 1 ATOM 4445 C CA . ARG A 1 557 ? 21.094 70.536 60.566 1.00 25.35 ? 598 ARG A CA 1 ATOM 4446 C C . ARG A 1 557 ? 21.943 69.756 59.551 1.00 26.17 ? 598 ARG A C 1 ATOM 4447 O O . ARG A 1 557 ? 22.650 70.347 58.746 1.00 26.85 ? 598 ARG A O 1 ATOM 4448 C CB . ARG A 1 557 ? 21.969 70.877 61.795 1.00 26.11 ? 598 ARG A CB 1 ATOM 4449 C CG . ARG A 1 557 ? 21.214 71.793 62.732 1.00 26.78 ? 598 ARG A CG 1 ATOM 4450 C CD . ARG A 1 557 ? 21.952 71.910 64.080 1.00 29.23 ? 598 ARG A CD 1 ATOM 4451 N NE . ARG A 1 557 ? 22.045 70.617 64.745 1.00 29.97 ? 598 ARG A NE 1 ATOM 4452 C CZ . ARG A 1 557 ? 22.653 70.426 65.923 1.00 36.13 ? 598 ARG A CZ 1 ATOM 4453 N NH1 . ARG A 1 557 ? 23.215 71.447 66.558 1.00 36.32 ? 598 ARG A NH1 1 ATOM 4454 N NH2 . ARG A 1 557 ? 22.706 69.215 66.460 1.00 34.47 ? 598 ARG A NH2 1 ATOM 4455 N N . ASP A 1 558 ? 21.855 68.431 59.596 1.00 25.54 ? 599 ASP A N 1 ATOM 4456 C CA . ASP A 1 558 ? 22.620 67.604 58.648 1.00 25.49 ? 599 ASP A CA 1 ATOM 4457 C C . ASP A 1 558 ? 22.011 67.796 57.252 1.00 24.45 ? 599 ASP A C 1 ATOM 4458 O O . ASP A 1 558 ? 22.740 67.731 56.252 1.00 25.46 ? 599 ASP A O 1 ATOM 4459 C CB . ASP A 1 558 ? 22.612 66.134 59.067 1.00 25.78 ? 599 ASP A CB 1 ATOM 4460 C CG . ASP A 1 558 ? 23.493 65.885 60.315 1.00 30.50 ? 599 ASP A CG 1 ATOM 4461 O OD1 . ASP A 1 558 ? 24.462 66.633 60.532 1.00 38.61 ? 599 ASP A OD1 1 ATOM 4462 O OD2 . ASP A 1 558 ? 23.176 65.008 61.112 1.00 32.21 ? 599 ASP A OD2 1 ATOM 4463 N N . TYR A 1 559 ? 20.707 68.036 57.176 1.00 23.27 ? 600 TYR A N 1 ATOM 4464 C CA . TYR A 1 559 ? 20.106 68.286 55.846 1.00 22.52 ? 600 TYR A CA 1 ATOM 4465 C C . TYR A 1 559 ? 20.649 69.627 55.333 1.00 23.69 ? 600 TYR A C 1 ATOM 4466 O O . TYR A 1 559 ? 20.947 69.759 54.155 1.00 22.98 ? 600 TYR A O 1 ATOM 4467 C CB . TYR A 1 559 ? 18.569 68.316 55.888 1.00 21.70 ? 600 TYR A CB 1 ATOM 4468 C CG . TYR A 1 559 ? 17.921 67.375 54.872 1.00 21.91 ? 600 TYR A CG 1 ATOM 4469 C CD1 . TYR A 1 559 ? 18.306 67.423 53.518 1.00 20.56 ? 600 TYR A CD1 1 ATOM 4470 C CD2 . TYR A 1 559 ? 16.928 66.487 55.268 1.00 21.60 ? 600 TYR A CD2 1 ATOM 4471 C CE1 . TYR A 1 559 ? 17.717 66.563 52.595 1.00 22.90 ? 600 TYR A CE1 1 ATOM 4472 C CE2 . TYR A 1 559 ? 16.326 65.580 54.316 1.00 20.32 ? 600 TYR A CE2 1 ATOM 4473 C CZ . TYR A 1 559 ? 16.722 65.690 53.004 1.00 21.72 ? 600 TYR A CZ 1 ATOM 4474 O OH . TYR A 1 559 ? 16.133 64.845 52.098 1.00 21.84 ? 600 TYR A OH 1 ATOM 4475 N N . ALA A 1 560 ? 20.769 70.634 56.218 1.00 23.14 ? 601 ALA A N 1 ATOM 4476 C CA . ALA A 1 560 ? 21.229 71.942 55.781 1.00 23.69 ? 601 ALA A CA 1 ATOM 4477 C C . ALA A 1 560 ? 22.631 71.840 55.159 1.00 25.32 ? 601 ALA A C 1 ATOM 4478 O O . ALA A 1 560 ? 22.921 72.469 54.124 1.00 25.65 ? 601 ALA A O 1 ATOM 4479 C CB . ALA A 1 560 ? 21.260 72.921 56.964 1.00 24.65 ? 601 ALA A CB 1 ATOM 4480 N N . VAL A 1 561 ? 23.505 71.050 55.786 1.00 26.12 ? 602 VAL A N 1 ATOM 4481 C CA . VAL A 1 561 ? 24.863 70.885 55.285 1.00 26.95 ? 602 VAL A CA 1 ATOM 4482 C C . VAL A 1 561 ? 24.858 70.287 53.875 1.00 26.61 ? 602 VAL A C 1 ATOM 4483 O O . VAL A 1 561 ? 25.550 70.789 52.970 1.00 27.32 ? 602 VAL A O 1 ATOM 4484 C CB . VAL A 1 561 ? 25.689 70.010 56.227 1.00 28.59 ? 602 VAL A CB 1 ATOM 4485 C CG1 . VAL A 1 561 ? 27.064 69.619 55.594 1.00 32.81 ? 602 VAL A CG1 1 ATOM 4486 C CG2 . VAL A 1 561 ? 25.908 70.794 57.505 1.00 31.64 ? 602 VAL A CG2 1 ATOM 4487 N N . VAL A 1 562 ? 24.094 69.213 53.699 1.00 25.06 ? 603 VAL A N 1 ATOM 4488 C CA . VAL A 1 562 ? 24.113 68.553 52.366 1.00 24.50 ? 603 VAL A CA 1 ATOM 4489 C C . VAL A 1 562 ? 23.451 69.403 51.304 1.00 23.89 ? 603 VAL A C 1 ATOM 4490 O O . VAL A 1 562 ? 23.916 69.420 50.152 1.00 23.94 ? 603 VAL A O 1 ATOM 4491 C CB . VAL A 1 562 ? 23.636 67.065 52.325 1.00 26.93 ? 603 VAL A CB 1 ATOM 4492 C CG1 . VAL A 1 562 ? 24.391 66.244 53.450 1.00 26.66 ? 603 VAL A CG1 1 ATOM 4493 C CG2 . VAL A 1 562 ? 22.176 66.934 52.410 1.00 28.18 ? 603 VAL A CG2 1 ATOM 4494 N N . LEU A 1 563 ? 22.414 70.153 51.676 1.00 22.54 ? 604 LEU A N 1 ATOM 4495 C CA . LEU A 1 563 ? 21.742 70.984 50.680 1.00 22.19 ? 604 LEU A CA 1 ATOM 4496 C C . LEU A 1 563 ? 22.711 72.021 50.133 1.00 23.21 ? 604 LEU A C 1 ATOM 4497 O O . LEU A 1 563 ? 22.666 72.338 48.950 1.00 24.67 ? 604 LEU A O 1 ATOM 4498 C CB . LEU A 1 563 ? 20.509 71.707 51.280 1.00 22.19 ? 604 LEU A CB 1 ATOM 4499 C CG . LEU A 1 563 ? 19.311 70.799 51.583 1.00 20.62 ? 604 LEU A CG 1 ATOM 4500 C CD1 . LEU A 1 563 ? 18.299 71.531 52.408 1.00 23.85 ? 604 LEU A CD1 1 ATOM 4501 C CD2 . LEU A 1 563 ? 18.695 70.296 50.216 1.00 22.96 ? 604 LEU A CD2 1 ATOM 4502 N N . ARG A 1 564 ? 23.618 72.548 50.975 1.00 23.97 ? 605 ARG A N 1 ATOM 4503 C CA . ARG A 1 564 ? 24.598 73.490 50.453 1.00 25.63 ? 605 ARG A CA 1 ATOM 4504 C C . ARG A 1 564 ? 25.584 72.787 49.496 1.00 25.69 ? 605 ARG A C 1 ATOM 4505 O O . ARG A 1 564 ? 25.912 73.321 48.433 1.00 25.86 ? 605 ARG A O 1 ATOM 4506 C CB . ARG A 1 564 ? 25.345 74.193 51.604 1.00 26.29 ? 605 ARG A CB 1 ATOM 4507 C CG . ARG A 1 564 ? 26.499 75.087 51.130 1.00 29.12 ? 605 ARG A CG 1 ATOM 4508 C CD . ARG A 1 564 ? 26.039 76.220 50.155 1.00 32.16 ? 605 ARG A CD 1 ATOM 4509 N NE . ARG A 1 564 ? 27.177 77.024 49.692 1.00 35.34 ? 605 ARG A NE 1 ATOM 4510 C CZ . ARG A 1 564 ? 27.618 78.107 50.323 1.00 43.40 ? 605 ARG A CZ 1 ATOM 4511 N NH1 . ARG A 1 564 ? 27.018 78.512 51.447 1.00 42.59 ? 605 ARG A NH1 1 ATOM 4512 N NH2 . ARG A 1 564 ? 28.666 78.780 49.852 1.00 44.41 ? 605 ARG A NH2 1 ATOM 4513 N N . LYS A 1 565 ? 26.055 71.591 49.872 1.00 26.03 ? 606 LYS A N 1 ATOM 4514 C CA . LYS A 1 565 ? 26.907 70.792 48.979 1.00 26.87 ? 606 LYS A CA 1 ATOM 4515 C C . LYS A 1 565 ? 26.213 70.533 47.623 1.00 26.21 ? 606 LYS A C 1 ATOM 4516 O O . LYS A 1 565 ? 26.831 70.687 46.563 1.00 25.77 ? 606 LYS A O 1 ATOM 4517 C CB A LYS A 1 565 ? 27.278 69.482 49.656 0.35 26.87 ? 606 LYS A CB 1 ATOM 4518 C CB B LYS A 1 565 ? 27.230 69.460 49.668 0.65 27.61 ? 606 LYS A CB 1 ATOM 4519 C CG A LYS A 1 565 ? 28.051 69.679 50.940 0.35 27.68 ? 606 LYS A CG 1 ATOM 4520 C CG B LYS A 1 565 ? 28.086 68.473 48.863 0.65 31.93 ? 606 LYS A CG 1 ATOM 4521 C CD A LYS A 1 565 ? 29.550 69.778 50.682 0.35 32.58 ? 606 LYS A CD 1 ATOM 4522 C CD B LYS A 1 565 ? 28.387 67.174 49.664 0.65 36.37 ? 606 LYS A CD 1 ATOM 4523 C CE A LYS A 1 565 ? 30.319 69.742 51.990 0.35 34.80 ? 606 LYS A CE 1 ATOM 4524 C CE B LYS A 1 565 ? 27.161 66.266 49.859 0.65 38.13 ? 606 LYS A CE 1 ATOM 4525 N NZ A LYS A 1 565 ? 29.544 68.926 52.936 0.35 35.02 ? 606 LYS A NZ 1 ATOM 4526 N NZ B LYS A 1 565 ? 27.473 65.002 50.619 0.65 37.38 ? 606 LYS A NZ 1 ATOM 4527 N N . TYR A 1 566 ? 24.919 70.167 47.665 1.00 23.90 ? 607 TYR A N 1 ATOM 4528 C CA . TYR A 1 566 ? 24.197 69.880 46.402 1.00 22.54 ? 607 TYR A CA 1 ATOM 4529 C C . TYR A 1 566 ? 23.979 71.156 45.595 1.00 22.76 ? 607 TYR A C 1 ATOM 4530 O O . TYR A 1 566 ? 24.044 71.098 44.377 1.00 23.55 ? 607 TYR A O 1 ATOM 4531 C CB . TYR A 1 566 ? 22.859 69.234 46.685 1.00 22.57 ? 607 TYR A CB 1 ATOM 4532 C CG . TYR A 1 566 ? 22.926 67.915 47.436 1.00 21.51 ? 607 TYR A CG 1 ATOM 4533 C CD1 . TYR A 1 566 ? 24.090 67.152 47.461 1.00 22.63 ? 607 TYR A CD1 1 ATOM 4534 C CD2 . TYR A 1 566 ? 21.807 67.455 48.129 1.00 22.29 ? 607 TYR A CD2 1 ATOM 4535 C CE1 . TYR A 1 566 ? 24.118 65.945 48.178 1.00 24.16 ? 607 TYR A CE1 1 ATOM 4536 C CE2 . TYR A 1 566 ? 21.808 66.268 48.806 1.00 21.73 ? 607 TYR A CE2 1 ATOM 4537 C CZ . TYR A 1 566 ? 22.974 65.523 48.823 1.00 25.56 ? 607 TYR A CZ 1 ATOM 4538 O OH . TYR A 1 566 ? 22.962 64.352 49.518 1.00 25.18 ? 607 TYR A OH 1 ATOM 4539 N N . ALA A 1 567 ? 23.740 72.280 46.264 1.00 22.81 ? 608 ALA A N 1 ATOM 4540 C CA . ALA A 1 567 ? 23.594 73.545 45.541 1.00 24.28 ? 608 ALA A CA 1 ATOM 4541 C C . ALA A 1 567 ? 24.915 73.938 44.868 1.00 25.38 ? 608 ALA A C 1 ATOM 4542 O O . ALA A 1 567 ? 24.911 74.341 43.699 1.00 25.70 ? 608 ALA A O 1 ATOM 4543 C CB . ALA A 1 567 ? 23.079 74.673 46.440 1.00 24.08 ? 608 ALA A CB 1 ATOM 4544 N N . ASP A 1 568 ? 26.039 73.804 45.584 1.00 26.61 ? 609 ASP A N 1 ATOM 4545 C CA . ASP A 1 568 ? 27.345 74.101 44.983 1.00 28.48 ? 609 ASP A CA 1 ATOM 4546 C C . ASP A 1 568 ? 27.572 73.207 43.742 1.00 27.70 ? 609 ASP A C 1 ATOM 4547 O O . ASP A 1 568 ? 28.116 73.663 42.710 1.00 27.49 ? 609 ASP A O 1 ATOM 4548 C CB . ASP A 1 568 ? 28.457 73.828 45.981 1.00 29.44 ? 609 ASP A CB 1 ATOM 4549 C CG . ASP A 1 568 ? 28.532 74.844 47.110 1.00 34.28 ? 609 ASP A CG 1 ATOM 4550 O OD1 . ASP A 1 568 ? 27.974 75.937 47.039 1.00 35.88 ? 609 ASP A OD1 1 ATOM 4551 O OD2 . ASP A 1 568 ? 29.254 74.541 48.092 1.00 40.92 ? 609 ASP A OD2 1 ATOM 4552 N N . LYS A 1 569 ? 27.146 71.948 43.844 1.00 26.53 ? 610 LYS A N 1 ATOM 4553 C CA . LYS A 1 569 ? 27.408 70.995 42.787 1.00 27.11 ? 610 LYS A CA 1 ATOM 4554 C C . LYS A 1 569 ? 26.612 71.311 41.529 1.00 26.85 ? 610 LYS A C 1 ATOM 4555 O O . LYS A 1 569 ? 27.166 71.346 40.431 1.00 28.44 ? 610 LYS A O 1 ATOM 4556 C CB . LYS A 1 569 ? 27.130 69.567 43.286 1.00 27.45 ? 610 LYS A CB 1 ATOM 4557 C CG . LYS A 1 569 ? 27.407 68.493 42.260 1.00 31.50 ? 610 LYS A CG 1 ATOM 4558 C CD . LYS A 1 569 ? 26.939 67.169 42.806 1.00 37.19 ? 610 LYS A CD 1 ATOM 4559 C CE . LYS A 1 569 ? 27.521 65.982 42.049 1.00 41.76 ? 610 LYS A CE 1 ATOM 4560 N NZ . LYS A 1 569 ? 26.472 64.878 42.096 1.00 41.04 ? 610 LYS A NZ 1 ATOM 4561 N N . ILE A 1 570 ? 25.320 71.570 41.706 1.00 25.32 ? 611 ILE A N 1 ATOM 4562 C CA . ILE A 1 570 ? 24.466 71.877 40.552 1.00 24.60 ? 611 ILE A CA 1 ATOM 4563 C C . ILE A 1 570 ? 24.868 73.238 39.894 1.00 25.47 ? 611 ILE A C 1 ATOM 4564 O O . ILE A 1 570 ? 24.904 73.359 38.659 1.00 24.84 ? 611 ILE A O 1 ATOM 4565 C CB . ILE A 1 570 ? 22.959 71.770 40.933 1.00 24.12 ? 611 ILE A CB 1 ATOM 4566 C CG1 . ILE A 1 570 ? 22.109 71.731 39.665 1.00 25.98 ? 611 ILE A CG1 1 ATOM 4567 C CG2 . ILE A 1 570 ? 22.527 72.889 41.887 1.00 24.42 ? 611 ILE A CG2 1 ATOM 4568 C CD1 . ILE A 1 570 ? 22.323 70.420 38.930 1.00 29.37 ? 611 ILE A CD1 1 ATOM 4569 N N . TYR A 1 571 ? 25.234 74.236 40.711 1.00 25.67 ? 612 TYR A N 1 ATOM 4570 C CA . TYR A 1 571 ? 25.764 75.478 40.214 1.00 28.03 ? 612 TYR A CA 1 ATOM 4571 C C . TYR A 1 571 ? 27.033 75.233 39.350 1.00 28.14 ? 612 TYR A C 1 ATOM 4572 O O . TYR A 1 571 ? 27.179 75.782 38.250 1.00 28.88 ? 612 TYR A O 1 ATOM 4573 C CB . TYR A 1 571 ? 26.045 76.438 41.402 1.00 27.31 ? 612 TYR A CB 1 ATOM 4574 C CG . TYR A 1 571 ? 26.800 77.674 40.998 1.00 31.76 ? 612 TYR A CG 1 ATOM 4575 C CD1 . TYR A 1 571 ? 26.143 78.754 40.418 1.00 37.66 ? 612 TYR A CD1 1 ATOM 4576 C CD2 . TYR A 1 571 ? 28.175 77.710 41.140 1.00 38.67 ? 612 TYR A CD2 1 ATOM 4577 C CE1 . TYR A 1 571 ? 26.876 79.905 40.045 1.00 41.37 ? 612 TYR A CE1 1 ATOM 4578 C CE2 . TYR A 1 571 ? 28.922 78.837 40.752 1.00 43.38 ? 612 TYR A CE2 1 ATOM 4579 C CZ . TYR A 1 571 ? 28.253 79.909 40.199 1.00 44.95 ? 612 TYR A CZ 1 ATOM 4580 O OH . TYR A 1 571 ? 28.988 81.010 39.827 1.00 52.58 ? 612 TYR A OH 1 ATOM 4581 N N . SER A 1 572 ? 27.916 74.338 39.816 1.00 28.07 ? 613 SER A N 1 ATOM 4582 C CA . SER A 1 572 ? 29.160 74.080 39.091 1.00 30.83 ? 613 SER A CA 1 ATOM 4583 C C . SER A 1 572 ? 28.886 73.430 37.740 1.00 29.94 ? 613 SER A C 1 ATOM 4584 O O . SER A 1 572 ? 29.580 73.729 36.790 1.00 31.52 ? 613 SER A O 1 ATOM 4585 C CB . SER A 1 572 ? 30.117 73.235 39.921 1.00 30.44 ? 613 SER A CB 1 ATOM 4586 O OG A SER A 1 572 ? 30.573 73.983 41.029 0.50 33.97 ? 613 SER A OG 1 ATOM 4587 O OG B SER A 1 572 ? 29.753 71.875 39.898 0.50 32.00 ? 613 SER A OG 1 ATOM 4588 N N . ILE A 1 573 ? 27.848 72.587 37.667 1.00 28.76 ? 614 ILE A N 1 ATOM 4589 C CA . ILE A 1 573 ? 27.477 71.975 36.405 1.00 29.01 ? 614 ILE A CA 1 ATOM 4590 C C . ILE A 1 573 ? 27.015 73.052 35.432 1.00 29.81 ? 614 ILE A C 1 ATOM 4591 O O . ILE A 1 573 ? 27.409 73.076 34.264 1.00 30.86 ? 614 ILE A O 1 ATOM 4592 C CB . ILE A 1 573 ? 26.395 70.873 36.598 1.00 28.46 ? 614 ILE A CB 1 ATOM 4593 C CG1 . ILE A 1 573 ? 27.037 69.700 37.366 1.00 27.40 ? 614 ILE A CG1 1 ATOM 4594 C CG2 . ILE A 1 573 ? 25.821 70.432 35.208 1.00 29.56 ? 614 ILE A CG2 1 ATOM 4595 C CD1 . ILE A 1 573 ? 26.018 68.649 37.861 1.00 28.79 ? 614 ILE A CD1 1 ATOM 4596 N N . SER A 1 574 ? 26.157 73.952 35.923 1.00 28.71 ? 615 SER A N 1 ATOM 4597 C CA . SER A 1 574 ? 25.597 74.999 35.070 1.00 28.82 ? 615 SER A CA 1 ATOM 4598 C C . SER A 1 574 ? 26.697 75.912 34.573 1.00 30.68 ? 615 SER A C 1 ATOM 4599 O O . SER A 1 574 ? 26.689 76.366 33.413 1.00 29.62 ? 615 SER A O 1 ATOM 4600 C CB . SER A 1 574 ? 24.542 75.789 35.862 1.00 28.57 ? 615 SER A CB 1 ATOM 4601 O OG . SER A 1 574 ? 23.895 76.703 34.992 1.00 29.44 ? 615 SER A OG 1 ATOM 4602 N N . MET A 1 575 ? 27.664 76.163 35.456 1.00 31.26 ? 616 MET A N 1 ATOM 4603 C CA . MET A 1 575 ? 28.792 77.065 35.157 1.00 33.99 ? 616 MET A CA 1 ATOM 4604 C C . MET A 1 575 ? 29.796 76.528 34.126 1.00 35.46 ? 616 MET A C 1 ATOM 4605 O O . MET A 1 575 ? 30.755 77.240 33.755 1.00 36.69 ? 616 MET A O 1 ATOM 4606 C CB . MET A 1 575 ? 29.488 77.504 36.446 1.00 35.41 ? 616 MET A CB 1 ATOM 4607 C CG . MET A 1 575 ? 28.756 78.669 37.127 1.00 37.03 ? 616 MET A CG 1 ATOM 4608 S SD . MET A 1 575 ? 28.652 80.177 36.066 1.00 46.19 ? 616 MET A SD 1 ATOM 4609 C CE . MET A 1 575 ? 30.384 80.566 35.813 1.00 44.86 ? 616 MET A CE 1 ATOM 4610 N N . LYS A 1 576 ? 29.554 75.307 33.644 1.00 35.85 ? 617 LYS A N 1 ATOM 4611 C CA . LYS A 1 576 ? 30.243 74.833 32.421 1.00 37.90 ? 617 LYS A CA 1 ATOM 4612 C C . LYS A 1 576 ? 29.791 75.638 31.176 1.00 37.42 ? 617 LYS A C 1 ATOM 4613 O O . LYS A 1 576 ? 30.442 75.583 30.119 1.00 37.10 ? 617 LYS A O 1 ATOM 4614 C CB . LYS A 1 576 ? 30.005 73.322 32.230 1.00 39.00 ? 617 LYS A CB 1 ATOM 4615 C CG . LYS A 1 576 ? 30.648 72.452 33.335 1.00 41.85 ? 617 LYS A CG 1 ATOM 4616 C CD . LYS A 1 576 ? 32.181 72.619 33.358 1.00 52.73 ? 617 LYS A CD 1 ATOM 4617 C CE . LYS A 1 576 ? 32.854 71.768 34.453 1.00 56.76 ? 617 LYS A CE 1 ATOM 4618 N NZ . LYS A 1 576 ? 32.641 72.298 35.844 1.00 58.99 ? 617 LYS A NZ 1 ATOM 4619 N N . HIS A 1 577 ? 28.695 76.399 31.319 1.00 35.44 ? 618 HIS A N 1 ATOM 4620 C CA . HIS A 1 577 ? 28.066 77.122 30.201 1.00 35.36 ? 618 HIS A CA 1 ATOM 4621 C C . HIS A 1 577 ? 27.895 78.612 30.539 1.00 34.57 ? 618 HIS A C 1 ATOM 4622 O O . HIS A 1 577 ? 26.757 79.120 30.570 1.00 33.38 ? 618 HIS A O 1 ATOM 4623 C CB . HIS A 1 577 ? 26.671 76.552 29.916 1.00 34.50 ? 618 HIS A CB 1 ATOM 4624 C CG . HIS A 1 577 ? 26.618 75.051 29.863 1.00 36.91 ? 618 HIS A CG 1 ATOM 4625 N ND1 . HIS A 1 577 ? 26.825 74.342 28.701 1.00 38.11 ? 618 HIS A ND1 1 ATOM 4626 C CD2 . HIS A 1 577 ? 26.348 74.130 30.825 1.00 39.32 ? 618 HIS A CD2 1 ATOM 4627 C CE1 . HIS A 1 577 ? 26.710 73.050 28.950 1.00 37.49 ? 618 HIS A CE1 1 ATOM 4628 N NE2 . HIS A 1 577 ? 26.418 72.892 30.231 1.00 39.59 ? 618 HIS A NE2 1 ATOM 4629 N N . PRO A 1 578 ? 29.010 79.322 30.793 1.00 35.67 ? 619 PRO A N 1 ATOM 4630 C CA . PRO A 1 578 ? 28.891 80.693 31.281 1.00 34.64 ? 619 PRO A CA 1 ATOM 4631 C C . PRO A 1 578 ? 28.196 81.608 30.292 1.00 35.02 ? 619 PRO A C 1 ATOM 4632 O O . PRO A 1 578 ? 27.417 82.470 30.729 1.00 34.64 ? 619 PRO A O 1 ATOM 4633 C CB . PRO A 1 578 ? 30.353 81.141 31.486 1.00 37.69 ? 619 PRO A CB 1 ATOM 4634 C CG . PRO A 1 578 ? 31.194 80.145 30.675 1.00 38.54 ? 619 PRO A CG 1 ATOM 4635 C CD . PRO A 1 578 ? 30.410 78.864 30.754 1.00 35.55 ? 619 PRO A CD 1 ATOM 4636 N N . GLN A 1 579 ? 28.447 81.451 28.985 1.00 35.03 ? 620 GLN A N 1 ATOM 4637 C CA A GLN A 1 579 ? 27.820 82.334 27.992 0.60 36.03 ? 620 GLN A CA 1 ATOM 4638 C CA B GLN A 1 579 ? 27.851 82.381 28.048 0.40 35.93 ? 620 GLN A CA 1 ATOM 4639 C C . GLN A 1 579 ? 26.314 82.226 28.028 1.00 34.87 ? 620 GLN A C 1 ATOM 4640 O O . GLN A 1 579 ? 25.598 83.227 27.989 1.00 34.91 ? 620 GLN A O 1 ATOM 4641 C CB A GLN A 1 579 ? 28.297 82.059 26.560 0.60 37.34 ? 620 GLN A CB 1 ATOM 4642 C CB B GLN A 1 579 ? 28.474 82.290 26.646 0.40 37.66 ? 620 GLN A CB 1 ATOM 4643 C CG A GLN A 1 579 ? 27.752 83.095 25.537 0.60 40.14 ? 620 GLN A CG 1 ATOM 4644 C CG B GLN A 1 579 ? 30.039 82.222 26.503 0.40 38.83 ? 620 GLN A CG 1 ATOM 4645 C CD A GLN A 1 579 ? 27.941 84.570 25.975 0.60 40.78 ? 620 GLN A CD 1 ATOM 4646 C CD B GLN A 1 579 ? 30.931 82.836 27.624 0.40 41.58 ? 620 GLN A CD 1 ATOM 4647 O OE1 A GLN A 1 579 ? 26.975 85.256 26.360 0.60 37.25 ? 620 GLN A OE1 1 ATOM 4648 O OE1 B GLN A 1 579 ? 30.710 83.944 28.132 0.40 39.53 ? 620 GLN A OE1 1 ATOM 4649 N NE2 A GLN A 1 579 ? 29.180 85.048 25.940 0.60 44.69 ? 620 GLN A NE2 1 ATOM 4650 N NE2 B GLN A 1 579 ? 32.002 82.110 27.949 0.40 43.72 ? 620 GLN A NE2 1 ATOM 4651 N N . GLU A 1 580 ? 25.815 80.991 28.108 1.00 33.41 ? 621 GLU A N 1 ATOM 4652 C CA . GLU A 1 580 ? 24.380 80.814 28.147 1.00 32.70 ? 621 GLU A CA 1 ATOM 4653 C C . GLU A 1 580 ? 23.786 81.364 29.431 1.00 31.35 ? 621 GLU A C 1 ATOM 4654 O O . GLU A 1 580 ? 22.674 81.910 29.416 1.00 32.34 ? 621 GLU A O 1 ATOM 4655 C CB . GLU A 1 580 ? 23.983 79.351 27.951 1.00 32.57 ? 621 GLU A CB 1 ATOM 4656 C CG . GLU A 1 580 ? 24.260 78.891 26.490 1.00 38.17 ? 621 GLU A CG 1 ATOM 4657 C CD . GLU A 1 580 ? 25.709 78.614 26.163 1.00 42.41 ? 621 GLU A CD 1 ATOM 4658 O OE1 . GLU A 1 580 ? 26.572 78.428 27.058 1.00 44.13 ? 621 GLU A OE1 1 ATOM 4659 O OE2 . GLU A 1 580 ? 26.019 78.604 24.952 1.00 50.44 ? 621 GLU A OE2 1 ATOM 4660 N N . MET A 1 581 ? 24.492 81.192 30.551 1.00 30.59 ? 622 MET A N 1 ATOM 4661 C CA . MET A 1 581 ? 23.979 81.751 31.798 1.00 29.76 ? 622 MET A CA 1 ATOM 4662 C C . MET A 1 581 ? 23.872 83.271 31.694 1.00 30.73 ? 622 MET A C 1 ATOM 4663 O O . MET A 1 581 ? 22.917 83.840 32.225 1.00 29.03 ? 622 MET A O 1 ATOM 4664 C CB . MET A 1 581 ? 24.810 81.310 33.011 1.00 30.00 ? 622 MET A CB 1 ATOM 4665 C CG . MET A 1 581 ? 24.707 79.801 33.255 1.00 29.76 ? 622 MET A CG 1 ATOM 4666 S SD . MET A 1 581 ? 25.659 79.319 34.719 1.00 31.71 ? 622 MET A SD 1 ATOM 4667 C CE . MET A 1 581 ? 24.776 80.192 36.031 1.00 31.01 ? 622 MET A CE 1 ATOM 4668 N N . LYS A 1 582 ? 24.821 83.913 30.988 1.00 31.04 ? 623 LYS A N 1 ATOM 4669 C CA . LYS A 1 582 ? 24.757 85.372 30.792 1.00 33.06 ? 623 LYS A CA 1 ATOM 4670 C C . LYS A 1 582 ? 23.546 85.731 29.902 1.00 33.66 ? 623 LYS A C 1 ATOM 4671 O O . LYS A 1 582 ? 22.707 86.570 30.250 1.00 33.06 ? 623 LYS A O 1 ATOM 4672 C CB . LYS A 1 582 ? 26.063 85.909 30.166 1.00 34.56 ? 623 LYS A CB 1 ATOM 4673 C CG . LYS A 1 582 ? 27.269 85.749 31.083 1.00 35.60 ? 623 LYS A CG 1 ATOM 4674 C CD . LYS A 1 582 ? 28.539 86.270 30.416 1.00 40.50 ? 623 LYS A CD 1 ATOM 4675 C CE . LYS A 1 582 ? 29.692 86.047 31.390 1.00 47.30 ? 623 LYS A CE 1 ATOM 4676 N NZ . LYS A 1 582 ? 30.874 85.345 30.815 1.00 52.42 ? 623 LYS A NZ 1 ATOM 4677 N N . THR A 1 583 ? 23.464 85.058 28.758 1.00 34.66 ? 624 THR A N 1 ATOM 4678 C CA . THR A 1 583 ? 22.414 85.304 27.777 1.00 36.19 ? 624 THR A CA 1 ATOM 4679 C C . THR A 1 583 ? 20.998 85.158 28.292 1.00 34.40 ? 624 THR A C 1 ATOM 4680 O O . THR A 1 583 ? 20.153 86.014 28.003 1.00 34.69 ? 624 THR A O 1 ATOM 4681 C CB . THR A 1 583 ? 22.609 84.407 26.545 1.00 37.29 ? 624 THR A CB 1 ATOM 4682 O OG1 . THR A 1 583 ? 23.829 84.791 25.925 1.00 40.57 ? 624 THR A OG1 1 ATOM 4683 C CG2 . THR A 1 583 ? 21.453 84.620 25.533 1.00 41.02 ? 624 THR A CG2 1 ATOM 4684 N N . TYR A 1 584 ? 20.747 84.100 29.070 1.00 32.80 ? 625 TYR A N 1 ATOM 4685 C CA . TYR A 1 584 ? 19.411 83.797 29.557 1.00 32.03 ? 625 TYR A CA 1 ATOM 4686 C C . TYR A 1 584 ? 19.224 84.195 31.023 1.00 31.09 ? 625 TYR A C 1 ATOM 4687 O O . TYR A 1 584 ? 18.197 83.885 31.619 1.00 30.72 ? 625 TYR A O 1 ATOM 4688 C CB . TYR A 1 584 ? 19.052 82.306 29.328 1.00 31.31 ? 625 TYR A CB 1 ATOM 4689 C CG . TYR A 1 584 ? 19.177 81.990 27.866 1.00 34.20 ? 625 TYR A CG 1 ATOM 4690 C CD1 . TYR A 1 584 ? 18.303 82.582 26.943 1.00 37.68 ? 625 TYR A CD1 1 ATOM 4691 C CD2 . TYR A 1 584 ? 20.194 81.158 27.393 1.00 35.64 ? 625 TYR A CD2 1 ATOM 4692 C CE1 . TYR A 1 584 ? 18.439 82.341 25.566 1.00 39.71 ? 625 TYR A CE1 1 ATOM 4693 C CE2 . TYR A 1 584 ? 20.332 80.895 26.034 1.00 39.54 ? 625 TYR A CE2 1 ATOM 4694 C CZ . TYR A 1 584 ? 19.441 81.479 25.124 1.00 41.11 ? 625 TYR A CZ 1 ATOM 4695 O OH . TYR A 1 584 ? 19.593 81.273 23.763 1.00 44.05 ? 625 TYR A OH 1 ATOM 4696 N N . SER A 1 585 ? 20.212 84.899 31.590 1.00 30.29 ? 626 SER A N 1 ATOM 4697 C CA . SER A 1 585 ? 20.053 85.474 32.932 1.00 30.20 ? 626 SER A CA 1 ATOM 4698 C C . SER A 1 585 ? 19.742 84.372 33.955 1.00 28.50 ? 626 SER A C 1 ATOM 4699 O O . SER A 1 585 ? 18.762 84.436 34.728 1.00 28.12 ? 626 SER A O 1 ATOM 4700 C CB A SER A 1 585 ? 18.979 86.579 32.947 0.65 30.09 ? 626 SER A CB 1 ATOM 4701 C CB B SER A 1 585 ? 18.924 86.515 32.887 0.35 30.56 ? 626 SER A CB 1 ATOM 4702 O OG A SER A 1 585 ? 19.388 87.669 32.140 0.65 27.89 ? 626 SER A OG 1 ATOM 4703 O OG B SER A 1 585 ? 18.826 87.220 34.095 0.35 33.34 ? 626 SER A OG 1 ATOM 4704 N N . VAL A 1 586 ? 20.546 83.314 33.924 1.00 28.63 ? 627 VAL A N 1 ATOM 4705 C CA . VAL A 1 586 ? 20.296 82.123 34.718 1.00 28.23 ? 627 VAL A CA 1 ATOM 4706 C C . VAL A 1 586 ? 21.003 82.320 36.043 1.00 29.52 ? 627 VAL A C 1 ATOM 4707 O O . VAL A 1 586 ? 22.259 82.343 36.086 1.00 31.86 ? 627 VAL A O 1 ATOM 4708 C CB . VAL A 1 586 ? 20.889 80.858 34.035 1.00 28.78 ? 627 VAL A CB 1 ATOM 4709 C CG1 . VAL A 1 586 ? 20.579 79.579 34.877 1.00 26.68 ? 627 VAL A CG1 1 ATOM 4710 C CG2 . VAL A 1 586 ? 20.444 80.779 32.583 1.00 30.09 ? 627 VAL A CG2 1 ATOM 4711 N N . SER A 1 587 ? 20.203 82.534 37.084 1.00 29.69 ? 628 SER A N 1 ATOM 4712 C CA . SER A 1 587 ? 20.712 82.837 38.427 1.00 30.32 ? 628 SER A CA 1 ATOM 4713 C C . SER A 1 587 ? 20.340 81.730 39.400 1.00 27.67 ? 628 SER A C 1 ATOM 4714 O O . SER A 1 587 ? 19.175 81.272 39.443 1.00 26.90 ? 628 SER A O 1 ATOM 4715 C CB . SER A 1 587 ? 20.076 84.109 38.990 1.00 30.85 ? 628 SER A CB 1 ATOM 4716 O OG . SER A 1 587 ? 20.759 84.387 40.217 1.00 35.88 ? 628 SER A OG 1 ATOM 4717 N N . PHE A 1 588 ? 21.342 81.307 40.173 1.00 27.93 ? 629 PHE A N 1 ATOM 4718 C CA . PHE A 1 588 ? 21.112 80.366 41.266 1.00 26.45 ? 629 PHE A CA 1 ATOM 4719 C C . PHE A 1 588 ? 20.927 81.088 42.606 1.00 26.22 ? 629 PHE A C 1 ATOM 4720 O O . PHE A 1 588 ? 20.823 80.432 43.656 1.00 25.40 ? 629 PHE A O 1 ATOM 4721 C CB . PHE A 1 588 ? 22.274 79.362 41.334 1.00 26.76 ? 629 PHE A CB 1 ATOM 4722 C CG . PHE A 1 588 ? 22.202 78.298 40.270 1.00 26.78 ? 629 PHE A CG 1 ATOM 4723 C CD1 . PHE A 1 588 ? 21.667 77.040 40.556 1.00 26.42 ? 629 PHE A CD1 1 ATOM 4724 C CD2 . PHE A 1 588 ? 22.630 78.566 38.974 1.00 28.20 ? 629 PHE A CD2 1 ATOM 4725 C CE1 . PHE A 1 588 ? 21.577 76.046 39.571 1.00 26.22 ? 629 PHE A CE1 1 ATOM 4726 C CE2 . PHE A 1 588 ? 22.560 77.590 37.992 1.00 28.34 ? 629 PHE A CE2 1 ATOM 4727 C CZ . PHE A 1 588 ? 22.019 76.307 38.294 1.00 26.23 ? 629 PHE A CZ 1 ATOM 4728 N N . ASP A 1 589 ? 20.832 82.415 42.564 1.00 26.95 ? 630 ASP A N 1 ATOM 4729 C CA . ASP A 1 589 ? 20.732 83.193 43.818 1.00 28.09 ? 630 ASP A CA 1 ATOM 4730 C C . ASP A 1 589 ? 19.567 82.735 44.717 1.00 27.57 ? 630 ASP A C 1 ATOM 4731 O O . ASP A 1 589 ? 19.731 82.607 45.949 1.00 27.73 ? 630 ASP A O 1 ATOM 4732 C CB . ASP A 1 589 ? 20.693 84.709 43.552 1.00 30.05 ? 630 ASP A CB 1 ATOM 4733 C CG . ASP A 1 589 ? 22.048 85.279 43.097 1.00 35.33 ? 630 ASP A CG 1 ATOM 4734 O OD1 . ASP A 1 589 ? 23.100 84.584 43.105 1.00 38.47 ? 630 ASP A OD1 1 ATOM 4735 O OD2 . ASP A 1 589 ? 22.060 86.476 42.733 1.00 39.78 ? 630 ASP A OD2 1 ATOM 4736 N N . SER A 1 590 ? 18.414 82.478 44.112 1.00 25.22 ? 631 SER A N 1 ATOM 4737 C CA . SER A 1 590 ? 17.242 82.025 44.897 1.00 24.71 ? 631 SER A CA 1 ATOM 4738 C C . SER A 1 590 ? 17.501 80.707 45.614 1.00 24.17 ? 631 SER A C 1 ATOM 4739 O O . SER A 1 590 ? 17.064 80.528 46.760 1.00 22.76 ? 631 SER A O 1 ATOM 4740 C CB . SER A 1 590 ? 15.949 81.952 44.053 1.00 26.34 ? 631 SER A CB 1 ATOM 4741 O OG . SER A 1 590 ? 16.084 80.973 43.030 1.00 26.58 ? 631 SER A OG 1 ATOM 4742 N N . LEU A 1 591 ? 18.204 79.778 44.952 1.00 22.66 ? 632 LEU A N 1 ATOM 4743 C CA . LEU A 1 591 ? 18.481 78.482 45.583 1.00 23.05 ? 632 LEU A CA 1 ATOM 4744 C C . LEU A 1 591 ? 19.447 78.626 46.772 1.00 23.15 ? 632 LEU A C 1 ATOM 4745 O O . LEU A 1 591 ? 19.215 78.056 47.855 1.00 22.95 ? 632 LEU A O 1 ATOM 4746 C CB . LEU A 1 591 ? 19.005 77.480 44.555 1.00 23.20 ? 632 LEU A CB 1 ATOM 4747 C CG . LEU A 1 591 ? 19.269 76.086 45.134 1.00 22.16 ? 632 LEU A CG 1 ATOM 4748 C CD1 . LEU A 1 591 ? 18.002 75.426 45.717 1.00 21.24 ? 632 LEU A CD1 1 ATOM 4749 C CD2 . LEU A 1 591 ? 19.751 75.253 43.982 1.00 24.91 ? 632 LEU A CD2 1 ATOM 4750 N N . PHE A 1 592 ? 20.504 79.413 46.579 1.00 23.39 ? 633 PHE A N 1 ATOM 4751 C CA . PHE A 1 592 ? 21.430 79.615 47.687 1.00 24.85 ? 633 PHE A CA 1 ATOM 4752 C C . PHE A 1 592 ? 20.766 80.352 48.831 1.00 24.11 ? 633 PHE A C 1 ATOM 4753 O O . PHE A 1 592 ? 21.054 80.048 49.998 1.00 26.82 ? 633 PHE A O 1 ATOM 4754 C CB . PHE A 1 592 ? 22.668 80.348 47.170 1.00 25.33 ? 633 PHE A CB 1 ATOM 4755 C CG . PHE A 1 592 ? 23.589 79.434 46.421 1.00 27.73 ? 633 PHE A CG 1 ATOM 4756 C CD1 . PHE A 1 592 ? 24.366 78.502 47.111 1.00 29.68 ? 633 PHE A CD1 1 ATOM 4757 C CD2 . PHE A 1 592 ? 23.679 79.488 45.045 1.00 30.34 ? 633 PHE A CD2 1 ATOM 4758 C CE1 . PHE A 1 592 ? 25.227 77.618 46.419 1.00 30.44 ? 633 PHE A CE1 1 ATOM 4759 C CE2 . PHE A 1 592 ? 24.554 78.612 44.336 1.00 31.71 ? 633 PHE A CE2 1 ATOM 4760 C CZ . PHE A 1 592 ? 25.310 77.674 45.034 1.00 30.48 ? 633 PHE A CZ 1 ATOM 4761 N N . SER A 1 593 ? 19.878 81.300 48.521 1.00 23.68 ? 634 SER A N 1 ATOM 4762 C CA . SER A 1 593 ? 19.134 82.019 49.568 1.00 24.28 ? 634 SER A CA 1 ATOM 4763 C C . SER A 1 593 ? 18.273 81.035 50.371 1.00 24.06 ? 634 SER A C 1 ATOM 4764 O O . SER A 1 593 ? 18.217 81.077 51.617 1.00 25.16 ? 634 SER A O 1 ATOM 4765 C CB . SER A 1 593 ? 18.245 83.098 48.929 1.00 25.98 ? 634 SER A CB 1 ATOM 4766 O OG . SER A 1 593 ? 17.463 83.758 49.920 1.00 27.77 ? 634 SER A OG 1 ATOM 4767 N N . ALA A 1 594 ? 17.552 80.166 49.664 1.00 22.38 ? 635 ALA A N 1 ATOM 4768 C CA . ALA A 1 594 ? 16.724 79.158 50.329 1.00 21.72 ? 635 ALA A CA 1 ATOM 4769 C C . ALA A 1 594 ? 17.552 78.252 51.251 1.00 22.79 ? 635 ALA A C 1 ATOM 4770 O O . ALA A 1 594 ? 17.147 77.959 52.421 1.00 23.50 ? 635 ALA A O 1 ATOM 4771 C CB . ALA A 1 594 ? 15.955 78.311 49.292 1.00 21.11 ? 635 ALA A CB 1 ATOM 4772 N N . VAL A 1 595 ? 18.717 77.831 50.756 1.00 23.38 ? 636 VAL A N 1 ATOM 4773 C CA . VAL A 1 595 ? 19.605 76.939 51.528 1.00 23.52 ? 636 VAL A CA 1 ATOM 4774 C C . VAL A 1 595 ? 20.122 77.699 52.759 1.00 25.00 ? 636 VAL A C 1 ATOM 4775 O O . VAL A 1 595 ? 20.181 77.139 53.852 1.00 25.40 ? 636 VAL A O 1 ATOM 4776 C CB . VAL A 1 595 ? 20.757 76.421 50.662 1.00 23.99 ? 636 VAL A CB 1 ATOM 4777 C CG1 . VAL A 1 595 ? 21.742 75.645 51.515 1.00 26.75 ? 636 VAL A CG1 1 ATOM 4778 C CG2 . VAL A 1 595 ? 20.171 75.458 49.619 1.00 22.97 ? 636 VAL A CG2 1 ATOM 4779 N N . LYS A 1 596 ? 20.513 78.959 52.560 1.00 26.15 ? 637 LYS A N 1 ATOM 4780 C CA . LYS A 1 596 ? 20.923 79.803 53.711 1.00 26.94 ? 637 LYS A CA 1 ATOM 4781 C C . LYS A 1 596 ? 19.815 79.915 54.754 1.00 26.47 ? 637 LYS A C 1 ATOM 4782 O O . LYS A 1 596 ? 20.059 79.770 55.976 1.00 26.65 ? 637 LYS A O 1 ATOM 4783 C CB . LYS A 1 596 ? 21.319 81.199 53.195 1.00 28.33 ? 637 LYS A CB 1 ATOM 4784 C CG . LYS A 1 596 ? 21.777 82.180 54.286 1.00 33.34 ? 637 LYS A CG 1 ATOM 4785 C CD . LYS A 1 596 ? 22.196 83.515 53.655 1.00 39.15 ? 637 LYS A CD 1 ATOM 4786 C CE . LYS A 1 596 ? 22.597 84.535 54.744 1.00 43.39 ? 637 LYS A CE 1 ATOM 4787 N NZ . LYS A 1 596 ? 21.346 84.984 55.454 1.00 46.41 ? 637 LYS A NZ 1 ATOM 4788 N N . ASN A 1 597 ? 18.581 80.153 54.297 1.00 25.22 ? 638 ASN A N 1 ATOM 4789 C CA . ASN A 1 597 ? 17.468 80.232 55.217 1.00 25.72 ? 638 ASN A CA 1 ATOM 4790 C C . ASN A 1 597 ? 17.213 78.912 55.934 1.00 25.23 ? 638 ASN A C 1 ATOM 4791 O O . ASN A 1 597 ? 16.895 78.899 57.121 1.00 25.74 ? 638 ASN A O 1 ATOM 4792 C CB . ASN A 1 597 ? 16.186 80.687 54.491 1.00 24.96 ? 638 ASN A CB 1 ATOM 4793 C CG . ASN A 1 597 ? 16.250 82.135 54.059 1.00 25.31 ? 638 ASN A CG 1 ATOM 4794 O OD1 . ASN A 1 597 ? 17.148 82.901 54.464 1.00 27.31 ? 638 ASN A OD1 1 ATOM 4795 N ND2 . ASN A 1 597 ? 15.282 82.539 53.235 1.00 25.10 ? 638 ASN A ND2 1 ATOM 4796 N N . PHE A 1 598 ? 17.316 77.798 55.199 1.00 23.65 ? 639 PHE A N 1 ATOM 4797 C CA . PHE A 1 598 ? 17.131 76.496 55.783 1.00 23.26 ? 639 PHE A CA 1 ATOM 4798 C C . PHE A 1 598 ? 18.163 76.317 56.893 1.00 24.66 ? 639 PHE A C 1 ATOM 4799 O O . PHE A 1 598 ? 17.819 75.831 57.983 1.00 24.59 ? 639 PHE A O 1 ATOM 4800 C CB . PHE A 1 598 ? 17.291 75.381 54.724 1.00 23.27 ? 639 PHE A CB 1 ATOM 4801 C CG . PHE A 1 598 ? 16.868 74.035 55.212 1.00 21.87 ? 639 PHE A CG 1 ATOM 4802 C CD1 . PHE A 1 598 ? 15.655 73.487 54.787 1.00 22.87 ? 639 PHE A CD1 1 ATOM 4803 C CD2 . PHE A 1 598 ? 17.680 73.295 56.077 1.00 20.22 ? 639 PHE A CD2 1 ATOM 4804 C CE1 . PHE A 1 598 ? 15.246 72.238 55.226 1.00 23.59 ? 639 PHE A CE1 1 ATOM 4805 C CE2 . PHE A 1 598 ? 17.292 72.033 56.521 1.00 22.88 ? 639 PHE A CE2 1 ATOM 4806 C CZ . PHE A 1 598 ? 16.059 71.489 56.092 1.00 22.33 ? 639 PHE A CZ 1 ATOM 4807 N N . THR A 1 599 ? 19.412 76.692 56.612 1.00 24.83 ? 640 THR A N 1 ATOM 4808 C CA . THR A 1 599 ? 20.518 76.553 57.603 1.00 26.70 ? 640 THR A CA 1 ATOM 4809 C C . THR A 1 599 ? 20.218 77.327 58.872 1.00 28.38 ? 640 THR A C 1 ATOM 4810 O O . THR A 1 599 ? 20.340 76.776 59.998 1.00 28.07 ? 640 THR A O 1 ATOM 4811 C CB . THR A 1 599 ? 21.821 76.998 56.966 1.00 27.65 ? 640 THR A CB 1 ATOM 4812 O OG1 . THR A 1 599 ? 22.018 76.213 55.769 1.00 27.46 ? 640 THR A OG1 1 ATOM 4813 C CG2 . THR A 1 599 ? 23.012 76.717 57.903 1.00 29.22 ? 640 THR A CG2 1 ATOM 4814 N N . GLU A 1 600 ? 19.801 78.584 58.697 1.00 27.45 ? 641 GLU A N 1 ATOM 4815 C CA . GLU A 1 600 ? 19.455 79.458 59.824 1.00 29.76 ? 641 GLU A CA 1 ATOM 4816 C C . GLU A 1 600 ? 18.247 78.924 60.640 1.00 28.50 ? 641 GLU A C 1 ATOM 4817 O O . GLU A 1 600 ? 18.297 78.832 61.895 1.00 28.96 ? 641 GLU A O 1 ATOM 4818 C CB . GLU A 1 600 ? 19.250 80.901 59.309 1.00 30.44 ? 641 GLU A CB 1 ATOM 4819 C CG . GLU A 1 600 ? 20.604 81.542 58.872 1.00 37.77 ? 641 GLU A CG 1 ATOM 4820 C CD . GLU A 1 600 ? 20.447 82.905 58.193 1.00 43.70 ? 641 GLU A CD 1 ATOM 4821 O OE1 . GLU A 1 600 ? 21.476 83.456 57.734 1.00 48.10 ? 641 GLU A OE1 1 ATOM 4822 O OE2 . GLU A 1 600 ? 19.309 83.414 58.113 1.00 48.88 ? 641 GLU A OE2 1 ATOM 4823 N N . ILE A 1 601 ? 17.170 78.547 59.944 1.00 27.14 ? 642 ILE A N 1 ATOM 4824 C CA . ILE A 1 601 ? 15.970 78.104 60.618 1.00 26.51 ? 642 ILE A CA 1 ATOM 4825 C C . ILE A 1 601 ? 16.200 76.760 61.298 1.00 26.09 ? 642 ILE A C 1 ATOM 4826 O O . ILE A 1 601 ? 15.714 76.531 62.384 1.00 27.77 ? 642 ILE A O 1 ATOM 4827 C CB . ILE A 1 601 ? 14.748 78.054 59.644 1.00 26.18 ? 642 ILE A CB 1 ATOM 4828 C CG1 . ILE A 1 601 ? 14.422 79.473 59.225 1.00 26.27 ? 642 ILE A CG1 1 ATOM 4829 C CG2 . ILE A 1 601 ? 13.542 77.380 60.309 1.00 26.36 ? 642 ILE A CG2 1 ATOM 4830 C CD1 . ILE A 1 601 ? 13.476 79.525 57.976 1.00 27.77 ? 642 ILE A CD1 1 ATOM 4831 N N . ALA A 1 602 ? 16.944 75.859 60.661 1.00 25.47 ? 643 ALA A N 1 ATOM 4832 C CA . ALA A 1 602 ? 17.238 74.543 61.271 1.00 26.41 ? 643 ALA A CA 1 ATOM 4833 C C . ALA A 1 602 ? 18.078 74.728 62.546 1.00 27.78 ? 643 ALA A C 1 ATOM 4834 O O . ALA A 1 602 ? 17.869 74.028 63.536 1.00 27.36 ? 643 ALA A O 1 ATOM 4835 C CB . ALA A 1 602 ? 17.993 73.679 60.299 1.00 27.54 ? 643 ALA A CB 1 ATOM 4836 N N . SER A 1 603 ? 18.998 75.679 62.519 1.00 28.53 ? 644 SER A N 1 ATOM 4837 C CA . SER A 1 603 ? 19.807 75.937 63.710 1.00 31.02 ? 644 SER A CA 1 ATOM 4838 C C . SER A 1 603 ? 18.927 76.413 64.866 1.00 30.64 ? 644 SER A C 1 ATOM 4839 O O . SER A 1 603 ? 19.119 75.990 66.029 1.00 32.38 ? 644 SER A O 1 ATOM 4840 C CB . SER A 1 603 ? 20.918 76.922 63.407 1.00 32.23 ? 644 SER A CB 1 ATOM 4841 O OG . SER A 1 603 ? 21.626 77.234 64.616 1.00 39.28 ? 644 SER A OG 1 ATOM 4842 N N . LYS A 1 604 ? 17.980 77.282 64.577 1.00 29.95 ? 645 LYS A N 1 ATOM 4843 C CA . LYS A 1 604 ? 17.099 77.786 65.624 1.00 31.33 ? 645 LYS A CA 1 ATOM 4844 C C . LYS A 1 604 ? 16.167 76.691 66.136 1.00 30.13 ? 645 LYS A C 1 ATOM 4845 O O . LYS A 1 604 ? 15.931 76.579 67.334 1.00 29.98 ? 645 LYS A O 1 ATOM 4846 C CB . LYS A 1 604 ? 16.320 79.010 65.154 1.00 32.26 ? 645 LYS A CB 1 ATOM 4847 C CG A LYS A 1 604 ? 17.210 80.226 64.856 0.50 35.42 ? 645 LYS A CG 1 ATOM 4848 C CG B LYS A 1 604 ? 17.175 80.283 65.031 0.50 34.58 ? 645 LYS A CG 1 ATOM 4849 C CD A LYS A 1 604 ? 16.406 81.514 64.914 0.50 40.25 ? 645 LYS A CD 1 ATOM 4850 C CD B LYS A 1 604 ? 17.686 80.751 66.387 0.50 37.68 ? 645 LYS A CD 1 ATOM 4851 C CE A LYS A 1 604 ? 17.294 82.761 64.883 0.50 43.37 ? 645 LYS A CE 1 ATOM 4852 C CE B LYS A 1 604 ? 18.435 82.075 66.294 0.50 41.50 ? 645 LYS A CE 1 ATOM 4853 N NZ A LYS A 1 604 ? 17.387 83.376 63.516 0.50 43.19 ? 645 LYS A NZ 1 ATOM 4854 N NZ B LYS A 1 604 ? 19.167 82.337 67.565 0.50 44.94 ? 645 LYS A NZ 1 ATOM 4855 N N . PHE A 1 605 ? 15.655 75.852 65.225 1.00 26.89 ? 646 PHE A N 1 ATOM 4856 C CA . PHE A 1 605 ? 14.799 74.764 65.628 1.00 26.59 ? 646 PHE A CA 1 ATOM 4857 C C . PHE A 1 605 ? 15.575 73.807 66.549 1.00 27.71 ? 646 PHE A C 1 ATOM 4858 O O . PHE A 1 605 ? 15.040 73.324 67.552 1.00 29.76 ? 646 PHE A O 1 ATOM 4859 C CB . PHE A 1 605 ? 14.312 74.017 64.355 1.00 26.29 ? 646 PHE A CB 1 ATOM 4860 C CG . PHE A 1 605 ? 13.532 72.791 64.655 1.00 26.39 ? 646 PHE A CG 1 ATOM 4861 C CD1 . PHE A 1 605 ? 12.170 72.879 64.873 1.00 26.49 ? 646 PHE A CD1 1 ATOM 4862 C CD2 . PHE A 1 605 ? 14.178 71.545 64.761 1.00 28.14 ? 646 PHE A CD2 1 ATOM 4863 C CE1 . PHE A 1 605 ? 11.417 71.738 65.188 1.00 29.25 ? 646 PHE A CE1 1 ATOM 4864 C CE2 . PHE A 1 605 ? 13.423 70.368 65.071 1.00 29.93 ? 646 PHE A CE2 1 ATOM 4865 C CZ . PHE A 1 605 ? 12.045 70.488 65.274 1.00 25.68 ? 646 PHE A CZ 1 ATOM 4866 N N . SER A 1 606 ? 16.835 73.535 66.209 1.00 28.37 ? 647 SER A N 1 ATOM 4867 C CA . SER A 1 606 ? 17.660 72.639 67.012 1.00 29.63 ? 647 SER A CA 1 ATOM 4868 C C . SER A 1 606 ? 17.845 73.190 68.439 1.00 31.52 ? 647 SER A C 1 ATOM 4869 O O . SER A 1 606 ? 17.799 72.406 69.388 1.00 32.65 ? 647 SER A O 1 ATOM 4870 C CB . SER A 1 606 ? 19.038 72.439 66.391 1.00 29.96 ? 647 SER A CB 1 ATOM 4871 O OG A SER A 1 606 ? 18.928 71.799 65.131 0.50 30.80 ? 647 SER A OG 1 ATOM 4872 O OG B SER A 1 606 ? 19.671 71.338 67.011 0.50 32.28 ? 647 SER A OG 1 ATOM 4873 N N . GLU A 1 607 ? 18.031 74.500 68.547 1.00 31.98 ? 648 GLU A N 1 ATOM 4874 C CA . GLU A 1 607 ? 18.107 75.181 69.861 1.00 34.61 ? 648 GLU A CA 1 ATOM 4875 C C . GLU A 1 607 ? 16.819 74.954 70.646 1.00 34.47 ? 648 GLU A C 1 ATOM 4876 O O . GLU A 1 607 ? 16.873 74.587 71.850 1.00 35.01 ? 648 GLU A O 1 ATOM 4877 C CB . GLU A 1 607 ? 18.348 76.676 69.702 1.00 37.37 ? 648 GLU A CB 1 ATOM 4878 C CG . GLU A 1 607 ? 19.682 77.031 69.066 1.00 42.76 ? 648 GLU A CG 1 ATOM 4879 C CD . GLU A 1 607 ? 19.938 78.544 68.943 1.00 51.41 ? 648 GLU A CD 1 ATOM 4880 O OE1 . GLU A 1 607 ? 19.065 79.395 69.282 1.00 53.54 ? 648 GLU A OE1 1 ATOM 4881 O OE2 . GLU A 1 607 ? 21.050 78.882 68.489 1.00 56.64 ? 648 GLU A OE2 1 ATOM 4882 N N . ARG A 1 608 ? 15.655 75.136 69.986 1.00 32.39 ? 649 ARG A N 1 ATOM 4883 C CA . ARG A 1 608 ? 14.389 74.933 70.692 1.00 32.69 ? 649 ARG A CA 1 ATOM 4884 C C . ARG A 1 608 ? 14.211 73.479 71.082 1.00 32.83 ? 649 ARG A C 1 ATOM 4885 O O . ARG A 1 608 ? 13.655 73.179 72.117 1.00 34.15 ? 649 ARG A O 1 ATOM 4886 C CB . ARG A 1 608 ? 13.177 75.399 69.873 1.00 31.42 ? 649 ARG A CB 1 ATOM 4887 C CG . ARG A 1 608 ? 13.158 76.890 69.582 1.00 33.91 ? 649 ARG A CG 1 ATOM 4888 C CD . ARG A 1 608 ? 11.786 77.403 69.137 1.00 32.23 ? 649 ARG A CD 1 ATOM 4889 N NE . ARG A 1 608 ? 11.268 76.646 67.982 1.00 29.36 ? 649 ARG A NE 1 ATOM 4890 C CZ . ARG A 1 608 ? 11.637 76.857 66.723 1.00 31.20 ? 649 ARG A CZ 1 ATOM 4891 N NH1 . ARG A 1 608 ? 12.564 77.776 66.445 1.00 30.58 ? 649 ARG A NH1 1 ATOM 4892 N NH2 . ARG A 1 608 ? 11.084 76.139 65.740 1.00 29.48 ? 649 ARG A NH2 1 ATOM 4893 N N . LEU A 1 609 ? 14.682 72.559 70.240 1.00 32.85 ? 650 LEU A N 1 ATOM 4894 C CA . LEU A 1 609 ? 14.513 71.157 70.503 1.00 34.29 ? 650 LEU A CA 1 ATOM 4895 C C . LEU A 1 609 ? 15.322 70.741 71.731 1.00 37.50 ? 650 LEU A C 1 ATOM 4896 O O . LEU A 1 609 ? 14.916 69.843 72.473 1.00 37.55 ? 650 LEU A O 1 ATOM 4897 C CB . LEU A 1 609 ? 14.934 70.339 69.260 1.00 35.97 ? 650 LEU A CB 1 ATOM 4898 C CG . LEU A 1 609 ? 14.441 68.894 69.185 1.00 35.76 ? 650 LEU A CG 1 ATOM 4899 C CD1 . LEU A 1 609 ? 12.966 68.793 68.930 1.00 34.17 ? 650 LEU A CD1 1 ATOM 4900 C CD2 . LEU A 1 609 ? 15.274 68.142 68.097 1.00 39.01 ? 650 LEU A CD2 1 ATOM 4901 N N . GLN A 1 610 ? 16.448 71.402 71.931 1.00 39.63 ? 651 GLN A N 1 ATOM 4902 C CA . GLN A 1 610 ? 17.318 70.985 73.007 1.00 43.39 ? 651 GLN A CA 1 ATOM 4903 C C . GLN A 1 610 ? 16.796 71.576 74.295 1.00 44.46 ? 651 GLN A C 1 ATOM 4904 O O . GLN A 1 610 ? 16.927 70.916 75.340 1.00 47.17 ? 651 GLN A O 1 ATOM 4905 C CB A GLN A 1 610 ? 18.785 71.304 72.719 0.65 44.11 ? 651 GLN A CB 1 ATOM 4906 C CB B GLN A 1 610 ? 18.770 71.442 72.751 0.35 43.51 ? 651 GLN A CB 1 ATOM 4907 C CG A GLN A 1 610 ? 19.348 70.408 71.620 0.65 47.27 ? 651 GLN A CG 1 ATOM 4908 C CG B GLN A 1 610 ? 19.073 72.885 73.174 0.35 44.95 ? 651 GLN A CG 1 ATOM 4909 C CD A GLN A 1 610 ? 20.833 70.595 71.407 0.65 51.02 ? 651 GLN A CD 1 ATOM 4910 C CD B GLN A 1 610 ? 20.365 73.441 72.595 0.35 47.62 ? 651 GLN A CD 1 ATOM 4911 O OE1 A GLN A 1 610 ? 21.565 70.954 72.333 0.65 55.15 ? 651 GLN A OE1 1 ATOM 4912 O OE1 B GLN A 1 610 ? 20.950 72.866 71.676 0.35 45.65 ? 651 GLN A OE1 1 ATOM 4913 N NE2 A GLN A 1 610 ? 21.289 70.354 70.177 0.65 52.39 ? 651 GLN A NE2 1 ATOM 4914 N NE2 B GLN A 1 610 ? 20.808 74.579 73.127 0.35 48.56 ? 651 GLN A NE2 1 ATOM 4915 N N . ASP A 1 611 ? 16.162 72.759 74.185 1.00 44.73 ? 652 ASP A N 1 ATOM 4916 C CA . ASP A 1 611 ? 15.773 73.692 75.269 1.00 46.43 ? 652 ASP A CA 1 ATOM 4917 C C . ASP A 1 611 ? 14.298 73.708 75.624 1.00 44.52 ? 652 ASP A C 1 ATOM 4918 O O . ASP A 1 611 ? 13.899 74.463 76.512 1.00 46.18 ? 652 ASP A O 1 ATOM 4919 C CB . ASP A 1 611 ? 16.021 75.144 74.820 1.00 47.78 ? 652 ASP A CB 1 ATOM 4920 C CG . ASP A 1 611 ? 17.453 75.625 75.040 1.00 53.55 ? 652 ASP A CG 1 ATOM 4921 O OD1 . ASP A 1 611 ? 17.672 76.839 74.787 1.00 61.43 ? 652 ASP A OD1 1 ATOM 4922 O OD2 . ASP A 1 611 ? 18.335 74.836 75.460 1.00 58.91 ? 652 ASP A OD2 1 ATOM 4923 N N . PHE A 1 612 ? 13.456 72.968 74.906 1.00 42.39 ? 653 PHE A N 1 ATOM 4924 C CA . PHE A 1 612 ? 12.024 73.133 75.164 1.00 40.04 ? 653 PHE A CA 1 ATOM 4925 C C . PHE A 1 612 ? 11.700 72.457 76.444 1.00 39.01 ? 653 PHE A C 1 ATOM 4926 O O . PHE A 1 612 ? 12.453 71.595 76.908 1.00 41.45 ? 653 PHE A O 1 ATOM 4927 C CB . PHE A 1 612 ? 11.123 72.585 74.061 1.00 39.63 ? 653 PHE A CB 1 ATOM 4928 C CG . PHE A 1 612 ? 11.020 71.060 73.999 1.00 37.74 ? 653 PHE A CG 1 ATOM 4929 C CD1 . PHE A 1 612 ? 9.930 70.410 74.569 1.00 36.86 ? 653 PHE A CD1 1 ATOM 4930 C CD2 . PHE A 1 612 ? 11.922 70.329 73.250 1.00 38.62 ? 653 PHE A CD2 1 ATOM 4931 C CE1 . PHE A 1 612 ? 9.742 69.073 74.431 1.00 40.19 ? 653 PHE A CE1 1 ATOM 4932 C CE2 . PHE A 1 612 ? 11.768 68.953 73.089 1.00 42.01 ? 653 PHE A CE2 1 ATOM 4933 C CZ . PHE A 1 612 ? 10.679 68.315 73.674 1.00 45.02 ? 653 PHE A CZ 1 ATOM 4934 N N . ASP A 1 613 ? 10.574 72.870 77.001 0.50 35.10 ? 654 ASP A N 1 ATOM 4935 C CA . ASP A 1 613 ? 10.121 72.315 78.240 0.50 33.44 ? 654 ASP A CA 1 ATOM 4936 C C . ASP A 1 613 ? 9.804 70.833 78.085 0.50 30.49 ? 654 ASP A C 1 ATOM 4937 O O . ASP A 1 613 ? 8.852 70.468 77.434 0.50 30.96 ? 654 ASP A O 1 ATOM 4938 C CB . ASP A 1 613 ? 8.916 73.105 78.742 0.50 31.50 ? 654 ASP A CB 1 ATOM 4939 C CG . ASP A 1 613 ? 8.381 72.557 80.026 0.50 33.41 ? 654 ASP A CG 1 ATOM 4940 O OD1 . ASP A 1 613 ? 8.781 71.403 80.307 0.50 32.48 ? 654 ASP A OD1 1 ATOM 4941 O OD2 . ASP A 1 613 ? 7.608 73.285 80.721 0.50 33.00 ? 654 ASP A OD2 1 ATOM 4942 N N . LYS A 1 614 ? 10.578 69.990 78.743 0.50 31.65 ? 655 LYS A N 1 ATOM 4943 C CA . LYS A 1 614 ? 10.522 68.535 78.581 0.50 33.33 ? 655 LYS A CA 1 ATOM 4944 C C . LYS A 1 614 ? 9.332 67.696 79.179 0.50 33.61 ? 655 LYS A C 1 ATOM 4945 O O . LYS A 1 614 ? 9.264 66.563 78.874 0.50 32.76 ? 655 LYS A O 1 ATOM 4946 C CB . LYS A 1 614 ? 11.893 67.935 79.064 0.50 34.51 ? 655 LYS A CB 1 ATOM 4947 C CG . LYS A 1 614 ? 13.102 68.407 78.235 0.50 36.81 ? 655 LYS A CG 1 ATOM 4948 C CD . LYS A 1 614 ? 14.432 68.022 78.836 0.50 42.54 ? 655 LYS A CD 1 ATOM 4949 C CE . LYS A 1 614 ? 15.599 68.271 77.865 0.50 42.31 ? 655 LYS A CE 1 ATOM 4950 N NZ . LYS A 1 614 ? 16.945 68.132 78.579 0.50 45.59 ? 655 LYS A NZ 1 ATOM 4951 N N A SER A 1 615 ? 8.800 68.344 80.246 0.50 33.15 ? 656 SER A N 1 ATOM 4952 N N B SER A 1 615 ? 8.241 68.040 79.888 0.50 36.83 ? 656 SER A N 1 ATOM 4953 C CA A SER A 1 615 ? 7.530 68.023 80.834 0.50 31.61 ? 656 SER A CA 1 ATOM 4954 C CA B SER A 1 615 ? 7.303 66.759 80.067 0.50 36.04 ? 656 SER A CA 1 ATOM 4955 C C A SER A 1 615 ? 6.337 68.247 79.857 0.50 29.20 ? 656 SER A C 1 ATOM 4956 C C B SER A 1 615 ? 5.829 66.705 79.519 0.50 34.15 ? 656 SER A C 1 ATOM 4957 O O A SER A 1 615 ? 5.243 67.798 80.162 0.50 31.03 ? 656 SER A O 1 ATOM 4958 O O B SER A 1 615 ? 4.904 66.021 80.035 0.50 33.04 ? 656 SER A O 1 ATOM 4959 C CB A SER A 1 615 ? 7.353 68.819 82.131 0.50 30.50 ? 656 SER A CB 1 ATOM 4960 C CB B SER A 1 615 ? 7.210 66.269 81.524 0.50 35.95 ? 656 SER A CB 1 ATOM 4961 O OG A SER A 1 615 ? 7.139 70.177 81.850 0.50 31.97 ? 656 SER A OG 1 ATOM 4962 O OG B SER A 1 615 ? 5.877 66.548 81.990 0.50 36.90 ? 656 SER A OG 1 ATOM 4963 N N A ASN A 1 616 ? 6.516 68.913 78.705 0.50 28.65 ? 657 ASN A N 1 ATOM 4964 N N B ASN A 1 616 ? 5.623 67.443 78.484 0.50 31.19 ? 657 ASN A N 1 ATOM 4965 C CA A ASN A 1 616 ? 5.367 69.229 77.810 0.50 27.20 ? 657 ASN A CA 1 ATOM 4966 C CA B ASN A 1 616 ? 4.301 67.886 78.145 0.50 31.44 ? 657 ASN A CA 1 ATOM 4967 C C A ASN A 1 616 ? 5.256 68.335 76.586 0.50 26.55 ? 657 ASN A C 1 ATOM 4968 C C B ASN A 1 616 ? 3.844 67.119 76.892 0.50 30.59 ? 657 ASN A C 1 ATOM 4969 O O A ASN A 1 616 ? 6.045 68.455 75.623 0.50 26.38 ? 657 ASN A O 1 ATOM 4970 O O B ASN A 1 616 ? 4.356 67.338 75.826 0.50 30.05 ? 657 ASN A O 1 ATOM 4971 C CB A ASN A 1 616 ? 5.385 70.688 77.375 0.50 27.09 ? 657 ASN A CB 1 ATOM 4972 C CB B ASN A 1 616 ? 4.467 69.379 77.916 0.50 31.07 ? 657 ASN A CB 1 ATOM 4973 C CG A ASN A 1 616 ? 4.048 71.137 76.813 0.50 27.38 ? 657 ASN A CG 1 ATOM 4974 C CG B ASN A 1 616 ? 3.208 70.056 77.492 0.50 32.02 ? 657 ASN A CG 1 ATOM 4975 O OD1 A ASN A 1 616 ? 3.377 70.389 76.108 0.50 24.94 ? 657 ASN A OD1 1 ATOM 4976 O OD1 B ASN A 1 616 ? 2.429 69.508 76.716 0.50 34.98 ? 657 ASN A OD1 1 ATOM 4977 N ND2 A ASN A 1 616 ? 3.655 72.369 77.122 0.50 31.64 ? 657 ASN A ND2 1 ATOM 4978 N ND2 B ASN A 1 616 ? 3.038 71.280 77.938 0.50 34.07 ? 657 ASN A ND2 1 ATOM 4979 N N A PRO A 1 617 ? 4.300 67.393 76.621 0.50 25.17 ? 658 PRO A N 1 ATOM 4980 N N B PRO A 1 617 ? 2.893 66.173 77.041 0.50 30.65 ? 658 PRO A N 1 ATOM 4981 C CA A PRO A 1 617 ? 4.204 66.382 75.582 0.50 24.71 ? 658 PRO A CA 1 ATOM 4982 C CA B PRO A 1 617 ? 2.493 65.340 75.894 0.50 29.27 ? 658 PRO A CA 1 ATOM 4983 C C A PRO A 1 617 ? 3.680 66.964 74.262 0.50 23.18 ? 658 PRO A C 1 ATOM 4984 C C B PRO A 1 617 ? 2.215 66.076 74.561 0.50 27.67 ? 658 PRO A C 1 ATOM 4985 O O A PRO A 1 617 ? 3.908 66.336 73.215 0.50 21.45 ? 658 PRO A O 1 ATOM 4986 O O B PRO A 1 617 ? 2.705 65.627 73.512 0.50 26.25 ? 658 PRO A O 1 ATOM 4987 C CB A PRO A 1 617 ? 3.183 65.378 76.150 0.50 24.30 ? 658 PRO A CB 1 ATOM 4988 C CB B PRO A 1 617 ? 1.220 64.653 76.396 0.50 30.28 ? 658 PRO A CB 1 ATOM 4989 C CG A PRO A 1 617 ? 2.295 66.255 77.052 0.50 24.99 ? 658 PRO A CG 1 ATOM 4990 C CG B PRO A 1 617 ? 1.414 64.579 77.903 0.50 31.40 ? 658 PRO A CG 1 ATOM 4991 C CD A PRO A 1 617 ? 3.294 67.215 77.691 0.50 27.66 ? 658 PRO A CD 1 ATOM 4992 C CD B PRO A 1 617 ? 2.187 65.805 78.283 0.50 31.45 ? 658 PRO A CD 1 ATOM 4993 N N A ILE A 1 618 ? 2.955 68.085 74.316 0.50 24.64 ? 659 ILE A N 1 ATOM 4994 N N B ILE A 1 618 ? 1.439 67.155 74.577 0.50 27.96 ? 659 ILE A N 1 ATOM 4995 C CA A ILE A 1 618 ? 2.374 68.710 73.119 0.50 25.06 ? 659 ILE A CA 1 ATOM 4996 C CA B ILE A 1 618 ? 1.138 67.838 73.310 0.50 27.66 ? 659 ILE A CA 1 ATOM 4997 C C A ILE A 1 618 ? 3.469 69.443 72.352 0.50 23.85 ? 659 ILE A C 1 ATOM 4998 C C B ILE A 1 618 ? 2.311 68.642 72.791 0.50 26.23 ? 659 ILE A C 1 ATOM 4999 O O A ILE A 1 618 ? 3.526 69.383 71.136 0.50 23.18 ? 659 ILE A O 1 ATOM 5000 O O B ILE A 1 618 ? 2.560 68.662 71.595 0.50 26.02 ? 659 ILE A O 1 ATOM 5001 C CB A ILE A 1 618 ? 1.243 69.740 73.423 0.50 26.64 ? 659 ILE A CB 1 ATOM 5002 C CB B ILE A 1 618 ? -0.134 68.655 73.328 0.50 27.41 ? 659 ILE A CB 1 ATOM 5003 C CG1 A ILE A 1 618 ? 0.169 69.158 74.352 0.50 30.08 ? 659 ILE A CG1 1 ATOM 5004 C CG1 B ILE A 1 618 ? -1.304 67.695 73.485 0.50 30.23 ? 659 ILE A CG1 1 ATOM 5005 C CG2 A ILE A 1 618 ? 0.641 70.263 72.101 0.50 26.37 ? 659 ILE A CG2 1 ATOM 5006 C CG2 B ILE A 1 618 ? -0.267 69.465 72.047 0.50 30.33 ? 659 ILE A CG2 1 ATOM 5007 C CD1 A ILE A 1 618 ? -0.051 67.704 74.101 0.50 32.43 ? 659 ILE A CD1 1 ATOM 5008 C CD1 B ILE A 1 618 ? -1.045 66.366 72.839 0.50 28.87 ? 659 ILE A CD1 1 ATOM 5009 N N A VAL A 1 619 ? 4.340 70.130 73.077 0.50 23.67 ? 660 VAL A N 1 ATOM 5010 N N B VAL A 1 619 ? 3.049 69.312 73.671 0.50 26.24 ? 660 VAL A N 1 ATOM 5011 C CA A VAL A 1 619 ? 5.489 70.756 72.451 0.50 24.12 ? 660 VAL A CA 1 ATOM 5012 C CA B VAL A 1 619 ? 4.262 70.008 73.174 0.50 24.79 ? 660 VAL A CA 1 ATOM 5013 C C A VAL A 1 619 ? 6.446 69.701 71.890 0.50 23.34 ? 660 VAL A C 1 ATOM 5014 C C B VAL A 1 619 ? 5.281 69.030 72.508 0.50 23.86 ? 660 VAL A C 1 ATOM 5015 O O A VAL A 1 619 ? 6.959 69.831 70.775 0.50 22.40 ? 660 VAL A O 1 ATOM 5016 O O B VAL A 1 619 ? 5.840 69.291 71.416 0.50 23.65 ? 660 VAL A O 1 ATOM 5017 C CB A VAL A 1 619 ? 6.222 71.690 73.417 0.50 24.39 ? 660 VAL A CB 1 ATOM 5018 C CB B VAL A 1 619 ? 4.911 70.891 74.275 0.50 25.93 ? 660 VAL A CB 1 ATOM 5019 C CG1 A VAL A 1 619 ? 7.524 72.169 72.792 0.50 26.10 ? 660 VAL A CG1 1 ATOM 5020 C CG1 B VAL A 1 619 ? 6.244 71.488 73.781 0.50 26.40 ? 660 VAL A CG1 1 ATOM 5021 C CG2 A VAL A 1 619 ? 5.300 72.847 73.842 0.50 27.19 ? 660 VAL A CG2 1 ATOM 5022 C CG2 B VAL A 1 619 ? 3.965 72.021 74.690 0.50 26.86 ? 660 VAL A CG2 1 ATOM 5023 N N A LEU A 1 620 ? 6.700 68.646 72.668 0.50 23.52 ? 661 LEU A N 1 ATOM 5024 N N B LEU A 1 620 ? 5.466 67.853 73.094 0.50 23.22 ? 661 LEU A N 1 ATOM 5025 C CA A LEU A 1 620 ? 7.457 67.489 72.199 0.50 22.02 ? 661 LEU A CA 1 ATOM 5026 C CA B LEU A 1 620 ? 6.357 66.858 72.546 0.50 23.16 ? 661 LEU A CA 1 ATOM 5027 C C A LEU A 1 620 ? 6.875 66.949 70.880 0.50 22.53 ? 661 LEU A C 1 ATOM 5028 C C B LEU A 1 620 ? 5.796 66.367 71.233 0.50 21.99 ? 661 LEU A C 1 ATOM 5029 O O A LEU A 1 620 ? 7.589 66.851 69.897 0.50 20.23 ? 661 LEU A O 1 ATOM 5030 O O B LEU A 1 620 ? 6.528 66.078 70.273 0.50 22.14 ? 661 LEU A O 1 ATOM 5031 C CB A LEU A 1 620 ? 7.496 66.444 73.336 0.50 23.78 ? 661 LEU A CB 1 ATOM 5032 C CB B LEU A 1 620 ? 6.492 65.664 73.498 0.50 22.16 ? 661 LEU A CB 1 ATOM 5033 C CG A LEU A 1 620 ? 8.068 65.068 72.990 0.50 22.70 ? 661 LEU A CG 1 ATOM 5034 C CG B LEU A 1 620 ? 7.366 64.494 72.958 0.50 25.49 ? 661 LEU A CG 1 ATOM 5035 C CD1 A LEU A 1 620 ? 9.470 65.117 72.395 0.50 23.03 ? 661 LEU A CD1 1 ATOM 5036 C CD1 B LEU A 1 620 ? 8.743 64.956 72.479 0.50 25.49 ? 661 LEU A CD1 1 ATOM 5037 C CD2 A LEU A 1 620 ? 8.008 64.176 74.215 0.50 23.52 ? 661 LEU A CD2 1 ATOM 5038 C CD2 B LEU A 1 620 ? 7.499 63.381 74.014 0.50 23.61 ? 661 LEU A CD2 1 ATOM 5039 N N A ARG A 1 621 ? 5.577 66.659 70.854 0.50 22.00 ? 662 ARG A N 1 ATOM 5040 N N B ARG A 1 621 ? 4.482 66.242 71.188 0.50 22.29 ? 662 ARG A N 1 ATOM 5041 C CA A ARG A 1 621 ? 4.984 65.970 69.702 0.50 23.00 ? 662 ARG A CA 1 ATOM 5042 C CA B ARG A 1 621 ? 3.876 65.884 69.902 0.50 22.76 ? 662 ARG A CA 1 ATOM 5043 C C A ARG A 1 621 ? 4.847 66.944 68.603 0.50 23.53 ? 662 ARG A C 1 ATOM 5044 C C B ARG A 1 621 ? 4.192 66.834 68.697 0.50 23.88 ? 662 ARG A C 1 ATOM 5045 O O A ARG A 1 621 ? 5.102 66.595 67.455 0.50 21.86 ? 662 ARG A O 1 ATOM 5046 O O B ARG A 1 621 ? 4.326 66.346 67.587 0.50 22.99 ? 662 ARG A O 1 ATOM 5047 C CB A ARG A 1 621 ? 3.594 65.444 70.026 0.50 22.49 ? 662 ARG A CB 1 ATOM 5048 C CB B ARG A 1 621 ? 2.388 65.584 70.094 0.50 22.34 ? 662 ARG A CB 1 ATOM 5049 C CG A ARG A 1 621 ? 2.787 65.089 68.792 0.50 21.89 ? 662 ARG A CG 1 ATOM 5050 C CG B ARG A 1 621 ? 1.739 65.064 68.842 0.50 21.87 ? 662 ARG A CG 1 ATOM 5051 C CD A ARG A 1 621 ? 3.085 63.681 68.317 0.50 20.21 ? 662 ARG A CD 1 ATOM 5052 C CD B ARG A 1 621 ? 1.783 63.557 68.676 0.50 30.49 ? 662 ARG A CD 1 ATOM 5053 N NE A ARG A 1 621 ? 1.862 63.301 67.629 0.50 21.71 ? 662 ARG A NE 1 ATOM 5054 N NE B ARG A 1 621 ? 0.665 63.178 67.794 0.50 33.11 ? 662 ARG A NE 1 ATOM 5055 C CZ A ARG A 1 621 ? 1.319 62.090 67.608 0.50 21.83 ? 662 ARG A CZ 1 ATOM 5056 C CZ B ARG A 1 621 ? 0.301 61.938 67.507 0.50 30.71 ? 662 ARG A CZ 1 ATOM 5057 N NH1 A ARG A 1 621 ? 1.911 61.017 68.144 0.50 23.81 ? 662 ARG A NH1 1 ATOM 5058 N NH1 B ARG A 1 621 ? 0.987 60.898 67.975 0.50 31.27 ? 662 ARG A NH1 1 ATOM 5059 N NH2 A ARG A 1 621 ? 0.155 61.965 66.995 0.50 23.98 ? 662 ARG A NH2 1 ATOM 5060 N NH2 B ARG A 1 621 ? -0.748 61.749 66.719 0.50 31.89 ? 662 ARG A NH2 1 ATOM 5061 N N . MET A 1 622 ? 4.387 68.154 68.933 1.00 25.79 ? 663 MET A N 1 ATOM 5062 C CA . MET A 1 622 ? 4.487 69.225 67.895 1.00 26.12 ? 663 MET A CA 1 ATOM 5063 C C . MET A 1 622 ? 5.893 69.233 67.286 1.00 27.05 ? 663 MET A C 1 ATOM 5064 O O . MET A 1 622 ? 6.065 69.274 66.058 1.00 25.02 ? 663 MET A O 1 ATOM 5065 C CB A MET A 1 622 ? 4.250 70.617 68.510 0.50 27.18 ? 663 MET A CB 1 ATOM 5066 C CB B MET A 1 622 ? 3.981 70.571 68.472 0.50 27.12 ? 663 MET A CB 1 ATOM 5067 C CG A MET A 1 622 ? 4.819 71.797 67.661 0.50 27.76 ? 663 MET A CG 1 ATOM 5068 C CG B MET A 1 622 ? 2.470 70.516 68.929 0.50 25.63 ? 663 MET A CG 1 ATOM 5069 S SD A MET A 1 622 ? 4.511 73.427 68.404 0.50 25.77 ? 663 MET A SD 1 ATOM 5070 S SD B MET A 1 622 ? 1.562 72.019 69.473 0.50 27.94 ? 663 MET A SD 1 ATOM 5071 C CE A MET A 1 622 ? 3.843 72.916 69.982 0.50 35.59 ? 663 MET A CE 1 ATOM 5072 C CE B MET A 1 622 ? 2.356 72.398 71.110 0.50 20.84 ? 663 MET A CE 1 ATOM 5073 N N . MET A 1 623 ? 6.946 69.158 68.127 1.00 24.99 ? 664 MET A N 1 ATOM 5074 C CA . MET A 1 623 ? 8.293 69.088 67.630 1.00 25.84 ? 664 MET A CA 1 ATOM 5075 C C . MET A 1 623 ? 8.601 67.779 66.875 1.00 25.12 ? 664 MET A C 1 ATOM 5076 O O . MET A 1 623 ? 9.263 67.779 65.841 1.00 25.88 ? 664 MET A O 1 ATOM 5077 C CB A MET A 1 623 ? 9.210 69.097 68.881 0.50 27.32 ? 664 MET A CB 1 ATOM 5078 C CB B MET A 1 623 ? 9.347 69.482 68.682 0.50 26.39 ? 664 MET A CB 1 ATOM 5079 C CG A MET A 1 623 ? 8.845 70.139 69.905 0.50 30.40 ? 664 MET A CG 1 ATOM 5080 C CG B MET A 1 623 ? 9.345 70.961 68.894 0.50 21.45 ? 664 MET A CG 1 ATOM 5081 S SD A MET A 1 623 ? 8.997 71.748 69.145 0.50 32.89 ? 664 MET A SD 1 ATOM 5082 S SD B MET A 1 623 ? 10.734 71.639 69.826 0.50 25.22 ? 664 MET A SD 1 ATOM 5083 C CE A MET A 1 623 ? 10.523 72.313 69.898 0.50 28.87 ? 664 MET A CE 1 ATOM 5084 C CE B MET A 1 623 ? 11.702 72.248 68.438 0.50 21.31 ? 664 MET A CE 1 ATOM 5085 N N . ASN A 1 624 ? 8.086 66.673 67.407 1.00 25.40 ? 665 ASN A N 1 ATOM 5086 C CA . ASN A 1 624 ? 8.287 65.372 66.742 1.00 23.87 ? 665 ASN A CA 1 ATOM 5087 C C . ASN A 1 624 ? 7.556 65.405 65.381 1.00 23.73 ? 665 ASN A C 1 ATOM 5088 O O . ASN A 1 624 ? 8.077 64.864 64.446 1.00 23.45 ? 665 ASN A O 1 ATOM 5089 C CB . ASN A 1 624 ? 7.797 64.211 67.575 1.00 25.83 ? 665 ASN A CB 1 ATOM 5090 C CG . ASN A 1 624 ? 8.880 63.713 68.537 1.00 25.00 ? 665 ASN A CG 1 ATOM 5091 O OD1 . ASN A 1 624 ? 10.079 63.911 68.282 1.00 26.13 ? 665 ASN A OD1 1 ATOM 5092 N ND2 . ASN A 1 624 ? 8.459 63.112 69.648 1.00 25.46 ? 665 ASN A ND2 1 ATOM 5093 N N . ASP A 1 625 ? 6.408 66.044 65.306 1.00 22.96 ? 666 ASP A N 1 ATOM 5094 C CA . ASP A 1 625 ? 5.697 66.153 63.992 1.00 23.19 ? 666 ASP A CA 1 ATOM 5095 C C . ASP A 1 625 ? 6.525 67.018 63.046 1.00 23.19 ? 666 ASP A C 1 ATOM 5096 O O . ASP A 1 625 ? 6.592 66.716 61.854 1.00 23.48 ? 666 ASP A O 1 ATOM 5097 C CB . ASP A 1 625 ? 4.309 66.765 64.201 1.00 23.88 ? 666 ASP A CB 1 ATOM 5098 C CG . ASP A 1 625 ? 3.269 65.742 64.722 1.00 24.16 ? 666 ASP A CG 1 ATOM 5099 O OD1 . ASP A 1 625 ? 3.639 64.542 64.873 1.00 26.56 ? 666 ASP A OD1 1 ATOM 5100 O OD2 . ASP A 1 625 ? 2.089 66.149 64.884 1.00 25.64 ? 666 ASP A OD2 1 ATOM 5101 N N . GLN A 1 626 ? 7.128 68.107 63.526 1.00 21.09 ? 667 GLN A N 1 ATOM 5102 C CA . GLN A 1 626 ? 8.005 68.884 62.638 1.00 21.67 ? 667 GLN A CA 1 ATOM 5103 C C . GLN A 1 626 ? 9.158 68.043 62.114 1.00 21.69 ? 667 GLN A C 1 ATOM 5104 O O . GLN A 1 626 ? 9.531 68.137 60.947 1.00 21.95 ? 667 GLN A O 1 ATOM 5105 C CB . GLN A 1 626 ? 8.527 70.144 63.374 1.00 21.79 ? 667 GLN A CB 1 ATOM 5106 C CG . GLN A 1 626 ? 7.380 71.174 63.559 1.00 21.93 ? 667 GLN A CG 1 ATOM 5107 C CD . GLN A 1 626 ? 7.849 72.406 64.294 1.00 23.66 ? 667 GLN A CD 1 ATOM 5108 O OE1 . GLN A 1 626 ? 7.955 72.382 65.523 1.00 26.46 ? 667 GLN A OE1 1 ATOM 5109 N NE2 . GLN A 1 626 ? 8.077 73.504 63.573 1.00 23.73 ? 667 GLN A NE2 1 ATOM 5110 N N . LEU A 1 627 ? 9.757 67.227 62.987 1.00 23.32 ? 668 LEU A N 1 ATOM 5111 C CA . LEU A 1 627 ? 10.796 66.304 62.535 1.00 22.62 ? 668 LEU A CA 1 ATOM 5112 C C . LEU A 1 627 ? 10.307 65.278 61.502 1.00 21.27 ? 668 LEU A C 1 ATOM 5113 O O . LEU A 1 627 ? 10.980 65.072 60.475 1.00 23.36 ? 668 LEU A O 1 ATOM 5114 C CB . LEU A 1 627 ? 11.411 65.580 63.765 1.00 23.64 ? 668 LEU A CB 1 ATOM 5115 C CG . LEU A 1 627 ? 12.273 66.562 64.591 1.00 26.94 ? 668 LEU A CG 1 ATOM 5116 C CD1 . LEU A 1 627 ? 12.728 65.841 65.872 1.00 30.42 ? 668 LEU A CD1 1 ATOM 5117 C CD2 . LEU A 1 627 ? 13.472 67.099 63.775 1.00 29.55 ? 668 LEU A CD2 1 ATOM 5118 N N . MET A 1 628 ? 9.141 64.709 61.777 1.00 22.09 ? 669 MET A N 1 ATOM 5119 C CA . MET A 1 628 ? 8.598 63.653 60.926 1.00 22.61 ? 669 MET A CA 1 ATOM 5120 C C . MET A 1 628 ? 8.209 64.219 59.569 1.00 21.36 ? 669 MET A C 1 ATOM 5121 O O . MET A 1 628 ? 8.411 63.581 58.539 1.00 22.05 ? 669 MET A O 1 ATOM 5122 C CB . MET A 1 628 ? 7.385 63.039 61.579 1.00 23.02 ? 669 MET A CB 1 ATOM 5123 C CG . MET A 1 628 ? 6.675 61.995 60.660 1.00 25.18 ? 669 MET A CG 1 ATOM 5124 S SD . MET A 1 628 ? 5.273 61.208 61.488 1.00 28.46 ? 669 MET A SD 1 ATOM 5125 C CE . MET A 1 628 ? 4.023 62.514 61.395 1.00 26.07 ? 669 MET A CE 1 ATOM 5126 N N . PHE A 1 629 ? 7.596 65.391 59.582 1.00 21.17 ? 670 PHE A N 1 ATOM 5127 C CA . PHE A 1 629 ? 7.133 65.988 58.289 1.00 21.11 ? 670 PHE A CA 1 ATOM 5128 C C . PHE A 1 629 ? 8.194 66.749 57.546 1.00 21.31 ? 670 PHE A C 1 ATOM 5129 O O . PHE A 1 629 ? 7.917 67.260 56.435 1.00 20.35 ? 670 PHE A O 1 ATOM 5130 C CB . PHE A 1 629 ? 5.896 66.858 58.493 1.00 20.42 ? 670 PHE A CB 1 ATOM 5131 C CG . PHE A 1 629 ? 4.652 66.082 58.833 1.00 21.28 ? 670 PHE A CG 1 ATOM 5132 C CD1 . PHE A 1 629 ? 4.103 65.154 57.914 1.00 21.56 ? 670 PHE A CD1 1 ATOM 5133 C CD2 . PHE A 1 629 ? 3.957 66.310 60.029 1.00 22.50 ? 670 PHE A CD2 1 ATOM 5134 C CE1 . PHE A 1 629 ? 2.966 64.441 58.212 1.00 23.63 ? 670 PHE A CE1 1 ATOM 5135 C CE2 . PHE A 1 629 ? 2.781 65.615 60.332 1.00 25.18 ? 670 PHE A CE2 1 ATOM 5136 C CZ . PHE A 1 629 ? 2.273 64.652 59.404 1.00 23.43 ? 670 PHE A CZ 1 ATOM 5137 N N . LEU A 1 630 ? 9.420 66.821 58.073 1.00 21.01 ? 671 LEU A N 1 ATOM 5138 C CA . LEU A 1 630 ? 10.487 67.515 57.358 1.00 20.17 ? 671 LEU A CA 1 ATOM 5139 C C . LEU A 1 630 ? 10.862 66.782 56.053 1.00 19.91 ? 671 LEU A C 1 ATOM 5140 O O . LEU A 1 630 ? 10.903 67.409 54.983 1.00 20.13 ? 671 LEU A O 1 ATOM 5141 C CB . LEU A 1 630 ? 11.742 67.708 58.274 1.00 21.58 ? 671 LEU A CB 1 ATOM 5142 C CG . LEU A 1 630 ? 12.892 68.417 57.589 1.00 22.68 ? 671 LEU A CG 1 ATOM 5143 C CD1 . LEU A 1 630 ? 12.489 69.799 57.064 1.00 24.60 ? 671 LEU A CD1 1 ATOM 5144 C CD2 . LEU A 1 630 ? 14.106 68.546 58.588 1.00 24.34 ? 671 LEU A CD2 1 ATOM 5145 N N . GLU A 1 631 ? 11.105 65.463 56.110 1.00 18.55 ? 672 GLU A N 1 ATOM 5146 C CA . GLU A 1 631 ? 11.333 64.735 54.849 1.00 18.76 ? 672 GLU A CA 1 ATOM 5147 C C . GLU A 1 631 ? 10.107 64.923 53.926 1.00 17.64 ? 672 GLU A C 1 ATOM 5148 O O . GLU A 1 631 ? 10.273 65.091 52.678 1.00 19.11 ? 672 GLU A O 1 ATOM 5149 C CB . GLU A 1 631 ? 11.519 63.235 55.102 1.00 18.84 ? 672 GLU A CB 1 ATOM 5150 C CG . GLU A 1 631 ? 12.101 62.556 53.874 1.00 18.50 ? 672 GLU A CG 1 ATOM 5151 C CD . GLU A 1 631 ? 13.594 62.842 53.780 1.00 21.62 ? 672 GLU A CD 1 ATOM 5152 O OE1 . GLU A 1 631 ? 14.349 62.431 54.680 1.00 21.01 ? 672 GLU A OE1 1 ATOM 5153 O OE2 . GLU A 1 631 ? 14.059 63.475 52.795 1.00 21.40 ? 672 GLU A OE2 1 ATOM 5154 N N . ARG A 1 632 ? 8.913 64.931 54.491 1.00 17.67 ? 673 ARG A N 1 ATOM 5155 C CA . ARG A 1 632 ? 7.681 65.015 53.690 1.00 18.26 ? 673 ARG A CA 1 ATOM 5156 C C . ARG A 1 632 ? 7.653 66.357 52.898 1.00 18.24 ? 673 ARG A C 1 ATOM 5157 O O . ARG A 1 632 ? 7.072 66.462 51.820 1.00 18.30 ? 673 ARG A O 1 ATOM 5158 C CB . ARG A 1 632 ? 6.432 64.937 54.625 1.00 19.82 ? 673 ARG A CB 1 ATOM 5159 C CG . ARG A 1 632 ? 5.228 64.272 53.914 1.00 19.19 ? 673 ARG A CG 1 ATOM 5160 C CD . ARG A 1 632 ? 5.371 62.738 54.038 1.00 18.68 ? 673 ARG A CD 1 ATOM 5161 N NE . ARG A 1 632 ? 4.955 62.231 55.377 1.00 17.59 ? 673 ARG A NE 1 ATOM 5162 C CZ . ARG A 1 632 ? 5.771 61.690 56.269 1.00 19.17 ? 673 ARG A CZ 1 ATOM 5163 N NH1 . ARG A 1 632 ? 7.103 61.581 56.076 1.00 19.38 ? 673 ARG A NH1 1 ATOM 5164 N NH2 . ARG A 1 632 ? 5.239 61.244 57.413 1.00 20.60 ? 673 ARG A NH2 1 ATOM 5165 N N . ALA A 1 633 ? 8.255 67.406 53.501 1.00 17.24 ? 674 ALA A N 1 ATOM 5166 C CA . ALA A 1 633 ? 8.191 68.728 52.896 1.00 17.60 ? 674 ALA A CA 1 ATOM 5167 C C . ALA A 1 633 ? 8.969 68.775 51.584 1.00 17.17 ? 674 ALA A C 1 ATOM 5168 O O . ALA A 1 633 ? 8.744 69.720 50.796 1.00 19.87 ? 674 ALA A O 1 ATOM 5169 C CB . ALA A 1 633 ? 8.730 69.776 53.864 1.00 18.27 ? 674 ALA A CB 1 ATOM 5170 N N . PHE A 1 634 ? 9.884 67.828 51.338 1.00 17.23 ? 675 PHE A N 1 ATOM 5171 C CA . PHE A 1 634 ? 10.615 67.868 50.066 1.00 17.25 ? 675 PHE A CA 1 ATOM 5172 C C . PHE A 1 634 ? 9.846 67.272 48.935 1.00 18.14 ? 675 PHE A C 1 ATOM 5173 O O . PHE A 1 634 ? 10.297 67.298 47.799 1.00 18.44 ? 675 PHE A O 1 ATOM 5174 C CB . PHE A 1 634 ? 11.955 67.175 50.233 1.00 17.92 ? 675 PHE A CB 1 ATOM 5175 C CG . PHE A 1 634 ? 12.858 67.951 51.139 1.00 18.98 ? 675 PHE A CG 1 ATOM 5176 C CD1 . PHE A 1 634 ? 13.349 69.202 50.741 1.00 21.15 ? 675 PHE A CD1 1 ATOM 5177 C CD2 . PHE A 1 634 ? 13.239 67.424 52.370 1.00 21.95 ? 675 PHE A CD2 1 ATOM 5178 C CE1 . PHE A 1 634 ? 14.247 69.947 51.564 1.00 21.60 ? 675 PHE A CE1 1 ATOM 5179 C CE2 . PHE A 1 634 ? 14.113 68.179 53.222 1.00 22.36 ? 675 PHE A CE2 1 ATOM 5180 C CZ . PHE A 1 634 ? 14.598 69.450 52.811 1.00 22.16 ? 675 PHE A CZ 1 ATOM 5181 N N . ILE A 1 635 ? 8.663 66.753 49.214 1.00 17.52 ? 676 ILE A N 1 ATOM 5182 C CA . ILE A 1 635 ? 7.777 66.213 48.128 1.00 17.27 ? 676 ILE A CA 1 ATOM 5183 C C . ILE A 1 635 ? 7.071 67.328 47.371 1.00 17.99 ? 676 ILE A C 1 ATOM 5184 O O . ILE A 1 635 ? 6.467 68.216 47.968 1.00 19.94 ? 676 ILE A O 1 ATOM 5185 C CB . ILE A 1 635 ? 6.732 65.282 48.781 1.00 16.91 ? 676 ILE A CB 1 ATOM 5186 C CG1 . ILE A 1 635 ? 7.446 64.055 49.378 1.00 17.47 ? 676 ILE A CG1 1 ATOM 5187 C CG2 . ILE A 1 635 ? 5.587 64.842 47.789 1.00 18.13 ? 676 ILE A CG2 1 ATOM 5188 C CD1 . ILE A 1 635 ? 8.183 63.163 48.342 1.00 18.97 ? 676 ILE A CD1 1 ATOM 5189 N N . ASP A 1 636 ? 7.101 67.237 46.039 1.00 17.24 ? 677 ASP A N 1 ATOM 5190 C CA . ASP A 1 636 ? 6.291 68.113 45.182 1.00 18.39 ? 677 ASP A CA 1 ATOM 5191 C C . ASP A 1 636 ? 5.086 67.308 44.676 1.00 17.98 ? 677 ASP A C 1 ATOM 5192 O O . ASP A 1 636 ? 5.272 66.270 44.058 1.00 18.70 ? 677 ASP A O 1 ATOM 5193 C CB . ASP A 1 636 ? 7.147 68.518 43.992 1.00 18.65 ? 677 ASP A CB 1 ATOM 5194 C CG . ASP A 1 636 ? 6.485 69.602 43.146 1.00 18.91 ? 677 ASP A CG 1 ATOM 5195 O OD1 . ASP A 1 636 ? 5.239 69.651 43.086 1.00 20.31 ? 677 ASP A OD1 1 ATOM 5196 O OD2 . ASP A 1 636 ? 7.244 70.420 42.536 1.00 19.92 ? 677 ASP A OD2 1 ATOM 5197 N N . PRO A 1 637 ? 3.849 67.749 44.979 1.00 19.58 ? 678 PRO A N 1 ATOM 5198 C CA . PRO A 1 637 ? 2.698 66.947 44.593 1.00 21.05 ? 678 PRO A CA 1 ATOM 5199 C C . PRO A 1 637 ? 2.544 66.869 43.082 1.00 22.10 ? 678 PRO A C 1 ATOM 5200 O O . PRO A 1 637 ? 1.756 66.039 42.609 1.00 25.57 ? 678 PRO A O 1 ATOM 5201 C CB . PRO A 1 637 ? 1.506 67.726 45.183 1.00 20.75 ? 678 PRO A CB 1 ATOM 5202 C CG . PRO A 1 637 ? 2.019 69.116 45.415 1.00 22.56 ? 678 PRO A CG 1 ATOM 5203 C CD . PRO A 1 637 ? 3.498 68.978 45.684 1.00 20.17 ? 678 PRO A CD 1 ATOM 5204 N N . LEU A 1 638 ? 3.246 67.691 42.317 1.00 19.41 ? 679 LEU A N 1 ATOM 5205 C CA . LEU A 1 638 ? 3.183 67.588 40.832 1.00 19.69 ? 679 LEU A CA 1 ATOM 5206 C C . LEU A 1 638 ? 4.244 66.630 40.249 1.00 20.72 ? 679 LEU A C 1 ATOM 5207 O O . LEU A 1 638 ? 4.267 66.364 39.012 1.00 22.00 ? 679 LEU A O 1 ATOM 5208 C CB . LEU A 1 638 ? 3.366 68.970 40.212 1.00 20.52 ? 679 LEU A CB 1 ATOM 5209 C CG . LEU A 1 638 ? 2.257 69.959 40.653 1.00 21.24 ? 679 LEU A CG 1 ATOM 5210 C CD1 . LEU A 1 638 ? 2.501 71.280 39.957 1.00 22.34 ? 679 LEU A CD1 1 ATOM 5211 C CD2 . LEU A 1 638 ? 0.855 69.400 40.293 1.00 23.18 ? 679 LEU A CD2 1 ATOM 5212 N N . GLY A 1 639 ? 5.118 66.138 41.133 1.00 19.65 ? 680 GLY A N 1 ATOM 5213 C CA . GLY A 1 639 ? 6.179 65.186 40.735 1.00 21.06 ? 680 GLY A CA 1 ATOM 5214 C C . GLY A 1 639 ? 7.257 65.821 39.874 1.00 21.78 ? 680 GLY A C 1 ATOM 5215 O O . GLY A 1 639 ? 7.270 67.014 39.661 1.00 24.90 ? 680 GLY A O 1 ATOM 5216 N N . LEU A 1 640 ? 8.214 65.032 39.412 1.00 21.67 ? 681 LEU A N 1 ATOM 5217 C CA . LEU A 1 640 ? 9.243 65.553 38.517 1.00 23.86 ? 681 LEU A CA 1 ATOM 5218 C C . LEU A 1 640 ? 8.770 65.438 37.086 1.00 24.48 ? 681 LEU A C 1 ATOM 5219 O O . LEU A 1 640 ? 7.861 64.659 36.748 1.00 23.89 ? 681 LEU A O 1 ATOM 5220 C CB . LEU A 1 640 ? 10.550 64.738 38.724 1.00 23.82 ? 681 LEU A CB 1 ATOM 5221 C CG . LEU A 1 640 ? 11.167 65.086 40.081 1.00 25.34 ? 681 LEU A CG 1 ATOM 5222 C CD1 . LEU A 1 640 ? 12.171 64.028 40.495 1.00 29.41 ? 681 LEU A CD1 1 ATOM 5223 C CD2 . LEU A 1 640 ? 11.877 66.516 40.066 1.00 30.29 ? 681 LEU A CD2 1 ATOM 5224 N N . PRO A 1 641 ? 9.371 66.224 36.177 1.00 26.35 ? 682 PRO A N 1 ATOM 5225 C CA . PRO A 1 641 ? 8.902 66.204 34.798 1.00 26.43 ? 682 PRO A CA 1 ATOM 5226 C C . PRO A 1 641 ? 8.762 64.802 34.140 1.00 26.97 ? 682 PRO A C 1 ATOM 5227 O O . PRO A 1 641 ? 9.711 64.007 34.106 1.00 28.48 ? 682 PRO A O 1 ATOM 5228 C CB . PRO A 1 641 ? 9.949 67.114 34.070 1.00 28.25 ? 682 PRO A CB 1 ATOM 5229 C CG . PRO A 1 641 ? 10.440 68.005 35.105 1.00 27.32 ? 682 PRO A CG 1 ATOM 5230 C CD . PRO A 1 641 ? 10.520 67.128 36.373 1.00 26.24 ? 682 PRO A CD 1 ATOM 5231 N N . ASP A 1 642 ? 7.552 64.484 33.688 1.00 27.73 ? 683 ASP A N 1 ATOM 5232 C CA . ASP A 1 642 ? 7.187 63.185 33.065 1.00 29.43 ? 683 ASP A CA 1 ATOM 5233 C C . ASP A 1 642 ? 7.438 61.979 33.978 1.00 27.22 ? 683 ASP A C 1 ATOM 5234 O O . ASP A 1 642 ? 7.423 60.828 33.533 1.00 27.24 ? 683 ASP A O 1 ATOM 5235 C CB . ASP A 1 642 ? 7.904 62.984 31.735 1.00 31.94 ? 683 ASP A CB 1 ATOM 5236 C CG . ASP A 1 642 ? 7.617 64.110 30.769 1.00 38.23 ? 683 ASP A CG 1 ATOM 5237 O OD1 . ASP A 1 642 ? 6.422 64.373 30.478 1.00 42.97 ? 683 ASP A OD1 1 ATOM 5238 O OD2 . ASP A 1 642 ? 8.598 64.740 30.345 1.00 44.70 ? 683 ASP A OD2 1 ATOM 5239 N N . ARG A 1 643 ? 7.670 62.246 35.272 1.00 25.22 ? 684 ARG A N 1 ATOM 5240 C CA . ARG A 1 643 ? 7.851 61.142 36.231 1.00 23.42 ? 684 ARG A CA 1 ATOM 5241 C C . ARG A 1 643 ? 6.995 61.433 37.502 1.00 21.48 ? 684 ARG A C 1 ATOM 5242 O O . ARG A 1 643 ? 7.518 61.783 38.580 1.00 21.67 ? 684 ARG A O 1 ATOM 5243 C CB . ARG A 1 643 ? 9.344 60.926 36.574 1.00 23.71 ? 684 ARG A CB 1 ATOM 5244 C CG . ARG A 1 643 ? 10.221 60.473 35.344 1.00 26.04 ? 684 ARG A CG 1 ATOM 5245 C CD . ARG A 1 643 ? 11.644 60.062 35.768 1.00 28.99 ? 684 ARG A CD 1 ATOM 5246 N NE . ARG A 1 643 ? 12.390 61.192 36.347 1.00 27.25 ? 684 ARG A NE 1 ATOM 5247 C CZ . ARG A 1 643 ? 13.534 61.065 37.001 1.00 28.17 ? 684 ARG A CZ 1 ATOM 5248 N NH1 . ARG A 1 643 ? 14.080 59.848 37.155 1.00 26.58 ? 684 ARG A NH1 1 ATOM 5249 N NH2 . ARG A 1 643 ? 14.152 62.156 37.519 1.00 28.00 ? 684 ARG A NH2 1 ATOM 5250 N N . PRO A 1 644 ? 5.669 61.228 37.405 1.00 21.83 ? 685 PRO A N 1 ATOM 5251 C CA . PRO A 1 644 ? 4.747 61.692 38.460 1.00 20.93 ? 685 PRO A CA 1 ATOM 5252 C C . PRO A 1 644 ? 4.921 60.964 39.781 1.00 19.48 ? 685 PRO A C 1 ATOM 5253 O O . PRO A 1 644 ? 4.469 61.474 40.798 1.00 20.99 ? 685 PRO A O 1 ATOM 5254 C CB . PRO A 1 644 ? 3.338 61.421 37.896 1.00 24.04 ? 685 PRO A CB 1 ATOM 5255 C CG . PRO A 1 644 ? 3.567 60.442 36.762 1.00 23.34 ? 685 PRO A CG 1 ATOM 5256 C CD . PRO A 1 644 ? 4.960 60.717 36.228 1.00 23.53 ? 685 PRO A CD 1 ATOM 5257 N N . PHE A 1 645 ? 5.548 59.801 39.749 1.00 18.26 ? 686 PHE A N 1 ATOM 5258 C CA . PHE A 1 645 ? 5.740 59.000 40.981 1.00 19.11 ? 686 PHE A CA 1 ATOM 5259 C C . PHE A 1 645 ? 7.103 59.213 41.625 1.00 18.77 ? 686 PHE A C 1 ATOM 5260 O O . PHE A 1 645 ? 7.352 58.666 42.731 1.00 19.82 ? 686 PHE A O 1 ATOM 5261 C CB . PHE A 1 645 ? 5.463 57.502 40.725 1.00 18.91 ? 686 PHE A CB 1 ATOM 5262 C CG . PHE A 1 645 ? 4.057 57.244 40.256 1.00 18.67 ? 686 PHE A CG 1 ATOM 5263 C CD1 . PHE A 1 645 ? 2.970 57.595 41.039 1.00 19.97 ? 686 PHE A CD1 1 ATOM 5264 C CD2 . PHE A 1 645 ? 3.836 56.746 38.972 1.00 20.05 ? 686 PHE A CD2 1 ATOM 5265 C CE1 . PHE A 1 645 ? 1.667 57.374 40.602 1.00 19.39 ? 686 PHE A CE1 1 ATOM 5266 C CE2 . PHE A 1 645 ? 2.551 56.517 38.496 1.00 21.47 ? 686 PHE A CE2 1 ATOM 5267 C CZ . PHE A 1 645 ? 1.433 56.852 39.323 1.00 20.49 ? 686 PHE A CZ 1 ATOM 5268 N N . TYR A 1 646 ? 7.952 60.056 41.024 1.00 17.82 ? 687 TYR A N 1 ATOM 5269 C CA . TYR A 1 646 ? 9.169 60.474 41.707 1.00 17.69 ? 687 TYR A CA 1 ATOM 5270 C C . TYR A 1 646 ? 8.891 61.915 42.105 1.00 17.57 ? 687 TYR A C 1 ATOM 5271 O O . TYR A 1 646 ? 8.863 62.831 41.257 1.00 20.41 ? 687 TYR A O 1 ATOM 5272 C CB . TYR A 1 646 ? 10.408 60.381 40.776 1.00 18.63 ? 687 TYR A CB 1 ATOM 5273 C CG . TYR A 1 646 ? 10.858 58.962 40.504 1.00 18.52 ? 687 TYR A CG 1 ATOM 5274 C CD1 . TYR A 1 646 ? 10.563 57.909 41.394 1.00 18.99 ? 687 TYR A CD1 1 ATOM 5275 C CD2 . TYR A 1 646 ? 11.543 58.676 39.337 1.00 20.20 ? 687 TYR A CD2 1 ATOM 5276 C CE1 . TYR A 1 646 ? 11.018 56.607 41.144 1.00 19.33 ? 687 TYR A CE1 1 ATOM 5277 C CE2 . TYR A 1 646 ? 12.007 57.374 39.067 1.00 21.35 ? 687 TYR A CE2 1 ATOM 5278 C CZ . TYR A 1 646 ? 11.709 56.365 39.963 1.00 20.85 ? 687 TYR A CZ 1 ATOM 5279 O OH . TYR A 1 646 ? 12.166 55.070 39.749 1.00 22.53 ? 687 TYR A OH 1 ATOM 5280 N N . ARG A 1 647 ? 8.710 62.146 43.395 1.00 17.12 ? 688 ARG A N 1 ATOM 5281 C CA . ARG A 1 647 ? 8.181 63.426 43.839 1.00 15.60 ? 688 ARG A CA 1 ATOM 5282 C C . ARG A 1 647 ? 9.145 64.184 44.792 1.00 16.57 ? 688 ARG A C 1 ATOM 5283 O O . ARG A 1 647 ? 8.838 65.317 45.138 1.00 19.15 ? 688 ARG A O 1 ATOM 5284 C CB . ARG A 1 647 ? 6.859 63.249 44.571 1.00 15.85 ? 688 ARG A CB 1 ATOM 5285 C CG . ARG A 1 647 ? 5.863 62.443 43.669 1.00 17.94 ? 688 ARG A CG 1 ATOM 5286 C CD . ARG A 1 647 ? 4.411 62.622 44.105 1.00 15.85 ? 688 ARG A CD 1 ATOM 5287 N NE . ARG A 1 647 ? 4.185 62.239 45.507 1.00 18.00 ? 688 ARG A NE 1 ATOM 5288 C CZ . ARG A 1 647 ? 3.122 62.548 46.239 1.00 20.43 ? 688 ARG A CZ 1 ATOM 5289 N NH1 . ARG A 1 647 ? 3.135 62.188 47.571 1.00 20.26 ? 688 ARG A NH1 1 ATOM 5290 N NH2 . ARG A 1 647 ? 2.096 63.237 45.725 1.00 20.27 ? 688 ARG A NH2 1 ATOM 5291 N N . HIS A 1 648 ? 10.240 63.541 45.171 1.00 17.91 ? 689 HIS A N 1 ATOM 5292 C CA . HIS A 1 648 ? 11.183 64.168 46.118 1.00 18.01 ? 689 HIS A CA 1 ATOM 5293 C C . HIS A 1 648 ? 12.010 65.145 45.254 1.00 19.43 ? 689 HIS A C 1 ATOM 5294 O O . HIS A 1 648 ? 12.609 64.771 44.231 1.00 21.91 ? 689 HIS A O 1 ATOM 5295 C CB . HIS A 1 648 ? 12.063 63.071 46.725 1.00 18.30 ? 689 HIS A CB 1 ATOM 5296 C CG . HIS A 1 648 ? 12.712 63.489 48.009 1.00 17.43 ? 689 HIS A CG 1 ATOM 5297 N ND1 . HIS A 1 648 ? 13.652 64.496 48.087 1.00 18.38 ? 689 HIS A ND1 1 ATOM 5298 C CD2 . HIS A 1 648 ? 12.528 63.030 49.259 1.00 18.20 ? 689 HIS A CD2 1 ATOM 5299 C CE1 . HIS A 1 648 ? 14.023 64.646 49.355 1.00 19.47 ? 689 HIS A CE1 1 ATOM 5300 N NE2 . HIS A 1 648 ? 13.358 63.766 50.090 1.00 18.07 ? 689 HIS A NE2 1 ATOM 5301 N N . VAL A 1 649 ? 12.116 66.384 45.695 1.00 17.41 ? 690 VAL A N 1 ATOM 5302 C CA . VAL A 1 649 ? 12.779 67.424 44.886 1.00 18.21 ? 690 VAL A CA 1 ATOM 5303 C C . VAL A 1 649 ? 14.318 67.401 45.086 1.00 18.79 ? 690 VAL A C 1 ATOM 5304 O O . VAL A 1 649 ? 15.076 67.900 44.215 1.00 20.17 ? 690 VAL A O 1 ATOM 5305 C CB . VAL A 1 649 ? 12.185 68.824 45.223 1.00 18.95 ? 690 VAL A CB 1 ATOM 5306 C CG1 A VAL A 1 649 ? 12.992 69.995 44.600 0.70 16.49 ? 690 VAL A CG1 1 ATOM 5307 C CG1 B VAL A 1 649 ? 10.704 68.884 44.908 0.30 19.43 ? 690 VAL A CG1 1 ATOM 5308 C CG2 A VAL A 1 649 ? 10.800 68.881 44.681 0.70 18.21 ? 690 VAL A CG2 1 ATOM 5309 C CG2 B VAL A 1 649 ? 12.457 69.142 46.682 0.30 21.47 ? 690 VAL A CG2 1 ATOM 5310 N N . ILE A 1 650 ? 14.766 66.844 46.220 1.00 19.41 ? 691 ILE A N 1 ATOM 5311 C CA . ILE A 1 650 ? 16.210 66.800 46.499 1.00 19.42 ? 691 ILE A CA 1 ATOM 5312 C C . ILE A 1 650 ? 16.842 65.559 45.916 1.00 20.64 ? 691 ILE A C 1 ATOM 5313 O O . ILE A 1 650 ? 17.946 65.641 45.399 1.00 21.47 ? 691 ILE A O 1 ATOM 5314 C CB . ILE A 1 650 ? 16.532 66.829 48.025 1.00 20.75 ? 691 ILE A CB 1 ATOM 5315 C CG1 . ILE A 1 650 ? 15.733 67.938 48.722 1.00 21.49 ? 691 ILE A CG1 1 ATOM 5316 C CG2 . ILE A 1 650 ? 18.099 67.006 48.204 1.00 23.10 ? 691 ILE A CG2 1 ATOM 5317 C CD1 . ILE A 1 650 ? 15.887 69.329 48.087 1.00 21.63 ? 691 ILE A CD1 1 ATOM 5318 N N A TYR A 1 651 ? 16.137 64.431 45.957 0.70 19.57 ? 692 TYR A N 1 ATOM 5319 N N B TYR A 1 651 ? 16.122 64.422 45.904 0.30 19.82 ? 692 TYR A N 1 ATOM 5320 C CA A TYR A 1 651 ? 16.717 63.169 45.477 0.70 18.99 ? 692 TYR A CA 1 ATOM 5321 C CA B TYR A 1 651 ? 16.752 63.082 45.672 0.30 19.57 ? 692 TYR A CA 1 ATOM 5322 C C A TYR A 1 651 ? 15.749 62.592 44.435 0.70 19.39 ? 692 TYR A C 1 ATOM 5323 C C B TYR A 1 651 ? 16.243 62.142 44.574 0.30 19.66 ? 692 TYR A C 1 ATOM 5324 O O A TYR A 1 651 ? 14.527 62.733 44.593 0.70 18.74 ? 692 TYR A O 1 ATOM 5325 O O B TYR A 1 651 ? 16.772 61.033 44.423 0.30 19.76 ? 692 TYR A O 1 ATOM 5326 C CB A TYR A 1 651 ? 16.857 62.198 46.650 0.70 19.81 ? 692 TYR A CB 1 ATOM 5327 C CB B TYR A 1 651 ? 16.705 62.283 46.963 0.30 19.74 ? 692 TYR A CB 1 ATOM 5328 C CG A TYR A 1 651 ? 17.872 62.625 47.710 0.70 18.22 ? 692 TYR A CG 1 ATOM 5329 C CG B TYR A 1 651 ? 17.652 62.817 47.971 0.30 19.89 ? 692 TYR A CG 1 ATOM 5330 C CD1 A TYR A 1 651 ? 19.266 62.630 47.427 0.70 20.08 ? 692 TYR A CD1 1 ATOM 5331 C CD1 B TYR A 1 651 ? 18.983 63.041 47.642 0.30 21.18 ? 692 TYR A CD1 1 ATOM 5332 C CD2 A TYR A 1 651 ? 17.472 63.003 49.005 0.70 19.70 ? 692 TYR A CD2 1 ATOM 5333 C CD2 B TYR A 1 651 ? 17.228 63.110 49.253 0.30 19.52 ? 692 TYR A CD2 1 ATOM 5334 C CE1 A TYR A 1 651 ? 20.213 63.039 48.386 0.70 18.94 ? 692 TYR A CE1 1 ATOM 5335 C CE1 B TYR A 1 651 ? 19.852 63.523 48.554 0.30 21.22 ? 692 TYR A CE1 1 ATOM 5336 C CE2 A TYR A 1 651 ? 18.394 63.375 49.955 0.70 19.96 ? 692 TYR A CE2 1 ATOM 5337 C CE2 B TYR A 1 651 ? 18.080 63.595 50.162 0.30 20.81 ? 692 TYR A CE2 1 ATOM 5338 C CZ A TYR A 1 651 ? 19.761 63.369 49.674 0.70 20.05 ? 692 TYR A CZ 1 ATOM 5339 C CZ B TYR A 1 651 ? 19.391 63.797 49.822 0.30 20.76 ? 692 TYR A CZ 1 ATOM 5340 O OH A TYR A 1 651 ? 20.742 63.711 50.581 0.70 20.66 ? 692 TYR A OH 1 ATOM 5341 O OH B TYR A 1 651 ? 20.237 64.286 50.756 0.30 22.98 ? 692 TYR A OH 1 ATOM 5342 N N A ALA A 1 652 ? 16.287 61.932 43.419 0.70 19.53 ? 693 ALA A N 1 ATOM 5343 N N B ALA A 1 652 ? 15.220 62.535 43.834 0.30 19.19 ? 693 ALA A N 1 ATOM 5344 C CA A ALA A 1 652 ? 15.488 60.984 42.613 0.70 18.84 ? 693 ALA A CA 1 ATOM 5345 C CA B ALA A 1 652 ? 14.656 61.591 42.865 0.30 19.12 ? 693 ALA A CA 1 ATOM 5346 C C A ALA A 1 652 ? 16.446 59.940 42.100 0.70 19.51 ? 693 ALA A C 1 ATOM 5347 C C B ALA A 1 652 ? 15.724 61.197 41.871 0.30 19.12 ? 693 ALA A C 1 ATOM 5348 O O A ALA A 1 652 ? 17.657 60.179 42.061 0.70 20.80 ? 693 ALA A O 1 ATOM 5349 O O B ALA A 1 652 ? 16.699 61.923 41.699 0.30 20.10 ? 693 ALA A O 1 ATOM 5350 C CB A ALA A 1 652 ? 14.819 61.678 41.444 0.70 19.88 ? 693 ALA A CB 1 ATOM 5351 C CB B ALA A 1 652 ? 13.554 62.216 42.140 0.30 18.75 ? 693 ALA A CB 1 ATOM 5352 N N A PRO A 1 653 ? 15.920 58.778 41.700 0.70 18.42 ? 694 PRO A N 1 ATOM 5353 N N B PRO A 1 653 ? 15.535 60.050 41.196 0.30 19.33 ? 694 PRO A N 1 ATOM 5354 C CA A PRO A 1 653 ? 16.757 57.836 41.000 0.70 18.72 ? 694 PRO A CA 1 ATOM 5355 C CA B PRO A 1 653 ? 16.473 59.649 40.167 0.30 20.34 ? 694 PRO A CA 1 ATOM 5356 C C A PRO A 1 653 ? 17.297 58.509 39.747 0.70 19.00 ? 694 PRO A C 1 ATOM 5357 C C B PRO A 1 653 ? 16.391 60.587 38.984 0.30 20.07 ? 694 PRO A C 1 ATOM 5358 O O A PRO A 1 653 ? 16.557 59.224 39.062 0.70 20.27 ? 694 PRO A O 1 ATOM 5359 O O B PRO A 1 653 ? 15.299 61.022 38.624 0.30 21.83 ? 694 PRO A O 1 ATOM 5360 C CB A PRO A 1 653 ? 15.764 56.724 40.598 0.70 19.08 ? 694 PRO A CB 1 ATOM 5361 C CB B PRO A 1 653 ? 15.946 58.281 39.727 0.30 20.06 ? 694 PRO A CB 1 ATOM 5362 C CG A PRO A 1 653 ? 14.677 56.836 41.627 0.70 18.41 ? 694 PRO A CG 1 ATOM 5363 C CG B PRO A 1 653 ? 15.090 57.798 40.872 0.30 19.89 ? 694 PRO A CG 1 ATOM 5364 C CD A PRO A 1 653 ? 14.519 58.325 41.833 0.70 18.42 ? 694 PRO A CD 1 ATOM 5365 C CD B PRO A 1 653 ? 14.461 59.058 41.395 0.30 18.20 ? 694 PRO A CD 1 ATOM 5366 N N A SER A 1 654 ? 18.591 58.335 39.474 0.70 19.18 ? 695 SER A N 1 ATOM 5367 N N B SER A 1 654 ? 17.515 60.892 38.367 0.30 20.96 ? 695 SER A N 1 ATOM 5368 C CA A SER A 1 654 ? 19.157 58.918 38.248 0.70 19.47 ? 695 SER A CA 1 ATOM 5369 C CA B SER A 1 654 ? 17.492 61.605 37.086 0.30 20.22 ? 695 SER A CA 1 ATOM 5370 C C A SER A 1 654 ? 18.402 58.475 37.001 0.70 20.75 ? 695 SER A C 1 ATOM 5371 C C B SER A 1 654 ? 16.858 60.699 36.013 0.30 19.74 ? 695 SER A C 1 ATOM 5372 O O A SER A 1 654 ? 18.085 57.298 36.821 0.70 21.53 ? 695 SER A O 1 ATOM 5373 O O B SER A 1 654 ? 16.988 59.483 36.105 0.30 19.45 ? 695 SER A O 1 ATOM 5374 C CB A SER A 1 654 ? 20.625 58.499 38.085 0.70 20.29 ? 695 SER A CB 1 ATOM 5375 C CB B SER A 1 654 ? 18.925 62.011 36.742 0.30 21.20 ? 695 SER A CB 1 ATOM 5376 O OG A SER A 1 654 ? 21.159 58.939 36.844 0.70 21.40 ? 695 SER A OG 1 ATOM 5377 O OG B SER A 1 654 ? 19.186 62.014 35.353 0.30 23.41 ? 695 SER A OG 1 ATOM 5378 N N A SER A 1 655 ? 18.182 59.423 36.100 0.70 20.07 ? 696 SER A N 1 ATOM 5379 N N B SER A 1 655 ? 16.150 61.266 35.023 0.30 16.80 ? 696 SER A N 1 ATOM 5380 C CA A SER A 1 655 ? 17.495 59.144 34.851 0.70 22.70 ? 696 SER A CA 1 ATOM 5381 C CA B SER A 1 655 ? 15.546 60.462 33.983 0.30 21.38 ? 696 SER A CA 1 ATOM 5382 C C A SER A 1 655 ? 18.374 58.300 33.906 0.70 23.88 ? 696 SER A C 1 ATOM 5383 C C B SER A 1 655 ? 16.535 60.140 32.870 0.30 21.92 ? 696 SER A C 1 ATOM 5384 O O A SER A 1 655 ? 17.886 57.837 32.854 0.70 24.94 ? 696 SER A O 1 ATOM 5385 O O B SER A 1 655 ? 16.139 59.633 31.823 0.30 25.79 ? 696 SER A O 1 ATOM 5386 C CB A SER A 1 655 ? 17.011 60.469 34.222 0.70 23.82 ? 696 SER A CB 1 ATOM 5387 C CB B SER A 1 655 ? 14.258 61.081 33.415 0.30 20.97 ? 696 SER A CB 1 ATOM 5388 O OG A SER A 1 655 ? 17.844 60.898 33.182 0.70 31.68 ? 696 SER A OG 1 ATOM 5389 O OG B SER A 1 655 ? 14.353 62.471 33.272 0.30 24.68 ? 696 SER A OG 1 ATOM 5390 N N A HIS A 1 656 ? 19.618 58.065 34.320 0.70 23.45 ? 697 HIS A N 1 ATOM 5391 C CA A HIS A 1 656 ? 20.555 57.234 33.559 0.70 25.38 ? 697 HIS A CA 1 ATOM 5392 C C A HIS A 1 656 ? 20.912 55.939 34.255 0.70 26.06 ? 697 HIS A C 1 ATOM 5393 O O A HIS A 1 656 ? 21.575 55.073 33.672 0.70 27.60 ? 697 HIS A O 1 ATOM 5394 C CB A HIS A 1 656 ? 21.811 58.058 33.268 0.70 27.17 ? 697 HIS A CB 1 ATOM 5395 C CG A HIS A 1 656 ? 21.494 59.351 32.596 0.70 28.94 ? 697 HIS A CG 1 ATOM 5396 N ND1 A HIS A 1 656 ? 21.326 59.448 31.235 0.70 29.93 ? 697 HIS A ND1 1 ATOM 5397 C CD2 A HIS A 1 656 ? 21.196 60.570 33.102 0.70 31.22 ? 697 HIS A CD2 1 ATOM 5398 C CE1 A HIS A 1 656 ? 20.988 60.686 30.921 0.70 33.34 ? 697 HIS A CE1 1 ATOM 5399 N NE2 A HIS A 1 656 ? 20.907 61.393 32.036 0.70 29.31 ? 697 HIS A NE2 1 ATOM 5400 N N A ASN A 1 657 ? 20.477 55.799 35.502 0.70 23.96 ? 698 ASN A N 1 ATOM 5401 C CA A ASN A 1 657 ? 20.847 54.636 36.301 0.70 22.95 ? 698 ASN A CA 1 ATOM 5402 C C A ASN A 1 657 ? 19.975 54.560 37.517 0.70 22.44 ? 698 ASN A C 1 ATOM 5403 O O A ASN A 1 657 ? 20.265 55.245 38.497 0.70 22.11 ? 698 ASN A O 1 ATOM 5404 C CB A ASN A 1 657 ? 22.326 54.742 36.748 0.70 23.33 ? 698 ASN A CB 1 ATOM 5405 C CG A ASN A 1 657 ? 22.749 53.591 37.674 0.70 21.89 ? 698 ASN A CG 1 ATOM 5406 O OD1 A ASN A 1 657 ? 22.024 52.609 37.804 0.70 21.34 ? 698 ASN A OD1 1 ATOM 5407 N ND2 A ASN A 1 657 ? 23.947 53.704 38.289 0.70 22.67 ? 698 ASN A ND2 1 ATOM 5408 N N . LYS A 1 658 ? 18.928 53.727 37.492 0.70 22.62 ? 699 LYS A N 1 ATOM 5409 C CA A LYS A 1 658 ? 18.025 53.643 38.669 0.35 19.95 ? 699 LYS A CA 1 ATOM 5410 C CA B LYS A 1 658 ? 17.524 53.811 37.893 0.35 26.01 ? 699 LYS A CA 1 ATOM 5411 C C A LYS A 1 658 ? 18.682 53.348 40.001 0.70 20.97 ? 699 LYS A C 1 ATOM 5412 O O A LYS A 1 658 ? 18.110 53.720 41.031 0.70 20.62 ? 699 LYS A O 1 ATOM 5413 C CB A LYS A 1 658 ? 16.914 52.630 38.439 0.35 20.31 ? 699 LYS A CB 1 ATOM 5414 C CB B LYS A 1 658 ? 16.873 52.427 37.906 0.35 25.54 ? 699 LYS A CB 1 ATOM 5415 C CG A LYS A 1 658 ? 15.925 53.093 37.389 0.35 21.03 ? 699 LYS A CG 1 ATOM 5416 C CG B LYS A 1 658 ? 15.490 52.398 37.263 0.35 27.35 ? 699 LYS A CG 1 ATOM 5417 C CD A LYS A 1 658 ? 15.119 54.286 37.867 0.35 22.18 ? 699 LYS A CD 1 ATOM 5418 C CD B LYS A 1 658 ? 14.502 53.220 38.051 0.35 27.43 ? 699 LYS A CD 1 ATOM 5419 C CE A LYS A 1 658 ? 13.785 54.420 37.118 0.35 22.95 ? 699 LYS A CE 1 ATOM 5420 C CE B LYS A 1 658 ? 13.490 53.893 37.150 0.35 27.43 ? 699 LYS A CE 1 ATOM 5421 N NZ A LYS A 1 658 ? 13.769 54.053 35.659 0.35 25.60 ? 699 LYS A NZ 1 ATOM 5422 N NZ B LYS A 1 658 ? 12.825 53.000 36.192 0.35 27.19 ? 699 LYS A NZ 1 ATOM 5423 N N A TYR A 1 659 ? 19.832 52.673 39.984 0.70 20.79 ? 700 TYR A N 1 ATOM 5424 C CA A TYR A 1 659 ? 20.500 52.323 41.247 0.70 20.86 ? 700 TYR A CA 1 ATOM 5425 C C A TYR A 1 659 ? 21.099 53.526 41.972 0.70 21.05 ? 700 TYR A C 1 ATOM 5426 O O A TYR A 1 659 ? 21.325 53.447 43.173 0.70 23.18 ? 700 TYR A O 1 ATOM 5427 C CB A TYR A 1 659 ? 21.639 51.348 41.013 0.70 21.03 ? 700 TYR A CB 1 ATOM 5428 C CG A TYR A 1 659 ? 21.206 49.976 40.502 0.70 21.80 ? 700 TYR A CG 1 ATOM 5429 C CD1 A TYR A 1 659 ? 20.086 49.346 41.016 0.70 23.37 ? 700 TYR A CD1 1 ATOM 5430 C CD2 A TYR A 1 659 ? 21.975 49.287 39.564 0.70 22.19 ? 700 TYR A CD2 1 ATOM 5431 C CE1 A TYR A 1 659 ? 19.701 48.061 40.569 0.70 23.30 ? 700 TYR A CE1 1 ATOM 5432 C CE2 A TYR A 1 659 ? 21.601 47.993 39.087 0.70 21.48 ? 700 TYR A CE2 1 ATOM 5433 C CZ A TYR A 1 659 ? 20.458 47.399 39.598 0.70 24.41 ? 700 TYR A CZ 1 ATOM 5434 O OH A TYR A 1 659 ? 20.094 46.143 39.159 0.70 24.09 ? 700 TYR A OH 1 ATOM 5435 N N A ALA A 1 660 ? 21.400 54.586 41.222 0.70 21.00 ? 701 ALA A N 1 ATOM 5436 C CA A ALA A 1 660 ? 22.092 55.753 41.743 0.70 21.07 ? 701 ALA A CA 1 ATOM 5437 C C A ALA A 1 660 ? 21.114 56.835 42.143 0.70 22.13 ? 701 ALA A C 1 ATOM 5438 O O A ALA A 1 660 ? 20.169 57.132 41.398 0.70 22.46 ? 701 ALA A O 1 ATOM 5439 C CB A ALA A 1 660 ? 23.073 56.316 40.636 0.70 21.22 ? 701 ALA A CB 1 ATOM 5440 N N A GLY A 1 661 ? 21.322 57.442 43.305 0.70 21.82 ? 702 GLY A N 1 ATOM 5441 C CA A GLY A 1 661 ? 20.559 58.666 43.616 0.70 21.92 ? 702 GLY A CA 1 ATOM 5442 C C A GLY A 1 661 ? 21.212 59.879 42.945 0.70 22.27 ? 702 GLY A C 1 ATOM 5443 O O A GLY A 1 661 ? 22.459 59.938 42.806 0.70 24.60 ? 702 GLY A O 1 ATOM 5444 N N A GLU A 1 662 ? 20.369 60.811 42.487 0.70 21.96 ? 703 GLU A N 1 ATOM 5445 C CA A GLU A 1 662 ? 20.841 62.088 41.929 0.70 22.34 ? 703 GLU A CA 1 ATOM 5446 C C A GLU A 1 662 ? 20.332 63.217 42.831 0.70 23.16 ? 703 GLU A C 1 ATOM 5447 O O A GLU A 1 662 ? 19.207 63.130 43.326 0.70 22.79 ? 703 GLU A O 1 ATOM 5448 C CB A GLU A 1 662 ? 20.334 62.286 40.490 0.70 22.76 ? 703 GLU A CB 1 ATOM 5449 C CG A GLU A 1 662 ? 20.930 63.538 39.834 0.70 24.19 ? 703 GLU A CG 1 ATOM 5450 C CD A GLU A 1 662 ? 22.457 63.480 39.820 0.70 24.49 ? 703 GLU A CD 1 ATOM 5451 O OE1 A GLU A 1 662 ? 23.018 62.724 39.008 0.70 26.46 ? 703 GLU A OE1 1 ATOM 5452 O OE2 A GLU A 1 662 ? 23.095 64.138 40.681 0.70 24.70 ? 703 GLU A OE2 1 ATOM 5453 N N . SER A 1 663 ? 21.158 64.248 43.062 1.00 25.11 ? 704 SER A N 1 ATOM 5454 C CA A SER A 1 663 ? 20.664 65.418 43.802 0.70 23.93 ? 704 SER A CA 1 ATOM 5455 C CA B SER A 1 663 ? 20.532 65.357 43.772 0.30 23.48 ? 704 SER A CA 1 ATOM 5456 C C . SER A 1 663 ? 20.145 66.543 42.902 1.00 22.93 ? 704 SER A C 1 ATOM 5457 O O . SER A 1 663 ? 20.688 66.786 41.832 1.00 25.63 ? 704 SER A O 1 ATOM 5458 C CB A SER A 1 663 ? 21.707 65.914 44.838 0.70 24.23 ? 704 SER A CB 1 ATOM 5459 C CB B SER A 1 663 ? 21.395 65.807 44.949 0.30 23.74 ? 704 SER A CB 1 ATOM 5460 O OG A SER A 1 663 ? 22.977 66.124 44.224 0.70 25.13 ? 704 SER A OG 1 ATOM 5461 O OG B SER A 1 663 ? 21.765 64.678 45.694 0.30 22.70 ? 704 SER A OG 1 ATOM 5462 N N . PHE A 1 664 ? 19.128 67.268 43.378 1.00 21.31 ? 705 PHE A N 1 ATOM 5463 C CA . PHE A 1 664 ? 18.429 68.302 42.564 1.00 20.59 ? 705 PHE A CA 1 ATOM 5464 C C . PHE A 1 664 ? 18.196 67.744 41.163 1.00 19.79 ? 705 PHE A C 1 ATOM 5465 O O . PHE A 1 664 ? 18.572 68.359 40.190 1.00 20.61 ? 705 PHE A O 1 ATOM 5466 C CB . PHE A 1 664 ? 19.173 69.640 42.553 1.00 21.37 ? 705 PHE A CB 1 ATOM 5467 C CG . PHE A 1 664 ? 19.101 70.368 43.905 1.00 20.32 ? 705 PHE A CG 1 ATOM 5468 C CD1 . PHE A 1 664 ? 17.849 70.681 44.476 1.00 20.60 ? 705 PHE A CD1 1 ATOM 5469 C CD2 . PHE A 1 664 ? 20.258 70.795 44.532 1.00 20.29 ? 705 PHE A CD2 1 ATOM 5470 C CE1 . PHE A 1 664 ? 17.768 71.352 45.721 1.00 21.97 ? 705 PHE A CE1 1 ATOM 5471 C CE2 . PHE A 1 664 ? 20.201 71.451 45.751 1.00 22.94 ? 705 PHE A CE2 1 ATOM 5472 C CZ . PHE A 1 664 ? 18.947 71.739 46.351 1.00 21.18 ? 705 PHE A CZ 1 ATOM 5473 N N . PRO A 1 665 ? 17.478 66.611 41.088 1.00 19.95 ? 706 PRO A N 1 ATOM 5474 C CA . PRO A 1 665 ? 17.336 65.929 39.801 1.00 20.32 ? 706 PRO A CA 1 ATOM 5475 C C . PRO A 1 665 ? 16.629 66.762 38.767 1.00 19.95 ? 706 PRO A C 1 ATOM 5476 O O . PRO A 1 665 ? 16.895 66.605 37.569 1.00 22.32 ? 706 PRO A O 1 ATOM 5477 C CB . PRO A 1 665 ? 16.452 64.692 40.175 1.00 19.96 ? 706 PRO A CB 1 ATOM 5478 C CG . PRO A 1 665 ? 15.753 65.056 41.454 1.00 20.92 ? 706 PRO A CG 1 ATOM 5479 C CD . PRO A 1 665 ? 16.830 65.866 42.198 1.00 20.28 ? 706 PRO A CD 1 ATOM 5480 N N . GLY A 1 666 ? 15.674 67.599 39.196 1.00 19.73 ? 707 GLY A N 1 ATOM 5481 C CA . GLY A 1 666 ? 14.963 68.385 38.175 1.00 19.73 ? 707 GLY A CA 1 ATOM 5482 C C . GLY A 1 666 ? 15.895 69.365 37.484 1.00 19.42 ? 707 GLY A C 1 ATOM 5483 O O . GLY A 1 666 ? 15.850 69.522 36.225 1.00 21.31 ? 707 GLY A O 1 ATOM 5484 N N . ILE A 1 667 ? 16.759 70.031 38.280 1.00 19.93 ? 708 ILE A N 1 ATOM 5485 C CA . ILE A 1 667 ? 17.748 70.907 37.625 1.00 20.98 ? 708 ILE A CA 1 ATOM 5486 C C . ILE A 1 667 ? 18.786 70.083 36.839 1.00 22.15 ? 708 ILE A C 1 ATOM 5487 O O . ILE A 1 667 ? 19.145 70.454 35.723 1.00 23.74 ? 708 ILE A O 1 ATOM 5488 C CB . ILE A 1 667 ? 18.508 71.783 38.657 1.00 21.52 ? 708 ILE A CB 1 ATOM 5489 C CG1 . ILE A 1 667 ? 17.469 72.523 39.544 1.00 22.44 ? 708 ILE A CG1 1 ATOM 5490 C CG2 . ILE A 1 667 ? 19.367 72.807 37.893 1.00 23.29 ? 708 ILE A CG2 1 ATOM 5491 C CD1 . ILE A 1 667 ? 18.145 73.263 40.740 1.00 23.21 ? 708 ILE A CD1 1 ATOM 5492 N N . TYR A 1 668 ? 19.252 68.989 37.424 1.00 21.94 ? 709 TYR A N 1 ATOM 5493 C CA . TYR A 1 668 ? 20.272 68.169 36.782 1.00 23.42 ? 709 TYR A CA 1 ATOM 5494 C C . TYR A 1 668 ? 19.793 67.712 35.403 1.00 23.01 ? 709 TYR A C 1 ATOM 5495 O O . TYR A 1 668 ? 20.507 67.860 34.416 1.00 23.78 ? 709 TYR A O 1 ATOM 5496 C CB . TYR A 1 668 ? 20.619 66.965 37.649 1.00 22.21 ? 709 TYR A CB 1 ATOM 5497 C CG . TYR A 1 668 ? 21.686 66.091 37.018 1.00 23.91 ? 709 TYR A CG 1 ATOM 5498 C CD1 . TYR A 1 668 ? 23.032 66.302 37.289 1.00 27.55 ? 709 TYR A CD1 1 ATOM 5499 C CD2 . TYR A 1 668 ? 21.328 65.107 36.094 1.00 26.36 ? 709 TYR A CD2 1 ATOM 5500 C CE1 . TYR A 1 668 ? 24.044 65.527 36.671 1.00 28.61 ? 709 TYR A CE1 1 ATOM 5501 C CE2 . TYR A 1 668 ? 22.324 64.329 35.449 1.00 27.04 ? 709 TYR A CE2 1 ATOM 5502 C CZ . TYR A 1 668 ? 23.666 64.559 35.751 1.00 29.07 ? 709 TYR A CZ 1 ATOM 5503 O OH . TYR A 1 668 ? 24.687 63.807 35.190 1.00 30.00 ? 709 TYR A OH 1 ATOM 5504 N N . ASP A 1 669 ? 18.593 67.133 35.336 1.00 22.37 ? 710 ASP A N 1 ATOM 5505 C CA . ASP A 1 669 ? 18.084 66.708 34.032 1.00 22.72 ? 710 ASP A CA 1 ATOM 5506 C C . ASP A 1 669 ? 17.849 67.866 33.058 1.00 23.90 ? 710 ASP A C 1 ATOM 5507 O O . ASP A 1 669 ? 18.034 67.709 31.838 1.00 24.82 ? 710 ASP A O 1 ATOM 5508 C CB . ASP A 1 669 ? 16.799 65.875 34.202 1.00 22.44 ? 710 ASP A CB 1 ATOM 5509 C CG . ASP A 1 669 ? 17.050 64.493 34.776 1.00 24.35 ? 710 ASP A CG 1 ATOM 5510 O OD1 . ASP A 1 669 ? 18.198 63.991 34.737 1.00 26.36 ? 710 ASP A OD1 1 ATOM 5511 O OD2 . ASP A 1 669 ? 16.051 63.903 35.287 1.00 26.33 ? 710 ASP A OD2 1 ATOM 5512 N N . ALA A 1 670 ? 17.409 69.036 33.545 1.00 22.87 ? 711 ALA A N 1 ATOM 5513 C CA . ALA A 1 670 ? 17.250 70.205 32.665 1.00 23.87 ? 711 ALA A CA 1 ATOM 5514 C C . ALA A 1 670 ? 18.610 70.638 32.066 1.00 24.19 ? 711 ALA A C 1 ATOM 5515 O O . ALA A 1 670 ? 18.685 71.048 30.898 1.00 26.12 ? 711 ALA A O 1 ATOM 5516 C CB . ALA A 1 670 ? 16.604 71.381 33.407 1.00 23.57 ? 711 ALA A CB 1 ATOM 5517 N N . LEU A 1 671 ? 19.699 70.451 32.827 1.00 24.98 ? 712 LEU A N 1 ATOM 5518 C CA . LEU A 1 671 ? 21.046 70.804 32.325 1.00 25.86 ? 712 LEU A CA 1 ATOM 5519 C C . LEU A 1 671 ? 21.734 69.712 31.483 1.00 27.66 ? 712 LEU A C 1 ATOM 5520 O O . LEU A 1 671 ? 22.716 69.986 30.806 1.00 28.83 ? 712 LEU A O 1 ATOM 5521 C CB . LEU A 1 671 ? 21.984 71.106 33.497 1.00 26.47 ? 712 LEU A CB 1 ATOM 5522 C CG . LEU A 1 671 ? 21.743 72.474 34.164 1.00 25.39 ? 712 LEU A CG 1 ATOM 5523 C CD1 . LEU A 1 671 ? 22.422 72.493 35.577 1.00 26.00 ? 712 LEU A CD1 1 ATOM 5524 C CD2 . LEU A 1 671 ? 22.253 73.582 33.252 1.00 25.60 ? 712 LEU A CD2 1 ATOM 5525 N N . PHE A 1 672 ? 21.243 68.476 31.588 1.00 27.33 ? 713 PHE A N 1 ATOM 5526 C CA . PHE A 1 672 ? 22.006 67.349 31.028 1.00 28.66 ? 713 PHE A CA 1 ATOM 5527 C C . PHE A 1 672 ? 22.040 67.426 29.512 1.00 29.67 ? 713 PHE A C 1 ATOM 5528 O O . PHE A 1 672 ? 20.984 67.532 28.873 1.00 30.13 ? 713 PHE A O 1 ATOM 5529 C CB . PHE A 1 672 ? 21.419 65.998 31.493 1.00 27.94 ? 713 PHE A CB 1 ATOM 5530 C CG . PHE A 1 672 ? 22.257 64.819 31.038 1.00 30.49 ? 713 PHE A CG 1 ATOM 5531 C CD1 . PHE A 1 672 ? 23.399 64.447 31.758 1.00 32.11 ? 713 PHE A CD1 1 ATOM 5532 C CD2 . PHE A 1 672 ? 21.957 64.169 29.837 1.00 31.26 ? 713 PHE A CD2 1 ATOM 5533 C CE1 . PHE A 1 672 ? 24.211 63.376 31.309 1.00 35.10 ? 713 PHE A CE1 1 ATOM 5534 C CE2 . PHE A 1 672 ? 22.755 63.103 29.377 1.00 32.10 ? 713 PHE A CE2 1 ATOM 5535 C CZ . PHE A 1 672 ? 23.879 62.714 30.094 1.00 34.71 ? 713 PHE A CZ 1 ATOM 5536 N N . ASP A 1 673 ? 23.243 67.381 28.932 1.00 31.79 ? 714 ASP A N 1 ATOM 5537 C CA . ASP A 1 673 ? 23.407 67.454 27.466 1.00 34.49 ? 714 ASP A CA 1 ATOM 5538 C C . ASP A 1 673 ? 22.729 68.696 26.863 1.00 35.23 ? 714 ASP A C 1 ATOM 5539 O O . ASP A 1 673 ? 22.237 68.664 25.731 1.00 35.89 ? 714 ASP A O 1 ATOM 5540 C CB . ASP A 1 673 ? 22.880 66.142 26.821 1.00 34.37 ? 714 ASP A CB 1 ATOM 5541 C CG . ASP A 1 673 ? 23.324 65.970 25.355 1.00 37.69 ? 714 ASP A CG 1 ATOM 5542 O OD1 . ASP A 1 673 ? 24.490 66.264 25.031 1.00 39.12 ? 714 ASP A OD1 1 ATOM 5543 O OD2 . ASP A 1 673 ? 22.484 65.519 24.534 1.00 40.58 ? 714 ASP A OD2 1 ATOM 5544 N N . ILE A 1 674 ? 22.691 69.806 27.616 1.00 34.29 ? 715 ILE A N 1 ATOM 5545 C CA . ILE A 1 674 ? 21.904 70.952 27.179 1.00 33.35 ? 715 ILE A CA 1 ATOM 5546 C C . ILE A 1 674 ? 22.522 71.583 25.925 1.00 35.75 ? 715 ILE A C 1 ATOM 5547 O O . ILE A 1 674 ? 21.796 72.156 25.129 1.00 35.47 ? 715 ILE A O 1 ATOM 5548 C CB . ILE A 1 674 ? 21.721 72.011 28.309 1.00 33.41 ? 715 ILE A CB 1 ATOM 5549 C CG1 . ILE A 1 674 ? 20.742 73.102 27.869 1.00 32.03 ? 715 ILE A CG1 1 ATOM 5550 C CG2 . ILE A 1 674 ? 23.053 72.618 28.718 1.00 32.44 ? 715 ILE A CG2 1 ATOM 5551 C CD1 . ILE A 1 674 ? 20.213 73.920 29.055 1.00 30.72 ? 715 ILE A CD1 1 ATOM 5552 N N . GLU A 1 675 ? 23.830 71.417 25.741 1.00 36.97 ? 716 GLU A N 1 ATOM 5553 C CA . GLU A 1 675 ? 24.507 72.006 24.582 1.00 41.21 ? 716 GLU A CA 1 ATOM 5554 C C . GLU A 1 675 ? 24.032 71.414 23.257 1.00 42.37 ? 716 GLU A C 1 ATOM 5555 O O . GLU A 1 675 ? 24.294 71.985 22.199 1.00 44.31 ? 716 GLU A O 1 ATOM 5556 C CB . GLU A 1 675 ? 26.040 71.912 24.727 1.00 42.03 ? 716 GLU A CB 1 ATOM 5557 C CG . GLU A 1 675 ? 26.652 70.515 24.641 1.00 43.36 ? 716 GLU A CG 1 ATOM 5558 C CD . GLU A 1 675 ? 26.615 69.735 25.961 1.00 44.62 ? 716 GLU A CD 1 ATOM 5559 O OE1 . GLU A 1 675 ? 25.850 70.090 26.879 1.00 40.48 ? 716 GLU A OE1 1 ATOM 5560 O OE2 . GLU A 1 675 ? 27.366 68.748 26.070 1.00 48.92 ? 716 GLU A OE2 1 ATOM 5561 N N . SER A 1 676 ? 23.325 70.285 23.329 1.00 43.36 ? 717 SER A N 1 ATOM 5562 C CA . SER A 1 676 ? 22.789 69.572 22.156 1.00 45.17 ? 717 SER A CA 1 ATOM 5563 C C . SER A 1 676 ? 21.344 69.938 21.829 1.00 45.64 ? 717 SER A C 1 ATOM 5564 O O . SER A 1 676 ? 20.844 69.583 20.759 1.00 46.95 ? 717 SER A O 1 ATOM 5565 C CB . SER A 1 676 ? 22.895 68.048 22.351 1.00 44.85 ? 717 SER A CB 1 ATOM 5566 O OG . SER A 1 676 ? 24.255 67.655 22.535 1.00 46.29 ? 717 SER A OG 1 ATOM 5567 N N . LYS A 1 677 ? 20.670 70.665 22.720 1.00 44.84 ? 718 LYS A N 1 ATOM 5568 C CA . LYS A 1 677 ? 19.269 71.005 22.489 1.00 44.66 ? 718 LYS A CA 1 ATOM 5569 C C . LYS A 1 677 ? 19.148 72.036 21.379 1.00 46.55 ? 718 LYS A C 1 ATOM 5570 O O . LYS A 1 677 ? 19.940 72.969 21.279 1.00 47.14 ? 718 LYS A O 1 ATOM 5571 C CB . LYS A 1 677 ? 18.575 71.505 23.764 1.00 43.77 ? 718 LYS A CB 1 ATOM 5572 C CG . LYS A 1 677 ? 18.605 70.495 24.889 1.00 42.94 ? 718 LYS A CG 1 ATOM 5573 C CD . LYS A 1 677 ? 17.682 69.300 24.628 1.00 47.30 ? 718 LYS A CD 1 ATOM 5574 C CE . LYS A 1 677 ? 17.761 68.282 25.777 1.00 47.63 ? 718 LYS A CE 1 ATOM 5575 N NZ . LYS A 1 677 ? 17.098 68.781 27.036 1.00 48.36 ? 718 LYS A NZ 1 ATOM 5576 N N . VAL A 1 678 ? 18.125 71.862 20.562 1.00 47.26 ? 719 VAL A N 1 ATOM 5577 C CA . VAL A 1 678 ? 17.956 72.669 19.362 1.00 48.94 ? 719 VAL A CA 1 ATOM 5578 C C . VAL A 1 678 ? 17.457 74.095 19.654 1.00 48.05 ? 719 VAL A C 1 ATOM 5579 O O . VAL A 1 678 ? 17.791 75.036 18.930 1.00 49.51 ? 719 VAL A O 1 ATOM 5580 C CB . VAL A 1 678 ? 17.050 71.898 18.358 1.00 49.95 ? 719 VAL A CB 1 ATOM 5581 C CG1 . VAL A 1 678 ? 16.046 72.806 17.663 1.00 52.42 ? 719 VAL A CG1 1 ATOM 5582 C CG2 . VAL A 1 678 ? 17.919 71.116 17.357 1.00 51.98 ? 719 VAL A CG2 1 ATOM 5583 N N . ASP A 1 679 ? 16.684 74.246 20.730 1.00 46.30 ? 720 ASP A N 1 ATOM 5584 C CA . ASP A 1 679 ? 16.134 75.545 21.131 1.00 44.83 ? 720 ASP A CA 1 ATOM 5585 C C . ASP A 1 679 ? 16.743 75.916 22.499 1.00 42.67 ? 720 ASP A C 1 ATOM 5586 O O . ASP A 1 679 ? 16.171 75.573 23.544 1.00 40.36 ? 720 ASP A O 1 ATOM 5587 C CB . ASP A 1 679 ? 14.604 75.427 21.224 1.00 44.61 ? 720 ASP A CB 1 ATOM 5588 C CG . ASP A 1 679 ? 13.901 76.759 21.468 1.00 46.25 ? 720 ASP A CG 1 ATOM 5589 O OD1 . ASP A 1 679 ? 14.547 77.771 21.784 1.00 46.19 ? 720 ASP A OD1 1 ATOM 5590 O OD2 . ASP A 1 679 ? 12.660 76.789 21.358 1.00 50.85 ? 720 ASP A OD2 1 ATOM 5591 N N . PRO A 1 680 ? 17.905 76.600 22.501 1.00 41.61 ? 721 PRO A N 1 ATOM 5592 C CA . PRO A 1 680 ? 18.562 76.890 23.776 1.00 40.49 ? 721 PRO A CA 1 ATOM 5593 C C . PRO A 1 680 ? 17.729 77.800 24.686 1.00 38.82 ? 721 PRO A C 1 ATOM 5594 O O . PRO A 1 680 ? 17.798 77.658 25.900 1.00 37.60 ? 721 PRO A O 1 ATOM 5595 C CB . PRO A 1 680 ? 19.862 77.598 23.361 1.00 41.78 ? 721 PRO A CB 1 ATOM 5596 C CG . PRO A 1 680 ? 19.696 77.958 21.912 1.00 43.52 ? 721 PRO A CG 1 ATOM 5597 C CD . PRO A 1 680 ? 18.760 76.950 21.347 1.00 43.11 ? 721 PRO A CD 1 ATOM 5598 N N . SER A 1 681 ? 16.959 78.723 24.112 1.00 38.91 ? 722 SER A N 1 ATOM 5599 C CA . SER A 1 681 ? 16.077 79.592 24.927 1.00 38.67 ? 722 SER A CA 1 ATOM 5600 C C . SER A 1 681 ? 15.088 78.777 25.738 1.00 36.65 ? 722 SER A C 1 ATOM 5601 O O . SER A 1 681 ? 14.920 78.980 26.947 1.00 34.24 ? 722 SER A O 1 ATOM 5602 C CB . SER A 1 681 ? 15.338 80.622 24.049 1.00 40.01 ? 722 SER A CB 1 ATOM 5603 O OG . SER A 1 681 ? 14.549 81.472 24.870 1.00 42.16 ? 722 SER A OG 1 ATOM 5604 N N . LYS A 1 682 ? 14.432 77.826 25.079 1.00 36.56 ? 723 LYS A N 1 ATOM 5605 C CA . LYS A 1 682 ? 13.502 76.957 25.780 1.00 35.18 ? 723 LYS A CA 1 ATOM 5606 C C . LYS A 1 682 ? 14.222 76.090 26.835 1.00 32.88 ? 723 LYS A C 1 ATOM 5607 O O . LYS A 1 682 ? 13.714 75.916 27.948 1.00 31.32 ? 723 LYS A O 1 ATOM 5608 C CB . LYS A 1 682 ? 12.728 76.091 24.768 1.00 36.88 ? 723 LYS A CB 1 ATOM 5609 C CG . LYS A 1 682 ? 11.731 75.120 25.386 1.00 41.40 ? 723 LYS A CG 1 ATOM 5610 C CD . LYS A 1 682 ? 11.206 74.122 24.331 1.00 49.91 ? 723 LYS A CD 1 ATOM 5611 C CE . LYS A 1 682 ? 10.119 73.216 24.918 1.00 53.37 ? 723 LYS A CE 1 ATOM 5612 N NZ . LYS A 1 682 ? 9.618 72.244 23.891 1.00 58.37 ? 723 LYS A NZ 1 ATOM 5613 N N . ALA A 1 683 ? 15.397 75.555 26.489 1.00 31.83 ? 724 ALA A N 1 ATOM 5614 C CA . ALA A 1 683 ? 16.090 74.626 27.381 1.00 30.20 ? 724 ALA A CA 1 ATOM 5615 C C . ALA A 1 683 ? 16.548 75.386 28.633 1.00 28.48 ? 724 ALA A C 1 ATOM 5616 O O . ALA A 1 683 ? 16.334 74.920 29.746 1.00 27.32 ? 724 ALA A O 1 ATOM 5617 C CB . ALA A 1 683 ? 17.318 74.021 26.661 1.00 31.42 ? 724 ALA A CB 1 ATOM 5618 N N . TRP A 1 684 ? 17.148 76.566 28.428 1.00 29.31 ? 725 TRP A N 1 ATOM 5619 C CA . TRP A 1 684 ? 17.579 77.380 29.583 1.00 28.16 ? 725 TRP A CA 1 ATOM 5620 C C . TRP A 1 684 ? 16.382 77.933 30.379 1.00 28.03 ? 725 TRP A C 1 ATOM 5621 O O . TRP A 1 684 ? 16.479 78.061 31.600 1.00 26.51 ? 725 TRP A O 1 ATOM 5622 C CB . TRP A 1 684 ? 18.614 78.438 29.176 1.00 28.67 ? 725 TRP A CB 1 ATOM 5623 C CG . TRP A 1 684 ? 19.942 77.785 28.899 1.00 27.91 ? 725 TRP A CG 1 ATOM 5624 C CD1 . TRP A 1 684 ? 20.463 77.475 27.665 1.00 30.61 ? 725 TRP A CD1 1 ATOM 5625 C CD2 . TRP A 1 684 ? 20.900 77.372 29.864 1.00 26.97 ? 725 TRP A CD2 1 ATOM 5626 N NE1 . TRP A 1 684 ? 21.709 76.857 27.816 1.00 31.06 ? 725 TRP A NE1 1 ATOM 5627 C CE2 . TRP A 1 684 ? 21.985 76.781 29.157 1.00 28.48 ? 725 TRP A CE2 1 ATOM 5628 C CE3 . TRP A 1 684 ? 20.935 77.402 31.278 1.00 26.90 ? 725 TRP A CE3 1 ATOM 5629 C CZ2 . TRP A 1 684 ? 23.125 76.280 29.809 1.00 28.75 ? 725 TRP A CZ2 1 ATOM 5630 C CZ3 . TRP A 1 684 ? 22.073 76.893 31.928 1.00 27.49 ? 725 TRP A CZ3 1 ATOM 5631 C CH2 . TRP A 1 684 ? 23.143 76.331 31.182 1.00 28.40 ? 725 TRP A CH2 1 ATOM 5632 N N . GLY A 1 685 ? 15.254 78.229 29.717 1.00 28.49 ? 726 GLY A N 1 ATOM 5633 C CA . GLY A 1 685 ? 14.011 78.566 30.434 1.00 27.88 ? 726 GLY A CA 1 ATOM 5634 C C . GLY A 1 685 ? 13.610 77.472 31.413 1.00 26.02 ? 726 GLY A C 1 ATOM 5635 O O . GLY A 1 685 ? 13.189 77.746 32.561 1.00 26.31 ? 726 GLY A O 1 ATOM 5636 N N . GLU A 1 686 ? 13.719 76.218 30.972 1.00 25.23 ? 727 GLU A N 1 ATOM 5637 C CA . GLU A 1 686 ? 13.396 75.093 31.810 1.00 24.94 ? 727 GLU A CA 1 ATOM 5638 C C . GLU A 1 686 ? 14.396 74.906 32.935 1.00 23.10 ? 727 GLU A C 1 ATOM 5639 O O . GLU A 1 686 ? 14.026 74.539 34.024 1.00 22.61 ? 727 GLU A O 1 ATOM 5640 C CB . GLU A 1 686 ? 13.253 73.825 30.953 1.00 26.17 ? 727 GLU A CB 1 ATOM 5641 C CG A GLU A 1 686 ? 12.843 72.603 31.780 1.00 26.59 ? 727 GLU A CG 1 ATOM 5642 C CD A GLU A 1 686 ? 11.459 72.677 32.462 1.00 27.39 ? 727 GLU A CD 1 ATOM 5643 O OE1 A GLU A 1 686 ? 10.620 73.574 32.159 1.00 28.65 ? 727 GLU A OE1 1 ATOM 5644 O OE2 A GLU A 1 686 ? 11.242 71.786 33.322 1.00 28.34 ? 727 GLU A OE2 1 ATOM 5645 N N . VAL A 1 687 ? 15.687 75.204 32.694 1.00 24.14 ? 728 VAL A N 1 ATOM 5646 C CA . VAL A 1 687 ? 16.639 75.206 33.819 1.00 23.57 ? 728 VAL A CA 1 ATOM 5647 C C . VAL A 1 687 ? 16.172 76.227 34.887 1.00 23.25 ? 728 VAL A C 1 ATOM 5648 O O . VAL A 1 687 ? 16.150 75.917 36.063 1.00 21.87 ? 728 VAL A O 1 ATOM 5649 C CB . VAL A 1 687 ? 18.068 75.580 33.348 1.00 24.51 ? 728 VAL A CB 1 ATOM 5650 C CG1 . VAL A 1 687 ? 19.001 75.771 34.549 1.00 26.10 ? 728 VAL A CG1 1 ATOM 5651 C CG2 . VAL A 1 687 ? 18.591 74.477 32.337 1.00 24.39 ? 728 VAL A CG2 1 ATOM 5652 N N . LYS A 1 688 ? 15.818 77.429 34.443 1.00 24.19 ? 729 LYS A N 1 ATOM 5653 C CA . LYS A 1 688 ? 15.367 78.483 35.358 1.00 23.55 ? 729 LYS A CA 1 ATOM 5654 C C . LYS A 1 688 ? 14.092 78.056 36.069 1.00 23.47 ? 729 LYS A C 1 ATOM 5655 O O . LYS A 1 688 ? 13.977 78.259 37.245 1.00 22.08 ? 729 LYS A O 1 ATOM 5656 C CB A LYS A 1 688 ? 15.150 79.799 34.615 0.35 24.62 ? 729 LYS A CB 1 ATOM 5657 C CB B LYS A 1 688 ? 15.180 79.803 34.632 0.65 24.67 ? 729 LYS A CB 1 ATOM 5658 C CG A LYS A 1 688 ? 16.449 80.396 34.075 0.35 25.34 ? 729 LYS A CG 1 ATOM 5659 C CG B LYS A 1 688 ? 16.541 80.403 34.244 0.65 25.19 ? 729 LYS A CG 1 ATOM 5660 C CD A LYS A 1 688 ? 16.218 81.778 33.488 0.35 26.41 ? 729 LYS A CD 1 ATOM 5661 C CD B LYS A 1 688 ? 16.401 81.634 33.358 0.65 26.96 ? 729 LYS A CD 1 ATOM 5662 C CE A LYS A 1 688 ? 15.336 81.716 32.245 0.35 26.97 ? 729 LYS A CE 1 ATOM 5663 C CE B LYS A 1 688 ? 15.657 82.771 34.032 0.65 28.21 ? 729 LYS A CE 1 ATOM 5664 N NZ A LYS A 1 688 ? 15.651 82.818 31.285 0.35 30.60 ? 729 LYS A NZ 1 ATOM 5665 N NZ B LYS A 1 688 ? 15.927 84.099 33.393 0.65 31.29 ? 729 LYS A NZ 1 ATOM 5666 N N . ARG A 1 689 ? 13.195 77.389 35.357 1.00 21.59 ? 730 ARG A N 1 ATOM 5667 C CA . ARG A 1 689 ? 11.998 76.863 36.051 1.00 21.12 ? 730 ARG A CA 1 ATOM 5668 C C . ARG A 1 689 ? 12.346 75.880 37.141 1.00 20.50 ? 730 ARG A C 1 ATOM 5669 O O . ARG A 1 689 ? 11.784 75.930 38.241 1.00 19.91 ? 730 ARG A O 1 ATOM 5670 C CB . ARG A 1 689 ? 11.046 76.219 35.059 1.00 22.15 ? 730 ARG A CB 1 ATOM 5671 C CG . ARG A 1 689 ? 9.658 75.965 35.737 1.00 23.41 ? 730 ARG A CG 1 ATOM 5672 C CD . ARG A 1 689 ? 8.616 75.476 34.715 1.00 27.29 ? 730 ARG A CD 1 ATOM 5673 N NE . ARG A 1 689 ? 8.835 74.051 34.458 1.00 26.78 ? 730 ARG A NE 1 ATOM 5674 C CZ . ARG A 1 689 ? 8.352 73.072 35.235 1.00 29.41 ? 730 ARG A CZ 1 ATOM 5675 N NH1 . ARG A 1 689 ? 7.662 73.341 36.362 1.00 30.64 ? 730 ARG A NH1 1 ATOM 5676 N NH2 . ARG A 1 689 ? 8.589 71.803 34.911 1.00 29.03 ? 730 ARG A NH2 1 ATOM 5677 N N . GLN A 1 690 ? 13.277 74.964 36.857 1.00 19.68 ? 731 GLN A N 1 ATOM 5678 C CA . GLN A 1 690 ? 13.682 73.984 37.868 1.00 19.86 ? 731 GLN A CA 1 ATOM 5679 C C . GLN A 1 690 ? 14.406 74.625 39.066 1.00 19.68 ? 731 GLN A C 1 ATOM 5680 O O . GLN A 1 690 ? 14.255 74.155 40.203 1.00 19.21 ? 731 GLN A O 1 ATOM 5681 C CB . GLN A 1 690 ? 14.523 72.870 37.228 1.00 20.95 ? 731 GLN A CB 1 ATOM 5682 C CG . GLN A 1 690 ? 13.693 72.031 36.225 1.00 20.53 ? 731 GLN A CG 1 ATOM 5683 C CD . GLN A 1 690 ? 12.526 71.332 36.900 1.00 22.46 ? 731 GLN A CD 1 ATOM 5684 O OE1 . GLN A 1 690 ? 12.610 70.858 38.047 1.00 22.24 ? 731 GLN A OE1 1 ATOM 5685 N NE2 . GLN A 1 690 ? 11.375 71.294 36.194 1.00 27.87 ? 731 GLN A NE2 1 ATOM 5686 N N . ILE A 1 691 ? 15.197 75.678 38.805 1.00 20.16 ? 732 ILE A N 1 ATOM 5687 C CA . ILE A 1 691 ? 15.824 76.393 39.923 1.00 20.66 ? 732 ILE A CA 1 ATOM 5688 C C . ILE A 1 691 ? 14.743 76.979 40.832 1.00 20.52 ? 732 ILE A C 1 ATOM 5689 O O . ILE A 1 691 ? 14.843 76.866 42.076 1.00 21.34 ? 732 ILE A O 1 ATOM 5690 C CB . ILE A 1 691 ? 16.764 77.531 39.387 1.00 20.57 ? 732 ILE A CB 1 ATOM 5691 C CG1 . ILE A 1 691 ? 17.974 76.909 38.682 1.00 21.70 ? 732 ILE A CG1 1 ATOM 5692 C CG2 . ILE A 1 691 ? 17.240 78.482 40.560 1.00 23.04 ? 732 ILE A CG2 1 ATOM 5693 C CD1 . ILE A 1 691 ? 18.784 77.920 37.903 1.00 23.01 ? 732 ILE A CD1 1 ATOM 5694 N N . TYR A 1 692 ? 13.749 77.623 40.235 1.00 21.16 ? 733 TYR A N 1 ATOM 5695 C CA . TYR A 1 692 ? 12.607 78.195 40.997 1.00 21.43 ? 733 TYR A CA 1 ATOM 5696 C C . TYR A 1 692 ? 11.888 77.107 41.832 1.00 20.72 ? 733 TYR A C 1 ATOM 5697 O O . TYR A 1 692 ? 11.617 77.305 43.020 1.00 20.46 ? 733 TYR A O 1 ATOM 5698 C CB . TYR A 1 692 ? 11.633 78.811 40.014 1.00 21.70 ? 733 TYR A CB 1 ATOM 5699 C CG . TYR A 1 692 ? 10.169 79.072 40.413 1.00 24.14 ? 733 TYR A CG 1 ATOM 5700 C CD1 . TYR A 1 692 ? 9.836 79.772 41.583 1.00 25.54 ? 733 TYR A CD1 1 ATOM 5701 C CD2 . TYR A 1 692 ? 9.121 78.691 39.537 1.00 24.25 ? 733 TYR A CD2 1 ATOM 5702 C CE1 . TYR A 1 692 ? 8.443 80.096 41.860 1.00 25.65 ? 733 TYR A CE1 1 ATOM 5703 C CE2 . TYR A 1 692 ? 7.785 79.012 39.780 1.00 22.46 ? 733 TYR A CE2 1 ATOM 5704 C CZ . TYR A 1 692 ? 7.451 79.737 40.927 1.00 25.43 ? 733 TYR A CZ 1 ATOM 5705 O OH . TYR A 1 692 ? 6.099 80.054 41.165 1.00 26.71 ? 733 TYR A OH 1 ATOM 5706 N N . VAL A 1 693 ? 11.558 75.981 41.206 1.00 19.42 ? 734 VAL A N 1 ATOM 5707 C CA . VAL A 1 693 ? 10.887 74.895 41.955 1.00 18.71 ? 734 VAL A CA 1 ATOM 5708 C C . VAL A 1 693 ? 11.771 74.400 43.104 1.00 19.25 ? 734 VAL A C 1 ATOM 5709 O O . VAL A 1 693 ? 11.287 74.208 44.226 1.00 20.85 ? 734 VAL A O 1 ATOM 5710 C CB . VAL A 1 693 ? 10.563 73.736 40.968 1.00 19.11 ? 734 VAL A CB 1 ATOM 5711 C CG1 . VAL A 1 693 ? 10.100 72.484 41.783 1.00 20.87 ? 734 VAL A CG1 1 ATOM 5712 C CG2 . VAL A 1 693 ? 9.441 74.213 40.036 1.00 20.99 ? 734 VAL A CG2 1 ATOM 5713 N N . ALA A 1 694 ? 13.085 74.247 42.868 1.00 18.74 ? 735 ALA A N 1 ATOM 5714 C CA . ALA A 1 694 ? 13.980 73.745 43.937 1.00 19.57 ? 735 ALA A CA 1 ATOM 5715 C C . ALA A 1 694 ? 14.115 74.777 45.063 1.00 18.74 ? 735 ALA A C 1 ATOM 5716 O O . ALA A 1 694 ? 14.039 74.392 46.257 1.00 19.35 ? 735 ALA A O 1 ATOM 5717 C CB . ALA A 1 694 ? 15.351 73.387 43.354 1.00 19.92 ? 735 ALA A CB 1 ATOM 5718 N N . ALA A 1 695 ? 14.301 76.059 44.693 1.00 19.43 ? 736 ALA A N 1 ATOM 5719 C CA . ALA A 1 695 ? 14.441 77.132 45.724 1.00 19.29 ? 736 ALA A CA 1 ATOM 5720 C C . ALA A 1 695 ? 13.178 77.215 46.561 1.00 20.28 ? 736 ALA A C 1 ATOM 5721 O O . ALA A 1 695 ? 13.231 77.253 47.792 1.00 21.51 ? 736 ALA A O 1 ATOM 5722 C CB . ALA A 1 695 ? 14.736 78.454 45.043 1.00 20.34 ? 736 ALA A CB 1 ATOM 5723 N N . PHE A 1 696 ? 12.030 77.183 45.877 1.00 19.83 ? 737 PHE A N 1 ATOM 5724 C CA . PHE A 1 696 ? 10.755 77.244 46.575 1.00 19.48 ? 737 PHE A CA 1 ATOM 5725 C C . PHE A 1 696 ? 10.612 76.058 47.544 1.00 19.03 ? 737 PHE A C 1 ATOM 5726 O O . PHE A 1 696 ? 10.215 76.245 48.712 1.00 19.28 ? 737 PHE A O 1 ATOM 5727 C CB . PHE A 1 696 ? 9.576 77.223 45.591 1.00 20.25 ? 737 PHE A CB 1 ATOM 5728 C CG . PHE A 1 696 ? 8.285 76.874 46.274 1.00 19.77 ? 737 PHE A CG 1 ATOM 5729 C CD1 . PHE A 1 696 ? 7.738 77.759 47.253 1.00 21.90 ? 737 PHE A CD1 1 ATOM 5730 C CD2 . PHE A 1 696 ? 7.693 75.651 46.037 1.00 22.28 ? 737 PHE A CD2 1 ATOM 5731 C CE1 . PHE A 1 696 ? 6.540 77.374 47.945 1.00 23.58 ? 737 PHE A CE1 1 ATOM 5732 C CE2 . PHE A 1 696 ? 6.436 75.278 46.718 1.00 22.47 ? 737 PHE A CE2 1 ATOM 5733 C CZ . PHE A 1 696 ? 5.933 76.166 47.670 1.00 21.20 ? 737 PHE A CZ 1 ATOM 5734 N N . THR A 1 697 ? 10.976 74.861 47.083 1.00 18.27 ? 738 THR A N 1 ATOM 5735 C CA . THR A 1 697 ? 10.751 73.634 47.896 1.00 17.58 ? 738 THR A CA 1 ATOM 5736 C C . THR A 1 697 ? 11.664 73.710 49.108 1.00 18.51 ? 738 THR A C 1 ATOM 5737 O O . THR A 1 697 ? 11.247 73.375 50.205 1.00 19.30 ? 738 THR A O 1 ATOM 5738 C CB . THR A 1 697 ? 11.021 72.385 47.103 1.00 18.32 ? 738 THR A CB 1 ATOM 5739 O OG1 . THR A 1 697 ? 10.123 72.396 45.960 1.00 18.64 ? 738 THR A OG1 1 ATOM 5740 C CG2 . THR A 1 697 ? 10.643 71.171 47.992 1.00 19.46 ? 738 THR A CG2 1 ATOM 5741 N N . VAL A 1 698 ? 12.924 74.094 48.905 1.00 17.96 ? 739 VAL A N 1 ATOM 5742 C CA . VAL A 1 698 ? 13.856 74.208 50.079 1.00 18.65 ? 739 VAL A CA 1 ATOM 5743 C C . VAL A 1 698 ? 13.355 75.247 51.074 1.00 19.62 ? 739 VAL A C 1 ATOM 5744 O O . VAL A 1 698 ? 13.344 74.974 52.306 1.00 20.22 ? 739 VAL A O 1 ATOM 5745 C CB . VAL A 1 698 ? 15.283 74.552 49.609 1.00 19.17 ? 739 VAL A CB 1 ATOM 5746 C CG1 . VAL A 1 698 ? 16.195 74.903 50.816 1.00 21.72 ? 739 VAL A CG1 1 ATOM 5747 C CG2 . VAL A 1 698 ? 15.845 73.344 48.830 1.00 19.75 ? 739 VAL A CG2 1 ATOM 5748 N N . GLN A 1 699 ? 12.893 76.401 50.583 1.00 19.89 ? 740 GLN A N 1 ATOM 5749 C CA . GLN A 1 699 ? 12.360 77.434 51.518 1.00 21.02 ? 740 GLN A CA 1 ATOM 5750 C C . GLN A 1 699 ? 11.078 76.919 52.223 1.00 19.97 ? 740 GLN A C 1 ATOM 5751 O O . GLN A 1 699 ? 10.913 77.121 53.448 1.00 20.82 ? 740 GLN A O 1 ATOM 5752 C CB . GLN A 1 699 ? 12.051 78.724 50.782 1.00 21.60 ? 740 GLN A CB 1 ATOM 5753 C CG . GLN A 1 699 ? 11.458 79.798 51.712 1.00 22.10 ? 740 GLN A CG 1 ATOM 5754 C CD . GLN A 1 699 ? 12.499 80.410 52.608 1.00 24.08 ? 740 GLN A CD 1 ATOM 5755 O OE1 . GLN A 1 699 ? 13.711 80.379 52.298 1.00 24.29 ? 740 GLN A OE1 1 ATOM 5756 N NE2 . GLN A 1 699 ? 12.060 80.951 53.748 1.00 25.90 ? 740 GLN A NE2 1 ATOM 5757 N N . ALA A 1 700 ? 10.222 76.213 51.494 1.00 19.12 ? 741 ALA A N 1 ATOM 5758 C CA . ALA A 1 700 ? 8.994 75.711 52.100 1.00 20.01 ? 741 ALA A CA 1 ATOM 5759 C C . ALA A 1 700 ? 9.310 74.667 53.152 1.00 19.38 ? 741 ALA A C 1 ATOM 5760 O O . ALA A 1 700 ? 8.701 74.669 54.259 1.00 20.72 ? 741 ALA A O 1 ATOM 5761 C CB . ALA A 1 700 ? 8.084 75.107 50.991 1.00 20.06 ? 741 ALA A CB 1 ATOM 5762 N N . ALA A 1 701 ? 10.294 73.803 52.890 1.00 18.48 ? 742 ALA A N 1 ATOM 5763 C CA . ALA A 1 701 ? 10.699 72.813 53.902 1.00 18.43 ? 742 ALA A CA 1 ATOM 5764 C C . ALA A 1 701 ? 11.272 73.538 55.109 1.00 19.88 ? 742 ALA A C 1 ATOM 5765 O O . ALA A 1 701 ? 10.944 73.155 56.244 1.00 20.14 ? 742 ALA A O 1 ATOM 5766 C CB . ALA A 1 701 ? 11.748 71.848 53.326 1.00 18.07 ? 742 ALA A CB 1 ATOM 5767 N N . ALA A 1 702 ? 12.146 74.529 54.870 1.00 20.38 ? 743 ALA A N 1 ATOM 5768 C CA . ALA A 1 702 ? 12.692 75.345 55.985 1.00 21.92 ? 743 ALA A CA 1 ATOM 5769 C C . ALA A 1 702 ? 11.561 75.883 56.879 1.00 22.14 ? 743 ALA A C 1 ATOM 5770 O O . ALA A 1 702 ? 11.612 75.843 58.147 1.00 23.26 ? 743 ALA A O 1 ATOM 5771 C CB . ALA A 1 702 ? 13.525 76.481 55.433 1.00 22.29 ? 743 ALA A CB 1 ATOM 5772 N N . GLU A 1 703 ? 10.513 76.416 56.243 1.00 20.93 ? 744 GLU A N 1 ATOM 5773 C CA . GLU A 1 703 ? 9.448 77.075 56.992 1.00 21.92 ? 744 GLU A CA 1 ATOM 5774 C C . GLU A 1 703 ? 8.615 76.117 57.864 1.00 21.14 ? 744 GLU A C 1 ATOM 5775 O O . GLU A 1 703 ? 7.992 76.565 58.803 1.00 21.59 ? 744 GLU A O 1 ATOM 5776 C CB . GLU A 1 703 ? 8.543 77.899 56.041 1.00 22.83 ? 744 GLU A CB 1 ATOM 5777 C CG . GLU A 1 703 ? 9.341 79.110 55.553 1.00 24.19 ? 744 GLU A CG 1 ATOM 5778 C CD . GLU A 1 703 ? 8.578 80.030 54.604 1.00 28.30 ? 744 GLU A CD 1 ATOM 5779 O OE1 . GLU A 1 703 ? 7.425 79.710 54.238 1.00 30.49 ? 744 GLU A OE1 1 ATOM 5780 O OE2 . GLU A 1 703 ? 9.133 81.103 54.227 1.00 30.60 ? 744 GLU A OE2 1 ATOM 5781 N N . THR A 1 704 ? 8.638 74.811 57.549 1.00 21.28 ? 745 THR A N 1 ATOM 5782 C CA . THR A 1 704 ? 8.001 73.816 58.433 1.00 20.44 ? 745 THR A CA 1 ATOM 5783 C C . THR A 1 704 ? 8.711 73.706 59.775 1.00 22.06 ? 745 THR A C 1 ATOM 5784 O O . THR A 1 704 ? 8.125 73.186 60.703 1.00 22.46 ? 745 THR A O 1 ATOM 5785 C CB . THR A 1 704 ? 7.884 72.403 57.839 1.00 19.97 ? 745 THR A CB 1 ATOM 5786 O OG1 . THR A 1 704 ? 9.163 71.749 57.755 1.00 20.08 ? 745 THR A OG1 1 ATOM 5787 C CG2 . THR A 1 704 ? 7.300 72.492 56.390 1.00 20.29 ? 745 THR A CG2 1 ATOM 5788 N N . LEU A 1 705 ? 9.962 74.174 59.832 1.00 21.14 ? 746 LEU A N 1 ATOM 5789 C CA . LEU A 1 705 ? 10.726 74.150 61.110 1.00 22.37 ? 746 LEU A CA 1 ATOM 5790 C C . LEU A 1 705 ? 10.644 75.470 61.851 1.00 23.79 ? 746 LEU A C 1 ATOM 5791 O O . LEU A 1 705 ? 11.133 75.567 62.977 1.00 25.60 ? 746 LEU A O 1 ATOM 5792 C CB . LEU A 1 705 ? 12.188 73.821 60.844 1.00 21.84 ? 746 LEU A CB 1 ATOM 5793 C CG . LEU A 1 705 ? 12.426 72.502 60.106 1.00 24.16 ? 746 LEU A CG 1 ATOM 5794 C CD1 . LEU A 1 705 ? 13.934 72.375 59.829 1.00 23.93 ? 746 LEU A CD1 1 ATOM 5795 C CD2 . LEU A 1 705 ? 11.882 71.316 60.925 1.00 25.21 ? 746 LEU A CD2 1 ATOM 5796 N N . SER A 1 706 ? 10.065 76.513 61.240 1.00 23.28 ? 747 SER A N 1 ATOM 5797 C CA . SER A 1 706 ? 9.828 77.757 61.977 1.00 23.83 ? 747 SER A CA 1 ATOM 5798 C C . SER A 1 706 ? 8.856 77.534 63.156 1.00 24.20 ? 747 SER A C 1 ATOM 5799 O O . SER A 1 706 ? 8.099 76.548 63.193 1.00 24.10 ? 747 SER A O 1 ATOM 5800 C CB . SER A 1 706 ? 9.246 78.801 61.040 1.00 26.34 ? 747 SER A CB 1 ATOM 5801 O OG . SER A 1 706 ? 10.164 79.081 60.009 1.00 29.28 ? 747 SER A OG 1 ATOM 5802 N N . GLU A 1 707 ? 8.862 78.439 64.132 1.00 24.90 ? 748 GLU A N 1 ATOM 5803 C CA . GLU A 1 707 ? 7.782 78.447 65.119 1.00 28.01 ? 748 GLU A CA 1 ATOM 5804 C C . GLU A 1 707 ? 6.416 78.386 64.421 1.00 26.65 ? 748 GLU A C 1 ATOM 5805 O O . GLU A 1 707 ? 6.191 79.015 63.377 1.00 26.46 ? 748 GLU A O 1 ATOM 5806 C CB . GLU A 1 707 ? 7.887 79.653 66.070 1.00 30.33 ? 748 GLU A CB 1 ATOM 5807 C CG . GLU A 1 707 ? 9.210 79.577 66.817 1.00 34.58 ? 748 GLU A CG 1 ATOM 5808 C CD . GLU A 1 707 ? 9.276 80.439 68.043 1.00 45.54 ? 748 GLU A CD 1 ATOM 5809 O OE1 . GLU A 1 707 ? 9.515 81.652 67.895 1.00 49.00 ? 748 GLU A OE1 1 ATOM 5810 O OE2 . GLU A 1 707 ? 9.131 79.882 69.146 1.00 49.18 ? 748 GLU A OE2 1 ATOM 5811 N N . VAL A 1 708 ? 5.526 77.575 64.965 1.00 26.30 ? 749 VAL A N 1 ATOM 5812 C CA . VAL A 1 708 ? 4.301 77.213 64.202 1.00 26.06 ? 749 VAL A CA 1 ATOM 5813 C C . VAL A 1 708 ? 3.240 78.349 64.183 1.00 28.42 ? 749 VAL A C 1 ATOM 5814 O O . VAL A 1 708 ? 2.360 78.359 63.330 1.00 28.23 ? 749 VAL A O 1 ATOM 5815 C CB . VAL A 1 708 ? 3.670 75.874 64.708 1.00 26.21 ? 749 VAL A CB 1 ATOM 5816 C CG1 . VAL A 1 708 ? 4.675 74.736 64.638 1.00 26.11 ? 749 VAL A CG1 1 ATOM 5817 C CG2 . VAL A 1 708 ? 3.136 76.051 66.187 1.00 27.77 ? 749 VAL A CG2 1 ATOM 5818 N N . ALA A 1 709 ? 3.348 79.290 65.125 1.00 28.44 ? 750 ALA A N 1 ATOM 5819 C CA . ALA A 1 709 ? 2.379 80.404 65.280 1.00 30.51 ? 750 ALA A CA 1 ATOM 5820 C C . ALA A 1 709 ? 2.979 81.404 66.258 1.00 33.64 ? 750 ALA A C 1 ATOM 5821 O O . ALA A 1 709 ? 2.425 82.501 66.469 1.00 36.44 ? 750 ALA A O 1 ATOM 5822 C CB . ALA A 1 709 ? 1.063 79.913 65.816 1.00 30.77 ? 750 ALA A CB 1 ATOM 5823 O OXT . ALA A 1 709 ? 3.964 81.095 66.931 1.00 34.25 ? 750 ALA A OXT 1 HETATM 5824 ZN ZN . ZN B 2 . ? 17.500 41.069 43.239 1.00 16.65 ? 1751 ZN A ZN 1 HETATM 5825 ZN ZN . ZN C 2 . ? 16.796 41.887 46.387 1.00 15.96 ? 1752 ZN A ZN 1 HETATM 5826 CA CA . CA D 3 . ? -0.808 49.849 41.483 1.00 15.17 ? 1753 CA A CA 1 HETATM 5827 CL CL . CL E 4 . ? 19.083 46.860 51.737 1.00 20.18 ? 1754 CL A CL 1 HETATM 5828 C C1 . NAG F 5 . ? 11.721 25.973 57.789 1.00 23.38 ? 1755 NAG A C1 1 HETATM 5829 C C2 . NAG F 5 . ? 11.559 24.509 57.397 1.00 27.71 ? 1755 NAG A C2 1 HETATM 5830 C C3 . NAG F 5 . ? 10.111 24.057 57.633 1.00 27.06 ? 1755 NAG A C3 1 HETATM 5831 C C4 . NAG F 5 . ? 9.586 24.421 59.013 1.00 25.24 ? 1755 NAG A C4 1 HETATM 5832 C C5 . NAG F 5 . ? 9.954 25.873 59.359 1.00 26.54 ? 1755 NAG A C5 1 HETATM 5833 C C6 . NAG F 5 . ? 9.591 26.265 60.803 1.00 27.03 ? 1755 NAG A C6 1 HETATM 5834 C C7 . NAG F 5 . ? 13.129 23.744 55.692 1.00 34.85 ? 1755 NAG A C7 1 HETATM 5835 C C8 . NAG F 5 . ? 13.427 23.588 54.232 1.00 36.40 ? 1755 NAG A C8 1 HETATM 5836 N N2 . NAG F 5 . ? 11.954 24.316 56.018 1.00 30.43 ? 1755 NAG A N2 1 HETATM 5837 O O3 . NAG F 5 . ? 10.080 22.666 57.570 1.00 28.60 ? 1755 NAG A O3 1 HETATM 5838 O O4 . NAG F 5 . ? 8.171 24.286 58.948 1.00 27.81 ? 1755 NAG A O4 1 HETATM 5839 O O5 . NAG F 5 . ? 11.341 26.083 59.143 1.00 24.22 ? 1755 NAG A O5 1 HETATM 5840 O O6 . NAG F 5 . ? 10.161 25.305 61.676 1.00 32.31 ? 1755 NAG A O6 1 HETATM 5841 O O7 . NAG F 5 . ? 13.974 23.382 56.508 1.00 36.22 ? 1755 NAG A O7 1 HETATM 5842 C C1 . NAG G 5 . ? 7.668 23.381 59.961 1.00 31.15 ? 1756 NAG A C1 1 HETATM 5843 C C2 . NAG G 5 . ? 6.187 23.707 60.201 1.00 33.80 ? 1756 NAG A C2 1 HETATM 5844 C C3 . NAG G 5 . ? 5.578 22.705 61.190 1.00 35.70 ? 1756 NAG A C3 1 HETATM 5845 C C4 . NAG G 5 . ? 5.835 21.258 60.776 1.00 36.91 ? 1756 NAG A C4 1 HETATM 5846 C C5 . NAG G 5 . ? 7.346 21.062 60.530 1.00 36.94 ? 1756 NAG A C5 1 HETATM 5847 C C6 . NAG G 5 . ? 7.673 19.657 60.019 1.00 39.07 ? 1756 NAG A C6 1 HETATM 5848 C C7 . NAG G 5 . ? 5.648 26.177 60.101 1.00 33.47 ? 1756 NAG A C7 1 HETATM 5849 C C8 . NAG G 5 . ? 5.504 26.102 58.620 1.00 30.62 ? 1756 NAG A C8 1 HETATM 5850 N N2 . NAG G 5 . ? 5.978 25.051 60.748 1.00 29.80 ? 1756 NAG A N2 1 HETATM 5851 O O3 . NAG G 5 . ? 4.191 22.963 61.254 1.00 40.43 ? 1756 NAG A O3 1 HETATM 5852 O O4 . NAG G 5 . ? 5.300 20.373 61.769 1.00 39.25 ? 1756 NAG A O4 1 HETATM 5853 O O5 . NAG G 5 . ? 7.836 22.023 59.580 1.00 34.43 ? 1756 NAG A O5 1 HETATM 5854 O O6 . NAG G 5 . ? 7.273 19.560 58.662 1.00 40.11 ? 1756 NAG A O6 1 HETATM 5855 O O7 . NAG G 5 . ? 5.475 27.274 60.690 1.00 34.20 ? 1756 NAG A O7 1 HETATM 5856 C C1 . NAG H 5 . ? 4.056 27.954 25.269 1.00 40.06 ? 1757 NAG A C1 1 HETATM 5857 C C2 . NAG H 5 . ? 2.654 28.527 25.180 1.00 42.31 ? 1757 NAG A C2 1 HETATM 5858 C C3 . NAG H 5 . ? 1.674 27.542 24.570 1.00 45.35 ? 1757 NAG A C3 1 HETATM 5859 C C4 . NAG H 5 . ? 2.158 27.055 23.200 1.00 47.14 ? 1757 NAG A C4 1 HETATM 5860 C C5 . NAG H 5 . ? 3.676 26.803 23.068 1.00 47.62 ? 1757 NAG A C5 1 HETATM 5861 C C6 . NAG H 5 . ? 4.145 27.288 21.683 1.00 49.04 ? 1757 NAG A C6 1 HETATM 5862 C C7 . NAG H 5 . ? 1.888 30.185 26.791 1.00 43.87 ? 1757 NAG A C7 1 HETATM 5863 C C8 . NAG H 5 . ? 1.891 31.203 25.680 1.00 42.79 ? 1757 NAG A C8 1 HETATM 5864 N N2 . NAG H 5 . ? 2.243 28.929 26.513 1.00 42.45 ? 1757 NAG A N2 1 HETATM 5865 O O3 . NAG H 5 . ? 0.471 28.253 24.416 1.00 44.92 ? 1757 NAG A O3 1 HETATM 5866 O O4 . NAG H 5 . ? 1.476 25.869 22.815 1.00 50.19 ? 1757 NAG A O4 1 HETATM 5867 O O5 . NAG H 5 . ? 4.547 27.364 24.073 1.00 43.51 ? 1757 NAG A O5 1 HETATM 5868 O O6 . NAG H 5 . ? 3.463 28.473 21.279 1.00 50.06 ? 1757 NAG A O6 1 HETATM 5869 O O7 . NAG H 5 . ? 1.556 30.530 27.926 1.00 45.60 ? 1757 NAG A O7 1 HETATM 5870 C C1 . NAG I 5 . ? 19.946 24.846 17.868 1.00 29.00 ? 1758 NAG A C1 1 HETATM 5871 C C2 . NAG I 5 . ? 20.527 23.636 17.128 1.00 30.06 ? 1758 NAG A C2 1 HETATM 5872 C C3 . NAG I 5 . ? 19.690 23.368 15.879 1.00 31.12 ? 1758 NAG A C3 1 HETATM 5873 C C4 . NAG I 5 . ? 18.186 23.254 16.198 1.00 32.06 ? 1758 NAG A C4 1 HETATM 5874 C C5 . NAG I 5 . ? 17.697 24.388 17.138 1.00 30.98 ? 1758 NAG A C5 1 HETATM 5875 C C6 . NAG I 5 . ? 16.280 24.176 17.694 1.00 28.04 ? 1758 NAG A C6 1 HETATM 5876 C C7 . NAG I 5 . ? 22.957 23.357 17.383 1.00 34.32 ? 1758 NAG A C7 1 HETATM 5877 C C8 . NAG I 5 . ? 24.326 23.728 16.883 1.00 34.18 ? 1758 NAG A C8 1 HETATM 5878 N N2 . NAG I 5 . ? 21.907 23.906 16.759 1.00 32.36 ? 1758 NAG A N2 1 HETATM 5879 O O3 . NAG I 5 . ? 20.180 22.212 15.220 1.00 27.02 ? 1758 NAG A O3 1 HETATM 5880 O O4 . NAG I 5 . ? 17.477 23.279 14.971 1.00 37.74 ? 1758 NAG A O4 1 HETATM 5881 O O5 . NAG I 5 . ? 18.602 24.556 18.223 1.00 29.57 ? 1758 NAG A O5 1 HETATM 5882 O O6 . NAG I 5 . ? 16.183 23.002 18.476 1.00 27.32 ? 1758 NAG A O6 1 HETATM 5883 O O7 . NAG I 5 . ? 22.838 22.575 18.325 1.00 36.51 ? 1758 NAG A O7 1 HETATM 5884 C C1 . NAG J 5 . ? 16.494 22.219 14.860 1.00 40.78 ? 1767 NAG A C1 1 HETATM 5885 C C2 . NAG J 5 . ? 15.482 22.679 13.803 1.00 42.28 ? 1767 NAG A C2 1 HETATM 5886 C C3 . NAG J 5 . ? 14.481 21.580 13.425 1.00 44.42 ? 1767 NAG A C3 1 HETATM 5887 C C4 . NAG J 5 . ? 15.206 20.257 13.180 1.00 45.38 ? 1767 NAG A C4 1 HETATM 5888 C C5 . NAG J 5 . ? 16.054 19.917 14.417 1.00 44.31 ? 1767 NAG A C5 1 HETATM 5889 C C6 . NAG J 5 . ? 16.728 18.549 14.335 1.00 44.15 ? 1767 NAG A C6 1 HETATM 5890 C C7 . NAG J 5 . ? 15.021 25.129 13.900 1.00 39.87 ? 1767 NAG A C7 1 HETATM 5891 C C8 . NAG J 5 . ? 16.038 25.432 12.837 1.00 36.65 ? 1767 NAG A C8 1 HETATM 5892 N N2 . NAG J 5 . ? 14.803 23.865 14.295 1.00 39.49 ? 1767 NAG A N2 1 HETATM 5893 O O3 . NAG J 5 . ? 13.797 21.949 12.248 1.00 46.08 ? 1767 NAG A O3 1 HETATM 5894 O O4 . NAG J 5 . ? 14.291 19.235 12.813 1.00 47.96 ? 1767 NAG A O4 1 HETATM 5895 O O5 . NAG J 5 . ? 17.039 20.935 14.568 1.00 43.07 ? 1767 NAG A O5 1 HETATM 5896 O O6 . NAG J 5 . ? 17.551 18.491 13.189 1.00 43.45 ? 1767 NAG A O6 1 HETATM 5897 O O7 . NAG J 5 . ? 14.398 26.075 14.408 1.00 40.51 ? 1767 NAG A O7 1 HETATM 5898 C C1 . NAG K 5 . ? 19.924 54.521 10.693 1.00 53.62 ? 1759 NAG A C1 1 HETATM 5899 C C2 . NAG K 5 . ? 19.542 55.973 10.385 1.00 58.22 ? 1759 NAG A C2 1 HETATM 5900 C C3 . NAG K 5 . ? 18.041 56.050 10.093 1.00 58.62 ? 1759 NAG A C3 1 HETATM 5901 C C4 . NAG K 5 . ? 17.732 55.189 8.867 1.00 58.62 ? 1759 NAG A C4 1 HETATM 5902 C C5 . NAG K 5 . ? 18.231 53.746 9.044 1.00 57.70 ? 1759 NAG A C5 1 HETATM 5903 C C6 . NAG K 5 . ? 18.260 53.041 7.687 1.00 56.81 ? 1759 NAG A C6 1 HETATM 5904 C C7 . NAG K 5 . ? 21.084 57.621 11.361 1.00 59.97 ? 1759 NAG A C7 1 HETATM 5905 C C8 . NAG K 5 . ? 21.384 58.500 12.540 1.00 59.89 ? 1759 NAG A C8 1 HETATM 5906 N N2 . NAG K 5 . ? 19.970 56.879 11.447 1.00 59.01 ? 1759 NAG A N2 1 HETATM 5907 O O3 . NAG K 5 . ? 17.639 57.382 9.855 1.00 59.18 ? 1759 NAG A O3 1 HETATM 5908 O O4 . NAG K 5 . ? 16.341 55.207 8.606 1.00 59.79 ? 1759 NAG A O4 1 HETATM 5909 O O5 . NAG K 5 . ? 19.541 53.655 9.615 1.00 56.43 ? 1759 NAG A O5 1 HETATM 5910 O O6 . NAG K 5 . ? 17.364 51.957 7.692 1.00 56.00 ? 1759 NAG A O6 1 HETATM 5911 O O7 . NAG K 5 . ? 21.853 57.616 10.390 1.00 60.42 ? 1759 NAG A O7 1 HETATM 5912 C C1 . NAG L 5 . ? 36.483 37.859 52.695 1.00 27.87 ? 1760 NAG A C1 1 HETATM 5913 C C2 . NAG L 5 . ? 36.527 37.811 51.167 1.00 27.68 ? 1760 NAG A C2 1 HETATM 5914 C C3 . NAG L 5 . ? 37.879 37.267 50.627 1.00 31.52 ? 1760 NAG A C3 1 HETATM 5915 C C4 . NAG L 5 . ? 39.112 37.992 51.214 1.00 31.98 ? 1760 NAG A C4 1 HETATM 5916 C C5 . NAG L 5 . ? 38.929 38.097 52.742 1.00 32.85 ? 1760 NAG A C5 1 HETATM 5917 C C6 . NAG L 5 . ? 40.053 38.920 53.383 1.00 33.09 ? 1760 NAG A C6 1 HETATM 5918 C C7 . NAG L 5 . ? 34.466 37.691 49.849 1.00 22.44 ? 1760 NAG A C7 1 HETATM 5919 C C8 . NAG L 5 . ? 33.312 36.900 49.320 1.00 23.80 ? 1760 NAG A C8 1 HETATM 5920 N N2 . NAG L 5 . ? 35.363 37.101 50.637 1.00 24.90 ? 1760 NAG A N2 1 HETATM 5921 O O3 . NAG L 5 . ? 37.931 37.411 49.223 1.00 32.61 ? 1760 NAG A O3 1 HETATM 5922 O O4 . NAG L 5 . ? 40.391 37.368 50.881 1.00 31.98 ? 1760 NAG A O4 1 HETATM 5923 O O5 . NAG L 5 . ? 37.639 38.597 53.140 1.00 30.95 ? 1760 NAG A O5 1 HETATM 5924 O O6 . NAG L 5 . ? 40.122 40.228 52.838 1.00 35.92 ? 1760 NAG A O6 1 HETATM 5925 O O7 . NAG L 5 . ? 34.553 38.857 49.517 1.00 19.56 ? 1760 NAG A O7 1 HETATM 5926 C C1 . NAG M 5 . ? 24.296 61.779 68.821 1.00 20.48 ? 1761 NAG A C1 1 HETATM 5927 C C2 . NAG M 5 . ? 22.913 62.369 69.052 1.00 20.21 ? 1761 NAG A C2 1 HETATM 5928 C C3 . NAG M 5 . ? 23.098 63.815 69.482 1.00 20.73 ? 1761 NAG A C3 1 HETATM 5929 C C4 . NAG M 5 . ? 24.074 63.952 70.658 1.00 20.67 ? 1761 NAG A C4 1 HETATM 5930 C C5 . NAG M 5 . ? 25.387 63.258 70.328 1.00 19.85 ? 1761 NAG A C5 1 HETATM 5931 C C6 . NAG M 5 . ? 26.372 63.283 71.505 1.00 26.86 ? 1761 NAG A C6 1 HETATM 5932 C C7 . NAG M 5 . ? 20.930 61.774 67.690 1.00 28.50 ? 1761 NAG A C7 1 HETATM 5933 C C8 . NAG M 5 . ? 20.379 61.132 68.928 1.00 29.08 ? 1761 NAG A C8 1 HETATM 5934 N N2 . NAG M 5 . ? 22.116 62.349 67.818 1.00 21.98 ? 1761 NAG A N2 1 HETATM 5935 O O3 . NAG M 5 . ? 21.835 64.392 69.776 1.00 23.04 ? 1761 NAG A O3 1 HETATM 5936 O O4 . NAG M 5 . ? 24.392 65.312 70.839 1.00 23.09 ? 1761 NAG A O4 1 HETATM 5937 O O5 . NAG M 5 . ? 25.075 61.913 70.008 1.00 20.23 ? 1761 NAG A O5 1 HETATM 5938 O O6 . NAG M 5 . ? 25.782 62.635 72.606 1.00 28.50 ? 1761 NAG A O6 1 HETATM 5939 O O7 . NAG M 5 . ? 20.251 61.813 66.591 1.00 31.60 ? 1761 NAG A O7 1 HETATM 5940 C C1 . NAG N 5 . ? 24.100 65.753 72.179 1.00 24.60 ? 1762 NAG A C1 1 HETATM 5941 C C2 . NAG N 5 . ? 24.703 67.154 72.276 1.00 27.74 ? 1762 NAG A C2 1 HETATM 5942 C C3 . NAG N 5 . ? 24.484 67.698 73.682 1.00 30.44 ? 1762 NAG A C3 1 HETATM 5943 C C4 . NAG N 5 . ? 22.990 67.630 74.013 1.00 28.92 ? 1762 NAG A C4 1 HETATM 5944 C C5 . NAG N 5 . ? 22.450 66.218 73.796 1.00 28.84 ? 1762 NAG A C5 1 HETATM 5945 C C6 . NAG N 5 . ? 20.943 66.200 74.074 1.00 30.63 ? 1762 NAG A C6 1 HETATM 5946 C C7 . NAG N 5 . ? 26.718 67.451 70.885 1.00 32.20 ? 1762 NAG A C7 1 HETATM 5947 C C8 . NAG N 5 . ? 25.910 67.994 69.739 1.00 32.02 ? 1762 NAG A C8 1 HETATM 5948 N N2 . NAG N 5 . ? 26.129 67.079 72.027 1.00 30.97 ? 1762 NAG A N2 1 HETATM 5949 O O3 . NAG N 5 . ? 24.941 69.040 73.729 1.00 29.34 ? 1762 NAG A O3 1 HETATM 5950 O O4 . NAG N 5 . ? 22.820 67.989 75.372 1.00 31.26 ? 1762 NAG A O4 1 HETATM 5951 O O5 . NAG N 5 . ? 22.703 65.829 72.432 1.00 23.63 ? 1762 NAG A O5 1 HETATM 5952 O O6 . NAG N 5 . ? 20.258 67.153 73.267 1.00 37.49 ? 1762 NAG A O6 1 HETATM 5953 O O7 . NAG N 5 . ? 27.943 67.326 70.778 1.00 38.15 ? 1762 NAG A O7 1 HETATM 5954 C C1 . NAG O 5 . ? 15.228 83.901 52.789 1.00 17.26 ? 1763 NAG A C1 1 HETATM 5955 C C2 . NAG O 5 . ? 14.212 84.042 51.646 1.00 17.33 ? 1763 NAG A C2 1 HETATM 5956 C C3 . NAG O 5 . ? 14.092 85.523 51.286 1.00 20.67 ? 1763 NAG A C3 1 HETATM 5957 C C4 . NAG O 5 . ? 13.682 86.338 52.534 1.00 22.21 ? 1763 NAG A C4 1 HETATM 5958 C C5 . NAG O 5 . ? 14.609 86.011 53.720 1.00 24.56 ? 1763 NAG A C5 1 HETATM 5959 C C6 . NAG O 5 . ? 14.018 86.597 55.007 1.00 24.38 ? 1763 NAG A C6 1 HETATM 5960 C C7 . NAG O 5 . ? 13.763 82.539 49.775 1.00 17.58 ? 1763 NAG A C7 1 HETATM 5961 C C8 . NAG O 5 . ? 14.309 81.760 48.614 1.00 16.77 ? 1763 NAG A C8 1 HETATM 5962 N N2 . NAG O 5 . ? 14.619 83.241 50.497 1.00 15.18 ? 1763 NAG A N2 1 HETATM 5963 O O3 . NAG O 5 . ? 13.133 85.664 50.266 1.00 21.13 ? 1763 NAG A O3 1 HETATM 5964 O O4 . NAG O 5 . ? 13.868 87.732 52.358 1.00 26.27 ? 1763 NAG A O4 1 HETATM 5965 O O5 . NAG O 5 . ? 14.677 84.612 53.892 1.00 20.89 ? 1763 NAG A O5 1 HETATM 5966 O O6 . NAG O 5 . ? 15.018 86.687 56.004 1.00 34.17 ? 1763 NAG A O6 1 HETATM 5967 O O7 . NAG O 5 . ? 12.552 82.491 50.044 1.00 17.03 ? 1763 NAG A O7 1 HETATM 5968 C C1 . NAG P 5 . ? 12.746 88.240 51.616 1.00 27.83 ? 1764 NAG A C1 1 HETATM 5969 C C2 . NAG P 5 . ? 12.208 89.519 52.248 1.00 32.21 ? 1764 NAG A C2 1 HETATM 5970 C C3 . NAG P 5 . ? 11.221 90.247 51.332 1.00 31.26 ? 1764 NAG A C3 1 HETATM 5971 C C4 . NAG P 5 . ? 11.868 90.449 49.960 1.00 32.30 ? 1764 NAG A C4 1 HETATM 5972 C C5 . NAG P 5 . ? 12.189 89.029 49.485 1.00 31.26 ? 1764 NAG A C5 1 HETATM 5973 C C6 . NAG P 5 . ? 12.624 88.907 48.028 1.00 36.18 ? 1764 NAG A C6 1 HETATM 5974 C C7 . NAG P 5 . ? 12.306 89.682 54.665 1.00 37.68 ? 1764 NAG A C7 1 HETATM 5975 C C8 . NAG P 5 . ? 13.642 90.369 54.549 1.00 36.38 ? 1764 NAG A C8 1 HETATM 5976 N N2 . NAG P 5 . ? 11.640 89.274 53.564 1.00 34.29 ? 1764 NAG A N2 1 HETATM 5977 O O3 . NAG P 5 . ? 10.883 91.480 51.945 1.00 31.79 ? 1764 NAG A O3 1 HETATM 5978 O O4 . NAG P 5 . ? 10.964 90.987 49.011 1.00 31.61 ? 1764 NAG A O4 1 HETATM 5979 O O5 . NAG P 5 . ? 13.199 88.503 50.313 1.00 29.59 ? 1764 NAG A O5 1 HETATM 5980 O O6 . NAG P 5 . ? 13.979 89.243 47.890 1.00 43.01 ? 1764 NAG A O6 1 HETATM 5981 O O7 . NAG P 5 . ? 11.857 89.490 55.790 1.00 41.89 ? 1764 NAG A O7 1 HETATM 5982 C C1 . BMA Q 6 . ? 10.825 92.403 49.014 1.00 34.53 ? 1765 BMA A C1 1 HETATM 5983 C C2 . BMA Q 6 . ? 10.533 92.823 47.569 1.00 33.48 ? 1765 BMA A C2 1 HETATM 5984 C C3 . BMA Q 6 . ? 10.238 94.298 47.446 1.00 36.29 ? 1765 BMA A C3 1 HETATM 5985 C C4 . BMA Q 6 . ? 9.124 94.652 48.443 1.00 37.10 ? 1765 BMA A C4 1 HETATM 5986 C C5 . BMA Q 6 . ? 9.434 94.115 49.855 1.00 38.44 ? 1765 BMA A C5 1 HETATM 5987 C C6 . BMA Q 6 . ? 8.329 94.349 50.892 1.00 38.65 ? 1765 BMA A C6 1 HETATM 5988 O O2 . BMA Q 6 . ? 9.362 92.146 47.161 1.00 31.96 ? 1765 BMA A O2 1 HETATM 5989 O O3 . BMA Q 6 . ? 9.821 94.498 46.112 1.00 33.90 ? 1765 BMA A O3 1 HETATM 5990 O O4 . BMA Q 6 . ? 8.991 96.035 48.448 1.00 36.56 ? 1765 BMA A O4 1 HETATM 5991 O O5 . BMA Q 6 . ? 9.686 92.719 49.800 1.00 35.10 ? 1765 BMA A O5 1 HETATM 5992 O O6 . BMA Q 6 . ? 8.765 93.830 52.142 1.00 38.50 ? 1765 BMA A O6 1 HETATM 5993 C C1 . MAN R 7 . ? 10.507 95.599 45.469 1.00 36.97 ? 1766 MAN A C1 1 HETATM 5994 C C2 . MAN R 7 . ? 9.680 95.975 44.232 1.00 36.84 ? 1766 MAN A C2 1 HETATM 5995 C C3 . MAN R 7 . ? 9.785 94.862 43.175 1.00 38.54 ? 1766 MAN A C3 1 HETATM 5996 C C4 . MAN R 7 . ? 11.240 94.487 42.877 1.00 39.98 ? 1766 MAN A C4 1 HETATM 5997 C C5 . MAN R 7 . ? 11.954 94.174 44.200 1.00 38.45 ? 1766 MAN A C5 1 HETATM 5998 C C6 . MAN R 7 . ? 13.405 93.718 44.016 1.00 40.86 ? 1766 MAN A C6 1 HETATM 5999 O O2 . MAN R 7 . ? 10.139 97.225 43.745 1.00 38.22 ? 1766 MAN A O2 1 HETATM 6000 O O3 . MAN R 7 . ? 9.139 95.185 41.966 1.00 41.73 ? 1766 MAN A O3 1 HETATM 6001 O O4 . MAN R 7 . ? 11.274 93.367 41.999 1.00 40.44 ? 1766 MAN A O4 1 HETATM 6002 O O5 . MAN R 7 . ? 11.848 95.277 45.097 1.00 35.80 ? 1766 MAN A O5 1 HETATM 6003 O O6 . MAN R 7 . ? 14.171 94.800 43.521 1.00 40.49 ? 1766 MAN A O6 1 HETATM 6004 C CAR . SDR S 8 . ? 20.118 43.378 46.193 1.00 31.53 ? 1 SDR A CAR 1 HETATM 6005 O OAC . SDR S 8 . ? 19.910 44.304 47.018 1.00 33.23 ? 1 SDR A OAC 1 HETATM 6006 C CAB . SDR S 8 . ? 21.263 42.437 46.426 1.00 32.28 ? 1 SDR A CAB 1 HETATM 6007 N NAP . SDR S 8 . ? 19.832 43.588 44.880 1.00 28.88 ? 1 SDR A NAP 1 HETATM 6008 C CAW . SDR S 8 . ? 18.994 44.681 44.402 1.00 29.13 ? 1 SDR A CAW 1 HETATM 6009 C CAU . SDR S 8 . ? 18.174 44.220 43.215 1.00 29.41 ? 1 SDR A CAU 1 HETATM 6010 O OAF . SDR S 8 . ? 18.525 43.271 42.491 1.00 28.76 ? 1 SDR A OAF 1 HETATM 6011 C CAO . SDR S 8 . ? 19.811 45.906 44.005 1.00 30.41 ? 1 SDR A CAO 1 HETATM 6012 C CAS . SDR S 8 . ? 20.427 46.595 45.205 1.00 33.26 ? 1 SDR A CAS 1 HETATM 6013 O OAD . SDR S 8 . ? 21.654 46.375 45.473 1.00 34.00 ? 1 SDR A OAD 1 HETATM 6014 O OAG . SDR S 8 . ? 19.690 47.355 45.875 1.00 30.35 ? 1 SDR A OAG 1 HETATM 6015 C C . SDR S 8 . ? 17.074 44.559 40.346 1.00 29.61 ? 1 SDR A C 1 HETATM 6016 N N . SDR S 8 . ? 17.016 44.894 42.735 1.00 28.46 ? 1 SDR A N 1 HETATM 6017 O O . SDR S 8 . ? 16.831 43.740 39.450 1.00 27.72 ? 1 SDR A O 1 HETATM 6018 C CA . SDR S 8 . ? 16.223 44.474 41.572 1.00 29.22 ? 1 SDR A CA 1 HETATM 6019 C CB . SDR S 8 . ? 15.156 45.552 41.523 1.00 30.69 ? 1 SDR A CB 1 HETATM 6020 C CAI . SDR S 8 . ? 14.648 49.900 39.636 1.00 39.90 ? 1 SDR A CAI 1 HETATM 6021 C CAJ . SDR S 8 . ? 14.466 48.404 39.478 1.00 34.39 ? 1 SDR A CAJ 1 HETATM 6022 C CAK . SDR S 8 . ? 13.681 47.817 40.626 1.00 34.52 ? 1 SDR A CAK 1 HETATM 6023 C CAL . SDR S 8 . ? 13.110 46.421 40.332 1.00 33.68 ? 1 SDR A CAL 1 HETATM 6024 C CAM . SDR S 8 . ? 14.088 45.234 40.499 1.00 33.29 ? 1 SDR A CAM 1 HETATM 6025 O OXT . SDR S 8 . ? 18.010 45.404 40.292 1.00 30.51 ? 1 SDR A OXT 1 HETATM 6026 O O . HOH T 9 . ? 8.209 44.636 46.402 1.00 14.99 ? 1800 HOH A O 1 HETATM 6027 O O . HOH T 9 . ? 6.793 58.313 37.489 1.00 17.62 ? 1801 HOH A O 1 HETATM 6028 O O . HOH T 9 . ? 7.964 69.535 59.149 1.00 15.62 ? 1802 HOH A O 1 HETATM 6029 O O . HOH T 9 . ? 13.718 44.668 49.887 1.00 18.43 ? 1803 HOH A O 1 HETATM 6030 O O . HOH T 9 . ? 9.271 50.596 46.529 1.00 18.21 ? 1804 HOH A O 1 HETATM 6031 O O . HOH T 9 . ? 0.969 50.427 39.943 1.00 15.76 ? 1805 HOH A O 1 HETATM 6032 O O . HOH T 9 . ? 11.904 61.660 43.737 1.00 22.31 ? 1806 HOH A O 1 HETATM 6033 O O . HOH T 9 . ? 13.558 29.721 40.126 1.00 17.02 ? 1807 HOH A O 1 HETATM 6034 O O . HOH T 9 . ? 15.139 41.819 38.896 1.00 17.53 ? 1808 HOH A O 1 HETATM 6035 O O . HOH T 9 . ? 9.586 60.819 57.705 1.00 15.04 ? 1809 HOH A O 1 HETATM 6036 O O . HOH T 9 . ? 10.852 36.639 42.357 1.00 14.64 ? 1810 HOH A O 1 HETATM 6037 O O . HOH T 9 . ? -5.416 59.636 59.820 1.00 16.20 ? 1811 HOH A O 1 HETATM 6038 O O . HOH T 9 . ? 13.722 26.989 51.689 1.00 16.26 ? 1812 HOH A O 1 HETATM 6039 O O . HOH T 9 . ? 7.480 71.759 45.296 1.00 18.33 ? 1813 HOH A O 1 HETATM 6040 O O . HOH T 9 . ? 5.763 68.901 55.411 1.00 17.80 ? 1814 HOH A O 1 HETATM 6041 O O . HOH T 9 . ? 16.876 37.035 43.937 1.00 16.81 ? 1815 HOH A O 1 HETATM 6042 O O . HOH T 9 . ? -3.613 62.121 53.943 1.00 19.14 ? 1816 HOH A O 1 HETATM 6043 O O . HOH T 9 . ? 29.502 36.149 44.300 1.00 15.45 ? 1817 HOH A O 1 HETATM 6044 O O . HOH T 9 . ? 6.414 75.921 61.013 1.00 15.84 ? 1818 HOH A O 1 HETATM 6045 O O . HOH T 9 . ? -3.470 60.056 61.844 1.00 16.80 ? 1819 HOH A O 1 HETATM 6046 O O . HOH T 9 . ? 19.272 47.786 54.797 1.00 18.48 ? 1820 HOH A O 1 HETATM 6047 O O . HOH T 9 . ? 3.957 70.379 64.458 1.00 17.40 ? 1821 HOH A O 1 HETATM 6048 O O . HOH T 9 . ? -7.011 51.513 51.551 1.00 19.64 ? 1822 HOH A O 1 HETATM 6049 O O . HOH T 9 . ? 17.887 40.558 32.311 1.00 18.22 ? 1823 HOH A O 1 HETATM 6050 O O . HOH T 9 . ? 20.036 61.455 62.962 1.00 16.91 ? 1824 HOH A O 1 HETATM 6051 O O . HOH T 9 . ? -4.440 59.429 57.255 1.00 17.07 ? 1825 HOH A O 1 HETATM 6052 O O . HOH T 9 . ? 3.672 71.963 43.602 1.00 17.73 ? 1826 HOH A O 1 HETATM 6053 O O . HOH T 9 . ? 29.988 42.651 32.200 1.00 20.24 ? 1827 HOH A O 1 HETATM 6054 O O . HOH T 9 . ? 23.971 46.114 34.719 1.00 19.14 ? 1828 HOH A O 1 HETATM 6055 O O . HOH T 9 . ? 14.760 36.731 28.087 1.00 16.88 ? 1829 HOH A O 1 HETATM 6056 O O . HOH T 9 . ? 18.512 33.464 43.480 1.00 18.70 ? 1830 HOH A O 1 HETATM 6057 O O . HOH T 9 . ? 28.910 33.834 32.827 1.00 18.34 ? 1831 HOH A O 1 HETATM 6058 O O . HOH T 9 . ? 5.999 75.319 54.194 1.00 19.85 ? 1832 HOH A O 1 HETATM 6059 O O . HOH T 9 . ? 3.621 62.243 50.554 1.00 20.18 ? 1833 HOH A O 1 HETATM 6060 O O . HOH T 9 . ? 14.637 32.073 48.160 1.00 16.18 ? 1834 HOH A O 1 HETATM 6061 O O . HOH T 9 . ? 4.525 34.857 45.484 1.00 19.42 ? 1835 HOH A O 1 HETATM 6062 O O . HOH T 9 . ? 0.255 56.853 45.701 1.00 21.92 ? 1836 HOH A O 1 HETATM 6063 O O . HOH T 9 . ? 0.263 65.251 66.060 0.50 17.29 ? 1837 HOH A O 1 HETATM 6064 O O . HOH T 9 . ? -0.299 43.391 60.839 1.00 22.14 ? 1838 HOH A O 1 HETATM 6065 O O . HOH T 9 . ? 14.525 38.053 34.978 1.00 18.34 ? 1839 HOH A O 1 HETATM 6066 O O . HOH T 9 . ? 22.389 87.922 32.602 1.00 14.52 ? 1840 HOH A O 1 HETATM 6067 O O . HOH T 9 . ? 23.310 67.647 34.261 1.00 19.86 ? 1841 HOH A O 1 HETATM 6068 O O . HOH T 9 . ? 23.347 68.659 43.162 1.00 18.01 ? 1842 HOH A O 1 HETATM 6069 O O . HOH T 9 . ? 20.699 45.755 36.451 1.00 20.51 ? 1843 HOH A O 1 HETATM 6070 O O . HOH T 9 . ? 24.501 37.236 32.519 1.00 16.52 ? 1844 HOH A O 1 HETATM 6071 O O . HOH T 9 . ? 16.264 55.953 35.274 1.00 25.99 ? 1845 HOH A O 1 HETATM 6072 O O . HOH T 9 . ? 25.815 37.013 38.094 1.00 18.57 ? 1846 HOH A O 1 HETATM 6073 O O . HOH T 9 . ? 9.541 29.117 43.137 1.00 17.42 ? 1847 HOH A O 1 HETATM 6074 O O . HOH T 9 . ? 27.576 31.069 28.896 1.00 19.01 ? 1848 HOH A O 1 HETATM 6075 O O . HOH T 9 . ? 20.806 27.474 48.847 1.00 18.20 ? 1849 HOH A O 1 HETATM 6076 O O . HOH T 9 . ? 10.110 30.870 26.812 1.00 19.44 ? 1850 HOH A O 1 HETATM 6077 O O . HOH T 9 . ? 29.059 60.604 57.453 1.00 22.93 ? 1851 HOH A O 1 HETATM 6078 O O . HOH T 9 . ? 19.290 35.994 43.159 1.00 19.46 ? 1852 HOH A O 1 HETATM 6079 O O . HOH T 9 . ? 20.158 31.134 43.564 1.00 19.34 ? 1853 HOH A O 1 HETATM 6080 O O . HOH T 9 . ? 8.145 50.391 40.706 1.00 25.15 ? 1854 HOH A O 1 HETATM 6081 O O . HOH T 9 . ? -2.649 44.100 37.831 1.00 17.90 ? 1855 HOH A O 1 HETATM 6082 O O . HOH T 9 . ? 6.534 60.774 67.185 1.00 18.49 ? 1856 HOH A O 1 HETATM 6083 O O . HOH T 9 . ? 5.112 64.696 37.104 1.00 21.01 ? 1857 HOH A O 1 HETATM 6084 O O . HOH T 9 . ? 14.817 80.821 38.334 1.00 16.10 ? 1858 HOH A O 1 HETATM 6085 O O . HOH T 9 . ? 6.959 55.358 43.603 1.00 25.46 ? 1859 HOH A O 1 HETATM 6086 O O . HOH T 9 . ? 13.969 40.753 53.515 1.00 18.73 ? 1860 HOH A O 1 HETATM 6087 O O . HOH T 9 . ? 11.220 27.460 54.357 1.00 19.44 ? 1861 HOH A O 1 HETATM 6088 O O . HOH T 9 . ? 23.175 44.450 36.667 1.00 22.84 ? 1862 HOH A O 1 HETATM 6089 O O . HOH T 9 . ? 13.940 68.049 34.813 1.00 19.72 ? 1863 HOH A O 1 HETATM 6090 O O . HOH T 9 . ? 4.356 66.973 51.515 1.00 18.49 ? 1864 HOH A O 1 HETATM 6091 O O . HOH T 9 . ? 4.102 68.588 49.320 1.00 21.45 ? 1865 HOH A O 1 HETATM 6092 O O . HOH T 9 . ? -4.556 55.176 51.823 1.00 20.51 ? 1866 HOH A O 1 HETATM 6093 O O . HOH T 9 . ? 1.378 59.245 46.402 1.00 22.09 ? 1867 HOH A O 1 HETATM 6094 O O . HOH T 9 . ? 2.590 33.027 45.426 1.00 20.20 ? 1868 HOH A O 1 HETATM 6095 O O . HOH T 9 . ? -3.903 57.604 46.390 1.00 25.84 ? 1869 HOH A O 1 HETATM 6096 O O . HOH T 9 . ? 11.126 63.350 58.299 1.00 22.94 ? 1870 HOH A O 1 HETATM 6097 O O . HOH T 9 . ? 28.542 53.856 53.033 1.00 19.49 ? 1871 HOH A O 1 HETATM 6098 O O . HOH T 9 . ? 13.741 71.422 40.548 1.00 18.45 ? 1872 HOH A O 1 HETATM 6099 O O . HOH T 9 . ? 19.056 27.681 35.142 1.00 20.80 ? 1873 HOH A O 1 HETATM 6100 O O . HOH T 9 . ? 13.335 77.726 63.641 1.00 22.00 ? 1874 HOH A O 1 HETATM 6101 O O . HOH T 9 . ? 34.398 41.895 50.104 1.00 22.20 ? 1875 HOH A O 1 HETATM 6102 O O . HOH T 9 . ? 26.501 38.914 36.292 1.00 19.40 ? 1876 HOH A O 1 HETATM 6103 O O . HOH T 9 . ? -2.598 59.268 48.623 1.00 22.97 ? 1877 HOH A O 1 HETATM 6104 O O . HOH T 9 . ? 8.793 74.595 66.740 1.00 21.19 ? 1878 HOH A O 1 HETATM 6105 O O . HOH T 9 . ? 24.320 31.539 28.790 1.00 19.55 ? 1879 HOH A O 1 HETATM 6106 O O . HOH T 9 . ? 5.587 62.604 65.061 1.00 22.70 ? 1880 HOH A O 1 HETATM 6107 O O . HOH T 9 . ? 14.249 31.778 29.615 1.00 19.54 ? 1881 HOH A O 1 HETATM 6108 O O . HOH T 9 . ? 12.124 34.990 53.708 1.00 19.58 ? 1882 HOH A O 1 HETATM 6109 O O . HOH T 9 . ? 10.700 37.377 54.447 1.00 26.58 ? 1883 HOH A O 1 HETATM 6110 O O . HOH T 9 . ? 21.159 63.492 61.073 1.00 19.67 ? 1884 HOH A O 1 HETATM 6111 O O . HOH T 9 . ? 3.556 27.492 41.441 1.00 24.09 ? 1885 HOH A O 1 HETATM 6112 O O . HOH T 9 . ? 19.560 53.526 45.241 1.00 25.94 ? 1886 HOH A O 1 HETATM 6113 O O . HOH T 9 . ? 19.261 60.045 50.032 1.00 24.79 ? 1887 HOH A O 1 HETATM 6114 O O . HOH T 9 . ? 20.468 52.978 47.759 1.00 25.73 ? 1888 HOH A O 1 HETATM 6115 O O . HOH T 9 . ? 31.185 40.266 46.498 1.00 19.62 ? 1889 HOH A O 1 HETATM 6116 O O . HOH T 9 . ? 5.440 78.023 54.497 1.00 21.72 ? 1890 HOH A O 1 HETATM 6117 O O . HOH T 9 . ? 32.369 35.220 59.138 1.00 19.69 ? 1891 HOH A O 1 HETATM 6118 O O . HOH T 9 . ? 21.949 61.541 36.989 1.00 30.37 ? 1892 HOH A O 1 HETATM 6119 O O . HOH T 9 . ? 16.317 72.192 29.741 1.00 18.04 ? 1893 HOH A O 1 HETATM 6120 O O . HOH T 9 . ? 14.659 58.818 74.603 1.00 18.32 ? 1894 HOH A O 1 HETATM 6121 O O . HOH T 9 . ? 29.537 70.290 46.231 1.00 20.07 ? 1895 HOH A O 1 HETATM 6122 O O . HOH T 9 . ? -2.261 55.517 46.234 1.00 23.23 ? 1896 HOH A O 1 HETATM 6123 O O . HOH T 9 . ? 24.135 40.619 69.414 1.00 20.85 ? 1897 HOH A O 1 HETATM 6124 O O . HOH T 9 . ? 5.681 62.783 70.575 1.00 17.70 ? 1898 HOH A O 1 HETATM 6125 O O . HOH T 9 . ? 16.710 68.148 64.361 1.00 18.50 ? 1899 HOH A O 1 HETATM 6126 O O . HOH T 9 . ? 25.254 32.835 67.782 1.00 21.08 ? 1900 HOH A O 1 HETATM 6127 O O . HOH T 9 . ? -6.269 58.602 38.059 1.00 25.17 ? 1901 HOH A O 1 HETATM 6128 O O . HOH T 9 . ? 15.006 61.836 73.227 1.00 22.54 ? 1902 HOH A O 1 HETATM 6129 O O . HOH T 9 . ? 0.257 31.330 58.268 1.00 23.04 ? 1903 HOH A O 1 HETATM 6130 O O . HOH T 9 . ? 18.339 55.434 30.539 1.00 34.71 ? 1904 HOH A O 1 HETATM 6131 O O . HOH T 9 . ? 9.137 69.015 40.968 1.00 20.21 ? 1905 HOH A O 1 HETATM 6132 O O . HOH T 9 . ? 12.111 36.906 28.723 1.00 19.28 ? 1906 HOH A O 1 HETATM 6133 O O . HOH T 9 . ? 0.442 33.234 43.496 1.00 20.54 ? 1907 HOH A O 1 HETATM 6134 O O . HOH T 9 . ? 1.080 63.256 43.033 1.00 28.75 ? 1908 HOH A O 1 HETATM 6135 O O . HOH T 9 . ? 33.898 48.000 58.999 1.00 22.90 ? 1909 HOH A O 1 HETATM 6136 O O . HOH T 9 . ? 17.268 81.756 37.465 1.00 20.93 ? 1910 HOH A O 1 HETATM 6137 O O A HOH T 9 . ? 14.878 68.668 41.729 0.50 17.11 ? 1911 HOH A O 1 HETATM 6138 O O B HOH T 9 . ? 15.669 69.833 41.195 0.50 18.12 ? 1911 HOH A O 1 HETATM 6139 O O . HOH T 9 . ? 16.395 26.074 34.679 1.00 22.57 ? 1912 HOH A O 1 HETATM 6140 O O . HOH T 9 . ? 23.185 55.085 31.353 1.00 27.72 ? 1913 HOH A O 1 HETATM 6141 O O . HOH T 9 . ? 17.731 82.527 41.275 1.00 27.17 ? 1914 HOH A O 1 HETATM 6142 O O . HOH T 9 . ? 24.123 75.013 54.651 1.00 22.57 ? 1915 HOH A O 1 HETATM 6143 O O . HOH T 9 . ? 23.132 67.551 40.812 1.00 26.24 ? 1916 HOH A O 1 HETATM 6144 O O . HOH T 9 . ? 8.139 51.802 43.625 1.00 37.96 ? 1917 HOH A O 1 HETATM 6145 O O . HOH T 9 . ? 30.085 27.033 33.743 1.00 22.08 ? 1918 HOH A O 1 HETATM 6146 O O . HOH T 9 . ? 6.231 38.719 26.587 1.00 29.54 ? 1919 HOH A O 1 HETATM 6147 O O . HOH T 9 . ? 18.862 69.009 65.891 1.00 24.64 ? 1920 HOH A O 1 HETATM 6148 O O . HOH T 9 . ? 25.713 58.708 46.304 1.00 23.04 ? 1921 HOH A O 1 HETATM 6149 O O . HOH T 9 . ? 21.892 74.513 60.742 1.00 23.59 ? 1922 HOH A O 1 HETATM 6150 O O . HOH T 9 . ? -2.213 33.845 40.749 1.00 22.56 ? 1923 HOH A O 1 HETATM 6151 O O . HOH T 9 . ? 13.481 82.762 55.795 1.00 25.62 ? 1924 HOH A O 1 HETATM 6152 O O . HOH T 9 . ? 25.826 35.570 68.161 1.00 19.09 ? 1925 HOH A O 1 HETATM 6153 O O . HOH T 9 . ? 23.817 73.155 59.515 1.00 22.73 ? 1926 HOH A O 1 HETATM 6154 O O . HOH T 9 . ? -1.311 61.518 62.262 1.00 26.04 ? 1927 HOH A O 1 HETATM 6155 O O . HOH T 9 . ? 10.105 35.975 70.036 1.00 25.92 ? 1928 HOH A O 1 HETATM 6156 O O . HOH T 9 . ? 14.011 57.666 35.102 1.00 26.67 ? 1929 HOH A O 1 HETATM 6157 O O . HOH T 9 . ? 13.509 29.437 28.638 1.00 21.74 ? 1930 HOH A O 1 HETATM 6158 O O . HOH T 9 . ? 36.739 42.415 65.238 1.00 20.85 ? 1931 HOH A O 1 HETATM 6159 O O . HOH T 9 . ? 10.816 28.934 40.493 1.00 23.24 ? 1932 HOH A O 1 HETATM 6160 O O . HOH T 9 . ? 11.779 40.869 55.398 1.00 20.46 ? 1933 HOH A O 1 HETATM 6161 O O . HOH T 9 . ? 23.366 56.585 45.217 1.00 31.04 ? 1934 HOH A O 1 HETATM 6162 O O . HOH T 9 . ? 25.679 27.045 24.520 1.00 24.75 ? 1935 HOH A O 1 HETATM 6163 O O . HOH T 9 . ? 25.552 55.987 37.574 1.00 28.56 ? 1936 HOH A O 1 HETATM 6164 O O . HOH T 9 . ? 20.210 31.329 26.412 1.00 23.48 ? 1937 HOH A O 1 HETATM 6165 O O . HOH T 9 . ? 30.863 52.369 52.758 1.00 23.65 ? 1938 HOH A O 1 HETATM 6166 O O . HOH T 9 . ? 6.524 76.294 67.440 1.00 23.18 ? 1939 HOH A O 1 HETATM 6167 O O . HOH T 9 . ? 21.275 32.316 28.714 1.00 19.65 ? 1940 HOH A O 1 HETATM 6168 O O . HOH T 9 . ? 25.434 70.542 31.363 1.00 23.17 ? 1941 HOH A O 1 HETATM 6169 O O . HOH T 9 . ? 19.154 69.570 28.617 1.00 24.88 ? 1942 HOH A O 1 HETATM 6170 O O . HOH T 9 . ? 23.555 78.872 50.664 1.00 19.25 ? 1943 HOH A O 1 HETATM 6171 O O . HOH T 9 . ? -9.904 45.788 34.448 1.00 34.04 ? 1944 HOH A O 1 HETATM 6172 O O . HOH T 9 . ? 29.240 40.262 64.843 1.00 22.72 ? 1945 HOH A O 1 HETATM 6173 O O . HOH T 9 . ? 11.578 27.664 29.433 1.00 26.30 ? 1946 HOH A O 1 HETATM 6174 O O . HOH T 9 . ? 25.324 63.331 50.075 1.00 23.58 ? 1947 HOH A O 1 HETATM 6175 O O . HOH T 9 . ? 16.160 29.014 28.176 1.00 22.17 ? 1948 HOH A O 1 HETATM 6176 O O . HOH T 9 . ? 13.809 79.842 68.049 1.00 25.51 ? 1949 HOH A O 1 HETATM 6177 O O . HOH T 9 . ? 4.949 31.526 30.589 1.00 32.98 ? 1950 HOH A O 1 HETATM 6178 O O . HOH T 9 . ? 14.314 81.305 40.859 1.00 31.33 ? 1951 HOH A O 1 HETATM 6179 O O . HOH T 9 . ? 10.289 81.044 63.731 1.00 23.69 ? 1952 HOH A O 1 HETATM 6180 O O . HOH T 9 . ? 4.160 63.402 72.830 1.00 20.81 ? 1953 HOH A O 1 HETATM 6181 O O . HOH T 9 . ? -10.514 48.523 48.673 1.00 27.18 ? 1954 HOH A O 1 HETATM 6182 O O . HOH T 9 . ? 21.712 84.038 47.315 1.00 21.93 ? 1955 HOH A O 1 HETATM 6183 O O . HOH T 9 . ? 27.187 53.956 50.560 1.00 22.82 ? 1956 HOH A O 1 HETATM 6184 O O . HOH T 9 . ? 20.934 50.375 76.147 1.00 29.20 ? 1957 HOH A O 1 HETATM 6185 O O . HOH T 9 . ? 7.506 38.517 29.358 1.00 26.59 ? 1958 HOH A O 1 HETATM 6186 O O . HOH T 9 . ? 38.306 34.311 26.561 1.00 31.03 ? 1959 HOH A O 1 HETATM 6187 O O . HOH T 9 . ? 4.615 62.046 75.205 1.00 15.96 ? 1960 HOH A O 1 HETATM 6188 O O . HOH T 9 . ? -1.638 32.103 44.728 1.00 29.60 ? 1961 HOH A O 1 HETATM 6189 O O . HOH T 9 . ? -12.946 47.229 37.763 1.00 26.79 ? 1962 HOH A O 1 HETATM 6190 O O . HOH T 9 . ? 29.493 50.447 39.043 1.00 32.40 ? 1963 HOH A O 1 HETATM 6191 O O . HOH T 9 . ? 19.515 49.974 44.924 1.00 31.76 ? 1964 HOH A O 1 HETATM 6192 O O . HOH T 9 . ? -10.145 43.721 47.167 1.00 29.63 ? 1965 HOH A O 1 HETATM 6193 O O . HOH T 9 . ? 30.080 25.255 47.500 1.00 25.29 ? 1966 HOH A O 1 HETATM 6194 O O . HOH T 9 . ? 29.483 54.401 34.804 1.00 30.71 ? 1967 HOH A O 1 HETATM 6195 O O . HOH T 9 . ? -0.738 58.057 43.338 1.00 20.14 ? 1968 HOH A O 1 HETATM 6196 O O . HOH T 9 . ? 22.629 58.436 24.601 1.00 29.87 ? 1969 HOH A O 1 HETATM 6197 O O . HOH T 9 . ? -3.059 38.618 63.026 1.00 26.21 ? 1970 HOH A O 1 HETATM 6198 O O . HOH T 9 . ? 11.665 38.370 56.625 1.00 28.87 ? 1971 HOH A O 1 HETATM 6199 O O . HOH T 9 . ? 25.695 66.968 30.221 1.00 24.88 ? 1972 HOH A O 1 HETATM 6200 O O . HOH T 9 . ? 16.534 69.438 20.993 1.00 50.49 ? 1973 HOH A O 1 HETATM 6201 O O . HOH T 9 . ? 12.071 63.850 35.702 1.00 31.45 ? 1974 HOH A O 1 HETATM 6202 O O . HOH T 9 . ? 25.128 65.752 40.202 1.00 34.18 ? 1975 HOH A O 1 HETATM 6203 O O . HOH T 9 . ? 31.879 55.211 26.262 1.00 27.41 ? 1976 HOH A O 1 HETATM 6204 O O . HOH T 9 . ? 17.962 30.794 29.260 1.00 21.66 ? 1977 HOH A O 1 HETATM 6205 O O . HOH T 9 . ? 28.977 26.004 36.157 1.00 24.45 ? 1978 HOH A O 1 HETATM 6206 O O . HOH T 9 . ? 16.661 79.608 21.246 1.00 31.27 ? 1979 HOH A O 1 HETATM 6207 O O . HOH T 9 . ? 19.962 25.592 36.911 1.00 22.44 ? 1980 HOH A O 1 HETATM 6208 O O . HOH T 9 . ? 28.109 45.180 68.975 1.00 22.69 ? 1981 HOH A O 1 HETATM 6209 O O . HOH T 9 . ? 17.800 52.320 75.162 1.00 24.77 ? 1982 HOH A O 1 HETATM 6210 O O . HOH T 9 . ? 13.525 93.434 40.569 1.00 31.67 ? 1983 HOH A O 1 HETATM 6211 O O . HOH T 9 . ? 0.427 33.391 36.659 1.00 36.89 ? 1984 HOH A O 1 HETATM 6212 O O . HOH T 9 . ? 30.724 48.910 47.175 1.00 35.63 ? 1985 HOH A O 1 HETATM 6213 O O . HOH T 9 . ? 25.582 25.451 20.141 1.00 26.84 ? 1986 HOH A O 1 HETATM 6214 O O . HOH T 9 . ? 35.019 51.026 31.216 1.00 36.20 ? 1987 HOH A O 1 HETATM 6215 O O . HOH T 9 . ? 20.574 30.191 29.935 1.00 21.52 ? 1988 HOH A O 1 HETATM 6216 O O . HOH T 9 . ? 12.838 69.455 32.758 1.00 28.53 ? 1989 HOH A O 1 HETATM 6217 O O . HOH T 9 . ? 24.619 29.433 30.499 1.00 22.69 ? 1990 HOH A O 1 HETATM 6218 O O . HOH T 9 . ? 26.379 40.128 13.408 1.00 23.33 ? 1991 HOH A O 1 HETATM 6219 O O . HOH T 9 . ? -2.704 32.880 56.024 1.00 32.28 ? 1992 HOH A O 1 HETATM 6220 O O . HOH T 9 . ? 24.193 82.112 42.356 1.00 26.38 ? 1993 HOH A O 1 HETATM 6221 O O . HOH T 9 . ? 29.452 78.851 27.692 1.00 31.30 ? 1994 HOH A O 1 HETATM 6222 O O . HOH T 9 . ? 10.509 27.145 51.734 1.00 22.70 ? 1995 HOH A O 1 HETATM 6223 O O . HOH T 9 . ? 5.103 40.201 23.377 1.00 32.74 ? 1996 HOH A O 1 HETATM 6224 O O . HOH T 9 . ? 36.143 43.067 57.341 1.00 24.95 ? 1997 HOH A O 1 HETATM 6225 O O . HOH T 9 . ? 36.794 52.347 68.607 1.00 25.42 ? 1998 HOH A O 1 HETATM 6226 O O . HOH T 9 . ? 9.913 69.962 38.650 1.00 27.84 ? 1999 HOH A O 1 HETATM 6227 O O . HOH T 9 . ? 22.965 65.372 66.118 1.00 27.63 ? 2000 HOH A O 1 HETATM 6228 O O . HOH T 9 . ? 27.291 56.978 70.469 1.00 24.10 ? 2001 HOH A O 1 HETATM 6229 O O . HOH T 9 . ? 6.994 75.971 37.772 1.00 23.99 ? 2002 HOH A O 1 HETATM 6230 O O . HOH T 9 . ? 34.780 41.302 19.364 1.00 33.31 ? 2003 HOH A O 1 HETATM 6231 O O . HOH T 9 . ? 39.703 43.844 58.198 1.00 24.06 ? 2004 HOH A O 1 HETATM 6232 O O . HOH T 9 . ? 27.166 17.045 40.353 1.00 30.08 ? 2005 HOH A O 1 HETATM 6233 O O . HOH T 9 . ? 27.921 72.288 53.370 1.00 27.78 ? 2006 HOH A O 1 HETATM 6234 O O . HOH T 9 . ? 30.831 41.444 40.282 1.00 29.34 ? 2007 HOH A O 1 HETATM 6235 O O . HOH T 9 . ? 26.502 60.218 30.929 1.00 34.07 ? 2008 HOH A O 1 HETATM 6236 O O . HOH T 9 . ? -1.632 46.009 55.880 1.00 29.42 ? 2009 HOH A O 1 HETATM 6237 O O . HOH T 9 . ? 1.645 31.041 64.930 1.00 31.15 ? 2010 HOH A O 1 HETATM 6238 O O . HOH T 9 . ? 21.531 25.003 24.044 1.00 26.41 ? 2011 HOH A O 1 HETATM 6239 O O . HOH T 9 . ? 0.787 66.130 63.018 1.00 31.37 ? 2012 HOH A O 1 HETATM 6240 O O . HOH T 9 . ? 24.047 61.273 35.054 1.00 31.37 ? 2013 HOH A O 1 HETATM 6241 O O . HOH T 9 . ? 11.135 76.669 28.662 1.00 27.39 ? 2014 HOH A O 1 HETATM 6242 O O . HOH T 9 . ? 26.489 23.522 45.759 1.00 24.26 ? 2015 HOH A O 1 HETATM 6243 O O . HOH T 9 . ? -3.989 37.424 56.628 1.00 35.27 ? 2016 HOH A O 1 HETATM 6244 O O . HOH T 9 . ? 16.165 67.387 72.706 1.00 36.71 ? 2017 HOH A O 1 HETATM 6245 O O . HOH T 9 . ? 5.273 66.204 33.929 1.00 38.24 ? 2018 HOH A O 1 HETATM 6246 O O . HOH T 9 . ? -3.098 37.703 32.759 1.00 25.36 ? 2019 HOH A O 1 HETATM 6247 O O . HOH T 9 . ? 24.322 77.710 53.233 1.00 26.74 ? 2020 HOH A O 1 HETATM 6248 O O . HOH T 9 . ? 20.935 74.522 23.862 1.00 32.21 ? 2021 HOH A O 1 HETATM 6249 O O . HOH T 9 . ? 10.402 51.638 39.656 1.00 26.21 ? 2022 HOH A O 1 HETATM 6250 O O . HOH T 9 . ? 0.361 63.222 48.073 1.00 30.22 ? 2023 HOH A O 1 HETATM 6251 O O . HOH T 9 . ? 26.711 66.074 26.593 1.00 28.21 ? 2024 HOH A O 1 HETATM 6252 O O . HOH T 9 . ? 31.662 46.867 36.562 1.00 31.66 ? 2025 HOH A O 1 HETATM 6253 O O . HOH T 9 . ? 28.369 63.709 23.230 1.00 33.60 ? 2026 HOH A O 1 HETATM 6254 O O . HOH T 9 . ? -4.293 53.148 37.258 1.00 25.89 ? 2027 HOH A O 1 HETATM 6255 O O . HOH T 9 . ? 28.650 44.464 65.519 1.00 28.38 ? 2028 HOH A O 1 HETATM 6256 O O . HOH T 9 . ? 8.474 82.439 52.110 1.00 31.79 ? 2029 HOH A O 1 HETATM 6257 O O . HOH T 9 . ? 32.977 29.750 24.535 1.00 28.00 ? 2030 HOH A O 1 HETATM 6258 O O . HOH T 9 . ? 15.224 24.618 58.521 1.00 28.72 ? 2031 HOH A O 1 HETATM 6259 O O . HOH T 9 . ? 4.323 43.569 75.971 1.00 31.10 ? 2032 HOH A O 1 HETATM 6260 O O . HOH T 9 . ? 9.253 52.116 75.308 1.00 26.09 ? 2033 HOH A O 1 HETATM 6261 O O . HOH T 9 . ? 18.906 65.963 28.235 1.00 30.47 ? 2034 HOH A O 1 HETATM 6262 O O . HOH T 9 . ? 18.094 32.262 70.631 1.00 23.92 ? 2035 HOH A O 1 HETATM 6263 O O . HOH T 9 . ? 13.924 50.518 19.050 1.00 26.80 ? 2036 HOH A O 1 HETATM 6264 O O . HOH T 9 . ? 22.230 51.091 44.861 1.00 37.82 ? 2037 HOH A O 1 HETATM 6265 O O . HOH T 9 . ? 3.446 27.336 57.423 1.00 36.42 ? 2038 HOH A O 1 HETATM 6266 O O . HOH T 9 . ? 25.942 24.863 57.604 1.00 27.01 ? 2039 HOH A O 1 HETATM 6267 O O . HOH T 9 . ? 3.637 27.146 54.713 1.00 27.80 ? 2040 HOH A O 1 HETATM 6268 O O . HOH T 9 . ? 23.991 45.501 39.070 1.00 30.38 ? 2041 HOH A O 1 HETATM 6269 O O . HOH T 9 . ? -4.536 53.702 34.600 1.00 32.34 ? 2042 HOH A O 1 HETATM 6270 O O . HOH T 9 . ? 21.657 75.129 67.050 1.00 33.85 ? 2043 HOH A O 1 HETATM 6271 O O . HOH T 9 . ? 21.729 88.334 44.274 1.00 26.79 ? 2044 HOH A O 1 HETATM 6272 O O . HOH T 9 . ? -4.215 37.195 51.541 1.00 45.00 ? 2045 HOH A O 1 HETATM 6273 O O . HOH T 9 . ? 33.836 28.797 34.270 1.00 28.37 ? 2046 HOH A O 1 HETATM 6274 O O . HOH T 9 . ? -6.099 41.437 44.519 1.00 37.58 ? 2047 HOH A O 1 HETATM 6275 O O . HOH T 9 . ? 13.816 65.332 35.723 1.00 33.56 ? 2048 HOH A O 1 HETATM 6276 O O . HOH T 9 . ? 33.712 40.427 47.635 1.00 29.96 ? 2049 HOH A O 1 HETATM 6277 O O . HOH T 9 . ? 31.135 31.627 17.209 1.00 26.72 ? 2050 HOH A O 1 HETATM 6278 O O . HOH T 9 . ? 30.375 59.841 25.349 1.00 31.70 ? 2051 HOH A O 1 HETATM 6279 O O . HOH T 9 . ? 12.244 43.564 17.314 1.00 32.41 ? 2052 HOH A O 1 HETATM 6280 O O . HOH T 9 . ? 26.701 69.234 29.207 1.00 31.40 ? 2053 HOH A O 1 HETATM 6281 O O . HOH T 9 . ? -5.218 41.879 50.667 1.00 30.60 ? 2054 HOH A O 1 HETATM 6282 O O . HOH T 9 . ? 19.572 58.262 68.750 1.00 41.43 ? 2055 HOH A O 1 HETATM 6283 O O . HOH T 9 . ? -3.311 46.992 53.361 1.00 32.04 ? 2056 HOH A O 1 HETATM 6284 O O . HOH T 9 . ? -7.289 48.215 48.144 1.00 36.45 ? 2057 HOH A O 1 HETATM 6285 O O . HOH T 9 . ? 10.132 24.303 54.119 1.00 35.41 ? 2058 HOH A O 1 HETATM 6286 O O . HOH T 9 . ? -6.535 42.341 46.972 1.00 39.17 ? 2059 HOH A O 1 HETATM 6287 O O . HOH T 9 . ? -0.752 32.301 60.824 1.00 30.89 ? 2060 HOH A O 1 HETATM 6288 O O . HOH T 9 . ? 16.245 79.273 69.486 1.00 34.65 ? 2061 HOH A O 1 HETATM 6289 O O . HOH T 9 . ? -8.755 41.289 48.165 0.70 29.58 ? 2062 HOH A O 1 HETATM 6290 O O . HOH T 9 . ? 19.859 56.038 23.126 1.00 30.09 ? 2063 HOH A O 1 HETATM 6291 O O . HOH T 9 . ? 32.567 42.749 20.105 1.00 34.75 ? 2064 HOH A O 1 HETATM 6292 O O . HOH T 9 . ? 21.481 24.111 51.135 1.00 28.64 ? 2065 HOH A O 1 HETATM 6293 O O . HOH T 9 . ? 28.297 24.226 53.298 0.50 28.13 ? 2066 HOH A O 1 HETATM 6294 O O . HOH T 9 . ? 29.727 28.124 59.180 1.00 37.43 ? 2067 HOH A O 1 HETATM 6295 O O . HOH T 9 . ? 27.588 20.266 40.030 1.00 25.11 ? 2068 HOH A O 1 HETATM 6296 O O . HOH T 9 . ? 4.779 27.465 30.599 1.00 45.44 ? 2069 HOH A O 1 HETATM 6297 O O . HOH T 9 . ? 5.439 81.724 54.147 1.00 34.00 ? 2070 HOH A O 1 HETATM 6298 O O . HOH T 9 . ? 8.285 29.360 33.517 1.00 33.68 ? 2071 HOH A O 1 HETATM 6299 O O . HOH T 9 . ? -1.086 51.430 72.715 1.00 26.36 ? 2072 HOH A O 1 HETATM 6300 O O . HOH T 9 . ? 38.795 30.987 45.345 1.00 39.65 ? 2073 HOH A O 1 HETATM 6301 O O . HOH T 9 . ? 8.814 56.412 43.592 1.00 33.30 ? 2074 HOH A O 1 HETATM 6302 O O . HOH T 9 . ? 23.266 75.658 25.760 1.00 30.03 ? 2075 HOH A O 1 HETATM 6303 O O . HOH T 9 . ? 6.227 68.365 37.247 1.00 32.65 ? 2076 HOH A O 1 HETATM 6304 O O . HOH T 9 . ? 29.201 28.200 25.167 1.00 33.29 ? 2077 HOH A O 1 HETATM 6305 O O . HOH T 9 . ? 38.649 55.431 61.908 1.00 31.82 ? 2078 HOH A O 1 HETATM 6306 O O . HOH T 9 . ? 12.865 71.742 80.296 1.00 24.54 ? 2079 HOH A O 1 HETATM 6307 O O . HOH T 9 . ? 11.656 81.068 61.377 1.00 31.49 ? 2080 HOH A O 1 HETATM 6308 O O . HOH T 9 . ? 1.504 36.880 68.738 1.00 29.21 ? 2081 HOH A O 1 HETATM 6309 O O . HOH T 9 . ? 42.629 30.819 41.028 1.00 40.77 ? 2082 HOH A O 1 HETATM 6310 O O . HOH T 9 . ? 4.860 72.254 80.212 1.00 35.41 ? 2083 HOH A O 1 HETATM 6311 O O . HOH T 9 . ? 28.771 57.991 48.227 1.00 33.23 ? 2084 HOH A O 1 HETATM 6312 O O . HOH T 9 . ? 12.964 32.791 70.946 1.00 27.15 ? 2085 HOH A O 1 HETATM 6313 O O . HOH T 9 . ? 3.438 31.309 38.649 1.00 43.61 ? 2086 HOH A O 1 HETATM 6314 O O . HOH T 9 . ? 14.916 73.105 23.941 1.00 40.06 ? 2087 HOH A O 1 HETATM 6315 O O . HOH T 9 . ? 18.908 40.511 76.104 1.00 26.18 ? 2088 HOH A O 1 HETATM 6316 O O . HOH T 9 . ? 20.296 45.772 79.088 1.00 26.27 ? 2089 HOH A O 1 HETATM 6317 O O . HOH T 9 . ? 5.680 56.471 35.770 1.00 37.29 ? 2090 HOH A O 1 HETATM 6318 O O . HOH T 9 . ? 37.078 40.218 55.601 1.00 35.34 ? 2091 HOH A O 1 HETATM 6319 O O . HOH T 9 . ? 23.414 60.027 40.037 1.00 42.65 ? 2092 HOH A O 1 HETATM 6320 O O . HOH T 9 . ? 30.696 71.370 43.801 1.00 29.00 ? 2093 HOH A O 1 HETATM 6321 O O . HOH T 9 . ? 40.701 40.128 42.975 1.00 41.79 ? 2094 HOH A O 1 HETATM 6322 O O . HOH T 9 . ? 2.875 38.306 27.211 1.00 34.12 ? 2095 HOH A O 1 HETATM 6323 O O . HOH T 9 . ? 38.415 43.051 55.299 1.00 34.54 ? 2096 HOH A O 1 HETATM 6324 O O . HOH T 9 . ? -0.924 57.026 74.260 1.00 34.52 ? 2097 HOH A O 1 HETATM 6325 O O . HOH T 9 . ? 26.975 31.043 63.611 1.00 40.01 ? 2098 HOH A O 1 HETATM 6326 O O . HOH T 9 . ? 25.507 85.795 42.683 1.00 23.95 ? 2099 HOH A O 1 HETATM 6327 O O . HOH T 9 . ? 12.175 56.816 31.719 1.00 42.99 ? 2100 HOH A O 1 HETATM 6328 O O . HOH T 9 . ? -14.397 42.621 41.709 1.00 39.47 ? 2101 HOH A O 1 HETATM 6329 O O . HOH T 9 . ? 22.081 80.602 22.947 1.00 29.25 ? 2102 HOH A O 1 HETATM 6330 O O . HOH T 9 . ? 10.754 36.554 76.437 1.00 26.00 ? 2103 HOH A O 1 HETATM 6331 O O . HOH T 9 . ? 14.101 55.295 32.821 1.00 46.45 ? 2104 HOH A O 1 HETATM 6332 O O . HOH T 9 . ? 28.144 53.599 37.176 1.00 37.09 ? 2105 HOH A O 1 HETATM 6333 O O . HOH T 9 . ? 28.502 60.912 68.607 1.00 40.45 ? 2106 HOH A O 1 HETATM 6334 O O . HOH T 9 . ? 25.354 66.494 56.854 1.00 29.24 ? 2107 HOH A O 1 HETATM 6335 O O . HOH T 9 . ? 15.437 25.439 30.114 1.00 33.08 ? 2108 HOH A O 1 HETATM 6336 O O . HOH T 9 . ? 7.538 58.029 33.715 1.00 43.26 ? 2109 HOH A O 1 HETATM 6337 O O . HOH T 9 . ? 6.454 42.640 27.367 1.00 33.25 ? 2110 HOH A O 1 HETATM 6338 O O . HOH T 9 . ? 35.225 44.237 68.225 1.00 29.72 ? 2111 HOH A O 1 HETATM 6339 O O . HOH T 9 . ? 30.860 35.281 16.865 1.00 26.19 ? 2112 HOH A O 1 HETATM 6340 O O . HOH T 9 . ? 37.267 25.929 47.673 1.00 32.75 ? 2113 HOH A O 1 HETATM 6341 O O . HOH T 9 . ? 12.019 29.088 19.252 1.00 30.03 ? 2114 HOH A O 1 HETATM 6342 O O . HOH T 9 . ? 27.320 28.154 28.337 1.00 36.57 ? 2115 HOH A O 1 HETATM 6343 O O . HOH T 9 . ? 15.851 55.206 72.377 1.00 36.40 ? 2116 HOH A O 1 HETATM 6344 O O . HOH T 9 . ? 6.591 95.807 42.325 1.00 44.71 ? 2117 HOH A O 1 HETATM 6345 O O . HOH T 9 . ? 9.605 74.814 69.508 1.00 37.86 ? 2118 HOH A O 1 HETATM 6346 O O . HOH T 9 . ? 10.496 84.000 51.404 1.00 29.37 ? 2119 HOH A O 1 HETATM 6347 O O . HOH T 9 . ? 40.919 32.301 39.517 1.00 24.54 ? 2120 HOH A O 1 HETATM 6348 O O . HOH T 9 . ? 30.238 75.648 43.096 1.00 35.56 ? 2121 HOH A O 1 HETATM 6349 O O . HOH T 9 . ? 25.294 64.933 44.837 1.00 35.25 ? 2122 HOH A O 1 HETATM 6350 O O . HOH T 9 . ? 25.255 56.881 32.551 1.00 35.25 ? 2123 HOH A O 1 HETATM 6351 O O . HOH T 9 . ? 32.759 84.875 32.478 1.00 34.22 ? 2124 HOH A O 1 HETATM 6352 O O . HOH T 9 . ? 39.089 57.715 57.428 1.00 39.29 ? 2125 HOH A O 1 HETATM 6353 O O . HOH T 9 . ? 8.737 54.182 31.330 1.00 50.12 ? 2126 HOH A O 1 HETATM 6354 O O . HOH T 9 . ? 23.463 24.259 30.502 1.00 30.39 ? 2127 HOH A O 1 HETATM 6355 O O . HOH T 9 . ? 5.812 44.608 25.636 1.00 45.25 ? 2128 HOH A O 1 HETATM 6356 O O . HOH T 9 . ? 17.448 25.775 59.515 1.00 27.16 ? 2129 HOH A O 1 HETATM 6357 O O . HOH T 9 . ? -0.146 29.614 45.041 1.00 42.59 ? 2130 HOH A O 1 HETATM 6358 O O . HOH T 9 . ? 2.681 63.532 40.706 1.00 32.35 ? 2131 HOH A O 1 HETATM 6359 O O . HOH T 9 . ? 22.627 58.595 21.949 1.00 41.94 ? 2132 HOH A O 1 HETATM 6360 O O . HOH T 9 . ? 21.338 23.958 27.094 1.00 33.35 ? 2133 HOH A O 1 HETATM 6361 O O . HOH T 9 . ? 29.361 72.968 49.991 1.00 35.98 ? 2134 HOH A O 1 HETATM 6362 O O . HOH T 9 . ? 22.338 83.471 49.882 1.00 28.77 ? 2135 HOH A O 1 HETATM 6363 O O . HOH T 9 . ? 24.351 82.287 24.648 1.00 32.25 ? 2136 HOH A O 1 HETATM 6364 O O . HOH T 9 . ? 35.966 34.416 51.105 1.00 35.60 ? 2137 HOH A O 1 HETATM 6365 O O . HOH T 9 . ? 24.496 83.496 46.024 1.00 35.04 ? 2138 HOH A O 1 HETATM 6366 O O . HOH T 9 . ? 26.214 62.300 65.853 1.00 35.64 ? 2139 HOH A O 1 HETATM 6367 O O . HOH T 9 . ? 6.777 26.790 40.875 1.00 45.16 ? 2140 HOH A O 1 HETATM 6368 O O . HOH T 9 . ? 12.140 22.961 43.899 1.00 39.52 ? 2141 HOH A O 1 HETATM 6369 O O . HOH T 9 . ? 24.656 67.896 63.321 1.00 38.74 ? 2142 HOH A O 1 HETATM 6370 O O . HOH T 9 . ? 36.938 48.244 30.440 1.00 36.21 ? 2143 HOH A O 1 HETATM 6371 O O . HOH T 9 . ? 30.962 72.087 47.829 1.00 29.95 ? 2144 HOH A O 1 HETATM 6372 O O . HOH T 9 . ? -5.196 44.466 31.032 1.00 34.74 ? 2145 HOH A O 1 HETATM 6373 O O . HOH T 9 . ? 27.071 64.869 35.030 1.00 35.98 ? 2146 HOH A O 1 HETATM 6374 O O . HOH T 9 . ? 19.314 24.922 12.479 1.00 34.34 ? 2147 HOH A O 1 HETATM 6375 O O . HOH T 9 . ? 30.944 70.294 37.596 1.00 33.33 ? 2148 HOH A O 1 HETATM 6376 O O . HOH T 9 . ? 1.211 59.909 43.752 1.00 24.94 ? 2149 HOH A O 1 HETATM 6377 O O . HOH T 9 . ? 3.049 64.910 50.841 1.00 28.62 ? 2150 HOH A O 1 HETATM 6378 O O . HOH T 9 . ? -8.309 49.478 50.104 1.00 34.98 ? 2151 HOH A O 1 HETATM 6379 O O . HOH T 9 . ? 9.479 28.638 38.211 1.00 36.07 ? 2152 HOH A O 1 HETATM 6380 O O . HOH T 9 . ? 15.360 24.665 32.581 1.00 35.71 ? 2153 HOH A O 1 HETATM 6381 O O . HOH T 9 . ? -1.808 63.460 49.037 1.00 30.06 ? 2154 HOH A O 1 HETATM 6382 O O . HOH T 9 . ? 29.154 25.727 31.574 1.00 28.58 ? 2155 HOH A O 1 HETATM 6383 O O . HOH T 9 . ? 26.716 64.603 29.031 1.00 30.71 ? 2156 HOH A O 1 HETATM 6384 O O . HOH T 9 . ? 25.624 68.065 32.797 1.00 29.60 ? 2157 HOH A O 1 HETATM 6385 O O . HOH T 9 . ? 28.332 63.527 57.601 1.00 38.63 ? 2158 HOH A O 1 HETATM 6386 O O . HOH T 9 . ? 29.751 67.539 45.740 1.00 34.94 ? 2159 HOH A O 1 HETATM 6387 O O . HOH T 9 . ? 29.249 61.902 27.306 1.00 37.04 ? 2160 HOH A O 1 HETATM 6388 O O . HOH T 9 . ? 27.329 66.037 46.590 1.00 30.24 ? 2161 HOH A O 1 HETATM 6389 O O . HOH T 9 . ? 18.246 22.272 48.714 1.00 31.25 ? 2162 HOH A O 1 HETATM 6390 O O . HOH T 9 . ? 34.908 35.770 58.324 1.00 34.55 ? 2163 HOH A O 1 HETATM 6391 O O . HOH T 9 . ? 24.501 79.339 55.405 1.00 34.67 ? 2164 HOH A O 1 HETATM 6392 O O . HOH T 9 . ? 11.734 24.675 51.762 1.00 40.54 ? 2165 HOH A O 1 HETATM 6393 O O . HOH T 9 . ? 21.262 56.593 25.368 1.00 28.07 ? 2166 HOH A O 1 HETATM 6394 O O . HOH T 9 . ? 36.195 37.819 56.945 1.00 36.48 ? 2167 HOH A O 1 HETATM 6395 O O . HOH T 9 . ? 28.338 35.816 67.392 1.00 34.41 ? 2168 HOH A O 1 HETATM 6396 O O . HOH T 9 . ? 29.794 37.856 66.017 1.00 30.33 ? 2169 HOH A O 1 HETATM 6397 O O . HOH T 9 . ? 13.917 80.553 63.022 1.00 34.12 ? 2170 HOH A O 1 HETATM 6398 O O . HOH T 9 . ? 11.895 73.740 81.718 1.00 33.16 ? 2171 HOH A O 1 HETATM 6399 O O . HOH T 9 . ? 47.311 32.404 26.242 1.00 36.93 ? 2172 HOH A O 1 HETATM 6400 O O . HOH T 9 . ? 31.482 51.575 50.162 1.00 37.23 ? 2173 HOH A O 1 HETATM 6401 O O . HOH T 9 . ? 14.874 70.001 81.905 1.00 25.42 ? 2174 HOH A O 1 HETATM 6402 O O . HOH T 9 . ? 25.564 71.601 61.045 1.00 38.46 ? 2175 HOH A O 1 HETATM 6403 O O . HOH T 9 . ? 23.500 74.448 65.686 1.00 31.29 ? 2176 HOH A O 1 HETATM 6404 O O . HOH T 9 . ? 14.588 69.975 30.304 1.00 29.02 ? 2177 HOH A O 1 HETATM 6405 O O . HOH T 9 . ? 10.978 27.222 32.015 1.00 46.63 ? 2178 HOH A O 1 HETATM 6406 O O . HOH T 9 . ? -2.050 44.384 58.815 1.00 39.87 ? 2179 HOH A O 1 HETATM 6407 O O . HOH T 9 . ? 28.988 63.797 69.058 1.00 38.40 ? 2180 HOH A O 1 HETATM 6408 O O . HOH T 9 . ? 31.370 69.987 41.702 1.00 36.26 ? 2181 HOH A O 1 HETATM 6409 O O . HOH T 9 . ? 27.272 65.100 38.861 1.00 34.15 ? 2182 HOH A O 1 HETATM 6410 O O . HOH T 9 . ? -5.464 34.127 47.758 1.00 36.46 ? 2183 HOH A O 1 HETATM 6411 O O . HOH T 9 . ? 12.448 50.122 27.765 1.00 40.89 ? 2184 HOH A O 1 HETATM 6412 O O . HOH T 9 . ? 13.810 49.031 29.879 1.00 32.69 ? 2185 HOH A O 1 HETATM 6413 O O . HOH T 9 . ? 13.615 81.372 66.013 1.00 35.80 ? 2186 HOH A O 1 HETATM 6414 O O . HOH T 9 . ? 7.761 26.353 54.771 1.00 40.40 ? 2187 HOH A O 1 HETATM 6415 O O . HOH T 9 . ? 18.243 58.097 29.918 1.00 42.61 ? 2188 HOH A O 1 HETATM 6416 O O . HOH T 9 . ? 20.883 79.562 65.726 1.00 33.05 ? 2189 HOH A O 1 HETATM 6417 O O . HOH T 9 . ? 4.968 30.090 37.237 1.00 42.71 ? 2190 HOH A O 1 HETATM 6418 O O . HOH T 9 . ? 1.192 31.689 67.483 1.00 36.14 ? 2191 HOH A O 1 HETATM 6419 O O . HOH T 9 . ? 28.782 29.569 61.951 1.00 35.66 ? 2192 HOH A O 1 HETATM 6420 O O . HOH T 9 . ? 15.830 82.677 58.042 1.00 53.78 ? 2193 HOH A O 1 HETATM 6421 O O . HOH T 9 . ? 37.195 56.823 64.098 1.00 34.19 ? 2194 HOH A O 1 HETATM 6422 O O . HOH T 9 . ? 27.849 67.429 34.061 1.00 38.49 ? 2195 HOH A O 1 HETATM 6423 O O . HOH T 9 . ? 18.473 24.474 61.533 1.00 40.03 ? 2196 HOH A O 1 HETATM 6424 O O . HOH T 9 . ? 12.588 28.591 60.557 1.00 37.37 ? 2197 HOH A O 1 HETATM 6425 O O . HOH T 9 . ? 10.873 41.158 17.634 1.00 33.32 ? 2198 HOH A O 1 HETATM 6426 O O . HOH T 9 . ? 21.446 73.479 69.084 1.00 39.88 ? 2199 HOH A O 1 HETATM 6427 O O . HOH T 9 . ? 32.566 27.618 56.458 1.00 31.95 ? 2200 HOH A O 1 HETATM 6428 O O . HOH T 9 . ? 18.976 54.043 73.168 1.00 33.35 ? 2201 HOH A O 1 HETATM 6429 O O . HOH T 9 . ? 25.977 74.483 58.580 1.00 33.91 ? 2202 HOH A O 1 HETATM 6430 O O . HOH T 9 . ? -9.060 46.346 32.155 0.50 26.55 ? 2203 HOH A O 1 HETATM 6431 O O . HOH T 9 . ? 30.157 42.120 66.586 1.00 26.56 ? 2204 HOH A O 1 HETATM 6432 O O . HOH T 9 . ? 27.437 25.673 22.632 1.00 33.73 ? 2205 HOH A O 1 HETATM 6433 O O . HOH T 9 . ? 28.884 64.255 25.786 1.00 31.35 ? 2206 HOH A O 1 HETATM 6434 O O . HOH T 9 . ? 39.815 57.527 59.960 1.00 37.01 ? 2207 HOH A O 1 HETATM 6435 O O . HOH T 9 . ? 6.919 81.480 62.825 1.00 40.32 ? 2208 HOH A O 1 HETATM 6436 O O . HOH T 9 . ? 35.758 31.721 53.579 1.00 31.61 ? 2209 HOH A O 1 HETATM 6437 O O . HOH T 9 . ? 26.429 74.893 55.826 1.00 34.17 ? 2210 HOH A O 1 HETATM 6438 O O . HOH T 9 . ? -9.199 45.610 48.837 1.00 35.32 ? 2211 HOH A O 1 HETATM 6439 O O . HOH T 9 . ? 32.000 58.018 26.783 1.00 39.42 ? 2212 HOH A O 1 HETATM 6440 O O . HOH T 9 . ? -4.067 46.463 25.189 1.00 40.07 ? 2213 HOH A O 1 HETATM 6441 O O . HOH T 9 . ? 24.443 81.458 50.681 1.00 38.59 ? 2214 HOH A O 1 HETATM 6442 O O . HOH T 9 . ? 22.500 55.103 69.791 1.00 45.70 ? 2215 HOH A O 1 HETATM 6443 O O . HOH T 9 . ? -10.571 43.350 38.880 1.00 40.00 ? 2216 HOH A O 1 HETATM 6444 O O . HOH T 9 . ? -5.306 36.076 40.869 1.00 39.82 ? 2217 HOH A O 1 HETATM 6445 O O . HOH T 9 . ? 2.258 67.005 36.934 1.00 49.90 ? 2218 HOH A O 1 HETATM 6446 O O . HOH T 9 . ? -5.730 50.427 28.458 1.00 42.18 ? 2219 HOH A O 1 HETATM 6447 O O . HOH T 9 . ? 31.924 73.875 44.036 1.00 36.77 ? 2220 HOH A O 1 HETATM 6448 O O . HOH T 9 . ? 34.170 55.255 67.874 1.00 37.32 ? 2221 HOH A O 1 HETATM 6449 O O . HOH T 9 . ? 37.696 41.856 52.758 1.00 32.84 ? 2222 HOH A O 1 HETATM 6450 O O . HOH T 9 . ? -12.787 45.562 35.770 1.00 38.61 ? 2223 HOH A O 1 HETATM 6451 O O . HOH T 9 . ? 28.472 41.883 68.722 1.00 28.55 ? 2224 HOH A O 1 HETATM 6452 O O . HOH T 9 . ? 17.144 20.821 51.795 1.00 34.75 ? 2225 HOH A O 1 HETATM 6453 O O . HOH T 9 . ? 20.220 57.742 27.693 1.00 39.11 ? 2226 HOH A O 1 HETATM 6454 O O . HOH T 9 . ? 32.676 41.532 67.238 1.00 32.47 ? 2227 HOH A O 1 HETATM 6455 O O . HOH T 9 . ? 25.169 43.042 71.539 1.00 38.09 ? 2228 HOH A O 1 HETATM 6456 O O . HOH T 9 . ? 24.341 21.863 31.399 1.00 36.46 ? 2229 HOH A O 1 HETATM 6457 O O . HOH T 9 . ? -1.885 68.428 42.027 1.00 46.09 ? 2230 HOH A O 1 HETATM 6458 O O . HOH T 9 . ? 32.147 74.587 36.746 1.00 26.69 ? 2231 HOH A O 1 HETATM 6459 O O . HOH T 9 . ? 8.640 22.593 46.762 1.00 40.82 ? 2232 HOH A O 1 HETATM 6460 O O . HOH T 9 . ? 17.523 56.718 26.930 1.00 42.05 ? 2233 HOH A O 1 HETATM 6461 O O . HOH T 9 . ? 44.839 27.424 41.170 1.00 32.51 ? 2234 HOH A O 1 HETATM 6462 O O . HOH T 9 . ? 30.624 25.673 38.395 1.00 36.35 ? 2235 HOH A O 1 HETATM 6463 O O . HOH T 9 . ? 32.055 54.823 35.601 0.50 32.24 ? 2236 HOH A O 1 HETATM 6464 O O . HOH T 9 . ? 35.862 34.099 54.488 1.00 34.12 ? 2237 HOH A O 1 HETATM 6465 O O . HOH T 9 . ? 17.220 66.015 70.668 1.00 43.39 ? 2238 HOH A O 1 HETATM 6466 O O . HOH T 9 . ? 7.820 49.168 78.053 0.50 24.13 ? 2239 HOH A O 1 HETATM 6467 O O . HOH T 9 . ? 15.676 78.189 72.235 1.00 38.02 ? 2240 HOH A O 1 HETATM 6468 O O . HOH T 9 . ? 6.564 24.386 56.626 1.00 41.46 ? 2241 HOH A O 1 HETATM 6469 O O . HOH T 9 . ? -6.988 39.930 37.756 1.00 45.34 ? 2242 HOH A O 1 HETATM 6470 O O . HOH T 9 . ? 10.591 82.634 56.729 1.00 40.41 ? 2243 HOH A O 1 HETATM 6471 O O . HOH T 9 . ? 43.596 39.841 64.113 0.50 29.79 ? 2244 HOH A O 1 HETATM 6472 O O . HOH T 9 . ? 33.057 54.591 70.368 0.50 23.27 ? 2245 HOH A O 1 HETATM 6473 O O . HOH T 9 . ? 38.911 38.817 64.875 1.00 29.71 ? 2246 HOH A O 1 HETATM 6474 O O . HOH T 9 . ? 14.318 40.594 12.250 0.50 25.27 ? 2247 HOH A O 1 HETATM 6475 O O . HOH T 9 . ? -3.561 32.452 42.961 1.00 39.84 ? 2248 HOH A O 1 HETATM 6476 O O . HOH T 9 . ? 25.418 69.105 60.738 1.00 40.65 ? 2249 HOH A O 1 HETATM 6477 O O . HOH T 9 . ? 22.669 60.249 17.701 0.50 30.34 ? 2250 HOH A O 1 HETATM 6478 O O . HOH T 9 . ? 5.842 53.630 30.299 1.00 42.67 ? 2251 HOH A O 1 HETATM 6479 O O . HOH T 9 . ? -0.143 60.394 48.444 1.00 26.98 ? 2252 HOH A O 1 HETATM 6480 O O . HOH T 9 . ? 9.995 76.122 30.955 1.00 28.56 ? 2253 HOH A O 1 HETATM 6481 O O . HOH T 9 . ? 22.447 45.379 41.395 1.00 30.03 ? 2254 HOH A O 1 HETATM 6482 O O . HOH T 9 . ? 7.956 56.374 75.730 1.00 21.18 ? 2255 HOH A O 1 HETATM 6483 O O . HOH T 9 . ? 6.734 53.795 75.578 1.00 22.04 ? 2256 HOH A O 1 HETATM 6484 O O . HOH T 9 . ? 11.049 52.442 28.320 1.00 51.93 ? 2257 HOH A O 1 HETATM 6485 O O . HOH T 9 . ? 29.550 60.843 52.322 1.00 27.08 ? 2258 HOH A O 1 HETATM 6486 O O . HOH T 9 . ? 24.673 20.539 34.160 1.00 36.32 ? 2259 HOH A O 1 HETATM 6487 O O . HOH T 9 . ? -2.223 40.907 30.765 1.00 47.73 ? 2260 HOH A O 1 HETATM 6488 O O . HOH T 9 . ? 27.180 64.500 59.919 1.00 39.21 ? 2261 HOH A O 1 HETATM 6489 O O . HOH T 9 . ? 37.672 50.015 45.520 1.00 47.04 ? 2262 HOH A O 1 HETATM 6490 O O . HOH T 9 . ? 23.356 47.861 42.245 1.00 45.58 ? 2263 HOH A O 1 HETATM 6491 O O . HOH T 9 . ? 16.034 81.784 61.867 1.00 42.22 ? 2264 HOH A O 1 HETATM 6492 O O . HOH T 9 . ? 20.250 80.664 63.106 1.00 37.08 ? 2265 HOH A O 1 HETATM 6493 O O . HOH T 9 . ? 6.773 93.515 53.468 1.00 44.95 ? 2266 HOH A O 1 HETATM 6494 O O . HOH T 9 . ? 3.895 64.116 34.918 1.00 34.95 ? 2267 HOH A O 1 HETATM 6495 O O . HOH T 9 . ? 25.258 66.629 67.189 1.00 36.10 ? 2268 HOH A O 1 HETATM 6496 O O . HOH T 9 . ? 20.268 64.198 25.624 1.00 44.05 ? 2269 HOH A O 1 HETATM 6497 O O . HOH T 9 . ? 38.388 34.396 48.391 1.00 34.67 ? 2270 HOH A O 1 HETATM 6498 O O . HOH T 9 . ? 16.821 42.426 44.499 1.00 17.14 ? 2271 HOH A O 1 HETATM 6499 O O . HOH T 9 . ? 14.279 43.614 44.017 1.00 32.99 ? 2272 HOH A O 1 HETATM 6500 O O . HOH T 9 . ? 14.017 45.130 46.337 1.00 29.28 ? 2273 HOH A O 1 HETATM 6501 O O . HOH T 9 . ? 22.978 44.452 43.906 1.00 39.73 ? 2274 HOH A O 1 HETATM 6502 O O . HOH T 9 . ? -4.483 43.825 49.868 1.00 37.40 ? 2275 HOH A O 1 HETATM 6503 O O . HOH T 9 . ? 25.465 44.356 45.029 1.00 32.18 ? 2276 HOH A O 1 HETATM 6504 O O . HOH T 9 . ? 28.524 47.740 45.693 1.00 46.30 ? 2277 HOH A O 1 HETATM 6505 O O . HOH T 9 . ? 8.307 69.834 37.021 1.00 38.81 ? 2278 HOH A O 1 HETATM 6506 O O . HOH T 9 . ? -7.590 41.607 41.105 1.00 34.28 ? 2279 HOH A O 1 HETATM 6507 O O . HOH T 9 . ? 37.568 50.044 41.817 1.00 36.19 ? 2280 HOH A O 1 HETATM 6508 O O . HOH T 9 . ? 24.144 53.942 46.215 1.00 39.48 ? 2281 HOH A O 1 HETATM 6509 O O . HOH T 9 . ? 31.226 24.473 54.852 1.00 38.57 ? 2282 HOH A O 1 HETATM 6510 O O . HOH T 9 . ? 11.994 48.011 37.330 1.00 43.73 ? 2283 HOH A O 1 HETATM 6511 O O . HOH T 9 . ? 15.906 85.858 35.407 1.00 33.80 ? 2284 HOH A O 1 HETATM 6512 O O . HOH T 9 . ? 23.193 48.495 45.468 1.00 39.11 ? 2285 HOH A O 1 HETATM 6513 O O . HOH T 9 . ? 21.913 56.222 67.765 1.00 40.45 ? 2286 HOH A O 1 HETATM 6514 O O . HOH T 9 . ? 33.721 49.854 50.306 1.00 35.47 ? 2287 HOH A O 1 HETATM 6515 O O . HOH T 9 . ? -2.150 45.018 65.791 1.00 45.06 ? 2288 HOH A O 1 HETATM 6516 O O . HOH T 9 . ? -0.925 47.735 61.475 1.00 47.70 ? 2289 HOH A O 1 HETATM 6517 O O . HOH T 9 . ? 18.358 68.173 75.109 1.00 32.98 ? 2290 HOH A O 1 HETATM 6518 O O . HOH T 9 . ? 25.648 74.527 22.272 1.00 29.64 ? 2291 HOH A O 1 HETATM 6519 O O . HOH T 9 . ? 29.799 34.662 64.973 1.00 36.21 ? 2292 HOH A O 1 HETATM 6520 O O . HOH T 9 . ? -6.328 40.778 56.701 1.00 52.69 ? 2293 HOH A O 1 HETATM 6521 O O . HOH T 9 . ? -6.883 44.907 49.373 1.00 49.46 ? 2294 HOH A O 1 HETATM 6522 O O . HOH T 9 . ? 37.313 37.789 13.134 1.00 31.23 ? 2295 HOH A O 1 HETATM 6523 O O . HOH T 9 . ? 42.912 48.781 64.662 1.00 36.74 ? 2296 HOH A O 1 HETATM 6524 O O . HOH T 9 . ? 21.878 67.305 69.657 1.00 42.62 ? 2297 HOH A O 1 HETATM 6525 O O . HOH T 9 . ? 0.283 63.593 61.630 1.00 29.74 ? 2298 HOH A O 1 HETATM 6526 O O . HOH T 9 . ? 9.137 81.186 58.626 1.00 41.49 ? 2299 HOH A O 1 HETATM 6527 O O . HOH T 9 . ? 12.641 50.849 76.357 1.00 34.16 ? 2300 HOH A O 1 HETATM 6528 O O . HOH T 9 . ? 25.572 81.953 53.137 1.00 41.05 ? 2301 HOH A O 1 HETATM 6529 O O . HOH T 9 . ? 11.816 50.581 36.983 0.50 22.55 ? 2302 HOH A O 1 HETATM 6530 O O . HOH T 9 . ? 10.609 55.484 75.229 1.00 23.01 ? 2303 HOH A O 1 HETATM 6531 O O . HOH T 9 . ? 4.980 31.464 24.607 1.00 28.20 ? 2304 HOH A O 1 HETATM 6532 O O . HOH T 9 . ? 37.762 41.129 58.321 1.00 40.40 ? 2305 HOH A O 1 HETATM 6533 O O . HOH T 9 . ? 23.068 79.550 60.383 1.00 42.12 ? 2306 HOH A O 1 HETATM 6534 O O . HOH T 9 . ? 12.165 75.496 73.144 1.00 41.30 ? 2307 HOH A O 1 HETATM 6535 O O . HOH T 9 . ? 12.169 27.751 21.464 1.00 37.98 ? 2308 HOH A O 1 HETATM 6536 O O . HOH T 9 . ? 19.104 62.084 36.688 0.70 16.47 ? 2309 HOH A O 1 HETATM 6537 O O . HOH T 9 . ? 19.307 63.536 32.340 1.00 28.97 ? 2310 HOH A O 1 HETATM 6538 O O . HOH T 9 . ? 12.097 69.514 41.349 0.50 22.57 ? 2311 HOH A O 1 HETATM 6539 O O . HOH T 9 . ? 6.826 24.675 50.146 0.50 22.32 ? 2312 HOH A O 1 HETATM 6540 O O . HOH T 9 . ? -1.145 48.380 73.075 0.40 25.88 ? 2313 HOH A O 1 HETATM 6541 O O . HOH T 9 . ? -2.329 45.234 71.536 0.40 28.78 ? 2314 HOH A O 1 HETATM 6542 O O . HOH T 9 . ? -4.119 43.643 66.941 0.60 36.10 ? 2315 HOH A O 1 HETATM 6543 O O . HOH T 9 . ? 26.823 52.474 11.438 1.00 34.52 ? 2316 HOH A O 1 HETATM 6544 O O . HOH T 9 . ? 15.531 57.312 31.682 1.00 50.68 ? 2317 HOH A O 1 HETATM 6545 O O . HOH T 9 . ? 29.503 69.733 39.889 1.00 35.81 ? 2318 HOH A O 1 HETATM 6546 O O . HOH T 9 . ? 16.882 61.986 38.471 0.70 16.54 ? 2319 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . LYS A 14 ? 0.9855 0.7712 0.5361 0.2575 -0.0827 0.0180 55 LYS A N 2 C CA . LYS A 14 ? 0.9552 0.7541 0.5256 0.2469 -0.0805 0.0123 55 LYS A CA 3 C C . LYS A 14 ? 0.9091 0.7217 0.5104 0.2324 -0.0701 0.0156 55 LYS A C 4 O O . LYS A 14 ? 0.9007 0.7170 0.5167 0.2287 -0.0713 0.0175 55 LYS A O 5 C CB . LYS A 14 ? 0.9593 0.7647 0.5397 0.2468 -0.0987 -0.0006 55 LYS A CB 6 C CG . LYS A 14 ? 1.0051 0.8039 0.5652 0.2543 -0.1044 -0.0067 55 LYS A CG 7 C CD . LYS A 14 ? 1.0133 0.8260 0.5986 0.2443 -0.1106 -0.0162 55 LYS A CD 8 C CE . LYS A 14 ? 1.0192 0.8311 0.5960 0.2434 -0.1022 -0.0164 55 LYS A CE 9 N NZ . LYS A 14 ? 0.9989 0.8263 0.6060 0.2290 -0.0977 -0.0189 55 LYS A NZ 10 N N . HIS A 15 ? 0.8760 0.6953 0.4860 0.2247 -0.0601 0.0164 56 HIS A N 11 C CA . HIS A 15 ? 0.8219 0.6553 0.4620 0.2105 -0.0524 0.0174 56 HIS A CA 12 C C . HIS A 15 ? 0.7772 0.6226 0.4360 0.2035 -0.0616 0.0073 56 HIS A C 13 O O . HIS A 15 ? 0.7933 0.6416 0.4521 0.2008 -0.0579 0.0054 56 HIS A O 14 C CB . HIS A 15 ? 0.8257 0.6588 0.4643 0.2065 -0.0348 0.0255 56 HIS A CB 15 C CG . HIS A 15 ? 0.8658 0.6888 0.4920 0.2109 -0.0234 0.0365 56 HIS A CG 16 N ND1 . HIS A 15 ? 0.8997 0.7131 0.5060 0.2164 -0.0110 0.0440 56 HIS A ND1 17 C CD2 . HIS A 15 ? 0.8753 0.6958 0.5065 0.2105 -0.0222 0.0414 56 HIS A CD2 18 C CE1 . HIS A 15 ? 0.9315 0.7371 0.5318 0.2190 -0.0023 0.0535 56 HIS A CE1 19 N NE2 . HIS A 15 ? 0.9174 0.7268 0.5323 0.2155 -0.0092 0.0520 56 HIS A NE2 20 N N . ASN A 16 ? 0.7128 0.5651 0.3881 0.2008 -0.0735 0.0010 57 ASN A N 21 C CA . ASN A 16 ? 0.6608 0.5239 0.3546 0.1945 -0.0826 -0.0084 57 ASN A CA 22 C C . ASN A 16 ? 0.6039 0.4796 0.3269 0.1840 -0.0827 -0.0095 57 ASN A C 23 O O . ASN A 16 ? 0.5770 0.4524 0.3042 0.1819 -0.0751 -0.0030 57 ASN A O 24 C CB . ASN A 16 ? 0.6613 0.5195 0.3451 0.2032 -0.0996 -0.0169 57 ASN A CB 25 C CG . ASN A 16 ? 0.6876 0.5387 0.3626 0.2116 -0.1077 -0.0161 57 ASN A CG 26 O OD1 . ASN A 16 ? 0.6776 0.5304 0.3612 0.2088 -0.1027 -0.0108 57 ASN A OD1 27 N ND2 . ASN A 16 ? 0.6902 0.5321 0.3466 0.2227 -0.1209 -0.0214 57 ASN A ND2 28 N N . MET A 17 ? 0.5741 0.4604 0.3171 0.1776 -0.0907 -0.0174 58 MET A N 29 C CA . MET A 17 ? 0.5485 0.4467 0.3187 0.1677 -0.0894 -0.0180 58 MET A CA 30 C C . MET A 17 ? 0.5445 0.4404 0.3166 0.1720 -0.0950 -0.0173 58 MET A C 31 O O . MET A 17 ? 0.5388 0.4394 0.3242 0.1664 -0.0885 -0.0135 58 MET A O 32 C CB . MET A 17 ? 0.5232 0.4333 0.3159 0.1599 -0.0963 -0.0260 58 MET A CB 33 C CG . MET A 17 ? 0.5551 0.4771 0.3735 0.1487 -0.0895 -0.0243 58 MET A CG 34 S SD . MET A 17 ? 0.6245 0.5597 0.4695 0.1405 -0.0976 -0.0329 58 MET A SD 35 C CE . MET A 17 ? 0.6140 0.5484 0.4523 0.1385 -0.0953 -0.0345 58 MET A CE 36 N N . LYS A 18 ? 0.5654 0.4538 0.3243 0.1821 -0.1073 -0.0210 59 LYS A N 37 C CA . LYS A 18 ? 0.5715 0.4578 0.3328 0.1868 -0.1136 -0.0207 59 LYS A CA 38 C C . LYS A 18 ? 0.5728 0.4511 0.3225 0.1893 -0.1025 -0.0107 59 LYS A C 39 O O . LYS A 18 ? 0.5769 0.4583 0.3391 0.1871 -0.1017 -0.0089 59 LYS A O 40 C CB . LYS A 18 ? 0.6022 0.4802 0.3483 0.1986 -0.1295 -0.0264 59 LYS A CB 41 C CG . LYS A 18 ? 0.6496 0.5263 0.4006 0.2034 -0.1377 -0.0268 59 LYS A CG 42 C CD . LYS A 18 ? 0.7365 0.6070 0.4766 0.2142 -0.1556 -0.0343 59 LYS A CD 43 C CE . LYS A 18 ? 0.8197 0.6906 0.5686 0.2189 -0.1660 -0.0362 59 LYS A CE 44 N NZ . LYS A 18 ? 0.8541 0.7126 0.5826 0.2269 -0.1608 -0.0274 59 LYS A NZ 45 N N . ALA A 19 ? 0.5837 0.4521 0.3112 0.1935 -0.0932 -0.0043 60 ALA A N 46 C CA . ALA A 19 ? 0.6039 0.4644 0.3212 0.1953 -0.0811 0.0060 60 ALA A CA 47 C C . ALA A 19 ? 0.5654 0.4359 0.3060 0.1831 -0.0699 0.0093 60 ALA A C 48 O O . ALA A 19 ? 0.5696 0.4384 0.3151 0.1824 -0.0656 0.0141 60 ALA A O 49 C CB . ALA A 19 ? 0.6325 0.4815 0.3236 0.2015 -0.0725 0.0120 60 ALA A CB 50 N N . PHE A 20 ? 0.5359 0.4163 0.2899 0.1741 -0.0659 0.0064 61 PHE A N 51 C CA . PHE A 20 ? 0.5117 0.4021 0.2876 0.1626 -0.0567 0.0082 61 PHE A CA 52 C C . PHE A 20 ? 0.5016 0.4000 0.2982 0.1588 -0.0630 0.0043 61 PHE A C 53 O O . PHE A 20 ? 0.4963 0.3961 0.3026 0.1548 -0.0564 0.0083 61 PHE A O 54 C CB . PHE A 20 ? 0.4745 0.3741 0.2607 0.1544 -0.0536 0.0048 61 PHE A CB 55 C CG . PHE A 20 ? 0.4633 0.3748 0.2742 0.1428 -0.0483 0.0041 61 PHE A CG 56 C CD1 . PHE A 20 ? 0.4478 0.3589 0.2625 0.1380 -0.0361 0.0107 61 PHE A CD1 57 C CD2 . PHE A 20 ? 0.4400 0.3621 0.2698 0.1374 -0.0557 -0.0030 61 PHE A CD2 58 C CE1 . PHE A 20 ? 0.4329 0.3544 0.2696 0.1277 -0.0320 0.0095 61 PHE A CE1 59 C CE2 . PHE A 20 ? 0.4244 0.3567 0.2752 0.1274 -0.0507 -0.0036 61 PHE A CE2 60 C CZ . PHE A 20 ? 0.4387 0.3704 0.2919 0.1229 -0.0393 0.0024 61 PHE A CZ 61 N N . LEU A 21 ? 0.4892 0.3928 0.2933 0.1600 -0.0755 -0.0038 62 LEU A N 62 C CA . LEU A 21 ? 0.4879 0.4007 0.3142 0.1558 -0.0809 -0.0081 62 LEU A CA 63 C C . LEU A 21 ? 0.5059 0.4117 0.3275 0.1626 -0.0836 -0.0050 62 LEU A C 64 O O . LEU A 21 ? 0.5070 0.4182 0.3448 0.1583 -0.0813 -0.0046 62 LEU A O 65 C CB . LEU A 21 ? 0.4934 0.4130 0.3299 0.1560 -0.0938 -0.0172 62 LEU A CB 66 C CG . LEU A 21 ? 0.4566 0.3850 0.3037 0.1481 -0.0925 -0.0214 62 LEU A CG 67 C CD1 . LEU A 21 ? 0.5081 0.4397 0.3609 0.1507 -0.1064 -0.0299 62 LEU A CD1 68 C CD2 . LEU A 21 ? 0.4456 0.3857 0.3155 0.1365 -0.0843 -0.0210 62 LEU A CD2 69 N N . ASP A 22 ? 0.5312 0.4244 0.3295 0.1737 -0.0885 -0.0027 63 ASP A N 70 C CA . ASP A 22 ? 0.5594 0.4448 0.3515 0.1813 -0.0923 0.0003 63 ASP A CA 71 C C . ASP A 22 ? 0.5620 0.4425 0.3526 0.1790 -0.0793 0.0091 63 ASP A C 72 O O . ASP A 22 ? 0.5698 0.4473 0.3640 0.1819 -0.0807 0.0113 63 ASP A O 73 C CB . ASP A 22 ? 0.5978 0.4696 0.3624 0.1944 -0.1004 0.0010 63 ASP A CB 74 C CG . ASP A 22 ? 0.6330 0.5084 0.4014 0.1987 -0.1169 -0.0086 63 ASP A CG 75 O OD1 . ASP A 22 ? 0.6544 0.5426 0.4482 0.1921 -0.1222 -0.0151 63 ASP A OD1 76 O OD2 . ASP A 22 ? 0.6894 0.5543 0.4348 0.2090 -0.1245 -0.0096 63 ASP A OD2 77 N N . GLU A 23 ? 0.5528 0.4326 0.3394 0.1739 -0.0671 0.0141 64 GLU A N 78 C CA . GLU A 23 ? 0.5568 0.4315 0.3425 0.1716 -0.0546 0.0226 64 GLU A CA 79 C C . GLU A 23 ? 0.5260 0.4117 0.3381 0.1614 -0.0507 0.0207 64 GLU A C 80 O O . GLU A 23 ? 0.5315 0.4127 0.3461 0.1606 -0.0439 0.0262 64 GLU A O 81 C CB . GLU A 23 ? 0.5646 0.4348 0.3381 0.1700 -0.0430 0.0284 64 GLU A CB 82 C CG . GLU A 23 ? 0.5988 0.4641 0.3733 0.1667 -0.0291 0.0374 64 GLU A CG 83 C CD . GLU A 23 ? 0.6793 0.5306 0.4389 0.1754 -0.0276 0.0447 64 GLU A CD 84 O OE1 . GLU A 23 ? 0.7034 0.5442 0.4406 0.1862 -0.0330 0.0462 64 GLU A OE1 85 O OE2 . GLU A 23 ? 0.6450 0.4950 0.4147 0.1718 -0.0212 0.0490 64 GLU A OE2 86 N N . LEU A 24 ? 0.4974 0.3962 0.3278 0.1542 -0.0548 0.0132 65 LEU A N 87 C CA . LEU A 24 ? 0.4711 0.3808 0.3258 0.1450 -0.0517 0.0106 65 LEU A CA 88 C C . LEU A 24 ? 0.4794 0.3881 0.3416 0.1489 -0.0575 0.0094 65 LEU A C 89 O O . LEU A 24 ? 0.4960 0.4034 0.3547 0.1558 -0.0685 0.0057 65 LEU A O 90 C CB . LEU A 24 ? 0.4475 0.3704 0.3179 0.1384 -0.0563 0.0028 65 LEU A CB 91 C CG . LEU A 24 ? 0.4354 0.3610 0.3016 0.1339 -0.0521 0.0025 65 LEU A CG 92 C CD1 . LEU A 24 ? 0.4157 0.3528 0.2965 0.1292 -0.0591 -0.0055 65 LEU A CD1 93 C CD2 . LEU A 24 ? 0.3925 0.3197 0.2640 0.1262 -0.0393 0.0072 65 LEU A CD2 94 N N . LYS A 25 ? 0.4568 0.3664 0.3300 0.1446 -0.0506 0.0120 66 LYS A N 95 C CA . LYS A 25 ? 0.4736 0.3812 0.3536 0.1488 -0.0553 0.0115 66 LYS A CA 96 C C . LYS A 25 ? 0.4511 0.3695 0.3545 0.1405 -0.0521 0.0076 66 LYS A C 97 O O . LYS A 25 ? 0.4337 0.3541 0.3428 0.1332 -0.0424 0.0098 66 LYS A O 98 C CB . LYS A 25 ? 0.5010 0.3944 0.3669 0.1545 -0.0498 0.0200 66 LYS A CB 99 C CG . LYS A 25 ? 0.5532 0.4333 0.3922 0.1642 -0.0516 0.0254 66 LYS A CG 100 C CD . LYS A 25 ? 0.6641 0.5421 0.4961 0.1735 -0.0656 0.0209 66 LYS A CD 101 C CE . LYS A 25 ? 0.7102 0.5727 0.5134 0.1849 -0.0677 0.0267 66 LYS A CE 102 N NZ . LYS A 25 ? 0.6927 0.5541 0.4823 0.1844 -0.0645 0.0273 66 LYS A NZ 103 N N . ALA A 26 ? 0.4444 0.3689 0.3609 0.1423 -0.0601 0.0020 67 ALA A N 104 C CA . ALA A 26 ? 0.4296 0.3641 0.3680 0.1357 -0.0575 -0.0021 67 ALA A CA 105 C C . ALA A 26 ? 0.4270 0.3549 0.3660 0.1345 -0.0492 0.0029 67 ALA A C 106 O O . ALA A 26 ? 0.3954 0.3292 0.3468 0.1269 -0.0424 0.0015 67 ALA A O 107 C CB . ALA A 26 ? 0.4231 0.3638 0.3744 0.1397 -0.0677 -0.0082 67 ALA A CB 108 N N . GLU A 27 ? 0.4480 0.3633 0.3737 0.1423 -0.0501 0.0085 68 GLU A N 109 C CA . GLU A 27 ? 0.4609 0.3685 0.3876 0.1418 -0.0427 0.0137 68 GLU A CA 110 C C . GLU A 27 ? 0.4461 0.3517 0.3707 0.1346 -0.0313 0.0180 68 GLU A C 111 O O . GLU A 27 ? 0.4485 0.3537 0.3828 0.1301 -0.0250 0.0189 68 GLU A O 112 C CB . GLU A 27 ? 0.4940 0.3870 0.4053 0.1522 -0.0459 0.0197 68 GLU A CB 113 C CG A GLU A 27 ? 0.5077 0.3928 0.4231 0.1521 -0.0395 0.0243 68 GLU A CG 114 C CG B GLU A 27 ? 0.5398 0.4218 0.4274 0.1567 -0.0432 0.0268 68 GLU A CG 115 C CD A GLU A 27 ? 0.5400 0.4327 0.4759 0.1502 -0.0421 0.0183 68 GLU A CD 116 C CD B GLU A 27 ? 0.6361 0.5047 0.5050 0.1688 -0.0494 0.0314 68 GLU A CD 117 O OE1 A GLU A 27 ? 0.5371 0.4377 0.4815 0.1528 -0.0509 0.0121 68 GLU A OE1 118 O OE1 B GLU A 27 ? 0.6487 0.5158 0.5043 0.1746 -0.0568 0.0300 68 GLU A OE1 119 O OE2 A GLU A 27 ? 0.5866 0.4769 0.5306 0.1462 -0.0352 0.0198 68 GLU A OE2 120 O OE2 B GLU A 27 ? 0.6868 0.5456 0.5534 0.1726 -0.0469 0.0366 68 GLU A OE2 121 N N . ASN A 28 ? 0.4349 0.3393 0.3475 0.1337 -0.0290 0.0205 69 ASN A N 122 C CA . ASN A 28 ? 0.4318 0.3354 0.3435 0.1269 -0.0187 0.0243 69 ASN A CA 123 C C . ASN A 28 ? 0.4134 0.3297 0.3422 0.1173 -0.0163 0.0183 69 ASN A C 124 O O . ASN A 28 ? 0.4104 0.3269 0.3465 0.1111 -0.0087 0.0197 69 ASN A O 125 C CB . ASN A 28 ? 0.4505 0.3500 0.3452 0.1292 -0.0172 0.0280 69 ASN A CB 126 C CG . ASN A 28 ? 0.4930 0.3774 0.3679 0.1384 -0.0161 0.0359 69 ASN A CG 127 O OD1 . ASN A 28 ? 0.5461 0.4221 0.4207 0.1408 -0.0128 0.0406 69 ASN A OD1 128 N ND2 . ASN A 28 ? 0.4922 0.3728 0.3503 0.1439 -0.0191 0.0372 69 ASN A ND2 129 N N . ILE A 29 ? 0.3882 0.3147 0.3232 0.1161 -0.0228 0.0118 70 ILE A N 130 C CA . ILE A 29 ? 0.3707 0.3093 0.3212 0.1074 -0.0207 0.0062 70 ILE A CA 131 C C . ILE A 29 ? 0.3669 0.3073 0.3312 0.1049 -0.0182 0.0041 70 ILE A C 132 O O . ILE A 29 ? 0.3692 0.3134 0.3417 0.0979 -0.0121 0.0029 70 ILE A O 133 C CB . ILE A 29 ? 0.3604 0.3089 0.3165 0.1071 -0.0281 -0.0001 70 ILE A CB 134 C CG1 . ILE A 29 ? 0.3722 0.3184 0.3143 0.1095 -0.0305 0.0014 70 ILE A CG1 135 C CG2 . ILE A 29 ? 0.3561 0.3165 0.3274 0.0982 -0.0248 -0.0052 70 ILE A CG2 136 C CD1 . ILE A 29 ? 0.3967 0.3507 0.3435 0.1105 -0.0394 -0.0047 70 ILE A CD1 137 N N . LYS A 30 ? 0.3672 0.3043 0.3337 0.1111 -0.0232 0.0035 71 LYS A N 138 C CA . LYS A 30 ? 0.3684 0.3060 0.3474 0.1100 -0.0211 0.0014 71 LYS A CA 139 C C . LYS A 30 ? 0.3854 0.3147 0.3624 0.1072 -0.0128 0.0063 71 LYS A C 140 O O . LYS A 30 ? 0.3818 0.3146 0.3696 0.1014 -0.0084 0.0036 71 LYS A O 141 C CB . LYS A 30 ? 0.3813 0.3148 0.3606 0.1185 -0.0283 0.0011 71 LYS A CB 142 C CG . LYS A 30 ? 0.3830 0.3172 0.3758 0.1183 -0.0269 -0.0016 71 LYS A CG 143 C CD . LYS A 30 ? 0.4195 0.3496 0.4120 0.1277 -0.0350 -0.0017 71 LYS A CD 144 C CE . LYS A 30 ? 0.4715 0.4027 0.4780 0.1282 -0.0343 -0.0048 71 LYS A CE 145 N NZ . LYS A 30 ? 0.4779 0.4050 0.4849 0.1377 -0.0426 -0.0049 71 LYS A NZ 146 N N . LYS A 31 ? 0.4010 0.3187 0.3643 0.1115 -0.0110 0.0136 72 LYS A N 147 C CA . LYS A 31 ? 0.4165 0.3254 0.3782 0.1091 -0.0029 0.0192 72 LYS A CA 148 C C . LYS A 31 ? 0.3899 0.3043 0.3567 0.1001 0.0035 0.0181 72 LYS A C 149 O O . LYS A 31 ? 0.3839 0.2972 0.3594 0.0954 0.0085 0.0178 72 LYS A O 150 C CB . LYS A 31 ? 0.4422 0.3381 0.3870 0.1156 -0.0014 0.0278 72 LYS A CB 151 C CG . LYS A 31 ? 0.5372 0.4245 0.4773 0.1244 -0.0064 0.0300 72 LYS A CG 152 C CD . LYS A 31 ? 0.6218 0.4963 0.5420 0.1319 -0.0055 0.0384 72 LYS A CD 153 C CE . LYS A 31 ? 0.6936 0.5590 0.6087 0.1412 -0.0113 0.0406 72 LYS A CE 154 N NZ . LYS A 31 ? 0.7429 0.5943 0.6367 0.1492 -0.0101 0.0494 72 LYS A NZ 155 N N . PHE A 32 ? 0.3776 0.2980 0.3393 0.0981 0.0026 0.0172 73 PHE A N 156 C CA . PHE A 32 ? 0.3560 0.2820 0.3224 0.0901 0.0079 0.0161 73 PHE A CA 157 C C . PHE A 32 ? 0.3474 0.2831 0.3280 0.0842 0.0074 0.0089 73 PHE A C 158 O O . PHE A 32 ? 0.3519 0.2886 0.3393 0.0781 0.0123 0.0080 73 PHE A O 159 C CB . PHE A 32 ? 0.3563 0.2862 0.3136 0.0898 0.0067 0.0166 73 PHE A CB 160 C CG . PHE A 32 ? 0.3785 0.2986 0.3201 0.0956 0.0083 0.0238 73 PHE A CG 161 C CD1 . PHE A 32 ? 0.4160 0.3252 0.3535 0.0973 0.0144 0.0307 73 PHE A CD1 162 C CD2 . PHE A 32 ? 0.3725 0.2940 0.3032 0.0992 0.0041 0.0235 73 PHE A CD2 163 C CE1 . PHE A 32 ? 0.4566 0.3563 0.3783 0.1032 0.0168 0.0378 73 PHE A CE1 164 C CE2 . PHE A 32 ? 0.4343 0.3465 0.3484 0.1052 0.0057 0.0298 73 PHE A CE2 165 C CZ . PHE A 32 ? 0.4526 0.3539 0.3616 0.1073 0.0125 0.0372 73 PHE A CZ 166 N N . LEU A 33 ? 0.3349 0.2775 0.3203 0.0861 0.0016 0.0036 74 LEU A N 167 C CA . LEU A 33 ? 0.3293 0.2811 0.3275 0.0810 0.0021 -0.0030 74 LEU A CA 168 C C . LEU A 33 ? 0.3332 0.2800 0.3385 0.0802 0.0054 -0.0035 74 LEU A C 169 O O . LEU A 33 ? 0.3246 0.2746 0.3366 0.0745 0.0090 -0.0065 74 LEU A O 170 C CB . LEU A 33 ? 0.3262 0.2861 0.3304 0.0835 -0.0039 -0.0081 74 LEU A CB 171 C CG . LEU A 33 ? 0.3207 0.2899 0.3375 0.0785 -0.0022 -0.0145 74 LEU A CG 172 C CD1 . LEU A 33 ? 0.3114 0.2870 0.3277 0.0716 0.0008 -0.0159 74 LEU A CD1 173 C CD2 . LEU A 33 ? 0.3399 0.3160 0.3645 0.0819 -0.0075 -0.0188 74 LEU A CD2 174 N N . TYR A 34 ? 0.3376 0.2763 0.3416 0.0863 0.0038 -0.0008 75 TYR A N 175 C CA . TYR A 34 ? 0.3488 0.2814 0.3595 0.0857 0.0070 -0.0010 75 TYR A CA 176 C C . TYR A 34 ? 0.3568 0.2846 0.3670 0.0801 0.0134 0.0021 75 TYR A C 177 O O . TYR A 34 ? 0.3571 0.2859 0.3756 0.0756 0.0161 -0.0014 75 TYR A O 178 C CB . TYR A 34 ? 0.3571 0.2798 0.3644 0.0935 0.0045 0.0029 75 TYR A CB 179 C CG . TYR A 34 ? 0.3810 0.2968 0.3957 0.0933 0.0075 0.0027 75 TYR A CG 180 C CD1 . TYR A 34 ? 0.3847 0.3044 0.4100 0.0944 0.0054 -0.0034 75 TYR A CD1 181 C CD2 . TYR A 34 ? 0.4249 0.3304 0.4369 0.0917 0.0127 0.0084 75 TYR A CD2 182 C CE1 . TYR A 34 ? 0.4089 0.3215 0.4409 0.0946 0.0078 -0.0041 75 TYR A CE1 183 C CE2 . TYR A 34 ? 0.4642 0.3623 0.4843 0.0914 0.0151 0.0079 75 TYR A CE2 184 C CZ . TYR A 34 ? 0.4781 0.3798 0.5075 0.0929 0.0124 0.0014 75 TYR A CZ 185 O OH . TYR A 34 ? 0.5176 0.4120 0.5549 0.0929 0.0144 0.0002 75 TYR A OH 186 N N . ASN A 35 ? 0.3490 0.2718 0.3499 0.0807 0.0156 0.0085 76 ASN A N 187 C CA . ASN A 35 ? 0.3583 0.2764 0.3602 0.0759 0.0217 0.0121 76 ASN A CA 188 C C . ASN A 35 ? 0.3431 0.2699 0.3515 0.0681 0.0234 0.0072 76 ASN A C 189 O O . ASN A 35 ? 0.3504 0.2746 0.3654 0.0635 0.0271 0.0070 76 ASN A O 190 C CB . ASN A 35 ? 0.3679 0.2802 0.3578 0.0786 0.0240 0.0197 76 ASN A CB 191 C CG . ASN A 35 ? 0.3940 0.3017 0.3861 0.0741 0.0308 0.0242 76 ASN A CG 192 O OD1 . ASN A 35 ? 0.4059 0.3195 0.3993 0.0690 0.0328 0.0232 76 ASN A OD1 193 N ND2 . ASN A 35 ? 0.4355 0.3323 0.4293 0.0758 0.0345 0.0293 76 ASN A ND2 194 N N . PHE A 36 ? 0.3232 0.2601 0.3302 0.0669 0.0202 0.0030 77 PHE A N 195 C CA . PHE A 36 ? 0.3154 0.2601 0.3262 0.0602 0.0215 -0.0008 77 PHE A CA 196 C C . PHE A 36 ? 0.3018 0.2519 0.3216 0.0573 0.0206 -0.0082 77 PHE A C 197 O O . PHE A 36 ? 0.3085 0.2647 0.3308 0.0522 0.0214 -0.0118 77 PHE A O 198 C CB . PHE A 36 ? 0.3202 0.2728 0.3251 0.0600 0.0189 -0.0015 77 PHE A CB 199 C CG . PHE A 36 ? 0.3242 0.2727 0.3191 0.0623 0.0199 0.0047 77 PHE A CG 200 C CD1 . PHE A 36 ? 0.3351 0.2745 0.3272 0.0632 0.0245 0.0109 77 PHE A CD1 201 C CD2 . PHE A 36 ? 0.3206 0.2744 0.3091 0.0636 0.0167 0.0042 77 PHE A CD2 202 C CE1 . PHE A 36 ? 0.3377 0.2731 0.3193 0.0659 0.0264 0.0170 77 PHE A CE1 203 C CE2 . PHE A 36 ? 0.3299 0.2799 0.3077 0.0662 0.0177 0.0095 77 PHE A CE2 204 C CZ . PHE A 36 ? 0.3289 0.2698 0.3029 0.0675 0.0229 0.0159 77 PHE A CZ 205 N N . THR A 37 ? 0.3113 0.2592 0.3352 0.0611 0.0190 -0.0105 78 THR A N 206 C CA . THR A 37 ? 0.3094 0.2635 0.3406 0.0593 0.0184 -0.0176 78 THR A CA 207 C C . THR A 37 ? 0.3198 0.2677 0.3578 0.0600 0.0197 -0.0202 78 THR A C 208 O O . THR A 37 ? 0.3188 0.2707 0.3620 0.0605 0.0191 -0.0259 78 THR A O 209 C CB . THR A 37 ? 0.3143 0.2751 0.3464 0.0633 0.0146 -0.0203 78 THR A CB 210 O OG1 . THR A 37 ? 0.3156 0.2700 0.3464 0.0698 0.0122 -0.0170 78 THR A OG1 211 C CG2 . THR A 37 ? 0.2867 0.2549 0.3137 0.0619 0.0128 -0.0194 78 THR A CG2 212 N N . GLN A 38 ? 0.3273 0.2653 0.3655 0.0601 0.0218 -0.0159 79 GLN A N 213 C CA . GLN A 38 ? 0.3583 0.2890 0.4035 0.0609 0.0228 -0.0181 79 GLN A CA 214 C C . GLN A 38 ? 0.3544 0.2862 0.4051 0.0552 0.0244 -0.0236 79 GLN A C 215 O O . GLN A 38 ? 0.3715 0.2997 0.4282 0.0558 0.0244 -0.0281 79 GLN A O 216 C CB . GLN A 38 ? 0.3722 0.2909 0.4163 0.0634 0.0247 -0.0108 79 GLN A CB 217 C CG . GLN A 38 ? 0.4001 0.3163 0.4375 0.0703 0.0223 -0.0059 79 GLN A CG 218 C CD . GLN A 38 ? 0.4170 0.3375 0.4580 0.0746 0.0186 -0.0111 79 GLN A CD 219 O OE1 . GLN A 38 ? 0.4685 0.3844 0.5162 0.0764 0.0186 -0.0139 79 GLN A OE1 220 N NE2 . GLN A 38 ? 0.4100 0.3396 0.4480 0.0763 0.0153 -0.0128 79 GLN A NE2 221 N N . ILE A 39 ? 0.3451 0.2809 0.3937 0.0502 0.0254 -0.0232 80 ILE A N 222 C CA . ILE A 39 ? 0.3548 0.2920 0.4075 0.0449 0.0258 -0.0286 80 ILE A CA 223 C C . ILE A 39 ? 0.3315 0.2786 0.3795 0.0416 0.0251 -0.0309 80 ILE A C 224 O O . ILE A 39 ? 0.3319 0.2833 0.3745 0.0424 0.0248 -0.0269 80 ILE A O 225 C CB . ILE A 39 ? 0.3680 0.2974 0.4256 0.0414 0.0278 -0.0253 80 ILE A CB 226 C CG1 . ILE A 39 ? 0.3784 0.3095 0.4317 0.0397 0.0295 -0.0186 80 ILE A CG1 227 C CG2 . ILE A 39 ? 0.4004 0.3188 0.4637 0.0443 0.0289 -0.0232 80 ILE A CG2 228 C CD1 . ILE A 39 ? 0.4205 0.3455 0.4804 0.0358 0.0321 -0.0152 80 ILE A CD1 229 N N . PRO A 40 ? 0.3299 0.2801 0.3793 0.0381 0.0246 -0.0372 81 PRO A N 230 C CA . PRO A 40 ? 0.3136 0.2723 0.3579 0.0349 0.0241 -0.0386 81 PRO A CA 231 C C . PRO A 40 ? 0.3128 0.2716 0.3557 0.0316 0.0245 -0.0335 81 PRO A C 232 O O . PRO A 40 ? 0.3219 0.2741 0.3696 0.0301 0.0256 -0.0308 81 PRO A O 233 C CB . PRO A 40 ? 0.3328 0.2921 0.3782 0.0325 0.0234 -0.0461 81 PRO A CB 234 C CG . PRO A 40 ? 0.3585 0.3116 0.4088 0.0359 0.0236 -0.0498 81 PRO A CG 235 C CD . PRO A 40 ? 0.3266 0.2722 0.3811 0.0376 0.0243 -0.0434 81 PRO A CD 236 N N . HIS A 41 ? 0.2818 0.2478 0.3191 0.0307 0.0241 -0.0321 82 HIS A N 237 C CA . HIS A 41 ? 0.2809 0.2480 0.3167 0.0277 0.0245 -0.0280 82 HIS A CA 238 C C . HIS A 41 ? 0.2703 0.2444 0.3028 0.0242 0.0231 -0.0314 82 HIS A C 239 O O . HIS A 41 ? 0.2751 0.2542 0.3031 0.0237 0.0229 -0.0289 82 HIS A O 240 C CB . HIS A 41 ? 0.2934 0.2606 0.3246 0.0308 0.0253 -0.0215 82 HIS A CB 241 C CG . HIS A 41 ? 0.2965 0.2556 0.3293 0.0345 0.0268 -0.0171 82 HIS A CG 242 N ND1 . HIS A 41 ? 0.3241 0.2818 0.3549 0.0395 0.0257 -0.0167 82 HIS A ND1 243 C CD2 . HIS A 41 ? 0.3123 0.2636 0.3494 0.0339 0.0293 -0.0132 82 HIS A CD2 244 C CE1 . HIS A 41 ? 0.3259 0.2750 0.3580 0.0422 0.0273 -0.0122 82 HIS A CE1 245 N NE2 . HIS A 41 ? 0.3305 0.2755 0.3665 0.0388 0.0299 -0.0098 82 HIS A NE2 246 N N . LEU A 42 ? 0.2743 0.2482 0.3084 0.0221 0.0220 -0.0373 83 LEU A N 247 C CA . LEU A 42 ? 0.2690 0.2484 0.2988 0.0192 0.0205 -0.0406 83 LEU A CA 248 C C . LEU A 42 ? 0.2667 0.2470 0.2976 0.0159 0.0199 -0.0375 83 LEU A C 249 O O . LEU A 42 ? 0.2905 0.2660 0.3280 0.0145 0.0202 -0.0356 83 LEU A O 250 C CB . LEU A 42 ? 0.2637 0.2407 0.2942 0.0184 0.0192 -0.0477 83 LEU A CB 251 C CG . LEU A 42 ? 0.2641 0.2459 0.2879 0.0164 0.0176 -0.0515 83 LEU A CG 252 C CD1 . LEU A 42 ? 0.2727 0.2607 0.2901 0.0182 0.0193 -0.0518 83 LEU A CD1 253 C CD2 . LEU A 42 ? 0.2911 0.2681 0.3152 0.0165 0.0159 -0.0591 83 LEU A CD2 254 N N . ALA A 43 ? 0.2608 0.2470 0.2862 0.0147 0.0191 -0.0367 84 ALA A N 255 C CA . ALA A 43 ? 0.2604 0.2480 0.2870 0.0118 0.0183 -0.0341 84 ALA A CA 256 C C . ALA A 43 ? 0.2763 0.2609 0.3086 0.0088 0.0162 -0.0376 84 ALA A C 257 O O . ALA A 43 ? 0.2746 0.2584 0.3054 0.0084 0.0141 -0.0435 84 ALA A O 258 C CB . ALA A 43 ? 0.2573 0.2514 0.2769 0.0109 0.0172 -0.0341 84 ALA A CB 259 N N . GLY A 44 ? 0.2773 0.2602 0.3167 0.0070 0.0168 -0.0341 85 GLY A N 260 C CA . GLY A 44 ? 0.3016 0.2822 0.3493 0.0037 0.0143 -0.0369 85 GLY A CA 261 C C . GLY A 44 ? 0.3173 0.2910 0.3737 0.0037 0.0146 -0.0388 85 GLY A C 262 O O . GLY A 44 ? 0.3403 0.3115 0.4053 0.0009 0.0119 -0.0419 85 GLY A O 263 N N . THR A 45 ? 0.2964 0.2666 0.3512 0.0067 0.0172 -0.0375 86 THR A N 264 C CA . THR A 45 ? 0.3105 0.2731 0.3737 0.0070 0.0176 -0.0390 86 THR A CA 265 C C . THR A 45 ? 0.3195 0.2776 0.3902 0.0073 0.0219 -0.0316 86 THR A C 266 O O . THR A 45 ? 0.3233 0.2836 0.3899 0.0087 0.0249 -0.0254 86 THR A O 267 C CB . THR A 45 ? 0.3213 0.2817 0.3796 0.0106 0.0179 -0.0423 86 THR A CB 268 O OG1 . THR A 45 ? 0.3199 0.2815 0.3731 0.0141 0.0210 -0.0368 86 THR A OG1 269 C CG2 . THR A 45 ? 0.3364 0.3009 0.3866 0.0109 0.0150 -0.0491 86 THR A CG2 270 N N . GLU A 46 ? 0.3350 0.2860 0.4166 0.0061 0.0223 -0.0322 87 GLU A N 271 C CA . GLU A 46 ? 0.3528 0.2985 0.4421 0.0062 0.0271 -0.0247 87 GLU A CA 272 C C . GLU A 46 ? 0.3504 0.2938 0.4312 0.0112 0.0308 -0.0189 87 GLU A C 273 O O . GLU A 46 ? 0.3537 0.2958 0.4336 0.0124 0.0351 -0.0114 87 GLU A O 274 C CB . GLU A 46 ? 0.3919 0.3295 0.4949 0.0042 0.0267 -0.0269 87 GLU A CB 275 C CG . GLU A 46 ? 0.4362 0.3670 0.5478 0.0044 0.0327 -0.0184 87 GLU A CG 276 C CD . GLU A 46 ? 0.5501 0.4840 0.6689 0.0013 0.0359 -0.0131 87 GLU A CD 277 O OE1 . GLU A 46 ? 0.6007 0.5302 0.7229 0.0024 0.0422 -0.0048 87 GLU A OE1 278 O OE2 . GLU A 46 ? 0.5665 0.5071 0.6873 -0.0017 0.0324 -0.0168 87 GLU A OE2 279 N N . GLN A 47 ? 0.3480 0.2908 0.4225 0.0143 0.0291 -0.0226 88 GLN A N 280 C CA A GLN A 47 ? 0.3511 0.2919 0.4183 0.0194 0.0313 -0.0182 88 GLN A CA 281 C CA B GLN A 47 ? 0.3456 0.2867 0.4124 0.0195 0.0311 -0.0185 88 GLN A CA 282 C C . GLN A 47 ? 0.3289 0.2761 0.3863 0.0211 0.0322 -0.0140 88 GLN A C 283 O O . GLN A 47 ? 0.3297 0.2739 0.3823 0.0247 0.0349 -0.0076 88 GLN A O 284 C CB A GLN A 47 ? 0.3628 0.3033 0.4271 0.0222 0.0289 -0.0240 88 GLN A CB 285 C CB B GLN A 47 ? 0.3485 0.2906 0.4114 0.0221 0.0284 -0.0247 88 GLN A CB 286 C CG A GLN A 47 ? 0.4046 0.3372 0.4781 0.0216 0.0282 -0.0278 88 GLN A CG 287 C CG B GLN A 47 ? 0.3753 0.3096 0.4462 0.0224 0.0278 -0.0285 88 GLN A CG 288 C CD A GLN A 47 ? 0.4396 0.3734 0.5184 0.0173 0.0247 -0.0353 88 GLN A CD 289 C CD B GLN A 47 ? 0.3728 0.3095 0.4417 0.0226 0.0245 -0.0375 88 GLN A CD 290 O OE1 A GLN A 47 ? 0.3678 0.3087 0.4419 0.0152 0.0224 -0.0386 88 GLN A OE1 291 O OE1 B GLN A 47 ? 0.3387 0.2805 0.4003 0.0255 0.0239 -0.0396 88 GLN A OE1 292 N NE2 A GLN A 47 ? 0.4694 0.3955 0.5577 0.0162 0.0239 -0.0383 88 GLN A NE2 293 N NE2 B GLN A 47 ? 0.3983 0.3313 0.4741 0.0199 0.0223 -0.0431 88 GLN A NE2 294 N N . ASN A 48 ? 0.3131 0.2680 0.3669 0.0187 0.0298 -0.0174 89 ASN A N 295 C CA . ASN A 48 ? 0.3222 0.2826 0.3676 0.0201 0.0303 -0.0138 89 ASN A CA 296 C C . ASN A 48 ? 0.3323 0.2918 0.3800 0.0188 0.0336 -0.0075 89 ASN A C 297 O O . ASN A 48 ? 0.3463 0.3065 0.3867 0.0217 0.0354 -0.0026 89 ASN A O 298 C CB . ASN A 48 ? 0.3074 0.2759 0.3477 0.0184 0.0270 -0.0189 89 ASN A CB 299 C CG . ASN A 48 ? 0.3490 0.3224 0.3804 0.0208 0.0268 -0.0161 89 ASN A CG 300 O OD1 . ASN A 48 ? 0.3281 0.2993 0.3556 0.0249 0.0278 -0.0127 89 ASN A OD1 301 N ND2 . ASN A 48 ? 0.3267 0.3064 0.3550 0.0186 0.0252 -0.0178 89 ASN A ND2 302 N N . PHE A 49 ? 0.3250 0.2827 0.3831 0.0148 0.0344 -0.0079 90 PHE A N 303 C CA . PHE A 49 ? 0.3281 0.2845 0.3912 0.0136 0.0387 -0.0017 90 PHE A CA 304 C C . PHE A 49 ? 0.3257 0.2740 0.3881 0.0172 0.0437 0.0053 90 PHE A C 305 O O . PHE A 49 ? 0.3212 0.2686 0.3779 0.0198 0.0477 0.0117 90 PHE A O 306 C CB A PHE A 49 ? 0.3331 0.2892 0.4103 0.0083 0.0378 -0.0046 90 PHE A CB 307 C CB B PHE A 49 ? 0.3272 0.2835 0.4042 0.0084 0.0378 -0.0044 90 PHE A CB 308 C CG A PHE A 49 ? 0.3570 0.3126 0.4430 0.0064 0.0425 0.0013 90 PHE A CG 309 C CG B PHE A 49 ? 0.3347 0.2888 0.4209 0.0069 0.0432 0.0020 90 PHE A CG 310 C CD1 A PHE A 49 ? 0.3601 0.3185 0.4393 0.0084 0.0460 0.0069 90 PHE A CD1 311 C CD1 B PHE A 49 ? 0.3307 0.2894 0.4133 0.0073 0.0458 0.0063 90 PHE A CD1 312 C CD2 A PHE A 49 ? 0.3924 0.3448 0.4946 0.0025 0.0432 0.0006 90 PHE A CD2 313 C CD2 B PHE A 49 ? 0.3552 0.3027 0.4550 0.0049 0.0458 0.0036 90 PHE A CD2 314 C CE1 A PHE A 49 ? 0.3672 0.3255 0.4554 0.0068 0.0511 0.0122 90 PHE A CE1 315 C CE1 B PHE A 49 ? 0.3308 0.2876 0.4226 0.0061 0.0516 0.0122 90 PHE A CE1 316 C CE2 A PHE A 49 ? 0.4014 0.3539 0.5141 0.0004 0.0481 0.0060 90 PHE A CE2 317 C CE2 B PHE A 49 ? 0.3570 0.3027 0.4669 0.0033 0.0515 0.0098 90 PHE A CE2 318 C CZ A PHE A 49 ? 0.4037 0.3593 0.5093 0.0027 0.0525 0.0119 90 PHE A CZ 319 C CZ B PHE A 49 ? 0.3520 0.3026 0.4578 0.0040 0.0548 0.0142 90 PHE A CZ 320 N N . GLN A 50 ? 0.3307 0.2724 0.3972 0.0182 0.0436 0.0041 91 GLN A N 321 C CA A GLN A 50 ? 0.3501 0.2830 0.4149 0.0222 0.0483 0.0111 91 GLN A CA 322 C CA B GLN A 50 ? 0.3514 0.2843 0.4162 0.0222 0.0481 0.0109 91 GLN A CA 323 C C . GLN A 50 ? 0.3447 0.2782 0.3943 0.0280 0.0482 0.0144 91 GLN A C 324 O O . GLN A 50 ? 0.3600 0.2887 0.4042 0.0314 0.0526 0.0218 91 GLN A O 325 C CB A GLN A 50 ? 0.3628 0.2881 0.4352 0.0223 0.0478 0.0091 91 GLN A CB 326 C CB B GLN A 50 ? 0.3627 0.2886 0.4344 0.0224 0.0469 0.0080 91 GLN A CB 327 C CG A GLN A 50 ? 0.4051 0.3273 0.4939 0.0169 0.0486 0.0074 91 GLN A CG 328 C CG B GLN A 50 ? 0.4128 0.3361 0.5007 0.0168 0.0473 0.0057 91 GLN A CG 329 C CD A GLN A 50 ? 0.4372 0.3566 0.5336 0.0151 0.0551 0.0152 91 GLN A CD 330 C CD B GLN A 50 ? 0.4521 0.3690 0.5477 0.0165 0.0451 0.0011 91 GLN A CD 331 O OE1 A GLN A 50 ? 0.4748 0.3964 0.5841 0.0101 0.0551 0.0135 91 GLN A OE1 332 O OE1 B GLN A 50 ? 0.4972 0.4142 0.5864 0.0194 0.0417 -0.0035 91 GLN A OE1 333 N NE2 A GLN A 50 ? 0.4444 0.3588 0.5329 0.0196 0.0606 0.0237 91 GLN A NE2 334 N NE2 B GLN A 50 ? 0.4986 0.4097 0.6089 0.0129 0.0470 0.0019 91 GLN A NE2 335 N N . LEU A 51 ? 0.3218 0.2612 0.3645 0.0294 0.0431 0.0090 92 LEU A N 336 C CA . LEU A 51 ? 0.3262 0.2668 0.3562 0.0347 0.0421 0.0114 92 LEU A CA 337 C C . LEU A 51 ? 0.3081 0.2522 0.3317 0.0349 0.0439 0.0153 92 LEU A C 338 O O . LEU A 51 ? 0.3338 0.2745 0.3477 0.0399 0.0455 0.0205 92 LEU A O 339 C CB . LEU A 51 ? 0.3013 0.2480 0.3278 0.0357 0.0366 0.0048 92 LEU A CB 340 C CG . LEU A 51 ? 0.3125 0.2607 0.3284 0.0411 0.0343 0.0061 92 LEU A CG 341 C CD1 . LEU A 51 ? 0.3487 0.2877 0.3602 0.0472 0.0356 0.0114 92 LEU A CD1 342 C CD2 . LEU A 51 ? 0.2973 0.2526 0.3135 0.0409 0.0297 -0.0007 92 LEU A CD2 343 N N . ALA A 52 ? 0.2993 0.2499 0.3275 0.0301 0.0433 0.0125 93 ALA A N 344 C CA . ALA A 52 ? 0.3001 0.2539 0.3236 0.0303 0.0454 0.0161 93 ALA A CA 345 C C . ALA A 52 ? 0.3107 0.2574 0.3341 0.0325 0.0521 0.0242 93 ALA A C 346 O O . ALA A 52 ? 0.3288 0.2742 0.3417 0.0366 0.0543 0.0288 93 ALA A O 347 C CB . ALA A 52 ? 0.2994 0.2602 0.3302 0.0246 0.0439 0.0122 93 ALA A CB 348 N N . LYS A 53 ? 0.3160 0.2577 0.3507 0.0298 0.0557 0.0260 94 LYS A N 349 C CA . LYS A 53 ? 0.3349 0.2692 0.3710 0.0316 0.0633 0.0344 94 LYS A CA 350 C C . LYS A 53 ? 0.3467 0.2729 0.3701 0.0387 0.0650 0.0397 94 LYS A C 351 O O . LYS A 53 ? 0.3639 0.2857 0.3792 0.0426 0.0703 0.0467 94 LYS A O 352 C CB . LYS A 53 ? 0.3557 0.2864 0.4093 0.0268 0.0662 0.0347 94 LYS A CB 353 C CG . LYS A 53 ? 0.3756 0.3141 0.4414 0.0205 0.0649 0.0307 94 LYS A CG 354 C CD . LYS A 53 ? 0.5019 0.4367 0.5864 0.0158 0.0683 0.0318 94 LYS A CD 355 C CE . LYS A 53 ? 0.5308 0.4625 0.6217 0.0140 0.0634 0.0258 94 LYS A CE 356 N NZ . LYS A 53 ? 0.6050 0.5325 0.7151 0.0093 0.0654 0.0258 94 LYS A NZ 357 N N . GLN A 54 ? 0.3484 0.2726 0.3691 0.0408 0.0603 0.0362 95 GLN A N 358 C CA . GLN A 54 ? 0.3630 0.2797 0.3714 0.0480 0.0605 0.0406 95 GLN A CA 359 C C . GLN A 54 ? 0.3643 0.2839 0.3571 0.0529 0.0584 0.0416 95 GLN A C 360 O O . GLN A 54 ? 0.3843 0.2972 0.3657 0.0585 0.0619 0.0482 95 GLN A O 361 C CB . GLN A 54 ? 0.3560 0.2719 0.3664 0.0491 0.0550 0.0354 95 GLN A CB 362 C CG . GLN A 54 ? 0.3784 0.2866 0.3766 0.0570 0.0540 0.0395 95 GLN A CG 363 C CD . GLN A 54 ? 0.3778 0.2881 0.3771 0.0587 0.0475 0.0333 95 GLN A CD 364 O OE1 . GLN A 54 ? 0.3865 0.2973 0.3969 0.0551 0.0465 0.0288 95 GLN A OE1 365 N NE2 . GLN A 54 ? 0.3825 0.2941 0.3707 0.0643 0.0430 0.0327 95 GLN A NE2 366 N N . ILE A 55 ? 0.3487 0.2779 0.3407 0.0508 0.0527 0.0350 96 ILE A N 367 C CA . ILE A 55 ? 0.3499 0.2825 0.3290 0.0547 0.0497 0.0348 96 ILE A CA 368 C C . ILE A 55 ? 0.3520 0.2834 0.3261 0.0555 0.0554 0.0403 96 ILE A C 369 O O . ILE A 55 ? 0.3598 0.2869 0.3198 0.0617 0.0562 0.0442 96 ILE A O 370 C CB . ILE A 55 ? 0.3379 0.2811 0.3199 0.0512 0.0434 0.0269 96 ILE A CB 371 C CG1 A ILE A 55 ? 0.3772 0.3223 0.3643 0.0505 0.0386 0.0213 96 ILE A CG1 372 C CG1 B ILE A 55 ? 0.3362 0.2798 0.3201 0.0525 0.0383 0.0223 96 ILE A CG1 373 C CG2 . ILE A 55 ? 0.3356 0.2824 0.3060 0.0545 0.0403 0.0265 96 ILE A CG2 374 C CD1 A ILE A 55 ? 0.3834 0.3245 0.3626 0.0569 0.0354 0.0221 96 ILE A CD1 375 C CD1 B ILE A 55 ? 0.2651 0.2181 0.2545 0.0485 0.0334 0.0147 96 ILE A CD1 376 N N . GLN A 56 ? 0.3429 0.2776 0.3284 0.0498 0.0593 0.0404 97 GLN A N 377 C CA . GLN A 56 ? 0.3570 0.2905 0.3399 0.0505 0.0659 0.0460 97 GLN A CA 378 C C . GLN A 56 ? 0.3782 0.3008 0.3530 0.0562 0.0726 0.0546 97 GLN A C 379 O O . GLN A 56 ? 0.3922 0.3118 0.3536 0.0615 0.0753 0.0587 97 GLN A O 380 C CB . GLN A 56 ? 0.3577 0.2959 0.3572 0.0433 0.0691 0.0450 97 GLN A CB 381 C CG . GLN A 56 ? 0.3834 0.3208 0.3838 0.0437 0.0770 0.0511 97 GLN A CG 382 C CD . GLN A 56 ? 0.4054 0.3472 0.4249 0.0367 0.0798 0.0502 97 GLN A CD 383 O OE1 . GLN A 56 ? 0.3887 0.3302 0.4214 0.0322 0.0783 0.0474 97 GLN A OE1 384 N NE2 . GLN A 56 ? 0.3797 0.3257 0.4013 0.0360 0.0836 0.0521 97 GLN A NE2 385 N N . SER A 57 ? 0.3939 0.3098 0.3759 0.0555 0.0753 0.0572 98 SER A N 386 C CA . SER A 57 ? 0.4092 0.3136 0.3835 0.0609 0.0824 0.0662 98 SER A CA 387 C C . SER A 57 ? 0.4112 0.3101 0.3649 0.0698 0.0788 0.0679 98 SER A C 388 O O . SER A 57 ? 0.4323 0.3239 0.3721 0.0760 0.0839 0.0748 98 SER A O 389 C CB . SER A 57 ? 0.4158 0.3139 0.4025 0.0584 0.0846 0.0678 98 SER A CB 390 O OG A SER A 57 ? 0.4200 0.3064 0.3994 0.0637 0.0918 0.0771 98 SER A OG 391 O OG B SER A 57 ? 0.4572 0.3573 0.4615 0.0518 0.0903 0.0691 98 SER A OG 392 N N . GLN A 58 ? 0.3958 0.2979 0.3477 0.0706 0.0699 0.0615 99 GLN A N 393 C CA . GLN A 58 ? 0.4064 0.3040 0.3412 0.0788 0.0648 0.0620 99 GLN A CA 394 C C . GLN A 58 ? 0.4010 0.3018 0.3219 0.0825 0.0627 0.0611 99 GLN A C 395 O O . GLN A 58 ? 0.4243 0.3175 0.3282 0.0903 0.0631 0.0655 99 GLN A O 396 C CB . GLN A 58 ? 0.4020 0.3028 0.3407 0.0786 0.0561 0.0552 99 GLN A CB 397 C CG . GLN A 58 ? 0.4275 0.3213 0.3744 0.0782 0.0580 0.0572 99 GLN A CG 398 C CD . GLN A 58 ? 0.4450 0.3424 0.3960 0.0786 0.0497 0.0502 99 GLN A CD 399 O OE1 . GLN A 58 ? 0.4505 0.3578 0.4102 0.0736 0.0456 0.0429 99 GLN A OE1 400 N NE2 . GLN A 58 ? 0.5557 0.4450 0.5000 0.0850 0.0476 0.0528 99 GLN A NE2 401 N N . TRP A 59 ? 0.3892 0.3005 0.3167 0.0772 0.0603 0.0556 100 TRP A N 402 C CA . TRP A 59 ? 0.3866 0.3006 0.3019 0.0806 0.0584 0.0547 100 TRP A CA 403 C C . TRP A 59 ? 0.4093 0.3167 0.3153 0.0843 0.0673 0.0625 100 TRP A C 404 O O . TRP A 59 ? 0.4358 0.3397 0.3252 0.0910 0.0664 0.0639 100 TRP A O 405 C CB . TRP A 59 ? 0.3563 0.2821 0.2815 0.0739 0.0549 0.0480 100 TRP A CB 406 C CG . TRP A 59 ? 0.3609 0.2931 0.2901 0.0722 0.0459 0.0406 100 TRP A CG 407 C CD1 . TRP A 59 ? 0.3733 0.3027 0.3007 0.0754 0.0408 0.0388 100 TRP A CD1 408 C CD2 . TRP A 59 ? 0.3419 0.2844 0.2789 0.0667 0.0414 0.0339 100 TRP A CD2 409 N NE1 . TRP A 59 ? 0.3522 0.2903 0.2861 0.0722 0.0338 0.0314 100 TRP A NE1 410 C CE2 . TRP A 59 ? 0.3244 0.2701 0.2636 0.0669 0.0343 0.0286 100 TRP A CE2 411 C CE3 . TRP A 59 ? 0.3196 0.2688 0.2617 0.0620 0.0429 0.0323 100 TRP A CE3 412 C CZ2 . TRP A 59 ? 0.3177 0.2730 0.2641 0.0622 0.0292 0.0219 100 TRP A CZ2 413 C CZ3 . TRP A 59 ? 0.3272 0.2852 0.2754 0.0575 0.0373 0.0257 100 TRP A CZ3 414 C CH2 . TRP A 59 ? 0.3164 0.2773 0.2664 0.0576 0.0309 0.0208 100 TRP A CH2 415 N N . LYS A 60 ? 0.4147 0.3201 0.3318 0.0803 0.0760 0.0673 101 LYS A N 416 C CA . LYS A 60 ? 0.4493 0.3474 0.3589 0.0842 0.0865 0.0760 101 LYS A CA 417 C C . LYS A 60 ? 0.4743 0.3596 0.3656 0.0934 0.0884 0.0825 101 LYS A C 418 O O . LYS A 60 ? 0.5024 0.3820 0.3757 0.1005 0.0916 0.0867 101 LYS A O 419 C CB . LYS A 60 ? 0.4497 0.3483 0.3779 0.0776 0.0955 0.0800 101 LYS A CB 420 C CG . LYS A 60 ? 0.4968 0.4071 0.4413 0.0696 0.0942 0.0745 101 LYS A CG 421 C CD . LYS A 60 ? 0.5975 0.5081 0.5609 0.0638 0.1028 0.0785 101 LYS A CD 422 C CE . LYS A 60 ? 0.6055 0.5273 0.5819 0.0575 0.1019 0.0738 101 LYS A CE 423 N NZ . LYS A 60 ? 0.6834 0.6052 0.6733 0.0545 0.1121 0.0794 101 LYS A NZ 424 N N . GLU A 61 ? 0.4770 0.3570 0.3719 0.0937 0.0864 0.0834 102 GLU A N 425 C CA . GLU A 61 ? 0.5099 0.3770 0.3882 0.1025 0.0873 0.0896 102 GLU A CA 426 C C . GLU A 61 ? 0.5038 0.3703 0.3623 0.1102 0.0783 0.0858 102 GLU A C 427 O O . GLU A 61 ? 0.5213 0.3776 0.3595 0.1192 0.0801 0.0913 102 GLU A O 428 C CB . GLU A 61 ? 0.5264 0.3896 0.4141 0.1010 0.0845 0.0892 102 GLU A CB 429 C CG A GLU A 61 ? 0.5475 0.4125 0.4584 0.0923 0.0897 0.0898 102 GLU A CG 430 C CG B GLU A 61 ? 0.5682 0.4176 0.4393 0.1102 0.0850 0.0958 102 GLU A CG 431 C CD A GLU A 61 ? 0.5824 0.4473 0.5039 0.0900 0.0830 0.0850 102 GLU A CD 432 C CD B GLU A 61 ? 0.6383 0.4823 0.5214 0.1080 0.0858 0.0976 102 GLU A CD 433 O OE1 A GLU A 61 ? 0.5729 0.4342 0.4842 0.0959 0.0760 0.0834 102 GLU A OE1 434 O OE1 B GLU A 61 ? 0.6625 0.5127 0.5666 0.0992 0.0874 0.0944 102 GLU A OE1 435 O OE2 A GLU A 61 ? 0.5751 0.4439 0.5161 0.0823 0.0845 0.0825 102 GLU A OE2 436 O OE2 B GLU A 61 ? 0.6908 0.5240 0.5620 0.1153 0.0846 0.1020 102 GLU A OE2 437 N N . PHE A 62 ? 0.4666 0.3436 0.3308 0.1070 0.0684 0.0765 103 PHE A N 438 C CA . PHE A 62 ? 0.4751 0.3524 0.3239 0.1135 0.0586 0.0719 103 PHE A CA 439 C C . PHE A 62 ? 0.4922 0.3677 0.3250 0.1184 0.0610 0.0736 103 PHE A C 440 O O . PHE A 62 ? 0.5201 0.3919 0.3357 0.1260 0.0545 0.0718 103 PHE A O 441 C CB . PHE A 62 ? 0.4498 0.3394 0.3109 0.1080 0.0486 0.0617 103 PHE A CB 442 C CG . PHE A 62 ? 0.4389 0.3300 0.3119 0.1055 0.0438 0.0585 103 PHE A CG 443 C CD1 . PHE A 62 ? 0.5046 0.3856 0.3743 0.1098 0.0457 0.0637 103 PHE A CD1 444 C CD2 . PHE A 62 ? 0.4288 0.3314 0.3163 0.0990 0.0377 0.0503 103 PHE A CD2 445 C CE1 . PHE A 62 ? 0.5136 0.3964 0.3952 0.1075 0.0412 0.0601 103 PHE A CE1 446 C CE2 . PHE A 62 ? 0.4286 0.3328 0.3271 0.0969 0.0337 0.0469 103 PHE A CE2 447 C CZ . PHE A 62 ? 0.4639 0.3587 0.3601 0.1010 0.0353 0.0514 103 PHE A CZ 448 N N . GLY A 63 ? 0.4787 0.3575 0.3180 0.1140 0.0697 0.0762 104 GLY A N 449 C CA . GLY A 63 ? 0.4894 0.3653 0.3135 0.1191 0.0741 0.0789 104 GLY A CA 450 C C . GLY A 63 ? 0.4764 0.3630 0.3088 0.1137 0.0740 0.0740 104 GLY A C 451 O O . GLY A 63 ? 0.4886 0.3732 0.3088 0.1181 0.0774 0.0756 104 GLY A O 452 N N . LEU A 64 ? 0.4409 0.3385 0.2931 0.1046 0.0702 0.0680 105 LEU A N 453 C CA . LEU A 64 ? 0.4325 0.3398 0.2922 0.0997 0.0698 0.0637 105 LEU A CA 454 C C . LEU A 64 ? 0.4423 0.3490 0.3056 0.0984 0.0814 0.0695 105 LEU A C 455 O O . LEU A 64 ? 0.4683 0.3703 0.3379 0.0972 0.0904 0.0762 105 LEU A O 456 C CB . LEU A 64 ? 0.3997 0.3180 0.2794 0.0904 0.0640 0.0568 105 LEU A CB 457 C CG . LEU A 64 ? 0.4065 0.3271 0.2848 0.0912 0.0529 0.0504 105 LEU A CG 458 C CD1 . LEU A 64 ? 0.3886 0.3206 0.2851 0.0821 0.0488 0.0438 105 LEU A CD1 459 C CD2 . LEU A 64 ? 0.4092 0.3286 0.2715 0.0977 0.0458 0.0470 105 LEU A CD2 460 N N . ASP A 65 ? 0.4418 0.3533 0.3025 0.0986 0.0815 0.0670 106 ASP A N 461 C CA . ASP A 65 ? 0.4679 0.3792 0.3311 0.0984 0.0926 0.0723 106 ASP A CA 462 C C . ASP A 65 ? 0.4659 0.3845 0.3539 0.0889 0.0975 0.0729 106 ASP A C 463 O O . ASP A 65 ? 0.4807 0.3966 0.3751 0.0882 0.1083 0.0795 106 ASP A O 464 C CB . ASP A 65 ? 0.4493 0.3644 0.3045 0.1009 0.0902 0.0684 106 ASP A CB 465 C CG . ASP A 65 ? 0.4903 0.3966 0.3198 0.1114 0.0870 0.0686 106 ASP A CG 466 O OD1 . ASP A 65 ? 0.5265 0.4226 0.3424 0.1182 0.0948 0.0759 106 ASP A OD1 467 O OD2 . ASP A 65 ? 0.4759 0.3847 0.2987 0.1130 0.0767 0.0616 106 ASP A OD2 468 N N . SER A 66 ? 0.4317 0.3594 0.3335 0.0818 0.0895 0.0658 107 SER A N 469 C CA . SER A 66 ? 0.4101 0.3446 0.3345 0.0730 0.0922 0.0651 107 SER A CA 470 C C . SER A 66 ? 0.3818 0.3207 0.3147 0.0680 0.0829 0.0587 107 SER A C 471 O O . SER A 66 ? 0.3627 0.3037 0.2878 0.0695 0.0742 0.0533 107 SER A O 472 C CB . SER A 66 ? 0.4069 0.3497 0.3394 0.0697 0.0935 0.0627 107 SER A CB 473 O OG A SER A 66 ? 0.3748 0.3240 0.3044 0.0686 0.0840 0.0553 107 SER A OG 474 O OG B SER A 66 ? 0.4270 0.3790 0.3770 0.0616 0.0884 0.0571 107 SER A OG 475 N N . VAL A 67 ? 0.3727 0.3126 0.3218 0.0622 0.0850 0.0594 108 VAL A N 476 C CA . VAL A 67 ? 0.3584 0.3029 0.3163 0.0572 0.0769 0.0529 108 VAL A CA 477 C C . VAL A 67 ? 0.3613 0.3112 0.3400 0.0492 0.0788 0.0515 108 VAL A C 478 O O . VAL A 67 ? 0.3853 0.3309 0.3734 0.0476 0.0855 0.0562 108 VAL A O 479 C CB . VAL A 67 ? 0.3689 0.3063 0.3220 0.0600 0.0749 0.0541 108 VAL A CB 480 C CG1 . VAL A 67 ? 0.3518 0.2952 0.3119 0.0558 0.0660 0.0464 108 VAL A CG1 481 C CG2 . VAL A 67 ? 0.3824 0.3125 0.3145 0.0690 0.0734 0.0566 108 VAL A CG2 482 N N . GLU A 68 ? 0.3449 0.3036 0.3307 0.0444 0.0729 0.0450 109 GLU A N 483 C CA . GLU A 68 ? 0.3563 0.3202 0.3604 0.0374 0.0736 0.0431 109 GLU A CA 484 C C . GLU A 68 ? 0.3372 0.3056 0.3475 0.0328 0.0657 0.0359 109 GLU A C 485 O O . GLU A 68 ? 0.3534 0.3234 0.3546 0.0344 0.0595 0.0320 109 GLU A O 486 C CB . GLU A 68 ? 0.3769 0.3475 0.3848 0.0359 0.0745 0.0422 109 GLU A CB 487 C CG . GLU A 68 ? 0.4550 0.4219 0.4585 0.0403 0.0838 0.0493 109 GLU A CG 488 C CD . GLU A 68 ? 0.5852 0.5474 0.6003 0.0390 0.0928 0.0555 109 GLU A CD 489 O OE1 . GLU A 68 ? 0.6160 0.5812 0.6492 0.0329 0.0921 0.0536 109 GLU A OE1 490 O OE2 . GLU A 68 ? 0.6495 0.6047 0.6557 0.0444 0.1007 0.0625 109 GLU A OE2 491 N N . LEU A 69 ? 0.3222 0.2926 0.3485 0.0272 0.0659 0.0342 110 LEU A N 492 C CA . LEU A 69 ? 0.3087 0.2842 0.3403 0.0228 0.0583 0.0268 110 LEU A CA 493 C C . LEU A 69 ? 0.3116 0.2949 0.3486 0.0193 0.0554 0.0233 110 LEU A C 494 O O . LEU A 69 ? 0.3381 0.3232 0.3851 0.0175 0.0594 0.0258 110 LEU A O 495 C CB . LEU A 69 ? 0.3256 0.2984 0.3701 0.0191 0.0584 0.0254 110 LEU A CB 496 C CG . LEU A 69 ? 0.3419 0.3062 0.3837 0.0219 0.0612 0.0287 110 LEU A CG 497 C CD1 . LEU A 69 ? 0.4078 0.3706 0.4639 0.0174 0.0597 0.0255 110 LEU A CD1 498 C CD2 . LEU A 69 ? 0.3584 0.3215 0.3861 0.0261 0.0569 0.0267 110 LEU A CD2 499 N N . ALA A 70 ? 0.2889 0.2768 0.3203 0.0184 0.0488 0.0180 111 ALA A N 500 C CA . ALA A 70 ? 0.2764 0.2711 0.3119 0.0153 0.0452 0.0145 111 ALA A CA 501 C C . ALA A 70 ? 0.2745 0.2711 0.3158 0.0112 0.0397 0.0086 111 ALA A C 502 O O . ALA A 70 ? 0.3091 0.3054 0.3430 0.0120 0.0361 0.0054 111 ALA A O 503 C CB . ALA A 70 ? 0.2931 0.2907 0.3162 0.0179 0.0421 0.0134 111 ALA A CB 504 N N . HIS A 71 ? 0.2791 0.2777 0.3336 0.0071 0.0390 0.0069 112 HIS A N 505 C CA . HIS A 71 ? 0.2723 0.2716 0.3312 0.0038 0.0335 0.0008 112 HIS A CA 506 C C . HIS A 71 ? 0.2565 0.2616 0.3165 0.0012 0.0280 -0.0035 112 HIS A C 507 O O . HIS A 71 ? 0.2738 0.2824 0.3367 0.0009 0.0286 -0.0018 112 HIS A O 508 C CB . HIS A 71 ? 0.2826 0.2781 0.3554 0.0012 0.0352 0.0008 112 HIS A CB 509 C CG . HIS A 71 ? 0.3187 0.3167 0.4062 -0.0015 0.0370 0.0024 112 HIS A CG 510 N ND1 . HIS A 71 ? 0.3798 0.3760 0.4735 -0.0003 0.0445 0.0089 112 HIS A ND1 511 C CD2 . HIS A 71 ? 0.3324 0.3346 0.4300 -0.0051 0.0323 -0.0018 112 HIS A CD2 512 C CE1 . HIS A 71 ? 0.3819 0.3817 0.4904 -0.0034 0.0446 0.0087 112 HIS A CE1 513 N NE2 . HIS A 71 ? 0.3831 0.3866 0.4947 -0.0063 0.0368 0.0020 112 HIS A NE2 514 N N . TYR A 72 ? 0.2518 0.2574 0.3089 -0.0004 0.0226 -0.0092 113 TYR A N 515 C CA . TYR A 72 ? 0.2513 0.2612 0.3067 -0.0023 0.0169 -0.0135 113 TYR A CA 516 C C . TYR A 72 ? 0.2519 0.2600 0.3103 -0.0044 0.0126 -0.0191 113 TYR A C 517 O O . TYR A 72 ? 0.2656 0.2696 0.3234 -0.0037 0.0139 -0.0200 113 TYR A O 518 C CB . TYR A 72 ? 0.2378 0.2500 0.2791 -0.0004 0.0152 -0.0140 113 TYR A CB 519 C CG . TYR A 72 ? 0.2261 0.2391 0.2631 0.0023 0.0190 -0.0089 113 TYR A CG 520 C CD1 . TYR A 72 ? 0.2126 0.2289 0.2521 0.0021 0.0189 -0.0072 113 TYR A CD1 521 C CD2 . TYR A 72 ? 0.2687 0.2786 0.2999 0.0054 0.0225 -0.0060 113 TYR A CD2 522 C CE1 . TYR A 72 ? 0.2726 0.2889 0.3078 0.0050 0.0226 -0.0029 113 TYR A CE1 523 C CE2 . TYR A 72 ? 0.2729 0.2827 0.2992 0.0084 0.0255 -0.0019 113 TYR A CE2 524 C CZ . TYR A 72 ? 0.2747 0.2874 0.3029 0.0082 0.0258 -0.0004 113 TYR A CZ 525 O OH . TYR A 72 ? 0.2903 0.3023 0.3127 0.0118 0.0291 0.0035 113 TYR A OH 526 N N . ASP A 73 ? 0.2499 0.2604 0.3103 -0.0064 0.0072 -0.0232 114 ASP A N 527 C CA . ASP A 73 ? 0.2547 0.2629 0.3158 -0.0079 0.0022 -0.0295 114 ASP A CA 528 C C . ASP A 73 ? 0.2510 0.2611 0.2986 -0.0070 -0.0017 -0.0327 114 ASP A C 529 O O . ASP A 73 ? 0.2433 0.2564 0.2892 -0.0076 -0.0052 -0.0333 114 ASP A O 530 C CB . ASP A 73 ? 0.2769 0.2856 0.3525 -0.0107 -0.0018 -0.0322 114 ASP A CB 531 C CG . ASP A 73 ? 0.3179 0.3247 0.4089 -0.0119 0.0030 -0.0286 114 ASP A CG 532 O OD1 . ASP A 73 ? 0.3326 0.3347 0.4241 -0.0113 0.0061 -0.0281 114 ASP A OD1 533 O OD2 . ASP A 73 ? 0.3752 0.3849 0.4777 -0.0132 0.0039 -0.0261 114 ASP A OD2 534 N N . VAL A 74 ? 0.2452 0.2531 0.2834 -0.0055 -0.0007 -0.0345 115 VAL A N 535 C CA . VAL A 74 ? 0.2435 0.2531 0.2683 -0.0044 -0.0023 -0.0362 115 VAL A CA 536 C C . VAL A 74 ? 0.2601 0.2666 0.2794 -0.0041 -0.0050 -0.0421 115 VAL A C 537 O O . VAL A 74 ? 0.2674 0.2702 0.2922 -0.0041 -0.0047 -0.0445 115 VAL A O 538 C CB . VAL A 74 ? 0.2398 0.2506 0.2578 -0.0022 0.0023 -0.0323 115 VAL A CB 539 C CG1 . VAL A 74 ? 0.2281 0.2412 0.2496 -0.0019 0.0048 -0.0268 115 VAL A CG1 540 C CG2 . VAL A 74 ? 0.2353 0.2428 0.2541 -0.0007 0.0056 -0.0326 115 VAL A CG2 541 N N . LEU A 75 ? 0.2621 0.2698 0.2699 -0.0033 -0.0070 -0.0440 116 LEU A N 542 C CA . LEU A 75 ? 0.2638 0.2682 0.2640 -0.0023 -0.0088 -0.0496 116 LEU A CA 543 C C . LEU A 75 ? 0.2615 0.2649 0.2588 -0.0005 -0.0038 -0.0494 116 LEU A C 544 O O . LEU A 75 ? 0.2789 0.2851 0.2713 0.0006 -0.0002 -0.0460 116 LEU A O 545 C CB . LEU A 75 ? 0.2597 0.2651 0.2473 -0.0016 -0.0114 -0.0508 116 LEU A CB 546 C CG . LEU A 75 ? 0.2893 0.2906 0.2677 -0.0002 -0.0140 -0.0571 116 LEU A CG 547 C CD1 . LEU A 75 ? 0.3167 0.3151 0.3020 -0.0013 -0.0207 -0.0618 116 LEU A CD1 548 C CD2 . LEU A 75 ? 0.3247 0.3266 0.2884 0.0011 -0.0145 -0.0568 116 LEU A CD2 549 N N . LEU A 76 ? 0.2741 0.2735 0.2751 0.0000 -0.0041 -0.0533 117 LEU A N 550 C CA . LEU A 76 ? 0.2756 0.2735 0.2740 0.0022 0.0000 -0.0541 117 LEU A CA 551 C C . LEU A 76 ? 0.2956 0.2901 0.2862 0.0036 -0.0019 -0.0607 117 LEU A C 552 O O . LEU A 76 ? 0.3118 0.3048 0.2985 0.0030 -0.0066 -0.0643 117 LEU A O 553 C CB . LEU A 76 ? 0.2688 0.2641 0.2782 0.0022 0.0023 -0.0522 117 LEU A CB 554 C CG . LEU A 76 ? 0.2739 0.2716 0.2894 0.0017 0.0049 -0.0455 117 LEU A CG 555 C CD1 . LEU A 76 ? 0.2602 0.2540 0.2839 0.0027 0.0078 -0.0436 117 LEU A CD1 556 C CD2 . LEU A 76 ? 0.2780 0.2803 0.2859 0.0031 0.0076 -0.0419 117 LEU A CD2 557 N N . SER A 77 ? 0.2915 0.2849 0.2793 0.0059 0.0017 -0.0624 118 SER A N 558 C CA . SER A 77 ? 0.3105 0.3007 0.2891 0.0080 0.0010 -0.0687 118 SER A CA 559 C C . SER A 77 ? 0.3248 0.3116 0.3084 0.0099 0.0034 -0.0713 118 SER A C 560 O O . SER A 77 ? 0.3124 0.3013 0.3010 0.0107 0.0076 -0.0676 118 SER A O 561 C CB . SER A 77 ? 0.3326 0.3264 0.2992 0.0095 0.0045 -0.0674 118 SER A CB 562 O OG . SER A 77 ? 0.3472 0.3381 0.3048 0.0124 0.0062 -0.0726 118 SER A OG 563 N N . TYR A 78 ? 0.3315 0.3127 0.3140 0.0109 0.0004 -0.0779 119 TYR A N 564 C CA . TYR A 78 ? 0.3325 0.3098 0.3200 0.0129 0.0024 -0.0808 119 TYR A CA 565 C C . TYR A 78 ? 0.3516 0.3242 0.3297 0.0156 0.0011 -0.0887 119 TYR A C 566 O O . TYR A 78 ? 0.3778 0.3479 0.3495 0.0153 -0.0040 -0.0929 119 TYR A O 567 C CB . TYR A 78 ? 0.3241 0.2970 0.3251 0.0109 -0.0006 -0.0810 119 TYR A CB 568 C CG . TYR A 78 ? 0.3332 0.3090 0.3441 0.0085 0.0008 -0.0736 119 TYR A CG 569 C CD1 . TYR A 78 ? 0.3263 0.3038 0.3406 0.0098 0.0057 -0.0685 119 TYR A CD1 570 C CD2 . TYR A 78 ? 0.3519 0.3283 0.3683 0.0053 -0.0028 -0.0720 119 TYR A CD2 571 C CE1 . TYR A 78 ? 0.3105 0.2900 0.3320 0.0082 0.0071 -0.0616 119 TYR A CE1 572 C CE2 . TYR A 78 ? 0.3665 0.3453 0.3916 0.0035 -0.0008 -0.0651 119 TYR A CE2 573 C CZ . TYR A 78 ? 0.3426 0.3224 0.3693 0.0052 0.0043 -0.0601 119 TYR A CZ 574 O OH . TYR A 78 ? 0.3308 0.3120 0.3641 0.0040 0.0065 -0.0534 119 TYR A OH 575 N N . PRO A 79 ? 0.3674 0.3385 0.3453 0.0187 0.0050 -0.0911 120 PRO A N 576 C CA . PRO A 79 ? 0.3759 0.3412 0.3453 0.0217 0.0035 -0.0994 120 PRO A CA 577 C C . PRO A 79 ? 0.4144 0.3725 0.3904 0.0206 -0.0033 -0.1049 120 PRO A C 578 O O . PRO A 79 ? 0.4011 0.3581 0.3911 0.0177 -0.0052 -0.1021 120 PRO A O 579 C CB . PRO A 79 ? 0.3962 0.3614 0.3679 0.0252 0.0093 -0.1003 120 PRO A CB 580 C CG . PRO A 79 ? 0.3677 0.3399 0.3456 0.0242 0.0139 -0.0923 120 PRO A CG 581 C CD . PRO A 79 ? 0.3415 0.3151 0.3262 0.0201 0.0104 -0.0871 120 PRO A CD 582 N N . ASN A 80 ? 0.4284 0.3811 0.3942 0.0230 -0.0069 -0.1129 121 ASN A N 583 C CA . ASN A 80 ? 0.4850 0.4301 0.4573 0.0224 -0.0138 -0.1196 121 ASN A CA 584 C C . ASN A 80 ? 0.5008 0.4408 0.4799 0.0248 -0.0113 -0.1229 121 ASN A C 585 O O . ASN A 80 ? 0.5076 0.4466 0.4774 0.0291 -0.0073 -0.1264 121 ASN A O 586 C CB . ASN A 80 ? 0.4955 0.4364 0.4525 0.0247 -0.0193 -0.1272 121 ASN A CB 587 C CG . ASN A 80 ? 0.5495 0.4826 0.5132 0.0239 -0.0282 -0.1350 121 ASN A CG 588 O OD1 . ASN A 80 ? 0.5789 0.5075 0.5551 0.0235 -0.0287 -0.1372 121 ASN A OD1 589 N ND2 . ASN A 80 ? 0.6177 0.5488 0.5735 0.0238 -0.0356 -0.1392 121 ASN A ND2 590 N N . LYS A 81 ? 0.5248 0.4619 0.5206 0.0222 -0.0130 -0.1212 122 LYS A N 591 C CA . LYS A 81 ? 0.5570 0.4886 0.5614 0.0242 -0.0110 -0.1236 122 LYS A CA 592 C C . LYS A 81 ? 0.5795 0.5029 0.5777 0.0278 -0.0144 -0.1342 122 LYS A C 593 O O . LYS A 81 ? 0.5869 0.5069 0.5861 0.0312 -0.0110 -0.1368 122 LYS A O 594 C CB . LYS A 81 ? 0.5618 0.4904 0.5850 0.0203 -0.0128 -0.1197 122 LYS A CB 595 C CG . LYS A 81 ? 0.5998 0.5342 0.6296 0.0188 -0.0071 -0.1093 122 LYS A CG 596 C CD . LYS A 81 ? 0.6638 0.5962 0.7100 0.0145 -0.0089 -0.1045 122 LYS A CD 597 C CE . LYS A 81 ? 0.6983 0.6377 0.7464 0.0127 -0.0045 -0.0944 122 LYS A CE 598 N NZ . LYS A 81 ? 0.7365 0.6759 0.7964 0.0082 -0.0068 -0.0904 122 LYS A NZ 599 N N . THR A 82 ? 0.5953 0.5153 0.5865 0.0275 -0.0214 -0.1407 123 THR A N 600 C CA . THR A 82 ? 0.6250 0.5361 0.6092 0.0313 -0.0259 -0.1517 123 THR A CA 601 C C . THR A 82 ? 0.6359 0.5472 0.5970 0.0360 -0.0252 -0.1568 123 THR A C 602 O O . THR A 82 ? 0.6555 0.5593 0.6072 0.0398 -0.0293 -0.1664 123 THR A O 603 C CB . THR A 82 ? 0.6402 0.5442 0.6358 0.0282 -0.0359 -0.1574 123 THR A CB 604 O OG1 . THR A 82 ? 0.6579 0.5650 0.6486 0.0259 -0.0417 -0.1574 123 THR A OG1 605 C CG2 . THR A 82 ? 0.6270 0.5304 0.6456 0.0237 -0.0350 -0.1515 123 THR A CG2 606 N N . HIS A 83 ? 0.6203 0.5397 0.5722 0.0361 -0.0194 -0.1502 124 HIS A N 607 C CA . HIS A 83 ? 0.6272 0.5475 0.5575 0.0401 -0.0173 -0.1529 124 HIS A CA 608 C C . HIS A 83 ? 0.5963 0.5257 0.5239 0.0406 -0.0072 -0.1445 124 HIS A C 609 O O . HIS A 83 ? 0.5801 0.5157 0.5036 0.0384 -0.0060 -0.1384 124 HIS A O 610 C CB . HIS A 83 ? 0.6431 0.5635 0.5661 0.0381 -0.0247 -0.1535 124 HIS A CB 611 C CG . HIS A 83 ? 0.7184 0.6356 0.6176 0.0429 -0.0257 -0.1588 124 HIS A CG 612 N ND1 . HIS A 83 ? 0.7970 0.7092 0.6826 0.0490 -0.0217 -0.1652 124 HIS A ND1 613 C CD2 . HIS A 83 ? 0.7635 0.6809 0.6493 0.0431 -0.0302 -0.1589 124 HIS A CD2 614 C CE1 . HIS A 83 ? 0.8221 0.7315 0.6860 0.0527 -0.0233 -0.1686 124 HIS A CE1 615 N NE2 . HIS A 83 ? 0.8148 0.7271 0.6782 0.0492 -0.0287 -0.1648 124 HIS A NE2 616 N N . PRO A 84 ? 0.5788 0.5088 0.5099 0.0435 -0.0003 -0.1444 125 PRO A N 617 C CA . PRO A 84 ? 0.5559 0.4948 0.4896 0.0434 0.0086 -0.1365 125 PRO A CA 618 C C . PRO A 84 ? 0.5495 0.4931 0.4667 0.0458 0.0144 -0.1347 125 PRO A C 619 O O . PRO A 84 ? 0.5639 0.5028 0.4645 0.0496 0.0140 -0.1409 125 PRO A O 620 C CB . PRO A 84 ? 0.5686 0.5055 0.5108 0.0467 0.0130 -0.1388 125 PRO A CB 621 C CG . PRO A 84 ? 0.5816 0.5084 0.5180 0.0501 0.0083 -0.1493 125 PRO A CG 622 C CD . PRO A 84 ? 0.5919 0.5144 0.5284 0.0465 -0.0013 -0.1516 125 PRO A CD 623 N N . ASN A 85 ? 0.4971 0.4494 0.4187 0.0435 0.0195 -0.1262 126 ASN A N 624 C CA . ASN A 85 ? 0.4918 0.4495 0.4010 0.0450 0.0261 -0.1229 126 ASN A CA 625 C C . ASN A 85 ? 0.4947 0.4540 0.4017 0.0498 0.0349 -0.1249 126 ASN A C 626 O O . ASN A 85 ? 0.4888 0.4498 0.4094 0.0504 0.0373 -0.1243 126 ASN A O 627 C CB . ASN A 85 ? 0.4479 0.4143 0.3651 0.0406 0.0281 -0.1132 126 ASN A CB 628 C CG . ASN A 85 ? 0.4709 0.4366 0.3900 0.0362 0.0204 -0.1108 126 ASN A CG 629 O OD1 . ASN A 85 ? 0.4677 0.4284 0.3766 0.0364 0.0147 -0.1150 126 ASN A OD1 630 N ND2 . ASN A 85 ? 0.4215 0.3923 0.3538 0.0323 0.0200 -0.1041 126 ASN A ND2 631 N N . TYR A 86 ? 0.5215 0.4795 0.4112 0.0537 0.0396 -0.1275 127 TYR A N 632 C CA . TYR A 86 ? 0.5280 0.4892 0.4165 0.0581 0.0497 -0.1282 127 TYR A CA 633 C C . TYR A 86 ? 0.5418 0.5040 0.4119 0.0609 0.0565 -0.1272 127 TYR A C 634 O O . TYR A 86 ? 0.5334 0.4923 0.3894 0.0601 0.0525 -0.1270 127 TYR A O 635 C CB . TYR A 86 ? 0.5495 0.5043 0.4397 0.0627 0.0497 -0.1365 127 TYR A CB 636 C CG . TYR A 86 ? 0.5779 0.5227 0.4495 0.0668 0.0459 -0.1454 127 TYR A CG 637 C CD1 . TYR A 86 ? 0.6062 0.5483 0.4632 0.0732 0.0532 -0.1502 127 TYR A CD1 638 C CD2 . TYR A 86 ? 0.5949 0.5327 0.4635 0.0647 0.0350 -0.1492 127 TYR A CD2 639 C CE1 . TYR A 86 ? 0.6334 0.5655 0.4715 0.0777 0.0492 -0.1589 127 TYR A CE1 640 C CE2 . TYR A 86 ? 0.6242 0.5523 0.4755 0.0688 0.0303 -0.1581 127 TYR A CE2 641 C CZ . TYR A 86 ? 0.6516 0.5766 0.4869 0.0755 0.0373 -0.1630 127 TYR A CZ 642 O OH . TYR A 86 ? 0.6671 0.5818 0.4838 0.0801 0.0321 -0.1722 127 TYR A OH 643 N N . ILE A 87 ? 0.5324 0.4993 0.4036 0.0642 0.0670 -0.1261 128 ILE A N 644 C CA . ILE A 87 ? 0.5264 0.4944 0.3813 0.0672 0.0755 -0.1244 128 ILE A CA 645 C C . ILE A 87 ? 0.5511 0.5146 0.3977 0.0741 0.0818 -0.1317 128 ILE A C 646 O O . ILE A 87 ? 0.5316 0.4962 0.3917 0.0758 0.0832 -0.1348 128 ILE A O 647 C CB . ILE A 87 ? 0.5167 0.4957 0.3819 0.0644 0.0840 -0.1152 128 ILE A CB 648 C CG1 . ILE A 87 ? 0.4894 0.4722 0.3622 0.0578 0.0774 -0.1083 128 ILE A CG1 649 C CG2 . ILE A 87 ? 0.5527 0.5321 0.4014 0.0677 0.0943 -0.1132 128 ILE A CG2 650 C CD1 . ILE A 87 ? 0.5079 0.5012 0.3981 0.0545 0.0826 -0.1006 128 ILE A CD1 651 N N . SER A 88 ? 0.5759 0.5338 0.3996 0.0785 0.0851 -0.1346 129 SER A N 652 C CA . SER A 88 ? 0.6000 0.5534 0.4125 0.0859 0.0926 -0.1412 129 SER A CA 653 C C . SER A 88 ? 0.6151 0.5717 0.4149 0.0892 0.1057 -0.1371 129 SER A C 654 O O . SER A 88 ? 0.6076 0.5657 0.3982 0.0869 0.1071 -0.1308 129 SER A O 655 C CB . SER A 88 ? 0.6322 0.5727 0.4250 0.0902 0.0845 -0.1510 129 SER A CB 656 O OG . SER A 88 ? 0.6610 0.5977 0.4668 0.0879 0.0737 -0.1560 129 SER A OG 657 N N . ILE A 89 ? 0.6363 0.5934 0.4354 0.0951 0.1157 -0.1408 130 ILE A N 658 C CA . ILE A 89 ? 0.6645 0.6198 0.4436 0.1006 0.1276 -0.1400 130 ILE A CA 659 C C . ILE A 89 ? 0.7056 0.6473 0.4596 0.1073 0.1228 -0.1502 130 ILE A C 660 O O . ILE A 89 ? 0.6893 0.6261 0.4474 0.1101 0.1180 -0.1587 130 ILE A O 661 C CB . ILE A 89 ? 0.6627 0.6263 0.4539 0.1038 0.1424 -0.1382 130 ILE A CB 662 C CG1 . ILE A 89 ? 0.6563 0.6331 0.4713 0.0974 0.1469 -0.1281 130 ILE A CG1 663 C CG2 . ILE A 89 ? 0.6874 0.6462 0.4538 0.1112 0.1551 -0.1393 130 ILE A CG2 664 C CD1 . ILE A 89 ? 0.6912 0.6773 0.5237 0.0999 0.1597 -0.1267 130 ILE A CD1 665 N N . ILE A 90 ? 0.7444 0.6798 0.4727 0.1097 0.1233 -0.1492 131 ILE A N 666 C CA . ILE A 90 ? 0.8049 0.7266 0.5064 0.1162 0.1173 -0.1587 131 ILE A CA 667 C C . ILE A 90 ? 0.8477 0.7652 0.5244 0.1244 0.1309 -0.1592 131 ILE A C 668 O O . ILE A 90 ? 0.8504 0.7722 0.5207 0.1236 0.1405 -0.1504 131 ILE A O 669 C CB . ILE A 90 ? 0.8109 0.7266 0.5024 0.1123 0.1024 -0.1587 131 ILE A CB 670 C CG1 . ILE A 90 ? 0.8508 0.7529 0.5240 0.1175 0.0912 -0.1707 131 ILE A CG1 671 C CG2 . ILE A 90 ? 0.8210 0.7383 0.4982 0.1109 0.1069 -0.1495 131 ILE A CG2 672 C CD1 . ILE A 90 ? 0.8592 0.7566 0.5290 0.1132 0.0750 -0.1716 131 ILE A CD1 673 N N . ASN A 91 ? 0.8849 0.7940 0.5485 0.1323 0.1324 -0.1692 132 ASN A N 674 C CA . ASN A 91 ? 0.9407 0.8442 0.5778 0.1412 0.1453 -0.1707 132 ASN A CA 675 C C . ASN A 91 ? 0.9804 0.8710 0.5830 0.1455 0.1384 -0.1737 132 ASN A C 676 O O . ASN A 91 ? 0.9737 0.8600 0.5747 0.1416 0.1230 -0.1755 132 ASN A O 677 C CB . ASN A 91 ? 0.9547 0.8556 0.5927 0.1487 0.1522 -0.1797 132 ASN A CB 678 C CG . ASN A 91 ? 0.9742 0.8618 0.5997 0.1533 0.1387 -0.1932 132 ASN A CG 679 O OD1 . ASN A 91 ? 0.9876 0.8663 0.5974 0.1527 0.1256 -0.1966 132 ASN A OD1 680 N ND2 . ASN A 91 ? 0.9638 0.8501 0.5976 0.1579 0.1418 -0.2012 132 ASN A ND2 681 N N . GLU A 92 ? 1.0305 0.9146 0.6054 0.1539 0.1496 -0.1743 133 GLU A N 682 C CA . GLU A 92 ? 1.0799 0.9515 0.6195 0.1589 0.1442 -0.1761 133 GLU A CA 683 C C . GLU A 92 ? 1.0994 0.9578 0.6247 0.1625 0.1265 -0.1894 133 GLU A C 684 O O . GLU A 92 ? 1.1186 0.9679 0.6220 0.1639 0.1160 -0.1909 133 GLU A O 685 C CB . GLU A 92 ? 1.1141 0.9809 0.6268 0.1681 0.1614 -0.1743 133 GLU A CB 686 C CG . GLU A 92 ? 1.1645 1.0229 0.6449 0.1713 0.1618 -0.1692 133 GLU A CG 687 C CD . GLU A 92 ? 1.2263 1.0785 0.6784 0.1816 0.1795 -0.1683 133 GLU A CD 688 O OE1 . GLU A 92 ? 1.2384 1.1002 0.7054 0.1815 0.1969 -0.1628 133 GLU A OE1 689 O OE2 . GLU A 92 ? 1.2715 1.1093 0.6869 0.1899 0.1760 -0.1732 133 GLU A OE2 690 N N . ASP A 93 ? 1.0999 0.9571 0.6386 0.1641 0.1228 -0.1989 134 ASP A N 691 C CA . ASP A 93 ? 1.1173 0.9624 0.6470 0.1671 0.1061 -0.2121 134 ASP A CA 692 C C . ASP A 93 ? 1.0889 0.9371 0.6416 0.1576 0.0889 -0.2121 134 ASP A C 693 O O . ASP A 93 ? 1.1061 0.9450 0.6550 0.1587 0.0738 -0.2223 134 ASP A O 694 C CB . ASP A 93 ? 1.1301 0.9718 0.6647 0.1731 0.1100 -0.2225 134 ASP A CB 695 C CG . ASP A 93 ? 1.1781 1.0144 0.6860 0.1841 0.1258 -0.2247 134 ASP A CG 696 O OD1 . ASP A 93 ? 1.2183 1.0486 0.6966 0.1887 0.1299 -0.2214 134 ASP A OD1 697 O OD2 . ASP A 93 ? 1.1997 1.0374 0.7158 0.1884 0.1345 -0.2296 134 ASP A OD2 698 N N . GLY A 94 ? 1.0463 0.9072 0.6230 0.1484 0.0913 -0.2008 135 GLY A N 699 C CA . GLY A 94 ? 1.0084 0.8735 0.6090 0.1393 0.0772 -0.1995 135 GLY A CA 700 C C . GLY A 94 ? 0.9748 0.8448 0.6052 0.1358 0.0752 -0.2032 135 GLY A C 701 O O . GLY A 94 ? 0.9705 0.8411 0.6191 0.1296 0.0626 -0.2047 135 GLY A O 702 N N . ASN A 95 ? 0.9572 0.8303 0.5929 0.1400 0.0879 -0.2043 136 ASN A N 703 C CA . ASN A 95 ? 0.9185 0.7968 0.5829 0.1372 0.0876 -0.2066 136 ASN A CA 704 C C . ASN A 95 ? 0.8628 0.7560 0.5539 0.1292 0.0937 -0.1946 136 ASN A C 705 O O . ASN A 95 ? 0.8459 0.7466 0.5348 0.1294 0.1063 -0.1862 136 ASN A O 706 C CB . ASN A 95 ? 0.9401 0.8157 0.5998 0.1456 0.0982 -0.2133 136 ASN A CB 707 C CG . ASN A 95 ? 0.9949 0.8550 0.6257 0.1547 0.0933 -0.2259 136 ASN A CG 708 O OD1 . ASN A 95 ? 1.0357 0.8921 0.6491 0.1633 0.1045 -0.2295 136 ASN A OD1 709 N ND2 . ASN A 95 ? 1.0372 0.8881 0.6633 0.1532 0.0765 -0.2329 136 ASN A ND2 710 N N . GLU A 96 ? 0.8311 0.7281 0.5474 0.1225 0.0846 -0.1937 137 GLU A N 711 C CA . GLU A 96 ? 0.7718 0.6821 0.5145 0.1153 0.0890 -0.1834 137 GLU A CA 712 C C . GLU A 96 ? 0.7645 0.6795 0.5243 0.1181 0.0976 -0.1852 137 GLU A C 713 O O . GLU A 96 ? 0.7633 0.6747 0.5358 0.1182 0.0912 -0.1914 137 GLU A O 714 C CB . GLU A 96 ? 0.7505 0.6621 0.5103 0.1072 0.0756 -0.1811 137 GLU A CB 715 C CG . GLU A 96 ? 0.7439 0.6499 0.4872 0.1053 0.0658 -0.1811 137 GLU A CG 716 C CD . GLU A 96 ? 0.7257 0.6351 0.4869 0.0968 0.0548 -0.1767 137 GLU A CD 717 O OE1 . GLU A 96 ? 0.7051 0.6159 0.4875 0.0936 0.0502 -0.1781 137 GLU A OE1 718 O OE2 . GLU A 96 ? 0.7299 0.6401 0.4827 0.0939 0.0509 -0.1720 137 GLU A OE2 719 N N . ILE A 97 ? 0.7565 0.6793 0.5166 0.1205 0.1122 -0.1799 138 ILE A N 720 C CA . ILE A 97 ? 0.7552 0.6823 0.5284 0.1248 0.1222 -0.1823 138 ILE A CA 721 C C . ILE A 97 ? 0.7166 0.6560 0.5215 0.1189 0.1235 -0.1752 138 ILE A C 722 O O . ILE A 97 ? 0.7158 0.6587 0.5361 0.1217 0.1286 -0.1775 138 ILE A O 723 C CB . ILE A 97 ? 0.7729 0.7018 0.5307 0.1318 0.1385 -0.1814 138 ILE A CB 724 C CG1 . ILE A 97 ? 0.7750 0.7137 0.5342 0.1275 0.1471 -0.1694 138 ILE A CG1 725 C CG2 . ILE A 97 ? 0.8036 0.7186 0.5288 0.1397 0.1374 -0.1904 138 ILE A CG2 726 C CD1 . ILE A 97 ? 0.7883 0.7309 0.5383 0.1334 0.1652 -0.1667 138 ILE A CD1 727 N N . PHE A 98 ? 0.6863 0.6317 0.5005 0.1111 0.1185 -0.1668 139 PHE A N 728 C CA . PHE A 98 ? 0.6484 0.6039 0.4905 0.1055 0.1174 -0.1605 139 PHE A CA 729 C C . PHE A 98 ? 0.6191 0.5741 0.4652 0.0980 0.1054 -0.1563 139 PHE A C 730 O O . PHE A 98 ? 0.6091 0.5622 0.4403 0.0960 0.1032 -0.1533 139 PHE A O 731 C CB . PHE A 98 ? 0.6389 0.6068 0.4911 0.1044 0.1299 -0.1519 139 PHE A CB 732 C CG . PHE A 98 ? 0.6240 0.6019 0.5014 0.0977 0.1267 -0.1444 139 PHE A CG 733 C CD1 . PHE A 98 ? 0.6268 0.6086 0.5261 0.0982 0.1256 -0.1457 139 PHE A CD1 734 C CD2 . PHE A 98 ? 0.6212 0.6038 0.4996 0.0913 0.1239 -0.1362 139 PHE A CD2 735 C CE1 . PHE A 98 ? 0.6218 0.6119 0.5428 0.0926 0.1219 -0.1390 139 PHE A CE1 736 C CE2 . PHE A 98 ? 0.5881 0.5792 0.4887 0.0855 0.1204 -0.1297 139 PHE A CE2 737 C CZ . PHE A 98 ? 0.5864 0.5810 0.5076 0.0863 0.1192 -0.1312 139 PHE A CZ 738 N N . ASN A 99 ? 0.6037 0.5599 0.4696 0.0944 0.0980 -0.1560 140 ASN A N 739 C CA . ASN A 99 ? 0.5768 0.5340 0.4506 0.0872 0.0880 -0.1510 140 ASN A CA 740 C C . ASN A 99 ? 0.5521 0.5193 0.4499 0.0827 0.0887 -0.1435 140 ASN A C 741 O O . ASN A 99 ? 0.5377 0.5072 0.4505 0.0848 0.0909 -0.1449 140 ASN A O 742 C CB . ASN A 99 ? 0.5907 0.5379 0.4648 0.0865 0.0761 -0.1577 140 ASN A CB 743 C CG . ASN A 99 ? 0.6247 0.5608 0.4756 0.0906 0.0721 -0.1660 140 ASN A CG 744 O OD1 . ASN A 99 ? 0.6371 0.5725 0.4694 0.0917 0.0747 -0.1648 140 ASN A OD1 745 N ND2 . ASN A 99 ? 0.6893 0.6163 0.5413 0.0929 0.0655 -0.1746 140 ASN A ND2 746 N N . THR A 100 ? 0.5276 0.4998 0.4284 0.0768 0.0858 -0.1359 141 THR A N 747 C CA . THR A 100 ? 0.5055 0.4858 0.4274 0.0724 0.0844 -0.1291 141 THR A CA 748 C C . THR A 100 ? 0.4995 0.4746 0.4323 0.0706 0.0749 -0.1313 141 THR A C 749 O O . THR A 100 ? 0.5049 0.4707 0.4292 0.0712 0.0683 -0.1371 141 THR A O 750 C CB . THR A 100 ? 0.4969 0.4832 0.4180 0.0670 0.0838 -0.1208 141 THR A CB 751 O OG1 . THR A 100 ? 0.5064 0.4863 0.4165 0.0640 0.0751 -0.1216 141 THR A OG1 752 C CG2 . THR A 100 ? 0.4948 0.4859 0.4063 0.0688 0.0942 -0.1181 141 THR A CG2 753 N N . SER A 101 ? 0.4826 0.4632 0.4340 0.0686 0.0740 -0.1267 142 SER A N 754 C CA . SER A 101 ? 0.4733 0.4490 0.4362 0.0675 0.0667 -0.1279 142 SER A CA 755 C C . SER A 101 ? 0.4727 0.4433 0.4324 0.0626 0.0575 -0.1264 142 SER A C 756 O O . SER A 101 ? 0.4836 0.4572 0.4367 0.0589 0.0564 -0.1221 142 SER A O 757 C CB . SER A 101 ? 0.4750 0.4582 0.4567 0.0668 0.0680 -0.1221 142 SER A CB 758 O OG A SER A 101 ? 0.3917 0.3802 0.3773 0.0615 0.0651 -0.1144 142 SER A OG 759 O OG B SER A 101 ? 0.5084 0.4861 0.5006 0.0679 0.0632 -0.1240 142 SER A OG 760 N N . LEU A 102 ? 0.4778 0.4406 0.4430 0.0624 0.0512 -0.1299 143 LEU A N 761 C CA . LEU A 102 ? 0.4784 0.4370 0.4443 0.0575 0.0430 -0.1281 143 LEU A CA 762 C C . LEU A 102 ? 0.4641 0.4263 0.4451 0.0540 0.0407 -0.1206 143 LEU A C 763 O O . LEU A 102 ? 0.4606 0.4213 0.4434 0.0496 0.0353 -0.1175 143 LEU A O 764 C CB . LEU A 102 ? 0.5071 0.4546 0.4703 0.0587 0.0368 -0.1361 143 LEU A CB 765 C CG . LEU A 102 ? 0.5226 0.4651 0.4683 0.0628 0.0380 -0.1443 143 LEU A CG 766 C CD1 . LEU A 102 ? 0.6126 0.5438 0.5581 0.0646 0.0316 -0.1531 143 LEU A CD1 767 C CD2 . LEU A 102 ? 0.5345 0.4793 0.4659 0.0604 0.0367 -0.1423 143 LEU A CD2 768 N N . PHE A 103 ? 0.4501 0.4174 0.4414 0.0561 0.0450 -0.1177 144 PHE A N 769 C CA . PHE A 103 ? 0.4398 0.4102 0.4439 0.0538 0.0430 -0.1105 144 PHE A CA 770 C C . PHE A 103 ? 0.4244 0.4018 0.4371 0.0572 0.0483 -0.1084 144 PHE A C 771 O O . PHE A 103 ? 0.4426 0.4209 0.4542 0.0615 0.0532 -0.1132 144 PHE A O 772 C CB . PHE A 103 ? 0.4644 0.4259 0.4762 0.0532 0.0375 -0.1115 144 PHE A CB 773 C CG . PHE A 103 ? 0.4756 0.4307 0.4909 0.0580 0.0384 -0.1181 144 PHE A CG 774 C CD1 . PHE A 103 ? 0.5182 0.4746 0.5447 0.0614 0.0405 -0.1162 144 PHE A CD1 775 C CD2 . PHE A 103 ? 0.5561 0.5038 0.5634 0.0598 0.0370 -0.1264 144 PHE A CD2 776 C CE1 . PHE A 103 ? 0.5684 0.5191 0.5987 0.0662 0.0415 -0.1222 144 PHE A CE1 777 C CE2 . PHE A 103 ? 0.5861 0.5277 0.5966 0.0647 0.0380 -0.1329 144 PHE A CE2 778 C CZ . PHE A 103 ? 0.5727 0.5158 0.5951 0.0678 0.0405 -0.1306 144 PHE A CZ 779 N N . GLU A 104 ? 0.3919 0.3745 0.4134 0.0555 0.0473 -0.1015 145 GLU A N 780 C CA . GLU A 104 ? 0.3789 0.3677 0.4112 0.0587 0.0505 -0.0993 145 GLU A CA 781 C C . GLU A 104 ? 0.3919 0.3741 0.4331 0.0621 0.0482 -0.1012 145 GLU A C 782 O O . GLU A 104 ? 0.3912 0.3663 0.4339 0.0604 0.0433 -0.0995 145 GLU A O 783 C CB . GLU A 104 ? 0.3781 0.3731 0.4159 0.0559 0.0485 -0.0917 145 GLU A CB 784 C CG . GLU A 104 ? 0.3314 0.3334 0.3630 0.0525 0.0505 -0.0887 145 GLU A CG 785 C CD . GLU A 104 ? 0.3661 0.3722 0.4028 0.0499 0.0472 -0.0817 145 GLU A CD 786 O OE1 . GLU A 104 ? 0.3727 0.3743 0.4068 0.0472 0.0428 -0.0790 145 GLU A OE1 787 O OE2 . GLU A 104 ? 0.3744 0.3881 0.4185 0.0511 0.0492 -0.0794 145 GLU A OE2 788 N N . PRO A 105 ? 0.3960 0.3806 0.4440 0.0671 0.0519 -0.1043 146 PRO A N 789 C CA . PRO A 105 ? 0.3994 0.3781 0.4569 0.0708 0.0495 -0.1052 146 PRO A CA 790 C C . PRO A 105 ? 0.3916 0.3697 0.4555 0.0692 0.0447 -0.0978 146 PRO A C 791 O O . PRO A 105 ? 0.3991 0.3854 0.4667 0.0686 0.0450 -0.0930 146 PRO A O 792 C CB . PRO A 105 ? 0.4103 0.3954 0.4757 0.0761 0.0547 -0.1080 146 PRO A CB 793 C CG . PRO A 105 ? 0.4265 0.4175 0.4835 0.0755 0.0607 -0.1109 146 PRO A CG 794 C CD . PRO A 105 ? 0.4114 0.4044 0.4597 0.0697 0.0588 -0.1065 146 PRO A CD 795 N N . PRO A 106 ? 0.3952 0.3637 0.4601 0.0685 0.0404 -0.0967 147 PRO A N 796 C CA . PRO A 106 ? 0.3932 0.3613 0.4615 0.0669 0.0368 -0.0890 147 PRO A CA 797 C C . PRO A 106 ? 0.4067 0.3771 0.4845 0.0718 0.0362 -0.0864 147 PRO A C 798 O O . PRO A 106 ? 0.4214 0.3903 0.5050 0.0764 0.0377 -0.0908 147 PRO A O 799 C CB . PRO A 106 ? 0.4124 0.3690 0.4799 0.0649 0.0333 -0.0883 147 PRO A CB 800 C CG . PRO A 106 ? 0.4238 0.3744 0.4900 0.0664 0.0343 -0.0962 147 PRO A CG 801 C CD . PRO A 106 ? 0.4156 0.3736 0.4767 0.0677 0.0386 -0.1014 147 PRO A CD 802 N N . PRO A 107 ? 0.4091 0.3827 0.4884 0.0710 0.0335 -0.0796 148 PRO A N 803 C CA . PRO A 107 ? 0.4158 0.3912 0.5037 0.0761 0.0318 -0.0774 148 PRO A CA 804 C C . PRO A 107 ? 0.4122 0.3768 0.5043 0.0800 0.0293 -0.0766 148 PRO A C 805 O O . PRO A 107 ? 0.4039 0.3589 0.4922 0.0777 0.0283 -0.0757 148 PRO A O 806 C CB . PRO A 107 ? 0.4043 0.3840 0.4900 0.0742 0.0289 -0.0706 148 PRO A CB 807 C CG . PRO A 107 ? 0.4116 0.3879 0.4883 0.0686 0.0285 -0.0681 148 PRO A CG 808 C CD . PRO A 107 ? 0.4173 0.3915 0.4902 0.0662 0.0316 -0.0742 148 PRO A CD 809 N N . PRO A 108 ? 0.4110 0.3768 0.5116 0.0858 0.0281 -0.0766 149 PRO A N 810 C CA . PRO A 108 ? 0.4272 0.3824 0.5321 0.0903 0.0257 -0.0757 149 PRO A CA 811 C C . PRO A 108 ? 0.4211 0.3667 0.5207 0.0885 0.0226 -0.0686 149 PRO A C 812 O O . PRO A 108 ? 0.4184 0.3667 0.5144 0.0877 0.0203 -0.0627 149 PRO A O 813 C CB . PRO A 108 ? 0.4342 0.3948 0.5482 0.0964 0.0237 -0.0752 149 PRO A CB 814 C CG . PRO A 108 ? 0.4243 0.3986 0.5420 0.0955 0.0273 -0.0794 149 PRO A CG 815 C CD . PRO A 108 ? 0.4090 0.3864 0.5169 0.0886 0.0290 -0.0780 149 PRO A CD 816 N N . GLY A 109 ? 0.4401 0.3743 0.5396 0.0881 0.0227 -0.0693 150 GLY A N 817 C CA . GLY A 109 ? 0.4649 0.3891 0.5608 0.0866 0.0209 -0.0622 150 GLY A CA 818 C C . GLY A 109 ? 0.4932 0.4167 0.5828 0.0795 0.0221 -0.0609 150 GLY A C 819 O O . GLY A 109 ? 0.5107 0.4254 0.5988 0.0776 0.0217 -0.0556 150 GLY A O 820 N N . TYR A 110 ? 0.4952 0.4274 0.5816 0.0758 0.0239 -0.0655 151 TYR A N 821 C CA . TYR A 110 ? 0.5210 0.4539 0.6014 0.0692 0.0246 -0.0650 151 TYR A CA 822 C C . TYR A 110 ? 0.5630 0.4951 0.6429 0.0669 0.0259 -0.0731 151 TYR A C 823 O O . TYR A 110 ? 0.5752 0.5102 0.6497 0.0620 0.0262 -0.0745 151 TYR A O 824 C CB . TYR A 110 ? 0.4962 0.4407 0.5716 0.0669 0.0250 -0.0637 151 TYR A CB 825 C CG . TYR A 110 ? 0.4426 0.3898 0.5163 0.0683 0.0232 -0.0565 151 TYR A CG 826 C CD1 . TYR A 110 ? 0.4269 0.3722 0.4952 0.0648 0.0226 -0.0505 151 TYR A CD1 827 C CD2 . TYR A 110 ? 0.3979 0.3502 0.4754 0.0733 0.0219 -0.0561 151 TYR A CD2 828 C CE1 . TYR A 110 ? 0.4033 0.3505 0.4685 0.0667 0.0207 -0.0443 151 TYR A CE1 829 C CE2 . TYR A 110 ? 0.3620 0.3164 0.4372 0.0751 0.0193 -0.0503 151 TYR A CE2 830 C CZ . TYR A 110 ? 0.3776 0.3293 0.4458 0.0718 0.0188 -0.0445 151 TYR A CZ 831 O OH . TYR A 110 ? 0.3469 0.3001 0.4115 0.0741 0.0161 -0.0392 151 TYR A OH 832 N N . GLU A 111 ? 0.5968 0.5253 0.6812 0.0709 0.0266 -0.0789 152 GLU A N 833 C CA . GLU A 111 ? 0.6376 0.5646 0.7201 0.0698 0.0277 -0.0874 152 GLU A CA 834 C C . GLU A 111 ? 0.6591 0.5758 0.7420 0.0658 0.0256 -0.0884 152 GLU A C 835 O O . GLU A 111 ? 0.6776 0.5924 0.7576 0.0642 0.0253 -0.0955 152 GLU A O 836 C CB . GLU A 111 ? 0.6503 0.5763 0.7378 0.0758 0.0293 -0.0938 152 GLU A CB 837 C CG . GLU A 111 ? 0.6561 0.5923 0.7469 0.0802 0.0313 -0.0927 152 GLU A CG 838 C CD . GLU A 111 ? 0.6724 0.6053 0.7708 0.0850 0.0291 -0.0877 152 GLU A CD 839 O OE1 . GLU A 111 ? 0.6732 0.6117 0.7773 0.0898 0.0301 -0.0894 152 GLU A OE1 840 O OE2 . GLU A 111 ? 0.6757 0.6004 0.7745 0.0841 0.0265 -0.0819 152 GLU A OE2 841 N N . ASN A 112 ? 0.6709 0.5811 0.7574 0.0644 0.0241 -0.0813 153 ASN A N 842 C CA . ASN A 112 ? 0.6809 0.5819 0.7702 0.0601 0.0225 -0.0809 153 ASN A CA 843 C C . ASN A 112 ? 0.6757 0.5793 0.7625 0.0548 0.0222 -0.0740 153 ASN A C 844 O O . ASN A 112 ? 0.6836 0.5804 0.7746 0.0509 0.0212 -0.0723 153 ASN A O 845 C CB . ASN A 112 ? 0.7004 0.5891 0.7982 0.0627 0.0218 -0.0788 153 ASN A CB 846 C CG . ASN A 112 ? 0.7162 0.5950 0.8197 0.0588 0.0201 -0.0815 153 ASN A CG 847 O OD1 . ASN A 112 ? 0.7363 0.6132 0.8398 0.0582 0.0186 -0.0905 153 ASN A OD1 848 N ND2 . ASN A 112 ? 0.7366 0.6088 0.8452 0.0561 0.0203 -0.0740 153 ASN A ND2 849 N N . VAL A 113 ? 0.6552 0.5687 0.7359 0.0545 0.0232 -0.0702 154 VAL A N 850 C CA . VAL A 113 ? 0.6319 0.5489 0.7090 0.0497 0.0231 -0.0650 154 VAL A CA 851 C C . VAL A 113 ? 0.6249 0.5443 0.6991 0.0451 0.0218 -0.0712 154 VAL A C 852 O O . VAL A 113 ? 0.6386 0.5627 0.7082 0.0461 0.0220 -0.0779 154 VAL A O 853 C CB . VAL A 113 ? 0.6286 0.5547 0.7002 0.0512 0.0240 -0.0595 154 VAL A CB 854 C CG1 . VAL A 113 ? 0.5977 0.5280 0.6651 0.0464 0.0239 -0.0548 154 VAL A CG1 855 C CG2 . VAL A 113 ? 0.6386 0.5602 0.7128 0.0560 0.0240 -0.0533 154 VAL A CG2 856 N N A SER A 114 ? 0.6040 0.5197 0.6813 0.0405 0.0208 -0.0684 155 SER A N 857 N N B SER A 114 ? 0.6187 0.5345 0.6958 0.0404 0.0206 -0.0695 155 SER A N 858 C CA A SER A 114 ? 0.5805 0.4979 0.6561 0.0360 0.0186 -0.0731 155 SER A CA 859 C CA B SER A 114 ? 0.6110 0.5266 0.6869 0.0370 0.0180 -0.0770 155 SER A CA 860 C C A SER A 114 ? 0.5482 0.4751 0.6166 0.0333 0.0190 -0.0698 155 SER A C 861 C C B SER A 114 ? 0.5892 0.5140 0.6566 0.0339 0.0173 -0.0779 155 SER A C 862 O O A SER A 114 ? 0.5264 0.4573 0.5928 0.0341 0.0208 -0.0627 155 SER A O 863 O O B SER A 114 ? 0.6012 0.5286 0.6623 0.0342 0.0163 -0.0850 155 SER A O 864 C CB A SER A 114 ? 0.5920 0.5007 0.6773 0.0322 0.0169 -0.0721 155 SER A CB 865 C CB B SER A 114 ? 0.6201 0.5260 0.7058 0.0337 0.0159 -0.0774 155 SER A CB 866 O OG A SER A 114 ? 0.6044 0.5137 0.6892 0.0285 0.0135 -0.0786 155 SER A OG 867 O OG B SER A 114 ? 0.6473 0.5508 0.7326 0.0324 0.0124 -0.0868 155 SER A OG 868 N N A ASP A 115 ? 0.5210 0.4509 0.5851 0.0305 0.0168 -0.0752 156 ASP A N 869 N N B ASP A 115 ? 0.5516 0.4805 0.6184 0.0313 0.0181 -0.0707 156 ASP A N 870 C CA A ASP A 115 ? 0.4933 0.4309 0.5517 0.0274 0.0165 -0.0724 156 ASP A CA 871 C CA B ASP A 115 ? 0.5111 0.4477 0.5713 0.0281 0.0172 -0.0705 156 ASP A CA 872 C C A ASP A 115 ? 0.4608 0.4072 0.5113 0.0297 0.0190 -0.0702 156 ASP A C 873 C C B ASP A 115 ? 0.4722 0.4181 0.5236 0.0301 0.0193 -0.0693 156 ASP A C 874 O O A ASP A 115 ? 0.4495 0.4016 0.4969 0.0279 0.0195 -0.0652 156 ASP A O 875 O O B ASP A 115 ? 0.4588 0.4103 0.5072 0.0284 0.0198 -0.0641 156 ASP A O 876 C CB A ASP A 115 ? 0.5019 0.4380 0.5664 0.0243 0.0169 -0.0648 156 ASP A CB 877 C CB B ASP A 115 ? 0.5160 0.4525 0.5805 0.0244 0.0173 -0.0634 156 ASP A CB 878 C CG A ASP A 115 ? 0.5319 0.4614 0.6054 0.0205 0.0142 -0.0670 156 ASP A CG 879 C CG B ASP A 115 ? 0.5343 0.4628 0.6092 0.0212 0.0154 -0.0645 156 ASP A CG 880 O OD1 A ASP A 115 ? 0.5774 0.5007 0.6549 0.0211 0.0120 -0.0735 156 ASP A OD1 881 O OD1 B ASP A 115 ? 0.5629 0.4904 0.6386 0.0188 0.0118 -0.0711 156 ASP A OD1 882 O OD2 A ASP A 115 ? 0.5556 0.4864 0.6331 0.0170 0.0143 -0.0622 156 ASP A OD2 883 O OD2 B ASP A 115 ? 0.5513 0.4743 0.6338 0.0212 0.0175 -0.0585 156 ASP A OD2 884 N N . ILE A 116 ? 0.4474 0.3950 0.4956 0.0337 0.0205 -0.0741 157 ILE A N 885 C CA . ILE A 116 ? 0.3966 0.3533 0.4383 0.0353 0.0228 -0.0736 157 ILE A CA 886 C C . ILE A 116 ? 0.3890 0.3491 0.4224 0.0332 0.0221 -0.0786 157 ILE A C 887 O O . ILE A 116 ? 0.3860 0.3424 0.4168 0.0343 0.0214 -0.0856 157 ILE A O 888 C CB . ILE A 116 ? 0.3848 0.3422 0.4285 0.0404 0.0251 -0.0762 157 ILE A CB 889 C CG1 . ILE A 116 ? 0.3554 0.3093 0.4061 0.0429 0.0251 -0.0706 157 ILE A CG1 890 C CG2 . ILE A 116 ? 0.3527 0.3198 0.3912 0.0415 0.0278 -0.0766 157 ILE A CG2 891 C CD1 . ILE A 116 ? 0.3396 0.2925 0.3948 0.0486 0.0266 -0.0733 157 ILE A CD1 892 N N . VAL A 117 ? 0.3724 0.3388 0.4009 0.0305 0.0219 -0.0751 158 VAL A N 893 C CA . VAL A 117 ? 0.3664 0.3356 0.3860 0.0287 0.0211 -0.0789 158 VAL A CA 894 C C . VAL A 117 ? 0.3676 0.3409 0.3815 0.0321 0.0249 -0.0824 158 VAL A C 895 O O . VAL A 117 ? 0.3521 0.3309 0.3679 0.0337 0.0278 -0.0791 158 VAL A O 896 C CB . VAL A 117 ? 0.3604 0.3352 0.3766 0.0251 0.0202 -0.0736 158 VAL A CB 897 C CG1 . VAL A 117 ? 0.3508 0.3338 0.3647 0.0262 0.0235 -0.0690 158 VAL A CG1 898 C CG2 . VAL A 117 ? 0.3778 0.3522 0.3859 0.0231 0.0176 -0.0778 158 VAL A CG2 899 N N . PRO A 118 ? 0.3663 0.3368 0.3732 0.0333 0.0248 -0.0893 159 PRO A N 900 C CA . PRO A 118 ? 0.3865 0.3611 0.3880 0.0367 0.0296 -0.0923 159 PRO A CA 901 C C . PRO A 118 ? 0.3615 0.3441 0.3567 0.0352 0.0322 -0.0884 159 PRO A C 902 O O . PRO A 118 ? 0.3646 0.3485 0.3570 0.0316 0.0294 -0.0851 159 PRO A O 903 C CB . PRO A 118 ? 0.4045 0.3730 0.3977 0.0384 0.0284 -0.1006 159 PRO A CB 904 C CG . PRO A 118 ? 0.4176 0.3813 0.4095 0.0348 0.0223 -0.1014 159 PRO A CG 905 C CD . PRO A 118 ? 0.3960 0.3596 0.3999 0.0319 0.0203 -0.0949 159 PRO A CD 906 N N . PRO A 119 ? 0.3564 0.3445 0.3507 0.0378 0.0376 -0.0887 160 PRO A N 907 C CA . PRO A 119 ? 0.3440 0.3393 0.3332 0.0361 0.0403 -0.0849 160 PRO A CA 908 C C . PRO A 119 ? 0.3432 0.3365 0.3192 0.0342 0.0387 -0.0866 160 PRO A C 909 O O . PRO A 119 ? 0.3468 0.3349 0.3143 0.0361 0.0384 -0.0925 160 PRO A O 910 C CB . PRO A 119 ? 0.3461 0.3461 0.3367 0.0398 0.0469 -0.0866 160 PRO A CB 911 C CG . PRO A 119 ? 0.3578 0.3554 0.3591 0.0429 0.0466 -0.0884 160 PRO A CG 912 C CD . PRO A 119 ? 0.3565 0.3448 0.3556 0.0424 0.0416 -0.0921 160 PRO A CD 913 N N . PHE A 120 ? 0.3204 0.3173 0.2946 0.0308 0.0372 -0.0815 161 PHE A N 914 C CA . PHE A 120 ? 0.3245 0.3202 0.2866 0.0291 0.0355 -0.0821 161 PHE A CA 915 C C . PHE A 120 ? 0.3249 0.3269 0.2873 0.0263 0.0365 -0.0755 161 PHE A C 916 O O . PHE A 120 ? 0.3012 0.3072 0.2737 0.0254 0.0368 -0.0711 161 PHE A O 917 C CB . PHE A 120 ? 0.3291 0.3183 0.2899 0.0272 0.0285 -0.0847 161 PHE A CB 918 C CG . PHE A 120 ? 0.3280 0.3185 0.2978 0.0236 0.0244 -0.0794 161 PHE A CG 919 C CD1 . PHE A 120 ? 0.3263 0.3170 0.2919 0.0205 0.0205 -0.0774 161 PHE A CD1 920 C CD2 . PHE A 120 ? 0.3451 0.3358 0.3267 0.0237 0.0246 -0.0767 161 PHE A CD2 921 C CE1 . PHE A 120 ? 0.3416 0.3333 0.3155 0.0176 0.0175 -0.0727 161 PHE A CE1 922 C CE2 . PHE A 120 ? 0.3348 0.3260 0.3233 0.0209 0.0218 -0.0716 161 PHE A CE2 923 C CZ . PHE A 120 ? 0.3192 0.3111 0.3039 0.0177 0.0184 -0.0697 161 PHE A CZ 924 N N . SER A 121 ? 0.3378 0.3397 0.2887 0.0253 0.0365 -0.0751 162 SER A N 925 C CA . SER A 121 ? 0.3259 0.3326 0.2762 0.0225 0.0367 -0.0691 162 SER A CA 926 C C . SER A 121 ? 0.3165 0.3204 0.2653 0.0197 0.0298 -0.0682 162 SER A C 927 O O . SER A 121 ? 0.3409 0.3404 0.2802 0.0199 0.0267 -0.0714 162 SER A O 928 C CB . SER A 121 ? 0.3494 0.3576 0.2882 0.0235 0.0418 -0.0686 162 SER A CB 929 O OG . SER A 121 ? 0.3331 0.3449 0.2761 0.0260 0.0488 -0.0692 162 SER A OG 930 N N . ALA A 122 ? 0.3146 0.3206 0.2731 0.0174 0.0274 -0.0641 163 ALA A N 931 C CA . ALA A 122 ? 0.3136 0.3172 0.2727 0.0149 0.0214 -0.0633 163 ALA A CA 932 C C . ALA A 122 ? 0.3295 0.3340 0.2790 0.0135 0.0201 -0.0615 163 ALA A C 933 O O . ALA A 122 ? 0.3071 0.3158 0.2548 0.0130 0.0232 -0.0575 163 ALA A O 934 C CB . ALA A 122 ? 0.2964 0.3023 0.2666 0.0133 0.0204 -0.0585 163 ALA A CB 935 N N . PHE A 123 ? 0.3311 0.3313 0.2758 0.0129 0.0148 -0.0646 164 PHE A N 936 C CA . PHE A 123 ? 0.3365 0.3359 0.2719 0.0119 0.0113 -0.0639 164 PHE A CA 937 C C . PHE A 123 ? 0.3622 0.3590 0.2823 0.0146 0.0135 -0.0669 164 PHE A C 938 O O . PHE A 123 ? 0.3851 0.3807 0.2953 0.0144 0.0113 -0.0659 164 PHE A O 939 C CB . PHE A 123 ? 0.3226 0.3265 0.2610 0.0096 0.0114 -0.0576 164 PHE A CB 940 C CG . PHE A 123 ? 0.3061 0.3116 0.2575 0.0075 0.0090 -0.0549 164 PHE A CG 941 C CD1 . PHE A 123 ? 0.3131 0.3165 0.2682 0.0059 0.0033 -0.0560 164 PHE A CD1 942 C CD2 . PHE A 123 ? 0.2897 0.2987 0.2495 0.0074 0.0124 -0.0514 164 PHE A CD2 943 C CE1 . PHE A 123 ? 0.3204 0.3253 0.2871 0.0042 0.0023 -0.0528 164 PHE A CE1 944 C CE2 . PHE A 123 ? 0.2962 0.3059 0.2657 0.0061 0.0108 -0.0485 164 PHE A CE2 945 C CZ . PHE A 123 ? 0.2887 0.2964 0.2617 0.0045 0.0063 -0.0490 164 PHE A CZ 946 N N . SER A 124 ? 0.3586 0.3542 0.2762 0.0173 0.0181 -0.0702 165 SER A N 947 C CA . SER A 124 ? 0.3866 0.3782 0.2879 0.0205 0.0199 -0.0739 165 SER A CA 948 C C . SER A 124 ? 0.4082 0.3935 0.3015 0.0210 0.0117 -0.0789 165 SER A C 949 O O . SER A 124 ? 0.4131 0.3959 0.3148 0.0201 0.0061 -0.0825 165 SER A O 950 C CB . SER A 124 ? 0.3949 0.3851 0.2951 0.0239 0.0253 -0.0781 165 SER A CB 951 O OG . SER A 124 ? 0.4324 0.4179 0.3150 0.0275 0.0270 -0.0819 165 SER A OG 952 N N . PRO A 125 ? 0.4392 0.4216 0.3162 0.0227 0.0108 -0.0791 166 PRO A N 953 C CA . PRO A 125 ? 0.4653 0.4410 0.3330 0.0244 0.0028 -0.0853 166 PRO A CA 954 C C . PRO A 125 ? 0.4872 0.4573 0.3483 0.0283 0.0037 -0.0928 166 PRO A C 955 O O . PRO A 125 ? 0.4833 0.4549 0.3441 0.0302 0.0117 -0.0927 166 PRO A O 956 C CB . PRO A 125 ? 0.4842 0.4579 0.3343 0.0260 0.0028 -0.0828 166 PRO A CB 957 C CG . PRO A 125 ? 0.4655 0.4430 0.3120 0.0268 0.0135 -0.0777 166 PRO A CG 958 C CD . PRO A 125 ? 0.4431 0.4276 0.3097 0.0234 0.0168 -0.0740 166 PRO A CD 959 N N . GLN A 126 ? 0.5024 0.4662 0.3593 0.0296 -0.0048 -0.0996 167 GLN A N 960 C CA . GLN A 126 ? 0.5322 0.4891 0.3795 0.0340 -0.0056 -0.1079 167 GLN A CA 961 C C . GLN A 126 ? 0.5555 0.5080 0.3787 0.0389 -0.0021 -0.1092 167 GLN A C 962 O O . GLN A 126 ? 0.5667 0.5194 0.3790 0.0390 -0.0028 -0.1051 167 GLN A O 963 C CB . GLN A 126 ? 0.5393 0.4905 0.3910 0.0335 -0.0169 -0.1151 167 GLN A CB 964 C CG . GLN A 126 ? 0.5625 0.5174 0.4385 0.0284 -0.0200 -0.1131 167 GLN A CG 965 C CD . GLN A 126 ? 0.6377 0.5873 0.5204 0.0276 -0.0308 -0.1201 167 GLN A CD 966 O OE1 . GLN A 126 ? 0.6716 0.6148 0.5408 0.0308 -0.0372 -0.1267 167 GLN A OE1 967 N NE2 . GLN A 126 ? 0.6116 0.5636 0.5153 0.0235 -0.0329 -0.1186 167 GLN A NE2 968 N N . GLY A 127 ? 0.5684 0.5170 0.3835 0.0433 0.0027 -0.1143 168 GLY A N 969 C CA . GLY A 127 ? 0.5905 0.5333 0.3810 0.0491 0.0062 -0.1170 168 GLY A CA 970 C C . GLY A 127 ? 0.6046 0.5452 0.3910 0.0534 0.0138 -0.1215 168 GLY A C 971 O O . GLY A 127 ? 0.5838 0.5285 0.3872 0.0518 0.0174 -0.1216 168 GLY A O 972 N N . MET A 128 ? 0.6338 0.5676 0.3967 0.0595 0.0162 -0.1255 169 MET A N 973 C CA . MET A 128 ? 0.6546 0.5856 0.4100 0.0648 0.0245 -0.1300 169 MET A CA 974 C C . MET A 128 ? 0.6614 0.5913 0.3958 0.0693 0.0350 -0.1262 169 MET A C 975 O O . MET A 128 ? 0.6873 0.6095 0.4014 0.0759 0.0374 -0.1321 169 MET A O 976 C CB . MET A 128 ? 0.6839 0.6052 0.4317 0.0689 0.0161 -0.1415 169 MET A CB 977 C CG . MET A 128 ? 0.7298 0.6522 0.5012 0.0649 0.0089 -0.1452 169 MET A CG 978 S SD . MET A 128 ? 0.9056 0.8158 0.6687 0.0696 -0.0014 -0.1592 169 MET A SD 979 C CE . MET A 128 ? 0.8638 0.7772 0.6560 0.0658 -0.0015 -0.1607 169 MET A CE 980 N N . PRO A 129 ? 0.6560 0.5932 0.3949 0.0659 0.0417 -0.1162 170 PRO A N 981 C CA . PRO A 129 ? 0.6773 0.6139 0.3986 0.0693 0.0526 -0.1111 170 PRO A CA 982 C C . PRO A 129 ? 0.7080 0.6449 0.4265 0.0741 0.0645 -0.1137 170 PRO A C 983 O O . PRO A 129 ? 0.6807 0.6236 0.4192 0.0722 0.0678 -0.1145 170 PRO A O 984 C CB . PRO A 129 ? 0.6608 0.6069 0.3972 0.0633 0.0572 -0.1005 170 PRO A CB 985 C CG . PRO A 129 ? 0.6159 0.5690 0.3796 0.0579 0.0528 -0.1007 170 PRO A CG 986 C CD . PRO A 129 ? 0.6174 0.5640 0.3800 0.0587 0.0405 -0.1093 170 PRO A CD 987 N N . GLU A 130 ? 0.7500 0.6799 0.4433 0.0806 0.0706 -0.1153 171 GLU A N 988 C CA . GLU A 130 ? 0.7898 0.7209 0.4796 0.0854 0.0843 -0.1162 171 GLU A CA 989 C C . GLU A 130 ? 0.8062 0.7379 0.4816 0.0874 0.0967 -0.1079 171 GLU A C 990 O O . GLU A 130 ? 0.8357 0.7611 0.4908 0.0889 0.0936 -0.1053 171 GLU A O 991 C CB . GLU A 130 ? 0.8158 0.7371 0.4897 0.0927 0.0822 -0.1274 171 GLU A CB 992 C CG . GLU A 130 ? 0.8831 0.7921 0.5287 0.0978 0.0733 -0.1330 171 GLU A CG 993 C CD . GLU A 130 ? 0.9721 0.8715 0.5994 0.1064 0.0747 -0.1436 171 GLU A CD 994 O OE1 . GLU A 130 ? 1.0015 0.8963 0.6337 0.1069 0.0638 -0.1530 171 GLU A OE1 995 O OE2 . GLU A 130 ? 1.0006 0.8970 0.6090 0.1126 0.0869 -0.1424 171 GLU A OE2 996 N N . GLY A 131 ? 0.7958 0.7352 0.4830 0.0872 0.1105 -0.1034 172 GLY A N 997 C CA . GLY A 131 ? 0.8002 0.7411 0.4775 0.0885 0.1238 -0.0949 172 GLY A CA 998 C C . GLY A 131 ? 0.7820 0.7326 0.4778 0.0879 0.1383 -0.0912 172 GLY A C 999 O O . GLY A 131 ? 0.7780 0.7324 0.4889 0.0886 0.1390 -0.0966 172 GLY A O 1000 N N . ASP A 132 ? 0.7726 0.7273 0.4683 0.0866 0.1496 -0.0818 173 ASP A N 1001 C CA . ASP A 132 ? 0.7525 0.7165 0.4654 0.0863 0.1646 -0.0777 173 ASP A CA 1002 C C . ASP A 132 ? 0.7033 0.6792 0.4470 0.0780 0.1627 -0.0714 173 ASP A C 1003 O O . ASP A 132 ? 0.6833 0.6593 0.4287 0.0730 0.1553 -0.0666 173 ASP A O 1004 C CB . ASP A 132 ? 0.7772 0.7382 0.4720 0.0901 0.1793 -0.0709 173 ASP A CB 1005 C CG . ASP A 132 ? 0.8279 0.7764 0.4892 0.0994 0.1821 -0.0769 173 ASP A CG 1006 O OD1 . ASP A 132 ? 0.8541 0.7995 0.5129 0.1038 0.1790 -0.0866 173 ASP A OD1 1007 O OD2 . ASP A 132 ? 0.8655 0.8066 0.5024 0.1025 0.1872 -0.0719 173 ASP A OD2 1008 N N . LEU A 133 ? 0.6683 0.6536 0.4358 0.0770 0.1694 -0.0717 174 LEU A N 1009 C CA . LEU A 133 ? 0.6263 0.6228 0.4236 0.0697 0.1669 -0.0668 174 LEU A CA 1010 C C . LEU A 133 ? 0.6191 0.6219 0.4250 0.0665 0.1779 -0.0567 174 LEU A C 1011 O O . LEU A 133 ? 0.6374 0.6401 0.4363 0.0702 0.1920 -0.0540 174 LEU A O 1012 C CB . LEU A 133 ? 0.6181 0.6217 0.4376 0.0705 0.1684 -0.0719 174 LEU A CB 1013 C CG A LEU A 133 ? 0.5927 0.6024 0.4367 0.0658 0.1579 -0.0738 174 LEU A CG 1014 C CG B LEU A 133 ? 0.5884 0.5877 0.4084 0.0722 0.1571 -0.0812 174 LEU A CG 1015 C CD1 A LEU A 133 ? 0.5860 0.5899 0.4233 0.0628 0.1425 -0.0758 174 LEU A CD1 1016 C CD1 B LEU A 133 ? 0.5679 0.5749 0.4110 0.0733 0.1611 -0.0845 174 LEU A CD1 1017 C CD2 A LEU A 133 ? 0.5855 0.5969 0.4392 0.0699 0.1596 -0.0812 174 LEU A CD2 1018 C CD2 B LEU A 133 ? 0.5363 0.5343 0.3609 0.0668 0.1418 -0.0809 174 LEU A CD2 1019 N N . VAL A 134 ? 0.5966 0.6046 0.4179 0.0597 0.1718 -0.0512 175 VAL A N 1020 C CA . VAL A 134 ? 0.5851 0.6016 0.4242 0.0554 0.1806 -0.0426 175 VAL A CA 1021 C C . VAL A 134 ? 0.5627 0.5894 0.4325 0.0503 0.1741 -0.0431 175 VAL A C 1022 O O . VAL A 134 ? 0.5511 0.5767 0.4241 0.0475 0.1609 -0.0457 175 VAL A O 1023 C CB . VAL A 134 ? 0.5982 0.6102 0.4254 0.0523 0.1794 -0.0349 175 VAL A CB 1024 C CG1 . VAL A 134 ? 0.5806 0.6015 0.4298 0.0469 0.1865 -0.0263 175 VAL A CG1 1025 C CG2 . VAL A 134 ? 0.6117 0.6133 0.4077 0.0581 0.1863 -0.0338 175 VAL A CG2 1026 N N . TYR A 135 ? 0.5397 0.5760 0.4318 0.0493 0.1834 -0.0407 176 TYR A N 1027 C CA . TYR A 135 ? 0.5186 0.5644 0.4394 0.0451 0.1776 -0.0411 176 TYR A CA 1028 C C . TYR A 135 ? 0.5081 0.5585 0.4414 0.0389 0.1770 -0.0331 176 TYR A C 1029 O O . TYR A 135 ? 0.5099 0.5623 0.4446 0.0382 0.1884 -0.0270 176 TYR A O 1030 C CB . TYR A 135 ? 0.5072 0.5611 0.4467 0.0480 0.1865 -0.0440 176 TYR A CB 1031 C CG . TYR A 135 ? 0.4965 0.5611 0.4670 0.0438 0.1828 -0.0427 176 TYR A CG 1032 C CD1 . TYR A 135 ? 0.4480 0.5134 0.4273 0.0422 0.1696 -0.0466 176 TYR A CD1 1033 C CD2 . TYR A 135 ? 0.4979 0.5717 0.4891 0.0417 0.1925 -0.0376 176 TYR A CD2 1034 C CE1 . TYR A 135 ? 0.4705 0.5451 0.4769 0.0389 0.1654 -0.0455 176 TYR A CE1 1035 C CE2 . TYR A 135 ? 0.4739 0.5574 0.4937 0.0381 0.1879 -0.0370 176 TYR A CE2 1036 C CZ . TYR A 135 ? 0.4328 0.5163 0.4589 0.0370 0.1741 -0.0411 176 TYR A CZ 1037 O OH . TYR A 135 ? 0.4425 0.5348 0.4951 0.0342 0.1693 -0.0406 176 TYR A OH 1038 N N . VAL A 136 ? 0.4816 0.5331 0.4232 0.0346 0.1643 -0.0332 177 VAL A N 1039 C CA . VAL A 136 ? 0.4802 0.5334 0.4286 0.0291 0.1612 -0.0265 177 VAL A CA 1040 C C . VAL A 136 ? 0.4545 0.5173 0.4316 0.0250 0.1568 -0.0258 177 VAL A C 1041 O O . VAL A 136 ? 0.4490 0.5126 0.4324 0.0206 0.1500 -0.0223 177 VAL A O 1042 C CB . VAL A 136 ? 0.4758 0.5207 0.4057 0.0278 0.1501 -0.0265 177 VAL A CB 1043 C CG1 . VAL A 136 ? 0.5099 0.5450 0.4110 0.0319 0.1541 -0.0268 177 VAL A CG1 1044 C CG2 . VAL A 136 ? 0.4881 0.5322 0.4212 0.0280 0.1378 -0.0328 177 VAL A CG2 1045 N N . ASN A 137 ? 0.4544 0.5242 0.4489 0.0270 0.1607 -0.0291 178 ASN A N 1046 C CA . ASN A 137 ? 0.4462 0.5250 0.4678 0.0241 0.1558 -0.0293 178 ASN A CA 1047 C C . ASN A 137 ? 0.4318 0.5075 0.4512 0.0224 0.1409 -0.0317 178 ASN A C 1048 O O . ASN A 137 ? 0.4320 0.5024 0.4391 0.0252 0.1357 -0.0366 178 ASN A O 1049 C CB . ASN A 137 ? 0.4540 0.5389 0.4923 0.0198 0.1616 -0.0227 178 ASN A CB 1050 C CG . ASN A 137 ? 0.4477 0.5432 0.5167 0.0182 0.1598 -0.0238 178 ASN A CG 1051 O OD1 . ASN A 137 ? 0.4237 0.5230 0.5022 0.0213 0.1583 -0.0289 178 ASN A OD1 1052 N ND2 . ASN A 137 ? 0.4421 0.5423 0.5273 0.0135 0.1594 -0.0190 178 ASN A ND2 1053 N N . TYR A 138 ? 0.4159 0.4944 0.4466 0.0179 0.1345 -0.0283 179 TYR A N 1054 C CA . TYR A 138 ? 0.3990 0.4750 0.4285 0.0164 0.1214 -0.0301 179 TYR A CA 1055 C C . TYR A 138 ? 0.4003 0.4679 0.4089 0.0150 0.1164 -0.0281 179 TYR A C 1056 O O . TYR A 138 ? 0.3859 0.4512 0.3930 0.0134 0.1061 -0.0289 179 TYR A O 1057 C CB . TYR A 138 ? 0.3922 0.4748 0.4434 0.0130 0.1161 -0.0281 179 TYR A CB 1058 C CG . TYR A 138 ? 0.3860 0.4768 0.4595 0.0146 0.1172 -0.0310 179 TYR A CG 1059 C CD1 . TYR A 138 ? 0.3761 0.4667 0.4523 0.0176 0.1104 -0.0360 179 TYR A CD1 1060 C CD2 . TYR A 138 ? 0.3956 0.4943 0.4886 0.0133 0.1248 -0.0285 179 TYR A CD2 1061 C CE1 . TYR A 138 ? 0.3926 0.4908 0.4897 0.0196 0.1110 -0.0387 179 TYR A CE1 1062 C CE2 . TYR A 138 ? 0.4224 0.5293 0.5376 0.0150 0.1252 -0.0315 179 TYR A CE2 1063 C CZ . TYR A 138 ? 0.3996 0.5062 0.5164 0.0183 0.1179 -0.0366 179 TYR A CZ 1064 O OH . TYR A 138 ? 0.4018 0.5163 0.5407 0.0204 0.1178 -0.0394 179 TYR A OH 1065 N N . ALA A 139 ? 0.4117 0.4745 0.4038 0.0158 0.1236 -0.0256 180 ALA A N 1066 C CA . ALA A 139 ? 0.4283 0.4832 0.4007 0.0147 0.1192 -0.0233 180 ALA A CA 1067 C C . ALA A 139 ? 0.4234 0.4795 0.4035 0.0100 0.1130 -0.0188 180 ALA A C 1068 O O . ALA A 139 ? 0.4090 0.4596 0.3777 0.0089 0.1050 -0.0184 180 ALA A O 1069 C CB . ALA A 139 ? 0.4377 0.4862 0.3953 0.0172 0.1110 -0.0289 180 ALA A CB 1070 N N . ARG A 140 ? 0.4124 0.4754 0.4124 0.0074 0.1164 -0.0158 181 ARG A N 1071 C CA . ARG A 140 ? 0.4060 0.4699 0.4143 0.0031 0.1112 -0.0117 181 ARG A CA 1072 C C . ARG A 140 ? 0.4110 0.4698 0.4071 0.0015 0.1164 -0.0057 181 ARG A C 1073 O O . ARG A 140 ? 0.4125 0.4683 0.3967 0.0036 0.1256 -0.0040 181 ARG A O 1074 C CB . ARG A 140 ? 0.3917 0.4645 0.4263 0.0010 0.1128 -0.0111 181 ARG A CB 1075 C CG . ARG A 140 ? 0.4021 0.4794 0.4495 0.0025 0.1055 -0.0164 181 ARG A CG 1076 C CD . ARG A 140 ? 0.4110 0.4973 0.4841 0.0015 0.1081 -0.0164 181 ARG A CD 1077 N NE . ARG A 140 ? 0.4048 0.4948 0.4833 0.0025 0.1207 -0.0151 181 ARG A NE 1078 C CZ . ARG A 140 ? 0.4485 0.5469 0.5501 0.0018 0.1258 -0.0148 181 ARG A CZ 1079 N NH1 . ARG A 140 ? 0.4343 0.5383 0.5562 0.0002 0.1182 -0.0162 181 ARG A NH1 1080 N NH2 . ARG A 140 ? 0.4493 0.5506 0.5541 0.0030 0.1384 -0.0133 181 ARG A NH2 1081 N N . THR A 141 ? 0.4070 0.4642 0.4050 -0.0018 0.1105 -0.0024 182 THR A N 1082 C CA . THR A 141 ? 0.4126 0.4647 0.4007 -0.0035 0.1151 0.0038 182 THR A CA 1083 C C . THR A 141 ? 0.4261 0.4816 0.4233 -0.0041 0.1281 0.0080 182 THR A C 1084 O O . THR A 141 ? 0.4484 0.4988 0.4302 -0.0024 0.1367 0.0116 182 THR A O 1085 C CB . THR A 141 ? 0.4057 0.4569 0.4002 -0.0072 0.1071 0.0066 182 THR A CB 1086 O OG1 . THR A 141 ? 0.4134 0.4608 0.3970 -0.0061 0.0965 0.0032 182 THR A OG1 1087 C CG2 . THR A 141 ? 0.4183 0.4643 0.4050 -0.0090 0.1122 0.0135 182 THR A CG2 1088 N N . GLU A 142 ? 0.4200 0.4840 0.4421 -0.0060 0.1298 0.0074 183 GLU A N 1089 C CA . GLU A 142 ? 0.4405 0.5090 0.4756 -0.0070 0.1424 0.0114 183 GLU A CA 1090 C C . GLU A 142 ? 0.4482 0.5169 0.4745 -0.0027 0.1530 0.0098 183 GLU A C 1091 O O . GLU A 142 ? 0.4608 0.5295 0.4870 -0.0026 0.1654 0.0145 183 GLU A O 1092 C CB . GLU A 142 ? 0.4364 0.5144 0.5022 -0.0100 0.1409 0.0104 183 GLU A CB 1093 C CG . GLU A 142 ? 0.4536 0.5377 0.5303 -0.0076 0.1350 0.0033 183 GLU A CG 1094 C CD . GLU A 142 ? 0.4857 0.5693 0.5650 -0.0086 0.1204 -0.0001 183 GLU A CD 1095 O OE1 . GLU A 142 ? 0.4719 0.5485 0.5350 -0.0092 0.1139 0.0011 183 GLU A OE1 1096 O OE2 . GLU A 142 ? 0.4720 0.5621 0.5698 -0.0084 0.1156 -0.0039 183 GLU A OE2 1097 N N . ASP A 143 ? 0.4469 0.5155 0.4658 0.0009 0.1484 0.0033 184 ASP A N 1098 C CA . ASP A 143 ? 0.4584 0.5263 0.4674 0.0057 0.1577 0.0008 184 ASP A CA 1099 C C . ASP A 143 ? 0.4733 0.5313 0.4533 0.0083 0.1628 0.0037 184 ASP A C 1100 O O . ASP A 143 ? 0.4977 0.5543 0.4700 0.0111 0.1750 0.0057 184 ASP A O 1101 C CB . ASP A 143 ? 0.4505 0.5197 0.4590 0.0089 0.1504 -0.0071 184 ASP A CB 1102 C CG . ASP A 143 ? 0.4279 0.5066 0.4637 0.0076 0.1464 -0.0101 184 ASP A CG 1103 O OD1 . ASP A 143 ? 0.4293 0.5156 0.4857 0.0062 0.1541 -0.0079 184 ASP A OD1 1104 O OD2 . ASP A 143 ? 0.4015 0.4801 0.4385 0.0081 0.1357 -0.0146 184 ASP A OD2 1105 N N . PHE A 144 ? 0.4779 0.5287 0.4416 0.0077 0.1532 0.0039 185 PHE A N 1106 C CA . PHE A 144 ? 0.4871 0.5277 0.4227 0.0102 0.1560 0.0067 185 PHE A CA 1107 C C . PHE A 144 ? 0.5099 0.5481 0.4441 0.0081 0.1650 0.0154 185 PHE A C 1108 O O . PHE A 144 ? 0.5195 0.5513 0.4343 0.0114 0.1740 0.0185 185 PHE A O 1109 C CB . PHE A 144 ? 0.4821 0.5164 0.4026 0.0104 0.1425 0.0040 185 PHE A CB 1110 C CG . PHE A 144 ? 0.4617 0.4944 0.3736 0.0141 0.1366 -0.0040 185 PHE A CG 1111 C CD1 . PHE A 144 ? 0.4607 0.4979 0.3863 0.0127 0.1269 -0.0088 185 PHE A CD1 1112 C CD2 . PHE A 144 ? 0.4906 0.5170 0.3807 0.0193 0.1412 -0.0067 185 PHE A CD2 1113 C CE1 . PHE A 144 ? 0.4676 0.5029 0.3863 0.0158 0.1216 -0.0159 185 PHE A CE1 1114 C CE2 . PHE A 144 ? 0.4803 0.5048 0.3636 0.0226 0.1354 -0.0145 185 PHE A CE2 1115 C CZ . PHE A 144 ? 0.4570 0.4862 0.3557 0.0206 0.1255 -0.0189 185 PHE A CZ 1116 N N . PHE A 145 ? 0.4973 0.5398 0.4514 0.0029 0.1628 0.0194 186 PHE A N 1117 C CA . PHE A 145 ? 0.5202 0.5617 0.4792 0.0003 0.1732 0.0280 186 PHE A CA 1118 C C . PHE A 145 ? 0.5413 0.5867 0.5061 0.0023 0.1891 0.0301 186 PHE A C 1119 O O . PHE A 145 ? 0.5586 0.5981 0.5096 0.0038 0.1999 0.0362 186 PHE A O 1120 C CB . PHE A 145 ? 0.5057 0.5529 0.4909 -0.0057 0.1692 0.0309 186 PHE A CB 1121 C CG . PHE A 145 ? 0.5048 0.5470 0.4841 -0.0081 0.1565 0.0315 186 PHE A CG 1122 C CD1 . PHE A 145 ? 0.5298 0.5622 0.4820 -0.0056 0.1521 0.0324 186 PHE A CD1 1123 C CD2 . PHE A 145 ? 0.4944 0.5417 0.4961 -0.0126 0.1490 0.0313 186 PHE A CD2 1124 C CE1 . PHE A 145 ? 0.5367 0.5650 0.4849 -0.0076 0.1407 0.0330 186 PHE A CE1 1125 C CE2 . PHE A 145 ? 0.4592 0.5019 0.4558 -0.0144 0.1377 0.0317 186 PHE A CE2 1126 C CZ . PHE A 145 ? 0.4840 0.5175 0.4545 -0.0121 0.1339 0.0327 186 PHE A CZ 1127 N N . LYS A 146 ? 0.5385 0.5935 0.5243 0.0025 0.1905 0.0252 187 LYS A N 1128 C CA . LYS A 146 ? 0.5584 0.6187 0.5535 0.0045 0.2057 0.0264 187 LYS A CA 1129 C C . LYS A 146 ? 0.5879 0.6407 0.5543 0.0109 0.2140 0.0256 187 LYS A C 1130 O O . LYS A 146 ? 0.5883 0.6387 0.5481 0.0126 0.2284 0.0313 187 LYS A O 1131 C CB . LYS A 146 ? 0.5447 0.6163 0.5663 0.0043 0.2034 0.0201 187 LYS A CB 1132 C CG . LYS A 146 ? 0.5869 0.6648 0.6189 0.0072 0.2184 0.0199 187 LYS A CG 1133 C CD . LYS A 146 ? 0.6413 0.7226 0.6889 0.0041 0.2324 0.0283 187 LYS A CD 1134 C CE . LYS A 146 ? 0.6672 0.7616 0.7534 0.0008 0.2340 0.0270 187 LYS A CE 1135 N NZ . LYS A 146 ? 0.6791 0.7775 0.7828 -0.0035 0.2179 0.0238 187 LYS A NZ 1136 N N . LEU A 147 ? 0.5924 0.6409 0.5413 0.0146 0.2049 0.0186 188 LEU A N 1137 C CA . LEU A 147 ? 0.6288 0.6691 0.5486 0.0210 0.2099 0.0164 188 LEU A CA 1138 C C . LEU A 147 ? 0.6546 0.6841 0.5491 0.0224 0.2153 0.0235 188 LEU A C 1139 O O . LEU A 147 ? 0.6702 0.6957 0.5506 0.0266 0.2288 0.0266 188 LEU A O 1140 C CB . LEU A 147 ? 0.6311 0.6674 0.5378 0.0233 0.1954 0.0081 188 LEU A CB 1141 C CG . LEU A 147 ? 0.6348 0.6779 0.5546 0.0255 0.1936 0.0001 188 LEU A CG 1142 C CD1 . LEU A 147 ? 0.6430 0.6831 0.5562 0.0258 0.1779 -0.0067 188 LEU A CD1 1143 C CD2 . LEU A 147 ? 0.6309 0.6713 0.5366 0.0318 0.2061 -0.0018 188 LEU A CD2 1144 N N . GLU A 148 ? 0.6552 0.6799 0.5438 0.0193 0.2049 0.0261 189 GLU A N 1145 C CA . GLU A 148 ? 0.6935 0.7066 0.5547 0.0213 0.2064 0.0317 189 GLU A CA 1146 C C . GLU A 148 ? 0.7081 0.7201 0.5748 0.0185 0.2187 0.0423 189 GLU A C 1147 O O . GLU A 148 ? 0.7225 0.7268 0.5684 0.0225 0.2301 0.0475 189 GLU A O 1148 C CB . GLU A 148 ? 0.7035 0.7111 0.5538 0.0200 0.1897 0.0293 189 GLU A CB 1149 C CG . GLU A 148 ? 0.7614 0.7649 0.5932 0.0250 0.1809 0.0202 189 GLU A CG 1150 C CD . GLU A 148 ? 0.8083 0.8131 0.6456 0.0225 0.1640 0.0149 189 GLU A CD 1151 O OE1 . GLU A 148 ? 0.8012 0.8147 0.6612 0.0197 0.1597 0.0107 189 GLU A OE1 1152 O OE2 . GLU A 148 ? 0.8407 0.8374 0.6594 0.0236 0.1551 0.0148 189 GLU A OE2 1153 N N . ARG A 149 ? 0.6811 0.7005 0.5760 0.0121 0.2169 0.0455 190 ARG A N 1154 C CA . ARG A 149 ? 0.6906 0.7089 0.5944 0.0085 0.2272 0.0557 190 ARG A CA 1155 C C . ARG A 149 ? 0.6980 0.7229 0.6181 0.0086 0.2449 0.0593 190 ARG A C 1156 O O . ARG A 149 ? 0.7179 0.7376 0.6304 0.0092 0.2584 0.0680 190 ARG A O 1157 C CB . ARG A 149 ? 0.6614 0.6840 0.5886 0.0015 0.2173 0.0573 190 ARG A CB 1158 C CG . ARG A 149 ? 0.6309 0.6469 0.5431 0.0013 0.2014 0.0550 190 ARG A CG 1159 C CD . ARG A 149 ? 0.5735 0.5954 0.5109 -0.0048 0.1908 0.0542 190 ARG A CD 1160 N NE . ARG A 149 ? 0.5806 0.5956 0.5031 -0.0049 0.1773 0.0532 190 ARG A NE 1161 C CZ . ARG A 149 ? 0.5684 0.5851 0.5054 -0.0094 0.1675 0.0534 190 ARG A CZ 1162 N NH1 . ARG A 149 ? 0.5319 0.5568 0.4980 -0.0140 0.1690 0.0542 190 ARG A NH1 1163 N NH2 . ARG A 149 ? 0.5540 0.5645 0.4768 -0.0089 0.1559 0.0524 190 ARG A NH2 1164 N N . ASP A 150 ? 0.6868 0.7228 0.6296 0.0081 0.2453 0.0531 191 ASP A N 1165 C CA . ASP A 150 ? 0.7082 0.7521 0.6710 0.0080 0.2617 0.0560 191 ASP A CA 1166 C C . ASP A 150 ? 0.7207 0.7625 0.6651 0.0153 0.2726 0.0531 191 ASP A C 1167 O O . ASP A 150 ? 0.7447 0.7852 0.6858 0.0174 0.2897 0.0593 191 ASP A O 1168 C CB . ASP A 150 ? 0.6863 0.7442 0.6877 0.0035 0.2570 0.0516 191 ASP A CB 1169 C CG . ASP A 150 ? 0.7137 0.7736 0.7340 -0.0034 0.2466 0.0541 191 ASP A CG 1170 O OD1 . ASP A 150 ? 0.7632 0.8170 0.7791 -0.0061 0.2510 0.0624 191 ASP A OD1 1171 O OD2 . ASP A 150 ? 0.6994 0.7662 0.7380 -0.0058 0.2341 0.0478 191 ASP A OD2 1172 N N . MET A 151 ? 0.7144 0.7556 0.6468 0.0194 0.2632 0.0438 192 MET A N 1173 C CA . MET A 151 ? 0.7322 0.7715 0.6483 0.0266 0.2723 0.0396 192 MET A CA 1174 C C . MET A 151 ? 0.7556 0.7804 0.6301 0.0328 0.2738 0.0408 192 MET A C 1175 O O . MET A 151 ? 0.7656 0.7868 0.6225 0.0394 0.2833 0.0385 192 MET A O 1176 C CB . MET A 151 ? 0.7120 0.7576 0.6372 0.0284 0.2623 0.0286 192 MET A CB 1177 C CG . MET A 151 ? 0.7010 0.7607 0.6655 0.0239 0.2617 0.0266 192 MET A CG 1178 S SD . MET A 151 ? 0.7018 0.7674 0.6746 0.0265 0.2497 0.0144 192 MET A SD 1179 C CE . MET A 151 ? 0.7029 0.7696 0.6688 0.0341 0.2664 0.0116 192 MET A CE 1180 N N . LYS A 152 ? 0.7572 0.7735 0.6161 0.0309 0.2641 0.0440 193 LYS A N 1181 C CA . LYS A 152 ? 0.7872 0.7892 0.6065 0.0367 0.2622 0.0446 193 LYS A CA 1182 C C . LYS A 152 ? 0.7891 0.7881 0.5900 0.0431 0.2559 0.0341 193 LYS A C 1183 O O . LYS A 152 ? 0.8032 0.7939 0.5770 0.0502 0.2638 0.0334 193 LYS A O 1184 C CB . LYS A 152 ? 0.8241 0.8187 0.6260 0.0401 0.2803 0.0542 193 LYS A CB 1185 C CG . LYS A 152 ? 0.8688 0.8562 0.6645 0.0367 0.2805 0.0645 193 LYS A CG 1186 C CD . LYS A 152 ? 0.8806 0.8779 0.7135 0.0278 0.2802 0.0693 193 LYS A CD 1187 C CE . LYS A 152 ? 0.9179 0.9077 0.7454 0.0253 0.2872 0.0813 193 LYS A CE 1188 N NZ . LYS A 152 ? 0.9125 0.9062 0.7628 0.0175 0.2758 0.0832 193 LYS A NZ 1189 N N . ILE A 153 ? 0.7563 0.7616 0.5725 0.0406 0.2421 0.0260 194 ILE A N 1190 C CA . ILE A 153 ? 0.7670 0.7693 0.5687 0.0457 0.2339 0.0157 194 ILE A CA 1191 C C . ILE A 153 ? 0.7632 0.7585 0.5503 0.0448 0.2163 0.0126 194 ILE A C 1192 O O . ILE A 153 ? 0.7440 0.7432 0.5471 0.0388 0.2067 0.0144 194 ILE A O 1193 C CB . ILE A 153 ? 0.7501 0.7639 0.5780 0.0450 0.2334 0.0085 194 ILE A CB 1194 C CG1 . ILE A 153 ? 0.7867 0.8038 0.6176 0.0492 0.2517 0.0096 194 ILE A CG1 1195 C CG2 . ILE A 153 ? 0.7442 0.7549 0.5619 0.0482 0.2200 -0.0022 194 ILE A CG2 1196 C CD1 . ILE A 153 ? 0.7787 0.8101 0.6459 0.0463 0.2560 0.0076 194 ILE A CD1 1197 N N . ASN A 154 ? 0.7895 0.7741 0.5456 0.0511 0.2126 0.0083 195 ASN A N 1198 C CA . ASN A 154 ? 0.7961 0.7730 0.5357 0.0511 0.1966 0.0056 195 ASN A CA 1199 C C . ASN A 154 ? 0.7705 0.7490 0.5127 0.0523 0.1840 -0.0054 195 ASN A C 1200 O O . ASN A 154 ? 0.7768 0.7518 0.5060 0.0582 0.1864 -0.0121 195 ASN A O 1201 C CB . ASN A 154 ? 0.8421 0.8053 0.5452 0.0572 0.1995 0.0086 195 ASN A CB 1202 C CG . ASN A 154 ? 0.8975 0.8526 0.5839 0.0574 0.1829 0.0064 195 ASN A CG 1203 O OD1 . ASN A 154 ? 0.8768 0.8367 0.5797 0.0524 0.1700 0.0036 195 ASN A OD1 1204 N ND2 . ASN A 154 ? 1.0151 0.9576 0.6682 0.0637 0.1833 0.0076 195 ASN A ND2 1205 N N . CYS A 155 ? 0.7258 0.7091 0.4852 0.0469 0.1710 -0.0073 196 CYS A N 1206 C CA . CYS A 155 ? 0.7056 0.6904 0.4701 0.0472 0.1591 -0.0167 196 CYS A CA 1207 C C . CYS A 155 ? 0.7133 0.6879 0.4533 0.0508 0.1473 -0.0220 196 CYS A C 1208 O O . CYS A 155 ? 0.7033 0.6780 0.4457 0.0517 0.1380 -0.0302 196 CYS A O 1209 C CB . CYS A 155 ? 0.6756 0.6697 0.4686 0.0404 0.1507 -0.0167 196 CYS A CB 1210 S SG . CYS A 155 ? 0.6716 0.6784 0.4953 0.0378 0.1612 -0.0154 196 CYS A SG 1211 N N . SER A 156 ? 0.7274 0.6930 0.4444 0.0531 0.1473 -0.0174 197 SER A N 1212 C CA . SER A 156 ? 0.7431 0.6993 0.4388 0.0561 0.1342 -0.0223 197 SER A CA 1213 C C . SER A 156 ? 0.7513 0.7014 0.4297 0.0628 0.1324 -0.0319 197 SER A C 1214 O O . SER A 156 ? 0.7787 0.7246 0.4415 0.0684 0.1434 -0.0321 197 SER A O 1215 C CB . SER A 156 ? 0.7609 0.7086 0.4358 0.0574 0.1339 -0.0152 197 SER A CB 1216 O OG . SER A 156 ? 0.8126 0.7489 0.4587 0.0635 0.1261 -0.0202 197 SER A OG 1217 N N . GLY A 157 ? 0.7363 0.6861 0.4187 0.0622 0.1187 -0.0399 198 GLY A N 1218 C CA . GLY A 157 ? 0.7312 0.6747 0.3993 0.0680 0.1145 -0.0500 198 GLY A CA 1219 C C . GLY A 157 ? 0.7155 0.6654 0.3988 0.0688 0.1218 -0.0547 198 GLY A C 1220 O O . GLY A 157 ? 0.7235 0.6682 0.3954 0.0741 0.1205 -0.0630 198 GLY A O 1221 N N . LYS A 158 ? 0.6819 0.6427 0.3910 0.0637 0.1289 -0.0498 199 LYS A N 1222 C CA . LYS A 158 ? 0.6718 0.6393 0.3976 0.0644 0.1358 -0.0537 199 LYS A CA 1223 C C . LYS A 158 ? 0.6441 0.6179 0.3935 0.0598 0.1251 -0.0582 199 LYS A C 1224 O O . LYS A 158 ? 0.6201 0.5957 0.3781 0.0548 0.1156 -0.0558 199 LYS A O 1225 C CB . LYS A 158 ? 0.6641 0.6400 0.4052 0.0623 0.1507 -0.0461 199 LYS A CB 1226 C CG . LYS A 158 ? 0.7154 0.6862 0.4369 0.0658 0.1633 -0.0392 199 LYS A CG 1227 C CD . LYS A 158 ? 0.7606 0.7222 0.4554 0.0743 0.1685 -0.0448 199 LYS A CD 1228 C CE . LYS A 158 ? 0.8209 0.7761 0.4936 0.0781 0.1810 -0.0371 199 LYS A CE 1229 N NZ . LYS A 158 ? 0.8510 0.7928 0.4888 0.0862 0.1782 -0.0426 199 LYS A NZ 1230 N N . ILE A 159 ? 0.6353 0.6121 0.3950 0.0617 0.1271 -0.0643 200 ILE A N 1231 C CA . ILE A 159 ? 0.6129 0.5968 0.3979 0.0572 0.1196 -0.0668 200 ILE A CA 1232 C C . ILE A 159 ? 0.5910 0.5860 0.3999 0.0537 0.1285 -0.0610 200 ILE A C 1233 O O . ILE A 159 ? 0.6002 0.5983 0.4116 0.0566 0.1406 -0.0604 200 ILE A O 1234 C CB . ILE A 159 ? 0.6224 0.6032 0.4075 0.0609 0.1155 -0.0765 200 ILE A CB 1235 C CG1 . ILE A 159 ? 0.6447 0.6147 0.4089 0.0637 0.1046 -0.0827 200 ILE A CG1 1236 C CG2 . ILE A 159 ? 0.5980 0.5862 0.4099 0.0564 0.1094 -0.0777 200 ILE A CG2 1237 C CD1 . ILE A 159 ? 0.6476 0.6123 0.4077 0.0683 0.1012 -0.0929 200 ILE A CD1 1238 N N . VAL A 160 ? 0.5591 0.5601 0.3858 0.0477 0.1227 -0.0568 201 VAL A N 1239 C CA . VAL A 160 ? 0.5400 0.5512 0.3898 0.0443 0.1295 -0.0518 201 VAL A CA 1240 C C . VAL A 160 ? 0.5303 0.5473 0.4008 0.0438 0.1259 -0.0565 201 VAL A C 1241 O O . VAL A 160 ? 0.5112 0.5256 0.3832 0.0429 0.1152 -0.0607 201 VAL A O 1242 C CB . VAL A 160 ? 0.5411 0.5552 0.3976 0.0386 0.1267 -0.0439 201 VAL A CB 1243 C CG1 A VAL A 160 ? 0.5473 0.5555 0.3837 0.0399 0.1324 -0.0386 201 VAL A CG1 1244 C CG1 B VAL A 160 ? 0.5053 0.5282 0.3883 0.0338 0.1221 -0.0424 201 VAL A CG1 1245 C CG2 A VAL A 160 ? 0.4969 0.5097 0.3569 0.0353 0.1130 -0.0454 201 VAL A CG2 1246 C CG2 B VAL A 160 ? 0.5521 0.5660 0.4015 0.0390 0.1384 -0.0369 201 VAL A CG2 1247 N N . ILE A 161 ? 0.5063 0.5304 0.3917 0.0448 0.1352 -0.0560 202 ILE A N 1248 C CA . ILE A 161 ? 0.4736 0.5041 0.3809 0.0440 0.1319 -0.0590 202 ILE A CA 1249 C C . ILE A 161 ? 0.4635 0.5036 0.3934 0.0394 0.1337 -0.0530 202 ILE A C 1250 O O . ILE A 161 ? 0.4593 0.5038 0.3939 0.0388 0.1435 -0.0482 202 ILE A O 1251 C CB . ILE A 161 ? 0.4861 0.5169 0.3948 0.0496 0.1387 -0.0650 202 ILE A CB 1252 C CG1 . ILE A 161 ? 0.4623 0.4989 0.3935 0.0490 0.1340 -0.0681 202 ILE A CG1 1253 C CG2 . ILE A 161 ? 0.4656 0.4994 0.3720 0.0524 0.1542 -0.0620 202 ILE A CG2 1254 C CD1 . ILE A 161 ? 0.4902 0.5238 0.4189 0.0548 0.1363 -0.0759 202 ILE A CD1 1255 N N . ALA A 162 ? 0.4214 0.4643 0.3647 0.0362 0.1240 -0.0532 203 ALA A N 1256 C CA . ALA A 162 ? 0.4142 0.4651 0.3773 0.0320 0.1236 -0.0483 203 ALA A CA 1257 C C . ALA A 162 ? 0.3999 0.4557 0.3818 0.0324 0.1188 -0.0515 203 ALA A C 1258 O O . ALA A 162 ? 0.4186 0.4700 0.3966 0.0338 0.1115 -0.0560 203 ALA A O 1259 C CB . ALA A 162 ? 0.3930 0.4413 0.3514 0.0275 0.1154 -0.0440 203 ALA A CB 1260 N N . ARG A 163 ? 0.4073 0.4719 0.4100 0.0310 0.1221 -0.0490 204 ARG A N 1261 C CA . ARG A 163 ? 0.3957 0.4650 0.4167 0.0310 0.1157 -0.0511 204 ARG A CA 1262 C C . ARG A 163 ? 0.3846 0.4538 0.4100 0.0271 0.1055 -0.0485 204 ARG A C 1263 O O . ARG A 163 ? 0.3717 0.4421 0.3973 0.0235 0.1053 -0.0437 204 ARG A O 1264 C CB . ARG A 163 ? 0.4054 0.4842 0.4482 0.0321 0.1225 -0.0509 204 ARG A CB 1265 C CG . ARG A 163 ? 0.4103 0.4951 0.4627 0.0290 0.1294 -0.0454 204 ARG A CG 1266 C CD . ARG A 163 ? 0.4583 0.5531 0.5360 0.0302 0.1340 -0.0463 204 ARG A CD 1267 N NE . ARG A 163 ? 0.4542 0.5554 0.5440 0.0275 0.1425 -0.0413 204 ARG A NE 1268 C CZ . ARG A 163 ? 0.4857 0.5966 0.6011 0.0271 0.1453 -0.0410 204 ARG A CZ 1269 N NH1 . ARG A 163 ? 0.4202 0.5354 0.5508 0.0294 0.1392 -0.0452 204 ARG A NH1 1270 N NH2 . ARG A 163 ? 0.4367 0.5530 0.5634 0.0242 0.1536 -0.0362 204 ARG A NH2 1271 N N . TYR A 164 ? 0.3587 0.4258 0.3868 0.0282 0.0972 -0.0515 205 TYR A N 1272 C CA . TYR A 164 ? 0.3497 0.4171 0.3835 0.0253 0.0880 -0.0493 205 TYR A CA 1273 C C . TYR A 164 ? 0.3477 0.4235 0.4010 0.0237 0.0884 -0.0465 205 TYR A C 1274 O O . TYR A 164 ? 0.3515 0.4336 0.4188 0.0254 0.0940 -0.0476 205 TYR A O 1275 C CB . TYR A 164 ? 0.3345 0.3989 0.3703 0.0276 0.0811 -0.0529 205 TYR A CB 1276 C CG . TYR A 164 ? 0.3303 0.3861 0.3507 0.0278 0.0759 -0.0548 205 TYR A CG 1277 C CD1 . TYR A 164 ? 0.3122 0.3635 0.3289 0.0311 0.0754 -0.0597 205 TYR A CD1 1278 C CD2 . TYR A 164 ? 0.2968 0.3492 0.3084 0.0245 0.0708 -0.0519 205 TYR A CD2 1279 C CE1 . TYR A 164 ? 0.2954 0.3389 0.3008 0.0309 0.0697 -0.0616 205 TYR A CE1 1280 C CE2 . TYR A 164 ? 0.3210 0.3664 0.3216 0.0244 0.0655 -0.0537 205 TYR A CE2 1281 C CZ . TYR A 164 ? 0.3126 0.3537 0.3106 0.0274 0.0649 -0.0584 205 TYR A CZ 1282 O OH . TYR A 164 ? 0.3235 0.3577 0.3127 0.0268 0.0593 -0.0600 205 TYR A OH 1283 N N . GLY A 165 ? 0.3371 0.4131 0.3926 0.0204 0.0823 -0.0432 206 GLY A N 1284 C CA . GLY A 165 ? 0.3491 0.4322 0.4237 0.0190 0.0802 -0.0415 206 GLY A CA 1285 C C . GLY A 165 ? 0.3583 0.4420 0.4322 0.0148 0.0802 -0.0368 206 GLY A C 1286 O O . GLY A 165 ? 0.3568 0.4365 0.4168 0.0132 0.0843 -0.0346 206 GLY A O 1287 N N . LYS A 166 ? 0.3565 0.4446 0.4451 0.0132 0.0752 -0.0356 207 LYS A N 1288 C CA . LYS A 166 ? 0.3524 0.4422 0.4455 0.0092 0.0755 -0.0315 207 LYS A CA 1289 C C . LYS A 166 ? 0.3517 0.4350 0.4302 0.0070 0.0697 -0.0293 207 LYS A C 1290 O O . LYS A 166 ? 0.3453 0.4294 0.4299 0.0049 0.0642 -0.0276 207 LYS A O 1291 C CB . LYS A 166 ? 0.3587 0.4509 0.4531 0.0075 0.0867 -0.0287 207 LYS A CB 1292 C CG . LYS A 166 ? 0.3923 0.4921 0.5035 0.0095 0.0946 -0.0304 207 LYS A CG 1293 C CD . LYS A 166 ? 0.4212 0.5285 0.5567 0.0092 0.0896 -0.0317 207 LYS A CD 1294 C CE . LYS A 166 ? 0.4593 0.5749 0.6134 0.0103 0.0990 -0.0324 207 LYS A CE 1295 N NZ . LYS A 166 ? 0.4910 0.6143 0.6703 0.0106 0.0933 -0.0344 207 LYS A NZ 1296 N N . VAL A 167 ? 0.3457 0.4227 0.4055 0.0076 0.0708 -0.0294 208 VAL A N 1297 C CA . VAL A 167 ? 0.3245 0.3956 0.3707 0.0057 0.0653 -0.0274 208 VAL A CA 1298 C C . VAL A 167 ? 0.3320 0.3973 0.3644 0.0078 0.0617 -0.0300 208 VAL A C 1299 O O . VAL A 167 ? 0.3328 0.3973 0.3624 0.0104 0.0648 -0.0331 208 VAL A O 1300 C CB . VAL A 167 ? 0.3330 0.4016 0.3699 0.0031 0.0708 -0.0233 208 VAL A CB 1301 C CG1 . VAL A 167 ? 0.3312 0.4054 0.3834 0.0007 0.0758 -0.0202 208 VAL A CG1 1302 C CG2 . VAL A 167 ? 0.3395 0.4048 0.3624 0.0049 0.0777 -0.0241 208 VAL A CG2 1303 N N . PHE A 168 ? 0.3037 0.3646 0.3276 0.0066 0.0555 -0.0288 209 PHE A N 1304 C CA . PHE A 168 ? 0.3067 0.3620 0.3191 0.0079 0.0518 -0.0309 209 PHE A CA 1305 C C . PHE A 168 ? 0.3182 0.3700 0.3179 0.0088 0.0568 -0.0324 209 PHE A C 1306 O O . PHE A 168 ? 0.3350 0.3860 0.3280 0.0077 0.0612 -0.0302 209 PHE A O 1307 C CB . PHE A 168 ? 0.3002 0.3521 0.3063 0.0060 0.0458 -0.0286 209 PHE A CB 1308 C CG . PHE A 168 ? 0.3200 0.3665 0.3154 0.0068 0.0421 -0.0303 209 PHE A CG 1309 C CD1 . PHE A 168 ? 0.3182 0.3634 0.3161 0.0090 0.0397 -0.0331 209 PHE A CD1 1310 C CD2 . PHE A 168 ? 0.3590 0.4015 0.3428 0.0053 0.0409 -0.0289 209 PHE A CD2 1311 C CE1 . PHE A 168 ? 0.3630 0.4031 0.3532 0.0093 0.0364 -0.0346 209 PHE A CE1 1312 C CE2 . PHE A 168 ? 0.3868 0.4246 0.3628 0.0058 0.0369 -0.0308 209 PHE A CE2 1313 C CZ . PHE A 168 ? 0.3523 0.3891 0.3323 0.0076 0.0350 -0.0337 209 PHE A CZ 1314 N N . ARG A 169 ? 0.3219 0.3709 0.3176 0.0113 0.0558 -0.0362 210 ARG A N 1315 C CA . ARG A 169 ? 0.3265 0.3716 0.3098 0.0129 0.0600 -0.0387 210 ARG A CA 1316 C C . ARG A 169 ? 0.3401 0.3798 0.3082 0.0116 0.0579 -0.0375 210 ARG A C 1317 O O . ARG A 169 ? 0.3558 0.3926 0.3124 0.0127 0.0620 -0.0384 210 ARG A O 1318 C CB . ARG A 169 ? 0.3237 0.3661 0.3067 0.0157 0.0583 -0.0436 210 ARG A CB 1319 C CG . ARG A 169 ? 0.2984 0.3365 0.2792 0.0150 0.0503 -0.0442 210 ARG A CG 1320 C CD . ARG A 169 ? 0.3294 0.3646 0.3126 0.0177 0.0489 -0.0486 210 ARG A CD 1321 N NE . ARG A 169 ? 0.2892 0.3280 0.2859 0.0190 0.0480 -0.0483 210 ARG A NE 1322 C CZ . ARG A 169 ? 0.2948 0.3339 0.2970 0.0182 0.0430 -0.0458 210 ARG A CZ 1323 N NH1 . ARG A 169 ? 0.2921 0.3288 0.2890 0.0159 0.0390 -0.0435 210 ARG A NH1 1324 N NH2 . ARG A 169 ? 0.2866 0.3283 0.2997 0.0201 0.0418 -0.0457 210 ARG A NH2 1325 N N . GLY A 170 ? 0.3353 0.3735 0.3028 0.0096 0.0514 -0.0357 211 GLY A N 1326 C CA . GLY A 170 ? 0.3654 0.3991 0.3204 0.0084 0.0487 -0.0343 211 GLY A CA 1327 C C . GLY A 170 ? 0.3684 0.4030 0.3192 0.0070 0.0533 -0.0302 211 GLY A C 1328 O O . GLY A 170 ? 0.3809 0.4111 0.3182 0.0074 0.0540 -0.0298 211 GLY A O 1329 N N . ASN A 171 ? 0.3617 0.4014 0.3243 0.0055 0.0560 -0.0272 212 ASN A N 1330 C CA . ASN A 171 ? 0.3694 0.4098 0.3302 0.0042 0.0618 -0.0230 212 ASN A CA 1331 C C . ASN A 171 ? 0.3849 0.4247 0.3389 0.0063 0.0701 -0.0238 212 ASN A C 1332 O O . ASN A 171 ? 0.4086 0.4450 0.3512 0.0063 0.0742 -0.0210 212 ASN A O 1333 C CB . ASN A 171 ? 0.3588 0.4050 0.3359 0.0021 0.0629 -0.0202 212 ASN A CB 1334 C CG . ASN A 171 ? 0.3610 0.4070 0.3422 0.0002 0.0552 -0.0187 212 ASN A CG 1335 O OD1 . ASN A 171 ? 0.3639 0.4118 0.3534 0.0007 0.0503 -0.0207 212 ASN A OD1 1336 N ND2 . ASN A 171 ? 0.3797 0.4227 0.3545 -0.0017 0.0541 -0.0151 212 ASN A ND2 1337 N N . LYS A 172 ? 0.3753 0.4176 0.3353 0.0086 0.0730 -0.0277 213 LYS A N 1338 C CA . LYS A 172 ? 0.3915 0.4326 0.3435 0.0114 0.0813 -0.0292 213 LYS A CA 1339 C C . LYS A 172 ? 0.4014 0.4347 0.3322 0.0134 0.0801 -0.0309 213 LYS A C 1340 O O . LYS A 172 ? 0.4118 0.4421 0.3304 0.0150 0.0868 -0.0294 213 LYS A O 1341 C CB . LYS A 172 ? 0.3717 0.4159 0.3326 0.0142 0.0836 -0.0340 213 LYS A CB 1342 C CG . LYS A 172 ? 0.3634 0.4150 0.3455 0.0130 0.0829 -0.0335 213 LYS A CG 1343 C CD . LYS A 172 ? 0.3618 0.4158 0.3515 0.0164 0.0848 -0.0383 213 LYS A CD 1344 C CE . LYS A 172 ? 0.3552 0.4162 0.3655 0.0158 0.0832 -0.0380 213 LYS A CE 1345 N NZ . LYS A 172 ? 0.3612 0.4290 0.3843 0.0162 0.0920 -0.0368 213 LYS A NZ 1346 N N . VAL A 173 ? 0.3957 0.4254 0.3220 0.0137 0.0716 -0.0343 214 VAL A N 1347 C CA . VAL A 173 ? 0.3954 0.4176 0.3034 0.0158 0.0686 -0.0372 214 VAL A CA 1348 C C . VAL A 173 ? 0.4074 0.4261 0.3040 0.0143 0.0671 -0.0326 214 VAL A C 1349 O O . VAL A 173 ? 0.4286 0.4418 0.3083 0.0166 0.0689 -0.0329 214 VAL A O 1350 C CB . VAL A 173 ? 0.4019 0.4217 0.3115 0.0160 0.0597 -0.0420 214 VAL A CB 1351 C CG1 . VAL A 173 ? 0.4201 0.4323 0.3123 0.0176 0.0547 -0.0450 214 VAL A CG1 1352 C CG2 . VAL A 173 ? 0.3878 0.4093 0.3054 0.0182 0.0617 -0.0467 214 VAL A CG2 1353 N N . LYS A 174 ? 0.3955 0.4169 0.3010 0.0109 0.0635 -0.0285 215 LYS A N 1354 C CA . LYS A 174 ? 0.4203 0.4385 0.3169 0.0095 0.0622 -0.0238 215 LYS A CA 1355 C C . LYS A 174 ? 0.4347 0.4521 0.3247 0.0104 0.0720 -0.0198 215 LYS A C 1356 O O . LYS A 174 ? 0.4615 0.4728 0.3342 0.0121 0.0731 -0.0182 215 LYS A O 1357 C CB . LYS A 174 ? 0.4133 0.4351 0.3225 0.0060 0.0578 -0.0202 215 LYS A CB 1358 C CG . LYS A 174 ? 0.4536 0.4719 0.3547 0.0047 0.0571 -0.0151 215 LYS A CG 1359 C CD . LYS A 174 ? 0.5078 0.5285 0.4196 0.0017 0.0513 -0.0126 215 LYS A CD 1360 C CE . LYS A 174 ? 0.5659 0.5832 0.4713 0.0004 0.0517 -0.0071 215 LYS A CE 1361 N NZ . LYS A 174 ? 0.5838 0.6044 0.4988 -0.0014 0.0592 -0.0029 215 LYS A NZ 1362 N N . ASN A 175 ? 0.4359 0.4593 0.3397 0.0096 0.0792 -0.0184 216 ASN A N 1363 C CA . ASN A 175 ? 0.4275 0.4511 0.3287 0.0099 0.0899 -0.0139 216 ASN A CA 1364 C C . ASN A 175 ? 0.4428 0.4612 0.3257 0.0144 0.0954 -0.0164 216 ASN A C 1365 O O . ASN A 175 ? 0.4738 0.4876 0.3429 0.0157 0.1011 -0.0124 216 ASN A O 1366 C CB . ASN A 175 ? 0.4095 0.4415 0.3318 0.0083 0.0961 -0.0128 216 ASN A CB 1367 C CG . ASN A 175 ? 0.4269 0.4636 0.3667 0.0042 0.0907 -0.0104 216 ASN A CG 1368 O OD1 . ASN A 175 ? 0.4513 0.4849 0.3868 0.0024 0.0845 -0.0080 216 ASN A OD1 1369 N ND2 . ASN A 175 ? 0.4175 0.4615 0.3770 0.0032 0.0930 -0.0111 216 ASN A ND2 1370 N N . ALA A 176 ? 0.4484 0.4668 0.3305 0.0171 0.0936 -0.0229 217 ALA A N 1371 C CA . ALA A 176 ? 0.4757 0.4883 0.3392 0.0220 0.0976 -0.0267 217 ALA A CA 1372 C C . ALA A 176 ? 0.5065 0.5101 0.3479 0.0238 0.0917 -0.0270 217 ALA A C 1373 O O . ALA A 176 ? 0.5415 0.5392 0.3642 0.0273 0.0971 -0.0261 217 ALA A O 1374 C CB . ALA A 176 ? 0.4662 0.4800 0.3346 0.0244 0.0953 -0.0342 217 ALA A CB 1375 N N . GLN A 177 ? 0.5158 0.5184 0.3593 0.0217 0.0807 -0.0282 218 GLN A N 1376 C CA . GLN A 177 ? 0.5476 0.5422 0.3722 0.0234 0.0736 -0.0290 218 GLN A CA 1377 C C . GLN A 177 ? 0.5651 0.5558 0.3774 0.0236 0.0780 -0.0221 218 GLN A C 1378 O O . GLN A 177 ? 0.5619 0.5447 0.3525 0.0274 0.0783 -0.0223 218 GLN A O 1379 C CB . GLN A 177 ? 0.5513 0.5471 0.3847 0.0204 0.0620 -0.0303 218 GLN A CB 1380 C CG . GLN A 177 ? 0.5989 0.5945 0.4363 0.0215 0.0559 -0.0377 218 GLN A CG 1381 C CD . GLN A 177 ? 0.6492 0.6448 0.4929 0.0191 0.0447 -0.0392 218 GLN A CD 1382 O OE1 . GLN A 177 ? 0.6675 0.6645 0.5203 0.0187 0.0404 -0.0438 218 GLN A OE1 1383 N NE2 . GLN A 177 ? 0.6925 0.6861 0.5312 0.0178 0.0404 -0.0354 218 GLN A NE2 1384 N N . LEU A 178 ? 0.5561 0.5517 0.3823 0.0195 0.0809 -0.0159 219 LEU A N 1385 C CA . LEU A 178 ? 0.5745 0.5665 0.3922 0.0189 0.0849 -0.0085 219 LEU A CA 1386 C C . LEU A 178 ? 0.5881 0.5781 0.3966 0.0216 0.0979 -0.0051 219 LEU A C 1387 O O . LEU A 178 ? 0.6107 0.5943 0.4035 0.0231 0.1017 0.0002 219 LEU A O 1388 C CB . LEU A 178 ? 0.5649 0.5623 0.4015 0.0137 0.0832 -0.0036 219 LEU A CB 1389 C CG . LEU A 178 ? 0.5866 0.5840 0.4273 0.0119 0.0706 -0.0058 219 LEU A CG 1390 C CD1 . LEU A 178 ? 0.6263 0.6295 0.4866 0.0073 0.0687 -0.0023 219 LEU A CD1 1391 C CD2 . LEU A 178 ? 0.6546 0.6438 0.4760 0.0141 0.0639 -0.0052 219 LEU A CD2 1392 N N . ALA A 179 ? 0.5750 0.5699 0.3923 0.0225 0.1051 -0.0080 220 ALA A N 1393 C CA . ALA A 179 ? 0.5863 0.5788 0.3927 0.0262 0.1179 -0.0063 220 ALA A CA 1394 C C . ALA A 179 ? 0.6097 0.5930 0.3893 0.0324 0.1167 -0.0110 220 ALA A C 1395 O O . ALA A 179 ? 0.6204 0.6003 0.3869 0.0364 0.1272 -0.0096 220 ALA A O 1396 C CB . ALA A 179 ? 0.5703 0.5715 0.3961 0.0256 0.1256 -0.0083 220 ALA A CB 1397 N N . GLY A 180 ? 0.5989 0.5783 0.3707 0.0335 0.1042 -0.0167 221 GLY A N 1398 C CA . GLY A 180 ? 0.6112 0.5812 0.3571 0.0397 0.1019 -0.0217 221 GLY A CA 1399 C C . GLY A 180 ? 0.6125 0.5829 0.3584 0.0429 0.1013 -0.0306 221 GLY A C 1400 O O . GLY A 180 ? 0.6255 0.5879 0.3499 0.0485 0.0998 -0.0355 221 GLY A O 1401 N N . ALA A 181 ? 0.5879 0.5671 0.3575 0.0398 0.1016 -0.0331 222 ALA A N 1402 C CA . ALA A 181 ? 0.5946 0.5745 0.3666 0.0428 0.1019 -0.0412 222 ALA A CA 1403 C C . ALA A 181 ? 0.5948 0.5685 0.3569 0.0447 0.0891 -0.0488 222 ALA A C 1404 O O . ALA A 181 ? 0.5878 0.5606 0.3520 0.0418 0.0789 -0.0480 222 ALA A O 1405 C CB . ALA A 181 ? 0.5676 0.5579 0.3679 0.0389 0.1035 -0.0416 222 ALA A CB 1406 N N . LYS A 182 ? 0.5887 0.5580 0.3410 0.0496 0.0894 -0.0564 223 LYS A N 1407 C CA . LYS A 182 ? 0.5998 0.5640 0.3477 0.0506 0.0765 -0.0642 223 LYS A CA 1408 C C . LYS A 182 ? 0.5838 0.5532 0.3529 0.0484 0.0724 -0.0696 223 LYS A C 1409 O O . LYS A 182 ? 0.5825 0.5478 0.3505 0.0491 0.0625 -0.0763 223 LYS A O 1410 C CB . LYS A 182 ? 0.6404 0.5939 0.3615 0.0575 0.0752 -0.0703 223 LYS A CB 1411 C CG . LYS A 182 ? 0.6720 0.6240 0.3884 0.0625 0.0831 -0.0758 223 LYS A CG 1412 C CD . LYS A 182 ? 0.7359 0.6762 0.4222 0.0697 0.0812 -0.0812 223 LYS A CD 1413 C CE . LYS A 182 ? 0.7747 0.7131 0.4519 0.0755 0.0928 -0.0843 223 LYS A CE 1414 N NZ . LYS A 182 ? 0.8259 0.7520 0.4704 0.0832 0.0920 -0.0885 223 LYS A NZ 1415 N N . GLY A 183 ? 0.5560 0.5338 0.3442 0.0460 0.0799 -0.0666 224 GLY A N 1416 C CA . GLY A 183 ? 0.5427 0.5249 0.3500 0.0446 0.0769 -0.0711 224 GLY A CA 1417 C C . GLY A 183 ? 0.5202 0.5120 0.3475 0.0419 0.0852 -0.0661 224 GLY A C 1418 O O . GLY A 183 ? 0.5260 0.5202 0.3506 0.0426 0.0953 -0.0613 224 GLY A O 1419 N N . VAL A 184 ? 0.4892 0.4863 0.3367 0.0389 0.0809 -0.0671 225 VAL A N 1420 C CA . VAL A 184 ? 0.4654 0.4714 0.3328 0.0368 0.0870 -0.0635 225 VAL A CA 1421 C C . VAL A 184 ? 0.4710 0.4787 0.3510 0.0384 0.0858 -0.0690 225 VAL A C 1422 O O . VAL A 184 ? 0.4517 0.4565 0.3350 0.0376 0.0771 -0.0727 225 VAL A O 1423 C CB . VAL A 184 ? 0.4471 0.4586 0.3290 0.0314 0.0823 -0.0578 225 VAL A CB 1424 C CG1 . VAL A 184 ? 0.4117 0.4321 0.3133 0.0299 0.0885 -0.0545 225 VAL A CG1 1425 C CG2 . VAL A 184 ? 0.4663 0.4753 0.3366 0.0296 0.0818 -0.0524 225 VAL A CG2 1426 N N . ILE A 185 ? 0.4514 0.4637 0.3390 0.0406 0.0949 -0.0693 226 ILE A N 1427 C CA . ILE A 185 ? 0.4357 0.4508 0.3382 0.0420 0.0944 -0.0735 226 ILE A CA 1428 C C . ILE A 185 ? 0.4166 0.4412 0.3403 0.0390 0.0969 -0.0685 226 ILE A C 1429 O O . ILE A 185 ? 0.4244 0.4540 0.3516 0.0385 0.1051 -0.0641 226 ILE A O 1430 C CB . ILE A 185 ? 0.4486 0.4614 0.3439 0.0478 0.1026 -0.0786 226 ILE A CB 1431 C CG1 . ILE A 185 ? 0.4638 0.4661 0.3372 0.0513 0.0986 -0.0847 226 ILE A CG1 1432 C CG2 . ILE A 185 ? 0.4474 0.4641 0.3603 0.0495 0.1033 -0.0822 226 ILE A CG2 1433 C CD1 . ILE A 185 ? 0.4588 0.4577 0.3190 0.0575 0.1078 -0.0890 226 ILE A CD1 1434 N N . LEU A 186 ? 0.3883 0.4149 0.3258 0.0369 0.0896 -0.0688 227 LEU A N 1435 C CA . LEU A 186 ? 0.3733 0.4082 0.3309 0.0346 0.0900 -0.0649 227 LEU A CA 1436 C C . LEU A 186 ? 0.3639 0.4012 0.3341 0.0378 0.0916 -0.0689 227 LEU A C 1437 O O . LEU A 186 ? 0.3727 0.4044 0.3389 0.0400 0.0877 -0.0740 227 LEU A O 1438 C CB . LEU A 186 ? 0.3443 0.3788 0.3067 0.0307 0.0806 -0.0621 227 LEU A CB 1439 C CG . LEU A 186 ? 0.3589 0.3910 0.3100 0.0276 0.0781 -0.0582 227 LEU A CG 1440 C CD1 . LEU A 186 ? 0.3558 0.3862 0.3104 0.0247 0.0683 -0.0571 227 LEU A CD1 1441 C CD2 . LEU A 186 ? 0.3918 0.4299 0.3484 0.0254 0.0838 -0.0525 227 LEU A CD2 1442 N N . TYR A 187 ? 0.3583 0.4037 0.3440 0.0382 0.0973 -0.0669 228 TYR A N 1443 C CA . TYR A 187 ? 0.3587 0.4070 0.3578 0.0415 0.0986 -0.0706 228 TYR A CA 1444 C C . TYR A 187 ? 0.3579 0.4149 0.3777 0.0400 0.0981 -0.0671 228 TYR A C 1445 O O . TYR A 187 ? 0.3476 0.4095 0.3721 0.0368 0.1001 -0.0623 228 TYR A O 1446 C CB . TYR A 187 ? 0.3688 0.4167 0.3631 0.0463 0.1083 -0.0746 228 TYR A CB 1447 C CG . TYR A 187 ? 0.3781 0.4346 0.3826 0.0464 0.1186 -0.0712 228 TYR A CG 1448 C CD1 . TYR A 187 ? 0.3759 0.4403 0.4012 0.0482 0.1218 -0.0719 228 TYR A CD1 1449 C CD2 . TYR A 187 ? 0.4019 0.4586 0.3967 0.0444 0.1246 -0.0669 228 TYR A CD2 1450 C CE1 . TYR A 187 ? 0.3781 0.4510 0.4156 0.0479 0.1311 -0.0687 228 TYR A CE1 1451 C CE2 . TYR A 187 ? 0.3900 0.4548 0.3962 0.0441 0.1347 -0.0631 228 TYR A CE2 1452 C CZ . TYR A 187 ? 0.4066 0.4797 0.4349 0.0456 0.1378 -0.0642 228 TYR A CZ 1453 O OH . TYR A 187 ? 0.4240 0.5054 0.4663 0.0449 0.1474 -0.0606 228 TYR A OH 1454 N N . SER A 188 ? 0.3479 0.4066 0.3805 0.0425 0.0952 -0.0698 229 SER A N 1455 C CA . SER A 188 ? 0.3298 0.3964 0.3824 0.0419 0.0936 -0.0675 229 SER A CA 1456 C C . SER A 188 ? 0.3282 0.4022 0.3943 0.0449 0.1024 -0.0689 229 SER A C 1457 O O . SER A 188 ? 0.3299 0.4027 0.3981 0.0493 0.1047 -0.0735 229 SER A O 1458 C CB . SER A 188 ? 0.3193 0.3827 0.3774 0.0432 0.0845 -0.0689 229 SER A CB 1459 O OG . SER A 188 ? 0.3324 0.3901 0.3803 0.0401 0.0772 -0.0667 229 SER A OG 1460 N N . ASP A 189 ? 0.3263 0.4079 0.4023 0.0427 0.1075 -0.0652 230 ASP A N 1461 C CA . ASP A 189 ? 0.3430 0.4327 0.4344 0.0453 0.1167 -0.0662 230 ASP A CA 1462 C C . ASP A 189 ? 0.3395 0.4357 0.4535 0.0467 0.1113 -0.0672 230 ASP A C 1463 O O . ASP A 189 ? 0.3377 0.4353 0.4582 0.0441 0.1030 -0.0647 230 ASP A O 1464 C CB . ASP A 189 ? 0.3428 0.4379 0.4370 0.0423 0.1253 -0.0616 230 ASP A CB 1465 C CG . ASP A 189 ? 0.3641 0.4659 0.4694 0.0454 0.1377 -0.0628 230 ASP A CG 1466 O OD1 . ASP A 189 ? 0.3796 0.4778 0.4700 0.0472 0.1468 -0.0633 230 ASP A OD1 1467 O OD2 . ASP A 189 ? 0.3730 0.4833 0.5013 0.0466 0.1380 -0.0636 230 ASP A OD2 1468 N N . PRO A 190 ? 0.3490 0.4493 0.4749 0.0513 0.1159 -0.0709 231 PRO A N 1469 C CA . PRO A 190 ? 0.3467 0.4533 0.4945 0.0530 0.1102 -0.0718 231 PRO A CA 1470 C C . PRO A 190 ? 0.3595 0.4754 0.5254 0.0495 0.1097 -0.0679 231 PRO A C 1471 O O . PRO A 190 ? 0.3524 0.4717 0.5323 0.0498 0.1012 -0.0678 231 PRO A O 1472 C CB . PRO A 190 ? 0.3653 0.4757 0.5233 0.0585 0.1177 -0.0762 231 PRO A CB 1473 C CG . PRO A 190 ? 0.3842 0.4861 0.5208 0.0604 0.1229 -0.0790 231 PRO A CG 1474 C CD . PRO A 190 ? 0.3455 0.4429 0.4636 0.0558 0.1243 -0.0753 231 PRO A CD 1475 N N . ALA A 191 ? 0.3628 0.4822 0.5280 0.0464 0.1184 -0.0647 232 ALA A N 1476 C CA . ALA A 191 ? 0.3751 0.5025 0.5577 0.0424 0.1180 -0.0609 232 ALA A CA 1477 C C . ALA A 191 ? 0.3673 0.4914 0.5468 0.0392 0.1054 -0.0587 232 ALA A C 1478 O O . ALA A 191 ? 0.3624 0.4925 0.5599 0.0381 0.0993 -0.0580 232 ALA A O 1479 C CB . ALA A 191 ? 0.3883 0.5174 0.5662 0.0393 0.1296 -0.0570 232 ALA A CB 1480 N N . ASP A 192 ? 0.3669 0.4814 0.5239 0.0383 0.1009 -0.0583 233 ASP A N 1481 C CA . ASP A 192 ? 0.3682 0.4784 0.5187 0.0355 0.0904 -0.0560 233 ASP A CA 1482 C C . ASP A 192 ? 0.3634 0.4682 0.5102 0.0385 0.0805 -0.0584 233 ASP A C 1483 O O . ASP A 192 ? 0.3705 0.4735 0.5172 0.0374 0.0712 -0.0569 233 ASP A O 1484 C CB . ASP A 192 ? 0.3707 0.4738 0.4993 0.0323 0.0927 -0.0534 233 ASP A CB 1485 C CG . ASP A 192 ? 0.3694 0.4764 0.4993 0.0295 0.1029 -0.0502 233 ASP A CG 1486 O OD1 . ASP A 192 ? 0.3933 0.5051 0.5349 0.0261 0.1018 -0.0470 233 ASP A OD1 1487 O OD2 . ASP A 192 ? 0.3732 0.4780 0.4924 0.0310 0.1121 -0.0509 233 ASP A OD2 1488 N N . TYR A 193 ? 0.3465 0.4482 0.4897 0.0427 0.0824 -0.0621 234 TYR A N 1489 C CA . TYR A 193 ? 0.3336 0.4287 0.4715 0.0455 0.0738 -0.0639 234 TYR A CA 1490 C C . TYR A 193 ? 0.3484 0.4458 0.4994 0.0509 0.0731 -0.0676 234 TYR A C 1491 O O . TYR A 193 ? 0.3431 0.4339 0.4885 0.0539 0.0681 -0.0693 234 TYR A O 1492 C CB . TYR A 193 ? 0.3319 0.4170 0.4478 0.0449 0.0739 -0.0644 234 TYR A CB 1493 C CG . TYR A 193 ? 0.3295 0.4117 0.4328 0.0400 0.0723 -0.0606 234 TYR A CG 1494 C CD1 . TYR A 193 ? 0.3207 0.4034 0.4157 0.0374 0.0797 -0.0593 234 TYR A CD1 1495 C CD2 . TYR A 193 ? 0.3009 0.3797 0.4008 0.0383 0.0635 -0.0581 234 TYR A CD2 1496 C CE1 . TYR A 193 ? 0.3288 0.4088 0.4129 0.0331 0.0778 -0.0557 234 TYR A CE1 1497 C CE2 . TYR A 193 ? 0.3443 0.4209 0.4339 0.0340 0.0620 -0.0548 234 TYR A CE2 1498 C CZ . TYR A 193 ? 0.3340 0.4112 0.4161 0.0314 0.0689 -0.0536 234 TYR A CZ 1499 O OH . TYR A 193 ? 0.3276 0.4022 0.3999 0.0276 0.0670 -0.0503 234 TYR A OH 1500 N N . PHE A 194 ? 0.3421 0.4488 0.5115 0.0524 0.0783 -0.0688 235 PHE A N 1501 C CA . PHE A 194 ? 0.3558 0.4655 0.5396 0.0577 0.0771 -0.0723 235 PHE A CA 1502 C C . PHE A 194 ? 0.3623 0.4826 0.5699 0.0576 0.0748 -0.0717 235 PHE A C 1503 O O . PHE A 194 ? 0.3754 0.5039 0.5953 0.0563 0.0829 -0.0715 235 PHE A O 1504 C CB . PHE A 194 ? 0.3699 0.4802 0.5529 0.0607 0.0874 -0.0758 235 PHE A CB 1505 C CG . PHE A 194 ? 0.3733 0.4841 0.5673 0.0668 0.0857 -0.0799 235 PHE A CG 1506 C CD1 . PHE A 194 ? 0.3926 0.4934 0.5740 0.0698 0.0819 -0.0822 235 PHE A CD1 1507 C CD2 . PHE A 194 ? 0.3881 0.5091 0.6061 0.0696 0.0877 -0.0815 235 PHE A CD2 1508 C CE1 . PHE A 194 ? 0.3989 0.4994 0.5905 0.0757 0.0802 -0.0859 235 PHE A CE1 1509 C CE2 . PHE A 194 ? 0.4069 0.5284 0.6356 0.0756 0.0857 -0.0853 235 PHE A CE2 1510 C CZ . PHE A 194 ? 0.4275 0.5383 0.6424 0.0788 0.0819 -0.0874 235 PHE A CZ 1511 N N . ALA A 195 ? 0.3490 0.4684 0.5620 0.0590 0.0637 -0.0712 236 ALA A N 1512 C CA . ALA A 195 ? 0.3664 0.4949 0.6021 0.0596 0.0590 -0.0714 236 ALA A CA 1513 C C . ALA A 195 ? 0.3759 0.5117 0.6320 0.0646 0.0621 -0.0753 236 ALA A C 1514 O O . ALA A 195 ? 0.3736 0.5047 0.6261 0.0694 0.0609 -0.0778 236 ALA A O 1515 C CB . ALA A 195 ? 0.3611 0.4851 0.5937 0.0608 0.0458 -0.0704 236 ALA A CB 1516 N N . PRO A 196 ? 0.3873 0.5346 0.6660 0.0635 0.0668 -0.0757 237 PRO A N 1517 C CA . PRO A 196 ? 0.3956 0.5514 0.6972 0.0682 0.0700 -0.0793 237 PRO A CA 1518 C C . PRO A 196 ? 0.3885 0.5427 0.6977 0.0742 0.0583 -0.0819 237 PRO A C 1519 O O . PRO A 196 ? 0.3983 0.5505 0.7076 0.0740 0.0466 -0.0808 237 PRO A O 1520 C CB . PRO A 196 ? 0.3989 0.5670 0.7248 0.0648 0.0731 -0.0783 237 PRO A CB 1521 C CG . PRO A 196 ? 0.3985 0.5638 0.7106 0.0582 0.0769 -0.0741 237 PRO A CG 1522 C CD . PRO A 196 ? 0.3876 0.5402 0.6713 0.0575 0.0704 -0.0725 237 PRO A CD 1523 N N . GLY A 197 ? 0.3960 0.5500 0.7100 0.0797 0.0613 -0.0853 238 GLY A N 1524 C CA . GLY A 197 ? 0.3916 0.5450 0.7159 0.0861 0.0513 -0.0879 238 GLY A CA 1525 C C . GLY A 197 ? 0.3958 0.5361 0.6992 0.0885 0.0415 -0.0867 238 GLY A C 1526 O O . GLY A 197 ? 0.4226 0.5612 0.7326 0.0938 0.0319 -0.0880 238 GLY A O 1527 N N . VAL A 198 ? 0.3583 0.4890 0.6368 0.0848 0.0440 -0.0842 239 VAL A N 1528 C CA . VAL A 198 ? 0.3386 0.4564 0.5970 0.0866 0.0367 -0.0827 239 VAL A CA 1529 C C . VAL A 198 ? 0.3382 0.4481 0.5823 0.0878 0.0438 -0.0843 239 VAL A C 1530 O O . VAL A 198 ? 0.3461 0.4578 0.5858 0.0851 0.0541 -0.0852 239 VAL A O 1531 C CB . VAL A 198 ? 0.3285 0.4410 0.5714 0.0818 0.0303 -0.0783 239 VAL A CB 1532 C CG1 A VAL A 198 ? 0.3369 0.4584 0.5882 0.0762 0.0339 -0.0771 239 VAL A CG1 1533 C CG1 B VAL A 198 ? 0.3071 0.4063 0.5296 0.0835 0.0242 -0.0762 239 VAL A CG1 1534 C CG2 A VAL A 198 ? 0.3246 0.4251 0.5423 0.0798 0.0315 -0.0762 239 VAL A CG2 1535 C CG2 B VAL A 198 ? 0.3146 0.4342 0.5724 0.0816 0.0220 -0.0777 239 VAL A CG2 1536 N N . LYS A 199 ? 0.3405 0.4413 0.5778 0.0924 0.0383 -0.0848 240 LYS A N 1537 C CA . LYS A 199 ? 0.3607 0.4529 0.5856 0.0939 0.0434 -0.0868 240 LYS A CA 1538 C C . LYS A 199 ? 0.3598 0.4428 0.5613 0.0887 0.0448 -0.0842 240 LYS A C 1539 O O . LYS A 199 ? 0.3510 0.4308 0.5439 0.0857 0.0388 -0.0802 240 LYS A O 1540 C CB . LYS A 199 ? 0.3751 0.4599 0.6017 0.1004 0.0365 -0.0877 240 LYS A CB 1541 C CG . LYS A 199 ? 0.4008 0.4941 0.6510 0.1066 0.0357 -0.0913 240 LYS A CG 1542 C CD . LYS A 199 ? 0.4570 0.5574 0.7159 0.1068 0.0475 -0.0955 240 LYS A CD 1543 C CE . LYS A 199 ? 0.5181 0.6255 0.7998 0.1137 0.0474 -0.0994 240 LYS A CE 1544 N NZ . LYS A 199 ? 0.5384 0.6530 0.8283 0.1141 0.0602 -0.1034 240 LYS A NZ 1545 N N . SER A 200 ? 0.3720 0.4508 0.5639 0.0881 0.0524 -0.0867 241 SER A N 1546 C CA . SER A 200 ? 0.3699 0.4391 0.5406 0.0841 0.0528 -0.0851 241 SER A CA 1547 C C . SER A 200 ? 0.3557 0.4136 0.5180 0.0861 0.0450 -0.0833 241 SER A C 1548 O O . SER A 200 ? 0.3609 0.4159 0.5307 0.0915 0.0419 -0.0848 241 SER A O 1549 C CB . SER A 200 ? 0.4125 0.4784 0.5752 0.0844 0.0613 -0.0893 241 SER A CB 1550 O OG . SER A 200 ? 0.4836 0.5582 0.6510 0.0830 0.0702 -0.0908 241 SER A OG 1551 N N . TYR A 201 ? 0.3412 0.3922 0.4879 0.0818 0.0426 -0.0800 242 TYR A N 1552 C CA . TYR A 201 ? 0.3350 0.3744 0.4725 0.0829 0.0370 -0.0779 242 TYR A CA 1553 C C . TYR A 201 ? 0.3564 0.3885 0.4930 0.0864 0.0398 -0.0822 242 TYR A C 1554 O O . TYR A 201 ? 0.3512 0.3840 0.4843 0.0853 0.0464 -0.0862 242 TYR A O 1555 C CB . TYR A 201 ? 0.3314 0.3654 0.4532 0.0772 0.0359 -0.0744 242 TYR A CB 1556 C CG . TYR A 201 ? 0.3136 0.3381 0.4293 0.0784 0.0295 -0.0705 242 TYR A CG 1557 C CD1 . TYR A 201 ? 0.3312 0.3568 0.4495 0.0800 0.0231 -0.0664 242 TYR A CD1 1558 C CD2 . TYR A 201 ? 0.3481 0.3618 0.4559 0.0784 0.0298 -0.0710 242 TYR A CD2 1559 C CE1 . TYR A 201 ? 0.3623 0.3784 0.4740 0.0819 0.0180 -0.0624 242 TYR A CE1 1560 C CE2 . TYR A 201 ? 0.3484 0.3529 0.4517 0.0798 0.0248 -0.0668 242 TYR A CE2 1561 C CZ . TYR A 201 ? 0.3591 0.3648 0.4636 0.0817 0.0193 -0.0622 242 TYR A CZ 1562 O OH . TYR A 201 ? 0.4509 0.4469 0.5495 0.0835 0.0152 -0.0576 242 TYR A OH 1563 N N . PRO A 202 ? 0.3675 0.3920 0.5065 0.0909 0.0348 -0.0814 243 PRO A N 1564 C CA . PRO A 202 ? 0.3827 0.4027 0.5213 0.0930 0.0270 -0.0764 243 PRO A CA 1565 C C . PRO A 202 ? 0.3959 0.4223 0.5485 0.0981 0.0223 -0.0761 243 PRO A C 1566 O O . PRO A 202 ? 0.4154 0.4366 0.5662 0.1010 0.0152 -0.0721 243 PRO A O 1567 C CB . PRO A 202 ? 0.3915 0.3984 0.5245 0.0953 0.0255 -0.0762 243 PRO A CB 1568 C CG . PRO A 202 ? 0.4005 0.4082 0.5401 0.0982 0.0308 -0.0827 243 PRO A CG 1569 C CD . PRO A 202 ? 0.3911 0.4080 0.5295 0.0941 0.0375 -0.0858 243 PRO A CD 1570 N N . ASP A 203 ? 0.3921 0.4293 0.5583 0.0995 0.0261 -0.0800 244 ASP A N 1571 C CA . ASP A 203 ? 0.4046 0.4485 0.5873 0.1049 0.0216 -0.0808 244 ASP A CA 1572 C C . ASP A 203 ? 0.3821 0.4360 0.5713 0.1025 0.0186 -0.0789 244 ASP A C 1573 O O . ASP A 203 ? 0.3794 0.4384 0.5817 0.1066 0.0129 -0.0791 244 ASP A O 1574 C CB . ASP A 203 ? 0.4184 0.4676 0.6151 0.1090 0.0272 -0.0864 244 ASP A CB 1575 C CG . ASP A 203 ? 0.4791 0.5170 0.6697 0.1121 0.0289 -0.0887 244 ASP A CG 1576 O OD1 . ASP A 203 ? 0.4796 0.5073 0.6652 0.1151 0.0226 -0.0859 244 ASP A OD1 1577 O OD2 . ASP A 203 ? 0.5445 0.5832 0.7343 0.1114 0.0367 -0.0931 244 ASP A OD2 1578 N N . GLY A 204 ? 0.3691 0.4248 0.5489 0.0960 0.0216 -0.0770 245 GLY A N 1579 C CA . GLY A 204 ? 0.3371 0.4004 0.5208 0.0931 0.0184 -0.0748 245 GLY A CA 1580 C C . GLY A 204 ? 0.3303 0.3903 0.4978 0.0864 0.0210 -0.0720 245 GLY A C 1581 O O . GLY A 204 ? 0.3475 0.3989 0.5015 0.0848 0.0237 -0.0715 245 GLY A O 1582 N N . TRP A 205 ? 0.3048 0.3717 0.4747 0.0826 0.0201 -0.0704 246 TRP A N 1583 C CA . TRP A 205 ? 0.2917 0.3555 0.4466 0.0766 0.0214 -0.0673 246 TRP A CA 1584 C C . TRP A 205 ? 0.2918 0.3611 0.4454 0.0715 0.0303 -0.0686 246 TRP A C 1585 O O . TRP A 205 ? 0.2897 0.3580 0.4329 0.0666 0.0311 -0.0661 246 TRP A O 1586 C CB . TRP A 205 ? 0.2899 0.3547 0.4436 0.0757 0.0138 -0.0639 246 TRP A CB 1587 C CG . TRP A 205 ? 0.3066 0.3820 0.4784 0.0770 0.0107 -0.0655 246 TRP A CG 1588 C CD1 . TRP A 205 ? 0.3277 0.4053 0.5118 0.0827 0.0037 -0.0668 246 TRP A CD1 1589 C CD2 . TRP A 205 ? 0.2991 0.3840 0.4794 0.0724 0.0140 -0.0658 246 TRP A CD2 1590 N NE1 . TRP A 205 ? 0.3475 0.4358 0.5482 0.0818 0.0022 -0.0684 246 TRP A NE1 1591 C CE2 . TRP A 205 ? 0.3226 0.4154 0.5216 0.0753 0.0087 -0.0676 246 TRP A CE2 1592 C CE3 . TRP A 205 ? 0.3487 0.4358 0.5228 0.0663 0.0207 -0.0647 246 TRP A CE3 1593 C CZ2 . TRP A 205 ? 0.3403 0.4433 0.5536 0.0719 0.0102 -0.0683 246 TRP A CZ2 1594 C CZ3 . TRP A 205 ? 0.3563 0.4530 0.5429 0.0630 0.0226 -0.0648 246 TRP A CZ3 1595 C CH2 . TRP A 205 ? 0.3391 0.4438 0.5460 0.0657 0.0175 -0.0666 246 TRP A CH2 1596 N N . ASN A 206 ? 0.2833 0.3578 0.4464 0.0731 0.0372 -0.0724 247 ASN A N 1597 C CA . ASN A 206 ? 0.2887 0.3675 0.4491 0.0692 0.0466 -0.0736 247 ASN A CA 1598 C C . ASN A 206 ? 0.2968 0.3673 0.4404 0.0678 0.0509 -0.0747 247 ASN A C 1599 O O . ASN A 206 ? 0.3091 0.3712 0.4467 0.0704 0.0481 -0.0757 247 ASN A O 1600 C CB . ASN A 206 ? 0.2924 0.3807 0.4701 0.0718 0.0533 -0.0771 247 ASN A CB 1601 C CG . ASN A 206 ? 0.3053 0.4045 0.4974 0.0693 0.0542 -0.0757 247 ASN A CG 1602 O OD1 . ASN A 206 ? 0.3333 0.4327 0.5201 0.0649 0.0511 -0.0723 247 ASN A OD1 1603 N ND2 . ASN A 206 ? 0.3040 0.4126 0.5159 0.0720 0.0584 -0.0783 247 ASN A ND2 1604 N N . LEU A 207 ? 0.2927 0.3652 0.4288 0.0637 0.0575 -0.0745 248 LEU A N 1605 C CA . LEU A 207 ? 0.2999 0.3648 0.4196 0.0622 0.0611 -0.0760 248 LEU A CA 1606 C C . LEU A 207 ? 0.3048 0.3696 0.4270 0.0662 0.0680 -0.0812 248 LEU A C 1607 O O . LEU A 207 ? 0.3222 0.3952 0.4543 0.0673 0.0748 -0.0827 248 LEU A O 1608 C CB . LEU A 207 ? 0.2881 0.3549 0.3982 0.0570 0.0650 -0.0738 248 LEU A CB 1609 C CG . LEU A 207 ? 0.3429 0.4021 0.4348 0.0552 0.0676 -0.0752 248 LEU A CG 1610 C CD1 . LEU A 207 ? 0.3207 0.3710 0.4031 0.0539 0.0603 -0.0737 248 LEU A CD1 1611 C CD2 . LEU A 207 ? 0.3638 0.4262 0.4481 0.0510 0.0727 -0.0731 248 LEU A CD2 1612 N N . PRO A 208 ? 0.3080 0.3636 0.4228 0.0687 0.0663 -0.0841 249 PRO A N 1613 C CA . PRO A 208 ? 0.3190 0.3732 0.4332 0.0724 0.0729 -0.0895 249 PRO A CA 1614 C C . PRO A 208 ? 0.3163 0.3691 0.4162 0.0699 0.0796 -0.0912 249 PRO A C 1615 O O . PRO A 208 ? 0.3255 0.3760 0.4139 0.0653 0.0778 -0.0883 249 PRO A O 1616 C CB . PRO A 208 ? 0.3489 0.3922 0.4585 0.0751 0.0678 -0.0918 249 PRO A CB 1617 C CG . PRO A 208 ? 0.3233 0.3624 0.4301 0.0727 0.0597 -0.0871 249 PRO A CG 1618 C CD . PRO A 208 ? 0.3199 0.3659 0.4272 0.0684 0.0586 -0.0824 249 PRO A CD 1619 N N . GLY A 209 ? 0.3293 0.3827 0.4290 0.0735 0.0872 -0.0960 250 GLY A N 1620 C CA . GLY A 209 ? 0.3557 0.4078 0.4409 0.0722 0.0941 -0.0976 250 GLY A CA 1621 C C . GLY A 209 ? 0.3546 0.3956 0.4208 0.0704 0.0902 -0.0993 250 GLY A C 1622 O O . GLY A 209 ? 0.3736 0.4128 0.4255 0.0684 0.0937 -0.0994 250 GLY A O 1623 N N . GLY A 210 ? 0.3478 0.3813 0.4143 0.0712 0.0829 -0.1005 251 GLY A N 1624 C CA . GLY A 210 ? 0.3471 0.3704 0.3991 0.0688 0.0776 -0.1016 251 GLY A CA 1625 C C . GLY A 210 ? 0.3351 0.3575 0.3842 0.0634 0.0709 -0.0957 251 GLY A C 1626 O O . GLY A 210 ? 0.3405 0.3556 0.3789 0.0610 0.0668 -0.0962 251 GLY A O 1627 N N . GLY A 211 ? 0.3198 0.3496 0.3789 0.0618 0.0695 -0.0905 252 GLY A N 1628 C CA . GLY A 211 ? 0.3020 0.3314 0.3584 0.0573 0.0636 -0.0850 252 GLY A CA 1629 C C . GLY A 211 ? 0.3016 0.3325 0.3464 0.0531 0.0658 -0.0832 252 GLY A C 1630 O O . GLY A 211 ? 0.3256 0.3613 0.3681 0.0534 0.0727 -0.0842 252 GLY A O 1631 N N . VAL A 212 ? 0.3045 0.3314 0.3424 0.0493 0.0603 -0.0802 253 VAL A N 1632 C CA . VAL A 212 ? 0.3065 0.3338 0.3329 0.0455 0.0613 -0.0785 253 VAL A CA 1633 C C . VAL A 212 ? 0.3049 0.3331 0.3321 0.0417 0.0559 -0.0730 253 VAL A C 1634 O O . VAL A 212 ? 0.3055 0.3293 0.3350 0.0414 0.0504 -0.0716 253 VAL A O 1635 C CB . VAL A 212 ? 0.2952 0.3141 0.3074 0.0453 0.0604 -0.0829 253 VAL A CB 1636 C CG1 . VAL A 212 ? 0.3195 0.3390 0.3194 0.0421 0.0615 -0.0812 253 VAL A CG1 1637 C CG2 . VAL A 212 ? 0.3132 0.3290 0.3232 0.0500 0.0650 -0.0895 253 VAL A CG2 1638 N N . GLN A 213 ? 0.2933 0.3266 0.3180 0.0388 0.0578 -0.0697 254 GLN A N 1639 C CA . GLN A 213 ? 0.2826 0.3167 0.3068 0.0352 0.0529 -0.0647 254 GLN A CA 1640 C C . GLN A 213 ? 0.2989 0.3275 0.3103 0.0323 0.0504 -0.0646 254 GLN A C 1641 O O . GLN A 213 ? 0.3144 0.3431 0.3165 0.0313 0.0536 -0.0654 254 GLN A O 1642 C CB . GLN A 213 ? 0.2846 0.3268 0.3141 0.0336 0.0560 -0.0614 254 GLN A CB 1643 C CG . GLN A 213 ? 0.2731 0.3162 0.3015 0.0301 0.0513 -0.0566 254 GLN A CG 1644 C CD . GLN A 213 ? 0.2874 0.3372 0.3193 0.0279 0.0546 -0.0537 254 GLN A CD 1645 O OE1 . GLN A 213 ? 0.3004 0.3498 0.3263 0.0248 0.0531 -0.0507 254 GLN A OE1 1646 N NE2 . GLN A 213 ? 0.2845 0.3406 0.3272 0.0296 0.0592 -0.0545 254 GLN A NE2 1647 N N . ARG A 214 ? 0.2803 0.3038 0.2913 0.0314 0.0448 -0.0637 255 ARG A N 1648 C CA . ARG A 214 ? 0.3010 0.3204 0.3029 0.0282 0.0415 -0.0628 255 ARG A CA 1649 C C . ARG A 214 ? 0.2911 0.3149 0.2917 0.0251 0.0406 -0.0579 255 ARG A C 1650 O O . ARG A 214 ? 0.2747 0.3039 0.2821 0.0253 0.0416 -0.0551 255 ARG A O 1651 C CB . ARG A 214 ? 0.2952 0.3087 0.2999 0.0280 0.0366 -0.0625 255 ARG A CB 1652 C CG . ARG A 214 ? 0.3145 0.3218 0.3193 0.0305 0.0367 -0.0678 255 ARG A CG 1653 C CD . ARG A 214 ? 0.3257 0.3283 0.3378 0.0311 0.0332 -0.0661 255 ARG A CD 1654 N NE . ARG A 214 ? 0.3489 0.3456 0.3632 0.0337 0.0333 -0.0709 255 ARG A NE 1655 C CZ . ARG A 214 ? 0.3525 0.3500 0.3718 0.0375 0.0360 -0.0732 255 ARG A CZ 1656 N NH1 . ARG A 214 ? 0.3186 0.3234 0.3421 0.0390 0.0389 -0.0714 255 ARG A NH1 1657 N NH2 . ARG A 214 ? 0.3504 0.3416 0.3715 0.0399 0.0359 -0.0779 255 ARG A NH2 1658 N N . GLY A 215 ? 0.2874 0.3086 0.2796 0.0225 0.0381 -0.0571 256 GLY A N 1659 C CA . GLY A 215 ? 0.2737 0.2980 0.2653 0.0197 0.0363 -0.0524 256 GLY A CA 1660 C C . GLY A 215 ? 0.2898 0.3120 0.2709 0.0173 0.0350 -0.0523 256 GLY A C 1661 O O . GLY A 215 ? 0.2912 0.3113 0.2641 0.0181 0.0371 -0.0554 256 GLY A O 1662 N N A ASN A 216 ? 0.2917 0.3139 0.2724 0.0149 0.0314 -0.0488 257 ASN A N 1663 N N B ASN A 216 ? 0.2873 0.3099 0.2685 0.0150 0.0316 -0.0486 257 ASN A N 1664 C CA A ASN A 216 ? 0.2905 0.3108 0.2618 0.0130 0.0296 -0.0487 257 ASN A CA 1665 C CA B ASN A 216 ? 0.2920 0.3135 0.2652 0.0126 0.0295 -0.0473 257 ASN A CA 1666 C C A ASN A 216 ? 0.2915 0.3152 0.2578 0.0125 0.0334 -0.0469 257 ASN A C 1667 C C B ASN A 216 ? 0.2964 0.3204 0.2629 0.0123 0.0333 -0.0464 257 ASN A C 1668 O O A ASN A 216 ? 0.2858 0.3141 0.2581 0.0126 0.0365 -0.0446 257 ASN A O 1669 O O B ASN A 216 ? 0.2924 0.3210 0.2642 0.0124 0.0367 -0.0442 257 ASN A O 1670 C CB A ASN A 216 ? 0.2841 0.3036 0.2570 0.0108 0.0249 -0.0457 257 ASN A CB 1671 C CB B ASN A 216 ? 0.2856 0.3087 0.2636 0.0110 0.0263 -0.0429 257 ASN A CB 1672 C CG A ASN A 216 ? 0.2962 0.3199 0.2713 0.0094 0.0250 -0.0410 257 ASN A CG 1673 C CG B ASN A 216 ? 0.2830 0.3053 0.2551 0.0087 0.0236 -0.0411 257 ASN A CG 1674 O OD1 A ASN A 216 ? 0.2935 0.3186 0.2632 0.0082 0.0258 -0.0394 257 ASN A OD1 1675 O OD1 B ASN A 216 ? 0.2934 0.3129 0.2582 0.0083 0.0224 -0.0434 257 ASN A OD1 1676 N ND2 A ASN A 216 ? 0.3271 0.3521 0.3098 0.0099 0.0239 -0.0387 257 ASN A ND2 1677 N ND2 B ASN A 216 ? 0.3187 0.3432 0.2939 0.0075 0.0220 -0.0372 257 ASN A ND2 1678 N N . ILE A 217 ? 0.3075 0.3283 0.2627 0.0121 0.0329 -0.0480 258 ILE A N 1679 C CA . ILE A 217 ? 0.3284 0.3508 0.2764 0.0117 0.0367 -0.0459 258 ILE A CA 1680 C C . ILE A 217 ? 0.3454 0.3664 0.2870 0.0095 0.0328 -0.0430 258 ILE A C 1681 O O . ILE A 217 ? 0.3657 0.3854 0.2974 0.0096 0.0348 -0.0419 258 ILE A O 1682 C CB . ILE A 217 ? 0.3338 0.3532 0.2714 0.0142 0.0406 -0.0497 258 ILE A CB 1683 C CG1 . ILE A 217 ? 0.3271 0.3403 0.2579 0.0152 0.0353 -0.0546 258 ILE A CG1 1684 C CG2 . ILE A 217 ? 0.3556 0.3776 0.3004 0.0165 0.0459 -0.0518 258 ILE A CG2 1685 C CD1 . ILE A 217 ? 0.4235 0.4318 0.3390 0.0180 0.0374 -0.0588 258 ILE A CD1 1686 N N . LEU A 218 ? 0.3558 0.3767 0.3027 0.0080 0.0277 -0.0416 259 LEU A N 1687 C CA . LEU A 218 ? 0.3785 0.3987 0.3213 0.0061 0.0239 -0.0387 259 LEU A CA 1688 C C . LEU A 218 ? 0.3885 0.4119 0.3319 0.0048 0.0267 -0.0341 259 LEU A C 1689 O O . LEU A 218 ? 0.3988 0.4260 0.3498 0.0048 0.0301 -0.0325 259 LEU A O 1690 C CB . LEU A 218 ? 0.3929 0.4132 0.3437 0.0049 0.0192 -0.0378 259 LEU A CB 1691 C CG . LEU A 218 ? 0.3993 0.4159 0.3507 0.0052 0.0153 -0.0416 259 LEU A CG 1692 C CD1 . LEU A 218 ? 0.4507 0.4680 0.4110 0.0039 0.0121 -0.0394 259 LEU A CD1 1693 C CD2 . LEU A 218 ? 0.4675 0.4805 0.4093 0.0053 0.0120 -0.0441 259 LEU A CD2 1694 N N . ASN A 219 ? 0.3907 0.4124 0.3266 0.0039 0.0249 -0.0319 260 ASN A N 1695 C CA . ASN A 219 ? 0.4164 0.4405 0.3547 0.0022 0.0260 -0.0271 260 ASN A CA 1696 C C . ASN A 219 ? 0.3930 0.4163 0.3324 0.0010 0.0203 -0.0253 260 ASN A C 1697 O O . ASN A 219 ? 0.4323 0.4531 0.3639 0.0006 0.0182 -0.0238 260 ASN A O 1698 C CB . ASN A 219 ? 0.4423 0.4647 0.3704 0.0025 0.0302 -0.0252 260 ASN A CB 1699 C CG . ASN A 219 ? 0.5102 0.5351 0.4411 0.0033 0.0375 -0.0253 260 ASN A CG 1700 O OD1 . ASN A 219 ? 0.5691 0.5981 0.5092 0.0020 0.0406 -0.0224 260 ASN A OD1 1701 N ND2 . ASN A 219 ? 0.5424 0.5651 0.4661 0.0056 0.0402 -0.0288 260 ASN A ND2 1702 N N . LEU A 220 ? 0.3661 0.3912 0.3146 0.0007 0.0178 -0.0254 261 LEU A N 1703 C CA . LEU A 220 ? 0.3591 0.3835 0.3094 -0.0001 0.0129 -0.0241 261 LEU A CA 1704 C C . LEU A 220 ? 0.3564 0.3824 0.3091 -0.0011 0.0124 -0.0201 261 LEU A C 1705 O O . LEU A 220 ? 0.3364 0.3614 0.2886 -0.0016 0.0088 -0.0188 261 LEU A O 1706 C CB . LEU A 220 ? 0.3679 0.3931 0.3268 0.0004 0.0115 -0.0252 261 LEU A CB 1707 C CG . LEU A 220 ? 0.3750 0.3979 0.3341 0.0011 0.0106 -0.0290 261 LEU A CG 1708 C CD1 . LEU A 220 ? 0.3519 0.3754 0.3203 0.0018 0.0106 -0.0289 261 LEU A CD1 1709 C CD2 . LEU A 220 ? 0.3781 0.3984 0.3328 0.0006 0.0063 -0.0304 261 LEU A CD2 1710 N N . ASN A 221 ? 0.3442 0.3724 0.3002 -0.0014 0.0159 -0.0185 262 ASN A N 1711 C CA . ASN A 221 ? 0.3243 0.3536 0.2840 -0.0024 0.0148 -0.0152 262 ASN A CA 1712 C C . ASN A 221 ? 0.3074 0.3368 0.2715 -0.0019 0.0108 -0.0148 262 ASN A C 1713 O O . ASN A 221 ? 0.2972 0.3257 0.2605 -0.0024 0.0083 -0.0127 262 ASN A O 1714 C CB . ASN A 221 ? 0.3292 0.3564 0.2821 -0.0035 0.0150 -0.0125 262 ASN A CB 1715 C CG . ASN A 221 ? 0.3736 0.4007 0.3227 -0.0038 0.0204 -0.0118 262 ASN A CG 1716 O OD1 . ASN A 221 ? 0.3773 0.4073 0.3331 -0.0038 0.0240 -0.0123 262 ASN A OD1 1717 N ND2 . ASN A 221 ? 0.3898 0.4134 0.3283 -0.0037 0.0211 -0.0107 262 ASN A ND2 1718 N N . GLY A 222 ? 0.2751 0.3053 0.2437 -0.0007 0.0106 -0.0166 263 GLY A N 1719 C CA . GLY A 222 ? 0.2615 0.2916 0.2340 0.0003 0.0081 -0.0158 263 GLY A CA 1720 C C . GLY A 222 ? 0.2472 0.2757 0.2185 0.0003 0.0057 -0.0160 263 GLY A C 1721 O O . GLY A 222 ? 0.2663 0.2947 0.2407 0.0012 0.0044 -0.0150 263 GLY A O 1722 N N . ALA A 223 ? 0.2352 0.2624 0.2025 -0.0005 0.0051 -0.0176 264 ALA A N 1723 C CA . ALA A 223 ? 0.2362 0.2623 0.2042 -0.0007 0.0020 -0.0180 264 ALA A CA 1724 C C . ALA A 223 ? 0.2420 0.2678 0.2161 -0.0001 0.0022 -0.0192 264 ALA A C 1725 O O . ALA A 223 ? 0.2785 0.3042 0.2563 -0.0002 0.0003 -0.0187 264 ALA A O 1726 C CB . ALA A 223 ? 0.2517 0.2759 0.2128 -0.0014 0.0001 -0.0198 264 ALA A CB 1727 N N . GLY A 224 ? 0.2370 0.2625 0.2127 0.0006 0.0045 -0.0207 265 GLY A N 1728 C CA . GLY A 224 ? 0.2391 0.2634 0.2205 0.0011 0.0049 -0.0216 265 GLY A CA 1729 C C . GLY A 224 ? 0.2374 0.2598 0.2183 0.0001 0.0032 -0.0250 265 GLY A C 1730 O O . GLY A 224 ? 0.2737 0.2954 0.2486 -0.0001 0.0029 -0.0273 265 GLY A O 1731 N N . ASP A 225 ? 0.2320 0.2533 0.2193 -0.0003 0.0019 -0.0254 266 ASP A N 1732 C CA . ASP A 225 ? 0.2489 0.2682 0.2372 -0.0013 -0.0008 -0.0293 266 ASP A CA 1733 C C . ASP A 225 ? 0.2642 0.2834 0.2448 -0.0018 -0.0042 -0.0310 266 ASP A C 1734 O O . ASP A 225 ? 0.2738 0.2944 0.2540 -0.0022 -0.0064 -0.0291 266 ASP A O 1735 C CB . ASP A 225 ? 0.2542 0.2731 0.2529 -0.0022 -0.0019 -0.0288 266 ASP A CB 1736 C CG . ASP A 225 ? 0.2676 0.2849 0.2693 -0.0034 -0.0063 -0.0331 266 ASP A CG 1737 O OD1 . ASP A 225 ? 0.2760 0.2907 0.2739 -0.0032 -0.0071 -0.0369 266 ASP A OD1 1738 O OD2 . ASP A 225 ? 0.2656 0.2841 0.2735 -0.0045 -0.0093 -0.0328 266 ASP A OD2 1739 N N . PRO A 226 ? 0.2868 0.3038 0.2609 -0.0014 -0.0050 -0.0348 267 PRO A N 1740 C CA . PRO A 226 ? 0.2999 0.3157 0.2643 -0.0012 -0.0079 -0.0360 267 PRO A CA 1741 C C . PRO A 226 ? 0.2877 0.3031 0.2543 -0.0019 -0.0139 -0.0371 267 PRO A C 1742 O O . PRO A 226 ? 0.3104 0.3254 0.2695 -0.0015 -0.0166 -0.0364 267 PRO A O 1743 C CB . PRO A 226 ? 0.3072 0.3198 0.2648 -0.0001 -0.0077 -0.0407 267 PRO A CB 1744 C CG . PRO A 226 ? 0.3344 0.3475 0.2969 0.0003 -0.0032 -0.0407 267 PRO A CG 1745 C CD . PRO A 226 ? 0.3033 0.3185 0.2771 -0.0005 -0.0023 -0.0375 267 PRO A CD 1746 N N . LEU A 227 ? 0.2778 0.2934 0.2557 -0.0029 -0.0159 -0.0384 268 LEU A N 1747 C CA . LEU A 227 ? 0.2841 0.2998 0.2667 -0.0035 -0.0219 -0.0399 268 LEU A CA 1748 C C . LEU A 227 ? 0.2560 0.2753 0.2462 -0.0041 -0.0221 -0.0357 268 LEU A C 1749 O O . LEU A 227 ? 0.2677 0.2877 0.2613 -0.0044 -0.0273 -0.0367 268 LEU A O 1750 C CB . LEU A 227 ? 0.2681 0.2821 0.2610 -0.0045 -0.0244 -0.0440 268 LEU A CB 1751 C CG . LEU A 227 ? 0.2958 0.3056 0.2819 -0.0036 -0.0251 -0.0491 268 LEU A CG 1752 C CD1 . LEU A 227 ? 0.3232 0.3311 0.3214 -0.0048 -0.0287 -0.0533 268 LEU A CD1 1753 C CD2 . LEU A 227 ? 0.3469 0.3542 0.3182 -0.0019 -0.0292 -0.0520 268 LEU A CD2 1754 N N . THR A 228 ? 0.2337 0.2551 0.2261 -0.0040 -0.0168 -0.0314 269 THR A N 1755 C CA . THR A 228 ? 0.2381 0.2624 0.2378 -0.0040 -0.0163 -0.0278 269 THR A CA 1756 C C . THR A 228 ? 0.2184 0.2438 0.2117 -0.0030 -0.0130 -0.0238 269 THR A C 1757 O O . THR A 228 ? 0.2264 0.2533 0.2246 -0.0024 -0.0096 -0.0208 269 THR A O 1758 C CB . THR A 228 ? 0.2212 0.2463 0.2333 -0.0045 -0.0127 -0.0264 269 THR A CB 1759 O OG1 . THR A 228 ? 0.2256 0.2493 0.2349 -0.0038 -0.0078 -0.0254 269 THR A OG1 1760 C CG2 . THR A 228 ? 0.2504 0.2747 0.2727 -0.0060 -0.0162 -0.0301 269 THR A CG2 1761 N N . PRO A 229 ? 0.2347 0.2591 0.2173 -0.0026 -0.0140 -0.0237 270 PRO A N 1762 C CA . PRO A 229 ? 0.2405 0.2657 0.2188 -0.0020 -0.0113 -0.0203 270 PRO A CA 1763 C C . PRO A 229 ? 0.2408 0.2678 0.2241 -0.0015 -0.0121 -0.0175 270 PRO A C 1764 O O . PRO A 229 ? 0.2610 0.2884 0.2460 -0.0015 -0.0161 -0.0178 270 PRO A O 1765 C CB . PRO A 229 ? 0.2589 0.2822 0.2260 -0.0020 -0.0125 -0.0206 270 PRO A CB 1766 C CG . PRO A 229 ? 0.2667 0.2883 0.2317 -0.0020 -0.0179 -0.0238 270 PRO A CG 1767 C CD . PRO A 229 ? 0.2549 0.2769 0.2289 -0.0026 -0.0180 -0.0267 270 PRO A CD 1768 N N . GLY A 230 ? 0.2364 0.2644 0.2223 -0.0005 -0.0085 -0.0151 271 GLY A N 1769 C CA . GLY A 230 ? 0.2345 0.2637 0.2243 0.0006 -0.0085 -0.0126 271 GLY A CA 1770 C C . GLY A 230 ? 0.2373 0.2678 0.2364 0.0013 -0.0062 -0.0118 271 GLY A C 1771 O O . GLY A 230 ? 0.2524 0.2836 0.2538 0.0030 -0.0046 -0.0095 271 GLY A O 1772 N N . TYR A 231 ? 0.2284 0.2589 0.2334 0.0002 -0.0060 -0.0135 272 TYR A N 1773 C CA . TYR A 231 ? 0.2324 0.2641 0.2483 0.0005 -0.0039 -0.0125 272 TYR A CA 1774 C C . TYR A 231 ? 0.2163 0.2464 0.2358 -0.0001 -0.0010 -0.0132 272 TYR A C 1775 O O . TYR A 231 ? 0.2328 0.2614 0.2489 -0.0013 -0.0027 -0.0160 272 TYR A O 1776 C CB . TYR A 231 ? 0.2242 0.2579 0.2482 -0.0007 -0.0082 -0.0140 272 TYR A CB 1777 C CG . TYR A 231 ? 0.2374 0.2721 0.2571 0.0000 -0.0118 -0.0134 272 TYR A CG 1778 C CD1 . TYR A 231 ? 0.2343 0.2706 0.2570 0.0018 -0.0099 -0.0107 272 TYR A CD1 1779 C CD2 . TYR A 231 ? 0.2313 0.2645 0.2423 -0.0006 -0.0165 -0.0153 272 TYR A CD2 1780 C CE1 . TYR A 231 ? 0.2401 0.2766 0.2587 0.0027 -0.0132 -0.0101 272 TYR A CE1 1781 C CE2 . TYR A 231 ? 0.2371 0.2702 0.2432 0.0003 -0.0195 -0.0142 272 TYR A CE2 1782 C CZ . TYR A 231 ? 0.2460 0.2808 0.2566 0.0018 -0.0180 -0.0117 272 TYR A CZ 1783 O OH . TYR A 231 ? 0.2583 0.2925 0.2646 0.0028 -0.0211 -0.0106 272 TYR A OH 1784 N N . PRO A 232 ? 0.2255 0.2555 0.2517 0.0009 0.0034 -0.0107 273 PRO A N 1785 C CA . PRO A 232 ? 0.2195 0.2470 0.2486 0.0005 0.0064 -0.0109 273 PRO A CA 1786 C C . PRO A 232 ? 0.2285 0.2560 0.2669 -0.0021 0.0036 -0.0141 273 PRO A C 1787 O O . PRO A 232 ? 0.2238 0.2535 0.2711 -0.0033 0.0012 -0.0147 273 PRO A O 1788 C CB . PRO A 232 ? 0.2305 0.2573 0.2640 0.0027 0.0123 -0.0065 273 PRO A CB 1789 C CG . PRO A 232 ? 0.2358 0.2658 0.2742 0.0031 0.0119 -0.0051 273 PRO A CG 1790 C CD . PRO A 232 ? 0.2411 0.2724 0.2713 0.0028 0.0066 -0.0073 273 PRO A CD 1791 N N . ALA A 233 ? 0.2247 0.2493 0.2613 -0.0028 0.0036 -0.0163 274 ALA A N 1792 C CA . ALA A 233 ? 0.2309 0.2544 0.2752 -0.0050 0.0004 -0.0202 274 ALA A CA 1793 C C . ALA A 233 ? 0.2448 0.2675 0.3031 -0.0058 0.0042 -0.0181 274 ALA A C 1794 O O . ALA A 233 ? 0.2656 0.2848 0.3268 -0.0061 0.0064 -0.0185 274 ALA A O 1795 C CB . ALA A 233 ? 0.2552 0.2756 0.2916 -0.0049 -0.0003 -0.0234 274 ALA A CB 1796 N N . ASN A 234 ? 0.2476 0.2732 0.3144 -0.0059 0.0055 -0.0155 275 ASN A N 1797 C CA . ASN A 234 ? 0.2676 0.2929 0.3491 -0.0066 0.0103 -0.0125 275 ASN A CA 1798 C C . ASN A 234 ? 0.2827 0.3089 0.3793 -0.0098 0.0060 -0.0162 275 ASN A C 1799 O O . ASN A 234 ? 0.2680 0.2938 0.3615 -0.0110 -0.0009 -0.0216 275 ASN A O 1800 C CB . ASN A 234 ? 0.2850 0.3132 0.3685 -0.0047 0.0148 -0.0077 275 ASN A CB 1801 C CG . ASN A 234 ? 0.2601 0.2930 0.3464 -0.0052 0.0099 -0.0094 275 ASN A CG 1802 O OD1 . ASN A 234 ? 0.2891 0.3234 0.3807 -0.0073 0.0034 -0.0137 275 ASN A OD1 1803 N ND2 . ASN A 234 ? 0.2922 0.3270 0.3739 -0.0027 0.0125 -0.0061 275 ASN A ND2 1804 N N . GLU A 235 ? 0.3011 0.3281 0.4143 -0.0110 0.0101 -0.0135 276 GLU A N 1805 C CA A GLU A 235 ? 0.3332 0.3603 0.4631 -0.0143 0.0060 -0.0174 276 GLU A CA 1806 C CA B GLU A 235 ? 0.3268 0.3543 0.4582 -0.0143 0.0066 -0.0169 276 GLU A CA 1807 C C . GLU A 235 ? 0.3345 0.3662 0.4705 -0.0155 -0.0019 -0.0215 276 GLU A C 1808 O O . GLU A 235 ? 0.3701 0.4013 0.5151 -0.0178 -0.0086 -0.0269 276 GLU A O 1809 C CB A GLU A 235 ? 0.3534 0.3797 0.5012 -0.0155 0.0132 -0.0130 276 GLU A CB 1810 C CB B GLU A 235 ? 0.3325 0.3611 0.4821 -0.0152 0.0138 -0.0119 276 GLU A CB 1811 C CG A GLU A 235 ? 0.4076 0.4275 0.5530 -0.0153 0.0178 -0.0113 276 GLU A CG 1812 C CG B GLU A 235 ? 0.3602 0.3837 0.5177 -0.0164 0.0184 -0.0103 276 GLU A CG 1813 C CD A GLU A 235 ? 0.4396 0.4566 0.5971 -0.0186 0.0132 -0.0164 276 GLU A CD 1814 C CD B GLU A 235 ? 0.3703 0.3895 0.5146 -0.0132 0.0265 -0.0046 276 GLU A CD 1815 O OE1 A GLU A 235 ? 0.5085 0.5279 0.6740 -0.0208 0.0052 -0.0222 276 GLU A OE1 1816 O OE1 B GLU A 235 ? 0.4056 0.4268 0.5398 -0.0102 0.0298 -0.0009 276 GLU A OE1 1817 O OE2 A GLU A 235 ? 0.4999 0.5115 0.6590 -0.0187 0.0173 -0.0147 276 GLU A OE2 1818 O OE2 B GLU A 235 ? 0.3602 0.3740 0.5045 -0.0134 0.0289 -0.0039 276 GLU A OE2 1819 N N . TYR A 236 ? 0.3095 0.3452 0.4406 -0.0137 -0.0019 -0.0194 277 TYR A N 1820 C CA . TYR A 236 ? 0.3068 0.3466 0.4434 -0.0144 -0.0098 -0.0231 277 TYR A CA 1821 C C . TYR A 236 ? 0.3170 0.3561 0.4349 -0.0128 -0.0159 -0.0258 277 TYR A C 1822 O O . TYR A 236 ? 0.3141 0.3561 0.4330 -0.0125 -0.0221 -0.0278 277 TYR A O 1823 C CB . TYR A 236 ? 0.3171 0.3623 0.4672 -0.0139 -0.0063 -0.0193 277 TYR A CB 1824 C CG . TYR A 236 ? 0.2985 0.3440 0.4370 -0.0108 0.0005 -0.0139 277 TYR A CG 1825 C CD1 . TYR A 236 ? 0.3009 0.3480 0.4271 -0.0087 -0.0032 -0.0144 277 TYR A CD1 1826 C CD2 . TYR A 236 ? 0.2869 0.3305 0.4263 -0.0096 0.0103 -0.0085 277 TYR A CD2 1827 C CE1 . TYR A 236 ? 0.3334 0.3803 0.4487 -0.0057 0.0024 -0.0100 277 TYR A CE1 1828 C CE2 . TYR A 236 ? 0.3211 0.3643 0.4480 -0.0061 0.0158 -0.0042 277 TYR A CE2 1829 C CZ . TYR A 236 ? 0.3240 0.3690 0.4395 -0.0043 0.0114 -0.0054 277 TYR A CZ 1830 O OH . TYR A 236 ? 0.3623 0.4067 0.4663 -0.0009 0.0157 -0.0019 277 TYR A OH 1831 N N . ALA A 237 ? 0.3090 0.3441 0.4104 -0.0117 -0.0142 -0.0258 278 ALA A N 1832 C CA . ALA A 237 ? 0.3102 0.3445 0.3937 -0.0102 -0.0181 -0.0273 278 ALA A CA 1833 C C . ALA A 237 ? 0.3300 0.3637 0.4122 -0.0109 -0.0273 -0.0331 278 ALA A C 1834 O O . ALA A 237 ? 0.3455 0.3774 0.4358 -0.0126 -0.0308 -0.0373 278 ALA A O 1835 C CB . ALA A 237 ? 0.3150 0.3453 0.3844 -0.0093 -0.0144 -0.0268 278 ALA A CB 1836 N N . TYR A 238 ? 0.3261 0.3608 0.3982 -0.0095 -0.0316 -0.0333 279 TYR A N 1837 C CA . TYR A 238 ? 0.3510 0.3837 0.4160 -0.0092 -0.0404 -0.0385 279 TYR A CA 1838 C C . TYR A 238 ? 0.3477 0.3762 0.3930 -0.0080 -0.0392 -0.0393 279 TYR A C 1839 O O . TYR A 238 ? 0.3884 0.4169 0.4237 -0.0070 -0.0344 -0.0355 279 TYR A O 1840 C CB . TYR A 238 ? 0.3677 0.4032 0.4333 -0.0080 -0.0464 -0.0384 279 TYR A CB 1841 C CG A TYR A 238 ? 0.3339 0.3666 0.3924 -0.0072 -0.0563 -0.0439 279 TYR A CG 1842 C CG B TYR A 238 ? 0.4218 0.4536 0.4692 -0.0063 -0.0527 -0.0412 279 TYR A CG 1843 C CD1 A TYR A 238 ? 0.3259 0.3591 0.3976 -0.0083 -0.0634 -0.0490 279 TYR A CD1 1844 C CD1 B TYR A 238 ? 0.4520 0.4822 0.4997 -0.0058 -0.0623 -0.0465 279 TYR A CD1 1845 C CD2 A TYR A 238 ? 0.3509 0.3801 0.3889 -0.0052 -0.0585 -0.0440 279 TYR A CD2 1846 C CD2 B TYR A 238 ? 0.4407 0.4700 0.4705 -0.0050 -0.0489 -0.0386 279 TYR A CD2 1847 C CE1 A TYR A 238 ? 0.3785 0.4084 0.4418 -0.0069 -0.0732 -0.0545 279 TYR A CE1 1848 C CE1 B TYR A 238 ? 0.4919 0.5177 0.5206 -0.0036 -0.0674 -0.0486 279 TYR A CE1 1849 C CE2 A TYR A 238 ? 0.3748 0.4005 0.4038 -0.0038 -0.0671 -0.0488 279 TYR A CE2 1850 C CE2 B TYR A 238 ? 0.4980 0.5236 0.5111 -0.0034 -0.0532 -0.0403 279 TYR A CE2 1851 C CZ A TYR A 238 ? 0.3758 0.4017 0.4168 -0.0044 -0.0748 -0.0542 279 TYR A CZ 1852 C CZ B TYR A 238 ? 0.5032 0.5267 0.5146 -0.0025 -0.0621 -0.0451 279 TYR A CZ 1853 O OH A TYR A 238 ? 0.4399 0.4616 0.4704 -0.0024 -0.0842 -0.0594 279 TYR A OH 1854 O OH B TYR A 238 ? 0.5541 0.5729 0.5463 -0.0003 -0.0655 -0.0461 279 TYR A OH 1855 N N . ARG A 239 ? 0.3415 0.3663 0.3826 -0.0082 -0.0431 -0.0443 280 ARG A N 1856 C CA . ARG A 239 ? 0.3471 0.3681 0.3716 -0.0071 -0.0409 -0.0453 280 ARG A CA 1857 C C . ARG A 239 ? 0.3764 0.3944 0.3849 -0.0052 -0.0468 -0.0482 280 ARG A C 1858 O O . ARG A 239 ? 0.3874 0.4040 0.3975 -0.0049 -0.0548 -0.0527 280 ARG A O 1859 C CB A ARG A 239 ? 0.3486 0.3667 0.3780 -0.0081 -0.0391 -0.0484 280 ARG A CB 1860 C CB B ARG A 239 ? 0.3429 0.3607 0.3716 -0.0080 -0.0404 -0.0493 280 ARG A CB 1861 C CG A ARG A 239 ? 0.3314 0.3515 0.3731 -0.0093 -0.0316 -0.0439 280 ARG A CG 1862 C CG B ARG A 239 ? 0.3053 0.3234 0.3399 -0.0088 -0.0322 -0.0456 280 ARG A CG 1863 C CD A ARG A 239 ? 0.3477 0.3647 0.3959 -0.0103 -0.0291 -0.0459 280 ARG A CD 1864 C CD B ARG A 239 ? 0.2630 0.2777 0.3041 -0.0097 -0.0321 -0.0494 280 ARG A CD 1865 N NE A ARG A 239 ? 0.3313 0.3493 0.3845 -0.0103 -0.0209 -0.0404 280 ARG A NE 1866 N NE B ARG A 239 ? 0.2500 0.2655 0.2990 -0.0103 -0.0246 -0.0447 280 ARG A NE 1867 C CZ A ARG A 239 ? 0.3046 0.3246 0.3719 -0.0113 -0.0173 -0.0367 280 ARG A CZ 1868 C CZ B ARG A 239 ? 0.2323 0.2497 0.2972 -0.0118 -0.0223 -0.0419 280 ARG A CZ 1869 N NH1 A ARG A 239 ? 0.3786 0.4009 0.4600 -0.0130 -0.0209 -0.0378 280 ARG A NH1 1870 N NH1 B ARG A 239 ? 0.1777 0.1973 0.2550 -0.0133 -0.0274 -0.0439 280 ARG A NH1 1871 N NH2 A ARG A 239 ? 0.2679 0.2874 0.3354 -0.0105 -0.0100 -0.0318 280 ARG A NH2 1872 N NH2 B ARG A 239 ? 0.2336 0.2507 0.3022 -0.0115 -0.0150 -0.0373 280 ARG A NH2 1873 N N . ARG A 240 ? 0.3720 0.3887 0.3651 -0.0039 -0.0431 -0.0457 281 ARG A N 1874 C CA . ARG A 240 ? 0.4161 0.4285 0.3922 -0.0018 -0.0472 -0.0485 281 ARG A CA 1875 C C . ARG A 240 ? 0.4410 0.4493 0.4145 -0.0013 -0.0507 -0.0550 281 ARG A C 1876 O O . ARG A 240 ? 0.4212 0.4290 0.4013 -0.0024 -0.0472 -0.0564 281 ARG A O 1877 C CB . ARG A 240 ? 0.4109 0.4222 0.3725 -0.0008 -0.0411 -0.0450 281 ARG A CB 1878 C CG . ARG A 240 ? 0.4302 0.4447 0.3934 -0.0010 -0.0387 -0.0392 281 ARG A CG 1879 C CD . ARG A 240 ? 0.4371 0.4504 0.3875 -0.0002 -0.0335 -0.0359 281 ARG A CD 1880 N NE . ARG A 240 ? 0.4519 0.4671 0.4029 -0.0002 -0.0330 -0.0311 281 ARG A NE 1881 C CZ . ARG A 240 ? 0.5109 0.5249 0.4523 0.0003 -0.0297 -0.0276 281 ARG A CZ 1882 N NH1 . ARG A 240 ? 0.5383 0.5499 0.4693 0.0008 -0.0261 -0.0281 281 ARG A NH1 1883 N NH2 . ARG A 240 ? 0.5569 0.5723 0.5001 0.0003 -0.0298 -0.0237 281 ARG A NH2 1884 N N . GLY A 241 ? 0.4740 0.4785 0.4369 0.0008 -0.0581 -0.0589 282 GLY A N 1885 C CA . GLY A 241 ? 0.5296 0.5287 0.4839 0.0023 -0.0613 -0.0654 282 GLY A CA 1886 C C . GLY A 241 ? 0.5482 0.5453 0.4891 0.0035 -0.0533 -0.0639 282 GLY A C 1887 O O . GLY A 241 ? 0.5499 0.5488 0.4845 0.0036 -0.0475 -0.0583 282 GLY A O 1888 N N . ILE A 242 ? 0.5787 0.5720 0.5164 0.0043 -0.0529 -0.0689 283 ILE A N 1889 C CA . ILE A 242 ? 0.5916 0.5833 0.5178 0.0057 -0.0451 -0.0679 283 ILE A CA 1890 C C . ILE A 242 ? 0.6059 0.5955 0.5124 0.0083 -0.0431 -0.0653 283 ILE A C 1891 O O . ILE A 242 ? 0.5985 0.5898 0.5005 0.0083 -0.0352 -0.0609 283 ILE A O 1892 C CB A ILE A 242 ? 0.6022 0.5893 0.5268 0.0070 -0.0460 -0.0748 283 ILE A CB 1893 C CB B ILE A 242 ? 0.6002 0.5873 0.5247 0.0070 -0.0458 -0.0747 283 ILE A CB 1894 C CG1 A ILE A 242 ? 0.5975 0.5853 0.5203 0.0073 -0.0366 -0.0730 283 ILE A CG1 1895 C CG1 B ILE A 242 ? 0.5883 0.5775 0.5329 0.0042 -0.0450 -0.0756 283 ILE A CG1 1896 C CG2 A ILE A 242 ? 0.6286 0.6091 0.5358 0.0107 -0.0523 -0.0808 283 ILE A CG2 1897 C CG2 B ILE A 242 ? 0.6068 0.5922 0.5180 0.0091 -0.0379 -0.0741 283 ILE A CG2 1898 C CD1 A ILE A 242 ? 0.5542 0.5468 0.4940 0.0043 -0.0318 -0.0689 283 ILE A CD1 1899 C CD1 B ILE A 242 ? 0.5648 0.5586 0.5174 0.0024 -0.0363 -0.0693 283 ILE A CD1 1900 N N . ALA A 243 ? 0.6304 0.6161 0.5259 0.0106 -0.0504 -0.0676 284 ALA A N 1901 C CA . ALA A 243 ? 0.6482 0.6307 0.5237 0.0133 -0.0483 -0.0646 284 ALA A CA 1902 C C . ALA A 243 ? 0.6430 0.6297 0.5207 0.0117 -0.0434 -0.0565 284 ALA A C 1903 O O . ALA A 243 ? 0.6503 0.6352 0.5145 0.0131 -0.0383 -0.0527 284 ALA A O 1904 C CB . ALA A 243 ? 0.6693 0.6460 0.5320 0.0166 -0.0581 -0.0687 284 ALA A CB 1905 N N . GLU A 244 ? 0.6207 0.6128 0.5157 0.0087 -0.0445 -0.0540 285 GLU A N 1906 C CA . GLU A 244 ? 0.6109 0.6066 0.5090 0.0073 -0.0408 -0.0471 285 GLU A CA 1907 C C . GLU A 244 ? 0.5843 0.5850 0.4945 0.0048 -0.0331 -0.0439 285 GLU A C 1908 O O . GLU A 244 ? 0.5840 0.5880 0.4990 0.0035 -0.0301 -0.0388 285 GLU A O 1909 C CB . GLU A 244 ? 0.6132 0.6110 0.5201 0.0067 -0.0479 -0.0462 285 GLU A CB 1910 C CG . GLU A 244 ? 0.6697 0.6626 0.5630 0.0097 -0.0557 -0.0477 285 GLU A CG 1911 C CD . GLU A 244 ? 0.7471 0.7358 0.6368 0.0116 -0.0635 -0.0553 285 GLU A CD 1912 O OE1 . GLU A 244 ? 0.7449 0.7359 0.6493 0.0098 -0.0655 -0.0594 285 GLU A OE1 1913 O OE2 . GLU A 244 ? 0.8059 0.7885 0.6775 0.0152 -0.0676 -0.0572 285 GLU A OE2 1914 N N . ALA A 245 ? 0.5644 0.5650 0.4786 0.0045 -0.0302 -0.0472 286 ALA A N 1915 C CA . ALA A 245 ? 0.5383 0.5430 0.4639 0.0026 -0.0239 -0.0447 286 ALA A CA 1916 C C . ALA A 245 ? 0.5399 0.5459 0.4593 0.0028 -0.0171 -0.0399 286 ALA A C 1917 O O . ALA A 245 ? 0.5294 0.5326 0.4352 0.0043 -0.0156 -0.0391 286 ALA A O 1918 C CB . ALA A 245 ? 0.5357 0.5392 0.4659 0.0027 -0.0225 -0.0491 286 ALA A CB 1919 N N . VAL A 246 ? 0.5063 0.5164 0.4360 0.0012 -0.0130 -0.0366 287 VAL A N 1920 C CA . VAL A 246 ? 0.5106 0.5224 0.4376 0.0011 -0.0073 -0.0325 287 VAL A CA 1921 C C . VAL A 246 ? 0.4983 0.5104 0.4247 0.0017 -0.0017 -0.0340 287 VAL A C 1922 O O . VAL A 246 ? 0.4925 0.5055 0.4270 0.0015 -0.0011 -0.0362 287 VAL A O 1923 C CB . VAL A 246 ? 0.4904 0.5061 0.4279 -0.0003 -0.0063 -0.0285 287 VAL A CB 1924 C CG1 . VAL A 246 ? 0.4976 0.5150 0.4336 -0.0006 -0.0009 -0.0248 287 VAL A CG1 1925 C CG2 . VAL A 246 ? 0.5286 0.5442 0.4670 -0.0007 -0.0113 -0.0269 287 VAL A CG2 1926 N N . GLY A 247 ? 0.4921 0.5032 0.4091 0.0026 0.0025 -0.0328 288 GLY A N 1927 C CA . GLY A 247 ? 0.4808 0.4937 0.3997 0.0031 0.0089 -0.0330 288 GLY A CA 1928 C C . GLY A 247 ? 0.4829 0.4931 0.3964 0.0050 0.0107 -0.0378 288 GLY A C 1929 O O . GLY A 247 ? 0.4821 0.4943 0.3985 0.0056 0.0163 -0.0381 288 GLY A O 1930 N N . LEU A 248 ? 0.4816 0.4876 0.3880 0.0062 0.0058 -0.0418 289 LEU A N 1931 C CA . LEU A 248 ? 0.4850 0.4879 0.3871 0.0083 0.0065 -0.0474 289 LEU A CA 1932 C C . LEU A 248 ? 0.4924 0.4928 0.3804 0.0108 0.0118 -0.0477 289 LEU A C 1933 O O . LEU A 248 ? 0.5083 0.5061 0.3844 0.0117 0.0114 -0.0456 289 LEU A O 1934 C CB A LEU A 248 ? 0.4879 0.4867 0.3882 0.0089 -0.0013 -0.0525 289 LEU A CB 1935 C CB B LEU A 248 ? 0.4896 0.4884 0.3901 0.0089 -0.0013 -0.0524 289 LEU A CB 1936 C CG A LEU A 248 ? 0.4913 0.4918 0.4059 0.0066 -0.0065 -0.0528 289 LEU A CG 1937 C CG B LEU A 248 ? 0.4897 0.4896 0.4050 0.0073 -0.0044 -0.0548 289 LEU A CG 1938 C CD1 A LEU A 248 ? 0.5029 0.4991 0.4159 0.0074 -0.0139 -0.0586 289 LEU A CD1 1939 C CD1 B LEU A 248 ? 0.4740 0.4782 0.4015 0.0047 -0.0054 -0.0500 289 LEU A CD1 1940 C CD2 A LEU A 248 ? 0.4898 0.4933 0.4180 0.0055 -0.0029 -0.0521 289 LEU A CD2 1941 C CD2 B LEU A 248 ? 0.5045 0.4998 0.4179 0.0081 -0.0117 -0.0607 289 LEU A CD2 1942 N N . PRO A 249 ? 0.4940 0.4949 0.3831 0.0123 0.0171 -0.0502 290 PRO A N 1943 C CA . PRO A 249 ? 0.4981 0.4968 0.3742 0.0150 0.0234 -0.0504 290 PRO A CA 1944 C C . PRO A 249 ? 0.5150 0.5066 0.3746 0.0181 0.0193 -0.0551 290 PRO A C 1945 O O . PRO A 249 ? 0.5017 0.4905 0.3631 0.0184 0.0124 -0.0601 290 PRO A O 1946 C CB . PRO A 249 ? 0.5100 0.5110 0.3935 0.0162 0.0291 -0.0529 290 PRO A CB 1947 C CG . PRO A 249 ? 0.5042 0.5071 0.4023 0.0145 0.0247 -0.0546 290 PRO A CG 1948 C CD . PRO A 249 ? 0.4863 0.4901 0.3893 0.0117 0.0184 -0.0518 290 PRO A CD 1949 N N . SER A 250 ? 0.5215 0.5098 0.3652 0.0206 0.0238 -0.0536 291 SER A N 1950 C CA . SER A 250 ? 0.5485 0.5292 0.3731 0.0243 0.0196 -0.0577 291 SER A CA 1951 C C . SER A 250 ? 0.5455 0.5223 0.3593 0.0286 0.0246 -0.0627 291 SER A C 1952 O O . SER A 250 ? 0.5569 0.5264 0.3529 0.0326 0.0214 -0.0671 291 SER A O 1953 C CB . SER A 250 ? 0.5799 0.5579 0.3908 0.0250 0.0205 -0.0522 291 SER A CB 1954 O OG . SER A 250 ? 0.6348 0.6146 0.4424 0.0255 0.0314 -0.0473 291 SER A OG 1955 N N . ILE A 251 ? 0.5134 0.4948 0.3372 0.0283 0.0326 -0.0623 292 ILE A N 1956 C CA . ILE A 251 ? 0.5115 0.4898 0.3263 0.0326 0.0387 -0.0669 292 ILE A CA 1957 C C . ILE A 251 ? 0.4960 0.4778 0.3276 0.0318 0.0388 -0.0709 292 ILE A C 1958 O O . ILE A 251 ? 0.4598 0.4477 0.3090 0.0281 0.0386 -0.0676 292 ILE A O 1959 C CB . ILE A 251 ? 0.5136 0.4934 0.3209 0.0343 0.0508 -0.0619 292 ILE A CB 1960 C CG1 . ILE A 251 ? 0.4908 0.4795 0.3170 0.0303 0.0568 -0.0555 292 ILE A CG1 1961 C CG2 . ILE A 251 ? 0.5606 0.5347 0.3475 0.0363 0.0507 -0.0584 292 ILE A CG2 1962 C CD1 . ILE A 251 ? 0.4997 0.4906 0.3221 0.0316 0.0692 -0.0508 292 ILE A CD1 1963 N N . PRO A 252 ? 0.4954 0.4724 0.3208 0.0355 0.0385 -0.0782 293 PRO A N 1964 C CA . PRO A 252 ? 0.4896 0.4692 0.3309 0.0351 0.0389 -0.0818 293 PRO A CA 1965 C C . PRO A 252 ? 0.4776 0.4644 0.3313 0.0345 0.0486 -0.0779 293 PRO A C 1966 O O . PRO A 252 ? 0.4805 0.4689 0.3272 0.0363 0.0572 -0.0749 293 PRO A O 1967 C CB . PRO A 252 ? 0.5119 0.4840 0.3406 0.0401 0.0381 -0.0902 293 PRO A CB 1968 C CG . PRO A 252 ? 0.5389 0.5039 0.3471 0.0422 0.0324 -0.0919 293 PRO A CG 1969 C CD . PRO A 252 ? 0.5182 0.4867 0.3216 0.0408 0.0377 -0.0836 293 PRO A CD 1970 N N . VAL A 253 ? 0.4373 0.4284 0.3095 0.0323 0.0470 -0.0779 294 VAL A N 1971 C CA . VAL A 253 ? 0.4039 0.4024 0.2904 0.0315 0.0541 -0.0743 294 VAL A CA 1972 C C . VAL A 253 ? 0.3957 0.3940 0.2943 0.0325 0.0525 -0.0788 294 VAL A C 1973 O O . VAL A 253 ? 0.3933 0.3880 0.2955 0.0314 0.0449 -0.0815 294 VAL A O 1974 C CB . VAL A 253 ? 0.3944 0.3988 0.2924 0.0270 0.0525 -0.0674 294 VAL A CB 1975 C CG1 . VAL A 253 ? 0.3847 0.3966 0.2974 0.0265 0.0590 -0.0642 294 VAL A CG1 1976 C CG2 . VAL A 253 ? 0.3843 0.3878 0.2708 0.0256 0.0524 -0.0629 294 VAL A CG2 1977 N N . HIS A 254 ? 0.3943 0.3960 0.2994 0.0349 0.0597 -0.0795 295 HIS A N 1978 C CA . HIS A 254 ? 0.3800 0.3813 0.2971 0.0362 0.0583 -0.0834 295 HIS A CA 1979 C C . HIS A 254 ? 0.3716 0.3803 0.3019 0.0371 0.0655 -0.0809 295 HIS A C 1980 O O . HIS A 254 ? 0.3974 0.4095 0.3240 0.0386 0.0734 -0.0792 295 HIS A O 1981 C CB . HIS A 254 ? 0.4072 0.4008 0.3134 0.0405 0.0578 -0.0914 295 HIS A CB 1982 C CG . HIS A 254 ? 0.3910 0.3821 0.3081 0.0417 0.0545 -0.0958 295 HIS A CG 1983 N ND1 . HIS A 254 ? 0.3835 0.3720 0.3088 0.0388 0.0465 -0.0958 295 HIS A ND1 1984 C CD2 . HIS A 254 ? 0.4088 0.3990 0.3302 0.0456 0.0586 -0.1002 295 HIS A CD2 1985 C CE1 . HIS A 254 ? 0.3930 0.3788 0.3269 0.0407 0.0457 -0.0996 295 HIS A CE1 1986 N NE2 . HIS A 254 ? 0.3918 0.3784 0.3233 0.0449 0.0525 -0.1027 295 HIS A NE2 1987 N N . PRO A 255 ? 0.3539 0.3652 0.3001 0.0363 0.0627 -0.0801 296 PRO A N 1988 C CA . PRO A 255 ? 0.3400 0.3584 0.3001 0.0374 0.0682 -0.0782 296 PRO A CA 1989 C C . PRO A 255 ? 0.3563 0.3726 0.3202 0.0419 0.0709 -0.0840 296 PRO A C 1990 O O . PRO A 255 ? 0.3607 0.3702 0.3220 0.0431 0.0661 -0.0886 296 PRO A O 1991 C CB . PRO A 255 ? 0.3234 0.3447 0.2964 0.0343 0.0624 -0.0740 296 PRO A CB 1992 C CG . PRO A 255 ? 0.3352 0.3489 0.3042 0.0335 0.0548 -0.0766 296 PRO A CG 1993 C CD . PRO A 255 ? 0.3417 0.3497 0.2940 0.0341 0.0545 -0.0803 296 PRO A CD 1994 N N . ILE A 256 ? 0.3568 0.3791 0.3281 0.0443 0.0785 -0.0837 297 ILE A N 1995 C CA . ILE A 256 ? 0.3596 0.3810 0.3364 0.0491 0.0820 -0.0889 297 ILE A CA 1996 C C . ILE A 256 ? 0.3591 0.3893 0.3547 0.0498 0.0855 -0.0863 297 ILE A C 1997 O O . ILE A 256 ? 0.3606 0.3977 0.3633 0.0470 0.0868 -0.0809 297 ILE A O 1998 C CB . ILE A 256 ? 0.3877 0.4061 0.3506 0.0531 0.0895 -0.0935 297 ILE A CB 1999 C CG1 . ILE A 256 ? 0.3925 0.4180 0.3549 0.0527 0.0987 -0.0891 297 ILE A CG1 2000 C CG2 . ILE A 256 ? 0.4039 0.4126 0.3478 0.0532 0.0844 -0.0974 297 ILE A CG2 2001 C CD1 . ILE A 256 ? 0.4107 0.4334 0.3590 0.0574 0.1077 -0.0929 297 ILE A CD1 2002 N N . GLY A 257 ? 0.3513 0.3810 0.3553 0.0539 0.0866 -0.0904 298 GLY A N 2003 C CA . GLY A 257 ? 0.3519 0.3897 0.3741 0.0556 0.0899 -0.0890 298 GLY A CA 2004 C C . GLY A 257 ? 0.3680 0.4114 0.3922 0.0586 0.1006 -0.0904 298 GLY A C 2005 O O . GLY A 257 ? 0.3764 0.4166 0.3856 0.0598 0.1062 -0.0924 298 GLY A O 2006 N N . TYR A 258 ? 0.3564 0.4080 0.3991 0.0602 0.1036 -0.0894 299 TYR A N 2007 C CA . TYR A 258 ? 0.3707 0.4292 0.4185 0.0625 0.1148 -0.0897 299 TYR A CA 2008 C C . TYR A 258 ? 0.3912 0.4465 0.4349 0.0685 0.1211 -0.0961 299 TYR A C 2009 O O . TYR A 258 ? 0.4064 0.4641 0.4451 0.0704 0.1312 -0.0967 299 TYR A O 2010 C CB . TYR A 258 ? 0.3739 0.4439 0.4441 0.0615 0.1168 -0.0858 299 TYR A CB 2011 C CG . TYR A 258 ? 0.3422 0.4154 0.4310 0.0637 0.1110 -0.0871 299 TYR A CG 2012 C CD1 . TYR A 258 ? 0.3402 0.4136 0.4353 0.0609 0.1013 -0.0837 299 TYR A CD1 2013 C CD2 . TYR A 258 ? 0.3735 0.4499 0.4741 0.0691 0.1158 -0.0913 299 TYR A CD2 2014 C CE1 . TYR A 258 ? 0.3511 0.4271 0.4621 0.0634 0.0956 -0.0843 299 TYR A CE1 2015 C CE2 . TYR A 258 ? 0.3608 0.4400 0.4788 0.0715 0.1100 -0.0921 299 TYR A CE2 2016 C CZ . TYR A 258 ? 0.3227 0.4014 0.4451 0.0687 0.0997 -0.0885 299 TYR A CZ 2017 O OH . TYR A 258 ? 0.3276 0.4082 0.4652 0.0718 0.0937 -0.0892 299 TYR A OH 2018 N N . TYR A 259 ? 0.3825 0.4317 0.4268 0.0715 0.1157 -0.1009 300 TYR A N 2019 C CA . TYR A 259 ? 0.4095 0.4537 0.4463 0.0773 0.1214 -0.1078 300 TYR A CA 2020 C C . TYR A 259 ? 0.4278 0.4645 0.4400 0.0773 0.1243 -0.1098 300 TYR A C 2021 O O . TYR A 259 ? 0.4426 0.4794 0.4470 0.0812 0.1338 -0.1126 300 TYR A O 2022 C CB . TYR A 259 ? 0.4157 0.4527 0.4558 0.0804 0.1143 -0.1128 300 TYR A CB 2023 C CG . TYR A 259 ? 0.4142 0.4569 0.4764 0.0826 0.1124 -0.1124 300 TYR A CG 2024 C CD1 . TYR A 259 ? 0.4619 0.5163 0.5414 0.0837 0.1189 -0.1100 300 TYR A CD1 2025 C CD2 . TYR A 259 ? 0.4547 0.4907 0.5212 0.0841 0.1042 -0.1146 300 TYR A CD2 2026 C CE1 . TYR A 259 ? 0.4536 0.5130 0.5536 0.0863 0.1161 -0.1101 300 TYR A CE1 2027 C CE2 . TYR A 259 ? 0.4621 0.5024 0.5478 0.0869 0.1020 -0.1142 300 TYR A CE2 2028 C CZ . TYR A 259 ? 0.4655 0.5176 0.5676 0.0882 0.1075 -0.1122 300 TYR A CZ 2029 O OH . TYR A 259 ? 0.4649 0.5210 0.5860 0.0914 0.1043 -0.1122 300 TYR A OH 2030 N N . ASP A 260 ? 0.4209 0.4512 0.4210 0.0733 0.1162 -0.1085 301 ASP A N 2031 C CA . ASP A 260 ? 0.4453 0.4683 0.4223 0.0733 0.1171 -0.1103 301 ASP A CA 2032 C C . ASP A 260 ? 0.4475 0.4756 0.4178 0.0716 0.1252 -0.1051 301 ASP A C 2033 O O . ASP A 260 ? 0.4639 0.4880 0.4171 0.0746 0.1316 -0.1074 301 ASP A O 2034 C CB . ASP A 260 ? 0.4390 0.4545 0.4074 0.0694 0.1058 -0.1100 301 ASP A CB 2035 C CG . ASP A 260 ? 0.4651 0.4723 0.4344 0.0717 0.0988 -0.1163 301 ASP A CG 2036 O OD1 . ASP A 260 ? 0.5176 0.5223 0.4874 0.0770 0.1030 -0.1222 301 ASP A OD1 2037 O OD2 . ASP A 260 ? 0.4610 0.4636 0.4304 0.0681 0.0894 -0.1153 301 ASP A OD2 2038 N N . ALA A 261 ? 0.4260 0.4624 0.4093 0.0671 0.1250 -0.0982 302 ALA A N 2039 C CA . ALA A 261 ? 0.4404 0.4822 0.4205 0.0651 0.1332 -0.0926 302 ALA A CA 2040 C C . ALA A 261 ? 0.4550 0.5011 0.4372 0.0698 0.1466 -0.0941 302 ALA A C 2041 O O . ALA A 261 ? 0.4830 0.5277 0.4509 0.0708 0.1549 -0.0923 302 ALA A O 2042 C CB . ALA A 261 ? 0.4145 0.4649 0.4122 0.0599 0.1306 -0.0858 302 ALA A CB 2043 N N . GLN A 262 ? 0.4502 0.5016 0.4506 0.0729 0.1490 -0.0969 303 GLN A N 2044 C CA . GLN A 262 ? 0.4795 0.5357 0.4852 0.0780 0.1620 -0.0988 303 GLN A CA 2045 C C . GLN A 262 ? 0.5095 0.5566 0.4904 0.0831 0.1680 -0.1038 303 GLN A C 2046 O O . GLN A 262 ? 0.5187 0.5678 0.4927 0.0855 0.1801 -0.1022 303 GLN A O 2047 C CB . GLN A 262 ? 0.4729 0.5336 0.4995 0.0814 0.1606 -0.1028 303 GLN A CB 2048 C CG . GLN A 262 ? 0.5264 0.5934 0.5627 0.0870 0.1739 -0.1052 303 GLN A CG 2049 C CD . GLN A 262 ? 0.5656 0.6460 0.6303 0.0848 0.1769 -0.1006 303 GLN A CD 2050 O OE1 . GLN A 262 ? 0.6472 0.7345 0.7169 0.0826 0.1857 -0.0954 303 GLN A OE1 2051 N NE2 . GLN A 262 ? 0.5489 0.6326 0.6324 0.0851 0.1689 -0.1021 303 GLN A NE2 2052 N N . LYS A 263 ? 0.5203 0.5570 0.4876 0.0849 0.1594 -0.1098 304 LYS A N 2053 C CA . LYS A 263 ? 0.5434 0.5700 0.4861 0.0902 0.1628 -0.1158 304 LYS A CA 2054 C C . LYS A 263 ? 0.5567 0.5792 0.4773 0.0884 0.1653 -0.1119 304 LYS A C 2055 O O . LYS A 263 ? 0.5886 0.6057 0.4896 0.0933 0.1731 -0.1145 304 LYS A O 2056 C CB . LYS A 263 ? 0.5499 0.5661 0.4850 0.0915 0.1512 -0.1229 304 LYS A CB 2057 C CG . LYS A 263 ? 0.5682 0.5859 0.5212 0.0946 0.1493 -0.1277 304 LYS A CG 2058 C CD . LYS A 263 ? 0.6361 0.6508 0.5822 0.1026 0.1586 -0.1348 304 LYS A CD 2059 C CE . LYS A 263 ? 0.6993 0.7213 0.6700 0.1053 0.1615 -0.1362 304 LYS A CE 2060 N NZ . LYS A 263 ? 0.7166 0.7524 0.7070 0.1026 0.1689 -0.1287 304 LYS A NZ 2061 N N . LEU A 264 ? 0.5304 0.5548 0.4532 0.0819 0.1586 -0.1057 305 LEU A N 2062 C CA . LEU A 264 ? 0.5475 0.5679 0.4505 0.0800 0.1601 -0.1014 305 LEU A CA 2063 C C . LEU A 264 ? 0.5537 0.5820 0.4613 0.0792 0.1733 -0.0942 305 LEU A C 2064 O O . LEU A 264 ? 0.5917 0.6153 0.4790 0.0812 0.1801 -0.0922 305 LEU A O 2065 C CB . LEU A 264 ? 0.5186 0.5373 0.4218 0.0735 0.1474 -0.0979 305 LEU A CB 2066 C CG . LEU A 264 ? 0.5218 0.5314 0.4172 0.0737 0.1345 -0.1042 305 LEU A CG 2067 C CD1 . LEU A 264 ? 0.4906 0.4998 0.3878 0.0673 0.1237 -0.0998 305 LEU A CD1 2068 C CD2 . LEU A 264 ? 0.5717 0.5700 0.4408 0.0789 0.1345 -0.1106 305 LEU A CD2 2069 N N . LEU A 265 ? 0.5288 0.5684 0.4627 0.0765 0.1767 -0.0902 306 LEU A N 2070 C CA . LEU A 265 ? 0.5242 0.5719 0.4665 0.0747 0.1884 -0.0829 306 LEU A CA 2071 C C . LEU A 265 ? 0.5534 0.6041 0.4967 0.0807 0.2039 -0.0845 306 LEU A C 2072 O O . LEU A 265 ? 0.5602 0.6145 0.5023 0.0805 0.2159 -0.0788 306 LEU A O 2073 C CB . LEU A 265 ? 0.4972 0.5560 0.4687 0.0693 0.1852 -0.0782 306 LEU A CB 2074 C CG . LEU A 265 ? 0.4658 0.5229 0.4381 0.0632 0.1713 -0.0754 306 LEU A CG 2075 C CD1 . LEU A 265 ? 0.4704 0.5377 0.4712 0.0589 0.1669 -0.0721 306 LEU A CD1 2076 C CD2 . LEU A 265 ? 0.4862 0.5390 0.4411 0.0601 0.1725 -0.0696 306 LEU A CD2 2077 N N . GLU A 266 ? 0.5680 0.6175 0.5146 0.0860 0.2041 -0.0920 307 GLU A N 2078 C CA . GLU A 266 ? 0.5921 0.6471 0.5469 0.0915 0.2187 -0.0936 307 GLU A CA 2079 C C . GLU A 266 ? 0.6293 0.6781 0.5587 0.0965 0.2317 -0.0931 307 GLU A C 2080 O O . GLU A 266 ? 0.6415 0.6964 0.5781 0.0995 0.2467 -0.0909 307 GLU A O 2081 C CB . GLU A 266 ? 0.5832 0.6382 0.5484 0.0963 0.2157 -0.1019 307 GLU A CB 2082 C CG . GLU A 266 ? 0.6210 0.6628 0.5619 0.1013 0.2099 -0.1102 307 GLU A CG 2083 C CD . GLU A 266 ? 0.6733 0.7150 0.6274 0.1050 0.2050 -0.1177 307 GLU A CD 2084 O OE1 . GLU A 266 ? 0.6951 0.7471 0.6770 0.1037 0.2057 -0.1161 307 GLU A OE1 2085 O OE2 . GLU A 266 ? 0.6881 0.7189 0.6250 0.1094 0.2003 -0.1254 307 GLU A OE2 2086 N N . LYS A 267 ? 0.6517 0.6883 0.5515 0.0975 0.2259 -0.0949 308 LYS A N 2087 C CA . LYS A 267 ? 0.6828 0.7115 0.5543 0.1029 0.2367 -0.0947 308 LYS A CA 2088 C C . LYS A 267 ? 0.6884 0.7173 0.5514 0.0986 0.2412 -0.0850 308 LYS A C 2089 O O . LYS A 267 ? 0.6954 0.7180 0.5349 0.1027 0.2511 -0.0829 308 LYS A O 2090 C CB . LYS A 267 ? 0.7055 0.7198 0.5480 0.1077 0.2278 -0.1032 308 LYS A CB 2091 C CG . LYS A 267 ? 0.7222 0.7342 0.5676 0.1141 0.2277 -0.1132 308 LYS A CG 2092 C CD . LYS A 267 ? 0.7379 0.7371 0.5644 0.1161 0.2133 -0.1217 308 LYS A CD 2093 C CE . LYS A 267 ? 0.7693 0.7646 0.5956 0.1235 0.2148 -0.1319 308 LYS A CE 2094 N NZ . LYS A 267 ? 0.7956 0.7775 0.6028 0.1258 0.2013 -0.1408 308 LYS A NZ 2095 N N . MET A 268 ? 0.6600 0.6957 0.5414 0.0906 0.2342 -0.0789 309 MET A N 2096 C CA . MET A 268 ? 0.6726 0.7077 0.5464 0.0862 0.2371 -0.0698 309 MET A CA 2097 C C . MET A 268 ? 0.6967 0.7353 0.5694 0.0883 0.2563 -0.0630 309 MET A C 2098 O O . MET A 268 ? 0.6902 0.7391 0.5864 0.0888 0.2668 -0.0618 309 MET A O 2099 C CB . MET A 268 ? 0.6443 0.6862 0.5395 0.0777 0.2263 -0.0650 309 MET A CB 2100 C CG A MET A 268 ? 0.6316 0.6658 0.5162 0.0760 0.2085 -0.0699 309 MET A CG 2101 C CG B MET A 268 ? 0.6487 0.6854 0.5399 0.0752 0.2084 -0.0696 309 MET A CG 2102 S SD A MET A 268 ? 0.5798 0.6156 0.4724 0.0673 0.1948 -0.0642 309 MET A SD 2103 S SD B MET A 268 ? 0.6773 0.7014 0.5356 0.0746 0.2021 -0.0673 309 MET A SD 2104 C CE A MET A 268 ? 0.5988 0.6297 0.4711 0.0661 0.2023 -0.0555 309 MET A CE 2105 C CE B MET A 268 ? 0.6830 0.7134 0.5507 0.0685 0.2091 -0.0552 309 MET A CE 2106 N N . GLY A 269 ? 0.7207 0.7504 0.5661 0.0897 0.2606 -0.0586 310 GLY A N 2107 C CA . GLY A 269 ? 0.7419 0.7726 0.5815 0.0919 0.2792 -0.0512 310 GLY A CA 2108 C C . GLY A 269 ? 0.7484 0.7798 0.5890 0.0856 0.2805 -0.0406 310 GLY A C 2109 O O . GLY A 269 ? 0.7197 0.7575 0.5814 0.0782 0.2707 -0.0377 310 GLY A O 2110 N N . GLY A 270 ? 0.7782 0.8025 0.5957 0.0889 0.2926 -0.0347 311 GLY A N 2111 C CA . GLY A 270 ? 0.7830 0.8066 0.5998 0.0835 0.2949 -0.0241 311 GLY A CA 2112 C C . GLY A 270 ? 0.7757 0.8137 0.6303 0.0771 0.3029 -0.0174 311 GLY A C 2113 O O . GLY A 270 ? 0.7837 0.8304 0.6573 0.0791 0.3148 -0.0183 311 GLY A O 2114 N N . SER A 271 ? 0.7697 0.8101 0.6358 0.0695 0.2959 -0.0111 312 SER A N 2115 C CA . SER A 271 ? 0.7690 0.8216 0.6697 0.0630 0.3024 -0.0041 312 SER A CA 2116 C C . SER A 271 ? 0.7388 0.8044 0.6753 0.0597 0.2953 -0.0095 312 SER A C 2117 O O . SER A 271 ? 0.7258 0.7906 0.6623 0.0595 0.2802 -0.0167 312 SER A O 2118 C CB . SER A 271 ? 0.7707 0.8202 0.6700 0.0564 0.2959 0.0037 312 SER A CB 2119 O OG . SER A 271 ? 0.7986 0.8584 0.7293 0.0502 0.3031 0.0111 312 SER A OG 2120 N N . ALA A 272 ? 0.7338 0.8113 0.7010 0.0574 0.3064 -0.0058 313 ALA A N 2121 C CA . ALA A 272 ? 0.7017 0.7921 0.7052 0.0540 0.2996 -0.0098 313 ALA A CA 2122 C C . ALA A 272 ? 0.6787 0.7711 0.6951 0.0463 0.2835 -0.0079 313 ALA A C 2123 O O . ALA A 272 ? 0.6796 0.7657 0.6832 0.0429 0.2815 -0.0018 313 ALA A O 2124 C CB . ALA A 272 ? 0.7051 0.8077 0.7391 0.0533 0.3159 -0.0056 313 ALA A CB 2125 N N . PRO A 273 ? 0.6498 0.7503 0.6905 0.0441 0.2720 -0.0132 314 PRO A N 2126 C CA . PRO A 273 ? 0.6314 0.7346 0.6868 0.0371 0.2584 -0.0111 314 PRO A CA 2127 C C . PRO A 273 ? 0.6292 0.7387 0.7054 0.0316 0.2670 -0.0024 314 PRO A C 2128 O O . PRO A 273 ? 0.6342 0.7517 0.7295 0.0323 0.2808 -0.0001 314 PRO A O 2129 C CB . PRO A 273 ? 0.6079 0.7196 0.6872 0.0371 0.2482 -0.0181 314 PRO A CB 2130 C CG . PRO A 273 ? 0.6192 0.7368 0.7084 0.0426 0.2608 -0.0215 314 PRO A CG 2131 C CD . PRO A 273 ? 0.6471 0.7545 0.7034 0.0481 0.2713 -0.0210 314 PRO A CD 2132 N N . PRO A 274 ? 0.6263 0.7321 0.6996 0.0261 0.2592 0.0025 315 PRO A N 2133 C CA . PRO A 274 ? 0.6322 0.7420 0.7229 0.0208 0.2677 0.0111 315 PRO A CA 2134 C C . PRO A 274 ? 0.6235 0.7475 0.7559 0.0171 0.2681 0.0105 315 PRO A C 2135 O O . PRO A 274 ? 0.6256 0.7552 0.7774 0.0141 0.2796 0.0168 315 PRO A O 2136 C CB . PRO A 274 ? 0.6141 0.7163 0.6922 0.0163 0.2557 0.0144 315 PRO A CB 2137 C CG . PRO A 274 ? 0.5983 0.6979 0.6675 0.0176 0.2382 0.0064 315 PRO A CG 2138 C CD . PRO A 274 ? 0.6110 0.7082 0.6648 0.0246 0.2430 0.0004 315 PRO A CD 2139 N N . ASP A 275 ? 0.6160 0.7453 0.7620 0.0176 0.2554 0.0031 316 ASP A N 2140 C CA . ASP A 275 ? 0.6090 0.7514 0.7938 0.0148 0.2522 0.0012 316 ASP A CA 2141 C C . ASP A 275 ? 0.5984 0.7435 0.7879 0.0177 0.2386 -0.0078 316 ASP A C 2142 O O . ASP A 275 ? 0.5875 0.7242 0.7513 0.0210 0.2312 -0.0119 316 ASP A O 2143 C CB . ASP A 275 ? 0.6047 0.7495 0.8074 0.0075 0.2457 0.0060 316 ASP A CB 2144 C CG . ASP A 275 ? 0.6112 0.7485 0.7982 0.0054 0.2280 0.0041 316 ASP A CG 2145 O OD1 . ASP A 275 ? 0.6411 0.7785 0.8258 0.0077 0.2160 -0.0027 316 ASP A OD1 2146 O OD2 . ASP A 275 ? 0.6234 0.7545 0.8009 0.0015 0.2264 0.0096 316 ASP A OD2 2147 N N . SER A 276 ? 0.5816 0.7381 0.8044 0.0164 0.2348 -0.0105 317 SER A N 2148 C CA . SER A 276 ? 0.5773 0.7370 0.8074 0.0197 0.2231 -0.0185 317 SER A CA 2149 C C . SER A 276 ? 0.5535 0.7065 0.7704 0.0183 0.2046 -0.0214 317 SER A C 2150 O O . SER A 276 ? 0.5518 0.7041 0.7663 0.0219 0.1957 -0.0276 317 SER A O 2151 C CB . SER A 276 ? 0.5751 0.7487 0.8448 0.0191 0.2236 -0.0206 317 SER A CB 2152 O OG . SER A 276 ? 0.5895 0.7671 0.8792 0.0134 0.2142 -0.0185 317 SER A OG 2153 N N . SER A 277 ? 0.5399 0.6878 0.7489 0.0134 0.1992 -0.0169 318 SER A N 2154 C CA . SER A 277 ? 0.5065 0.6476 0.7015 0.0122 0.1828 -0.0191 318 SER A CA 2155 C C . SER A 277 ? 0.5037 0.6337 0.6644 0.0157 0.1809 -0.0211 318 SER A C 2156 O O . SER A 277 ? 0.4924 0.6167 0.6409 0.0156 0.1681 -0.0238 318 SER A O 2157 C CB . SER A 277 ? 0.5104 0.6495 0.7081 0.0062 0.1776 -0.0140 318 SER A CB 2158 O OG . SER A 277 ? 0.5153 0.6466 0.6915 0.0049 0.1856 -0.0082 318 SER A OG 2159 N N . TRP A 278 ? 0.4916 0.6182 0.6372 0.0187 0.1938 -0.0198 319 TRP A N 2160 C CA . TRP A 278 ? 0.4843 0.6008 0.5988 0.0228 0.1933 -0.0226 319 TRP A CA 2161 C C . TRP A 278 ? 0.4854 0.6033 0.6002 0.0287 0.1940 -0.0297 319 TRP A C 2162 O O . TRP A 278 ? 0.4888 0.5984 0.5803 0.0322 0.1910 -0.0334 319 TRP A O 2163 C CB . TRP A 278 ? 0.4990 0.6093 0.5929 0.0236 0.2061 -0.0174 319 TRP A CB 2164 C CG . TRP A 278 ? 0.5018 0.6053 0.5822 0.0192 0.2014 -0.0119 319 TRP A CG 2165 C CD1 . TRP A 278 ? 0.4637 0.5708 0.5607 0.0135 0.1974 -0.0074 319 TRP A CD1 2166 C CD2 . TRP A 278 ? 0.5134 0.6052 0.5616 0.0206 0.1994 -0.0108 319 TRP A CD2 2167 N NE1 . TRP A 278 ? 0.4973 0.5956 0.5742 0.0112 0.1936 -0.0033 319 TRP A NE1 2168 C CE2 . TRP A 278 ? 0.5148 0.6039 0.5620 0.0154 0.1944 -0.0053 319 TRP A CE2 2169 C CE3 . TRP A 278 ? 0.5128 0.5960 0.5333 0.0257 0.2006 -0.0144 319 TRP A CE3 2170 C CZ2 . TRP A 278 ? 0.5112 0.5896 0.5311 0.0155 0.1907 -0.0029 319 TRP A CZ2 2171 C CZ3 . TRP A 278 ? 0.5236 0.5962 0.5171 0.0257 0.1965 -0.0123 319 TRP A CZ3 2172 C CH2 . TRP A 278 ? 0.5389 0.6094 0.5325 0.0206 0.1917 -0.0065 319 TRP A CH2 2173 N N . ARG A 279 ? 0.4739 0.6022 0.6156 0.0299 0.1977 -0.0317 320 ARG A N 2174 C CA . ARG A 279 ? 0.4739 0.6039 0.6184 0.0357 0.1984 -0.0384 320 ARG A CA 2175 C C . ARG A 279 ? 0.4524 0.5836 0.6065 0.0360 0.1833 -0.0433 320 ARG A C 2176 O O . ARG A 279 ? 0.4558 0.5941 0.6326 0.0330 0.1768 -0.0424 320 ARG A O 2177 C CB . ARG A 279 ? 0.4779 0.6185 0.6466 0.0377 0.2114 -0.0383 320 ARG A CB 2178 C CG . ARG A 279 ? 0.5315 0.6702 0.6880 0.0399 0.2287 -0.0349 320 ARG A CG 2179 C CD . ARG A 279 ? 0.6057 0.7551 0.7868 0.0431 0.2411 -0.0362 320 ARG A CD 2180 N NE . ARG A 279 ? 0.6990 0.8473 0.8710 0.0448 0.2593 -0.0317 320 ARG A NE 2181 C CZ . ARG A 279 ? 0.7337 0.8870 0.9189 0.0407 0.2695 -0.0244 320 ARG A CZ 2182 N NH1 . ARG A 279 ? 0.7109 0.8708 0.9203 0.0344 0.2626 -0.0212 320 ARG A NH1 2183 N NH2 . ARG A 279 ? 0.7484 0.8993 0.9221 0.0431 0.2869 -0.0202 320 ARG A NH2 2184 N N . GLY A 280 ? 0.4600 0.5840 0.5969 0.0398 0.1776 -0.0484 321 GLY A N 2185 C CA . GLY A 280 ? 0.4332 0.5579 0.5793 0.0413 0.1650 -0.0531 321 GLY A CA 2186 C C . GLY A 280 ? 0.4398 0.5716 0.6045 0.0462 0.1698 -0.0577 321 GLY A C 2187 O O . GLY A 280 ? 0.4429 0.5821 0.6213 0.0472 0.1820 -0.0564 321 GLY A O 2188 N N . SER A 281 ? 0.4276 0.5571 0.5933 0.0495 0.1607 -0.0627 322 SER A N 2189 C CA . SER A 281 ? 0.4414 0.5777 0.6273 0.0543 0.1627 -0.0672 322 SER A CA 2190 C C . SER A 281 ? 0.4385 0.5696 0.6113 0.0604 0.1692 -0.0723 322 SER A C 2191 O O . SER A 281 ? 0.4522 0.5882 0.6402 0.0650 0.1713 -0.0763 322 SER A O 2192 C CB . SER A 281 ? 0.4333 0.5707 0.6316 0.0547 0.1483 -0.0693 322 SER A CB 2193 O OG . SER A 281 ? 0.4755 0.6197 0.6914 0.0502 0.1432 -0.0656 322 SER A OG 2194 N N . LEU A 282 ? 0.4390 0.5601 0.5839 0.0607 0.1716 -0.0726 323 LEU A N 2195 C CA . LEU A 282 ? 0.4367 0.5516 0.5677 0.0668 0.1765 -0.0783 323 LEU A CA 2196 C C . LEU A 282 ? 0.4629 0.5836 0.5992 0.0700 0.1929 -0.0781 323 LEU A C 2197 O O . LEU A 282 ? 0.4570 0.5834 0.5999 0.0669 0.2013 -0.0727 323 LEU A O 2198 C CB . LEU A 282 ? 0.4480 0.5499 0.5476 0.0666 0.1729 -0.0795 323 LEU A CB 2199 C CG . LEU A 282 ? 0.4133 0.5084 0.5059 0.0640 0.1575 -0.0802 323 LEU A CG 2200 C CD1 . LEU A 282 ? 0.4171 0.5010 0.4806 0.0626 0.1550 -0.0800 323 LEU A CD1 2201 C CD2 . LEU A 282 ? 0.4388 0.5319 0.5387 0.0684 0.1512 -0.0860 323 LEU A CD2 2202 N N . LYS A 283 ? 0.4746 0.5932 0.6081 0.0764 0.1977 -0.0840 324 LYS A N 2203 C CA . LYS A 283 ? 0.5085 0.6321 0.6464 0.0806 0.2141 -0.0846 324 LYS A CA 2204 C C . LYS A 283 ? 0.5238 0.6376 0.6301 0.0820 0.2223 -0.0840 324 LYS A C 2205 O O . LYS A 283 ? 0.5493 0.6566 0.6399 0.0881 0.2275 -0.0893 324 LYS A O 2206 C CB . LYS A 283 ? 0.5158 0.6430 0.6686 0.0871 0.2160 -0.0911 324 LYS A CB 2207 C CG A LYS A 283 ? 0.5165 0.6513 0.6971 0.0859 0.2047 -0.0918 324 LYS A CG 2208 C CG B LYS A 283 ? 0.5185 0.6554 0.7025 0.0860 0.2072 -0.0913 324 LYS A CG 2209 C CD A LYS A 283 ? 0.5275 0.6673 0.7269 0.0925 0.2068 -0.0976 324 LYS A CD 2210 C CD B LYS A 283 ? 0.5168 0.6674 0.7284 0.0826 0.2140 -0.0861 324 LYS A CD 2211 C CE A LYS A 283 ? 0.5253 0.6720 0.7504 0.0910 0.1944 -0.0974 324 LYS A CE 2212 C CE B LYS A 283 ? 0.5036 0.6608 0.7388 0.0793 0.2006 -0.0850 324 LYS A CE 2213 N NZ A LYS A 283 ? 0.5244 0.6732 0.7647 0.0974 0.1919 -0.1033 324 LYS A NZ 2214 N NZ B LYS A 283 ? 0.4817 0.6522 0.7451 0.0758 0.2062 -0.0805 324 LYS A NZ 2215 N N . VAL A 284 ? 0.5181 0.6301 0.6148 0.0766 0.2223 -0.0776 325 VAL A N 2216 C CA . VAL A 284 ? 0.5396 0.6428 0.6072 0.0773 0.2296 -0.0754 325 VAL A CA 2217 C C . VAL A 284 ? 0.5328 0.6424 0.6084 0.0726 0.2388 -0.0668 325 VAL A C 2218 O O . VAL A 284 ? 0.5032 0.6224 0.6047 0.0678 0.2356 -0.0630 325 VAL A O 2219 C CB . VAL A 284 ? 0.5436 0.6344 0.5847 0.0754 0.2167 -0.0767 325 VAL A CB 2220 C CG1 . VAL A 284 ? 0.5692 0.6527 0.6019 0.0798 0.2082 -0.0851 325 VAL A CG1 2221 C CG2 . VAL A 284 ? 0.5188 0.6119 0.5687 0.0679 0.2051 -0.0716 325 VAL A CG2 2222 N N . PRO A 285 ? 0.5520 0.6556 0.6052 0.0742 0.2499 -0.0636 326 PRO A N 2223 C CA . PRO A 285 ? 0.5553 0.6642 0.6161 0.0700 0.2600 -0.0549 326 PRO A CA 2224 C C . PRO A 285 ? 0.5374 0.6443 0.5961 0.0625 0.2498 -0.0491 326 PRO A C 2225 O O . PRO A 285 ? 0.5233 0.6368 0.5978 0.0578 0.2550 -0.0422 326 PRO A O 2226 C CB . PRO A 285 ? 0.5886 0.6900 0.6226 0.0751 0.2749 -0.0535 326 PRO A CB 2227 C CG . PRO A 285 ? 0.6135 0.7032 0.6200 0.0809 0.2685 -0.0617 326 PRO A CG 2228 C CD . PRO A 285 ? 0.5761 0.6683 0.5980 0.0807 0.2546 -0.0682 326 PRO A CD 2229 N N . TYR A 286 ? 0.5243 0.6224 0.5653 0.0616 0.2354 -0.0521 327 TYR A N 2230 C CA . TYR A 286 ? 0.5183 0.6125 0.5521 0.0554 0.2255 -0.0472 327 TYR A CA 2231 C C . TYR A 286 ? 0.5392 0.6278 0.5534 0.0546 0.2351 -0.0406 327 TYR A C 2232 O O . TYR A 286 ? 0.5400 0.6301 0.5593 0.0490 0.2339 -0.0338 327 TYR A O 2233 C CB . TYR A 286 ? 0.4983 0.6023 0.5617 0.0494 0.2183 -0.0443 327 TYR A CB 2234 C CG . TYR A 286 ? 0.4739 0.5798 0.5492 0.0500 0.2052 -0.0503 327 TYR A CG 2235 C CD1 . TYR A 286 ? 0.4402 0.5389 0.5027 0.0482 0.1907 -0.0521 327 TYR A CD1 2236 C CD2 . TYR A 286 ? 0.4785 0.5931 0.5774 0.0529 0.2076 -0.0540 327 TYR A CD2 2237 C CE1 . TYR A 286 ? 0.4517 0.5515 0.5243 0.0490 0.1796 -0.0569 327 TYR A CE1 2238 C CE2 . TYR A 286 ? 0.4542 0.5698 0.5629 0.0539 0.1957 -0.0591 327 TYR A CE2 2239 C CZ . TYR A 286 ? 0.4491 0.5568 0.5438 0.0520 0.1821 -0.0604 327 TYR A CZ 2240 O OH . TYR A 286 ? 0.4424 0.5502 0.5460 0.0532 0.1710 -0.0647 327 TYR A OH 2241 N N . ASN A 287 ? 0.5601 0.6416 0.5510 0.0606 0.2443 -0.0427 328 ASN A N 2242 C CA . ASN A 287 ? 0.5923 0.6662 0.5589 0.0615 0.2532 -0.0371 328 ASN A CA 2243 C C . ASN A 287 ? 0.5875 0.6520 0.5338 0.0585 0.2398 -0.0362 328 ASN A C 2244 O O . ASN A 287 ? 0.5751 0.6353 0.5149 0.0589 0.2264 -0.0423 328 ASN A O 2245 C CB . ASN A 287 ? 0.6054 0.6722 0.5484 0.0697 0.2641 -0.0410 328 ASN A CB 2246 C CG . ASN A 287 ? 0.6349 0.7105 0.5953 0.0729 0.2817 -0.0397 328 ASN A CG 2247 O OD1 . ASN A 287 ? 0.6387 0.7247 0.6256 0.0686 0.2885 -0.0337 328 ASN A OD1 2248 N ND2 . ASN A 287 ? 0.6067 0.6782 0.5528 0.0808 0.2892 -0.0456 328 ASN A ND2 2249 N N . VAL A 288 ? 0.6084 0.6696 0.5453 0.0555 0.2439 -0.0284 329 VAL A N 2250 C CA . VAL A 288 ? 0.6076 0.6612 0.5289 0.0521 0.2313 -0.0266 329 VAL A CA 2251 C C . VAL A 288 ? 0.6315 0.6716 0.5161 0.0574 0.2287 -0.0300 329 VAL A C 2252 O O . VAL A 288 ? 0.6276 0.6610 0.4989 0.0559 0.2156 -0.0316 329 VAL A O 2253 C CB . VAL A 288 ? 0.6076 0.6636 0.5370 0.0463 0.2351 -0.0167 329 VAL A CB 2254 C CG1 . VAL A 288 ? 0.6178 0.6642 0.5258 0.0441 0.2246 -0.0142 329 VAL A CG1 2255 C CG2 . VAL A 288 ? 0.5860 0.6544 0.5519 0.0403 0.2311 -0.0153 329 VAL A CG2 2256 N N . GLY A 289 ? 0.6601 0.6960 0.5287 0.0641 0.2408 -0.0317 330 GLY A N 2257 C CA . GLY A 289 ? 0.6947 0.7172 0.5271 0.0699 0.2390 -0.0351 330 GLY A CA 2258 C C . GLY A 289 ? 0.7214 0.7368 0.5330 0.0700 0.2461 -0.0266 330 GLY A C 2259 O O . GLY A 289 ? 0.7245 0.7454 0.5486 0.0674 0.2583 -0.0184 330 GLY A O 2260 N N . PRO A 290 ? 0.7419 0.7448 0.5222 0.0730 0.2386 -0.0284 331 PRO A N 2261 C CA . PRO A 290 ? 0.7442 0.7400 0.5098 0.0758 0.2239 -0.0380 331 PRO A CA 2262 C C . PRO A 290 ? 0.7558 0.7476 0.5088 0.0840 0.2296 -0.0464 331 PRO A C 2263 O O . PRO A 290 ? 0.7832 0.7732 0.5253 0.0892 0.2451 -0.0441 331 PRO A O 2264 C CB . PRO A 290 ? 0.7597 0.7434 0.4952 0.0771 0.2178 -0.0352 331 PRO A CB 2265 C CG . PRO A 290 ? 0.7980 0.7782 0.5184 0.0808 0.2358 -0.0274 331 PRO A CG 2266 C CD . PRO A 290 ? 0.7758 0.7696 0.5304 0.0753 0.2464 -0.0209 331 PRO A CD 2267 N N . GLY A 291 ? 0.7454 0.7356 0.5001 0.0851 0.2175 -0.0558 332 GLY A N 2268 C CA . GLY A 291 ? 0.7631 0.7476 0.5038 0.0929 0.2197 -0.0652 332 GLY A CA 2269 C C . GLY A 291 ? 0.7618 0.7556 0.5239 0.0950 0.2307 -0.0677 332 GLY A C 2270 O O . GLY A 291 ? 0.7392 0.7449 0.5300 0.0901 0.2363 -0.0623 332 GLY A O 2271 N N . PHE A 292 ? 0.7783 0.7662 0.5266 0.1027 0.2334 -0.0762 333 PHE A N 2272 C CA . PHE A 292 ? 0.7717 0.7669 0.5381 0.1060 0.2426 -0.0805 333 PHE A CA 2273 C C . PHE A 292 ? 0.8056 0.8011 0.5625 0.1120 0.2632 -0.0769 333 PHE A C 2274 O O . PHE A 292 ? 0.8273 0.8142 0.5568 0.1153 0.2692 -0.0730 333 PHE A O 2275 C CB . PHE A 292 ? 0.7681 0.7565 0.5264 0.1111 0.2332 -0.0927 333 PHE A CB 2276 C CG . PHE A 292 ? 0.7524 0.7418 0.5252 0.1056 0.2148 -0.0966 333 PHE A CG 2277 C CD1 . PHE A 292 ? 0.7512 0.7301 0.5082 0.1087 0.2022 -0.1060 333 PHE A CD1 2278 C CD2 . PHE A 292 ? 0.7177 0.7179 0.5195 0.0976 0.2102 -0.0911 333 PHE A CD2 2279 C CE1 . PHE A 292 ? 0.7629 0.7423 0.5334 0.1037 0.1864 -0.1092 333 PHE A CE1 2280 C CE2 . PHE A 292 ? 0.7088 0.7091 0.5222 0.0930 0.1941 -0.0945 333 PHE A CE2 2281 C CZ . PHE A 292 ? 0.6916 0.6816 0.4896 0.0961 0.1828 -0.1033 333 PHE A CZ 2282 N N . THR A 293 ? 0.8052 0.8103 0.5847 0.1138 0.2738 -0.0781 334 THR A N 2283 C CA . THR A 293 ? 0.8466 0.8531 0.6202 0.1200 0.2946 -0.0755 334 THR A CA 2284 C C . THR A 293 ? 0.8884 0.8816 0.6273 0.1305 0.2985 -0.0833 334 THR A C 2285 O O . THR A 293 ? 0.8921 0.8782 0.6211 0.1334 0.2861 -0.0932 334 THR A O 2286 C CB . THR A 293 ? 0.8327 0.8534 0.6413 0.1198 0.3041 -0.0762 334 THR A CB 2287 O OG1 . THR A 293 ? 0.8306 0.8503 0.6451 0.1230 0.2947 -0.0871 334 THR A OG1 2288 C CG2 . THR A 293 ? 0.8246 0.8587 0.6682 0.1103 0.3017 -0.0686 334 THR A CG2 2289 N N . GLY A 294 ? 0.9239 0.9143 0.6462 0.1362 0.3167 -0.0788 335 GLY A N 2290 C CA . GLY A 294 ? 0.9684 0.9453 0.6536 0.1469 0.3231 -0.0847 335 GLY A CA 2291 C C . GLY A 294 ? 0.9898 0.9576 0.6598 0.1538 0.3131 -0.0985 335 GLY A C 2292 O O . GLY A 294 ? 1.0202 0.9734 0.6553 0.1590 0.3061 -0.1033 335 GLY A O 2293 N N . ASN A 295 ? 0.9770 0.9527 0.6723 0.1543 0.3125 -0.1050 336 ASN A N 2294 C CA . ASN A 295 ? 0.9916 0.9588 0.6757 0.1606 0.3030 -0.1183 336 ASN A CA 2295 C C . ASN A 295 ? 0.9757 0.9351 0.6522 0.1566 0.2801 -0.1238 336 ASN A C 2296 O O . ASN A 295 ? 1.0021 0.9492 0.6557 0.1626 0.2716 -0.1338 336 ASN A O 2297 C CB . ASN A 295 ? 0.9829 0.9611 0.6994 0.1612 0.3067 -0.1231 336 ASN A CB 2298 C CG . ASN A 295 ? 1.0275 1.0096 0.7445 0.1689 0.3287 -0.1226 336 ASN A CG 2299 O OD1 . ASN A 295 ? 1.0794 1.0575 0.7752 0.1729 0.3430 -0.1169 336 ASN A OD1 2300 N ND2 . ASN A 295 ? 1.0489 1.0387 0.7901 0.1713 0.3317 -0.1283 336 ASN A ND2 2301 N N . PHE A 296 ? 0.9363 0.9029 0.6330 0.1467 0.2703 -0.1174 337 PHE A N 2302 C CA . PHE A 296 ? 0.9104 0.8717 0.6056 0.1419 0.2494 -0.1215 337 PHE A CA 2303 C C . PHE A 296 ? 0.9066 0.8634 0.5856 0.1375 0.2438 -0.1141 337 PHE A C 2304 O O . PHE A 296 ? 0.8811 0.8383 0.5680 0.1307 0.2286 -0.1134 337 PHE A O 2305 C CB . PHE A 296 ? 0.8765 0.8498 0.6098 0.1342 0.2411 -0.1211 337 PHE A CB 2306 C CG . PHE A 296 ? 0.8680 0.8500 0.6248 0.1372 0.2504 -0.1244 337 PHE A CG 2307 C CD1 . PHE A 296 ? 0.8621 0.8579 0.6444 0.1343 0.2634 -0.1164 337 PHE A CD1 2308 C CD2 . PHE A 296 ? 0.8731 0.8495 0.6275 0.1430 0.2458 -0.1356 337 PHE A CD2 2309 C CE1 . PHE A 296 ? 0.8570 0.8614 0.6623 0.1373 0.2717 -0.1196 337 PHE A CE1 2310 C CE2 . PHE A 296 ? 0.8655 0.8500 0.6421 0.1461 0.2541 -0.1387 337 PHE A CE2 2311 C CZ . PHE A 296 ? 0.8546 0.8534 0.6568 0.1434 0.2671 -0.1307 337 PHE A CZ 2312 N N . SER A 297 ? 0.9212 0.8734 0.5774 0.1415 0.2564 -0.1083 338 SER A N 2313 C CA . SER A 297 ? 0.9232 0.8711 0.5639 0.1380 0.2534 -0.1000 338 SER A CA 2314 C C . SER A 297 ? 0.9237 0.8587 0.5399 0.1391 0.2353 -0.1064 338 SER A C 2315 O O . SER A 297 ? 0.9233 0.8563 0.5341 0.1341 0.2271 -0.1007 338 SER A O 2316 C CB . SER A 297 ? 0.9521 0.8961 0.5708 0.1435 0.2719 -0.0929 338 SER A CB 2317 O OG . SER A 297 ? 1.0054 0.9355 0.5887 0.1541 0.2740 -0.1006 338 SER A OG 2318 N N . THR A 298 ? 0.9290 0.8555 0.5320 0.1455 0.2287 -0.1183 339 THR A N 2319 C CA . THR A 298 ? 0.9388 0.8522 0.5178 0.1477 0.2115 -0.1259 339 THR A CA 2320 C C . THR A 298 ? 0.9142 0.8306 0.5154 0.1412 0.1932 -0.1315 339 THR A C 2321 O O . THR A 298 ? 0.9236 0.8309 0.5111 0.1412 0.1776 -0.1371 339 THR A O 2322 C CB . THR A 298 ? 0.9721 0.8721 0.5196 0.1592 0.2139 -0.1363 339 THR A CB 2323 O OG1 . THR A 298 ? 0.9731 0.8779 0.5363 0.1627 0.2215 -0.1425 339 THR A OG1 2324 C CG2 . THR A 298 ? 0.9989 0.8917 0.5147 0.1661 0.2284 -0.1303 339 THR A CG2 2325 N N . GLN A 299 ? 0.8811 0.8100 0.5167 0.1357 0.1953 -0.1298 340 GLN A N 2326 C CA . GLN A 299 ? 0.8447 0.7779 0.5043 0.1285 0.1799 -0.1325 340 GLN A CA 2327 C C . GLN A 299 ? 0.8194 0.7577 0.4887 0.1198 0.1730 -0.1233 340 GLN A C 2328 O O . GLN A 299 ? 0.8094 0.7525 0.4786 0.1176 0.1826 -0.1135 340 GLN A O 2329 C CB . GLN A 299 ? 0.8236 0.7671 0.5141 0.1271 0.1844 -0.1344 340 GLN A CB 2330 C CG . GLN A 299 ? 0.8596 0.7970 0.5403 0.1364 0.1899 -0.1448 340 GLN A CG 2331 C CD . GLN A 299 ? 0.8671 0.8144 0.5774 0.1362 0.1959 -0.1466 340 GLN A CD 2332 O OE1 . GLN A 299 ? 0.8499 0.8092 0.5886 0.1295 0.1967 -0.1401 340 GLN A OE1 2333 N NE2 . GLN A 299 ? 0.8862 0.8280 0.5889 0.1442 0.1998 -0.1560 340 GLN A NE2 2334 N N . LYS A 300 ? 0.7923 0.7291 0.4698 0.1149 0.1565 -0.1267 341 LYS A N 2335 C CA . LYS A 300 ? 0.7613 0.7027 0.4496 0.1067 0.1484 -0.1192 341 LYS A CA 2336 C C . LYS A 300 ? 0.7207 0.6696 0.4393 0.1004 0.1394 -0.1206 341 LYS A C 2337 O O . LYS A 300 ? 0.7093 0.6581 0.4378 0.1026 0.1382 -0.1277 341 LYS A O 2338 C CB . LYS A 300 ? 0.7750 0.7056 0.4400 0.1073 0.1356 -0.1216 341 LYS A CB 2339 C CG . LYS A 300 ? 0.8416 0.7608 0.4710 0.1155 0.1401 -0.1237 341 LYS A CG 2340 C CD . LYS A 300 ? 0.8899 0.8112 0.5099 0.1149 0.1514 -0.1125 341 LYS A CD 2341 C CE . LYS A 300 ? 0.9490 0.8610 0.5378 0.1247 0.1631 -0.1145 341 LYS A CE 2342 N NZ . LYS A 300 ? 1.0261 0.9330 0.5930 0.1256 0.1668 -0.1061 341 LYS A NZ 2343 N N . VAL A 301 ? 0.6855 0.6402 0.4178 0.0929 0.1335 -0.1137 342 VAL A N 2344 C CA . VAL A 301 ? 0.6528 0.6127 0.4097 0.0870 0.1233 -0.1147 342 VAL A CA 2345 C C . VAL A 301 ? 0.6475 0.6002 0.3955 0.0846 0.1080 -0.1174 342 VAL A C 2346 O O . VAL A 301 ? 0.6553 0.6048 0.3883 0.0838 0.1059 -0.1134 342 VAL A O 2347 C CB . VAL A 301 ? 0.6281 0.6004 0.4095 0.0804 0.1276 -0.1052 342 VAL A CB 2348 C CG1 . VAL A 301 ? 0.5934 0.5692 0.3950 0.0743 0.1156 -0.1053 342 VAL A CG1 2349 C CG2 . VAL A 301 ? 0.6453 0.6254 0.4408 0.0828 0.1411 -0.1041 342 VAL A CG2 2350 N N . LYS A 302 ? 0.6412 0.5914 0.3991 0.0835 0.0976 -0.1241 343 LYS A N 2351 C CA . LYS A 302 ? 0.6446 0.5891 0.3989 0.0807 0.0829 -0.1270 343 LYS A CA 2352 C C . LYS A 302 ? 0.6160 0.5666 0.3969 0.0740 0.0751 -0.1251 343 LYS A C 2353 O O . LYS A 302 ? 0.5937 0.5462 0.3902 0.0741 0.0752 -0.1286 343 LYS A O 2354 C CB . LYS A 302 ? 0.6756 0.6086 0.4138 0.0864 0.0761 -0.1381 343 LYS A CB 2355 C CG . LYS A 302 ? 0.6827 0.6094 0.4190 0.0839 0.0603 -0.1425 343 LYS A CG 2356 C CD . LYS A 302 ? 0.7720 0.6868 0.4899 0.0908 0.0551 -0.1541 343 LYS A CD 2357 C CE . LYS A 302 ? 0.8282 0.7365 0.5475 0.0886 0.0389 -0.1603 343 LYS A CE 2358 N NZ . LYS A 302 ? 0.8892 0.7944 0.5931 0.0878 0.0322 -0.1574 343 LYS A NZ 2359 N N . MET A 303 ? 0.6081 0.5609 0.3928 0.0686 0.0683 -0.1198 344 MET A N 2360 C CA . MET A 303 ? 0.5889 0.5462 0.3959 0.0625 0.0606 -0.1179 344 MET A CA 2361 C C . MET A 303 ? 0.6011 0.5504 0.4055 0.0623 0.0476 -0.1251 344 MET A C 2362 O O . MET A 303 ? 0.6090 0.5506 0.3943 0.0653 0.0426 -0.1294 344 MET A O 2363 C CB . MET A 303 ? 0.5739 0.5380 0.3880 0.0569 0.0602 -0.1085 344 MET A CB 2364 C CG . MET A 303 ? 0.5631 0.5347 0.3798 0.0567 0.0723 -0.1013 344 MET A CG 2365 S SD . MET A 303 ? 0.5288 0.5080 0.3551 0.0503 0.0720 -0.0907 344 MET A SD 2366 C CE . MET A 303 ? 0.4842 0.4689 0.3371 0.0454 0.0652 -0.0904 344 MET A CE 2367 N N . HIS A 304 ? 0.5765 0.5275 0.4005 0.0590 0.0422 -0.1264 345 HIS A N 2368 C CA . HIS A 304 ? 0.5729 0.5176 0.3995 0.0574 0.0300 -0.1319 345 HIS A CA 2369 C C . HIS A 304 ? 0.5447 0.4954 0.3924 0.0509 0.0259 -0.1260 345 HIS A C 2370 O O . HIS A 304 ? 0.5369 0.4904 0.4013 0.0496 0.0275 -0.1255 345 HIS A O 2371 C CB . HIS A 304 ? 0.5863 0.5248 0.4168 0.0606 0.0278 -0.1407 345 HIS A CB 2372 C CG . HIS A 304 ? 0.6223 0.5559 0.4356 0.0677 0.0344 -0.1466 345 HIS A CG 2373 N ND1 . HIS A 304 ? 0.6438 0.5828 0.4592 0.0702 0.0464 -0.1436 345 HIS A ND1 2374 C CD2 . HIS A 304 ? 0.6475 0.5713 0.4415 0.0732 0.0308 -0.1553 345 HIS A CD2 2375 C CE1 . HIS A 304 ? 0.6426 0.5756 0.4406 0.0769 0.0508 -0.1499 345 HIS A CE1 2376 N NE2 . HIS A 304 ? 0.7005 0.6238 0.4843 0.0790 0.0414 -0.1572 345 HIS A NE2 2377 N N . ILE A 305 ? 0.5407 0.4928 0.3868 0.0474 0.0205 -0.1220 346 ILE A N 2378 C CA . ILE A 305 ? 0.5166 0.4749 0.3814 0.0414 0.0176 -0.1156 346 ILE A CA 2379 C C . ILE A 305 ? 0.5275 0.4812 0.3949 0.0390 0.0062 -0.1188 346 ILE A C 2380 O O . ILE A 305 ? 0.5472 0.4973 0.4009 0.0399 0.0011 -0.1206 346 ILE A O 2381 C CB . ILE A 305 ? 0.5112 0.4769 0.3754 0.0389 0.0226 -0.1064 346 ILE A CB 2382 C CG1 . ILE A 305 ? 0.5201 0.4904 0.3820 0.0413 0.0340 -0.1035 346 ILE A CG1 2383 C CG2 . ILE A 305 ? 0.4769 0.4483 0.3597 0.0334 0.0195 -0.1005 346 ILE A CG2 2384 C CD1 . ILE A 305 ? 0.5194 0.4934 0.3978 0.0416 0.0386 -0.1038 346 ILE A CD1 2385 N N . HIS A 306 ? 0.5110 0.4647 0.3963 0.0361 0.0023 -0.1194 347 HIS A N 2386 C CA . HIS A 306 ? 0.5071 0.4567 0.3989 0.0335 -0.0080 -0.1229 347 HIS A CA 2387 C C . HIS A 306 ? 0.4712 0.4259 0.3827 0.0281 -0.0098 -0.1166 347 HIS A C 2388 O O . HIS A 306 ? 0.4671 0.4189 0.3894 0.0256 -0.0169 -0.1191 347 HIS A O 2389 C CB . HIS A 306 ? 0.5234 0.4652 0.4175 0.0359 -0.0121 -0.1319 347 HIS A CB 2390 C CG . HIS A 306 ? 0.5785 0.5146 0.4535 0.0420 -0.0098 -0.1387 347 HIS A CG 2391 N ND1 . HIS A 306 ? 0.6611 0.5926 0.5163 0.0450 -0.0140 -0.1427 347 HIS A ND1 2392 C CD2 . HIS A 306 ? 0.6043 0.5384 0.4761 0.0461 -0.0034 -0.1422 347 HIS A CD2 2393 C CE1 . HIS A 306 ? 0.6550 0.5815 0.4948 0.0508 -0.0100 -0.1483 347 HIS A CE1 2394 N NE2 . HIS A 306 ? 0.6553 0.5836 0.5056 0.0514 -0.0034 -0.1482 347 HIS A NE2 2395 N N . SER A 307 ? 0.4419 0.4039 0.3580 0.0264 -0.0031 -0.1086 348 SER A N 2396 C CA . SER A 307 ? 0.4170 0.3837 0.3494 0.0220 -0.0039 -0.1023 348 SER A CA 2397 C C . SER A 307 ? 0.4287 0.3956 0.3615 0.0191 -0.0110 -0.1012 348 SER A C 2398 O O . SER A 307 ? 0.4469 0.4123 0.3658 0.0206 -0.0137 -0.1031 348 SER A O 2399 C CB . SER A 307 ? 0.3953 0.3694 0.3291 0.0214 0.0037 -0.0946 348 SER A CB 2400 O OG . SER A 307 ? 0.4040 0.3787 0.3381 0.0244 0.0102 -0.0958 348 SER A OG 2401 N N . THR A 308 ? 0.4192 0.3880 0.3677 0.0154 -0.0134 -0.0978 349 THR A N 2402 C CA . THR A 308 ? 0.4092 0.3789 0.3608 0.0127 -0.0200 -0.0968 349 THR A CA 2403 C C . THR A 308 ? 0.4013 0.3774 0.3627 0.0096 -0.0170 -0.0884 349 THR A C 2404 O O . THR A 308 ? 0.3926 0.3707 0.3635 0.0089 -0.0122 -0.0846 349 THR A O 2405 C CB . THR A 308 ? 0.4318 0.3967 0.3957 0.0110 -0.0270 -0.1018 349 THR A CB 2406 O OG1 . THR A 308 ? 0.4810 0.4460 0.4604 0.0094 -0.0234 -0.0992 349 THR A OG1 2407 C CG2 . THR A 308 ? 0.4354 0.3929 0.3900 0.0142 -0.0317 -0.1114 349 THR A CG2 2408 N N . ASN A 309 ? 0.3796 0.3585 0.3377 0.0082 -0.0201 -0.0858 350 ASN A N 2409 C CA . ASN A 309 ? 0.3754 0.3600 0.3429 0.0054 -0.0181 -0.0784 350 ASN A CA 2410 C C . ASN A 309 ? 0.3763 0.3601 0.3587 0.0026 -0.0233 -0.0790 350 ASN A C 2411 O O . ASN A 309 ? 0.4055 0.3863 0.3879 0.0024 -0.0303 -0.0841 350 ASN A O 2412 C CB . ASN A 309 ? 0.3818 0.3697 0.3388 0.0055 -0.0184 -0.0750 350 ASN A CB 2413 C CG . ASN A 309 ? 0.4102 0.3990 0.3536 0.0080 -0.0127 -0.0738 350 ASN A CG 2414 O OD1 . ASN A 309 ? 0.4060 0.3958 0.3513 0.0090 -0.0069 -0.0730 350 ASN A OD1 2415 N ND2 . ASN A 309 ? 0.4751 0.4635 0.4050 0.0092 -0.0141 -0.0737 350 ASN A ND2 2416 N N . GLU A 310 ? 0.3586 0.3452 0.3540 0.0005 -0.0199 -0.0736 351 GLU A N 2417 C CA . GLU A 310 ? 0.3631 0.3487 0.3752 -0.0022 -0.0229 -0.0736 351 GLU A CA 2418 C C . GLU A 310 ? 0.3318 0.3224 0.3521 -0.0039 -0.0190 -0.0658 351 GLU A C 2419 O O . GLU A 310 ? 0.3186 0.3109 0.3376 -0.0030 -0.0129 -0.0612 351 GLU A O 2420 C CB . GLU A 310 ? 0.3858 0.3666 0.4066 -0.0020 -0.0210 -0.0759 351 GLU A CB 2421 C CG A GLU A 310 ? 0.4345 0.4090 0.4510 -0.0004 -0.0257 -0.0847 351 GLU A CG 2422 C CG B GLU A 310 ? 0.4427 0.4180 0.4545 0.0007 -0.0230 -0.0835 351 GLU A CG 2423 C CD A GLU A 310 ? 0.4637 0.4330 0.4921 -0.0007 -0.0246 -0.0867 351 GLU A CD 2424 C CD B GLU A 310 ? 0.5067 0.4772 0.5218 0.0001 -0.0314 -0.0912 351 GLU A CD 2425 O OE1 A GLU A 310 ? 0.5112 0.4751 0.5434 -0.0009 -0.0303 -0.0938 351 GLU A OE1 2426 O OE1 B GLU A 310 ? 0.5520 0.5178 0.5568 0.0027 -0.0340 -0.0981 351 GLU A OE1 2427 O OE2 A GLU A 310 ? 0.4626 0.4326 0.4963 -0.0006 -0.0184 -0.0815 351 GLU A OE2 2428 O OE2 B GLU A 310 ? 0.5309 0.5022 0.5592 -0.0029 -0.0355 -0.0907 351 GLU A OE2 2429 N N . VAL A 311 ? 0.3167 0.3095 0.3456 -0.0061 -0.0225 -0.0646 352 VAL A N 2430 C CA . VAL A 311 ? 0.3003 0.2973 0.3380 -0.0074 -0.0183 -0.0574 352 VAL A CA 2431 C C . VAL A 311 ? 0.2978 0.2921 0.3485 -0.0083 -0.0142 -0.0552 352 VAL A C 2432 O O . VAL A 311 ? 0.3112 0.3020 0.3734 -0.0099 -0.0172 -0.0587 352 VAL A O 2433 C CB . VAL A 311 ? 0.2891 0.2893 0.3340 -0.0093 -0.0228 -0.0568 352 VAL A CB 2434 C CG1 . VAL A 311 ? 0.3012 0.3050 0.3557 -0.0103 -0.0176 -0.0497 352 VAL A CG1 2435 C CG2 . VAL A 311 ? 0.3074 0.3096 0.3382 -0.0080 -0.0267 -0.0582 352 VAL A CG2 2436 N N . THR A 312 ? 0.2716 0.2672 0.3209 -0.0072 -0.0077 -0.0492 353 THR A N 2437 C CA . THR A 312 ? 0.2690 0.2609 0.3258 -0.0068 -0.0029 -0.0465 353 THR A CA 2438 C C . THR A 312 ? 0.2582 0.2528 0.3176 -0.0063 0.0026 -0.0387 353 THR A C 2439 O O . THR A 312 ? 0.2572 0.2558 0.3077 -0.0051 0.0037 -0.0360 353 THR A O 2440 C CB . THR A 312 ? 0.2920 0.2813 0.3394 -0.0042 -0.0011 -0.0487 353 THR A CB 2441 O OG1 . THR A 312 ? 0.3363 0.3233 0.3784 -0.0040 -0.0060 -0.0562 353 THR A OG1 2442 C CG2 . THR A 312 ? 0.2985 0.2829 0.3535 -0.0035 0.0027 -0.0468 353 THR A CG2 2443 N N . ARG A 313 ? 0.2664 0.2581 0.3372 -0.0070 0.0063 -0.0350 354 ARG A N 2444 C CA . ARG A 313 ? 0.2638 0.2569 0.3358 -0.0059 0.0120 -0.0276 354 ARG A CA 2445 C C . ARG A 313 ? 0.2654 0.2568 0.3269 -0.0024 0.0157 -0.0248 354 ARG A C 2446 O O . ARG A 313 ? 0.2861 0.2733 0.3470 -0.0012 0.0162 -0.0267 354 ARG A O 2447 C CB . ARG A 313 ? 0.2774 0.2674 0.3652 -0.0076 0.0155 -0.0239 354 ARG A CB 2448 C CG . ARG A 313 ? 0.2748 0.2661 0.3629 -0.0060 0.0219 -0.0160 354 ARG A CG 2449 C CD . ARG A 313 ? 0.3187 0.3096 0.4242 -0.0087 0.0246 -0.0132 354 ARG A CD 2450 N NE . ARG A 313 ? 0.3206 0.3171 0.4318 -0.0112 0.0197 -0.0164 354 ARG A NE 2451 C CZ . ARG A 313 ? 0.3664 0.3651 0.4931 -0.0135 0.0211 -0.0145 354 ARG A CZ 2452 N NH1 . ARG A 313 ? 0.3629 0.3583 0.5007 -0.0138 0.0279 -0.0091 354 ARG A NH1 2453 N NH2 . ARG A 313 ? 0.3749 0.3791 0.5060 -0.0152 0.0160 -0.0176 354 ARG A NH2 2454 N N . ILE A 314 ? 0.2430 0.2376 0.2974 -0.0006 0.0180 -0.0205 355 ILE A N 2455 C CA . ILE A 314 ? 0.2522 0.2458 0.2976 0.0030 0.0209 -0.0176 355 ILE A CA 2456 C C . ILE A 314 ? 0.2622 0.2550 0.3083 0.0048 0.0256 -0.0108 355 ILE A C 2457 O O . ILE A 314 ? 0.2634 0.2583 0.3148 0.0033 0.0264 -0.0088 355 ILE A O 2458 C CB . ILE A 314 ? 0.2379 0.2359 0.2720 0.0041 0.0184 -0.0198 355 ILE A CB 2459 C CG1 . ILE A 314 ? 0.2251 0.2278 0.2571 0.0030 0.0171 -0.0186 355 ILE A CG1 2460 C CG2 . ILE A 314 ? 0.2435 0.2413 0.2760 0.0028 0.0148 -0.0262 355 ILE A CG2 2461 C CD1 . ILE A 314 ? 0.2339 0.2403 0.2550 0.0045 0.0159 -0.0189 355 ILE A CD1 2462 N N . TYR A 315 ? 0.2596 0.2494 0.2996 0.0084 0.0284 -0.0075 356 TYR A N 2463 C CA . TYR A 315 ? 0.2622 0.2494 0.3012 0.0111 0.0333 -0.0009 356 TYR A CA 2464 C C . TYR A 315 ? 0.2503 0.2378 0.2769 0.0154 0.0332 0.0009 356 TYR A C 2465 O O . TYR A 315 ? 0.2641 0.2491 0.2866 0.0179 0.0324 0.0001 356 TYR A O 2466 C CB . TYR A 315 ? 0.2690 0.2492 0.3143 0.0119 0.0373 0.0022 356 TYR A CB 2467 C CG . TYR A 315 ? 0.2887 0.2675 0.3483 0.0076 0.0374 0.0006 356 TYR A CG 2468 C CD1 . TYR A 315 ? 0.2859 0.2648 0.3550 0.0059 0.0413 0.0045 356 TYR A CD1 2469 C CD2 . TYR A 315 ? 0.2923 0.2701 0.3562 0.0055 0.0334 -0.0054 356 TYR A CD2 2470 C CE1 . TYR A 315 ? 0.2977 0.2757 0.3822 0.0018 0.0408 0.0026 356 TYR A CE1 2471 C CE2 . TYR A 315 ? 0.3019 0.2780 0.3798 0.0016 0.0325 -0.0077 356 TYR A CE2 2472 C CZ . TYR A 315 ? 0.2892 0.2658 0.3776 -0.0003 0.0358 -0.0038 356 TYR A CZ 2473 O OH . TYR A 315 ? 0.3421 0.3175 0.4465 -0.0044 0.0344 -0.0064 356 TYR A OH 2474 N N . ASN A 316 ? 0.2532 0.2431 0.2747 0.0168 0.0341 0.0036 357 ASN A N 2475 C CA . ASN A 316 ? 0.2545 0.2436 0.2648 0.0215 0.0340 0.0057 357 ASN A CA 2476 C C . ASN A 316 ? 0.2672 0.2503 0.2749 0.0252 0.0392 0.0119 357 ASN A C 2477 O O . ASN A 316 ? 0.3072 0.2893 0.3208 0.0240 0.0435 0.0152 357 ASN A O 2478 C CB . ASN A 316 ? 0.2451 0.2392 0.2502 0.0215 0.0319 0.0051 357 ASN A CB 2479 C CG . ASN A 316 ? 0.2607 0.2603 0.2664 0.0182 0.0272 -0.0002 357 ASN A CG 2480 O OD1 . ASN A 316 ? 0.2498 0.2499 0.2559 0.0174 0.0250 -0.0037 357 ASN A OD1 2481 N ND2 . ASN A 316 ? 0.2741 0.2778 0.2795 0.0167 0.0260 -0.0005 357 ASN A ND2 2482 N N . VAL A 317 ? 0.2602 0.2392 0.2593 0.0301 0.0391 0.0138 358 VAL A N 2483 C CA . VAL A 317 ? 0.2769 0.2496 0.2699 0.0347 0.0442 0.0202 358 VAL A CA 2484 C C . VAL A 317 ? 0.2814 0.2558 0.2630 0.0384 0.0426 0.0208 358 VAL A C 2485 O O . VAL A 317 ? 0.2835 0.2605 0.2596 0.0397 0.0372 0.0172 358 VAL A O 2486 C CB . VAL A 317 ? 0.2916 0.2573 0.2803 0.0389 0.0447 0.0224 358 VAL A CB 2487 C CG1 . VAL A 317 ? 0.3109 0.2688 0.2928 0.0438 0.0510 0.0299 358 VAL A CG1 2488 C CG2 . VAL A 317 ? 0.3065 0.2706 0.3059 0.0354 0.0447 0.0202 358 VAL A CG2 2489 N N . ILE A 318 ? 0.2910 0.2640 0.2700 0.0401 0.0473 0.0250 359 ILE A N 2490 C CA . ILE A 318 ? 0.2852 0.2593 0.2535 0.0437 0.0459 0.0252 359 ILE A CA 2491 C C . ILE A 318 ? 0.2959 0.2623 0.2537 0.0502 0.0513 0.0314 359 ILE A C 2492 O O . ILE A 318 ? 0.3150 0.2789 0.2770 0.0499 0.0584 0.0362 359 ILE A O 2493 C CB . ILE A 318 ? 0.2755 0.2559 0.2500 0.0400 0.0465 0.0239 359 ILE A CB 2494 C CG1 . ILE A 318 ? 0.2752 0.2623 0.2598 0.0336 0.0417 0.0183 359 ILE A CG1 2495 C CG2 . ILE A 318 ? 0.3071 0.2880 0.2702 0.0440 0.0446 0.0235 359 ILE A CG2 2496 C CD1 . ILE A 318 ? 0.3104 0.3005 0.2897 0.0338 0.0349 0.0135 359 ILE A CD1 2497 N N . GLY A 319 ? 0.3063 0.2688 0.2509 0.0559 0.0477 0.0312 360 GLY A N 2498 C CA . GLY A 319 ? 0.3247 0.2785 0.2556 0.0634 0.0521 0.0370 360 GLY A CA 2499 C C . GLY A 319 ? 0.3306 0.2846 0.2494 0.0678 0.0500 0.0360 360 GLY A C 2500 O O . GLY A 319 ? 0.3471 0.3060 0.2651 0.0668 0.0429 0.0305 360 GLY A O 2501 N N . THR A 320 ? 0.3451 0.2937 0.2549 0.0726 0.0566 0.0413 361 THR A N 2502 C CA . THR A 320 ? 0.3636 0.3117 0.2611 0.0773 0.0552 0.0402 361 THR A CA 2503 C C . THR A 320 ? 0.3856 0.3234 0.2637 0.0867 0.0567 0.0441 361 THR A C 2504 O O . THR A 320 ? 0.3967 0.3277 0.2714 0.0894 0.0642 0.0506 361 THR A O 2505 C CB . THR A 320 ? 0.3842 0.3354 0.2878 0.0751 0.0625 0.0426 361 THR A CB 2506 O OG1 . THR A 320 ? 0.3783 0.3385 0.2993 0.0668 0.0605 0.0390 361 THR A OG1 2507 C CG2 . THR A 320 ? 0.4065 0.3571 0.2981 0.0800 0.0615 0.0413 361 THR A CG2 2508 N N . LEU A 321 ? 0.3867 0.3231 0.2523 0.0916 0.0492 0.0401 362 LEU A N 2509 C CA . LEU A 321 ? 0.4105 0.3369 0.2547 0.1016 0.0494 0.0429 362 LEU A CA 2510 C C . LEU A 321 ? 0.4077 0.3353 0.2438 0.1044 0.0485 0.0404 362 LEU A C 2511 O O . LEU A 321 ? 0.3997 0.3312 0.2354 0.1040 0.0395 0.0338 362 LEU A O 2512 C CB . LEU A 321 ? 0.4147 0.3385 0.2522 0.1052 0.0393 0.0391 362 LEU A CB 2513 C CG . LEU A 321 ? 0.4816 0.3946 0.2958 0.1163 0.0370 0.0409 362 LEU A CG 2514 C CD1 . LEU A 321 ? 0.5347 0.4379 0.3379 0.1215 0.0480 0.0499 362 LEU A CD1 2515 C CD2 . LEU A 321 ? 0.4906 0.4018 0.3025 0.1190 0.0271 0.0375 362 LEU A CD2 2516 N N . ARG A 322 ? 0.4163 0.3407 0.2480 0.1069 0.0584 0.0456 363 ARG A N 2517 C CA A ARG A 322 ? 0.4222 0.3478 0.2476 0.1095 0.0594 0.0437 363 ARG A CA 2518 C CA B ARG A 322 ? 0.4306 0.3557 0.2553 0.1098 0.0598 0.0440 363 ARG A CA 2519 C C . ARG A 322 ? 0.4440 0.3628 0.2480 0.1185 0.0521 0.0401 363 ARG A C 2520 O O . ARG A 322 ? 0.4607 0.3699 0.2475 0.1265 0.0521 0.0430 363 ARG A O 2521 C CB A ARG A 322 ? 0.4333 0.3559 0.2578 0.1112 0.0727 0.0509 363 ARG A CB 2522 C CB B ARG A 322 ? 0.4474 0.3683 0.2686 0.1127 0.0732 0.0516 363 ARG A CB 2523 C CG A ARG A 322 ? 0.4314 0.3550 0.2503 0.1142 0.0754 0.0496 363 ARG A CG 2524 C CG B ARG A 322 ? 0.4636 0.3903 0.3058 0.1048 0.0815 0.0556 363 ARG A CG 2525 C CD A ARG A 322 ? 0.4844 0.4053 0.3039 0.1161 0.0895 0.0573 363 ARG A CD 2526 C CD B ARG A 322 ? 0.5575 0.4816 0.3982 0.1076 0.0945 0.0621 363 ARG A CD 2527 N NE A ARG A 322 ? 0.5773 0.4861 0.3753 0.1257 0.0948 0.0630 363 ARG A NE 2528 N NE B ARG A 322 ? 0.6005 0.5181 0.4413 0.1090 0.1045 0.0705 363 ARG A NE 2529 C CZ A ARG A 322 ? 0.6240 0.5270 0.4218 0.1267 0.1035 0.0708 363 ARG A CZ 2530 C CZ B ARG A 322 ? 0.6019 0.5236 0.4630 0.1019 0.1109 0.0740 363 ARG A CZ 2531 N NH1 A ARG A 322 ? 0.6237 0.5324 0.4433 0.1183 0.1078 0.0735 363 ARG A NH1 2532 N NH1 B ARG A 322 ? 0.6182 0.5329 0.4789 0.1036 0.1202 0.0819 363 ARG A NH1 2533 N NH2 A ARG A 322 ? 0.6475 0.5386 0.4229 0.1364 0.1079 0.0759 363 ARG A NH2 2534 N NH2 B ARG A 322 ? 0.5976 0.5300 0.4793 0.0933 0.1077 0.0695 363 ARG A NH2 2535 N N . GLY A 323 ? 0.4284 0.3520 0.2338 0.1173 0.0453 0.0336 364 GLY A N 2536 C CA . GLY A 323 ? 0.4373 0.3554 0.2251 0.1251 0.0371 0.0289 364 GLY A CA 2537 C C . GLY A 323 ? 0.4643 0.3735 0.2325 0.1343 0.0447 0.0329 364 GLY A C 2538 O O . GLY A 323 ? 0.4688 0.3795 0.2413 0.1330 0.0553 0.0373 364 GLY A O 2539 N N . ALA A 324 ? 0.4750 0.3748 0.2219 0.1438 0.0391 0.0313 365 ALA A N 2540 C CA . ALA A 324 ? 0.5092 0.3991 0.2335 0.1541 0.0452 0.0343 365 ALA A CA 2541 C C . ALA A 324 ? 0.5185 0.4099 0.2390 0.1561 0.0435 0.0292 365 ALA A C 2542 O O . ALA A 324 ? 0.5547 0.4404 0.2617 0.1626 0.0523 0.0325 365 ALA A O 2543 C CB . ALA A 324 ? 0.5144 0.3930 0.2158 0.1642 0.0388 0.0339 365 ALA A CB 2544 N N . VAL A 325 ? 0.4961 0.3939 0.2266 0.1514 0.0323 0.0211 366 VAL A N 2545 C CA . VAL A 325 ? 0.5154 0.4131 0.2405 0.1543 0.0285 0.0152 366 VAL A CA 2546 C C . VAL A 325 ? 0.4890 0.3984 0.2374 0.1441 0.0283 0.0125 366 VAL A C 2547 O O . VAL A 325 ? 0.4824 0.3934 0.2321 0.1444 0.0336 0.0124 366 VAL A O 2548 C CB . VAL A 325 ? 0.5453 0.4374 0.2573 0.1604 0.0139 0.0073 366 VAL A CB 2549 C CG1 . VAL A 325 ? 0.5405 0.4321 0.2483 0.1629 0.0094 0.0008 366 VAL A CG1 2550 C CG2 . VAL A 325 ? 0.5816 0.4609 0.2677 0.1719 0.0137 0.0099 366 VAL A CG2 2551 N N . GLU A 326 ? 0.4495 0.3667 0.2159 0.1353 0.0228 0.0107 367 GLU A N 2552 C CA . GLU A 326 ? 0.4351 0.3631 0.2234 0.1254 0.0223 0.0085 367 GLU A CA 2553 C C . GLU A 326 ? 0.3913 0.3259 0.1966 0.1172 0.0282 0.0134 367 GLU A C 2554 O O . GLU A 326 ? 0.3808 0.3213 0.1993 0.1105 0.0222 0.0108 367 GLU A O 2555 C CB . GLU A 326 ? 0.4376 0.3692 0.2326 0.1220 0.0094 0.0008 367 GLU A CB 2556 C CG . GLU A 326 ? 0.4747 0.3996 0.2545 0.1298 0.0020 -0.0052 367 GLU A CG 2557 C CD . GLU A 326 ? 0.4725 0.4020 0.2634 0.1250 -0.0098 -0.0125 367 GLU A CD 2558 O OE1 . GLU A 326 ? 0.4755 0.4104 0.2777 0.1198 -0.0096 -0.0144 367 GLU A OE1 2559 O OE2 . GLU A 326 ? 0.5033 0.4305 0.2912 0.1270 -0.0192 -0.0164 367 GLU A OE2 2560 N N . PRO A 327 ? 0.4026 0.3365 0.2091 0.1175 0.0401 0.0201 368 PRO A N 2561 C CA . PRO A 327 ? 0.3907 0.3302 0.2136 0.1100 0.0453 0.0244 368 PRO A CA 2562 C C . PRO A 327 ? 0.3738 0.3237 0.2175 0.1003 0.0434 0.0217 368 PRO A C 2563 O O . PRO A 327 ? 0.3628 0.3177 0.2203 0.0937 0.0444 0.0232 368 PRO A O 2564 C CB . PRO A 327 ? 0.4216 0.3573 0.2409 0.1132 0.0586 0.0320 368 PRO A CB 2565 C CG . PRO A 327 ? 0.4415 0.3739 0.2492 0.1196 0.0611 0.0309 368 PRO A CG 2566 C CD . PRO A 327 ? 0.4324 0.3596 0.2246 0.1253 0.0498 0.0245 368 PRO A CD 2567 N N . ASP A 328 ? 0.3601 0.3129 0.2052 0.1000 0.0402 0.0176 369 ASP A N 2568 C CA . ASP A 328 ? 0.3549 0.3168 0.2180 0.0915 0.0374 0.0149 369 ASP A CA 2569 C C . ASP A 328 ? 0.3388 0.3031 0.2048 0.0883 0.0263 0.0089 369 ASP A C 2570 O O . ASP A 328 ? 0.3249 0.2951 0.2016 0.0830 0.0226 0.0058 369 ASP A O 2571 C CB . ASP A 328 ? 0.3650 0.3287 0.2296 0.0925 0.0405 0.0142 369 ASP A CB 2572 C CG . ASP A 328 ? 0.4012 0.3600 0.2525 0.0986 0.0338 0.0090 369 ASP A CG 2573 O OD1 . ASP A 328 ? 0.4331 0.3853 0.2700 0.1043 0.0288 0.0070 369 ASP A OD1 2574 O OD2 . ASP A 328 ? 0.4421 0.4034 0.2972 0.0979 0.0331 0.0066 369 ASP A OD2 2575 N N . ARG A 329 ? 0.3417 0.3022 0.2006 0.0909 0.0210 0.0076 370 ARG A N 2576 C CA . ARG A 329 ? 0.3200 0.2841 0.1854 0.0869 0.0114 0.0025 370 ARG A CA 2577 C C . ARG A 329 ? 0.3261 0.2910 0.1960 0.0845 0.0116 0.0045 370 ARG A C 2578 O O . ARG A 329 ? 0.3427 0.3016 0.2026 0.0898 0.0144 0.0076 370 ARG A O 2579 C CB . ARG A 329 ? 0.3318 0.2902 0.1845 0.0934 0.0031 -0.0024 370 ARG A CB 2580 C CG . ARG A 329 ? 0.3200 0.2773 0.1690 0.0956 0.0021 -0.0052 370 ARG A CG 2581 C CD . ARG A 329 ? 0.3544 0.3190 0.2188 0.0879 -0.0029 -0.0088 370 ARG A CD 2582 N NE . ARG A 329 ? 0.3413 0.3053 0.2046 0.0891 -0.0039 -0.0113 370 ARG A NE 2583 C CZ . ARG A 329 ? 0.3165 0.2838 0.1858 0.0868 0.0023 -0.0089 370 ARG A CZ 2584 N NH1 . ARG A 329 ? 0.3153 0.2863 0.1913 0.0837 0.0106 -0.0038 370 ARG A NH1 2585 N NH2 . ARG A 329 ? 0.3389 0.3058 0.2085 0.0876 -0.0002 -0.0120 370 ARG A NH2 2586 N N . TYR A 330 ? 0.2997 0.2717 0.1844 0.0768 0.0094 0.0029 371 TYR A N 2587 C CA . TYR A 330 ? 0.2973 0.2707 0.1881 0.0739 0.0105 0.0047 371 TYR A CA 2588 C C . TYR A 330 ? 0.3052 0.2806 0.1996 0.0725 0.0023 0.0004 371 TYR A C 2589 O O . TYR A 330 ? 0.3052 0.2858 0.2080 0.0680 -0.0025 -0.0035 371 TYR A O 2590 C CB . TYR A 330 ? 0.2762 0.2563 0.1819 0.0660 0.0151 0.0064 371 TYR A CB 2591 C CG . TYR A 330 ? 0.2811 0.2611 0.1882 0.0659 0.0230 0.0103 371 TYR A CG 2592 C CD1 . TYR A 330 ? 0.3223 0.2961 0.2188 0.0723 0.0290 0.0144 371 TYR A CD1 2593 C CD2 . TYR A 330 ? 0.2814 0.2678 0.2010 0.0597 0.0248 0.0101 371 TYR A CD2 2594 C CE1 . TYR A 330 ? 0.3323 0.3067 0.2322 0.0720 0.0372 0.0182 371 TYR A CE1 2595 C CE2 . TYR A 330 ? 0.2947 0.2819 0.2181 0.0595 0.0317 0.0135 371 TYR A CE2 2596 C CZ . TYR A 330 ? 0.3142 0.2958 0.2289 0.0653 0.0383 0.0176 371 TYR A CZ 2597 O OH . TYR A 330 ? 0.3250 0.3082 0.2455 0.0649 0.0457 0.0210 371 TYR A OH 2598 N N . VAL A 331 ? 0.3013 0.2728 0.1907 0.0761 0.0010 0.0013 372 VAL A N 2599 C CA . VAL A 331 ? 0.2974 0.2716 0.1929 0.0745 -0.0057 -0.0022 372 VAL A CA 2600 C C . VAL A 331 ? 0.2906 0.2668 0.1941 0.0707 -0.0010 0.0007 372 VAL A C 2601 O O . VAL A 331 ? 0.3110 0.2824 0.2089 0.0737 0.0042 0.0051 372 VAL A O 2602 C CB . VAL A 331 ? 0.3407 0.3084 0.2241 0.0824 -0.0118 -0.0038 372 VAL A CB 2603 C CG1 . VAL A 331 ? 0.3180 0.2892 0.2100 0.0808 -0.0181 -0.0072 372 VAL A CG1 2604 C CG2 . VAL A 331 ? 0.3343 0.2995 0.2098 0.0864 -0.0173 -0.0077 372 VAL A CG2 2605 N N . ILE A 332 ? 0.2679 0.2510 0.1846 0.0641 -0.0024 -0.0017 373 ILE A N 2606 C CA . ILE A 332 ? 0.2766 0.2619 0.2015 0.0599 0.0022 0.0004 373 ILE A CA 2607 C C . ILE A 332 ? 0.2748 0.2615 0.2046 0.0599 -0.0019 -0.0020 373 ILE A C 2608 O O . ILE A 332 ? 0.2847 0.2757 0.2199 0.0582 -0.0073 -0.0061 373 ILE A O 2609 C CB . ILE A 332 ? 0.2546 0.2463 0.1901 0.0525 0.0047 -0.0003 373 ILE A CB 2610 C CG1 . ILE A 332 ? 0.2928 0.2837 0.2249 0.0528 0.0084 0.0018 373 ILE A CG1 2611 C CG2 . ILE A 332 ? 0.2755 0.2689 0.2193 0.0484 0.0090 0.0012 373 ILE A CG2 2612 C CD1 . ILE A 332 ? 0.3407 0.3378 0.2823 0.0463 0.0090 0.0005 373 ILE A CD1 2613 N N . LEU A 333 ? 0.2704 0.2535 0.1991 0.0619 0.0007 0.0006 374 LEU A N 2614 C CA . LEU A 333 ? 0.2551 0.2401 0.1907 0.0612 -0.0021 -0.0015 374 LEU A CA 2615 C C . LEU A 333 ? 0.2640 0.2512 0.2082 0.0560 0.0033 -0.0001 374 LEU A C 2616 O O . LEU A 333 ? 0.2811 0.2637 0.2227 0.0570 0.0086 0.0040 374 LEU A O 2617 C CB . LEU A 333 ? 0.2868 0.2646 0.2131 0.0685 -0.0040 0.0004 374 LEU A CB 2618 C CG . LEU A 333 ? 0.2843 0.2632 0.2175 0.0689 -0.0066 -0.0012 374 LEU A CG 2619 C CD1 . LEU A 333 ? 0.3183 0.3039 0.2600 0.0673 -0.0133 -0.0068 374 LEU A CD1 2620 C CD2 . LEU A 333 ? 0.3279 0.2979 0.2497 0.0770 -0.0081 0.0017 374 LEU A CD2 2621 N N . GLY A 334 ? 0.2640 0.2576 0.2184 0.0508 0.0022 -0.0035 375 GLY A N 2622 C CA . GLY A 334 ? 0.2489 0.2445 0.2109 0.0457 0.0069 -0.0029 375 GLY A CA 2623 C C . GLY A 334 ? 0.2659 0.2652 0.2359 0.0437 0.0052 -0.0063 375 GLY A C 2624 O O . GLY A 334 ? 0.2697 0.2734 0.2432 0.0433 0.0014 -0.0095 375 GLY A O 2625 N N . GLY A 335 ? 0.2609 0.2586 0.2350 0.0422 0.0086 -0.0056 376 GLY A N 2626 C CA . GLY A 335 ? 0.2544 0.2559 0.2363 0.0400 0.0080 -0.0091 376 GLY A CA 2627 C C . GLY A 335 ? 0.2546 0.2543 0.2406 0.0370 0.0122 -0.0086 376 GLY A C 2628 O O . GLY A 335 ? 0.2756 0.2705 0.2593 0.0376 0.0152 -0.0051 376 GLY A O 2629 N N . HIS A 336 ? 0.2438 0.2469 0.2360 0.0342 0.0125 -0.0121 377 HIS A N 2630 C CA . HIS A 336 ? 0.2437 0.2447 0.2396 0.0313 0.0156 -0.0124 377 HIS A CA 2631 C C . HIS A 336 ? 0.2526 0.2484 0.2508 0.0341 0.0167 -0.0119 377 HIS A C 2632 O O . HIS A 336 ? 0.2762 0.2710 0.2738 0.0382 0.0148 -0.0119 377 HIS A O 2633 C CB . HIS A 336 ? 0.2389 0.2452 0.2384 0.0269 0.0157 -0.0166 377 HIS A CB 2634 C CG . HIS A 336 ? 0.2375 0.2467 0.2408 0.0275 0.0152 -0.0203 377 HIS A CG 2635 N ND1 . HIS A 336 ? 0.2423 0.2501 0.2492 0.0266 0.0169 -0.0230 377 HIS A ND1 2636 C CD2 . HIS A 336 ? 0.2152 0.2294 0.2202 0.0281 0.0136 -0.0222 377 HIS A CD2 2637 C CE1 . HIS A 336 ? 0.2624 0.2740 0.2724 0.0273 0.0168 -0.0262 377 HIS A CE1 2638 N NE2 . HIS A 336 ? 0.2456 0.2613 0.2552 0.0280 0.0150 -0.0256 377 HIS A NE2 2639 N N . ARG A 337 ? 0.2517 0.2443 0.2532 0.0317 0.0195 -0.0115 378 ARG A N 2640 C CA . ARG A 337 ? 0.2565 0.2427 0.2610 0.0336 0.0212 -0.0104 378 ARG A CA 2641 C C . ARG A 337 ? 0.2599 0.2468 0.2705 0.0309 0.0216 -0.0150 378 ARG A C 2642 O O . ARG A 337 ? 0.2637 0.2469 0.2773 0.0331 0.0218 -0.0160 378 ARG A O 2643 C CB . ARG A 337 ? 0.2789 0.2597 0.2834 0.0331 0.0245 -0.0057 378 ARG A CB 2644 C CG . ARG A 337 ? 0.2943 0.2674 0.3019 0.0351 0.0268 -0.0033 378 ARG A CG 2645 C CD . ARG A 337 ? 0.3143 0.2826 0.3236 0.0338 0.0310 0.0017 378 ARG A CD 2646 N NE . ARG A 337 ? 0.2929 0.2641 0.3099 0.0281 0.0315 -0.0010 378 ARG A NE 2647 C CZ . ARG A 337 ? 0.2770 0.2526 0.2940 0.0253 0.0316 -0.0008 378 ARG A CZ 2648 N NH1 . ARG A 337 ? 0.2681 0.2458 0.2778 0.0273 0.0318 0.0021 378 ARG A NH1 2649 N NH2 . ARG A 337 ? 0.2829 0.2606 0.3071 0.0206 0.0311 -0.0038 378 ARG A NH2 2650 N N . ASP A 338 ? 0.2470 0.2381 0.2588 0.0266 0.0213 -0.0181 379 ASP A N 2651 C CA . ASP A 338 ? 0.2424 0.2336 0.2582 0.0243 0.0214 -0.0231 379 ASP A CA 2652 C C . ASP A 338 ? 0.2509 0.2455 0.2668 0.0263 0.0207 -0.0267 379 ASP A C 2653 O O . ASP A 338 ? 0.2586 0.2582 0.2722 0.0272 0.0196 -0.0265 379 ASP A O 2654 C CB . ASP A 338 ? 0.2376 0.2320 0.2529 0.0200 0.0208 -0.0251 379 ASP A CB 2655 C CG . ASP A 338 ? 0.2427 0.2436 0.2534 0.0192 0.0196 -0.0260 379 ASP A CG 2656 O OD1 . ASP A 338 ? 0.2404 0.2431 0.2483 0.0204 0.0191 -0.0227 379 ASP A OD1 2657 O OD2 . ASP A 338 ? 0.2360 0.2398 0.2455 0.0174 0.0192 -0.0300 379 ASP A OD2 2658 N N . SER A 339 ? 0.2580 0.2502 0.2776 0.0268 0.0213 -0.0304 380 SER A N 2659 C CA . SER A 339 ? 0.2636 0.2589 0.2845 0.0290 0.0215 -0.0341 380 SER A CA 2660 C C . SER A 339 ? 0.2689 0.2642 0.2904 0.0271 0.0224 -0.0395 380 SER A C 2661 O O . SER A 339 ? 0.2854 0.2766 0.3073 0.0247 0.0221 -0.0407 380 SER A O 2662 C CB . SER A 339 ? 0.2748 0.2660 0.2992 0.0335 0.0213 -0.0329 380 SER A CB 2663 O OG . SER A 339 ? 0.2875 0.2712 0.3148 0.0335 0.0221 -0.0328 380 SER A OG 2664 N N . TRP A 340 ? 0.2655 0.2648 0.2873 0.0284 0.0235 -0.0432 381 TRP A N 2665 C CA . TRP A 340 ? 0.2652 0.2636 0.2859 0.0276 0.0247 -0.0487 381 TRP A CA 2666 C C . TRP A 340 ? 0.2886 0.2804 0.3139 0.0299 0.0248 -0.0508 381 TRP A C 2667 O O . TRP A 340 ? 0.2857 0.2729 0.3109 0.0284 0.0242 -0.0539 381 TRP A O 2668 C CB . TRP A 340 ? 0.2855 0.2903 0.3049 0.0284 0.0271 -0.0517 381 TRP A CB 2669 C CG . TRP A 340 ? 0.2789 0.2880 0.2923 0.0252 0.0272 -0.0506 381 TRP A CG 2670 C CD1 . TRP A 340 ? 0.2820 0.2973 0.2954 0.0247 0.0277 -0.0480 381 TRP A CD1 2671 C CD2 . TRP A 340 ? 0.2659 0.2731 0.2732 0.0222 0.0262 -0.0520 381 TRP A CD2 2672 N NE1 . TRP A 340 ? 0.2921 0.3091 0.2993 0.0216 0.0276 -0.0473 381 TRP A NE1 2673 C CE2 . TRP A 340 ? 0.2778 0.2901 0.2808 0.0202 0.0265 -0.0498 381 TRP A CE2 2674 C CE3 . TRP A 340 ? 0.2894 0.2910 0.2950 0.0212 0.0245 -0.0552 381 TRP A CE3 2675 C CZ2 . TRP A 340 ? 0.2870 0.2987 0.2833 0.0174 0.0251 -0.0503 381 TRP A CZ2 2676 C CZ3 . TRP A 340 ? 0.2721 0.2734 0.2715 0.0183 0.0227 -0.0561 381 TRP A CZ3 2677 C CH2 . TRP A 340 ? 0.2847 0.2911 0.2793 0.0167 0.0230 -0.0534 381 TRP A CH2 2678 N N . VAL A 341 ? 0.2848 0.2759 0.3147 0.0336 0.0250 -0.0493 382 VAL A N 2679 C CA . VAL A 341 ? 0.2931 0.2770 0.3278 0.0361 0.0249 -0.0505 382 VAL A CA 2680 C C . VAL A 341 ? 0.2908 0.2713 0.3277 0.0387 0.0238 -0.0446 382 VAL A C 2681 O O . VAL A 341 ? 0.2848 0.2624 0.3201 0.0369 0.0232 -0.0403 382 VAL A O 2682 C CB . VAL A 341 ? 0.3056 0.2903 0.3432 0.0392 0.0267 -0.0561 382 VAL A CB 2683 C CG1 . VAL A 341 ? 0.3218 0.2974 0.3638 0.0411 0.0262 -0.0581 382 VAL A CG1 2684 C CG2 . VAL A 341 ? 0.3358 0.3234 0.3685 0.0373 0.0283 -0.0616 382 VAL A CG2 2685 N N . PHE A 342 ? 0.2790 0.2599 0.3194 0.0432 0.0235 -0.0444 383 PHE A N 2686 C CA . PHE A 342 ? 0.2892 0.2656 0.3299 0.0464 0.0219 -0.0389 383 PHE A CA 2687 C C . PHE A 342 ? 0.2940 0.2753 0.3308 0.0468 0.0203 -0.0349 383 PHE A C 2688 O O . PHE A 342 ? 0.3140 0.2909 0.3480 0.0488 0.0191 -0.0297 383 PHE A O 2689 C CB . PHE A 342 ? 0.2943 0.2680 0.3404 0.0517 0.0213 -0.0402 383 PHE A CB 2690 C CG . PHE A 342 ? 0.3081 0.2757 0.3582 0.0518 0.0227 -0.0443 383 PHE A CG 2691 C CD1 . PHE A 342 ? 0.3252 0.2834 0.3760 0.0507 0.0231 -0.0418 383 PHE A CD1 2692 C CD2 . PHE A 342 ? 0.3324 0.3039 0.3857 0.0526 0.0241 -0.0508 383 PHE A CD2 2693 C CE1 . PHE A 342 ? 0.3370 0.2890 0.3924 0.0507 0.0238 -0.0464 383 PHE A CE1 2694 C CE2 . PHE A 342 ? 0.3051 0.2703 0.3614 0.0531 0.0252 -0.0555 383 PHE A CE2 2695 C CZ . PHE A 342 ? 0.3283 0.2840 0.3857 0.0519 0.0246 -0.0534 383 PHE A CZ 2696 N N . GLY A 343 ? 0.2829 0.2727 0.3192 0.0451 0.0203 -0.0372 384 GLY A N 2697 C CA . GLY A 343 ? 0.2750 0.2694 0.3079 0.0450 0.0183 -0.0340 384 GLY A CA 2698 C C . GLY A 343 ? 0.2797 0.2739 0.3140 0.0503 0.0151 -0.0318 384 GLY A C 2699 O O . GLY A 343 ? 0.2769 0.2708 0.3065 0.0513 0.0127 -0.0280 384 GLY A O 2700 N N . GLY A 344 ? 0.2893 0.2840 0.3301 0.0539 0.0146 -0.0345 385 GLY A N 2701 C CA . GLY A 344 ? 0.2918 0.2857 0.3346 0.0595 0.0108 -0.0328 385 GLY A CA 2702 C C . GLY A 344 ? 0.2825 0.2831 0.3250 0.0599 0.0074 -0.0322 385 GLY A C 2703 O O . GLY A 344 ? 0.2954 0.2930 0.3340 0.0637 0.0033 -0.0290 385 GLY A O 2704 N N . ILE A 345 ? 0.2653 0.2742 0.3113 0.0562 0.0089 -0.0352 386 ILE A N 2705 C CA . ILE A 345 ? 0.2602 0.2747 0.3059 0.0555 0.0059 -0.0344 386 ILE A CA 2706 C C . ILE A 345 ? 0.2594 0.2733 0.2969 0.0506 0.0077 -0.0323 386 ILE A C 2707 O O . ILE A 345 ? 0.2660 0.2777 0.2972 0.0513 0.0051 -0.0290 386 ILE A O 2708 C CB . ILE A 345 ? 0.2444 0.2686 0.3008 0.0547 0.0065 -0.0385 386 ILE A CB 2709 C CG1 . ILE A 345 ? 0.2929 0.3180 0.3585 0.0604 0.0035 -0.0403 386 ILE A CG1 2710 C CG2 . ILE A 345 ? 0.2616 0.2913 0.3183 0.0527 0.0040 -0.0378 386 ILE A CG2 2711 C CD1 . ILE A 345 ? 0.3078 0.3426 0.3867 0.0600 0.0050 -0.0444 386 ILE A CD1 2712 N N . ASP A 346 ? 0.2547 0.2705 0.2921 0.0462 0.0120 -0.0343 387 ASP A N 2713 C CA . ASP A 346 ? 0.2493 0.2660 0.2804 0.0416 0.0131 -0.0327 387 ASP A CA 2714 C C . ASP A 346 ? 0.2536 0.2632 0.2793 0.0400 0.0151 -0.0310 387 ASP A C 2715 O O . ASP A 346 ? 0.2567 0.2652 0.2839 0.0383 0.0178 -0.0338 387 ASP A O 2716 C CB . ASP A 346 ? 0.2607 0.2838 0.2950 0.0380 0.0163 -0.0361 387 ASP A CB 2717 C CG . ASP A 346 ? 0.2669 0.2913 0.2954 0.0337 0.0172 -0.0349 387 ASP A CG 2718 O OD1 . ASP A 346 ? 0.2439 0.2651 0.2671 0.0333 0.0153 -0.0317 387 ASP A OD1 2719 O OD2 . ASP A 346 ? 0.2461 0.2743 0.2750 0.0309 0.0202 -0.0372 387 ASP A OD2 2720 N N . PRO A 347 ? 0.2477 0.2526 0.2676 0.0404 0.0140 -0.0268 388 PRO A N 2721 C CA . PRO A 347 ? 0.2406 0.2458 0.2563 0.0423 0.0109 -0.0237 388 PRO A CA 2722 C C . PRO A 347 ? 0.2663 0.2651 0.2790 0.0477 0.0088 -0.0204 388 PRO A C 2723 O O . PRO A 347 ? 0.2705 0.2680 0.2775 0.0501 0.0062 -0.0177 388 PRO A O 2724 C CB . PRO A 347 ? 0.2404 0.2440 0.2503 0.0388 0.0125 -0.0211 388 PRO A CB 2725 C CG . PRO A 347 ? 0.2490 0.2467 0.2600 0.0377 0.0155 -0.0206 388 PRO A CG 2726 C CD . PRO A 347 ? 0.2507 0.2501 0.2677 0.0378 0.0163 -0.0251 388 PRO A CD 2727 N N . GLN A 348 ? 0.2776 0.2714 0.2928 0.0501 0.0099 -0.0204 389 GLN A N 2728 C CA . GLN A 348 ? 0.2843 0.2700 0.2944 0.0549 0.0088 -0.0160 389 GLN A CA 2729 C C . GLN A 348 ? 0.2904 0.2765 0.2985 0.0606 0.0036 -0.0155 389 GLN A C 2730 O O . GLN A 348 ? 0.2971 0.2768 0.2972 0.0648 0.0022 -0.0112 389 GLN A O 2731 C CB . GLN A 348 ? 0.2896 0.2686 0.3029 0.0563 0.0111 -0.0156 389 GLN A CB 2732 C CG . GLN A 348 ? 0.2843 0.2617 0.3003 0.0510 0.0154 -0.0165 389 GLN A CG 2733 C CD . GLN A 348 ? 0.2727 0.2487 0.2838 0.0475 0.0175 -0.0130 389 GLN A CD 2734 O OE1 . GLN A 348 ? 0.3077 0.2823 0.3122 0.0494 0.0168 -0.0090 389 GLN A OE1 2735 N NE2 . GLN A 348 ? 0.2966 0.2729 0.3113 0.0426 0.0200 -0.0149 389 GLN A NE2 2736 N N . SER A 349 ? 0.2812 0.2748 0.2964 0.0609 0.0007 -0.0197 390 SER A N 2737 C CA A SER A 349 ? 0.2976 0.2923 0.3121 0.0660 -0.0054 -0.0199 390 SER A CA 2738 C CA B SER A 349 ? 0.3012 0.2965 0.3162 0.0657 -0.0054 -0.0201 390 SER A CA 2739 C C . SER A 349 ? 0.2925 0.2871 0.2984 0.0657 -0.0075 -0.0177 390 SER A C 2740 O O . SER A 349 ? 0.3103 0.3014 0.3100 0.0710 -0.0124 -0.0162 390 SER A O 2741 C CB A SER A 349 ? 0.2964 0.2999 0.3230 0.0660 -0.0078 -0.0250 390 SER A CB 2742 C CB B SER A 349 ? 0.2984 0.3032 0.3254 0.0645 -0.0070 -0.0254 390 SER A CB 2743 O OG A SER A 349 ? 0.2717 0.2830 0.3021 0.0607 -0.0063 -0.0273 390 SER A OG 2744 O OG B SER A 349 ? 0.3065 0.3154 0.3349 0.0666 -0.0127 -0.0265 390 SER A OG 2745 N N . GLY A 350 ? 0.2759 0.2736 0.2807 0.0601 -0.0041 -0.0177 391 GLY A N 2746 C CA . GLY A 350 ? 0.2671 0.2639 0.2632 0.0598 -0.0054 -0.0154 391 GLY A CA 2747 C C . GLY A 350 ? 0.2739 0.2620 0.2598 0.0616 -0.0024 -0.0102 391 GLY A C 2748 O O . GLY A 350 ? 0.2865 0.2703 0.2629 0.0657 -0.0047 -0.0075 391 GLY A O 2749 N N . ALA A 351 ? 0.2693 0.2547 0.2572 0.0586 0.0029 -0.0088 392 ALA A N 2750 C CA . ALA A 351 ? 0.2866 0.2643 0.2674 0.0593 0.0069 -0.0035 392 ALA A CA 2751 C C . ALA A 351 ? 0.2983 0.2673 0.2716 0.0664 0.0056 0.0006 392 ALA A C 2752 O O . ALA A 351 ? 0.3084 0.2714 0.2720 0.0691 0.0074 0.0054 392 ALA A O 2753 C CB . ALA A 351 ? 0.2874 0.2641 0.2743 0.0545 0.0121 -0.0035 392 ALA A CB 2754 N N . ALA A 352 ? 0.2992 0.2677 0.2764 0.0699 0.0023 -0.0014 393 ALA A N 2755 C CA . ALA A 352 ? 0.3097 0.2697 0.2796 0.0772 0.0001 0.0022 393 ALA A CA 2756 C C . ALA A 352 ? 0.3254 0.2845 0.2851 0.0822 -0.0051 0.0028 393 ALA A C 2757 O O . ALA A 352 ? 0.3369 0.2873 0.2845 0.0880 -0.0052 0.0076 393 ALA A O 2758 C CB . ALA A 352 ? 0.3252 0.2862 0.3035 0.0798 -0.0031 -0.0011 393 ALA A CB 2759 N N . VAL A 353 ? 0.3169 0.2846 0.2811 0.0801 -0.0094 -0.0020 394 VAL A N 2760 C CA . VAL A 353 ? 0.3243 0.2916 0.2798 0.0846 -0.0154 -0.0025 394 VAL A CA 2761 C C . VAL A 353 ? 0.3267 0.2901 0.2707 0.0841 -0.0116 0.0015 394 VAL A C 2762 O O . VAL A 353 ? 0.3333 0.2897 0.2634 0.0904 -0.0138 0.0043 394 VAL A O 2763 C CB . VAL A 353 ? 0.3144 0.2919 0.2804 0.0820 -0.0207 -0.0087 394 VAL A CB 2764 C CG1 . VAL A 353 ? 0.3277 0.3060 0.2862 0.0836 -0.0253 -0.0097 394 VAL A CG1 2765 C CG2 . VAL A 353 ? 0.3127 0.2923 0.2872 0.0859 -0.0265 -0.0121 394 VAL A CG2 2766 N N . VAL A 354 ? 0.3173 0.2847 0.2664 0.0771 -0.0059 0.0016 395 VAL A N 2767 C CA . VAL A 354 ? 0.3143 0.2786 0.2547 0.0763 -0.0014 0.0054 395 VAL A CA 2768 C C . VAL A 354 ? 0.3362 0.2899 0.2666 0.0810 0.0031 0.0120 395 VAL A C 2769 O O . VAL A 354 ? 0.3367 0.2849 0.2546 0.0853 0.0040 0.0154 395 VAL A O 2770 C CB . VAL A 354 ? 0.3053 0.2751 0.2541 0.0683 0.0038 0.0047 395 VAL A CB 2771 C CG1 . VAL A 354 ? 0.3265 0.2928 0.2671 0.0682 0.0087 0.0091 395 VAL A CG1 2772 C CG2 . VAL A 354 ? 0.3139 0.2932 0.2704 0.0640 0.0001 -0.0008 395 VAL A CG2 2773 N N . HIS A 355 ? 0.3368 0.2872 0.2727 0.0806 0.0060 0.0136 396 HIS A N 2774 C CA . HIS A 355 ? 0.3436 0.2836 0.2720 0.0843 0.0112 0.0204 396 HIS A CA 2775 C C . HIS A 355 ? 0.3701 0.3022 0.2831 0.0936 0.0070 0.0231 396 HIS A C 2776 O O . HIS A 355 ? 0.3944 0.3186 0.2947 0.0977 0.0111 0.0288 396 HIS A O 2777 C CB . HIS A 355 ? 0.3559 0.2940 0.2944 0.0822 0.0136 0.0206 396 HIS A CB 2778 C CG . HIS A 355 ? 0.3600 0.2910 0.2988 0.0808 0.0218 0.0267 396 HIS A CG 2779 N ND1 . HIS A 355 ? 0.3674 0.3005 0.3093 0.0756 0.0276 0.0284 396 HIS A ND1 2780 C CD2 . HIS A 355 ? 0.4004 0.3224 0.3390 0.0834 0.0250 0.0312 396 HIS A CD2 2781 C CE1 . HIS A 355 ? 0.3897 0.3158 0.3342 0.0749 0.0342 0.0336 396 HIS A CE1 2782 N NE2 . HIS A 355 ? 0.3857 0.3047 0.3280 0.0795 0.0329 0.0356 396 HIS A NE2 2783 N N . GLU A 356 ? 0.3623 0.2966 0.2765 0.0972 -0.0011 0.0188 397 GLU A N 2784 C CA . GLU A 356 ? 0.3797 0.3064 0.2792 0.1067 -0.0069 0.0205 397 GLU A CA 2785 C C . GLU A 356 ? 0.3931 0.3200 0.2810 0.1093 -0.0095 0.0197 397 GLU A C 2786 O O . GLU A 356 ? 0.4177 0.3354 0.2885 0.1169 -0.0104 0.0235 397 GLU A O 2787 C CB . GLU A 356 ? 0.3891 0.3194 0.2962 0.1094 -0.0156 0.0153 397 GLU A CB 2788 C CG . GLU A 356 ? 0.3976 0.3206 0.2909 0.1196 -0.0237 0.0158 397 GLU A CG 2789 C CD . GLU A 356 ? 0.4705 0.3799 0.3493 0.1265 -0.0201 0.0234 397 GLU A CD 2790 O OE1 . GLU A 356 ? 0.4684 0.3734 0.3477 0.1234 -0.0106 0.0290 397 GLU A OE1 2791 O OE2 . GLU A 356 ? 0.4761 0.3790 0.3436 0.1353 -0.0272 0.0238 397 GLU A OE2 2792 N N . ILE A 357 ? 0.3671 0.3035 0.2631 0.1032 -0.0106 0.0150 398 ILE A N 2793 C CA . ILE A 357 ? 0.3674 0.3037 0.2528 0.1053 -0.0126 0.0142 398 ILE A CA 2794 C C . ILE A 357 ? 0.3851 0.3145 0.2591 0.1064 -0.0039 0.0208 398 ILE A C 2795 O O . ILE A 357 ? 0.3911 0.3134 0.2483 0.1132 -0.0046 0.0232 398 ILE A O 2796 C CB . ILE A 357 ? 0.3427 0.2904 0.2404 0.0982 -0.0152 0.0081 398 ILE A CB 2797 C CG1 . ILE A 357 ? 0.3418 0.2952 0.2482 0.0992 -0.0247 0.0018 398 ILE A CG1 2798 C CG2 . ILE A 357 ? 0.3400 0.2871 0.2282 0.0989 -0.0147 0.0083 398 ILE A CG2 2799 C CD1 . ILE A 357 ? 0.3422 0.3070 0.2642 0.0913 -0.0258 -0.0035 398 ILE A CD1 2800 N N . VAL A 358 ? 0.3757 0.3069 0.2588 0.1001 0.0046 0.0237 399 VAL A N 2801 C CA . VAL A 358 ? 0.3962 0.3214 0.2718 0.1006 0.0140 0.0304 399 VAL A CA 2802 C C . VAL A 358 ? 0.4078 0.3204 0.2679 0.1091 0.0164 0.0370 399 VAL A C 2803 O O . VAL A 358 ? 0.4443 0.3501 0.2890 0.1144 0.0200 0.0413 399 VAL A O 2804 C CB . VAL A 358 ? 0.3788 0.3076 0.2690 0.0924 0.0219 0.0323 399 VAL A CB 2805 C CG1 . VAL A 358 ? 0.4023 0.3247 0.2865 0.0933 0.0320 0.0398 399 VAL A CG1 2806 C CG2 . VAL A 358 ? 0.3813 0.3215 0.2846 0.0844 0.0202 0.0266 399 VAL A CG2 2807 N N . ARG A 359 ? 0.4060 0.3150 0.2695 0.1108 0.0146 0.0379 400 ARG A N 2808 C CA . ARG A 359 ? 0.4297 0.3259 0.2781 0.1194 0.0163 0.0444 400 ARG A CA 2809 C C . ARG A 359 ? 0.4536 0.3442 0.2822 0.1288 0.0096 0.0437 400 ARG A C 2810 O O . ARG A 359 ? 0.4794 0.3594 0.2903 0.1356 0.0142 0.0501 400 ARG A O 2811 C CB . ARG A 359 ? 0.4291 0.3231 0.2850 0.1202 0.0132 0.0441 400 ARG A CB 2812 C CG . ARG A 359 ? 0.4500 0.3297 0.2924 0.1279 0.0173 0.0524 400 ARG A CG 2813 C CD . ARG A 359 ? 0.4863 0.3633 0.3334 0.1311 0.0111 0.0510 400 ARG A CD 2814 N NE . ARG A 359 ? 0.4951 0.3756 0.3383 0.1359 -0.0010 0.0445 400 ARG A NE 2815 C CZ . ARG A 359 ? 0.5298 0.4026 0.3539 0.1456 -0.0067 0.0457 400 ARG A CZ 2816 N NH1 . ARG A 359 ? 0.5290 0.4065 0.3533 0.1489 -0.0184 0.0388 400 ARG A NH1 2817 N NH2 . ARG A 359 ? 0.5337 0.3940 0.3385 0.1522 -0.0009 0.0538 400 ARG A NH2 2818 N N . SER A 360 ? 0.4497 0.3469 0.2811 0.1293 -0.0010 0.0360 401 SER A N 2819 C CA . SER A 360 ? 0.4814 0.3735 0.2950 0.1383 -0.0091 0.0341 401 SER A CA 2820 C C . SER A 360 ? 0.4852 0.3755 0.2866 0.1396 -0.0050 0.0354 401 SER A C 2821 O O . SER A 360 ? 0.5089 0.3888 0.2891 0.1485 -0.0045 0.0391 401 SER A O 2822 C CB . SER A 360 ? 0.4699 0.3701 0.2922 0.1379 -0.0215 0.0251 401 SER A CB 2823 O OG A SER A 360 ? 0.4453 0.3394 0.2498 0.1471 -0.0300 0.0230 401 SER A OG 2824 O OG B SER A 360 ? 0.5155 0.4160 0.3465 0.1388 -0.0257 0.0241 401 SER A OG 2825 N N . PHE A 361 ? 0.4622 0.3621 0.2762 0.1312 -0.0016 0.0326 402 PHE A N 2826 C CA . PHE A 361 ? 0.4696 0.3680 0.2730 0.1326 0.0029 0.0341 402 PHE A CA 2827 C C . PHE A 361 ? 0.5104 0.3990 0.3022 0.1361 0.0144 0.0433 402 PHE A C 2828 O O . PHE A 361 ? 0.5239 0.4055 0.2977 0.1427 0.0170 0.0460 402 PHE A O 2829 C CB . PHE A 361 ? 0.4433 0.3533 0.2631 0.1228 0.0054 0.0304 402 PHE A CB 2830 C CG . PHE A 361 ? 0.4178 0.3354 0.2430 0.1210 -0.0047 0.0220 402 PHE A CG 2831 C CD1 . PHE A 361 ? 0.4533 0.3673 0.2641 0.1274 -0.0107 0.0190 402 PHE A CD1 2832 C CD2 . PHE A 361 ? 0.4245 0.3528 0.2696 0.1128 -0.0079 0.0171 402 PHE A CD2 2833 C CE1 . PHE A 361 ? 0.4459 0.3668 0.2635 0.1255 -0.0201 0.0113 402 PHE A CE1 2834 C CE2 . PHE A 361 ? 0.4124 0.3478 0.2639 0.1108 -0.0165 0.0098 402 PHE A CE2 2835 C CZ . PHE A 361 ? 0.4374 0.3691 0.2759 0.1169 -0.0227 0.0069 402 PHE A CZ 2836 N N . GLY A 362 ? 0.4988 0.3867 0.3012 0.1318 0.0216 0.0481 403 GLY A N 2837 C CA . GLY A 362 ? 0.5186 0.3976 0.3134 0.1341 0.0336 0.0574 403 GLY A CA 2838 C C . GLY A 362 ? 0.5584 0.4232 0.3298 0.1457 0.0332 0.0629 403 GLY A C 2839 O O . GLY A 362 ? 0.5900 0.4462 0.3474 0.1505 0.0422 0.0700 403 GLY A O 2840 N N . THR A 363 ? 0.5667 0.4289 0.3339 0.1504 0.0230 0.0597 404 THR A N 2841 C CA . THR A 363 ? 0.5883 0.4367 0.3318 0.1624 0.0203 0.0639 404 THR A CA 2842 C C . THR A 363 ? 0.6095 0.4530 0.3310 0.1703 0.0179 0.0628 404 THR A C 2843 O O . THR A 363 ? 0.6351 0.4658 0.3342 0.1792 0.0235 0.0698 404 THR A O 2844 C CB . THR A 363 ? 0.5926 0.4405 0.3382 0.1659 0.0079 0.0595 404 THR A CB 2845 O OG1 A THR A 363 ? 0.5901 0.4402 0.3533 0.1600 0.0114 0.0616 404 THR A OG1 2846 O OG1 B THR A 363 ? 0.5798 0.4343 0.3256 0.1672 -0.0048 0.0501 404 THR A OG1 2847 C CG2 A THR A 363 ? 0.6044 0.4379 0.3245 0.1788 0.0038 0.0633 404 THR A CG2 2848 C CG2 B THR A 363 ? 0.5789 0.4335 0.3480 0.1575 0.0093 0.0587 404 THR A CG2 2849 N N . LEU A 364 ? 0.5939 0.4465 0.3210 0.1674 0.0102 0.0543 405 LEU A N 2850 C CA . LEU A 364 ? 0.6020 0.4507 0.3101 0.1741 0.0077 0.0521 405 LEU A CA 2851 C C . LEU A 364 ? 0.6096 0.4559 0.3126 0.1730 0.0219 0.0586 405 LEU A C 2852 O O . LEU A 364 ? 0.6071 0.4432 0.2870 0.1820 0.0256 0.0625 405 LEU A O 2853 C CB . LEU A 364 ? 0.5964 0.4563 0.3154 0.1698 -0.0032 0.0415 405 LEU A CB 2854 C CG A LEU A 364 ? 0.5942 0.4580 0.3205 0.1707 -0.0178 0.0340 405 LEU A CG 2855 C CG B LEU A 364 ? 0.5964 0.4555 0.3111 0.1755 -0.0191 0.0342 405 LEU A CG 2856 C CD1 A LEU A 364 ? 0.5927 0.4682 0.3332 0.1645 -0.0255 0.0248 405 LEU A CD1 2857 C CD1 B LEU A 364 ? 0.5667 0.4290 0.2961 0.1728 -0.0239 0.0334 405 LEU A CD1 2858 C CD2 A LEU A 364 ? 0.6434 0.4949 0.3458 0.1836 -0.0264 0.0340 405 LEU A CD2 2859 C CD2 B LEU A 364 ? 0.6022 0.4706 0.3253 0.1719 -0.0280 0.0248 405 LEU A CD2 2860 N N . LYS A 365 ? 0.5750 0.4307 0.2993 0.1624 0.0299 0.0597 406 LYS A N 2861 C CA . LYS A 365 ? 0.5912 0.4464 0.3151 0.1604 0.0433 0.0655 406 LYS A CA 2862 C C . LYS A 365 ? 0.6319 0.4739 0.3406 0.1671 0.0543 0.0762 406 LYS A C 2863 O O . LYS A 365 ? 0.6444 0.4802 0.3381 0.1724 0.0630 0.0810 406 LYS A O 2864 C CB . LYS A 365 ? 0.5767 0.4441 0.3283 0.1476 0.0488 0.0647 406 LYS A CB 2865 C CG . LYS A 365 ? 0.6078 0.4754 0.3610 0.1456 0.0622 0.0703 406 LYS A CG 2866 C CD . LYS A 365 ? 0.6905 0.5698 0.4702 0.1337 0.0664 0.0690 406 LYS A CD 2867 C CE . LYS A 365 ? 0.7014 0.5799 0.4839 0.1323 0.0803 0.0756 406 LYS A CE 2868 N NZ . LYS A 365 ? 0.7493 0.6192 0.5308 0.1340 0.0908 0.0851 406 LYS A NZ 2869 N N . LYS A 366 ? 0.6283 0.4655 0.3400 0.1675 0.0543 0.0801 407 LYS A N 2870 C CA . LYS A 366 ? 0.6674 0.4909 0.3645 0.1740 0.0650 0.0911 407 LYS A CA 2871 C C . LYS A 366 ? 0.7103 0.5202 0.3749 0.1879 0.0627 0.0936 407 LYS A C 2872 O O . LYS A 366 ? 0.7438 0.5423 0.3923 0.1942 0.0740 0.1030 407 LYS A O 2873 C CB . LYS A 366 ? 0.6686 0.4894 0.3770 0.1712 0.0654 0.0948 407 LYS A CB 2874 C CG . LYS A 366 ? 0.6908 0.5219 0.4283 0.1585 0.0722 0.0950 407 LYS A CG 2875 C CD . LYS A 366 ? 0.7256 0.5541 0.4750 0.1557 0.0720 0.0977 407 LYS A CD 2876 C CE . LYS A 366 ? 0.6901 0.5282 0.4673 0.1435 0.0783 0.0973 407 LYS A CE 2877 N NZ . LYS A 366 ? 0.7610 0.5958 0.5492 0.1412 0.0779 0.0994 407 LYS A NZ 2878 N N . GLU A 367 ? 0.7107 0.5216 0.3656 0.1927 0.0484 0.0851 408 GLU A N 2879 C CA . GLU A 367 ? 0.7528 0.5512 0.3760 0.2063 0.0437 0.0855 408 GLU A CA 2880 C C . GLU A 367 ? 0.7533 0.5521 0.3643 0.2093 0.0466 0.0831 408 GLU A C 2881 O O . GLU A 367 ? 0.7829 0.5714 0.3667 0.2208 0.0424 0.0823 408 GLU A O 2882 C CB . GLU A 367 ? 0.7638 0.5621 0.3828 0.2108 0.0257 0.0773 408 GLU A CB 2883 C CG . GLU A 367 ? 0.8387 0.6334 0.4638 0.2110 0.0225 0.0803 408 GLU A CG 2884 C CD . GLU A 367 ? 0.9209 0.7163 0.5437 0.2157 0.0044 0.0719 408 GLU A CD 2885 O OE1 . GLU A 367 ? 0.9778 0.7620 0.5859 0.2244 0.0002 0.0755 408 GLU A OE1 2886 O OE2 . GLU A 367 ? 0.9534 0.7603 0.5896 0.2107 -0.0056 0.0619 408 GLU A OE2 2887 N N . GLY A 368 ? 0.7145 0.5248 0.3453 0.1995 0.0534 0.0816 409 GLY A N 2888 C CA . GLY A 368 ? 0.7154 0.5272 0.3386 0.2012 0.0579 0.0798 409 GLY A CA 2889 C C . GLY A 368 ? 0.6935 0.5165 0.3269 0.1967 0.0465 0.0684 409 GLY A C 2890 O O . GLY A 368 ? 0.7034 0.5270 0.3291 0.1990 0.0485 0.0658 409 GLY A O 2891 N N . TRP A 369 ? 0.6579 0.4894 0.3088 0.1904 0.0349 0.0616 410 TRP A N 2892 C CA . TRP A 369 ? 0.6349 0.4766 0.2963 0.1860 0.0240 0.0512 410 TRP A CA 2893 C C . TRP A 369 ? 0.6001 0.4551 0.2879 0.1734 0.0307 0.0505 410 TRP A C 2894 O O . TRP A 369 ? 0.6047 0.4632 0.3081 0.1666 0.0388 0.0558 410 TRP A O 2895 C CB . TRP A 369 ? 0.6369 0.4819 0.3059 0.1852 0.0091 0.0444 410 TRP A CB 2896 C CG . TRP A 369 ? 0.6228 0.4794 0.3078 0.1789 -0.0020 0.0340 410 TRP A CG 2897 C CD1 . TRP A 369 ? 0.6280 0.4836 0.3033 0.1839 -0.0130 0.0263 410 TRP A CD1 2898 C CD2 . TRP A 369 ? 0.5822 0.4527 0.2956 0.1666 -0.0029 0.0306 410 TRP A CD2 2899 N NE1 . TRP A 369 ? 0.5999 0.4680 0.2973 0.1750 -0.0205 0.0185 410 TRP A NE1 2900 C CE2 . TRP A 369 ? 0.5638 0.4409 0.2836 0.1647 -0.0142 0.0212 410 TRP A CE2 2901 C CE3 . TRP A 369 ? 0.5637 0.4410 0.2973 0.1573 0.0045 0.0343 410 TRP A CE3 2902 C CZ2 . TRP A 369 ? 0.5124 0.4027 0.2575 0.1539 -0.0174 0.0163 410 TRP A CZ2 2903 C CZ3 . TRP A 369 ? 0.5426 0.4327 0.2998 0.1471 0.0007 0.0289 410 TRP A CZ3 2904 C CH2 . TRP A 369 ? 0.5149 0.4112 0.2772 0.1455 -0.0097 0.0203 410 TRP A CH2 2905 N N . ARG A 370 ? 0.5738 0.4356 0.2662 0.1707 0.0267 0.0440 411 ARG A N 2906 C CA . ARG A 370 ? 0.5366 0.4122 0.2555 0.1585 0.0284 0.0410 411 ARG A CA 2907 C C . ARG A 370 ? 0.5152 0.3974 0.2397 0.1564 0.0153 0.0309 411 ARG A C 2908 O O . ARG A 370 ? 0.5204 0.3972 0.2285 0.1640 0.0082 0.0266 411 ARG A O 2909 C CB . ARG A 370 ? 0.5578 0.4354 0.2787 0.1564 0.0404 0.0447 411 ARG A CB 2910 C CG . ARG A 370 ? 0.5820 0.4565 0.3058 0.1552 0.0551 0.0545 411 ARG A CG 2911 C CD . ARG A 370 ? 0.5700 0.4491 0.3009 0.1519 0.0661 0.0571 411 ARG A CD 2912 N NE . ARG A 370 ? 0.5745 0.4516 0.3127 0.1494 0.0791 0.0661 411 ARG A NE 2913 C CZ . ARG A 370 ? 0.5431 0.4275 0.3044 0.1397 0.0812 0.0674 411 ARG A CZ 2914 N NH1 . ARG A 370 ? 0.4888 0.3838 0.2681 0.1313 0.0723 0.0603 411 ARG A NH1 2915 N NH2 . ARG A 370 ? 0.5577 0.4386 0.3242 0.1385 0.0928 0.0758 411 ARG A NH2 2916 N N . PRO A 371 ? 0.4673 0.3613 0.2156 0.1460 0.0124 0.0271 412 PRO A N 2917 C CA . PRO A 371 ? 0.4554 0.3562 0.2114 0.1430 0.0015 0.0183 412 PRO A CA 2918 C C . PRO A 371 ? 0.4516 0.3535 0.2038 0.1434 0.0047 0.0166 412 PRO A C 2919 O O . PRO A 371 ? 0.4704 0.3714 0.2213 0.1429 0.0160 0.0221 412 PRO A O 2920 C CB . PRO A 371 ? 0.4382 0.3509 0.2204 0.1313 0.0013 0.0167 412 PRO A CB 2921 C CG . PRO A 371 ? 0.4407 0.3538 0.2289 0.1274 0.0142 0.0243 412 PRO A CG 2922 C CD . PRO A 371 ? 0.4505 0.3514 0.2186 0.1367 0.0199 0.0311 412 PRO A CD 2923 N N . ARG A 372 ? 0.4345 0.3383 0.1863 0.1441 -0.0054 0.0089 413 ARG A N 2924 C CA . ARG A 372 ? 0.4389 0.3435 0.1878 0.1446 -0.0036 0.0065 413 ARG A CA 2925 C C . ARG A 372 ? 0.4319 0.3468 0.2013 0.1342 0.0041 0.0084 413 ARG A C 2926 O O . ARG A 372 ? 0.4230 0.3373 0.1901 0.1347 0.0134 0.0120 413 ARG A O 2927 C CB . ARG A 372 ? 0.4506 0.3564 0.1998 0.1457 -0.0170 -0.0027 413 ARG A CB 2928 C CG . ARG A 372 ? 0.4850 0.3914 0.2321 0.1460 -0.0161 -0.0059 413 ARG A CG 2929 C CD . ARG A 372 ? 0.5117 0.4195 0.2621 0.1461 -0.0295 -0.0149 413 ARG A CD 2930 N NE . ARG A 372 ? 0.4901 0.3989 0.2411 0.1454 -0.0289 -0.0182 413 ARG A NE 2931 C CZ . ARG A 372 ? 0.5488 0.4492 0.2809 0.1543 -0.0292 -0.0201 413 ARG A CZ 2932 N NH1 . ARG A 372 ? 0.5577 0.4474 0.2668 0.1648 -0.0295 -0.0187 413 ARG A NH1 2933 N NH2 . ARG A 372 ? 0.5310 0.4333 0.2666 0.1528 -0.0288 -0.0233 413 ARG A NH2 2934 N N . ARG A 373 ? 0.4008 0.3247 0.1899 0.1255 0.0000 0.0059 414 ARG A N 2935 C CA . ARG A 373 ? 0.3777 0.3113 0.1866 0.1154 0.0056 0.0072 414 ARG A CA 2936 C C . ARG A 373 ? 0.3887 0.3242 0.2065 0.1111 0.0128 0.0130 414 ARG A C 2937 O O . ARG A 373 ? 0.3951 0.3265 0.2081 0.1141 0.0113 0.0147 414 ARG A O 2938 C CB . ARG A 373 ? 0.3696 0.3114 0.1938 0.1085 -0.0033 0.0007 414 ARG A CB 2939 C CG . ARG A 373 ? 0.3671 0.3065 0.1842 0.1125 -0.0121 -0.0058 414 ARG A CG 2940 C CD . ARG A 373 ? 0.3717 0.3191 0.2054 0.1053 -0.0201 -0.0117 414 ARG A CD 2941 N NE . ARG A 373 ? 0.3705 0.3138 0.1958 0.1101 -0.0275 -0.0172 414 ARG A NE 2942 C CZ . ARG A 373 ? 0.3837 0.3212 0.1988 0.1168 -0.0367 -0.0216 414 ARG A CZ 2943 N NH1 . ARG A 373 ? 0.3820 0.3181 0.1958 0.1188 -0.0406 -0.0215 414 ARG A NH1 2944 N NH2 . ARG A 373 ? 0.4124 0.3453 0.2189 0.1216 -0.0426 -0.0267 414 ARG A NH2 2945 N N . THR A 374 ? 0.3638 0.3058 0.1956 0.1040 0.0199 0.0155 415 THR A N 2946 C CA . THR A 374 ? 0.3511 0.2958 0.1945 0.0988 0.0260 0.0200 415 THR A CA 2947 C C . THR A 374 ? 0.3429 0.2929 0.1980 0.0934 0.0190 0.0163 415 THR A C 2948 O O . THR A 374 ? 0.3356 0.2917 0.1991 0.0891 0.0124 0.0110 415 THR A O 2949 C CB . THR A 374 ? 0.3459 0.2966 0.2023 0.0926 0.0338 0.0223 415 THR A CB 2950 O OG1 . THR A 374 ? 0.3616 0.3071 0.2082 0.0980 0.0424 0.0271 415 THR A OG1 2951 C CG2 . THR A 374 ? 0.3513 0.3062 0.2231 0.0856 0.0380 0.0252 415 THR A CG2 2952 N N . ILE A 375 ? 0.3352 0.2824 0.1911 0.0938 0.0210 0.0195 416 ILE A N 2953 C CA . ILE A 375 ? 0.3215 0.2739 0.1901 0.0885 0.0163 0.0168 416 ILE A CA 2954 C C . ILE A 375 ? 0.3162 0.2723 0.1983 0.0818 0.0234 0.0201 416 ILE A C 2955 O O . ILE A 375 ? 0.3406 0.2920 0.2200 0.0835 0.0313 0.0259 416 ILE A O 2956 C CB . ILE A 375 ? 0.3337 0.2803 0.1942 0.0941 0.0112 0.0166 416 ILE A CB 2957 C CG1 . ILE A 375 ? 0.3600 0.3025 0.2069 0.1013 0.0030 0.0127 416 ILE A CG1 2958 C CG2 . ILE A 375 ? 0.3302 0.2834 0.2055 0.0883 0.0066 0.0131 416 ILE A CG2 2959 C CD1 . ILE A 375 ? 0.3831 0.3183 0.2194 0.1085 -0.0020 0.0132 416 ILE A CD1 2960 N N . LEU A 376 ? 0.3046 0.2691 0.2014 0.0742 0.0209 0.0164 417 LEU A N 2961 C CA . LEU A 376 ? 0.2984 0.2664 0.2084 0.0679 0.0259 0.0183 417 LEU A CA 2962 C C . LEU A 376 ? 0.3044 0.2741 0.2207 0.0658 0.0216 0.0158 417 LEU A C 2963 O O . LEU A 376 ? 0.3166 0.2896 0.2340 0.0655 0.0147 0.0111 417 LEU A O 2964 C CB . LEU A 376 ? 0.2842 0.2599 0.2050 0.0612 0.0261 0.0158 417 LEU A CB 2965 C CG . LEU A 376 ? 0.3009 0.2762 0.2177 0.0629 0.0300 0.0177 417 LEU A CG 2966 C CD1 . LEU A 376 ? 0.3179 0.3008 0.2466 0.0562 0.0295 0.0152 417 LEU A CD1 2967 C CD2 . LEU A 376 ? 0.3425 0.3124 0.2561 0.0659 0.0390 0.0240 417 LEU A CD2 2968 N N . PHE A 377 ? 0.2916 0.2588 0.2125 0.0646 0.0261 0.0189 418 PHE A N 2969 C CA . PHE A 377 ? 0.2853 0.2537 0.2126 0.0630 0.0229 0.0167 418 PHE A CA 2970 C C . PHE A 377 ? 0.2853 0.2584 0.2265 0.0557 0.0261 0.0160 418 PHE A C 2971 O O . PHE A 377 ? 0.2978 0.2694 0.2425 0.0539 0.0323 0.0197 418 PHE A O 2972 C CB . PHE A 377 ? 0.3088 0.2688 0.2290 0.0686 0.0249 0.0209 418 PHE A CB 2973 C CG . PHE A 377 ? 0.3301 0.2843 0.2351 0.0766 0.0212 0.0216 418 PHE A CG 2974 C CD1 . PHE A 377 ? 0.3539 0.3093 0.2572 0.0792 0.0128 0.0171 418 PHE A CD1 2975 C CD2 . PHE A 377 ? 0.3707 0.3181 0.2632 0.0818 0.0262 0.0265 418 PHE A CD2 2976 C CE1 . PHE A 377 ? 0.3579 0.3074 0.2467 0.0872 0.0081 0.0171 418 PHE A CE1 2977 C CE2 . PHE A 377 ? 0.3781 0.3190 0.2541 0.0902 0.0220 0.0267 418 PHE A CE2 2978 C CZ . PHE A 377 ? 0.3746 0.3165 0.2487 0.0929 0.0124 0.0217 418 PHE A CZ 2979 N N . ALA A 378 ? 0.2765 0.2552 0.2258 0.0516 0.0220 0.0113 419 ALA A N 2980 C CA . ALA A 378 ? 0.2605 0.2434 0.2214 0.0451 0.0243 0.0099 419 ALA A CA 2981 C C . ALA A 378 ? 0.2655 0.2488 0.2323 0.0439 0.0227 0.0074 419 ALA A C 2982 O O . ALA A 378 ? 0.2713 0.2563 0.2371 0.0455 0.0182 0.0045 419 ALA A O 2983 C CB . ALA A 378 ? 0.2602 0.2501 0.2250 0.0406 0.0221 0.0065 419 ALA A CB 2984 N N . SER A 379 ? 0.2500 0.2316 0.2240 0.0409 0.0264 0.0085 420 SER A N 2985 C CA . SER A 379 ? 0.2516 0.2337 0.2327 0.0389 0.0255 0.0056 420 SER A CA 2986 C C . SER A 379 ? 0.2482 0.2357 0.2372 0.0326 0.0256 0.0022 420 SER A C 2987 O O . SER A 379 ? 0.2606 0.2469 0.2551 0.0298 0.0287 0.0037 420 SER A O 2988 C CB . SER A 379 ? 0.2752 0.2500 0.2581 0.0406 0.0295 0.0094 420 SER A CB 2989 O OG . SER A 379 ? 0.2767 0.2516 0.2671 0.0384 0.0286 0.0061 420 SER A OG 2990 N N . TRP A 380 ? 0.2452 0.2384 0.2350 0.0306 0.0220 -0.0021 421 TRP A N 2991 C CA . TRP A 380 ? 0.2372 0.2351 0.2318 0.0254 0.0216 -0.0051 421 TRP A CA 2992 C C . TRP A 380 ? 0.2579 0.2552 0.2588 0.0229 0.0220 -0.0082 421 TRP A C 2993 O O . TRP A 380 ? 0.2652 0.2610 0.2668 0.0248 0.0214 -0.0097 421 TRP A O 2994 C CB . TRP A 380 ? 0.2408 0.2445 0.2334 0.0244 0.0183 -0.0083 421 TRP A CB 2995 C CG . TRP A 380 ? 0.2347 0.2395 0.2213 0.0266 0.0166 -0.0067 421 TRP A CG 2996 C CD1 . TRP A 380 ? 0.2275 0.2343 0.2116 0.0287 0.0134 -0.0082 421 TRP A CD1 2997 C CD2 . TRP A 380 ? 0.2193 0.2235 0.2031 0.0268 0.0177 -0.0039 421 TRP A CD2 2998 N NE1 . TRP A 380 ? 0.2175 0.2243 0.1965 0.0304 0.0120 -0.0067 421 TRP A NE1 2999 C CE2 . TRP A 380 ? 0.2141 0.2193 0.1923 0.0294 0.0149 -0.0041 421 TRP A CE2 3000 C CE3 . TRP A 380 ? 0.2258 0.2288 0.2121 0.0252 0.0208 -0.0016 421 TRP A CE3 3001 C CZ2 . TRP A 380 ? 0.2512 0.2558 0.2248 0.0308 0.0153 -0.0019 421 TRP A CZ2 3002 C CZ3 . TRP A 380 ? 0.2383 0.2413 0.2211 0.0264 0.0217 0.0008 421 TRP A CZ3 3003 C CH2 . TRP A 380 ? 0.2461 0.2497 0.2218 0.0294 0.0189 0.0005 421 TRP A CH2 3004 N N . ASP A 381 ? 0.2476 0.2462 0.2532 0.0189 0.0223 -0.0097 422 ASP A N 3005 C CA . ASP A 381 ? 0.2288 0.2266 0.2394 0.0166 0.0218 -0.0136 422 ASP A CA 3006 C C . ASP A 381 ? 0.2438 0.2466 0.2526 0.0141 0.0193 -0.0180 422 ASP A C 3007 O O . ASP A 381 ? 0.2425 0.2492 0.2476 0.0133 0.0181 -0.0176 422 ASP A O 3008 C CB . ASP A 381 ? 0.2454 0.2403 0.2634 0.0140 0.0234 -0.0126 422 ASP A CB 3009 C CG . ASP A 381 ? 0.2444 0.2355 0.2684 0.0130 0.0233 -0.0158 422 ASP A CG 3010 O OD1 . ASP A 381 ? 0.2572 0.2483 0.2795 0.0139 0.0221 -0.0195 422 ASP A OD1 3011 O OD2 . ASP A 381 ? 0.2641 0.2519 0.2958 0.0112 0.0248 -0.0146 422 ASP A OD2 3012 N N . ALA A 382 ? 0.2281 0.2302 0.2389 0.0132 0.0187 -0.0222 423 ALA A N 3013 C CA . ALA A 382 ? 0.2457 0.2512 0.2537 0.0111 0.0170 -0.0264 423 ALA A CA 3014 C C . ALA A 382 ? 0.2290 0.2393 0.2318 0.0117 0.0165 -0.0264 423 ALA A C 3015 O O . ALA A 382 ? 0.2392 0.2523 0.2386 0.0097 0.0154 -0.0280 423 ALA A O 3016 C CB . ALA A 382 ? 0.2334 0.2390 0.2432 0.0078 0.0152 -0.0276 423 ALA A CB 3017 N N . ALA A 383 ? 0.2318 0.2427 0.2342 0.0145 0.0171 -0.0247 424 ALA A N 3018 C CA . ALA A 383 ? 0.2297 0.2452 0.2293 0.0147 0.0166 -0.0251 424 ALA A CA 3019 C C . ALA A 383 ? 0.2341 0.2517 0.2335 0.0140 0.0175 -0.0291 424 ALA A C 3020 O O . ALA A 383 ? 0.2363 0.2576 0.2330 0.0127 0.0177 -0.0297 424 ALA A O 3021 C CB . ALA A 383 ? 0.2387 0.2545 0.2391 0.0182 0.0161 -0.0231 424 ALA A CB 3022 N N . GLU A 384 ? 0.2338 0.2485 0.2357 0.0151 0.0186 -0.0316 425 GLU A N 3023 C CA . GLU A 384 ? 0.2444 0.2608 0.2454 0.0152 0.0201 -0.0356 425 GLU A CA 3024 C C . GLU A 384 ? 0.2435 0.2600 0.2393 0.0126 0.0199 -0.0379 425 GLU A C 3025 O O . GLU A 384 ? 0.2554 0.2736 0.2480 0.0127 0.0216 -0.0405 425 GLU A O 3026 C CB . GLU A 384 ? 0.2440 0.2569 0.2488 0.0174 0.0212 -0.0382 425 GLU A CB 3027 C CG . GLU A 384 ? 0.2454 0.2580 0.2550 0.0208 0.0213 -0.0364 425 GLU A CG 3028 C CD . GLU A 384 ? 0.2434 0.2617 0.2550 0.0223 0.0221 -0.0368 425 GLU A CD 3029 O OE1 . GLU A 384 ? 0.2730 0.2954 0.2823 0.0204 0.0231 -0.0375 425 GLU A OE1 3030 O OE2 . GLU A 384 ? 0.2465 0.2649 0.2625 0.0255 0.0215 -0.0362 425 GLU A OE2 3031 N N . PHE A 385 ? 0.2463 0.2609 0.2410 0.0106 0.0177 -0.0367 426 PHE A N 3032 C CA . PHE A 385 ? 0.2446 0.2589 0.2340 0.0085 0.0162 -0.0390 426 PHE A CA 3033 C C . PHE A 385 ? 0.2411 0.2585 0.2267 0.0069 0.0152 -0.0362 426 PHE A C 3034 O O . PHE A 385 ? 0.2627 0.2793 0.2444 0.0053 0.0130 -0.0371 426 PHE A O 3035 C CB . PHE A 385 ? 0.2441 0.2542 0.2369 0.0074 0.0138 -0.0403 426 PHE A CB 3036 C CG . PHE A 385 ? 0.2653 0.2713 0.2611 0.0086 0.0142 -0.0441 426 PHE A CG 3037 C CD1 . PHE A 385 ? 0.2586 0.2625 0.2499 0.0084 0.0130 -0.0492 426 PHE A CD1 3038 C CD2 . PHE A 385 ? 0.2629 0.2665 0.2652 0.0103 0.0157 -0.0426 426 PHE A CD2 3039 C CE1 . PHE A 385 ? 0.2678 0.2672 0.2615 0.0098 0.0131 -0.0537 426 PHE A CE1 3040 C CE2 . PHE A 385 ? 0.2659 0.2651 0.2715 0.0116 0.0161 -0.0463 426 PHE A CE2 3041 C CZ . PHE A 385 ? 0.2812 0.2783 0.2827 0.0113 0.0147 -0.0522 426 PHE A CZ 3042 N N . GLY A 386 ? 0.2383 0.2589 0.2252 0.0076 0.0163 -0.0331 427 GLY A N 3043 C CA . GLY A 386 ? 0.2430 0.2662 0.2265 0.0062 0.0154 -0.0307 427 GLY A CA 3044 C C . GLY A 386 ? 0.2176 0.2413 0.2039 0.0064 0.0140 -0.0270 427 GLY A C 3045 O O . GLY A 386 ? 0.2301 0.2546 0.2142 0.0051 0.0124 -0.0253 427 GLY A O 3046 N N . LEU A 387 ? 0.2130 0.2360 0.2034 0.0085 0.0145 -0.0259 428 LEU A N 3047 C CA . LEU A 387 ? 0.2188 0.2415 0.2101 0.0096 0.0135 -0.0225 428 LEU A CA 3048 C C . LEU A 387 ? 0.2237 0.2445 0.2154 0.0084 0.0126 -0.0210 428 LEU A C 3049 O O . LEU A 387 ? 0.2195 0.2409 0.2102 0.0084 0.0118 -0.0186 428 LEU A O 3050 C CB . LEU A 387 ? 0.2286 0.2545 0.2181 0.0094 0.0125 -0.0211 428 LEU A CB 3051 C CG . LEU A 387 ? 0.2266 0.2554 0.2179 0.0098 0.0136 -0.0227 428 LEU A CG 3052 C CD1 . LEU A 387 ? 0.2318 0.2632 0.2227 0.0090 0.0125 -0.0213 428 LEU A CD1 3053 C CD2 . LEU A 387 ? 0.2385 0.2669 0.2339 0.0128 0.0140 -0.0233 428 LEU A CD2 3054 N N . LEU A 388 ? 0.2165 0.2350 0.2106 0.0074 0.0128 -0.0228 429 LEU A N 3055 C CA . LEU A 388 ? 0.2105 0.2281 0.2068 0.0056 0.0116 -0.0222 429 LEU A CA 3056 C C . LEU A 388 ? 0.2114 0.2275 0.2113 0.0068 0.0129 -0.0184 429 LEU A C 3057 O O . LEU A 388 ? 0.2249 0.2422 0.2256 0.0061 0.0122 -0.0166 429 LEU A O 3058 C CB . LEU A 388 ? 0.2165 0.2318 0.2155 0.0042 0.0107 -0.0258 429 LEU A CB 3059 C CG . LEU A 388 ? 0.2306 0.2465 0.2240 0.0036 0.0098 -0.0297 429 LEU A CG 3060 C CD1 . LEU A 388 ? 0.2524 0.2652 0.2481 0.0026 0.0080 -0.0337 429 LEU A CD1 3061 C CD2 . LEU A 388 ? 0.2682 0.2868 0.2555 0.0025 0.0082 -0.0294 429 LEU A CD2 3062 N N . GLY A 389 ? 0.2279 0.2413 0.2295 0.0091 0.0150 -0.0170 430 GLY A N 3063 C CA . GLY A 389 ? 0.2186 0.2296 0.2222 0.0109 0.0172 -0.0129 430 GLY A CA 3064 C C . GLY A 389 ? 0.2240 0.2365 0.2227 0.0128 0.0170 -0.0102 430 GLY A C 3065 O O . GLY A 389 ? 0.2247 0.2369 0.2246 0.0130 0.0183 -0.0074 430 GLY A O 3066 N N . SER A 390 ? 0.2116 0.2256 0.2057 0.0143 0.0156 -0.0110 431 SER A N 3067 C CA . SER A 390 ? 0.2095 0.2244 0.1991 0.0163 0.0146 -0.0092 431 SER A CA 3068 C C . SER A 390 ? 0.2131 0.2308 0.2026 0.0138 0.0132 -0.0094 431 SER A C 3069 O O . SER A 390 ? 0.2137 0.2313 0.2016 0.0150 0.0134 -0.0073 431 SER A O 3070 C CB . SER A 390 ? 0.2111 0.2272 0.1981 0.0181 0.0126 -0.0106 431 SER A CB 3071 O OG . SER A 390 ? 0.2281 0.2477 0.2164 0.0153 0.0115 -0.0136 431 SER A OG 3072 N N . THR A 391 ? 0.2118 0.2318 0.2023 0.0108 0.0118 -0.0121 432 THR A N 3073 C CA . THR A 391 ? 0.2037 0.2260 0.1932 0.0088 0.0099 -0.0123 432 THR A CA 3074 C C . THR A 391 ? 0.2026 0.2246 0.1960 0.0079 0.0103 -0.0110 432 THR A C 3075 O O . THR A 391 ? 0.2031 0.2260 0.1958 0.0082 0.0096 -0.0094 432 THR A O 3076 C CB . THR A 391 ? 0.2019 0.2259 0.1897 0.0063 0.0085 -0.0150 432 THR A CB 3077 O OG1 . THR A 391 ? 0.2162 0.2412 0.2021 0.0071 0.0089 -0.0159 432 THR A OG1 3078 C CG2 . THR A 391 ? 0.2349 0.2605 0.2205 0.0048 0.0063 -0.0145 432 THR A CG2 3079 N N . GLU A 392 ? 0.2086 0.2290 0.2072 0.0069 0.0115 -0.0116 433 GLU A N 3080 C CA . GLU A 392 ? 0.1989 0.2196 0.2040 0.0058 0.0119 -0.0105 433 GLU A CA 3081 C C . GLU A 392 ? 0.1993 0.2190 0.2050 0.0084 0.0151 -0.0065 433 GLU A C 3082 O O . GLU A 392 ? 0.2067 0.2278 0.2153 0.0083 0.0153 -0.0051 433 GLU A O 3083 C CB . GLU A 392 ? 0.2104 0.2293 0.2226 0.0041 0.0124 -0.0121 433 GLU A CB 3084 C CG . GLU A 392 ? 0.2236 0.2430 0.2342 0.0019 0.0088 -0.0166 433 GLU A CG 3085 C CD . GLU A 392 ? 0.2426 0.2645 0.2511 0.0005 0.0051 -0.0177 433 GLU A CD 3086 O OE1 . GLU A 392 ? 0.2262 0.2494 0.2408 -0.0003 0.0042 -0.0168 433 GLU A OE1 3087 O OE2 . GLU A 392 ? 0.2307 0.2534 0.2318 0.0003 0.0034 -0.0193 433 GLU A OE2 3088 N N . TRP A 393 ? 0.2081 0.2249 0.2106 0.0113 0.0176 -0.0047 434 TRP A N 3089 C CA . TRP A 393 ? 0.2184 0.2333 0.2190 0.0146 0.0210 -0.0008 434 TRP A CA 3090 C C . TRP A 393 ? 0.2280 0.2444 0.2226 0.0162 0.0192 -0.0006 434 TRP A C 3091 O O . TRP A 393 ? 0.2302 0.2466 0.2254 0.0178 0.0213 0.0017 434 TRP A O 3092 C CB . TRP A 393 ? 0.2237 0.2344 0.2202 0.0178 0.0231 0.0007 434 TRP A CB 3093 C CG . TRP A 393 ? 0.2168 0.2241 0.2094 0.0221 0.0271 0.0051 434 TRP A CG 3094 C CD1 . TRP A 393 ? 0.2478 0.2522 0.2449 0.0229 0.0324 0.0088 434 TRP A CD1 3095 C CD2 . TRP A 393 ? 0.2397 0.2454 0.2226 0.0264 0.0263 0.0060 434 TRP A CD2 3096 N NE1 . TRP A 393 ? 0.2656 0.2666 0.2549 0.0278 0.0355 0.0124 434 TRP A NE1 3097 C CE2 . TRP A 393 ? 0.2445 0.2461 0.2246 0.0302 0.0314 0.0104 434 TRP A CE2 3098 C CE3 . TRP A 393 ? 0.2399 0.2470 0.2166 0.0275 0.0218 0.0035 434 TRP A CE3 3099 C CZ2 . TRP A 393 ? 0.2748 0.2732 0.2442 0.0355 0.0317 0.0120 434 TRP A CZ2 3100 C CZ3 . TRP A 393 ? 0.2550 0.2591 0.2227 0.0325 0.0214 0.0047 434 TRP A CZ3 3101 C CH2 . TRP A 393 ? 0.2655 0.2651 0.2288 0.0367 0.0262 0.0089 434 TRP A CH2 3102 N N . ALA A 394 ? 0.2146 0.2324 0.2045 0.0159 0.0157 -0.0029 435 ALA A N 3103 C CA . ALA A 394 ? 0.2145 0.2334 0.1999 0.0171 0.0135 -0.0030 435 ALA A CA 3104 C C . ALA A 394 ? 0.2214 0.2429 0.2105 0.0147 0.0123 -0.0032 435 ALA A C 3105 O O . ALA A 394 ? 0.2143 0.2360 0.2018 0.0164 0.0122 -0.0021 435 ALA A O 3106 C CB . ALA A 394 ? 0.2237 0.2436 0.2053 0.0167 0.0102 -0.0053 435 ALA A CB 3107 N N . GLU A 395 ? 0.2136 0.2369 0.2073 0.0112 0.0110 -0.0049 436 GLU A N 3108 C CA . GLU A 395 ? 0.2071 0.2327 0.2048 0.0094 0.0092 -0.0052 436 GLU A CA 3109 C C . GLU A 395 ? 0.2133 0.2391 0.2173 0.0107 0.0123 -0.0027 436 GLU A C 3110 O O . GLU A 395 ? 0.2278 0.2552 0.2336 0.0112 0.0116 -0.0020 436 GLU A O 3111 C CB . GLU A 395 ? 0.2144 0.2412 0.2152 0.0061 0.0066 -0.0078 436 GLU A CB 3112 C CG . GLU A 395 ? 0.2091 0.2360 0.2028 0.0050 0.0040 -0.0098 436 GLU A CG 3113 C CD . GLU A 395 ? 0.2452 0.2725 0.2389 0.0025 0.0014 -0.0124 436 GLU A CD 3114 O OE1 . GLU A 395 ? 0.2278 0.2554 0.2162 0.0017 -0.0007 -0.0131 436 GLU A OE1 3115 O OE2 . GLU A 395 ? 0.2497 0.2765 0.2485 0.0015 0.0016 -0.0138 436 GLU A OE2 3116 N N . GLU A 396 ? 0.2223 0.2464 0.2303 0.0112 0.0161 -0.0013 437 GLU A N 3117 C CA . GLU A 396 ? 0.2222 0.2464 0.2375 0.0123 0.0203 0.0015 437 GLU A CA 3118 C C . GLU A 396 ? 0.2311 0.2540 0.2402 0.0165 0.0230 0.0041 437 GLU A C 3119 O O . GLU A 396 ? 0.2277 0.2522 0.2410 0.0175 0.0248 0.0056 437 GLU A O 3120 C CB . GLU A 396 ? 0.2514 0.2728 0.2709 0.0123 0.0244 0.0031 437 GLU A CB 3121 C CG . GLU A 396 ? 0.2799 0.3016 0.3098 0.0126 0.0296 0.0064 437 GLU A CG 3122 C CD . GLU A 396 ? 0.3917 0.4118 0.4306 0.0101 0.0312 0.0063 437 GLU A CD 3123 O OE1 . GLU A 396 ? 0.5218 0.5442 0.5722 0.0067 0.0293 0.0044 437 GLU A OE1 3124 O OE2 . GLU A 396 ? 0.3762 0.3923 0.4102 0.0117 0.0334 0.0075 437 GLU A OE2 3125 N N . ASN A 397 ? 0.2059 0.2259 0.2051 0.0191 0.0227 0.0042 438 ASN A N 3126 C CA . ASN A 397 ? 0.2165 0.2337 0.2079 0.0241 0.0251 0.0063 438 ASN A CA 3127 C C . ASN A 397 ? 0.2250 0.2425 0.2092 0.0253 0.0207 0.0043 438 ASN A C 3128 O O . ASN A 397 ? 0.2326 0.2472 0.2088 0.0295 0.0211 0.0049 438 ASN A O 3129 C CB . ASN A 397 ? 0.2249 0.2375 0.2104 0.0272 0.0280 0.0082 438 ASN A CB 3130 C CG . ASN A 397 ? 0.2577 0.2690 0.2506 0.0266 0.0335 0.0112 438 ASN A CG 3131 O OD1 . ASN A 397 ? 0.3056 0.3166 0.3018 0.0282 0.0386 0.0143 438 ASN A OD1 3132 N ND2 . ASN A 397 ? 0.2542 0.2648 0.2509 0.0241 0.0330 0.0103 438 ASN A ND2 3133 N N . SER A 398 ? 0.2113 0.2320 0.1985 0.0217 0.0164 0.0019 439 SER A N 3134 C CA . SER A 398 ? 0.2197 0.2402 0.2012 0.0222 0.0121 0.0000 439 SER A CA 3135 C C . SER A 398 ? 0.2142 0.2332 0.1916 0.0261 0.0126 0.0008 439 SER A C 3136 O O . SER A 398 ? 0.2331 0.2500 0.2040 0.0283 0.0099 -0.0005 439 SER A O 3137 C CB . SER A 398 ? 0.2162 0.2398 0.2015 0.0180 0.0082 -0.0017 439 SER A CB 3138 O OG . SER A 398 ? 0.2433 0.2691 0.2348 0.0173 0.0087 -0.0010 439 SER A OG 3139 N N . ARG A 399 ? 0.2191 0.2391 0.2010 0.0272 0.0159 0.0026 440 ARG A N 3140 C CA . ARG A 399 ? 0.2210 0.2393 0.1986 0.0315 0.0168 0.0031 440 ARG A CA 3141 C C . ARG A 399 ? 0.2365 0.2500 0.2045 0.0368 0.0195 0.0042 440 ARG A C 3142 O O . ARG A 399 ? 0.2510 0.2615 0.2110 0.0406 0.0174 0.0028 440 ARG A O 3143 C CB . ARG A 399 ? 0.2220 0.2430 0.2078 0.0316 0.0203 0.0048 440 ARG A CB 3144 C CG . ARG A 399 ? 0.2484 0.2735 0.2423 0.0273 0.0160 0.0033 440 ARG A CG 3145 C CD . ARG A 399 ? 0.2930 0.3220 0.2994 0.0253 0.0186 0.0046 440 ARG A CD 3146 N NE . ARG A 399 ? 0.2575 0.2896 0.2694 0.0218 0.0132 0.0027 440 ARG A NE 3147 C CZ . ARG A 399 ? 0.2727 0.3058 0.2857 0.0179 0.0093 0.0011 440 ARG A CZ 3148 N NH1 . ARG A 399 ? 0.3038 0.3355 0.3144 0.0164 0.0103 0.0008 440 ARG A NH1 3149 N NH2 . ARG A 399 ? 0.2616 0.2965 0.2775 0.0159 0.0044 -0.0003 440 ARG A NH2 3150 N N . LEU A 400 ? 0.2340 0.2461 0.2022 0.0376 0.0240 0.0065 441 LEU A N 3151 C CA . LEU A 400 ? 0.2517 0.2584 0.2093 0.0431 0.0264 0.0078 441 LEU A CA 3152 C C . LEU A 400 ? 0.2595 0.2641 0.2098 0.0438 0.0203 0.0048 441 LEU A C 3153 O O . LEU A 400 ? 0.2667 0.2672 0.2071 0.0487 0.0185 0.0038 441 LEU A O 3154 C CB . LEU A 400 ? 0.2561 0.2613 0.2160 0.0433 0.0321 0.0113 441 LEU A CB 3155 C CG . LEU A 400 ? 0.2803 0.2882 0.2513 0.0415 0.0383 0.0143 441 LEU A CG 3156 C CD1 . LEU A 400 ? 0.3299 0.3348 0.3020 0.0421 0.0439 0.0179 441 LEU A CD1 3157 C CD2 . LEU A 400 ? 0.3059 0.3135 0.2754 0.0455 0.0424 0.0159 441 LEU A CD2 3158 N N . LEU A 401 ? 0.2451 0.2526 0.2007 0.0390 0.0169 0.0031 442 LEU A N 3159 C CA . LEU A 401 ? 0.2534 0.2597 0.2046 0.0393 0.0119 0.0005 442 LEU A CA 3160 C C . LEU A 401 ? 0.2622 0.2687 0.2113 0.0396 0.0067 -0.0024 442 LEU A C 3161 O O . LEU A 401 ? 0.2941 0.2977 0.2372 0.0427 0.0030 -0.0044 442 LEU A O 3162 C CB . LEU A 401 ? 0.2294 0.2392 0.1878 0.0341 0.0106 -0.0006 442 LEU A CB 3163 C CG . LEU A 401 ? 0.2690 0.2778 0.2297 0.0339 0.0148 0.0017 442 LEU A CG 3164 C CD1 . LEU A 401 ? 0.2619 0.2743 0.2302 0.0285 0.0137 0.0001 442 LEU A CD1 3165 C CD2 . LEU A 401 ? 0.2850 0.2894 0.2385 0.0383 0.0148 0.0022 442 LEU A CD2 3166 N N A GLN A 402 ? 0.2460 0.2554 0.2002 0.0366 0.0058 -0.0029 443 GLN A N 3167 N N B GLN A 402 ? 0.2632 0.2727 0.2178 0.0365 0.0061 -0.0027 443 GLN A N 3168 C CA A GLN A 402 ? 0.2399 0.2486 0.1926 0.0367 0.0007 -0.0055 443 GLN A CA 3169 C CA B GLN A 402 ? 0.2687 0.2781 0.2227 0.0363 0.0016 -0.0050 443 GLN A CA 3170 C C A GLN A 402 ? 0.2556 0.2601 0.2007 0.0424 0.0005 -0.0060 443 GLN A C 3171 C C B GLN A 402 ? 0.2745 0.2792 0.2199 0.0423 0.0007 -0.0059 443 GLN A C 3172 O O A GLN A 402 ? 0.2530 0.2553 0.1950 0.0439 -0.0044 -0.0088 443 GLN A O 3173 O O B GLN A 402 ? 0.2660 0.2683 0.2078 0.0438 -0.0042 -0.0087 443 GLN A O 3174 C CB A GLN A 402 ? 0.2050 0.2174 0.1647 0.0317 -0.0009 -0.0057 443 GLN A CB 3175 C CB B GLN A 402 ? 0.2729 0.2853 0.2331 0.0333 0.0023 -0.0041 443 GLN A CB 3176 C CG A GLN A 402 ? 0.2030 0.2165 0.1656 0.0319 0.0019 -0.0041 443 GLN A CG 3177 C CG B GLN A 402 ? 0.2612 0.2722 0.2200 0.0346 -0.0008 -0.0055 443 GLN A CG 3178 C CD A GLN A 402 ? 0.2422 0.2592 0.2114 0.0270 0.0002 -0.0040 443 GLN A CD 3179 C CD B GLN A 402 ? 0.3112 0.3227 0.2720 0.0312 -0.0057 -0.0074 443 GLN A CD 3180 O OE1 A GLN A 402 ? 0.2431 0.2613 0.2137 0.0235 -0.0020 -0.0049 443 GLN A OE1 3181 O OE1 B GLN A 402 ? 0.3254 0.3395 0.2901 0.0270 -0.0060 -0.0071 443 GLN A OE1 3182 N NE2 A GLN A 402 ? 0.2615 0.2801 0.2348 0.0269 0.0014 -0.0029 443 GLN A NE2 3183 N NE2 B GLN A 402 ? 0.2032 0.2118 0.1615 0.0331 -0.0094 -0.0093 443 GLN A NE2 3184 N N . GLU A 403 ? 0.2594 0.2624 0.2016 0.0460 0.0059 -0.0035 444 GLU A N 3185 C CA . GLU A 403 ? 0.2611 0.2596 0.1945 0.0521 0.0061 -0.0043 444 GLU A CA 3186 C C . GLU A 403 ? 0.2725 0.2657 0.1948 0.0579 0.0067 -0.0041 444 GLU A C 3187 O O . GLU A 403 ? 0.2740 0.2623 0.1867 0.0635 0.0047 -0.0060 444 GLU A O 3188 C CB . GLU A 403 ? 0.2862 0.2857 0.2221 0.0536 0.0117 -0.0019 444 GLU A CB 3189 C CG . GLU A 403 ? 0.2907 0.2953 0.2375 0.0484 0.0104 -0.0020 444 GLU A CG 3190 C CD . GLU A 403 ? 0.3585 0.3626 0.3056 0.0468 0.0036 -0.0053 444 GLU A CD 3191 O OE1 . GLU A 403 ? 0.3005 0.3008 0.2410 0.0492 -0.0007 -0.0080 444 GLU A OE1 3192 O OE2 . GLU A 403 ? 0.3444 0.3519 0.2992 0.0428 0.0023 -0.0051 444 GLU A OE2 3193 N N . ARG A 404 ? 0.2701 0.2636 0.1931 0.0568 0.0085 -0.0024 445 ARG A N 3194 C CA . ARG A 404 ? 0.2685 0.2563 0.1802 0.0629 0.0099 -0.0012 445 ARG A CA 3195 C C . ARG A 404 ? 0.2919 0.2793 0.2033 0.0621 0.0052 -0.0029 445 ARG A C 3196 O O . ARG A 404 ? 0.3017 0.2839 0.2032 0.0675 0.0043 -0.0027 445 ARG A O 3197 C CB . ARG A 404 ? 0.2830 0.2699 0.1947 0.0642 0.0185 0.0038 445 ARG A CB 3198 C CG . ARG A 404 ? 0.2949 0.2824 0.2078 0.0658 0.0244 0.0059 445 ARG A CG 3199 C CD . ARG A 404 ? 0.2876 0.2748 0.2033 0.0662 0.0334 0.0112 445 ARG A CD 3200 N NE . ARG A 404 ? 0.2739 0.2637 0.1956 0.0662 0.0388 0.0129 445 ARG A NE 3201 C CZ . ARG A 404 ? 0.2666 0.2583 0.1964 0.0651 0.0468 0.0173 445 ARG A CZ 3202 N NH1 . ARG A 404 ? 0.2905 0.2810 0.2224 0.0638 0.0503 0.0205 445 ARG A NH1 3203 N NH2 . ARG A 404 ? 0.2752 0.2704 0.2127 0.0648 0.0508 0.0182 445 ARG A NH2 3204 N N . GLY A 405 ? 0.2687 0.2613 0.1905 0.0558 0.0020 -0.0046 446 GLY A N 3205 C CA . GLY A 405 ? 0.2749 0.2683 0.1990 0.0544 -0.0012 -0.0059 446 GLY A CA 3206 C C . GLY A 405 ? 0.2715 0.2627 0.1917 0.0572 -0.0088 -0.0101 446 GLY A C 3207 O O . GLY A 405 ? 0.2852 0.2788 0.2107 0.0544 -0.0133 -0.0130 446 GLY A O 3208 N N . VAL A 406 ? 0.2874 0.2741 0.1993 0.0626 -0.0107 -0.0103 447 VAL A N 3209 C CA . VAL A 406 ? 0.2807 0.2652 0.1899 0.0657 -0.0191 -0.0149 447 VAL A CA 3210 C C . VAL A 406 ? 0.2809 0.2705 0.2015 0.0611 -0.0228 -0.0170 447 VAL A C 3211 O O . VAL A 406 ? 0.2712 0.2633 0.1987 0.0586 -0.0283 -0.0206 447 VAL A O 3212 C CB . VAL A 406 ? 0.3088 0.2859 0.2036 0.0741 -0.0204 -0.0145 447 VAL A CB 3213 C CG1 . VAL A 406 ? 0.3292 0.3046 0.2229 0.0771 -0.0300 -0.0196 447 VAL A CG1 3214 C CG2 . VAL A 406 ? 0.3376 0.3098 0.2212 0.0789 -0.0170 -0.0133 447 VAL A CG2 3215 N N . ALA A 407 ? 0.2717 0.2624 0.1946 0.0600 -0.0194 -0.0146 448 ALA A N 3216 C CA . ALA A 407 ? 0.2583 0.2533 0.1911 0.0568 -0.0225 -0.0166 448 ALA A CA 3217 C C . ALA A 407 ? 0.2714 0.2681 0.2075 0.0545 -0.0168 -0.0134 448 ALA A C 3218 O O . ALA A 407 ? 0.2837 0.2766 0.2130 0.0570 -0.0117 -0.0097 448 ALA A O 3219 C CB . ALA A 407 ? 0.2842 0.2759 0.2129 0.0625 -0.0297 -0.0197 448 ALA A CB 3220 N N . TYR A 408 ? 0.2536 0.2556 0.2006 0.0497 -0.0174 -0.0149 449 TYR A N 3221 C CA . TYR A 408 ? 0.2493 0.2529 0.2007 0.0476 -0.0132 -0.0131 449 TYR A CA 3222 C C . TYR A 408 ? 0.2564 0.2620 0.2136 0.0485 -0.0174 -0.0158 449 TYR A C 3223 O O . TYR A 408 ? 0.2531 0.2632 0.2187 0.0458 -0.0210 -0.0189 449 TYR A O 3224 C CB . TYR A 408 ? 0.2390 0.2477 0.1983 0.0407 -0.0090 -0.0124 449 TYR A CB 3225 C CG . TYR A 408 ? 0.2372 0.2472 0.2010 0.0386 -0.0054 -0.0114 449 TYR A CG 3226 C CD1 . TYR A 408 ? 0.2467 0.2537 0.2075 0.0391 -0.0005 -0.0082 449 TYR A CD1 3227 C CD2 . TYR A 408 ? 0.2721 0.2861 0.2438 0.0362 -0.0066 -0.0138 449 TYR A CD2 3228 C CE1 . TYR A 408 ? 0.2717 0.2791 0.2371 0.0374 0.0024 -0.0077 449 TYR A CE1 3229 C CE2 . TYR A 408 ? 0.2516 0.2663 0.2271 0.0347 -0.0034 -0.0134 449 TYR A CE2 3230 C CZ . TYR A 408 ? 0.2638 0.2750 0.2359 0.0353 0.0007 -0.0105 449 TYR A CZ 3231 O OH . TYR A 408 ? 0.2594 0.2707 0.2357 0.0339 0.0034 -0.0106 449 TYR A OH 3232 N N . ILE A 409 ? 0.2482 0.2505 0.2019 0.0521 -0.0166 -0.0143 450 ILE A N 3233 C CA . ILE A 409 ? 0.2411 0.2452 0.2011 0.0532 -0.0199 -0.0165 450 ILE A CA 3234 C C . ILE A 409 ? 0.2396 0.2453 0.2048 0.0502 -0.0145 -0.0149 450 ILE A C 3235 O O . ILE A 409 ? 0.2551 0.2564 0.2148 0.0516 -0.0101 -0.0114 450 ILE A O 3236 C CB . ILE A 409 ? 0.2618 0.2596 0.2125 0.0611 -0.0244 -0.0164 450 ILE A CB 3237 C CG1 . ILE A 409 ? 0.2891 0.2843 0.2330 0.0649 -0.0305 -0.0187 450 ILE A CG1 3238 C CG2 . ILE A 409 ? 0.2787 0.2787 0.2372 0.0627 -0.0285 -0.0189 450 ILE A CG2 3239 C CD1 . ILE A 409 ? 0.3004 0.3015 0.2557 0.0615 -0.0361 -0.0234 450 ILE A CD1 3240 N N . ASN A 410 ? 0.2330 0.2448 0.2093 0.0461 -0.0144 -0.0174 451 ASN A N 3241 C CA . ASN A 410 ? 0.2450 0.2582 0.2261 0.0434 -0.0097 -0.0167 451 ASN A CA 3242 C C . ASN A 410 ? 0.2594 0.2699 0.2411 0.0478 -0.0111 -0.0168 451 ASN A C 3243 O O . ASN A 410 ? 0.2852 0.2944 0.2657 0.0525 -0.0166 -0.0181 451 ASN A O 3244 C CB . ASN A 410 ? 0.2344 0.2545 0.2257 0.0381 -0.0087 -0.0193 451 ASN A CB 3245 C CG . ASN A 410 ? 0.2488 0.2699 0.2424 0.0342 -0.0031 -0.0187 451 ASN A CG 3246 O OD1 . ASN A 410 ? 0.2678 0.2865 0.2568 0.0327 -0.0001 -0.0165 451 ASN A OD1 3247 N ND2 . ASN A 410 ? 0.2583 0.2830 0.2595 0.0330 -0.0020 -0.0209 451 ASN A ND2 3248 N N . ALA A 411 ? 0.2473 0.2568 0.2310 0.0465 -0.0067 -0.0156 452 ALA A N 3249 C CA . ALA A 411 ? 0.2663 0.2726 0.2508 0.0508 -0.0078 -0.0155 452 ALA A CA 3250 C C . ALA A 411 ? 0.2676 0.2755 0.2589 0.0475 -0.0034 -0.0162 452 ALA A C 3251 O O . ALA A 411 ? 0.2793 0.2821 0.2683 0.0489 -0.0005 -0.0140 452 ALA A O 3252 C CB . ALA A 411 ? 0.2953 0.2931 0.2685 0.0558 -0.0072 -0.0113 452 ALA A CB 3253 N N . ASP A 412 ? 0.2695 0.2841 0.2692 0.0434 -0.0027 -0.0194 453 ASP A N 3254 C CA . ASP A 412 ? 0.2596 0.2761 0.2660 0.0418 0.0004 -0.0213 453 ASP A CA 3255 C C . ASP A 412 ? 0.2730 0.2901 0.2850 0.0463 -0.0030 -0.0231 453 ASP A C 3256 O O . ASP A 412 ? 0.2731 0.2871 0.2813 0.0511 -0.0075 -0.0221 453 ASP A O 3257 C CB . ASP A 412 ? 0.2434 0.2659 0.2548 0.0364 0.0032 -0.0236 453 ASP A CB 3258 C CG . ASP A 412 ? 0.2894 0.3118 0.3039 0.0344 0.0075 -0.0253 453 ASP A CG 3259 O OD1 . ASP A 412 ? 0.2917 0.3103 0.3070 0.0371 0.0080 -0.0252 453 ASP A OD1 3260 O OD2 . ASP A 412 ? 0.2545 0.2804 0.2702 0.0305 0.0100 -0.0268 453 ASP A OD2 3261 N N . SER A 413 ? 0.2568 0.2775 0.2772 0.0453 -0.0010 -0.0259 454 SER A N 3262 C CA A SER A 413 ? 0.2682 0.2894 0.2952 0.0498 -0.0037 -0.0277 454 SER A CA 3263 C CA B SER A 413 ? 0.2738 0.2950 0.3008 0.0498 -0.0037 -0.0277 454 SER A CA 3264 C C . SER A 413 ? 0.2771 0.2997 0.3058 0.0538 -0.0105 -0.0283 454 SER A C 3265 O O . SER A 413 ? 0.2746 0.3022 0.3068 0.0518 -0.0125 -0.0298 454 SER A O 3266 C CB A SER A 413 ? 0.2752 0.3028 0.3128 0.0475 -0.0006 -0.0314 454 SER A CB 3267 C CB B SER A 413 ? 0.2754 0.3029 0.3131 0.0476 -0.0005 -0.0314 454 SER A CB 3268 O OG A SER A 413 ? 0.2430 0.2689 0.2780 0.0441 0.0048 -0.0315 454 SER A OG 3269 O OG B SER A 413 ? 0.2807 0.3156 0.3246 0.0444 -0.0004 -0.0332 454 SER A OG 3270 N N . SER A 414 ? 0.2825 0.2998 0.3082 0.0597 -0.0142 -0.0273 455 SER A N 3271 C CA . SER A 414 ? 0.3072 0.3251 0.3339 0.0645 -0.0219 -0.0285 455 SER A CA 3272 C C . SER A 414 ? 0.2920 0.3179 0.3345 0.0649 -0.0246 -0.0328 455 SER A C 3273 O O . SER A 414 ? 0.3019 0.3307 0.3490 0.0672 -0.0312 -0.0349 455 SER A O 3274 C CB . SER A 414 ? 0.3213 0.3302 0.3381 0.0713 -0.0253 -0.0256 455 SER A CB 3275 O OG . SER A 414 ? 0.3524 0.3546 0.3559 0.0708 -0.0222 -0.0213 455 SER A OG 3276 N N . ILE A 415 ? 0.3007 0.3300 0.3518 0.0630 -0.0198 -0.0345 456 ILE A N 3277 C CA . ILE A 415 ? 0.3229 0.3601 0.3902 0.0637 -0.0211 -0.0385 456 ILE A CA 3278 C C . ILE A 415 ? 0.3291 0.3726 0.4041 0.0581 -0.0134 -0.0402 456 ILE A C 3279 O O . ILE A 415 ? 0.3597 0.4000 0.4281 0.0555 -0.0077 -0.0389 456 ILE A O 3280 C CB . ILE A 415 ? 0.3219 0.3561 0.3929 0.0698 -0.0238 -0.0392 456 ILE A CB 3281 C CG1 . ILE A 415 ? 0.3582 0.3851 0.4209 0.0698 -0.0182 -0.0367 456 ILE A CG1 3282 C CG2 . ILE A 415 ? 0.3764 0.4057 0.4418 0.0762 -0.0327 -0.0383 456 ILE A CG2 3283 C CD1 . ILE A 415 ? 0.3890 0.4154 0.4599 0.0734 -0.0173 -0.0386 456 ILE A CD1 3284 N N . GLU A 416 ? 0.3152 0.3675 0.4042 0.0563 -0.0133 -0.0431 457 GLU A N 3285 C CA . GLU A 416 ? 0.3236 0.3818 0.4208 0.0526 -0.0055 -0.0449 457 GLU A CA 3286 C C . GLU A 416 ? 0.3189 0.3849 0.4346 0.0549 -0.0070 -0.0484 457 GLU A C 3287 O O . GLU A 416 ? 0.3320 0.4047 0.4580 0.0523 -0.0009 -0.0502 457 GLU A O 3288 C CB . GLU A 416 ? 0.3223 0.3835 0.4169 0.0464 -0.0013 -0.0439 457 GLU A CB 3289 C CG . GLU A 416 ? 0.3368 0.4034 0.4398 0.0450 -0.0056 -0.0445 457 GLU A CG 3290 C CD . GLU A 416 ? 0.3299 0.3973 0.4276 0.0393 -0.0023 -0.0426 457 GLU A CD 3291 O OE1 . GLU A 416 ? 0.3335 0.3968 0.4192 0.0367 0.0024 -0.0407 457 GLU A OE1 3292 O OE2 . GLU A 416 ? 0.3224 0.3943 0.4285 0.0374 -0.0048 -0.0432 457 GLU A OE2 3293 N N . GLY A 417 ? 0.3242 0.3891 0.4438 0.0602 -0.0152 -0.0492 458 GLY A N 3294 C CA . GLY A 417 ? 0.3162 0.3884 0.4546 0.0633 -0.0189 -0.0526 458 GLY A CA 3295 C C . GLY A 417 ? 0.3345 0.4021 0.4702 0.0696 -0.0296 -0.0527 458 GLY A C 3296 O O . GLY A 417 ? 0.3460 0.4048 0.4647 0.0714 -0.0327 -0.0498 458 GLY A O 3297 N N . ASN A 418 ? 0.3152 0.3886 0.4675 0.0733 -0.0353 -0.0560 459 ASN A N 3298 C CA . ASN A 418 ? 0.3284 0.3973 0.4781 0.0801 -0.0466 -0.0566 459 ASN A CA 3299 C C . ASN A 418 ? 0.3125 0.3890 0.4788 0.0807 -0.0547 -0.0603 459 ASN A C 3300 O O . ASN A 418 ? 0.3359 0.4117 0.5074 0.0870 -0.0644 -0.0625 459 ASN A O 3301 C CB . ASN A 418 ? 0.3423 0.4080 0.4940 0.0864 -0.0480 -0.0571 459 ASN A CB 3302 C CG . ASN A 418 ? 0.3648 0.4408 0.5400 0.0868 -0.0457 -0.0612 459 ASN A CG 3303 O OD1 . ASN A 418 ? 0.3902 0.4760 0.5811 0.0825 -0.0429 -0.0634 459 ASN A OD1 3304 N ND2 . ASN A 418 ? 0.4558 0.5294 0.6341 0.0923 -0.0466 -0.0619 459 ASN A ND2 3305 N N . TYR A 419 ? 0.3042 0.3876 0.4792 0.0743 -0.0509 -0.0610 460 TYR A N 3306 C CA . TYR A 419 ? 0.2979 0.3899 0.4932 0.0736 -0.0570 -0.0648 460 TYR A CA 3307 C C . TYR A 419 ? 0.3012 0.3885 0.4874 0.0745 -0.0663 -0.0650 460 TYR A C 3308 O O . TYR A 419 ? 0.3100 0.3972 0.5022 0.0795 -0.0776 -0.0681 460 TYR A O 3309 C CB . TYR A 419 ? 0.2962 0.3981 0.5075 0.0663 -0.0474 -0.0652 460 TYR A CB 3310 C CG . TYR A 419 ? 0.3357 0.4467 0.5704 0.0649 -0.0526 -0.0687 460 TYR A CG 3311 C CD1 . TYR A 419 ? 0.3792 0.4965 0.6346 0.0695 -0.0591 -0.0728 460 TYR A CD1 3312 C CD2 . TYR A 419 ? 0.3918 0.5052 0.6295 0.0589 -0.0511 -0.0681 460 TYR A CD2 3313 C CE1 . TYR A 419 ? 0.4175 0.5436 0.6971 0.0679 -0.0644 -0.0764 460 TYR A CE1 3314 C CE2 . TYR A 419 ? 0.4156 0.5373 0.6770 0.0573 -0.0561 -0.0714 460 TYR A CE2 3315 C CZ . TYR A 419 ? 0.4321 0.5603 0.7146 0.0615 -0.0625 -0.0756 460 TYR A CZ 3316 O OH . TYR A 419 ? 0.4813 0.6179 0.7891 0.0596 -0.0676 -0.0791 460 TYR A OH 3317 N N . THR A 420 ? 0.2856 0.3689 0.4574 0.0699 -0.0619 -0.0620 461 THR A N 3318 C CA . THR A 420 ? 0.2932 0.3718 0.4561 0.0709 -0.0704 -0.0625 461 THR A CA 3319 C C . THR A 420 ? 0.2844 0.3553 0.4252 0.0680 -0.0653 -0.0582 461 THR A C 3320 O O . THR A 420 ? 0.2806 0.3503 0.4139 0.0647 -0.0555 -0.0550 461 THR A O 3321 C CB . THR A 420 ? 0.2986 0.3856 0.4822 0.0671 -0.0742 -0.0661 461 THR A CB 3322 O OG1 . THR A 420 ? 0.3282 0.4101 0.5045 0.0700 -0.0852 -0.0680 461 THR A OG1 3323 C CG2 . THR A 420 ? 0.2916 0.3833 0.4795 0.0586 -0.0635 -0.0638 461 THR A CG2 3324 N N . LEU A 421 ? 0.2785 0.3445 0.4093 0.0692 -0.0720 -0.0585 462 LEU A N 3325 C CA . LEU A 421 ? 0.2736 0.3331 0.3851 0.0664 -0.0673 -0.0547 462 LEU A CA 3326 C C . LEU A 421 ? 0.2680 0.3329 0.3861 0.0581 -0.0594 -0.0536 462 LEU A C 3327 O O . LEU A 421 ? 0.2773 0.3498 0.4140 0.0548 -0.0605 -0.0563 462 LEU A O 3328 C CB . LEU A 421 ? 0.2817 0.3342 0.3810 0.0707 -0.0770 -0.0558 462 LEU A CB 3329 C CG . LEU A 421 ? 0.2800 0.3243 0.3570 0.0701 -0.0734 -0.0518 462 LEU A CG 3330 C CD1 . LEU A 421 ? 0.3232 0.3603 0.3843 0.0735 -0.0687 -0.0476 462 LEU A CD1 3331 C CD2 . LEU A 421 ? 0.3178 0.3563 0.3855 0.0746 -0.0834 -0.0539 462 LEU A CD2 3332 N N . ARG A 422 ? 0.2518 0.3126 0.3554 0.0550 -0.0517 -0.0497 463 ARG A N 3333 C CA . ARG A 422 ? 0.2633 0.3270 0.3685 0.0480 -0.0451 -0.0481 463 ARG A CA 3334 C C . ARG A 422 ? 0.2662 0.3222 0.3525 0.0482 -0.0461 -0.0456 463 ARG A C 3335 O O . ARG A 422 ? 0.2752 0.3245 0.3461 0.0512 -0.0448 -0.0431 463 ARG A O 3336 C CB . ARG A 422 ? 0.2694 0.3357 0.3749 0.0441 -0.0342 -0.0459 463 ARG A CB 3337 C CG . ARG A 422 ? 0.3225 0.3898 0.4246 0.0377 -0.0274 -0.0435 463 ARG A CG 3338 C CD . ARG A 422 ? 0.3558 0.4246 0.4561 0.0346 -0.0176 -0.0417 463 ARG A CD 3339 N NE . ARG A 422 ? 0.3720 0.4387 0.4626 0.0300 -0.0126 -0.0389 463 ARG A NE 3340 C CZ . ARG A 422 ? 0.4052 0.4712 0.4896 0.0273 -0.0051 -0.0372 463 ARG A CZ 3341 N NH1 . ARG A 422 ? 0.3968 0.4640 0.4835 0.0288 -0.0012 -0.0382 463 ARG A NH1 3342 N NH2 . ARG A 422 ? 0.3899 0.4539 0.4657 0.0235 -0.0019 -0.0349 463 ARG A NH2 3343 N N . VAL A 423 ? 0.2618 0.3187 0.3503 0.0450 -0.0479 -0.0462 464 VAL A N 3344 C CA . VAL A 423 ? 0.2469 0.2971 0.3187 0.0449 -0.0481 -0.0440 464 VAL A CA 3345 C C . VAL A 423 ? 0.2502 0.3034 0.3257 0.0381 -0.0425 -0.0425 464 VAL A C 3346 O O . VAL A 423 ? 0.2550 0.3138 0.3458 0.0348 -0.0433 -0.0443 464 VAL A O 3347 C CB . VAL A 423 ? 0.2605 0.3063 0.3280 0.0496 -0.0585 -0.0468 464 VAL A CB 3348 C CG1 . VAL A 423 ? 0.2689 0.3082 0.3199 0.0494 -0.0575 -0.0444 464 VAL A CG1 3349 C CG2 . VAL A 423 ? 0.2981 0.3396 0.3594 0.0572 -0.0646 -0.0479 464 VAL A CG2 3350 N N . ASP A 424 ? 0.2435 0.2932 0.3062 0.0359 -0.0366 -0.0390 465 ASP A N 3351 C CA . ASP A 424 ? 0.2548 0.3058 0.3179 0.0302 -0.0321 -0.0372 465 ASP A CA 3352 C C . ASP A 424 ? 0.2562 0.3003 0.3038 0.0321 -0.0345 -0.0358 465 ASP A C 3353 O O . ASP A 424 ? 0.2522 0.2917 0.2872 0.0347 -0.0327 -0.0338 465 ASP A O 3354 C CB . ASP A 424 ? 0.2495 0.3025 0.3107 0.0259 -0.0227 -0.0344 465 ASP A CB 3355 C CG . ASP A 424 ? 0.3063 0.3651 0.3791 0.0251 -0.0185 -0.0355 465 ASP A CG 3356 O OD1 . ASP A 424 ? 0.2986 0.3609 0.3831 0.0274 -0.0223 -0.0382 465 ASP A OD1 3357 O OD2 . ASP A 424 ? 0.3548 0.4145 0.4246 0.0222 -0.0111 -0.0336 465 ASP A OD2 3358 N N . CYS A 425 ? 0.2568 0.3000 0.3056 0.0306 -0.0377 -0.0366 466 CYS A N 3359 C CA . CYS A 425 ? 0.2447 0.2813 0.2787 0.0329 -0.0397 -0.0355 466 CYS A CA 3360 C C . CYS A 425 ? 0.2505 0.2868 0.2878 0.0298 -0.0415 -0.0360 466 CYS A C 3361 O O . CYS A 425 ? 0.2867 0.3274 0.3380 0.0264 -0.0425 -0.0375 466 CYS A O 3362 C CB . CYS A 425 ? 0.2546 0.2858 0.2800 0.0402 -0.0470 -0.0375 466 CYS A CB 3363 S SG . CYS A 425 ? 0.2849 0.3171 0.3214 0.0430 -0.0580 -0.0431 466 CYS A SG 3364 N N . THR A 426 ? 0.2431 0.2742 0.2680 0.0311 -0.0417 -0.0347 467 THR A N 3365 C CA . THR A 426 ? 0.2386 0.2680 0.2649 0.0295 -0.0447 -0.0357 467 THR A CA 3366 C C . THR A 426 ? 0.2611 0.2895 0.2942 0.0325 -0.0540 -0.0405 467 THR A C 3367 O O . THR A 426 ? 0.2552 0.2812 0.2837 0.0381 -0.0592 -0.0427 467 THR A O 3368 C CB . THR A 426 ? 0.2335 0.2572 0.2446 0.0316 -0.0433 -0.0336 467 THR A CB 3369 O OG1 . THR A 426 ? 0.2465 0.2678 0.2586 0.0310 -0.0472 -0.0352 467 THR A OG1 3370 C CG2 . THR A 426 ? 0.2537 0.2720 0.2514 0.0388 -0.0462 -0.0342 467 THR A CG2 3371 N N . PRO A 427 ? 0.2462 0.2758 0.2898 0.0290 -0.0565 -0.0420 468 PRO A N 3372 C CA . PRO A 427 ? 0.2573 0.2850 0.3073 0.0319 -0.0664 -0.0472 468 PRO A CA 3373 C C . PRO A 427 ? 0.2639 0.2840 0.2971 0.0392 -0.0723 -0.0493 468 PRO A C 3374 O O . PRO A 427 ? 0.2825 0.3005 0.3175 0.0437 -0.0813 -0.0540 468 PRO A O 3375 C CB . PRO A 427 ? 0.2862 0.3141 0.3457 0.0268 -0.0665 -0.0472 468 PRO A CB 3376 C CG . PRO A 427 ? 0.2566 0.2897 0.3216 0.0205 -0.0566 -0.0424 468 PRO A CG 3377 C CD . PRO A 427 ? 0.2534 0.2852 0.3028 0.0225 -0.0507 -0.0390 468 PRO A CD 3378 N N . LEU A 428 ? 0.2587 0.2745 0.2760 0.0406 -0.0676 -0.0460 469 LEU A N 3379 C CA . LEU A 428 ? 0.2846 0.2926 0.2850 0.0480 -0.0722 -0.0477 469 LEU A CA 3380 C C . LEU A 428 ? 0.2888 0.2948 0.2820 0.0542 -0.0754 -0.0488 469 LEU A C 3381 O O . LEU A 428 ? 0.3297 0.3292 0.3106 0.0612 -0.0812 -0.0513 469 LEU A O 3382 C CB . LEU A 428 ? 0.2678 0.2726 0.2541 0.0483 -0.0652 -0.0435 469 LEU A CB 3383 C CG . LEU A 428 ? 0.2750 0.2796 0.2652 0.0441 -0.0640 -0.0431 469 LEU A CG 3384 C CD1 . LEU A 428 ? 0.2995 0.3015 0.2771 0.0448 -0.0574 -0.0390 469 LEU A CD1 3385 C CD2 . LEU A 428 ? 0.2917 0.2917 0.2835 0.0468 -0.0732 -0.0484 469 LEU A CD2 3386 N N . MET A 429 ? 0.2887 0.2998 0.2889 0.0523 -0.0717 -0.0470 470 MET A N 3387 C CA A MET A 429 ? 0.2872 0.2964 0.2813 0.0582 -0.0744 -0.0475 470 MET A CA 3388 C CA B MET A 429 ? 0.2920 0.3007 0.2856 0.0586 -0.0750 -0.0478 470 MET A CA 3389 C C . MET A 429 ? 0.2944 0.3072 0.3026 0.0593 -0.0823 -0.0521 470 MET A C 3390 O O . MET A 429 ? 0.2957 0.3068 0.2998 0.0646 -0.0855 -0.0528 470 MET A O 3391 C CB A MET A 429 ? 0.2933 0.3049 0.2850 0.0563 -0.0654 -0.0426 470 MET A CB 3392 C CB B MET A 429 ? 0.2965 0.3054 0.2826 0.0583 -0.0663 -0.0426 470 MET A CB 3393 C CG A MET A 429 ? 0.2752 0.2821 0.2514 0.0573 -0.0587 -0.0382 470 MET A CG 3394 C CG B MET A 429 ? 0.2959 0.2987 0.2647 0.0609 -0.0618 -0.0393 470 MET A CG 3395 S SD A MET A 429 ? 0.2988 0.3079 0.2740 0.0553 -0.0495 -0.0333 470 MET A SD 3396 S SD B MET A 429 ? 0.3187 0.3203 0.2787 0.0615 -0.0526 -0.0335 470 MET A SD 3397 C CE A MET A 429 ? 0.3180 0.3230 0.2799 0.0549 -0.0424 -0.0289 470 MET A CE 3398 C CE B MET A 429 ? 0.3021 0.3110 0.2736 0.0521 -0.0443 -0.0308 470 MET A CE 3399 N N . TYR A 430 ? 0.2880 0.3056 0.3136 0.0546 -0.0853 -0.0550 471 TYR A N 3400 C CA . TYR A 430 ? 0.2834 0.3056 0.3256 0.0552 -0.0925 -0.0594 471 TYR A CA 3401 C C . TYR A 430 ? 0.3093 0.3255 0.3433 0.0638 -0.1039 -0.0641 471 TYR A C 3402 O O . TYR A 430 ? 0.3178 0.3357 0.3564 0.0674 -0.1082 -0.0659 471 TYR A O 3403 C CB . TYR A 430 ? 0.2823 0.3094 0.3446 0.0492 -0.0948 -0.0620 471 TYR A CB 3404 C CG . TYR A 430 ? 0.2666 0.3008 0.3419 0.0407 -0.0848 -0.0581 471 TYR A CG 3405 C CD1 . TYR A 430 ? 0.2676 0.3042 0.3375 0.0386 -0.0748 -0.0531 471 TYR A CD1 3406 C CD2 . TYR A 430 ? 0.2886 0.3264 0.3813 0.0351 -0.0856 -0.0594 471 TYR A CD2 3407 C CE1 . TYR A 430 ? 0.2783 0.3206 0.3587 0.0313 -0.0661 -0.0498 471 TYR A CE1 3408 C CE2 . TYR A 430 ? 0.2993 0.3426 0.4023 0.0279 -0.0763 -0.0555 471 TYR A CE2 3409 C CZ . TYR A 430 ? 0.3013 0.3468 0.3976 0.0263 -0.0669 -0.0509 471 TYR A CZ 3410 O OH . TYR A 430 ? 0.3296 0.3798 0.4347 0.0197 -0.0580 -0.0472 471 TYR A OH 3411 N N . SER A 431 ? 0.3030 0.3120 0.3249 0.0676 -0.1092 -0.0665 472 SER A N 3412 C CA . SER A 431 ? 0.3223 0.3248 0.3357 0.0764 -0.1214 -0.0719 472 SER A CA 3413 C C . SER A 431 ? 0.3320 0.3290 0.3257 0.0836 -0.1197 -0.0689 472 SER A C 3414 O O . SER A 431 ? 0.3389 0.3335 0.3306 0.0900 -0.1282 -0.0722 472 SER A O 3415 C CB . SER A 431 ? 0.3390 0.3346 0.3433 0.0787 -0.1268 -0.0753 472 SER A CB 3416 O OG A SER A 431 ? 0.3616 0.3623 0.3876 0.0724 -0.1303 -0.0787 472 SER A OG 3417 O OG B SER A 431 ? 0.3030 0.2912 0.2967 0.0878 -0.1390 -0.0810 472 SER A OG 3418 N N . LEU A 432 ? 0.3365 0.3312 0.3166 0.0826 -0.1092 -0.0628 473 LEU A N 3419 C CA . LEU A 432 ? 0.3529 0.3424 0.3157 0.0885 -0.1057 -0.0589 473 LEU A CA 3420 C C . LEU A 432 ? 0.3464 0.3411 0.3209 0.0881 -0.1062 -0.0586 473 LEU A C 3421 O O . LEU A 432 ? 0.3667 0.3569 0.3327 0.0953 -0.1112 -0.0592 473 LEU A O 3422 C CB . LEU A 432 ? 0.3522 0.3407 0.3051 0.0854 -0.0933 -0.0523 473 LEU A CB 3423 C CG . LEU A 432 ? 0.3655 0.3506 0.3061 0.0887 -0.0866 -0.0468 473 LEU A CG 3424 C CD1 . LEU A 432 ? 0.4269 0.4017 0.3466 0.0992 -0.0918 -0.0471 473 LEU A CD1 3425 C CD2 . LEU A 432 ? 0.4190 0.4054 0.3564 0.0834 -0.0749 -0.0413 473 LEU A CD2 3426 N N . VAL A 433 ? 0.3260 0.3299 0.3193 0.0801 -0.1005 -0.0574 474 VAL A N 3427 C CA . VAL A 433 ? 0.3269 0.3364 0.3322 0.0795 -0.0996 -0.0571 474 VAL A CA 3428 C C . VAL A 433 ? 0.3412 0.3525 0.3581 0.0834 -0.1114 -0.0630 474 VAL A C 3429 O O . VAL A 433 ? 0.3499 0.3601 0.3652 0.0885 -0.1147 -0.0632 474 VAL A O 3430 C CB . VAL A 433 ? 0.3031 0.3218 0.3254 0.0702 -0.0907 -0.0549 474 VAL A CB 3431 C CG1 . VAL A 433 ? 0.3499 0.3750 0.3870 0.0697 -0.0903 -0.0555 474 VAL A CG1 3432 C CG2 . VAL A 433 ? 0.3280 0.3447 0.3383 0.0672 -0.0795 -0.0489 474 VAL A CG2 3433 N N . HIS A 434 ? 0.3396 0.3533 0.3686 0.0813 -0.1185 -0.0681 475 HIS A N 3434 C CA . HIS A 434 ? 0.3560 0.3715 0.3978 0.0851 -0.1312 -0.0746 475 HIS A CA 3435 C C . HIS A 434 ? 0.3693 0.3747 0.3902 0.0961 -0.1403 -0.0765 475 HIS A C 3436 O O . HIS A 434 ? 0.3959 0.4017 0.4202 0.1011 -0.1465 -0.0784 475 HIS A O 3437 C CB . HIS A 434 ? 0.3484 0.3663 0.4047 0.0815 -0.1378 -0.0798 475 HIS A CB 3438 C CG . HIS A 434 ? 0.3920 0.4194 0.4701 0.0713 -0.1298 -0.0782 475 HIS A CG 3439 N ND1 . HIS A 434 ? 0.4697 0.4979 0.5560 0.0663 -0.1304 -0.0797 475 HIS A ND1 3440 C CD2 . HIS A 434 ? 0.4144 0.4500 0.5056 0.0656 -0.1204 -0.0746 475 HIS A CD2 3441 C CE1 . HIS A 434 ? 0.4740 0.5105 0.5781 0.0579 -0.1218 -0.0770 475 HIS A CE1 3442 N NE2 . HIS A 434 ? 0.3918 0.4330 0.4990 0.0575 -0.1157 -0.0741 475 HIS A NE2 3443 N N . ASN A 435 ? 0.3611 0.3573 0.3599 0.1000 -0.1403 -0.0755 476 ASN A N 3444 C CA . ASN A 435 ? 0.3967 0.3822 0.3735 0.1111 -0.1490 -0.0775 476 ASN A CA 3445 C C . ASN A 435 ? 0.4053 0.3872 0.3694 0.1159 -0.1445 -0.0724 476 ASN A C 3446 O O . ASN A 435 ? 0.4273 0.4042 0.3839 0.1243 -0.1535 -0.0746 476 ASN A O 3447 C CB . ASN A 435 ? 0.4100 0.3863 0.3650 0.1144 -0.1482 -0.0770 476 ASN A CB 3448 C CG . ASN A 435 ? 0.4440 0.4207 0.4081 0.1125 -0.1565 -0.0836 476 ASN A CG 3449 O OD1 . ASN A 435 ? 0.4315 0.4157 0.4196 0.1081 -0.1624 -0.0882 476 ASN A OD1 3450 N ND2 . ASN A 435 ? 0.4292 0.3976 0.3746 0.1161 -0.1566 -0.0840 476 ASN A ND2 3451 N N . LEU A 436 ? 0.3940 0.3783 0.3564 0.1108 -0.1312 -0.0657 477 LEU A N 3452 C CA . LEU A 436 ? 0.3822 0.3626 0.3331 0.1148 -0.1260 -0.0604 477 LEU A CA 3453 C C . LEU A 436 ? 0.3736 0.3601 0.3418 0.1150 -0.1304 -0.0624 477 LEU A C 3454 O O . LEU A 436 ? 0.3870 0.3680 0.3459 0.1227 -0.1350 -0.0619 477 LEU A O 3455 C CB . LEU A 436 ? 0.3623 0.3443 0.3100 0.1084 -0.1109 -0.0533 477 LEU A CB 3456 C CG . LEU A 436 ? 0.3991 0.3778 0.3386 0.1112 -0.1046 -0.0477 477 LEU A CG 3457 C CD1 . LEU A 436 ? 0.4252 0.3916 0.3405 0.1220 -0.1091 -0.0461 477 LEU A CD1 3458 C CD2 . LEU A 436 ? 0.3824 0.3633 0.3213 0.1042 -0.0906 -0.0416 477 LEU A CD2 3459 N N . THR A 437 ? 0.3704 0.3682 0.3637 0.1069 -0.1283 -0.0644 478 THR A N 3460 C CA . THR A 437 ? 0.3534 0.3580 0.3650 0.1070 -0.1312 -0.0662 478 THR A CA 3461 C C . THR A 437 ? 0.3829 0.3863 0.3998 0.1141 -0.1466 -0.0728 478 THR A C 3462 O O . THR A 437 ? 0.3822 0.3878 0.4070 0.1176 -0.1506 -0.0738 478 THR A O 3463 C CB . THR A 437 ? 0.3438 0.3607 0.3808 0.0970 -0.1241 -0.0664 478 THR A CB 3464 O OG1 . THR A 437 ? 0.3298 0.3514 0.3805 0.0925 -0.1283 -0.0707 478 THR A OG1 3465 C CG2 . THR A 437 ? 0.3119 0.3296 0.3428 0.0909 -0.1093 -0.0598 478 THR A CG2 3466 N N . LYS A 438 ? 0.3979 0.3973 0.4099 0.1168 -0.1557 -0.0775 479 LYS A N 3467 C CA . LYS A 438 ? 0.4250 0.4219 0.4397 0.1244 -0.1717 -0.0844 479 LYS A CA 3468 C C . LYS A 438 ? 0.4480 0.4330 0.4366 0.1358 -0.1765 -0.0825 479 LYS A C 3469 O O . LYS A 438 ? 0.4641 0.4467 0.4540 0.1434 -0.1895 -0.0873 479 LYS A O 3470 C CB . LYS A 438 ? 0.4374 0.4325 0.4535 0.1240 -0.1801 -0.0904 479 LYS A CB 3471 C CG . LYS A 438 ? 0.4281 0.4352 0.4755 0.1140 -0.1796 -0.0939 479 LYS A CG 3472 C CD . LYS A 438 ? 0.4855 0.4897 0.5331 0.1130 -0.1865 -0.0990 479 LYS A CD 3473 C CE . LYS A 438 ? 0.4723 0.4876 0.5497 0.1023 -0.1830 -0.1006 479 LYS A CE 3474 N NZ . LYS A 438 ? 0.4779 0.4904 0.5592 0.1014 -0.1913 -0.1064 479 LYS A NZ 3475 N N . GLU A 439 ? 0.4530 0.4304 0.4185 0.1371 -0.1662 -0.0755 480 GLU A N 3476 C CA . GLU A 439 ? 0.4895 0.4545 0.4280 0.1477 -0.1685 -0.0723 480 GLU A CA 3477 C C . GLU A 439 ? 0.4793 0.4442 0.4169 0.1484 -0.1610 -0.0662 480 GLU A C 3478 O O . GLU A 439 ? 0.5134 0.4679 0.4303 0.1572 -0.1625 -0.0628 480 GLU A O 3479 C CB . GLU A 439 ? 0.5112 0.4661 0.4228 0.1502 -0.1621 -0.0682 480 GLU A CB 3480 C CG . GLU A 439 ? 0.6068 0.5590 0.5139 0.1514 -0.1698 -0.0740 480 GLU A CG 3481 C CD . GLU A 439 ? 0.6873 0.6345 0.5912 0.1605 -0.1876 -0.0819 480 GLU A CD 3482 O OE1 . GLU A 439 ? 0.7350 0.6753 0.6264 0.1698 -0.1938 -0.0813 480 GLU A OE1 3483 O OE2 . GLU A 439 ? 0.7434 0.6932 0.6574 0.1586 -0.1958 -0.0888 480 GLU A OE2 3484 N N . LEU A 440 ? 0.4411 0.4168 0.4005 0.1395 -0.1527 -0.0647 481 LEU A N 3485 C CA . LEU A 440 ? 0.4255 0.4017 0.3864 0.1396 -0.1455 -0.0596 481 LEU A CA 3486 C C . LEU A 440 ? 0.4383 0.4216 0.4206 0.1411 -0.1535 -0.0640 481 LEU A C 3487 O O . LEU A 440 ? 0.4418 0.4339 0.4453 0.1378 -0.1603 -0.0703 481 LEU A O 3488 C CB . LEU A 440 ? 0.4031 0.3859 0.3727 0.1292 -0.1305 -0.0550 481 LEU A CB 3489 C CG . LEU A 440 ? 0.4042 0.3811 0.3554 0.1270 -0.1214 -0.0502 481 LEU A CG 3490 C CD1 . LEU A 440 ? 0.3653 0.3498 0.3278 0.1167 -0.1081 -0.0466 481 LEU A CD1 3491 C CD2 . LEU A 440 ? 0.4442 0.4082 0.3691 0.1350 -0.1190 -0.0445 481 LEU A CD2 3492 N N . LYS A 441 ? 0.4394 0.4186 0.4165 0.1461 -0.1526 -0.0606 482 LYS A N 3493 C CA . LYS A 441 ? 0.4592 0.4449 0.4564 0.1483 -0.1597 -0.0644 482 LYS A CA 3494 C C . LYS A 441 ? 0.4373 0.4358 0.4599 0.1385 -0.1500 -0.0642 482 LYS A C 3495 O O . LYS A 441 ? 0.4420 0.4407 0.4605 0.1328 -0.1368 -0.0588 482 LYS A O 3496 C CB . LYS A 441 ? 0.4834 0.4592 0.4652 0.1578 -0.1623 -0.0607 482 LYS A CB 3497 C CG . LYS A 441 ? 0.5501 0.5118 0.5038 0.1688 -0.1715 -0.0603 482 LYS A CG 3498 C CD . LYS A 441 ? 0.6494 0.6026 0.5928 0.1785 -0.1760 -0.0574 482 LYS A CD 3499 C CE . LYS A 441 ? 0.7280 0.6643 0.6361 0.1874 -0.1746 -0.0511 482 LYS A CE 3500 N NZ . LYS A 441 ? 0.7962 0.7242 0.6867 0.1963 -0.1878 -0.0555 482 LYS A NZ 3501 N N . SER A 442 ? 0.4271 0.4366 0.4764 0.1364 -0.1562 -0.0701 483 SER A N 3502 C CA . SER A 442 ? 0.4148 0.4359 0.4875 0.1284 -0.1466 -0.0697 483 SER A CA 3503 C C . SER A 442 ? 0.4069 0.4255 0.4780 0.1324 -0.1432 -0.0664 483 SER A C 3504 O O . SER A 442 ? 0.4245 0.4385 0.4927 0.1412 -0.1532 -0.0680 483 SER A O 3505 C CB . SER A 442 ? 0.4056 0.4395 0.5091 0.1252 -0.1531 -0.0765 483 SER A CB 3506 O OG . SER A 442 ? 0.4113 0.4557 0.5354 0.1182 -0.1427 -0.0756 483 SER A OG 3507 N N . PRO A 443 ? 0.3925 0.4138 0.4661 0.1263 -0.1297 -0.0621 484 PRO A N 3508 C CA . PRO A 443 ? 0.4015 0.4210 0.4762 0.1293 -0.1257 -0.0594 484 PRO A CA 3509 C C . PRO A 443 ? 0.3955 0.4273 0.4993 0.1273 -0.1263 -0.0639 484 PRO A C 3510 O O . PRO A 443 ? 0.4090 0.4405 0.5170 0.1297 -0.1234 -0.0625 484 PRO A O 3511 C CB . PRO A 443 ? 0.3876 0.4049 0.4529 0.1228 -0.1110 -0.0537 484 PRO A CB 3512 C CG . PRO A 443 ? 0.3682 0.3938 0.4427 0.1136 -0.1059 -0.0554 484 PRO A CG 3513 C CD . PRO A 443 ? 0.3802 0.4059 0.4551 0.1165 -0.1180 -0.0599 484 PRO A CD 3514 N N . ASP A 444 ? 0.3926 0.4352 0.5171 0.1225 -0.1292 -0.0689 485 ASP A N 3515 C CA . ASP A 444 ? 0.3828 0.4386 0.5367 0.1186 -0.1262 -0.0724 485 ASP A CA 3516 C C . ASP A 444 ? 0.4026 0.4610 0.5708 0.1263 -0.1379 -0.0768 485 ASP A C 3517 O O . ASP A 444 ? 0.4113 0.4653 0.5743 0.1328 -0.1512 -0.0797 485 ASP A O 3518 C CB . ASP A 444 ? 0.3639 0.4304 0.5366 0.1108 -0.1249 -0.0758 485 ASP A CB 3519 C CG . ASP A 444 ? 0.3761 0.4414 0.5377 0.1027 -0.1136 -0.0719 485 ASP A CG 3520 O OD1 . ASP A 444 ? 0.4168 0.4736 0.5568 0.1027 -0.1069 -0.0668 485 ASP A OD1 3521 O OD2 . ASP A 444 ? 0.3597 0.4329 0.5358 0.0963 -0.1118 -0.0740 485 ASP A OD2 3522 N N . GLU A 445 ? 0.4103 0.4761 0.5969 0.1258 -0.1332 -0.0777 486 GLU A N 3523 C CA . GLU A 445 ? 0.4404 0.5120 0.6479 0.1319 -0.1434 -0.0827 486 GLU A CA 3524 C C . GLU A 445 ? 0.4264 0.5076 0.6560 0.1300 -0.1525 -0.0889 486 GLU A C 3525 O O . GLU A 445 ? 0.4198 0.5098 0.6635 0.1215 -0.1455 -0.0898 486 GLU A O 3526 C CB . GLU A 445 ? 0.4440 0.5244 0.6715 0.1298 -0.1343 -0.0830 486 GLU A CB 3527 C CG . GLU A 445 ? 0.5266 0.6021 0.7399 0.1264 -0.1201 -0.0776 486 GLU A CG 3528 C CD . GLU A 445 ? 0.6315 0.6925 0.8198 0.1337 -0.1224 -0.0732 486 GLU A CD 3529 O OE1 . GLU A 445 ? 0.6783 0.7349 0.8653 0.1425 -0.1344 -0.0748 486 GLU A OE1 3530 O OE2 . GLU A 445 ? 0.6609 0.7151 0.8317 0.1306 -0.1123 -0.0682 486 GLU A OE2 3531 N N . GLY A 446 ? 0.4464 0.5256 0.6792 0.1380 -0.1683 -0.0932 487 GLY A N 3532 C CA . GLY A 446 ? 0.4411 0.5291 0.6969 0.1368 -0.1787 -0.0998 487 GLY A CA 3533 C C . GLY A 446 ? 0.4518 0.5325 0.6903 0.1366 -0.1856 -0.1006 487 GLY A C 3534 O O . GLY A 446 ? 0.4623 0.5477 0.7162 0.1366 -0.1964 -0.1065 487 GLY A O 3535 N N . PHE A 447 ? 0.4334 0.5027 0.6409 0.1362 -0.1791 -0.0949 488 PHE A N 3536 C CA . PHE A 447 ? 0.4424 0.5037 0.6308 0.1367 -0.1848 -0.0953 488 PHE A CA 3537 C C . PHE A 447 ? 0.4659 0.5112 0.6208 0.1464 -0.1912 -0.0923 488 PHE A C 3538 O O . PHE A 447 ? 0.4797 0.5163 0.6117 0.1464 -0.1906 -0.0902 488 PHE A O 3539 C CB . PHE A 447 ? 0.4176 0.4804 0.6004 0.1266 -0.1708 -0.0913 488 PHE A CB 3540 C CG . PHE A 447 ? 0.4094 0.4861 0.6220 0.1176 -0.1659 -0.0943 488 PHE A CG 3541 C CD1 . PHE A 447 ? 0.4058 0.4857 0.6288 0.1147 -0.1730 -0.0987 488 PHE A CD1 3542 C CD2 . PHE A 447 ? 0.4308 0.5172 0.6618 0.1122 -0.1540 -0.0926 488 PHE A CD2 3543 C CE1 . PHE A 447 ? 0.4201 0.5125 0.6716 0.1060 -0.1677 -0.1008 488 PHE A CE1 3544 C CE2 . PHE A 447 ? 0.4017 0.5007 0.6598 0.1040 -0.1483 -0.0947 488 PHE A CE2 3545 C CZ . PHE A 447 ? 0.4293 0.5313 0.6981 0.1007 -0.1549 -0.0985 488 PHE A CZ 3546 N N . GLU A 448 ? 0.4913 0.5322 0.6425 0.1548 -0.1968 -0.0919 489 GLU A N 3547 C CA . GLU A 448 ? 0.5318 0.5567 0.6504 0.1646 -0.2026 -0.0884 489 GLU A CA 3548 C C . GLU A 448 ? 0.5483 0.5673 0.6567 0.1703 -0.2177 -0.0934 489 GLU A C 3549 O O . GLU A 448 ? 0.5635 0.5900 0.6935 0.1712 -0.2297 -0.1009 489 GLU A O 3550 C CB . GLU A 448 ? 0.5463 0.5666 0.6626 0.1733 -0.2064 -0.0868 489 GLU A CB 3551 C CG . GLU A 448 ? 0.6050 0.6377 0.7541 0.1735 -0.2108 -0.0917 489 GLU A CG 3552 C CD . GLU A 448 ? 0.5718 0.6178 0.7451 0.1630 -0.1961 -0.0909 489 GLU A CD 3553 O OE1 . GLU A 448 ? 0.5740 0.6180 0.7413 0.1609 -0.1837 -0.0855 489 GLU A OE1 3554 O OE2 . GLU A 448 ? 0.5792 0.6378 0.7790 0.1574 -0.1978 -0.0962 489 GLU A OE2 3555 N N . GLY A 449 ? 0.5593 0.5650 0.6354 0.1739 -0.2168 -0.0895 490 GLY A N 3556 C CA . GLY A 449 ? 0.5691 0.5678 0.6316 0.1794 -0.2300 -0.0941 490 GLY A CA 3557 C C . GLY A 449 ? 0.5548 0.5602 0.6281 0.1709 -0.2285 -0.0978 490 GLY A C 3558 O O . GLY A 449 ? 0.5836 0.5836 0.6474 0.1748 -0.2394 -0.1024 490 GLY A O 3559 N N . LYS A 450 ? 0.5101 0.5269 0.6034 0.1595 -0.2155 -0.0961 491 LYS A N 3560 C CA . LYS A 450 ? 0.4940 0.5170 0.5982 0.1507 -0.2124 -0.0986 491 LYS A CA 3561 C C . LYS A 450 ? 0.4669 0.4847 0.5503 0.1453 -0.1975 -0.0915 491 LYS A C 3562 O O . LYS A 450 ? 0.4704 0.4835 0.5396 0.1459 -0.1874 -0.0849 491 LYS A O 3563 C CB . LYS A 450 ? 0.4756 0.5152 0.6174 0.1416 -0.2080 -0.1016 491 LYS A CB 3564 C CG . LYS A 450 ? 0.5116 0.5588 0.6800 0.1459 -0.2219 -0.1088 491 LYS A CG 3565 C CD . LYS A 450 ? 0.5635 0.6071 0.7317 0.1505 -0.2391 -0.1164 491 LYS A CD 3566 C CE . LYS A 450 ? 0.6134 0.6652 0.8105 0.1545 -0.2540 -0.1243 491 LYS A CE 3567 N NZ . LYS A 450 ? 0.6313 0.6997 0.8657 0.1454 -0.2455 -0.1249 491 LYS A NZ 3568 N N . SER A 451 ? 0.4594 0.4777 0.5419 0.1402 -0.1967 -0.0932 492 SER A N 3569 C CA . SER A 451 ? 0.4296 0.4436 0.4942 0.1349 -0.1833 -0.0870 492 SER A CA 3570 C C . SER A 451 ? 0.4076 0.4317 0.4886 0.1244 -0.1680 -0.0831 492 SER A C 3571 O O . SER A 451 ? 0.3875 0.4231 0.4961 0.1194 -0.1674 -0.0860 492 SER A O 3572 C CB . SER A 451 ? 0.4471 0.4585 0.5064 0.1330 -0.1876 -0.0904 492 SER A CB 3573 O OG . SER A 451 ? 0.4435 0.4668 0.5307 0.1238 -0.1858 -0.0937 492 SER A OG 3574 N N . LEU A 452 ? 0.3834 0.4029 0.4471 0.1212 -0.1555 -0.0765 493 LEU A N 3575 C CA . LEU A 452 ? 0.3677 0.3953 0.4433 0.1114 -0.1413 -0.0729 493 LEU A CA 3576 C C . LEU A 452 ? 0.3604 0.3963 0.4541 0.1034 -0.1409 -0.0763 493 LEU A C 3577 O O . LEU A 452 ? 0.3333 0.3793 0.4478 0.0963 -0.1338 -0.0763 493 LEU A O 3578 C CB . LEU A 452 ? 0.3576 0.3775 0.4097 0.1100 -0.1300 -0.0659 493 LEU A CB 3579 C CG . LEU A 452 ? 0.3578 0.3834 0.4159 0.1007 -0.1154 -0.0618 493 LEU A CG 3580 C CD1 . LEU A 452 ? 0.3465 0.3803 0.4236 0.0986 -0.1110 -0.0619 493 LEU A CD1 3581 C CD2 . LEU A 452 ? 0.3662 0.3829 0.4006 0.1011 -0.1069 -0.0555 493 LEU A CD2 3582 N N . TYR A 453 ? 0.3662 0.3974 0.4517 0.1049 -0.1482 -0.0792 494 TYR A N 3583 C CA . TYR A 453 ? 0.3757 0.4140 0.4795 0.0977 -0.1486 -0.0825 494 TYR A CA 3584 C C . TYR A 453 ? 0.3764 0.4259 0.5121 0.0956 -0.1542 -0.0877 494 TYR A C 3585 O O . TYR A 453 ? 0.3674 0.4262 0.5239 0.0872 -0.1478 -0.0878 494 TYR A O 3586 C CB . TYR A 453 ? 0.3904 0.4212 0.4819 0.1010 -0.1580 -0.0861 494 TYR A CB 3587 C CG . TYR A 453 ? 0.3662 0.4031 0.4759 0.0935 -0.1585 -0.0893 494 TYR A CG 3588 C CD1 . TYR A 453 ? 0.3764 0.4128 0.4800 0.0868 -0.1485 -0.0854 494 TYR A CD1 3589 C CD2 . TYR A 453 ? 0.3893 0.4320 0.5227 0.0933 -0.1697 -0.0963 494 TYR A CD2 3590 C CE1 . TYR A 453 ? 0.3856 0.4267 0.5054 0.0801 -0.1488 -0.0879 494 TYR A CE1 3591 C CE2 . TYR A 453 ? 0.3950 0.4426 0.5460 0.0862 -0.1700 -0.0989 494 TYR A CE2 3592 C CZ . TYR A 453 ? 0.3833 0.4297 0.5267 0.0798 -0.1596 -0.0945 494 TYR A CZ 3593 O OH . TYR A 453 ? 0.4004 0.4508 0.5606 0.0730 -0.1595 -0.0965 494 TYR A OH 3594 N N . GLU A 454 ? 0.3846 0.4329 0.5238 0.1033 -0.1662 -0.0919 495 GLU A N 3595 C CA . GLU A 454 ? 0.3968 0.4560 0.5679 0.1021 -0.1728 -0.0974 495 GLU A CA 3596 C C . GLU A 454 ? 0.3845 0.4540 0.5742 0.0965 -0.1607 -0.0943 495 GLU A C 3597 O O . GLU A 454 ? 0.3745 0.4548 0.5907 0.0894 -0.1568 -0.0959 495 GLU A O 3598 C CB . GLU A 454 ? 0.4219 0.4774 0.5926 0.1124 -0.1890 -0.1028 495 GLU A CB 3599 C CG . GLU A 454 ? 0.4604 0.5280 0.6669 0.1106 -0.1962 -0.1089 495 GLU A CG 3600 C CD . GLU A 454 ? 0.5188 0.5831 0.7271 0.1206 -0.2145 -0.1154 495 GLU A CD 3601 O OE1 . GLU A 454 ? 0.5454 0.5986 0.7316 0.1272 -0.2248 -0.1177 495 GLU A OE1 3602 O OE2 . GLU A 454 ? 0.5537 0.6265 0.7859 0.1220 -0.2188 -0.1185 495 GLU A OE2 3603 N N . SER A 455 ? 0.3790 0.4446 0.5542 0.0995 -0.1540 -0.0896 496 SER A N 3604 C CA . SER A 455 ? 0.3738 0.4481 0.5643 0.0950 -0.1425 -0.0869 496 SER A CA 3605 C C . SER A 455 ? 0.3643 0.4434 0.5584 0.0851 -0.1281 -0.0830 496 SER A C 3606 O O . SER A 455 ? 0.3646 0.4541 0.5815 0.0793 -0.1213 -0.0834 496 SER A O 3607 C CB . SER A 455 ? 0.3793 0.4477 0.5544 0.1008 -0.1395 -0.0832 496 SER A CB 3608 O OG . SER A 455 ? 0.3683 0.4265 0.5150 0.1012 -0.1328 -0.0776 496 SER A OG 3609 N N . TRP A 456 ? 0.3462 0.4173 0.5173 0.0834 -0.1236 -0.0793 497 TRP A N 3610 C CA . TRP A 456 ? 0.3427 0.4168 0.5143 0.0747 -0.1112 -0.0755 497 TRP A CA 3611 C C . TRP A 456 ? 0.3412 0.4236 0.5360 0.0684 -0.1123 -0.0787 497 TRP A C 3612 O O . TRP A 456 ? 0.3204 0.4106 0.5299 0.0615 -0.1021 -0.0768 497 TRP A O 3613 C CB . TRP A 456 ? 0.3255 0.3891 0.4686 0.0754 -0.1085 -0.0716 497 TRP A CB 3614 C CG . TRP A 456 ? 0.3323 0.3971 0.4720 0.0674 -0.0975 -0.0678 497 TRP A CG 3615 C CD1 . TRP A 456 ? 0.3085 0.3806 0.4597 0.0605 -0.0862 -0.0654 497 TRP A CD1 3616 C CD2 . TRP A 456 ? 0.3374 0.3953 0.4596 0.0662 -0.0969 -0.0659 497 TRP A CD2 3617 N NE1 . TRP A 456 ? 0.3082 0.3781 0.4499 0.0551 -0.0793 -0.0622 497 TRP A NE1 3618 C CE2 . TRP A 456 ? 0.3201 0.3817 0.4449 0.0584 -0.0856 -0.0624 497 TRP A CE2 3619 C CE3 . TRP A 456 ? 0.3236 0.3724 0.4278 0.0715 -0.1049 -0.0670 497 TRP A CE3 3620 C CZ2 . TRP A 456 ? 0.3228 0.3796 0.4341 0.0555 -0.0825 -0.0600 497 TRP A CZ2 3621 C CZ3 . TRP A 456 ? 0.3356 0.3799 0.4267 0.0685 -0.1010 -0.0647 497 TRP A CZ3 3622 C CH2 . TRP A 456 ? 0.3211 0.3696 0.4165 0.0605 -0.0901 -0.0612 497 TRP A CH2 3623 N N . THR A 457 ? 0.3528 0.4329 0.5507 0.0710 -0.1245 -0.0833 498 THR A N 3624 C CA . THR A 457 ? 0.3659 0.4527 0.5859 0.0649 -0.1260 -0.0862 498 THR A CA 3625 C C . THR A 457 ? 0.3728 0.4719 0.6254 0.0625 -0.1255 -0.0890 498 THR A C 3626 O O . THR A 457 ? 0.3708 0.4777 0.6430 0.0550 -0.1183 -0.0882 498 THR A O 3627 C CB . THR A 457 ? 0.3810 0.4617 0.5964 0.0687 -0.1402 -0.0913 498 THR A CB 3628 O OG1 . THR A 457 ? 0.3648 0.4350 0.5514 0.0699 -0.1382 -0.0882 498 THR A OG1 3629 C CG2 . THR A 457 ? 0.4024 0.4897 0.6432 0.0621 -0.1423 -0.0946 498 THR A CG2 3630 N N . LYS A 458 ? 0.3812 0.4818 0.6393 0.0690 -0.1324 -0.0919 499 LYS A N 3631 C CA . LYS A 458 ? 0.3949 0.5073 0.6842 0.0675 -0.1317 -0.0945 499 LYS A CA 3632 C C . LYS A 458 ? 0.3820 0.5009 0.6768 0.0618 -0.1147 -0.0895 499 LYS A C 3633 O O . LYS A 458 ? 0.3881 0.5168 0.7077 0.0558 -0.1083 -0.0896 499 LYS A O 3634 C CB . LYS A 458 ? 0.4071 0.5192 0.7000 0.0764 -0.1435 -0.0987 499 LYS A CB 3635 C CG . LYS A 458 ? 0.4519 0.5766 0.7820 0.0755 -0.1478 -0.1037 499 LYS A CG 3636 C CD . LYS A 458 ? 0.5285 0.6553 0.8636 0.0827 -0.1520 -0.1054 499 LYS A CD 3637 C CE . LYS A 458 ? 0.5576 0.6967 0.9308 0.0831 -0.1596 -0.1115 499 LYS A CE 3638 N NZ . LYS A 458 ? 0.5661 0.7149 0.9667 0.0739 -0.1543 -0.1124 499 LYS A NZ 3639 N N . LYS A 459 ? 0.3726 0.4853 0.6438 0.0636 -0.1073 -0.0849 500 LYS A N 3640 C CA . LYS A 459 ? 0.3603 0.4777 0.6338 0.0595 -0.0922 -0.0807 500 LYS A CA 3641 C C . LYS A 459 ? 0.3540 0.4720 0.6230 0.0513 -0.0800 -0.0763 500 LYS A C 3642 O O . LYS A 459 ? 0.3478 0.4718 0.6253 0.0470 -0.0679 -0.0739 500 LYS A O 3643 C CB . LYS A 459 ? 0.3598 0.4699 0.6111 0.0648 -0.0898 -0.0780 500 LYS A CB 3644 C CG . LYS A 459 ? 0.3725 0.4840 0.6326 0.0725 -0.0984 -0.0815 500 LYS A CG 3645 C CD . LYS A 459 ? 0.3576 0.4613 0.5963 0.0773 -0.0950 -0.0782 500 LYS A CD 3646 C CE . LYS A 459 ? 0.3612 0.4665 0.6097 0.0847 -0.1023 -0.0811 500 LYS A CE 3647 N NZ . LYS A 459 ? 0.3762 0.4716 0.6017 0.0902 -0.1008 -0.0777 500 LYS A NZ 3648 N N . SER A 460 ? 0.3499 0.4610 0.6041 0.0497 -0.0831 -0.0753 501 SER A N 3649 C CA . SER A 460 ? 0.3555 0.4652 0.6013 0.0429 -0.0726 -0.0709 501 SER A CA 3650 C C . SER A 460 ? 0.3659 0.4741 0.6157 0.0398 -0.0786 -0.0724 501 SER A C 3651 O O . SER A 460 ? 0.3510 0.4507 0.5804 0.0404 -0.0811 -0.0711 501 SER A O 3652 C CB . SER A 460 ? 0.3408 0.4414 0.5568 0.0445 -0.0677 -0.0666 501 SER A CB 3653 O OG . SER A 460 ? 0.3930 0.4930 0.6015 0.0382 -0.0569 -0.0623 501 SER A OG 3654 N N . PRO A 461 ? 0.3861 0.5023 0.6636 0.0367 -0.0813 -0.0755 502 PRO A N 3655 C CA . PRO A 461 ? 0.4056 0.5201 0.6895 0.0339 -0.0880 -0.0777 502 PRO A CA 3656 C C . PRO A 461 ? 0.4258 0.5377 0.7008 0.0272 -0.0779 -0.0726 502 PRO A C 3657 O O . PRO A 461 ? 0.4042 0.5200 0.6809 0.0228 -0.0648 -0.0682 502 PRO A O 3658 C CB . PRO A 461 ? 0.3989 0.5240 0.7183 0.0316 -0.0912 -0.0817 502 PRO A CB 3659 C CG . PRO A 461 ? 0.4051 0.5385 0.7360 0.0310 -0.0808 -0.0796 502 PRO A CG 3660 C CD . PRO A 461 ? 0.3786 0.5057 0.6837 0.0365 -0.0794 -0.0778 502 PRO A CD 3661 N N . SER A 462 ? 0.4634 0.5682 0.7274 0.0268 -0.0839 -0.0733 503 SER A N 3662 C CA A SER A 462 ? 0.4901 0.5922 0.7470 0.0206 -0.0753 -0.0687 503 SER A CA 3663 C CA B SER A 462 ? 0.4861 0.5882 0.7430 0.0207 -0.0754 -0.0687 503 SER A CA 3664 C C . SER A 462 ? 0.5033 0.6133 0.7885 0.0139 -0.0711 -0.0685 503 SER A C 3665 O O . SER A 462 ? 0.5182 0.6327 0.8261 0.0144 -0.0794 -0.0733 503 SER A O 3666 C CB A SER A 462 ? 0.4962 0.5887 0.7355 0.0223 -0.0830 -0.0698 503 SER A CB 3667 C CB B SER A 462 ? 0.4900 0.5824 0.7292 0.0226 -0.0835 -0.0700 503 SER A CB 3668 O OG A SER A 462 ? 0.5005 0.5900 0.7314 0.0167 -0.0745 -0.0649 503 SER A OG 3669 O OG B SER A 462 ? 0.4843 0.5773 0.7404 0.0226 -0.0945 -0.0753 503 SER A OG 3670 N N . PRO A 463 ? 0.5299 0.6413 0.8142 0.0079 -0.0581 -0.0628 504 PRO A N 3671 C CA . PRO A 463 ? 0.5634 0.6814 0.8742 0.0014 -0.0530 -0.0618 504 PRO A CA 3672 C C . PRO A 463 ? 0.5943 0.7099 0.9180 -0.0005 -0.0631 -0.0653 504 PRO A C 3673 O O . PRO A 463 ? 0.6007 0.7231 0.9534 -0.0031 -0.0656 -0.0679 504 PRO A O 3674 C CB . PRO A 463 ? 0.5571 0.6732 0.8557 -0.0035 -0.0387 -0.0546 504 PRO A CB 3675 C CG . PRO A 463 ? 0.5576 0.6720 0.8354 0.0002 -0.0340 -0.0529 504 PRO A CG 3676 C CD . PRO A 463 ? 0.5255 0.6340 0.7885 0.0069 -0.0466 -0.0572 504 PRO A CD 3677 N N . GLU A 464 ? 0.6282 0.7343 0.9317 0.0009 -0.0688 -0.0656 505 GLU A N 3678 C CA . GLU A 464 ? 0.6528 0.7553 0.9662 -0.0013 -0.0772 -0.0685 505 GLU A CA 3679 C C . GLU A 464 ? 0.6657 0.7663 0.9863 0.0040 -0.0945 -0.0769 505 GLU A C 3680 O O . GLU A 464 ? 0.6802 0.7803 1.0180 0.0015 -0.1016 -0.0804 505 GLU A O 3681 C CB . GLU A 464 ? 0.6560 0.7494 0.9476 -0.0032 -0.0740 -0.0646 505 GLU A CB 3682 C CG . GLU A 464 ? 0.6816 0.7687 0.9410 0.0010 -0.0713 -0.0620 505 GLU A CG 3683 C CD . GLU A 464 ? 0.7026 0.7924 0.9533 -0.0020 -0.0565 -0.0553 505 GLU A CD 3684 O OE1 . GLU A 464 ? 0.6877 0.7722 0.9136 0.0002 -0.0534 -0.0526 505 GLU A OE1 3685 O OE2 . GLU A 464 ? 0.7197 0.8167 0.9885 -0.0063 -0.0481 -0.0528 505 GLU A OE2 3686 N N . PHE A 465 ? 0.6680 0.7670 0.9757 0.0114 -0.1016 -0.0802 506 PHE A N 3687 C CA . PHE A 465 ? 0.6746 0.7688 0.9806 0.0176 -0.1184 -0.0877 506 PHE A CA 3688 C C . PHE A 465 ? 0.6676 0.7672 0.9869 0.0230 -0.1274 -0.0931 506 PHE A C 3689 O O . PHE A 465 ? 0.6677 0.7719 0.9855 0.0248 -0.1215 -0.0909 506 PHE A O 3690 C CB . PHE A 465 ? 0.6893 0.7723 0.9606 0.0233 -0.1220 -0.0873 506 PHE A CB 3691 C CG . PHE A 465 ? 0.7033 0.7803 0.9599 0.0191 -0.1146 -0.0825 506 PHE A CG 3692 C CD1 . PHE A 465 ? 0.6994 0.7741 0.9344 0.0184 -0.1032 -0.0760 506 PHE A CD1 3693 C CD2 . PHE A 465 ? 0.7341 0.8073 0.9986 0.0161 -0.1198 -0.0848 506 PHE A CD2 3694 C CE1 . PHE A 465 ? 0.7167 0.7860 0.9383 0.0150 -0.0970 -0.0717 506 PHE A CE1 3695 C CE2 . PHE A 465 ? 0.7386 0.8059 0.9893 0.0126 -0.1132 -0.0803 506 PHE A CE2 3696 C CZ . PHE A 465 ? 0.7223 0.7879 0.9515 0.0122 -0.1019 -0.0737 506 PHE A CZ 3697 N N . SER A 466 ? 0.6673 0.7658 0.9995 0.0259 -0.1423 -0.1006 507 SER A N 3698 C CA . SER A 466 ? 0.6575 0.7608 1.0028 0.0317 -0.1528 -0.1063 507 SER A CA 3699 C C . SER A 466 ? 0.6471 0.7415 0.9619 0.0414 -0.1608 -0.1081 507 SER A C 3700 O O . SER A 466 ? 0.6589 0.7429 0.9512 0.0450 -0.1669 -0.1096 507 SER A O 3701 C CB . SER A 466 ? 0.6658 0.7722 1.0402 0.0311 -0.1665 -0.1142 507 SER A CB 3702 O OG . SER A 466 ? 0.6794 0.7919 1.0697 0.0361 -0.1756 -0.1194 507 SER A OG 3703 N N . GLY A 467 ? 0.6220 0.7202 0.9360 0.0458 -0.1601 -0.1078 508 GLY A N 3704 C CA . GLY A 467 ? 0.5941 0.6840 0.8807 0.0554 -0.1671 -0.1089 508 GLY A CA 3705 C C . GLY A 467 ? 0.5585 0.6393 0.8105 0.0564 -0.1583 -0.1027 508 GLY A C 3706 O O . GLY A 467 ? 0.5571 0.6285 0.7838 0.0642 -0.1651 -0.1038 508 GLY A O 3707 N N . MET A 468 ? 0.5311 0.6144 0.7827 0.0487 -0.1437 -0.0965 509 MET A N 3708 C CA . MET A 468 ? 0.5089 0.5855 0.7314 0.0483 -0.1332 -0.0899 509 MET A CA 3709 C C . MET A 468 ? 0.4795 0.5612 0.7004 0.0456 -0.1192 -0.0839 509 MET A C 3710 O O . MET A 468 ? 0.4745 0.5654 0.7171 0.0400 -0.1117 -0.0825 509 MET A O 3711 C CB . MET A 468 ? 0.5203 0.5938 0.7385 0.0422 -0.1275 -0.0871 509 MET A CB 3712 C CG . MET A 468 ? 0.5627 0.6310 0.7832 0.0431 -0.1388 -0.0924 509 MET A CG 3713 S SD . MET A 468 ? 0.6055 0.6612 0.7956 0.0537 -0.1508 -0.0960 509 MET A SD 3714 C CE . MET A 468 ? 0.5983 0.6468 0.7623 0.0511 -0.1397 -0.0895 509 MET A CE 3715 N N . PRO A 469 ? 0.4421 0.5173 0.6368 0.0494 -0.1149 -0.0801 510 PRO A N 3716 C CA . PRO A 469 ? 0.4138 0.4928 0.6062 0.0471 -0.1023 -0.0750 510 PRO A CA 3717 C C . PRO A 469 ? 0.3874 0.4671 0.5752 0.0397 -0.0895 -0.0696 510 PRO A C 3718 O O . PRO A 469 ? 0.3864 0.4607 0.5635 0.0378 -0.0896 -0.0684 510 PRO A O 3719 C CB . PRO A 469 ? 0.4148 0.4855 0.5815 0.0543 -0.1041 -0.0735 510 PRO A CB 3720 C CG . PRO A 469 ? 0.4189 0.4802 0.5672 0.0576 -0.1114 -0.0748 510 PRO A CG 3721 C CD . PRO A 469 ? 0.4495 0.5137 0.6172 0.0567 -0.1217 -0.0807 510 PRO A CD 3722 N N . ARG A 470 ? 0.3598 0.4454 0.5543 0.0361 -0.0785 -0.0662 511 ARG A N 3723 C CA . ARG A 470 ? 0.3373 0.4226 0.5240 0.0303 -0.0663 -0.0609 511 ARG A CA 3724 C C . ARG A 470 ? 0.3334 0.4101 0.4920 0.0328 -0.0638 -0.0576 511 ARG A C 3725 O O . ARG A 470 ? 0.3300 0.4038 0.4777 0.0377 -0.0647 -0.0573 511 ARG A O 3726 C CB . ARG A 470 ? 0.3422 0.4353 0.5408 0.0272 -0.0557 -0.0587 511 ARG A CB 3727 C CG . ARG A 470 ? 0.3653 0.4583 0.5563 0.0215 -0.0432 -0.0535 511 ARG A CG 3728 C CD . ARG A 470 ? 0.4535 0.5529 0.6529 0.0204 -0.0338 -0.0521 511 ARG A CD 3729 N NE . ARG A 470 ? 0.5168 0.6252 0.7434 0.0177 -0.0327 -0.0540 511 ARG A NE 3730 C CZ . ARG A 470 ? 0.5856 0.6981 0.8236 0.0117 -0.0247 -0.0514 511 ARG A CZ 3731 N NH1 . ARG A 470 ? 0.5874 0.6954 0.8105 0.0080 -0.0178 -0.0470 511 ARG A NH1 3732 N NH2 . ARG A 470 ? 0.5648 0.6858 0.8296 0.0094 -0.0234 -0.0530 511 ARG A NH2 3733 N N . ILE A 471 ? 0.3107 0.3833 0.4590 0.0294 -0.0608 -0.0550 512 ILE A N 3734 C CA . ILE A 471 ? 0.3064 0.3725 0.4316 0.0299 -0.0555 -0.0510 512 ILE A CA 3735 C C . ILE A 471 ? 0.3052 0.3733 0.4300 0.0233 -0.0449 -0.0467 512 ILE A C 3736 O O . ILE A 471 ? 0.3214 0.3906 0.4543 0.0191 -0.0446 -0.0464 512 ILE A O 3737 C CB . ILE A 471 ? 0.3050 0.3626 0.4138 0.0338 -0.0631 -0.0520 512 ILE A CB 3738 C CG1 . ILE A 471 ? 0.3510 0.4054 0.4563 0.0414 -0.0732 -0.0559 512 ILE A CG1 3739 C CG2 . ILE A 471 ? 0.3195 0.3715 0.4075 0.0333 -0.0564 -0.0475 512 ILE A CG2 3740 C CD1 . ILE A 471 ? 0.3631 0.4088 0.4526 0.0462 -0.0813 -0.0576 512 ILE A CD1 3741 N N . SER A 472 ? 0.3038 0.3717 0.4191 0.0224 -0.0367 -0.0434 513 SER A N 3742 C CA . SER A 472 ? 0.3127 0.3821 0.4268 0.0168 -0.0271 -0.0397 513 SER A CA 3743 C C . SER A 472 ? 0.3047 0.3677 0.4015 0.0159 -0.0261 -0.0370 513 SER A C 3744 O O . SER A 472 ? 0.3028 0.3602 0.3872 0.0199 -0.0312 -0.0376 513 SER A O 3745 C CB . SER A 472 ? 0.3145 0.3870 0.4279 0.0163 -0.0189 -0.0382 513 SER A CB 3746 O OG . SER A 472 ? 0.3516 0.4310 0.4834 0.0166 -0.0187 -0.0405 513 SER A OG 3747 N N . LYS A 473 ? 0.3071 0.3709 0.4030 0.0111 -0.0191 -0.0338 514 LYS A N 3748 C CA . LYS A 473 ? 0.3083 0.3669 0.3895 0.0097 -0.0172 -0.0309 514 LYS A CA 3749 C C . LYS A 473 ? 0.3258 0.3821 0.3933 0.0109 -0.0126 -0.0291 514 LYS A C 3750 O O . LYS A 473 ? 0.3404 0.3998 0.4109 0.0111 -0.0083 -0.0293 514 LYS A O 3751 C CB . LYS A 473 ? 0.3092 0.3696 0.3957 0.0042 -0.0114 -0.0282 514 LYS A CB 3752 C CG . LYS A 473 ? 0.3257 0.3886 0.4288 0.0020 -0.0148 -0.0296 514 LYS A CG 3753 C CD . LYS A 473 ? 0.3568 0.4192 0.4619 -0.0030 -0.0094 -0.0260 514 LYS A CD 3754 C CE . LYS A 473 ? 0.4211 0.4884 0.5333 -0.0062 -0.0001 -0.0235 514 LYS A CE 3755 N NZ . LYS A 473 ? 0.4318 0.5049 0.5660 -0.0076 -0.0007 -0.0254 514 LYS A NZ 3756 N N . LEU A 474 ? 0.3203 0.3715 0.3740 0.0114 -0.0130 -0.0273 515 LEU A N 3757 C CA . LEU A 474 ? 0.3096 0.3586 0.3518 0.0118 -0.0086 -0.0255 515 LEU A CA 3758 C C . LEU A 474 ? 0.3127 0.3623 0.3517 0.0075 -0.0024 -0.0228 515 LEU A C 3759 O O . LEU A 474 ? 0.3192 0.3672 0.3565 0.0052 -0.0025 -0.0212 515 LEU A O 3760 C CB . LEU A 474 ? 0.2985 0.3420 0.3285 0.0148 -0.0120 -0.0248 515 LEU A CB 3761 C CG . LEU A 474 ? 0.3056 0.3466 0.3334 0.0202 -0.0175 -0.0268 515 LEU A CG 3762 C CD1 . LEU A 474 ? 0.3186 0.3539 0.3341 0.0229 -0.0198 -0.0256 515 LEU A CD1 3763 C CD2 . LEU A 474 ? 0.2976 0.3390 0.3244 0.0227 -0.0155 -0.0270 515 LEU A CD2 3764 N N . GLY A 475 ? 0.3159 0.3668 0.3530 0.0070 0.0028 -0.0225 516 GLY A N 3765 C CA . GLY A 475 ? 0.3088 0.3590 0.3395 0.0040 0.0081 -0.0204 516 GLY A CA 3766 C C . GLY A 475 ? 0.3038 0.3506 0.3236 0.0054 0.0087 -0.0201 516 GLY A C 3767 O O . GLY A 475 ? 0.3054 0.3489 0.3191 0.0065 0.0056 -0.0194 516 GLY A O 3768 N N . SER A 476 ? 0.2874 0.3350 0.3055 0.0053 0.0128 -0.0209 517 SER A N 3769 C CA . SER A 476 ? 0.2975 0.3418 0.3076 0.0065 0.0130 -0.0211 517 SER A CA 3770 C C . SER A 476 ? 0.2859 0.3314 0.2997 0.0087 0.0147 -0.0233 517 SER A C 3771 O O . SER A 476 ? 0.2874 0.3360 0.3099 0.0101 0.0141 -0.0246 517 SER A O 3772 C CB . SER A 476 ? 0.3313 0.3740 0.3337 0.0042 0.0159 -0.0201 517 SER A CB 3773 O OG . SER A 476 ? 0.3703 0.4098 0.3667 0.0052 0.0150 -0.0206 517 SER A OG 3774 N N . GLY A 477 ? 0.2647 0.3076 0.2727 0.0089 0.0164 -0.0240 518 GLY A N 3775 C CA . GLY A 477 ? 0.2807 0.3240 0.2917 0.0110 0.0181 -0.0262 518 GLY A CA 3776 C C . GLY A 477 ? 0.2582 0.2982 0.2685 0.0140 0.0150 -0.0260 518 GLY A C 3777 O O . GLY A 477 ? 0.2913 0.3305 0.3038 0.0160 0.0158 -0.0276 518 GLY A O 3778 N N . ASN A 478 ? 0.2351 0.2731 0.2425 0.0146 0.0115 -0.0241 519 ASN A N 3779 C CA . ASN A 478 ? 0.2210 0.2552 0.2264 0.0178 0.0095 -0.0233 519 ASN A CA 3780 C C . ASN A 478 ? 0.2156 0.2467 0.2150 0.0178 0.0078 -0.0208 519 ASN A C 3781 O O . ASN A 478 ? 0.2101 0.2424 0.2077 0.0153 0.0075 -0.0201 519 ASN A O 3782 C CB . ASN A 478 ? 0.2284 0.2636 0.2391 0.0214 0.0067 -0.0242 519 ASN A CB 3783 C CG . ASN A 478 ? 0.2625 0.2944 0.2730 0.0246 0.0070 -0.0244 519 ASN A CG 3784 O OD1 . ASN A 478 ? 0.2689 0.2959 0.2738 0.0260 0.0069 -0.0224 519 ASN A OD1 3785 N ND2 . ASN A 478 ? 0.2508 0.2852 0.2678 0.0256 0.0082 -0.0267 519 ASN A ND2 3786 N N . ASP A 479 ? 0.2100 0.2370 0.2065 0.0206 0.0071 -0.0194 520 ASP A N 3787 C CA . ASP A 479 ? 0.2185 0.2425 0.2099 0.0204 0.0073 -0.0169 520 ASP A CA 3788 C C . ASP A 479 ? 0.2187 0.2426 0.2070 0.0215 0.0046 -0.0157 520 ASP A C 3789 O O . ASP A 479 ? 0.2381 0.2602 0.2228 0.0212 0.0050 -0.0139 520 ASP A O 3790 C CB . ASP A 479 ? 0.2189 0.2382 0.2084 0.0231 0.0086 -0.0152 520 ASP A CB 3791 C CG . ASP A 479 ? 0.2470 0.2654 0.2393 0.0211 0.0113 -0.0163 520 ASP A CG 3792 O OD1 . ASP A 479 ? 0.2434 0.2626 0.2357 0.0178 0.0123 -0.0168 520 ASP A OD1 3793 O OD2 . ASP A 479 ? 0.2676 0.2843 0.2621 0.0232 0.0119 -0.0170 520 ASP A OD2 3794 N N . PHE A 480 ? 0.2381 0.2641 0.2289 0.0225 0.0017 -0.0171 521 PHE A N 3795 C CA . PHE A 480 ? 0.2321 0.2581 0.2208 0.0229 -0.0013 -0.0167 521 PHE A CA 3796 C C . PHE A 480 ? 0.2403 0.2686 0.2297 0.0187 -0.0003 -0.0165 521 PHE A C 3797 O O . PHE A 480 ? 0.2434 0.2709 0.2306 0.0188 -0.0024 -0.0159 521 PHE A O 3798 C CB . PHE A 480 ? 0.2482 0.2759 0.2413 0.0249 -0.0054 -0.0188 521 PHE A CB 3799 C CG . PHE A 480 ? 0.2268 0.2596 0.2287 0.0219 -0.0043 -0.0207 521 PHE A CG 3800 C CD1 . PHE A 480 ? 0.2625 0.2981 0.2673 0.0179 -0.0032 -0.0207 521 PHE A CD1 3801 C CD2 . PHE A 480 ? 0.2659 0.3002 0.2728 0.0232 -0.0035 -0.0222 521 PHE A CD2 3802 C CE1 . PHE A 480 ? 0.2510 0.2910 0.2634 0.0153 -0.0008 -0.0219 521 PHE A CE1 3803 C CE2 . PHE A 480 ? 0.2876 0.3269 0.3031 0.0207 -0.0014 -0.0239 521 PHE A CE2 3804 C CZ . PHE A 480 ? 0.2730 0.3150 0.2907 0.0167 0.0004 -0.0235 521 PHE A CZ 3805 N N . GLU A 481 ? 0.2188 0.2492 0.2103 0.0154 0.0026 -0.0170 522 GLU A N 3806 C CA . GLU A 481 ? 0.2222 0.2544 0.2136 0.0118 0.0033 -0.0166 522 GLU A CA 3807 C C . GLU A 481 ? 0.2191 0.2491 0.2058 0.0114 0.0024 -0.0148 522 GLU A C 3808 O O . GLU A 481 ? 0.2264 0.2567 0.2130 0.0105 0.0006 -0.0143 522 GLU A O 3809 C CB . GLU A 481 ? 0.2416 0.2751 0.2332 0.0092 0.0067 -0.0174 522 GLU A CB 3810 C CG . GLU A 481 ? 0.2766 0.3114 0.2667 0.0060 0.0076 -0.0167 522 GLU A CG 3811 C CD . GLU A 481 ? 0.3741 0.4084 0.3605 0.0042 0.0103 -0.0175 522 GLU A CD 3812 O OE1 . GLU A 481 ? 0.4297 0.4620 0.4132 0.0043 0.0099 -0.0177 522 GLU A OE1 3813 O OE2 . GLU A 481 ? 0.4029 0.4387 0.3892 0.0028 0.0127 -0.0180 522 GLU A OE2 3814 N N . VAL A 482 ? 0.2136 0.2416 0.1977 0.0121 0.0036 -0.0139 523 VAL A N 3815 C CA . VAL A 482 ? 0.2163 0.2431 0.1977 0.0117 0.0031 -0.0123 523 VAL A CA 3816 C C . VAL A 482 ? 0.2232 0.2483 0.2025 0.0146 0.0009 -0.0115 523 VAL A C 3817 O O . VAL A 482 ? 0.2234 0.2483 0.2014 0.0141 -0.0005 -0.0109 523 VAL A O 3818 C CB . VAL A 482 ? 0.2304 0.2558 0.2117 0.0116 0.0051 -0.0114 523 VAL A CB 3819 C CG1 . VAL A 482 ? 0.2268 0.2495 0.2076 0.0151 0.0064 -0.0104 523 VAL A CG1 3820 C CG2 . VAL A 482 ? 0.2480 0.2734 0.2286 0.0105 0.0045 -0.0102 523 VAL A CG2 3821 N N . PHE A 483 ? 0.2091 0.2326 0.1874 0.0181 0.0003 -0.0117 524 PHE A N 3822 C CA . PHE A 483 ? 0.2137 0.2346 0.1881 0.0217 -0.0021 -0.0114 524 PHE A CA 3823 C C . PHE A 483 ? 0.2220 0.2441 0.1983 0.0210 -0.0057 -0.0130 524 PHE A C 3824 O O . PHE A 483 ? 0.2335 0.2538 0.2070 0.0222 -0.0076 -0.0128 524 PHE A O 3825 C CB . PHE A 483 ? 0.2215 0.2397 0.1930 0.0261 -0.0025 -0.0114 524 PHE A CB 3826 C CG . PHE A 483 ? 0.2462 0.2624 0.2164 0.0269 0.0016 -0.0092 524 PHE A CG 3827 C CD1 . PHE A 483 ? 0.2900 0.3037 0.2565 0.0285 0.0039 -0.0068 524 PHE A CD1 3828 C CD2 . PHE A 483 ? 0.2530 0.2699 0.2266 0.0258 0.0033 -0.0096 524 PHE A CD2 3829 C CE1 . PHE A 483 ? 0.3075 0.3195 0.2749 0.0286 0.0082 -0.0045 524 PHE A CE1 3830 C CE2 . PHE A 483 ? 0.2494 0.2641 0.2232 0.0259 0.0069 -0.0077 524 PHE A CE2 3831 C CZ . PHE A 483 ? 0.2843 0.2966 0.2555 0.0272 0.0094 -0.0050 524 PHE A CZ 3832 N N . PHE A 484 ? 0.2257 0.2505 0.2074 0.0191 -0.0065 -0.0146 525 PHE A N 3833 C CA . PHE A 484 ? 0.2166 0.2426 0.2025 0.0181 -0.0098 -0.0161 525 PHE A CA 3834 C C . PHE A 484 ? 0.2186 0.2462 0.2066 0.0137 -0.0086 -0.0151 525 PHE A C 3835 O O . PHE A 484 ? 0.2265 0.2526 0.2141 0.0135 -0.0109 -0.0150 525 PHE A O 3836 C CB . PHE A 484 ? 0.2168 0.2454 0.2093 0.0181 -0.0107 -0.0181 525 PHE A CB 3837 C CG . PHE A 484 ? 0.2189 0.2485 0.2176 0.0178 -0.0148 -0.0200 525 PHE A CG 3838 C CD1 . PHE A 484 ? 0.2124 0.2388 0.2081 0.0214 -0.0198 -0.0213 525 PHE A CD1 3839 C CD2 . PHE A 484 ? 0.2493 0.2828 0.2568 0.0140 -0.0135 -0.0203 525 PHE A CD2 3840 C CE1 . PHE A 484 ? 0.2570 0.2840 0.2598 0.0210 -0.0244 -0.0237 525 PHE A CE1 3841 C CE2 . PHE A 484 ? 0.2486 0.2831 0.2643 0.0133 -0.0172 -0.0221 525 PHE A CE2 3842 C CZ . PHE A 484 ? 0.2612 0.2923 0.2748 0.0168 -0.0232 -0.0240 525 PHE A CZ 3843 N N . GLN A 485 ? 0.2097 0.2394 0.1990 0.0107 -0.0051 -0.0144 526 GLN A N 3844 C CA . GLN A 485 ? 0.2176 0.2483 0.2079 0.0070 -0.0038 -0.0133 526 GLN A CA 3845 C C . GLN A 485 ? 0.2139 0.2426 0.1989 0.0064 -0.0037 -0.0115 526 GLN A C 3846 O O . GLN A 485 ? 0.2331 0.2611 0.2180 0.0045 -0.0044 -0.0104 526 GLN A O 3847 C CB . GLN A 485 ? 0.2324 0.2656 0.2243 0.0045 0.0002 -0.0133 526 GLN A CB 3848 C CG . GLN A 485 ? 0.2505 0.2865 0.2489 0.0051 0.0010 -0.0151 526 GLN A CG 3849 C CD . GLN A 485 ? 0.2398 0.2774 0.2457 0.0040 -0.0005 -0.0155 526 GLN A CD 3850 O OE1 . GLN A 485 ? 0.2648 0.3009 0.2706 0.0026 -0.0019 -0.0143 526 GLN A OE1 3851 N NE2 . GLN A 485 ? 0.2480 0.2886 0.2616 0.0046 -0.0003 -0.0172 526 GLN A NE2 3852 N N . ARG A 486 ? 0.2075 0.2352 0.1891 0.0080 -0.0029 -0.0112 527 ARG A N 3853 C CA . ARG A 486 ? 0.2102 0.2368 0.1888 0.0076 -0.0032 -0.0098 527 ARG A CA 3854 C C . ARG A 486 ? 0.2202 0.2446 0.1973 0.0106 -0.0051 -0.0095 527 ARG A C 3855 O O . ARG A 486 ? 0.2214 0.2449 0.1978 0.0101 -0.0066 -0.0087 527 ARG A O 3856 C CB . ARG A 486 ? 0.2154 0.2423 0.1931 0.0073 -0.0011 -0.0096 527 ARG A CB 3857 C CG . ARG A 486 ? 0.2018 0.2284 0.1783 0.0061 -0.0020 -0.0085 527 ARG A CG 3858 C CD . ARG A 486 ? 0.2259 0.2528 0.2036 0.0061 -0.0009 -0.0086 527 ARG A CD 3859 N NE . ARG A 486 ? 0.2100 0.2375 0.1877 0.0043 0.0004 -0.0101 527 ARG A NE 3860 C CZ . ARG A 486 ? 0.2153 0.2429 0.1945 0.0035 0.0004 -0.0108 527 ARG A CZ 3861 N NH1 . ARG A 486 ? 0.2290 0.2567 0.2108 0.0038 -0.0006 -0.0099 527 ARG A NH1 3862 N NH2 . ARG A 486 ? 0.2197 0.2472 0.1983 0.0023 0.0012 -0.0126 527 ARG A NH2 3863 N N . LEU A 487 ? 0.2139 0.2372 0.1898 0.0139 -0.0050 -0.0100 528 LEU A N 3864 C CA . LEU A 487 ? 0.2208 0.2415 0.1934 0.0174 -0.0059 -0.0096 528 LEU A CA 3865 C C . LEU A 487 ? 0.2237 0.2424 0.1952 0.0199 -0.0096 -0.0113 528 LEU A C 3866 O O . LEU A 487 ? 0.2481 0.2642 0.2161 0.0229 -0.0108 -0.0113 528 LEU A O 3867 C CB . LEU A 487 ? 0.2024 0.2219 0.1726 0.0204 -0.0032 -0.0087 528 LEU A CB 3868 C CG . LEU A 487 ? 0.2222 0.2433 0.1950 0.0182 0.0000 -0.0073 528 LEU A CG 3869 C CD1 . LEU A 487 ? 0.2685 0.2877 0.2399 0.0211 0.0032 -0.0059 528 LEU A CD1 3870 C CD2 . LEU A 487 ? 0.2685 0.2904 0.2427 0.0167 -0.0002 -0.0064 528 LEU A CD2 3871 N N . GLY A 488 ? 0.2169 0.2366 0.1917 0.0191 -0.0115 -0.0129 529 GLY A N 3872 C CA . GLY A 488 ? 0.2147 0.2326 0.1903 0.0211 -0.0160 -0.0151 529 GLY A CA 3873 C C . GLY A 488 ? 0.2188 0.2335 0.1886 0.0267 -0.0178 -0.0163 529 GLY A C 3874 O O . GLY A 488 ? 0.2302 0.2416 0.1966 0.0299 -0.0214 -0.0179 529 GLY A O 3875 N N . ILE A 489 ? 0.2287 0.2438 0.1968 0.0282 -0.0155 -0.0156 530 ILE A N 3876 C CA . ILE A 489 ? 0.2173 0.2286 0.1786 0.0340 -0.0170 -0.0163 530 ILE A CA 3877 C C . ILE A 489 ? 0.2224 0.2349 0.1884 0.0344 -0.0209 -0.0189 530 ILE A C 3878 O O . ILE A 489 ? 0.2300 0.2462 0.2025 0.0313 -0.0192 -0.0187 530 ILE A O 3879 C CB . ILE A 489 ? 0.2245 0.2347 0.1817 0.0354 -0.0119 -0.0134 530 ILE A CB 3880 C CG1 . ILE A 489 ? 0.2409 0.2503 0.1953 0.0353 -0.0084 -0.0112 530 ILE A CG1 3881 C CG2 . ILE A 489 ? 0.2427 0.2484 0.1922 0.0417 -0.0130 -0.0135 530 ILE A CG2 3882 C CD1 . ILE A 489 ? 0.2579 0.2677 0.2128 0.0346 -0.0028 -0.0082 530 ILE A CD1 3883 N N . ALA A 490 ? 0.2305 0.2400 0.1938 0.0387 -0.0265 -0.0216 531 ALA A N 3884 C CA . ALA A 490 ? 0.2292 0.2400 0.1981 0.0397 -0.0312 -0.0245 531 ALA A CA 3885 C C . ALA A 490 ? 0.2463 0.2582 0.2153 0.0405 -0.0285 -0.0232 531 ALA A C 3886 O O . ALA A 490 ? 0.2445 0.2528 0.2046 0.0443 -0.0260 -0.0211 531 ALA A O 3887 C CB . ALA A 490 ? 0.2454 0.2507 0.2067 0.0462 -0.0379 -0.0275 531 ALA A CB 3888 N N . SER A 491 ? 0.2265 0.2432 0.2059 0.0372 -0.0284 -0.0243 532 SER A N 3889 C CA . SER A 491 ? 0.2354 0.2535 0.2162 0.0376 -0.0255 -0.0232 532 SER A CA 3890 C C . SER A 491 ? 0.2431 0.2642 0.2329 0.0384 -0.0296 -0.0262 532 SER A C 3891 O O . SER A 491 ? 0.2534 0.2775 0.2524 0.0364 -0.0332 -0.0288 532 SER A O 3892 C CB . SER A 491 ? 0.2231 0.2449 0.2081 0.0319 -0.0191 -0.0211 532 SER A CB 3893 O OG . SER A 491 ? 0.2408 0.2604 0.2189 0.0312 -0.0155 -0.0185 532 SER A OG 3894 N N . GLY A 492 ? 0.2460 0.2662 0.2345 0.0411 -0.0287 -0.0257 533 GLY A N 3895 C CA . GLY A 492 ? 0.2478 0.2710 0.2456 0.0425 -0.0325 -0.0285 533 GLY A CA 3896 C C . GLY A 492 ? 0.2427 0.2665 0.2414 0.0432 -0.0287 -0.0271 533 GLY A C 3897 O O . GLY A 492 ? 0.2526 0.2727 0.2430 0.0440 -0.0244 -0.0242 533 GLY A O 3898 N N . ARG A 493 ? 0.2471 0.2752 0.2568 0.0431 -0.0306 -0.0296 534 ARG A N 3899 C CA . ARG A 493 ? 0.2613 0.2898 0.2733 0.0445 -0.0281 -0.0291 534 ARG A CA 3900 C C . ARG A 493 ? 0.2688 0.3001 0.2907 0.0478 -0.0340 -0.0325 534 ARG A C 3901 O O . ARG A 493 ? 0.2605 0.2959 0.2923 0.0465 -0.0382 -0.0354 534 ARG A O 3902 C CB . ARG A 493 ? 0.2524 0.2852 0.2701 0.0390 -0.0208 -0.0282 534 ARG A CB 3903 C CG . ARG A 493 ? 0.2872 0.3271 0.3184 0.0350 -0.0203 -0.0305 534 ARG A CG 3904 C CD . ARG A 493 ? 0.3272 0.3703 0.3608 0.0298 -0.0128 -0.0294 534 ARG A CD 3905 N NE . ARG A 493 ? 0.3642 0.4062 0.3963 0.0310 -0.0091 -0.0291 534 ARG A NE 3906 C CZ . ARG A 493 ? 0.3580 0.4027 0.3932 0.0279 -0.0034 -0.0293 534 ARG A CZ 3907 N NH1 . ARG A 493 ? 0.3089 0.3515 0.3420 0.0294 -0.0008 -0.0293 534 ARG A NH1 3908 N NH2 . ARG A 493 ? 0.3646 0.4134 0.4040 0.0235 -0.0003 -0.0294 534 ARG A NH2 3909 N N . ALA A 494 ? 0.2595 0.2883 0.2795 0.0519 -0.0345 -0.0321 535 ALA A N 3910 C CA . ALA A 494 ? 0.2648 0.2964 0.2950 0.0555 -0.0403 -0.0354 535 ALA A CA 3911 C C . ALA A 494 ? 0.2742 0.3058 0.3069 0.0570 -0.0369 -0.0346 535 ALA A C 3912 O O . ALA A 494 ? 0.2785 0.3043 0.3004 0.0584 -0.0331 -0.0314 535 ALA A O 3913 C CB . ALA A 494 ? 0.2769 0.3026 0.2985 0.0625 -0.0492 -0.0365 535 ALA A CB 3914 N N . ARG A 495 ? 0.2628 0.3005 0.3103 0.0569 -0.0380 -0.0375 536 ARG A N 3915 C CA . ARG A 495 ? 0.2599 0.2974 0.3106 0.0590 -0.0353 -0.0373 536 ARG A CA 3916 C C . ARG A 495 ? 0.2670 0.3108 0.3342 0.0612 -0.0401 -0.0413 536 ARG A C 3917 O O . ARG A 495 ? 0.2706 0.3201 0.3487 0.0593 -0.0436 -0.0439 536 ARG A O 3918 C CB . ARG A 495 ? 0.2729 0.3128 0.3255 0.0536 -0.0258 -0.0361 536 ARG A CB 3919 C CG . ARG A 495 ? 0.2734 0.3218 0.3382 0.0478 -0.0220 -0.0379 536 ARG A CG 3920 C CD . ARG A 495 ? 0.3286 0.3787 0.3946 0.0443 -0.0136 -0.0374 536 ARG A CD 3921 N NE . ARG A 495 ? 0.3410 0.3846 0.3926 0.0431 -0.0100 -0.0344 536 ARG A NE 3922 C CZ . ARG A 495 ? 0.3517 0.3957 0.4002 0.0386 -0.0037 -0.0336 536 ARG A CZ 3923 N NH1 . ARG A 495 ? 0.3468 0.3850 0.3842 0.0380 -0.0018 -0.0311 536 ARG A NH1 3924 N NH2 . ARG A 495 ? 0.3530 0.4031 0.4096 0.0351 0.0008 -0.0352 536 ARG A NH2 3925 N N . TYR A 496 ? 0.2702 0.3133 0.3408 0.0647 -0.0399 -0.0416 537 TYR A N 3926 C CA . TYR A 496 ? 0.2781 0.3284 0.3669 0.0664 -0.0432 -0.0455 537 TYR A CA 3927 C C . TYR A 496 ? 0.2852 0.3434 0.3866 0.0607 -0.0345 -0.0465 537 TYR A C 3928 O O . TYR A 496 ? 0.2912 0.3470 0.3852 0.0579 -0.0269 -0.0443 537 TYR A O 3929 C CB . TYR A 496 ? 0.2856 0.3319 0.3741 0.0738 -0.0484 -0.0460 537 TYR A CB 3930 C CG . TYR A 496 ? 0.3002 0.3476 0.3949 0.0790 -0.0597 -0.0493 537 TYR A CG 3931 C CD1 . TYR A 496 ? 0.2945 0.3358 0.3762 0.0819 -0.0663 -0.0486 537 TYR A CD1 3932 C CD2 . TYR A 496 ? 0.2846 0.3392 0.3987 0.0813 -0.0639 -0.0533 537 TYR A CD2 3933 C CE1 . TYR A 496 ? 0.3223 0.3638 0.4086 0.0870 -0.0778 -0.0522 537 TYR A CE1 3934 C CE2 . TYR A 496 ? 0.3067 0.3623 0.4273 0.0862 -0.0756 -0.0568 537 TYR A CE2 3935 C CZ . TYR A 496 ? 0.3320 0.3807 0.4382 0.0889 -0.0826 -0.0563 537 TYR A CZ 3936 O OH . TYR A 496 ? 0.3433 0.3923 0.4549 0.0940 -0.0948 -0.0604 537 TYR A OH 3937 N N . THR A 497 ? 0.2860 0.3530 0.4059 0.0591 -0.0357 -0.0497 538 THR A N 3938 C CA . THR A 497 ? 0.2915 0.3660 0.4228 0.0537 -0.0267 -0.0502 538 THR A CA 3939 C C . THR A 497 ? 0.3103 0.3932 0.4629 0.0554 -0.0269 -0.0537 538 THR A C 3940 O O . THR A 497 ? 0.2907 0.3743 0.4508 0.0605 -0.0352 -0.0561 538 THR A O 3941 C CB . THR A 497 ? 0.2938 0.3716 0.4269 0.0476 -0.0245 -0.0495 538 THR A CB 3942 O OG1 . THR A 497 ? 0.3188 0.4015 0.4572 0.0427 -0.0145 -0.0489 538 THR A OG1 3943 C CG2 . THR A 497 ? 0.2926 0.3759 0.4414 0.0480 -0.0318 -0.0524 538 THR A CG2 3944 N N . LYS A 498 ? 0.3231 0.4122 0.4847 0.0514 -0.0177 -0.0540 539 LYS A N 3945 C CA . LYS A 498 ? 0.3677 0.4660 0.5511 0.0521 -0.0152 -0.0570 539 LYS A CA 3946 C C . LYS A 498 ? 0.3877 0.4944 0.5900 0.0492 -0.0176 -0.0587 539 LYS A C 3947 O O . LYS A 498 ? 0.3797 0.4846 0.5778 0.0469 -0.0218 -0.0578 539 LYS A O 3948 C CB . LYS A 498 ? 0.3624 0.4629 0.5452 0.0491 -0.0032 -0.0564 539 LYS A CB 3949 C CG . LYS A 498 ? 0.4146 0.5154 0.5900 0.0426 0.0043 -0.0537 539 LYS A CG 3950 C CD . LYS A 498 ? 0.4934 0.5920 0.6589 0.0410 0.0144 -0.0528 539 LYS A CD 3951 C CE . LYS A 498 ? 0.5011 0.6008 0.6616 0.0351 0.0219 -0.0505 539 LYS A CE 3952 N NZ . LYS A 498 ? 0.5156 0.6096 0.6589 0.0340 0.0284 -0.0494 539 LYS A NZ 3953 N N . ASN A 499 ? 0.4255 0.5415 0.6498 0.0493 -0.0146 -0.0612 540 ASN A N 3954 C CA . ASN A 499 ? 0.4659 0.5908 0.7113 0.0455 -0.0143 -0.0624 540 ASN A CA 3955 C C . ASN A 499 ? 0.4994 0.6276 0.7452 0.0388 -0.0017 -0.0596 540 ASN A C 3956 O O . ASN A 499 ? 0.5115 0.6414 0.7616 0.0342 -0.0015 -0.0583 540 ASN A O 3957 C CB . ASN A 499 ? 0.4671 0.6007 0.7378 0.0491 -0.0178 -0.0664 540 ASN A CB 3958 C CG . ASN A 499 ? 0.4628 0.6048 0.7576 0.0464 -0.0219 -0.0685 540 ASN A CG 3959 O OD1 . ASN A 499 ? 0.4439 0.5865 0.7390 0.0409 -0.0191 -0.0666 540 ASN A OD1 3960 N ND2 . ASN A 499 ? 0.4784 0.6269 0.7948 0.0504 -0.0288 -0.0725 540 ASN A ND2 3961 N N . TRP A 500 ? 0.5310 0.6585 0.7697 0.0387 0.0083 -0.0585 541 TRP A N 3962 C CA . TRP A 500 ? 0.5520 0.6828 0.7909 0.0339 0.0215 -0.0562 541 TRP A CA 3963 C C . TRP A 500 ? 0.5628 0.6906 0.7909 0.0279 0.0254 -0.0524 541 TRP A C 3964 O O . TRP A 500 ? 0.5555 0.6766 0.7628 0.0266 0.0297 -0.0501 541 TRP A O 3965 C CB . TRP A 500 ? 0.5612 0.6875 0.7857 0.0363 0.0280 -0.0562 541 TRP A CB 3966 C CG . TRP A 500 ? 0.5956 0.7271 0.8264 0.0351 0.0407 -0.0562 541 TRP A CG 3967 C CD1 . TRP A 500 ? 0.6117 0.7504 0.8561 0.0312 0.0489 -0.0548 541 TRP A CD1 3968 C CD2 . TRP A 500 ? 0.6230 0.7519 0.8455 0.0380 0.0472 -0.0576 541 TRP A CD2 3969 N NE1 . TRP A 500 ? 0.6312 0.7720 0.8752 0.0319 0.0605 -0.0551 541 TRP A NE1 3970 C CE2 . TRP A 500 ? 0.6327 0.7676 0.8633 0.0361 0.0593 -0.0571 541 TRP A CE2 3971 C CE3 . TRP A 500 ? 0.6346 0.7563 0.8437 0.0421 0.0440 -0.0590 541 TRP A CE3 3972 C CZ2 . TRP A 500 ? 0.6412 0.7751 0.8661 0.0387 0.0679 -0.0588 541 TRP A CZ2 3973 C CZ3 . TRP A 500 ? 0.6336 0.7543 0.8383 0.0442 0.0522 -0.0607 541 TRP A CZ3 3974 C CH2 . TRP A 500 ? 0.6386 0.7652 0.8506 0.0427 0.0638 -0.0608 541 TRP A CH2 3975 N N . GLU A 501 ? 0.5687 0.7015 0.8120 0.0244 0.0241 -0.0519 542 GLU A N 3976 C CA . GLU A 501 ? 0.5765 0.7060 0.8111 0.0191 0.0260 -0.0483 542 GLU A CA 3977 C C . GLU A 501 ? 0.5827 0.7098 0.8037 0.0157 0.0381 -0.0446 542 GLU A C 3978 O O . GLU A 501 ? 0.5901 0.7102 0.7923 0.0136 0.0378 -0.0420 542 GLU A O 3979 C CB . GLU A 501 ? 0.5784 0.7143 0.8355 0.0159 0.0234 -0.0486 542 GLU A CB 3980 N N . THR A 502 ? 0.5844 0.7170 0.8145 0.0155 0.0487 -0.0444 543 THR A N 3981 C CA . THR A 502 ? 0.5862 0.7161 0.8021 0.0131 0.0604 -0.0411 543 THR A CA 3982 C C . THR A 502 ? 0.5800 0.7020 0.7718 0.0158 0.0607 -0.0417 543 THR A C 3983 O O . THR A 502 ? 0.5795 0.6970 0.7549 0.0142 0.0677 -0.0394 543 THR A O 3984 C CB . THR A 502 ? 0.5923 0.7301 0.8240 0.0124 0.0728 -0.0405 543 THR A CB 3985 O OG1 . THR A 502 ? 0.6108 0.7531 0.8531 0.0171 0.0730 -0.0446 543 THR A OG1 3986 C CG2 . THR A 502 ? 0.5951 0.7400 0.8500 0.0083 0.0743 -0.0387 543 THR A CG2 3987 N N . ASN A 503 ? 0.5658 0.6857 0.7557 0.0200 0.0529 -0.0448 544 ASN A N 3988 C CA . ASN A 503 ? 0.5556 0.6673 0.7245 0.0224 0.0516 -0.0454 544 ASN A CA 3989 C C . ASN A 503 ? 0.5414 0.6457 0.6953 0.0219 0.0428 -0.0441 544 ASN A C 3990 O O . ASN A 503 ? 0.5371 0.6349 0.6761 0.0239 0.0406 -0.0445 544 ASN A O 3991 C CB . ASN A 503 ? 0.5581 0.6709 0.7325 0.0277 0.0499 -0.0491 544 ASN A CB 3992 C CG . ASN A 503 ? 0.5827 0.6959 0.7535 0.0291 0.0600 -0.0503 544 ASN A CG 3993 O OD1 . ASN A 503 ? 0.6230 0.7402 0.7977 0.0269 0.0694 -0.0491 544 ASN A OD1 3994 N ND2 . ASN A 503 ? 0.5708 0.6794 0.7338 0.0330 0.0584 -0.0528 544 ASN A ND2 3995 N N . LYS A 504 ? 0.5234 0.6286 0.6819 0.0192 0.0381 -0.0425 545 LYS A N 3996 C CA . LYS A 504 ? 0.5125 0.6112 0.6589 0.0194 0.0294 -0.0416 545 LYS A CA 3997 C C . LYS A 504 ? 0.5042 0.5950 0.6282 0.0186 0.0313 -0.0397 545 LYS A C 3998 O O . LYS A 504 ? 0.5094 0.5944 0.6226 0.0208 0.0254 -0.0399 545 LYS A O 3999 C CB . LYS A 504 ? 0.5176 0.6179 0.6712 0.0162 0.0254 -0.0402 545 LYS A CB 4000 C CG . LYS A 504 ? 0.5418 0.6353 0.6821 0.0168 0.0169 -0.0395 545 LYS A CG 4001 C CD . LYS A 504 ? 0.5906 0.6848 0.7370 0.0140 0.0126 -0.0386 545 LYS A CD 4002 C CE . LYS A 504 ? 0.6122 0.6988 0.7423 0.0151 0.0057 -0.0377 545 LYS A CE 4003 N NZ . LYS A 504 ? 0.6234 0.7095 0.7565 0.0119 0.0028 -0.0366 545 LYS A NZ 4004 N N . PHE A 505 ? 0.4858 0.5762 0.6031 0.0155 0.0392 -0.0377 546 PHE A N 4005 C CA . PHE A 505 ? 0.4791 0.5624 0.5763 0.0145 0.0406 -0.0362 546 PHE A CA 4006 C C . PHE A 505 ? 0.4766 0.5580 0.5666 0.0166 0.0462 -0.0381 546 PHE A C 4007 O O . PHE A 505 ? 0.4780 0.5543 0.5529 0.0156 0.0485 -0.0373 546 PHE A O 4008 C CB . PHE A 505 ? 0.4741 0.5564 0.5654 0.0102 0.0446 -0.0328 546 PHE A CB 4009 C CG . PHE A 505 ? 0.4824 0.5654 0.5792 0.0080 0.0391 -0.0311 546 PHE A CG 4010 C CD1 . PHE A 505 ? 0.4998 0.5874 0.6089 0.0050 0.0426 -0.0294 546 PHE A CD1 4011 C CD2 . PHE A 505 ? 0.4773 0.5558 0.5671 0.0091 0.0309 -0.0311 546 PHE A CD2 4012 C CE1 . PHE A 505 ? 0.5036 0.5911 0.6183 0.0030 0.0370 -0.0282 546 PHE A CE1 4013 C CE2 . PHE A 505 ? 0.4843 0.5627 0.5782 0.0075 0.0256 -0.0300 546 PHE A CE2 4014 C CZ . PHE A 505 ? 0.4973 0.5801 0.6038 0.0044 0.0282 -0.0288 546 PHE A CZ 4015 N N . SER A 506 ? 0.4589 0.5444 0.5602 0.0196 0.0479 -0.0408 547 SER A N 4016 C CA . SER A 506 ? 0.4512 0.5349 0.5469 0.0218 0.0534 -0.0431 547 SER A CA 4017 C C . SER A 506 ? 0.4511 0.5295 0.5408 0.0253 0.0483 -0.0453 547 SER A C 4018 O O . SER A 506 ? 0.4549 0.5295 0.5362 0.0267 0.0517 -0.0472 547 SER A O 4019 C CB . SER A 506 ? 0.4513 0.5422 0.5616 0.0231 0.0607 -0.0448 547 SER A CB 4020 O OG A SER A 506 ? 0.3980 0.4931 0.5131 0.0196 0.0664 -0.0420 547 SER A OG 4021 O OG B SER A 506 ? 0.4770 0.5717 0.6017 0.0267 0.0570 -0.0474 547 SER A OG 4022 N N . GLY A 507 ? 0.4332 0.5102 0.5259 0.0268 0.0403 -0.0449 548 GLY A N 4023 C CA . GLY A 507 ? 0.4263 0.4985 0.5158 0.0306 0.0360 -0.0464 548 GLY A CA 4024 C C . GLY A 507 ? 0.4121 0.4885 0.5157 0.0348 0.0362 -0.0494 548 GLY A C 4025 O O . GLY A 507 ? 0.4497 0.5328 0.5647 0.0347 0.0415 -0.0507 548 GLY A O 4026 N N . TYR A 508 ? 0.3686 0.4408 0.4717 0.0386 0.0304 -0.0500 549 TYR A N 4027 C CA . TYR A 508 ? 0.3317 0.4060 0.4461 0.0434 0.0292 -0.0526 549 TYR A CA 4028 C C . TYR A 508 ? 0.3084 0.3805 0.4190 0.0444 0.0359 -0.0552 549 TYR A C 4029 O O . TYR A 508 ? 0.3034 0.3712 0.4014 0.0419 0.0395 -0.0547 549 TYR A O 4030 C CB . TYR A 508 ? 0.3303 0.3987 0.4412 0.0472 0.0209 -0.0516 549 TYR A CB 4031 C CG . TYR A 508 ? 0.2928 0.3522 0.3871 0.0461 0.0199 -0.0493 549 TYR A CG 4032 C CD1 . TYR A 508 ? 0.2808 0.3336 0.3690 0.0481 0.0214 -0.0502 549 TYR A CD1 4033 C CD2 . TYR A 508 ? 0.2929 0.3501 0.3783 0.0430 0.0174 -0.0463 549 TYR A CD2 4034 C CE1 . TYR A 508 ? 0.2655 0.3103 0.3403 0.0466 0.0207 -0.0480 549 TYR A CE1 4035 C CE2 . TYR A 508 ? 0.2929 0.3425 0.3646 0.0418 0.0170 -0.0441 549 TYR A CE2 4036 C CZ . TYR A 508 ? 0.2698 0.3135 0.3370 0.0435 0.0186 -0.0449 549 TYR A CZ 4037 O OH . TYR A 508 ? 0.2836 0.3205 0.3397 0.0420 0.0182 -0.0427 549 TYR A OH 4038 N N . PRO A 509 ? 0.2858 0.3609 0.4076 0.0484 0.0376 -0.0582 550 PRO A N 4039 C CA . PRO A 509 ? 0.2727 0.3467 0.3912 0.0490 0.0452 -0.0610 550 PRO A CA 4040 C C . PRO A 509 ? 0.2758 0.3400 0.3791 0.0493 0.0448 -0.0616 550 PRO A C 4041 O O . PRO A 509 ? 0.2807 0.3429 0.3758 0.0479 0.0506 -0.0633 550 PRO A O 4042 C CB . PRO A 509 ? 0.2718 0.3502 0.4058 0.0540 0.0458 -0.0642 550 PRO A CB 4043 C CG . PRO A 509 ? 0.2621 0.3490 0.4116 0.0536 0.0423 -0.0630 550 PRO A CG 4044 C CD . PRO A 509 ? 0.2921 0.3738 0.4318 0.0518 0.0343 -0.0596 550 PRO A CD 4045 N N . LEU A 510 ? 0.2506 0.3083 0.3499 0.0510 0.0382 -0.0601 551 LEU A N 4046 C CA . LEU A 510 ? 0.2571 0.3055 0.3451 0.0514 0.0379 -0.0607 551 LEU A CA 4047 C C . LEU A 510 ? 0.2539 0.2975 0.3287 0.0471 0.0361 -0.0576 551 LEU A C 4048 O O . LEU A 510 ? 0.2696 0.3053 0.3361 0.0469 0.0344 -0.0572 551 LEU A O 4049 C CB . LEU A 510 ? 0.2568 0.2999 0.3483 0.0560 0.0328 -0.0605 551 LEU A CB 4050 C CG . LEU A 510 ? 0.2567 0.3041 0.3610 0.0605 0.0352 -0.0643 551 LEU A CG 4051 C CD1 . LEU A 510 ? 0.2594 0.3011 0.3669 0.0654 0.0297 -0.0636 551 LEU A CD1 4052 C CD2 . LEU A 510 ? 0.2495 0.2952 0.3502 0.0604 0.0421 -0.0685 551 LEU A CD2 4053 N N . TYR A 511 ? 0.2578 0.3064 0.3320 0.0437 0.0362 -0.0554 552 TYR A N 4054 C CA . TYR A 511 ? 0.2537 0.2988 0.3166 0.0397 0.0344 -0.0524 552 TYR A CA 4055 C C . TYR A 511 ? 0.2546 0.2940 0.3066 0.0379 0.0371 -0.0540 552 TYR A C 4056 O O . TYR A 511 ? 0.2702 0.3110 0.3198 0.0373 0.0422 -0.0568 552 TYR A O 4057 C CB . TYR A 511 ? 0.2470 0.2989 0.3123 0.0366 0.0360 -0.0508 552 TYR A CB 4058 C CG . TYR A 511 ? 0.2482 0.2980 0.3031 0.0324 0.0351 -0.0481 552 TYR A CG 4059 C CD1 . TYR A 511 ? 0.2772 0.3226 0.3267 0.0320 0.0299 -0.0453 552 TYR A CD1 4060 C CD2 . TYR A 511 ? 0.2537 0.3060 0.3043 0.0293 0.0399 -0.0482 552 TYR A CD2 4061 C CE1 . TYR A 511 ? 0.2657 0.3098 0.3068 0.0283 0.0293 -0.0429 552 TYR A CE1 4062 C CE2 . TYR A 511 ? 0.2696 0.3202 0.3115 0.0258 0.0387 -0.0455 552 TYR A CE2 4063 C CZ . TYR A 511 ? 0.2676 0.3144 0.3054 0.0253 0.0335 -0.0433 552 TYR A CZ 4064 O OH . TYR A 511 ? 0.2937 0.3391 0.3233 0.0219 0.0326 -0.0409 552 TYR A OH 4065 N N . HIS A 512 ? 0.2581 0.2907 0.3034 0.0372 0.0335 -0.0522 553 HIS A N 4066 C CA . HIS A 512 ? 0.2624 0.2890 0.2982 0.0349 0.0342 -0.0534 553 HIS A CA 4067 C C . HIS A 512 ? 0.2725 0.2956 0.3086 0.0373 0.0369 -0.0583 553 HIS A C 4068 O O . HIS A 512 ? 0.2694 0.2886 0.2982 0.0358 0.0381 -0.0609 553 HIS A O 4069 C CB . HIS A 512 ? 0.2626 0.2919 0.2910 0.0310 0.0361 -0.0529 553 HIS A CB 4070 C CG . HIS A 512 ? 0.2582 0.2881 0.2835 0.0282 0.0328 -0.0485 553 HIS A CG 4071 N ND1 . HIS A 512 ? 0.2514 0.2829 0.2702 0.0249 0.0337 -0.0475 553 HIS A ND1 4072 C CD2 . HIS A 512 ? 0.2568 0.2857 0.2841 0.0287 0.0288 -0.0450 553 HIS A CD2 4073 C CE1 . HIS A 512 ? 0.2577 0.2892 0.2753 0.0233 0.0304 -0.0437 553 HIS A CE1 4074 N NE2 . HIS A 512 ? 0.2389 0.2688 0.2611 0.0256 0.0275 -0.0423 553 HIS A NE2 4075 N N . SER A 513 ? 0.2804 0.3043 0.3251 0.0412 0.0372 -0.0597 554 SER A N 4076 C CA . SER A 513 ? 0.2739 0.2938 0.3200 0.0442 0.0394 -0.0643 554 SER A CA 4077 C C . SER A 513 ? 0.3125 0.3243 0.3604 0.0461 0.0355 -0.0634 554 SER A C 4078 O O . SER A 513 ? 0.2908 0.3011 0.3395 0.0460 0.0319 -0.0589 554 SER A O 4079 C CB . SER A 513 ? 0.2737 0.2998 0.3295 0.0477 0.0428 -0.0667 554 SER A CB 4080 O OG A SER A 513 ? 0.2532 0.2805 0.3186 0.0509 0.0394 -0.0648 554 SER A OG 4081 O OG B SER A 513 ? 0.3091 0.3307 0.3687 0.0517 0.0435 -0.0705 554 SER A OG 4082 N N . VAL A 514 ? 0.2855 0.2915 0.3331 0.0479 0.0366 -0.0675 555 VAL A N 4083 C CA . VAL A 514 ? 0.3001 0.2976 0.3503 0.0498 0.0336 -0.0667 555 VAL A CA 4084 C C . VAL A 514 ? 0.3092 0.3081 0.3680 0.0542 0.0319 -0.0644 555 VAL A C 4085 O O . VAL A 514 ? 0.3400 0.3320 0.4003 0.0560 0.0290 -0.0615 555 VAL A O 4086 C CB . VAL A 514 ? 0.3022 0.2934 0.3516 0.0512 0.0351 -0.0726 555 VAL A CB 4087 C CG1 . VAL A 514 ? 0.3133 0.3077 0.3691 0.0560 0.0384 -0.0770 555 VAL A CG1 4088 C CG2 . VAL A 514 ? 0.3225 0.3040 0.3744 0.0520 0.0321 -0.0712 555 VAL A CG2 4089 N N . TYR A 515 ? 0.2962 0.3035 0.3609 0.0561 0.0336 -0.0654 556 TYR A N 4090 C CA . TYR A 515 ? 0.3047 0.3142 0.3791 0.0609 0.0315 -0.0644 556 TYR A CA 4091 C C . TYR A 515 ? 0.3161 0.3269 0.3902 0.0608 0.0269 -0.0589 556 TYR A C 4092 O O . TYR A 515 ? 0.3303 0.3413 0.4105 0.0650 0.0235 -0.0574 556 TYR A O 4093 C CB . TYR A 515 ? 0.3028 0.3210 0.3864 0.0634 0.0352 -0.0683 556 TYR A CB 4094 C CG . TYR A 515 ? 0.3073 0.3232 0.3896 0.0644 0.0401 -0.0740 556 TYR A CG 4095 C CD1 . TYR A 515 ? 0.3102 0.3178 0.3937 0.0677 0.0392 -0.0765 556 TYR A CD1 4096 C CD2 . TYR A 515 ? 0.3173 0.3383 0.3959 0.0622 0.0455 -0.0769 556 TYR A CD2 4097 C CE1 . TYR A 515 ? 0.3068 0.3112 0.3881 0.0688 0.0432 -0.0824 556 TYR A CE1 4098 C CE2 . TYR A 515 ? 0.3074 0.3253 0.3826 0.0637 0.0499 -0.0825 556 TYR A CE2 4099 C CZ . TYR A 515 ? 0.3214 0.3312 0.3981 0.0670 0.0485 -0.0855 556 TYR A CZ 4100 O OH . TYR A 515 ? 0.3669 0.3728 0.4393 0.0687 0.0522 -0.0916 556 TYR A OH 4101 N N . GLU A 516 ? 0.2953 0.3065 0.3617 0.0564 0.0263 -0.0559 557 GLU A N 4102 C CA . GLU A 516 ? 0.3014 0.3131 0.3658 0.0564 0.0221 -0.0510 557 GLU A CA 4103 C C . GLU A 516 ? 0.3018 0.3036 0.3621 0.0585 0.0192 -0.0472 557 GLU A C 4104 O O . GLU A 516 ? 0.3022 0.2987 0.3557 0.0555 0.0196 -0.0449 557 GLU A O 4105 C CB . GLU A 516 ? 0.3143 0.3292 0.3718 0.0511 0.0229 -0.0493 557 GLU A CB 4106 C CG . GLU A 516 ? 0.3753 0.3972 0.4355 0.0508 0.0208 -0.0476 557 GLU A CG 4107 C CD . GLU A 516 ? 0.2778 0.2999 0.3298 0.0463 0.0205 -0.0448 557 GLU A CD 4108 O OE1 . GLU A 516 ? 0.3579 0.3847 0.4087 0.0428 0.0235 -0.0463 557 GLU A OE1 4109 O OE2 . GLU A 516 ? 0.3565 0.3730 0.4029 0.0466 0.0180 -0.0413 557 GLU A OE2 4110 N N . THR A 517 ? 0.2965 0.2957 0.3616 0.0638 0.0164 -0.0464 558 THR A N 4111 C CA . THR A 517 ? 0.2984 0.2873 0.3601 0.0664 0.0146 -0.0428 558 THR A CA 4112 C C . THR A 517 ? 0.2915 0.2789 0.3517 0.0709 0.0096 -0.0384 558 THR A C 4113 O O . THR A 517 ? 0.2799 0.2745 0.3440 0.0726 0.0068 -0.0394 558 THR A O 4114 C CB . THR A 517 ? 0.3215 0.3058 0.3895 0.0700 0.0156 -0.0459 558 THR A CB 4115 O OG1 . THR A 517 ? 0.3258 0.3164 0.4028 0.0743 0.0142 -0.0488 558 THR A OG1 4116 C CG2 . THR A 517 ? 0.2983 0.2816 0.3663 0.0664 0.0201 -0.0508 558 THR A CG2 4117 N N . TYR A 518 ? 0.3020 0.2794 0.3571 0.0735 0.0085 -0.0340 559 TYR A N 4118 C CA . TYR A 518 ? 0.3152 0.2889 0.3672 0.0792 0.0036 -0.0299 559 TYR A CA 4119 C C . TYR A 518 ? 0.3155 0.2933 0.3769 0.0846 0.0001 -0.0332 559 TYR A C 4120 O O . TYR A 518 ? 0.3178 0.2993 0.3798 0.0879 -0.0049 -0.0326 559 TYR A O 4121 C CB . TYR A 518 ? 0.3212 0.2822 0.3669 0.0814 0.0043 -0.0246 559 TYR A CB 4122 C CG . TYR A 518 ? 0.3225 0.2780 0.3639 0.0886 -0.0006 -0.0204 559 TYR A CG 4123 C CD1 . TYR A 518 ? 0.3427 0.2971 0.3741 0.0901 -0.0033 -0.0160 559 TYR A CD1 4124 C CD2 . TYR A 518 ? 0.3559 0.3070 0.4025 0.0945 -0.0029 -0.0211 559 TYR A CD2 4125 C CE1 . TYR A 518 ? 0.3734 0.3217 0.3987 0.0973 -0.0083 -0.0122 559 TYR A CE1 4126 C CE2 . TYR A 518 ? 0.3863 0.3317 0.4278 0.1017 -0.0082 -0.0171 559 TYR A CE2 4127 C CZ . TYR A 518 ? 0.4022 0.3462 0.4324 0.1031 -0.0109 -0.0128 559 TYR A CZ 4128 O OH . TYR A 518 ? 0.4312 0.3687 0.4540 0.1109 -0.0166 -0.0090 559 TYR A OH 4129 N N . GLU A 519 ? 0.3217 0.2992 0.3911 0.0854 0.0026 -0.0372 560 GLU A N 4130 C CA . GLU A 519 ? 0.3317 0.3132 0.4119 0.0908 -0.0002 -0.0406 560 GLU A CA 4131 C C . GLU A 519 ? 0.3200 0.3144 0.4082 0.0896 -0.0012 -0.0443 560 GLU A C 4132 O O . GLU A 519 ? 0.3253 0.3239 0.4209 0.0942 -0.0060 -0.0453 560 GLU A O 4133 C CB . GLU A 519 ? 0.3375 0.3162 0.4247 0.0918 0.0034 -0.0447 560 GLU A CB 4134 C CG . GLU A 519 ? 0.3803 0.3456 0.4628 0.0947 0.0030 -0.0410 560 GLU A CG 4135 C CD . GLU A 519 ? 0.3683 0.3271 0.4421 0.0892 0.0067 -0.0381 560 GLU A CD 4136 O OE1 . GLU A 519 ? 0.3692 0.3330 0.4427 0.0835 0.0103 -0.0413 560 GLU A OE1 4137 O OE2 . GLU A 519 ? 0.4297 0.3782 0.4973 0.0907 0.0060 -0.0326 560 GLU A OE2 4138 N N . LEU A 520 ? 0.3045 0.3051 0.3919 0.0834 0.0032 -0.0463 561 LEU A N 4139 C CA . LEU A 520 ? 0.2960 0.3084 0.3910 0.0816 0.0031 -0.0491 561 LEU A CA 4140 C C . LEU A 520 ? 0.3019 0.3164 0.3955 0.0837 -0.0036 -0.0463 561 LEU A C 4141 O O . LEU A 520 ? 0.3050 0.3272 0.4095 0.0860 -0.0069 -0.0487 561 LEU A O 4142 C CB . LEU A 520 ? 0.2883 0.3045 0.3787 0.0746 0.0086 -0.0501 561 LEU A CB 4143 C CG . LEU A 520 ? 0.2780 0.3056 0.3754 0.0721 0.0091 -0.0519 561 LEU A CG 4144 C CD1 . LEU A 520 ? 0.2682 0.3040 0.3812 0.0750 0.0106 -0.0564 561 LEU A CD1 4145 C CD2 . LEU A 520 ? 0.3081 0.3378 0.3987 0.0655 0.0144 -0.0522 561 LEU A CD2 4146 N N . VAL A 521 ? 0.2974 0.3051 0.3782 0.0828 -0.0054 -0.0416 562 VAL A N 4147 C CA . VAL A 521 ? 0.2923 0.3003 0.3688 0.0851 -0.0118 -0.0390 562 VAL A CA 4148 C C . VAL A 521 ? 0.3232 0.3267 0.4014 0.0930 -0.0186 -0.0380 562 VAL A C 4149 O O . VAL A 521 ? 0.3276 0.3366 0.4125 0.0963 -0.0248 -0.0398 562 VAL A O 4150 C CB . VAL A 521 ? 0.3036 0.3050 0.3651 0.0825 -0.0110 -0.0341 562 VAL A CB 4151 C CG1 . VAL A 521 ? 0.3224 0.3232 0.3779 0.0859 -0.0180 -0.0318 562 VAL A CG1 4152 C CG2 . VAL A 521 ? 0.2920 0.2984 0.3523 0.0749 -0.0055 -0.0353 562 VAL A CG2 4153 N N . GLU A 522 ? 0.3293 0.3226 0.4020 0.0963 -0.0178 -0.0353 563 GLU A N 4154 C CA . GLU A 522 ? 0.3609 0.3477 0.4321 0.1044 -0.0243 -0.0333 563 GLU A CA 4155 C C . GLU A 522 ? 0.3535 0.3474 0.4410 0.1084 -0.0275 -0.0383 563 GLU A C 4156 O O . GLU A 522 ? 0.3693 0.3630 0.4591 0.1147 -0.0352 -0.0382 563 GLU A O 4157 C CB . GLU A 522 ? 0.3823 0.3560 0.4444 0.1065 -0.0217 -0.0287 563 GLU A CB 4158 C CG . GLU A 522 ? 0.4397 0.4042 0.4960 0.1153 -0.0282 -0.0249 563 GLU A CG 4159 C CD . GLU A 522 ? 0.5132 0.4779 0.5814 0.1206 -0.0306 -0.0280 563 GLU A CD 4160 O OE1 . GLU A 522 ? 0.5450 0.5134 0.6236 0.1177 -0.0256 -0.0321 563 GLU A OE1 4161 O OE2 . GLU A 522 ? 0.5474 0.5084 0.6141 0.1282 -0.0381 -0.0266 563 GLU A OE2 4162 N N . LYS A 523 ? 0.3321 0.3322 0.4310 0.1053 -0.0217 -0.0427 564 LYS A N 4163 C CA . LYS A 523 ? 0.3292 0.3364 0.4450 0.1093 -0.0237 -0.0475 564 LYS A CA 4164 C C . LYS A 523 ? 0.3273 0.3480 0.4559 0.1074 -0.0256 -0.0514 564 LYS A C 4165 O O . LYS A 523 ? 0.3616 0.3875 0.5028 0.1123 -0.0314 -0.0539 564 LYS A O 4166 C CB . LYS A 523 ? 0.3214 0.3289 0.4439 0.1077 -0.0163 -0.0509 564 LYS A CB 4167 C CG . LYS A 523 ? 0.3644 0.3585 0.4790 0.1107 -0.0155 -0.0480 564 LYS A CG 4168 C CD . LYS A 523 ? 0.4042 0.3985 0.5259 0.1094 -0.0086 -0.0524 564 LYS A CD 4169 C CE . LYS A 523 ? 0.4608 0.4412 0.5753 0.1113 -0.0073 -0.0497 564 LYS A CE 4170 N NZ . LYS A 523 ? 0.5160 0.4898 0.6320 0.1194 -0.0137 -0.0472 564 LYS A NZ 4171 N N . PHE A 524 ? 0.3190 0.3453 0.4456 0.1004 -0.0207 -0.0518 565 PHE A N 4172 C CA . PHE A 524 ? 0.3209 0.3603 0.4621 0.0975 -0.0197 -0.0557 565 PHE A CA 4173 C C . PHE A 524 ? 0.3242 0.3670 0.4617 0.0946 -0.0237 -0.0543 565 PHE A C 4174 O O . PHE A 524 ? 0.3582 0.4100 0.5091 0.0951 -0.0274 -0.0569 565 PHE A O 4175 C CB . PHE A 524 ? 0.3091 0.3539 0.4552 0.0923 -0.0095 -0.0586 565 PHE A CB 4176 C CG . PHE A 524 ? 0.3210 0.3633 0.4727 0.0956 -0.0058 -0.0612 565 PHE A CG 4177 C CD1 . PHE A 524 ? 0.3601 0.4068 0.5274 0.1015 -0.0091 -0.0642 565 PHE A CD1 4178 C CD2 . PHE A 524 ? 0.3429 0.3780 0.4847 0.0933 0.0004 -0.0610 565 PHE A CD2 4179 C CE1 . PHE A 524 ? 0.3551 0.3993 0.5278 0.1049 -0.0057 -0.0668 565 PHE A CE1 4180 C CE2 . PHE A 524 ? 0.3370 0.3691 0.4839 0.0966 0.0037 -0.0639 565 PHE A CE2 4181 C CZ . PHE A 524 ? 0.3432 0.3795 0.5051 0.1026 0.0007 -0.0667 565 PHE A CZ 4182 N N . TYR A 525 ? 0.3105 0.3468 0.4314 0.0915 -0.0229 -0.0504 566 TYR A N 4183 C CA . TYR A 525 ? 0.3086 0.3483 0.4264 0.0888 -0.0264 -0.0495 566 TYR A CA 4184 C C . TYR A 525 ? 0.3169 0.3511 0.4275 0.0944 -0.0363 -0.0475 566 TYR A C 4185 O O . TYR A 525 ? 0.3234 0.3633 0.4406 0.0950 -0.0425 -0.0494 566 TYR A O 4186 C CB . TYR A 525 ? 0.2968 0.3335 0.4014 0.0823 -0.0204 -0.0468 566 TYR A CB 4187 C CG . TYR A 525 ? 0.3131 0.3579 0.4253 0.0761 -0.0127 -0.0494 566 TYR A CG 4188 C CD1 . TYR A 525 ? 0.2983 0.3430 0.4132 0.0752 -0.0057 -0.0512 566 TYR A CD1 4189 C CD2 . TYR A 525 ? 0.3141 0.3662 0.4300 0.0716 -0.0122 -0.0499 566 TYR A CD2 4190 C CE1 . TYR A 525 ? 0.3002 0.3515 0.4198 0.0702 0.0017 -0.0534 566 TYR A CE1 4191 C CE2 . TYR A 525 ? 0.2986 0.3574 0.4203 0.0664 -0.0047 -0.0516 566 TYR A CE2 4192 C CZ . TYR A 525 ? 0.3120 0.3702 0.4348 0.0659 0.0022 -0.0533 566 TYR A CZ 4193 O OH . TYR A 525 ? 0.3180 0.3823 0.4449 0.0615 0.0096 -0.0549 566 TYR A OH 4194 N N . ASP A 526 ? 0.3079 0.3306 0.4043 0.0986 -0.0380 -0.0436 567 ASP A N 4195 C CA . ASP A 526 ? 0.3182 0.3341 0.4028 0.1038 -0.0464 -0.0408 567 ASP A CA 4196 C C . ASP A 526 ? 0.3417 0.3459 0.4164 0.1107 -0.0488 -0.0372 567 ASP A C 4197 O O . ASP A 526 ? 0.3528 0.3470 0.4108 0.1114 -0.0472 -0.0322 567 ASP A O 4198 C CB . ASP A 526 ? 0.2941 0.3073 0.3647 0.0991 -0.0441 -0.0378 567 ASP A CB 4199 C CG . ASP A 526 ? 0.3234 0.3314 0.3823 0.1040 -0.0527 -0.0360 567 ASP A CG 4200 O OD1 . ASP A 526 ? 0.3719 0.3803 0.4351 0.1102 -0.0615 -0.0380 567 ASP A OD1 4201 O OD2 . ASP A 526 ? 0.3385 0.3421 0.3838 0.1016 -0.0504 -0.0328 567 ASP A OD2 4202 N N . PRO A 527 ? 0.3556 0.3607 0.4411 0.1162 -0.0526 -0.0395 568 PRO A N 4203 C CA . PRO A 527 ? 0.3790 0.3726 0.4560 0.1227 -0.0542 -0.0359 568 PRO A CA 4204 C C . PRO A 527 ? 0.3941 0.3765 0.4523 0.1286 -0.0604 -0.0309 568 PRO A C 4205 O O . PRO A 527 ? 0.4187 0.3893 0.4640 0.1314 -0.0578 -0.0257 568 PRO A O 4206 C CB . PRO A 527 ? 0.3775 0.3763 0.4718 0.1281 -0.0593 -0.0403 568 PRO A CB 4207 C CG . PRO A 527 ? 0.3863 0.3993 0.4991 0.1219 -0.0549 -0.0458 568 PRO A CG 4208 C CD . PRO A 527 ? 0.3662 0.3834 0.4736 0.1156 -0.0533 -0.0454 568 PRO A CD 4209 N N . MET A 528 ? 0.3847 0.3705 0.4411 0.1305 -0.0681 -0.0326 569 MET A N 4210 C CA . MET A 528 ? 0.4163 0.3914 0.4535 0.1371 -0.0747 -0.0285 569 MET A CA 4211 C C . MET A 528 ? 0.4016 0.3729 0.4229 0.1327 -0.0701 -0.0248 569 MET A C 4212 O O . MET A 528 ? 0.4152 0.3772 0.4183 0.1377 -0.0738 -0.0210 569 MET A O 4213 C CB . MET A 528 ? 0.4468 0.4261 0.4899 0.1432 -0.0873 -0.0328 569 MET A CB 4214 C CG . MET A 528 ? 0.5040 0.4857 0.5618 0.1491 -0.0931 -0.0359 569 MET A CG 4215 S SD . MET A 528 ? 0.6531 0.6185 0.6962 0.1570 -0.0922 -0.0294 569 MET A SD 4216 C CE . MET A 528 ? 0.6465 0.5984 0.6631 0.1657 -0.1010 -0.0246 569 MET A CE 4217 N N . PHE A 529 ? 0.3633 0.3417 0.3911 0.1238 -0.0619 -0.0260 570 PHE A N 4218 C CA . PHE A 529 ? 0.3530 0.3300 0.3689 0.1188 -0.0575 -0.0234 570 PHE A CA 4219 C C . PHE A 529 ? 0.3612 0.3398 0.3714 0.1210 -0.0653 -0.0251 570 PHE A C 4220 O O . PHE A 529 ? 0.3606 0.3350 0.3569 0.1196 -0.0633 -0.0221 570 PHE A O 4221 C CB . PHE A 529 ? 0.3666 0.3317 0.3665 0.1191 -0.0506 -0.0164 570 PHE A CB 4222 C CG . PHE A 529 ? 0.3704 0.3367 0.3783 0.1135 -0.0417 -0.0162 570 PHE A CG 4223 C CD1 . PHE A 529 ? 0.3669 0.3369 0.3753 0.1053 -0.0342 -0.0160 570 PHE A CD1 4224 C CD2 . PHE A 529 ? 0.3888 0.3533 0.4051 0.1164 -0.0416 -0.0170 570 PHE A CD2 4225 C CE1 . PHE A 529 ? 0.3593 0.3307 0.3756 0.1003 -0.0269 -0.0169 570 PHE A CE1 4226 C CE2 . PHE A 529 ? 0.3845 0.3500 0.4086 0.1114 -0.0340 -0.0178 570 PHE A CE2 4227 C CZ . PHE A 529 ? 0.3476 0.3164 0.3711 0.1034 -0.0268 -0.0178 570 PHE A CZ 4228 N N . LYS A 530 ? 0.3526 0.3384 0.3758 0.1238 -0.0739 -0.0304 571 LYS A N 4229 C CA . LYS A 530 ? 0.3692 0.3568 0.3893 0.1260 -0.0828 -0.0332 571 LYS A CA 4230 C C . LYS A 530 ? 0.3557 0.3522 0.3825 0.1176 -0.0790 -0.0356 571 LYS A C 4231 O O . LYS A 530 ? 0.3503 0.3447 0.3674 0.1180 -0.0826 -0.0357 571 LYS A O 4232 C CB . LYS A 530 ? 0.3748 0.3671 0.4080 0.1319 -0.0943 -0.0385 571 LYS A CB 4233 C CG . LYS A 530 ? 0.3852 0.3910 0.4449 0.1273 -0.0929 -0.0437 571 LYS A CG 4234 C CD . LYS A 530 ? 0.4096 0.4192 0.4823 0.1340 -0.1052 -0.0488 571 LYS A CD 4235 C CE . LYS A 530 ? 0.4479 0.4717 0.5487 0.1295 -0.1033 -0.0539 571 LYS A CE 4236 N NZ . LYS A 530 ? 0.4499 0.4792 0.5665 0.1353 -0.1160 -0.0595 571 LYS A NZ 4237 N N . TYR A 531 ? 0.3357 0.3415 0.3785 0.1104 -0.0720 -0.0377 572 TYR A N 4238 C CA . TYR A 531 ? 0.3352 0.3484 0.3832 0.1024 -0.0677 -0.0392 572 TYR A CA 4239 C C . TYR A 531 ? 0.3282 0.3347 0.3590 0.0992 -0.0607 -0.0343 572 TYR A C 4240 O O . TYR A 531 ? 0.3356 0.3431 0.3613 0.0964 -0.0612 -0.0344 572 TYR A O 4241 C CB . TYR A 531 ? 0.3287 0.3529 0.3967 0.0962 -0.0615 -0.0423 572 TYR A CB 4242 C CG . TYR A 531 ? 0.3285 0.3602 0.4155 0.0994 -0.0681 -0.0472 572 TYR A CG 4243 C CD1 . TYR A 531 ? 0.3379 0.3735 0.4319 0.1016 -0.0779 -0.0509 572 TYR A CD1 4244 C CD2 . TYR A 531 ? 0.3521 0.3866 0.4505 0.1007 -0.0651 -0.0483 572 TYR A CD2 4245 C CE1 . TYR A 531 ? 0.3808 0.4237 0.4943 0.1047 -0.0844 -0.0555 572 TYR A CE1 4246 C CE2 . TYR A 531 ? 0.3722 0.4138 0.4891 0.1040 -0.0710 -0.0528 572 TYR A CE2 4247 C CZ . TYR A 531 ? 0.3881 0.4342 0.5131 0.1058 -0.0806 -0.0563 572 TYR A CZ 4248 O OH . TYR A 531 ? 0.4285 0.4823 0.5744 0.1090 -0.0866 -0.0609 572 TYR A OH 4249 N N . HIS A 532 ? 0.3187 0.3184 0.3414 0.0997 -0.0544 -0.0301 573 HIS A N 4250 C CA . HIS A 532 ? 0.3185 0.3112 0.3256 0.0972 -0.0479 -0.0251 573 HIS A CA 4251 C C . HIS A 532 ? 0.3162 0.3010 0.3062 0.1028 -0.0533 -0.0226 573 HIS A C 4252 O O . HIS A 532 ? 0.3187 0.3026 0.3006 0.0998 -0.0507 -0.0212 573 HIS A O 4253 C CB . HIS A 532 ? 0.3228 0.3084 0.3254 0.0980 -0.0417 -0.0210 573 HIS A CB 4254 C CG . HIS A 532 ? 0.3391 0.3305 0.3533 0.0913 -0.0342 -0.0226 573 HIS A CG 4255 N ND1 . HIS A 532 ? 0.3246 0.3224 0.3541 0.0911 -0.0345 -0.0267 573 HIS A ND1 4256 C CD2 . HIS A 532 ? 0.3640 0.3554 0.3762 0.0851 -0.0263 -0.0210 573 HIS A CD2 4257 C CE1 . HIS A 532 ? 0.3528 0.3539 0.3878 0.0851 -0.0270 -0.0275 573 HIS A CE1 4258 N NE2 . HIS A 532 ? 0.3805 0.3777 0.4053 0.0814 -0.0224 -0.0242 573 HIS A NE2 4259 N N . LEU A 533 ? 0.3364 0.3150 0.3203 0.1112 -0.0606 -0.0222 574 LEU A N 4260 C CA . LEU A 533 ? 0.3473 0.3176 0.3131 0.1174 -0.0660 -0.0202 574 LEU A CA 4261 C C . LEU A 533 ? 0.3539 0.3302 0.3226 0.1155 -0.0716 -0.0248 574 LEU A C 4262 O O . LEU A 533 ? 0.3443 0.3164 0.2994 0.1157 -0.0706 -0.0229 574 LEU A O 4263 C CB . LEU A 533 ? 0.3648 0.3273 0.3233 0.1274 -0.0740 -0.0195 574 LEU A CB 4264 C CG . LEU A 533 ? 0.3763 0.3297 0.3144 0.1347 -0.0803 -0.0180 574 LEU A CG 4265 C CD1 . LEU A 533 ? 0.4319 0.3761 0.3515 0.1343 -0.0710 -0.0109 574 LEU A CD1 4266 C CD2 . LEU A 533 ? 0.4034 0.3500 0.3364 0.1449 -0.0895 -0.0181 574 LEU A CD2 4267 N N . THR A 534 ? 0.3407 0.3269 0.3277 0.1137 -0.0773 -0.0307 575 THR A N 4268 C CA . THR A 534 ? 0.3303 0.3228 0.3233 0.1111 -0.0825 -0.0354 575 THR A CA 4269 C C . THR A 534 ? 0.3209 0.3161 0.3122 0.1031 -0.0743 -0.0338 575 THR A C 4270 O O . THR A 534 ? 0.3204 0.3135 0.3029 0.1033 -0.0766 -0.0342 575 THR A O 4271 C CB . THR A 534 ? 0.3354 0.3390 0.3524 0.1093 -0.0882 -0.0416 575 THR A CB 4272 O OG1 . THR A 534 ? 0.3547 0.3551 0.3722 0.1179 -0.0985 -0.0437 575 THR A OG1 4273 C CG2 . THR A 534 ? 0.3421 0.3526 0.3682 0.1051 -0.0922 -0.0460 575 THR A CG2 4274 N N . VAL A 535 ? 0.2972 0.2969 0.2963 0.0966 -0.0648 -0.0321 576 VAL A N 4275 C CA . VAL A 535 ? 0.2966 0.2983 0.2934 0.0894 -0.0570 -0.0303 576 VAL A CA 4276 C C . VAL A 535 ? 0.3048 0.2971 0.2817 0.0915 -0.0536 -0.0253 576 VAL A C 4277 O O . VAL A 535 ? 0.3012 0.2939 0.2732 0.0884 -0.0518 -0.0249 576 VAL A O 4278 C CB . VAL A 535 ? 0.2842 0.2921 0.2929 0.0826 -0.0486 -0.0301 576 VAL A CB 4279 C CG1 . VAL A 535 ? 0.2813 0.2904 0.2859 0.0756 -0.0409 -0.0279 576 VAL A CG1 4280 C CG2 . VAL A 535 ? 0.2996 0.3178 0.3281 0.0802 -0.0514 -0.0351 576 VAL A CG2 4281 N N . ALA A 536 ? 0.3196 0.3032 0.2856 0.0969 -0.0523 -0.0212 577 ALA A N 4282 C CA . ALA A 536 ? 0.3299 0.3039 0.2768 0.0999 -0.0488 -0.0160 577 ALA A CA 4283 C C . ALA A 536 ? 0.3375 0.3075 0.2722 0.1052 -0.0560 -0.0175 577 ALA A C 4284 O O . ALA A 536 ? 0.3392 0.3059 0.2631 0.1045 -0.0525 -0.0152 577 ALA A O 4285 C CB . ALA A 536 ? 0.3369 0.3017 0.2748 0.1052 -0.0463 -0.0111 577 ALA A CB 4286 N N . GLN A 537 ? 0.3603 0.3304 0.2972 0.1107 -0.0662 -0.0215 578 GLN A N 4287 C CA . GLN A 537 ? 0.3538 0.3207 0.2810 0.1158 -0.0748 -0.0244 578 GLN A CA 4288 C C . GLN A 537 ? 0.3517 0.3257 0.2864 0.1094 -0.0749 -0.0280 578 GLN A C 4289 O O . GLN A 537 ? 0.3511 0.3205 0.2731 0.1118 -0.0766 -0.0281 578 GLN A O 4290 C CB . GLN A 537 ? 0.3700 0.3367 0.3013 0.1225 -0.0867 -0.0290 578 GLN A CB 4291 C CG . GLN A 537 ? 0.3690 0.3262 0.2884 0.1306 -0.0876 -0.0249 578 GLN A CG 4292 C CD . GLN A 537 ? 0.4356 0.3929 0.3602 0.1374 -0.1000 -0.0295 578 GLN A CD 4293 O OE1 . GLN A 537 ? 0.4258 0.3914 0.3659 0.1354 -0.1074 -0.0359 578 GLN A OE1 4294 N NE2 . GLN A 537 ? 0.4413 0.3895 0.3545 0.1455 -0.1022 -0.0261 578 GLN A NE2 4295 N N . VAL A 538 ? 0.3322 0.3168 0.2871 0.1019 -0.0732 -0.0310 579 VAL A N 4296 C CA . VAL A 538 ? 0.3284 0.3195 0.2913 0.0957 -0.0731 -0.0339 579 VAL A CA 4297 C C . VAL A 538 ? 0.3233 0.3123 0.2774 0.0913 -0.0636 -0.0296 579 VAL A C 4298 O O . VAL A 538 ? 0.3173 0.3041 0.2634 0.0914 -0.0645 -0.0299 579 VAL A O 4299 C CB . VAL A 538 ? 0.3128 0.3154 0.2993 0.0888 -0.0723 -0.0374 579 VAL A CB 4300 C CG1 . VAL A 538 ? 0.3066 0.3148 0.3004 0.0820 -0.0706 -0.0392 579 VAL A CG1 4301 C CG2 . VAL A 538 ? 0.3295 0.3352 0.3277 0.0930 -0.0823 -0.0423 579 VAL A CG2 4302 N N . ARG A 539 ? 0.3100 0.2997 0.2659 0.0876 -0.0546 -0.0256 580 ARG A N 4303 C CA . ARG A 539 ? 0.2956 0.2842 0.2454 0.0831 -0.0462 -0.0219 580 ARG A CA 4304 C C . ARG A 539 ? 0.3269 0.3057 0.2570 0.0890 -0.0452 -0.0181 580 ARG A C 4305 O O . ARG A 539 ? 0.3160 0.2938 0.2398 0.0876 -0.0429 -0.0173 580 ARG A O 4306 C CB . ARG A 539 ? 0.2946 0.2848 0.2497 0.0787 -0.0377 -0.0187 580 ARG A CB 4307 C CG . ARG A 539 ? 0.2712 0.2710 0.2443 0.0724 -0.0366 -0.0221 580 ARG A CG 4308 C CD . ARG A 539 ? 0.2899 0.2897 0.2662 0.0695 -0.0292 -0.0195 580 ARG A CD 4309 N NE . ARG A 539 ? 0.2844 0.2927 0.2759 0.0641 -0.0275 -0.0226 580 ARG A NE 4310 C CZ . ARG A 539 ? 0.2993 0.3093 0.2967 0.0613 -0.0223 -0.0222 580 ARG A CZ 4311 N NH1 . ARG A 539 ? 0.3313 0.3350 0.3222 0.0630 -0.0185 -0.0188 580 ARG A NH1 4312 N NH2 . ARG A 539 ? 0.2655 0.2831 0.2753 0.0568 -0.0206 -0.0252 580 ARG A NH2 4313 N N . GLY A 540 ? 0.3403 0.3117 0.2606 0.0958 -0.0464 -0.0156 581 GLY A N 4314 C CA . GLY A 540 ? 0.3566 0.3176 0.2567 0.1025 -0.0446 -0.0113 581 GLY A CA 4315 C C . GLY A 540 ? 0.3645 0.3223 0.2544 0.1077 -0.0523 -0.0146 581 GLY A C 4316 O O . GLY A 540 ? 0.3646 0.3175 0.2416 0.1095 -0.0490 -0.0124 581 GLY A O 4317 N N . GLY A 541 ? 0.3613 0.3222 0.2581 0.1097 -0.0625 -0.0204 582 GLY A N 4318 C CA . GLY A 541 ? 0.3637 0.3216 0.2525 0.1145 -0.0714 -0.0248 582 GLY A CA 4319 C C . GLY A 541 ? 0.3612 0.3237 0.2544 0.1086 -0.0692 -0.0267 582 GLY A C 4320 O O . GLY A 541 ? 0.3644 0.3215 0.2444 0.1126 -0.0713 -0.0274 582 GLY A O 4321 N N . MET A 542 ? 0.3339 0.3060 0.2452 0.0995 -0.0651 -0.0275 583 MET A N 4322 C CA . MET A 542 ? 0.3256 0.3020 0.2418 0.0935 -0.0625 -0.0287 583 MET A CA 4323 C C . MET A 542 ? 0.3274 0.2985 0.2297 0.0942 -0.0542 -0.0236 583 MET A C 4324 O O . MET A 542 ? 0.3294 0.2980 0.2243 0.0954 -0.0552 -0.0247 583 MET A O 4325 C CB . MET A 542 ? 0.3113 0.2981 0.2477 0.0841 -0.0587 -0.0296 583 MET A CB 4326 C CG . MET A 542 ? 0.3261 0.3189 0.2780 0.0831 -0.0668 -0.0351 583 MET A CG 4327 S SD . MET A 542 ? 0.3643 0.3684 0.3380 0.0730 -0.0608 -0.0354 583 MET A SD 4328 C CE . MET A 542 ? 0.3452 0.3516 0.3207 0.0673 -0.0589 -0.0359 583 MET A CE 4329 N N . VAL A 543 ? 0.3167 0.2860 0.2162 0.0934 -0.0460 -0.0182 584 VAL A N 4330 C CA . VAL A 543 ? 0.3264 0.2911 0.2149 0.0939 -0.0375 -0.0130 584 VAL A CA 4331 C C . VAL A 543 ? 0.3519 0.3068 0.2203 0.1030 -0.0398 -0.0120 584 VAL A C 4332 O O . VAL A 543 ? 0.3455 0.2983 0.2063 0.1035 -0.0365 -0.0111 584 VAL A O 4333 C CB . VAL A 543 ? 0.3531 0.3170 0.2437 0.0918 -0.0289 -0.0075 584 VAL A CB 4334 C CG1 . VAL A 543 ? 0.3411 0.2993 0.2206 0.0932 -0.0199 -0.0016 584 VAL A CG1 4335 C CG2 . VAL A 543 ? 0.3320 0.3053 0.2410 0.0825 -0.0258 -0.0087 584 VAL A CG2 4336 N N . PHE A 544 ? 0.3601 0.3090 0.2197 0.1103 -0.0454 -0.0124 585 PHE A N 4337 C CA . PHE A 544 ? 0.3797 0.3182 0.2177 0.1202 -0.0483 -0.0117 585 PHE A CA 4338 C C . PHE A 544 ? 0.3932 0.3316 0.2275 0.1216 -0.0546 -0.0171 585 PHE A C 4339 O O . PHE A 544 ? 0.4054 0.3379 0.2249 0.1256 -0.0509 -0.0152 585 PHE A O 4340 C CB . PHE A 544 ? 0.4002 0.3327 0.2307 0.1280 -0.0561 -0.0126 585 PHE A CB 4341 C CG . PHE A 544 ? 0.4365 0.3566 0.2417 0.1390 -0.0575 -0.0104 585 PHE A CG 4342 C CD1 . PHE A 544 ? 0.4602 0.3720 0.2521 0.1436 -0.0498 -0.0029 585 PHE A CD1 4343 C CD2 . PHE A 544 ? 0.4807 0.3968 0.2751 0.1447 -0.0659 -0.0156 585 PHE A CD2 4344 C CE1 . PHE A 544 ? 0.5213 0.4208 0.2880 0.1541 -0.0497 -0.0002 585 PHE A CE1 4345 C CE2 . PHE A 544 ? 0.4666 0.3704 0.2354 0.1555 -0.0669 -0.0137 585 PHE A CE2 4346 C CZ . PHE A 544 ? 0.5070 0.4026 0.2616 0.1602 -0.0582 -0.0057 585 PHE A CZ 4347 N N . GLU A 545 ? 0.3891 0.3340 0.2373 0.1183 -0.0634 -0.0236 586 GLU A N 4348 C CA . GLU A 545 ? 0.3970 0.3413 0.2430 0.1199 -0.0709 -0.0294 586 GLU A CA 4349 C C . GLU A 545 ? 0.3710 0.3187 0.2204 0.1140 -0.0636 -0.0281 586 GLU A C 4350 O O . GLU A 545 ? 0.3844 0.3273 0.2224 0.1177 -0.0642 -0.0293 586 GLU A O 4351 C CB . GLU A 545 ? 0.4122 0.3635 0.2762 0.1165 -0.0812 -0.0363 586 GLU A CB 4352 C CG . GLU A 545 ? 0.5072 0.4544 0.3670 0.1239 -0.0924 -0.0404 586 GLU A CG 4353 C CD . GLU A 545 ? 0.5519 0.4879 0.3883 0.1342 -0.0984 -0.0426 586 GLU A CD 4354 O OE1 . GLU A 545 ? 0.6470 0.5742 0.4645 0.1417 -0.0957 -0.0384 586 GLU A OE1 4355 O OE2 . GLU A 545 ? 0.6538 0.5891 0.4901 0.1347 -0.1046 -0.0480 586 GLU A OE2 4356 N N . LEU A 546 ? 0.3523 0.3081 0.2170 0.1051 -0.0566 -0.0255 587 LEU A N 4357 C CA . LEU A 546 ? 0.3333 0.2925 0.2020 0.0995 -0.0499 -0.0240 587 LEU A CA 4358 C C . LEU A 546 ? 0.3466 0.2991 0.1992 0.1038 -0.0417 -0.0188 587 LEU A C 4359 O O . LEU A 546 ? 0.3627 0.3144 0.2113 0.1038 -0.0395 -0.0192 587 LEU A O 4360 C CB . LEU A 546 ? 0.3204 0.2889 0.2074 0.0897 -0.0443 -0.0221 587 LEU A CB 4361 C CG . LEU A 546 ? 0.3223 0.2983 0.2266 0.0845 -0.0507 -0.0269 587 LEU A CG 4362 C CD1 . LEU A 546 ? 0.3065 0.2895 0.2247 0.0775 -0.0451 -0.0246 587 LEU A CD1 4363 C CD2 . LEU A 546 ? 0.3586 0.3374 0.2685 0.0805 -0.0524 -0.0299 587 LEU A CD2 4364 N N . ALA A 547 ? 0.3608 0.3082 0.2041 0.1080 -0.0369 -0.0139 588 ALA A N 4365 C CA . ALA A 547 ? 0.3822 0.3237 0.2123 0.1115 -0.0272 -0.0079 588 ALA A CA 4366 C C . ALA A 547 ? 0.3991 0.3302 0.2070 0.1222 -0.0303 -0.0086 588 ALA A C 4367 O O . ALA A 547 ? 0.4181 0.3443 0.2144 0.1256 -0.0226 -0.0046 588 ALA A O 4368 C CB . ALA A 547 ? 0.3763 0.3169 0.2080 0.1102 -0.0191 -0.0015 588 ALA A CB 4369 N N . ASN A 548 ? 0.4114 0.3390 0.2137 0.1275 -0.0413 -0.0137 589 ASN A N 4370 C CA . ASN A 548 ? 0.4316 0.3479 0.2101 0.1390 -0.0449 -0.0143 589 ASN A CA 4371 C C . ASN A 548 ? 0.4507 0.3645 0.2238 0.1431 -0.0559 -0.0221 589 ASN A C 4372 O O . ASN A 548 ? 0.4837 0.3879 0.2357 0.1522 -0.0572 -0.0227 589 ASN A O 4373 C CB . ASN A 548 ? 0.4393 0.3495 0.2089 0.1451 -0.0478 -0.0120 589 ASN A CB 4374 C CG A ASN A 548 ? 0.4653 0.3632 0.2093 0.1553 -0.0425 -0.0067 589 ASN A CG 4375 C CG B ASN A 548 ? 0.4642 0.3720 0.2309 0.1444 -0.0354 -0.0032 589 ASN A CG 4376 O OD1 A ASN A 548 ? 0.4771 0.3733 0.2167 0.1545 -0.0303 -0.0004 589 ASN A OD1 4377 O OD1 B ASN A 548 ? 0.5016 0.4019 0.2521 0.1497 -0.0273 0.0020 589 ASN A OD1 4378 N ND2 A ASN A 548 ? 0.5384 0.4273 0.2655 0.1652 -0.0514 -0.0092 589 ASN A ND2 4379 N ND2 B ASN A 548 ? 0.4710 0.3850 0.2538 0.1379 -0.0336 -0.0013 589 ASN A ND2 4380 N N . SER A 549 ? 0.4300 0.3517 0.2213 0.1368 -0.0638 -0.0282 590 SER A N 4381 C CA . SER A 549 ? 0.4334 0.3527 0.2217 0.1402 -0.0750 -0.0361 590 SER A CA 4382 C C . SER A 549 ? 0.4308 0.3473 0.2107 0.1414 -0.0703 -0.0362 590 SER A C 4383 O O . SER A 549 ? 0.4309 0.3529 0.2198 0.1347 -0.0610 -0.0325 590 SER A O 4384 C CB . SER A 549 ? 0.4385 0.3677 0.2513 0.1319 -0.0825 -0.0416 590 SER A CB 4385 O OG . SER A 549 ? 0.4785 0.4049 0.2901 0.1353 -0.0943 -0.0496 590 SER A OG 4386 N N . ILE A 550 ? 0.4314 0.3390 0.1939 0.1503 -0.0770 -0.0407 591 ILE A N 4387 C CA . ILE A 550 ? 0.4391 0.3435 0.1931 0.1522 -0.0728 -0.0414 591 ILE A CA 4388 C C . ILE A 550 ? 0.4287 0.3420 0.2037 0.1427 -0.0740 -0.0447 591 ILE A C 4389 O O . ILE A 550 ? 0.4393 0.3558 0.2181 0.1386 -0.0646 -0.0411 591 ILE A O 4390 C CB . ILE A 550 ? 0.4551 0.3478 0.1862 0.1641 -0.0815 -0.0470 591 ILE A CB 4391 C CG1 A ILE A 550 ? 0.4981 0.3812 0.2060 0.1738 -0.0776 -0.0419 591 ILE A CG1 4392 C CG1 B ILE A 550 ? 0.5033 0.3865 0.2116 0.1738 -0.0780 -0.0420 591 ILE A CG1 4393 C CG2 A ILE A 550 ? 0.4898 0.3796 0.2143 0.1659 -0.0785 -0.0491 591 ILE A CG2 4394 C CG2 B ILE A 550 ? 0.4931 0.3827 0.2167 0.1661 -0.0779 -0.0487 591 ILE A CG2 4395 C CD1 A ILE A 550 ? 0.5030 0.3738 0.1865 0.1862 -0.0866 -0.0473 591 ILE A CD1 4396 C CD1 B ILE A 550 ? 0.5014 0.3844 0.2044 0.1728 -0.0614 -0.0322 591 ILE A CD1 4397 N N . VAL A 551 ? 0.4392 0.3560 0.2276 0.1397 -0.0855 -0.0513 592 VAL A N 4398 C CA . VAL A 551 ? 0.4230 0.3482 0.2328 0.1301 -0.0865 -0.0538 592 VAL A CA 4399 C C . VAL A 551 ? 0.3991 0.3342 0.2283 0.1211 -0.0829 -0.0502 592 VAL A C 4400 O O . VAL A 551 ? 0.4156 0.3513 0.2474 0.1224 -0.0878 -0.0510 592 VAL A O 4401 C CB . VAL A 551 ? 0.4430 0.3668 0.2588 0.1312 -0.1002 -0.0627 592 VAL A CB 4402 C CG1 . VAL A 551 ? 0.4478 0.3799 0.2864 0.1210 -0.1008 -0.0645 592 VAL A CG1 4403 C CG2 . VAL A 551 ? 0.4789 0.3919 0.2740 0.1407 -0.1042 -0.0671 592 VAL A CG2 4404 N N . LEU A 552 ? 0.4003 0.3429 0.2432 0.1124 -0.0751 -0.0467 593 LEU A N 4405 C CA . LEU A 552 ? 0.3787 0.3301 0.2389 0.1042 -0.0717 -0.0437 593 LEU A CA 4406 C C . LEU A 552 ? 0.3790 0.3344 0.2538 0.1017 -0.0820 -0.0492 593 LEU A C 4407 O O . LEU A 552 ? 0.3884 0.3434 0.2692 0.1012 -0.0899 -0.0549 593 LEU A O 4408 C CB . LEU A 552 ? 0.3561 0.3145 0.2285 0.0954 -0.0631 -0.0401 593 LEU A CB 4409 C CG . LEU A 552 ? 0.3743 0.3314 0.2378 0.0961 -0.0518 -0.0337 593 LEU A CG 4410 C CD1 . LEU A 552 ? 0.3563 0.3198 0.2321 0.0882 -0.0461 -0.0317 593 LEU A CD1 4411 C CD2 . LEU A 552 ? 0.4237 0.3815 0.2856 0.0964 -0.0466 -0.0288 593 LEU A CD2 4412 N N . PRO A 553 ? 0.3646 0.3240 0.2467 0.1000 -0.0820 -0.0476 594 PRO A N 4413 C CA . PRO A 553 ? 0.3783 0.3414 0.2745 0.0986 -0.0916 -0.0528 594 PRO A CA 4414 C C . PRO A 553 ? 0.3600 0.3329 0.2794 0.0883 -0.0898 -0.0531 594 PRO A C 4415 O O . PRO A 553 ? 0.3466 0.3260 0.2794 0.0841 -0.0888 -0.0522 594 PRO A O 4416 C CB . PRO A 553 ? 0.3763 0.3390 0.2695 0.1019 -0.0914 -0.0504 594 PRO A CB 4417 C CG . PRO A 553 ? 0.3890 0.3526 0.2770 0.0993 -0.0784 -0.0427 594 PRO A CG 4418 C CD . PRO A 553 ? 0.3759 0.3352 0.2524 0.1007 -0.0736 -0.0413 594 PRO A CD 4419 N N . PHE A 554 ? 0.3516 0.3250 0.2746 0.0847 -0.0890 -0.0542 595 PHE A N 4420 C CA . PHE A 554 ? 0.3442 0.3255 0.2872 0.0753 -0.0870 -0.0541 595 PHE A CA 4421 C C . PHE A 554 ? 0.3644 0.3441 0.3153 0.0755 -0.0969 -0.0605 595 PHE A C 4422 O O . PHE A 554 ? 0.3889 0.3613 0.3276 0.0811 -0.1015 -0.0636 595 PHE A O 4423 C CB . PHE A 554 ? 0.3306 0.3128 0.2711 0.0711 -0.0780 -0.0497 595 PHE A CB 4424 C CG . PHE A 554 ? 0.3150 0.2994 0.2508 0.0695 -0.0679 -0.0434 595 PHE A CG 4425 C CD1 . PHE A 554 ? 0.3251 0.3130 0.2654 0.0686 -0.0660 -0.0416 595 PHE A CD1 4426 C CD2 . PHE A 554 ? 0.3226 0.3060 0.2518 0.0683 -0.0603 -0.0395 595 PHE A CD2 4427 C CE1 . PHE A 554 ? 0.3256 0.3152 0.2626 0.0667 -0.0567 -0.0360 595 PHE A CE1 4428 C CE2 . PHE A 554 ? 0.3208 0.3063 0.2474 0.0664 -0.0513 -0.0340 595 PHE A CE2 4429 C CZ . PHE A 554 ? 0.3248 0.3132 0.2553 0.0655 -0.0497 -0.0324 595 PHE A CZ 4430 N N . ASP A 555 ? 0.3374 0.3236 0.3088 0.0698 -0.1003 -0.0628 596 ASP A N 4431 C CA . ASP A 555 ? 0.3247 0.3101 0.3076 0.0686 -0.1092 -0.0686 596 ASP A CA 4432 C C . ASP A 555 ? 0.3233 0.3138 0.3213 0.0595 -0.1037 -0.0662 596 ASP A C 4433 O O . ASP A 555 ? 0.3013 0.2995 0.3163 0.0530 -0.1002 -0.0643 596 ASP A O 4434 C CB . ASP A 555 ? 0.3428 0.3307 0.3389 0.0700 -0.1190 -0.0739 596 ASP A CB 4435 C CG . ASP A 555 ? 0.3647 0.3498 0.3700 0.0706 -0.1300 -0.0810 596 ASP A CG 4436 O OD1 . ASP A 555 ? 0.3810 0.3637 0.3876 0.0679 -0.1293 -0.0815 596 ASP A OD1 4437 O OD2 . ASP A 555 ? 0.4119 0.3963 0.4228 0.0746 -0.1406 -0.0868 596 ASP A OD2 4438 N N . CYS A 556 ? 0.3213 0.3073 0.3127 0.0595 -0.1026 -0.0661 597 CYS A N 4439 C CA . CYS A 556 ? 0.3150 0.3046 0.3192 0.0515 -0.0978 -0.0635 597 CYS A CA 4440 C C . CYS A 556 ? 0.3094 0.3028 0.3360 0.0464 -0.1033 -0.0668 597 CYS A C 4441 O O . CYS A 556 ? 0.3069 0.3052 0.3466 0.0390 -0.0976 -0.0633 597 CYS A O 4442 C CB . CYS A 556 ? 0.3062 0.2897 0.3002 0.0530 -0.0970 -0.0634 597 CYS A CB 4443 S SG . CYS A 556 ? 0.3844 0.3588 0.3727 0.0602 -0.1099 -0.0720 597 CYS A SG 4444 N N . ARG A 557 ? 0.2991 0.2904 0.3311 0.0501 -0.1142 -0.0734 598 ARG A N 4445 C CA . ARG A 557 ? 0.3041 0.2993 0.3599 0.0449 -0.1192 -0.0765 598 ARG A CA 4446 C C . ARG A 557 ? 0.3057 0.3106 0.3779 0.0392 -0.1134 -0.0731 598 ARG A C 4447 O O . ARG A 557 ? 0.3060 0.3156 0.3985 0.0326 -0.1123 -0.0727 598 ARG A O 4448 C CB . ARG A 557 ? 0.3141 0.3053 0.3726 0.0508 -0.1332 -0.0850 598 ARG A CB 4449 C CG . ARG A 557 ? 0.3308 0.3121 0.3745 0.0564 -0.1392 -0.0891 598 ARG A CG 4450 C CD . ARG A 557 ? 0.3648 0.3406 0.4050 0.0642 -0.1534 -0.0977 598 ARG A CD 4451 N NE . ARG A 557 ? 0.3792 0.3546 0.4049 0.0709 -0.1540 -0.0972 598 ARG A NE 4452 C CZ . ARG A 557 ? 0.4611 0.4316 0.4799 0.0789 -0.1657 -0.1037 598 ARG A CZ 4453 N NH1 . ARG A 557 ? 0.4627 0.4286 0.4885 0.0811 -0.1781 -0.1118 598 ARG A NH1 4454 N NH2 . ARG A 557 ? 0.4449 0.4147 0.4500 0.0848 -0.1653 -0.1023 598 ARG A NH2 4455 N N . ASP A 558 ? 0.3000 0.3073 0.3630 0.0418 -0.1092 -0.0705 599 ASP A N 4456 C CA . ASP A 558 ? 0.2918 0.3079 0.3688 0.0371 -0.1033 -0.0674 599 ASP A CA 4457 C C . ASP A 558 ? 0.2765 0.2961 0.3565 0.0298 -0.0918 -0.0609 599 ASP A C 4458 O O . ASP A 558 ? 0.2814 0.3078 0.3781 0.0240 -0.0870 -0.0589 599 ASP A O 4459 C CB . ASP A 558 ? 0.2990 0.3159 0.3646 0.0422 -0.1019 -0.0663 599 ASP A CB 4460 C CG . ASP A 558 ? 0.3596 0.3740 0.4252 0.0492 -0.1138 -0.0726 599 ASP A CG 4461 O OD1 . ASP A 558 ? 0.4563 0.4721 0.5385 0.0482 -0.1221 -0.0778 599 ASP A OD1 4462 O OD2 . ASP A 558 ? 0.3882 0.3985 0.4371 0.0558 -0.1152 -0.0725 599 ASP A OD2 4463 N N . TYR A 559 ? 0.2682 0.2831 0.3326 0.0304 -0.0874 -0.0578 600 TYR A N 4464 C CA . TYR A 559 ? 0.2572 0.2747 0.3238 0.0239 -0.0776 -0.0520 600 TYR A CA 4465 C C . TYR A 559 ? 0.2662 0.2841 0.3498 0.0186 -0.0794 -0.0528 600 TYR A C 4466 O O . TYR A 559 ? 0.2520 0.2745 0.3466 0.0124 -0.0726 -0.0489 600 TYR A O 4467 C CB . TYR A 559 ? 0.2547 0.2673 0.3026 0.0258 -0.0732 -0.0488 600 TYR A CB 4468 C CG . TYR A 559 ? 0.2579 0.2742 0.3002 0.0229 -0.0631 -0.0430 600 TYR A CG 4469 C CD1 . TYR A 559 ? 0.2354 0.2569 0.2890 0.0164 -0.0567 -0.0394 600 TYR A CD1 4470 C CD2 . TYR A 559 ? 0.2602 0.2743 0.2862 0.0269 -0.0601 -0.0411 600 TYR A CD2 4471 C CE1 . TYR A 559 ? 0.2662 0.2904 0.3137 0.0143 -0.0483 -0.0349 600 TYR A CE1 4472 C CE2 . TYR A 559 ? 0.2443 0.2616 0.2661 0.0243 -0.0514 -0.0363 600 TYR A CE2 4473 C CZ . TYR A 559 ? 0.2570 0.2790 0.2893 0.0181 -0.0463 -0.0336 600 TYR A CZ 4474 O OH . TYR A 559 ? 0.2594 0.2838 0.2868 0.0160 -0.0389 -0.0297 600 TYR A OH 4475 N N . ALA A 560 ? 0.2604 0.2730 0.3458 0.0211 -0.0885 -0.0579 601 ALA A N 4476 C CA . ALA A 560 ? 0.2621 0.2741 0.3641 0.0160 -0.0905 -0.0587 601 ALA A CA 4477 C C . ALA A 560 ? 0.2723 0.2918 0.3978 0.0111 -0.0896 -0.0588 601 ALA A C 4478 O O . ALA A 560 ? 0.2712 0.2932 0.4104 0.0045 -0.0841 -0.0552 601 ALA A O 4479 C CB . ALA A 560 ? 0.2770 0.2817 0.3779 0.0204 -0.1018 -0.0654 601 ALA A CB 4480 N N . VAL A 561 ? 0.2797 0.3026 0.4101 0.0144 -0.0948 -0.0628 602 VAL A N 4481 C CA . VAL A 561 ? 0.2798 0.3104 0.4337 0.0104 -0.0943 -0.0634 602 VAL A CA 4482 C C . VAL A 561 ? 0.2722 0.3093 0.4295 0.0049 -0.0813 -0.0564 602 VAL A C 4483 O O . VAL A 561 ? 0.2736 0.3150 0.4495 -0.0012 -0.0765 -0.0540 602 VAL A O 4484 C CB . VAL A 561 ? 0.2990 0.3321 0.4552 0.0159 -0.1022 -0.0687 602 VAL A CB 4485 C CG1 . VAL A 561 ? 0.3409 0.3836 0.5220 0.0118 -0.1000 -0.0687 602 VAL A CG1 4486 C CG2 . VAL A 561 ? 0.3396 0.3665 0.4963 0.0206 -0.1159 -0.0763 602 VAL A CG2 4487 N N . VAL A 562 ? 0.2586 0.2958 0.3979 0.0074 -0.0755 -0.0532 603 VAL A N 4488 C CA . VAL A 562 ? 0.2489 0.2917 0.3902 0.0029 -0.0637 -0.0473 603 VAL A CA 4489 C C . VAL A 562 ? 0.2425 0.2832 0.3822 -0.0023 -0.0564 -0.0419 603 VAL A C 4490 O O . VAL A 562 ? 0.2381 0.2833 0.3881 -0.0074 -0.0482 -0.0379 603 VAL A O 4491 C CB . VAL A 562 ? 0.2844 0.3287 0.4103 0.0063 -0.0593 -0.0454 603 VAL A CB 4492 C CG1 . VAL A 562 ? 0.2797 0.3254 0.4077 0.0121 -0.0674 -0.0507 603 VAL A CG1 4493 C CG2 . VAL A 562 ? 0.3093 0.3479 0.4134 0.0085 -0.0568 -0.0428 603 VAL A CG2 4494 N N . LEU A 563 ? 0.2317 0.2654 0.3592 -0.0009 -0.0591 -0.0418 604 LEU A N 4495 C CA . LEU A 563 ? 0.2290 0.2600 0.3543 -0.0054 -0.0528 -0.0367 604 LEU A CA 4496 C C . LEU A 563 ? 0.2341 0.2668 0.3810 -0.0110 -0.0521 -0.0360 604 LEU A C 4497 O O . LEU A 563 ? 0.2512 0.2848 0.4014 -0.0158 -0.0437 -0.0304 604 LEU A O 4498 C CB . LEU A 563 ? 0.2365 0.2596 0.3469 -0.0025 -0.0569 -0.0374 604 LEU A CB 4499 C CG . LEU A 563 ? 0.2244 0.2456 0.3133 0.0020 -0.0550 -0.0363 604 LEU A CG 4500 C CD1 . LEU A 563 ? 0.2717 0.2856 0.3490 0.0057 -0.0601 -0.0383 604 LEU A CD1 4501 C CD2 . LEU A 563 ? 0.2553 0.2790 0.3379 -0.0015 -0.0446 -0.0298 604 LEU A CD2 4502 N N . ARG A 564 ? 0.2386 0.2714 0.4009 -0.0103 -0.0609 -0.0415 605 ARG A N 4503 C CA . ARG A 564 ? 0.2510 0.2859 0.4368 -0.0160 -0.0599 -0.0408 605 ARG A CA 4504 C C . ARG A 564 ? 0.2443 0.2879 0.4441 -0.0197 -0.0512 -0.0375 605 ARG A C 4505 O O . ARG A 564 ? 0.2423 0.2874 0.4529 -0.0253 -0.0432 -0.0325 605 ARG A O 4506 C CB . ARG A 564 ? 0.2552 0.2883 0.4556 -0.0143 -0.0723 -0.0483 605 ARG A CB 4507 C CG . ARG A 564 ? 0.2805 0.3166 0.5095 -0.0204 -0.0717 -0.0480 605 ARG A CG 4508 C CD . ARG A 564 ? 0.3197 0.3512 0.5510 -0.0260 -0.0647 -0.0418 605 ARG A CD 4509 N NE . ARG A 564 ? 0.3495 0.3839 0.6093 -0.0321 -0.0631 -0.0409 605 ARG A NE 4510 C CZ . ARG A 564 ? 0.4475 0.4781 0.7235 -0.0333 -0.0721 -0.0455 605 ARG A CZ 4511 N NH1 . ARG A 564 ? 0.4433 0.4668 0.7081 -0.0284 -0.0834 -0.0517 605 ARG A NH1 4512 N NH2 . ARG A 564 ? 0.4500 0.4837 0.7538 -0.0393 -0.0697 -0.0443 605 ARG A NH2 4513 N N . LYS A 565 ? 0.2470 0.2959 0.4462 -0.0164 -0.0525 -0.0403 606 LYS A N 4514 C CA . LYS A 565 ? 0.2511 0.3083 0.4614 -0.0190 -0.0439 -0.0375 606 LYS A CA 4515 C C . LYS A 565 ? 0.2470 0.3039 0.4448 -0.0219 -0.0312 -0.0300 606 LYS A C 4516 O O . LYS A 565 ? 0.2361 0.2970 0.4459 -0.0265 -0.0223 -0.0257 606 LYS A O 4517 C CB A LYS A 565 ? 0.2508 0.3122 0.4578 -0.0139 -0.0477 -0.0415 606 LYS A CB 4518 C CB B LYS A 565 ? 0.2606 0.3219 0.4667 -0.0137 -0.0478 -0.0415 606 LYS A CB 4519 C CG A LYS A 565 ? 0.2568 0.3187 0.4761 -0.0105 -0.0606 -0.0490 606 LYS A CG 4520 C CG B LYS A 565 ? 0.3091 0.3789 0.5253 -0.0153 -0.0395 -0.0395 606 LYS A CG 4521 C CD A LYS A 565 ? 0.3063 0.3763 0.5551 -0.0138 -0.0603 -0.0507 606 LYS A CD 4522 C CD B LYS A 565 ? 0.3658 0.4385 0.5776 -0.0094 -0.0447 -0.0438 606 LYS A CD 4523 C CE A LYS A 565 ? 0.3306 0.4014 0.5902 -0.0094 -0.0742 -0.0589 606 LYS A CE 4524 C CE B LYS A 565 ? 0.3987 0.4668 0.5832 -0.0051 -0.0435 -0.0424 606 LYS A CE 4525 N NZ A LYS A 565 ? 0.3432 0.4091 0.5782 -0.0021 -0.0802 -0.0615 606 LYS A NZ 4526 N NZ B LYS A 565 ? 0.3900 0.4601 0.5703 0.0005 -0.0479 -0.0460 606 LYS A NZ 4527 N N . TYR A 566 ? 0.2274 0.2794 0.4013 -0.0190 -0.0306 -0.0284 607 TYR A N 4528 C CA . TYR A 566 ? 0.2149 0.2661 0.3756 -0.0211 -0.0200 -0.0220 607 TYR A CA 4529 C C . TYR A 566 ? 0.2177 0.2648 0.3821 -0.0258 -0.0157 -0.0171 607 TYR A C 4530 O O . TYR A 566 ? 0.2277 0.2760 0.3912 -0.0289 -0.0059 -0.0117 607 TYR A O 4531 C CB . TYR A 566 ? 0.2245 0.2716 0.3614 -0.0170 -0.0212 -0.0219 607 TYR A CB 4532 C CG . TYR A 566 ? 0.2123 0.2621 0.3429 -0.0122 -0.0245 -0.0256 607 TYR A CG 4533 C CD1 . TYR A 566 ? 0.2198 0.2763 0.3635 -0.0119 -0.0237 -0.0277 607 TYR A CD1 4534 C CD2 . TYR A 566 ? 0.2298 0.2752 0.3419 -0.0078 -0.0282 -0.0268 607 TYR A CD2 4535 C CE1 . TYR A 566 ? 0.2410 0.2990 0.3782 -0.0071 -0.0271 -0.0309 607 TYR A CE1 4536 C CE2 . TYR A 566 ? 0.2244 0.2714 0.3300 -0.0033 -0.0306 -0.0295 607 TYR A CE2 4537 C CZ . TYR A 566 ? 0.2668 0.3197 0.3846 -0.0030 -0.0303 -0.0315 607 TYR A CZ 4538 O OH . TYR A 566 ? 0.2641 0.3176 0.3749 0.0018 -0.0330 -0.0339 607 TYR A OH 4539 N N . ALA A 567 ? 0.2190 0.2607 0.3869 -0.0260 -0.0229 -0.0191 608 ALA A N 4540 C CA . ALA A 567 ? 0.2375 0.2746 0.4103 -0.0305 -0.0192 -0.0144 608 ALA A CA 4541 C C . ALA A 567 ? 0.2419 0.2839 0.4385 -0.0356 -0.0134 -0.0121 608 ALA A C 4542 O O . ALA A 567 ? 0.2462 0.2870 0.4432 -0.0395 -0.0039 -0.0054 608 ALA A O 4543 C CB . ALA A 567 ? 0.2375 0.2675 0.4099 -0.0293 -0.0285 -0.0176 608 ALA A CB 4544 N N . ASP A 568 ? 0.2492 0.2964 0.4654 -0.0355 -0.0188 -0.0173 609 ASP A N 4545 C CA . ASP A 568 ? 0.2625 0.3156 0.5040 -0.0404 -0.0129 -0.0153 609 ASP A CA 4546 C C . ASP A 568 ? 0.2524 0.3105 0.4895 -0.0417 0.0002 -0.0097 609 ASP A C 4547 O O . ASP A 568 ? 0.2457 0.3052 0.4938 -0.0463 0.0100 -0.0040 609 ASP A O 4548 C CB . ASP A 568 ? 0.2659 0.3249 0.5277 -0.0390 -0.0215 -0.0225 609 ASP A CB 4549 C CG . ASP A 568 ? 0.3257 0.3799 0.5970 -0.0384 -0.0342 -0.0283 609 ASP A CG 4550 O OD1 . ASP A 568 ? 0.3491 0.3961 0.6180 -0.0403 -0.0355 -0.0265 609 ASP A OD1 4551 O OD2 . ASP A 568 ? 0.4046 0.4626 0.6877 -0.0357 -0.0436 -0.0353 609 ASP A OD2 4552 N N . LYS A 569 ? 0.2423 0.3028 0.4631 -0.0374 0.0004 -0.0114 610 LYS A N 4553 C CA . LYS A 569 ? 0.2493 0.3147 0.4660 -0.0378 0.0115 -0.0076 610 LYS A CA 4554 C C . LYS A 569 ? 0.2532 0.3134 0.4537 -0.0398 0.0211 -0.0002 610 LYS A C 4555 O O . LYS A 569 ? 0.2706 0.3330 0.4769 -0.0427 0.0320 0.0049 610 LYS A O 4556 C CB . LYS A 569 ? 0.2570 0.3253 0.4607 -0.0326 0.0083 -0.0117 610 LYS A CB 4557 C CG . LYS A 569 ? 0.3082 0.3812 0.5073 -0.0324 0.0189 -0.0088 610 LYS A CG 4558 C CD . LYS A 569 ? 0.3848 0.4587 0.5694 -0.0273 0.0149 -0.0127 610 LYS A CD 4559 C CE . LYS A 569 ? 0.4404 0.5204 0.6260 -0.0264 0.0233 -0.0120 610 LYS A CE 4560 N NZ . LYS A 569 ? 0.4401 0.5170 0.6023 -0.0224 0.0223 -0.0129 610 LYS A NZ 4561 N N . ILE A 570 ? 0.2429 0.2958 0.4233 -0.0379 0.0171 0.0004 611 ILE A N 4562 C CA . ILE A 570 ? 0.2412 0.2885 0.4049 -0.0391 0.0247 0.0071 611 ILE A CA 4563 C C . ILE A 570 ? 0.2494 0.2932 0.4253 -0.0440 0.0298 0.0127 611 ILE A C 4564 O O . ILE A 570 ? 0.2436 0.2858 0.4145 -0.0460 0.0402 0.0192 611 ILE A O 4565 C CB . ILE A 570 ? 0.2448 0.2860 0.3855 -0.0356 0.0187 0.0060 611 ILE A CB 4566 C CG1 . ILE A 570 ? 0.2761 0.3129 0.3982 -0.0359 0.0264 0.0121 611 ILE A CG1 4567 C CG2 . ILE A 570 ? 0.2494 0.2851 0.3935 -0.0355 0.0093 0.0036 611 ILE A CG2 4568 C CD1 . ILE A 570 ? 0.3199 0.3614 0.4345 -0.0344 0.0334 0.0126 611 ILE A CD1 4569 N N . TYR A 571 ? 0.2470 0.2890 0.4392 -0.0459 0.0226 0.0101 612 TYR A N 4570 C CA . TYR A 571 ? 0.2727 0.3118 0.4806 -0.0508 0.0268 0.0148 612 TYR A CA 4571 C C . TYR A 571 ? 0.2660 0.3118 0.4913 -0.0542 0.0381 0.0186 612 TYR A C 4572 O O . TYR A 571 ? 0.2762 0.3191 0.5021 -0.0574 0.0485 0.0261 612 TYR A O 4573 C CB . TYR A 571 ? 0.2587 0.2956 0.4835 -0.0517 0.0155 0.0095 612 TYR A CB 4574 C CG . TYR A 571 ? 0.3084 0.3432 0.5550 -0.0573 0.0194 0.0136 612 TYR A CG 4575 C CD1 . TYR A 571 ? 0.3885 0.4142 0.6282 -0.0595 0.0222 0.0196 612 TYR A CD1 4576 C CD2 . TYR A 571 ? 0.3843 0.4262 0.6588 -0.0604 0.0208 0.0118 612 TYR A CD2 4577 C CE1 . TYR A 571 ? 0.4292 0.4524 0.6904 -0.0649 0.0263 0.0239 612 TYR A CE1 4578 C CE2 . TYR A 571 ? 0.4369 0.4772 0.7343 -0.0661 0.0250 0.0159 612 TYR A CE2 4579 C CZ . TYR A 571 ? 0.4625 0.4931 0.7522 -0.0683 0.0280 0.0221 612 TYR A CZ 4580 O OH . TYR A 571 ? 0.5522 0.5806 0.8650 -0.0739 0.0325 0.0264 612 TYR A OH 4581 N N . SER A 572 ? 0.2580 0.3127 0.4960 -0.0530 0.0367 0.0136 613 SER A N 4582 C CA . SER A 572 ? 0.2842 0.3462 0.5410 -0.0559 0.0472 0.0164 613 SER A CA 4583 C C . SER A 572 ? 0.2791 0.3406 0.5179 -0.0552 0.0603 0.0227 613 SER A C 4584 O O . SER A 572 ? 0.2953 0.3583 0.5440 -0.0584 0.0718 0.0286 613 SER A O 4585 C CB . SER A 572 ? 0.2703 0.3418 0.5443 -0.0542 0.0419 0.0092 613 SER A CB 4586 O OG A SER A 572 ? 0.3083 0.3801 0.6023 -0.0554 0.0308 0.0039 613 SER A OG 4587 O OG B SER A 572 ? 0.2950 0.3695 0.5515 -0.0496 0.0424 0.0069 613 SER A OG 4588 N N . ILE A 573 ? 0.2737 0.3327 0.4862 -0.0509 0.0583 0.0215 614 ILE A N 4589 C CA . ILE A 573 ? 0.2839 0.3413 0.4771 -0.0496 0.0691 0.0266 614 ILE A CA 4590 C C . ILE A 573 ? 0.2997 0.3487 0.4844 -0.0522 0.0759 0.0348 614 ILE A C 4591 O O . ILE A 573 ? 0.3138 0.3624 0.4964 -0.0535 0.0883 0.0411 614 ILE A O 4592 C CB . ILE A 573 ? 0.2857 0.3417 0.4539 -0.0446 0.0641 0.0230 614 ILE A CB 4593 C CG1 . ILE A 573 ? 0.2664 0.3308 0.4437 -0.0420 0.0601 0.0162 614 ILE A CG1 4594 C CG2 . ILE A 573 ? 0.3085 0.3606 0.4540 -0.0432 0.0741 0.0285 614 ILE A CG2 4595 C CD1 . ILE A 573 ? 0.2914 0.3545 0.4481 -0.0373 0.0533 0.0118 614 ILE A CD1 4596 N N . SER A 574 ? 0.2902 0.3319 0.4689 -0.0525 0.0678 0.0348 615 SER A N 4597 C CA . SER A 574 ? 0.2977 0.3304 0.4668 -0.0544 0.0728 0.0425 615 SER A CA 4598 C C . SER A 574 ? 0.3138 0.3469 0.5051 -0.0595 0.0814 0.0480 615 SER A C 4599 O O . SER A 574 ? 0.3044 0.3323 0.4886 -0.0609 0.0922 0.0563 615 SER A O 4600 C CB . SER A 574 ? 0.2993 0.3249 0.4612 -0.0536 0.0613 0.0403 615 SER A CB 4601 O OG . SER A 574 ? 0.3174 0.3337 0.4674 -0.0547 0.0657 0.0477 615 SER A OG 4602 N N . MET A 575 ? 0.3100 0.3490 0.5287 -0.0620 0.0768 0.0435 616 MET A N 4603 C CA . MET A 575 ? 0.3351 0.3756 0.5808 -0.0674 0.0839 0.0479 616 MET A CA 4604 C C . MET A 575 ? 0.3490 0.3956 0.6027 -0.0687 0.0989 0.0527 616 MET A C 4605 O O . MET A 575 ? 0.3566 0.4046 0.6331 -0.0733 0.1069 0.0574 616 MET A O 4606 C CB . MET A 575 ? 0.3424 0.3872 0.6158 -0.0695 0.0729 0.0408 616 MET A CB 4607 C CG . MET A 575 ? 0.3663 0.4022 0.6385 -0.0703 0.0625 0.0396 616 MET A CG 4608 S SD . MET A 575 ? 0.4849 0.5103 0.7597 -0.0753 0.0721 0.0508 616 MET A SD 4609 C CE . MET A 575 ? 0.4526 0.4855 0.7663 -0.0814 0.0813 0.0535 616 MET A CE 4610 N N . LYS A 576 ? 0.3591 0.4088 0.5941 -0.0646 0.1032 0.0518 617 LYS A N 4611 C CA . LYS A 576 ? 0.3844 0.4372 0.6186 -0.0648 0.1191 0.0576 617 LYS A CA 4612 C C . LYS A 576 ? 0.3870 0.4297 0.6052 -0.0659 0.1298 0.0680 617 LYS A C 4613 O O . LYS A 576 ? 0.3822 0.4256 0.6019 -0.0667 0.1444 0.0745 617 LYS A O 4614 C CB . LYS A 576 ? 0.4028 0.4601 0.6190 -0.0596 0.1199 0.0534 617 LYS A CB 4615 C CG . LYS A 576 ? 0.4296 0.4974 0.6633 -0.0583 0.1117 0.0442 617 LYS A CG 4616 C CD . LYS A 576 ? 0.5531 0.6299 0.8206 -0.0619 0.1184 0.0445 617 LYS A CD 4617 C CE . LYS A 576 ? 0.5948 0.6818 0.8800 -0.0601 0.1095 0.0353 617 LYS A CE 4618 N NZ . LYS A 576 ? 0.6199 0.7059 0.9154 -0.0608 0.0933 0.0290 617 LYS A NZ 4619 N N . HIS A 577 ? 0.3703 0.4032 0.5732 -0.0656 0.1225 0.0696 618 HIS A N 4620 C CA . HIS A 577 ? 0.3795 0.4014 0.5628 -0.0655 0.1303 0.0790 618 HIS A CA 4621 C C . HIS A 577 ? 0.3681 0.3824 0.5630 -0.0695 0.1260 0.0825 618 HIS A C 4622 O O . HIS A 577 ? 0.3622 0.3675 0.5387 -0.0679 0.1194 0.0837 618 HIS A O 4623 C CB . HIS A 577 ? 0.3820 0.3980 0.5310 -0.0603 0.1251 0.0777 618 HIS A CB 4624 C CG . HIS A 577 ? 0.4142 0.4368 0.5513 -0.0560 0.1250 0.0721 618 HIS A CG 4625 N ND1 . HIS A 577 ? 0.4343 0.4570 0.5568 -0.0535 0.1368 0.0758 618 HIS A ND1 4626 C CD2 . HIS A 577 ? 0.4428 0.4715 0.5797 -0.0535 0.1146 0.0630 618 HIS A CD2 4627 C CE1 . HIS A 577 ? 0.4269 0.4556 0.5420 -0.0500 0.1334 0.0690 618 HIS A CE1 4628 N NE2 . HIS A 577 ? 0.4493 0.4818 0.5731 -0.0500 0.1202 0.0615 618 HIS A NE2 4629 N N . PRO A 578 ? 0.3704 0.3882 0.5967 -0.0747 0.1296 0.0841 619 PRO A N 4630 C CA . PRO A 578 ? 0.3550 0.3660 0.5952 -0.0786 0.1237 0.0858 619 PRO A CA 4631 C C . PRO A 578 ? 0.3701 0.3682 0.5922 -0.0788 0.1302 0.0960 619 PRO A C 4632 O O . PRO A 578 ? 0.3694 0.3594 0.5872 -0.0791 0.1211 0.0957 619 PRO A O 4633 C CB . PRO A 578 ? 0.3787 0.3966 0.6569 -0.0843 0.1292 0.0866 619 PRO A CB 4634 C CG . PRO A 578 ? 0.3861 0.4123 0.6658 -0.0834 0.1430 0.0890 619 PRO A CG 4635 C CD . PRO A 578 ? 0.3566 0.3852 0.6088 -0.0772 0.1378 0.0832 619 PRO A CD 4636 N N . GLN A 579 ? 0.3750 0.3704 0.5855 -0.0783 0.1455 0.1048 620 GLN A N 4637 C CA A GLN A 579 ? 0.3984 0.3805 0.5903 -0.0780 0.1521 0.1152 620 GLN A CA 4638 C CA B GLN A 579 ? 0.3964 0.3787 0.5901 -0.0783 0.1517 0.1150 620 GLN A CA 4639 C C . GLN A 579 ? 0.3966 0.3712 0.5573 -0.0730 0.1419 0.1131 620 GLN A C 4640 O O . GLN A 579 ? 0.4028 0.3670 0.5566 -0.0734 0.1377 0.1170 620 GLN A O 4641 C CB A GLN A 579 ? 0.4194 0.3996 0.5998 -0.0770 0.1703 0.1247 620 GLN A CB 4642 C CB B GLN A 579 ? 0.4212 0.4013 0.6084 -0.0783 0.1707 0.1253 620 GLN A CB 4643 C CG A GLN A 579 ? 0.4658 0.4311 0.6284 -0.0768 0.1776 0.1365 620 GLN A CG 4644 C CG B GLN A 579 ? 0.4224 0.4118 0.6413 -0.0829 0.1832 0.1276 620 GLN A CG 4645 C CD A GLN A 579 ? 0.4685 0.4273 0.6538 -0.0824 0.1749 0.1404 620 GLN A CD 4646 C CD B GLN A 579 ? 0.4412 0.4375 0.7012 -0.0890 0.1767 0.1227 620 GLN A CD 4647 O OE1 A GLN A 579 ? 0.4295 0.3800 0.6057 -0.0816 0.1641 0.1396 620 GLN A OE1 4648 O OE1 B GLN A 579 ? 0.4135 0.4034 0.6850 -0.0923 0.1696 0.1234 620 GLN A OE1 4649 N NE2 A GLN A 579 ? 0.5063 0.4691 0.7226 -0.0880 0.1844 0.1443 620 GLN A NE2 4650 N NE2 B GLN A 579 ? 0.4564 0.4657 0.7392 -0.0903 0.1798 0.1178 620 GLN A NE2 4651 N N . GLU A 580 ? 0.3824 0.3622 0.5249 -0.0683 0.1377 0.1068 621 GLU A N 4652 C CA . GLU A 580 ? 0.3847 0.3583 0.4994 -0.0636 0.1281 0.1044 621 GLU A CA 4653 C C . GLU A 580 ? 0.3649 0.3377 0.4887 -0.0644 0.1127 0.0978 621 GLU A C 4654 O O . GLU A 580 ? 0.3856 0.3498 0.4933 -0.0623 0.1061 0.0991 621 GLU A O 4655 C CB . GLU A 580 ? 0.3878 0.3671 0.4827 -0.0586 0.1270 0.0991 621 GLU A CB 4656 C CG . GLU A 580 ? 0.4655 0.4421 0.5426 -0.0563 0.1417 0.1063 621 GLU A CG 4657 C CD . GLU A 580 ? 0.5101 0.4942 0.6072 -0.0591 0.1548 0.1087 621 GLU A CD 4658 O OE1 . GLU A 580 ? 0.5194 0.5133 0.6439 -0.0622 0.1521 0.1031 621 GLU A OE1 4659 O OE2 . GLU A 580 ? 0.6172 0.5970 0.7024 -0.0579 0.1684 0.1166 621 GLU A OE2 4660 N N . MET A 581 ? 0.3441 0.3257 0.4926 -0.0668 0.1066 0.0903 622 MET A N 4661 C CA . MET A 581 ? 0.3312 0.3114 0.4879 -0.0671 0.0922 0.0837 622 MET A CA 4662 C C . MET A 581 ? 0.3442 0.3142 0.5092 -0.0704 0.0921 0.0897 622 MET A C 4663 O O . MET A 581 ? 0.3273 0.2911 0.4847 -0.0688 0.0820 0.0874 622 MET A O 4664 C CB . MET A 581 ? 0.3227 0.3135 0.5038 -0.0686 0.0854 0.0745 622 MET A CB 4665 C CG . MET A 581 ? 0.3203 0.3199 0.4907 -0.0646 0.0832 0.0679 622 MET A CG 4666 S SD . MET A 581 ? 0.3320 0.3430 0.5297 -0.0656 0.0741 0.0573 622 MET A SD 4667 C CE . MET A 581 ? 0.3250 0.3299 0.5231 -0.0647 0.0578 0.0513 622 MET A CE 4668 N N . LYS A 582 ? 0.3437 0.3117 0.5240 -0.0748 0.1037 0.0976 623 LYS A N 4669 C CA . LYS A 582 ? 0.3701 0.3274 0.5587 -0.0782 0.1048 0.1045 623 LYS A CA 4670 C C . LYS A 582 ? 0.3919 0.3372 0.5497 -0.0744 0.1063 0.1115 623 LYS A C 4671 O O . LYS A 582 ? 0.3888 0.3258 0.5417 -0.0737 0.0979 0.1114 623 LYS A O 4672 C CB . LYS A 582 ? 0.3810 0.3389 0.5931 -0.0837 0.1185 0.1122 623 LYS A CB 4673 C CG . LYS A 582 ? 0.3791 0.3481 0.6255 -0.0878 0.1158 0.1053 623 LYS A CG 4674 C CD . LYS A 582 ? 0.4324 0.4025 0.7037 -0.0935 0.1302 0.1133 623 LYS A CD 4675 C CE . LYS A 582 ? 0.5029 0.4850 0.8092 -0.0971 0.1256 0.1052 623 LYS A CE 4676 N NZ . LYS A 582 ? 0.5595 0.5517 0.8805 -0.0989 0.1391 0.1078 623 LYS A NZ 4677 N N . THR A 583 ? 0.4117 0.3564 0.5487 -0.0717 0.1166 0.1171 624 THR A N 4678 C CA . THR A 583 ? 0.4448 0.3784 0.5517 -0.0677 0.1188 0.1241 624 THR A CA 4679 C C . THR A 583 ? 0.4296 0.3603 0.5173 -0.0630 0.1050 0.1182 624 THR A C 4680 O O . THR A 583 ? 0.4408 0.3607 0.5166 -0.0616 0.1019 0.1228 624 THR A O 4681 C CB . THR A 583 ? 0.4651 0.3997 0.5519 -0.0647 0.1312 0.1291 624 THR A CB 4682 O OG1 . THR A 583 ? 0.5011 0.4359 0.6045 -0.0688 0.1457 0.1369 624 THR A OG1 4683 C CG2 . THR A 583 ? 0.5275 0.4501 0.5809 -0.0597 0.1318 0.1356 624 THR A CG2 4684 N N . TYR A 584 ? 0.4067 0.3469 0.4926 -0.0607 0.0970 0.1083 625 TYR A N 4685 C CA . TYR A 584 ? 0.4033 0.3422 0.4715 -0.0561 0.0850 0.1024 625 TYR A CA 4686 C C . TYR A 584 ? 0.3850 0.3266 0.4699 -0.0572 0.0723 0.0941 625 TYR A C 4687 O O . TYR A 584 ? 0.3839 0.3259 0.4575 -0.0535 0.0623 0.0882 625 TYR A O 4688 C CB . TYR A 584 ? 0.3977 0.3437 0.4481 -0.0519 0.0849 0.0977 625 TYR A CB 4689 C CG . TYR A 584 ? 0.4419 0.3839 0.4738 -0.0501 0.0967 0.1056 625 TYR A CG 4690 C CD1 . TYR A 584 ? 0.4971 0.4275 0.5071 -0.0472 0.0977 0.1127 625 TYR A CD1 4691 C CD2 . TYR A 584 ? 0.4564 0.4053 0.4925 -0.0509 0.1070 0.1062 625 TYR A CD2 4692 C CE1 . TYR A 584 ? 0.5308 0.4561 0.5218 -0.0450 0.1088 0.1203 625 TYR A CE1 4693 C CE2 . TYR A 584 ? 0.5134 0.4578 0.5312 -0.0488 0.1185 0.1135 625 TYR A CE2 4694 C CZ . TYR A 584 ? 0.5451 0.4774 0.5394 -0.0457 0.1192 0.1205 625 TYR A CZ 4695 O OH . TYR A 584 ? 0.5908 0.5175 0.5653 -0.0430 0.1307 0.1280 625 TYR A OH 4696 N N . SER A 585 ? 0.3654 0.3083 0.4771 -0.0621 0.0728 0.0936 626 SER A N 4697 C CA . SER A 585 ? 0.3591 0.3023 0.4861 -0.0629 0.0606 0.0862 626 SER A CA 4698 C C . SER A 585 ? 0.3355 0.2881 0.4594 -0.0596 0.0516 0.0756 626 SER A C 4699 O O . SER A 585 ? 0.3340 0.2848 0.4498 -0.0564 0.0411 0.0701 626 SER A O 4700 C CB A SER A 585 ? 0.3647 0.2963 0.4823 -0.0613 0.0544 0.0889 626 SER A CB 4701 C CB B SER A 585 ? 0.3713 0.3029 0.4870 -0.0610 0.0547 0.0891 626 SER A CB 4702 O OG A SER A 585 ? 0.3378 0.2602 0.4617 -0.0648 0.0624 0.0986 626 SER A OG 4703 O OG B SER A 585 ? 0.4019 0.3322 0.5326 -0.0618 0.0440 0.0827 626 SER A OG 4704 N N . VAL A 586 ? 0.3321 0.2945 0.4614 -0.0601 0.0562 0.0729 627 VAL A N 4705 C CA . VAL A 586 ? 0.3258 0.2967 0.4500 -0.0568 0.0496 0.0642 627 VAL A CA 4706 C C . VAL A 586 ? 0.3327 0.3086 0.4804 -0.0586 0.0416 0.0565 627 VAL A C 4707 O O . VAL A 586 ? 0.3534 0.3346 0.5227 -0.0623 0.0460 0.0565 627 VAL A O 4708 C CB . VAL A 586 ? 0.3318 0.3106 0.4512 -0.0561 0.0585 0.0649 627 VAL A CB 4709 C CG1 . VAL A 586 ? 0.3044 0.2913 0.4179 -0.0525 0.0513 0.0560 627 VAL A CG1 4710 C CG2 . VAL A 586 ? 0.3574 0.3303 0.4554 -0.0547 0.0679 0.0733 627 VAL A CG2 4711 N N . SER A 587 ? 0.3367 0.3106 0.4806 -0.0558 0.0300 0.0502 628 SER A N 4712 C CA . SER A 587 ? 0.3375 0.3141 0.5004 -0.0565 0.0205 0.0423 628 SER A CA 4713 C C . SER A 587 ? 0.3044 0.2876 0.4593 -0.0520 0.0130 0.0338 628 SER A C 4714 O O . SER A 587 ? 0.3021 0.2836 0.4363 -0.0478 0.0101 0.0328 628 SER A O 4715 C CB . SER A 587 ? 0.3466 0.3139 0.5116 -0.0563 0.0125 0.0413 628 SER A CB 4716 O OG . SER A 587 ? 0.4028 0.3728 0.5876 -0.0571 0.0039 0.0334 628 SER A OG 4717 N N . PHE A 588 ? 0.2996 0.2900 0.4717 -0.0529 0.0099 0.0279 629 PHE A N 4718 C CA . PHE A 588 ? 0.2808 0.2766 0.4476 -0.0485 0.0018 0.0196 629 PHE A CA 4719 C C . PHE A 588 ? 0.2769 0.2689 0.4506 -0.0468 -0.0104 0.0125 629 PHE A C 4720 O O . PHE A 588 ? 0.2663 0.2618 0.4368 -0.0429 -0.0179 0.0053 629 PHE A O 4721 C CB . PHE A 588 ? 0.2773 0.2830 0.4564 -0.0494 0.0050 0.0170 629 PHE A CB 4722 C CG . PHE A 588 ? 0.2805 0.2904 0.4466 -0.0488 0.0149 0.0215 629 PHE A CG 4723 C CD1 . PHE A 588 ? 0.2797 0.2937 0.4305 -0.0445 0.0129 0.0178 629 PHE A CD1 4724 C CD2 . PHE A 588 ? 0.2981 0.3069 0.4664 -0.0523 0.0264 0.0294 629 PHE A CD2 4725 C CE1 . PHE A 588 ? 0.2801 0.2973 0.4186 -0.0438 0.0215 0.0213 629 PHE A CE1 4726 C CE2 . PHE A 588 ? 0.3033 0.3153 0.4583 -0.0512 0.0352 0.0330 629 PHE A CE2 4727 C CZ . PHE A 588 ? 0.2801 0.2963 0.4201 -0.0469 0.0324 0.0285 629 PHE A CZ 4728 N N . ASP A 589 ? 0.2861 0.2703 0.4674 -0.0491 -0.0124 0.0147 630 ASP A N 4729 C CA . ASP A 589 ? 0.2994 0.2794 0.4885 -0.0474 -0.0241 0.0075 630 ASP A CA 4730 C C . ASP A 589 ? 0.3000 0.2785 0.4691 -0.0409 -0.0317 0.0020 630 ASP A C 4731 O O . ASP A 589 ? 0.3005 0.2801 0.4731 -0.0378 -0.0409 -0.0060 630 ASP A O 4732 C CB . ASP A 589 ? 0.3241 0.2946 0.5230 -0.0508 -0.0247 0.0111 630 ASP A CB 4733 C CG . ASP A 589 ? 0.3816 0.3537 0.6071 -0.0572 -0.0198 0.0142 630 ASP A CG 4734 O OD1 . ASP A 589 ? 0.4140 0.3948 0.6529 -0.0590 -0.0171 0.0126 630 ASP A OD1 4735 O OD2 . ASP A 589 ? 0.4378 0.4020 0.6719 -0.0605 -0.0186 0.0184 630 ASP A OD2 4736 N N . SER A 590 ? 0.2779 0.2539 0.4265 -0.0388 -0.0279 0.0063 631 SER A N 4737 C CA . SER A 590 ? 0.2778 0.2529 0.4083 -0.0328 -0.0338 0.0019 631 SER A CA 4738 C C . SER A 590 ? 0.2695 0.2524 0.3964 -0.0296 -0.0359 -0.0035 631 SER A C 4739 O O . SER A 590 ? 0.2540 0.2360 0.3747 -0.0249 -0.0435 -0.0098 631 SER A O 4740 C CB . SER A 590 ? 0.3060 0.2776 0.4170 -0.0312 -0.0293 0.0075 631 SER A CB 4741 O OG . SER A 590 ? 0.3095 0.2865 0.4138 -0.0325 -0.0208 0.0122 631 SER A OG 4742 N N . LEU A 591 ? 0.2471 0.2370 0.3769 -0.0318 -0.0291 -0.0010 632 LEU A N 4743 C CA . LEU A 591 ? 0.2507 0.2477 0.3774 -0.0287 -0.0309 -0.0058 632 LEU A CA 4744 C C . LEU A 591 ? 0.2462 0.2451 0.3884 -0.0279 -0.0392 -0.0131 632 LEU A C 4745 O O . LEU A 591 ? 0.2457 0.2456 0.3809 -0.0230 -0.0458 -0.0190 632 LEU A O 4746 C CB . LEU A 591 ? 0.2504 0.2541 0.3769 -0.0310 -0.0215 -0.0016 632 LEU A CB 4747 C CG . LEU A 591 ? 0.2361 0.2467 0.3590 -0.0278 -0.0229 -0.0060 632 LEU A CG 4748 C CD1 . LEU A 591 ? 0.2317 0.2407 0.3346 -0.0225 -0.0264 -0.0083 632 LEU A CD1 4749 C CD2 . LEU A 591 ? 0.2692 0.2852 0.3920 -0.0302 -0.0131 -0.0015 632 LEU A CD2 4750 N N . PHE A 592 ? 0.2422 0.2411 0.4053 -0.0324 -0.0391 -0.0126 633 PHE A N 4751 C CA . PHE A 592 ? 0.2548 0.2552 0.4340 -0.0315 -0.0482 -0.0201 633 PHE A CA 4752 C C . PHE A 592 ? 0.2499 0.2429 0.4230 -0.0274 -0.0587 -0.0259 633 PHE A C 4753 O O . PHE A 592 ? 0.2837 0.2776 0.4576 -0.0233 -0.0675 -0.0333 633 PHE A O 4754 C CB . PHE A 592 ? 0.2518 0.2538 0.4568 -0.0377 -0.0454 -0.0180 633 PHE A CB 4755 C CG . PHE A 592 ? 0.2762 0.2872 0.4901 -0.0405 -0.0370 -0.0149 633 PHE A CG 4756 C CD1 . PHE A 592 ? 0.2962 0.3145 0.5171 -0.0382 -0.0411 -0.0206 633 PHE A CD1 4757 C CD2 . PHE A 592 ? 0.3089 0.3207 0.5233 -0.0448 -0.0250 -0.0065 633 PHE A CD2 4758 C CE1 . PHE A 592 ? 0.3000 0.3269 0.5296 -0.0404 -0.0331 -0.0181 633 PHE A CE1 4759 C CE2 . PHE A 592 ? 0.3208 0.3410 0.5429 -0.0469 -0.0164 -0.0038 633 PHE A CE2 4760 C CZ . PHE A 592 ? 0.3001 0.3279 0.5302 -0.0447 -0.0205 -0.0098 633 PHE A CZ 4761 N N . SER A 593 ? 0.2494 0.2348 0.4155 -0.0278 -0.0581 -0.0228 634 SER A N 4762 C CA . SER A 593 ? 0.2620 0.2399 0.4207 -0.0233 -0.0674 -0.0283 634 SER A CA 4763 C C . SER A 593 ? 0.2656 0.2448 0.4036 -0.0165 -0.0701 -0.0319 634 SER A C 4764 O O . SER A 593 ? 0.2816 0.2582 0.4161 -0.0114 -0.0791 -0.0391 634 SER A O 4765 C CB . SER A 593 ? 0.2878 0.2578 0.4415 -0.0248 -0.0647 -0.0232 634 SER A CB 4766 O OG . SER A 593 ? 0.3156 0.2783 0.4612 -0.0199 -0.0731 -0.0285 634 SER A OG 4767 N N . ALA A 594 ? 0.2481 0.2306 0.3717 -0.0160 -0.0624 -0.0268 635 ALA A N 4768 C CA . ALA A 594 ? 0.2453 0.2294 0.3506 -0.0101 -0.0636 -0.0292 635 ALA A CA 4769 C C . ALA A 594 ? 0.2561 0.2451 0.3646 -0.0072 -0.0683 -0.0350 635 ALA A C 4770 O O . ALA A 594 ? 0.2694 0.2562 0.3673 -0.0011 -0.0746 -0.0403 635 ALA A O 4771 C CB . ALA A 594 ? 0.2406 0.2282 0.3331 -0.0110 -0.0545 -0.0228 635 ALA A CB 4772 N N . VAL A 595 ? 0.2567 0.2519 0.3796 -0.0112 -0.0654 -0.0339 636 VAL A N 4773 C CA . VAL A 595 ? 0.2551 0.2555 0.3830 -0.0086 -0.0698 -0.0390 636 VAL A CA 4774 C C . VAL A 595 ? 0.2725 0.2686 0.4087 -0.0058 -0.0815 -0.0468 636 VAL A C 4775 O O . VAL A 595 ? 0.2801 0.2760 0.4091 -0.0001 -0.0882 -0.0524 636 VAL A O 4776 C CB . VAL A 595 ? 0.2532 0.2614 0.3969 -0.0136 -0.0637 -0.0361 636 VAL A CB 4777 C CG1 . VAL A 595 ? 0.2840 0.2971 0.4353 -0.0108 -0.0696 -0.0419 636 VAL A CG1 4778 C CG2 . VAL A 595 ? 0.2432 0.2551 0.3744 -0.0146 -0.0533 -0.0298 636 VAL A CG2 4779 N N . LYS A 596 ? 0.2834 0.2756 0.4346 -0.0096 -0.0840 -0.0472 637 LYS A N 4780 C CA . LYS A 596 ? 0.2925 0.2794 0.4516 -0.0069 -0.0961 -0.0552 637 LYS A CA 4781 C C . LYS A 596 ? 0.2959 0.2757 0.4339 0.0005 -0.1019 -0.0594 637 LYS A C 4782 O O . LYS A 596 ? 0.3002 0.2777 0.4344 0.0063 -0.1114 -0.0668 637 LYS A O 4783 C CB . LYS A 596 ? 0.3053 0.2880 0.4830 -0.0126 -0.0966 -0.0538 637 LYS A CB 4784 C CG . LYS A 596 ? 0.3673 0.3438 0.5556 -0.0105 -0.1094 -0.0624 637 LYS A CG 4785 C CD . LYS A 596 ? 0.4355 0.4080 0.6442 -0.0170 -0.1088 -0.0601 637 LYS A CD 4786 C CE . LYS A 596 ? 0.4879 0.4533 0.7074 -0.0148 -0.1224 -0.0693 637 LYS A CE 4787 N NZ . LYS A 596 ? 0.5364 0.4927 0.7341 -0.0085 -0.1269 -0.0723 637 LYS A NZ 4788 N N . ASN A 597 ? 0.2861 0.2623 0.4098 0.0009 -0.0963 -0.0547 638 ASN A N 4789 C CA . ASN A 597 ? 0.3010 0.2711 0.4052 0.0079 -0.1002 -0.0579 638 ASN A CA 4790 C C . ASN A 597 ? 0.2990 0.2723 0.3874 0.0138 -0.1003 -0.0598 638 ASN A C 4791 O O . ASN A 597 ? 0.3108 0.2794 0.3877 0.0206 -0.1070 -0.0654 638 ASN A O 4792 C CB . ASN A 597 ? 0.2960 0.2626 0.3897 0.0069 -0.0936 -0.0521 638 ASN A CB 4793 C CG . ASN A 597 ? 0.2984 0.2590 0.4042 0.0029 -0.0953 -0.0512 638 ASN A CG 4794 O OD1 . ASN A 597 ? 0.3195 0.2773 0.4408 0.0015 -0.1024 -0.0558 638 ASN A OD1 4795 N ND2 . ASN A 597 ? 0.2988 0.2569 0.3981 0.0013 -0.0892 -0.0452 638 ASN A ND2 4796 N N . PHE A 598 ? 0.2769 0.2576 0.3639 0.0114 -0.0924 -0.0548 639 PHE A N 4797 C CA . PHE A 598 ? 0.2754 0.2592 0.3492 0.0163 -0.0917 -0.0557 639 PHE A CA 4798 C C . PHE A 598 ? 0.2914 0.2749 0.3706 0.0202 -0.1014 -0.0631 639 PHE A C 4799 O O . PHE A 598 ? 0.2965 0.2769 0.3608 0.0273 -0.1058 -0.0669 639 PHE A O 4800 C CB . PHE A 598 ? 0.2724 0.2641 0.3475 0.0123 -0.0823 -0.0497 639 PHE A CB 4801 C CG . PHE A 598 ? 0.2589 0.2530 0.3191 0.0172 -0.0803 -0.0496 639 PHE A CG 4802 C CD1 . PHE A 598 ? 0.2762 0.2705 0.3222 0.0179 -0.0731 -0.0449 639 PHE A CD1 4803 C CD2 . PHE A 598 ? 0.2371 0.2329 0.2981 0.0210 -0.0856 -0.0541 639 PHE A CD2 4804 C CE1 . PHE A 598 ? 0.2890 0.2850 0.3224 0.0220 -0.0708 -0.0444 639 PHE A CE1 4805 C CE2 . PHE A 598 ? 0.2751 0.2722 0.3222 0.0255 -0.0834 -0.0534 639 PHE A CE2 4806 C CZ . PHE A 598 ? 0.2725 0.2698 0.3060 0.0258 -0.0755 -0.0484 639 PHE A CZ 4807 N N . THR A 599 ? 0.2855 0.2721 0.3858 0.0157 -0.1046 -0.0649 640 THR A N 4808 C CA . THR A 599 ? 0.3062 0.2932 0.4150 0.0191 -0.1150 -0.0723 640 THR A CA 4809 C C . THR A 599 ? 0.3334 0.3114 0.4336 0.0255 -0.1258 -0.0796 640 THR A C 4810 O O . THR A 599 ? 0.3340 0.3096 0.4231 0.0328 -0.1327 -0.0849 640 THR A O 4811 C CB . THR A 599 ? 0.3075 0.2995 0.4435 0.0123 -0.1159 -0.0725 640 THR A CB 4812 O OG1 . THR A 599 ? 0.3008 0.3009 0.4418 0.0071 -0.1048 -0.0654 640 THR A OG1 4813 C CG2 . THR A 599 ? 0.3231 0.3170 0.4699 0.0155 -0.1267 -0.0801 640 THR A CG2 4814 N N . GLU A 600 ? 0.3223 0.2945 0.4263 0.0234 -0.1271 -0.0800 641 GLU A N 4815 C CA . GLU A 600 ? 0.3574 0.3201 0.4533 0.0295 -0.1370 -0.0871 641 GLU A CA 4816 C C . GLU A 600 ? 0.3522 0.3102 0.4202 0.0378 -0.1357 -0.0876 641 GLU A C 4817 O O . GLU A 600 ? 0.3638 0.3165 0.4202 0.0457 -0.1443 -0.0943 641 GLU A O 4818 C CB . GLU A 600 ? 0.3639 0.3215 0.4712 0.0248 -0.1374 -0.0865 641 GLU A CB 4819 C CG . GLU A 600 ? 0.4462 0.4066 0.5825 0.0180 -0.1415 -0.0882 641 GLU A CG 4820 C CD . GLU A 600 ? 0.5185 0.4741 0.6677 0.0123 -0.1402 -0.0859 641 GLU A CD 4821 O OE1 . GLU A 600 ? 0.5654 0.5231 0.7392 0.0061 -0.1418 -0.0861 641 GLU A OE1 4822 O OE2 . GLU A 600 ? 0.5907 0.5404 0.7263 0.0141 -0.1373 -0.0837 641 GLU A OE2 4823 N N . ILE A 601 ? 0.3380 0.2979 0.3952 0.0364 -0.1251 -0.0804 642 ILE A N 4824 C CA . ILE A 601 ? 0.3392 0.2953 0.3728 0.0434 -0.1225 -0.0800 642 ILE A CA 4825 C C . ILE A 601 ? 0.3368 0.2956 0.3590 0.0486 -0.1228 -0.0808 642 ILE A C 4826 O O . ILE A 601 ? 0.3657 0.3191 0.3702 0.0567 -0.1259 -0.0841 642 ILE A O 4827 C CB . ILE A 601 ? 0.3365 0.2944 0.3638 0.0402 -0.1114 -0.0721 642 ILE A CB 4828 C CG1 . ILE A 601 ? 0.3366 0.2896 0.3718 0.0371 -0.1127 -0.0722 642 ILE A CG1 4829 C CG2 . ILE A 601 ? 0.3470 0.3027 0.3520 0.0472 -0.1075 -0.0711 642 ILE A CG2 4830 C CD1 . ILE A 601 ? 0.3550 0.3107 0.3894 0.0322 -0.1025 -0.0639 642 ILE A CD1 4831 N N . ALA A 602 ? 0.3230 0.2898 0.3548 0.0444 -0.1191 -0.0776 643 ALA A N 4832 C CA . ALA A 602 ? 0.3374 0.3066 0.3596 0.0492 -0.1195 -0.0782 643 ALA A CA 4833 C C . ALA A 602 ? 0.3567 0.3211 0.3778 0.0556 -0.1323 -0.0867 643 ALA A C 4834 O O . ALA A 602 ? 0.3583 0.3191 0.3621 0.0634 -0.1348 -0.0887 643 ALA A O 4835 C CB . ALA A 602 ? 0.3442 0.3227 0.3797 0.0431 -0.1140 -0.0739 643 ALA A CB 4836 N N . SER A 603 ? 0.3603 0.3240 0.3996 0.0526 -0.1403 -0.0916 644 SER A N 4837 C CA . SER A 603 ? 0.3934 0.3521 0.4329 0.0588 -0.1539 -0.1006 644 SER A CA 4838 C C . SER A 603 ? 0.3997 0.3478 0.4169 0.0677 -0.1588 -0.1051 644 SER A C 4839 O O . SER A 603 ? 0.4281 0.3713 0.4309 0.0763 -0.1662 -0.1103 644 SER A O 4840 C CB . SER A 603 ? 0.3995 0.3596 0.4653 0.0532 -0.1615 -0.1050 644 SER A CB 4841 O OG . SER A 603 ? 0.4909 0.4453 0.5562 0.0597 -0.1760 -0.1146 644 SER A OG 4842 N N . LYS A 604 ? 0.3935 0.3375 0.4069 0.0663 -0.1547 -0.1034 645 LYS A N 4843 C CA . LYS A 604 ? 0.4213 0.3553 0.4140 0.0748 -0.1584 -0.1076 645 LYS A CA 4844 C C . LYS A 604 ? 0.4146 0.3477 0.3826 0.0814 -0.1512 -0.1037 645 LYS A C 4845 O O . LYS A 604 ? 0.4216 0.3472 0.3705 0.0909 -0.1562 -0.1083 645 LYS A O 4846 C CB . LYS A 604 ? 0.4330 0.3632 0.4293 0.0717 -0.1558 -0.1067 645 LYS A CB 4847 C CG A LYS A 604 ? 0.4659 0.3945 0.4853 0.0663 -0.1641 -0.1115 645 LYS A CG 4848 C CG B LYS A 604 ? 0.4564 0.3837 0.4737 0.0676 -0.1653 -0.1125 645 LYS A CG 4849 C CD A LYS A 604 ? 0.5306 0.4513 0.5475 0.0671 -0.1652 -0.1134 645 LYS A CD 4850 C CD B LYS A 604 ? 0.5007 0.4193 0.5116 0.0758 -0.1797 -0.1233 645 LYS A CD 4851 C CE A LYS A 604 ? 0.5642 0.4811 0.6023 0.0634 -0.1754 -0.1196 645 LYS A CE 4852 C CE B LYS A 604 ? 0.5432 0.4581 0.5756 0.0718 -0.1895 -0.1295 645 LYS A CE 4853 N NZ A LYS A 604 ? 0.5536 0.4748 0.6127 0.0529 -0.1689 -0.1132 645 LYS A NZ 4854 N NZ B LYS A 604 ? 0.5903 0.4981 0.6192 0.0794 -0.2049 -0.1406 645 LYS A NZ 4855 N N . PHE A 605 ? 0.3710 0.3114 0.3394 0.0766 -0.1392 -0.0952 646 PHE A N 4856 C CA . PHE A 605 ? 0.3741 0.3142 0.3222 0.0819 -0.1318 -0.0910 646 PHE A CA 4857 C C . PHE A 605 ? 0.3914 0.3303 0.3311 0.0883 -0.1377 -0.0941 646 PHE A C 4858 O O . PHE A 605 ? 0.4266 0.3595 0.3446 0.0970 -0.1374 -0.0947 646 PHE A O 4859 C CB . PHE A 605 ? 0.3652 0.3141 0.3197 0.0745 -0.1193 -0.0819 646 PHE A CB 4860 C CG . PHE A 605 ? 0.3719 0.3215 0.3094 0.0787 -0.1113 -0.0771 646 PHE A CG 4861 C CD1 . PHE A 605 ? 0.3789 0.3252 0.3022 0.0820 -0.1046 -0.0742 646 PHE A CD1 4862 C CD2 . PHE A 605 ? 0.3931 0.3465 0.3297 0.0795 -0.1107 -0.0756 646 PHE A CD2 4863 C CE1 . PHE A 605 ? 0.4186 0.3653 0.3274 0.0859 -0.0967 -0.0696 646 PHE A CE1 4864 C CE2 . PHE A 605 ? 0.4210 0.3742 0.3418 0.0835 -0.1030 -0.0707 646 PHE A CE2 4865 C CZ . PHE A 605 ? 0.3727 0.3226 0.2803 0.0864 -0.0959 -0.0677 646 PHE A CZ 4866 N N . SER A 606 ? 0.3923 0.3366 0.3490 0.0842 -0.1428 -0.0957 647 SER A N 4867 C CA . SER A 606 ? 0.4104 0.3541 0.3613 0.0900 -0.1492 -0.0988 647 SER A CA 4868 C C . SER A 606 ? 0.4427 0.3758 0.3793 0.1000 -0.1615 -0.1074 647 SER A C 4869 O O . SER A 606 ? 0.4649 0.3933 0.3825 0.1084 -0.1635 -0.1083 647 SER A O 4870 C CB . SER A 606 ? 0.4038 0.3554 0.3789 0.0838 -0.1536 -0.1000 647 SER A CB 4871 O OG A SER A 606 ? 0.4078 0.3686 0.3936 0.0757 -0.1424 -0.0923 647 SER A OG 4872 O OG B SER A 606 ? 0.4353 0.3874 0.4039 0.0890 -0.1574 -0.1011 647 SER A OG 4873 N N . GLU A 607 ? 0.4470 0.3760 0.3922 0.0990 -0.1691 -0.1135 648 GLU A N 4874 C CA . GLU A 607 ? 0.4888 0.4066 0.4198 0.1086 -0.1811 -0.1225 648 GLU A CA 4875 C C . GLU A 607 ? 0.4994 0.4095 0.4009 0.1173 -0.1750 -0.1205 648 GLU A C 4876 O O . GLU A 607 ? 0.5159 0.4180 0.3964 0.1278 -0.1809 -0.1245 648 GLU A O 4877 C CB . GLU A 607 ? 0.5197 0.4343 0.4659 0.1052 -0.1887 -0.1285 648 GLU A CB 4878 C CG . GLU A 607 ? 0.5757 0.4969 0.5522 0.0972 -0.1958 -0.1314 648 GLU A CG 4879 C CD . GLU A 607 ? 0.6811 0.5983 0.6739 0.0937 -0.2035 -0.1374 648 GLU A CD 4880 O OE1 . GLU A 607 ? 0.7147 0.6238 0.6959 0.0971 -0.2035 -0.1395 648 GLU A OE1 4881 O OE2 . GLU A 607 ? 0.7370 0.6591 0.7558 0.0874 -0.2095 -0.1400 648 GLU A OE2 4882 N N . ARG A 608 ? 0.4731 0.3851 0.3724 0.1135 -0.1630 -0.1141 649 ARG A N 4883 C CA . ARG A 608 ? 0.4877 0.3932 0.3613 0.1214 -0.1560 -0.1118 649 ARG A CA 4884 C C . ARG A 608 ? 0.4944 0.4009 0.3522 0.1260 -0.1498 -0.1065 649 ARG A C 4885 O O . ARG A 608 ? 0.5216 0.4203 0.3556 0.1357 -0.1488 -0.1072 649 ARG A O 4886 C CB . ARG A 608 ? 0.4696 0.3778 0.3463 0.1163 -0.1448 -0.1060 649 ARG A CB 4887 C CG . ARG A 608 ? 0.4981 0.4033 0.3869 0.1130 -0.1501 -0.1107 649 ARG A CG 4888 C CD . ARG A 608 ? 0.4783 0.3831 0.3633 0.1117 -0.1403 -0.1062 649 ARG A CD 4889 N NE . ARG A 608 ? 0.4360 0.3505 0.3290 0.1040 -0.1280 -0.0967 649 ARG A NE 4890 C CZ . ARG A 608 ? 0.4498 0.3718 0.3641 0.0938 -0.1259 -0.0932 649 ARG A CZ 4891 N NH1 . ARG A 608 ? 0.4365 0.3578 0.3677 0.0895 -0.1346 -0.0979 649 ARG A NH1 4892 N NH2 . ARG A 608 ? 0.4240 0.3538 0.3425 0.0880 -0.1150 -0.0850 649 ARG A NH2 4893 N N . LEU A 609 ? 0.4870 0.4029 0.3581 0.1192 -0.1451 -0.1011 650 LEU A N 4894 C CA . LEU A 609 ? 0.5091 0.4262 0.3676 0.1226 -0.1386 -0.0956 650 LEU A CA 4895 C C . LEU A 609 ? 0.5568 0.4668 0.4013 0.1323 -0.1493 -0.1012 650 LEU A C 4896 O O . LEU A 609 ? 0.5659 0.4712 0.3896 0.1397 -0.1453 -0.0981 650 LEU A O 4897 C CB . LEU A 609 ? 0.5202 0.4487 0.3979 0.1128 -0.1323 -0.0895 650 LEU A CB 4898 C CG . LEU A 609 ? 0.5200 0.4511 0.3877 0.1139 -0.1220 -0.0818 650 LEU A CG 4899 C CD1 . LEU A 609 ? 0.5030 0.4340 0.3615 0.1133 -0.1095 -0.0755 650 LEU A CD1 4900 C CD2 . LEU A 609 ? 0.5509 0.4923 0.4389 0.1054 -0.1199 -0.0785 650 LEU A CD2 4901 N N . GLN A 610 ? 0.5801 0.4891 0.4364 0.1321 -0.1628 -0.1091 651 GLN A N 4902 C CA . GLN A 610 ? 0.6334 0.5364 0.4788 0.1409 -0.1742 -0.1148 651 GLN A CA 4903 C C . GLN A 610 ? 0.6599 0.5498 0.4796 0.1524 -0.1797 -0.1204 651 GLN A C 4904 O O . GLN A 610 ? 0.7039 0.5865 0.5020 0.1625 -0.1835 -0.1216 651 GLN A O 4905 C CB A GLN A 610 ? 0.6328 0.5407 0.5024 0.1364 -0.1868 -0.1210 651 GLN A CB 4906 C CB B GLN A 610 ? 0.6254 0.5327 0.4951 0.1366 -0.1875 -0.1217 651 GLN A CB 4907 C CG A GLN A 610 ? 0.6620 0.5820 0.5520 0.1275 -0.1805 -0.1149 651 GLN A CG 4908 C CG B GLN A 610 ? 0.6439 0.5451 0.5189 0.1382 -0.1997 -0.1313 651 GLN A CG 4909 C CD A GLN A 610 ? 0.6998 0.6250 0.6139 0.1239 -0.1921 -0.1207 651 GLN A CD 4910 C CD B GLN A 610 ? 0.6652 0.5730 0.5712 0.1307 -0.2096 -0.1365 651 GLN A CD 4911 O OE1 A GLN A 610 ? 0.7550 0.6742 0.6661 0.1305 -0.2063 -0.1292 651 GLN A OE1 4912 O OE1 B GLN A 610 ? 0.6302 0.5484 0.5560 0.1228 -0.2053 -0.1321 651 GLN A OE1 4913 N NE2 A GLN A 610 ? 0.7052 0.6418 0.6438 0.1135 -0.1863 -0.1164 651 GLN A NE2 4914 N NE2 B GLN A 610 ? 0.6776 0.5790 0.5884 0.1333 -0.2226 -0.1461 651 GLN A NE2 4915 N N . ASP A 611 ? 0.6638 0.5507 0.4850 0.1511 -0.1792 -0.1231 652 ASP A N 4916 C CA . ASP A 611 ? 0.6957 0.5704 0.4979 0.1607 -0.1863 -0.1306 652 ASP A CA 4917 C C . ASP A 611 ? 0.6807 0.5501 0.4608 0.1659 -0.1742 -0.1260 652 ASP A C 4918 O O . ASP A 611 ? 0.7108 0.5698 0.4739 0.1744 -0.1788 -0.1319 652 ASP A O 4919 C CB . ASP A 611 ? 0.7062 0.5811 0.5281 0.1550 -0.1935 -0.1370 652 ASP A CB 4920 C CG . ASP A 611 ? 0.7741 0.6484 0.6121 0.1544 -0.2106 -0.1464 652 ASP A CG 4921 O OD1 . ASP A 611 ? 0.8691 0.7422 0.7226 0.1505 -0.2173 -0.1521 652 ASP A OD1 4922 O OD2 . ASP A 611 ? 0.8424 0.7172 0.6786 0.1579 -0.2175 -0.1481 652 ASP A OD2 4923 N N . PHE A 612 ? 0.6508 0.5272 0.4325 0.1608 -0.1590 -0.1160 653 PHE A N 4924 C CA . PHE A 612 ? 0.6279 0.5003 0.3930 0.1649 -0.1476 -0.1120 653 PHE A CA 4925 C C . PHE A 612 ? 0.6283 0.4908 0.3629 0.1775 -0.1462 -0.1116 653 PHE A C 4926 O O . PHE A 612 ? 0.6622 0.5231 0.3897 0.1815 -0.1509 -0.1117 653 PHE A O 4927 C CB . PHE A 612 ? 0.6159 0.4981 0.3916 0.1562 -0.1321 -0.1018 653 PHE A CB 4928 C CG . PHE A 612 ? 0.5928 0.4789 0.3624 0.1563 -0.1232 -0.0936 653 PHE A CG 4929 C CD1 . PHE A 612 ? 0.5898 0.4718 0.3390 0.1627 -0.1119 -0.0878 653 PHE A CD1 4930 C CD2 . PHE A 612 ? 0.5954 0.4898 0.3821 0.1491 -0.1249 -0.0913 653 PHE A CD2 4931 C CE1 . PHE A 612 ? 0.6319 0.5175 0.3777 0.1619 -0.1030 -0.0800 653 PHE A CE1 4932 C CE2 . PHE A 612 ? 0.6385 0.5366 0.4212 0.1484 -0.1163 -0.0837 653 PHE A CE2 4933 C CZ . PHE A 612 ? 0.6848 0.5783 0.4474 0.1546 -0.1055 -0.0779 653 PHE A CZ 4934 N N . ASP A 613 ? 0.5870 0.4429 0.3038 0.1840 -0.1393 -0.1111 654 ASP A N 4935 C CA . ASP A 613 ? 0.5796 0.4253 0.2655 0.1967 -0.1360 -0.1102 654 ASP A CA 4936 C C . ASP A 613 ? 0.5425 0.3925 0.2234 0.1957 -0.1240 -0.0998 654 ASP A C 4937 O O . ASP A 613 ? 0.5442 0.4007 0.2314 0.1904 -0.1103 -0.0918 654 ASP A O 4938 C CB . ASP A 613 ? 0.5624 0.4012 0.2331 0.2030 -0.1294 -0.1112 654 ASP A CB 4939 C CG . ASP A 613 ? 0.6013 0.4291 0.2388 0.2165 -0.1244 -0.1097 654 ASP A CG 4940 O OD1 . ASP A 613 ? 0.5925 0.4199 0.2215 0.2190 -0.1230 -0.1052 654 ASP A OD1 4941 O OD2 . ASP A 613 ? 0.6046 0.4241 0.2253 0.2246 -0.1220 -0.1129 654 ASP A OD2 4942 N N . LYS A 614 ? 0.5628 0.4084 0.2315 0.2017 -0.1297 -0.1002 655 LYS A N 4943 C CA . LYS A 614 ? 0.5836 0.4329 0.2497 0.2004 -0.1206 -0.0910 655 LYS A CA 4944 C C . LYS A 614 ? 0.5965 0.4408 0.2399 0.2073 -0.1050 -0.0822 655 LYS A C 4945 O O . LYS A 614 ? 0.5834 0.4318 0.2294 0.2044 -0.0972 -0.0745 655 LYS A O 4946 C CB . LYS A 614 ? 0.6007 0.4470 0.2634 0.2045 -0.1336 -0.0949 655 LYS A CB 4947 C CG . LYS A 614 ? 0.6175 0.4722 0.3089 0.1953 -0.1459 -0.1008 655 LYS A CG 4948 C CD . LYS A 614 ? 0.6925 0.5433 0.3805 0.2006 -0.1605 -0.1064 655 LYS A CD 4949 C CE . LYS A 614 ? 0.6752 0.5367 0.3957 0.1900 -0.1697 -0.1102 655 LYS A CE 4950 N NZ . LYS A 614 ? 0.7189 0.5760 0.4372 0.1963 -0.1867 -0.1179 655 LYS A NZ 4951 N N A SER A 615 ? 0.6024 0.4354 0.2218 0.2184 -0.1055 -0.0862 656 SER A N 4952 N N B SER A 615 ? 0.6463 0.4831 0.2698 0.2151 -0.0967 -0.0809 656 SER A N 4953 C CA A SER A 615 ? 0.5915 0.4191 0.1906 0.2252 -0.0907 -0.0797 656 SER A CA 4954 C CA B SER A 615 ? 0.6402 0.4769 0.2521 0.2173 -0.0794 -0.0692 656 SER A CA 4955 C C A SER A 615 ? 0.5516 0.3891 0.1688 0.2160 -0.0767 -0.0737 656 SER A C 4956 C C B SER A 615 ? 0.6118 0.4547 0.2309 0.2124 -0.0619 -0.0614 656 SER A C 4957 O O A SER A 615 ? 0.5791 0.4148 0.1850 0.2196 -0.0625 -0.0666 656 SER A O 4958 O O B SER A 615 ? 0.6042 0.4432 0.2081 0.2178 -0.0485 -0.0539 656 SER A O 4959 C CB A SER A 615 ? 0.5915 0.4048 0.1623 0.2390 -0.0960 -0.0868 656 SER A CB 4960 C CB B SER A 615 ? 0.6555 0.4779 0.2325 0.2322 -0.0782 -0.0683 656 SER A CB 4961 O OG A SER A 615 ? 0.6064 0.4207 0.1874 0.2364 -0.1010 -0.0940 656 SER A OG 4962 O OG B SER A 615 ? 0.6738 0.4917 0.2364 0.2377 -0.0650 -0.0647 656 SER A OG 4963 N N A ASN A 616 ? 0.5321 0.3797 0.1768 0.2045 -0.0803 -0.0760 657 ASN A N 4964 N N B ASN A 616 ? 0.5634 0.4155 0.2061 0.2026 -0.0624 -0.0631 657 ASN A N 4965 C CA A ASN A 616 ? 0.5056 0.3617 0.1662 0.1968 -0.0685 -0.0711 657 ASN A CA 4966 C CA B ASN A 616 ? 0.5638 0.4195 0.2114 0.2003 -0.0504 -0.0595 657 ASN A CA 4967 C C A ASN A 616 ? 0.4857 0.3543 0.1686 0.1850 -0.0608 -0.0632 657 ASN A C 4968 C C B ASN A 616 ? 0.5408 0.4093 0.2119 0.1883 -0.0405 -0.0513 657 ASN A C 4969 O O A ASN A 616 ? 0.4739 0.3503 0.1783 0.1756 -0.0677 -0.0650 657 ASN A O 4970 O O B ASN A 616 ? 0.5236 0.4008 0.2172 0.1782 -0.0458 -0.0528 657 ASN A O 4971 C CB A ASN A 616 ? 0.4993 0.3569 0.1729 0.1931 -0.0760 -0.0786 657 ASN A CB 4972 C CB B ASN A 616 ? 0.5562 0.4117 0.2125 0.1986 -0.0601 -0.0685 657 ASN A CB 4973 C CG A ASN A 616 ? 0.4985 0.3612 0.1807 0.1892 -0.0642 -0.0744 657 ASN A CG 4974 C CG B ASN A 616 ? 0.5644 0.4239 0.2284 0.1959 -0.0505 -0.0664 657 ASN A CG 4975 O OD1 A ASN A 616 ? 0.4613 0.3322 0.1541 0.1829 -0.0527 -0.0661 657 ASN A OD1 4976 O OD1 B ASN A 616 ? 0.5945 0.4627 0.2719 0.1889 -0.0390 -0.0588 657 ASN A OD1 4977 N ND2 A ASN A 616 ? 0.5553 0.4130 0.2337 0.1931 -0.0674 -0.0806 657 ASN A ND2 4978 N ND2 B ASN A 616 ? 0.5946 0.4480 0.2521 0.2010 -0.0559 -0.0738 657 ASN A ND2 4979 N N A PRO A 617 ? 0.4695 0.3397 0.1473 0.1856 -0.0463 -0.0542 658 PRO A N 4980 N N B PRO A 617 ? 0.5434 0.4125 0.2088 0.1897 -0.0259 -0.0423 658 PRO A N 4981 C CA A PRO A 617 ? 0.4541 0.3346 0.1503 0.1757 -0.0391 -0.0467 658 PRO A CA 4982 C CA B PRO A 617 ? 0.5149 0.3954 0.2019 0.1788 -0.0172 -0.0348 658 PRO A CA 4983 C C A PRO A 617 ? 0.4226 0.3141 0.1440 0.1645 -0.0362 -0.0458 658 PRO A C 4984 C C B PRO A 617 ? 0.4821 0.3736 0.1955 0.1675 -0.0182 -0.0362 658 PRO A C 4985 O O A PRO A 617 ? 0.3917 0.2921 0.1312 0.1551 -0.0344 -0.0420 658 PRO A O 4986 O O B PRO A 617 ? 0.4551 0.3551 0.1873 0.1579 -0.0203 -0.0346 658 PRO A O 4987 C CB A PRO A 617 ? 0.4545 0.3320 0.1368 0.1809 -0.0243 -0.0380 658 PRO A CB 4988 C CB B PRO A 617 ? 0.5318 0.4101 0.2085 0.1834 -0.0010 -0.0266 658 PRO A CB 4989 C CG A PRO A 617 ? 0.4716 0.3413 0.1366 0.1901 -0.0202 -0.0404 658 PRO A CG 4990 C CG B PRO A 617 ? 0.5610 0.4254 0.2066 0.1973 -0.0020 -0.0280 658 PRO A CG 4991 C CD A PRO A 617 ? 0.5117 0.3734 0.1659 0.1962 -0.0359 -0.0508 658 PRO A CD 4992 C CD B PRO A 617 ? 0.5658 0.4247 0.2046 0.2015 -0.0168 -0.0388 658 PRO A CD 4993 N N A ILE A 618 ? 0.4416 0.3318 0.1630 0.1660 -0.0352 -0.0490 659 ILE A N 4994 N N B ILE A 618 ? 0.4856 0.3767 0.1999 0.1688 -0.0165 -0.0390 659 ILE A N 4995 C CA A ILE A 618 ? 0.4364 0.3359 0.1799 0.1565 -0.0325 -0.0481 659 ILE A CA 4996 C CA B ILE A 618 ? 0.4706 0.3715 0.2090 0.1585 -0.0173 -0.0397 659 ILE A CA 4997 C C A ILE A 618 ? 0.4145 0.3175 0.1741 0.1494 -0.0452 -0.0540 659 ILE A C 4998 C C B ILE A 618 ? 0.4484 0.3506 0.1975 0.1537 -0.0315 -0.0470 659 ILE A C 4999 O O A ILE A 618 ? 0.3963 0.3084 0.1762 0.1394 -0.0442 -0.0516 659 ILE A O 5000 O O B ILE A 618 ? 0.4360 0.3469 0.2056 0.1436 -0.0332 -0.0459 659 ILE A O 5001 C CB A ILE A 618 ? 0.4588 0.3555 0.1979 0.1607 -0.0278 -0.0497 659 ILE A CB 5002 C CB B ILE A 618 ? 0.4669 0.3683 0.2065 0.1603 -0.0101 -0.0394 659 ILE A CB 5003 C CG1 A ILE A 618 ? 0.5098 0.4017 0.2313 0.1692 -0.0151 -0.0445 659 ILE A CG1 5004 C CG1 B ILE A 618 ? 0.5026 0.4062 0.2400 0.1616 0.0053 -0.0308 659 ILE A CG1 5005 C CG2 A ILE A 618 ? 0.4443 0.3508 0.2070 0.1505 -0.0251 -0.0479 659 ILE A CG2 5006 C CG2 B ILE A 618 ? 0.4932 0.4031 0.2560 0.1503 -0.0135 -0.0411 659 ILE A CG2 5007 C CD1 A ILE A 618 ? 0.5370 0.4336 0.2616 0.1660 -0.0057 -0.0359 659 ILE A CD1 5008 C CD1 B ILE A 618 ? 0.4798 0.3897 0.2274 0.1548 0.0091 -0.0245 659 ILE A CD1 5009 N N A VAL A 619 ? 0.4179 0.3133 0.1683 0.1550 -0.0569 -0.0618 660 VAL A N 5010 N N B VAL A 619 ? 0.4560 0.3493 0.1916 0.1609 -0.0419 -0.0544 660 VAL A N 5011 C CA A VAL A 619 ? 0.4173 0.3156 0.1836 0.1487 -0.0690 -0.0674 660 VAL A CA 5012 C CA B VAL A 619 ? 0.4329 0.3278 0.1812 0.1559 -0.0557 -0.0612 660 VAL A CA 5013 C C A VAL A 619 ? 0.4020 0.3064 0.1784 0.1429 -0.0709 -0.0645 660 VAL A C 5014 C C B VAL A 619 ? 0.4150 0.3162 0.1752 0.1490 -0.0588 -0.0587 660 VAL A C 5015 O O A VAL A 619 ? 0.3806 0.2929 0.1777 0.1333 -0.0735 -0.0643 660 VAL A O 5016 O O B VAL A 619 ? 0.4029 0.3118 0.1839 0.1395 -0.0631 -0.0595 660 VAL A O 5017 C CB A VAL A 619 ? 0.4277 0.3163 0.1828 0.1563 -0.0818 -0.0770 660 VAL A CB 5018 C CB B VAL A 619 ? 0.4563 0.3403 0.1889 0.1651 -0.0675 -0.0704 660 VAL A CB 5019 C CG1 A VAL A 619 ? 0.4420 0.3341 0.2156 0.1495 -0.0942 -0.0823 660 VAL A CG1 5020 C CG1 B VAL A 619 ? 0.4563 0.3424 0.2044 0.1595 -0.0818 -0.0771 660 VAL A CG1 5021 C CG2 A VAL A 619 ? 0.4676 0.3504 0.2150 0.1614 -0.0804 -0.0806 660 VAL A CG2 5022 C CG2 B VAL A 619 ? 0.4722 0.3510 0.1975 0.1702 -0.0653 -0.0737 660 VAL A CG2 5023 N N A LEU A 620 ? 0.4107 0.3110 0.1720 0.1491 -0.0695 -0.0623 661 LEU A N 5024 N N B LEU A 620 ? 0.4120 0.3105 0.1599 0.1535 -0.0555 -0.0549 661 LEU A N 5025 C CA A LEU A 620 ? 0.3872 0.2928 0.1565 0.1445 -0.0695 -0.0586 661 LEU A CA 5026 C CA B LEU A 620 ? 0.4061 0.3100 0.1640 0.1481 -0.0577 -0.0523 661 LEU A CA 5027 C C A LEU A 620 ? 0.3840 0.3003 0.1716 0.1341 -0.0597 -0.0516 661 LEU A C 5028 C C B LEU A 620 ? 0.3811 0.2958 0.1584 0.1375 -0.0487 -0.0459 661 LEU A C 5029 O O A LEU A 620 ? 0.3465 0.2701 0.1521 0.1258 -0.0630 -0.0517 661 LEU A O 5030 O O B LEU A 620 ? 0.3750 0.2970 0.1693 0.1294 -0.0519 -0.0456 661 LEU A O 5031 C CB A LEU A 620 ? 0.4195 0.3174 0.1664 0.1541 -0.0670 -0.0560 661 LEU A CB 5032 C CB B LEU A 620 ? 0.4018 0.2994 0.1407 0.1560 -0.0545 -0.0487 661 LEU A CB 5033 C CG A LEU A 620 ? 0.4029 0.3050 0.1548 0.1509 -0.0648 -0.0509 661 LEU A CG 5034 C CG B LEU A 620 ? 0.4389 0.3418 0.1877 0.1509 -0.0559 -0.0455 661 LEU A CG 5035 C CD1 A LEU A 620 ? 0.3997 0.3069 0.1683 0.1452 -0.0760 -0.0554 661 LEU A CD1 5036 C CD1 B LEU A 620 ? 0.4328 0.3393 0.1962 0.1463 -0.0692 -0.0520 661 LEU A CD1 5037 C CD2 A LEU A 620 ? 0.4245 0.3171 0.1520 0.1615 -0.0623 -0.0481 661 LEU A CD2 5038 C CD2 B LEU A 620 ? 0.4248 0.3195 0.1526 0.1599 -0.0534 -0.0419 661 LEU A CD2 5039 N N A ARG A 621 ? 0.3783 0.2956 0.1618 0.1347 -0.0478 -0.0458 662 ARG A N 5040 N N B ARG A 621 ? 0.3854 0.3012 0.1603 0.1379 -0.0373 -0.0408 662 ARG A N 5041 C CA A ARG A 621 ? 0.3827 0.3093 0.1818 0.1259 -0.0386 -0.0391 662 ARG A CA 5042 C CA B ARG A 621 ? 0.3817 0.3076 0.1757 0.1280 -0.0298 -0.0354 662 ARG A CA 5043 C C A ARG A 621 ? 0.3814 0.3144 0.1984 0.1178 -0.0408 -0.0410 662 ARG A C 5044 C C B ARG A 621 ? 0.3868 0.3196 0.2010 0.1190 -0.0356 -0.0387 662 ARG A C 5045 O O A ARG A 621 ? 0.3521 0.2930 0.1854 0.1091 -0.0398 -0.0386 662 ARG A O 5046 O O B ARG A 621 ? 0.3678 0.3085 0.1974 0.1106 -0.0335 -0.0355 662 ARG A O 5047 C CB A ARG A 621 ? 0.3792 0.3050 0.1704 0.1290 -0.0257 -0.0328 662 ARG A CB 5048 C CB B ARG A 621 ? 0.3777 0.3039 0.1673 0.1302 -0.0169 -0.0296 662 ARG A CB 5049 C CG A ARG A 621 ? 0.3624 0.2978 0.1715 0.1199 -0.0176 -0.0274 662 ARG A CG 5050 C CG B ARG A 621 ? 0.3622 0.2983 0.1705 0.1208 -0.0097 -0.0242 662 ARG A CG 5051 C CD A ARG A 621 ? 0.3378 0.2774 0.1527 0.1156 -0.0136 -0.0223 662 ARG A CD 5052 C CD B ARG A 621 ? 0.4700 0.4085 0.2799 0.1187 -0.0035 -0.0181 662 ARG A CD 5053 N NE A ARG A 621 ? 0.3516 0.2971 0.1764 0.1109 -0.0033 -0.0167 662 ARG A NE 5054 N NE B ARG A 621 ? 0.4960 0.4420 0.3198 0.1124 0.0058 -0.0128 662 ARG A NE 5055 C CZ A ARG A 621 ? 0.3523 0.2993 0.1777 0.1103 0.0056 -0.0104 662 ARG A CZ 5056 C CZ B ARG A 621 ? 0.4631 0.4120 0.2916 0.1097 0.0134 -0.0069 662 ARG A CZ 5057 N NH1 A ARG A 621 ? 0.3816 0.3247 0.1985 0.1134 0.0062 -0.0081 662 ARG A NH1 5058 N NH1 B ARG A 621 ? 0.4740 0.4193 0.2947 0.1122 0.0133 -0.0049 662 ARG A NH1 5059 N NH2 A ARG A 621 ? 0.3742 0.3267 0.2102 0.1061 0.0138 -0.0065 662 ARG A NH2 5060 N NH2 B ARG A 621 ? 0.4713 0.4269 0.3133 0.1043 0.0205 -0.0032 662 ARG A NH2 5061 N N . MET A 622 ? 0.4125 0.3416 0.2258 0.1210 -0.0431 -0.0450 663 MET A N 5062 C CA . MET A 622 ? 0.4093 0.3432 0.2400 0.1134 -0.0474 -0.0475 663 MET A CA 5063 C C . MET A 622 ? 0.4158 0.3531 0.2591 0.1076 -0.0563 -0.0505 663 MET A C 5064 O O . MET A 622 ? 0.3819 0.3266 0.2422 0.0987 -0.0555 -0.0484 663 MET A O 5065 C CB A MET A 622 ? 0.4270 0.3542 0.2514 0.1186 -0.0526 -0.0536 663 MET A CB 5066 C CB B MET A 622 ? 0.4261 0.3538 0.2503 0.1186 -0.0504 -0.0525 663 MET A CB 5067 C CG A MET A 622 ? 0.4281 0.3576 0.2690 0.1119 -0.0607 -0.0578 663 MET A CG 5068 C CG B MET A 622 ? 0.4110 0.3370 0.2256 0.1237 -0.0396 -0.0487 663 MET A CG 5069 S SD A MET A 622 ? 0.4081 0.3288 0.2421 0.1182 -0.0671 -0.0652 663 MET A SD 5070 S SD B MET A 622 ? 0.4445 0.3644 0.2528 0.1297 -0.0401 -0.0534 663 MET A SD 5071 C CE A MET A 622 ? 0.5444 0.4564 0.3514 0.1311 -0.0622 -0.0654 663 MET A CE 5072 C CE B MET A 622 ? 0.3667 0.2735 0.1514 0.1418 -0.0493 -0.0613 663 MET A CE 5073 N N . MET A 623 ? 0.3941 0.3260 0.2293 0.1127 -0.0649 -0.0552 664 MET A N 5074 C CA . MET A 623 ? 0.3993 0.3349 0.2475 0.1078 -0.0730 -0.0580 664 MET A CA 5075 C C . MET A 623 ? 0.3851 0.3280 0.2414 0.1022 -0.0677 -0.0524 664 MET A C 5076 O O . MET A 623 ? 0.3869 0.3364 0.2601 0.0943 -0.0695 -0.0521 664 MET A O 5077 C CB A MET A 623 ? 0.4252 0.3527 0.2602 0.1163 -0.0829 -0.0640 664 MET A CB 5078 C CB B MET A 623 ? 0.4114 0.3397 0.2514 0.1145 -0.0850 -0.0655 664 MET A CB 5079 C CG A MET A 623 ? 0.4720 0.3903 0.2929 0.1244 -0.0876 -0.0697 664 MET A CG 5080 C CG B MET A 623 ? 0.3498 0.2735 0.1916 0.1158 -0.0921 -0.0719 664 MET A CG 5081 S SD A MET A 623 ? 0.4970 0.4169 0.3358 0.1180 -0.0939 -0.0746 664 MET A SD 5082 S SD B MET A 623 ? 0.4007 0.3172 0.2403 0.1213 -0.1087 -0.0821 664 MET A SD 5083 C CE A MET A 623 ? 0.4477 0.3619 0.2873 0.1218 -0.1104 -0.0844 664 MET A CE 5084 C CE B MET A 623 ? 0.3381 0.2635 0.2080 0.1089 -0.1134 -0.0831 664 MET A CE 5085 N N . ASN A 624 ? 0.3935 0.3344 0.2373 0.1067 -0.0608 -0.0479 665 ASN A N 5086 C CA . ASN A 624 ? 0.3697 0.3168 0.2205 0.1019 -0.0555 -0.0426 665 ASN A CA 5087 C C . ASN A 624 ? 0.3603 0.3155 0.2260 0.0929 -0.0482 -0.0383 665 ASN A C 5088 O O . ASN A 624 ? 0.3505 0.3119 0.2285 0.0865 -0.0476 -0.0366 665 ASN A O 5089 C CB . ASN A 624 ? 0.4012 0.3438 0.2362 0.1083 -0.0489 -0.0381 665 ASN A CB 5090 C CG . ASN A 624 ? 0.3963 0.3332 0.2206 0.1151 -0.0565 -0.0411 665 ASN A CG 5091 O OD1 . ASN A 624 ? 0.4066 0.3458 0.2405 0.1126 -0.0655 -0.0455 665 ASN A OD1 5092 N ND2 . ASN A 624 ? 0.4111 0.3404 0.2158 0.1238 -0.0529 -0.0388 665 ASN A ND2 5093 N N . ASP A 625 ? 0.3512 0.3058 0.2153 0.0931 -0.0434 -0.0370 666 ASP A N 5094 C CA . ASP A 625 ? 0.3469 0.3089 0.2251 0.0850 -0.0377 -0.0334 666 ASP A CA 5095 C C . ASP A 625 ? 0.3409 0.3066 0.2337 0.0783 -0.0443 -0.0365 666 ASP A C 5096 O O . ASP A 625 ? 0.3383 0.3106 0.2434 0.0710 -0.0416 -0.0337 666 ASP A O 5097 C CB . ASP A 625 ? 0.3577 0.3181 0.2315 0.0875 -0.0322 -0.0320 666 ASP A CB 5098 C CG . ASP A 625 ? 0.3645 0.3240 0.2294 0.0913 -0.0224 -0.0267 666 ASP A CG 5099 O OD1 . ASP A 625 ? 0.3957 0.3555 0.2579 0.0917 -0.0200 -0.0239 666 ASP A OD1 5100 O OD2 . ASP A 625 ? 0.3841 0.3430 0.2469 0.0934 -0.0168 -0.0251 666 ASP A OD2 5101 N N . GLN A 626 ? 0.3160 0.2773 0.2080 0.0808 -0.0526 -0.0421 667 GLN A N 5102 C CA . GLN A 626 ? 0.3171 0.2818 0.2245 0.0742 -0.0584 -0.0446 667 GLN A CA 5103 C C . GLN A 626 ? 0.3127 0.2823 0.2291 0.0700 -0.0600 -0.0440 667 GLN A C 5104 O O . GLN A 626 ? 0.3094 0.2848 0.2396 0.0626 -0.0590 -0.0425 667 GLN A O 5105 C CB . GLN A 626 ? 0.3213 0.2797 0.2269 0.0779 -0.0678 -0.0514 667 GLN A CB 5106 C CG . GLN A 626 ? 0.3260 0.2805 0.2268 0.0803 -0.0659 -0.0519 667 GLN A CG 5107 C CD . GLN A 626 ? 0.3510 0.2985 0.2496 0.0844 -0.0753 -0.0589 667 GLN A CD 5108 O OE1 . GLN A 626 ? 0.3934 0.3341 0.2778 0.0926 -0.0791 -0.0629 667 GLN A OE1 5109 N NE2 . GLN A 626 ? 0.3472 0.2953 0.2589 0.0791 -0.0789 -0.0606 667 GLN A NE2 5110 N N . LEU A 627 ? 0.3369 0.3040 0.2451 0.0752 -0.0626 -0.0454 668 LEU A N 5111 C CA . LEU A 627 ? 0.3237 0.2956 0.2401 0.0719 -0.0636 -0.0446 668 LEU A CA 5112 C C . LEU A 627 ? 0.3028 0.2810 0.2245 0.0665 -0.0545 -0.0386 668 LEU A C 5113 O O . LEU A 627 ? 0.3229 0.3071 0.2577 0.0601 -0.0542 -0.0378 668 LEU A O 5114 C CB . LEU A 627 ? 0.3422 0.3091 0.2468 0.0797 -0.0681 -0.0469 668 LEU A CB 5115 C CG . LEU A 627 ? 0.3861 0.3479 0.2896 0.0839 -0.0795 -0.0541 668 LEU A CG 5116 C CD1 . LEU A 627 ? 0.4373 0.3929 0.3257 0.0929 -0.0841 -0.0562 668 LEU A CD1 5117 C CD2 . LEU A 627 ? 0.4106 0.3779 0.3345 0.0772 -0.0855 -0.0572 668 LEU A CD2 5118 N N . MET A 628 ? 0.3170 0.2936 0.2288 0.0691 -0.0474 -0.0347 669 MET A N 5119 C CA . MET A 628 ? 0.3206 0.3022 0.2365 0.0648 -0.0393 -0.0294 669 MET A CA 5120 C C . MET A 628 ? 0.2988 0.2859 0.2267 0.0572 -0.0368 -0.0278 669 MET A C 5121 O O . MET A 628 ? 0.3031 0.2955 0.2394 0.0518 -0.0337 -0.0255 669 MET A O 5122 C CB . MET A 628 ? 0.3306 0.3091 0.2350 0.0693 -0.0324 -0.0257 669 MET A CB 5123 C CG . MET A 628 ? 0.3543 0.3379 0.2646 0.0644 -0.0242 -0.0205 669 MET A CG 5124 S SD . MET A 628 ? 0.4007 0.3807 0.2999 0.0696 -0.0154 -0.0158 669 MET A SD 5125 C CE . MET A 628 ? 0.3702 0.3502 0.2700 0.0696 -0.0135 -0.0161 669 MET A CE 5126 N N . PHE A 629 ? 0.2972 0.2824 0.2248 0.0574 -0.0379 -0.0290 670 PHE A N 5127 C CA . PHE A 629 ? 0.2916 0.2811 0.2293 0.0508 -0.0356 -0.0271 670 PHE A CA 5128 C C . PHE A 629 ? 0.2898 0.2813 0.2386 0.0458 -0.0405 -0.0293 670 PHE A C 5129 O O . PHE A 629 ? 0.2742 0.2686 0.2305 0.0405 -0.0387 -0.0274 670 PHE A O 5130 C CB . PHE A 629 ? 0.2851 0.2719 0.2187 0.0528 -0.0338 -0.0267 670 PHE A CB 5131 C CG . PHE A 629 ? 0.2983 0.2851 0.2252 0.0556 -0.0267 -0.0231 670 PHE A CG 5132 C CD1 . PHE A 629 ? 0.2984 0.2903 0.2307 0.0512 -0.0209 -0.0190 670 PHE A CD1 5133 C CD2 . PHE A 629 ? 0.3192 0.3008 0.2349 0.0626 -0.0254 -0.0239 670 PHE A CD2 5134 C CE1 . PHE A 629 ? 0.3256 0.3179 0.2543 0.0534 -0.0144 -0.0158 670 PHE A CE1 5135 C CE2 . PHE A 629 ? 0.3545 0.3365 0.2658 0.0651 -0.0179 -0.0201 670 PHE A CE2 5136 C CZ . PHE A 629 ? 0.3280 0.3156 0.2468 0.0601 -0.0123 -0.0159 670 PHE A CZ 5137 N N . LEU A 630 ? 0.2857 0.2760 0.2366 0.0474 -0.0466 -0.0330 671 LEU A N 5138 C CA . LEU A 630 ? 0.2699 0.2626 0.2337 0.0424 -0.0506 -0.0348 671 LEU A CA 5139 C C . LEU A 630 ? 0.2614 0.2608 0.2344 0.0360 -0.0458 -0.0314 671 LEU A C 5140 O O . LEU A 630 ? 0.2607 0.2623 0.2419 0.0307 -0.0443 -0.0298 671 LEU A O 5141 C CB . LEU A 630 ? 0.2879 0.2783 0.2537 0.0457 -0.0588 -0.0401 671 LEU A CB 5142 C CG . LEU A 630 ? 0.2956 0.2888 0.2773 0.0404 -0.0628 -0.0420 671 LEU A CG 5143 C CD1 . LEU A 630 ? 0.3188 0.3102 0.3058 0.0371 -0.0635 -0.0419 671 LEU A CD1 5144 C CD2 . LEU A 630 ? 0.3163 0.3074 0.3010 0.0443 -0.0719 -0.0478 671 LEU A CD2 5145 N N . GLU A 631 ? 0.2442 0.2459 0.2149 0.0369 -0.0430 -0.0301 672 GLU A N 5146 C CA . GLU A 631 ? 0.2425 0.2499 0.2204 0.0314 -0.0379 -0.0271 672 GLU A CA 5147 C C . GLU A 631 ? 0.2285 0.2369 0.2048 0.0283 -0.0326 -0.0235 672 GLU A C 5148 O O . GLU A 631 ? 0.2437 0.2554 0.2269 0.0229 -0.0301 -0.0216 672 GLU A O 5149 C CB . GLU A 631 ? 0.2443 0.2531 0.2185 0.0335 -0.0353 -0.0261 672 GLU A CB 5150 C CG . GLU A 631 ? 0.2353 0.2497 0.2181 0.0283 -0.0316 -0.0245 672 GLU A CG 5151 C CD . GLU A 631 ? 0.2702 0.2871 0.2639 0.0269 -0.0356 -0.0273 672 GLU A CD 5152 O OE1 . GLU A 631 ? 0.2630 0.2789 0.2564 0.0308 -0.0399 -0.0299 672 GLU A OE1 5153 O OE2 . GLU A 631 ? 0.2633 0.2832 0.2665 0.0219 -0.0346 -0.0268 672 GLU A OE2 5154 N N . ARG A 632 ? 0.2327 0.2382 0.2004 0.0316 -0.0309 -0.0225 673 ARG A N 5155 C CA . ARG A 632 ? 0.2401 0.2468 0.2070 0.0292 -0.0264 -0.0192 673 ARG A CA 5156 C C . ARG A 632 ? 0.2380 0.2444 0.2105 0.0255 -0.0283 -0.0191 673 ARG A C 5157 O O . ARG A 632 ? 0.2374 0.2457 0.2121 0.0219 -0.0255 -0.0165 673 ARG A O 5158 C CB . ARG A 632 ? 0.2638 0.2674 0.2220 0.0341 -0.0245 -0.0186 673 ARG A CB 5159 C CG . ARG A 632 ? 0.2549 0.2612 0.2132 0.0321 -0.0188 -0.0150 673 ARG A CG 5160 C CD . ARG A 632 ? 0.2483 0.2563 0.2053 0.0326 -0.0153 -0.0136 673 ARG A CD 5161 N NE . ARG A 632 ? 0.2384 0.2428 0.1871 0.0386 -0.0137 -0.0134 673 ARG A NE 5162 C CZ . ARG A 632 ? 0.2609 0.2628 0.2048 0.0423 -0.0154 -0.0146 673 ARG A CZ 5163 N NH1 . ARG A 632 ? 0.2619 0.2649 0.2096 0.0409 -0.0193 -0.0168 673 ARG A NH1 5164 N NH2 . ARG A 632 ? 0.2833 0.2813 0.2182 0.0479 -0.0130 -0.0136 673 ARG A NH2 5165 N N . ALA A 633 ? 0.2258 0.2290 0.2002 0.0270 -0.0336 -0.0222 674 ALA A N 5166 C CA . ALA A 633 ? 0.2292 0.2309 0.2088 0.0241 -0.0355 -0.0219 674 ALA A CA 5167 C C . ALA A 633 ? 0.2196 0.2247 0.2080 0.0180 -0.0337 -0.0199 674 ALA A C 5168 O O . ALA A 633 ? 0.2530 0.2570 0.2448 0.0150 -0.0336 -0.0181 674 ALA A O 5169 C CB . ALA A 633 ? 0.2389 0.2359 0.2195 0.0270 -0.0419 -0.0261 674 ALA A CB 5170 N N . PHE A 634 ? 0.2179 0.2268 0.2099 0.0165 -0.0322 -0.0200 675 PHE A N 5171 C CA . PHE A 634 ? 0.2145 0.2267 0.2143 0.0112 -0.0295 -0.0179 675 PHE A CA 5172 C C . PHE A 634 ? 0.2263 0.2406 0.2223 0.0087 -0.0242 -0.0143 675 PHE A C 5173 O O . PHE A 634 ? 0.2281 0.2444 0.2281 0.0048 -0.0213 -0.0122 675 PHE A O 5174 C CB . PHE A 634 ? 0.2196 0.2351 0.2260 0.0107 -0.0301 -0.0198 675 PHE A CB 5175 C CG . PHE A 634 ? 0.2315 0.2451 0.2444 0.0123 -0.0364 -0.0236 675 PHE A CG 5176 C CD1 . PHE A 634 ? 0.2564 0.2686 0.2784 0.0090 -0.0383 -0.0237 675 PHE A CD1 5177 C CD2 . PHE A 634 ? 0.2705 0.2831 0.2805 0.0171 -0.0406 -0.0272 675 PHE A CD2 5178 C CE1 . PHE A 634 ? 0.2601 0.2703 0.2902 0.0102 -0.0449 -0.0279 675 PHE A CE1 5179 C CE2 . PHE A 634 ? 0.2743 0.2847 0.2905 0.0188 -0.0477 -0.0316 675 PHE A CE2 5180 C CZ . PHE A 634 ? 0.2685 0.2779 0.2955 0.0152 -0.0501 -0.0321 675 PHE A CZ 5181 N N . ILE A 635 ? 0.2212 0.2349 0.2097 0.0112 -0.0229 -0.0136 676 ILE A N 5182 C CA . ILE A 635 ? 0.2184 0.2339 0.2037 0.0091 -0.0188 -0.0106 676 ILE A CA 5183 C C . ILE A 635 ? 0.2285 0.2418 0.2134 0.0073 -0.0193 -0.0085 676 ILE A C 5184 O O . ILE A 635 ? 0.2546 0.2648 0.2383 0.0095 -0.0220 -0.0090 676 ILE A O 5185 C CB . ILE A 635 ? 0.2158 0.2315 0.1953 0.0124 -0.0174 -0.0107 676 ILE A CB 5186 C CG1 . ILE A 635 ? 0.2223 0.2397 0.2017 0.0140 -0.0165 -0.0121 676 ILE A CG1 5187 C CG2 . ILE A 635 ? 0.2314 0.2486 0.2087 0.0107 -0.0146 -0.0083 676 ILE A CG2 5188 C CD1 . ILE A 635 ? 0.2390 0.2600 0.2216 0.0107 -0.0136 -0.0115 676 ILE A CD1 5189 N N . ASP A 636 ? 0.2185 0.2330 0.2034 0.0039 -0.0167 -0.0059 677 ASP A N 5190 C CA . ASP A 636 ? 0.2347 0.2468 0.2174 0.0026 -0.0170 -0.0033 677 ASP A CA 5191 C C . ASP A 636 ? 0.2306 0.2442 0.2082 0.0033 -0.0156 -0.0024 677 ASP A C 5192 O O . ASP A 636 ? 0.2394 0.2555 0.2156 0.0020 -0.0130 -0.0023 677 ASP A O 5193 C CB . ASP A 636 ? 0.2374 0.2491 0.2221 -0.0012 -0.0148 -0.0009 677 ASP A CB 5194 C CG . ASP A 636 ? 0.2429 0.2508 0.2250 -0.0022 -0.0156 0.0022 677 ASP A CG 5195 O OD1 . ASP A 636 ? 0.2623 0.2693 0.2401 -0.0005 -0.0171 0.0027 677 ASP A OD1 5196 O OD2 . ASP A 636 ? 0.2554 0.2611 0.2405 -0.0048 -0.0145 0.0044 677 ASP A OD2 5197 N N . PRO A 637 ? 0.2520 0.2641 0.2279 0.0054 -0.0174 -0.0021 678 PRO A N 5198 C CA . PRO A 637 ? 0.2707 0.2848 0.2442 0.0060 -0.0165 -0.0017 678 PRO A CA 5199 C C . PRO A 637 ? 0.2851 0.2991 0.2557 0.0034 -0.0160 0.0003 678 PRO A C 5200 O O . PRO A 637 ? 0.3288 0.3446 0.2980 0.0035 -0.0157 0.0001 678 PRO A O 5201 C CB . PRO A 637 ? 0.2673 0.2798 0.2413 0.0088 -0.0187 -0.0016 678 PRO A CB 5202 C CG . PRO A 637 ? 0.2912 0.2997 0.2662 0.0088 -0.0211 -0.0014 678 PRO A CG 5203 C CD . PRO A 637 ? 0.2602 0.2689 0.2372 0.0074 -0.0204 -0.0025 678 PRO A CD 5204 N N . LEU A 638 ? 0.2522 0.2637 0.2217 0.0013 -0.0160 0.0022 679 LEU A N 5205 C CA . LEU A 638 ? 0.2577 0.2682 0.2221 -0.0006 -0.0150 0.0044 679 LEU A CA 5206 C C . LEU A 638 ? 0.2706 0.2831 0.2336 -0.0025 -0.0113 0.0040 679 LEU A C 5207 O O . LEU A 638 ? 0.2890 0.3006 0.2462 -0.0036 -0.0099 0.0054 679 LEU A O 5208 C CB . LEU A 638 ? 0.2702 0.2762 0.2331 -0.0016 -0.0160 0.0075 679 LEU A CB 5209 C CG . LEU A 638 ? 0.2799 0.2833 0.2438 0.0005 -0.0199 0.0080 679 LEU A CG 5210 C CD1 . LEU A 638 ? 0.2962 0.2943 0.2584 -0.0006 -0.0207 0.0115 679 LEU A CD1 5211 C CD2 . LEU A 638 ? 0.3048 0.3097 0.2661 0.0023 -0.0220 0.0074 679 LEU A CD2 5212 N N . GLY A 639 ? 0.2545 0.2695 0.2225 -0.0024 -0.0098 0.0020 680 GLY A N 5213 C CA . GLY A 639 ? 0.2715 0.2889 0.2398 -0.0038 -0.0062 0.0012 680 GLY A CA 5214 C C . GLY A 639 ? 0.2809 0.2970 0.2495 -0.0062 -0.0034 0.0035 680 GLY A C 5215 O O . GLY A 639 ? 0.3214 0.3344 0.2904 -0.0070 -0.0042 0.0059 680 GLY A O 5216 N N . LEU A 640 ? 0.2786 0.2970 0.2479 -0.0072 0.0005 0.0030 681 LEU A N 5217 C CA . LEU A 640 ? 0.3065 0.3239 0.2763 -0.0095 0.0046 0.0056 681 LEU A CA 5218 C C . LEU A 640 ? 0.3187 0.3335 0.2779 -0.0096 0.0066 0.0078 681 LEU A C 5219 O O . LEU A 640 ? 0.3134 0.3281 0.2660 -0.0082 0.0049 0.0063 681 LEU A O 5220 C CB . LEU A 640 ? 0.3023 0.3240 0.2787 -0.0101 0.0082 0.0037 681 LEU A CB 5221 C CG . LEU A 640 ? 0.3175 0.3410 0.3045 -0.0098 0.0055 0.0017 681 LEU A CG 5222 C CD1 . LEU A 640 ? 0.3656 0.3935 0.3585 -0.0093 0.0073 -0.0011 681 LEU A CD1 5223 C CD2 . LEU A 640 ? 0.3784 0.3999 0.3726 -0.0120 0.0057 0.0041 681 LEU A CD2 5224 N N . PRO A 641 ? 0.3440 0.3560 0.3010 -0.0112 0.0102 0.0115 682 PRO A N 5225 C CA . PRO A 641 ? 0.3505 0.3587 0.2950 -0.0107 0.0118 0.0139 682 PRO A CA 5226 C C . PRO A 641 ? 0.3594 0.3690 0.2963 -0.0093 0.0133 0.0112 682 PRO A C 5227 O O . PRO A 641 ? 0.3764 0.3893 0.3166 -0.0097 0.0175 0.0095 682 PRO A O 5228 C CB . PRO A 641 ? 0.3742 0.3797 0.3195 -0.0127 0.0176 0.0186 682 PRO A CB 5229 C CG . PRO A 641 ? 0.3578 0.3643 0.3159 -0.0143 0.0161 0.0189 682 PRO A CG 5230 C CD . PRO A 641 ? 0.3396 0.3515 0.3057 -0.0135 0.0131 0.0137 682 PRO A CD 5231 N N . ASP A 642 ? 0.3726 0.3801 0.3009 -0.0075 0.0092 0.0101 683 ASP A N 5232 C CA . ASP A 642 ? 0.3964 0.4044 0.3175 -0.0060 0.0088 0.0068 683 ASP A CA 5233 C C . ASP A 642 ? 0.3639 0.3770 0.2933 -0.0060 0.0089 0.0026 683 ASP A C 5234 O O . ASP A 642 ? 0.3652 0.3790 0.2909 -0.0051 0.0096 -0.0004 683 ASP A O 5235 C CB . ASP A 642 ? 0.4325 0.4378 0.3433 -0.0057 0.0142 0.0084 683 ASP A CB 5236 C CG . ASP A 642 ? 0.5176 0.5169 0.4182 -0.0052 0.0144 0.0131 683 ASP A CG 5237 O OD1 . ASP A 642 ? 0.5809 0.5769 0.4749 -0.0036 0.0086 0.0131 683 ASP A OD1 5238 O OD2 . ASP A 642 ? 0.6003 0.5979 0.5004 -0.0063 0.0205 0.0170 683 ASP A OD2 5239 N N . ARG A 643 ? 0.3339 0.3500 0.2742 -0.0067 0.0079 0.0022 684 ARG A N 5240 C CA . ARG A 643 ? 0.3074 0.3275 0.2548 -0.0061 0.0076 -0.0014 684 ARG A CA 5241 C C . ARG A 643 ? 0.2807 0.3016 0.2339 -0.0053 0.0031 -0.0020 684 ARG A C 5242 O O . ARG A 643 ? 0.2801 0.3026 0.2406 -0.0054 0.0029 -0.0021 684 ARG A O 5243 C CB . ARG A 643 ? 0.3078 0.3309 0.2623 -0.0070 0.0120 -0.0018 684 ARG A CB 5244 C CG . ARG A 643 ? 0.3390 0.3619 0.2884 -0.0073 0.0177 -0.0015 684 ARG A CG 5245 C CD . ARG A 643 ? 0.3720 0.3989 0.3307 -0.0078 0.0219 -0.0025 684 ARG A CD 5246 N NE . ARG A 643 ? 0.3465 0.3745 0.3144 -0.0095 0.0225 -0.0002 684 ARG A NE 5247 C CZ . ARG A 643 ? 0.3531 0.3851 0.3322 -0.0099 0.0242 -0.0013 684 ARG A CZ 5248 N NH1 . ARG A 643 ? 0.3310 0.3661 0.3129 -0.0087 0.0258 -0.0044 684 ARG A NH1 5249 N NH2 . ARG A 643 ? 0.3477 0.3803 0.3360 -0.0115 0.0237 0.0004 684 ARG A NH2 5250 N N . PRO A 644 ? 0.2864 0.3063 0.2366 -0.0043 -0.0006 -0.0027 685 PRO A N 5251 C CA . PRO A 644 ? 0.2734 0.2936 0.2282 -0.0033 -0.0041 -0.0026 685 PRO A CA 5252 C C . PRO A 644 ? 0.2518 0.2748 0.2135 -0.0023 -0.0037 -0.0046 685 PRO A C 5253 O O . PRO A 644 ? 0.2698 0.2928 0.2350 -0.0011 -0.0054 -0.0043 685 PRO A O 5254 C CB . PRO A 644 ? 0.3143 0.3335 0.2657 -0.0025 -0.0076 -0.0033 685 PRO A CB 5255 C CG . PRO A 644 ? 0.3076 0.3262 0.2530 -0.0028 -0.0064 -0.0050 685 PRO A CG 5256 C CD . PRO A 644 ? 0.3113 0.3292 0.2534 -0.0039 -0.0019 -0.0036 685 PRO A CD 5257 N N . PHE A 645 ? 0.2355 0.2602 0.1981 -0.0024 -0.0013 -0.0065 686 PHE A N 5258 C CA . PHE A 645 ? 0.2439 0.2704 0.2119 -0.0010 -0.0007 -0.0080 686 PHE A CA 5259 C C . PHE A 645 ? 0.2378 0.2655 0.2097 -0.0009 0.0008 -0.0082 686 PHE A C 5260 O O . PHE A 645 ? 0.2497 0.2782 0.2251 0.0008 0.0007 -0.0093 686 PHE A O 5261 C CB . PHE A 645 ? 0.2412 0.2683 0.2090 -0.0007 0.0003 -0.0102 686 PHE A CB 5262 C CG . PHE A 645 ? 0.2389 0.2652 0.2054 -0.0008 -0.0022 -0.0106 686 PHE A CG 5263 C CD1 . PHE A 645 ? 0.2542 0.2807 0.2241 0.0002 -0.0041 -0.0097 686 PHE A CD1 5264 C CD2 . PHE A 645 ? 0.2582 0.2835 0.2200 -0.0016 -0.0027 -0.0120 686 PHE A CD2 5265 C CE1 . PHE A 645 ? 0.2465 0.2729 0.2174 0.0001 -0.0065 -0.0102 686 PHE A CE1 5266 C CE2 . PHE A 645 ? 0.2765 0.3011 0.2380 -0.0015 -0.0060 -0.0129 686 PHE A CE2 5267 C CZ . PHE A 645 ? 0.2620 0.2875 0.2291 -0.0009 -0.0080 -0.0120 686 PHE A CZ 5268 N N . TYR A 646 ? 0.2259 0.2534 0.1978 -0.0024 0.0020 -0.0069 687 TYR A N 5269 C CA . TYR A 646 ? 0.2217 0.2505 0.1998 -0.0025 0.0025 -0.0071 687 TYR A CA 5270 C C . TYR A 646 ? 0.2206 0.2474 0.1997 -0.0027 -0.0001 -0.0055 687 TYR A C 5271 O O . TYR A 646 ? 0.2578 0.2828 0.2350 -0.0044 0.0004 -0.0033 687 TYR A O 5272 C CB . TYR A 646 ? 0.2326 0.2629 0.2124 -0.0043 0.0066 -0.0068 687 TYR A CB 5273 C CG . TYR A 646 ? 0.2306 0.2629 0.2103 -0.0036 0.0092 -0.0090 687 TYR A CG 5274 C CD1 . TYR A 646 ? 0.2359 0.2688 0.2169 -0.0016 0.0078 -0.0110 687 TYR A CD1 5275 C CD2 . TYR A 646 ? 0.2523 0.2853 0.2301 -0.0048 0.0135 -0.0087 687 TYR A CD2 5276 C CE1 . TYR A 646 ? 0.2395 0.2737 0.2211 -0.0009 0.0101 -0.0130 687 TYR A CE1 5277 C CE2 . TYR A 646 ? 0.2662 0.3008 0.2441 -0.0039 0.0160 -0.0111 687 TYR A CE2 5278 C CZ . TYR A 646 ? 0.2591 0.2942 0.2391 -0.0020 0.0139 -0.0133 687 TYR A CZ 5279 O OH . TYR A 646 ? 0.2797 0.3158 0.2606 -0.0010 0.0161 -0.0156 687 TYR A OH 5280 N N . ARG A 647 ? 0.2141 0.2405 0.1959 -0.0006 -0.0030 -0.0066 688 ARG A N 5281 C CA . ARG A 647 ? 0.1957 0.2196 0.1776 -0.0001 -0.0060 -0.0057 688 ARG A CA 5282 C C . ARG A 647 ? 0.2061 0.2295 0.1940 0.0005 -0.0083 -0.0069 688 ARG A C 5283 O O . ARG A 647 ? 0.2395 0.2603 0.2280 0.0009 -0.0110 -0.0065 688 ARG A O 5284 C CB . ARG A 647 ? 0.2003 0.2231 0.1790 0.0024 -0.0079 -0.0060 688 ARG A CB 5285 C CG . ARG A 647 ? 0.2278 0.2513 0.2026 0.0018 -0.0065 -0.0054 688 ARG A CG 5286 C CD . ARG A 647 ? 0.2020 0.2246 0.1756 0.0036 -0.0082 -0.0050 688 ARG A CD 5287 N NE . ARG A 647 ? 0.2288 0.2514 0.2036 0.0066 -0.0083 -0.0061 688 ARG A NE 5288 C CZ . ARG A 647 ? 0.2600 0.2817 0.2347 0.0089 -0.0091 -0.0057 688 ARG A CZ 5289 N NH1 . ARG A 647 ? 0.2581 0.2792 0.2324 0.0122 -0.0084 -0.0065 688 ARG A NH1 5290 N NH2 . ARG A 647 ? 0.2581 0.2793 0.2327 0.0086 -0.0105 -0.0046 688 ARG A NH2 5291 N N . HIS A 648 ? 0.2207 0.2465 0.2132 0.0008 -0.0077 -0.0087 689 HIS A N 5292 C CA . HIS A 648 ? 0.2198 0.2454 0.2189 0.0018 -0.0110 -0.0106 689 HIS A CA 5293 C C . HIS A 648 ? 0.2356 0.2614 0.2413 -0.0019 -0.0096 -0.0090 689 HIS A C 5294 O O . HIS A 648 ? 0.2656 0.2938 0.2733 -0.0043 -0.0053 -0.0077 689 HIS A O 5295 C CB . HIS A 648 ? 0.2216 0.2499 0.2239 0.0036 -0.0110 -0.0130 689 HIS A CB 5296 C CG . HIS A 648 ? 0.2095 0.2368 0.2159 0.0062 -0.0160 -0.0158 689 HIS A CG 5297 N ND1 . HIS A 648 ? 0.2185 0.2460 0.2338 0.0047 -0.0185 -0.0168 689 HIS A ND1 5298 C CD2 . HIS A 648 ? 0.2212 0.2468 0.2236 0.0106 -0.0190 -0.0178 689 HIS A CD2 5299 C CE1 . HIS A 648 ? 0.2325 0.2584 0.2491 0.0082 -0.0239 -0.0200 689 HIS A CE1 5300 N NE2 . HIS A 648 ? 0.2181 0.2427 0.2259 0.0121 -0.0242 -0.0205 689 HIS A NE2 5301 N N . VAL A 649 ? 0.2097 0.2328 0.2192 -0.0021 -0.0130 -0.0093 690 VAL A N 5302 C CA . VAL A 649 ? 0.2177 0.2402 0.2340 -0.0058 -0.0115 -0.0070 690 VAL A CA 5303 C C . VAL A 649 ? 0.2197 0.2455 0.2486 -0.0072 -0.0114 -0.0088 690 VAL A C 5304 O O . VAL A 649 ? 0.2346 0.2612 0.2706 -0.0107 -0.0077 -0.0064 690 VAL A O 5305 C CB . VAL A 649 ? 0.2287 0.2462 0.2449 -0.0056 -0.0153 -0.0065 690 VAL A CB 5306 C CG1 A VAL A 649 ? 0.1951 0.2111 0.2204 -0.0093 -0.0142 -0.0043 690 VAL A CG1 5307 C CG1 B VAL A 649 ? 0.2393 0.2542 0.2449 -0.0043 -0.0151 -0.0046 690 VAL A CG1 5308 C CG2 A VAL A 649 ? 0.2236 0.2387 0.2295 -0.0050 -0.0143 -0.0041 690 VAL A CG2 5309 C CG2 B VAL A 649 ? 0.2599 0.2761 0.2798 -0.0026 -0.0213 -0.0107 690 VAL A CG2 5310 N N . ILE A 650 ? 0.2262 0.2535 0.2579 -0.0042 -0.0152 -0.0126 691 ILE A N 5311 C CA . ILE A 650 ? 0.2207 0.2515 0.2656 -0.0051 -0.0163 -0.0149 691 ILE A CA 5312 C C . ILE A 650 ? 0.2339 0.2697 0.2806 -0.0056 -0.0114 -0.0146 691 ILE A C 5313 O O . ILE A 650 ? 0.2394 0.2788 0.2974 -0.0081 -0.0086 -0.0143 691 ILE A O 5314 C CB . ILE A 650 ? 0.2370 0.2668 0.2846 -0.0011 -0.0239 -0.0196 691 ILE A CB 5315 C CG1 . ILE A 650 ? 0.2498 0.2740 0.2928 0.0006 -0.0290 -0.0205 691 ILE A CG1 5316 C CG2 . ILE A 650 ? 0.2598 0.2935 0.3243 -0.0025 -0.0260 -0.0221 691 ILE A CG2 5317 C CD1 . ILE A 650 ? 0.2498 0.2717 0.3003 -0.0034 -0.0286 -0.0185 691 ILE A CD1 5318 N N A TYR A 651 ? 0.2238 0.2597 0.2602 -0.0032 -0.0100 -0.0148 692 TYR A N 5319 N N B TYR A 651 ? 0.2269 0.2629 0.2632 -0.0033 -0.0098 -0.0146 692 TYR A N 5320 C CA A TYR A 651 ? 0.2146 0.2546 0.2524 -0.0032 -0.0059 -0.0151 692 TYR A CA 5321 C CA B TYR A 651 ? 0.2218 0.2619 0.2598 -0.0026 -0.0066 -0.0156 692 TYR A CA 5322 C C A TYR A 651 ? 0.2237 0.2627 0.2504 -0.0040 -0.0010 -0.0125 692 TYR A C 5323 C C B TYR A 651 ? 0.2254 0.2663 0.2554 -0.0035 -0.0007 -0.0136 692 TYR A C 5324 O O A TYR A 651 ? 0.2196 0.2553 0.2371 -0.0030 -0.0025 -0.0116 692 TYR A O 5325 O O B TYR A 651 ? 0.2251 0.2690 0.2567 -0.0026 0.0017 -0.0148 692 TYR A O 5326 C CB A TYR A 651 ? 0.2252 0.2658 0.2618 0.0011 -0.0098 -0.0184 692 TYR A CB 5327 C CB B TYR A 651 ? 0.2250 0.2647 0.2604 0.0019 -0.0113 -0.0188 692 TYR A CB 5328 C CG A TYR A 651 ? 0.2013 0.2428 0.2482 0.0028 -0.0158 -0.0217 692 TYR A CG 5329 C CG B TYR A 651 ? 0.2234 0.2637 0.2685 0.0034 -0.0172 -0.0219 692 TYR A CG 5330 C CD1 A TYR A 651 ? 0.2184 0.2648 0.2799 0.0010 -0.0149 -0.0229 692 TYR A CD1 5331 C CD1 B TYR A 651 ? 0.2334 0.2780 0.2932 0.0012 -0.0166 -0.0229 692 TYR A CD1 5332 C CD2 A TYR A 651 ? 0.2227 0.2604 0.2652 0.0065 -0.0225 -0.0240 692 TYR A CD2 5333 C CD2 B TYR A 651 ? 0.2218 0.2582 0.2618 0.0073 -0.0236 -0.0242 692 TYR A CD2 5334 C CE1 A TYR A 651 ? 0.1999 0.2474 0.2725 0.0026 -0.0213 -0.0265 692 TYR A CE1 5335 C CE1 B TYR A 651 ? 0.2304 0.2756 0.3004 0.0025 -0.0229 -0.0263 692 TYR A CE1 5336 C CE2 A TYR A 651 ? 0.2232 0.2612 0.2742 0.0084 -0.0288 -0.0276 692 TYR A CE2 5337 C CE2 B TYR A 651 ? 0.2355 0.2718 0.2836 0.0091 -0.0300 -0.0277 692 TYR A CE2 5338 C CZ A TYR A 651 ? 0.2174 0.2604 0.2839 0.0065 -0.0289 -0.0291 692 TYR A CZ 5339 C CZ B TYR A 651 ? 0.2281 0.2690 0.2917 0.0066 -0.0301 -0.0289 692 TYR A CZ 5340 O OH A TYR A 651 ? 0.2214 0.2652 0.2984 0.0085 -0.0360 -0.0332 692 TYR A OH 5341 O OH B TYR A 651 ? 0.2532 0.2940 0.3260 0.0085 -0.0374 -0.0329 692 TYR A OH 5342 N N A ALA A 652 ? 0.2240 0.2659 0.2520 -0.0056 0.0046 -0.0116 693 ALA A N 5343 N N B ALA A 652 ? 0.2232 0.2612 0.2445 -0.0048 0.0012 -0.0109 693 ALA A N 5344 C CA A ALA A 652 ? 0.2192 0.2602 0.2366 -0.0052 0.0081 -0.0107 693 ALA A CA 5345 C CA B ALA A 652 ? 0.2252 0.2632 0.2380 -0.0050 0.0055 -0.0099 693 ALA A CA 5346 C C A ALA A 652 ? 0.2250 0.2698 0.2466 -0.0051 0.0124 -0.0120 693 ALA A C 5347 C C B ALA A 652 ? 0.2225 0.2638 0.2402 -0.0069 0.0112 -0.0094 693 ALA A C 5348 O O A ALA A 652 ? 0.2365 0.2847 0.2691 -0.0062 0.0141 -0.0124 693 ALA A O 5349 O O B ALA A 652 ? 0.2312 0.2743 0.2584 -0.0088 0.0127 -0.0086 693 ALA A O 5350 C CB A ALA A 652 ? 0.2356 0.2738 0.2459 -0.0075 0.0110 -0.0074 693 ALA A CB 5351 C CB B ALA A 652 ? 0.2245 0.2591 0.2288 -0.0062 0.0060 -0.0072 693 ALA A CB 5352 N N A PRO A 653 ? 0.2138 0.2582 0.2278 -0.0039 0.0143 -0.0127 694 PRO A N 5353 N N B PRO A 653 ? 0.2268 0.2689 0.2386 -0.0062 0.0146 -0.0099 694 PRO A N 5354 C CA A PRO A 653 ? 0.2158 0.2631 0.2325 -0.0038 0.0191 -0.0138 694 PRO A CA 5355 C CA B PRO A 653 ? 0.2378 0.2826 0.2525 -0.0074 0.0207 -0.0095 694 PRO A CA 5356 C C A PRO A 653 ? 0.2188 0.2668 0.2364 -0.0064 0.0249 -0.0113 694 PRO A C 5357 C C B PRO A 653 ? 0.2364 0.2790 0.2471 -0.0099 0.0249 -0.0058 694 PRO A C 5358 O O A PRO A 653 ? 0.2386 0.2833 0.2483 -0.0079 0.0257 -0.0087 694 PRO A O 5359 O O B PRO A 653 ? 0.2633 0.3020 0.2642 -0.0101 0.0233 -0.0041 694 PRO A O 5360 C CB A PRO A 653 ? 0.2247 0.2695 0.2307 -0.0024 0.0197 -0.0147 694 PRO A CB 5361 C CB B PRO A 653 ? 0.2373 0.2815 0.2435 -0.0056 0.0223 -0.0111 694 PRO A CB 5362 C CG A PRO A 653 ? 0.2184 0.2605 0.2206 -0.0011 0.0143 -0.0147 694 PRO A CG 5363 C CG B PRO A 653 ? 0.2365 0.2791 0.2402 -0.0034 0.0168 -0.0128 694 PRO A CG 5364 C CD A PRO A 653 ? 0.2184 0.2594 0.2221 -0.0026 0.0122 -0.0127 694 PRO A CD 5365 C CD B PRO A 653 ? 0.2161 0.2564 0.2191 -0.0041 0.0129 -0.0111 694 PRO A CD 5366 N N A SER A 654 ? 0.2163 0.2686 0.2439 -0.0069 0.0291 -0.0119 695 SER A N 5367 N N B SER A 654 ? 0.2444 0.2895 0.2625 -0.0116 0.0303 -0.0044 695 SER A N 5368 C CA A SER A 654 ? 0.2195 0.2723 0.2479 -0.0093 0.0361 -0.0090 695 SER A CA 5369 C CA B SER A 654 ? 0.2378 0.2803 0.2501 -0.0136 0.0358 -0.0003 695 SER A CA 5370 C C A SER A 654 ? 0.2420 0.2912 0.2551 -0.0089 0.0400 -0.0078 695 SER A C 5371 C C B SER A 654 ? 0.2375 0.2777 0.2350 -0.0120 0.0389 -0.0005 695 SER A C 5372 O O A SER A 654 ? 0.2542 0.3029 0.2610 -0.0068 0.0401 -0.0104 695 SER A O 5373 O O B SER A 654 ? 0.2333 0.2756 0.2301 -0.0102 0.0392 -0.0038 695 SER A O 5374 C CB A SER A 654 ? 0.2235 0.2821 0.2652 -0.0092 0.0410 -0.0102 695 SER A CB 5375 C CB B SER A 654 ? 0.2446 0.2909 0.2700 -0.0156 0.0419 0.0012 695 SER A CB 5376 O OG A SER A 654 ? 0.2376 0.2965 0.2791 -0.0111 0.0492 -0.0071 695 SER A OG 5377 O OG B SER A 654 ? 0.2753 0.3203 0.2939 -0.0162 0.0501 0.0044 695 SER A OG 5378 N N A SER A 655 ? 0.2363 0.2826 0.2436 -0.0107 0.0433 -0.0040 696 SER A N 5379 N N B SER A 655 ? 0.2058 0.2411 0.1913 -0.0125 0.0405 0.0027 696 SER A N 5380 C CA A SER A 655 ? 0.2762 0.3183 0.2678 -0.0100 0.0466 -0.0028 696 SER A CA 5381 C CA B SER A 655 ? 0.2696 0.3021 0.2406 -0.0107 0.0424 0.0019 696 SER A CA 5382 C C A SER A 655 ? 0.2909 0.3350 0.2813 -0.0089 0.0542 -0.0038 696 SER A C 5383 C C B SER A 655 ? 0.2769 0.3103 0.2458 -0.0105 0.0512 0.0030 696 SER A C 5384 O O A SER A 655 ? 0.3103 0.3507 0.2866 -0.0074 0.0568 -0.0039 696 SER A O 5385 O O B SER A 655 ? 0.3317 0.3616 0.2867 -0.0088 0.0535 0.0028 696 SER A O 5386 C CB A SER A 655 ? 0.2942 0.3317 0.2792 -0.0118 0.0474 0.0020 696 SER A CB 5387 C CB B SER A 655 ? 0.2709 0.2975 0.2284 -0.0105 0.0391 0.0042 696 SER A CB 5388 O OG A SER A 655 ? 0.3938 0.4312 0.3787 -0.0128 0.0556 0.0054 696 SER A OG 5389 O OG B SER A 655 ? 0.3181 0.3422 0.2773 -0.0124 0.0400 0.0088 696 SER A OG 5390 N N A HIS A 656 ? 0.2788 0.3285 0.2840 -0.0091 0.0572 -0.0049 697 HIS A N 5391 C CA A HIS A 656 ? 0.3017 0.3542 0.3085 -0.0076 0.0648 -0.0062 697 HIS A CA 5392 C C A HIS A 656 ? 0.3070 0.3631 0.3203 -0.0053 0.0624 -0.0112 697 HIS A C 5393 O O A HIS A 656 ? 0.3257 0.3837 0.3394 -0.0035 0.0679 -0.0131 697 HIS A O 5394 C CB A HIS A 656 ? 0.3186 0.3750 0.3386 -0.0098 0.0719 -0.0030 697 HIS A CB 5395 C CG A HIS A 656 ? 0.3445 0.3967 0.3585 -0.0121 0.0747 0.0024 697 HIS A CG 5396 N ND1 A HIS A 656 ? 0.3634 0.4112 0.3628 -0.0113 0.0817 0.0054 697 HIS A ND1 5397 C CD2 A HIS A 656 ? 0.3724 0.4229 0.3910 -0.0147 0.0707 0.0053 697 HIS A CD2 5398 C CE1 A HIS A 656 ? 0.4091 0.4528 0.4049 -0.0135 0.0823 0.0105 697 HIS A CE1 5399 N NE2 A HIS A 656 ? 0.3534 0.3987 0.3613 -0.0157 0.0757 0.0104 697 HIS A NE2 5400 N N A ASN A 657 ? 0.2787 0.3352 0.2965 -0.0050 0.0544 -0.0131 698 ASN A N 5401 C CA A ASN A 657 ? 0.2627 0.3220 0.2872 -0.0026 0.0516 -0.0171 698 ASN A CA 5402 C C A ASN A 657 ? 0.2574 0.3146 0.2806 -0.0019 0.0430 -0.0182 698 ASN A C 5403 O O A ASN A 657 ? 0.2495 0.3085 0.2820 -0.0026 0.0389 -0.0178 698 ASN A O 5404 C CB A ASN A 657 ? 0.2591 0.3251 0.3023 -0.0027 0.0538 -0.0178 698 ASN A CB 5405 C CG A ASN A 657 ? 0.2375 0.3060 0.2880 0.0003 0.0500 -0.0219 698 ASN A CG 5406 O OD1 A ASN A 657 ? 0.2347 0.2999 0.2761 0.0024 0.0475 -0.0239 698 ASN A OD1 5407 N ND2 A ASN A 657 ? 0.2397 0.3140 0.3075 0.0006 0.0496 -0.0230 698 ASN A ND2 5408 N N . LYS A 658 ? 0.2646 0.3179 0.2769 -0.0004 0.0403 -0.0198 699 LYS A N 5409 C CA A LYS A 658 ? 0.2320 0.2831 0.2429 0.0004 0.0332 -0.0203 699 LYS A CA 5410 C CA B LYS A 658 ? 0.3120 0.3609 0.3153 -0.0005 0.0349 -0.0193 699 LYS A CA 5411 C C A LYS A 658 ? 0.2405 0.2942 0.2621 0.0021 0.0293 -0.0219 699 LYS A C 5412 O O A LYS A 658 ? 0.2367 0.2888 0.2578 0.0026 0.0239 -0.0214 699 LYS A O 5413 C CB A LYS A 658 ? 0.2414 0.2885 0.2419 0.0016 0.0316 -0.0219 699 LYS A CB 5414 C CB B LYS A 658 ? 0.3088 0.3552 0.3062 0.0016 0.0334 -0.0222 699 LYS A CB 5415 C CG A LYS A 658 ? 0.2557 0.2990 0.2443 0.0002 0.0324 -0.0204 699 LYS A CG 5416 C CG B LYS A 658 ? 0.3376 0.3792 0.3225 0.0011 0.0317 -0.0219 699 LYS A CG 5417 C CD A LYS A 658 ? 0.2713 0.3130 0.2583 -0.0013 0.0284 -0.0176 699 LYS A CD 5418 C CD B LYS A 658 ? 0.3394 0.3795 0.3233 0.0001 0.0266 -0.0198 699 LYS A CD 5419 C CE A LYS A 658 ? 0.2864 0.3238 0.2617 -0.0018 0.0268 -0.0169 699 LYS A CE 5420 C CE B LYS A 658 ? 0.3439 0.3806 0.3177 -0.0012 0.0259 -0.0181 699 LYS A CE 5421 N NZ A LYS A 658 ? 0.3238 0.3591 0.2896 -0.0016 0.0306 -0.0176 699 LYS A NZ 5422 N NZ B LYS A 658 ? 0.3449 0.3786 0.3097 -0.0004 0.0263 -0.0203 699 LYS A NZ 5423 N N A TYR A 659 ? 0.2340 0.2915 0.2645 0.0035 0.0319 -0.0239 700 TYR A N 5424 C CA A TYR A 659 ? 0.2308 0.2906 0.2712 0.0059 0.0275 -0.0256 700 TYR A CA 5425 C C A TYR A 659 ? 0.2289 0.2914 0.2793 0.0048 0.0241 -0.0248 700 TYR A C 5426 O O A TYR A 659 ? 0.2543 0.3170 0.3095 0.0070 0.0184 -0.0261 700 TYR A O 5427 C CB A TYR A 659 ? 0.2288 0.2924 0.2777 0.0079 0.0308 -0.0281 700 TYR A CB 5428 C CG A TYR A 659 ? 0.2422 0.3029 0.2831 0.0098 0.0330 -0.0300 700 TYR A CG 5429 C CD1 A TYR A 659 ? 0.2668 0.3224 0.2988 0.0109 0.0291 -0.0301 700 TYR A CD1 5430 C CD2 A TYR A 659 ? 0.2454 0.3085 0.2892 0.0106 0.0390 -0.0318 700 TYR A CD2 5431 C CE1 A TYR A 659 ? 0.2688 0.3214 0.2953 0.0125 0.0308 -0.0321 700 TYR A CE1 5432 C CE2 A TYR A 659 ? 0.2399 0.2996 0.2766 0.0126 0.0406 -0.0341 700 TYR A CE2 5433 C CZ A TYR A 659 ? 0.2815 0.3359 0.3099 0.0133 0.0361 -0.0343 700 TYR A CZ 5434 O OH A TYR A 659 ? 0.2805 0.3313 0.3036 0.0150 0.0373 -0.0368 700 TYR A OH 5435 N N A ALA A 660 ? 0.2268 0.2909 0.2803 0.0016 0.0278 -0.0227 701 ALA A N 5436 C CA A ALA A 660 ? 0.2228 0.2896 0.2882 0.0001 0.0253 -0.0221 701 ALA A CA 5437 C C A ALA A 660 ? 0.2398 0.3024 0.2985 -0.0013 0.0211 -0.0201 701 ALA A C 5438 O O A ALA A 660 ? 0.2490 0.3080 0.2965 -0.0029 0.0234 -0.0178 701 ALA A O 5439 C CB A ALA A 660 ? 0.2201 0.2911 0.2949 -0.0028 0.0329 -0.0203 701 ALA A CB 5440 N N A GLY A 661 ? 0.2338 0.2964 0.2990 -0.0005 0.0145 -0.0213 702 GLY A N 5441 C CA A GLY A 661 ? 0.2376 0.2965 0.2986 -0.0020 0.0110 -0.0196 702 GLY A CA 5442 C C A GLY A 661 ? 0.2383 0.2990 0.3089 -0.0058 0.0142 -0.0174 702 GLY A C 5443 O O A GLY A 661 ? 0.2612 0.3269 0.3465 -0.0068 0.0164 -0.0182 702 GLY A O 5444 N N A GLU A 662 ? 0.2382 0.2949 0.3012 -0.0080 0.0150 -0.0144 703 GLU A N 5445 C CA A GLU A 662 ? 0.2402 0.2971 0.3114 -0.0117 0.0176 -0.0117 703 GLU A CA 5446 C C A GLU A 662 ? 0.2517 0.3049 0.3233 -0.0118 0.0106 -0.0120 703 GLU A C 5447 O O A GLU A 662 ? 0.2523 0.3015 0.3121 -0.0098 0.0067 -0.0124 703 GLU A O 5448 C CB A GLU A 662 ? 0.2497 0.3042 0.3108 -0.0138 0.0249 -0.0075 703 GLU A CB 5449 C CG A GLU A 662 ? 0.2650 0.3193 0.3347 -0.0176 0.0291 -0.0038 703 GLU A CG 5450 C CD A GLU A 662 ? 0.2604 0.3210 0.3491 -0.0188 0.0326 -0.0047 703 GLU A CD 5451 O OE1 A GLU A 662 ? 0.2841 0.3480 0.3734 -0.0186 0.0397 -0.0042 703 GLU A OE1 5452 O OE2 A GLU A 662 ? 0.2575 0.3200 0.3611 -0.0197 0.0277 -0.0065 703 GLU A OE2 5453 N N . SER A 663 ? 0.2712 0.3256 0.3572 -0.0140 0.0091 -0.0120 704 SER A N 5454 C CA A SER A 663 ? 0.2577 0.3076 0.3439 -0.0142 0.0027 -0.0124 704 SER A CA 5455 C CA B SER A 663 ? 0.2528 0.3024 0.3371 -0.0140 0.0028 -0.0122 704 SER A CA 5456 C C . SER A 663 ? 0.2476 0.2935 0.3302 -0.0175 0.0063 -0.0077 704 SER A C 5457 O O . SER A 663 ? 0.2798 0.3270 0.3671 -0.0206 0.0135 -0.0042 704 SER A O 5458 C CB A SER A 663 ? 0.2550 0.3073 0.3582 -0.0139 -0.0038 -0.0162 704 SER A CB 5459 C CB B SER A 663 ? 0.2507 0.3020 0.3495 -0.0131 -0.0046 -0.0164 704 SER A CB 5460 O OG A SER A 663 ? 0.2589 0.3164 0.3796 -0.0171 0.0010 -0.0153 704 SER A OG 5461 O OG B SER A 663 ? 0.2364 0.2906 0.3356 -0.0094 -0.0077 -0.0201 704 SER A OG 5462 N N . PHE A 664 ? 0.2316 0.2720 0.3060 -0.0166 0.0014 -0.0076 705 PHE A N 5463 C CA . PHE A 664 ? 0.2261 0.2616 0.2947 -0.0191 0.0040 -0.0030 705 PHE A CA 5464 C C . PHE A 664 ? 0.2190 0.2548 0.2782 -0.0202 0.0122 0.0010 705 PHE A C 5465 O O . PHE A 664 ? 0.2288 0.2635 0.2908 -0.0231 0.0179 0.0051 705 PHE A O 5466 C CB . PHE A 664 ? 0.2315 0.2656 0.3147 -0.0224 0.0035 -0.0017 705 PHE A CB 5467 C CG . PHE A 664 ? 0.2172 0.2488 0.3060 -0.0207 -0.0060 -0.0059 705 PHE A CG 5468 C CD1 . PHE A 664 ? 0.2267 0.2531 0.3029 -0.0180 -0.0110 -0.0068 705 PHE A CD1 5469 C CD2 . PHE A 664 ? 0.2100 0.2441 0.3169 -0.0219 -0.0096 -0.0090 705 PHE A CD2 5470 C CE1 . PHE A 664 ? 0.2439 0.2672 0.3236 -0.0158 -0.0194 -0.0110 705 PHE A CE1 5471 C CE2 . PHE A 664 ? 0.2433 0.2743 0.3541 -0.0199 -0.0188 -0.0134 705 PHE A CE2 5472 C CZ . PHE A 664 ? 0.2277 0.2530 0.3240 -0.0167 -0.0235 -0.0144 705 PHE A CZ 5473 N N . PRO A 665 ? 0.2249 0.2612 0.2718 -0.0176 0.0124 -0.0003 706 PRO A N 5474 C CA . PRO A 665 ? 0.2325 0.2692 0.2703 -0.0181 0.0195 0.0024 706 PRO A CA 5475 C C . PRO A 665 ? 0.2327 0.2642 0.2611 -0.0196 0.0223 0.0071 706 PRO A C 5476 O O . PRO A 665 ? 0.2644 0.2955 0.2881 -0.0207 0.0292 0.0102 706 PRO A O 5477 C CB . PRO A 665 ? 0.2315 0.2685 0.2585 -0.0148 0.0167 -0.0006 706 PRO A CB 5478 C CG . PRO A 665 ? 0.2445 0.2795 0.2709 -0.0128 0.0092 -0.0028 706 PRO A CG 5479 C CD . PRO A 665 ? 0.2309 0.2673 0.2723 -0.0139 0.0065 -0.0042 706 PRO A CD 5480 N N . GLY A 666 ? 0.2330 0.2599 0.2569 -0.0191 0.0171 0.0077 707 GLY A N 5481 C CA . GLY A 666 ? 0.2380 0.2595 0.2523 -0.0201 0.0193 0.0125 707 GLY A CA 5482 C C . GLY A 666 ? 0.2318 0.2518 0.2542 -0.0234 0.0247 0.0168 707 GLY A C 5483 O O . GLY A 666 ? 0.2595 0.2767 0.2737 -0.0243 0.0308 0.0214 707 GLY A O 5484 N N . ILE A 667 ? 0.2322 0.2539 0.2709 -0.0252 0.0226 0.0155 708 ILE A N 5485 C CA . ILE A 667 ? 0.2422 0.2632 0.2916 -0.0288 0.0285 0.0198 708 ILE A CA 5486 C C . ILE A 667 ? 0.2541 0.2801 0.3073 -0.0297 0.0371 0.0209 708 ILE A C 5487 O O . ILE A 667 ? 0.2756 0.2995 0.3270 -0.0315 0.0450 0.0262 708 ILE A O 5488 C CB . ILE A 667 ? 0.2425 0.2644 0.3109 -0.0307 0.0238 0.0176 708 ILE A CB 5489 C CG1 . ILE A 667 ? 0.2573 0.2741 0.3211 -0.0290 0.0150 0.0156 708 ILE A CG1 5490 C CG2 . ILE A 667 ? 0.2618 0.2817 0.3416 -0.0349 0.0303 0.0230 708 ILE A CG2 5491 C CD1 . ILE A 667 ? 0.2612 0.2786 0.3422 -0.0298 0.0085 0.0117 708 ILE A CD1 5492 N N . TYR A 668 ? 0.2478 0.2799 0.3059 -0.0281 0.0357 0.0161 709 TYR A N 5493 C CA . TYR A 668 ? 0.2630 0.3004 0.3262 -0.0285 0.0434 0.0163 709 TYR A CA 5494 C C . TYR A 668 ? 0.2648 0.2991 0.3103 -0.0275 0.0506 0.0200 709 TYR A C 5495 O O . TYR A 668 ? 0.2738 0.3084 0.3212 -0.0290 0.0595 0.0239 709 TYR A O 5496 C CB . TYR A 668 ? 0.2442 0.2876 0.3122 -0.0261 0.0397 0.0103 709 TYR A CB 5497 C CG . TYR A 668 ? 0.2617 0.3108 0.3359 -0.0261 0.0475 0.0101 709 TYR A CG 5498 C CD1 . TYR A 668 ? 0.2989 0.3536 0.3941 -0.0281 0.0498 0.0094 709 TYR A CD1 5499 C CD2 . TYR A 668 ? 0.2980 0.3464 0.3573 -0.0241 0.0527 0.0107 709 TYR A CD2 5500 C CE1 . TYR A 668 ? 0.3082 0.3685 0.4105 -0.0279 0.0578 0.0094 709 TYR A CE1 5501 C CE2 . TYR A 668 ? 0.3031 0.3564 0.3677 -0.0238 0.0606 0.0105 709 TYR A CE2 5502 C CZ . TYR A 668 ? 0.3197 0.3790 0.4058 -0.0257 0.0634 0.0100 709 TYR A CZ 5503 O OH . TYR A 668 ? 0.3273 0.3921 0.4207 -0.0252 0.0713 0.0096 709 TYR A OH 5504 N N . ASP A 669 ? 0.2633 0.2947 0.2919 -0.0248 0.0467 0.0185 710 ASP A N 5505 C CA . ASP A 669 ? 0.2748 0.3027 0.2858 -0.0234 0.0520 0.0212 710 ASP A CA 5506 C C . ASP A 669 ? 0.2943 0.3156 0.2983 -0.0249 0.0561 0.0278 710 ASP A C 5507 O O . ASP A 669 ? 0.3101 0.3290 0.3040 -0.0244 0.0638 0.0313 710 ASP A O 5508 C CB . ASP A 669 ? 0.2766 0.3028 0.2731 -0.0203 0.0459 0.0178 710 ASP A CB 5509 C CG . ASP A 669 ? 0.2980 0.3296 0.2975 -0.0184 0.0444 0.0124 710 ASP A CG 5510 O OD1 . ASP A 669 ? 0.3186 0.3550 0.3279 -0.0188 0.0492 0.0113 710 ASP A OD1 5511 O OD2 . ASP A 669 ? 0.3257 0.3565 0.3183 -0.0164 0.0384 0.0093 710 ASP A OD2 5512 N N . ALA A 670 ? 0.2813 0.2988 0.2890 -0.0263 0.0513 0.0296 711 ALA A N 5513 C CA . ALA A 670 ? 0.2981 0.3086 0.3003 -0.0278 0.0552 0.0364 711 ALA A CA 5514 C C . ALA A 670 ? 0.2977 0.3096 0.3117 -0.0307 0.0652 0.0408 711 ALA A C 5515 O O . ALA A 670 ? 0.3269 0.3338 0.3316 -0.0309 0.0727 0.0469 711 ALA A O 5516 C CB . ALA A 670 ? 0.2943 0.3005 0.3007 -0.0287 0.0478 0.0370 711 ALA A CB 5517 N N . LEU A 671 ? 0.2987 0.3177 0.3329 -0.0326 0.0657 0.0377 712 LEU A N 5518 C CA . LEU A 671 ? 0.3040 0.3257 0.3530 -0.0356 0.0754 0.0415 712 LEU A CA 5519 C C . LEU A 671 ? 0.3267 0.3525 0.3716 -0.0341 0.0847 0.0416 712 LEU A C 5520 O O . LEU A 671 ? 0.3384 0.3655 0.3917 -0.0360 0.0947 0.0459 712 LEU A O 5521 C CB . LEU A 671 ? 0.3011 0.3288 0.3757 -0.0382 0.0714 0.0379 712 LEU A CB 5522 C CG . LEU A 671 ? 0.2859 0.3091 0.3699 -0.0407 0.0651 0.0390 712 LEU A CG 5523 C CD1 . LEU A 671 ? 0.2843 0.3136 0.3899 -0.0417 0.0573 0.0326 712 LEU A CD1 5524 C CD2 . LEU A 671 ? 0.2882 0.3067 0.3777 -0.0441 0.0739 0.0470 712 LEU A CD2 5525 N N . PHE A 672 ? 0.3255 0.3537 0.3593 -0.0307 0.0814 0.0365 713 PHE A N 5526 C CA . PHE A 672 ? 0.3407 0.3740 0.3742 -0.0291 0.0890 0.0349 713 PHE A CA 5527 C C . PHE A 672 ? 0.3604 0.3885 0.3781 -0.0280 0.0995 0.0408 713 PHE A C 5528 O O . PHE A 672 ? 0.3758 0.3966 0.3724 -0.0259 0.0977 0.0427 713 PHE A O 5529 C CB . PHE A 672 ? 0.3335 0.3695 0.3584 -0.0256 0.0826 0.0282 713 PHE A CB 5530 C CG . PHE A 672 ? 0.3635 0.4048 0.3902 -0.0238 0.0896 0.0258 713 PHE A CG 5531 C CD1 . PHE A 672 ? 0.3743 0.4237 0.4222 -0.0248 0.0903 0.0226 713 PHE A CD1 5532 C CD2 . PHE A 672 ? 0.3809 0.4186 0.3883 -0.0209 0.0956 0.0269 713 PHE A CD2 5533 C CE1 . PHE A 672 ? 0.4095 0.4640 0.4601 -0.0228 0.0972 0.0204 713 PHE A CE1 5534 C CE2 . PHE A 672 ? 0.3897 0.4318 0.3984 -0.0189 0.1026 0.0245 713 PHE A CE2 5535 C CZ . PHE A 672 ? 0.4125 0.4631 0.4430 -0.0199 0.1038 0.0215 713 PHE A CZ 5536 N N . ASP A 673 ? 0.3828 0.4145 0.4105 -0.0291 0.1106 0.0436 714 ASP A N 5537 C CA . ASP A 673 ? 0.4239 0.4504 0.4363 -0.0276 0.1224 0.0496 714 ASP A CA 5538 C C . ASP A 673 ? 0.4405 0.4572 0.4407 -0.0285 0.1231 0.0568 714 ASP A C 5539 O O . ASP A 673 ? 0.4588 0.4683 0.4365 -0.0256 0.1278 0.0606 714 ASP A O 5540 C CB . ASP A 673 ? 0.4299 0.4552 0.4208 -0.0227 0.1227 0.0456 714 ASP A CB 5541 C CG . ASP A 673 ? 0.4781 0.4996 0.4545 -0.0202 0.1359 0.0504 714 ASP A CG 5542 O OD1 . ASP A 673 ? 0.4904 0.5154 0.4805 -0.0220 0.1469 0.0542 714 ASP A OD1 5543 O OD2 . ASP A 673 ? 0.5254 0.5402 0.4764 -0.0162 0.1351 0.0501 714 ASP A OD2 5544 N N . ILE A 674 ? 0.4242 0.4400 0.4389 -0.0322 0.1180 0.0585 715 ILE A N 5545 C CA . ILE A 674 ? 0.4193 0.4254 0.4223 -0.0327 0.1167 0.0647 715 ILE A CA 5546 C C . ILE A 674 ? 0.4532 0.4539 0.4513 -0.0333 0.1305 0.0737 715 ILE A C 5547 O O . ILE A 674 ? 0.4592 0.4503 0.4380 -0.0317 0.1316 0.0792 715 ILE A O 5548 C CB . ILE A 674 ? 0.4146 0.4203 0.4345 -0.0363 0.1078 0.0640 715 ILE A CB 5549 C CG1 . ILE A 674 ? 0.4054 0.4005 0.4111 -0.0360 0.1052 0.0697 715 ILE A CG1 5550 C CG2 . ILE A 674 ? 0.3911 0.4021 0.4393 -0.0409 0.1131 0.0658 715 ILE A CG2 5551 C CD1 . ILE A 674 ? 0.3853 0.3795 0.4023 -0.0380 0.0938 0.0671 715 ILE A CD1 5552 N N . GLU A 675 ? 0.4610 0.4679 0.4759 -0.0353 0.1410 0.0752 716 GLU A N 5553 C CA . GLU A 675 ? 0.5172 0.5194 0.5292 -0.0359 0.1557 0.0843 716 GLU A CA 5554 C C . GLU A 675 ? 0.5445 0.5399 0.5254 -0.0305 0.1622 0.0870 716 GLU A C 5555 O O . GLU A 675 ? 0.5746 0.5631 0.5457 -0.0299 0.1735 0.0954 716 GLU A O 5556 C CB . GLU A 675 ? 0.5152 0.5267 0.5549 -0.0392 0.1658 0.0849 716 GLU A CB 5557 C CG . GLU A 675 ? 0.5287 0.5488 0.5698 -0.0364 0.1698 0.0791 716 GLU A CG 5558 C CD . GLU A 675 ? 0.5371 0.5661 0.5921 -0.0366 0.1574 0.0691 716 GLU A CD 5559 O OE1 . GLU A 675 ? 0.4847 0.5123 0.5411 -0.0376 0.1446 0.0658 716 GLU A OE1 5560 O OE2 . GLU A 675 ? 0.5858 0.6230 0.6499 -0.0353 0.1609 0.0646 716 GLU A OE2 5561 N N . SER A 676 ? 0.5618 0.5585 0.5272 -0.0264 0.1550 0.0798 717 SER A N 5562 C CA . SER A 676 ? 0.5969 0.5873 0.5321 -0.0207 0.1587 0.0803 717 SER A CA 5563 C C . SER A 676 ? 0.6143 0.5946 0.5251 -0.0179 0.1495 0.0814 717 SER A C 5564 O O . SER A 676 ? 0.6422 0.6152 0.5265 -0.0131 0.1521 0.0829 717 SER A O 5565 C CB . SER A 676 ? 0.5911 0.5886 0.5243 -0.0177 0.1564 0.0715 717 SER A CB 5566 O OG . SER A 676 ? 0.5992 0.6059 0.5538 -0.0195 0.1655 0.0706 717 SER A OG 5567 N N . LYS A 677 ? 0.6017 0.5812 0.5209 -0.0206 0.1387 0.0805 718 LYS A N 5568 C CA . LYS A 677 ? 0.6092 0.5800 0.5077 -0.0179 0.1292 0.0811 718 LYS A CA 5569 C C . LYS A 677 ? 0.6422 0.6016 0.5248 -0.0167 0.1363 0.0910 718 LYS A C 5570 O O . LYS A 677 ? 0.6459 0.6039 0.5413 -0.0201 0.1448 0.0980 718 LYS A O 5571 C CB . LYS A 677 ? 0.5927 0.5658 0.5047 -0.0206 0.1161 0.0774 718 LYS A CB 5572 C CG . LYS A 677 ? 0.5744 0.5575 0.4998 -0.0212 0.1087 0.0680 718 LYS A CG 5573 C CD . LYS A 677 ? 0.6360 0.6188 0.5425 -0.0166 0.1025 0.0619 718 LYS A CD 5574 C CE . LYS A 677 ? 0.6323 0.6246 0.5527 -0.0173 0.0960 0.0533 718 LYS A CE 5575 N NZ . LYS A 677 ? 0.6372 0.6312 0.5691 -0.0193 0.0849 0.0505 718 LYS A NZ 5576 N N . VAL A 678 ? 0.6632 0.6142 0.5182 -0.0117 0.1324 0.0915 719 VAL A N 5577 C CA . VAL A 678 ? 0.6953 0.6342 0.5298 -0.0091 0.1391 0.1008 719 VAL A CA 5578 C C . VAL A 678 ? 0.6846 0.6169 0.5240 -0.0116 0.1345 0.1068 719 VAL A C 5579 O O . VAL A 678 ? 0.7078 0.6317 0.5418 -0.0119 0.1432 0.1163 719 VAL A O 5580 C CB . VAL A 678 ? 0.7212 0.6532 0.5233 -0.0021 0.1355 0.0984 719 VAL A CB 5581 C CG1 . VAL A 678 ? 0.7639 0.6832 0.5446 0.0011 0.1310 0.1044 719 VAL A CG1 5582 C CG2 . VAL A 678 ? 0.7511 0.6828 0.5412 0.0012 0.1486 0.0994 719 VAL A CG2 5583 N N . ASP A 679 ? 0.6579 0.5935 0.5079 -0.0134 0.1213 0.1014 720 ASP A N 5584 C CA . ASP A 679 ? 0.6392 0.5690 0.4950 -0.0156 0.1155 0.1057 720 ASP A CA 5585 C C . ASP A 679 ? 0.5983 0.5369 0.4860 -0.0215 0.1128 0.1024 720 ASP A C 5586 O O . ASP A 679 ? 0.5643 0.5087 0.4606 -0.0221 0.1017 0.0948 720 ASP A O 5587 C CB . ASP A 679 ? 0.6431 0.5690 0.4830 -0.0118 0.1016 0.1015 720 ASP A CB 5588 C CG . ASP A 679 ? 0.6657 0.5841 0.5074 -0.0127 0.0954 0.1062 720 ASP A CG 5589 O OD1 . ASP A 679 ? 0.6601 0.5770 0.5181 -0.0169 0.1000 0.1115 720 ASP A OD1 5590 O OD2 . ASP A 679 ? 0.7302 0.6441 0.5577 -0.0091 0.0853 0.1043 720 ASP A OD2 5591 N N . PRO A 680 ? 0.5788 0.5181 0.4842 -0.0258 0.1229 0.1081 721 PRO A N 5592 C CA . PRO A 680 ? 0.5515 0.4992 0.4875 -0.0312 0.1199 0.1043 721 PRO A CA 5593 C C . PRO A 680 ? 0.5290 0.4737 0.4723 -0.0327 0.1079 0.1027 721 PRO A C 5594 O O . PRO A 680 ? 0.5051 0.4572 0.4664 -0.0349 0.1004 0.0959 721 PRO A O 5595 C CB . PRO A 680 ? 0.5631 0.5100 0.5145 -0.0352 0.1336 0.1121 721 PRO A CB 5596 C CG . PRO A 680 ? 0.5970 0.5326 0.5241 -0.0319 0.1430 0.1216 721 PRO A CG 5597 C CD . PRO A 680 ? 0.6018 0.5355 0.5008 -0.0257 0.1381 0.1174 721 PRO A CD 5598 N N . SER A 681 ? 0.5386 0.4722 0.4676 -0.0310 0.1063 0.1090 722 SER A N 5599 C CA . SER A 681 ? 0.5349 0.4650 0.4695 -0.0317 0.0948 0.1074 722 SER A CA 5600 C C . SER A 681 ? 0.5086 0.4445 0.4393 -0.0291 0.0823 0.0978 722 SER A C 5601 O O . SER A 681 ? 0.4713 0.4117 0.4178 -0.0310 0.0742 0.0923 722 SER A O 5602 C CB . SER A 681 ? 0.5622 0.4788 0.4792 -0.0293 0.0950 0.1159 722 SER A CB 5603 O OG . SER A 681 ? 0.5880 0.5016 0.5122 -0.0300 0.0843 0.1141 722 SER A OG 5604 N N . LYS A 682 ? 0.5146 0.4503 0.4241 -0.0246 0.0809 0.0956 723 LYS A N 5605 C CA . LYS A 682 ? 0.4964 0.4377 0.4026 -0.0222 0.0702 0.0869 723 LYS A CA 5606 C C . LYS A 682 ? 0.4570 0.4101 0.3820 -0.0247 0.0695 0.0794 723 LYS A C 5607 O O . LYS A 682 ? 0.4328 0.3906 0.3666 -0.0249 0.0604 0.0730 723 LYS A O 5608 C CB . LYS A 682 ? 0.5275 0.4657 0.4082 -0.0170 0.0692 0.0861 723 LYS A CB 5609 C CG . LYS A 682 ? 0.5839 0.5277 0.4614 -0.0146 0.0586 0.0773 723 LYS A CG 5610 C CD . LYS A 682 ? 0.7000 0.6416 0.5546 -0.0098 0.0586 0.0758 723 LYS A CD 5611 C CE . LYS A 682 ? 0.7429 0.6894 0.5956 -0.0077 0.0479 0.0675 723 LYS A CE 5612 N NZ . LYS A 682 ? 0.8140 0.7580 0.6457 -0.0032 0.0471 0.0654 723 LYS A NZ 5613 N N . ALA A 683 ? 0.4403 0.3980 0.3712 -0.0262 0.0792 0.0802 724 ALA A N 5614 C CA . ALA A 683 ? 0.4107 0.3793 0.3576 -0.0278 0.0786 0.0731 724 ALA A CA 5615 C C . ALA A 683 ? 0.3796 0.3517 0.3510 -0.0318 0.0744 0.0712 724 ALA A C 5616 O O . ALA A 683 ? 0.3599 0.3381 0.3401 -0.0318 0.0666 0.0641 724 ALA A O 5617 C CB . ALA A 683 ? 0.4242 0.3963 0.3733 -0.0284 0.0909 0.0752 724 ALA A CB 5618 N N . TRP A 684 ? 0.3882 0.3556 0.3697 -0.0350 0.0795 0.0776 725 TRP A N 5619 C CA . TRP A 684 ? 0.3651 0.3348 0.3702 -0.0388 0.0748 0.0756 725 TRP A CA 5620 C C . TRP A 684 ? 0.3658 0.3317 0.3676 -0.0373 0.0627 0.0724 725 TRP A C 5621 O O . TRP A 684 ? 0.3400 0.3102 0.3569 -0.0386 0.0557 0.0668 725 TRP A O 5622 C CB . TRP A 684 ? 0.3679 0.3340 0.3875 -0.0431 0.0836 0.0829 725 TRP A CB 5623 C CG . TRP A 684 ? 0.3517 0.3253 0.3833 -0.0451 0.0937 0.0831 725 TRP A CG 5624 C CD1 . TRP A 684 ? 0.3896 0.3617 0.4116 -0.0443 0.1061 0.0891 725 TRP A CD1 5625 C CD2 . TRP A 684 ? 0.3286 0.3123 0.3838 -0.0476 0.0922 0.0771 725 TRP A CD2 5626 N NE1 . TRP A 684 ? 0.3864 0.3678 0.4260 -0.0464 0.1129 0.0869 725 TRP A NE1 5627 C CE2 . TRP A 684 ? 0.3445 0.3331 0.4047 -0.0485 0.1041 0.0796 725 TRP A CE2 5628 C CE3 . TRP A 684 ? 0.3205 0.3094 0.3921 -0.0487 0.0816 0.0695 725 TRP A CE3 5629 C CZ2 . TRP A 684 ? 0.3367 0.3356 0.4200 -0.0507 0.1055 0.0749 725 TRP A CZ2 5630 C CZ3 . TRP A 684 ? 0.3176 0.3162 0.4107 -0.0507 0.0826 0.0648 725 TRP A CZ3 5631 C CH2 . TRP A 684 ? 0.3255 0.3291 0.4246 -0.0518 0.0943 0.0676 725 TRP A CH2 5632 N N . GLY A 685 ? 0.3808 0.3389 0.3629 -0.0342 0.0602 0.0757 726 GLY A N 5633 C CA . GLY A 685 ? 0.3753 0.3309 0.3531 -0.0320 0.0489 0.0721 726 GLY A CA 5634 C C . GLY A 685 ? 0.3483 0.3124 0.3278 -0.0302 0.0419 0.0631 726 GLY A C 5635 O O . GLY A 685 ? 0.3487 0.3144 0.3367 -0.0300 0.0337 0.0583 726 GLY A O 5636 N N . GLU A 686 ? 0.3396 0.3086 0.3103 -0.0285 0.0451 0.0609 727 GLU A N 5637 C CA . GLU A 686 ? 0.3331 0.3095 0.3051 -0.0268 0.0395 0.0531 727 GLU A CA 5638 C C . GLU A 686 ? 0.3005 0.2842 0.2928 -0.0293 0.0389 0.0486 727 GLU A C 5639 O O . GLU A 686 ? 0.2915 0.2792 0.2885 -0.0282 0.0318 0.0427 727 GLU A O 5640 C CB . GLU A 686 ? 0.3528 0.3315 0.3099 -0.0243 0.0432 0.0521 727 GLU A CB 5641 C CG A GLU A 686 ? 0.3555 0.3413 0.3135 -0.0225 0.0375 0.0444 727 GLU A CG 5642 C CD A GLU A 686 ? 0.3676 0.3521 0.3210 -0.0201 0.0278 0.0411 727 GLU A CD 5643 O OE1 A GLU A 686 ? 0.3879 0.3660 0.3346 -0.0192 0.0246 0.0443 727 GLU A OE1 5644 O OE2 A GLU A 686 ? 0.3764 0.3667 0.3337 -0.0191 0.0238 0.0352 727 GLU A OE2 5645 N N . VAL A 687 ? 0.3088 0.2942 0.3141 -0.0326 0.0462 0.0515 728 VAL A N 5646 C CA . VAL A 687 ? 0.2924 0.2841 0.3190 -0.0350 0.0441 0.0470 728 VAL A CA 5647 C C . VAL A 687 ? 0.2867 0.2751 0.3217 -0.0354 0.0352 0.0448 728 VAL A C 5648 O O . VAL A 687 ? 0.2653 0.2580 0.3077 -0.0345 0.0284 0.0384 728 VAL A O 5649 C CB . VAL A 687 ? 0.2987 0.2921 0.3406 -0.0388 0.0533 0.0511 728 VAL A CB 5650 C CG1 . VAL A 687 ? 0.3089 0.3081 0.3747 -0.0413 0.0494 0.0462 728 VAL A CG1 5651 C CG2 . VAL A 687 ? 0.2987 0.2958 0.3323 -0.0378 0.0627 0.0525 728 VAL A CG2 5652 N N . LYS A 688 ? 0.3019 0.2823 0.3347 -0.0364 0.0356 0.0501 729 LYS A N 5653 C CA . LYS A 688 ? 0.2929 0.2690 0.3330 -0.0366 0.0276 0.0483 729 LYS A CA 5654 C C . LYS A 688 ? 0.2954 0.2720 0.3245 -0.0325 0.0190 0.0431 729 LYS A C 5655 O O . LYS A 688 ? 0.2746 0.2526 0.3118 -0.0318 0.0120 0.0379 729 LYS A O 5656 C CB A LYS A 688 ? 0.3103 0.2768 0.3484 -0.0381 0.0301 0.0557 729 LYS A CB 5657 C CB B LYS A 688 ? 0.3107 0.2773 0.3493 -0.0382 0.0301 0.0556 729 LYS A CB 5658 C CG A LYS A 688 ? 0.3149 0.2804 0.3676 -0.0427 0.0387 0.0611 729 LYS A CG 5659 C CG B LYS A 688 ? 0.3118 0.2781 0.3672 -0.0429 0.0380 0.0602 729 LYS A CG 5660 C CD A LYS A 688 ? 0.3322 0.2871 0.3842 -0.0442 0.0405 0.0684 729 LYS A CD 5661 C CD B LYS A 688 ? 0.3386 0.2946 0.3910 -0.0445 0.0423 0.0689 729 LYS A CD 5662 C CE A LYS A 688 ? 0.3494 0.2978 0.3776 -0.0413 0.0442 0.0747 729 LYS A CE 5663 C CE B LYS A 688 ? 0.3559 0.3048 0.4112 -0.0440 0.0337 0.0679 729 LYS A CE 5664 N NZ A LYS A 688 ? 0.3984 0.3375 0.4266 -0.0435 0.0514 0.0843 729 LYS A NZ 5665 N NZ B LYS A 688 ? 0.3962 0.3356 0.4569 -0.0469 0.0381 0.0759 729 LYS A NZ 5666 N N . ARG A 689 ? 0.2776 0.2535 0.2890 -0.0297 0.0198 0.0443 730 ARG A N 5667 C CA . ARG A 689 ? 0.2740 0.2515 0.2771 -0.0259 0.0123 0.0393 730 ARG A CA 5668 C C . ARG A 689 ? 0.2611 0.2464 0.2712 -0.0251 0.0094 0.0324 730 ARG A C 5669 O O . ARG A 689 ? 0.2527 0.2388 0.2649 -0.0231 0.0027 0.0278 730 ARG A O 5670 C CB . ARG A 689 ? 0.2936 0.2697 0.2782 -0.0233 0.0135 0.0413 730 ARG A CB 5671 C CG . ARG A 689 ? 0.3116 0.2881 0.2896 -0.0197 0.0056 0.0371 730 ARG A CG 5672 C CD . ARG A 689 ? 0.3671 0.3415 0.3283 -0.0171 0.0054 0.0390 730 ARG A CD 5673 N NE . ARG A 689 ? 0.3603 0.3405 0.3169 -0.0165 0.0081 0.0362 730 ARG A NE 5674 C CZ . ARG A 689 ? 0.3915 0.3772 0.3489 -0.0148 0.0045 0.0307 730 ARG A CZ 5675 N NH1 . ARG A 689 ? 0.4050 0.3916 0.3676 -0.0133 -0.0015 0.0274 730 ARG A NH1 5676 N NH2 . ARG A 689 ? 0.3866 0.3767 0.3399 -0.0143 0.0072 0.0285 730 ARG A NH2 5677 N N . GLN A 690 ? 0.2478 0.2387 0.2612 -0.0263 0.0148 0.0317 731 GLN A N 5678 C CA . GLN A 690 ? 0.2456 0.2436 0.2656 -0.0253 0.0121 0.0255 731 GLN A CA 5679 C C . GLN A 690 ? 0.2373 0.2364 0.2740 -0.0265 0.0076 0.0220 731 GLN A C 5680 O O . GLN A 690 ? 0.2296 0.2317 0.2684 -0.0242 0.0020 0.0164 731 GLN A O 5681 C CB . GLN A 690 ? 0.2576 0.2610 0.2775 -0.0261 0.0189 0.0257 731 GLN A CB 5682 C CG . GLN A 690 ? 0.2585 0.2610 0.2606 -0.0239 0.0215 0.0272 731 GLN A CG 5683 C CD . GLN A 690 ? 0.2851 0.2888 0.2794 -0.0206 0.0151 0.0228 731 GLN A CD 5684 O OE1 . GLN A 690 ? 0.2789 0.2866 0.2796 -0.0195 0.0110 0.0180 731 GLN A OE1 5685 N NE2 . GLN A 690 ? 0.3596 0.3596 0.3399 -0.0188 0.0139 0.0247 731 GLN A NE2 5686 N N . ILE A 691 ? 0.2405 0.2367 0.2888 -0.0299 0.0100 0.0252 732 ILE A N 5687 C CA . ILE A 691 ? 0.2415 0.2377 0.3060 -0.0309 0.0044 0.0214 732 ILE A CA 5688 C C . ILE A 691 ? 0.2429 0.2346 0.3022 -0.0279 -0.0039 0.0183 732 ILE A C 5689 O O . ILE A 691 ? 0.2509 0.2445 0.3155 -0.0259 -0.0104 0.0123 732 ILE A O 5690 C CB . ILE A 691 ? 0.2366 0.2296 0.3155 -0.0355 0.0087 0.0261 732 ILE A CB 5691 C CG1 . ILE A 691 ? 0.2462 0.2450 0.3335 -0.0382 0.0172 0.0283 732 ILE A CG1 5692 C CG2 . ILE A 691 ? 0.2627 0.2540 0.3585 -0.0364 0.0012 0.0217 732 ILE A CG2 5693 C CD1 . ILE A 691 ? 0.2599 0.2553 0.3591 -0.0427 0.0239 0.0345 732 ILE A CD1 5694 N N . TYR A 692 ? 0.2565 0.2420 0.3054 -0.0272 -0.0038 0.0223 733 TYR A N 5695 C CA . TYR A 692 ? 0.2633 0.2445 0.3066 -0.0240 -0.0110 0.0198 733 TYR A CA 5696 C C . TYR A 692 ? 0.2555 0.2412 0.2905 -0.0198 -0.0148 0.0145 733 TYR A C 5697 O O . TYR A 692 ? 0.2518 0.2368 0.2889 -0.0172 -0.0209 0.0096 733 TYR A O 5698 C CB . TYR A 692 ? 0.2725 0.2474 0.3046 -0.0236 -0.0094 0.0254 733 TYR A CB 5699 C CG . TYR A 692 ? 0.3079 0.2794 0.3300 -0.0196 -0.0150 0.0239 733 TYR A CG 5700 C CD1 . TYR A 692 ? 0.3248 0.2936 0.3519 -0.0174 -0.0217 0.0195 733 TYR A CD1 5701 C CD2 . TYR A 692 ? 0.3143 0.2849 0.3222 -0.0177 -0.0135 0.0270 733 TYR A CD2 5702 C CE1 . TYR A 692 ? 0.3302 0.2958 0.3486 -0.0136 -0.0260 0.0187 733 TYR A CE1 5703 C CE2 . TYR A 692 ? 0.2951 0.2627 0.2956 -0.0143 -0.0183 0.0262 733 TYR A CE2 5704 C CZ . TYR A 692 ? 0.3316 0.2968 0.3378 -0.0122 -0.0241 0.0223 733 TYR A CZ 5705 O OH . TYR A 692 ? 0.3509 0.3136 0.3506 -0.0085 -0.0282 0.0215 733 TYR A OH 5706 N N . VAL A 693 ? 0.2410 0.2306 0.2662 -0.0190 -0.0109 0.0156 734 VAL A N 5707 C CA . VAL A 693 ? 0.2330 0.2267 0.2513 -0.0154 -0.0137 0.0112 734 VAL A CA 5708 C C . VAL A 693 ? 0.2355 0.2334 0.2627 -0.0146 -0.0163 0.0059 734 VAL A C 5709 O O . VAL A 693 ? 0.2563 0.2545 0.2814 -0.0112 -0.0212 0.0016 734 VAL A O 5710 C CB . VAL A 693 ? 0.2403 0.2373 0.2485 -0.0153 -0.0088 0.0132 734 VAL A CB 5711 C CG1 . VAL A 693 ? 0.2624 0.2641 0.2665 -0.0122 -0.0109 0.0087 734 VAL A CG1 5712 C CG2 . VAL A 693 ? 0.2693 0.2614 0.2668 -0.0147 -0.0085 0.0173 734 VAL A CG2 5713 N N . ALA A 694 ? 0.2245 0.2255 0.2622 -0.0176 -0.0132 0.0062 735 ALA A N 5714 C CA . ALA A 694 ? 0.2306 0.2358 0.2774 -0.0166 -0.0164 0.0009 735 ALA A CA 5715 C C . ALA A 694 ? 0.2187 0.2202 0.2732 -0.0154 -0.0237 -0.0028 735 ALA A C 5716 O O . ALA A 694 ? 0.2266 0.2290 0.2797 -0.0117 -0.0290 -0.0080 735 ALA A O 5717 C CB . ALA A 694 ? 0.2296 0.2395 0.2876 -0.0200 -0.0113 0.0021 735 ALA A CB 5718 N N . ALA A 695 ? 0.2266 0.2233 0.2882 -0.0182 -0.0239 -0.0003 736 ALA A N 5719 C CA . ALA A 695 ? 0.2238 0.2159 0.2933 -0.0171 -0.0313 -0.0043 736 ALA A CA 5720 C C . ALA A 695 ? 0.2415 0.2301 0.2989 -0.0121 -0.0363 -0.0072 736 ALA A C 5721 O O . ALA A 695 ? 0.2571 0.2448 0.3152 -0.0086 -0.0426 -0.0128 736 ALA A O 5722 C CB . ALA A 695 ? 0.2358 0.2226 0.3144 -0.0211 -0.0299 -0.0003 736 ALA A CB 5723 N N . PHE A 696 ? 0.2403 0.2271 0.2860 -0.0114 -0.0333 -0.0033 737 PHE A N 5724 C CA . PHE A 696 ? 0.2403 0.2244 0.2754 -0.0067 -0.0370 -0.0055 737 PHE A CA 5725 C C . PHE A 696 ? 0.2350 0.2236 0.2643 -0.0027 -0.0384 -0.0098 737 PHE A C 5726 O O . PHE A 696 ? 0.2401 0.2263 0.2662 0.0016 -0.0434 -0.0142 737 PHE A O 5727 C CB . PHE A 696 ? 0.2540 0.2368 0.2788 -0.0066 -0.0334 -0.0007 737 PHE A CB 5728 C CG . PHE A 696 ? 0.2512 0.2339 0.2661 -0.0018 -0.0357 -0.0029 737 PHE A CG 5729 C CD1 . PHE A 696 ? 0.2798 0.2577 0.2945 0.0017 -0.0410 -0.0062 737 PHE A CD1 5730 C CD2 . PHE A 696 ? 0.2840 0.2715 0.2909 -0.0005 -0.0326 -0.0023 737 PHE A CD2 5731 C CE1 . PHE A 696 ? 0.3038 0.2822 0.3098 0.0066 -0.0420 -0.0082 737 PHE A CE1 5732 C CE2 . PHE A 696 ? 0.2890 0.2768 0.2882 0.0040 -0.0341 -0.0042 737 PHE A CE2 5733 C CZ . PHE A 696 ? 0.2743 0.2577 0.2734 0.0074 -0.0384 -0.0070 737 PHE A CZ 5734 N N . THR A 697 ? 0.2240 0.2183 0.2517 -0.0039 -0.0341 -0.0086 738 THR A N 5735 C CA . THR A 697 ? 0.2163 0.2142 0.2376 -0.0001 -0.0346 -0.0118 738 THR A CA 5736 C C . THR A 697 ? 0.2260 0.2238 0.2536 0.0020 -0.0400 -0.0171 738 THR A C 5737 O O . THR A 697 ? 0.2385 0.2353 0.2596 0.0067 -0.0433 -0.0205 738 THR A O 5738 C CB . THR A 697 ? 0.2244 0.2278 0.2437 -0.0020 -0.0291 -0.0095 738 THR A CB 5739 O OG1 . THR A 697 ? 0.2310 0.2337 0.2435 -0.0035 -0.0251 -0.0051 738 THR A OG1 5740 C CG2 . THR A 697 ? 0.2403 0.2464 0.2526 0.0021 -0.0298 -0.0124 738 THR A CG2 5741 N N . VAL A 698 ? 0.2144 0.2132 0.2547 -0.0013 -0.0408 -0.0176 739 VAL A N 5742 C CA . VAL A 698 ? 0.2208 0.2193 0.2685 0.0008 -0.0474 -0.0234 739 VAL A CA 5743 C C . VAL A 698 ? 0.2361 0.2281 0.2812 0.0044 -0.0542 -0.0272 739 VAL A C 5744 O O . VAL A 698 ? 0.2459 0.2365 0.2860 0.0096 -0.0594 -0.0321 739 VAL A O 5745 C CB . VAL A 698 ? 0.2208 0.2220 0.2857 -0.0039 -0.0471 -0.0232 739 VAL A CB 5746 C CG1 . VAL A 698 ? 0.2504 0.2505 0.3246 -0.0016 -0.0556 -0.0298 739 VAL A CG1 5747 C CG2 . VAL A 698 ? 0.2252 0.2334 0.2917 -0.0061 -0.0406 -0.0206 739 VAL A CG2 5748 N N . GLN A 699 ? 0.2404 0.2277 0.2875 0.0024 -0.0541 -0.0249 740 GLN A N 5749 C CA . GLN A 699 ? 0.2580 0.2383 0.3024 0.0062 -0.0606 -0.0288 740 GLN A CA 5750 C C . GLN A 699 ? 0.2505 0.2297 0.2788 0.0121 -0.0604 -0.0299 740 GLN A C 5751 O O . GLN A 699 ? 0.2641 0.2397 0.2873 0.0175 -0.0659 -0.0351 740 GLN A O 5752 C CB . GLN A 699 ? 0.2652 0.2406 0.3147 0.0030 -0.0600 -0.0256 740 GLN A CB 5753 C CG . GLN A 699 ? 0.2751 0.2429 0.3218 0.0071 -0.0666 -0.0299 740 GLN A CG 5754 C CD . GLN A 699 ? 0.2977 0.2625 0.3549 0.0078 -0.0744 -0.0361 740 GLN A CD 5755 O OE1 . GLN A 699 ? 0.2947 0.2625 0.3658 0.0035 -0.0747 -0.0361 740 GLN A OE1 5756 N NE2 . GLN A 699 ? 0.3246 0.2835 0.3758 0.0134 -0.0810 -0.0418 740 GLN A NE2 5757 N N . ALA A 700 ? 0.2411 0.2235 0.2617 0.0115 -0.0542 -0.0254 741 ALA A N 5758 C CA . ALA A 700 ? 0.2568 0.2387 0.2646 0.0166 -0.0532 -0.0259 741 ALA A CA 5759 C C . ALA A 700 ? 0.2500 0.2340 0.2523 0.0208 -0.0545 -0.0294 741 ALA A C 5760 O O . ALA A 700 ? 0.2711 0.2518 0.2645 0.0267 -0.0569 -0.0325 741 ALA A O 5761 C CB . ALA A 700 ? 0.2579 0.2433 0.2609 0.0144 -0.0466 -0.0204 741 ALA A CB 5762 N N . ALA A 701 ? 0.2354 0.2241 0.2426 0.0184 -0.0532 -0.0291 742 ALA A N 5763 C CA . ALA A 701 ? 0.2359 0.2261 0.2383 0.0227 -0.0550 -0.0324 742 ALA A CA 5764 C C . ALA A 701 ? 0.2557 0.2408 0.2590 0.0267 -0.0632 -0.0384 742 ALA A C 5765 O O . ALA A 701 ? 0.2634 0.2458 0.2562 0.0329 -0.0655 -0.0413 742 ALA A O 5766 C CB . ALA A 701 ? 0.2270 0.2231 0.2364 0.0192 -0.0525 -0.0312 742 ALA A CB 5767 N N . ALA A 702 ? 0.2582 0.2419 0.2742 0.0233 -0.0674 -0.0402 743 ALA A N 5768 C CA . ALA A 702 ? 0.2788 0.2570 0.2970 0.0270 -0.0764 -0.0467 743 ALA A CA 5769 C C . ALA A 702 ? 0.2882 0.2598 0.2932 0.0332 -0.0786 -0.0490 743 ALA A C 5770 O O . ALA A 702 ? 0.3066 0.2740 0.3031 0.0398 -0.0841 -0.0543 743 ALA A O 5771 C CB . ALA A 702 ? 0.2783 0.2553 0.3132 0.0218 -0.0795 -0.0473 743 ALA A CB 5772 N N . GLU A 703 ? 0.2741 0.2444 0.2767 0.0317 -0.0743 -0.0453 744 GLU A N 5773 C CA . GLU A 703 ? 0.2921 0.2563 0.2844 0.0372 -0.0760 -0.0475 744 GLU A CA 5774 C C . GLU A 703 ? 0.2875 0.2518 0.2641 0.0438 -0.0731 -0.0478 744 GLU A C 5775 O O . GLU A 703 ? 0.2981 0.2569 0.2653 0.0499 -0.0754 -0.0510 744 GLU A O 5776 C CB . GLU A 703 ? 0.3032 0.2661 0.2982 0.0340 -0.0725 -0.0433 744 GLU A CB 5777 C CG . GLU A 703 ? 0.3169 0.2766 0.3258 0.0294 -0.0768 -0.0442 744 GLU A CG 5778 C CD . GLU A 703 ? 0.3687 0.3260 0.3807 0.0263 -0.0741 -0.0399 744 GLU A CD 5779 O OE1 . GLU A 703 ? 0.3985 0.3574 0.4026 0.0275 -0.0691 -0.0362 744 GLU A OE1 5780 O OE2 . GLU A 703 ? 0.3953 0.3488 0.4184 0.0228 -0.0772 -0.0401 744 GLU A OE2 5781 N N . THR A 704 ? 0.2881 0.2583 0.2622 0.0426 -0.0678 -0.0443 745 THR A N 5782 C CA . THR A 704 ? 0.2821 0.2521 0.2424 0.0486 -0.0648 -0.0443 745 THR A CA 5783 C C . THR A 704 ? 0.3064 0.2719 0.2598 0.0549 -0.0713 -0.0500 745 THR A C 5784 O O . THR A 704 ? 0.3169 0.2797 0.2568 0.0613 -0.0697 -0.0506 745 THR A O 5785 C CB . THR A 704 ? 0.2741 0.2507 0.2337 0.0461 -0.0580 -0.0396 745 THR A CB 5786 O OG1 . THR A 704 ? 0.2726 0.2523 0.2381 0.0440 -0.0603 -0.0406 745 THR A OG1 5787 C CG2 . THR A 704 ? 0.2745 0.2554 0.2411 0.0397 -0.0525 -0.0343 745 THR A CG2 5788 N N . LEU A 705 ? 0.2918 0.2566 0.2549 0.0530 -0.0785 -0.0540 746 LEU A N 5789 C CA . LEU A 705 ? 0.3109 0.2709 0.2681 0.0593 -0.0866 -0.0603 746 LEU A CA 5790 C C . LEU A 705 ? 0.3322 0.2843 0.2873 0.0632 -0.0940 -0.0662 746 LEU A C 5791 O O . LEU A 705 ? 0.3594 0.3061 0.3073 0.0695 -0.1014 -0.0722 746 LEU A O 5792 C CB . LEU A 705 ? 0.2985 0.2625 0.2687 0.0555 -0.0911 -0.0620 746 LEU A CB 5793 C CG . LEU A 705 ? 0.3243 0.2960 0.2975 0.0517 -0.0844 -0.0569 746 LEU A CG 5794 C CD1 . LEU A 705 ? 0.3149 0.2906 0.3035 0.0480 -0.0893 -0.0592 746 LEU A CD1 5795 C CD2 . LEU A 705 ? 0.3436 0.3142 0.3002 0.0581 -0.0811 -0.0557 746 LEU A CD2 5796 N N . SER A 706 ? 0.3243 0.2748 0.2852 0.0600 -0.0928 -0.0650 747 SER A N 5797 C CA . SER A 706 ? 0.3353 0.2774 0.2929 0.0645 -0.0993 -0.0707 747 SER A CA 5798 C C . SER A 706 ? 0.3485 0.2852 0.2856 0.0740 -0.0979 -0.0727 747 SER A C 5799 O O . SER A 706 ? 0.3495 0.2893 0.2769 0.0759 -0.0900 -0.0681 747 SER A O 5800 C CB . SER A 706 ? 0.3642 0.3057 0.3308 0.0595 -0.0969 -0.0679 747 SER A CB 5801 O OG . SER A 706 ? 0.3942 0.3396 0.3786 0.0513 -0.0978 -0.0659 747 SER A OG 5802 N N . GLU A 707 ? 0.3624 0.2906 0.2929 0.0802 -0.1052 -0.0795 748 GLU A N 5803 C CA . GLU A 707 ? 0.4101 0.3325 0.3216 0.0891 -0.1025 -0.0809 748 GLU A CA 5804 C C . GLU A 707 ? 0.3918 0.3180 0.3027 0.0871 -0.0921 -0.0743 748 GLU A C 5805 O O . GLU A 707 ? 0.3843 0.3132 0.3080 0.0806 -0.0905 -0.0714 748 GLU A O 5806 C CB . GLU A 707 ? 0.4447 0.3570 0.3508 0.0955 -0.1117 -0.0893 748 GLU A CB 5807 C CG . GLU A 707 ? 0.4996 0.4085 0.4058 0.0981 -0.1225 -0.0961 748 GLU A CG 5808 C CD . GLU A 707 ? 0.6460 0.5438 0.5406 0.1070 -0.1319 -0.1051 748 GLU A CD 5809 O OE1 . GLU A 707 ? 0.6877 0.5812 0.5928 0.1050 -0.1386 -0.1097 748 GLU A OE1 5810 O OE2 . GLU A 707 ? 0.7001 0.5933 0.5751 0.1160 -0.1326 -0.1077 748 GLU A OE2 5811 N N . VAL A 708 ? 0.3920 0.3186 0.2887 0.0925 -0.0849 -0.0716 749 VAL A N 5812 C CA . VAL A 708 ? 0.3864 0.3187 0.2850 0.0897 -0.0745 -0.0646 749 VAL A CA 5813 C C . VAL A 708 ? 0.4176 0.3461 0.3160 0.0919 -0.0733 -0.0655 749 VAL A C 5814 O O . VAL A 708 ? 0.4115 0.3448 0.3164 0.0881 -0.0671 -0.0605 749 VAL A O 5815 C CB . VAL A 708 ? 0.3916 0.3265 0.2779 0.0939 -0.0662 -0.0605 749 VAL A CB 5816 C CG1 . VAL A 708 ? 0.3888 0.3274 0.2760 0.0914 -0.0671 -0.0591 749 VAL A CG1 5817 C CG2 . VAL A 708 ? 0.4206 0.3471 0.2875 0.1050 -0.0661 -0.0645 749 VAL A CG2 5818 N N . ALA A 709 ? 0.4232 0.3430 0.3144 0.0983 -0.0798 -0.0724 750 ALA A N 5819 C CA . ALA A 709 ? 0.4516 0.3666 0.3412 0.1019 -0.0793 -0.0743 750 ALA A CA 5820 C C . ALA A 709 ? 0.4966 0.4013 0.3802 0.1078 -0.0894 -0.0833 750 ALA A C 5821 O O . ALA A 709 ? 0.5343 0.4332 0.4173 0.1111 -0.0915 -0.0867 750 ALA A O 5822 C CB . ALA A 709 ? 0.4586 0.3742 0.3361 0.1083 -0.0700 -0.0715 750 ALA A CB 5823 O OXT . ALA A 709 ? 0.5071 0.4088 0.3853 0.1104 -0.0958 -0.0876 750 ALA A OXT # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ARG 1 42 ? ? ? A . n A 1 2 SER 2 43 ? ? ? A . n A 1 3 LYS 3 44 ? ? ? A . n A 1 4 SER 4 45 ? ? ? A . n A 1 5 SER 5 46 ? ? ? A . n A 1 6 ASN 6 47 ? ? ? A . n A 1 7 GLU 7 48 ? ? ? A . n A 1 8 ALA 8 49 ? ? ? A . n A 1 9 THR 9 50 ? ? ? A . n A 1 10 ASN 10 51 ? ? ? A . n A 1 11 ILE 11 52 ? ? ? A . n A 1 12 THR 12 53 ? ? ? A . n A 1 13 PRO 13 54 ? ? ? A . n A 1 14 LYS 14 55 55 LYS LYS A . n A 1 15 HIS 15 56 56 HIS HIS A . n A 1 16 ASN 16 57 57 ASN ASN A . n A 1 17 MET 17 58 58 MET MET A . n A 1 18 LYS 18 59 59 LYS LYS A . n A 1 19 ALA 19 60 60 ALA ALA A . n A 1 20 PHE 20 61 61 PHE PHE A . n A 1 21 LEU 21 62 62 LEU LEU A . n A 1 22 ASP 22 63 63 ASP ASP A . n A 1 23 GLU 23 64 64 GLU GLU A . n A 1 24 LEU 24 65 65 LEU LEU A . n A 1 25 LYS 25 66 66 LYS LYS A . n A 1 26 ALA 26 67 67 ALA ALA A . n A 1 27 GLU 27 68 68 GLU GLU A . n A 1 28 ASN 28 69 69 ASN ASN A . n A 1 29 ILE 29 70 70 ILE ILE A . n A 1 30 LYS 30 71 71 LYS LYS A . n A 1 31 LYS 31 72 72 LYS LYS A . n A 1 32 PHE 32 73 73 PHE PHE A . n A 1 33 LEU 33 74 74 LEU LEU A . n A 1 34 TYR 34 75 75 TYR TYR A . n A 1 35 ASN 35 76 76 ASN ASN A . n A 1 36 PHE 36 77 77 PHE PHE A . n A 1 37 THR 37 78 78 THR THR A . n A 1 38 GLN 38 79 79 GLN GLN A . n A 1 39 ILE 39 80 80 ILE ILE A . n A 1 40 PRO 40 81 81 PRO PRO A . n A 1 41 HIS 41 82 82 HIS HIS A . n A 1 42 LEU 42 83 83 LEU LEU A . n A 1 43 ALA 43 84 84 ALA ALA A . n A 1 44 GLY 44 85 85 GLY GLY A . n A 1 45 THR 45 86 86 THR THR A . n A 1 46 GLU 46 87 87 GLU GLU A . n A 1 47 GLN 47 88 88 GLN GLN A . n A 1 48 ASN 48 89 89 ASN ASN A . n A 1 49 PHE 49 90 90 PHE PHE A . n A 1 50 GLN 50 91 91 GLN GLN A . n A 1 51 LEU 51 92 92 LEU LEU A . n A 1 52 ALA 52 93 93 ALA ALA A . n A 1 53 LYS 53 94 94 LYS LYS A . n A 1 54 GLN 54 95 95 GLN GLN A . n A 1 55 ILE 55 96 96 ILE ILE A . n A 1 56 GLN 56 97 97 GLN GLN A . n A 1 57 SER 57 98 98 SER SER A . n A 1 58 GLN 58 99 99 GLN GLN A . n A 1 59 TRP 59 100 100 TRP TRP A . n A 1 60 LYS 60 101 101 LYS LYS A . n A 1 61 GLU 61 102 102 GLU GLU A . n A 1 62 PHE 62 103 103 PHE PHE A . n A 1 63 GLY 63 104 104 GLY GLY A . n A 1 64 LEU 64 105 105 LEU LEU A . n A 1 65 ASP 65 106 106 ASP ASP A . n A 1 66 SER 66 107 107 SER SER A . n A 1 67 VAL 67 108 108 VAL VAL A . n A 1 68 GLU 68 109 109 GLU GLU A . n A 1 69 LEU 69 110 110 LEU LEU A . n A 1 70 ALA 70 111 111 ALA ALA A . n A 1 71 HIS 71 112 112 HIS HIS A . n A 1 72 TYR 72 113 113 TYR TYR A . n A 1 73 ASP 73 114 114 ASP ASP A . n A 1 74 VAL 74 115 115 VAL VAL A . n A 1 75 LEU 75 116 116 LEU LEU A . n A 1 76 LEU 76 117 117 LEU LEU A . n A 1 77 SER 77 118 118 SER SER A . n A 1 78 TYR 78 119 119 TYR TYR A . n A 1 79 PRO 79 120 120 PRO PRO A . n A 1 80 ASN 80 121 121 ASN ASN A . n A 1 81 LYS 81 122 122 LYS LYS A . n A 1 82 THR 82 123 123 THR THR A . n A 1 83 HIS 83 124 124 HIS HIS A . n A 1 84 PRO 84 125 125 PRO PRO A . n A 1 85 ASN 85 126 126 ASN ASN A . n A 1 86 TYR 86 127 127 TYR TYR A . n A 1 87 ILE 87 128 128 ILE ILE A . n A 1 88 SER 88 129 129 SER SER A . n A 1 89 ILE 89 130 130 ILE ILE A . n A 1 90 ILE 90 131 131 ILE ILE A . n A 1 91 ASN 91 132 132 ASN ASN A . n A 1 92 GLU 92 133 133 GLU GLU A . n A 1 93 ASP 93 134 134 ASP ASP A . n A 1 94 GLY 94 135 135 GLY GLY A . n A 1 95 ASN 95 136 136 ASN ASN A . n A 1 96 GLU 96 137 137 GLU GLU A . n A 1 97 ILE 97 138 138 ILE ILE A . n A 1 98 PHE 98 139 139 PHE PHE A . n A 1 99 ASN 99 140 140 ASN ASN A . n A 1 100 THR 100 141 141 THR THR A . n A 1 101 SER 101 142 142 SER SER A . n A 1 102 LEU 102 143 143 LEU LEU A . n A 1 103 PHE 103 144 144 PHE PHE A . n A 1 104 GLU 104 145 145 GLU GLU A . n A 1 105 PRO 105 146 146 PRO PRO A . n A 1 106 PRO 106 147 147 PRO PRO A . n A 1 107 PRO 107 148 148 PRO PRO A . n A 1 108 PRO 108 149 149 PRO PRO A . n A 1 109 GLY 109 150 150 GLY GLY A . n A 1 110 TYR 110 151 151 TYR TYR A . n A 1 111 GLU 111 152 152 GLU GLU A . n A 1 112 ASN 112 153 153 ASN ASN A . n A 1 113 VAL 113 154 154 VAL VAL A . n A 1 114 SER 114 155 155 SER SER A . n A 1 115 ASP 115 156 156 ASP ASP A . n A 1 116 ILE 116 157 157 ILE ILE A . n A 1 117 VAL 117 158 158 VAL VAL A . n A 1 118 PRO 118 159 159 PRO PRO A . n A 1 119 PRO 119 160 160 PRO PRO A . n A 1 120 PHE 120 161 161 PHE PHE A . n A 1 121 SER 121 162 162 SER SER A . n A 1 122 ALA 122 163 163 ALA ALA A . n A 1 123 PHE 123 164 164 PHE PHE A . n A 1 124 SER 124 165 165 SER SER A . n A 1 125 PRO 125 166 166 PRO PRO A . n A 1 126 GLN 126 167 167 GLN GLN A . n A 1 127 GLY 127 168 168 GLY GLY A . n A 1 128 MET 128 169 169 MET MET A . n A 1 129 PRO 129 170 170 PRO PRO A . n A 1 130 GLU 130 171 171 GLU GLU A . n A 1 131 GLY 131 172 172 GLY GLY A . n A 1 132 ASP 132 173 173 ASP ASP A . n A 1 133 LEU 133 174 174 LEU LEU A . n A 1 134 VAL 134 175 175 VAL VAL A . n A 1 135 TYR 135 176 176 TYR TYR A . n A 1 136 VAL 136 177 177 VAL VAL A . n A 1 137 ASN 137 178 178 ASN ASN A . n A 1 138 TYR 138 179 179 TYR TYR A . n A 1 139 ALA 139 180 180 ALA ALA A . n A 1 140 ARG 140 181 181 ARG ARG A . n A 1 141 THR 141 182 182 THR THR A . n A 1 142 GLU 142 183 183 GLU GLU A . n A 1 143 ASP 143 184 184 ASP ASP A . n A 1 144 PHE 144 185 185 PHE PHE A . n A 1 145 PHE 145 186 186 PHE PHE A . n A 1 146 LYS 146 187 187 LYS LYS A . n A 1 147 LEU 147 188 188 LEU LEU A . n A 1 148 GLU 148 189 189 GLU GLU A . n A 1 149 ARG 149 190 190 ARG ARG A . n A 1 150 ASP 150 191 191 ASP ASP A . n A 1 151 MET 151 192 192 MET MET A . n A 1 152 LYS 152 193 193 LYS LYS A . n A 1 153 ILE 153 194 194 ILE ILE A . n A 1 154 ASN 154 195 195 ASN ASN A . n A 1 155 CYS 155 196 196 CYS CYS A . n A 1 156 SER 156 197 197 SER SER A . n A 1 157 GLY 157 198 198 GLY GLY A . n A 1 158 LYS 158 199 199 LYS LYS A . n A 1 159 ILE 159 200 200 ILE ILE A . n A 1 160 VAL 160 201 201 VAL VAL A . n A 1 161 ILE 161 202 202 ILE ILE A . n A 1 162 ALA 162 203 203 ALA ALA A . n A 1 163 ARG 163 204 204 ARG ARG A . n A 1 164 TYR 164 205 205 TYR TYR A . n A 1 165 GLY 165 206 206 GLY GLY A . n A 1 166 LYS 166 207 207 LYS LYS A . n A 1 167 VAL 167 208 208 VAL VAL A . n A 1 168 PHE 168 209 209 PHE PHE A . n A 1 169 ARG 169 210 210 ARG ARG A . n A 1 170 GLY 170 211 211 GLY GLY A . n A 1 171 ASN 171 212 212 ASN ASN A . n A 1 172 LYS 172 213 213 LYS LYS A . n A 1 173 VAL 173 214 214 VAL VAL A . n A 1 174 LYS 174 215 215 LYS LYS A . n A 1 175 ASN 175 216 216 ASN ASN A . n A 1 176 ALA 176 217 217 ALA ALA A . n A 1 177 GLN 177 218 218 GLN GLN A . n A 1 178 LEU 178 219 219 LEU LEU A . n A 1 179 ALA 179 220 220 ALA ALA A . n A 1 180 GLY 180 221 221 GLY GLY A . n A 1 181 ALA 181 222 222 ALA ALA A . n A 1 182 LYS 182 223 223 LYS LYS A . n A 1 183 GLY 183 224 224 GLY GLY A . n A 1 184 VAL 184 225 225 VAL VAL A . n A 1 185 ILE 185 226 226 ILE ILE A . n A 1 186 LEU 186 227 227 LEU LEU A . n A 1 187 TYR 187 228 228 TYR TYR A . n A 1 188 SER 188 229 229 SER SER A . n A 1 189 ASP 189 230 230 ASP ASP A . n A 1 190 PRO 190 231 231 PRO PRO A . n A 1 191 ALA 191 232 232 ALA ALA A . n A 1 192 ASP 192 233 233 ASP ASP A . n A 1 193 TYR 193 234 234 TYR TYR A . n A 1 194 PHE 194 235 235 PHE PHE A . n A 1 195 ALA 195 236 236 ALA ALA A . n A 1 196 PRO 196 237 237 PRO PRO A . n A 1 197 GLY 197 238 238 GLY GLY A . n A 1 198 VAL 198 239 239 VAL VAL A . n A 1 199 LYS 199 240 240 LYS LYS A . n A 1 200 SER 200 241 241 SER SER A . n A 1 201 TYR 201 242 242 TYR TYR A . n A 1 202 PRO 202 243 243 PRO PRO A . n A 1 203 ASP 203 244 244 ASP ASP A . n A 1 204 GLY 204 245 245 GLY GLY A . n A 1 205 TRP 205 246 246 TRP TRP A . n A 1 206 ASN 206 247 247 ASN ASN A . n A 1 207 LEU 207 248 248 LEU LEU A . n A 1 208 PRO 208 249 249 PRO PRO A . n A 1 209 GLY 209 250 250 GLY GLY A . n A 1 210 GLY 210 251 251 GLY GLY A . n A 1 211 GLY 211 252 252 GLY GLY A . n A 1 212 VAL 212 253 253 VAL VAL A . n A 1 213 GLN 213 254 254 GLN GLN A . n A 1 214 ARG 214 255 255 ARG ARG A . n A 1 215 GLY 215 256 256 GLY GLY A . n A 1 216 ASN 216 257 257 ASN ASN A . n A 1 217 ILE 217 258 258 ILE ILE A . n A 1 218 LEU 218 259 259 LEU LEU A . n A 1 219 ASN 219 260 260 ASN ASN A . n A 1 220 LEU 220 261 261 LEU LEU A . n A 1 221 ASN 221 262 262 ASN ASN A . n A 1 222 GLY 222 263 263 GLY GLY A . n A 1 223 ALA 223 264 264 ALA ALA A . n A 1 224 GLY 224 265 265 GLY GLY A . n A 1 225 ASP 225 266 266 ASP ASP A . n A 1 226 PRO 226 267 267 PRO PRO A . n A 1 227 LEU 227 268 268 LEU LEU A . n A 1 228 THR 228 269 269 THR THR A . n A 1 229 PRO 229 270 270 PRO PRO A . n A 1 230 GLY 230 271 271 GLY GLY A . n A 1 231 TYR 231 272 272 TYR TYR A . n A 1 232 PRO 232 273 273 PRO PRO A . n A 1 233 ALA 233 274 274 ALA ALA A . n A 1 234 ASN 234 275 275 ASN ASN A . n A 1 235 GLU 235 276 276 GLU GLU A . n A 1 236 TYR 236 277 277 TYR TYR A . n A 1 237 ALA 237 278 278 ALA ALA A . n A 1 238 TYR 238 279 279 TYR TYR A . n A 1 239 ARG 239 280 280 ARG ARG A . n A 1 240 ARG 240 281 281 ARG ARG A . n A 1 241 GLY 241 282 282 GLY GLY A . n A 1 242 ILE 242 283 283 ILE ILE A . n A 1 243 ALA 243 284 284 ALA ALA A . n A 1 244 GLU 244 285 285 GLU GLU A . n A 1 245 ALA 245 286 286 ALA ALA A . n A 1 246 VAL 246 287 287 VAL VAL A . n A 1 247 GLY 247 288 288 GLY GLY A . n A 1 248 LEU 248 289 289 LEU LEU A . n A 1 249 PRO 249 290 290 PRO PRO A . n A 1 250 SER 250 291 291 SER SER A . n A 1 251 ILE 251 292 292 ILE ILE A . n A 1 252 PRO 252 293 293 PRO PRO A . n A 1 253 VAL 253 294 294 VAL VAL A . n A 1 254 HIS 254 295 295 HIS HIS A . n A 1 255 PRO 255 296 296 PRO PRO A . n A 1 256 ILE 256 297 297 ILE ILE A . n A 1 257 GLY 257 298 298 GLY GLY A . n A 1 258 TYR 258 299 299 TYR TYR A . n A 1 259 TYR 259 300 300 TYR TYR A . n A 1 260 ASP 260 301 301 ASP ASP A . n A 1 261 ALA 261 302 302 ALA ALA A . n A 1 262 GLN 262 303 303 GLN GLN A . n A 1 263 LYS 263 304 304 LYS LYS A . n A 1 264 LEU 264 305 305 LEU LEU A . n A 1 265 LEU 265 306 306 LEU LEU A . n A 1 266 GLU 266 307 307 GLU GLU A . n A 1 267 LYS 267 308 308 LYS LYS A . n A 1 268 MET 268 309 309 MET MET A . n A 1 269 GLY 269 310 310 GLY GLY A . n A 1 270 GLY 270 311 311 GLY GLY A . n A 1 271 SER 271 312 312 SER SER A . n A 1 272 ALA 272 313 313 ALA ALA A . n A 1 273 PRO 273 314 314 PRO PRO A . n A 1 274 PRO 274 315 315 PRO PRO A . n A 1 275 ASP 275 316 316 ASP ASP A . n A 1 276 SER 276 317 317 SER SER A . n A 1 277 SER 277 318 318 SER SER A . n A 1 278 TRP 278 319 319 TRP TRP A . n A 1 279 ARG 279 320 320 ARG ARG A . n A 1 280 GLY 280 321 321 GLY GLY A . n A 1 281 SER 281 322 322 SER SER A . n A 1 282 LEU 282 323 323 LEU LEU A . n A 1 283 LYS 283 324 324 LYS LYS A . n A 1 284 VAL 284 325 325 VAL VAL A . n A 1 285 PRO 285 326 326 PRO PRO A . n A 1 286 TYR 286 327 327 TYR TYR A . n A 1 287 ASN 287 328 328 ASN ASN A . n A 1 288 VAL 288 329 329 VAL VAL A . n A 1 289 GLY 289 330 330 GLY GLY A . n A 1 290 PRO 290 331 331 PRO PRO A . n A 1 291 GLY 291 332 332 GLY GLY A . n A 1 292 PHE 292 333 333 PHE PHE A . n A 1 293 THR 293 334 334 THR THR A . n A 1 294 GLY 294 335 335 GLY GLY A . n A 1 295 ASN 295 336 336 ASN ASN A . n A 1 296 PHE 296 337 337 PHE PHE A . n A 1 297 SER 297 338 338 SER SER A . n A 1 298 THR 298 339 339 THR THR A . n A 1 299 GLN 299 340 340 GLN GLN A . n A 1 300 LYS 300 341 341 LYS LYS A . n A 1 301 VAL 301 342 342 VAL VAL A . n A 1 302 LYS 302 343 343 LYS LYS A . n A 1 303 MET 303 344 344 MET MET A . n A 1 304 HIS 304 345 345 HIS HIS A . n A 1 305 ILE 305 346 346 ILE ILE A . n A 1 306 HIS 306 347 347 HIS HIS A . n A 1 307 SER 307 348 348 SER SER A . n A 1 308 THR 308 349 349 THR THR A . n A 1 309 ASN 309 350 350 ASN ASN A . n A 1 310 GLU 310 351 351 GLU GLU A . n A 1 311 VAL 311 352 352 VAL VAL A . n A 1 312 THR 312 353 353 THR THR A . n A 1 313 ARG 313 354 354 ARG ARG A . n A 1 314 ILE 314 355 355 ILE ILE A . n A 1 315 TYR 315 356 356 TYR TYR A . n A 1 316 ASN 316 357 357 ASN ASN A . n A 1 317 VAL 317 358 358 VAL VAL A . n A 1 318 ILE 318 359 359 ILE ILE A . n A 1 319 GLY 319 360 360 GLY GLY A . n A 1 320 THR 320 361 361 THR THR A . n A 1 321 LEU 321 362 362 LEU LEU A . n A 1 322 ARG 322 363 363 ARG ARG A . n A 1 323 GLY 323 364 364 GLY GLY A . n A 1 324 ALA 324 365 365 ALA ALA A . n A 1 325 VAL 325 366 366 VAL VAL A . n A 1 326 GLU 326 367 367 GLU GLU A . n A 1 327 PRO 327 368 368 PRO PRO A . n A 1 328 ASP 328 369 369 ASP ASP A . n A 1 329 ARG 329 370 370 ARG ARG A . n A 1 330 TYR 330 371 371 TYR TYR A . n A 1 331 VAL 331 372 372 VAL VAL A . n A 1 332 ILE 332 373 373 ILE ILE A . n A 1 333 LEU 333 374 374 LEU LEU A . n A 1 334 GLY 334 375 375 GLY GLY A . n A 1 335 GLY 335 376 376 GLY GLY A . n A 1 336 HIS 336 377 377 HIS HIS A . n A 1 337 ARG 337 378 378 ARG ARG A . n A 1 338 ASP 338 379 379 ASP ASP A . n A 1 339 SER 339 380 380 SER SER A . n A 1 340 TRP 340 381 381 TRP TRP A . n A 1 341 VAL 341 382 382 VAL VAL A . n A 1 342 PHE 342 383 383 PHE PHE A . n A 1 343 GLY 343 384 384 GLY GLY A . n A 1 344 GLY 344 385 385 GLY GLY A . n A 1 345 ILE 345 386 386 ILE ILE A . n A 1 346 ASP 346 387 387 ASP ASP A . n A 1 347 PRO 347 388 388 PRO PRO A . n A 1 348 GLN 348 389 389 GLN GLN A . n A 1 349 SER 349 390 390 SER SER A . n A 1 350 GLY 350 391 391 GLY GLY A . n A 1 351 ALA 351 392 392 ALA ALA A . n A 1 352 ALA 352 393 393 ALA ALA A . n A 1 353 VAL 353 394 394 VAL VAL A . n A 1 354 VAL 354 395 395 VAL VAL A . n A 1 355 HIS 355 396 396 HIS HIS A . n A 1 356 GLU 356 397 397 GLU GLU A . n A 1 357 ILE 357 398 398 ILE ILE A . n A 1 358 VAL 358 399 399 VAL VAL A . n A 1 359 ARG 359 400 400 ARG ARG A . n A 1 360 SER 360 401 401 SER SER A . n A 1 361 PHE 361 402 402 PHE PHE A . n A 1 362 GLY 362 403 403 GLY GLY A . n A 1 363 THR 363 404 404 THR THR A . n A 1 364 LEU 364 405 405 LEU LEU A . n A 1 365 LYS 365 406 406 LYS LYS A . n A 1 366 LYS 366 407 407 LYS LYS A . n A 1 367 GLU 367 408 408 GLU GLU A . n A 1 368 GLY 368 409 409 GLY GLY A . n A 1 369 TRP 369 410 410 TRP TRP A . n A 1 370 ARG 370 411 411 ARG ARG A . n A 1 371 PRO 371 412 412 PRO PRO A . n A 1 372 ARG 372 413 413 ARG ARG A . n A 1 373 ARG 373 414 414 ARG ARG A . n A 1 374 THR 374 415 415 THR THR A . n A 1 375 ILE 375 416 416 ILE ILE A . n A 1 376 LEU 376 417 417 LEU LEU A . n A 1 377 PHE 377 418 418 PHE PHE A . n A 1 378 ALA 378 419 419 ALA ALA A . n A 1 379 SER 379 420 420 SER SER A . n A 1 380 TRP 380 421 421 TRP TRP A . n A 1 381 ASP 381 422 422 ASP ASP A . n A 1 382 ALA 382 423 423 ALA ALA A . n A 1 383 ALA 383 424 424 ALA ALA 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 613 654 654 ASP ASP A . n A 1 614 LYS 614 655 655 LYS LYS 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 # _pdbx_molecule_features.prd_id PRD_000797 _pdbx_molecule_features.name '(2S)-2-[(N-ACETYL-L-ALPHA-ASPARTYL)AMINO]NONANOIC ACID' _pdbx_molecule_features.type Polypeptide _pdbx_molecule_features.class 'Enzyme inhibitor' _pdbx_molecule_features.details ? # _pdbx_molecule.instance_id 1 _pdbx_molecule.prd_id PRD_000797 _pdbx_molecule.asym_id S # 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 435 A ASN 476 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 597 A ASN 638 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 35 A ASN 76 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 99 A ASN 140 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 418 A ASN 459 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 80 A ASN 121 ? 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)' 12370 ? 1 MORE -97 ? 1 'SSA (A^2)' 49560 ? # 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 129.9930000000 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 2271 ? 1_555 ZN ? C ZN . ? A ZN 1752 ? 1_555 OD2 ? A ASP 412 ? A ASP 453 ? 1_555 114.3 ? 2 O ? T HOH . ? A HOH 2271 ? 1_555 ZN ? C ZN . ? A ZN 1752 ? 1_555 OD1 ? A ASP 346 ? A ASP 387 ? 1_555 103.6 ? 3 OD2 ? A ASP 412 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 1752 ? 1_555 OD1 ? A ASP 346 ? A ASP 387 ? 1_555 120.3 ? 4 O ? T HOH . ? A HOH 2271 ? 1_555 ZN ? C ZN . ? A ZN 1752 ? 1_555 NE2 ? A HIS 336 ? A HIS 377 ? 1_555 109.5 ? 5 OD2 ? A ASP 412 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 1752 ? 1_555 NE2 ? A HIS 336 ? A HIS 377 ? 1_555 101.0 ? 6 OD1 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? C ZN . ? A ZN 1752 ? 1_555 NE2 ? A HIS 336 ? A HIS 377 ? 1_555 108.0 ? 7 O ? T HOH . ? A HOH 2271 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 157.3 ? 8 O ? T HOH . ? A HOH 2271 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 96.9 ? 9 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 91.1 ? 10 O ? T HOH . ? A HOH 2271 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 97.8 ? 11 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 102.0 ? 12 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 98.5 ? 13 O ? T HOH . ? A HOH 2271 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 92.3 ? 14 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 89.3 ? 15 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 154.6 ? 16 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 56.8 ? 17 O ? T HOH . ? A HOH 2271 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OAF ? S SDR . ? A SDR 1 ? 1_555 74.4 ? 18 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OAF ? S SDR . ? A SDR 1 ? 1_555 83.2 ? 19 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OAF ? S SDR . ? A SDR 1 ? 1_555 102.3 ? 20 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OAF ? S SDR . ? A SDR 1 ? 1_555 158.5 ? 21 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OAF ? S SDR . ? A SDR 1 ? 1_555 103.0 ? 22 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? A TYR 231 ? A TYR 272 ? 1_555 80.7 ? 23 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? T HOH . ? A HOH 1805 ? 1_555 95.9 ? 24 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? T HOH . ? A HOH 1805 ? 1_555 145.9 ? 25 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 104.2 ? 26 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 73.8 ? 27 O ? T HOH . ? A HOH 1805 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 74.3 ? 28 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 172.7 ? 29 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 92.0 ? 30 O ? T HOH . ? A HOH 1805 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 89.7 ? 31 O ? A THR 228 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 72.7 ? 32 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 91.7 ? 33 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 85.6 ? 34 O ? T HOH . ? A HOH 1805 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 128.5 ? 35 O ? A THR 228 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 151.2 ? 36 OG1 ? A THR 228 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 88.5 ? 37 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 87.8 ? 38 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 135.8 ? 39 O ? T HOH . ? A HOH 1805 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 77.4 ? 40 O ? A THR 228 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 150.2 ? 41 OG1 ? A THR 228 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 98.0 ? 42 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 52.0 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2011-10-05 2 'Structure model' 1 1 2011-11-16 3 'Structure model' 1 2 2012-12-12 # _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 ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Database references' 2 3 'Structure model' Other # _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 17.6046 _pdbx_refine_tls.origin_y 49.6948 _pdbx_refine_tls.origin_z 44.9835 _pdbx_refine_tls.T[1][1] 0.0294 _pdbx_refine_tls.T[2][2] 0.0741 _pdbx_refine_tls.T[3][3] 0.0500 _pdbx_refine_tls.T[1][2] 0.0154 _pdbx_refine_tls.T[1][3] 0.0118 _pdbx_refine_tls.T[2][3] -0.0263 _pdbx_refine_tls.L[1][1] 0.6414 _pdbx_refine_tls.L[2][2] 1.0953 _pdbx_refine_tls.L[3][3] 0.3479 _pdbx_refine_tls.L[1][2] -0.3721 _pdbx_refine_tls.L[1][3] 0.0537 _pdbx_refine_tls.L[2][3] 0.0634 _pdbx_refine_tls.S[1][1] -0.0570 _pdbx_refine_tls.S[1][2] 0.0486 _pdbx_refine_tls.S[1][3] -0.0182 _pdbx_refine_tls.S[2][1] -0.0125 _pdbx_refine_tls.S[2][2] 0.0630 _pdbx_refine_tls.S[2][3] -0.1933 _pdbx_refine_tls.S[3][1] 0.0374 _pdbx_refine_tls.S[3][2] 0.0868 _pdbx_refine_tls.S[3][3] -0.0060 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id A _pdbx_refine_tls_group.beg_auth_seq_id 55 _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id A _pdbx_refine_tls_group.end_auth_seq_id 750 _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal SERGUI 'data collection' . ? 1 REFMAC refinement . ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 REFMAC phasing . ? 5 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 NH2 A ARG 684 ? ? O A PRO 694 ? B 1.96 2 1 ND2 A ASN 260 ? ? O A HOH 2185 ? ? 2.00 3 1 OE1 A GLU 152 ? ? O A HOH 2005 ? ? 2.13 4 1 O A HOH 1859 ? ? O A HOH 2074 ? ? 2.13 5 1 OG A SER 613 ? B O A HOH 2318 ? ? 2.16 # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 OE2 A GLU 276 ? B 1_555 O2 A BMA 1765 ? ? 2_565 1.73 2 1 O A HOH 2012 ? ? 1_555 O A HOH 2298 ? ? 2_565 1.77 3 1 O A HOH 1908 ? ? 1_555 O A HOH 2230 ? ? 2_565 2.13 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 N _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 SER _pdbx_validate_rmsd_bond.auth_seq_id_1 656 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 B _pdbx_validate_rmsd_bond.auth_atom_id_2 CA _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 SER _pdbx_validate_rmsd_bond.auth_seq_id_2 656 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 B _pdbx_validate_rmsd_bond.bond_value 1.598 _pdbx_validate_rmsd_bond.bond_target_value 1.459 _pdbx_validate_rmsd_bond.bond_deviation 0.139 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.020 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 NE A ARG 370 ? ? CZ A ARG 370 ? ? NH1 A ARG 370 ? ? 123.33 120.30 3.03 0.50 N 2 1 NE A ARG 440 ? ? CZ A ARG 440 ? ? NH2 A ARG 440 ? ? 116.68 120.30 -3.62 0.50 N 3 1 CA A LYS 655 ? ? C A LYS 655 ? ? N A SER 656 ? B 132.59 117.20 15.39 2.20 Y 4 1 O A LYS 655 ? ? C A LYS 655 ? ? N A SER 656 ? B 109.65 122.70 -13.05 1.60 Y 5 1 NE A ARG 662 ? A CZ A ARG 662 ? A NH2 A ARG 662 ? A 117.00 120.30 -3.30 0.50 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 ? ? -150.63 74.40 2 1 PHE A 164 ? ? 83.27 5.60 3 1 ASN A 178 ? ? 56.56 -125.11 4 1 LYS A 207 ? ? 76.02 -46.91 5 1 VAL A 382 ? ? -132.68 -108.16 6 1 ALA A 452 ? ? -154.00 57.19 7 1 ASP A 453 ? ? -78.45 -160.63 8 1 SER A 517 ? ? -133.66 -156.30 9 1 TRP A 541 ? ? -48.30 79.45 10 1 ASP A 567 ? ? -154.26 68.00 11 1 ASP A 683 ? ? 58.55 13.58 12 1 ASN A 698 ? A -166.41 98.90 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A GLU 542 ? CG ? A GLU 501 CG 2 1 Y 1 A GLU 542 ? CD ? A GLU 501 CD 3 1 Y 1 A GLU 542 ? OE1 ? A GLU 501 OE1 4 1 Y 1 A GLU 542 ? OE2 ? A GLU 501 OE2 5 1 N 1 A SDR 1 ? CAA ? S SDR 1 CAA # 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 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'ZINC ION' ZN 3 'CALCIUM ION' CA 4 'CHLORIDE ION' CL 5 N-ACETYL-D-GLUCOSAMINE NAG 6 BETA-D-MANNOSE BMA 7 ALPHA-D-MANNOSE MAN 8 '(2S)-2-[(N-acetyl-L-alpha-aspartyl)amino]nonanoic acid' SDR 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 ZN 1 1751 1751 ZN ZN A . C 2 ZN 1 1752 1752 ZN ZN A . D 3 CA 1 1753 1753 CA CA A . E 4 CL 1 1754 1754 CL CL A . F 5 NAG 1 1755 1755 NAG NAG A . G 5 NAG 2 1756 1756 NAG NAG A . H 5 NAG 1 1757 1757 NAG NAG A . I 5 NAG 1 1758 1758 NAG NAG A . J 5 NAG 2 1767 1767 NAG NAG A . K 5 NAG 1 1759 1759 NAG NAG A . L 5 NAG 1 1760 1760 NAG NAG A . M 5 NAG 1 1761 1761 NAG NAG A . N 5 NAG 2 1762 1762 NAG NAG A . O 5 NAG 1 1763 1763 NAG NAG A . P 5 NAG 2 1764 1764 NAG NAG A . Q 6 BMA 3 1765 1765 BMA BMA A . R 7 MAN 4 1766 1766 MAN MAN A . S 8 SDR 1 1 1 SDR SDR A . T 9 HOH 1 1800 1800 HOH HOH A . T 9 HOH 2 1801 1801 HOH HOH A . T 9 HOH 3 1802 1802 HOH HOH A . T 9 HOH 4 1803 1803 HOH HOH A . T 9 HOH 5 1804 1804 HOH HOH A . T 9 HOH 6 1805 1805 HOH HOH A . T 9 HOH 7 1806 1806 HOH HOH A . T 9 HOH 8 1807 1807 HOH HOH A . T 9 HOH 9 1808 1808 HOH HOH A . T 9 HOH 10 1809 1809 HOH HOH A . T 9 HOH 11 1810 1810 HOH HOH A . T 9 HOH 12 1811 1811 HOH HOH A . T 9 HOH 13 1812 1812 HOH HOH A . T 9 HOH 14 1813 1813 HOH HOH A . T 9 HOH 15 1814 1814 HOH HOH A . T 9 HOH 16 1815 1815 HOH HOH A . T 9 HOH 17 1816 1816 HOH HOH A . T 9 HOH 18 1817 1817 HOH HOH A . T 9 HOH 19 1818 1818 HOH HOH A . T 9 HOH 20 1819 1819 HOH HOH A . T 9 HOH 21 1820 1820 HOH HOH A . T 9 HOH 22 1821 1821 HOH HOH A . T 9 HOH 23 1822 1822 HOH HOH A . T 9 HOH 24 1823 1823 HOH HOH A . T 9 HOH 25 1824 1824 HOH HOH A . T 9 HOH 26 1825 1825 HOH HOH A . T 9 HOH 27 1826 1826 HOH HOH A . T 9 HOH 28 1827 1827 HOH HOH A . T 9 HOH 29 1828 1828 HOH HOH A . T 9 HOH 30 1829 1829 HOH HOH A . T 9 HOH 31 1830 1830 HOH HOH A . T 9 HOH 32 1831 1831 HOH HOH A . T 9 HOH 33 1832 1832 HOH HOH A . T 9 HOH 34 1833 1833 HOH HOH A . T 9 HOH 35 1834 1834 HOH HOH A . T 9 HOH 36 1835 1835 HOH HOH A . T 9 HOH 37 1836 1836 HOH HOH A . T 9 HOH 38 1837 1837 HOH HOH A . T 9 HOH 39 1838 1838 HOH HOH A . T 9 HOH 40 1839 1839 HOH HOH A . T 9 HOH 41 1840 1840 HOH HOH A . T 9 HOH 42 1841 1841 HOH HOH A . T 9 HOH 43 1842 1842 HOH HOH A . T 9 HOH 44 1843 1843 HOH HOH A . T 9 HOH 45 1844 1844 HOH HOH A . T 9 HOH 46 1845 1845 HOH HOH A . T 9 HOH 47 1846 1846 HOH HOH A . T 9 HOH 48 1847 1847 HOH HOH A . T 9 HOH 49 1848 1848 HOH HOH A . T 9 HOH 50 1849 1849 HOH HOH A . T 9 HOH 51 1850 1850 HOH HOH A . T 9 HOH 52 1851 1851 HOH HOH A . T 9 HOH 53 1852 1852 HOH HOH A . T 9 HOH 54 1853 1853 HOH HOH A . T 9 HOH 55 1854 1854 HOH HOH A . T 9 HOH 56 1855 1855 HOH HOH A . T 9 HOH 57 1856 1856 HOH HOH A . T 9 HOH 58 1857 1857 HOH HOH A . T 9 HOH 59 1858 1858 HOH HOH A . T 9 HOH 60 1859 1859 HOH HOH A . T 9 HOH 61 1860 1860 HOH HOH A . T 9 HOH 62 1861 1861 HOH HOH A . T 9 HOH 63 1862 1862 HOH HOH A . T 9 HOH 64 1863 1863 HOH HOH A . T 9 HOH 65 1864 1864 HOH HOH A . T 9 HOH 66 1865 1865 HOH HOH A . T 9 HOH 67 1866 1866 HOH HOH A . T 9 HOH 68 1867 1867 HOH HOH A . T 9 HOH 69 1868 1868 HOH HOH A . T 9 HOH 70 1869 1869 HOH HOH A . T 9 HOH 71 1870 1870 HOH HOH A . T 9 HOH 72 1871 1871 HOH HOH A . T 9 HOH 73 1872 1872 HOH HOH A . T 9 HOH 74 1873 1873 HOH HOH A . T 9 HOH 75 1874 1874 HOH HOH A . T 9 HOH 76 1875 1875 HOH HOH A . T 9 HOH 77 1876 1876 HOH HOH A . T 9 HOH 78 1877 1877 HOH HOH A . T 9 HOH 79 1878 1878 HOH HOH A . T 9 HOH 80 1879 1879 HOH HOH A . T 9 HOH 81 1880 1880 HOH HOH A . T 9 HOH 82 1881 1881 HOH HOH A . T 9 HOH 83 1882 1882 HOH HOH A . T 9 HOH 84 1883 1883 HOH HOH A . T 9 HOH 85 1884 1884 HOH HOH A . T 9 HOH 86 1885 1885 HOH HOH A . T 9 HOH 87 1886 1886 HOH HOH A . T 9 HOH 88 1887 1887 HOH HOH A . T 9 HOH 89 1888 1888 HOH HOH A . T 9 HOH 90 1889 1889 HOH HOH A . T 9 HOH 91 1890 1890 HOH HOH A . T 9 HOH 92 1891 1891 HOH HOH A . T 9 HOH 93 1892 1892 HOH HOH A . T 9 HOH 94 1893 1893 HOH HOH A . T 9 HOH 95 1894 1894 HOH HOH A . T 9 HOH 96 1895 1895 HOH HOH A . T 9 HOH 97 1896 1896 HOH HOH A . T 9 HOH 98 1897 1897 HOH HOH A . T 9 HOH 99 1898 1898 HOH HOH A . T 9 HOH 100 1899 1899 HOH HOH A . T 9 HOH 101 1900 1900 HOH HOH A . T 9 HOH 102 1901 1901 HOH HOH A . T 9 HOH 103 1902 1902 HOH HOH A . T 9 HOH 104 1903 1903 HOH HOH A . T 9 HOH 105 1904 1904 HOH HOH A . T 9 HOH 106 1905 1905 HOH HOH A . T 9 HOH 107 1906 1906 HOH HOH A . T 9 HOH 108 1907 1907 HOH HOH A . T 9 HOH 109 1908 1908 HOH HOH A . T 9 HOH 110 1909 1909 HOH HOH A . T 9 HOH 111 1910 1910 HOH HOH A . T 9 HOH 112 1911 1911 HOH HOH A . T 9 HOH 113 1912 1912 HOH HOH A . T 9 HOH 114 1913 1913 HOH HOH A . T 9 HOH 115 1914 1914 HOH HOH A . T 9 HOH 116 1915 1915 HOH HOH A . T 9 HOH 117 1916 1916 HOH HOH A . T 9 HOH 118 1917 1917 HOH HOH A . T 9 HOH 119 1918 1918 HOH HOH A . T 9 HOH 120 1919 1919 HOH HOH A . T 9 HOH 121 1920 1920 HOH HOH A . T 9 HOH 122 1921 1921 HOH HOH A . T 9 HOH 123 1922 1922 HOH HOH A . T 9 HOH 124 1923 1923 HOH HOH A . T 9 HOH 125 1924 1924 HOH HOH A . T 9 HOH 126 1925 1925 HOH HOH A . T 9 HOH 127 1926 1926 HOH HOH A . T 9 HOH 128 1927 1927 HOH HOH A . T 9 HOH 129 1928 1928 HOH HOH A . T 9 HOH 130 1929 1929 HOH HOH A . T 9 HOH 131 1930 1930 HOH HOH A . T 9 HOH 132 1931 1931 HOH HOH A . T 9 HOH 133 1932 1932 HOH HOH A . T 9 HOH 134 1933 1933 HOH HOH A . T 9 HOH 135 1934 1934 HOH HOH A . T 9 HOH 136 1935 1935 HOH HOH A . T 9 HOH 137 1936 1936 HOH HOH A . T 9 HOH 138 1937 1937 HOH HOH A . T 9 HOH 139 1938 1938 HOH HOH A . T 9 HOH 140 1939 1939 HOH HOH A . T 9 HOH 141 1940 1940 HOH HOH A . T 9 HOH 142 1941 1941 HOH HOH A . T 9 HOH 143 1942 1942 HOH HOH A . T 9 HOH 144 1943 1943 HOH HOH A . T 9 HOH 145 1944 1944 HOH HOH A . T 9 HOH 146 1945 1945 HOH HOH A . T 9 HOH 147 1946 1946 HOH HOH A . T 9 HOH 148 1947 1947 HOH HOH A . T 9 HOH 149 1948 1948 HOH HOH A . T 9 HOH 150 1949 1949 HOH HOH A . T 9 HOH 151 1950 1950 HOH HOH A . T 9 HOH 152 1951 1951 HOH HOH A . T 9 HOH 153 1952 1952 HOH HOH A . T 9 HOH 154 1953 1953 HOH HOH A . T 9 HOH 155 1954 1954 HOH HOH A . T 9 HOH 156 1955 1955 HOH HOH A . T 9 HOH 157 1956 1956 HOH HOH A . T 9 HOH 158 1957 1957 HOH HOH A . T 9 HOH 159 1958 1958 HOH HOH A . T 9 HOH 160 1959 1959 HOH HOH A . T 9 HOH 161 1960 1960 HOH HOH A . T 9 HOH 162 1961 1961 HOH HOH A . T 9 HOH 163 1962 1962 HOH HOH A . T 9 HOH 164 1963 1963 HOH HOH A . T 9 HOH 165 1964 1964 HOH HOH A . T 9 HOH 166 1965 1965 HOH HOH A . T 9 HOH 167 1966 1966 HOH HOH A . T 9 HOH 168 1967 1967 HOH HOH A . T 9 HOH 169 1968 1968 HOH HOH A . T 9 HOH 170 1969 1969 HOH HOH A . T 9 HOH 171 1970 1970 HOH HOH A . T 9 HOH 172 1971 1971 HOH HOH A . T 9 HOH 173 1972 1972 HOH HOH A . T 9 HOH 174 1973 1973 HOH HOH A . T 9 HOH 175 1974 1974 HOH HOH A . T 9 HOH 176 1975 1975 HOH HOH A . T 9 HOH 177 1976 1976 HOH HOH A . T 9 HOH 178 1977 1977 HOH HOH A . T 9 HOH 179 1978 1978 HOH HOH A . T 9 HOH 180 1979 1979 HOH HOH A . T 9 HOH 181 1980 1980 HOH HOH A . T 9 HOH 182 1981 1981 HOH HOH A . T 9 HOH 183 1982 1982 HOH HOH A . T 9 HOH 184 1983 1983 HOH HOH A . T 9 HOH 185 1984 1984 HOH HOH A . T 9 HOH 186 1985 1985 HOH HOH A . T 9 HOH 187 1986 1986 HOH HOH A . T 9 HOH 188 1987 1987 HOH HOH A . T 9 HOH 189 1988 1988 HOH HOH A . T 9 HOH 190 1989 1989 HOH HOH A . T 9 HOH 191 1990 1990 HOH HOH A . T 9 HOH 192 1991 1991 HOH HOH A . T 9 HOH 193 1992 1992 HOH HOH A . T 9 HOH 194 1993 1993 HOH HOH A . T 9 HOH 195 1994 1994 HOH HOH A . T 9 HOH 196 1995 1995 HOH HOH A . T 9 HOH 197 1996 1996 HOH HOH A . T 9 HOH 198 1997 1997 HOH HOH A . T 9 HOH 199 1998 1998 HOH HOH A . T 9 HOH 200 1999 1999 HOH HOH A . T 9 HOH 201 2000 2000 HOH HOH A . T 9 HOH 202 2001 2001 HOH HOH A . T 9 HOH 203 2002 2002 HOH HOH A . T 9 HOH 204 2003 2003 HOH HOH A . T 9 HOH 205 2004 2004 HOH HOH A . T 9 HOH 206 2005 2005 HOH HOH A . T 9 HOH 207 2006 2006 HOH HOH A . T 9 HOH 208 2007 2007 HOH HOH A . T 9 HOH 209 2008 2008 HOH HOH A . T 9 HOH 210 2009 2009 HOH HOH A . T 9 HOH 211 2010 2010 HOH HOH A . T 9 HOH 212 2011 2011 HOH HOH A . T 9 HOH 213 2012 2012 HOH HOH A . T 9 HOH 214 2013 2013 HOH HOH A . T 9 HOH 215 2014 2014 HOH HOH A . T 9 HOH 216 2015 2015 HOH HOH A . T 9 HOH 217 2016 2016 HOH HOH A . T 9 HOH 218 2017 2017 HOH HOH A . T 9 HOH 219 2018 2018 HOH HOH A . T 9 HOH 220 2019 2019 HOH HOH A . T 9 HOH 221 2020 2020 HOH HOH A . T 9 HOH 222 2021 2021 HOH HOH A . T 9 HOH 223 2022 2022 HOH HOH A . T 9 HOH 224 2023 2023 HOH HOH A . T 9 HOH 225 2024 2024 HOH HOH A . T 9 HOH 226 2025 2025 HOH HOH A . T 9 HOH 227 2026 2026 HOH HOH A . T 9 HOH 228 2027 2027 HOH HOH A . T 9 HOH 229 2028 2028 HOH HOH A . T 9 HOH 230 2029 2029 HOH HOH A . T 9 HOH 231 2030 2030 HOH HOH A . T 9 HOH 232 2031 2031 HOH HOH A . T 9 HOH 233 2032 2032 HOH HOH A . T 9 HOH 234 2033 2033 HOH HOH A . T 9 HOH 235 2034 2034 HOH HOH A . T 9 HOH 236 2035 2035 HOH HOH A . T 9 HOH 237 2036 2036 HOH HOH A . T 9 HOH 238 2037 2037 HOH HOH A . T 9 HOH 239 2038 2038 HOH HOH A . T 9 HOH 240 2039 2039 HOH HOH A . T 9 HOH 241 2040 2040 HOH HOH A . T 9 HOH 242 2041 2041 HOH HOH A . T 9 HOH 243 2042 2042 HOH HOH A . T 9 HOH 244 2043 2043 HOH HOH A . T 9 HOH 245 2044 2044 HOH HOH A . T 9 HOH 246 2045 2045 HOH HOH A . T 9 HOH 247 2046 2046 HOH HOH A . T 9 HOH 248 2047 2047 HOH HOH A . T 9 HOH 249 2048 2048 HOH HOH A . T 9 HOH 250 2049 2049 HOH HOH A . T 9 HOH 251 2050 2050 HOH HOH A . T 9 HOH 252 2051 2051 HOH HOH A . T 9 HOH 253 2052 2052 HOH HOH A . T 9 HOH 254 2053 2053 HOH HOH A . T 9 HOH 255 2054 2054 HOH HOH A . T 9 HOH 256 2055 2055 HOH HOH A . T 9 HOH 257 2056 2056 HOH HOH A . T 9 HOH 258 2057 2057 HOH HOH A . T 9 HOH 259 2058 2058 HOH HOH A . T 9 HOH 260 2059 2059 HOH HOH A . T 9 HOH 261 2060 2060 HOH HOH A . T 9 HOH 262 2061 2061 HOH HOH A . T 9 HOH 263 2062 2062 HOH HOH A . T 9 HOH 264 2063 2063 HOH HOH A . T 9 HOH 265 2064 2064 HOH HOH A . T 9 HOH 266 2065 2065 HOH HOH A . T 9 HOH 267 2066 2066 HOH HOH A . T 9 HOH 268 2067 2067 HOH HOH A . T 9 HOH 269 2068 2068 HOH HOH A . T 9 HOH 270 2069 2069 HOH HOH A . T 9 HOH 271 2070 2070 HOH HOH A . T 9 HOH 272 2071 2071 HOH HOH A . T 9 HOH 273 2072 2072 HOH HOH A . T 9 HOH 274 2073 2073 HOH HOH A . T 9 HOH 275 2074 2074 HOH HOH A . T 9 HOH 276 2075 2075 HOH HOH A . T 9 HOH 277 2076 2076 HOH HOH A . T 9 HOH 278 2077 2077 HOH HOH A . T 9 HOH 279 2078 2078 HOH HOH A . T 9 HOH 280 2079 2079 HOH HOH A . T 9 HOH 281 2080 2080 HOH HOH A . T 9 HOH 282 2081 2081 HOH HOH A . T 9 HOH 283 2082 2082 HOH HOH A . T 9 HOH 284 2083 2083 HOH HOH A . T 9 HOH 285 2084 2084 HOH HOH A . T 9 HOH 286 2085 2085 HOH HOH A . T 9 HOH 287 2086 2086 HOH HOH A . T 9 HOH 288 2087 2087 HOH HOH A . T 9 HOH 289 2088 2088 HOH HOH A . T 9 HOH 290 2089 2089 HOH HOH A . T 9 HOH 291 2090 2090 HOH HOH A . T 9 HOH 292 2091 2091 HOH HOH A . T 9 HOH 293 2092 2092 HOH HOH A . T 9 HOH 294 2093 2093 HOH HOH A . T 9 HOH 295 2094 2094 HOH HOH A . T 9 HOH 296 2095 2095 HOH HOH A . T 9 HOH 297 2096 2096 HOH HOH A . T 9 HOH 298 2097 2097 HOH HOH A . T 9 HOH 299 2098 2098 HOH HOH A . T 9 HOH 300 2099 2099 HOH HOH A . T 9 HOH 301 2100 2100 HOH HOH A . T 9 HOH 302 2101 2101 HOH HOH A . T 9 HOH 303 2102 2102 HOH HOH A . T 9 HOH 304 2103 2103 HOH HOH A . T 9 HOH 305 2104 2104 HOH HOH A . T 9 HOH 306 2105 2105 HOH HOH A . T 9 HOH 307 2106 2106 HOH HOH A . T 9 HOH 308 2107 2107 HOH HOH A . T 9 HOH 309 2108 2108 HOH HOH A . T 9 HOH 310 2109 2109 HOH HOH A . T 9 HOH 311 2110 2110 HOH HOH A . T 9 HOH 312 2111 2111 HOH HOH A . T 9 HOH 313 2112 2112 HOH HOH A . T 9 HOH 314 2113 2113 HOH HOH A . T 9 HOH 315 2114 2114 HOH HOH A . T 9 HOH 316 2115 2115 HOH HOH A . T 9 HOH 317 2116 2116 HOH HOH A . T 9 HOH 318 2117 2117 HOH HOH A . T 9 HOH 319 2118 2118 HOH HOH A . T 9 HOH 320 2119 2119 HOH HOH A . T 9 HOH 321 2120 2120 HOH HOH A . T 9 HOH 322 2121 2121 HOH HOH A . T 9 HOH 323 2122 2122 HOH HOH A . T 9 HOH 324 2123 2123 HOH HOH A . T 9 HOH 325 2124 2124 HOH HOH A . T 9 HOH 326 2125 2125 HOH HOH A . T 9 HOH 327 2126 2126 HOH HOH A . T 9 HOH 328 2127 2127 HOH HOH A . T 9 HOH 329 2128 2128 HOH HOH A . T 9 HOH 330 2129 2129 HOH HOH A . T 9 HOH 331 2130 2130 HOH HOH A . T 9 HOH 332 2131 2131 HOH HOH A . T 9 HOH 333 2132 2132 HOH HOH A . T 9 HOH 334 2133 2133 HOH HOH A . T 9 HOH 335 2134 2134 HOH HOH A . T 9 HOH 336 2135 2135 HOH HOH A . T 9 HOH 337 2136 2136 HOH HOH A . T 9 HOH 338 2137 2137 HOH HOH A . T 9 HOH 339 2138 2138 HOH HOH A . T 9 HOH 340 2139 2139 HOH HOH A . T 9 HOH 341 2140 2140 HOH HOH A . T 9 HOH 342 2141 2141 HOH HOH A . T 9 HOH 343 2142 2142 HOH HOH A . T 9 HOH 344 2143 2143 HOH HOH A . T 9 HOH 345 2144 2144 HOH HOH A . T 9 HOH 346 2145 2145 HOH HOH A . T 9 HOH 347 2146 2146 HOH HOH A . T 9 HOH 348 2147 2147 HOH HOH A . T 9 HOH 349 2148 2148 HOH HOH A . T 9 HOH 350 2149 2149 HOH HOH A . T 9 HOH 351 2150 2150 HOH HOH A . T 9 HOH 352 2151 2151 HOH HOH A . T 9 HOH 353 2152 2152 HOH HOH A . T 9 HOH 354 2153 2153 HOH HOH A . T 9 HOH 355 2154 2154 HOH HOH A . T 9 HOH 356 2155 2155 HOH HOH A . T 9 HOH 357 2156 2156 HOH HOH A . T 9 HOH 358 2157 2157 HOH HOH A . T 9 HOH 359 2158 2158 HOH HOH A . T 9 HOH 360 2159 2159 HOH HOH A . T 9 HOH 361 2160 2160 HOH HOH A . T 9 HOH 362 2161 2161 HOH HOH A . T 9 HOH 363 2162 2162 HOH HOH A . T 9 HOH 364 2163 2163 HOH HOH A . T 9 HOH 365 2164 2164 HOH HOH A . T 9 HOH 366 2165 2165 HOH HOH A . T 9 HOH 367 2166 2166 HOH HOH A . T 9 HOH 368 2167 2167 HOH HOH A . T 9 HOH 369 2168 2168 HOH HOH A . T 9 HOH 370 2169 2169 HOH HOH A . T 9 HOH 371 2170 2170 HOH HOH A . T 9 HOH 372 2171 2171 HOH HOH A . T 9 HOH 373 2172 2172 HOH HOH A . T 9 HOH 374 2173 2173 HOH HOH A . T 9 HOH 375 2174 2174 HOH HOH A . T 9 HOH 376 2175 2175 HOH HOH A . T 9 HOH 377 2176 2176 HOH HOH A . T 9 HOH 378 2177 2177 HOH HOH A . T 9 HOH 379 2178 2178 HOH HOH A . T 9 HOH 380 2179 2179 HOH HOH A . T 9 HOH 381 2180 2180 HOH HOH A . T 9 HOH 382 2181 2181 HOH HOH A . T 9 HOH 383 2182 2182 HOH HOH A . T 9 HOH 384 2183 2183 HOH HOH A . T 9 HOH 385 2184 2184 HOH HOH A . T 9 HOH 386 2185 2185 HOH HOH A . T 9 HOH 387 2186 2186 HOH HOH A . T 9 HOH 388 2187 2187 HOH HOH A . T 9 HOH 389 2188 2188 HOH HOH A . T 9 HOH 390 2189 2189 HOH HOH A . T 9 HOH 391 2190 2190 HOH HOH A . T 9 HOH 392 2191 2191 HOH HOH A . T 9 HOH 393 2192 2192 HOH HOH A . T 9 HOH 394 2193 2193 HOH HOH A . T 9 HOH 395 2194 2194 HOH HOH A . T 9 HOH 396 2195 2195 HOH HOH A . T 9 HOH 397 2196 2196 HOH HOH A . T 9 HOH 398 2197 2197 HOH HOH A . T 9 HOH 399 2198 2198 HOH HOH A . T 9 HOH 400 2199 2199 HOH HOH A . T 9 HOH 401 2200 2200 HOH HOH A . T 9 HOH 402 2201 2201 HOH HOH A . T 9 HOH 403 2202 2202 HOH HOH A . T 9 HOH 404 2203 2203 HOH HOH A . T 9 HOH 405 2204 2204 HOH HOH A . T 9 HOH 406 2205 2205 HOH HOH A . T 9 HOH 407 2206 2206 HOH HOH A . T 9 HOH 408 2207 2207 HOH HOH A . T 9 HOH 409 2208 2208 HOH HOH A . T 9 HOH 410 2209 2209 HOH HOH A . T 9 HOH 411 2210 2210 HOH HOH A . T 9 HOH 412 2211 2211 HOH HOH A . T 9 HOH 413 2212 2212 HOH HOH A . T 9 HOH 414 2213 2213 HOH HOH A . T 9 HOH 415 2214 2214 HOH HOH A . T 9 HOH 416 2215 2215 HOH HOH A . T 9 HOH 417 2216 2216 HOH HOH A . T 9 HOH 418 2217 2217 HOH HOH A . T 9 HOH 419 2218 2218 HOH HOH A . T 9 HOH 420 2219 2219 HOH HOH A . T 9 HOH 421 2220 2220 HOH HOH A . T 9 HOH 422 2221 2221 HOH HOH A . T 9 HOH 423 2222 2222 HOH HOH A . T 9 HOH 424 2223 2223 HOH HOH A . T 9 HOH 425 2224 2224 HOH HOH A . T 9 HOH 426 2225 2225 HOH HOH A . T 9 HOH 427 2226 2226 HOH HOH A . T 9 HOH 428 2227 2227 HOH HOH A . T 9 HOH 429 2228 2228 HOH HOH A . T 9 HOH 430 2229 2229 HOH HOH A . T 9 HOH 431 2230 2230 HOH HOH A . T 9 HOH 432 2231 2231 HOH HOH A . T 9 HOH 433 2232 2232 HOH HOH A . T 9 HOH 434 2233 2233 HOH HOH A . T 9 HOH 435 2234 2234 HOH HOH A . T 9 HOH 436 2235 2235 HOH HOH A . T 9 HOH 437 2236 2236 HOH HOH A . T 9 HOH 438 2237 2237 HOH HOH A . T 9 HOH 439 2238 2238 HOH HOH A . T 9 HOH 440 2239 2239 HOH HOH A . T 9 HOH 441 2240 2240 HOH HOH A . T 9 HOH 442 2241 2241 HOH HOH A . T 9 HOH 443 2242 2242 HOH HOH A . T 9 HOH 444 2243 2243 HOH HOH A . T 9 HOH 445 2244 2244 HOH HOH A . T 9 HOH 446 2245 2245 HOH HOH A . T 9 HOH 447 2246 2246 HOH HOH A . T 9 HOH 448 2247 2247 HOH HOH A . T 9 HOH 449 2248 2248 HOH HOH A . T 9 HOH 450 2249 2249 HOH HOH A . T 9 HOH 451 2250 2250 HOH HOH A . T 9 HOH 452 2251 2251 HOH HOH A . T 9 HOH 453 2252 2252 HOH HOH A . T 9 HOH 454 2253 2253 HOH HOH A . T 9 HOH 455 2254 2254 HOH HOH A . T 9 HOH 456 2255 2255 HOH HOH A . T 9 HOH 457 2256 2256 HOH HOH A . T 9 HOH 458 2257 2257 HOH HOH A . T 9 HOH 459 2258 2258 HOH HOH A . T 9 HOH 460 2259 2259 HOH HOH A . T 9 HOH 461 2260 2260 HOH HOH A . T 9 HOH 462 2261 2261 HOH HOH A . T 9 HOH 463 2262 2262 HOH HOH A . T 9 HOH 464 2263 2263 HOH HOH A . T 9 HOH 465 2264 2264 HOH HOH A . T 9 HOH 466 2265 2265 HOH HOH A . T 9 HOH 467 2266 2266 HOH HOH A . T 9 HOH 468 2267 2267 HOH HOH A . T 9 HOH 469 2268 2268 HOH HOH A . T 9 HOH 470 2269 2269 HOH HOH A . T 9 HOH 471 2270 2270 HOH HOH A . T 9 HOH 472 2271 2271 HOH HOH A . T 9 HOH 473 2272 2272 HOH HOH A . T 9 HOH 474 2273 2273 HOH HOH A . T 9 HOH 475 2274 2274 HOH HOH A . T 9 HOH 476 2275 2275 HOH HOH A . T 9 HOH 477 2276 2276 HOH HOH A . T 9 HOH 478 2277 2277 HOH HOH A . T 9 HOH 479 2278 2278 HOH HOH A . T 9 HOH 480 2279 2279 HOH HOH A . T 9 HOH 481 2280 2280 HOH HOH A . T 9 HOH 482 2281 2281 HOH HOH A . T 9 HOH 483 2282 2282 HOH HOH A . T 9 HOH 484 2283 2283 HOH HOH A . T 9 HOH 485 2284 2284 HOH HOH A . T 9 HOH 486 2285 2285 HOH HOH A . T 9 HOH 487 2286 2286 HOH HOH A . T 9 HOH 488 2287 2287 HOH HOH A . T 9 HOH 489 2288 2288 HOH HOH A . T 9 HOH 490 2289 2289 HOH HOH A . T 9 HOH 491 2290 2290 HOH HOH A . T 9 HOH 492 2291 2291 HOH HOH A . T 9 HOH 493 2292 2292 HOH HOH A . T 9 HOH 494 2293 2293 HOH HOH A . T 9 HOH 495 2294 2294 HOH HOH A . T 9 HOH 496 2295 2295 HOH HOH A . T 9 HOH 497 2296 2296 HOH HOH A . T 9 HOH 498 2297 2297 HOH HOH A . T 9 HOH 499 2298 2298 HOH HOH A . T 9 HOH 500 2299 2299 HOH HOH A . T 9 HOH 501 2300 2300 HOH HOH A . T 9 HOH 502 2301 2301 HOH HOH A . T 9 HOH 503 2302 2302 HOH HOH A . T 9 HOH 504 2303 2303 HOH HOH A . T 9 HOH 505 2304 2304 HOH HOH A . T 9 HOH 506 2305 2305 HOH HOH A . T 9 HOH 507 2306 2306 HOH HOH A . T 9 HOH 508 2307 2307 HOH HOH A . T 9 HOH 509 2308 2308 HOH HOH A . T 9 HOH 510 2309 2309 HOH HOH A . T 9 HOH 511 2310 2310 HOH HOH A . T 9 HOH 512 2311 2311 HOH HOH A . T 9 HOH 513 2312 2312 HOH HOH A . T 9 HOH 514 2313 2313 HOH HOH A . T 9 HOH 515 2314 2314 HOH HOH A . T 9 HOH 516 2315 2315 HOH HOH A . T 9 HOH 517 2316 2316 HOH HOH A . T 9 HOH 518 2317 2317 HOH HOH A . T 9 HOH 519 2318 2318 HOH HOH A . T 9 HOH 520 2319 2319 HOH HOH A . #