data_4MCQ # _entry.id 4MCQ # _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 4MCQ RCSB RCSB081746 WWPDB D_1000081746 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4MCP . unspecified PDB 4MCR . unspecified PDB 4MCS . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MCQ _pdbx_database_status.recvd_initial_deposition_date 2013-08-21 _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.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Navratil, M.' 1 'Barinka, C.' 2 # _citation.id primary _citation.title ;Structural and biochemical characterization of the folyl-poly-gamma-l-glutamate hydrolyzing activity of human glutamate carboxypeptidase II. ; _citation.journal_abbrev 'Febs J.' _citation.journal_volume 281 _citation.page_first 3228 _citation.page_last 3242 _citation.year 2014 _citation.journal_id_ASTM ? _citation.country UK _citation.journal_id_ISSN 1742-464X _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24863754 _citation.pdbx_database_id_DOI 10.1111/febs.12857 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Navratil, M.' 1 primary 'Ptacek, J.' 2 primary 'Sacha, P.' 3 primary 'Starkova, J.' 4 primary 'Lubkowski, J.' 5 primary 'Barinka, C.' 6 primary 'Konvalinka, J.' 7 # _cell.entry_id 4MCQ _cell.length_a 101.646 _cell.length_b 130.140 _cell.length_c 159.867 _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 4MCQ _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' 84972.914 1 3.4.17.21 E424A 'Glutamate carboxypeptidase II, unp residues 44-750' ? 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 'N-(4-{[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-gamma-glutamyl-L-gamma-glutamyl-L-glutamic acid' 699.625 1 ? ? ? ? 9 water nat water 18.015 521 ? ? ? ? # _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 ;MKLCILLAVVAFVGLSLGRSGLNDIFEAQKIEWHEGSGSGSENLYFQGRSKSSNEATNITPKHNMKAFLDELKAENIKKF LYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYEN VSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPAD YFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSA PPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAA VVHEIVRSFGTLKKEGWRPRRTILFASWDAAEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSL VHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYH SVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLF SAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALF DIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_seq_one_letter_code_can ;MKLCILLAVVAFVGLSLGRSGLNDIFEAQKIEWHEGSGSGSENLYFQGRSKSSNEATNITPKHNMKAFLDELKAENIKKF LYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYEN VSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPAD YFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSA PPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAA VVHEIVRSFGTLKKEGWRPRRTILFASWDAAEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSL VHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYH SVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLF SAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALF DIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _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 MET n 1 2 LYS n 1 3 LEU n 1 4 CYS n 1 5 ILE n 1 6 LEU n 1 7 LEU n 1 8 ALA n 1 9 VAL n 1 10 VAL n 1 11 ALA n 1 12 PHE n 1 13 VAL n 1 14 GLY n 1 15 LEU n 1 16 SER n 1 17 LEU n 1 18 GLY n 1 19 ARG n 1 20 SER n 1 21 GLY n 1 22 LEU n 1 23 ASN n 1 24 ASP n 1 25 ILE n 1 26 PHE n 1 27 GLU n 1 28 ALA n 1 29 GLN n 1 30 LYS n 1 31 ILE n 1 32 GLU n 1 33 TRP n 1 34 HIS n 1 35 GLU n 1 36 GLY n 1 37 SER n 1 38 GLY n 1 39 SER n 1 40 GLY n 1 41 SER n 1 42 GLU n 1 43 ASN n 1 44 LEU n 1 45 TYR n 1 46 PHE n 1 47 GLN n 1 48 GLY n 1 49 ARG n 1 50 SER n 1 51 LYS n 1 52 SER n 1 53 SER n 1 54 ASN n 1 55 GLU n 1 56 ALA n 1 57 THR n 1 58 ASN n 1 59 ILE n 1 60 THR n 1 61 PRO n 1 62 LYS n 1 63 HIS n 1 64 ASN n 1 65 MET n 1 66 LYS n 1 67 ALA n 1 68 PHE n 1 69 LEU n 1 70 ASP n 1 71 GLU n 1 72 LEU n 1 73 LYS n 1 74 ALA n 1 75 GLU n 1 76 ASN n 1 77 ILE n 1 78 LYS n 1 79 LYS n 1 80 PHE n 1 81 LEU n 1 82 TYR n 1 83 ASN n 1 84 PHE n 1 85 THR n 1 86 GLN n 1 87 ILE n 1 88 PRO n 1 89 HIS n 1 90 LEU n 1 91 ALA n 1 92 GLY n 1 93 THR n 1 94 GLU n 1 95 GLN n 1 96 ASN n 1 97 PHE n 1 98 GLN n 1 99 LEU n 1 100 ALA n 1 101 LYS n 1 102 GLN n 1 103 ILE n 1 104 GLN n 1 105 SER n 1 106 GLN n 1 107 TRP n 1 108 LYS n 1 109 GLU n 1 110 PHE n 1 111 GLY n 1 112 LEU n 1 113 ASP n 1 114 SER n 1 115 VAL n 1 116 GLU n 1 117 LEU n 1 118 ALA n 1 119 HIS n 1 120 TYR n 1 121 ASP n 1 122 VAL n 1 123 LEU n 1 124 LEU n 1 125 SER n 1 126 TYR n 1 127 PRO n 1 128 ASN n 1 129 LYS n 1 130 THR n 1 131 HIS n 1 132 PRO n 1 133 ASN n 1 134 TYR n 1 135 ILE n 1 136 SER n 1 137 ILE n 1 138 ILE n 1 139 ASN n 1 140 GLU n 1 141 ASP n 1 142 GLY n 1 143 ASN n 1 144 GLU n 1 145 ILE n 1 146 PHE n 1 147 ASN n 1 148 THR n 1 149 SER n 1 150 LEU n 1 151 PHE n 1 152 GLU n 1 153 PRO n 1 154 PRO n 1 155 PRO n 1 156 PRO n 1 157 GLY n 1 158 TYR n 1 159 GLU n 1 160 ASN n 1 161 VAL n 1 162 SER n 1 163 ASP n 1 164 ILE n 1 165 VAL n 1 166 PRO n 1 167 PRO n 1 168 PHE n 1 169 SER n 1 170 ALA n 1 171 PHE n 1 172 SER n 1 173 PRO n 1 174 GLN n 1 175 GLY n 1 176 MET n 1 177 PRO n 1 178 GLU n 1 179 GLY n 1 180 ASP n 1 181 LEU n 1 182 VAL n 1 183 TYR n 1 184 VAL n 1 185 ASN n 1 186 TYR n 1 187 ALA n 1 188 ARG n 1 189 THR n 1 190 GLU n 1 191 ASP n 1 192 PHE n 1 193 PHE n 1 194 LYS n 1 195 LEU n 1 196 GLU n 1 197 ARG n 1 198 ASP n 1 199 MET n 1 200 LYS n 1 201 ILE n 1 202 ASN n 1 203 CYS n 1 204 SER n 1 205 GLY n 1 206 LYS n 1 207 ILE n 1 208 VAL n 1 209 ILE n 1 210 ALA n 1 211 ARG n 1 212 TYR n 1 213 GLY n 1 214 LYS n 1 215 VAL n 1 216 PHE n 1 217 ARG n 1 218 GLY n 1 219 ASN n 1 220 LYS n 1 221 VAL n 1 222 LYS n 1 223 ASN n 1 224 ALA n 1 225 GLN n 1 226 LEU n 1 227 ALA n 1 228 GLY n 1 229 ALA n 1 230 LYS n 1 231 GLY n 1 232 VAL n 1 233 ILE n 1 234 LEU n 1 235 TYR n 1 236 SER n 1 237 ASP n 1 238 PRO n 1 239 ALA n 1 240 ASP n 1 241 TYR n 1 242 PHE n 1 243 ALA n 1 244 PRO n 1 245 GLY n 1 246 VAL n 1 247 LYS n 1 248 SER n 1 249 TYR n 1 250 PRO n 1 251 ASP n 1 252 GLY n 1 253 TRP n 1 254 ASN n 1 255 LEU n 1 256 PRO n 1 257 GLY n 1 258 GLY n 1 259 GLY n 1 260 VAL n 1 261 GLN n 1 262 ARG n 1 263 GLY n 1 264 ASN n 1 265 ILE n 1 266 LEU n 1 267 ASN n 1 268 LEU n 1 269 ASN n 1 270 GLY n 1 271 ALA n 1 272 GLY n 1 273 ASP n 1 274 PRO n 1 275 LEU n 1 276 THR n 1 277 PRO n 1 278 GLY n 1 279 TYR n 1 280 PRO n 1 281 ALA n 1 282 ASN n 1 283 GLU n 1 284 TYR n 1 285 ALA n 1 286 TYR n 1 287 ARG n 1 288 ARG n 1 289 GLY n 1 290 ILE n 1 291 ALA n 1 292 GLU n 1 293 ALA n 1 294 VAL n 1 295 GLY n 1 296 LEU n 1 297 PRO n 1 298 SER n 1 299 ILE n 1 300 PRO n 1 301 VAL n 1 302 HIS n 1 303 PRO n 1 304 ILE n 1 305 GLY n 1 306 TYR n 1 307 TYR n 1 308 ASP n 1 309 ALA n 1 310 GLN n 1 311 LYS n 1 312 LEU n 1 313 LEU n 1 314 GLU n 1 315 LYS n 1 316 MET n 1 317 GLY n 1 318 GLY n 1 319 SER n 1 320 ALA n 1 321 PRO n 1 322 PRO n 1 323 ASP n 1 324 SER n 1 325 SER n 1 326 TRP n 1 327 ARG n 1 328 GLY n 1 329 SER n 1 330 LEU n 1 331 LYS n 1 332 VAL n 1 333 PRO n 1 334 TYR n 1 335 ASN n 1 336 VAL n 1 337 GLY n 1 338 PRO n 1 339 GLY n 1 340 PHE n 1 341 THR n 1 342 GLY n 1 343 ASN n 1 344 PHE n 1 345 SER n 1 346 THR n 1 347 GLN n 1 348 LYS n 1 349 VAL n 1 350 LYS n 1 351 MET n 1 352 HIS n 1 353 ILE n 1 354 HIS n 1 355 SER n 1 356 THR n 1 357 ASN n 1 358 GLU n 1 359 VAL n 1 360 THR n 1 361 ARG n 1 362 ILE n 1 363 TYR n 1 364 ASN n 1 365 VAL n 1 366 ILE n 1 367 GLY n 1 368 THR n 1 369 LEU n 1 370 ARG n 1 371 GLY n 1 372 ALA n 1 373 VAL n 1 374 GLU n 1 375 PRO n 1 376 ASP n 1 377 ARG n 1 378 TYR n 1 379 VAL n 1 380 ILE n 1 381 LEU n 1 382 GLY n 1 383 GLY n 1 384 HIS n 1 385 ARG n 1 386 ASP n 1 387 SER n 1 388 TRP n 1 389 VAL n 1 390 PHE n 1 391 GLY n 1 392 GLY n 1 393 ILE n 1 394 ASP n 1 395 PRO n 1 396 GLN n 1 397 SER n 1 398 GLY n 1 399 ALA n 1 400 ALA n 1 401 VAL n 1 402 VAL n 1 403 HIS n 1 404 GLU n 1 405 ILE n 1 406 VAL n 1 407 ARG n 1 408 SER n 1 409 PHE n 1 410 GLY n 1 411 THR n 1 412 LEU n 1 413 LYS n 1 414 LYS n 1 415 GLU n 1 416 GLY n 1 417 TRP n 1 418 ARG n 1 419 PRO n 1 420 ARG n 1 421 ARG n 1 422 THR n 1 423 ILE n 1 424 LEU n 1 425 PHE n 1 426 ALA n 1 427 SER n 1 428 TRP n 1 429 ASP n 1 430 ALA n 1 431 ALA n 1 432 GLU n 1 433 PHE n 1 434 GLY n 1 435 LEU n 1 436 LEU n 1 437 GLY n 1 438 SER n 1 439 THR n 1 440 GLU n 1 441 TRP n 1 442 ALA n 1 443 GLU n 1 444 GLU n 1 445 ASN n 1 446 SER n 1 447 ARG n 1 448 LEU n 1 449 LEU n 1 450 GLN n 1 451 GLU n 1 452 ARG n 1 453 GLY n 1 454 VAL n 1 455 ALA n 1 456 TYR n 1 457 ILE n 1 458 ASN n 1 459 ALA n 1 460 ASP n 1 461 SER n 1 462 SER n 1 463 ILE n 1 464 GLU n 1 465 GLY n 1 466 ASN n 1 467 TYR n 1 468 THR n 1 469 LEU n 1 470 ARG n 1 471 VAL n 1 472 ASP n 1 473 CYS n 1 474 THR n 1 475 PRO n 1 476 LEU n 1 477 MET n 1 478 TYR n 1 479 SER n 1 480 LEU n 1 481 VAL n 1 482 HIS n 1 483 ASN n 1 484 LEU n 1 485 THR n 1 486 LYS n 1 487 GLU n 1 488 LEU n 1 489 LYS n 1 490 SER n 1 491 PRO n 1 492 ASP n 1 493 GLU n 1 494 GLY n 1 495 PHE n 1 496 GLU n 1 497 GLY n 1 498 LYS n 1 499 SER n 1 500 LEU n 1 501 TYR n 1 502 GLU n 1 503 SER n 1 504 TRP n 1 505 THR n 1 506 LYS n 1 507 LYS n 1 508 SER n 1 509 PRO n 1 510 SER n 1 511 PRO n 1 512 GLU n 1 513 PHE n 1 514 SER n 1 515 GLY n 1 516 MET n 1 517 PRO n 1 518 ARG n 1 519 ILE n 1 520 SER n 1 521 LYS n 1 522 LEU n 1 523 GLY n 1 524 SER n 1 525 GLY n 1 526 ASN n 1 527 ASP n 1 528 PHE n 1 529 GLU n 1 530 VAL n 1 531 PHE n 1 532 PHE n 1 533 GLN n 1 534 ARG n 1 535 LEU n 1 536 GLY n 1 537 ILE n 1 538 ALA n 1 539 SER n 1 540 GLY n 1 541 ARG n 1 542 ALA n 1 543 ARG n 1 544 TYR n 1 545 THR n 1 546 LYS n 1 547 ASN n 1 548 TRP n 1 549 GLU n 1 550 THR n 1 551 ASN n 1 552 LYS n 1 553 PHE n 1 554 SER n 1 555 GLY n 1 556 TYR n 1 557 PRO n 1 558 LEU n 1 559 TYR n 1 560 HIS n 1 561 SER n 1 562 VAL n 1 563 TYR n 1 564 GLU n 1 565 THR n 1 566 TYR n 1 567 GLU n 1 568 LEU n 1 569 VAL n 1 570 GLU n 1 571 LYS n 1 572 PHE n 1 573 TYR n 1 574 ASP n 1 575 PRO n 1 576 MET n 1 577 PHE n 1 578 LYS n 1 579 TYR n 1 580 HIS n 1 581 LEU n 1 582 THR n 1 583 VAL n 1 584 ALA n 1 585 GLN n 1 586 VAL n 1 587 ARG n 1 588 GLY n 1 589 GLY n 1 590 MET n 1 591 VAL n 1 592 PHE n 1 593 GLU n 1 594 LEU n 1 595 ALA n 1 596 ASN n 1 597 SER n 1 598 ILE n 1 599 VAL n 1 600 LEU n 1 601 PRO n 1 602 PHE n 1 603 ASP n 1 604 CYS n 1 605 ARG n 1 606 ASP n 1 607 TYR n 1 608 ALA n 1 609 VAL n 1 610 VAL n 1 611 LEU n 1 612 ARG n 1 613 LYS n 1 614 TYR n 1 615 ALA n 1 616 ASP n 1 617 LYS n 1 618 ILE n 1 619 TYR n 1 620 SER n 1 621 ILE n 1 622 SER n 1 623 MET n 1 624 LYS n 1 625 HIS n 1 626 PRO n 1 627 GLN n 1 628 GLU n 1 629 MET n 1 630 LYS n 1 631 THR n 1 632 TYR n 1 633 SER n 1 634 VAL n 1 635 SER n 1 636 PHE n 1 637 ASP n 1 638 SER n 1 639 LEU n 1 640 PHE n 1 641 SER n 1 642 ALA n 1 643 VAL n 1 644 LYS n 1 645 ASN n 1 646 PHE n 1 647 THR n 1 648 GLU n 1 649 ILE n 1 650 ALA n 1 651 SER n 1 652 LYS n 1 653 PHE n 1 654 SER n 1 655 GLU n 1 656 ARG n 1 657 LEU n 1 658 GLN n 1 659 ASP n 1 660 PHE n 1 661 ASP n 1 662 LYS n 1 663 SER n 1 664 ASN n 1 665 PRO n 1 666 ILE n 1 667 VAL n 1 668 LEU n 1 669 ARG n 1 670 MET n 1 671 MET n 1 672 ASN n 1 673 ASP n 1 674 GLN n 1 675 LEU n 1 676 MET n 1 677 PHE n 1 678 LEU n 1 679 GLU n 1 680 ARG n 1 681 ALA n 1 682 PHE n 1 683 ILE n 1 684 ASP n 1 685 PRO n 1 686 LEU n 1 687 GLY n 1 688 LEU n 1 689 PRO n 1 690 ASP n 1 691 ARG n 1 692 PRO n 1 693 PHE n 1 694 TYR n 1 695 ARG n 1 696 HIS n 1 697 VAL n 1 698 ILE n 1 699 TYR n 1 700 ALA n 1 701 PRO n 1 702 SER n 1 703 SER n 1 704 HIS n 1 705 ASN n 1 706 LYS n 1 707 TYR n 1 708 ALA n 1 709 GLY n 1 710 GLU n 1 711 SER n 1 712 PHE n 1 713 PRO n 1 714 GLY n 1 715 ILE n 1 716 TYR n 1 717 ASP n 1 718 ALA n 1 719 LEU n 1 720 PHE n 1 721 ASP n 1 722 ILE n 1 723 GLU n 1 724 SER n 1 725 LYS n 1 726 VAL n 1 727 ASP n 1 728 PRO n 1 729 SER n 1 730 LYS n 1 731 ALA n 1 732 TRP n 1 733 GLY n 1 734 GLU n 1 735 VAL n 1 736 LYS n 1 737 ARG n 1 738 GLN n 1 739 ILE n 1 740 TYR n 1 741 VAL n 1 742 ALA n 1 743 ALA n 1 744 PHE n 1 745 THR n 1 746 VAL n 1 747 GLN n 1 748 ALA n 1 749 ALA n 1 750 ALA n 1 751 GLU n 1 752 THR n 1 753 LEU n 1 754 SER n 1 755 GLU n 1 756 VAL n 1 757 ALA n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'FOLH1, FOLH, NAALAD1, PSM, PSMA, GIG27' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Drosophila Melanogaster' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7227 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ;Schneider's S2 ; _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 4MCQ _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 51 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 757 _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 4MCQ MET A 1 ? UNP Q04609 ? ? 'INITIATING METHIONINE' -6 1 1 4MCQ LYS A 2 ? UNP Q04609 ? ? 'EXPRESSION TAG' -5 2 1 4MCQ LEU A 3 ? UNP Q04609 ? ? 'EXPRESSION TAG' -4 3 1 4MCQ CYS A 4 ? UNP Q04609 ? ? 'EXPRESSION TAG' -3 4 1 4MCQ ILE A 5 ? UNP Q04609 ? ? 'EXPRESSION TAG' -2 5 1 4MCQ LEU A 6 ? UNP Q04609 ? ? 'EXPRESSION TAG' -1 6 1 4MCQ LEU A 7 ? UNP Q04609 ? ? 'EXPRESSION TAG' 0 7 1 4MCQ ALA A 8 ? UNP Q04609 ? ? 'EXPRESSION TAG' 1 8 1 4MCQ VAL A 9 ? UNP Q04609 ? ? 'EXPRESSION TAG' 2 9 1 4MCQ VAL A 10 ? UNP Q04609 ? ? 'EXPRESSION TAG' 3 10 1 4MCQ ALA A 11 ? UNP Q04609 ? ? 'EXPRESSION TAG' 4 11 1 4MCQ PHE A 12 ? UNP Q04609 ? ? 'EXPRESSION TAG' 5 12 1 4MCQ VAL A 13 ? UNP Q04609 ? ? 'EXPRESSION TAG' 6 13 1 4MCQ GLY A 14 ? UNP Q04609 ? ? 'EXPRESSION TAG' 7 14 1 4MCQ LEU A 15 ? UNP Q04609 ? ? 'EXPRESSION TAG' 8 15 1 4MCQ SER A 16 ? UNP Q04609 ? ? 'EXPRESSION TAG' 9 16 1 4MCQ LEU A 17 ? UNP Q04609 ? ? 'EXPRESSION TAG' 10 17 1 4MCQ GLY A 18 ? UNP Q04609 ? ? 'EXPRESSION TAG' 11 18 1 4MCQ ARG A 19 ? UNP Q04609 ? ? 'EXPRESSION TAG' 12 19 1 4MCQ SER A 20 ? UNP Q04609 ? ? 'EXPRESSION TAG' 13 20 1 4MCQ GLY A 21 ? UNP Q04609 ? ? 'EXPRESSION TAG' 14 21 1 4MCQ LEU A 22 ? UNP Q04609 ? ? 'EXPRESSION TAG' 15 22 1 4MCQ ASN A 23 ? UNP Q04609 ? ? 'EXPRESSION TAG' 16 23 1 4MCQ ASP A 24 ? UNP Q04609 ? ? 'EXPRESSION TAG' 17 24 1 4MCQ ILE A 25 ? UNP Q04609 ? ? 'EXPRESSION TAG' 18 25 1 4MCQ PHE A 26 ? UNP Q04609 ? ? 'EXPRESSION TAG' 19 26 1 4MCQ GLU A 27 ? UNP Q04609 ? ? 'EXPRESSION TAG' 20 27 1 4MCQ ALA A 28 ? UNP Q04609 ? ? 'EXPRESSION TAG' 21 28 1 4MCQ GLN A 29 ? UNP Q04609 ? ? 'EXPRESSION TAG' 22 29 1 4MCQ LYS A 30 ? UNP Q04609 ? ? 'EXPRESSION TAG' 23 30 1 4MCQ ILE A 31 ? UNP Q04609 ? ? 'EXPRESSION TAG' 24 31 1 4MCQ GLU A 32 ? UNP Q04609 ? ? 'EXPRESSION TAG' 25 32 1 4MCQ TRP A 33 ? UNP Q04609 ? ? 'EXPRESSION TAG' 26 33 1 4MCQ HIS A 34 ? UNP Q04609 ? ? 'EXPRESSION TAG' 27 34 1 4MCQ GLU A 35 ? UNP Q04609 ? ? 'EXPRESSION TAG' 28 35 1 4MCQ GLY A 36 ? UNP Q04609 ? ? 'EXPRESSION TAG' 29 36 1 4MCQ SER A 37 ? UNP Q04609 ? ? 'EXPRESSION TAG' 30 37 1 4MCQ GLY A 38 ? UNP Q04609 ? ? 'EXPRESSION TAG' 31 38 1 4MCQ SER A 39 ? UNP Q04609 ? ? 'EXPRESSION TAG' 32 39 1 4MCQ GLY A 40 ? UNP Q04609 ? ? 'EXPRESSION TAG' 33 40 1 4MCQ SER A 41 ? UNP Q04609 ? ? 'EXPRESSION TAG' 34 41 1 4MCQ GLU A 42 ? UNP Q04609 ? ? 'EXPRESSION TAG' 35 42 1 4MCQ ASN A 43 ? UNP Q04609 ? ? 'EXPRESSION TAG' 36 43 1 4MCQ LEU A 44 ? UNP Q04609 ? ? 'EXPRESSION TAG' 37 44 1 4MCQ TYR A 45 ? UNP Q04609 ? ? 'EXPRESSION TAG' 38 45 1 4MCQ PHE A 46 ? UNP Q04609 ? ? 'EXPRESSION TAG' 39 46 1 4MCQ GLN A 47 ? UNP Q04609 ? ? 'EXPRESSION TAG' 40 47 1 4MCQ GLY A 48 ? UNP Q04609 ? ? 'EXPRESSION TAG' 41 48 1 4MCQ ARG A 49 ? UNP Q04609 ? ? 'EXPRESSION TAG' 42 49 1 4MCQ SER A 50 ? UNP Q04609 ? ? 'EXPRESSION TAG' 43 50 1 4MCQ ALA A 431 ? UNP Q04609 GLU 424 'ENGINEERED MUTATION' 424 51 # 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 29C non-polymer . 'N-(4-{[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-gamma-glutamyl-L-gamma-glutamyl-L-glutamic acid' ? 'C29 H33 N9 O12' 699.625 ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 4MCQ _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.11 _exptl_crystal.density_percent_sol 60.46 _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_pH_range ? _exptl_crystal_grow.pdbx_details ;33% (v/v) pentaerythritol, propoxylate PO/OH 5/4, 0.5% (w/v) PEG 3350, 0.10 M Tris HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K ; # _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 'RAYONIX MX-225' _diffrn_detector.pdbx_collection_date 2010-03-03 _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) 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 0.918 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'BESSY BEAMLINE 14.2' _diffrn_source.pdbx_synchrotron_site BESSY _diffrn_source.pdbx_synchrotron_beamline 14.2 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.918 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MCQ _reflns.observed_criterion_sigma_I -3 _reflns.observed_criterion_sigma_F -3 _reflns.d_resolution_low 50.0 _reflns.d_resolution_high 2.00 _reflns.number_obs 72031 _reflns.number_all 72031 _reflns.percent_possible_obs 99.3 _reflns.pdbx_Rmerge_I_obs 0.051 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 30.1 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.00 _reflns_shell.d_res_low 2.07 _reflns_shell.percent_possible_all 94.8 _reflns_shell.Rmerge_I_obs 0.226 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 5.0 _reflns_shell.pdbx_redundancy 4.4 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4MCQ _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 69042 _refine.ls_number_reflns_all 69371 _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 22.96 _refine.ls_d_res_high 2.00 _refine.ls_percent_reflns_obs 98.04 _refine.ls_R_factor_obs 0.13797 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.13735 _refine.ls_R_factor_R_free 0.17168 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 1.7 _refine.ls_number_reflns_R_free 1188 _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 0.961 _refine.B_iso_mean 27.576 _refine.aniso_B[1][1] -0.07 _refine.aniso_B[2][2] 0.13 _refine.aniso_B[3][3] -0.05 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.221 _refine.pdbx_overall_ESU_R_Free 0.107 _refine.overall_SU_ML 0.073 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 5.774 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_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_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 5516 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 230 _refine_hist.number_atoms_solvent 521 _refine_hist.number_atoms_total 6267 _refine_hist.d_res_high 2.00 _refine_hist.d_res_low 22.96 # 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_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.021 0.022 ? 6197 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.664 1.995 ? 8411 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.966 5.000 ? 726 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.789 23.671 ? 286 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 13.860 15.000 ? 998 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 16.095 15.000 ? 37 'X-RAY DIFFRACTION' ? r_chiral_restr 0.118 0.200 ? 898 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.008 0.021 ? 4782 '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 1.413 1.500 ? 3588 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 2.276 2.000 ? 5822 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 3.458 3.000 ? 2609 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 5.096 4.500 ? 2587 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr 1.981 3.000 ? 6197 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.000 _refine_ls_shell.d_res_low 2.052 _refine_ls_shell.number_reflns_R_work 4431 _refine_ls_shell.R_factor_R_work 0.146 _refine_ls_shell.percent_reflns_obs 86.16 _refine_ls_shell.R_factor_R_free 0.206 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 64 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_obs ? # _pdbx_refine.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine.entry_id 4MCQ _pdbx_refine.R_factor_all_no_cutoff ? _pdbx_refine.R_factor_obs_no_cutoff ? _pdbx_refine.free_R_factor_no_cutoff ? _pdbx_refine.free_R_error_no_cutoff ? _pdbx_refine.free_R_val_test_set_size_perc_no_cutoff ? _pdbx_refine.free_R_val_test_set_ct_no_cutoff ? _pdbx_refine.R_factor_all_4sig_cutoff ? _pdbx_refine.R_factor_obs_4sig_cutoff ? _pdbx_refine.free_R_factor_4sig_cutoff ? _pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff ? _pdbx_refine.free_R_val_test_set_ct_4sig_cutoff ? _pdbx_refine.number_reflns_obs_4sig_cutoff ? # _struct.entry_id 4MCQ _struct.title ;A high resolution structure of human glutamate carboxypeptidase II (GCPII) in complex with folyldi-gamma-L-glutamic acid (pteroyltri-gamma-L-glutamic 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 4MCQ _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'hydrolase, metallopeptidase, hydrolase-hydrolase inhibitor complex, Prostate specific membrane antigen, folate hydrolase 1, FOLH1' # 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 64 ? LEU A 72 ? ASN A 57 LEU A 65 1 ? 9 HELX_P HELX_P2 2 LYS A 73 ? THR A 85 ? LYS A 66 THR A 78 1 ? 13 HELX_P HELX_P3 3 THR A 93 ? PHE A 110 ? THR A 86 PHE A 103 1 ? 18 HELX_P HELX_P4 4 ARG A 188 ? ASP A 198 ? ARG A 181 ASP A 191 1 ? 11 HELX_P HELX_P5 5 PHE A 216 ? ALA A 227 ? PHE A 209 ALA A 220 1 ? 12 HELX_P HELX_P6 6 ASP A 237 ? PHE A 242 ? ASP A 230 PHE A 235 1 ? 6 HELX_P HELX_P7 7 GLY A 289 ? ALA A 293 ? GLY A 282 ALA A 286 5 ? 5 HELX_P HELX_P8 8 GLY A 305 ? GLU A 314 ? GLY A 298 GLU A 307 1 ? 10 HELX_P HELX_P9 9 ASP A 323 ? ARG A 327 ? ASP A 316 ARG A 320 5 ? 5 HELX_P HELX_P10 10 THR A 341 ? SER A 345 ? THR A 334 SER A 338 5 ? 5 HELX_P HELX_P11 11 PRO A 395 ? GLU A 415 ? PRO A 388 GLU A 408 1 ? 21 HELX_P HELX_P12 12 ALA A 430 ? GLY A 434 ? ALA A 423 GLY A 427 5 ? 5 HELX_P HELX_P13 13 LEU A 435 ? ARG A 452 ? LEU A 428 ARG A 445 1 ? 18 HELX_P HELX_P14 14 MET A 477 ? GLU A 487 ? MET A 470 GLU A 480 1 ? 11 HELX_P HELX_P15 15 SER A 499 ? SER A 508 ? SER A 492 SER A 501 1 ? 10 HELX_P HELX_P16 16 PHE A 528 ? ARG A 534 ? PHE A 521 ARG A 527 1 ? 7 HELX_P HELX_P17 17 THR A 565 ? TYR A 573 ? THR A 558 TYR A 566 1 ? 9 HELX_P HELX_P18 18 PHE A 577 ? SER A 597 ? PHE A 570 SER A 590 1 ? 21 HELX_P HELX_P19 19 ASP A 603 ? MET A 623 ? ASP A 596 MET A 616 1 ? 21 HELX_P HELX_P20 20 HIS A 625 ? SER A 633 ? HIS A 618 SER A 626 1 ? 9 HELX_P HELX_P21 21 PHE A 636 ? ASP A 659 ? PHE A 629 ASP A 652 1 ? 24 HELX_P HELX_P22 22 ASN A 664 ? PHE A 682 ? ASN A 657 PHE A 675 1 ? 19 HELX_P HELX_P23 23 PHE A 712 ? PHE A 720 ? PHE A 705 PHE A 713 1 ? 9 HELX_P HELX_P24 24 ASP A 721 ? LYS A 725 ? ASP A 714 LYS A 718 5 ? 5 HELX_P HELX_P25 25 ASP A 727 ? THR A 752 ? 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 483 ND2 ? ? ? 1_555 M NAG . C1 ? ? A ASN 476 A NAG 812 1_555 ? ? ? ? ? ? ? 1.429 ? covale2 covale ? ? A ASN 83 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 76 A NAG 805 1_555 ? ? ? ? ? ? ? 1.431 ? covale3 covale ? ? A ASN 466 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 459 A NAG 811 1_555 ? ? ? ? ? ? ? 1.436 ? covale4 covale ? ? O NAG . O4 ? ? ? 1_555 P NAG . C1 ? ? A NAG 814 A NAG 815 1_555 ? ? ? ? ? ? ? 1.437 ? covale5 covale ? ? P NAG . O4 ? ? ? 1_555 Q BMA . C1 ? ? A NAG 815 A BMA 816 1_555 ? ? ? ? ? ? ? 1.440 ? covale6 covale ? ? A ASN 645 ND2 ? ? ? 1_555 O NAG . C1 ? ? A ASN 638 A NAG 814 1_555 ? ? ? ? ? ? ? 1.440 ? covale7 covale ? ? M NAG . O4 ? ? ? 1_555 N NAG . C1 ? ? A NAG 812 A NAG 813 1_555 ? ? ? ? ? ? ? 1.445 ? covale8 covale ? ? A ASN 147 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 140 A NAG 808 1_555 ? ? ? ? ? ? ? 1.448 ? covale9 covale ? ? A ASN 128 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 121 A NAG 807 1_555 ? ? ? ? ? ? ? 1.449 ? covale10 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 805 A NAG 806 1_555 ? ? ? ? ? ? ? 1.449 ? covale11 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 808 A NAG 809 1_555 ? ? ? ? ? ? ? 1.457 ? covale12 covale ? ? Q BMA . O3 ? ? ? 1_555 R MAN . C1 ? ? A BMA 816 A MAN 817 1_555 ? ? ? ? ? ? ? 1.458 ? covale13 covale ? ? A ASN 202 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 195 A NAG 810 1_555 ? ? ? ? ? ? ? 1.460 ? metalc1 metalc ? ? C ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 802 A HOH 1309 1_555 ? ? ? ? ? ? ? 1.969 ? metalc2 metalc ? ? B ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 801 A HOH 1309 1_555 ? ? ? ? ? ? ? 1.970 ? metalc3 metalc ? ? A ASP 394 OD1 ? ? ? 1_555 C ZN . ZN ? ? A ASP 387 A ZN 802 1_555 ? ? ? ? ? ? ? 1.984 ? metalc4 metalc ? ? A ASP 460 OD2 ? ? ? 1_555 C ZN . ZN ? ? A ASP 453 A ZN 802 1_555 ? ? ? ? ? ? ? 1.986 ? metalc5 metalc ? ? A ASP 394 OD2 ? ? ? 1_555 B ZN . ZN ? ? A ASP 387 A ZN 801 1_555 ? ? ? ? ? ? ? 1.997 ? metalc6 metalc ? ? A HIS 384 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 377 A ZN 802 1_555 ? ? ? ? ? ? ? 2.024 ? metalc7 metalc ? ? A GLU 432 OE2 ? ? ? 1_555 B ZN . ZN ? ? A GLU 425 A ZN 801 1_555 ? ? ? ? ? ? ? 2.071 ? metalc8 metalc ? ? A HIS 560 NE2 ? ? ? 1_555 B ZN . ZN ? ? A HIS 553 A ZN 801 1_555 ? ? ? ? ? ? ? 2.071 ? metalc9 metalc ? ? B ZN . ZN ? ? ? 1_555 S 29C . OAF ? ? A ZN 801 A 29C 818 1_555 ? ? ? ? ? ? ? 2.157 ? metalc10 metalc ? ? A GLU 432 OE1 ? ? ? 1_555 B ZN . ZN ? ? A GLU 425 A ZN 801 1_555 ? ? ? ? ? ? ? 2.183 ? metalc11 metalc ? ? A GLU 443 OE2 ? ? ? 1_555 D CA . CA ? ? A GLU 436 A CA 803 1_555 ? ? ? ? ? ? ? 2.326 ? metalc12 metalc ? ? A TYR 279 O ? ? ? 1_555 D CA . CA ? ? A TYR 272 A CA 803 1_555 ? ? ? ? ? ? ? 2.341 ? metalc13 metalc ? ? A THR 276 O ? ? ? 1_555 D CA . CA ? ? A THR 269 A CA 803 1_555 ? ? ? ? ? ? ? 2.362 ? metalc14 metalc ? ? D CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 803 A HOH 906 1_555 ? ? ? ? ? ? ? 2.369 ? metalc15 metalc ? ? A GLU 440 OE1 ? ? ? 1_555 D CA . CA ? ? A GLU 433 A CA 803 1_555 ? ? ? ? ? ? ? 2.374 ? metalc16 metalc ? ? A THR 276 OG1 ? ? ? 1_555 D CA . CA ? ? A THR 269 A CA 803 1_555 ? ? ? ? ? ? ? 2.384 ? metalc17 metalc ? ? A GLU 440 OE2 ? ? ? 1_555 D CA . CA ? ? A GLU 433 A CA 803 1_555 ? ? ? ? ? ? ? 2.389 ? # 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 249 A . ? TYR 242 A PRO 250 A ? PRO 243 A 1 5.82 2 GLY 337 A . ? GLY 330 A PRO 338 A ? PRO 331 A 1 -2.88 3 ASP 394 A . ? ASP 387 A PRO 395 A ? PRO 388 A 1 6.12 # 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 114 ? TYR A 126 ? SER A 107 TYR A 119 A 2 THR A 356 ? LEU A 369 ? THR A 349 LEU A 362 A 3 ARG A 421 ? TRP A 428 ? ARG A 414 TRP A 421 A 4 GLU A 374 ? HIS A 384 ? GLU A 367 HIS A 377 A 5 GLY A 453 ? ASN A 458 ? GLY A 446 ASN A 451 A 6 ALA A 538 ? THR A 545 ? ALA A 531 THR A 538 A 7 THR A 468 ? CYS A 473 ? THR A 461 CYS A 466 B 1 GLU A 144 ? ASN A 147 ? GLU A 137 ASN A 140 B 2 TYR A 134 ? ILE A 138 ? TYR A 127 ILE A 131 B 3 LYS A 348 ? HIS A 352 ? LYS A 341 HIS A 345 B 4 GLU A 178 ? GLY A 179 ? GLU A 171 GLY A 172 C 1 SER A 169 ? ALA A 170 ? SER A 162 ALA A 163 C 2 GLY A 263 ? ASN A 264 ? GLY A 256 ASN A 257 D 1 LEU A 181 ? TYR A 183 ? LEU A 174 TYR A 176 D 2 ILE A 207 ? ARG A 211 ? ILE A 200 ARG A 204 D 3 GLY A 231 ? TYR A 235 ? GLY A 224 TYR A 228 D 4 VAL A 301 ? ILE A 304 ? VAL A 294 ILE A 297 E 1 TYR A 699 ? SER A 702 ? TYR A 692 SER A 695 E 2 ASN A 705 ? SER A 711 ? 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 118 ? N ALA A 111 O ASN A 364 ? O ASN A 357 A 2 3 N GLY A 367 ? N GLY A 360 O PHE A 425 ? O PHE A 418 A 3 4 O LEU A 424 ? O LEU A 417 N LEU A 381 ? N LEU A 374 A 4 5 N ILE A 380 ? N ILE A 373 O ILE A 457 ? O ILE A 450 A 5 6 N ASN A 458 ? N ASN A 451 O GLY A 540 ? O GLY A 533 A 6 7 O THR A 545 ? O THR A 538 N THR A 468 ? N THR A 461 B 1 2 O ILE A 145 ? O ILE A 138 N ILE A 137 ? N ILE A 130 B 2 3 N SER A 136 ? N SER A 129 O LYS A 350 ? O LYS A 343 B 3 4 O VAL A 349 ? O VAL A 342 N GLY A 179 ? N GLY A 172 C 1 2 O ALA A 170 ? O ALA A 163 N GLY A 263 ? N GLY A 256 D 1 2 N VAL A 182 ? N VAL A 175 O ILE A 209 ? O ILE A 202 D 2 3 N ALA A 210 ? N ALA A 203 O ILE A 233 ? O ILE A 226 D 3 4 N LEU A 234 ? N LEU A 227 O HIS A 302 ? O HIS A 295 E 1 2 N SER A 702 ? N SER A 695 O ALA A 708 ? 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 801' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ZN A 802' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 803' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CL A 804' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 805' AC6 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 806' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 807' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 808' AC9 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 809' BC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 810' BC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 811' BC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 812' BC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 813' BC5 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 814' BC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 815' BC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE BMA A 816' BC8 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE MAN A 817' BC9 Software ? ? ? ? 30 'BINDING SITE FOR RESIDUE 29C A 818' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 ASP A 394 ? ASP A 387 . ? 1_555 ? 2 AC1 6 GLU A 432 ? GLU A 425 . ? 1_555 ? 3 AC1 6 HIS A 560 ? HIS A 553 . ? 1_555 ? 4 AC1 6 ZN C . ? ZN A 802 . ? 1_555 ? 5 AC1 6 29C S . ? 29C A 818 . ? 1_555 ? 6 AC1 6 HOH T . ? HOH A 1309 . ? 1_555 ? 7 AC2 6 HIS A 384 ? HIS A 377 . ? 1_555 ? 8 AC2 6 ASP A 394 ? ASP A 387 . ? 1_555 ? 9 AC2 6 GLU A 432 ? GLU A 425 . ? 1_555 ? 10 AC2 6 ASP A 460 ? ASP A 453 . ? 1_555 ? 11 AC2 6 ZN B . ? ZN A 801 . ? 1_555 ? 12 AC2 6 HOH T . ? HOH A 1309 . ? 1_555 ? 13 AC3 5 THR A 276 ? THR A 269 . ? 1_555 ? 14 AC3 5 TYR A 279 ? TYR A 272 . ? 1_555 ? 15 AC3 5 GLU A 440 ? GLU A 433 . ? 1_555 ? 16 AC3 5 GLU A 443 ? GLU A 436 . ? 1_555 ? 17 AC3 5 HOH T . ? HOH A 906 . ? 1_555 ? 18 AC4 5 ASN A 458 ? ASN A 451 . ? 1_555 ? 19 AC4 5 ASP A 460 ? ASP A 453 . ? 1_555 ? 20 AC4 5 ARG A 541 ? ARG A 534 . ? 1_555 ? 21 AC4 5 ARG A 543 ? ARG A 536 . ? 1_555 ? 22 AC4 5 HOH T . ? HOH A 921 . ? 1_555 ? 23 AC5 6 ASN A 83 ? ASN A 76 . ? 1_555 ? 24 AC5 6 GLN A 102 ? GLN A 95 . ? 1_555 ? 25 AC5 6 GLN A 106 ? GLN A 99 . ? 1_555 ? 26 AC5 6 NAG G . ? NAG A 806 . ? 1_555 ? 27 AC5 6 HOH T . ? HOH A 1124 . ? 1_555 ? 28 AC5 6 HOH T . ? HOH A 1255 . ? 1_555 ? 29 AC6 1 NAG F . ? NAG A 805 . ? 1_555 ? 30 AC7 4 ASN A 128 ? ASN A 121 . ? 1_555 ? 31 AC7 4 HIS A 131 ? HIS A 124 . ? 1_555 ? 32 AC7 4 THR A 356 ? THR A 349 . ? 1_555 ? 33 AC7 4 HOH T . ? HOH A 1100 . ? 1_555 ? 34 AC8 5 TYR A 134 ? TYR A 127 . ? 1_555 ? 35 AC8 5 GLU A 144 ? GLU A 137 . ? 1_555 ? 36 AC8 5 ILE A 145 ? ILE A 138 . ? 1_555 ? 37 AC8 5 ASN A 147 ? ASN A 140 . ? 1_555 ? 38 AC8 5 NAG J . ? NAG A 809 . ? 1_555 ? 39 AC9 2 NAG I . ? NAG A 808 . ? 1_555 ? 40 AC9 2 HOH T . ? HOH A 1342 . ? 1_555 ? 41 BC1 2 ASN A 202 ? ASN A 195 . ? 1_555 ? 42 BC1 2 SER A 204 ? SER A 197 . ? 1_555 ? 43 BC2 9 TRP A 253 ? TRP A 246 . ? 1_555 ? 44 BC2 9 ASN A 466 ? ASN A 459 . ? 1_555 ? 45 BC2 9 PHE A 572 ? PHE A 565 . ? 1_555 ? 46 BC2 9 TYR A 573 ? TYR A 566 . ? 1_555 ? 47 BC2 9 HOH T . ? HOH A 978 . ? 1_555 ? 48 BC2 9 HOH T . ? HOH A 1140 . ? 1_555 ? 49 BC2 9 HOH T . ? HOH A 1299 . ? 1_555 ? 50 BC2 9 HOH T . ? HOH A 1322 . ? 1_555 ? 51 BC2 9 HOH T . ? HOH A 1374 . ? 1_555 ? 52 BC3 6 SER A 479 ? SER A 472 . ? 1_555 ? 53 BC3 6 ASN A 483 ? ASN A 476 . ? 1_555 ? 54 BC3 6 PRO A 601 ? PRO A 594 . ? 1_555 ? 55 BC3 6 NAG N . ? NAG A 813 . ? 1_555 ? 56 BC3 6 HOH T . ? HOH A 1406 . ? 1_555 ? 57 BC3 6 HOH T . ? HOH A 1420 . ? 1_555 ? 58 BC4 3 GLN A 658 ? GLN A 651 . ? 1_555 ? 59 BC4 3 NAG M . ? NAG A 812 . ? 1_555 ? 60 BC4 3 HOH T . ? HOH A 1262 . ? 1_555 ? 61 BC5 9 TYR A 284 ? TYR A 277 . ? 2_565 ? 62 BC5 9 SER A 638 ? SER A 631 . ? 1_555 ? 63 BC5 9 SER A 641 ? SER A 634 . ? 1_555 ? 64 BC5 9 ASN A 645 ? ASN A 638 . ? 1_555 ? 65 BC5 9 GLN A 747 ? GLN A 740 . ? 1_555 ? 66 BC5 9 NAG P . ? NAG A 815 . ? 1_555 ? 67 BC5 9 HOH T . ? HOH A 1024 . ? 1_555 ? 68 BC5 9 HOH T . ? HOH A 1057 . ? 2_565 ? 69 BC5 9 HOH T . ? HOH A 1183 . ? 1_555 ? 70 BC6 3 GLU A 283 ? GLU A 276 . ? 2_565 ? 71 BC6 3 NAG O . ? NAG A 814 . ? 1_555 ? 72 BC6 3 BMA Q . ? BMA A 816 . ? 1_555 ? 73 BC7 5 HIS A 119 ? HIS A 112 . ? 2_565 ? 74 BC7 5 GLU A 283 ? GLU A 276 . ? 2_565 ? 75 BC7 5 ARG A 361 ? ARG A 354 . ? 2_565 ? 76 BC7 5 NAG P . ? NAG A 815 . ? 1_555 ? 77 BC7 5 MAN R . ? MAN A 817 . ? 1_555 ? 78 BC8 8 PHE A 242 ? PHE A 235 . ? 7_555 ? 79 BC8 8 LYS A 247 ? LYS A 240 . ? 7_555 ? 80 BC8 8 SER A 248 ? SER A 241 . ? 7_555 ? 81 BC8 8 GLU A 283 ? GLU A 276 . ? 2_565 ? 82 BC8 8 ARG A 361 ? ARG A 354 . ? 2_565 ? 83 BC8 8 BMA Q . ? BMA A 816 . ? 1_555 ? 84 BC8 8 HOH T . ? HOH A 1261 . ? 7_555 ? 85 BC8 8 HOH T . ? HOH A 1277 . ? 1_555 ? 86 BC9 30 LYS A 214 ? LYS A 207 . ? 1_555 ? 87 BC9 30 ARG A 217 ? ARG A 210 . ? 1_555 ? 88 BC9 30 ASN A 264 ? ASN A 257 . ? 1_555 ? 89 BC9 30 ASP A 394 ? ASP A 387 . ? 1_555 ? 90 BC9 30 ALA A 431 ? ALA A 424 . ? 1_555 ? 91 BC9 30 GLU A 432 ? GLU A 425 . ? 1_555 ? 92 BC9 30 GLY A 434 ? GLY A 427 . ? 1_555 ? 93 BC9 30 ARG A 470 ? ARG A 463 . ? 1_555 ? 94 BC9 30 ARG A 518 ? ARG A 511 . ? 1_555 ? 95 BC9 30 GLY A 525 ? GLY A 518 . ? 1_555 ? 96 BC9 30 ASN A 526 ? ASN A 519 . ? 1_555 ? 97 BC9 30 ARG A 541 ? ARG A 534 . ? 1_555 ? 98 BC9 30 ARG A 543 ? ARG A 536 . ? 1_555 ? 99 BC9 30 TRP A 548 ? TRP A 541 . ? 1_555 ? 100 BC9 30 GLU A 549 ? GLU A 542 . ? 1_555 ? 101 BC9 30 TYR A 559 ? TYR A 552 . ? 1_555 ? 102 BC9 30 HIS A 560 ? HIS A 553 . ? 1_555 ? 103 BC9 30 ASN A 705 ? ASN A 698 . ? 1_555 ? 104 BC9 30 LYS A 706 ? LYS A 699 . ? 1_555 ? 105 BC9 30 TYR A 707 ? TYR A 700 . ? 1_555 ? 106 BC9 30 ZN B . ? ZN A 801 . ? 1_555 ? 107 BC9 30 HOH T . ? HOH A 909 . ? 1_555 ? 108 BC9 30 HOH T . ? HOH A 1060 . ? 1_555 ? 109 BC9 30 HOH T . ? HOH A 1067 . ? 1_555 ? 110 BC9 30 HOH T . ? HOH A 1260 . ? 1_555 ? 111 BC9 30 HOH T . ? HOH A 1268 . ? 1_555 ? 112 BC9 30 HOH T . ? HOH A 1276 . ? 1_555 ? 113 BC9 30 HOH T . ? HOH A 1309 . ? 1_555 ? 114 BC9 30 HOH T . ? HOH A 1373 . ? 1_555 ? 115 BC9 30 HOH T . ? HOH A 1415 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MCQ _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 4MCQ _atom_sites.fract_transf_matrix[1][1] 0.009838 _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] 0.007684 _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] 0.006255 _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 . HIS A 1 63 ? 14.990 46.582 80.427 1.00 46.65 ? 56 HIS A N 1 ATOM 2 C CA . HIS A 1 63 ? 14.477 46.794 79.003 1.00 46.17 ? 56 HIS A CA 1 ATOM 3 C C . HIS A 1 63 ? 14.901 48.085 78.315 1.00 44.67 ? 56 HIS A C 1 ATOM 4 O O . HIS A 1 63 ? 14.189 49.114 78.364 1.00 46.12 ? 56 HIS A O 1 ATOM 5 C CB . HIS A 1 63 ? 12.957 46.627 78.902 1.00 46.83 ? 56 HIS A CB 1 ATOM 6 C CG . HIS A 1 63 ? 12.474 45.265 79.291 1.00 49.56 ? 56 HIS A CG 1 ATOM 7 N ND1 . HIS A 1 63 ? 11.325 45.069 80.032 1.00 50.86 ? 56 HIS A ND1 1 ATOM 8 C CD2 . HIS A 1 63 ? 13.007 44.034 79.079 1.00 50.87 ? 56 HIS A CD2 1 ATOM 9 C CE1 . HIS A 1 63 ? 11.163 43.773 80.242 1.00 52.68 ? 56 HIS A CE1 1 ATOM 10 N NE2 . HIS A 1 63 ? 12.168 43.124 79.674 1.00 52.70 ? 56 HIS A NE2 1 ATOM 11 N N . ASN A 1 64 ? 16.040 48.016 77.636 1.00 40.89 ? 57 ASN A N 1 ATOM 12 C CA . ASN A 1 64 ? 16.650 49.171 77.000 1.00 37.06 ? 57 ASN A CA 1 ATOM 13 C C . ASN A 1 64 ? 17.293 48.627 75.732 1.00 35.18 ? 57 ASN A C 1 ATOM 14 O O . ASN A 1 64 ? 17.130 47.445 75.393 1.00 32.07 ? 57 ASN A O 1 ATOM 15 C CB . ASN A 1 64 ? 17.692 49.822 77.933 1.00 36.84 ? 57 ASN A CB 1 ATOM 16 C CG . ASN A 1 64 ? 18.686 48.814 78.516 1.00 36.61 ? 57 ASN A CG 1 ATOM 17 O OD1 . ASN A 1 64 ? 18.843 47.672 78.024 1.00 35.01 ? 57 ASN A OD1 1 ATOM 18 N ND2 . ASN A 1 64 ? 19.375 49.230 79.578 1.00 35.88 ? 57 ASN A ND2 1 ATOM 19 N N . MET A 1 65 ? 17.989 49.481 74.998 1.00 34.09 ? 58 MET A N 1 ATOM 20 C CA . MET A 1 65 ? 18.486 49.001 73.725 1.00 33.43 ? 58 MET A CA 1 ATOM 21 C C . MET A 1 65 ? 19.466 47.828 73.871 1.00 33.08 ? 58 MET A C 1 ATOM 22 O O . MET A 1 65 ? 19.460 46.905 73.044 1.00 32.12 ? 58 MET A O 1 ATOM 23 C CB . MET A 1 65 ? 19.140 50.073 72.921 1.00 33.56 ? 58 MET A CB 1 ATOM 24 C CG . MET A 1 65 ? 19.096 49.595 71.476 1.00 35.40 ? 58 MET A CG 1 ATOM 25 S SD . MET A 1 65 ? 20.100 50.540 70.418 1.00 40.78 ? 58 MET A SD 1 ATOM 26 C CE . MET A 1 65 ? 19.392 52.109 70.594 1.00 41.45 ? 58 MET A CE 1 ATOM 27 N N . LYS A 1 66 ? 20.297 47.882 74.909 1.00 31.90 ? 59 LYS A N 1 ATOM 28 C CA . LYS A 1 66 ? 21.268 46.830 75.147 1.00 32.22 ? 59 LYS A CA 1 ATOM 29 C C . LYS A 1 66 ? 20.612 45.455 75.355 1.00 32.18 ? 59 LYS A C 1 ATOM 30 O O . LYS A 1 66 ? 21.140 44.445 74.873 1.00 32.23 ? 59 LYS A O 1 ATOM 31 C CB . LYS A 1 66 ? 22.172 47.163 76.338 1.00 31.86 ? 59 LYS A CB 1 ATOM 32 C CG . LYS A 1 66 ? 23.231 46.056 76.623 1.00 32.29 ? 59 LYS A CG 1 ATOM 33 C CD . LYS A 1 66 ? 24.143 46.468 77.789 0.10 30.99 ? 59 LYS A CD 1 ATOM 34 C CE . LYS A 1 66 ? 25.465 45.688 77.811 0.20 30.16 ? 59 LYS A CE 1 ATOM 35 N NZ . LYS A 1 66 ? 25.289 44.245 78.111 0.20 27.83 ? 59 LYS A NZ 1 ATOM 36 N N . ALA A 1 67 ? 19.486 45.408 76.083 1.00 31.92 ? 60 ALA A N 1 ATOM 37 C CA . ALA A 1 67 ? 18.725 44.137 76.224 1.00 31.28 ? 60 ALA A CA 1 ATOM 38 C C . ALA A 1 67 ? 18.275 43.657 74.836 1.00 30.14 ? 60 ALA A C 1 ATOM 39 O O . ALA A 1 67 ? 18.430 42.484 74.484 1.00 29.49 ? 60 ALA A O 1 ATOM 40 C CB . ALA A 1 67 ? 17.507 44.286 77.181 1.00 31.37 ? 60 ALA A CB 1 ATOM 41 N N . PHE A 1 68 ? 17.758 44.584 74.037 1.00 29.01 ? 61 PHE A N 1 ATOM 42 C CA . PHE A 1 68 ? 17.357 44.228 72.668 1.00 28.15 ? 61 PHE A CA 1 ATOM 43 C C . PHE A 1 68 ? 18.543 43.664 71.829 1.00 28.07 ? 61 PHE A C 1 ATOM 44 O O . PHE A 1 68 ? 18.431 42.588 71.207 1.00 27.94 ? 61 PHE A O 1 ATOM 45 C CB . PHE A 1 68 ? 16.701 45.418 71.933 1.00 27.38 ? 61 PHE A CB 1 ATOM 46 C CG . PHE A 1 68 ? 16.629 45.206 70.452 1.00 26.41 ? 61 PHE A CG 1 ATOM 47 C CD1 . PHE A 1 68 ? 15.689 44.309 69.902 1.00 25.16 ? 61 PHE A CD1 1 ATOM 48 C CD2 . PHE A 1 68 ? 17.554 45.824 69.602 1.00 25.96 ? 61 PHE A CD2 1 ATOM 49 C CE1 . PHE A 1 68 ? 15.674 44.049 68.519 1.00 24.37 ? 61 PHE A CE1 1 ATOM 50 C CE2 . PHE A 1 68 ? 17.553 45.565 68.222 1.00 24.91 ? 61 PHE A CE2 1 ATOM 51 C CZ . PHE A 1 68 ? 16.609 44.676 67.674 1.00 24.11 ? 61 PHE A CZ 1 ATOM 52 N N . LEU A 1 69 ? 19.660 44.400 71.798 1.00 27.87 ? 62 LEU A N 1 ATOM 53 C CA . LEU A 1 69 ? 20.843 43.994 71.029 1.00 28.63 ? 62 LEU A CA 1 ATOM 54 C C . LEU A 1 69 ? 21.403 42.659 71.516 1.00 29.19 ? 62 LEU A C 1 ATOM 55 O O . LEU A 1 69 ? 21.840 41.822 70.714 1.00 28.46 ? 62 LEU A O 1 ATOM 56 C CB . LEU A 1 69 ? 21.910 45.092 71.100 1.00 28.66 ? 62 LEU A CB 1 ATOM 57 C CG . LEU A 1 69 ? 21.482 46.415 70.451 1.00 28.56 ? 62 LEU A CG 1 ATOM 58 C CD1 . LEU A 1 69 ? 22.462 47.526 70.832 1.00 27.46 ? 62 LEU A CD1 1 ATOM 59 C CD2 . LEU A 1 69 ? 21.327 46.292 68.900 1.00 27.07 ? 62 LEU A CD2 1 ATOM 60 N N . ASP A 1 70 ? 21.383 42.446 72.832 1.00 30.34 ? 63 ASP A N 1 ATOM 61 C CA . ASP A 1 70 ? 22.034 41.250 73.398 1.00 31.81 ? 63 ASP A CA 1 ATOM 62 C C . ASP A 1 70 ? 21.247 39.985 73.069 1.00 31.17 ? 63 ASP A C 1 ATOM 63 O O . ASP A 1 70 ? 21.810 38.902 73.052 1.00 30.86 ? 63 ASP A O 1 ATOM 64 C CB . ASP A 1 70 ? 22.218 41.358 74.942 1.00 31.96 ? 63 ASP A CB 1 ATOM 65 C CG . ASP A 1 70 ? 23.387 42.270 75.341 1.00 34.90 ? 63 ASP A CG 1 ATOM 66 O OD1 . ASP A 1 70 ? 24.234 42.627 74.491 1.00 38.03 ? 63 ASP A OD1 1 ATOM 67 O OD2 . ASP A 1 70 ? 23.456 42.661 76.514 1.00 37.77 ? 63 ASP A OD2 1 ATOM 68 N N . GLU A 1 71 ? 19.944 40.128 72.852 1.00 30.95 ? 64 GLU A N 1 ATOM 69 C CA . GLU A 1 71 ? 19.088 38.988 72.562 1.00 30.62 ? 64 GLU A CA 1 ATOM 70 C C . GLU A 1 71 ? 19.331 38.429 71.133 1.00 29.54 ? 64 GLU A C 1 ATOM 71 O O . GLU A 1 71 ? 19.109 37.230 70.882 1.00 29.07 ? 64 GLU A O 1 ATOM 72 C CB . GLU A 1 71 ? 17.612 39.376 72.762 1.00 30.93 ? 64 GLU A CB 1 ATOM 73 C CG . GLU A 1 71 ? 16.588 38.255 72.481 1.00 31.22 ? 64 GLU A CG 1 ATOM 74 C CD . GLU A 1 71 ? 16.835 36.985 73.340 1.00 33.90 ? 64 GLU A CD 1 ATOM 75 O OE1 . GLU A 1 71 ? 17.170 37.118 74.532 1.00 33.82 ? 64 GLU A OE1 1 ATOM 76 O OE2 . GLU A 1 71 ? 16.689 35.854 72.820 1.00 34.56 ? 64 GLU A OE2 1 ATOM 77 N N . LEU A 1 72 ? 19.786 39.288 70.218 1.00 28.43 ? 65 LEU A N 1 ATOM 78 C CA . LEU A 1 72 ? 20.114 38.867 68.820 1.00 27.49 ? 65 LEU A CA 1 ATOM 79 C C . LEU A 1 72 ? 21.256 37.858 68.784 1.00 27.73 ? 65 LEU A C 1 ATOM 80 O O . LEU A 1 72 ? 22.286 38.105 69.396 1.00 27.29 ? 65 LEU A O 1 ATOM 81 C CB . LEU A 1 72 ? 20.511 40.070 67.940 1.00 26.46 ? 65 LEU A CB 1 ATOM 82 C CG . LEU A 1 72 ? 19.539 41.242 67.830 1.00 25.04 ? 65 LEU A CG 1 ATOM 83 C CD1 . LEU A 1 72 ? 20.236 42.484 67.261 1.00 24.37 ? 65 LEU A CD1 1 ATOM 84 C CD2 . LEU A 1 72 ? 18.283 40.854 66.992 1.00 22.68 ? 65 LEU A CD2 1 ATOM 85 N N . LYS A 1 73 ? 21.110 36.770 68.014 1.00 27.49 ? 66 LYS A N 1 ATOM 86 C CA . LYS A 1 73 ? 22.147 35.736 67.968 1.00 28.09 ? 66 LYS A CA 1 ATOM 87 C C . LYS A 1 73 ? 22.547 35.393 66.543 1.00 27.18 ? 66 LYS A C 1 ATOM 88 O O . LYS A 1 73 ? 21.681 35.148 65.708 1.00 25.78 ? 66 LYS A O 1 ATOM 89 C CB . LYS A 1 73 ? 21.651 34.445 68.649 1.00 28.56 ? 66 LYS A CB 1 ATOM 90 C CG . LYS A 1 73 ? 21.108 34.623 70.104 1.00 33.54 ? 66 LYS A CG 1 ATOM 91 C CD . LYS A 1 73 ? 22.246 34.702 71.072 1.00 38.14 ? 66 LYS A CD 1 ATOM 92 C CE . LYS A 1 73 ? 21.799 34.653 72.579 1.00 41.66 ? 66 LYS A CE 1 ATOM 93 N NZ . LYS A 1 73 ? 21.244 35.935 73.043 1.00 42.05 ? 66 LYS A NZ 1 ATOM 94 N N . ALA A 1 74 ? 23.851 35.339 66.277 1.00 27.49 ? 67 ALA A N 1 ATOM 95 C CA . ALA A 1 74 ? 24.364 34.924 64.964 1.00 27.10 ? 67 ALA A CA 1 ATOM 96 C C . ALA A 1 74 ? 23.834 33.531 64.628 1.00 27.72 ? 67 ALA A C 1 ATOM 97 O O . ALA A 1 74 ? 23.473 33.278 63.480 1.00 26.63 ? 67 ALA A O 1 ATOM 98 C CB . ALA A 1 74 ? 25.917 34.876 64.956 1.00 27.95 ? 67 ALA A CB 1 ATOM 99 N N . GLU A 1 75 ? 23.830 32.619 65.606 1.00 28.04 ? 68 GLU A N 1 ATOM 100 C CA . GLU A 1 75 ? 23.384 31.246 65.318 1.00 29.17 ? 68 GLU A CA 1 ATOM 101 C C . GLU A 1 75 ? 21.921 31.191 64.856 1.00 28.16 ? 68 GLU A C 1 ATOM 102 O O . GLU A 1 75 ? 21.578 30.346 64.017 1.00 27.87 ? 68 GLU A O 1 ATOM 103 C CB . GLU A 1 75 ? 23.602 30.304 66.514 1.00 30.49 ? 68 GLU A CB 1 ATOM 104 C CG . GLU A 1 75 ? 23.346 28.821 66.172 1.00 34.40 ? 68 GLU A CG 1 ATOM 105 C CD . GLU A 1 75 ? 24.601 28.048 65.738 0.80 39.19 ? 68 GLU A CD 1 ATOM 106 O OE1 . GLU A 1 75 ? 25.097 28.274 64.602 0.75 41.21 ? 68 GLU A OE1 1 ATOM 107 O OE2 . GLU A 1 75 ? 25.078 27.200 66.525 0.20 38.55 ? 68 GLU A OE2 1 ATOM 108 N N . ASN A 1 76 ? 21.064 32.083 65.377 1.00 27.00 ? 69 ASN A N 1 ATOM 109 C CA . ASN A 1 76 ? 19.651 32.125 64.929 1.00 26.37 ? 69 ASN A CA 1 ATOM 110 C C . ASN A 1 76 ? 19.541 32.606 63.493 1.00 25.26 ? 69 ASN A C 1 ATOM 111 O O . ASN A 1 76 ? 18.830 32.009 62.680 1.00 25.78 ? 69 ASN A O 1 ATOM 112 C CB . ASN A 1 76 ? 18.773 33.009 65.846 1.00 26.57 ? 69 ASN A CB 1 ATOM 113 C CG . ASN A 1 76 ? 18.533 32.370 67.225 1.00 27.46 ? 69 ASN A CG 1 ATOM 114 O OD1 . ASN A 1 76 ? 18.527 31.155 67.358 1.00 26.97 ? 69 ASN A OD1 1 ATOM 115 N ND2 . ASN A 1 76 ? 18.347 33.203 68.249 1.00 26.45 ? 69 ASN A ND2 1 ATOM 116 N N . ILE A 1 77 ? 20.255 33.680 63.168 1.00 24.51 ? 70 ILE A N 1 ATOM 117 C CA . ILE A 1 77 ? 20.271 34.190 61.788 1.00 23.50 ? 70 ILE A CA 1 ATOM 118 C C . ILE A 1 77 ? 20.731 33.079 60.823 1.00 23.89 ? 70 ILE A C 1 ATOM 119 O O . ILE A 1 77 ? 20.130 32.886 59.782 1.00 22.56 ? 70 ILE A O 1 ATOM 120 C CB . ILE A 1 77 ? 21.164 35.465 61.642 1.00 23.89 ? 70 ILE A CB 1 ATOM 121 C CG1 . ILE A 1 77 ? 20.676 36.589 62.581 1.00 23.04 ? 70 ILE A CG1 1 ATOM 122 C CG2 . ILE A 1 77 ? 21.178 35.959 60.147 1.00 22.71 ? 70 ILE A CG2 1 ATOM 123 C CD1 . ILE A 1 77 ? 21.736 37.733 62.846 1.00 23.98 ? 70 ILE A CD1 1 ATOM 124 N N . LYS A 1 78 ? 21.783 32.333 61.196 1.00 24.07 ? 71 LYS A N 1 ATOM 125 C CA . LYS A 1 78 ? 22.279 31.234 60.365 1.00 24.00 ? 71 LYS A CA 1 ATOM 126 C C . LYS A 1 78 ? 21.170 30.209 60.129 1.00 24.82 ? 71 LYS A C 1 ATOM 127 O O . LYS A 1 78 ? 20.901 29.821 58.989 1.00 25.34 ? 71 LYS A O 1 ATOM 128 C CB . LYS A 1 78 ? 23.476 30.537 61.066 1.00 24.37 ? 71 LYS A CB 1 ATOM 129 C CG . LYS A 1 78 ? 24.033 29.274 60.316 1.00 25.64 ? 71 LYS A CG 1 ATOM 130 C CD . LYS A 1 78 ? 25.333 28.780 60.981 1.00 27.56 ? 71 LYS A CD 1 ATOM 131 C CE . LYS A 1 78 ? 25.879 27.520 60.329 1.00 31.48 ? 71 LYS A CE 1 ATOM 132 N NZ . LYS A 1 78 ? 27.002 27.031 61.165 1.00 30.73 ? 71 LYS A NZ 1 ATOM 133 N N . LYS A 1 79 ? 20.561 29.731 61.218 1.00 25.20 ? 72 LYS A N 1 ATOM 134 C CA . LYS A 1 79 ? 19.409 28.794 61.144 1.00 25.88 ? 72 LYS A CA 1 ATOM 135 C C . LYS A 1 79 ? 18.263 29.277 60.213 1.00 24.28 ? 72 LYS A C 1 ATOM 136 O O . LYS A 1 79 ? 17.734 28.500 59.414 1.00 23.00 ? 72 LYS A O 1 ATOM 137 C CB . LYS A 1 79 ? 18.839 28.490 62.542 1.00 25.43 ? 72 LYS A CB 1 ATOM 138 C CG . LYS A 1 79 ? 19.762 27.562 63.353 0.95 28.29 ? 72 LYS A CG 1 ATOM 139 C CD . LYS A 1 79 ? 19.382 27.470 64.835 0.35 26.39 ? 72 LYS A CD 1 ATOM 140 C CE . LYS A 1 79 ? 20.337 26.514 65.549 0.15 26.18 ? 72 LYS A CE 1 ATOM 141 N NZ . LYS A 1 79 ? 19.866 26.185 66.916 0.20 25.39 ? 72 LYS A NZ 1 ATOM 142 N N . PHE A 1 80 ? 17.894 30.547 60.343 1.00 23.46 ? 73 PHE A N 1 ATOM 143 C CA . PHE A 1 80 ? 16.849 31.111 59.513 1.00 22.95 ? 73 PHE A CA 1 ATOM 144 C C . PHE A 1 80 ? 17.278 31.180 58.038 1.00 22.89 ? 73 PHE A C 1 ATOM 145 O O . PHE A 1 80 ? 16.489 30.855 57.133 1.00 22.50 ? 73 PHE A O 1 ATOM 146 C CB . PHE A 1 80 ? 16.431 32.508 60.006 1.00 22.49 ? 73 PHE A CB 1 ATOM 147 C CG . PHE A 1 80 ? 15.858 32.522 61.399 1.00 23.57 ? 73 PHE A CG 1 ATOM 148 C CD1 . PHE A 1 80 ? 15.213 31.398 61.932 1.00 24.49 ? 73 PHE A CD1 1 ATOM 149 C CD2 . PHE A 1 80 ? 15.947 33.690 62.185 1.00 23.96 ? 73 PHE A CD2 1 ATOM 150 C CE1 . PHE A 1 80 ? 14.686 31.433 63.247 1.00 25.51 ? 73 PHE A CE1 1 ATOM 151 C CE2 . PHE A 1 80 ? 15.427 33.750 63.473 1.00 22.63 ? 73 PHE A CE2 1 ATOM 152 C CZ . PHE A 1 80 ? 14.792 32.631 64.011 1.00 24.90 ? 73 PHE A CZ 1 ATOM 153 N N . LEU A 1 81 ? 18.514 31.601 57.795 1.00 21.84 ? 74 LEU A N 1 ATOM 154 C CA . LEU A 1 81 ? 18.992 31.683 56.429 1.00 21.21 ? 74 LEU A CA 1 ATOM 155 C C . LEU A 1 81 ? 18.957 30.303 55.781 1.00 21.71 ? 74 LEU A C 1 ATOM 156 O O . LEU A 1 81 ? 18.447 30.149 54.667 1.00 21.42 ? 74 LEU A O 1 ATOM 157 C CB . LEU A 1 81 ? 20.409 32.270 56.375 1.00 21.15 ? 74 LEU A CB 1 ATOM 158 C CG . LEU A 1 81 ? 20.927 32.373 54.937 1.00 19.16 ? 74 LEU A CG 1 ATOM 159 C CD1 . LEU A 1 81 ? 20.063 33.375 54.164 1.00 17.19 ? 74 LEU A CD1 1 ATOM 160 C CD2 . LEU A 1 81 ? 22.396 32.756 54.829 1.00 18.20 ? 74 LEU A CD2 1 ATOM 161 N N . TYR A 1 82 ? 19.461 29.282 56.486 1.00 21.90 ? 75 TYR A N 1 ATOM 162 C CA . TYR A 1 82 ? 19.384 27.919 55.966 1.00 23.07 ? 75 TYR A CA 1 ATOM 163 C C . TYR A 1 82 ? 17.910 27.566 55.631 1.00 23.18 ? 75 TYR A C 1 ATOM 164 O O . TYR A 1 82 ? 17.602 27.029 54.568 1.00 23.98 ? 75 TYR A O 1 ATOM 165 C CB . TYR A 1 82 ? 19.917 26.914 56.989 1.00 23.20 ? 75 TYR A CB 1 ATOM 166 C CG . TYR A 1 82 ? 19.877 25.507 56.451 1.00 24.20 ? 75 TYR A CG 1 ATOM 167 C CD1 . TYR A 1 82 ? 20.917 25.028 55.667 1.00 25.83 ? 75 TYR A CD1 1 ATOM 168 C CD2 . TYR A 1 82 ? 18.791 24.656 56.721 1.00 26.66 ? 75 TYR A CD2 1 ATOM 169 C CE1 . TYR A 1 82 ? 20.895 23.745 55.145 1.00 28.19 ? 75 TYR A CE1 1 ATOM 170 C CE2 . TYR A 1 82 ? 18.749 23.325 56.191 1.00 29.92 ? 75 TYR A CE2 1 ATOM 171 C CZ . TYR A 1 82 ? 19.823 22.893 55.414 1.00 31.03 ? 75 TYR A CZ 1 ATOM 172 O OH . TYR A 1 82 ? 19.858 21.607 54.887 1.00 35.31 ? 75 TYR A OH 1 ATOM 173 N N . ASN A 1 83 ? 17.014 27.870 56.565 1.00 22.85 ? 76 ASN A N 1 ATOM 174 C CA . ASN A 1 83 ? 15.604 27.566 56.424 1.00 22.88 ? 76 ASN A CA 1 ATOM 175 C C . ASN A 1 83 ? 14.925 28.235 55.200 1.00 22.31 ? 76 ASN A C 1 ATOM 176 O O . ASN A 1 83 ? 14.014 27.644 54.581 1.00 22.68 ? 76 ASN A O 1 ATOM 177 C CB . ASN A 1 83 ? 14.888 27.984 57.701 1.00 23.88 ? 76 ASN A CB 1 ATOM 178 C CG . ASN A 1 83 ? 13.414 27.660 57.681 1.00 25.35 ? 76 ASN A CG 1 ATOM 179 O OD1 . ASN A 1 83 ? 12.586 28.505 57.329 1.00 25.00 ? 76 ASN A OD1 1 ATOM 180 N ND2 . ASN A 1 83 ? 13.078 26.430 58.048 1.00 27.45 ? 76 ASN A ND2 1 ATOM 181 N N . PHE A 1 84 ? 15.390 29.436 54.857 1.00 20.41 ? 77 PHE A N 1 ATOM 182 C CA . PHE A 1 84 ? 14.755 30.270 53.829 1.00 20.11 ? 77 PHE A CA 1 ATOM 183 C C . PHE A 1 84 ? 15.313 30.005 52.421 1.00 20.25 ? 77 PHE A C 1 ATOM 184 O O . PHE A 1 84 ? 14.824 30.609 51.436 1.00 19.50 ? 77 PHE A O 1 ATOM 185 C CB . PHE A 1 84 ? 14.988 31.764 54.132 1.00 19.68 ? 77 PHE A CB 1 ATOM 186 C CG . PHE A 1 84 ? 14.271 32.307 55.343 1.00 20.66 ? 77 PHE A CG 1 ATOM 187 C CD1 . PHE A 1 84 ? 13.324 31.548 56.061 1.00 20.29 ? 77 PHE A CD1 1 ATOM 188 C CD2 . PHE A 1 84 ? 14.542 33.632 55.762 1.00 20.46 ? 77 PHE A CD2 1 ATOM 189 C CE1 . PHE A 1 84 ? 12.661 32.112 57.179 1.00 21.79 ? 77 PHE A CE1 1 ATOM 190 C CE2 . PHE A 1 84 ? 13.886 34.195 56.855 1.00 21.57 ? 77 PHE A CE2 1 ATOM 191 C CZ . PHE A 1 84 ? 12.943 33.437 57.576 1.00 21.12 ? 77 PHE A CZ 1 ATOM 192 N N . THR A 1 85 ? 16.325 29.134 52.308 1.00 19.86 ? 78 THR A N 1 ATOM 193 C CA . THR A 1 85 ? 17.067 29.019 51.050 1.00 21.14 ? 78 THR A CA 1 ATOM 194 C C . THR A 1 85 ? 17.186 27.598 50.469 1.00 22.25 ? 78 THR A C 1 ATOM 195 O O . THR A 1 85 ? 18.002 27.374 49.539 1.00 22.48 ? 78 THR A O 1 ATOM 196 C CB . THR A 1 85 ? 18.485 29.592 51.216 1.00 20.71 ? 78 THR A CB 1 ATOM 197 O OG1 . THR A 1 85 ? 19.134 28.887 52.268 1.00 19.77 ? 78 THR A OG1 1 ATOM 198 C CG2 . THR A 1 85 ? 18.383 31.077 51.577 1.00 17.19 ? 78 THR A CG2 1 ATOM 199 N N . GLN A 1 86 ? 16.366 26.669 50.971 1.00 23.10 ? 79 GLN A N 1 ATOM 200 C CA . GLN A 1 86 ? 16.440 25.261 50.510 1.00 25.31 ? 79 GLN A CA 1 ATOM 201 C C . GLN A 1 86 ? 15.749 25.052 49.164 1.00 25.43 ? 79 GLN A C 1 ATOM 202 O O . GLN A 1 86 ? 16.097 24.125 48.420 1.00 25.27 ? 79 GLN A O 1 ATOM 203 C CB . GLN A 1 86 ? 15.874 24.255 51.565 1.00 25.80 ? 79 GLN A CB 1 ATOM 204 C CG . GLN A 1 86 ? 16.693 24.219 52.853 1.00 27.72 ? 79 GLN A CG 1 ATOM 205 C CD . GLN A 1 86 ? 18.168 24.257 52.530 1.00 31.50 ? 79 GLN A CD 1 ATOM 206 O OE1 . GLN A 1 86 ? 18.689 23.289 51.981 1.00 33.27 ? 79 GLN A OE1 1 ATOM 207 N NE2 . GLN A 1 86 ? 18.845 25.401 52.797 1.00 31.16 ? 79 GLN A NE2 1 ATOM 208 N N . ILE A 1 87 ? 14.750 25.890 48.874 1.00 25.37 ? 80 ILE A N 1 ATOM 209 C CA . ILE A 1 87 ? 14.004 25.791 47.622 1.00 25.78 ? 80 ILE A CA 1 ATOM 210 C C . ILE A 1 87 ? 13.813 27.194 47.066 1.00 24.24 ? 80 ILE A C 1 ATOM 211 O O . ILE A 1 87 ? 13.907 28.168 47.840 1.00 24.76 ? 80 ILE A O 1 ATOM 212 C CB . ILE A 1 87 ? 12.612 25.124 47.821 1.00 26.03 ? 80 ILE A CB 1 ATOM 213 C CG1 . ILE A 1 87 ? 11.694 26.009 48.670 1.00 27.32 ? 80 ILE A CG1 1 ATOM 214 C CG2 . ILE A 1 87 ? 12.744 23.645 48.361 1.00 28.57 ? 80 ILE A CG2 1 ATOM 215 C CD1 . ILE A 1 87 ? 10.266 25.403 48.857 1.00 30.52 ? 80 ILE A CD1 1 ATOM 216 N N . PRO A 1 88 ? 13.541 27.311 45.747 1.00 23.15 ? 81 PRO A N 1 ATOM 217 C CA . PRO A 1 88 ? 13.303 28.649 45.168 1.00 22.51 ? 81 PRO A CA 1 ATOM 218 C C . PRO A 1 88 ? 12.045 29.303 45.715 1.00 22.22 ? 81 PRO A C 1 ATOM 219 O O . PRO A 1 88 ? 11.066 28.579 46.050 1.00 22.90 ? 81 PRO A O 1 ATOM 220 C CB . PRO A 1 88 ? 13.110 28.364 43.679 1.00 22.68 ? 81 PRO A CB 1 ATOM 221 C CG . PRO A 1 88 ? 13.845 27.044 43.446 1.00 22.73 ? 81 PRO A CG 1 ATOM 222 C CD . PRO A 1 88 ? 13.598 26.254 44.703 1.00 22.91 ? 81 PRO A CD 1 ATOM 223 N N . HIS A 1 89 ? 12.054 30.636 45.810 1.00 19.31 ? 82 HIS A N 1 ATOM 224 C CA . HIS A 1 89 ? 10.856 31.334 46.280 1.00 19.99 ? 82 HIS A CA 1 ATOM 225 C C . HIS A 1 89 ? 10.493 32.456 45.311 1.00 18.71 ? 82 HIS A C 1 ATOM 226 O O . HIS A 1 89 ? 10.427 33.645 45.705 1.00 17.95 ? 82 HIS A O 1 ATOM 227 C CB . HIS A 1 89 ? 11.053 31.883 47.722 1.00 19.95 ? 82 HIS A CB 1 ATOM 228 C CG . HIS A 1 89 ? 11.184 30.801 48.751 1.00 21.23 ? 82 HIS A CG 1 ATOM 229 N ND1 . HIS A 1 89 ? 12.400 30.433 49.296 1.00 19.59 ? 82 HIS A ND1 1 ATOM 230 C CD2 . HIS A 1 89 ? 10.253 29.966 49.288 1.00 20.80 ? 82 HIS A CD2 1 ATOM 231 C CE1 . HIS A 1 89 ? 12.203 29.433 50.142 1.00 21.79 ? 82 HIS A CE1 1 ATOM 232 N NE2 . HIS A 1 89 ? 10.910 29.128 50.150 1.00 20.25 ? 82 HIS A NE2 1 ATOM 233 N N . LEU A 1 90 ? 10.281 32.073 44.055 1.00 17.49 ? 83 LEU A N 1 ATOM 234 C CA . LEU A 1 90 ? 9.990 33.034 43.000 1.00 18.62 ? 83 LEU A CA 1 ATOM 235 C C . LEU A 1 90 ? 8.653 33.711 43.289 1.00 18.36 ? 83 LEU A C 1 ATOM 236 O O . LEU A 1 90 ? 7.694 33.025 43.677 1.00 19.07 ? 83 LEU A O 1 ATOM 237 C CB . LEU A 1 90 ? 9.952 32.311 41.623 1.00 17.22 ? 83 LEU A CB 1 ATOM 238 C CG . LEU A 1 90 ? 9.850 33.232 40.377 1.00 18.29 ? 83 LEU A CG 1 ATOM 239 C CD1 . LEU A 1 90 ? 11.092 34.140 40.209 1.00 15.60 ? 83 LEU A CD1 1 ATOM 240 C CD2 . LEU A 1 90 ? 9.689 32.239 39.093 1.00 16.91 ? 83 LEU A CD2 1 ATOM 241 N N . ALA A 1 91 ? 8.567 35.037 43.113 1.00 17.92 ? 84 ALA A N 1 ATOM 242 C CA . ALA A 1 91 ? 7.280 35.703 43.278 1.00 17.68 ? 84 ALA A CA 1 ATOM 243 C C . ALA A 1 91 ? 6.148 35.067 42.444 1.00 18.90 ? 84 ALA A C 1 ATOM 244 O O . ALA A 1 91 ? 6.345 34.712 41.265 1.00 18.80 ? 84 ALA A O 1 ATOM 245 C CB . ALA A 1 91 ? 7.383 37.185 42.923 1.00 16.67 ? 84 ALA A CB 1 ATOM 246 N N . GLY A 1 92 ? 4.973 34.956 43.077 1.00 19.26 ? 85 GLY A N 1 ATOM 247 C CA . GLY A 1 92 ? 3.758 34.447 42.462 1.00 19.74 ? 85 GLY A CA 1 ATOM 248 C C . GLY A 1 92 ? 3.709 32.931 42.410 1.00 21.89 ? 85 GLY A C 1 ATOM 249 O O . GLY A 1 92 ? 2.755 32.362 41.863 1.00 23.20 ? 85 GLY A O 1 ATOM 250 N N . THR A 1 93 ? 4.710 32.255 42.963 1.00 21.01 ? 86 THR A N 1 ATOM 251 C CA . THR A 1 93 ? 4.671 30.800 42.990 1.00 21.39 ? 86 THR A CA 1 ATOM 252 C C . THR A 1 93 ? 4.154 30.261 44.334 1.00 21.46 ? 86 THR A C 1 ATOM 253 O O . THR A 1 93 ? 4.202 30.938 45.358 1.00 20.14 ? 86 THR A O 1 ATOM 254 C CB . THR A 1 93 ? 6.089 30.124 42.705 1.00 21.87 ? 86 THR A CB 1 ATOM 255 O OG1 . THR A 1 93 ? 7.015 30.425 43.772 1.00 21.20 ? 86 THR A OG1 1 ATOM 256 C CG2 . THR A 1 93 ? 6.666 30.556 41.332 1.00 20.56 ? 86 THR A CG2 1 ATOM 257 N N . GLU A 1 94 ? 3.720 29.006 44.329 1.00 21.74 ? 87 GLU A N 1 ATOM 258 C CA . GLU A 1 94 ? 3.172 28.387 45.514 1.00 23.77 ? 87 GLU A CA 1 ATOM 259 C C . GLU A 1 94 ? 4.189 28.303 46.691 1.00 23.71 ? 87 GLU A C 1 ATOM 260 O O . GLU A 1 94 ? 3.836 28.516 47.858 1.00 24.31 ? 87 GLU A O 1 ATOM 261 C CB . GLU A 1 94 ? 2.593 26.996 45.151 1.00 24.80 ? 87 GLU A CB 1 ATOM 262 C CG . GLU A 1 94 ? 2.160 26.183 46.360 1.00 30.60 ? 87 GLU A CG 1 ATOM 263 C CD . GLU A 1 94 ? 0.878 26.691 47.047 0.75 34.91 ? 87 GLU A CD 1 ATOM 264 O OE1 . GLU A 1 94 ? 0.628 26.268 48.202 0.75 38.35 ? 87 GLU A OE1 1 ATOM 265 O OE2 . GLU A 1 94 ? 0.123 27.501 46.451 0.75 37.09 ? 87 GLU A OE2 1 ATOM 266 N N . GLN A 1 95 ? 5.440 27.975 46.383 1.00 23.12 ? 88 GLN A N 1 ATOM 267 C CA A GLN A 1 95 ? 6.528 27.943 47.343 0.50 23.02 ? 88 GLN A CA 1 ATOM 268 C CA C GLN A 1 95 ? 6.437 27.926 47.434 0.50 23.29 ? 88 GLN A CA 1 ATOM 269 C C . GLN A 1 95 ? 6.651 29.287 48.092 1.00 22.97 ? 88 GLN A C 1 ATOM 270 O O . GLN A 1 95 ? 6.896 29.336 49.304 1.00 21.76 ? 88 GLN A O 1 ATOM 271 C CB A GLN A 1 95 ? 7.836 27.607 46.601 0.50 23.05 ? 88 GLN A CB 1 ATOM 272 C CB C GLN A 1 95 ? 7.748 27.346 46.932 0.50 23.81 ? 88 GLN A CB 1 ATOM 273 C CG A GLN A 1 95 ? 7.780 26.263 45.822 0.50 23.44 ? 88 GLN A CG 1 ATOM 274 C CG C GLN A 1 95 ? 7.613 25.900 46.519 0.50 25.04 ? 88 GLN A CG 1 ATOM 275 C CD A GLN A 1 95 ? 7.496 26.415 44.314 0.50 23.47 ? 88 GLN A CD 1 ATOM 276 C CD C GLN A 1 95 ? 8.358 25.648 45.240 0.50 28.06 ? 88 GLN A CD 1 ATOM 277 O OE1 A GLN A 1 95 ? 6.510 26.989 43.924 0.50 17.45 ? 88 GLN A OE1 1 ATOM 278 O OE1 C GLN A 1 95 ? 9.456 26.221 45.008 0.50 27.29 ? 88 GLN A OE1 1 ATOM 279 N NE2 A GLN A 1 95 ? 8.385 25.843 43.465 0.50 28.19 ? 88 GLN A NE2 1 ATOM 280 N NE2 C GLN A 1 95 ? 7.763 24.809 44.362 0.50 29.37 ? 88 GLN A NE2 1 ATOM 281 N N . ASN A 1 96 ? 6.500 30.388 47.347 1.00 21.50 ? 89 ASN A N 1 ATOM 282 C CA . ASN A 1 96 ? 6.636 31.685 47.999 1.00 21.23 ? 89 ASN A CA 1 ATOM 283 C C . ASN A 1 96 ? 5.391 32.056 48.831 1.00 21.88 ? 89 ASN A C 1 ATOM 284 O O . ASN A 1 96 ? 5.501 32.808 49.817 1.00 21.97 ? 89 ASN A O 1 ATOM 285 C CB . ASN A 1 96 ? 6.954 32.822 47.012 1.00 20.71 ? 89 ASN A CB 1 ATOM 286 C CG . ASN A 1 96 ? 7.556 34.050 47.716 1.00 21.16 ? 89 ASN A CG 1 ATOM 287 O OD1 . ASN A 1 96 ? 8.324 33.908 48.676 1.00 20.91 ? 89 ASN A OD1 1 ATOM 288 N ND2 . ASN A 1 96 ? 7.224 35.253 47.235 1.00 19.38 ? 89 ASN A ND2 1 ATOM 289 N N . PHE A 1 97 ? 4.202 31.615 48.394 1.00 21.04 ? 90 PHE A N 1 ATOM 290 C CA . PHE A 1 97 ? 3.015 31.718 49.251 1.00 21.67 ? 90 PHE A CA 1 ATOM 291 C C . PHE A 1 97 ? 3.223 30.870 50.534 1.00 22.13 ? 90 PHE A C 1 ATOM 292 O O . PHE A 1 97 ? 2.960 31.359 51.654 1.00 20.29 ? 90 PHE A O 1 ATOM 293 C CB A PHE A 1 97 ? 1.762 31.290 48.449 0.65 22.73 ? 90 PHE A CB 1 ATOM 294 C CB B PHE A 1 97 ? 1.737 31.271 48.541 0.35 21.77 ? 90 PHE A CB 1 ATOM 295 C CG A PHE A 1 97 ? 0.460 31.270 49.240 0.65 24.04 ? 90 PHE A CG 1 ATOM 296 C CG B PHE A 1 97 ? 0.585 31.020 49.483 0.35 21.15 ? 90 PHE A CG 1 ATOM 297 C CD1 A PHE A 1 97 ? 0.087 32.345 50.068 0.65 24.57 ? 90 PHE A CD1 1 ATOM 298 C CD1 B PHE A 1 97 ? -0.156 32.082 49.992 0.35 21.00 ? 90 PHE A CD1 1 ATOM 299 C CD2 A PHE A 1 97 ? -0.421 30.188 49.100 0.65 27.23 ? 90 PHE A CD2 1 ATOM 300 C CD2 B PHE A 1 97 ? 0.266 29.726 49.880 0.35 20.43 ? 90 PHE A CD2 1 ATOM 301 C CE1 A PHE A 1 97 ? -1.137 32.349 50.774 0.65 24.68 ? 90 PHE A CE1 1 ATOM 302 C CE1 B PHE A 1 97 ? -1.212 31.867 50.859 0.35 20.96 ? 90 PHE A CE1 1 ATOM 303 C CE2 A PHE A 1 97 ? -1.657 30.148 49.815 0.65 28.68 ? 90 PHE A CE2 1 ATOM 304 C CE2 B PHE A 1 97 ? -0.787 29.488 50.748 0.35 20.22 ? 90 PHE A CE2 1 ATOM 305 C CZ A PHE A 1 97 ? -2.009 31.247 50.657 0.65 27.99 ? 90 PHE A CZ 1 ATOM 306 C CZ B PHE A 1 97 ? -1.532 30.561 51.244 0.35 21.18 ? 90 PHE A CZ 1 ATOM 307 N N A GLN A 1 98 ? 3.699 29.633 50.405 0.60 21.79 ? 91 GLN A N 1 ATOM 308 N N B GLN A 1 98 ? 3.714 29.640 50.363 0.40 21.81 ? 91 GLN A N 1 ATOM 309 C CA A GLN A 1 98 ? 3.909 28.836 51.642 0.60 23.25 ? 91 GLN A CA 1 ATOM 310 C CA B GLN A 1 98 ? 4.003 28.749 51.509 0.40 22.87 ? 91 GLN A CA 1 ATOM 311 C C A GLN A 1 98 ? 4.913 29.490 52.606 0.60 22.66 ? 91 GLN A C 1 ATOM 312 C C B GLN A 1 98 ? 4.930 29.415 52.550 0.40 22.49 ? 91 GLN A C 1 ATOM 313 O O A GLN A 1 98 ? 4.688 29.492 53.810 0.60 22.79 ? 91 GLN A O 1 ATOM 314 O O B GLN A 1 98 ? 4.645 29.384 53.743 0.40 22.57 ? 91 GLN A O 1 ATOM 315 C CB A GLN A 1 98 ? 4.277 27.365 51.375 0.60 23.99 ? 91 GLN A CB 1 ATOM 316 C CB B GLN A 1 98 ? 4.527 27.366 51.039 0.40 23.40 ? 91 GLN A CB 1 ATOM 317 C CG A GLN A 1 98 ? 3.127 26.539 50.734 0.60 27.94 ? 91 GLN A CG 1 ATOM 318 C CG B GLN A 1 98 ? 3.418 26.541 50.324 0.40 25.98 ? 91 GLN A CG 1 ATOM 319 C CD A GLN A 1 98 ? 1.867 26.446 51.606 0.60 32.67 ? 91 GLN A CD 1 ATOM 320 C CD B GLN A 1 98 ? 3.859 25.214 49.698 0.40 28.92 ? 91 GLN A CD 1 ATOM 321 O OE1 A GLN A 1 98 ? 1.946 26.264 52.831 0.60 34.79 ? 91 GLN A OE1 1 ATOM 322 O OE1 B GLN A 1 98 ? 5.043 24.955 49.472 0.40 31.22 ? 91 GLN A OE1 1 ATOM 323 N NE2 A GLN A 1 98 ? 0.690 26.554 50.967 0.60 33.61 ? 91 GLN A NE2 1 ATOM 324 N NE2 B GLN A 1 98 ? 2.875 24.369 49.398 0.40 30.92 ? 91 GLN A NE2 1 ATOM 325 N N . LEU A 1 99 ? 6.013 30.035 52.077 1.00 22.09 ? 92 LEU A N 1 ATOM 326 C CA . LEU A 1 99 ? 6.961 30.752 52.927 1.00 21.64 ? 92 LEU A CA 1 ATOM 327 C C . LEU A 1 99 ? 6.281 31.975 53.606 1.00 21.60 ? 92 LEU A C 1 ATOM 328 O O . LEU A 1 99 ? 6.517 32.231 54.803 1.00 22.04 ? 92 LEU A O 1 ATOM 329 C CB . LEU A 1 99 ? 8.203 31.187 52.137 1.00 20.23 ? 92 LEU A CB 1 ATOM 330 C CG . LEU A 1 99 ? 9.333 31.829 52.959 1.00 20.41 ? 92 LEU A CG 1 ATOM 331 C CD1 . LEU A 1 99 ? 9.911 30.873 54.124 1.00 20.24 ? 92 LEU A CD1 1 ATOM 332 C CD2 . LEU A 1 99 ? 10.485 32.306 52.066 1.00 18.71 ? 92 LEU A CD2 1 ATOM 333 N N . ALA A 1 100 ? 5.497 32.752 52.848 1.00 20.78 ? 93 ALA A N 1 ATOM 334 C CA . ALA A 1 100 ? 4.691 33.818 53.491 1.00 21.53 ? 93 ALA A CA 1 ATOM 335 C C . ALA A 1 100 ? 3.885 33.323 54.716 1.00 22.28 ? 93 ALA A C 1 ATOM 336 O O . ALA A 1 100 ? 3.879 33.981 55.774 1.00 22.42 ? 93 ALA A O 1 ATOM 337 C CB . ALA A 1 100 ? 3.768 34.540 52.501 1.00 20.47 ? 93 ALA A CB 1 ATOM 338 N N . LYS A 1 101 ? 3.184 32.202 54.570 1.00 22.45 ? 94 LYS A N 1 ATOM 339 C CA . LYS A 1 101 ? 2.374 31.649 55.673 1.00 23.68 ? 94 LYS A CA 1 ATOM 340 C C . LYS A 1 101 ? 3.241 31.220 56.848 1.00 23.98 ? 94 LYS A C 1 ATOM 341 O O . LYS A 1 101 ? 2.849 31.377 58.020 1.00 24.32 ? 94 LYS A O 1 ATOM 342 C CB . LYS A 1 101 ? 1.522 30.467 55.173 1.00 24.30 ? 94 LYS A CB 1 ATOM 343 C CG . LYS A 1 101 ? 0.406 30.933 54.194 1.00 27.89 ? 94 LYS A CG 1 ATOM 344 C CD . LYS A 1 101 ? -0.673 29.832 54.097 1.00 33.37 ? 94 LYS A CD 1 ATOM 345 C CE . LYS A 1 101 ? -0.427 28.881 52.939 0.20 32.11 ? 94 LYS A CE 1 ATOM 346 N NZ . LYS A 1 101 ? -1.538 27.904 52.840 0.20 32.39 ? 94 LYS A NZ 1 ATOM 347 N N . GLN A 1 102 ? 4.417 30.667 56.531 1.00 23.92 ? 95 GLN A N 1 ATOM 348 C CA . GLN A 1 102 ? 5.367 30.267 57.584 1.00 23.45 ? 95 GLN A CA 1 ATOM 349 C C . GLN A 1 102 ? 5.816 31.524 58.351 1.00 23.34 ? 95 GLN A C 1 ATOM 350 O O . GLN A 1 102 ? 5.817 31.517 59.561 1.00 22.79 ? 95 GLN A O 1 ATOM 351 C CB . GLN A 1 102 ? 6.582 29.534 57.012 1.00 23.14 ? 95 GLN A CB 1 ATOM 352 C CG . GLN A 1 102 ? 7.660 29.336 58.068 1.00 24.51 ? 95 GLN A CG 1 ATOM 353 C CD . GLN A 1 102 ? 9.000 28.941 57.492 1.00 25.12 ? 95 GLN A CD 1 ATOM 354 O OE1 . GLN A 1 102 ? 9.076 28.249 56.472 1.00 25.73 ? 95 GLN A OE1 1 ATOM 355 N NE2 . GLN A 1 102 ? 10.063 29.365 58.149 1.00 23.83 ? 95 GLN A NE2 1 ATOM 356 N N . ILE A 1 103 ? 6.186 32.588 57.635 1.00 23.09 ? 96 ILE A N 1 ATOM 357 C CA . ILE A 1 103 ? 6.695 33.787 58.274 1.00 23.25 ? 96 ILE A CA 1 ATOM 358 C C . ILE A 1 103 ? 5.579 34.382 59.156 1.00 23.44 ? 96 ILE A C 1 ATOM 359 O O . ILE A 1 103 ? 5.808 34.769 60.326 1.00 22.97 ? 96 ILE A O 1 ATOM 360 C CB . ILE A 1 103 ? 7.123 34.881 57.233 1.00 23.20 ? 96 ILE A CB 1 ATOM 361 C CG1 . ILE A 1 103 ? 8.315 34.456 56.342 1.00 24.99 ? 96 ILE A CG1 1 ATOM 362 C CG2 . ILE A 1 103 ? 7.448 36.228 57.945 1.00 24.26 ? 96 ILE A CG2 1 ATOM 363 C CD1 . ILE A 1 103 ? 9.499 33.894 57.040 1.00 26.76 ? 96 ILE A CD1 1 ATOM 364 N N . GLN A 1 104 ? 4.364 34.453 58.599 1.00 23.81 ? 97 GLN A N 1 ATOM 365 C CA . GLN A 1 104 ? 3.225 34.928 59.360 1.00 24.14 ? 97 GLN A CA 1 ATOM 366 C C . GLN A 1 104 ? 3.058 34.161 60.686 1.00 24.17 ? 97 GLN A C 1 ATOM 367 O O . GLN A 1 104 ? 2.903 34.781 61.755 1.00 23.66 ? 97 GLN A O 1 ATOM 368 C CB . GLN A 1 104 ? 1.954 34.808 58.535 1.00 24.49 ? 97 GLN A CB 1 ATOM 369 C CG . GLN A 1 104 ? 0.696 35.301 59.259 1.00 23.93 ? 97 GLN A CG 1 ATOM 370 C CD . GLN A 1 104 ? -0.596 35.015 58.485 1.00 24.69 ? 97 GLN A CD 1 ATOM 371 O OE1 . GLN A 1 104 ? -0.645 34.082 57.650 1.00 25.79 ? 97 GLN A OE1 1 ATOM 372 N NE2 . GLN A 1 104 ? -1.654 35.811 58.760 1.00 22.56 ? 97 GLN A NE2 1 ATOM 373 N N . SER A 1 105 ? 3.069 32.833 60.606 1.00 24.06 ? 98 SER A N 1 ATOM 374 C CA . SER A 1 105 ? 2.930 32.000 61.784 1.00 24.73 ? 98 SER A CA 1 ATOM 375 C C . SER A 1 105 ? 4.027 32.243 62.822 1.00 25.04 ? 98 SER A C 1 ATOM 376 O O . SER A 1 105 ? 3.729 32.310 64.023 1.00 25.27 ? 98 SER A O 1 ATOM 377 C CB . SER A 1 105 ? 3.006 30.513 61.405 1.00 24.45 ? 98 SER A CB 1 ATOM 378 O OG A SER A 1 105 ? 2.713 29.717 62.529 0.50 22.50 ? 98 SER A OG 1 ATOM 379 O OG B SER A 1 105 ? 1.795 30.148 60.779 0.50 26.63 ? 98 SER A OG 1 ATOM 380 N N . GLN A 1 106 ? 5.286 32.300 62.363 1.00 24.17 ? 99 GLN A N 1 ATOM 381 C CA . GLN A 1 106 ? 6.404 32.478 63.296 1.00 24.27 ? 99 GLN A CA 1 ATOM 382 C C . GLN A 1 106 ? 6.390 33.876 63.899 1.00 23.55 ? 99 GLN A C 1 ATOM 383 O O . GLN A 1 106 ? 6.654 34.047 65.087 1.00 24.21 ? 99 GLN A O 1 ATOM 384 C CB . GLN A 1 106 ? 7.729 32.213 62.603 1.00 23.74 ? 99 GLN A CB 1 ATOM 385 C CG . GLN A 1 106 ? 7.899 30.732 62.282 1.00 26.30 ? 99 GLN A CG 1 ATOM 386 C CD . GLN A 1 106 ? 9.251 30.451 61.661 1.00 29.74 ? 99 GLN A CD 1 ATOM 387 O OE1 . GLN A 1 106 ? 9.574 30.932 60.578 1.00 29.30 ? 99 GLN A OE1 1 ATOM 388 N NE2 . GLN A 1 106 ? 10.044 29.659 62.349 1.00 34.05 ? 99 GLN A NE2 1 ATOM 389 N N . TRP A 1 107 ? 6.084 34.886 63.110 1.00 23.16 ? 100 TRP A N 1 ATOM 390 C CA . TRP A 1 107 ? 5.952 36.239 63.695 1.00 23.43 ? 100 TRP A CA 1 ATOM 391 C C . TRP A 1 107 ? 4.898 36.315 64.797 1.00 24.70 ? 100 TRP A C 1 ATOM 392 O O . TRP A 1 107 ? 5.089 37.059 65.775 1.00 24.36 ? 100 TRP A O 1 ATOM 393 C CB . TRP A 1 107 ? 5.669 37.315 62.633 1.00 22.48 ? 100 TRP A CB 1 ATOM 394 C CG . TRP A 1 107 ? 6.907 37.634 61.815 1.00 20.54 ? 100 TRP A CG 1 ATOM 395 C CD1 . TRP A 1 107 ? 8.127 37.002 61.878 1.00 20.67 ? 100 TRP A CD1 1 ATOM 396 C CD2 . TRP A 1 107 ? 7.012 38.616 60.783 1.00 19.14 ? 100 TRP A CD2 1 ATOM 397 N NE1 . TRP A 1 107 ? 9.003 37.558 60.943 1.00 19.86 ? 100 TRP A NE1 1 ATOM 398 C CE2 . TRP A 1 107 ? 8.336 38.545 60.260 1.00 19.47 ? 100 TRP A CE2 1 ATOM 399 C CE3 . TRP A 1 107 ? 6.110 39.574 60.247 1.00 18.16 ? 100 TRP A CE3 1 ATOM 400 C CZ2 . TRP A 1 107 ? 8.784 39.392 59.229 1.00 19.76 ? 100 TRP A CZ2 1 ATOM 401 C CZ3 . TRP A 1 107 ? 6.536 40.385 59.205 1.00 19.19 ? 100 TRP A CZ3 1 ATOM 402 C CH2 . TRP A 1 107 ? 7.888 40.302 58.716 1.00 20.95 ? 100 TRP A CH2 1 ATOM 403 N N . LYS A 1 108 ? 3.775 35.604 64.614 1.00 26.22 ? 101 LYS A N 1 ATOM 404 C CA . LYS A 1 108 ? 2.774 35.487 65.686 1.00 28.91 ? 101 LYS A CA 1 ATOM 405 C C . LYS A 1 108 ? 3.373 34.762 66.903 1.00 28.69 ? 101 LYS A C 1 ATOM 406 O O . LYS A 1 108 ? 3.241 35.266 68.007 1.00 29.43 ? 101 LYS A O 1 ATOM 407 C CB . LYS A 1 108 ? 1.480 34.777 65.249 1.00 29.85 ? 101 LYS A CB 1 ATOM 408 C CG . LYS A 1 108 ? 0.620 35.571 64.370 1.00 34.61 ? 101 LYS A CG 1 ATOM 409 C CD . LYS A 1 108 ? -0.494 34.738 63.713 1.00 39.91 ? 101 LYS A CD 1 ATOM 410 C CE . LYS A 1 108 ? -1.417 35.702 62.966 1.00 41.03 ? 101 LYS A CE 1 ATOM 411 N NZ . LYS A 1 108 ? -2.636 35.021 62.491 1.00 44.37 ? 101 LYS A NZ 1 ATOM 412 N N A GLU A 1 109 ? 4.042 33.628 66.665 0.50 29.05 ? 102 GLU A N 1 ATOM 413 N N B GLU A 1 109 ? 4.026 33.612 66.725 0.50 29.43 ? 102 GLU A N 1 ATOM 414 C CA A GLU A 1 109 ? 4.690 32.837 67.734 0.50 29.13 ? 102 GLU A CA 1 ATOM 415 C CA B GLU A 1 109 ? 4.607 32.917 67.902 0.50 29.81 ? 102 GLU A CA 1 ATOM 416 C C A GLU A 1 109 ? 5.666 33.726 68.512 0.50 28.38 ? 102 GLU A C 1 ATOM 417 C C B GLU A 1 109 ? 5.668 33.778 68.572 0.50 28.80 ? 102 GLU A C 1 ATOM 418 O O A GLU A 1 109 ? 5.745 33.651 69.743 0.50 27.56 ? 102 GLU A O 1 ATOM 419 O O B GLU A 1 109 ? 5.820 33.725 69.796 0.50 27.99 ? 102 GLU A O 1 ATOM 420 C CB A GLU A 1 109 ? 5.469 31.628 67.166 0.50 29.69 ? 102 GLU A CB 1 ATOM 421 C CB B GLU A 1 109 ? 5.227 31.553 67.569 0.50 30.68 ? 102 GLU A CB 1 ATOM 422 C CG A GLU A 1 109 ? 4.651 30.579 66.405 0.50 31.90 ? 102 GLU A CG 1 ATOM 423 C CG B GLU A 1 109 ? 4.428 30.337 68.011 0.50 35.19 ? 102 GLU A CG 1 ATOM 424 C CD A GLU A 1 109 ? 5.519 29.551 65.666 0.50 33.90 ? 102 GLU A CD 1 ATOM 425 C CD B GLU A 1 109 ? 4.196 30.252 69.522 0.50 39.70 ? 102 GLU A CD 1 ATOM 426 O OE1 A GLU A 1 109 ? 5.038 28.947 64.677 0.50 33.04 ? 102 GLU A OE1 1 ATOM 427 O OE1 B GLU A 1 109 ? 5.185 30.228 70.299 0.50 41.52 ? 102 GLU A OE1 1 ATOM 428 O OE2 A GLU A 1 109 ? 6.692 29.368 66.058 0.50 34.58 ? 102 GLU A OE2 1 ATOM 429 O OE2 B GLU A 1 109 ? 3.009 30.191 69.931 0.50 41.75 ? 102 GLU A OE2 1 ATOM 430 N N . PHE A 1 110 ? 6.404 34.556 67.773 1.00 27.58 ? 103 PHE A N 1 ATOM 431 C CA . PHE A 1 110 ? 7.455 35.450 68.320 1.00 27.89 ? 103 PHE A CA 1 ATOM 432 C C . PHE A 1 110 ? 6.879 36.548 69.243 1.00 27.65 ? 103 PHE A C 1 ATOM 433 O O . PHE A 1 110 ? 7.627 37.175 69.987 1.00 28.45 ? 103 PHE A O 1 ATOM 434 C CB . PHE A 1 110 ? 8.302 36.136 67.188 1.00 27.07 ? 103 PHE A CB 1 ATOM 435 C CG . PHE A 1 110 ? 9.233 35.181 66.404 1.00 27.49 ? 103 PHE A CG 1 ATOM 436 C CD1 . PHE A 1 110 ? 9.566 33.899 66.890 1.00 25.96 ? 103 PHE A CD1 1 ATOM 437 C CD2 . PHE A 1 110 ? 9.802 35.613 65.199 1.00 25.69 ? 103 PHE A CD2 1 ATOM 438 C CE1 . PHE A 1 110 ? 10.445 33.032 66.151 1.00 28.89 ? 103 PHE A CE1 1 ATOM 439 C CE2 . PHE A 1 110 ? 10.675 34.774 64.431 1.00 27.68 ? 103 PHE A CE2 1 ATOM 440 C CZ . PHE A 1 110 ? 11.013 33.494 64.895 1.00 26.96 ? 103 PHE A CZ 1 ATOM 441 N N . GLY A 1 111 ? 5.577 36.829 69.118 1.00 27.23 ? 104 GLY A N 1 ATOM 442 C CA . GLY A 1 111 ? 4.846 37.717 70.029 1.00 26.48 ? 104 GLY A CA 1 ATOM 443 C C . GLY A 1 111 ? 4.241 38.984 69.407 1.00 26.89 ? 104 GLY A C 1 ATOM 444 O O . GLY A 1 111 ? 3.748 39.843 70.138 1.00 27.75 ? 104 GLY A O 1 ATOM 445 N N . LEU A 1 112 ? 4.285 39.152 68.086 1.00 25.65 ? 105 LEU A N 1 ATOM 446 C CA . LEU A 1 112 ? 3.680 40.365 67.499 1.00 25.07 ? 105 LEU A CA 1 ATOM 447 C C . LEU A 1 112 ? 2.170 40.449 67.810 1.00 25.67 ? 105 LEU A C 1 ATOM 448 O O . LEU A 1 112 ? 1.513 39.428 67.996 1.00 26.03 ? 105 LEU A O 1 ATOM 449 C CB . LEU A 1 112 ? 3.967 40.486 65.996 1.00 24.70 ? 105 LEU A CB 1 ATOM 450 C CG . LEU A 1 112 ? 5.438 40.651 65.598 1.00 22.75 ? 105 LEU A CG 1 ATOM 451 C CD1 . LEU A 1 112 ? 5.551 41.039 64.075 1.00 20.44 ? 105 LEU A CD1 1 ATOM 452 C CD2 . LEU A 1 112 ? 6.131 41.729 66.499 1.00 20.95 ? 105 LEU A CD2 1 ATOM 453 N N . ASP A 1 113 ? 1.633 41.657 67.912 1.00 25.63 ? 106 ASP A N 1 ATOM 454 C CA . ASP A 1 113 ? 0.193 41.829 68.219 1.00 27.32 ? 106 ASP A CA 1 ATOM 455 C C . ASP A 1 113 ? -0.740 41.351 67.110 1.00 27.51 ? 106 ASP A C 1 ATOM 456 O O . ASP A 1 113 ? -1.803 40.807 67.379 1.00 27.99 ? 106 ASP A O 1 ATOM 457 C CB . ASP A 1 113 ? -0.133 43.288 68.552 1.00 27.10 ? 106 ASP A CB 1 ATOM 458 C CG . ASP A 1 113 ? 0.605 43.750 69.790 1.00 27.63 ? 106 ASP A CG 1 ATOM 459 O OD1 . ASP A 1 113 ? 0.363 43.152 70.858 1.00 26.12 ? 106 ASP A OD1 1 ATOM 460 O OD2 . ASP A 1 113 ? 1.451 44.654 69.674 1.00 26.83 ? 106 ASP A OD2 1 ATOM 461 N N . SER A 1 114 ? -0.338 41.569 65.875 1.00 25.91 ? 107 SER A N 1 ATOM 462 C CA . SER A 1 114 ? -1.147 41.167 64.755 1.00 26.06 ? 107 SER A CA 1 ATOM 463 C C . SER A 1 114 ? -0.176 40.870 63.609 1.00 25.24 ? 107 SER A C 1 ATOM 464 O O . SER A 1 114 ? 0.879 41.505 63.489 1.00 24.30 ? 107 SER A O 1 ATOM 465 C CB . SER A 1 114 ? -2.178 42.280 64.420 1.00 26.28 ? 107 SER A CB 1 ATOM 466 O OG A SER A 1 114 ? -1.513 43.472 64.055 0.50 25.88 ? 107 SER A OG 1 ATOM 467 O OG B SER A 1 114 ? -2.205 42.541 63.043 0.50 28.08 ? 107 SER A OG 1 ATOM 468 N N . VAL A 1 115 ? -0.480 39.822 62.851 1.00 24.35 ? 108 VAL A N 1 ATOM 469 C CA . VAL A 1 115 ? 0.300 39.504 61.661 1.00 23.97 ? 108 VAL A CA 1 ATOM 470 C C . VAL A 1 115 ? -0.655 39.076 60.541 1.00 24.25 ? 108 VAL A C 1 ATOM 471 O O . VAL A 1 115 ? -1.317 38.029 60.635 1.00 24.70 ? 108 VAL A O 1 ATOM 472 C CB . VAL A 1 115 ? 1.410 38.427 61.903 1.00 23.44 ? 108 VAL A CB 1 ATOM 473 C CG1 . VAL A 1 115 ? 2.359 38.426 60.689 1.00 19.69 ? 108 VAL A CG1 1 ATOM 474 C CG2 . VAL A 1 115 ? 2.187 38.703 63.195 1.00 22.01 ? 108 VAL A CG2 1 ATOM 475 N N . GLU A 1 116 ? -0.724 39.891 59.502 1.00 23.85 ? 109 GLU A N 1 ATOM 476 C CA . GLU A 1 116 ? -1.643 39.662 58.385 1.00 24.89 ? 109 GLU A CA 1 ATOM 477 C C . GLU A 1 116 ? -0.931 39.517 57.024 1.00 23.63 ? 109 GLU A C 1 ATOM 478 O O . GLU A 1 116 ? 0.161 40.066 56.828 1.00 23.53 ? 109 GLU A O 1 ATOM 479 C CB . GLU A 1 116 ? -2.689 40.821 58.320 1.00 26.49 ? 109 GLU A CB 1 ATOM 480 C CG . GLU A 1 116 ? -3.652 40.906 59.593 1.00 30.52 ? 109 GLU A CG 1 ATOM 481 C CD . GLU A 1 116 ? -4.439 39.598 59.858 0.75 36.40 ? 109 GLU A CD 1 ATOM 482 O OE1 . GLU A 1 116 ? -5.013 39.010 58.907 0.75 38.71 ? 109 GLU A OE1 1 ATOM 483 O OE2 . GLU A 1 116 ? -4.479 39.136 61.026 0.75 39.43 ? 109 GLU A OE2 1 ATOM 484 N N . LEU A 1 117 ? -1.545 38.775 56.084 1.00 22.54 ? 110 LEU A N 1 ATOM 485 C CA . LEU A 1 117 ? -1.123 38.809 54.672 1.00 21.53 ? 110 LEU A CA 1 ATOM 486 C C . LEU A 1 117 ? -1.903 39.915 53.930 1.00 22.08 ? 110 LEU A C 1 ATOM 487 O O . LEU A 1 117 ? -3.102 40.009 54.085 1.00 22.87 ? 110 LEU A O 1 ATOM 488 C CB . LEU A 1 117 ? -1.420 37.480 53.996 1.00 21.83 ? 110 LEU A CB 1 ATOM 489 C CG . LEU A 1 117 ? -0.683 36.253 54.528 1.00 24.23 ? 110 LEU A CG 1 ATOM 490 C CD1 . LEU A 1 117 ? -1.002 34.995 53.695 1.00 29.06 ? 110 LEU A CD1 1 ATOM 491 C CD2 . LEU A 1 117 ? 0.822 36.492 54.577 1.00 23.59 ? 110 LEU A CD2 1 ATOM 492 N N . ALA A 1 118 ? -1.226 40.741 53.152 1.00 20.97 ? 111 ALA A N 1 ATOM 493 C CA . ALA A 1 118 ? -1.859 41.738 52.302 1.00 20.89 ? 111 ALA A CA 1 ATOM 494 C C . ALA A 1 118 ? -1.510 41.236 50.894 1.00 20.76 ? 111 ALA A C 1 ATOM 495 O O . ALA A 1 118 ? -0.310 41.172 50.507 1.00 21.57 ? 111 ALA A O 1 ATOM 496 C CB . ALA A 1 118 ? -1.232 43.168 52.547 1.00 19.52 ? 111 ALA A CB 1 ATOM 497 N N . HIS A 1 119 ? -2.527 40.875 50.129 1.00 20.33 ? 112 HIS A N 1 ATOM 498 C CA . HIS A 1 119 ? -2.311 40.309 48.793 1.00 19.65 ? 112 HIS A CA 1 ATOM 499 C C . HIS A 1 119 ? -2.781 41.274 47.702 1.00 19.04 ? 112 HIS A C 1 ATOM 500 O O . HIS A 1 119 ? -3.641 42.106 47.970 1.00 17.91 ? 112 HIS A O 1 ATOM 501 C CB . HIS A 1 119 ? -3.004 38.955 48.658 1.00 19.80 ? 112 HIS A CB 1 ATOM 502 C CG . HIS A 1 119 ? -4.503 39.017 48.677 1.00 22.92 ? 112 HIS A CG 1 ATOM 503 N ND1 . HIS A 1 119 ? -5.249 38.753 49.814 1.00 26.35 ? 112 HIS A ND1 1 ATOM 504 C CD2 . HIS A 1 119 ? -5.402 39.296 47.697 1.00 25.87 ? 112 HIS A CD2 1 ATOM 505 C CE1 . HIS A 1 119 ? -6.542 38.854 49.528 1.00 26.62 ? 112 HIS A CE1 1 ATOM 506 N NE2 . HIS A 1 119 ? -6.660 39.198 48.254 1.00 24.77 ? 112 HIS A NE2 1 ATOM 507 N N . TYR A 1 120 ? -2.187 41.179 46.508 1.00 17.66 ? 113 TYR A N 1 ATOM 508 C CA . TYR A 1 120 ? -2.472 42.064 45.365 1.00 17.78 ? 113 TYR A CA 1 ATOM 509 C C . TYR A 1 120 ? -2.354 41.197 44.130 1.00 17.48 ? 113 TYR A C 1 ATOM 510 O O . TYR A 1 120 ? -1.661 40.153 44.179 1.00 18.62 ? 113 TYR A O 1 ATOM 511 C CB . TYR A 1 120 ? -1.466 43.247 45.267 1.00 17.00 ? 113 TYR A CB 1 ATOM 512 C CG . TYR A 1 120 ? -1.478 44.016 46.551 1.00 16.34 ? 113 TYR A CG 1 ATOM 513 C CD1 . TYR A 1 120 ? -2.465 44.984 46.778 1.00 14.61 ? 113 TYR A CD1 1 ATOM 514 C CD2 . TYR A 1 120 ? -0.584 43.696 47.591 1.00 15.85 ? 113 TYR A CD2 1 ATOM 515 C CE1 . TYR A 1 120 ? -2.522 45.668 48.043 1.00 16.45 ? 113 TYR A CE1 1 ATOM 516 C CE2 . TYR A 1 120 ? -0.649 44.370 48.839 1.00 14.38 ? 113 TYR A CE2 1 ATOM 517 C CZ . TYR A 1 120 ? -1.620 45.328 49.042 1.00 16.76 ? 113 TYR A CZ 1 ATOM 518 O OH . TYR A 1 120 ? -1.697 45.965 50.265 1.00 17.05 ? 113 TYR A OH 1 ATOM 519 N N . ASP A 1 121 ? -3.007 41.600 43.046 1.00 16.99 ? 114 ASP A N 1 ATOM 520 C CA . ASP A 1 121 ? -2.892 40.821 41.782 1.00 17.84 ? 114 ASP A CA 1 ATOM 521 C C . ASP A 1 121 ? -2.196 41.720 40.805 1.00 17.39 ? 114 ASP A C 1 ATOM 522 O O . ASP A 1 121 ? -2.793 42.706 40.295 1.00 17.84 ? 114 ASP A O 1 ATOM 523 C CB . ASP A 1 121 ? -4.286 40.374 41.270 1.00 18.90 ? 114 ASP A CB 1 ATOM 524 C CG . ASP A 1 121 ? -4.971 39.387 42.220 1.00 22.03 ? 114 ASP A CG 1 ATOM 525 O OD1 . ASP A 1 121 ? -4.343 38.379 42.634 1.00 21.81 ? 114 ASP A OD1 1 ATOM 526 O OD2 . ASP A 1 121 ? -6.138 39.638 42.593 1.00 25.73 ? 114 ASP A OD2 1 ATOM 527 N N . VAL A 1 122 ? -0.914 41.416 40.575 1.00 16.76 ? 115 VAL A N 1 ATOM 528 C CA . VAL A 1 122 ? -0.022 42.328 39.811 1.00 15.98 ? 115 VAL A CA 1 ATOM 529 C C . VAL A 1 122 ? 0.510 41.633 38.545 1.00 17.07 ? 115 VAL A C 1 ATOM 530 O O . VAL A 1 122 ? 0.547 40.387 38.492 1.00 18.18 ? 115 VAL A O 1 ATOM 531 C CB . VAL A 1 122 ? 1.151 42.831 40.688 1.00 15.03 ? 115 VAL A CB 1 ATOM 532 C CG1 . VAL A 1 122 ? 0.622 43.571 41.930 1.00 15.22 ? 115 VAL A CG1 1 ATOM 533 C CG2 . VAL A 1 122 ? 2.094 41.658 41.093 1.00 14.48 ? 115 VAL A CG2 1 ATOM 534 N N . LEU A 1 123 ? 0.907 42.425 37.546 1.00 16.66 ? 116 LEU A N 1 ATOM 535 C CA . LEU A 1 123 ? 1.586 41.885 36.355 1.00 15.73 ? 116 LEU A CA 1 ATOM 536 C C . LEU A 1 123 ? 2.948 41.299 36.714 1.00 16.53 ? 116 LEU A C 1 ATOM 537 O O . LEU A 1 123 ? 3.800 42.019 37.226 1.00 18.32 ? 116 LEU A O 1 ATOM 538 C CB . LEU A 1 123 ? 1.790 42.955 35.279 1.00 15.50 ? 116 LEU A CB 1 ATOM 539 C CG . LEU A 1 123 ? 2.035 42.317 33.901 1.00 16.24 ? 116 LEU A CG 1 ATOM 540 C CD1 . LEU A 1 123 ? 0.728 41.626 33.388 1.00 16.74 ? 116 LEU A CD1 1 ATOM 541 C CD2 . LEU A 1 123 ? 2.496 43.425 32.953 1.00 18.13 ? 116 LEU A CD2 1 ATOM 542 N N . LEU A 1 124 ? 3.129 40.000 36.471 1.00 15.74 ? 117 LEU A N 1 ATOM 543 C CA . LEU A 1 124 ? 4.456 39.330 36.581 1.00 16.62 ? 117 LEU A CA 1 ATOM 544 C C . LEU A 1 124 ? 4.827 38.777 35.213 1.00 18.23 ? 117 LEU A C 1 ATOM 545 O O . LEU A 1 124 ? 4.074 38.981 34.249 1.00 19.84 ? 117 LEU A O 1 ATOM 546 C CB . LEU A 1 124 ? 4.471 38.231 37.688 1.00 15.89 ? 117 LEU A CB 1 ATOM 547 C CG . LEU A 1 124 ? 4.146 38.672 39.142 1.00 15.06 ? 117 LEU A CG 1 ATOM 548 C CD1 . LEU A 1 124 ? 4.324 37.449 40.136 1.00 15.18 ? 117 LEU A CD1 1 ATOM 549 C CD2 . LEU A 1 124 ? 4.995 39.924 39.629 1.00 13.70 ? 117 LEU A CD2 1 ATOM 550 N N . SER A 1 125 ? 5.993 38.119 35.090 1.00 19.75 ? 118 SER A N 1 ATOM 551 C CA . SER A 1 125 ? 6.478 37.627 33.807 1.00 19.73 ? 118 SER A CA 1 ATOM 552 C C . SER A 1 125 ? 7.235 36.318 34.034 1.00 20.48 ? 118 SER A C 1 ATOM 553 O O . SER A 1 125 ? 8.029 36.231 34.987 1.00 19.90 ? 118 SER A O 1 ATOM 554 C CB . SER A 1 125 ? 7.439 38.679 33.214 1.00 20.39 ? 118 SER A CB 1 ATOM 555 O OG . SER A 1 125 ? 8.255 38.183 32.137 1.00 21.10 ? 118 SER A OG 1 ATOM 556 N N . TYR A 1 126 ? 7.004 35.321 33.175 1.00 20.07 ? 119 TYR A N 1 ATOM 557 C CA . TYR A 1 126 ? 7.656 34.041 33.312 1.00 21.49 ? 119 TYR A CA 1 ATOM 558 C C . TYR A 1 126 ? 7.986 33.467 31.958 1.00 23.25 ? 119 TYR A C 1 ATOM 559 O O . TYR A 1 126 ? 7.259 33.691 30.987 1.00 23.57 ? 119 TYR A O 1 ATOM 560 C CB . TYR A 1 126 ? 6.718 33.033 33.964 1.00 21.85 ? 119 TYR A CB 1 ATOM 561 C CG . TYR A 1 126 ? 6.226 33.422 35.343 1.00 22.97 ? 119 TYR A CG 1 ATOM 562 C CD1 . TYR A 1 126 ? 7.076 33.364 36.466 1.00 22.07 ? 119 TYR A CD1 1 ATOM 563 C CD2 . TYR A 1 126 ? 4.890 33.819 35.530 1.00 24.21 ? 119 TYR A CD2 1 ATOM 564 C CE1 . TYR A 1 126 ? 6.595 33.705 37.755 1.00 21.38 ? 119 TYR A CE1 1 ATOM 565 C CE2 . TYR A 1 126 ? 4.404 34.160 36.807 1.00 22.25 ? 119 TYR A CE2 1 ATOM 566 C CZ . TYR A 1 126 ? 5.248 34.080 37.902 1.00 22.62 ? 119 TYR A CZ 1 ATOM 567 O OH . TYR A 1 126 ? 4.739 34.384 39.140 1.00 21.27 ? 119 TYR A OH 1 ATOM 568 N N . PRO A 1 127 ? 9.079 32.689 31.884 1.00 24.21 ? 120 PRO A N 1 ATOM 569 C CA . PRO A 1 127 ? 9.388 31.948 30.665 1.00 24.95 ? 120 PRO A CA 1 ATOM 570 C C . PRO A 1 127 ? 8.303 30.897 30.417 1.00 26.46 ? 120 PRO A C 1 ATOM 571 O O . PRO A 1 127 ? 7.628 30.443 31.363 1.00 25.91 ? 120 PRO A O 1 ATOM 572 C CB . PRO A 1 127 ? 10.725 31.220 30.991 1.00 24.03 ? 120 PRO A CB 1 ATOM 573 C CG . PRO A 1 127 ? 11.299 31.965 32.198 1.00 25.13 ? 120 PRO A CG 1 ATOM 574 C CD . PRO A 1 127 ? 10.091 32.519 32.947 1.00 23.34 ? 120 PRO A CD 1 ATOM 575 N N . ASN A 1 128 ? 8.144 30.532 29.157 1.00 27.71 ? 121 ASN A N 1 ATOM 576 C CA . ASN A 1 128 ? 7.267 29.431 28.786 1.00 30.62 ? 121 ASN A CA 1 ATOM 577 C C . ASN A 1 128 ? 8.037 28.101 28.973 1.00 31.63 ? 121 ASN A C 1 ATOM 578 O O . ASN A 1 128 ? 9.037 27.820 28.276 1.00 30.39 ? 121 ASN A O 1 ATOM 579 C CB . ASN A 1 128 ? 6.776 29.650 27.355 1.00 30.91 ? 121 ASN A CB 1 ATOM 580 C CG . ASN A 1 128 ? 5.791 28.586 26.898 1.00 35.40 ? 121 ASN A CG 1 ATOM 581 O OD1 . ASN A 1 128 ? 5.917 27.417 27.254 1.00 36.69 ? 121 ASN A OD1 1 ATOM 582 N ND2 . ASN A 1 128 ? 4.813 28.985 26.100 1.00 41.02 ? 121 ASN A ND2 1 ATOM 583 N N . LYS A 1 129 ? 7.587 27.331 29.967 1.00 33.85 ? 122 LYS A N 1 ATOM 584 C CA . LYS A 1 129 ? 8.068 25.972 30.278 1.00 36.24 ? 122 LYS A CA 1 ATOM 585 C C . LYS A 1 129 ? 8.253 25.037 29.085 1.00 37.46 ? 122 LYS A C 1 ATOM 586 O O . LYS A 1 129 ? 9.160 24.199 29.101 1.00 37.92 ? 122 LYS A O 1 ATOM 587 C CB . LYS A 1 129 ? 7.129 25.280 31.287 1.00 37.25 ? 122 LYS A CB 1 ATOM 588 C CG . LYS A 1 129 ? 7.389 25.653 32.757 1.00 38.92 ? 122 LYS A CG 1 ATOM 589 C CD . LYS A 1 129 ? 6.095 25.650 33.557 0.20 38.72 ? 122 LYS A CD 1 ATOM 590 C CE . LYS A 1 129 ? 6.257 26.403 34.868 0.20 38.40 ? 122 LYS A CE 1 ATOM 591 N NZ . LYS A 1 129 ? 4.944 26.710 35.488 0.20 37.95 ? 122 LYS A NZ 1 ATOM 592 N N . THR A 1 130 ? 7.419 25.158 28.057 1.00 38.16 ? 123 THR A N 1 ATOM 593 C CA . THR A 1 130 ? 7.518 24.223 26.937 1.00 39.80 ? 123 THR A CA 1 ATOM 594 C C . THR A 1 130 ? 8.080 24.842 25.644 1.00 39.68 ? 123 THR A C 1 ATOM 595 O O . THR A 1 130 ? 8.143 24.187 24.624 1.00 39.55 ? 123 THR A O 1 ATOM 596 C CB . THR A 1 130 ? 6.167 23.461 26.687 1.00 40.54 ? 123 THR A CB 1 ATOM 597 O OG1 . THR A 1 130 ? 5.110 24.411 26.496 1.00 41.23 ? 123 THR A OG1 1 ATOM 598 C CG2 . THR A 1 130 ? 5.821 22.579 27.893 1.00 41.57 ? 123 THR A CG2 1 ATOM 599 N N . HIS A 1 131 ? 8.493 26.102 25.694 1.00 38.88 ? 124 HIS A N 1 ATOM 600 C CA . HIS A 1 131 ? 9.016 26.764 24.516 1.00 38.71 ? 124 HIS A CA 1 ATOM 601 C C . HIS A 1 131 ? 10.133 27.674 25.041 1.00 37.00 ? 124 HIS A C 1 ATOM 602 O O . HIS A 1 131 ? 9.905 28.852 25.242 1.00 35.80 ? 124 HIS A O 1 ATOM 603 C CB . HIS A 1 131 ? 7.885 27.564 23.874 1.00 40.06 ? 124 HIS A CB 1 ATOM 604 C CG . HIS A 1 131 ? 8.113 27.948 22.445 1.00 44.22 ? 124 HIS A CG 1 ATOM 605 N ND1 . HIS A 1 131 ? 7.304 28.859 21.792 0.85 47.32 ? 124 HIS A ND1 1 ATOM 606 C CD2 . HIS A 1 131 ? 9.040 27.555 21.541 0.60 46.70 ? 124 HIS A CD2 1 ATOM 607 C CE1 . HIS A 1 131 ? 7.718 28.999 20.545 0.40 47.35 ? 124 HIS A CE1 1 ATOM 608 N NE2 . HIS A 1 131 ? 8.774 28.225 20.368 0.50 48.07 ? 124 HIS A NE2 1 ATOM 609 N N . PRO A 1 132 ? 11.330 27.095 25.303 1.00 35.68 ? 125 PRO A N 1 ATOM 610 C CA . PRO A 1 132 ? 12.456 27.777 25.973 1.00 34.36 ? 125 PRO A CA 1 ATOM 611 C C . PRO A 1 132 ? 13.042 28.967 25.197 1.00 32.96 ? 125 PRO A C 1 ATOM 612 O O . PRO A 1 132 ? 13.067 28.970 23.949 1.00 33.32 ? 125 PRO A O 1 ATOM 613 C CB . PRO A 1 132 ? 13.515 26.670 26.147 1.00 35.02 ? 125 PRO A CB 1 ATOM 614 C CG . PRO A 1 132 ? 12.850 25.367 25.762 1.00 35.16 ? 125 PRO A CG 1 ATOM 615 C CD . PRO A 1 132 ? 11.627 25.682 24.971 1.00 36.10 ? 125 PRO A CD 1 ATOM 616 N N . ASN A 1 133 ? 13.440 30.001 25.940 1.00 30.84 ? 126 ASN A N 1 ATOM 617 C CA . ASN A 1 133 ? 14.175 31.155 25.389 1.00 29.50 ? 126 ASN A CA 1 ATOM 618 C C . ASN A 1 133 ? 15.610 30.770 25.107 1.00 29.53 ? 126 ASN A C 1 ATOM 619 O O . ASN A 1 133 ? 16.249 30.029 25.910 1.00 29.06 ? 126 ASN A O 1 ATOM 620 C CB . ASN A 1 133 ? 14.168 32.363 26.367 1.00 27.90 ? 126 ASN A CB 1 ATOM 621 C CG . ASN A 1 133 ? 12.769 32.788 26.725 1.00 27.38 ? 126 ASN A CG 1 ATOM 622 O OD1 . ASN A 1 133 ? 11.854 32.694 25.906 1.00 27.83 ? 126 ASN A OD1 1 ATOM 623 N ND2 . ASN A 1 133 ? 12.583 33.218 27.955 1.00 23.89 ? 126 ASN A ND2 1 ATOM 624 N N . TYR A 1 134 ? 16.114 31.255 23.977 1.00 29.84 ? 127 TYR A N 1 ATOM 625 C CA . TYR A 1 134 ? 17.528 31.057 23.631 1.00 30.70 ? 127 TYR A CA 1 ATOM 626 C C . TYR A 1 134 ? 17.897 31.985 22.487 1.00 30.62 ? 127 TYR A C 1 ATOM 627 O O . TYR A 1 134 ? 17.016 32.632 21.892 1.00 30.42 ? 127 TYR A O 1 ATOM 628 C CB . TYR A 1 134 ? 17.866 29.579 23.339 1.00 31.13 ? 127 TYR A CB 1 ATOM 629 C CG . TYR A 1 134 ? 17.339 29.050 22.013 1.00 33.53 ? 127 TYR A CG 1 ATOM 630 C CD1 . TYR A 1 134 ? 18.189 28.873 20.923 1.00 36.26 ? 127 TYR A CD1 1 ATOM 631 C CD2 . TYR A 1 134 ? 15.979 28.732 21.850 1.00 34.66 ? 127 TYR A CD2 1 ATOM 632 C CE1 . TYR A 1 134 ? 17.700 28.369 19.688 1.00 35.36 ? 127 TYR A CE1 1 ATOM 633 C CE2 . TYR A 1 134 ? 15.492 28.246 20.642 1.00 35.57 ? 127 TYR A CE2 1 ATOM 634 C CZ . TYR A 1 134 ? 16.353 28.064 19.564 1.00 36.45 ? 127 TYR A CZ 1 ATOM 635 O OH . TYR A 1 134 ? 15.841 27.589 18.362 1.00 36.47 ? 127 TYR A OH 1 ATOM 636 N N . ILE A 1 135 ? 19.199 32.088 22.232 1.00 30.83 ? 128 ILE A N 1 ATOM 637 C CA . ILE A 1 135 ? 19.746 32.898 21.148 1.00 30.34 ? 128 ILE A CA 1 ATOM 638 C C . ILE A 1 135 ? 20.587 32.006 20.238 1.00 31.28 ? 128 ILE A C 1 ATOM 639 O O . ILE A 1 135 ? 21.255 31.090 20.721 1.00 30.71 ? 128 ILE A O 1 ATOM 640 C CB . ILE A 1 135 ? 20.643 34.036 21.703 1.00 30.06 ? 128 ILE A CB 1 ATOM 641 C CG1 . ILE A 1 135 ? 19.842 35.002 22.588 1.00 28.92 ? 128 ILE A CG1 1 ATOM 642 C CG2 . ILE A 1 135 ? 21.274 34.825 20.581 1.00 29.85 ? 128 ILE A CG2 1 ATOM 643 C CD1 . ILE A 1 135 ? 20.721 35.760 23.640 1.00 27.01 ? 128 ILE A CD1 1 ATOM 644 N N . SER A 1 136 ? 20.577 32.297 18.937 1.00 32.01 ? 129 SER A N 1 ATOM 645 C CA . SER A 1 136 ? 21.361 31.547 17.950 1.00 34.25 ? 129 SER A CA 1 ATOM 646 C C . SER A 1 136 ? 22.229 32.441 17.088 1.00 35.22 ? 129 SER A C 1 ATOM 647 O O . SER A 1 136 ? 21.916 33.621 16.864 1.00 35.13 ? 129 SER A O 1 ATOM 648 C CB . SER A 1 136 ? 20.436 30.798 16.981 1.00 33.84 ? 129 SER A CB 1 ATOM 649 O OG . SER A 1 136 ? 19.658 29.854 17.678 1.00 36.27 ? 129 SER A OG 1 ATOM 650 N N . ILE A 1 137 ? 23.310 31.857 16.586 1.00 36.69 ? 130 ILE A N 1 ATOM 651 C CA . ILE A 1 137 ? 23.949 32.354 15.381 1.00 38.81 ? 130 ILE A CA 1 ATOM 652 C C . ILE A 1 137 ? 23.343 31.485 14.279 1.00 40.79 ? 130 ILE A C 1 ATOM 653 O O . ILE A 1 137 ? 23.348 30.260 14.362 1.00 40.23 ? 130 ILE A O 1 ATOM 654 C CB . ILE A 1 137 ? 25.498 32.201 15.423 1.00 39.13 ? 130 ILE A CB 1 ATOM 655 C CG1 . ILE A 1 137 ? 26.119 33.092 16.527 1.00 38.19 ? 130 ILE A CG1 1 ATOM 656 C CG2 . ILE A 1 137 ? 26.112 32.433 14.023 1.00 38.16 ? 130 ILE A CG2 1 ATOM 657 C CD1 . ILE A 1 137 ? 27.636 32.904 16.662 1.00 36.62 ? 130 ILE A CD1 1 ATOM 658 N N . ILE A 1 138 ? 22.788 32.137 13.275 1.00 43.53 ? 131 ILE A N 1 ATOM 659 C CA . ILE A 1 138 ? 22.107 31.454 12.187 1.00 47.10 ? 131 ILE A CA 1 ATOM 660 C C . ILE A 1 138 ? 22.922 31.707 10.895 1.00 48.71 ? 131 ILE A C 1 ATOM 661 O O . ILE A 1 138 ? 23.403 32.820 10.691 1.00 48.45 ? 131 ILE A O 1 ATOM 662 C CB . ILE A 1 138 ? 20.605 31.929 12.187 1.00 47.30 ? 131 ILE A CB 1 ATOM 663 C CG1 . ILE A 1 138 ? 19.696 30.926 11.487 1.00 49.42 ? 131 ILE A CG1 1 ATOM 664 C CG2 . ILE A 1 138 ? 20.432 33.375 11.687 1.00 47.08 ? 131 ILE A CG2 1 ATOM 665 C CD1 . ILE A 1 138 ? 18.232 31.073 11.903 1.00 51.19 ? 131 ILE A CD1 1 ATOM 666 N N . ASN A 1 139 ? 23.162 30.678 10.071 1.00 51.55 ? 132 ASN A N 1 ATOM 667 C CA . ASN A 1 139 ? 23.859 30.894 8.780 1.00 53.84 ? 132 ASN A CA 1 ATOM 668 C C . ASN A 1 139 ? 22.929 31.388 7.643 1.00 56.09 ? 132 ASN A C 1 ATOM 669 O O . ASN A 1 139 ? 21.737 31.578 7.888 1.00 56.47 ? 132 ASN A O 1 ATOM 670 C CB . ASN A 1 139 ? 24.767 29.701 8.371 1.00 53.71 ? 132 ASN A CB 1 ATOM 671 C CG . ASN A 1 139 ? 23.998 28.413 8.084 1.00 52.53 ? 132 ASN A CG 1 ATOM 672 O OD1 . ASN A 1 139 ? 22.802 28.429 7.779 1.00 51.85 ? 132 ASN A OD1 1 ATOM 673 N ND2 . ASN A 1 139 ? 24.702 27.277 8.175 1.00 49.47 ? 132 ASN A ND2 1 ATOM 674 N N . GLU A 1 140 ? 23.469 31.607 6.430 1.00 58.40 ? 133 GLU A N 1 ATOM 675 C CA . GLU A 1 140 ? 22.673 32.042 5.246 1.00 60.60 ? 133 GLU A CA 1 ATOM 676 C C . GLU A 1 140 ? 21.457 31.163 4.893 1.00 61.72 ? 133 GLU A C 1 ATOM 677 O O . GLU A 1 140 ? 20.445 31.673 4.408 1.00 62.35 ? 133 GLU A O 1 ATOM 678 C CB . GLU A 1 140 ? 23.548 32.152 3.989 1.00 60.83 ? 133 GLU A CB 1 ATOM 679 C CG . GLU A 1 140 ? 23.701 33.564 3.460 0.20 60.27 ? 133 GLU A CG 1 ATOM 680 C CD . GLU A 1 140 ? 24.660 33.646 2.287 0.20 59.74 ? 133 GLU A CD 1 ATOM 681 O OE1 . GLU A 1 140 ? 24.360 34.388 1.332 0.20 58.95 ? 133 GLU A OE1 1 ATOM 682 O OE2 . GLU A 1 140 ? 25.712 32.977 2.322 0.20 58.59 ? 133 GLU A OE2 1 ATOM 683 N N . ASP A 1 141 ? 21.582 29.853 5.118 1.00 62.10 ? 134 ASP A N 1 ATOM 684 C CA . ASP A 1 141 ? 20.508 28.882 4.882 1.00 62.22 ? 134 ASP A CA 1 ATOM 685 C C . ASP A 1 141 ? 19.480 28.864 6.011 1.00 61.61 ? 134 ASP A C 1 ATOM 686 O O . ASP A 1 141 ? 18.425 28.241 5.905 1.00 62.13 ? 134 ASP A O 1 ATOM 687 C CB . ASP A 1 141 ? 21.118 27.499 4.696 0.50 62.65 ? 134 ASP A CB 1 ATOM 688 C CG . ASP A 1 141 ? 22.093 27.463 3.542 1.00 63.59 ? 134 ASP A CG 1 ATOM 689 O OD1 . ASP A 1 141 ? 21.831 28.158 2.540 1.00 64.85 ? 134 ASP A OD1 1 ATOM 690 O OD2 . ASP A 1 141 ? 23.125 26.762 3.629 1.00 63.98 ? 134 ASP A OD2 1 ATOM 691 N N . GLY A 1 142 ? 19.788 29.562 7.095 1.00 60.03 ? 135 GLY A N 1 ATOM 692 C CA . GLY A 1 142 ? 18.914 29.565 8.243 1.00 58.10 ? 135 GLY A CA 1 ATOM 693 C C . GLY A 1 142 ? 19.142 28.388 9.181 1.00 56.21 ? 135 GLY A C 1 ATOM 694 O O . GLY A 1 142 ? 18.261 28.069 9.984 1.00 56.85 ? 135 GLY A O 1 ATOM 695 N N . ASN A 1 143 ? 20.314 27.754 9.102 1.00 53.57 ? 136 ASN A N 1 ATOM 696 C CA . ASN A 1 143 ? 20.693 26.741 10.091 1.00 51.27 ? 136 ASN A CA 1 ATOM 697 C C . ASN A 1 143 ? 21.266 27.394 11.364 1.00 49.57 ? 136 ASN A C 1 ATOM 698 O O . ASN A 1 143 ? 22.178 28.222 11.286 1.00 49.10 ? 136 ASN A O 1 ATOM 699 C CB . ASN A 1 143 ? 21.700 25.758 9.521 0.50 51.00 ? 136 ASN A CB 1 ATOM 700 C CG . ASN A 1 143 ? 21.168 25.013 8.329 0.50 51.13 ? 136 ASN A CG 1 ATOM 701 O OD1 . ASN A 1 143 ? 21.915 24.345 7.654 0.75 51.16 ? 136 ASN A OD1 1 ATOM 702 N ND2 . ASN A 1 143 ? 19.876 25.123 8.065 0.75 50.56 ? 136 ASN A ND2 1 ATOM 703 N N . GLU A 1 144 ? 20.736 27.001 12.518 1.00 47.37 ? 137 GLU A N 1 ATOM 704 C CA . GLU A 1 144 ? 21.201 27.544 13.812 1.00 45.59 ? 137 GLU A CA 1 ATOM 705 C C . GLU A 1 144 ? 22.431 26.754 14.218 1.00 44.66 ? 137 GLU A C 1 ATOM 706 O O . GLU A 1 144 ? 22.340 25.593 14.638 1.00 44.38 ? 137 GLU A O 1 ATOM 707 C CB . GLU A 1 144 ? 20.087 27.489 14.856 1.00 45.01 ? 137 GLU A CB 1 ATOM 708 C CG . GLU A 1 144 ? 18.852 28.277 14.410 1.00 44.44 ? 137 GLU A CG 1 ATOM 709 C CD . GLU A 1 144 ? 17.782 28.417 15.477 1.00 42.90 ? 137 GLU A CD 1 ATOM 710 O OE1 . GLU A 1 144 ? 17.686 27.562 16.373 1.00 40.65 ? 137 GLU A OE1 1 ATOM 711 O OE2 . GLU A 1 144 ? 17.022 29.395 15.418 1.00 44.50 ? 137 GLU A OE2 1 ATOM 712 N N . ILE A 1 145 ? 23.589 27.382 14.039 1.00 43.46 ? 138 ILE A N 1 ATOM 713 C CA . ILE A 1 145 ? 24.885 26.704 14.183 1.00 41.93 ? 138 ILE A CA 1 ATOM 714 C C . ILE A 1 145 ? 25.480 26.831 15.591 1.00 41.07 ? 138 ILE A C 1 ATOM 715 O O . ILE A 1 145 ? 26.441 26.134 15.939 1.00 41.35 ? 138 ILE A O 1 ATOM 716 C CB . ILE A 1 145 ? 25.923 27.188 13.117 1.00 42.16 ? 138 ILE A CB 1 ATOM 717 C CG1 . ILE A 1 145 ? 26.197 28.700 13.246 1.00 41.25 ? 138 ILE A CG1 1 ATOM 718 C CG2 . ILE A 1 145 ? 25.490 26.743 11.691 1.00 40.66 ? 138 ILE A CG2 1 ATOM 719 C CD1 . ILE A 1 145 ? 27.461 29.165 12.467 1.00 44.20 ? 138 ILE A CD1 1 ATOM 720 N N . PHE A 1 146 ? 24.910 27.724 16.388 1.00 38.67 ? 139 PHE A N 1 ATOM 721 C CA . PHE A 1 146 ? 25.274 27.859 17.790 1.00 37.35 ? 139 PHE A CA 1 ATOM 722 C C . PHE A 1 146 ? 24.042 28.301 18.560 1.00 36.03 ? 139 PHE A C 1 ATOM 723 O O . PHE A 1 146 ? 23.332 29.195 18.112 1.00 34.97 ? 139 PHE A O 1 ATOM 724 C CB . PHE A 1 146 ? 26.402 28.896 17.997 1.00 37.42 ? 139 PHE A CB 1 ATOM 725 C CG . PHE A 1 146 ? 26.559 29.328 19.443 1.00 37.30 ? 139 PHE A CG 1 ATOM 726 C CD1 . PHE A 1 146 ? 27.179 28.485 20.370 1.00 37.34 ? 139 PHE A CD1 1 ATOM 727 C CD2 . PHE A 1 146 ? 26.058 30.556 19.884 1.00 35.91 ? 139 PHE A CD2 1 ATOM 728 C CE1 . PHE A 1 146 ? 27.297 28.876 21.728 1.00 37.06 ? 139 PHE A CE1 1 ATOM 729 C CE2 . PHE A 1 146 ? 26.174 30.936 21.226 1.00 35.97 ? 139 PHE A CE2 1 ATOM 730 C CZ . PHE A 1 146 ? 26.783 30.101 22.142 1.00 35.89 ? 139 PHE A CZ 1 ATOM 731 N N . ASN A 1 147 ? 23.804 27.677 19.714 1.00 35.26 ? 140 ASN A N 1 ATOM 732 C CA . ASN A 1 147 ? 22.684 28.020 20.584 1.00 34.45 ? 140 ASN A CA 1 ATOM 733 C C . ASN A 1 147 ? 23.184 28.348 21.964 1.00 33.22 ? 140 ASN A C 1 ATOM 734 O O . ASN A 1 147 ? 24.021 27.610 22.494 1.00 32.93 ? 140 ASN A O 1 ATOM 735 C CB . ASN A 1 147 ? 21.727 26.839 20.707 1.00 34.96 ? 140 ASN A CB 1 ATOM 736 C CG . ASN A 1 147 ? 20.971 26.556 19.423 1.00 37.55 ? 140 ASN A CG 1 ATOM 737 O OD1 . ASN A 1 147 ? 20.727 27.464 18.612 1.00 37.50 ? 140 ASN A OD1 1 ATOM 738 N ND2 . ASN A 1 147 ? 20.585 25.289 19.232 1.00 39.67 ? 140 ASN A ND2 1 ATOM 739 N N . THR A 1 148 ? 22.666 29.423 22.571 1.00 31.86 ? 141 THR A N 1 ATOM 740 C CA . THR A 1 148 ? 23.000 29.727 23.973 1.00 30.74 ? 141 THR A CA 1 ATOM 741 C C . THR A 1 148 ? 22.351 28.666 24.874 1.00 30.87 ? 141 THR A C 1 ATOM 742 O O . THR A 1 148 ? 21.479 27.915 24.422 1.00 30.73 ? 141 THR A O 1 ATOM 743 C CB . THR A 1 148 ? 22.560 31.151 24.391 1.00 30.62 ? 141 THR A CB 1 ATOM 744 O OG1 . THR A 1 148 ? 21.155 31.311 24.170 1.00 30.76 ? 141 THR A OG1 1 ATOM 745 C CG2 . THR A 1 148 ? 23.295 32.203 23.582 1.00 30.29 ? 141 THR A CG2 1 ATOM 746 N N . SER A 1 149 ? 22.746 28.622 26.143 1.00 31.03 ? 142 SER A N 1 ATOM 747 C CA . SER A 1 149 ? 22.256 27.603 27.068 1.00 31.06 ? 142 SER A CA 1 ATOM 748 C C . SER A 1 149 ? 20.748 27.731 27.414 1.00 31.34 ? 142 SER A C 1 ATOM 749 O O . SER A 1 149 ? 20.170 28.832 27.403 1.00 30.30 ? 142 SER A O 1 ATOM 750 C CB . SER A 1 149 ? 23.076 27.676 28.359 1.00 31.91 ? 142 SER A CB 1 ATOM 751 O OG A SER A 1 149 ? 22.547 28.655 29.268 0.50 28.17 ? 142 SER A OG 1 ATOM 752 O OG B SER A 1 149 ? 23.195 26.395 28.921 0.50 32.74 ? 142 SER A OG 1 ATOM 753 N N . LEU A 1 150 ? 20.132 26.605 27.753 1.00 30.97 ? 143 LEU A N 1 ATOM 754 C CA . LEU A 1 150 ? 18.719 26.610 28.166 1.00 31.96 ? 143 LEU A CA 1 ATOM 755 C C . LEU A 1 150 ? 18.539 26.809 29.684 1.00 31.19 ? 143 LEU A C 1 ATOM 756 O O . LEU A 1 150 ? 17.431 27.129 30.119 1.00 31.08 ? 143 LEU A O 1 ATOM 757 C CB . LEU A 1 150 ? 17.979 25.342 27.666 1.00 32.32 ? 143 LEU A CB 1 ATOM 758 C CG . LEU A 1 150 ? 17.920 25.154 26.138 1.00 33.99 ? 143 LEU A CG 1 ATOM 759 C CD1 . LEU A 1 150 ? 17.129 23.915 25.781 1.00 36.08 ? 143 LEU A CD1 1 ATOM 760 C CD2 . LEU A 1 150 ? 17.353 26.410 25.421 1.00 34.47 ? 143 LEU A CD2 1 ATOM 761 N N . PHE A 1 151 ? 19.630 26.647 30.457 1.00 30.21 ? 144 PHE A N 1 ATOM 762 C CA . PHE A 1 151 ? 19.626 26.749 31.939 1.00 29.88 ? 144 PHE A CA 1 ATOM 763 C C . PHE A 1 151 ? 21.066 26.855 32.442 1.00 28.14 ? 144 PHE A C 1 ATOM 764 O O . PHE A 1 151 ? 21.968 26.434 31.746 1.00 27.67 ? 144 PHE A O 1 ATOM 765 C CB . PHE A 1 151 ? 18.937 25.505 32.563 1.00 30.75 ? 144 PHE A CB 1 ATOM 766 C CG . PHE A 1 151 ? 19.603 24.178 32.185 1.00 33.58 ? 144 PHE A CG 1 ATOM 767 C CD1 . PHE A 1 151 ? 20.583 23.611 33.004 1.00 34.95 ? 144 PHE A CD1 1 ATOM 768 C CD2 . PHE A 1 151 ? 19.270 23.522 30.997 1.00 38.16 ? 144 PHE A CD2 1 ATOM 769 C CE1 . PHE A 1 151 ? 21.189 22.417 32.684 1.00 36.94 ? 144 PHE A CE1 1 ATOM 770 C CE2 . PHE A 1 151 ? 19.895 22.316 30.629 1.00 39.85 ? 144 PHE A CE2 1 ATOM 771 C CZ . PHE A 1 151 ? 20.857 21.755 31.480 1.00 39.94 ? 144 PHE A CZ 1 ATOM 772 N N . GLU A 1 152 ? 21.289 27.412 33.634 1.00 26.78 ? 145 GLU A N 1 ATOM 773 C CA . GLU A 1 152 ? 22.607 27.360 34.292 1.00 26.14 ? 145 GLU A CA 1 ATOM 774 C C . GLU A 1 152 ? 22.864 25.953 34.826 1.00 26.15 ? 145 GLU A C 1 ATOM 775 O O . GLU A 1 152 ? 21.955 25.357 35.404 1.00 25.72 ? 145 GLU A O 1 ATOM 776 C CB . GLU A 1 152 ? 22.656 28.297 35.505 1.00 25.70 ? 145 GLU A CB 1 ATOM 777 C CG . GLU A 1 152 ? 22.413 29.713 35.199 1.00 24.12 ? 145 GLU A CG 1 ATOM 778 C CD . GLU A 1 152 ? 22.425 30.542 36.474 1.00 23.57 ? 145 GLU A CD 1 ATOM 779 O OE1 . GLU A 1 152 ? 21.365 30.611 37.135 1.00 22.32 ? 145 GLU A OE1 1 ATOM 780 O OE2 . GLU A 1 152 ? 23.504 31.108 36.818 1.00 24.23 ? 145 GLU A OE2 1 ATOM 781 N N . PRO A 1 153 ? 24.084 25.419 34.640 1.00 26.83 ? 146 PRO A N 1 ATOM 782 C CA . PRO A 1 153 ? 24.393 24.142 35.252 1.00 26.67 ? 146 PRO A CA 1 ATOM 783 C C . PRO A 1 153 ? 24.135 24.252 36.766 1.00 26.93 ? 146 PRO A C 1 ATOM 784 O O . PRO A 1 153 ? 24.642 25.178 37.428 1.00 25.58 ? 146 PRO A O 1 ATOM 785 C CB . PRO A 1 153 ? 25.877 23.950 34.931 1.00 27.74 ? 146 PRO A CB 1 ATOM 786 C CG . PRO A 1 153 ? 26.084 24.688 33.635 1.00 27.86 ? 146 PRO A CG 1 ATOM 787 C CD . PRO A 1 153 ? 25.169 25.891 33.750 1.00 27.38 ? 146 PRO A CD 1 ATOM 788 N N . PRO A 1 154 ? 23.251 23.391 37.300 1.00 26.83 ? 147 PRO A N 1 ATOM 789 C CA . PRO A 1 154 ? 22.923 23.635 38.711 1.00 26.82 ? 147 PRO A CA 1 ATOM 790 C C . PRO A 1 154 ? 24.109 23.278 39.650 1.00 27.05 ? 147 PRO A C 1 ATOM 791 O O . PRO A 1 154 ? 24.918 22.382 39.322 1.00 25.41 ? 147 PRO A O 1 ATOM 792 C CB . PRO A 1 154 ? 21.738 22.701 38.963 1.00 27.44 ? 147 PRO A CB 1 ATOM 793 C CG . PRO A 1 154 ? 21.817 21.676 37.852 1.00 27.59 ? 147 PRO A CG 1 ATOM 794 C CD . PRO A 1 154 ? 22.354 22.418 36.673 1.00 26.76 ? 147 PRO A CD 1 ATOM 795 N N . PRO A 1 155 ? 24.200 23.967 40.811 1.00 27.16 ? 148 PRO A N 1 ATOM 796 C CA . PRO A 1 155 ? 25.318 23.732 41.737 1.00 27.49 ? 148 PRO A CA 1 ATOM 797 C C . PRO A 1 155 ? 25.274 22.331 42.411 1.00 27.37 ? 148 PRO A C 1 ATOM 798 O O . PRO A 1 155 ? 24.190 21.716 42.484 1.00 26.60 ? 148 PRO A O 1 ATOM 799 C CB . PRO A 1 155 ? 25.132 24.851 42.774 1.00 27.40 ? 148 PRO A CB 1 ATOM 800 C CG . PRO A 1 155 ? 23.680 25.204 42.730 1.00 27.97 ? 148 PRO A CG 1 ATOM 801 C CD . PRO A 1 155 ? 23.266 24.991 41.300 1.00 26.93 ? 148 PRO A CD 1 ATOM 802 N N . PRO A 1 156 ? 26.416 21.854 42.947 1.00 27.11 ? 149 PRO A N 1 ATOM 803 C CA . PRO A 1 156 ? 26.479 20.520 43.568 1.00 27.83 ? 149 PRO A CA 1 ATOM 804 C C . PRO A 1 156 ? 25.367 20.237 44.596 1.00 28.01 ? 149 PRO A C 1 ATOM 805 O O . PRO A 1 156 ? 25.128 21.050 45.518 1.00 26.45 ? 149 PRO A O 1 ATOM 806 C CB . PRO A 1 156 ? 27.849 20.521 44.240 1.00 27.83 ? 149 PRO A CB 1 ATOM 807 C CG . PRO A 1 156 ? 28.683 21.419 43.365 1.00 27.89 ? 149 PRO A CG 1 ATOM 808 C CD . PRO A 1 156 ? 27.739 22.522 42.970 1.00 28.02 ? 149 PRO A CD 1 ATOM 809 N N . GLY A 1 157 ? 24.665 19.118 44.405 1.00 28.59 ? 150 GLY A N 1 ATOM 810 C CA . GLY A 1 157 ? 23.597 18.736 45.325 1.00 31.12 ? 150 GLY A CA 1 ATOM 811 C C . GLY A 1 157 ? 22.222 19.356 45.046 1.00 32.93 ? 150 GLY A C 1 ATOM 812 O O . GLY A 1 157 ? 21.244 18.980 45.696 1.00 34.42 ? 150 GLY A O 1 ATOM 813 N N . TYR A 1 158 ? 22.146 20.280 44.086 1.00 33.61 ? 151 TYR A N 1 ATOM 814 C CA . TYR A 1 158 ? 20.879 20.914 43.655 1.00 35.09 ? 151 TYR A CA 1 ATOM 815 C C . TYR A 1 158 ? 20.481 20.530 42.216 1.00 37.32 ? 151 TYR A C 1 ATOM 816 O O . TYR A 1 158 ? 19.580 21.156 41.638 1.00 37.49 ? 151 TYR A O 1 ATOM 817 C CB . TYR A 1 158 ? 21.024 22.413 43.620 1.00 33.88 ? 151 TYR A CB 1 ATOM 818 C CG . TYR A 1 158 ? 21.264 23.091 44.938 1.00 30.36 ? 151 TYR A CG 1 ATOM 819 C CD1 . TYR A 1 158 ? 20.205 23.660 45.623 1.00 28.19 ? 151 TYR A CD1 1 ATOM 820 C CD2 . TYR A 1 158 ? 22.551 23.175 45.490 1.00 26.35 ? 151 TYR A CD2 1 ATOM 821 C CE1 . TYR A 1 158 ? 20.402 24.305 46.821 1.00 25.96 ? 151 TYR A CE1 1 ATOM 822 C CE2 . TYR A 1 158 ? 22.768 23.814 46.692 1.00 24.38 ? 151 TYR A CE2 1 ATOM 823 C CZ . TYR A 1 158 ? 21.680 24.380 47.344 1.00 24.57 ? 151 TYR A CZ 1 ATOM 824 O OH . TYR A 1 158 ? 21.825 25.027 48.505 1.00 23.73 ? 151 TYR A OH 1 ATOM 825 N N . GLU A 1 159 ? 21.199 19.583 41.619 1.00 38.53 ? 152 GLU A N 1 ATOM 826 C CA . GLU A 1 159 ? 20.973 19.176 40.239 0.80 41.12 ? 152 GLU A CA 1 ATOM 827 C C . GLU A 1 159 ? 19.583 18.495 40.032 0.80 42.61 ? 152 GLU A C 1 ATOM 828 O O . GLU A 1 159 ? 19.174 18.257 38.891 0.80 42.57 ? 152 GLU A O 1 ATOM 829 C CB . GLU A 1 159 ? 22.114 18.274 39.736 0.20 41.09 ? 152 GLU A CB 1 ATOM 830 C CG . GLU A 1 159 ? 23.530 18.857 39.859 0.30 42.03 ? 152 GLU A CG 1 ATOM 831 C CD . GLU A 1 159 ? 24.308 18.395 41.108 1.00 42.92 ? 152 GLU A CD 1 ATOM 832 O OE1 . GLU A 1 159 ? 23.715 17.910 42.088 1.00 40.85 ? 152 GLU A OE1 1 ATOM 833 O OE2 . GLU A 1 159 ? 25.556 18.521 41.110 1.00 45.25 ? 152 GLU A OE2 1 ATOM 834 N N . ASN A 1 160 ? 18.877 18.208 41.133 1.00 44.18 ? 153 ASN A N 1 ATOM 835 C CA . ASN A 1 160 ? 17.522 17.606 41.105 1.00 45.61 ? 153 ASN A CA 1 ATOM 836 C C . ASN A 1 160 ? 16.474 18.499 41.809 1.00 45.72 ? 153 ASN A C 1 ATOM 837 O O . ASN A 1 160 ? 15.374 18.058 42.135 1.00 46.47 ? 153 ASN A O 1 ATOM 838 C CB . ASN A 1 160 ? 17.543 16.203 41.734 1.00 46.30 ? 153 ASN A CB 1 ATOM 839 C CG . ASN A 1 160 ? 16.286 15.377 41.401 1.00 47.81 ? 153 ASN A CG 1 ATOM 840 O OD1 . ASN A 1 160 ? 16.001 15.084 40.232 1.00 50.03 ? 153 ASN A OD1 1 ATOM 841 N ND2 . ASN A 1 160 ? 15.542 14.995 42.439 1.00 48.32 ? 153 ASN A ND2 1 ATOM 842 N N . VAL A 1 161 ? 16.826 19.754 42.071 1.00 44.78 ? 154 VAL A N 1 ATOM 843 C CA . VAL A 1 161 ? 15.838 20.707 42.543 1.00 43.91 ? 154 VAL A CA 1 ATOM 844 C C . VAL A 1 161 ? 14.899 21.068 41.355 1.00 43.18 ? 154 VAL A C 1 ATOM 845 O O . VAL A 1 161 ? 15.341 21.339 40.224 1.00 43.26 ? 154 VAL A O 1 ATOM 846 C CB . VAL A 1 161 ? 16.499 21.949 43.213 1.00 44.13 ? 154 VAL A CB 1 ATOM 847 C CG1 . VAL A 1 161 ? 15.448 23.003 43.574 1.00 43.12 ? 154 VAL A CG1 1 ATOM 848 C CG2 . VAL A 1 161 ? 17.251 21.503 44.472 1.00 45.41 ? 154 VAL A CG2 1 ATOM 849 N N . SER A 1 162 ? 13.602 20.986 41.597 1.00 41.40 ? 155 SER A N 1 ATOM 850 C CA . SER A 1 162 ? 12.677 21.438 40.592 0.75 39.01 ? 155 SER A CA 1 ATOM 851 C C . SER A 1 162 ? 12.371 22.935 40.738 0.75 36.99 ? 155 SER A C 1 ATOM 852 O O . SER A 1 162 ? 12.585 23.595 41.806 0.75 36.00 ? 155 SER A O 1 ATOM 853 C CB . SER A 1 162 ? 11.388 20.600 40.632 0.20 38.98 ? 155 SER A CB 1 ATOM 854 O OG . SER A 1 162 ? 10.881 20.529 41.948 0.20 38.41 ? 155 SER A OG 1 ATOM 855 N N . ASP A 1 163 ? 11.872 23.467 39.635 1.00 34.63 ? 156 ASP A N 1 ATOM 856 C CA . ASP A 1 163 ? 11.299 24.772 39.638 1.00 32.06 ? 156 ASP A CA 1 ATOM 857 C C . ASP A 1 163 ? 12.386 25.828 39.757 1.00 29.10 ? 156 ASP A C 1 ATOM 858 O O . ASP A 1 163 ? 12.120 26.909 40.301 1.00 28.23 ? 156 ASP A O 1 ATOM 859 C CB . ASP A 1 163 ? 10.322 24.913 40.813 1.00 33.60 ? 156 ASP A CB 1 ATOM 860 C CG . ASP A 1 163 ? 9.111 23.975 40.700 0.80 37.75 ? 156 ASP A CG 1 ATOM 861 O OD1 . ASP A 1 163 ? 8.642 23.699 39.572 0.80 41.76 ? 156 ASP A OD1 1 ATOM 862 O OD2 . ASP A 1 163 ? 8.635 23.508 41.751 0.80 41.60 ? 156 ASP A OD2 1 ATOM 863 N N . ILE A 1 164 ? 13.583 25.548 39.231 1.00 26.13 ? 157 ILE A N 1 ATOM 864 C CA . ILE A 1 164 ? 14.573 26.627 39.078 1.00 24.49 ? 157 ILE A CA 1 ATOM 865 C C . ILE A 1 164 ? 14.208 27.405 37.790 1.00 24.86 ? 157 ILE A C 1 ATOM 866 O O . ILE A 1 164 ? 14.280 26.826 36.689 1.00 25.74 ? 157 ILE A O 1 ATOM 867 C CB . ILE A 1 164 ? 16.041 26.112 39.034 1.00 23.70 ? 157 ILE A CB 1 ATOM 868 C CG1 . ILE A 1 164 ? 16.443 25.489 40.386 1.00 22.36 ? 157 ILE A CG1 1 ATOM 869 C CG2 . ILE A 1 164 ? 17.015 27.283 38.691 1.00 21.61 ? 157 ILE A CG2 1 ATOM 870 C CD1 . ILE A 1 164 ? 17.745 24.609 40.331 1.00 22.10 ? 157 ILE A CD1 1 ATOM 871 N N . VAL A 1 165 ? 13.781 28.668 37.915 1.00 23.09 ? 158 VAL A N 1 ATOM 872 C CA . VAL A 1 165 ? 13.450 29.434 36.727 1.00 22.36 ? 158 VAL A CA 1 ATOM 873 C C . VAL A 1 165 ? 14.722 29.612 35.873 1.00 23.01 ? 158 VAL A C 1 ATOM 874 O O . VAL A 1 165 ? 15.738 30.058 36.404 1.00 23.17 ? 158 VAL A O 1 ATOM 875 C CB . VAL A 1 165 ? 12.710 30.807 37.051 1.00 21.99 ? 158 VAL A CB 1 ATOM 876 C CG1 . VAL A 1 165 ? 13.708 31.960 37.578 1.00 19.76 ? 158 VAL A CG1 1 ATOM 877 C CG2 . VAL A 1 165 ? 11.957 31.253 35.842 1.00 21.57 ? 158 VAL A CG2 1 ATOM 878 N N . PRO A 1 166 ? 14.677 29.260 34.560 1.00 23.74 ? 159 PRO A N 1 ATOM 879 C CA . PRO A 1 166 ? 15.889 29.482 33.735 1.00 23.85 ? 159 PRO A CA 1 ATOM 880 C C . PRO A 1 166 ? 16.160 30.962 33.608 1.00 23.32 ? 159 PRO A C 1 ATOM 881 O O . PRO A 1 166 ? 15.242 31.782 33.789 1.00 23.15 ? 159 PRO A O 1 ATOM 882 C CB . PRO A 1 166 ? 15.522 28.875 32.344 1.00 23.74 ? 159 PRO A CB 1 ATOM 883 C CG . PRO A 1 166 ? 14.028 28.838 32.339 1.00 25.34 ? 159 PRO A CG 1 ATOM 884 C CD . PRO A 1 166 ? 13.601 28.608 33.789 1.00 23.61 ? 159 PRO A CD 1 ATOM 885 N N . PRO A 1 167 ? 17.417 31.326 33.309 1.00 22.70 ? 160 PRO A N 1 ATOM 886 C CA . PRO A 1 167 ? 17.649 32.756 33.136 1.00 22.14 ? 160 PRO A CA 1 ATOM 887 C C . PRO A 1 167 ? 16.729 33.383 32.066 1.00 20.79 ? 160 PRO A C 1 ATOM 888 O O . PRO A 1 167 ? 16.538 32.814 31.002 1.00 20.50 ? 160 PRO A O 1 ATOM 889 C CB . PRO A 1 167 ? 19.102 32.811 32.637 1.00 20.98 ? 160 PRO A CB 1 ATOM 890 C CG . PRO A 1 167 ? 19.727 31.558 33.244 1.00 22.21 ? 160 PRO A CG 1 ATOM 891 C CD . PRO A 1 167 ? 18.644 30.530 33.101 1.00 22.96 ? 160 PRO A CD 1 ATOM 892 N N . PHE A 1 168 ? 16.260 34.586 32.338 1.00 19.56 ? 161 PHE A N 1 ATOM 893 C CA . PHE A 1 168 ? 15.446 35.341 31.415 1.00 19.48 ? 161 PHE A CA 1 ATOM 894 C C . PHE A 1 168 ? 15.398 36.766 31.924 1.00 19.22 ? 161 PHE A C 1 ATOM 895 O O . PHE A 1 168 ? 15.724 37.028 33.108 1.00 18.60 ? 161 PHE A O 1 ATOM 896 C CB . PHE A 1 168 ? 14.002 34.756 31.343 1.00 20.34 ? 161 PHE A CB 1 ATOM 897 C CG . PHE A 1 168 ? 13.102 35.112 32.540 1.00 21.38 ? 161 PHE A CG 1 ATOM 898 C CD1 . PHE A 1 168 ? 11.914 35.889 32.357 1.00 20.62 ? 161 PHE A CD1 1 ATOM 899 C CD2 . PHE A 1 168 ? 13.363 34.602 33.825 1.00 21.14 ? 161 PHE A CD2 1 ATOM 900 C CE1 . PHE A 1 168 ? 11.014 36.174 33.448 1.00 19.86 ? 161 PHE A CE1 1 ATOM 901 C CE2 . PHE A 1 168 ? 12.491 34.883 34.925 1.00 21.68 ? 161 PHE A CE2 1 ATOM 902 C CZ . PHE A 1 168 ? 11.309 35.698 34.759 1.00 20.16 ? 161 PHE A CZ 1 ATOM 903 N N . SER A 1 169 ? 14.982 37.679 31.038 1.00 19.21 ? 162 SER A N 1 ATOM 904 C CA . SER A 1 169 ? 14.750 39.064 31.394 1.00 19.26 ? 162 SER A CA 1 ATOM 905 C C . SER A 1 169 ? 13.274 39.290 31.654 1.00 19.42 ? 162 SER A C 1 ATOM 906 O O . SER A 1 169 ? 12.487 39.309 30.710 1.00 19.48 ? 162 SER A O 1 ATOM 907 C CB . SER A 1 169 ? 15.261 39.982 30.279 1.00 19.36 ? 162 SER A CB 1 ATOM 908 O OG . SER A 1 169 ? 16.695 39.846 30.159 1.00 21.09 ? 162 SER A OG 1 ATOM 909 N N . ALA A 1 170 ? 12.887 39.494 32.925 1.00 19.00 ? 163 ALA A N 1 ATOM 910 C CA . ALA A 1 170 ? 11.430 39.607 33.230 1.00 18.24 ? 163 ALA A CA 1 ATOM 911 C C . ALA A 1 170 ? 10.856 40.822 32.518 1.00 19.08 ? 163 ALA A C 1 ATOM 912 O O . ALA A 1 170 ? 11.455 41.915 32.561 1.00 18.14 ? 163 ALA A O 1 ATOM 913 C CB . ALA A 1 170 ? 11.152 39.700 34.751 1.00 16.59 ? 163 ALA A CB 1 ATOM 914 N N . PHE A 1 171 ? 9.693 40.586 31.876 1.00 19.88 ? 164 PHE A N 1 ATOM 915 C CA . PHE A 1 171 ? 8.851 41.566 31.121 1.00 20.62 ? 164 PHE A CA 1 ATOM 916 C C . PHE A 1 171 ? 9.305 41.804 29.680 1.00 21.74 ? 164 PHE A C 1 ATOM 917 O O . PHE A 1 171 ? 8.717 42.631 28.993 1.00 22.73 ? 164 PHE A O 1 ATOM 918 C CB . PHE A 1 171 ? 8.647 42.885 31.854 1.00 19.33 ? 164 PHE A CB 1 ATOM 919 C CG . PHE A 1 171 ? 7.989 42.711 33.234 1.00 21.42 ? 164 PHE A CG 1 ATOM 920 C CD1 . PHE A 1 171 ? 6.598 42.513 33.338 1.00 19.38 ? 164 PHE A CD1 1 ATOM 921 C CD2 . PHE A 1 171 ? 8.791 42.708 34.406 1.00 17.26 ? 164 PHE A CD2 1 ATOM 922 C CE1 . PHE A 1 171 ? 5.987 42.361 34.579 1.00 18.92 ? 164 PHE A CE1 1 ATOM 923 C CE2 . PHE A 1 171 ? 8.220 42.552 35.651 1.00 19.78 ? 164 PHE A CE2 1 ATOM 924 C CZ . PHE A 1 171 ? 6.783 42.358 35.762 1.00 18.84 ? 164 PHE A CZ 1 ATOM 925 N N . SER A 1 172 ? 10.316 41.076 29.216 1.00 21.47 ? 165 SER A N 1 ATOM 926 C CA . SER A 1 172 ? 10.605 41.064 27.776 1.00 22.84 ? 165 SER A CA 1 ATOM 927 C C . SER A 1 172 ? 9.353 40.720 26.989 1.00 23.92 ? 165 SER A C 1 ATOM 928 O O . SER A 1 172 ? 8.616 39.784 27.367 1.00 23.30 ? 165 SER A O 1 ATOM 929 C CB . SER A 1 172 ? 11.706 40.059 27.397 1.00 23.23 ? 165 SER A CB 1 ATOM 930 O OG . SER A 1 172 ? 11.910 40.029 25.963 1.00 22.76 ? 165 SER A OG 1 ATOM 931 N N . PRO A 1 173 ? 9.097 41.464 25.889 1.00 24.70 ? 166 PRO A N 1 ATOM 932 C CA . PRO A 1 173 ? 8.050 41.007 24.996 1.00 25.60 ? 166 PRO A CA 1 ATOM 933 C C . PRO A 1 173 ? 8.524 39.762 24.241 1.00 26.48 ? 166 PRO A C 1 ATOM 934 O O . PRO A 1 173 ? 9.718 39.423 24.276 1.00 26.17 ? 166 PRO A O 1 ATOM 935 C CB . PRO A 1 173 ? 7.882 42.190 24.020 1.00 26.59 ? 166 PRO A CB 1 ATOM 936 C CG . PRO A 1 173 ? 9.286 42.791 23.929 1.00 24.90 ? 166 PRO A CG 1 ATOM 937 C CD . PRO A 1 173 ? 9.724 42.713 25.406 1.00 24.64 ? 166 PRO A CD 1 ATOM 938 N N . GLN A 1 174 ? 7.595 39.071 23.597 1.00 28.04 ? 167 GLN A N 1 ATOM 939 C CA . GLN A 1 174 ? 7.900 37.932 22.708 1.00 29.71 ? 167 GLN A CA 1 ATOM 940 C C . GLN A 1 174 ? 8.451 38.402 21.382 1.00 30.63 ? 167 GLN A C 1 ATOM 941 O O . GLN A 1 174 ? 8.155 39.519 20.947 1.00 30.84 ? 167 GLN A O 1 ATOM 942 C CB . GLN A 1 174 ? 6.635 37.098 22.454 1.00 30.23 ? 167 GLN A CB 1 ATOM 943 C CG . GLN A 1 174 ? 6.089 36.462 23.754 1.00 32.13 ? 167 GLN A CG 1 ATOM 944 C CD . GLN A 1 174 ? 4.792 35.670 23.562 1.00 37.83 ? 167 GLN A CD 1 ATOM 945 O OE1 . GLN A 1 174 ? 4.277 35.586 22.470 1.00 39.60 ? 167 GLN A OE1 1 ATOM 946 N NE2 . GLN A 1 174 ? 4.267 35.094 24.649 1.00 38.97 ? 167 GLN A NE2 1 ATOM 947 N N . GLY A 1 175 ? 9.269 37.563 20.740 1.00 31.14 ? 168 GLY A N 1 ATOM 948 C CA . GLY A 1 175 ? 9.701 37.848 19.378 1.00 32.49 ? 168 GLY A CA 1 ATOM 949 C C . GLY A 1 175 ? 10.840 36.931 18.962 1.00 33.67 ? 168 GLY A C 1 ATOM 950 O O . GLY A 1 175 ? 11.469 36.262 19.802 1.00 32.90 ? 168 GLY A O 1 ATOM 951 N N . MET A 1 176 ? 11.101 36.894 17.662 1.00 34.42 ? 169 MET A N 1 ATOM 952 C CA . MET A 1 176 ? 12.239 36.166 17.161 1.00 35.48 ? 169 MET A CA 1 ATOM 953 C C . MET A 1 176 ? 13.050 37.050 16.220 1.00 35.39 ? 169 MET A C 1 ATOM 954 O O . MET A 1 176 ? 13.308 36.645 15.097 1.00 34.75 ? 169 MET A O 1 ATOM 955 C CB . MET A 1 176 ? 11.779 34.879 16.454 1.00 36.02 ? 169 MET A CB 1 ATOM 956 C CG . MET A 1 176 ? 11.105 33.853 17.367 1.00 41.64 ? 169 MET A CG 1 ATOM 957 S SD . MET A 1 176 ? 10.986 32.289 16.498 1.00 53.37 ? 169 MET A SD 1 ATOM 958 C CE . MET A 1 176 ? 9.894 31.340 17.569 1.00 53.42 ? 169 MET A CE 1 ATOM 959 N N . PRO A 1 177 ? 13.485 38.242 16.675 1.00 35.33 ? 170 PRO A N 1 ATOM 960 C CA . PRO A 1 177 ? 14.236 39.082 15.735 1.00 35.74 ? 170 PRO A CA 1 ATOM 961 C C . PRO A 1 177 ? 15.601 38.486 15.322 1.00 36.60 ? 170 PRO A C 1 ATOM 962 O O . PRO A 1 177 ? 16.288 37.815 16.129 1.00 36.17 ? 170 PRO A O 1 ATOM 963 C CB . PRO A 1 177 ? 14.445 40.377 16.508 1.00 35.15 ? 170 PRO A CB 1 ATOM 964 C CG . PRO A 1 177 ? 14.466 39.930 17.968 1.00 34.90 ? 170 PRO A CG 1 ATOM 965 C CD . PRO A 1 177 ? 13.478 38.801 18.040 1.00 35.44 ? 170 PRO A CD 1 ATOM 966 N N . GLU A 1 178 ? 15.969 38.756 14.068 1.00 37.47 ? 171 GLU A N 1 ATOM 967 C CA . GLU A 1 178 ? 17.179 38.250 13.438 1.00 38.22 ? 171 GLU A CA 1 ATOM 968 C C . GLU A 1 178 ? 17.903 39.486 12.937 1.00 39.47 ? 171 GLU A C 1 ATOM 969 O O . GLU A 1 178 ? 17.263 40.388 12.383 1.00 41.03 ? 171 GLU A O 1 ATOM 970 C CB . GLU A 1 178 ? 16.785 37.365 12.239 1.00 37.98 ? 171 GLU A CB 1 ATOM 971 C CG . GLU A 1 178 ? 17.871 36.564 11.656 0.30 35.18 ? 171 GLU A CG 1 ATOM 972 C CD . GLU A 1 178 ? 17.382 35.886 10.430 0.30 33.87 ? 171 GLU A CD 1 ATOM 973 O OE1 . GLU A 1 178 ? 16.480 35.033 10.567 0.30 31.10 ? 171 GLU A OE1 1 ATOM 974 O OE2 . GLU A 1 178 ? 17.875 36.246 9.344 0.30 32.28 ? 171 GLU A OE2 1 ATOM 975 N N . GLY A 1 179 ? 19.216 39.564 13.110 1.00 38.97 ? 172 GLY A N 1 ATOM 976 C CA . GLY A 1 179 ? 19.921 40.772 12.687 1.00 38.59 ? 172 GLY A CA 1 ATOM 977 C C . GLY A 1 179 ? 21.406 40.747 12.944 1.00 37.94 ? 172 GLY A C 1 ATOM 978 O O . GLY A 1 179 ? 21.956 39.723 13.334 1.00 37.79 ? 172 GLY A O 1 ATOM 979 N N . ASP A 1 180 ? 22.053 41.886 12.719 1.00 37.53 ? 173 ASP A N 1 ATOM 980 C CA . ASP A 1 180 ? 23.497 42.012 12.945 1.00 36.96 ? 173 ASP A CA 1 ATOM 981 C C . ASP A 1 180 ? 23.737 42.620 14.314 1.00 35.44 ? 173 ASP A C 1 ATOM 982 O O . ASP A 1 180 ? 22.979 43.500 14.752 1.00 34.28 ? 173 ASP A O 1 ATOM 983 C CB . ASP A 1 180 ? 24.114 42.933 11.920 1.00 37.27 ? 173 ASP A CB 1 ATOM 984 C CG . ASP A 1 180 ? 24.065 42.364 10.525 1.00 40.62 ? 173 ASP A CG 1 ATOM 985 O OD1 . ASP A 1 180 ? 24.314 41.151 10.364 1.00 43.95 ? 173 ASP A OD1 1 ATOM 986 O OD2 . ASP A 1 180 ? 23.786 43.145 9.593 1.00 43.35 ? 173 ASP A OD2 1 ATOM 987 N N . LEU A 1 181 ? 24.810 42.173 14.954 1.00 34.40 ? 174 LEU A N 1 ATOM 988 C CA . LEU A 1 181 ? 25.141 42.631 16.289 1.00 34.27 ? 174 LEU A CA 1 ATOM 989 C C . LEU A 1 181 ? 25.890 43.950 16.275 1.00 34.05 ? 174 LEU A C 1 ATOM 990 O O . LEU A 1 181 ? 26.757 44.168 15.420 1.00 34.22 ? 174 LEU A O 1 ATOM 991 C CB . LEU A 1 181 ? 26.021 41.563 16.949 1.00 34.63 ? 174 LEU A CB 1 ATOM 992 C CG A LEU A 1 181 ? 25.784 41.104 18.384 0.50 33.69 ? 174 LEU A CG 1 ATOM 993 C CG B LEU A 1 181 ? 25.417 40.216 17.346 0.50 32.87 ? 174 LEU A CG 1 ATOM 994 C CD1 A LEU A 1 181 ? 24.321 40.740 18.670 0.50 33.43 ? 174 LEU A CD1 1 ATOM 995 C CD1 B LEU A 1 181 ? 26.478 39.395 18.042 0.50 31.27 ? 174 LEU A CD1 1 ATOM 996 C CD2 A LEU A 1 181 ? 26.696 39.911 18.648 0.50 32.01 ? 174 LEU A CD2 1 ATOM 997 C CD2 B LEU A 1 181 ? 24.194 40.408 18.260 0.50 31.63 ? 174 LEU A CD2 1 ATOM 998 N N . VAL A 1 182 ? 25.567 44.815 17.230 1.00 33.61 ? 175 VAL A N 1 ATOM 999 C CA . VAL A 1 182 ? 26.433 45.926 17.611 1.00 33.58 ? 175 VAL A CA 1 ATOM 1000 C C . VAL A 1 182 ? 26.738 45.784 19.119 1.00 33.14 ? 175 VAL A C 1 ATOM 1001 O O . VAL A 1 182 ? 25.829 45.554 19.943 1.00 32.00 ? 175 VAL A O 1 ATOM 1002 C CB . VAL A 1 182 ? 25.772 47.324 17.322 1.00 34.50 ? 175 VAL A CB 1 ATOM 1003 C CG1 . VAL A 1 182 ? 26.590 48.468 17.900 1.00 33.94 ? 175 VAL A CG1 1 ATOM 1004 C CG2 . VAL A 1 182 ? 25.625 47.529 15.845 1.00 34.71 ? 175 VAL A CG2 1 ATOM 1005 N N . TYR A 1 183 ? 28.015 45.920 19.470 1.00 32.01 ? 176 TYR A N 1 ATOM 1006 C CA . TYR A 1 183 ? 28.427 45.873 20.863 1.00 30.93 ? 176 TYR A CA 1 ATOM 1007 C C . TYR A 1 183 ? 28.477 47.300 21.428 1.00 30.77 ? 176 TYR A C 1 ATOM 1008 O O . TYR A 1 183 ? 29.106 48.183 20.843 1.00 30.04 ? 176 TYR A O 1 ATOM 1009 C CB . TYR A 1 183 ? 29.786 45.182 20.976 1.00 30.78 ? 176 TYR A CB 1 ATOM 1010 C CG . TYR A 1 183 ? 30.463 45.338 22.321 1.00 30.20 ? 176 TYR A CG 1 ATOM 1011 C CD1 . TYR A 1 183 ? 29.898 44.787 23.473 1.00 29.93 ? 176 TYR A CD1 1 ATOM 1012 C CD2 . TYR A 1 183 ? 31.663 46.043 22.435 1.00 30.29 ? 176 TYR A CD2 1 ATOM 1013 C CE1 . TYR A 1 183 ? 30.500 44.946 24.733 1.00 30.98 ? 176 TYR A CE1 1 ATOM 1014 C CE2 . TYR A 1 183 ? 32.283 46.210 23.676 1.00 31.16 ? 176 TYR A CE2 1 ATOM 1015 C CZ . TYR A 1 183 ? 31.712 45.651 24.821 1.00 30.82 ? 176 TYR A CZ 1 ATOM 1016 O OH . TYR A 1 183 ? 32.323 45.787 26.058 1.00 28.74 ? 176 TYR A OH 1 ATOM 1017 N N . VAL A 1 184 ? 27.833 47.509 22.575 1.00 30.40 ? 177 VAL A N 1 ATOM 1018 C CA . VAL A 1 184 ? 27.560 48.864 23.069 1.00 29.81 ? 177 VAL A CA 1 ATOM 1019 C C . VAL A 1 184 ? 28.114 49.074 24.479 1.00 29.67 ? 177 VAL A C 1 ATOM 1020 O O . VAL A 1 184 ? 27.609 49.914 25.244 1.00 29.13 ? 177 VAL A O 1 ATOM 1021 C CB . VAL A 1 184 ? 26.026 49.191 23.042 1.00 29.66 ? 177 VAL A CB 1 ATOM 1022 C CG1 . VAL A 1 184 ? 25.476 49.034 21.620 1.00 26.87 ? 177 VAL A CG1 1 ATOM 1023 C CG2 . VAL A 1 184 ? 25.224 48.255 24.021 1.00 29.72 ? 177 VAL A CG2 1 ATOM 1024 N N . ASN A 1 185 ? 29.144 48.297 24.824 1.00 29.21 ? 178 ASN A N 1 ATOM 1025 C CA . ASN A 1 185 ? 29.800 48.428 26.123 1.00 28.35 ? 178 ASN A CA 1 ATOM 1026 C C . ASN A 1 185 ? 28.761 48.193 27.226 1.00 27.50 ? 178 ASN A C 1 ATOM 1027 O O . ASN A 1 185 ? 28.062 47.172 27.187 1.00 27.53 ? 178 ASN A O 1 ATOM 1028 C CB . ASN A 1 185 ? 30.535 49.795 26.234 1.00 28.20 ? 178 ASN A CB 1 ATOM 1029 C CG . ASN A 1 185 ? 31.647 49.792 27.282 1.00 28.11 ? 178 ASN A CG 1 ATOM 1030 O OD1 . ASN A 1 185 ? 32.136 48.733 27.678 1.00 26.81 ? 178 ASN A OD1 1 ATOM 1031 N ND2 . ASN A 1 185 ? 32.048 50.982 27.735 1.00 26.89 ? 178 ASN A ND2 1 ATOM 1032 N N . TYR A 1 186 ? 28.627 49.116 28.188 1.00 26.34 ? 179 TYR A N 1 ATOM 1033 C CA . TYR A 1 186 ? 27.631 48.963 29.263 1.00 25.51 ? 179 TYR A CA 1 ATOM 1034 C C . TYR A 1 186 ? 26.219 49.478 28.912 1.00 25.32 ? 179 TYR A C 1 ATOM 1035 O O . TYR A 1 186 ? 25.345 49.487 29.773 1.00 24.82 ? 179 TYR A O 1 ATOM 1036 C CB . TYR A 1 186 ? 28.108 49.638 30.583 1.00 24.16 ? 179 TYR A CB 1 ATOM 1037 C CG . TYR A 1 186 ? 29.373 49.039 31.172 1.00 24.71 ? 179 TYR A CG 1 ATOM 1038 C CD1 . TYR A 1 186 ? 29.349 47.824 31.887 1.00 22.42 ? 179 TYR A CD1 1 ATOM 1039 C CD2 . TYR A 1 186 ? 30.604 49.707 31.044 1.00 25.37 ? 179 TYR A CD2 1 ATOM 1040 C CE1 . TYR A 1 186 ? 30.523 47.292 32.456 1.00 24.80 ? 179 TYR A CE1 1 ATOM 1041 C CE2 . TYR A 1 186 ? 31.774 49.178 31.591 1.00 24.39 ? 179 TYR A CE2 1 ATOM 1042 C CZ . TYR A 1 186 ? 31.737 47.994 32.304 1.00 24.99 ? 179 TYR A CZ 1 ATOM 1043 O OH . TYR A 1 186 ? 32.918 47.516 32.838 1.00 25.85 ? 179 TYR A OH 1 ATOM 1044 N N . ALA A 1 187 ? 26.011 49.899 27.660 1.00 25.62 ? 180 ALA A N 1 ATOM 1045 C CA . ALA A 1 187 ? 24.727 50.466 27.213 1.00 26.25 ? 180 ALA A CA 1 ATOM 1046 C C . ALA A 1 187 ? 24.290 51.702 28.044 1.00 25.89 ? 180 ALA A C 1 ATOM 1047 O O . ALA A 1 187 ? 23.087 51.959 28.217 1.00 26.18 ? 180 ALA A O 1 ATOM 1048 C CB . ALA A 1 187 ? 23.603 49.390 27.188 1.00 25.33 ? 180 ALA A CB 1 ATOM 1049 N N . ARG A 1 188 ? 25.274 52.470 28.523 1.00 25.76 ? 181 ARG A N 1 ATOM 1050 C CA . ARG A 1 188 ? 24.984 53.690 29.307 1.00 25.17 ? 181 ARG A CA 1 ATOM 1051 C C . ARG A 1 188 ? 24.654 54.810 28.328 1.00 25.23 ? 181 ARG A C 1 ATOM 1052 O O . ARG A 1 188 ? 24.956 54.710 27.133 1.00 24.34 ? 181 ARG A O 1 ATOM 1053 C CB . ARG A 1 188 ? 26.196 54.110 30.143 1.00 24.32 ? 181 ARG A CB 1 ATOM 1054 C CG . ARG A 1 188 ? 26.543 53.114 31.273 1.00 24.38 ? 181 ARG A CG 1 ATOM 1055 C CD . ARG A 1 188 ? 27.886 53.412 31.844 1.00 23.74 ? 181 ARG A CD 1 ATOM 1056 N NE . ARG A 1 188 ? 28.919 53.266 30.819 1.00 23.57 ? 181 ARG A NE 1 ATOM 1057 C CZ . ARG A 1 188 ? 30.228 53.403 31.023 1.00 26.63 ? 181 ARG A CZ 1 ATOM 1058 N NH1 . ARG A 1 188 ? 30.720 53.680 32.229 1.00 27.13 ? 181 ARG A NH1 1 ATOM 1059 N NH2 . ARG A 1 188 ? 31.052 53.273 30.002 1.00 27.94 ? 181 ARG A NH2 1 ATOM 1060 N N . THR A 1 189 ? 24.033 55.867 28.833 1.00 25.03 ? 182 THR A N 1 ATOM 1061 C CA . THR A 1 189 ? 23.833 57.057 28.016 1.00 26.18 ? 182 THR A CA 1 ATOM 1062 C C . THR A 1 189 ? 25.133 57.480 27.295 1.00 26.62 ? 182 THR A C 1 ATOM 1063 O O . THR A 1 189 ? 25.117 57.733 26.073 1.00 26.34 ? 182 THR A O 1 ATOM 1064 C CB . THR A 1 189 ? 23.273 58.211 28.873 1.00 25.53 ? 182 THR A CB 1 ATOM 1065 O OG1 . THR A 1 189 ? 22.013 57.787 29.412 1.00 26.22 ? 182 THR A OG1 1 ATOM 1066 C CG2 . THR A 1 189 ? 23.048 59.464 28.024 1.00 25.96 ? 182 THR A CG2 1 ATOM 1067 N N . GLU A 1 190 ? 26.251 57.544 28.027 1.00 27.99 ? 183 GLU A N 1 ATOM 1068 C CA . GLU A 1 190 ? 27.518 58.001 27.415 1.00 30.25 ? 183 GLU A CA 1 ATOM 1069 C C . GLU A 1 190 ? 28.071 57.001 26.365 1.00 30.10 ? 183 GLU A C 1 ATOM 1070 O O . GLU A 1 190 ? 28.776 57.394 25.424 1.00 30.25 ? 183 GLU A O 1 ATOM 1071 C CB . GLU A 1 190 ? 28.571 58.372 28.465 1.00 30.55 ? 183 GLU A CB 1 ATOM 1072 C CG . GLU A 1 190 ? 29.025 57.222 29.324 1.00 33.90 ? 183 GLU A CG 1 ATOM 1073 C CD . GLU A 1 190 ? 28.266 57.178 30.661 1.00 35.45 ? 183 GLU A CD 1 ATOM 1074 O OE1 . GLU A 1 190 ? 27.010 57.465 30.702 1.00 34.35 ? 183 GLU A OE1 1 ATOM 1075 O OE2 . GLU A 1 190 ? 28.962 56.867 31.661 1.00 35.67 ? 183 GLU A OE2 1 ATOM 1076 N N . ASP A 1 191 ? 27.718 55.723 26.513 1.00 30.10 ? 184 ASP A N 1 ATOM 1077 C CA . ASP A 1 191 ? 28.170 54.707 25.541 1.00 30.31 ? 184 ASP A CA 1 ATOM 1078 C C . ASP A 1 191 ? 27.439 54.928 24.215 1.00 30.57 ? 184 ASP A C 1 ATOM 1079 O O . ASP A 1 191 ? 28.063 54.904 23.141 1.00 31.03 ? 184 ASP A O 1 ATOM 1080 C CB . ASP A 1 191 ? 27.902 53.289 26.077 1.00 30.17 ? 184 ASP A CB 1 ATOM 1081 C CG . ASP A 1 191 ? 28.742 52.952 27.277 1.00 28.02 ? 184 ASP A CG 1 ATOM 1082 O OD1 . ASP A 1 191 ? 29.916 53.381 27.328 1.00 27.41 ? 184 ASP A OD1 1 ATOM 1083 O OD2 . ASP A 1 191 ? 28.233 52.238 28.165 1.00 24.52 ? 184 ASP A OD2 1 ATOM 1084 N N . PHE A 1 192 ? 26.120 55.182 24.302 1.00 30.68 ? 185 PHE A N 1 ATOM 1085 C CA . PHE A 1 192 ? 25.337 55.533 23.118 1.00 30.06 ? 185 PHE A CA 1 ATOM 1086 C C . PHE A 1 192 ? 25.743 56.875 22.501 1.00 31.10 ? 185 PHE A C 1 ATOM 1087 O O . PHE A 1 192 ? 25.855 56.964 21.268 1.00 30.78 ? 185 PHE A O 1 ATOM 1088 C CB . PHE A 1 192 ? 23.829 55.410 23.361 1.00 28.97 ? 185 PHE A CB 1 ATOM 1089 C CG . PHE A 1 192 ? 23.361 53.983 23.390 1.00 26.67 ? 185 PHE A CG 1 ATOM 1090 C CD1 . PHE A 1 192 ? 23.088 53.344 24.593 1.00 24.92 ? 185 PHE A CD1 1 ATOM 1091 C CD2 . PHE A 1 192 ? 23.242 53.252 22.203 1.00 25.73 ? 185 PHE A CD2 1 ATOM 1092 C CE1 . PHE A 1 192 ? 22.660 51.996 24.636 1.00 26.72 ? 185 PHE A CE1 1 ATOM 1093 C CE2 . PHE A 1 192 ? 22.837 51.887 22.242 1.00 26.75 ? 185 PHE A CE2 1 ATOM 1094 C CZ . PHE A 1 192 ? 22.549 51.265 23.471 1.00 26.38 ? 185 PHE A CZ 1 ATOM 1095 N N . PHE A 1 193 ? 25.978 57.901 23.322 1.00 31.62 ? 186 PHE A N 1 ATOM 1096 C CA . PHE A 1 193 ? 26.594 59.135 22.800 1.00 33.32 ? 186 PHE A CA 1 ATOM 1097 C C . PHE A 1 193 ? 27.849 58.816 21.970 1.00 34.46 ? 186 PHE A C 1 ATOM 1098 O O . PHE A 1 193 ? 27.993 59.285 20.840 1.00 34.69 ? 186 PHE A O 1 ATOM 1099 C CB . PHE A 1 193 ? 26.993 60.123 23.905 1.00 32.57 ? 186 PHE A CB 1 ATOM 1100 C CG . PHE A 1 193 ? 25.828 60.854 24.542 1.00 32.85 ? 186 PHE A CG 1 ATOM 1101 C CD1 . PHE A 1 193 ? 24.569 60.851 23.964 1.00 32.36 ? 186 PHE A CD1 1 ATOM 1102 C CD2 . PHE A 1 193 ? 26.024 61.583 25.736 1.00 33.41 ? 186 PHE A CD2 1 ATOM 1103 C CE1 . PHE A 1 193 ? 23.514 61.540 24.583 1.00 33.34 ? 186 PHE A CE1 1 ATOM 1104 C CE2 . PHE A 1 193 ? 24.994 62.280 26.353 1.00 29.82 ? 186 PHE A CE2 1 ATOM 1105 C CZ . PHE A 1 193 ? 23.734 62.253 25.783 1.00 32.52 ? 186 PHE A CZ 1 ATOM 1106 N N . LYS A 1 194 ? 28.769 58.052 22.561 1.00 35.79 ? 187 LYS A N 1 ATOM 1107 C CA . LYS A 1 194 ? 30.061 57.736 21.946 1.00 36.91 ? 187 LYS A CA 1 ATOM 1108 C C . LYS A 1 194 ? 29.858 57.037 20.591 1.00 37.68 ? 187 LYS A C 1 ATOM 1109 O O . LYS A 1 194 ? 30.480 57.426 19.592 1.00 37.57 ? 187 LYS A O 1 ATOM 1110 C CB . LYS A 1 194 ? 30.896 56.870 22.904 1.00 37.69 ? 187 LYS A CB 1 ATOM 1111 C CG . LYS A 1 194 ? 32.243 56.301 22.383 1.00 40.19 ? 187 LYS A CG 1 ATOM 1112 C CD . LYS A 1 194 ? 33.361 57.339 22.209 1.00 45.21 ? 187 LYS A CD 1 ATOM 1113 C CE . LYS A 1 194 ? 33.960 57.840 23.537 1.00 45.98 ? 187 LYS A CE 1 ATOM 1114 N NZ . LYS A 1 194 ? 35.174 58.663 23.253 0.30 45.70 ? 187 LYS A NZ 1 ATOM 1115 N N . LEU A 1 195 ? 28.983 56.027 20.563 1.00 37.95 ? 188 LEU A N 1 ATOM 1116 C CA . LEU A 1 195 ? 28.631 55.300 19.342 1.00 39.34 ? 188 LEU A CA 1 ATOM 1117 C C . LEU A 1 195 ? 28.003 56.180 18.277 1.00 40.12 ? 188 LEU A C 1 ATOM 1118 O O . LEU A 1 195 ? 28.476 56.192 17.146 1.00 39.27 ? 188 LEU A O 1 ATOM 1119 C CB . LEU A 1 195 ? 27.626 54.191 19.623 1.00 39.25 ? 188 LEU A CB 1 ATOM 1120 C CG . LEU A 1 195 ? 28.162 52.856 20.056 1.00 40.29 ? 188 LEU A CG 1 ATOM 1121 C CD1 . LEU A 1 195 ? 26.974 52.038 20.606 1.00 42.34 ? 188 LEU A CD1 1 ATOM 1122 C CD2 . LEU A 1 195 ? 28.822 52.185 18.892 1.00 39.97 ? 188 LEU A CD2 1 ATOM 1123 N N . GLU A 1 196 ? 26.921 56.879 18.637 1.00 40.58 ? 189 GLU A N 1 ATOM 1124 C CA . GLU A 1 196 ? 26.124 57.592 17.637 1.00 41.80 ? 189 GLU A CA 1 ATOM 1125 C C . GLU A 1 196 ? 26.795 58.913 17.242 1.00 42.21 ? 189 GLU A C 1 ATOM 1126 O O . GLU A 1 196 ? 26.966 59.182 16.061 1.00 42.74 ? 189 GLU A O 1 ATOM 1127 C CB . GLU A 1 196 ? 24.657 57.773 18.082 1.00 41.86 ? 189 GLU A CB 1 ATOM 1128 C CG . GLU A 1 196 ? 24.308 57.094 19.384 0.20 43.08 ? 189 GLU A CG 1 ATOM 1129 C CD . GLU A 1 196 ? 23.149 56.130 19.292 0.80 45.31 ? 189 GLU A CD 1 ATOM 1130 O OE1 . GLU A 1 196 ? 22.005 56.555 18.993 0.80 46.41 ? 189 GLU A OE1 1 ATOM 1131 O OE2 . GLU A 1 196 ? 23.381 54.936 19.545 0.20 45.47 ? 189 GLU A OE2 1 ATOM 1132 N N . ARG A 1 197 ? 27.234 59.701 18.224 1.00 42.14 ? 190 ARG A N 1 ATOM 1133 C CA . ARG A 1 197 ? 27.836 61.008 17.945 1.00 42.26 ? 190 ARG A CA 1 ATOM 1134 C C . ARG A 1 197 ? 29.306 60.963 17.490 1.00 43.16 ? 190 ARG A C 1 ATOM 1135 O O . ARG A 1 197 ? 29.676 61.695 16.566 1.00 42.62 ? 190 ARG A O 1 ATOM 1136 C CB . ARG A 1 197 ? 27.676 61.977 19.128 1.00 41.06 ? 190 ARG A CB 1 ATOM 1137 C CG . ARG A 1 197 ? 26.235 62.152 19.585 1.00 39.14 ? 190 ARG A CG 1 ATOM 1138 C CD . ARG A 1 197 ? 26.186 62.886 20.902 1.00 37.73 ? 190 ARG A CD 1 ATOM 1139 N NE . ARG A 1 197 ? 24.812 63.238 21.276 1.00 36.75 ? 190 ARG A NE 1 ATOM 1140 C CZ . ARG A 1 197 ? 24.498 64.053 22.277 1.00 35.44 ? 190 ARG A CZ 1 ATOM 1141 N NH1 . ARG A 1 197 ? 25.447 64.583 23.029 1.00 33.55 ? 190 ARG A NH1 1 ATOM 1142 N NH2 . ARG A 1 197 ? 23.234 64.330 22.538 1.00 36.04 ? 190 ARG A NH2 1 ATOM 1143 N N . ASP A 1 198 ? 30.149 60.167 18.159 1.00 44.22 ? 191 ASP A N 1 ATOM 1144 C CA . ASP A 1 198 ? 31.579 60.131 17.825 1.00 46.36 ? 191 ASP A CA 1 ATOM 1145 C C . ASP A 1 198 ? 31.892 59.082 16.767 1.00 46.89 ? 191 ASP A C 1 ATOM 1146 O O . ASP A 1 198 ? 32.625 59.362 15.833 1.00 47.23 ? 191 ASP A O 1 ATOM 1147 C CB . ASP A 1 198 ? 32.469 59.890 19.048 1.00 46.71 ? 191 ASP A CB 1 ATOM 1148 C CG . ASP A 1 198 ? 32.214 60.874 20.161 1.00 49.09 ? 191 ASP A CG 1 ATOM 1149 O OD1 . ASP A 1 198 ? 31.692 61.971 19.868 1.00 50.12 ? 191 ASP A OD1 1 ATOM 1150 O OD2 . ASP A 1 198 ? 32.522 60.543 21.337 1.00 51.16 ? 191 ASP A OD2 1 ATOM 1151 N N . MET A 1 199 ? 31.355 57.871 16.911 1.00 47.05 ? 192 MET A N 1 ATOM 1152 C CA . MET A 1 199 ? 31.732 56.790 15.993 1.00 47.74 ? 192 MET A CA 1 ATOM 1153 C C . MET A 1 199 ? 30.848 56.742 14.757 1.00 47.70 ? 192 MET A C 1 ATOM 1154 O O . MET A 1 199 ? 31.192 56.065 13.798 1.00 46.70 ? 192 MET A O 1 ATOM 1155 C CB . MET A 1 199 ? 31.756 55.430 16.702 1.00 47.49 ? 192 MET A CB 1 ATOM 1156 C CG . MET A 1 199 ? 32.743 55.356 17.850 1.00 47.50 ? 192 MET A CG 1 ATOM 1157 S SD . MET A 1 199 ? 32.757 53.730 18.617 1.00 46.32 ? 192 MET A SD 1 ATOM 1158 C CE . MET A 1 199 ? 33.895 52.905 17.470 1.00 45.25 ? 192 MET A CE 1 ATOM 1159 N N . LYS A 1 200 ? 29.721 57.458 14.796 1.00 48.03 ? 193 LYS A N 1 ATOM 1160 C CA . LYS A 1 200 ? 28.738 57.485 13.709 1.00 48.97 ? 193 LYS A CA 1 ATOM 1161 C C . LYS A 1 200 ? 28.219 56.082 13.405 1.00 48.65 ? 193 LYS A C 1 ATOM 1162 O O . LYS A 1 200 ? 28.036 55.720 12.244 1.00 48.58 ? 193 LYS A O 1 ATOM 1163 C CB . LYS A 1 200 ? 29.288 58.174 12.434 1.00 49.40 ? 193 LYS A CB 1 ATOM 1164 C CG . LYS A 1 200 ? 29.117 59.704 12.425 1.00 52.33 ? 193 LYS A CG 1 ATOM 1165 C CD . LYS A 1 200 ? 30.280 60.427 13.112 1.00 55.43 ? 193 LYS A CD 1 ATOM 1166 C CE . LYS A 1 200 ? 30.205 61.952 12.954 1.00 55.80 ? 193 LYS A CE 1 ATOM 1167 N NZ . LYS A 1 200 ? 29.154 62.569 13.808 0.75 55.15 ? 193 LYS A NZ 1 ATOM 1168 N N . ILE A 1 201 ? 27.998 55.288 14.458 1.00 47.62 ? 194 ILE A N 1 ATOM 1169 C CA . ILE A 1 201 ? 27.437 53.947 14.293 1.00 46.96 ? 194 ILE A CA 1 ATOM 1170 C C . ILE A 1 201 ? 25.944 53.973 14.573 1.00 46.56 ? 194 ILE A C 1 ATOM 1171 O O . ILE A 1 201 ? 25.490 54.566 15.541 1.00 46.39 ? 194 ILE A O 1 ATOM 1172 C CB . ILE A 1 201 ? 28.223 52.859 15.089 1.00 46.88 ? 194 ILE A CB 1 ATOM 1173 C CG1 . ILE A 1 201 ? 29.470 52.457 14.277 1.00 46.71 ? 194 ILE A CG1 1 ATOM 1174 C CG2 . ILE A 1 201 ? 27.355 51.608 15.346 1.00 46.22 ? 194 ILE A CG2 1 ATOM 1175 C CD1 . ILE A 1 201 ? 30.670 52.036 15.095 1.00 46.19 ? 194 ILE A CD1 1 ATOM 1176 N N . ASN A 1 202 ? 25.177 53.365 13.690 1.00 46.33 ? 195 ASN A N 1 ATOM 1177 C CA . ASN A 1 202 ? 23.736 53.467 13.765 1.00 46.82 ? 195 ASN A CA 1 ATOM 1178 C C . ASN A 1 202 ? 23.184 52.124 14.277 1.00 44.79 ? 195 ASN A C 1 ATOM 1179 O O . ASN A 1 202 ? 23.422 51.064 13.681 1.00 42.69 ? 195 ASN A O 1 ATOM 1180 C CB . ASN A 1 202 ? 23.197 53.921 12.392 1.00 48.82 ? 195 ASN A CB 1 ATOM 1181 C CG . ASN A 1 202 ? 21.661 53.964 12.307 1.00 54.85 ? 195 ASN A CG 1 ATOM 1182 O OD1 . ASN A 1 202 ? 20.954 53.873 13.322 1.00 55.28 ? 195 ASN A OD1 1 ATOM 1183 N ND2 . ASN A 1 202 ? 21.150 54.100 11.051 1.00 64.97 ? 195 ASN A ND2 1 ATOM 1184 N N . CYS A 1 203 ? 22.500 52.181 15.423 1.00 42.60 ? 196 CYS A N 1 ATOM 1185 C CA . CYS A 1 203 ? 21.977 50.985 16.081 1.00 41.63 ? 196 CYS A CA 1 ATOM 1186 C C . CYS A 1 203 ? 20.608 50.588 15.568 1.00 41.29 ? 196 CYS A C 1 ATOM 1187 O O . CYS A 1 203 ? 20.058 49.537 15.959 1.00 40.57 ? 196 CYS A O 1 ATOM 1188 C CB . CYS A 1 203 ? 21.929 51.170 17.611 1.00 41.54 ? 196 CYS A CB 1 ATOM 1189 S SG . CYS A 1 203 ? 23.555 51.018 18.316 1.00 41.61 ? 196 CYS A SG 1 ATOM 1190 N N . SER A 1 204 ? 20.056 51.419 14.693 1.00 41.12 ? 197 SER A N 1 ATOM 1191 C CA . SER A 1 204 ? 18.705 51.210 14.174 1.00 41.83 ? 197 SER A CA 1 ATOM 1192 C C . SER A 1 204 ? 18.508 49.841 13.481 1.00 41.46 ? 197 SER A C 1 ATOM 1193 O O . SER A 1 204 ? 19.227 49.508 12.543 1.00 41.81 ? 197 SER A O 1 ATOM 1194 C CB . SER A 1 204 ? 18.339 52.365 13.239 1.00 42.30 ? 197 SER A CB 1 ATOM 1195 O OG . SER A 1 204 ? 17.038 52.213 12.715 1.00 42.91 ? 197 SER A OG 1 ATOM 1196 N N . GLY A 1 205 ? 17.549 49.045 13.962 1.00 40.40 ? 198 GLY A N 1 ATOM 1197 C CA . GLY A 1 205 ? 17.339 47.698 13.425 1.00 39.44 ? 198 GLY A CA 1 ATOM 1198 C C . GLY A 1 205 ? 18.479 46.706 13.674 1.00 38.85 ? 198 GLY A C 1 ATOM 1199 O O . GLY A 1 205 ? 18.513 45.658 13.040 1.00 38.42 ? 198 GLY A O 1 ATOM 1200 N N . LYS A 1 206 ? 19.401 47.010 14.601 1.00 37.40 ? 199 LYS A N 1 ATOM 1201 C CA . LYS A 1 206 ? 20.478 46.062 14.971 1.00 36.23 ? 199 LYS A CA 1 ATOM 1202 C C . LYS A 1 206 ? 20.102 45.339 16.300 1.00 35.44 ? 199 LYS A C 1 ATOM 1203 O O . LYS A 1 206 ? 19.296 45.840 17.071 1.00 33.97 ? 199 LYS A O 1 ATOM 1204 C CB . LYS A 1 206 ? 21.835 46.780 15.101 1.00 35.19 ? 199 LYS A CB 1 ATOM 1205 C CG . LYS A 1 206 ? 22.384 47.434 13.792 1.00 36.90 ? 199 LYS A CG 1 ATOM 1206 C CD . LYS A 1 206 ? 22.692 46.407 12.708 0.30 35.34 ? 199 LYS A CD 1 ATOM 1207 C CE . LYS A 1 206 ? 23.157 47.088 11.446 0.30 36.30 ? 199 LYS A CE 1 ATOM 1208 N NZ . LYS A 1 206 ? 22.077 47.918 10.885 0.60 35.96 ? 199 LYS A NZ 1 ATOM 1209 N N . ILE A 1 207 ? 20.652 44.153 16.542 1.00 34.71 ? 200 ILE A N 1 ATOM 1210 C CA . ILE A 1 207 ? 20.596 43.562 17.881 1.00 34.32 ? 200 ILE A CA 1 ATOM 1211 C C . ILE A 1 207 ? 21.803 44.037 18.689 1.00 33.22 ? 200 ILE A C 1 ATOM 1212 O O . ILE A 1 207 ? 22.952 43.838 18.305 1.00 34.21 ? 200 ILE A O 1 ATOM 1213 C CB . ILE A 1 207 ? 20.555 42.037 17.825 1.00 34.98 ? 200 ILE A CB 1 ATOM 1214 C CG1 . ILE A 1 207 ? 19.271 41.601 17.121 1.00 35.38 ? 200 ILE A CG1 1 ATOM 1215 C CG2 . ILE A 1 207 ? 20.615 41.461 19.252 1.00 35.20 ? 200 ILE A CG2 1 ATOM 1216 C CD1 . ILE A 1 207 ? 19.298 40.175 16.710 1.00 35.93 ? 200 ILE A CD1 1 ATOM 1217 N N . VAL A 1 208 ? 21.548 44.682 19.807 1.00 31.74 ? 201 VAL A N 1 ATOM 1218 C CA . VAL A 1 208 ? 22.623 45.207 20.609 1.00 30.05 ? 201 VAL A CA 1 ATOM 1219 C C . VAL A 1 208 ? 23.051 44.172 21.667 1.00 29.30 ? 201 VAL A C 1 ATOM 1220 O O . VAL A 1 208 ? 22.213 43.530 22.324 1.00 30.14 ? 201 VAL A O 1 ATOM 1221 C CB . VAL A 1 208 ? 22.196 46.615 21.207 1.00 30.61 ? 201 VAL A CB 1 ATOM 1222 C CG1 A VAL A 1 208 ? 21.864 47.612 20.071 0.50 30.37 ? 201 VAL A CG1 1 ATOM 1223 C CG1 B VAL A 1 208 ? 22.554 46.776 22.659 0.50 29.18 ? 201 VAL A CG1 1 ATOM 1224 C CG2 A VAL A 1 208 ? 21.098 46.507 22.179 0.50 28.49 ? 201 VAL A CG2 1 ATOM 1225 C CG2 B VAL A 1 208 ? 22.659 47.765 20.290 0.50 30.36 ? 201 VAL A CG2 1 ATOM 1226 N N . ILE A 1 209 ? 24.351 43.998 21.825 1.00 27.24 ? 202 ILE A N 1 ATOM 1227 C CA . ILE A 1 209 ? 24.870 43.209 22.930 1.00 26.54 ? 202 ILE A CA 1 ATOM 1228 C C . ILE A 1 209 ? 25.601 44.145 23.899 1.00 26.48 ? 202 ILE A C 1 ATOM 1229 O O . ILE A 1 209 ? 26.446 44.958 23.500 1.00 25.49 ? 202 ILE A O 1 ATOM 1230 C CB . ILE A 1 209 ? 25.741 42.010 22.459 1.00 26.94 ? 202 ILE A CB 1 ATOM 1231 C CG1 . ILE A 1 209 ? 26.221 41.162 23.653 1.00 25.76 ? 202 ILE A CG1 1 ATOM 1232 C CG2 . ILE A 1 209 ? 26.894 42.468 21.505 1.00 26.37 ? 202 ILE A CG2 1 ATOM 1233 C CD1 . ILE A 1 209 ? 26.757 39.743 23.185 1.00 26.54 ? 202 ILE A CD1 1 ATOM 1234 N N . ALA A 1 210 ? 25.194 44.069 25.157 1.00 25.52 ? 203 ALA A N 1 ATOM 1235 C CA . ALA A 1 210 ? 25.718 44.932 26.193 1.00 26.04 ? 203 ALA A CA 1 ATOM 1236 C C . ALA A 1 210 ? 26.177 44.086 27.379 1.00 26.15 ? 203 ALA A C 1 ATOM 1237 O O . ALA A 1 210 ? 25.515 43.104 27.765 1.00 26.34 ? 203 ALA A O 1 ATOM 1238 C CB . ALA A 1 210 ? 24.636 45.953 26.657 1.00 24.69 ? 203 ALA A CB 1 ATOM 1239 N N . ARG A 1 211 ? 27.281 44.494 27.990 1.00 25.93 ? 204 ARG A N 1 ATOM 1240 C CA . ARG A 1 211 ? 27.685 43.862 29.234 1.00 25.62 ? 204 ARG A CA 1 ATOM 1241 C C . ARG A 1 211 ? 26.967 44.480 30.427 1.00 25.07 ? 204 ARG A C 1 ATOM 1242 O O . ARG A 1 211 ? 26.709 45.706 30.472 1.00 24.79 ? 204 ARG A O 1 ATOM 1243 C CB . ARG A 1 211 ? 29.213 43.867 29.412 1.00 25.76 ? 204 ARG A CB 1 ATOM 1244 C CG . ARG A 1 211 ? 29.891 45.229 29.305 1.00 28.03 ? 204 ARG A CG 1 ATOM 1245 C CD . ARG A 1 211 ? 31.354 45.068 29.678 1.00 29.04 ? 204 ARG A CD 1 ATOM 1246 N NE . ARG A 1 211 ? 32.172 46.253 29.371 1.00 29.83 ? 204 ARG A NE 1 ATOM 1247 C CZ . ARG A 1 211 ? 33.407 46.463 29.828 1.00 29.40 ? 204 ARG A CZ 1 ATOM 1248 N NH1 . ARG A 1 211 ? 33.955 45.616 30.673 1.00 28.15 ? 204 ARG A NH1 1 ATOM 1249 N NH2 . ARG A 1 211 ? 34.087 47.557 29.467 1.00 31.37 ? 204 ARG A NH2 1 ATOM 1250 N N . TYR A 1 212 ? 26.610 43.618 31.386 1.00 23.49 ? 205 TYR A N 1 ATOM 1251 C CA . TYR A 1 212 ? 26.012 44.068 32.626 1.00 22.35 ? 205 TYR A CA 1 ATOM 1252 C C . TYR A 1 212 ? 27.047 44.890 33.403 1.00 22.33 ? 205 TYR A C 1 ATOM 1253 O O . TYR A 1 212 ? 28.269 44.675 33.239 1.00 21.68 ? 205 TYR A O 1 ATOM 1254 C CB . TYR A 1 212 ? 25.656 42.840 33.450 1.00 21.80 ? 205 TYR A CB 1 ATOM 1255 C CG . TYR A 1 212 ? 24.269 42.210 33.292 1.00 19.72 ? 205 TYR A CG 1 ATOM 1256 C CD1 . TYR A 1 212 ? 24.145 40.819 33.072 1.00 18.66 ? 205 TYR A CD1 1 ATOM 1257 C CD2 . TYR A 1 212 ? 23.109 42.950 33.493 1.00 18.87 ? 205 TYR A CD2 1 ATOM 1258 C CE1 . TYR A 1 212 ? 22.876 40.181 33.036 1.00 19.51 ? 205 TYR A CE1 1 ATOM 1259 C CE2 . TYR A 1 212 ? 21.840 42.334 33.473 1.00 18.49 ? 205 TYR A CE2 1 ATOM 1260 C CZ . TYR A 1 212 ? 21.734 40.954 33.256 1.00 19.03 ? 205 TYR A CZ 1 ATOM 1261 O OH . TYR A 1 212 ? 20.501 40.359 33.266 1.00 18.54 ? 205 TYR A OH 1 ATOM 1262 N N . GLY A 1 213 ? 26.587 45.783 34.273 1.00 22.59 ? 206 GLY A N 1 ATOM 1263 C CA . GLY A 1 213 ? 27.504 46.523 35.162 1.00 22.26 ? 206 GLY A CA 1 ATOM 1264 C C . GLY A 1 213 ? 27.216 47.998 35.043 1.00 22.52 ? 206 GLY A C 1 ATOM 1265 O O . GLY A 1 213 ? 26.596 48.413 34.042 1.00 22.18 ? 206 GLY A O 1 ATOM 1266 N N . LYS A 1 214 ? 27.600 48.763 36.085 1.00 22.53 ? 207 LYS A N 1 ATOM 1267 C CA . LYS A 1 214 ? 27.635 50.257 36.085 1.00 22.93 ? 207 LYS A CA 1 ATOM 1268 C C . LYS A 1 214 ? 26.280 50.865 36.276 1.00 22.54 ? 207 LYS A C 1 ATOM 1269 O O . LYS A 1 214 ? 26.149 51.799 37.064 1.00 22.50 ? 207 LYS A O 1 ATOM 1270 C CB . LYS A 1 214 ? 28.252 50.870 34.807 1.00 22.41 ? 207 LYS A CB 1 ATOM 1271 C CG . LYS A 1 214 ? 29.693 50.382 34.499 1.00 25.55 ? 207 LYS A CG 1 ATOM 1272 C CD . LYS A 1 214 ? 30.671 50.702 35.611 1.00 29.39 ? 207 LYS A CD 1 ATOM 1273 C CE . LYS A 1 214 ? 32.092 50.292 35.160 1.00 30.84 ? 207 LYS A CE 1 ATOM 1274 N NZ . LYS A 1 214 ? 32.969 50.315 36.377 1.00 35.52 ? 207 LYS A NZ 1 ATOM 1275 N N . VAL A 1 215 ? 25.269 50.354 35.566 1.00 21.93 ? 208 VAL A N 1 ATOM 1276 C CA . VAL A 1 215 ? 23.927 50.933 35.699 1.00 20.72 ? 208 VAL A CA 1 ATOM 1277 C C . VAL A 1 215 ? 22.862 49.847 35.718 1.00 20.40 ? 208 VAL A C 1 ATOM 1278 O O . VAL A 1 215 ? 23.113 48.701 35.257 1.00 21.36 ? 208 VAL A O 1 ATOM 1279 C CB . VAL A 1 215 ? 23.624 52.036 34.592 1.00 20.95 ? 208 VAL A CB 1 ATOM 1280 C CG1 . VAL A 1 215 ? 24.762 53.170 34.559 1.00 21.66 ? 208 VAL A CG1 1 ATOM 1281 C CG2 . VAL A 1 215 ? 23.402 51.410 33.195 1.00 20.06 ? 208 VAL A CG2 1 ATOM 1282 N N . PHE A 1 216 ? 21.694 50.191 36.267 1.00 18.43 ? 209 PHE A N 1 ATOM 1283 C CA . PHE A 1 216 ? 20.497 49.303 36.243 1.00 17.59 ? 209 PHE A CA 1 ATOM 1284 C C . PHE A 1 216 ? 20.168 48.833 34.801 1.00 18.42 ? 209 PHE A C 1 ATOM 1285 O O . PHE A 1 216 ? 20.096 49.675 33.874 1.00 18.92 ? 209 PHE A O 1 ATOM 1286 C CB . PHE A 1 216 ? 19.295 50.055 36.834 1.00 16.47 ? 209 PHE A CB 1 ATOM 1287 C CG . PHE A 1 216 ? 17.985 49.303 36.737 1.00 16.75 ? 209 PHE A CG 1 ATOM 1288 C CD1 . PHE A 1 216 ? 17.876 48.036 37.339 1.00 16.54 ? 209 PHE A CD1 1 ATOM 1289 C CD2 . PHE A 1 216 ? 16.831 49.885 36.110 1.00 15.94 ? 209 PHE A CD2 1 ATOM 1290 C CE1 . PHE A 1 216 ? 16.696 47.283 37.288 1.00 18.16 ? 209 PHE A CE1 1 ATOM 1291 C CE2 . PHE A 1 216 ? 15.621 49.155 36.073 1.00 19.18 ? 209 PHE A CE2 1 ATOM 1292 C CZ . PHE A 1 216 ? 15.563 47.819 36.655 1.00 19.37 ? 209 PHE A CZ 1 ATOM 1293 N N . ARG A 1 217 ? 19.917 47.529 34.620 1.00 18.03 ? 210 ARG A N 1 ATOM 1294 C CA . ARG A 1 217 ? 19.736 46.957 33.274 1.00 19.08 ? 210 ARG A CA 1 ATOM 1295 C C . ARG A 1 217 ? 18.488 47.516 32.572 1.00 19.91 ? 210 ARG A C 1 ATOM 1296 O O . ARG A 1 217 ? 18.435 47.550 31.341 1.00 19.72 ? 210 ARG A O 1 ATOM 1297 C CB . ARG A 1 217 ? 19.623 45.419 33.327 1.00 19.17 ? 210 ARG A CB 1 ATOM 1298 C CG . ARG A 1 217 ? 18.340 44.914 34.086 1.00 17.09 ? 210 ARG A CG 1 ATOM 1299 C CD . ARG A 1 217 ? 18.367 43.347 34.322 1.00 16.69 ? 210 ARG A CD 1 ATOM 1300 N NE . ARG A 1 217 ? 19.140 42.931 35.524 1.00 17.19 ? 210 ARG A NE 1 ATOM 1301 C CZ . ARG A 1 217 ? 18.735 43.177 36.779 1.00 18.99 ? 210 ARG A CZ 1 ATOM 1302 N NH1 . ARG A 1 217 ? 17.561 43.803 36.988 1.00 17.15 ? 210 ARG A NH1 1 ATOM 1303 N NH2 . ARG A 1 217 ? 19.466 42.771 37.836 1.00 18.24 ? 210 ARG A NH2 1 ATOM 1304 N N . GLY A 1 218 ? 17.495 47.961 33.348 1.00 20.50 ? 211 GLY A N 1 ATOM 1305 C CA . GLY A 1 218 ? 16.340 48.661 32.765 1.00 20.10 ? 211 GLY A CA 1 ATOM 1306 C C . GLY A 1 218 ? 16.751 49.922 31.980 1.00 20.24 ? 211 GLY A C 1 ATOM 1307 O O . GLY A 1 218 ? 16.194 50.206 30.892 1.00 18.34 ? 211 GLY A O 1 ATOM 1308 N N . ASN A 1 219 ? 17.708 50.688 32.522 1.00 19.66 ? 212 ASN A N 1 ATOM 1309 C CA . ASN A 1 219 ? 18.197 51.856 31.789 1.00 20.45 ? 212 ASN A CA 1 ATOM 1310 C C . ASN A 1 219 ? 18.910 51.505 30.496 1.00 21.21 ? 212 ASN A C 1 ATOM 1311 O O . ASN A 1 219 ? 18.812 52.235 29.497 1.00 21.93 ? 212 ASN A O 1 ATOM 1312 C CB . ASN A 1 219 ? 19.093 52.718 32.656 1.00 19.76 ? 212 ASN A CB 1 ATOM 1313 C CG . ASN A 1 219 ? 18.311 53.366 33.805 1.00 21.04 ? 212 ASN A CG 1 ATOM 1314 O OD1 . ASN A 1 219 ? 18.237 52.810 34.894 1.00 22.88 ? 212 ASN A OD1 1 ATOM 1315 N ND2 . ASN A 1 219 ? 17.699 54.506 33.548 1.00 18.47 ? 212 ASN A ND2 1 ATOM 1316 N N . LYS A 1 220 ? 19.649 50.396 30.529 1.00 21.35 ? 213 LYS A N 1 ATOM 1317 C CA . LYS A 1 220 ? 20.318 49.884 29.330 1.00 21.08 ? 213 LYS A CA 1 ATOM 1318 C C . LYS A 1 220 ? 19.308 49.598 28.226 1.00 21.43 ? 213 LYS A C 1 ATOM 1319 O O . LYS A 1 220 ? 19.545 49.968 27.037 1.00 21.37 ? 213 LYS A O 1 ATOM 1320 C CB . LYS A 1 220 ? 21.073 48.573 29.622 1.00 20.29 ? 213 LYS A CB 1 ATOM 1321 C CG . LYS A 1 220 ? 22.214 48.650 30.673 1.00 20.21 ? 213 LYS A CG 1 ATOM 1322 C CD . LYS A 1 220 ? 22.841 47.234 30.879 1.00 19.28 ? 213 LYS A CD 1 ATOM 1323 C CE . LYS A 1 220 ? 23.793 47.200 32.097 1.00 18.45 ? 213 LYS A CE 1 ATOM 1324 N NZ . LYS A 1 220 ? 25.214 47.650 31.829 1.00 17.95 ? 213 LYS A NZ 1 ATOM 1325 N N . VAL A 1 221 ? 18.234 48.877 28.598 1.00 20.57 ? 214 VAL A N 1 ATOM 1326 C CA . VAL A 1 221 ? 17.220 48.473 27.647 1.00 21.17 ? 214 VAL A CA 1 ATOM 1327 C C . VAL A 1 221 ? 16.527 49.741 27.097 1.00 22.17 ? 214 VAL A C 1 ATOM 1328 O O . VAL A 1 221 ? 16.337 49.855 25.870 1.00 21.52 ? 214 VAL A O 1 ATOM 1329 C CB . VAL A 1 221 ? 16.224 47.430 28.239 1.00 21.59 ? 214 VAL A CB 1 ATOM 1330 C CG1 . VAL A 1 221 ? 15.005 47.200 27.301 1.00 22.04 ? 214 VAL A CG1 1 ATOM 1331 C CG2 . VAL A 1 221 ? 16.955 46.075 28.537 1.00 20.92 ? 214 VAL A CG2 1 ATOM 1332 N N A LYS A 1 222 ? 16.179 50.685 27.972 0.50 21.64 ? 215 LYS A N 1 ATOM 1333 N N B LYS A 1 222 ? 16.185 50.674 27.994 0.50 21.90 ? 215 LYS A N 1 ATOM 1334 C CA A LYS A 1 222 ? 15.569 51.936 27.475 0.50 22.35 ? 215 LYS A CA 1 ATOM 1335 C CA B LYS A 1 222 ? 15.602 51.982 27.599 0.50 22.94 ? 215 LYS A CA 1 ATOM 1336 C C A LYS A 1 222 ? 16.490 52.656 26.492 0.50 23.20 ? 215 LYS A C 1 ATOM 1337 C C B LYS A 1 222 ? 16.476 52.673 26.551 0.50 23.49 ? 215 LYS A C 1 ATOM 1338 O O A LYS A 1 222 ? 16.032 53.137 25.435 0.50 23.43 ? 215 LYS A O 1 ATOM 1339 O O B LYS A 1 222 ? 15.978 53.122 25.499 0.50 23.78 ? 215 LYS A O 1 ATOM 1340 C CB A LYS A 1 222 ? 15.240 52.900 28.599 0.50 21.65 ? 215 LYS A CB 1 ATOM 1341 C CB B LYS A 1 222 ? 15.480 52.894 28.822 0.50 22.44 ? 215 LYS A CB 1 ATOM 1342 C CG A LYS A 1 222 ? 14.743 54.240 28.070 0.50 22.47 ? 215 LYS A CG 1 ATOM 1343 C CG B LYS A 1 222 ? 14.897 54.289 28.573 0.50 24.94 ? 215 LYS A CG 1 ATOM 1344 C CD A LYS A 1 222 ? 14.465 55.228 29.210 0.50 23.07 ? 215 LYS A CD 1 ATOM 1345 C CD B LYS A 1 222 ? 14.703 55.044 29.925 0.50 25.72 ? 215 LYS A CD 1 ATOM 1346 C CE A LYS A 1 222 ? 14.872 56.657 28.811 0.50 23.62 ? 215 LYS A CE 1 ATOM 1347 C CE B LYS A 1 222 ? 14.382 56.541 29.752 0.50 28.96 ? 215 LYS A CE 1 ATOM 1348 N NZ A LYS A 1 222 ? 15.545 57.348 29.958 0.50 28.55 ? 215 LYS A NZ 1 ATOM 1349 N NZ B LYS A 1 222 ? 13.222 56.804 28.848 0.50 29.41 ? 215 LYS A NZ 1 ATOM 1350 N N . ASN A 1 223 ? 17.779 52.748 26.845 1.00 23.25 ? 216 ASN A N 1 ATOM 1351 C CA . ASN A 1 223 ? 18.760 53.409 25.972 1.00 23.59 ? 216 ASN A CA 1 ATOM 1352 C C . ASN A 1 223 ? 18.870 52.680 24.630 1.00 24.80 ? 216 ASN A C 1 ATOM 1353 O O . ASN A 1 223 ? 18.909 53.322 23.574 1.00 23.84 ? 216 ASN A O 1 ATOM 1354 C CB . ASN A 1 223 ? 20.149 53.455 26.638 1.00 22.03 ? 216 ASN A CB 1 ATOM 1355 C CG . ASN A 1 223 ? 20.160 54.279 27.912 1.00 23.46 ? 216 ASN A CG 1 ATOM 1356 O OD1 . ASN A 1 223 ? 19.231 55.067 28.170 1.00 22.61 ? 216 ASN A OD1 1 ATOM 1357 N ND2 . ASN A 1 223 ? 21.203 54.094 28.740 1.00 23.19 ? 216 ASN A ND2 1 ATOM 1358 N N . ALA A 1 224 ? 18.924 51.341 24.665 1.00 25.40 ? 217 ALA A N 1 ATOM 1359 C CA . ALA A 1 224 ? 18.977 50.584 23.410 1.00 27.25 ? 217 ALA A CA 1 ATOM 1360 C C . ALA A 1 224 ? 17.717 50.812 22.562 1.00 28.47 ? 217 ALA A C 1 ATOM 1361 O O . ALA A 1 224 ? 17.784 51.024 21.345 1.00 27.73 ? 217 ALA A O 1 ATOM 1362 C CB . ALA A 1 224 ? 19.236 49.069 23.660 1.00 26.47 ? 217 ALA A CB 1 ATOM 1363 N N . GLN A 1 225 ? 16.572 50.776 23.218 1.00 30.42 ? 218 GLN A N 1 ATOM 1364 C CA . GLN A 1 225 ? 15.291 50.954 22.547 1.00 32.95 ? 218 GLN A CA 1 ATOM 1365 C C . GLN A 1 225 ? 15.247 52.324 21.845 1.00 34.02 ? 218 GLN A C 1 ATOM 1366 O O . GLN A 1 225 ? 14.886 52.418 20.659 1.00 34.31 ? 218 GLN A O 1 ATOM 1367 C CB . GLN A 1 225 ? 14.215 50.847 23.609 1.00 33.56 ? 218 GLN A CB 1 ATOM 1368 C CG . GLN A 1 225 ? 12.953 50.256 23.173 1.00 37.09 ? 218 GLN A CG 1 ATOM 1369 C CD . GLN A 1 225 ? 11.965 50.172 24.320 1.00 39.79 ? 218 GLN A CD 1 ATOM 1370 O OE1 . GLN A 1 225 ? 12.020 49.241 25.145 1.00 36.80 ? 218 GLN A OE1 1 ATOM 1371 N NE2 . GLN A 1 225 ? 11.055 51.151 24.385 1.00 40.83 ? 218 GLN A NE2 1 ATOM 1372 N N . LEU A 1 226 ? 15.668 53.371 22.552 1.00 34.33 ? 219 LEU A N 1 ATOM 1373 C CA . LEU A 1 226 ? 15.708 54.714 21.981 1.00 35.28 ? 219 LEU A CA 1 ATOM 1374 C C . LEU A 1 226 ? 16.752 54.905 20.871 1.00 35.07 ? 219 LEU A C 1 ATOM 1375 O O . LEU A 1 226 ? 16.558 55.742 19.996 1.00 34.16 ? 219 LEU A O 1 ATOM 1376 C CB . LEU A 1 226 ? 15.825 55.784 23.080 1.00 36.23 ? 219 LEU A CB 1 ATOM 1377 C CG . LEU A 1 226 ? 14.566 55.893 23.978 1.00 38.65 ? 219 LEU A CG 1 ATOM 1378 C CD1 . LEU A 1 226 ? 14.720 56.916 25.145 1.00 40.64 ? 219 LEU A CD1 1 ATOM 1379 C CD2 . LEU A 1 226 ? 13.246 56.159 23.177 1.00 43.03 ? 219 LEU A CD2 1 ATOM 1380 N N . ALA A 1 227 ? 17.825 54.109 20.883 1.00 34.14 ? 220 ALA A N 1 ATOM 1381 C CA . ALA A 1 227 ? 18.780 54.079 19.767 1.00 33.93 ? 220 ALA A CA 1 ATOM 1382 C C . ALA A 1 227 ? 18.242 53.296 18.552 1.00 33.36 ? 220 ALA A C 1 ATOM 1383 O O . ALA A 1 227 ? 18.893 53.229 17.535 1.00 33.64 ? 220 ALA A O 1 ATOM 1384 C CB . ALA A 1 227 ? 20.099 53.497 20.229 1.00 33.58 ? 220 ALA A CB 1 ATOM 1385 N N . GLY A 1 228 ? 17.065 52.687 18.668 1.00 32.81 ? 221 GLY A N 1 ATOM 1386 C CA . GLY A 1 228 ? 16.463 51.969 17.539 1.00 31.91 ? 221 GLY A CA 1 ATOM 1387 C C . GLY A 1 228 ? 16.807 50.479 17.427 1.00 31.64 ? 221 GLY A C 1 ATOM 1388 O O . GLY A 1 228 ? 16.480 49.845 16.412 1.00 30.16 ? 221 GLY A O 1 ATOM 1389 N N . ALA A 1 229 ? 17.415 49.898 18.474 1.00 31.27 ? 222 ALA A N 1 ATOM 1390 C CA . ALA A 1 229 ? 17.757 48.458 18.480 1.00 30.77 ? 222 ALA A CA 1 ATOM 1391 C C . ALA A 1 229 ? 16.484 47.606 18.322 1.00 30.81 ? 222 ALA A C 1 ATOM 1392 O O . ALA A 1 229 ? 15.384 48.050 18.684 1.00 29.89 ? 222 ALA A O 1 ATOM 1393 C CB . ALA A 1 229 ? 18.510 48.073 19.755 1.00 29.60 ? 222 ALA A CB 1 ATOM 1394 N N . LYS A 1 230 ? 16.610 46.397 17.778 1.00 30.10 ? 223 LYS A N 1 ATOM 1395 C CA . LYS A 1 230 ? 15.431 45.543 17.739 1.00 30.14 ? 223 LYS A CA 1 ATOM 1396 C C . LYS A 1 230 ? 15.525 44.392 18.715 1.00 29.15 ? 223 LYS A C 1 ATOM 1397 O O . LYS A 1 230 ? 14.624 43.556 18.765 1.00 28.60 ? 223 LYS A O 1 ATOM 1398 C CB . LYS A 1 230 ? 15.117 45.038 16.326 1.00 31.44 ? 223 LYS A CB 1 ATOM 1399 C CG . LYS A 1 230 ? 16.108 44.125 15.716 1.00 33.12 ? 223 LYS A CG 1 ATOM 1400 C CD . LYS A 1 230 ? 15.524 43.581 14.395 1.00 35.77 ? 223 LYS A CD 1 ATOM 1401 C CE . LYS A 1 230 ? 16.591 43.070 13.516 1.00 37.38 ? 223 LYS A CE 1 ATOM 1402 N NZ . LYS A 1 230 ? 16.102 42.647 12.143 0.50 34.34 ? 223 LYS A NZ 1 ATOM 1403 N N . GLY A 1 231 ? 16.609 44.344 19.486 1.00 27.90 ? 224 GLY A N 1 ATOM 1404 C CA . GLY A 1 231 ? 16.683 43.389 20.606 1.00 27.13 ? 224 GLY A CA 1 ATOM 1405 C C . GLY A 1 231 ? 17.923 43.671 21.411 1.00 26.31 ? 224 GLY A C 1 ATOM 1406 O O . GLY A 1 231 ? 18.803 44.384 20.935 1.00 25.39 ? 224 GLY A O 1 ATOM 1407 N N . VAL A 1 232 ? 17.966 43.182 22.650 1.00 26.27 ? 225 VAL A N 1 ATOM 1408 C CA . VAL A 1 232 ? 19.116 43.397 23.521 1.00 25.52 ? 225 VAL A CA 1 ATOM 1409 C C . VAL A 1 232 ? 19.536 42.049 24.115 1.00 25.65 ? 225 VAL A C 1 ATOM 1410 O O . VAL A 1 232 ? 18.693 41.257 24.576 1.00 24.16 ? 225 VAL A O 1 ATOM 1411 C CB . VAL A 1 232 ? 18.809 44.355 24.672 1.00 25.76 ? 225 VAL A CB 1 ATOM 1412 C CG1 . VAL A 1 232 ? 20.085 44.629 25.471 1.00 24.78 ? 225 VAL A CG1 1 ATOM 1413 C CG2 . VAL A 1 232 ? 18.201 45.659 24.141 1.00 25.59 ? 225 VAL A CG2 1 ATOM 1414 N N . ILE A 1 233 ? 20.845 41.794 24.062 1.00 25.34 ? 226 ILE A N 1 ATOM 1415 C CA . ILE A 1 233 ? 21.435 40.637 24.713 1.00 24.19 ? 226 ILE A CA 1 ATOM 1416 C C . ILE A 1 233 ? 22.316 41.184 25.833 1.00 23.67 ? 226 ILE A C 1 ATOM 1417 O O . ILE A 1 233 ? 23.225 41.994 25.585 1.00 22.65 ? 226 ILE A O 1 ATOM 1418 C CB . ILE A 1 233 ? 22.241 39.797 23.703 1.00 24.60 ? 226 ILE A CB 1 ATOM 1419 C CG1 . ILE A 1 233 ? 21.297 39.236 22.619 1.00 23.91 ? 226 ILE A CG1 1 ATOM 1420 C CG2 . ILE A 1 233 ? 23.037 38.708 24.423 1.00 22.99 ? 226 ILE A CG2 1 ATOM 1421 C CD1 . ILE A 1 233 ? 22.020 38.617 21.445 1.00 25.09 ? 226 ILE A CD1 1 ATOM 1422 N N . LEU A 1 234 ? 22.014 40.782 27.066 1.00 22.96 ? 227 LEU A N 1 ATOM 1423 C CA . LEU A 1 234 ? 22.810 41.218 28.225 1.00 22.44 ? 227 LEU A CA 1 ATOM 1424 C C . LEU A 1 234 ? 23.759 40.088 28.591 1.00 23.17 ? 227 LEU A C 1 ATOM 1425 O O . LEU A 1 234 ? 23.352 38.903 28.521 1.00 23.60 ? 227 LEU A O 1 ATOM 1426 C CB . LEU A 1 234 ? 21.875 41.513 29.393 1.00 21.28 ? 227 LEU A CB 1 ATOM 1427 C CG . LEU A 1 234 ? 20.886 42.658 29.093 1.00 21.95 ? 227 LEU A CG 1 ATOM 1428 C CD1 . LEU A 1 234 ? 19.808 42.715 30.191 1.00 20.69 ? 227 LEU A CD1 1 ATOM 1429 C CD2 . LEU A 1 234 ? 21.665 43.991 29.029 1.00 22.37 ? 227 LEU A CD2 1 ATOM 1430 N N . TYR A 1 235 ? 25.004 40.401 28.963 1.00 22.81 ? 228 TYR A N 1 ATOM 1431 C CA . TYR A 1 235 ? 25.905 39.306 29.397 1.00 23.74 ? 228 TYR A CA 1 ATOM 1432 C C . TYR A 1 235 ? 26.786 39.778 30.524 1.00 24.13 ? 228 TYR A C 1 ATOM 1433 O O . TYR A 1 235 ? 27.011 40.991 30.679 1.00 24.04 ? 228 TYR A O 1 ATOM 1434 C CB . TYR A 1 235 ? 26.739 38.701 28.240 1.00 22.87 ? 228 TYR A CB 1 ATOM 1435 C CG . TYR A 1 235 ? 27.978 39.498 27.905 1.00 22.97 ? 228 TYR A CG 1 ATOM 1436 C CD1 . TYR A 1 235 ? 29.222 39.148 28.433 1.00 21.60 ? 228 TYR A CD1 1 ATOM 1437 C CD2 . TYR A 1 235 ? 27.890 40.631 27.084 1.00 22.73 ? 228 TYR A CD2 1 ATOM 1438 C CE1 . TYR A 1 235 ? 30.368 39.921 28.120 1.00 24.76 ? 228 TYR A CE1 1 ATOM 1439 C CE2 . TYR A 1 235 ? 29.014 41.398 26.766 1.00 24.26 ? 228 TYR A CE2 1 ATOM 1440 C CZ . TYR A 1 235 ? 30.245 41.046 27.303 1.00 23.74 ? 228 TYR A CZ 1 ATOM 1441 O OH . TYR A 1 235 ? 31.327 41.831 27.024 1.00 26.15 ? 228 TYR A OH 1 ATOM 1442 N N . SER A 1 236 ? 27.288 38.811 31.302 1.00 24.74 ? 229 SER A N 1 ATOM 1443 C CA . SER A 1 236 ? 28.209 39.092 32.400 1.00 24.18 ? 229 SER A CA 1 ATOM 1444 C C . SER A 1 236 ? 29.658 38.910 31.944 1.00 24.65 ? 229 SER A C 1 ATOM 1445 O O . SER A 1 236 ? 30.108 37.777 31.714 1.00 24.75 ? 229 SER A O 1 ATOM 1446 C CB . SER A 1 236 ? 27.892 38.206 33.619 1.00 23.31 ? 229 SER A CB 1 ATOM 1447 O OG . SER A 1 236 ? 26.542 38.356 34.019 1.00 22.29 ? 229 SER A OG 1 ATOM 1448 N N . ASP A 1 237 ? 30.382 40.021 31.820 1.00 24.74 ? 230 ASP A N 1 ATOM 1449 C CA . ASP A 1 237 ? 31.781 39.948 31.430 1.00 25.51 ? 230 ASP A CA 1 ATOM 1450 C C . ASP A 1 237 ? 32.666 39.608 32.640 1.00 25.46 ? 230 ASP A C 1 ATOM 1451 O O . ASP A 1 237 ? 32.482 40.196 33.707 1.00 25.42 ? 230 ASP A O 1 ATOM 1452 C CB . ASP A 1 237 ? 32.239 41.267 30.775 1.00 25.10 ? 230 ASP A CB 1 ATOM 1453 C CG . ASP A 1 237 ? 33.516 41.083 29.921 1.00 27.12 ? 230 ASP A CG 1 ATOM 1454 O OD1 . ASP A 1 237 ? 33.417 41.091 28.661 1.00 27.89 ? 230 ASP A OD1 1 ATOM 1455 O OD2 . ASP A 1 237 ? 34.606 40.895 30.506 1.00 27.48 ? 230 ASP A OD2 1 ATOM 1456 N N . PRO A 1 238 ? 33.646 38.681 32.478 1.00 26.75 ? 231 PRO A N 1 ATOM 1457 C CA . PRO A 1 238 ? 34.548 38.412 33.611 1.00 27.21 ? 231 PRO A CA 1 ATOM 1458 C C . PRO A 1 238 ? 35.240 39.682 34.132 1.00 28.28 ? 231 PRO A C 1 ATOM 1459 O O . PRO A 1 238 ? 35.571 39.753 35.332 1.00 27.95 ? 231 PRO A O 1 ATOM 1460 C CB . PRO A 1 238 ? 35.621 37.478 33.026 1.00 28.31 ? 231 PRO A CB 1 ATOM 1461 C CG . PRO A 1 238 ? 35.088 37.014 31.709 1.00 27.31 ? 231 PRO A CG 1 ATOM 1462 C CD . PRO A 1 238 ? 33.945 37.853 31.290 1.00 25.94 ? 231 PRO A CD 1 ATOM 1463 N N . ALA A 1 239 ? 35.435 40.691 33.279 1.00 28.16 ? 232 ALA A N 1 ATOM 1464 C CA . ALA A 1 239 ? 36.019 41.948 33.799 1.00 29.56 ? 232 ALA A CA 1 ATOM 1465 C C . ALA A 1 239 ? 35.177 42.538 34.964 1.00 29.16 ? 232 ALA A C 1 ATOM 1466 O O . ALA A 1 239 ? 35.717 43.121 35.929 1.00 28.86 ? 232 ALA A O 1 ATOM 1467 C CB . ALA A 1 239 ? 36.213 42.985 32.669 1.00 30.32 ? 232 ALA A CB 1 ATOM 1468 N N . ASP A 1 240 ? 33.860 42.333 34.904 1.00 28.65 ? 233 ASP A N 1 ATOM 1469 C CA . ASP A 1 240 ? 32.950 42.888 35.905 1.00 27.64 ? 233 ASP A CA 1 ATOM 1470 C C . ASP A 1 240 ? 32.453 41.882 36.932 1.00 27.34 ? 233 ASP A C 1 ATOM 1471 O O . ASP A 1 240 ? 31.919 42.299 37.987 1.00 27.28 ? 233 ASP A O 1 ATOM 1472 C CB . ASP A 1 240 ? 31.771 43.577 35.211 1.00 26.92 ? 233 ASP A CB 1 ATOM 1473 C CG . ASP A 1 240 ? 32.246 44.529 34.135 1.00 27.41 ? 233 ASP A CG 1 ATOM 1474 O OD1 . ASP A 1 240 ? 32.715 45.619 34.530 1.00 26.84 ? 233 ASP A OD1 1 ATOM 1475 O OD2 . ASP A 1 240 ? 32.213 44.160 32.927 1.00 25.23 ? 233 ASP A OD2 1 ATOM 1476 N N . TYR A 1 241 ? 32.572 40.585 36.631 1.00 25.26 ? 234 TYR A N 1 ATOM 1477 C CA . TYR A 1 241 ? 32.011 39.573 37.539 1.00 26.02 ? 234 TYR A CA 1 ATOM 1478 C C . TYR A 1 241 ? 32.962 38.436 37.919 1.00 26.78 ? 234 TYR A C 1 ATOM 1479 O O . TYR A 1 241 ? 32.509 37.389 38.366 1.00 27.61 ? 234 TYR A O 1 ATOM 1480 C CB . TYR A 1 241 ? 30.730 38.984 36.935 1.00 24.93 ? 234 TYR A CB 1 ATOM 1481 C CG . TYR A 1 241 ? 29.662 40.057 36.878 1.00 25.11 ? 234 TYR A CG 1 ATOM 1482 C CD1 . TYR A 1 241 ? 29.461 40.819 35.706 1.00 23.29 ? 234 TYR A CD1 1 ATOM 1483 C CD2 . TYR A 1 241 ? 28.888 40.344 38.014 1.00 23.01 ? 234 TYR A CD2 1 ATOM 1484 C CE1 . TYR A 1 241 ? 28.498 41.847 35.668 1.00 21.27 ? 234 TYR A CE1 1 ATOM 1485 C CE2 . TYR A 1 241 ? 27.927 41.364 37.994 1.00 25.68 ? 234 TYR A CE2 1 ATOM 1486 C CZ . TYR A 1 241 ? 27.738 42.108 36.813 1.00 24.07 ? 234 TYR A CZ 1 ATOM 1487 O OH . TYR A 1 241 ? 26.777 43.073 36.804 1.00 21.59 ? 234 TYR A OH 1 ATOM 1488 N N . PHE A 1 242 ? 34.259 38.624 37.721 1.00 27.56 ? 235 PHE A N 1 ATOM 1489 C CA . PHE A 1 242 ? 35.222 37.569 38.078 1.00 28.73 ? 235 PHE A CA 1 ATOM 1490 C C . PHE A 1 242 ? 36.397 38.286 38.718 1.00 29.97 ? 235 PHE A C 1 ATOM 1491 O O . PHE A 1 242 ? 37.222 38.894 38.018 1.00 29.04 ? 235 PHE A O 1 ATOM 1492 C CB . PHE A 1 242 ? 35.652 36.787 36.851 1.00 28.37 ? 235 PHE A CB 1 ATOM 1493 C CG . PHE A 1 242 ? 36.424 35.520 37.166 1.00 28.14 ? 235 PHE A CG 1 ATOM 1494 C CD1 . PHE A 1 242 ? 35.749 34.306 37.286 1.00 27.88 ? 235 PHE A CD1 1 ATOM 1495 C CD2 . PHE A 1 242 ? 37.799 35.560 37.377 1.00 27.46 ? 235 PHE A CD2 1 ATOM 1496 C CE1 . PHE A 1 242 ? 36.429 33.099 37.551 1.00 28.43 ? 235 PHE A CE1 1 ATOM 1497 C CE2 . PHE A 1 242 ? 38.535 34.353 37.659 1.00 29.48 ? 235 PHE A CE2 1 ATOM 1498 C CZ . PHE A 1 242 ? 37.825 33.109 37.761 1.00 28.96 ? 235 PHE A CZ 1 ATOM 1499 N N . ALA A 1 243 ? 36.427 38.279 40.046 1.00 31.31 ? 236 ALA A N 1 ATOM 1500 C CA . ALA A 1 243 ? 37.517 38.918 40.777 1.00 33.21 ? 236 ALA A CA 1 ATOM 1501 C C . ALA A 1 243 ? 38.847 38.143 40.600 1.00 34.67 ? 236 ALA A C 1 ATOM 1502 O O . ALA A 1 243 ? 38.879 36.915 40.717 1.00 34.03 ? 236 ALA A O 1 ATOM 1503 C CB . ALA A 1 243 ? 37.142 39.032 42.243 1.00 33.58 ? 236 ALA A CB 1 ATOM 1504 N N . PRO A 1 244 ? 39.944 38.857 40.290 1.00 36.63 ? 237 PRO A N 1 ATOM 1505 C CA . PRO A 1 244 ? 41.222 38.174 40.094 1.00 37.41 ? 237 PRO A CA 1 ATOM 1506 C C . PRO A 1 244 ? 41.630 37.310 41.303 1.00 37.70 ? 237 PRO A C 1 ATOM 1507 O O . PRO A 1 244 ? 41.416 37.718 42.454 1.00 37.68 ? 237 PRO A O 1 ATOM 1508 C CB . PRO A 1 244 ? 42.227 39.332 39.886 1.00 38.31 ? 237 PRO A CB 1 ATOM 1509 C CG . PRO A 1 244 ? 41.386 40.524 39.498 1.00 39.21 ? 237 PRO A CG 1 ATOM 1510 C CD . PRO A 1 244 ? 40.066 40.334 40.213 1.00 36.97 ? 237 PRO A CD 1 ATOM 1511 N N . GLY A 1 245 ? 42.175 36.120 41.040 1.00 37.18 ? 238 GLY A N 1 ATOM 1512 C CA . GLY A 1 245 ? 42.695 35.238 42.096 1.00 37.07 ? 238 GLY A CA 1 ATOM 1513 C C . GLY A 1 245 ? 41.677 34.480 42.947 1.00 37.06 ? 238 GLY A C 1 ATOM 1514 O O . GLY A 1 245 ? 42.065 33.782 43.895 1.00 37.97 ? 238 GLY A O 1 ATOM 1515 N N . VAL A 1 246 ? 40.385 34.559 42.605 1.00 35.06 ? 239 VAL A N 1 ATOM 1516 C CA . VAL A 1 246 ? 39.341 33.786 43.315 1.00 33.17 ? 239 VAL A CA 1 ATOM 1517 C C . VAL A 1 246 ? 38.737 32.741 42.364 1.00 33.19 ? 239 VAL A C 1 ATOM 1518 O O . VAL A 1 246 ? 38.685 32.950 41.158 1.00 33.69 ? 239 VAL A O 1 ATOM 1519 C CB . VAL A 1 246 ? 38.284 34.735 44.088 1.00 33.46 ? 239 VAL A CB 1 ATOM 1520 C CG1 A VAL A 1 246 ? 38.696 36.205 44.039 0.50 32.25 ? 239 VAL A CG1 1 ATOM 1521 C CG1 B VAL A 1 246 ? 37.069 33.934 44.637 0.50 31.14 ? 239 VAL A CG1 1 ATOM 1522 C CG2 A VAL A 1 246 ? 36.816 34.465 43.755 0.50 31.85 ? 239 VAL A CG2 1 ATOM 1523 C CG2 B VAL A 1 246 ? 38.965 35.579 45.171 0.50 32.20 ? 239 VAL A CG2 1 ATOM 1524 N N . LYS A 1 247 ? 38.344 31.595 42.898 1.00 32.54 ? 240 LYS A N 1 ATOM 1525 C CA . LYS A 1 247 ? 37.808 30.526 42.070 1.00 33.11 ? 240 LYS A CA 1 ATOM 1526 C C . LYS A 1 247 ? 36.299 30.737 41.811 1.00 32.31 ? 240 LYS A C 1 ATOM 1527 O O . LYS A 1 247 ? 35.619 31.400 42.585 1.00 31.48 ? 240 LYS A O 1 ATOM 1528 C CB . LYS A 1 247 ? 38.063 29.158 42.726 1.00 33.20 ? 240 LYS A CB 1 ATOM 1529 C CG . LYS A 1 247 ? 39.548 28.639 42.717 1.00 34.86 ? 240 LYS A CG 1 ATOM 1530 C CD . LYS A 1 247 ? 40.085 28.415 41.295 0.65 35.93 ? 240 LYS A CD 1 ATOM 1531 C CE . LYS A 1 247 ? 41.498 27.824 41.288 0.50 37.55 ? 240 LYS A CE 1 ATOM 1532 N NZ . LYS A 1 247 ? 42.149 28.019 39.944 0.70 37.20 ? 240 LYS A NZ 1 ATOM 1533 N N . SER A 1 248 ? 35.826 30.206 40.683 1.00 32.41 ? 241 SER A N 1 ATOM 1534 C CA . SER A 1 248 ? 34.411 30.088 40.331 1.00 32.17 ? 241 SER A CA 1 ATOM 1535 C C . SER A 1 248 ? 33.671 29.229 41.344 1.00 30.88 ? 241 SER A C 1 ATOM 1536 O O . SER A 1 248 ? 34.232 28.233 41.828 1.00 28.93 ? 241 SER A O 1 ATOM 1537 C CB . SER A 1 248 ? 34.338 29.271 39.019 1.00 33.73 ? 241 SER A CB 1 ATOM 1538 O OG . SER A 1 248 ? 34.570 30.087 37.913 1.00 36.53 ? 241 SER A OG 1 ATOM 1539 N N . TYR A 1 249 ? 32.394 29.541 41.586 1.00 30.16 ? 242 TYR A N 1 ATOM 1540 C CA . TYR A 1 249 ? 31.499 28.648 42.342 1.00 29.31 ? 242 TYR A CA 1 ATOM 1541 C C . TYR A 1 249 ? 31.505 27.234 41.719 1.00 29.65 ? 242 TYR A C 1 ATOM 1542 O O . TYR A 1 249 ? 31.498 27.122 40.509 1.00 28.98 ? 242 TYR A O 1 ATOM 1543 C CB . TYR A 1 249 ? 30.062 29.228 42.411 1.00 28.53 ? 242 TYR A CB 1 ATOM 1544 C CG . TYR A 1 249 ? 29.313 28.647 43.590 1.00 27.64 ? 242 TYR A CG 1 ATOM 1545 C CD1 . TYR A 1 249 ? 29.540 29.125 44.903 1.00 26.20 ? 242 TYR A CD1 1 ATOM 1546 C CD2 . TYR A 1 249 ? 28.459 27.542 43.417 1.00 28.67 ? 242 TYR A CD2 1 ATOM 1547 C CE1 . TYR A 1 249 ? 28.909 28.532 46.015 1.00 27.78 ? 242 TYR A CE1 1 ATOM 1548 C CE2 . TYR A 1 249 ? 27.809 26.946 44.531 1.00 30.77 ? 242 TYR A CE2 1 ATOM 1549 C CZ . TYR A 1 249 ? 28.049 27.445 45.819 1.00 30.24 ? 242 TYR A CZ 1 ATOM 1550 O OH . TYR A 1 249 ? 27.386 26.837 46.858 1.00 35.43 ? 242 TYR A OH 1 ATOM 1551 N N . PRO A 1 250 ? 31.510 26.152 42.533 1.00 30.50 ? 243 PRO A N 1 ATOM 1552 C CA . PRO A 1 250 ? 31.398 26.028 44.013 1.00 31.17 ? 243 PRO A CA 1 ATOM 1553 C C . PRO A 1 250 ? 32.723 26.195 44.820 1.00 31.76 ? 243 PRO A C 1 ATOM 1554 O O . PRO A 1 250 ? 32.706 26.074 46.062 1.00 31.92 ? 243 PRO A O 1 ATOM 1555 C CB . PRO A 1 250 ? 30.902 24.582 44.182 1.00 30.92 ? 243 PRO A CB 1 ATOM 1556 C CG . PRO A 1 250 ? 31.648 23.840 43.048 1.00 30.63 ? 243 PRO A CG 1 ATOM 1557 C CD . PRO A 1 250 ? 31.541 24.815 41.875 1.00 30.64 ? 243 PRO A CD 1 ATOM 1558 N N . ASP A 1 251 ? 33.840 26.449 44.147 1.00 30.84 ? 244 ASP A N 1 ATOM 1559 C CA . ASP A 1 251 ? 35.120 26.464 44.853 1.00 32.11 ? 244 ASP A CA 1 ATOM 1560 C C . ASP A 1 251 ? 35.539 27.843 45.343 1.00 31.21 ? 244 ASP A C 1 ATOM 1561 O O . ASP A 1 251 ? 36.545 27.959 46.033 1.00 31.07 ? 244 ASP A O 1 ATOM 1562 C CB . ASP A 1 251 ? 36.238 25.868 44.006 1.00 32.93 ? 244 ASP A CB 1 ATOM 1563 C CG . ASP A 1 251 ? 35.930 24.433 43.557 1.00 37.42 ? 244 ASP A CG 1 ATOM 1564 O OD1 . ASP A 1 251 ? 35.529 23.569 44.390 1.00 39.06 ? 244 ASP A OD1 1 ATOM 1565 O OD2 . ASP A 1 251 ? 36.072 24.180 42.347 1.00 43.57 ? 244 ASP A OD2 1 ATOM 1566 N N . GLY A 1 252 ? 34.765 28.871 44.994 1.00 29.20 ? 245 GLY A N 1 ATOM 1567 C CA . GLY A 1 252 ? 35.054 30.222 45.395 1.00 28.18 ? 245 GLY A CA 1 ATOM 1568 C C . GLY A 1 252 ? 33.806 31.004 45.058 1.00 27.85 ? 245 GLY A C 1 ATOM 1569 O O . GLY A 1 252 ? 32.764 30.418 44.686 1.00 28.07 ? 245 GLY A O 1 ATOM 1570 N N . TRP A 1 253 ? 33.887 32.317 45.186 1.00 26.38 ? 246 TRP A N 1 ATOM 1571 C CA . TRP A 1 253 ? 32.670 33.105 45.085 1.00 26.00 ? 246 TRP A CA 1 ATOM 1572 C C . TRP A 1 253 ? 32.516 33.811 43.721 1.00 26.10 ? 246 TRP A C 1 ATOM 1573 O O . TRP A 1 253 ? 31.634 34.701 43.554 1.00 25.62 ? 246 TRP A O 1 ATOM 1574 C CB . TRP A 1 253 ? 32.548 34.088 46.271 1.00 25.84 ? 246 TRP A CB 1 ATOM 1575 C CG . TRP A 1 253 ? 33.807 34.839 46.611 1.00 26.99 ? 246 TRP A CG 1 ATOM 1576 C CD1 . TRP A 1 253 ? 34.787 34.448 47.490 1.00 28.70 ? 246 TRP A CD1 1 ATOM 1577 C CD2 . TRP A 1 253 ? 34.222 36.108 46.086 1.00 28.77 ? 246 TRP A CD2 1 ATOM 1578 N NE1 . TRP A 1 253 ? 35.786 35.402 47.543 1.00 29.06 ? 246 TRP A NE1 1 ATOM 1579 C CE2 . TRP A 1 253 ? 35.468 36.429 46.694 1.00 29.20 ? 246 TRP A CE2 1 ATOM 1580 C CE3 . TRP A 1 253 ? 33.675 36.998 45.145 1.00 28.19 ? 246 TRP A CE3 1 ATOM 1581 C CZ2 . TRP A 1 253 ? 36.174 37.616 46.409 1.00 29.49 ? 246 TRP A CZ2 1 ATOM 1582 C CZ3 . TRP A 1 253 ? 34.390 38.202 44.855 1.00 30.41 ? 246 TRP A CZ3 1 ATOM 1583 C CH2 . TRP A 1 253 ? 35.639 38.482 45.487 1.00 28.64 ? 246 TRP A CH2 1 ATOM 1584 N N . ASN A 1 254 ? 33.355 33.430 42.751 1.00 25.72 ? 247 ASN A N 1 ATOM 1585 C CA . ASN A 1 254 ? 33.240 33.996 41.380 1.00 26.42 ? 247 ASN A CA 1 ATOM 1586 C C . ASN A 1 254 ? 32.155 33.360 40.533 1.00 26.24 ? 247 ASN A C 1 ATOM 1587 O O . ASN A 1 254 ? 31.766 32.204 40.780 1.00 25.63 ? 247 ASN A O 1 ATOM 1588 C CB . ASN A 1 254 ? 34.571 33.907 40.600 1.00 26.09 ? 247 ASN A CB 1 ATOM 1589 C CG . ASN A 1 254 ? 35.448 35.147 40.831 1.00 26.34 ? 247 ASN A CG 1 ATOM 1590 O OD1 . ASN A 1 254 ? 34.949 36.226 41.234 1.00 26.59 ? 247 ASN A OD1 1 ATOM 1591 N ND2 . ASN A 1 254 ? 36.755 34.992 40.628 1.00 24.71 ? 247 ASN A ND2 1 ATOM 1592 N N . LEU A 1 255 ? 31.734 34.114 39.509 1.00 25.58 ? 248 LEU A N 1 ATOM 1593 C CA . LEU A 1 255 ? 30.746 33.677 38.516 1.00 25.58 ? 248 LEU A CA 1 ATOM 1594 C C . LEU A 1 255 ? 31.395 32.741 37.503 1.00 25.81 ? 248 LEU A C 1 ATOM 1595 O O . LEU A 1 255 ? 32.393 33.111 36.865 1.00 25.69 ? 248 LEU A O 1 ATOM 1596 C CB . LEU A 1 255 ? 30.131 34.890 37.793 1.00 25.17 ? 248 LEU A CB 1 ATOM 1597 C CG . LEU A 1 255 ? 28.988 34.554 36.818 1.00 25.08 ? 248 LEU A CG 1 ATOM 1598 C CD1 . LEU A 1 255 ? 27.716 34.106 37.560 1.00 21.85 ? 248 LEU A CD1 1 ATOM 1599 C CD2 . LEU A 1 255 ? 28.694 35.771 35.944 1.00 26.46 ? 248 LEU A CD2 1 ATOM 1600 N N . PRO A 1 256 ? 30.852 31.507 37.364 1.00 25.61 ? 249 PRO A N 1 ATOM 1601 C CA . PRO A 1 256 ? 31.322 30.627 36.310 1.00 25.59 ? 249 PRO A CA 1 ATOM 1602 C C . PRO A 1 256 ? 30.847 31.056 34.924 1.00 25.24 ? 249 PRO A C 1 ATOM 1603 O O . PRO A 1 256 ? 29.872 31.830 34.819 1.00 24.88 ? 249 PRO A O 1 ATOM 1604 C CB . PRO A 1 256 ? 30.721 29.254 36.671 1.00 25.94 ? 249 PRO A CB 1 ATOM 1605 C CG . PRO A 1 256 ? 29.735 29.498 37.644 1.00 26.84 ? 249 PRO A CG 1 ATOM 1606 C CD . PRO A 1 256 ? 29.916 30.843 38.281 1.00 25.41 ? 249 PRO A CD 1 ATOM 1607 N N . GLY A 1 257 ? 31.484 30.504 33.882 1.00 25.00 ? 250 GLY A N 1 ATOM 1608 C CA . GLY A 1 257 ? 31.159 30.866 32.484 1.00 25.45 ? 250 GLY A CA 1 ATOM 1609 C C . GLY A 1 257 ? 29.717 30.532 32.106 1.00 26.05 ? 250 GLY A C 1 ATOM 1610 O O . GLY A 1 257 ? 29.152 31.103 31.157 1.00 26.15 ? 250 GLY A O 1 ATOM 1611 N N . GLY A 1 258 ? 29.135 29.583 32.835 1.00 25.21 ? 251 GLY A N 1 ATOM 1612 C CA . GLY A 1 258 ? 27.751 29.149 32.589 1.00 25.20 ? 251 GLY A CA 1 ATOM 1613 C C . GLY A 1 258 ? 26.756 29.922 33.455 1.00 24.29 ? 251 GLY A C 1 ATOM 1614 O O . GLY A 1 258 ? 25.569 29.770 33.277 1.00 24.54 ? 251 GLY A O 1 ATOM 1615 N N . GLY A 1 259 ? 27.246 30.739 34.388 1.00 23.64 ? 252 GLY A N 1 ATOM 1616 C CA . GLY A 1 259 ? 26.395 31.544 35.291 1.00 22.35 ? 252 GLY A CA 1 ATOM 1617 C C . GLY A 1 259 ? 25.729 32.702 34.549 1.00 22.09 ? 252 GLY A C 1 ATOM 1618 O O . GLY A 1 259 ? 26.298 33.272 33.611 1.00 21.82 ? 252 GLY A O 1 ATOM 1619 N N . VAL A 1 260 ? 24.516 33.035 34.962 1.00 21.91 ? 253 VAL A N 1 ATOM 1620 C CA . VAL A 1 260 ? 23.710 34.094 34.320 1.00 20.94 ? 253 VAL A CA 1 ATOM 1621 C C . VAL A 1 260 ? 22.911 34.874 35.358 1.00 21.56 ? 253 VAL A C 1 ATOM 1622 O O . VAL A 1 260 ? 22.273 34.298 36.263 1.00 20.64 ? 253 VAL A O 1 ATOM 1623 C CB . VAL A 1 260 ? 22.679 33.531 33.286 1.00 20.83 ? 253 VAL A CB 1 ATOM 1624 C CG1 . VAL A 1 260 ? 22.039 34.642 32.493 1.00 19.40 ? 253 VAL A CG1 1 ATOM 1625 C CG2 . VAL A 1 260 ? 23.340 32.519 32.300 1.00 20.03 ? 253 VAL A CG2 1 ATOM 1626 N N . GLN A 1 261 ? 22.895 36.189 35.168 1.00 21.19 ? 254 GLN A N 1 ATOM 1627 C CA . GLN A 1 261 ? 22.231 37.103 36.064 1.00 20.20 ? 254 GLN A CA 1 ATOM 1628 C C . GLN A 1 261 ? 20.785 37.309 35.573 1.00 20.50 ? 254 GLN A C 1 ATOM 1629 O O . GLN A 1 261 ? 20.553 37.889 34.468 1.00 20.50 ? 254 GLN A O 1 ATOM 1630 C CB . GLN A 1 261 ? 23.002 38.446 36.081 1.00 20.20 ? 254 GLN A CB 1 ATOM 1631 C CG . GLN A 1 261 ? 22.294 39.545 36.926 1.00 18.78 ? 254 GLN A CG 1 ATOM 1632 C CD . GLN A 1 261 ? 22.889 40.942 36.736 1.00 20.17 ? 254 GLN A CD 1 ATOM 1633 O OE1 . GLN A 1 261 ? 22.148 41.936 36.719 1.00 19.53 ? 254 GLN A OE1 1 ATOM 1634 N NE2 . GLN A 1 261 ? 24.242 41.036 36.654 1.00 18.97 ? 254 GLN A NE2 1 ATOM 1635 N N . ARG A 1 262 ? 19.810 36.842 36.366 1.00 18.89 ? 255 ARG A N 1 ATOM 1636 C CA . ARG A 1 262 ? 18.388 37.199 36.095 1.00 19.64 ? 255 ARG A CA 1 ATOM 1637 C C . ARG A 1 262 ? 18.096 38.655 36.432 1.00 19.09 ? 255 ARG A C 1 ATOM 1638 O O . ARG A 1 262 ? 18.905 39.332 37.098 1.00 19.80 ? 255 ARG A O 1 ATOM 1639 C CB . ARG A 1 262 ? 17.431 36.291 36.869 1.00 18.07 ? 255 ARG A CB 1 ATOM 1640 C CG . ARG A 1 262 ? 17.454 34.825 36.315 1.00 19.57 ? 255 ARG A CG 1 ATOM 1641 C CD . ARG A 1 262 ? 17.025 33.828 37.413 1.00 19.90 ? 255 ARG A CD 1 ATOM 1642 N NE . ARG A 1 262 ? 17.279 32.435 37.058 1.00 19.21 ? 255 ARG A NE 1 ATOM 1643 C CZ . ARG A 1 262 ? 18.483 31.858 37.049 1.00 19.13 ? 255 ARG A CZ 1 ATOM 1644 N NH1 . ARG A 1 262 ? 19.558 32.575 37.391 1.00 17.16 ? 255 ARG A NH1 1 ATOM 1645 N NH2 . ARG A 1 262 ? 18.613 30.562 36.702 1.00 18.81 ? 255 ARG A NH2 1 ATOM 1646 N N . GLY A 1 263 ? 16.937 39.158 35.985 1.00 19.01 ? 256 GLY A N 1 ATOM 1647 C CA . GLY A 1 263 ? 16.473 40.451 36.531 1.00 17.50 ? 256 GLY A CA 1 ATOM 1648 C C . GLY A 1 263 ? 15.495 41.156 35.591 1.00 17.52 ? 256 GLY A C 1 ATOM 1649 O O . GLY A 1 263 ? 15.555 40.987 34.342 1.00 17.34 ? 256 GLY A O 1 ATOM 1650 N N . ASN A 1 264 ? 14.584 41.940 36.179 1.00 16.78 ? 257 ASN A N 1 ATOM 1651 C CA . ASN A 1 264 ? 13.565 42.631 35.369 1.00 16.42 ? 257 ASN A CA 1 ATOM 1652 C C . ASN A 1 264 ? 14.250 43.809 34.618 1.00 16.62 ? 257 ASN A C 1 ATOM 1653 O O . ASN A 1 264 ? 15.309 44.313 35.056 1.00 16.14 ? 257 ASN A O 1 ATOM 1654 C CB . ASN A 1 264 ? 12.349 43.108 36.210 1.00 15.94 ? 257 ASN A CB 1 ATOM 1655 C CG . ASN A 1 264 ? 12.602 44.456 36.933 1.00 17.60 ? 257 ASN A CG 1 ATOM 1656 O OD1 . ASN A 1 264 ? 12.618 45.511 36.309 1.00 18.65 ? 257 ASN A OD1 1 ATOM 1657 N ND2 . ASN A 1 264 ? 12.792 44.405 38.261 1.00 17.42 ? 257 ASN A ND2 1 ATOM 1658 N N . ILE A 1 265 ? 13.640 44.224 33.511 1.00 16.21 ? 258 ILE A N 1 ATOM 1659 C CA . ILE A 1 265 ? 14.145 45.290 32.654 1.00 17.17 ? 258 ILE A CA 1 ATOM 1660 C C . ILE A 1 265 ? 13.074 46.389 32.438 1.00 18.45 ? 258 ILE A C 1 ATOM 1661 O O . ILE A 1 265 ? 12.991 47.017 31.319 1.00 18.43 ? 258 ILE A O 1 ATOM 1662 C CB . ILE A 1 265 ? 14.529 44.684 31.282 1.00 17.66 ? 258 ILE A CB 1 ATOM 1663 C CG1 . ILE A 1 265 ? 13.366 43.822 30.731 1.00 19.15 ? 258 ILE A CG1 1 ATOM 1664 C CG2 . ILE A 1 265 ? 15.864 43.869 31.383 1.00 18.07 ? 258 ILE A CG2 1 ATOM 1665 C CD1 . ILE A 1 265 ? 13.609 43.401 29.176 1.00 21.38 ? 258 ILE A CD1 1 ATOM 1666 N N . LEU A 1 266 ? 12.249 46.588 33.472 1.00 17.86 ? 259 LEU A N 1 ATOM 1667 C CA . LEU A 1 266 ? 11.191 47.628 33.460 1.00 18.72 ? 259 LEU A CA 1 ATOM 1668 C C . LEU A 1 266 ? 11.773 49.010 33.651 1.00 18.73 ? 259 LEU A C 1 ATOM 1669 O O . LEU A 1 266 ? 12.856 49.129 34.208 1.00 19.52 ? 259 LEU A O 1 ATOM 1670 C CB . LEU A 1 266 ? 10.192 47.421 34.610 1.00 17.70 ? 259 LEU A CB 1 ATOM 1671 C CG . LEU A 1 266 ? 9.351 46.118 34.493 1.00 18.54 ? 259 LEU A CG 1 ATOM 1672 C CD1 . LEU A 1 266 ? 8.493 45.969 35.715 1.00 19.28 ? 259 LEU A CD1 1 ATOM 1673 C CD2 . LEU A 1 266 ? 8.486 46.123 33.262 1.00 18.94 ? 259 LEU A CD2 1 ATOM 1674 N N . ASN A 1 267 ? 11.007 50.049 33.271 1.00 18.68 ? 260 ASN A N 1 ATOM 1675 C CA . ASN A 1 267 ? 11.319 51.429 33.668 1.00 18.24 ? 260 ASN A CA 1 ATOM 1676 C C . ASN A 1 267 ? 10.056 51.987 34.289 1.00 17.82 ? 260 ASN A C 1 ATOM 1677 O O . ASN A 1 267 ? 9.338 52.765 33.658 1.00 18.49 ? 260 ASN A O 1 ATOM 1678 C CB . ASN A 1 267 ? 11.768 52.253 32.428 1.00 18.99 ? 260 ASN A CB 1 ATOM 1679 C CG . ASN A 1 267 ? 13.215 51.942 32.040 1.00 21.20 ? 260 ASN A CG 1 ATOM 1680 O OD1 . ASN A 1 267 ? 14.156 52.572 32.573 1.00 23.97 ? 260 ASN A OD1 1 ATOM 1681 N ND2 . ASN A 1 267 ? 13.411 50.954 31.131 1.00 21.20 ? 260 ASN A ND2 1 ATOM 1682 N N . LEU A 1 268 ? 9.775 51.566 35.515 1.00 16.78 ? 261 LEU A N 1 ATOM 1683 C CA . LEU A 1 268 ? 8.529 51.928 36.219 1.00 16.95 ? 261 LEU A CA 1 ATOM 1684 C C . LEU A 1 268 ? 8.561 53.363 36.762 1.00 17.27 ? 261 LEU A C 1 ATOM 1685 O O . LEU A 1 268 ? 7.492 53.961 37.017 1.00 16.45 ? 261 LEU A O 1 ATOM 1686 C CB . LEU A 1 268 ? 8.354 51.000 37.426 1.00 16.13 ? 261 LEU A CB 1 ATOM 1687 C CG . LEU A 1 268 ? 8.060 49.567 36.987 1.00 15.18 ? 261 LEU A CG 1 ATOM 1688 C CD1 . LEU A 1 268 ? 7.941 48.667 38.244 1.00 15.78 ? 261 LEU A CD1 1 ATOM 1689 C CD2 . LEU A 1 268 ? 6.732 49.594 36.208 1.00 15.65 ? 261 LEU A CD2 1 ATOM 1690 N N . ASN A 1 269 ? 9.773 53.874 37.017 1.00 16.61 ? 262 ASN A N 1 ATOM 1691 C CA . ASN A 1 269 ? 9.921 55.200 37.658 1.00 17.29 ? 262 ASN A CA 1 ATOM 1692 C C . ASN A 1 269 ? 9.036 55.357 38.916 1.00 17.25 ? 262 ASN A C 1 ATOM 1693 O O . ASN A 1 269 ? 8.387 56.416 39.132 1.00 17.54 ? 262 ASN A O 1 ATOM 1694 C CB . ASN A 1 269 ? 9.633 56.334 36.647 1.00 17.02 ? 262 ASN A CB 1 ATOM 1695 C CG . ASN A 1 269 ? 10.658 56.393 35.521 1.00 19.35 ? 262 ASN A CG 1 ATOM 1696 O OD1 . ASN A 1 269 ? 11.878 56.154 35.744 1.00 21.24 ? 262 ASN A OD1 1 ATOM 1697 N ND2 . ASN A 1 269 ? 10.188 56.711 34.297 1.00 19.39 ? 262 ASN A ND2 1 ATOM 1698 N N . GLY A 1 270 ? 8.989 54.306 39.735 1.00 16.18 ? 263 GLY A N 1 ATOM 1699 C CA . GLY A 1 270 ? 8.252 54.381 40.995 1.00 15.84 ? 263 GLY A CA 1 ATOM 1700 C C . GLY A 1 270 ? 6.789 53.921 40.926 1.00 15.98 ? 263 GLY A C 1 ATOM 1701 O O . GLY A 1 270 ? 6.095 53.950 41.943 1.00 16.82 ? 263 GLY A O 1 ATOM 1702 N N . ALA A 1 271 ? 6.319 53.497 39.763 1.00 14.84 ? 264 ALA A N 1 ATOM 1703 C CA . ALA A 1 271 ? 4.878 53.254 39.550 1.00 15.52 ? 264 ALA A CA 1 ATOM 1704 C C . ALA A 1 271 ? 4.307 52.021 40.276 1.00 15.39 ? 264 ALA A C 1 ATOM 1705 O O . ALA A 1 271 ? 3.102 51.993 40.573 1.00 16.90 ? 264 ALA A O 1 ATOM 1706 C CB . ALA A 1 271 ? 4.515 53.159 37.993 1.00 15.49 ? 264 ALA A CB 1 ATOM 1707 N N . GLY A 1 272 ? 5.122 51.004 40.530 1.00 14.70 ? 265 GLY A N 1 ATOM 1708 C CA . GLY A 1 272 ? 4.582 49.738 41.126 1.00 14.49 ? 265 GLY A CA 1 ATOM 1709 C C . GLY A 1 272 ? 4.042 48.870 39.986 1.00 16.39 ? 265 GLY A C 1 ATOM 1710 O O . GLY A 1 272 ? 4.529 48.930 38.858 1.00 16.51 ? 265 GLY A O 1 ATOM 1711 N N . ASP A 1 273 ? 2.997 48.090 40.251 1.00 17.17 ? 266 ASP A N 1 ATOM 1712 C CA . ASP A 1 273 ? 2.373 47.258 39.219 1.00 16.84 ? 266 ASP A CA 1 ATOM 1713 C C . ASP A 1 273 ? 2.130 48.057 37.958 1.00 17.27 ? 266 ASP A C 1 ATOM 1714 O O . ASP A 1 273 ? 1.442 49.098 38.003 1.00 17.22 ? 266 ASP A O 1 ATOM 1715 C CB . ASP A 1 273 ? 1.058 46.702 39.788 1.00 17.37 ? 266 ASP A CB 1 ATOM 1716 C CG . ASP A 1 273 ? 0.155 46.060 38.738 1.00 17.63 ? 266 ASP A CG 1 ATOM 1717 O OD1 . ASP A 1 273 ? 0.650 45.287 37.865 1.00 18.58 ? 266 ASP A OD1 1 ATOM 1718 O OD2 . ASP A 1 273 ? -1.074 46.293 38.812 1.00 19.06 ? 266 ASP A OD2 1 ATOM 1719 N N . PRO A 1 274 ? 2.659 47.569 36.814 1.00 17.43 ? 267 PRO A N 1 ATOM 1720 C CA . PRO A 1 274 ? 2.527 48.277 35.564 1.00 17.49 ? 267 PRO A CA 1 ATOM 1721 C C . PRO A 1 274 ? 1.079 48.583 35.229 1.00 17.35 ? 267 PRO A C 1 ATOM 1722 O O . PRO A 1 274 ? 0.814 49.565 34.535 1.00 18.13 ? 267 PRO A O 1 ATOM 1723 C CB . PRO A 1 274 ? 3.028 47.237 34.527 1.00 18.00 ? 267 PRO A CB 1 ATOM 1724 C CG . PRO A 1 274 ? 4.125 46.546 35.243 1.00 19.22 ? 267 PRO A CG 1 ATOM 1725 C CD . PRO A 1 274 ? 3.577 46.415 36.693 1.00 17.85 ? 267 PRO A CD 1 ATOM 1726 N N . LEU A 1 275 ? 0.139 47.750 35.685 1.00 17.30 ? 268 LEU A N 1 ATOM 1727 C CA . LEU A 1 275 ? -1.267 47.952 35.288 1.00 16.98 ? 268 LEU A CA 1 ATOM 1728 C C . LEU A 1 275 ? -2.092 48.946 36.126 1.00 16.27 ? 268 LEU A C 1 ATOM 1729 O O . LEU A 1 275 ? -3.178 49.352 35.686 1.00 17.40 ? 268 LEU A O 1 ATOM 1730 C CB . LEU A 1 275 ? -2.026 46.596 35.193 1.00 16.24 ? 268 LEU A CB 1 ATOM 1731 C CG . LEU A 1 275 ? -1.316 45.557 34.292 1.00 17.13 ? 268 LEU A CG 1 ATOM 1732 C CD1 . LEU A 1 275 ? -2.188 44.288 34.206 1.00 18.81 ? 268 LEU A CD1 1 ATOM 1733 C CD2 . LEU A 1 275 ? -1.046 46.121 32.887 1.00 19.42 ? 268 LEU A CD2 1 ATOM 1734 N N . THR A 1 276 ? -1.632 49.312 37.319 1.00 16.26 ? 269 THR A N 1 ATOM 1735 C CA . THR A 1 276 ? -2.480 50.090 38.279 1.00 16.07 ? 269 THR A CA 1 ATOM 1736 C C . THR A 1 276 ? -1.746 51.251 38.950 1.00 16.31 ? 269 THR A C 1 ATOM 1737 O O . THR A 1 276 ? -1.783 51.355 40.207 1.00 17.46 ? 269 THR A O 1 ATOM 1738 C CB . THR A 1 276 ? -2.955 49.175 39.472 1.00 15.41 ? 269 THR A CB 1 ATOM 1739 O OG1 . THR A 1 276 ? -1.775 48.584 40.111 1.00 16.62 ? 269 THR A OG1 1 ATOM 1740 C CG2 . THR A 1 276 ? -3.917 48.086 38.955 1.00 15.04 ? 269 THR A CG2 1 ATOM 1741 N N . PRO A 1 277 ? -1.071 52.125 38.141 1.00 16.47 ? 270 PRO A N 1 ATOM 1742 C CA . PRO A 1 277 ? -0.285 53.187 38.762 1.00 16.42 ? 270 PRO A CA 1 ATOM 1743 C C . PRO A 1 277 ? -1.163 54.115 39.587 1.00 16.78 ? 270 PRO A C 1 ATOM 1744 O O . PRO A 1 277 ? -2.201 54.550 39.078 1.00 16.76 ? 270 PRO A O 1 ATOM 1745 C CB . PRO A 1 277 ? 0.312 53.963 37.572 1.00 15.56 ? 270 PRO A CB 1 ATOM 1746 C CG . PRO A 1 277 ? -0.607 53.579 36.349 1.00 15.23 ? 270 PRO A CG 1 ATOM 1747 C CD . PRO A 1 277 ? -0.958 52.127 36.656 1.00 15.89 ? 270 PRO A CD 1 ATOM 1748 N N . GLY A 1 278 ? -0.780 54.375 40.838 1.00 16.44 ? 271 GLY A N 1 ATOM 1749 C CA . GLY A 1 278 ? -1.578 55.286 41.704 1.00 15.63 ? 271 GLY A CA 1 ATOM 1750 C C . GLY A 1 278 ? -2.451 54.593 42.751 1.00 16.99 ? 271 GLY A C 1 ATOM 1751 O O . GLY A 1 278 ? -2.804 55.204 43.778 1.00 17.63 ? 271 GLY A O 1 ATOM 1752 N N . TYR A 1 279 ? -2.824 53.328 42.497 1.00 16.23 ? 272 TYR A N 1 ATOM 1753 C CA . TYR A 1 279 ? -3.894 52.670 43.253 1.00 16.45 ? 272 TYR A CA 1 ATOM 1754 C C . TYR A 1 279 ? -3.516 51.213 43.518 1.00 16.36 ? 272 TYR A C 1 ATOM 1755 O O . TYR A 1 279 ? -2.891 50.568 42.680 1.00 16.81 ? 272 TYR A O 1 ATOM 1756 C CB . TYR A 1 279 ? -5.235 52.744 42.504 1.00 16.02 ? 272 TYR A CB 1 ATOM 1757 C CG . TYR A 1 279 ? -5.537 54.176 42.136 1.00 17.65 ? 272 TYR A CG 1 ATOM 1758 C CD1 . TYR A 1 279 ? -6.118 55.051 43.076 1.00 16.76 ? 272 TYR A CD1 1 ATOM 1759 C CD2 . TYR A 1 279 ? -5.171 54.682 40.870 1.00 16.77 ? 272 TYR A CD2 1 ATOM 1760 C CE1 . TYR A 1 279 ? -6.358 56.404 42.737 1.00 16.42 ? 272 TYR A CE1 1 ATOM 1761 C CE2 . TYR A 1 279 ? -5.375 56.004 40.538 1.00 16.22 ? 272 TYR A CE2 1 ATOM 1762 C CZ . TYR A 1 279 ? -5.985 56.852 41.461 1.00 14.81 ? 272 TYR A CZ 1 ATOM 1763 O OH . TYR A 1 279 ? -6.190 58.149 41.092 1.00 15.04 ? 272 TYR A OH 1 ATOM 1764 N N . PRO A 1 280 ? -3.912 50.667 44.685 1.00 17.44 ? 273 PRO A N 1 ATOM 1765 C CA . PRO A 1 280 ? -3.506 49.262 44.912 1.00 17.69 ? 273 PRO A CA 1 ATOM 1766 C C . PRO A 1 280 ? -4.236 48.279 43.963 1.00 17.97 ? 273 PRO A C 1 ATOM 1767 O O . PRO A 1 280 ? -5.443 48.482 43.657 1.00 17.83 ? 273 PRO A O 1 ATOM 1768 C CB . PRO A 1 280 ? -3.947 48.981 46.356 1.00 17.28 ? 273 PRO A CB 1 ATOM 1769 C CG . PRO A 1 280 ? -5.106 49.967 46.562 1.00 17.79 ? 273 PRO A CG 1 ATOM 1770 C CD . PRO A 1 280 ? -4.736 51.214 45.770 1.00 17.55 ? 273 PRO A CD 1 ATOM 1771 N N . ALA A 1 281 ? -3.517 47.231 43.553 1.00 16.89 ? 274 ALA A N 1 ATOM 1772 C CA . ALA A 1 281 ? -4.036 46.206 42.638 1.00 17.49 ? 274 ALA A CA 1 ATOM 1773 C C . ALA A 1 281 ? -4.886 45.190 43.435 1.00 18.50 ? 274 ALA A C 1 ATOM 1774 O O . ALA A 1 281 ? -4.562 43.977 43.585 1.00 19.01 ? 274 ALA A O 1 ATOM 1775 C CB . ALA A 1 281 ? -2.859 45.527 41.895 1.00 16.19 ? 274 ALA A CB 1 ATOM 1776 N N . ASN A 1 282 ? -5.977 45.703 43.977 1.00 19.54 ? 275 ASN A N 1 ATOM 1777 C CA . ASN A 1 282 ? -6.877 44.912 44.793 1.00 21.79 ? 275 ASN A CA 1 ATOM 1778 C C . ASN A 1 282 ? -7.879 44.167 43.920 1.00 23.28 ? 275 ASN A C 1 ATOM 1779 O O . ASN A 1 282 ? -7.758 44.158 42.693 1.00 22.97 ? 275 ASN A O 1 ATOM 1780 C CB . ASN A 1 282 ? -7.555 45.805 45.885 1.00 21.76 ? 275 ASN A CB 1 ATOM 1781 C CG . ASN A 1 282 ? -8.378 46.942 45.289 1.00 23.17 ? 275 ASN A CG 1 ATOM 1782 O OD1 . ASN A 1 282 ? -8.891 46.821 44.165 1.00 22.50 ? 275 ASN A OD1 1 ATOM 1783 N ND2 . ASN A 1 282 ? -8.508 48.076 46.039 1.00 24.96 ? 275 ASN A ND2 1 ATOM 1784 N N C GLU A 1 283 ? -8.893 43.540 44.534 0.42 24.61 ? 276 GLU A N 1 ATOM 1785 N N D GLU A 1 283 ? -8.872 43.607 44.600 0.58 24.69 ? 276 GLU A N 1 ATOM 1786 C CA C GLU A 1 283 ? -9.817 42.625 43.829 0.42 25.95 ? 276 GLU A CA 1 ATOM 1787 C CA D GLU A 1 283 ? -9.868 42.768 44.021 0.58 25.97 ? 276 GLU A CA 1 ATOM 1788 C C C GLU A 1 283 ? -10.830 43.367 42.919 0.42 25.76 ? 276 GLU A C 1 ATOM 1789 C C D GLU A 1 283 ? -10.540 43.452 42.828 0.58 25.85 ? 276 GLU A C 1 ATOM 1790 O O C GLU A 1 283 ? -11.535 42.717 42.124 0.42 25.59 ? 276 GLU A O 1 ATOM 1791 O O D GLU A 1 283 ? -10.702 42.861 41.761 0.58 26.11 ? 276 GLU A O 1 ATOM 1792 C CB C GLU A 1 283 ? -10.568 41.713 44.838 0.42 26.60 ? 276 GLU A CB 1 ATOM 1793 C CB D GLU A 1 283 ? -10.927 42.463 45.102 0.58 26.57 ? 276 GLU A CB 1 ATOM 1794 C CG C GLU A 1 283 ? -11.385 40.527 44.250 0.62 29.74 ? 276 GLU A CG 1 ATOM 1795 C CG D GLU A 1 283 ? -10.918 41.037 45.580 0.38 27.90 ? 276 GLU A CG 1 ATOM 1796 C CD C GLU A 1 283 ? -10.489 39.379 43.844 0.62 31.72 ? 276 GLU A CD 1 ATOM 1797 C CD D GLU A 1 283 ? -9.855 40.735 46.622 0.38 29.12 ? 276 GLU A CD 1 ATOM 1798 O OE1 C GLU A 1 283 ? -9.697 38.925 44.703 0.62 29.35 ? 276 GLU A OE1 1 ATOM 1799 O OE1 D GLU A 1 283 ? -9.412 39.581 46.633 0.38 28.47 ? 276 GLU A OE1 1 ATOM 1800 O OE2 C GLU A 1 283 ? -10.582 38.963 42.665 0.62 34.07 ? 276 GLU A OE2 1 ATOM 1801 O OE2 D GLU A 1 283 ? -9.469 41.612 47.442 0.38 30.62 ? 276 GLU A OE2 1 ATOM 1802 N N . TYR A 1 284 ? -10.941 44.698 43.033 1.00 25.07 ? 277 TYR A N 1 ATOM 1803 C CA . TYR A 1 284 ? -11.843 45.397 42.078 1.00 24.82 ? 277 TYR A CA 1 ATOM 1804 C C . TYR A 1 284 ? -11.133 46.408 41.228 1.00 24.17 ? 277 TYR A C 1 ATOM 1805 O O . TYR A 1 284 ? -11.797 47.232 40.588 1.00 24.50 ? 277 TYR A O 1 ATOM 1806 C CB . TYR A 1 284 ? -13.029 46.043 42.815 1.00 24.63 ? 277 TYR A CB 1 ATOM 1807 C CG . TYR A 1 284 ? -12.569 46.994 43.881 1.00 24.57 ? 277 TYR A CG 1 ATOM 1808 C CD1 . TYR A 1 284 ? -12.300 48.334 43.561 1.00 26.66 ? 277 TYR A CD1 1 ATOM 1809 C CD2 . TYR A 1 284 ? -12.401 46.568 45.215 1.00 22.41 ? 277 TYR A CD2 1 ATOM 1810 C CE1 . TYR A 1 284 ? -11.858 49.245 44.531 1.00 26.72 ? 277 TYR A CE1 1 ATOM 1811 C CE2 . TYR A 1 284 ? -11.945 47.465 46.188 1.00 26.55 ? 277 TYR A CE2 1 ATOM 1812 C CZ . TYR A 1 284 ? -11.685 48.803 45.828 1.00 27.10 ? 277 TYR A CZ 1 ATOM 1813 O OH . TYR A 1 284 ? -11.255 49.709 46.761 1.00 27.92 ? 277 TYR A OH 1 ATOM 1814 N N . ALA A 1 285 ? -9.798 46.374 41.242 1.00 23.62 ? 278 ALA A N 1 ATOM 1815 C CA . ALA A 1 285 ? -8.963 47.351 40.531 1.00 25.37 ? 278 ALA A CA 1 ATOM 1816 C C . ALA A 1 285 ? -9.308 47.359 39.027 1.00 26.11 ? 278 ALA A C 1 ATOM 1817 O O . ALA A 1 285 ? -9.616 46.299 38.455 1.00 24.90 ? 278 ALA A O 1 ATOM 1818 C CB . ALA A 1 285 ? -7.458 47.009 40.728 1.00 25.97 ? 278 ALA A CB 1 ATOM 1819 N N . TYR A 1 286 ? -9.351 48.559 38.436 1.00 26.33 ? 279 TYR A N 1 ATOM 1820 C CA . TYR A 1 286 ? -9.423 48.702 36.977 1.00 27.10 ? 279 TYR A CA 1 ATOM 1821 C C . TYR A 1 286 ? -7.988 48.657 36.484 1.00 26.01 ? 279 TYR A C 1 ATOM 1822 O O . TYR A 1 286 ? -7.115 49.330 37.031 1.00 27.73 ? 279 TYR A O 1 ATOM 1823 C CB . TYR A 1 286 ? -10.120 50.015 36.483 1.00 28.96 ? 279 TYR A CB 1 ATOM 1824 C CG A TYR A 1 286 ? -10.503 49.947 34.984 0.50 26.78 ? 279 TYR A CG 1 ATOM 1825 C CG B TYR A 1 286 ? -9.492 50.620 35.170 0.50 29.30 ? 279 TYR A CG 1 ATOM 1826 C CD1 A TYR A 1 286 ? -11.546 49.136 34.526 0.50 25.12 ? 279 TYR A CD1 1 ATOM 1827 C CD1 B TYR A 1 286 ? -10.205 50.617 33.973 0.50 30.21 ? 279 TYR A CD1 1 ATOM 1828 C CD2 A TYR A 1 286 ? -9.758 50.659 34.036 0.50 25.72 ? 279 TYR A CD2 1 ATOM 1829 C CD2 B TYR A 1 286 ? -8.198 51.148 35.150 0.50 29.95 ? 279 TYR A CD2 1 ATOM 1830 C CE1 A TYR A 1 286 ? -11.859 49.061 33.150 0.50 27.14 ? 279 TYR A CE1 1 ATOM 1831 C CE1 B TYR A 1 286 ? -9.666 51.141 32.790 0.50 30.69 ? 279 TYR A CE1 1 ATOM 1832 C CE2 A TYR A 1 286 ? -10.066 50.599 32.673 0.50 26.38 ? 279 TYR A CE2 1 ATOM 1833 C CE2 B TYR A 1 286 ? -7.631 51.676 33.960 0.50 31.35 ? 279 TYR A CE2 1 ATOM 1834 C CZ A TYR A 1 286 ? -11.102 49.797 32.240 0.50 27.23 ? 279 TYR A CZ 1 ATOM 1835 C CZ B TYR A 1 286 ? -8.385 51.662 32.784 0.50 31.85 ? 279 TYR A CZ 1 ATOM 1836 O OH A TYR A 1 286 ? -11.347 49.744 30.894 0.50 29.44 ? 279 TYR A OH 1 ATOM 1837 O OH B TYR A 1 286 ? -7.874 52.178 31.602 0.50 34.53 ? 279 TYR A OH 1 ATOM 1838 N N . ARG A 1 287 ? -7.727 47.798 35.528 1.00 23.26 ? 280 ARG A N 1 ATOM 1839 C CA . ARG A 1 287 ? -6.382 47.618 35.003 1.00 22.93 ? 280 ARG A CA 1 ATOM 1840 C C . ARG A 1 287 ? -6.227 48.277 33.663 1.00 23.19 ? 280 ARG A C 1 ATOM 1841 O O . ARG A 1 287 ? -7.068 48.127 32.812 1.00 22.28 ? 280 ARG A O 1 ATOM 1842 C CB A ARG A 1 287 ? -6.079 46.125 34.879 0.65 23.59 ? 280 ARG A CB 1 ATOM 1843 C CB B ARG A 1 287 ? -6.102 46.127 34.825 0.35 22.04 ? 280 ARG A CB 1 ATOM 1844 C CG A ARG A 1 287 ? -5.389 45.576 36.141 0.65 24.40 ? 280 ARG A CG 1 ATOM 1845 C CG B ARG A 1 287 ? -5.939 45.425 36.148 0.35 18.43 ? 280 ARG A CG 1 ATOM 1846 C CD A ARG A 1 287 ? -6.278 44.770 37.047 0.65 28.37 ? 280 ARG A CD 1 ATOM 1847 C CD B ARG A 1 287 ? -5.496 43.982 36.017 0.35 11.60 ? 280 ARG A CD 1 ATOM 1848 N NE A ARG A 1 287 ? -5.559 44.349 38.264 0.65 28.00 ? 280 ARG A NE 1 ATOM 1849 N NE B ARG A 1 287 ? -5.174 43.539 37.364 0.35 9.71 ? 280 ARG A NE 1 ATOM 1850 C CZ A ARG A 1 287 ? -6.160 43.962 39.383 0.65 28.40 ? 280 ARG A CZ 1 ATOM 1851 C CZ B ARG A 1 287 ? -6.108 43.245 38.262 0.35 9.12 ? 280 ARG A CZ 1 ATOM 1852 N NH1 A ARG A 1 287 ? -7.481 43.928 39.450 0.65 30.76 ? 280 ARG A NH1 1 ATOM 1853 N NH1 B ARG A 1 287 ? -7.379 43.339 37.921 0.35 9.76 ? 280 ARG A NH1 1 ATOM 1854 N NH2 A ARG A 1 287 ? -5.452 43.624 40.441 0.65 26.60 ? 280 ARG A NH2 1 ATOM 1855 N NH2 B ARG A 1 287 ? -5.793 42.886 39.492 0.35 9.20 ? 280 ARG A NH2 1 ATOM 1856 N N . ARG A 1 288 ? -5.137 48.989 33.457 1.00 22.83 ? 281 ARG A N 1 ATOM 1857 C CA . ARG A 1 288 ? -4.783 49.367 32.096 1.00 24.14 ? 281 ARG A CA 1 ATOM 1858 C C . ARG A 1 288 ? -4.664 48.144 31.177 1.00 25.00 ? 281 ARG A C 1 ATOM 1859 O O . ARG A 1 288 ? -4.280 47.026 31.631 1.00 22.98 ? 281 ARG A O 1 ATOM 1860 C CB . ARG A 1 288 ? -3.448 50.120 32.087 1.00 23.88 ? 281 ARG A CB 1 ATOM 1861 C CG . ARG A 1 288 ? -3.585 51.464 32.771 1.00 24.94 ? 281 ARG A CG 1 ATOM 1862 C CD . ARG A 1 288 ? -2.290 52.187 32.737 1.00 27.18 ? 281 ARG A CD 1 ATOM 1863 N NE . ARG A 1 288 ? -2.431 53.533 33.285 1.00 25.91 ? 281 ARG A NE 1 ATOM 1864 C CZ . ARG A 1 288 ? -1.572 54.520 33.059 1.00 28.14 ? 281 ARG A CZ 1 ATOM 1865 N NH1 . ARG A 1 288 ? -0.533 54.302 32.274 1.00 26.30 ? 281 ARG A NH1 1 ATOM 1866 N NH2 . ARG A 1 288 ? -1.750 55.717 33.624 1.00 28.74 ? 281 ARG A NH2 1 ATOM 1867 N N . GLY A 1 289 ? -4.965 48.362 29.893 1.00 24.91 ? 282 GLY A N 1 ATOM 1868 C CA . GLY A 1 289 ? -4.560 47.388 28.877 1.00 27.34 ? 282 GLY A CA 1 ATOM 1869 C C . GLY A 1 289 ? -3.026 47.319 28.805 1.00 28.57 ? 282 GLY A C 1 ATOM 1870 O O . GLY A 1 289 ? -2.303 48.271 29.198 1.00 28.50 ? 282 GLY A O 1 ATOM 1871 N N . ILE A 1 290 ? -2.513 46.216 28.294 1.00 30.16 ? 283 ILE A N 1 ATOM 1872 C CA . ILE A 1 290 ? -1.057 46.018 28.163 1.00 31.46 ? 283 ILE A CA 1 ATOM 1873 C C . ILE A 1 290 ? -0.365 47.136 27.371 1.00 31.99 ? 283 ILE A C 1 ATOM 1874 O O . ILE A 1 290 ? 0.682 47.637 27.801 1.00 32.19 ? 283 ILE A O 1 ATOM 1875 C CB A ILE A 1 290 ? -0.757 44.552 27.680 0.65 32.14 ? 283 ILE A CB 1 ATOM 1876 C CB B ILE A 1 290 ? -0.681 44.632 27.507 0.35 31.55 ? 283 ILE A CB 1 ATOM 1877 C CG1 A ILE A 1 290 ? 0.642 44.081 28.086 0.65 32.33 ? 283 ILE A CG1 1 ATOM 1878 C CG1 B ILE A 1 290 ? -0.892 43.468 28.488 0.35 31.17 ? 283 ILE A CG1 1 ATOM 1879 C CG2 A ILE A 1 290 ? -1.087 44.368 26.202 0.65 33.16 ? 283 ILE A CG2 1 ATOM 1880 C CG2 B ILE A 1 290 ? 0.776 44.634 26.915 0.35 30.71 ? 283 ILE A CG2 1 ATOM 1881 C CD1 A ILE A 1 290 ? 0.735 43.717 29.556 0.65 32.09 ? 283 ILE A CD1 1 ATOM 1882 C CD1 B ILE A 1 290 ? 0.047 43.476 29.691 0.35 30.39 ? 283 ILE A CD1 1 ATOM 1883 N N . ALA A 1 291 ? -0.964 47.584 26.268 1.00 32.86 ? 284 ALA A N 1 ATOM 1884 C CA . ALA A 1 291 ? -0.382 48.683 25.462 1.00 33.26 ? 284 ALA A CA 1 ATOM 1885 C C . ALA A 1 291 ? -0.275 50.000 26.215 1.00 33.84 ? 284 ALA A C 1 ATOM 1886 O O . ALA A 1 291 ? 0.492 50.865 25.821 1.00 35.01 ? 284 ALA A O 1 ATOM 1887 C CB . ALA A 1 291 ? -1.174 48.884 24.115 1.00 33.79 ? 284 ALA A CB 1 ATOM 1888 N N . GLU A 1 292 ? -1.034 50.169 27.301 1.00 33.28 ? 285 GLU A N 1 ATOM 1889 C CA . GLU A 1 292 ? -0.910 51.373 28.139 1.00 32.81 ? 285 GLU A CA 1 ATOM 1890 C C . GLU A 1 292 ? -0.185 51.120 29.495 1.00 30.46 ? 285 GLU A C 1 ATOM 1891 O O . GLU A 1 292 ? -0.100 52.036 30.310 1.00 29.29 ? 285 GLU A O 1 ATOM 1892 C CB . GLU A 1 292 ? -2.306 52.041 28.392 1.00 34.50 ? 285 GLU A CB 1 ATOM 1893 C CG . GLU A 1 292 ? -2.988 52.634 27.152 1.00 39.15 ? 285 GLU A CG 1 ATOM 1894 C CD . GLU A 1 292 ? -3.537 51.567 26.183 1.00 46.01 ? 285 GLU A CD 1 ATOM 1895 O OE1 . GLU A 1 292 ? -4.234 50.598 26.591 1.00 48.67 ? 285 GLU A OE1 1 ATOM 1896 O OE2 . GLU A 1 292 ? -3.275 51.706 24.976 1.00 51.51 ? 285 GLU A OE2 1 ATOM 1897 N N . ALA A 1 293 ? 0.329 49.898 29.717 1.00 28.08 ? 286 ALA A N 1 ATOM 1898 C CA . ALA A 1 293 ? 0.993 49.543 30.994 1.00 26.50 ? 286 ALA A CA 1 ATOM 1899 C C . ALA A 1 293 ? 2.214 50.474 31.178 1.00 26.01 ? 286 ALA A C 1 ATOM 1900 O O . ALA A 1 293 ? 2.746 51.006 30.181 1.00 26.24 ? 286 ALA A O 1 ATOM 1901 C CB . ALA A 1 293 ? 1.421 48.114 30.990 1.00 24.08 ? 286 ALA A CB 1 ATOM 1902 N N . VAL A 1 294 ? 2.636 50.673 32.425 1.00 23.09 ? 287 VAL A N 1 ATOM 1903 C CA . VAL A 1 294 ? 3.787 51.522 32.696 1.00 22.09 ? 287 VAL A CA 1 ATOM 1904 C C . VAL A 1 294 ? 5.070 50.689 32.578 1.00 21.61 ? 287 VAL A C 1 ATOM 1905 O O . VAL A 1 294 ? 5.153 49.603 33.190 1.00 21.54 ? 287 VAL A O 1 ATOM 1906 C CB . VAL A 1 294 ? 3.753 52.205 34.124 1.00 21.79 ? 287 VAL A CB 1 ATOM 1907 C CG1 . VAL A 1 294 ? 5.083 53.083 34.323 1.00 19.95 ? 287 VAL A CG1 1 ATOM 1908 C CG2 . VAL A 1 294 ? 2.512 53.099 34.221 1.00 22.11 ? 287 VAL A CG2 1 ATOM 1909 N N . GLY A 1 295 ? 6.026 51.174 31.764 1.00 20.69 ? 288 GLY A N 1 ATOM 1910 C CA . GLY A 1 295 ? 7.422 50.770 31.938 1.00 20.49 ? 288 GLY A CA 1 ATOM 1911 C C . GLY A 1 295 ? 7.870 49.539 31.173 1.00 20.67 ? 288 GLY A C 1 ATOM 1912 O O . GLY A 1 295 ? 9.001 49.130 31.318 1.00 19.69 ? 288 GLY A O 1 ATOM 1913 N N . LEU A 1 296 ? 6.996 48.965 30.348 1.00 21.39 ? 289 LEU A N 1 ATOM 1914 C CA . LEU A 1 296 ? 7.343 47.721 29.626 1.00 23.06 ? 289 LEU A CA 1 ATOM 1915 C C . LEU A 1 296 ? 8.278 47.991 28.450 1.00 24.52 ? 289 LEU A C 1 ATOM 1916 O O . LEU A 1 296 ? 8.111 48.995 27.702 1.00 24.31 ? 289 LEU A O 1 ATOM 1917 C CB A LEU A 1 296 ? 6.089 47.002 29.100 0.65 22.67 ? 289 LEU A CB 1 ATOM 1918 C CB B LEU A 1 296 ? 6.106 46.918 29.190 0.35 22.86 ? 289 LEU A CB 1 ATOM 1919 C CG A LEU A 1 296 ? 4.919 46.700 30.051 0.65 22.76 ? 289 LEU A CG 1 ATOM 1920 C CG B LEU A 1 296 ? 5.560 45.911 30.218 0.35 22.83 ? 289 LEU A CG 1 ATOM 1921 C CD1 A LEU A 1 296 ? 3.815 45.996 29.257 0.65 20.20 ? 289 LEU A CD1 1 ATOM 1922 C CD1 B LEU A 1 296 ? 4.866 46.619 31.400 0.35 21.94 ? 289 LEU A CD1 1 ATOM 1923 C CD2 A LEU A 1 296 ? 5.387 45.825 31.268 0.65 22.52 ? 289 LEU A CD2 1 ATOM 1924 C CD2 B LEU A 1 296 ? 4.588 44.925 29.562 0.35 22.31 ? 289 LEU A CD2 1 ATOM 1925 N N . PRO A 1 297 ? 9.254 47.095 28.252 1.00 25.96 ? 290 PRO A N 1 ATOM 1926 C CA . PRO A 1 297 ? 10.153 47.251 27.115 1.00 26.38 ? 290 PRO A CA 1 ATOM 1927 C C . PRO A 1 297 ? 9.450 46.842 25.814 1.00 27.70 ? 290 PRO A C 1 ATOM 1928 O O . PRO A 1 297 ? 8.550 45.986 25.831 1.00 27.99 ? 290 PRO A O 1 ATOM 1929 C CB . PRO A 1 297 ? 11.293 46.280 27.452 1.00 27.76 ? 290 PRO A CB 1 ATOM 1930 C CG . PRO A 1 297 ? 10.665 45.218 28.243 1.00 26.46 ? 290 PRO A CG 1 ATOM 1931 C CD . PRO A 1 297 ? 9.584 45.907 29.067 1.00 26.54 ? 290 PRO A CD 1 ATOM 1932 N N A SER A 1 298 ? 9.869 47.436 24.702 0.60 27.33 ? 291 SER A N 1 ATOM 1933 N N B SER A 1 298 ? 9.852 47.443 24.694 0.40 27.43 ? 291 SER A N 1 ATOM 1934 C CA A SER A 1 298 ? 9.215 47.195 23.437 0.60 27.97 ? 291 SER A CA 1 ATOM 1935 C CA B SER A 1 298 ? 9.212 47.163 23.410 0.40 27.93 ? 291 SER A CA 1 ATOM 1936 C C A SER A 1 298 ? 9.977 46.188 22.557 0.60 27.47 ? 291 SER A C 1 ATOM 1937 C C B SER A 1 298 ? 10.035 46.271 22.492 0.40 27.49 ? 291 SER A C 1 ATOM 1938 O O A SER A 1 298 ? 9.446 45.744 21.553 0.60 27.11 ? 291 SER A O 1 ATOM 1939 O O B SER A 1 298 ? 9.628 46.032 21.365 0.40 27.31 ? 291 SER A O 1 ATOM 1940 C CB A SER A 1 298 ? 8.981 48.524 22.684 0.60 28.24 ? 291 SER A CB 1 ATOM 1941 C CB B SER A 1 298 ? 8.897 48.454 22.645 0.40 28.08 ? 291 SER A CB 1 ATOM 1942 O OG A SER A 1 298 ? 10.216 49.145 22.335 0.60 29.51 ? 291 SER A OG 1 ATOM 1943 O OG B SER A 1 298 ? 8.224 49.378 23.452 0.40 29.28 ? 291 SER A OG 1 ATOM 1944 N N . ILE A 1 299 ? 11.197 45.814 22.951 1.00 26.93 ? 292 ILE A N 1 ATOM 1945 C CA . ILE A 1 299 ? 12.040 44.897 22.140 1.00 26.88 ? 292 ILE A CA 1 ATOM 1946 C C . ILE A 1 299 ? 12.453 43.720 23.024 1.00 26.50 ? 292 ILE A C 1 ATOM 1947 O O . ILE A 1 299 ? 12.516 43.866 24.256 1.00 27.07 ? 292 ILE A O 1 ATOM 1948 C CB . ILE A 1 299 ? 13.279 45.619 21.539 1.00 26.57 ? 292 ILE A CB 1 ATOM 1949 C CG1 . ILE A 1 299 ? 14.108 46.308 22.654 1.00 25.26 ? 292 ILE A CG1 1 ATOM 1950 C CG2 . ILE A 1 299 ? 12.796 46.653 20.474 1.00 26.89 ? 292 ILE A CG2 1 ATOM 1951 C CD1 . ILE A 1 299 ? 15.375 47.044 22.146 1.00 24.82 ? 292 ILE A CD1 1 ATOM 1952 N N . PRO A 1 300 ? 12.638 42.544 22.422 1.00 25.95 ? 293 PRO A N 1 ATOM 1953 C CA . PRO A 1 300 ? 13.035 41.375 23.212 1.00 25.76 ? 293 PRO A CA 1 ATOM 1954 C C . PRO A 1 300 ? 14.433 41.532 23.817 1.00 24.86 ? 293 PRO A C 1 ATOM 1955 O O . PRO A 1 300 ? 15.322 42.200 23.217 1.00 24.52 ? 293 PRO A O 1 ATOM 1956 C CB . PRO A 1 300 ? 13.044 40.227 22.182 1.00 25.07 ? 293 PRO A CB 1 ATOM 1957 C CG . PRO A 1 300 ? 12.167 40.730 21.041 1.00 26.97 ? 293 PRO A CG 1 ATOM 1958 C CD . PRO A 1 300 ? 12.478 42.209 20.987 1.00 25.89 ? 293 PRO A CD 1 ATOM 1959 N N . VAL A 1 301 ? 14.618 40.895 24.970 1.00 23.18 ? 294 VAL A N 1 ATOM 1960 C CA . VAL A 1 301 ? 15.822 41.027 25.790 1.00 22.01 ? 294 VAL A CA 1 ATOM 1961 C C . VAL A 1 301 ? 16.068 39.674 26.468 1.00 22.77 ? 294 VAL A C 1 ATOM 1962 O O . VAL A 1 301 ? 15.114 38.980 26.902 1.00 23.12 ? 294 VAL A O 1 ATOM 1963 C CB . VAL A 1 301 ? 15.671 42.113 26.871 1.00 21.80 ? 294 VAL A CB 1 ATOM 1964 C CG1 . VAL A 1 301 ? 16.969 42.243 27.746 1.00 18.63 ? 294 VAL A CG1 1 ATOM 1965 C CG2 . VAL A 1 301 ? 15.292 43.487 26.261 1.00 20.18 ? 294 VAL A CG2 1 ATOM 1966 N N . HIS A 1 302 ? 17.335 39.281 26.552 1.00 22.48 ? 295 HIS A N 1 ATOM 1967 C CA . HIS A 1 302 ? 17.688 38.005 27.152 1.00 22.73 ? 295 HIS A CA 1 ATOM 1968 C C . HIS A 1 302 ? 19.136 38.056 27.691 1.00 22.93 ? 295 HIS A C 1 ATOM 1969 O O . HIS A 1 302 ? 20.010 38.657 27.052 1.00 23.78 ? 295 HIS A O 1 ATOM 1970 C CB . HIS A 1 302 ? 17.516 36.872 26.113 1.00 23.17 ? 295 HIS A CB 1 ATOM 1971 C CG . HIS A 1 302 ? 17.641 35.482 26.684 1.00 22.59 ? 295 HIS A CG 1 ATOM 1972 N ND1 . HIS A 1 302 ? 16.719 34.952 27.562 1.00 20.02 ? 295 HIS A ND1 1 ATOM 1973 C CD2 . HIS A 1 302 ? 18.560 34.503 26.464 1.00 23.79 ? 295 HIS A CD2 1 ATOM 1974 C CE1 . HIS A 1 302 ? 17.078 33.719 27.886 1.00 22.65 ? 295 HIS A CE1 1 ATOM 1975 N NE2 . HIS A 1 302 ? 18.190 33.419 27.226 1.00 23.27 ? 295 HIS A NE2 1 ATOM 1976 N N . PRO A 1 303 ? 19.377 37.462 28.884 1.00 22.36 ? 296 PRO A N 1 ATOM 1977 C CA . PRO A 1 303 ? 20.690 37.489 29.514 1.00 21.87 ? 296 PRO A CA 1 ATOM 1978 C C . PRO A 1 303 ? 21.406 36.149 29.318 1.00 23.04 ? 296 PRO A C 1 ATOM 1979 O O . PRO A 1 303 ? 20.764 35.094 29.272 1.00 23.07 ? 296 PRO A O 1 ATOM 1980 C CB . PRO A 1 303 ? 20.348 37.715 31.002 1.00 22.26 ? 296 PRO A CB 1 ATOM 1981 C CG . PRO A 1 303 ? 19.020 36.918 31.198 1.00 21.38 ? 296 PRO A CG 1 ATOM 1982 C CD . PRO A 1 303 ? 18.324 36.927 29.800 1.00 21.17 ? 296 PRO A CD 1 ATOM 1983 N N . ILE A 1 304 ? 22.727 36.210 29.172 1.00 23.21 ? 297 ILE A N 1 ATOM 1984 C CA . ILE A 1 304 ? 23.585 35.033 28.964 1.00 23.03 ? 297 ILE A CA 1 ATOM 1985 C C . ILE A 1 304 ? 24.881 35.160 29.792 1.00 23.55 ? 297 ILE A C 1 ATOM 1986 O O . ILE A 1 304 ? 25.227 36.257 30.280 1.00 23.60 ? 297 ILE A O 1 ATOM 1987 C CB . ILE A 1 304 ? 23.958 34.829 27.455 1.00 21.87 ? 297 ILE A CB 1 ATOM 1988 C CG1 . ILE A 1 304 ? 24.804 35.999 26.929 1.00 21.89 ? 297 ILE A CG1 1 ATOM 1989 C CG2 . ILE A 1 304 ? 22.714 34.572 26.588 1.00 20.77 ? 297 ILE A CG2 1 ATOM 1990 C CD1 . ILE A 1 304 ? 25.284 35.789 25.426 1.00 22.03 ? 297 ILE A CD1 1 ATOM 1991 N N . GLY A 1 305 ? 25.601 34.043 29.920 1.00 24.27 ? 298 GLY A N 1 ATOM 1992 C CA . GLY A 1 305 ? 26.864 33.999 30.622 1.00 24.74 ? 298 GLY A CA 1 ATOM 1993 C C . GLY A 1 305 ? 28.016 34.241 29.661 1.00 26.29 ? 298 GLY A C 1 ATOM 1994 O O . GLY A 1 305 ? 27.811 34.419 28.443 1.00 25.55 ? 298 GLY A O 1 ATOM 1995 N N . TYR A 1 306 ? 29.232 34.296 30.206 1.00 25.80 ? 299 TYR A N 1 ATOM 1996 C CA . TYR A 1 306 ? 30.358 34.640 29.364 1.00 25.90 ? 299 TYR A CA 1 ATOM 1997 C C . TYR A 1 306 ? 30.917 33.540 28.442 1.00 26.15 ? 299 TYR A C 1 ATOM 1998 O O . TYR A 1 306 ? 31.529 33.865 27.439 1.00 26.29 ? 299 TYR A O 1 ATOM 1999 C CB . TYR A 1 306 ? 31.455 35.374 30.148 1.00 25.37 ? 299 TYR A CB 1 ATOM 2000 C CG . TYR A 1 306 ? 32.083 34.634 31.307 1.00 25.03 ? 299 TYR A CG 1 ATOM 2001 C CD1 . TYR A 1 306 ? 31.682 34.923 32.620 1.00 25.85 ? 299 TYR A CD1 1 ATOM 2002 C CD2 . TYR A 1 306 ? 33.152 33.716 31.107 1.00 25.53 ? 299 TYR A CD2 1 ATOM 2003 C CE1 . TYR A 1 306 ? 32.259 34.291 33.712 1.00 24.92 ? 299 TYR A CE1 1 ATOM 2004 C CE2 . TYR A 1 306 ? 33.769 33.065 32.213 1.00 25.87 ? 299 TYR A CE2 1 ATOM 2005 C CZ . TYR A 1 306 ? 33.286 33.376 33.516 1.00 25.33 ? 299 TYR A CZ 1 ATOM 2006 O OH . TYR A 1 306 ? 33.790 32.796 34.647 1.00 21.43 ? 299 TYR A OH 1 ATOM 2007 N N . TYR A 1 307 ? 30.719 32.260 28.746 1.00 26.29 ? 300 TYR A N 1 ATOM 2008 C CA . TYR A 1 307 ? 30.976 31.240 27.700 1.00 27.05 ? 300 TYR A CA 1 ATOM 2009 C C . TYR A 1 307 ? 30.166 31.496 26.408 1.00 27.33 ? 300 TYR A C 1 ATOM 2010 O O . TYR A 1 307 ? 30.710 31.436 25.303 1.00 27.57 ? 300 TYR A O 1 ATOM 2011 C CB . TYR A 1 307 ? 30.659 29.820 28.182 1.00 26.98 ? 300 TYR A CB 1 ATOM 2012 C CG . TYR A 1 307 ? 31.560 29.264 29.244 1.00 30.30 ? 300 TYR A CG 1 ATOM 2013 C CD1 . TYR A 1 307 ? 32.889 29.746 29.401 1.00 31.44 ? 300 TYR A CD1 1 ATOM 2014 C CD2 . TYR A 1 307 ? 31.119 28.205 30.082 1.00 32.37 ? 300 TYR A CD2 1 ATOM 2015 C CE1 . TYR A 1 307 ? 33.741 29.207 30.346 1.00 31.07 ? 300 TYR A CE1 1 ATOM 2016 C CE2 . TYR A 1 307 ? 31.984 27.648 31.062 1.00 32.16 ? 300 TYR A CE2 1 ATOM 2017 C CZ . TYR A 1 307 ? 33.285 28.165 31.170 1.00 32.69 ? 300 TYR A CZ 1 ATOM 2018 O OH . TYR A 1 307 ? 34.150 27.661 32.102 1.00 33.55 ? 300 TYR A OH 1 ATOM 2019 N N . ASP A 1 308 ? 28.865 31.722 26.553 1.00 27.27 ? 301 ASP A N 1 ATOM 2020 C CA . ASP A 1 308 ? 27.983 32.048 25.423 1.00 28.16 ? 301 ASP A CA 1 ATOM 2021 C C . ASP A 1 308 ? 28.305 33.421 24.784 1.00 28.61 ? 301 ASP A C 1 ATOM 2022 O O . ASP A 1 308 ? 28.270 33.563 23.559 1.00 28.42 ? 301 ASP A O 1 ATOM 2023 C CB . ASP A 1 308 ? 26.517 32.023 25.887 1.00 28.34 ? 301 ASP A CB 1 ATOM 2024 C CG . ASP A 1 308 ? 25.977 30.598 26.045 1.00 29.30 ? 301 ASP A CG 1 ATOM 2025 O OD1 . ASP A 1 308 ? 26.610 29.670 25.506 1.00 29.34 ? 301 ASP A OD1 1 ATOM 2026 O OD2 . ASP A 1 308 ? 24.911 30.410 26.691 1.00 30.66 ? 301 ASP A OD2 1 ATOM 2027 N N . ALA A 1 309 ? 28.580 34.438 25.614 1.00 29.17 ? 302 ALA A N 1 ATOM 2028 C CA . ALA A 1 309 ? 28.969 35.759 25.092 1.00 29.89 ? 302 ALA A CA 1 ATOM 2029 C C . ALA A 1 309 ? 30.197 35.668 24.206 1.00 30.98 ? 302 ALA A C 1 ATOM 2030 O O . ALA A 1 309 ? 30.253 36.283 23.135 1.00 31.22 ? 302 ALA A O 1 ATOM 2031 C CB . ALA A 1 309 ? 29.208 36.768 26.257 1.00 28.93 ? 302 ALA A CB 1 ATOM 2032 N N . GLN A 1 310 ? 31.188 34.896 24.648 1.00 31.54 ? 303 GLN A N 1 ATOM 2033 C CA . GLN A 1 310 ? 32.394 34.742 23.860 1.00 33.25 ? 303 GLN A CA 1 ATOM 2034 C C . GLN A 1 310 ? 32.091 34.240 22.431 1.00 33.15 ? 303 GLN A C 1 ATOM 2035 O O . GLN A 1 310 ? 32.643 34.745 21.472 1.00 32.69 ? 303 GLN A O 1 ATOM 2036 C CB . GLN A 1 310 ? 33.440 33.866 24.556 1.00 33.08 ? 303 GLN A CB 1 ATOM 2037 C CG . GLN A 1 310 ? 34.602 33.545 23.607 1.00 38.03 ? 303 GLN A CG 1 ATOM 2038 C CD . GLN A 1 310 ? 35.945 33.513 24.272 1.00 44.21 ? 303 GLN A CD 1 ATOM 2039 O OE1 . GLN A 1 310 ? 36.983 33.435 23.589 1.00 49.73 ? 303 GLN A OE1 1 ATOM 2040 N NE2 . GLN A 1 310 ? 35.960 33.555 25.593 1.00 44.06 ? 303 GLN A NE2 1 ATOM 2041 N N . LYS A 1 311 ? 31.195 33.266 22.319 1.00 33.38 ? 304 LYS A N 1 ATOM 2042 C CA . LYS A 1 311 ? 30.788 32.720 21.036 1.00 33.19 ? 304 LYS A CA 1 ATOM 2043 C C . LYS A 1 311 ? 30.056 33.757 20.177 1.00 33.41 ? 304 LYS A C 1 ATOM 2044 O O . LYS A 1 311 ? 30.146 33.710 18.954 1.00 33.99 ? 304 LYS A O 1 ATOM 2045 C CB . LYS A 1 311 ? 29.909 31.478 21.248 1.00 32.91 ? 304 LYS A CB 1 ATOM 2046 C CG . LYS A 1 311 ? 30.613 30.332 22.013 1.00 32.06 ? 304 LYS A CG 1 ATOM 2047 C CD . LYS A 1 311 ? 31.710 29.599 21.159 0.50 32.04 ? 304 LYS A CD 1 ATOM 2048 C CE . LYS A 1 311 ? 31.091 28.832 20.026 0.40 32.11 ? 304 LYS A CE 1 ATOM 2049 N NZ . LYS A 1 311 ? 32.050 27.933 19.317 0.20 31.73 ? 304 LYS A NZ 1 ATOM 2050 N N . LEU A 1 312 ? 29.324 34.667 20.817 1.00 32.61 ? 305 LEU A N 1 ATOM 2051 C CA . LEU A 1 312 ? 28.648 35.755 20.105 1.00 33.39 ? 305 LEU A CA 1 ATOM 2052 C C . LEU A 1 312 ? 29.602 36.884 19.681 1.00 33.90 ? 305 LEU A C 1 ATOM 2053 O O . LEU A 1 312 ? 29.429 37.473 18.608 1.00 34.89 ? 305 LEU A O 1 ATOM 2054 C CB . LEU A 1 312 ? 27.498 36.344 20.943 1.00 32.27 ? 305 LEU A CB 1 ATOM 2055 C CG . LEU A 1 312 ? 26.300 35.399 21.192 1.00 31.53 ? 305 LEU A CG 1 ATOM 2056 C CD1 . LEU A 1 312 ? 25.136 36.158 21.815 1.00 30.46 ? 305 LEU A CD1 1 ATOM 2057 C CD2 . LEU A 1 312 ? 25.848 34.719 19.891 1.00 29.49 ? 305 LEU A CD2 1 ATOM 2058 N N . LEU A 1 313 ? 30.590 37.181 20.522 1.00 33.43 ? 306 LEU A N 1 ATOM 2059 C CA . LEU A 1 313 ? 31.497 38.297 20.288 1.00 33.59 ? 306 LEU A CA 1 ATOM 2060 C C . LEU A 1 313 ? 32.728 37.969 19.429 1.00 34.80 ? 306 LEU A C 1 ATOM 2061 O O . LEU A 1 313 ? 33.318 38.879 18.827 1.00 34.48 ? 306 LEU A O 1 ATOM 2062 C CB . LEU A 1 313 ? 31.978 38.854 21.607 1.00 32.56 ? 306 LEU A CB 1 ATOM 2063 C CG . LEU A 1 313 ? 30.943 39.423 22.591 1.00 31.35 ? 306 LEU A CG 1 ATOM 2064 C CD1 . LEU A 1 313 ? 31.605 39.607 23.945 1.00 30.64 ? 306 LEU A CD1 1 ATOM 2065 C CD2 . LEU A 1 313 ? 30.278 40.738 22.116 1.00 28.03 ? 306 LEU A CD2 1 ATOM 2066 N N . GLU A 1 314 ? 33.148 36.700 19.400 1.00 36.03 ? 307 GLU A N 1 ATOM 2067 C CA . GLU A 1 314 ? 34.450 36.370 18.820 1.00 37.82 ? 307 GLU A CA 1 ATOM 2068 C C . GLU A 1 314 ? 34.504 36.667 17.319 1.00 38.38 ? 307 GLU A C 1 ATOM 2069 O O . GLU A 1 314 ? 35.582 36.876 16.748 1.00 38.68 ? 307 GLU A O 1 ATOM 2070 C CB . GLU A 1 314 ? 34.858 34.925 19.143 1.00 37.84 ? 307 GLU A CB 1 ATOM 2071 C CG . GLU A 1 314 ? 34.024 33.884 18.472 1.00 39.27 ? 307 GLU A CG 1 ATOM 2072 C CD . GLU A 1 314 ? 34.309 32.488 18.975 1.00 41.99 ? 307 GLU A CD 1 ATOM 2073 O OE1 . GLU A 1 314 ? 35.233 32.315 19.790 1.00 42.79 ? 307 GLU A OE1 1 ATOM 2074 O OE2 . GLU A 1 314 ? 33.597 31.556 18.545 1.00 42.13 ? 307 GLU A OE2 1 ATOM 2075 N N . LYS A 1 315 ? 33.340 36.678 16.684 1.00 39.04 ? 308 LYS A N 1 ATOM 2076 C CA . LYS A 1 315 ? 33.282 36.876 15.248 1.00 40.51 ? 308 LYS A CA 1 ATOM 2077 C C . LYS A 1 315 ? 33.052 38.334 14.871 1.00 40.70 ? 308 LYS A C 1 ATOM 2078 O O . LYS A 1 315 ? 33.128 38.683 13.693 1.00 40.63 ? 308 LYS A O 1 ATOM 2079 C CB . LYS A 1 315 ? 32.210 35.982 14.627 1.00 40.86 ? 308 LYS A CB 1 ATOM 2080 C CG . LYS A 1 315 ? 32.688 34.540 14.351 1.00 42.31 ? 308 LYS A CG 1 ATOM 2081 C CD . LYS A 1 315 ? 31.501 33.586 14.367 1.00 42.52 ? 308 LYS A CD 1 ATOM 2082 C CE . LYS A 1 315 ? 31.902 32.224 13.824 1.00 42.04 ? 308 LYS A CE 1 ATOM 2083 N NZ . LYS A 1 315 ? 30.683 31.407 13.543 1.00 40.93 ? 308 LYS A NZ 1 ATOM 2084 N N . MET A 1 316 ? 32.836 39.192 15.863 1.00 40.00 ? 309 MET A N 1 ATOM 2085 C CA . MET A 1 316 ? 32.491 40.593 15.569 1.00 40.49 ? 309 MET A CA 1 ATOM 2086 C C . MET A 1 316 ? 33.484 41.399 14.695 1.00 40.91 ? 309 MET A C 1 ATOM 2087 O O . MET A 1 316 ? 34.697 41.372 14.921 1.00 40.59 ? 309 MET A O 1 ATOM 2088 C CB . MET A 1 316 ? 32.163 41.326 16.854 1.00 39.87 ? 309 MET A CB 1 ATOM 2089 C CG A MET A 1 316 ? 30.784 40.842 17.339 0.50 38.94 ? 309 MET A CG 1 ATOM 2090 C CG B MET A 1 316 ? 30.984 40.801 17.611 0.50 40.37 ? 309 MET A CG 1 ATOM 2091 S SD A MET A 1 316 ? 29.845 41.871 18.465 0.50 35.25 ? 309 MET A SD 1 ATOM 2092 S SD B MET A 1 316 ? 29.549 41.534 16.889 0.50 40.21 ? 309 MET A SD 1 ATOM 2093 C CE A MET A 1 316 ? 29.700 43.410 17.539 0.50 36.57 ? 309 MET A CE 1 ATOM 2094 C CE B MET A 1 316 ? 29.840 43.285 17.175 0.50 40.41 ? 309 MET A CE 1 ATOM 2095 N N . GLY A 1 317 ? 32.945 42.116 13.706 1.00 41.47 ? 310 GLY A N 1 ATOM 2096 C CA . GLY A 1 317 ? 33.754 42.916 12.763 1.00 41.97 ? 310 GLY A CA 1 ATOM 2097 C C . GLY A 1 317 ? 33.470 44.404 12.876 1.00 43.13 ? 310 GLY A C 1 ATOM 2098 O O . GLY A 1 317 ? 33.216 44.921 13.980 1.00 42.66 ? 310 GLY A O 1 ATOM 2099 N N . GLY A 1 318 ? 33.498 45.109 11.744 1.00 43.55 ? 311 GLY A N 1 ATOM 2100 C CA . GLY A 1 318 ? 33.256 46.547 11.747 1.00 44.52 ? 311 GLY A CA 1 ATOM 2101 C C . GLY A 1 318 ? 34.358 47.240 12.527 1.00 45.17 ? 311 GLY A C 1 ATOM 2102 O O . GLY A 1 318 ? 35.515 46.810 12.489 1.00 44.59 ? 311 GLY A O 1 ATOM 2103 N N . SER A 1 319 ? 33.990 48.295 13.249 1.00 45.47 ? 312 SER A N 1 ATOM 2104 C CA . SER A 1 319 ? 34.947 49.164 13.946 1.00 46.39 ? 312 SER A CA 1 ATOM 2105 C C . SER A 1 319 ? 35.569 48.572 15.202 1.00 46.06 ? 312 SER A C 1 ATOM 2106 O O . SER A 1 319 ? 34.903 47.852 15.969 1.00 45.89 ? 312 SER A O 1 ATOM 2107 C CB . SER A 1 319 ? 34.260 50.475 14.339 1.00 47.04 ? 312 SER A CB 1 ATOM 2108 O OG . SER A 1 319 ? 33.726 51.104 13.186 1.00 49.00 ? 312 SER A OG 1 ATOM 2109 N N . ALA A 1 320 ? 36.840 48.910 15.415 1.00 45.61 ? 313 ALA A N 1 ATOM 2110 C CA . ALA A 1 320 ? 37.559 48.610 16.651 1.00 45.21 ? 313 ALA A CA 1 ATOM 2111 C C . ALA A 1 320 ? 36.862 49.299 17.831 1.00 44.58 ? 313 ALA A C 1 ATOM 2112 O O . ALA A 1 320 ? 36.201 50.329 17.624 1.00 44.54 ? 313 ALA A O 1 ATOM 2113 C CB . ALA A 1 320 ? 39.023 49.107 16.533 1.00 44.56 ? 313 ALA A CB 1 ATOM 2114 N N . PRO A 1 321 ? 37.000 48.744 19.066 1.00 44.00 ? 314 PRO A N 1 ATOM 2115 C CA . PRO A 1 321 ? 36.553 49.488 20.259 1.00 43.41 ? 314 PRO A CA 1 ATOM 2116 C C . PRO A 1 321 ? 37.238 50.861 20.322 1.00 43.16 ? 314 PRO A C 1 ATOM 2117 O O . PRO A 1 321 ? 38.427 50.943 20.031 1.00 42.26 ? 314 PRO A O 1 ATOM 2118 C CB . PRO A 1 321 ? 37.002 48.615 21.440 1.00 42.75 ? 314 PRO A CB 1 ATOM 2119 C CG . PRO A 1 321 ? 38.009 47.652 20.872 1.00 43.71 ? 314 PRO A CG 1 ATOM 2120 C CD . PRO A 1 321 ? 37.622 47.451 19.424 1.00 44.39 ? 314 PRO A CD 1 ATOM 2121 N N . PRO A 1 322 ? 36.493 51.927 20.716 1.00 43.09 ? 315 PRO A N 1 ATOM 2122 C CA . PRO A 1 322 ? 37.103 53.274 20.650 1.00 43.33 ? 315 PRO A CA 1 ATOM 2123 C C . PRO A 1 322 ? 38.311 53.446 21.588 1.00 43.73 ? 315 PRO A C 1 ATOM 2124 O O . PRO A 1 322 ? 39.200 54.248 21.318 1.00 43.26 ? 315 PRO A O 1 ATOM 2125 C CB . PRO A 1 322 ? 35.942 54.220 21.014 1.00 42.30 ? 315 PRO A CB 1 ATOM 2126 C CG . PRO A 1 322 ? 34.981 53.351 21.831 1.00 42.49 ? 315 PRO A CG 1 ATOM 2127 C CD . PRO A 1 322 ? 35.099 51.960 21.221 1.00 42.65 ? 315 PRO A CD 1 ATOM 2128 N N . ASP A 1 323 ? 38.337 52.670 22.666 1.00 44.21 ? 316 ASP A N 1 ATOM 2129 C CA . ASP A 1 323 ? 39.400 52.725 23.670 1.00 45.00 ? 316 ASP A CA 1 ATOM 2130 C C . ASP A 1 323 ? 39.266 51.534 24.641 1.00 44.74 ? 316 ASP A C 1 ATOM 2131 O O . ASP A 1 323 ? 38.304 50.771 24.564 1.00 44.97 ? 316 ASP A O 1 ATOM 2132 C CB . ASP A 1 323 ? 39.412 54.094 24.413 1.00 45.26 ? 316 ASP A CB 1 ATOM 2133 C CG . ASP A 1 323 ? 38.152 54.340 25.257 1.00 46.01 ? 316 ASP A CG 1 ATOM 2134 O OD1 . ASP A 1 323 ? 37.828 53.514 26.134 1.00 46.83 ? 316 ASP A OD1 1 ATOM 2135 O OD2 . ASP A 1 323 ? 37.488 55.383 25.069 1.00 46.70 ? 316 ASP A OD2 1 ATOM 2136 N N . SER A 1 324 ? 40.211 51.414 25.568 1.00 44.37 ? 317 SER A N 1 ATOM 2137 C CA . SER A 1 324 ? 40.328 50.253 26.456 1.00 43.85 ? 317 SER A CA 1 ATOM 2138 C C . SER A 1 324 ? 39.194 50.130 27.500 1.00 42.62 ? 317 SER A C 1 ATOM 2139 O O . SER A 1 324 ? 38.943 49.025 28.007 1.00 43.01 ? 317 SER A O 1 ATOM 2140 C CB . SER A 1 324 ? 41.706 50.269 27.148 1.00 44.05 ? 317 SER A CB 1 ATOM 2141 O OG . SER A 1 324 ? 41.685 51.255 28.185 1.00 44.85 ? 317 SER A OG 1 ATOM 2142 N N . SER A 1 325 ? 38.512 51.238 27.813 1.00 40.69 ? 318 SER A N 1 ATOM 2143 C CA . SER A 1 325 ? 37.336 51.198 28.703 1.00 38.99 ? 318 SER A CA 1 ATOM 2144 C C . SER A 1 325 ? 36.145 50.431 28.095 1.00 37.97 ? 318 SER A C 1 ATOM 2145 O O . SER A 1 325 ? 35.178 50.113 28.800 1.00 37.75 ? 318 SER A O 1 ATOM 2146 C CB . SER A 1 325 ? 36.893 52.606 29.116 1.00 39.30 ? 318 SER A CB 1 ATOM 2147 O OG . SER A 1 325 ? 36.275 53.292 28.036 1.00 39.08 ? 318 SER A OG 1 ATOM 2148 N N . TRP A 1 326 ? 36.228 50.165 26.788 1.00 36.36 ? 319 TRP A N 1 ATOM 2149 C CA . TRP A 1 326 ? 35.265 49.344 26.046 1.00 35.00 ? 319 TRP A CA 1 ATOM 2150 C C . TRP A 1 326 ? 35.612 47.832 26.028 1.00 35.19 ? 319 TRP A C 1 ATOM 2151 O O . TRP A 1 326 ? 34.762 47.000 25.683 1.00 34.26 ? 319 TRP A O 1 ATOM 2152 C CB . TRP A 1 326 ? 35.069 49.892 24.612 1.00 34.50 ? 319 TRP A CB 1 ATOM 2153 C CG . TRP A 1 326 ? 34.091 51.070 24.587 1.00 33.27 ? 319 TRP A CG 1 ATOM 2154 C CD1 . TRP A 1 326 ? 34.213 52.266 25.272 1.00 32.47 ? 319 TRP A CD1 1 ATOM 2155 C CD2 . TRP A 1 326 ? 32.841 51.140 23.872 1.00 32.16 ? 319 TRP A CD2 1 ATOM 2156 N NE1 . TRP A 1 326 ? 33.119 53.074 25.013 1.00 33.32 ? 319 TRP A NE1 1 ATOM 2157 C CE2 . TRP A 1 326 ? 32.252 52.407 24.177 1.00 33.44 ? 319 TRP A CE2 1 ATOM 2158 C CE3 . TRP A 1 326 ? 32.153 50.253 23.010 1.00 30.24 ? 319 TRP A CE3 1 ATOM 2159 C CZ2 . TRP A 1 326 ? 31.000 52.807 23.654 1.00 31.24 ? 319 TRP A CZ2 1 ATOM 2160 C CZ3 . TRP A 1 326 ? 30.923 50.661 22.468 1.00 30.47 ? 319 TRP A CZ3 1 ATOM 2161 C CH2 . TRP A 1 326 ? 30.349 51.925 22.817 1.00 30.69 ? 319 TRP A CH2 1 ATOM 2162 N N A ARG A 1 327 ? 36.845 47.496 26.413 0.50 35.08 ? 320 ARG A N 1 ATOM 2163 N N B ARG A 1 327 ? 36.841 47.497 26.417 0.50 34.92 ? 320 ARG A N 1 ATOM 2164 C CA A ARG A 1 327 ? 37.313 46.112 26.415 0.50 35.75 ? 320 ARG A CA 1 ATOM 2165 C CA B ARG A 1 327 ? 37.288 46.114 26.416 0.50 35.44 ? 320 ARG A CA 1 ATOM 2166 C C A ARG A 1 327 ? 37.126 45.426 27.764 0.50 35.49 ? 320 ARG A C 1 ATOM 2167 C C B ARG A 1 327 ? 37.077 45.452 27.774 0.50 35.32 ? 320 ARG A C 1 ATOM 2168 O O A ARG A 1 327 ? 37.607 45.915 28.785 0.50 35.52 ? 320 ARG A O 1 ATOM 2169 O O B ARG A 1 327 ? 37.460 45.996 28.809 0.50 35.38 ? 320 ARG A O 1 ATOM 2170 C CB A ARG A 1 327 ? 38.796 46.030 26.008 0.50 35.64 ? 320 ARG A CB 1 ATOM 2171 C CB B ARG A 1 327 ? 38.761 46.016 25.975 0.50 35.17 ? 320 ARG A CB 1 ATOM 2172 C CG A ARG A 1 327 ? 39.043 46.074 24.513 0.50 37.59 ? 320 ARG A CG 1 ATOM 2173 C CG B ARG A 1 327 ? 39.049 46.775 24.687 0.50 36.26 ? 320 ARG A CG 1 ATOM 2174 C CD A ARG A 1 327 ? 40.478 45.628 24.146 0.50 41.38 ? 320 ARG A CD 1 ATOM 2175 C CD B ARG A 1 327 ? 40.341 46.319 23.975 0.50 38.86 ? 320 ARG A CD 1 ATOM 2176 N NE A ARG A 1 327 ? 40.628 45.460 22.704 0.50 45.02 ? 320 ARG A NE 1 ATOM 2177 N NE B ARG A 1 327 ? 41.576 46.767 24.620 0.50 41.21 ? 320 ARG A NE 1 ATOM 2178 C CZ A ARG A 1 327 ? 41.461 46.156 21.934 0.50 46.99 ? 320 ARG A CZ 1 ATOM 2179 C CZ B ARG A 1 327 ? 42.213 47.905 24.335 0.50 43.09 ? 320 ARG A CZ 1 ATOM 2180 N NH1 A ARG A 1 327 ? 42.253 47.084 22.460 0.50 46.90 ? 320 ARG A NH1 1 ATOM 2181 N NH1 B ARG A 1 327 ? 43.348 48.203 24.959 0.50 43.39 ? 320 ARG A NH1 1 ATOM 2182 N NH2 A ARG A 1 327 ? 41.501 45.913 20.629 0.50 47.48 ? 320 ARG A NH2 1 ATOM 2183 N NH2 B ARG A 1 327 ? 41.723 48.749 23.432 0.50 42.37 ? 320 ARG A NH2 1 ATOM 2184 N N . GLY A 1 328 ? 36.446 44.277 27.755 1.00 35.36 ? 321 GLY A N 1 ATOM 2185 C CA . GLY A 1 328 ? 36.349 43.413 28.940 1.00 34.71 ? 321 GLY A CA 1 ATOM 2186 C C . GLY A 1 328 ? 37.540 42.465 28.963 1.00 35.29 ? 321 GLY A C 1 ATOM 2187 O O . GLY A 1 328 ? 38.606 42.786 28.405 1.00 33.57 ? 321 GLY A O 1 ATOM 2188 N N . SER A 1 329 ? 37.364 41.291 29.574 1.00 35.83 ? 322 SER A N 1 ATOM 2189 C CA . SER A 1 329 ? 38.470 40.322 29.778 1.00 36.55 ? 322 SER A CA 1 ATOM 2190 C C . SER A 1 329 ? 38.406 39.087 28.911 1.00 35.85 ? 322 SER A C 1 ATOM 2191 O O . SER A 1 329 ? 39.256 38.220 29.014 1.00 35.52 ? 322 SER A O 1 ATOM 2192 C CB . SER A 1 329 ? 38.489 39.833 31.227 1.00 36.77 ? 322 SER A CB 1 ATOM 2193 O OG . SER A 1 329 ? 38.853 40.894 32.049 1.00 41.16 ? 322 SER A OG 1 ATOM 2194 N N . LEU A 1 330 ? 37.379 38.970 28.091 1.00 35.41 ? 323 LEU A N 1 ATOM 2195 C CA . LEU A 1 330 ? 37.338 37.836 27.172 1.00 36.04 ? 323 LEU A CA 1 ATOM 2196 C C . LEU A 1 330 ? 38.444 37.953 26.109 1.00 37.15 ? 323 LEU A C 1 ATOM 2197 O O . LEU A 1 330 ? 38.896 39.053 25.758 1.00 37.44 ? 323 LEU A O 1 ATOM 2198 C CB . LEU A 1 330 ? 35.945 37.685 26.540 1.00 34.70 ? 323 LEU A CB 1 ATOM 2199 C CG . LEU A 1 330 ? 34.864 37.411 27.601 1.00 32.42 ? 323 LEU A CG 1 ATOM 2200 C CD1 . LEU A 1 330 ? 33.529 37.580 26.968 1.00 30.26 ? 323 LEU A CD1 1 ATOM 2201 C CD2 . LEU A 1 330 ? 35.026 36.014 28.191 1.00 29.03 ? 323 LEU A CD2 1 ATOM 2202 N N . LYS A 1 331 ? 38.880 36.820 25.599 1.00 38.22 ? 324 LYS A N 1 ATOM 2203 C CA . LYS A 1 331 ? 39.893 36.838 24.565 1.00 39.35 ? 324 LYS A CA 1 ATOM 2204 C C . LYS A 1 331 ? 39.218 37.039 23.205 1.00 39.65 ? 324 LYS A C 1 ATOM 2205 O O . LYS A 1 331 ? 39.220 36.146 22.365 1.00 40.19 ? 324 LYS A O 1 ATOM 2206 C CB . LYS A 1 331 ? 40.792 35.599 24.662 0.75 39.26 ? 324 LYS A CB 1 ATOM 2207 C CG . LYS A 1 331 ? 41.775 35.663 25.847 0.50 39.83 ? 324 LYS A CG 1 ATOM 2208 C CD . LYS A 1 331 ? 42.594 36.956 25.846 0.20 39.53 ? 324 LYS A CD 1 ATOM 2209 C CE . LYS A 1 331 ? 43.432 37.095 27.104 0.20 39.46 ? 324 LYS A CE 1 ATOM 2210 N NZ . LYS A 1 331 ? 42.584 37.141 28.317 0.20 39.38 ? 324 LYS A NZ 1 ATOM 2211 N N . VAL A 1 332 ? 38.625 38.227 23.038 1.00 39.24 ? 325 VAL A N 1 ATOM 2212 C CA . VAL A 1 332 ? 37.958 38.676 21.805 1.00 39.49 ? 325 VAL A CA 1 ATOM 2213 C C . VAL A 1 332 ? 38.370 40.145 21.549 1.00 39.74 ? 325 VAL A C 1 ATOM 2214 O O . VAL A 1 332 ? 38.834 40.820 22.469 1.00 38.95 ? 325 VAL A O 1 ATOM 2215 C CB . VAL A 1 332 ? 36.378 38.540 21.866 1.00 38.98 ? 325 VAL A CB 1 ATOM 2216 C CG1 . VAL A 1 332 ? 35.942 37.085 22.159 1.00 39.87 ? 325 VAL A CG1 1 ATOM 2217 C CG2 . VAL A 1 332 ? 35.711 39.542 22.873 1.00 37.90 ? 325 VAL A CG2 1 ATOM 2218 N N . PRO A 1 333 ? 38.191 40.652 20.318 1.00 40.36 ? 326 PRO A N 1 ATOM 2219 C CA . PRO A 1 333 ? 38.657 42.042 20.124 1.00 40.57 ? 326 PRO A CA 1 ATOM 2220 C C . PRO A 1 333 ? 37.713 43.114 20.687 1.00 39.87 ? 326 PRO A C 1 ATOM 2221 O O . PRO A 1 333 ? 38.140 44.248 20.824 1.00 40.12 ? 326 PRO A O 1 ATOM 2222 C CB . PRO A 1 333 ? 38.765 42.192 18.599 1.00 41.27 ? 326 PRO A CB 1 ATOM 2223 C CG . PRO A 1 333 ? 37.864 41.132 18.029 1.00 42.45 ? 326 PRO A CG 1 ATOM 2224 C CD . PRO A 1 333 ? 37.749 40.015 19.060 1.00 41.23 ? 326 PRO A CD 1 ATOM 2225 N N . TYR A 1 334 ? 36.459 42.773 20.993 1.00 38.19 ? 327 TYR A N 1 ATOM 2226 C CA . TYR A 1 334 ? 35.482 43.790 21.452 1.00 37.80 ? 327 TYR A CA 1 ATOM 2227 C C . TYR A 1 334 ? 35.183 44.835 20.371 1.00 37.63 ? 327 TYR A C 1 ATOM 2228 O O . TYR A 1 334 ? 34.907 46.015 20.664 1.00 37.22 ? 327 TYR A O 1 ATOM 2229 C CB . TYR A 1 334 ? 35.940 44.461 22.746 1.00 37.33 ? 327 TYR A CB 1 ATOM 2230 C CG . TYR A 1 334 ? 35.822 43.524 23.902 1.00 36.68 ? 327 TYR A CG 1 ATOM 2231 C CD1 . TYR A 1 334 ? 34.589 43.361 24.553 1.00 34.99 ? 327 TYR A CD1 1 ATOM 2232 C CD2 . TYR A 1 334 ? 36.913 42.757 24.319 1.00 35.03 ? 327 TYR A CD2 1 ATOM 2233 C CE1 . TYR A 1 334 ? 34.443 42.475 25.596 1.00 34.10 ? 327 TYR A CE1 1 ATOM 2234 C CE2 . TYR A 1 334 ? 36.774 41.863 25.371 1.00 34.73 ? 327 TYR A CE2 1 ATOM 2235 C CZ . TYR A 1 334 ? 35.534 41.733 26.002 1.00 33.59 ? 327 TYR A CZ 1 ATOM 2236 O OH . TYR A 1 334 ? 35.365 40.867 27.046 1.00 31.33 ? 327 TYR A OH 1 ATOM 2237 N N . ASN A 1 335 ? 35.246 44.374 19.123 1.00 36.91 ? 328 ASN A N 1 ATOM 2238 C CA . ASN A 1 335 ? 34.810 45.154 17.992 1.00 37.30 ? 328 ASN A CA 1 ATOM 2239 C C . ASN A 1 335 ? 33.360 45.532 18.165 1.00 37.16 ? 328 ASN A C 1 ATOM 2240 O O . ASN A 1 335 ? 32.538 44.727 18.611 1.00 36.91 ? 328 ASN A O 1 ATOM 2241 C CB . ASN A 1 335 ? 35.019 44.376 16.687 1.00 36.92 ? 328 ASN A CB 1 ATOM 2242 C CG . ASN A 1 335 ? 36.465 44.317 16.283 1.00 37.52 ? 328 ASN A CG 1 ATOM 2243 O OD1 . ASN A 1 335 ? 37.250 45.195 16.662 1.00 37.88 ? 328 ASN A OD1 1 ATOM 2244 N ND2 . ASN A 1 335 ? 36.838 43.292 15.498 1.00 34.31 ? 328 ASN A ND2 1 ATOM 2245 N N . VAL A 1 336 ? 33.061 46.780 17.841 1.00 38.01 ? 329 VAL A N 1 ATOM 2246 C CA . VAL A 1 336 ? 31.708 47.329 17.978 1.00 38.43 ? 329 VAL A CA 1 ATOM 2247 C C . VAL A 1 336 ? 30.710 46.817 16.908 1.00 39.01 ? 329 VAL A C 1 ATOM 2248 O O . VAL A 1 336 ? 29.504 46.844 17.106 1.00 38.27 ? 329 VAL A O 1 ATOM 2249 C CB . VAL A 1 336 ? 31.784 48.867 17.998 1.00 38.70 ? 329 VAL A CB 1 ATOM 2250 C CG1 . VAL A 1 336 ? 30.387 49.471 18.034 1.00 39.76 ? 329 VAL A CG1 1 ATOM 2251 C CG2 . VAL A 1 336 ? 32.511 49.299 19.263 1.00 38.82 ? 329 VAL A CG2 1 ATOM 2252 N N . GLY A 1 337 ? 31.209 46.341 15.768 1.00 40.21 ? 330 GLY A N 1 ATOM 2253 C CA . GLY A 1 337 ? 30.298 45.943 14.698 1.00 41.56 ? 330 GLY A CA 1 ATOM 2254 C C . GLY A 1 337 ? 30.007 47.137 13.803 1.00 42.89 ? 330 GLY A C 1 ATOM 2255 O O . GLY A 1 337 ? 30.847 48.033 13.674 1.00 42.76 ? 330 GLY A O 1 ATOM 2256 N N . PRO A 1 338 ? 28.839 47.146 13.146 1.00 43.82 ? 331 PRO A N 1 ATOM 2257 C CA . PRO A 1 338 ? 27.792 46.124 13.115 1.00 44.23 ? 331 PRO A CA 1 ATOM 2258 C C . PRO A 1 338 ? 28.237 44.844 12.386 1.00 44.18 ? 331 PRO A C 1 ATOM 2259 O O . PRO A 1 338 ? 29.052 44.904 11.462 1.00 43.27 ? 331 PRO A O 1 ATOM 2260 C CB . PRO A 1 338 ? 26.664 46.816 12.332 1.00 44.46 ? 331 PRO A CB 1 ATOM 2261 C CG . PRO A 1 338 ? 27.414 47.668 11.323 1.00 45.74 ? 331 PRO A CG 1 ATOM 2262 C CD . PRO A 1 338 ? 28.615 48.189 12.118 1.00 45.16 ? 331 PRO A CD 1 ATOM 2263 N N . GLY A 1 339 ? 27.737 43.694 12.827 1.00 44.34 ? 332 GLY A N 1 ATOM 2264 C CA . GLY A 1 339 ? 27.993 42.436 12.118 1.00 45.33 ? 332 GLY A CA 1 ATOM 2265 C C . GLY A 1 339 ? 29.353 41.789 12.349 1.00 46.03 ? 332 GLY A C 1 ATOM 2266 O O . GLY A 1 339 ? 30.198 42.323 13.093 1.00 45.56 ? 332 GLY A O 1 ATOM 2267 N N . PHE A 1 340 ? 29.550 40.640 11.696 1.00 46.60 ? 333 PHE A N 1 ATOM 2268 C CA . PHE A 1 340 ? 30.738 39.789 11.846 1.00 47.79 ? 333 PHE A CA 1 ATOM 2269 C C . PHE A 1 340 ? 31.808 40.087 10.763 1.00 49.78 ? 333 PHE A C 1 ATOM 2270 O O . PHE A 1 340 ? 31.480 40.672 9.720 1.00 49.63 ? 333 PHE A O 1 ATOM 2271 C CB . PHE A 1 340 ? 30.338 38.296 11.793 1.00 46.84 ? 333 PHE A CB 1 ATOM 2272 C CG . PHE A 1 340 ? 29.417 37.836 12.924 1.00 46.06 ? 333 PHE A CG 1 ATOM 2273 C CD1 . PHE A 1 340 ? 28.403 36.914 12.677 1.00 44.90 ? 333 PHE A CD1 1 ATOM 2274 C CD2 . PHE A 1 340 ? 29.583 38.302 14.222 1.00 43.38 ? 333 PHE A CD2 1 ATOM 2275 C CE1 . PHE A 1 340 ? 27.563 36.473 13.705 1.00 44.29 ? 333 PHE A CE1 1 ATOM 2276 C CE2 . PHE A 1 340 ? 28.745 37.872 15.257 1.00 43.47 ? 333 PHE A CE2 1 ATOM 2277 C CZ . PHE A 1 340 ? 27.731 36.956 14.996 1.00 42.98 ? 333 PHE A CZ 1 ATOM 2278 N N . THR A 1 341 ? 33.060 39.672 11.006 1.00 51.28 ? 334 THR A N 1 ATOM 2279 C CA . THR A 1 341 ? 34.174 39.871 10.054 1.00 53.95 ? 334 THR A CA 1 ATOM 2280 C C . THR A 1 341 ? 34.022 39.053 8.758 1.00 55.16 ? 334 THR A C 1 ATOM 2281 O O . THR A 1 341 ? 33.361 38.008 8.738 1.00 54.69 ? 334 THR A O 1 ATOM 2282 C CB . THR A 1 341 ? 35.558 39.490 10.670 1.00 54.20 ? 334 THR A CB 1 ATOM 2283 O OG1 . THR A 1 341 ? 35.502 38.164 11.208 1.00 54.63 ? 334 THR A OG1 1 ATOM 2284 C CG2 . THR A 1 341 ? 35.955 40.434 11.771 1.00 54.46 ? 334 THR A CG2 1 ATOM 2285 N N . GLY A 1 342 ? 34.671 39.535 7.693 1.00 56.77 ? 335 GLY A N 1 ATOM 2286 C CA . GLY A 1 342 ? 34.706 38.883 6.388 1.00 57.86 ? 335 GLY A CA 1 ATOM 2287 C C . GLY A 1 342 ? 34.064 37.517 6.213 1.00 58.81 ? 335 GLY A C 1 ATOM 2288 O O . GLY A 1 342 ? 32.957 37.432 5.692 1.00 59.06 ? 335 GLY A O 1 ATOM 2289 N N . ASN A 1 343 ? 34.759 36.454 6.635 1.00 59.54 ? 336 ASN A N 1 ATOM 2290 C CA . ASN A 1 343 ? 34.305 35.053 6.457 1.00 60.25 ? 336 ASN A CA 1 ATOM 2291 C C . ASN A 1 343 ? 32.869 34.775 6.935 1.00 59.51 ? 336 ASN A C 1 ATOM 2292 O O . ASN A 1 343 ? 32.149 33.987 6.328 1.00 59.67 ? 336 ASN A O 1 ATOM 2293 C CB . ASN A 1 343 ? 35.269 34.059 7.151 1.00 61.11 ? 336 ASN A CB 1 ATOM 2294 C CG . ASN A 1 343 ? 36.593 33.865 6.400 1.00 63.58 ? 336 ASN A CG 1 ATOM 2295 O OD1 . ASN A 1 343 ? 37.132 34.801 5.787 1.00 65.90 ? 336 ASN A OD1 1 ATOM 2296 N ND2 . ASN A 1 343 ? 37.130 32.634 6.452 1.00 66.44 ? 336 ASN A ND2 1 ATOM 2297 N N . PHE A 1 344 ? 32.466 35.430 8.023 1.00 58.14 ? 337 PHE A N 1 ATOM 2298 C CA . PHE A 1 344 ? 31.184 35.142 8.658 1.00 56.97 ? 337 PHE A CA 1 ATOM 2299 C C . PHE A 1 344 ? 30.148 36.256 8.464 1.00 56.04 ? 337 PHE A C 1 ATOM 2300 O O . PHE A 1 344 ? 29.206 36.358 9.244 1.00 55.76 ? 337 PHE A O 1 ATOM 2301 C CB . PHE A 1 344 ? 31.388 34.865 10.157 1.00 56.74 ? 337 PHE A CB 1 ATOM 2302 C CG . PHE A 1 344 ? 32.583 33.998 10.463 1.00 56.77 ? 337 PHE A CG 1 ATOM 2303 C CD1 . PHE A 1 344 ? 33.787 34.569 10.870 1.00 56.43 ? 337 PHE A CD1 1 ATOM 2304 C CD2 . PHE A 1 344 ? 32.507 32.609 10.338 1.00 56.85 ? 337 PHE A CD2 1 ATOM 2305 C CE1 . PHE A 1 344 ? 34.900 33.770 11.151 1.00 56.34 ? 337 PHE A CE1 1 ATOM 2306 C CE2 . PHE A 1 344 ? 33.619 31.799 10.618 1.00 56.46 ? 337 PHE A CE2 1 ATOM 2307 C CZ . PHE A 1 344 ? 34.814 32.387 11.027 1.00 56.43 ? 337 PHE A CZ 1 ATOM 2308 N N . SER A 1 345 ? 30.294 37.077 7.423 1.00 55.12 ? 338 SER A N 1 ATOM 2309 C CA . SER A 1 345 ? 29.447 38.272 7.323 1.00 54.30 ? 338 SER A CA 1 ATOM 2310 C C . SER A 1 345 ? 28.022 37.991 6.865 1.00 53.48 ? 338 SER A C 1 ATOM 2311 O O . SER A 1 345 ? 27.149 38.853 6.998 1.00 53.93 ? 338 SER A O 1 ATOM 2312 C CB . SER A 1 345 ? 30.086 39.366 6.474 1.00 54.57 ? 338 SER A CB 1 ATOM 2313 O OG . SER A 1 345 ? 30.042 38.999 5.117 1.00 54.26 ? 338 SER A OG 1 ATOM 2314 N N . THR A 1 346 ? 27.769 36.783 6.381 1.00 52.15 ? 339 THR A N 1 ATOM 2315 C CA . THR A 1 346 ? 26.412 36.391 5.987 1.00 51.60 ? 339 THR A CA 1 ATOM 2316 C C . THR A 1 346 ? 25.626 35.771 7.146 1.00 50.81 ? 339 THR A C 1 ATOM 2317 O O . THR A 1 346 ? 24.412 35.590 7.055 1.00 51.58 ? 339 THR A O 1 ATOM 2318 C CB . THR A 1 346 ? 26.413 35.422 4.802 1.00 51.76 ? 339 THR A CB 1 ATOM 2319 O OG1 . THR A 1 346 ? 27.135 34.231 5.156 1.00 50.58 ? 339 THR A OG1 1 ATOM 2320 C CG2 . THR A 1 346 ? 27.044 36.077 3.552 1.00 52.10 ? 339 THR A CG2 1 ATOM 2321 N N . GLN A 1 347 ? 26.326 35.456 8.234 1.00 49.21 ? 340 GLN A N 1 ATOM 2322 C CA . GLN A 1 347 ? 25.700 34.909 9.447 1.00 46.75 ? 340 GLN A CA 1 ATOM 2323 C C . GLN A 1 347 ? 25.021 36.026 10.219 1.00 45.12 ? 340 GLN A C 1 ATOM 2324 O O . GLN A 1 347 ? 25.453 37.173 10.133 1.00 43.48 ? 340 GLN A O 1 ATOM 2325 C CB . GLN A 1 347 ? 26.742 34.199 10.321 1.00 47.05 ? 340 GLN A CB 1 ATOM 2326 C CG . GLN A 1 347 ? 27.486 33.050 9.569 1.00 46.05 ? 340 GLN A CG 1 ATOM 2327 C CD . GLN A 1 347 ? 28.468 32.270 10.432 1.00 46.10 ? 340 GLN A CD 1 ATOM 2328 O OE1 . GLN A 1 347 ? 28.725 32.611 11.590 1.00 46.56 ? 340 GLN A OE1 1 ATOM 2329 N NE2 . GLN A 1 347 ? 29.021 31.201 9.865 1.00 45.84 ? 340 GLN A NE2 1 ATOM 2330 N N . LYS A 1 348 ? 23.951 35.688 10.939 1.00 43.33 ? 341 LYS A N 1 ATOM 2331 C CA . LYS A 1 348 ? 23.208 36.653 11.751 1.00 41.86 ? 341 LYS A CA 1 ATOM 2332 C C . LYS A 1 348 ? 22.925 36.080 13.158 1.00 40.46 ? 341 LYS A C 1 ATOM 2333 O O . LYS A 1 348 ? 23.205 34.897 13.423 1.00 40.06 ? 341 LYS A O 1 ATOM 2334 C CB . LYS A 1 348 ? 21.923 37.128 11.012 1.00 42.20 ? 341 LYS A CB 1 ATOM 2335 C CG . LYS A 1 348 ? 22.218 37.811 9.651 1.00 41.23 ? 341 LYS A CG 1 ATOM 2336 C CD . LYS A 1 348 ? 21.121 38.702 9.085 0.50 40.86 ? 341 LYS A CD 1 ATOM 2337 C CE . LYS A 1 348 ? 21.654 39.401 7.835 0.20 41.11 ? 341 LYS A CE 1 ATOM 2338 N NZ . LYS A 1 348 ? 20.627 40.182 7.105 0.20 41.04 ? 341 LYS A NZ 1 ATOM 2339 N N . VAL A 1 349 ? 22.447 36.931 14.072 1.00 38.08 ? 342 VAL A N 1 ATOM 2340 C CA . VAL A 1 349 ? 22.070 36.496 15.420 1.00 36.20 ? 342 VAL A CA 1 ATOM 2341 C C . VAL A 1 349 ? 20.542 36.460 15.501 1.00 35.74 ? 342 VAL A C 1 ATOM 2342 O O . VAL A 1 349 ? 19.887 37.357 14.986 1.00 35.30 ? 342 VAL A O 1 ATOM 2343 C CB . VAL A 1 349 ? 22.680 37.424 16.495 1.00 35.81 ? 342 VAL A CB 1 ATOM 2344 C CG1 . VAL A 1 349 ? 22.015 37.210 17.864 1.00 33.38 ? 342 VAL A CG1 1 ATOM 2345 C CG2 . VAL A 1 349 ? 24.220 37.189 16.532 1.00 36.05 ? 342 VAL A CG2 1 ATOM 2346 N N . LYS A 1 350 ? 19.983 35.415 16.106 1.00 34.66 ? 343 LYS A N 1 ATOM 2347 C CA . LYS A 1 350 ? 18.533 35.292 16.203 1.00 34.17 ? 343 LYS A CA 1 ATOM 2348 C C . LYS A 1 350 ? 18.124 35.022 17.658 1.00 33.32 ? 343 LYS A C 1 ATOM 2349 O O . LYS A 1 350 ? 18.582 34.063 18.260 1.00 33.25 ? 343 LYS A O 1 ATOM 2350 C CB . LYS A 1 350 ? 18.016 34.174 15.257 1.00 34.47 ? 343 LYS A CB 1 ATOM 2351 C CG . LYS A 1 350 ? 16.465 33.993 15.295 1.00 34.40 ? 343 LYS A CG 1 ATOM 2352 C CD . LYS A 1 350 ? 15.971 32.957 14.249 1.00 38.02 ? 343 LYS A CD 1 ATOM 2353 C CE . LYS A 1 350 ? 14.467 33.132 14.060 1.00 39.38 ? 343 LYS A CE 1 ATOM 2354 N NZ . LYS A 1 350 ? 13.888 32.254 13.021 1.00 42.60 ? 343 LYS A NZ 1 ATOM 2355 N N . MET A 1 351 ? 17.259 35.869 18.210 1.00 32.46 ? 344 MET A N 1 ATOM 2356 C CA . MET A 1 351 ? 16.680 35.648 19.530 1.00 31.81 ? 344 MET A CA 1 ATOM 2357 C C . MET A 1 351 ? 15.380 34.833 19.379 1.00 31.99 ? 344 MET A C 1 ATOM 2358 O O . MET A 1 351 ? 14.721 34.896 18.341 1.00 31.27 ? 344 MET A O 1 ATOM 2359 C CB . MET A 1 351 ? 16.400 36.995 20.224 1.00 31.10 ? 344 MET A CB 1 ATOM 2360 C CG . MET A 1 351 ? 17.594 37.957 20.178 1.00 29.30 ? 344 MET A CG 1 ATOM 2361 S SD . MET A 1 351 ? 17.301 39.539 21.045 1.00 28.45 ? 344 MET A SD 1 ATOM 2362 C CE . MET A 1 351 ? 17.237 38.987 22.779 1.00 26.32 ? 344 MET A CE 1 ATOM 2363 N N . HIS A 1 352 ? 15.023 34.084 20.421 1.00 31.44 ? 345 HIS A N 1 ATOM 2364 C CA . HIS A 1 352 ? 13.746 33.379 20.483 1.00 30.60 ? 345 HIS A CA 1 ATOM 2365 C C . HIS A 1 352 ? 13.232 33.610 21.891 1.00 29.92 ? 345 HIS A C 1 ATOM 2366 O O . HIS A 1 352 ? 13.688 32.950 22.857 1.00 29.02 ? 345 HIS A O 1 ATOM 2367 C CB . HIS A 1 352 ? 13.900 31.879 20.276 1.00 30.90 ? 345 HIS A CB 1 ATOM 2368 C CG . HIS A 1 352 ? 14.805 31.502 19.143 1.00 33.38 ? 345 HIS A CG 1 ATOM 2369 N ND1 . HIS A 1 352 ? 16.174 31.652 19.205 1.00 34.66 ? 345 HIS A ND1 1 ATOM 2370 C CD2 . HIS A 1 352 ? 14.541 30.939 17.939 1.00 35.13 ? 345 HIS A CD2 1 ATOM 2371 C CE1 . HIS A 1 352 ? 16.715 31.215 18.076 1.00 35.83 ? 345 HIS A CE1 1 ATOM 2372 N NE2 . HIS A 1 352 ? 15.744 30.790 17.288 1.00 36.19 ? 345 HIS A NE2 1 ATOM 2373 N N . ILE A 1 353 ? 12.320 34.565 22.025 1.00 28.93 ? 346 ILE A N 1 ATOM 2374 C CA . ILE A 1 353 ? 11.771 34.894 23.348 1.00 28.54 ? 346 ILE A CA 1 ATOM 2375 C C . ILE A 1 353 ? 10.271 34.620 23.324 1.00 29.39 ? 346 ILE A C 1 ATOM 2376 O O . ILE A 1 353 ? 9.536 35.149 22.472 1.00 29.81 ? 346 ILE A O 1 ATOM 2377 C CB . ILE A 1 353 ? 12.062 36.365 23.752 1.00 28.68 ? 346 ILE A CB 1 ATOM 2378 C CG1 . ILE A 1 353 ? 13.564 36.714 23.566 1.00 28.41 ? 346 ILE A CG1 1 ATOM 2379 C CG2 . ILE A 1 353 ? 11.516 36.668 25.195 1.00 26.70 ? 346 ILE A CG2 1 ATOM 2380 C CD1 . ILE A 1 353 ? 14.591 35.851 24.341 1.00 27.97 ? 346 ILE A CD1 1 ATOM 2381 N N . HIS A 1 354 ? 9.832 33.814 24.285 1.00 28.74 ? 347 HIS A N 1 ATOM 2382 C CA . HIS A 1 354 ? 8.451 33.332 24.369 1.00 28.97 ? 347 HIS A CA 1 ATOM 2383 C C . HIS A 1 354 ? 7.819 33.519 25.766 1.00 27.66 ? 347 HIS A C 1 ATOM 2384 O O . HIS A 1 354 ? 6.763 32.901 26.076 1.00 27.32 ? 347 HIS A O 1 ATOM 2385 C CB . HIS A 1 354 ? 8.436 31.858 23.974 1.00 28.66 ? 347 HIS A CB 1 ATOM 2386 C CG . HIS A 1 354 ? 9.021 31.614 22.615 1.00 33.82 ? 347 HIS A CG 1 ATOM 2387 N ND1 . HIS A 1 354 ? 10.208 30.934 22.424 1.00 36.07 ? 347 HIS A ND1 1 ATOM 2388 C CD2 . HIS A 1 354 ? 8.623 32.035 21.387 1.00 35.96 ? 347 HIS A CD2 1 ATOM 2389 C CE1 . HIS A 1 354 ? 10.494 30.909 21.131 1.00 37.79 ? 347 HIS A CE1 1 ATOM 2390 N NE2 . HIS A 1 354 ? 9.550 31.571 20.482 1.00 38.93 ? 347 HIS A NE2 1 ATOM 2391 N N . SER A 1 355 ? 8.480 34.342 26.595 1.00 25.96 ? 348 SER A N 1 ATOM 2392 C CA . SER A 1 355 ? 8.027 34.639 27.956 1.00 25.48 ? 348 SER A CA 1 ATOM 2393 C C . SER A 1 355 ? 6.651 35.303 27.889 1.00 25.87 ? 348 SER A C 1 ATOM 2394 O O . SER A 1 355 ? 6.343 35.946 26.881 1.00 25.61 ? 348 SER A O 1 ATOM 2395 C CB . SER A 1 355 ? 9.006 35.598 28.659 1.00 24.58 ? 348 SER A CB 1 ATOM 2396 O OG . SER A 1 355 ? 10.311 35.010 28.734 1.00 23.96 ? 348 SER A OG 1 ATOM 2397 N N . THR A 1 356 ? 5.844 35.182 28.954 1.00 25.60 ? 349 THR A N 1 ATOM 2398 C CA . THR A 1 356 ? 4.511 35.812 28.955 1.00 26.44 ? 349 THR A CA 1 ATOM 2399 C C . THR A 1 356 ? 4.328 36.635 30.195 1.00 25.95 ? 349 THR A C 1 ATOM 2400 O O . THR A 1 356 ? 4.819 36.270 31.258 1.00 27.12 ? 349 THR A O 1 ATOM 2401 C CB . THR A 1 356 ? 3.382 34.768 28.904 1.00 27.03 ? 349 THR A CB 1 ATOM 2402 O OG1 . THR A 1 356 ? 3.547 33.903 30.020 1.00 29.86 ? 349 THR A OG1 1 ATOM 2403 C CG2 . THR A 1 356 ? 3.493 33.914 27.645 1.00 26.13 ? 349 THR A CG2 1 ATOM 2404 N N . ASN A 1 357 ? 3.627 37.748 30.071 1.00 25.25 ? 350 ASN A N 1 ATOM 2405 C CA . ASN A 1 357 ? 3.290 38.552 31.239 1.00 24.55 ? 350 ASN A CA 1 ATOM 2406 C C . ASN A 1 357 ? 1.924 38.063 31.714 1.00 25.07 ? 350 ASN A C 1 ATOM 2407 O O . ASN A 1 357 ? 1.024 37.818 30.905 1.00 24.19 ? 350 ASN A O 1 ATOM 2408 C CB . ASN A 1 357 ? 3.166 40.007 30.849 1.00 24.77 ? 350 ASN A CB 1 ATOM 2409 C CG . ASN A 1 357 ? 4.434 40.555 30.243 1.00 26.38 ? 350 ASN A CG 1 ATOM 2410 O OD1 . ASN A 1 357 ? 5.552 40.206 30.646 1.00 25.27 ? 350 ASN A OD1 1 ATOM 2411 N ND2 . ASN A 1 357 ? 4.269 41.409 29.243 1.00 28.36 ? 350 ASN A ND2 1 ATOM 2412 N N . GLU A 1 358 ? 1.760 37.903 33.015 1.00 24.52 ? 351 GLU A N 1 ATOM 2413 C CA . GLU A 1 358 ? 0.466 37.488 33.534 1.00 25.00 ? 351 GLU A CA 1 ATOM 2414 C C . GLU A 1 358 ? 0.204 38.041 34.907 1.00 23.22 ? 351 GLU A C 1 ATOM 2415 O O . GLU A 1 358 ? 1.112 38.088 35.739 1.00 21.47 ? 351 GLU A O 1 ATOM 2416 C CB . GLU A 1 358 ? 0.340 35.988 33.621 1.00 27.03 ? 351 GLU A CB 1 ATOM 2417 C CG . GLU A 1 358 ? 1.568 35.240 33.818 1.00 32.55 ? 351 GLU A CG 1 ATOM 2418 C CD . GLU A 1 358 ? 1.307 33.802 33.414 0.85 40.23 ? 351 GLU A CD 1 ATOM 2419 O OE1 . GLU A 1 358 ? 0.798 33.601 32.286 0.85 45.23 ? 351 GLU A OE1 1 ATOM 2420 O OE2 . GLU A 1 358 ? 1.554 32.896 34.232 0.85 41.60 ? 351 GLU A OE2 1 ATOM 2421 N N . VAL A 1 359 ? -1.054 38.438 35.121 1.00 22.09 ? 352 VAL A N 1 ATOM 2422 C CA . VAL A 1 359 ? -1.499 38.973 36.383 1.00 20.83 ? 352 VAL A CA 1 ATOM 2423 C C . VAL A 1 359 ? -1.507 37.809 37.361 1.00 21.25 ? 352 VAL A C 1 ATOM 2424 O O . VAL A 1 359 ? -2.083 36.764 37.064 1.00 20.25 ? 352 VAL A O 1 ATOM 2425 C CB . VAL A 1 359 ? -2.902 39.600 36.271 1.00 21.06 ? 352 VAL A CB 1 ATOM 2426 C CG1 . VAL A 1 359 ? -3.372 40.151 37.653 1.00 19.71 ? 352 VAL A CG1 1 ATOM 2427 C CG2 . VAL A 1 359 ? -2.877 40.730 35.221 1.00 19.87 ? 352 VAL A CG2 1 ATOM 2428 N N . THR A 1 360 ? -0.815 37.989 38.483 1.00 19.31 ? 353 THR A N 1 ATOM 2429 C CA . THR A 1 360 ? -0.522 36.889 39.408 1.00 20.04 ? 353 THR A CA 1 ATOM 2430 C C . THR A 1 360 ? -0.657 37.417 40.827 1.00 19.73 ? 353 THR A C 1 ATOM 2431 O O . THR A 1 360 ? -0.287 38.578 41.106 1.00 18.84 ? 353 THR A O 1 ATOM 2432 C CB . THR A 1 360 ? 0.928 36.377 39.189 1.00 18.90 ? 353 THR A CB 1 ATOM 2433 O OG1 . THR A 1 360 ? 1.083 36.041 37.793 1.00 20.06 ? 353 THR A OG1 1 ATOM 2434 C CG2 . THR A 1 360 ? 1.188 35.095 40.002 1.00 19.97 ? 353 THR A CG2 1 ATOM 2435 N N . ARG A 1 361 ? -1.170 36.579 41.724 1.00 19.40 ? 354 ARG A N 1 ATOM 2436 C CA . ARG A 1 361 ? -1.355 37.031 43.124 1.00 19.82 ? 354 ARG A CA 1 ATOM 2437 C C . ARG A 1 361 ? -0.021 37.032 43.879 1.00 19.31 ? 354 ARG A C 1 ATOM 2438 O O . ARG A 1 361 ? 0.751 36.061 43.754 1.00 19.55 ? 354 ARG A O 1 ATOM 2439 C CB . ARG A 1 361 ? -2.418 36.155 43.862 1.00 20.68 ? 354 ARG A CB 1 ATOM 2440 C CG . ARG A 1 361 ? -2.676 36.635 45.346 1.00 20.92 ? 354 ARG A CG 1 ATOM 2441 C CD . ARG A 1 361 ? -4.069 36.188 45.785 1.00 23.00 ? 354 ARG A CD 1 ATOM 2442 N NE . ARG A 1 361 ? -5.057 36.943 45.016 1.00 21.84 ? 354 ARG A NE 1 ATOM 2443 C CZ . ARG A 1 361 ? -6.365 36.907 45.196 1.00 24.66 ? 354 ARG A CZ 1 ATOM 2444 N NH1 . ARG A 1 361 ? -6.929 36.123 46.130 1.00 23.39 ? 354 ARG A NH1 1 ATOM 2445 N NH2 . ARG A 1 361 ? -7.115 37.678 44.432 1.00 25.92 ? 354 ARG A NH2 1 ATOM 2446 N N . ILE A 1 362 ? 0.221 38.093 44.672 1.00 17.88 ? 355 ILE A N 1 ATOM 2447 C CA . ILE A 1 362 ? 1.417 38.215 45.523 1.00 18.03 ? 355 ILE A CA 1 ATOM 2448 C C . ILE A 1 362 ? 0.978 38.505 46.958 1.00 18.75 ? 355 ILE A C 1 ATOM 2449 O O . ILE A 1 362 ? -0.141 38.979 47.170 1.00 18.43 ? 355 ILE A O 1 ATOM 2450 C CB . ILE A 1 362 ? 2.408 39.310 45.006 1.00 17.32 ? 355 ILE A CB 1 ATOM 2451 C CG1 . ILE A 1 362 ? 1.751 40.691 45.025 1.00 15.34 ? 355 ILE A CG1 1 ATOM 2452 C CG2 . ILE A 1 362 ? 2.877 38.939 43.560 1.00 15.44 ? 355 ILE A CG2 1 ATOM 2453 C CD1 . ILE A 1 362 ? 2.757 41.895 44.905 1.00 16.22 ? 355 ILE A CD1 1 ATOM 2454 N N . TYR A 1 363 ? 1.856 38.229 47.923 1.00 18.07 ? 356 TYR A N 1 ATOM 2455 C CA . TYR A 1 363 ? 1.517 38.316 49.333 1.00 18.01 ? 356 TYR A CA 1 ATOM 2456 C C . TYR A 1 363 ? 2.610 38.985 50.159 1.00 17.89 ? 356 TYR A C 1 ATOM 2457 O O . TYR A 1 363 ? 3.710 38.417 50.314 1.00 18.66 ? 356 TYR A O 1 ATOM 2458 C CB . TYR A 1 363 ? 1.320 36.909 49.925 1.00 17.80 ? 356 TYR A CB 1 ATOM 2459 C CG . TYR A 1 363 ? 0.286 36.048 49.199 1.00 20.32 ? 356 TYR A CG 1 ATOM 2460 C CD1 . TYR A 1 363 ? -1.034 35.992 49.655 1.00 18.81 ? 356 TYR A CD1 1 ATOM 2461 C CD2 . TYR A 1 363 ? 0.638 35.301 48.047 1.00 20.12 ? 356 TYR A CD2 1 ATOM 2462 C CE1 . TYR A 1 363 ? -1.999 35.209 49.001 1.00 20.55 ? 356 TYR A CE1 1 ATOM 2463 C CE2 . TYR A 1 363 ? -0.312 34.503 47.389 1.00 22.56 ? 356 TYR A CE2 1 ATOM 2464 C CZ . TYR A 1 363 ? -1.643 34.474 47.876 1.00 23.43 ? 356 TYR A CZ 1 ATOM 2465 O OH . TYR A 1 363 ? -2.599 33.715 47.227 1.00 24.24 ? 356 TYR A OH 1 ATOM 2466 N N . ASN A 1 364 ? 2.285 40.116 50.774 1.00 18.08 ? 357 ASN A N 1 ATOM 2467 C CA . ASN A 1 364 ? 3.163 40.725 51.801 1.00 19.28 ? 357 ASN A CA 1 ATOM 2468 C C . ASN A 1 364 ? 2.748 40.173 53.176 1.00 19.55 ? 357 ASN A C 1 ATOM 2469 O O . ASN A 1 364 ? 1.532 40.001 53.430 1.00 21.58 ? 357 ASN A O 1 ATOM 2470 C CB . ASN A 1 364 ? 2.960 42.253 51.850 1.00 17.75 ? 357 ASN A CB 1 ATOM 2471 C CG . ASN A 1 364 ? 3.340 42.929 50.547 1.00 19.34 ? 357 ASN A CG 1 ATOM 2472 O OD1 . ASN A 1 364 ? 4.210 42.439 49.830 1.00 19.37 ? 357 ASN A OD1 1 ATOM 2473 N ND2 . ASN A 1 364 ? 2.671 44.036 50.211 1.00 19.04 ? 357 ASN A ND2 1 ATOM 2474 N N . VAL A 1 365 ? 3.712 39.984 54.079 1.00 18.73 ? 358 VAL A N 1 ATOM 2475 C CA . VAL A 1 365 ? 3.373 39.717 55.480 1.00 18.07 ? 358 VAL A CA 1 ATOM 2476 C C . VAL A 1 365 ? 3.599 41.029 56.229 1.00 18.06 ? 358 VAL A C 1 ATOM 2477 O O . VAL A 1 365 ? 4.686 41.619 56.129 1.00 18.54 ? 358 VAL A O 1 ATOM 2478 C CB . VAL A 1 365 ? 4.243 38.617 56.128 1.00 17.82 ? 358 VAL A CB 1 ATOM 2479 C CG1 . VAL A 1 365 ? 3.675 38.229 57.539 1.00 17.04 ? 358 VAL A CG1 1 ATOM 2480 C CG2 . VAL A 1 365 ? 4.337 37.376 55.213 1.00 17.33 ? 358 VAL A CG2 1 ATOM 2481 N N . ILE A 1 366 ? 2.579 41.474 56.954 1.00 17.69 ? 359 ILE A N 1 ATOM 2482 C CA . ILE A 1 366 ? 2.620 42.738 57.703 1.00 17.51 ? 359 ILE A CA 1 ATOM 2483 C C . ILE A 1 366 ? 2.431 42.429 59.190 1.00 18.89 ? 359 ILE A C 1 ATOM 2484 O O . ILE A 1 366 ? 1.322 41.995 59.603 1.00 20.56 ? 359 ILE A O 1 ATOM 2485 C CB . ILE A 1 366 ? 1.515 43.738 57.218 1.00 17.58 ? 359 ILE A CB 1 ATOM 2486 C CG1 . ILE A 1 366 ? 1.594 43.951 55.666 1.00 14.43 ? 359 ILE A CG1 1 ATOM 2487 C CG2 . ILE A 1 366 ? 1.619 45.107 58.009 1.00 16.71 ? 359 ILE A CG2 1 ATOM 2488 C CD1 . ILE A 1 366 ? 2.943 44.705 55.208 1.00 19.85 ? 359 ILE A CD1 1 ATOM 2489 N N . GLY A 1 367 ? 3.493 42.634 59.990 1.00 18.90 ? 360 GLY A N 1 ATOM 2490 C CA . GLY A 1 367 ? 3.459 42.371 61.443 1.00 18.85 ? 360 GLY A CA 1 ATOM 2491 C C . GLY A 1 367 ? 3.355 43.676 62.211 1.00 19.78 ? 360 GLY A C 1 ATOM 2492 O O . GLY A 1 367 ? 3.968 44.637 61.802 1.00 20.04 ? 360 GLY A O 1 ATOM 2493 N N . THR A 1 368 ? 2.588 43.730 63.317 1.00 20.24 ? 361 THR A N 1 ATOM 2494 C CA . THR A 1 368 ? 2.425 44.976 64.094 1.00 20.74 ? 361 THR A CA 1 ATOM 2495 C C . THR A 1 368 ? 2.834 44.760 65.546 1.00 22.08 ? 361 THR A C 1 ATOM 2496 O O . THR A 1 368 ? 2.377 43.788 66.215 1.00 20.79 ? 361 THR A O 1 ATOM 2497 C CB . THR A 1 368 ? 0.953 45.462 64.056 1.00 20.71 ? 361 THR A CB 1 ATOM 2498 O OG1 . THR A 1 368 ? 0.619 45.723 62.692 1.00 22.68 ? 361 THR A OG1 1 ATOM 2499 C CG2 . THR A 1 368 ? 0.742 46.795 64.807 1.00 21.73 ? 361 THR A CG2 1 ATOM 2500 N N . LEU A 1 369 ? 3.674 45.669 66.056 1.00 22.12 ? 362 LEU A N 1 ATOM 2501 C CA . LEU A 1 369 ? 3.962 45.691 67.498 1.00 22.34 ? 362 LEU A CA 1 ATOM 2502 C C . LEU A 1 369 ? 3.476 47.073 67.955 1.00 22.79 ? 362 LEU A C 1 ATOM 2503 O O . LEU A 1 369 ? 4.143 48.063 67.700 1.00 23.02 ? 362 LEU A O 1 ATOM 2504 C CB . LEU A 1 369 ? 5.477 45.462 67.734 1.00 22.20 ? 362 LEU A CB 1 ATOM 2505 C CG . LEU A 1 369 ? 6.062 45.565 69.167 1.00 25.13 ? 362 LEU A CG 1 ATOM 2506 C CD1 . LEU A 1 369 ? 5.269 44.778 70.157 1.00 24.45 ? 362 LEU A CD1 1 ATOM 2507 C CD2 . LEU A 1 369 ? 7.499 45.095 69.179 1.00 24.76 ? 362 LEU A CD2 1 ATOM 2508 N N A ARG A 1 370 ? 2.313 47.117 68.607 0.35 22.65 ? 363 ARG A N 1 ATOM 2509 N N B ARG A 1 370 ? 2.322 47.113 68.621 0.35 22.54 ? 363 ARG A N 1 ATOM 2510 N N C ARG A 1 370 ? 2.314 47.109 68.615 0.30 22.62 ? 363 ARG A N 1 ATOM 2511 C CA A ARG A 1 370 ? 1.675 48.377 68.975 0.35 22.95 ? 363 ARG A CA 1 ATOM 2512 C CA B ARG A 1 370 ? 1.651 48.360 68.989 0.35 22.75 ? 363 ARG A CA 1 ATOM 2513 C CA C ARG A 1 370 ? 1.637 48.353 68.997 0.30 22.84 ? 363 ARG A CA 1 ATOM 2514 C C A ARG A 1 370 ? 2.531 49.164 69.967 0.35 23.17 ? 363 ARG A C 1 ATOM 2515 C C B ARG A 1 370 ? 2.472 49.172 70.000 0.35 23.05 ? 363 ARG A C 1 ATOM 2516 C C C ARG A 1 370 ? 2.478 49.169 69.995 0.30 23.08 ? 363 ARG A C 1 ATOM 2517 O O A ARG A 1 370 ? 3.067 48.597 70.937 0.35 22.70 ? 363 ARG A O 1 ATOM 2518 O O B ARG A 1 370 ? 2.928 48.626 71.021 0.35 22.53 ? 363 ARG A O 1 ATOM 2519 O O C ARG A 1 370 ? 2.964 48.619 70.998 0.30 22.66 ? 363 ARG A O 1 ATOM 2520 C CB A ARG A 1 370 ? 0.284 48.120 69.580 0.35 23.30 ? 363 ARG A CB 1 ATOM 2521 C CB B ARG A 1 370 ? 0.272 48.028 69.584 0.35 22.95 ? 363 ARG A CB 1 ATOM 2522 C CB C ARG A 1 370 ? 0.251 48.032 69.608 0.30 23.04 ? 363 ARG A CB 1 ATOM 2523 C CG A ARG A 1 370 ? -0.381 49.360 70.149 0.35 23.12 ? 363 ARG A CG 1 ATOM 2524 C CG B ARG A 1 370 ? -0.609 49.220 69.889 0.35 22.30 ? 363 ARG A CG 1 ATOM 2525 C CG C ARG A 1 370 ? -0.599 47.037 68.786 0.15 22.55 ? 363 ARG A CG 1 ATOM 2526 C CD A ARG A 1 370 ? -1.806 49.083 70.591 0.35 25.88 ? 363 ARG A CD 1 ATOM 2527 C CD B ARG A 1 370 ? -2.042 48.772 70.148 0.35 23.63 ? 363 ARG A CD 1 ATOM 2528 C CD C ARG A 1 370 ? -1.963 46.702 69.435 0.15 23.03 ? 363 ARG A CD 1 ATOM 2529 N NE A ARG A 1 370 ? -1.909 47.784 71.259 0.35 28.65 ? 363 ARG A NE 1 ATOM 2530 N NE B ARG A 1 370 ? -2.104 47.643 71.083 0.35 25.91 ? 363 ARG A NE 1 ATOM 2531 N NE C ARG A 1 370 ? -2.823 45.908 68.546 0.30 22.25 ? 363 ARG A NE 1 ATOM 2532 C CZ A ARG A 1 370 ? -1.694 47.575 72.554 0.35 27.68 ? 363 ARG A CZ 1 ATOM 2533 C CZ B ARG A 1 370 ? -2.544 46.425 70.773 0.35 24.15 ? 363 ARG A CZ 1 ATOM 2534 C CZ C ARG A 1 370 ? -3.406 44.752 68.870 0.30 21.68 ? 363 ARG A CZ 1 ATOM 2535 N NH1 A ARG A 1 370 ? -1.358 48.576 73.354 0.35 28.28 ? 363 ARG A NH1 1 ATOM 2536 N NH1 B ARG A 1 370 ? -2.978 46.167 69.542 0.35 24.10 ? 363 ARG A NH1 1 ATOM 2537 N NH1 C ARG A 1 370 ? -4.157 44.114 67.980 0.30 20.96 ? 363 ARG A NH1 1 ATOM 2538 N NH2 A ARG A 1 370 ? -1.823 46.357 73.046 0.35 28.68 ? 363 ARG A NH2 1 ATOM 2539 N NH2 B ARG A 1 370 ? -2.565 45.477 71.698 0.35 20.86 ? 363 ARG A NH2 1 ATOM 2540 N NH2 C ARG A 1 370 ? -3.258 44.238 70.080 0.30 21.59 ? 363 ARG A NH2 1 ATOM 2541 N N . GLY A 1 371 ? 2.652 50.465 69.715 1.00 23.02 ? 364 GLY A N 1 ATOM 2542 C CA . GLY A 1 371 ? 3.314 51.393 70.657 1.00 23.06 ? 364 GLY A CA 1 ATOM 2543 C C . GLY A 1 371 ? 2.523 51.604 71.950 1.00 24.42 ? 364 GLY A C 1 ATOM 2544 O O . GLY A 1 371 ? 1.286 51.703 71.949 1.00 23.79 ? 364 GLY A O 1 ATOM 2545 N N . ALA A 1 372 ? 3.244 51.704 73.069 1.00 24.91 ? 365 ALA A N 1 ATOM 2546 C CA . ALA A 1 372 ? 2.619 51.964 74.362 1.00 25.22 ? 365 ALA A CA 1 ATOM 2547 C C . ALA A 1 372 ? 2.151 53.390 74.471 1.00 26.13 ? 365 ALA A C 1 ATOM 2548 O O . ALA A 1 372 ? 1.162 53.652 75.166 1.00 26.57 ? 365 ALA A O 1 ATOM 2549 C CB . ALA A 1 372 ? 3.577 51.660 75.515 1.00 24.94 ? 365 ALA A CB 1 ATOM 2550 N N . VAL A 1 373 ? 2.846 54.336 73.831 1.00 25.76 ? 366 VAL A N 1 ATOM 2551 C CA . VAL A 1 373 ? 2.510 55.754 74.098 1.00 25.45 ? 366 VAL A CA 1 ATOM 2552 C C . VAL A 1 373 ? 2.046 56.489 72.829 1.00 24.95 ? 366 VAL A C 1 ATOM 2553 O O . VAL A 1 373 ? 1.130 57.325 72.897 1.00 25.01 ? 366 VAL A O 1 ATOM 2554 C CB . VAL A 1 373 ? 3.685 56.540 74.750 1.00 26.03 ? 366 VAL A CB 1 ATOM 2555 C CG1 . VAL A 1 373 ? 3.321 58.067 74.917 1.00 24.41 ? 366 VAL A CG1 1 ATOM 2556 C CG2 . VAL A 1 373 ? 4.142 55.890 76.096 1.00 27.72 ? 366 VAL A CG2 1 ATOM 2557 N N . GLU A 1 374 ? 2.668 56.181 71.681 1.00 23.94 ? 367 GLU A N 1 ATOM 2558 C CA . GLU A 1 374 ? 2.256 56.796 70.416 1.00 23.86 ? 367 GLU A CA 1 ATOM 2559 C C . GLU A 1 374 ? 1.948 55.701 69.399 1.00 22.32 ? 367 GLU A C 1 ATOM 2560 O O . GLU A 1 374 ? 2.747 55.503 68.485 1.00 20.32 ? 367 GLU A O 1 ATOM 2561 C CB . GLU A 1 374 ? 3.338 57.725 69.870 1.00 23.79 ? 367 GLU A CB 1 ATOM 2562 C CG . GLU A 1 374 ? 3.710 58.857 70.828 1.00 26.48 ? 367 GLU A CG 1 ATOM 2563 C CD . GLU A 1 374 ? 4.713 59.805 70.184 1.00 27.40 ? 367 GLU A CD 1 ATOM 2564 O OE1 . GLU A 1 374 ? 4.295 60.689 69.419 1.00 27.74 ? 367 GLU A OE1 1 ATOM 2565 O OE2 . GLU A 1 374 ? 5.921 59.666 70.451 1.00 27.52 ? 367 GLU A OE2 1 ATOM 2566 N N . PRO A 1 375 ? 0.836 54.948 69.603 1.00 22.33 ? 368 PRO A N 1 ATOM 2567 C CA . PRO A 1 375 ? 0.532 53.815 68.698 1.00 21.64 ? 368 PRO A CA 1 ATOM 2568 C C . PRO A 1 375 ? 0.262 54.314 67.260 1.00 21.27 ? 368 PRO A C 1 ATOM 2569 O O . PRO A 1 375 ? 0.355 53.540 66.310 1.00 20.79 ? 368 PRO A O 1 ATOM 2570 C CB . PRO A 1 375 ? -0.691 53.155 69.351 1.00 21.27 ? 368 PRO A CB 1 ATOM 2571 C CG . PRO A 1 375 ? -1.313 54.261 70.222 1.00 22.93 ? 368 PRO A CG 1 ATOM 2572 C CD . PRO A 1 375 ? -0.113 55.013 70.746 1.00 23.08 ? 368 PRO A CD 1 ATOM 2573 N N . ASP A 1 376 ? 0.014 55.623 67.120 1.00 20.41 ? 369 ASP A N 1 ATOM 2574 C CA . ASP A 1 376 ? -0.291 56.235 65.799 1.00 20.91 ? 369 ASP A CA 1 ATOM 2575 C C . ASP A 1 376 ? 0.957 56.814 65.118 1.00 19.61 ? 369 ASP A C 1 ATOM 2576 O O . ASP A 1 376 ? 0.856 57.681 64.258 1.00 18.57 ? 369 ASP A O 1 ATOM 2577 C CB . ASP A 1 376 ? -1.375 57.319 65.948 1.00 20.81 ? 369 ASP A CB 1 ATOM 2578 C CG . ASP A 1 376 ? -0.861 58.575 66.633 1.00 25.51 ? 369 ASP A CG 1 ATOM 2579 O OD1 . ASP A 1 376 ? 0.129 58.472 67.417 1.00 27.29 ? 369 ASP A OD1 1 ATOM 2580 O OD2 . ASP A 1 376 ? -1.471 59.666 66.412 1.00 29.48 ? 369 ASP A OD2 1 ATOM 2581 N N . ARG A 1 377 ? 2.134 56.325 65.511 1.00 19.59 ? 370 ARG A N 1 ATOM 2582 C CA . ARG A 1 377 ? 3.386 56.713 64.858 1.00 18.91 ? 370 ARG A CA 1 ATOM 2583 C C . ARG A 1 377 ? 4.046 55.433 64.470 1.00 19.09 ? 370 ARG A C 1 ATOM 2584 O O . ARG A 1 377 ? 4.182 54.536 65.341 1.00 19.20 ? 370 ARG A O 1 ATOM 2585 C CB . ARG A 1 377 ? 4.264 57.527 65.818 1.00 18.44 ? 370 ARG A CB 1 ATOM 2586 C CG . ARG A 1 377 ? 3.638 58.918 66.153 1.00 17.35 ? 370 ARG A CG 1 ATOM 2587 C CD . ARG A 1 377 ? 3.812 59.831 64.909 1.00 18.02 ? 370 ARG A CD 1 ATOM 2588 N NE . ARG A 1 377 ? 3.202 61.172 64.978 1.00 17.67 ? 370 ARG A NE 1 ATOM 2589 C CZ . ARG A 1 377 ? 1.966 61.476 64.542 1.00 18.25 ? 370 ARG A CZ 1 ATOM 2590 N NH1 . ARG A 1 377 ? 1.100 60.539 64.077 1.00 17.86 ? 370 ARG A NH1 1 ATOM 2591 N NH2 . ARG A 1 377 ? 1.580 62.740 64.566 1.00 16.86 ? 370 ARG A NH2 1 ATOM 2592 N N . TYR A 1 378 ? 4.445 55.323 63.190 1.00 18.79 ? 371 TYR A N 1 ATOM 2593 C CA . TYR A 1 378 ? 4.948 54.033 62.680 1.00 18.32 ? 371 TYR A CA 1 ATOM 2594 C C . TYR A 1 378 ? 6.397 54.073 62.303 1.00 18.55 ? 371 TYR A C 1 ATOM 2595 O O . TYR A 1 378 ? 6.838 54.917 61.470 1.00 18.49 ? 371 TYR A O 1 ATOM 2596 C CB . TYR A 1 378 ? 4.177 53.585 61.433 1.00 18.18 ? 371 TYR A CB 1 ATOM 2597 C CG . TYR A 1 378 ? 2.646 53.549 61.568 1.00 19.07 ? 371 TYR A CG 1 ATOM 2598 C CD1 . TYR A 1 378 ? 2.026 53.119 62.752 1.00 18.66 ? 371 TYR A CD1 1 ATOM 2599 C CD2 . TYR A 1 378 ? 1.835 53.870 60.462 1.00 18.10 ? 371 TYR A CD2 1 ATOM 2600 C CE1 . TYR A 1 378 ? 0.626 53.067 62.853 1.00 20.63 ? 371 TYR A CE1 1 ATOM 2601 C CE2 . TYR A 1 378 ? 0.461 53.802 60.529 1.00 19.02 ? 371 TYR A CE2 1 ATOM 2602 C CZ . TYR A 1 378 ? -0.146 53.404 61.723 1.00 19.79 ? 371 TYR A CZ 1 ATOM 2603 O OH . TYR A 1 378 ? -1.512 53.329 61.779 1.00 18.83 ? 371 TYR A OH 1 ATOM 2604 N N . VAL A 1 379 ? 7.141 53.119 62.852 1.00 17.86 ? 372 VAL A N 1 ATOM 2605 C CA . VAL A 1 379 ? 8.516 52.913 62.430 1.00 17.55 ? 372 VAL A CA 1 ATOM 2606 C C . VAL A 1 379 ? 8.478 51.555 61.704 1.00 17.81 ? 372 VAL A C 1 ATOM 2607 O O . VAL A 1 379 ? 8.042 50.555 62.284 1.00 17.37 ? 372 VAL A O 1 ATOM 2608 C CB . VAL A 1 379 ? 9.473 52.872 63.655 1.00 17.28 ? 372 VAL A CB 1 ATOM 2609 C CG1 . VAL A 1 379 ? 10.913 52.497 63.203 1.00 15.97 ? 372 VAL A CG1 1 ATOM 2610 C CG2 . VAL A 1 379 ? 9.439 54.259 64.409 1.00 16.65 ? 372 VAL A CG2 1 ATOM 2611 N N . ILE A 1 380 ? 8.922 51.536 60.434 1.00 17.63 ? 373 ILE A N 1 ATOM 2612 C CA . ILE A 1 380 ? 8.773 50.352 59.578 1.00 16.98 ? 373 ILE A CA 1 ATOM 2613 C C . ILE A 1 380 ? 10.111 49.722 59.279 1.00 17.29 ? 373 ILE A C 1 ATOM 2614 O O . ILE A 1 380 ? 11.061 50.402 58.847 1.00 18.10 ? 373 ILE A O 1 ATOM 2615 C CB . ILE A 1 380 ? 8.034 50.712 58.276 1.00 17.04 ? 373 ILE A CB 1 ATOM 2616 C CG1 . ILE A 1 380 ? 6.749 51.468 58.622 1.00 17.41 ? 373 ILE A CG1 1 ATOM 2617 C CG2 . ILE A 1 380 ? 7.746 49.432 57.383 1.00 15.50 ? 373 ILE A CG2 1 ATOM 2618 C CD1 . ILE A 1 380 ? 6.016 52.048 57.363 1.00 20.39 ? 373 ILE A CD1 1 ATOM 2619 N N . LEU A 1 381 ? 10.192 48.418 59.516 1.00 16.71 ? 374 LEU A N 1 ATOM 2620 C CA . LEU A 1 381 ? 11.336 47.627 59.095 1.00 16.73 ? 374 LEU A CA 1 ATOM 2621 C C . LEU A 1 381 ? 10.820 46.709 58.008 1.00 17.10 ? 374 LEU A C 1 ATOM 2622 O O . LEU A 1 381 ? 9.998 45.822 58.310 1.00 17.84 ? 374 LEU A O 1 ATOM 2623 C CB . LEU A 1 381 ? 11.888 46.791 60.273 1.00 15.84 ? 374 LEU A CB 1 ATOM 2624 C CG . LEU A 1 381 ? 13.090 45.883 59.940 1.00 16.59 ? 374 LEU A CG 1 ATOM 2625 C CD1 . LEU A 1 381 ? 14.329 46.651 59.348 1.00 16.26 ? 374 LEU A CD1 1 ATOM 2626 C CD2 . LEU A 1 381 ? 13.526 45.010 61.167 1.00 16.24 ? 374 LEU A CD2 1 ATOM 2627 N N . GLY A 1 382 ? 11.296 46.881 56.763 1.00 17.26 ? 375 GLY A N 1 ATOM 2628 C CA . GLY A 1 382 ? 10.745 46.096 55.629 1.00 16.37 ? 375 GLY A CA 1 ATOM 2629 C C . GLY A 1 382 ? 11.843 45.554 54.725 1.00 16.76 ? 375 GLY A C 1 ATOM 2630 O O . GLY A 1 382 ? 12.860 46.210 54.518 1.00 16.73 ? 375 GLY A O 1 ATOM 2631 N N . GLY A 1 383 ? 11.638 44.358 54.174 1.00 16.20 ? 376 GLY A N 1 ATOM 2632 C CA . GLY A 1 383 ? 12.559 43.820 53.192 1.00 16.11 ? 376 GLY A CA 1 ATOM 2633 C C . GLY A 1 383 ? 11.790 42.747 52.462 1.00 16.32 ? 376 GLY A C 1 ATOM 2634 O O . GLY A 1 383 ? 10.823 42.230 52.994 1.00 17.15 ? 376 GLY A O 1 ATOM 2635 N N . HIS A 1 384 ? 12.221 42.387 51.256 1.00 16.42 ? 377 HIS A N 1 ATOM 2636 C CA . HIS A 1 384 ? 11.453 41.428 50.469 1.00 16.05 ? 377 HIS A CA 1 ATOM 2637 C C . HIS A 1 384 ? 11.819 39.976 50.766 1.00 17.71 ? 377 HIS A C 1 ATOM 2638 O O . HIS A 1 384 ? 12.876 39.719 51.387 1.00 18.07 ? 377 HIS A O 1 ATOM 2639 C CB . HIS A 1 384 ? 11.545 41.755 48.951 1.00 15.85 ? 377 HIS A CB 1 ATOM 2640 C CG . HIS A 1 384 ? 12.845 41.428 48.281 1.00 16.23 ? 377 HIS A CG 1 ATOM 2641 N ND1 . HIS A 1 384 ? 12.995 40.314 47.478 1.00 17.14 ? 377 HIS A ND1 1 ATOM 2642 C CD2 . HIS A 1 384 ? 13.984 42.157 48.124 1.00 15.85 ? 377 HIS A CD2 1 ATOM 2643 C CE1 . HIS A 1 384 ? 14.182 40.347 46.886 1.00 16.44 ? 377 HIS A CE1 1 ATOM 2644 N NE2 . HIS A 1 384 ? 14.797 41.448 47.272 1.00 15.61 ? 377 HIS A NE2 1 ATOM 2645 N N . ARG A 1 385 ? 10.966 39.061 50.289 1.00 17.24 ? 378 ARG A N 1 ATOM 2646 C CA . ARG A 1 385 ? 11.034 37.654 50.595 1.00 17.27 ? 378 ARG A CA 1 ATOM 2647 C C . ARG A 1 385 ? 11.178 36.845 49.286 1.00 17.52 ? 378 ARG A C 1 ATOM 2648 O O . ARG A 1 385 ? 11.795 35.747 49.264 1.00 17.20 ? 378 ARG A O 1 ATOM 2649 C CB . ARG A 1 385 ? 9.735 37.256 51.297 1.00 17.43 ? 378 ARG A CB 1 ATOM 2650 C CG . ARG A 1 385 ? 9.650 35.776 51.725 1.00 17.17 ? 378 ARG A CG 1 ATOM 2651 C CD . ARG A 1 385 ? 8.231 35.409 52.153 1.00 18.07 ? 378 ARG A CD 1 ATOM 2652 N NE . ARG A 1 385 ? 7.223 35.476 51.052 1.00 18.22 ? 378 ARG A NE 1 ATOM 2653 C CZ . ARG A 1 385 ? 6.310 36.456 50.866 1.00 17.83 ? 378 ARG A CZ 1 ATOM 2654 N NH1 . ARG A 1 385 ? 6.228 37.514 51.679 1.00 14.84 ? 378 ARG A NH1 1 ATOM 2655 N NH2 . ARG A 1 385 ? 5.459 36.395 49.826 1.00 17.72 ? 378 ARG A NH2 1 ATOM 2656 N N . ASP A 1 386 ? 10.616 37.380 48.189 1.00 16.90 ? 379 ASP A N 1 ATOM 2657 C CA . ASP A 1 386 ? 10.738 36.692 46.861 1.00 16.34 ? 379 ASP A CA 1 ATOM 2658 C C . ASP A 1 386 ? 12.177 36.721 46.377 1.00 16.58 ? 379 ASP A C 1 ATOM 2659 O O . ASP A 1 386 ? 12.890 37.706 46.592 1.00 16.36 ? 379 ASP A O 1 ATOM 2660 C CB . ASP A 1 386 ? 9.846 37.324 45.795 1.00 14.68 ? 379 ASP A CB 1 ATOM 2661 C CG . ASP A 1 386 ? 10.253 38.768 45.488 1.00 15.55 ? 379 ASP A CG 1 ATOM 2662 O OD1 . ASP A 1 386 ? 10.292 39.638 46.421 1.00 16.55 ? 379 ASP A OD1 1 ATOM 2663 O OD2 . ASP A 1 386 ? 10.529 39.029 44.320 1.00 15.44 ? 379 ASP A OD2 1 ATOM 2664 N N . SER A 1 387 ? 12.593 35.646 45.704 1.00 16.59 ? 380 SER A N 1 ATOM 2665 C CA . SER A 1 387 ? 13.951 35.524 45.221 1.00 17.91 ? 380 SER A CA 1 ATOM 2666 C C . SER A 1 387 ? 13.909 35.090 43.741 1.00 18.79 ? 380 SER A C 1 ATOM 2667 O O . SER A 1 387 ? 12.869 34.545 43.293 1.00 19.76 ? 380 SER A O 1 ATOM 2668 C CB . SER A 1 387 ? 14.715 34.488 46.072 1.00 17.44 ? 380 SER A CB 1 ATOM 2669 O OG . SER A 1 387 ? 14.126 33.193 45.966 1.00 19.39 ? 380 SER A OG 1 ATOM 2670 N N . TRP A 1 388 ? 14.988 35.337 42.977 1.00 18.18 ? 381 TRP A N 1 ATOM 2671 C CA . TRP A 1 388 ? 15.103 34.733 41.627 1.00 18.51 ? 381 TRP A CA 1 ATOM 2672 C C . TRP A 1 388 ? 15.204 33.210 41.677 1.00 18.66 ? 381 TRP A C 1 ATOM 2673 O O . TRP A 1 388 ? 14.432 32.519 41.036 1.00 19.93 ? 381 TRP A O 1 ATOM 2674 C CB . TRP A 1 388 ? 16.232 35.378 40.752 1.00 18.42 ? 381 TRP A CB 1 ATOM 2675 C CG . TRP A 1 388 ? 15.745 36.693 40.211 1.00 17.45 ? 381 TRP A CG 1 ATOM 2676 C CD1 . TRP A 1 388 ? 16.249 37.951 40.469 1.00 19.13 ? 381 TRP A CD1 1 ATOM 2677 C CD2 . TRP A 1 388 ? 14.607 36.873 39.352 1.00 17.95 ? 381 TRP A CD2 1 ATOM 2678 N NE1 . TRP A 1 388 ? 15.481 38.906 39.801 1.00 20.01 ? 381 TRP A NE1 1 ATOM 2679 C CE2 . TRP A 1 388 ? 14.457 38.268 39.130 1.00 19.41 ? 381 TRP A CE2 1 ATOM 2680 C CE3 . TRP A 1 388 ? 13.680 35.975 38.747 1.00 17.30 ? 381 TRP A CE3 1 ATOM 2681 C CZ2 . TRP A 1 388 ? 13.406 38.797 38.326 1.00 18.70 ? 381 TRP A CZ2 1 ATOM 2682 C CZ3 . TRP A 1 388 ? 12.623 36.499 37.977 1.00 16.24 ? 381 TRP A CZ3 1 ATOM 2683 C CH2 . TRP A 1 388 ? 12.499 37.902 37.772 1.00 18.60 ? 381 TRP A CH2 1 ATOM 2684 N N . VAL A 1 389 ? 16.125 32.666 42.466 1.00 19.32 ? 382 VAL A N 1 ATOM 2685 C CA . VAL A 1 389 ? 16.166 31.217 42.690 1.00 18.46 ? 382 VAL A CA 1 ATOM 2686 C C . VAL A 1 389 ? 16.204 31.014 44.214 1.00 19.28 ? 382 VAL A C 1 ATOM 2687 O O . VAL A 1 389 ? 15.171 31.205 44.867 1.00 19.32 ? 382 VAL A O 1 ATOM 2688 C CB . VAL A 1 389 ? 17.343 30.515 41.917 1.00 17.70 ? 382 VAL A CB 1 ATOM 2689 C CG1 . VAL A 1 389 ? 17.108 28.947 41.859 1.00 16.72 ? 382 VAL A CG1 1 ATOM 2690 C CG2 . VAL A 1 389 ? 17.373 31.012 40.486 1.00 17.74 ? 382 VAL A CG2 1 ATOM 2691 N N . PHE A 1 390 ? 17.366 30.653 44.783 1.00 19.34 ? 383 PHE A N 1 ATOM 2692 C CA . PHE A 1 390 ? 17.435 30.290 46.223 1.00 19.34 ? 383 PHE A CA 1 ATOM 2693 C C . PHE A 1 390 ? 17.558 31.500 47.116 1.00 19.80 ? 383 PHE A C 1 ATOM 2694 O O . PHE A 1 390 ? 17.212 31.426 48.305 1.00 20.68 ? 383 PHE A O 1 ATOM 2695 C CB . PHE A 1 390 ? 18.587 29.297 46.498 1.00 18.26 ? 383 PHE A CB 1 ATOM 2696 C CG . PHE A 1 390 ? 18.439 28.028 45.731 1.00 20.91 ? 383 PHE A CG 1 ATOM 2697 C CD1 . PHE A 1 390 ? 17.405 27.130 46.042 1.00 21.02 ? 383 PHE A CD1 1 ATOM 2698 C CD2 . PHE A 1 390 ? 19.250 27.767 44.623 1.00 21.23 ? 383 PHE A CD2 1 ATOM 2699 C CE1 . PHE A 1 390 ? 17.216 25.963 45.290 1.00 20.97 ? 383 PHE A CE1 1 ATOM 2700 C CE2 . PHE A 1 390 ? 19.057 26.580 43.855 1.00 21.51 ? 383 PHE A CE2 1 ATOM 2701 C CZ . PHE A 1 390 ? 18.039 25.699 44.194 1.00 21.12 ? 383 PHE A CZ 1 ATOM 2702 N N . GLY A 1 391 ? 18.065 32.606 46.560 1.00 19.65 ? 384 GLY A N 1 ATOM 2703 C CA . GLY A 1 391 ? 18.165 33.869 47.339 1.00 18.74 ? 384 GLY A CA 1 ATOM 2704 C C . GLY A 1 391 ? 19.084 33.811 48.550 1.00 19.37 ? 384 GLY A C 1 ATOM 2705 O O . GLY A 1 391 ? 18.804 34.495 49.564 1.00 18.97 ? 384 GLY A O 1 ATOM 2706 N N . GLY A 1 392 ? 20.199 33.038 48.437 1.00 19.18 ? 385 GLY A N 1 ATOM 2707 C CA . GLY A 1 392 ? 21.172 32.878 49.535 1.00 18.71 ? 385 GLY A CA 1 ATOM 2708 C C . GLY A 1 392 ? 21.615 34.222 50.092 1.00 19.52 ? 385 GLY A C 1 ATOM 2709 O O . GLY A 1 392 ? 21.743 34.384 51.310 1.00 19.33 ? 385 GLY A O 1 ATOM 2710 N N . ILE A 1 393 ? 21.884 35.190 49.193 1.00 18.48 ? 386 ILE A N 1 ATOM 2711 C CA . ILE A 1 393 ? 22.189 36.521 49.643 1.00 18.21 ? 386 ILE A CA 1 ATOM 2712 C C . ILE A 1 393 ? 20.924 37.372 49.483 1.00 18.21 ? 386 ILE A C 1 ATOM 2713 O O . ILE A 1 393 ? 20.392 37.958 50.472 1.00 18.90 ? 386 ILE A O 1 ATOM 2714 C CB . ILE A 1 393 ? 23.406 37.126 48.883 1.00 18.11 ? 386 ILE A CB 1 ATOM 2715 C CG1 . ILE A 1 393 ? 24.697 36.454 49.369 1.00 19.55 ? 386 ILE A CG1 1 ATOM 2716 C CG2 . ILE A 1 393 ? 23.491 38.672 49.107 1.00 18.48 ? 386 ILE A CG2 1 ATOM 2717 C CD1 . ILE A 1 393 ? 25.910 36.882 48.600 1.00 20.83 ? 386 ILE A CD1 1 ATOM 2718 N N . ASP A 1 394 ? 20.418 37.410 48.251 1.00 17.22 ? 387 ASP A N 1 ATOM 2719 C CA . ASP A 1 394 ? 19.359 38.364 47.896 1.00 17.42 ? 387 ASP A CA 1 ATOM 2720 C C . ASP A 1 394 ? 18.025 37.616 47.761 1.00 16.55 ? 387 ASP A C 1 ATOM 2721 O O . ASP A 1 394 ? 17.837 36.910 46.763 1.00 17.79 ? 387 ASP A O 1 ATOM 2722 C CB . ASP A 1 394 ? 19.775 39.063 46.577 1.00 17.25 ? 387 ASP A CB 1 ATOM 2723 C CG . ASP A 1 394 ? 18.714 40.015 46.042 1.00 19.63 ? 387 ASP A CG 1 ATOM 2724 O OD1 . ASP A 1 394 ? 17.726 40.237 46.784 1.00 18.47 ? 387 ASP A OD1 1 ATOM 2725 O OD2 . ASP A 1 394 ? 18.844 40.505 44.859 1.00 19.50 ? 387 ASP A OD2 1 ATOM 2726 N N . PRO A 1 395 ? 17.081 37.773 48.716 1.00 16.12 ? 388 PRO A N 1 ATOM 2727 C CA . PRO A 1 395 ? 17.019 38.660 49.888 1.00 16.63 ? 388 PRO A CA 1 ATOM 2728 C C . PRO A 1 395 ? 17.190 37.939 51.211 1.00 18.04 ? 388 PRO A C 1 ATOM 2729 O O . PRO A 1 395 ? 17.117 38.597 52.252 1.00 19.28 ? 388 PRO A O 1 ATOM 2730 C CB . PRO A 1 395 ? 15.563 39.194 49.838 1.00 15.89 ? 388 PRO A CB 1 ATOM 2731 C CG . PRO A 1 395 ? 14.766 37.928 49.423 1.00 15.56 ? 388 PRO A CG 1 ATOM 2732 C CD . PRO A 1 395 ? 15.755 37.187 48.429 1.00 16.15 ? 388 PRO A CD 1 ATOM 2733 N N . GLN A 1 396 ? 17.415 36.613 51.207 1.00 18.84 ? 389 GLN A N 1 ATOM 2734 C CA . GLN A 1 396 ? 17.207 35.880 52.454 1.00 19.08 ? 389 GLN A CA 1 ATOM 2735 C C . GLN A 1 396 ? 18.251 36.222 53.522 1.00 19.89 ? 389 GLN A C 1 ATOM 2736 O O . GLN A 1 396 ? 17.975 36.054 54.708 1.00 19.72 ? 389 GLN A O 1 ATOM 2737 C CB . GLN A 1 396 ? 17.087 34.352 52.270 1.00 18.74 ? 389 GLN A CB 1 ATOM 2738 C CG . GLN A 1 396 ? 16.064 33.897 51.222 1.00 19.25 ? 389 GLN A CG 1 ATOM 2739 C CD . GLN A 1 396 ? 14.655 34.441 51.433 1.00 20.23 ? 389 GLN A CD 1 ATOM 2740 O OE1 . GLN A 1 396 ? 14.322 34.996 52.486 1.00 20.82 ? 389 GLN A OE1 1 ATOM 2741 N NE2 . GLN A 1 396 ? 13.803 34.252 50.425 1.00 19.12 ? 389 GLN A NE2 1 ATOM 2742 N N . SER A 1 397 ? 19.440 36.693 53.114 1.00 20.23 ? 390 SER A N 1 ATOM 2743 C CA . SER A 1 397 ? 20.399 37.151 54.122 1.00 20.13 ? 390 SER A CA 1 ATOM 2744 C C . SER A 1 397 ? 19.841 38.378 54.886 1.00 19.44 ? 390 SER A C 1 ATOM 2745 O O . SER A 1 397 ? 20.181 38.584 56.067 1.00 19.83 ? 390 SER A O 1 ATOM 2746 C CB . SER A 1 397 ? 21.793 37.436 53.528 1.00 19.72 ? 390 SER A CB 1 ATOM 2747 O OG . SER A 1 397 ? 21.750 38.612 52.756 1.00 19.48 ? 390 SER A OG 1 ATOM 2748 N N . GLY A 1 398 ? 18.996 39.174 54.218 1.00 18.63 ? 391 GLY A N 1 ATOM 2749 C CA . GLY A 1 398 ? 18.290 40.284 54.886 1.00 18.11 ? 391 GLY A CA 1 ATOM 2750 C C . GLY A 1 398 ? 17.076 39.787 55.648 1.00 18.35 ? 391 GLY A C 1 ATOM 2751 O O . GLY A 1 398 ? 16.834 40.194 56.800 1.00 18.73 ? 391 GLY A O 1 ATOM 2752 N N . ALA A 1 399 ? 16.302 38.906 55.026 1.00 17.78 ? 392 ALA A N 1 ATOM 2753 C CA . ALA A 1 399 ? 15.069 38.392 55.663 1.00 19.04 ? 392 ALA A CA 1 ATOM 2754 C C . ALA A 1 399 ? 15.369 37.594 56.928 1.00 19.21 ? 392 ALA A C 1 ATOM 2755 O O . ALA A 1 399 ? 14.600 37.653 57.905 1.00 20.06 ? 392 ALA A O 1 ATOM 2756 C CB . ALA A 1 399 ? 14.238 37.548 54.677 1.00 18.73 ? 392 ALA A CB 1 ATOM 2757 N N . ALA A 1 400 ? 16.493 36.867 56.947 1.00 19.97 ? 393 ALA A N 1 ATOM 2758 C CA . ALA A 1 400 ? 16.849 36.094 58.155 1.00 19.63 ? 393 ALA A CA 1 ATOM 2759 C C . ALA A 1 400 ? 17.162 37.066 59.300 1.00 20.59 ? 393 ALA A C 1 ATOM 2760 O O . ALA A 1 400 ? 16.897 36.796 60.490 1.00 21.08 ? 393 ALA A O 1 ATOM 2761 C CB . ALA A 1 400 ? 18.064 35.219 57.866 1.00 19.93 ? 393 ALA A CB 1 ATOM 2762 N N . VAL A 1 401 ? 17.746 38.206 58.944 1.00 20.28 ? 394 VAL A N 1 ATOM 2763 C CA . VAL A 1 401 ? 18.089 39.248 59.948 1.00 20.25 ? 394 VAL A CA 1 ATOM 2764 C C . VAL A 1 401 ? 16.808 39.895 60.491 1.00 20.74 ? 394 VAL A C 1 ATOM 2765 O O . VAL A 1 401 ? 16.670 40.094 61.714 1.00 19.84 ? 394 VAL A O 1 ATOM 2766 C CB . VAL A 1 401 ? 19.064 40.288 59.314 1.00 20.47 ? 394 VAL A CB 1 ATOM 2767 C CG1 . VAL A 1 401 ? 18.986 41.693 59.946 1.00 18.41 ? 394 VAL A CG1 1 ATOM 2768 C CG2 . VAL A 1 401 ? 20.510 39.704 59.313 1.00 19.57 ? 394 VAL A CG2 1 ATOM 2769 N N . VAL A 1 402 ? 15.863 40.185 59.587 1.00 20.54 ? 395 VAL A N 1 ATOM 2770 C CA . VAL A 1 402 ? 14.556 40.743 60.010 1.00 20.76 ? 395 VAL A CA 1 ATOM 2771 C C . VAL A 1 402 ? 13.897 39.747 60.973 1.00 21.40 ? 395 VAL A C 1 ATOM 2772 O O . VAL A 1 402 ? 13.437 40.143 62.030 1.00 21.28 ? 395 VAL A O 1 ATOM 2773 C CB . VAL A 1 402 ? 13.576 41.014 58.829 1.00 20.95 ? 395 VAL A CB 1 ATOM 2774 C CG1 . VAL A 1 402 ? 12.127 41.442 59.382 1.00 18.78 ? 395 VAL A CG1 1 ATOM 2775 C CG2 . VAL A 1 402 ? 14.125 42.172 57.916 1.00 19.99 ? 395 VAL A CG2 1 ATOM 2776 N N . HIS A 1 403 ? 13.900 38.464 60.605 1.00 20.31 ? 396 HIS A N 1 ATOM 2777 C CA . HIS A 1 403 ? 13.291 37.410 61.428 1.00 20.23 ? 396 HIS A CA 1 ATOM 2778 C C . HIS A 1 403 ? 13.861 37.402 62.857 1.00 21.22 ? 396 HIS A C 1 ATOM 2779 O O . HIS A 1 403 ? 13.104 37.390 63.829 1.00 21.92 ? 396 HIS A O 1 ATOM 2780 C CB . HIS A 1 403 ? 13.524 36.055 60.760 1.00 19.59 ? 396 HIS A CB 1 ATOM 2781 C CG . HIS A 1 403 ? 12.380 35.092 60.879 1.00 20.80 ? 396 HIS A CG 1 ATOM 2782 N ND1 . HIS A 1 403 ? 11.075 35.437 60.574 1.00 17.96 ? 396 HIS A ND1 1 ATOM 2783 C CD2 . HIS A 1 403 ? 12.363 33.767 61.184 1.00 21.94 ? 396 HIS A CD2 1 ATOM 2784 C CE1 . HIS A 1 403 ? 10.297 34.376 60.721 1.00 20.46 ? 396 HIS A CE1 1 ATOM 2785 N NE2 . HIS A 1 403 ? 11.052 33.346 61.084 1.00 22.40 ? 396 HIS A NE2 1 ATOM 2786 N N . GLU A 1 404 ? 15.184 37.454 62.991 1.00 21.24 ? 397 GLU A N 1 ATOM 2787 C CA . GLU A 1 404 ? 15.833 37.542 64.306 1.00 22.02 ? 397 GLU A CA 1 ATOM 2788 C C . GLU A 1 404 ? 15.510 38.850 65.071 1.00 21.97 ? 397 GLU A C 1 ATOM 2789 O O . GLU A 1 404 ? 15.403 38.847 66.303 1.00 22.52 ? 397 GLU A O 1 ATOM 2790 C CB . GLU A 1 404 ? 17.355 37.344 64.134 1.00 22.56 ? 397 GLU A CB 1 ATOM 2791 C CG . GLU A 1 404 ? 18.181 37.299 65.435 1.00 21.69 ? 397 GLU A CG 1 ATOM 2792 C CD . GLU A 1 404 ? 17.773 36.224 66.439 1.00 25.12 ? 397 GLU A CD 1 ATOM 2793 O OE1 . GLU A 1 404 ? 16.788 35.463 66.214 1.00 24.14 ? 397 GLU A OE1 1 ATOM 2794 O OE2 . GLU A 1 404 ? 18.470 36.144 67.486 1.00 26.80 ? 397 GLU A OE2 1 ATOM 2795 N N . ILE A 1 405 ? 15.360 39.958 64.347 1.00 20.83 ? 398 ILE A N 1 ATOM 2796 C CA . ILE A 1 405 ? 14.997 41.225 64.962 1.00 20.46 ? 398 ILE A CA 1 ATOM 2797 C C . ILE A 1 405 ? 13.590 41.137 65.538 1.00 21.11 ? 398 ILE A C 1 ATOM 2798 O O . ILE A 1 405 ? 13.374 41.497 66.704 1.00 19.97 ? 398 ILE A O 1 ATOM 2799 C CB . ILE A 1 405 ? 15.151 42.402 63.931 1.00 20.26 ? 398 ILE A CB 1 ATOM 2800 C CG1 . ILE A 1 405 ? 16.671 42.692 63.724 1.00 19.08 ? 398 ILE A CG1 1 ATOM 2801 C CG2 . ILE A 1 405 ? 14.394 43.671 64.397 1.00 16.36 ? 398 ILE A CG2 1 ATOM 2802 C CD1 . ILE A 1 405 ? 16.994 43.599 62.484 1.00 15.61 ? 398 ILE A CD1 1 ATOM 2803 N N . VAL A 1 406 ? 12.651 40.614 64.746 1.00 21.28 ? 399 VAL A N 1 ATOM 2804 C CA . VAL A 1 406 ? 11.262 40.348 65.251 1.00 22.41 ? 399 VAL A CA 1 ATOM 2805 C C . VAL A 1 406 ? 11.312 39.469 66.480 1.00 23.23 ? 399 VAL A C 1 ATOM 2806 O O . VAL A 1 406 ? 10.656 39.786 67.509 1.00 23.94 ? 399 VAL A O 1 ATOM 2807 C CB . VAL A 1 406 ? 10.305 39.695 64.166 1.00 21.53 ? 399 VAL A CB 1 ATOM 2808 C CG1 . VAL A 1 406 ? 8.949 39.307 64.778 1.00 20.52 ? 399 VAL A CG1 1 ATOM 2809 C CG2 . VAL A 1 406 ? 10.095 40.644 62.972 1.00 20.72 ? 399 VAL A CG2 1 ATOM 2810 N N . ARG A 1 407 ? 12.102 38.385 66.420 1.00 24.14 ? 400 ARG A N 1 ATOM 2811 C CA . ARG A 1 407 ? 12.173 37.478 67.559 1.00 25.06 ? 400 ARG A CA 1 ATOM 2812 C C . ARG A 1 407 ? 12.666 38.223 68.803 1.00 26.72 ? 400 ARG A C 1 ATOM 2813 O O . ARG A 1 407 ? 12.117 38.038 69.911 1.00 27.90 ? 400 ARG A O 1 ATOM 2814 C CB . ARG A 1 407 ? 13.066 36.242 67.281 1.00 25.10 ? 400 ARG A CB 1 ATOM 2815 C CG . ARG A 1 407 ? 12.898 35.137 68.324 1.00 24.96 ? 400 ARG A CG 1 ATOM 2816 C CD . ARG A 1 407 ? 14.103 34.091 68.239 1.00 25.77 ? 400 ARG A CD 1 ATOM 2817 N NE . ARG A 1 407 ? 15.377 34.756 68.515 1.00 26.73 ? 400 ARG A NE 1 ATOM 2818 C CZ . ARG A 1 407 ? 15.851 35.051 69.735 1.00 29.20 ? 400 ARG A CZ 1 ATOM 2819 N NH1 . ARG A 1 407 ? 17.011 35.676 69.848 1.00 27.49 ? 400 ARG A NH1 1 ATOM 2820 N NH2 . ARG A 1 407 ? 15.173 34.726 70.843 1.00 28.73 ? 400 ARG A NH2 1 ATOM 2821 N N . SER A 1 408 ? 13.669 39.083 68.628 1.00 26.99 ? 401 SER A N 1 ATOM 2822 C CA . SER A 1 408 ? 14.247 39.798 69.758 1.00 27.82 ? 401 SER A CA 1 ATOM 2823 C C . SER A 1 408 ? 13.262 40.801 70.359 1.00 27.61 ? 401 SER A C 1 ATOM 2824 O O . SER A 1 408 ? 13.097 40.848 71.599 1.00 27.89 ? 401 SER A O 1 ATOM 2825 C CB . SER A 1 408 ? 15.552 40.505 69.368 1.00 28.42 ? 401 SER A CB 1 ATOM 2826 O OG . SER A 1 408 ? 16.055 41.241 70.496 1.00 29.85 ? 401 SER A OG 1 ATOM 2827 N N . PHE A 1 409 ? 12.636 41.614 69.502 1.00 26.08 ? 402 PHE A N 1 ATOM 2828 C CA . PHE A 1 409 ? 11.602 42.536 69.974 1.00 26.77 ? 402 PHE A CA 1 ATOM 2829 C C . PHE A 1 409 ? 10.484 41.776 70.704 1.00 27.54 ? 402 PHE A C 1 ATOM 2830 O O . PHE A 1 409 ? 9.986 42.251 71.729 1.00 27.11 ? 402 PHE A O 1 ATOM 2831 C CB . PHE A 1 409 ? 11.000 43.384 68.848 1.00 25.40 ? 402 PHE A CB 1 ATOM 2832 C CG . PHE A 1 409 ? 11.805 44.605 68.482 1.00 24.98 ? 402 PHE A CG 1 ATOM 2833 C CD1 . PHE A 1 409 ? 11.980 45.653 69.395 1.00 24.35 ? 402 PHE A CD1 1 ATOM 2834 C CD2 . PHE A 1 409 ? 12.348 44.731 67.186 1.00 22.67 ? 402 PHE A CD2 1 ATOM 2835 C CE1 . PHE A 1 409 ? 12.707 46.806 69.023 1.00 24.44 ? 402 PHE A CE1 1 ATOM 2836 C CE2 . PHE A 1 409 ? 13.065 45.897 66.788 1.00 21.11 ? 402 PHE A CE2 1 ATOM 2837 C CZ . PHE A 1 409 ? 13.231 46.925 67.701 1.00 23.17 ? 402 PHE A CZ 1 ATOM 2838 N N . GLY A 1 410 ? 10.113 40.597 70.192 1.00 27.74 ? 403 GLY A N 1 ATOM 2839 C CA . GLY A 1 410 ? 9.068 39.780 70.808 1.00 28.65 ? 403 GLY A CA 1 ATOM 2840 C C . GLY A 1 410 ? 9.437 39.211 72.179 1.00 30.19 ? 403 GLY A C 1 ATOM 2841 O O . GLY A 1 410 ? 8.570 39.087 73.050 1.00 30.89 ? 403 GLY A O 1 ATOM 2842 N N . THR A 1 411 ? 10.709 38.867 72.388 1.00 30.22 ? 404 THR A N 1 ATOM 2843 C CA . THR A 1 411 ? 11.158 38.373 73.704 1.00 31.09 ? 404 THR A CA 1 ATOM 2844 C C . THR A 1 411 ? 10.916 39.520 74.713 1.00 31.67 ? 404 THR A C 1 ATOM 2845 O O . THR A 1 411 ? 10.386 39.287 75.792 1.00 31.71 ? 404 THR A O 1 ATOM 2846 C CB . THR A 1 411 ? 12.639 37.930 73.695 1.00 30.74 ? 404 THR A CB 1 ATOM 2847 O OG1 A THR A 1 411 ? 12.872 37.008 72.611 0.50 30.36 ? 404 THR A OG1 1 ATOM 2848 O OG1 B THR A 1 411 ? 13.482 39.070 73.510 0.50 30.69 ? 404 THR A OG1 1 ATOM 2849 C CG2 A THR A 1 411 ? 13.064 37.307 75.017 0.50 30.60 ? 404 THR A CG2 1 ATOM 2850 C CG2 B THR A 1 411 ? 12.915 36.894 72.588 0.50 30.58 ? 404 THR A CG2 1 ATOM 2851 N N . LEU A 1 412 ? 11.264 40.753 74.352 1.00 31.75 ? 405 LEU A N 1 ATOM 2852 C CA . LEU A 1 412 ? 11.080 41.887 75.267 1.00 32.79 ? 405 LEU A CA 1 ATOM 2853 C C . LEU A 1 412 ? 9.589 42.108 75.553 1.00 33.66 ? 405 LEU A C 1 ATOM 2854 O O . LEU A 1 412 ? 9.174 42.319 76.709 1.00 32.83 ? 405 LEU A O 1 ATOM 2855 C CB . LEU A 1 412 ? 11.688 43.181 74.677 1.00 32.46 ? 405 LEU A CB 1 ATOM 2856 C CG A LEU A 1 412 ? 13.189 43.232 74.416 0.50 31.96 ? 405 LEU A CG 1 ATOM 2857 C CG B LEU A 1 412 ? 13.151 43.488 75.022 0.50 32.32 ? 405 LEU A CG 1 ATOM 2858 C CD1 A LEU A 1 412 ? 13.551 44.519 73.697 0.50 31.03 ? 405 LEU A CD1 1 ATOM 2859 C CD1 B LEU A 1 412 ? 14.147 42.464 74.419 0.50 30.60 ? 405 LEU A CD1 1 ATOM 2860 C CD2 A LEU A 1 412 ? 13.940 43.115 75.725 0.50 31.22 ? 405 LEU A CD2 1 ATOM 2861 C CD2 B LEU A 1 412 ? 13.486 44.901 74.567 0.50 31.49 ? 405 LEU A CD2 1 ATOM 2862 N N . LYS A 1 413 ? 8.804 42.070 74.479 1.00 33.88 ? 406 LYS A N 1 ATOM 2863 C CA . LYS A 1 413 ? 7.367 42.184 74.556 1.00 35.04 ? 406 LYS A CA 1 ATOM 2864 C C . LYS A 1 413 ? 6.755 41.113 75.488 1.00 35.54 ? 406 LYS A C 1 ATOM 2865 O O . LYS A 1 413 ? 5.848 41.430 76.247 1.00 34.15 ? 406 LYS A O 1 ATOM 2866 C CB . LYS A 1 413 ? 6.786 42.058 73.165 1.00 35.28 ? 406 LYS A CB 1 ATOM 2867 C CG . LYS A 1 413 ? 5.413 42.634 73.014 1.00 39.65 ? 406 LYS A CG 1 ATOM 2868 C CD . LYS A 1 413 ? 4.367 41.571 72.975 1.00 43.47 ? 406 LYS A CD 1 ATOM 2869 C CE . LYS A 1 413 ? 3.134 42.069 72.253 1.00 44.40 ? 406 LYS A CE 1 ATOM 2870 N NZ . LYS A 1 413 ? 2.163 40.948 72.306 1.00 47.87 ? 406 LYS A NZ 1 ATOM 2871 N N . LYS A 1 414 ? 7.228 39.864 75.418 1.00 36.10 ? 407 LYS A N 1 ATOM 2872 C CA . LYS A 1 414 ? 6.715 38.826 76.350 1.00 38.44 ? 407 LYS A CA 1 ATOM 2873 C C . LYS A 1 414 ? 7.029 39.099 77.808 1.00 39.30 ? 407 LYS A C 1 ATOM 2874 O O . LYS A 1 414 ? 6.322 38.603 78.688 1.00 40.86 ? 407 LYS A O 1 ATOM 2875 C CB . LYS A 1 414 ? 7.158 37.413 75.982 1.00 38.15 ? 407 LYS A CB 1 ATOM 2876 C CG . LYS A 1 414 ? 6.353 36.867 74.823 1.00 40.98 ? 407 LYS A CG 1 ATOM 2877 C CD . LYS A 1 414 ? 6.990 35.645 74.167 1.00 42.59 ? 407 LYS A CD 1 ATOM 2878 C CE . LYS A 1 414 ? 6.262 35.376 72.863 1.00 43.94 ? 407 LYS A CE 1 ATOM 2879 N NZ . LYS A 1 414 ? 6.596 34.016 72.393 1.00 43.82 ? 407 LYS A NZ 1 ATOM 2880 N N . GLU A 1 415 ? 8.078 39.879 78.068 1.00 40.17 ? 408 GLU A N 1 ATOM 2881 C CA . GLU A 1 415 ? 8.425 40.305 79.442 1.00 41.44 ? 408 GLU A CA 1 ATOM 2882 C C . GLU A 1 415 ? 7.732 41.616 79.866 1.00 40.51 ? 408 GLU A C 1 ATOM 2883 O O . GLU A 1 415 ? 8.037 42.169 80.931 1.00 41.19 ? 408 GLU A O 1 ATOM 2884 C CB . GLU A 1 415 ? 9.946 40.421 79.611 1.00 42.15 ? 408 GLU A CB 1 ATOM 2885 C CG . GLU A 1 415 ? 10.704 39.135 79.213 1.00 47.72 ? 408 GLU A CG 1 ATOM 2886 C CD . GLU A 1 415 ? 12.224 39.257 79.286 1.00 55.40 ? 408 GLU A CD 1 ATOM 2887 O OE1 . GLU A 1 415 ? 12.894 38.192 79.214 1.00 58.58 ? 408 GLU A OE1 1 ATOM 2888 O OE2 . GLU A 1 415 ? 12.754 40.396 79.401 1.00 57.76 ? 408 GLU A OE2 1 ATOM 2889 N N . GLY A 1 416 ? 6.810 42.113 79.044 1.00 38.78 ? 409 GLY A N 1 ATOM 2890 C CA . GLY A 1 416 ? 5.967 43.239 79.458 1.00 36.61 ? 409 GLY A CA 1 ATOM 2891 C C . GLY A 1 416 ? 6.373 44.552 78.819 1.00 35.47 ? 409 GLY A C 1 ATOM 2892 O O . GLY A 1 416 ? 5.737 45.567 79.057 1.00 34.98 ? 409 GLY A O 1 ATOM 2893 N N . TRP A 1 417 ? 7.420 44.547 77.985 1.00 33.34 ? 410 TRP A N 1 ATOM 2894 C CA . TRP A 1 417 ? 7.859 45.787 77.354 1.00 32.41 ? 410 TRP A CA 1 ATOM 2895 C C . TRP A 1 417 ? 7.033 46.080 76.090 1.00 31.33 ? 410 TRP A C 1 ATOM 2896 O O . TRP A 1 417 ? 6.560 45.158 75.404 1.00 31.67 ? 410 TRP A O 1 ATOM 2897 C CB . TRP A 1 417 ? 9.343 45.668 77.004 1.00 33.26 ? 410 TRP A CB 1 ATOM 2898 C CG . TRP A 1 417 ? 9.965 46.824 76.217 1.00 33.13 ? 410 TRP A CG 1 ATOM 2899 C CD1 . TRP A 1 417 ? 10.500 47.988 76.743 1.00 32.80 ? 410 TRP A CD1 1 ATOM 2900 C CD2 . TRP A 1 417 ? 10.120 46.918 74.788 1.00 32.14 ? 410 TRP A CD2 1 ATOM 2901 N NE1 . TRP A 1 417 ? 10.991 48.775 75.723 1.00 32.61 ? 410 TRP A NE1 1 ATOM 2902 C CE2 . TRP A 1 417 ? 10.774 48.149 74.519 1.00 31.95 ? 410 TRP A CE2 1 ATOM 2903 C CE3 . TRP A 1 417 ? 9.755 46.088 73.700 1.00 30.87 ? 410 TRP A CE3 1 ATOM 2904 C CZ2 . TRP A 1 417 ? 11.080 48.566 73.210 1.00 28.01 ? 410 TRP A CZ2 1 ATOM 2905 C CZ3 . TRP A 1 417 ? 10.079 46.481 72.428 1.00 28.75 ? 410 TRP A CZ3 1 ATOM 2906 C CH2 . TRP A 1 417 ? 10.721 47.738 72.186 1.00 28.90 ? 410 TRP A CH2 1 ATOM 2907 N N . ARG A 1 418 ? 6.877 47.348 75.775 1.00 29.10 ? 411 ARG A N 1 ATOM 2908 C CA . ARG A 1 418 ? 6.389 47.770 74.445 1.00 28.08 ? 411 ARG A CA 1 ATOM 2909 C C . ARG A 1 418 ? 7.211 48.974 74.032 1.00 26.32 ? 411 ARG A C 1 ATOM 2910 O O . ARG A 1 418 ? 7.588 49.778 74.903 1.00 26.59 ? 411 ARG A O 1 ATOM 2911 C CB . ARG A 1 418 ? 4.931 48.240 74.505 1.00 28.61 ? 411 ARG A CB 1 ATOM 2912 C CG . ARG A 1 418 ? 3.910 47.139 74.496 1.00 29.80 ? 411 ARG A CG 1 ATOM 2913 C CD . ARG A 1 418 ? 2.427 47.645 74.319 1.00 28.96 ? 411 ARG A CD 1 ATOM 2914 N NE . ARG A 1 418 ? 1.598 46.435 74.290 1.00 26.71 ? 411 ARG A NE 1 ATOM 2915 C CZ . ARG A 1 418 ? 1.438 45.671 73.204 1.00 27.25 ? 411 ARG A CZ 1 ATOM 2916 N NH1 . ARG A 1 418 ? 1.996 46.030 72.032 1.00 23.67 ? 411 ARG A NH1 1 ATOM 2917 N NH2 . ARG A 1 418 ? 0.720 44.555 73.287 1.00 26.77 ? 411 ARG A NH2 1 ATOM 2918 N N . PRO A 1 419 ? 7.474 49.122 72.722 1.00 24.35 ? 412 PRO A N 1 ATOM 2919 C CA . PRO A 1 419 ? 8.119 50.336 72.250 1.00 23.52 ? 412 PRO A CA 1 ATOM 2920 C C . PRO A 1 419 ? 7.182 51.524 72.456 1.00 23.36 ? 412 PRO A C 1 ATOM 2921 O O . PRO A 1 419 ? 5.967 51.349 72.528 1.00 22.77 ? 412 PRO A O 1 ATOM 2922 C CB . PRO A 1 419 ? 8.317 50.066 70.737 1.00 23.24 ? 412 PRO A CB 1 ATOM 2923 C CG . PRO A 1 419 ? 7.212 49.107 70.388 1.00 22.98 ? 412 PRO A CG 1 ATOM 2924 C CD . PRO A 1 419 ? 7.080 48.230 71.604 1.00 23.73 ? 412 PRO A CD 1 ATOM 2925 N N . ARG A 1 420 ? 7.739 52.728 72.544 1.00 22.77 ? 413 ARG A N 1 ATOM 2926 C CA . ARG A 1 420 ? 6.920 53.924 72.678 1.00 22.17 ? 413 ARG A CA 1 ATOM 2927 C C . ARG A 1 420 ? 5.983 54.076 71.446 1.00 22.35 ? 413 ARG A C 1 ATOM 2928 O O . ARG A 1 420 ? 4.761 54.339 71.583 1.00 22.96 ? 413 ARG A O 1 ATOM 2929 C CB . ARG A 1 420 ? 7.831 55.144 72.763 1.00 21.41 ? 413 ARG A CB 1 ATOM 2930 C CG . ARG A 1 420 ? 7.083 56.498 72.865 1.00 23.30 ? 413 ARG A CG 1 ATOM 2931 C CD . ARG A 1 420 ? 8.050 57.680 72.704 1.00 23.29 ? 413 ARG A CD 1 ATOM 2932 N NE . ARG A 1 420 ? 7.288 58.927 72.633 1.00 24.54 ? 413 ARG A NE 1 ATOM 2933 C CZ . ARG A 1 420 ? 6.837 59.609 73.668 1.00 26.59 ? 413 ARG A CZ 1 ATOM 2934 N NH1 . ARG A 1 420 ? 7.102 59.206 74.917 1.00 23.85 ? 413 ARG A NH1 1 ATOM 2935 N NH2 . ARG A 1 420 ? 6.132 60.727 73.439 1.00 27.85 ? 413 ARG A NH2 1 ATOM 2936 N N . ARG A 1 421 ? 6.576 53.965 70.262 1.00 21.07 ? 414 ARG A N 1 ATOM 2937 C CA . ARG A 1 421 ? 5.839 54.053 68.955 1.00 20.68 ? 414 ARG A CA 1 ATOM 2938 C C . ARG A 1 421 ? 5.598 52.653 68.366 1.00 20.39 ? 414 ARG A C 1 ATOM 2939 O O . ARG A 1 421 ? 6.287 51.656 68.713 1.00 20.71 ? 414 ARG A O 1 ATOM 2940 C CB . ARG A 1 421 ? 6.632 54.880 67.944 1.00 19.22 ? 414 ARG A CB 1 ATOM 2941 C CG . ARG A 1 421 ? 7.071 56.269 68.479 1.00 19.73 ? 414 ARG A CG 1 ATOM 2942 C CD . ARG A 1 421 ? 7.806 57.198 67.447 1.00 19.90 ? 414 ARG A CD 1 ATOM 2943 N NE . ARG A 1 421 ? 8.040 58.446 68.165 1.00 22.43 ? 414 ARG A NE 1 ATOM 2944 C CZ . ARG A 1 421 ? 9.060 58.658 69.013 1.00 22.07 ? 414 ARG A CZ 1 ATOM 2945 N NH1 . ARG A 1 421 ? 10.060 57.765 69.119 1.00 21.45 ? 414 ARG A NH1 1 ATOM 2946 N NH2 . ARG A 1 421 ? 9.104 59.788 69.720 1.00 20.29 ? 414 ARG A NH2 1 ATOM 2947 N N . THR A 1 422 ? 4.623 52.562 67.476 1.00 20.11 ? 415 THR A N 1 ATOM 2948 C CA . THR A 1 422 ? 4.317 51.298 66.797 1.00 19.17 ? 415 THR A CA 1 ATOM 2949 C C . THR A 1 422 ? 5.448 50.928 65.847 1.00 19.29 ? 415 THR A C 1 ATOM 2950 O O . THR A 1 422 ? 5.988 51.795 65.141 1.00 19.21 ? 415 THR A O 1 ATOM 2951 C CB . THR A 1 422 ? 2.954 51.408 66.036 1.00 18.87 ? 415 THR A CB 1 ATOM 2952 O OG1 . THR A 1 422 ? 1.891 51.450 67.000 1.00 19.09 ? 415 THR A OG1 1 ATOM 2953 C CG2 . THR A 1 422 ? 2.726 50.198 65.103 1.00 16.48 ? 415 THR A CG2 1 ATOM 2954 N N . ILE A 1 423 ? 5.824 49.652 65.853 1.00 17.86 ? 416 ILE A N 1 ATOM 2955 C CA . ILE A 1 423 ? 6.753 49.169 64.879 1.00 18.53 ? 416 ILE A CA 1 ATOM 2956 C C . ILE A 1 423 ? 5.972 48.233 63.955 1.00 18.32 ? 416 ILE A C 1 ATOM 2957 O O . ILE A 1 423 ? 5.255 47.331 64.418 1.00 18.42 ? 416 ILE A O 1 ATOM 2958 C CB . ILE A 1 423 ? 7.924 48.376 65.517 1.00 18.78 ? 416 ILE A CB 1 ATOM 2959 C CG1 . ILE A 1 423 ? 8.651 49.218 66.595 1.00 18.34 ? 416 ILE A CG1 1 ATOM 2960 C CG2 . ILE A 1 423 ? 8.903 47.912 64.422 1.00 17.96 ? 416 ILE A CG2 1 ATOM 2961 C CD1 . ILE A 1 423 ? 9.715 48.390 67.373 1.00 18.24 ? 416 ILE A CD1 1 ATOM 2962 N N . LEU A 1 424 ? 6.092 48.481 62.658 1.00 18.09 ? 417 LEU A N 1 ATOM 2963 C CA . LEU A 1 424 ? 5.609 47.568 61.615 1.00 17.72 ? 417 LEU A CA 1 ATOM 2964 C C . LEU A 1 424 ? 6.755 46.796 60.979 1.00 17.52 ? 417 LEU A C 1 ATOM 2965 O O . LEU A 1 424 ? 7.822 47.366 60.668 1.00 17.55 ? 417 LEU A O 1 ATOM 2966 C CB . LEU A 1 424 ? 4.888 48.356 60.510 1.00 17.61 ? 417 LEU A CB 1 ATOM 2967 C CG . LEU A 1 424 ? 3.745 49.251 61.013 1.00 18.18 ? 417 LEU A CG 1 ATOM 2968 C CD1 . LEU A 1 424 ? 3.045 49.958 59.824 1.00 16.15 ? 417 LEU A CD1 1 ATOM 2969 C CD2 . LEU A 1 424 ? 2.694 48.411 61.853 1.00 15.80 ? 417 LEU A CD2 1 ATOM 2970 N N . PHE A 1 425 ? 6.520 45.501 60.746 1.00 16.59 ? 418 PHE A N 1 ATOM 2971 C CA . PHE A 1 425 ? 7.519 44.633 60.139 1.00 16.92 ? 418 PHE A CA 1 ATOM 2972 C C . PHE A 1 425 ? 6.919 44.120 58.851 1.00 18.07 ? 418 PHE A C 1 ATOM 2973 O O . PHE A 1 425 ? 5.725 43.751 58.834 1.00 18.59 ? 418 PHE A O 1 ATOM 2974 C CB . PHE A 1 425 ? 7.802 43.449 61.061 1.00 17.42 ? 418 PHE A CB 1 ATOM 2975 C CG . PHE A 1 425 ? 8.421 43.856 62.354 1.00 19.18 ? 418 PHE A CG 1 ATOM 2976 C CD1 . PHE A 1 425 ? 9.805 44.081 62.437 1.00 18.53 ? 418 PHE A CD1 1 ATOM 2977 C CD2 . PHE A 1 425 ? 7.621 44.053 63.497 1.00 19.02 ? 418 PHE A CD2 1 ATOM 2978 C CE1 . PHE A 1 425 ? 10.384 44.475 63.701 1.00 19.12 ? 418 PHE A CE1 1 ATOM 2979 C CE2 . PHE A 1 425 ? 8.182 44.448 64.719 1.00 20.13 ? 418 PHE A CE2 1 ATOM 2980 C CZ . PHE A 1 425 ? 9.567 44.633 64.826 1.00 19.00 ? 418 PHE A CZ 1 ATOM 2981 N N . ALA A 1 426 ? 7.704 44.133 57.756 1.00 18.15 ? 419 ALA A N 1 ATOM 2982 C CA . ALA A 1 426 ? 7.161 43.709 56.440 1.00 17.86 ? 419 ALA A CA 1 ATOM 2983 C C . ALA A 1 426 ? 8.052 42.717 55.737 1.00 17.59 ? 419 ALA A C 1 ATOM 2984 O O . ALA A 1 426 ? 9.266 42.908 55.684 1.00 17.12 ? 419 ALA A O 1 ATOM 2985 C CB . ALA A 1 426 ? 6.930 44.924 55.548 1.00 16.74 ? 419 ALA A CB 1 ATOM 2986 N N . SER A 1 427 ? 7.423 41.654 55.216 1.00 17.51 ? 420 SER A N 1 ATOM 2987 C CA . SER A 1 427 ? 8.043 40.722 54.315 1.00 16.89 ? 420 SER A CA 1 ATOM 2988 C C . SER A 1 427 ? 7.374 41.004 52.959 1.00 17.53 ? 420 SER A C 1 ATOM 2989 O O . SER A 1 427 ? 6.231 40.580 52.752 1.00 17.52 ? 420 SER A O 1 ATOM 2990 C CB . SER A 1 427 ? 7.731 39.276 54.774 1.00 16.76 ? 420 SER A CB 1 ATOM 2991 O OG . SER A 1 427 ? 8.250 38.323 53.829 1.00 17.22 ? 420 SER A OG 1 ATOM 2992 N N . TRP A 1 428 ? 8.061 41.737 52.057 1.00 17.03 ? 421 TRP A N 1 ATOM 2993 C CA . TRP A 1 428 ? 7.473 42.188 50.798 1.00 16.56 ? 421 TRP A CA 1 ATOM 2994 C C . TRP A 1 428 ? 7.603 41.087 49.748 1.00 17.52 ? 421 TRP A C 1 ATOM 2995 O O . TRP A 1 428 ? 8.578 40.276 49.772 1.00 16.89 ? 421 TRP A O 1 ATOM 2996 C CB . TRP A 1 428 ? 8.234 43.395 50.236 1.00 15.89 ? 421 TRP A CB 1 ATOM 2997 C CG . TRP A 1 428 ? 8.318 44.617 51.155 1.00 16.05 ? 421 TRP A CG 1 ATOM 2998 C CD1 . TRP A 1 428 ? 9.463 45.305 51.503 1.00 15.69 ? 421 TRP A CD1 1 ATOM 2999 C CD2 . TRP A 1 428 ? 7.215 45.341 51.749 1.00 15.99 ? 421 TRP A CD2 1 ATOM 3000 N NE1 . TRP A 1 428 ? 9.144 46.398 52.285 1.00 16.22 ? 421 TRP A NE1 1 ATOM 3001 C CE2 . TRP A 1 428 ? 7.770 46.451 52.444 1.00 15.46 ? 421 TRP A CE2 1 ATOM 3002 C CE3 . TRP A 1 428 ? 5.801 45.181 51.729 1.00 15.81 ? 421 TRP A CE3 1 ATOM 3003 C CZ2 . TRP A 1 428 ? 6.973 47.382 53.136 1.00 14.86 ? 421 TRP A CZ2 1 ATOM 3004 C CZ3 . TRP A 1 428 ? 4.987 46.128 52.443 1.00 16.08 ? 421 TRP A CZ3 1 ATOM 3005 C CH2 . TRP A 1 428 ? 5.586 47.192 53.150 1.00 15.84 ? 421 TRP A CH2 1 ATOM 3006 N N . ASP A 1 429 ? 6.628 41.049 48.835 1.00 16.76 ? 422 ASP A N 1 ATOM 3007 C CA . ASP A 1 429 ? 6.663 40.086 47.738 1.00 16.92 ? 422 ASP A CA 1 ATOM 3008 C C . ASP A 1 429 ? 6.949 40.859 46.466 1.00 17.14 ? 422 ASP A C 1 ATOM 3009 O O . ASP A 1 429 ? 6.791 42.113 46.428 1.00 16.84 ? 422 ASP A O 1 ATOM 3010 C CB . ASP A 1 429 ? 5.305 39.386 47.623 1.00 17.53 ? 422 ASP A CB 1 ATOM 3011 C CG . ASP A 1 429 ? 5.375 38.024 46.889 1.00 18.61 ? 422 ASP A CG 1 ATOM 3012 O OD1 . ASP A 1 429 ? 6.442 37.681 46.293 1.00 19.73 ? 422 ASP A OD1 1 ATOM 3013 O OD2 . ASP A 1 429 ? 4.340 37.290 46.911 1.00 17.77 ? 422 ASP A OD2 1 ATOM 3014 N N . ALA A 1 430 ? 7.355 40.098 45.439 1.00 16.76 ? 423 ALA A N 1 ATOM 3015 C CA . ALA A 1 430 ? 7.564 40.592 44.060 1.00 17.09 ? 423 ALA A CA 1 ATOM 3016 C C . ALA A 1 430 ? 8.517 41.801 43.979 1.00 16.64 ? 423 ALA A C 1 ATOM 3017 O O . ALA A 1 430 ? 8.396 42.612 43.066 1.00 16.96 ? 423 ALA A O 1 ATOM 3018 C CB . ALA A 1 430 ? 6.191 40.933 43.435 1.00 15.80 ? 423 ALA A CB 1 ATOM 3019 N N . ALA A 1 431 ? 9.450 41.959 44.919 1.00 17.25 ? 424 ALA A N 1 ATOM 3020 C CA . ALA A 1 431 ? 10.441 43.043 44.735 1.00 16.24 ? 424 ALA A CA 1 ATOM 3021 C C . ALA A 1 431 ? 11.231 42.832 43.457 1.00 16.23 ? 424 ALA A C 1 ATOM 3022 O O . ALA A 1 431 ? 11.562 43.816 42.754 1.00 16.39 ? 424 ALA A O 1 ATOM 3023 C CB . ALA A 1 431 ? 11.381 43.171 45.879 1.00 16.02 ? 424 ALA A CB 1 ATOM 3024 N N . GLU A 1 432 ? 11.550 41.571 43.145 1.00 15.90 ? 425 GLU A N 1 ATOM 3025 C CA . GLU A 1 432 ? 12.391 41.307 41.980 1.00 16.56 ? 425 GLU A CA 1 ATOM 3026 C C . GLU A 1 432 ? 11.743 41.729 40.658 1.00 16.50 ? 425 GLU A C 1 ATOM 3027 O O . GLU A 1 432 ? 12.432 41.929 39.631 1.00 17.92 ? 425 GLU A O 1 ATOM 3028 C CB . GLU A 1 432 ? 12.827 39.820 41.903 1.00 15.45 ? 425 GLU A CB 1 ATOM 3029 C CG . GLU A 1 432 ? 13.798 39.354 43.069 1.00 16.91 ? 425 GLU A CG 1 ATOM 3030 C CD . GLU A 1 432 ? 15.180 40.096 43.200 1.00 16.04 ? 425 GLU A CD 1 ATOM 3031 O OE1 . GLU A 1 432 ? 15.515 41.107 42.591 1.00 19.09 ? 425 GLU A OE1 1 ATOM 3032 O OE2 . GLU A 1 432 ? 16.069 39.682 43.966 1.00 17.36 ? 425 GLU A OE2 1 ATOM 3033 N N . PHE A 1 433 ? 10.425 41.881 40.680 1.00 16.85 ? 426 PHE A N 1 ATOM 3034 C CA . PHE A 1 433 ? 9.664 42.223 39.486 1.00 15.78 ? 426 PHE A CA 1 ATOM 3035 C C . PHE A 1 433 ? 9.308 43.691 39.449 1.00 16.06 ? 426 PHE A C 1 ATOM 3036 O O . PHE A 1 433 ? 8.431 44.090 38.681 1.00 15.25 ? 426 PHE A O 1 ATOM 3037 C CB . PHE A 1 433 ? 8.382 41.380 39.431 1.00 16.75 ? 426 PHE A CB 1 ATOM 3038 C CG . PHE A 1 433 ? 8.647 39.919 39.062 1.00 17.10 ? 426 PHE A CG 1 ATOM 3039 C CD1 . PHE A 1 433 ? 8.526 39.493 37.747 1.00 14.79 ? 426 PHE A CD1 1 ATOM 3040 C CD2 . PHE A 1 433 ? 9.007 38.980 40.078 1.00 16.99 ? 426 PHE A CD2 1 ATOM 3041 C CE1 . PHE A 1 433 ? 8.784 38.078 37.379 1.00 15.02 ? 426 PHE A CE1 1 ATOM 3042 C CE2 . PHE A 1 433 ? 9.305 37.641 39.784 1.00 17.32 ? 426 PHE A CE2 1 ATOM 3043 C CZ . PHE A 1 433 ? 9.147 37.143 38.419 1.00 18.42 ? 426 PHE A CZ 1 ATOM 3044 N N . GLY A 1 434 ? 9.940 44.499 40.305 1.00 15.76 ? 427 GLY A N 1 ATOM 3045 C CA . GLY A 1 434 ? 9.755 45.969 40.193 1.00 15.51 ? 427 GLY A CA 1 ATOM 3046 C C . GLY A 1 434 ? 9.274 46.609 41.480 1.00 15.08 ? 427 GLY A C 1 ATOM 3047 O O . GLY A 1 434 ? 8.539 47.602 41.439 1.00 16.76 ? 427 GLY A O 1 ATOM 3048 N N . LEU A 1 435 ? 9.652 46.040 42.621 1.00 14.51 ? 428 LEU A N 1 ATOM 3049 C CA . LEU A 1 435 ? 9.271 46.594 43.947 1.00 13.92 ? 428 LEU A CA 1 ATOM 3050 C C . LEU A 1 435 ? 7.738 46.603 44.060 1.00 14.42 ? 428 LEU A C 1 ATOM 3051 O O . LEU A 1 435 ? 7.124 47.529 44.616 1.00 14.74 ? 428 LEU A O 1 ATOM 3052 C CB . LEU A 1 435 ? 9.863 48.023 44.204 1.00 13.82 ? 428 LEU A CB 1 ATOM 3053 C CG . LEU A 1 435 ? 11.278 48.218 43.629 1.00 13.42 ? 428 LEU A CG 1 ATOM 3054 C CD1 . LEU A 1 435 ? 11.699 49.703 43.762 1.00 14.42 ? 428 LEU A CD1 1 ATOM 3055 C CD2 . LEU A 1 435 ? 12.295 47.279 44.353 1.00 13.33 ? 428 LEU A CD2 1 ATOM 3056 N N . LEU A 1 436 ? 7.107 45.547 43.576 1.00 13.96 ? 429 LEU A N 1 ATOM 3057 C CA . LEU A 1 436 ? 5.649 45.635 43.399 1.00 14.03 ? 429 LEU A CA 1 ATOM 3058 C C . LEU A 1 436 ? 4.905 45.502 44.725 1.00 14.54 ? 429 LEU A C 1 ATOM 3059 O O . LEU A 1 436 ? 3.890 46.173 44.933 1.00 15.64 ? 429 LEU A O 1 ATOM 3060 C CB . LEU A 1 436 ? 5.155 44.543 42.412 1.00 12.36 ? 429 LEU A CB 1 ATOM 3061 C CG . LEU A 1 436 ? 5.858 44.553 41.041 1.00 13.66 ? 429 LEU A CG 1 ATOM 3062 C CD1 . LEU A 1 436 ? 5.303 43.477 40.186 1.00 13.13 ? 429 LEU A CD1 1 ATOM 3063 C CD2 . LEU A 1 436 ? 5.742 45.921 40.318 1.00 12.97 ? 429 LEU A CD2 1 ATOM 3064 N N . GLY A 1 437 ? 5.355 44.584 45.582 1.00 15.48 ? 430 GLY A N 1 ATOM 3065 C CA . GLY A 1 437 ? 4.640 44.330 46.862 1.00 15.75 ? 430 GLY A CA 1 ATOM 3066 C C . GLY A 1 437 ? 4.700 45.539 47.788 1.00 15.82 ? 430 GLY A C 1 ATOM 3067 O O . GLY A 1 437 ? 3.695 45.944 48.367 1.00 15.77 ? 430 GLY A O 1 ATOM 3068 N N . SER A 1 438 ? 5.872 46.124 47.971 1.00 15.45 ? 431 SER A N 1 ATOM 3069 C CA . SER A 1 438 ? 5.950 47.288 48.849 1.00 15.52 ? 431 SER A CA 1 ATOM 3070 C C . SER A 1 438 ? 5.155 48.449 48.253 1.00 14.97 ? 431 SER A C 1 ATOM 3071 O O . SER A 1 438 ? 4.470 49.177 48.981 1.00 14.33 ? 431 SER A O 1 ATOM 3072 C CB . SER A 1 438 ? 7.404 47.774 49.019 1.00 15.81 ? 431 SER A CB 1 ATOM 3073 O OG . SER A 1 438 ? 8.029 48.131 47.751 1.00 15.99 ? 431 SER A OG 1 ATOM 3074 N N . THR A 1 439 ? 5.293 48.659 46.938 1.00 14.48 ? 432 THR A N 1 ATOM 3075 C CA . THR A 1 439 ? 4.605 49.793 46.330 1.00 14.38 ? 432 THR A CA 1 ATOM 3076 C C . THR A 1 439 ? 3.071 49.664 46.387 1.00 14.31 ? 432 THR A C 1 ATOM 3077 O O . THR A 1 439 ? 2.408 50.658 46.697 1.00 15.30 ? 432 THR A O 1 ATOM 3078 C CB . THR A 1 439 ? 5.060 50.029 44.846 1.00 14.06 ? 432 THR A CB 1 ATOM 3079 O OG1 . THR A 1 439 ? 6.501 50.136 44.814 1.00 16.51 ? 432 THR A OG1 1 ATOM 3080 C CG2 . THR A 1 439 ? 4.503 51.335 44.311 1.00 11.61 ? 432 THR A CG2 1 ATOM 3081 N N . GLU A 1 440 ? 2.507 48.487 46.054 1.00 13.35 ? 433 GLU A N 1 ATOM 3082 C CA . GLU A 1 440 ? 1.029 48.319 46.139 1.00 14.86 ? 433 GLU A CA 1 ATOM 3083 C C . GLU A 1 440 ? 0.548 48.542 47.570 1.00 15.39 ? 433 GLU A C 1 ATOM 3084 O O . GLU A 1 440 ? -0.488 49.207 47.792 1.00 15.90 ? 433 GLU A O 1 ATOM 3085 C CB . GLU A 1 440 ? 0.554 46.925 45.618 1.00 14.85 ? 433 GLU A CB 1 ATOM 3086 C CG . GLU A 1 440 ? 0.831 46.698 44.068 1.00 15.47 ? 433 GLU A CG 1 ATOM 3087 C CD . GLU A 1 440 ? 0.245 47.829 43.240 1.00 15.68 ? 433 GLU A CD 1 ATOM 3088 O OE1 . GLU A 1 440 ? -0.980 48.117 43.342 1.00 16.40 ? 433 GLU A OE1 1 ATOM 3089 O OE2 . GLU A 1 440 ? 0.983 48.502 42.493 1.00 17.25 ? 433 GLU A OE2 1 ATOM 3090 N N . TRP A 1 441 ? 1.273 47.989 48.552 1.00 14.70 ? 434 TRP A N 1 ATOM 3091 C CA . TRP A 1 441 ? 0.859 48.173 49.946 1.00 15.05 ? 434 TRP A CA 1 ATOM 3092 C C . TRP A 1 441 ? 0.917 49.648 50.351 1.00 15.24 ? 434 TRP A C 1 ATOM 3093 O O . TRP A 1 441 ? 0.024 50.138 51.020 1.00 16.32 ? 434 TRP A O 1 ATOM 3094 C CB . TRP A 1 441 ? 1.744 47.327 50.873 1.00 15.53 ? 434 TRP A CB 1 ATOM 3095 C CG . TRP A 1 441 ? 1.312 47.370 52.315 1.00 15.95 ? 434 TRP A CG 1 ATOM 3096 C CD1 . TRP A 1 441 ? 0.324 46.600 52.919 1.00 16.44 ? 434 TRP A CD1 1 ATOM 3097 C CD2 . TRP A 1 441 ? 1.838 48.233 53.330 1.00 17.90 ? 434 TRP A CD2 1 ATOM 3098 N NE1 . TRP A 1 441 ? 0.225 46.946 54.263 1.00 17.76 ? 434 TRP A NE1 1 ATOM 3099 C CE2 . TRP A 1 441 ? 1.150 47.922 54.547 1.00 17.07 ? 434 TRP A CE2 1 ATOM 3100 C CE3 . TRP A 1 441 ? 2.866 49.214 53.343 1.00 16.60 ? 434 TRP A CE3 1 ATOM 3101 C CZ2 . TRP A 1 441 ? 1.439 48.580 55.782 1.00 16.83 ? 434 TRP A CZ2 1 ATOM 3102 C CZ3 . TRP A 1 441 ? 3.163 49.871 54.566 1.00 18.49 ? 434 TRP A CZ3 1 ATOM 3103 C CH2 . TRP A 1 441 ? 2.417 49.564 55.766 1.00 16.63 ? 434 TRP A CH2 1 ATOM 3104 N N . ALA A 1 442 ? 1.972 50.354 49.941 1.00 15.00 ? 435 ALA A N 1 ATOM 3105 C CA . ALA A 1 442 ? 2.072 51.774 50.270 1.00 15.54 ? 435 ALA A CA 1 ATOM 3106 C C . ALA A 1 442 ? 0.990 52.583 49.525 1.00 15.76 ? 435 ALA A C 1 ATOM 3107 O O . ALA A 1 442 ? 0.458 53.549 50.076 1.00 15.23 ? 435 ALA A O 1 ATOM 3108 C CB . ALA A 1 442 ? 3.499 52.324 49.925 1.00 14.35 ? 435 ALA A CB 1 ATOM 3109 N N . GLU A 1 443 ? 0.657 52.186 48.283 1.00 15.13 ? 436 GLU A N 1 ATOM 3110 C CA . GLU A 1 443 ? -0.465 52.861 47.560 1.00 15.37 ? 436 GLU A CA 1 ATOM 3111 C C . GLU A 1 443 ? -1.784 52.635 48.291 1.00 15.87 ? 436 GLU A C 1 ATOM 3112 O O . GLU A 1 443 ? -2.648 53.542 48.410 1.00 15.86 ? 436 GLU A O 1 ATOM 3113 C CB . GLU A 1 443 ? -0.612 52.357 46.096 1.00 14.48 ? 436 GLU A CB 1 ATOM 3114 C CG . GLU A 1 443 ? 0.537 52.936 45.208 1.00 16.03 ? 436 GLU A CG 1 ATOM 3115 C CD . GLU A 1 443 ? 0.387 52.563 43.724 1.00 15.91 ? 436 GLU A CD 1 ATOM 3116 O OE1 . GLU A 1 443 ? 0.759 53.392 42.844 1.00 16.43 ? 436 GLU A OE1 1 ATOM 3117 O OE2 . GLU A 1 443 ? -0.107 51.433 43.456 1.00 16.10 ? 436 GLU A OE2 1 ATOM 3118 N N . GLU A 1 444 ? -1.946 51.423 48.806 1.00 15.15 ? 437 GLU A N 1 ATOM 3119 C CA . GLU A 1 444 ? -3.163 51.151 49.570 1.00 16.21 ? 437 GLU A CA 1 ATOM 3120 C C . GLU A 1 444 ? -3.238 52.007 50.869 1.00 16.17 ? 437 GLU A C 1 ATOM 3121 O O . GLU A 1 444 ? -4.305 52.534 51.256 1.00 15.82 ? 437 GLU A O 1 ATOM 3122 C CB . GLU A 1 444 ? -3.192 49.652 49.927 1.00 16.63 ? 437 GLU A CB 1 ATOM 3123 C CG . GLU A 1 444 ? -4.518 49.213 50.641 1.00 20.55 ? 437 GLU A CG 1 ATOM 3124 C CD . GLU A 1 444 ? -4.740 47.704 50.450 1.00 28.09 ? 437 GLU A CD 1 ATOM 3125 O OE1 . GLU A 1 444 ? -5.637 47.276 49.717 1.00 36.76 ? 437 GLU A OE1 1 ATOM 3126 O OE2 . GLU A 1 444 ? -3.954 46.931 50.934 1.00 27.77 ? 437 GLU A OE2 1 ATOM 3127 N N . ASN A 1 445 ? -2.100 52.131 51.548 1.00 16.07 ? 438 ASN A N 1 ATOM 3128 C CA . ASN A 1 445 ? -2.059 52.716 52.905 1.00 15.78 ? 438 ASN A CA 1 ATOM 3129 C C . ASN A 1 445 ? -1.450 54.103 52.918 1.00 15.50 ? 438 ASN A C 1 ATOM 3130 O O . ASN A 1 445 ? -1.085 54.600 53.992 1.00 14.80 ? 438 ASN A O 1 ATOM 3131 C CB . ASN A 1 445 ? -1.295 51.743 53.843 1.00 16.10 ? 438 ASN A CB 1 ATOM 3132 C CG . ASN A 1 445 ? -2.062 50.475 54.023 1.00 16.41 ? 438 ASN A CG 1 ATOM 3133 O OD1 . ASN A 1 445 ? -3.102 50.517 54.646 1.00 18.79 ? 438 ASN A OD1 1 ATOM 3134 N ND2 . ASN A 1 445 ? -1.637 49.374 53.393 1.00 16.11 ? 438 ASN A ND2 1 ATOM 3135 N N . SER A 1 446 ? -1.409 54.760 51.742 1.00 14.48 ? 439 SER A N 1 ATOM 3136 C CA . SER A 1 446 ? -0.684 56.029 51.593 1.00 15.91 ? 439 SER A CA 1 ATOM 3137 C C . SER A 1 446 ? -1.153 57.097 52.596 1.00 16.32 ? 439 SER A C 1 ATOM 3138 O O . SER A 1 446 ? -0.303 57.874 53.084 1.00 16.91 ? 439 SER A O 1 ATOM 3139 C CB . SER A 1 446 ? -0.838 56.608 50.158 1.00 16.17 ? 439 SER A CB 1 ATOM 3140 O OG . SER A 1 446 ? -2.180 56.921 49.939 1.00 16.18 ? 439 SER A OG 1 ATOM 3141 N N . ARG A 1 447 ? -2.470 57.177 52.886 1.00 15.09 ? 440 ARG A N 1 ATOM 3142 C CA . ARG A 1 447 ? -2.934 58.211 53.837 1.00 15.56 ? 440 ARG A CA 1 ATOM 3143 C C . ARG A 1 447 ? -2.431 57.939 55.270 1.00 15.83 ? 440 ARG A C 1 ATOM 3144 O O . ARG A 1 447 ? -2.090 58.881 56.024 1.00 16.11 ? 440 ARG A O 1 ATOM 3145 C CB . ARG A 1 447 ? -4.467 58.328 53.817 1.00 15.17 ? 440 ARG A CB 1 ATOM 3146 C CG . ARG A 1 447 ? -4.962 58.821 52.397 1.00 16.90 ? 440 ARG A CG 1 ATOM 3147 C CD . ARG A 1 447 ? -6.295 58.186 51.974 1.00 19.28 ? 440 ARG A CD 1 ATOM 3148 N NE . ARG A 1 447 ? -6.682 58.749 50.660 1.00 18.86 ? 440 ARG A NE 1 ATOM 3149 C CZ . ARG A 1 447 ? -6.220 58.351 49.472 1.00 19.31 ? 440 ARG A CZ 1 ATOM 3150 N NH1 . ARG A 1 447 ? -5.372 57.315 49.370 1.00 21.25 ? 440 ARG A NH1 1 ATOM 3151 N NH2 . ARG A 1 447 ? -6.600 58.999 48.379 1.00 16.80 ? 440 ARG A NH2 1 ATOM 3152 N N . LEU A 1 448 ? -2.372 56.669 55.664 1.00 15.27 ? 441 LEU A N 1 ATOM 3153 C CA . LEU A 1 448 ? -1.862 56.350 57.015 1.00 15.87 ? 441 LEU A CA 1 ATOM 3154 C C . LEU A 1 448 ? -0.361 56.664 57.075 1.00 16.45 ? 441 LEU A C 1 ATOM 3155 O O . LEU A 1 448 ? 0.136 57.216 58.067 1.00 16.87 ? 441 LEU A O 1 ATOM 3156 C CB . LEU A 1 448 ? -2.068 54.869 57.335 1.00 15.26 ? 441 LEU A CB 1 ATOM 3157 C CG . LEU A 1 448 ? -3.496 54.318 57.186 1.00 16.40 ? 441 LEU A CG 1 ATOM 3158 C CD1 . LEU A 1 448 ? -3.542 52.797 57.715 1.00 18.39 ? 441 LEU A CD1 1 ATOM 3159 C CD2 . LEU A 1 448 ? -4.553 55.247 57.894 1.00 15.90 ? 441 LEU A CD2 1 ATOM 3160 N N . LEU A 1 449 ? 0.353 56.302 56.005 1.00 16.04 ? 442 LEU A N 1 ATOM 3161 C CA . LEU A 1 449 ? 1.823 56.411 55.973 1.00 17.58 ? 442 LEU A CA 1 ATOM 3162 C C . LEU A 1 449 ? 2.250 57.880 55.926 1.00 18.11 ? 442 LEU A C 1 ATOM 3163 O O . LEU A 1 449 ? 3.177 58.292 56.619 1.00 20.42 ? 442 LEU A O 1 ATOM 3164 C CB . LEU A 1 449 ? 2.358 55.614 54.761 1.00 17.45 ? 442 LEU A CB 1 ATOM 3165 C CG . LEU A 1 449 ? 2.194 54.093 54.791 1.00 18.61 ? 442 LEU A CG 1 ATOM 3166 C CD1 . LEU A 1 449 ? 2.608 53.455 53.415 1.00 17.56 ? 442 LEU A CD1 1 ATOM 3167 C CD2 . LEU A 1 449 ? 3.060 53.465 55.910 1.00 20.42 ? 442 LEU A CD2 1 ATOM 3168 N N . GLN A 1 450 ? 1.524 58.673 55.144 1.00 17.64 ? 443 GLN A N 1 ATOM 3169 C CA . GLN A 1 450 ? 1.772 60.120 54.971 1.00 19.32 ? 443 GLN A CA 1 ATOM 3170 C C . GLN A 1 450 ? 1.654 60.837 56.353 1.00 18.12 ? 443 GLN A C 1 ATOM 3171 O O . GLN A 1 450 ? 2.448 61.739 56.684 1.00 17.96 ? 443 GLN A O 1 ATOM 3172 C CB . GLN A 1 450 ? 0.606 60.676 54.093 1.00 18.71 ? 443 GLN A CB 1 ATOM 3173 C CG A GLN A 1 450 ? 1.069 61.542 53.101 0.50 19.19 ? 443 GLN A CG 1 ATOM 3174 C CG B GLN A 1 450 ? 0.306 62.164 54.201 0.50 18.41 ? 443 GLN A CG 1 ATOM 3175 C CD A GLN A 1 450 ? 0.199 61.472 51.930 0.50 16.23 ? 443 GLN A CD 1 ATOM 3176 C CD B GLN A 1 450 ? 1.276 63.066 53.383 0.50 18.33 ? 443 GLN A CD 1 ATOM 3177 O OE1 A GLN A 1 450 ? 0.675 61.152 50.875 0.50 16.01 ? 443 GLN A OE1 1 ATOM 3178 O OE1 B GLN A 1 450 ? 1.723 62.677 52.275 0.50 21.16 ? 443 GLN A OE1 1 ATOM 3179 N NE2 A GLN A 1 450 ? -1.097 61.753 52.099 0.50 15.99 ? 443 GLN A NE2 1 ATOM 3180 N NE2 B GLN A 1 450 ? 1.587 64.249 53.912 0.50 8.28 ? 443 GLN A NE2 1 ATOM 3181 N N . GLU A 1 451 ? 0.582 60.515 57.092 1.00 17.52 ? 444 GLU A N 1 ATOM 3182 C CA . GLU A 1 451 ? 0.300 61.233 58.334 1.00 16.72 ? 444 GLU A CA 1 ATOM 3183 C C . GLU A 1 451 ? 0.927 60.625 59.567 1.00 16.40 ? 444 GLU A C 1 ATOM 3184 O O . GLU A 1 451 ? 1.007 61.298 60.587 1.00 16.61 ? 444 GLU A O 1 ATOM 3185 C CB . GLU A 1 451 ? -1.213 61.510 58.539 1.00 17.35 ? 444 GLU A CB 1 ATOM 3186 C CG . GLU A 1 451 ? -1.900 62.015 57.242 1.00 18.07 ? 444 GLU A CG 1 ATOM 3187 C CD . GLU A 1 451 ? -1.308 63.355 56.724 1.00 20.23 ? 444 GLU A CD 1 ATOM 3188 O OE1 . GLU A 1 451 ? -0.339 63.888 57.335 1.00 18.68 ? 444 GLU A OE1 1 ATOM 3189 O OE2 . GLU A 1 451 ? -1.816 63.865 55.691 1.00 22.93 ? 444 GLU A OE2 1 ATOM 3190 N N . ARG A 1 452 ? 1.375 59.369 59.485 1.00 15.75 ? 445 ARG A N 1 ATOM 3191 C CA . ARG A 1 452 ? 1.861 58.684 60.701 1.00 15.82 ? 445 ARG A CA 1 ATOM 3192 C C . ARG A 1 452 ? 3.275 58.082 60.544 1.00 16.44 ? 445 ARG A C 1 ATOM 3193 O O . ARG A 1 452 ? 3.804 57.552 61.509 1.00 16.87 ? 445 ARG A O 1 ATOM 3194 C CB . ARG A 1 452 ? 0.913 57.532 61.059 1.00 15.97 ? 445 ARG A CB 1 ATOM 3195 C CG . ARG A 1 452 ? -0.578 58.008 61.320 1.00 15.92 ? 445 ARG A CG 1 ATOM 3196 C CD . ARG A 1 452 ? -1.523 56.805 61.523 1.00 16.32 ? 445 ARG A CD 1 ATOM 3197 N NE . ARG A 1 452 ? -2.912 57.260 61.479 1.00 16.32 ? 445 ARG A NE 1 ATOM 3198 C CZ . ARG A 1 452 ? -3.980 56.467 61.461 1.00 17.71 ? 445 ARG A CZ 1 ATOM 3199 N NH1 . ARG A 1 452 ? -3.833 55.125 61.503 1.00 16.84 ? 445 ARG A NH1 1 ATOM 3200 N NH2 . ARG A 1 452 ? -5.208 57.030 61.399 1.00 17.40 ? 445 ARG A NH2 1 ATOM 3201 N N . GLY A 1 453 ? 3.869 58.135 59.339 1.00 16.85 ? 446 GLY A N 1 ATOM 3202 C CA . GLY A 1 453 ? 5.099 57.351 59.076 1.00 17.07 ? 446 GLY A CA 1 ATOM 3203 C C . GLY A 1 453 ? 6.318 58.134 59.588 1.00 18.16 ? 446 GLY A C 1 ATOM 3204 O O . GLY A 1 453 ? 6.658 59.212 59.084 1.00 18.74 ? 446 GLY A O 1 ATOM 3205 N N . VAL A 1 454 ? 6.966 57.598 60.605 1.00 17.75 ? 447 VAL A N 1 ATOM 3206 C CA . VAL A 1 454 ? 8.186 58.182 61.143 1.00 18.53 ? 447 VAL A CA 1 ATOM 3207 C C . VAL A 1 454 ? 9.403 57.878 60.268 1.00 17.94 ? 447 VAL A C 1 ATOM 3208 O O . VAL A 1 454 ? 10.130 58.806 59.875 1.00 17.26 ? 447 VAL A O 1 ATOM 3209 C CB . VAL A 1 454 ? 8.420 57.704 62.603 1.00 19.15 ? 447 VAL A CB 1 ATOM 3210 C CG1 . VAL A 1 454 ? 9.812 58.138 63.135 1.00 17.83 ? 447 VAL A CG1 1 ATOM 3211 C CG2 . VAL A 1 454 ? 7.306 58.322 63.455 1.00 21.85 ? 447 VAL A CG2 1 ATOM 3212 N N . ALA A 1 455 ? 9.599 56.588 59.928 1.00 17.36 ? 448 ALA A N 1 ATOM 3213 C CA . ALA A 1 455 ? 10.808 56.172 59.289 1.00 15.69 ? 448 ALA A CA 1 ATOM 3214 C C . ALA A 1 455 ? 10.585 54.821 58.682 1.00 16.78 ? 448 ALA A C 1 ATOM 3215 O O . ALA A 1 455 ? 9.782 54.010 59.192 1.00 17.28 ? 448 ALA A O 1 ATOM 3216 C CB . ALA A 1 455 ? 11.974 56.101 60.316 1.00 16.45 ? 448 ALA A CB 1 ATOM 3217 N N . TYR A 1 456 ? 11.329 54.570 57.601 1.00 15.87 ? 449 TYR A N 1 ATOM 3218 C CA . TYR A 1 456 ? 11.364 53.253 56.969 1.00 15.65 ? 449 TYR A CA 1 ATOM 3219 C C . TYR A 1 456 ? 12.831 52.777 56.968 1.00 16.43 ? 449 TYR A C 1 ATOM 3220 O O . TYR A 1 456 ? 13.726 53.490 56.445 1.00 16.86 ? 449 TYR A O 1 ATOM 3221 C CB . TYR A 1 456 ? 10.814 53.320 55.542 1.00 14.92 ? 449 TYR A CB 1 ATOM 3222 C CG . TYR A 1 456 ? 10.916 51.983 54.838 1.00 15.81 ? 449 TYR A CG 1 ATOM 3223 C CD1 . TYR A 1 456 ? 9.911 50.996 55.007 1.00 15.77 ? 449 TYR A CD1 1 ATOM 3224 C CD2 . TYR A 1 456 ? 12.007 51.680 54.059 1.00 15.34 ? 449 TYR A CD2 1 ATOM 3225 C CE1 . TYR A 1 456 ? 10.015 49.750 54.383 1.00 16.11 ? 449 TYR A CE1 1 ATOM 3226 C CE2 . TYR A 1 456 ? 12.133 50.413 53.416 1.00 15.58 ? 449 TYR A CE2 1 ATOM 3227 C CZ . TYR A 1 456 ? 11.138 49.463 53.591 1.00 16.48 ? 449 TYR A CZ 1 ATOM 3228 O OH . TYR A 1 456 ? 11.245 48.219 52.961 1.00 18.20 ? 449 TYR A OH 1 ATOM 3229 N N . ILE A 1 457 ? 13.089 51.607 57.563 1.00 15.68 ? 450 ILE A N 1 ATOM 3230 C CA . ILE A 1 457 ? 14.419 50.962 57.488 1.00 16.30 ? 450 ILE A CA 1 ATOM 3231 C C . ILE A 1 457 ? 14.302 49.749 56.553 1.00 17.60 ? 450 ILE A C 1 ATOM 3232 O O . ILE A 1 457 ? 13.459 48.862 56.801 1.00 18.45 ? 450 ILE A O 1 ATOM 3233 C CB . ILE A 1 457 ? 14.946 50.506 58.881 1.00 16.14 ? 450 ILE A CB 1 ATOM 3234 C CG1 . ILE A 1 457 ? 15.058 51.721 59.868 1.00 15.70 ? 450 ILE A CG1 1 ATOM 3235 C CG2 . ILE A 1 457 ? 16.356 49.774 58.754 1.00 15.57 ? 450 ILE A CG2 1 ATOM 3236 C CD1 . ILE A 1 457 ? 15.928 52.894 59.299 1.00 16.05 ? 450 ILE A CD1 1 ATOM 3237 N N . ASN A 1 458 ? 15.103 49.716 55.475 1.00 16.91 ? 451 ASN A N 1 ATOM 3238 C CA . ASN A 1 458 ? 15.049 48.597 54.543 1.00 17.11 ? 451 ASN A CA 1 ATOM 3239 C C . ASN A 1 458 ? 15.844 47.407 55.073 1.00 18.54 ? 451 ASN A C 1 ATOM 3240 O O . ASN A 1 458 ? 16.724 47.559 55.953 1.00 18.98 ? 451 ASN A O 1 ATOM 3241 C CB . ASN A 1 458 ? 15.629 49.016 53.155 1.00 16.51 ? 451 ASN A CB 1 ATOM 3242 C CG . ASN A 1 458 ? 15.053 48.190 51.986 1.00 16.86 ? 451 ASN A CG 1 ATOM 3243 O OD1 . ASN A 1 458 ? 13.846 48.061 51.845 1.00 19.05 ? 451 ASN A OD1 1 ATOM 3244 N ND2 . ASN A 1 458 ? 15.926 47.636 51.149 1.00 17.40 ? 451 ASN A ND2 1 ATOM 3245 N N . ALA A 1 459 ? 15.599 46.221 54.509 1.00 18.48 ? 452 ALA A N 1 ATOM 3246 C CA . ALA A 1 459 ? 16.352 45.037 54.960 1.00 18.43 ? 452 ALA A CA 1 ATOM 3247 C C . ALA A 1 459 ? 16.419 44.018 53.841 1.00 18.99 ? 452 ALA A C 1 ATOM 3248 O O . ALA A 1 459 ? 15.944 42.863 53.981 1.00 19.52 ? 452 ALA A O 1 ATOM 3249 C CB . ALA A 1 459 ? 15.698 44.416 56.226 1.00 17.31 ? 452 ALA A CB 1 ATOM 3250 N N . ASP A 1 460 ? 17.013 44.417 52.725 1.00 18.84 ? 453 ASP A N 1 ATOM 3251 C CA . ASP A 1 460 ? 17.364 43.423 51.707 1.00 19.13 ? 453 ASP A CA 1 ATOM 3252 C C . ASP A 1 460 ? 18.736 42.832 52.119 1.00 19.16 ? 453 ASP A C 1 ATOM 3253 O O . ASP A 1 460 ? 19.083 42.842 53.327 1.00 19.40 ? 453 ASP A O 1 ATOM 3254 C CB . ASP A 1 460 ? 17.340 44.052 50.284 1.00 19.11 ? 453 ASP A CB 1 ATOM 3255 C CG . ASP A 1 460 ? 17.203 43.025 49.175 1.00 20.68 ? 453 ASP A CG 1 ATOM 3256 O OD1 . ASP A 1 460 ? 17.208 41.816 49.512 1.00 22.63 ? 453 ASP A OD1 1 ATOM 3257 O OD2 . ASP A 1 460 ? 17.119 43.431 47.956 1.00 20.66 ? 453 ASP A OD2 1 ATOM 3258 N N . SER A 1 461 ? 19.496 42.352 51.140 1.00 18.73 ? 454 SER A N 1 ATOM 3259 C CA A SER A 1 461 ? 20.745 41.601 51.380 0.70 18.69 ? 454 SER A CA 1 ATOM 3260 C CA B SER A 1 461 ? 20.715 41.584 51.407 0.30 19.53 ? 454 SER A CA 1 ATOM 3261 C C . SER A 1 461 ? 21.592 42.208 52.501 1.00 19.70 ? 454 SER A C 1 ATOM 3262 O O . SER A 1 461 ? 21.909 43.413 52.477 1.00 19.59 ? 454 SER A O 1 ATOM 3263 C CB A SER A 1 461 ? 21.554 41.464 50.105 0.70 17.62 ? 454 SER A CB 1 ATOM 3264 C CB B SER A 1 461 ? 21.490 41.305 50.120 0.30 19.27 ? 454 SER A CB 1 ATOM 3265 O OG A SER A 1 461 ? 20.741 41.108 49.016 0.70 13.08 ? 454 SER A OG 1 ATOM 3266 O OG B SER A 1 461 ? 22.139 42.462 49.632 0.30 19.98 ? 454 SER A OG 1 ATOM 3267 N N . SER A 1 462 ? 21.937 41.389 53.501 1.00 20.48 ? 455 SER A N 1 ATOM 3268 C CA . SER A 1 462 ? 22.735 41.892 54.647 1.00 21.56 ? 455 SER A CA 1 ATOM 3269 C C . SER A 1 462 ? 24.224 42.012 54.325 1.00 21.36 ? 455 SER A C 1 ATOM 3270 O O . SER A 1 462 ? 24.971 42.716 54.999 1.00 20.33 ? 455 SER A O 1 ATOM 3271 C CB . SER A 1 462 ? 22.569 40.959 55.845 1.00 21.59 ? 455 SER A CB 1 ATOM 3272 O OG . SER A 1 462 ? 21.252 41.063 56.345 1.00 23.80 ? 455 SER A OG 1 ATOM 3273 N N . ILE A 1 463 ? 24.675 41.266 53.323 1.00 21.70 ? 456 ILE A N 1 ATOM 3274 C CA . ILE A 1 463 ? 26.096 41.248 53.001 1.00 23.19 ? 456 ILE A CA 1 ATOM 3275 C C . ILE A 1 463 ? 26.223 41.270 51.494 1.00 24.37 ? 456 ILE A C 1 ATOM 3276 O O . ILE A 1 463 ? 25.439 40.609 50.800 1.00 24.62 ? 456 ILE A O 1 ATOM 3277 C CB . ILE A 1 463 ? 26.762 39.941 53.509 1.00 23.56 ? 456 ILE A CB 1 ATOM 3278 C CG1 . ILE A 1 463 ? 25.815 38.728 53.220 1.00 25.34 ? 456 ILE A CG1 1 ATOM 3279 C CG2 . ILE A 1 463 ? 27.044 40.027 55.004 1.00 22.25 ? 456 ILE A CG2 1 ATOM 3280 C CD1 . ILE A 1 463 ? 26.508 37.540 52.895 1.00 30.18 ? 456 ILE A CD1 1 ATOM 3281 N N . GLU A 1 464 ? 27.219 41.996 50.990 1.00 25.42 ? 457 GLU A N 1 ATOM 3282 C CA . GLU A 1 464 ? 27.628 41.885 49.568 1.00 26.27 ? 457 GLU A CA 1 ATOM 3283 C C . GLU A 1 464 ? 29.157 41.833 49.513 1.00 26.87 ? 457 GLU A C 1 ATOM 3284 O O . GLU A 1 464 ? 29.786 41.986 48.462 1.00 27.82 ? 457 GLU A O 1 ATOM 3285 C CB . GLU A 1 464 ? 27.063 43.068 48.745 1.00 25.33 ? 457 GLU A CB 1 ATOM 3286 C CG . GLU A 1 464 ? 27.661 44.460 49.169 1.00 25.87 ? 457 GLU A CG 1 ATOM 3287 C CD . GLU A 1 464 ? 26.929 45.654 48.516 1.00 26.27 ? 457 GLU A CD 1 ATOM 3288 O OE1 . GLU A 1 464 ? 25.891 45.432 47.866 1.00 25.25 ? 457 GLU A OE1 1 ATOM 3289 O OE2 . GLU A 1 464 ? 27.379 46.817 48.651 1.00 28.91 ? 457 GLU A OE2 1 ATOM 3290 N N . GLY A 1 465 ? 29.746 41.603 50.677 1.00 26.74 ? 458 GLY A N 1 ATOM 3291 C CA . GLY A 1 465 ? 31.182 41.599 50.866 1.00 26.61 ? 458 GLY A CA 1 ATOM 3292 C C . GLY A 1 465 ? 31.450 41.400 52.366 1.00 27.03 ? 458 GLY A C 1 ATOM 3293 O O . GLY A 1 465 ? 30.509 41.274 53.156 1.00 26.46 ? 458 GLY A O 1 ATOM 3294 N N . ASN A 1 466 ? 32.717 41.395 52.768 1.00 26.98 ? 459 ASN A N 1 ATOM 3295 C CA . ASN A 1 466 ? 33.058 41.174 54.160 1.00 27.74 ? 459 ASN A CA 1 ATOM 3296 C C . ASN A 1 466 ? 34.065 42.212 54.661 1.00 27.54 ? 459 ASN A C 1 ATOM 3297 O O . ASN A 1 466 ? 34.783 41.967 55.613 1.00 28.21 ? 459 ASN A O 1 ATOM 3298 C CB . ASN A 1 466 ? 33.582 39.724 54.376 1.00 28.59 ? 459 ASN A CB 1 ATOM 3299 C CG . ASN A 1 466 ? 34.888 39.448 53.651 1.00 30.59 ? 459 ASN A CG 1 ATOM 3300 O OD1 . ASN A 1 466 ? 35.504 40.353 53.071 1.00 31.51 ? 459 ASN A OD1 1 ATOM 3301 N ND2 . ASN A 1 466 ? 35.343 38.189 53.708 1.00 34.85 ? 459 ASN A ND2 1 ATOM 3302 N N . TYR A 1 467 ? 34.107 43.376 54.015 1.00 27.30 ? 460 TYR A N 1 ATOM 3303 C CA . TYR A 1 467 ? 35.132 44.347 54.314 1.00 27.32 ? 460 TYR A CA 1 ATOM 3304 C C . TYR A 1 467 ? 34.677 45.390 55.351 1.00 27.04 ? 460 TYR A C 1 ATOM 3305 O O . TYR A 1 467 ? 35.325 45.532 56.404 1.00 27.17 ? 460 TYR A O 1 ATOM 3306 C CB . TYR A 1 467 ? 35.643 44.997 53.025 1.00 28.09 ? 460 TYR A CB 1 ATOM 3307 C CG . TYR A 1 467 ? 36.725 46.048 53.216 1.00 30.31 ? 460 TYR A CG 1 ATOM 3308 C CD1 . TYR A 1 467 ? 38.051 45.718 53.652 1.00 32.02 ? 460 TYR A CD1 1 ATOM 3309 C CD2 . TYR A 1 467 ? 36.426 47.383 52.952 1.00 32.56 ? 460 TYR A CD2 1 ATOM 3310 C CE1 . TYR A 1 467 ? 39.046 46.747 53.819 1.00 32.79 ? 460 TYR A CE1 1 ATOM 3311 C CE2 . TYR A 1 467 ? 37.374 48.387 53.099 1.00 34.13 ? 460 TYR A CE2 1 ATOM 3312 C CZ . TYR A 1 467 ? 38.659 48.085 53.529 1.00 36.28 ? 460 TYR A CZ 1 ATOM 3313 O OH . TYR A 1 467 ? 39.489 49.183 53.642 1.00 40.80 ? 460 TYR A OH 1 ATOM 3314 N N . THR A 1 468 ? 33.580 46.104 55.090 1.00 25.65 ? 461 THR A N 1 ATOM 3315 C CA . THR A 1 468 ? 33.143 47.118 56.056 1.00 25.19 ? 461 THR A CA 1 ATOM 3316 C C . THR A 1 468 ? 31.667 47.423 55.916 1.00 24.89 ? 461 THR A C 1 ATOM 3317 O O . THR A 1 468 ? 30.977 46.839 55.058 1.00 24.93 ? 461 THR A O 1 ATOM 3318 C CB . THR A 1 468 ? 33.986 48.428 55.959 1.00 25.57 ? 461 THR A CB 1 ATOM 3319 O OG1 . THR A 1 468 ? 33.787 49.228 57.146 1.00 24.99 ? 461 THR A OG1 1 ATOM 3320 C CG2 . THR A 1 468 ? 33.613 49.226 54.680 1.00 24.53 ? 461 THR A CG2 1 ATOM 3321 N N . LEU A 1 469 ? 31.176 48.332 56.765 1.00 24.25 ? 462 LEU A N 1 ATOM 3322 C CA . LEU A 1 469 ? 29.773 48.724 56.717 1.00 23.67 ? 462 LEU A CA 1 ATOM 3323 C C . LEU A 1 469 ? 29.500 49.632 55.544 1.00 23.49 ? 462 LEU A C 1 ATOM 3324 O O . LEU A 1 469 ? 30.392 50.395 55.129 1.00 24.22 ? 462 LEU A O 1 ATOM 3325 C CB . LEU A 1 469 ? 29.391 49.471 58.020 1.00 23.92 ? 462 LEU A CB 1 ATOM 3326 C CG . LEU A 1 469 ? 27.904 49.683 58.295 1.00 22.37 ? 462 LEU A CG 1 ATOM 3327 C CD1 . LEU A 1 469 ? 27.181 48.300 58.502 1.00 22.90 ? 462 LEU A CD1 1 ATOM 3328 C CD2 . LEU A 1 469 ? 27.791 50.599 59.559 1.00 20.47 ? 462 LEU A CD2 1 ATOM 3329 N N . ARG A 1 470 ? 28.276 49.555 55.020 1.00 21.15 ? 463 ARG A N 1 ATOM 3330 C CA . ARG A 1 470 ? 27.801 50.465 54.027 1.00 21.89 ? 463 ARG A CA 1 ATOM 3331 C C . ARG A 1 470 ? 26.470 50.975 54.540 1.00 21.30 ? 463 ARG A C 1 ATOM 3332 O O . ARG A 1 470 ? 25.628 50.171 54.929 1.00 21.37 ? 463 ARG A O 1 ATOM 3333 C CB . ARG A 1 470 ? 27.607 49.742 52.669 1.00 21.93 ? 463 ARG A CB 1 ATOM 3334 C CG . ARG A 1 470 ? 26.661 50.475 51.739 1.00 23.99 ? 463 ARG A CG 1 ATOM 3335 C CD . ARG A 1 470 ? 26.485 49.757 50.422 1.00 25.70 ? 463 ARG A CD 1 ATOM 3336 N NE . ARG A 1 470 ? 25.427 50.410 49.642 1.00 28.23 ? 463 ARG A NE 1 ATOM 3337 C CZ . ARG A 1 470 ? 24.861 49.874 48.562 1.00 28.26 ? 463 ARG A CZ 1 ATOM 3338 N NH1 . ARG A 1 470 ? 25.247 48.656 48.159 1.00 25.15 ? 463 ARG A NH1 1 ATOM 3339 N NH2 . ARG A 1 470 ? 23.901 50.530 47.905 1.00 28.38 ? 463 ARG A NH2 1 ATOM 3340 N N . VAL A 1 471 ? 26.283 52.291 54.564 1.00 20.72 ? 464 VAL A N 1 ATOM 3341 C CA . VAL A 1 471 ? 24.983 52.880 54.933 1.00 19.61 ? 464 VAL A CA 1 ATOM 3342 C C . VAL A 1 471 ? 24.571 53.901 53.889 1.00 19.81 ? 464 VAL A C 1 ATOM 3343 O O . VAL A 1 471 ? 25.384 54.753 53.533 1.00 19.05 ? 464 VAL A O 1 ATOM 3344 C CB . VAL A 1 471 ? 25.074 53.619 56.319 1.00 19.45 ? 464 VAL A CB 1 ATOM 3345 C CG1 . VAL A 1 471 ? 23.753 54.281 56.690 1.00 18.77 ? 464 VAL A CG1 1 ATOM 3346 C CG2 . VAL A 1 471 ? 25.552 52.659 57.447 1.00 20.88 ? 464 VAL A CG2 1 ATOM 3347 N N . ASP A 1 472 ? 23.301 53.848 53.430 1.00 19.31 ? 465 ASP A N 1 ATOM 3348 C CA . ASP A 1 472 ? 22.758 54.867 52.545 1.00 20.39 ? 465 ASP A CA 1 ATOM 3349 C C . ASP A 1 472 ? 21.482 55.328 53.278 1.00 19.37 ? 465 ASP A C 1 ATOM 3350 O O . ASP A 1 472 ? 20.670 54.501 53.657 1.00 19.39 ? 465 ASP A O 1 ATOM 3351 C CB . ASP A 1 472 ? 22.320 54.344 51.140 1.00 19.37 ? 465 ASP A CB 1 ATOM 3352 C CG . ASP A 1 472 ? 23.358 53.461 50.422 1.00 23.56 ? 465 ASP A CG 1 ATOM 3353 O OD1 . ASP A 1 472 ? 24.533 53.315 50.842 1.00 23.73 ? 465 ASP A OD1 1 ATOM 3354 O OD2 . ASP A 1 472 ? 22.949 52.879 49.366 1.00 28.38 ? 465 ASP A OD2 1 ATOM 3355 N N . CYS A 1 473 ? 21.295 56.621 53.465 1.00 19.05 ? 466 CYS A N 1 ATOM 3356 C CA . CYS A 1 473 ? 20.143 57.092 54.217 1.00 19.23 ? 466 CYS A CA 1 ATOM 3357 C C . CYS A 1 473 ? 19.942 58.599 54.026 1.00 19.01 ? 466 CYS A C 1 ATOM 3358 O O . CYS A 1 473 ? 20.829 59.341 53.557 1.00 20.81 ? 466 CYS A O 1 ATOM 3359 C CB . CYS A 1 473 ? 20.327 56.764 55.742 1.00 18.69 ? 466 CYS A CB 1 ATOM 3360 S SG . CYS A 1 473 ? 21.646 57.673 56.626 1.00 20.93 ? 466 CYS A SG 1 ATOM 3361 N N . THR A 1 474 ? 18.773 59.048 54.419 1.00 18.13 ? 467 THR A N 1 ATOM 3362 C CA . THR A 1 474 ? 18.509 60.465 54.526 1.00 18.05 ? 467 THR A CA 1 ATOM 3363 C C . THR A 1 474 ? 19.514 61.131 55.496 1.00 17.70 ? 467 THR A C 1 ATOM 3364 O O . THR A 1 474 ? 19.905 60.530 56.510 1.00 17.68 ? 467 THR A O 1 ATOM 3365 C CB . THR A 1 474 ? 17.056 60.696 55.003 1.00 17.76 ? 467 THR A CB 1 ATOM 3366 O OG1 . THR A 1 474 ? 16.869 62.082 55.253 1.00 18.37 ? 467 THR A OG1 1 ATOM 3367 C CG2 . THR A 1 474 ? 16.790 59.928 56.333 1.00 15.54 ? 467 THR A CG2 1 ATOM 3368 N N . PRO A 1 475 ? 19.923 62.384 55.216 1.00 17.95 ? 468 PRO A N 1 ATOM 3369 C CA . PRO A 1 475 ? 20.738 63.124 56.189 1.00 17.66 ? 468 PRO A CA 1 ATOM 3370 C C . PRO A 1 475 ? 20.098 63.182 57.605 1.00 18.48 ? 468 PRO A C 1 ATOM 3371 O O . PRO A 1 475 ? 20.838 63.347 58.596 1.00 17.77 ? 468 PRO A O 1 ATOM 3372 C CB . PRO A 1 475 ? 20.812 64.572 55.578 1.00 18.27 ? 468 PRO A CB 1 ATOM 3373 C CG . PRO A 1 475 ? 20.528 64.415 54.157 1.00 16.75 ? 468 PRO A CG 1 ATOM 3374 C CD . PRO A 1 475 ? 19.667 63.179 53.976 1.00 17.51 ? 468 PRO A CD 1 ATOM 3375 N N . LEU A 1 476 ? 18.761 63.062 57.708 1.00 18.19 ? 469 LEU A N 1 ATOM 3376 C CA . LEU A 1 476 ? 18.076 63.119 59.028 1.00 18.86 ? 469 LEU A CA 1 ATOM 3377 C C . LEU A 1 476 ? 18.510 61.986 59.975 1.00 19.41 ? 469 LEU A C 1 ATOM 3378 O O . LEU A 1 476 ? 18.348 62.093 61.204 1.00 20.81 ? 469 LEU A O 1 ATOM 3379 C CB . LEU A 1 476 ? 16.545 63.095 58.880 1.00 18.99 ? 469 LEU A CB 1 ATOM 3380 C CG . LEU A 1 476 ? 15.880 64.361 58.349 1.00 16.90 ? 469 LEU A CG 1 ATOM 3381 C CD1 . LEU A 1 476 ? 14.372 64.225 58.299 1.00 17.45 ? 469 LEU A CD1 1 ATOM 3382 C CD2 . LEU A 1 476 ? 16.318 65.575 59.210 1.00 16.38 ? 469 LEU A CD2 1 ATOM 3383 N N . MET A 1 477 ? 19.064 60.913 59.408 1.00 19.14 ? 470 MET A N 1 ATOM 3384 C CA . MET A 1 477 ? 19.533 59.788 60.198 1.00 19.51 ? 470 MET A CA 1 ATOM 3385 C C . MET A 1 477 ? 21.060 59.727 60.366 1.00 20.21 ? 470 MET A C 1 ATOM 3386 O O . MET A 1 477 ? 21.558 58.794 61.016 1.00 20.18 ? 470 MET A O 1 ATOM 3387 C CB . MET A 1 477 ? 19.028 58.437 59.613 1.00 19.79 ? 470 MET A CB 1 ATOM 3388 C CG . MET A 1 477 ? 17.519 58.190 59.728 1.00 21.86 ? 470 MET A CG 1 ATOM 3389 S SD . MET A 1 477 ? 17.164 56.620 58.864 1.00 23.70 ? 470 MET A SD 1 ATOM 3390 C CE . MET A 1 477 ? 15.383 56.718 58.745 1.00 21.15 ? 470 MET A CE 1 ATOM 3391 N N . TYR A 1 478 ? 21.824 60.691 59.829 1.00 19.96 ? 471 TYR A N 1 ATOM 3392 C CA . TYR A 1 478 ? 23.298 60.615 59.993 1.00 21.07 ? 471 TYR A CA 1 ATOM 3393 C C . TYR A 1 478 ? 23.774 60.505 61.460 1.00 22.03 ? 471 TYR A C 1 ATOM 3394 O O . TYR A 1 478 ? 24.609 59.629 61.807 1.00 21.87 ? 471 TYR A O 1 ATOM 3395 C CB . TYR A 1 478 ? 24.034 61.826 59.360 1.00 20.99 ? 471 TYR A CB 1 ATOM 3396 C CG . TYR A 1 478 ? 24.009 61.952 57.839 1.00 19.86 ? 471 TYR A CG 1 ATOM 3397 C CD1 . TYR A 1 478 ? 23.513 60.933 57.010 1.00 18.81 ? 471 TYR A CD1 1 ATOM 3398 C CD2 . TYR A 1 478 ? 24.516 63.124 57.234 1.00 19.71 ? 471 TYR A CD2 1 ATOM 3399 C CE1 . TYR A 1 478 ? 23.506 61.104 55.557 1.00 20.24 ? 471 TYR A CE1 1 ATOM 3400 C CE2 . TYR A 1 478 ? 24.506 63.306 55.849 1.00 19.75 ? 471 TYR A CE2 1 ATOM 3401 C CZ . TYR A 1 478 ? 24.004 62.312 55.020 1.00 20.45 ? 471 TYR A CZ 1 ATOM 3402 O OH . TYR A 1 478 ? 24.033 62.572 53.679 1.00 22.09 ? 471 TYR A OH 1 ATOM 3403 N N . SER A 1 479 ? 23.271 61.415 62.309 1.00 22.38 ? 472 SER A N 1 ATOM 3404 C CA . SER A 1 479 ? 23.666 61.444 63.731 1.00 22.48 ? 472 SER A CA 1 ATOM 3405 C C . SER A 1 479 ? 23.228 60.190 64.451 1.00 22.73 ? 472 SER A C 1 ATOM 3406 O O . SER A 1 479 ? 24.015 59.638 65.209 1.00 23.83 ? 472 SER A O 1 ATOM 3407 C CB . SER A 1 479 ? 23.139 62.697 64.423 1.00 22.54 ? 472 SER A CB 1 ATOM 3408 O OG A SER A 1 479 ? 23.798 63.829 63.868 0.50 24.10 ? 472 SER A OG 1 ATOM 3409 O OG B SER A 1 479 ? 23.525 62.750 65.799 0.50 21.19 ? 472 SER A OG 1 ATOM 3410 N N . LEU A 1 480 ? 21.991 59.738 64.210 1.00 22.14 ? 473 LEU A N 1 ATOM 3411 C CA . LEU A 1 480 ? 21.515 58.434 64.712 1.00 21.52 ? 473 LEU A CA 1 ATOM 3412 C C . LEU A 1 480 ? 22.536 57.313 64.376 1.00 21.78 ? 473 LEU A C 1 ATOM 3413 O O . LEU A 1 480 ? 22.958 56.545 65.266 1.00 20.98 ? 473 LEU A O 1 ATOM 3414 C CB . LEU A 1 480 ? 20.130 58.095 64.120 1.00 21.61 ? 473 LEU A CB 1 ATOM 3415 C CG . LEU A 1 480 ? 19.631 56.639 64.273 1.00 20.91 ? 473 LEU A CG 1 ATOM 3416 C CD1 . LEU A 1 480 ? 19.515 56.209 65.766 1.00 24.52 ? 473 LEU A CD1 1 ATOM 3417 C CD2 . LEU A 1 480 ? 18.358 56.433 63.559 1.00 23.78 ? 473 LEU A CD2 1 ATOM 3418 N N . VAL A 1 481 ? 22.943 57.233 63.100 1.00 21.11 ? 474 VAL A N 1 ATOM 3419 C CA . VAL A 1 481 ? 23.876 56.184 62.651 1.00 20.72 ? 474 VAL A CA 1 ATOM 3420 C C . VAL A 1 481 ? 25.279 56.331 63.260 1.00 22.02 ? 474 VAL A C 1 ATOM 3421 O O . VAL A 1 481 ? 25.906 55.339 63.708 1.00 21.77 ? 474 VAL A O 1 ATOM 3422 C CB . VAL A 1 481 ? 23.956 56.182 61.095 1.00 20.78 ? 474 VAL A CB 1 ATOM 3423 C CG1 . VAL A 1 481 ? 25.128 55.289 60.619 1.00 21.06 ? 474 VAL A CG1 1 ATOM 3424 C CG2 . VAL A 1 481 ? 22.579 55.703 60.505 1.00 20.84 ? 474 VAL A CG2 1 ATOM 3425 N N . HIS A 1 482 ? 25.780 57.568 63.327 1.00 22.93 ? 475 HIS A N 1 ATOM 3426 C CA . HIS A 1 482 ? 27.075 57.773 63.978 1.00 24.18 ? 475 HIS A CA 1 ATOM 3427 C C . HIS A 1 482 ? 27.010 57.327 65.444 1.00 24.60 ? 475 HIS A C 1 ATOM 3428 O O . HIS A 1 482 ? 27.917 56.608 65.913 1.00 23.46 ? 475 HIS A O 1 ATOM 3429 C CB . HIS A 1 482 ? 27.566 59.230 63.886 1.00 24.62 ? 475 HIS A CB 1 ATOM 3430 C CG . HIS A 1 482 ? 27.843 59.674 62.487 1.00 28.41 ? 475 HIS A CG 1 ATOM 3431 N ND1 . HIS A 1 482 ? 27.895 61.003 62.134 1.00 34.06 ? 475 HIS A ND1 1 ATOM 3432 C CD2 . HIS A 1 482 ? 28.044 58.973 61.346 1.00 29.19 ? 475 HIS A CD2 1 ATOM 3433 C CE1 . HIS A 1 482 ? 28.129 61.101 60.838 1.00 33.46 ? 475 HIS A CE1 1 ATOM 3434 N NE2 . HIS A 1 482 ? 28.236 59.886 60.339 1.00 29.62 ? 475 HIS A NE2 1 ATOM 3435 N N . ASN A 1 483 ? 25.965 57.739 66.161 1.00 24.09 ? 476 ASN A N 1 ATOM 3436 C CA . ASN A 1 483 ? 25.922 57.441 67.623 1.00 25.25 ? 476 ASN A CA 1 ATOM 3437 C C . ASN A 1 483 ? 25.780 55.948 67.866 1.00 25.34 ? 476 ASN A C 1 ATOM 3438 O O . ASN A 1 483 ? 26.418 55.381 68.774 1.00 26.26 ? 476 ASN A O 1 ATOM 3439 C CB . ASN A 1 483 ? 24.761 58.176 68.300 1.00 24.72 ? 476 ASN A CB 1 ATOM 3440 C CG . ASN A 1 483 ? 25.018 59.657 68.426 1.00 26.60 ? 476 ASN A CG 1 ATOM 3441 O OD1 . ASN A 1 483 ? 26.050 60.153 67.976 1.00 24.70 ? 476 ASN A OD1 1 ATOM 3442 N ND2 . ASN A 1 483 ? 24.085 60.376 69.044 1.00 29.43 ? 476 ASN A ND2 1 ATOM 3443 N N . LEU A 1 484 ? 24.936 55.313 67.072 1.00 25.27 ? 477 LEU A N 1 ATOM 3444 C CA . LEU A 1 484 ? 24.656 53.893 67.271 1.00 25.39 ? 477 LEU A CA 1 ATOM 3445 C C . LEU A 1 484 ? 25.888 53.044 66.992 1.00 25.62 ? 477 LEU A C 1 ATOM 3446 O O . LEU A 1 484 ? 26.226 52.178 67.788 1.00 25.84 ? 477 LEU A O 1 ATOM 3447 C CB . LEU A 1 484 ? 23.476 53.444 66.381 1.00 24.68 ? 477 LEU A CB 1 ATOM 3448 C CG . LEU A 1 484 ? 23.274 51.913 66.349 1.00 24.16 ? 477 LEU A CG 1 ATOM 3449 C CD1 . LEU A 1 484 ? 22.958 51.391 67.787 1.00 23.76 ? 477 LEU A CD1 1 ATOM 3450 C CD2 . LEU A 1 484 ? 22.171 51.490 65.327 1.00 23.23 ? 477 LEU A CD2 1 ATOM 3451 N N . THR A 1 485 ? 26.553 53.286 65.865 1.00 26.37 ? 478 THR A N 1 ATOM 3452 C CA . THR A 1 485 ? 27.775 52.531 65.495 1.00 26.83 ? 478 THR A CA 1 ATOM 3453 C C . THR A 1 485 ? 28.921 52.741 66.487 1.00 28.15 ? 478 THR A C 1 ATOM 3454 O O . THR A 1 485 ? 29.753 51.861 66.655 1.00 27.81 ? 478 THR A O 1 ATOM 3455 C CB . THR A 1 485 ? 28.251 52.787 64.020 1.00 26.52 ? 478 THR A CB 1 ATOM 3456 O OG1 . THR A 1 485 ? 28.591 54.169 63.837 1.00 25.01 ? 478 THR A OG1 1 ATOM 3457 C CG2 . THR A 1 485 ? 27.165 52.335 62.946 1.00 23.57 ? 478 THR A CG2 1 ATOM 3458 N N . LYS A 1 486 ? 28.956 53.883 67.178 1.00 30.05 ? 479 LYS A N 1 ATOM 3459 C CA . LYS A 1 486 ? 29.962 54.089 68.243 1.00 31.53 ? 479 LYS A CA 1 ATOM 3460 C C . LYS A 1 486 ? 29.723 53.158 69.434 1.00 31.12 ? 479 LYS A C 1 ATOM 3461 O O . LYS A 1 486 ? 30.646 52.884 70.171 1.00 31.60 ? 479 LYS A O 1 ATOM 3462 C CB . LYS A 1 486 ? 29.998 55.559 68.716 1.00 31.98 ? 479 LYS A CB 1 ATOM 3463 C CG . LYS A 1 486 ? 30.637 56.482 67.700 1.00 33.02 ? 479 LYS A CG 1 ATOM 3464 C CD . LYS A 1 486 ? 30.675 57.924 68.191 1.00 35.41 ? 479 LYS A CD 1 ATOM 3465 C CE . LYS A 1 486 ? 30.936 58.798 66.987 1.00 34.78 ? 479 LYS A CE 1 ATOM 3466 N NZ . LYS A 1 486 ? 30.884 60.233 67.306 1.00 35.04 ? 479 LYS A NZ 1 ATOM 3467 N N . GLU A 1 487 ? 28.488 52.667 69.582 1.00 30.86 ? 480 GLU A N 1 ATOM 3468 C CA . GLU A 1 487 ? 28.069 51.792 70.702 1.00 31.48 ? 480 GLU A CA 1 ATOM 3469 C C . GLU A 1 487 ? 28.129 50.303 70.339 1.00 31.64 ? 480 GLU A C 1 ATOM 3470 O O . GLU A 1 487 ? 27.942 49.449 71.198 1.00 32.47 ? 480 GLU A O 1 ATOM 3471 C CB . GLU A 1 487 ? 26.629 52.129 71.145 1.00 31.81 ? 480 GLU A CB 1 ATOM 3472 C CG . GLU A 1 487 ? 26.457 53.515 71.749 1.00 33.23 ? 480 GLU A CG 1 ATOM 3473 C CD . GLU A 1 487 ? 27.338 53.732 72.976 0.30 32.07 ? 480 GLU A CD 1 ATOM 3474 O OE1 . GLU A 1 487 ? 27.454 52.801 73.801 0.20 30.81 ? 480 GLU A OE1 1 ATOM 3475 O OE2 . GLU A 1 487 ? 27.915 54.830 73.108 0.20 31.63 ? 480 GLU A OE2 1 ATOM 3476 N N . LEU A 1 488 ? 28.382 50.000 69.072 1.00 29.76 ? 481 LEU A N 1 ATOM 3477 C CA . LEU A 1 488 ? 28.446 48.611 68.589 1.00 29.14 ? 481 LEU A CA 1 ATOM 3478 C C . LEU A 1 488 ? 29.898 48.108 68.449 1.00 29.32 ? 481 LEU A C 1 ATOM 3479 O O . LEU A 1 488 ? 30.794 48.888 68.132 1.00 29.09 ? 481 LEU A O 1 ATOM 3480 C CB . LEU A 1 488 ? 27.698 48.474 67.243 1.00 27.39 ? 481 LEU A CB 1 ATOM 3481 C CG . LEU A 1 488 ? 26.200 48.848 67.231 1.00 26.28 ? 481 LEU A CG 1 ATOM 3482 C CD1 . LEU A 1 488 ? 25.569 48.707 65.830 1.00 20.61 ? 481 LEU A CD1 1 ATOM 3483 C CD2 . LEU A 1 488 ? 25.411 48.018 68.265 1.00 25.73 ? 481 LEU A CD2 1 ATOM 3484 N N . LYS A 1 489 ? 30.115 46.807 68.647 1.00 29.77 ? 482 LYS A N 1 ATOM 3485 C CA . LYS A 1 489 ? 31.468 46.221 68.574 1.00 30.76 ? 482 LYS A CA 1 ATOM 3486 C C . LYS A 1 489 ? 31.834 45.993 67.094 1.00 30.71 ? 482 LYS A C 1 ATOM 3487 O O . LYS A 1 489 ? 30.987 45.562 66.327 1.00 30.42 ? 482 LYS A O 1 ATOM 3488 C CB . LYS A 1 489 ? 31.498 44.896 69.340 1.00 30.83 ? 482 LYS A CB 1 ATOM 3489 C CG . LYS A 1 489 ? 31.364 45.032 70.876 1.00 35.66 ? 482 LYS A CG 1 ATOM 3490 C CD . LYS A 1 489 ? 31.561 43.649 71.570 1.00 44.33 ? 482 LYS A CD 1 ATOM 3491 C CE . LYS A 1 489 ? 30.245 43.020 72.135 0.90 48.77 ? 482 LYS A CE 1 ATOM 3492 N NZ . LYS A 1 489 ? 28.952 43.141 71.275 0.90 50.15 ? 482 LYS A NZ 1 ATOM 3493 N N . SER A 1 490 ? 33.060 46.297 66.679 1.00 30.21 ? 483 SER A N 1 ATOM 3494 C CA . SER A 1 490 ? 33.450 45.967 65.300 1.00 30.40 ? 483 SER A CA 1 ATOM 3495 C C . SER A 1 490 ? 33.616 44.447 65.163 1.00 29.58 ? 483 SER A C 1 ATOM 3496 O O . SER A 1 490 ? 34.251 43.833 66.019 1.00 29.31 ? 483 SER A O 1 ATOM 3497 C CB . SER A 1 490 ? 34.767 46.638 64.894 1.00 30.27 ? 483 SER A CB 1 ATOM 3498 O OG . SER A 1 490 ? 35.095 46.197 63.583 1.00 30.15 ? 483 SER A OG 1 ATOM 3499 N N . PRO A 1 491 ? 33.059 43.836 64.087 1.00 29.21 ? 484 PRO A N 1 ATOM 3500 C CA . PRO A 1 491 ? 33.311 42.404 63.900 1.00 29.28 ? 484 PRO A CA 1 ATOM 3501 C C . PRO A 1 491 ? 34.585 42.129 63.093 1.00 30.50 ? 484 PRO A C 1 ATOM 3502 O O . PRO A 1 491 ? 34.881 40.957 62.822 1.00 29.87 ? 484 PRO A O 1 ATOM 3503 C CB . PRO A 1 491 ? 32.120 41.951 63.075 1.00 27.02 ? 484 PRO A CB 1 ATOM 3504 C CG . PRO A 1 491 ? 31.821 43.172 62.209 1.00 28.46 ? 484 PRO A CG 1 ATOM 3505 C CD . PRO A 1 491 ? 32.120 44.368 63.078 1.00 29.06 ? 484 PRO A CD 1 ATOM 3506 N N . ASP A 1 492 ? 35.317 43.186 62.710 1.00 31.52 ? 485 ASP A N 1 ATOM 3507 C CA . ASP A 1 492 ? 36.428 43.047 61.751 1.00 32.33 ? 485 ASP A CA 1 ATOM 3508 C C . ASP A 1 492 ? 37.709 42.531 62.430 1.00 33.52 ? 485 ASP A C 1 ATOM 3509 O O . ASP A 1 492 ? 38.023 42.942 63.553 1.00 33.58 ? 485 ASP A O 1 ATOM 3510 C CB . ASP A 1 492 ? 36.788 44.394 61.108 1.00 31.88 ? 485 ASP A CB 1 ATOM 3511 C CG . ASP A 1 492 ? 35.636 45.047 60.377 1.00 31.98 ? 485 ASP A CG 1 ATOM 3512 O OD1 . ASP A 1 492 ? 34.512 44.489 60.326 1.00 32.80 ? 485 ASP A OD1 1 ATOM 3513 O OD2 . ASP A 1 492 ? 35.860 46.152 59.841 1.00 30.75 ? 485 ASP A OD2 1 ATOM 3514 N N . GLU A 1 493 ? 38.458 41.678 61.725 1.00 34.15 ? 486 GLU A N 1 ATOM 3515 C CA . GLU A 1 493 ? 39.801 41.261 62.124 1.00 35.49 ? 486 GLU A CA 1 ATOM 3516 C C . GLU A 1 493 ? 40.701 42.490 62.290 1.00 35.70 ? 486 GLU A C 1 ATOM 3517 O O . GLU A 1 493 ? 40.731 43.365 61.432 1.00 36.04 ? 486 GLU A O 1 ATOM 3518 C CB . GLU A 1 493 ? 40.408 40.302 61.067 1.00 35.61 ? 486 GLU A CB 1 ATOM 3519 C CG . GLU A 1 493 ? 39.653 38.954 60.873 0.60 34.42 ? 486 GLU A CG 1 ATOM 3520 C CD . GLU A 1 493 ? 38.306 39.047 60.148 0.30 32.75 ? 486 GLU A CD 1 ATOM 3521 O OE1 . GLU A 1 493 ? 37.885 40.153 59.700 0.30 31.38 ? 486 GLU A OE1 1 ATOM 3522 O OE2 . GLU A 1 493 ? 37.655 37.984 60.039 0.30 29.68 ? 486 GLU A OE2 1 ATOM 3523 N N . GLY A 1 494 ? 41.429 42.564 63.394 1.00 36.45 ? 487 GLY A N 1 ATOM 3524 C CA . GLY A 1 494 ? 42.324 43.700 63.630 1.00 36.74 ? 487 GLY A CA 1 ATOM 3525 C C . GLY A 1 494 ? 41.664 44.842 64.374 1.00 37.30 ? 487 GLY A C 1 ATOM 3526 O O . GLY A 1 494 ? 42.334 45.793 64.771 1.00 37.10 ? 487 GLY A O 1 ATOM 3527 N N . PHE A 1 495 ? 40.345 44.769 64.558 1.00 37.34 ? 488 PHE A N 1 ATOM 3528 C CA . PHE A 1 495 ? 39.638 45.798 65.314 1.00 37.88 ? 488 PHE A CA 1 ATOM 3529 C C . PHE A 1 495 ? 38.898 45.206 66.513 1.00 38.53 ? 488 PHE A C 1 ATOM 3530 O O . PHE A 1 495 ? 37.856 45.736 66.906 1.00 38.57 ? 488 PHE A O 1 ATOM 3531 C CB . PHE A 1 495 ? 38.625 46.526 64.396 1.00 37.56 ? 488 PHE A CB 1 ATOM 3532 C CG . PHE A 1 495 ? 39.267 47.333 63.325 1.00 37.47 ? 488 PHE A CG 1 ATOM 3533 C CD1 . PHE A 1 495 ? 39.556 48.680 63.536 1.00 38.59 ? 488 PHE A CD1 1 ATOM 3534 C CD2 . PHE A 1 495 ? 39.619 46.745 62.106 1.00 37.89 ? 488 PHE A CD2 1 ATOM 3535 C CE1 . PHE A 1 495 ? 40.178 49.459 62.547 1.00 38.39 ? 488 PHE A CE1 1 ATOM 3536 C CE2 . PHE A 1 495 ? 40.243 47.504 61.110 1.00 38.55 ? 488 PHE A CE2 1 ATOM 3537 C CZ . PHE A 1 495 ? 40.505 48.881 61.332 1.00 38.69 ? 488 PHE A CZ 1 ATOM 3538 N N . GLU A 1 496 ? 39.377 44.089 67.058 1.00 39.21 ? 489 GLU A N 1 ATOM 3539 C CA . GLU A 1 496 ? 38.712 43.500 68.238 1.00 40.87 ? 489 GLU A CA 1 ATOM 3540 C C . GLU A 1 496 ? 38.787 44.448 69.454 1.00 40.49 ? 489 GLU A C 1 ATOM 3541 O O . GLU A 1 496 ? 39.812 45.071 69.694 1.00 40.18 ? 489 GLU A O 1 ATOM 3542 C CB . GLU A 1 496 ? 39.153 42.035 68.560 1.00 41.46 ? 489 GLU A CB 1 ATOM 3543 C CG . GLU A 1 496 ? 40.520 41.577 68.096 1.00 44.13 ? 489 GLU A CG 1 ATOM 3544 C CD . GLU A 1 496 ? 40.680 41.425 66.581 1.00 46.11 ? 489 GLU A CD 1 ATOM 3545 O OE1 . GLU A 1 496 ? 40.168 40.455 65.958 1.00 45.76 ? 489 GLU A OE1 1 ATOM 3546 O OE2 . GLU A 1 496 ? 41.395 42.279 66.027 1.00 47.04 ? 489 GLU A OE2 1 ATOM 3547 N N . GLY A 1 497 ? 37.670 44.622 70.154 1.00 39.81 ? 490 GLY A N 1 ATOM 3548 C CA . GLY A 1 497 ? 37.594 45.651 71.201 1.00 39.93 ? 490 GLY A CA 1 ATOM 3549 C C . GLY A 1 497 ? 37.384 47.087 70.689 1.00 39.58 ? 490 GLY A C 1 ATOM 3550 O O . GLY A 1 497 ? 37.265 48.019 71.494 1.00 40.26 ? 490 GLY A O 1 ATOM 3551 N N . LYS A 1 498 ? 37.355 47.291 69.369 1.00 37.72 ? 491 LYS A N 1 ATOM 3552 C CA . LYS A 1 498 ? 37.091 48.626 68.826 1.00 36.44 ? 491 LYS A CA 1 ATOM 3553 C C . LYS A 1 498 ? 35.635 48.719 68.375 1.00 34.73 ? 491 LYS A C 1 ATOM 3554 O O . LYS A 1 498 ? 34.998 47.695 68.129 1.00 34.26 ? 491 LYS A O 1 ATOM 3555 C CB . LYS A 1 498 ? 38.049 48.985 67.679 1.00 36.41 ? 491 LYS A CB 1 ATOM 3556 C CG . LYS A 1 498 ? 39.554 48.892 68.040 1.00 38.06 ? 491 LYS A CG 1 ATOM 3557 C CD . LYS A 1 498 ? 39.910 49.728 69.272 0.75 39.91 ? 491 LYS A CD 1 ATOM 3558 C CE . LYS A 1 498 ? 41.378 49.537 69.651 0.55 41.90 ? 491 LYS A CE 1 ATOM 3559 N NZ . LYS A 1 498 ? 42.197 49.921 68.475 0.50 41.72 ? 491 LYS A NZ 1 ATOM 3560 N N . SER A 1 499 ? 35.119 49.940 68.282 1.00 32.48 ? 492 SER A N 1 ATOM 3561 C CA . SER A 1 499 ? 33.735 50.149 67.875 1.00 30.90 ? 492 SER A CA 1 ATOM 3562 C C . SER A 1 499 ? 33.583 49.969 66.351 1.00 29.68 ? 492 SER A C 1 ATOM 3563 O O . SER A 1 499 ? 34.548 50.088 65.609 1.00 29.26 ? 492 SER A O 1 ATOM 3564 C CB . SER A 1 499 ? 33.263 51.531 68.298 1.00 30.57 ? 492 SER A CB 1 ATOM 3565 O OG . SER A 1 499 ? 33.737 52.509 67.407 1.00 30.14 ? 492 SER A OG 1 ATOM 3566 N N . LEU A 1 500 ? 32.367 49.682 65.907 1.00 28.50 ? 493 LEU A N 1 ATOM 3567 C CA . LEU A 1 500 ? 32.045 49.586 64.485 1.00 27.50 ? 493 LEU A CA 1 ATOM 3568 C C . LEU A 1 500 ? 32.292 50.967 63.831 1.00 27.58 ? 493 LEU A C 1 ATOM 3569 O O . LEU A 1 500 ? 32.745 51.041 62.666 1.00 27.07 ? 493 LEU A O 1 ATOM 3570 C CB . LEU A 1 500 ? 30.574 49.175 64.320 1.00 27.22 ? 493 LEU A CB 1 ATOM 3571 C CG . LEU A 1 500 ? 30.009 49.075 62.902 1.00 25.73 ? 493 LEU A CG 1 ATOM 3572 C CD1 . LEU A 1 500 ? 30.845 48.049 62.057 1.00 25.60 ? 493 LEU A CD1 1 ATOM 3573 C CD2 . LEU A 1 500 ? 28.509 48.731 62.929 1.00 22.73 ? 493 LEU A CD2 1 ATOM 3574 N N . TYR A 1 501 ? 31.977 52.040 64.565 1.00 26.35 ? 494 TYR A N 1 ATOM 3575 C CA . TYR A 1 501 ? 32.260 53.380 64.065 1.00 27.15 ? 494 TYR A CA 1 ATOM 3576 C C . TYR A 1 501 ? 33.752 53.499 63.717 1.00 27.85 ? 494 TYR A C 1 ATOM 3577 O O . TYR A 1 501 ? 34.108 54.052 62.666 1.00 27.87 ? 494 TYR A O 1 ATOM 3578 C CB . TYR A 1 501 ? 31.923 54.471 65.094 1.00 26.75 ? 494 TYR A CB 1 ATOM 3579 C CG . TYR A 1 501 ? 32.131 55.895 64.573 1.00 26.74 ? 494 TYR A CG 1 ATOM 3580 C CD1 . TYR A 1 501 ? 31.092 56.575 63.950 1.00 25.53 ? 494 TYR A CD1 1 ATOM 3581 C CD2 . TYR A 1 501 ? 33.371 56.552 64.706 1.00 28.26 ? 494 TYR A CD2 1 ATOM 3582 C CE1 . TYR A 1 501 ? 31.259 57.893 63.470 1.00 27.45 ? 494 TYR A CE1 1 ATOM 3583 C CE2 . TYR A 1 501 ? 33.552 57.880 64.236 1.00 28.13 ? 494 TYR A CE2 1 ATOM 3584 C CZ . TYR A 1 501 ? 32.486 58.524 63.617 1.00 27.06 ? 494 TYR A CZ 1 ATOM 3585 O OH . TYR A 1 501 ? 32.608 59.790 63.135 1.00 27.39 ? 494 TYR A OH 1 ATOM 3586 N N . GLU A 1 502 ? 34.615 53.027 64.607 1.00 28.55 ? 495 GLU A N 1 ATOM 3587 C CA . GLU A 1 502 ? 36.056 53.150 64.370 1.00 30.30 ? 495 GLU A CA 1 ATOM 3588 C C . GLU A 1 502 ? 36.528 52.360 63.121 1.00 29.99 ? 495 GLU A C 1 ATOM 3589 O O . GLU A 1 502 ? 37.256 52.901 62.287 1.00 29.66 ? 495 GLU A O 1 ATOM 3590 C CB . GLU A 1 502 ? 36.870 52.728 65.600 1.00 31.49 ? 495 GLU A CB 1 ATOM 3591 C CG . GLU A 1 502 ? 38.363 52.769 65.334 1.00 34.54 ? 495 GLU A CG 1 ATOM 3592 C CD . GLU A 1 502 ? 39.189 52.669 66.583 1.00 40.50 ? 495 GLU A CD 1 ATOM 3593 O OE1 . GLU A 1 502 ? 38.741 53.155 67.651 1.00 43.83 ? 495 GLU A OE1 1 ATOM 3594 O OE2 . GLU A 1 502 ? 40.288 52.095 66.490 1.00 43.27 ? 495 GLU A OE2 1 ATOM 3595 N N . SER A 1 503 ? 36.085 51.107 62.989 1.00 29.21 ? 496 SER A N 1 ATOM 3596 C CA . SER A 1 503 ? 36.533 50.277 61.877 1.00 29.12 ? 496 SER A CA 1 ATOM 3597 C C . SER A 1 503 ? 35.932 50.787 60.557 1.00 29.30 ? 496 SER A C 1 ATOM 3598 O O . SER A 1 503 ? 36.637 50.881 59.550 1.00 30.34 ? 496 SER A O 1 ATOM 3599 C CB . SER A 1 503 ? 36.261 48.786 62.122 1.00 28.79 ? 496 SER A CB 1 ATOM 3600 O OG . SER A 1 503 ? 34.876 48.494 62.177 1.00 29.37 ? 496 SER A OG 1 ATOM 3601 N N . TRP A 1 504 ? 34.644 51.129 60.577 1.00 28.05 ? 497 TRP A N 1 ATOM 3602 C CA . TRP A 1 504 ? 33.961 51.700 59.427 1.00 27.54 ? 497 TRP A CA 1 ATOM 3603 C C . TRP A 1 504 ? 34.599 53.037 58.983 1.00 28.00 ? 497 TRP A C 1 ATOM 3604 O O . TRP A 1 504 ? 34.853 53.240 57.779 1.00 28.45 ? 497 TRP A O 1 ATOM 3605 C CB . TRP A 1 504 ? 32.473 51.867 59.761 1.00 26.94 ? 497 TRP A CB 1 ATOM 3606 C CG . TRP A 1 504 ? 31.607 52.525 58.697 1.00 25.65 ? 497 TRP A CG 1 ATOM 3607 C CD1 . TRP A 1 504 ? 31.743 52.437 57.323 1.00 23.20 ? 497 TRP A CD1 1 ATOM 3608 C CD2 . TRP A 1 504 ? 30.431 53.304 58.941 1.00 25.79 ? 497 TRP A CD2 1 ATOM 3609 N NE1 . TRP A 1 504 ? 30.726 53.156 56.702 1.00 23.84 ? 497 TRP A NE1 1 ATOM 3610 C CE2 . TRP A 1 504 ? 29.905 53.693 57.667 1.00 24.51 ? 497 TRP A CE2 1 ATOM 3611 C CE3 . TRP A 1 504 ? 29.774 53.741 60.120 1.00 24.32 ? 497 TRP A CE3 1 ATOM 3612 C CZ2 . TRP A 1 504 ? 28.755 54.510 57.538 1.00 23.75 ? 497 TRP A CZ2 1 ATOM 3613 C CZ3 . TRP A 1 504 ? 28.611 54.539 59.988 1.00 24.16 ? 497 TRP A CZ3 1 ATOM 3614 C CH2 . TRP A 1 504 ? 28.130 54.926 58.702 1.00 24.41 ? 497 TRP A CH2 1 ATOM 3615 N N . THR A 1 505 ? 34.880 53.930 59.933 1.00 27.29 ? 498 THR A N 1 ATOM 3616 C CA . THR A 1 505 ? 35.468 55.218 59.597 1.00 28.28 ? 498 THR A CA 1 ATOM 3617 C C . THR A 1 505 ? 36.912 55.024 59.025 1.00 30.21 ? 498 THR A C 1 ATOM 3618 O O . THR A 1 505 ? 37.281 55.660 58.038 1.00 31.15 ? 498 THR A O 1 ATOM 3619 C CB . THR A 1 505 ? 35.461 56.170 60.819 1.00 28.09 ? 498 THR A CB 1 ATOM 3620 O OG1 A THR A 1 505 ? 34.104 56.394 61.238 0.75 24.74 ? 498 THR A OG1 1 ATOM 3621 C CG2 A THR A 1 505 ? 36.136 57.517 60.479 0.75 27.73 ? 498 THR A CG2 1 ATOM 3622 N N . LYS A 1 506 ? 37.706 54.146 59.632 1.00 30.75 ? 499 LYS A N 1 ATOM 3623 C CA . LYS A 1 506 ? 39.028 53.838 59.092 1.00 32.74 ? 499 LYS A CA 1 ATOM 3624 C C . LYS A 1 506 ? 38.943 53.250 57.666 1.00 33.50 ? 499 LYS A C 1 ATOM 3625 O O . LYS A 1 506 ? 39.668 53.695 56.789 1.00 35.01 ? 499 LYS A O 1 ATOM 3626 C CB . LYS A 1 506 ? 39.807 52.904 60.038 1.00 33.16 ? 499 LYS A CB 1 ATOM 3627 C CG . LYS A 1 506 ? 41.363 52.954 59.926 1.00 36.13 ? 499 LYS A CG 1 ATOM 3628 C CD . LYS A 1 506 ? 41.929 52.129 58.788 0.40 35.14 ? 499 LYS A CD 1 ATOM 3629 C CE . LYS A 1 506 ? 43.468 52.080 58.854 0.20 34.40 ? 499 LYS A CE 1 ATOM 3630 N NZ . LYS A 1 506 ? 44.096 53.433 58.811 0.20 32.02 ? 499 LYS A NZ 1 ATOM 3631 N N . LYS A 1 507 ? 38.056 52.283 57.425 1.00 33.15 ? 500 LYS A N 1 ATOM 3632 C CA . LYS A 1 507 ? 38.000 51.581 56.129 1.00 33.58 ? 500 LYS A CA 1 ATOM 3633 C C . LYS A 1 507 ? 37.284 52.363 55.027 1.00 33.31 ? 500 LYS A C 1 ATOM 3634 O O . LYS A 1 507 ? 37.553 52.170 53.845 1.00 33.42 ? 500 LYS A O 1 ATOM 3635 C CB . LYS A 1 507 ? 37.371 50.193 56.289 1.00 32.91 ? 500 LYS A CB 1 ATOM 3636 C CG . LYS A 1 507 ? 38.299 49.170 56.991 1.00 34.07 ? 500 LYS A CG 1 ATOM 3637 C CD . LYS A 1 507 ? 37.579 47.823 57.168 1.00 32.63 ? 500 LYS A CD 1 ATOM 3638 C CE . LYS A 1 507 ? 38.480 46.752 57.803 1.00 34.88 ? 500 LYS A CE 1 ATOM 3639 N NZ . LYS A 1 507 ? 37.788 45.391 57.756 1.00 34.04 ? 500 LYS A NZ 1 ATOM 3640 N N . SER A 1 508 ? 36.371 53.244 55.410 1.00 33.04 ? 501 SER A N 1 ATOM 3641 C CA . SER A 1 508 ? 35.551 53.923 54.426 1.00 33.33 ? 501 SER A CA 1 ATOM 3642 C C . SER A 1 508 ? 35.385 55.383 54.855 1.00 34.18 ? 501 SER A C 1 ATOM 3643 O O . SER A 1 508 ? 34.280 55.805 55.254 1.00 32.58 ? 501 SER A O 1 ATOM 3644 C CB . SER A 1 508 ? 34.213 53.212 54.319 1.00 33.12 ? 501 SER A CB 1 ATOM 3645 O OG . SER A 1 508 ? 33.537 53.653 53.176 1.00 32.52 ? 501 SER A OG 1 ATOM 3646 N N . PRO A 1 509 ? 36.500 56.161 54.785 1.00 35.35 ? 502 PRO A N 1 ATOM 3647 C CA . PRO A 1 509 ? 36.487 57.534 55.283 1.00 36.06 ? 502 PRO A CA 1 ATOM 3648 C C . PRO A 1 509 ? 35.537 58.381 54.462 1.00 36.64 ? 502 PRO A C 1 ATOM 3649 O O . PRO A 1 509 ? 35.440 58.220 53.256 1.00 35.50 ? 502 PRO A O 1 ATOM 3650 C CB . PRO A 1 509 ? 37.950 58.015 55.095 1.00 36.01 ? 502 PRO A CB 1 ATOM 3651 C CG . PRO A 1 509 ? 38.541 57.096 54.061 1.00 36.43 ? 502 PRO A CG 1 ATOM 3652 C CD . PRO A 1 509 ? 37.825 55.772 54.249 1.00 35.34 ? 502 PRO A CD 1 ATOM 3653 N N . SER A 1 510 ? 34.833 59.273 55.128 1.00 38.63 ? 503 SER A N 1 ATOM 3654 C CA . SER A 1 510 ? 34.062 60.281 54.434 1.00 42.06 ? 503 SER A CA 1 ATOM 3655 C C . SER A 1 510 ? 34.992 61.122 53.529 1.00 44.03 ? 503 SER A C 1 ATOM 3656 O O . SER A 1 510 ? 36.091 61.510 53.966 1.00 43.82 ? 503 SER A O 1 ATOM 3657 C CB . SER A 1 510 ? 33.355 61.165 55.461 1.00 42.07 ? 503 SER A CB 1 ATOM 3658 O OG . SER A 1 510 ? 33.202 62.458 54.948 1.00 43.38 ? 503 SER A OG 1 ATOM 3659 N N . PRO A 1 511 ? 34.578 61.376 52.270 1.00 45.88 ? 504 PRO A N 1 ATOM 3660 C CA . PRO A 1 511 ? 35.378 62.283 51.437 1.00 48.26 ? 504 PRO A CA 1 ATOM 3661 C C . PRO A 1 511 ? 35.361 63.771 51.932 1.00 50.43 ? 504 PRO A C 1 ATOM 3662 O O . PRO A 1 511 ? 36.349 64.498 51.721 1.00 50.96 ? 504 PRO A O 1 ATOM 3663 C CB . PRO A 1 511 ? 34.756 62.132 50.036 1.00 47.92 ? 504 PRO A CB 1 ATOM 3664 C CG . PRO A 1 511 ? 33.354 61.688 50.285 1.00 47.32 ? 504 PRO A CG 1 ATOM 3665 C CD . PRO A 1 511 ? 33.377 60.880 51.568 1.00 46.23 ? 504 PRO A CD 1 ATOM 3666 N N . GLU A 1 512 ? 34.286 64.194 52.613 1.00 52.58 ? 505 GLU A N 1 ATOM 3667 C CA . GLU A 1 512 ? 34.155 65.596 53.107 1.00 54.24 ? 505 GLU A CA 1 ATOM 3668 C C . GLU A 1 512 ? 34.775 65.878 54.486 1.00 54.37 ? 505 GLU A C 1 ATOM 3669 O O . GLU A 1 512 ? 35.235 67.001 54.727 1.00 55.17 ? 505 GLU A O 1 ATOM 3670 C CB . GLU A 1 512 ? 32.687 66.115 53.100 1.00 54.85 ? 505 GLU A CB 1 ATOM 3671 C CG . GLU A 1 512 ? 31.962 66.154 51.731 1.00 57.52 ? 505 GLU A CG 1 ATOM 3672 C CD . GLU A 1 512 ? 30.900 65.059 51.607 1.00 60.85 ? 505 GLU A CD 1 ATOM 3673 O OE1 . GLU A 1 512 ? 30.420 64.758 50.479 1.00 64.04 ? 505 GLU A OE1 1 ATOM 3674 O OE2 . GLU A 1 512 ? 30.521 64.497 52.657 1.00 61.35 ? 505 GLU A OE2 1 ATOM 3675 N N . PHE A 1 513 ? 34.774 64.901 55.398 1.00 53.75 ? 506 PHE A N 1 ATOM 3676 C CA . PHE A 1 513 ? 35.100 65.219 56.800 1.00 53.08 ? 506 PHE A CA 1 ATOM 3677 C C . PHE A 1 513 ? 36.030 64.239 57.489 1.00 53.26 ? 506 PHE A C 1 ATOM 3678 O O . PHE A 1 513 ? 35.868 63.015 57.434 1.00 52.91 ? 506 PHE A O 1 ATOM 3679 C CB . PHE A 1 513 ? 33.826 65.425 57.645 1.00 53.19 ? 506 PHE A CB 1 ATOM 3680 C CG . PHE A 1 513 ? 32.887 66.494 57.117 0.40 51.04 ? 506 PHE A CG 1 ATOM 3681 C CD1 . PHE A 1 513 ? 31.716 66.142 56.455 0.40 49.30 ? 506 PHE A CD1 1 ATOM 3682 C CD2 . PHE A 1 513 ? 33.163 67.841 57.307 0.30 49.66 ? 506 PHE A CD2 1 ATOM 3683 C CE1 . PHE A 1 513 ? 30.848 67.116 55.982 0.30 48.23 ? 506 PHE A CE1 1 ATOM 3684 C CE2 . PHE A 1 513 ? 32.301 68.815 56.832 0.30 48.86 ? 506 PHE A CE2 1 ATOM 3685 C CZ . PHE A 1 513 ? 31.143 68.453 56.170 0.30 48.18 ? 506 PHE A CZ 1 ATOM 3686 N N . SER A 1 514 ? 37.013 64.795 58.165 1.00 53.36 ? 507 SER A N 1 ATOM 3687 C CA . SER A 1 514 ? 37.980 63.983 58.881 1.00 53.00 ? 507 SER A CA 1 ATOM 3688 C C . SER A 1 514 ? 37.308 63.291 60.064 1.00 51.16 ? 507 SER A C 1 ATOM 3689 O O . SER A 1 514 ? 36.548 63.938 60.812 1.00 51.91 ? 507 SER A O 1 ATOM 3690 C CB . SER A 1 514 ? 39.151 64.851 59.374 1.00 53.60 ? 507 SER A CB 1 ATOM 3691 O OG . SER A 1 514 ? 40.270 64.697 58.519 1.00 56.09 ? 507 SER A OG 1 ATOM 3692 N N . GLY A 1 515 ? 37.581 61.990 60.220 1.00 47.95 ? 508 GLY A N 1 ATOM 3693 C CA . GLY A 1 515 ? 37.167 61.255 61.415 1.00 44.20 ? 508 GLY A CA 1 ATOM 3694 C C . GLY A 1 515 ? 35.692 60.875 61.376 1.00 41.63 ? 508 GLY A C 1 ATOM 3695 O O . GLY A 1 515 ? 35.133 60.471 62.408 1.00 40.42 ? 508 GLY A O 1 ATOM 3696 N N . MET A 1 516 ? 35.080 61.016 60.191 1.00 39.38 ? 509 MET A N 1 ATOM 3697 C CA . MET A 1 516 ? 33.701 60.547 59.906 1.00 38.28 ? 509 MET A CA 1 ATOM 3698 C C . MET A 1 516 ? 33.723 59.445 58.851 1.00 36.15 ? 509 MET A C 1 ATOM 3699 O O . MET A 1 516 ? 34.602 59.438 57.991 1.00 36.31 ? 509 MET A O 1 ATOM 3700 C CB . MET A 1 516 ? 32.843 61.649 59.290 1.00 39.00 ? 509 MET A CB 1 ATOM 3701 C CG . MET A 1 516 ? 33.071 63.000 59.855 1.00 44.50 ? 509 MET A CG 1 ATOM 3702 S SD . MET A 1 516 ? 31.983 63.265 61.216 1.00 53.66 ? 509 MET A SD 1 ATOM 3703 C CE . MET A 1 516 ? 30.548 63.846 60.296 1.00 53.42 ? 509 MET A CE 1 ATOM 3704 N N . PRO A 1 517 ? 32.722 58.546 58.860 1.00 34.18 ? 510 PRO A N 1 ATOM 3705 C CA . PRO A 1 517 ? 32.604 57.563 57.776 1.00 32.29 ? 510 PRO A CA 1 ATOM 3706 C C . PRO A 1 517 ? 31.777 58.065 56.595 1.00 30.96 ? 510 PRO A C 1 ATOM 3707 O O . PRO A 1 517 ? 30.949 58.977 56.738 1.00 31.49 ? 510 PRO A O 1 ATOM 3708 C CB . PRO A 1 517 ? 31.850 56.414 58.445 1.00 31.72 ? 510 PRO A CB 1 ATOM 3709 C CG . PRO A 1 517 ? 30.903 57.133 59.402 1.00 33.10 ? 510 PRO A CG 1 ATOM 3710 C CD . PRO A 1 517 ? 31.766 58.280 59.955 1.00 34.27 ? 510 PRO A CD 1 ATOM 3711 N N . ARG A 1 518 ? 31.952 57.427 55.442 1.00 29.23 ? 511 ARG A N 1 ATOM 3712 C CA . ARG A 1 518 ? 31.113 57.674 54.279 1.00 26.77 ? 511 ARG A CA 1 ATOM 3713 C C . ARG A 1 518 ? 29.680 57.166 54.496 1.00 26.44 ? 511 ARG A C 1 ATOM 3714 O O . ARG A 1 518 ? 29.460 55.997 54.820 1.00 26.31 ? 511 ARG A O 1 ATOM 3715 C CB . ARG A 1 518 ? 31.715 56.922 53.069 1.00 27.50 ? 511 ARG A CB 1 ATOM 3716 C CG . ARG A 1 518 ? 30.885 57.006 51.758 1.00 26.62 ? 511 ARG A CG 1 ATOM 3717 C CD . ARG A 1 518 ? 31.579 56.135 50.662 1.00 31.08 ? 511 ARG A CD 1 ATOM 3718 N NE . ARG A 1 518 ? 32.897 56.713 50.330 1.00 34.20 ? 511 ARG A NE 1 ATOM 3719 C CZ . ARG A 1 518 ? 33.084 57.694 49.436 1.00 36.08 ? 511 ARG A CZ 1 ATOM 3720 N NH1 . ARG A 1 518 ? 32.044 58.201 48.764 1.00 35.20 ? 511 ARG A NH1 1 ATOM 3721 N NH2 . ARG A 1 518 ? 34.312 58.168 49.200 1.00 36.13 ? 511 ARG A NH2 1 ATOM 3722 N N . ILE A 1 519 ? 28.705 58.019 54.249 1.00 25.60 ? 512 ILE A N 1 ATOM 3723 C CA . ILE A 1 519 ? 27.300 57.588 54.139 1.00 25.66 ? 512 ILE A CA 1 ATOM 3724 C C . ILE A 1 519 ? 26.788 58.120 52.793 1.00 25.52 ? 512 ILE A C 1 ATOM 3725 O O . ILE A 1 519 ? 26.907 59.329 52.502 1.00 26.53 ? 512 ILE A O 1 ATOM 3726 C CB . ILE A 1 519 ? 26.428 58.168 55.307 1.00 25.72 ? 512 ILE A CB 1 ATOM 3727 C CG1 . ILE A 1 519 ? 26.940 57.687 56.668 1.00 24.81 ? 512 ILE A CG1 1 ATOM 3728 C CG2 . ILE A 1 519 ? 24.876 57.853 55.081 1.00 24.65 ? 512 ILE A CG2 1 ATOM 3729 C CD1 . ILE A 1 519 ? 26.131 58.282 57.904 1.00 27.13 ? 512 ILE A CD1 1 ATOM 3730 N N . SER A 1 520 ? 26.226 57.251 51.977 1.00 23.63 ? 513 SER A N 1 ATOM 3731 C CA . SER A 1 520 ? 25.767 57.666 50.662 1.00 23.33 ? 513 SER A CA 1 ATOM 3732 C C . SER A 1 520 ? 24.295 58.092 50.674 1.00 22.30 ? 513 SER A C 1 ATOM 3733 O O . SER A 1 520 ? 23.530 57.753 51.608 1.00 21.52 ? 513 SER A O 1 ATOM 3734 C CB . SER A 1 520 ? 25.960 56.517 49.652 1.00 23.00 ? 513 SER A CB 1 ATOM 3735 O OG . SER A 1 520 ? 27.351 56.126 49.654 1.00 26.83 ? 513 SER A OG 1 ATOM 3736 N N A LYS A 1 521 ? 23.921 58.791 49.600 0.70 22.14 ? 514 LYS A N 1 ATOM 3737 N N B LYS A 1 521 ? 23.888 58.844 49.660 0.30 21.05 ? 514 LYS A N 1 ATOM 3738 C CA A LYS A 1 521 ? 22.533 59.183 49.297 0.70 22.64 ? 514 LYS A CA 1 ATOM 3739 C CA B LYS A 1 521 ? 22.481 59.210 49.520 0.30 19.97 ? 514 LYS A CA 1 ATOM 3740 C C A LYS A 1 521 ? 21.757 57.902 49.033 0.70 22.21 ? 514 LYS A C 1 ATOM 3741 C C B LYS A 1 521 ? 21.757 57.960 49.042 0.30 20.68 ? 514 LYS A C 1 ATOM 3742 O O A LYS A 1 521 ? 22.347 56.922 48.598 0.70 21.43 ? 514 LYS A O 1 ATOM 3743 O O B LYS A 1 521 ? 22.385 57.059 48.485 0.30 20.25 ? 514 LYS A O 1 ATOM 3744 C CB A LYS A 1 521 ? 22.523 60.015 47.999 0.70 22.34 ? 514 LYS A CB 1 ATOM 3745 C CB B LYS A 1 521 ? 22.333 60.315 48.484 0.30 18.99 ? 514 LYS A CB 1 ATOM 3746 C CG A LYS A 1 521 ? 23.270 61.341 48.131 0.70 25.60 ? 514 LYS A CG 1 ATOM 3747 C CG B LYS A 1 521 ? 22.682 59.868 47.074 0.30 14.59 ? 514 LYS A CG 1 ATOM 3748 C CD A LYS A 1 521 ? 22.856 62.353 47.039 0.70 27.82 ? 514 LYS A CD 1 ATOM 3749 C CD B LYS A 1 521 ? 22.727 61.066 46.140 0.30 12.58 ? 514 LYS A CD 1 ATOM 3750 C CE A LYS A 1 521 ? 23.338 61.916 45.689 0.70 29.37 ? 514 LYS A CE 1 ATOM 3751 C CE B LYS A 1 521 ? 23.832 62.059 46.540 0.30 10.67 ? 514 LYS A CE 1 ATOM 3752 N NZ A LYS A 1 521 ? 24.732 62.353 45.543 0.70 31.49 ? 514 LYS A NZ 1 ATOM 3753 N NZ B LYS A 1 521 ? 25.172 61.543 46.142 0.30 9.31 ? 514 LYS A NZ 1 ATOM 3754 N N . LEU A 1 522 ? 20.449 57.910 49.254 1.00 21.03 ? 515 LEU A N 1 ATOM 3755 C CA . LEU A 1 522 ? 19.634 56.792 48.812 1.00 22.34 ? 515 LEU A CA 1 ATOM 3756 C C . LEU A 1 522 ? 19.430 56.899 47.332 1.00 23.30 ? 515 LEU A C 1 ATOM 3757 O O . LEU A 1 522 ? 19.056 57.966 46.830 1.00 24.21 ? 515 LEU A O 1 ATOM 3758 C CB . LEU A 1 522 ? 18.248 56.824 49.466 1.00 21.15 ? 515 LEU A CB 1 ATOM 3759 C CG . LEU A 1 522 ? 18.315 56.296 50.912 1.00 20.77 ? 515 LEU A CG 1 ATOM 3760 C CD1 . LEU A 1 522 ? 17.032 56.769 51.594 1.00 21.60 ? 515 LEU A CD1 1 ATOM 3761 C CD2 . LEU A 1 522 ? 18.467 54.761 50.942 1.00 16.97 ? 515 LEU A CD2 1 ATOM 3762 N N . GLY A 1 523 ? 19.632 55.781 46.640 1.00 24.00 ? 516 GLY A N 1 ATOM 3763 C CA . GLY A 1 523 ? 19.269 55.707 45.227 1.00 23.35 ? 516 GLY A CA 1 ATOM 3764 C C . GLY A 1 523 ? 17.931 55.018 45.116 1.00 23.26 ? 516 GLY A C 1 ATOM 3765 O O . GLY A 1 523 ? 16.948 55.442 45.727 1.00 23.21 ? 516 GLY A O 1 ATOM 3766 N N . SER A 1 524 ? 17.889 53.955 44.295 1.00 21.52 ? 517 SER A N 1 ATOM 3767 C CA . SER A 1 524 ? 16.687 53.133 44.182 1.00 20.21 ? 517 SER A CA 1 ATOM 3768 C C . SER A 1 524 ? 16.997 51.680 43.760 1.00 19.28 ? 517 SER A C 1 ATOM 3769 O O . SER A 1 524 ? 18.144 51.244 43.922 1.00 20.40 ? 517 SER A O 1 ATOM 3770 C CB . SER A 1 524 ? 15.665 53.831 43.298 1.00 19.84 ? 517 SER A CB 1 ATOM 3771 O OG . SER A 1 524 ? 14.481 53.082 43.303 1.00 21.52 ? 517 SER A OG 1 ATOM 3772 N N . GLY A 1 525 ? 16.016 50.921 43.240 1.00 17.36 ? 518 GLY A N 1 ATOM 3773 C CA . GLY A 1 525 ? 16.257 49.502 42.944 1.00 16.93 ? 518 GLY A CA 1 ATOM 3774 C C . GLY A 1 525 ? 15.964 48.683 44.213 1.00 17.96 ? 518 GLY A C 1 ATOM 3775 O O . GLY A 1 525 ? 16.278 47.486 44.295 1.00 17.68 ? 518 GLY A O 1 ATOM 3776 N N . ASN A 1 526 ? 15.352 49.321 45.219 1.00 17.59 ? 519 ASN A N 1 ATOM 3777 C CA . ASN A 1 526 ? 14.959 48.567 46.434 1.00 17.83 ? 519 ASN A CA 1 ATOM 3778 C C . ASN A 1 526 ? 13.712 49.132 47.126 1.00 17.27 ? 519 ASN A C 1 ATOM 3779 O O . ASN A 1 526 ? 13.271 50.225 46.792 1.00 17.48 ? 519 ASN A O 1 ATOM 3780 C CB . ASN A 1 526 ? 16.151 48.372 47.390 1.00 18.89 ? 519 ASN A CB 1 ATOM 3781 C CG . ASN A 1 526 ? 16.254 46.926 47.864 1.00 21.72 ? 519 ASN A CG 1 ATOM 3782 O OD1 . ASN A 1 526 ? 15.338 46.417 48.594 1.00 24.08 ? 519 ASN A OD1 1 ATOM 3783 N ND2 . ASN A 1 526 ? 17.345 46.226 47.435 1.00 18.65 ? 519 ASN A ND2 1 ATOM 3784 N N . ASP A 1 527 ? 13.161 48.412 48.107 1.00 16.62 ? 520 ASP A N 1 ATOM 3785 C CA . ASP A 1 527 ? 11.773 48.649 48.559 1.00 15.26 ? 520 ASP A CA 1 ATOM 3786 C C . ASP A 1 527 ? 11.572 49.908 49.395 1.00 15.38 ? 520 ASP A C 1 ATOM 3787 O O . ASP A 1 527 ? 10.438 50.251 49.699 1.00 16.24 ? 520 ASP A O 1 ATOM 3788 C CB . ASP A 1 527 ? 11.252 47.428 49.365 1.00 15.24 ? 520 ASP A CB 1 ATOM 3789 C CG . ASP A 1 527 ? 10.915 46.226 48.453 1.00 16.12 ? 520 ASP A CG 1 ATOM 3790 O OD1 . ASP A 1 527 ? 10.107 46.414 47.513 1.00 15.43 ? 520 ASP A OD1 1 ATOM 3791 O OD2 . ASP A 1 527 ? 11.452 45.129 48.677 1.00 16.04 ? 520 ASP A OD2 1 ATOM 3792 N N . PHE A 1 528 ? 12.642 50.634 49.718 1.00 15.66 ? 521 PHE A N 1 ATOM 3793 C CA . PHE A 1 528 ? 12.464 51.974 50.324 1.00 16.59 ? 521 PHE A CA 1 ATOM 3794 C C . PHE A 1 528 ? 11.944 53.002 49.286 1.00 16.55 ? 521 PHE A C 1 ATOM 3795 O O . PHE A 1 528 ? 11.547 54.114 49.649 1.00 16.98 ? 521 PHE A O 1 ATOM 3796 C CB . PHE A 1 528 ? 13.801 52.491 50.917 1.00 16.00 ? 521 PHE A CB 1 ATOM 3797 C CG . PHE A 1 528 ? 14.918 52.544 49.924 1.00 18.42 ? 521 PHE A CG 1 ATOM 3798 C CD1 . PHE A 1 528 ? 15.026 53.619 49.019 1.00 19.55 ? 521 PHE A CD1 1 ATOM 3799 C CD2 . PHE A 1 528 ? 15.867 51.504 49.873 1.00 17.30 ? 521 PHE A CD2 1 ATOM 3800 C CE1 . PHE A 1 528 ? 16.066 53.640 48.051 1.00 19.31 ? 521 PHE A CE1 1 ATOM 3801 C CE2 . PHE A 1 528 ? 16.910 51.516 48.918 1.00 19.08 ? 521 PHE A CE2 1 ATOM 3802 C CZ . PHE A 1 528 ? 17.012 52.585 48.007 1.00 18.53 ? 521 PHE A CZ 1 ATOM 3803 N N . GLU A 1 529 ? 12.002 52.667 48.002 1.00 15.12 ? 522 GLU A N 1 ATOM 3804 C CA . GLU A 1 529 ? 11.711 53.669 46.974 1.00 15.34 ? 522 GLU A CA 1 ATOM 3805 C C . GLU A 1 529 ? 10.320 54.353 47.163 1.00 15.72 ? 522 GLU A C 1 ATOM 3806 O O . GLU A 1 529 ? 10.203 55.603 47.086 1.00 16.56 ? 522 GLU A O 1 ATOM 3807 C CB . GLU A 1 529 ? 11.795 53.090 45.536 1.00 13.98 ? 522 GLU A CB 1 ATOM 3808 C CG . GLU A 1 529 ? 11.620 54.229 44.434 1.00 15.58 ? 522 GLU A CG 1 ATOM 3809 C CD . GLU A 1 529 ? 11.451 53.631 43.035 1.00 18.59 ? 522 GLU A CD 1 ATOM 3810 O OE1 . GLU A 1 529 ? 10.456 52.935 42.804 1.00 22.11 ? 522 GLU A OE1 1 ATOM 3811 O OE2 . GLU A 1 529 ? 12.300 53.834 42.161 1.00 19.68 ? 522 GLU A OE2 1 ATOM 3812 N N . VAL A 1 530 ? 9.266 53.573 47.382 1.00 14.98 ? 523 VAL A N 1 ATOM 3813 C CA . VAL A 1 530 ? 7.944 54.217 47.497 1.00 14.87 ? 523 VAL A CA 1 ATOM 3814 C C . VAL A 1 530 ? 7.890 55.099 48.784 1.00 15.65 ? 523 VAL A C 1 ATOM 3815 O O . VAL A 1 530 ? 7.317 56.190 48.753 1.00 15.39 ? 523 VAL A O 1 ATOM 3816 C CB . VAL A 1 530 ? 6.754 53.186 47.471 1.00 15.48 ? 523 VAL A CB 1 ATOM 3817 C CG1 . VAL A 1 530 ? 6.777 52.230 48.748 1.00 14.74 ? 523 VAL A CG1 1 ATOM 3818 C CG2 . VAL A 1 530 ? 5.403 53.943 47.325 1.00 14.73 ? 523 VAL A CG2 1 ATOM 3819 N N . PHE A 1 531 ? 8.451 54.593 49.905 1.00 15.55 ? 524 PHE A N 1 ATOM 3820 C CA . PHE A 1 531 ? 8.421 55.320 51.176 1.00 15.76 ? 524 PHE A CA 1 ATOM 3821 C C . PHE A 1 531 ? 9.165 56.651 51.115 1.00 15.86 ? 524 PHE A C 1 ATOM 3822 O O . PHE A 1 531 ? 8.699 57.663 51.678 1.00 16.52 ? 524 PHE A O 1 ATOM 3823 C CB . PHE A 1 531 ? 9.010 54.413 52.293 1.00 16.70 ? 524 PHE A CB 1 ATOM 3824 C CG . PHE A 1 531 ? 8.181 53.161 52.455 1.00 18.04 ? 524 PHE A CG 1 ATOM 3825 C CD1 . PHE A 1 531 ? 6.946 53.229 53.128 1.00 19.79 ? 524 PHE A CD1 1 ATOM 3826 C CD2 . PHE A 1 531 ? 8.556 51.963 51.844 1.00 16.92 ? 524 PHE A CD2 1 ATOM 3827 C CE1 . PHE A 1 531 ? 6.115 52.081 53.243 1.00 19.71 ? 524 PHE A CE1 1 ATOM 3828 C CE2 . PHE A 1 531 ? 7.742 50.802 51.955 1.00 15.85 ? 524 PHE A CE2 1 ATOM 3829 C CZ . PHE A 1 531 ? 6.548 50.858 52.633 1.00 18.02 ? 524 PHE A CZ 1 ATOM 3830 N N . PHE A 1 532 ? 10.332 56.638 50.483 1.00 15.47 ? 525 PHE A N 1 ATOM 3831 C CA . PHE A 1 532 ? 11.230 57.831 50.447 1.00 15.51 ? 525 PHE A CA 1 ATOM 3832 C C . PHE A 1 532 ? 10.883 58.787 49.272 1.00 15.87 ? 525 PHE A C 1 ATOM 3833 O O . PHE A 1 532 ? 10.469 59.938 49.512 1.00 17.25 ? 525 PHE A O 1 ATOM 3834 C CB . PHE A 1 532 ? 12.720 57.368 50.379 1.00 14.76 ? 525 PHE A CB 1 ATOM 3835 C CG . PHE A 1 532 ? 13.686 58.481 50.609 1.00 15.46 ? 525 PHE A CG 1 ATOM 3836 C CD1 . PHE A 1 532 ? 13.638 59.199 51.841 1.00 15.73 ? 525 PHE A CD1 1 ATOM 3837 C CD2 . PHE A 1 532 ? 14.631 58.843 49.630 1.00 16.48 ? 525 PHE A CD2 1 ATOM 3838 C CE1 . PHE A 1 532 ? 14.541 60.248 52.112 1.00 17.16 ? 525 PHE A CE1 1 ATOM 3839 C CE2 . PHE A 1 532 ? 15.586 59.916 49.897 1.00 15.17 ? 525 PHE A CE2 1 ATOM 3840 C CZ . PHE A 1 532 ? 15.505 60.625 51.150 1.00 16.05 ? 525 PHE A CZ 1 ATOM 3841 N N A GLN A 1 533 ? 11.040 58.343 48.017 0.50 14.44 ? 526 GLN A N 1 ATOM 3842 N N B GLN A 1 533 ? 11.038 58.274 48.041 0.50 15.45 ? 526 GLN A N 1 ATOM 3843 C CA A GLN A 1 533 ? 10.883 59.285 46.889 0.50 13.44 ? 526 GLN A CA 1 ATOM 3844 C CA B GLN A 1 533 ? 10.900 59.067 46.816 0.50 15.53 ? 526 GLN A CA 1 ATOM 3845 C C A GLN A 1 533 ? 9.412 59.531 46.452 0.50 13.58 ? 526 GLN A C 1 ATOM 3846 C C B GLN A 1 533 ? 9.448 59.523 46.562 0.50 14.85 ? 526 GLN A C 1 ATOM 3847 O O A GLN A 1 533 ? 9.128 60.533 45.762 0.50 12.96 ? 526 GLN A O 1 ATOM 3848 O O B GLN A 1 533 ? 9.212 60.664 46.123 0.50 14.87 ? 526 GLN A O 1 ATOM 3849 C CB A GLN A 1 533 ? 11.735 58.858 45.673 0.50 13.07 ? 526 GLN A CB 1 ATOM 3850 C CB B GLN A 1 533 ? 11.413 58.244 45.609 0.50 15.77 ? 526 GLN A CB 1 ATOM 3851 C CG A GLN A 1 533 ? 13.250 58.881 45.872 0.50 11.13 ? 526 GLN A CG 1 ATOM 3852 C CG B GLN A 1 533 ? 12.796 57.598 45.830 0.50 17.85 ? 526 GLN A CG 1 ATOM 3853 C CD A GLN A 1 533 ? 13.852 57.527 46.284 0.50 8.64 ? 526 GLN A CD 1 ATOM 3854 C CD B GLN A 1 533 ? 13.876 58.648 45.937 0.50 20.51 ? 526 GLN A CD 1 ATOM 3855 O OE1 A GLN A 1 533 ? 13.180 56.715 46.881 0.50 7.87 ? 526 GLN A OE1 1 ATOM 3856 O OE1 B GLN A 1 533 ? 13.565 59.842 46.016 0.50 22.83 ? 526 GLN A OE1 1 ATOM 3857 N NE2 A GLN A 1 533 ? 15.149 57.309 45.973 0.50 8.49 ? 526 GLN A NE2 1 ATOM 3858 N NE2 B GLN A 1 533 ? 15.152 58.221 45.950 0.50 20.45 ? 526 GLN A NE2 1 ATOM 3859 N N . ARG A 1 534 ? 8.481 58.627 46.801 1.00 13.20 ? 527 ARG A N 1 ATOM 3860 C CA . ARG A 1 534 ? 7.072 58.969 46.572 1.00 13.75 ? 527 ARG A CA 1 ATOM 3861 C C . ARG A 1 534 ? 6.446 59.684 47.789 1.00 14.42 ? 527 ARG A C 1 ATOM 3862 O O . ARG A 1 534 ? 5.817 60.761 47.653 1.00 14.96 ? 527 ARG A O 1 ATOM 3863 C CB . ARG A 1 534 ? 6.179 57.766 46.127 1.00 13.54 ? 527 ARG A CB 1 ATOM 3864 C CG . ARG A 1 534 ? 4.815 58.320 45.570 1.00 12.39 ? 527 ARG A CG 1 ATOM 3865 C CD . ARG A 1 534 ? 3.735 57.230 45.489 1.00 14.12 ? 527 ARG A CD 1 ATOM 3866 N NE . ARG A 1 534 ? 4.057 56.166 44.524 1.00 14.09 ? 527 ARG A NE 1 ATOM 3867 C CZ . ARG A 1 534 ? 3.131 55.411 43.922 1.00 16.09 ? 527 ARG A CZ 1 ATOM 3868 N NH1 . ARG A 1 534 ? 1.806 55.653 44.101 1.00 14.22 ? 527 ARG A NH1 1 ATOM 3869 N NH2 . ARG A 1 534 ? 3.532 54.450 43.070 1.00 14.61 ? 527 ARG A NH2 1 ATOM 3870 N N . LEU A 1 535 ? 6.584 59.064 48.964 1.00 13.87 ? 528 LEU A N 1 ATOM 3871 C CA . LEU A 1 535 ? 5.844 59.517 50.165 1.00 14.76 ? 528 LEU A CA 1 ATOM 3872 C C . LEU A 1 535 ? 6.624 60.463 51.087 1.00 14.78 ? 528 LEU A C 1 ATOM 3873 O O . LEU A 1 535 ? 5.993 61.116 51.929 1.00 17.41 ? 528 LEU A O 1 ATOM 3874 C CB . LEU A 1 535 ? 5.329 58.306 50.991 1.00 14.38 ? 528 LEU A CB 1 ATOM 3875 C CG . LEU A 1 535 ? 4.360 57.379 50.227 1.00 13.53 ? 528 LEU A CG 1 ATOM 3876 C CD1 . LEU A 1 535 ? 3.897 56.247 51.183 1.00 13.38 ? 528 LEU A CD1 1 ATOM 3877 C CD2 . LEU A 1 535 ? 3.101 58.182 49.672 1.00 15.93 ? 528 LEU A CD2 1 ATOM 3878 N N . GLY A 1 536 ? 7.958 60.542 50.990 1.00 13.93 ? 529 GLY A N 1 ATOM 3879 C CA . GLY A 1 536 ? 8.702 61.523 51.843 1.00 13.01 ? 529 GLY A CA 1 ATOM 3880 C C . GLY A 1 536 ? 8.830 61.073 53.272 1.00 13.85 ? 529 GLY A C 1 ATOM 3881 O O . GLY A 1 536 ? 8.802 61.894 54.204 1.00 13.48 ? 529 GLY A O 1 ATOM 3882 N N . ILE A 1 537 ? 9.026 59.770 53.462 1.00 14.03 ? 530 ILE A N 1 ATOM 3883 C CA . ILE A 1 537 ? 9.243 59.232 54.800 1.00 14.32 ? 530 ILE A CA 1 ATOM 3884 C C . ILE A 1 537 ? 10.744 58.954 54.961 1.00 14.95 ? 530 ILE A C 1 ATOM 3885 O O . ILE A 1 537 ? 11.340 58.282 54.130 1.00 14.86 ? 530 ILE A O 1 ATOM 3886 C CB . ILE A 1 537 ? 8.427 57.933 54.990 1.00 14.21 ? 530 ILE A CB 1 ATOM 3887 C CG1 . ILE A 1 537 ? 6.921 58.257 54.931 1.00 15.20 ? 530 ILE A CG1 1 ATOM 3888 C CG2 . ILE A 1 537 ? 8.857 57.163 56.348 1.00 14.14 ? 530 ILE A CG2 1 ATOM 3889 C CD1 . ILE A 1 537 ? 6.048 56.965 54.783 1.00 15.91 ? 530 ILE A CD1 1 ATOM 3890 N N . ALA A 1 538 ? 11.366 59.520 55.997 1.00 15.11 ? 531 ALA A N 1 ATOM 3891 C CA . ALA A 1 538 ? 12.796 59.346 56.255 1.00 14.71 ? 531 ALA A CA 1 ATOM 3892 C C . ALA A 1 538 ? 13.157 57.887 56.157 1.00 16.36 ? 531 ALA A C 1 ATOM 3893 O O . ALA A 1 538 ? 12.540 57.054 56.855 1.00 15.85 ? 531 ALA A O 1 ATOM 3894 C CB . ALA A 1 538 ? 13.098 59.877 57.703 1.00 15.37 ? 531 ALA A CB 1 ATOM 3895 N N . SER A 1 539 ? 14.156 57.552 55.322 1.00 16.06 ? 532 SER A N 1 ATOM 3896 C CA . SER A 1 539 ? 14.459 56.151 55.070 1.00 16.04 ? 532 SER A CA 1 ATOM 3897 C C . SER A 1 539 ? 15.968 55.890 55.189 1.00 16.13 ? 532 SER A C 1 ATOM 3898 O O . SER A 1 539 ? 16.790 56.802 54.977 1.00 17.27 ? 532 SER A O 1 ATOM 3899 C CB . SER A 1 539 ? 13.930 55.762 53.664 1.00 15.07 ? 532 SER A CB 1 ATOM 3900 O OG . SER A 1 539 ? 12.493 55.795 53.598 1.00 16.60 ? 532 SER A OG 1 ATOM 3901 N N . GLY A 1 540 ? 16.339 54.646 55.485 1.00 16.83 ? 533 GLY A N 1 ATOM 3902 C CA . GLY A 1 540 ? 17.765 54.269 55.547 1.00 17.21 ? 533 GLY A CA 1 ATOM 3903 C C . GLY A 1 540 ? 17.951 52.774 55.248 1.00 18.60 ? 533 GLY A C 1 ATOM 3904 O O . GLY A 1 540 ? 16.973 51.982 55.287 1.00 18.50 ? 533 GLY A O 1 ATOM 3905 N N . ARG A 1 541 ? 19.196 52.376 54.982 1.00 18.40 ? 534 ARG A N 1 ATOM 3906 C CA . ARG A 1 541 ? 19.524 50.960 54.757 1.00 19.41 ? 534 ARG A CA 1 ATOM 3907 C C . ARG A 1 541 ? 20.981 50.788 55.176 1.00 19.93 ? 534 ARG A C 1 ATOM 3908 O O . ARG A 1 541 ? 21.767 51.772 55.142 1.00 18.99 ? 534 ARG A O 1 ATOM 3909 C CB . ARG A 1 541 ? 19.359 50.590 53.266 1.00 19.35 ? 534 ARG A CB 1 ATOM 3910 C CG . ARG A 1 541 ? 20.376 51.380 52.384 1.00 21.88 ? 534 ARG A CG 1 ATOM 3911 C CD . ARG A 1 541 ? 20.283 51.142 50.934 1.00 26.03 ? 534 ARG A CD 1 ATOM 3912 N NE . ARG A 1 541 ? 20.124 49.732 50.507 1.00 26.63 ? 534 ARG A NE 1 ATOM 3913 C CZ . ARG A 1 541 ? 20.062 49.397 49.224 1.00 26.34 ? 534 ARG A CZ 1 ATOM 3914 N NH1 . ARG A 1 541 ? 19.835 48.136 48.868 1.00 22.52 ? 534 ARG A NH1 1 ATOM 3915 N NH2 . ARG A 1 541 ? 20.231 50.357 48.290 1.00 25.19 ? 534 ARG A NH2 1 ATOM 3916 N N . ALA A 1 542 ? 21.354 49.551 55.529 1.00 19.60 ? 535 ALA A N 1 ATOM 3917 C CA . ALA A 1 542 ? 22.734 49.263 55.922 1.00 19.80 ? 535 ALA A CA 1 ATOM 3918 C C . ALA A 1 542 ? 23.042 47.801 55.595 1.00 20.03 ? 535 ALA A C 1 ATOM 3919 O O . ALA A 1 542 ? 22.154 46.936 55.652 1.00 19.47 ? 535 ALA A O 1 ATOM 3920 C CB . ALA A 1 542 ? 22.950 49.510 57.446 1.00 18.87 ? 535 ALA A CB 1 ATOM 3921 N N . ARG A 1 543 ? 24.306 47.527 55.274 1.00 20.51 ? 536 ARG A N 1 ATOM 3922 C CA . ARG A 1 543 ? 24.739 46.142 54.988 1.00 20.78 ? 536 ARG A CA 1 ATOM 3923 C C . ARG A 1 543 ? 26.248 46.116 55.069 1.00 21.84 ? 536 ARG A C 1 ATOM 3924 O O . ARG A 1 543 ? 26.881 47.180 55.084 1.00 21.64 ? 536 ARG A O 1 ATOM 3925 C CB . ARG A 1 543 ? 24.266 45.698 53.577 1.00 21.77 ? 536 ARG A CB 1 ATOM 3926 C CG . ARG A 1 543 ? 24.809 46.527 52.391 1.00 20.77 ? 536 ARG A CG 1 ATOM 3927 C CD . ARG A 1 543 ? 24.561 45.782 51.097 1.00 20.95 ? 536 ARG A CD 1 ATOM 3928 N NE . ARG A 1 543 ? 23.106 45.536 50.937 1.00 20.97 ? 536 ARG A NE 1 ATOM 3929 C CZ . ARG A 1 543 ? 22.452 45.503 49.783 1.00 21.39 ? 536 ARG A CZ 1 ATOM 3930 N NH1 . ARG A 1 543 ? 23.092 45.696 48.620 1.00 21.64 ? 536 ARG A NH1 1 ATOM 3931 N NH2 . ARG A 1 543 ? 21.141 45.279 49.791 1.00 19.97 ? 536 ARG A NH2 1 ATOM 3932 N N . TYR A 1 544 ? 26.824 44.920 55.162 1.00 21.51 ? 537 TYR A N 1 ATOM 3933 C CA . TYR A 1 544 ? 28.249 44.778 54.958 1.00 22.46 ? 537 TYR A CA 1 ATOM 3934 C C . TYR A 1 544 ? 28.574 44.703 53.459 1.00 23.30 ? 537 TYR A C 1 ATOM 3935 O O . TYR A 1 544 ? 27.776 44.163 52.663 1.00 21.68 ? 537 TYR A O 1 ATOM 3936 C CB . TYR A 1 544 ? 28.824 43.564 55.722 1.00 21.35 ? 537 TYR A CB 1 ATOM 3937 C CG . TYR A 1 544 ? 29.746 44.067 56.809 1.00 22.21 ? 537 TYR A CG 1 ATOM 3938 C CD1 . TYR A 1 544 ? 29.246 44.849 57.856 1.00 22.96 ? 537 TYR A CD1 1 ATOM 3939 C CD2 . TYR A 1 544 ? 31.131 43.830 56.756 1.00 21.60 ? 537 TYR A CD2 1 ATOM 3940 C CE1 . TYR A 1 544 ? 30.107 45.366 58.867 1.00 21.69 ? 537 TYR A CE1 1 ATOM 3941 C CE2 . TYR A 1 544 ? 31.989 44.335 57.752 1.00 20.96 ? 537 TYR A CE2 1 ATOM 3942 C CZ . TYR A 1 544 ? 31.461 45.092 58.804 1.00 21.57 ? 537 TYR A CZ 1 ATOM 3943 O OH . TYR A 1 544 ? 32.294 45.600 59.772 1.00 21.45 ? 537 TYR A OH 1 ATOM 3944 N N . THR A 1 545 ? 29.741 45.249 53.097 1.00 24.37 ? 538 THR A N 1 ATOM 3945 C CA . THR A 1 545 ? 30.098 45.440 51.688 1.00 25.22 ? 538 THR A CA 1 ATOM 3946 C C . THR A 1 545 ? 31.600 45.144 51.469 1.00 26.69 ? 538 THR A C 1 ATOM 3947 O O . THR A 1 545 ? 32.348 44.916 52.428 1.00 26.26 ? 538 THR A O 1 ATOM 3948 C CB . THR A 1 545 ? 29.759 46.890 51.208 1.00 24.86 ? 538 THR A CB 1 ATOM 3949 O OG1 . THR A 1 545 ? 29.829 46.961 49.769 1.00 25.56 ? 538 THR A OG1 1 ATOM 3950 C CG2 . THR A 1 545 ? 30.760 47.909 51.834 1.00 24.41 ? 538 THR A CG2 1 ATOM 3951 N N . LYS A 1 546 ? 32.024 45.183 50.204 1.00 28.27 ? 539 LYS A N 1 ATOM 3952 C CA . LYS A 1 546 ? 33.428 44.929 49.830 1.00 30.11 ? 539 LYS A CA 1 ATOM 3953 C C . LYS A 1 546 ? 34.256 46.212 49.899 1.00 30.77 ? 539 LYS A C 1 ATOM 3954 O O . LYS A 1 546 ? 33.726 47.281 50.171 1.00 28.62 ? 539 LYS A O 1 ATOM 3955 C CB . LYS A 1 546 ? 33.513 44.315 48.412 1.00 31.19 ? 539 LYS A CB 1 ATOM 3956 C CG . LYS A 1 546 ? 32.988 45.242 47.337 1.00 33.29 ? 539 LYS A CG 1 ATOM 3957 C CD . LYS A 1 546 ? 33.194 44.692 45.915 1.00 38.51 ? 539 LYS A CD 1 ATOM 3958 C CE . LYS A 1 546 ? 32.310 45.548 44.984 1.00 42.63 ? 539 LYS A CE 1 ATOM 3959 N NZ . LYS A 1 546 ? 31.968 44.939 43.699 0.65 45.01 ? 539 LYS A NZ 1 ATOM 3960 N N . ASN A 1 547 ? 35.553 46.093 49.670 1.00 33.12 ? 540 ASN A N 1 ATOM 3961 C CA . ASN A 1 547 ? 36.453 47.250 49.547 1.00 37.31 ? 540 ASN A CA 1 ATOM 3962 C C . ASN A 1 547 ? 36.277 47.875 48.151 1.00 40.37 ? 540 ASN A C 1 ATOM 3963 O O . ASN A 1 547 ? 36.800 47.320 47.169 1.00 41.34 ? 540 ASN A O 1 ATOM 3964 C CB . ASN A 1 547 ? 37.920 46.768 49.736 1.00 36.71 ? 540 ASN A CB 1 ATOM 3965 C CG . ASN A 1 547 ? 38.935 47.937 49.772 1.00 37.15 ? 540 ASN A CG 1 ATOM 3966 O OD1 . ASN A 1 547 ? 38.670 49.047 49.266 1.00 37.70 ? 540 ASN A OD1 1 ATOM 3967 N ND2 . ASN A 1 547 ? 40.091 47.689 50.394 1.00 37.76 ? 540 ASN A ND2 1 ATOM 3968 N N A TRP A 1 548 ? 35.542 48.983 48.064 0.30 42.23 ? 541 TRP A N 1 ATOM 3969 N N B TRP A 1 548 ? 35.561 48.999 48.063 0.70 42.04 ? 541 TRP A N 1 ATOM 3970 C CA A TRP A 1 548 ? 35.321 49.723 46.809 0.30 44.52 ? 541 TRP A CA 1 ATOM 3971 C CA B TRP A 1 548 ? 35.294 49.688 46.778 0.70 44.60 ? 541 TRP A CA 1 ATOM 3972 C C A TRP A 1 548 ? 36.642 50.023 46.082 0.30 46.55 ? 541 TRP A C 1 ATOM 3973 C C B TRP A 1 548 ? 36.510 50.408 46.137 0.70 46.86 ? 541 TRP A C 1 ATOM 3974 O O A TRP A 1 548 ? 36.759 49.827 44.863 0.30 46.59 ? 541 TRP A O 1 ATOM 3975 O O B TRP A 1 548 ? 36.415 50.895 45.001 0.70 47.51 ? 541 TRP A O 1 ATOM 3976 C CB A TRP A 1 548 ? 34.582 51.036 47.120 0.30 44.25 ? 541 TRP A CB 1 ATOM 3977 C CB B TRP A 1 548 ? 34.046 50.596 46.865 0.70 44.28 ? 541 TRP A CB 1 ATOM 3978 C CG A TRP A 1 548 ? 34.077 51.847 45.932 0.30 44.07 ? 541 TRP A CG 1 ATOM 3979 C CG B TRP A 1 548 ? 32.793 49.763 46.989 0.70 43.88 ? 541 TRP A CG 1 ATOM 3980 C CD1 A TRP A 1 548 ? 32.801 51.866 45.437 0.20 43.84 ? 541 TRP A CD1 1 ATOM 3981 C CD1 B TRP A 1 548 ? 32.225 49.303 48.157 0.70 42.50 ? 541 TRP A CD1 1 ATOM 3982 C CD2 A TRP A 1 548 ? 34.822 52.791 45.144 0.20 43.68 ? 541 TRP A CD2 1 ATOM 3983 C CD2 B TRP A 1 548 ? 32.014 49.199 45.914 0.40 42.90 ? 541 TRP A CD2 1 ATOM 3984 N NE1 A TRP A 1 548 ? 32.713 52.743 44.380 0.30 43.89 ? 541 TRP A NE1 1 ATOM 3985 N NE1 B TRP A 1 548 ? 31.126 48.535 47.867 0.70 43.18 ? 541 TRP A NE1 1 ATOM 3986 C CE2 A TRP A 1 548 ? 33.939 53.322 44.180 0.30 43.78 ? 541 TRP A CE2 1 ATOM 3987 C CE2 B TRP A 1 548 ? 30.977 48.446 46.504 0.40 42.93 ? 541 TRP A CE2 1 ATOM 3988 C CE3 A TRP A 1 548 ? 36.151 53.224 45.149 0.20 43.79 ? 541 TRP A CE3 1 ATOM 3989 C CE3 B TRP A 1 548 ? 32.085 49.274 44.517 0.40 42.11 ? 541 TRP A CE3 1 ATOM 3990 C CZ2 A TRP A 1 548 ? 34.343 54.262 43.232 0.30 44.01 ? 541 TRP A CZ2 1 ATOM 3991 C CZ2 B TRP A 1 548 ? 30.004 47.779 45.739 0.40 41.94 ? 541 TRP A CZ2 1 ATOM 3992 C CZ3 A TRP A 1 548 ? 36.550 54.163 44.208 0.30 44.30 ? 541 TRP A CZ3 1 ATOM 3993 C CZ3 B TRP A 1 548 ? 31.121 48.619 43.764 0.40 41.70 ? 541 TRP A CZ3 1 ATOM 3994 C CH2 A TRP A 1 548 ? 35.649 54.667 43.261 0.30 44.05 ? 541 TRP A CH2 1 ATOM 3995 C CH2 B TRP A 1 548 ? 30.097 47.880 44.375 0.40 41.19 ? 541 TRP A CH2 1 ATOM 3996 N N . GLU A 1 549 ? 37.637 50.455 46.858 1.00 48.64 ? 542 GLU A N 1 ATOM 3997 C CA . GLU A 1 549 ? 38.912 50.973 46.334 1.00 51.85 ? 542 GLU A CA 1 ATOM 3998 C C . GLU A 1 549 ? 39.716 49.900 45.604 1.00 54.28 ? 542 GLU A C 1 ATOM 3999 O O . GLU A 1 549 ? 40.339 50.168 44.565 1.00 55.27 ? 542 GLU A O 1 ATOM 4000 C CB . GLU A 1 549 ? 39.760 51.576 47.470 1.00 52.78 ? 542 GLU A CB 1 ATOM 4001 C CG . GLU A 1 549 ? 39.024 52.632 48.333 1.00 53.89 ? 542 GLU A CG 1 ATOM 4002 C CD . GLU A 1 549 ? 39.066 54.046 47.727 1.00 56.33 ? 542 GLU A CD 1 ATOM 4003 O OE1 . GLU A 1 549 ? 40.106 54.413 47.137 0.50 56.44 ? 542 GLU A OE1 1 ATOM 4004 O OE2 . GLU A 1 549 ? 38.065 54.794 47.856 0.50 56.02 ? 542 GLU A OE2 1 ATOM 4005 N N . THR A 1 550 ? 39.712 48.680 46.131 1.00 55.85 ? 543 THR A N 1 ATOM 4006 C CA . THR A 1 550 ? 40.573 47.649 45.556 1.00 57.01 ? 543 THR A CA 1 ATOM 4007 C C . THR A 1 550 ? 39.788 46.660 44.692 1.00 57.24 ? 543 THR A C 1 ATOM 4008 O O . THR A 1 550 ? 40.375 45.928 43.897 1.00 57.53 ? 543 THR A O 1 ATOM 4009 C CB . THR A 1 550 ? 41.442 46.913 46.641 1.00 57.53 ? 543 THR A CB 1 ATOM 4010 O OG1 . THR A 1 550 ? 40.591 46.203 47.560 1.00 58.21 ? 543 THR A OG1 1 ATOM 4011 C CG2 . THR A 1 550 ? 42.364 47.917 47.405 1.00 57.24 ? 543 THR A CG2 1 ATOM 4012 N N . ASN A 1 551 ? 38.466 46.638 44.843 1.00 57.10 ? 544 ASN A N 1 ATOM 4013 C CA . ASN A 1 551 ? 37.624 45.694 44.083 1.00 57.08 ? 544 ASN A CA 1 ATOM 4014 C C . ASN A 1 551 ? 36.813 46.435 43.016 1.00 57.27 ? 544 ASN A C 1 ATOM 4015 O O . ASN A 1 551 ? 35.803 47.104 43.327 1.00 57.62 ? 544 ASN A O 1 ATOM 4016 C CB . ASN A 1 551 ? 36.703 44.848 44.993 1.00 56.38 ? 544 ASN A CB 1 ATOM 4017 C CG . ASN A 1 551 ? 37.456 44.134 46.127 0.75 55.78 ? 544 ASN A CG 1 ATOM 4018 O OD1 . ASN A 1 551 ? 36.966 44.063 47.258 0.40 53.58 ? 544 ASN A OD1 1 ATOM 4019 N ND2 . ASN A 1 551 ? 38.647 43.605 45.826 0.75 54.37 ? 544 ASN A ND2 1 ATOM 4020 N N . LYS A 1 552 ? 37.268 46.285 41.768 1.00 57.08 ? 545 LYS A N 1 ATOM 4021 C CA . LYS A 1 552 ? 36.725 46.996 40.598 1.00 56.69 ? 545 LYS A CA 1 ATOM 4022 C C . LYS A 1 552 ? 35.508 46.291 39.921 1.00 56.01 ? 545 LYS A C 1 ATOM 4023 O O . LYS A 1 552 ? 34.835 46.891 39.057 1.00 56.78 ? 545 LYS A O 1 ATOM 4024 C CB . LYS A 1 552 ? 37.854 47.266 39.582 0.70 57.03 ? 545 LYS A CB 1 ATOM 4025 C CG . LYS A 1 552 ? 39.101 47.928 40.192 0.40 56.99 ? 545 LYS A CG 1 ATOM 4026 C CD . LYS A 1 552 ? 40.277 47.934 39.221 0.20 57.54 ? 545 LYS A CD 1 ATOM 4027 C CE . LYS A 1 552 ? 39.967 48.749 37.976 0.20 57.38 ? 545 LYS A CE 1 ATOM 4028 N NZ . LYS A 1 552 ? 41.128 48.791 37.050 0.20 57.09 ? 545 LYS A NZ 1 ATOM 4029 N N . PHE A 1 553 ? 35.214 45.043 40.316 1.00 54.24 ? 546 PHE A N 1 ATOM 4030 C CA . PHE A 1 553 ? 33.969 44.358 39.881 1.00 51.65 ? 546 PHE A CA 1 ATOM 4031 C C . PHE A 1 553 ? 32.656 45.005 40.449 1.00 50.42 ? 546 PHE A C 1 ATOM 4032 O O . PHE A 1 553 ? 32.707 45.857 41.366 1.00 49.67 ? 546 PHE A O 1 ATOM 4033 C CB . PHE A 1 553 ? 34.050 42.845 40.137 1.00 51.57 ? 546 PHE A CB 1 ATOM 4034 C CG . PHE A 1 553 ? 34.296 42.464 41.570 1.00 50.23 ? 546 PHE A CG 1 ATOM 4035 C CD1 . PHE A 1 553 ? 35.609 42.365 42.067 0.50 49.53 ? 546 PHE A CD1 1 ATOM 4036 C CD2 . PHE A 1 553 ? 33.224 42.170 42.418 1.00 48.39 ? 546 PHE A CD2 1 ATOM 4037 C CE1 . PHE A 1 553 ? 35.848 42.000 43.396 0.50 47.86 ? 546 PHE A CE1 1 ATOM 4038 C CE2 . PHE A 1 553 ? 33.444 41.802 43.748 1.00 47.21 ? 546 PHE A CE2 1 ATOM 4039 C CZ . PHE A 1 553 ? 34.765 41.720 44.240 0.50 47.68 ? 546 PHE A CZ 1 ATOM 4040 N N . SER A 1 554 ? 31.493 44.642 39.897 0.75 48.27 ? 547 SER A N 1 ATOM 4041 C CA . SER A 1 554 ? 30.254 45.292 40.364 0.75 46.84 ? 547 SER A CA 1 ATOM 4042 C C . SER A 1 554 ? 29.359 44.406 41.235 0.75 44.13 ? 547 SER A C 1 ATOM 4043 O O . SER A 1 554 ? 29.121 43.234 40.917 1.00 43.88 ? 547 SER A O 1 ATOM 4044 C CB . SER A 1 554 ? 29.471 45.924 39.216 1.00 47.84 ? 547 SER A CB 1 ATOM 4045 O OG . SER A 1 554 ? 29.229 44.980 38.211 1.00 50.29 ? 547 SER A OG 1 ATOM 4046 N N . GLY A 1 555 ? 28.891 44.989 42.341 1.00 41.43 ? 548 GLY A N 1 ATOM 4047 C CA . GLY A 1 555 ? 28.137 44.279 43.394 1.00 37.08 ? 548 GLY A CA 1 ATOM 4048 C C . GLY A 1 555 ? 28.904 43.041 43.802 0.65 34.43 ? 548 GLY A C 1 ATOM 4049 O O . GLY A 1 555 ? 30.103 43.112 43.989 0.65 33.72 ? 548 GLY A O 1 ATOM 4050 N N . TYR A 1 556 ? 28.222 41.896 43.898 1.00 31.78 ? 549 TYR A N 1 ATOM 4051 C CA . TYR A 1 556 ? 28.918 40.611 44.100 1.00 28.82 ? 549 TYR A CA 1 ATOM 4052 C C . TYR A 1 556 ? 28.753 39.683 42.849 1.00 26.29 ? 549 TYR A C 1 ATOM 4053 O O . TYR A 1 556 ? 27.721 39.732 42.199 1.00 26.98 ? 549 TYR A O 1 ATOM 4054 C CB . TYR A 1 556 ? 28.382 39.970 45.391 1.00 28.69 ? 549 TYR A CB 1 ATOM 4055 C CG . TYR A 1 556 ? 26.882 39.719 45.428 1.00 26.50 ? 549 TYR A CG 1 ATOM 4056 C CD1 . TYR A 1 556 ? 26.372 38.440 45.189 1.00 25.47 ? 549 TYR A CD1 1 ATOM 4057 C CD2 . TYR A 1 556 ? 25.967 40.769 45.709 1.00 23.84 ? 549 TYR A CD2 1 ATOM 4058 C CE1 . TYR A 1 556 ? 24.984 38.198 45.218 1.00 21.57 ? 549 TYR A CE1 1 ATOM 4059 C CE2 . TYR A 1 556 ? 24.592 40.531 45.741 1.00 23.12 ? 549 TYR A CE2 1 ATOM 4060 C CZ . TYR A 1 556 ? 24.115 39.242 45.512 1.00 19.87 ? 549 TYR A CZ 1 ATOM 4061 O OH . TYR A 1 556 ? 22.754 38.990 45.524 1.00 21.30 ? 549 TYR A OH 1 ATOM 4062 N N . PRO A 1 557 ? 29.747 38.844 42.526 1.00 24.54 ? 550 PRO A N 1 ATOM 4063 C CA . PRO A 1 557 ? 29.660 38.133 41.218 1.00 23.02 ? 550 PRO A CA 1 ATOM 4064 C C . PRO A 1 557 ? 28.420 37.257 40.995 1.00 21.46 ? 550 PRO A C 1 ATOM 4065 O O . PRO A 1 557 ? 27.950 37.130 39.848 1.00 21.55 ? 550 PRO A O 1 ATOM 4066 C CB . PRO A 1 557 ? 30.921 37.246 41.221 1.00 22.20 ? 550 PRO A CB 1 ATOM 4067 C CG . PRO A 1 557 ? 31.926 38.063 42.026 1.00 23.22 ? 550 PRO A CG 1 ATOM 4068 C CD . PRO A 1 557 ? 31.102 38.702 43.142 1.00 23.59 ? 550 PRO A CD 1 ATOM 4069 N N . LEU A 1 558 ? 27.922 36.623 42.051 1.00 19.61 ? 551 LEU A N 1 ATOM 4070 C CA . LEU A 1 558 ? 26.876 35.554 41.909 1.00 19.28 ? 551 LEU A CA 1 ATOM 4071 C C . LEU A 1 558 ? 25.456 36.120 42.000 1.00 19.35 ? 551 LEU A C 1 ATOM 4072 O O . LEU A 1 558 ? 24.455 35.374 41.996 1.00 19.55 ? 551 LEU A O 1 ATOM 4073 C CB . LEU A 1 558 ? 27.087 34.454 42.949 1.00 18.29 ? 551 LEU A CB 1 ATOM 4074 C CG . LEU A 1 558 ? 28.394 33.729 42.549 1.00 17.74 ? 551 LEU A CG 1 ATOM 4075 C CD1 . LEU A 1 558 ? 28.784 32.682 43.587 1.00 19.21 ? 551 LEU A CD1 1 ATOM 4076 C CD2 . LEU A 1 558 ? 28.318 33.075 41.134 1.00 16.27 ? 551 LEU A CD2 1 ATOM 4077 N N . TYR A 1 559 ? 25.378 37.443 42.098 1.00 18.85 ? 552 TYR A N 1 ATOM 4078 C CA . TYR A 1 559 ? 24.099 38.165 42.094 1.00 19.34 ? 552 TYR A CA 1 ATOM 4079 C C . TYR A 1 559 ? 23.049 37.624 41.092 1.00 19.30 ? 552 TYR A C 1 ATOM 4080 O O . TYR A 1 559 ? 23.291 37.628 39.872 1.00 20.46 ? 552 TYR A O 1 ATOM 4081 C CB . TYR A 1 559 ? 24.402 39.641 41.839 1.00 18.73 ? 552 TYR A CB 1 ATOM 4082 C CG . TYR A 1 559 ? 23.216 40.577 41.589 1.00 20.25 ? 552 TYR A CG 1 ATOM 4083 C CD1 . TYR A 1 559 ? 22.309 40.915 42.615 1.00 19.08 ? 552 TYR A CD1 1 ATOM 4084 C CD2 . TYR A 1 559 ? 23.065 41.196 40.333 1.00 19.26 ? 552 TYR A CD2 1 ATOM 4085 C CE1 . TYR A 1 559 ? 21.236 41.857 42.378 1.00 17.28 ? 552 TYR A CE1 1 ATOM 4086 C CE2 . TYR A 1 559 ? 22.055 42.100 40.085 1.00 16.98 ? 552 TYR A CE2 1 ATOM 4087 C CZ . TYR A 1 559 ? 21.136 42.422 41.096 1.00 17.97 ? 552 TYR A CZ 1 ATOM 4088 O OH . TYR A 1 559 ? 20.133 43.305 40.773 1.00 18.44 ? 552 TYR A OH 1 ATOM 4089 N N . HIS A 1 560 ? 21.888 37.187 41.596 1.00 18.88 ? 553 HIS A N 1 ATOM 4090 C CA . HIS A 1 560 ? 20.711 36.783 40.747 1.00 18.77 ? 553 HIS A CA 1 ATOM 4091 C C . HIS A 1 560 ? 20.959 35.540 39.882 1.00 19.79 ? 553 HIS A C 1 ATOM 4092 O O . HIS A 1 560 ? 20.229 35.301 38.898 1.00 19.76 ? 553 HIS A O 1 ATOM 4093 C CB . HIS A 1 560 ? 20.184 37.933 39.830 1.00 16.97 ? 553 HIS A CB 1 ATOM 4094 C CG . HIS A 1 560 ? 19.440 39.023 40.559 1.00 16.06 ? 553 HIS A CG 1 ATOM 4095 N ND1 . HIS A 1 560 ? 18.840 40.066 39.888 1.00 16.42 ? 553 HIS A ND1 1 ATOM 4096 C CD2 . HIS A 1 560 ? 19.170 39.221 41.883 1.00 16.30 ? 553 HIS A CD2 1 ATOM 4097 C CE1 . HIS A 1 560 ? 18.239 40.872 40.759 1.00 16.44 ? 553 HIS A CE1 1 ATOM 4098 N NE2 . HIS A 1 560 ? 18.400 40.368 41.973 1.00 17.36 ? 553 HIS A NE2 1 ATOM 4099 N N . SER A 1 561 ? 21.951 34.741 40.276 1.00 20.31 ? 554 SER A N 1 ATOM 4100 C CA . SER A 1 561 ? 22.289 33.508 39.596 1.00 19.35 ? 554 SER A CA 1 ATOM 4101 C C . SER A 1 561 ? 21.843 32.301 40.501 1.00 20.91 ? 554 SER A C 1 ATOM 4102 O O . SER A 1 561 ? 21.600 32.474 41.713 1.00 19.47 ? 554 SER A O 1 ATOM 4103 C CB . SER A 1 561 ? 23.798 33.445 39.308 1.00 19.56 ? 554 SER A CB 1 ATOM 4104 O OG A SER A 1 561 ? 24.555 33.272 40.481 0.50 21.25 ? 554 SER A OG 1 ATOM 4105 O OG B SER A 1 561 ? 24.269 32.094 39.180 0.50 18.55 ? 554 SER A OG 1 ATOM 4106 N N . VAL A 1 562 ? 21.705 31.133 39.878 1.00 19.05 ? 555 VAL A N 1 ATOM 4107 C CA . VAL A 1 562 ? 21.366 29.885 40.608 1.00 19.97 ? 555 VAL A CA 1 ATOM 4108 C C . VAL A 1 562 ? 22.421 29.606 41.721 1.00 20.40 ? 555 VAL A C 1 ATOM 4109 O O . VAL A 1 562 ? 22.129 28.878 42.685 1.00 21.54 ? 555 VAL A O 1 ATOM 4110 C CB . VAL A 1 562 ? 21.298 28.690 39.647 1.00 18.60 ? 555 VAL A CB 1 ATOM 4111 C CG1 . VAL A 1 562 ? 22.754 28.262 39.190 1.00 17.46 ? 555 VAL A CG1 1 ATOM 4112 C CG2 . VAL A 1 562 ? 20.625 27.457 40.293 1.00 19.36 ? 555 VAL A CG2 1 ATOM 4113 N N . TYR A 1 563 ? 23.616 30.206 41.605 1.00 20.23 ? 556 TYR A N 1 ATOM 4114 C CA . TYR A 1 563 ? 24.759 29.858 42.491 1.00 20.92 ? 556 TYR A CA 1 ATOM 4115 C C . TYR A 1 563 ? 24.702 30.613 43.812 1.00 21.57 ? 556 TYR A C 1 ATOM 4116 O O . TYR A 1 563 ? 25.531 30.339 44.726 1.00 21.66 ? 556 TYR A O 1 ATOM 4117 C CB . TYR A 1 563 ? 26.146 30.067 41.816 1.00 19.41 ? 556 TYR A CB 1 ATOM 4118 C CG . TYR A 1 563 ? 26.237 29.273 40.536 1.00 21.07 ? 556 TYR A CG 1 ATOM 4119 C CD1 . TYR A 1 563 ? 26.197 27.852 40.565 1.00 20.27 ? 556 TYR A CD1 1 ATOM 4120 C CD2 . TYR A 1 563 ? 26.302 29.908 39.304 1.00 20.01 ? 556 TYR A CD2 1 ATOM 4121 C CE1 . TYR A 1 563 ? 26.241 27.099 39.402 1.00 21.36 ? 556 TYR A CE1 1 ATOM 4122 C CE2 . TYR A 1 563 ? 26.370 29.135 38.096 1.00 22.78 ? 556 TYR A CE2 1 ATOM 4123 C CZ . TYR A 1 563 ? 26.312 27.756 38.162 1.00 21.67 ? 556 TYR A CZ 1 ATOM 4124 O OH . TYR A 1 563 ? 26.315 27.014 37.005 1.00 22.91 ? 556 TYR A OH 1 ATOM 4125 N N . GLU A 1 564 ? 23.751 31.547 43.915 1.00 20.61 ? 557 GLU A N 1 ATOM 4126 C CA . GLU A 1 564 ? 23.594 32.321 45.145 1.00 21.20 ? 557 GLU A CA 1 ATOM 4127 C C . GLU A 1 564 ? 22.821 31.461 46.189 1.00 21.02 ? 557 GLU A C 1 ATOM 4128 O O . GLU A 1 564 ? 21.576 31.449 46.209 1.00 20.83 ? 557 GLU A O 1 ATOM 4129 C CB . GLU A 1 564 ? 22.837 33.603 44.780 1.00 22.25 ? 557 GLU A CB 1 ATOM 4130 C CG . GLU A 1 564 ? 23.185 34.730 45.614 1.00 24.34 ? 557 GLU A CG 1 ATOM 4131 C CD . GLU A 1 564 ? 22.096 35.771 45.563 1.00 21.73 ? 557 GLU A CD 1 ATOM 4132 O OE1 . GLU A 1 564 ? 22.008 36.565 44.605 1.00 24.32 ? 557 GLU A OE1 1 ATOM 4133 O OE2 . GLU A 1 564 ? 21.317 35.771 46.495 1.00 22.74 ? 557 GLU A OE2 1 ATOM 4134 N N . THR A 1 565 ? 23.552 30.694 46.998 1.00 20.91 ? 558 THR A N 1 ATOM 4135 C CA . THR A 1 565 ? 22.970 29.634 47.816 1.00 21.02 ? 558 THR A CA 1 ATOM 4136 C C . THR A 1 565 ? 23.332 29.895 49.316 1.00 21.08 ? 558 THR A C 1 ATOM 4137 O O . THR A 1 565 ? 24.196 30.723 49.621 1.00 20.46 ? 558 THR A O 1 ATOM 4138 C CB . THR A 1 565 ? 23.570 28.259 47.438 1.00 21.52 ? 558 THR A CB 1 ATOM 4139 O OG1 . THR A 1 565 ? 24.999 28.367 47.507 1.00 22.52 ? 558 THR A OG1 1 ATOM 4140 C CG2 . THR A 1 565 ? 23.168 27.773 46.006 1.00 20.75 ? 558 THR A CG2 1 ATOM 4141 N N . TYR A 1 566 ? 22.703 29.156 50.230 1.00 21.04 ? 559 TYR A N 1 ATOM 4142 C CA . TYR A 1 566 ? 23.162 29.101 51.603 1.00 22.22 ? 559 TYR A CA 1 ATOM 4143 C C . TYR A 1 566 ? 24.692 28.806 51.667 1.00 22.26 ? 559 TYR A C 1 ATOM 4144 O O . TYR A 1 566 ? 25.424 29.475 52.406 1.00 22.17 ? 559 TYR A O 1 ATOM 4145 C CB . TYR A 1 566 ? 22.401 28.022 52.388 1.00 22.23 ? 559 TYR A CB 1 ATOM 4146 C CG . TYR A 1 566 ? 22.949 27.806 53.786 1.00 23.59 ? 559 TYR A CG 1 ATOM 4147 C CD1 . TYR A 1 566 ? 22.604 28.675 54.823 1.00 24.57 ? 559 TYR A CD1 1 ATOM 4148 C CD2 . TYR A 1 566 ? 23.849 26.752 54.058 1.00 27.01 ? 559 TYR A CD2 1 ATOM 4149 C CE1 . TYR A 1 566 ? 23.119 28.493 56.129 1.00 27.84 ? 559 TYR A CE1 1 ATOM 4150 C CE2 . TYR A 1 566 ? 24.389 26.561 55.350 1.00 28.49 ? 559 TYR A CE2 1 ATOM 4151 C CZ . TYR A 1 566 ? 24.015 27.439 56.381 1.00 28.87 ? 559 TYR A CZ 1 ATOM 4152 O OH . TYR A 1 566 ? 24.509 27.245 57.656 1.00 30.17 ? 559 TYR A OH 1 ATOM 4153 N N . GLU A 1 567 ? 25.162 27.825 50.897 1.00 21.61 ? 560 GLU A N 1 ATOM 4154 C CA . GLU A 1 567 ? 26.603 27.463 50.925 1.00 22.98 ? 560 GLU A CA 1 ATOM 4155 C C . GLU A 1 567 ? 27.515 28.602 50.542 1.00 22.33 ? 560 GLU A C 1 ATOM 4156 O O . GLU A 1 567 ? 28.612 28.723 51.096 1.00 23.56 ? 560 GLU A O 1 ATOM 4157 C CB . GLU A 1 567 ? 26.937 26.247 50.039 1.00 22.66 ? 560 GLU A CB 1 ATOM 4158 C CG . GLU A 1 567 ? 26.313 24.930 50.495 1.00 24.25 ? 560 GLU A CG 1 ATOM 4159 C CD . GLU A 1 567 ? 24.789 24.908 50.319 1.00 26.21 ? 560 GLU A CD 1 ATOM 4160 O OE1 . GLU A 1 567 ? 24.259 25.484 49.328 1.00 26.19 ? 560 GLU A OE1 1 ATOM 4161 O OE2 . GLU A 1 567 ? 24.121 24.314 51.188 1.00 26.32 ? 560 GLU A OE2 1 ATOM 4162 N N . LEU A 1 568 ? 27.102 29.413 49.579 1.00 21.75 ? 561 LEU A N 1 ATOM 4163 C CA . LEU A 1 568 ? 27.908 30.577 49.168 1.00 22.12 ? 561 LEU A CA 1 ATOM 4164 C C . LEU A 1 568 ? 28.199 31.484 50.372 1.00 22.87 ? 561 LEU A C 1 ATOM 4165 O O . LEU A 1 568 ? 29.347 31.932 50.550 1.00 22.99 ? 561 LEU A O 1 ATOM 4166 C CB . LEU A 1 568 ? 27.148 31.403 48.131 1.00 21.55 ? 561 LEU A CB 1 ATOM 4167 C CG . LEU A 1 568 ? 27.776 32.757 47.797 1.00 22.67 ? 561 LEU A CG 1 ATOM 4168 C CD1 . LEU A 1 568 ? 29.222 32.504 47.286 1.00 20.56 ? 561 LEU A CD1 1 ATOM 4169 C CD2 . LEU A 1 568 ? 26.861 33.562 46.785 1.00 20.01 ? 561 LEU A CD2 1 ATOM 4170 N N . VAL A 1 569 ? 27.154 31.747 51.175 1.00 22.34 ? 562 VAL A N 1 ATOM 4171 C CA . VAL A 1 569 ? 27.241 32.634 52.362 1.00 22.41 ? 562 VAL A CA 1 ATOM 4172 C C . VAL A 1 569 ? 28.074 31.954 53.485 1.00 24.15 ? 562 VAL A C 1 ATOM 4173 O O . VAL A 1 569 ? 29.031 32.538 54.010 1.00 24.34 ? 562 VAL A O 1 ATOM 4174 C CB . VAL A 1 569 ? 25.853 33.011 52.910 1.00 21.61 ? 562 VAL A CB 1 ATOM 4175 C CG1 . VAL A 1 569 ? 25.962 33.916 54.160 1.00 21.32 ? 562 VAL A CG1 1 ATOM 4176 C CG2 . VAL A 1 569 ? 25.013 33.756 51.871 1.00 21.65 ? 562 VAL A CG2 1 ATOM 4177 N N . GLU A 1 570 ? 27.686 30.732 53.848 1.00 24.97 ? 563 GLU A N 1 ATOM 4178 C CA . GLU A 1 570 ? 28.287 30.005 54.949 1.00 27.39 ? 563 GLU A CA 1 ATOM 4179 C C . GLU A 1 570 ? 29.767 29.690 54.697 1.00 27.53 ? 563 GLU A C 1 ATOM 4180 O O . GLU A 1 570 ? 30.604 29.731 55.628 1.00 28.69 ? 563 GLU A O 1 ATOM 4181 C CB . GLU A 1 570 ? 27.520 28.689 55.149 1.00 28.21 ? 563 GLU A CB 1 ATOM 4182 C CG . GLU A 1 570 ? 27.841 27.964 56.454 1.00 32.81 ? 563 GLU A CG 1 ATOM 4183 C CD . GLU A 1 570 ? 28.956 26.958 56.311 1.00 39.13 ? 563 GLU A CD 1 ATOM 4184 O OE1 . GLU A 1 570 ? 29.106 26.331 55.221 1.00 41.16 ? 563 GLU A OE1 1 ATOM 4185 O OE2 . GLU A 1 570 ? 29.704 26.792 57.302 1.00 41.95 ? 563 GLU A OE2 1 ATOM 4186 N N . LYS A 1 571 ? 30.112 29.364 53.453 1.00 26.69 ? 564 LYS A N 1 ATOM 4187 C CA . LYS A 1 571 ? 31.507 28.997 53.152 1.00 26.19 ? 564 LYS A CA 1 ATOM 4188 C C . LYS A 1 571 ? 32.396 30.215 52.851 1.00 26.75 ? 564 LYS A C 1 ATOM 4189 O O . LYS A 1 571 ? 33.568 30.232 53.247 1.00 26.31 ? 564 LYS A O 1 ATOM 4190 C CB . LYS A 1 571 ? 31.574 28.064 51.950 1.00 26.23 ? 564 LYS A CB 1 ATOM 4191 C CG . LYS A 1 571 ? 30.974 26.665 52.133 1.00 28.32 ? 564 LYS A CG 1 ATOM 4192 C CD . LYS A 1 571 ? 31.254 25.827 50.840 1.00 33.56 ? 564 LYS A CD 1 ATOM 4193 C CE . LYS A 1 571 ? 30.523 24.477 50.751 1.00 35.41 ? 564 LYS A CE 1 ATOM 4194 N NZ . LYS A 1 571 ? 30.659 23.693 51.986 1.00 37.23 ? 564 LYS A NZ 1 ATOM 4195 N N . PHE A 1 572 ? 31.872 31.212 52.121 1.00 25.51 ? 565 PHE A N 1 ATOM 4196 C CA . PHE A 1 572 ? 32.749 32.264 51.561 1.00 26.47 ? 565 PHE A CA 1 ATOM 4197 C C . PHE A 1 572 ? 32.548 33.665 52.097 1.00 26.97 ? 565 PHE A C 1 ATOM 4198 O O . PHE A 1 572 ? 33.520 34.427 52.164 1.00 29.65 ? 565 PHE A O 1 ATOM 4199 C CB . PHE A 1 572 ? 32.681 32.295 50.024 1.00 26.08 ? 565 PHE A CB 1 ATOM 4200 C CG . PHE A 1 572 ? 33.059 30.982 49.398 1.00 27.03 ? 565 PHE A CG 1 ATOM 4201 C CD1 . PHE A 1 572 ? 34.378 30.512 49.497 1.00 27.20 ? 565 PHE A CD1 1 ATOM 4202 C CD2 . PHE A 1 572 ? 32.099 30.199 48.752 1.00 25.86 ? 565 PHE A CD2 1 ATOM 4203 C CE1 . PHE A 1 572 ? 34.747 29.296 48.964 1.00 27.68 ? 565 PHE A CE1 1 ATOM 4204 C CE2 . PHE A 1 572 ? 32.458 28.960 48.181 1.00 26.29 ? 565 PHE A CE2 1 ATOM 4205 C CZ . PHE A 1 572 ? 33.787 28.493 48.305 1.00 27.57 ? 565 PHE A CZ 1 ATOM 4206 N N . TYR A 1 573 ? 31.330 34.026 52.483 1.00 25.58 ? 566 TYR A N 1 ATOM 4207 C CA . TYR A 1 573 ? 31.076 35.412 52.894 1.00 24.79 ? 566 TYR A CA 1 ATOM 4208 C C . TYR A 1 573 ? 31.144 35.592 54.389 1.00 24.62 ? 566 TYR A C 1 ATOM 4209 O O . TYR A 1 573 ? 31.795 36.553 54.871 1.00 24.36 ? 566 TYR A O 1 ATOM 4210 C CB . TYR A 1 573 ? 29.716 35.941 52.360 1.00 24.23 ? 566 TYR A CB 1 ATOM 4211 C CG . TYR A 1 573 ? 29.821 36.420 50.929 1.00 23.97 ? 566 TYR A CG 1 ATOM 4212 C CD1 . TYR A 1 573 ? 29.816 35.505 49.871 1.00 22.74 ? 566 TYR A CD1 1 ATOM 4213 C CD2 . TYR A 1 573 ? 29.974 37.798 50.628 1.00 25.10 ? 566 TYR A CD2 1 ATOM 4214 C CE1 . TYR A 1 573 ? 29.940 35.940 48.540 1.00 22.85 ? 566 TYR A CE1 1 ATOM 4215 C CE2 . TYR A 1 573 ? 30.117 38.251 49.290 1.00 23.47 ? 566 TYR A CE2 1 ATOM 4216 C CZ . TYR A 1 573 ? 30.103 37.300 48.266 1.00 22.83 ? 566 TYR A CZ 1 ATOM 4217 O OH . TYR A 1 573 ? 30.250 37.707 46.966 1.00 25.25 ? 566 TYR A OH 1 ATOM 4218 N N . ASP A 1 574 ? 30.466 34.707 55.132 1.00 24.07 ? 567 ASP A N 1 ATOM 4219 C CA . ASP A 1 574 ? 30.281 34.972 56.584 1.00 24.74 ? 567 ASP A CA 1 ATOM 4220 C C . ASP A 1 574 ? 30.113 33.695 57.418 1.00 25.72 ? 567 ASP A C 1 ATOM 4221 O O . ASP A 1 574 ? 29.025 33.456 57.992 1.00 25.35 ? 567 ASP A O 1 ATOM 4222 C CB . ASP A 1 574 ? 29.100 35.922 56.767 1.00 23.97 ? 567 ASP A CB 1 ATOM 4223 C CG . ASP A 1 574 ? 29.009 36.542 58.172 1.00 24.73 ? 567 ASP A CG 1 ATOM 4224 O OD1 . ASP A 1 574 ? 29.936 36.463 59.023 1.00 23.95 ? 567 ASP A OD1 1 ATOM 4225 O OD2 . ASP A 1 574 ? 27.950 37.122 58.420 1.00 25.74 ? 567 ASP A OD2 1 ATOM 4226 N N . PRO A 1 575 ? 31.188 32.879 57.502 1.00 27.02 ? 568 PRO A N 1 ATOM 4227 C CA . PRO A 1 575 ? 31.065 31.597 58.186 1.00 27.95 ? 568 PRO A CA 1 ATOM 4228 C C . PRO A 1 575 ? 30.607 31.675 59.637 1.00 28.43 ? 568 PRO A C 1 ATOM 4229 O O . PRO A 1 575 ? 29.897 30.772 60.077 1.00 29.70 ? 568 PRO A O 1 ATOM 4230 C CB . PRO A 1 575 ? 32.490 30.940 58.105 1.00 27.32 ? 568 PRO A CB 1 ATOM 4231 C CG . PRO A 1 575 ? 33.297 31.741 57.240 1.00 28.64 ? 568 PRO A CG 1 ATOM 4232 C CD . PRO A 1 575 ? 32.512 33.049 56.864 1.00 27.70 ? 568 PRO A CD 1 ATOM 4233 N N A MET A 1 576 ? 30.998 32.718 60.372 0.70 28.69 ? 569 MET A N 1 ATOM 4234 N N B MET A 1 576 ? 31.020 32.725 60.351 0.30 28.44 ? 569 MET A N 1 ATOM 4235 C CA A MET A 1 576 ? 30.585 32.869 61.780 0.70 28.95 ? 569 MET A CA 1 ATOM 4236 C CA B MET A 1 576 ? 30.660 32.936 61.759 0.30 28.32 ? 569 MET A CA 1 ATOM 4237 C C A MET A 1 576 ? 29.258 33.628 61.924 0.70 28.00 ? 569 MET A C 1 ATOM 4238 C C B MET A 1 576 ? 29.322 33.672 61.922 0.30 27.63 ? 569 MET A C 1 ATOM 4239 O O A MET A 1 576 ? 28.696 33.732 63.026 0.70 27.25 ? 569 MET A O 1 ATOM 4240 O O B MET A 1 576 ? 28.810 33.797 63.041 0.30 27.38 ? 569 MET A O 1 ATOM 4241 C CB A MET A 1 576 ? 31.680 33.555 62.593 0.70 30.03 ? 569 MET A CB 1 ATOM 4242 C CB B MET A 1 576 ? 31.771 33.712 62.482 0.30 28.81 ? 569 MET A CB 1 ATOM 4243 C CG A MET A 1 576 ? 33.013 32.739 62.645 0.70 34.66 ? 569 MET A CG 1 ATOM 4244 C CG B MET A 1 576 ? 33.126 32.963 62.560 0.30 30.70 ? 569 MET A CG 1 ATOM 4245 S SD A MET A 1 576 ? 32.789 31.014 63.148 0.70 42.31 ? 569 MET A SD 1 ATOM 4246 S SD B MET A 1 576 ? 34.485 33.923 63.289 0.30 34.28 ? 569 MET A SD 1 ATOM 4247 C CE A MET A 1 576 ? 32.438 31.198 64.915 0.70 43.57 ? 569 MET A CE 1 ATOM 4248 C CE B MET A 1 576 ? 35.261 34.613 61.829 0.20 33.15 ? 569 MET A CE 1 ATOM 4249 N N . PHE A 1 577 ? 28.766 34.160 60.809 1.00 26.61 ? 570 PHE A N 1 ATOM 4250 C CA . PHE A 1 577 ? 27.564 34.980 60.825 1.00 25.62 ? 570 PHE A CA 1 ATOM 4251 C C . PHE A 1 577 ? 27.734 36.215 61.685 1.00 24.88 ? 570 PHE A C 1 ATOM 4252 O O . PHE A 1 577 ? 26.760 36.809 62.128 1.00 23.42 ? 570 PHE A O 1 ATOM 4253 C CB . PHE A 1 577 ? 26.283 34.171 61.145 1.00 25.46 ? 570 PHE A CB 1 ATOM 4254 C CG . PHE A 1 577 ? 25.859 33.339 59.981 1.00 25.40 ? 570 PHE A CG 1 ATOM 4255 C CD1 . PHE A 1 577 ? 24.919 33.818 59.070 1.00 25.07 ? 570 PHE A CD1 1 ATOM 4256 C CD2 . PHE A 1 577 ? 26.513 32.113 59.724 1.00 23.45 ? 570 PHE A CD2 1 ATOM 4257 C CE1 . PHE A 1 577 ? 24.582 33.040 57.903 1.00 24.30 ? 570 PHE A CE1 1 ATOM 4258 C CE2 . PHE A 1 577 ? 26.198 31.351 58.597 1.00 24.92 ? 570 PHE A CE2 1 ATOM 4259 C CZ . PHE A 1 577 ? 25.232 31.811 57.684 1.00 24.21 ? 570 PHE A CZ 1 ATOM 4260 N N . LYS A 1 578 ? 28.995 36.611 61.881 1.00 23.97 ? 571 LYS A N 1 ATOM 4261 C CA . LYS A 1 578 ? 29.274 37.844 62.625 1.00 24.23 ? 571 LYS A CA 1 ATOM 4262 C C . LYS A 1 578 ? 28.928 39.109 61.830 1.00 23.67 ? 571 LYS A C 1 ATOM 4263 O O . LYS A 1 578 ? 28.532 40.128 62.424 1.00 23.67 ? 571 LYS A O 1 ATOM 4264 C CB . LYS A 1 578 ? 30.728 37.900 63.122 1.00 24.29 ? 571 LYS A CB 1 ATOM 4265 C CG . LYS A 1 578 ? 31.784 37.858 62.055 1.00 25.16 ? 571 LYS A CG 1 ATOM 4266 C CD . LYS A 1 578 ? 33.186 37.896 62.709 1.00 30.31 ? 571 LYS A CD 1 ATOM 4267 C CE . LYS A 1 578 ? 34.222 38.023 61.599 1.00 31.86 ? 571 LYS A CE 1 ATOM 4268 N NZ . LYS A 1 578 ? 35.576 38.354 62.085 1.00 33.89 ? 571 LYS A NZ 1 ATOM 4269 N N . TYR A 1 579 ? 29.096 39.088 60.511 1.00 23.00 ? 572 TYR A N 1 ATOM 4270 C CA . TYR A 1 579 ? 28.700 40.289 59.746 1.00 23.59 ? 572 TYR A CA 1 ATOM 4271 C C . TYR A 1 579 ? 27.192 40.421 59.734 1.00 23.07 ? 572 TYR A C 1 ATOM 4272 O O . TYR A 1 579 ? 26.679 41.541 59.858 1.00 24.40 ? 572 TYR A O 1 ATOM 4273 C CB . TYR A 1 579 ? 29.295 40.318 58.312 1.00 24.09 ? 572 TYR A CB 1 ATOM 4274 C CG . TYR A 1 579 ? 30.798 40.196 58.379 1.00 25.38 ? 572 TYR A CG 1 ATOM 4275 C CD1 . TYR A 1 579 ? 31.565 41.162 59.059 1.00 26.71 ? 572 TYR A CD1 1 ATOM 4276 C CD2 . TYR A 1 579 ? 31.453 39.089 57.845 1.00 26.58 ? 572 TYR A CD2 1 ATOM 4277 C CE1 . TYR A 1 579 ? 32.925 41.039 59.152 1.00 28.96 ? 572 TYR A CE1 1 ATOM 4278 C CE2 . TYR A 1 579 ? 32.812 38.966 57.938 1.00 28.65 ? 572 TYR A CE2 1 ATOM 4279 C CZ . TYR A 1 579 ? 33.549 39.927 58.589 1.00 30.03 ? 572 TYR A CZ 1 ATOM 4280 O OH . TYR A 1 579 ? 34.942 39.772 58.669 1.00 33.31 ? 572 TYR A OH 1 ATOM 4281 N N . HIS A 1 580 ? 26.478 39.300 59.590 1.00 22.24 ? 573 HIS A N 1 ATOM 4282 C CA . HIS A 1 580 ? 25.002 39.328 59.648 1.00 22.05 ? 573 HIS A CA 1 ATOM 4283 C C . HIS A 1 580 ? 24.568 39.897 61.021 1.00 21.68 ? 573 HIS A C 1 ATOM 4284 O O . HIS A 1 580 ? 23.679 40.729 61.089 1.00 21.23 ? 573 HIS A O 1 ATOM 4285 C CB . HIS A 1 580 ? 24.414 37.923 59.505 1.00 21.30 ? 573 HIS A CB 1 ATOM 4286 C CG . HIS A 1 580 ? 24.348 37.409 58.098 1.00 22.57 ? 573 HIS A CG 1 ATOM 4287 N ND1 . HIS A 1 580 ? 25.463 37.017 57.390 1.00 22.84 ? 573 HIS A ND1 1 ATOM 4288 C CD2 . HIS A 1 580 ? 23.284 37.181 57.286 1.00 24.23 ? 573 HIS A CD2 1 ATOM 4289 C CE1 . HIS A 1 580 ? 25.089 36.555 56.202 1.00 24.92 ? 573 HIS A CE1 1 ATOM 4290 N NE2 . HIS A 1 580 ? 23.770 36.657 56.109 1.00 25.88 ? 573 HIS A NE2 1 ATOM 4291 N N . LEU A 1 581 ? 25.177 39.389 62.105 1.00 22.19 ? 574 LEU A N 1 ATOM 4292 C CA . LEU A 1 581 ? 24.856 39.860 63.443 1.00 22.73 ? 574 LEU A CA 1 ATOM 4293 C C . LEU A 1 581 ? 25.081 41.386 63.567 1.00 23.87 ? 574 LEU A C 1 ATOM 4294 O O . LEU A 1 581 ? 24.192 42.111 64.042 1.00 23.77 ? 574 LEU A O 1 ATOM 4295 C CB . LEU A 1 581 ? 25.609 39.071 64.538 1.00 22.62 ? 574 LEU A CB 1 ATOM 4296 C CG . LEU A 1 581 ? 25.358 39.584 65.985 1.00 22.47 ? 574 LEU A CG 1 ATOM 4297 C CD1 . LEU A 1 581 ? 23.859 39.478 66.274 1.00 21.33 ? 574 LEU A CD1 1 ATOM 4298 C CD2 . LEU A 1 581 ? 26.155 38.741 67.029 1.00 22.20 ? 574 LEU A CD2 1 ATOM 4299 N N . THR A 1 582 ? 26.241 41.879 63.114 1.00 24.06 ? 575 THR A N 1 ATOM 4300 C CA . THR A 1 582 ? 26.512 43.356 63.090 1.00 23.26 ? 575 THR A CA 1 ATOM 4301 C C . THR A 1 582 ? 25.426 44.120 62.337 1.00 22.75 ? 575 THR A C 1 ATOM 4302 O O . THR A 1 582 ? 24.926 45.130 62.809 1.00 22.97 ? 575 THR A O 1 ATOM 4303 C CB . THR A 1 582 ? 27.918 43.633 62.503 1.00 22.87 ? 575 THR A CB 1 ATOM 4304 O OG1 . THR A 1 582 ? 28.882 43.135 63.438 1.00 24.55 ? 575 THR A OG1 1 ATOM 4305 C CG2 . THR A 1 582 ? 28.209 45.124 62.296 1.00 21.53 ? 575 THR A CG2 1 ATOM 4306 N N . VAL A 1 583 ? 25.022 43.605 61.180 1.00 22.22 ? 576 VAL A N 1 ATOM 4307 C CA . VAL A 1 583 ? 23.957 44.252 60.387 1.00 21.81 ? 576 VAL A CA 1 ATOM 4308 C C . VAL A 1 583 ? 22.622 44.192 61.135 1.00 22.12 ? 576 VAL A C 1 ATOM 4309 O O . VAL A 1 583 ? 21.867 45.159 61.127 1.00 22.19 ? 576 VAL A O 1 ATOM 4310 C CB . VAL A 1 583 ? 23.888 43.678 58.936 1.00 21.42 ? 576 VAL A CB 1 ATOM 4311 C CG1 . VAL A 1 583 ? 22.678 44.232 58.118 1.00 19.36 ? 576 VAL A CG1 1 ATOM 4312 C CG2 . VAL A 1 583 ? 25.202 43.952 58.200 1.00 21.73 ? 576 VAL A CG2 1 ATOM 4313 N N . ALA A 1 584 ? 22.330 43.069 61.794 1.00 21.93 ? 577 ALA A N 1 ATOM 4314 C CA . ALA A 1 584 ? 21.098 42.976 62.615 1.00 20.85 ? 577 ALA A CA 1 ATOM 4315 C C . ALA A 1 584 ? 21.099 44.044 63.720 1.00 21.24 ? 577 ALA A C 1 ATOM 4316 O O . ALA A 1 584 ? 20.077 44.697 64.021 1.00 20.64 ? 577 ALA A O 1 ATOM 4317 C CB . ALA A 1 584 ? 20.992 41.604 63.214 1.00 19.72 ? 577 ALA A CB 1 ATOM 4318 N N . GLN A 1 585 ? 22.253 44.219 64.332 1.00 21.16 ? 578 GLN A N 1 ATOM 4319 C CA . GLN A 1 585 ? 22.412 45.255 65.350 1.00 21.07 ? 578 GLN A CA 1 ATOM 4320 C C . GLN A 1 585 ? 22.243 46.672 64.799 1.00 20.76 ? 578 GLN A C 1 ATOM 4321 O O . GLN A 1 585 ? 21.631 47.548 65.470 1.00 20.58 ? 578 GLN A O 1 ATOM 4322 C CB . GLN A 1 585 ? 23.769 45.100 66.081 1.00 20.81 ? 578 GLN A CB 1 ATOM 4323 C CG . GLN A 1 585 ? 23.920 43.775 66.848 1.00 22.34 ? 578 GLN A CG 1 ATOM 4324 C CD . GLN A 1 585 ? 25.321 43.632 67.498 1.00 25.66 ? 578 GLN A CD 1 ATOM 4325 O OE1 . GLN A 1 585 ? 26.202 44.465 67.263 1.00 27.61 ? 578 GLN A OE1 1 ATOM 4326 N NE2 . GLN A 1 585 ? 25.521 42.578 68.307 1.00 25.08 ? 578 GLN A NE2 1 ATOM 4327 N N . VAL A 1 586 ? 22.780 46.929 63.603 1.00 20.45 ? 579 VAL A N 1 ATOM 4328 C CA . VAL A 1 586 ? 22.630 48.276 63.018 1.00 20.26 ? 579 VAL A CA 1 ATOM 4329 C C . VAL A 1 586 ? 21.161 48.507 62.627 1.00 20.35 ? 579 VAL A C 1 ATOM 4330 O O . VAL A 1 586 ? 20.552 49.530 63.000 1.00 20.85 ? 579 VAL A O 1 ATOM 4331 C CB . VAL A 1 586 ? 23.544 48.510 61.758 1.00 20.49 ? 579 VAL A CB 1 ATOM 4332 C CG1 . VAL A 1 586 ? 23.249 49.873 61.114 1.00 18.04 ? 579 VAL A CG1 1 ATOM 4333 C CG2 . VAL A 1 586 ? 25.051 48.361 62.090 1.00 20.65 ? 579 VAL A CG2 1 ATOM 4334 N N . ARG A 1 587 ? 20.569 47.581 61.865 1.00 19.63 ? 580 ARG A N 1 ATOM 4335 C CA . ARG A 1 587 ? 19.175 47.801 61.446 1.00 19.27 ? 580 ARG A CA 1 ATOM 4336 C C . ARG A 1 587 ? 18.208 47.802 62.658 1.00 19.68 ? 580 ARG A C 1 ATOM 4337 O O . ARG A 1 587 ? 17.339 48.662 62.759 1.00 18.85 ? 580 ARG A O 1 ATOM 4338 C CB . ARG A 1 587 ? 18.714 46.738 60.434 1.00 18.05 ? 580 ARG A CB 1 ATOM 4339 C CG . ARG A 1 587 ? 19.456 46.773 59.099 1.00 17.46 ? 580 ARG A CG 1 ATOM 4340 C CD . ARG A 1 587 ? 19.187 45.503 58.322 1.00 16.99 ? 580 ARG A CD 1 ATOM 4341 N NE . ARG A 1 587 ? 19.837 45.560 57.013 1.00 17.09 ? 580 ARG A NE 1 ATOM 4342 C CZ . ARG A 1 587 ? 19.861 44.559 56.138 1.00 18.61 ? 580 ARG A CZ 1 ATOM 4343 N NH1 . ARG A 1 587 ? 19.266 43.387 56.439 1.00 19.59 ? 580 ARG A NH1 1 ATOM 4344 N NH2 . ARG A 1 587 ? 20.462 44.732 54.956 1.00 16.89 ? 580 ARG A NH2 1 ATOM 4345 N N . GLY A 1 588 ? 18.348 46.803 63.535 1.00 19.51 ? 581 GLY A N 1 ATOM 4346 C CA . GLY A 1 588 ? 17.513 46.669 64.721 1.00 19.86 ? 581 GLY A CA 1 ATOM 4347 C C . GLY A 1 588 ? 17.696 47.847 65.686 1.00 20.50 ? 581 GLY A C 1 ATOM 4348 O O . GLY A 1 588 ? 16.735 48.374 66.230 1.00 19.82 ? 581 GLY A O 1 ATOM 4349 N N . GLY A 1 589 ? 18.948 48.251 65.904 1.00 20.65 ? 582 GLY A N 1 ATOM 4350 C CA . GLY A 1 589 ? 19.233 49.392 66.784 1.00 19.89 ? 582 GLY A CA 1 ATOM 4351 C C . GLY A 1 589 ? 18.637 50.670 66.237 1.00 20.29 ? 582 GLY A C 1 ATOM 4352 O O . GLY A 1 589 ? 18.177 51.518 67.019 1.00 19.71 ? 582 GLY A O 1 ATOM 4353 N N . MET A 1 590 ? 18.650 50.844 64.900 1.00 19.41 ? 583 MET A N 1 ATOM 4354 C CA . MET A 1 590 ? 18.091 52.060 64.316 1.00 19.78 ? 583 MET A CA 1 ATOM 4355 C C . MET A 1 590 ? 16.564 52.045 64.577 1.00 19.76 ? 583 MET A C 1 ATOM 4356 O O . MET A 1 590 ? 16.008 53.019 65.060 1.00 19.51 ? 583 MET A O 1 ATOM 4357 C CB . MET A 1 590 ? 18.395 52.165 62.805 1.00 20.03 ? 583 MET A CB 1 ATOM 4358 C CG . MET A 1 590 ? 19.852 52.528 62.531 1.00 21.74 ? 583 MET A CG 1 ATOM 4359 S SD . MET A 1 590 ? 20.264 52.542 60.766 1.00 23.64 ? 583 MET A SD 1 ATOM 4360 C CE . MET A 1 590 ? 19.477 54.084 60.226 1.00 20.36 ? 583 MET A CE 1 ATOM 4361 N N . VAL A 1 591 ? 15.919 50.905 64.320 1.00 19.11 ? 584 VAL A N 1 ATOM 4362 C CA . VAL A 1 591 ? 14.487 50.771 64.539 1.00 19.52 ? 584 VAL A CA 1 ATOM 4363 C C . VAL A 1 591 ? 14.180 51.026 66.032 1.00 20.40 ? 584 VAL A C 1 ATOM 4364 O O . VAL A 1 591 ? 13.220 51.756 66.346 1.00 21.19 ? 584 VAL A O 1 ATOM 4365 C CB . VAL A 1 591 ? 13.984 49.348 64.122 1.00 19.45 ? 584 VAL A CB 1 ATOM 4366 C CG1 . VAL A 1 591 ? 12.544 49.063 64.691 1.00 16.92 ? 584 VAL A CG1 1 ATOM 4367 C CG2 . VAL A 1 591 ? 14.113 49.150 62.579 1.00 18.58 ? 584 VAL A CG2 1 ATOM 4368 N N . PHE A 1 592 ? 14.985 50.431 66.932 1.00 20.32 ? 585 PHE A N 1 ATOM 4369 C CA . PHE A 1 592 ? 14.768 50.578 68.360 1.00 20.79 ? 585 PHE A CA 1 ATOM 4370 C C . PHE A 1 592 ? 14.801 52.064 68.741 1.00 22.33 ? 585 PHE A C 1 ATOM 4371 O O . PHE A 1 592 ? 13.922 52.539 69.478 1.00 22.28 ? 585 PHE A O 1 ATOM 4372 C CB . PHE A 1 592 ? 15.845 49.824 69.179 1.00 21.01 ? 585 PHE A CB 1 ATOM 4373 C CG . PHE A 1 592 ? 15.536 49.775 70.662 1.00 22.00 ? 585 PHE A CG 1 ATOM 4374 C CD1 . PHE A 1 592 ? 14.984 48.626 71.228 1.00 22.81 ? 585 PHE A CD1 1 ATOM 4375 C CD2 . PHE A 1 592 ? 15.722 50.910 71.466 1.00 23.82 ? 585 PHE A CD2 1 ATOM 4376 C CE1 . PHE A 1 592 ? 14.659 48.567 72.598 1.00 23.80 ? 585 PHE A CE1 1 ATOM 4377 C CE2 . PHE A 1 592 ? 15.423 50.883 72.859 1.00 25.26 ? 585 PHE A CE2 1 ATOM 4378 C CZ . PHE A 1 592 ? 14.888 49.701 73.429 1.00 25.78 ? 585 PHE A CZ 1 ATOM 4379 N N . GLU A 1 593 ? 15.825 52.799 68.287 1.00 23.50 ? 586 GLU A N 1 ATOM 4380 C CA . GLU A 1 593 ? 15.948 54.230 68.679 1.00 24.33 ? 586 GLU A CA 1 ATOM 4381 C C . GLU A 1 593 ? 14.817 55.048 68.071 1.00 23.45 ? 586 GLU A C 1 ATOM 4382 O O . GLU A 1 593 ? 14.231 55.915 68.748 1.00 23.06 ? 586 GLU A O 1 ATOM 4383 C CB . GLU A 1 593 ? 17.271 54.830 68.220 1.00 25.07 ? 586 GLU A CB 1 ATOM 4384 C CG . GLU A 1 593 ? 18.407 54.572 69.170 1.00 34.95 ? 586 GLU A CG 1 ATOM 4385 C CD . GLU A 1 593 ? 18.134 55.246 70.542 1.00 41.46 ? 586 GLU A CD 1 ATOM 4386 O OE1 . GLU A 1 593 ? 17.759 54.514 71.465 1.00 43.67 ? 586 GLU A OE1 1 ATOM 4387 O OE2 . GLU A 1 593 ? 18.207 56.501 70.669 1.00 45.96 ? 586 GLU A OE2 1 ATOM 4388 N N . LEU A 1 594 ? 14.514 54.779 66.802 1.00 21.65 ? 587 LEU A N 1 ATOM 4389 C CA . LEU A 1 594 ? 13.413 55.502 66.100 1.00 21.53 ? 587 LEU A CA 1 ATOM 4390 C C . LEU A 1 594 ? 12.061 55.279 66.827 1.00 21.84 ? 587 LEU A C 1 ATOM 4391 O O . LEU A 1 594 ? 11.243 56.213 66.993 1.00 21.37 ? 587 LEU A O 1 ATOM 4392 C CB . LEU A 1 594 ? 13.327 55.079 64.612 1.00 21.03 ? 587 LEU A CB 1 ATOM 4393 C CG . LEU A 1 594 ? 14.505 55.594 63.767 1.00 20.33 ? 587 LEU A CG 1 ATOM 4394 C CD1 . LEU A 1 594 ? 14.653 54.750 62.523 1.00 17.42 ? 587 LEU A CD1 1 ATOM 4395 C CD2 . LEU A 1 594 ? 14.230 57.081 63.348 1.00 19.58 ? 587 LEU A CD2 1 ATOM 4396 N N . ALA A 1 595 ? 11.845 54.042 67.279 1.00 21.36 ? 588 ALA A N 1 ATOM 4397 C CA . ALA A 1 595 ? 10.587 53.665 67.926 1.00 22.12 ? 588 ALA A CA 1 ATOM 4398 C C . ALA A 1 595 ? 10.480 53.983 69.422 1.00 23.12 ? 588 ALA A C 1 ATOM 4399 O O . ALA A 1 595 ? 9.365 54.023 69.957 1.00 22.82 ? 588 ALA A O 1 ATOM 4400 C CB . ALA A 1 595 ? 10.296 52.155 67.669 1.00 21.33 ? 588 ALA A CB 1 ATOM 4401 N N . ASN A 1 596 ? 11.616 54.238 70.095 1.00 23.89 ? 589 ASN A N 1 ATOM 4402 C CA . ASN A 1 596 ? 11.611 54.396 71.551 1.00 24.59 ? 589 ASN A CA 1 ATOM 4403 C C . ASN A 1 596 ? 12.134 55.699 72.125 1.00 24.81 ? 589 ASN A C 1 ATOM 4404 O O . ASN A 1 596 ? 11.825 56.056 73.274 1.00 25.52 ? 589 ASN A O 1 ATOM 4405 C CB . ASN A 1 596 ? 12.350 53.228 72.197 1.00 24.63 ? 589 ASN A CB 1 ATOM 4406 C CG A ASN A 1 596 ? 11.722 52.799 73.511 0.50 26.37 ? 589 ASN A CG 1 ATOM 4407 C CG B ASN A 1 596 ? 11.566 51.965 72.078 0.50 23.79 ? 589 ASN A CG 1 ATOM 4408 O OD1 A ASN A 1 596 ? 10.505 52.587 73.595 0.50 27.00 ? 589 ASN A OD1 1 ATOM 4409 O OD1 B ASN A 1 596 ? 11.828 51.125 71.204 0.50 24.56 ? 589 ASN A OD1 1 ATOM 4410 N ND2 A ASN A 1 596 ? 12.550 52.657 74.549 0.50 27.69 ? 589 ASN A ND2 1 ATOM 4411 N ND2 B ASN A 1 596 ? 10.543 51.845 72.904 0.50 21.59 ? 589 ASN A ND2 1 ATOM 4412 N N . SER A 1 597 ? 12.932 56.412 71.342 1.00 24.37 ? 590 SER A N 1 ATOM 4413 C CA . SER A 1 597 ? 13.500 57.660 71.845 1.00 24.85 ? 590 SER A CA 1 ATOM 4414 C C . SER A 1 597 ? 12.391 58.715 72.040 1.00 23.92 ? 590 SER A C 1 ATOM 4415 O O . SER A 1 597 ? 11.468 58.828 71.216 1.00 24.04 ? 590 SER A O 1 ATOM 4416 C CB . SER A 1 597 ? 14.662 58.102 70.937 1.00 25.81 ? 590 SER A CB 1 ATOM 4417 O OG . SER A 1 597 ? 14.996 59.436 71.192 1.00 26.31 ? 590 SER A OG 1 ATOM 4418 N N . ILE A 1 598 ? 12.456 59.452 73.151 1.00 23.59 ? 591 ILE A N 1 ATOM 4419 C CA . ILE A 1 598 ? 11.385 60.399 73.512 1.00 23.42 ? 591 ILE A CA 1 ATOM 4420 C C . ILE A 1 598 ? 11.307 61.456 72.421 1.00 23.10 ? 591 ILE A C 1 ATOM 4421 O O . ILE A 1 598 ? 10.213 61.721 71.872 1.00 22.53 ? 591 ILE A O 1 ATOM 4422 C CB . ILE A 1 598 ? 11.659 61.037 74.895 1.00 22.63 ? 591 ILE A CB 1 ATOM 4423 C CG1 . ILE A 1 598 ? 11.629 59.957 75.989 1.00 28.13 ? 591 ILE A CG1 1 ATOM 4424 C CG2 . ILE A 1 598 ? 10.650 62.097 75.241 1.00 22.12 ? 591 ILE A CG2 1 ATOM 4425 C CD1 . ILE A 1 598 ? 10.381 59.055 75.918 1.00 30.36 ? 591 ILE A CD1 1 ATOM 4426 N N . VAL A 1 599 ? 12.475 62.020 72.078 1.00 23.13 ? 592 VAL A N 1 ATOM 4427 C CA . VAL A 1 599 ? 12.587 62.949 70.950 1.00 22.43 ? 592 VAL A CA 1 ATOM 4428 C C . VAL A 1 599 ? 13.067 62.132 69.766 1.00 22.46 ? 592 VAL A C 1 ATOM 4429 O O . VAL A 1 599 ? 14.032 61.373 69.863 1.00 21.97 ? 592 VAL A O 1 ATOM 4430 C CB . VAL A 1 599 ? 13.540 64.122 71.242 1.00 22.50 ? 592 VAL A CB 1 ATOM 4431 C CG1 . VAL A 1 599 ? 13.606 65.089 70.025 1.00 22.05 ? 592 VAL A CG1 1 ATOM 4432 C CG2 . VAL A 1 599 ? 13.027 64.923 72.496 1.00 23.75 ? 592 VAL A CG2 1 ATOM 4433 N N . LEU A 1 600 ? 12.365 62.241 68.645 1.00 21.85 ? 593 LEU A N 1 ATOM 4434 C CA . LEU A 1 600 ? 12.792 61.534 67.410 1.00 22.05 ? 593 LEU A CA 1 ATOM 4435 C C . LEU A 1 600 ? 14.290 61.805 67.135 1.00 21.68 ? 593 LEU A C 1 ATOM 4436 O O . LEU A 1 600 ? 14.760 62.952 67.273 1.00 21.95 ? 593 LEU A O 1 ATOM 4437 C CB . LEU A 1 600 ? 11.891 61.919 66.222 1.00 21.36 ? 593 LEU A CB 1 ATOM 4438 C CG . LEU A 1 600 ? 10.509 61.245 66.175 1.00 23.22 ? 593 LEU A CG 1 ATOM 4439 C CD1 . LEU A 1 600 ? 9.669 61.808 65.010 1.00 22.88 ? 593 LEU A CD1 1 ATOM 4440 C CD2 . LEU A 1 600 ? 10.647 59.705 66.048 1.00 23.22 ? 593 LEU A CD2 1 ATOM 4441 N N . PRO A 1 601 ? 15.055 60.744 66.807 1.00 21.06 ? 594 PRO A N 1 ATOM 4442 C CA . PRO A 1 601 ? 16.520 60.895 66.680 1.00 21.11 ? 594 PRO A CA 1 ATOM 4443 C C . PRO A 1 601 ? 16.923 61.409 65.261 1.00 21.40 ? 594 PRO A C 1 ATOM 4444 O O . PRO A 1 601 ? 17.701 60.739 64.542 1.00 21.13 ? 594 PRO A O 1 ATOM 4445 C CB . PRO A 1 601 ? 17.023 59.479 66.906 1.00 21.00 ? 594 PRO A CB 1 ATOM 4446 C CG . PRO A 1 601 ? 15.914 58.583 66.357 1.00 22.12 ? 594 PRO A CG 1 ATOM 4447 C CD . PRO A 1 601 ? 14.617 59.345 66.699 1.00 20.22 ? 594 PRO A CD 1 ATOM 4448 N N . PHE A 1 602 ? 16.354 62.549 64.866 1.00 20.62 ? 595 PHE A N 1 ATOM 4449 C CA . PHE A 1 602 ? 16.658 63.179 63.570 1.00 21.46 ? 595 PHE A CA 1 ATOM 4450 C C . PHE A 1 602 ? 17.349 64.523 63.854 1.00 22.21 ? 595 PHE A C 1 ATOM 4451 O O . PHE A 1 602 ? 16.887 65.303 64.711 1.00 22.61 ? 595 PHE A O 1 ATOM 4452 C CB . PHE A 1 602 ? 15.382 63.538 62.799 1.00 19.46 ? 595 PHE A CB 1 ATOM 4453 C CG . PHE A 1 602 ? 14.583 62.358 62.290 1.00 20.07 ? 595 PHE A CG 1 ATOM 4454 C CD1 . PHE A 1 602 ? 15.177 61.133 62.004 1.00 18.89 ? 595 PHE A CD1 1 ATOM 4455 C CD2 . PHE A 1 602 ? 13.200 62.500 62.088 1.00 20.07 ? 595 PHE A CD2 1 ATOM 4456 C CE1 . PHE A 1 602 ? 14.402 60.048 61.506 1.00 19.23 ? 595 PHE A CE1 1 ATOM 4457 C CE2 . PHE A 1 602 ? 12.407 61.427 61.621 1.00 19.56 ? 595 PHE A CE2 1 ATOM 4458 C CZ . PHE A 1 602 ? 13.006 60.215 61.314 1.00 16.53 ? 595 PHE A CZ 1 ATOM 4459 N N . ASP A 1 603 ? 18.394 64.842 63.103 1.00 21.59 ? 596 ASP A N 1 ATOM 4460 C CA . ASP A 1 603 ? 19.076 66.133 63.303 1.00 21.34 ? 596 ASP A CA 1 ATOM 4461 C C . ASP A 1 603 ? 18.917 66.938 62.007 1.00 21.21 ? 596 ASP A C 1 ATOM 4462 O O . ASP A 1 603 ? 19.569 66.655 60.986 1.00 20.73 ? 596 ASP A O 1 ATOM 4463 C CB . ASP A 1 603 ? 20.549 65.945 63.666 1.00 21.05 ? 596 ASP A CB 1 ATOM 4464 C CG . ASP A 1 603 ? 21.214 67.288 64.064 1.00 23.70 ? 596 ASP A CG 1 ATOM 4465 O OD1 . ASP A 1 603 ? 20.645 68.384 63.795 1.00 24.16 ? 596 ASP A OD1 1 ATOM 4466 O OD2 . ASP A 1 603 ? 22.300 67.259 64.639 1.00 28.68 ? 596 ASP A OD2 1 ATOM 4467 N N . CYS A 1 604 ? 18.005 67.896 62.043 1.00 20.67 ? 597 CYS A N 1 ATOM 4468 C CA . CYS A 1 604 ? 17.700 68.689 60.863 1.00 22.23 ? 597 CYS A CA 1 ATOM 4469 C C . CYS A 1 604 ? 18.933 69.474 60.382 1.00 22.16 ? 597 CYS A C 1 ATOM 4470 O O . CYS A 1 604 ? 19.016 69.779 59.203 1.00 22.37 ? 597 CYS A O 1 ATOM 4471 C CB . CYS A 1 604 ? 16.547 69.676 61.173 1.00 21.73 ? 597 CYS A CB 1 ATOM 4472 S SG . CYS A 1 604 ? 16.889 70.830 62.636 1.00 26.29 ? 597 CYS A SG 1 ATOM 4473 N N . ARG A 1 605 ? 19.860 69.810 61.291 1.00 21.72 ? 598 ARG A N 1 ATOM 4474 C CA . ARG A 1 605 ? 21.074 70.528 60.882 1.00 23.21 ? 598 ARG A CA 1 ATOM 4475 C C . ARG A 1 605 ? 21.935 69.716 59.873 1.00 23.17 ? 598 ARG A C 1 ATOM 4476 O O . ARG A 1 605 ? 22.639 70.308 59.016 1.00 22.75 ? 598 ARG A O 1 ATOM 4477 C CB . ARG A 1 605 ? 21.928 70.907 62.096 1.00 23.10 ? 598 ARG A CB 1 ATOM 4478 C CG . ARG A 1 605 ? 21.230 71.896 63.083 1.00 25.24 ? 598 ARG A CG 1 ATOM 4479 C CD . ARG A 1 605 ? 22.045 72.011 64.393 1.00 26.69 ? 598 ARG A CD 1 ATOM 4480 N NE . ARG A 1 605 ? 22.103 70.711 65.039 1.00 27.21 ? 598 ARG A NE 1 ATOM 4481 C CZ . ARG A 1 605 ? 22.722 70.478 66.195 1.00 30.24 ? 598 ARG A CZ 1 ATOM 4482 N NH1 . ARG A 1 605 ? 23.317 71.483 66.844 1.00 28.49 ? 598 ARG A NH1 1 ATOM 4483 N NH2 . ARG A 1 605 ? 22.745 69.238 66.705 1.00 29.48 ? 598 ARG A NH2 1 ATOM 4484 N N . ASP A 1 606 ? 21.870 68.380 59.952 1.00 22.26 ? 599 ASP A N 1 ATOM 4485 C CA . ASP A 1 606 ? 22.586 67.557 58.958 1.00 22.57 ? 599 ASP A CA 1 ATOM 4486 C C . ASP A 1 606 ? 22.002 67.744 57.539 1.00 21.38 ? 599 ASP A C 1 ATOM 4487 O O . ASP A 1 606 ? 22.753 67.697 56.544 1.00 21.47 ? 599 ASP A O 1 ATOM 4488 C CB . ASP A 1 606 ? 22.619 66.063 59.344 1.00 21.79 ? 599 ASP A CB 1 ATOM 4489 C CG . ASP A 1 606 ? 23.549 65.798 60.528 1.00 24.84 ? 599 ASP A CG 1 ATOM 4490 O OD1 . ASP A 1 606 ? 24.587 66.444 60.586 1.00 30.08 ? 599 ASP A OD1 1 ATOM 4491 O OD2 . ASP A 1 606 ? 23.285 64.965 61.408 1.00 24.66 ? 599 ASP A OD2 1 ATOM 4492 N N . TYR A 1 607 ? 20.690 67.972 57.427 1.00 20.39 ? 600 TYR A N 1 ATOM 4493 C CA . TYR A 1 607 ? 20.117 68.293 56.107 1.00 19.28 ? 600 TYR A CA 1 ATOM 4494 C C . TYR A 1 607 ? 20.657 69.638 55.593 1.00 19.80 ? 600 TYR A C 1 ATOM 4495 O O . TYR A 1 607 ? 20.924 69.766 54.369 1.00 18.73 ? 600 TYR A O 1 ATOM 4496 C CB . TYR A 1 607 ? 18.572 68.341 56.118 1.00 18.69 ? 600 TYR A CB 1 ATOM 4497 C CG . TYR A 1 607 ? 17.939 67.374 55.144 1.00 18.53 ? 600 TYR A CG 1 ATOM 4498 C CD1 . TYR A 1 607 ? 18.260 67.414 53.779 1.00 18.67 ? 600 TYR A CD1 1 ATOM 4499 C CD2 . TYR A 1 607 ? 16.994 66.445 55.580 1.00 17.57 ? 600 TYR A CD2 1 ATOM 4500 C CE1 . TYR A 1 607 ? 17.690 66.522 52.854 1.00 18.16 ? 600 TYR A CE1 1 ATOM 4501 C CE2 . TYR A 1 607 ? 16.403 65.529 54.664 1.00 18.03 ? 600 TYR A CE2 1 ATOM 4502 C CZ . TYR A 1 607 ? 16.755 65.591 53.302 1.00 17.34 ? 600 TYR A CZ 1 ATOM 4503 O OH . TYR A 1 607 ? 16.196 64.708 52.416 1.00 17.28 ? 600 TYR A OH 1 ATOM 4504 N N . ALA A 1 608 ? 20.791 70.631 56.490 1.00 18.97 ? 601 ALA A N 1 ATOM 4505 C CA . ALA A 1 608 ? 21.270 71.966 56.066 1.00 19.96 ? 601 ALA A CA 1 ATOM 4506 C C . ALA A 1 608 ? 22.676 71.873 55.426 1.00 20.73 ? 601 ALA A C 1 ATOM 4507 O O . ALA A 1 608 ? 22.967 72.488 54.367 1.00 20.84 ? 601 ALA A O 1 ATOM 4508 C CB . ALA A 1 608 ? 21.301 72.962 57.246 1.00 19.14 ? 601 ALA A CB 1 ATOM 4509 N N . VAL A 1 609 ? 23.542 71.108 56.060 1.00 20.99 ? 602 VAL A N 1 ATOM 4510 C CA . VAL A 1 609 ? 24.879 70.874 55.542 1.00 22.03 ? 602 VAL A CA 1 ATOM 4511 C C . VAL A 1 609 ? 24.857 70.225 54.121 1.00 22.22 ? 602 VAL A C 1 ATOM 4512 O O . VAL A 1 609 ? 25.544 70.730 53.197 1.00 22.08 ? 602 VAL A O 1 ATOM 4513 C CB . VAL A 1 609 ? 25.760 70.024 56.515 1.00 23.28 ? 602 VAL A CB 1 ATOM 4514 C CG1 . VAL A 1 609 ? 27.129 69.658 55.859 1.00 25.23 ? 602 VAL A CG1 1 ATOM 4515 C CG2 . VAL A 1 609 ? 26.037 70.821 57.822 1.00 25.27 ? 602 VAL A CG2 1 ATOM 4516 N N . VAL A 1 610 ? 24.081 69.158 53.914 1.00 20.80 ? 603 VAL A N 1 ATOM 4517 C CA . VAL A 1 610 ? 24.135 68.535 52.575 1.00 20.39 ? 603 VAL A CA 1 ATOM 4518 C C . VAL A 1 610 ? 23.446 69.394 51.523 1.00 20.14 ? 603 VAL A C 1 ATOM 4519 O O . VAL A 1 610 ? 23.859 69.362 50.358 1.00 20.12 ? 603 VAL A O 1 ATOM 4520 C CB . VAL A 1 610 ? 23.673 67.039 52.477 1.00 20.39 ? 603 VAL A CB 1 ATOM 4521 C CG1 . VAL A 1 610 ? 24.367 66.173 53.571 1.00 21.35 ? 603 VAL A CG1 1 ATOM 4522 C CG2 . VAL A 1 610 ? 22.249 66.906 52.568 1.00 21.62 ? 603 VAL A CG2 1 ATOM 4523 N N . LEU A 1 611 ? 22.408 70.146 51.907 1.00 18.83 ? 604 LEU A N 1 ATOM 4524 C CA . LEU A 1 611 ? 21.742 71.001 50.936 1.00 19.23 ? 604 LEU A CA 1 ATOM 4525 C C . LEU A 1 611 ? 22.747 71.985 50.332 1.00 19.31 ? 604 LEU A C 1 ATOM 4526 O O . LEU A 1 611 ? 22.698 72.291 49.115 1.00 19.29 ? 604 LEU A O 1 ATOM 4527 C CB . LEU A 1 611 ? 20.546 71.760 51.568 1.00 17.88 ? 604 LEU A CB 1 ATOM 4528 C CG . LEU A 1 611 ? 19.364 70.802 51.836 1.00 18.27 ? 604 LEU A CG 1 ATOM 4529 C CD1 . LEU A 1 611 ? 18.305 71.527 52.696 1.00 19.84 ? 604 LEU A CD1 1 ATOM 4530 C CD2 . LEU A 1 611 ? 18.719 70.293 50.509 1.00 18.07 ? 604 LEU A CD2 1 ATOM 4531 N N . ARG A 1 612 ? 23.643 72.488 51.166 1.00 20.16 ? 605 ARG A N 1 ATOM 4532 C CA . ARG A 1 612 ? 24.649 73.444 50.672 1.00 21.16 ? 605 ARG A CA 1 ATOM 4533 C C . ARG A 1 612 ? 25.602 72.756 49.719 1.00 21.25 ? 605 ARG A C 1 ATOM 4534 O O . ARG A 1 612 ? 25.912 73.292 48.650 1.00 21.28 ? 605 ARG A O 1 ATOM 4535 C CB . ARG A 1 612 ? 25.419 74.120 51.803 1.00 21.27 ? 605 ARG A CB 1 ATOM 4536 C CG . ARG A 1 612 ? 26.541 75.041 51.317 1.00 23.81 ? 605 ARG A CG 1 ATOM 4537 C CD . ARG A 1 612 ? 25.997 76.236 50.442 1.00 28.27 ? 605 ARG A CD 1 ATOM 4538 N NE . ARG A 1 612 ? 27.159 77.008 49.979 1.00 31.87 ? 605 ARG A NE 1 ATOM 4539 C CZ . ARG A 1 612 ? 27.604 78.103 50.568 1.00 36.51 ? 605 ARG A CZ 1 ATOM 4540 N NH1 . ARG A 1 612 ? 26.972 78.593 51.631 1.00 38.18 ? 605 ARG A NH1 1 ATOM 4541 N NH2 . ARG A 1 612 ? 28.686 78.706 50.100 1.00 37.85 ? 605 ARG A NH2 1 ATOM 4542 N N . LYS A 1 613 ? 26.033 71.555 50.087 1.00 21.16 ? 606 LYS A N 1 ATOM 4543 C CA . LYS A 1 613 ? 26.879 70.763 49.218 1.00 22.59 ? 606 LYS A CA 1 ATOM 4544 C C . LYS A 1 613 ? 26.186 70.504 47.848 1.00 21.48 ? 606 LYS A C 1 ATOM 4545 O O . LYS A 1 613 ? 26.812 70.682 46.798 1.00 21.10 ? 606 LYS A O 1 ATOM 4546 C CB . LYS A 1 613 ? 27.241 69.444 49.912 1.00 23.08 ? 606 LYS A CB 1 ATOM 4547 C CG . LYS A 1 613 ? 28.145 68.539 49.111 1.00 28.81 ? 606 LYS A CG 1 ATOM 4548 C CD . LYS A 1 613 ? 28.491 67.238 49.916 1.00 35.24 ? 606 LYS A CD 1 ATOM 4549 C CE . LYS A 1 613 ? 27.255 66.289 49.944 1.00 35.78 ? 606 LYS A CE 1 ATOM 4550 N NZ . LYS A 1 613 ? 27.487 64.943 50.600 1.00 37.35 ? 606 LYS A NZ 1 ATOM 4551 N N . TYR A 1 614 ? 24.906 70.105 47.859 1.00 20.11 ? 607 TYR A N 1 ATOM 4552 C CA . TYR A 1 614 ? 24.196 69.858 46.592 1.00 19.22 ? 607 TYR A CA 1 ATOM 4553 C C . TYR A 1 614 ? 23.988 71.119 45.761 1.00 18.77 ? 607 TYR A C 1 ATOM 4554 O O . TYR A 1 614 ? 24.018 71.056 44.541 1.00 19.58 ? 607 TYR A O 1 ATOM 4555 C CB . TYR A 1 614 ? 22.825 69.241 46.845 1.00 17.28 ? 607 TYR A CB 1 ATOM 4556 C CG . TYR A 1 614 ? 22.886 67.928 47.622 1.00 19.09 ? 607 TYR A CG 1 ATOM 4557 C CD1 . TYR A 1 614 ? 24.039 67.127 47.595 1.00 20.32 ? 607 TYR A CD1 1 ATOM 4558 C CD2 . TYR A 1 614 ? 21.784 67.483 48.353 1.00 19.29 ? 607 TYR A CD2 1 ATOM 4559 C CE1 . TYR A 1 614 ? 24.103 65.894 48.304 1.00 22.60 ? 607 TYR A CE1 1 ATOM 4560 C CE2 . TYR A 1 614 ? 21.803 66.254 49.046 1.00 20.09 ? 607 TYR A CE2 1 ATOM 4561 C CZ . TYR A 1 614 ? 22.972 65.480 49.031 1.00 21.27 ? 607 TYR A CZ 1 ATOM 4562 O OH . TYR A 1 614 ? 22.984 64.297 49.725 1.00 22.35 ? 607 TYR A OH 1 ATOM 4563 N N . ALA A 1 615 ? 23.721 72.239 46.411 1.00 17.98 ? 608 ALA A N 1 ATOM 4564 C CA . ALA A 1 615 ? 23.540 73.484 45.711 1.00 18.88 ? 608 ALA A CA 1 ATOM 4565 C C . ALA A 1 615 ? 24.876 73.897 45.053 1.00 20.58 ? 608 ALA A C 1 ATOM 4566 O O . ALA A 1 615 ? 24.894 74.338 43.867 1.00 19.51 ? 608 ALA A O 1 ATOM 4567 C CB . ALA A 1 615 ? 23.036 74.588 46.690 1.00 18.81 ? 608 ALA A CB 1 ATOM 4568 N N . ASP A 1 616 ? 25.997 73.727 45.780 1.00 21.43 ? 609 ASP A N 1 ATOM 4569 C CA . ASP A 1 616 ? 27.337 74.048 45.181 1.00 23.21 ? 609 ASP A CA 1 ATOM 4570 C C . ASP A 1 616 ? 27.569 73.158 43.921 1.00 22.49 ? 609 ASP A C 1 ATOM 4571 O O . ASP A 1 616 ? 28.041 73.606 42.867 1.00 22.15 ? 609 ASP A O 1 ATOM 4572 C CB . ASP A 1 616 ? 28.496 73.803 46.168 1.00 23.86 ? 609 ASP A CB 1 ATOM 4573 C CG . ASP A 1 616 ? 28.564 74.828 47.304 1.00 27.39 ? 609 ASP A CG 1 ATOM 4574 O OD1 . ASP A 1 616 ? 28.032 75.928 47.203 1.00 28.45 ? 609 ASP A OD1 1 ATOM 4575 O OD2 . ASP A 1 616 ? 29.200 74.507 48.337 1.00 34.21 ? 609 ASP A OD2 1 ATOM 4576 N N . LYS A 1 617 ? 27.182 71.903 44.044 1.00 21.81 ? 610 LYS A N 1 ATOM 4577 C CA . LYS A 1 617 ? 27.396 70.949 42.999 1.00 22.06 ? 610 LYS A CA 1 ATOM 4578 C C . LYS A 1 617 ? 26.562 71.305 41.742 1.00 21.96 ? 610 LYS A C 1 ATOM 4579 O O . LYS A 1 617 ? 27.114 71.340 40.606 1.00 20.75 ? 610 LYS A O 1 ATOM 4580 C CB . LYS A 1 617 ? 27.059 69.556 43.509 1.00 22.25 ? 610 LYS A CB 1 ATOM 4581 C CG . LYS A 1 617 ? 27.345 68.460 42.491 1.00 26.71 ? 610 LYS A CG 1 ATOM 4582 C CD . LYS A 1 617 ? 26.527 67.214 42.812 1.00 32.69 ? 610 LYS A CD 1 ATOM 4583 C CE . LYS A 1 617 ? 27.226 65.961 42.312 1.00 38.93 ? 610 LYS A CE 1 ATOM 4584 N NZ . LYS A 1 617 ? 26.269 64.849 42.229 1.00 41.43 ? 610 LYS A NZ 1 ATOM 4585 N N . ILE A 1 618 ? 25.255 71.559 41.927 1.00 20.65 ? 611 ILE A N 1 ATOM 4586 C CA . ILE A 1 618 ? 24.420 71.852 40.790 1.00 20.96 ? 611 ILE A CA 1 ATOM 4587 C C . ILE A 1 618 ? 24.834 73.211 40.126 1.00 21.57 ? 611 ILE A C 1 ATOM 4588 O O . ILE A 1 618 ? 24.862 73.358 38.885 1.00 20.83 ? 611 ILE A O 1 ATOM 4589 C CB . ILE A 1 618 ? 22.877 71.777 41.143 1.00 20.94 ? 611 ILE A CB 1 ATOM 4590 C CG1 . ILE A 1 618 ? 22.038 71.747 39.846 1.00 21.78 ? 611 ILE A CG1 1 ATOM 4591 C CG2 . ILE A 1 618 ? 22.438 72.950 42.023 1.00 20.32 ? 611 ILE A CG2 1 ATOM 4592 C CD1 . ILE A 1 618 ? 22.243 70.446 39.030 1.00 21.74 ? 611 ILE A CD1 1 ATOM 4593 N N . TYR A 1 619 ? 25.146 74.198 40.952 1.00 22.05 ? 612 TYR A N 1 ATOM 4594 C CA . TYR A 1 619 ? 25.687 75.461 40.456 1.00 23.62 ? 612 TYR A CA 1 ATOM 4595 C C . TYR A 1 619 ? 26.944 75.204 39.594 1.00 23.66 ? 612 TYR A C 1 ATOM 4596 O O . TYR A 1 619 ? 27.104 75.798 38.508 1.00 22.57 ? 612 TYR A O 1 ATOM 4597 C CB . TYR A 1 619 ? 26.011 76.414 41.640 1.00 23.82 ? 612 TYR A CB 1 ATOM 4598 C CG . TYR A 1 619 ? 26.864 77.584 41.219 1.00 28.30 ? 612 TYR A CG 1 ATOM 4599 C CD1 . TYR A 1 619 ? 26.294 78.721 40.644 1.00 31.32 ? 612 TYR A CD1 1 ATOM 4600 C CD2 . TYR A 1 619 ? 28.263 77.534 41.371 1.00 33.15 ? 612 TYR A CD2 1 ATOM 4601 C CE1 . TYR A 1 619 ? 27.093 79.793 40.237 1.00 36.01 ? 612 TYR A CE1 1 ATOM 4602 C CE2 . TYR A 1 619 ? 29.085 78.599 40.968 1.00 37.85 ? 612 TYR A CE2 1 ATOM 4603 C CZ . TYR A 1 619 ? 28.490 79.714 40.404 1.00 39.67 ? 612 TYR A CZ 1 ATOM 4604 O OH . TYR A 1 619 ? 29.306 80.729 39.998 1.00 46.67 ? 612 TYR A OH 1 ATOM 4605 N N . SER A 1 620 ? 27.862 74.359 40.077 1.00 23.56 ? 613 SER A N 1 ATOM 4606 C CA . SER A 1 620 ? 29.120 74.184 39.322 1.00 24.74 ? 613 SER A CA 1 ATOM 4607 C C . SER A 1 620 ? 28.843 73.517 37.976 1.00 24.46 ? 613 SER A C 1 ATOM 4608 O O . SER A 1 620 ? 29.549 73.835 37.024 1.00 23.93 ? 613 SER A O 1 ATOM 4609 C CB . SER A 1 620 ? 30.235 73.406 40.058 1.00 25.13 ? 613 SER A CB 1 ATOM 4610 O OG A SER A 1 620 ? 30.472 73.918 41.353 0.50 25.56 ? 613 SER A OG 1 ATOM 4611 O OG B SER A 1 620 ? 29.806 72.088 40.323 0.50 26.53 ? 613 SER A OG 1 ATOM 4612 N N . ILE A 1 621 ? 27.843 72.607 37.909 1.00 23.44 ? 614 ILE A N 1 ATOM 4613 C CA . ILE A 1 621 ? 27.429 72.010 36.644 1.00 23.34 ? 614 ILE A CA 1 ATOM 4614 C C . ILE A 1 621 ? 26.928 73.090 35.653 1.00 23.72 ? 614 ILE A C 1 ATOM 4615 O O . ILE A 1 621 ? 27.363 73.138 34.489 1.00 24.41 ? 614 ILE A O 1 ATOM 4616 C CB . ILE A 1 621 ? 26.339 70.921 36.839 1.00 23.57 ? 614 ILE A CB 1 ATOM 4617 C CG1 . ILE A 1 621 ? 26.938 69.653 37.497 1.00 22.48 ? 614 ILE A CG1 1 ATOM 4618 C CG2 . ILE A 1 621 ? 25.686 70.577 35.465 1.00 24.34 ? 614 ILE A CG2 1 ATOM 4619 C CD1 . ILE A 1 621 ? 25.877 68.663 38.100 1.00 21.24 ? 614 ILE A CD1 1 ATOM 4620 N N . SER A 1 622 ? 26.024 73.950 36.103 1.00 22.42 ? 615 SER A N 1 ATOM 4621 C CA . SER A 1 622 ? 25.525 75.028 35.275 1.00 23.19 ? 615 SER A CA 1 ATOM 4622 C C . SER A 1 622 ? 26.645 75.942 34.817 1.00 24.60 ? 615 SER A C 1 ATOM 4623 O O . SER A 1 622 ? 26.646 76.423 33.665 1.00 24.07 ? 615 SER A O 1 ATOM 4624 C CB . SER A 1 622 ? 24.467 75.812 36.056 1.00 22.81 ? 615 SER A CB 1 ATOM 4625 O OG . SER A 1 622 ? 23.881 76.826 35.252 1.00 23.98 ? 615 SER A OG 1 ATOM 4626 N N . MET A 1 623 ? 27.608 76.186 35.705 1.00 25.81 ? 616 MET A N 1 ATOM 4627 C CA . MET A 1 623 ? 28.717 77.109 35.380 1.00 27.63 ? 616 MET A CA 1 ATOM 4628 C C . MET A 1 623 ? 29.689 76.601 34.310 1.00 28.68 ? 616 MET A C 1 ATOM 4629 O O . MET A 1 623 ? 30.558 77.336 33.897 1.00 28.21 ? 616 MET A O 1 ATOM 4630 C CB . MET A 1 623 ? 29.436 77.595 36.616 1.00 27.49 ? 616 MET A CB 1 ATOM 4631 C CG . MET A 1 623 ? 28.706 78.768 37.279 0.80 30.79 ? 616 MET A CG 1 ATOM 4632 S SD . MET A 1 623 ? 28.608 80.322 36.297 0.80 37.89 ? 616 MET A SD 1 ATOM 4633 C CE . MET A 1 623 ? 30.343 80.659 35.985 0.80 34.84 ? 616 MET A CE 1 ATOM 4634 N N . LYS A 1 624 ? 29.486 75.380 33.812 1.00 29.84 ? 617 LYS A N 1 ATOM 4635 C CA . LYS A 1 624 ? 30.167 74.956 32.574 1.00 31.99 ? 617 LYS A CA 1 ATOM 4636 C C . LYS A 1 624 ? 29.655 75.717 31.317 1.00 30.84 ? 617 LYS A C 1 ATOM 4637 O O . LYS A 1 624 ? 30.284 75.637 30.275 1.00 29.89 ? 617 LYS A O 1 ATOM 4638 C CB . LYS A 1 624 ? 30.068 73.430 32.346 1.00 33.65 ? 617 LYS A CB 1 ATOM 4639 C CG . LYS A 1 624 ? 30.716 72.554 33.440 1.00 38.75 ? 617 LYS A CG 1 ATOM 4640 C CD . LYS A 1 624 ? 30.806 71.033 33.022 1.00 45.70 ? 617 LYS A CD 1 ATOM 4641 C CE . LYS A 1 624 ? 29.600 70.151 33.457 1.00 49.65 ? 617 LYS A CE 1 ATOM 4642 N NZ . LYS A 1 624 ? 28.308 70.649 32.873 1.00 51.68 ? 617 LYS A NZ 1 ATOM 4643 N N . HIS A 1 625 ? 28.541 76.460 31.439 1.00 28.97 ? 618 HIS A N 1 ATOM 4644 C CA . HIS A 1 625 ? 27.915 77.217 30.334 1.00 27.45 ? 618 HIS A CA 1 ATOM 4645 C C . HIS A 1 625 ? 27.771 78.703 30.716 1.00 27.33 ? 618 HIS A C 1 ATOM 4646 O O . HIS A 1 625 ? 26.656 79.233 30.759 1.00 24.90 ? 618 HIS A O 1 ATOM 4647 C CB . HIS A 1 625 ? 26.525 76.626 30.036 1.00 26.92 ? 618 HIS A CB 1 ATOM 4648 C CG . HIS A 1 625 ? 26.486 75.119 30.107 1.00 27.95 ? 618 HIS A CG 1 ATOM 4649 N ND1 . HIS A 1 625 ? 26.799 74.313 29.031 1.00 27.74 ? 618 HIS A ND1 1 ATOM 4650 C CD2 . HIS A 1 625 ? 26.198 74.274 31.138 1.00 28.62 ? 618 HIS A CD2 1 ATOM 4651 C CE1 . HIS A 1 625 ? 26.704 73.038 29.389 1.00 29.61 ? 618 HIS A CE1 1 ATOM 4652 N NE2 . HIS A 1 625 ? 26.329 72.985 30.662 1.00 29.13 ? 618 HIS A NE2 1 ATOM 4653 N N . PRO A 1 626 ? 28.905 79.382 31.001 1.00 27.36 ? 619 PRO A N 1 ATOM 4654 C CA . PRO A 1 626 ? 28.770 80.762 31.493 1.00 27.89 ? 619 PRO A CA 1 ATOM 4655 C C . PRO A 1 626 ? 28.101 81.713 30.483 1.00 28.64 ? 619 PRO A C 1 ATOM 4656 O O . PRO A 1 626 ? 27.349 82.602 30.924 1.00 28.54 ? 619 PRO A O 1 ATOM 4657 C CB . PRO A 1 626 ? 30.231 81.200 31.763 1.00 28.42 ? 619 PRO A CB 1 ATOM 4658 C CG . PRO A 1 626 ? 31.080 80.288 30.832 1.00 28.11 ? 619 PRO A CG 1 ATOM 4659 C CD . PRO A 1 626 ? 30.315 78.966 30.889 1.00 27.47 ? 619 PRO A CD 1 ATOM 4660 N N . GLN A 1 627 ? 28.352 81.547 29.164 1.00 28.38 ? 620 GLN A N 1 ATOM 4661 C CA . GLN A 1 627 ? 27.696 82.425 28.158 1.00 28.73 ? 620 GLN A CA 1 ATOM 4662 C C . GLN A 1 627 ? 26.162 82.302 28.204 1.00 27.59 ? 620 GLN A C 1 ATOM 4663 O O . GLN A 1 627 ? 25.469 83.327 28.156 1.00 25.90 ? 620 GLN A O 1 ATOM 4664 C CB . GLN A 1 627 ? 28.239 82.239 26.714 1.00 30.10 ? 620 GLN A CB 1 ATOM 4665 C CG . GLN A 1 627 ? 27.781 83.332 25.656 0.70 33.18 ? 620 GLN A CG 1 ATOM 4666 C CD . GLN A 1 627 ? 27.863 84.803 26.146 0.70 35.51 ? 620 GLN A CD 1 ATOM 4667 O OE1 . GLN A 1 627 ? 26.836 85.425 26.475 0.60 35.16 ? 620 GLN A OE1 1 ATOM 4668 N NE2 . GLN A 1 627 ? 29.083 85.349 26.211 0.60 35.76 ? 620 GLN A NE2 1 ATOM 4669 N N . GLU A 1 628 ? 25.639 81.068 28.311 1.00 25.65 ? 621 GLU A N 1 ATOM 4670 C CA . GLU A 1 628 ? 24.206 80.891 28.356 1.00 26.14 ? 621 GLU A CA 1 ATOM 4671 C C . GLU A 1 628 ? 23.610 81.435 29.662 1.00 25.41 ? 621 GLU A C 1 ATOM 4672 O O . GLU A 1 628 ? 22.477 82.007 29.683 1.00 23.89 ? 621 GLU A O 1 ATOM 4673 C CB . GLU A 1 628 ? 23.826 79.408 28.182 1.00 26.77 ? 621 GLU A CB 1 ATOM 4674 C CG . GLU A 1 628 ? 24.133 78.851 26.755 1.00 30.86 ? 621 GLU A CG 1 ATOM 4675 C CD . GLU A 1 628 ? 25.605 78.736 26.392 1.00 34.55 ? 621 GLU A CD 1 ATOM 4676 O OE1 . GLU A 1 628 ? 26.497 78.522 27.251 1.00 34.35 ? 621 GLU A OE1 1 ATOM 4677 O OE2 . GLU A 1 628 ? 25.883 78.863 25.185 1.00 41.77 ? 621 GLU A OE2 1 ATOM 4678 N N . MET A 1 629 ? 24.325 81.209 30.768 1.00 24.48 ? 622 MET A N 1 ATOM 4679 C CA . MET A 1 629 ? 23.874 81.785 32.045 1.00 24.13 ? 622 MET A CA 1 ATOM 4680 C C . MET A 1 629 ? 23.741 83.303 31.935 1.00 24.66 ? 622 MET A C 1 ATOM 4681 O O . MET A 1 629 ? 22.794 83.872 32.466 1.00 23.55 ? 622 MET A O 1 ATOM 4682 C CB . MET A 1 629 ? 24.783 81.382 33.202 1.00 23.66 ? 622 MET A CB 1 ATOM 4683 C CG . MET A 1 629 ? 24.639 79.853 33.551 1.00 21.87 ? 622 MET A CG 1 ATOM 4684 S SD . MET A 1 629 ? 25.623 79.384 35.003 1.00 24.40 ? 622 MET A SD 1 ATOM 4685 C CE . MET A 1 629 ? 24.840 80.389 36.305 1.00 19.22 ? 622 MET A CE 1 ATOM 4686 N N . LYS A 1 630 ? 24.674 83.956 31.238 1.00 25.70 ? 623 LYS A N 1 ATOM 4687 C CA . LYS A 1 630 ? 24.568 85.407 31.009 1.00 27.49 ? 623 LYS A CA 1 ATOM 4688 C C . LYS A 1 630 ? 23.383 85.756 30.091 1.00 27.79 ? 623 LYS A C 1 ATOM 4689 O O . LYS A 1 630 ? 22.581 86.640 30.417 1.00 26.90 ? 623 LYS A O 1 ATOM 4690 C CB . LYS A 1 630 ? 25.847 85.979 30.406 1.00 27.35 ? 623 LYS A CB 1 ATOM 4691 C CG . LYS A 1 630 ? 27.087 85.853 31.255 1.00 28.75 ? 623 LYS A CG 1 ATOM 4692 C CD . LYS A 1 630 ? 28.263 86.407 30.466 1.00 31.66 ? 623 LYS A CD 1 ATOM 4693 C CE . LYS A 1 630 ? 29.512 86.489 31.316 1.00 35.93 ? 623 LYS A CE 1 ATOM 4694 N NZ . LYS A 1 630 ? 30.111 85.173 31.616 1.00 40.97 ? 623 LYS A NZ 1 ATOM 4695 N N . THR A 1 631 ? 23.284 85.049 28.957 1.00 28.32 ? 624 THR A N 1 ATOM 4696 C CA . THR A 1 631 ? 22.259 85.346 27.938 1.00 29.25 ? 624 THR A CA 1 ATOM 4697 C C . THR A 1 631 ? 20.854 85.183 28.484 1.00 28.30 ? 624 THR A C 1 ATOM 4698 O O . THR A 1 631 ? 19.969 86.021 28.240 1.00 27.84 ? 624 THR A O 1 ATOM 4699 C CB . THR A 1 631 ? 22.406 84.424 26.688 1.00 30.12 ? 624 THR A CB 1 ATOM 4700 O OG1 . THR A 1 631 ? 23.706 84.603 26.124 1.00 31.68 ? 624 THR A OG1 1 ATOM 4701 C CG2 . THR A 1 631 ? 21.370 84.790 25.622 1.00 32.23 ? 624 THR A CG2 1 ATOM 4702 N N . TYR A 1 632 ? 20.651 84.110 29.245 1.00 26.26 ? 625 TYR A N 1 ATOM 4703 C CA . TYR A 1 632 ? 19.318 83.795 29.752 1.00 26.50 ? 625 TYR A CA 1 ATOM 4704 C C . TYR A 1 632 ? 19.091 84.211 31.204 1.00 25.26 ? 625 TYR A C 1 ATOM 4705 O O . TYR A 1 632 ? 18.040 83.910 31.758 1.00 23.31 ? 625 TYR A O 1 ATOM 4706 C CB . TYR A 1 632 ? 18.974 82.306 29.530 1.00 25.94 ? 625 TYR A CB 1 ATOM 4707 C CG . TYR A 1 632 ? 19.093 81.976 28.051 1.00 28.88 ? 625 TYR A CG 1 ATOM 4708 C CD1 . TYR A 1 632 ? 18.210 82.557 27.114 1.00 29.01 ? 625 TYR A CD1 1 ATOM 4709 C CD2 . TYR A 1 632 ? 20.099 81.128 27.585 1.00 29.87 ? 625 TYR A CD2 1 ATOM 4710 C CE1 . TYR A 1 632 ? 18.319 82.280 25.735 1.00 31.98 ? 625 TYR A CE1 1 ATOM 4711 C CE2 . TYR A 1 632 ? 20.223 80.839 26.210 1.00 32.62 ? 625 TYR A CE2 1 ATOM 4712 C CZ . TYR A 1 632 ? 19.327 81.411 25.294 1.00 33.24 ? 625 TYR A CZ 1 ATOM 4713 O OH . TYR A 1 632 ? 19.467 81.130 23.950 1.00 35.02 ? 625 TYR A OH 1 ATOM 4714 N N . SER A 1 633 ? 20.080 84.893 31.798 1.00 23.40 ? 626 SER A N 1 ATOM 4715 C CA . SER A 1 633 ? 19.921 85.454 33.138 1.00 22.76 ? 626 SER A CA 1 ATOM 4716 C C . SER A 1 633 ? 19.629 84.324 34.157 1.00 22.72 ? 626 SER A C 1 ATOM 4717 O O . SER A 1 633 ? 18.691 84.390 34.947 1.00 22.10 ? 626 SER A O 1 ATOM 4718 C CB A SER A 1 633 ? 18.814 86.517 33.147 0.65 22.49 ? 626 SER A CB 1 ATOM 4719 C CB B SER A 1 633 ? 18.823 86.522 33.131 0.35 23.38 ? 626 SER A CB 1 ATOM 4720 O OG A SER A 1 633 ? 19.209 87.650 32.405 0.65 19.29 ? 626 SER A OG 1 ATOM 4721 O OG B SER A 1 633 ? 18.599 87.011 34.431 0.35 25.58 ? 626 SER A OG 1 ATOM 4722 N N . VAL A 1 634 ? 20.416 83.252 34.081 1.00 22.09 ? 627 VAL A N 1 ATOM 4723 C CA . VAL A 1 634 ? 20.240 82.087 34.953 1.00 22.58 ? 627 VAL A CA 1 ATOM 4724 C C . VAL A 1 634 ? 20.966 82.352 36.296 1.00 23.43 ? 627 VAL A C 1 ATOM 4725 O O . VAL A 1 634 ? 22.211 82.436 36.328 1.00 23.43 ? 627 VAL A O 1 ATOM 4726 C CB . VAL A 1 634 ? 20.811 80.809 34.261 1.00 22.45 ? 627 VAL A CB 1 ATOM 4727 C CG1 . VAL A 1 634 ? 20.532 79.525 35.102 1.00 19.73 ? 627 VAL A CG1 1 ATOM 4728 C CG2 . VAL A 1 634 ? 20.220 80.702 32.856 1.00 22.09 ? 627 VAL A CG2 1 ATOM 4729 N N . SER A 1 635 ? 20.191 82.550 37.356 1.00 23.46 ? 628 SER A N 1 ATOM 4730 C CA . SER A 1 635 ? 20.728 82.809 38.707 1.00 24.42 ? 628 SER A CA 1 ATOM 4731 C C . SER A 1 635 ? 20.353 81.697 39.674 1.00 23.55 ? 628 SER A C 1 ATOM 4732 O O . SER A 1 635 ? 19.189 81.258 39.706 1.00 23.73 ? 628 SER A O 1 ATOM 4733 C CB . SER A 1 635 ? 20.161 84.096 39.281 1.00 25.52 ? 628 SER A CB 1 ATOM 4734 O OG . SER A 1 635 ? 20.880 84.363 40.470 1.00 29.65 ? 628 SER A OG 1 ATOM 4735 N N . PHE A 1 636 ? 21.336 81.226 40.430 1.00 23.14 ? 629 PHE A N 1 ATOM 4736 C CA . PHE A 1 636 ? 21.118 80.297 41.564 1.00 21.73 ? 629 PHE A CA 1 ATOM 4737 C C . PHE A 1 636 ? 20.905 81.053 42.905 1.00 22.00 ? 629 PHE A C 1 ATOM 4738 O O . PHE A 1 636 ? 20.812 80.420 43.968 1.00 20.80 ? 629 PHE A O 1 ATOM 4739 C CB . PHE A 1 636 ? 22.288 79.297 41.645 1.00 20.84 ? 629 PHE A CB 1 ATOM 4740 C CG . PHE A 1 636 ? 22.196 78.215 40.596 1.00 21.18 ? 629 PHE A CG 1 ATOM 4741 C CD1 . PHE A 1 636 ? 21.631 76.985 40.893 1.00 18.98 ? 629 PHE A CD1 1 ATOM 4742 C CD2 . PHE A 1 636 ? 22.645 78.465 39.290 1.00 21.32 ? 629 PHE A CD2 1 ATOM 4743 C CE1 . PHE A 1 636 ? 21.503 75.965 39.903 1.00 18.46 ? 629 PHE A CE1 1 ATOM 4744 C CE2 . PHE A 1 636 ? 22.547 77.460 38.296 1.00 20.08 ? 629 PHE A CE2 1 ATOM 4745 C CZ . PHE A 1 636 ? 21.964 76.212 38.612 1.00 19.78 ? 629 PHE A CZ 1 ATOM 4746 N N . ASP A 1 637 ? 20.773 82.388 42.840 1.00 22.03 ? 630 ASP A N 1 ATOM 4747 C CA . ASP A 1 637 ? 20.673 83.206 44.079 1.00 23.29 ? 630 ASP A CA 1 ATOM 4748 C C . ASP A 1 637 ? 19.547 82.730 45.005 1.00 22.87 ? 630 ASP A C 1 ATOM 4749 O O . ASP A 1 637 ? 19.733 82.600 46.235 1.00 23.33 ? 630 ASP A O 1 ATOM 4750 C CB . ASP A 1 637 ? 20.543 84.709 43.783 1.00 23.26 ? 630 ASP A CB 1 ATOM 4751 C CG . ASP A 1 637 ? 21.878 85.362 43.325 1.00 27.41 ? 630 ASP A CG 1 ATOM 4752 O OD1 . ASP A 1 637 ? 22.984 84.740 43.341 1.00 30.07 ? 630 ASP A OD1 1 ATOM 4753 O OD2 . ASP A 1 637 ? 21.826 86.556 42.951 1.00 32.70 ? 630 ASP A OD2 1 ATOM 4754 N N . SER A 1 638 ? 18.375 82.476 44.431 1.00 21.71 ? 631 SER A N 1 ATOM 4755 C CA . SER A 1 638 ? 17.237 82.030 45.243 1.00 21.19 ? 631 SER A CA 1 ATOM 4756 C C . SER A 1 638 ? 17.488 80.671 45.949 1.00 20.32 ? 631 SER A C 1 ATOM 4757 O O . SER A 1 638 ? 17.078 80.495 47.120 1.00 19.37 ? 631 SER A O 1 ATOM 4758 C CB . SER A 1 638 ? 15.954 82.001 44.422 1.00 21.02 ? 631 SER A CB 1 ATOM 4759 O OG . SER A 1 638 ? 16.050 80.959 43.428 1.00 23.24 ? 631 SER A OG 1 ATOM 4760 N N . LEU A 1 639 ? 18.150 79.726 45.272 1.00 18.89 ? 632 LEU A N 1 ATOM 4761 C CA . LEU A 1 639 ? 18.430 78.440 45.896 1.00 18.76 ? 632 LEU A CA 1 ATOM 4762 C C . LEU A 1 639 ? 19.428 78.612 47.058 1.00 19.90 ? 632 LEU A C 1 ATOM 4763 O O . LEU A 1 639 ? 19.247 78.044 48.151 1.00 20.06 ? 632 LEU A O 1 ATOM 4764 C CB . LEU A 1 639 ? 18.988 77.449 44.889 1.00 18.97 ? 632 LEU A CB 1 ATOM 4765 C CG . LEU A 1 639 ? 19.293 76.036 45.396 1.00 17.54 ? 632 LEU A CG 1 ATOM 4766 C CD1 . LEU A 1 639 ? 18.054 75.396 46.019 1.00 15.41 ? 632 LEU A CD1 1 ATOM 4767 C CD2 . LEU A 1 639 ? 19.759 75.154 44.191 1.00 19.03 ? 632 LEU A CD2 1 ATOM 4768 N N . PHE A 1 640 ? 20.471 79.413 46.848 1.00 19.65 ? 633 PHE A N 1 ATOM 4769 C CA . PHE A 1 640 ? 21.444 79.586 47.924 1.00 20.82 ? 633 PHE A CA 1 ATOM 4770 C C . PHE A 1 640 ? 20.799 80.328 49.095 1.00 20.32 ? 633 PHE A C 1 ATOM 4771 O O . PHE A 1 640 ? 21.095 80.044 50.274 1.00 20.45 ? 633 PHE A O 1 ATOM 4772 C CB . PHE A 1 640 ? 22.709 80.299 47.428 1.00 20.84 ? 633 PHE A CB 1 ATOM 4773 C CG . PHE A 1 640 ? 23.625 79.396 46.645 1.00 22.76 ? 633 PHE A CG 1 ATOM 4774 C CD1 . PHE A 1 640 ? 24.404 78.435 47.308 1.00 22.90 ? 633 PHE A CD1 1 ATOM 4775 C CD2 . PHE A 1 640 ? 23.739 79.519 45.245 1.00 23.78 ? 633 PHE A CD2 1 ATOM 4776 C CE1 . PHE A 1 640 ? 25.255 77.565 46.599 1.00 21.97 ? 633 PHE A CE1 1 ATOM 4777 C CE2 . PHE A 1 640 ? 24.612 78.668 44.515 1.00 22.02 ? 633 PHE A CE2 1 ATOM 4778 C CZ . PHE A 1 640 ? 25.373 77.697 45.206 1.00 23.33 ? 633 PHE A CZ 1 ATOM 4779 N N . SER A 1 641 ? 19.921 81.277 48.776 1.00 19.33 ? 634 SER A N 1 ATOM 4780 C CA . SER A 1 641 ? 19.172 82.016 49.827 1.00 19.62 ? 634 SER A CA 1 ATOM 4781 C C . SER A 1 641 ? 18.271 81.054 50.644 1.00 19.03 ? 634 SER A C 1 ATOM 4782 O O . SER A 1 641 ? 18.217 81.116 51.876 1.00 20.00 ? 634 SER A O 1 ATOM 4783 C CB . SER A 1 641 ? 18.344 83.141 49.187 1.00 19.29 ? 634 SER A CB 1 ATOM 4784 O OG . SER A 1 641 ? 17.445 83.688 50.136 1.00 21.08 ? 634 SER A OG 1 ATOM 4785 N N . ALA A 1 642 ? 17.578 80.160 49.963 1.00 17.56 ? 635 ALA A N 1 ATOM 4786 C CA . ALA A 1 642 ? 16.697 79.180 50.631 1.00 17.66 ? 635 ALA A CA 1 ATOM 4787 C C . ALA A 1 642 ? 17.559 78.269 51.539 1.00 18.30 ? 635 ALA A C 1 ATOM 4788 O O . ALA A 1 642 ? 17.172 77.956 52.697 1.00 18.79 ? 635 ALA A O 1 ATOM 4789 C CB . ALA A 1 642 ? 15.918 78.312 49.563 1.00 16.65 ? 635 ALA A CB 1 ATOM 4790 N N . VAL A 1 643 ? 18.715 77.841 51.023 1.00 18.46 ? 636 VAL A N 1 ATOM 4791 C CA . VAL A 1 643 ? 19.629 76.940 51.796 1.00 18.68 ? 636 VAL A CA 1 ATOM 4792 C C . VAL A 1 643 ? 20.177 77.665 53.053 1.00 19.81 ? 636 VAL A C 1 ATOM 4793 O O . VAL A 1 643 ? 20.261 77.089 54.151 1.00 19.79 ? 636 VAL A O 1 ATOM 4794 C CB . VAL A 1 643 ? 20.753 76.382 50.900 1.00 18.30 ? 636 VAL A CB 1 ATOM 4795 C CG1 . VAL A 1 643 ? 21.768 75.655 51.709 1.00 18.32 ? 636 VAL A CG1 1 ATOM 4796 C CG2 . VAL A 1 643 ? 20.143 75.408 49.814 1.00 18.48 ? 636 VAL A CG2 1 ATOM 4797 N N . LYS A 1 644 ? 20.576 78.924 52.888 1.00 19.90 ? 637 LYS A N 1 ATOM 4798 C CA . LYS A 1 644 ? 20.968 79.766 53.999 1.00 20.57 ? 637 LYS A CA 1 ATOM 4799 C C . LYS A 1 644 ? 19.846 79.886 55.035 1.00 20.81 ? 637 LYS A C 1 ATOM 4800 O O . LYS A 1 644 ? 20.105 79.784 56.244 1.00 21.34 ? 637 LYS A O 1 ATOM 4801 C CB . LYS A 1 644 ? 21.404 81.155 53.477 1.00 20.43 ? 637 LYS A CB 1 ATOM 4802 C CG . LYS A 1 644 ? 21.802 82.169 54.529 1.00 26.34 ? 637 LYS A CG 1 ATOM 4803 C CD . LYS A 1 644 ? 22.285 83.510 53.811 1.00 31.27 ? 637 LYS A CD 1 ATOM 4804 C CE . LYS A 1 644 ? 22.738 84.582 54.799 1.00 37.24 ? 637 LYS A CE 1 ATOM 4805 N NZ . LYS A 1 644 ? 21.549 85.069 55.606 1.00 41.85 ? 637 LYS A NZ 1 ATOM 4806 N N . ASN A 1 645 ? 18.606 80.126 54.585 1.00 20.26 ? 638 ASN A N 1 ATOM 4807 C CA . ASN A 1 645 ? 17.477 80.237 55.517 1.00 20.30 ? 638 ASN A CA 1 ATOM 4808 C C . ASN A 1 645 ? 17.222 78.907 56.248 1.00 19.94 ? 638 ASN A C 1 ATOM 4809 O O . ASN A 1 645 ? 17.019 78.898 57.464 1.00 18.70 ? 638 ASN A O 1 ATOM 4810 C CB . ASN A 1 645 ? 16.211 80.656 54.811 1.00 18.96 ? 638 ASN A CB 1 ATOM 4811 C CG . ASN A 1 645 ? 16.290 82.055 54.300 1.00 22.01 ? 638 ASN A CG 1 ATOM 4812 O OD1 . ASN A 1 645 ? 17.211 82.803 54.661 1.00 21.74 ? 638 ASN A OD1 1 ATOM 4813 N ND2 . ASN A 1 645 ? 15.341 82.433 53.444 1.00 22.41 ? 638 ASN A ND2 1 ATOM 4814 N N . PHE A 1 646 ? 17.253 77.808 55.497 1.00 19.51 ? 639 PHE A N 1 ATOM 4815 C CA . PHE A 1 646 ? 17.104 76.483 56.069 1.00 19.65 ? 639 PHE A CA 1 ATOM 4816 C C . PHE A 1 646 ? 18.142 76.286 57.196 1.00 21.16 ? 639 PHE A C 1 ATOM 4817 O O . PHE A 1 646 ? 17.800 75.838 58.321 1.00 20.34 ? 639 PHE A O 1 ATOM 4818 C CB . PHE A 1 646 ? 17.245 75.419 54.977 1.00 19.07 ? 639 PHE A CB 1 ATOM 4819 C CG . PHE A 1 646 ? 16.890 74.020 55.446 1.00 19.79 ? 639 PHE A CG 1 ATOM 4820 C CD1 . PHE A 1 646 ? 15.663 73.439 55.078 1.00 18.05 ? 639 PHE A CD1 1 ATOM 4821 C CD2 . PHE A 1 646 ? 17.750 73.309 56.301 1.00 18.61 ? 639 PHE A CD2 1 ATOM 4822 C CE1 . PHE A 1 646 ? 15.298 72.160 55.525 1.00 20.92 ? 639 PHE A CE1 1 ATOM 4823 C CE2 . PHE A 1 646 ? 17.397 72.013 56.768 1.00 19.02 ? 639 PHE A CE2 1 ATOM 4824 C CZ . PHE A 1 646 ? 16.149 71.437 56.386 1.00 18.73 ? 639 PHE A CZ 1 ATOM 4825 N N . THR A 1 647 ? 19.408 76.616 56.903 1.00 22.06 ? 640 THR A N 1 ATOM 4826 C CA . THR A 1 647 ? 20.496 76.489 57.898 1.00 22.53 ? 640 THR A CA 1 ATOM 4827 C C . THR A 1 647 ? 20.185 77.293 59.185 1.00 23.41 ? 640 THR A C 1 ATOM 4828 O O . THR A 1 647 ? 20.283 76.768 60.304 1.00 23.50 ? 640 THR A O 1 ATOM 4829 C CB . THR A 1 647 ? 21.865 76.937 57.286 1.00 22.43 ? 640 THR A CB 1 ATOM 4830 O OG1 . THR A 1 647 ? 22.107 76.208 56.074 1.00 23.92 ? 640 THR A OG1 1 ATOM 4831 C CG2 . THR A 1 647 ? 23.065 76.681 58.258 1.00 23.25 ? 640 THR A CG2 1 ATOM 4832 N N . GLU A 1 648 ? 19.796 78.553 59.011 1.00 23.33 ? 641 GLU A N 1 ATOM 4833 C CA . GLU A 1 648 ? 19.487 79.435 60.144 1.00 24.55 ? 641 GLU A CA 1 ATOM 4834 C C . GLU A 1 648 ? 18.288 78.893 60.950 1.00 23.86 ? 641 GLU A C 1 ATOM 4835 O O . GLU A 1 648 ? 18.322 78.850 62.177 1.00 23.60 ? 641 GLU A O 1 ATOM 4836 C CB . GLU A 1 648 ? 19.207 80.901 59.657 1.00 24.72 ? 641 GLU A CB 1 ATOM 4837 C CG . GLU A 1 648 ? 20.527 81.572 59.194 0.80 29.33 ? 641 GLU A CG 1 ATOM 4838 C CD . GLU A 1 648 ? 20.352 82.907 58.488 0.80 34.91 ? 641 GLU A CD 1 ATOM 4839 O OE1 . GLU A 1 648 ? 21.388 83.498 58.109 0.80 36.26 ? 641 GLU A OE1 1 ATOM 4840 O OE2 . GLU A 1 648 ? 19.195 83.350 58.295 0.80 39.03 ? 641 GLU A OE2 1 ATOM 4841 N N . ILE A 1 649 ? 17.221 78.509 60.255 1.00 23.67 ? 642 ILE A N 1 ATOM 4842 C CA . ILE A 1 649 ? 15.988 78.085 60.936 1.00 22.65 ? 642 ILE A CA 1 ATOM 4843 C C . ILE A 1 649 ? 16.242 76.727 61.617 1.00 22.84 ? 642 ILE A C 1 ATOM 4844 O O . ILE A 1 649 ? 15.786 76.503 62.740 1.00 22.56 ? 642 ILE A O 1 ATOM 4845 C CB . ILE A 1 649 ? 14.769 78.036 59.984 1.00 22.78 ? 642 ILE A CB 1 ATOM 4846 C CG1 . ILE A 1 649 ? 14.364 79.455 59.558 1.00 22.36 ? 642 ILE A CG1 1 ATOM 4847 C CG2 . ILE A 1 649 ? 13.530 77.336 60.639 1.00 20.97 ? 642 ILE A CG2 1 ATOM 4848 C CD1 . ILE A 1 649 ? 13.496 79.407 58.294 1.00 21.42 ? 642 ILE A CD1 1 ATOM 4849 N N . ALA A 1 650 ? 16.952 75.840 60.944 1.00 22.13 ? 643 ALA A N 1 ATOM 4850 C CA . ALA A 1 650 ? 17.285 74.537 61.539 1.00 23.85 ? 643 ALA A CA 1 ATOM 4851 C C . ALA A 1 650 ? 18.084 74.714 62.815 1.00 25.18 ? 643 ALA A C 1 ATOM 4852 O O . ALA A 1 650 ? 17.862 73.993 63.806 1.00 26.67 ? 643 ALA A O 1 ATOM 4853 C CB . ALA A 1 650 ? 18.092 73.607 60.534 1.00 23.38 ? 643 ALA A CB 1 ATOM 4854 N N . SER A 1 651 ? 19.026 75.658 62.801 1.00 25.58 ? 644 SER A N 1 ATOM 4855 C CA . SER A 1 651 ? 19.860 75.881 63.951 1.00 26.88 ? 644 SER A CA 1 ATOM 4856 C C . SER A 1 651 ? 19.000 76.400 65.137 1.00 26.46 ? 644 SER A C 1 ATOM 4857 O O . SER A 1 651 ? 19.108 75.902 66.260 1.00 26.94 ? 644 SER A O 1 ATOM 4858 C CB . SER A 1 651 ? 20.982 76.853 63.567 1.00 27.62 ? 644 SER A CB 1 ATOM 4859 O OG . SER A 1 651 ? 21.696 77.217 64.707 1.00 32.71 ? 644 SER A OG 1 ATOM 4860 N N . LYS A 1 652 ? 18.116 77.351 64.881 1.00 25.57 ? 645 LYS A N 1 ATOM 4861 C CA . LYS A 1 652 ? 17.169 77.817 65.910 1.00 26.39 ? 645 LYS A CA 1 ATOM 4862 C C . LYS A 1 652 ? 16.207 76.702 66.422 1.00 25.84 ? 645 LYS A C 1 ATOM 4863 O O . LYS A 1 652 ? 15.966 76.589 67.635 1.00 25.52 ? 645 LYS A O 1 ATOM 4864 C CB . LYS A 1 652 ? 16.390 79.030 65.402 1.00 26.07 ? 645 LYS A CB 1 ATOM 4865 C CG . LYS A 1 652 ? 17.260 80.313 65.249 1.00 28.09 ? 645 LYS A CG 1 ATOM 4866 C CD . LYS A 1 652 ? 17.679 80.865 66.613 0.68 30.32 ? 645 LYS A CD 1 ATOM 4867 C CE . LYS A 1 652 ? 18.837 81.850 66.502 0.33 31.33 ? 645 LYS A CE 1 ATOM 4868 N NZ . LYS A 1 652 ? 19.502 81.996 67.828 0.33 32.27 ? 645 LYS A NZ 1 ATOM 4869 N N . PHE A 1 653 ? 15.680 75.881 65.516 1.00 24.66 ? 646 PHE A N 1 ATOM 4870 C CA . PHE A 1 653 ? 14.854 74.744 65.931 1.00 24.54 ? 646 PHE A CA 1 ATOM 4871 C C . PHE A 1 653 ? 15.642 73.798 66.855 1.00 25.50 ? 646 PHE A C 1 ATOM 4872 O O . PHE A 1 653 ? 15.114 73.310 67.867 1.00 25.33 ? 646 PHE A O 1 ATOM 4873 C CB . PHE A 1 653 ? 14.384 73.969 64.710 1.00 24.92 ? 646 PHE A CB 1 ATOM 4874 C CG . PHE A 1 653 ? 13.510 72.776 65.031 1.00 24.43 ? 646 PHE A CG 1 ATOM 4875 C CD1 . PHE A 1 653 ? 12.130 72.931 65.209 1.00 23.56 ? 646 PHE A CD1 1 ATOM 4876 C CD2 . PHE A 1 653 ? 14.075 71.506 65.149 1.00 23.25 ? 646 PHE A CD2 1 ATOM 4877 C CE1 . PHE A 1 653 ? 11.324 71.821 65.488 1.00 22.90 ? 646 PHE A CE1 1 ATOM 4878 C CE2 . PHE A 1 653 ? 13.281 70.368 65.440 1.00 23.41 ? 646 PHE A CE2 1 ATOM 4879 C CZ . PHE A 1 653 ? 11.897 70.532 65.604 1.00 23.35 ? 646 PHE A CZ 1 ATOM 4880 N N . SER A 1 654 ? 16.895 73.519 66.501 1.00 25.41 ? 647 SER A N 1 ATOM 4881 C CA . SER A 1 654 ? 17.708 72.622 67.336 1.00 27.22 ? 647 SER A CA 1 ATOM 4882 C C . SER A 1 654 ? 17.847 73.173 68.771 1.00 28.55 ? 647 SER A C 1 ATOM 4883 O O . SER A 1 654 ? 17.810 72.395 69.749 1.00 28.28 ? 647 SER A O 1 ATOM 4884 C CB . SER A 1 654 ? 19.074 72.447 66.715 1.00 26.52 ? 647 SER A CB 1 ATOM 4885 O OG A SER A 1 654 ? 18.951 71.693 65.531 0.50 26.86 ? 647 SER A OG 1 ATOM 4886 O OG B SER A 1 654 ? 19.772 71.387 67.325 0.50 29.83 ? 647 SER A OG 1 ATOM 4887 N N . GLU A 1 655 ? 18.045 74.486 68.888 1.00 29.08 ? 648 GLU A N 1 ATOM 4888 C CA . GLU A 1 655 ? 18.143 75.120 70.218 1.00 32.17 ? 648 GLU A CA 1 ATOM 4889 C C . GLU A 1 655 ? 16.841 74.949 71.004 1.00 31.65 ? 648 GLU A C 1 ATOM 4890 O O . GLU A 1 655 ? 16.878 74.621 72.211 1.00 31.33 ? 648 GLU A O 1 ATOM 4891 C CB . GLU A 1 655 ? 18.439 76.620 70.112 1.00 33.59 ? 648 GLU A CB 1 ATOM 4892 C CG . GLU A 1 655 ? 19.797 76.964 69.522 1.00 40.45 ? 648 GLU A CG 1 ATOM 4893 C CD . GLU A 1 655 ? 19.993 78.484 69.307 1.00 47.60 ? 648 GLU A CD 1 ATOM 4894 O OE1 . GLU A 1 655 ? 19.473 79.306 70.101 1.00 49.16 ? 648 GLU A OE1 1 ATOM 4895 O OE2 . GLU A 1 655 ? 20.674 78.852 68.322 1.00 52.38 ? 648 GLU A OE2 1 ATOM 4896 N N . ARG A 1 656 ? 15.693 75.168 70.332 1.00 30.26 ? 649 ARG A N 1 ATOM 4897 C CA . ARG A 1 656 ? 14.403 74.955 71.002 1.00 29.52 ? 649 ARG A CA 1 ATOM 4898 C C . ARG A 1 656 ? 14.197 73.500 71.398 1.00 29.83 ? 649 ARG A C 1 ATOM 4899 O O . ARG A 1 656 ? 13.652 73.224 72.475 1.00 29.47 ? 649 ARG A O 1 ATOM 4900 C CB . ARG A 1 656 ? 13.219 75.481 70.184 1.00 29.55 ? 649 ARG A CB 1 ATOM 4901 C CG . ARG A 1 656 ? 13.239 76.977 69.980 1.00 28.32 ? 649 ARG A CG 1 ATOM 4902 C CD . ARG A 1 656 ? 11.892 77.464 69.485 1.00 28.06 ? 649 ARG A CD 1 ATOM 4903 N NE . ARG A 1 656 ? 11.339 76.709 68.344 1.00 27.81 ? 649 ARG A NE 1 ATOM 4904 C CZ . ARG A 1 656 ? 11.656 76.914 67.062 1.00 28.85 ? 649 ARG A CZ 1 ATOM 4905 N NH1 . ARG A 1 656 ? 12.581 77.820 66.742 1.00 28.85 ? 649 ARG A NH1 1 ATOM 4906 N NH2 . ARG A 1 656 ? 11.068 76.199 66.099 1.00 25.69 ? 649 ARG A NH2 1 ATOM 4907 N N . LEU A 1 657 ? 14.678 72.575 70.570 1.00 29.97 ? 650 LEU A N 1 ATOM 4908 C CA . LEU A 1 657 ? 14.539 71.155 70.841 1.00 32.68 ? 650 LEU A CA 1 ATOM 4909 C C . LEU A 1 657 ? 15.344 70.764 72.093 1.00 35.97 ? 650 LEU A C 1 ATOM 4910 O O . LEU A 1 657 ? 14.940 69.848 72.809 1.00 35.40 ? 650 LEU A O 1 ATOM 4911 C CB . LEU A 1 657 ? 15.007 70.334 69.633 1.00 32.31 ? 650 LEU A CB 1 ATOM 4912 C CG . LEU A 1 657 ? 14.564 68.893 69.413 1.00 31.46 ? 650 LEU A CG 1 ATOM 4913 C CD1 . LEU A 1 657 ? 13.064 68.828 69.149 1.00 28.05 ? 650 LEU A CD1 1 ATOM 4914 C CD2 . LEU A 1 657 ? 15.390 68.212 68.221 1.00 28.70 ? 650 LEU A CD2 1 ATOM 4915 N N . GLN A 1 658 ? 16.460 71.464 72.339 1.00 39.59 ? 651 GLN A N 1 ATOM 4916 C CA . GLN A 1 658 ? 17.308 71.251 73.530 1.00 44.23 ? 651 GLN A CA 1 ATOM 4917 C C . GLN A 1 658 ? 16.627 71.741 74.810 1.00 45.73 ? 651 GLN A C 1 ATOM 4918 O O . GLN A 1 658 ? 16.737 71.087 75.833 1.00 46.82 ? 651 GLN A O 1 ATOM 4919 C CB . GLN A 1 658 ? 18.663 71.982 73.404 1.00 45.05 ? 651 GLN A CB 1 ATOM 4920 C CG . GLN A 1 658 ? 19.533 71.559 72.215 1.00 47.16 ? 651 GLN A CG 1 ATOM 4921 C CD . GLN A 1 658 ? 20.270 70.273 72.442 0.55 49.03 ? 651 GLN A CD 1 ATOM 4922 O OE1 . GLN A 1 658 ? 20.857 70.063 73.501 0.55 50.87 ? 651 GLN A OE1 1 ATOM 4923 N NE2 . GLN A 1 658 ? 20.260 69.405 71.444 0.55 49.58 ? 651 GLN A NE2 1 ATOM 4924 N N . ASP A 1 659 ? 15.903 72.863 74.691 1.00 47.34 ? 652 ASP A N 1 ATOM 4925 C CA . ASP A 1 659 ? 15.409 73.760 75.759 1.00 48.69 ? 652 ASP A CA 1 ATOM 4926 C C . ASP A 1 659 ? 13.961 73.664 76.340 1.00 48.58 ? 652 ASP A C 1 ATOM 4927 O O . ASP A 1 659 ? 13.603 74.563 77.079 1.00 49.03 ? 652 ASP A O 1 ATOM 4928 C CB . ASP A 1 659 ? 15.486 75.212 75.230 1.00 49.25 ? 652 ASP A CB 1 ATOM 4929 C CG . ASP A 1 659 ? 16.883 75.828 75.321 1.00 51.99 ? 652 ASP A CG 1 ATOM 4930 O OD1 . ASP A 1 659 ? 16.996 77.057 75.073 1.00 55.37 ? 652 ASP A OD1 1 ATOM 4931 O OD2 . ASP A 1 659 ? 17.858 75.109 75.639 1.00 55.02 ? 652 ASP A OD2 1 ATOM 4932 N N . PHE A 1 660 ? 13.134 72.654 76.008 1.00 48.03 ? 653 PHE A N 1 ATOM 4933 C CA . PHE A 1 660 ? 11.748 72.495 76.546 1.00 45.92 ? 653 PHE A CA 1 ATOM 4934 C C . PHE A 1 660 ? 11.657 71.238 77.515 1.00 46.83 ? 653 PHE A C 1 ATOM 4935 O O . PHE A 1 660 ? 10.638 70.974 78.267 1.00 45.87 ? 653 PHE A O 1 ATOM 4936 C CB . PHE A 1 660 ? 10.775 72.378 75.329 1.00 45.67 ? 653 PHE A CB 1 ATOM 4937 C CG . PHE A 1 660 ? 10.762 71.009 74.693 1.00 39.60 ? 653 PHE A CG 1 ATOM 4938 C CD1 . PHE A 1 660 ? 9.799 70.083 75.056 1.00 36.30 ? 653 PHE A CD1 1 ATOM 4939 C CD2 . PHE A 1 660 ? 11.759 70.620 73.806 1.00 36.82 ? 653 PHE A CD2 1 ATOM 4940 C CE1 . PHE A 1 660 ? 9.785 68.818 74.545 1.00 38.39 ? 653 PHE A CE1 1 ATOM 4941 C CE2 . PHE A 1 660 ? 11.782 69.327 73.268 1.00 38.87 ? 653 PHE A CE2 1 ATOM 4942 C CZ . PHE A 1 660 ? 10.782 68.418 73.617 1.00 39.51 ? 653 PHE A CZ 1 ATOM 4943 N N A SER A 1 663 ? 8.985 68.762 80.547 0.50 23.40 ? 656 SER A N 1 ATOM 4944 N N B SER A 1 663 ? 8.358 66.257 79.418 0.50 22.31 ? 656 SER A N 1 ATOM 4945 C CA A SER A 1 663 ? 7.766 68.156 81.032 0.50 23.16 ? 656 SER A CA 1 ATOM 4946 C CA B SER A 1 663 ? 7.142 65.828 80.197 0.50 22.80 ? 656 SER A CA 1 ATOM 4947 C C A SER A 1 663 ? 6.477 68.385 80.130 0.50 23.70 ? 656 SER A C 1 ATOM 4948 C C B SER A 1 663 ? 5.757 66.430 79.859 0.50 23.79 ? 656 SER A C 1 ATOM 4949 O O A SER A 1 663 ? 5.402 67.900 80.473 0.50 23.09 ? 656 SER A O 1 ATOM 4950 O O B SER A 1 663 ? 4.726 66.047 80.444 0.50 24.06 ? 656 SER A O 1 ATOM 4951 C CB A SER A 1 663 ? 7.510 68.733 82.390 0.50 22.30 ? 656 SER A CB 1 ATOM 4952 C CB B SER A 1 663 ? 7.354 65.991 81.719 0.50 21.85 ? 656 SER A CB 1 ATOM 4953 O OG A SER A 1 663 ? 7.030 70.012 82.154 0.50 19.97 ? 656 SER A OG 1 ATOM 4954 O OG B SER A 1 663 ? 7.733 64.750 82.189 0.50 19.60 ? 656 SER A OG 1 ATOM 4955 N N A ASN A 1 664 ? 6.564 69.103 79.004 0.50 23.48 ? 657 ASN A N 1 ATOM 4956 N N B ASN A 1 664 ? 5.722 67.406 78.977 0.50 24.14 ? 657 ASN A N 1 ATOM 4957 C CA A ASN A 1 664 ? 5.343 69.412 78.212 0.50 23.45 ? 657 ASN A CA 1 ATOM 4958 C CA B ASN A 1 664 ? 4.453 67.976 78.577 0.50 25.03 ? 657 ASN A CA 1 ATOM 4959 C C A ASN A 1 664 ? 5.141 68.547 76.944 0.50 23.54 ? 657 ASN A C 1 ATOM 4960 C C B ASN A 1 664 ? 4.037 67.214 77.304 0.50 25.02 ? 657 ASN A C 1 ATOM 4961 O O A ASN A 1 664 ? 5.818 68.775 75.934 0.50 23.11 ? 657 ASN A O 1 ATOM 4962 O O B ASN A 1 664 ? 4.599 67.449 76.229 0.50 24.98 ? 657 ASN A O 1 ATOM 4963 C CB A ASN A 1 664 ? 5.358 70.872 77.802 0.50 23.84 ? 657 ASN A CB 1 ATOM 4964 C CB B ASN A 1 664 ? 4.661 69.483 78.336 0.50 24.93 ? 657 ASN A CB 1 ATOM 4965 C CG A ASN A 1 664 ? 4.037 71.327 77.209 0.50 24.57 ? 657 ASN A CG 1 ATOM 4966 C CG B ASN A 1 664 ? 3.389 70.211 77.929 0.50 26.67 ? 657 ASN A CG 1 ATOM 4967 O OD1 A ASN A 1 664 ? 3.405 70.605 76.444 0.50 25.62 ? 657 ASN A OD1 1 ATOM 4968 O OD1 B ASN A 1 664 ? 2.584 69.701 77.147 0.50 29.67 ? 657 ASN A OD1 1 ATOM 4969 N ND2 A ASN A 1 664 ? 3.623 72.527 77.553 0.50 24.11 ? 657 ASN A ND2 1 ATOM 4970 N ND2 B ASN A 1 664 ? 3.226 71.424 78.420 0.50 24.68 ? 657 ASN A ND2 1 ATOM 4971 N N A PRO A 1 665 ? 4.203 67.562 76.986 0.50 23.51 ? 658 PRO A N 1 ATOM 4972 N N B PRO A 1 665 ? 3.070 66.276 77.414 0.50 25.14 ? 658 PRO A N 1 ATOM 4973 C CA A PRO A 1 665 ? 4.129 66.577 75.895 0.50 23.13 ? 658 PRO A CA 1 ATOM 4974 C CA B PRO A 1 665 ? 2.850 65.410 76.241 0.50 24.73 ? 658 PRO A CA 1 ATOM 4975 C C A PRO A 1 665 ? 3.558 67.140 74.597 0.50 23.02 ? 658 PRO A C 1 ATOM 4976 C C B PRO A 1 665 ? 2.437 66.139 74.948 0.50 24.90 ? 658 PRO A C 1 ATOM 4977 O O A PRO A 1 665 ? 3.759 66.539 73.540 0.50 23.31 ? 658 PRO A O 1 ATOM 4978 O O B PRO A 1 665 ? 2.907 65.775 73.875 0.50 24.54 ? 658 PRO A O 1 ATOM 4979 C CB A PRO A 1 665 ? 3.170 65.506 76.453 0.50 22.66 ? 658 PRO A CB 1 ATOM 4980 C CB B PRO A 1 665 ? 1.737 64.471 76.695 0.50 25.50 ? 658 PRO A CB 1 ATOM 4981 C CG A PRO A 1 665 ? 2.211 66.305 77.300 0.50 23.21 ? 658 PRO A CG 1 ATOM 4982 C CG B PRO A 1 665 ? 1.689 64.601 78.194 0.50 24.71 ? 658 PRO A CG 1 ATOM 4983 C CD A PRO A 1 665 ? 3.111 67.363 77.970 0.50 23.53 ? 658 PRO A CD 1 ATOM 4984 C CD B PRO A 1 665 ? 2.084 66.018 78.477 0.50 24.69 ? 658 PRO A CD 1 ATOM 4985 N N A ILE A 1 666 ? 2.821 68.250 74.663 0.50 22.96 ? 659 ILE A N 1 ATOM 4986 N N B ILE A 1 666 ? 1.577 67.151 75.021 0.50 24.66 ? 659 ILE A N 1 ATOM 4987 C CA A ILE A 1 666 ? 2.288 68.853 73.415 0.50 23.11 ? 659 ILE A CA 1 ATOM 4988 C CA B ILE A 1 666 ? 1.231 67.849 73.777 0.50 25.23 ? 659 ILE A CA 1 ATOM 4989 C C A ILE A 1 666 ? 3.402 69.541 72.624 0.50 22.75 ? 659 ILE A C 1 ATOM 4990 C C B ILE A 1 666 ? 2.405 68.664 73.239 0.50 24.57 ? 659 ILE A C 1 ATOM 4991 O O A ILE A 1 666 ? 3.498 69.376 71.413 0.50 23.08 ? 659 ILE A O 1 ATOM 4992 O O B ILE A 1 666 ? 2.599 68.730 72.055 0.50 24.86 ? 659 ILE A O 1 ATOM 4993 C CB A ILE A 1 666 ? 1.102 69.853 73.658 0.50 23.50 ? 659 ILE A CB 1 ATOM 4994 C CB B ILE A 1 666 ? -0.072 68.695 73.844 0.50 26.00 ? 659 ILE A CB 1 ATOM 4995 C CG1 A ILE A 1 666 ? -0.024 69.168 74.438 0.50 25.13 ? 659 ILE A CG1 1 ATOM 4996 C CG1 B ILE A 1 666 ? -1.272 67.769 73.993 0.50 27.43 ? 659 ILE A CG1 1 ATOM 4997 C CG2 A ILE A 1 666 ? 0.532 70.307 72.344 0.50 23.56 ? 659 ILE A CG2 1 ATOM 4998 C CG2 B ILE A 1 666 ? -0.263 69.480 72.561 0.50 25.20 ? 659 ILE A CG2 1 ATOM 4999 C CD1 A ILE A 1 666 ? -0.224 67.714 73.957 0.50 27.36 ? 659 ILE A CD1 1 ATOM 5000 C CD1 B ILE A 1 666 ? -1.209 66.589 73.031 0.50 27.78 ? 659 ILE A CD1 1 ATOM 5001 N N A VAL A 1 667 ? 4.221 70.333 73.309 0.50 22.43 ? 660 VAL A N 1 ATOM 5002 N N B VAL A 1 667 ? 3.198 69.291 74.100 0.50 24.69 ? 660 VAL A N 1 ATOM 5003 C CA A VAL A 1 667 ? 5.457 70.869 72.735 0.50 22.59 ? 660 VAL A CA 1 ATOM 5004 C CA B VAL A 1 667 ? 4.309 70.086 73.575 0.50 23.46 ? 660 VAL A CA 1 ATOM 5005 C C A VAL A 1 667 ? 6.323 69.745 72.137 0.50 22.60 ? 660 VAL A C 1 ATOM 5006 C C B VAL A 1 667 ? 5.360 69.146 72.958 0.50 23.01 ? 660 VAL A C 1 ATOM 5007 O O A VAL A 1 667 ? 6.814 69.852 71.001 0.50 22.89 ? 660 VAL A O 1 ATOM 5008 O O B VAL A 1 667 ? 5.931 69.424 71.909 0.50 23.77 ? 660 VAL A O 1 ATOM 5009 C CB A VAL A 1 667 ? 6.258 71.666 73.815 0.50 22.37 ? 660 VAL A CB 1 ATOM 5010 C CB B VAL A 1 667 ? 4.932 71.011 74.649 0.50 23.76 ? 660 VAL A CB 1 ATOM 5011 C CG1 A VAL A 1 667 ? 7.583 72.146 73.278 0.50 23.31 ? 660 VAL A CG1 1 ATOM 5012 C CG1 B VAL A 1 667 ? 6.304 71.572 74.173 0.50 22.47 ? 660 VAL A CG1 1 ATOM 5013 C CG2 A VAL A 1 667 ? 5.431 72.850 74.285 0.50 22.39 ? 660 VAL A CG2 1 ATOM 5014 C CG2 B VAL A 1 667 ? 3.956 72.145 75.046 0.50 23.08 ? 660 VAL A CG2 1 ATOM 5015 N N A LEU A 1 668 ? 6.474 68.656 72.885 0.50 21.64 ? 661 LEU A N 1 ATOM 5016 N N B LEU A 1 668 ? 5.604 68.010 73.584 0.50 21.64 ? 661 LEU A N 1 ATOM 5017 C CA A LEU A 1 668 ? 7.324 67.556 72.468 0.50 21.15 ? 661 LEU A CA 1 ATOM 5018 C CA B LEU A 1 668 ? 6.523 67.062 72.981 0.50 21.06 ? 661 LEU A CA 1 ATOM 5019 C C A LEU A 1 668 ? 6.776 66.933 71.190 0.50 21.09 ? 661 LEU A C 1 ATOM 5020 C C B LEU A 1 668 ? 5.964 66.559 71.639 0.50 20.69 ? 661 LEU A C 1 ATOM 5021 O O A LEU A 1 668 ? 7.478 66.822 70.173 0.50 21.31 ? 661 LEU A O 1 ATOM 5022 O O B LEU A 1 668 ? 6.710 66.229 70.726 0.50 20.35 ? 661 LEU A O 1 ATOM 5023 C CB A LEU A 1 668 ? 7.418 66.495 73.587 0.50 20.43 ? 661 LEU A CB 1 ATOM 5024 C CB B LEU A 1 668 ? 6.853 65.906 73.942 0.50 20.36 ? 661 LEU A CB 1 ATOM 5025 C CG A LEU A 1 668 ? 8.063 65.138 73.280 0.50 19.68 ? 661 LEU A CG 1 ATOM 5026 C CG B LEU A 1 668 ? 7.485 64.632 73.352 0.50 20.38 ? 661 LEU A CG 1 ATOM 5027 C CD1 A LEU A 1 668 ? 9.524 65.295 72.927 0.50 18.31 ? 661 LEU A CD1 1 ATOM 5028 C CD1 B LEU A 1 668 ? 8.914 64.841 72.873 0.50 19.97 ? 661 LEU A CD1 1 ATOM 5029 C CD2 A LEU A 1 668 ? 7.910 64.186 74.487 0.50 17.96 ? 661 LEU A CD2 1 ATOM 5030 C CD2 B LEU A 1 668 ? 7.410 63.503 74.374 0.50 16.94 ? 661 LEU A CD2 1 ATOM 5031 N N A ARG A 1 669 ? 5.512 66.532 71.259 0.50 20.68 ? 662 ARG A N 1 ATOM 5032 N N B ARG A 1 669 ? 4.648 66.496 71.509 0.50 20.63 ? 662 ARG A N 1 ATOM 5033 C CA A ARG A 1 669 ? 4.819 65.922 70.134 0.50 20.49 ? 662 ARG A CA 1 ATOM 5034 C CA B ARG A 1 669 ? 4.085 65.967 70.262 0.50 20.61 ? 662 ARG A CA 1 ATOM 5035 C C A ARG A 1 669 ? 4.722 66.947 69.013 0.50 20.54 ? 662 ARG A C 1 ATOM 5036 C C B ARG A 1 669 ? 4.340 66.901 69.069 0.50 20.68 ? 662 ARG A C 1 ATOM 5037 O O A ARG A 1 669 ? 4.980 66.594 67.869 0.50 19.11 ? 662 ARG A O 1 ATOM 5038 O O B ARG A 1 669 ? 4.521 66.439 67.952 0.50 19.43 ? 662 ARG A O 1 ATOM 5039 C CB A ARG A 1 669 ? 3.429 65.435 70.550 0.50 20.64 ? 662 ARG A CB 1 ATOM 5040 C CB B ARG A 1 669 ? 2.594 65.661 70.421 0.50 20.51 ? 662 ARG A CB 1 ATOM 5041 C CG A ARG A 1 669 ? 2.531 65.039 69.399 0.50 19.81 ? 662 ARG A CG 1 ATOM 5042 C CG B ARG A 1 669 ? 1.934 65.175 69.166 0.50 19.64 ? 662 ARG A CG 1 ATOM 5043 C CD A ARG A 1 669 ? 3.001 63.737 68.722 0.50 20.09 ? 662 ARG A CD 1 ATOM 5044 C CD B ARG A 1 669 ? 2.010 63.642 68.997 0.50 21.38 ? 662 ARG A CD 1 ATOM 5045 N NE A ARG A 1 669 ? 1.894 63.242 67.924 0.50 22.47 ? 662 ARG A NE 1 ATOM 5046 N NE B ARG A 1 669 ? 0.863 63.257 68.176 0.50 22.25 ? 662 ARG A NE 1 ATOM 5047 C CZ A ARG A 1 669 ? 1.362 62.031 68.015 0.50 23.37 ? 662 ARG A CZ 1 ATOM 5048 C CZ B ARG A 1 669 ? 0.489 62.026 67.872 0.50 22.16 ? 662 ARG A CZ 1 ATOM 5049 N NH1 A ARG A 1 669 ? 1.879 61.128 68.825 0.50 21.74 ? 662 ARG A NH1 1 ATOM 5050 N NH1 B ARG A 1 669 ? 1.194 60.974 68.305 0.50 20.45 ? 662 ARG A NH1 1 ATOM 5051 N NH2 A ARG A 1 669 ? 0.324 61.724 67.245 0.50 25.51 ? 662 ARG A NH2 1 ATOM 5052 N NH2 B ARG A 1 669 ? -0.590 61.873 67.095 0.50 19.98 ? 662 ARG A NH2 1 ATOM 5053 N N . MET A 1 670 ? 4.380 68.211 69.336 1.00 21.35 ? 663 MET A N 1 ATOM 5054 C CA . MET A 1 670 ? 4.526 69.275 68.296 1.00 21.70 ? 663 MET A CA 1 ATOM 5055 C C . MET A 1 670 ? 5.927 69.239 67.675 1.00 22.35 ? 663 MET A C 1 ATOM 5056 O O . MET A 1 670 ? 6.054 69.274 66.438 1.00 22.19 ? 663 MET A O 1 ATOM 5057 C CB A MET A 1 670 ? 4.345 70.701 68.855 0.50 21.40 ? 663 MET A CB 1 ATOM 5058 C CB B MET A 1 670 ? 4.069 70.645 68.840 0.50 22.02 ? 663 MET A CB 1 ATOM 5059 C CG A MET A 1 670 ? 4.921 71.865 67.941 0.50 20.19 ? 663 MET A CG 1 ATOM 5060 C CG B MET A 1 670 ? 2.611 70.552 69.398 0.50 22.88 ? 663 MET A CG 1 ATOM 5061 S SD A MET A 1 670 ? 4.706 73.515 68.692 0.50 21.12 ? 663 MET A SD 1 ATOM 5062 S SD B MET A 1 670 ? 1.582 71.982 69.873 0.50 23.34 ? 663 MET A SD 1 ATOM 5063 C CE A MET A 1 670 ? 3.076 73.247 69.298 0.50 22.61 ? 663 MET A CE 1 ATOM 5064 C CE B MET A 1 670 ? 2.399 72.493 71.450 0.50 16.58 ? 663 MET A CE 1 ATOM 5065 N N . MET A 1 671 ? 6.979 69.172 68.526 1.00 22.77 ? 664 MET A N 1 ATOM 5066 C CA . MET A 1 671 ? 8.356 69.113 67.994 1.00 22.57 ? 664 MET A CA 1 ATOM 5067 C C . MET A 1 671 ? 8.605 67.798 67.255 1.00 22.05 ? 664 MET A C 1 ATOM 5068 O O . MET A 1 671 ? 9.260 67.800 66.225 1.00 22.19 ? 664 MET A O 1 ATOM 5069 C CB A MET A 1 671 ? 9.357 69.147 69.160 0.50 23.22 ? 664 MET A CB 1 ATOM 5070 C CB B MET A 1 671 ? 9.452 69.505 69.021 0.50 22.53 ? 664 MET A CB 1 ATOM 5071 C CG A MET A 1 671 ? 9.067 70.210 70.182 0.50 24.39 ? 664 MET A CG 1 ATOM 5072 C CG B MET A 1 671 ? 9.276 70.935 69.631 0.50 20.98 ? 664 MET A CG 1 ATOM 5073 S SD A MET A 1 671 ? 9.219 71.774 69.356 0.50 27.54 ? 664 MET A SD 1 ATOM 5074 S SD B MET A 1 671 ? 10.713 71.778 70.419 0.50 21.49 ? 664 MET A SD 1 ATOM 5075 C CE A MET A 1 671 ? 11.002 71.969 69.219 0.50 26.02 ? 664 MET A CE 1 ATOM 5076 C CE B MET A 1 671 ? 11.557 72.344 68.948 0.50 20.46 ? 664 MET A CE 1 ATOM 5077 N N . ASN A 1 672 ? 8.147 66.667 67.795 1.00 21.75 ? 665 ASN A N 1 ATOM 5078 C CA . ASN A 1 672 ? 8.325 65.400 67.057 1.00 21.36 ? 665 ASN A CA 1 ATOM 5079 C C . ASN A 1 672 ? 7.589 65.457 65.722 1.00 20.36 ? 665 ASN A C 1 ATOM 5080 O O . ASN A 1 672 ? 8.028 64.880 64.765 1.00 21.04 ? 665 ASN A O 1 ATOM 5081 C CB . ASN A 1 672 ? 7.842 64.168 67.868 1.00 21.27 ? 665 ASN A CB 1 ATOM 5082 C CG . ASN A 1 672 ? 8.851 63.728 68.897 1.00 23.39 ? 665 ASN A CG 1 ATOM 5083 O OD1 . ASN A 1 672 ? 10.057 63.892 68.684 1.00 24.07 ? 665 ASN A OD1 1 ATOM 5084 N ND2 . ASN A 1 672 ? 8.376 63.159 70.020 1.00 20.74 ? 665 ASN A ND2 1 ATOM 5085 N N . ASP A 1 673 ? 6.440 66.113 65.655 1.00 20.39 ? 666 ASP A N 1 ATOM 5086 C CA . ASP A 1 673 ? 5.726 66.187 64.377 1.00 18.86 ? 666 ASP A CA 1 ATOM 5087 C C . ASP A 1 673 ? 6.514 67.077 63.400 1.00 18.64 ? 666 ASP A C 1 ATOM 5088 O O . ASP A 1 673 ? 6.566 66.765 62.233 1.00 18.30 ? 666 ASP A O 1 ATOM 5089 C CB . ASP A 1 673 ? 4.298 66.766 64.548 1.00 18.89 ? 666 ASP A CB 1 ATOM 5090 C CG . ASP A 1 673 ? 3.305 65.735 65.086 1.00 20.55 ? 666 ASP A CG 1 ATOM 5091 O OD1 . ASP A 1 673 ? 3.680 64.549 65.246 1.00 20.74 ? 666 ASP A OD1 1 ATOM 5092 O OD2 . ASP A 1 673 ? 2.148 66.119 65.363 1.00 22.41 ? 666 ASP A OD2 1 ATOM 5093 N N . GLN A 1 674 ? 7.147 68.157 63.879 1.00 17.77 ? 667 GLN A N 1 ATOM 5094 C CA . GLN A 1 674 ? 8.019 68.959 63.016 1.00 18.30 ? 667 GLN A CA 1 ATOM 5095 C C . GLN A 1 674 ? 9.186 68.104 62.515 1.00 18.72 ? 667 GLN A C 1 ATOM 5096 O O . GLN A 1 674 ? 9.512 68.112 61.317 1.00 19.32 ? 667 GLN A O 1 ATOM 5097 C CB . GLN A 1 674 ? 8.505 70.240 63.727 1.00 16.99 ? 667 GLN A CB 1 ATOM 5098 C CG . GLN A 1 674 ? 7.373 71.282 63.789 1.00 17.88 ? 667 GLN A CG 1 ATOM 5099 C CD . GLN A 1 674 ? 7.821 72.510 64.565 1.00 19.05 ? 667 GLN A CD 1 ATOM 5100 O OE1 . GLN A 1 674 ? 7.895 72.465 65.794 1.00 19.69 ? 667 GLN A OE1 1 ATOM 5101 N NE2 . GLN A 1 674 ? 8.141 73.613 63.853 1.00 16.23 ? 667 GLN A NE2 1 ATOM 5102 N N . LEU A 1 675 ? 9.767 67.297 63.405 1.00 19.26 ? 668 LEU A N 1 ATOM 5103 C CA . LEU A 1 675 ? 10.811 66.355 62.928 1.00 19.65 ? 668 LEU A CA 1 ATOM 5104 C C . LEU A 1 675 ? 10.292 65.322 61.933 1.00 19.86 ? 668 LEU A C 1 ATOM 5105 O O . LEU A 1 675 ? 10.936 65.033 60.890 1.00 20.25 ? 668 LEU A O 1 ATOM 5106 C CB . LEU A 1 675 ? 11.432 65.627 64.128 1.00 20.69 ? 668 LEU A CB 1 ATOM 5107 C CG . LEU A 1 675 ? 12.275 66.584 64.989 1.00 21.66 ? 668 LEU A CG 1 ATOM 5108 C CD1 . LEU A 1 675 ? 12.708 65.879 66.234 1.00 23.67 ? 668 LEU A CD1 1 ATOM 5109 C CD2 . LEU A 1 675 ? 13.470 67.071 64.187 1.00 23.78 ? 668 LEU A CD2 1 ATOM 5110 N N . MET A 1 676 ? 9.136 64.730 62.244 1.00 19.06 ? 669 MET A N 1 ATOM 5111 C CA . MET A 1 676 ? 8.590 63.703 61.339 1.00 19.64 ? 669 MET A CA 1 ATOM 5112 C C . MET A 1 676 ? 8.214 64.280 59.934 1.00 19.24 ? 669 MET A C 1 ATOM 5113 O O . MET A 1 676 ? 8.483 63.655 58.867 1.00 20.32 ? 669 MET A O 1 ATOM 5114 C CB . MET A 1 676 ? 7.359 63.087 61.984 1.00 19.50 ? 669 MET A CB 1 ATOM 5115 C CG . MET A 1 676 ? 6.719 61.996 61.091 1.00 22.85 ? 669 MET A CG 1 ATOM 5116 S SD . MET A 1 676 ? 5.300 61.238 61.871 1.00 23.95 ? 669 MET A SD 1 ATOM 5117 C CE . MET A 1 676 ? 4.119 62.582 61.767 1.00 20.98 ? 669 MET A CE 1 ATOM 5118 N N . PHE A 1 677 ? 7.585 65.453 59.929 1.00 17.99 ? 670 PHE A N 1 ATOM 5119 C CA . PHE A 1 677 ? 7.128 66.068 58.654 1.00 18.03 ? 670 PHE A CA 1 ATOM 5120 C C . PHE A 1 677 ? 8.195 66.786 57.857 1.00 17.45 ? 670 PHE A C 1 ATOM 5121 O O . PHE A 1 677 ? 7.902 67.320 56.771 1.00 18.63 ? 670 PHE A O 1 ATOM 5122 C CB . PHE A 1 677 ? 5.897 66.981 58.889 1.00 16.18 ? 670 PHE A CB 1 ATOM 5123 C CG . PHE A 1 677 ? 4.637 66.204 59.177 1.00 18.25 ? 670 PHE A CG 1 ATOM 5124 C CD1 . PHE A 1 677 ? 4.175 65.238 58.248 1.00 17.31 ? 670 PHE A CD1 1 ATOM 5125 C CD2 . PHE A 1 677 ? 3.907 66.415 60.369 1.00 17.99 ? 670 PHE A CD2 1 ATOM 5126 C CE1 . PHE A 1 677 ? 2.989 64.510 58.492 1.00 17.19 ? 670 PHE A CE1 1 ATOM 5127 C CE2 . PHE A 1 677 ? 2.734 65.706 60.622 1.00 17.64 ? 670 PHE A CE2 1 ATOM 5128 C CZ . PHE A 1 677 ? 2.272 64.743 59.697 1.00 15.04 ? 670 PHE A CZ 1 ATOM 5129 N N . LEU A 1 678 ? 9.424 66.836 58.388 1.00 17.71 ? 671 LEU A N 1 ATOM 5130 C CA . LEU A 1 678 ? 10.514 67.553 57.698 1.00 17.19 ? 671 LEU A CA 1 ATOM 5131 C C . LEU A 1 678 ? 10.886 66.813 56.400 1.00 16.66 ? 671 LEU A C 1 ATOM 5132 O O . LEU A 1 678 ? 10.939 67.397 55.305 1.00 15.46 ? 671 LEU A O 1 ATOM 5133 C CB . LEU A 1 678 ? 11.751 67.670 58.619 1.00 17.25 ? 671 LEU A CB 1 ATOM 5134 C CG . LEU A 1 678 ? 12.926 68.426 57.984 1.00 19.00 ? 671 LEU A CG 1 ATOM 5135 C CD1 . LEU A 1 678 ? 12.494 69.826 57.440 1.00 21.14 ? 671 LEU A CD1 1 ATOM 5136 C CD2 . LEU A 1 678 ? 14.099 68.558 59.008 1.00 20.74 ? 671 LEU A CD2 1 ATOM 5137 N N . GLU A 1 679 ? 11.147 65.512 56.492 1.00 16.35 ? 672 GLU A N 1 ATOM 5138 C CA . GLU A 1 679 ? 11.333 64.763 55.232 1.00 16.35 ? 672 GLU A CA 1 ATOM 5139 C C . GLU A 1 679 ? 10.138 64.955 54.269 1.00 16.14 ? 672 GLU A C 1 ATOM 5140 O O . GLU A 1 679 ? 10.288 65.135 52.997 1.00 16.47 ? 672 GLU A O 1 ATOM 5141 C CB . GLU A 1 679 ? 11.541 63.267 55.505 1.00 15.61 ? 672 GLU A CB 1 ATOM 5142 C CG . GLU A 1 679 ? 12.125 62.583 54.269 1.00 16.14 ? 672 GLU A CG 1 ATOM 5143 C CD . GLU A 1 679 ? 13.650 62.841 54.149 1.00 18.85 ? 672 GLU A CD 1 ATOM 5144 O OE1 . GLU A 1 679 ? 14.370 62.410 55.083 1.00 18.14 ? 672 GLU A OE1 1 ATOM 5145 O OE2 . GLU A 1 679 ? 14.105 63.496 53.148 1.00 18.03 ? 672 GLU A OE2 1 ATOM 5146 N N . ARG A 1 680 ? 8.943 64.933 54.862 1.00 15.91 ? 673 ARG A N 1 ATOM 5147 C CA . ARG A 1 680 ? 7.700 65.080 54.089 1.00 15.56 ? 673 ARG A CA 1 ATOM 5148 C C . ARG A 1 680 ? 7.631 66.410 53.311 1.00 15.58 ? 673 ARG A C 1 ATOM 5149 O O . ARG A 1 680 ? 7.045 66.503 52.219 1.00 14.73 ? 673 ARG A O 1 ATOM 5150 C CB . ARG A 1 680 ? 6.450 64.958 55.032 1.00 15.55 ? 673 ARG A CB 1 ATOM 5151 C CG . ARG A 1 680 ? 5.229 64.305 54.255 1.00 14.03 ? 673 ARG A CG 1 ATOM 5152 C CD . ARG A 1 680 ? 5.269 62.730 54.350 1.00 13.18 ? 673 ARG A CD 1 ATOM 5153 N NE . ARG A 1 680 ? 4.908 62.267 55.726 1.00 13.45 ? 673 ARG A NE 1 ATOM 5154 C CZ . ARG A 1 680 ? 5.745 61.757 56.636 1.00 16.07 ? 673 ARG A CZ 1 ATOM 5155 N NH1 . ARG A 1 680 ? 7.072 61.621 56.404 1.00 14.43 ? 673 ARG A NH1 1 ATOM 5156 N NH2 . ARG A 1 680 ? 5.244 61.358 57.806 1.00 16.24 ? 673 ARG A NH2 1 ATOM 5157 N N . ALA A 1 681 ? 8.217 67.450 53.897 1.00 15.35 ? 674 ALA A N 1 ATOM 5158 C CA . ALA A 1 681 ? 8.165 68.755 53.290 1.00 15.21 ? 674 ALA A CA 1 ATOM 5159 C C . ALA A 1 681 ? 8.933 68.829 51.967 1.00 15.78 ? 674 ALA A C 1 ATOM 5160 O O . ALA A 1 681 ? 8.669 69.737 51.164 1.00 16.52 ? 674 ALA A O 1 ATOM 5161 C CB . ALA A 1 681 ? 8.667 69.794 54.273 1.00 14.02 ? 674 ALA A CB 1 ATOM 5162 N N . PHE A 1 682 ? 9.855 67.882 51.703 1.00 16.19 ? 675 PHE A N 1 ATOM 5163 C CA . PHE A 1 682 ? 10.573 67.912 50.397 1.00 17.22 ? 675 PHE A CA 1 ATOM 5164 C C . PHE A 1 682 ? 9.791 67.323 49.226 1.00 17.33 ? 675 PHE A C 1 ATOM 5165 O O . PHE A 1 682 ? 10.255 67.353 48.062 1.00 18.91 ? 675 PHE A O 1 ATOM 5166 C CB . PHE A 1 682 ? 11.955 67.255 50.503 1.00 17.92 ? 675 PHE A CB 1 ATOM 5167 C CG . PHE A 1 682 ? 12.889 68.001 51.412 1.00 16.91 ? 675 PHE A CG 1 ATOM 5168 C CD1 . PHE A 1 682 ? 13.309 69.294 51.099 1.00 15.16 ? 675 PHE A CD1 1 ATOM 5169 C CD2 . PHE A 1 682 ? 13.345 67.402 52.579 1.00 18.18 ? 675 PHE A CD2 1 ATOM 5170 C CE1 . PHE A 1 682 ? 14.197 70.013 51.964 1.00 16.40 ? 675 PHE A CE1 1 ATOM 5171 C CE2 . PHE A 1 682 ? 14.216 68.098 53.457 1.00 19.68 ? 675 PHE A CE2 1 ATOM 5172 C CZ . PHE A 1 682 ? 14.652 69.414 53.133 1.00 16.90 ? 675 PHE A CZ 1 ATOM 5173 N N . ILE A 1 683 ? 8.623 66.770 49.523 1.00 16.34 ? 676 ILE A N 1 ATOM 5174 C CA . ILE A 1 683 ? 7.707 66.218 48.494 1.00 15.75 ? 676 ILE A CA 1 ATOM 5175 C C . ILE A 1 683 ? 6.993 67.336 47.738 1.00 17.26 ? 676 ILE A C 1 ATOM 5176 O O . ILE A 1 683 ? 6.436 68.280 48.362 1.00 18.98 ? 676 ILE A O 1 ATOM 5177 C CB . ILE A 1 683 ? 6.669 65.289 49.156 1.00 14.64 ? 676 ILE A CB 1 ATOM 5178 C CG1 . ILE A 1 683 ? 7.407 64.063 49.806 1.00 14.43 ? 676 ILE A CG1 1 ATOM 5179 C CG2 . ILE A 1 683 ? 5.483 64.945 48.179 1.00 14.33 ? 676 ILE A CG2 1 ATOM 5180 C CD1 . ILE A 1 683 ? 8.291 63.228 48.765 1.00 12.08 ? 676 ILE A CD1 1 ATOM 5181 N N . ASP A 1 684 ? 7.030 67.242 46.408 1.00 15.82 ? 677 ASP A N 1 ATOM 5182 C CA . ASP A 1 684 ? 6.249 68.101 45.549 1.00 16.75 ? 677 ASP A CA 1 ATOM 5183 C C . ASP A 1 684 ? 5.096 67.284 45.010 1.00 16.52 ? 677 ASP A C 1 ATOM 5184 O O . ASP A 1 684 ? 5.322 66.275 44.313 1.00 17.58 ? 677 ASP A O 1 ATOM 5185 C CB . ASP A 1 684 ? 7.105 68.589 44.368 1.00 15.10 ? 677 ASP A CB 1 ATOM 5186 C CG . ASP A 1 684 ? 6.396 69.632 43.553 1.00 16.33 ? 677 ASP A CG 1 ATOM 5187 O OD1 . ASP A 1 684 ? 5.118 69.666 43.521 1.00 16.97 ? 677 ASP A OD1 1 ATOM 5188 O OD2 . ASP A 1 684 ? 7.116 70.429 42.934 1.00 18.57 ? 677 ASP A OD2 1 ATOM 5189 N N . PRO A 1 685 ? 3.864 67.682 45.301 1.00 17.92 ? 678 PRO A N 1 ATOM 5190 C CA . PRO A 1 685 ? 2.755 66.815 44.882 1.00 19.36 ? 678 PRO A CA 1 ATOM 5191 C C . PRO A 1 685 ? 2.590 66.762 43.347 1.00 20.61 ? 678 PRO A C 1 ATOM 5192 O O . PRO A 1 685 ? 1.882 65.895 42.840 1.00 24.93 ? 678 PRO A O 1 ATOM 5193 C CB . PRO A 1 685 ? 1.514 67.510 45.503 1.00 19.55 ? 678 PRO A CB 1 ATOM 5194 C CG . PRO A 1 685 ? 1.919 68.921 45.734 1.00 17.70 ? 678 PRO A CG 1 ATOM 5195 C CD . PRO A 1 685 ? 3.397 68.850 46.082 1.00 17.40 ? 678 PRO A CD 1 ATOM 5196 N N . LEU A 1 686 ? 3.237 67.645 42.587 1.00 19.32 ? 679 LEU A N 1 ATOM 5197 C CA . LEU A 1 686 ? 3.147 67.573 41.110 1.00 17.98 ? 679 LEU A CA 1 ATOM 5198 C C . LEU A 1 686 ? 4.220 66.607 40.544 1.00 18.49 ? 679 LEU A C 1 ATOM 5199 O O . LEU A 1 686 ? 4.239 66.315 39.335 1.00 19.21 ? 679 LEU A O 1 ATOM 5200 C CB . LEU A 1 686 ? 3.376 68.992 40.550 1.00 17.41 ? 679 LEU A CB 1 ATOM 5201 C CG . LEU A 1 686 ? 2.235 69.997 40.922 1.00 17.79 ? 679 LEU A CG 1 ATOM 5202 C CD1 . LEU A 1 686 ? 2.378 71.421 40.328 1.00 14.61 ? 679 LEU A CD1 1 ATOM 5203 C CD2 . LEU A 1 686 ? 0.800 69.428 40.552 1.00 19.17 ? 679 LEU A CD2 1 ATOM 5204 N N . GLY A 1 687 ? 5.144 66.147 41.406 1.00 18.51 ? 680 GLY A N 1 ATOM 5205 C CA . GLY A 1 687 ? 6.179 65.184 40.997 1.00 18.01 ? 680 GLY A CA 1 ATOM 5206 C C . GLY A 1 687 ? 7.243 65.858 40.127 1.00 19.47 ? 680 GLY A C 1 ATOM 5207 O O . GLY A 1 687 ? 7.151 67.067 39.826 1.00 19.81 ? 680 GLY A O 1 ATOM 5208 N N . LEU A 1 688 ? 8.247 65.088 39.721 1.00 18.48 ? 681 LEU A N 1 ATOM 5209 C CA . LEU A 1 688 ? 9.242 65.568 38.769 1.00 19.16 ? 681 LEU A CA 1 ATOM 5210 C C . LEU A 1 688 ? 8.772 65.393 37.322 1.00 19.66 ? 681 LEU A C 1 ATOM 5211 O O . LEU A 1 688 ? 7.829 64.583 37.050 1.00 20.86 ? 681 LEU A O 1 ATOM 5212 C CB . LEU A 1 688 ? 10.562 64.776 39.001 1.00 19.57 ? 681 LEU A CB 1 ATOM 5213 C CG . LEU A 1 688 ? 11.302 65.109 40.319 1.00 20.01 ? 681 LEU A CG 1 ATOM 5214 C CD1 . LEU A 1 688 ? 12.356 64.044 40.630 1.00 20.43 ? 681 LEU A CD1 1 ATOM 5215 C CD2 . LEU A 1 688 ? 11.866 66.610 40.341 1.00 19.14 ? 681 LEU A CD2 1 ATOM 5216 N N . PRO A 1 689 ? 9.373 66.152 36.365 1.00 20.76 ? 682 PRO A N 1 ATOM 5217 C CA . PRO A 1 689 ? 8.867 66.096 34.974 1.00 20.98 ? 682 PRO A CA 1 ATOM 5218 C C . PRO A 1 689 ? 8.768 64.689 34.405 1.00 21.20 ? 682 PRO A C 1 ATOM 5219 O O . PRO A 1 689 ? 9.775 63.972 34.337 1.00 20.51 ? 682 PRO A O 1 ATOM 5220 C CB . PRO A 1 689 ? 9.865 67.000 34.183 1.00 21.49 ? 682 PRO A CB 1 ATOM 5221 C CG . PRO A 1 689 ? 10.275 68.027 35.246 1.00 21.96 ? 682 PRO A CG 1 ATOM 5222 C CD . PRO A 1 689 ? 10.476 67.141 36.495 1.00 20.39 ? 682 PRO A CD 1 ATOM 5223 N N . ASP A 1 690 ? 7.539 64.322 34.017 1.00 21.99 ? 683 ASP A N 1 ATOM 5224 C CA . ASP A 1 690 ? 7.174 63.017 33.426 1.00 22.18 ? 683 ASP A CA 1 ATOM 5225 C C . ASP A 1 690 ? 7.495 61.880 34.341 1.00 20.15 ? 683 ASP A C 1 ATOM 5226 O O . ASP A 1 690 ? 7.494 60.733 33.890 1.00 18.77 ? 683 ASP A O 1 ATOM 5227 C CB . ASP A 1 690 ? 7.876 62.732 32.074 1.00 24.64 ? 683 ASP A CB 1 ATOM 5228 C CG . ASP A 1 690 ? 7.563 63.769 31.040 1.00 29.35 ? 683 ASP A CG 1 ATOM 5229 O OD1 . ASP A 1 690 ? 6.377 64.069 30.812 1.00 32.49 ? 683 ASP A OD1 1 ATOM 5230 O OD2 . ASP A 1 690 ? 8.531 64.294 30.468 1.00 36.27 ? 683 ASP A OD2 1 ATOM 5231 N N . ARG A 1 691 ? 7.738 62.171 35.622 1.00 18.88 ? 684 ARG A N 1 ATOM 5232 C CA . ARG A 1 691 ? 7.920 61.066 36.608 1.00 17.49 ? 684 ARG A CA 1 ATOM 5233 C C . ARG A 1 691 ? 7.083 61.368 37.848 1.00 16.30 ? 684 ARG A C 1 ATOM 5234 O O . ARG A 1 691 ? 7.618 61.767 38.904 1.00 15.04 ? 684 ARG A O 1 ATOM 5235 C CB . ARG A 1 691 ? 9.424 60.823 36.947 1.00 17.99 ? 684 ARG A CB 1 ATOM 5236 C CG . ARG A 1 691 ? 10.297 60.426 35.679 1.00 18.02 ? 684 ARG A CG 1 ATOM 5237 C CD . ARG A 1 691 ? 11.721 59.990 36.048 1.00 17.51 ? 684 ARG A CD 1 ATOM 5238 N NE . ARG A 1 691 ? 12.482 61.120 36.653 1.00 18.78 ? 684 ARG A NE 1 ATOM 5239 C CZ . ARG A 1 691 ? 13.663 61.001 37.266 1.00 19.35 ? 684 ARG A CZ 1 ATOM 5240 N NH1 . ARG A 1 691 ? 14.228 59.776 37.373 1.00 16.34 ? 684 ARG A NH1 1 ATOM 5241 N NH2 . ARG A 1 691 ? 14.278 62.105 37.787 1.00 18.33 ? 684 ARG A NH2 1 ATOM 5242 N N . PRO A 1 692 ? 5.774 61.150 37.732 1.00 16.18 ? 685 PRO A N 1 ATOM 5243 C CA . PRO A 1 692 ? 4.890 61.652 38.784 1.00 15.84 ? 685 PRO A CA 1 ATOM 5244 C C . PRO A 1 692 ? 5.072 60.949 40.108 1.00 16.42 ? 685 PRO A C 1 ATOM 5245 O O . PRO A 1 692 ? 4.586 61.493 41.116 1.00 16.39 ? 685 PRO A O 1 ATOM 5246 C CB . PRO A 1 692 ? 3.440 61.349 38.246 1.00 17.47 ? 685 PRO A CB 1 ATOM 5247 C CG . PRO A 1 692 ? 3.604 60.232 37.144 1.00 18.56 ? 685 PRO A CG 1 ATOM 5248 C CD . PRO A 1 692 ? 5.041 60.647 36.543 1.00 16.19 ? 685 PRO A CD 1 ATOM 5249 N N . PHE A 1 693 ? 5.675 59.735 40.108 1.00 15.79 ? 686 PHE A N 1 ATOM 5250 C CA . PHE A 1 693 ? 5.923 59.010 41.389 1.00 16.18 ? 686 PHE A CA 1 ATOM 5251 C C . PHE A 1 693 ? 7.259 59.261 42.047 1.00 15.46 ? 686 PHE A C 1 ATOM 5252 O O . PHE A 1 693 ? 7.522 58.765 43.139 1.00 15.77 ? 686 PHE A O 1 ATOM 5253 C CB . PHE A 1 693 ? 5.607 57.514 41.238 1.00 15.77 ? 686 PHE A CB 1 ATOM 5254 C CG . PHE A 1 693 ? 4.186 57.297 40.728 1.00 17.44 ? 686 PHE A CG 1 ATOM 5255 C CD1 . PHE A 1 693 ? 3.079 57.709 41.507 1.00 15.21 ? 686 PHE A CD1 1 ATOM 5256 C CD2 . PHE A 1 693 ? 3.957 56.755 39.453 1.00 16.36 ? 686 PHE A CD2 1 ATOM 5257 C CE1 . PHE A 1 693 ? 1.729 57.518 41.024 1.00 14.13 ? 686 PHE A CE1 1 ATOM 5258 C CE2 . PHE A 1 693 ? 2.647 56.563 38.971 1.00 15.74 ? 686 PHE A CE2 1 ATOM 5259 C CZ . PHE A 1 693 ? 1.541 56.951 39.746 1.00 15.40 ? 686 PHE A CZ 1 ATOM 5260 N N . TYR A 1 694 ? 8.056 60.117 41.425 1.00 14.67 ? 687 TYR A N 1 ATOM 5261 C CA . TYR A 1 694 ? 9.237 60.618 42.086 1.00 14.71 ? 687 TYR A CA 1 ATOM 5262 C C . TYR A 1 694 ? 8.936 62.038 42.489 1.00 15.13 ? 687 TYR A C 1 ATOM 5263 O O . TYR A 1 694 ? 9.041 62.958 41.659 1.00 15.94 ? 687 TYR A O 1 ATOM 5264 C CB . TYR A 1 694 ? 10.450 60.578 41.125 1.00 14.88 ? 687 TYR A CB 1 ATOM 5265 C CG . TYR A 1 694 ? 10.913 59.161 40.802 1.00 15.56 ? 687 TYR A CG 1 ATOM 5266 C CD1 . TYR A 1 694 ? 10.691 58.087 41.720 1.00 15.19 ? 687 TYR A CD1 1 ATOM 5267 C CD2 . TYR A 1 694 ? 11.616 58.894 39.614 1.00 14.44 ? 687 TYR A CD2 1 ATOM 5268 C CE1 . TYR A 1 694 ? 11.137 56.756 41.425 1.00 15.25 ? 687 TYR A CE1 1 ATOM 5269 C CE2 . TYR A 1 694 ? 12.069 57.543 39.307 1.00 17.55 ? 687 TYR A CE2 1 ATOM 5270 C CZ . TYR A 1 694 ? 11.819 56.503 40.230 1.00 16.17 ? 687 TYR A CZ 1 ATOM 5271 O OH . TYR A 1 694 ? 12.287 55.216 39.966 1.00 14.15 ? 687 TYR A OH 1 ATOM 5272 N N . ARG A 1 695 ? 8.597 62.244 43.764 1.00 15.44 ? 688 ARG A N 1 ATOM 5273 C CA . ARG A 1 695 ? 8.082 63.548 44.204 1.00 14.62 ? 688 ARG A CA 1 ATOM 5274 C C . ARG A 1 695 ? 9.037 64.319 45.099 1.00 14.82 ? 688 ARG A C 1 ATOM 5275 O O . ARG A 1 695 ? 8.760 65.468 45.427 1.00 14.89 ? 688 ARG A O 1 ATOM 5276 C CB . ARG A 1 695 ? 6.768 63.326 44.953 1.00 14.68 ? 688 ARG A CB 1 ATOM 5277 C CG . ARG A 1 695 ? 5.801 62.438 44.101 1.00 14.67 ? 688 ARG A CG 1 ATOM 5278 C CD . ARG A 1 695 ? 4.325 62.637 44.481 1.00 20.33 ? 688 ARG A CD 1 ATOM 5279 N NE . ARG A 1 695 ? 4.163 62.223 45.867 1.00 22.96 ? 688 ARG A NE 1 ATOM 5280 C CZ . ARG A 1 695 ? 3.150 62.546 46.693 1.00 24.43 ? 688 ARG A CZ 1 ATOM 5281 N NH1 . ARG A 1 695 ? 3.178 62.066 47.954 1.00 19.49 ? 688 ARG A NH1 1 ATOM 5282 N NH2 . ARG A 1 695 ? 2.143 63.369 46.296 1.00 21.81 ? 688 ARG A NH2 1 ATOM 5283 N N . HIS A 1 696 ? 10.117 63.665 45.545 1.00 14.67 ? 689 HIS A N 1 ATOM 5284 C CA . HIS A 1 696 ? 11.076 64.272 46.443 1.00 13.85 ? 689 HIS A CA 1 ATOM 5285 C C . HIS A 1 696 ? 11.917 65.236 45.596 1.00 14.93 ? 689 HIS A C 1 ATOM 5286 O O . HIS A 1 696 ? 12.450 64.838 44.549 1.00 16.83 ? 689 HIS A O 1 ATOM 5287 C CB . HIS A 1 696 ? 11.978 63.182 47.071 1.00 13.64 ? 689 HIS A CB 1 ATOM 5288 C CG . HIS A 1 696 ? 12.647 63.595 48.355 1.00 14.52 ? 689 HIS A CG 1 ATOM 5289 N ND1 . HIS A 1 696 ? 13.593 64.597 48.407 1.00 14.19 ? 689 HIS A ND1 1 ATOM 5290 C CD2 . HIS A 1 696 ? 12.513 63.143 49.628 1.00 15.75 ? 689 HIS A CD2 1 ATOM 5291 C CE1 . HIS A 1 696 ? 14.027 64.742 49.653 1.00 15.29 ? 689 HIS A CE1 1 ATOM 5292 N NE2 . HIS A 1 696 ? 13.369 63.886 50.420 1.00 15.87 ? 689 HIS A NE2 1 ATOM 5293 N N . VAL A 1 697 ? 12.053 66.490 46.029 1.00 15.17 ? 690 VAL A N 1 ATOM 5294 C CA . VAL A 1 697 ? 12.732 67.516 45.192 1.00 15.41 ? 690 VAL A CA 1 ATOM 5295 C C . VAL A 1 697 ? 14.259 67.467 45.411 1.00 15.98 ? 690 VAL A C 1 ATOM 5296 O O . VAL A 1 697 ? 15.033 67.908 44.568 1.00 17.44 ? 690 VAL A O 1 ATOM 5297 C CB . VAL A 1 697 ? 12.125 68.935 45.489 1.00 15.04 ? 690 VAL A CB 1 ATOM 5298 C CG1 . VAL A 1 697 ? 12.906 70.072 44.780 1.00 13.16 ? 690 VAL A CG1 1 ATOM 5299 C CG2 . VAL A 1 697 ? 10.636 68.966 45.025 1.00 14.22 ? 690 VAL A CG2 1 ATOM 5300 N N . ILE A 1 698 ? 14.710 66.939 46.545 1.00 16.08 ? 691 ILE A N 1 ATOM 5301 C CA . ILE A 1 698 ? 16.172 66.877 46.778 1.00 15.79 ? 691 ILE A CA 1 ATOM 5302 C C . ILE A 1 698 ? 16.799 65.638 46.170 1.00 16.80 ? 691 ILE A C 1 ATOM 5303 O O . ILE A 1 698 ? 17.921 65.703 45.676 1.00 16.78 ? 691 ILE A O 1 ATOM 5304 C CB . ILE A 1 698 ? 16.526 66.905 48.324 1.00 15.64 ? 691 ILE A CB 1 ATOM 5305 C CG1 . ILE A 1 698 ? 15.731 68.037 49.023 1.00 15.17 ? 691 ILE A CG1 1 ATOM 5306 C CG2 . ILE A 1 698 ? 18.048 67.089 48.555 1.00 15.39 ? 691 ILE A CG2 1 ATOM 5307 C CD1 . ILE A 1 698 ? 15.827 69.436 48.344 1.00 14.25 ? 691 ILE A CD1 1 ATOM 5308 N N . TYR A 1 699 ? 16.079 64.503 46.202 1.00 17.06 ? 692 TYR A N 1 ATOM 5309 C CA . TYR A 1 699 ? 16.649 63.214 45.762 1.00 17.91 ? 692 TYR A CA 1 ATOM 5310 C C . TYR A 1 699 ? 15.757 62.488 44.789 1.00 18.26 ? 692 TYR A C 1 ATOM 5311 O O . TYR A 1 699 ? 14.561 62.324 45.082 1.00 20.36 ? 692 TYR A O 1 ATOM 5312 C CB . TYR A 1 699 ? 16.775 62.271 46.983 1.00 17.54 ? 692 TYR A CB 1 ATOM 5313 C CG . TYR A 1 699 ? 17.812 62.708 48.009 1.00 20.03 ? 692 TYR A CG 1 ATOM 5314 C CD1 . TYR A 1 699 ? 19.212 62.780 47.660 1.00 19.49 ? 692 TYR A CD1 1 ATOM 5315 C CD2 . TYR A 1 699 ? 17.430 63.041 49.323 1.00 16.73 ? 692 TYR A CD2 1 ATOM 5316 C CE1 . TYR A 1 699 ? 20.155 63.157 48.588 1.00 20.33 ? 692 TYR A CE1 1 ATOM 5317 C CE2 . TYR A 1 699 ? 18.394 63.433 50.281 1.00 18.47 ? 692 TYR A CE2 1 ATOM 5318 C CZ . TYR A 1 699 ? 19.748 63.465 49.927 1.00 20.30 ? 692 TYR A CZ 1 ATOM 5319 O OH . TYR A 1 699 ? 20.715 63.815 50.870 1.00 19.89 ? 692 TYR A OH 1 ATOM 5320 N N . ALA A 1 700 ? 16.286 61.972 43.671 1.00 17.43 ? 693 ALA A N 1 ATOM 5321 C CA . ALA A 1 700 ? 15.475 61.009 42.890 1.00 16.35 ? 693 ALA A CA 1 ATOM 5322 C C . ALA A 1 700 ? 16.453 59.990 42.360 1.00 16.69 ? 693 ALA A C 1 ATOM 5323 O O . ALA A 1 700 ? 17.672 60.264 42.325 1.00 17.75 ? 693 ALA A O 1 ATOM 5324 C CB . ALA A 1 700 ? 14.703 61.683 41.679 1.00 15.71 ? 693 ALA A CB 1 ATOM 5325 N N . PRO A 1 701 ? 15.943 58.837 41.916 1.00 16.13 ? 694 PRO A N 1 ATOM 5326 C CA . PRO A 1 701 ? 16.821 57.899 41.226 1.00 16.66 ? 694 PRO A CA 1 ATOM 5327 C C . PRO A 1 701 ? 17.322 58.586 39.948 1.00 17.82 ? 694 PRO A C 1 ATOM 5328 O O . PRO A 1 701 ? 16.520 59.271 39.307 1.00 19.08 ? 694 PRO A O 1 ATOM 5329 C CB . PRO A 1 701 ? 15.874 56.715 40.857 1.00 14.89 ? 694 PRO A CB 1 ATOM 5330 C CG . PRO A 1 701 ? 14.782 56.787 41.983 1.00 15.20 ? 694 PRO A CG 1 ATOM 5331 C CD . PRO A 1 701 ? 14.546 58.332 42.057 1.00 15.24 ? 694 PRO A CD 1 ATOM 5332 N N . SER A 1 702 ? 18.608 58.427 39.607 1.00 17.77 ? 695 SER A N 1 ATOM 5333 C CA . SER A 1 702 ? 19.182 59.018 38.405 1.00 18.75 ? 695 SER A CA 1 ATOM 5334 C C . SER A 1 702 ? 18.378 58.565 37.170 1.00 19.99 ? 695 SER A C 1 ATOM 5335 O O . SER A 1 702 ? 18.063 57.367 37.015 1.00 20.37 ? 695 SER A O 1 ATOM 5336 C CB . SER A 1 702 ? 20.670 58.593 38.236 1.00 19.13 ? 695 SER A CB 1 ATOM 5337 O OG . SER A 1 702 ? 21.101 58.971 36.926 1.00 19.30 ? 695 SER A OG 1 ATOM 5338 N N . SER A 1 703 ? 18.047 59.509 36.279 1.00 20.82 ? 696 SER A N 1 ATOM 5339 C CA . SER A 1 703 ? 17.357 59.166 35.058 1.00 20.48 ? 696 SER A CA 1 ATOM 5340 C C . SER A 1 703 ? 18.202 58.255 34.126 1.00 20.95 ? 696 SER A C 1 ATOM 5341 O O . SER A 1 703 ? 17.669 57.663 33.140 1.00 20.81 ? 696 SER A O 1 ATOM 5342 C CB . SER A 1 703 ? 16.905 60.448 34.341 1.00 20.85 ? 696 SER A CB 1 ATOM 5343 O OG A SER A 1 703 ? 16.008 61.189 35.134 0.50 14.97 ? 696 SER A OG 1 ATOM 5344 O OG B SER A 1 703 ? 18.013 61.135 33.842 0.50 24.51 ? 696 SER A OG 1 ATOM 5345 N N . HIS A 1 704 ? 19.497 58.157 34.411 1.00 19.85 ? 697 HIS A N 1 ATOM 5346 C CA . HIS A 1 704 ? 20.412 57.304 33.617 1.00 21.12 ? 697 HIS A CA 1 ATOM 5347 C C . HIS A 1 704 ? 20.770 56.014 34.339 1.00 21.50 ? 697 HIS A C 1 ATOM 5348 O O . HIS A 1 704 ? 21.370 55.116 33.730 1.00 23.26 ? 697 HIS A O 1 ATOM 5349 C CB . HIS A 1 704 ? 21.703 58.078 33.241 1.00 20.90 ? 697 HIS A CB 1 ATOM 5350 C CG . HIS A 1 704 ? 21.394 59.391 32.594 1.00 22.89 ? 697 HIS A CG 1 ATOM 5351 N ND1 . HIS A 1 704 ? 21.148 59.507 31.247 1.00 24.33 ? 697 HIS A ND1 1 ATOM 5352 C CD2 . HIS A 1 704 ? 21.174 60.621 33.127 1.00 25.07 ? 697 HIS A CD2 1 ATOM 5353 C CE1 . HIS A 1 704 ? 20.829 60.761 30.963 1.00 26.74 ? 697 HIS A CE1 1 ATOM 5354 N NE2 . HIS A 1 704 ? 20.839 61.459 32.091 1.00 25.42 ? 697 HIS A NE2 1 ATOM 5355 N N . ASN A 1 705 ? 20.397 55.902 35.615 1.00 20.57 ? 698 ASN A N 1 ATOM 5356 C CA . ASN A 1 705 ? 20.767 54.689 36.370 1.00 20.24 ? 698 ASN A CA 1 ATOM 5357 C C . ASN A 1 705 ? 19.903 54.626 37.620 1.00 19.02 ? 698 ASN A C 1 ATOM 5358 O O . ASN A 1 705 ? 20.229 55.265 38.631 1.00 18.17 ? 698 ASN A O 1 ATOM 5359 C CB . ASN A 1 705 ? 22.260 54.751 36.800 1.00 20.26 ? 698 ASN A CB 1 ATOM 5360 C CG . ASN A 1 705 ? 22.639 53.596 37.725 1.00 21.64 ? 698 ASN A CG 1 ATOM 5361 O OD1 . ASN A 1 705 ? 21.881 52.623 37.824 1.00 21.47 ? 698 ASN A OD1 1 ATOM 5362 N ND2 . ASN A 1 705 ? 23.793 53.702 38.428 1.00 20.46 ? 698 ASN A ND2 1 ATOM 5363 N N . LYS A 1 706 ? 18.807 53.859 37.568 1.00 18.86 ? 699 LYS A N 1 ATOM 5364 C CA . LYS A 1 706 ? 17.827 53.832 38.683 1.00 18.66 ? 699 LYS A CA 1 ATOM 5365 C C . LYS A 1 706 ? 18.515 53.531 40.024 1.00 18.81 ? 699 LYS A C 1 ATOM 5366 O O . LYS A 1 706 ? 18.057 53.986 41.093 1.00 18.80 ? 699 LYS A O 1 ATOM 5367 C CB . LYS A 1 706 ? 16.793 52.726 38.397 1.00 19.14 ? 699 LYS A CB 1 ATOM 5368 C CG . LYS A 1 706 ? 15.674 52.689 39.359 1.00 19.59 ? 699 LYS A CG 1 ATOM 5369 C CD . LYS A 1 706 ? 14.691 51.580 38.932 1.00 18.91 ? 699 LYS A CD 1 ATOM 5370 C CE . LYS A 1 706 ? 13.427 51.686 39.768 1.00 18.40 ? 699 LYS A CE 1 ATOM 5371 N NZ . LYS A 1 706 ? 12.505 50.537 39.465 1.00 18.85 ? 699 LYS A NZ 1 ATOM 5372 N N . TYR A 1 707 ? 19.613 52.765 40.004 1.00 18.53 ? 700 TYR A N 1 ATOM 5373 C CA . TYR A 1 707 ? 20.259 52.443 41.292 1.00 19.29 ? 700 TYR A CA 1 ATOM 5374 C C . TYR A 1 707 ? 20.886 53.639 42.015 1.00 19.69 ? 700 TYR A C 1 ATOM 5375 O O . TYR A 1 707 ? 21.059 53.595 43.234 1.00 20.87 ? 700 TYR A O 1 ATOM 5376 C CB . TYR A 1 707 ? 21.390 51.420 41.107 1.00 19.01 ? 700 TYR A CB 1 ATOM 5377 C CG . TYR A 1 707 ? 20.983 50.019 40.631 1.00 19.11 ? 700 TYR A CG 1 ATOM 5378 C CD1 . TYR A 1 707 ? 19.836 49.385 41.113 1.00 18.08 ? 700 TYR A CD1 1 ATOM 5379 C CD2 . TYR A 1 707 ? 21.824 49.308 39.767 1.00 20.40 ? 700 TYR A CD2 1 ATOM 5380 C CE1 . TYR A 1 707 ? 19.486 48.082 40.694 1.00 20.12 ? 700 TYR A CE1 1 ATOM 5381 C CE2 . TYR A 1 707 ? 21.508 47.988 39.340 1.00 21.95 ? 700 TYR A CE2 1 ATOM 5382 C CZ . TYR A 1 707 ? 20.340 47.395 39.807 1.00 21.33 ? 700 TYR A CZ 1 ATOM 5383 O OH . TYR A 1 707 ? 20.042 46.133 39.383 1.00 22.06 ? 700 TYR A OH 1 ATOM 5384 N N . ALA A 1 708 ? 21.319 54.651 41.274 1.00 18.97 ? 701 ALA A N 1 ATOM 5385 C CA . ALA A 1 708 ? 22.100 55.746 41.871 1.00 19.47 ? 701 ALA A CA 1 ATOM 5386 C C . ALA A 1 708 ? 21.183 56.901 42.285 1.00 20.11 ? 701 ALA A C 1 ATOM 5387 O O . ALA A 1 708 ? 20.242 57.230 41.544 1.00 20.67 ? 701 ALA A O 1 ATOM 5388 C CB . ALA A 1 708 ? 23.176 56.254 40.838 1.00 19.92 ? 701 ALA A CB 1 ATOM 5389 N N . GLY A 1 709 ? 21.434 57.536 43.436 1.00 19.84 ? 702 GLY A N 1 ATOM 5390 C CA . GLY A 1 709 ? 20.630 58.715 43.799 1.00 20.43 ? 702 GLY A CA 1 ATOM 5391 C C . GLY A 1 709 ? 21.215 59.948 43.090 1.00 20.69 ? 702 GLY A C 1 ATOM 5392 O O . GLY A 1 709 ? 22.433 60.047 42.891 1.00 20.19 ? 702 GLY A O 1 ATOM 5393 N N . GLU A 1 710 ? 20.354 60.882 42.700 1.00 19.32 ? 703 GLU A N 1 ATOM 5394 C CA . GLU A 1 710 ? 20.814 62.135 42.111 1.00 18.74 ? 703 GLU A CA 1 ATOM 5395 C C . GLU A 1 710 ? 20.273 63.243 43.022 1.00 18.00 ? 703 GLU A C 1 ATOM 5396 O O . GLU A 1 710 ? 19.152 63.151 43.495 1.00 18.06 ? 703 GLU A O 1 ATOM 5397 C CB . GLU A 1 710 ? 20.262 62.294 40.668 1.00 19.28 ? 703 GLU A CB 1 ATOM 5398 C CG . GLU A 1 710 ? 20.826 63.579 39.902 1.00 18.81 ? 703 GLU A CG 1 ATOM 5399 C CD . GLU A 1 710 ? 22.371 63.584 39.978 1.00 21.11 ? 703 GLU A CD 1 ATOM 5400 O OE1 . GLU A 1 710 ? 22.977 62.819 39.213 1.00 20.72 ? 703 GLU A OE1 1 ATOM 5401 O OE2 . GLU A 1 710 ? 22.985 64.279 40.842 1.00 23.68 ? 703 GLU A OE2 1 ATOM 5402 N N . SER A 1 711 ? 21.057 64.283 43.288 1.00 17.24 ? 704 SER A N 1 ATOM 5403 C CA . SER A 1 711 ? 20.571 65.390 44.079 1.00 17.10 ? 704 SER A CA 1 ATOM 5404 C C . SER A 1 711 ? 20.070 66.524 43.201 1.00 17.16 ? 704 SER A C 1 ATOM 5405 O O . SER A 1 711 ? 20.522 66.653 42.044 1.00 18.32 ? 704 SER A O 1 ATOM 5406 C CB . SER A 1 711 ? 21.680 65.870 45.075 1.00 17.57 ? 704 SER A CB 1 ATOM 5407 O OG . SER A 1 711 ? 22.886 66.207 44.373 1.00 18.84 ? 704 SER A OG 1 ATOM 5408 N N . PHE A 1 712 ? 19.139 67.343 43.726 1.00 16.99 ? 705 PHE A N 1 ATOM 5409 C CA . PHE A 1 712 ? 18.395 68.332 42.867 1.00 16.56 ? 705 PHE A CA 1 ATOM 5410 C C . PHE A 1 712 ? 18.140 67.763 41.458 1.00 16.07 ? 705 PHE A C 1 ATOM 5411 O O . PHE A 1 712 ? 18.527 68.372 40.446 1.00 15.53 ? 705 PHE A O 1 ATOM 5412 C CB . PHE A 1 712 ? 19.146 69.667 42.797 1.00 16.17 ? 705 PHE A CB 1 ATOM 5413 C CG . PHE A 1 712 ? 19.091 70.421 44.104 1.00 17.54 ? 705 PHE A CG 1 ATOM 5414 C CD1 . PHE A 1 712 ? 17.838 70.692 44.720 1.00 16.43 ? 705 PHE A CD1 1 ATOM 5415 C CD2 . PHE A 1 712 ? 20.279 70.813 44.757 1.00 16.27 ? 705 PHE A CD2 1 ATOM 5416 C CE1 . PHE A 1 712 ? 17.785 71.396 45.971 1.00 17.28 ? 705 PHE A CE1 1 ATOM 5417 C CE2 . PHE A 1 712 ? 20.232 71.503 45.985 1.00 18.55 ? 705 PHE A CE2 1 ATOM 5418 C CZ . PHE A 1 712 ? 18.978 71.806 46.586 1.00 17.17 ? 705 PHE A CZ 1 ATOM 5419 N N . PRO A 1 713 ? 17.458 66.600 41.397 1.00 15.87 ? 706 PRO A N 1 ATOM 5420 C CA . PRO A 1 713 ? 17.274 65.918 40.104 1.00 15.55 ? 706 PRO A CA 1 ATOM 5421 C C . PRO A 1 713 ? 16.546 66.757 39.079 1.00 16.44 ? 706 PRO A C 1 ATOM 5422 O O . PRO A 1 713 ? 16.836 66.623 37.895 1.00 17.93 ? 706 PRO A O 1 ATOM 5423 C CB . PRO A 1 713 ? 16.435 64.666 40.454 1.00 13.92 ? 706 PRO A CB 1 ATOM 5424 C CG . PRO A 1 713 ? 15.740 65.053 41.767 1.00 16.07 ? 706 PRO A CG 1 ATOM 5425 C CD . PRO A 1 713 ? 16.763 65.916 42.508 1.00 15.27 ? 706 PRO A CD 1 ATOM 5426 N N . GLY A 1 714 ? 15.582 67.595 39.489 1.00 16.58 ? 707 GLY A N 1 ATOM 5427 C CA . GLY A 1 714 ? 14.872 68.379 38.491 1.00 16.64 ? 707 GLY A CA 1 ATOM 5428 C C . GLY A 1 714 ? 15.815 69.333 37.758 1.00 17.27 ? 707 GLY A C 1 ATOM 5429 O O . GLY A 1 714 ? 15.765 69.455 36.490 1.00 17.63 ? 707 GLY A O 1 ATOM 5430 N N . ILE A 1 715 ? 16.681 70.016 38.525 1.00 16.66 ? 708 ILE A N 1 ATOM 5431 C CA . ILE A 1 715 ? 17.714 70.870 37.893 1.00 16.97 ? 708 ILE A CA 1 ATOM 5432 C C . ILE A 1 715 ? 18.751 70.039 37.129 1.00 17.92 ? 708 ILE A C 1 ATOM 5433 O O . ILE A 1 715 ? 19.175 70.425 36.016 1.00 17.31 ? 708 ILE A O 1 ATOM 5434 C CB . ILE A 1 715 ? 18.456 71.752 38.911 1.00 16.55 ? 708 ILE A CB 1 ATOM 5435 C CG1 . ILE A 1 715 ? 17.448 72.490 39.815 1.00 16.14 ? 708 ILE A CG1 1 ATOM 5436 C CG2 . ILE A 1 715 ? 19.310 72.837 38.178 1.00 17.87 ? 708 ILE A CG2 1 ATOM 5437 C CD1 . ILE A 1 715 ? 18.150 73.252 41.022 1.00 16.31 ? 708 ILE A CD1 1 ATOM 5438 N N . TYR A 1 716 ? 19.193 68.915 37.728 1.00 16.98 ? 709 TYR A N 1 ATOM 5439 C CA . TYR A 1 716 ? 20.221 68.123 37.078 1.00 17.33 ? 709 TYR A CA 1 ATOM 5440 C C . TYR A 1 716 ? 19.771 67.695 35.663 1.00 17.94 ? 709 TYR A C 1 ATOM 5441 O O . TYR A 1 716 ? 20.522 67.859 34.687 1.00 18.68 ? 709 TYR A O 1 ATOM 5442 C CB . TYR A 1 716 ? 20.610 66.896 37.937 1.00 16.59 ? 709 TYR A CB 1 ATOM 5443 C CG . TYR A 1 716 ? 21.686 66.057 37.249 1.00 18.09 ? 709 TYR A CG 1 ATOM 5444 C CD1 . TYR A 1 716 ? 23.041 66.255 37.540 1.00 19.22 ? 709 TYR A CD1 1 ATOM 5445 C CD2 . TYR A 1 716 ? 21.339 65.110 36.259 1.00 20.09 ? 709 TYR A CD2 1 ATOM 5446 C CE1 . TYR A 1 716 ? 24.065 65.508 36.898 1.00 20.80 ? 709 TYR A CE1 1 ATOM 5447 C CE2 . TYR A 1 716 ? 22.342 64.369 35.576 1.00 20.64 ? 709 TYR A CE2 1 ATOM 5448 C CZ . TYR A 1 716 ? 23.706 64.581 35.915 1.00 21.38 ? 709 TYR A CZ 1 ATOM 5449 O OH . TYR A 1 716 ? 24.691 63.865 35.284 1.00 22.17 ? 709 TYR A OH 1 ATOM 5450 N N . ASP A 1 717 ? 18.545 67.150 35.562 1.00 17.83 ? 710 ASP A N 1 ATOM 5451 C CA . ASP A 1 717 ? 18.044 66.650 34.295 1.00 18.54 ? 710 ASP A CA 1 ATOM 5452 C C . ASP A 1 717 ? 17.812 67.813 33.320 1.00 18.83 ? 710 ASP A C 1 ATOM 5453 O O . ASP A 1 717 ? 18.084 67.678 32.138 1.00 18.77 ? 710 ASP A O 1 ATOM 5454 C CB . ASP A 1 717 ? 16.767 65.806 34.454 1.00 18.83 ? 710 ASP A CB 1 ATOM 5455 C CG . ASP A 1 717 ? 17.045 64.415 35.045 1.00 19.09 ? 710 ASP A CG 1 ATOM 5456 O OD1 . ASP A 1 717 ? 18.206 63.954 35.073 1.00 20.89 ? 710 ASP A OD1 1 ATOM 5457 O OD2 . ASP A 1 717 ? 16.091 63.790 35.533 1.00 20.99 ? 710 ASP A OD2 1 ATOM 5458 N N . ALA A 1 718 ? 17.390 68.971 33.816 1.00 18.56 ? 711 ALA A N 1 ATOM 5459 C CA . ALA A 1 718 ? 17.266 70.146 32.928 1.00 19.35 ? 711 ALA A CA 1 ATOM 5460 C C . ALA A 1 718 ? 18.616 70.609 32.351 1.00 20.00 ? 711 ALA A C 1 ATOM 5461 O O . ALA A 1 718 ? 18.681 71.059 31.192 1.00 20.56 ? 711 ALA A O 1 ATOM 5462 C CB . ALA A 1 718 ? 16.532 71.334 33.675 1.00 18.81 ? 711 ALA A CB 1 ATOM 5463 N N . LEU A 1 719 ? 19.699 70.459 33.120 1.00 19.79 ? 712 LEU A N 1 ATOM 5464 C CA . LEU A 1 719 ? 21.063 70.794 32.616 1.00 19.96 ? 712 LEU A CA 1 ATOM 5465 C C . LEU A 1 719 ? 21.700 69.701 31.787 1.00 20.51 ? 712 LEU A C 1 ATOM 5466 O O . LEU A 1 719 ? 22.640 69.966 31.034 1.00 19.76 ? 712 LEU A O 1 ATOM 5467 C CB . LEU A 1 719 ? 22.009 71.122 33.788 1.00 20.74 ? 712 LEU A CB 1 ATOM 5468 C CG . LEU A 1 719 ? 21.703 72.480 34.440 1.00 20.34 ? 712 LEU A CG 1 ATOM 5469 C CD1 . LEU A 1 719 ? 22.335 72.565 35.834 1.00 20.29 ? 712 LEU A CD1 1 ATOM 5470 C CD2 . LEU A 1 719 ? 22.208 73.591 33.507 1.00 22.16 ? 712 LEU A CD2 1 ATOM 5471 N N . PHE A 1 720 ? 21.207 68.469 31.943 1.00 20.01 ? 713 PHE A N 1 ATOM 5472 C CA . PHE A 1 720 ? 21.921 67.335 31.348 1.00 22.31 ? 713 PHE A CA 1 ATOM 5473 C C . PHE A 1 720 ? 21.918 67.425 29.811 1.00 22.55 ? 713 PHE A C 1 ATOM 5474 O O . PHE A 1 720 ? 20.840 67.562 29.174 1.00 21.42 ? 713 PHE A O 1 ATOM 5475 C CB . PHE A 1 720 ? 21.413 65.957 31.826 1.00 21.78 ? 713 PHE A CB 1 ATOM 5476 C CG . PHE A 1 720 ? 22.241 64.811 31.276 1.00 23.60 ? 713 PHE A CG 1 ATOM 5477 C CD1 . PHE A 1 720 ? 23.434 64.419 31.927 1.00 22.74 ? 713 PHE A CD1 1 ATOM 5478 C CD2 . PHE A 1 720 ? 21.852 64.150 30.101 1.00 23.10 ? 713 PHE A CD2 1 ATOM 5479 C CE1 . PHE A 1 720 ? 24.251 63.377 31.404 1.00 25.54 ? 713 PHE A CE1 1 ATOM 5480 C CE2 . PHE A 1 720 ? 22.681 63.081 29.552 1.00 24.95 ? 713 PHE A CE2 1 ATOM 5481 C CZ . PHE A 1 720 ? 23.865 62.706 30.219 1.00 25.49 ? 713 PHE A CZ 1 ATOM 5482 N N . ASP A 1 721 ? 23.123 67.414 29.246 1.00 22.91 ? 714 ASP A N 1 ATOM 5483 C CA . ASP A 1 721 ? 23.324 67.432 27.766 1.00 25.25 ? 714 ASP A CA 1 ATOM 5484 C C . ASP A 1 721 ? 22.687 68.665 27.123 1.00 26.10 ? 714 ASP A C 1 ATOM 5485 O O . ASP A 1 721 ? 22.266 68.611 25.966 1.00 26.05 ? 714 ASP A O 1 ATOM 5486 C CB . ASP A 1 721 ? 22.763 66.133 27.125 1.00 25.14 ? 714 ASP A CB 1 ATOM 5487 C CG . ASP A 1 721 ? 23.169 65.966 25.647 1.00 27.32 ? 714 ASP A CG 1 ATOM 5488 O OD1 . ASP A 1 721 ? 24.341 66.180 25.277 1.00 28.54 ? 714 ASP A OD1 1 ATOM 5489 O OD2 . ASP A 1 721 ? 22.317 65.582 24.837 1.00 31.38 ? 714 ASP A OD2 1 ATOM 5490 N N . ILE A 1 722 ? 22.629 69.781 27.871 1.00 26.85 ? 715 ILE A N 1 ATOM 5491 C CA . ILE A 1 722 ? 21.816 70.933 27.458 1.00 27.13 ? 715 ILE A CA 1 ATOM 5492 C C . ILE A 1 722 ? 22.383 71.577 26.174 1.00 29.71 ? 715 ILE A C 1 ATOM 5493 O O . ILE A 1 722 ? 21.607 72.174 25.378 1.00 29.71 ? 715 ILE A O 1 ATOM 5494 C CB . ILE A 1 722 ? 21.677 71.982 28.604 1.00 26.43 ? 715 ILE A CB 1 ATOM 5495 C CG1 . ILE A 1 722 ? 20.698 73.096 28.230 1.00 25.06 ? 715 ILE A CG1 1 ATOM 5496 C CG2 . ILE A 1 722 ? 23.017 72.625 28.923 1.00 24.79 ? 715 ILE A CG2 1 ATOM 5497 C CD1 . ILE A 1 722 ? 20.138 73.781 29.431 1.00 23.49 ? 715 ILE A CD1 1 ATOM 5498 N N . GLU A 1 723 ? 23.708 71.426 25.967 1.00 31.55 ? 716 GLU A N 1 ATOM 5499 C CA . GLU A 1 723 ? 24.390 72.002 24.820 1.00 35.34 ? 716 GLU A CA 1 ATOM 5500 C C . GLU A 1 723 ? 23.935 71.366 23.499 1.00 36.68 ? 716 GLU A C 1 ATOM 5501 O O . GLU A 1 723 ? 24.194 71.917 22.423 1.00 37.76 ? 716 GLU A O 1 ATOM 5502 C CB . GLU A 1 723 ? 25.937 71.980 24.971 1.00 35.46 ? 716 GLU A CB 1 ATOM 5503 C CG . GLU A 1 723 ? 26.616 70.586 24.867 1.00 37.40 ? 716 GLU A CG 1 ATOM 5504 C CD . GLU A 1 723 ? 26.565 69.759 26.177 1.00 38.05 ? 716 GLU A CD 1 ATOM 5505 O OE1 . GLU A 1 723 ? 25.836 70.100 27.144 1.00 34.95 ? 716 GLU A OE1 1 ATOM 5506 O OE2 . GLU A 1 723 ? 27.278 68.734 26.229 1.00 39.84 ? 716 GLU A OE2 1 ATOM 5507 N N . SER A 1 724 ? 23.242 70.234 23.588 1.00 37.60 ? 717 SER A N 1 ATOM 5508 C CA . SER A 1 724 ? 22.725 69.523 22.414 1.00 38.81 ? 717 SER A CA 1 ATOM 5509 C C . SER A 1 724 ? 21.293 69.891 22.109 1.00 39.37 ? 717 SER A C 1 ATOM 5510 O O . SER A 1 724 ? 20.785 69.496 21.066 1.00 40.18 ? 717 SER A O 1 ATOM 5511 C CB . SER A 1 724 ? 22.767 68.008 22.642 1.00 38.99 ? 717 SER A CB 1 ATOM 5512 O OG . SER A 1 724 ? 24.113 67.595 22.758 1.00 38.10 ? 717 SER A OG 1 ATOM 5513 N N . LYS A 1 725 ? 20.633 70.638 22.993 1.00 38.45 ? 718 LYS A N 1 ATOM 5514 C CA . LYS A 1 725 ? 19.221 70.931 22.776 1.00 39.07 ? 718 LYS A CA 1 ATOM 5515 C C . LYS A 1 725 ? 19.070 71.927 21.631 1.00 39.79 ? 718 LYS A C 1 ATOM 5516 O O . LYS A 1 725 ? 19.914 72.828 21.454 1.00 39.50 ? 718 LYS A O 1 ATOM 5517 C CB . LYS A 1 725 ? 18.505 71.458 24.037 1.00 38.14 ? 718 LYS A CB 1 ATOM 5518 C CG . LYS A 1 725 ? 18.519 70.519 25.196 1.00 38.19 ? 718 LYS A CG 1 ATOM 5519 C CD . LYS A 1 725 ? 17.923 69.192 24.790 1.00 40.41 ? 718 LYS A CD 1 ATOM 5520 C CE . LYS A 1 725 ? 18.104 68.171 25.890 1.00 40.13 ? 718 LYS A CE 1 ATOM 5521 N NZ . LYS A 1 725 ? 17.225 68.585 27.046 1.00 38.26 ? 718 LYS A NZ 1 ATOM 5522 N N . VAL A 1 726 ? 17.976 71.782 20.882 1.00 40.28 ? 719 VAL A N 1 ATOM 5523 C CA . VAL A 1 726 ? 17.800 72.553 19.632 1.00 41.29 ? 719 VAL A CA 1 ATOM 5524 C C . VAL A 1 726 ? 17.328 73.989 19.935 1.00 40.26 ? 719 VAL A C 1 ATOM 5525 O O . VAL A 1 726 ? 17.642 74.922 19.207 1.00 40.05 ? 719 VAL A O 1 ATOM 5526 C CB . VAL A 1 726 ? 16.868 71.772 18.629 1.00 42.10 ? 719 VAL A CB 1 ATOM 5527 C CG1 . VAL A 1 726 ? 16.371 72.654 17.500 0.85 42.48 ? 719 VAL A CG1 1 ATOM 5528 C CG2 . VAL A 1 726 ? 17.630 70.543 18.052 0.68 43.15 ? 719 VAL A CG2 1 ATOM 5529 N N . ASP A 1 727 ? 16.629 74.168 21.057 1.00 38.95 ? 720 ASP A N 1 ATOM 5530 C CA . ASP A 1 727 ? 16.061 75.472 21.403 1.00 37.29 ? 720 ASP A CA 1 ATOM 5531 C C . ASP A 1 727 ? 16.679 75.890 22.729 1.00 35.75 ? 720 ASP A C 1 ATOM 5532 O O . ASP A 1 727 ? 16.145 75.533 23.783 1.00 33.89 ? 720 ASP A O 1 ATOM 5533 C CB . ASP A 1 727 ? 14.542 75.313 21.558 1.00 37.96 ? 720 ASP A CB 1 ATOM 5534 C CG . ASP A 1 727 ? 13.838 76.628 21.816 1.00 39.35 ? 720 ASP A CG 1 ATOM 5535 O OD1 . ASP A 1 727 ? 14.505 77.632 22.149 1.00 38.53 ? 720 ASP A OD1 1 ATOM 5536 O OD2 . ASP A 1 727 ? 12.594 76.647 21.702 1.00 43.02 ? 720 ASP A OD2 1 ATOM 5537 N N . PRO A 1 728 ? 17.832 76.588 22.695 1.00 34.55 ? 721 PRO A N 1 ATOM 5538 C CA . PRO A 1 728 ? 18.476 76.831 24.005 1.00 33.65 ? 721 PRO A CA 1 ATOM 5539 C C . PRO A 1 728 ? 17.630 77.716 24.940 1.00 32.11 ? 721 PRO A C 1 ATOM 5540 O O . PRO A 1 728 ? 17.672 77.546 26.147 1.00 31.12 ? 721 PRO A O 1 ATOM 5541 C CB . PRO A 1 728 ? 19.806 77.518 23.654 1.00 33.80 ? 721 PRO A CB 1 ATOM 5542 C CG . PRO A 1 728 ? 19.709 77.916 22.155 1.00 35.14 ? 721 PRO A CG 1 ATOM 5543 C CD . PRO A 1 728 ? 18.647 77.034 21.543 1.00 35.34 ? 721 PRO A CD 1 ATOM 5544 N N . SER A 1 729 ? 16.867 78.643 24.368 1.00 31.08 ? 722 SER A N 1 ATOM 5545 C CA . SER A 1 729 ? 15.996 79.520 25.148 1.00 31.64 ? 722 SER A CA 1 ATOM 5546 C C . SER A 1 729 ? 14.996 78.731 25.972 1.00 30.54 ? 722 SER A C 1 ATOM 5547 O O . SER A 1 729 ? 14.837 78.961 27.188 1.00 28.96 ? 722 SER A O 1 ATOM 5548 C CB . SER A 1 729 ? 15.259 80.506 24.242 1.00 32.18 ? 722 SER A CB 1 ATOM 5549 O OG . SER A 1 729 ? 14.511 81.348 25.075 1.00 36.14 ? 722 SER A OG 1 ATOM 5550 N N . LYS A 1 730 ? 14.337 77.778 25.311 1.00 29.67 ? 723 LYS A N 1 ATOM 5551 C CA . LYS A 1 730 ? 13.435 76.888 25.991 1.00 29.29 ? 723 LYS A CA 1 ATOM 5552 C C . LYS A 1 730 ? 14.178 76.017 27.053 1.00 26.98 ? 723 LYS A C 1 ATOM 5553 O O . LYS A 1 730 ? 13.701 75.861 28.197 1.00 25.06 ? 723 LYS A O 1 ATOM 5554 C CB . LYS A 1 730 ? 12.708 76.010 24.959 1.00 30.48 ? 723 LYS A CB 1 ATOM 5555 C CG . LYS A 1 730 ? 11.545 75.180 25.558 1.00 35.35 ? 723 LYS A CG 1 ATOM 5556 C CD . LYS A 1 730 ? 10.864 74.297 24.477 0.60 37.76 ? 723 LYS A CD 1 ATOM 5557 C CE . LYS A 1 730 ? 10.022 73.193 25.105 0.50 37.94 ? 723 LYS A CE 1 ATOM 5558 N NZ . LYS A 1 730 ? 9.419 72.356 24.036 0.40 39.24 ? 723 LYS A NZ 1 ATOM 5559 N N . ALA A 1 731 ? 15.325 75.448 26.682 1.00 24.62 ? 724 ALA A N 1 ATOM 5560 C CA . ALA A 1 731 ? 16.023 74.552 27.623 1.00 23.28 ? 724 ALA A CA 1 ATOM 5561 C C . ALA A 1 731 ? 16.487 75.330 28.887 1.00 22.26 ? 724 ALA A C 1 ATOM 5562 O O . ALA A 1 731 ? 16.317 74.850 30.008 1.00 22.09 ? 724 ALA A O 1 ATOM 5563 C CB . ALA A 1 731 ? 17.243 73.905 26.926 1.00 22.55 ? 724 ALA A CB 1 ATOM 5564 N N . TRP A 1 732 ? 17.106 76.504 28.687 1.00 20.86 ? 725 TRP A N 1 ATOM 5565 C CA . TRP A 1 732 ? 17.525 77.343 29.819 1.00 21.13 ? 725 TRP A CA 1 ATOM 5566 C C . TRP A 1 732 ? 16.346 77.902 30.616 1.00 20.41 ? 725 TRP A C 1 ATOM 5567 O O . TRP A 1 732 ? 16.442 78.040 31.861 1.00 20.42 ? 725 TRP A O 1 ATOM 5568 C CB . TRP A 1 732 ? 18.526 78.423 29.393 1.00 19.93 ? 725 TRP A CB 1 ATOM 5569 C CG . TRP A 1 732 ? 19.856 77.780 29.111 1.00 21.96 ? 725 TRP A CG 1 ATOM 5570 C CD1 . TRP A 1 732 ? 20.376 77.430 27.863 1.00 23.84 ? 725 TRP A CD1 1 ATOM 5571 C CD2 . TRP A 1 732 ? 20.814 77.346 30.082 1.00 23.43 ? 725 TRP A CD2 1 ATOM 5572 N NE1 . TRP A 1 732 ? 21.611 76.814 28.025 1.00 23.10 ? 725 TRP A NE1 1 ATOM 5573 C CE2 . TRP A 1 732 ? 21.908 76.771 29.369 1.00 23.77 ? 725 TRP A CE2 1 ATOM 5574 C CE3 . TRP A 1 732 ? 20.866 77.389 31.502 1.00 23.50 ? 725 TRP A CE3 1 ATOM 5575 C CZ2 . TRP A 1 732 ? 23.051 76.250 30.028 1.00 24.25 ? 725 TRP A CZ2 1 ATOM 5576 C CZ3 . TRP A 1 732 ? 22.029 76.880 32.157 1.00 23.06 ? 725 TRP A CZ3 1 ATOM 5577 C CH2 . TRP A 1 732 ? 23.092 76.309 31.407 1.00 24.12 ? 725 TRP A CH2 1 ATOM 5578 N N . GLY A 1 733 ? 15.220 78.146 29.941 1.00 20.17 ? 726 GLY A N 1 ATOM 5579 C CA . GLY A 1 733 ? 13.933 78.509 30.663 1.00 19.45 ? 726 GLY A CA 1 ATOM 5580 C C . GLY A 1 733 ? 13.576 77.410 31.660 1.00 19.93 ? 726 GLY A C 1 ATOM 5581 O O . GLY A 1 733 ? 13.162 77.676 32.822 1.00 20.43 ? 726 GLY A O 1 ATOM 5582 N N . GLU A 1 734 ? 13.728 76.153 31.232 1.00 20.22 ? 727 GLU A N 1 ATOM 5583 C CA . GLU A 1 734 ? 13.340 75.025 32.075 1.00 20.05 ? 727 GLU A CA 1 ATOM 5584 C C . GLU A 1 734 ? 14.351 74.860 33.239 1.00 19.50 ? 727 GLU A C 1 ATOM 5585 O O . GLU A 1 734 ? 13.978 74.513 34.377 1.00 18.15 ? 727 GLU A O 1 ATOM 5586 C CB . GLU A 1 734 ? 13.201 73.760 31.216 1.00 20.87 ? 727 GLU A CB 1 ATOM 5587 C CG A GLU A 1 734 ? 12.867 72.485 31.982 1.00 21.81 ? 727 GLU A CG 1 ATOM 5588 C CD A GLU A 1 734 ? 11.498 72.519 32.739 1.00 23.64 ? 727 GLU A CD 1 ATOM 5589 O OE1 A GLU A 1 734 ? 10.681 73.441 32.504 1.00 24.92 ? 727 GLU A OE1 1 ATOM 5590 O OE2 A GLU A 1 734 ? 11.251 71.605 33.571 1.00 23.90 ? 727 GLU A OE2 1 ATOM 5591 N N . VAL A 1 735 ? 15.633 75.134 32.963 1.00 19.18 ? 728 VAL A N 1 ATOM 5592 C CA . VAL A 1 735 ? 16.629 75.132 34.053 1.00 18.48 ? 728 VAL A CA 1 ATOM 5593 C C . VAL A 1 735 ? 16.163 76.162 35.113 1.00 18.65 ? 728 VAL A C 1 ATOM 5594 O O . VAL A 1 735 ? 16.085 75.862 36.306 1.00 18.63 ? 728 VAL A O 1 ATOM 5595 C CB . VAL A 1 735 ? 18.048 75.492 33.550 1.00 18.30 ? 728 VAL A CB 1 ATOM 5596 C CG1 . VAL A 1 735 ? 19.006 75.760 34.769 1.00 17.21 ? 728 VAL A CG1 1 ATOM 5597 C CG2 . VAL A 1 735 ? 18.604 74.335 32.643 1.00 18.06 ? 728 VAL A CG2 1 ATOM 5598 N N . LYS A 1 736 ? 15.862 77.385 34.672 1.00 18.47 ? 729 LYS A N 1 ATOM 5599 C CA . LYS A 1 736 ? 15.398 78.412 35.631 1.00 18.25 ? 729 LYS A CA 1 ATOM 5600 C C . LYS A 1 736 ? 14.108 77.965 36.382 1.00 17.97 ? 729 LYS A C 1 ATOM 5601 O O . LYS A 1 736 ? 13.923 78.263 37.590 1.00 16.34 ? 729 LYS A O 1 ATOM 5602 C CB . LYS A 1 736 ? 15.165 79.753 34.919 1.00 18.04 ? 729 LYS A CB 1 ATOM 5603 C CG . LYS A 1 736 ? 16.469 80.358 34.355 1.00 17.19 ? 729 LYS A CG 1 ATOM 5604 C CD . LYS A 1 736 ? 16.179 81.591 33.451 1.00 22.45 ? 729 LYS A CD 1 ATOM 5605 C CE . LYS A 1 736 ? 15.592 82.721 34.295 1.00 24.97 ? 729 LYS A CE 1 ATOM 5606 N NZ . LYS A 1 736 ? 15.840 84.063 33.660 1.00 31.03 ? 729 LYS A NZ 1 ATOM 5607 N N . ARG A 1 737 ? 13.181 77.333 35.654 1.00 17.24 ? 730 ARG A N 1 ATOM 5608 C CA . ARG A 1 737 ? 11.964 76.866 36.309 1.00 16.59 ? 730 ARG A CA 1 ATOM 5609 C C . ARG A 1 737 ? 12.302 75.868 37.447 1.00 16.57 ? 730 ARG A C 1 ATOM 5610 O O . ARG A 1 737 ? 11.729 75.951 38.548 1.00 17.79 ? 730 ARG A O 1 ATOM 5611 C CB . ARG A 1 737 ? 10.972 76.224 35.321 1.00 16.30 ? 730 ARG A CB 1 ATOM 5612 C CG . ARG A 1 737 ? 9.603 75.923 35.998 1.00 17.09 ? 730 ARG A CG 1 ATOM 5613 C CD . ARG A 1 737 ? 8.574 75.374 34.961 1.00 20.96 ? 730 ARG A CD 1 ATOM 5614 N NE . ARG A 1 737 ? 8.786 73.944 34.760 1.00 22.06 ? 730 ARG A NE 1 ATOM 5615 C CZ . ARG A 1 737 ? 8.329 73.000 35.584 1.00 24.12 ? 730 ARG A CZ 1 ATOM 5616 N NH1 . ARG A 1 737 ? 7.652 73.311 36.709 1.00 26.39 ? 730 ARG A NH1 1 ATOM 5617 N NH2 . ARG A 1 737 ? 8.571 71.741 35.306 1.00 25.38 ? 730 ARG A NH2 1 ATOM 5618 N N . GLN A 1 738 ? 13.231 74.937 37.184 1.00 15.78 ? 731 GLN A N 1 ATOM 5619 C CA . GLN A 1 738 ? 13.610 73.948 38.164 1.00 15.73 ? 731 GLN A CA 1 ATOM 5620 C C . GLN A 1 738 ? 14.372 74.562 39.366 1.00 16.28 ? 731 GLN A C 1 ATOM 5621 O O . GLN A 1 738 ? 14.238 74.091 40.498 1.00 16.00 ? 731 GLN A O 1 ATOM 5622 C CB . GLN A 1 738 ? 14.452 72.859 37.482 1.00 15.38 ? 731 GLN A CB 1 ATOM 5623 C CG . GLN A 1 738 ? 13.622 72.026 36.467 1.00 16.16 ? 731 GLN A CG 1 ATOM 5624 C CD . GLN A 1 738 ? 12.448 71.266 37.133 1.00 19.52 ? 731 GLN A CD 1 ATOM 5625 O OE1 . GLN A 1 738 ? 12.520 70.882 38.311 1.00 19.07 ? 731 GLN A OE1 1 ATOM 5626 N NE2 . GLN A 1 738 ? 11.376 71.019 36.364 1.00 21.23 ? 731 GLN A NE2 1 ATOM 5627 N N . ILE A 1 739 ? 15.176 75.595 39.099 1.00 16.22 ? 732 ILE A N 1 ATOM 5628 C CA . ILE A 1 739 ? 15.803 76.379 40.159 1.00 16.67 ? 732 ILE A CA 1 ATOM 5629 C C . ILE A 1 739 ? 14.738 76.959 41.107 1.00 17.23 ? 732 ILE A C 1 ATOM 5630 O O . ILE A 1 739 ? 14.889 76.847 42.329 1.00 19.04 ? 732 ILE A O 1 ATOM 5631 C CB . ILE A 1 739 ? 16.737 77.504 39.632 1.00 15.09 ? 732 ILE A CB 1 ATOM 5632 C CG1 . ILE A 1 739 ? 17.963 76.902 38.880 1.00 16.98 ? 732 ILE A CG1 1 ATOM 5633 C CG2 . ILE A 1 739 ? 17.190 78.488 40.836 1.00 16.15 ? 732 ILE A CG2 1 ATOM 5634 C CD1 . ILE A 1 739 ? 18.783 78.003 38.107 1.00 16.84 ? 732 ILE A CD1 1 ATOM 5635 N N . TYR A 1 740 ? 13.716 77.604 40.546 1.00 16.82 ? 733 TYR A N 1 ATOM 5636 C CA . TYR A 1 740 ? 12.576 78.176 41.305 1.00 18.01 ? 733 TYR A CA 1 ATOM 5637 C C . TYR A 1 740 ? 11.879 77.112 42.162 1.00 16.85 ? 733 TYR A C 1 ATOM 5638 O O . TYR A 1 740 ? 11.643 77.309 43.385 1.00 15.89 ? 733 TYR A O 1 ATOM 5639 C CB . TYR A 1 740 ? 11.583 78.705 40.286 1.00 18.63 ? 733 TYR A CB 1 ATOM 5640 C CG . TYR A 1 740 ? 10.132 79.037 40.726 1.00 21.79 ? 733 TYR A CG 1 ATOM 5641 C CD1 . TYR A 1 740 ? 9.841 79.742 41.923 1.00 22.77 ? 733 TYR A CD1 1 ATOM 5642 C CD2 . TYR A 1 740 ? 9.039 78.649 39.896 1.00 21.57 ? 733 TYR A CD2 1 ATOM 5643 C CE1 . TYR A 1 740 ? 8.467 80.071 42.243 1.00 23.16 ? 733 TYR A CE1 1 ATOM 5644 C CE2 . TYR A 1 740 ? 7.755 78.986 40.174 1.00 21.87 ? 733 TYR A CE2 1 ATOM 5645 C CZ . TYR A 1 740 ? 7.449 79.712 41.339 0.80 22.79 ? 733 TYR A CZ 1 ATOM 5646 O OH . TYR A 1 740 ? 6.107 80.021 41.591 0.80 21.32 ? 733 TYR A OH 1 ATOM 5647 N N . VAL A 1 741 ? 11.565 75.993 41.531 1.00 16.30 ? 734 VAL A N 1 ATOM 5648 C CA . VAL A 1 741 ? 10.904 74.873 42.251 1.00 15.99 ? 734 VAL A CA 1 ATOM 5649 C C . VAL A 1 741 ? 11.756 74.386 43.470 1.00 16.76 ? 734 VAL A C 1 ATOM 5650 O O . VAL A 1 741 ? 11.245 74.157 44.582 1.00 17.31 ? 734 VAL A O 1 ATOM 5651 C CB . VAL A 1 741 ? 10.560 73.693 41.282 1.00 15.10 ? 734 VAL A CB 1 ATOM 5652 C CG1 . VAL A 1 741 ? 10.077 72.431 42.087 1.00 15.66 ? 734 VAL A CG1 1 ATOM 5653 C CG2 . VAL A 1 741 ? 9.449 74.138 40.299 1.00 15.60 ? 734 VAL A CG2 1 ATOM 5654 N N . ALA A 1 742 ? 13.058 74.228 43.249 1.00 17.03 ? 735 ALA A N 1 ATOM 5655 C CA . ALA A 1 742 ? 13.970 73.742 44.292 1.00 16.23 ? 735 ALA A CA 1 ATOM 5656 C C . ALA A 1 742 ? 14.127 74.771 45.404 1.00 16.03 ? 735 ALA A C 1 ATOM 5657 O O . ALA A 1 742 ? 14.056 74.411 46.597 1.00 16.88 ? 735 ALA A O 1 ATOM 5658 C CB . ALA A 1 742 ? 15.366 73.341 43.673 1.00 15.75 ? 735 ALA A CB 1 ATOM 5659 N N . ALA A 1 743 ? 14.280 76.047 45.037 1.00 16.01 ? 736 ALA A N 1 ATOM 5660 C CA . ALA A 1 743 ? 14.455 77.137 46.043 1.00 15.60 ? 736 ALA A CA 1 ATOM 5661 C C . ALA A 1 743 ? 13.176 77.230 46.892 1.00 16.08 ? 736 ALA A C 1 ATOM 5662 O O . ALA A 1 743 ? 13.214 77.328 48.119 1.00 16.05 ? 736 ALA A O 1 ATOM 5663 C CB . ALA A 1 743 ? 14.694 78.475 45.321 1.00 14.49 ? 736 ALA A CB 1 ATOM 5664 N N . PHE A 1 744 ? 12.029 77.224 46.205 1.00 16.01 ? 737 PHE A N 1 ATOM 5665 C CA . PHE A 1 744 ? 10.769 77.262 46.883 1.00 16.17 ? 737 PHE A CA 1 ATOM 5666 C C . PHE A 1 744 ? 10.628 76.093 47.847 1.00 15.98 ? 737 PHE A C 1 ATOM 5667 O O . PHE A 1 744 ? 10.226 76.285 49.019 1.00 15.81 ? 737 PHE A O 1 ATOM 5668 C CB . PHE A 1 744 ? 9.580 77.247 45.902 1.00 15.83 ? 737 PHE A CB 1 ATOM 5669 C CG . PHE A 1 744 ? 8.280 76.924 46.595 1.00 17.86 ? 737 PHE A CG 1 ATOM 5670 C CD1 . PHE A 1 744 ? 7.749 77.833 47.560 1.00 16.91 ? 737 PHE A CD1 1 ATOM 5671 C CD2 . PHE A 1 744 ? 7.652 75.691 46.385 1.00 17.89 ? 737 PHE A CD2 1 ATOM 5672 C CE1 . PHE A 1 744 ? 6.557 77.505 48.281 1.00 14.78 ? 737 PHE A CE1 1 ATOM 5673 C CE2 . PHE A 1 744 ? 6.439 75.354 47.074 1.00 16.57 ? 737 PHE A CE2 1 ATOM 5674 C CZ . PHE A 1 744 ? 5.904 76.255 48.025 1.00 15.59 ? 737 PHE A CZ 1 ATOM 5675 N N . THR A 1 745 ? 10.908 74.883 47.360 1.00 15.90 ? 738 THR A N 1 ATOM 5676 C CA . THR A 1 745 ? 10.703 73.674 48.202 1.00 15.86 ? 738 THR A CA 1 ATOM 5677 C C . THR A 1 745 ? 11.612 73.703 49.426 1.00 16.86 ? 738 THR A C 1 ATOM 5678 O O . THR A 1 745 ? 11.176 73.361 50.540 1.00 16.61 ? 738 THR A O 1 ATOM 5679 C CB . THR A 1 745 ? 10.917 72.389 47.390 1.00 15.97 ? 738 THR A CB 1 ATOM 5680 O OG1 . THR A 1 745 ? 10.011 72.427 46.246 1.00 14.27 ? 738 THR A OG1 1 ATOM 5681 C CG2 . THR A 1 745 ? 10.638 71.133 48.246 1.00 15.83 ? 738 THR A CG2 1 ATOM 5682 N N . VAL A 1 746 ? 12.878 74.114 49.237 1.00 17.02 ? 739 VAL A N 1 ATOM 5683 C CA . VAL A 1 746 ? 13.822 74.210 50.367 1.00 16.43 ? 739 VAL A CA 1 ATOM 5684 C C . VAL A 1 746 ? 13.320 75.224 51.388 1.00 16.81 ? 739 VAL A C 1 ATOM 5685 O O . VAL A 1 746 ? 13.329 74.956 52.609 1.00 16.76 ? 739 VAL A O 1 ATOM 5686 C CB . VAL A 1 746 ? 15.281 74.502 49.876 1.00 16.22 ? 739 VAL A CB 1 ATOM 5687 C CG1 . VAL A 1 746 ? 16.291 74.885 51.044 1.00 16.04 ? 739 VAL A CG1 1 ATOM 5688 C CG2 . VAL A 1 746 ? 15.826 73.294 49.094 1.00 15.77 ? 739 VAL A CG2 1 ATOM 5689 N N . GLN A 1 747 ? 12.912 76.406 50.903 1.00 16.19 ? 740 GLN A N 1 ATOM 5690 C CA . GLN A 1 747 ? 12.370 77.440 51.816 1.00 16.83 ? 740 GLN A CA 1 ATOM 5691 C C . GLN A 1 747 ? 11.108 76.932 52.553 1.00 16.29 ? 740 GLN A C 1 ATOM 5692 O O . GLN A 1 747 ? 10.957 77.127 53.774 1.00 16.35 ? 740 GLN A O 1 ATOM 5693 C CB . GLN A 1 747 ? 11.997 78.720 51.067 1.00 15.26 ? 740 GLN A CB 1 ATOM 5694 C CG . GLN A 1 747 ? 11.475 79.860 51.986 1.00 16.68 ? 740 GLN A CG 1 ATOM 5695 C CD . GLN A 1 747 ? 12.554 80.429 52.907 1.00 18.71 ? 740 GLN A CD 1 ATOM 5696 O OE1 . GLN A 1 747 ? 13.773 80.320 52.619 1.00 18.98 ? 740 GLN A OE1 1 ATOM 5697 N NE2 . GLN A 1 747 ? 12.122 81.043 54.025 1.00 19.20 ? 740 GLN A NE2 1 ATOM 5698 N N . ALA A 1 748 ? 10.219 76.274 51.820 1.00 15.94 ? 741 ALA A N 1 ATOM 5699 C CA . ALA A 1 748 ? 8.997 75.756 52.430 1.00 16.20 ? 741 ALA A CA 1 ATOM 5700 C C . ALA A 1 748 ? 9.323 74.695 53.508 1.00 16.51 ? 741 ALA A C 1 ATOM 5701 O O . ALA A 1 748 ? 8.703 74.683 54.601 1.00 17.72 ? 741 ALA A O 1 ATOM 5702 C CB . ALA A 1 748 ? 8.077 75.159 51.360 1.00 15.10 ? 741 ALA A CB 1 ATOM 5703 N N . ALA A 1 749 ? 10.274 73.809 53.219 1.00 15.71 ? 742 ALA A N 1 ATOM 5704 C CA . ALA A 1 749 ? 10.703 72.806 54.234 1.00 16.68 ? 742 ALA A CA 1 ATOM 5705 C C . ALA A 1 749 ? 11.300 73.526 55.436 1.00 16.40 ? 742 ALA A C 1 ATOM 5706 O O . ALA A 1 749 ? 11.010 73.166 56.582 1.00 16.82 ? 742 ALA A O 1 ATOM 5707 C CB . ALA A 1 749 ? 11.723 71.830 53.651 1.00 15.42 ? 742 ALA A CB 1 ATOM 5708 N N . ALA A 1 750 ? 12.150 74.537 55.179 1.00 17.40 ? 743 ALA A N 1 ATOM 5709 C CA . ALA A 1 750 ? 12.717 75.334 56.272 1.00 18.31 ? 743 ALA A CA 1 ATOM 5710 C C . ALA A 1 750 ? 11.588 75.859 57.166 1.00 18.66 ? 743 ALA A C 1 ATOM 5711 O O . ALA A 1 750 ? 11.681 75.791 58.399 1.00 19.19 ? 743 ALA A O 1 ATOM 5712 C CB . ALA A 1 750 ? 13.582 76.534 55.746 1.00 17.61 ? 743 ALA A CB 1 ATOM 5713 N N . GLU A 1 751 ? 10.550 76.417 56.546 1.00 17.59 ? 744 GLU A N 1 ATOM 5714 C CA . GLU A 1 751 ? 9.491 77.056 57.317 1.00 17.75 ? 744 GLU A CA 1 ATOM 5715 C C . GLU A 1 751 ? 8.652 76.096 58.165 1.00 17.30 ? 744 GLU A C 1 ATOM 5716 O O . GLU A 1 751 ? 7.960 76.557 59.054 1.00 17.84 ? 744 GLU A O 1 ATOM 5717 C CB . GLU A 1 751 ? 8.593 77.950 56.437 1.00 17.60 ? 744 GLU A CB 1 ATOM 5718 C CG . GLU A 1 751 ? 9.374 79.188 55.985 1.00 19.09 ? 744 GLU A CG 1 ATOM 5719 C CD . GLU A 1 751 ? 8.623 80.038 54.981 1.00 22.22 ? 744 GLU A CD 1 ATOM 5720 O OE1 . GLU A 1 751 ? 7.474 79.702 54.581 1.00 25.74 ? 744 GLU A OE1 1 ATOM 5721 O OE2 . GLU A 1 751 ? 9.188 81.072 54.587 1.00 21.90 ? 744 GLU A OE2 1 ATOM 5722 N N . THR A 1 752 ? 8.711 74.786 57.890 1.00 17.25 ? 745 THR A N 1 ATOM 5723 C CA . THR A 1 752 ? 8.019 73.816 58.746 1.00 17.40 ? 745 THR A CA 1 ATOM 5724 C C . THR A 1 752 ? 8.723 73.710 60.123 1.00 18.80 ? 745 THR A C 1 ATOM 5725 O O . THR A 1 752 ? 8.117 73.211 61.082 1.00 18.80 ? 745 THR A O 1 ATOM 5726 C CB . THR A 1 752 ? 7.872 72.414 58.104 1.00 17.22 ? 745 THR A CB 1 ATOM 5727 O OG1 . THR A 1 752 ? 9.163 71.745 58.088 1.00 18.55 ? 745 THR A OG1 1 ATOM 5728 C CG2 . THR A 1 752 ? 7.214 72.502 56.665 1.00 14.65 ? 745 THR A CG2 1 ATOM 5729 N N . LEU A 1 753 ? 9.981 74.204 60.219 1.00 19.09 ? 746 LEU A N 1 ATOM 5730 C CA . LEU A 1 753 ? 10.744 74.186 61.456 1.00 19.81 ? 746 LEU A CA 1 ATOM 5731 C C . LEU A 1 753 ? 10.686 75.513 62.228 1.00 20.01 ? 746 LEU A C 1 ATOM 5732 O O . LEU A 1 753 ? 11.174 75.582 63.349 1.00 20.00 ? 746 LEU A O 1 ATOM 5733 C CB . LEU A 1 753 ? 12.208 73.842 61.161 1.00 19.94 ? 746 LEU A CB 1 ATOM 5734 C CG . LEU A 1 753 ? 12.420 72.498 60.451 1.00 20.89 ? 746 LEU A CG 1 ATOM 5735 C CD1 . LEU A 1 753 ? 13.936 72.309 60.138 1.00 19.40 ? 746 LEU A CD1 1 ATOM 5736 C CD2 . LEU A 1 753 ? 11.840 71.283 61.306 1.00 21.97 ? 746 LEU A CD2 1 ATOM 5737 N N . SER A 1 754 ? 10.133 76.574 61.617 1.00 19.86 ? 747 SER A N 1 ATOM 5738 C CA . SER A 1 754 ? 9.907 77.831 62.324 1.00 20.19 ? 747 SER A CA 1 ATOM 5739 C C . SER A 1 754 ? 8.928 77.587 63.492 1.00 20.88 ? 747 SER A C 1 ATOM 5740 O O . SER A 1 754 ? 8.204 76.571 63.500 1.00 21.19 ? 747 SER A O 1 ATOM 5741 C CB . SER A 1 754 ? 9.317 78.858 61.368 1.00 20.80 ? 747 SER A CB 1 ATOM 5742 O OG . SER A 1 754 ? 10.248 79.078 60.315 1.00 23.87 ? 747 SER A OG 1 ATOM 5743 N N . GLU A 1 755 ? 8.897 78.482 64.477 1.00 20.99 ? 748 GLU A N 1 ATOM 5744 C CA . GLU A 1 755 ? 7.764 78.505 65.428 1.00 23.07 ? 748 GLU A CA 1 ATOM 5745 C C . GLU A 1 755 ? 6.409 78.451 64.688 1.00 22.51 ? 748 GLU A C 1 ATOM 5746 O O . GLU A 1 755 ? 6.221 79.085 63.650 1.00 21.60 ? 748 GLU A O 1 ATOM 5747 C CB . GLU A 1 755 ? 7.874 79.707 66.391 1.00 24.77 ? 748 GLU A CB 1 ATOM 5748 C CG . GLU A 1 755 ? 9.187 79.541 67.190 1.00 28.74 ? 748 GLU A CG 1 ATOM 5749 C CD . GLU A 1 755 ? 9.289 80.374 68.406 1.00 36.06 ? 748 GLU A CD 1 ATOM 5750 O OE1 . GLU A 1 755 ? 9.546 81.581 68.284 1.00 38.72 ? 748 GLU A OE1 1 ATOM 5751 O OE2 . GLU A 1 755 ? 9.175 79.798 69.492 1.00 41.00 ? 748 GLU A OE2 1 ATOM 5752 N N . VAL A 1 756 ? 5.490 77.642 65.212 1.00 22.19 ? 749 VAL A N 1 ATOM 5753 C CA . VAL A 1 756 ? 4.284 77.258 64.468 1.00 21.59 ? 749 VAL A CA 1 ATOM 5754 C C . VAL A 1 756 ? 3.248 78.381 64.503 1.00 22.34 ? 749 VAL A C 1 ATOM 5755 O O . VAL A 1 756 ? 2.337 78.383 63.699 1.00 21.88 ? 749 VAL A O 1 ATOM 5756 C CB . VAL A 1 756 ? 3.685 75.929 65.037 1.00 21.15 ? 749 VAL A CB 1 ATOM 5757 C CG1 . VAL A 1 756 ? 4.723 74.791 64.933 1.00 19.79 ? 749 VAL A CG1 1 ATOM 5758 C CG2 . VAL A 1 756 ? 3.203 76.130 66.545 1.00 19.14 ? 749 VAL A CG2 1 ATOM 5759 N N . ALA A 1 757 ? 3.377 79.310 65.461 1.00 22.58 ? 750 ALA A N 1 ATOM 5760 C CA . ALA A 1 757 ? 2.423 80.425 65.560 1.00 24.15 ? 750 ALA A CA 1 ATOM 5761 C C . ALA A 1 757 ? 3.027 81.459 66.456 1.00 26.90 ? 750 ALA A C 1 ATOM 5762 O O . ALA A 1 757 ? 2.556 82.591 66.454 1.00 29.71 ? 750 ALA A O 1 ATOM 5763 C CB . ALA A 1 757 ? 1.123 79.968 66.170 1.00 22.68 ? 750 ALA A CB 1 ATOM 5764 O OXT . ALA A 1 757 ? 3.911 81.147 67.264 1.00 26.75 ? 750 ALA A OXT 1 HETATM 5765 ZN ZN . ZN B 2 . ? 17.442 41.192 43.614 1.00 18.66 ? 801 ZN A ZN 1 HETATM 5766 ZN ZN . ZN C 2 . ? 16.688 41.927 46.733 1.00 21.31 ? 802 ZN A ZN 1 HETATM 5767 CA CA . CA D 3 . ? -0.808 49.933 41.822 1.00 16.52 ? 803 CA A CA 1 HETATM 5768 CL CL . CL E 4 . ? 19.108 46.883 52.083 1.00 24.13 ? 804 CL A CL 1 HETATM 5769 C C1 . NAG F 5 . ? 11.712 26.006 58.103 1.00 34.72 ? 805 NAG A C1 1 HETATM 5770 C C2 . NAG F 5 . ? 11.427 24.596 57.609 1.00 40.47 ? 805 NAG A C2 1 HETATM 5771 C C3 . NAG F 5 . ? 9.957 24.245 57.817 1.00 41.30 ? 805 NAG A C3 1 HETATM 5772 C C4 . NAG F 5 . ? 9.435 24.543 59.210 1.00 40.80 ? 805 NAG A C4 1 HETATM 5773 C C5 . NAG F 5 . ? 9.844 25.964 59.610 1.00 38.67 ? 805 NAG A C5 1 HETATM 5774 C C6 . NAG F 5 . ? 9.444 26.292 61.056 1.00 38.92 ? 805 NAG A C6 1 HETATM 5775 C C7 . NAG F 5 . ? 12.824 23.861 55.803 1.00 45.52 ? 805 NAG A C7 1 HETATM 5776 C C8 . NAG F 5 . ? 13.026 23.778 54.326 1.00 45.31 ? 805 NAG A C8 1 HETATM 5777 N N2 . NAG F 5 . ? 11.717 24.474 56.198 1.00 42.67 ? 805 NAG A N2 1 HETATM 5778 O O3 . NAG F 5 . ? 9.833 22.879 57.607 1.00 42.86 ? 805 NAG A O3 1 HETATM 5779 O O4 . NAG F 5 . ? 8.029 24.475 59.114 1.00 43.50 ? 805 NAG A O4 1 HETATM 5780 O O5 . NAG F 5 . ? 11.243 26.152 59.431 1.00 34.43 ? 805 NAG A O5 1 HETATM 5781 O O6 . NAG F 5 . ? 10.086 25.353 61.904 1.00 40.65 ? 805 NAG A O6 1 HETATM 5782 O O7 . NAG F 5 . ? 13.663 23.397 56.581 1.00 48.59 ? 805 NAG A O7 1 HETATM 5783 C C1 . NAG G 5 . ? 7.456 23.596 60.114 1.00 48.78 ? 806 NAG A C1 1 HETATM 5784 C C2 . NAG G 5 . ? 5.962 23.891 60.284 1.00 50.66 ? 806 NAG A C2 1 HETATM 5785 C C3 . NAG G 5 . ? 5.258 22.837 61.173 1.00 54.60 ? 806 NAG A C3 1 HETATM 5786 C C4 . NAG G 5 . ? 5.693 21.386 60.941 1.00 56.14 ? 806 NAG A C4 1 HETATM 5787 C C5 . NAG G 5 . ? 7.229 21.310 60.783 1.00 55.57 ? 806 NAG A C5 1 HETATM 5788 C C6 . NAG G 5 . ? 7.708 19.926 60.345 1.00 56.75 ? 806 NAG A C6 1 HETATM 5789 C C7 . NAG G 5 . ? 5.407 26.371 60.291 1.00 46.43 ? 806 NAG A C7 1 HETATM 5790 C C8 . NAG G 5 . ? 5.243 26.446 58.795 1.00 44.13 ? 806 NAG A C8 1 HETATM 5791 N N2 . NAG G 5 . ? 5.729 25.200 60.880 1.00 46.80 ? 806 NAG A N2 1 HETATM 5792 O O3 . NAG G 5 . ? 3.863 22.923 60.932 1.00 57.42 ? 806 NAG A O3 1 HETATM 5793 O O4 . NAG G 5 . ? 5.159 20.534 61.966 1.00 57.70 ? 806 NAG A O4 1 HETATM 5794 O O5 . NAG G 5 . ? 7.650 22.233 59.781 1.00 52.11 ? 806 NAG A O5 1 HETATM 5795 O O6 . NAG G 5 . ? 7.283 19.700 59.013 1.00 55.80 ? 806 NAG A O6 1 HETATM 5796 O O7 . NAG G 5 . ? 5.233 27.409 60.977 1.00 45.27 ? 806 NAG A O7 1 HETATM 5797 C C1 . NAG H 5 . ? 3.862 28.042 25.546 1.00 49.79 ? 807 NAG A C1 1 HETATM 5798 C C2 . NAG H 5 . ? 2.479 28.651 25.423 1.00 52.09 ? 807 NAG A C2 1 HETATM 5799 C C3 . NAG H 5 . ? 1.512 27.780 24.623 1.00 56.07 ? 807 NAG A C3 1 HETATM 5800 C C4 . NAG H 5 . ? 2.083 27.553 23.217 1.00 60.11 ? 807 NAG A C4 1 HETATM 5801 C C5 . NAG H 5 . ? 3.511 26.957 23.356 1.00 60.23 ? 807 NAG A C5 1 HETATM 5802 C C6 . NAG H 5 . ? 4.253 26.768 22.006 1.00 62.96 ? 807 NAG A C6 1 HETATM 5803 C C7 . NAG H 5 . ? 1.762 30.286 26.984 1.00 51.79 ? 807 NAG A C7 1 HETATM 5804 C C8 . NAG H 5 . ? 1.944 31.315 25.888 1.00 51.71 ? 807 NAG A C8 1 HETATM 5805 N N2 . NAG H 5 . ? 2.011 28.997 26.732 1.00 49.34 ? 807 NAG A N2 1 HETATM 5806 O O3 . NAG H 5 . ? 0.309 28.488 24.527 1.00 55.85 ? 807 NAG A O3 1 HETATM 5807 O O4 . NAG H 5 . ? 1.182 26.732 22.471 1.00 63.34 ? 807 NAG A O4 1 HETATM 5808 O O5 . NAG H 5 . ? 4.319 27.777 24.231 1.00 55.21 ? 807 NAG A O5 1 HETATM 5809 O O6 . NAG H 5 . ? 4.999 25.549 21.845 1.00 65.42 ? 807 NAG A O6 1 HETATM 5810 O O7 . NAG H 5 . ? 1.370 30.669 28.079 1.00 53.85 ? 807 NAG A O7 1 HETATM 5811 C C1 . NAG I 5 . ? 19.828 24.935 18.050 1.00 43.31 ? 808 NAG A C1 1 HETATM 5812 C C2 . NAG I 5 . ? 20.449 23.727 17.368 1.00 45.82 ? 808 NAG A C2 1 HETATM 5813 C C3 . NAG I 5 . ? 19.615 23.321 16.151 1.00 47.29 ? 808 NAG A C3 1 HETATM 5814 C C4 . NAG I 5 . ? 18.107 23.175 16.442 1.00 49.12 ? 808 NAG A C4 1 HETATM 5815 C C5 . NAG I 5 . ? 17.569 24.344 17.318 1.00 46.74 ? 808 NAG A C5 1 HETATM 5816 C C6 . NAG I 5 . ? 16.140 24.136 17.862 1.00 45.58 ? 808 NAG A C6 1 HETATM 5817 C C7 . NAG I 5 . ? 22.906 23.463 17.448 1.00 50.05 ? 808 NAG A C7 1 HETATM 5818 C C8 . NAG I 5 . ? 24.255 23.781 16.854 1.00 50.43 ? 808 NAG A C8 1 HETATM 5819 N N2 . NAG I 5 . ? 21.805 23.994 16.896 1.00 48.34 ? 808 NAG A N2 1 HETATM 5820 O O3 . NAG I 5 . ? 20.196 22.136 15.642 1.00 45.62 ? 808 NAG A O3 1 HETATM 5821 O O4 . NAG I 5 . ? 17.433 23.139 15.187 1.00 56.11 ? 808 NAG A O4 1 HETATM 5822 O O5 . NAG I 5 . ? 18.463 24.681 18.385 1.00 43.33 ? 808 NAG A O5 1 HETATM 5823 O O6 . NAG I 5 . ? 16.035 23.000 18.702 1.00 46.25 ? 808 NAG A O6 1 HETATM 5824 O O7 . NAG I 5 . ? 22.864 22.722 18.420 1.00 51.67 ? 808 NAG A O7 1 HETATM 5825 C C1 . NAG J 5 . ? 16.409 22.109 15.074 1.00 60.99 ? 809 NAG A C1 1 HETATM 5826 C C2 . NAG J 5 . ? 15.394 22.612 14.043 1.00 63.45 ? 809 NAG A C2 1 HETATM 5827 C C3 . NAG J 5 . ? 14.331 21.563 13.693 1.00 65.59 ? 809 NAG A C3 1 HETATM 5828 C C4 . NAG J 5 . ? 15.010 20.248 13.293 1.00 66.32 ? 809 NAG A C4 1 HETATM 5829 C C5 . NAG J 5 . ? 15.882 19.824 14.494 1.00 65.11 ? 809 NAG A C5 1 HETATM 5830 C C6 . NAG J 5 . ? 16.516 18.449 14.304 1.00 65.64 ? 809 NAG A C6 1 HETATM 5831 C C7 . NAG J 5 . ? 15.177 25.055 14.060 1.00 61.97 ? 809 NAG A C7 1 HETATM 5832 C C8 . NAG J 5 . ? 14.427 26.239 14.620 1.00 59.58 ? 809 NAG A C8 1 HETATM 5833 N N2 . NAG J 5 . ? 14.775 23.849 14.490 1.00 62.56 ? 809 NAG A N2 1 HETATM 5834 O O3 . NAG J 5 . ? 13.536 22.039 12.632 1.00 66.39 ? 809 NAG A O3 1 HETATM 5835 O O4 . NAG J 5 . ? 14.070 19.272 12.834 1.00 67.65 ? 809 NAG A O4 1 HETATM 5836 O O5 . NAG J 5 . ? 16.894 20.813 14.734 1.00 62.73 ? 809 NAG A O5 1 HETATM 5837 O O6 . NAG J 5 . ? 17.828 18.606 13.814 1.00 65.01 ? 809 NAG A O6 1 HETATM 5838 O O7 . NAG J 5 . ? 16.104 25.223 13.254 1.00 62.11 ? 809 NAG A O7 1 HETATM 5839 C C1 . NAG K 5 . ? 19.774 54.155 10.565 1.00 74.30 ? 810 NAG A C1 1 HETATM 5840 C C2 . NAG K 5 . ? 19.067 55.512 10.508 1.00 79.39 ? 810 NAG A C2 1 HETATM 5841 C C3 . NAG K 5 . ? 17.614 55.271 10.089 1.00 80.52 ? 810 NAG A C3 1 HETATM 5842 C C4 . NAG K 5 . ? 17.537 54.596 8.712 1.00 81.64 ? 810 NAG A C4 1 HETATM 5843 C C5 . NAG K 5 . ? 18.364 53.303 8.632 1.00 80.96 ? 810 NAG A C5 1 HETATM 5844 C C6 . NAG K 5 . ? 18.619 52.981 7.147 1.00 81.74 ? 810 NAG A C6 1 HETATM 5845 C C7 . NAG K 5 . ? 19.868 57.254 12.156 1.00 81.67 ? 810 NAG A C7 1 HETATM 5846 C C8 . NAG K 5 . ? 19.711 57.710 13.589 1.00 82.13 ? 810 NAG A C8 1 HETATM 5847 N N2 . NAG K 5 . ? 19.132 56.185 11.804 1.00 80.44 ? 810 NAG A N2 1 HETATM 5848 O O3 . NAG K 5 . ? 16.913 56.496 10.082 1.00 80.59 ? 810 NAG A O3 1 HETATM 5849 O O4 . NAG K 5 . ? 16.191 54.318 8.375 1.00 82.86 ? 810 NAG A O4 1 HETATM 5850 O O5 . NAG K 5 . ? 19.613 53.395 9.347 1.00 78.74 ? 810 NAG A O5 1 HETATM 5851 O O6 . NAG K 5 . ? 18.697 51.594 6.885 1.00 81.90 ? 810 NAG A O6 1 HETATM 5852 O O7 . NAG K 5 . ? 20.632 57.860 11.403 1.00 81.70 ? 810 NAG A O7 1 HETATM 5853 C C1 . NAG L 5 . ? 36.572 37.769 53.095 1.00 39.56 ? 811 NAG A C1 1 HETATM 5854 C C2 . NAG L 5 . ? 36.582 37.867 51.566 1.00 38.84 ? 811 NAG A C2 1 HETATM 5855 C C3 . NAG L 5 . ? 37.933 37.405 50.976 1.00 42.85 ? 811 NAG A C3 1 HETATM 5856 C C4 . NAG L 5 . ? 39.115 38.144 51.631 1.00 43.42 ? 811 NAG A C4 1 HETATM 5857 C C5 . NAG L 5 . ? 38.996 37.992 53.157 1.00 44.57 ? 811 NAG A C5 1 HETATM 5858 C C6 . NAG L 5 . ? 40.142 38.745 53.844 1.00 45.12 ? 811 NAG A C6 1 HETATM 5859 C C7 . NAG L 5 . ? 34.496 37.698 50.281 1.00 30.91 ? 811 NAG A C7 1 HETATM 5860 C C8 . NAG L 5 . ? 33.391 36.847 49.728 1.00 29.00 ? 811 NAG A C8 1 HETATM 5861 N N2 . NAG L 5 . ? 35.460 37.123 51.014 1.00 35.95 ? 811 NAG A N2 1 HETATM 5862 O O3 . NAG L 5 . ? 37.982 37.674 49.586 1.00 42.83 ? 811 NAG A O3 1 HETATM 5863 O O4 . NAG L 5 . ? 40.422 37.703 51.153 1.00 45.18 ? 811 NAG A O4 1 HETATM 5864 O O5 . NAG L 5 . ? 37.720 38.404 53.661 1.00 43.84 ? 811 NAG A O5 1 HETATM 5865 O O6 . NAG L 5 . ? 40.062 40.123 53.521 1.00 45.26 ? 811 NAG A O6 1 HETATM 5866 O O7 . NAG L 5 . ? 34.475 38.888 50.043 1.00 28.76 ? 811 NAG A O7 1 HETATM 5867 C C1 . NAG M 5 . ? 24.241 61.784 69.229 1.00 29.68 ? 812 NAG A C1 1 HETATM 5868 C C2 . NAG M 5 . ? 22.910 62.489 69.419 1.00 30.93 ? 812 NAG A C2 1 HETATM 5869 C C3 . NAG M 5 . ? 23.152 63.923 69.846 1.00 31.91 ? 812 NAG A C3 1 HETATM 5870 C C4 . NAG M 5 . ? 24.064 63.982 71.062 1.00 33.24 ? 812 NAG A C4 1 HETATM 5871 C C5 . NAG M 5 . ? 25.376 63.263 70.722 1.00 32.56 ? 812 NAG A C5 1 HETATM 5872 C C6 . NAG M 5 . ? 26.442 63.175 71.828 1.00 34.87 ? 812 NAG A C6 1 HETATM 5873 C C7 . NAG M 5 . ? 21.003 61.828 68.127 1.00 33.97 ? 812 NAG A C7 1 HETATM 5874 C C8 . NAG M 5 . ? 20.177 61.874 66.883 1.00 30.37 ? 812 NAG A C8 1 HETATM 5875 N N2 . NAG M 5 . ? 22.123 62.530 68.211 1.00 30.65 ? 812 NAG A N2 1 HETATM 5876 O O3 . NAG M 5 . ? 21.912 64.492 70.127 1.00 32.22 ? 812 NAG A O3 1 HETATM 5877 O O4 . NAG M 5 . ? 24.290 65.341 71.240 1.00 37.26 ? 812 NAG A O4 1 HETATM 5878 O O5 . NAG M 5 . ? 25.062 61.920 70.373 1.00 32.18 ? 812 NAG A O5 1 HETATM 5879 O O6 . NAG M 5 . ? 25.845 62.734 73.018 1.00 35.50 ? 812 NAG A O6 1 HETATM 5880 O O7 . NAG M 5 . ? 20.613 61.150 69.071 1.00 40.09 ? 812 NAG A O7 1 HETATM 5881 C C1 . NAG N 5 . ? 24.075 65.742 72.611 1.00 41.86 ? 813 NAG A C1 1 HETATM 5882 C C2 . NAG N 5 . ? 24.633 67.148 72.720 1.00 44.99 ? 813 NAG A C2 1 HETATM 5883 C C3 . NAG N 5 . ? 24.437 67.706 74.125 1.00 47.71 ? 813 NAG A C3 1 HETATM 5884 C C4 . NAG N 5 . ? 22.950 67.648 74.509 1.00 49.36 ? 813 NAG A C4 1 HETATM 5885 C C5 . NAG N 5 . ? 22.474 66.184 74.348 1.00 48.15 ? 813 NAG A C5 1 HETATM 5886 C C6 . NAG N 5 . ? 20.986 65.975 74.631 1.00 50.94 ? 813 NAG A C6 1 HETATM 5887 C C7 . NAG N 5 . ? 26.563 67.529 71.240 1.00 48.59 ? 813 NAG A C7 1 HETATM 5888 C C8 . NAG N 5 . ? 25.730 68.154 70.160 1.00 44.69 ? 813 NAG A C8 1 HETATM 5889 N N2 . NAG N 5 . ? 26.033 67.097 72.389 1.00 46.38 ? 813 NAG A N2 1 HETATM 5890 O O3 . NAG N 5 . ? 24.930 69.013 74.100 1.00 46.32 ? 813 NAG A O3 1 HETATM 5891 O O4 . NAG N 5 . ? 22.781 68.185 75.819 1.00 52.79 ? 813 NAG A O4 1 HETATM 5892 O O5 . NAG N 5 . ? 22.724 65.716 73.027 1.00 42.75 ? 813 NAG A O5 1 HETATM 5893 O O6 . NAG N 5 . ? 20.212 66.903 73.881 1.00 53.07 ? 813 NAG A O6 1 HETATM 5894 O O7 . NAG N 5 . ? 27.772 67.413 71.064 1.00 51.99 ? 813 NAG A O7 1 HETATM 5895 C C1 . NAG O 5 . ? 15.316 83.793 52.970 1.00 25.31 ? 814 NAG A C1 1 HETATM 5896 C C2 . NAG O 5 . ? 14.294 83.950 51.857 1.00 25.38 ? 814 NAG A C2 1 HETATM 5897 C C3 . NAG O 5 . ? 14.176 85.460 51.577 1.00 29.51 ? 814 NAG A C3 1 HETATM 5898 C C4 . NAG O 5 . ? 13.748 86.248 52.844 1.00 32.81 ? 814 NAG A C4 1 HETATM 5899 C C5 . NAG O 5 . ? 14.685 85.940 54.018 1.00 34.05 ? 814 NAG A C5 1 HETATM 5900 C C6 . NAG O 5 . ? 14.096 86.501 55.344 1.00 36.91 ? 814 NAG A C6 1 HETATM 5901 C C7 . NAG O 5 . ? 13.807 82.487 49.974 1.00 21.99 ? 814 NAG A C7 1 HETATM 5902 C C8 . NAG O 5 . ? 14.350 81.775 48.766 1.00 18.17 ? 814 NAG A C8 1 HETATM 5903 N N2 . NAG O 5 . ? 14.676 83.204 50.673 1.00 22.76 ? 814 NAG A N2 1 HETATM 5904 O O3 . NAG O 5 . ? 13.273 85.641 50.521 1.00 27.58 ? 814 NAG A O3 1 HETATM 5905 O O4 . NAG O 5 . ? 13.826 87.664 52.724 1.00 36.91 ? 814 NAG A O4 1 HETATM 5906 O O5 . NAG O 5 . ? 14.854 84.538 54.096 1.00 28.53 ? 814 NAG A O5 1 HETATM 5907 O O6 . NAG O 5 . ? 15.110 86.831 56.306 1.00 43.35 ? 814 NAG A O6 1 HETATM 5908 O O7 . NAG O 5 . ? 12.609 82.401 50.294 1.00 21.09 ? 814 NAG A O7 1 HETATM 5909 C C1 . NAG P 5 . ? 12.735 88.198 51.956 1.00 39.40 ? 815 NAG A C1 1 HETATM 5910 C C2 . NAG P 5 . ? 12.260 89.505 52.547 1.00 43.10 ? 815 NAG A C2 1 HETATM 5911 C C3 . NAG P 5 . ? 11.273 90.269 51.647 1.00 43.28 ? 815 NAG A C3 1 HETATM 5912 C C4 . NAG P 5 . ? 11.835 90.385 50.222 1.00 43.43 ? 815 NAG A C4 1 HETATM 5913 C C5 . NAG P 5 . ? 12.145 88.946 49.794 1.00 43.13 ? 815 NAG A C5 1 HETATM 5914 C C6 . NAG P 5 . ? 12.688 88.814 48.376 1.00 45.99 ? 815 NAG A C6 1 HETATM 5915 C C7 . NAG P 5 . ? 12.228 89.643 54.943 1.00 49.10 ? 815 NAG A C7 1 HETATM 5916 C C8 . NAG P 5 . ? 13.564 90.361 54.876 1.00 48.60 ? 815 NAG A C8 1 HETATM 5917 N N2 . NAG P 5 . ? 11.635 89.235 53.812 1.00 44.77 ? 815 NAG A N2 1 HETATM 5918 O O3 . NAG P 5 . ? 11.035 91.522 52.265 1.00 41.04 ? 815 NAG A O3 1 HETATM 5919 O O4 . NAG P 5 . ? 10.913 90.925 49.288 1.00 44.77 ? 815 NAG A O4 1 HETATM 5920 O O5 . NAG P 5 . ? 13.143 88.418 50.642 1.00 39.49 ? 815 NAG A O5 1 HETATM 5921 O O6 . NAG P 5 . ? 13.742 89.743 48.229 1.00 50.85 ? 815 NAG A O6 1 HETATM 5922 O O7 . NAG P 5 . ? 11.696 89.410 56.030 1.00 52.86 ? 815 NAG A O7 1 HETATM 5923 C C1 . BMA Q 6 . ? 10.750 92.355 49.346 1.00 46.16 ? 816 BMA A C1 1 HETATM 5924 C C2 . BMA Q 6 . ? 10.562 92.865 47.917 1.00 47.01 ? 816 BMA A C2 1 HETATM 5925 C C3 . BMA Q 6 . ? 10.215 94.340 47.831 1.00 48.64 ? 816 BMA A C3 1 HETATM 5926 C C4 . BMA Q 6 . ? 9.121 94.720 48.862 1.00 48.71 ? 816 BMA A C4 1 HETATM 5927 C C5 . BMA Q 6 . ? 9.408 94.148 50.277 1.00 49.61 ? 816 BMA A C5 1 HETATM 5928 C C6 . BMA Q 6 . ? 8.320 94.386 51.338 1.00 50.64 ? 816 BMA A C6 1 HETATM 5929 O O2 . BMA Q 6 . ? 9.477 92.161 47.300 1.00 45.29 ? 816 BMA A O2 1 HETATM 5930 O O3 . BMA Q 6 . ? 9.800 94.486 46.460 1.00 48.16 ? 816 BMA A O3 1 HETATM 5931 O O4 . BMA Q 6 . ? 8.954 96.126 48.873 1.00 49.03 ? 816 BMA A O4 1 HETATM 5932 O O5 . BMA Q 6 . ? 9.640 92.728 50.177 1.00 46.54 ? 816 BMA A O5 1 HETATM 5933 O O6 . BMA Q 6 . ? 8.732 93.944 52.652 1.00 51.11 ? 816 BMA A O6 1 HETATM 5934 C C1 . MAN R 7 . ? 10.468 95.591 45.783 1.00 52.29 ? 817 MAN A C1 1 HETATM 5935 C C2 . MAN R 7 . ? 9.626 95.973 44.557 1.00 52.57 ? 817 MAN A C2 1 HETATM 5936 C C3 . MAN R 7 . ? 9.830 94.954 43.427 1.00 54.43 ? 817 MAN A C3 1 HETATM 5937 C C4 . MAN R 7 . ? 11.297 94.614 43.174 1.00 55.96 ? 817 MAN A C4 1 HETATM 5938 C C5 . MAN R 7 . ? 11.951 94.222 44.510 1.00 54.79 ? 817 MAN A C5 1 HETATM 5939 C C6 . MAN R 7 . ? 13.399 93.714 44.408 1.00 54.91 ? 817 MAN A C6 1 HETATM 5940 O O2 . MAN R 7 . ? 10.019 97.259 44.178 1.00 52.46 ? 817 MAN A O2 1 HETATM 5941 O O3 . MAN R 7 . ? 9.262 95.320 42.198 1.00 55.70 ? 817 MAN A O3 1 HETATM 5942 O O4 . MAN R 7 . ? 11.339 93.568 42.215 1.00 58.38 ? 817 MAN A O4 1 HETATM 5943 O O5 . MAN R 7 . ? 11.823 95.336 45.390 1.00 51.84 ? 817 MAN A O5 1 HETATM 5944 O O6 . MAN R 7 . ? 14.232 94.712 43.838 1.00 54.58 ? 817 MAN A O6 1 HETATM 5945 O O4 . 29C S 8 . ? 35.458 53.572 49.275 1.00 55.24 ? 818 29C A O4 1 HETATM 5946 C C4 . 29C S 8 . ? 34.688 54.284 48.417 1.00 55.27 ? 818 29C A C4 1 HETATM 5947 C C4A . 29C S 8 . ? 33.293 54.080 48.347 1.00 54.26 ? 818 29C A C4A 1 HETATM 5948 N N3 . 29C S 8 . ? 35.281 55.207 47.619 1.00 57.46 ? 818 29C A N3 1 HETATM 5949 C C8A . 29C S 8 . ? 32.579 54.863 47.422 1.00 55.19 ? 818 29C A C8A 1 HETATM 5950 N N5 . 29C S 8 . ? 32.636 53.182 49.135 1.00 51.64 ? 818 29C A N5 1 HETATM 5951 C C2 . 29C S 8 . ? 34.550 55.941 46.733 1.00 58.49 ? 818 29C A C2 1 HETATM 5952 N N8 . 29C S 8 . ? 31.251 54.740 47.296 1.00 53.74 ? 818 29C A N8 1 HETATM 5953 N N1 . 29C S 8 . ? 33.210 55.769 46.645 1.00 57.72 ? 818 29C A N1 1 HETATM 5954 C C6 . 29C S 8 . ? 31.306 53.072 48.995 1.00 50.67 ? 818 29C A C6 1 HETATM 5955 N N2 . 29C S 8 . ? 35.133 56.845 45.927 1.00 59.69 ? 818 29C A N2 1 HETATM 5956 C C7 . 29C S 8 . ? 30.630 53.878 48.067 1.00 52.20 ? 818 29C A C7 1 HETATM 5957 C C9 . 29C S 8 . ? 30.444 52.099 49.810 1.00 49.08 ? 818 29C A C9 1 HETATM 5958 N N10 . 29C S 8 . ? 29.026 52.326 49.383 1.00 49.21 ? 818 29C A N10 1 HETATM 5959 C CBP . 29C S 8 . ? 28.480 51.861 48.222 1.00 51.14 ? 818 29C A CBP 1 HETATM 5960 C CAN . 29C S 8 . ? 27.215 52.301 47.744 1.00 52.08 ? 818 29C A CAN 1 HETATM 5961 C CAO . 29C S 8 . ? 29.183 50.918 47.455 1.00 51.71 ? 818 29C A CAO 1 HETATM 5962 C CAP . 29C S 8 . ? 26.674 51.791 46.534 1.00 52.91 ? 818 29C A CAP 1 HETATM 5963 C CAQ . 29C S 8 . ? 28.651 50.422 46.260 1.00 53.53 ? 818 29C A CAQ 1 HETATM 5964 C CBQ . 29C S 8 . ? 27.402 50.843 45.769 1.00 54.32 ? 818 29C A CBQ 1 HETATM 5965 C CBN . 29C S 8 . ? 26.891 50.183 44.436 1.00 54.04 ? 818 29C A CBN 1 HETATM 5966 O OAH . 29C S 8 . ? 27.208 49.011 44.175 1.00 56.21 ? 818 29C A OAH 1 HETATM 5967 N NBG . 29C S 8 . ? 26.050 50.900 43.681 1.00 52.70 ? 818 29C A NBG 1 HETATM 5968 C CBX . 29C S 8 . ? 25.408 50.425 42.420 1.00 48.37 ? 818 29C A CBX 1 HETATM 5969 C CBK . 29C S 8 . ? 25.158 51.645 41.468 0.80 47.86 ? 818 29C A CBK 1 HETATM 5970 O OAE . 29C S 8 . ? 24.995 52.783 42.035 0.80 46.39 ? 818 29C A OAE 1 HETATM 5971 C CAX . 29C S 8 . ? 24.017 49.884 42.770 1.00 44.88 ? 818 29C A CAX 1 HETATM 5972 C CAU . 29C S 8 . ? 23.890 48.464 43.303 1.00 39.94 ? 818 29C A CAU 1 HETATM 5973 C CBM . 29C S 8 . ? 22.484 48.300 43.944 1.00 36.77 ? 818 29C A CBM 1 HETATM 5974 O OAG . 29C S 8 . ? 22.020 49.157 44.704 1.00 37.95 ? 818 29C A OAG 1 HETATM 5975 O OAL . 29C S 8 . ? 25.070 51.407 40.212 1.00 44.58 ? 818 29C A OAL 1 HETATM 5976 N NBF . 29C S 8 . ? 21.855 47.153 43.694 1.00 31.56 ? 818 29C A NBF 1 HETATM 5977 C CBW . 29C S 8 . ? 20.517 46.848 44.289 1.00 29.10 ? 818 29C A CBW 1 HETATM 5978 C CBJ . 29C S 8 . ? 20.724 46.496 45.772 1.00 31.69 ? 818 29C A CBJ 1 HETATM 5979 O OAK . 29C S 8 . ? 21.719 45.792 46.089 1.00 33.79 ? 818 29C A OAK 1 HETATM 5980 C CAW . 29C S 8 . ? 19.883 45.662 43.569 1.00 24.17 ? 818 29C A CAW 1 HETATM 5981 C CAT . 29C S 8 . ? 18.685 45.025 44.300 1.00 20.75 ? 818 29C A CAT 1 HETATM 5982 C CBL . 29C S 8 . ? 17.892 44.249 43.209 1.00 20.17 ? 818 29C A CBL 1 HETATM 5983 O OAF . 29C S 8 . ? 18.164 43.073 42.844 1.00 21.57 ? 818 29C A OAF 1 HETATM 5984 O OAD . 29C S 8 . ? 19.910 46.994 46.563 1.00 31.96 ? 818 29C A OAD 1 HETATM 5985 N N . 29C S 8 . ? 16.761 44.872 42.864 1.00 19.56 ? 818 29C A N 1 HETATM 5986 C CA . 29C S 8 . ? 15.972 44.355 41.711 1.00 19.07 ? 818 29C A CA 1 HETATM 5987 C C . 29C S 8 . ? 16.891 44.434 40.471 1.00 18.92 ? 818 29C A C 1 HETATM 5988 O O . 29C S 8 . ? 17.801 45.322 40.463 1.00 18.79 ? 818 29C A O 1 HETATM 5989 C CB . 29C S 8 . ? 14.671 45.162 41.343 1.00 18.47 ? 818 29C A CB 1 HETATM 5990 C CG . 29C S 8 . ? 15.004 46.649 41.054 1.00 20.08 ? 818 29C A CG 1 HETATM 5991 C CD . 29C S 8 . ? 13.763 47.431 40.538 1.00 22.58 ? 818 29C A CD 1 HETATM 5992 O OE2 . 29C S 8 . ? 12.896 46.780 39.857 1.00 23.94 ? 818 29C A OE2 1 HETATM 5993 O OE1 . 29C S 8 . ? 13.728 48.665 40.829 1.00 21.11 ? 818 29C A OE1 1 HETATM 5994 O OXT . 29C S 8 . ? 16.690 43.570 39.556 1.00 19.07 ? 818 29C A OXT 1 HETATM 5995 O O . HOH T 9 . ? 8.221 44.764 46.748 1.00 14.79 ? 901 HOH A O 1 HETATM 5996 O O . HOH T 9 . ? 6.902 58.247 38.003 1.00 16.23 ? 902 HOH A O 1 HETATM 5997 O O . HOH T 9 . ? 7.948 69.606 59.596 1.00 16.77 ? 903 HOH A O 1 HETATM 5998 O O . HOH T 9 . ? 13.639 44.765 50.207 1.00 20.42 ? 904 HOH A O 1 HETATM 5999 O O . HOH T 9 . ? 9.234 50.672 46.810 1.00 14.76 ? 905 HOH A O 1 HETATM 6000 O O . HOH T 9 . ? 0.893 50.490 40.270 1.00 16.83 ? 906 HOH A O 1 HETATM 6001 O O . HOH T 9 . ? 12.032 61.893 44.001 1.00 13.53 ? 907 HOH A O 1 HETATM 6002 O O . HOH T 9 . ? 13.497 29.902 40.420 1.00 17.40 ? 908 HOH A O 1 HETATM 6003 O O . HOH T 9 . ? 14.996 41.777 39.088 1.00 14.84 ? 909 HOH A O 1 HETATM 6004 O O . HOH T 9 . ? 9.655 60.875 58.124 1.00 14.41 ? 910 HOH A O 1 HETATM 6005 O O . HOH T 9 . ? 10.862 36.805 42.729 1.00 17.02 ? 911 HOH A O 1 HETATM 6006 O O . HOH T 9 . ? -5.405 59.777 60.147 1.00 17.06 ? 912 HOH A O 1 HETATM 6007 O O . HOH T 9 . ? 13.635 27.042 52.026 1.00 20.45 ? 913 HOH A O 1 HETATM 6008 O O . HOH T 9 . ? 7.427 71.774 45.655 1.00 19.98 ? 914 HOH A O 1 HETATM 6009 O O . HOH T 9 . ? 5.728 68.875 55.769 1.00 18.03 ? 915 HOH A O 1 HETATM 6010 O O . HOH T 9 . ? 16.780 37.156 44.293 1.00 16.13 ? 916 HOH A O 1 HETATM 6011 O O . HOH T 9 . ? -3.681 62.231 54.367 1.00 17.43 ? 917 HOH A O 1 HETATM 6012 O O . HOH T 9 . ? 29.441 36.140 44.758 1.00 20.54 ? 918 HOH A O 1 HETATM 6013 O O . HOH T 9 . ? 6.442 75.982 61.341 1.00 15.67 ? 919 HOH A O 1 HETATM 6014 O O . HOH T 9 . ? -3.518 60.204 62.231 1.00 17.58 ? 920 HOH A O 1 HETATM 6015 O O . HOH T 9 . ? 19.289 47.739 55.048 1.00 19.33 ? 921 HOH A O 1 HETATM 6016 O O . HOH T 9 . ? 3.991 70.456 64.738 1.00 19.02 ? 922 HOH A O 1 HETATM 6017 O O . HOH T 9 . ? 19.003 62.153 36.732 1.00 19.31 ? 923 HOH A O 1 HETATM 6018 O O . HOH T 9 . ? -7.053 51.655 51.832 1.00 19.41 ? 924 HOH A O 1 HETATM 6019 O O . HOH T 9 . ? 17.817 40.513 32.639 1.00 19.88 ? 925 HOH A O 1 HETATM 6020 O O . HOH T 9 . ? 20.018 61.458 63.274 1.00 21.10 ? 926 HOH A O 1 HETATM 6021 O O . HOH T 9 . ? -4.421 59.572 57.569 1.00 18.83 ? 927 HOH A O 1 HETATM 6022 O O . HOH T 9 . ? 3.557 71.973 43.895 1.00 17.28 ? 928 HOH A O 1 HETATM 6023 O O . HOH T 9 . ? 29.857 42.635 32.508 1.00 22.65 ? 929 HOH A O 1 HETATM 6024 O O . HOH T 9 . ? 23.785 46.031 35.045 1.00 20.18 ? 930 HOH A O 1 HETATM 6025 O O . HOH T 9 . ? 14.638 36.811 28.381 1.00 21.39 ? 931 HOH A O 1 HETATM 6026 O O . HOH T 9 . ? 18.484 33.645 43.891 1.00 17.26 ? 932 HOH A O 1 HETATM 6027 O O . HOH T 9 . ? 28.903 33.827 33.126 1.00 24.74 ? 933 HOH A O 1 HETATM 6028 O O . HOH T 9 . ? 5.993 75.404 54.579 1.00 19.26 ? 934 HOH A O 1 HETATM 6029 O O . HOH T 9 . ? 3.614 62.252 50.909 1.00 19.23 ? 935 HOH A O 1 HETATM 6030 O O . HOH T 9 . ? 14.547 32.122 48.476 1.00 18.66 ? 936 HOH A O 1 HETATM 6031 O O . HOH T 9 . ? 4.500 35.005 45.769 1.00 17.85 ? 937 HOH A O 1 HETATM 6032 O O . HOH T 9 . ? 0.201 56.943 46.118 1.00 19.20 ? 938 HOH A O 1 HETATM 6033 O O . HOH T 9 . ? -0.128 65.462 66.475 0.50 19.52 ? 939 HOH A O 1 HETATM 6034 O O . HOH T 9 . ? -0.423 43.490 61.118 1.00 24.57 ? 940 HOH A O 1 HETATM 6035 O O . HOH T 9 . ? 14.415 38.067 35.244 1.00 18.10 ? 941 HOH A O 1 HETATM 6036 O O . HOH T 9 . ? 22.144 88.016 32.711 1.00 21.92 ? 942 HOH A O 1 HETATM 6037 O O . HOH T 9 . ? 23.226 67.671 34.641 1.00 22.63 ? 943 HOH A O 1 HETATM 6038 O O . HOH T 9 . ? 23.173 68.703 43.384 1.00 19.63 ? 944 HOH A O 1 HETATM 6039 O O . HOH T 9 . ? 20.614 45.703 36.770 1.00 19.36 ? 945 HOH A O 1 HETATM 6040 O O . HOH T 9 . ? 24.406 37.199 32.871 1.00 21.37 ? 946 HOH A O 1 HETATM 6041 O O . HOH T 9 . ? 16.165 55.659 35.879 1.00 15.96 ? 947 HOH A O 1 HETATM 6042 O O . HOH T 9 . ? 25.627 37.120 38.442 1.00 22.79 ? 948 HOH A O 1 HETATM 6043 O O . HOH T 9 . ? 9.493 29.218 43.429 1.00 18.11 ? 949 HOH A O 1 HETATM 6044 O O . HOH T 9 . ? 27.399 31.097 28.990 1.00 20.19 ? 950 HOH A O 1 HETATM 6045 O O . HOH T 9 . ? 20.648 27.592 49.094 1.00 20.26 ? 951 HOH A O 1 HETATM 6046 O O . HOH T 9 . ? 10.014 30.996 27.129 1.00 23.22 ? 952 HOH A O 1 HETATM 6047 O O . HOH T 9 . ? 29.131 60.559 57.917 1.00 26.48 ? 953 HOH A O 1 HETATM 6048 O O . HOH T 9 . ? 16.889 61.990 38.686 1.00 17.87 ? 954 HOH A O 1 HETATM 6049 O O . HOH T 9 . ? 19.312 36.128 43.690 1.00 18.74 ? 955 HOH A O 1 HETATM 6050 O O . HOH T 9 . ? 20.134 31.375 43.885 1.00 19.29 ? 956 HOH A O 1 HETATM 6051 O O . HOH T 9 . ? 7.973 50.361 41.301 1.00 16.02 ? 957 HOH A O 1 HETATM 6052 O O . HOH T 9 . ? -2.688 44.211 38.106 1.00 18.60 ? 958 HOH A O 1 HETATM 6053 O O . HOH T 9 . ? 6.609 60.839 67.510 1.00 21.00 ? 959 HOH A O 1 HETATM 6054 O O . HOH T 9 . ? 5.142 64.653 37.486 1.00 14.86 ? 960 HOH A O 1 HETATM 6055 O O . HOH T 9 . ? 14.754 80.860 38.533 1.00 22.57 ? 961 HOH A O 1 HETATM 6056 O O . HOH T 9 . ? 6.780 54.941 44.261 1.00 16.87 ? 962 HOH A O 1 HETATM 6057 O O . HOH T 9 . ? 13.927 40.862 53.890 1.00 20.24 ? 963 HOH A O 1 HETATM 6058 O O . HOH T 9 . ? 11.041 27.471 54.727 1.00 22.08 ? 964 HOH A O 1 HETATM 6059 O O . HOH T 9 . ? 22.935 44.403 36.849 1.00 17.68 ? 965 HOH A O 1 HETATM 6060 O O . HOH T 9 . ? 13.887 67.957 35.151 1.00 20.67 ? 966 HOH A O 1 HETATM 6061 O O . HOH T 9 . ? 4.404 66.949 51.844 1.00 19.46 ? 967 HOH A O 1 HETATM 6062 O O . HOH T 9 . ? 3.991 68.535 49.639 1.00 18.07 ? 968 HOH A O 1 HETATM 6063 O O . HOH T 9 . ? -4.552 55.270 52.223 1.00 20.91 ? 969 HOH A O 1 HETATM 6064 O O . HOH T 9 . ? 1.144 59.260 46.910 1.00 25.78 ? 970 HOH A O 1 HETATM 6065 O O . HOH T 9 . ? 2.551 33.202 45.717 1.00 19.90 ? 971 HOH A O 1 HETATM 6066 O O . HOH T 9 . ? -3.975 57.605 46.747 1.00 26.29 ? 972 HOH A O 1 HETATM 6067 O O . HOH T 9 . ? 11.105 63.436 58.641 1.00 22.53 ? 973 HOH A O 1 HETATM 6068 O O . HOH T 9 . ? 28.587 53.802 53.583 1.00 20.17 ? 974 HOH A O 1 HETATM 6069 O O . HOH T 9 . ? 13.759 71.453 40.920 1.00 20.77 ? 975 HOH A O 1 HETATM 6070 O O . HOH T 9 . ? 18.857 27.768 35.364 1.00 21.66 ? 976 HOH A O 1 HETATM 6071 O O . HOH T 9 . ? 13.392 77.750 64.036 1.00 24.76 ? 977 HOH A O 1 HETATM 6072 O O . HOH T 9 . ? 34.534 41.773 50.471 1.00 28.07 ? 978 HOH A O 1 HETATM 6073 O O . HOH T 9 . ? 26.375 38.876 36.604 1.00 22.47 ? 979 HOH A O 1 HETATM 6074 O O . HOH T 9 . ? -2.546 59.378 48.940 1.00 20.94 ? 980 HOH A O 1 HETATM 6075 O O . HOH T 9 . ? 8.853 74.686 67.059 1.00 20.66 ? 981 HOH A O 1 HETATM 6076 O O . HOH T 9 . ? 24.261 31.679 29.000 1.00 25.23 ? 982 HOH A O 1 HETATM 6077 O O . HOH T 9 . ? 5.580 62.776 65.410 1.00 24.89 ? 983 HOH A O 1 HETATM 6078 O O . HOH T 9 . ? 14.227 31.826 29.874 1.00 23.20 ? 984 HOH A O 1 HETATM 6079 O O . HOH T 9 . ? 12.022 35.028 54.070 1.00 19.23 ? 985 HOH A O 1 HETATM 6080 O O . HOH T 9 . ? 10.486 37.264 54.853 1.00 27.24 ? 986 HOH A O 1 HETATM 6081 O O . HOH T 9 . ? 21.144 63.523 61.391 1.00 20.39 ? 987 HOH A O 1 HETATM 6082 O O . HOH T 9 . ? 3.503 27.785 41.773 1.00 31.01 ? 988 HOH A O 1 HETATM 6083 O O . HOH T 9 . ? 19.315 60.115 50.540 1.00 23.24 ? 989 HOH A O 1 HETATM 6084 O O . HOH T 9 . ? 20.827 53.291 47.740 1.00 25.65 ? 990 HOH A O 1 HETATM 6085 O O . HOH T 9 . ? 31.290 40.090 46.817 1.00 21.26 ? 991 HOH A O 1 HETATM 6086 O O . HOH T 9 . ? 5.527 78.052 54.851 1.00 20.32 ? 992 HOH A O 1 HETATM 6087 O O . HOH T 9 . ? 32.185 35.136 59.591 1.00 25.84 ? 993 HOH A O 1 HETATM 6088 O O . HOH T 9 . ? 21.893 61.627 37.090 1.00 22.75 ? 994 HOH A O 1 HETATM 6089 O O . HOH T 9 . ? 16.364 72.119 30.189 1.00 20.17 ? 995 HOH A O 1 HETATM 6090 O O . HOH T 9 . ? 14.771 59.110 75.009 1.00 25.68 ? 996 HOH A O 1 HETATM 6091 O O . HOH T 9 . ? 29.446 70.214 46.310 1.00 25.80 ? 997 HOH A O 1 HETATM 6092 O O . HOH T 9 . ? -2.228 55.636 46.603 1.00 22.37 ? 998 HOH A O 1 HETATM 6093 O O . HOH T 9 . ? 23.852 40.538 69.815 1.00 27.59 ? 999 HOH A O 1 HETATM 6094 O O . HOH T 9 . ? 5.552 62.783 70.818 1.00 19.41 ? 1000 HOH A O 1 HETATM 6095 O O . HOH T 9 . ? 16.816 68.252 64.633 1.00 25.79 ? 1001 HOH A O 1 HETATM 6096 O O . HOH T 9 . ? 24.964 32.754 68.199 1.00 31.52 ? 1002 HOH A O 1 HETATM 6097 O O . HOH T 9 . ? -6.308 58.712 38.454 1.00 22.72 ? 1003 HOH A O 1 HETATM 6098 O O . HOH T 9 . ? 15.041 61.822 73.543 1.00 24.12 ? 1004 HOH A O 1 HETATM 6099 O O . HOH T 9 . ? 0.262 31.469 58.478 1.00 25.33 ? 1005 HOH A O 1 HETATM 6100 O O . HOH T 9 . ? 18.187 55.461 30.889 1.00 26.92 ? 1006 HOH A O 1 HETATM 6101 O O . HOH T 9 . ? 8.875 68.994 41.203 1.00 19.28 ? 1007 HOH A O 1 HETATM 6102 O O . HOH T 9 . ? 12.036 37.009 29.042 1.00 20.29 ? 1008 HOH A O 1 HETATM 6103 O O . HOH T 9 . ? 0.361 33.462 43.695 1.00 24.57 ? 1009 HOH A O 1 HETATM 6104 O O . HOH T 9 . ? 33.950 47.807 59.546 1.00 27.65 ? 1010 HOH A O 1 HETATM 6105 O O . HOH T 9 . ? 17.288 81.581 37.650 1.00 21.54 ? 1011 HOH A O 1 HETATM 6106 O O . HOH T 9 . ? 15.075 68.933 41.973 1.00 27.81 ? 1012 HOH A O 1 HETATM 6107 O O . HOH T 9 . ? 16.384 26.343 35.003 1.00 26.20 ? 1013 HOH A O 1 HETATM 6108 O O . HOH T 9 . ? 23.146 55.218 31.640 1.00 24.90 ? 1014 HOH A O 1 HETATM 6109 O O . HOH T 9 . ? 17.756 82.512 41.558 1.00 25.99 ? 1015 HOH A O 1 HETATM 6110 O O . HOH T 9 . ? 24.015 74.979 54.844 1.00 26.26 ? 1016 HOH A O 1 HETATM 6111 O O . HOH T 9 . ? 23.097 67.411 40.941 1.00 25.62 ? 1017 HOH A O 1 HETATM 6112 O O . HOH T 9 . ? 8.358 51.660 43.672 1.00 21.47 ? 1018 HOH A O 1 HETATM 6113 O O . HOH T 9 . ? 29.894 27.128 34.010 1.00 25.62 ? 1019 HOH A O 1 HETATM 6114 O O . HOH T 9 . ? 6.096 38.735 26.823 1.00 28.39 ? 1020 HOH A O 1 HETATM 6115 O O . HOH T 9 . ? 18.899 69.051 66.184 1.00 28.19 ? 1021 HOH A O 1 HETATM 6116 O O . HOH T 9 . ? 21.880 74.455 60.977 1.00 28.29 ? 1022 HOH A O 1 HETATM 6117 O O . HOH T 9 . ? -2.273 34.063 40.991 1.00 24.72 ? 1023 HOH A O 1 HETATM 6118 O O . HOH T 9 . ? 13.562 82.770 56.146 1.00 27.90 ? 1024 HOH A O 1 HETATM 6119 O O . HOH T 9 . ? 25.795 35.553 68.533 1.00 28.50 ? 1025 HOH A O 1 HETATM 6120 O O . HOH T 9 . ? 23.887 73.307 59.646 1.00 33.06 ? 1026 HOH A O 1 HETATM 6121 O O . HOH T 9 . ? -1.305 61.615 62.687 1.00 27.45 ? 1027 HOH A O 1 HETATM 6122 O O . HOH T 9 . ? 9.960 36.091 70.312 1.00 30.20 ? 1028 HOH A O 1 HETATM 6123 O O . HOH T 9 . ? 14.013 57.577 35.557 1.00 21.55 ? 1029 HOH A O 1 HETATM 6124 O O . HOH T 9 . ? 13.474 29.423 28.881 1.00 19.74 ? 1030 HOH A O 1 HETATM 6125 O O . HOH T 9 . ? 10.828 29.046 40.898 1.00 22.98 ? 1031 HOH A O 1 HETATM 6126 O O . HOH T 9 . ? 11.676 40.980 55.805 1.00 22.53 ? 1032 HOH A O 1 HETATM 6127 O O . HOH T 9 . ? 19.219 63.602 32.357 1.00 29.81 ? 1033 HOH A O 1 HETATM 6128 O O . HOH T 9 . ? 12.584 53.401 36.236 1.00 21.01 ? 1034 HOH A O 1 HETATM 6129 O O . HOH T 9 . ? 23.496 56.746 45.238 0.90 38.21 ? 1035 HOH A O 1 HETATM 6130 O O . HOH T 9 . ? 21.972 61.309 52.041 1.00 26.50 ? 1036 HOH A O 1 HETATM 6131 O O . HOH T 9 . ? 25.682 27.245 24.667 1.00 29.20 ? 1037 HOH A O 1 HETATM 6132 O O . HOH T 9 . ? 25.370 55.976 37.790 1.00 26.24 ? 1038 HOH A O 1 HETATM 6133 O O . HOH T 9 . ? 20.065 31.384 26.574 1.00 27.06 ? 1039 HOH A O 1 HETATM 6134 O O . HOH T 9 . ? 30.891 52.550 53.560 1.00 23.96 ? 1040 HOH A O 1 HETATM 6135 O O . HOH T 9 . ? 6.624 76.322 67.711 1.00 27.71 ? 1041 HOH A O 1 HETATM 6136 O O . HOH T 9 . ? 10.580 55.689 75.687 1.00 30.51 ? 1042 HOH A O 1 HETATM 6137 O O . HOH T 9 . ? 21.207 32.458 29.003 1.00 24.61 ? 1043 HOH A O 1 HETATM 6138 O O . HOH T 9 . ? 25.321 70.544 31.492 1.00 24.77 ? 1044 HOH A O 1 HETATM 6139 O O . HOH T 9 . ? 19.102 69.461 28.817 1.00 25.51 ? 1045 HOH A O 1 HETATM 6140 O O . HOH T 9 . ? 23.554 78.996 50.981 1.00 24.45 ? 1046 HOH A O 1 HETATM 6141 O O . HOH T 9 . ? -9.649 46.142 34.685 1.00 34.57 ? 1047 HOH A O 1 HETATM 6142 O O . HOH T 9 . ? 29.138 40.351 65.226 1.00 27.89 ? 1048 HOH A O 1 HETATM 6143 O O . HOH T 9 . ? 11.605 27.741 29.620 1.00 33.44 ? 1049 HOH A O 1 HETATM 6144 O O . HOH T 9 . ? 25.288 63.419 50.435 1.00 24.75 ? 1050 HOH A O 1 HETATM 6145 O O . HOH T 9 . ? 16.074 29.002 28.492 1.00 27.20 ? 1051 HOH A O 1 HETATM 6146 O O . HOH T 9 . ? 13.859 79.909 68.293 1.00 31.30 ? 1052 HOH A O 1 HETATM 6147 O O . HOH T 9 . ? 4.848 31.688 30.743 1.00 33.81 ? 1053 HOH A O 1 HETATM 6148 O O . HOH T 9 . ? 14.439 81.358 40.923 1.00 33.72 ? 1054 HOH A O 1 HETATM 6149 O O . HOH T 9 . ? 10.269 80.887 63.974 1.00 30.71 ? 1055 HOH A O 1 HETATM 6150 O O . HOH T 9 . ? 4.115 63.419 73.294 1.00 29.06 ? 1056 HOH A O 1 HETATM 6151 O O . HOH T 9 . ? -10.539 48.733 48.903 1.00 26.78 ? 1057 HOH A O 1 HETATM 6152 O O . HOH T 9 . ? 21.785 83.988 47.496 1.00 28.45 ? 1058 HOH A O 1 HETATM 6153 O O . HOH T 9 . ? 18.090 21.292 39.152 1.00 42.46 ? 1059 HOH A O 1 HETATM 6154 O O . HOH T 9 . ? 27.337 53.970 51.115 1.00 24.19 ? 1060 HOH A O 1 HETATM 6155 O O . HOH T 9 . ? 7.366 38.629 29.701 1.00 27.74 ? 1061 HOH A O 1 HETATM 6156 O O . HOH T 9 . ? 38.143 34.473 26.715 1.00 31.66 ? 1062 HOH A O 1 HETATM 6157 O O . HOH T 9 . ? 4.739 62.050 75.566 1.00 24.50 ? 1063 HOH A O 1 HETATM 6158 O O . HOH T 9 . ? -1.779 32.367 45.035 1.00 31.57 ? 1064 HOH A O 1 HETATM 6159 O O . HOH T 9 . ? -10.152 43.833 47.412 1.00 33.40 ? 1065 HOH A O 1 HETATM 6160 O O A HOH T 9 . ? 29.503 54.459 34.877 0.80 23.83 ? 1066 HOH A O 1 HETATM 6161 O O B HOH T 9 . ? 28.709 56.577 34.236 0.20 12.81 ? 1066 HOH A O 1 HETATM 6162 O O . HOH T 9 . ? 11.737 47.656 37.702 1.00 19.48 ? 1067 HOH A O 1 HETATM 6163 O O . HOH T 9 . ? -0.677 58.258 43.686 1.00 19.80 ? 1068 HOH A O 1 HETATM 6164 O O . HOH T 9 . ? 22.613 58.400 24.715 1.00 35.56 ? 1069 HOH A O 1 HETATM 6165 O O . HOH T 9 . ? -3.014 38.657 63.509 1.00 30.74 ? 1070 HOH A O 1 HETATM 6166 O O . HOH T 9 . ? 11.560 38.511 56.956 1.00 29.55 ? 1071 HOH A O 1 HETATM 6167 O O . HOH T 9 . ? 25.630 66.979 30.491 1.00 29.12 ? 1072 HOH A O 1 HETATM 6168 O O . HOH T 9 . ? 16.640 69.107 21.029 1.00 50.16 ? 1073 HOH A O 1 HETATM 6169 O O . HOH T 9 . ? 11.961 63.759 35.840 1.00 26.43 ? 1074 HOH A O 1 HETATM 6170 O O . HOH T 9 . ? 25.176 65.885 40.490 0.50 21.85 ? 1075 HOH A O 1 HETATM 6171 O O A HOH T 9 . ? 31.685 55.244 26.523 0.70 26.48 ? 1076 HOH A O 1 HETATM 6172 O O B HOH T 9 . ? 33.604 54.425 28.244 0.30 16.50 ? 1076 HOH A O 1 HETATM 6173 O O . HOH T 9 . ? 17.930 30.936 29.411 1.00 26.15 ? 1077 HOH A O 1 HETATM 6174 O O . HOH T 9 . ? 28.937 26.094 36.385 1.00 27.99 ? 1078 HOH A O 1 HETATM 6175 O O . HOH T 9 . ? 16.652 79.646 21.449 1.00 40.42 ? 1079 HOH A O 1 HETATM 6176 O O . HOH T 9 . ? 19.842 25.737 37.079 1.00 25.78 ? 1080 HOH A O 1 HETATM 6177 O O . HOH T 9 . ? 27.963 45.207 69.400 1.00 26.67 ? 1081 HOH A O 1 HETATM 6178 O O . HOH T 9 . ? 17.816 52.237 75.504 1.00 33.47 ? 1082 HOH A O 1 HETATM 6179 O O . HOH T 9 . ? 0.379 33.681 36.902 1.00 43.85 ? 1083 HOH A O 1 HETATM 6180 O O . HOH T 9 . ? 25.666 25.542 20.547 1.00 35.32 ? 1084 HOH A O 1 HETATM 6181 O O . HOH T 9 . ? 20.464 30.210 30.194 1.00 26.22 ? 1085 HOH A O 1 HETATM 6182 O O . HOH T 9 . ? 12.923 69.395 33.084 1.00 28.23 ? 1086 HOH A O 1 HETATM 6183 O O . HOH T 9 . ? 24.523 29.461 30.712 1.00 25.70 ? 1087 HOH A O 1 HETATM 6184 O O . HOH T 9 . ? 24.192 82.279 42.574 1.00 31.89 ? 1088 HOH A O 1 HETATM 6185 O O . HOH T 9 . ? 29.292 79.081 27.835 1.00 31.49 ? 1089 HOH A O 1 HETATM 6186 O O . HOH T 9 . ? 10.455 27.217 51.975 1.00 27.60 ? 1090 HOH A O 1 HETATM 6187 O O . HOH T 9 . ? 4.995 40.039 23.692 1.00 34.63 ? 1091 HOH A O 1 HETATM 6188 O O . HOH T 9 . ? 36.046 42.911 58.037 1.00 31.81 ? 1092 HOH A O 1 HETATM 6189 O O . HOH T 9 . ? 36.759 52.147 69.187 1.00 30.61 ? 1093 HOH A O 1 HETATM 6190 O O . HOH T 9 . ? 9.978 69.807 39.025 1.00 22.25 ? 1094 HOH A O 1 HETATM 6191 O O . HOH T 9 . ? 22.775 65.278 66.505 1.00 30.21 ? 1095 HOH A O 1 HETATM 6192 O O . HOH T 9 . ? 27.149 56.883 70.928 1.00 32.06 ? 1096 HOH A O 1 HETATM 6193 O O . HOH T 9 . ? 6.981 75.761 38.134 1.00 24.96 ? 1097 HOH A O 1 HETATM 6194 O O . HOH T 9 . ? 39.726 43.813 58.930 1.00 33.97 ? 1098 HOH A O 1 HETATM 6195 O O . HOH T 9 . ? 28.123 71.857 53.061 1.00 38.10 ? 1099 HOH A O 1 HETATM 6196 O O . HOH T 9 . ? 4.837 31.497 25.046 1.00 38.04 ? 1100 HOH A O 1 HETATM 6197 O O . HOH T 9 . ? 26.303 60.164 30.979 1.00 37.02 ? 1101 HOH A O 1 HETATM 6198 O O . HOH T 9 . ? -1.856 46.083 56.101 1.00 34.03 ? 1102 HOH A O 1 HETATM 6199 O O . HOH T 9 . ? 1.601 31.062 65.288 1.00 35.53 ? 1103 HOH A O 1 HETATM 6200 O O . HOH T 9 . ? 21.463 25.190 24.104 1.00 33.92 ? 1104 HOH A O 1 HETATM 6201 O O . HOH T 9 . ? 23.961 61.327 35.204 1.00 28.15 ? 1105 HOH A O 1 HETATM 6202 O O . HOH T 9 . ? 11.166 76.561 28.942 1.00 30.62 ? 1106 HOH A O 1 HETATM 6203 O O . HOH T 9 . ? 26.301 23.339 46.003 1.00 32.33 ? 1107 HOH A O 1 HETATM 6204 O O . HOH T 9 . ? -4.055 37.569 57.063 1.00 37.66 ? 1108 HOH A O 1 HETATM 6205 O O . HOH T 9 . ? 16.064 67.574 73.046 1.00 36.44 ? 1109 HOH A O 1 HETATM 6206 O O . HOH T 9 . ? 11.492 48.833 29.896 1.00 22.25 ? 1110 HOH A O 1 HETATM 6207 O O . HOH T 9 . ? 5.436 65.997 34.211 1.00 39.03 ? 1111 HOH A O 1 HETATM 6208 O O . HOH T 9 . ? -2.969 38.009 33.015 1.00 28.13 ? 1112 HOH A O 1 HETATM 6209 O O . HOH T 9 . ? 24.294 77.824 53.452 1.00 37.74 ? 1113 HOH A O 1 HETATM 6210 O O . HOH T 9 . ? 20.892 74.389 24.098 1.00 39.72 ? 1114 HOH A O 1 HETATM 6211 O O . HOH T 9 . ? 10.131 51.721 40.391 1.00 19.73 ? 1115 HOH A O 1 HETATM 6212 O O . HOH T 9 . ? 30.827 84.158 28.822 1.00 34.08 ? 1116 HOH A O 1 HETATM 6213 O O . HOH T 9 . ? 0.483 63.189 48.572 1.00 38.97 ? 1117 HOH A O 1 HETATM 6214 O O . HOH T 9 . ? 26.481 66.166 26.487 1.00 33.85 ? 1118 HOH A O 1 HETATM 6215 O O . HOH T 9 . ? -4.303 53.340 37.581 1.00 32.61 ? 1119 HOH A O 1 HETATM 6216 O O . HOH T 9 . ? 28.491 44.443 65.939 1.00 35.98 ? 1120 HOH A O 1 HETATM 6217 O O . HOH T 9 . ? 8.594 82.474 52.482 1.00 29.58 ? 1121 HOH A O 1 HETATM 6218 O O . HOH T 9 . ? 32.890 29.972 24.774 1.00 39.73 ? 1122 HOH A O 1 HETATM 6219 O O . HOH T 9 . ? 14.924 52.637 35.131 1.00 26.82 ? 1123 HOH A O 1 HETATM 6220 O O . HOH T 9 . ? 15.078 24.703 58.825 1.00 36.45 ? 1124 HOH A O 1 HETATM 6221 O O . HOH T 9 . ? 4.359 43.749 76.420 1.00 36.48 ? 1125 HOH A O 1 HETATM 6222 O O . HOH T 9 . ? 8.985 52.062 75.679 1.00 35.26 ? 1126 HOH A O 1 HETATM 6223 O O . HOH T 9 . ? 18.817 66.067 28.312 1.00 35.15 ? 1127 HOH A O 1 HETATM 6224 O O . HOH T 9 . ? 17.819 32.268 70.856 1.00 36.51 ? 1128 HOH A O 1 HETATM 6225 O O . HOH T 9 . ? 13.778 50.331 19.295 1.00 33.52 ? 1129 HOH A O 1 HETATM 6226 O O . HOH T 9 . ? 17.720 65.309 30.796 1.00 30.74 ? 1130 HOH A O 1 HETATM 6227 O O . HOH T 9 . ? 25.825 24.978 57.888 1.00 37.12 ? 1131 HOH A O 1 HETATM 6228 O O . HOH T 9 . ? 29.410 69.862 39.911 1.00 37.85 ? 1132 HOH A O 1 HETATM 6229 O O . HOH T 9 . ? 3.649 27.410 55.030 1.00 30.51 ? 1133 HOH A O 1 HETATM 6230 O O . HOH T 9 . ? 14.737 81.549 28.856 1.00 39.05 ? 1134 HOH A O 1 HETATM 6231 O O . HOH T 9 . ? -4.670 53.894 34.944 1.00 30.09 ? 1135 HOH A O 1 HETATM 6232 O O . HOH T 9 . ? 21.637 75.097 67.442 1.00 35.88 ? 1136 HOH A O 1 HETATM 6233 O O . HOH T 9 . ? 21.520 88.476 44.466 1.00 30.51 ? 1137 HOH A O 1 HETATM 6234 O O . HOH T 9 . ? -4.305 37.326 51.754 1.00 43.20 ? 1138 HOH A O 1 HETATM 6235 O O . HOH T 9 . ? 13.885 65.231 36.192 1.00 35.62 ? 1139 HOH A O 1 HETATM 6236 O O . HOH T 9 . ? 33.717 40.231 47.876 1.00 40.32 ? 1140 HOH A O 1 HETATM 6237 O O . HOH T 9 . ? 11.966 50.050 36.738 1.00 17.31 ? 1141 HOH A O 1 HETATM 6238 O O . HOH T 9 . ? 31.089 31.733 17.477 0.80 27.65 ? 1142 HOH A O 1 HETATM 6239 O O . HOH T 9 . ? 30.281 59.577 25.486 0.50 22.61 ? 1143 HOH A O 1 HETATM 6240 O O . HOH T 9 . ? 12.148 43.363 17.659 1.00 32.22 ? 1144 HOH A O 1 HETATM 6241 O O . HOH T 9 . ? 26.686 69.277 29.481 1.00 32.39 ? 1145 HOH A O 1 HETATM 6242 O O . HOH T 9 . ? -5.046 42.280 50.915 1.00 38.07 ? 1146 HOH A O 1 HETATM 6243 O O . HOH T 9 . ? 36.601 43.357 49.574 1.00 39.36 ? 1147 HOH A O 1 HETATM 6244 O O . HOH T 9 . ? -3.443 47.087 53.612 1.00 37.63 ? 1148 HOH A O 1 HETATM 6245 O O . HOH T 9 . ? -6.295 42.667 47.185 0.75 40.57 ? 1149 HOH A O 1 HETATM 6246 O O . HOH T 9 . ? -0.827 32.486 60.977 1.00 45.78 ? 1150 HOH A O 1 HETATM 6247 O O . HOH T 9 . ? 16.206 79.348 69.709 1.00 45.38 ? 1151 HOH A O 1 HETATM 6248 O O . HOH T 9 . ? 19.760 55.843 23.420 1.00 33.03 ? 1152 HOH A O 1 HETATM 6249 O O . HOH T 9 . ? 32.421 42.842 20.306 1.00 37.43 ? 1153 HOH A O 1 HETATM 6250 O O . HOH T 9 . ? 21.427 24.037 51.473 1.00 37.26 ? 1154 HOH A O 1 HETATM 6251 O O . HOH T 9 . ? 27.206 20.201 40.054 1.00 28.71 ? 1155 HOH A O 1 HETATM 6252 O O . HOH T 9 . ? 5.557 81.722 54.470 1.00 34.30 ? 1156 HOH A O 1 HETATM 6253 O O . HOH T 9 . ? 8.135 29.375 33.927 0.80 33.10 ? 1157 HOH A O 1 HETATM 6254 O O . HOH T 9 . ? -1.239 51.403 73.006 0.50 13.56 ? 1158 HOH A O 1 HETATM 6255 O O . HOH T 9 . ? 8.955 56.605 44.276 1.00 22.79 ? 1159 HOH A O 1 HETATM 6256 O O . HOH T 9 . ? 23.004 75.722 25.981 1.00 33.95 ? 1160 HOH A O 1 HETATM 6257 O O . HOH T 9 . ? 6.205 68.213 37.463 1.00 36.23 ? 1161 HOH A O 1 HETATM 6258 O O . HOH T 9 . ? 38.811 55.243 62.696 1.00 39.72 ? 1162 HOH A O 1 HETATM 6259 O O . HOH T 9 . ? 12.954 71.705 80.528 1.00 33.64 ? 1163 HOH A O 1 HETATM 6260 O O . HOH T 9 . ? 11.742 80.894 61.730 1.00 32.62 ? 1164 HOH A O 1 HETATM 6261 O O . HOH T 9 . ? 1.372 37.086 69.141 1.00 37.42 ? 1165 HOH A O 1 HETATM 6262 O O . HOH T 9 . ? 12.873 32.961 71.260 1.00 32.41 ? 1166 HOH A O 1 HETATM 6263 O O . HOH T 9 . ? 18.758 40.522 76.352 1.00 36.26 ? 1167 HOH A O 1 HETATM 6264 O O . HOH T 9 . ? 20.313 45.813 79.241 1.00 45.16 ? 1168 HOH A O 1 HETATM 6265 O O . HOH T 9 . ? 5.880 56.224 36.320 1.00 24.72 ? 1169 HOH A O 1 HETATM 6266 O O . HOH T 9 . ? 23.359 60.097 40.214 1.00 29.23 ? 1170 HOH A O 1 HETATM 6267 O O . HOH T 9 . ? 30.707 71.445 43.905 1.00 38.58 ? 1171 HOH A O 1 HETATM 6268 O O . HOH T 9 . ? 8.610 74.829 75.948 1.00 33.90 ? 1172 HOH A O 1 HETATM 6269 O O . HOH T 9 . ? 2.795 38.394 27.505 1.00 36.77 ? 1173 HOH A O 1 HETATM 6270 O O . HOH T 9 . ? 38.510 43.079 55.944 1.00 35.41 ? 1174 HOH A O 1 HETATM 6271 O O . HOH T 9 . ? 25.249 86.068 42.986 1.00 28.11 ? 1175 HOH A O 1 HETATM 6272 O O . HOH T 9 . ? 11.887 56.297 31.789 1.00 36.72 ? 1176 HOH A O 1 HETATM 6273 O O . HOH T 9 . ? 21.942 80.746 23.282 1.00 36.91 ? 1177 HOH A O 1 HETATM 6274 O O . HOH T 9 . ? 13.718 55.192 33.171 1.00 27.88 ? 1178 HOH A O 1 HETATM 6275 O O . HOH T 9 . ? 24.604 23.112 53.346 1.00 40.71 ? 1179 HOH A O 1 HETATM 6276 O O . HOH T 9 . ? 25.401 66.611 57.091 1.00 32.49 ? 1180 HOH A O 1 HETATM 6277 O O . HOH T 9 . ? 6.537 42.922 27.569 1.00 36.30 ? 1181 HOH A O 1 HETATM 6278 O O . HOH T 9 . ? 35.011 43.974 68.635 1.00 39.29 ? 1182 HOH A O 1 HETATM 6279 O O . HOH T 9 . ? 10.439 84.037 51.634 1.00 37.48 ? 1183 HOH A O 1 HETATM 6280 O O . HOH T 9 . ? 25.311 64.805 44.892 0.50 16.75 ? 1184 HOH A O 1 HETATM 6281 O O . HOH T 9 . ? 25.089 56.762 32.559 1.00 35.93 ? 1185 HOH A O 1 HETATM 6282 O O A HOH T 9 . ? 39.446 57.563 58.693 0.70 32.44 ? 1186 HOH A O 1 HETATM 6283 O O B HOH T 9 . ? 40.129 56.822 60.780 0.30 14.07 ? 1186 HOH A O 1 HETATM 6284 O O . HOH T 9 . ? 8.720 54.439 31.617 1.00 30.18 ? 1187 HOH A O 1 HETATM 6285 O O . HOH T 9 . ? 23.351 24.403 30.755 1.00 37.57 ? 1188 HOH A O 1 HETATM 6286 O O . HOH T 9 . ? 5.722 44.908 25.981 1.00 39.08 ? 1189 HOH A O 1 HETATM 6287 O O . HOH T 9 . ? 17.275 25.864 59.717 1.00 33.79 ? 1190 HOH A O 1 HETATM 6288 O O . HOH T 9 . ? 2.603 63.217 41.156 1.00 35.58 ? 1191 HOH A O 1 HETATM 6289 O O . HOH T 9 . ? 22.889 58.703 21.865 1.00 44.32 ? 1192 HOH A O 1 HETATM 6290 O O . HOH T 9 . ? -4.148 44.193 27.597 1.00 48.93 ? 1193 HOH A O 1 HETATM 6291 O O . HOH T 9 . ? 22.319 83.427 50.306 1.00 38.63 ? 1194 HOH A O 1 HETATM 6292 O O . HOH T 9 . ? 24.501 83.241 46.013 1.00 47.33 ? 1195 HOH A O 1 HETATM 6293 O O A HOH T 9 . ? 24.771 68.031 63.727 0.70 32.05 ? 1196 HOH A O 1 HETATM 6294 O O B HOH T 9 . ? 25.443 70.276 63.872 0.30 15.70 ? 1196 HOH A O 1 HETATM 6295 O O A HOH T 9 . ? -5.196 44.462 31.532 0.80 32.75 ? 1197 HOH A O 1 HETATM 6296 O O B HOH T 9 . ? -5.013 42.497 32.399 0.20 24.02 ? 1197 HOH A O 1 HETATM 6297 O O . HOH T 9 . ? 26.951 64.859 35.449 1.00 42.68 ? 1198 HOH A O 1 HETATM 6298 O O . HOH T 9 . ? 17.782 64.592 67.612 1.00 36.98 ? 1199 HOH A O 1 HETATM 6299 O O . HOH T 9 . ? 33.768 53.292 32.061 1.00 39.42 ? 1200 HOH A O 1 HETATM 6300 O O . HOH T 9 . ? 3.018 64.852 51.351 1.00 28.47 ? 1201 HOH A O 1 HETATM 6301 O O . HOH T 9 . ? 4.231 72.076 36.783 1.00 35.49 ? 1202 HOH A O 1 HETATM 6302 O O . HOH T 9 . ? 9.193 28.771 38.373 1.00 37.87 ? 1203 HOH A O 1 HETATM 6303 O O A HOH T 9 . ? 15.189 24.951 32.789 0.70 24.79 ? 1204 HOH A O 1 HETATM 6304 O O B HOH T 9 . ? 15.304 25.504 30.524 0.30 8.34 ? 1204 HOH A O 1 HETATM 6305 O O . HOH T 9 . ? -1.953 63.518 49.445 1.00 29.60 ? 1205 HOH A O 1 HETATM 6306 O O . HOH T 9 . ? 29.023 25.873 31.804 1.00 36.83 ? 1206 HOH A O 1 HETATM 6307 O O . HOH T 9 . ? 26.631 64.834 29.177 1.00 33.94 ? 1207 HOH A O 1 HETATM 6308 O O . HOH T 9 . ? 25.589 68.010 33.075 1.00 28.79 ? 1208 HOH A O 1 HETATM 6309 O O . HOH T 9 . ? 29.663 67.468 45.789 1.00 38.62 ? 1209 HOH A O 1 HETATM 6310 O O . HOH T 9 . ? 34.701 35.700 58.617 1.00 45.94 ? 1210 HOH A O 1 HETATM 6311 O O . HOH T 9 . ? 21.130 56.572 25.600 1.00 29.95 ? 1211 HOH A O 1 HETATM 6312 O O . HOH T 9 . ? 28.200 36.070 67.822 0.50 25.47 ? 1212 HOH A O 1 HETATM 6313 O O . HOH T 9 . ? 29.606 37.994 66.470 1.00 44.67 ? 1213 HOH A O 1 HETATM 6314 O O . HOH T 9 . ? 13.868 80.447 63.393 1.00 40.51 ? 1214 HOH A O 1 HETATM 6315 O O . HOH T 9 . ? 11.978 73.589 82.185 0.40 18.37 ? 1215 HOH A O 1 HETATM 6316 O O . HOH T 9 . ? 35.046 49.139 33.553 0.50 19.22 ? 1216 HOH A O 1 HETATM 6317 O O . HOH T 9 . ? 14.974 70.016 82.473 1.00 37.44 ? 1217 HOH A O 1 HETATM 6318 O O . HOH T 9 . ? 4.747 50.225 28.603 1.00 36.23 ? 1218 HOH A O 1 HETATM 6319 O O . HOH T 9 . ? 23.410 74.356 66.151 1.00 41.64 ? 1219 HOH A O 1 HETATM 6320 O O . HOH T 9 . ? 16.599 84.807 41.353 1.00 37.96 ? 1220 HOH A O 1 HETATM 6321 O O . HOH T 9 . ? -1.987 44.692 59.096 0.50 20.88 ? 1221 HOH A O 1 HETATM 6322 O O . HOH T 9 . ? -5.419 34.077 47.909 1.00 44.00 ? 1222 HOH A O 1 HETATM 6323 O O . HOH T 9 . ? 12.567 50.302 27.663 1.00 27.14 ? 1223 HOH A O 1 HETATM 6324 O O . HOH T 9 . ? 17.884 58.132 30.168 1.00 40.23 ? 1224 HOH A O 1 HETATM 6325 O O . HOH T 9 . ? 15.786 82.574 58.110 1.00 43.63 ? 1225 HOH A O 1 HETATM 6326 O O . HOH T 9 . ? 10.670 41.080 17.837 1.00 37.12 ? 1226 HOH A O 1 HETATM 6327 O O . HOH T 9 . ? 18.930 53.950 73.598 1.00 39.91 ? 1227 HOH A O 1 HETATM 6328 O O . HOH T 9 . ? 25.993 74.629 58.425 1.00 42.32 ? 1228 HOH A O 1 HETATM 6329 O O . HOH T 9 . ? 30.024 42.047 66.871 1.00 44.83 ? 1229 HOH A O 1 HETATM 6330 O O . HOH T 9 . ? 28.718 64.383 25.846 1.00 39.03 ? 1230 HOH A O 1 HETATM 6331 O O . HOH T 9 . ? 26.367 74.767 55.949 1.00 47.01 ? 1231 HOH A O 1 HETATM 6332 O O . HOH T 9 . ? -9.397 45.751 49.014 1.00 42.45 ? 1232 HOH A O 1 HETATM 6333 O O . HOH T 9 . ? 24.678 59.864 32.929 1.00 42.83 ? 1233 HOH A O 1 HETATM 6334 O O . HOH T 9 . ? -3.480 46.781 25.328 1.00 49.23 ? 1234 HOH A O 1 HETATM 6335 O O . HOH T 9 . ? 1.766 66.643 37.608 1.00 45.31 ? 1235 HOH A O 1 HETATM 6336 O O . HOH T 9 . ? -5.428 50.836 28.853 1.00 41.39 ? 1236 HOH A O 1 HETATM 6337 O O . HOH T 9 . ? 28.197 41.699 68.916 1.00 44.59 ? 1237 HOH A O 1 HETATM 6338 O O . HOH T 9 . ? 20.035 57.797 27.815 1.00 32.00 ? 1238 HOH A O 1 HETATM 6339 O O . HOH T 9 . ? 13.979 68.878 75.897 1.00 38.56 ? 1239 HOH A O 1 HETATM 6340 O O . HOH T 9 . ? 30.503 25.853 38.612 1.00 40.01 ? 1240 HOH A O 1 HETATM 6341 O O . HOH T 9 . ? 35.746 33.978 55.158 0.80 33.56 ? 1241 HOH A O 1 HETATM 6342 O O . HOH T 9 . ? 6.000 53.575 30.556 1.00 31.55 ? 1242 HOH A O 1 HETATM 6343 O O . HOH T 9 . ? 0.021 60.471 48.816 1.00 30.44 ? 1243 HOH A O 1 HETATM 6344 O O . HOH T 9 . ? 10.059 75.783 31.364 1.00 38.38 ? 1244 HOH A O 1 HETATM 6345 O O . HOH T 9 . ? 8.140 56.598 76.142 1.00 26.94 ? 1245 HOH A O 1 HETATM 6346 O O . HOH T 9 . ? 6.942 53.774 75.856 1.00 32.65 ? 1246 HOH A O 1 HETATM 6347 O O . HOH T 9 . ? 11.199 52.517 28.400 1.00 32.72 ? 1247 HOH A O 1 HETATM 6348 O O A HOH T 9 . ? 29.760 60.785 53.237 0.50 17.17 ? 1248 HOH A O 1 HETATM 6349 O O B HOH T 9 . ? 29.377 60.767 51.188 0.50 35.97 ? 1248 HOH A O 1 HETATM 6350 O O A HOH T 9 . ? 36.448 46.503 31.701 0.70 27.01 ? 1249 HOH A O 1 HETATM 6351 O O B HOH T 9 . ? 36.842 48.425 30.591 0.30 14.98 ? 1249 HOH A O 1 HETATM 6352 O O . HOH T 9 . ? 4.017 64.029 35.236 1.00 38.81 ? 1250 HOH A O 1 HETATM 6353 O O . HOH T 9 . ? 17.315 59.159 45.278 1.00 26.73 ? 1251 HOH A O 1 HETATM 6354 O O . HOH T 9 . ? 15.644 54.937 72.907 0.50 29.27 ? 1252 HOH A O 1 HETATM 6355 O O . HOH T 9 . ? 26.932 31.119 64.034 1.00 49.82 ? 1253 HOH A O 1 HETATM 6356 O O . HOH T 9 . ? 29.317 28.161 59.758 1.00 45.73 ? 1254 HOH A O 1 HETATM 6357 O O . HOH T 9 . ? 12.273 28.426 61.114 1.00 51.31 ? 1255 HOH A O 1 HETATM 6358 O O . HOH T 9 . ? -7.593 41.692 41.346 1.00 38.84 ? 1256 HOH A O 1 HETATM 6359 O O . HOH T 9 . ? -6.211 41.604 44.802 0.80 34.11 ? 1257 HOH A O 1 HETATM 6360 O O . HOH T 9 . ? 42.293 34.815 38.313 1.00 39.20 ? 1258 HOH A O 1 HETATM 6361 O O . HOH T 9 . ? 26.494 42.151 41.327 1.00 31.63 ? 1259 HOH A O 1 HETATM 6362 O O . HOH T 9 . ? 22.503 45.362 41.406 1.00 20.41 ? 1260 HOH A O 1 HETATM 6363 O O . HOH T 9 . ? 37.627 28.751 39.152 1.00 41.70 ? 1261 HOH A O 1 HETATM 6364 O O . HOH T 9 . ? 23.174 68.210 69.419 0.60 38.27 ? 1262 HOH A O 1 HETATM 6365 O O . HOH T 9 . ? -12.974 47.719 38.029 1.00 29.23 ? 1263 HOH A O 1 HETATM 6366 O O . HOH T 9 . ? 24.175 45.599 39.151 1.00 29.60 ? 1264 HOH A O 1 HETATM 6367 O O . HOH T 9 . ? 24.896 47.793 37.894 1.00 38.91 ? 1265 HOH A O 1 HETATM 6368 O O . HOH T 9 . ? 26.261 40.060 13.829 1.00 37.99 ? 1266 HOH A O 1 HETATM 6369 O O . HOH T 9 . ? 20.765 50.383 76.605 1.00 37.66 ? 1267 HOH A O 1 HETATM 6370 O O . HOH T 9 . ? 19.398 49.914 45.763 1.00 36.34 ? 1268 HOH A O 1 HETATM 6371 O O . HOH T 9 . ? -0.347 63.841 62.812 1.00 41.17 ? 1269 HOH A O 1 HETATM 6372 O O . HOH T 9 . ? 25.682 43.673 39.120 1.00 28.53 ? 1270 HOH A O 1 HETATM 6373 O O . HOH T 9 . ? 34.474 41.252 19.666 1.00 40.16 ? 1271 HOH A O 1 HETATM 6374 O O . HOH T 9 . ? 16.963 63.227 69.387 1.00 46.53 ? 1272 HOH A O 1 HETATM 6375 O O . HOH T 9 . ? 34.944 50.889 31.460 1.00 46.36 ? 1273 HOH A O 1 HETATM 6376 O O . HOH T 9 . ? 24.289 43.774 42.711 1.00 26.30 ? 1274 HOH A O 1 HETATM 6377 O O . HOH T 9 . ? 11.657 28.997 19.407 1.00 42.02 ? 1275 HOH A O 1 HETATM 6378 O O . HOH T 9 . ? 21.824 52.117 45.302 1.00 38.92 ? 1276 HOH A O 1 HETATM 6379 O O . HOH T 9 . ? 9.979 97.245 40.303 1.00 30.84 ? 1277 HOH A O 1 HETATM 6380 O O . HOH T 9 . ? 30.787 35.444 17.154 1.00 41.17 ? 1278 HOH A O 1 HETATM 6381 O O . HOH T 9 . ? 26.162 59.602 47.744 1.00 44.37 ? 1279 HOH A O 1 HETATM 6382 O O . HOH T 9 . ? 35.358 56.132 51.702 1.00 35.85 ? 1280 HOH A O 1 HETATM 6383 O O . HOH T 9 . ? 22.705 60.055 17.508 1.00 52.27 ? 1281 HOH A O 1 HETATM 6384 O O . HOH T 9 . ? 25.621 63.003 38.988 1.00 35.95 ? 1282 HOH A O 1 HETATM 6385 O O . HOH T 9 . ? 25.670 74.486 22.506 1.00 45.91 ? 1283 HOH A O 1 HETATM 6386 O O . HOH T 9 . ? 34.625 36.278 55.152 1.00 43.13 ? 1284 HOH A O 1 HETATM 6387 O O . HOH T 9 . ? 31.001 69.885 41.986 1.00 39.65 ? 1285 HOH A O 1 HETATM 6388 O O . HOH T 9 . ? 30.399 75.713 43.612 1.00 48.65 ? 1286 HOH A O 1 HETATM 6389 O O . HOH T 9 . ? 33.758 29.056 34.498 1.00 37.08 ? 1287 HOH A O 1 HETATM 6390 O O . HOH T 9 . ? 22.859 80.310 57.587 1.00 45.12 ? 1288 HOH A O 1 HETATM 6391 O O . HOH T 9 . ? 12.098 27.650 21.895 1.00 40.75 ? 1289 HOH A O 1 HETATM 6392 O O . HOH T 9 . ? 13.917 61.388 33.389 1.00 44.44 ? 1290 HOH A O 1 HETATM 6393 O O . HOH T 9 . ? 29.355 72.807 50.332 1.00 38.62 ? 1291 HOH A O 1 HETATM 6394 O O . HOH T 9 . ? 7.678 26.765 54.811 1.00 48.23 ? 1292 HOH A O 1 HETATM 6395 O O . HOH T 9 . ? 40.219 41.246 26.778 1.00 43.74 ? 1293 HOH A O 1 HETATM 6396 O O . HOH T 9 . ? 28.576 29.835 62.399 0.40 17.93 ? 1294 HOH A O 1 HETATM 6397 O O . HOH T 9 . ? 32.872 54.339 71.013 1.00 39.37 ? 1295 HOH A O 1 HETATM 6398 O O . HOH T 9 . ? 14.175 40.617 12.574 1.00 46.83 ? 1296 HOH A O 1 HETATM 6399 O O . HOH T 9 . ? 30.003 25.271 47.629 1.00 37.67 ? 1297 HOH A O 1 HETATM 6400 O O . HOH T 9 . ? 8.944 41.784 20.037 1.00 48.55 ? 1298 HOH A O 1 HETATM 6401 O O . HOH T 9 . ? 35.953 34.465 51.361 1.00 44.30 ? 1299 HOH A O 1 HETATM 6402 O O . HOH T 9 . ? 27.382 62.988 63.909 0.75 35.55 ? 1300 HOH A O 1 HETATM 6403 O O . HOH T 9 . ? 34.250 54.903 68.471 1.00 47.19 ? 1301 HOH A O 1 HETATM 6404 O O . HOH T 9 . ? 7.398 57.438 34.055 1.00 45.20 ? 1302 HOH A O 1 HETATM 6405 O O . HOH T 9 . ? 23.208 78.331 23.296 1.00 41.37 ? 1303 HOH A O 1 HETATM 6406 O O . HOH T 9 . ? 21.205 42.120 46.396 1.00 36.16 ? 1304 HOH A O 1 HETATM 6407 O O . HOH T 9 . ? 42.464 30.812 41.299 1.00 50.85 ? 1305 HOH A O 1 HETATM 6408 O O . HOH T 9 . ? 7.026 81.630 63.073 1.00 49.05 ? 1306 HOH A O 1 HETATM 6409 O O . HOH T 9 . ? 24.577 79.482 55.500 1.00 38.16 ? 1307 HOH A O 1 HETATM 6410 O O . HOH T 9 . ? 27.594 66.001 55.388 1.00 41.52 ? 1308 HOH A O 1 HETATM 6411 O O . HOH T 9 . ? 16.703 42.529 44.858 1.00 17.76 ? 1309 HOH A O 1 HETATM 6412 O O . HOH T 9 . ? 15.752 39.604 76.199 0.50 30.97 ? 1310 HOH A O 1 HETATM 6413 O O . HOH T 9 . ? 25.156 42.848 71.906 1.00 44.22 ? 1311 HOH A O 1 HETATM 6414 O O . HOH T 9 . ? 23.584 31.466 70.261 0.50 20.05 ? 1312 HOH A O 1 HETATM 6415 O O . HOH T 9 . ? 12.181 22.848 44.358 0.50 21.34 ? 1313 HOH A O 1 HETATM 6416 O O . HOH T 9 . ? 22.593 55.255 70.188 1.00 50.09 ? 1314 HOH A O 1 HETATM 6417 O O . HOH T 9 . ? -0.540 31.080 63.524 0.70 37.08 ? 1315 HOH A O 1 HETATM 6418 O O . HOH T 9 . ? 20.404 61.961 27.325 1.00 41.39 ? 1316 HOH A O 1 HETATM 6419 O O . HOH T 9 . ? 38.751 30.776 45.864 0.60 36.34 ? 1317 HOH A O 1 HETATM 6420 O O . HOH T 9 . ? 26.871 28.137 28.764 1.00 44.41 ? 1318 HOH A O 1 HETATM 6421 O O . HOH T 9 . ? -7.292 48.161 48.461 1.00 31.29 ? 1319 HOH A O 1 HETATM 6422 O O . HOH T 9 . ? 42.852 52.847 25.254 1.00 50.12 ? 1320 HOH A O 1 HETATM 6423 O O . HOH T 9 . ? 31.112 29.285 11.257 1.00 44.02 ? 1321 HOH A O 1 HETATM 6424 O O . HOH T 9 . ? 37.905 41.738 53.254 1.00 39.07 ? 1322 HOH A O 1 HETATM 6425 O O . HOH T 9 . ? 25.574 71.420 61.474 1.00 46.79 ? 1323 HOH A O 1 HETATM 6426 O O . HOH T 9 . ? 30.764 76.770 49.101 1.00 52.26 ? 1324 HOH A O 1 HETATM 6427 O O . HOH T 9 . ? 24.569 58.536 44.050 0.35 20.38 ? 1325 HOH A O 1 HETATM 6428 O O . HOH T 9 . ? 24.819 62.766 42.863 0.50 23.50 ? 1326 HOH A O 1 HETATM 6429 O O . HOH T 9 . ? 9.771 47.273 80.710 0.50 35.01 ? 1327 HOH A O 1 HETATM 6430 O O . HOH T 9 . ? 13.684 30.497 66.971 0.75 41.50 ? 1328 HOH A O 1 HETATM 6431 O O . HOH T 9 . ? -0.129 29.632 45.246 0.50 33.28 ? 1329 HOH A O 1 HETATM 6432 O O . HOH T 9 . ? -4.288 29.543 53.431 0.50 24.59 ? 1330 HOH A O 1 HETATM 6433 O O . HOH T 9 . ? 1.703 40.922 27.471 1.00 43.16 ? 1331 HOH A O 1 HETATM 6434 O O . HOH T 9 . ? 8.334 30.235 36.378 0.50 20.73 ? 1332 HOH A O 1 HETATM 6435 O O . HOH T 9 . ? 5.230 30.268 37.350 0.60 31.37 ? 1333 HOH A O 1 HETATM 6436 O O . HOH T 9 . ? 10.898 27.228 32.412 0.80 33.22 ? 1334 HOH A O 1 HETATM 6437 O O . HOH T 9 . ? 15.258 71.697 22.214 0.50 28.32 ? 1335 HOH A O 1 HETATM 6438 O O . HOH T 9 . ? 20.256 64.188 25.896 0.50 27.77 ? 1336 HOH A O 1 HETATM 6439 O O . HOH T 9 . ? 29.212 61.801 27.228 1.00 44.03 ? 1337 HOH A O 1 HETATM 6440 O O . HOH T 9 . ? 32.000 57.796 26.835 0.50 27.45 ? 1338 HOH A O 1 HETATM 6441 O O . HOH T 9 . ? 31.430 56.985 31.557 0.50 20.94 ? 1339 HOH A O 1 HETATM 6442 O O . HOH T 9 . ? 8.406 50.558 25.691 1.00 44.13 ? 1340 HOH A O 1 HETATM 6443 O O . HOH T 9 . ? 29.018 57.735 48.901 0.30 10.60 ? 1341 HOH A O 1 HETATM 6444 O O . HOH T 9 . ? 19.071 24.870 12.674 0.25 12.76 ? 1342 HOH A O 1 HETATM 6445 O O . HOH T 9 . ? 10.016 38.547 15.945 0.40 26.94 ? 1343 HOH A O 1 HETATM 6446 O O . HOH T 9 . ? 32.509 46.408 36.923 0.50 23.30 ? 1344 HOH A O 1 HETATM 6447 O O . HOH T 9 . ? 34.893 20.996 44.319 1.00 48.89 ? 1345 HOH A O 1 HETATM 6448 O O . HOH T 9 . ? -14.344 42.771 41.620 0.60 33.01 ? 1346 HOH A O 1 HETATM 6449 O O . HOH T 9 . ? -8.290 49.599 50.436 1.00 31.42 ? 1347 HOH A O 1 HETATM 6450 O O . HOH T 9 . ? 29.025 28.189 25.492 0.30 17.05 ? 1348 HOH A O 1 HETATM 6451 O O . HOH T 9 . ? 36.069 37.722 57.447 0.25 17.21 ? 1349 HOH A O 1 HETATM 6452 O O . HOH T 9 . ? 36.536 42.325 65.810 1.00 32.79 ? 1350 HOH A O 1 HETATM 6453 O O . HOH T 9 . ? 43.340 40.009 64.537 1.00 52.02 ? 1351 HOH A O 1 HETATM 6454 O O . HOH T 9 . ? 29.509 69.312 53.145 0.70 32.41 ? 1352 HOH A O 1 HETATM 6455 O O . HOH T 9 . ? 37.317 56.735 64.472 1.00 39.71 ? 1353 HOH A O 1 HETATM 6456 O O . HOH T 9 . ? 28.185 24.601 53.649 0.75 37.71 ? 1354 HOH A O 1 HETATM 6457 O O . HOH T 9 . ? 32.396 27.689 56.660 0.50 16.72 ? 1355 HOH A O 1 HETATM 6458 O O . HOH T 9 . ? 24.329 82.214 24.696 1.00 45.23 ? 1356 HOH A O 1 HETATM 6459 O O . HOH T 9 . ? -0.363 59.507 76.816 0.80 51.89 ? 1357 HOH A O 1 HETATM 6460 O O . HOH T 9 . ? 8.352 69.879 37.409 0.80 33.62 ? 1358 HOH A O 1 HETATM 6461 O O . HOH T 9 . ? 11.143 63.847 30.697 1.00 55.74 ? 1359 HOH A O 1 HETATM 6462 O O . HOH T 9 . ? 1.141 31.882 67.799 0.60 26.68 ? 1360 HOH A O 1 HETATM 6463 O O . HOH T 9 . ? 9.363 81.179 58.957 0.50 25.47 ? 1361 HOH A O 1 HETATM 6464 O O . HOH T 9 . ? 6.212 83.794 56.411 0.50 37.17 ? 1362 HOH A O 1 HETATM 6465 O O . HOH T 9 . ? -2.300 43.820 56.850 0.50 22.28 ? 1363 HOH A O 1 HETATM 6466 O O . HOH T 9 . ? 4.042 46.618 25.447 0.40 29.89 ? 1364 HOH A O 1 HETATM 6467 O O . HOH T 9 . ? 0.002 57.961 36.096 0.85 45.66 ? 1365 HOH A O 1 HETATM 6468 O O . HOH T 9 . ? 0.846 63.566 38.504 0.80 41.69 ? 1366 HOH A O 1 HETATM 6469 O O . HOH T 9 . ? 10.153 23.951 44.812 1.00 45.74 ? 1367 HOH A O 1 HETATM 6470 O O . HOH T 9 . ? 8.620 22.560 47.054 0.50 31.19 ? 1368 HOH A O 1 HETATM 6471 O O . HOH T 9 . ? 23.050 60.968 20.340 1.00 44.52 ? 1369 HOH A O 1 HETATM 6472 O O . HOH T 9 . ? 18.356 60.184 19.403 0.40 29.50 ? 1370 HOH A O 1 HETATM 6473 O O . HOH T 9 . ? 28.113 63.764 23.251 1.00 43.70 ? 1371 HOH A O 1 HETATM 6474 O O A HOH T 9 . ? 13.893 58.666 33.141 0.15 5.28 ? 1372 HOH A O 1 HETATM 6475 O O B HOH T 9 . ? 15.295 57.284 32.411 0.50 20.40 ? 1372 HOH A O 1 HETATM 6476 O O . HOH T 9 . ? 23.112 43.856 44.952 0.70 31.32 ? 1373 HOH A O 1 HETATM 6477 O O . HOH T 9 . ? 37.133 40.036 56.089 0.50 16.80 ? 1374 HOH A O 1 HETATM 6478 O O . HOH T 9 . ? 29.590 34.895 65.352 0.60 40.01 ? 1375 HOH A O 1 HETATM 6479 O O . HOH T 9 . ? 18.011 59.351 70.726 1.00 45.93 ? 1376 HOH A O 1 HETATM 6480 O O . HOH T 9 . ? 5.139 53.268 78.287 1.00 35.88 ? 1377 HOH A O 1 HETATM 6481 O O . HOH T 9 . ? -1.180 56.874 74.394 1.00 63.62 ? 1378 HOH A O 1 HETATM 6482 O O . HOH T 9 . ? 0.882 57.944 78.063 1.00 48.05 ? 1379 HOH A O 1 HETATM 6483 O O . HOH T 9 . ? 27.384 65.791 46.460 1.00 33.12 ? 1380 HOH A O 1 HETATM 6484 O O . HOH T 9 . ? 30.883 67.199 43.080 1.00 48.42 ? 1381 HOH A O 1 HETATM 6485 O O . HOH T 9 . ? 30.753 71.785 48.240 1.00 49.03 ? 1382 HOH A O 1 HETATM 6486 O O . HOH T 9 . ? 31.978 73.588 44.484 0.60 39.25 ? 1383 HOH A O 1 HETATM 6487 O O . HOH T 9 . ? 32.430 72.174 36.013 1.00 66.33 ? 1384 HOH A O 1 HETATM 6488 O O . HOH T 9 . ? 31.995 77.106 38.580 1.00 57.39 ? 1385 HOH A O 1 HETATM 6489 O O . HOH T 9 . ? 30.831 70.393 37.666 0.70 30.50 ? 1386 HOH A O 1 HETATM 6490 O O . HOH T 9 . ? 32.500 87.637 30.844 0.50 25.35 ? 1387 HOH A O 1 HETATM 6491 O O . HOH T 9 . ? 32.451 84.618 32.697 1.00 40.79 ? 1388 HOH A O 1 HETATM 6492 O O . HOH T 9 . ? 21.935 87.966 46.859 0.50 21.36 ? 1389 HOH A O 1 HETATM 6493 O O . HOH T 9 . ? 26.487 85.728 45.814 0.80 35.40 ? 1390 HOH A O 1 HETATM 6494 O O . HOH T 9 . ? 20.570 80.854 63.211 0.60 40.50 ? 1391 HOH A O 1 HETATM 6495 O O . HOH T 9 . ? 13.747 81.537 66.254 0.75 35.83 ? 1392 HOH A O 1 HETATM 6496 O O . HOH T 9 . ? 12.196 81.047 70.338 0.25 9.11 ? 1393 HOH A O 1 HETATM 6497 O O . HOH T 9 . ? 17.219 66.262 71.059 0.70 32.41 ? 1394 HOH A O 1 HETATM 6498 O O . HOH T 9 . ? 19.554 41.508 78.675 0.70 34.87 ? 1395 HOH A O 1 HETATM 6499 O O . HOH T 9 . ? 22.724 50.170 78.649 0.50 27.18 ? 1396 HOH A O 1 HETATM 6500 O O . HOH T 9 . ? 15.829 29.183 66.254 0.90 50.18 ? 1397 HOH A O 1 HETATM 6501 O O . HOH T 9 . ? -2.729 32.769 56.217 1.00 32.46 ? 1398 HOH A O 1 HETATM 6502 O O . HOH T 9 . ? -4.171 51.449 69.344 1.00 50.87 ? 1399 HOH A O 1 HETATM 6503 O O . HOH T 9 . ? -2.304 41.490 30.889 0.55 47.84 ? 1400 HOH A O 1 HETATM 6504 O O . HOH T 9 . ? 12.412 24.900 36.104 0.38 21.54 ? 1401 HOH A O 1 HETATM 6505 O O . HOH T 9 . ? 18.319 23.733 36.722 0.60 29.19 ? 1402 HOH A O 1 HETATM 6506 O O . HOH T 9 . ? 24.217 21.949 31.637 0.50 31.43 ? 1403 HOH A O 1 HETATM 6507 O O . HOH T 9 . ? 37.348 50.310 41.900 0.50 34.03 ? 1404 HOH A O 1 HETATM 6508 O O . HOH T 9 . ? 37.303 26.069 48.313 0.85 40.73 ? 1405 HOH A O 1 HETATM 6509 O O . HOH T 9 . ? 21.212 67.084 70.582 0.60 35.34 ? 1406 HOH A O 1 HETATM 6510 O O . HOH T 9 . ? 21.508 73.573 69.438 0.50 23.36 ? 1407 HOH A O 1 HETATM 6511 O O . HOH T 9 . ? 12.058 75.610 73.468 1.00 50.02 ? 1408 HOH A O 1 HETATM 6512 O O . HOH T 9 . ? 1.159 63.282 43.354 1.00 32.42 ? 1409 HOH A O 1 HETATM 6513 O O . HOH T 9 . ? 4.466 73.392 34.718 1.00 46.60 ? 1410 HOH A O 1 HETATM 6514 O O . HOH T 9 . ? 0.019 65.071 40.361 0.50 60.10 ? 1411 HOH A O 1 HETATM 6515 O O . HOH T 9 . ? 33.483 73.743 41.540 1.00 53.75 ? 1412 HOH A O 1 HETATM 6516 O O . HOH T 9 . ? 13.207 27.732 17.638 0.50 28.87 ? 1413 HOH A O 1 HETATM 6517 O O . HOH T 9 . ? 1.304 60.201 44.059 1.00 25.52 ? 1414 HOH A O 1 HETATM 6518 O O . HOH T 9 . ? 26.606 54.568 40.506 1.00 45.41 ? 1415 HOH A O 1 HETATM 6519 O O . HOH T 9 . ? 28.544 48.072 38.604 0.75 32.69 ? 1416 HOH A O 1 HETATM 6520 O O . HOH T 9 . ? -0.796 37.732 66.590 0.50 32.03 ? 1417 HOH A O 1 HETATM 6521 O O . HOH T 9 . ? 7.049 26.962 40.594 0.40 30.17 ? 1418 HOH A O 1 HETATM 6522 O O . HOH T 9 . ? 35.992 30.670 8.174 1.00 49.85 ? 1419 HOH A O 1 HETATM 6523 O O . HOH T 9 . ? 19.670 58.350 69.004 1.00 51.25 ? 1420 HOH A O 1 HETATM 6524 O O . HOH T 9 . ? 24.565 81.528 50.839 0.50 21.90 ? 1421 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 . HIS A 63 ? 0.7501 0.6082 0.4140 0.1666 -0.0612 0.0193 56 HIS A N 2 C CA . HIS A 63 ? 0.7407 0.5798 0.4336 0.1866 -0.0646 0.0359 56 HIS A CA 3 C C . HIS A 63 ? 0.7132 0.5563 0.4277 0.1930 -0.0626 0.0222 56 HIS A C 4 O O . HIS A 63 ? 0.7156 0.5643 0.4723 0.2006 -0.0647 0.0241 56 HIS A O 5 C CB . HIS A 63 ? 0.7517 0.5908 0.4365 0.1863 -0.0740 0.0415 56 HIS A CB 6 C CG . HIS A 63 ? 0.8000 0.6161 0.4667 0.1725 -0.0736 0.0405 56 HIS A CG 7 N ND1 . HIS A 63 ? 0.8146 0.6488 0.4690 0.1656 -0.0685 0.0416 56 HIS A ND1 8 C CD2 . HIS A 63 ? 0.8305 0.6215 0.4806 0.1828 -0.0571 0.0280 56 HIS A CD2 9 C CE1 . HIS A 63 ? 0.8417 0.6533 0.5066 0.1730 -0.0618 0.0418 56 HIS A CE1 10 N NE2 . HIS A 63 ? 0.8580 0.6394 0.5047 0.1780 -0.0500 0.0333 56 HIS A NE2 11 N N . ASN A 64 ? 0.6731 0.5122 0.3683 0.1964 -0.0647 0.0118 57 ASN A N 12 C CA . ASN A 64 ? 0.6268 0.4795 0.3016 0.1951 -0.0744 0.0015 57 ASN A CA 13 C C . ASN A 64 ? 0.5886 0.4579 0.2902 0.1955 -0.0849 0.0077 57 ASN A C 14 O O . ASN A 64 ? 0.5627 0.4270 0.2288 0.2033 -0.0838 0.0082 57 ASN A O 15 C CB . ASN A 64 ? 0.6285 0.4722 0.2989 0.1922 -0.0686 0.0013 57 ASN A CB 16 C CG . ASN A 64 ? 0.6524 0.4714 0.2671 0.1853 -0.0860 -0.0160 57 ASN A CG 17 O OD1 . ASN A 64 ? 0.6684 0.4544 0.2074 0.1816 -0.0903 -0.0148 57 ASN A OD1 18 N ND2 . ASN A 64 ? 0.6707 0.4065 0.2860 0.2068 -0.0999 -0.0416 57 ASN A ND2 19 N N . MET A 65 ? 0.5528 0.4442 0.2980 0.1908 -0.0858 -0.0051 58 MET A N 20 C CA . MET A 65 ? 0.5444 0.4347 0.2911 0.1831 -0.0983 -0.0115 58 MET A CA 21 C C . MET A 65 ? 0.5397 0.4204 0.2966 0.1810 -0.0975 -0.0146 58 MET A C 22 O O . MET A 65 ? 0.5272 0.4065 0.2866 0.1807 -0.0995 -0.0294 58 MET A O 23 C CB . MET A 65 ? 0.5498 0.4389 0.2864 0.1788 -0.1004 -0.0065 58 MET A CB 24 C CG . MET A 65 ? 0.5412 0.4770 0.3265 0.1700 -0.0842 -0.0294 58 MET A CG 25 S SD . MET A 65 ? 0.5683 0.5904 0.3906 0.1478 -0.0469 -0.0206 58 MET A SD 26 C CE . MET A 65 ? 0.5748 0.5309 0.4692 0.1406 -0.0697 -0.0158 58 MET A CE 27 N N . LYS A 66 ? 0.5219 0.4076 0.2823 0.1821 -0.1116 -0.0137 59 LYS A N 28 C CA . LYS A 66 ? 0.5273 0.4032 0.2938 0.1766 -0.1120 -0.0021 59 LYS A CA 29 C C . LYS A 66 ? 0.5272 0.4082 0.2873 0.1664 -0.1050 -0.0043 59 LYS A C 30 O O . LYS A 66 ? 0.5287 0.4025 0.2932 0.1666 -0.0990 0.0074 59 LYS A O 31 C CB . LYS A 66 ? 0.5103 0.3980 0.3023 0.1799 -0.1245 -0.0043 59 LYS A CB 32 C CG . LYS A 66 ? 0.4975 0.3949 0.3345 0.1902 -0.1444 0.0116 59 LYS A CG 33 C CD . LYS A 66 ? 0.4951 0.3809 0.3012 0.2136 -0.1579 0.0172 59 LYS A CD 34 C CE . LYS A 66 ? 0.4842 0.3770 0.2846 0.2108 -0.1785 0.0108 59 LYS A CE 35 N NZ . LYS A 66 ? 0.4306 0.3714 0.2554 0.2418 -0.2092 0.0321 59 LYS A NZ 36 N N . ALA A 67 ? 0.5363 0.4077 0.2685 0.1596 -0.0928 -0.0003 60 ALA A N 37 C CA . ALA A 67 ? 0.5319 0.4035 0.2528 0.1578 -0.0849 0.0036 60 ALA A CA 38 C C . ALA A 67 ? 0.5188 0.3872 0.2389 0.1570 -0.0822 0.0146 60 ALA A C 39 O O . ALA A 67 ? 0.5273 0.3812 0.2116 0.1614 -0.0799 0.0256 60 ALA A O 40 C CB . ALA A 67 ? 0.5289 0.4168 0.2462 0.1568 -0.0857 0.0063 60 ALA A CB 41 N N . PHE A 68 ? 0.4915 0.3675 0.2432 0.1571 -0.0799 0.0183 61 PHE A N 42 C CA . PHE A 68 ? 0.4771 0.3505 0.2420 0.1561 -0.0679 0.0159 61 PHE A CA 43 C C . PHE A 68 ? 0.4765 0.3425 0.2474 0.1551 -0.0687 0.0174 61 PHE A C 44 O O . PHE A 68 ? 0.4777 0.3319 0.2518 0.1447 -0.0456 0.0298 61 PHE A O 45 C CB . PHE A 68 ? 0.4640 0.3347 0.2414 0.1501 -0.0711 0.0165 61 PHE A CB 46 C CG . PHE A 68 ? 0.4413 0.3302 0.2317 0.1304 -0.0471 0.0045 61 PHE A CG 47 C CD1 . PHE A 68 ? 0.4010 0.3427 0.2123 0.1261 -0.0487 0.0116 61 PHE A CD1 48 C CD2 . PHE A 68 ? 0.4078 0.3315 0.2468 0.1051 -0.0615 0.0114 61 PHE A CD2 49 C CE1 . PHE A 68 ? 0.3989 0.2935 0.2334 0.1042 -0.0720 -0.0105 61 PHE A CE1 50 C CE2 . PHE A 68 ? 0.3755 0.3328 0.2380 0.0914 -0.0469 0.0042 61 PHE A CE2 51 C CZ . PHE A 68 ? 0.3948 0.2973 0.2239 0.1181 -0.0536 -0.0131 61 PHE A CZ 52 N N . LEU A 69 ? 0.4657 0.3388 0.2544 0.1606 -0.0766 0.0137 62 LEU A N 53 C CA . LEU A 69 ? 0.4738 0.3526 0.2614 0.1526 -0.0862 0.0130 62 LEU A CA 54 C C . LEU A 69 ? 0.4827 0.3559 0.2701 0.1580 -0.0917 0.0098 62 LEU A C 55 O O . LEU A 69 ? 0.4783 0.3537 0.2493 0.1489 -0.1085 0.0158 62 LEU A O 56 C CB . LEU A 69 ? 0.4716 0.3499 0.2675 0.1513 -0.0733 0.0141 62 LEU A CB 57 C CG . LEU A 69 ? 0.4741 0.3459 0.2651 0.1469 -0.0773 0.0054 62 LEU A CG 58 C CD1 . LEU A 69 ? 0.4751 0.3307 0.2374 0.1421 -0.0286 -0.0109 62 LEU A CD1 59 C CD2 . LEU A 69 ? 0.4328 0.3367 0.2590 0.1525 -0.0168 -0.0126 62 LEU A CD2 60 N N . ASP A 70 ? 0.5067 0.3690 0.2768 0.1593 -0.0906 0.0173 63 ASP A N 61 C CA . ASP A 70 ? 0.5268 0.3879 0.2938 0.1614 -0.0879 0.0068 63 ASP A CA 62 C C . ASP A 70 ? 0.5220 0.3787 0.2835 0.1675 -0.0832 -0.0028 63 ASP A C 63 O O . ASP A 70 ? 0.5180 0.3787 0.2758 0.1762 -0.0864 0.0003 63 ASP A O 64 C CB . ASP A 70 ? 0.5307 0.4003 0.2830 0.1566 -0.0933 0.0030 63 ASP A CB 65 C CG . ASP A 70 ? 0.5507 0.4472 0.3280 0.1534 -0.0920 -0.0064 63 ASP A CG 66 O OD1 . ASP A 70 ? 0.5426 0.4815 0.4206 0.1206 -0.0687 -0.0127 63 ASP A OD1 67 O OD2 . ASP A 70 ? 0.5666 0.5128 0.3557 0.1570 -0.1309 0.0031 63 ASP A OD2 68 N N . GLU A 71 ? 0.5122 0.3766 0.2870 0.1655 -0.0739 0.0007 64 GLU A N 69 C CA . GLU A 71 ? 0.4965 0.3703 0.2963 0.1633 -0.0541 0.0074 64 GLU A CA 70 C C . GLU A 71 ? 0.4770 0.3587 0.2864 0.1654 -0.0529 0.0142 64 GLU A C 71 O O . GLU A 71 ? 0.4865 0.3501 0.2676 0.1600 -0.0565 0.0138 64 GLU A O 72 C CB . GLU A 71 ? 0.5031 0.3730 0.2988 0.1706 -0.0395 0.0063 64 GLU A CB 73 C CG . GLU A 71 ? 0.5064 0.3733 0.3063 0.1576 -0.0193 0.0258 64 GLU A CG 74 C CD . GLU A 71 ? 0.5552 0.4097 0.3228 0.1277 -0.0001 0.0399 64 GLU A CD 75 O OE1 . GLU A 71 ? 0.5317 0.4647 0.2883 0.0789 -0.0048 0.0699 64 GLU A OE1 76 O OE2 . GLU A 71 ? 0.5669 0.3683 0.3778 0.1434 0.0395 0.0393 64 GLU A OE2 77 N N . LEU A 72 ? 0.4509 0.3403 0.2890 0.1601 -0.0497 0.0173 65 LEU A N 78 C CA . LEU A 72 ? 0.4330 0.3252 0.2862 0.1553 -0.0595 0.0201 65 LEU A CA 79 C C . LEU A 72 ? 0.4252 0.3360 0.2924 0.1520 -0.0553 0.0206 65 LEU A C 80 O O . LEU A 72 ? 0.4207 0.3464 0.2699 0.1618 -0.0731 0.0383 65 LEU A O 81 C CB . LEU A 72 ? 0.4168 0.3177 0.2706 0.1484 -0.0563 0.0178 65 LEU A CB 82 C CG . LEU A 72 ? 0.3969 0.2920 0.2623 0.1279 -0.0818 0.0240 65 LEU A CG 83 C CD1 . LEU A 72 ? 0.3684 0.2844 0.2731 0.0955 -0.1185 0.0006 65 LEU A CD1 84 C CD2 . LEU A 72 ? 0.3575 0.2444 0.2595 0.1103 -0.0813 0.0313 65 LEU A CD2 85 N N . LYS A 73 ? 0.4228 0.3092 0.3124 0.1459 -0.0442 0.0233 66 LYS A N 86 C CA . LYS A 73 ? 0.4303 0.3222 0.3146 0.1466 -0.0474 0.0204 66 LYS A CA 87 C C . LYS A 73 ? 0.4101 0.3023 0.3202 0.1433 -0.0436 0.0187 66 LYS A C 88 O O . LYS A 73 ? 0.3964 0.2829 0.3002 0.1524 -0.0410 0.0115 66 LYS A O 89 C CB . LYS A 73 ? 0.4430 0.3263 0.3158 0.1402 -0.0444 0.0271 66 LYS A CB 90 C CG . LYS A 73 ? 0.5235 0.4189 0.3319 0.1508 -0.0256 0.0075 66 LYS A CG 91 C CD . LYS A 73 ? 0.5916 0.4999 0.3573 0.1781 -0.0362 0.0395 66 LYS A CD 92 C CE . LYS A 73 ? 0.6975 0.4860 0.3994 0.2101 0.0421 0.0342 66 LYS A CE 93 N NZ . LYS A 73 ? 0.7116 0.4753 0.4106 0.2485 0.0434 0.0850 66 LYS A NZ 94 N N . ALA A 74 ? 0.4002 0.3036 0.3403 0.1402 -0.0448 0.0126 67 ALA A N 95 C CA . ALA A 74 ? 0.3905 0.3110 0.3280 0.1343 -0.0488 0.0095 67 ALA A CA 96 C C . ALA A 74 ? 0.3954 0.3114 0.3464 0.1301 -0.0437 0.0162 67 ALA A C 97 O O . ALA A 74 ? 0.3639 0.2971 0.3505 0.1147 -0.0578 0.0133 67 ALA A O 98 C CB . ALA A 74 ? 0.3988 0.3396 0.3232 0.1156 -0.0391 0.0046 67 ALA A CB 99 N N . GLU A 75 ? 0.4087 0.2994 0.3574 0.1380 -0.0432 0.0328 68 GLU A N 100 C CA . GLU A 75 ? 0.4268 0.3123 0.3689 0.1401 -0.0378 0.0327 68 GLU A CA 101 C C . GLU A 75 ? 0.4180 0.2996 0.3523 0.1397 -0.0306 0.0350 68 GLU A C 102 O O . GLU A 75 ? 0.4107 0.2800 0.3682 0.1534 -0.0219 0.0339 68 GLU A O 103 C CB . GLU A 75 ? 0.4524 0.3139 0.3918 0.1344 -0.0340 0.0468 68 GLU A CB 104 C CG . GLU A 75 ? 0.5110 0.3736 0.4222 0.1503 -0.0172 0.0140 68 GLU A CG 105 C CD . GLU A 75 ? 0.5695 0.4435 0.4759 0.1781 0.0109 0.0198 68 GLU A CD 106 O OE1 . GLU A 75 ? 0.6161 0.4671 0.4825 0.1839 0.0414 0.0030 68 GLU A OE1 107 O OE2 . GLU A 75 ? 0.5694 0.4188 0.4763 0.1829 0.0081 0.0175 68 GLU A OE2 108 N N . ASN A 76 ? 0.4017 0.2845 0.3394 0.1420 -0.0275 0.0377 69 ASN A N 109 C CA . ASN A 76 ? 0.3943 0.2814 0.3261 0.1300 -0.0181 0.0247 69 ASN A CA 110 C C . ASN A 76 ? 0.3736 0.2680 0.3182 0.1215 -0.0180 0.0246 69 ASN A C 111 O O . ASN A 76 ? 0.3646 0.2753 0.3394 0.1098 -0.0171 0.0280 69 ASN A O 112 C CB . ASN A 76 ? 0.3944 0.2994 0.3154 0.1326 -0.0131 0.0324 69 ASN A CB 113 C CG . ASN A 76 ? 0.4392 0.2835 0.3203 0.1331 -0.0039 0.0403 69 ASN A CG 114 O OD1 . ASN A 76 ? 0.4753 0.2483 0.3010 0.1681 0.0102 0.0400 69 ASN A OD1 115 N ND2 . ASN A 76 ? 0.4337 0.3056 0.2654 0.1478 -0.0069 0.0602 69 ASN A ND2 116 N N . ILE A 77 ? 0.3623 0.2596 0.3091 0.1132 -0.0161 0.0140 70 ILE A N 117 C CA . ILE A 77 ? 0.3466 0.2405 0.3056 0.1070 -0.0135 0.0203 70 ILE A CA 118 C C . ILE A 77 ? 0.3379 0.2534 0.3164 0.1053 -0.0155 0.0199 70 ILE A C 119 O O . ILE A 77 ? 0.3117 0.2389 0.3062 0.1029 -0.0138 0.0233 70 ILE A O 120 C CB . ILE A 77 ? 0.3581 0.2431 0.3065 0.1055 -0.0138 0.0191 70 ILE A CB 121 C CG1 . ILE A 77 ? 0.3628 0.2413 0.2710 0.0807 -0.0136 0.0115 70 ILE A CG1 122 C CG2 . ILE A 77 ? 0.3596 0.2399 0.2630 0.0872 0.0171 0.0120 70 ILE A CG2 123 C CD1 . ILE A 77 ? 0.4167 0.1877 0.3066 0.0897 -0.0240 -0.0046 70 ILE A CD1 124 N N . LYS A 78 ? 0.3338 0.2455 0.3352 0.1124 -0.0167 0.0235 71 LYS A N 125 C CA . LYS A 78 ? 0.3294 0.2507 0.3318 0.1130 -0.0149 0.0170 71 LYS A CA 126 C C . LYS A 78 ? 0.3328 0.2806 0.3294 0.1044 -0.0175 0.0178 71 LYS A C 127 O O . LYS A 78 ? 0.3364 0.2946 0.3317 0.0877 -0.0002 0.0138 71 LYS A O 128 C CB . LYS A 78 ? 0.3252 0.2544 0.3462 0.1188 -0.0195 0.0073 71 LYS A CB 129 C CG . LYS A 78 ? 0.3500 0.2510 0.3729 0.1487 -0.0465 0.0028 71 LYS A CG 130 C CD . LYS A 78 ? 0.3701 0.2538 0.4229 0.1687 -0.0602 -0.0354 71 LYS A CD 131 C CE . LYS A 78 ? 0.3963 0.3462 0.4533 0.1645 -0.0692 -0.0338 71 LYS A CE 132 N NZ . LYS A 78 ? 0.3753 0.3414 0.4506 0.1791 -0.1012 -0.0255 71 LYS A NZ 133 N N . LYS A 79 ? 0.3408 0.2882 0.3282 0.0914 -0.0163 0.0268 72 LYS A N 134 C CA . LYS A 79 ? 0.3636 0.2865 0.3329 0.0958 -0.0183 0.0394 72 LYS A CA 135 C C . LYS A 79 ? 0.3447 0.2608 0.3167 0.1004 -0.0177 0.0392 72 LYS A C 136 O O . LYS A 79 ? 0.3433 0.2282 0.3023 0.1020 -0.0304 0.0450 72 LYS A O 137 C CB . LYS A 79 ? 0.3735 0.2897 0.3031 0.1006 -0.0170 0.0505 72 LYS A CB 138 C CG . LYS A 79 ? 0.3884 0.3193 0.3672 0.1077 -0.0099 0.0498 72 LYS A CG 139 C CD . LYS A 79 ? 0.3841 0.2907 0.3277 0.1049 -0.0410 0.0712 72 LYS A CD 140 C CE . LYS A 79 ? 0.3865 0.2681 0.3400 0.1188 -0.0309 0.0662 72 LYS A CE 141 N NZ . LYS A 79 ? 0.3855 0.2536 0.3254 0.1368 -0.0506 0.0709 72 LYS A NZ 142 N N . PHE A 80 ? 0.3369 0.2421 0.3122 0.0976 -0.0074 0.0320 73 PHE A N 143 C CA . PHE A 80 ? 0.3236 0.2466 0.3018 0.0976 -0.0038 0.0269 73 PHE A CA 144 C C . PHE A 80 ? 0.3160 0.2471 0.3063 0.0863 0.0003 0.0221 73 PHE A C 145 O O . PHE A 80 ? 0.3164 0.2520 0.2864 0.0838 0.0047 0.0395 73 PHE A O 146 C CB . PHE A 80 ? 0.3244 0.2343 0.2957 0.1044 -0.0075 0.0201 73 PHE A CB 147 C CG . PHE A 80 ? 0.3354 0.2393 0.3208 0.1204 -0.0076 0.0321 73 PHE A CG 148 C CD1 . PHE A 80 ? 0.3601 0.2541 0.3162 0.1163 0.0001 0.0387 73 PHE A CD1 149 C CD2 . PHE A 80 ? 0.3482 0.2616 0.3005 0.1188 -0.0205 0.0168 73 PHE A CD2 150 C CE1 . PHE A 80 ? 0.3723 0.2739 0.3228 0.1515 0.0042 0.0107 73 PHE A CE1 151 C CE2 . PHE A 80 ? 0.3074 0.2351 0.3171 0.1424 0.0103 0.0384 73 PHE A CE2 152 C CZ . PHE A 80 ? 0.3675 0.2526 0.3256 0.1354 -0.0114 0.0416 73 PHE A CZ 153 N N . LEU A 81 ? 0.2886 0.2388 0.3023 0.0856 0.0012 0.0146 74 LEU A N 154 C CA . LEU A 81 ? 0.2774 0.2304 0.2981 0.0796 -0.0056 0.0125 74 LEU A CA 155 C C . LEU A 81 ? 0.2831 0.2322 0.3095 0.0811 -0.0088 0.0105 74 LEU A C 156 O O . LEU A 81 ? 0.2775 0.2312 0.3049 0.0904 -0.0149 0.0121 74 LEU A O 157 C CB . LEU A 81 ? 0.2724 0.2434 0.2877 0.0729 -0.0060 0.0070 74 LEU A CB 158 C CG . LEU A 81 ? 0.2405 0.2258 0.2616 0.0758 -0.0102 -0.0030 74 LEU A CG 159 C CD1 . LEU A 81 ? 0.2368 0.1468 0.2693 0.0911 -0.0183 -0.0186 74 LEU A CD1 160 C CD2 . LEU A 81 ? 0.2180 0.2496 0.2237 0.1029 0.0098 -0.0743 74 LEU A CD2 161 N N . TYR A 82 ? 0.2873 0.2238 0.3209 0.0763 -0.0144 0.0129 75 TYR A N 162 C CA . TYR A 82 ? 0.3069 0.2304 0.3390 0.0790 -0.0050 0.0160 75 TYR A CA 163 C C . TYR A 82 ? 0.3081 0.2376 0.3350 0.0732 0.0008 0.0114 75 TYR A C 164 O O . TYR A 82 ? 0.3092 0.2516 0.3502 0.0647 0.0162 0.0022 75 TYR A O 165 C CB . TYR A 82 ? 0.3097 0.2239 0.3478 0.0865 -0.0115 0.0183 75 TYR A CB 166 C CG . TYR A 82 ? 0.3468 0.2238 0.3487 0.0906 -0.0104 0.0061 75 TYR A CG 167 C CD1 . TYR A 82 ? 0.3642 0.2335 0.3837 0.1101 -0.0030 0.0030 75 TYR A CD1 168 C CD2 . TYR A 82 ? 0.3632 0.2540 0.3956 0.1055 -0.0115 -0.0093 75 TYR A CD2 169 C CE1 . TYR A 82 ? 0.4045 0.2470 0.4193 0.0866 0.0050 -0.0250 75 TYR A CE1 170 C CE2 . TYR A 82 ? 0.4326 0.2584 0.4455 0.0830 -0.0019 -0.0024 75 TYR A CE2 171 C CZ . TYR A 82 ? 0.4586 0.2757 0.4445 0.0830 0.0007 -0.0314 75 TYR A CZ 172 O OH . TYR A 82 ? 0.5517 0.2791 0.5106 0.0317 -0.0327 -0.0185 75 TYR A OH 173 N N . ASN A 83 ? 0.3068 0.2282 0.3332 0.0806 0.0055 0.0128 76 ASN A N 174 C CA . ASN A 83 ? 0.3115 0.2288 0.3289 0.0679 0.0162 0.0107 76 ASN A CA 175 C C . ASN A 83 ? 0.3076 0.2194 0.3206 0.0696 0.0169 0.0092 76 ASN A C 176 O O . ASN A 83 ? 0.3092 0.2197 0.3326 0.0688 0.0183 0.0154 76 ASN A O 177 C CB . ASN A 83 ? 0.3244 0.2462 0.3367 0.0666 0.0149 -0.0028 76 ASN A CB 178 C CG . ASN A 83 ? 0.3455 0.2639 0.3536 0.0585 0.0377 -0.0015 76 ASN A CG 179 O OD1 . ASN A 83 ? 0.3612 0.2358 0.3527 0.0358 0.0444 -0.0004 76 ASN A OD1 180 N ND2 . ASN A 83 ? 0.4201 0.2595 0.3633 0.0848 0.0436 0.0252 76 ASN A ND2 181 N N . PHE A 84 ? 0.2888 0.1922 0.2943 0.0737 0.0301 0.0047 77 PHE A N 182 C CA . PHE A 84 ? 0.2906 0.1906 0.2828 0.0613 0.0313 0.0001 77 PHE A CA 183 C C . PHE A 84 ? 0.2860 0.1907 0.2925 0.0563 0.0230 -0.0090 77 PHE A C 184 O O . PHE A 84 ? 0.2700 0.1924 0.2785 0.0633 0.0273 -0.0131 77 PHE A O 185 C CB . PHE A 84 ? 0.2992 0.1783 0.2702 0.0611 0.0373 0.0108 77 PHE A CB 186 C CG . PHE A 84 ? 0.2952 0.1838 0.3057 0.0710 0.0335 0.0257 77 PHE A CG 187 C CD1 . PHE A 84 ? 0.2663 0.2287 0.2760 0.0654 0.0565 0.0174 77 PHE A CD1 188 C CD2 . PHE A 84 ? 0.2831 0.2199 0.2743 0.0558 -0.0002 -0.0053 77 PHE A CD2 189 C CE1 . PHE A 84 ? 0.3425 0.2268 0.2584 0.0427 0.0392 0.0127 77 PHE A CE1 190 C CE2 . PHE A 84 ? 0.3035 0.2277 0.2882 0.0557 0.0152 0.0382 77 PHE A CE2 191 C CZ . PHE A 84 ? 0.2891 0.2264 0.2867 0.0508 0.0196 0.0435 77 PHE A CZ 192 N N . THR A 85 ? 0.2655 0.1956 0.2935 0.0474 0.0165 -0.0236 78 THR A N 193 C CA . THR A 85 ? 0.2761 0.2052 0.3220 0.0468 0.0067 -0.0307 78 THR A CA 194 C C . THR A 85 ? 0.2895 0.2200 0.3359 0.0574 -0.0026 -0.0253 78 THR A C 195 O O . THR A 85 ? 0.2739 0.2376 0.3426 0.0620 -0.0086 -0.0267 78 THR A O 196 C CB . THR A 85 ? 0.2769 0.1915 0.3182 0.0440 0.0011 -0.0213 78 THR A CB 197 O OG1 . THR A 85 ? 0.2416 0.1833 0.3259 0.0590 -0.0032 -0.0420 78 THR A OG1 198 C CG2 . THR A 85 ? 0.2388 0.1545 0.2596 0.0511 0.0094 -0.0679 78 THR A CG2 199 N N . GLN A 86 ? 0.3037 0.2259 0.3480 0.0453 -0.0004 -0.0165 79 GLN A N 200 C CA . GLN A 86 ? 0.3273 0.2530 0.3812 0.0536 0.0091 -0.0171 79 GLN A CA 201 C C . GLN A 86 ? 0.3342 0.2507 0.3810 0.0509 0.0118 -0.0143 79 GLN A C 202 O O . GLN A 86 ? 0.3347 0.2441 0.3811 0.0506 0.0129 -0.0105 79 GLN A O 203 C CB . GLN A 86 ? 0.3370 0.2627 0.3805 0.0571 0.0134 -0.0102 79 GLN A CB 204 C CG . GLN A 86 ? 0.3440 0.3059 0.4032 0.0818 0.0044 -0.0213 79 GLN A CG 205 C CD . GLN A 86 ? 0.3902 0.3546 0.4519 0.0929 0.0026 -0.0171 79 GLN A CD 206 O OE1 . GLN A 86 ? 0.3774 0.3500 0.5366 0.1096 -0.0122 -0.0127 79 GLN A OE1 207 N NE2 . GLN A 86 ? 0.4266 0.3689 0.3884 0.0999 -0.0171 -0.0239 79 GLN A NE2 208 N N . ILE A 87 ? 0.3324 0.2435 0.3879 0.0418 0.0098 -0.0159 80 ILE A N 209 C CA . ILE A 87 ? 0.3313 0.2470 0.4011 0.0360 0.0094 -0.0133 80 ILE A CA 210 C C . ILE A 87 ? 0.3075 0.2336 0.3797 0.0331 0.0193 -0.0204 80 ILE A C 211 O O . ILE A 87 ? 0.3146 0.2414 0.3846 0.0296 0.0152 -0.0100 80 ILE A O 212 C CB . ILE A 87 ? 0.3332 0.2465 0.4090 0.0243 0.0093 -0.0110 80 ILE A CB 213 C CG1 . ILE A 87 ? 0.3353 0.2762 0.4262 0.0162 0.0247 -0.0096 80 ILE A CG1 214 C CG2 . ILE A 87 ? 0.3793 0.2736 0.4327 0.0268 -0.0266 0.0057 80 ILE A CG2 215 C CD1 . ILE A 87 ? 0.3390 0.3672 0.4534 -0.0183 -0.0393 -0.0271 80 ILE A CD1 216 N N . PRO A 88 ? 0.2890 0.2276 0.3629 0.0352 0.0226 -0.0292 81 PRO A N 217 C CA . PRO A 88 ? 0.2786 0.2245 0.3520 0.0425 0.0234 -0.0332 81 PRO A CA 218 C C . PRO A 88 ? 0.2702 0.2269 0.3472 0.0399 0.0246 -0.0294 81 PRO A C 219 O O . PRO A 88 ? 0.2756 0.2212 0.3732 0.0460 0.0205 -0.0309 81 PRO A O 220 C CB . PRO A 88 ? 0.2882 0.2313 0.3421 0.0401 0.0284 -0.0321 81 PRO A CB 221 C CG . PRO A 88 ? 0.2882 0.2247 0.3506 0.0557 0.0152 -0.0315 81 PRO A CG 222 C CD . PRO A 88 ? 0.2842 0.2303 0.3557 0.0358 0.0284 -0.0334 81 PRO A CD 223 N N . HIS A 89 ? 0.2316 0.1980 0.3041 0.0364 0.0212 -0.0377 82 HIS A N 224 C CA . HIS A 89 ? 0.2541 0.2086 0.2965 0.0333 0.0166 -0.0264 82 HIS A CA 225 C C . HIS A 89 ? 0.2300 0.2063 0.2742 0.0300 0.0139 -0.0248 82 HIS A C 226 O O . HIS A 89 ? 0.2470 0.1794 0.2554 0.0321 0.0135 -0.0054 82 HIS A O 227 C CB . HIS A 89 ? 0.2455 0.2227 0.2896 0.0281 0.0152 -0.0220 82 HIS A CB 228 C CG . HIS A 89 ? 0.2613 0.2291 0.3162 0.0279 0.0181 -0.0070 82 HIS A CG 229 N ND1 . HIS A 89 ? 0.2327 0.2289 0.2825 0.0312 0.0269 -0.0103 82 HIS A ND1 230 C CD2 . HIS A 89 ? 0.2290 0.2618 0.2994 0.0341 0.0334 -0.0167 82 HIS A CD2 231 C CE1 . HIS A 89 ? 0.2620 0.2406 0.3253 0.0322 0.0466 -0.0240 82 HIS A CE1 232 N NE2 . HIS A 89 ? 0.2626 0.2088 0.2979 0.0081 0.0437 -0.0104 82 HIS A NE2 233 N N . LEU A 90 ? 0.2094 0.1996 0.2553 0.0198 0.0176 -0.0293 83 LEU A N 234 C CA . LEU A 90 ? 0.2315 0.2247 0.2510 0.0100 0.0124 -0.0427 83 LEU A CA 235 C C . LEU A 90 ? 0.2284 0.2163 0.2527 0.0078 0.0025 -0.0385 83 LEU A C 236 O O . LEU A 90 ? 0.2494 0.2277 0.2471 0.0014 0.0022 -0.0141 83 LEU A O 237 C CB . LEU A 90 ? 0.2039 0.2273 0.2229 -0.0043 0.0208 -0.0507 83 LEU A CB 238 C CG . LEU A 90 ? 0.2290 0.2315 0.2345 -0.0404 0.0083 -0.0850 83 LEU A CG 239 C CD1 . LEU A 90 ? 0.2519 0.1501 0.1906 -0.0672 0.0310 -0.0748 83 LEU A CD1 240 C CD2 . LEU A 90 ? 0.2523 0.2365 0.1534 -0.0388 -0.0126 -0.0988 83 LEU A CD2 241 N N . ALA A 91 ? 0.2307 0.1938 0.2564 0.0119 0.0006 -0.0423 84 ALA A N 242 C CA . ALA A 91 ? 0.2048 0.1926 0.2740 0.0063 0.0101 -0.0514 84 ALA A CA 243 C C . ALA A 91 ? 0.2256 0.2057 0.2867 0.0092 0.0123 -0.0497 84 ALA A C 244 O O . ALA A 91 ? 0.2193 0.2090 0.2860 0.0081 0.0091 -0.0473 84 ALA A O 245 C CB . ALA A 91 ? 0.1920 0.1710 0.2704 0.0102 0.0197 -0.0486 84 ALA A CB 246 N N . GLY A 92 ? 0.2171 0.2097 0.3047 0.0070 0.0112 -0.0397 85 GLY A N 247 C CA . GLY A 92 ? 0.2331 0.2074 0.3095 -0.0021 0.0068 -0.0394 85 GLY A CA 248 C C . GLY A 92 ? 0.2525 0.2365 0.3427 -0.0004 0.0059 -0.0374 85 GLY A C 249 O O . GLY A 92 ? 0.2740 0.2461 0.3612 -0.0144 -0.0124 -0.0434 85 GLY A O 250 N N . THR A 93 ? 0.2408 0.2263 0.3313 0.0154 0.0143 -0.0299 86 THR A N 251 C CA . THR A 93 ? 0.2443 0.2164 0.3519 0.0091 0.0261 -0.0320 86 THR A CA 252 C C . THR A 93 ? 0.2486 0.2081 0.3587 0.0069 0.0184 -0.0317 86 THR A C 253 O O . THR A 93 ? 0.2436 0.1619 0.3594 0.0013 0.0145 -0.0263 86 THR A O 254 C CB . THR A 93 ? 0.2488 0.2297 0.3524 0.0162 0.0317 -0.0387 86 THR A CB 255 O OG1 . THR A 93 ? 0.2314 0.2193 0.3547 0.0199 0.0329 -0.0338 86 THR A OG1 256 C CG2 . THR A 93 ? 0.2394 0.2119 0.3298 0.0094 0.0677 -0.0422 86 THR A CG2 257 N N . GLU A 94 ? 0.2594 0.1916 0.3748 -0.0058 0.0074 -0.0243 87 GLU A N 258 C CA . GLU A 94 ? 0.2914 0.2205 0.3911 -0.0039 0.0220 -0.0302 87 GLU A CA 259 C C . GLU A 94 ? 0.2957 0.2157 0.3894 0.0024 0.0289 -0.0284 87 GLU A C 260 O O . GLU A 94 ? 0.3146 0.2180 0.3909 0.0049 0.0289 -0.0400 87 GLU A O 261 C CB . GLU A 94 ? 0.3104 0.2159 0.4158 -0.0293 0.0174 -0.0259 87 GLU A CB 262 C CG . GLU A 94 ? 0.3780 0.3207 0.4638 -0.0273 0.0210 -0.0122 87 GLU A CG 263 C CD . GLU A 94 ? 0.4004 0.3829 0.5430 -0.0347 0.0363 -0.0296 87 GLU A CD 264 O OE1 . GLU A 94 ? 0.4328 0.4506 0.5735 -0.0688 0.0365 -0.0051 87 GLU A OE1 265 O OE2 . GLU A 94 ? 0.4098 0.4200 0.5794 -0.0344 0.0295 -0.0266 87 GLU A OE2 266 N N . GLN A 95 ? 0.2822 0.2144 0.3819 0.0137 0.0236 -0.0233 88 GLN A N 267 C CA A GLN A 95 ? 0.2866 0.2162 0.3719 0.0229 0.0273 -0.0257 88 GLN A CA 268 C CA C GLN A 95 ? 0.2914 0.2158 0.3775 0.0191 0.0245 -0.0247 88 GLN A CA 269 C C . GLN A 95 ? 0.2885 0.2154 0.3688 0.0217 0.0259 -0.0224 88 GLN A C 270 O O . GLN A 95 ? 0.2702 0.2026 0.3538 0.0257 0.0081 -0.0063 88 GLN A O 271 C CB A GLN A 95 ? 0.2877 0.2176 0.3704 0.0297 0.0250 -0.0327 88 GLN A CB 272 C CB C GLN A 95 ? 0.2987 0.2226 0.3831 0.0248 0.0210 -0.0334 88 GLN A CB 273 C CG A GLN A 95 ? 0.2927 0.2348 0.3630 0.0471 0.0327 -0.0460 88 GLN A CG 274 C CG C GLN A 95 ? 0.3234 0.2269 0.4008 0.0228 0.0123 -0.0409 88 GLN A CG 275 C CD A GLN A 95 ? 0.2845 0.2488 0.3582 0.0791 0.0224 -0.0405 88 GLN A CD 276 C CD C GLN A 95 ? 0.3912 0.2633 0.4116 0.0201 0.0090 -0.0568 88 GLN A CD 277 O OE1 A GLN A 95 ? 0.2309 0.1766 0.2553 0.0701 0.0298 -0.0487 88 GLN A OE1 278 O OE1 C GLN A 95 ? 0.3253 0.2870 0.4244 0.0540 -0.0221 -0.0931 88 GLN A OE1 279 N NE2 A GLN A 95 ? 0.3687 0.3231 0.3792 0.0482 0.0472 -0.0255 88 GLN A NE2 280 N NE2 C GLN A 95 ? 0.4528 0.2365 0.4263 0.0013 -0.0049 -0.0370 88 GLN A NE2 281 N N . ASN A 96 ? 0.2634 0.2048 0.3486 0.0279 0.0279 -0.0106 89 ASN A N 282 C CA . ASN A 96 ? 0.2521 0.2159 0.3383 0.0277 0.0280 -0.0153 89 ASN A CA 283 C C . ASN A 96 ? 0.2559 0.2345 0.3407 0.0115 0.0327 -0.0156 89 ASN A C 284 O O . ASN A 96 ? 0.2543 0.2471 0.3334 0.0131 0.0132 -0.0315 89 ASN A O 285 C CB . ASN A 96 ? 0.2390 0.2091 0.3387 0.0178 0.0452 -0.0152 89 ASN A CB 286 C CG . ASN A 96 ? 0.2632 0.2245 0.3162 0.0397 0.0313 -0.0157 89 ASN A CG 287 O OD1 . ASN A 96 ? 0.2666 0.2259 0.3018 0.0218 0.0183 -0.0219 89 ASN A OD1 288 N ND2 . ASN A 96 ? 0.2534 0.1909 0.2919 0.0486 0.0698 -0.0155 89 ASN A ND2 289 N N . PHE A 97 ? 0.2462 0.2169 0.3364 0.0076 0.0256 -0.0076 90 PHE A N 290 C CA . PHE A 97 ? 0.2445 0.2298 0.3488 0.0040 0.0348 0.0001 90 PHE A CA 291 C C . PHE A 97 ? 0.2504 0.2291 0.3612 0.0055 0.0367 0.0004 90 PHE A C 292 O O . PHE A 97 ? 0.2202 0.2206 0.3299 -0.0014 0.0428 -0.0136 90 PHE A O 293 C CB A PHE A 97 ? 0.2573 0.2415 0.3647 0.0059 0.0419 -0.0051 90 PHE A CB 294 C CB B PHE A 97 ? 0.2480 0.2284 0.3507 0.0060 0.0364 -0.0006 90 PHE A CB 295 C CG A PHE A 97 ? 0.2702 0.2514 0.3917 0.0030 0.0582 0.0059 90 PHE A CG 296 C CG B PHE A 97 ? 0.2375 0.2162 0.3499 -0.0008 0.0315 0.0090 90 PHE A CG 297 C CD1 A PHE A 97 ? 0.2894 0.2460 0.3982 -0.0082 0.0605 0.0067 90 PHE A CD1 298 C CD1 B PHE A 97 ? 0.2478 0.2048 0.3453 -0.0078 0.0335 0.0154 90 PHE A CD1 299 C CD2 A PHE A 97 ? 0.3066 0.2792 0.4485 -0.0051 0.0848 -0.0041 90 PHE A CD2 300 C CD2 B PHE A 97 ? 0.2320 0.2069 0.3370 0.0129 0.0199 0.0234 90 PHE A CD2 301 C CE1 A PHE A 97 ? 0.3027 0.2538 0.3810 0.0041 0.0717 0.0266 90 PHE A CE1 302 C CE1 B PHE A 97 ? 0.2519 0.2171 0.3272 -0.0067 0.0309 0.0125 90 PHE A CE1 303 C CE2 A PHE A 97 ? 0.3289 0.3172 0.4435 0.0057 0.0943 -0.0057 90 PHE A CE2 304 C CE2 B PHE A 97 ? 0.2297 0.2096 0.3289 0.0199 0.0273 0.0289 90 PHE A CE2 305 C CZ A PHE A 97 ? 0.3102 0.3089 0.4442 0.0027 0.0768 -0.0094 90 PHE A CZ 306 C CZ B PHE A 97 ? 0.2631 0.2018 0.3399 0.0060 0.0244 0.0151 90 PHE A CZ 307 N N A GLN A 98 ? 0.2540 0.2134 0.3605 0.0001 0.0340 -0.0021 91 GLN A N 308 N N B GLN A 98 ? 0.2554 0.2145 0.3586 0.0034 0.0352 -0.0017 91 GLN A N 309 C CA A GLN A 98 ? 0.2807 0.2283 0.3744 0.0037 0.0378 0.0035 91 GLN A CA 310 C CA B GLN A 98 ? 0.2781 0.2198 0.3710 0.0073 0.0373 0.0015 91 GLN A CA 311 C C A GLN A 98 ? 0.2815 0.2197 0.3596 0.0144 0.0396 0.0015 91 GLN A C 312 C C B GLN A 98 ? 0.2796 0.2161 0.3588 0.0154 0.0389 0.0016 91 GLN A C 313 O O A GLN A 98 ? 0.2811 0.2173 0.3674 0.0185 0.0420 -0.0031 91 GLN A O 314 O O B GLN A 98 ? 0.2797 0.2147 0.3629 0.0174 0.0407 -0.0019 91 GLN A O 315 C CB A GLN A 98 ? 0.2948 0.2308 0.3857 0.0026 0.0392 0.0059 91 GLN A CB 316 C CB B GLN A 98 ? 0.2878 0.2183 0.3827 0.0078 0.0373 0.0034 91 GLN A CB 317 C CG A GLN A 98 ? 0.3369 0.2869 0.4376 -0.0274 0.0351 0.0256 91 GLN A CG 318 C CG B GLN A 98 ? 0.3275 0.2403 0.4192 -0.0145 0.0387 0.0114 91 GLN A CG 319 C CD A GLN A 98 ? 0.3769 0.3672 0.4971 -0.0326 0.0551 0.0546 91 GLN A CD 320 C CD B GLN A 98 ? 0.3837 0.2391 0.4759 -0.0159 0.0465 0.0160 91 GLN A CD 321 O OE1 A GLN A 98 ? 0.4057 0.3994 0.5168 -0.0504 0.0240 0.0570 91 GLN A OE1 322 O OE1 B GLN A 98 ? 0.4183 0.2378 0.5301 0.0002 0.0620 0.0251 91 GLN A OE1 323 N NE2 A GLN A 98 ? 0.4128 0.3661 0.4979 -0.0481 0.0472 0.0866 91 GLN A NE2 324 N NE2 B GLN A 98 ? 0.4198 0.2700 0.4848 -0.0396 0.0458 0.0284 91 GLN A NE2 325 N N . LEU A 99 ? 0.2796 0.2065 0.3532 0.0135 0.0369 -0.0003 92 LEU A N 326 C CA . LEU A 99 ? 0.2792 0.2060 0.3370 0.0239 0.0424 0.0036 92 LEU A CA 327 C C . LEU A 99 ? 0.2722 0.2145 0.3340 0.0293 0.0489 0.0050 92 LEU A C 328 O O . LEU A 99 ? 0.2968 0.2125 0.3282 0.0383 0.0491 0.0042 92 LEU A O 329 C CB . LEU A 99 ? 0.2518 0.2008 0.3158 0.0369 0.0519 -0.0107 92 LEU A CB 330 C CG . LEU A 99 ? 0.2704 0.2042 0.3009 0.0380 0.0366 0.0200 92 LEU A CG 331 C CD1 . LEU A 99 ? 0.2759 0.2300 0.2629 0.0831 0.0044 0.0251 92 LEU A CD1 332 C CD2 . LEU A 99 ? 0.2970 0.1828 0.2310 -0.0277 0.0486 -0.0294 92 LEU A CD2 333 N N . ALA A 100 ? 0.2606 0.2050 0.3239 0.0237 0.0385 0.0100 93 ALA A N 334 C CA . ALA A 100 ? 0.2699 0.2224 0.3257 0.0325 0.0456 0.0187 93 ALA A CA 335 C C . ALA A 100 ? 0.2791 0.2292 0.3382 0.0330 0.0368 0.0238 93 ALA A C 336 O O . ALA A 100 ? 0.2691 0.2400 0.3426 0.0331 0.0321 0.0232 93 ALA A O 337 C CB . ALA A 100 ? 0.2623 0.2173 0.2979 0.0280 0.0348 0.0086 93 ALA A CB 338 N N . LYS A 101 ? 0.2780 0.2227 0.3522 0.0286 0.0332 0.0236 94 LYS A N 339 C CA . LYS A 101 ? 0.2863 0.2457 0.3676 0.0300 0.0295 0.0280 94 LYS A CA 340 C C . LYS A 101 ? 0.2980 0.2441 0.3687 0.0398 0.0387 0.0249 94 LYS A C 341 O O . LYS A 101 ? 0.2942 0.2583 0.3716 0.0421 0.0367 0.0223 94 LYS A O 342 C CB . LYS A 101 ? 0.2892 0.2465 0.3874 0.0236 0.0241 0.0295 94 LYS A CB 343 C CG . LYS A 101 ? 0.3168 0.3034 0.4393 -0.0162 -0.0023 0.0389 94 LYS A CG 344 C CD . LYS A 101 ? 0.3502 0.3763 0.5413 -0.0206 -0.0319 0.0210 94 LYS A CD 345 C CE . LYS A 101 ? 0.3498 0.3472 0.5231 -0.0040 -0.0114 0.0304 94 LYS A CE 346 N NZ . LYS A 101 ? 0.3581 0.3410 0.5312 0.0002 -0.0133 0.0119 94 LYS A NZ 347 N N . GLN A 102 ? 0.2923 0.2515 0.3650 0.0586 0.0370 0.0245 95 GLN A N 348 C CA . GLN A 102 ? 0.3008 0.2434 0.3466 0.0600 0.0410 0.0220 95 GLN A CA 349 C C . GLN A 102 ? 0.3016 0.2456 0.3395 0.0576 0.0433 0.0284 95 GLN A C 350 O O . GLN A 102 ? 0.2991 0.2453 0.3215 0.0441 0.0392 0.0293 95 GLN A O 351 C CB . GLN A 102 ? 0.2944 0.2407 0.3440 0.0768 0.0321 0.0264 95 GLN A CB 352 C CG . GLN A 102 ? 0.3178 0.2489 0.3644 0.0829 0.0428 0.0029 95 GLN A CG 353 C CD . GLN A 102 ? 0.3126 0.2851 0.3565 0.0561 0.0537 0.0201 95 GLN A CD 354 O OE1 . GLN A 102 ? 0.3564 0.2347 0.3862 0.0586 0.0526 0.0233 95 GLN A OE1 355 N NE2 . GLN A 102 ? 0.3149 0.2722 0.3181 0.0500 0.0286 0.0183 95 GLN A NE2 356 N N . ILE A 103 ? 0.3134 0.2207 0.3429 0.0598 0.0460 0.0366 96 ILE A N 357 C CA . ILE A 103 ? 0.3215 0.2305 0.3313 0.0597 0.0388 0.0231 96 ILE A CA 358 C C . ILE A 103 ? 0.3203 0.2381 0.3322 0.0559 0.0446 0.0427 96 ILE A C 359 O O . ILE A 103 ? 0.3121 0.2220 0.3385 0.0644 0.0352 0.0487 96 ILE A O 360 C CB . ILE A 103 ? 0.3306 0.2213 0.3292 0.0484 0.0514 0.0235 96 ILE A CB 361 C CG1 . ILE A 103 ? 0.3641 0.2422 0.3432 0.0751 0.0124 -0.0167 96 ILE A CG1 362 C CG2 . ILE A 103 ? 0.3385 0.2263 0.3570 0.0658 0.0316 -0.0061 96 ILE A CG2 363 C CD1 . ILE A 103 ? 0.3867 0.2893 0.3404 0.0628 0.0175 0.0194 96 ILE A CD1 364 N N . GLN A 104 ? 0.3220 0.2485 0.3341 0.0555 0.0499 0.0494 97 GLN A N 365 C CA . GLN A 104 ? 0.3133 0.2689 0.3348 0.0578 0.0530 0.0590 97 GLN A CA 366 C C . GLN A 104 ? 0.3156 0.2646 0.3380 0.0535 0.0470 0.0616 97 GLN A C 367 O O . GLN A 104 ? 0.2953 0.2807 0.3229 0.0454 0.0543 0.0734 97 GLN A O 368 C CB . GLN A 104 ? 0.3198 0.2728 0.3377 0.0585 0.0478 0.0502 97 GLN A CB 369 C CG . GLN A 104 ? 0.2922 0.2825 0.3344 0.0571 0.0708 0.0523 97 GLN A CG 370 C CD . GLN A 104 ? 0.2782 0.2974 0.3622 0.0468 0.0845 0.0418 97 GLN A CD 371 O OE1 . GLN A 104 ? 0.2591 0.3199 0.4009 0.0474 0.0626 0.0368 97 GLN A OE1 372 N NE2 . GLN A 104 ? 0.1855 0.3026 0.3692 0.0534 0.0708 0.0312 97 GLN A NE2 373 N N . SER A 105 ? 0.3237 0.2513 0.3390 0.0513 0.0376 0.0668 98 SER A N 374 C CA . SER A 105 ? 0.3465 0.2500 0.3430 0.0448 0.0466 0.0625 98 SER A CA 375 C C . SER A 105 ? 0.3529 0.2581 0.3402 0.0554 0.0491 0.0605 98 SER A C 376 O O . SER A 105 ? 0.3446 0.2821 0.3333 0.0528 0.0451 0.0713 98 SER A O 377 C CB . SER A 105 ? 0.3512 0.2409 0.3366 0.0371 0.0429 0.0578 98 SER A CB 378 O OG A SER A 105 ? 0.3283 0.1894 0.3369 0.0615 0.0411 0.0728 98 SER A OG 379 O OG B SER A 105 ? 0.3767 0.2500 0.3850 0.0139 0.0563 0.0379 98 SER A OG 380 N N . GLN A 106 ? 0.3395 0.2452 0.3336 0.0624 0.0562 0.0639 99 GLN A N 381 C CA . GLN A 106 ? 0.3513 0.2529 0.3178 0.0771 0.0612 0.0571 99 GLN A CA 382 C C . GLN A 106 ? 0.3474 0.2495 0.2977 0.0825 0.0655 0.0597 99 GLN A C 383 O O . GLN A 106 ? 0.3623 0.2645 0.2927 0.0863 0.0697 0.0615 99 GLN A O 384 C CB . GLN A 106 ? 0.3400 0.2407 0.3213 0.0940 0.0598 0.0596 99 GLN A CB 385 C CG . GLN A 106 ? 0.3662 0.2722 0.3609 0.0821 0.0487 0.0264 99 GLN A CG 386 C CD . GLN A 106 ? 0.4165 0.3111 0.4022 0.1032 0.0431 0.0498 99 GLN A CD 387 O OE1 . GLN A 106 ? 0.4141 0.2921 0.4070 0.0556 0.0925 0.0465 99 GLN A OE1 388 N NE2 . GLN A 106 ? 0.4283 0.3883 0.4769 0.1400 0.0099 0.0896 99 GLN A NE2 389 N N . TRP A 107 ? 0.3517 0.2529 0.2754 0.0847 0.0692 0.0667 100 TRP A N 390 C CA . TRP A 107 ? 0.3677 0.2465 0.2760 0.0748 0.0589 0.0690 100 TRP A CA 391 C C . TRP A 107 ? 0.3953 0.2585 0.2846 0.0824 0.0597 0.0838 100 TRP A C 392 O O . TRP A 107 ? 0.4086 0.2531 0.2637 0.0802 0.0580 0.0854 100 TRP A O 393 C CB . TRP A 107 ? 0.3472 0.2454 0.2614 0.0702 0.0556 0.0745 100 TRP A CB 394 C CG . TRP A 107 ? 0.3181 0.2328 0.2293 0.0751 0.0413 0.0375 100 TRP A CG 395 C CD1 . TRP A 107 ? 0.3117 0.2285 0.2450 0.0564 0.0457 0.0188 100 TRP A CD1 396 C CD2 . TRP A 107 ? 0.2775 0.2068 0.2428 0.0475 0.0428 0.0211 100 TRP A CD2 397 N NE1 . TRP A 107 ? 0.2954 0.2463 0.2128 0.0626 0.0339 0.0214 100 TRP A NE1 398 C CE2 . TRP A 107 ? 0.3053 0.1954 0.2390 0.0693 0.0397 0.0056 100 TRP A CE2 399 C CE3 . TRP A 107 ? 0.2653 0.1894 0.2350 0.0577 0.0419 0.0166 100 TRP A CE3 400 C CZ2 . TRP A 107 ? 0.2845 0.2260 0.2400 0.0474 0.0427 0.0069 100 TRP A CZ2 401 C CZ3 . TRP A 107 ? 0.2673 0.1998 0.2620 0.0295 0.0392 0.0110 100 TRP A CZ3 402 C CH2 . TRP A 107 ? 0.2982 0.2040 0.2934 0.0742 0.0530 0.0040 100 TRP A CH2 403 N N . LYS A 108 ? 0.4149 0.2700 0.3110 0.0782 0.0592 0.0969 101 LYS A N 404 C CA . LYS A 108 ? 0.4391 0.3062 0.3529 0.0884 0.0666 0.0884 101 LYS A CA 405 C C . LYS A 108 ? 0.4420 0.3022 0.3457 0.0922 0.0704 0.0936 101 LYS A C 406 O O . LYS A 108 ? 0.4463 0.3152 0.3566 0.0918 0.0727 0.1036 101 LYS A O 407 C CB . LYS A 108 ? 0.4473 0.3202 0.3667 0.0880 0.0572 0.0897 101 LYS A CB 408 C CG . LYS A 108 ? 0.4804 0.3980 0.4364 0.0811 0.0441 0.0872 101 LYS A CG 409 C CD . LYS A 108 ? 0.5059 0.4830 0.5271 0.0274 0.0424 0.0813 101 LYS A CD 410 C CE . LYS A 108 ? 0.5176 0.5477 0.4934 0.0219 0.0384 0.1097 101 LYS A CE 411 N NZ . LYS A 108 ? 0.5683 0.6106 0.5066 -0.0001 0.0262 0.0948 101 LYS A NZ 412 N N A GLU A 109 ? 0.4475 0.3011 0.3550 0.0961 0.0709 0.0904 102 GLU A N 413 N N B GLU A 109 ? 0.4537 0.3083 0.3560 0.0948 0.0741 0.0906 102 GLU A N 414 C CA A GLU A 109 ? 0.4527 0.3053 0.3488 0.1041 0.0702 0.0820 102 GLU A CA 415 C CA B GLU A 109 ? 0.4642 0.3192 0.3489 0.0990 0.0775 0.0864 102 GLU A CA 416 C C A GLU A 109 ? 0.4510 0.2952 0.3321 0.1041 0.0762 0.0801 102 GLU A C 417 C C B GLU A 109 ? 0.4580 0.3035 0.3327 0.1025 0.0799 0.0819 102 GLU A C 418 O O A GLU A 109 ? 0.4459 0.2876 0.3136 0.0961 0.0848 0.0855 102 GLU A O 419 O O B GLU A 109 ? 0.4521 0.2974 0.3140 0.0947 0.0878 0.0884 102 GLU A O 420 C CB A GLU A 109 ? 0.4613 0.2963 0.3704 0.1049 0.0677 0.0771 102 GLU A CB 421 C CB B GLU A 109 ? 0.4793 0.3209 0.3652 0.0983 0.0792 0.0786 102 GLU A CB 422 C CG A GLU A 109 ? 0.4767 0.3260 0.4092 0.1192 0.0487 0.0632 102 GLU A CG 423 C CG B GLU A 109 ? 0.5231 0.3923 0.4216 0.0875 0.0865 0.0934 102 GLU A CG 424 C CD A GLU A 109 ? 0.5006 0.3026 0.4847 0.1499 0.0193 0.0385 102 GLU A CD 425 C CD B GLU A 109 ? 0.5769 0.4716 0.4599 0.1008 0.0897 0.0846 102 GLU A CD 426 O OE1 A GLU A 109 ? 0.4928 0.2505 0.5118 0.1560 0.0081 0.0218 102 GLU A OE1 427 O OE1 B GLU A 109 ? 0.5786 0.4791 0.5199 0.1206 0.0667 0.0752 102 GLU A OE1 428 O OE2 A GLU A 109 ? 0.5098 0.2922 0.5118 0.1674 0.0093 0.0457 102 GLU A OE2 429 O OE2 B GLU A 109 ? 0.5787 0.5105 0.4968 0.0823 0.1047 0.0917 102 GLU A OE2 430 N N . PHE A 110 ? 0.4465 0.2949 0.3066 0.1047 0.0835 0.0808 103 PHE A N 431 C CA . PHE A 110 ? 0.4480 0.3071 0.3043 0.1087 0.0789 0.0737 103 PHE A CA 432 C C . PHE A 110 ? 0.4508 0.3118 0.2880 0.1113 0.0727 0.0719 103 PHE A C 433 O O . PHE A 110 ? 0.4650 0.3256 0.2901 0.1154 0.0701 0.0724 103 PHE A O 434 C CB . PHE A 110 ? 0.4368 0.3012 0.2906 0.1090 0.0794 0.0726 103 PHE A CB 435 C CG . PHE A 110 ? 0.4072 0.3380 0.2994 0.0969 0.0683 0.0598 103 PHE A CG 436 C CD1 . PHE A 110 ? 0.3656 0.3236 0.2971 0.1146 0.0642 0.0406 103 PHE A CD1 437 C CD2 . PHE A 110 ? 0.3709 0.3440 0.2610 0.0914 0.0286 0.0405 103 PHE A CD2 438 C CE1 . PHE A 110 ? 0.4087 0.3895 0.2991 0.1027 0.0460 0.0288 103 PHE A CE1 439 C CE2 . PHE A 110 ? 0.3837 0.3509 0.3170 0.0783 0.0405 0.0332 103 PHE A CE2 440 C CZ . PHE A 110 ? 0.3618 0.3511 0.3113 0.0956 0.0446 0.0458 103 PHE A CZ 441 N N . GLY A 111 ? 0.4463 0.3029 0.2854 0.1172 0.0700 0.0745 104 GLY A N 442 C CA . GLY A 111 ? 0.4425 0.2908 0.2727 0.1190 0.0605 0.0728 104 GLY A CA 443 C C . GLY A 111 ? 0.4353 0.3042 0.2820 0.1165 0.0639 0.0598 104 GLY A C 444 O O . GLY A 111 ? 0.4374 0.3274 0.2894 0.1257 0.0747 0.0462 104 GLY A O 445 N N . LEU A 112 ? 0.4193 0.2968 0.2582 0.1100 0.0712 0.0594 105 LEU A N 446 C CA . LEU A 112 ? 0.4000 0.2949 0.2576 0.1014 0.0698 0.0618 105 LEU A CA 447 C C . LEU A 112 ? 0.4023 0.3023 0.2706 0.0985 0.0694 0.0652 105 LEU A C 448 O O . LEU A 112 ? 0.3970 0.3043 0.2874 0.1013 0.0710 0.0600 105 LEU A O 449 C CB . LEU A 112 ? 0.3940 0.2915 0.2529 0.0952 0.0731 0.0669 105 LEU A CB 450 C CG . LEU A 112 ? 0.3610 0.2982 0.2049 0.0873 0.0719 0.0591 105 LEU A CG 451 C CD1 . LEU A 112 ? 0.3119 0.2759 0.1886 0.0876 0.0375 0.0634 105 LEU A CD1 452 C CD2 . LEU A 112 ? 0.3501 0.2818 0.1638 0.1084 0.0907 0.0570 105 LEU A CD2 453 N N . ASP A 113 ? 0.3962 0.3060 0.2713 0.0943 0.0677 0.0635 106 ASP A N 454 C CA . ASP A 113 ? 0.4169 0.3323 0.2886 0.0849 0.0730 0.0608 106 ASP A CA 455 C C . ASP A 113 ? 0.4013 0.3367 0.3070 0.0827 0.0768 0.0669 106 ASP A C 456 O O . ASP A 113 ? 0.4037 0.3473 0.3123 0.0563 0.0921 0.0794 106 ASP A O 457 C CB . ASP A 113 ? 0.4226 0.3208 0.2860 0.0919 0.0662 0.0632 106 ASP A CB 458 C CG . ASP A 113 ? 0.4499 0.3278 0.2722 0.0737 0.0693 0.0663 106 ASP A CG 459 O OD1 . ASP A 113 ? 0.4510 0.3114 0.2297 0.0576 0.0668 0.0770 106 ASP A OD1 460 O OD2 . ASP A 113 ? 0.4417 0.2905 0.2870 0.0789 0.0409 0.0703 106 ASP A OD2 461 N N . SER A 114 ? 0.3864 0.3197 0.2783 0.0859 0.0785 0.0742 107 SER A N 462 C CA . SER A 114 ? 0.3796 0.3038 0.3068 0.0891 0.0793 0.0583 107 SER A CA 463 C C . SER A 114 ? 0.3719 0.2980 0.2888 0.0721 0.0814 0.0594 107 SER A C 464 O O . SER A 114 ? 0.3572 0.2921 0.2740 0.0670 0.0833 0.0553 107 SER A O 465 C CB . SER A 114 ? 0.3923 0.3032 0.3028 0.0827 0.0754 0.0799 107 SER A CB 466 O OG A SER A 114 ? 0.4063 0.2355 0.3412 0.1308 0.0562 0.0605 107 SER A OG 467 O OG B SER A 114 ? 0.4034 0.3426 0.3210 0.0998 0.0541 0.0591 107 SER A OG 468 N N . VAL A 115 ? 0.3509 0.2831 0.2912 0.0754 0.0845 0.0467 108 VAL A N 469 C CA . VAL A 115 ? 0.3290 0.2770 0.3045 0.0698 0.0770 0.0397 108 VAL A CA 470 C C . VAL A 115 ? 0.3276 0.2821 0.3116 0.0611 0.0752 0.0389 108 VAL A C 471 O O . VAL A 115 ? 0.3262 0.2943 0.3179 0.0421 0.0820 0.0433 108 VAL A O 472 C CB . VAL A 115 ? 0.3222 0.2773 0.2910 0.0767 0.0730 0.0388 108 VAL A CB 473 C CG1 . VAL A 115 ? 0.2577 0.2137 0.2764 0.1036 0.0590 0.0345 108 VAL A CG1 474 C CG2 . VAL A 115 ? 0.3040 0.2655 0.2666 0.0722 0.0810 0.0268 108 VAL A CG2 475 N N . GLU A 116 ? 0.3108 0.2787 0.3165 0.0583 0.0776 0.0423 109 GLU A N 476 C CA . GLU A 116 ? 0.3250 0.2877 0.3327 0.0526 0.0675 0.0353 109 GLU A CA 477 C C . GLU A 116 ? 0.3059 0.2702 0.3218 0.0447 0.0607 0.0336 109 GLU A C 478 O O . GLU A 116 ? 0.3166 0.2676 0.3096 0.0281 0.0541 0.0247 109 GLU A O 479 C CB . GLU A 116 ? 0.3321 0.3139 0.3606 0.0710 0.0706 0.0271 109 GLU A CB 480 C CG . GLU A 116 ? 0.4014 0.3857 0.3725 0.0304 0.0817 0.0490 109 GLU A CG 481 C CD . GLU A 116 ? 0.4426 0.4827 0.4576 -0.0071 0.0775 0.0555 109 GLU A CD 482 O OE1 . GLU A 116 ? 0.4580 0.5419 0.4709 -0.0019 0.0633 0.0296 109 GLU A OE1 483 O OE2 . GLU A 116 ? 0.4670 0.5671 0.4640 -0.0143 0.0964 0.0592 109 GLU A OE2 484 N N . LEU A 117 ? 0.2882 0.2550 0.3129 0.0358 0.0517 0.0358 110 LEU A N 485 C CA . LEU A 117 ? 0.2719 0.2366 0.3093 0.0347 0.0491 0.0375 110 LEU A CA 486 C C . LEU A 117 ? 0.2655 0.2608 0.3125 0.0277 0.0426 0.0418 110 LEU A C 487 O O . LEU A 117 ? 0.2617 0.2664 0.3407 0.0407 0.0268 0.0604 110 LEU A O 488 C CB . LEU A 117 ? 0.2685 0.2581 0.3029 0.0363 0.0577 0.0286 110 LEU A CB 489 C CG . LEU A 117 ? 0.3390 0.2325 0.3490 0.0293 0.0386 0.0214 110 LEU A CG 490 C CD1 . LEU A 117 ? 0.4440 0.2968 0.3633 0.0129 0.0122 -0.0196 110 LEU A CD1 491 C CD2 . LEU A 117 ? 0.2968 0.2642 0.3354 0.0472 0.0548 0.0084 110 LEU A CD2 492 N N . ALA A 118 ? 0.2633 0.2307 0.3026 0.0115 0.0280 0.0414 111 ALA A N 493 C CA . ALA A 118 ? 0.2667 0.2453 0.2817 0.0076 0.0280 0.0267 111 ALA A CA 494 C C . ALA A 118 ? 0.2591 0.2470 0.2824 0.0123 0.0284 0.0083 111 ALA A C 495 O O . ALA A 118 ? 0.2727 0.2740 0.2728 0.0325 0.0386 0.0185 111 ALA A O 496 C CB . ALA A 118 ? 0.2816 0.2217 0.2383 0.0080 0.0085 0.0034 111 ALA A CB 497 N N . HIS A 119 ? 0.2403 0.2458 0.2862 0.0153 0.0324 0.0151 112 HIS A N 498 C CA . HIS A 119 ? 0.2290 0.2289 0.2887 0.0206 0.0284 0.0022 112 HIS A CA 499 C C . HIS A 119 ? 0.2223 0.2213 0.2796 0.0134 0.0293 -0.0039 112 HIS A C 500 O O . HIS A 119 ? 0.1975 0.2169 0.2661 0.0223 0.0201 -0.0087 112 HIS A O 501 C CB . HIS A 119 ? 0.2304 0.2262 0.2953 0.0047 0.0383 0.0118 112 HIS A CB 502 C CG . HIS A 119 ? 0.2454 0.2663 0.3589 0.0205 0.0202 0.0062 112 HIS A CG 503 N ND1 . HIS A 119 ? 0.2717 0.3278 0.4013 0.0113 0.0225 0.0165 112 HIS A ND1 504 C CD2 . HIS A 119 ? 0.2934 0.3195 0.3698 0.0088 0.0135 0.0032 112 HIS A CD2 505 C CE1 . HIS A 119 ? 0.2818 0.3343 0.3951 0.0072 0.0104 -0.0029 112 HIS A CE1 506 N NE2 . HIS A 119 ? 0.2504 0.3012 0.3895 -0.0088 -0.0118 -0.0161 112 HIS A NE2 507 N N . TYR A 120 ? 0.2148 0.2063 0.2498 0.0122 0.0225 -0.0252 113 TYR A N 508 C CA . TYR A 120 ? 0.2217 0.1984 0.2552 0.0055 0.0094 -0.0344 113 TYR A CA 509 C C . TYR A 120 ? 0.2161 0.2012 0.2468 0.0026 0.0079 -0.0451 113 TYR A C 510 O O . TYR A 120 ? 0.2441 0.2183 0.2451 0.0090 -0.0106 -0.0532 113 TYR A O 511 C CB . TYR A 120 ? 0.2016 0.1909 0.2531 0.0029 0.0162 -0.0345 113 TYR A CB 512 C CG . TYR A 120 ? 0.2167 0.1781 0.2259 0.0023 0.0129 -0.0284 113 TYR A CG 513 C CD1 . TYR A 120 ? 0.2112 0.1293 0.2145 -0.0103 0.0568 -0.0462 113 TYR A CD1 514 C CD2 . TYR A 120 ? 0.2156 0.1868 0.1996 0.0039 0.0038 -0.0141 113 TYR A CD2 515 C CE1 . TYR A 120 ? 0.2454 0.1934 0.1861 -0.0066 0.0274 -0.0146 113 TYR A CE1 516 C CE2 . TYR A 120 ? 0.1800 0.1562 0.2101 0.0065 -0.0072 -0.0187 113 TYR A CE2 517 C CZ . TYR A 120 ? 0.2339 0.1789 0.2239 -0.0040 0.0039 -0.0421 113 TYR A CZ 518 O OH . TYR A 120 ? 0.2396 0.2135 0.1945 0.0361 -0.0078 -0.0153 113 TYR A OH 519 N N . ASP A 121 ? 0.2022 0.1967 0.2466 -0.0097 0.0033 -0.0421 114 ASP A N 520 C CA . ASP A 121 ? 0.2065 0.2057 0.2654 -0.0026 0.0050 -0.0331 114 ASP A CA 521 C C . ASP A 121 ? 0.1926 0.2106 0.2574 -0.0021 0.0066 -0.0416 114 ASP A C 522 O O . ASP A 121 ? 0.1858 0.2008 0.2912 0.0113 0.0049 -0.0303 114 ASP A O 523 C CB . ASP A 121 ? 0.2171 0.2268 0.2743 -0.0101 0.0052 -0.0308 114 ASP A CB 524 C CG . ASP A 121 ? 0.2344 0.2638 0.3388 -0.0032 0.0097 -0.0076 114 ASP A CG 525 O OD1 . ASP A 121 ? 0.2377 0.2349 0.3559 -0.0122 -0.0061 -0.0347 114 ASP A OD1 526 O OD2 . ASP A 121 ? 0.2315 0.3736 0.3724 0.0129 -0.0059 0.0368 114 ASP A OD2 527 N N . VAL A 122 ? 0.1968 0.1918 0.2480 -0.0005 0.0111 -0.0497 115 VAL A N 528 C CA . VAL A 122 ? 0.2006 0.1897 0.2166 0.0081 0.0070 -0.0487 115 VAL A CA 529 C C . VAL A 122 ? 0.2181 0.2034 0.2269 0.0059 0.0173 -0.0438 115 VAL A C 530 O O . VAL A 122 ? 0.2433 0.2076 0.2397 0.0095 0.0123 -0.0446 115 VAL A O 531 C CB . VAL A 122 ? 0.1761 0.1778 0.2171 -0.0036 0.0212 -0.0510 115 VAL A CB 532 C CG1 . VAL A 122 ? 0.2152 0.1720 0.1910 0.0203 -0.0032 -0.0643 115 VAL A CG1 533 C CG2 . VAL A 122 ? 0.1749 0.1804 0.1948 -0.0088 -0.0265 -0.0398 115 VAL A CG2 534 N N . LEU A 123 ? 0.2257 0.2038 0.2033 0.0083 0.0012 -0.0327 116 LEU A N 535 C CA . LEU A 123 ? 0.1945 0.1965 0.2063 0.0223 0.0044 -0.0403 116 LEU A CA 536 C C . LEU A 123 ? 0.1991 0.2087 0.2202 0.0123 0.0032 -0.0413 116 LEU A C 537 O O . LEU A 123 ? 0.2138 0.2175 0.2644 0.0256 -0.0014 -0.0465 116 LEU A O 538 C CB . LEU A 123 ? 0.1943 0.2003 0.1943 0.0186 0.0079 -0.0494 116 LEU A CB 539 C CG . LEU A 123 ? 0.2014 0.2277 0.1877 -0.0216 -0.0057 -0.0298 116 LEU A CG 540 C CD1 . LEU A 123 ? 0.1950 0.2280 0.2130 0.0044 -0.0142 -0.0846 116 LEU A CD1 541 C CD2 . LEU A 123 ? 0.2501 0.1973 0.2412 -0.0565 0.0043 -0.0158 116 LEU A CD2 542 N N . LEU A 124 ? 0.1943 0.1886 0.2151 0.0190 0.0052 -0.0481 117 LEU A N 543 C CA . LEU A 124 ? 0.2021 0.2129 0.2162 0.0163 0.0059 -0.0439 117 LEU A CA 544 C C . LEU A 124 ? 0.2182 0.2315 0.2429 0.0239 0.0047 -0.0503 117 LEU A C 545 O O . LEU A 124 ? 0.2321 0.2668 0.2547 0.0090 0.0035 -0.0623 117 LEU A O 546 C CB . LEU A 124 ? 0.1997 0.1959 0.2079 0.0120 -0.0009 -0.0473 117 LEU A CB 547 C CG . LEU A 124 ? 0.2104 0.1669 0.1950 -0.0094 0.0049 -0.0326 117 LEU A CG 548 C CD1 . LEU A 124 ? 0.2315 0.2069 0.1383 -0.0332 0.0069 -0.0189 117 LEU A CD1 549 C CD2 . LEU A 124 ? 0.1887 0.1718 0.1597 -0.0225 -0.0096 -0.0498 117 LEU A CD2 550 N N . SER A 125 ? 0.2337 0.2583 0.2584 0.0294 0.0134 -0.0486 118 SER A N 551 C CA . SER A 125 ? 0.2376 0.2442 0.2677 0.0252 0.0167 -0.0685 118 SER A CA 552 C C . SER A 125 ? 0.2476 0.2553 0.2750 0.0199 0.0141 -0.0674 118 SER A C 553 O O . SER A 125 ? 0.2106 0.2562 0.2891 0.0419 0.0133 -0.0693 118 SER A O 554 C CB . SER A 125 ? 0.2487 0.2493 0.2765 0.0246 0.0205 -0.0672 118 SER A CB 555 O OG . SER A 125 ? 0.2362 0.2925 0.2727 0.0087 0.0203 -0.0621 118 SER A OG 556 N N . TYR A 126 ? 0.2495 0.2406 0.2724 0.0106 0.0187 -0.0822 119 TYR A N 557 C CA . TYR A 126 ? 0.2613 0.2637 0.2915 0.0204 0.0142 -0.0834 119 TYR A CA 558 C C . TYR A 126 ? 0.2814 0.2823 0.3196 0.0196 0.0035 -0.0943 119 TYR A C 559 O O . TYR A 126 ? 0.2889 0.3023 0.3041 0.0173 0.0027 -0.1035 119 TYR A O 560 C CB . TYR A 126 ? 0.2663 0.2665 0.2974 0.0277 0.0127 -0.0774 119 TYR A CB 561 C CG . TYR A 126 ? 0.2770 0.2858 0.3098 0.0150 0.0344 -0.0551 119 TYR A CG 562 C CD1 . TYR A 126 ? 0.2674 0.2697 0.3014 0.0150 0.0311 -0.0541 119 TYR A CD1 563 C CD2 . TYR A 126 ? 0.2763 0.2927 0.3508 0.0209 0.0411 -0.0570 119 TYR A CD2 564 C CE1 . TYR A 126 ? 0.2449 0.2582 0.3090 0.0175 0.0378 -0.0547 119 TYR A CE1 565 C CE2 . TYR A 126 ? 0.2472 0.2727 0.3255 0.0116 0.0212 -0.0650 119 TYR A CE2 566 C CZ . TYR A 126 ? 0.2664 0.2757 0.3171 0.0255 0.0266 -0.0810 119 TYR A CZ 567 O OH . TYR A 126 ? 0.2270 0.2774 0.3036 0.0022 0.0325 -0.0699 119 TYR A OH 568 N N . PRO A 127 ? 0.2951 0.2805 0.3442 0.0214 0.0044 -0.1077 120 PRO A N 569 C CA . PRO A 127 ? 0.3085 0.2907 0.3486 0.0102 -0.0017 -0.1211 120 PRO A CA 570 C C . PRO A 127 ? 0.3280 0.2978 0.3794 0.0083 -0.0001 -0.1199 120 PRO A C 571 O O . PRO A 127 ? 0.3191 0.2898 0.3753 0.0167 0.0139 -0.1212 120 PRO A O 572 C CB . PRO A 127 ? 0.3003 0.2689 0.3435 0.0183 -0.0054 -0.1252 120 PRO A CB 573 C CG . PRO A 127 ? 0.3022 0.3123 0.3404 0.0310 0.0003 -0.1177 120 PRO A CG 574 C CD . PRO A 127 ? 0.2853 0.2711 0.3305 0.0144 -0.0096 -0.1174 120 PRO A CD 575 N N . ASN A 128 ? 0.3546 0.3066 0.3916 0.0016 -0.0074 -0.1333 121 ASN A N 576 C CA . ASN A 128 ? 0.3930 0.3334 0.4367 -0.0050 -0.0155 -0.1363 121 ASN A CA 577 C C . ASN A 128 ? 0.4158 0.3347 0.4510 -0.0081 -0.0132 -0.1378 121 ASN A C 578 O O . ASN A 128 ? 0.4104 0.3011 0.4432 -0.0162 -0.0088 -0.1349 121 ASN A O 579 C CB . ASN A 128 ? 0.3917 0.3376 0.4450 -0.0027 -0.0256 -0.1391 121 ASN A CB 580 C CG . ASN A 128 ? 0.4560 0.3894 0.4996 -0.0149 -0.0438 -0.1576 121 ASN A CG 581 O OD1 . ASN A 128 ? 0.4344 0.3913 0.5683 -0.0302 -0.0676 -0.1601 121 ASN A OD1 582 N ND2 . ASN A 128 ? 0.4902 0.4841 0.5843 0.0339 -0.0551 -0.1605 121 ASN A ND2 583 N N . LYS A 129 ? 0.4413 0.3709 0.4739 -0.0079 -0.0059 -0.1355 122 LYS A N 584 C CA . LYS A 129 ? 0.4712 0.3996 0.5061 0.0001 -0.0103 -0.1365 122 LYS A CA 585 C C . LYS A 129 ? 0.4814 0.4070 0.5349 -0.0019 -0.0165 -0.1405 122 LYS A C 586 O O . LYS A 129 ? 0.4775 0.4020 0.5613 0.0017 -0.0270 -0.1426 122 LYS A O 587 C CB . LYS A 129 ? 0.4888 0.4097 0.5168 -0.0039 -0.0062 -0.1378 122 LYS A CB 588 C CG . LYS A 129 ? 0.5064 0.4695 0.5028 -0.0158 -0.0147 -0.1279 122 LYS A CG 589 C CD . LYS A 129 ? 0.4895 0.4512 0.5305 -0.0065 -0.0079 -0.1247 122 LYS A CD 590 C CE . LYS A 129 ? 0.4776 0.4545 0.5267 -0.0075 -0.0058 -0.1230 122 LYS A CE 591 N NZ . LYS A 129 ? 0.4754 0.4346 0.5317 0.0062 -0.0094 -0.1290 122 LYS A NZ 592 N N . THR A 130 ? 0.4872 0.4236 0.5391 0.0001 -0.0245 -0.1414 123 THR A N 593 C CA . THR A 130 ? 0.5087 0.4512 0.5521 -0.0057 -0.0252 -0.1465 123 THR A CA 594 C C . THR A 130 ? 0.5179 0.4490 0.5407 -0.0023 -0.0184 -0.1508 123 THR A C 595 O O . THR A 130 ? 0.5282 0.4494 0.5248 -0.0106 -0.0123 -0.1596 123 THR A O 596 C CB . THR A 130 ? 0.5087 0.4628 0.5688 -0.0081 -0.0304 -0.1403 123 THR A CB 597 O OG1 . THR A 130 ? 0.4836 0.4891 0.5938 -0.0215 -0.0576 -0.1717 123 THR A OG1 598 C CG2 . THR A 130 ? 0.5130 0.4815 0.5848 -0.0225 -0.0330 -0.1241 123 THR A CG2 599 N N . HIS A 131 ? 0.5055 0.4458 0.5257 -0.0017 -0.0194 -0.1513 124 HIS A N 600 C CA . HIS A 131 ? 0.5020 0.4484 0.5204 0.0088 -0.0132 -0.1472 124 HIS A CA 601 C C . HIS A 131 ? 0.4846 0.4277 0.4933 0.0170 -0.0099 -0.1480 124 HIS A C 602 O O . HIS A 131 ? 0.4604 0.4131 0.4865 0.0036 -0.0126 -0.1485 124 HIS A O 603 C CB . HIS A 131 ? 0.5198 0.4705 0.5316 0.0052 -0.0171 -0.1416 124 HIS A CB 604 C CG . HIS A 131 ? 0.5823 0.5413 0.5566 0.0216 -0.0055 -0.1360 124 HIS A CG 605 N ND1 . HIS A 131 ? 0.6202 0.5709 0.6069 0.0404 -0.0026 -0.1111 124 HIS A ND1 606 C CD2 . HIS A 131 ? 0.6006 0.5774 0.5963 0.0438 0.0070 -0.1309 124 HIS A CD2 607 C CE1 . HIS A 131 ? 0.6258 0.5722 0.6011 0.0378 -0.0015 -0.1236 124 HIS A CE1 608 N NE2 . HIS A 131 ? 0.6225 0.5962 0.6078 0.0395 0.0081 -0.1159 124 HIS A NE2 609 N N . PRO A 132 ? 0.4662 0.4126 0.4769 0.0266 -0.0033 -0.1514 125 PRO A N 610 C CA . PRO A 132 ? 0.4512 0.3941 0.4600 0.0374 0.0027 -0.1522 125 PRO A CA 611 C C . PRO A 132 ? 0.4288 0.3859 0.4375 0.0448 0.0100 -0.1558 125 PRO A C 612 O O . PRO A 132 ? 0.4379 0.3860 0.4420 0.0555 0.0185 -0.1732 125 PRO A O 613 C CB . PRO A 132 ? 0.4593 0.3986 0.4725 0.0369 -0.0002 -0.1526 125 PRO A CB 614 C CG . PRO A 132 ? 0.4601 0.3965 0.4793 0.0332 -0.0036 -0.1441 125 PRO A CG 615 C CD . PRO A 132 ? 0.4751 0.4136 0.4826 0.0267 -0.0082 -0.1455 125 PRO A CD 616 N N . ASN A 133 ? 0.3943 0.3708 0.4065 0.0413 0.0165 -0.1496 126 ASN A N 617 C CA . ASN A 133 ? 0.3850 0.3567 0.3788 0.0415 0.0321 -0.1434 126 ASN A CA 618 C C . ASN A 133 ? 0.3835 0.3662 0.3721 0.0374 0.0448 -0.1461 126 ASN A C 619 O O . ASN A 133 ? 0.3547 0.3693 0.3801 0.0288 0.0596 -0.1444 126 ASN A O 620 C CB . ASN A 133 ? 0.3644 0.3370 0.3586 0.0504 0.0428 -0.1409 126 ASN A CB 621 C CG . ASN A 133 ? 0.3727 0.3213 0.3461 0.0448 0.0380 -0.1319 126 ASN A CG 622 O OD1 . ASN A 133 ? 0.3765 0.3332 0.3478 0.0738 0.0330 -0.1023 126 ASN A OD1 623 N ND2 . ASN A 133 ? 0.3147 0.2632 0.3297 0.0417 0.0782 -0.1114 126 ASN A ND2 624 N N . TYR A 134 ? 0.3958 0.3659 0.3718 0.0301 0.0427 -0.1415 127 TYR A N 625 C CA . TYR A 134 ? 0.4237 0.3788 0.3637 0.0407 0.0491 -0.1498 127 TYR A CA 626 C C . TYR A 134 ? 0.4241 0.3807 0.3586 0.0413 0.0510 -0.1509 127 TYR A C 627 O O . TYR A 134 ? 0.4262 0.3871 0.3424 0.0466 0.0427 -0.1541 127 TYR A O 628 C CB . TYR A 134 ? 0.4264 0.3812 0.3751 0.0307 0.0406 -0.1539 127 TYR A CB 629 C CG . TYR A 134 ? 0.4814 0.4072 0.3852 0.0437 0.0479 -0.1783 127 TYR A CG 630 C CD1 . TYR A 134 ? 0.5242 0.4455 0.4078 0.0482 0.0543 -0.1764 127 TYR A CD1 631 C CD2 . TYR A 134 ? 0.4977 0.4137 0.4053 0.0268 0.0268 -0.1938 127 TYR A CD2 632 C CE1 . TYR A 134 ? 0.5085 0.4334 0.4016 0.0563 0.0401 -0.2106 127 TYR A CE1 633 C CE2 . TYR A 134 ? 0.5020 0.4598 0.3894 0.0299 0.0305 -0.1831 127 TYR A CE2 634 C CZ . TYR A 134 ? 0.5204 0.4479 0.4163 0.0536 0.0361 -0.2127 127 TYR A CZ 635 O OH . TYR A 134 ? 0.5471 0.4382 0.4004 0.0734 0.0390 -0.2003 127 TYR A OH 636 N N . ILE A 135 ? 0.4239 0.3829 0.3643 0.0435 0.0536 -0.1495 128 ILE A N 637 C CA . ILE A 135 ? 0.4219 0.3807 0.3502 0.0363 0.0626 -0.1522 128 ILE A CA 638 C C . ILE A 135 ? 0.4385 0.3874 0.3625 0.0366 0.0645 -0.1580 128 ILE A C 639 O O . ILE A 135 ? 0.4310 0.3714 0.3645 0.0306 0.0619 -0.1606 128 ILE A O 640 C CB . ILE A 135 ? 0.4156 0.3844 0.3418 0.0347 0.0581 -0.1532 128 ILE A CB 641 C CG1 . ILE A 135 ? 0.4001 0.3761 0.3225 0.0162 0.0708 -0.1598 128 ILE A CG1 642 C CG2 . ILE A 135 ? 0.4004 0.3828 0.3507 0.0075 0.0457 -0.1416 128 ILE A CG2 643 C CD1 . ILE A 135 ? 0.3996 0.3855 0.2410 0.0134 0.1014 -0.1553 128 ILE A CD1 644 N N . SER A 136 ? 0.4608 0.4008 0.3545 0.0418 0.0772 -0.1656 129 SER A N 645 C CA . SER A 136 ? 0.4873 0.4354 0.3785 0.0548 0.0920 -0.1699 129 SER A CA 646 C C . SER A 136 ? 0.5044 0.4579 0.3758 0.0573 0.1004 -0.1686 129 SER A C 647 O O . SER A 136 ? 0.5042 0.4707 0.3599 0.0591 0.1099 -0.1777 129 SER A O 648 C CB . SER A 136 ? 0.4889 0.4219 0.3747 0.0560 0.0971 -0.1791 129 SER A CB 649 O OG . SER A 136 ? 0.5148 0.4295 0.4337 0.0453 0.0900 -0.1992 129 SER A OG 650 N N . ILE A 137 ? 0.5317 0.4775 0.3845 0.0664 0.1037 -0.1730 130 ILE A N 651 C CA . ILE A 137 ? 0.5625 0.5104 0.4016 0.0718 0.1123 -0.1677 130 ILE A CA 652 C C . ILE A 137 ? 0.5939 0.5432 0.4124 0.0735 0.1168 -0.1739 130 ILE A C 653 O O . ILE A 137 ? 0.5894 0.5413 0.3976 0.0758 0.1231 -0.1858 130 ILE A O 654 C CB . ILE A 137 ? 0.5691 0.5137 0.4036 0.0684 0.1091 -0.1608 130 ILE A CB 655 C CG1 . ILE A 137 ? 0.5580 0.4965 0.3964 0.0654 0.0933 -0.1482 130 ILE A CG1 656 C CG2 . ILE A 137 ? 0.5451 0.5036 0.4011 0.0701 0.1168 -0.1478 130 ILE A CG2 657 C CD1 . ILE A 137 ? 0.5613 0.4859 0.3440 0.0798 0.0958 -0.1424 130 ILE A CD1 658 N N . ILE A 138 ? 0.6371 0.5796 0.4368 0.0807 0.1177 -0.1727 131 ILE A N 659 C CA . ILE A 138 ? 0.6928 0.6220 0.4748 0.0818 0.1088 -0.1739 131 ILE A CA 660 C C . ILE A 138 ? 0.7293 0.6460 0.4754 0.0899 0.1136 -0.1806 131 ILE A C 661 O O . ILE A 138 ? 0.7313 0.6439 0.4655 0.0944 0.1183 -0.1781 131 ILE A O 662 C CB . ILE A 138 ? 0.6930 0.6208 0.4832 0.0828 0.1041 -0.1716 131 ILE A CB 663 C CG1 . ILE A 138 ? 0.7145 0.6427 0.5202 0.0784 0.1013 -0.1635 131 ILE A CG1 664 C CG2 . ILE A 138 ? 0.6908 0.6097 0.4883 0.0734 0.0972 -0.1790 131 ILE A CG2 665 C CD1 . ILE A 138 ? 0.7416 0.6415 0.5616 0.0830 0.1388 -0.1757 131 ILE A CD1 666 N N . ASN A 139 ? 0.7729 0.6773 0.5084 0.0953 0.1153 -0.1851 132 ASN A N 667 C CA . ASN A 139 ? 0.8190 0.7109 0.5157 0.1018 0.1209 -0.1965 132 ASN A CA 668 C C . ASN A 139 ? 0.8484 0.7400 0.5425 0.1054 0.1163 -0.1942 132 ASN A C 669 O O . ASN A 139 ? 0.8545 0.7452 0.5457 0.1031 0.1234 -0.1937 132 ASN A O 670 C CB . ASN A 139 ? 0.8211 0.7034 0.5162 0.0992 0.1175 -0.1972 132 ASN A CB 671 C CG . ASN A 139 ? 0.8276 0.7018 0.4663 0.1039 0.1144 -0.2200 132 ASN A CG 672 O OD1 . ASN A 139 ? 0.8397 0.6838 0.4464 0.1128 0.0948 -0.2363 132 ASN A OD1 673 N ND2 . ASN A 139 ? 0.8398 0.6767 0.3631 0.0847 0.0978 -0.2519 132 ASN A ND2 674 N N . GLU A 140 ? 0.8876 0.7756 0.5558 0.1057 0.1167 -0.1950 133 GLU A N 675 C CA . GLU A 140 ? 0.9176 0.8071 0.5778 0.1109 0.1116 -0.1915 133 GLU A CA 676 C C . GLU A 140 ? 0.9309 0.8196 0.5945 0.1097 0.1020 -0.1942 133 GLU A C 677 O O . GLU A 140 ? 0.9349 0.8290 0.6050 0.1110 0.0912 -0.1888 133 GLU A O 678 C CB . GLU A 140 ? 0.9204 0.8127 0.5780 0.1080 0.1165 -0.1860 133 GLU A CB 679 C CG . GLU A 140 ? 0.9243 0.8144 0.5512 0.1174 0.1321 -0.1884 133 GLU A CG 680 C CD . GLU A 140 ? 0.9354 0.8111 0.5230 0.1286 0.1424 -0.1942 133 GLU A CD 681 O OE1 . GLU A 140 ? 0.9272 0.8084 0.5041 0.1330 0.1594 -0.2012 133 GLU A OE1 682 O OE2 . GLU A 140 ? 0.9314 0.8086 0.4862 0.1288 0.1567 -0.1948 133 GLU A OE2 683 N N . ASP A 141 ? 0.9413 0.8205 0.5976 0.1076 0.0961 -0.2027 134 ASP A N 684 C CA . ASP A 141 ? 0.9459 0.8193 0.5986 0.1038 0.0874 -0.2078 134 ASP A CA 685 C C . ASP A 141 ? 0.9344 0.8107 0.5958 0.0963 0.0792 -0.2067 134 ASP A C 686 O O . ASP A 141 ? 0.9414 0.8181 0.6011 0.0876 0.0690 -0.2026 134 ASP A O 687 C CB . ASP A 141 ? 0.9541 0.8185 0.6075 0.1066 0.0851 -0.2082 134 ASP A CB 688 C CG . ASP A 141 ? 0.9762 0.8262 0.6137 0.1061 0.0806 -0.2040 134 ASP A CG 689 O OD1 . ASP A 141 ? 0.9928 0.8279 0.6433 0.1025 0.0561 -0.1855 134 ASP A OD1 690 O OD2 . ASP A 141 ? 0.9912 0.8212 0.6185 0.1092 0.0704 -0.2041 134 ASP A OD2 691 N N . GLY A 142 ? 0.9107 0.7902 0.5798 0.0933 0.0806 -0.2102 135 GLY A N 692 C CA . GLY A 142 ? 0.8735 0.7630 0.5711 0.0890 0.0718 -0.2075 135 GLY A CA 693 C C . GLY A 142 ? 0.8420 0.7406 0.5529 0.0876 0.0679 -0.2131 135 GLY A C 694 O O . GLY A 142 ? 0.8403 0.7550 0.5646 0.0785 0.0642 -0.1989 135 GLY A O 695 N N . ASN A 143 ? 0.8128 0.7013 0.5211 0.0845 0.0650 -0.2219 136 ASN A N 696 C CA . ASN A 143 ? 0.7764 0.6677 0.5037 0.0828 0.0653 -0.2270 136 ASN A CA 697 C C . ASN A 143 ? 0.7506 0.6443 0.4885 0.0845 0.0706 -0.2230 136 ASN A C 698 O O . ASN A 143 ? 0.7500 0.6426 0.4727 0.0780 0.0638 -0.2297 136 ASN A O 699 C CB . ASN A 143 ? 0.7788 0.6592 0.4996 0.0836 0.0634 -0.2314 136 ASN A CB 700 C CG . ASN A 143 ? 0.7803 0.6517 0.5104 0.0862 0.0632 -0.2391 136 ASN A CG 701 O OD1 . ASN A 143 ? 0.8018 0.6362 0.5055 0.0849 0.0561 -0.2575 136 ASN A OD1 702 N ND2 . ASN A 143 ? 0.7911 0.6292 0.5007 0.0710 0.0173 -0.2555 136 ASN A ND2 703 N N . GLU A 144 ? 0.7109 0.6177 0.4710 0.0852 0.0745 -0.2232 137 GLU A N 704 C CA . GLU A 144 ? 0.6755 0.5926 0.4638 0.0847 0.0803 -0.2100 137 GLU A CA 705 C C . GLU A 144 ? 0.6574 0.5803 0.4588 0.0808 0.0842 -0.2038 137 GLU A C 706 O O . GLU A 144 ? 0.6592 0.5676 0.4593 0.0811 0.0804 -0.2166 137 GLU A O 707 C CB . GLU A 144 ? 0.6744 0.5854 0.4503 0.0863 0.0765 -0.2177 137 GLU A CB 708 C CG . GLU A 144 ? 0.6584 0.5900 0.4400 0.0755 0.0707 -0.2169 137 GLU A CG 709 C CD . GLU A 144 ? 0.6343 0.5614 0.4340 0.0724 0.0564 -0.2107 137 GLU A CD 710 O OE1 . GLU A 144 ? 0.6009 0.5273 0.4160 0.0583 0.0470 -0.2328 137 GLU A OE1 711 O OE2 . GLU A 144 ? 0.6361 0.6004 0.4541 0.0811 0.0357 -0.1805 137 GLU A OE2 712 N N . ILE A 145 ? 0.6320 0.5616 0.4576 0.0838 0.0929 -0.1958 138 ILE A N 713 C CA . ILE A 145 ? 0.6060 0.5406 0.4464 0.0893 0.1134 -0.1980 138 ILE A CA 714 C C . ILE A 145 ? 0.5817 0.5281 0.4504 0.0850 0.1115 -0.1853 138 ILE A C 715 O O . ILE A 145 ? 0.5834 0.5309 0.4565 0.0976 0.1262 -0.1869 138 ILE A O 716 C CB . ILE A 145 ? 0.6063 0.5466 0.4487 0.0844 0.1093 -0.1915 138 ILE A CB 717 C CG1 . ILE A 145 ? 0.5919 0.5338 0.4413 0.0997 0.1389 -0.1943 138 ILE A CG1 718 C CG2 . ILE A 145 ? 0.5976 0.5360 0.4110 0.1159 0.1487 -0.2205 138 ILE A CG2 719 C CD1 . ILE A 145 ? 0.5923 0.5702 0.5167 0.0770 0.1225 -0.1499 138 ILE A CD1 720 N N . PHE A 146 ? 0.5454 0.4916 0.4320 0.0742 0.1113 -0.1898 139 PHE A N 721 C CA . PHE A 146 ? 0.5119 0.4793 0.4279 0.0633 0.1015 -0.1781 139 PHE A CA 722 C C . PHE A 146 ? 0.4980 0.4543 0.4165 0.0602 0.0942 -0.1790 139 PHE A C 723 O O . PHE A 146 ? 0.4852 0.4435 0.3997 0.0526 0.0898 -0.1848 139 PHE A O 724 C CB . PHE A 146 ? 0.5182 0.4765 0.4270 0.0540 0.1047 -0.1819 139 PHE A CB 725 C CG . PHE A 146 ? 0.4826 0.4961 0.4382 0.0347 0.1115 -0.1650 139 PHE A CG 726 C CD1 . PHE A 146 ? 0.4499 0.5222 0.4465 0.0162 0.1038 -0.1471 139 PHE A CD1 727 C CD2 . PHE A 146 ? 0.4596 0.4616 0.4433 0.0048 0.1203 -0.1674 139 PHE A CD2 728 C CE1 . PHE A 146 ? 0.4413 0.4957 0.4712 -0.0048 0.0843 -0.1740 139 PHE A CE1 729 C CE2 . PHE A 146 ? 0.4345 0.4649 0.4671 0.0018 0.0838 -0.1686 139 PHE A CE2 730 C CZ . PHE A 146 ? 0.4229 0.4789 0.4618 -0.0036 0.0851 -0.1630 139 PHE A CZ 731 N N . ASN A 147 ? 0.4831 0.4372 0.4192 0.0609 0.0840 -0.1731 140 ASN A N 732 C CA . ASN A 147 ? 0.4779 0.4196 0.4114 0.0541 0.0824 -0.1671 140 ASN A CA 733 C C . ASN A 147 ? 0.4530 0.3989 0.4103 0.0531 0.0816 -0.1579 140 ASN A C 734 O O . ASN A 147 ? 0.4552 0.3719 0.4239 0.0533 0.0849 -0.1602 140 ASN A O 735 C CB . ASN A 147 ? 0.4968 0.4204 0.4111 0.0517 0.0764 -0.1729 140 ASN A CB 736 C CG . ASN A 147 ? 0.5375 0.4567 0.4322 0.0501 0.0668 -0.1844 140 ASN A CG 737 O OD1 . ASN A 147 ? 0.5737 0.4636 0.3874 0.0517 0.0735 -0.1988 140 ASN A OD1 738 N ND2 . ASN A 147 ? 0.5942 0.4561 0.4568 0.0556 0.0741 -0.2410 140 ASN A ND2 739 N N . THR A 148 ? 0.4298 0.3756 0.4050 0.0577 0.0799 -0.1441 141 THR A N 740 C CA . THR A 148 ? 0.4092 0.3647 0.3940 0.0596 0.0822 -0.1392 141 THR A CA 741 C C . THR A 148 ? 0.4053 0.3695 0.3980 0.0613 0.0751 -0.1385 141 THR A C 742 O O . THR A 148 ? 0.4158 0.3525 0.3991 0.0538 0.0799 -0.1355 141 THR A O 743 C CB . THR A 148 ? 0.4041 0.3678 0.3914 0.0566 0.0815 -0.1376 141 THR A CB 744 O OG1 . THR A 148 ? 0.4142 0.3654 0.3888 0.0699 0.0956 -0.1136 141 THR A OG1 745 C CG2 . THR A 148 ? 0.4008 0.3615 0.3883 0.0614 0.0884 -0.1336 141 THR A CG2 746 N N . SER A 149 ? 0.3928 0.3729 0.4130 0.0642 0.0636 -0.1244 142 SER A N 747 C CA . SER A 149 ? 0.3895 0.3772 0.4131 0.0526 0.0517 -0.1229 142 SER A CA 748 C C . SER A 149 ? 0.3969 0.3789 0.4149 0.0440 0.0472 -0.1243 142 SER A C 749 O O . SER A 149 ? 0.3730 0.3719 0.4061 0.0508 0.0422 -0.1244 142 SER A O 750 C CB . SER A 149 ? 0.4060 0.3843 0.4220 0.0468 0.0465 -0.1170 142 SER A CB 751 O OG A SER A 149 ? 0.3500 0.3491 0.3709 0.0516 0.0445 -0.1087 142 SER A OG 752 O OG B SER A 149 ? 0.4199 0.3579 0.4659 0.0605 0.0273 -0.1281 142 SER A OG 753 N N . LEU A 150 ? 0.3962 0.3629 0.4176 0.0365 0.0489 -0.1283 143 LEU A N 754 C CA . LEU A 150 ? 0.4120 0.3706 0.4318 0.0338 0.0428 -0.1263 143 LEU A CA 755 C C . LEU A 150 ? 0.4039 0.3548 0.4262 0.0356 0.0463 -0.1237 143 LEU A C 756 O O . LEU A 150 ? 0.3957 0.3565 0.4285 0.0354 0.0463 -0.1203 143 LEU A O 757 C CB . LEU A 150 ? 0.4123 0.3780 0.4374 0.0275 0.0437 -0.1317 143 LEU A CB 758 C CG . LEU A 150 ? 0.4285 0.4006 0.4623 0.0269 0.0246 -0.1382 143 LEU A CG 759 C CD1 . LEU A 150 ? 0.4442 0.4205 0.5060 0.0243 0.0396 -0.1685 143 LEU A CD1 760 C CD2 . LEU A 150 ? 0.4032 0.4392 0.4672 0.0738 0.0245 -0.1334 143 LEU A CD2 761 N N . PHE A 151 ? 0.3941 0.3357 0.4178 0.0439 0.0464 -0.1074 144 PHE A N 762 C CA . PHE A 151 ? 0.3963 0.3132 0.4258 0.0475 0.0309 -0.1004 144 PHE A CA 763 C C . PHE A 151 ? 0.3736 0.2884 0.4070 0.0521 0.0354 -0.0912 144 PHE A C 764 O O . PHE A 151 ? 0.3809 0.2819 0.3884 0.0626 0.0279 -0.0746 144 PHE A O 765 C CB . PHE A 151 ? 0.4015 0.3357 0.4312 0.0447 0.0367 -0.0945 144 PHE A CB 766 C CG . PHE A 151 ? 0.4674 0.3387 0.4697 0.0416 0.0130 -0.1091 144 PHE A CG 767 C CD1 . PHE A 151 ? 0.4628 0.3816 0.4833 0.0532 -0.0042 -0.1234 144 PHE A CD1 768 C CD2 . PHE A 151 ? 0.5319 0.4034 0.5145 0.0484 -0.0209 -0.1115 144 PHE A CD2 769 C CE1 . PHE A 151 ? 0.5023 0.3882 0.5127 0.0723 -0.0222 -0.1374 144 PHE A CE1 770 C CE2 . PHE A 151 ? 0.5350 0.4414 0.5377 0.0794 -0.0313 -0.1255 144 PHE A CE2 771 C CZ . PHE A 151 ? 0.5307 0.4420 0.5448 0.0706 -0.0387 -0.1197 144 PHE A CZ 772 N N . GLU A 152 ? 0.3516 0.2726 0.3930 0.0566 0.0333 -0.0877 145 GLU A N 773 C CA . GLU A 152 ? 0.3378 0.2633 0.3921 0.0464 0.0343 -0.0952 145 GLU A CA 774 C C . GLU A 152 ? 0.3297 0.2755 0.3881 0.0546 0.0335 -0.0929 145 GLU A C 775 O O . GLU A 152 ? 0.3318 0.2473 0.3980 0.0574 0.0205 -0.0738 145 GLU A O 776 C CB . GLU A 152 ? 0.3381 0.2497 0.3887 0.0458 0.0300 -0.1034 145 GLU A CB 777 C CG . GLU A 152 ? 0.3104 0.2479 0.3581 0.0482 0.0240 -0.1060 145 GLU A CG 778 C CD . GLU A 152 ? 0.2970 0.2662 0.3321 0.0503 0.0286 -0.0834 145 GLU A CD 779 O OE1 . GLU A 152 ? 0.2776 0.2463 0.3241 0.0522 0.0192 -0.0905 145 GLU A OE1 780 O OE2 . GLU A 152 ? 0.3272 0.2658 0.3274 0.0296 0.0139 -0.0917 145 GLU A OE2 781 N N . PRO A 153 ? 0.3296 0.2960 0.3936 0.0503 0.0331 -0.0917 146 PRO A N 782 C CA . PRO A 153 ? 0.3242 0.2934 0.3957 0.0557 0.0328 -0.0906 146 PRO A CA 783 C C . PRO A 153 ? 0.3195 0.2994 0.4040 0.0564 0.0261 -0.0796 146 PRO A C 784 O O . PRO A 153 ? 0.3128 0.3014 0.3575 0.0527 0.0115 -0.0782 146 PRO A O 785 C CB . PRO A 153 ? 0.3302 0.3235 0.3999 0.0536 0.0341 -0.0894 146 PRO A CB 786 C CG . PRO A 153 ? 0.3324 0.3018 0.4243 0.0531 0.0373 -0.0800 146 PRO A CG 787 C CD . PRO A 153 ? 0.3244 0.3035 0.4124 0.0472 0.0426 -0.0913 146 PRO A CD 788 N N . PRO A 154 ? 0.3128 0.2959 0.4106 0.0592 0.0195 -0.0734 147 PRO A N 789 C CA . PRO A 154 ? 0.3050 0.2975 0.4164 0.0565 0.0186 -0.0755 147 PRO A CA 790 C C . PRO A 154 ? 0.3187 0.2888 0.4200 0.0502 0.0117 -0.0705 147 PRO A C 791 O O . PRO A 154 ? 0.2461 0.3111 0.4082 0.0619 0.0008 -0.0620 147 PRO A O 792 C CB . PRO A 154 ? 0.3165 0.2939 0.4320 0.0514 0.0196 -0.0800 147 PRO A CB 793 C CG . PRO A 154 ? 0.3276 0.3107 0.4099 0.0601 0.0114 -0.0787 147 PRO A CG 794 C CD . PRO A 154 ? 0.3160 0.2888 0.4118 0.0506 0.0344 -0.0815 147 PRO A CD 795 N N . PRO A 155 ? 0.3299 0.2786 0.4233 0.0433 0.0054 -0.0652 148 PRO A N 796 C CA . PRO A 155 ? 0.3501 0.2749 0.4193 0.0472 0.0026 -0.0632 148 PRO A CA 797 C C . PRO A 155 ? 0.3469 0.2763 0.4165 0.0603 0.0061 -0.0696 148 PRO A C 798 O O . PRO A 155 ? 0.3548 0.2705 0.3853 0.0497 -0.0157 -0.0665 148 PRO A O 799 C CB . PRO A 155 ? 0.3563 0.2721 0.4126 0.0512 0.0015 -0.0591 148 PRO A CB 800 C CG . PRO A 155 ? 0.3597 0.2708 0.4320 0.0358 0.0002 -0.0551 148 PRO A CG 801 C CD . PRO A 155 ? 0.3359 0.2642 0.4230 0.0400 0.0025 -0.0635 148 PRO A CD 802 N N . PRO A 156 ? 0.3349 0.2740 0.4211 0.0701 0.0153 -0.0718 149 PRO A N 803 C CA . PRO A 156 ? 0.3334 0.2814 0.4423 0.0812 0.0113 -0.0678 149 PRO A CA 804 C C . PRO A 156 ? 0.3193 0.2846 0.4604 0.0894 0.0013 -0.0558 149 PRO A C 805 O O . PRO A 156 ? 0.2910 0.2825 0.4313 0.0911 -0.0037 -0.0593 149 PRO A O 806 C CB . PRO A 156 ? 0.3295 0.2762 0.4514 0.0789 0.0145 -0.0643 149 PRO A CB 807 C CG . PRO A 156 ? 0.3463 0.2788 0.4346 0.0742 0.0168 -0.0720 149 PRO A CG 808 C CD . PRO A 156 ? 0.3517 0.2864 0.4264 0.0715 0.0129 -0.0663 149 PRO A CD 809 N N . GLY A 157 ? 0.3301 0.2769 0.4790 0.0988 -0.0060 -0.0540 150 GLY A N 810 C CA . GLY A 157 ? 0.3462 0.3184 0.5177 0.0843 0.0052 -0.0528 150 GLY A CA 811 C C . GLY A 157 ? 0.3697 0.3425 0.5390 0.0780 0.0059 -0.0572 150 GLY A C 812 O O . GLY A 157 ? 0.3737 0.3805 0.5535 0.0766 0.0100 -0.0456 150 GLY A O 813 N N . TYR A 158 ? 0.3850 0.3420 0.5497 0.0690 0.0014 -0.0618 151 TYR A N 814 C CA . TYR A 158 ? 0.4097 0.3531 0.5704 0.0632 0.0049 -0.0658 151 TYR A CA 815 C C . TYR A 158 ? 0.4367 0.3877 0.5936 0.0598 0.0026 -0.0661 151 TYR A C 816 O O . TYR A 158 ? 0.4216 0.3883 0.6145 0.0574 0.0084 -0.0643 151 TYR A O 817 C CB . TYR A 158 ? 0.3971 0.3415 0.5487 0.0718 0.0019 -0.0646 151 TYR A CB 818 C CG . TYR A 158 ? 0.3615 0.2821 0.5099 0.0701 0.0236 -0.0529 151 TYR A CG 819 C CD1 . TYR A 158 ? 0.3311 0.2567 0.4832 0.0571 0.0239 -0.0455 151 TYR A CD1 820 C CD2 . TYR A 158 ? 0.3142 0.2357 0.4510 0.0385 0.0489 -0.0534 151 TYR A CD2 821 C CE1 . TYR A 158 ? 0.2995 0.2516 0.4352 0.0681 0.0239 -0.0224 151 TYR A CE1 822 C CE2 . TYR A 158 ? 0.2627 0.2378 0.4255 0.0390 0.0280 -0.0225 151 TYR A CE2 823 C CZ . TYR A 158 ? 0.2996 0.2410 0.3925 0.0395 0.0308 -0.0291 151 TYR A CZ 824 O OH . TYR A 158 ? 0.2635 0.3001 0.3380 0.0494 0.0294 -0.0089 151 TYR A OH 825 N N . GLU A 159 ? 0.4638 0.3788 0.6211 0.0603 0.0043 -0.0797 152 GLU A N 826 C CA . GLU A 159 ? 0.4979 0.4198 0.6445 0.0490 0.0099 -0.0771 152 GLU A CA 827 C C . GLU A 159 ? 0.5140 0.4341 0.6708 0.0459 0.0133 -0.0759 152 GLU A C 828 O O . GLU A 159 ? 0.5034 0.4407 0.6733 0.0370 0.0024 -0.0760 152 GLU A O 829 C CB . GLU A 159 ? 0.5026 0.4168 0.6417 0.0488 0.0131 -0.0851 152 GLU A CB 830 C CG . GLU A 159 ? 0.5210 0.4354 0.6404 0.0324 0.0249 -0.1023 152 GLU A CG 831 C CD . GLU A 159 ? 0.5544 0.4614 0.6147 0.0069 0.0315 -0.1339 152 GLU A CD 832 O OE1 . GLU A 159 ? 0.5437 0.4175 0.5906 -0.0281 0.0197 -0.1276 152 GLU A OE1 833 O OE2 . GLU A 159 ? 0.5948 0.5148 0.6097 -0.0168 0.0017 -0.1773 152 GLU A OE2 834 N N . ASN A 160 ? 0.5275 0.4498 0.7012 0.0462 0.0208 -0.0657 153 ASN A N 835 C CA . ASN A 160 ? 0.5433 0.4669 0.7226 0.0391 0.0210 -0.0674 153 ASN A CA 836 C C . ASN A 160 ? 0.5429 0.4701 0.7240 0.0367 0.0202 -0.0665 153 ASN A C 837 O O . ASN A 160 ? 0.5464 0.4793 0.7399 0.0262 0.0195 -0.0594 153 ASN A O 838 C CB . ASN A 160 ? 0.5477 0.4782 0.7330 0.0342 0.0203 -0.0635 153 ASN A CB 839 C CG . ASN A 160 ? 0.5590 0.5139 0.7435 0.0304 0.0155 -0.0689 153 ASN A CG 840 O OD1 . ASN A 160 ? 0.5809 0.5765 0.7432 0.0416 0.0060 -0.0789 153 ASN A OD1 841 N ND2 . ASN A 160 ? 0.5426 0.5406 0.7525 0.0186 0.0188 -0.0489 153 ASN A ND2 842 N N . VAL A 161 ? 0.5331 0.4562 0.7119 0.0397 0.0138 -0.0657 154 VAL A N 843 C CA . VAL A 161 ? 0.5336 0.4563 0.6785 0.0359 0.0134 -0.0693 154 VAL A CA 844 C C . VAL A 161 ? 0.5185 0.4564 0.6656 0.0346 0.0121 -0.0616 154 VAL A C 845 O O . VAL A 161 ? 0.5273 0.4624 0.6537 0.0298 -0.0023 -0.0446 154 VAL A O 846 C CB . VAL A 161 ? 0.5346 0.4577 0.6843 0.0389 0.0153 -0.0716 154 VAL A CB 847 C CG1 . VAL A 161 ? 0.5433 0.3936 0.7015 0.0312 0.0247 -0.0791 154 VAL A CG1 848 C CG2 . VAL A 161 ? 0.5408 0.4917 0.6928 0.0336 0.0117 -0.0860 154 VAL A CG2 849 N N . SER A 162 ? 0.4977 0.4342 0.6409 0.0253 -0.0009 -0.0604 155 SER A N 850 C CA . SER A 162 ? 0.4714 0.4000 0.6108 0.0153 0.0057 -0.0593 155 SER A CA 851 C C . SER A 162 ? 0.4472 0.3808 0.5771 0.0031 0.0077 -0.0536 155 SER A C 852 O O . SER A 162 ? 0.4318 0.3572 0.5786 -0.0048 0.0116 -0.0482 155 SER A O 853 C CB . SER A 162 ? 0.4678 0.4054 0.6077 0.0159 0.0076 -0.0569 155 SER A CB 854 O OG . SER A 162 ? 0.4534 0.4028 0.6030 0.0120 0.0113 -0.0544 155 SER A OG 855 N N . ASP A 163 ? 0.4182 0.3523 0.5452 -0.0090 0.0105 -0.0542 156 ASP A N 856 C CA . ASP A 163 ? 0.3879 0.3308 0.4992 -0.0091 0.0181 -0.0606 156 ASP A CA 857 C C . ASP A 163 ? 0.3498 0.3037 0.4521 0.0006 0.0206 -0.0588 156 ASP A C 858 O O . ASP A 163 ? 0.3330 0.3030 0.4362 -0.0129 0.0255 -0.0667 156 ASP A O 859 C CB . ASP A 163 ? 0.4029 0.3552 0.5183 -0.0281 0.0179 -0.0534 156 ASP A CB 860 C CG . ASP A 163 ? 0.4543 0.4295 0.5502 -0.0648 0.0152 -0.0575 156 ASP A CG 861 O OD1 . ASP A 163 ? 0.4802 0.5043 0.6019 -0.0995 -0.0351 -0.0619 156 ASP A OD1 862 O OD2 . ASP A 163 ? 0.4855 0.5012 0.5939 -0.1224 0.0497 -0.0412 156 ASP A OD2 863 N N . ILE A 164 ? 0.3247 0.2571 0.4109 0.0205 0.0134 -0.0617 157 ILE A N 864 C CA . ILE A 164 ? 0.2941 0.2644 0.3720 0.0381 0.0236 -0.0584 157 ILE A CA 865 C C . ILE A 164 ? 0.3036 0.2661 0.3747 0.0352 0.0222 -0.0647 157 ILE A C 866 O O . ILE A 164 ? 0.3210 0.2969 0.3601 0.0519 0.0161 -0.0534 157 ILE A O 867 C CB . ILE A 164 ? 0.2913 0.2405 0.3683 0.0441 0.0252 -0.0676 157 ILE A CB 868 C CG1 . ILE A 164 ? 0.2469 0.2150 0.3874 0.0892 0.0371 -0.0566 157 ILE A CG1 869 C CG2 . ILE A 164 ? 0.2615 0.2365 0.3231 0.0538 0.0507 -0.0804 157 ILE A CG2 870 C CD1 . ILE A 164 ? 0.2236 0.2336 0.3823 0.1007 0.0305 -0.0842 157 ILE A CD1 871 N N . VAL A 165 ? 0.2738 0.2487 0.3546 0.0310 0.0265 -0.0644 158 VAL A N 872 C CA . VAL A 165 ? 0.2745 0.2373 0.3376 0.0262 0.0198 -0.0774 158 VAL A CA 873 C C . VAL A 165 ? 0.2868 0.2533 0.3338 0.0134 0.0230 -0.0755 158 VAL A C 874 O O . VAL A 165 ? 0.2754 0.2558 0.3490 0.0115 0.0418 -0.0583 158 VAL A O 875 C CB . VAL A 165 ? 0.2779 0.2241 0.3332 0.0183 0.0067 -0.0780 158 VAL A CB 876 C CG1 . VAL A 165 ? 0.2568 0.1916 0.3021 0.0234 0.0129 -0.0650 158 VAL A CG1 877 C CG2 . VAL A 165 ? 0.2704 0.2157 0.3331 0.0426 -0.0041 -0.0781 158 VAL A CG2 878 N N . PRO A 166 ? 0.2968 0.2644 0.3406 0.0122 0.0342 -0.0837 159 PRO A N 879 C CA . PRO A 166 ? 0.3022 0.2740 0.3297 0.0086 0.0288 -0.0837 159 PRO A CA 880 C C . PRO A 166 ? 0.2869 0.2757 0.3232 0.0103 0.0278 -0.0814 159 PRO A C 881 O O . PRO A 166 ? 0.2789 0.2749 0.3257 0.0124 0.0181 -0.0797 159 PRO A O 882 C CB . PRO A 166 ? 0.2973 0.2736 0.3308 0.0027 0.0189 -0.0842 159 PRO A CB 883 C CG . PRO A 166 ? 0.3091 0.3057 0.3480 0.0144 0.0286 -0.0870 159 PRO A CG 884 C CD . PRO A 166 ? 0.2930 0.2845 0.3195 0.0162 0.0187 -0.0802 159 PRO A CD 885 N N . PRO A 167 ? 0.2674 0.2734 0.3216 0.0164 0.0250 -0.0754 160 PRO A N 886 C CA . PRO A 167 ? 0.2572 0.2653 0.3185 0.0190 0.0256 -0.0731 160 PRO A CA 887 C C . PRO A 167 ? 0.2358 0.2545 0.2995 0.0171 0.0248 -0.0753 160 PRO A C 888 O O . PRO A 167 ? 0.2349 0.2440 0.2999 0.0169 0.0234 -0.0625 160 PRO A O 889 C CB . PRO A 167 ? 0.2236 0.2575 0.3159 0.0242 0.0330 -0.0770 160 PRO A CB 890 C CG . PRO A 167 ? 0.2450 0.2619 0.3369 0.0166 0.0281 -0.0750 160 PRO A CG 891 C CD . PRO A 167 ? 0.2759 0.2674 0.3291 0.0142 0.0274 -0.0712 160 PRO A CD 892 N N . PHE A 168 ? 0.2138 0.2531 0.2763 0.0208 0.0383 -0.0769 161 PHE A N 893 C CA . PHE A 168 ? 0.2206 0.2513 0.2682 0.0134 0.0291 -0.0752 161 PHE A CA 894 C C . PHE A 168 ? 0.2293 0.2468 0.2540 0.0127 0.0245 -0.0787 161 PHE A C 895 O O . PHE A 168 ? 0.2234 0.2400 0.2430 0.0226 0.0165 -0.0700 161 PHE A O 896 C CB . PHE A 168 ? 0.2252 0.2636 0.2839 0.0120 0.0255 -0.0759 161 PHE A CB 897 C CG . PHE A 168 ? 0.2513 0.2739 0.2868 0.0106 0.0187 -0.0671 161 PHE A CG 898 C CD1 . PHE A 168 ? 0.2761 0.2207 0.2864 0.0253 0.0023 -0.0614 161 PHE A CD1 899 C CD2 . PHE A 168 ? 0.2603 0.2605 0.2824 0.0031 -0.0371 -0.0934 161 PHE A CD2 900 C CE1 . PHE A 168 ? 0.2692 0.2039 0.2815 -0.0065 -0.0042 -0.0655 161 PHE A CE1 901 C CE2 . PHE A 168 ? 0.2477 0.2809 0.2951 0.0003 -0.0270 -0.0767 161 PHE A CE2 902 C CZ . PHE A 168 ? 0.2529 0.2195 0.2935 0.0033 -0.0703 -0.0486 161 PHE A CZ 903 N N . SER A 169 ? 0.2375 0.2462 0.2461 0.0056 0.0232 -0.0806 162 SER A N 904 C CA . SER A 169 ? 0.2386 0.2464 0.2465 0.0107 0.0364 -0.0768 162 SER A CA 905 C C . SER A 169 ? 0.2422 0.2574 0.2380 0.0081 0.0246 -0.0732 162 SER A C 906 O O . SER A 169 ? 0.2394 0.2632 0.2373 -0.0029 0.0128 -0.0930 162 SER A O 907 C CB . SER A 169 ? 0.2374 0.2524 0.2458 0.0079 0.0246 -0.0707 162 SER A CB 908 O OG . SER A 169 ? 0.2573 0.2415 0.3022 0.0158 0.0620 -0.0723 162 SER A OG 909 N N . ALA A 170 ? 0.2373 0.2512 0.2333 0.0159 0.0407 -0.0766 163 ALA A N 910 C CA . ALA A 170 ? 0.2210 0.2461 0.2258 0.0239 0.0228 -0.0633 163 ALA A CA 911 C C . ALA A 170 ? 0.2399 0.2615 0.2236 0.0179 0.0208 -0.0590 163 ALA A C 912 O O . ALA A 170 ? 0.2321 0.2459 0.2112 0.0203 0.0133 -0.0674 163 ALA A O 913 C CB . ALA A 170 ? 0.1866 0.2287 0.2151 0.0174 0.0308 -0.0654 163 ALA A CB 914 N N . PHE A 171 ? 0.2616 0.2728 0.2209 0.0158 0.0126 -0.0567 164 PHE A N 915 C CA . PHE A 171 ? 0.2734 0.2837 0.2260 0.0250 0.0142 -0.0620 164 PHE A CA 916 C C . PHE A 171 ? 0.2971 0.2882 0.2406 0.0223 0.0051 -0.0616 164 PHE A C 917 O O . PHE A 171 ? 0.3080 0.2933 0.2622 0.0290 0.0001 -0.0599 164 PHE A O 918 C CB . PHE A 171 ? 0.2635 0.2640 0.2067 0.0173 0.0079 -0.0583 164 PHE A CB 919 C CG . PHE A 171 ? 0.2735 0.2942 0.2461 0.0146 0.0202 -0.0505 164 PHE A CG 920 C CD1 . PHE A 171 ? 0.2659 0.2283 0.2419 -0.0199 0.0254 -0.0357 164 PHE A CD1 921 C CD2 . PHE A 171 ? 0.2463 0.2231 0.1863 -0.0182 0.0205 -0.0486 164 PHE A CD2 922 C CE1 . PHE A 171 ? 0.2582 0.2127 0.2481 -0.0037 0.0280 -0.0613 164 PHE A CE1 923 C CE2 . PHE A 171 ? 0.2482 0.2751 0.2282 -0.0007 0.0222 -0.0343 164 PHE A CE2 924 C CZ . PHE A 171 ? 0.2176 0.2249 0.2732 0.0004 -0.0002 -0.0424 164 PHE A CZ 925 N N . SER A 172 ? 0.2884 0.2825 0.2447 0.0377 0.0177 -0.0806 165 SER A N 926 C CA . SER A 172 ? 0.3114 0.3020 0.2541 0.0289 0.0086 -0.0749 165 SER A CA 927 C C . SER A 172 ? 0.3207 0.3191 0.2690 0.0310 0.0098 -0.0810 165 SER A C 928 O O . SER A 172 ? 0.2984 0.3106 0.2760 0.0235 -0.0031 -0.0727 165 SER A O 929 C CB . SER A 172 ? 0.3220 0.3130 0.2474 0.0378 0.0199 -0.0888 165 SER A CB 930 O OG . SER A 172 ? 0.3204 0.3062 0.2379 0.0355 -0.0148 -0.0719 165 SER A OG 931 N N . PRO A 173 ? 0.3348 0.3298 0.2736 0.0328 0.0100 -0.0816 166 PRO A N 932 C CA . PRO A 173 ? 0.3490 0.3421 0.2814 0.0198 -0.0035 -0.0875 166 PRO A CA 933 C C . PRO A 173 ? 0.3620 0.3648 0.2792 0.0231 0.0034 -0.0960 166 PRO A C 934 O O . PRO A 173 ? 0.3616 0.3727 0.2598 0.0222 -0.0067 -0.0973 166 PRO A O 935 C CB . PRO A 173 ? 0.3632 0.3570 0.2900 0.0145 -0.0024 -0.0804 166 PRO A CB 936 C CG . PRO A 173 ? 0.3324 0.3403 0.2734 0.0150 -0.0018 -0.0852 166 PRO A CG 937 C CD . PRO A 173 ? 0.3290 0.3246 0.2825 0.0277 0.0079 -0.0947 166 PRO A CD 938 N N . GLN A 174 ? 0.3747 0.3827 0.3077 0.0225 -0.0051 -0.1060 167 GLN A N 939 C CA . GLN A 174 ? 0.3980 0.3935 0.3372 0.0217 0.0026 -0.1128 167 GLN A CA 940 C C . GLN A 174 ? 0.4128 0.4076 0.3433 0.0270 0.0070 -0.1158 167 GLN A C 941 O O . GLN A 174 ? 0.3929 0.4214 0.3575 0.0315 0.0078 -0.1061 167 GLN A O 942 C CB . GLN A 174 ? 0.3991 0.3952 0.3542 0.0214 -0.0160 -0.1106 167 GLN A CB 943 C CG . GLN A 174 ? 0.4160 0.4327 0.3720 -0.0188 -0.0024 -0.1088 167 GLN A CG 944 C CD . GLN A 174 ? 0.4834 0.5204 0.4333 -0.0567 -0.0436 -0.0935 167 GLN A CD 945 O OE1 . GLN A 174 ? 0.5204 0.5466 0.4373 -0.0790 -0.0794 -0.0737 167 GLN A OE1 946 N NE2 . GLN A 174 ? 0.4719 0.5166 0.4918 -0.0969 -0.0364 -0.0631 167 GLN A NE2 947 N N . GLY A 175 ? 0.4253 0.4184 0.3396 0.0194 0.0131 -0.1274 168 GLY A N 948 C CA . GLY A 175 ? 0.4506 0.4382 0.3455 0.0335 0.0238 -0.1278 168 GLY A CA 949 C C . GLY A 175 ? 0.4678 0.4646 0.3466 0.0381 0.0303 -0.1267 168 GLY A C 950 O O . GLY A 175 ? 0.4467 0.4672 0.3359 0.0482 0.0408 -0.1197 168 GLY A O 951 N N . MET A 176 ? 0.4919 0.4734 0.3422 0.0420 0.0232 -0.1338 169 MET A N 952 C CA . MET A 176 ? 0.5119 0.4948 0.3412 0.0461 0.0310 -0.1344 169 MET A CA 953 C C . MET A 176 ? 0.5088 0.4939 0.3419 0.0531 0.0301 -0.1346 169 MET A C 954 O O . MET A 176 ? 0.4987 0.5152 0.3062 0.0538 0.0265 -0.1277 169 MET A O 955 C CB . MET A 176 ? 0.5204 0.4890 0.3590 0.0446 0.0276 -0.1458 169 MET A CB 956 C CG . MET A 176 ? 0.5900 0.5639 0.4279 0.0234 0.0342 -0.1275 169 MET A CG 957 S SD . MET A 176 ? 0.7335 0.6320 0.6620 -0.0413 0.0331 -0.1153 169 MET A SD 958 C CE . MET A 176 ? 0.7424 0.6969 0.5900 -0.0047 0.0736 -0.1029 169 MET A CE 959 N N . PRO A 177 ? 0.5114 0.4906 0.3402 0.0593 0.0393 -0.1311 170 PRO A N 960 C CA . PRO A 177 ? 0.5256 0.4969 0.3352 0.0616 0.0457 -0.1267 170 PRO A CA 961 C C . PRO A 177 ? 0.5433 0.5107 0.3366 0.0605 0.0558 -0.1268 170 PRO A C 962 O O . PRO A 177 ? 0.5315 0.5148 0.3280 0.0635 0.0587 -0.1243 170 PRO A O 963 C CB . PRO A 177 ? 0.5177 0.4856 0.3322 0.0670 0.0499 -0.1300 170 PRO A CB 964 C CG . PRO A 177 ? 0.5029 0.4800 0.3431 0.0605 0.0438 -0.1288 170 PRO A CG 965 C CD . PRO A 177 ? 0.5159 0.4848 0.3458 0.0589 0.0431 -0.1287 170 PRO A CD 966 N N . GLU A 178 ? 0.5636 0.5230 0.3369 0.0584 0.0583 -0.1288 171 GLU A N 967 C CA . GLU A 178 ? 0.5806 0.5312 0.3402 0.0545 0.0623 -0.1254 171 GLU A CA 968 C C . GLU A 178 ? 0.5883 0.5447 0.3664 0.0536 0.0655 -0.1139 171 GLU A C 969 O O . GLU A 178 ? 0.6013 0.5691 0.3884 0.0497 0.0575 -0.1006 171 GLU A O 970 C CB . GLU A 178 ? 0.5826 0.5273 0.3329 0.0533 0.0606 -0.1315 171 GLU A CB 971 C CG . GLU A 178 ? 0.5837 0.4937 0.2593 0.0454 0.0464 -0.1646 171 GLU A CG 972 C CD . GLU A 178 ? 0.5874 0.4714 0.2280 0.0452 0.0452 -0.1824 171 GLU A CD 973 O OE1 . GLU A 178 ? 0.5878 0.4438 0.1499 0.0308 -0.0001 -0.2279 171 GLU A OE1 974 O OE2 . GLU A 178 ? 0.6070 0.4613 0.1581 0.0501 0.0357 -0.2343 171 GLU A OE2 975 N N . GLY A 179 ? 0.5816 0.5450 0.3539 0.0563 0.0755 -0.1078 172 GLY A N 976 C CA . GLY A 179 ? 0.5775 0.5408 0.3478 0.0546 0.0900 -0.1083 172 GLY A CA 977 C C . GLY A 179 ? 0.5722 0.5337 0.3357 0.0514 0.1035 -0.1051 172 GLY A C 978 O O . GLY A 179 ? 0.5690 0.5291 0.3375 0.0520 0.1019 -0.1073 172 GLY A O 979 N N . ASP A 180 ? 0.5725 0.5323 0.3211 0.0487 0.1123 -0.1029 173 ASP A N 980 C CA . ASP A 180 ? 0.5665 0.5214 0.3163 0.0474 0.1283 -0.0954 173 ASP A CA 981 C C . ASP A 180 ? 0.5362 0.5009 0.3094 0.0418 0.1350 -0.0896 173 ASP A C 982 O O . ASP A 180 ? 0.5351 0.4801 0.2871 0.0438 0.1356 -0.0991 173 ASP A O 983 C CB . ASP A 180 ? 0.5760 0.5353 0.3047 0.0519 0.1375 -0.0956 173 ASP A CB 984 C CG . ASP A 180 ? 0.6528 0.5708 0.3195 0.0566 0.1130 -0.0932 173 ASP A CG 985 O OD1 . ASP A 180 ? 0.7337 0.6032 0.3330 0.0663 0.1299 -0.1206 173 ASP A OD1 986 O OD2 . ASP A 180 ? 0.7226 0.6446 0.2798 0.0528 0.1100 -0.0478 173 ASP A OD2 987 N N . LEU A 181 ? 0.5041 0.4860 0.3169 0.0390 0.1423 -0.0772 174 LEU A N 988 C CA . LEU A 181 ? 0.4818 0.4778 0.3422 0.0439 0.1377 -0.0700 174 LEU A CA 989 C C . LEU A 181 ? 0.4807 0.4712 0.3417 0.0461 0.1367 -0.0723 174 LEU A C 990 O O . LEU A 181 ? 0.4931 0.4671 0.3399 0.0391 0.1309 -0.0778 174 LEU A O 991 C CB . LEU A 181 ? 0.4788 0.4843 0.3524 0.0445 0.1363 -0.0601 174 LEU A CB 992 C CG A LEU A 181 ? 0.4645 0.4763 0.3390 0.0531 0.1422 -0.0655 174 LEU A CG 993 C CG B LEU A 181 ? 0.4513 0.4625 0.3350 0.0553 0.1470 -0.0618 174 LEU A CG 994 C CD1 A LEU A 181 ? 0.4495 0.4606 0.3598 0.0763 0.1393 -0.0569 174 LEU A CD1 995 C CD1 B LEU A 181 ? 0.4257 0.4473 0.3147 0.0592 0.1775 -0.0600 174 LEU A CD1 996 C CD2 A LEU A 181 ? 0.4480 0.4557 0.3124 0.0535 0.1558 -0.0628 174 LEU A CD2 997 C CD2 B LEU A 181 ? 0.4447 0.4403 0.3166 0.0700 0.1361 -0.0740 174 LEU A CD2 998 N N . VAL A 182 ? 0.4688 0.4658 0.3424 0.0470 0.1378 -0.0692 175 VAL A N 999 C CA . VAL A 182 ? 0.4722 0.4549 0.3486 0.0456 0.1414 -0.0615 175 VAL A CA 1000 C C . VAL A 182 ? 0.4495 0.4511 0.3582 0.0404 0.1429 -0.0563 175 VAL A C 1001 O O . VAL A 182 ? 0.4387 0.4482 0.3288 0.0323 0.1560 -0.0500 175 VAL A O 1002 C CB . VAL A 182 ? 0.4874 0.4659 0.3576 0.0415 0.1310 -0.0573 175 VAL A CB 1003 C CG1 . VAL A 182 ? 0.4973 0.4409 0.3513 0.0451 0.1300 -0.0641 175 VAL A CG1 1004 C CG2 . VAL A 182 ? 0.5194 0.4523 0.3471 0.0461 0.1346 -0.0499 175 VAL A CG2 1005 N N . TYR A 183 ? 0.4220 0.4276 0.3665 0.0397 0.1471 -0.0538 176 TYR A N 1006 C CA . TYR A 183 ? 0.3987 0.4069 0.3694 0.0394 0.1468 -0.0538 176 TYR A CA 1007 C C . TYR A 183 ? 0.3850 0.4084 0.3756 0.0407 0.1506 -0.0465 176 TYR A C 1008 O O . TYR A 183 ? 0.3826 0.3882 0.3703 0.0478 0.1554 -0.0295 176 TYR A O 1009 C CB . TYR A 183 ? 0.3950 0.3940 0.3801 0.0405 0.1421 -0.0568 176 TYR A CB 1010 C CG . TYR A 183 ? 0.3767 0.3759 0.3946 0.0517 0.1344 -0.0673 176 TYR A CG 1011 C CD1 . TYR A 183 ? 0.3647 0.3537 0.4186 0.0379 0.1089 -0.0444 176 TYR A CD1 1012 C CD2 . TYR A 183 ? 0.3615 0.3702 0.4192 0.0382 0.1096 -0.0533 176 TYR A CD2 1013 C CE1 . TYR A 183 ? 0.3328 0.3773 0.4668 0.0316 0.0983 -0.0718 176 TYR A CE1 1014 C CE2 . TYR A 183 ? 0.3583 0.3763 0.4491 0.0267 0.1132 -0.0547 176 TYR A CE2 1015 C CZ . TYR A 183 ? 0.3550 0.3588 0.4571 0.0223 0.1120 -0.0695 176 TYR A CZ 1016 O OH . TYR A 183 ? 0.2710 0.3370 0.4839 0.0043 0.0992 -0.0688 176 TYR A OH 1017 N N . VAL A 184 ? 0.3771 0.4069 0.3709 0.0316 0.1479 -0.0464 177 VAL A N 1018 C CA . VAL A 184 ? 0.3613 0.4037 0.3674 0.0246 0.1455 -0.0389 177 VAL A CA 1019 C C . VAL A 184 ? 0.3552 0.3949 0.3771 0.0197 0.1338 -0.0403 177 VAL A C 1020 O O . VAL A 184 ? 0.3456 0.3904 0.3706 0.0261 0.1499 -0.0388 177 VAL A O 1021 C CB . VAL A 184 ? 0.3502 0.4119 0.3645 0.0216 0.1507 -0.0281 177 VAL A CB 1022 C CG1 . VAL A 184 ? 0.3158 0.3796 0.3253 0.0098 0.1787 -0.0280 177 VAL A CG1 1023 C CG2 . VAL A 184 ? 0.3397 0.4201 0.3692 0.0327 0.1664 -0.0260 177 VAL A CG2 1024 N N . ASN A 185 ? 0.3443 0.3864 0.3790 0.0168 0.1175 -0.0412 178 ASN A N 1025 C CA . ASN A 185 ? 0.3339 0.3718 0.3713 0.0106 0.1052 -0.0407 178 ASN A CA 1026 C C . ASN A 185 ? 0.3233 0.3614 0.3602 0.0147 0.0954 -0.0435 178 ASN A C 1027 O O . ASN A 185 ? 0.3236 0.3678 0.3545 0.0019 0.0929 -0.0475 178 ASN A O 1028 C CB . ASN A 185 ? 0.3294 0.3658 0.3762 0.0078 0.0990 -0.0353 178 ASN A CB 1029 C CG . ASN A 185 ? 0.3033 0.3705 0.3941 0.0026 0.1055 -0.0276 178 ASN A CG 1030 O OD1 . ASN A 185 ? 0.2470 0.3756 0.3958 0.0019 0.1210 -0.0147 178 ASN A OD1 1031 N ND2 . ASN A 185 ? 0.2941 0.3718 0.3558 -0.0012 0.0752 -0.0141 178 ASN A ND2 1032 N N . TYR A 186 ? 0.3116 0.3453 0.3436 0.0180 0.0823 -0.0475 179 TYR A N 1033 C CA . TYR A 186 ? 0.2962 0.3364 0.3364 0.0131 0.0791 -0.0480 179 TYR A CA 1034 C C . TYR A 186 ? 0.2986 0.3327 0.3308 0.0089 0.0762 -0.0540 179 TYR A C 1035 O O . TYR A 186 ? 0.2958 0.3261 0.3210 0.0043 0.0684 -0.0633 179 TYR A O 1036 C CB . TYR A 186 ? 0.2765 0.3142 0.3271 0.0158 0.0703 -0.0468 179 TYR A CB 1037 C CG . TYR A 186 ? 0.2580 0.3476 0.3331 -0.0140 0.0762 -0.0447 179 TYR A CG 1038 C CD1 . TYR A 186 ? 0.2146 0.2942 0.3428 0.0222 0.0823 -0.0795 179 TYR A CD1 1039 C CD2 . TYR A 186 ? 0.2460 0.3778 0.3401 0.0054 0.0675 -0.0532 179 TYR A CD2 1040 C CE1 . TYR A 186 ? 0.2135 0.3467 0.3818 -0.0062 0.0897 -0.0576 179 TYR A CE1 1041 C CE2 . TYR A 186 ? 0.1908 0.3406 0.3950 -0.0129 0.0937 -0.0527 179 TYR A CE2 1042 C CZ . TYR A 186 ? 0.2155 0.3323 0.4017 0.0069 0.0869 -0.0590 179 TYR A CZ 1043 O OH . TYR A 186 ? 0.2186 0.3279 0.4355 -0.0066 0.0685 -0.0313 179 TYR A OH 1044 N N . ALA A 187 ? 0.3112 0.3290 0.3332 0.0119 0.0804 -0.0568 180 ALA A N 1045 C CA . ALA A 187 ? 0.3280 0.3373 0.3319 0.0065 0.0845 -0.0546 180 ALA A CA 1046 C C . ALA A 187 ? 0.3307 0.3373 0.3154 0.0088 0.0919 -0.0515 180 ALA A C 1047 O O . ALA A 187 ? 0.3408 0.3435 0.3101 0.0042 0.0953 -0.0423 180 ALA A O 1048 C CB . ALA A 187 ? 0.3299 0.3266 0.3057 -0.0008 0.0937 -0.0622 180 ALA A CB 1049 N N . ARG A 188 ? 0.3299 0.3343 0.3145 0.0052 0.0954 -0.0410 181 ARG A N 1050 C CA . ARG A 188 ? 0.3166 0.3250 0.3148 0.0169 0.0962 -0.0305 181 ARG A CA 1051 C C . ARG A 188 ? 0.3111 0.3219 0.3253 0.0097 0.1007 -0.0272 181 ARG A C 1052 O O . ARG A 188 ? 0.3005 0.3140 0.3100 0.0167 0.1056 -0.0157 181 ARG A O 1053 C CB . ARG A 188 ? 0.2982 0.3243 0.3015 0.0079 0.1045 -0.0239 181 ARG A CB 1054 C CG . ARG A 188 ? 0.2654 0.3417 0.3190 0.0411 0.1020 -0.0448 181 ARG A CG 1055 C CD . ARG A 188 ? 0.2710 0.3034 0.3274 0.0099 0.0740 -0.0315 181 ARG A CD 1056 N NE . ARG A 188 ? 0.2539 0.2743 0.3673 0.0144 0.0880 -0.0523 181 ARG A NE 1057 C CZ . ARG A 188 ? 0.2868 0.3237 0.4013 0.0082 0.0680 -0.0562 181 ARG A CZ 1058 N NH1 . ARG A 188 ? 0.3133 0.2901 0.4273 0.0015 0.0158 -0.0399 181 ARG A NH1 1059 N NH2 . ARG A 188 ? 0.2557 0.3573 0.4483 -0.0019 0.0873 -0.0631 181 ARG A NH2 1060 N N . THR A 189 ? 0.3049 0.3109 0.3352 0.0121 0.1116 -0.0249 182 THR A N 1061 C CA . THR A 189 ? 0.3271 0.3177 0.3499 0.0190 0.1214 -0.0271 182 THR A CA 1062 C C . THR A 189 ? 0.3301 0.3252 0.3559 0.0248 0.1291 -0.0323 182 THR A C 1063 O O . THR A 189 ? 0.3284 0.2989 0.3733 0.0505 0.1287 -0.0350 182 THR A O 1064 C CB . THR A 189 ? 0.3173 0.3184 0.3344 0.0208 0.1262 -0.0255 182 THR A CB 1065 O OG1 . THR A 189 ? 0.3610 0.2937 0.3415 0.0060 0.1211 -0.0123 182 THR A OG1 1066 C CG2 . THR A 189 ? 0.3359 0.2858 0.3644 0.0163 0.1244 -0.0308 182 THR A CG2 1067 N N . GLU A 190 ? 0.3454 0.3495 0.3685 0.0180 0.1361 -0.0314 183 GLU A N 1068 C CA . GLU A 190 ? 0.3685 0.3830 0.3978 0.0109 0.1300 -0.0308 183 GLU A CA 1069 C C . GLU A 190 ? 0.3716 0.3790 0.3927 0.0088 0.1320 -0.0352 183 GLU A C 1070 O O . GLU A 190 ? 0.3626 0.3747 0.4118 0.0016 0.1339 -0.0453 183 GLU A O 1071 C CB . GLU A 190 ? 0.3690 0.3953 0.3962 0.0059 0.1318 -0.0199 183 GLU A CB 1072 C CG . GLU A 190 ? 0.4254 0.4439 0.4187 0.0252 0.1219 -0.0114 183 GLU A CG 1073 C CD . GLU A 190 ? 0.4272 0.4846 0.4349 0.0248 0.1034 0.0025 183 GLU A CD 1074 O OE1 . GLU A 190 ? 0.4074 0.4394 0.4582 0.0323 0.0685 -0.0024 183 GLU A OE1 1075 O OE2 . GLU A 190 ? 0.4143 0.4741 0.4669 0.0753 0.0500 -0.0101 183 GLU A OE2 1076 N N . ASP A 191 ? 0.3807 0.3707 0.3920 0.0093 0.1241 -0.0345 184 ASP A N 1077 C CA . ASP A 191 ? 0.3842 0.3710 0.3962 0.0070 0.1231 -0.0292 184 ASP A CA 1078 C C . ASP A 191 ? 0.3908 0.3797 0.3909 0.0071 0.1272 -0.0263 184 ASP A C 1079 O O . ASP A 191 ? 0.4055 0.3645 0.4088 0.0169 0.1232 -0.0327 184 ASP A O 1080 C CB . ASP A 191 ? 0.3802 0.3626 0.4034 0.0070 0.1199 -0.0272 184 ASP A CB 1081 C CG . ASP A 191 ? 0.3426 0.3386 0.3833 0.0054 0.1350 -0.0370 184 ASP A CG 1082 O OD1 . ASP A 191 ? 0.3301 0.3065 0.4048 0.0105 0.1489 -0.0352 184 ASP A OD1 1083 O OD2 . ASP A 191 ? 0.2357 0.3281 0.3678 0.0012 0.1619 -0.0795 184 ASP A OD2 1084 N N . PHE A 192 ? 0.3942 0.3860 0.3852 0.0045 0.1227 -0.0246 185 PHE A N 1085 C CA . PHE A 192 ? 0.3801 0.3933 0.3684 0.0017 0.1306 -0.0201 185 PHE A CA 1086 C C . PHE A 192 ? 0.3927 0.4115 0.3774 -0.0017 0.1399 -0.0126 185 PHE A C 1087 O O . PHE A 192 ? 0.3820 0.4070 0.3802 -0.0056 0.1436 -0.0093 185 PHE A O 1088 C CB . PHE A 192 ? 0.3701 0.3832 0.3472 -0.0050 0.1292 -0.0270 185 PHE A CB 1089 C CG . PHE A 192 ? 0.3230 0.3719 0.3184 0.0084 0.1168 -0.0454 185 PHE A CG 1090 C CD1 . PHE A 192 ? 0.3003 0.3498 0.2964 0.0141 0.0958 -0.0507 185 PHE A CD1 1091 C CD2 . PHE A 192 ? 0.3009 0.3596 0.3171 -0.0111 0.0899 -0.0324 185 PHE A CD2 1092 C CE1 . PHE A 192 ? 0.3425 0.3790 0.2935 0.0109 0.0830 -0.0654 185 PHE A CE1 1093 C CE2 . PHE A 192 ? 0.3233 0.3751 0.3179 -0.0078 0.0705 -0.0692 185 PHE A CE2 1094 C CZ . PHE A 192 ? 0.3370 0.3575 0.3077 -0.0098 0.0680 -0.0580 185 PHE A CZ 1095 N N . PHE A 193 ? 0.4059 0.4191 0.3765 -0.0047 0.1428 -0.0138 186 PHE A N 1096 C CA . PHE A 193 ? 0.4417 0.4292 0.3950 0.0056 0.1435 -0.0079 186 PHE A CA 1097 C C . PHE A 193 ? 0.4578 0.4435 0.4080 0.0048 0.1512 -0.0182 186 PHE A C 1098 O O . PHE A 193 ? 0.4907 0.4286 0.3986 0.0138 0.1398 -0.0240 186 PHE A O 1099 C CB . PHE A 193 ? 0.4406 0.4158 0.3810 0.0055 0.1438 -0.0015 186 PHE A CB 1100 C CG . PHE A 193 ? 0.4414 0.4143 0.3924 0.0118 0.1285 0.0124 186 PHE A CG 1101 C CD1 . PHE A 193 ? 0.4335 0.3924 0.4036 0.0232 0.1170 0.0230 186 PHE A CD1 1102 C CD2 . PHE A 193 ? 0.4559 0.4047 0.4087 0.0084 0.1187 0.0209 186 PHE A CD2 1103 C CE1 . PHE A 193 ? 0.4652 0.3934 0.4080 0.0333 0.1009 0.0296 186 PHE A CE1 1104 C CE2 . PHE A 193 ? 0.4084 0.3691 0.3552 0.0075 0.1247 0.0531 186 PHE A CE2 1105 C CZ . PHE A 193 ? 0.4683 0.3765 0.3906 0.0294 0.0978 0.0622 186 PHE A CZ 1106 N N . LYS A 194 ? 0.4750 0.4569 0.4277 0.0120 0.1542 -0.0203 187 LYS A N 1107 C CA . LYS A 194 ? 0.4684 0.4919 0.4421 0.0074 0.1799 -0.0151 187 LYS A CA 1108 C C . LYS A 194 ? 0.4796 0.5010 0.4510 0.0110 0.1837 -0.0122 187 LYS A C 1109 O O . LYS A 194 ? 0.4822 0.4928 0.4523 0.0068 0.1916 -0.0113 187 LYS A O 1110 C CB . LYS A 194 ? 0.4779 0.5052 0.4487 0.0093 0.1802 -0.0185 187 LYS A CB 1111 C CG . LYS A 194 ? 0.4963 0.5263 0.5044 0.0023 0.1865 -0.0200 187 LYS A CG 1112 C CD . LYS A 194 ? 0.5286 0.5937 0.5953 -0.0319 0.1753 -0.0172 187 LYS A CD 1113 C CE . LYS A 194 ? 0.5334 0.6172 0.5964 -0.0262 0.1763 -0.0198 187 LYS A CE 1114 N NZ . LYS A 194 ? 0.5303 0.5931 0.6127 -0.0237 0.1628 -0.0265 187 LYS A NZ 1115 N N . LEU A 195 ? 0.4816 0.5086 0.4518 0.0080 0.1910 -0.0079 188 LEU A N 1116 C CA . LEU A 195 ? 0.5082 0.5313 0.4552 0.0055 0.1890 -0.0061 188 LEU A CA 1117 C C . LEU A 195 ? 0.5232 0.5404 0.4605 0.0070 0.1877 -0.0050 188 LEU A C 1118 O O . LEU A 195 ? 0.5149 0.5395 0.4373 0.0072 0.2026 -0.0115 188 LEU A O 1119 C CB . LEU A 195 ? 0.5114 0.5284 0.4514 0.0049 0.1897 -0.0074 188 LEU A CB 1120 C CG . LEU A 195 ? 0.5249 0.5328 0.4730 0.0054 0.1951 -0.0127 188 LEU A CG 1121 C CD1 . LEU A 195 ? 0.5203 0.5596 0.5285 -0.0058 0.1935 -0.0329 188 LEU A CD1 1122 C CD2 . LEU A 195 ? 0.5318 0.5289 0.4577 0.0094 0.1928 -0.0175 188 LEU A CD2 1123 N N . GLU A 196 ? 0.5343 0.5442 0.4631 0.0124 0.1894 -0.0076 189 GLU A N 1124 C CA . GLU A 196 ? 0.5568 0.5531 0.4782 0.0158 0.1852 -0.0030 189 GLU A CA 1125 C C . GLU A 196 ? 0.5683 0.5588 0.4764 0.0171 0.1906 0.0007 189 GLU A C 1126 O O . GLU A 196 ? 0.5886 0.5556 0.4798 0.0231 0.1784 -0.0043 189 GLU A O 1127 C CB . GLU A 196 ? 0.5512 0.5577 0.4813 0.0152 0.1872 -0.0003 189 GLU A CB 1128 C CG . GLU A 196 ? 0.5745 0.5629 0.4993 0.0147 0.1723 0.0068 189 GLU A CG 1129 C CD . GLU A 196 ? 0.6048 0.5585 0.5581 0.0032 0.1501 0.0156 189 GLU A CD 1130 O OE1 . GLU A 196 ? 0.6043 0.5716 0.5872 0.0197 0.1650 0.0240 189 GLU A OE1 1131 O OE2 . GLU A 196 ? 0.6080 0.5669 0.5525 0.0196 0.1486 0.0155 189 GLU A OE2 1132 N N . ARG A 197 ? 0.5708 0.5571 0.4730 0.0144 0.1974 -0.0006 190 ARG A N 1133 C CA . ARG A 197 ? 0.5714 0.5575 0.4769 0.0138 0.2062 0.0037 190 ARG A CA 1134 C C . ARG A 197 ? 0.5854 0.5661 0.4883 0.0168 0.2153 0.0002 190 ARG A C 1135 O O . ARG A 197 ? 0.6007 0.5509 0.4674 0.0265 0.2127 0.0021 190 ARG A O 1136 C CB . ARG A 197 ? 0.5524 0.5463 0.4612 0.0127 0.2144 0.0049 190 ARG A CB 1137 C CG . ARG A 197 ? 0.5328 0.5120 0.4422 0.0173 0.2089 -0.0127 190 ARG A CG 1138 C CD . ARG A 197 ? 0.4849 0.4957 0.4527 0.0090 0.2097 -0.0184 190 ARG A CD 1139 N NE . ARG A 197 ? 0.5113 0.4615 0.4235 0.0390 0.1950 -0.0761 190 ARG A NE 1140 C CZ . ARG A 197 ? 0.4696 0.4663 0.4105 0.0167 0.1854 -0.0724 190 ARG A CZ 1141 N NH1 . ARG A 197 ? 0.4726 0.4027 0.3994 0.0048 0.2106 -0.1285 190 ARG A NH1 1142 N NH2 . ARG A 197 ? 0.4692 0.4658 0.4342 0.0229 0.1657 -0.0980 190 ARG A NH2 1143 N N . ASP A 198 ? 0.6028 0.5727 0.5047 0.0172 0.2195 0.0051 191 ASP A N 1144 C CA . ASP A 198 ? 0.6144 0.6004 0.5464 0.0158 0.2185 0.0064 191 ASP A CA 1145 C C . ASP A 198 ? 0.6193 0.6123 0.5497 0.0155 0.2265 0.0083 191 ASP A C 1146 O O . ASP A 198 ? 0.6209 0.6123 0.5610 0.0019 0.2297 0.0172 191 ASP A O 1147 C CB . ASP A 198 ? 0.6262 0.6005 0.5481 0.0119 0.2164 0.0083 191 ASP A CB 1148 C CG . ASP A 198 ? 0.6561 0.6175 0.5916 0.0076 0.2013 0.0030 191 ASP A CG 1149 O OD1 . ASP A 198 ? 0.6943 0.6129 0.5971 0.0041 0.1854 0.0075 191 ASP A OD1 1150 O OD2 . ASP A 198 ? 0.6870 0.6467 0.6099 -0.0151 0.1765 0.0070 191 ASP A OD2 1151 N N . MET A 199 ? 0.6222 0.6164 0.5489 0.0173 0.2323 0.0089 192 MET A N 1152 C CA . MET A 199 ? 0.6396 0.6231 0.5509 0.0189 0.2274 0.0070 192 MET A CA 1153 C C . MET A 199 ? 0.6504 0.6259 0.5358 0.0215 0.2307 0.0095 192 MET A C 1154 O O . MET A 199 ? 0.6446 0.6167 0.5132 0.0259 0.2466 0.0116 192 MET A O 1155 C CB . MET A 199 ? 0.6320 0.6223 0.5500 0.0209 0.2279 0.0079 192 MET A CB 1156 C CG . MET A 199 ? 0.6197 0.6096 0.5754 0.0228 0.2175 -0.0042 192 MET A CG 1157 S SD . MET A 199 ? 0.5457 0.5982 0.6159 0.0127 0.2066 -0.0205 192 MET A SD 1158 C CE . MET A 199 ? 0.5707 0.5762 0.5721 0.0414 0.1996 -0.0405 192 MET A CE 1159 N N . LYS A 200 ? 0.6597 0.6357 0.5295 0.0240 0.2286 0.0095 193 LYS A N 1160 C CA . LYS A 200 ? 0.6757 0.6530 0.5317 0.0256 0.2178 0.0105 193 LYS A CA 1161 C C . LYS A 200 ? 0.6759 0.6572 0.5152 0.0308 0.2163 0.0039 193 LYS A C 1162 O O . LYS A 200 ? 0.6856 0.6651 0.4949 0.0296 0.2160 0.0067 193 LYS A O 1163 C CB . LYS A 200 ? 0.6826 0.6604 0.5339 0.0281 0.2155 0.0113 193 LYS A CB 1164 C CG . LYS A 200 ? 0.7323 0.6837 0.5721 0.0132 0.1960 0.0411 193 LYS A CG 1165 C CD . LYS A 200 ? 0.7717 0.7321 0.6022 0.0018 0.1741 0.0445 193 LYS A CD 1166 C CE . LYS A 200 ? 0.7739 0.7391 0.6069 0.0178 0.1956 0.0340 193 LYS A CE 1167 N NZ . LYS A 200 ? 0.7824 0.7489 0.5642 0.0157 0.2086 0.0464 193 LYS A NZ 1168 N N . ILE A 201 ? 0.6642 0.6516 0.4933 0.0362 0.2154 -0.0036 194 ILE A N 1169 C CA . ILE A 201 ? 0.6588 0.6451 0.4803 0.0371 0.2096 -0.0080 194 ILE A CA 1170 C C . ILE A 201 ? 0.6591 0.6417 0.4679 0.0361 0.2019 -0.0139 194 ILE A C 1171 O O . ILE A 201 ? 0.6560 0.6370 0.4695 0.0350 0.2086 -0.0162 194 ILE A O 1172 C CB . ILE A 201 ? 0.6557 0.6456 0.4798 0.0352 0.2121 -0.0048 194 ILE A CB 1173 C CG1 . ILE A 201 ? 0.6521 0.6415 0.4809 0.0391 0.2076 0.0032 194 ILE A CG1 1174 C CG2 . ILE A 201 ? 0.6605 0.6380 0.4576 0.0407 0.2208 -0.0079 194 ILE A CG2 1175 C CD1 . ILE A 201 ? 0.6376 0.6450 0.4725 0.0282 0.2234 0.0564 194 ILE A CD1 1176 N N . ASN A 202 ? 0.6635 0.6427 0.4540 0.0393 0.1956 -0.0236 195 ASN A N 1177 C CA . ASN A 202 ? 0.6744 0.6486 0.4557 0.0428 0.1747 -0.0272 195 ASN A CA 1178 C C . ASN A 202 ? 0.6538 0.6266 0.4211 0.0470 0.1693 -0.0330 195 ASN A C 1179 O O . ASN A 202 ? 0.6354 0.6118 0.3746 0.0578 0.1838 -0.0388 195 ASN A O 1180 C CB . ASN A 202 ? 0.7076 0.6739 0.4733 0.0395 0.1679 -0.0221 195 ASN A CB 1181 C CG . ASN A 202 ? 0.7604 0.7590 0.5643 0.0549 0.1632 -0.0312 195 ASN A CG 1182 O OD1 . ASN A 202 ? 0.7842 0.7562 0.5598 0.0531 0.1422 -0.0184 195 ASN A OD1 1183 N ND2 . ASN A 202 ? 0.9536 0.8934 0.6214 0.0546 0.1395 -0.0043 195 ASN A ND2 1184 N N . CYS A 203 ? 0.6362 0.5952 0.3870 0.0556 0.1625 -0.0447 196 CYS A N 1185 C CA . CYS A 203 ? 0.6193 0.5846 0.3776 0.0546 0.1488 -0.0447 196 CYS A CA 1186 C C . CYS A 203 ? 0.6114 0.5826 0.3748 0.0599 0.1411 -0.0444 196 CYS A C 1187 O O . CYS A 203 ? 0.5954 0.5730 0.3728 0.0724 0.1454 -0.0421 196 CYS A O 1188 C CB . CYS A 203 ? 0.6204 0.5806 0.3771 0.0531 0.1436 -0.0427 196 CYS A CB 1189 S SG . CYS A 203 ? 0.6511 0.5616 0.3680 0.0646 0.1299 -0.0153 196 CYS A SG 1190 N N . SER A 204 ? 0.6098 0.5783 0.3743 0.0546 0.1308 -0.0335 197 SER A N 1191 C CA . SER A 204 ? 0.6211 0.5854 0.3827 0.0501 0.1052 -0.0281 197 SER A CA 1192 C C . SER A 204 ? 0.6139 0.5878 0.3734 0.0538 0.1048 -0.0386 197 SER A C 1193 O O . SER A 204 ? 0.6258 0.5977 0.3652 0.0489 0.1071 -0.0520 197 SER A O 1194 C CB . SER A 204 ? 0.6217 0.5874 0.3980 0.0425 0.1016 -0.0122 197 SER A CB 1195 O OG . SER A 204 ? 0.6262 0.5828 0.4212 0.0487 0.0756 0.0181 197 SER A OG 1196 N N . GLY A 205 ? 0.6019 0.5741 0.3590 0.0546 0.0984 -0.0445 198 GLY A N 1197 C CA . GLY A 205 ? 0.5886 0.5584 0.3514 0.0609 0.1020 -0.0539 198 GLY A CA 1198 C C . GLY A 205 ? 0.5815 0.5481 0.3462 0.0544 0.1064 -0.0622 198 GLY A C 1199 O O . GLY A 205 ? 0.5790 0.5506 0.3300 0.0684 0.1141 -0.0793 198 GLY A O 1200 N N . LYS A 206 ? 0.5597 0.5293 0.3319 0.0560 0.1081 -0.0576 199 LYS A N 1201 C CA . LYS A 206 ? 0.5388 0.5102 0.3275 0.0521 0.1098 -0.0535 199 LYS A CA 1202 C C . LYS A 206 ? 0.5236 0.4978 0.3251 0.0511 0.1051 -0.0610 199 LYS A C 1203 O O . LYS A 206 ? 0.4976 0.4767 0.3164 0.0536 0.1101 -0.0499 199 LYS A O 1204 C CB . LYS A 206 ? 0.5245 0.5056 0.3069 0.0595 0.1145 -0.0604 199 LYS A CB 1205 C CG . LYS A 206 ? 0.5357 0.5076 0.3584 0.0550 0.1072 -0.0351 199 LYS A CG 1206 C CD . LYS A 206 ? 0.5305 0.5092 0.3027 0.0596 0.1275 -0.0227 199 LYS A CD 1207 C CE . LYS A 206 ? 0.5562 0.5006 0.3223 0.0626 0.1245 -0.0126 199 LYS A CE 1208 N NZ . LYS A 206 ? 0.5815 0.5067 0.2780 0.0562 0.1290 0.0168 199 LYS A NZ 1209 N N . ILE A 207 ? 0.5070 0.4822 0.3296 0.0481 0.1024 -0.0597 200 ILE A N 1210 C CA . ILE A 207 ? 0.4974 0.4675 0.3388 0.0381 0.0970 -0.0694 200 ILE A CA 1211 C C . ILE A 207 ? 0.4837 0.4484 0.3300 0.0402 0.0992 -0.0722 200 ILE A C 1212 O O . ILE A 207 ? 0.4924 0.4592 0.3481 0.0247 0.0921 -0.0859 200 ILE A O 1213 C CB . ILE A 207 ? 0.5074 0.4750 0.3465 0.0287 0.0919 -0.0610 200 ILE A CB 1214 C CG1 . ILE A 207 ? 0.5377 0.4841 0.3222 0.0310 0.0679 -0.0694 200 ILE A CG1 1215 C CG2 . ILE A 207 ? 0.5201 0.4829 0.3343 0.0208 0.0848 -0.0615 200 ILE A CG2 1216 C CD1 . ILE A 207 ? 0.5436 0.4843 0.3373 0.0399 0.0558 -0.0522 200 ILE A CD1 1217 N N . VAL A 208 ? 0.4577 0.4231 0.3249 0.0358 0.0970 -0.0661 201 VAL A N 1218 C CA . VAL A 208 ? 0.4232 0.4029 0.3155 0.0341 0.1033 -0.0647 201 VAL A CA 1219 C C . VAL A 208 ? 0.3982 0.3908 0.3240 0.0365 0.1042 -0.0690 201 VAL A C 1220 O O . VAL A 208 ? 0.4021 0.3983 0.3444 0.0400 0.1004 -0.0591 201 VAL A O 1221 C CB . VAL A 208 ? 0.4315 0.4061 0.3253 0.0261 0.0914 -0.0611 201 VAL A CB 1222 C CG1 A VAL A 208 ? 0.4310 0.3969 0.3260 0.0233 0.0820 -0.0484 201 VAL A CG1 1223 C CG1 B VAL A 208 ? 0.4297 0.3998 0.2788 0.0287 0.1325 -0.0583 201 VAL A CG1 1224 C CG2 A VAL A 208 ? 0.4136 0.3892 0.2795 0.0296 0.1019 -0.0677 201 VAL A CG2 1225 C CG2 B VAL A 208 ? 0.4224 0.4107 0.3204 0.0269 0.1085 -0.0543 201 VAL A CG2 1226 N N . ILE A 209 ? 0.3637 0.3642 0.3068 0.0375 0.1169 -0.0743 202 ILE A N 1227 C CA . ILE A 209 ? 0.3435 0.3573 0.3076 0.0403 0.1160 -0.0790 202 ILE A CA 1228 C C . ILE A 209 ? 0.3358 0.3531 0.3171 0.0417 0.1098 -0.0715 202 ILE A C 1229 O O . ILE A 209 ? 0.3320 0.3353 0.3012 0.0297 0.1113 -0.0769 202 ILE A O 1230 C CB . ILE A 209 ? 0.3452 0.3579 0.3204 0.0412 0.1149 -0.0717 202 ILE A CB 1231 C CG1 . ILE A 209 ? 0.3314 0.3493 0.2979 0.0563 0.1158 -0.0807 202 ILE A CG1 1232 C CG2 . ILE A 209 ? 0.3378 0.3625 0.3017 0.0409 0.1309 -0.0745 202 ILE A CG2 1233 C CD1 . ILE A 209 ? 0.3084 0.3538 0.3460 0.0504 0.1048 -0.0868 202 ILE A CD1 1234 N N . ALA A 210 ? 0.3323 0.3374 0.2997 0.0389 0.1016 -0.0620 203 ALA A N 1235 C CA . ALA A 210 ? 0.3244 0.3329 0.3318 0.0296 0.0897 -0.0551 203 ALA A CA 1236 C C . ALA A 210 ? 0.3153 0.3333 0.3449 0.0272 0.0788 -0.0527 203 ALA A C 1237 O O . ALA A 210 ? 0.3230 0.3206 0.3573 0.0183 0.0633 -0.0325 203 ALA A O 1238 C CB . ALA A 210 ? 0.3020 0.3227 0.3134 0.0355 0.1089 -0.0626 203 ALA A CB 1239 N N . ARG A 211 ? 0.2970 0.3252 0.3630 0.0225 0.0742 -0.0498 204 ARG A N 1240 C CA . ARG A 211 ? 0.2858 0.3333 0.3541 0.0136 0.0737 -0.0492 204 ARG A CA 1241 C C . ARG A 211 ? 0.2753 0.3263 0.3508 0.0136 0.0694 -0.0450 204 ARG A C 1242 O O . ARG A 211 ? 0.2704 0.3250 0.3462 0.0160 0.0578 -0.0256 204 ARG A O 1243 C CB . ARG A 211 ? 0.2748 0.3286 0.3752 0.0177 0.0818 -0.0481 204 ARG A CB 1244 C CG . ARG A 211 ? 0.2891 0.3640 0.4119 -0.0098 0.0835 -0.0331 204 ARG A CG 1245 C CD . ARG A 211 ? 0.2876 0.3949 0.4206 -0.0463 0.0989 -0.0066 204 ARG A CD 1246 N NE . ARG A 211 ? 0.3256 0.3656 0.4419 -0.0437 0.1195 -0.0359 204 ARG A NE 1247 C CZ . ARG A 211 ? 0.2992 0.3504 0.4676 -0.0267 0.1121 -0.0387 204 ARG A CZ 1248 N NH1 . ARG A 211 ? 0.2751 0.3144 0.4798 -0.0484 0.1341 -0.0219 204 ARG A NH1 1249 N NH2 . ARG A 211 ? 0.2723 0.4004 0.5190 -0.0289 0.1285 -0.0288 204 ARG A NH2 1250 N N . TYR A 212 ? 0.2579 0.3071 0.3274 0.0087 0.0695 -0.0471 205 TYR A N 1251 C CA . TYR A 212 ? 0.2308 0.2968 0.3213 0.0034 0.0590 -0.0446 205 TYR A CA 1252 C C . TYR A 212 ? 0.2380 0.2940 0.3165 0.0092 0.0580 -0.0522 205 TYR A C 1253 O O . TYR A 212 ? 0.2124 0.3070 0.3041 -0.0036 0.0581 -0.0564 205 TYR A O 1254 C CB . TYR A 212 ? 0.2263 0.2848 0.3170 -0.0044 0.0628 -0.0436 205 TYR A CB 1255 C CG . TYR A 212 ? 0.2013 0.2659 0.2819 0.0118 0.0740 -0.0297 205 TYR A CG 1256 C CD1 . TYR A 212 ? 0.1861 0.2657 0.2571 0.0032 0.0374 -0.0799 205 TYR A CD1 1257 C CD2 . TYR A 212 ? 0.2190 0.2360 0.2618 0.0214 0.0435 -0.0453 205 TYR A CD2 1258 C CE1 . TYR A 212 ? 0.2039 0.2474 0.2896 0.0184 0.0517 -0.0517 205 TYR A CE1 1259 C CE2 . TYR A 212 ? 0.1878 0.2391 0.2757 0.0364 0.0449 -0.0697 205 TYR A CE2 1260 C CZ . TYR A 212 ? 0.1961 0.2563 0.2704 0.0222 0.0376 -0.0595 205 TYR A CZ 1261 O OH . TYR A 212 ? 0.2174 0.2455 0.2412 0.0165 0.0114 -0.0780 205 TYR A OH 1262 N N . GLY A 213 ? 0.2389 0.2829 0.3365 0.0179 0.0444 -0.0489 206 GLY A N 1263 C CA . GLY A 213 ? 0.2365 0.2677 0.3414 0.0077 0.0548 -0.0520 206 GLY A CA 1264 C C . GLY A 213 ? 0.2368 0.2733 0.3456 0.0012 0.0575 -0.0398 206 GLY A C 1265 O O . GLY A 213 ? 0.2391 0.2645 0.3388 0.0000 0.0702 -0.0320 206 GLY A O 1266 N N . LYS A 214 ? 0.2355 0.2711 0.3491 0.0029 0.0580 -0.0392 207 LYS A N 1267 C CA . LYS A 214 ? 0.2280 0.2861 0.3568 0.0081 0.0601 -0.0497 207 LYS A CA 1268 C C . LYS A 214 ? 0.2315 0.2819 0.3428 0.0008 0.0581 -0.0477 207 LYS A C 1269 O O . LYS A 214 ? 0.2416 0.2641 0.3492 -0.0211 0.0449 -0.0597 207 LYS A O 1270 C CB . LYS A 214 ? 0.2131 0.2822 0.3560 0.0093 0.0756 -0.0470 207 LYS A CB 1271 C CG . LYS A 214 ? 0.2121 0.3378 0.4206 0.0328 0.0458 -0.0492 207 LYS A CG 1272 C CD . LYS A 214 ? 0.2113 0.4113 0.4940 0.0205 0.0138 -0.0620 207 LYS A CD 1273 C CE . LYS A 214 ? 0.2125 0.4456 0.5136 0.0379 0.0060 -0.0765 207 LYS A CE 1274 N NZ . LYS A 214 ? 0.2747 0.5169 0.5578 0.0510 -0.0248 -0.1032 207 LYS A NZ 1275 N N . VAL A 215 ? 0.2276 0.2748 0.3307 -0.0070 0.0484 -0.0445 208 VAL A N 1276 C CA . VAL A 215 ? 0.2071 0.2738 0.3063 -0.0143 0.0546 -0.0395 208 VAL A CA 1277 C C . VAL A 215 ? 0.2050 0.2738 0.2961 -0.0072 0.0464 -0.0513 208 VAL A C 1278 O O . VAL A 215 ? 0.2030 0.2884 0.3198 -0.0013 0.0468 -0.0507 208 VAL A O 1279 C CB . VAL A 215 ? 0.2102 0.2779 0.3078 -0.0164 0.0514 -0.0415 208 VAL A CB 1280 C CG1 . VAL A 215 ? 0.2490 0.2893 0.2847 -0.0452 0.0507 -0.0350 208 VAL A CG1 1281 C CG2 . VAL A 215 ? 0.2050 0.2809 0.2762 -0.0369 0.0476 -0.0145 208 VAL A CG2 1282 N N . PHE A 216 ? 0.1837 0.2577 0.2588 -0.0008 0.0474 -0.0579 209 PHE A N 1283 C CA . PHE A 216 ? 0.1916 0.2423 0.2342 -0.0016 0.0394 -0.0512 209 PHE A CA 1284 C C . PHE A 216 ? 0.2062 0.2499 0.2436 0.0016 0.0425 -0.0489 209 PHE A C 1285 O O . PHE A 216 ? 0.2208 0.2461 0.2518 0.0008 0.0386 -0.0393 209 PHE A O 1286 C CB . PHE A 216 ? 0.1720 0.2384 0.2152 -0.0094 0.0398 -0.0506 209 PHE A CB 1287 C CG . PHE A 216 ? 0.1868 0.2380 0.2113 0.0028 0.0411 -0.0478 209 PHE A CG 1288 C CD1 . PHE A 216 ? 0.1865 0.2188 0.2231 0.0113 0.0333 -0.0677 209 PHE A CD1 1289 C CD2 . PHE A 216 ? 0.1599 0.2570 0.1887 -0.0118 0.0437 -0.0760 209 PHE A CD2 1290 C CE1 . PHE A 216 ? 0.2005 0.2273 0.2619 -0.0018 0.0427 -0.0528 209 PHE A CE1 1291 C CE2 . PHE A 216 ? 0.2086 0.2521 0.2679 -0.0095 0.0344 -0.0244 209 PHE A CE2 1292 C CZ . PHE A 216 ? 0.2259 0.2477 0.2623 0.0126 0.0287 -0.0409 209 PHE A CZ 1293 N N . ARG A 217 ? 0.2104 0.2316 0.2428 0.0082 0.0400 -0.0578 210 ARG A N 1294 C CA . ARG A 217 ? 0.2313 0.2451 0.2483 0.0035 0.0324 -0.0445 210 ARG A CA 1295 C C . ARG A 217 ? 0.2442 0.2505 0.2616 0.0029 0.0353 -0.0443 210 ARG A C 1296 O O . ARG A 217 ? 0.2341 0.2619 0.2531 0.0010 0.0195 -0.0364 210 ARG A O 1297 C CB . ARG A 217 ? 0.2357 0.2385 0.2540 -0.0033 0.0429 -0.0467 210 ARG A CB 1298 C CG . ARG A 217 ? 0.1671 0.2450 0.2371 -0.0037 0.0231 -0.0613 210 ARG A CG 1299 C CD . ARG A 217 ? 0.1400 0.2224 0.2716 -0.0072 0.0110 -0.0440 210 ARG A CD 1300 N NE . ARG A 217 ? 0.2426 0.2073 0.2032 -0.0041 0.0110 -0.0530 210 ARG A NE 1301 C CZ . ARG A 217 ? 0.2113 0.2711 0.2390 0.0302 0.0320 -0.0346 210 ARG A CZ 1302 N NH1 . ARG A 217 ? 0.2599 0.1787 0.2129 0.0678 0.0033 -0.0387 210 ARG A NH1 1303 N NH2 . ARG A 217 ? 0.2050 0.2204 0.2676 0.0559 0.0281 -0.0363 210 ARG A NH2 1304 N N . GLY A 218 ? 0.2475 0.2544 0.2768 -0.0057 0.0423 -0.0317 211 GLY A N 1305 C CA . GLY A 218 ? 0.2426 0.2583 0.2628 -0.0020 0.0293 -0.0272 211 GLY A CA 1306 C C . GLY A 218 ? 0.2509 0.2663 0.2517 0.0022 0.0374 -0.0332 211 GLY A C 1307 O O . GLY A 218 ? 0.2515 0.2487 0.1964 -0.0038 0.0424 -0.0535 211 GLY A O 1308 N N . ASN A 219 ? 0.2412 0.2521 0.2536 0.0072 0.0407 -0.0424 212 ASN A N 1309 C CA . ASN A 219 ? 0.2542 0.2694 0.2532 0.0152 0.0445 -0.0342 212 ASN A CA 1310 C C . ASN A 219 ? 0.2644 0.2787 0.2626 0.0120 0.0410 -0.0369 212 ASN A C 1311 O O . ASN A 219 ? 0.2685 0.2924 0.2721 0.0148 0.0358 -0.0080 212 ASN A O 1312 C CB . ASN A 219 ? 0.2720 0.2448 0.2339 0.0165 0.0409 -0.0511 212 ASN A CB 1313 C CG . ASN A 219 ? 0.2862 0.2682 0.2448 0.0227 0.0362 -0.0372 212 ASN A CG 1314 O OD1 . ASN A 219 ? 0.3568 0.2540 0.2582 0.0026 0.0688 -0.0289 212 ASN A OD1 1315 N ND2 . ASN A 219 ? 0.2387 0.2570 0.2061 0.0496 -0.0354 -0.0281 212 ASN A ND2 1316 N N . LYS A 220 ? 0.2569 0.2759 0.2781 0.0129 0.0510 -0.0369 213 LYS A N 1317 C CA . LYS A 220 ? 0.2608 0.2890 0.2510 0.0164 0.0501 -0.0408 213 LYS A CA 1318 C C . LYS A 220 ? 0.2589 0.2961 0.2593 0.0265 0.0505 -0.0279 213 LYS A C 1319 O O . LYS A 220 ? 0.2478 0.3016 0.2625 0.0243 0.0523 -0.0298 213 LYS A O 1320 C CB . LYS A 220 ? 0.2482 0.2752 0.2473 0.0173 0.0490 -0.0334 213 LYS A CB 1321 C CG . LYS A 220 ? 0.2225 0.2685 0.2765 -0.0007 0.0438 -0.0399 213 LYS A CG 1322 C CD . LYS A 220 ? 0.2030 0.2698 0.2596 0.0112 0.0648 -0.0203 213 LYS A CD 1323 C CE . LYS A 220 ? 0.1684 0.2629 0.2697 -0.0562 0.0802 -0.0183 213 LYS A CE 1324 N NZ . LYS A 220 ? 0.1690 0.2420 0.2708 -0.0427 0.1128 -0.0153 213 LYS A NZ 1325 N N . VAL A 221 ? 0.2535 0.2761 0.2519 0.0339 0.0544 -0.0264 214 VAL A N 1326 C CA . VAL A 221 ? 0.2761 0.2750 0.2532 0.0293 0.0533 -0.0261 214 VAL A CA 1327 C C . VAL A 221 ? 0.2898 0.3009 0.2514 0.0238 0.0549 -0.0298 214 VAL A C 1328 O O . VAL A 221 ? 0.2945 0.3041 0.2190 0.0245 0.0608 -0.0137 214 VAL A O 1329 C CB . VAL A 221 ? 0.2760 0.2744 0.2697 0.0332 0.0474 -0.0215 214 VAL A CB 1330 C CG1 . VAL A 221 ? 0.2899 0.2846 0.2626 0.0371 0.0391 -0.0359 214 VAL A CG1 1331 C CG2 . VAL A 221 ? 0.2685 0.2367 0.2896 0.0272 0.0522 -0.0035 214 VAL A CG2 1332 N N A LYS A 222 ? 0.2910 0.2933 0.2380 0.0226 0.0609 -0.0388 215 LYS A N 1333 N N B LYS A 222 ? 0.2943 0.2964 0.2410 0.0215 0.0612 -0.0377 215 LYS A N 1334 C CA A LYS A 222 ? 0.2987 0.3107 0.2396 0.0244 0.0570 -0.0360 215 LYS A CA 1335 C CA B LYS A 222 ? 0.3064 0.3170 0.2481 0.0219 0.0573 -0.0318 215 LYS A CA 1336 C C A LYS A 222 ? 0.3086 0.3265 0.2463 0.0215 0.0589 -0.0369 215 LYS A C 1337 C C B LYS A 222 ? 0.3119 0.3297 0.2509 0.0205 0.0588 -0.0359 215 LYS A C 1338 O O A LYS A 222 ? 0.3031 0.3409 0.2459 0.0258 0.0576 -0.0327 215 LYS A O 1339 O O B LYS A 222 ? 0.3059 0.3447 0.2527 0.0262 0.0561 -0.0325 215 LYS A O 1340 C CB A LYS A 222 ? 0.2893 0.2979 0.2351 0.0311 0.0590 -0.0405 215 LYS A CB 1341 C CB B LYS A 222 ? 0.3002 0.3051 0.2469 0.0257 0.0602 -0.0370 215 LYS A CB 1342 C CG A LYS A 222 ? 0.3091 0.2971 0.2473 0.0252 0.0491 -0.0486 215 LYS A CG 1343 C CG B LYS A 222 ? 0.3406 0.3188 0.2879 0.0083 0.0485 -0.0135 215 LYS A CG 1344 C CD A LYS A 222 ? 0.2907 0.3068 0.2790 0.0555 0.0826 -0.0614 215 LYS A CD 1345 C CD B LYS A 222 ? 0.3425 0.3202 0.3143 0.0149 0.0814 -0.0095 215 LYS A CD 1346 C CE A LYS A 222 ? 0.3163 0.3101 0.2709 0.0605 0.0952 -0.0734 215 LYS A CE 1347 C CE B LYS A 222 ? 0.3651 0.3424 0.3928 -0.0153 0.0530 0.0164 215 LYS A CE 1348 N NZ A LYS A 222 ? 0.3881 0.3415 0.3551 -0.0020 0.0586 -0.0645 215 LYS A NZ 1349 N NZ B LYS A 222 ? 0.3686 0.3205 0.4281 -0.0148 0.0482 0.0230 215 LYS A NZ 1350 N N . ASN A 223 ? 0.3030 0.3324 0.2478 0.0243 0.0618 -0.0412 216 ASN A N 1351 C CA . ASN A 223 ? 0.3239 0.3315 0.2409 0.0195 0.0690 -0.0395 216 ASN A CA 1352 C C . ASN A 223 ? 0.3495 0.3424 0.2501 0.0232 0.0707 -0.0392 216 ASN A C 1353 O O . ASN A 223 ? 0.3526 0.3240 0.2290 0.0309 0.0798 -0.0389 216 ASN A O 1354 C CB . ASN A 223 ? 0.2972 0.3138 0.2260 0.0290 0.0704 -0.0321 216 ASN A CB 1355 C CG . ASN A 223 ? 0.3190 0.3298 0.2426 0.0320 0.0643 -0.0302 216 ASN A CG 1356 O OD1 . ASN A 223 ? 0.3391 0.3257 0.1941 0.0512 0.0629 -0.0287 216 ASN A OD1 1357 N ND2 . ASN A 223 ? 0.3141 0.3157 0.2511 0.0181 0.0822 -0.0424 216 ASN A ND2 1358 N N . ALA A 224 ? 0.3571 0.3407 0.2670 0.0224 0.0718 -0.0428 217 ALA A N 1359 C CA . ALA A 224 ? 0.3865 0.3725 0.2760 0.0244 0.0680 -0.0384 217 ALA A CA 1360 C C . ALA A 224 ? 0.3986 0.3890 0.2940 0.0290 0.0691 -0.0382 217 ALA A C 1361 O O . ALA A 224 ? 0.3878 0.3878 0.2777 0.0440 0.0667 -0.0233 217 ALA A O 1362 C CB . ALA A 224 ? 0.3845 0.3536 0.2674 0.0177 0.0772 -0.0441 217 ALA A CB 1363 N N . GLN A 225 ? 0.4293 0.4150 0.3113 0.0288 0.0723 -0.0389 218 GLN A N 1364 C CA . GLN A 225 ? 0.4583 0.4603 0.3331 0.0254 0.0668 -0.0387 218 GLN A CA 1365 C C . GLN A 225 ? 0.4735 0.4800 0.3391 0.0308 0.0631 -0.0379 218 GLN A C 1366 O O . GLN A 225 ? 0.4870 0.4797 0.3369 0.0433 0.0607 -0.0390 218 GLN A O 1367 C CB . GLN A 225 ? 0.4602 0.4827 0.3319 0.0180 0.0708 -0.0474 218 GLN A CB 1368 C CG . GLN A 225 ? 0.5072 0.5351 0.3670 -0.0091 0.0907 -0.0287 218 GLN A CG 1369 C CD . GLN A 225 ? 0.5202 0.5830 0.4085 -0.0144 0.1234 -0.0019 218 GLN A CD 1370 O OE1 . GLN A 225 ? 0.4758 0.6203 0.3020 -0.0713 0.1071 0.0109 218 GLN A OE1 1371 N NE2 . GLN A 225 ? 0.5321 0.5861 0.4331 -0.0151 0.1529 -0.0269 218 GLN A NE2 1372 N N . LEU A 226 ? 0.4917 0.4718 0.3408 0.0360 0.0674 -0.0418 219 LEU A N 1373 C CA . LEU A 226 ? 0.5112 0.4888 0.3403 0.0353 0.0707 -0.0323 219 LEU A CA 1374 C C . LEU A 226 ? 0.5132 0.4795 0.3395 0.0308 0.0711 -0.0276 219 LEU A C 1375 O O . LEU A 226 ? 0.5210 0.4681 0.3085 0.0370 0.0754 -0.0129 219 LEU A O 1376 C CB . LEU A 226 ? 0.5283 0.4924 0.3559 0.0291 0.0538 -0.0400 219 LEU A CB 1377 C CG . LEU A 226 ? 0.5580 0.5360 0.3744 0.0458 0.0483 -0.0353 219 LEU A CG 1378 C CD1 . LEU A 226 ? 0.6319 0.5310 0.3811 0.0534 0.0331 -0.0185 219 LEU A CD1 1379 C CD2 . LEU A 226 ? 0.6085 0.6090 0.4174 0.0556 0.0329 -0.0015 219 LEU A CD2 1380 N N . ALA A 227 ? 0.4985 0.4739 0.3247 0.0281 0.0754 -0.0288 220 ALA A N 1381 C CA . ALA A 227 ? 0.4930 0.4641 0.3317 0.0231 0.0742 -0.0320 220 ALA A CA 1382 C C . ALA A 227 ? 0.4908 0.4612 0.3153 0.0264 0.0775 -0.0306 220 ALA A C 1383 O O . ALA A 227 ? 0.4967 0.4599 0.3214 0.0164 0.0732 -0.0285 220 ALA A O 1384 C CB . ALA A 227 ? 0.4802 0.4638 0.3316 0.0160 0.0764 -0.0349 220 ALA A CB 1385 N N . GLY A 228 ? 0.4933 0.4436 0.3094 0.0261 0.0683 -0.0302 221 GLY A N 1386 C CA . GLY A 228 ? 0.4887 0.4363 0.2872 0.0356 0.0736 -0.0412 221 GLY A CA 1387 C C . GLY A 228 ? 0.4813 0.4390 0.2818 0.0360 0.0734 -0.0425 221 GLY A C 1388 O O . GLY A 228 ? 0.4601 0.4258 0.2599 0.0386 0.0812 -0.0390 221 GLY A O 1389 N N . ALA A 229 ? 0.4711 0.4340 0.2828 0.0401 0.0673 -0.0552 222 ALA A N 1390 C CA . ALA A 229 ? 0.4635 0.4304 0.2749 0.0388 0.0708 -0.0484 222 ALA A CA 1391 C C . ALA A 229 ? 0.4675 0.4357 0.2674 0.0435 0.0641 -0.0509 222 ALA A C 1392 O O . ALA A 229 ? 0.4535 0.4332 0.2487 0.0619 0.0763 -0.0289 222 ALA A O 1393 C CB . ALA A 229 ? 0.4552 0.4165 0.2529 0.0420 0.0709 -0.0680 222 ALA A CB 1394 N N . LYS A 230 ? 0.4630 0.4281 0.2523 0.0431 0.0593 -0.0655 223 LYS A N 1395 C CA . LYS A 230 ? 0.4664 0.4293 0.2492 0.0354 0.0470 -0.0684 223 LYS A CA 1396 C C . LYS A 230 ? 0.4465 0.4137 0.2471 0.0336 0.0458 -0.0744 223 LYS A C 1397 O O . LYS A 230 ? 0.4356 0.4231 0.2280 0.0332 0.0354 -0.0711 223 LYS A O 1398 C CB . LYS A 230 ? 0.4794 0.4493 0.2657 0.0359 0.0518 -0.0748 223 LYS A CB 1399 C CG . LYS A 230 ? 0.5210 0.4560 0.2813 0.0510 0.0463 -0.0774 223 LYS A CG 1400 C CD . LYS A 230 ? 0.5577 0.5480 0.2533 0.0379 0.0359 -0.0911 223 LYS A CD 1401 C CE . LYS A 230 ? 0.5951 0.5572 0.2681 0.0500 0.0232 -0.1166 223 LYS A CE 1402 N NZ . LYS A 230 ? 0.6101 0.5382 0.1562 0.0508 0.0659 -0.1221 223 LYS A NZ 1403 N N . GLY A 231 ? 0.4247 0.3901 0.2453 0.0340 0.0383 -0.0745 224 GLY A N 1404 C CA . GLY A 231 ? 0.4002 0.3861 0.2446 0.0277 0.0467 -0.0809 224 GLY A CA 1405 C C . GLY A 231 ? 0.3826 0.3743 0.2426 0.0357 0.0530 -0.0780 224 GLY A C 1406 O O . GLY A 231 ? 0.3787 0.3701 0.2156 0.0343 0.0593 -0.0775 224 GLY A O 1407 N N . VAL A 232 ? 0.3742 0.3568 0.2671 0.0334 0.0530 -0.0630 225 VAL A N 1408 C CA . VAL A 232 ? 0.3670 0.3341 0.2684 0.0417 0.0501 -0.0683 225 VAL A CA 1409 C C . VAL A 232 ? 0.3533 0.3371 0.2840 0.0425 0.0609 -0.0725 225 VAL A C 1410 O O . VAL A 232 ? 0.3468 0.3125 0.2585 0.0384 0.0644 -0.0756 225 VAL A O 1411 C CB . VAL A 232 ? 0.3725 0.3273 0.2788 0.0362 0.0475 -0.0668 225 VAL A CB 1412 C CG1 . VAL A 232 ? 0.3676 0.3286 0.2450 0.0460 0.0378 -0.0598 225 VAL A CG1 1413 C CG2 . VAL A 232 ? 0.3866 0.3234 0.2621 0.0634 0.0353 -0.0890 225 VAL A CG2 1414 N N . ILE A 233 ? 0.3437 0.3302 0.2889 0.0455 0.0546 -0.0780 226 ILE A N 1415 C CA . ILE A 233 ? 0.3219 0.3168 0.2804 0.0489 0.0606 -0.0868 226 ILE A CA 1416 C C . ILE A 233 ? 0.3124 0.3100 0.2770 0.0548 0.0648 -0.0844 226 ILE A C 1417 O O . ILE A 233 ? 0.2964 0.2966 0.2676 0.0636 0.0640 -0.0950 226 ILE A O 1418 C CB . ILE A 233 ? 0.3308 0.3238 0.2798 0.0496 0.0607 -0.0863 226 ILE A CB 1419 C CG1 . ILE A 233 ? 0.3190 0.3306 0.2587 0.0458 0.0574 -0.0909 226 ILE A CG1 1420 C CG2 . ILE A 233 ? 0.3034 0.2953 0.2749 0.0493 0.0613 -0.0831 226 ILE A CG2 1421 C CD1 . ILE A 233 ? 0.3853 0.3437 0.2242 0.0615 0.0448 -0.0752 226 ILE A CD1 1422 N N . LEU A 234 ? 0.2967 0.2897 0.2857 0.0644 0.0755 -0.0840 227 LEU A N 1423 C CA . LEU A 234 ? 0.2851 0.2777 0.2898 0.0605 0.0819 -0.0774 227 LEU A CA 1424 C C . LEU A 234 ? 0.2809 0.2904 0.3088 0.0538 0.0833 -0.0795 227 LEU A C 1425 O O . LEU A 234 ? 0.2965 0.2816 0.3183 0.0485 0.0761 -0.0799 227 LEU A O 1426 C CB . LEU A 234 ? 0.2689 0.2564 0.2830 0.0676 0.0955 -0.0720 227 LEU A CB 1427 C CG . LEU A 234 ? 0.2583 0.2699 0.3059 0.0651 0.1154 -0.0553 227 LEU A CG 1428 C CD1 . LEU A 234 ? 0.2396 0.2616 0.2847 0.1343 0.1240 -0.0613 227 LEU A CD1 1429 C CD2 . LEU A 234 ? 0.2757 0.2313 0.3427 0.0749 0.1239 -0.0457 227 LEU A CD2 1430 N N . TYR A 235 ? 0.2680 0.2809 0.3175 0.0449 0.0836 -0.0816 228 TYR A N 1431 C CA . TYR A 235 ? 0.2682 0.3036 0.3299 0.0394 0.0816 -0.0779 228 TYR A CA 1432 C C . TYR A 235 ? 0.2667 0.3095 0.3406 0.0396 0.0832 -0.0748 228 TYR A C 1433 O O . TYR A 235 ? 0.2689 0.3074 0.3371 0.0571 0.0891 -0.0842 228 TYR A O 1434 C CB . TYR A 235 ? 0.2510 0.2773 0.3404 0.0367 0.0878 -0.0792 228 TYR A CB 1435 C CG . TYR A 235 ? 0.2443 0.2906 0.3378 0.0401 0.0845 -0.0848 228 TYR A CG 1436 C CD1 . TYR A 235 ? 0.2141 0.2911 0.3154 0.0184 0.0840 -0.0986 228 TYR A CD1 1437 C CD2 . TYR A 235 ? 0.2308 0.3091 0.3234 0.0257 0.0804 -0.0659 228 TYR A CD2 1438 C CE1 . TYR A 235 ? 0.2587 0.3269 0.3550 0.0264 0.0843 -0.0756 228 TYR A CE1 1439 C CE2 . TYR A 235 ? 0.2427 0.3248 0.3543 0.0423 0.0882 -0.0696 228 TYR A CE2 1440 C CZ . TYR A 235 ? 0.2322 0.3414 0.3281 0.0372 0.1071 -0.0671 228 TYR A CZ 1441 O OH . TYR A 235 ? 0.2601 0.3696 0.3637 0.0266 0.0963 -0.0577 228 TYR A OH 1442 N N . SER A 236 ? 0.2722 0.3151 0.3525 0.0364 0.0876 -0.0713 229 SER A N 1443 C CA . SER A 236 ? 0.2544 0.3123 0.3517 0.0369 0.0899 -0.0643 229 SER A CA 1444 C C . SER A 236 ? 0.2547 0.3203 0.3614 0.0338 0.0905 -0.0697 229 SER A C 1445 O O . SER A 236 ? 0.2582 0.3209 0.3612 0.0280 0.0725 -0.0823 229 SER A O 1446 C CB . SER A 236 ? 0.2417 0.3001 0.3435 0.0349 0.1046 -0.0637 229 SER A CB 1447 O OG . SER A 236 ? 0.2420 0.2786 0.3262 0.0092 0.1174 -0.0318 229 SER A OG 1448 N N . ASP A 237 ? 0.2454 0.3198 0.3746 0.0266 0.0840 -0.0735 230 ASP A N 1449 C CA . ASP A 237 ? 0.2535 0.3271 0.3885 0.0213 0.0939 -0.0714 230 ASP A CA 1450 C C . ASP A 237 ? 0.2436 0.3188 0.4047 0.0242 0.0885 -0.0686 230 ASP A C 1451 O O . ASP A 237 ? 0.2412 0.3275 0.3972 0.0178 0.0804 -0.0529 230 ASP A O 1452 C CB . ASP A 237 ? 0.2524 0.3230 0.3783 0.0177 0.0928 -0.0717 230 ASP A CB 1453 C CG . ASP A 237 ? 0.2790 0.3458 0.4055 -0.0015 0.1084 -0.0652 230 ASP A CG 1454 O OD1 . ASP A 237 ? 0.3153 0.3353 0.4091 -0.0474 0.1311 -0.0299 230 ASP A OD1 1455 O OD2 . ASP A 237 ? 0.2747 0.3427 0.4265 -0.0384 0.1117 -0.0706 230 ASP A OD2 1456 N N . PRO A 238 ? 0.2583 0.3285 0.4293 0.0243 0.0853 -0.0748 231 PRO A N 1457 C CA . PRO A 238 ? 0.2611 0.3311 0.4416 0.0344 0.0769 -0.0761 231 PRO A CA 1458 C C . PRO A 238 ? 0.2654 0.3485 0.4605 0.0321 0.0758 -0.0715 231 PRO A C 1459 O O . PRO A 238 ? 0.2509 0.3468 0.4640 0.0387 0.0632 -0.0701 231 PRO A O 1460 C CB . PRO A 238 ? 0.2884 0.3426 0.4445 0.0286 0.0839 -0.0791 231 PRO A CB 1461 C CG . PRO A 238 ? 0.2888 0.3169 0.4317 0.0319 0.0795 -0.0833 231 PRO A CG 1462 C CD . PRO A 238 ? 0.2355 0.3257 0.4242 0.0314 0.0847 -0.0801 231 PRO A CD 1463 N N . ALA A 239 ? 0.2557 0.3511 0.4631 0.0222 0.0791 -0.0649 232 ALA A N 1464 C CA . ALA A 239 ? 0.2891 0.3635 0.4705 0.0176 0.0786 -0.0619 232 ALA A CA 1465 C C . ALA A 239 ? 0.2804 0.3641 0.4632 0.0148 0.0763 -0.0605 232 ALA A C 1466 O O . ALA A 239 ? 0.2668 0.3544 0.4752 -0.0067 0.0752 -0.0578 232 ALA A O 1467 C CB . ALA A 239 ? 0.2999 0.3773 0.4747 0.0098 0.0750 -0.0587 232 ALA A CB 1468 N N . ASP A 240 ? 0.2838 0.3565 0.4480 0.0227 0.0691 -0.0564 233 ASP A N 1469 C CA . ASP A 240 ? 0.2699 0.3404 0.4399 0.0269 0.0655 -0.0507 233 ASP A CA 1470 C C . ASP A 240 ? 0.2643 0.3348 0.4397 0.0315 0.0597 -0.0535 233 ASP A C 1471 O O . ASP A 240 ? 0.2965 0.3130 0.4270 0.0187 0.0545 -0.0574 233 ASP A O 1472 C CB . ASP A 240 ? 0.2649 0.3296 0.4283 0.0267 0.0626 -0.0459 233 ASP A CB 1473 C CG . ASP A 240 ? 0.2769 0.3276 0.4368 0.0201 0.0530 -0.0479 233 ASP A CG 1474 O OD1 . ASP A 240 ? 0.2424 0.3100 0.4672 -0.0238 0.0569 -0.0265 233 ASP A OD1 1475 O OD2 . ASP A 240 ? 0.2687 0.2927 0.3972 0.0372 0.0684 -0.0398 233 ASP A OD2 1476 N N . TYR A 241 ? 0.2199 0.3091 0.4308 0.0457 0.0506 -0.0599 234 TYR A N 1477 C CA . TYR A 241 ? 0.2333 0.3229 0.4324 0.0511 0.0462 -0.0548 234 TYR A CA 1478 C C . TYR A 241 ? 0.2431 0.3328 0.4414 0.0536 0.0430 -0.0560 234 TYR A C 1479 O O . TYR A 241 ? 0.2582 0.3358 0.4549 0.0491 0.0367 -0.0539 234 TYR A O 1480 C CB . TYR A 241 ? 0.2084 0.3243 0.4145 0.0501 0.0570 -0.0431 234 TYR A CB 1481 C CG . TYR A 241 ? 0.2270 0.3192 0.4076 0.0508 0.0472 -0.0448 234 TYR A CG 1482 C CD1 . TYR A 241 ? 0.1908 0.3000 0.3941 0.0298 0.0482 -0.0399 234 TYR A CD1 1483 C CD2 . TYR A 241 ? 0.1910 0.3209 0.3622 0.0482 0.0407 -0.0592 234 TYR A CD2 1484 C CE1 . TYR A 241 ? 0.1641 0.2949 0.3490 0.0223 0.0158 -0.0304 234 TYR A CE1 1485 C CE2 . TYR A 241 ? 0.2654 0.3321 0.3779 0.0583 0.0278 -0.0166 234 TYR A CE2 1486 C CZ . TYR A 241 ? 0.2396 0.3180 0.3568 0.0688 0.0166 -0.0451 234 TYR A CZ 1487 O OH . TYR A 241 ? 0.2312 0.2885 0.3003 0.0934 0.0281 -0.0371 234 TYR A OH 1488 N N . PHE A 242 ? 0.2429 0.3468 0.4574 0.0632 0.0375 -0.0642 235 PHE A N 1489 C CA . PHE A 242 ? 0.2543 0.3549 0.4825 0.0605 0.0429 -0.0679 235 PHE A CA 1490 C C . PHE A 242 ? 0.2565 0.3744 0.5075 0.0583 0.0376 -0.0660 235 PHE A C 1491 O O . PHE A 242 ? 0.2349 0.3645 0.5037 0.0411 0.0364 -0.0588 235 PHE A O 1492 C CB . PHE A 242 ? 0.2525 0.3478 0.4777 0.0671 0.0377 -0.0708 235 PHE A CB 1493 C CG . PHE A 242 ? 0.2749 0.3346 0.4594 0.0767 0.0663 -0.0870 235 PHE A CG 1494 C CD1 . PHE A 242 ? 0.2895 0.3318 0.4377 0.0709 0.0683 -0.0959 235 PHE A CD1 1495 C CD2 . PHE A 242 ? 0.2613 0.3289 0.4529 0.0975 0.0910 -0.0757 235 PHE A CD2 1496 C CE1 . PHE A 242 ? 0.2760 0.3433 0.4607 0.0636 0.1098 -0.0679 235 PHE A CE1 1497 C CE2 . PHE A 242 ? 0.3043 0.3211 0.4943 0.0734 0.0773 -0.0648 235 PHE A CE2 1498 C CZ . PHE A 242 ? 0.2824 0.3345 0.4833 0.0837 0.0797 -0.0867 235 PHE A CZ 1499 N N . ALA A 243 ? 0.2754 0.3896 0.5247 0.0591 0.0390 -0.0729 236 ALA A N 1500 C CA . ALA A 243 ? 0.2973 0.4068 0.5576 0.0520 0.0387 -0.0806 236 ALA A CA 1501 C C . ALA A 243 ? 0.3069 0.4237 0.5866 0.0494 0.0375 -0.0779 236 ALA A C 1502 O O . ALA A 243 ? 0.2934 0.4256 0.5740 0.0551 0.0387 -0.0874 236 ALA A O 1503 C CB . ALA A 243 ? 0.3074 0.4149 0.5534 0.0458 0.0454 -0.0816 236 ALA A CB 1504 N N . PRO A 244 ? 0.3212 0.4453 0.6250 0.0459 0.0320 -0.0779 237 PRO A N 1505 C CA . PRO A 244 ? 0.3296 0.4465 0.6452 0.0474 0.0331 -0.0808 237 PRO A CA 1506 C C . PRO A 244 ? 0.3256 0.4522 0.6546 0.0466 0.0258 -0.0809 237 PRO A C 1507 O O . PRO A 244 ? 0.3290 0.4467 0.6557 0.0480 0.0229 -0.0850 237 PRO A O 1508 C CB . PRO A 244 ? 0.3362 0.4559 0.6635 0.0488 0.0321 -0.0789 237 PRO A CB 1509 C CG . PRO A 244 ? 0.3504 0.4702 0.6690 0.0418 0.0327 -0.0663 237 PRO A CG 1510 C CD . PRO A 244 ? 0.3224 0.4473 0.6349 0.0486 0.0412 -0.0747 237 PRO A CD 1511 N N . GLY A 245 ? 0.3133 0.4443 0.6549 0.0483 0.0207 -0.0831 238 GLY A N 1512 C CA . GLY A 245 ? 0.3063 0.4518 0.6503 0.0526 0.0096 -0.0747 238 GLY A CA 1513 C C . GLY A 245 ? 0.3124 0.4532 0.6423 0.0669 0.0055 -0.0750 238 GLY A C 1514 O O . GLY A 245 ? 0.3081 0.4661 0.6682 0.0706 -0.0118 -0.0652 238 GLY A O 1515 N N . VAL A 246 ? 0.2919 0.4178 0.6224 0.0912 0.0191 -0.0872 239 VAL A N 1516 C CA . VAL A 246 ? 0.2789 0.3895 0.5916 0.0919 0.0189 -0.0985 239 VAL A CA 1517 C C . VAL A 246 ? 0.2751 0.3956 0.5901 0.0987 0.0221 -0.0915 239 VAL A C 1518 O O . VAL A 246 ? 0.2804 0.4089 0.5905 0.0933 0.0166 -0.1008 239 VAL A O 1519 C CB . VAL A 246 ? 0.2868 0.3884 0.5961 0.0899 0.0209 -0.0976 239 VAL A CB 1520 C CG1 A VAL A 246 ? 0.2741 0.3652 0.5861 0.1070 0.0144 -0.0905 239 VAL A CG1 1521 C CG1 B VAL A 246 ? 0.2510 0.3687 0.5632 0.0918 0.0224 -0.1196 239 VAL A CG1 1522 C CG2 A VAL A 246 ? 0.2754 0.3645 0.5701 0.1012 0.0117 -0.1100 239 VAL A CG2 1523 C CG2 B VAL A 246 ? 0.2684 0.3751 0.5797 0.0813 0.0159 -0.1073 239 VAL A CG2 1524 N N . LYS A 247 ? 0.2606 0.3880 0.5879 0.0963 0.0217 -0.0922 240 LYS A N 1525 C CA . LYS A 247 ? 0.2821 0.3933 0.5825 0.0948 0.0265 -0.0863 240 LYS A CA 1526 C C . LYS A 247 ? 0.2869 0.3783 0.5621 0.0799 0.0281 -0.0805 240 LYS A C 1527 O O . LYS A 247 ? 0.2636 0.3732 0.5590 0.0804 0.0416 -0.0877 240 LYS A O 1528 C CB . LYS A 247 ? 0.2759 0.3950 0.5904 0.1024 0.0217 -0.0805 240 LYS A CB 1529 C CG . LYS A 247 ? 0.2639 0.4459 0.6146 0.1246 0.0294 -0.0915 240 LYS A CG 1530 C CD . LYS A 247 ? 0.2592 0.4713 0.6347 0.1559 0.0401 -0.1005 240 LYS A CD 1531 C CE . LYS A 247 ? 0.2762 0.4811 0.6693 0.1738 0.0630 -0.0948 240 LYS A CE 1532 N NZ . LYS A 247 ? 0.2571 0.4691 0.6872 0.1923 0.0689 -0.0809 240 LYS A NZ 1533 N N . SER A 248 ? 0.3097 0.3780 0.5434 0.0655 0.0304 -0.0729 241 SER A N 1534 C CA . SER A 248 ? 0.3133 0.3824 0.5265 0.0653 0.0306 -0.0730 241 SER A CA 1535 C C . SER A 248 ? 0.3089 0.3629 0.5013 0.0744 0.0313 -0.0818 241 SER A C 1536 O O . SER A 248 ? 0.2949 0.3221 0.4821 0.0801 0.0331 -0.0953 241 SER A O 1537 C CB . SER A 248 ? 0.3277 0.4304 0.5235 0.0534 0.0332 -0.0587 241 SER A CB 1538 O OG . SER A 248 ? 0.3446 0.4894 0.5536 0.0489 0.0257 -0.0055 241 SER A OG 1539 N N . TYR A 249 ? 0.3092 0.3353 0.5014 0.0797 0.0239 -0.0800 242 TYR A N 1540 C CA . TYR A 249 ? 0.3030 0.3193 0.4913 0.0882 0.0245 -0.0788 242 TYR A CA 1541 C C . TYR A 249 ? 0.3127 0.3199 0.4936 0.0830 0.0153 -0.0795 242 TYR A C 1542 O O . TYR A 249 ? 0.2926 0.3168 0.4916 0.0960 0.0194 -0.0807 242 TYR A O 1543 C CB . TYR A 249 ? 0.2961 0.3063 0.4815 0.0899 0.0163 -0.0723 242 TYR A CB 1544 C CG . TYR A 249 ? 0.2818 0.2914 0.4766 0.1157 0.0172 -0.0551 242 TYR A CG 1545 C CD1 . TYR A 249 ? 0.2742 0.2581 0.4631 0.1475 0.0398 -0.0572 242 TYR A CD1 1546 C CD2 . TYR A 249 ? 0.2810 0.3393 0.4691 0.1148 0.0020 -0.0407 242 TYR A CD2 1547 C CE1 . TYR A 249 ? 0.2902 0.3161 0.4490 0.1667 0.0658 -0.0804 242 TYR A CE1 1548 C CE2 . TYR A 249 ? 0.3357 0.3480 0.4855 0.1088 0.0372 -0.0579 242 TYR A CE2 1549 C CZ . TYR A 249 ? 0.3572 0.3314 0.4601 0.1297 0.0761 -0.0790 242 TYR A CZ 1550 O OH . TYR A 249 ? 0.5325 0.3565 0.4569 0.1740 0.0923 -0.0519 242 TYR A OH 1551 N N . PRO A 250 ? 0.3362 0.3167 0.5060 0.0794 0.0107 -0.0805 243 PRO A N 1552 C CA . PRO A 250 ? 0.3460 0.3238 0.5141 0.0773 0.0079 -0.0805 243 PRO A CA 1553 C C . PRO A 250 ? 0.3559 0.3274 0.5234 0.0876 0.0027 -0.0837 243 PRO A C 1554 O O . PRO A 250 ? 0.3619 0.3314 0.5193 0.0991 -0.0035 -0.0874 243 PRO A O 1555 C CB . PRO A 250 ? 0.3470 0.3130 0.5145 0.0763 0.0102 -0.0811 243 PRO A CB 1556 C CG . PRO A 250 ? 0.3575 0.2952 0.5110 0.0657 0.0258 -0.0799 243 PRO A CG 1557 C CD . PRO A 250 ? 0.3412 0.3187 0.5042 0.0806 0.0086 -0.0806 243 PRO A CD 1558 N N . ASP A 251 ? 0.3320 0.3128 0.5270 0.0968 0.0071 -0.0887 244 ASP A N 1559 C CA . ASP A 251 ? 0.3547 0.3267 0.5385 0.0947 -0.0024 -0.0930 244 ASP A CA 1560 C C . ASP A 251 ? 0.3259 0.3244 0.5352 0.0947 -0.0135 -0.0851 244 ASP A C 1561 O O . ASP A 251 ? 0.3109 0.3222 0.5474 0.1002 -0.0290 -0.0875 244 ASP A O 1562 C CB . ASP A 251 ? 0.3610 0.3355 0.5546 0.1023 0.0047 -0.0930 244 ASP A CB 1563 C CG . ASP A 251 ? 0.4608 0.3731 0.5876 0.0954 0.0128 -0.1150 244 ASP A CG 1564 O OD1 . ASP A 251 ? 0.5034 0.3536 0.6271 0.1327 -0.0027 -0.1060 244 ASP A OD1 1565 O OD2 . ASP A 251 ? 0.5814 0.4624 0.6114 0.1004 0.0530 -0.1354 244 ASP A OD2 1566 N N . GLY A 252 ? 0.2877 0.3083 0.5132 0.0955 -0.0239 -0.0812 245 GLY A N 1567 C CA . GLY A 252 ? 0.2739 0.3060 0.4906 0.1028 -0.0155 -0.0758 245 GLY A CA 1568 C C . GLY A 252 ? 0.2751 0.3070 0.4759 0.0900 -0.0148 -0.0732 245 GLY A C 1569 O O . GLY A 252 ? 0.2798 0.2956 0.4908 0.0830 -0.0285 -0.0666 245 GLY A O 1570 N N . TRP A 253 ? 0.2571 0.2921 0.4530 0.0779 -0.0108 -0.0766 246 TRP A N 1571 C CA . TRP A 253 ? 0.2456 0.2997 0.4426 0.0713 0.0000 -0.0814 246 TRP A CA 1572 C C . TRP A 253 ? 0.2489 0.3086 0.4339 0.0599 0.0089 -0.0813 246 TRP A C 1573 O O . TRP A 253 ? 0.2519 0.2980 0.4232 0.0506 0.0014 -0.0767 246 TRP A O 1574 C CB . TRP A 253 ? 0.2296 0.3185 0.4336 0.0741 -0.0002 -0.0829 246 TRP A CB 1575 C CG . TRP A 253 ? 0.2613 0.3190 0.4449 0.0667 -0.0031 -0.0870 246 TRP A CG 1576 C CD1 . TRP A 253 ? 0.2589 0.3510 0.4805 0.0604 -0.0261 -0.0764 246 TRP A CD1 1577 C CD2 . TRP A 253 ? 0.2720 0.3431 0.4778 0.0793 -0.0007 -0.0646 246 TRP A CD2 1578 N NE1 . TRP A 253 ? 0.2547 0.3472 0.5021 0.0512 -0.0455 -0.0661 246 TRP A NE1 1579 C CE2 . TRP A 253 ? 0.2692 0.3602 0.4799 0.0628 -0.0257 -0.0644 246 TRP A CE2 1580 C CE3 . TRP A 253 ? 0.2391 0.3540 0.4780 0.1047 -0.0070 -0.0624 246 TRP A CE3 1581 C CZ2 . TRP A 253 ? 0.2644 0.3566 0.4993 0.0819 -0.0167 -0.0822 246 TRP A CZ2 1582 C CZ3 . TRP A 253 ? 0.2616 0.3915 0.5024 0.0681 -0.0124 -0.0667 246 TRP A CZ3 1583 C CH2 . TRP A 253 ? 0.2260 0.3889 0.4731 0.1048 -0.0049 -0.0870 246 TRP A CH2 1584 N N . ASN A 254 ? 0.2387 0.3104 0.4280 0.0515 0.0224 -0.0781 247 ASN A N 1585 C CA . ASN A 254 ? 0.2388 0.3308 0.4340 0.0484 0.0282 -0.0722 247 ASN A CA 1586 C C . ASN A 254 ? 0.2459 0.3202 0.4307 0.0508 0.0285 -0.0749 247 ASN A C 1587 O O . ASN A 254 ? 0.2290 0.3171 0.4277 0.0414 0.0434 -0.0622 247 ASN A O 1588 C CB . ASN A 254 ? 0.2207 0.3417 0.4289 0.0485 0.0311 -0.0653 247 ASN A CB 1589 C CG . ASN A 254 ? 0.2201 0.3418 0.4387 0.0461 0.0392 -0.0615 247 ASN A CG 1590 O OD1 . ASN A 254 ? 0.2152 0.3590 0.4361 0.0627 0.0273 -0.0516 247 ASN A OD1 1591 N ND2 . ASN A 254 ? 0.1742 0.3837 0.3807 -0.0019 0.0346 -0.0595 247 ASN A ND2 1592 N N . LEU A 255 ? 0.2551 0.2976 0.4189 0.0591 0.0297 -0.0740 248 LEU A N 1593 C CA . LEU A 255 ? 0.2573 0.2976 0.4167 0.0547 0.0276 -0.0737 248 LEU A CA 1594 C C . LEU A 255 ? 0.2659 0.3019 0.4126 0.0466 0.0296 -0.0764 248 LEU A C 1595 O O . LEU A 255 ? 0.2614 0.2992 0.4155 0.0484 0.0256 -0.0828 248 LEU A O 1596 C CB . LEU A 255 ? 0.2507 0.2934 0.4123 0.0441 0.0187 -0.0655 248 LEU A CB 1597 C CG . LEU A 255 ? 0.2723 0.2933 0.3873 0.0507 0.0212 -0.0540 248 LEU A CG 1598 C CD1 . LEU A 255 ? 0.2594 0.2486 0.3220 0.0489 0.0111 -0.0623 248 LEU A CD1 1599 C CD2 . LEU A 255 ? 0.3195 0.2781 0.4078 0.0514 0.0146 -0.0509 248 LEU A CD2 1600 N N . PRO A 256 ? 0.2633 0.2959 0.4135 0.0484 0.0329 -0.0770 249 PRO A N 1601 C CA . PRO A 256 ? 0.2672 0.2944 0.4106 0.0436 0.0361 -0.0805 249 PRO A CA 1602 C C . PRO A 256 ? 0.2720 0.2863 0.4007 0.0401 0.0436 -0.0815 249 PRO A C 1603 O O . PRO A 256 ? 0.2777 0.2844 0.3830 0.0482 0.0359 -0.0854 249 PRO A O 1604 C CB . PRO A 256 ? 0.2777 0.3041 0.4035 0.0362 0.0440 -0.0747 249 PRO A CB 1605 C CG . PRO A 256 ? 0.2608 0.3191 0.4397 0.0433 0.0413 -0.0813 249 PRO A CG 1606 C CD . PRO A 256 ? 0.2622 0.2865 0.4168 0.0429 0.0423 -0.0806 249 PRO A CD 1607 N N . GLY A 257 ? 0.2615 0.2852 0.4029 0.0468 0.0494 -0.0832 250 GLY A N 1608 C CA . GLY A 257 ? 0.2792 0.2905 0.3972 0.0465 0.0498 -0.0954 250 GLY A CA 1609 C C . GLY A 257 ? 0.2926 0.2933 0.4035 0.0471 0.0467 -0.0874 250 GLY A C 1610 O O . GLY A 257 ? 0.3175 0.2642 0.4116 0.0473 0.0400 -0.0794 250 GLY A O 1611 N N . GLY A 258 ? 0.2835 0.2848 0.3895 0.0446 0.0525 -0.0790 251 GLY A N 1612 C CA . GLY A 258 ? 0.2861 0.2843 0.3870 0.0612 0.0523 -0.0748 251 GLY A CA 1613 C C . GLY A 258 ? 0.2746 0.2728 0.3753 0.0622 0.0516 -0.0751 251 GLY A C 1614 O O . GLY A 258 ? 0.2857 0.2630 0.3835 0.0626 0.0571 -0.0686 251 GLY A O 1615 N N . GLY A 259 ? 0.2765 0.2539 0.3678 0.0656 0.0512 -0.0756 252 GLY A N 1616 C CA . GLY A 259 ? 0.2535 0.2498 0.3456 0.0507 0.0501 -0.0804 252 GLY A CA 1617 C C . GLY A 259 ? 0.2551 0.2456 0.3385 0.0539 0.0522 -0.0850 252 GLY A C 1618 O O . GLY A 259 ? 0.2723 0.2370 0.3197 0.0501 0.0459 -0.0882 252 GLY A O 1619 N N . VAL A 260 ? 0.2477 0.2530 0.3315 0.0483 0.0418 -0.0822 253 VAL A N 1620 C CA . VAL A 260 ? 0.2438 0.2404 0.3115 0.0489 0.0452 -0.0850 253 VAL A CA 1621 C C . VAL A 260 ? 0.2605 0.2452 0.3133 0.0405 0.0381 -0.0789 253 VAL A C 1622 O O . VAL A 260 ? 0.2385 0.2497 0.2960 0.0446 0.0576 -0.0716 253 VAL A O 1623 C CB . VAL A 260 ? 0.2473 0.2292 0.3149 0.0529 0.0316 -0.0963 253 VAL A CB 1624 C CG1 . VAL A 260 ? 0.2092 0.2339 0.2940 0.0496 0.0395 -0.1060 253 VAL A CG1 1625 C CG2 . VAL A 260 ? 0.2190 0.2652 0.2768 0.0694 0.0569 -0.0938 253 VAL A CG2 1626 N N . GLN A 261 ? 0.2646 0.2278 0.3125 0.0303 0.0354 -0.0790 254 GLN A N 1627 C CA . GLN A 261 ? 0.2351 0.2320 0.3003 0.0326 0.0429 -0.0829 254 GLN A CA 1628 C C . GLN A 261 ? 0.2477 0.2396 0.2915 0.0258 0.0386 -0.0785 254 GLN A C 1629 O O . GLN A 261 ? 0.2651 0.2457 0.2677 0.0256 0.0498 -0.0948 254 GLN A O 1630 C CB . GLN A 261 ? 0.2408 0.2261 0.3006 0.0273 0.0352 -0.0897 254 GLN A CB 1631 C CG . GLN A 261 ? 0.1968 0.2136 0.3030 0.0367 0.0132 -0.0912 254 GLN A CG 1632 C CD . GLN A 261 ? 0.2049 0.2537 0.3075 0.0484 0.0049 -0.0635 254 GLN A CD 1633 O OE1 . GLN A 261 ? 0.1969 0.2594 0.2857 0.0441 -0.0393 -0.0719 254 GLN A OE1 1634 N NE2 . GLN A 261 ? 0.1855 0.2537 0.2812 0.0504 0.0085 -0.0469 254 GLN A NE2 1635 N N . ARG A 262 ? 0.2107 0.2408 0.2660 0.0316 0.0485 -0.0776 255 ARG A N 1636 C CA . ARG A 262 ? 0.2278 0.2394 0.2789 0.0276 0.0338 -0.0636 255 ARG A CA 1637 C C . ARG A 262 ? 0.2167 0.2376 0.2708 0.0333 0.0375 -0.0580 255 ARG A C 1638 O O . ARG A 262 ? 0.2137 0.2479 0.2905 0.0279 0.0190 -0.0624 255 ARG A O 1639 C CB . ARG A 262 ? 0.1917 0.2190 0.2757 0.0197 0.0354 -0.0603 255 ARG A CB 1640 C CG . ARG A 262 ? 0.2437 0.2249 0.2750 0.0259 0.0375 -0.0714 255 ARG A CG 1641 C CD . ARG A 262 ? 0.2652 0.1986 0.2923 -0.0046 0.0470 -0.0731 255 ARG A CD 1642 N NE . ARG A 262 ? 0.2164 0.2051 0.3082 -0.0013 0.0072 -0.0506 255 ARG A NE 1643 C CZ . ARG A 262 ? 0.2274 0.2332 0.2662 -0.0049 0.0133 -0.0388 255 ARG A CZ 1644 N NH1 . ARG A 262 ? 0.1732 0.2328 0.2459 -0.0196 0.0052 -0.0418 255 ARG A NH1 1645 N NH2 . ARG A 262 ? 0.2220 0.2316 0.2611 0.0169 0.0004 -0.0503 255 ARG A NH2 1646 N N . GLY A 263 ? 0.2170 0.2409 0.2642 0.0311 0.0426 -0.0466 256 GLY A N 1647 C CA . GLY A 263 ? 0.2141 0.2018 0.2490 0.0273 0.0362 -0.0399 256 GLY A CA 1648 C C . GLY A 263 ? 0.2029 0.2210 0.2417 0.0154 0.0354 -0.0409 256 GLY A C 1649 O O . GLY A 263 ? 0.2044 0.2222 0.2323 0.0117 0.0348 -0.0382 256 GLY A O 1650 N N . ASN A 264 ? 0.2123 0.1917 0.2336 0.0199 0.0357 -0.0338 257 ASN A N 1651 C CA . ASN A 264 ? 0.2002 0.2165 0.2071 0.0119 0.0177 -0.0381 257 ASN A CA 1652 C C . ASN A 264 ? 0.2011 0.2189 0.2115 0.0087 0.0167 -0.0293 257 ASN A C 1653 O O . ASN A 264 ? 0.2010 0.1965 0.2155 0.0066 0.0175 -0.0190 257 ASN A O 1654 C CB . ASN A 264 ? 0.1951 0.2072 0.2032 0.0098 0.0220 -0.0475 257 ASN A CB 1655 C CG . ASN A 264 ? 0.2156 0.2288 0.2243 0.0073 0.0072 -0.0400 257 ASN A CG 1656 O OD1 . ASN A 264 ? 0.2270 0.2192 0.2621 0.0191 -0.0352 -0.0496 257 ASN A OD1 1657 N ND2 . ASN A 264 ? 0.2133 0.2306 0.2177 0.0276 -0.0115 -0.0543 257 ASN A ND2 1658 N N . ILE A 265 ? 0.1955 0.2317 0.1886 0.0250 0.0192 -0.0346 258 ILE A N 1659 C CA . ILE A 265 ? 0.2088 0.2398 0.2037 0.0227 0.0221 -0.0419 258 ILE A CA 1660 C C . ILE A 265 ? 0.2314 0.2507 0.2187 0.0251 0.0235 -0.0384 258 ILE A C 1661 O O . ILE A 265 ? 0.2316 0.2599 0.2086 0.0422 0.0141 -0.0377 258 ILE A O 1662 C CB . ILE A 265 ? 0.2126 0.2578 0.2003 0.0195 0.0109 -0.0510 258 ILE A CB 1663 C CG1 . ILE A 265 ? 0.2773 0.2598 0.1902 -0.0218 0.0329 -0.0790 258 ILE A CG1 1664 C CG2 . ILE A 265 ? 0.2289 0.2521 0.2052 0.0284 0.0450 -0.0366 258 ILE A CG2 1665 C CD1 . ILE A 265 ? 0.2565 0.3402 0.2156 -0.0125 0.0559 -0.0869 258 ILE A CD1 1666 N N . LEU A 266 ? 0.2222 0.2449 0.2114 0.0285 0.0252 -0.0487 259 LEU A N 1667 C CA . LEU A 266 ? 0.2429 0.2378 0.2304 0.0142 0.0263 -0.0298 259 LEU A CA 1668 C C . LEU A 266 ? 0.2392 0.2469 0.2255 0.0071 0.0283 -0.0287 259 LEU A C 1669 O O . LEU A 266 ? 0.2455 0.2709 0.2252 -0.0019 0.0392 -0.0259 259 LEU A O 1670 C CB . LEU A 266 ? 0.2274 0.2187 0.2264 0.0145 0.0329 -0.0258 259 LEU A CB 1671 C CG . LEU A 266 ? 0.2335 0.2431 0.2278 -0.0077 0.0176 -0.0334 259 LEU A CG 1672 C CD1 . LEU A 266 ? 0.2629 0.2581 0.2113 -0.0055 0.0460 -0.0311 259 LEU A CD1 1673 C CD2 . LEU A 266 ? 0.2801 0.2038 0.2356 -0.0289 0.0043 -0.0490 259 LEU A CD2 1674 N N . ASN A 267 ? 0.2531 0.2375 0.2188 0.0039 0.0278 -0.0139 260 ASN A N 1675 C CA . ASN A 267 ? 0.2424 0.2414 0.2092 0.0023 0.0252 -0.0182 260 ASN A CA 1676 C C . ASN A 267 ? 0.2343 0.2366 0.2058 -0.0033 0.0182 -0.0202 260 ASN A C 1677 O O . ASN A 267 ? 0.2290 0.2325 0.2410 0.0047 0.0139 -0.0173 260 ASN A O 1678 C CB . ASN A 267 ? 0.2455 0.2554 0.2203 -0.0044 0.0362 -0.0125 260 ASN A CB 1679 C CG . ASN A 267 ? 0.2795 0.2886 0.2374 -0.0041 0.0276 -0.0136 260 ASN A CG 1680 O OD1 . ASN A 267 ? 0.3261 0.3087 0.2759 -0.0368 -0.0017 0.0017 260 ASN A OD1 1681 N ND2 . ASN A 267 ? 0.3300 0.2849 0.1906 0.0177 0.0444 0.0112 260 ASN A ND2 1682 N N . LEU A 268 ? 0.2177 0.2175 0.2022 -0.0046 0.0234 -0.0229 261 LEU A N 1683 C CA . LEU A 268 ? 0.2333 0.2124 0.1981 0.0024 0.0149 -0.0125 261 LEU A CA 1684 C C . LEU A 268 ? 0.2351 0.2128 0.2082 0.0098 0.0125 -0.0062 261 LEU A C 1685 O O . LEU A 268 ? 0.2103 0.2164 0.1983 0.0200 -0.0040 0.0092 261 LEU A O 1686 C CB . LEU A 268 ? 0.2246 0.1959 0.1920 0.0013 0.0158 -0.0053 261 LEU A CB 1687 C CG . LEU A 268 ? 0.2179 0.1869 0.1718 -0.0232 0.0037 0.0023 261 LEU A CG 1688 C CD1 . LEU A 268 ? 0.2274 0.2132 0.1589 -0.0152 0.0262 0.0062 261 LEU A CD1 1689 C CD2 . LEU A 268 ? 0.2651 0.2074 0.1221 -0.0170 -0.0202 -0.0244 261 LEU A CD2 1690 N N . ASN A 269 ? 0.2314 0.2031 0.1965 0.0044 0.0000 0.0013 262 ASN A N 1691 C CA . ASN A 269 ? 0.2436 0.2218 0.1915 0.0030 0.0086 -0.0087 262 ASN A CA 1692 C C . ASN A 269 ? 0.2251 0.2268 0.2034 -0.0006 0.0063 -0.0116 262 ASN A C 1693 O O . ASN A 269 ? 0.2280 0.2206 0.2176 -0.0109 -0.0012 -0.0250 262 ASN A O 1694 C CB . ASN A 269 ? 0.2387 0.2157 0.1920 0.0191 0.0063 -0.0024 262 ASN A CB 1695 C CG . ASN A 269 ? 0.2761 0.2524 0.2067 -0.0007 0.0085 0.0082 262 ASN A CG 1696 O OD1 . ASN A 269 ? 0.2788 0.3088 0.2192 -0.0040 0.0585 0.0153 262 ASN A OD1 1697 N ND2 . ASN A 269 ? 0.2917 0.2978 0.1470 -0.0247 0.0220 -0.0069 262 ASN A ND2 1698 N N . GLY A 270 ? 0.2067 0.2209 0.1869 -0.0098 0.0072 -0.0042 263 GLY A N 1699 C CA . GLY A 270 ? 0.1922 0.2188 0.1908 -0.0094 0.0137 -0.0118 263 GLY A CA 1700 C C . GLY A 270 ? 0.1993 0.2215 0.1860 -0.0058 0.0107 -0.0117 263 GLY A C 1701 O O . GLY A 270 ? 0.2034 0.2228 0.2125 -0.0012 0.0206 -0.0247 263 GLY A O 1702 N N . ALA A 271 ? 0.1976 0.1930 0.1731 -0.0090 0.0018 -0.0169 264 ALA A N 1703 C CA . ALA A 271 ? 0.2069 0.2154 0.1672 -0.0073 0.0059 -0.0108 264 ALA A CA 1704 C C . ALA A 271 ? 0.2020 0.2139 0.1685 -0.0088 0.0061 -0.0148 264 ALA A C 1705 O O . ALA A 271 ? 0.2207 0.2628 0.1585 -0.0040 0.0066 -0.0159 264 ALA A O 1706 C CB . ALA A 271 ? 0.2224 0.1969 0.1692 -0.0179 -0.0082 -0.0266 264 ALA A CB 1707 N N . GLY A 272 ? 0.1962 0.2057 0.1564 0.0008 0.0022 -0.0173 265 GLY A N 1708 C CA . GLY A 272 ? 0.1918 0.1926 0.1660 -0.0213 -0.0030 -0.0283 265 GLY A CA 1709 C C . GLY A 272 ? 0.2002 0.2167 0.2058 -0.0169 0.0064 -0.0237 265 GLY A C 1710 O O . GLY A 272 ? 0.2076 0.2256 0.1940 -0.0333 0.0151 -0.0272 265 GLY A O 1711 N N . ASP A 273 ? 0.2167 0.2128 0.2227 -0.0226 0.0040 -0.0230 266 ASP A N 1712 C CA . ASP A 273 ? 0.2087 0.2214 0.2096 -0.0098 0.0013 -0.0296 266 ASP A CA 1713 C C . ASP A 273 ? 0.2122 0.2312 0.2128 -0.0024 0.0069 -0.0403 266 ASP A C 1714 O O . ASP A 273 ? 0.2123 0.2416 0.2002 0.0111 0.0008 -0.0198 266 ASP A O 1715 C CB . ASP A 273 ? 0.1940 0.2372 0.2285 -0.0134 0.0202 -0.0387 266 ASP A CB 1716 C CG . ASP A 273 ? 0.2135 0.2454 0.2108 -0.0109 0.0118 -0.0274 266 ASP A CG 1717 O OD1 . ASP A 273 ? 0.1798 0.2545 0.2716 -0.0001 -0.0048 -0.0534 266 ASP A OD1 1718 O OD2 . ASP A 273 ? 0.2312 0.2590 0.2341 -0.0006 -0.0134 -0.0158 266 ASP A OD2 1719 N N . PRO A 274 ? 0.2117 0.2440 0.2066 0.0138 0.0088 -0.0380 267 PRO A N 1720 C CA . PRO A 274 ? 0.2242 0.2373 0.2030 0.0206 0.0037 -0.0372 267 PRO A CA 1721 C C . PRO A 274 ? 0.2176 0.2303 0.2112 0.0164 0.0063 -0.0379 267 PRO A C 1722 O O . PRO A 274 ? 0.2395 0.2559 0.1935 0.0182 0.0076 -0.0191 267 PRO A O 1723 C CB . PRO A 274 ? 0.2296 0.2372 0.2170 0.0332 0.0061 -0.0369 267 PRO A CB 1724 C CG . PRO A 274 ? 0.2592 0.2549 0.2159 0.0265 0.0045 -0.0220 267 PRO A CG 1725 C CD . PRO A 274 ? 0.2421 0.2370 0.1989 0.0146 0.0225 -0.0542 267 PRO A CD 1726 N N . LEU A 275 ? 0.2184 0.2358 0.2028 0.0087 -0.0081 -0.0404 268 LEU A N 1727 C CA . LEU A 275 ? 0.2066 0.2225 0.2160 0.0004 -0.0143 -0.0408 268 LEU A CA 1728 C C . LEU A 275 ? 0.2063 0.2026 0.2092 -0.0028 -0.0117 -0.0315 268 LEU A C 1729 O O . LEU A 275 ? 0.2082 0.2177 0.2351 -0.0086 0.0026 -0.0165 268 LEU A O 1730 C CB . LEU A 275 ? 0.2163 0.2032 0.1972 0.0053 -0.0204 -0.0504 268 LEU A CB 1731 C CG . LEU A 275 ? 0.2208 0.2114 0.2183 0.0086 -0.0280 -0.0570 268 LEU A CG 1732 C CD1 . LEU A 275 ? 0.2664 0.1751 0.2729 0.0175 -0.0560 -0.0479 268 LEU A CD1 1733 C CD2 . LEU A 275 ? 0.2341 0.2984 0.2052 0.0160 0.0029 -0.0635 268 LEU A CD2 1734 N N . THR A 276 ? 0.2016 0.2054 0.2107 -0.0191 -0.0035 -0.0271 269 THR A N 1735 C CA . THR A 276 ? 0.1996 0.2017 0.2091 -0.0090 -0.0013 -0.0284 269 THR A CA 1736 C C . THR A 276 ? 0.2060 0.2148 0.1990 -0.0135 -0.0026 -0.0171 269 THR A C 1737 O O . THR A 276 ? 0.2314 0.2193 0.2124 -0.0190 -0.0075 -0.0253 269 THR A O 1738 C CB . THR A 276 ? 0.1901 0.1988 0.1965 -0.0215 -0.0075 -0.0268 269 THR A CB 1739 O OG1 . THR A 276 ? 0.2114 0.2066 0.2132 0.0081 0.0040 -0.0204 269 THR A OG1 1740 C CG2 . THR A 276 ? 0.1468 0.2055 0.2190 0.0119 0.0064 -0.0210 269 THR A CG2 1741 N N . PRO A 277 ? 0.2010 0.2214 0.2031 -0.0053 -0.0080 -0.0123 270 PRO A N 1742 C CA . PRO A 277 ? 0.2139 0.2139 0.1959 -0.0097 -0.0027 -0.0207 270 PRO A CA 1743 C C . PRO A 277 ? 0.2082 0.2267 0.2026 -0.0046 0.0021 -0.0126 270 PRO A C 1744 O O . PRO A 277 ? 0.2297 0.1898 0.2171 0.0047 0.0066 0.0098 270 PRO A O 1745 C CB . PRO A 277 ? 0.2071 0.2208 0.1630 -0.0110 0.0012 -0.0116 270 PRO A CB 1746 C CG . PRO A 277 ? 0.1825 0.2019 0.1942 -0.0309 -0.0245 -0.0125 270 PRO A CG 1747 C CD . PRO A 277 ? 0.2147 0.2118 0.1771 -0.0099 -0.0140 -0.0088 270 PRO A CD 1748 N N . GLY A 278 ? 0.2186 0.2178 0.1880 -0.0186 -0.0050 -0.0246 271 GLY A N 1749 C CA . GLY A 278 ? 0.1960 0.2075 0.1902 -0.0042 -0.0076 -0.0188 271 GLY A CA 1750 C C . GLY A 278 ? 0.2151 0.2251 0.2053 0.0008 -0.0105 -0.0210 271 GLY A C 1751 O O . GLY A 278 ? 0.2325 0.2242 0.2131 0.0142 -0.0081 -0.0177 271 GLY A O 1752 N N . TYR A 279 ? 0.2134 0.1920 0.2110 0.0061 -0.0102 -0.0076 272 TYR A N 1753 C CA . TYR A 279 ? 0.2019 0.2108 0.2123 0.0111 -0.0072 -0.0029 272 TYR A CA 1754 C C . TYR A 279 ? 0.1975 0.2086 0.2152 0.0139 -0.0028 -0.0023 272 TYR A C 1755 O O . TYR A 279 ? 0.2004 0.2260 0.2120 0.0170 -0.0238 0.0036 272 TYR A O 1756 C CB . TYR A 279 ? 0.2102 0.1879 0.2105 0.0290 -0.0056 -0.0030 272 TYR A CB 1757 C CG . TYR A 279 ? 0.2156 0.2138 0.2410 0.0101 0.0029 -0.0077 272 TYR A CG 1758 C CD1 . TYR A 279 ? 0.1840 0.1873 0.2652 0.0113 0.0217 -0.0123 272 TYR A CD1 1759 C CD2 . TYR A 279 ? 0.1809 0.2159 0.2401 0.0133 -0.0137 0.0110 272 TYR A CD2 1760 C CE1 . TYR A 279 ? 0.1742 0.2216 0.2281 0.0572 -0.0229 0.0208 272 TYR A CE1 1761 C CE2 . TYR A 279 ? 0.2106 0.1890 0.2165 0.0241 -0.0208 -0.0124 272 TYR A CE2 1762 C CZ . TYR A 279 ? 0.1399 0.2097 0.2128 0.0268 -0.0103 0.0067 272 TYR A CZ 1763 O OH . TYR A 279 ? 0.1965 0.1878 0.1872 0.0397 -0.0181 -0.0202 272 TYR A OH 1764 N N . PRO A 280 ? 0.2128 0.2175 0.2321 0.0104 0.0027 -0.0053 273 PRO A N 1765 C CA . PRO A 280 ? 0.2195 0.2126 0.2399 0.0055 0.0048 -0.0063 273 PRO A CA 1766 C C . PRO A 280 ? 0.2173 0.2231 0.2421 0.0071 0.0054 -0.0114 273 PRO A C 1767 O O . PRO A 280 ? 0.2047 0.2341 0.2386 -0.0048 0.0130 -0.0165 273 PRO A O 1768 C CB . PRO A 280 ? 0.2050 0.2219 0.2294 0.0167 0.0159 -0.0116 273 PRO A CB 1769 C CG . PRO A 280 ? 0.2161 0.2087 0.2509 0.0101 0.0183 -0.0001 273 PRO A CG 1770 C CD . PRO A 280 ? 0.2085 0.2185 0.2397 0.0055 0.0203 -0.0055 273 PRO A CD 1771 N N . ALA A 281 ? 0.2058 0.2085 0.2271 0.0006 0.0288 -0.0120 274 ALA A N 1772 C CA . ALA A 281 ? 0.1964 0.2148 0.2532 0.0054 0.0208 -0.0188 274 ALA A CA 1773 C C . ALA A 281 ? 0.1946 0.2262 0.2820 0.0013 0.0156 -0.0248 274 ALA A C 1774 O O . ALA A 281 ? 0.1759 0.2588 0.2876 0.0162 0.0109 -0.0174 274 ALA A O 1775 C CB . ALA A 281 ? 0.1748 0.2062 0.2338 0.0164 0.0228 -0.0084 274 ALA A CB 1776 N N . ASN A 282 ? 0.2066 0.2322 0.3034 0.0115 0.0222 -0.0289 275 ASN A N 1777 C CA . ASN A 282 ? 0.2312 0.2539 0.3424 0.0028 0.0218 -0.0228 275 ASN A CA 1778 C C . ASN A 282 ? 0.2517 0.2667 0.3661 0.0007 0.0183 -0.0170 275 ASN A C 1779 O O . ASN A 282 ? 0.2377 0.2599 0.3751 -0.0015 0.0149 -0.0329 275 ASN A O 1780 C CB . ASN A 282 ? 0.2332 0.2572 0.3362 0.0120 0.0351 -0.0205 275 ASN A CB 1781 C CG . ASN A 282 ? 0.2408 0.2775 0.3620 0.0020 0.0244 -0.0358 275 ASN A CG 1782 O OD1 . ASN A 282 ? 0.2190 0.2863 0.3495 0.0377 0.0301 -0.0380 275 ASN A OD1 1783 N ND2 . ASN A 282 ? 0.2553 0.2988 0.3941 -0.0072 0.0481 -0.0644 275 ASN A ND2 1784 N N C GLU A 283 ? 0.2609 0.2857 0.3881 -0.0045 0.0091 -0.0145 276 GLU A N 1785 N N D GLU A 283 ? 0.2611 0.2869 0.3897 -0.0016 0.0130 -0.0120 276 GLU A N 1786 C CA C GLU A 283 ? 0.2735 0.3061 0.4061 -0.0076 0.0057 -0.0133 276 GLU A CA 1787 C CA D GLU A 283 ? 0.2711 0.3084 0.4070 -0.0038 0.0159 -0.0104 276 GLU A CA 1788 C C C GLU A 283 ? 0.2756 0.3025 0.4004 -0.0029 0.0068 -0.0133 276 GLU A C 1789 C C D GLU A 283 ? 0.2769 0.3057 0.3993 -0.0004 0.0154 -0.0099 276 GLU A C 1790 O O C GLU A 283 ? 0.2734 0.2958 0.4030 -0.0050 0.0096 -0.0243 276 GLU A O 1791 O O D GLU A 283 ? 0.2868 0.2998 0.4053 0.0019 0.0208 -0.0245 276 GLU A O 1792 C CB C GLU A 283 ? 0.2931 0.3076 0.4100 -0.0107 0.0070 -0.0072 276 GLU A CB 1793 C CB D GLU A 283 ? 0.2819 0.3155 0.4119 -0.0031 0.0237 -0.0019 276 GLU A CB 1794 C CG C GLU A 283 ? 0.3100 0.3700 0.4498 -0.0275 -0.0106 -0.0109 276 GLU A CG 1795 C CG D GLU A 283 ? 0.2949 0.3195 0.4456 -0.0145 0.0490 -0.0184 276 GLU A CG 1796 C CD C GLU A 283 ? 0.3229 0.4074 0.4749 0.0012 -0.0286 -0.0116 276 GLU A CD 1797 C CD D GLU A 283 ? 0.2658 0.3456 0.4947 -0.0070 0.0684 -0.0241 276 GLU A CD 1798 O OE1 C GLU A 283 ? 0.2208 0.4543 0.4397 -0.0416 -0.0643 -0.0104 276 GLU A OE1 1799 O OE1 D GLU A 283 ? 0.2527 0.3257 0.5032 -0.0217 0.1048 -0.0268 276 GLU A OE1 1800 O OE2 C GLU A 283 ? 0.3641 0.4438 0.4865 -0.0513 -0.0909 -0.0329 276 GLU A OE2 1801 O OE2 D GLU A 283 ? 0.3003 0.3648 0.4980 -0.0174 0.1161 -0.0484 276 GLU A OE2 1802 N N . TYR A 284 ? 0.2658 0.2914 0.3953 0.0017 0.0100 -0.0139 277 TYR A N 1803 C CA . TYR A 284 ? 0.2604 0.2985 0.3842 0.0076 0.0080 -0.0180 277 TYR A CA 1804 C C . TYR A 284 ? 0.2639 0.3010 0.3534 0.0077 -0.0010 -0.0256 277 TYR A C 1805 O O . TYR A 284 ? 0.2619 0.3110 0.3579 0.0015 0.0038 -0.0346 277 TYR A O 1806 C CB . TYR A 284 ? 0.2589 0.2914 0.3854 0.0202 0.0022 -0.0199 277 TYR A CB 1807 C CG . TYR A 284 ? 0.2380 0.2919 0.4034 0.0173 0.0158 -0.0275 277 TYR A CG 1808 C CD1 . TYR A 284 ? 0.2649 0.3267 0.4210 -0.0015 0.0447 -0.0361 277 TYR A CD1 1809 C CD2 . TYR A 284 ? 0.1723 0.3077 0.3714 0.0210 0.0625 -0.0430 277 TYR A CD2 1810 C CE1 . TYR A 284 ? 0.2876 0.3148 0.4127 0.0171 0.0309 -0.0449 277 TYR A CE1 1811 C CE2 . TYR A 284 ? 0.2865 0.3017 0.4204 -0.0053 0.0586 -0.0299 277 TYR A CE2 1812 C CZ . TYR A 284 ? 0.3028 0.3072 0.4197 0.0091 0.0353 -0.0230 277 TYR A CZ 1813 O OH . TYR A 284 ? 0.3152 0.2826 0.4629 -0.0105 0.0254 -0.0032 277 TYR A OH 1814 N N . ALA A 285 ? 0.2495 0.3124 0.3355 0.0094 0.0014 -0.0235 278 ALA A N 1815 C CA . ALA A 285 ? 0.2722 0.3328 0.3587 0.0089 -0.0158 -0.0101 278 ALA A CA 1816 C C . ALA A 285 ? 0.3010 0.3342 0.3568 0.0080 -0.0107 -0.0149 278 ALA A C 1817 O O . ALA A 285 ? 0.2948 0.3058 0.3454 0.0007 -0.0117 -0.0023 278 ALA A O 1818 C CB . ALA A 285 ? 0.2551 0.3592 0.3721 -0.0025 -0.0071 -0.0062 278 ALA A CB 1819 N N . TYR A 286 ? 0.3152 0.3305 0.3545 0.0077 -0.0092 -0.0082 279 TYR A N 1820 C CA . TYR A 286 ? 0.3270 0.3384 0.3643 0.0159 -0.0184 -0.0180 279 TYR A CA 1821 C C . TYR A 286 ? 0.3064 0.3345 0.3473 -0.0075 -0.0245 -0.0239 279 TYR A C 1822 O O . TYR A 286 ? 0.3446 0.3178 0.3909 -0.0549 0.0024 -0.0406 279 TYR A O 1823 C CB . TYR A 286 ? 0.3680 0.3532 0.3789 0.0360 -0.0080 -0.0163 279 TYR A CB 1824 C CG A TYR A 286 ? 0.3186 0.3355 0.3633 0.0572 -0.0399 -0.0233 279 TYR A CG 1825 C CG B TYR A 286 ? 0.3812 0.3431 0.3890 0.0504 -0.0023 -0.0271 279 TYR A CG 1826 C CD1 A TYR A 286 ? 0.2647 0.3353 0.3543 0.0897 -0.0323 -0.0112 279 TYR A CD1 1827 C CD1 B TYR A 286 ? 0.3956 0.3513 0.4006 0.0841 -0.0167 -0.0416 279 TYR A CD1 1828 C CD2 A TYR A 286 ? 0.3135 0.3150 0.3485 0.0859 -0.0355 -0.0189 279 TYR A CD2 1829 C CD2 B TYR A 286 ? 0.3877 0.3456 0.4046 0.0616 -0.0064 -0.0493 279 TYR A CD2 1830 C CE1 A TYR A 286 ? 0.2950 0.3570 0.3791 0.0741 -0.0448 -0.0412 279 TYR A CE1 1831 C CE1 B TYR A 286 ? 0.4042 0.3477 0.4141 0.0903 -0.0108 -0.0383 279 TYR A CE1 1832 C CE2 A TYR A 286 ? 0.3053 0.3316 0.3654 0.0894 -0.0459 -0.0320 279 TYR A CE2 1833 C CE2 B TYR A 286 ? 0.4158 0.3764 0.3988 0.1112 -0.0154 -0.0314 279 TYR A CE2 1834 C CZ A TYR A 286 ? 0.3241 0.3510 0.3594 0.0844 -0.0714 -0.0230 279 TYR A CZ 1835 C CZ B TYR A 286 ? 0.4092 0.3855 0.4153 0.0979 -0.0152 -0.0391 279 TYR A CZ 1836 O OH A TYR A 286 ? 0.3525 0.3821 0.3839 0.0952 -0.1360 -0.0009 279 TYR A OH 1837 O OH B TYR A 286 ? 0.4327 0.4660 0.4130 0.1267 -0.0393 0.0071 279 TYR A OH 1838 N N . ARG A 287 ? 0.2727 0.3063 0.3046 -0.0024 -0.0286 -0.0261 280 ARG A N 1839 C CA . ARG A 287 ? 0.2613 0.3041 0.3058 -0.0026 -0.0387 -0.0236 280 ARG A CA 1840 C C . ARG A 287 ? 0.2646 0.3116 0.3049 -0.0070 -0.0377 -0.0339 280 ARG A C 1841 O O . ARG A 287 ? 0.2609 0.3162 0.2694 -0.0354 -0.0685 -0.0298 280 ARG A O 1842 C CB A ARG A 287 ? 0.2623 0.3159 0.3178 0.0108 -0.0298 -0.0246 280 ARG A CB 1843 C CB B ARG A 287 ? 0.2492 0.2942 0.2936 0.0090 -0.0277 -0.0232 280 ARG A CB 1844 C CG A ARG A 287 ? 0.2552 0.3499 0.3218 -0.0134 -0.0506 -0.0056 280 ARG A CG 1845 C CG B ARG A 287 ? 0.1940 0.2255 0.2808 0.0236 -0.0152 -0.0127 280 ARG A CG 1846 C CD A ARG A 287 ? 0.2908 0.4084 0.3787 -0.0357 -0.0503 0.0202 280 ARG A CD 1847 C CD B ARG A 287 ? 0.1018 0.1513 0.1874 0.0158 0.0176 -0.0223 280 ARG A CD 1848 N NE A ARG A 287 ? 0.2918 0.3754 0.3967 -0.0336 -0.0487 0.0203 280 ARG A NE 1849 N NE B ARG A 287 ? 0.0721 0.0876 0.2092 0.0539 -0.0020 -0.0073 280 ARG A NE 1850 C CZ A ARG A 287 ? 0.2896 0.3838 0.4056 -0.0142 -0.0320 0.0208 280 ARG A CZ 1851 C CZ B ARG A 287 ? 0.0597 0.0887 0.1981 0.0457 -0.0103 0.0076 280 ARG A CZ 1852 N NH1 A ARG A 287 ? 0.2910 0.4351 0.4425 -0.0273 -0.0279 0.0292 280 ARG A NH1 1853 N NH1 B ARG A 287 ? 0.0408 0.1121 0.2178 -0.0226 -0.0071 0.0174 280 ARG A NH1 1854 N NH2 A ARG A 287 ? 0.2613 0.3375 0.4116 0.0034 -0.0188 0.0249 280 ARG A NH2 1855 N NH2 B ARG A 287 ? 0.0572 0.1011 0.1912 0.0419 -0.0030 -0.0156 280 ARG A NH2 1856 N N . ARG A 288 ? 0.2635 0.2985 0.3055 -0.0172 -0.0370 -0.0509 281 ARG A N 1857 C CA . ARG A 288 ? 0.3008 0.3181 0.2981 -0.0125 -0.0368 -0.0603 281 ARG A CA 1858 C C . ARG A 288 ? 0.3198 0.3366 0.2934 -0.0121 -0.0380 -0.0654 281 ARG A C 1859 O O . ARG A 288 ? 0.3059 0.3117 0.2552 0.0093 -0.0343 -0.0779 281 ARG A O 1860 C CB . ARG A 288 ? 0.3021 0.3102 0.2948 -0.0273 -0.0303 -0.0516 281 ARG A CB 1861 C CG . ARG A 288 ? 0.3018 0.3395 0.3063 -0.0480 -0.0208 -0.0786 281 ARG A CG 1862 C CD . ARG A 288 ? 0.3150 0.3610 0.3567 -0.0543 -0.0121 -0.0777 281 ARG A CD 1863 N NE . ARG A 288 ? 0.2772 0.3547 0.3522 -0.0288 -0.0222 -0.0600 281 ARG A NE 1864 C CZ . ARG A 288 ? 0.3272 0.3602 0.3817 -0.0285 0.0338 -0.0315 281 ARG A CZ 1865 N NH1 . ARG A 288 ? 0.2254 0.3919 0.3819 -0.0448 0.0074 0.0028 281 ARG A NH1 1866 N NH2 . ARG A 288 ? 0.3490 0.3250 0.4179 -0.0164 -0.0011 -0.0131 281 ARG A NH2 1867 N N . GLY A 289 ? 0.3088 0.3570 0.2805 -0.0103 -0.0472 -0.0585 282 GLY A N 1868 C CA . GLY A 289 ? 0.3561 0.3956 0.2871 -0.0092 -0.0456 -0.0679 282 GLY A CA 1869 C C . GLY A 289 ? 0.3709 0.4104 0.3041 -0.0026 -0.0407 -0.0713 282 GLY A C 1870 O O . GLY A 289 ? 0.3566 0.4416 0.2843 -0.0055 -0.0390 -0.0785 282 GLY A O 1871 N N . ILE A 290 ? 0.3988 0.4194 0.3278 0.0048 -0.0463 -0.0786 283 ILE A N 1872 C CA . ILE A 290 ? 0.4079 0.4379 0.3494 0.0052 -0.0443 -0.0801 283 ILE A CA 1873 C C . ILE A 290 ? 0.4149 0.4511 0.3494 0.0088 -0.0377 -0.0765 283 ILE A C 1874 O O . ILE A 290 ? 0.4023 0.4758 0.3447 0.0057 -0.0313 -0.0759 283 ILE A O 1875 C CB A ILE A 290 ? 0.4138 0.4481 0.3592 0.0079 -0.0442 -0.0811 283 ILE A CB 1876 C CB B ILE A 290 ? 0.4089 0.4381 0.3517 0.0053 -0.0449 -0.0790 283 ILE A CB 1877 C CG1 A ILE A 290 ? 0.4166 0.4384 0.3733 0.0177 -0.0552 -0.0769 283 ILE A CG1 1878 C CG1 B ILE A 290 ? 0.4022 0.4303 0.3517 0.0096 -0.0552 -0.0735 283 ILE A CG1 1879 C CG2 A ILE A 290 ? 0.4298 0.4759 0.3542 0.0074 -0.0424 -0.0925 283 ILE A CG2 1880 C CG2 B ILE A 290 ? 0.3997 0.4293 0.3376 0.0077 -0.0598 -0.0870 283 ILE A CG2 1881 C CD1 A ILE A 290 ? 0.4196 0.4250 0.3746 0.0356 -0.0506 -0.0793 283 ILE A CD1 1882 C CD1 B ILE A 290 ? 0.3724 0.4216 0.3605 0.0077 -0.0494 -0.0812 283 ILE A CD1 1883 N N . ALA A 291 ? 0.4231 0.4725 0.3528 0.0094 -0.0380 -0.0689 284 ALA A N 1884 C CA . ALA A 291 ? 0.4311 0.4789 0.3534 0.0111 -0.0285 -0.0611 284 ALA A CA 1885 C C . ALA A 291 ? 0.4336 0.4858 0.3660 0.0022 -0.0291 -0.0477 284 ALA A C 1886 O O . ALA A 291 ? 0.4459 0.5121 0.3720 -0.0039 -0.0094 -0.0373 284 ALA A O 1887 C CB . ALA A 291 ? 0.4310 0.4952 0.3575 0.0165 -0.0224 -0.0613 284 ALA A CB 1888 N N . GLU A 292 ? 0.4197 0.4785 0.3662 0.0048 -0.0232 -0.0451 285 GLU A N 1889 C CA . GLU A 292 ? 0.4118 0.4718 0.3629 0.0020 -0.0277 -0.0364 285 GLU A CA 1890 C C . GLU A 292 ? 0.3747 0.4402 0.3423 -0.0115 -0.0209 -0.0350 285 GLU A C 1891 O O . GLU A 292 ? 0.3725 0.4356 0.3045 -0.0275 -0.0151 -0.0337 285 GLU A O 1892 C CB . GLU A 292 ? 0.4240 0.4913 0.3953 0.0100 -0.0329 -0.0362 285 GLU A CB 1893 C CG . GLU A 292 ? 0.5044 0.5465 0.4367 0.0139 -0.0340 -0.0071 285 GLU A CG 1894 C CD . GLU A 292 ? 0.6134 0.6228 0.5117 0.0017 -0.0325 -0.0181 285 GLU A CD 1895 O OE1 . GLU A 292 ? 0.6463 0.6271 0.5755 -0.0058 -0.0243 0.0195 285 GLU A OE1 1896 O OE2 . GLU A 292 ? 0.6991 0.7110 0.5470 0.0150 -0.0253 0.0283 285 GLU A OE2 1897 N N . ALA A 293 ? 0.3341 0.4192 0.3136 -0.0208 -0.0217 -0.0272 286 ALA A N 1898 C CA . ALA A 293 ? 0.3128 0.3920 0.3019 -0.0235 -0.0124 -0.0298 286 ALA A CA 1899 C C . ALA A 293 ? 0.3112 0.3873 0.2898 -0.0167 -0.0125 -0.0363 286 ALA A C 1900 O O . ALA A 293 ? 0.3151 0.3969 0.2847 -0.0282 -0.0023 -0.0135 286 ALA A O 1901 C CB . ALA A 293 ? 0.2762 0.3738 0.2647 -0.0180 -0.0114 -0.0284 286 ALA A CB 1902 N N . VAL A 294 ? 0.2793 0.3409 0.2571 0.0042 -0.0102 -0.0505 287 VAL A N 1903 C CA . VAL A 294 ? 0.2678 0.3184 0.2531 0.0111 0.0014 -0.0546 287 VAL A CA 1904 C C . VAL A 294 ? 0.2693 0.3094 0.2421 0.0129 -0.0136 -0.0538 287 VAL A C 1905 O O . VAL A 294 ? 0.2845 0.2922 0.2414 0.0168 -0.0196 -0.0591 287 VAL A O 1906 C CB . VAL A 294 ? 0.2584 0.3067 0.2628 0.0128 -0.0111 -0.0591 287 VAL A CB 1907 C CG1 . VAL A 294 ? 0.2242 0.3105 0.2231 0.0040 -0.0140 -0.0214 287 VAL A CG1 1908 C CG2 . VAL A 294 ? 0.2345 0.3238 0.2817 0.0278 0.0660 -0.0419 287 VAL A CG2 1909 N N . GLY A 295 ? 0.2496 0.2994 0.2369 0.0105 -0.0107 -0.0594 288 GLY A N 1910 C CA . GLY A 295 ? 0.2578 0.2979 0.2227 0.0164 0.0104 -0.0604 288 GLY A CA 1911 C C . GLY A 295 ? 0.2673 0.2937 0.2244 0.0136 0.0081 -0.0552 288 GLY A C 1912 O O . GLY A 295 ? 0.2413 0.2928 0.2139 0.0283 0.0069 -0.0721 288 GLY A O 1913 N N . LEU A 296 ? 0.2781 0.3123 0.2223 0.0040 0.0100 -0.0562 289 LEU A N 1914 C CA . LEU A 296 ? 0.3082 0.3192 0.2487 0.0070 0.0055 -0.0442 289 LEU A CA 1915 C C . LEU A 296 ? 0.3296 0.3363 0.2655 0.0140 0.0137 -0.0486 289 LEU A C 1916 O O . LEU A 296 ? 0.3354 0.3144 0.2736 0.0187 0.0056 -0.0430 289 LEU A O 1917 C CB A LEU A 296 ? 0.2998 0.3200 0.2414 -0.0008 0.0052 -0.0379 289 LEU A CB 1918 C CB B LEU A 296 ? 0.3050 0.3174 0.2462 0.0034 0.0102 -0.0552 289 LEU A CB 1919 C CG A LEU A 296 ? 0.3040 0.3250 0.2356 -0.0169 -0.0185 -0.0174 289 LEU A CG 1920 C CG B LEU A 296 ? 0.3128 0.3105 0.2441 -0.0068 0.0116 -0.0787 289 LEU A CG 1921 C CD1 A LEU A 296 ? 0.2413 0.3378 0.1881 -0.0135 -0.0070 -0.0204 289 LEU A CD1 1922 C CD1 B LEU A 296 ? 0.3142 0.2965 0.2228 -0.0342 0.0044 -0.1105 289 LEU A CD1 1923 C CD2 A LEU A 296 ? 0.2967 0.3453 0.2134 -0.0335 -0.0501 -0.0076 289 LEU A CD2 1924 C CD2 B LEU A 296 ? 0.3247 0.2844 0.2385 -0.0018 0.0100 -0.1135 289 LEU A CD2 1925 N N . PRO A 297 ? 0.3483 0.3452 0.2927 0.0221 0.0061 -0.0454 290 PRO A N 1926 C CA . PRO A 297 ? 0.3588 0.3597 0.2836 0.0205 0.0168 -0.0535 290 PRO A CA 1927 C C . PRO A 297 ? 0.3807 0.3754 0.2962 0.0163 0.0171 -0.0557 290 PRO A C 1928 O O . PRO A 297 ? 0.3833 0.3773 0.3028 0.0065 0.0137 -0.0612 290 PRO A O 1929 C CB . PRO A 297 ? 0.3663 0.3771 0.3110 0.0156 0.0182 -0.0381 290 PRO A CB 1930 C CG . PRO A 297 ? 0.3436 0.3569 0.3046 0.0354 0.0199 -0.0341 290 PRO A CG 1931 C CD . PRO A 297 ? 0.3637 0.3530 0.2914 0.0195 0.0168 -0.0443 290 PRO A CD 1932 N N A SER A 298 ? 0.3881 0.3693 0.2807 0.0169 0.0184 -0.0578 291 SER A N 1933 N N B SER A 298 ? 0.3859 0.3744 0.2818 0.0179 0.0175 -0.0598 291 SER A N 1934 C CA A SER A 298 ? 0.4056 0.3749 0.2822 0.0204 0.0235 -0.0612 291 SER A CA 1935 C CA B SER A 298 ? 0.3985 0.3822 0.2803 0.0232 0.0214 -0.0639 291 SER A CA 1936 C C A SER A 298 ? 0.3953 0.3795 0.2688 0.0203 0.0273 -0.0645 291 SER A C 1937 C C B SER A 298 ? 0.3926 0.3813 0.2705 0.0212 0.0248 -0.0652 291 SER A C 1938 O O A SER A 298 ? 0.3950 0.3855 0.2493 0.0235 0.0274 -0.0704 291 SER A O 1939 O O B SER A 298 ? 0.3913 0.3842 0.2618 0.0227 0.0214 -0.0686 291 SER A O 1940 C CB A SER A 298 ? 0.4101 0.3754 0.2873 0.0213 0.0242 -0.0569 291 SER A CB 1941 C CB B SER A 298 ? 0.4003 0.3833 0.2831 0.0232 0.0213 -0.0613 291 SER A CB 1942 O OG A SER A 298 ? 0.4471 0.3576 0.3165 0.0148 0.0380 -0.0321 291 SER A OG 1943 O OG B SER A 298 ? 0.4213 0.3981 0.2931 0.0409 0.0320 -0.0549 291 SER A OG 1944 N N . ILE A 299 ? 0.3871 0.3762 0.2597 0.0244 0.0325 -0.0635 292 ILE A N 1945 C CA . ILE A 299 ? 0.3900 0.3694 0.2618 0.0200 0.0259 -0.0639 292 ILE A CA 1946 C C . ILE A 299 ? 0.3785 0.3621 0.2662 0.0181 0.0240 -0.0734 292 ILE A C 1947 O O . ILE A 299 ? 0.3988 0.3603 0.2693 0.0180 0.0239 -0.0597 292 ILE A O 1948 C CB . ILE A 299 ? 0.3813 0.3760 0.2523 0.0314 0.0380 -0.0660 292 ILE A CB 1949 C CG1 . ILE A 299 ? 0.3499 0.3520 0.2578 0.0324 0.0147 -0.0572 292 ILE A CG1 1950 C CG2 . ILE A 299 ? 0.4071 0.3948 0.2198 0.0171 0.0316 -0.0666 292 ILE A CG2 1951 C CD1 . ILE A 299 ? 0.3302 0.3317 0.2809 0.0990 0.0246 -0.0418 292 ILE A CD1 1952 N N . PRO A 300 ? 0.3608 0.3586 0.2665 0.0281 0.0302 -0.0738 293 PRO A N 1953 C CA . PRO A 300 ? 0.3616 0.3558 0.2611 0.0225 0.0261 -0.0730 293 PRO A CA 1954 C C . PRO A 300 ? 0.3426 0.3437 0.2580 0.0237 0.0261 -0.0741 293 PRO A C 1955 O O . PRO A 300 ? 0.3312 0.3321 0.2684 0.0319 0.0212 -0.0645 293 PRO A O 1956 C CB . PRO A 300 ? 0.3684 0.3400 0.2438 0.0268 0.0202 -0.0827 293 PRO A CB 1957 C CG . PRO A 300 ? 0.3787 0.3699 0.2760 0.0270 0.0166 -0.0667 293 PRO A CG 1958 C CD . PRO A 300 ? 0.3805 0.3498 0.2534 0.0213 0.0108 -0.0845 293 PRO A CD 1959 N N . VAL A 301 ? 0.3176 0.3199 0.2431 0.0215 0.0374 -0.0705 294 VAL A N 1960 C CA . VAL A 301 ? 0.2871 0.3030 0.2462 0.0183 0.0383 -0.0738 294 VAL A CA 1961 C C . VAL A 301 ? 0.2959 0.3100 0.2589 0.0227 0.0407 -0.0820 294 VAL A C 1962 O O . VAL A 301 ? 0.2906 0.3207 0.2669 0.0248 0.0470 -0.0820 294 VAL A O 1963 C CB . VAL A 301 ? 0.2854 0.2954 0.2475 0.0209 0.0267 -0.0711 294 VAL A CB 1964 C CG1 . VAL A 301 ? 0.2213 0.2430 0.2434 -0.0042 0.0348 -0.0805 294 VAL A CG1 1965 C CG2 . VAL A 301 ? 0.2478 0.2814 0.2374 0.0173 0.0366 -0.0494 294 VAL A CG2 1966 N N . HIS A 302 ? 0.2862 0.3036 0.2644 0.0226 0.0432 -0.0873 295 HIS A N 1967 C CA . HIS A 302 ? 0.2947 0.3021 0.2665 0.0291 0.0422 -0.0882 295 HIS A CA 1968 C C . HIS A 302 ? 0.2924 0.3105 0.2680 0.0216 0.0480 -0.0814 295 HIS A C 1969 O O . HIS A 302 ? 0.2797 0.3457 0.2778 0.0347 0.0483 -0.0686 295 HIS A O 1970 C CB . HIS A 302 ? 0.3102 0.3029 0.2672 0.0289 0.0406 -0.0936 295 HIS A CB 1971 C CG . HIS A 302 ? 0.3054 0.2832 0.2695 0.0434 0.0330 -0.1102 295 HIS A CG 1972 N ND1 . HIS A 302 ? 0.2507 0.2678 0.2421 0.0573 0.0181 -0.1243 295 HIS A ND1 1973 C CD2 . HIS A 302 ? 0.3023 0.3043 0.2974 0.0557 0.0154 -0.1066 295 HIS A CD2 1974 C CE1 . HIS A 302 ? 0.2684 0.2713 0.3207 0.0509 0.0278 -0.1283 295 HIS A CE1 1975 N NE2 . HIS A 302 ? 0.2974 0.2784 0.3082 0.0580 0.0497 -0.1328 295 HIS A NE2 1976 N N . PRO A 303 ? 0.2896 0.2995 0.2604 0.0228 0.0518 -0.0834 296 PRO A N 1977 C CA . PRO A 303 ? 0.2738 0.2929 0.2642 0.0347 0.0590 -0.0811 296 PRO A CA 1978 C C . PRO A 303 ? 0.2913 0.3037 0.2802 0.0282 0.0613 -0.0860 296 PRO A C 1979 O O . PRO A 303 ? 0.2917 0.2963 0.2884 0.0260 0.0724 -0.0660 296 PRO A O 1980 C CB . PRO A 303 ? 0.2728 0.2913 0.2816 0.0279 0.0514 -0.0782 296 PRO A CB 1981 C CG . PRO A 303 ? 0.2600 0.2998 0.2525 0.0269 0.0588 -0.0743 296 PRO A CG 1982 C CD . PRO A 303 ? 0.2714 0.2919 0.2409 0.0238 0.0588 -0.0871 296 PRO A CD 1983 N N . ILE A 304 ? 0.2847 0.3044 0.2928 0.0383 0.0649 -0.0872 297 ILE A N 1984 C CA . ILE A 304 ? 0.2933 0.2994 0.2821 0.0442 0.0699 -0.0921 297 ILE A CA 1985 C C . ILE A 304 ? 0.2975 0.3048 0.2923 0.0433 0.0726 -0.0905 297 ILE A C 1986 O O . ILE A 304 ? 0.3142 0.3018 0.2806 0.0468 0.0771 -0.0868 297 ILE A O 1987 C CB . ILE A 304 ? 0.2731 0.2947 0.2632 0.0443 0.0761 -0.0808 297 ILE A CB 1988 C CG1 . ILE A 304 ? 0.2842 0.2974 0.2501 0.0569 0.0765 -0.0743 297 ILE A CG1 1989 C CG2 . ILE A 304 ? 0.3058 0.2761 0.2071 0.0346 0.0734 -0.0855 297 ILE A CG2 1990 C CD1 . ILE A 304 ? 0.3075 0.3068 0.2227 0.0932 0.1158 -0.0502 297 ILE A CD1 1991 N N . GLY A 305 ? 0.3058 0.3039 0.3123 0.0463 0.0720 -0.0912 298 GLY A N 1992 C CA . GLY A 305 ? 0.2826 0.3197 0.3375 0.0384 0.0801 -0.0888 298 GLY A CA 1993 C C . GLY A 305 ? 0.2996 0.3336 0.3655 0.0473 0.0770 -0.0918 298 GLY A C 1994 O O . GLY A 305 ? 0.2938 0.3276 0.3493 0.0500 0.0710 -0.0968 298 GLY A O 1995 N N . TYR A 306 ? 0.2778 0.3208 0.3815 0.0428 0.0754 -0.0908 299 TYR A N 1996 C CA . TYR A 306 ? 0.2813 0.3149 0.3878 0.0435 0.0808 -0.0979 299 TYR A CA 1997 C C . TYR A 306 ? 0.2889 0.3200 0.3844 0.0432 0.0817 -0.1070 299 TYR A C 1998 O O . TYR A 306 ? 0.2892 0.3109 0.3988 0.0474 0.0890 -0.1086 299 TYR A O 1999 C CB . TYR A 306 ? 0.2753 0.3060 0.3823 0.0312 0.0785 -0.0976 299 TYR A CB 2000 C CG . TYR A 306 ? 0.2674 0.2999 0.3836 0.0130 0.0777 -0.0987 299 TYR A CG 2001 C CD1 . TYR A 306 ? 0.2724 0.3128 0.3969 -0.0137 0.0693 -0.0668 299 TYR A CD1 2002 C CD2 . TYR A 306 ? 0.2773 0.3059 0.3866 0.0005 0.0793 -0.0773 299 TYR A CD2 2003 C CE1 . TYR A 306 ? 0.2430 0.3160 0.3876 0.0093 0.0377 -0.1134 299 TYR A CE1 2004 C CE2 . TYR A 306 ? 0.2596 0.3298 0.3933 0.0140 0.0577 -0.0979 299 TYR A CE2 2005 C CZ . TYR A 306 ? 0.2385 0.3344 0.3892 0.0146 0.0556 -0.0930 299 TYR A CZ 2006 O OH . TYR A 306 ? 0.1554 0.2902 0.3685 0.0550 0.0682 -0.1248 299 TYR A OH 2007 N N . TYR A 307 ? 0.2911 0.3151 0.3927 0.0545 0.0816 -0.1086 300 TYR A N 2008 C CA . TYR A 307 ? 0.3017 0.3331 0.3927 0.0634 0.0915 -0.1069 300 TYR A CA 2009 C C . TYR A 307 ? 0.3166 0.3336 0.3883 0.0655 0.0960 -0.1084 300 TYR A C 2010 O O . TYR A 307 ? 0.3168 0.3407 0.3899 0.0758 0.0922 -0.1018 300 TYR A O 2011 C CB . TYR A 307 ? 0.2947 0.3277 0.4025 0.0593 0.0903 -0.1066 300 TYR A CB 2012 C CG . TYR A 307 ? 0.3283 0.3676 0.4550 0.0706 0.0867 -0.0858 300 TYR A CG 2013 C CD1 . TYR A 307 ? 0.3367 0.4081 0.4497 0.0651 0.0896 -0.0765 300 TYR A CD1 2014 C CD2 . TYR A 307 ? 0.3445 0.4116 0.4738 0.0567 0.0931 -0.0889 300 TYR A CD2 2015 C CE1 . TYR A 307 ? 0.3032 0.4102 0.4670 0.0956 0.0914 -0.0912 300 TYR A CE1 2016 C CE2 . TYR A 307 ? 0.3585 0.4051 0.4583 0.0825 0.1043 -0.0833 300 TYR A CE2 2017 C CZ . TYR A 307 ? 0.3432 0.4285 0.4704 0.1075 0.0929 -0.0883 300 TYR A CZ 2018 O OH . TYR A 307 ? 0.3754 0.4492 0.4500 0.1325 0.1329 -0.0688 300 TYR A OH 2019 N N . ASP A 308 ? 0.3200 0.3329 0.3832 0.0734 0.0978 -0.1106 301 ASP A N 2020 C CA . ASP A 308 ? 0.3358 0.3525 0.3814 0.0639 0.0981 -0.1185 301 ASP A CA 2021 C C . ASP A 308 ? 0.3363 0.3628 0.3879 0.0678 0.0995 -0.1180 301 ASP A C 2022 O O . ASP A 308 ? 0.3286 0.3696 0.3814 0.0695 0.0951 -0.1133 301 ASP A O 2023 C CB . ASP A 308 ? 0.3418 0.3575 0.3771 0.0604 0.0938 -0.1165 301 ASP A CB 2024 C CG . ASP A 308 ? 0.3838 0.3548 0.3745 0.0683 0.0851 -0.1222 301 ASP A CG 2025 O OD1 . ASP A 308 ? 0.3993 0.3393 0.3761 0.0857 0.0708 -0.1449 301 ASP A OD1 2026 O OD2 . ASP A 308 ? 0.4316 0.3788 0.3543 0.0632 0.0791 -0.1416 301 ASP A OD2 2027 N N . ALA A 309 ? 0.3483 0.3614 0.3984 0.0555 0.0867 -0.1219 302 ALA A N 2028 C CA . ALA A 309 ? 0.3596 0.3692 0.4066 0.0559 0.0979 -0.1224 302 ALA A CA 2029 C C . ALA A 309 ? 0.3920 0.3793 0.4058 0.0528 0.1031 -0.1251 302 ALA A C 2030 O O . ALA A 309 ? 0.4049 0.3689 0.4123 0.0472 0.0863 -0.1143 302 ALA A O 2031 C CB . ALA A 309 ? 0.3517 0.3592 0.3883 0.0547 0.1097 -0.1294 302 ALA A CB 2032 N N . GLN A 310 ? 0.3852 0.3963 0.4167 0.0637 0.1098 -0.1223 303 GLN A N 2033 C CA . GLN A 310 ? 0.4074 0.4236 0.4323 0.0645 0.1237 -0.1223 303 GLN A CA 2034 C C . GLN A 310 ? 0.4047 0.4265 0.4283 0.0706 0.1223 -0.1155 303 GLN A C 2035 O O . GLN A 310 ? 0.3935 0.4332 0.4151 0.0759 0.1273 -0.1155 303 GLN A O 2036 C CB . GLN A 310 ? 0.3964 0.4284 0.4317 0.0672 0.1225 -0.1284 303 GLN A CB 2037 C CG . GLN A 310 ? 0.4301 0.5143 0.5003 0.0690 0.1505 -0.1190 303 GLN A CG 2038 C CD . GLN A 310 ? 0.4661 0.6333 0.5802 0.0644 0.1441 -0.1316 303 GLN A CD 2039 O OE1 . GLN A 310 ? 0.5253 0.7104 0.6537 0.0562 0.1535 -0.1411 303 GLN A OE1 2040 N NE2 . GLN A 310 ? 0.4649 0.6299 0.5789 0.0743 0.1735 -0.1297 303 GLN A NE2 2041 N N . LYS A 311 ? 0.4137 0.4250 0.4296 0.0689 0.1214 -0.1162 304 LYS A N 2042 C CA . LYS A 311 ? 0.4168 0.4241 0.4199 0.0730 0.1352 -0.1196 304 LYS A CA 2043 C C . LYS A 311 ? 0.4169 0.4348 0.4173 0.0645 0.1365 -0.1145 304 LYS A C 2044 O O . LYS A 311 ? 0.4205 0.4461 0.4247 0.0690 0.1391 -0.1040 304 LYS A O 2045 C CB . LYS A 311 ? 0.4134 0.4182 0.4185 0.0733 0.1369 -0.1235 304 LYS A CB 2046 C CG . LYS A 311 ? 0.4136 0.3928 0.4117 0.0852 0.1415 -0.1329 304 LYS A CG 2047 C CD . LYS A 311 ? 0.4241 0.3956 0.3974 0.0812 0.1630 -0.1453 304 LYS A CD 2048 C CE . LYS A 311 ? 0.4124 0.3843 0.4234 0.0844 0.1523 -0.1458 304 LYS A CE 2049 N NZ . LYS A 311 ? 0.4173 0.3907 0.3974 0.0907 0.1576 -0.1507 304 LYS A NZ 2050 N N . LEU A 312 ? 0.4119 0.4192 0.4077 0.0645 0.1384 -0.1139 305 LEU A N 2051 C CA . LEU A 312 ? 0.4183 0.4435 0.4068 0.0563 0.1402 -0.1062 305 LEU A CA 2052 C C . LEU A 312 ? 0.4258 0.4496 0.4126 0.0563 0.1479 -0.0986 305 LEU A C 2053 O O . LEU A 312 ? 0.4373 0.4658 0.4223 0.0482 0.1396 -0.0897 305 LEU A O 2054 C CB . LEU A 312 ? 0.3960 0.4320 0.3981 0.0614 0.1347 -0.1070 305 LEU A CB 2055 C CG . LEU A 312 ? 0.4006 0.4297 0.3674 0.0602 0.1244 -0.1127 305 LEU A CG 2056 C CD1 . LEU A 312 ? 0.3837 0.4240 0.3496 0.0464 0.1281 -0.0988 305 LEU A CD1 2057 C CD2 . LEU A 312 ? 0.3578 0.4056 0.3572 0.0792 0.1220 -0.1490 305 LEU A CD2 2058 N N . LEU A 313 ? 0.4189 0.4445 0.4068 0.0578 0.1560 -0.1004 306 LEU A N 2059 C CA . LEU A 313 ? 0.4199 0.4424 0.4136 0.0640 0.1660 -0.1022 306 LEU A CA 2060 C C . LEU A 313 ? 0.4381 0.4574 0.4264 0.0705 0.1718 -0.1032 306 LEU A C 2061 O O . LEU A 313 ? 0.4316 0.4516 0.4266 0.0855 0.1773 -0.1038 306 LEU A O 2062 C CB . LEU A 313 ? 0.4087 0.4232 0.4052 0.0555 0.1666 -0.1050 306 LEU A CB 2063 C CG . LEU A 313 ? 0.3776 0.4067 0.4067 0.0570 0.1595 -0.0995 306 LEU A CG 2064 C CD1 . LEU A 313 ? 0.3644 0.4107 0.3891 0.0601 0.1426 -0.1139 306 LEU A CD1 2065 C CD2 . LEU A 313 ? 0.2755 0.3722 0.4170 0.0669 0.1618 -0.1245 306 LEU A CD2 2066 N N . GLU A 314 ? 0.4645 0.4670 0.4375 0.0729 0.1783 -0.1069 307 GLU A N 2067 C CA . GLU A 314 ? 0.4875 0.4802 0.4691 0.0810 0.1798 -0.1106 307 GLU A CA 2068 C C . GLU A 314 ? 0.5041 0.4870 0.4670 0.0796 0.1878 -0.1088 307 GLU A C 2069 O O . GLU A 314 ? 0.5082 0.4831 0.4782 0.0853 0.1841 -0.1114 307 GLU A O 2070 C CB . GLU A 314 ? 0.4926 0.4772 0.4677 0.0826 0.1752 -0.1076 307 GLU A CB 2071 C CG . GLU A 314 ? 0.4952 0.4713 0.5253 0.0815 0.1605 -0.0932 307 GLU A CG 2072 C CD . GLU A 314 ? 0.5321 0.4888 0.5743 0.0948 0.1458 -0.0823 307 GLU A CD 2073 O OE1 . GLU A 314 ? 0.5551 0.4737 0.5967 0.0853 0.1335 -0.0508 307 GLU A OE1 2074 O OE2 . GLU A 314 ? 0.5580 0.4605 0.5820 0.1199 0.1585 -0.0902 307 GLU A OE2 2075 N N . LYS A 315 ? 0.5142 0.4997 0.4693 0.0791 0.1931 -0.1082 308 LYS A N 2076 C CA . LYS A 315 ? 0.5405 0.5204 0.4780 0.0732 0.1911 -0.1094 308 LYS A CA 2077 C C . LYS A 315 ? 0.5383 0.5339 0.4740 0.0681 0.1962 -0.1036 308 LYS A C 2078 O O . LYS A 315 ? 0.5401 0.5371 0.4663 0.0662 0.1977 -0.1033 308 LYS A O 2079 C CB . LYS A 315 ? 0.5444 0.5237 0.4841 0.0738 0.1890 -0.1108 308 LYS A CB 2080 C CG . LYS A 315 ? 0.5783 0.5239 0.5053 0.0779 0.1752 -0.1159 308 LYS A CG 2081 C CD . LYS A 315 ? 0.6270 0.4914 0.4969 0.0738 0.1539 -0.1253 308 LYS A CD 2082 C CE . LYS A 315 ? 0.6049 0.5080 0.4841 0.0960 0.1709 -0.1333 308 LYS A CE 2083 N NZ . LYS A 315 ? 0.6372 0.4595 0.4584 0.0951 0.1747 -0.1368 308 LYS A NZ 2084 N N . MET A 316 ? 0.5260 0.5331 0.4604 0.0699 0.2144 -0.1001 309 MET A N 2085 C CA . MET A 316 ? 0.5329 0.5460 0.4596 0.0653 0.2122 -0.0929 309 MET A CA 2086 C C . MET A 316 ? 0.5473 0.5514 0.4555 0.0688 0.2231 -0.0913 309 MET A C 2087 O O . MET A 316 ? 0.5431 0.5495 0.4494 0.0721 0.2256 -0.0931 309 MET A O 2088 C CB . MET A 316 ? 0.5264 0.5397 0.4485 0.0654 0.2112 -0.0893 309 MET A CB 2089 C CG A MET A 316 ? 0.5142 0.5278 0.4375 0.0577 0.1885 -0.0833 309 MET A CG 2090 C CG B MET A 316 ? 0.5185 0.5472 0.4680 0.0559 0.1980 -0.0860 309 MET A CG 2091 S SD A MET A 316 ? 0.4969 0.4801 0.3623 0.0283 0.1484 -0.0720 309 MET A SD 2092 S SD B MET A 316 ? 0.5123 0.5476 0.4679 0.0200 0.1641 -0.0834 309 MET A SD 2093 C CE A MET A 316 ? 0.5014 0.4968 0.3912 0.0275 0.1415 -0.0668 309 MET A CE 2094 C CE B MET A 316 ? 0.5153 0.5568 0.4630 0.0141 0.1651 -0.0795 309 MET A CE 2095 N N . GLY A 317 ? 0.5592 0.5586 0.4576 0.0702 0.2288 -0.0862 310 GLY A N 2096 C CA . GLY A 317 ? 0.5616 0.5714 0.4616 0.0689 0.2480 -0.0764 310 GLY A CA 2097 C C . GLY A 317 ? 0.5788 0.5872 0.4727 0.0643 0.2537 -0.0689 310 GLY A C 2098 O O . GLY A 317 ? 0.5810 0.5789 0.4610 0.0663 0.2664 -0.0669 310 GLY A O 2099 N N . GLY A 318 ? 0.5838 0.5974 0.4732 0.0667 0.2624 -0.0659 311 GLY A N 2100 C CA . GLY A 318 ? 0.5922 0.6048 0.4943 0.0617 0.2673 -0.0541 311 GLY A CA 2101 C C . GLY A 318 ? 0.5959 0.6121 0.5082 0.0624 0.2646 -0.0493 311 GLY A C 2102 O O . GLY A 318 ? 0.5878 0.6062 0.5002 0.0707 0.2762 -0.0526 311 GLY A O 2103 N N . SER A 319 ? 0.5958 0.6136 0.5180 0.0651 0.2678 -0.0479 312 SER A N 2104 C CA . SER A 319 ? 0.5989 0.6164 0.5469 0.0621 0.2602 -0.0456 312 SER A CA 2105 C C . SER A 319 ? 0.5851 0.6120 0.5527 0.0556 0.2577 -0.0499 312 SER A C 2106 O O . SER A 319 ? 0.5949 0.6062 0.5423 0.0566 0.2590 -0.0592 312 SER A O 2107 C CB . SER A 319 ? 0.6100 0.6249 0.5522 0.0674 0.2596 -0.0428 312 SER A CB 2108 O OG . SER A 319 ? 0.6352 0.6400 0.5864 0.0765 0.2504 -0.0310 312 SER A OG 2109 N N . ALA A 320 ? 0.5683 0.6031 0.5615 0.0461 0.2544 -0.0457 313 ALA A N 2110 C CA . ALA A 320 ? 0.5422 0.5970 0.5785 0.0394 0.2471 -0.0442 313 ALA A CA 2111 C C . ALA A 320 ? 0.5237 0.5859 0.5841 0.0323 0.2401 -0.0404 313 ALA A C 2112 O O . ALA A 320 ? 0.5154 0.5829 0.5939 0.0330 0.2386 -0.0426 313 ALA A O 2113 C CB . ALA A 320 ? 0.5332 0.5938 0.5658 0.0372 0.2583 -0.0404 313 ALA A CB 2114 N N . PRO A 321 ? 0.5081 0.5730 0.5904 0.0271 0.2311 -0.0358 314 PRO A N 2115 C CA . PRO A 321 ? 0.4997 0.5589 0.5907 0.0237 0.2298 -0.0348 314 PRO A CA 2116 C C . PRO A 321 ? 0.4883 0.5577 0.5936 0.0210 0.2297 -0.0286 314 PRO A C 2117 O O . PRO A 321 ? 0.4803 0.5359 0.5894 0.0109 0.2360 -0.0227 314 PRO A O 2118 C CB . PRO A 321 ? 0.4917 0.5520 0.5803 0.0224 0.2313 -0.0346 314 PRO A CB 2119 C CG . PRO A 321 ? 0.5145 0.5611 0.5849 0.0200 0.2323 -0.0256 314 PRO A CG 2120 C CD . PRO A 321 ? 0.5237 0.5697 0.5932 0.0252 0.2234 -0.0372 314 PRO A CD 2121 N N . PRO A 322 ? 0.4858 0.5529 0.5985 0.0186 0.2258 -0.0260 315 PRO A N 2122 C CA . PRO A 322 ? 0.4825 0.5581 0.6058 0.0143 0.2228 -0.0221 315 PRO A CA 2123 C C . PRO A 322 ? 0.4776 0.5636 0.6203 0.0093 0.2173 -0.0221 315 PRO A C 2124 O O . PRO A 322 ? 0.4679 0.5584 0.6174 0.0074 0.2247 -0.0209 315 PRO A O 2125 C CB . PRO A 322 ? 0.4631 0.5465 0.5976 0.0174 0.2281 -0.0228 315 PRO A CB 2126 C CG . PRO A 322 ? 0.4699 0.5460 0.5985 0.0277 0.2278 -0.0187 315 PRO A CG 2127 C CD . PRO A 322 ? 0.4785 0.5535 0.5884 0.0214 0.2281 -0.0252 315 PRO A CD 2128 N N . ASP A 323 ? 0.4798 0.5642 0.6356 0.0043 0.2063 -0.0191 316 ASP A N 2129 C CA . ASP A 323 ? 0.4809 0.5714 0.6572 0.0053 0.1967 -0.0224 316 ASP A CA 2130 C C . ASP A 323 ? 0.4748 0.5649 0.6601 0.0034 0.1872 -0.0240 316 ASP A C 2131 O O . ASP A 323 ? 0.4882 0.5616 0.6589 -0.0009 0.1899 -0.0203 316 ASP A O 2132 C CB . ASP A 323 ? 0.4856 0.5718 0.6622 0.0049 0.1961 -0.0219 316 ASP A CB 2133 C CG . ASP A 323 ? 0.4865 0.5780 0.6835 0.0054 0.1918 -0.0202 316 ASP A CG 2134 O OD1 . ASP A 323 ? 0.5095 0.5974 0.6722 0.0056 0.1769 -0.0102 316 ASP A OD1 2135 O OD2 . ASP A 323 ? 0.4652 0.5868 0.7221 -0.0022 0.1858 -0.0197 316 ASP A OD2 2136 N N . SER A 324 ? 0.4653 0.5596 0.6607 0.0025 0.1762 -0.0258 317 SER A N 2137 C CA . SER A 324 ? 0.4545 0.5577 0.6537 -0.0028 0.1642 -0.0315 317 SER A CA 2138 C C . SER A 324 ? 0.4364 0.5419 0.6409 0.0016 0.1615 -0.0357 317 SER A C 2139 O O . SER A 324 ? 0.4429 0.5496 0.6416 -0.0054 0.1604 -0.0302 317 SER A O 2140 C CB . SER A 324 ? 0.4553 0.5588 0.6593 0.0015 0.1573 -0.0326 317 SER A CB 2141 O OG . SER A 324 ? 0.4704 0.5662 0.6676 -0.0236 0.1284 -0.0344 317 SER A OG 2142 N N . SER A 325 ? 0.4175 0.5150 0.6133 -0.0029 0.1586 -0.0411 318 SER A N 2143 C CA . SER A 325 ? 0.4019 0.4934 0.5862 0.0017 0.1558 -0.0493 318 SER A CA 2144 C C . SER A 325 ? 0.3904 0.4863 0.5657 0.0042 0.1610 -0.0503 318 SER A C 2145 O O . SER A 325 ? 0.3996 0.4825 0.5519 -0.0122 0.1569 -0.0520 318 SER A O 2146 C CB . SER A 325 ? 0.3995 0.4981 0.5953 0.0017 0.1525 -0.0457 318 SER A CB 2147 O OG . SER A 325 ? 0.4216 0.4769 0.5861 0.0087 0.1488 -0.0515 318 SER A OG 2148 N N . TRP A 326 ? 0.3736 0.4649 0.5428 0.0078 0.1621 -0.0462 319 TRP A N 2149 C CA . TRP A 326 ? 0.3548 0.4519 0.5230 0.0210 0.1677 -0.0482 319 TRP A CA 2150 C C . TRP A 326 ? 0.3562 0.4546 0.5262 0.0255 0.1666 -0.0572 319 TRP A C 2151 O O . TRP A 326 ? 0.3488 0.4374 0.5153 0.0347 0.1699 -0.0636 319 TRP A O 2152 C CB . TRP A 326 ? 0.3424 0.4500 0.5184 0.0130 0.1755 -0.0412 319 TRP A CB 2153 C CG . TRP A 326 ? 0.3513 0.4335 0.4793 0.0186 0.1745 -0.0368 319 TRP A CG 2154 C CD1 . TRP A 326 ? 0.3531 0.4145 0.4659 0.0115 0.1780 -0.0353 319 TRP A CD1 2155 C CD2 . TRP A 326 ? 0.3422 0.4315 0.4480 0.0169 0.1911 -0.0377 319 TRP A CD2 2156 N NE1 . TRP A 326 ? 0.3826 0.4092 0.4740 0.0154 0.1514 -0.0552 319 TRP A NE1 2157 C CE2 . TRP A 326 ? 0.3858 0.4204 0.4641 0.0213 0.1447 -0.0265 319 TRP A CE2 2158 C CE3 . TRP A 326 ? 0.3068 0.4312 0.4109 0.0194 0.2070 -0.0223 319 TRP A CE3 2159 C CZ2 . TRP A 326 ? 0.3408 0.4164 0.4296 0.0203 0.1710 -0.0236 319 TRP A CZ2 2160 C CZ3 . TRP A 326 ? 0.3340 0.4190 0.4047 0.0061 0.1794 0.0111 319 TRP A CZ3 2161 C CH2 . TRP A 326 ? 0.3639 0.3978 0.4040 0.0212 0.1555 0.0031 319 TRP A CH2 2162 N N A ARG A 327 ? 0.3515 0.4542 0.5269 0.0306 0.1674 -0.0613 320 ARG A N 2163 N N B ARG A 327 ? 0.3494 0.4526 0.5247 0.0315 0.1680 -0.0618 320 ARG A N 2164 C CA A ARG A 327 ? 0.3559 0.4594 0.5427 0.0274 0.1618 -0.0600 320 ARG A CA 2165 C CA B ARG A 327 ? 0.3508 0.4565 0.5391 0.0294 0.1628 -0.0608 320 ARG A CA 2166 C C A ARG A 327 ? 0.3546 0.4541 0.5395 0.0277 0.1579 -0.0648 320 ARG A C 2167 C C B ARG A 327 ? 0.3511 0.4530 0.5376 0.0291 0.1585 -0.0649 320 ARG A C 2168 O O A ARG A 327 ? 0.3600 0.4439 0.5453 0.0189 0.1479 -0.0670 320 ARG A O 2169 O O B ARG A 327 ? 0.3549 0.4445 0.5446 0.0204 0.1481 -0.0662 320 ARG A O 2170 C CB A ARG A 327 ? 0.3469 0.4611 0.5462 0.0278 0.1670 -0.0609 320 ARG A CB 2171 C CB B ARG A 327 ? 0.3417 0.4562 0.5382 0.0307 0.1682 -0.0629 320 ARG A CB 2172 C CG A ARG A 327 ? 0.3649 0.4962 0.5670 0.0237 0.1694 -0.0593 320 ARG A CG 2173 C CG B ARG A 327 ? 0.3478 0.4749 0.5548 0.0327 0.1732 -0.0625 320 ARG A CG 2174 C CD A ARG A 327 ? 0.3807 0.5705 0.6207 0.0199 0.2099 -0.0658 320 ARG A CD 2175 C CD B ARG A 327 ? 0.3716 0.5162 0.5887 0.0322 0.1995 -0.0586 320 ARG A CD 2176 N NE A ARG A 327 ? 0.4195 0.6413 0.6495 0.0189 0.2088 -0.0615 320 ARG A NE 2177 N NE B ARG A 327 ? 0.3774 0.5479 0.6403 0.0273 0.1909 -0.0476 320 ARG A NE 2178 C CZ A ARG A 327 ? 0.4439 0.6717 0.6696 0.0191 0.2325 -0.0521 320 ARG A CZ 2179 C CZ B ARG A 327 ? 0.4203 0.5477 0.6690 0.0218 0.1733 -0.0508 320 ARG A CZ 2180 N NH1 A ARG A 327 ? 0.4356 0.6714 0.6749 0.0157 0.2467 -0.0559 320 ARG A NH1 2181 N NH1 B ARG A 327 ? 0.4153 0.5476 0.6857 0.0291 0.1676 -0.0444 320 ARG A NH1 2182 N NH2 A ARG A 327 ? 0.4392 0.6932 0.6713 0.0490 0.2493 -0.0651 320 ARG A NH2 2183 N NH2 B ARG A 327 ? 0.3945 0.5502 0.6651 0.0309 0.1716 -0.0541 320 ARG A NH2 2184 N N . GLY A 328 ? 0.3436 0.4557 0.5440 0.0269 0.1516 -0.0661 321 GLY A N 2185 C CA . GLY A 328 ? 0.3367 0.4479 0.5339 0.0316 0.1547 -0.0712 321 GLY A CA 2186 C C . GLY A 328 ? 0.3488 0.4512 0.5409 0.0327 0.1412 -0.0719 321 GLY A C 2187 O O . GLY A 328 ? 0.3197 0.4362 0.5196 0.0395 0.1469 -0.0743 321 GLY A O 2188 N N . SER A 329 ? 0.3618 0.4556 0.5441 0.0320 0.1378 -0.0712 322 SER A N 2189 C CA . SER A 329 ? 0.3745 0.4685 0.5457 0.0378 0.1403 -0.0822 322 SER A CA 2190 C C . SER A 329 ? 0.3653 0.4648 0.5317 0.0434 0.1495 -0.0834 322 SER A C 2191 O O . SER A 329 ? 0.3551 0.4665 0.5280 0.0504 0.1386 -0.0833 322 SER A O 2192 C CB . SER A 329 ? 0.3840 0.4680 0.5450 0.0380 0.1298 -0.0839 322 SER A CB 2193 O OG . SER A 329 ? 0.4453 0.5537 0.5647 0.0375 0.1288 -0.0830 322 SER A OG 2194 N N . LEU A 330 ? 0.3567 0.4650 0.5236 0.0448 0.1593 -0.0852 323 LEU A N 2195 C CA . LEU A 330 ? 0.3654 0.4689 0.5349 0.0420 0.1650 -0.0851 323 LEU A CA 2196 C C . LEU A 330 ? 0.3797 0.4826 0.5490 0.0509 0.1665 -0.0911 323 LEU A C 2197 O O . LEU A 330 ? 0.3793 0.4881 0.5551 0.0391 0.1617 -0.0853 323 LEU A O 2198 C CB . LEU A 330 ? 0.3453 0.4571 0.5158 0.0489 0.1723 -0.0881 323 LEU A CB 2199 C CG . LEU A 330 ? 0.3098 0.4199 0.5019 0.0352 0.1644 -0.0779 323 LEU A CG 2200 C CD1 . LEU A 330 ? 0.2948 0.4045 0.4503 0.0488 0.1981 -0.0909 323 LEU A CD1 2201 C CD2 . LEU A 330 ? 0.2630 0.3846 0.4554 0.0297 0.1474 -0.0952 323 LEU A CD2 2202 N N . LYS A 331 ? 0.4012 0.4879 0.5630 0.0579 0.1726 -0.0941 324 LYS A N 2203 C CA . LYS A 331 ? 0.4203 0.5061 0.5686 0.0592 0.1819 -0.0962 324 LYS A CA 2204 C C . LYS A 331 ? 0.4326 0.5087 0.5652 0.0568 0.1880 -0.0983 324 LYS A C 2205 O O . LYS A 331 ? 0.4577 0.5048 0.5642 0.0514 0.1790 -0.1098 324 LYS A O 2206 C CB . LYS A 331 ? 0.4203 0.4993 0.5721 0.0653 0.1828 -0.1002 324 LYS A CB 2207 C CG . LYS A 331 ? 0.4174 0.5109 0.5849 0.0709 0.1790 -0.0941 324 LYS A CG 2208 C CD . LYS A 331 ? 0.3926 0.5092 0.5998 0.0732 0.1821 -0.0920 324 LYS A CD 2209 C CE . LYS A 331 ? 0.3865 0.5061 0.6065 0.0762 0.1816 -0.0965 324 LYS A CE 2210 N NZ . LYS A 331 ? 0.3895 0.4976 0.6088 0.0711 0.1758 -0.0902 324 LYS A NZ 2211 N N . VAL A 332 ? 0.4239 0.5080 0.5590 0.0599 0.2005 -0.0952 325 VAL A N 2212 C CA . VAL A 332 ? 0.4309 0.5157 0.5537 0.0530 0.2038 -0.0901 325 VAL A CA 2213 C C . VAL A 332 ? 0.4340 0.5209 0.5548 0.0520 0.2103 -0.0836 325 VAL A C 2214 O O . VAL A 332 ? 0.4190 0.5133 0.5474 0.0427 0.2159 -0.0771 325 VAL A O 2215 C CB . VAL A 332 ? 0.4218 0.5054 0.5537 0.0606 0.2040 -0.0945 325 VAL A CB 2216 C CG1 . VAL A 332 ? 0.4281 0.5261 0.5605 0.0411 0.1918 -0.0857 325 VAL A CG1 2217 C CG2 . VAL A 332 ? 0.4128 0.5211 0.5059 0.0506 0.2153 -0.0962 325 VAL A CG2 2218 N N . PRO A 333 ? 0.4510 0.5275 0.5548 0.0509 0.2118 -0.0816 326 PRO A N 2219 C CA . PRO A 333 ? 0.4583 0.5305 0.5527 0.0504 0.2095 -0.0813 326 PRO A CA 2220 C C . PRO A 333 ? 0.4553 0.5192 0.5403 0.0481 0.2066 -0.0815 326 PRO A C 2221 O O . PRO A 333 ? 0.4509 0.5243 0.5489 0.0359 0.2044 -0.0759 326 PRO A O 2222 C CB . PRO A 333 ? 0.4697 0.5342 0.5639 0.0475 0.2060 -0.0788 326 PRO A CB 2223 C CG . PRO A 333 ? 0.4831 0.5503 0.5793 0.0387 0.1925 -0.0736 326 PRO A CG 2224 C CD . PRO A 333 ? 0.4609 0.5388 0.5669 0.0411 0.2025 -0.0751 326 PRO A CD 2225 N N . TYR A 334 ? 0.4322 0.5061 0.5127 0.0517 0.2114 -0.0807 327 TYR A N 2226 C CA . TYR A 334 ? 0.4318 0.5042 0.4999 0.0438 0.2025 -0.0700 327 TYR A CA 2227 C C . TYR A 334 ? 0.4298 0.5072 0.4927 0.0414 0.2079 -0.0686 327 TYR A C 2228 O O . TYR A 334 ? 0.4251 0.5054 0.4836 0.0296 0.2108 -0.0562 327 TYR A O 2229 C CB . TYR A 334 ? 0.4203 0.4992 0.4987 0.0430 0.2017 -0.0704 327 TYR A CB 2230 C CG . TYR A 334 ? 0.4160 0.4802 0.4972 0.0361 0.1751 -0.0764 327 TYR A CG 2231 C CD1 . TYR A 334 ? 0.4039 0.4609 0.4645 0.0271 0.1601 -0.0838 327 TYR A CD1 2232 C CD2 . TYR A 334 ? 0.4172 0.4516 0.4619 0.0218 0.1450 -0.0903 327 TYR A CD2 2233 C CE1 . TYR A 334 ? 0.3768 0.4511 0.4675 0.0269 0.1421 -0.0810 327 TYR A CE1 2234 C CE2 . TYR A 334 ? 0.3927 0.4551 0.4715 0.0101 0.1304 -0.0749 327 TYR A CE2 2235 C CZ . TYR A 334 ? 0.3754 0.4419 0.4588 0.0307 0.1357 -0.0745 327 TYR A CZ 2236 O OH . TYR A 334 ? 0.3014 0.4006 0.4880 0.0143 0.1352 -0.0553 327 TYR A OH 2237 N N . ASN A 335 ? 0.4288 0.5061 0.4674 0.0407 0.2146 -0.0664 328 ASN A N 2238 C CA . ASN A 335 ? 0.4496 0.5038 0.4636 0.0485 0.2080 -0.0696 328 ASN A CA 2239 C C . ASN A 335 ? 0.4579 0.4990 0.4546 0.0567 0.2047 -0.0688 328 ASN A C 2240 O O . ASN A 335 ? 0.4684 0.4771 0.4567 0.0707 0.1948 -0.0685 328 ASN A O 2241 C CB . ASN A 335 ? 0.4399 0.5092 0.4536 0.0443 0.2149 -0.0740 328 ASN A CB 2242 C CG . ASN A 335 ? 0.4484 0.5194 0.4574 0.0388 0.2062 -0.0642 328 ASN A CG 2243 O OD1 . ASN A 335 ? 0.4304 0.5433 0.4655 0.0039 0.2181 -0.0252 328 ASN A OD1 2244 N ND2 . ASN A 335 ? 0.3825 0.5054 0.4155 0.0556 0.2506 -0.0547 328 ASN A ND2 2245 N N . VAL A 336 ? 0.4845 0.5040 0.4555 0.0548 0.1973 -0.0613 329 VAL A N 2246 C CA . VAL A 336 ? 0.5057 0.5055 0.4488 0.0604 0.1979 -0.0641 329 VAL A CA 2247 C C . VAL A 336 ? 0.5237 0.5188 0.4395 0.0606 0.2015 -0.0579 329 VAL A C 2248 O O . VAL A 336 ? 0.5297 0.5104 0.4138 0.0608 0.2044 -0.0556 329 VAL A O 2249 C CB . VAL A 336 ? 0.5040 0.5041 0.4623 0.0630 0.1897 -0.0668 329 VAL A CB 2250 C CG1 . VAL A 336 ? 0.5140 0.5058 0.4909 0.0552 0.1858 -0.0423 329 VAL A CG1 2251 C CG2 . VAL A 336 ? 0.5159 0.4781 0.4807 0.0495 0.1735 -0.0641 329 VAL A CG2 2252 N N . GLY A 337 ? 0.5570 0.5349 0.4356 0.0663 0.1978 -0.0637 330 GLY A N 2253 C CA . GLY A 337 ? 0.5788 0.5602 0.4400 0.0620 0.2006 -0.0639 330 GLY A CA 2254 C C . GLY A 337 ? 0.6003 0.5774 0.4517 0.0625 0.1951 -0.0610 330 GLY A C 2255 O O . GLY A 337 ? 0.5991 0.5666 0.4587 0.0615 0.1968 -0.0565 330 GLY A O 2256 N N . PRO A 338 ? 0.6113 0.5966 0.4568 0.0607 0.1917 -0.0587 331 PRO A N 2257 C CA . PRO A 338 ? 0.6166 0.6051 0.4586 0.0604 0.1966 -0.0599 331 PRO A CA 2258 C C . PRO A 338 ? 0.6172 0.6090 0.4522 0.0640 0.1966 -0.0683 331 PRO A C 2259 O O . PRO A 338 ? 0.6075 0.5955 0.4409 0.0668 0.2009 -0.0687 331 PRO A O 2260 C CB . PRO A 338 ? 0.6177 0.6146 0.4567 0.0547 0.1956 -0.0535 331 PRO A CB 2261 C CG . PRO A 338 ? 0.6384 0.6163 0.4831 0.0541 0.1733 -0.0493 331 PRO A CG 2262 C CD . PRO A 338 ? 0.6249 0.6037 0.4871 0.0543 0.1826 -0.0543 331 PRO A CD 2263 N N . GLY A 339 ? 0.6166 0.6128 0.4552 0.0665 0.1980 -0.0768 332 GLY A N 2264 C CA . GLY A 339 ? 0.6340 0.6242 0.4639 0.0721 0.2087 -0.0849 332 GLY A CA 2265 C C . GLY A 339 ? 0.6439 0.6346 0.4701 0.0749 0.2145 -0.0885 332 GLY A C 2266 O O . GLY A 339 ? 0.6443 0.6330 0.4534 0.0779 0.2223 -0.0906 332 GLY A O 2267 N N . PHE A 340 ? 0.6572 0.6403 0.4728 0.0773 0.2212 -0.0968 333 PHE A N 2268 C CA . PHE A 340 ? 0.6693 0.6537 0.4928 0.0838 0.2251 -0.0999 333 PHE A CA 2269 C C . PHE A 340 ? 0.6976 0.6751 0.5186 0.0828 0.2341 -0.1000 333 PHE A C 2270 O O . PHE A 340 ? 0.6945 0.6712 0.5201 0.0790 0.2363 -0.0943 333 PHE A O 2271 C CB . PHE A 340 ? 0.6570 0.6442 0.4784 0.0900 0.2242 -0.1053 333 PHE A CB 2272 C CG . PHE A 340 ? 0.6432 0.6170 0.4897 0.0855 0.1975 -0.1016 333 PHE A CG 2273 C CD1 . PHE A 340 ? 0.6231 0.5994 0.4832 0.0972 0.1912 -0.1075 333 PHE A CD1 2274 C CD2 . PHE A 340 ? 0.6075 0.5753 0.4653 0.1150 0.1940 -0.0971 333 PHE A CD2 2275 C CE1 . PHE A 340 ? 0.6208 0.5800 0.4818 0.1003 0.1702 -0.1090 333 PHE A CE1 2276 C CE2 . PHE A 340 ? 0.5973 0.5637 0.4906 0.1083 0.1714 -0.0804 333 PHE A CE2 2277 C CZ . PHE A 340 ? 0.5900 0.5725 0.4704 0.1080 0.1754 -0.0901 333 PHE A CZ 2278 N N . THR A 341 ? 0.7133 0.6945 0.5407 0.0941 0.2449 -0.1048 334 THR A N 2279 C CA . THR A 341 ? 0.7457 0.7291 0.5750 0.0986 0.2550 -0.1081 334 THR A CA 2280 C C . THR A 341 ? 0.7700 0.7532 0.5726 0.0969 0.2657 -0.1120 334 THR A C 2281 O O . THR A 341 ? 0.7730 0.7526 0.5522 0.0907 0.2755 -0.1157 334 THR A O 2282 C CB . THR A 341 ? 0.7453 0.7302 0.5836 0.0974 0.2506 -0.1076 334 THR A CB 2283 O OG1 . THR A 341 ? 0.7175 0.7295 0.6284 0.1202 0.2552 -0.0996 334 THR A OG1 2284 C CG2 . THR A 341 ? 0.7518 0.7307 0.5865 0.1027 0.2518 -0.1115 334 THR A CG2 2285 N N . GLY A 342 ? 0.7959 0.7737 0.5871 0.1010 0.2685 -0.1118 335 GLY A N 2286 C CA . GLY A 342 ? 0.8147 0.7976 0.5860 0.1057 0.2799 -0.1150 335 GLY A CA 2287 C C . GLY A 342 ? 0.8290 0.8098 0.5956 0.1066 0.2792 -0.1146 335 GLY A C 2288 O O . GLY A 342 ? 0.8290 0.8232 0.5916 0.1052 0.2803 -0.1070 335 GLY A O 2289 N N . ASN A 343 ? 0.8403 0.8127 0.6090 0.1135 0.2755 -0.1196 336 ASN A N 2290 C CA . ASN A 343 ? 0.8547 0.8123 0.6221 0.1134 0.2624 -0.1267 336 ASN A CA 2291 C C . ASN A 343 ? 0.8506 0.7974 0.6130 0.1101 0.2500 -0.1297 336 ASN A C 2292 O O . ASN A 343 ? 0.8569 0.7975 0.6125 0.1027 0.2398 -0.1285 336 ASN A O 2293 C CB . ASN A 343 ? 0.8712 0.8157 0.6349 0.1162 0.2591 -0.1224 336 ASN A CB 2294 C CG . ASN A 343 ? 0.8919 0.8420 0.6815 0.1232 0.2555 -0.1211 336 ASN A CG 2295 O OD1 . ASN A 343 ? 0.9285 0.8302 0.7451 0.1221 0.2457 -0.1096 336 ASN A OD1 2296 N ND2 . ASN A 343 ? 0.9431 0.8504 0.7308 0.1179 0.2210 -0.0887 336 ASN A ND2 2297 N N . PHE A 344 ? 0.8325 0.7791 0.5975 0.1108 0.2448 -0.1301 337 PHE A N 2298 C CA . PHE A 344 ? 0.8215 0.7634 0.5795 0.1100 0.2312 -0.1340 337 PHE A CA 2299 C C . PHE A 344 ? 0.8161 0.7556 0.5575 0.1087 0.2293 -0.1325 337 PHE A C 2300 O O . PHE A 344 ? 0.8219 0.7518 0.5447 0.1102 0.2264 -0.1326 337 PHE A O 2301 C CB . PHE A 344 ? 0.8138 0.7582 0.5837 0.1102 0.2326 -0.1340 337 PHE A CB 2302 C CG . PHE A 344 ? 0.7992 0.7575 0.6003 0.1082 0.2229 -0.1379 337 PHE A CG 2303 C CD1 . PHE A 344 ? 0.7857 0.7411 0.6171 0.1086 0.2198 -0.1354 337 PHE A CD1 2304 C CD2 . PHE A 344 ? 0.7880 0.7558 0.6160 0.1077 0.2135 -0.1367 337 PHE A CD2 2305 C CE1 . PHE A 344 ? 0.7632 0.7477 0.6295 0.1072 0.2228 -0.1438 337 PHE A CE1 2306 C CE2 . PHE A 344 ? 0.7748 0.7549 0.6153 0.1099 0.2230 -0.1450 337 PHE A CE2 2307 C CZ . PHE A 344 ? 0.7609 0.7510 0.6320 0.1175 0.2171 -0.1401 337 PHE A CZ 2308 N N . SER A 345 ? 0.8145 0.7480 0.5318 0.1081 0.2226 -0.1346 338 SER A N 2309 C CA . SER A 345 ? 0.8102 0.7457 0.5070 0.1028 0.2193 -0.1267 338 SER A CA 2310 C C . SER A 345 ? 0.8093 0.7350 0.4876 0.1050 0.2096 -0.1307 338 SER A C 2311 O O . SER A 345 ? 0.8159 0.7372 0.4958 0.1018 0.1974 -0.1266 338 SER A O 2312 C CB . SER A 345 ? 0.8139 0.7508 0.5084 0.1003 0.2196 -0.1255 338 SER A CB 2313 O OG . SER A 345 ? 0.8193 0.7460 0.4961 0.0762 0.2406 -0.1053 338 SER A OG 2314 N N . THR A 346 ? 0.7969 0.7230 0.4615 0.1095 0.2083 -0.1350 339 THR A N 2315 C CA . THR A 346 ? 0.7953 0.7109 0.4543 0.1079 0.1966 -0.1395 339 THR A CA 2316 C C . THR A 346 ? 0.7722 0.6968 0.4614 0.1039 0.1843 -0.1402 339 THR A C 2317 O O . THR A 346 ? 0.7732 0.7064 0.4800 0.0972 0.1768 -0.1344 339 THR A O 2318 C CB . THR A 346 ? 0.7994 0.7166 0.4506 0.1064 0.1983 -0.1409 339 THR A CB 2319 O OG1 . THR A 346 ? 0.8267 0.7195 0.3753 0.1148 0.2170 -0.1499 339 THR A OG1 2320 C CG2 . THR A 346 ? 0.8135 0.7222 0.4438 0.0999 0.1929 -0.1290 339 THR A CG2 2321 N N . GLN A 347 ? 0.7474 0.6689 0.4533 0.1004 0.1789 -0.1462 340 GLN A N 2322 C CA . GLN A 347 ? 0.7128 0.6270 0.4365 0.1010 0.1716 -0.1590 340 GLN A CA 2323 C C . GLN A 347 ? 0.6877 0.6135 0.4132 0.0933 0.1656 -0.1577 340 GLN A C 2324 O O . GLN A 347 ? 0.6775 0.5900 0.3843 0.0989 0.1828 -0.1734 340 GLN A O 2325 C CB . GLN A 347 ? 0.7148 0.6271 0.4458 0.1026 0.1684 -0.1584 340 GLN A CB 2326 C CG . GLN A 347 ? 0.7051 0.6064 0.4381 0.1115 0.1859 -0.1705 340 GLN A CG 2327 C CD . GLN A 347 ? 0.7004 0.5890 0.4619 0.1194 0.1903 -0.1609 340 GLN A CD 2328 O OE1 . GLN A 347 ? 0.6949 0.5852 0.4890 0.1209 0.1725 -0.1452 340 GLN A OE1 2329 N NE2 . GLN A 347 ? 0.7033 0.5883 0.4499 0.1135 0.1901 -0.1481 340 GLN A NE2 2330 N N . LYS A 348 ? 0.6588 0.5901 0.3974 0.0864 0.1500 -0.1546 341 LYS A N 2331 C CA . LYS A 348 ? 0.6326 0.5762 0.3814 0.0800 0.1362 -0.1448 341 LYS A CA 2332 C C . LYS A 348 ? 0.6095 0.5536 0.3740 0.0733 0.1208 -0.1495 341 LYS A C 2333 O O . LYS A 348 ? 0.6129 0.5445 0.3644 0.0676 0.1161 -0.1595 341 LYS A O 2334 C CB . LYS A 348 ? 0.6303 0.5863 0.3868 0.0826 0.1355 -0.1392 341 LYS A CB 2335 C CG . LYS A 348 ? 0.6233 0.5847 0.3583 0.0865 0.1379 -0.1471 341 LYS A CG 2336 C CD . LYS A 348 ? 0.6382 0.5669 0.3472 0.0914 0.1384 -0.1446 341 LYS A CD 2337 C CE . LYS A 348 ? 0.6457 0.5624 0.3537 0.0900 0.1255 -0.1362 341 LYS A CE 2338 N NZ . LYS A 348 ? 0.6486 0.5547 0.3559 0.0884 0.1177 -0.1401 341 LYS A NZ 2339 N N . VAL A 349 ? 0.5675 0.5247 0.3544 0.0723 0.1174 -0.1466 342 VAL A N 2340 C CA . VAL A 349 ? 0.5377 0.5003 0.3374 0.0696 0.1023 -0.1486 342 VAL A CA 2341 C C . VAL A 349 ? 0.5366 0.4885 0.3328 0.0644 0.0937 -0.1484 342 VAL A C 2342 O O . VAL A 349 ? 0.5242 0.4808 0.3361 0.0772 0.0911 -0.1521 342 VAL A O 2343 C CB . VAL A 349 ? 0.5303 0.5010 0.3291 0.0682 0.1025 -0.1386 342 VAL A CB 2344 C CG1 . VAL A 349 ? 0.4993 0.4640 0.3048 0.0794 0.0965 -0.1763 342 VAL A CG1 2345 C CG2 . VAL A 349 ? 0.5348 0.5102 0.3247 0.0713 0.1108 -0.1224 342 VAL A CG2 2346 N N . LYS A 350 ? 0.5218 0.4701 0.3247 0.0511 0.0831 -0.1512 343 LYS A N 2347 C CA . LYS A 350 ? 0.5140 0.4600 0.3241 0.0418 0.0631 -0.1437 343 LYS A CA 2348 C C . LYS A 350 ? 0.4942 0.4487 0.3227 0.0440 0.0621 -0.1436 343 LYS A C 2349 O O . LYS A 350 ? 0.4883 0.4624 0.3125 0.0503 0.0692 -0.1308 343 LYS A O 2350 C CB . LYS A 350 ? 0.5214 0.4689 0.3192 0.0371 0.0567 -0.1463 343 LYS A CB 2351 C CG . LYS A 350 ? 0.5264 0.4678 0.3127 0.0181 0.0346 -0.1534 343 LYS A CG 2352 C CD . LYS A 350 ? 0.5895 0.5174 0.3374 -0.0008 0.0164 -0.1621 343 LYS A CD 2353 C CE . LYS A 350 ? 0.6127 0.5454 0.3380 -0.0032 -0.0066 -0.1647 343 LYS A CE 2354 N NZ . LYS A 350 ? 0.6700 0.5474 0.4012 0.0080 -0.0349 -0.1666 343 LYS A NZ 2355 N N . MET A 351 ? 0.4808 0.4303 0.3221 0.0371 0.0496 -0.1406 344 MET A N 2356 C CA . MET A 351 ? 0.4667 0.4176 0.3241 0.0371 0.0423 -0.1419 344 MET A CA 2357 C C . MET A 351 ? 0.4681 0.4180 0.3291 0.0327 0.0372 -0.1368 344 MET A C 2358 O O . MET A 351 ? 0.4658 0.4199 0.3024 0.0169 0.0294 -0.1413 344 MET A O 2359 C CB . MET A 351 ? 0.4695 0.4047 0.3074 0.0346 0.0366 -0.1483 344 MET A CB 2360 C CG . MET A 351 ? 0.4549 0.3798 0.2783 0.0328 0.0510 -0.1494 344 MET A CG 2361 S SD . MET A 351 ? 0.4548 0.3716 0.2542 0.0313 0.0632 -0.1234 344 MET A SD 2362 C CE . MET A 351 ? 0.3892 0.4151 0.1957 0.0295 0.0057 -0.1527 344 MET A CE 2363 N N . HIS A 352 ? 0.4523 0.4106 0.3314 0.0412 0.0424 -0.1352 345 HIS A N 2364 C CA . HIS A 352 ? 0.4302 0.4067 0.3255 0.0385 0.0347 -0.1414 345 HIS A CA 2365 C C . HIS A 352 ? 0.4140 0.3947 0.3280 0.0369 0.0346 -0.1427 345 HIS A C 2366 O O . HIS A 352 ? 0.3857 0.3974 0.3195 0.0432 0.0465 -0.1433 345 HIS A O 2367 C CB . HIS A 352 ? 0.4337 0.4098 0.3304 0.0450 0.0334 -0.1463 345 HIS A CB 2368 C CG . HIS A 352 ? 0.4850 0.4445 0.3387 0.0453 0.0471 -0.1466 345 HIS A CG 2369 N ND1 . HIS A 352 ? 0.5053 0.4558 0.3557 0.0367 0.0778 -0.1446 345 HIS A ND1 2370 C CD2 . HIS A 352 ? 0.5237 0.4482 0.3627 0.0512 0.0461 -0.1646 345 HIS A CD2 2371 C CE1 . HIS A 352 ? 0.5403 0.4707 0.3502 0.0361 0.0600 -0.1586 345 HIS A CE1 2372 N NE2 . HIS A 352 ? 0.5502 0.4544 0.3701 0.0323 0.0638 -0.1792 345 HIS A NE2 2373 N N . ILE A 353 ? 0.4002 0.3766 0.3223 0.0376 0.0196 -0.1391 346 ILE A N 2374 C CA . ILE A 353 ? 0.3983 0.3617 0.3242 0.0323 0.0185 -0.1398 346 ILE A CA 2375 C C . ILE A 353 ? 0.4072 0.3739 0.3352 0.0297 0.0069 -0.1350 346 ILE A C 2376 O O . ILE A 353 ? 0.4067 0.3751 0.3506 0.0337 -0.0162 -0.1391 346 ILE A O 2377 C CB . ILE A 353 ? 0.4015 0.3733 0.3146 0.0293 0.0281 -0.1380 346 ILE A CB 2378 C CG1 . ILE A 353 ? 0.3939 0.3581 0.3272 0.0340 0.0264 -0.1103 346 ILE A CG1 2379 C CG2 . ILE A 353 ? 0.4174 0.3104 0.2865 0.0256 0.0318 -0.1616 346 ILE A CG2 2380 C CD1 . ILE A 353 ? 0.3750 0.3939 0.2937 0.0401 0.0553 -0.0938 346 ILE A CD1 2381 N N . HIS A 354 ? 0.3980 0.3548 0.3391 0.0260 0.0017 -0.1368 347 HIS A N 2382 C CA . HIS A 354 ? 0.3947 0.3713 0.3347 0.0279 -0.0037 -0.1383 347 HIS A CA 2383 C C . HIS A 354 ? 0.3740 0.3517 0.3251 0.0302 -0.0073 -0.1326 347 HIS A C 2384 O O . HIS A 354 ? 0.3725 0.3523 0.3132 0.0268 -0.0192 -0.1428 347 HIS A O 2385 C CB . HIS A 354 ? 0.3907 0.3667 0.3316 0.0231 -0.0063 -0.1428 347 HIS A CB 2386 C CG . HIS A 354 ? 0.4646 0.4466 0.3737 0.0454 0.0177 -0.1504 347 HIS A CG 2387 N ND1 . HIS A 354 ? 0.4848 0.4785 0.4069 0.0512 0.0102 -0.1474 347 HIS A ND1 2388 C CD2 . HIS A 354 ? 0.5045 0.4914 0.3703 0.0669 0.0022 -0.1690 347 HIS A CD2 2389 C CE1 . HIS A 354 ? 0.5071 0.5142 0.4145 0.0572 0.0291 -0.1451 347 HIS A CE1 2390 N NE2 . HIS A 354 ? 0.5327 0.5540 0.3924 0.0375 0.0272 -0.1336 347 HIS A NE2 2391 N N . SER A 355 ? 0.3476 0.3267 0.3121 0.0300 -0.0129 -0.1247 348 SER A N 2392 C CA . SER A 355 ? 0.3322 0.3259 0.3099 0.0273 -0.0068 -0.1063 348 SER A CA 2393 C C . SER A 355 ? 0.3305 0.3315 0.3207 0.0230 -0.0084 -0.1032 348 SER A C 2394 O O . SER A 355 ? 0.3264 0.3398 0.3066 0.0285 -0.0037 -0.1009 348 SER A O 2395 C CB . SER A 355 ? 0.3157 0.3247 0.2934 0.0257 -0.0161 -0.1062 348 SER A CB 2396 O OG . SER A 355 ? 0.3319 0.2883 0.2900 0.0199 0.0050 -0.1075 348 SER A OG 2397 N N . THR A 356 ? 0.3313 0.3161 0.3254 0.0126 -0.0079 -0.1056 349 THR A N 2398 C CA . THR A 356 ? 0.3386 0.3236 0.3425 0.0002 0.0018 -0.1067 349 THR A CA 2399 C C . THR A 356 ? 0.3304 0.3224 0.3332 0.0070 0.0006 -0.0970 349 THR A C 2400 O O . THR A 356 ? 0.3486 0.3360 0.3456 0.0226 0.0117 -0.0993 349 THR A O 2401 C CB . THR A 356 ? 0.3543 0.3327 0.3397 -0.0073 0.0041 -0.1091 349 THR A CB 2402 O OG1 . THR A 356 ? 0.3822 0.3504 0.4017 -0.0159 0.0252 -0.0852 349 THR A OG1 2403 C CG2 . THR A 356 ? 0.3375 0.3118 0.3436 -0.0192 -0.0101 -0.1397 349 THR A CG2 2404 N N . ASN A 357 ? 0.3189 0.3082 0.3321 0.0051 0.0000 -0.0868 350 ASN A N 2405 C CA . ASN A 357 ? 0.3086 0.3092 0.3151 0.0016 0.0001 -0.0792 350 ASN A CA 2406 C C . ASN A 357 ? 0.3130 0.3135 0.3261 -0.0030 -0.0103 -0.0773 350 ASN A C 2407 O O . ASN A 357 ? 0.2842 0.3302 0.3047 -0.0199 -0.0268 -0.0794 350 ASN A O 2408 C CB . ASN A 357 ? 0.3187 0.3012 0.3211 -0.0047 0.0164 -0.0894 350 ASN A CB 2409 C CG . ASN A 357 ? 0.3493 0.3364 0.3163 0.0104 0.0212 -0.0745 350 ASN A CG 2410 O OD1 . ASN A 357 ? 0.3681 0.3456 0.2462 -0.0103 0.0136 -0.0758 350 ASN A OD1 2411 N ND2 . ASN A 357 ? 0.4058 0.3528 0.3188 0.0431 0.0496 -0.0652 350 ASN A ND2 2412 N N . GLU A 358 ? 0.3062 0.3033 0.3220 0.0082 -0.0036 -0.0772 351 GLU A N 2413 C CA . GLU A 358 ? 0.3104 0.2904 0.3492 -0.0015 -0.0053 -0.0730 351 GLU A CA 2414 C C . GLU A 358 ? 0.2856 0.2669 0.3297 0.0079 -0.0001 -0.0675 351 GLU A C 2415 O O . GLU A 358 ? 0.2576 0.2466 0.3113 0.0349 0.0102 -0.0668 351 GLU A O 2416 C CB . GLU A 358 ? 0.3393 0.3154 0.3722 0.0053 -0.0075 -0.0718 351 GLU A CB 2417 C CG . GLU A 358 ? 0.4113 0.3610 0.4645 -0.0114 -0.0366 -0.0565 351 GLU A CG 2418 C CD . GLU A 358 ? 0.5702 0.4206 0.5376 -0.0586 -0.0662 -0.0861 351 GLU A CD 2419 O OE1 . GLU A 358 ? 0.6011 0.5486 0.5686 -0.0981 -0.0858 -0.0711 351 GLU A OE1 2420 O OE2 . GLU A 358 ? 0.6129 0.3886 0.5788 -0.0645 -0.0597 -0.0664 351 GLU A OE2 2421 N N . VAL A 359 ? 0.2707 0.2448 0.3237 0.0175 -0.0059 -0.0595 352 VAL A N 2422 C CA . VAL A 359 ? 0.2560 0.2314 0.3037 0.0175 0.0021 -0.0455 352 VAL A CA 2423 C C . VAL A 359 ? 0.2540 0.2328 0.3205 0.0117 0.0004 -0.0479 352 VAL A C 2424 O O . VAL A 359 ? 0.2292 0.2104 0.3297 -0.0150 0.0028 -0.0385 352 VAL A O 2425 C CB . VAL A 359 ? 0.2542 0.2448 0.3009 0.0219 0.0013 -0.0461 352 VAL A CB 2426 C CG1 . VAL A 359 ? 0.2417 0.2226 0.2845 0.0078 -0.0289 -0.0599 352 VAL A CG1 2427 C CG2 . VAL A 359 ? 0.2308 0.2280 0.2958 0.0214 0.0226 -0.0306 352 VAL A CG2 2428 N N . THR A 360 ? 0.2256 0.2247 0.2831 0.0227 0.0041 -0.0423 353 THR A N 2429 C CA . THR A 360 ? 0.2332 0.2372 0.2907 0.0233 0.0094 -0.0400 353 THR A CA 2430 C C . THR A 360 ? 0.2292 0.2338 0.2867 0.0185 0.0094 -0.0279 353 THR A C 2431 O O . THR A 360 ? 0.2195 0.2170 0.2790 0.0184 -0.0123 -0.0388 353 THR A O 2432 C CB . THR A 360 ? 0.2028 0.2360 0.2794 0.0204 0.0138 -0.0321 353 THR A CB 2433 O OG1 . THR A 360 ? 0.2305 0.2417 0.2897 -0.0009 0.0162 -0.0440 353 THR A OG1 2434 C CG2 . THR A 360 ? 0.2183 0.2694 0.2710 0.0121 0.0010 -0.0172 353 THR A CG2 2435 N N . ARG A 361 ? 0.2131 0.2225 0.3015 0.0172 0.0210 -0.0165 354 ARG A N 2436 C CA . ARG A 361 ? 0.2244 0.2361 0.2925 0.0019 0.0125 -0.0014 354 ARG A CA 2437 C C . ARG A 361 ? 0.2200 0.2194 0.2940 0.0027 0.0159 -0.0077 354 ARG A C 2438 O O . ARG A 361 ? 0.2312 0.2223 0.2893 0.0053 0.0118 -0.0089 354 ARG A O 2439 C CB . ARG A 361 ? 0.2224 0.2570 0.3063 0.0063 0.0315 -0.0036 354 ARG A CB 2440 C CG . ARG A 361 ? 0.2161 0.2840 0.2946 -0.0141 0.0094 0.0159 354 ARG A CG 2441 C CD . ARG A 361 ? 0.2330 0.2878 0.3530 -0.0237 0.0139 0.0110 354 ARG A CD 2442 N NE . ARG A 361 ? 0.1891 0.2316 0.4089 -0.0431 0.0050 -0.0143 354 ARG A NE 2443 C CZ . ARG A 361 ? 0.2112 0.2890 0.4365 -0.0398 0.0014 0.0222 354 ARG A CZ 2444 N NH1 . ARG A 361 ? 0.1652 0.2692 0.4543 -0.0727 -0.0208 0.0096 354 ARG A NH1 2445 N NH2 . ARG A 361 ? 0.2250 0.3167 0.4429 -0.0399 -0.0247 0.0328 354 ARG A NH2 2446 N N . ILE A 362 ? 0.2063 0.1940 0.2787 -0.0029 0.0071 0.0032 355 ILE A N 2447 C CA . ILE A 362 ? 0.2123 0.1984 0.2741 0.0030 0.0250 -0.0080 355 ILE A CA 2448 C C . ILE A 362 ? 0.2206 0.2053 0.2861 0.0087 0.0224 -0.0067 355 ILE A C 2449 O O . ILE A 362 ? 0.2020 0.2113 0.2868 0.0239 0.0438 -0.0001 355 ILE A O 2450 C CB . ILE A 362 ? 0.1908 0.1916 0.2755 -0.0042 0.0161 -0.0103 355 ILE A CB 2451 C CG1 . ILE A 362 ? 0.1699 0.1580 0.2546 -0.0030 0.0149 -0.0188 355 ILE A CG1 2452 C CG2 . ILE A 362 ? 0.1703 0.1770 0.2392 0.0053 0.0304 -0.0129 355 ILE A CG2 2453 C CD1 . ILE A 362 ? 0.2181 0.1506 0.2474 -0.0075 -0.0225 -0.0071 355 ILE A CD1 2454 N N . TYR A 363 ? 0.2244 0.1881 0.2738 0.0161 0.0161 0.0005 356 TYR A N 2455 C CA . TYR A 363 ? 0.2280 0.1931 0.2632 0.0120 0.0265 0.0004 356 TYR A CA 2456 C C . TYR A 363 ? 0.2270 0.2030 0.2497 0.0059 0.0294 0.0048 356 TYR A C 2457 O O . TYR A 363 ? 0.2468 0.2246 0.2374 -0.0004 0.0277 -0.0011 356 TYR A O 2458 C CB . TYR A 363 ? 0.2232 0.1811 0.2718 0.0095 0.0250 0.0085 356 TYR A CB 2459 C CG . TYR A 363 ? 0.2524 0.1972 0.3222 0.0054 0.0208 0.0091 356 TYR A CG 2460 C CD1 . TYR A 363 ? 0.2241 0.1716 0.3187 -0.0021 0.0270 0.0393 356 TYR A CD1 2461 C CD2 . TYR A 363 ? 0.2722 0.1881 0.3041 0.0131 0.0014 0.0350 356 TYR A CD2 2462 C CE1 . TYR A 363 ? 0.2533 0.1899 0.3375 0.0163 0.0094 0.0307 356 TYR A CE1 2463 C CE2 . TYR A 363 ? 0.2562 0.2540 0.3468 0.0092 -0.0018 0.0393 356 TYR A CE2 2464 C CZ . TYR A 363 ? 0.2750 0.2543 0.3608 -0.0026 0.0246 0.0216 356 TYR A CZ 2465 O OH . TYR A 363 ? 0.2717 0.2590 0.3901 -0.0102 0.0043 0.0328 356 TYR A OH 2466 N N . ASN A 364 ? 0.2479 0.1975 0.2412 0.0049 0.0164 0.0141 357 ASN A N 2467 C CA . ASN A 364 ? 0.2615 0.2279 0.2429 0.0085 0.0187 0.0239 357 ASN A CA 2468 C C . ASN A 364 ? 0.2614 0.2382 0.2431 0.0132 0.0256 0.0383 357 ASN A C 2469 O O . ASN A 364 ? 0.2903 0.2726 0.2568 -0.0010 0.0218 0.0494 357 ASN A O 2470 C CB . ASN A 364 ? 0.2447 0.2044 0.2253 0.0120 0.0134 0.0178 357 ASN A CB 2471 C CG . ASN A 364 ? 0.2399 0.2175 0.2773 0.0217 0.0137 0.0220 357 ASN A CG 2472 O OD1 . ASN A 364 ? 0.2632 0.2055 0.2672 0.0131 -0.0068 -0.0118 357 ASN A OD1 2473 N ND2 . ASN A 364 ? 0.2404 0.2057 0.2770 0.0637 -0.0053 0.0364 357 ASN A ND2 2474 N N . VAL A 365 ? 0.2655 0.2157 0.2305 0.0149 0.0299 0.0291 358 VAL A N 2475 C CA . VAL A 365 ? 0.2600 0.2080 0.2186 0.0340 0.0342 0.0142 358 VAL A CA 2476 C C . VAL A 365 ? 0.2609 0.1949 0.2304 0.0409 0.0367 0.0099 358 VAL A C 2477 O O . VAL A 365 ? 0.2876 0.1926 0.2242 0.0489 0.0148 -0.0055 358 VAL A O 2478 C CB . VAL A 365 ? 0.2684 0.1903 0.2182 0.0408 0.0476 0.0156 358 VAL A CB 2479 C CG1 . VAL A 365 ? 0.2608 0.2005 0.1861 0.0448 0.0083 0.0318 358 VAL A CG1 2480 C CG2 . VAL A 365 ? 0.2466 0.2062 0.2054 0.0327 0.0484 -0.0093 358 VAL A CG2 2481 N N . ILE A 366 ? 0.2555 0.1977 0.2187 0.0514 0.0260 0.0189 359 ILE A N 2482 C CA . ILE A 366 ? 0.2522 0.1959 0.2171 0.0458 0.0279 0.0231 359 ILE A CA 2483 C C . ILE A 366 ? 0.2752 0.2075 0.2349 0.0533 0.0381 0.0252 359 ILE A C 2484 O O . ILE A 366 ? 0.3007 0.2236 0.2568 0.0500 0.0353 0.0424 359 ILE A O 2485 C CB . ILE A 366 ? 0.2588 0.1912 0.2180 0.0522 0.0363 0.0197 359 ILE A CB 2486 C CG1 . ILE A 366 ? 0.1652 0.1954 0.1877 0.0338 0.0226 0.0539 359 ILE A CG1 2487 C CG2 . ILE A 366 ? 0.2340 0.2208 0.1799 0.0100 0.0256 -0.0030 359 ILE A CG2 2488 C CD1 . ILE A 366 ? 0.2648 0.2706 0.2188 -0.0082 0.0713 0.0469 359 ILE A CD1 2489 N N . GLY A 367 ? 0.2799 0.2050 0.2331 0.0535 0.0391 0.0214 360 GLY A N 2490 C CA . GLY A 367 ? 0.2882 0.2143 0.2138 0.0522 0.0528 0.0275 360 GLY A CA 2491 C C . GLY A 367 ? 0.3047 0.2300 0.2167 0.0583 0.0534 0.0302 360 GLY A C 2492 O O . GLY A 367 ? 0.3114 0.2228 0.2269 0.0529 0.0668 0.0133 360 GLY A O 2493 N N . THR A 368 ? 0.3031 0.2474 0.2183 0.0692 0.0556 0.0271 361 THR A N 2494 C CA . THR A 368 ? 0.3284 0.2414 0.2182 0.0821 0.0433 0.0428 361 THR A CA 2495 C C . THR A 368 ? 0.3498 0.2585 0.2304 0.0842 0.0441 0.0394 361 THR A C 2496 O O . THR A 368 ? 0.3381 0.2286 0.2229 0.0791 0.0606 0.0535 361 THR A O 2497 C CB . THR A 368 ? 0.3290 0.2469 0.2110 0.0851 0.0409 0.0285 361 THR A CB 2498 O OG1 . THR A 368 ? 0.3418 0.2673 0.2524 0.0730 0.0186 0.0970 361 THR A OG1 2499 C CG2 . THR A 368 ? 0.3286 0.2505 0.2463 0.0696 0.0543 0.0263 361 THR A CG2 2500 N N . LEU A 369 ? 0.3554 0.2579 0.2270 0.0925 0.0373 0.0429 362 LEU A N 2501 C CA . LEU A 369 ? 0.3748 0.2697 0.2042 0.1056 0.0366 0.0396 362 LEU A CA 2502 C C . LEU A 369 ? 0.3821 0.2796 0.2041 0.1068 0.0423 0.0456 362 LEU A C 2503 O O . LEU A 369 ? 0.3952 0.2739 0.2052 0.0990 0.0421 0.0385 362 LEU A O 2504 C CB . LEU A 369 ? 0.3796 0.2762 0.1876 0.0962 0.0289 0.0498 362 LEU A CB 2505 C CG . LEU A 369 ? 0.3876 0.3306 0.2366 0.0882 0.0059 0.0615 362 LEU A CG 2506 C CD1 . LEU A 369 ? 0.3989 0.4175 0.1122 0.0934 0.0212 0.0761 362 LEU A CD1 2507 C CD2 . LEU A 369 ? 0.3505 0.3481 0.2422 0.1232 0.0049 0.0299 362 LEU A CD2 2508 N N A ARG A 370 ? 0.3843 0.2796 0.1967 0.1117 0.0461 0.0438 363 ARG A N 2509 N N B ARG A 370 ? 0.3830 0.2780 0.1953 0.1119 0.0466 0.0428 363 ARG A N 2510 N N C ARG A 370 ? 0.3824 0.2784 0.1986 0.1111 0.0461 0.0439 363 ARG A N 2511 C CA A ARG A 370 ? 0.3887 0.2864 0.1965 0.1155 0.0488 0.0472 363 ARG A CA 2512 C CA B ARG A 370 ? 0.3859 0.2841 0.1942 0.1152 0.0505 0.0451 363 ARG A CA 2513 C CA C ARG A 370 ? 0.3836 0.2840 0.1999 0.1146 0.0490 0.0467 363 ARG A CA 2514 C C A ARG A 370 ? 0.3920 0.2860 0.2022 0.1163 0.0451 0.0467 363 ARG A C 2515 C C B ARG A 370 ? 0.3908 0.2850 0.1998 0.1161 0.0455 0.0459 363 ARG A C 2516 C C C ARG A 370 ? 0.3896 0.2850 0.2024 0.1158 0.0454 0.0470 363 ARG A C 2517 O O A ARG A 370 ? 0.3873 0.2876 0.1875 0.1182 0.0376 0.0400 363 ARG A O 2518 O O B ARG A 370 ? 0.3866 0.2889 0.1805 0.1169 0.0391 0.0397 363 ARG A O 2519 O O C ARG A 370 ? 0.3859 0.2877 0.1873 0.1169 0.0397 0.0416 363 ARG A O 2520 C CB A ARG A 370 ? 0.3882 0.2908 0.2062 0.1151 0.0462 0.0517 363 ARG A CB 2521 C CB B ARG A 370 ? 0.3839 0.2854 0.2024 0.1156 0.0485 0.0483 363 ARG A CB 2522 C CB C ARG A 370 ? 0.3816 0.2861 0.2077 0.1138 0.0477 0.0500 363 ARG A CB 2523 C CG A ARG A 370 ? 0.3990 0.2838 0.1954 0.1152 0.0640 0.0574 363 ARG A CG 2524 C CG B ARG A 370 ? 0.3890 0.2718 0.1865 0.1121 0.0745 0.0422 363 ARG A CG 2525 C CG C ARG A 370 ? 0.3723 0.2730 0.2114 0.1129 0.0637 0.0474 363 ARG A CG 2526 C CD A ARG A 370 ? 0.4128 0.3225 0.2480 0.1030 0.0566 0.0830 363 ARG A CD 2527 C CD B ARG A 370 ? 0.4007 0.2926 0.2043 0.1031 0.0703 0.0557 363 ARG A CD 2528 C CD C ARG A 370 ? 0.3710 0.2704 0.2337 0.1105 0.0757 0.0483 363 ARG A CD 2529 N NE A ARG A 370 ? 0.4356 0.3533 0.2997 0.1011 0.0643 0.0927 363 ARG A NE 2530 N NE B ARG A 370 ? 0.4276 0.3082 0.2485 0.0865 0.0971 0.0536 363 ARG A NE 2531 N NE C ARG A 370 ? 0.3392 0.2626 0.2436 0.1045 0.0908 0.0476 363 ARG A NE 2532 C CZ A ARG A 370 ? 0.4160 0.3461 0.2893 0.1185 0.0634 0.1065 363 ARG A CZ 2533 C CZ B ARG A 370 ? 0.4200 0.2837 0.2137 0.0962 0.1055 0.0545 363 ARG A CZ 2534 C CZ C ARG A 370 ? 0.3143 0.2564 0.2531 0.1151 0.1022 0.0459 363 ARG A CZ 2535 N NH1 A ARG A 370 ? 0.4027 0.3501 0.3217 0.1109 0.0462 0.1106 363 ARG A NH1 2536 N NH1 B ARG A 370 ? 0.4010 0.3075 0.2071 0.0806 0.1158 0.0559 363 ARG A NH1 2537 N NH1 C ARG A 370 ? 0.2869 0.2325 0.2768 0.1003 0.1044 0.0511 363 ARG A NH1 2538 N NH2 A ARG A 370 ? 0.4224 0.3438 0.3235 0.1050 0.0658 0.1159 363 ARG A NH2 2539 N NH2 B ARG A 370 ? 0.4026 0.2691 0.1208 0.0956 0.1099 0.0424 363 ARG A NH2 2540 N NH2 C ARG A 370 ? 0.2931 0.2569 0.2703 0.1226 0.0932 0.0471 363 ARG A NH2 2541 N N . GLY A 371 ? 0.3885 0.2860 0.2001 0.1203 0.0467 0.0507 364 GLY A N 2542 C CA . GLY A 371 ? 0.4013 0.2864 0.1885 0.1202 0.0374 0.0488 364 GLY A CA 2543 C C . GLY A 371 ? 0.4270 0.3042 0.1966 0.1208 0.0286 0.0517 364 GLY A C 2544 O O . GLY A 371 ? 0.4190 0.2986 0.1860 0.1257 0.0136 0.0544 364 GLY A O 2545 N N . ALA A 372 ? 0.4468 0.3092 0.1902 0.1231 0.0289 0.0616 365 ALA A N 2546 C CA . ALA A 372 ? 0.4540 0.3150 0.1892 0.1433 0.0345 0.0421 365 ALA A CA 2547 C C . ALA A 372 ? 0.4649 0.3319 0.1961 0.1392 0.0314 0.0444 365 ALA A C 2548 O O . ALA A 372 ? 0.4716 0.3440 0.1940 0.1460 0.0557 0.0309 365 ALA A O 2549 C CB . ALA A 372 ? 0.4537 0.3032 0.1905 0.1429 0.0330 0.0542 365 ALA A CB 2550 N N . VAL A 373 ? 0.4711 0.3350 0.1726 0.1399 0.0242 0.0467 366 VAL A N 2551 C CA . VAL A 373 ? 0.4640 0.3279 0.1751 0.1443 0.0239 0.0413 366 VAL A CA 2552 C C . VAL A 373 ? 0.4476 0.3193 0.1811 0.1421 0.0253 0.0378 366 VAL A C 2553 O O . VAL A 373 ? 0.4412 0.3301 0.1790 0.1486 0.0408 0.0363 366 VAL A O 2554 C CB . VAL A 373 ? 0.4806 0.3294 0.1788 0.1382 0.0191 0.0393 366 VAL A CB 2555 C CG1 . VAL A 373 ? 0.4511 0.3151 0.1613 0.1592 0.0639 0.0260 366 VAL A CG1 2556 C CG2 . VAL A 373 ? 0.4884 0.3721 0.1925 0.1360 0.0108 0.0465 366 VAL A CG2 2557 N N . GLU A 374 ? 0.4242 0.3164 0.1689 0.1404 0.0170 0.0339 367 GLU A N 2558 C CA . GLU A 374 ? 0.4157 0.3086 0.1820 0.1347 0.0155 0.0192 367 GLU A CA 2559 C C . GLU A 374 ? 0.3882 0.2968 0.1631 0.1263 0.0133 0.0217 367 GLU A C 2560 O O . GLU A 374 ? 0.3587 0.2898 0.1236 0.1284 0.0001 0.0083 367 GLU A O 2561 C CB . GLU A 374 ? 0.4075 0.3006 0.1957 0.1313 0.0083 0.0155 367 GLU A CB 2562 C CG . GLU A 374 ? 0.4441 0.3307 0.2311 0.1332 0.0005 -0.0016 367 GLU A CG 2563 C CD . GLU A 374 ? 0.4561 0.3412 0.2436 0.1308 -0.0290 0.0042 367 GLU A CD 2564 O OE1 . GLU A 374 ? 0.4862 0.3576 0.2103 0.1507 -0.0890 -0.0205 367 GLU A OE1 2565 O OE2 . GLU A 374 ? 0.4224 0.3406 0.2825 0.1790 -0.0080 0.0030 367 GLU A OE2 2566 N N . PRO A 375 ? 0.3820 0.2952 0.1712 0.1208 0.0257 0.0261 368 PRO A N 2567 C CA . PRO A 375 ? 0.3737 0.2745 0.1739 0.1114 0.0253 0.0343 368 PRO A CA 2568 C C . PRO A 375 ? 0.3557 0.2757 0.1767 0.1043 0.0183 0.0244 368 PRO A C 2569 O O . PRO A 375 ? 0.3526 0.2705 0.1666 0.0933 0.0432 0.0340 368 PRO A O 2570 C CB . PRO A 375 ? 0.3641 0.2682 0.1757 0.1227 0.0253 0.0267 368 PRO A CB 2571 C CG . PRO A 375 ? 0.3861 0.2963 0.1885 0.1119 0.0319 0.0328 368 PRO A CG 2572 C CD . PRO A 375 ? 0.3938 0.2998 0.1833 0.1169 0.0280 0.0273 368 PRO A CD 2573 N N . ASP A 376 ? 0.3401 0.2575 0.1779 0.0998 0.0103 0.0291 369 ASP A N 2574 C CA . ASP A 376 ? 0.3365 0.2625 0.1955 0.0940 0.0160 0.0115 369 ASP A CA 2575 C C . ASP A 376 ? 0.3222 0.2409 0.1817 0.0918 0.0100 0.0043 369 ASP A C 2576 O O . ASP A 376 ? 0.3084 0.2262 0.1709 0.0858 0.0050 -0.0065 369 ASP A O 2577 C CB . ASP A 376 ? 0.3254 0.2607 0.2042 0.1013 0.0056 0.0083 369 ASP A CB 2578 C CG . ASP A 376 ? 0.3889 0.3141 0.2662 0.0987 0.0289 -0.0031 369 ASP A CG 2579 O OD1 . ASP A 376 ? 0.3820 0.3449 0.3097 0.0787 0.0196 -0.0236 369 ASP A OD1 2580 O OD2 . ASP A 376 ? 0.4498 0.3314 0.3387 0.1245 0.0970 -0.0352 369 ASP A OD2 2581 N N . ARG A 377 ? 0.3159 0.2372 0.1910 0.0824 0.0109 -0.0080 370 ARG A N 2582 C CA . ARG A 377 ? 0.3069 0.2274 0.1840 0.0896 0.0117 -0.0040 370 ARG A CA 2583 C C . ARG A 377 ? 0.3015 0.2377 0.1859 0.0849 0.0095 -0.0043 370 ARG A C 2584 O O . ARG A 377 ? 0.3058 0.2360 0.1874 0.0888 0.0043 -0.0012 370 ARG A O 2585 C CB . ARG A 377 ? 0.2958 0.2251 0.1795 0.0924 -0.0040 -0.0026 370 ARG A CB 2586 C CG . ARG A 377 ? 0.3194 0.1895 0.1502 0.0872 0.0113 0.0117 370 ARG A CG 2587 C CD . ARG A 377 ? 0.2935 0.2377 0.1531 0.1252 -0.0486 0.0342 370 ARG A CD 2588 N NE . ARG A 377 ? 0.3150 0.2120 0.1441 0.1032 -0.0356 0.0496 370 ARG A NE 2589 C CZ . ARG A 377 ? 0.2893 0.2267 0.1775 0.1149 0.0170 0.0013 370 ARG A CZ 2590 N NH1 . ARG A 377 ? 0.3233 0.2117 0.1435 0.0858 0.0167 0.0228 370 ARG A NH1 2591 N NH2 . ARG A 377 ? 0.2950 0.2046 0.1410 0.0937 0.0118 0.0041 370 ARG A NH2 2592 N N . TYR A 378 ? 0.3003 0.2393 0.1741 0.0769 0.0039 -0.0074 371 TYR A N 2593 C CA . TYR A 378 ? 0.2807 0.2385 0.1769 0.0751 0.0078 -0.0047 371 TYR A CA 2594 C C . TYR A 378 ? 0.2843 0.2359 0.1845 0.0783 -0.0032 -0.0055 371 TYR A C 2595 O O . TYR A 378 ? 0.2692 0.2401 0.1931 0.0813 0.0156 0.0054 371 TYR A O 2596 C CB . TYR A 378 ? 0.2756 0.2427 0.1721 0.0589 0.0049 0.0003 371 TYR A CB 2597 C CG . TYR A 378 ? 0.2843 0.2435 0.1967 0.0743 0.0072 -0.0066 371 TYR A CG 2598 C CD1 . TYR A 378 ? 0.2627 0.2438 0.2025 0.0614 -0.0026 0.0003 371 TYR A CD1 2599 C CD2 . TYR A 378 ? 0.2762 0.1983 0.2133 0.0759 0.0154 0.0296 371 TYR A CD2 2600 C CE1 . TYR A 378 ? 0.2939 0.2698 0.2199 0.0721 0.0143 0.0081 371 TYR A CE1 2601 C CE2 . TYR A 378 ? 0.2806 0.2225 0.2196 0.1047 0.0196 0.0203 371 TYR A CE2 2602 C CZ . TYR A 378 ? 0.2746 0.2291 0.2482 0.0957 0.0184 0.0418 371 TYR A CZ 2603 O OH . TYR A 378 ? 0.2605 0.2211 0.2337 0.0655 0.0104 0.0249 371 TYR A OH 2604 N N . VAL A 379 ? 0.2788 0.2210 0.1786 0.0823 -0.0115 -0.0114 372 VAL A N 2605 C CA . VAL A 379 ? 0.2723 0.2206 0.1739 0.0915 -0.0059 -0.0240 372 VAL A CA 2606 C C . VAL A 379 ? 0.2744 0.2247 0.1775 0.0809 -0.0036 -0.0183 372 VAL A C 2607 O O . VAL A 379 ? 0.2686 0.2282 0.1632 0.0747 0.0033 -0.0095 372 VAL A O 2608 C CB . VAL A 379 ? 0.2609 0.2178 0.1778 0.0967 -0.0103 -0.0369 372 VAL A CB 2609 C CG1 . VAL A 379 ? 0.2559 0.1912 0.1594 0.1233 -0.0145 0.0020 372 VAL A CG1 2610 C CG2 . VAL A 379 ? 0.2911 0.2013 0.1400 0.0880 -0.0095 -0.0167 372 VAL A CG2 2611 N N . ILE A 380 ? 0.2589 0.2303 0.1804 0.0806 -0.0135 -0.0137 373 ILE A N 2612 C CA . ILE A 380 ? 0.2471 0.2208 0.1773 0.0732 -0.0052 -0.0103 373 ILE A CA 2613 C C . ILE A 380 ? 0.2559 0.2114 0.1894 0.0683 -0.0096 -0.0045 373 ILE A C 2614 O O . ILE A 380 ? 0.2767 0.1958 0.2151 0.0666 -0.0197 -0.0051 373 ILE A O 2615 C CB . ILE A 380 ? 0.2451 0.2300 0.1724 0.0780 -0.0037 -0.0142 373 ILE A CB 2616 C CG1 . ILE A 380 ? 0.2340 0.2335 0.1939 0.0824 -0.0187 0.0093 373 ILE A CG1 2617 C CG2 . ILE A 380 ? 0.2132 0.2263 0.1492 0.0316 0.0182 -0.0085 373 ILE A CG2 2618 C CD1 . ILE A 380 ? 0.2746 0.3102 0.1898 0.1176 -0.0274 0.0757 373 ILE A CD1 2619 N N . LEU A 381 ? 0.2486 0.2009 0.1854 0.0604 -0.0149 -0.0005 374 LEU A N 2620 C CA . LEU A 381 ? 0.2601 0.1985 0.1770 0.0587 -0.0040 -0.0034 374 LEU A CA 2621 C C . LEU A 381 ? 0.2569 0.2129 0.1796 0.0535 0.0020 -0.0129 374 LEU A C 2622 O O . LEU A 381 ? 0.2973 0.2074 0.1732 0.0522 0.0232 -0.0183 374 LEU A O 2623 C CB . LEU A 381 ? 0.2496 0.1845 0.1675 0.0597 -0.0092 0.0097 374 LEU A CB 2624 C CG . LEU A 381 ? 0.2742 0.1937 0.1623 0.0516 0.0020 0.0361 374 LEU A CG 2625 C CD1 . LEU A 381 ? 0.3072 0.1866 0.1239 0.0281 0.0243 0.0113 374 LEU A CD1 2626 C CD2 . LEU A 381 ? 0.2996 0.1818 0.1356 0.0837 -0.0147 0.0568 374 LEU A CD2 2627 N N . GLY A 382 ? 0.2606 0.2148 0.1803 0.0570 -0.0017 -0.0143 375 GLY A N 2628 C CA . GLY A 382 ? 0.2317 0.2073 0.1828 0.0474 0.0059 -0.0391 375 GLY A CA 2629 C C . GLY A 382 ? 0.2325 0.2110 0.1930 0.0424 -0.0011 -0.0326 375 GLY A C 2630 O O . GLY A 382 ? 0.2399 0.2006 0.1949 0.0283 -0.0021 -0.0445 375 GLY A O 2631 N N . GLY A 383 ? 0.2206 0.1964 0.1986 0.0474 -0.0002 -0.0363 376 GLY A N 2632 C CA . GLY A 383 ? 0.2267 0.2063 0.1790 0.0329 0.0096 -0.0390 376 GLY A CA 2633 C C . GLY A 383 ? 0.2173 0.2050 0.1975 0.0309 0.0111 -0.0267 376 GLY A C 2634 O O . GLY A 383 ? 0.2308 0.2323 0.1884 0.0193 0.0187 -0.0269 376 GLY A O 2635 N N . HIS A 384 ? 0.2343 0.2036 0.1859 0.0265 0.0113 -0.0216 377 HIS A N 2636 C CA . HIS A 384 ? 0.2163 0.1836 0.2098 0.0373 0.0052 -0.0187 377 HIS A CA 2637 C C . HIS A 384 ? 0.2336 0.2120 0.2273 0.0291 0.0108 -0.0139 377 HIS A C 2638 O O . HIS A 384 ? 0.2282 0.2116 0.2465 0.0504 0.0192 -0.0084 377 HIS A O 2639 C CB . HIS A 384 ? 0.1966 0.1952 0.2102 0.0339 0.0182 -0.0254 377 HIS A CB 2640 C CG . HIS A 384 ? 0.1939 0.1876 0.2351 0.0303 0.0143 -0.0331 377 HIS A CG 2641 N ND1 . HIS A 384 ? 0.1620 0.2146 0.2743 0.0381 -0.0045 -0.0400 377 HIS A ND1 2642 C CD2 . HIS A 384 ? 0.1250 0.2051 0.2719 0.0834 0.0215 -0.0065 377 HIS A CD2 2643 C CE1 . HIS A 384 ? 0.1776 0.2141 0.2327 0.0289 -0.0231 0.0126 377 HIS A CE1 2644 N NE2 . HIS A 384 ? 0.1785 0.2029 0.2115 0.0182 0.0151 -0.0085 377 HIS A NE2 2645 N N . ARG A 385 ? 0.2293 0.1902 0.2353 0.0218 0.0228 -0.0218 378 ARG A N 2646 C CA . ARG A 385 ? 0.2299 0.1912 0.2351 0.0240 0.0105 -0.0132 378 ARG A CA 2647 C C . ARG A 385 ? 0.2292 0.1970 0.2394 0.0258 0.0121 -0.0143 378 ARG A C 2648 O O . ARG A 385 ? 0.2166 0.1888 0.2479 0.0233 -0.0083 -0.0100 378 ARG A O 2649 C CB . ARG A 385 ? 0.2364 0.1941 0.2316 0.0309 0.0236 -0.0091 378 ARG A CB 2650 C CG . ARG A 385 ? 0.2268 0.1754 0.2500 0.0139 0.0020 -0.0044 378 ARG A CG 2651 C CD . ARG A 385 ? 0.2065 0.2405 0.2396 0.0338 0.0316 -0.0017 378 ARG A CD 2652 N NE . ARG A 385 ? 0.2313 0.2081 0.2529 0.0051 0.0128 0.0426 378 ARG A NE 2653 C CZ . ARG A 385 ? 0.1948 0.2217 0.2609 0.0067 0.0306 -0.0130 378 ARG A CZ 2654 N NH1 . ARG A 385 ? 0.1795 0.1807 0.2036 -0.0020 0.0529 -0.0046 378 ARG A NH1 2655 N NH2 . ARG A 385 ? 0.2324 0.1932 0.2477 0.0256 0.0263 -0.0102 378 ARG A NH2 2656 N N . ASP A 386 ? 0.2058 0.1998 0.2362 0.0311 -0.0007 -0.0227 379 ASP A N 2657 C CA . ASP A 386 ? 0.1973 0.1908 0.2325 0.0344 0.0111 -0.0272 379 ASP A CA 2658 C C . ASP A 386 ? 0.2049 0.1925 0.2323 0.0314 0.0138 -0.0245 379 ASP A C 2659 O O . ASP A 386 ? 0.2013 0.1818 0.2383 0.0417 0.0078 -0.0329 379 ASP A O 2660 C CB . ASP A 386 ? 0.1763 0.1635 0.2179 0.0305 0.0128 -0.0217 379 ASP A CB 2661 C CG . ASP A 386 ? 0.1824 0.1853 0.2230 0.0304 0.0110 -0.0199 379 ASP A CG 2662 O OD1 . ASP A 386 ? 0.2111 0.1516 0.2659 0.0074 -0.0231 -0.0421 379 ASP A OD1 2663 O OD2 . ASP A 386 ? 0.1635 0.1958 0.2272 0.0063 0.0109 -0.0341 379 ASP A OD2 2664 N N . SER A 387 ? 0.2093 0.1873 0.2335 0.0390 0.0121 -0.0160 380 SER A N 2665 C CA . SER A 387 ? 0.2089 0.2183 0.2530 0.0263 0.0139 -0.0215 380 SER A CA 2666 C C . SER A 387 ? 0.2240 0.2342 0.2557 0.0188 0.0161 -0.0295 380 SER A C 2667 O O . SER A 387 ? 0.2349 0.2630 0.2525 0.0040 0.0185 -0.0289 380 SER A O 2668 C CB . SER A 387 ? 0.2047 0.2041 0.2539 0.0170 0.0141 -0.0040 380 SER A CB 2669 O OG . SER A 387 ? 0.2254 0.2333 0.2779 0.0463 0.0090 -0.0332 380 SER A OG 2670 N N . TRP A 388 ? 0.2101 0.2194 0.2611 0.0283 0.0179 -0.0349 381 TRP A N 2671 C CA . TRP A 388 ? 0.2140 0.2258 0.2632 0.0279 0.0191 -0.0317 381 TRP A CA 2672 C C . TRP A 388 ? 0.2172 0.2218 0.2700 0.0236 0.0183 -0.0365 381 TRP A C 2673 O O . TRP A 388 ? 0.2271 0.2460 0.2839 0.0414 0.0264 -0.0403 381 TRP A O 2674 C CB . TRP A 388 ? 0.2155 0.2230 0.2613 0.0133 0.0153 -0.0231 381 TRP A CB 2675 C CG . TRP A 388 ? 0.2042 0.1981 0.2606 0.0152 0.0239 -0.0420 381 TRP A CG 2676 C CD1 . TRP A 388 ? 0.2416 0.2286 0.2565 0.0261 0.0356 -0.0560 381 TRP A CD1 2677 C CD2 . TRP A 388 ? 0.2162 0.2013 0.2645 -0.0064 0.0200 -0.0220 381 TRP A CD2 2678 N NE1 . TRP A 388 ? 0.2680 0.2331 0.2590 0.0349 0.0123 -0.0707 381 TRP A NE1 2679 C CE2 . TRP A 388 ? 0.2343 0.2259 0.2771 0.0069 0.0210 -0.0404 381 TRP A CE2 2680 C CE3 . TRP A 388 ? 0.2124 0.2345 0.2105 -0.0258 0.0072 -0.0022 381 TRP A CE3 2681 C CZ2 . TRP A 388 ? 0.2433 0.2199 0.2473 -0.0092 -0.0006 -0.0584 381 TRP A CZ2 2682 C CZ3 . TRP A 388 ? 0.2139 0.2181 0.1850 -0.0460 0.0039 -0.0194 381 TRP A CZ3 2683 C CH2 . TRP A 388 ? 0.2287 0.2240 0.2537 -0.0107 0.0371 -0.0480 381 TRP A CH2 2684 N N . VAL A 389 ? 0.2171 0.2088 0.3079 0.0284 0.0250 -0.0399 382 VAL A N 2685 C CA . VAL A 389 ? 0.2194 0.1882 0.2935 0.0213 0.0170 -0.0397 382 VAL A CA 2686 C C . VAL A 389 ? 0.2298 0.2001 0.3026 0.0269 0.0140 -0.0426 382 VAL A C 2687 O O . VAL A 389 ? 0.2161 0.2062 0.3116 0.0099 0.0038 -0.0351 382 VAL A O 2688 C CB . VAL A 389 ? 0.2106 0.1758 0.2861 0.0187 0.0198 -0.0400 382 VAL A CB 2689 C CG1 . VAL A 389 ? 0.1778 0.1589 0.2983 0.0124 0.0052 -0.0394 382 VAL A CG1 2690 C CG2 . VAL A 389 ? 0.1903 0.1743 0.3094 -0.0246 0.0306 -0.0413 382 VAL A CG2 2691 N N . PHE A 390 ? 0.2415 0.1950 0.2984 0.0201 -0.0057 -0.0401 383 PHE A N 2692 C CA . PHE A 390 ? 0.2394 0.1944 0.3008 0.0278 0.0059 -0.0415 383 PHE A CA 2693 C C . PHE A 390 ? 0.2423 0.2062 0.3034 0.0343 0.0096 -0.0429 383 PHE A C 2694 O O . PHE A 390 ? 0.2612 0.2282 0.2961 0.0167 0.0105 -0.0356 383 PHE A O 2695 C CB . PHE A 390 ? 0.2312 0.1736 0.2888 0.0437 0.0096 -0.0453 383 PHE A CB 2696 C CG . PHE A 390 ? 0.2646 0.1934 0.3365 0.0444 0.0085 -0.0440 383 PHE A CG 2697 C CD1 . PHE A 390 ? 0.2734 0.1680 0.3573 0.0521 0.0167 -0.0300 383 PHE A CD1 2698 C CD2 . PHE A 390 ? 0.3060 0.1632 0.3372 0.0836 0.0163 -0.0463 383 PHE A CD2 2699 C CE1 . PHE A 390 ? 0.2725 0.1717 0.3525 0.0671 0.0147 -0.0377 383 PHE A CE1 2700 C CE2 . PHE A 390 ? 0.3107 0.1612 0.3452 0.0543 -0.0108 -0.0271 383 PHE A CE2 2701 C CZ . PHE A 390 ? 0.2789 0.1724 0.3510 0.0774 0.0082 -0.0205 383 PHE A CZ 2702 N N . GLY A 391 ? 0.2379 0.1955 0.3129 0.0290 0.0016 -0.0381 384 GLY A N 2703 C CA . GLY A 391 ? 0.2195 0.1935 0.2990 0.0535 0.0082 -0.0406 384 GLY A CA 2704 C C . GLY A 391 ? 0.2476 0.1942 0.2939 0.0462 0.0129 -0.0274 384 GLY A C 2705 O O . GLY A 391 ? 0.2598 0.1893 0.2717 0.0437 0.0193 -0.0149 384 GLY A O 2706 N N . GLY A 392 ? 0.2309 0.1950 0.3028 0.0474 -0.0029 -0.0257 385 GLY A N 2707 C CA . GLY A 392 ? 0.2271 0.1896 0.2942 0.0408 0.0057 -0.0113 385 GLY A CA 2708 C C . GLY A 392 ? 0.2290 0.2188 0.2936 0.0397 0.0002 -0.0207 385 GLY A C 2709 O O . GLY A 392 ? 0.2230 0.2271 0.2843 0.0300 0.0027 -0.0145 385 GLY A O 2710 N N . ILE A 393 ? 0.2047 0.1925 0.3049 0.0456 0.0012 -0.0189 386 ILE A N 2711 C CA . ILE A 393 ? 0.2032 0.1860 0.3027 0.0547 0.0050 -0.0269 386 ILE A CA 2712 C C . ILE A 393 ? 0.2002 0.1974 0.2939 0.0514 0.0041 -0.0266 386 ILE A C 2713 O O . ILE A 393 ? 0.2150 0.1978 0.3052 0.0488 0.0039 -0.0381 386 ILE A O 2714 C CB . ILE A 393 ? 0.1955 0.1716 0.3208 0.0587 0.0092 -0.0351 386 ILE A CB 2715 C CG1 . ILE A 393 ? 0.1925 0.2153 0.3347 0.0554 0.0112 -0.0287 386 ILE A CG1 2716 C CG2 . ILE A 393 ? 0.2280 0.1632 0.3110 0.0549 0.0023 -0.0454 386 ILE A CG2 2717 C CD1 . ILE A 393 ? 0.1694 0.2503 0.3716 0.0652 0.0245 -0.0411 386 ILE A CD1 2718 N N . ASP A 394 ? 0.1885 0.1895 0.2760 0.0518 0.0033 -0.0300 387 ASP A N 2719 C CA . ASP A 394 ? 0.1948 0.1994 0.2676 0.0478 0.0000 -0.0215 387 ASP A CA 2720 C C . ASP A 394 ? 0.1865 0.1917 0.2505 0.0483 -0.0024 -0.0323 387 ASP A C 2721 O O . ASP A 394 ? 0.2070 0.2039 0.2649 0.0488 0.0134 -0.0357 387 ASP A O 2722 C CB . ASP A 394 ? 0.1836 0.2108 0.2607 0.0449 -0.0004 -0.0180 387 ASP A CB 2723 C CG . ASP A 394 ? 0.2405 0.2259 0.2793 0.0520 0.0180 -0.0070 387 ASP A CG 2724 O OD1 . ASP A 394 ? 0.2181 0.2348 0.2487 0.0717 0.0255 0.0036 387 ASP A OD1 2725 O OD2 . ASP A 394 ? 0.2494 0.2384 0.2528 0.0076 0.0436 -0.0372 387 ASP A OD2 2726 N N . PRO A 395 ? 0.1853 0.1907 0.2364 0.0436 -0.0008 -0.0359 388 PRO A N 2727 C CA . PRO A 395 ? 0.1976 0.1897 0.2443 0.0453 -0.0024 -0.0346 388 PRO A CA 2728 C C . PRO A 395 ? 0.2267 0.2021 0.2564 0.0421 -0.0013 -0.0335 388 PRO A C 2729 O O . PRO A 395 ? 0.2580 0.2124 0.2621 0.0430 0.0113 -0.0393 388 PRO A O 2730 C CB . PRO A 395 ? 0.1835 0.1829 0.2373 0.0368 -0.0093 -0.0311 388 PRO A CB 2731 C CG . PRO A 395 ? 0.1732 0.1959 0.2218 0.0390 -0.0052 -0.0446 388 PRO A CG 2732 C CD . PRO A 395 ? 0.1857 0.1890 0.2388 0.0396 -0.0043 -0.0489 388 PRO A CD 2733 N N . GLN A 396 ? 0.2340 0.2130 0.2688 0.0421 -0.0131 -0.0256 389 GLN A N 2734 C CA . GLN A 396 ? 0.2382 0.2136 0.2729 0.0445 -0.0106 -0.0166 389 GLN A CA 2735 C C . GLN A 396 ? 0.2550 0.2229 0.2777 0.0412 -0.0092 -0.0231 389 GLN A C 2736 O O . GLN A 396 ? 0.2666 0.2112 0.2712 0.0457 -0.0196 -0.0197 389 GLN A O 2737 C CB . GLN A 396 ? 0.2395 0.2098 0.2626 0.0391 -0.0065 -0.0345 389 GLN A CB 2738 C CG . GLN A 396 ? 0.2361 0.2129 0.2824 0.0552 -0.0217 -0.0090 389 GLN A CG 2739 C CD . GLN A 396 ? 0.2512 0.2334 0.2840 0.0449 -0.0031 -0.0136 389 GLN A CD 2740 O OE1 . GLN A 396 ? 0.2619 0.2239 0.3050 0.0675 -0.0161 -0.0202 389 GLN A OE1 2741 N NE2 . GLN A 396 ? 0.2277 0.2222 0.2765 0.0476 -0.0152 0.0027 389 GLN A NE2 2742 N N . SER A 397 ? 0.2542 0.2206 0.2938 0.0465 -0.0129 -0.0187 390 SER A N 2743 C CA . SER A 397 ? 0.2505 0.2256 0.2885 0.0523 -0.0026 -0.0158 390 SER A CA 2744 C C . SER A 397 ? 0.2413 0.2234 0.2739 0.0571 0.0034 -0.0144 390 SER A C 2745 O O . SER A 397 ? 0.2436 0.2250 0.2848 0.0522 0.0094 -0.0223 390 SER A O 2746 C CB . SER A 397 ? 0.2331 0.2307 0.2852 0.0522 0.0101 -0.0023 390 SER A CB 2747 O OG . SER A 397 ? 0.2344 0.2078 0.2980 0.0434 0.0288 -0.0125 390 SER A OG 2748 N N . GLY A 398 ? 0.2299 0.2092 0.2685 0.0523 0.0075 -0.0100 391 GLY A N 2749 C CA . GLY A 398 ? 0.2354 0.2129 0.2398 0.0479 0.0062 -0.0180 391 GLY A CA 2750 C C . GLY A 398 ? 0.2401 0.2168 0.2401 0.0499 -0.0017 -0.0171 391 GLY A C 2751 O O . GLY A 398 ? 0.2455 0.2209 0.2449 0.0434 -0.0049 -0.0160 391 GLY A O 2752 N N . ALA A 399 ? 0.2436 0.1974 0.2345 0.0525 -0.0027 -0.0144 392 ALA A N 2753 C CA . ALA A 399 ? 0.2518 0.2154 0.2560 0.0569 -0.0131 -0.0146 392 ALA A CA 2754 C C . ALA A 399 ? 0.2546 0.2127 0.2625 0.0645 -0.0155 -0.0118 392 ALA A C 2755 O O . ALA A 399 ? 0.2522 0.2215 0.2882 0.0758 -0.0163 -0.0350 392 ALA A O 2756 C CB . ALA A 399 ? 0.2527 0.2083 0.2504 0.0549 -0.0145 -0.0134 392 ALA A CB 2757 N N . ALA A 400 ? 0.2719 0.2129 0.2737 0.0735 -0.0182 -0.0162 393 ALA A N 2758 C CA . ALA A 400 ? 0.2713 0.2129 0.2614 0.0809 -0.0229 -0.0033 393 ALA A CA 2759 C C . ALA A 400 ? 0.2840 0.2249 0.2732 0.0801 -0.0114 -0.0017 393 ALA A C 2760 O O . ALA A 400 ? 0.2900 0.2522 0.2585 0.0714 -0.0220 -0.0014 393 ALA A O 2761 C CB . ALA A 400 ? 0.2693 0.2110 0.2769 0.0856 -0.0161 -0.0023 393 ALA A CB 2762 N N . VAL A 401 ? 0.2723 0.2184 0.2798 0.0664 -0.0094 -0.0081 394 VAL A N 2763 C CA . VAL A 401 ? 0.2784 0.2258 0.2650 0.0749 -0.0038 -0.0124 394 VAL A CA 2764 C C . VAL A 401 ? 0.2935 0.2250 0.2695 0.0743 -0.0059 -0.0005 394 VAL A C 2765 O O . VAL A 401 ? 0.2936 0.2153 0.2446 0.0814 -0.0257 -0.0021 394 VAL A O 2766 C CB . VAL A 401 ? 0.2782 0.2188 0.2808 0.0636 0.0034 -0.0234 394 VAL A CB 2767 C CG1 . VAL A 401 ? 0.2570 0.2148 0.2274 0.0717 0.0197 -0.0228 394 VAL A CG1 2768 C CG2 . VAL A 401 ? 0.2513 0.2295 0.2626 0.0733 -0.0410 -0.0302 394 VAL A CG2 2769 N N . VAL A 402 ? 0.2860 0.2311 0.2633 0.0681 -0.0102 0.0122 395 VAL A N 2770 C CA . VAL A 402 ? 0.3009 0.2328 0.2547 0.0693 0.0114 0.0204 395 VAL A CA 2771 C C . VAL A 402 ? 0.3110 0.2403 0.2617 0.0671 0.0162 0.0157 395 VAL A C 2772 O O . VAL A 402 ? 0.3122 0.2470 0.2493 0.0520 0.0058 0.0083 395 VAL A O 2773 C CB . VAL A 402 ? 0.2903 0.2435 0.2620 0.0736 0.0091 0.0297 395 VAL A CB 2774 C CG1 . VAL A 402 ? 0.2863 0.2268 0.2001 0.0782 0.0452 0.0069 395 VAL A CG1 2775 C CG2 . VAL A 402 ? 0.3149 0.2247 0.2197 0.0448 0.0199 0.0324 395 VAL A CG2 2776 N N . HIS A 403 ? 0.2964 0.2146 0.2606 0.0673 0.0070 0.0144 396 HIS A N 2777 C CA . HIS A 403 ? 0.2993 0.2227 0.2465 0.0795 0.0091 0.0147 396 HIS A CA 2778 C C . HIS A 403 ? 0.3132 0.2383 0.2545 0.0777 0.0062 0.0063 396 HIS A C 2779 O O . HIS A 403 ? 0.3278 0.2400 0.2649 0.0681 0.0088 0.0202 396 HIS A O 2780 C CB . HIS A 403 ? 0.2840 0.2149 0.2452 0.0672 0.0093 0.0088 396 HIS A CB 2781 C CG . HIS A 403 ? 0.3046 0.2239 0.2618 0.0684 0.0371 0.0034 396 HIS A CG 2782 N ND1 . HIS A 403 ? 0.2952 0.2078 0.1793 0.0755 0.0589 -0.0209 396 HIS A ND1 2783 C CD2 . HIS A 403 ? 0.3025 0.2259 0.3050 0.0694 0.0523 0.0271 396 HIS A CD2 2784 C CE1 . HIS A 403 ? 0.2903 0.2202 0.2666 0.0589 0.0465 0.0113 396 HIS A CE1 2785 N NE2 . HIS A 403 ? 0.3016 0.2415 0.3080 0.0677 0.0354 0.0024 396 HIS A NE2 2786 N N . GLU A 404 ? 0.3099 0.2492 0.2477 0.1020 -0.0093 0.0107 397 GLU A N 2787 C CA . GLU A 404 ? 0.3260 0.2572 0.2533 0.0975 -0.0143 0.0087 397 GLU A CA 2788 C C . GLU A 404 ? 0.3368 0.2544 0.2434 0.0924 -0.0181 0.0179 397 GLU A C 2789 O O . GLU A 404 ? 0.3492 0.2627 0.2436 0.0803 -0.0353 0.0146 397 GLU A O 2790 C CB . GLU A 404 ? 0.3203 0.2740 0.2627 0.1027 -0.0282 0.0111 397 GLU A CB 2791 C CG . GLU A 404 ? 0.3426 0.2509 0.2304 0.0821 -0.0220 0.0090 397 GLU A CG 2792 C CD . GLU A 404 ? 0.3924 0.3111 0.2507 0.0729 -0.0391 0.0321 397 GLU A CD 2793 O OE1 . GLU A 404 ? 0.3895 0.2965 0.2311 0.0790 -0.0017 -0.0108 397 GLU A OE1 2794 O OE2 . GLU A 404 ? 0.4541 0.3237 0.2403 0.0413 -0.0590 0.0493 397 GLU A OE2 2795 N N . ILE A 405 ? 0.3208 0.2405 0.2298 0.0987 -0.0345 0.0226 398 ILE A N 2796 C CA . ILE A 405 ? 0.3200 0.2372 0.2203 0.0930 -0.0097 0.0359 398 ILE A CA 2797 C C . ILE A 405 ? 0.3348 0.2409 0.2263 0.0890 -0.0097 0.0355 398 ILE A C 2798 O O . ILE A 405 ? 0.3357 0.2215 0.2014 0.0874 -0.0226 0.0359 398 ILE A O 2799 C CB . ILE A 405 ? 0.3152 0.2335 0.2208 0.0961 -0.0068 0.0404 398 ILE A CB 2800 C CG1 . ILE A 405 ? 0.3050 0.2357 0.1842 0.0732 -0.0004 0.0488 398 ILE A CG1 2801 C CG2 . ILE A 405 ? 0.2756 0.2278 0.1180 0.0963 -0.0134 0.0373 398 ILE A CG2 2802 C CD1 . ILE A 405 ? 0.2644 0.1973 0.1311 0.0941 -0.0010 0.0589 398 ILE A CD1 2803 N N . VAL A 406 ? 0.3323 0.2518 0.2241 0.0863 -0.0138 0.0433 399 VAL A N 2804 C CA . VAL A 406 ? 0.3521 0.2685 0.2305 0.0870 0.0007 0.0330 399 VAL A CA 2805 C C . VAL A 406 ? 0.3688 0.2659 0.2478 0.0941 0.0047 0.0355 399 VAL A C 2806 O O . VAL A 406 ? 0.3824 0.2642 0.2629 0.0930 0.0161 0.0241 399 VAL A O 2807 C CB . VAL A 406 ? 0.3309 0.2595 0.2276 0.0805 -0.0111 0.0392 399 VAL A CB 2808 C CG1 . VAL A 406 ? 0.3494 0.2746 0.1557 0.0838 -0.0013 0.0231 399 VAL A CG1 2809 C CG2 . VAL A 406 ? 0.3182 0.2545 0.2142 0.0697 0.0146 0.0400 399 VAL A CG2 2810 N N . ARG A 407 ? 0.3838 0.2741 0.2591 0.1051 0.0066 0.0293 400 ARG A N 2811 C CA . ARG A 407 ? 0.4080 0.2811 0.2628 0.1144 0.0028 0.0376 400 ARG A CA 2812 C C . ARG A 407 ? 0.4305 0.3070 0.2776 0.1149 0.0086 0.0310 400 ARG A C 2813 O O . ARG A 407 ? 0.4490 0.3237 0.2871 0.1144 -0.0005 0.0367 400 ARG A O 2814 C CB . ARG A 407 ? 0.4126 0.2746 0.2665 0.1147 0.0005 0.0472 400 ARG A CB 2815 C CG . ARG A 407 ? 0.4228 0.2695 0.2558 0.1373 -0.0054 0.0544 400 ARG A CG 2816 C CD . ARG A 407 ? 0.4175 0.3164 0.2450 0.1396 -0.0020 0.0840 400 ARG A CD 2817 N NE . ARG A 407 ? 0.4398 0.3427 0.2330 0.1297 -0.0005 0.0962 400 ARG A NE 2818 C CZ . ARG A 407 ? 0.4717 0.3831 0.2547 0.0883 -0.0032 0.0704 400 ARG A CZ 2819 N NH1 . ARG A 407 ? 0.4442 0.3799 0.2201 0.0761 0.0063 0.0860 400 ARG A NH1 2820 N NH2 . ARG A 407 ? 0.4864 0.3772 0.2277 0.1032 -0.0164 0.0681 400 ARG A NH2 2821 N N . SER A 408 ? 0.4310 0.3135 0.2807 0.1154 0.0057 0.0242 401 SER A N 2822 C CA . SER A 408 ? 0.4454 0.3325 0.2788 0.1147 0.0005 0.0261 401 SER A CA 2823 C C . SER A 408 ? 0.4458 0.3296 0.2736 0.1162 0.0006 0.0286 401 SER A C 2824 O O . SER A 408 ? 0.4567 0.3293 0.2737 0.1182 -0.0032 0.0418 401 SER A O 2825 C CB . SER A 408 ? 0.4474 0.3515 0.2807 0.1041 -0.0034 0.0179 401 SER A CB 2826 O OG . SER A 408 ? 0.4733 0.3724 0.2881 0.1162 0.0047 0.0217 401 SER A OG 2827 N N . PHE A 409 ? 0.4335 0.3098 0.2473 0.1211 0.0009 0.0309 402 PHE A N 2828 C CA . PHE A 409 ? 0.4467 0.3203 0.2501 0.1274 0.0078 0.0313 402 PHE A CA 2829 C C . PHE A 409 ? 0.4570 0.3294 0.2600 0.1335 0.0162 0.0270 402 PHE A C 2830 O O . PHE A 409 ? 0.4591 0.3299 0.2410 0.1407 0.0179 0.0054 402 PHE A O 2831 C CB . PHE A 409 ? 0.4257 0.3081 0.2312 0.1232 0.0076 0.0330 402 PHE A CB 2832 C CG . PHE A 409 ? 0.4147 0.2957 0.2386 0.1254 -0.0058 0.0239 402 PHE A CG 2833 C CD1 . PHE A 409 ? 0.3877 0.2944 0.2430 0.1080 -0.0116 0.0278 402 PHE A CD1 2834 C CD2 . PHE A 409 ? 0.3579 0.2821 0.2212 0.1103 -0.0124 0.0286 402 PHE A CD2 2835 C CE1 . PHE A 409 ? 0.3948 0.2841 0.2494 0.1175 0.0084 0.0261 402 PHE A CE1 2836 C CE2 . PHE A 409 ? 0.3114 0.2711 0.2196 0.1225 -0.0040 -0.0001 402 PHE A CE2 2837 C CZ . PHE A 409 ? 0.3427 0.2846 0.2528 0.1060 -0.0172 0.0146 402 PHE A CZ 2838 N N . GLY A 410 ? 0.4710 0.3213 0.2615 0.1425 0.0186 0.0233 403 GLY A N 2839 C CA . GLY A 410 ? 0.4954 0.3236 0.2694 0.1465 0.0221 0.0412 403 GLY A CA 2840 C C . GLY A 410 ? 0.5155 0.3523 0.2791 0.1409 0.0238 0.0370 403 GLY A C 2841 O O . GLY A 410 ? 0.5311 0.3646 0.2779 0.1316 0.0259 0.0347 403 GLY A O 2842 N N . THR A 411 ? 0.5229 0.3451 0.2801 0.1569 0.0208 0.0485 404 THR A N 2843 C CA . THR A 411 ? 0.5317 0.3635 0.2861 0.1570 0.0223 0.0460 404 THR A CA 2844 C C . THR A 411 ? 0.5418 0.3704 0.2909 0.1603 0.0187 0.0535 404 THR A C 2845 O O . THR A 411 ? 0.5548 0.3660 0.2838 0.1626 0.0104 0.0602 404 THR A O 2846 C CB . THR A 411 ? 0.5284 0.3507 0.2886 0.1624 0.0185 0.0483 404 THR A CB 2847 O OG1 A THR A 411 ? 0.5162 0.3443 0.2928 0.1525 0.0210 0.0502 404 THR A OG1 2848 O OG1 B THR A 411 ? 0.5306 0.3523 0.2831 0.1663 0.0481 0.0382 404 THR A OG1 2849 C CG2 A THR A 411 ? 0.5213 0.3717 0.2695 0.1483 0.0348 0.0548 404 THR A CG2 2850 C CG2 B THR A 411 ? 0.5223 0.3474 0.2920 0.1565 0.0258 0.0459 404 THR A CG2 2851 N N . LEU A 412 ? 0.5455 0.3677 0.2931 0.1644 0.0148 0.0647 405 LEU A N 2852 C CA . LEU A 412 ? 0.5635 0.3822 0.3000 0.1587 0.0184 0.0667 405 LEU A CA 2853 C C . LEU A 412 ? 0.5774 0.3942 0.3072 0.1549 0.0290 0.0702 405 LEU A C 2854 O O . LEU A 412 ? 0.5744 0.3883 0.2845 0.1501 0.0284 0.0730 405 LEU A O 2855 C CB . LEU A 412 ? 0.5591 0.3801 0.2939 0.1531 0.0131 0.0708 405 LEU A CB 2856 C CG A LEU A 412 ? 0.5581 0.3774 0.2788 0.1488 -0.0020 0.0770 405 LEU A CG 2857 C CG B LEU A 412 ? 0.5522 0.3767 0.2988 0.1534 0.0119 0.0651 405 LEU A CG 2858 C CD1 A LEU A 412 ? 0.5503 0.3754 0.2533 0.1516 -0.0153 0.0838 405 LEU A CD1 2859 C CD1 B LEU A 412 ? 0.5255 0.3623 0.2746 0.1412 0.0014 0.0724 405 LEU A CD1 2860 C CD2 A LEU A 412 ? 0.5511 0.3695 0.2655 0.1447 -0.0117 0.0886 405 LEU A CD2 2861 C CD2 B LEU A 412 ? 0.5377 0.3650 0.2935 0.1644 0.0060 0.0560 405 LEU A CD2 2862 N N . LYS A 413 ? 0.5871 0.3973 0.3027 0.1553 0.0324 0.0761 406 LYS A N 2863 C CA . LYS A 413 ? 0.6016 0.4030 0.3268 0.1593 0.0473 0.0828 406 LYS A CA 2864 C C . LYS A 413 ? 0.6150 0.4165 0.3189 0.1644 0.0504 0.0878 406 LYS A C 2865 O O . LYS A 413 ? 0.5998 0.3932 0.3046 0.1708 0.0604 0.0992 406 LYS A O 2866 C CB . LYS A 413 ? 0.6033 0.3974 0.3395 0.1579 0.0444 0.0773 406 LYS A CB 2867 C CG . LYS A 413 ? 0.6204 0.4499 0.4360 0.1489 0.0485 0.0627 406 LYS A CG 2868 C CD . LYS A 413 ? 0.6447 0.4953 0.5114 0.1343 0.0413 0.0344 406 LYS A CD 2869 C CE . LYS A 413 ? 0.6463 0.5220 0.5185 0.1317 0.0345 0.0248 406 LYS A CE 2870 N NZ . LYS A 413 ? 0.6380 0.5772 0.6035 0.1044 0.0521 0.0376 406 LYS A NZ 2871 N N . LYS A 414 ? 0.6250 0.4255 0.3209 0.1765 0.0514 0.0874 407 LYS A N 2872 C CA . LYS A 414 ? 0.6544 0.4525 0.3534 0.1744 0.0572 0.0865 407 LYS A CA 2873 C C . LYS A 414 ? 0.6770 0.4632 0.3530 0.1817 0.0542 0.0871 407 LYS A C 2874 O O . LYS A 414 ? 0.6871 0.4854 0.3798 0.1795 0.0527 0.0800 407 LYS A O 2875 C CB . LYS A 414 ? 0.6537 0.4550 0.3408 0.1740 0.0659 0.0834 407 LYS A CB 2876 C CG . LYS A 414 ? 0.6586 0.4782 0.4202 0.1587 0.0637 0.0650 407 LYS A CG 2877 C CD . LYS A 414 ? 0.7004 0.4890 0.4286 0.1504 0.0782 0.0469 407 LYS A CD 2878 C CE . LYS A 414 ? 0.7216 0.5157 0.4322 0.1287 0.0799 0.0526 407 LYS A CE 2879 N NZ . LYS A 414 ? 0.7215 0.5196 0.4239 0.1447 0.0697 0.0628 407 LYS A NZ 2880 N N . GLU A 415 ? 0.6896 0.4745 0.3618 0.1882 0.0507 0.0877 408 GLU A N 2881 C CA . GLU A 415 ? 0.7102 0.4823 0.3819 0.1959 0.0427 0.0776 408 GLU A CA 2882 C C . GLU A 415 ? 0.6967 0.4851 0.3573 0.1915 0.0455 0.0759 408 GLU A C 2883 O O . GLU A 415 ? 0.7074 0.4941 0.3633 0.1851 0.0482 0.0618 408 GLU A O 2884 C CB . GLU A 415 ? 0.7162 0.4919 0.3934 0.1961 0.0361 0.0850 408 GLU A CB 2885 C CG . GLU A 415 ? 0.7710 0.5400 0.5019 0.2129 0.0217 0.0632 408 GLU A CG 2886 C CD . GLU A 415 ? 0.8149 0.6382 0.6515 0.2082 -0.0036 0.0609 408 GLU A CD 2887 O OE1 . GLU A 415 ? 0.8491 0.6483 0.7283 0.2055 -0.0338 0.0891 408 GLU A OE1 2888 O OE2 . GLU A 415 ? 0.8579 0.6438 0.6927 0.2097 -0.0307 0.0518 408 GLU A OE2 2889 N N . GLY A 416 ? 0.6787 0.4594 0.3354 0.1919 0.0455 0.0775 409 GLY A N 2890 C CA . GLY A 416 ? 0.6491 0.4463 0.2956 0.1889 0.0465 0.0765 409 GLY A CA 2891 C C . GLY A 416 ? 0.6266 0.4349 0.2862 0.1874 0.0380 0.0648 409 GLY A C 2892 O O . GLY A 416 ? 0.6222 0.4312 0.2757 0.1904 0.0579 0.0626 409 GLY A O 2893 N N . TRP A 417 ? 0.6004 0.4175 0.2487 0.1798 0.0261 0.0642 410 TRP A N 2894 C CA . TRP A 417 ? 0.5706 0.4159 0.2448 0.1714 0.0153 0.0589 410 TRP A CA 2895 C C . TRP A 417 ? 0.5551 0.3981 0.2371 0.1681 0.0156 0.0644 410 TRP A C 2896 O O . TRP A 417 ? 0.5648 0.4141 0.2245 0.1647 0.0128 0.0722 410 TRP A O 2897 C CB . TRP A 417 ? 0.5747 0.4123 0.2766 0.1715 0.0047 0.0592 410 TRP A CB 2898 C CG . TRP A 417 ? 0.5462 0.4239 0.2886 0.1680 -0.0181 0.0731 410 TRP A CG 2899 C CD1 . TRP A 417 ? 0.5125 0.4034 0.3303 0.1736 -0.0298 0.0774 410 TRP A CD1 2900 C CD2 . TRP A 417 ? 0.5213 0.3956 0.3040 0.1892 0.0050 0.0288 410 TRP A CD2 2901 N NE1 . TRP A 417 ? 0.5148 0.4350 0.2891 0.1510 -0.0719 0.0746 410 TRP A NE1 2902 C CE2 . TRP A 417 ? 0.5104 0.3953 0.3081 0.1850 -0.0046 0.0395 410 TRP A CE2 2903 C CE3 . TRP A 417 ? 0.4832 0.3850 0.3047 0.2003 -0.0198 0.0527 410 TRP A CE3 2904 C CZ2 . TRP A 417 ? 0.4244 0.3679 0.2717 0.2166 -0.0276 0.0279 410 TRP A CZ2 2905 C CZ3 . TRP A 417 ? 0.4456 0.3662 0.2805 0.2246 -0.0144 0.0431 410 TRP A CZ3 2906 C CH2 . TRP A 417 ? 0.4250 0.3712 0.3017 0.2135 0.0046 0.0051 410 TRP A CH2 2907 N N . ARG A 418 ? 0.5167 0.3679 0.2211 0.1708 0.0167 0.0466 411 ARG A N 2908 C CA . ARG A 418 ? 0.4893 0.3595 0.2180 0.1587 0.0152 0.0458 411 ARG A CA 2909 C C . ARG A 418 ? 0.4649 0.3395 0.1954 0.1568 0.0104 0.0409 411 ARG A C 2910 O O . ARG A 418 ? 0.4760 0.3343 0.1997 0.1561 0.0131 0.0407 411 ARG A O 2911 C CB . ARG A 418 ? 0.4888 0.3663 0.2319 0.1566 0.0230 0.0409 411 ARG A CB 2912 C CG . ARG A 418 ? 0.4849 0.3876 0.2597 0.1469 0.0336 0.0313 411 ARG A CG 2913 C CD . ARG A 418 ? 0.4678 0.3809 0.2514 0.1465 0.0304 0.0302 411 ARG A CD 2914 N NE . ARG A 418 ? 0.4339 0.3911 0.1897 0.1389 0.0914 0.0488 411 ARG A NE 2915 C CZ . ARG A 418 ? 0.4584 0.3761 0.2008 0.0976 0.0797 0.0531 411 ARG A CZ 2916 N NH1 . ARG A 418 ? 0.4430 0.3548 0.1016 0.1345 0.1116 -0.0143 411 ARG A NH1 2917 N NH2 . ARG A 418 ? 0.4481 0.3754 0.1936 0.0784 0.0990 0.1069 411 ARG A NH2 2918 N N . PRO A 419 ? 0.4354 0.3163 0.1735 0.1506 0.0065 0.0360 412 PRO A N 2919 C CA . PRO A 419 ? 0.4346 0.2987 0.1602 0.1445 -0.0008 0.0272 412 PRO A CA 2920 C C . PRO A 419 ? 0.4288 0.2979 0.1608 0.1367 0.0005 0.0186 412 PRO A C 2921 O O . PRO A 419 ? 0.4212 0.2869 0.1568 0.1306 -0.0061 0.0195 412 PRO A O 2922 C CB . PRO A 419 ? 0.4329 0.2979 0.1522 0.1409 0.0035 0.0307 412 PRO A CB 2923 C CG . PRO A 419 ? 0.4225 0.2890 0.1613 0.1476 -0.0113 0.0400 412 PRO A CG 2924 C CD . PRO A 419 ? 0.4295 0.3123 0.1595 0.1450 0.0117 0.0333 412 PRO A CD 2925 N N . ARG A 420 ? 0.4205 0.2824 0.1623 0.1332 -0.0041 0.0188 413 ARG A N 2926 C CA . ARG A 420 ? 0.4018 0.2770 0.1634 0.1414 -0.0103 0.0053 413 ARG A CA 2927 C C . ARG A 420 ? 0.3999 0.2854 0.1636 0.1258 -0.0111 0.0084 413 ARG A C 2928 O O . ARG A 420 ? 0.4095 0.2903 0.1724 0.1285 -0.0229 0.0078 413 ARG A O 2929 C CB . ARG A 420 ? 0.3867 0.2649 0.1616 0.1437 -0.0093 -0.0045 413 ARG A CB 2930 C CG . ARG A 420 ? 0.4236 0.2601 0.2014 0.1481 -0.0023 -0.0038 413 ARG A CG 2931 C CD . ARG A 420 ? 0.4442 0.2496 0.1909 0.1540 -0.0257 0.0090 413 ARG A CD 2932 N NE . ARG A 420 ? 0.4647 0.3009 0.1666 0.1425 -0.0568 -0.0633 413 ARG A NE 2933 C CZ . ARG A 420 ? 0.5038 0.3405 0.1658 0.1661 -0.0373 -0.0487 413 ARG A CZ 2934 N NH1 . ARG A 420 ? 0.4649 0.3081 0.1331 0.1507 -0.1107 -0.1001 413 ARG A NH1 2935 N NH2 . ARG A 420 ? 0.5180 0.3921 0.1480 0.1802 -0.0649 -0.0543 413 ARG A NH2 2936 N N . ARG A 421 ? 0.3863 0.2750 0.1393 0.1182 -0.0098 -0.0001 414 ARG A N 2937 C CA . ARG A 421 ? 0.3719 0.2582 0.1554 0.1084 -0.0123 0.0199 414 ARG A CA 2938 C C . ARG A 421 ? 0.3599 0.2578 0.1569 0.1021 -0.0082 0.0164 414 ARG A C 2939 O O . ARG A 421 ? 0.3546 0.2449 0.1871 0.1053 0.0019 0.0250 414 ARG A O 2940 C CB . ARG A 421 ? 0.3474 0.2590 0.1236 0.1061 -0.0097 0.0086 414 ARG A CB 2941 C CG . ARG A 421 ? 0.3668 0.2441 0.1385 0.1013 -0.0133 0.0043 414 ARG A CG 2942 C CD . ARG A 421 ? 0.3271 0.2762 0.1527 0.0771 -0.0061 -0.0105 414 ARG A CD 2943 N NE . ARG A 421 ? 0.3733 0.2770 0.2017 0.1004 -0.0282 -0.0254 414 ARG A NE 2944 C CZ . ARG A 421 ? 0.3533 0.2429 0.2421 0.0873 -0.0434 -0.0280 414 ARG A CZ 2945 N NH1 . ARG A 421 ? 0.3707 0.2410 0.2031 0.1112 -0.0317 -0.0301 414 ARG A NH1 2946 N NH2 . ARG A 421 ? 0.3604 0.2401 0.1702 0.1324 -0.0290 -0.0485 414 ARG A NH2 2947 N N . THR A 422 ? 0.3419 0.2468 0.1754 0.0946 0.0047 0.0272 415 THR A N 2948 C CA . THR A 422 ? 0.3238 0.2496 0.1547 0.0939 0.0140 0.0081 415 THR A CA 2949 C C . THR A 422 ? 0.3151 0.2485 0.1691 0.0963 0.0115 0.0190 415 THR A C 2950 O O . THR A 422 ? 0.3042 0.2576 0.1680 0.0938 0.0236 0.0212 415 THR A O 2951 C CB . THR A 422 ? 0.3160 0.2492 0.1516 0.0974 0.0124 0.0108 415 THR A CB 2952 O OG1 . THR A 422 ? 0.3153 0.2409 0.1690 0.0741 0.0233 0.0099 415 THR A OG1 2953 C CG2 . THR A 422 ? 0.3171 0.2176 0.0915 0.0943 -0.0048 0.0298 415 THR A CG2 2954 N N . ILE A 423 ? 0.2999 0.2308 0.1477 0.1055 0.0064 0.0144 416 ILE A N 2955 C CA . ILE A 423 ? 0.2924 0.2395 0.1721 0.1005 0.0070 0.0226 416 ILE A CA 2956 C C . ILE A 423 ? 0.2917 0.2329 0.1711 0.0960 0.0060 0.0217 416 ILE A C 2957 O O . ILE A 423 ? 0.2933 0.2291 0.1774 0.1052 -0.0062 0.0321 416 ILE A O 2958 C CB . ILE A 423 ? 0.2881 0.2515 0.1739 0.1042 0.0072 0.0179 416 ILE A CB 2959 C CG1 . ILE A 423 ? 0.2878 0.2363 0.1728 0.1047 -0.0055 0.0254 416 ILE A CG1 2960 C CG2 . ILE A 423 ? 0.3017 0.2168 0.1638 0.1010 0.0271 -0.0125 416 ILE A CG2 2961 C CD1 . ILE A 423 ? 0.2817 0.2208 0.1903 0.1043 -0.0536 0.0146 416 ILE A CD1 2962 N N . LEU A 424 ? 0.2890 0.2253 0.1730 0.0921 -0.0033 0.0345 417 LEU A N 2963 C CA . LEU A 424 ? 0.2837 0.2048 0.1848 0.0787 0.0032 0.0221 417 LEU A CA 2964 C C . LEU A 424 ? 0.2795 0.2083 0.1777 0.0681 0.0069 0.0202 417 LEU A C 2965 O O . LEU A 424 ? 0.3005 0.1828 0.1835 0.0498 0.0024 -0.0010 417 LEU A O 2966 C CB . LEU A 424 ? 0.2706 0.2212 0.1773 0.0757 0.0034 0.0282 417 LEU A CB 2967 C CG . LEU A 424 ? 0.2723 0.2123 0.2058 0.0774 0.0149 0.0523 417 LEU A CG 2968 C CD1 . LEU A 424 ? 0.2270 0.2232 0.1632 0.0372 -0.0367 0.0507 417 LEU A CD1 2969 C CD2 . LEU A 424 ? 0.2290 0.2369 0.1342 0.0791 0.0080 0.0682 417 LEU A CD2 2970 N N . PHE A 425 ? 0.2754 0.1860 0.1688 0.0654 0.0106 0.0221 418 PHE A N 2971 C CA . PHE A 425 ? 0.2607 0.2078 0.1744 0.0683 0.0144 0.0292 418 PHE A CA 2972 C C . PHE A 425 ? 0.2661 0.2270 0.1933 0.0655 0.0168 0.0205 418 PHE A C 2973 O O . PHE A 425 ? 0.2650 0.2295 0.2117 0.0570 0.0127 0.0162 418 PHE A O 2974 C CB . PHE A 425 ? 0.2654 0.2175 0.1788 0.0723 0.0062 0.0282 418 PHE A CB 2975 C CG . PHE A 425 ? 0.2896 0.2424 0.1967 0.0642 -0.0099 0.0411 418 PHE A CG 2976 C CD1 . PHE A 425 ? 0.2579 0.2435 0.2026 0.0634 -0.0161 0.0605 418 PHE A CD1 2977 C CD2 . PHE A 425 ? 0.2871 0.2325 0.2028 0.0448 0.0004 0.0551 418 PHE A CD2 2978 C CE1 . PHE A 425 ? 0.2801 0.2441 0.2019 0.0724 -0.0049 0.0305 418 PHE A CE1 2979 C CE2 . PHE A 425 ? 0.3314 0.2411 0.1923 0.0314 0.0114 0.0643 418 PHE A CE2 2980 C CZ . PHE A 425 ? 0.3076 0.2343 0.1798 0.0464 -0.0029 0.0524 418 PHE A CZ 2981 N N . ALA A 426 ? 0.2618 0.2355 0.1920 0.0744 0.0096 0.0197 419 ALA A N 2982 C CA . ALA A 426 ? 0.2673 0.2167 0.1942 0.0655 0.0193 0.0130 419 ALA A CA 2983 C C . ALA A 426 ? 0.2617 0.2111 0.1956 0.0504 0.0167 0.0070 419 ALA A C 2984 O O . ALA A 426 ? 0.2555 0.2092 0.1856 0.0348 0.0101 -0.0117 419 ALA A O 2985 C CB . ALA A 426 ? 0.2540 0.2115 0.1703 0.0748 0.0224 0.0271 419 ALA A CB 2986 N N . SER A 427 ? 0.2607 0.2038 0.2005 0.0348 0.0067 0.0079 420 SER A N 2987 C CA . SER A 427 ? 0.2541 0.1905 0.1971 0.0319 0.0168 0.0024 420 SER A CA 2988 C C . SER A 427 ? 0.2463 0.2049 0.2146 0.0262 0.0201 0.0020 420 SER A C 2989 O O . SER A 427 ? 0.2499 0.2236 0.1918 0.0130 0.0177 -0.0054 420 SER A O 2990 C CB . SER A 427 ? 0.2480 0.1847 0.2042 0.0374 0.0240 0.0081 420 SER A CB 2991 O OG . SER A 427 ? 0.2880 0.1823 0.1841 0.0274 0.0086 -0.0014 420 SER A OG 2992 N N . TRP A 428 ? 0.2519 0.1858 0.2093 0.0196 0.0176 0.0015 421 TRP A N 2993 C CA . TRP A 428 ? 0.2420 0.1704 0.2164 0.0148 0.0089 -0.0153 421 TRP A CA 2994 C C . TRP A 428 ? 0.2406 0.1934 0.2315 0.0174 0.0131 -0.0172 421 TRP A C 2995 O O . TRP A 428 ? 0.2188 0.1912 0.2316 0.0247 0.0146 -0.0274 421 TRP A O 2996 C CB . TRP A 428 ? 0.2362 0.1596 0.2077 0.0061 0.0184 -0.0073 421 TRP A CB 2997 C CG . TRP A 428 ? 0.2195 0.1857 0.2044 0.0207 0.0173 -0.0042 421 TRP A CG 2998 C CD1 . TRP A 428 ? 0.2256 0.1943 0.1759 0.0247 0.0334 -0.0075 421 TRP A CD1 2999 C CD2 . TRP A 428 ? 0.2142 0.2064 0.1870 0.0098 0.0224 -0.0019 421 TRP A CD2 3000 N NE1 . TRP A 428 ? 0.2243 0.2001 0.1919 0.0491 0.0433 0.0029 421 TRP A NE1 3001 C CE2 . TRP A 428 ? 0.2110 0.2122 0.1643 0.0160 0.0132 0.0074 421 TRP A CE2 3002 C CE3 . TRP A 428 ? 0.2158 0.1946 0.1901 0.0587 0.0269 0.0399 421 TRP A CE3 3003 C CZ2 . TRP A 428 ? 0.1969 0.1806 0.1868 0.0358 0.0239 0.0302 421 TRP A CZ2 3004 C CZ3 . TRP A 428 ? 0.2299 0.1859 0.1950 0.0267 0.0273 0.0085 421 TRP A CZ3 3005 C CH2 . TRP A 428 ? 0.2337 0.1824 0.1857 0.0180 -0.0363 0.0333 421 TRP A CH2 3006 N N . ASP A 429 ? 0.2269 0.1844 0.2255 0.0165 0.0032 -0.0149 422 ASP A N 3007 C CA . ASP A 429 ? 0.2146 0.2000 0.2284 0.0086 0.0186 -0.0150 422 ASP A CA 3008 C C . ASP A 429 ? 0.2099 0.2078 0.2334 0.0117 0.0153 -0.0158 422 ASP A C 3009 O O . ASP A 429 ? 0.2161 0.2001 0.2234 0.0082 0.0290 -0.0149 422 ASP A O 3010 C CB . ASP A 429 ? 0.2134 0.2048 0.2477 -0.0044 0.0139 -0.0190 422 ASP A CB 3011 C CG . ASP A 429 ? 0.2271 0.2158 0.2641 0.0085 0.0296 -0.0161 422 ASP A CG 3012 O OD1 . ASP A 429 ? 0.2543 0.2343 0.2608 0.0216 0.0171 -0.0097 422 ASP A OD1 3013 O OD2 . ASP A 429 ? 0.2146 0.2153 0.2451 0.0059 -0.0047 -0.0239 422 ASP A OD2 3014 N N . ALA A 430 ? 0.2019 0.2109 0.2239 0.0209 0.0197 -0.0133 423 ALA A N 3015 C CA . ALA A 430 ? 0.2073 0.2070 0.2349 0.0161 0.0042 -0.0098 423 ALA A CA 3016 C C . ALA A 430 ? 0.1956 0.2097 0.2269 0.0164 0.0120 -0.0192 423 ALA A C 3017 O O . ALA A 430 ? 0.2105 0.1940 0.2397 0.0107 0.0150 -0.0213 423 ALA A O 3018 C CB . ALA A 430 ? 0.1739 0.2108 0.2154 0.0150 -0.0034 -0.0096 423 ALA A CB 3019 N N . ALA A 431 ? 0.2055 0.2101 0.2399 0.0292 0.0164 -0.0292 424 ALA A N 3020 C CA . ALA A 431 ? 0.2045 0.1928 0.2197 0.0210 0.0190 -0.0338 424 ALA A CA 3021 C C . ALA A 431 ? 0.2058 0.1976 0.2132 0.0264 0.0161 -0.0366 424 ALA A C 3022 O O . ALA A 431 ? 0.2121 0.2110 0.1993 0.0232 0.0209 -0.0542 424 ALA A O 3023 C CB . ALA A 431 ? 0.1947 0.2007 0.2130 0.0411 0.0199 -0.0275 424 ALA A CB 3024 N N . GLU A 432 ? 0.2133 0.1907 0.2002 0.0261 0.0183 -0.0488 425 GLU A N 3025 C CA . GLU A 432 ? 0.2041 0.2021 0.2229 0.0248 0.0317 -0.0331 425 GLU A CA 3026 C C . GLU A 432 ? 0.2028 0.1968 0.2273 0.0193 0.0287 -0.0367 425 GLU A C 3027 O O . GLU A 432 ? 0.2277 0.2100 0.2430 0.0261 0.0482 -0.0305 425 GLU A O 3028 C CB . GLU A 432 ? 0.2086 0.1738 0.2045 0.0232 0.0275 -0.0465 425 GLU A CB 3029 C CG . GLU A 432 ? 0.1890 0.2184 0.2352 0.0006 0.0096 -0.0414 425 GLU A CG 3030 C CD . GLU A 432 ? 0.1525 0.2163 0.2405 -0.0258 0.0580 -0.0658 425 GLU A CD 3031 O OE1 . GLU A 432 ? 0.2194 0.2294 0.2766 0.0084 0.0643 -0.0363 425 GLU A OE1 3032 O OE2 . GLU A 432 ? 0.2079 0.2293 0.2224 0.0128 0.0394 -0.0120 425 GLU A OE2 3033 N N . PHE A 433 ? 0.2001 0.1985 0.2413 0.0051 0.0232 -0.0371 426 PHE A N 3034 C CA . PHE A 433 ? 0.1933 0.1866 0.2195 -0.0073 0.0151 -0.0445 426 PHE A CA 3035 C C . PHE A 433 ? 0.1937 0.1974 0.2191 -0.0019 0.0169 -0.0419 426 PHE A C 3036 O O . PHE A 433 ? 0.1841 0.1977 0.1974 -0.0039 0.0137 -0.0411 426 PHE A O 3037 C CB . PHE A 433 ? 0.1926 0.1895 0.2541 -0.0083 0.0202 -0.0445 426 PHE A CB 3038 C CG . PHE A 433 ? 0.1995 0.1908 0.2592 -0.0064 0.0028 -0.0615 426 PHE A CG 3039 C CD1 . PHE A 433 ? 0.1362 0.2076 0.2180 0.0093 0.0372 -0.0501 426 PHE A CD1 3040 C CD2 . PHE A 433 ? 0.1844 0.2041 0.2570 -0.0068 -0.0328 -0.0414 426 PHE A CD2 3041 C CE1 . PHE A 433 ? 0.1241 0.1715 0.2750 -0.0049 -0.0142 -0.0466 426 PHE A CE1 3042 C CE2 . PHE A 433 ? 0.2056 0.2258 0.2264 -0.0086 0.0155 -0.0510 426 PHE A CE2 3043 C CZ . PHE A 433 ? 0.2230 0.2465 0.2300 0.0041 -0.0033 -0.0550 426 PHE A CZ 3044 N N . GLY A 434 ? 0.1864 0.1874 0.2247 -0.0088 0.0145 -0.0501 427 GLY A N 3045 C CA . GLY A 434 ? 0.1980 0.1840 0.2071 0.0055 0.0278 -0.0437 427 GLY A CA 3046 C C . GLY A 434 ? 0.1872 0.1867 0.1991 0.0000 0.0161 -0.0368 427 GLY A C 3047 O O . GLY A 434 ? 0.1992 0.2226 0.2147 0.0031 0.0271 -0.0493 427 GLY A O 3048 N N . LEU A 435 ? 0.1667 0.1847 0.1997 -0.0052 0.0118 -0.0278 428 LEU A N 3049 C CA . LEU A 435 ? 0.1617 0.1787 0.1884 -0.0027 0.0085 -0.0223 428 LEU A CA 3050 C C . LEU A 435 ? 0.1650 0.1862 0.1964 0.0051 -0.0027 -0.0269 428 LEU A C 3051 O O . LEU A 435 ? 0.1644 0.1953 0.2001 0.0177 0.0039 -0.0437 428 LEU A O 3052 C CB . LEU A 435 ? 0.1645 0.1827 0.1779 -0.0050 -0.0004 -0.0164 428 LEU A CB 3053 C CG . LEU A 435 ? 0.1462 0.1593 0.2043 0.0022 -0.0071 -0.0117 428 LEU A CG 3054 C CD1 . LEU A 435 ? 0.1959 0.1595 0.1925 -0.0040 -0.0186 -0.0530 428 LEU A CD1 3055 C CD2 . LEU A 435 ? 0.1554 0.1656 0.1853 0.0428 -0.0154 -0.0430 428 LEU A CD2 3056 N N . LEU A 436 ? 0.1560 0.1953 0.1790 -0.0057 -0.0083 -0.0210 429 LEU A N 3057 C CA . LEU A 436 ? 0.1558 0.1918 0.1854 0.0055 0.0050 -0.0176 429 LEU A CA 3058 C C . LEU A 436 ? 0.1760 0.1965 0.1797 0.0066 0.0057 -0.0254 429 LEU A C 3059 O O . LEU A 436 ? 0.1876 0.2049 0.2017 -0.0020 0.0238 -0.0260 429 LEU A O 3060 C CB . LEU A 436 ? 0.1480 0.1698 0.1517 0.0058 -0.0096 -0.0163 429 LEU A CB 3061 C CG . LEU A 436 ? 0.1829 0.1527 0.1833 0.0189 0.0103 -0.0206 429 LEU A CG 3062 C CD1 . LEU A 436 ? 0.1490 0.1646 0.1850 -0.0089 -0.0071 -0.0406 429 LEU A CD1 3063 C CD2 . LEU A 436 ? 0.2190 0.1578 0.1158 0.0052 0.0261 0.0094 429 LEU A CD2 3064 N N . GLY A 437 ? 0.1949 0.2054 0.1877 -0.0016 0.0113 -0.0136 430 GLY A N 3065 C CA . GLY A 437 ? 0.2010 0.2063 0.1911 0.0075 0.0222 -0.0236 430 GLY A CA 3066 C C . GLY A 437 ? 0.1947 0.1953 0.2109 0.0165 0.0147 -0.0080 430 GLY A C 3067 O O . GLY A 437 ? 0.2038 0.1946 0.2008 0.0272 0.0151 -0.0116 430 GLY A O 3068 N N . SER A 438 ? 0.1884 0.1852 0.2132 0.0182 0.0000 -0.0072 431 SER A N 3069 C CA . SER A 438 ? 0.1881 0.2016 0.1998 0.0273 -0.0023 -0.0143 431 SER A CA 3070 C C . SER A 438 ? 0.1794 0.1970 0.1922 0.0204 -0.0013 -0.0095 431 SER A C 3071 O O . SER A 438 ? 0.1700 0.1660 0.2082 0.0301 0.0027 -0.0206 431 SER A O 3072 C CB . SER A 438 ? 0.1750 0.2253 0.2000 0.0170 -0.0030 -0.0127 431 SER A CB 3073 O OG . SER A 438 ? 0.1976 0.2443 0.1653 0.0296 -0.0290 0.0108 431 SER A OG 3074 N N . THR A 439 ? 0.1745 0.1922 0.1832 0.0107 -0.0065 -0.0005 432 THR A N 3075 C CA . THR A 439 ? 0.1741 0.1885 0.1838 0.0089 0.0022 0.0098 432 THR A CA 3076 C C . THR A 439 ? 0.1806 0.1897 0.1731 0.0100 0.0250 0.0087 432 THR A C 3077 O O . THR A 439 ? 0.2115 0.2040 0.1659 -0.0024 0.0244 0.0045 432 THR A O 3078 C CB . THR A 439 ? 0.1651 0.1907 0.1782 0.0204 0.0114 0.0102 432 THR A CB 3079 O OG1 . THR A 439 ? 0.1925 0.2200 0.2147 0.0054 0.0051 0.0095 432 THR A OG1 3080 C CG2 . THR A 439 ? 0.1103 0.1563 0.1744 0.0032 -0.0146 0.0162 432 THR A CG2 3081 N N . GLU A 440 ? 0.1721 0.1935 0.1414 -0.0113 0.0137 0.0025 433 GLU A N 3082 C CA . GLU A 440 ? 0.1951 0.2006 0.1688 0.0051 0.0177 -0.0079 433 GLU A CA 3083 C C . GLU A 440 ? 0.1932 0.2029 0.1884 0.0084 0.0185 -0.0089 433 GLU A C 3084 O O . GLU A 440 ? 0.1854 0.2157 0.2030 0.0130 0.0196 -0.0014 433 GLU A O 3085 C CB . GLU A 440 ? 0.1932 0.2057 0.1654 -0.0104 0.0169 -0.0065 433 GLU A CB 3086 C CG . GLU A 440 ? 0.2163 0.2091 0.1624 0.0291 -0.0174 -0.0365 433 GLU A CG 3087 C CD . GLU A 440 ? 0.2352 0.1850 0.1753 -0.0130 -0.0131 -0.0386 433 GLU A CD 3088 O OE1 . GLU A 440 ? 0.1997 0.2197 0.2037 0.0141 -0.0204 -0.0141 433 GLU A OE1 3089 O OE2 . GLU A 440 ? 0.2200 0.2291 0.2063 -0.0033 0.0249 -0.0192 433 GLU A OE2 3090 N N . TRP A 441 ? 0.1889 0.1878 0.1817 0.0080 0.0194 -0.0001 434 TRP A N 3091 C CA . TRP A 441 ? 0.1986 0.1835 0.1896 0.0114 0.0134 -0.0001 434 TRP A CA 3092 C C . TRP A 441 ? 0.1880 0.1993 0.1916 0.0233 0.0105 -0.0016 434 TRP A C 3093 O O . TRP A 441 ? 0.2199 0.2064 0.1937 0.0267 0.0167 -0.0175 434 TRP A O 3094 C CB . TRP A 441 ? 0.2013 0.1919 0.1966 0.0209 0.0180 0.0092 434 TRP A CB 3095 C CG . TRP A 441 ? 0.2087 0.1969 0.2001 0.0232 0.0273 -0.0070 434 TRP A CG 3096 C CD1 . TRP A 441 ? 0.2514 0.1827 0.1904 0.0203 0.0424 0.0168 434 TRP A CD1 3097 C CD2 . TRP A 441 ? 0.2464 0.2166 0.2169 0.0289 0.0235 -0.0150 434 TRP A CD2 3098 N NE1 . TRP A 441 ? 0.2655 0.1913 0.2178 0.0347 0.0443 0.0059 434 TRP A NE1 3099 C CE2 . TRP A 441 ? 0.2370 0.1923 0.2191 0.0407 0.0269 -0.0153 434 TRP A CE2 3100 C CE3 . TRP A 441 ? 0.2222 0.1945 0.2139 0.0329 0.0302 -0.0300 434 TRP A CE3 3101 C CZ2 . TRP A 441 ? 0.2405 0.2080 0.1908 0.0492 -0.0282 0.0093 434 TRP A CZ2 3102 C CZ3 . TRP A 441 ? 0.2871 0.2112 0.2041 0.0661 0.0164 -0.0110 434 TRP A CZ3 3103 C CH2 . TRP A 441 ? 0.2199 0.2383 0.1735 0.0300 -0.0083 0.0136 434 TRP A CH2 3104 N N . ALA A 442 ? 0.1896 0.1817 0.1983 0.0050 0.0129 0.0006 435 ALA A N 3105 C CA . ALA A 442 ? 0.1816 0.2050 0.2036 0.0119 0.0141 -0.0197 435 ALA A CA 3106 C C . ALA A 442 ? 0.1896 0.2164 0.1927 0.0149 0.0177 -0.0177 435 ALA A C 3107 O O . ALA A 442 ? 0.1943 0.2204 0.1640 0.0282 0.0265 -0.0332 435 ALA A O 3108 C CB . ALA A 442 ? 0.1542 0.1812 0.2096 -0.0001 0.0506 -0.0326 435 ALA A CB 3109 N N . GLU A 443 ? 0.1741 0.2371 0.1635 0.0016 0.0093 -0.0182 436 GLU A N 3110 C CA . GLU A 443 ? 0.1941 0.2156 0.1741 0.0212 0.0123 -0.0059 436 GLU A CA 3111 C C . GLU A 443 ? 0.1989 0.2148 0.1891 0.0146 0.0075 -0.0032 436 GLU A C 3112 O O . GLU A 443 ? 0.1889 0.2060 0.2074 0.0265 -0.0076 -0.0028 436 GLU A O 3113 C CB . GLU A 443 ? 0.1925 0.2119 0.1457 0.0212 0.0157 -0.0202 436 GLU A CB 3114 C CG . GLU A 443 ? 0.2168 0.2242 0.1679 0.0081 0.0307 -0.0237 436 GLU A CG 3115 C CD . GLU A 443 ? 0.2024 0.2181 0.1841 0.0092 0.0225 -0.0216 436 GLU A CD 3116 O OE1 . GLU A 443 ? 0.2203 0.2184 0.1856 0.0215 0.0061 -0.0075 436 GLU A OE1 3117 O OE2 . GLU A 443 ? 0.1796 0.2234 0.2084 -0.0004 0.0054 -0.0214 436 GLU A OE2 3118 N N . GLU A 444 ? 0.2012 0.1868 0.1874 -0.0081 0.0062 -0.0016 437 GLU A N 3119 C CA . GLU A 444 ? 0.2055 0.2025 0.2076 -0.0036 0.0130 0.0049 437 GLU A CA 3120 C C . GLU A 444 ? 0.2057 0.1927 0.2158 0.0162 0.0182 0.0071 437 GLU A C 3121 O O . GLU A 444 ? 0.2013 0.2037 0.1958 0.0227 0.0244 0.0227 437 GLU A O 3122 C CB . GLU A 444 ? 0.2024 0.1890 0.2404 -0.0135 0.0096 -0.0015 437 GLU A CB 3123 C CG . GLU A 444 ? 0.2676 0.2249 0.2881 -0.0358 0.0313 0.0325 437 GLU A CG 3124 C CD . GLU A 444 ? 0.3577 0.2674 0.4419 -0.0318 -0.0248 0.0681 437 GLU A CD 3125 O OE1 . GLU A 444 ? 0.4638 0.3898 0.5430 -0.0761 -0.0266 0.0450 437 GLU A OE1 3126 O OE2 . GLU A 444 ? 0.4253 0.2120 0.4176 -0.0201 0.0009 0.1046 437 GLU A OE2 3127 N N . ASN A 445 ? 0.2152 0.1931 0.2022 0.0159 0.0062 0.0018 438 ASN A N 3128 C CA . ASN A 445 ? 0.2187 0.1847 0.1959 0.0207 0.0106 0.0171 438 ASN A CA 3129 C C . ASN A 445 ? 0.2110 0.1939 0.1839 0.0237 0.0116 0.0085 438 ASN A C 3130 O O . ASN A 445 ? 0.1927 0.2071 0.1624 0.0315 0.0033 0.0202 438 ASN A O 3131 C CB . ASN A 445 ? 0.2211 0.1770 0.2133 0.0172 0.0093 0.0218 438 ASN A CB 3132 C CG . ASN A 445 ? 0.2228 0.1872 0.2134 0.0341 0.0329 0.0368 438 ASN A CG 3133 O OD1 . ASN A 445 ? 0.2672 0.1775 0.2691 0.0283 0.0729 0.0749 438 ASN A OD1 3134 N ND2 . ASN A 445 ? 0.2073 0.1692 0.2356 0.0123 0.0211 0.0067 438 ASN A ND2 3135 N N . SER A 446 ? 0.1985 0.1870 0.1644 0.0308 0.0254 0.0107 439 SER A N 3136 C CA . SER A 446 ? 0.2266 0.2077 0.1701 0.0254 0.0195 0.0094 439 SER A CA 3137 C C . SER A 446 ? 0.2211 0.2154 0.1834 0.0325 0.0219 0.0046 439 SER A C 3138 O O . SER A 446 ? 0.2346 0.2215 0.1864 0.0445 0.0207 0.0003 439 SER A O 3139 C CB . SER A 446 ? 0.2150 0.2228 0.1765 0.0366 0.0187 0.0130 439 SER A CB 3140 O OG . SER A 446 ? 0.2286 0.1989 0.1873 0.0071 -0.0135 0.0211 439 SER A OG 3141 N N . ARG A 447 ? 0.2045 0.2126 0.1560 0.0430 0.0160 0.0175 440 ARG A N 3142 C CA . ARG A 447 ? 0.2092 0.2007 0.1813 0.0392 -0.0014 0.0197 440 ARG A CA 3143 C C . ARG A 447 ? 0.2168 0.2080 0.1767 0.0314 0.0053 0.0130 440 ARG A C 3144 O O . ARG A 447 ? 0.2303 0.2174 0.1644 0.0170 -0.0055 0.0065 440 ARG A O 3145 C CB . ARG A 447 ? 0.1951 0.1934 0.1878 0.0432 -0.0007 0.0229 440 ARG A CB 3146 C CG . ARG A 447 ? 0.1930 0.2066 0.2422 0.0353 -0.0451 0.0128 440 ARG A CG 3147 C CD . ARG A 447 ? 0.2227 0.2171 0.2928 0.0173 -0.0736 0.0166 440 ARG A CD 3148 N NE . ARG A 447 ? 0.2546 0.2238 0.2380 0.0174 -0.0235 0.0025 440 ARG A NE 3149 C CZ . ARG A 447 ? 0.2376 0.2376 0.2585 0.0234 -0.0151 -0.0185 440 ARG A CZ 3150 N NH1 . ARG A 447 ? 0.2417 0.2740 0.2914 0.0390 0.0343 -0.0478 440 ARG A NH1 3151 N NH2 . ARG A 447 ? 0.2196 0.2278 0.1908 0.0204 -0.0075 -0.0620 440 ARG A NH2 3152 N N . LEU A 448 ? 0.2110 0.1965 0.1725 0.0414 0.0029 0.0246 441 LEU A N 3153 C CA . LEU A 448 ? 0.2192 0.2051 0.1785 0.0340 0.0144 0.0180 441 LEU A CA 3154 C C . LEU A 448 ? 0.2350 0.2039 0.1859 0.0268 0.0216 0.0193 441 LEU A C 3155 O O . LEU A 448 ? 0.2442 0.2298 0.1667 0.0299 0.0280 0.0225 441 LEU A O 3156 C CB . LEU A 448 ? 0.2131 0.1998 0.1668 0.0155 0.0074 0.0312 441 LEU A CB 3157 C CG . LEU A 448 ? 0.2061 0.2139 0.2028 0.0220 0.0274 0.0254 441 LEU A CG 3158 C CD1 . LEU A 448 ? 0.2713 0.2410 0.1862 0.0049 -0.0120 0.0562 441 LEU A CD1 3159 C CD2 . LEU A 448 ? 0.2111 0.1944 0.1986 0.0003 0.0265 0.0138 441 LEU A CD2 3160 N N . LEU A 449 ? 0.2332 0.1850 0.1909 0.0408 0.0315 0.0132 442 LEU A N 3161 C CA . LEU A 449 ? 0.2478 0.2192 0.2008 0.0440 0.0243 0.0048 442 LEU A CA 3162 C C . LEU A 449 ? 0.2456 0.2406 0.2017 0.0394 0.0209 -0.0084 442 LEU A C 3163 O O . LEU A 449 ? 0.2550 0.2871 0.2337 0.0423 0.0337 -0.0204 442 LEU A O 3164 C CB . LEU A 449 ? 0.2445 0.2171 0.2011 0.0481 0.0209 0.0003 442 LEU A CB 3165 C CG . LEU A 449 ? 0.2861 0.2289 0.1917 0.0364 -0.0026 -0.0154 442 LEU A CG 3166 C CD1 . LEU A 449 ? 0.1951 0.2895 0.1824 0.0072 0.0148 -0.0324 442 LEU A CD1 3167 C CD2 . LEU A 449 ? 0.3117 0.2856 0.1784 0.0250 -0.0225 -0.0005 442 LEU A CD2 3168 N N . GLN A 450 ? 0.2607 0.2075 0.2020 0.0488 0.0194 0.0064 443 GLN A N 3169 C CA . GLN A 450 ? 0.2777 0.2410 0.2152 0.0335 -0.0051 -0.0154 443 GLN A CA 3170 C C . GLN A 450 ? 0.2714 0.2550 0.1619 0.0215 0.0002 -0.0043 443 GLN A C 3171 O O . GLN A 450 ? 0.2805 0.2586 0.1430 0.0117 -0.0029 -0.0105 443 GLN A O 3172 C CB . GLN A 450 ? 0.3200 0.2102 0.1806 0.0245 -0.0073 0.0160 443 GLN A CB 3173 C CG A GLN A 450 ? 0.3135 0.2230 0.1924 0.0283 0.0037 -0.0161 443 GLN A CG 3174 C CG B GLN A 450 ? 0.2480 0.2489 0.2026 0.0343 0.0243 0.0000 443 GLN A CG 3175 C CD A GLN A 450 ? 0.2484 0.2160 0.1522 0.0414 0.0022 -0.0217 443 GLN A CD 3176 C CD B GLN A 450 ? 0.2465 0.2089 0.2410 -0.0009 0.0100 -0.0144 443 GLN A CD 3177 O OE1 A GLN A 450 ? 0.2088 0.2346 0.1648 0.0756 0.0241 -0.0266 443 GLN A OE1 3178 O OE1 B GLN A 450 ? 0.2693 0.3049 0.2297 0.0173 0.0379 0.0667 443 GLN A OE1 3179 N NE2 A GLN A 450 ? 0.2413 0.2504 0.1157 0.0239 0.0545 0.0069 443 GLN A NE2 3180 N NE2 B GLN A 450 ? 0.0564 0.0520 0.2062 0.0287 -0.0202 -0.0239 443 GLN A NE2 3181 N N . GLU A 451 ? 0.2512 0.2413 0.1730 0.0329 -0.0087 0.0032 444 GLU A N 3182 C CA . GLU A 451 ? 0.2331 0.2333 0.1686 0.0491 -0.0027 0.0160 444 GLU A CA 3183 C C . GLU A 451 ? 0.2226 0.2305 0.1698 0.0545 -0.0026 0.0109 444 GLU A C 3184 O O . GLU A 451 ? 0.2379 0.2263 0.1667 0.0565 -0.0081 0.0097 444 GLU A O 3185 C CB . GLU A 451 ? 0.2425 0.2423 0.1743 0.0542 -0.0105 0.0198 444 GLU A CB 3186 C CG . GLU A 451 ? 0.2539 0.2320 0.2004 0.0345 -0.0342 0.0353 444 GLU A CG 3187 C CD . GLU A 451 ? 0.3164 0.2437 0.2084 0.0309 -0.0320 0.0267 444 GLU A CD 3188 O OE1 . GLU A 451 ? 0.2618 0.2278 0.2201 0.0281 -0.0086 0.0092 444 GLU A OE1 3189 O OE2 . GLU A 451 ? 0.3979 0.2318 0.2413 0.0569 -0.0455 0.0243 444 GLU A OE2 3190 N N . ARG A 452 ? 0.2150 0.2088 0.1744 0.0554 -0.0037 0.0218 445 ARG A N 3191 C CA . ARG A 452 ? 0.2144 0.2264 0.1600 0.0547 0.0071 0.0131 445 ARG A CA 3192 C C . ARG A 452 ? 0.2266 0.2289 0.1692 0.0578 0.0001 0.0104 445 ARG A C 3193 O O . ARG A 452 ? 0.2208 0.2490 0.1709 0.0595 0.0035 0.0057 445 ARG A O 3194 C CB . ARG A 452 ? 0.2078 0.2326 0.1662 0.0535 0.0088 0.0271 445 ARG A CB 3195 C CG . ARG A 452 ? 0.2189 0.2311 0.1548 0.0608 0.0197 0.0143 445 ARG A CG 3196 C CD . ARG A 452 ? 0.2089 0.2273 0.1836 0.0637 0.0243 0.0194 445 ARG A CD 3197 N NE . ARG A 452 ? 0.2259 0.2510 0.1431 0.0634 0.0394 0.0435 445 ARG A NE 3198 C CZ . ARG A 452 ? 0.2474 0.2212 0.2041 0.0673 0.0503 0.0288 445 ARG A CZ 3199 N NH1 . ARG A 452 ? 0.2700 0.2255 0.1440 0.0762 0.0600 0.0191 445 ARG A NH1 3200 N NH2 . ARG A 452 ? 0.2695 0.2447 0.1468 0.0844 0.0961 0.0160 445 ARG A NH2 3201 N N . GLY A 453 ? 0.2223 0.2408 0.1770 0.0618 0.0110 0.0004 446 GLY A N 3202 C CA . GLY A 453 ? 0.2404 0.2335 0.1744 0.0610 -0.0037 0.0072 446 GLY A CA 3203 C C . GLY A 453 ? 0.2621 0.2424 0.1856 0.0603 -0.0128 0.0004 446 GLY A C 3204 O O . GLY A 453 ? 0.2819 0.2460 0.1840 0.0378 -0.0172 0.0086 446 GLY A O 3205 N N . VAL A 454 ? 0.2596 0.2512 0.1635 0.0652 -0.0148 -0.0034 447 VAL A N 3206 C CA . VAL A 454 ? 0.2699 0.2563 0.1778 0.0536 -0.0134 -0.0245 447 VAL A CA 3207 C C . VAL A 454 ? 0.2538 0.2416 0.1859 0.0613 -0.0284 -0.0165 447 VAL A C 3208 O O . VAL A 454 ? 0.2287 0.2336 0.1933 0.0580 -0.0366 -0.0110 447 VAL A O 3209 C CB . VAL A 454 ? 0.2666 0.2740 0.1867 0.0567 -0.0145 -0.0185 447 VAL A CB 3210 C CG1 . VAL A 454 ? 0.2799 0.2524 0.1449 0.0467 -0.0058 -0.0603 447 VAL A CG1 3211 C CG2 . VAL A 454 ? 0.3211 0.3155 0.1936 0.0547 0.0396 -0.0468 447 VAL A CG2 3212 N N . ALA A 455 ? 0.2411 0.2402 0.1781 0.0556 -0.0354 -0.0221 448 ALA A N 3213 C CA . ALA A 455 ? 0.2335 0.2136 0.1487 0.0636 -0.0280 -0.0324 448 ALA A CA 3214 C C . ALA A 455 ? 0.2399 0.2244 0.1733 0.0516 -0.0204 -0.0245 448 ALA A C 3215 O O . ALA A 455 ? 0.2308 0.2474 0.1784 0.0465 0.0127 -0.0322 448 ALA A O 3216 C CB . ALA A 455 ? 0.2286 0.2176 0.1788 0.0574 -0.0291 -0.0396 448 ALA A CB 3217 N N . TYR A 456 ? 0.2306 0.2073 0.1648 0.0562 -0.0175 -0.0288 449 TYR A N 3218 C CA . TYR A 456 ? 0.2233 0.2017 0.1694 0.0565 -0.0250 -0.0259 449 TYR A CA 3219 C C . TYR A 456 ? 0.2354 0.2086 0.1802 0.0538 -0.0286 -0.0209 449 TYR A C 3220 O O . TYR A 456 ? 0.2226 0.2236 0.1942 0.0411 -0.0406 -0.0070 449 TYR A O 3221 C CB . TYR A 456 ? 0.2170 0.1824 0.1672 0.0622 -0.0328 -0.0316 449 TYR A CB 3222 C CG . TYR A 456 ? 0.2208 0.2040 0.1758 0.0389 -0.0251 -0.0359 449 TYR A CG 3223 C CD1 . TYR A 456 ? 0.2647 0.1821 0.1522 0.0151 -0.0308 -0.0074 449 TYR A CD1 3224 C CD2 . TYR A 456 ? 0.2161 0.1993 0.1674 0.0338 -0.0063 -0.0303 449 TYR A CD2 3225 C CE1 . TYR A 456 ? 0.2380 0.1795 0.1944 0.0421 -0.0121 -0.0336 449 TYR A CE1 3226 C CE2 . TYR A 456 ? 0.2282 0.1620 0.2015 0.0283 -0.0340 -0.0450 449 TYR A CE2 3227 C CZ . TYR A 456 ? 0.2393 0.1900 0.1968 0.0294 -0.0043 -0.0259 449 TYR A CZ 3228 O OH . TYR A 456 ? 0.2561 0.2206 0.2146 0.0634 0.0129 -0.0228 449 TYR A OH 3229 N N . ILE A 457 ? 0.2404 0.1861 0.1692 0.0548 -0.0314 -0.0267 450 ILE A N 3230 C CA . ILE A 457 ? 0.2287 0.2077 0.1829 0.0441 -0.0134 -0.0334 450 ILE A CA 3231 C C . ILE A 457 ? 0.2458 0.2137 0.2091 0.0494 -0.0050 -0.0334 450 ILE A C 3232 O O . ILE A 457 ? 0.2662 0.2163 0.2182 0.0412 0.0100 -0.0366 450 ILE A O 3233 C CB . ILE A 457 ? 0.2307 0.1971 0.1852 0.0535 -0.0174 -0.0223 450 ILE A CB 3234 C CG1 . ILE A 457 ? 0.2561 0.1713 0.1689 0.0370 -0.0041 -0.0197 450 ILE A CG1 3235 C CG2 . ILE A 457 ? 0.2086 0.1857 0.1972 0.0366 -0.0379 -0.0511 450 ILE A CG2 3236 C CD1 . ILE A 457 ? 0.2423 0.1553 0.2120 0.0823 -0.0111 -0.0081 450 ILE A CD1 3237 N N . ASN A 458 ? 0.2295 0.2246 0.1883 0.0539 0.0010 -0.0355 451 ASN A N 3238 C CA . ASN A 458 ? 0.2389 0.2068 0.2043 0.0536 -0.0178 -0.0314 451 ASN A CA 3239 C C . ASN A 458 ? 0.2621 0.2226 0.2197 0.0444 -0.0230 -0.0293 451 ASN A C 3240 O O . ASN A 458 ? 0.2899 0.2208 0.2101 0.0433 -0.0358 -0.0410 451 ASN A O 3241 C CB . ASN A 458 ? 0.2419 0.2002 0.1850 0.0510 -0.0146 -0.0305 451 ASN A CB 3242 C CG . ASN A 458 ? 0.2302 0.2144 0.1959 0.0507 0.0016 -0.0039 451 ASN A CG 3243 O OD1 . ASN A 458 ? 0.2557 0.2632 0.2048 0.0558 -0.0176 -0.0201 451 ASN A OD1 3244 N ND2 . ASN A 458 ? 0.2724 0.1917 0.1967 0.0654 0.0273 -0.0147 451 ASN A ND2 3245 N N . ALA A 459 ? 0.2650 0.2051 0.2320 0.0487 -0.0230 -0.0292 452 ALA A N 3246 C CA . ALA A 459 ? 0.2433 0.2239 0.2331 0.0489 -0.0358 -0.0242 452 ALA A CA 3247 C C . ALA A 459 ? 0.2447 0.2332 0.2437 0.0560 -0.0223 -0.0195 452 ALA A C 3248 O O . ALA A 459 ? 0.2533 0.2474 0.2409 0.0358 -0.0261 -0.0169 452 ALA A O 3249 C CB . ALA A 459 ? 0.2283 0.2060 0.2231 0.0460 -0.0413 -0.0119 452 ALA A CB 3250 N N . ASP A 460 ? 0.2455 0.2345 0.2358 0.0488 -0.0194 -0.0110 453 ASP A N 3251 C CA . ASP A 460 ? 0.2358 0.2333 0.2575 0.0518 -0.0202 -0.0199 453 ASP A CA 3252 C C . ASP A 460 ? 0.2330 0.2352 0.2597 0.0522 -0.0257 -0.0181 453 ASP A C 3253 O O . ASP A 460 ? 0.2153 0.2436 0.2782 0.0612 -0.0374 -0.0185 453 ASP A O 3254 C CB . ASP A 460 ? 0.2568 0.2326 0.2367 0.0419 -0.0175 -0.0333 453 ASP A CB 3255 C CG . ASP A 460 ? 0.2499 0.2488 0.2870 0.0282 -0.0039 -0.0249 453 ASP A CG 3256 O OD1 . ASP A 460 ? 0.3213 0.2587 0.2796 0.0265 -0.0108 -0.0034 453 ASP A OD1 3257 O OD2 . ASP A 460 ? 0.2567 0.2640 0.2642 0.0177 -0.0263 -0.0506 453 ASP A OD2 3258 N N . SER A 461 ? 0.2228 0.2249 0.2639 0.0571 -0.0258 -0.0206 454 SER A N 3259 C CA A SER A 461 ? 0.2208 0.2292 0.2598 0.0488 -0.0275 -0.0194 454 SER A CA 3260 C CA B SER A 461 ? 0.2321 0.2394 0.2702 0.0524 -0.0243 -0.0176 454 SER A CA 3261 C C . SER A 461 ? 0.2294 0.2440 0.2751 0.0492 -0.0280 -0.0198 454 SER A C 3262 O O . SER A 461 ? 0.2293 0.2462 0.2686 0.0502 -0.0118 -0.0120 454 SER A O 3263 C CB A SER A 461 ? 0.2023 0.2114 0.2556 0.0512 -0.0293 -0.0258 454 SER A CB 3264 C CB B SER A 461 ? 0.2268 0.2317 0.2736 0.0541 -0.0207 -0.0186 454 SER A CB 3265 O OG A SER A 461 ? 0.1476 0.1466 0.2027 0.0389 -0.0397 -0.0286 454 SER A OG 3266 O OG B SER A 461 ? 0.2475 0.2384 0.2733 0.0538 -0.0199 -0.0066 454 SER A OG 3267 N N . SER A 462 ? 0.2426 0.2588 0.2768 0.0552 -0.0304 -0.0182 455 SER A N 3268 C CA . SER A 462 ? 0.2618 0.2717 0.2855 0.0604 -0.0361 -0.0238 455 SER A CA 3269 C C . SER A 462 ? 0.2637 0.2544 0.2931 0.0643 -0.0354 -0.0239 455 SER A C 3270 O O . SER A 462 ? 0.2636 0.2223 0.2863 0.0824 -0.0392 -0.0366 455 SER A O 3271 C CB . SER A 462 ? 0.2641 0.2813 0.2748 0.0532 -0.0302 -0.0187 455 SER A CB 3272 O OG . SER A 462 ? 0.2840 0.3250 0.2953 0.0604 -0.0419 -0.0280 455 SER A OG 3273 N N . ILE A 463 ? 0.2743 0.2525 0.2974 0.0667 -0.0415 -0.0324 456 ILE A N 3274 C CA . ILE A 463 ? 0.2860 0.2712 0.3239 0.0636 -0.0456 -0.0346 456 ILE A CA 3275 C C . ILE A 463 ? 0.2951 0.2944 0.3363 0.0559 -0.0410 -0.0244 456 ILE A C 3276 O O . ILE A 463 ? 0.3063 0.3128 0.3162 0.0474 -0.0435 -0.0259 456 ILE A O 3277 C CB . ILE A 463 ? 0.2929 0.2743 0.3278 0.0654 -0.0583 -0.0327 456 ILE A CB 3278 C CG1 . ILE A 463 ? 0.3321 0.2668 0.3639 0.0882 -0.0440 -0.0326 456 ILE A CG1 3279 C CG2 . ILE A 463 ? 0.2649 0.2462 0.3341 0.0785 -0.0724 -0.0235 456 ILE A CG2 3280 C CD1 . ILE A 463 ? 0.4751 0.2791 0.3922 0.0887 -0.0549 -0.0290 456 ILE A CD1 3281 N N . GLU A 464 ? 0.3036 0.3009 0.3613 0.0519 -0.0428 -0.0255 457 GLU A N 3282 C CA . GLU A 464 ? 0.3094 0.3103 0.3784 0.0508 -0.0364 -0.0344 457 GLU A CA 3283 C C . GLU A 464 ? 0.3158 0.3144 0.3905 0.0555 -0.0333 -0.0392 457 GLU A C 3284 O O . GLU A 464 ? 0.3387 0.3274 0.3908 0.0436 -0.0313 -0.0366 457 GLU A O 3285 C CB . GLU A 464 ? 0.3092 0.2841 0.3688 0.0581 -0.0386 -0.0350 457 GLU A CB 3286 C CG . GLU A 464 ? 0.2940 0.3015 0.3874 0.0457 -0.0300 -0.0405 457 GLU A CG 3287 C CD . GLU A 464 ? 0.3165 0.3081 0.3733 0.0135 -0.0427 -0.0414 457 GLU A CD 3288 O OE1 . GLU A 464 ? 0.3131 0.3106 0.3354 0.0408 -0.0638 -0.0575 457 GLU A OE1 3289 O OE2 . GLU A 464 ? 0.3895 0.3264 0.3823 -0.0041 -0.0535 -0.0914 457 GLU A OE2 3290 N N . GLY A 465 ? 0.3095 0.3119 0.3946 0.0597 -0.0473 -0.0432 458 GLY A N 3291 C CA . GLY A 465 ? 0.2908 0.3141 0.4060 0.0725 -0.0305 -0.0555 458 GLY A CA 3292 C C . GLY A 465 ? 0.2921 0.3207 0.4143 0.0783 -0.0352 -0.0532 458 GLY A C 3293 O O . GLY A 465 ? 0.3028 0.3051 0.3974 0.0812 -0.0206 -0.0514 458 GLY A O 3294 N N . ASN A 466 ? 0.2912 0.3126 0.4213 0.0860 -0.0434 -0.0624 459 ASN A N 3295 C CA . ASN A 466 ? 0.3012 0.3182 0.4344 0.0852 -0.0496 -0.0658 459 ASN A CA 3296 C C . ASN A 466 ? 0.2896 0.3195 0.4370 0.0842 -0.0472 -0.0716 459 ASN A C 3297 O O . ASN A 466 ? 0.3146 0.3195 0.4375 0.0718 -0.0475 -0.0747 459 ASN A O 3298 C CB . ASN A 466 ? 0.3061 0.3290 0.4509 0.0863 -0.0553 -0.0631 459 ASN A CB 3299 C CG . ASN A 466 ? 0.3298 0.3698 0.4627 0.1026 -0.0605 -0.0619 459 ASN A CG 3300 O OD1 . ASN A 466 ? 0.3665 0.3597 0.4707 0.1553 -0.0472 -0.0086 459 ASN A OD1 3301 N ND2 . ASN A 466 ? 0.4160 0.3980 0.5098 0.0976 -0.0569 -0.0921 459 ASN A ND2 3302 N N . TYR A 467 ? 0.2838 0.3183 0.4350 0.0772 -0.0401 -0.0820 460 TYR A N 3303 C CA . TYR A 467 ? 0.2818 0.3222 0.4338 0.0730 -0.0500 -0.0876 460 TYR A CA 3304 C C . TYR A 467 ? 0.2760 0.3202 0.4312 0.0742 -0.0551 -0.0778 460 TYR A C 3305 O O . TYR A 467 ? 0.2745 0.3204 0.4374 0.0804 -0.0613 -0.0847 460 TYR A O 3306 C CB . TYR A 467 ? 0.2999 0.3304 0.4369 0.0668 -0.0447 -0.0896 460 TYR A CB 3307 C CG . TYR A 467 ? 0.3320 0.3677 0.4518 0.0504 -0.0458 -0.1025 460 TYR A CG 3308 C CD1 . TYR A 467 ? 0.3591 0.3854 0.4718 0.0504 -0.0382 -0.0985 460 TYR A CD1 3309 C CD2 . TYR A 467 ? 0.3781 0.3931 0.4658 0.0536 -0.0273 -0.1008 460 TYR A CD2 3310 C CE1 . TYR A 467 ? 0.3410 0.4397 0.4650 0.0455 -0.0611 -0.1273 460 TYR A CE1 3311 C CE2 . TYR A 467 ? 0.3774 0.4318 0.4874 0.0355 -0.0262 -0.1221 460 TYR A CE2 3312 C CZ . TYR A 467 ? 0.4082 0.4609 0.5094 0.0013 -0.0499 -0.1172 460 TYR A CZ 3313 O OH . TYR A 467 ? 0.4538 0.5636 0.5326 -0.0613 -0.0338 -0.1443 460 TYR A OH 3314 N N . THR A 468 ? 0.2573 0.3050 0.4121 0.0738 -0.0574 -0.0716 461 THR A N 3315 C CA . THR A 468 ? 0.2516 0.2985 0.4068 0.0710 -0.0578 -0.0684 461 THR A CA 3316 C C . THR A 468 ? 0.2604 0.2952 0.3901 0.0749 -0.0545 -0.0611 461 THR A C 3317 O O . THR A 468 ? 0.2468 0.3055 0.3950 0.0755 -0.0516 -0.0646 461 THR A O 3318 C CB . THR A 468 ? 0.2616 0.2979 0.4119 0.0710 -0.0549 -0.0647 461 THR A CB 3319 O OG1 . THR A 468 ? 0.2659 0.2850 0.3986 0.0494 -0.0876 -0.0677 461 THR A OG1 3320 C CG2 . THR A 468 ? 0.2261 0.3160 0.3897 0.0740 -0.0533 -0.0609 461 THR A CG2 3321 N N . LEU A 469 ? 0.2586 0.2936 0.3691 0.0763 -0.0451 -0.0608 462 LEU A N 3322 C CA . LEU A 469 ? 0.2519 0.2933 0.3542 0.0748 -0.0445 -0.0621 462 LEU A CA 3323 C C . LEU A 469 ? 0.2486 0.2939 0.3500 0.0629 -0.0439 -0.0579 462 LEU A C 3324 O O . LEU A 469 ? 0.2407 0.3088 0.3707 0.0570 -0.0505 -0.0481 462 LEU A O 3325 C CB . LEU A 469 ? 0.2614 0.2854 0.3618 0.0852 -0.0398 -0.0751 462 LEU A CB 3326 C CG . LEU A 469 ? 0.2488 0.2628 0.3383 0.0747 -0.0364 -0.1004 462 LEU A CG 3327 C CD1 . LEU A 469 ? 0.2253 0.2960 0.3487 0.0835 -0.0335 -0.0827 462 LEU A CD1 3328 C CD2 . LEU A 469 ? 0.2458 0.2615 0.2704 0.1429 -0.0486 -0.0760 462 LEU A CD2 3329 N N . ARG A 470 ? 0.2179 0.2706 0.3150 0.0611 -0.0339 -0.0556 463 ARG A N 3330 C CA . ARG A 470 ? 0.2281 0.2789 0.3246 0.0616 -0.0391 -0.0669 463 ARG A CA 3331 C C . ARG A 470 ? 0.2266 0.2657 0.3168 0.0619 -0.0398 -0.0610 463 ARG A C 3332 O O . ARG A 470 ? 0.2234 0.2692 0.3194 0.0701 -0.0142 -0.0672 463 ARG A O 3333 C CB . ARG A 470 ? 0.2280 0.2785 0.3265 0.0607 -0.0480 -0.0650 463 ARG A CB 3334 C CG . ARG A 470 ? 0.2761 0.2911 0.3441 0.0459 -0.0693 -0.0684 463 ARG A CG 3335 C CD . ARG A 470 ? 0.3190 0.3029 0.3543 0.0380 -0.0659 -0.0730 463 ARG A CD 3336 N NE . ARG A 470 ? 0.3670 0.3199 0.3857 0.0468 -0.0603 -0.0761 463 ARG A NE 3337 C CZ . ARG A 470 ? 0.3751 0.3167 0.3818 0.0582 -0.0570 -0.0602 463 ARG A CZ 3338 N NH1 . ARG A 470 ? 0.3839 0.2748 0.2969 0.0610 -0.0175 -0.0946 463 ARG A NH1 3339 N NH2 . ARG A 470 ? 0.3374 0.3038 0.4370 0.0715 -0.0503 -0.0135 463 ARG A NH2 3340 N N . VAL A 471 ? 0.2348 0.2509 0.3014 0.0554 -0.0418 -0.0603 464 VAL A N 3341 C CA . VAL A 471 ? 0.2232 0.2476 0.2742 0.0601 -0.0415 -0.0460 464 VAL A CA 3342 C C . VAL A 471 ? 0.2284 0.2517 0.2724 0.0458 -0.0440 -0.0528 464 VAL A C 3343 O O . VAL A 471 ? 0.2061 0.2557 0.2617 0.0366 -0.0398 -0.0494 464 VAL A O 3344 C CB . VAL A 471 ? 0.2251 0.2387 0.2750 0.0662 -0.0516 -0.0481 464 VAL A CB 3345 C CG1 . VAL A 471 ? 0.2048 0.2845 0.2239 0.0605 0.0148 -0.0212 464 VAL A CG1 3346 C CG2 . VAL A 471 ? 0.2678 0.2410 0.2844 0.0489 -0.0431 -0.0371 464 VAL A CG2 3347 N N . ASP A 472 ? 0.2240 0.2449 0.2644 0.0516 -0.0454 -0.0461 465 ASP A N 3348 C CA . ASP A 472 ? 0.2371 0.2611 0.2764 0.0474 -0.0342 -0.0492 465 ASP A CA 3349 C C . ASP A 472 ? 0.2311 0.2474 0.2573 0.0412 -0.0235 -0.0467 465 ASP A C 3350 O O . ASP A 472 ? 0.2126 0.2588 0.2654 0.0421 -0.0141 -0.0376 465 ASP A O 3351 C CB . ASP A 472 ? 0.2353 0.2533 0.2474 0.0469 -0.0301 -0.0614 465 ASP A CB 3352 C CG . ASP A 472 ? 0.2590 0.3176 0.3185 0.0515 -0.0314 -0.0722 465 ASP A CG 3353 O OD1 . ASP A 472 ? 0.2594 0.3284 0.3135 0.0845 -0.0364 -0.1208 465 ASP A OD1 3354 O OD2 . ASP A 472 ? 0.3285 0.3949 0.3549 0.0618 0.0042 -0.0823 465 ASP A OD2 3355 N N . CYS A 473 ? 0.2423 0.2346 0.2468 0.0379 -0.0240 -0.0379 466 CYS A N 3356 C CA . CYS A 473 ? 0.2395 0.2354 0.2557 0.0338 -0.0364 -0.0319 466 CYS A CA 3357 C C . CYS A 473 ? 0.2321 0.2319 0.2580 0.0419 -0.0389 -0.0275 466 CYS A C 3358 O O . CYS A 473 ? 0.2659 0.2352 0.2895 0.0517 -0.0354 -0.0218 466 CYS A O 3359 C CB . CYS A 473 ? 0.2341 0.2334 0.2424 0.0149 -0.0460 -0.0400 466 CYS A CB 3360 S SG . CYS A 473 ? 0.2668 0.2691 0.2594 0.0212 -0.0581 -0.0420 466 CYS A SG 3361 N N . THR A 474 ? 0.2412 0.2180 0.2297 0.0438 -0.0457 -0.0342 467 THR A N 3362 C CA . THR A 474 ? 0.2402 0.2121 0.2333 0.0380 -0.0425 -0.0253 467 THR A CA 3363 C C . THR A 474 ? 0.2318 0.2084 0.2323 0.0392 -0.0553 -0.0187 467 THR A C 3364 O O . THR A 474 ? 0.2146 0.2028 0.2541 0.0399 -0.0613 -0.0216 467 THR A O 3365 C CB . THR A 474 ? 0.2397 0.2053 0.2298 0.0424 -0.0342 -0.0180 467 THR A CB 3366 O OG1 . THR A 474 ? 0.2687 0.2191 0.2099 0.0253 -0.0475 -0.0261 467 THR A OG1 3367 C CG2 . THR A 474 ? 0.2377 0.1969 0.1557 0.0487 -0.0099 -0.0295 467 THR A CG2 3368 N N . PRO A 475 ? 0.2349 0.2083 0.2388 0.0306 -0.0597 -0.0168 468 PRO A N 3369 C CA . PRO A 475 ? 0.2361 0.2082 0.2265 0.0314 -0.0663 -0.0190 468 PRO A CA 3370 C C . PRO A 475 ? 0.2416 0.2233 0.2369 0.0319 -0.0690 -0.0212 468 PRO A C 3371 O O . PRO A 475 ? 0.2279 0.2211 0.2261 0.0158 -0.0721 -0.0271 468 PRO A O 3372 C CB . PRO A 475 ? 0.2513 0.2069 0.2357 0.0254 -0.0658 -0.0206 468 PRO A CB 3373 C CG . PRO A 475 ? 0.2291 0.1846 0.2226 0.0292 -0.0651 0.0143 468 PRO A CG 3374 C CD . PRO A 475 ? 0.2275 0.2070 0.2307 0.0306 -0.0736 -0.0109 468 PRO A CD 3375 N N . LEU A 476 ? 0.2350 0.2162 0.2398 0.0342 -0.0704 -0.0283 469 LEU A N 3376 C CA . LEU A 476 ? 0.2338 0.2349 0.2479 0.0525 -0.0765 -0.0336 469 LEU A CA 3377 C C . LEU A 476 ? 0.2505 0.2379 0.2488 0.0542 -0.0732 -0.0411 469 LEU A C 3378 O O . LEU A 476 ? 0.2626 0.2662 0.2616 0.0764 -0.0801 -0.0431 469 LEU A O 3379 C CB . LEU A 476 ? 0.2296 0.2249 0.2669 0.0473 -0.0707 -0.0297 469 LEU A CB 3380 C CG . LEU A 476 ? 0.2031 0.2140 0.2247 0.0564 -0.0899 -0.0352 469 LEU A CG 3381 C CD1 . LEU A 476 ? 0.2026 0.2317 0.2283 0.0266 -0.1009 -0.0367 469 LEU A CD1 3382 C CD2 . LEU A 476 ? 0.1997 0.2143 0.2083 0.0676 -0.0678 -0.0203 469 LEU A CD2 3383 N N . MET A 477 ? 0.2393 0.2334 0.2544 0.0531 -0.0693 -0.0507 470 MET A N 3384 C CA . MET A 477 ? 0.2612 0.2378 0.2424 0.0518 -0.0755 -0.0445 470 MET A CA 3385 C C . MET A 477 ? 0.2708 0.2424 0.2544 0.0483 -0.0762 -0.0494 470 MET A C 3386 O O . MET A 477 ? 0.2938 0.2155 0.2574 0.0449 -0.0682 -0.0419 470 MET A O 3387 C CB . MET A 477 ? 0.2580 0.2461 0.2477 0.0446 -0.0714 -0.0314 470 MET A CB 3388 C CG . MET A 477 ? 0.2656 0.2789 0.2861 0.0611 -0.0780 -0.0362 470 MET A CG 3389 S SD . MET A 477 ? 0.2995 0.2833 0.3176 0.0508 -0.0776 -0.0058 470 MET A SD 3390 C CE . MET A 477 ? 0.2641 0.2566 0.2827 0.0825 -0.0745 0.0052 470 MET A CE 3391 N N . TYR A 478 ? 0.2687 0.2424 0.2473 0.0458 -0.0718 -0.0510 471 TYR A N 3392 C CA . TYR A 478 ? 0.2714 0.2607 0.2682 0.0480 -0.0871 -0.0509 471 TYR A CA 3393 C C . TYR A 478 ? 0.2828 0.2675 0.2868 0.0561 -0.0826 -0.0519 471 TYR A C 3394 O O . TYR A 478 ? 0.2512 0.2618 0.3177 0.0491 -0.0891 -0.0474 471 TYR A O 3395 C CB . TYR A 478 ? 0.2703 0.2683 0.2587 0.0439 -0.0785 -0.0488 471 TYR A CB 3396 C CG . TYR A 478 ? 0.2389 0.2543 0.2613 0.0555 -0.0935 -0.0371 471 TYR A CG 3397 C CD1 . TYR A 478 ? 0.2296 0.2223 0.2627 0.0603 -0.0631 -0.0441 471 TYR A CD1 3398 C CD2 . TYR A 478 ? 0.2352 0.2262 0.2875 0.0609 -0.0739 -0.0399 471 TYR A CD2 3399 C CE1 . TYR A 478 ? 0.2390 0.2639 0.2659 0.0275 -0.0959 -0.0532 471 TYR A CE1 3400 C CE2 . TYR A 478 ? 0.2322 0.2195 0.2986 0.0484 -0.0868 -0.0474 471 TYR A CE2 3401 C CZ . TYR A 478 ? 0.2612 0.2463 0.2692 0.0542 -0.0769 -0.0553 471 TYR A CZ 3402 O OH . TYR A 478 ? 0.2657 0.2700 0.3032 0.0490 -0.0688 -0.0354 471 TYR A OH 3403 N N . SER A 479 ? 0.2951 0.2722 0.2829 0.0676 -0.0910 -0.0721 472 SER A N 3404 C CA . SER A 479 ? 0.3019 0.2769 0.2753 0.0855 -0.0940 -0.0691 472 SER A CA 3405 C C . SER A 479 ? 0.3071 0.2828 0.2736 0.0911 -0.0943 -0.0717 472 SER A C 3406 O O . SER A 479 ? 0.3259 0.3077 0.2716 0.0980 -0.0935 -0.0680 472 SER A O 3407 C CB . SER A 479 ? 0.3122 0.2746 0.2694 0.0768 -0.1052 -0.0795 472 SER A CB 3408 O OG A SER A 479 ? 0.3613 0.2917 0.2624 0.0892 -0.1047 -0.0840 472 SER A OG 3409 O OG B SER A 479 ? 0.2495 0.2814 0.2743 0.1044 -0.0819 -0.0578 472 SER A OG 3410 N N . LEU A 480 ? 0.3050 0.2703 0.2656 0.0909 -0.0894 -0.0805 473 LEU A N 3411 C CA . LEU A 480 ? 0.2941 0.2660 0.2573 0.0930 -0.0824 -0.0726 473 LEU A CA 3412 C C . LEU A 480 ? 0.3034 0.2696 0.2543 0.0870 -0.0813 -0.0786 473 LEU A C 3413 O O . LEU A 480 ? 0.3104 0.2602 0.2265 0.0788 -0.0581 -0.0802 473 LEU A O 3414 C CB . LEU A 480 ? 0.2994 0.2657 0.2560 0.0878 -0.0767 -0.0708 473 LEU A CB 3415 C CG . LEU A 480 ? 0.2823 0.2563 0.2558 0.0963 -0.0754 -0.0544 473 LEU A CG 3416 C CD1 . LEU A 480 ? 0.3544 0.2708 0.3062 0.0509 -0.0339 -0.0367 473 LEU A CD1 3417 C CD2 . LEU A 480 ? 0.2770 0.3183 0.3081 0.0416 -0.0414 -0.0620 473 LEU A CD2 3418 N N . VAL A 481 ? 0.2899 0.2696 0.2425 0.0823 -0.0718 -0.0833 474 VAL A N 3419 C CA . VAL A 481 ? 0.2818 0.2559 0.2493 0.0909 -0.0836 -0.0821 474 VAL A CA 3420 C C . VAL A 481 ? 0.3024 0.2707 0.2635 0.0908 -0.0862 -0.0764 474 VAL A C 3421 O O . VAL A 481 ? 0.2971 0.2703 0.2596 0.0837 -0.0779 -0.0726 474 VAL A O 3422 C CB . VAL A 481 ? 0.2771 0.2613 0.2509 0.1014 -0.0784 -0.0901 474 VAL A CB 3423 C CG1 . VAL A 481 ? 0.2721 0.2756 0.2522 0.1028 -0.0498 -0.0757 474 VAL A CG1 3424 C CG2 . VAL A 481 ? 0.3050 0.2450 0.2417 0.0911 -0.0855 -0.0877 474 VAL A CG2 3425 N N . HIS A 482 ? 0.3112 0.2831 0.2766 0.0836 -0.0955 -0.0660 475 HIS A N 3426 C CA . HIS A 482 ? 0.3313 0.2999 0.2873 0.0878 -0.1224 -0.0605 475 HIS A CA 3427 C C . HIS A 482 ? 0.3408 0.2963 0.2974 0.0906 -0.1200 -0.0538 475 HIS A C 3428 O O . HIS A 482 ? 0.3222 0.3038 0.2650 0.1015 -0.1332 -0.0516 475 HIS A O 3429 C CB . HIS A 482 ? 0.3227 0.3016 0.3108 0.0906 -0.1272 -0.0390 475 HIS A CB 3430 C CG . HIS A 482 ? 0.3793 0.3279 0.3720 0.0811 -0.0920 -0.0500 475 HIS A CG 3431 N ND1 . HIS A 482 ? 0.4782 0.3742 0.4417 0.0476 -0.0744 -0.0264 475 HIS A ND1 3432 C CD2 . HIS A 482 ? 0.3728 0.3665 0.3697 0.0564 -0.1118 -0.0610 475 HIS A CD2 3433 C CE1 . HIS A 482 ? 0.4534 0.3739 0.4438 0.0398 -0.0603 -0.0581 475 HIS A CE1 3434 N NE2 . HIS A 482 ? 0.3763 0.3279 0.4211 0.0133 -0.1009 -0.0819 475 HIS A NE2 3435 N N . ASN A 483 ? 0.3327 0.2925 0.2900 0.0920 -0.1171 -0.0628 476 ASN A N 3436 C CA . ASN A 483 ? 0.3566 0.2976 0.3052 0.0962 -0.1224 -0.0657 476 ASN A CA 3437 C C . ASN A 483 ? 0.3561 0.2979 0.3086 0.0991 -0.1232 -0.0663 476 ASN A C 3438 O O . ASN A 483 ? 0.3613 0.3030 0.3335 0.0975 -0.1158 -0.0738 476 ASN A O 3439 C CB . ASN A 483 ? 0.3634 0.2886 0.2872 0.0926 -0.1238 -0.0850 476 ASN A CB 3440 C CG . ASN A 483 ? 0.3781 0.3114 0.3211 0.0850 -0.1240 -0.0654 476 ASN A CG 3441 O OD1 . ASN A 483 ? 0.3641 0.2559 0.3181 0.0497 -0.1290 -0.0943 476 ASN A OD1 3442 N ND2 . ASN A 483 ? 0.4172 0.3460 0.3548 0.0933 -0.1185 -0.0834 476 ASN A ND2 3443 N N . LEU A 484 ? 0.3526 0.2921 0.3152 0.0924 -0.1179 -0.0706 477 LEU A N 3444 C CA . LEU A 484 ? 0.3506 0.2996 0.3145 0.0940 -0.1231 -0.0605 477 LEU A CA 3445 C C . LEU A 484 ? 0.3465 0.3054 0.3213 0.0929 -0.1310 -0.0608 477 LEU A C 3446 O O . LEU A 484 ? 0.3351 0.3200 0.3266 0.0940 -0.1374 -0.0622 477 LEU A O 3447 C CB . LEU A 484 ? 0.3482 0.2983 0.2912 0.0745 -0.1219 -0.0589 477 LEU A CB 3448 C CG . LEU A 484 ? 0.3443 0.2860 0.2875 0.1040 -0.1199 -0.0446 477 LEU A CG 3449 C CD1 . LEU A 484 ? 0.3239 0.2634 0.3153 0.0895 -0.1337 -0.0045 477 LEU A CD1 3450 C CD2 . LEU A 484 ? 0.3583 0.2565 0.2678 0.0861 -0.1127 -0.0317 477 LEU A CD2 3451 N N . THR A 485 ? 0.3551 0.3134 0.3332 0.0985 -0.1298 -0.0665 478 THR A N 3452 C CA . THR A 485 ? 0.3611 0.3134 0.3447 0.1107 -0.1279 -0.0655 478 THR A CA 3453 C C . THR A 485 ? 0.3846 0.3318 0.3529 0.1134 -0.1308 -0.0649 478 THR A C 3454 O O . THR A 485 ? 0.3976 0.3195 0.3392 0.1205 -0.1347 -0.0473 478 THR A O 3455 C CB . THR A 485 ? 0.3537 0.3083 0.3455 0.1042 -0.1260 -0.0711 478 THR A CB 3456 O OG1 . THR A 485 ? 0.3187 0.2811 0.3505 0.1266 -0.0873 -0.0863 478 THR A OG1 3457 C CG2 . THR A 485 ? 0.2881 0.2767 0.3307 0.0985 -0.1255 -0.0669 478 THR A CG2 3458 N N . LYS A 486 ? 0.4187 0.3429 0.3801 0.1165 -0.1449 -0.0648 479 LYS A N 3459 C CA . LYS A 486 ? 0.4409 0.3609 0.3960 0.1219 -0.1513 -0.0770 479 LYS A CA 3460 C C . LYS A 486 ? 0.4453 0.3543 0.3826 0.1348 -0.1567 -0.0793 479 LYS A C 3461 O O . LYS A 486 ? 0.4504 0.3735 0.3766 0.1270 -0.1668 -0.0864 479 LYS A O 3462 C CB . LYS A 486 ? 0.4470 0.3538 0.4142 0.1162 -0.1498 -0.0761 479 LYS A CB 3463 C CG . LYS A 486 ? 0.4468 0.3627 0.4451 0.1211 -0.1453 -0.0838 479 LYS A CG 3464 C CD . LYS A 486 ? 0.4679 0.3814 0.4959 0.0963 -0.1410 -0.0933 479 LYS A CD 3465 C CE . LYS A 486 ? 0.4720 0.3816 0.4677 0.1149 -0.1450 -0.1092 479 LYS A CE 3466 N NZ . LYS A 486 ? 0.4428 0.4036 0.4847 0.1031 -0.1086 -0.1595 479 LYS A NZ 3467 N N . GLU A 487 ? 0.4475 0.3549 0.3700 0.1382 -0.1486 -0.0855 480 GLU A N 3468 C CA . GLU A 487 ? 0.4617 0.3619 0.3724 0.1446 -0.1527 -0.0746 480 GLU A CA 3469 C C . GLU A 487 ? 0.4585 0.3749 0.3685 0.1362 -0.1526 -0.0583 480 GLU A C 3470 O O . GLU A 487 ? 0.4822 0.3884 0.3628 0.1437 -0.1643 -0.0341 480 GLU A O 3471 C CB . GLU A 487 ? 0.4709 0.3739 0.3639 0.1319 -0.1434 -0.0844 480 GLU A CB 3472 C CG . GLU A 487 ? 0.4954 0.3741 0.3928 0.1611 -0.1529 -0.0615 480 GLU A CG 3473 C CD . GLU A 487 ? 0.4913 0.3753 0.3520 0.1618 -0.1410 -0.0821 480 GLU A CD 3474 O OE1 . GLU A 487 ? 0.4827 0.3488 0.3391 0.1812 -0.1372 -0.0973 480 GLU A OE1 3475 O OE2 . GLU A 487 ? 0.4916 0.3682 0.3418 0.1647 -0.1462 -0.0820 480 GLU A OE2 3476 N N . LEU A 488 ? 0.4315 0.3652 0.3341 0.1369 -0.1632 -0.0640 481 LEU A N 3477 C CA . LEU A 488 ? 0.4077 0.3591 0.3401 0.1382 -0.1643 -0.0505 481 LEU A CA 3478 C C . LEU A 488 ? 0.4010 0.3651 0.3477 0.1391 -0.1673 -0.0558 481 LEU A C 3479 O O . LEU A 488 ? 0.4031 0.3585 0.3437 0.1356 -0.1775 -0.0586 481 LEU A O 3480 C CB . LEU A 488 ? 0.3766 0.3498 0.3142 0.1384 -0.1677 -0.0583 481 LEU A CB 3481 C CG . LEU A 488 ? 0.3753 0.3403 0.2826 0.1314 -0.1609 -0.0400 481 LEU A CG 3482 C CD1 . LEU A 488 ? 0.2862 0.2521 0.2447 0.1465 -0.1860 -0.0041 481 LEU A CD1 3483 C CD2 . LEU A 488 ? 0.3181 0.3442 0.3152 0.1296 -0.1326 -0.0505 481 LEU A CD2 3484 N N . LYS A 489 ? 0.4006 0.3679 0.3625 0.1389 -0.1659 -0.0540 482 LYS A N 3485 C CA . LYS A 489 ? 0.4077 0.3819 0.3791 0.1397 -0.1545 -0.0578 482 LYS A CA 3486 C C . LYS A 489 ? 0.3998 0.3785 0.3885 0.1298 -0.1461 -0.0618 482 LYS A C 3487 O O . LYS A 489 ? 0.4106 0.3905 0.3547 0.1251 -0.1404 -0.0677 482 LYS A O 3488 C CB . LYS A 489 ? 0.4027 0.3798 0.3888 0.1390 -0.1667 -0.0514 482 LYS A CB 3489 C CG . LYS A 489 ? 0.4601 0.4555 0.4393 0.1515 -0.1506 -0.0164 482 LYS A CG 3490 C CD . LYS A 489 ? 0.5851 0.5326 0.5664 0.1505 -0.1788 0.0392 482 LYS A CD 3491 C CE . LYS A 489 ? 0.6271 0.6073 0.6187 0.1277 -0.1824 0.0547 482 LYS A CE 3492 N NZ . LYS A 489 ? 0.6854 0.6346 0.5855 0.1365 -0.2067 0.0684 482 LYS A NZ 3493 N N . SER A 490 ? 0.3796 0.3658 0.4025 0.1395 -0.1354 -0.0670 483 SER A N 3494 C CA . SER A 490 ? 0.3670 0.3626 0.4252 0.1306 -0.1318 -0.0625 483 SER A CA 3495 C C . SER A 490 ? 0.3507 0.3506 0.4226 0.1369 -0.1246 -0.0661 483 SER A C 3496 O O . SER A 490 ? 0.3504 0.3536 0.4094 0.1425 -0.1194 -0.0677 483 SER A O 3497 C CB . SER A 490 ? 0.3632 0.3602 0.4266 0.1386 -0.1301 -0.0527 483 SER A CB 3498 O OG . SER A 490 ? 0.3341 0.3535 0.4577 0.1311 -0.1282 -0.0604 483 SER A OG 3499 N N . PRO A 491 ? 0.3361 0.3409 0.4329 0.1308 -0.1224 -0.0675 484 PRO A N 3500 C CA . PRO A 491 ? 0.3324 0.3371 0.4427 0.1351 -0.1181 -0.0752 484 PRO A CA 3501 C C . PRO A 491 ? 0.3404 0.3510 0.4675 0.1349 -0.1203 -0.0689 484 PRO A C 3502 O O . PRO A 491 ? 0.3478 0.3332 0.4538 0.1333 -0.1180 -0.0806 484 PRO A O 3503 C CB . PRO A 491 ? 0.2967 0.3183 0.4115 0.1457 -0.1171 -0.0787 484 PRO A CB 3504 C CG . PRO A 491 ? 0.3311 0.3248 0.4253 0.1225 -0.0979 -0.0866 484 PRO A CG 3505 C CD . PRO A 491 ? 0.3318 0.3419 0.4302 0.1200 -0.1233 -0.0709 484 PRO A CD 3506 N N . ASP A 492 ? 0.3462 0.3592 0.4920 0.1335 -0.1299 -0.0634 485 ASP A N 3507 C CA . ASP A 492 ? 0.3507 0.3740 0.5037 0.1318 -0.1316 -0.0718 485 ASP A CA 3508 C C . ASP A 492 ? 0.3622 0.3879 0.5232 0.1336 -0.1386 -0.0796 485 ASP A C 3509 O O . ASP A 492 ? 0.3628 0.3964 0.5165 0.1452 -0.1429 -0.0846 485 ASP A O 3510 C CB . ASP A 492 ? 0.3466 0.3658 0.4986 0.1295 -0.1298 -0.0703 485 ASP A CB 3511 C CG . ASP A 492 ? 0.3617 0.3546 0.4986 0.1048 -0.1216 -0.0663 485 ASP A CG 3512 O OD1 . ASP A 492 ? 0.3769 0.3644 0.5047 0.0893 -0.1396 -0.0758 485 ASP A OD1 3513 O OD2 . ASP A 492 ? 0.3581 0.3136 0.4966 0.0664 -0.0833 -0.0834 485 ASP A OD2 3514 N N . GLU A 493 ? 0.3644 0.3940 0.5391 0.1319 -0.1371 -0.0952 486 GLU A N 3515 C CA . GLU A 493 ? 0.3776 0.4047 0.5661 0.1318 -0.1310 -0.1052 486 GLU A CA 3516 C C . GLU A 493 ? 0.3753 0.4129 0.5679 0.1356 -0.1412 -0.1078 486 GLU A C 3517 O O . GLU A 493 ? 0.3812 0.4212 0.5669 0.1251 -0.1384 -0.1106 486 GLU A O 3518 C CB . GLU A 493 ? 0.3857 0.3975 0.5696 0.1279 -0.1162 -0.1176 486 GLU A CB 3519 C CG . GLU A 493 ? 0.3578 0.3870 0.5628 0.1405 -0.1049 -0.1276 486 GLU A CG 3520 C CD . GLU A 493 ? 0.3429 0.3604 0.5407 0.1451 -0.1008 -0.1375 486 GLU A CD 3521 O OE1 . GLU A 493 ? 0.3172 0.3537 0.5214 0.1405 -0.0871 -0.1644 486 GLU A OE1 3522 O OE2 . GLU A 493 ? 0.3076 0.2912 0.5286 0.1995 -0.1044 -0.1564 486 GLU A OE2 3523 N N . GLY A 494 ? 0.3799 0.4299 0.5751 0.1392 -0.1465 -0.1058 487 GLY A N 3524 C CA . GLY A 494 ? 0.3812 0.4383 0.5763 0.1345 -0.1648 -0.1020 487 GLY A CA 3525 C C . GLY A 494 ? 0.3915 0.4488 0.5768 0.1336 -0.1733 -0.0991 487 GLY A C 3526 O O . GLY A 494 ? 0.3657 0.4654 0.5783 0.1213 -0.1695 -0.1056 487 GLY A O 3527 N N . PHE A 495 ? 0.3946 0.4521 0.5718 0.1368 -0.1876 -0.0929 488 PHE A N 3528 C CA . PHE A 495 ? 0.4184 0.4495 0.5713 0.1468 -0.1974 -0.0884 488 PHE A CA 3529 C C . PHE A 495 ? 0.4453 0.4550 0.5636 0.1462 -0.2025 -0.0902 488 PHE A C 3530 O O . PHE A 495 ? 0.4618 0.4441 0.5596 0.1443 -0.1954 -0.0969 488 PHE A O 3531 C CB . PHE A 495 ? 0.4101 0.4522 0.5648 0.1423 -0.2004 -0.0873 488 PHE A CB 3532 C CG . PHE A 495 ? 0.4161 0.4423 0.5651 0.1396 -0.2104 -0.0807 488 PHE A CG 3533 C CD1 . PHE A 495 ? 0.4346 0.4587 0.5728 0.1256 -0.2025 -0.0928 488 PHE A CD1 3534 C CD2 . PHE A 495 ? 0.4265 0.4436 0.5695 0.1171 -0.2074 -0.0874 488 PHE A CD2 3535 C CE1 . PHE A 495 ? 0.4231 0.4455 0.5900 0.1106 -0.1811 -0.0985 488 PHE A CE1 3536 C CE2 . PHE A 495 ? 0.4322 0.4602 0.5723 0.1000 -0.2009 -0.1005 488 PHE A CE2 3537 C CZ . PHE A 495 ? 0.4129 0.4604 0.5967 0.0912 -0.1731 -0.1034 488 PHE A CZ 3538 N N . GLU A 496 ? 0.4691 0.4582 0.5623 0.1527 -0.2094 -0.0870 489 GLU A N 3539 C CA . GLU A 496 ? 0.5003 0.4761 0.5764 0.1546 -0.2081 -0.0777 489 GLU A CA 3540 C C . GLU A 496 ? 0.4989 0.4791 0.5604 0.1548 -0.2157 -0.0775 489 GLU A C 3541 O O . GLU A 496 ? 0.5017 0.4856 0.5392 0.1400 -0.2218 -0.0803 489 GLU A O 3542 C CB . GLU A 496 ? 0.4961 0.4945 0.5846 0.1668 -0.2161 -0.0597 489 GLU A CB 3543 C CG . GLU A 496 ? 0.5392 0.5254 0.6120 0.1731 -0.2084 -0.0357 489 GLU A CG 3544 C CD . GLU A 496 ? 0.5669 0.5624 0.6225 0.1679 -0.2302 -0.0070 489 GLU A CD 3545 O OE1 . GLU A 496 ? 0.5453 0.5637 0.6294 0.1642 -0.2447 0.0176 489 GLU A OE1 3546 O OE2 . GLU A 496 ? 0.5845 0.5768 0.6260 0.1844 -0.2164 0.0263 489 GLU A OE2 3547 N N . GLY A 497 ? 0.4977 0.4616 0.5531 0.1616 -0.2141 -0.0819 490 GLY A N 3548 C CA . GLY A 497 ? 0.4968 0.4631 0.5572 0.1681 -0.2116 -0.0833 490 GLY A CA 3549 C C . GLY A 497 ? 0.4917 0.4596 0.5526 0.1609 -0.2065 -0.0916 490 GLY A C 3550 O O . GLY A 497 ? 0.5031 0.4605 0.5659 0.1752 -0.1920 -0.0981 490 GLY A O 3551 N N . LYS A 498 ? 0.4630 0.4413 0.5287 0.1613 -0.2116 -0.0885 491 LYS A N 3552 C CA . LYS A 498 ? 0.4356 0.4335 0.5154 0.1489 -0.2125 -0.0897 491 LYS A CA 3553 C C . LYS A 498 ? 0.4191 0.4134 0.4871 0.1447 -0.2057 -0.0872 491 LYS A C 3554 O O . LYS A 498 ? 0.4021 0.4172 0.4824 0.1358 -0.2042 -0.0803 491 LYS A O 3555 C CB . LYS A 498 ? 0.4350 0.4284 0.5199 0.1545 -0.2111 -0.0914 491 LYS A CB 3556 C CG . LYS A 498 ? 0.4326 0.4718 0.5417 0.1428 -0.2214 -0.0893 491 LYS A CG 3557 C CD . LYS A 498 ? 0.4262 0.4848 0.6053 0.1328 -0.2276 -0.1057 491 LYS A CD 3558 C CE . LYS A 498 ? 0.4101 0.5399 0.6420 0.1230 -0.2136 -0.0977 491 LYS A CE 3559 N NZ . LYS A 498 ? 0.3499 0.5539 0.6811 0.1195 -0.2002 -0.1049 491 LYS A NZ 3560 N N . SER A 499 ? 0.3930 0.3885 0.4525 0.1356 -0.1978 -0.0863 492 SER A N 3561 C CA . SER A 499 ? 0.3836 0.3638 0.4265 0.1299 -0.1803 -0.0865 492 SER A CA 3562 C C . SER A 499 ? 0.3646 0.3493 0.4138 0.1251 -0.1747 -0.0922 492 SER A C 3563 O O . SER A 499 ? 0.3729 0.3470 0.3917 0.1236 -0.1717 -0.0949 492 SER A O 3564 C CB . SER A 499 ? 0.3729 0.3642 0.4244 0.1306 -0.1744 -0.0867 492 SER A CB 3565 O OG . SER A 499 ? 0.3748 0.3355 0.4347 0.1199 -0.1740 -0.0820 492 SER A OG 3566 N N . LEU A 500 ? 0.3485 0.3346 0.3994 0.1193 -0.1638 -0.0976 493 LEU A N 3567 C CA . LEU A 500 ? 0.3252 0.3280 0.3916 0.1040 -0.1594 -0.0876 493 LEU A CA 3568 C C . LEU A 500 ? 0.3249 0.3282 0.3945 0.0931 -0.1549 -0.0935 493 LEU A C 3569 O O . LEU A 500 ? 0.3203 0.3268 0.3813 0.0762 -0.1555 -0.1004 493 LEU A O 3570 C CB . LEU A 500 ? 0.3227 0.3263 0.3849 0.0941 -0.1551 -0.0986 493 LEU A CB 3571 C CG . LEU A 500 ? 0.2810 0.3176 0.3788 0.1085 -0.1379 -0.0993 493 LEU A CG 3572 C CD1 . LEU A 500 ? 0.3002 0.2891 0.3835 0.0900 -0.0917 -0.1035 493 LEU A CD1 3573 C CD2 . LEU A 500 ? 0.2596 0.2884 0.3153 0.0938 -0.1692 -0.1401 493 LEU A CD2 3574 N N . TYR A 501 ? 0.3205 0.3072 0.3733 0.0798 -0.1595 -0.1133 494 TYR A N 3575 C CA . TYR A 501 ? 0.3234 0.3180 0.3900 0.0896 -0.1525 -0.1147 494 TYR A CA 3576 C C . TYR A 501 ? 0.3250 0.3252 0.4079 0.0869 -0.1576 -0.1190 494 TYR A C 3577 O O . TYR A 501 ? 0.3299 0.3282 0.4005 0.0762 -0.1511 -0.1326 494 TYR A O 3578 C CB . TYR A 501 ? 0.3199 0.3091 0.3871 0.0887 -0.1556 -0.1076 494 TYR A CB 3579 C CG . TYR A 501 ? 0.3260 0.3124 0.3774 0.0847 -0.1413 -0.1121 494 TYR A CG 3580 C CD1 . TYR A 501 ? 0.2933 0.3077 0.3690 0.1074 -0.1083 -0.1110 494 TYR A CD1 3581 C CD2 . TYR A 501 ? 0.3467 0.3323 0.3947 0.0717 -0.1034 -0.0909 494 TYR A CD2 3582 C CE1 . TYR A 501 ? 0.3067 0.3296 0.4065 0.0740 -0.0874 -0.1102 494 TYR A CE1 3583 C CE2 . TYR A 501 ? 0.3314 0.3112 0.4262 0.0819 -0.0841 -0.0868 494 TYR A CE2 3584 C CZ . TYR A 501 ? 0.3339 0.2926 0.4014 0.0629 -0.0980 -0.0909 494 TYR A CZ 3585 O OH . TYR A 501 ? 0.3614 0.2521 0.4272 0.0941 -0.0748 -0.1035 494 TYR A OH 3586 N N . GLU A 502 ? 0.3258 0.3330 0.4257 0.0959 -0.1596 -0.1159 495 GLU A N 3587 C CA . GLU A 502 ? 0.3308 0.3638 0.4564 0.0960 -0.1646 -0.1098 495 GLU A CA 3588 C C . GLU A 502 ? 0.3254 0.3577 0.4562 0.0926 -0.1542 -0.1046 495 GLU A C 3589 O O . GLU A 502 ? 0.3089 0.3479 0.4699 0.0857 -0.1439 -0.1154 495 GLU A O 3590 C CB . GLU A 502 ? 0.3432 0.3893 0.4637 0.0939 -0.1684 -0.1065 495 GLU A CB 3591 C CG . GLU A 502 ? 0.3587 0.4393 0.5142 0.1080 -0.1972 -0.1020 495 GLU A CG 3592 C CD . GLU A 502 ? 0.4119 0.5479 0.5788 0.1116 -0.2278 -0.1361 495 GLU A CD 3593 O OE1 . GLU A 502 ? 0.4741 0.5983 0.5926 0.0943 -0.2217 -0.1745 495 GLU A OE1 3594 O OE2 . GLU A 502 ? 0.4016 0.6241 0.6183 0.1539 -0.2544 -0.1235 495 GLU A OE2 3595 N N . SER A 503 ? 0.3145 0.3459 0.4494 0.0864 -0.1481 -0.1007 496 SER A N 3596 C CA . SER A 503 ? 0.3002 0.3467 0.4595 0.0803 -0.1436 -0.0960 496 SER A CA 3597 C C . SER A 503 ? 0.3032 0.3502 0.4598 0.0760 -0.1331 -0.0923 496 SER A C 3598 O O . SER A 503 ? 0.3091 0.3630 0.4804 0.0712 -0.1221 -0.0939 496 SER A O 3599 C CB . SER A 503 ? 0.2960 0.3476 0.4502 0.0863 -0.1379 -0.0966 496 SER A CB 3600 O OG . SER A 503 ? 0.3040 0.3509 0.4610 0.0657 -0.1575 -0.1092 496 SER A OG 3601 N N . TRP A 504 ? 0.2905 0.3245 0.4506 0.0857 -0.1308 -0.0861 497 TRP A N 3602 C CA . TRP A 504 ? 0.2833 0.3234 0.4397 0.0705 -0.1249 -0.0848 497 TRP A CA 3603 C C . TRP A 504 ? 0.2884 0.3261 0.4494 0.0712 -0.1261 -0.0884 497 TRP A C 3604 O O . TRP A 504 ? 0.3013 0.3277 0.4517 0.0629 -0.1199 -0.0952 497 TRP A O 3605 C CB . TRP A 504 ? 0.2730 0.3216 0.4290 0.0735 -0.1257 -0.0740 497 TRP A CB 3606 C CG . TRP A 504 ? 0.2631 0.2980 0.4133 0.0580 -0.1003 -0.0628 497 TRP A CG 3607 C CD1 . TRP A 504 ? 0.2378 0.2573 0.3863 -0.0008 -0.0930 -0.0216 497 TRP A CD1 3608 C CD2 . TRP A 504 ? 0.2844 0.2883 0.4071 0.0510 -0.0829 -0.0521 497 TRP A CD2 3609 N NE1 . TRP A 504 ? 0.2339 0.2642 0.4076 0.0088 -0.0678 -0.0487 497 TRP A NE1 3610 C CE2 . TRP A 504 ? 0.2682 0.2697 0.3934 0.0312 -0.0765 -0.0481 497 TRP A CE2 3611 C CE3 . TRP A 504 ? 0.2511 0.2822 0.3904 0.0468 -0.0669 -0.0295 497 TRP A CE3 3612 C CZ2 . TRP A 504 ? 0.2349 0.2867 0.3806 0.0335 -0.0738 -0.0510 497 TRP A CZ2 3613 C CZ3 . TRP A 504 ? 0.2653 0.2718 0.3807 0.0615 -0.0502 -0.0466 497 TRP A CZ3 3614 C CH2 . TRP A 504 ? 0.2417 0.2940 0.3915 0.0478 -0.0800 -0.0436 497 TRP A CH2 3615 N N . THR A 505 ? 0.2660 0.3226 0.4483 0.0682 -0.1264 -0.0980 498 THR A N 3616 C CA . THR A 505 ? 0.2773 0.3242 0.4726 0.0662 -0.1288 -0.1086 498 THR A CA 3617 C C . THR A 505 ? 0.3011 0.3505 0.4962 0.0632 -0.1218 -0.1040 498 THR A C 3618 O O . THR A 505 ? 0.3139 0.3655 0.5039 0.0560 -0.1043 -0.1060 498 THR A O 3619 C CB . THR A 505 ? 0.2792 0.3196 0.4682 0.0677 -0.1250 -0.1077 498 THR A CB 3620 O OG1 A THR A 505 ? 0.2502 0.2562 0.4334 0.0675 -0.1434 -0.1419 498 THR A OG1 3621 C CG2 A THR A 505 ? 0.2724 0.3109 0.4702 0.0596 -0.1347 -0.1186 498 THR A CG2 3622 N N . LYS A 506 ? 0.2927 0.3575 0.5180 0.0659 -0.1350 -0.1092 499 LYS A N 3623 C CA . LYS A 506 ? 0.3146 0.3817 0.5475 0.0661 -0.1270 -0.0964 499 LYS A CA 3624 C C . LYS A 506 ? 0.3224 0.3917 0.5588 0.0652 -0.1209 -0.0864 499 LYS A C 3625 O O . LYS A 506 ? 0.3546 0.4030 0.5724 0.0539 -0.1181 -0.0826 499 LYS A O 3626 C CB . LYS A 506 ? 0.3090 0.3924 0.5584 0.0618 -0.1319 -0.0915 499 LYS A CB 3627 C CG . LYS A 506 ? 0.3359 0.4395 0.5973 0.0972 -0.1225 -0.0743 499 LYS A CG 3628 C CD . LYS A 506 ? 0.3027 0.4167 0.6155 0.1039 -0.1298 -0.0776 499 LYS A CD 3629 C CE . LYS A 506 ? 0.2785 0.4103 0.6181 0.1079 -0.1491 -0.0743 499 LYS A CE 3630 N NZ . LYS A 506 ? 0.1950 0.4052 0.6162 0.1316 -0.1539 -0.0683 499 LYS A NZ 3631 N N . LYS A 507 ? 0.3335 0.3731 0.5528 0.0645 -0.1167 -0.0877 500 LYS A N 3632 C CA . LYS A 507 ? 0.3305 0.3864 0.5588 0.0646 -0.1026 -0.0844 500 LYS A CA 3633 C C . LYS A 507 ? 0.3189 0.3897 0.5570 0.0574 -0.0978 -0.0860 500 LYS A C 3634 O O . LYS A 507 ? 0.3118 0.3963 0.5614 0.0717 -0.0727 -0.0868 500 LYS A O 3635 C CB . LYS A 507 ? 0.3258 0.3698 0.5546 0.0627 -0.1066 -0.0941 500 LYS A CB 3636 C CG . LYS A 507 ? 0.3615 0.3835 0.5493 0.0670 -0.0938 -0.0869 500 LYS A CG 3637 C CD . LYS A 507 ? 0.3685 0.3531 0.5180 0.0763 -0.0740 -0.1034 500 LYS A CD 3638 C CE . LYS A 507 ? 0.3805 0.3973 0.5473 0.0758 -0.0959 -0.0870 500 LYS A CE 3639 N NZ . LYS A 507 ? 0.3813 0.3891 0.5226 0.0789 -0.1082 -0.0914 500 LYS A NZ 3640 N N . SER A 508 ? 0.3087 0.3880 0.5587 0.0521 -0.0913 -0.0827 501 SER A N 3641 C CA . SER A 508 ? 0.3101 0.3921 0.5641 0.0426 -0.0893 -0.0794 501 SER A CA 3642 C C . SER A 508 ? 0.3187 0.4013 0.5784 0.0355 -0.0879 -0.0811 501 SER A C 3643 O O . SER A 508 ? 0.2989 0.3808 0.5578 0.0274 -0.0908 -0.0796 501 SER A O 3644 C CB . SER A 508 ? 0.3138 0.3941 0.5505 0.0440 -0.1007 -0.0824 501 SER A CB 3645 O OG . SER A 508 ? 0.3033 0.3825 0.5497 0.0554 -0.0960 -0.0571 501 SER A OG 3646 N N . PRO A 509 ? 0.3265 0.4128 0.6038 0.0248 -0.0828 -0.0840 502 PRO A N 3647 C CA . PRO A 509 ? 0.3319 0.4182 0.6199 0.0233 -0.0776 -0.0859 502 PRO A CA 3648 C C . PRO A 509 ? 0.3324 0.4275 0.6321 0.0150 -0.0810 -0.0811 502 PRO A C 3649 O O . PRO A 509 ? 0.3009 0.4136 0.6341 0.0144 -0.0755 -0.0874 502 PRO A O 3650 C CB . PRO A 509 ? 0.3326 0.4151 0.6205 0.0239 -0.0757 -0.0897 502 PRO A CB 3651 C CG . PRO A 509 ? 0.3339 0.4261 0.6240 0.0186 -0.0712 -0.0941 502 PRO A CG 3652 C CD . PRO A 509 ? 0.3276 0.4089 0.6062 0.0305 -0.0715 -0.0907 502 PRO A CD 3653 N N . SER A 510 ? 0.3615 0.4495 0.6566 0.0139 -0.0771 -0.0813 503 SER A N 3654 C CA . SER A 510 ? 0.4212 0.4841 0.6925 0.0222 -0.0707 -0.0746 503 SER A CA 3655 C C . SER A 510 ? 0.4500 0.5058 0.7171 0.0165 -0.0732 -0.0727 503 SER A C 3656 O O . SER A 510 ? 0.4513 0.4972 0.7164 0.0069 -0.0717 -0.0669 503 SER A O 3657 C CB . SER A 510 ? 0.4232 0.4799 0.6953 0.0266 -0.0672 -0.0755 503 SER A CB 3658 O OG . SER A 510 ? 0.4407 0.4910 0.7165 0.0487 -0.0405 -0.0694 503 SER A OG 3659 N N . PRO A 511 ? 0.4801 0.5319 0.7310 0.0157 -0.0815 -0.0711 504 PRO A N 3660 C CA . PRO A 511 ? 0.5084 0.5663 0.7587 0.0086 -0.0795 -0.0721 504 PRO A CA 3661 C C . PRO A 511 ? 0.5404 0.5886 0.7868 0.0070 -0.0820 -0.0746 504 PRO A C 3662 O O . PRO A 511 ? 0.5559 0.5912 0.7891 -0.0028 -0.0740 -0.0719 504 PRO A O 3663 C CB . PRO A 511 ? 0.5042 0.5640 0.7525 0.0025 -0.0798 -0.0703 504 PRO A CB 3664 C CG . PRO A 511 ? 0.4930 0.5635 0.7413 0.0180 -0.0886 -0.0672 504 PRO A CG 3665 C CD . PRO A 511 ? 0.4822 0.5345 0.7398 0.0170 -0.0752 -0.0708 504 PRO A CD 3666 N N . GLU A 512 ? 0.5697 0.6178 0.8101 0.0106 -0.0858 -0.0763 505 GLU A N 3667 C CA . GLU A 512 ? 0.5938 0.6413 0.8257 0.0073 -0.1001 -0.0802 505 GLU A CA 3668 C C . GLU A 512 ? 0.5985 0.6396 0.8276 0.0072 -0.1077 -0.0815 505 GLU A C 3669 O O . GLU A 512 ? 0.6205 0.6464 0.8290 -0.0025 -0.1147 -0.0763 505 GLU A O 3670 C CB . GLU A 512 ? 0.5933 0.6557 0.8348 0.0070 -0.0956 -0.0779 505 GLU A CB 3671 C CG . GLU A 512 ? 0.6212 0.7139 0.8502 0.0018 -0.0971 -0.0602 505 GLU A CG 3672 C CD . GLU A 512 ? 0.6850 0.7478 0.8791 -0.0056 -0.0758 -0.0458 505 GLU A CD 3673 O OE1 . GLU A 512 ? 0.7345 0.8175 0.8809 0.0081 -0.0696 -0.0441 505 GLU A OE1 3674 O OE2 . GLU A 512 ? 0.6945 0.7582 0.8784 -0.0014 -0.0716 -0.0302 505 GLU A OE2 3675 N N . PHE A 513 ? 0.5907 0.6286 0.8228 0.0155 -0.1164 -0.0858 506 PHE A N 3676 C CA . PHE A 513 ? 0.5754 0.6197 0.8217 0.0224 -0.1248 -0.0874 506 PHE A CA 3677 C C . PHE A 513 ? 0.5737 0.6279 0.8217 0.0197 -0.1348 -0.0907 506 PHE A C 3678 O O . PHE A 513 ? 0.5793 0.6173 0.8137 0.0335 -0.1407 -0.0964 506 PHE A O 3679 C CB . PHE A 513 ? 0.5848 0.6224 0.8136 0.0211 -0.1208 -0.0882 506 PHE A CB 3680 C CG . PHE A 513 ? 0.5476 0.6014 0.7901 0.0224 -0.1159 -0.0919 506 PHE A CG 3681 C CD1 . PHE A 513 ? 0.5324 0.5867 0.7538 0.0242 -0.1101 -0.0896 506 PHE A CD1 3682 C CD2 . PHE A 513 ? 0.5283 0.5900 0.7686 0.0244 -0.1134 -0.0910 506 PHE A CD2 3683 C CE1 . PHE A 513 ? 0.5121 0.5745 0.7456 0.0197 -0.1117 -0.0944 506 PHE A CE1 3684 C CE2 . PHE A 513 ? 0.5256 0.5720 0.7588 0.0189 -0.1103 -0.0957 506 PHE A CE2 3685 C CZ . PHE A 513 ? 0.5110 0.5743 0.7454 0.0271 -0.1104 -0.0930 506 PHE A CZ 3686 N N . SER A 514 ? 0.5733 0.6294 0.8246 0.0249 -0.1399 -0.0898 507 SER A N 3687 C CA . SER A 514 ? 0.5579 0.6263 0.8296 0.0299 -0.1383 -0.0930 507 SER A CA 3688 C C . SER A 514 ? 0.5367 0.5978 0.8092 0.0360 -0.1434 -0.0972 507 SER A C 3689 O O . SER A 514 ? 0.5564 0.6013 0.8143 0.0410 -0.1326 -0.0980 507 SER A O 3690 C CB . SER A 514 ? 0.5623 0.6335 0.8404 0.0211 -0.1392 -0.0967 507 SER A CB 3691 O OG . SER A 514 ? 0.5730 0.6832 0.8748 0.0072 -0.1136 -0.1071 507 SER A OG 3692 N N . GLY A 515 ? 0.4970 0.5553 0.7696 0.0300 -0.1480 -0.1071 508 GLY A N 3693 C CA . GLY A 515 ? 0.4600 0.5068 0.7126 0.0400 -0.1562 -0.1191 508 GLY A CA 3694 C C . GLY A 515 ? 0.4329 0.4758 0.6729 0.0498 -0.1510 -0.1187 508 GLY A C 3695 O O . GLY A 515 ? 0.4145 0.4617 0.6592 0.0550 -0.1686 -0.1231 508 GLY A O 3696 N N . MET A 516 ? 0.4193 0.4449 0.6318 0.0482 -0.1375 -0.1199 509 MET A N 3697 C CA . MET A 516 ? 0.4098 0.4408 0.6036 0.0395 -0.1211 -0.1135 509 MET A CA 3698 C C . MET A 516 ? 0.3806 0.4177 0.5752 0.0387 -0.1173 -0.1031 509 MET A C 3699 O O . MET A 516 ? 0.3851 0.4111 0.5834 0.0368 -0.1135 -0.1124 509 MET A O 3700 C CB . MET A 516 ? 0.4233 0.4432 0.6151 0.0333 -0.1109 -0.1108 509 MET A CB 3701 C CG . MET A 516 ? 0.4992 0.5136 0.6777 0.0063 -0.0822 -0.1235 509 MET A CG 3702 S SD . MET A 516 ? 0.5732 0.6761 0.7894 -0.0470 0.0013 -0.1293 509 MET A SD 3703 C CE . MET A 516 ? 0.6309 0.6434 0.7551 -0.0162 -0.0315 -0.1013 509 MET A CE 3704 N N . PRO A 517 ? 0.3582 0.4007 0.5397 0.0374 -0.1068 -0.0972 510 PRO A N 3705 C CA . PRO A 517 ? 0.3380 0.3811 0.5078 0.0395 -0.0971 -0.0944 510 PRO A CA 3706 C C . PRO A 517 ? 0.3328 0.3652 0.4780 0.0382 -0.0847 -0.0883 510 PRO A C 3707 O O . PRO A 517 ? 0.3479 0.3710 0.4773 0.0335 -0.0771 -0.0925 510 PRO A O 3708 C CB . PRO A 517 ? 0.3249 0.3737 0.5067 0.0424 -0.1013 -0.0937 510 PRO A CB 3709 C CG . PRO A 517 ? 0.3573 0.3767 0.5234 0.0219 -0.0921 -0.1022 510 PRO A CG 3710 C CD . PRO A 517 ? 0.3527 0.4097 0.5396 0.0336 -0.1073 -0.1011 510 PRO A CD 3711 N N . ARG A 518 ? 0.3080 0.3500 0.4522 0.0370 -0.0705 -0.0800 511 ARG A N 3712 C CA . ARG A 518 ? 0.2780 0.3314 0.4077 0.0259 -0.0631 -0.0756 511 ARG A CA 3713 C C . ARG A 518 ? 0.2804 0.3301 0.3940 0.0409 -0.0557 -0.0673 511 ARG A C 3714 O O . ARG A 518 ? 0.2726 0.3266 0.4003 0.0348 -0.0504 -0.0659 511 ARG A O 3715 C CB . ARG A 518 ? 0.2739 0.3493 0.4215 0.0317 -0.0542 -0.0690 511 ARG A CB 3716 C CG . ARG A 518 ? 0.2889 0.3385 0.3837 0.0000 -0.0239 -0.0804 511 ARG A CG 3717 C CD . ARG A 518 ? 0.2941 0.3869 0.4999 0.0616 0.0214 -0.0577 511 ARG A CD 3718 N NE . ARG A 518 ? 0.3377 0.4355 0.5260 0.0399 0.0134 -0.0257 511 ARG A NE 3719 C CZ . ARG A 518 ? 0.3237 0.4930 0.5541 0.0385 -0.0115 -0.0001 511 ARG A CZ 3720 N NH1 . ARG A 518 ? 0.3593 0.4942 0.4838 0.0528 -0.0531 0.0599 511 ARG A NH1 3721 N NH2 . ARG A 518 ? 0.2861 0.5229 0.5636 0.0155 -0.0257 -0.0108 511 ARG A NH2 3722 N N . ILE A 519 ? 0.2644 0.3113 0.3966 0.0419 -0.0463 -0.0701 512 ILE A N 3723 C CA . ILE A 519 ? 0.2741 0.3106 0.3902 0.0439 -0.0412 -0.0575 512 ILE A CA 3724 C C . ILE A 519 ? 0.2787 0.3100 0.3810 0.0342 -0.0337 -0.0526 512 ILE A C 3725 O O . ILE A 519 ? 0.3077 0.2945 0.4056 0.0383 -0.0299 -0.0290 512 ILE A O 3726 C CB . ILE A 519 ? 0.2640 0.3308 0.3823 0.0424 -0.0411 -0.0645 512 ILE A CB 3727 C CG1 . ILE A 519 ? 0.2804 0.2951 0.3668 0.0741 -0.0391 -0.0875 512 ILE A CG1 3728 C CG2 . ILE A 519 ? 0.2507 0.3052 0.3806 0.0213 -0.0204 -0.0839 512 ILE A CG2 3729 C CD1 . ILE A 519 ? 0.2980 0.3412 0.3915 0.0734 -0.0116 -0.1318 512 ILE A CD1 3730 N N . SER A 520 ? 0.2519 0.2886 0.3574 0.0284 -0.0267 -0.0480 513 SER A N 3731 C CA . SER A 520 ? 0.2472 0.2909 0.3482 0.0381 -0.0197 -0.0376 513 SER A CA 3732 C C . SER A 520 ? 0.2431 0.2722 0.3317 0.0365 -0.0188 -0.0347 513 SER A C 3733 O O . SER A 520 ? 0.2405 0.2646 0.3124 0.0267 -0.0074 -0.0488 513 SER A O 3734 C CB . SER A 520 ? 0.2547 0.2753 0.3436 0.0538 -0.0188 -0.0362 513 SER A CB 3735 O OG . SER A 520 ? 0.3110 0.3447 0.3635 0.0756 0.0127 -0.0397 513 SER A OG 3736 N N A LYS A 521 ? 0.2358 0.2717 0.3335 0.0362 -0.0212 -0.0193 514 LYS A N 3737 N N B LYS A 521 ? 0.2257 0.2614 0.3124 0.0311 -0.0191 -0.0317 514 LYS A N 3738 C CA A LYS A 521 ? 0.2492 0.2757 0.3354 0.0254 -0.0300 -0.0165 514 LYS A CA 3739 C CA B LYS A 521 ? 0.2190 0.2480 0.2915 0.0256 -0.0215 -0.0288 514 LYS A CA 3740 C C A LYS A 521 ? 0.2566 0.2641 0.3231 0.0304 -0.0150 -0.0134 514 LYS A C 3741 C C B LYS A 521 ? 0.2368 0.2513 0.2975 0.0265 -0.0149 -0.0258 514 LYS A C 3742 O O A LYS A 521 ? 0.2514 0.2504 0.3122 0.0498 0.0006 -0.0264 514 LYS A O 3743 O O B LYS A 521 ? 0.2341 0.2407 0.2943 0.0369 -0.0087 -0.0277 514 LYS A O 3744 C CB A LYS A 521 ? 0.2341 0.2648 0.3498 0.0282 -0.0340 0.0024 514 LYS A CB 3745 C CB B LYS A 521 ? 0.2008 0.2370 0.2835 0.0242 -0.0223 -0.0283 514 LYS A CB 3746 C CG A LYS A 521 ? 0.2893 0.2997 0.3835 0.0235 -0.0418 -0.0030 514 LYS A CG 3747 C CG B LYS A 521 ? 0.1402 0.1859 0.2280 0.0175 -0.0285 -0.0253 514 LYS A CG 3748 C CD A LYS A 521 ? 0.3167 0.3453 0.3947 0.0342 -0.0384 0.0240 514 LYS A CD 3749 C CD B LYS A 521 ? 0.1172 0.1906 0.1699 -0.0009 -0.0202 -0.0370 514 LYS A CD 3750 C CE A LYS A 521 ? 0.3036 0.3980 0.4144 0.0260 -0.0306 0.0288 514 LYS A CE 3751 C CE B LYS A 521 ? 0.0807 0.1922 0.1323 0.0059 -0.0113 -0.0032 514 LYS A CE 3752 N NZ A LYS A 521 ? 0.2938 0.4341 0.4686 0.0075 -0.0285 0.0291 514 LYS A NZ 3753 N NZ B LYS A 521 ? 0.0671 0.1612 0.1254 0.0082 -0.0316 0.0138 514 LYS A NZ 3754 N N . LEU A 522 ? 0.2381 0.2572 0.3036 0.0248 -0.0089 -0.0227 515 LEU A N 3755 C CA . LEU A 522 ? 0.2869 0.2746 0.2871 0.0207 -0.0025 -0.0308 515 LEU A CA 3756 C C . LEU A 522 ? 0.3195 0.2794 0.2863 0.0150 0.0077 -0.0350 515 LEU A C 3757 O O . LEU A 522 ? 0.3579 0.2801 0.2818 0.0170 0.0081 -0.0380 515 LEU A O 3758 C CB . LEU A 522 ? 0.2609 0.2761 0.2663 0.0127 -0.0019 -0.0242 515 LEU A CB 3759 C CG . LEU A 522 ? 0.2814 0.2576 0.2499 0.0260 0.0064 -0.0068 515 LEU A CG 3760 C CD1 . LEU A 522 ? 0.3081 0.2960 0.2165 0.0495 0.0190 0.0307 515 LEU A CD1 3761 C CD2 . LEU A 522 ? 0.2019 0.2193 0.2235 0.0100 -0.0167 0.0213 515 LEU A CD2 3762 N N . GLY A 523 ? 0.3431 0.2764 0.2923 -0.0046 0.0143 -0.0406 516 GLY A N 3763 C CA . GLY A 523 ? 0.3363 0.2640 0.2869 -0.0193 0.0068 -0.0470 516 GLY A CA 3764 C C . GLY A 523 ? 0.3127 0.2762 0.2946 0.0019 0.0273 -0.0453 516 GLY A C 3765 O O . GLY A 523 ? 0.3603 0.2392 0.2821 0.0147 0.0517 -0.0513 516 GLY A O 3766 N N . SER A 524 ? 0.2842 0.2549 0.2786 0.0020 0.0281 -0.0445 517 SER A N 3767 C CA . SER A 524 ? 0.2596 0.2582 0.2500 0.0123 0.0086 -0.0381 517 SER A CA 3768 C C . SER A 524 ? 0.2430 0.2542 0.2351 0.0101 0.0083 -0.0338 517 SER A C 3769 O O . SER A 524 ? 0.2572 0.2593 0.2585 0.0032 -0.0025 -0.0446 517 SER A O 3770 C CB . SER A 524 ? 0.2502 0.2581 0.2453 0.0234 0.0049 -0.0275 517 SER A CB 3771 O OG . SER A 524 ? 0.2494 0.2824 0.2857 0.0341 0.0349 0.0031 517 SER A OG 3772 N N . GLY A 525 ? 0.2183 0.2294 0.2116 -0.0004 0.0066 -0.0215 518 GLY A N 3773 C CA . GLY A 525 ? 0.2166 0.2276 0.1988 -0.0005 0.0200 -0.0352 518 GLY A CA 3774 C C . GLY A 525 ? 0.2371 0.2310 0.2140 0.0135 -0.0066 -0.0304 518 GLY A C 3775 O O . GLY A 525 ? 0.2468 0.2147 0.2101 0.0090 -0.0132 -0.0544 518 GLY A O 3776 N N . ASN A 526 ? 0.2169 0.2410 0.2103 0.0068 0.0062 -0.0225 519 ASN A N 3777 C CA . ASN A 526 ? 0.2231 0.2369 0.2173 0.0197 0.0040 -0.0123 519 ASN A CA 3778 C C . ASN A 526 ? 0.2189 0.2220 0.2150 0.0144 0.0070 -0.0086 519 ASN A C 3779 O O . ASN A 526 ? 0.2340 0.2113 0.2188 0.0182 0.0062 -0.0075 519 ASN A O 3780 C CB . ASN A 526 ? 0.2327 0.2415 0.2435 0.0222 0.0063 -0.0032 519 ASN A CB 3781 C CG . ASN A 526 ? 0.2530 0.2689 0.3033 0.0498 0.0045 0.0005 519 ASN A CG 3782 O OD1 . ASN A 526 ? 0.2967 0.2928 0.3254 0.0166 0.0021 -0.0114 519 ASN A OD1 3783 N ND2 . ASN A 526 ? 0.1766 0.2613 0.2705 0.0702 -0.0297 -0.0143 519 ASN A ND2 3784 N N . ASP A 527 ? 0.2103 0.2074 0.2137 0.0062 0.0211 -0.0221 520 ASP A N 3785 C CA . ASP A 527 ? 0.1886 0.1880 0.2031 0.0103 0.0034 -0.0275 520 ASP A CA 3786 C C . ASP A 527 ? 0.1955 0.1995 0.1893 0.0170 0.0055 -0.0239 520 ASP A C 3787 O O . ASP A 527 ? 0.1989 0.2196 0.1985 0.0105 -0.0022 -0.0386 520 ASP A O 3788 C CB . ASP A 527 ? 0.1962 0.1859 0.1968 -0.0072 0.0244 -0.0268 520 ASP A CB 3789 C CG . ASP A 527 ? 0.2136 0.1965 0.2021 0.0102 -0.0116 -0.0364 520 ASP A CG 3790 O OD1 . ASP A 527 ? 0.2049 0.1908 0.1905 0.0139 -0.0144 -0.0201 520 ASP A OD1 3791 O OD2 . ASP A 527 ? 0.2350 0.1644 0.2097 0.0214 -0.0199 -0.0402 520 ASP A OD2 3792 N N . PHE A 528 ? 0.2016 0.2078 0.1855 0.0156 -0.0122 -0.0388 521 PHE A N 3793 C CA . PHE A 528 ? 0.2215 0.2112 0.1975 0.0287 -0.0059 -0.0201 521 PHE A CA 3794 C C . PHE A 528 ? 0.2139 0.2218 0.1929 0.0355 0.0001 -0.0245 521 PHE A C 3795 O O . PHE A 528 ? 0.2442 0.2045 0.1963 0.0512 0.0128 -0.0166 521 PHE A O 3796 C CB . PHE A 528 ? 0.2138 0.2184 0.1756 0.0222 -0.0045 -0.0281 521 PHE A CB 3797 C CG . PHE A 528 ? 0.2418 0.2447 0.2133 0.0243 -0.0035 -0.0234 521 PHE A CG 3798 C CD1 . PHE A 528 ? 0.2536 0.2507 0.2382 -0.0036 0.0069 -0.0162 521 PHE A CD1 3799 C CD2 . PHE A 528 ? 0.2156 0.2367 0.2047 0.0244 -0.0086 -0.0445 521 PHE A CD2 3800 C CE1 . PHE A 528 ? 0.2359 0.2581 0.2396 -0.0012 -0.0026 -0.0343 521 PHE A CE1 3801 C CE2 . PHE A 528 ? 0.2416 0.2413 0.2420 -0.0011 -0.0028 -0.0515 521 PHE A CE2 3802 C CZ . PHE A 528 ? 0.2473 0.2524 0.2041 -0.0005 0.0148 -0.0494 521 PHE A CZ 3803 N N . GLU A 529 ? 0.1863 0.2162 0.1720 0.0287 0.0056 -0.0258 522 GLU A N 3804 C CA . GLU A 529 ? 0.1985 0.2081 0.1761 0.0321 0.0147 -0.0138 522 GLU A CA 3805 C C . GLU A 529 ? 0.1970 0.2120 0.1880 0.0238 0.0176 -0.0115 522 GLU A C 3806 O O . GLU A 529 ? 0.2132 0.2042 0.2117 0.0229 0.0296 0.0002 522 GLU A O 3807 C CB . GLU A 529 ? 0.1829 0.1985 0.1497 0.0196 0.0230 -0.0206 522 GLU A CB 3808 C CG . GLU A 529 ? 0.2253 0.2128 0.1538 0.0473 0.0041 -0.0480 522 GLU A CG 3809 C CD . GLU A 529 ? 0.2415 0.2647 0.2001 0.0065 -0.0132 -0.0174 522 GLU A CD 3810 O OE1 . GLU A 529 ? 0.2859 0.2864 0.2676 -0.0268 -0.0619 0.0000 522 GLU A OE1 3811 O OE2 . GLU A 529 ? 0.2852 0.2411 0.2212 0.0357 0.0430 -0.0623 522 GLU A OE2 3812 N N . VAL A 530 ? 0.1903 0.2009 0.1777 0.0160 0.0099 -0.0033 523 VAL A N 3813 C CA . VAL A 530 ? 0.1888 0.2062 0.1699 0.0059 0.0042 -0.0036 523 VAL A CA 3814 C C . VAL A 530 ? 0.2072 0.2061 0.1811 0.0068 0.0059 0.0009 523 VAL A C 3815 O O . VAL A 530 ? 0.2269 0.1853 0.1725 -0.0050 0.0254 0.0053 523 VAL A O 3816 C CB . VAL A 530 ? 0.1915 0.2144 0.1822 0.0108 -0.0126 -0.0022 523 VAL A CB 3817 C CG1 . VAL A 530 ? 0.1794 0.2318 0.1486 -0.0083 0.0006 0.0044 523 VAL A CG1 3818 C CG2 . VAL A 530 ? 0.1630 0.1931 0.2033 -0.0013 -0.0210 -0.0060 523 VAL A CG2 3819 N N . PHE A 531 ? 0.2030 0.2106 0.1773 -0.0101 -0.0146 0.0048 524 PHE A N 3820 C CA . PHE A 531 ? 0.2238 0.1937 0.1810 0.0074 -0.0012 0.0084 524 PHE A CA 3821 C C . PHE A 531 ? 0.2180 0.2020 0.1826 0.0137 -0.0109 0.0048 524 PHE A C 3822 O O . PHE A 531 ? 0.2345 0.1893 0.2038 0.0235 0.0000 0.0086 524 PHE A O 3823 C CB . PHE A 531 ? 0.2346 0.2006 0.1993 0.0030 0.0096 0.0111 524 PHE A CB 3824 C CG . PHE A 531 ? 0.2754 0.1891 0.2208 0.0001 0.0224 0.0170 524 PHE A CG 3825 C CD1 . PHE A 531 ? 0.2596 0.2154 0.2769 -0.0050 0.0334 -0.0038 524 PHE A CD1 3826 C CD2 . PHE A 531 ? 0.2481 0.2002 0.1946 0.0166 0.0013 0.0163 524 PHE A CD2 3827 C CE1 . PHE A 531 ? 0.3000 0.1903 0.2585 -0.0038 0.0258 -0.0136 524 PHE A CE1 3828 C CE2 . PHE A 531 ? 0.2284 0.2048 0.1689 -0.0116 0.0033 0.0127 524 PHE A CE2 3829 C CZ . PHE A 531 ? 0.2490 0.2079 0.2276 0.0096 0.0201 -0.0332 524 PHE A CZ 3830 N N . PHE A 532 ? 0.2054 0.2051 0.1771 0.0080 -0.0166 0.0040 525 PHE A N 3831 C CA . PHE A 532 ? 0.1933 0.2166 0.1793 0.0142 -0.0205 0.0034 525 PHE A CA 3832 C C . PHE A 532 ? 0.2025 0.2106 0.1895 0.0140 -0.0084 -0.0069 525 PHE A C 3833 O O . PHE A 532 ? 0.2400 0.2135 0.2016 0.0279 -0.0119 -0.0146 525 PHE A O 3834 C CB . PHE A 532 ? 0.1830 0.2179 0.1600 0.0102 -0.0237 -0.0038 525 PHE A CB 3835 C CG . PHE A 532 ? 0.1691 0.2210 0.1973 0.0255 -0.0510 -0.0019 525 PHE A CG 3836 C CD1 . PHE A 532 ? 0.2001 0.2011 0.1963 0.0325 -0.0492 -0.0239 525 PHE A CD1 3837 C CD2 . PHE A 532 ? 0.2066 0.1957 0.2236 0.0124 -0.0446 0.0159 525 PHE A CD2 3838 C CE1 . PHE A 532 ? 0.2178 0.2152 0.2189 0.0213 -0.0494 -0.0248 525 PHE A CE1 3839 C CE2 . PHE A 532 ? 0.1693 0.1937 0.2132 -0.0007 -0.0729 -0.0238 525 PHE A CE2 3840 C CZ . PHE A 532 ? 0.1785 0.2202 0.2111 0.0326 -0.0419 -0.0178 525 PHE A CZ 3841 N N A GLN A 533 ? 0.1810 0.2057 0.1618 0.0079 -0.0109 -0.0098 526 GLN A N 3842 N N B GLN A 533 ? 0.1948 0.2183 0.1738 0.0101 -0.0058 -0.0103 526 GLN A N 3843 C CA A GLN A 533 ? 0.1630 0.1884 0.1592 0.0074 -0.0111 -0.0159 526 GLN A CA 3844 C CA B GLN A 533 ? 0.1872 0.2196 0.1832 0.0116 -0.0028 -0.0111 526 GLN A CA 3845 C C A GLN A 533 ? 0.1629 0.1898 0.1632 0.0078 -0.0037 -0.0153 526 GLN A C 3846 C C B GLN A 533 ? 0.1808 0.2053 0.1781 0.0098 0.0035 -0.0143 526 GLN A C 3847 O O A GLN A 533 ? 0.1549 0.1852 0.1522 -0.0168 -0.0012 -0.0135 526 GLN A O 3848 O O B GLN A 533 ? 0.1828 0.2045 0.1777 -0.0060 0.0123 -0.0109 526 GLN A O 3849 C CB A GLN A 533 ? 0.1499 0.1861 0.1603 0.0146 -0.0063 -0.0063 526 GLN A CB 3850 C CB B GLN A 533 ? 0.1896 0.2201 0.1895 0.0200 0.0057 -0.0085 526 GLN A CB 3851 C CG A GLN A 533 ? 0.1367 0.1439 0.1423 0.0076 -0.0184 -0.0219 526 GLN A CG 3852 C CG B GLN A 533 ? 0.1998 0.2532 0.2253 0.0123 0.0026 0.0059 526 GLN A CG 3853 C CD A GLN A 533 ? 0.0926 0.1229 0.1125 0.0032 -0.0105 -0.0194 526 GLN A CD 3854 C CD B GLN A 533 ? 0.2510 0.2714 0.2570 0.0001 -0.0011 0.0114 526 GLN A CD 3855 O OE1 A GLN A 533 ? 0.0678 0.0997 0.1314 0.0290 -0.0103 0.0110 526 GLN A OE1 3856 O OE1 B GLN A 533 ? 0.3034 0.2781 0.2859 0.0036 -0.0174 0.0356 526 GLN A OE1 3857 N NE2 A GLN A 533 ? 0.0907 0.1236 0.1082 0.0386 -0.0061 -0.0330 526 GLN A NE2 3858 N NE2 B GLN A 533 ? 0.2246 0.2822 0.2699 -0.0135 0.0280 0.0271 526 GLN A NE2 3859 N N . ARG A 534 ? 0.1569 0.1943 0.1500 0.0021 -0.0002 -0.0169 527 ARG A N 3860 C CA . ARG A 534 ? 0.1676 0.1971 0.1576 0.0034 -0.0005 -0.0228 527 ARG A CA 3861 C C . ARG A 534 ? 0.1940 0.1893 0.1645 0.0137 -0.0044 -0.0222 527 ARG A C 3862 O O . ARG A 534 ? 0.2138 0.1837 0.1707 0.0128 -0.0083 -0.0217 527 ARG A O 3863 C CB . ARG A 534 ? 0.1468 0.1872 0.1802 -0.0039 -0.0127 -0.0167 527 ARG A CB 3864 C CG . ARG A 534 ? 0.1153 0.1849 0.1705 -0.0208 0.0048 -0.0315 527 ARG A CG 3865 C CD . ARG A 534 ? 0.1735 0.1548 0.2079 -0.0391 0.0327 -0.0283 527 ARG A CD 3866 N NE . ARG A 534 ? 0.2195 0.1615 0.1543 -0.0359 -0.0078 -0.0135 527 ARG A NE 3867 C CZ . ARG A 534 ? 0.2014 0.2213 0.1887 -0.0104 0.0036 -0.0325 527 ARG A CZ 3868 N NH1 . ARG A 534 ? 0.1747 0.2029 0.1625 0.0393 0.0196 -0.0067 527 ARG A NH1 3869 N NH2 . ARG A 534 ? 0.1892 0.1721 0.1938 -0.0142 0.0031 -0.0239 527 ARG A NH2 3870 N N . LEU A 535 ? 0.1861 0.1941 0.1467 0.0135 -0.0053 -0.0249 528 LEU A N 3871 C CA . LEU A 535 ? 0.2050 0.1874 0.1683 0.0135 0.0039 -0.0203 528 LEU A CA 3872 C C . LEU A 535 ? 0.2071 0.1836 0.1706 0.0217 -0.0024 -0.0215 528 LEU A C 3873 O O . LEU A 535 ? 0.2398 0.2156 0.2059 0.0261 -0.0012 -0.0235 528 LEU A O 3874 C CB . LEU A 535 ? 0.1994 0.1774 0.1697 0.0225 0.0100 -0.0218 528 LEU A CB 3875 C CG . LEU A 535 ? 0.1705 0.1772 0.1663 0.0215 -0.0172 0.0246 528 LEU A CG 3876 C CD1 . LEU A 535 ? 0.1923 0.1541 0.1619 0.0161 0.0202 -0.0008 528 LEU A CD1 3877 C CD2 . LEU A 535 ? 0.2080 0.2028 0.1942 0.0665 -0.0036 0.0375 528 LEU A CD2 3878 N N . GLY A 536 ? 0.2039 0.1526 0.1725 0.0193 -0.0138 -0.0111 529 GLY A N 3879 C CA . GLY A 536 ? 0.1886 0.1717 0.1338 0.0293 -0.0291 -0.0098 529 GLY A CA 3880 C C . GLY A 536 ? 0.1881 0.1807 0.1574 0.0281 -0.0144 -0.0110 529 GLY A C 3881 O O . GLY A 536 ? 0.1833 0.1922 0.1364 0.0360 -0.0241 -0.0001 529 GLY A O 3882 N N . ILE A 537 ? 0.1971 0.1758 0.1598 0.0267 -0.0217 0.0002 530 ILE A N 3883 C CA . ILE A 537 ? 0.1989 0.1913 0.1538 0.0241 -0.0237 -0.0036 530 ILE A CA 3884 C C . ILE A 537 ? 0.2145 0.1899 0.1636 0.0233 -0.0290 -0.0152 530 ILE A C 3885 O O . ILE A 537 ? 0.2069 0.2146 0.1431 0.0090 -0.0061 -0.0219 530 ILE A O 3886 C CB . ILE A 537 ? 0.1964 0.1846 0.1588 0.0291 -0.0352 0.0025 530 ILE A CB 3887 C CG1 . ILE A 537 ? 0.1959 0.2002 0.1812 0.0166 -0.0289 -0.0233 530 ILE A CG1 3888 C CG2 . ILE A 537 ? 0.2276 0.1882 0.1216 0.0212 -0.0399 0.0184 530 ILE A CG2 3889 C CD1 . ILE A 537 ? 0.2031 0.1814 0.2200 -0.0058 -0.0361 -0.0384 530 ILE A CD1 3890 N N . ALA A 538 ? 0.2275 0.1955 0.1510 0.0192 -0.0426 -0.0180 531 ALA A N 3891 C CA . ALA A 538 ? 0.2103 0.1882 0.1602 0.0300 -0.0369 -0.0234 531 ALA A CA 3892 C C . ALA A 538 ? 0.2200 0.2231 0.1783 0.0337 -0.0284 -0.0214 531 ALA A C 3893 O O . ALA A 538 ? 0.2249 0.2085 0.1686 0.0317 -0.0159 -0.0052 531 ALA A O 3894 C CB . ALA A 538 ? 0.2272 0.2188 0.1380 0.0233 -0.0350 -0.0244 531 ALA A CB 3895 N N . SER A 539 ? 0.2254 0.2177 0.1669 0.0414 -0.0302 -0.0256 532 SER A N 3896 C CA . SER A 539 ? 0.2140 0.2149 0.1803 0.0421 -0.0281 -0.0249 532 SER A CA 3897 C C . SER A 539 ? 0.2153 0.2090 0.1884 0.0440 -0.0425 -0.0288 532 SER A C 3898 O O . SER A 539 ? 0.2360 0.2102 0.2098 0.0469 -0.0344 -0.0388 532 SER A O 3899 C CB . SER A 539 ? 0.1916 0.2050 0.1759 0.0319 -0.0411 -0.0167 532 SER A CB 3900 O OG . SER A 539 ? 0.2041 0.2404 0.1860 0.0405 -0.0228 0.0097 532 SER A OG 3901 N N . GLY A 540 ? 0.2197 0.2116 0.2081 0.0478 -0.0420 -0.0347 533 GLY A N 3902 C CA . GLY A 540 ? 0.2145 0.2085 0.2309 0.0479 -0.0286 -0.0390 533 GLY A CA 3903 C C . GLY A 540 ? 0.2362 0.2218 0.2485 0.0459 -0.0287 -0.0351 533 GLY A C 3904 O O . GLY A 540 ? 0.2403 0.2214 0.2412 0.0348 -0.0394 -0.0507 533 GLY A O 3905 N N . ARG A 541 ? 0.2352 0.2204 0.2434 0.0486 -0.0177 -0.0353 534 ARG A N 3906 C CA . ARG A 541 ? 0.2472 0.2380 0.2522 0.0452 -0.0263 -0.0356 534 ARG A CA 3907 C C . ARG A 541 ? 0.2495 0.2456 0.2619 0.0487 -0.0342 -0.0356 534 ARG A C 3908 O O . ARG A 541 ? 0.2321 0.2275 0.2618 0.0374 -0.0406 -0.0369 534 ARG A O 3909 C CB . ARG A 541 ? 0.2406 0.2370 0.2575 0.0346 -0.0168 -0.0533 534 ARG A CB 3910 C CG . ARG A 541 ? 0.3198 0.2470 0.2642 0.0069 -0.0002 -0.0482 534 ARG A CG 3911 C CD . ARG A 541 ? 0.3795 0.2870 0.3222 -0.0390 0.0143 -0.0511 534 ARG A CD 3912 N NE . ARG A 541 ? 0.3496 0.3254 0.3367 -0.0370 0.0196 -0.0865 534 ARG A NE 3913 C CZ . ARG A 541 ? 0.3585 0.2929 0.3494 0.0152 0.0283 -0.0769 534 ARG A CZ 3914 N NH1 . ARG A 541 ? 0.3199 0.2334 0.3024 0.0291 -0.0537 -0.0720 534 ARG A NH1 3915 N NH2 . ARG A 541 ? 0.2890 0.2923 0.3755 0.0090 0.0510 -0.0377 534 ARG A NH2 3916 N N . ALA A 542 ? 0.2457 0.2509 0.2479 0.0620 -0.0479 -0.0300 535 ALA A N 3917 C CA . ALA A 542 ? 0.2436 0.2578 0.2507 0.0562 -0.0462 -0.0350 535 ALA A CA 3918 C C . ALA A 542 ? 0.2456 0.2582 0.2571 0.0559 -0.0541 -0.0333 535 ALA A C 3919 O O . ALA A 542 ? 0.2407 0.2425 0.2564 0.0387 -0.0513 0.0017 535 ALA A O 3920 C CB . ALA A 542 ? 0.2291 0.2556 0.2323 0.0459 -0.0635 -0.0607 535 ALA A CB 3921 N N . ARG A 543 ? 0.2446 0.2698 0.2647 0.0558 -0.0477 -0.0353 536 ARG A N 3922 C CA . ARG A 543 ? 0.2422 0.2684 0.2789 0.0569 -0.0592 -0.0401 536 ARG A CA 3923 C C . ARG A 543 ? 0.2523 0.2741 0.3035 0.0620 -0.0517 -0.0415 536 ARG A C 3924 O O . ARG A 543 ? 0.2387 0.2723 0.3112 0.0647 -0.0699 -0.0512 536 ARG A O 3925 C CB . ARG A 543 ? 0.2661 0.2774 0.2833 0.0406 -0.0383 -0.0448 536 ARG A CB 3926 C CG . ARG A 543 ? 0.2554 0.2589 0.2748 0.0211 -0.0758 -0.0207 536 ARG A CG 3927 C CD . ARG A 543 ? 0.2233 0.3152 0.2575 0.0264 -0.0220 -0.0153 536 ARG A CD 3928 N NE . ARG A 543 ? 0.2325 0.2881 0.2760 0.0033 -0.0372 -0.0063 536 ARG A NE 3929 C CZ . ARG A 543 ? 0.2157 0.3125 0.2844 0.0124 -0.0145 -0.0201 536 ARG A CZ 3930 N NH1 . ARG A 543 ? 0.2037 0.3324 0.2861 0.0097 0.0032 0.0247 536 ARG A NH1 3931 N NH2 . ARG A 543 ? 0.2243 0.2512 0.2831 -0.0011 -0.0197 -0.0513 536 ARG A NH2 3932 N N . TYR A 544 ? 0.2430 0.2765 0.2976 0.0778 -0.0562 -0.0433 537 TYR A N 3933 C CA . TYR A 544 ? 0.2488 0.2891 0.3152 0.0738 -0.0514 -0.0362 537 TYR A CA 3934 C C . TYR A 544 ? 0.2538 0.2948 0.3366 0.0685 -0.0410 -0.0317 537 TYR A C 3935 O O . TYR A 544 ? 0.2276 0.2877 0.3082 0.0747 -0.0394 -0.0374 537 TYR A O 3936 C CB . TYR A 544 ? 0.2384 0.2621 0.3107 0.0749 -0.0580 -0.0262 537 TYR A CB 3937 C CG . TYR A 544 ? 0.2638 0.2677 0.3123 0.0713 -0.0694 -0.0276 537 TYR A CG 3938 C CD1 . TYR A 544 ? 0.2920 0.2579 0.3221 0.0566 -0.0730 -0.0342 537 TYR A CD1 3939 C CD2 . TYR A 544 ? 0.2456 0.2789 0.2960 0.0594 -0.0883 -0.0242 537 TYR A CD2 3940 C CE1 . TYR A 544 ? 0.2635 0.2670 0.2936 0.0657 -0.0882 -0.0251 537 TYR A CE1 3941 C CE2 . TYR A 544 ? 0.2451 0.2273 0.3240 0.0664 -0.0891 -0.0275 537 TYR A CE2 3942 C CZ . TYR A 544 ? 0.2657 0.2572 0.2966 0.0495 -0.0908 -0.0226 537 TYR A CZ 3943 O OH . TYR A 544 ? 0.2747 0.2518 0.2884 0.0510 -0.0919 -0.0345 537 TYR A OH 3944 N N . THR A 545 ? 0.2583 0.2946 0.3728 0.0592 -0.0323 -0.0355 538 THR A N 3945 C CA . THR A 545 ? 0.2674 0.3035 0.3871 0.0464 -0.0256 -0.0412 538 THR A CA 3946 C C . THR A 545 ? 0.2744 0.3189 0.4208 0.0488 -0.0282 -0.0520 538 THR A C 3947 O O . THR A 545 ? 0.2645 0.3161 0.4169 0.0471 -0.0318 -0.0513 538 THR A O 3948 C CB . THR A 545 ? 0.2685 0.3004 0.3757 0.0473 -0.0299 -0.0457 538 THR A CB 3949 O OG1 . THR A 545 ? 0.2887 0.2925 0.3897 0.0400 -0.0379 0.0079 538 THR A OG1 3950 C CG2 . THR A 545 ? 0.2757 0.2887 0.3629 0.0186 -0.0053 -0.0348 538 THR A CG2 3951 N N . LYS A 546 ? 0.2904 0.3376 0.4460 0.0422 -0.0216 -0.0661 539 LYS A N 3952 C CA . LYS A 546 ? 0.2960 0.3704 0.4774 0.0360 -0.0269 -0.0652 539 LYS A CA 3953 C C . LYS A 546 ? 0.2971 0.3756 0.4961 0.0313 -0.0223 -0.0622 539 LYS A C 3954 O O . LYS A 546 ? 0.2551 0.3524 0.4798 0.0232 -0.0159 -0.0608 539 LYS A O 3955 C CB . LYS A 546 ? 0.3172 0.3827 0.4852 0.0352 -0.0236 -0.0652 539 LYS A CB 3956 C CG . LYS A 546 ? 0.3556 0.4274 0.4818 0.0129 -0.0494 -0.0483 539 LYS A CG 3957 C CD . LYS A 546 ? 0.4325 0.4802 0.5504 0.0377 -0.0207 -0.0777 539 LYS A CD 3958 C CE . LYS A 546 ? 0.5414 0.5302 0.5480 0.0218 -0.0584 -0.0476 539 LYS A CE 3959 N NZ . LYS A 546 ? 0.5891 0.5319 0.5890 -0.0173 -0.0346 -0.0666 539 LYS A NZ 3960 N N . ASN A 547 ? 0.3069 0.4125 0.5387 0.0398 -0.0204 -0.0656 540 ASN A N 3961 C CA . ASN A 547 ? 0.3467 0.4678 0.6030 0.0261 -0.0168 -0.0662 540 ASN A CA 3962 C C . ASN A 547 ? 0.3927 0.5022 0.6386 0.0245 -0.0116 -0.0621 540 ASN A C 3963 O O . ASN A 547 ? 0.4171 0.5120 0.6416 0.0182 -0.0073 -0.0663 540 ASN A O 3964 C CB . ASN A 547 ? 0.3343 0.4675 0.5929 0.0152 -0.0220 -0.0669 540 ASN A CB 3965 C CG . ASN A 547 ? 0.3154 0.4916 0.6045 0.0150 -0.0187 -0.0594 540 ASN A CG 3966 O OD1 . ASN A 547 ? 0.3596 0.4794 0.5932 -0.0580 0.0008 -0.0360 540 ASN A OD1 3967 N ND2 . ASN A 547 ? 0.3144 0.5275 0.5927 -0.0320 -0.0618 -0.0516 540 ASN A ND2 3968 N N A TRP A 548 ? 0.4173 0.5185 0.6686 0.0270 -0.0104 -0.0663 541 TRP A N 3969 N N B TRP A 548 ? 0.4136 0.5160 0.6675 0.0228 -0.0058 -0.0634 541 TRP A N 3970 C CA A TRP A 548 ? 0.4487 0.5463 0.6963 0.0295 -0.0121 -0.0633 541 TRP A CA 3971 C CA B TRP A 548 ? 0.4457 0.5522 0.6964 0.0273 -0.0085 -0.0579 541 TRP A CA 3972 C C A TRP A 548 ? 0.4713 0.5710 0.7264 0.0274 -0.0101 -0.0627 541 TRP A C 3973 C C B TRP A 548 ? 0.4736 0.5774 0.7293 0.0234 -0.0084 -0.0563 541 TRP A C 3974 O O A TRP A 548 ? 0.4754 0.5688 0.7257 0.0256 -0.0109 -0.0642 541 TRP A O 3975 O O B TRP A 548 ? 0.4808 0.5884 0.7360 0.0222 -0.0057 -0.0495 541 TRP A O 3976 C CB A TRP A 548 ? 0.4467 0.5419 0.6927 0.0297 -0.0103 -0.0642 541 TRP A CB 3977 C CB B TRP A 548 ? 0.4472 0.5423 0.6927 0.0244 -0.0043 -0.0551 541 TRP A CB 3978 C CG A TRP A 548 ? 0.4499 0.5394 0.6850 0.0337 -0.0032 -0.0668 541 TRP A CG 3979 C CG B TRP A 548 ? 0.4401 0.5514 0.6756 0.0373 -0.0054 -0.0612 541 TRP A CG 3980 C CD1 A TRP A 548 ? 0.4481 0.5394 0.6782 0.0271 -0.0006 -0.0653 541 TRP A CD1 3981 C CD1 B TRP A 548 ? 0.4158 0.5434 0.6555 0.0412 0.0083 -0.0713 541 TRP A CD1 3982 C CD2 A TRP A 548 ? 0.4493 0.5315 0.6786 0.0319 0.0018 -0.0668 541 TRP A CD2 3983 C CD2 B TRP A 548 ? 0.4522 0.5318 0.6458 0.0462 -0.0017 -0.0585 541 TRP A CD2 3984 N NE1 A TRP A 548 ? 0.4508 0.5387 0.6779 0.0303 0.0061 -0.0628 541 TRP A NE1 3985 N NE1 B TRP A 548 ? 0.4669 0.5286 0.6450 0.0209 0.0155 -0.0693 541 TRP A NE1 3986 C CE2 A TRP A 548 ? 0.4528 0.5323 0.6784 0.0274 0.0041 -0.0625 541 TRP A CE2 3987 C CE2 B TRP A 548 ? 0.4585 0.5261 0.6462 0.0423 -0.0027 -0.0600 541 TRP A CE2 3988 C CE3 A TRP A 548 ? 0.4544 0.5291 0.6800 0.0339 0.0056 -0.0635 541 TRP A CE3 3989 C CE3 B TRP A 548 ? 0.4543 0.5058 0.6398 0.0580 0.0005 -0.0679 541 TRP A CE3 3990 C CZ2 A TRP A 548 ? 0.4533 0.5314 0.6872 0.0256 0.0054 -0.0606 541 TRP A CZ2 3991 C CZ2 B TRP A 548 ? 0.4761 0.4892 0.6281 0.0684 -0.0052 -0.0745 541 TRP A CZ2 3992 C CZ3 A TRP A 548 ? 0.4620 0.5364 0.6845 0.0375 0.0090 -0.0571 541 TRP A CZ3 3993 C CZ3 B TRP A 548 ? 0.4655 0.4914 0.6272 0.0696 0.0087 -0.0726 541 TRP A CZ3 3994 C CH2 A TRP A 548 ? 0.4522 0.5339 0.6874 0.0308 0.0055 -0.0587 541 TRP A CH2 3995 C CH2 B TRP A 548 ? 0.4586 0.4723 0.6340 0.0749 0.0044 -0.0722 541 TRP A CH2 3996 N N . GLU A 549 ? 0.4943 0.5975 0.7561 0.0240 -0.0132 -0.0623 542 GLU A N 3997 C CA . GLU A 549 ? 0.5298 0.6358 0.8043 0.0257 -0.0068 -0.0652 542 GLU A CA 3998 C C . GLU A 549 ? 0.5602 0.6651 0.8372 0.0295 -0.0030 -0.0654 542 GLU A C 3999 O O . GLU A 549 ? 0.5740 0.6749 0.8509 0.0223 0.0051 -0.0586 542 GLU A O 4000 C CB . GLU A 549 ? 0.5467 0.6429 0.8156 0.0232 -0.0104 -0.0669 542 GLU A CB 4001 C CG . GLU A 549 ? 0.5633 0.6487 0.8354 0.0306 -0.0104 -0.0785 542 GLU A CG 4002 C CD . GLU A 549 ? 0.5882 0.6788 0.8730 0.0269 -0.0003 -0.0704 542 GLU A CD 4003 O OE1 . GLU A 549 ? 0.5774 0.6841 0.8828 0.0098 0.0089 -0.0726 542 GLU A OE1 4004 O OE2 . GLU A 549 ? 0.5682 0.6829 0.8772 0.0459 -0.0119 -0.0639 542 GLU A OE2 4005 N N . THR A 550 ? 0.5789 0.6834 0.8594 0.0291 -0.0016 -0.0644 543 THR A N 4006 C CA . THR A 550 ? 0.5816 0.7070 0.8774 0.0325 0.0024 -0.0704 543 THR A CA 4007 C C . THR A 550 ? 0.5855 0.7103 0.8790 0.0330 0.0057 -0.0743 543 THR A C 4008 O O . THR A 550 ? 0.5807 0.7187 0.8861 0.0359 0.0155 -0.0749 543 THR A O 4009 C CB . THR A 550 ? 0.5895 0.7159 0.8801 0.0295 0.0021 -0.0704 543 THR A CB 4010 O OG1 . THR A 550 ? 0.5937 0.7264 0.8916 0.0162 0.0001 -0.0621 543 THR A OG1 4011 C CG2 . THR A 550 ? 0.5651 0.7283 0.8812 0.0177 0.0040 -0.0700 543 THR A CG2 4012 N N . ASN A 551 ? 0.5837 0.7112 0.8747 0.0398 0.0055 -0.0754 544 ASN A N 4013 C CA . ASN A 551 ? 0.5927 0.7102 0.8659 0.0398 0.0042 -0.0731 544 ASN A CA 4014 C C . ASN A 551 ? 0.5992 0.7160 0.8606 0.0368 0.0062 -0.0721 544 ASN A C 4015 O O . ASN A 551 ? 0.6127 0.7101 0.8663 0.0438 0.0010 -0.0810 544 ASN A O 4016 C CB . ASN A 551 ? 0.5811 0.6988 0.8621 0.0430 0.0037 -0.0735 544 ASN A CB 4017 C CG . ASN A 551 ? 0.5711 0.6894 0.8589 0.0376 0.0046 -0.0772 544 ASN A CG 4018 O OD1 . ASN A 551 ? 0.5126 0.6751 0.8478 0.0287 0.0031 -0.0763 544 ASN A OD1 4019 N ND2 . ASN A 551 ? 0.5680 0.6570 0.8409 0.0532 -0.0012 -0.0733 544 ASN A ND2 4020 N N . LYS A 552 ? 0.6014 0.7168 0.8503 0.0302 0.0145 -0.0667 545 LYS A N 4021 C CA . LYS A 552 ? 0.5969 0.7149 0.8422 0.0234 0.0209 -0.0608 545 LYS A CA 4022 C C . LYS A 552 ? 0.6014 0.7005 0.8262 0.0218 0.0206 -0.0573 545 LYS A C 4023 O O . LYS A 552 ? 0.6099 0.7118 0.8354 0.0223 0.0130 -0.0522 545 LYS A O 4024 C CB . LYS A 552 ? 0.6040 0.7169 0.8459 0.0195 0.0259 -0.0601 545 LYS A CB 4025 C CG . LYS A 552 ? 0.5934 0.7152 0.8565 0.0200 0.0340 -0.0620 545 LYS A CG 4026 C CD . LYS A 552 ? 0.6008 0.7134 0.8719 0.0211 0.0452 -0.0654 545 LYS A CD 4027 C CE . LYS A 552 ? 0.5959 0.7110 0.8733 0.0222 0.0539 -0.0631 545 LYS A CE 4028 N NZ . LYS A 552 ? 0.5914 0.7049 0.8726 0.0304 0.0543 -0.0641 545 LYS A NZ 4029 N N . PHE A 553 ? 0.5841 0.6810 0.7957 0.0240 0.0216 -0.0617 546 PHE A N 4030 C CA . PHE A 553 ? 0.5666 0.6434 0.7523 0.0280 0.0294 -0.0655 546 PHE A CA 4031 C C . PHE A 553 ? 0.5544 0.6331 0.7281 0.0273 0.0291 -0.0604 546 PHE A C 4032 O O . PHE A 553 ? 0.5559 0.6185 0.7127 0.0335 0.0370 -0.0618 546 PHE A O 4033 C CB . PHE A 553 ? 0.5679 0.6395 0.7519 0.0294 0.0228 -0.0666 546 PHE A CB 4034 C CG . PHE A 553 ? 0.5582 0.6070 0.7432 0.0269 0.0140 -0.0803 546 PHE A CG 4035 C CD1 . PHE A 553 ? 0.5617 0.5773 0.7427 0.0342 0.0130 -0.0810 546 PHE A CD1 4036 C CD2 . PHE A 553 ? 0.5445 0.5572 0.7368 -0.0063 -0.0072 -0.0782 546 PHE A CD2 4037 C CE1 . PHE A 553 ? 0.5394 0.5419 0.7371 0.0350 0.0053 -0.0849 546 PHE A CE1 4038 C CE2 . PHE A 553 ? 0.5529 0.5076 0.7333 -0.0139 -0.0058 -0.0925 546 PHE A CE2 4039 C CZ . PHE A 553 ? 0.5531 0.5292 0.7291 0.0232 0.0047 -0.0745 546 PHE A CZ 4040 N N . SER A 554 ? 0.5400 0.6038 0.6903 0.0269 0.0359 -0.0605 547 SER A N 4041 C CA . SER A 554 ? 0.5297 0.5892 0.6608 0.0194 0.0271 -0.0565 547 SER A CA 4042 C C . SER A 554 ? 0.4992 0.5498 0.6278 0.0247 0.0317 -0.0642 547 SER A C 4043 O O . SER A 554 ? 0.4956 0.5554 0.6160 0.0199 0.0327 -0.0701 547 SER A O 4044 C CB . SER A 554 ? 0.5507 0.5976 0.6693 0.0195 0.0238 -0.0559 547 SER A CB 4045 O OG . SER A 554 ? 0.6023 0.6387 0.6697 -0.0050 0.0028 -0.0660 547 SER A OG 4046 N N . GLY A 555 ? 0.4757 0.4988 0.5995 0.0248 0.0329 -0.0652 548 GLY A N 4047 C CA . GLY A 555 ? 0.4208 0.4352 0.5525 0.0328 0.0270 -0.0703 548 GLY A CA 4048 C C . GLY A 555 ? 0.3866 0.4109 0.5105 0.0260 0.0151 -0.0657 548 GLY A C 4049 O O . GLY A 555 ? 0.3734 0.4002 0.5073 0.0177 0.0143 -0.0706 548 GLY A O 4050 N N . TYR A 556 ? 0.3576 0.3700 0.4797 0.0378 0.0095 -0.0678 549 TYR A N 4051 C CA . TYR A 556 ? 0.3272 0.3398 0.4279 0.0292 0.0013 -0.0637 549 TYR A CA 4052 C C . TYR A 556 ? 0.2870 0.3062 0.4055 0.0387 0.0069 -0.0626 549 TYR A C 4053 O O . TYR A 556 ? 0.3299 0.2980 0.3970 0.0068 -0.0246 -0.0745 549 TYR A O 4054 C CB . TYR A 556 ? 0.3142 0.3583 0.4175 0.0382 0.0099 -0.0647 549 TYR A CB 4055 C CG . TYR A 556 ? 0.2944 0.3365 0.3759 0.0357 -0.0040 -0.0662 549 TYR A CG 4056 C CD1 . TYR A 556 ? 0.2752 0.3399 0.3525 0.0344 0.0170 -0.0472 549 TYR A CD1 4057 C CD2 . TYR A 556 ? 0.2428 0.3252 0.3379 0.0318 -0.0069 -0.0664 549 TYR A CD2 4058 C CE1 . TYR A 556 ? 0.2355 0.3194 0.2644 0.0406 -0.0365 -0.0322 549 TYR A CE1 4059 C CE2 . TYR A 556 ? 0.2672 0.3128 0.2984 0.0413 -0.0263 -0.0606 549 TYR A CE2 4060 C CZ . TYR A 556 ? 0.2338 0.2847 0.2362 0.0297 -0.0275 -0.0540 549 TYR A CZ 4061 O OH . TYR A 556 ? 0.2488 0.2637 0.2967 0.0518 0.0326 -0.0971 549 TYR A OH 4062 N N . PRO A 557 ? 0.2662 0.2864 0.3795 0.0317 0.0121 -0.0630 550 PRO A N 4063 C CA . PRO A 557 ? 0.2381 0.2742 0.3621 0.0388 0.0143 -0.0576 550 PRO A CA 4064 C C . PRO A 557 ? 0.2068 0.2655 0.3428 0.0467 0.0208 -0.0512 550 PRO A C 4065 O O . PRO A 557 ? 0.2264 0.2784 0.3138 0.0477 0.0475 -0.0389 550 PRO A O 4066 C CB . PRO A 557 ? 0.2201 0.2684 0.3550 0.0429 0.0189 -0.0668 550 PRO A CB 4067 C CG . PRO A 557 ? 0.2354 0.2865 0.3602 0.0474 0.0045 -0.0477 550 PRO A CG 4068 C CD . PRO A 557 ? 0.2495 0.2686 0.3779 0.0642 0.0079 -0.0664 550 PRO A CD 4069 N N . LEU A 558 ? 0.1766 0.2554 0.3129 0.0501 0.0269 -0.0500 551 LEU A N 4070 C CA . LEU A 558 ? 0.1844 0.2313 0.3166 0.0527 0.0210 -0.0498 551 LEU A CA 4071 C C . LEU A 558 ? 0.1872 0.2365 0.3113 0.0419 0.0214 -0.0467 551 LEU A C 4072 O O . LEU A 558 ? 0.2012 0.2325 0.3090 0.0305 0.0151 -0.0480 551 LEU A O 4073 C CB . LEU A 558 ? 0.1630 0.2253 0.3063 0.0596 0.0291 -0.0496 551 LEU A CB 4074 C CG . LEU A 558 ? 0.1572 0.2277 0.2890 0.0776 0.0180 -0.0590 551 LEU A CG 4075 C CD1 . LEU A 558 ? 0.2089 0.2496 0.2712 0.0790 0.0217 -0.0309 551 LEU A CD1 4076 C CD2 . LEU A 558 ? 0.0989 0.2531 0.2661 0.0467 0.0105 -0.0427 551 LEU A CD2 4077 N N . TYR A 559 ? 0.1863 0.2177 0.3121 0.0419 0.0236 -0.0473 552 TYR A N 4078 C CA . TYR A 559 ? 0.2027 0.2253 0.3064 0.0484 0.0149 -0.0418 552 TYR A CA 4079 C C . TYR A 559 ? 0.2067 0.2258 0.3008 0.0458 0.0154 -0.0481 552 TYR A C 4080 O O . TYR A 559 ? 0.2210 0.2393 0.3168 0.0509 0.0186 -0.0459 552 TYR A O 4081 C CB . TYR A 559 ? 0.1819 0.2165 0.3130 0.0427 0.0092 -0.0470 552 TYR A CB 4082 C CG . TYR A 559 ? 0.2335 0.2271 0.3087 0.0499 0.0143 -0.0381 552 TYR A CG 4083 C CD1 . TYR A 559 ? 0.1906 0.2354 0.2989 0.0337 -0.0022 -0.0505 552 TYR A CD1 4084 C CD2 . TYR A 559 ? 0.2213 0.2309 0.2793 0.0225 -0.0212 -0.0476 552 TYR A CD2 4085 C CE1 . TYR A 559 ? 0.1883 0.1847 0.2834 0.0139 -0.0283 -0.0523 552 TYR A CE1 4086 C CE2 . TYR A 559 ? 0.1583 0.1986 0.2880 0.0329 0.0293 -0.0397 552 TYR A CE2 4087 C CZ . TYR A 559 ? 0.2181 0.2076 0.2571 0.0527 0.0186 -0.0316 552 TYR A CZ 4088 O OH . TYR A 559 ? 0.2040 0.2388 0.2575 0.0473 0.0245 -0.0340 552 TYR A OH 4089 N N . HIS A 560 ? 0.2126 0.2247 0.2798 0.0443 0.0113 -0.0383 553 HIS A N 4090 C CA . HIS A 560 ? 0.2220 0.2069 0.2843 0.0449 0.0083 -0.0507 553 HIS A CA 4091 C C . HIS A 560 ? 0.2354 0.2279 0.2886 0.0486 0.0096 -0.0496 553 HIS A C 4092 O O . HIS A 560 ? 0.2430 0.2204 0.2872 0.0450 -0.0183 -0.0506 553 HIS A O 4093 C CB . HIS A 560 ? 0.1897 0.1945 0.2603 0.0521 0.0105 -0.0518 553 HIS A CB 4094 C CG . HIS A 560 ? 0.1782 0.1905 0.2414 0.0675 -0.0046 -0.0588 553 HIS A CG 4095 N ND1 . HIS A 560 ? 0.2279 0.1691 0.2266 0.0612 0.0102 -0.0524 553 HIS A ND1 4096 C CD2 . HIS A 560 ? 0.1762 0.1535 0.2894 0.0400 0.0368 -0.0565 553 HIS A CD2 4097 C CE1 . HIS A 560 ? 0.1603 0.2232 0.2409 0.0471 -0.0054 -0.0441 553 HIS A CE1 4098 N NE2 . HIS A 560 ? 0.2091 0.2082 0.2421 0.0308 0.0054 -0.0629 553 HIS A NE2 4099 N N . SER A 561 ? 0.2301 0.2416 0.3000 0.0505 0.0187 -0.0423 554 SER A N 4100 C CA . SER A 561 ? 0.2228 0.2099 0.3025 0.0373 0.0222 -0.0403 554 SER A CA 4101 C C . SER A 561 ? 0.2336 0.2454 0.3151 0.0415 0.0242 -0.0417 554 SER A C 4102 O O . SER A 561 ? 0.2163 0.2541 0.2693 0.0501 0.0434 -0.0314 554 SER A O 4103 C CB . SER A 561 ? 0.2357 0.2125 0.2949 0.0371 0.0201 -0.0406 554 SER A CB 4104 O OG A SER A 561 ? 0.2336 0.2631 0.3105 0.0327 0.0023 -0.0612 554 SER A OG 4105 O OG B SER A 561 ? 0.1845 0.1912 0.3289 0.0303 0.0056 -0.0509 554 SER A OG 4106 N N . VAL A 562 ? 0.2146 0.1866 0.3226 0.0439 0.0209 -0.0550 555 VAL A N 4107 C CA . VAL A 562 ? 0.2049 0.2285 0.3251 0.0408 0.0268 -0.0523 555 VAL A CA 4108 C C . VAL A 562 ? 0.2266 0.2247 0.3238 0.0465 0.0198 -0.0647 555 VAL A C 4109 O O . VAL A 562 ? 0.2442 0.2386 0.3354 0.0316 0.0177 -0.0788 555 VAL A O 4110 C CB . VAL A 562 ? 0.1868 0.2026 0.3172 0.0328 0.0333 -0.0590 555 VAL A CB 4111 C CG1 . VAL A 562 ? 0.1287 0.2274 0.3073 0.0703 0.0054 -0.0409 555 VAL A CG1 4112 C CG2 . VAL A 562 ? 0.1689 0.2246 0.3421 0.0226 0.0475 -0.0406 555 VAL A CG2 4113 N N . TYR A 563 ? 0.2091 0.2370 0.3226 0.0502 0.0217 -0.0770 556 TYR A N 4114 C CA . TYR A 563 ? 0.2385 0.2370 0.3192 0.0555 0.0141 -0.0729 556 TYR A CA 4115 C C . TYR A 563 ? 0.2460 0.2421 0.3313 0.0570 0.0128 -0.0726 556 TYR A C 4116 O O . TYR A 563 ? 0.2476 0.2453 0.3299 0.0635 -0.0013 -0.0524 556 TYR A O 4117 C CB . TYR A 563 ? 0.2116 0.2202 0.3057 0.0634 0.0142 -0.0784 556 TYR A CB 4118 C CG . TYR A 563 ? 0.2414 0.2305 0.3286 0.0617 0.0157 -0.0779 556 TYR A CG 4119 C CD1 . TYR A 563 ? 0.2058 0.2269 0.3375 0.0423 0.0097 -0.0886 556 TYR A CD1 4120 C CD2 . TYR A 563 ? 0.2154 0.2459 0.2987 0.0205 0.0527 -0.0882 556 TYR A CD2 4121 C CE1 . TYR A 563 ? 0.2020 0.2721 0.3373 0.0505 0.0126 -0.0887 556 TYR A CE1 4122 C CE2 . TYR A 563 ? 0.2816 0.2387 0.3452 0.0435 0.0318 -0.0867 556 TYR A CE2 4123 C CZ . TYR A 563 ? 0.2296 0.2462 0.3475 0.0726 0.0544 -0.0999 556 TYR A CZ 4124 O OH . TYR A 563 ? 0.2591 0.2884 0.3228 0.0345 0.0288 -0.1019 556 TYR A OH 4125 N N . GLU A 564 ? 0.2383 0.2132 0.3314 0.0627 0.0122 -0.0695 557 GLU A N 4126 C CA . GLU A 564 ? 0.2484 0.2250 0.3320 0.0646 0.0258 -0.0593 557 GLU A CA 4127 C C . GLU A 564 ? 0.2513 0.2266 0.3207 0.0657 0.0201 -0.0557 557 GLU A C 4128 O O . GLU A 564 ? 0.2435 0.2500 0.2980 0.0603 0.0464 -0.0585 557 GLU A O 4129 C CB . GLU A 564 ? 0.2911 0.2179 0.3363 0.0535 0.0272 -0.0685 557 GLU A CB 4130 C CG . GLU A 564 ? 0.3156 0.2107 0.3983 0.0583 0.0294 -0.0603 557 GLU A CG 4131 C CD . GLU A 564 ? 0.2231 0.2593 0.3429 0.0910 0.0355 -0.0408 557 GLU A CD 4132 O OE1 . GLU A 564 ? 0.3353 0.2460 0.3426 0.0666 0.1084 -0.0496 557 GLU A OE1 4133 O OE2 . GLU A 564 ? 0.2848 0.2365 0.3425 0.0348 0.0256 -0.0369 557 GLU A OE2 4134 N N . THR A 565 ? 0.2558 0.2338 0.3046 0.0521 0.0142 -0.0528 558 THR A N 4135 C CA . THR A 565 ? 0.2570 0.2279 0.3135 0.0625 0.0081 -0.0441 558 THR A CA 4136 C C . THR A 565 ? 0.2577 0.2263 0.3170 0.0604 -0.0007 -0.0383 558 THR A C 4137 O O . THR A 565 ? 0.2524 0.2169 0.3081 0.0688 0.0016 -0.0296 558 THR A O 4138 C CB . THR A 565 ? 0.2760 0.2250 0.3165 0.0520 0.0045 -0.0489 558 THR A CB 4139 O OG1 . THR A 565 ? 0.2817 0.2176 0.3560 0.0711 0.0195 -0.0631 558 THR A OG1 4140 C CG2 . THR A 565 ? 0.2653 0.2161 0.3067 0.0348 -0.0069 -0.0497 558 THR A CG2 4141 N N . TYR A 566 ? 0.2470 0.2352 0.3172 0.0697 -0.0070 -0.0284 559 TYR A N 4142 C CA . TYR A 566 ? 0.2702 0.2401 0.3338 0.0642 -0.0007 -0.0212 559 TYR A CA 4143 C C . TYR A 566 ? 0.2735 0.2341 0.3380 0.0694 -0.0050 -0.0152 559 TYR A C 4144 O O . TYR A 566 ? 0.2858 0.2146 0.3420 0.0663 -0.0093 -0.0057 559 TYR A O 4145 C CB . TYR A 566 ? 0.2756 0.2279 0.3409 0.0464 -0.0025 -0.0241 559 TYR A CB 4146 C CG . TYR A 566 ? 0.2865 0.2427 0.3670 0.0459 -0.0177 -0.0101 559 TYR A CG 4147 C CD1 . TYR A 566 ? 0.3038 0.2644 0.3650 0.0621 -0.0015 0.0016 559 TYR A CD1 4148 C CD2 . TYR A 566 ? 0.3251 0.2981 0.4030 0.0608 -0.0111 -0.0134 559 TYR A CD2 4149 C CE1 . TYR A 566 ? 0.3440 0.3006 0.4130 0.0649 -0.0294 -0.0202 559 TYR A CE1 4150 C CE2 . TYR A 566 ? 0.3390 0.3261 0.4172 0.0724 -0.0087 -0.0186 559 TYR A CE2 4151 C CZ . TYR A 566 ? 0.3606 0.2996 0.4366 0.0711 -0.0305 -0.0295 559 TYR A CZ 4152 O OH . TYR A 566 ? 0.3951 0.3055 0.4456 0.0938 -0.0155 -0.0228 559 TYR A OH 4153 N N . GLU A 567 ? 0.2592 0.2261 0.3356 0.0852 0.0096 -0.0237 560 GLU A N 4154 C CA . GLU A 567 ? 0.2747 0.2450 0.3533 0.0810 -0.0050 -0.0353 560 GLU A CA 4155 C C . GLU A 567 ? 0.2629 0.2394 0.3459 0.0820 -0.0032 -0.0453 560 GLU A C 4156 O O . GLU A 567 ? 0.2760 0.2602 0.3588 0.0900 -0.0069 -0.0559 560 GLU A O 4157 C CB . GLU A 567 ? 0.2649 0.2366 0.3593 0.0841 0.0067 -0.0417 560 GLU A CB 4158 C CG . GLU A 567 ? 0.2936 0.2372 0.3904 0.0883 -0.0143 -0.0146 560 GLU A CG 4159 C CD . GLU A 567 ? 0.3165 0.2694 0.4096 0.0740 -0.0012 -0.0205 560 GLU A CD 4160 O OE1 . GLU A 567 ? 0.3031 0.2712 0.4207 0.0928 -0.0327 0.0003 560 GLU A OE1 4161 O OE2 . GLU A 567 ? 0.3555 0.2632 0.3813 0.0588 0.0175 -0.0595 560 GLU A OE2 4162 N N . LEU A 568 ? 0.2546 0.2228 0.3487 0.0854 -0.0089 -0.0481 561 LEU A N 4163 C CA . LEU A 568 ? 0.2625 0.2315 0.3464 0.0768 -0.0181 -0.0365 561 LEU A CA 4164 C C . LEU A 568 ? 0.2671 0.2457 0.3560 0.0716 -0.0221 -0.0351 561 LEU A C 4165 O O . LEU A 568 ? 0.2564 0.2551 0.3619 0.0674 -0.0064 -0.0207 561 LEU A O 4166 C CB . LEU A 568 ? 0.2560 0.2212 0.3416 0.0639 -0.0292 -0.0230 561 LEU A CB 4167 C CG . LEU A 568 ? 0.2564 0.2475 0.3572 0.0695 -0.0435 -0.0001 561 LEU A CG 4168 C CD1 . LEU A 568 ? 0.2551 0.2352 0.2907 0.0393 -0.0173 -0.0147 561 LEU A CD1 4169 C CD2 . LEU A 568 ? 0.2355 0.1870 0.3376 0.0694 -0.0226 0.0093 561 LEU A CD2 4170 N N . VAL A 569 ? 0.2591 0.2429 0.3468 0.0855 -0.0184 -0.0354 562 VAL A N 4171 C CA . VAL A 569 ? 0.2684 0.2398 0.3430 0.0837 -0.0241 -0.0408 562 VAL A CA 4172 C C . VAL A 569 ? 0.2780 0.2664 0.3731 0.0915 -0.0237 -0.0393 562 VAL A C 4173 O O . VAL A 569 ? 0.2703 0.2745 0.3798 0.0897 -0.0290 -0.0228 562 VAL A O 4174 C CB . VAL A 569 ? 0.2573 0.2425 0.3210 0.0815 -0.0266 -0.0489 562 VAL A CB 4175 C CG1 . VAL A 569 ? 0.2671 0.2222 0.3206 0.0627 0.0052 -0.0733 562 VAL A CG1 4176 C CG2 . VAL A 569 ? 0.2847 0.2249 0.3126 0.0823 -0.0218 -0.0372 562 VAL A CG2 4177 N N . GLU A 570 ? 0.2859 0.2616 0.4009 0.1015 -0.0180 -0.0351 563 GLU A N 4178 C CA . GLU A 570 ? 0.3188 0.3045 0.4172 0.1006 -0.0273 -0.0398 563 GLU A CA 4179 C C . GLU A 570 ? 0.3199 0.3055 0.4205 0.1009 -0.0242 -0.0482 563 GLU A C 4180 O O . GLU A 570 ? 0.3499 0.3231 0.4170 0.1037 -0.0266 -0.0527 563 GLU A O 4181 C CB . GLU A 570 ? 0.3269 0.3109 0.4338 0.0969 -0.0180 -0.0331 563 GLU A CB 4182 C CG . GLU A 570 ? 0.3855 0.3816 0.4794 0.1399 -0.0493 -0.0306 563 GLU A CG 4183 C CD . GLU A 570 ? 0.4426 0.4836 0.5602 0.1657 -0.0623 -0.0333 563 GLU A CD 4184 O OE1 . GLU A 570 ? 0.4712 0.4828 0.6096 0.2099 -0.0719 -0.0723 563 GLU A OE1 4185 O OE2 . GLU A 570 ? 0.4970 0.5323 0.5645 0.1376 -0.0742 0.0061 563 GLU A OE2 4186 N N . LYS A 571 ? 0.3162 0.2878 0.4100 0.0978 -0.0271 -0.0599 564 LYS A N 4187 C CA . LYS A 571 ? 0.2974 0.2784 0.4191 0.1010 -0.0296 -0.0540 564 LYS A CA 4188 C C . LYS A 571 ? 0.2938 0.2982 0.4242 0.1020 -0.0338 -0.0556 564 LYS A C 4189 O O . LYS A 571 ? 0.2833 0.3077 0.4085 0.0886 -0.0605 -0.0466 564 LYS A O 4190 C CB . LYS A 571 ? 0.3044 0.2714 0.4208 0.1160 -0.0226 -0.0599 564 LYS A CB 4191 C CG . LYS A 571 ? 0.3306 0.2936 0.4516 0.0755 0.0057 -0.0566 564 LYS A CG 4192 C CD . LYS A 571 ? 0.4454 0.3211 0.5083 0.0562 0.0100 -0.0734 564 LYS A CD 4193 C CE . LYS A 571 ? 0.4650 0.3387 0.5415 0.0657 -0.0161 -0.0486 564 LYS A CE 4194 N NZ . LYS A 571 ? 0.5279 0.3296 0.5569 0.0667 -0.0113 -0.0626 564 LYS A NZ 4195 N N . PHE A 572 ? 0.2878 0.2722 0.4093 0.1072 -0.0287 -0.0586 565 PHE A N 4196 C CA . PHE A 572 ? 0.2890 0.2871 0.4296 0.0955 -0.0278 -0.0665 565 PHE A CA 4197 C C . PHE A 572 ? 0.2852 0.2942 0.4451 0.0939 -0.0338 -0.0590 565 PHE A C 4198 O O . PHE A 572 ? 0.3111 0.3190 0.4965 0.0870 -0.0333 -0.0612 565 PHE A O 4199 C CB . PHE A 572 ? 0.2832 0.2820 0.4255 0.0927 -0.0174 -0.0569 565 PHE A CB 4200 C CG . PHE A 572 ? 0.2844 0.3287 0.4137 0.0931 -0.0059 -0.0827 565 PHE A CG 4201 C CD1 . PHE A 572 ? 0.2817 0.3395 0.4123 0.1144 -0.0002 -0.0842 565 PHE A CD1 4202 C CD2 . PHE A 572 ? 0.2444 0.3279 0.4102 0.0883 -0.0074 -0.0822 565 PHE A CD2 4203 C CE1 . PHE A 572 ? 0.2524 0.3621 0.4371 0.1255 0.0241 -0.1095 565 PHE A CE1 4204 C CE2 . PHE A 572 ? 0.2270 0.3417 0.4301 0.1278 0.0017 -0.0714 565 PHE A CE2 4205 C CZ . PHE A 572 ? 0.2133 0.3976 0.4365 0.1223 0.0131 -0.0997 565 PHE A CZ 4206 N N . TYR A 573 ? 0.2664 0.2918 0.4135 0.1027 -0.0380 -0.0543 566 TYR A N 4207 C CA . TYR A 573 ? 0.2607 0.2861 0.3950 0.1011 -0.0400 -0.0517 566 TYR A CA 4208 C C . TYR A 573 ? 0.2623 0.2877 0.3854 0.1063 -0.0344 -0.0487 566 TYR A C 4209 O O . TYR A 573 ? 0.2464 0.2965 0.3826 0.1055 -0.0177 -0.0557 566 TYR A O 4210 C CB . TYR A 573 ? 0.2402 0.2876 0.3926 0.1088 -0.0366 -0.0436 566 TYR A CB 4211 C CG . TYR A 573 ? 0.2367 0.2876 0.3865 0.0804 -0.0319 -0.0509 566 TYR A CG 4212 C CD1 . TYR A 573 ? 0.2034 0.2803 0.3800 0.0731 -0.0165 -0.0565 566 TYR A CD1 4213 C CD2 . TYR A 573 ? 0.2879 0.2795 0.3862 0.0765 -0.0332 -0.0551 566 TYR A CD2 4214 C CE1 . TYR A 573 ? 0.2202 0.2925 0.3554 0.0766 -0.0341 -0.0707 566 TYR A CE1 4215 C CE2 . TYR A 573 ? 0.2504 0.2889 0.3522 0.0882 -0.0361 -0.0813 566 TYR A CE2 4216 C CZ . TYR A 573 ? 0.2171 0.3052 0.3452 0.0746 -0.0465 -0.0569 566 TYR A CZ 4217 O OH . TYR A 573 ? 0.2579 0.3454 0.3562 0.0417 0.0001 -0.0695 566 TYR A OH 4218 N N . ASP A 574 ? 0.2605 0.2750 0.3787 0.1111 -0.0387 -0.0443 567 ASP A N 4219 C CA . ASP A 574 ? 0.2838 0.2822 0.3739 0.1084 -0.0439 -0.0399 567 ASP A CA 4220 C C . ASP A 574 ? 0.3002 0.2888 0.3880 0.1164 -0.0531 -0.0365 567 ASP A C 4221 O O . ASP A 574 ? 0.3036 0.2782 0.3811 0.1143 -0.0617 -0.0389 567 ASP A O 4222 C CB . ASP A 574 ? 0.2804 0.2755 0.3549 0.1056 -0.0400 -0.0474 567 ASP A CB 4223 C CG . ASP A 574 ? 0.2868 0.2873 0.3653 0.1066 -0.0180 -0.0409 567 ASP A CG 4224 O OD1 . ASP A 574 ? 0.2726 0.3278 0.3094 0.0624 0.0394 -0.0378 567 ASP A OD1 4225 O OD2 . ASP A 574 ? 0.3177 0.2889 0.3715 0.1299 0.0137 -0.0632 567 ASP A OD2 4226 N N . PRO A 575 ? 0.3133 0.3034 0.4099 0.1266 -0.0595 -0.0288 568 PRO A N 4227 C CA . PRO A 575 ? 0.3325 0.3068 0.4224 0.1330 -0.0621 -0.0243 568 PRO A CA 4228 C C . PRO A 575 ? 0.3374 0.3180 0.4247 0.1382 -0.0661 -0.0261 568 PRO A C 4229 O O . PRO A 575 ? 0.3622 0.3233 0.4429 0.1345 -0.0618 -0.0287 568 PRO A O 4230 C CB . PRO A 575 ? 0.3116 0.3153 0.4110 0.1300 -0.0690 -0.0207 568 PRO A CB 4231 C CG . PRO A 575 ? 0.3366 0.3207 0.4307 0.1281 -0.0649 -0.0109 568 PRO A CG 4232 C CD . PRO A 575 ? 0.3203 0.3049 0.4269 0.1307 -0.0516 -0.0284 568 PRO A CD 4233 N N A MET A 576 ? 0.3421 0.3214 0.4263 0.1434 -0.0711 -0.0250 569 MET A N 4234 N N B MET A 576 ? 0.3437 0.3159 0.4210 0.1375 -0.0702 -0.0246 569 MET A N 4235 C CA A MET A 576 ? 0.3451 0.3372 0.4175 0.1451 -0.0730 -0.0212 569 MET A CA 4236 C CA B MET A 576 ? 0.3441 0.3197 0.4119 0.1367 -0.0737 -0.0217 569 MET A CA 4237 C C A MET A 576 ? 0.3422 0.3218 0.3998 0.1332 -0.0718 -0.0194 569 MET A C 4238 C C B MET A 576 ? 0.3416 0.3112 0.3967 0.1294 -0.0731 -0.0199 569 MET A C 4239 O O A MET A 576 ? 0.3274 0.3235 0.3843 0.1385 -0.0756 -0.0112 569 MET A O 4240 O O B MET A 576 ? 0.3377 0.3116 0.3907 0.1308 -0.0744 -0.0159 569 MET A O 4241 C CB A MET A 576 ? 0.3607 0.3550 0.4251 0.1439 -0.0749 -0.0247 569 MET A CB 4242 C CB B MET A 576 ? 0.3507 0.3274 0.4164 0.1367 -0.0752 -0.0247 569 MET A CB 4243 C CG A MET A 576 ? 0.3961 0.4438 0.4769 0.1707 -0.0831 -0.0323 569 MET A CG 4244 C CG B MET A 576 ? 0.3636 0.3587 0.4441 0.1480 -0.0794 -0.0254 569 MET A CG 4245 S SD A MET A 576 ? 0.5092 0.5348 0.5635 0.1962 -0.0746 -0.0240 569 MET A SD 4246 S SD B MET A 576 ? 0.3801 0.4350 0.4871 0.1473 -0.0896 -0.0504 569 MET A SD 4247 C CE A MET A 576 ? 0.5377 0.5674 0.5504 0.1864 -0.0834 -0.0055 569 MET A CE 4248 C CE B MET A 576 ? 0.3780 0.3846 0.4966 0.1687 -0.0864 -0.0305 569 MET A CE 4249 N N . PHE A 577 ? 0.3269 0.3035 0.3805 0.1265 -0.0728 -0.0164 570 PHE A N 4250 C CA . PHE A 577 ? 0.3218 0.2892 0.3622 0.1095 -0.0683 -0.0203 570 PHE A CA 4251 C C . PHE A 577 ? 0.3112 0.2915 0.3427 0.1054 -0.0716 -0.0207 570 PHE A C 4252 O O . PHE A 577 ? 0.2680 0.2874 0.3342 0.1001 -0.0542 -0.0307 570 PHE A O 4253 C CB . PHE A 577 ? 0.3232 0.2766 0.3676 0.1047 -0.0643 -0.0248 570 PHE A CB 4254 C CG . PHE A 577 ? 0.3268 0.2912 0.3470 0.0848 -0.0500 -0.0221 570 PHE A CG 4255 C CD1 . PHE A 577 ? 0.3352 0.2729 0.3442 0.0866 -0.0480 -0.0282 570 PHE A CD1 4256 C CD2 . PHE A 577 ? 0.3042 0.2332 0.3536 0.0764 -0.0492 -0.0271 570 PHE A CD2 4257 C CE1 . PHE A 577 ? 0.3497 0.2507 0.3229 0.0803 -0.0472 -0.0295 570 PHE A CE1 4258 C CE2 . PHE A 577 ? 0.3311 0.2836 0.3318 0.0970 -0.0479 -0.0212 570 PHE A CE2 4259 C CZ . PHE A 577 ? 0.3106 0.2843 0.3249 0.1013 -0.0590 -0.0430 570 PHE A CZ 4260 N N . LYS A 578 ? 0.2929 0.2941 0.3236 0.1066 -0.0794 -0.0129 571 LYS A N 4261 C CA . LYS A 578 ? 0.2949 0.2940 0.3315 0.1078 -0.0877 -0.0167 571 LYS A CA 4262 C C . LYS A 578 ? 0.2849 0.2901 0.3242 0.1101 -0.0868 -0.0192 571 LYS A C 4263 O O . LYS A 578 ? 0.2918 0.2942 0.3131 0.1090 -0.0884 -0.0228 571 LYS A O 4264 C CB . LYS A 578 ? 0.2842 0.3062 0.3323 0.1135 -0.0943 -0.0070 571 LYS A CB 4265 C CG . LYS A 578 ? 0.2833 0.3142 0.3584 0.1218 -0.1017 -0.0299 571 LYS A CG 4266 C CD . LYS A 578 ? 0.3005 0.4117 0.4392 0.0864 -0.1100 -0.0532 571 LYS A CD 4267 C CE . LYS A 578 ? 0.3467 0.4127 0.4510 0.1027 -0.0957 -0.0577 571 LYS A CE 4268 N NZ . LYS A 578 ? 0.3595 0.4698 0.4581 0.1069 -0.1085 -0.0220 571 LYS A NZ 4269 N N . TYR A 579 ? 0.2719 0.2876 0.3144 0.0993 -0.0829 -0.0270 572 TYR A N 4270 C CA . TYR A 579 ? 0.2833 0.2948 0.3181 0.0981 -0.0682 -0.0281 572 TYR A CA 4271 C C . TYR A 579 ? 0.2878 0.2857 0.3029 0.0979 -0.0592 -0.0295 572 TYR A C 4272 O O . TYR A 579 ? 0.3105 0.3046 0.3119 0.0932 -0.0492 -0.0270 572 TYR A O 4273 C CB . TYR A 579 ? 0.2845 0.2987 0.3320 0.0916 -0.0618 -0.0313 572 TYR A CB 4274 C CG . TYR A 579 ? 0.2905 0.3096 0.3640 0.0995 -0.0512 -0.0267 572 TYR A CG 4275 C CD1 . TYR A 579 ? 0.2881 0.3184 0.4081 0.0918 -0.0421 -0.0375 572 TYR A CD1 4276 C CD2 . TYR A 579 ? 0.2956 0.3423 0.3718 0.1031 -0.0408 -0.0342 572 TYR A CD2 4277 C CE1 . TYR A 579 ? 0.3021 0.3707 0.4274 0.0971 -0.0697 -0.0069 572 TYR A CE1 4278 C CE2 . TYR A 579 ? 0.2901 0.3716 0.4265 0.1064 -0.0553 -0.0212 572 TYR A CE2 4279 C CZ . TYR A 579 ? 0.3281 0.3815 0.4312 0.0993 -0.0539 -0.0251 572 TYR A CZ 4280 O OH . TYR A 579 ? 0.3394 0.4711 0.4548 0.0742 -0.0840 0.0056 572 TYR A OH 4281 N N . HIS A 580 ? 0.2842 0.2684 0.2924 0.0946 -0.0579 -0.0252 573 HIS A N 4282 C CA . HIS A 580 ? 0.2884 0.2608 0.2883 0.0879 -0.0604 -0.0278 573 HIS A CA 4283 C C . HIS A 580 ? 0.2885 0.2511 0.2840 0.0824 -0.0656 -0.0287 573 HIS A C 4284 O O . HIS A 580 ? 0.2971 0.2409 0.2684 0.0678 -0.0583 -0.0298 573 HIS A O 4285 C CB . HIS A 580 ? 0.2795 0.2478 0.2819 0.0928 -0.0721 -0.0368 573 HIS A CB 4286 C CG . HIS A 580 ? 0.3079 0.2493 0.3004 0.0900 -0.0660 -0.0344 573 HIS A CG 4287 N ND1 . HIS A 580 ? 0.3185 0.2463 0.3029 0.0934 -0.0855 -0.0287 573 HIS A ND1 4288 C CD2 . HIS A 580 ? 0.3248 0.2847 0.3111 0.1031 -0.0782 -0.0273 573 HIS A CD2 4289 C CE1 . HIS A 580 ? 0.3329 0.2890 0.3247 0.0820 -0.0953 -0.0028 573 HIS A CE1 4290 N NE2 . HIS A 580 ? 0.3411 0.2996 0.3426 0.0938 -0.0710 -0.0460 573 HIS A NE2 4291 N N . LEU A 581 ? 0.3027 0.2641 0.2762 0.0791 -0.0654 -0.0207 574 LEU A N 4292 C CA . LEU A 581 ? 0.3126 0.2713 0.2797 0.0949 -0.0693 -0.0254 574 LEU A CA 4293 C C . LEU A 581 ? 0.3212 0.2878 0.2978 0.0933 -0.0690 -0.0250 574 LEU A C 4294 O O . LEU A 581 ? 0.3196 0.2985 0.2850 0.0994 -0.0568 -0.0423 574 LEU A O 4295 C CB . LEU A 581 ? 0.3193 0.2761 0.2638 0.1004 -0.0501 -0.0188 574 LEU A CB 4296 C CG . LEU A 581 ? 0.3192 0.2787 0.2558 0.1143 -0.0833 -0.0298 574 LEU A CG 4297 C CD1 . LEU A 581 ? 0.3195 0.2605 0.2301 0.1588 -0.0417 -0.0418 574 LEU A CD1 4298 C CD2 . LEU A 581 ? 0.3324 0.2484 0.2627 0.1214 -0.0951 -0.0031 574 LEU A CD2 4299 N N . THR A 582 ? 0.3203 0.2912 0.3024 0.0882 -0.0682 -0.0175 575 THR A N 4300 C CA . THR A 582 ? 0.3113 0.2779 0.2944 0.0885 -0.0792 -0.0207 575 THR A CA 4301 C C . THR A 582 ? 0.3078 0.2723 0.2840 0.0839 -0.0622 -0.0173 575 THR A C 4302 O O . THR A 582 ? 0.3183 0.2806 0.2738 0.0757 -0.0539 -0.0135 575 THR A O 4303 C CB . THR A 582 ? 0.3065 0.2699 0.2923 0.0951 -0.0731 -0.0190 575 THR A CB 4304 O OG1 . THR A 582 ? 0.3047 0.3005 0.3273 0.0944 -0.1145 -0.0147 575 THR A OG1 4305 C CG2 . THR A 582 ? 0.3204 0.2474 0.2502 0.1062 -0.0868 0.0036 575 THR A CG2 4306 N N . VAL A 583 ? 0.2918 0.2784 0.2738 0.0795 -0.0697 -0.0223 576 VAL A N 4307 C CA . VAL A 583 ? 0.2808 0.2785 0.2692 0.0796 -0.0682 -0.0254 576 VAL A CA 4308 C C . VAL A 583 ? 0.3016 0.2754 0.2631 0.0855 -0.0693 -0.0217 576 VAL A C 4309 O O . VAL A 583 ? 0.2935 0.2894 0.2602 0.0919 -0.0833 -0.0150 576 VAL A O 4310 C CB . VAL A 583 ? 0.2708 0.2868 0.2563 0.0790 -0.0680 -0.0218 576 VAL A CB 4311 C CG1 . VAL A 583 ? 0.2252 0.2742 0.2360 0.0873 -0.0598 -0.0361 576 VAL A CG1 4312 C CG2 . VAL A 583 ? 0.2427 0.3199 0.2629 0.0745 -0.0652 -0.0446 576 VAL A CG2 4313 N N . ALA A 584 ? 0.3050 0.2732 0.2549 0.0749 -0.0756 -0.0174 577 ALA A N 4314 C CA . ALA A 584 ? 0.3005 0.2500 0.2414 0.0857 -0.0674 -0.0220 577 ALA A CA 4315 C C . ALA A 584 ? 0.3073 0.2453 0.2542 0.0890 -0.0675 -0.0115 577 ALA A C 4316 O O . ALA A 584 ? 0.3094 0.2238 0.2509 0.1035 -0.0548 -0.0178 577 ALA A O 4317 C CB . ALA A 584 ? 0.2862 0.2239 0.2392 0.0731 -0.0741 -0.0145 577 ALA A CB 4318 N N . GLN A 585 ? 0.3117 0.2469 0.2454 0.0913 -0.0798 -0.0079 578 GLN A N 4319 C CA . GLN A 585 ? 0.3158 0.2429 0.2419 0.1045 -0.0752 -0.0180 578 GLN A CA 4320 C C . GLN A 585 ? 0.2969 0.2498 0.2420 0.1010 -0.0813 -0.0131 578 GLN A C 4321 O O . GLN A 585 ? 0.3120 0.2226 0.2472 0.0882 -0.0884 -0.0146 578 GLN A O 4322 C CB . GLN A 585 ? 0.3064 0.2338 0.2503 0.1193 -0.0810 -0.0221 578 GLN A CB 4323 C CG . GLN A 585 ? 0.3323 0.2779 0.2385 0.1269 -0.0704 -0.0076 578 GLN A CG 4324 C CD . GLN A 585 ? 0.3556 0.3001 0.3193 0.1210 -0.1039 -0.0133 578 GLN A CD 4325 O OE1 . GLN A 585 ? 0.3603 0.2959 0.3927 0.1212 -0.0845 0.0233 578 GLN A OE1 4326 N NE2 . GLN A 585 ? 0.3465 0.3269 0.2792 0.1116 -0.1321 -0.0022 578 GLN A NE2 4327 N N . VAL A 586 ? 0.2884 0.2529 0.2356 0.0948 -0.0865 -0.0192 579 VAL A N 4328 C CA . VAL A 586 ? 0.2788 0.2519 0.2388 0.0949 -0.0694 -0.0134 579 VAL A CA 4329 C C . VAL A 586 ? 0.2809 0.2534 0.2387 0.0828 -0.0592 -0.0251 579 VAL A C 4330 O O . VAL A 586 ? 0.2942 0.2572 0.2405 0.0724 -0.0533 -0.0275 579 VAL A O 4331 C CB . VAL A 586 ? 0.2687 0.2610 0.2486 0.0976 -0.0671 -0.0096 579 VAL A CB 4332 C CG1 . VAL A 586 ? 0.2372 0.2342 0.2137 0.1253 -0.0582 -0.0091 579 VAL A CG1 4333 C CG2 . VAL A 586 ? 0.2503 0.2620 0.2722 0.1052 -0.0737 -0.0017 579 VAL A CG2 4334 N N . ARG A 587 ? 0.2777 0.2508 0.2173 0.0727 -0.0514 -0.0304 580 ARG A N 4335 C CA . ARG A 587 ? 0.2681 0.2505 0.2133 0.0769 -0.0481 -0.0326 580 ARG A CA 4336 C C . ARG A 587 ? 0.2854 0.2481 0.2139 0.0807 -0.0508 -0.0315 580 ARG A C 4337 O O . ARG A 587 ? 0.2668 0.2287 0.2206 0.0821 -0.0417 -0.0175 580 ARG A O 4338 C CB . ARG A 587 ? 0.2504 0.2253 0.2099 0.0738 -0.0445 -0.0444 580 ARG A CB 4339 C CG . ARG A 587 ? 0.2626 0.2140 0.1867 0.0747 -0.0576 -0.0447 580 ARG A CG 4340 C CD . ARG A 587 ? 0.2187 0.2178 0.2091 0.0641 -0.0234 -0.0539 580 ARG A CD 4341 N NE . ARG A 587 ? 0.2384 0.2155 0.1951 0.0161 -0.0454 -0.0524 580 ARG A NE 4342 C CZ . ARG A 587 ? 0.2494 0.2202 0.2373 0.0483 -0.0016 -0.0496 580 ARG A CZ 4343 N NH1 . ARG A 587 ? 0.2839 0.2347 0.2257 -0.0079 -0.0071 -0.0761 580 ARG A NH1 4344 N NH2 . ARG A 587 ? 0.2212 0.2408 0.1796 0.0482 -0.0252 -0.0435 580 ARG A NH2 4345 N N . GLY A 588 ? 0.2936 0.2386 0.2088 0.0759 -0.0576 -0.0261 581 GLY A N 4346 C CA . GLY A 588 ? 0.3029 0.2500 0.2015 0.0756 -0.0508 -0.0311 581 GLY A CA 4347 C C . GLY A 588 ? 0.3163 0.2525 0.2101 0.0856 -0.0537 -0.0186 581 GLY A C 4348 O O . GLY A 588 ? 0.3020 0.2516 0.1992 0.1014 -0.0488 -0.0025 581 GLY A O 4349 N N . GLY A 589 ? 0.3231 0.2544 0.2070 0.0803 -0.0658 -0.0161 582 GLY A N 4350 C CA . GLY A 589 ? 0.3280 0.2395 0.1880 0.0938 -0.0578 -0.0275 582 GLY A CA 4351 C C . GLY A 589 ? 0.3287 0.2512 0.1910 0.0884 -0.0517 -0.0274 582 GLY A C 4352 O O . GLY A 589 ? 0.3388 0.2424 0.1676 0.0891 -0.0472 -0.0438 582 GLY A O 4353 N N . MET A 590 ? 0.3049 0.2488 0.1835 0.0812 -0.0552 -0.0260 583 MET A N 4354 C CA . MET A 590 ? 0.3000 0.2544 0.1971 0.0825 -0.0470 -0.0059 583 MET A CA 4355 C C . MET A 590 ? 0.3082 0.2471 0.1955 0.0847 -0.0351 -0.0086 583 MET A C 4356 O O . MET A 590 ? 0.3105 0.2290 0.2018 0.0834 -0.0333 0.0185 583 MET A O 4357 C CB . MET A 590 ? 0.2954 0.2605 0.2049 0.0784 -0.0357 -0.0042 583 MET A CB 4358 C CG . MET A 590 ? 0.2940 0.3062 0.2256 0.0782 -0.0424 0.0335 583 MET A CG 4359 S SD . MET A 590 ? 0.3107 0.3161 0.2713 0.0810 -0.0274 0.0017 583 MET A SD 4360 C CE . MET A 590 ? 0.2435 0.2669 0.2630 0.0670 -0.0378 0.0318 583 MET A CE 4361 N N . VAL A 591 ? 0.2970 0.2516 0.1775 0.0696 -0.0424 -0.0064 584 VAL A N 4362 C CA . VAL A 591 ? 0.3174 0.2416 0.1824 0.0795 -0.0368 -0.0093 584 VAL A CA 4363 C C . VAL A 591 ? 0.3265 0.2493 0.1990 0.0830 -0.0431 -0.0095 584 VAL A C 4364 O O . VAL A 591 ? 0.3329 0.2536 0.2184 0.0887 -0.0394 -0.0043 584 VAL A O 4365 C CB . VAL A 591 ? 0.3058 0.2565 0.1767 0.0694 -0.0443 -0.0115 584 VAL A CB 4366 C CG1 . VAL A 591 ? 0.2924 0.1921 0.1581 0.0910 -0.0320 0.0030 584 VAL A CG1 4367 C CG2 . VAL A 591 ? 0.3053 0.2197 0.1808 0.0596 -0.0328 -0.0265 584 VAL A CG2 4368 N N . PHE A 592 ? 0.3232 0.2565 0.1923 0.0881 -0.0599 -0.0067 585 PHE A N 4369 C CA . PHE A 592 ? 0.3407 0.2697 0.1795 0.1093 -0.0652 -0.0006 585 PHE A CA 4370 C C . PHE A 592 ? 0.3565 0.2865 0.2054 0.1098 -0.0630 -0.0007 585 PHE A C 4371 O O . PHE A 592 ? 0.3690 0.2828 0.1945 0.1046 -0.0637 -0.0026 585 PHE A O 4372 C CB . PHE A 592 ? 0.3369 0.2763 0.1850 0.1169 -0.0502 0.0000 585 PHE A CB 4373 C CG . PHE A 592 ? 0.3525 0.3055 0.1779 0.1362 -0.1008 0.0061 585 PHE A CG 4374 C CD1 . PHE A 592 ? 0.3586 0.3034 0.2044 0.1548 -0.0893 0.0059 585 PHE A CD1 4375 C CD2 . PHE A 592 ? 0.3704 0.3269 0.2075 0.1375 -0.0697 -0.0259 585 PHE A CD2 4376 C CE1 . PHE A 592 ? 0.3597 0.3183 0.2263 0.1818 -0.0828 0.0231 585 PHE A CE1 4377 C CE2 . PHE A 592 ? 0.3943 0.3303 0.2349 0.1467 -0.0585 0.0236 585 PHE A CE2 4378 C CZ . PHE A 592 ? 0.3860 0.3299 0.2636 0.1646 -0.0640 0.0174 585 PHE A CZ 4379 N N . GLU A 593 ? 0.3820 0.2984 0.2124 0.1087 -0.0619 0.0100 586 GLU A N 4380 C CA . GLU A 593 ? 0.3926 0.3153 0.2166 0.1060 -0.0672 -0.0067 586 GLU A CA 4381 C C . GLU A 593 ? 0.3773 0.2977 0.2157 0.1040 -0.0509 -0.0129 586 GLU A C 4382 O O . GLU A 593 ? 0.3749 0.2907 0.2104 0.1088 -0.0315 -0.0254 586 GLU A O 4383 C CB . GLU A 593 ? 0.4057 0.3408 0.2059 0.0932 -0.0783 0.0039 586 GLU A CB 4384 C CG . GLU A 593 ? 0.5123 0.4634 0.3522 0.0763 -0.0881 -0.0031 586 GLU A CG 4385 C CD . GLU A 593 ? 0.6628 0.5403 0.3721 0.0599 -0.0925 -0.0462 586 GLU A CD 4386 O OE1 . GLU A 593 ? 0.7168 0.5645 0.3778 0.0660 -0.1487 -0.0174 586 GLU A OE1 4387 O OE2 . GLU A 593 ? 0.6479 0.5641 0.5342 0.0922 -0.0877 -0.0258 586 GLU A OE2 4388 N N . LEU A 594 ? 0.3584 0.2835 0.1807 0.1018 -0.0401 -0.0188 587 LEU A N 4389 C CA . LEU A 594 ? 0.3639 0.2632 0.1909 0.0949 -0.0348 -0.0177 587 LEU A CA 4390 C C . LEU A 594 ? 0.3668 0.2705 0.1923 0.0991 -0.0384 -0.0149 587 LEU A C 4391 O O . LEU A 594 ? 0.3610 0.2529 0.1978 0.0839 -0.0525 -0.0118 587 LEU A O 4392 C CB . LEU A 594 ? 0.3607 0.2584 0.1797 0.0965 -0.0215 -0.0054 587 LEU A CB 4393 C CG . LEU A 594 ? 0.3662 0.2240 0.1822 0.1046 0.0028 -0.0226 587 LEU A CG 4394 C CD1 . LEU A 594 ? 0.2774 0.2372 0.1471 0.1104 -0.0523 -0.0415 587 LEU A CD1 4395 C CD2 . LEU A 594 ? 0.3172 0.2093 0.2173 0.1141 -0.0258 0.0010 587 LEU A CD2 4396 N N . ALA A 595 ? 0.3727 0.2583 0.1804 0.0911 -0.0430 -0.0074 588 ALA A N 4397 C CA . ALA A 595 ? 0.3781 0.2755 0.1866 0.1013 -0.0483 -0.0074 588 ALA A CA 4398 C C . ALA A 595 ? 0.3941 0.2880 0.1961 0.1104 -0.0476 -0.0026 588 ALA A C 4399 O O . ALA A 595 ? 0.3978 0.2963 0.1727 0.0973 -0.0445 -0.0062 588 ALA A O 4400 C CB . ALA A 595 ? 0.3674 0.2593 0.1835 0.1020 -0.0618 0.0169 588 ALA A CB 4401 N N . ASN A 596 ? 0.4194 0.2871 0.2011 0.1203 -0.0495 -0.0034 589 ASN A N 4402 C CA . ASN A 596 ? 0.4316 0.3017 0.2007 0.1313 -0.0459 -0.0043 589 ASN A CA 4403 C C . ASN A 596 ? 0.4292 0.3076 0.2059 0.1308 -0.0477 -0.0130 589 ASN A C 4404 O O . ASN A 596 ? 0.4361 0.3326 0.2009 0.1198 -0.0503 -0.0080 589 ASN A O 4405 C CB . ASN A 596 ? 0.4418 0.2939 0.2001 0.1350 -0.0371 -0.0027 589 ASN A CB 4406 C CG A ASN A 596 ? 0.4629 0.3186 0.2202 0.1353 -0.0430 0.0144 589 ASN A CG 4407 C CG B ASN A 596 ? 0.4279 0.2964 0.1794 0.1318 -0.0307 -0.0114 589 ASN A CG 4408 O OD1 A ASN A 596 ? 0.4625 0.2894 0.2737 0.1282 -0.0310 0.0300 589 ASN A OD1 4409 O OD1 B ASN A 596 ? 0.4218 0.3273 0.1839 0.1131 -0.0133 -0.0271 589 ASN A OD1 4410 N ND2 A ASN A 596 ? 0.5067 0.3344 0.2110 0.1350 -0.0454 0.0291 589 ASN A ND2 4411 N ND2 B ASN A 596 ? 0.4256 0.2675 0.1271 0.1274 -0.0311 -0.0129 589 ASN A ND2 4412 N N . SER A 597 ? 0.4249 0.2980 0.2029 0.1264 -0.0491 -0.0171 590 SER A N 4413 C CA . SER A 597 ? 0.4297 0.3048 0.2094 0.1268 -0.0448 -0.0297 590 SER A CA 4414 C C . SER A 597 ? 0.4265 0.2872 0.1951 0.1243 -0.0485 -0.0324 590 SER A C 4415 O O . SER A 597 ? 0.4094 0.2724 0.2315 0.1433 -0.0362 -0.0432 590 SER A O 4416 C CB . SER A 597 ? 0.4547 0.3172 0.2086 0.0974 -0.0491 -0.0313 590 SER A CB 4417 O OG . SER A 597 ? 0.4396 0.3041 0.2557 0.1418 -0.0221 -0.0474 590 SER A OG 4418 N N . ILE A 598 ? 0.4224 0.2877 0.1862 0.1312 -0.0401 -0.0262 591 ILE A N 4419 C CA . ILE A 598 ? 0.4341 0.2820 0.1735 0.1362 -0.0578 -0.0249 591 ILE A CA 4420 C C . ILE A 598 ? 0.4269 0.2822 0.1684 0.1341 -0.0635 -0.0397 591 ILE A C 4421 O O . ILE A 598 ? 0.4223 0.2745 0.1590 0.1326 -0.0646 -0.0582 591 ILE A O 4422 C CB . ILE A 598 ? 0.4267 0.2826 0.1506 0.1388 -0.0575 -0.0172 591 ILE A CB 4423 C CG1 . ILE A 598 ? 0.4899 0.3307 0.2482 0.1192 -0.0579 0.0142 591 ILE A CG1 4424 C CG2 . ILE A 598 ? 0.4406 0.2652 0.1344 0.1395 -0.0557 0.0025 591 ILE A CG2 4425 C CD1 . ILE A 598 ? 0.5557 0.3856 0.2120 0.0669 -0.0831 0.0262 591 ILE A CD1 4426 N N . VAL A 599 ? 0.4234 0.2848 0.1704 0.1238 -0.0637 -0.0404 592 VAL A N 4427 C CA . VAL A 599 ? 0.4214 0.2785 0.1522 0.1162 -0.0632 -0.0401 592 VAL A CA 4428 C C . VAL A 599 ? 0.3983 0.2844 0.1706 0.1160 -0.0641 -0.0367 592 VAL A C 4429 O O . VAL A 599 ? 0.3988 0.2707 0.1653 0.1189 -0.0718 -0.0222 592 VAL A O 4430 C CB . VAL A 599 ? 0.4357 0.2744 0.1445 0.1088 -0.0574 -0.0406 592 VAL A CB 4431 C CG1 . VAL A 599 ? 0.4342 0.2598 0.1436 0.1204 -0.0758 -0.0380 592 VAL A CG1 4432 C CG2 . VAL A 599 ? 0.4620 0.2900 0.1503 0.1092 -0.0335 -0.0412 592 VAL A CG2 4433 N N . LEU A 600 ? 0.3853 0.2776 0.1673 0.1095 -0.0598 -0.0389 593 LEU A N 4434 C CA . LEU A 600 ? 0.3642 0.2802 0.1933 0.1109 -0.0522 -0.0526 593 LEU A CA 4435 C C . LEU A 600 ? 0.3526 0.2734 0.1975 0.1060 -0.0442 -0.0498 593 LEU A C 4436 O O . LEU A 600 ? 0.3540 0.2791 0.2009 0.0989 -0.0361 -0.0748 593 LEU A O 4437 C CB . LEU A 600 ? 0.3657 0.2835 0.1622 0.1094 -0.0560 -0.0479 593 LEU A CB 4438 C CG . LEU A 600 ? 0.3718 0.3035 0.2069 0.1094 -0.0533 -0.0438 593 LEU A CG 4439 C CD1 . LEU A 600 ? 0.3358 0.3285 0.2049 0.1211 -0.0688 -0.0325 593 LEU A CD1 4440 C CD2 . LEU A 600 ? 0.3881 0.3189 0.1752 0.1006 -0.0355 -0.0257 593 LEU A CD2 4441 N N . PRO A 601 ? 0.3296 0.2713 0.1989 0.1020 -0.0438 -0.0518 594 PRO A N 4442 C CA . PRO A 601 ? 0.3280 0.2731 0.2010 0.0966 -0.0658 -0.0480 594 PRO A CA 4443 C C . PRO A 601 ? 0.3286 0.2744 0.2098 0.0859 -0.0680 -0.0459 594 PRO A C 4444 O O . PRO A 601 ? 0.3130 0.2815 0.2082 0.1013 -0.0650 -0.0454 594 PRO A O 4445 C CB . PRO A 601 ? 0.3185 0.2795 0.1998 0.0986 -0.0822 -0.0493 594 PRO A CB 4446 C CG . PRO A 601 ? 0.3116 0.2929 0.2357 0.0914 -0.0564 -0.0466 594 PRO A CG 4447 C CD . PRO A 601 ? 0.3199 0.2528 0.1952 0.1122 -0.0445 -0.0566 594 PRO A CD 4448 N N . PHE A 602 ? 0.3217 0.2577 0.2042 0.0837 -0.0761 -0.0352 595 PHE A N 4449 C CA . PHE A 602 ? 0.3270 0.2616 0.2267 0.0652 -0.0668 -0.0394 595 PHE A CA 4450 C C . PHE A 602 ? 0.3263 0.2740 0.2434 0.0592 -0.0675 -0.0498 595 PHE A C 4451 O O . PHE A 602 ? 0.3432 0.2914 0.2242 0.0595 -0.0415 -0.0568 595 PHE A O 4452 C CB . PHE A 602 ? 0.2963 0.2484 0.1946 0.0578 -0.0769 -0.0264 595 PHE A CB 4453 C CG . PHE A 602 ? 0.3142 0.2658 0.1826 0.0552 -0.0601 -0.0175 595 PHE A CG 4454 C CD1 . PHE A 602 ? 0.3140 0.2397 0.1637 0.0215 -0.0699 0.0037 595 PHE A CD1 4455 C CD2 . PHE A 602 ? 0.3160 0.2448 0.2014 0.0334 -0.0703 -0.0279 595 PHE A CD2 4456 C CE1 . PHE A 602 ? 0.3186 0.2622 0.1499 0.0030 -0.0787 0.0508 595 PHE A CE1 4457 C CE2 . PHE A 602 ? 0.3309 0.2399 0.1722 0.0414 -0.0717 0.0007 595 PHE A CE2 4458 C CZ . PHE A 602 ? 0.2827 0.1926 0.1528 0.0285 -0.0474 0.0097 595 PHE A CZ 4459 N N . ASP A 603 ? 0.3064 0.2673 0.2463 0.0606 -0.0626 -0.0513 596 ASP A N 4460 C CA . ASP A 603 ? 0.3035 0.2594 0.2478 0.0566 -0.0867 -0.0496 596 ASP A CA 4461 C C . ASP A 603 ? 0.2923 0.2513 0.2622 0.0545 -0.0857 -0.0483 596 ASP A C 4462 O O . ASP A 603 ? 0.3039 0.2502 0.2332 0.0440 -0.0951 -0.0440 596 ASP A O 4463 C CB . ASP A 603 ? 0.2995 0.2541 0.2459 0.0556 -0.0844 -0.0497 596 ASP A CB 4464 C CG . ASP A 603 ? 0.3401 0.2799 0.2805 0.0625 -0.1018 -0.0669 596 ASP A CG 4465 O OD1 . ASP A 603 ? 0.3347 0.2765 0.3068 0.0652 -0.0953 -0.0622 596 ASP A OD1 4466 O OD2 . ASP A 603 ? 0.3783 0.3162 0.3950 0.0826 -0.1122 -0.0544 596 ASP A OD2 4467 N N . CYS A 604 ? 0.2802 0.2382 0.2669 0.0587 -0.0994 -0.0469 597 CYS A N 4468 C CA . CYS A 604 ? 0.2892 0.2704 0.2850 0.0611 -0.0914 -0.0560 597 CYS A CA 4469 C C . CYS A 604 ? 0.2848 0.2664 0.2905 0.0627 -0.0881 -0.0598 597 CYS A C 4470 O O . CYS A 604 ? 0.2799 0.2792 0.2907 0.0517 -0.0715 -0.0596 597 CYS A O 4471 C CB . CYS A 604 ? 0.2876 0.2661 0.2716 0.0834 -0.0944 -0.0571 597 CYS A CB 4472 S SG . CYS A 604 ? 0.3475 0.3429 0.3083 0.0838 -0.0913 -0.0751 597 CYS A SG 4473 N N . ARG A 605 ? 0.2742 0.2557 0.2952 0.0505 -0.0956 -0.0756 598 ARG A N 4474 C CA . ARG A 605 ? 0.2995 0.2717 0.3104 0.0471 -0.0986 -0.0755 598 ARG A CA 4475 C C . ARG A 605 ? 0.2958 0.2639 0.3206 0.0478 -0.0974 -0.0692 598 ARG A C 4476 O O . ARG A 605 ? 0.2794 0.2594 0.3253 0.0421 -0.1011 -0.0621 598 ARG A O 4477 C CB . ARG A 605 ? 0.3036 0.2676 0.3062 0.0400 -0.1025 -0.0728 598 ARG A CB 4478 C CG . ARG A 605 ? 0.3333 0.3204 0.3050 0.0572 -0.1055 -0.0860 598 ARG A CG 4479 C CD . ARG A 605 ? 0.3490 0.3387 0.3263 0.0974 -0.1255 -0.0768 598 ARG A CD 4480 N NE . ARG A 605 ? 0.3819 0.3655 0.2864 0.0847 -0.1192 -0.0496 598 ARG A NE 4481 C CZ . ARG A 605 ? 0.4549 0.3835 0.3106 0.0296 -0.1537 -0.0777 598 ARG A CZ 4482 N NH1 . ARG A 605 ? 0.4477 0.4067 0.2281 0.0041 -0.1705 -0.0989 598 ARG A NH1 4483 N NH2 . ARG A 605 ? 0.4577 0.3774 0.2848 0.0358 -0.1375 -0.0457 598 ARG A NH2 4484 N N . ASP A 606 ? 0.2904 0.2394 0.3159 0.0500 -0.1012 -0.0664 599 ASP A N 4485 C CA . ASP A 606 ? 0.2829 0.2497 0.3249 0.0475 -0.0878 -0.0495 599 ASP A CA 4486 C C . ASP A 606 ? 0.2649 0.2333 0.3140 0.0467 -0.0855 -0.0487 599 ASP A C 4487 O O . ASP A 606 ? 0.2699 0.2334 0.3123 0.0496 -0.0720 -0.0391 599 ASP A O 4488 C CB . ASP A 606 ? 0.2605 0.2338 0.3334 0.0639 -0.0942 -0.0350 599 ASP A CB 4489 C CG . ASP A 606 ? 0.2960 0.2876 0.3602 0.0321 -0.1190 -0.0378 599 ASP A CG 4490 O OD1 . ASP A 606 ? 0.3426 0.3355 0.4647 0.0294 -0.1533 0.0390 599 ASP A OD1 4491 O OD2 . ASP A 606 ? 0.2869 0.3225 0.3273 0.0478 -0.1405 -0.0438 599 ASP A OD2 4492 N N . TYR A 607 ? 0.2413 0.2292 0.3041 0.0284 -0.0783 -0.0533 600 TYR A N 4493 C CA . TYR A 607 ? 0.2277 0.2129 0.2919 0.0267 -0.0746 -0.0472 600 TYR A CA 4494 C C . TYR A 607 ? 0.2195 0.2312 0.3015 0.0189 -0.0725 -0.0560 600 TYR A C 4495 O O . TYR A 607 ? 0.1872 0.2273 0.2969 0.0229 -0.0732 -0.0438 600 TYR A O 4496 C CB . TYR A 607 ? 0.2213 0.2145 0.2742 0.0146 -0.0834 -0.0514 600 TYR A CB 4497 C CG . TYR A 607 ? 0.2435 0.1900 0.2703 0.0303 -0.0621 -0.0521 600 TYR A CG 4498 C CD1 . TYR A 607 ? 0.2525 0.2054 0.2514 0.0147 -0.0529 -0.0644 600 TYR A CD1 4499 C CD2 . TYR A 607 ? 0.2314 0.1917 0.2442 0.0178 -0.0447 -0.0751 600 TYR A CD2 4500 C CE1 . TYR A 607 ? 0.2359 0.1955 0.2583 0.0099 -0.0706 -0.0448 600 TYR A CE1 4501 C CE2 . TYR A 607 ? 0.2144 0.2377 0.2327 0.0136 -0.0555 -0.0598 600 TYR A CE2 4502 C CZ . TYR A 607 ? 0.2197 0.2151 0.2240 0.0182 -0.0631 -0.0570 600 TYR A CZ 4503 O OH . TYR A 607 ? 0.2246 0.2700 0.1616 0.0091 -0.0626 -0.0645 600 TYR A OH 4504 N N . ALA A 608 ? 0.2067 0.2182 0.2956 0.0230 -0.0697 -0.0700 601 ALA A N 4505 C CA . ALA A 608 ? 0.2310 0.2242 0.3028 0.0272 -0.0633 -0.0609 601 ALA A CA 4506 C C . ALA A 608 ? 0.2303 0.2387 0.3186 0.0328 -0.0752 -0.0585 601 ALA A C 4507 O O . ALA A 608 ? 0.2168 0.2455 0.3293 0.0337 -0.0680 -0.0475 601 ALA A O 4508 C CB . ALA A 608 ? 0.2282 0.2030 0.2959 0.0210 -0.0717 -0.0607 601 ALA A CB 4509 N N . VAL A 609 ? 0.2493 0.2392 0.3090 0.0402 -0.0921 -0.0588 602 VAL A N 4510 C CA . VAL A 609 ? 0.2432 0.2758 0.3179 0.0334 -0.0797 -0.0584 602 VAL A CA 4511 C C . VAL A 609 ? 0.2430 0.2699 0.3314 0.0259 -0.0848 -0.0531 602 VAL A C 4512 O O . VAL A 609 ? 0.2237 0.2937 0.3213 0.0172 -0.0751 -0.0631 602 VAL A O 4513 C CB . VAL A 609 ? 0.2610 0.3020 0.3213 0.0426 -0.0836 -0.0626 602 VAL A CB 4514 C CG1 . VAL A 609 ? 0.2584 0.3425 0.3575 0.0737 -0.0798 -0.0364 602 VAL A CG1 4515 C CG2 . VAL A 609 ? 0.3379 0.3148 0.3075 0.0325 -0.0879 -0.0745 602 VAL A CG2 4516 N N . VAL A 610 ? 0.2221 0.2387 0.3295 0.0205 -0.0789 -0.0414 603 VAL A N 4517 C CA . VAL A 610 ? 0.2273 0.2261 0.3213 0.0269 -0.0710 -0.0321 603 VAL A CA 4518 C C . VAL A 610 ? 0.2229 0.2172 0.3250 0.0195 -0.0555 -0.0364 603 VAL A C 4519 O O . VAL A 610 ? 0.2398 0.1954 0.3290 0.0224 -0.0422 -0.0349 603 VAL A O 4520 C CB . VAL A 610 ? 0.2224 0.2263 0.3259 0.0291 -0.0668 -0.0243 603 VAL A CB 4521 C CG1 . VAL A 610 ? 0.2424 0.2436 0.3251 0.0379 -0.0827 0.0054 603 VAL A CG1 4522 C CG2 . VAL A 610 ? 0.2397 0.2573 0.3243 0.0389 -0.1025 -0.0114 603 VAL A CG2 4523 N N . LEU A 611 ? 0.1987 0.2003 0.3165 0.0176 -0.0508 -0.0382 604 LEU A N 4524 C CA . LEU A 611 ? 0.1896 0.2184 0.3225 0.0082 -0.0409 -0.0342 604 LEU A CA 4525 C C . LEU A 611 ? 0.1853 0.2171 0.3309 0.0058 -0.0401 -0.0424 604 LEU A C 4526 O O . LEU A 611 ? 0.1772 0.2266 0.3290 0.0010 -0.0326 -0.0393 604 LEU A O 4527 C CB . LEU A 611 ? 0.1651 0.2119 0.3021 0.0075 -0.0392 -0.0359 604 LEU A CB 4528 C CG . LEU A 611 ? 0.1768 0.2320 0.2854 -0.0053 -0.0387 -0.0478 604 LEU A CG 4529 C CD1 . LEU A 611 ? 0.2188 0.2564 0.2784 -0.0006 -0.0054 -0.0114 604 LEU A CD1 4530 C CD2 . LEU A 611 ? 0.1719 0.2066 0.3081 -0.0306 -0.0514 -0.0593 604 LEU A CD2 4531 N N . ARG A 612 ? 0.1951 0.2280 0.3428 0.0020 -0.0497 -0.0436 605 ARG A N 4532 C CA . ARG A 612 ? 0.2117 0.2316 0.3608 -0.0082 -0.0468 -0.0429 605 ARG A CA 4533 C C . ARG A 612 ? 0.2011 0.2409 0.3650 -0.0030 -0.0560 -0.0389 605 ARG A C 4534 O O . ARG A 612 ? 0.1835 0.2411 0.3837 0.0043 -0.0421 -0.0239 605 ARG A O 4535 C CB . ARG A 612 ? 0.2081 0.2397 0.3602 -0.0111 -0.0505 -0.0441 605 ARG A CB 4536 C CG . ARG A 612 ? 0.2798 0.2216 0.4031 -0.0283 -0.0402 -0.0482 605 ARG A CG 4537 C CD . ARG A 612 ? 0.3371 0.2553 0.4817 -0.0322 -0.0346 -0.0510 605 ARG A CD 4538 N NE . ARG A 612 ? 0.3789 0.2795 0.5525 -0.0744 -0.0201 -0.1081 605 ARG A NE 4539 C CZ . ARG A 612 ? 0.4329 0.3157 0.6383 -0.0992 0.0162 -0.0967 605 ARG A CZ 4540 N NH1 . ARG A 612 ? 0.4919 0.3119 0.6466 -0.0627 0.0193 -0.1299 605 ARG A NH1 4541 N NH2 . ARG A 612 ? 0.4395 0.3142 0.6843 -0.1308 0.0232 -0.0496 605 ARG A NH2 4542 N N . LYS A 613 ? 0.2103 0.2340 0.3595 0.0043 -0.0611 -0.0387 606 LYS A N 4543 C CA . LYS A 613 ? 0.2286 0.2534 0.3761 0.0059 -0.0541 -0.0276 606 LYS A CA 4544 C C . LYS A 613 ? 0.2062 0.2462 0.3635 0.0028 -0.0490 -0.0230 606 LYS A C 4545 O O . LYS A 613 ? 0.1905 0.2480 0.3632 0.0053 -0.0492 -0.0179 606 LYS A O 4546 C CB . LYS A 613 ? 0.2329 0.2516 0.3923 0.0152 -0.0502 -0.0143 606 LYS A CB 4547 C CG . LYS A 613 ? 0.3466 0.2937 0.4543 0.0260 -0.0606 -0.0214 606 LYS A CG 4548 C CD . LYS A 613 ? 0.4362 0.3227 0.5798 -0.0113 -0.0538 0.0035 606 LYS A CD 4549 C CE . LYS A 613 ? 0.3405 0.3938 0.6249 -0.0057 -0.0796 -0.0238 606 LYS A CE 4550 N NZ . LYS A 613 ? 0.3412 0.3873 0.6905 0.0308 -0.0632 -0.0437 606 LYS A NZ 4551 N N . TYR A 614 ? 0.1917 0.2271 0.3452 -0.0061 -0.0498 -0.0178 607 TYR A N 4552 C CA . TYR A 614 ? 0.1920 0.2038 0.3345 -0.0093 -0.0294 -0.0288 607 TYR A CA 4553 C C . TYR A 614 ? 0.1788 0.2103 0.3238 -0.0076 -0.0271 -0.0259 607 TYR A C 4554 O O . TYR A 614 ? 0.1993 0.2102 0.3344 0.0033 -0.0176 -0.0168 607 TYR A O 4555 C CB . TYR A 614 ? 0.1475 0.1868 0.3223 -0.0002 -0.0216 -0.0385 607 TYR A CB 4556 C CG . TYR A 614 ? 0.1996 0.2069 0.3186 0.0013 -0.0211 -0.0191 607 TYR A CG 4557 C CD1 . TYR A 614 ? 0.2063 0.2365 0.3291 0.0179 -0.0151 0.0028 607 TYR A CD1 4558 C CD2 . TYR A 614 ? 0.2054 0.2088 0.3186 0.0034 -0.0282 -0.0127 607 TYR A CD2 4559 C CE1 . TYR A 614 ? 0.2629 0.2593 0.3363 0.0027 -0.0315 0.0122 607 TYR A CE1 4560 C CE2 . TYR A 614 ? 0.2448 0.2369 0.2815 0.0418 -0.0528 0.0006 607 TYR A CE2 4561 C CZ . TYR A 614 ? 0.2300 0.2589 0.3192 0.0189 -0.0529 0.0068 607 TYR A CZ 4562 O OH . TYR A 614 ? 0.2340 0.2639 0.3512 0.0355 -0.1019 0.0020 607 TYR A OH 4563 N N . ALA A 615 ? 0.1721 0.1875 0.3234 -0.0176 -0.0238 -0.0350 608 ALA A N 4564 C CA . ALA A 615 ? 0.1703 0.2110 0.3360 -0.0090 -0.0317 -0.0261 608 ALA A CA 4565 C C . ALA A 615 ? 0.1829 0.2329 0.3661 -0.0148 -0.0325 -0.0268 608 ALA A C 4566 O O . ALA A 615 ? 0.1507 0.2382 0.3522 -0.0208 -0.0431 -0.0168 608 ALA A O 4567 C CB . ALA A 615 ? 0.1837 0.2058 0.3249 0.0020 -0.0333 -0.0261 608 ALA A CB 4568 N N . ASP A 616 ? 0.1832 0.2524 0.3787 -0.0101 -0.0392 -0.0316 609 ASP A N 4569 C CA . ASP A 616 ? 0.2023 0.2764 0.4032 -0.0109 -0.0299 -0.0328 609 ASP A CA 4570 C C . ASP A 616 ? 0.1909 0.2638 0.3997 -0.0084 -0.0202 -0.0241 609 ASP A C 4571 O O . ASP A 616 ? 0.1703 0.2686 0.4026 -0.0090 -0.0101 -0.0212 609 ASP A O 4572 C CB . ASP A 616 ? 0.2123 0.2867 0.4074 -0.0059 -0.0368 -0.0431 609 ASP A CB 4573 C CG . ASP A 616 ? 0.2630 0.3159 0.4619 -0.0020 -0.0516 -0.0539 609 ASP A CG 4574 O OD1 . ASP A 616 ? 0.3073 0.2731 0.5002 0.0272 -0.0658 -0.1209 609 ASP A OD1 4575 O OD2 . ASP A 616 ? 0.3535 0.4857 0.4604 -0.0246 -0.0515 -0.0761 609 ASP A OD2 4576 N N . LYS A 617 ? 0.1922 0.2425 0.3939 -0.0103 -0.0188 -0.0189 610 LYS A N 4577 C CA . LYS A 617 ? 0.2050 0.2493 0.3836 -0.0155 -0.0025 -0.0129 610 LYS A CA 4578 C C . LYS A 617 ? 0.2065 0.2390 0.3886 -0.0152 0.0021 -0.0054 610 LYS A C 4579 O O . LYS A 617 ? 0.2013 0.2086 0.3786 -0.0169 -0.0049 -0.0029 610 LYS A O 4580 C CB . LYS A 617 ? 0.2201 0.2333 0.3918 -0.0117 -0.0064 -0.0062 610 LYS A CB 4581 C CG . LYS A 617 ? 0.2947 0.3001 0.4200 -0.0045 0.0229 -0.0152 610 LYS A CG 4582 C CD . LYS A 617 ? 0.3670 0.3697 0.5051 -0.0159 0.0392 -0.0251 610 LYS A CD 4583 C CE . LYS A 617 ? 0.4848 0.4273 0.5671 -0.0142 0.0481 -0.0362 610 LYS A CE 4584 N NZ . LYS A 617 ? 0.5079 0.4733 0.5929 -0.0379 0.0232 -0.0533 610 LYS A NZ 4585 N N . ILE A 618 ? 0.1897 0.2223 0.3723 -0.0195 0.0084 -0.0071 611 ILE A N 4586 C CA . ILE A 618 ? 0.1936 0.2272 0.3756 -0.0243 0.0033 -0.0134 611 ILE A CA 4587 C C . ILE A 618 ? 0.2036 0.2340 0.3819 -0.0266 0.0087 -0.0146 611 ILE A C 4588 O O . ILE A 618 ? 0.2108 0.2064 0.3741 -0.0202 -0.0006 -0.0244 611 ILE A O 4589 C CB . ILE A 618 ? 0.1963 0.2454 0.3536 -0.0220 0.0107 -0.0243 611 ILE A CB 4590 C CG1 . ILE A 618 ? 0.2030 0.2595 0.3649 -0.0275 -0.0001 -0.0443 611 ILE A CG1 4591 C CG2 . ILE A 618 ? 0.1780 0.2269 0.3671 -0.0241 0.0071 -0.0255 611 ILE A CG2 4592 C CD1 . ILE A 618 ? 0.2112 0.2750 0.3397 -0.0264 0.0054 -0.0702 611 ILE A CD1 4593 N N . TYR A 619 ? 0.2115 0.2362 0.3899 -0.0390 -0.0023 -0.0181 612 TYR A N 4594 C CA . TYR A 619 ? 0.2242 0.2546 0.4185 -0.0357 0.0049 -0.0099 612 TYR A CA 4595 C C . TYR A 619 ? 0.2240 0.2600 0.4149 -0.0338 0.0035 -0.0123 612 TYR A C 4596 O O . TYR A 619 ? 0.1879 0.2551 0.4144 -0.0246 -0.0170 0.0013 612 TYR A O 4597 C CB . TYR A 619 ? 0.2267 0.2556 0.4225 -0.0399 0.0055 -0.0149 612 TYR A CB 4598 C CG . TYR A 619 ? 0.2962 0.3025 0.4764 -0.0541 0.0094 -0.0100 612 TYR A CG 4599 C CD1 . TYR A 619 ? 0.3428 0.3363 0.5106 -0.0433 0.0021 -0.0107 612 TYR A CD1 4600 C CD2 . TYR A 619 ? 0.3526 0.3634 0.5434 -0.0603 0.0225 0.0027 612 TYR A CD2 4601 C CE1 . TYR A 619 ? 0.4033 0.3921 0.5725 -0.0679 0.0078 0.0025 612 TYR A CE1 4602 C CE2 . TYR A 619 ? 0.3988 0.4175 0.6218 -0.0805 0.0157 -0.0074 612 TYR A CE2 4603 C CZ . TYR A 619 ? 0.4371 0.4343 0.6356 -0.0844 -0.0053 0.0104 612 TYR A CZ 4604 O OH . TYR A 619 ? 0.5029 0.5692 0.7011 -0.1193 0.0056 0.0169 612 TYR A OH 4605 N N . SER A 620 ? 0.2244 0.2561 0.4146 -0.0293 0.0043 -0.0105 613 SER A N 4606 C CA . SER A 620 ? 0.2347 0.2743 0.4309 -0.0312 0.0098 -0.0071 613 SER A CA 4607 C C . SER A 620 ? 0.2324 0.2698 0.4269 -0.0306 0.0240 -0.0012 613 SER A C 4608 O O . SER A 620 ? 0.2112 0.2780 0.4197 -0.0492 0.0312 0.0012 613 SER A O 4609 C CB . SER A 620 ? 0.2455 0.2746 0.4348 -0.0345 0.0058 -0.0060 613 SER A CB 4610 O OG A SER A 620 ? 0.2116 0.2960 0.4635 -0.0536 -0.0166 -0.0124 613 SER A OG 4611 O OG B SER A 620 ? 0.2727 0.2816 0.4535 -0.0335 -0.0057 -0.0119 613 SER A OG 4612 N N . ILE A 621 ? 0.2268 0.2448 0.4189 -0.0255 0.0293 0.0046 614 ILE A N 4613 C CA . ILE A 621 ? 0.2338 0.2439 0.4091 -0.0336 0.0384 0.0133 614 ILE A CA 4614 C C . ILE A 621 ? 0.2464 0.2549 0.3998 -0.0299 0.0523 0.0094 614 ILE A C 4615 O O . ILE A 621 ? 0.2635 0.2667 0.3973 -0.0136 0.0674 0.0109 614 ILE A O 4616 C CB . ILE A 621 ? 0.2392 0.2457 0.4104 -0.0397 0.0349 0.0166 614 ILE A CB 4617 C CG1 . ILE A 621 ? 0.2143 0.2312 0.4086 -0.0695 0.0448 0.0333 614 ILE A CG1 4618 C CG2 . ILE A 621 ? 0.2385 0.2609 0.4252 -0.0406 0.0314 0.0022 614 ILE A CG2 4619 C CD1 . ILE A 621 ? 0.2469 0.1770 0.3829 -0.0784 0.0663 0.0161 614 ILE A CD1 4620 N N . SER A 622 ? 0.2309 0.2334 0.3875 -0.0278 0.0501 0.0032 615 SER A N 4621 C CA . SER A 622 ? 0.2392 0.2443 0.3976 -0.0283 0.0539 0.0024 615 SER A CA 4622 C C . SER A 622 ? 0.2581 0.2532 0.4234 -0.0203 0.0629 0.0051 615 SER A C 4623 O O . SER A 622 ? 0.2596 0.2530 0.4018 -0.0225 0.0641 0.0031 615 SER A O 4624 C CB . SER A 622 ? 0.2462 0.2289 0.3914 -0.0166 0.0513 -0.0020 615 SER A CB 4625 O OG . SER A 622 ? 0.2794 0.2922 0.3393 0.0148 0.0614 0.0119 615 SER A OG 4626 N N . MET A 623 ? 0.2611 0.2749 0.4445 -0.0243 0.0605 0.0098 616 MET A N 4627 C CA . MET A 623 ? 0.2760 0.2966 0.4769 -0.0335 0.0715 0.0226 616 MET A CA 4628 C C . MET A 623 ? 0.2788 0.3246 0.4862 -0.0392 0.0698 0.0295 616 MET A C 4629 O O . MET A 623 ? 0.2599 0.3275 0.4844 -0.0554 0.0611 0.0295 616 MET A O 4630 C CB . MET A 623 ? 0.2716 0.2946 0.4782 -0.0382 0.0760 0.0257 616 MET A CB 4631 C CG . MET A 623 ? 0.3270 0.3029 0.5398 -0.0249 0.0644 0.0378 616 MET A CG 4632 S SD . MET A 623 ? 0.4332 0.3539 0.6524 0.0112 0.0429 0.0705 616 MET A SD 4633 C CE . MET A 623 ? 0.3985 0.2616 0.6634 -0.0208 0.0345 0.0956 616 MET A CE 4634 N N . LYS A 624 ? 0.3075 0.3211 0.5051 -0.0245 0.0820 0.0292 617 LYS A N 4635 C CA . LYS A 624 ? 0.3443 0.3500 0.5211 -0.0278 0.0882 0.0335 617 LYS A CA 4636 C C . LYS A 624 ? 0.3296 0.3328 0.5092 -0.0307 0.0981 0.0308 617 LYS A C 4637 O O . LYS A 624 ? 0.3050 0.3293 0.5013 -0.0154 0.1020 0.0237 617 LYS A O 4638 C CB . LYS A 624 ? 0.3814 0.3547 0.5421 -0.0235 0.0907 0.0306 617 LYS A CB 4639 C CG . LYS A 624 ? 0.4295 0.4535 0.5893 -0.0042 0.0806 0.0403 617 LYS A CG 4640 C CD . LYS A 624 ? 0.5183 0.5228 0.6952 -0.0258 0.0902 0.0270 617 LYS A CD 4641 C CE . LYS A 624 ? 0.5008 0.6469 0.7386 -0.0372 0.0892 0.0229 617 LYS A CE 4642 N NZ . LYS A 624 ? 0.5305 0.7156 0.7173 -0.0489 0.0663 0.0373 617 LYS A NZ 4643 N N . HIS A 625 ? 0.2971 0.3159 0.4876 -0.0370 0.0978 0.0282 618 HIS A N 4644 C CA . HIS A 625 ? 0.2901 0.2927 0.4602 -0.0501 0.1066 0.0375 618 HIS A CA 4645 C C . HIS A 625 ? 0.2877 0.2971 0.4535 -0.0546 0.1068 0.0466 618 HIS A C 4646 O O . HIS A 625 ? 0.2500 0.2793 0.4165 -0.0576 0.1173 0.0337 618 HIS A O 4647 C CB . HIS A 625 ? 0.2734 0.2987 0.4506 -0.0455 0.1045 0.0398 618 HIS A CB 4648 C CG . HIS A 625 ? 0.2866 0.3123 0.4630 -0.0407 0.1073 0.0428 618 HIS A CG 4649 N ND1 . HIS A 625 ? 0.3187 0.3543 0.3809 -0.0496 0.0981 0.0602 618 HIS A ND1 4650 C CD2 . HIS A 625 ? 0.2939 0.3460 0.4474 0.0008 0.0938 0.0389 618 HIS A CD2 4651 C CE1 . HIS A 625 ? 0.3274 0.3526 0.4447 -0.0349 0.0823 0.0259 618 HIS A CE1 4652 N NE2 . HIS A 625 ? 0.3027 0.3488 0.4552 -0.0364 0.0576 0.0486 618 HIS A NE2 4653 N N . PRO A 626 ? 0.2838 0.2942 0.4613 -0.0656 0.1113 0.0528 619 PRO A N 4654 C CA . PRO A 626 ? 0.2878 0.2973 0.4744 -0.0583 0.1114 0.0559 619 PRO A CA 4655 C C . PRO A 626 ? 0.3013 0.3063 0.4803 -0.0595 0.1102 0.0596 619 PRO A C 4656 O O . PRO A 626 ? 0.3022 0.3076 0.4744 -0.0579 0.1016 0.0596 619 PRO A O 4657 C CB . PRO A 626 ? 0.2893 0.3111 0.4794 -0.0592 0.1065 0.0440 619 PRO A CB 4658 C CG . PRO A 626 ? 0.2674 0.3076 0.4930 -0.0563 0.0974 0.0295 619 PRO A CG 4659 C CD . PRO A 626 ? 0.2892 0.2817 0.4726 -0.0495 0.1108 0.0565 619 PRO A CD 4660 N N . GLN A 627 ? 0.3134 0.2985 0.4661 -0.0594 0.1182 0.0753 620 GLN A N 4661 C CA . GLN A 627 ? 0.3325 0.3019 0.4570 -0.0469 0.1211 0.0813 620 GLN A CA 4662 C C . GLN A 627 ? 0.3334 0.2858 0.4289 -0.0465 0.1172 0.0796 620 GLN A C 4663 O O . GLN A 627 ? 0.3173 0.2607 0.4058 -0.0478 0.1214 0.0869 620 GLN A O 4664 C CB . GLN A 627 ? 0.3640 0.3098 0.4698 -0.0351 0.1254 0.0906 620 GLN A CB 4665 C CG . GLN A 627 ? 0.4011 0.3633 0.4959 -0.0174 0.1245 0.0977 620 GLN A CG 4666 C CD . GLN A 627 ? 0.4209 0.3757 0.5524 -0.0141 0.1363 0.1154 620 GLN A CD 4667 O OE1 . GLN A 627 ? 0.4225 0.3865 0.5269 0.0273 0.1374 0.1113 620 GLN A OE1 4668 N NE2 . GLN A 627 ? 0.4136 0.4024 0.5425 -0.0225 0.1815 0.1581 620 GLN A NE2 4669 N N . GLU A 628 ? 0.3204 0.2588 0.3954 -0.0492 0.1109 0.0769 621 GLU A N 4670 C CA . GLU A 628 ? 0.3277 0.2611 0.4042 -0.0399 0.0921 0.0674 621 GLU A CA 4671 C C . GLU A 628 ? 0.3140 0.2495 0.4019 -0.0350 0.0824 0.0575 621 GLU A C 4672 O O . GLU A 628 ? 0.2991 0.2287 0.3797 -0.0286 0.0613 0.0647 621 GLU A O 4673 C CB . GLU A 628 ? 0.3442 0.2640 0.4088 -0.0312 0.0849 0.0564 621 GLU A CB 4674 C CG . GLU A 628 ? 0.4112 0.3205 0.4409 -0.0387 0.1034 0.0519 621 GLU A CG 4675 C CD . GLU A 628 ? 0.4654 0.3784 0.4687 -0.0520 0.1269 0.0614 621 GLU A CD 4676 O OE1 . GLU A 628 ? 0.5492 0.3279 0.4279 0.0074 0.1120 0.0615 621 GLU A OE1 4677 O OE2 . GLU A 628 ? 0.5756 0.5138 0.4977 -0.0578 0.1307 0.0473 621 GLU A OE2 4678 N N . MET A 629 ? 0.2901 0.2452 0.3945 -0.0338 0.0766 0.0526 622 MET A N 4679 C CA . MET A 629 ? 0.2817 0.2378 0.3972 -0.0385 0.0782 0.0634 622 MET A CA 4680 C C . MET A 629 ? 0.2843 0.2451 0.4073 -0.0461 0.0773 0.0601 622 MET A C 4681 O O . MET A 629 ? 0.2568 0.2267 0.4112 -0.0508 0.0696 0.0589 622 MET A O 4682 C CB . MET A 629 ? 0.2785 0.2359 0.3844 -0.0385 0.0764 0.0643 622 MET A CB 4683 C CG . MET A 629 ? 0.2704 0.2135 0.3468 -0.0108 0.0573 0.0691 622 MET A CG 4684 S SD . MET A 629 ? 0.2483 0.2880 0.3904 0.0080 0.0367 0.0301 622 MET A SD 4685 C CE . MET A 629 ? 0.1963 0.2538 0.2802 0.0158 -0.0019 0.0451 622 MET A CE 4686 N N . LYS A 630 ? 0.2952 0.2608 0.4204 -0.0532 0.0817 0.0668 623 LYS A N 4687 C CA . LYS A 630 ? 0.3239 0.2812 0.4392 -0.0538 0.0858 0.0697 623 LYS A CA 4688 C C . LYS A 630 ? 0.3291 0.2927 0.4339 -0.0509 0.0816 0.0694 623 LYS A C 4689 O O . LYS A 630 ? 0.3330 0.2798 0.4092 -0.0497 0.0727 0.0601 623 LYS A O 4690 C CB . LYS A 630 ? 0.3134 0.2813 0.4443 -0.0658 0.0964 0.0769 623 LYS A CB 4691 C CG . LYS A 630 ? 0.3448 0.2775 0.4699 -0.0814 0.0956 0.0606 623 LYS A CG 4692 C CD . LYS A 630 ? 0.3538 0.2931 0.5558 -0.0836 0.1087 0.0252 623 LYS A CD 4693 C CE . LYS A 630 ? 0.4326 0.3090 0.6234 -0.0568 0.0522 0.0238 623 LYS A CE 4694 N NZ . LYS A 630 ? 0.5175 0.3576 0.6813 -0.0395 0.0162 0.0404 623 LYS A NZ 4695 N N . THR A 631 ? 0.3459 0.3051 0.4249 -0.0462 0.0840 0.0699 624 THR A N 4696 C CA . THR A 631 ? 0.3670 0.3238 0.4205 -0.0406 0.0781 0.0688 624 THR A CA 4697 C C . THR A 631 ? 0.3644 0.3028 0.4081 -0.0387 0.0714 0.0645 624 THR A C 4698 O O . THR A 631 ? 0.3743 0.2870 0.3965 -0.0342 0.0626 0.0662 624 THR A O 4699 C CB . THR A 631 ? 0.3748 0.3400 0.4293 -0.0347 0.0790 0.0717 624 THR A CB 4700 O OG1 . THR A 631 ? 0.4045 0.3812 0.4178 -0.0235 0.0720 0.0910 624 THR A OG1 4701 C CG2 . THR A 631 ? 0.3926 0.3996 0.4324 -0.0238 0.0669 0.0530 624 THR A CG2 4702 N N . TYR A 632 ? 0.3413 0.2695 0.3869 -0.0448 0.0666 0.0636 625 TYR A N 4703 C CA . TYR A 632 ? 0.3398 0.2805 0.3862 -0.0393 0.0641 0.0579 625 TYR A CA 4704 C C . TYR A 632 ? 0.3154 0.2627 0.3815 -0.0401 0.0597 0.0595 625 TYR A C 4705 O O . TYR A 632 ? 0.2637 0.2624 0.3593 -0.0486 0.0549 0.0573 625 TYR A O 4706 C CB . TYR A 632 ? 0.3317 0.2673 0.3866 -0.0484 0.0612 0.0578 625 TYR A CB 4707 C CG . TYR A 632 ? 0.3783 0.3181 0.4007 -0.0505 0.0743 0.0554 625 TYR A CG 4708 C CD1 . TYR A 632 ? 0.3652 0.3255 0.4114 -0.0617 0.0849 0.0720 625 TYR A CD1 4709 C CD2 . TYR A 632 ? 0.3866 0.3461 0.4022 -0.0447 0.0915 0.0580 625 TYR A CD2 4710 C CE1 . TYR A 632 ? 0.4006 0.3904 0.4239 -0.0429 0.0674 0.0583 625 TYR A CE1 4711 C CE2 . TYR A 632 ? 0.4437 0.3623 0.4331 -0.0429 0.0665 0.0465 625 TYR A CE2 4712 C CZ . TYR A 632 ? 0.4411 0.3884 0.4332 -0.0314 0.0689 0.0469 625 TYR A CZ 4713 O OH . TYR A 632 ? 0.4582 0.4385 0.4339 -0.0189 0.0368 0.0374 625 TYR A OH 4714 N N . SER A 633 ? 0.2863 0.2306 0.3720 -0.0409 0.0499 0.0574 626 SER A N 4715 C CA . SER A 633 ? 0.2739 0.2189 0.3720 -0.0323 0.0481 0.0556 626 SER A CA 4716 C C . SER A 633 ? 0.2723 0.2265 0.3641 -0.0365 0.0405 0.0463 626 SER A C 4717 O O . SER A 633 ? 0.2620 0.2326 0.3450 -0.0143 0.0336 0.0330 626 SER A O 4718 C CB A SER A 633 ? 0.2797 0.2107 0.3639 -0.0330 0.0558 0.0543 626 SER A CB 4719 C CB B SER A 633 ? 0.2869 0.2240 0.3773 -0.0343 0.0515 0.0549 626 SER A CB 4720 O OG A SER A 633 ? 0.1986 0.1647 0.3696 0.0035 0.0507 0.0557 626 SER A OG 4721 O OG B SER A 633 ? 0.3245 0.2491 0.3980 -0.0343 0.0555 0.0530 626 SER A OG 4722 N N . VAL A 634 ? 0.2569 0.2177 0.3646 -0.0331 0.0265 0.0510 627 VAL A N 4723 C CA . VAL A 634 ? 0.2761 0.2237 0.3581 -0.0465 0.0308 0.0420 627 VAL A CA 4724 C C . VAL A 634 ? 0.2840 0.2360 0.3700 -0.0430 0.0219 0.0388 627 VAL A C 4725 O O . VAL A 634 ? 0.2784 0.2499 0.3617 -0.0226 0.0142 0.0470 627 VAL A O 4726 C CB . VAL A 634 ? 0.2817 0.2124 0.3586 -0.0464 0.0300 0.0436 627 VAL A CB 4727 C CG1 . VAL A 634 ? 0.2405 0.2061 0.3028 -0.0540 0.0402 0.0503 627 VAL A CG1 4728 C CG2 . VAL A 634 ? 0.3135 0.2061 0.3194 -0.0789 0.0465 0.0279 627 VAL A CG2 4729 N N . SER A 635 ? 0.2912 0.2357 0.3642 -0.0444 0.0205 0.0319 628 SER A N 4730 C CA . SER A 635 ? 0.3035 0.2402 0.3839 -0.0463 0.0137 0.0162 628 SER A CA 4731 C C . SER A 635 ? 0.2842 0.2442 0.3663 -0.0368 0.0124 0.0124 628 SER A C 4732 O O . SER A 635 ? 0.2837 0.2504 0.3673 -0.0420 0.0311 0.0197 628 SER A O 4733 C CB . SER A 635 ? 0.3373 0.2459 0.3863 -0.0640 0.0067 0.0174 628 SER A CB 4734 O OG . SER A 635 ? 0.4544 0.2689 0.4033 -0.0521 -0.0315 0.0068 628 SER A OG 4735 N N . PHE A 636 ? 0.2603 0.2452 0.3737 -0.0363 0.0101 -0.0061 629 PHE A N 4736 C CA . PHE A 636 ? 0.2359 0.2215 0.3682 -0.0207 -0.0030 -0.0103 629 PHE A CA 4737 C C . PHE A 636 ? 0.2306 0.2329 0.3723 -0.0228 -0.0127 -0.0136 629 PHE A C 4738 O O . PHE A 636 ? 0.1972 0.2232 0.3698 -0.0200 -0.0260 -0.0118 629 PHE A O 4739 C CB . PHE A 636 ? 0.2167 0.2162 0.3586 -0.0210 0.0046 -0.0226 629 PHE A CB 4740 C CG . PHE A 636 ? 0.2022 0.2493 0.3531 -0.0072 0.0050 -0.0238 629 PHE A CG 4741 C CD1 . PHE A 636 ? 0.1875 0.2199 0.3137 -0.0022 -0.0138 -0.0052 629 PHE A CD1 4742 C CD2 . PHE A 636 ? 0.1966 0.2927 0.3206 -0.0029 -0.0258 -0.0360 629 PHE A CD2 4743 C CE1 . PHE A 636 ? 0.1832 0.2229 0.2953 0.0346 0.0442 -0.0179 629 PHE A CE1 4744 C CE2 . PHE A 636 ? 0.2255 0.2215 0.3159 -0.0043 -0.0133 -0.0499 629 PHE A CE2 4745 C CZ . PHE A 636 ? 0.2347 0.2443 0.2725 -0.0103 0.0049 -0.0044 629 PHE A CZ 4746 N N . ASP A 637 ? 0.2396 0.2220 0.3752 -0.0323 -0.0284 -0.0268 630 ASP A N 4747 C CA . ASP A 637 ? 0.2559 0.2464 0.3824 -0.0254 -0.0266 -0.0172 630 ASP A CA 4748 C C . ASP A 637 ? 0.2524 0.2373 0.3790 -0.0325 -0.0371 -0.0157 630 ASP A C 4749 O O . ASP A 637 ? 0.2494 0.2519 0.3850 -0.0247 -0.0527 -0.0069 630 ASP A O 4750 C CB . ASP A 637 ? 0.2721 0.2348 0.3768 -0.0417 -0.0277 -0.0204 630 ASP A CB 4751 C CG . ASP A 637 ? 0.3374 0.2872 0.4166 -0.0344 -0.0229 -0.0149 630 ASP A CG 4752 O OD1 . ASP A 637 ? 0.3438 0.3395 0.4592 -0.0346 0.0085 -0.0054 630 ASP A OD1 4753 O OD2 . ASP A 637 ? 0.4453 0.3181 0.4791 -0.0626 -0.0003 0.0345 630 ASP A OD2 4754 N N . SER A 638 ? 0.2419 0.2214 0.3613 -0.0310 -0.0451 -0.0171 631 SER A N 4755 C CA . SER A 638 ? 0.2449 0.2202 0.3399 -0.0247 -0.0469 -0.0174 631 SER A CA 4756 C C . SER A 638 ? 0.2318 0.2034 0.3365 -0.0311 -0.0429 -0.0264 631 SER A C 4757 O O . SER A 638 ? 0.2273 0.1944 0.3140 -0.0264 -0.0464 -0.0257 631 SER A O 4758 C CB . SER A 638 ? 0.2314 0.2176 0.3494 -0.0378 -0.0444 -0.0248 631 SER A CB 4759 O OG . SER A 638 ? 0.2912 0.2184 0.3733 -0.0088 -0.0611 -0.0201 631 SER A OG 4760 N N . LEU A 639 ? 0.1964 0.2050 0.3162 -0.0239 -0.0424 -0.0260 632 LEU A N 4761 C CA . LEU A 639 ? 0.2009 0.1917 0.3199 -0.0212 -0.0356 -0.0277 632 LEU A CA 4762 C C . LEU A 639 ? 0.2133 0.2001 0.3427 -0.0135 -0.0347 -0.0208 632 LEU A C 4763 O O . LEU A 639 ? 0.2202 0.2035 0.3385 -0.0309 -0.0428 -0.0109 632 LEU A O 4764 C CB . LEU A 639 ? 0.2096 0.1869 0.3242 -0.0254 -0.0288 -0.0213 632 LEU A CB 4765 C CG . LEU A 639 ? 0.2002 0.1823 0.2837 -0.0054 -0.0162 -0.0019 632 LEU A CG 4766 C CD1 . LEU A 639 ? 0.1993 0.1705 0.2156 0.0064 -0.0350 0.0422 632 LEU A CD1 4767 C CD2 . LEU A 639 ? 0.2406 0.1645 0.3178 -0.0153 0.0428 -0.0005 632 LEU A CD2 4768 N N . PHE A 640 ? 0.2003 0.1927 0.3534 -0.0087 -0.0367 -0.0171 633 PHE A N 4769 C CA . PHE A 640 ? 0.2247 0.2102 0.3562 -0.0110 -0.0381 -0.0256 633 PHE A CA 4770 C C . PHE A 640 ? 0.2180 0.1982 0.3558 -0.0023 -0.0322 -0.0212 633 PHE A C 4771 O O . PHE A 640 ? 0.2268 0.1833 0.3667 0.0100 -0.0436 -0.0155 633 PHE A O 4772 C CB . PHE A 640 ? 0.2200 0.2250 0.3467 -0.0035 -0.0276 -0.0109 633 PHE A CB 4773 C CG . PHE A 640 ? 0.2461 0.2452 0.3733 0.0119 -0.0294 -0.0320 633 PHE A CG 4774 C CD1 . PHE A 640 ? 0.2398 0.2328 0.3973 -0.0111 -0.0059 -0.0202 633 PHE A CD1 4775 C CD2 . PHE A 640 ? 0.2321 0.2757 0.3954 -0.0033 -0.0285 -0.0554 633 PHE A CD2 4776 C CE1 . PHE A 640 ? 0.2083 0.2279 0.3984 -0.0445 -0.0082 -0.0265 633 PHE A CE1 4777 C CE2 . PHE A 640 ? 0.1897 0.2547 0.3921 0.0012 -0.0324 -0.0528 633 PHE A CE2 4778 C CZ . PHE A 640 ? 0.2423 0.2603 0.3835 -0.0089 -0.0235 -0.0582 633 PHE A CZ 4779 N N . SER A 641 ? 0.2120 0.1755 0.3469 -0.0065 -0.0307 -0.0216 634 SER A N 4780 C CA . SER A 641 ? 0.2229 0.1851 0.3375 0.0009 -0.0387 -0.0254 634 SER A CA 4781 C C . SER A 641 ? 0.2176 0.1873 0.3179 -0.0031 -0.0448 -0.0305 634 SER A C 4782 O O . SER A 641 ? 0.2412 0.2032 0.3152 -0.0248 -0.0570 -0.0421 634 SER A O 4783 C CB . SER A 641 ? 0.2186 0.1809 0.3332 0.0177 -0.0335 -0.0249 634 SER A CB 4784 O OG . SER A 641 ? 0.2366 0.2096 0.3547 0.0127 -0.0642 -0.0406 634 SER A OG 4785 N N . ALA A 642 ? 0.2069 0.1715 0.2888 -0.0027 -0.0575 -0.0342 635 ALA A N 4786 C CA . ALA A 642 ? 0.2068 0.1763 0.2878 -0.0017 -0.0591 -0.0332 635 ALA A CA 4787 C C . ALA A 642 ? 0.2097 0.1857 0.2997 0.0064 -0.0598 -0.0350 635 ALA A C 4788 O O . ALA A 642 ? 0.2104 0.1991 0.3045 0.0233 -0.0493 -0.0474 635 ALA A O 4789 C CB . ALA A 642 ? 0.1847 0.1748 0.2728 -0.0149 -0.0572 -0.0344 635 ALA A CB 4790 N N . VAL A 643 ? 0.2106 0.1884 0.3022 0.0034 -0.0536 -0.0391 636 VAL A N 4791 C CA . VAL A 643 ? 0.2159 0.1900 0.3039 0.0065 -0.0626 -0.0353 636 VAL A CA 4792 C C . VAL A 643 ? 0.2294 0.1989 0.3241 0.0084 -0.0618 -0.0338 636 VAL A C 4793 O O . VAL A 643 ? 0.2326 0.1940 0.3251 0.0128 -0.0568 -0.0196 636 VAL A O 4794 C CB . VAL A 643 ? 0.2168 0.1815 0.2969 0.0060 -0.0677 -0.0311 636 VAL A CB 4795 C CG1 . VAL A 643 ? 0.1973 0.2244 0.2742 -0.0234 -0.0645 -0.0417 636 VAL A CG1 4796 C CG2 . VAL A 643 ? 0.2466 0.1724 0.2830 -0.0182 -0.0521 -0.0269 636 VAL A CG2 4797 N N . LYS A 644 ? 0.2439 0.1767 0.3354 0.0097 -0.0705 -0.0458 637 LYS A N 4798 C CA . LYS A 644 ? 0.2395 0.2074 0.3346 0.0038 -0.0947 -0.0504 637 LYS A CA 4799 C C . LYS A 644 ? 0.2438 0.2131 0.3336 0.0055 -0.0967 -0.0512 637 LYS A C 4800 O O . LYS A 644 ? 0.2342 0.2338 0.3428 -0.0004 -0.1065 -0.0564 637 LYS A O 4801 C CB . LYS A 644 ? 0.2546 0.1802 0.3413 -0.0028 -0.0955 -0.0591 637 LYS A CB 4802 C CG . LYS A 644 ? 0.3632 0.2380 0.3992 -0.0262 -0.0980 -0.0606 637 LYS A CG 4803 C CD . LYS A 644 ? 0.4434 0.2544 0.4900 -0.0527 -0.0587 -0.0646 637 LYS A CD 4804 C CE . LYS A 644 ? 0.5182 0.3494 0.5470 -0.0129 -0.0553 -0.1032 637 LYS A CE 4805 N NZ . LYS A 644 ? 0.5827 0.4040 0.6031 -0.0024 -0.0263 -0.0854 637 LYS A NZ 4806 N N . ASN A 645 ? 0.2353 0.2205 0.3139 0.0056 -0.0954 -0.0545 638 ASN A N 4807 C CA . ASN A 645 ? 0.2367 0.2202 0.3144 0.0179 -0.0878 -0.0516 638 ASN A CA 4808 C C . ASN A 645 ? 0.2294 0.2228 0.3053 0.0198 -0.0861 -0.0555 638 ASN A C 4809 O O . ASN A 645 ? 0.1981 0.2313 0.2811 0.0391 -0.0708 -0.0654 638 ASN A O 4810 C CB . ASN A 645 ? 0.2356 0.2027 0.2819 0.0115 -0.1004 -0.0525 638 ASN A CB 4811 C CG . ASN A 645 ? 0.2712 0.2237 0.3411 -0.0057 -0.0938 -0.0640 638 ASN A CG 4812 O OD1 . ASN A 645 ? 0.2958 0.1932 0.3367 -0.0733 -0.1080 -0.0543 638 ASN A OD1 4813 N ND2 . ASN A 645 ? 0.2890 0.2528 0.3096 0.0325 -0.0755 -0.0456 638 ASN A ND2 4814 N N . PHE A 646 ? 0.2291 0.2124 0.2998 0.0375 -0.0755 -0.0674 639 PHE A N 4815 C CA . PHE A 646 ? 0.2336 0.2187 0.2941 0.0210 -0.0720 -0.0644 639 PHE A CA 4816 C C . PHE A 646 ? 0.2487 0.2363 0.3190 0.0231 -0.0786 -0.0688 639 PHE A C 4817 O O . PHE A 646 ? 0.2322 0.2416 0.2987 0.0152 -0.0798 -0.0654 639 PHE A O 4818 C CB . PHE A 646 ? 0.2311 0.2026 0.2908 0.0169 -0.0629 -0.0687 639 PHE A CB 4819 C CG . PHE A 646 ? 0.2574 0.2259 0.2686 0.0270 -0.0650 -0.0533 639 PHE A CG 4820 C CD1 . PHE A 646 ? 0.2466 0.1985 0.2407 0.0435 -0.0606 -0.0608 639 PHE A CD1 4821 C CD2 . PHE A 646 ? 0.2521 0.2016 0.2532 0.0360 -0.0490 -0.0663 639 PHE A CD2 4822 C CE1 . PHE A 646 ? 0.2438 0.2549 0.2961 0.0338 -0.0613 -0.0424 639 PHE A CE1 4823 C CE2 . PHE A 646 ? 0.2958 0.2192 0.2074 0.0128 -0.0770 -0.0544 639 PHE A CE2 4824 C CZ . PHE A 646 ? 0.2268 0.2488 0.2357 0.0543 -0.0790 -0.0576 639 PHE A CZ 4825 N N . THR A 647 ? 0.2527 0.2490 0.3364 0.0152 -0.0862 -0.0770 640 THR A N 4826 C CA . THR A 647 ? 0.2663 0.2485 0.3410 0.0336 -0.1007 -0.0716 640 THR A CA 4827 C C . THR A 647 ? 0.2821 0.2557 0.3517 0.0248 -0.1046 -0.0699 640 THR A C 4828 O O . THR A 647 ? 0.2815 0.2659 0.3453 0.0222 -0.1129 -0.0687 640 THR A O 4829 C CB . THR A 647 ? 0.2619 0.2535 0.3368 0.0265 -0.1027 -0.0741 640 THR A CB 4830 O OG1 . THR A 647 ? 0.2935 0.2640 0.3514 0.0434 -0.0937 -0.0570 640 THR A OG1 4831 C CG2 . THR A 647 ? 0.2504 0.2839 0.3490 0.0477 -0.0928 -0.0309 640 THR A CG2 4832 N N . GLU A 648 ? 0.2903 0.2339 0.3621 0.0311 -0.1054 -0.0727 641 GLU A N 4833 C CA . GLU A 648 ? 0.3243 0.2488 0.3596 0.0235 -0.1042 -0.0711 641 GLU A CA 4834 C C . GLU A 648 ? 0.3165 0.2444 0.3454 0.0210 -0.1150 -0.0666 641 GLU A C 4835 O O . GLU A 648 ? 0.3079 0.2594 0.3292 0.0167 -0.1135 -0.0774 641 GLU A O 4836 C CB . GLU A 648 ? 0.3275 0.2419 0.3699 0.0065 -0.1143 -0.0658 641 GLU A CB 4837 C CG . GLU A 648 ? 0.4089 0.2667 0.4387 -0.0019 -0.0933 -0.0686 641 GLU A CG 4838 C CD . GLU A 648 ? 0.4815 0.3134 0.5315 -0.0087 -0.1020 -0.0334 641 GLU A CD 4839 O OE1 . GLU A 648 ? 0.5401 0.2919 0.5455 -0.0969 -0.1395 -0.0624 641 GLU A OE1 4840 O OE2 . GLU A 648 ? 0.5430 0.3234 0.6163 0.0468 -0.0731 -0.0326 641 GLU A OE2 4841 N N . ILE A 649 ? 0.3178 0.2555 0.3259 0.0248 -0.1177 -0.0690 642 ILE A N 4842 C CA . ILE A 649 ? 0.3047 0.2494 0.3066 0.0231 -0.1188 -0.0608 642 ILE A CA 4843 C C . ILE A 649 ? 0.3085 0.2552 0.3040 0.0250 -0.1237 -0.0730 642 ILE A C 4844 O O . ILE A 649 ? 0.3171 0.2544 0.2857 0.0026 -0.1275 -0.0697 642 ILE A O 4845 C CB . ILE A 649 ? 0.3047 0.2542 0.3063 0.0286 -0.1147 -0.0431 642 ILE A CB 4846 C CG1 . ILE A 649 ? 0.2987 0.2481 0.3025 0.0473 -0.0952 -0.0301 642 ILE A CG1 4847 C CG2 . ILE A 649 ? 0.2729 0.2441 0.2796 0.0043 -0.1451 -0.0507 642 ILE A CG2 4848 C CD1 . ILE A 649 ? 0.3287 0.2202 0.2650 0.0047 -0.0826 -0.0076 642 ILE A CD1 4849 N N . ALA A 650 ? 0.2924 0.2495 0.2987 0.0452 -0.1199 -0.0920 643 ALA A N 4850 C CA . ALA A 650 ? 0.3337 0.2635 0.3088 0.0400 -0.1109 -0.0877 643 ALA A CA 4851 C C . ALA A 650 ? 0.3483 0.2793 0.3291 0.0420 -0.1143 -0.0908 643 ALA A C 4852 O O . ALA A 650 ? 0.3687 0.2860 0.3586 0.0275 -0.1099 -0.0859 643 ALA A O 4853 C CB . ALA A 650 ? 0.3280 0.2514 0.3086 0.0581 -0.1054 -0.0876 643 ALA A CB 4854 N N . SER A 651 ? 0.3452 0.2896 0.3369 0.0385 -0.1148 -0.0951 644 SER A N 4855 C CA . SER A 651 ? 0.3640 0.3062 0.3508 0.0426 -0.1222 -0.0993 644 SER A CA 4856 C C . SER A 651 ? 0.3598 0.3008 0.3447 0.0448 -0.1304 -0.0984 644 SER A C 4857 O O . SER A 651 ? 0.3695 0.3019 0.3520 0.0476 -0.1353 -0.1018 644 SER A O 4858 C CB . SER A 651 ? 0.3537 0.3385 0.3570 0.0338 -0.1279 -0.0920 644 SER A CB 4859 O OG . SER A 651 ? 0.4327 0.3906 0.4192 0.0372 -0.0873 -0.1153 644 SER A OG 4860 N N . LYS A 652 ? 0.3625 0.2721 0.3368 0.0491 -0.1290 -0.1005 645 LYS A N 4861 C CA . LYS A 652 ? 0.3757 0.2832 0.3435 0.0491 -0.1310 -0.0963 645 LYS A CA 4862 C C . LYS A 652 ? 0.3691 0.2815 0.3311 0.0627 -0.1311 -0.0946 645 LYS A C 4863 O O . LYS A 652 ? 0.3517 0.2837 0.3343 0.0543 -0.1328 -0.1007 645 LYS A O 4864 C CB . LYS A 652 ? 0.3793 0.2622 0.3491 0.0561 -0.1316 -0.1015 645 LYS A CB 4865 C CG . LYS A 652 ? 0.4033 0.3050 0.3588 0.0092 -0.1392 -0.1063 645 LYS A CG 4866 C CD . LYS A 652 ? 0.4394 0.3188 0.3935 0.0043 -0.1530 -0.1038 645 LYS A CD 4867 C CE . LYS A 652 ? 0.4470 0.3239 0.4193 -0.0102 -0.1660 -0.1104 645 LYS A CE 4868 N NZ . LYS A 652 ? 0.4737 0.3344 0.4178 -0.0245 -0.1545 -0.0949 645 LYS A NZ 4869 N N . PHE A 653 ? 0.3586 0.2709 0.3074 0.0743 -0.1369 -0.0911 646 PHE A N 4870 C CA . PHE A 653 ? 0.3625 0.2756 0.2943 0.0817 -0.1341 -0.0889 646 PHE A CA 4871 C C . PHE A 653 ? 0.3787 0.2933 0.2969 0.0845 -0.1335 -0.0931 646 PHE A C 4872 O O . PHE A 653 ? 0.3697 0.2977 0.2948 0.0844 -0.1307 -0.0846 646 PHE A O 4873 C CB . PHE A 653 ? 0.3716 0.2790 0.2962 0.0738 -0.1258 -0.0800 646 PHE A CB 4874 C CG . PHE A 653 ? 0.3627 0.2730 0.2924 0.0623 -0.1199 -0.0729 646 PHE A CG 4875 C CD1 . PHE A 653 ? 0.3446 0.2803 0.2700 0.0290 -0.1416 -0.0512 646 PHE A CD1 4876 C CD2 . PHE A 653 ? 0.3367 0.2830 0.2635 0.0714 -0.0810 -0.0886 646 PHE A CD2 4877 C CE1 . PHE A 653 ? 0.3216 0.2913 0.2571 0.0292 -0.1641 -0.0627 646 PHE A CE1 4878 C CE2 . PHE A 653 ? 0.3279 0.2829 0.2788 0.0547 -0.0992 -0.0802 646 PHE A CE2 4879 C CZ . PHE A 653 ? 0.3116 0.2797 0.2956 0.0455 -0.1084 -0.0650 646 PHE A CZ 4880 N N . SER A 654 ? 0.3636 0.3005 0.3010 0.0984 -0.1385 -0.0990 647 SER A N 4881 C CA . SER A 654 ? 0.3891 0.3327 0.3122 0.1026 -0.1375 -0.0972 647 SER A CA 4882 C C . SER A 654 ? 0.4008 0.3579 0.3261 0.1141 -0.1298 -0.0987 647 SER A C 4883 O O . SER A 654 ? 0.3934 0.3771 0.3039 0.1240 -0.1198 -0.0866 647 SER A O 4884 C CB . SER A 654 ? 0.3839 0.3229 0.3005 0.1277 -0.1346 -0.0970 647 SER A CB 4885 O OG A SER A 654 ? 0.3812 0.2973 0.3418 0.1047 -0.1365 -0.1221 647 SER A OG 4886 O OG B SER A 654 ? 0.4308 0.3473 0.3552 0.1054 -0.1214 -0.0656 647 SER A OG 4887 N N . GLU A 655 ? 0.4088 0.3526 0.3434 0.1122 -0.1404 -0.1077 648 GLU A N 4888 C CA . GLU A 655 ? 0.4592 0.3918 0.3713 0.1044 -0.1466 -0.1064 648 GLU A CA 4889 C C . GLU A 655 ? 0.4517 0.3917 0.3590 0.1049 -0.1567 -0.1006 648 GLU A C 4890 O O . GLU A 655 ? 0.4298 0.4047 0.3558 0.1073 -0.1773 -0.0948 648 GLU A O 4891 C CB . GLU A 655 ? 0.4827 0.4023 0.3911 0.0884 -0.1530 -0.1079 648 GLU A CB 4892 C CG . GLU A 655 ? 0.5596 0.4844 0.4928 0.0622 -0.1146 -0.1146 648 GLU A CG 4893 C CD . GLU A 655 ? 0.6813 0.5092 0.6180 0.0292 -0.0856 -0.1298 648 GLU A CD 4894 O OE1 . GLU A 655 ? 0.7045 0.5284 0.6349 -0.0062 -0.0622 -0.1659 648 GLU A OE1 4895 O OE2 . GLU A 655 ? 0.7309 0.5796 0.6797 0.0024 -0.0608 -0.1161 648 GLU A OE2 4896 N N . ARG A 656 ? 0.4439 0.3617 0.3440 0.1329 -0.1567 -0.0925 649 ARG A N 4897 C CA . ARG A 656 ? 0.4408 0.3595 0.3212 0.1292 -0.1544 -0.0896 649 ARG A CA 4898 C C . ARG A 656 ? 0.4474 0.3673 0.3186 0.1271 -0.1462 -0.0979 649 ARG A C 4899 O O . ARG A 656 ? 0.4412 0.3580 0.3205 0.1350 -0.1247 -0.1060 649 ARG A O 4900 C CB . ARG A 656 ? 0.4376 0.3491 0.3357 0.1300 -0.1506 -0.0931 649 ARG A CB 4901 C CG . ARG A 656 ? 0.4164 0.3503 0.3092 0.1329 -0.1550 -0.0655 649 ARG A CG 4902 C CD . ARG A 656 ? 0.4103 0.3185 0.3370 0.1286 -0.1314 -0.0516 649 ARG A CD 4903 N NE . ARG A 656 ? 0.4139 0.3388 0.3040 0.1307 -0.1078 -0.0690 649 ARG A NE 4904 C CZ . ARG A 656 ? 0.4325 0.3326 0.3308 0.0968 -0.0951 -0.0652 649 ARG A CZ 4905 N NH1 . ARG A 656 ? 0.4208 0.3074 0.3680 0.1083 -0.0638 -0.0454 649 ARG A NH1 4906 N NH2 . ARG A 656 ? 0.3643 0.3341 0.2775 0.1041 -0.1140 -0.0553 649 ARG A NH2 4907 N N . LEU A 657 ? 0.4515 0.3815 0.3057 0.1339 -0.1384 -0.1038 650 LEU A N 4908 C CA . LEU A 657 ? 0.5051 0.4076 0.3289 0.1371 -0.1271 -0.0999 650 LEU A CA 4909 C C . LEU A 657 ? 0.5537 0.4496 0.3634 0.1397 -0.1345 -0.0923 650 LEU A C 4910 O O . LEU A 657 ? 0.5488 0.4452 0.3507 0.1473 -0.1345 -0.0835 650 LEU A O 4911 C CB . LEU A 657 ? 0.5085 0.3839 0.3349 0.1287 -0.1093 -0.1079 650 LEU A CB 4912 C CG . LEU A 657 ? 0.4887 0.3905 0.3160 0.1458 -0.0750 -0.1326 650 LEU A CG 4913 C CD1 . LEU A 657 ? 0.4584 0.3495 0.2577 0.1588 -0.0828 -0.1123 650 LEU A CD1 4914 C CD2 . LEU A 657 ? 0.4934 0.3327 0.2641 0.1506 -0.0746 -0.1537 650 LEU A CD2 4915 N N . GLN A 658 ? 0.6024 0.5022 0.3996 0.1306 -0.1463 -0.0966 651 GLN A N 4916 C CA . GLN A 658 ? 0.6618 0.5627 0.4559 0.1314 -0.1605 -0.0917 651 GLN A CA 4917 C C . GLN A 658 ? 0.6896 0.5809 0.4668 0.1264 -0.1618 -0.0977 651 GLN A C 4918 O O . GLN A 658 ? 0.7039 0.6036 0.4712 0.1172 -0.1799 -0.0810 651 GLN A O 4919 C CB . GLN A 658 ? 0.6745 0.5727 0.4642 0.1306 -0.1569 -0.0897 651 GLN A CB 4920 C CG . GLN A 658 ? 0.6967 0.6084 0.4867 0.1513 -0.1612 -0.0835 651 GLN A CG 4921 C CD . GLN A 658 ? 0.7210 0.6088 0.5329 0.1440 -0.1778 -0.0893 651 GLN A CD 4922 O OE1 . GLN A 658 ? 0.7144 0.6536 0.5646 0.1251 -0.1936 -0.0790 651 GLN A OE1 4923 N NE2 . GLN A 658 ? 0.7290 0.6335 0.5210 0.1383 -0.1936 -0.0986 651 GLN A NE2 4924 N N . ASP A 659 ? 0.7163 0.5888 0.4935 0.1345 -0.1568 -0.1112 652 ASP A N 4925 C CA . ASP A 659 ? 0.7456 0.6018 0.5023 0.1252 -0.1491 -0.1286 652 ASP A CA 4926 C C . ASP A 659 ? 0.7453 0.5981 0.5022 0.1287 -0.1419 -0.1391 652 ASP A C 4927 O O . ASP A 659 ? 0.7527 0.5973 0.5129 0.1143 -0.1437 -0.1415 652 ASP A O 4928 C CB . ASP A 659 ? 0.7574 0.6070 0.5067 0.1338 -0.1505 -0.1276 652 ASP A CB 4929 C CG . ASP A 659 ? 0.7816 0.6321 0.5615 0.1373 -0.1369 -0.1158 652 ASP A CG 4930 O OD1 . ASP A 659 ? 0.8434 0.6349 0.6253 0.1395 -0.1096 -0.1089 652 ASP A OD1 4931 O OD2 . ASP A 659 ? 0.7826 0.6752 0.6323 0.1641 -0.1210 -0.1052 652 ASP A OD2 4932 N N . PHE A 660 ? 0.7397 0.5998 0.4854 0.1237 -0.1412 -0.1504 653 PHE A N 4933 C CA . PHE A 660 ? 0.7248 0.5873 0.4326 0.1183 -0.1432 -0.1493 653 PHE A CA 4934 C C . PHE A 660 ? 0.7440 0.6165 0.4188 0.1121 -0.1447 -0.1594 653 PHE A C 4935 O O . PHE A 660 ? 0.7529 0.6205 0.3695 0.1003 -0.1271 -0.1959 653 PHE A O 4936 C CB . PHE A 660 ? 0.7106 0.5762 0.4483 0.1375 -0.1336 -0.1379 653 PHE A CB 4937 C CG . PHE A 660 ? 0.6119 0.5470 0.3458 0.1376 -0.1399 -0.1310 653 PHE A CG 4938 C CD1 . PHE A 660 ? 0.5863 0.5073 0.2857 0.1905 -0.0823 -0.1139 653 PHE A CD1 4939 C CD2 . PHE A 660 ? 0.6010 0.5121 0.2857 0.1059 -0.1446 -0.1146 653 PHE A CD2 4940 C CE1 . PHE A 660 ? 0.6177 0.4913 0.3494 0.1449 -0.0665 -0.0949 653 PHE A CE1 4941 C CE2 . PHE A 660 ? 0.6023 0.5032 0.3714 0.1429 -0.0826 -0.0852 653 PHE A CE2 4942 C CZ . PHE A 660 ? 0.6288 0.4711 0.4012 0.1612 -0.0434 -0.0745 653 PHE A CZ 4943 N N A SER A 663 ? 0.4209 0.3358 0.1324 0.1806 -0.1251 -0.0443 656 SER A N 4944 N N B SER A 663 ? 0.4700 0.2843 0.0931 0.2277 -0.0706 -0.0468 656 SER A N 4945 C CA A SER A 663 ? 0.4549 0.3193 0.1055 0.1765 -0.1002 -0.0411 656 SER A CA 4946 C CA B SER A 663 ? 0.4786 0.3008 0.0869 0.1947 -0.0680 -0.0396 656 SER A CA 4947 C C A SER A 663 ? 0.4569 0.3250 0.1185 0.1800 -0.0966 -0.0377 656 SER A C 4948 C C B SER A 663 ? 0.4903 0.3161 0.0976 0.1956 -0.0674 -0.0426 656 SER A C 4949 O O A SER A 663 ? 0.4495 0.3152 0.1123 0.1934 -0.0927 -0.0292 656 SER A O 4950 O O B SER A 663 ? 0.4870 0.3138 0.1131 0.1949 -0.0667 -0.0453 656 SER A O 4951 C CB A SER A 663 ? 0.4328 0.3163 0.0982 0.1804 -0.1090 -0.0456 656 SER A CB 4952 C CB B SER A 663 ? 0.4536 0.2997 0.0768 0.1907 -0.0822 -0.0327 656 SER A CB 4953 O OG A SER A 663 ? 0.4341 0.2663 0.0584 0.0920 -0.0994 -0.0667 656 SER A OG 4954 O OG B SER A 663 ? 0.4180 0.2845 0.0419 0.0879 -0.0791 -0.0052 656 SER A OG 4955 N N A ASN A 664 ? 0.4651 0.3185 0.1084 0.1685 -0.0954 -0.0350 657 ASN A N 4956 N N B ASN A 664 ? 0.5010 0.3066 0.1094 0.1953 -0.0576 -0.0386 657 ASN A N 4957 C CA A ASN A 664 ? 0.4555 0.3113 0.1241 0.1700 -0.0684 -0.0435 657 ASN A CA 4958 C CA B ASN A 664 ? 0.4979 0.3254 0.1276 0.1864 -0.0478 -0.0386 657 ASN A CA 4959 C C A ASN A 664 ? 0.4552 0.3182 0.1207 0.1625 -0.0592 -0.0404 657 ASN A C 4960 C C B ASN A 664 ? 0.4922 0.3234 0.1346 0.1772 -0.0368 -0.0361 657 ASN A C 4961 O O A ASN A 664 ? 0.4441 0.3212 0.1128 0.1542 -0.0639 -0.0526 657 ASN A O 4962 O O B ASN A 664 ? 0.4912 0.3244 0.1334 0.1742 -0.0261 -0.0342 657 ASN A O 4963 C CB A ASN A 664 ? 0.4606 0.3168 0.1282 0.1673 -0.0743 -0.0367 657 ASN A CB 4964 C CB B ASN A 664 ? 0.5025 0.3124 0.1319 0.1924 -0.0574 -0.0470 657 ASN A CB 4965 C CG A ASN A 664 ? 0.4665 0.3339 0.1330 0.1542 -0.0762 -0.0415 657 ASN A CG 4966 C CG B ASN A 664 ? 0.5250 0.3342 0.1538 0.1844 -0.0716 -0.0554 657 ASN A CG 4967 O OD1 A ASN A 664 ? 0.4622 0.3752 0.1361 0.1276 -0.0973 -0.0157 657 ASN A OD1 4968 O OD1 B ASN A 664 ? 0.5661 0.4007 0.1603 0.1704 -0.1100 -0.0410 657 ASN A OD1 4969 N ND2 A ASN A 664 ? 0.4557 0.3336 0.1264 0.1411 -0.0980 -0.0459 657 ASN A ND2 4970 N ND2 B ASN A 664 ? 0.5157 0.3314 0.0906 0.2023 -0.0879 -0.0720 657 ASN A ND2 4971 N N A PRO A 665 ? 0.4544 0.3095 0.1293 0.1612 -0.0423 -0.0411 658 PRO A N 4972 N N B PRO A 665 ? 0.4864 0.3292 0.1395 0.1707 -0.0255 -0.0247 658 PRO A N 4973 C CA A PRO A 665 ? 0.4456 0.2997 0.1335 0.1615 -0.0331 -0.0340 658 PRO A CA 4974 C CA B PRO A 665 ? 0.4729 0.3246 0.1418 0.1635 -0.0240 -0.0236 658 PRO A CA 4975 C C A PRO A 665 ? 0.4438 0.2924 0.1385 0.1561 -0.0291 -0.0273 658 PRO A C 4976 C C B PRO A 665 ? 0.4683 0.3251 0.1526 0.1566 -0.0202 -0.0286 658 PRO A C 4977 O O A PRO A 665 ? 0.4493 0.2937 0.1424 0.1546 -0.0273 -0.0248 658 PRO A O 4978 O O B PRO A 665 ? 0.4688 0.3152 0.1481 0.1509 -0.0191 -0.0335 658 PRO A O 4979 C CB A PRO A 665 ? 0.4469 0.2863 0.1277 0.1649 -0.0318 -0.0272 658 PRO A CB 4980 C CB B PRO A 665 ? 0.4766 0.3445 0.1476 0.1631 -0.0301 -0.0179 658 PRO A CB 4981 C CG A PRO A 665 ? 0.4476 0.3013 0.1328 0.1624 -0.0265 -0.0327 658 PRO A CG 4982 C CG B PRO A 665 ? 0.4648 0.3495 0.1246 0.1595 -0.0207 -0.0232 658 PRO A CG 4983 C CD A PRO A 665 ? 0.4581 0.3077 0.1281 0.1605 -0.0359 -0.0413 658 PRO A CD 4984 C CD B PRO A 665 ? 0.4834 0.3248 0.1297 0.1729 -0.0306 -0.0218 658 PRO A CD 4985 N N A ILE A 666 ? 0.4328 0.2872 0.1523 0.1506 -0.0307 -0.0261 659 ILE A N 4986 N N B ILE A 666 ? 0.4571 0.3200 0.1596 0.1548 -0.0156 -0.0298 659 ILE A N 4987 C CA A ILE A 666 ? 0.4288 0.2877 0.1615 0.1406 -0.0329 -0.0299 659 ILE A CA 4988 C CA B ILE A 666 ? 0.4575 0.3271 0.1738 0.1518 -0.0168 -0.0354 659 ILE A CA 4989 C C A ILE A 666 ? 0.4194 0.2891 0.1557 0.1397 -0.0349 -0.0341 659 ILE A C 4990 C C B ILE A 666 ? 0.4474 0.3155 0.1705 0.1498 -0.0234 -0.0386 659 ILE A C 4991 O O A ILE A 666 ? 0.4150 0.2872 0.1744 0.1274 -0.0367 -0.0347 659 ILE A O 4992 O O B ILE A 666 ? 0.4451 0.3188 0.1805 0.1484 -0.0213 -0.0441 659 ILE A O 4993 C CB A ILE A 666 ? 0.4290 0.2919 0.1719 0.1411 -0.0323 -0.0220 659 ILE A CB 4994 C CB B ILE A 666 ? 0.4640 0.3369 0.1868 0.1468 -0.0203 -0.0257 659 ILE A CB 4995 C CG1 A ILE A 666 ? 0.4456 0.3032 0.2058 0.1288 -0.0288 -0.0304 659 ILE A CG1 4996 C CG1 B ILE A 666 ? 0.4763 0.3628 0.2029 0.1359 -0.0107 -0.0311 659 ILE A CG1 4997 C CG2 A ILE A 666 ? 0.4351 0.2815 0.1782 0.1392 -0.0388 -0.0256 659 ILE A CG2 4998 C CG2 B ILE A 666 ? 0.4551 0.3442 0.1582 0.1566 -0.0060 -0.0209 659 ILE A CG2 4999 C CD1 A ILE A 666 ? 0.4523 0.3195 0.2676 0.1144 -0.0294 -0.0497 659 ILE A CD1 5000 C CD1 B ILE A 666 ? 0.4939 0.3676 0.1940 0.1295 -0.0038 -0.0412 659 ILE A CD1 5001 N N A VAL A 667 ? 0.4090 0.2858 0.1575 0.1352 -0.0399 -0.0359 660 VAL A N 5002 N N B VAL A 667 ? 0.4370 0.3173 0.1836 0.1526 -0.0281 -0.0384 660 VAL A N 5003 C CA A VAL A 667 ? 0.4100 0.2867 0.1615 0.1338 -0.0417 -0.0436 660 VAL A CA 5004 C CA B VAL A 667 ? 0.4223 0.3047 0.1643 0.1475 -0.0355 -0.0376 660 VAL A CA 5005 C C A VAL A 667 ? 0.4059 0.2888 0.1637 0.1373 -0.0443 -0.0376 660 VAL A C 5006 C C B VAL A 667 ? 0.4173 0.2984 0.1585 0.1449 -0.0382 -0.0388 660 VAL A C 5007 O O A VAL A 667 ? 0.4098 0.2882 0.1716 0.1418 -0.0360 -0.0436 660 VAL A O 5008 O O B VAL A 667 ? 0.4181 0.3163 0.1688 0.1377 -0.0425 -0.0390 660 VAL A O 5009 C CB A VAL A 667 ? 0.4069 0.2933 0.1498 0.1297 -0.0418 -0.0370 660 VAL A CB 5010 C CB B VAL A 667 ? 0.4299 0.3082 0.1644 0.1510 -0.0332 -0.0403 660 VAL A CB 5011 C CG1 A VAL A 667 ? 0.3991 0.3126 0.1738 0.1284 -0.0616 -0.0432 660 VAL A CG1 5012 C CG1 B VAL A 667 ? 0.4163 0.3103 0.1271 0.1426 -0.0349 -0.0276 660 VAL A CG1 5013 C CG2 A VAL A 667 ? 0.4184 0.2721 0.1602 0.1157 -0.0366 -0.0357 660 VAL A CG2 5014 C CG2 B VAL A 667 ? 0.4129 0.2993 0.1645 0.1535 -0.0328 -0.0305 660 VAL A CG2 5015 N N A LEU A 668 ? 0.3931 0.2736 0.1553 0.1418 -0.0487 -0.0330 661 LEU A N 5016 N N B LEU A 668 ? 0.3932 0.2814 0.1477 0.1465 -0.0454 -0.0412 661 LEU A N 5017 C CA A LEU A 668 ? 0.3879 0.2670 0.1486 0.1404 -0.0453 -0.0322 661 LEU A CA 5018 C CA B LEU A 668 ? 0.3892 0.2711 0.1397 0.1413 -0.0430 -0.0468 661 LEU A CA 5019 C C A LEU A 668 ? 0.3857 0.2641 0.1515 0.1408 -0.0466 -0.0263 661 LEU A C 5020 C C B LEU A 668 ? 0.3807 0.2634 0.1418 0.1378 -0.0432 -0.0397 661 LEU A C 5021 O O A LEU A 668 ? 0.3842 0.2563 0.1688 0.1571 -0.0454 -0.0244 661 LEU A O 5022 O O B LEU A 668 ? 0.3828 0.2555 0.1346 0.1402 -0.0385 -0.0400 661 LEU A O 5023 C CB A LEU A 668 ? 0.3786 0.2601 0.1376 0.1473 -0.0451 -0.0319 661 LEU A CB 5024 C CB B LEU A 668 ? 0.3803 0.2562 0.1369 0.1490 -0.0470 -0.0515 661 LEU A CB 5025 C CG A LEU A 668 ? 0.3695 0.2612 0.1168 0.1370 -0.0366 -0.0249 661 LEU A CG 5026 C CG B LEU A 668 ? 0.3770 0.2649 0.1321 0.1407 -0.0534 -0.0553 661 LEU A CG 5027 C CD1 A LEU A 668 ? 0.3752 0.2773 0.0432 0.1459 -0.0145 -0.0342 661 LEU A CD1 5028 C CD1 B LEU A 668 ? 0.3866 0.2675 0.1043 0.1438 -0.0304 -0.0774 661 LEU A CD1 5029 C CD2 A LEU A 668 ? 0.3512 0.2344 0.0966 0.1784 -0.0292 -0.0063 661 LEU A CD2 5030 C CD2 B LEU A 668 ? 0.3587 0.2283 0.0563 0.1694 -0.0980 -0.0658 661 LEU A CD2 5031 N N A ARG A 669 ? 0.3759 0.2589 0.1510 0.1370 -0.0512 -0.0237 662 ARG A N 5032 N N B ARG A 669 ? 0.3792 0.2583 0.1462 0.1369 -0.0421 -0.0390 662 ARG A N 5033 C CA A ARG A 669 ? 0.3715 0.2561 0.1507 0.1294 -0.0457 -0.0269 662 ARG A CA 5034 C CA B ARG A 669 ? 0.3745 0.2593 0.1493 0.1252 -0.0429 -0.0338 662 ARG A CA 5035 C C A ARG A 669 ? 0.3681 0.2574 0.1547 0.1293 -0.0545 -0.0277 662 ARG A C 5036 C C B ARG A 669 ? 0.3755 0.2545 0.1557 0.1266 -0.0501 -0.0319 662 ARG A C 5037 O O A ARG A 669 ? 0.3533 0.2416 0.1308 0.1228 -0.0670 -0.0234 662 ARG A O 5038 O O B ARG A 669 ? 0.3711 0.2267 0.1401 0.1267 -0.0435 -0.0362 662 ARG A O 5039 C CB A ARG A 669 ? 0.3741 0.2580 0.1521 0.1293 -0.0449 -0.0331 662 ARG A CB 5040 C CB B ARG A 669 ? 0.3691 0.2633 0.1466 0.1330 -0.0393 -0.0359 662 ARG A CB 5041 C CG A ARG A 669 ? 0.3618 0.2416 0.1492 0.1248 -0.0307 -0.0464 662 ARG A CG 5042 C CG B ARG A 669 ? 0.3503 0.2530 0.1429 0.1195 -0.0294 -0.0502 662 ARG A CG 5043 C CD A ARG A 669 ? 0.3565 0.2668 0.1397 0.1359 -0.0015 -0.0589 662 ARG A CD 5044 C CD B ARG A 669 ? 0.3743 0.2865 0.1515 0.1154 -0.0171 -0.0505 662 ARG A CD 5045 N NE A ARG A 669 ? 0.3608 0.2815 0.2115 0.1340 0.0168 -0.0709 662 ARG A NE 5046 N NE B ARG A 669 ? 0.3773 0.2941 0.1737 0.1185 0.0006 -0.0721 662 ARG A NE 5047 C CZ A ARG A 669 ? 0.3740 0.3014 0.2125 0.1166 0.0112 -0.0357 662 ARG A CZ 5048 C CZ B ARG A 669 ? 0.3755 0.2849 0.1815 0.1065 0.0122 -0.0464 662 ARG A CZ 5049 N NH1 A ARG A 669 ? 0.3311 0.3297 0.1651 0.1309 0.0107 -0.0201 662 ARG A NH1 5050 N NH1 B ARG A 669 ? 0.3695 0.2930 0.1143 0.1063 0.0168 -0.0180 662 ARG A NH1 5051 N NH2 A ARG A 669 ? 0.4073 0.3471 0.2147 0.1112 0.0068 -0.0659 662 ARG A NH2 5052 N NH2 B ARG A 669 ? 0.3348 0.3109 0.1134 0.1048 0.0627 -0.0586 662 ARG A NH2 5053 N N . MET A 670 ? 0.3859 0.2562 0.1688 0.1229 -0.0570 -0.0347 663 MET A N 5054 C CA . MET A 670 ? 0.3836 0.2608 0.1799 0.1169 -0.0529 -0.0352 663 MET A CA 5055 C C . MET A 670 ? 0.3838 0.2719 0.1933 0.1157 -0.0631 -0.0454 663 MET A C 5056 O O . MET A 670 ? 0.3892 0.2636 0.1900 0.1021 -0.0788 -0.0395 663 MET A O 5057 C CB A MET A 670 ? 0.3840 0.2559 0.1731 0.1117 -0.0473 -0.0414 663 MET A CB 5058 C CB B MET A 670 ? 0.3902 0.2685 0.1778 0.1160 -0.0505 -0.0398 663 MET A CB 5059 C CG A MET A 670 ? 0.3713 0.2345 0.1610 0.1097 -0.0408 -0.0527 663 MET A CG 5060 C CG B MET A 670 ? 0.3903 0.2834 0.1954 0.1243 -0.0484 -0.0304 663 MET A CG 5061 S SD A MET A 670 ? 0.3930 0.2166 0.1925 0.1010 0.0277 -0.0361 663 MET A SD 5062 S SD B MET A 670 ? 0.4109 0.3373 0.1385 0.1076 -0.0519 -0.0834 663 MET A SD 5063 C CE A MET A 670 ? 0.4033 0.2641 0.1917 0.0692 0.0010 -0.0624 663 MET A CE 5064 C CE B MET A 670 ? 0.2899 0.2870 0.0529 0.1672 -0.0778 -0.0220 663 MET A CE 5065 N N . MET A 671 ? 0.3783 0.2758 0.2108 0.1158 -0.0745 -0.0493 664 MET A N 5066 C CA . MET A 671 ? 0.3700 0.2722 0.2153 0.1094 -0.0846 -0.0556 664 MET A CA 5067 C C . MET A 671 ? 0.3675 0.2660 0.2043 0.0979 -0.0806 -0.0580 664 MET A C 5068 O O . MET A 671 ? 0.3873 0.2486 0.2071 0.0848 -0.0959 -0.0587 664 MET A O 5069 C CB A MET A 671 ? 0.3760 0.2829 0.2233 0.1076 -0.0810 -0.0691 664 MET A CB 5070 C CB B MET A 671 ? 0.3681 0.2741 0.2135 0.1049 -0.0850 -0.0684 664 MET A CB 5071 C CG A MET A 671 ? 0.3867 0.2939 0.2459 0.1088 -0.0809 -0.0619 664 MET A CG 5072 C CG B MET A 671 ? 0.3368 0.2539 0.2064 0.0997 -0.1178 -0.0533 664 MET A CG 5073 S SD A MET A 671 ? 0.4284 0.3103 0.3078 0.1149 -0.0807 -0.0363 664 MET A SD 5074 S SD B MET A 671 ? 0.3304 0.2900 0.1959 0.0834 -0.1378 -0.0758 664 MET A SD 5075 C CE A MET A 671 ? 0.4130 0.3120 0.2635 0.1130 -0.0863 -0.0316 664 MET A CE 5076 C CE B MET A 671 ? 0.3137 0.2825 0.1812 0.0704 -0.1514 -0.0638 664 MET A CE 5077 N N . ASN A 672 ? 0.3542 0.2572 0.2150 0.0910 -0.0782 -0.0529 665 ASN A N 5078 C CA . ASN A 672 ? 0.3566 0.2562 0.1985 0.0907 -0.0618 -0.0433 665 ASN A CA 5079 C C . ASN A 672 ? 0.3304 0.2488 0.1944 0.0918 -0.0552 -0.0320 665 ASN A C 5080 O O . ASN A 672 ? 0.3570 0.2624 0.1800 0.0773 -0.0682 -0.0307 665 ASN A O 5081 C CB . ASN A 672 ? 0.3522 0.2508 0.2049 0.1063 -0.0774 -0.0297 665 ASN A CB 5082 C CG . ASN A 672 ? 0.3915 0.2749 0.2222 0.0894 -0.0692 -0.0406 665 ASN A CG 5083 O OD1 . ASN A 672 ? 0.3655 0.3007 0.2482 0.1267 -0.1077 -0.0334 665 ASN A OD1 5084 N ND2 . ASN A 672 ? 0.3944 0.2585 0.1351 0.1016 -0.0454 -0.0950 665 ASN A ND2 5085 N N . ASP A 673 ? 0.3358 0.2334 0.2054 0.0840 -0.0565 -0.0247 666 ASP A N 5086 C CA . ASP A 673 ? 0.3086 0.2335 0.1744 0.0703 -0.0506 -0.0274 666 ASP A CA 5087 C C . ASP A 673 ? 0.2960 0.2407 0.1715 0.0697 -0.0451 -0.0371 666 ASP A C 5088 O O . ASP A 673 ? 0.2883 0.2530 0.1539 0.0440 -0.0752 -0.0194 666 ASP A O 5089 C CB . ASP A 673 ? 0.3051 0.2358 0.1767 0.0700 -0.0479 -0.0240 666 ASP A CB 5090 C CG . ASP A 673 ? 0.3292 0.2544 0.1972 0.0692 -0.0454 -0.0302 666 ASP A CG 5091 O OD1 . ASP A 673 ? 0.3533 0.2452 0.1893 0.0737 -0.0421 0.0124 666 ASP A OD1 5092 O OD2 . ASP A 673 ? 0.3734 0.2646 0.2133 0.0738 -0.0746 -0.0347 666 ASP A OD2 5093 N N . GLN A 674 ? 0.2816 0.2171 0.1765 0.0661 -0.0543 -0.0310 667 GLN A N 5094 C CA . GLN A 674 ? 0.2934 0.2134 0.1882 0.0688 -0.0564 -0.0389 667 GLN A CA 5095 C C . GLN A 674 ? 0.2989 0.2104 0.2020 0.0646 -0.0620 -0.0416 667 GLN A C 5096 O O . GLN A 674 ? 0.3026 0.2211 0.2104 0.0502 -0.0483 -0.0481 667 GLN A O 5097 C CB . GLN A 674 ? 0.2969 0.1759 0.1725 0.0871 -0.0558 -0.0385 667 GLN A CB 5098 C CG . GLN A 674 ? 0.2920 0.2036 0.1835 0.0826 -0.0573 -0.0276 667 GLN A CG 5099 C CD . GLN A 674 ? 0.3206 0.2242 0.1790 0.0914 -0.0449 -0.0244 667 GLN A CD 5100 O OE1 . GLN A 674 ? 0.3412 0.2493 0.1574 0.0563 -0.0319 -0.0047 667 GLN A OE1 5101 N NE2 . GLN A 674 ? 0.2579 0.2360 0.1225 0.0726 -0.0211 0.0010 667 GLN A NE2 5102 N N . LEU A 675 ? 0.2873 0.2193 0.2250 0.0614 -0.0768 -0.0398 668 LEU A N 5103 C CA . LEU A 675 ? 0.2973 0.2294 0.2198 0.0689 -0.0773 -0.0458 668 LEU A CA 5104 C C . LEU A 675 ? 0.2986 0.2506 0.2051 0.0666 -0.0729 -0.0356 668 LEU A C 5105 O O . LEU A 675 ? 0.2938 0.2367 0.2386 0.0706 -0.0650 -0.0451 668 LEU A O 5106 C CB . LEU A 675 ? 0.2994 0.2572 0.2295 0.0716 -0.1034 -0.0501 668 LEU A CB 5107 C CG . LEU A 675 ? 0.3293 0.2508 0.2427 0.0811 -0.1052 -0.0644 668 LEU A CG 5108 C CD1 . LEU A 675 ? 0.3845 0.3131 0.2018 0.0686 -0.1457 -0.0666 668 LEU A CD1 5109 C CD2 . LEU A 675 ? 0.3294 0.2804 0.2935 0.0249 -0.1050 -0.0904 668 LEU A CD2 5110 N N . MET A 676 ? 0.2947 0.2410 0.1883 0.0666 -0.0760 -0.0234 669 MET A N 5111 C CA . MET A 676 ? 0.3064 0.2386 0.2011 0.0601 -0.0607 -0.0241 669 MET A CA 5112 C C . MET A 676 ? 0.3082 0.2369 0.1859 0.0617 -0.0452 -0.0251 669 MET A C 5113 O O . MET A 676 ? 0.3290 0.2376 0.2052 0.0581 -0.0518 -0.0199 669 MET A O 5114 C CB . MET A 676 ? 0.3095 0.2399 0.1914 0.0589 -0.0468 -0.0269 669 MET A CB 5115 C CG . MET A 676 ? 0.3331 0.2685 0.2663 0.0474 -0.0397 -0.0329 669 MET A CG 5116 S SD . MET A 676 ? 0.3747 0.2887 0.2465 0.0706 0.0324 -0.0036 669 MET A SD 5117 C CE . MET A 676 ? 0.3379 0.2737 0.1854 0.0703 -0.0491 0.0511 669 MET A CE 5118 N N . PHE A 677 ? 0.2828 0.2222 0.1783 0.0654 -0.0452 -0.0195 670 PHE A N 5119 C CA . PHE A 677 ? 0.2591 0.2275 0.1984 0.0562 -0.0328 -0.0214 670 PHE A CA 5120 C C . PHE A 677 ? 0.2450 0.2239 0.1939 0.0543 -0.0318 -0.0272 670 PHE A C 5121 O O . PHE A 677 ? 0.2561 0.2423 0.2092 0.0344 -0.0272 -0.0272 670 PHE A O 5122 C CB . PHE A 677 ? 0.2395 0.1949 0.1803 0.0597 -0.0123 -0.0410 670 PHE A CB 5123 C CG . PHE A 677 ? 0.2616 0.2302 0.2016 0.0527 -0.0186 -0.0330 670 PHE A CG 5124 C CD1 . PHE A 677 ? 0.2611 0.2189 0.1774 0.0275 -0.0107 -0.0017 670 PHE A CD1 5125 C CD2 . PHE A 677 ? 0.2514 0.2228 0.2092 0.0194 0.0034 -0.0239 670 PHE A CD2 5126 C CE1 . PHE A 677 ? 0.1982 0.2619 0.1928 0.0420 -0.0130 -0.0091 670 PHE A CE1 5127 C CE2 . PHE A 677 ? 0.2568 0.2189 0.1945 0.0203 0.0108 -0.0270 670 PHE A CE2 5128 C CZ . PHE A 677 ? 0.2077 0.2480 0.1158 0.0231 -0.0119 -0.0275 670 PHE A CZ 5129 N N . LEU A 678 ? 0.2454 0.2223 0.2049 0.0431 -0.0343 -0.0322 671 LEU A N 5130 C CA . LEU A 678 ? 0.2192 0.2316 0.2021 0.0387 -0.0438 -0.0327 671 LEU A CA 5131 C C . LEU A 678 ? 0.2170 0.2166 0.1992 0.0362 -0.0423 -0.0285 671 LEU A C 5132 O O . LEU A 678 ? 0.1838 0.1972 0.2063 0.0374 -0.0362 -0.0152 671 LEU A O 5133 C CB . LEU A 678 ? 0.2177 0.2360 0.2014 0.0496 -0.0550 -0.0210 671 LEU A CB 5134 C CG . LEU A 678 ? 0.2343 0.2405 0.2470 0.0354 -0.1013 0.0017 671 LEU A CG 5135 C CD1 . LEU A 678 ? 0.2857 0.2019 0.3156 0.0628 -0.0562 -0.0311 671 LEU A CD1 5136 C CD2 . LEU A 678 ? 0.2715 0.2540 0.2626 0.0171 -0.0882 -0.0360 671 LEU A CD2 5137 N N . GLU A 679 ? 0.2154 0.2076 0.1982 0.0357 -0.0423 -0.0327 672 GLU A N 5138 C CA . GLU A 679 ? 0.2084 0.2138 0.1990 0.0372 -0.0164 -0.0310 672 GLU A CA 5139 C C . GLU A 679 ? 0.2009 0.2187 0.1937 0.0298 -0.0220 -0.0226 672 GLU A C 5140 O O . GLU A 679 ? 0.1877 0.2282 0.2098 0.0118 -0.0233 -0.0087 672 GLU A O 5141 C CB . GLU A 679 ? 0.1970 0.1888 0.2070 0.0382 -0.0170 -0.0296 672 GLU A CB 5142 C CG . GLU A 679 ? 0.1816 0.1981 0.2333 0.0176 0.0144 -0.0433 672 GLU A CG 5143 C CD . GLU A 679 ? 0.2101 0.2495 0.2564 -0.0087 -0.0183 -0.0118 672 GLU A CD 5144 O OE1 . GLU A 679 ? 0.2223 0.1925 0.2741 0.0158 0.0151 0.0087 672 GLU A OE1 5145 O OE2 . GLU A 679 ? 0.2219 0.2218 0.2413 0.0259 0.0123 -0.0180 672 GLU A OE2 5146 N N . ARG A 680 ? 0.2009 0.2037 0.1999 0.0194 -0.0208 -0.0118 673 ARG A N 5147 C CA . ARG A 680 ? 0.1937 0.1968 0.2005 0.0151 -0.0216 0.0041 673 ARG A CA 5148 C C . ARG A 680 ? 0.2053 0.1994 0.1871 0.0068 -0.0166 -0.0072 673 ARG A C 5149 O O . ARG A 680 ? 0.1950 0.1849 0.1798 -0.0104 -0.0201 0.0016 673 ARG A O 5150 C CB . ARG A 680 ? 0.2023 0.1963 0.1921 0.0190 -0.0200 0.0003 673 ARG A CB 5151 C CG . ARG A 680 ? 0.1695 0.1657 0.1977 -0.0117 -0.0263 0.0098 673 ARG A CG 5152 C CD . ARG A 680 ? 0.1559 0.1761 0.1687 0.0500 0.0220 0.0124 673 ARG A CD 5153 N NE . ARG A 680 ? 0.2195 0.1644 0.1272 0.0280 -0.0333 -0.0285 673 ARG A NE 5154 C CZ . ARG A 680 ? 0.2361 0.2076 0.1667 0.0541 0.0074 -0.0175 673 ARG A CZ 5155 N NH1 . ARG A 680 ? 0.2011 0.1529 0.1940 0.0540 0.0322 -0.0225 673 ARG A NH1 5156 N NH2 . ARG A 680 ? 0.2592 0.2244 0.1332 0.0443 0.0118 -0.0615 673 ARG A NH2 5157 N N . ALA A 681 ? 0.2098 0.1857 0.1877 0.0139 -0.0088 -0.0201 674 ALA A N 5158 C CA . ALA A 681 ? 0.2170 0.1827 0.1780 0.0274 -0.0116 -0.0212 674 ALA A CA 5159 C C . ALA A 681 ? 0.2127 0.1965 0.1903 0.0263 -0.0146 -0.0202 674 ALA A C 5160 O O . ALA A 681 ? 0.2188 0.2105 0.1982 0.0428 0.0000 -0.0096 674 ALA A O 5161 C CB . ALA A 681 ? 0.2042 0.1691 0.1591 0.0112 -0.0203 -0.0283 674 ALA A CB 5162 N N . PHE A 682 ? 0.2197 0.2010 0.1945 0.0172 -0.0207 -0.0344 675 PHE A N 5163 C CA . PHE A 682 ? 0.2213 0.2119 0.2208 0.0207 -0.0181 -0.0284 675 PHE A CA 5164 C C . PHE A 682 ? 0.2230 0.2236 0.2119 0.0213 -0.0244 -0.0134 675 PHE A C 5165 O O . PHE A 682 ? 0.2435 0.2261 0.2489 0.0092 -0.0118 -0.0027 675 PHE A O 5166 C CB . PHE A 682 ? 0.2186 0.2325 0.2297 0.0185 -0.0291 -0.0246 675 PHE A CB 5167 C CG . PHE A 682 ? 0.2232 0.2151 0.2042 0.0260 -0.0205 -0.0453 675 PHE A CG 5168 C CD1 . PHE A 682 ? 0.1926 0.1802 0.2032 0.0427 0.0086 -0.0724 675 PHE A CD1 5169 C CD2 . PHE A 682 ? 0.2424 0.2388 0.2094 0.0192 -0.0334 -0.0292 675 PHE A CD2 5170 C CE1 . PHE A 682 ? 0.1834 0.2396 0.2000 0.0505 -0.0087 -0.0558 675 PHE A CE1 5171 C CE2 . PHE A 682 ? 0.2324 0.2398 0.2755 0.0253 -0.0370 -0.0423 675 PHE A CE2 5172 C CZ . PHE A 682 ? 0.1791 0.2174 0.2455 0.0451 -0.0235 -0.0295 675 PHE A CZ 5173 N N . ILE A 683 ? 0.2129 0.2038 0.2039 0.0082 -0.0246 -0.0038 676 ILE A N 5174 C CA . ILE A 683 ? 0.2091 0.2004 0.1890 0.0166 -0.0312 0.0045 676 ILE A CA 5175 C C . ILE A 683 ? 0.2220 0.2261 0.2077 0.0180 -0.0171 -0.0043 676 ILE A C 5176 O O . ILE A 683 ? 0.2596 0.2381 0.2231 0.0197 -0.0167 -0.0100 676 ILE A O 5177 C CB . ILE A 683 ? 0.1751 0.1881 0.1929 0.0112 -0.0341 -0.0006 676 ILE A CB 5178 C CG1 . ILE A 683 ? 0.1822 0.1844 0.1816 0.0174 -0.0229 -0.0108 676 ILE A CG1 5179 C CG2 . ILE A 683 ? 0.1847 0.1954 0.1643 -0.0029 -0.0224 -0.0148 676 ILE A CG2 5180 C CD1 . ILE A 683 ? 0.1643 0.1737 0.1209 0.0089 0.0041 0.0103 676 ILE A CD1 5181 N N . ASP A 684 ? 0.2059 0.2225 0.1726 0.0123 -0.0230 0.0027 677 ASP A N 5182 C CA . ASP A 684 ? 0.2236 0.2228 0.1900 0.0126 -0.0074 0.0003 677 ASP A CA 5183 C C . ASP A 684 ? 0.2075 0.2394 0.1808 0.0126 -0.0111 -0.0019 677 ASP A C 5184 O O . ASP A 684 ? 0.2179 0.2435 0.2065 -0.0016 -0.0044 0.0111 677 ASP A O 5185 C CB . ASP A 684 ? 0.1853 0.2221 0.1661 0.0084 -0.0021 0.0047 677 ASP A CB 5186 C CG . ASP A 684 ? 0.2185 0.2168 0.1850 0.0040 0.0045 0.0042 677 ASP A CG 5187 O OD1 . ASP A 684 ? 0.2329 0.2422 0.1697 0.0213 -0.0289 -0.0069 677 ASP A OD1 5188 O OD2 . ASP A 684 ? 0.2193 0.2317 0.2544 -0.0133 0.0000 0.0061 677 ASP A OD2 5189 N N . PRO A 685 ? 0.2296 0.2585 0.1928 0.0225 -0.0156 -0.0084 678 PRO A N 5190 C CA . PRO A 685 ? 0.2404 0.2747 0.2203 0.0061 -0.0070 -0.0055 678 PRO A CA 5191 C C . PRO A 685 ? 0.2607 0.2747 0.2475 -0.0014 -0.0109 0.0030 678 PRO A C 5192 O O . PRO A 685 ? 0.3073 0.3292 0.3106 -0.0406 -0.0215 0.0217 678 PRO A O 5193 C CB . PRO A 685 ? 0.2402 0.2719 0.2305 0.0148 -0.0004 -0.0037 678 PRO A CB 5194 C CG . PRO A 685 ? 0.2004 0.2753 0.1967 0.0194 -0.0026 -0.0219 678 PRO A CG 5195 C CD . PRO A 685 ? 0.2150 0.2616 0.1845 0.0308 -0.0203 -0.0223 678 PRO A CD 5196 N N . LEU A 686 ? 0.2406 0.2536 0.2396 0.0136 -0.0029 0.0201 679 LEU A N 5197 C CA . LEU A 686 ? 0.2256 0.2315 0.2261 0.0180 -0.0132 0.0107 679 LEU A CA 5198 C C . LEU A 686 ? 0.2381 0.2402 0.2243 0.0129 -0.0158 0.0025 679 LEU A C 5199 O O . LEU A 686 ? 0.2425 0.2593 0.2279 0.0164 -0.0178 0.0220 679 LEU A O 5200 C CB . LEU A 686 ? 0.2111 0.2270 0.2231 0.0153 -0.0163 0.0309 679 LEU A CB 5201 C CG . LEU A 686 ? 0.2275 0.2019 0.2463 0.0075 0.0018 -0.0063 679 LEU A CG 5202 C CD1 . LEU A 686 ? 0.1838 0.1872 0.1839 0.0073 0.0233 0.0019 679 LEU A CD1 5203 C CD2 . LEU A 686 ? 0.2051 0.2606 0.2624 -0.0107 0.0281 -0.0135 679 LEU A CD2 5204 N N . GLY A 687 ? 0.2347 0.2301 0.2384 0.0135 -0.0113 0.0058 680 GLY A N 5205 C CA . GLY A 687 ? 0.2116 0.2349 0.2378 0.0133 -0.0033 0.0082 680 GLY A CA 5206 C C . GLY A 687 ? 0.2420 0.2429 0.2548 0.0086 -0.0082 0.0045 680 GLY A C 5207 O O . GLY A 687 ? 0.2599 0.2237 0.2688 0.0021 -0.0216 0.0026 680 GLY A O 5208 N N . LEU A 688 ? 0.2116 0.2452 0.2453 0.0114 0.0125 -0.0019 681 LEU A N 5209 C CA . LEU A 688 ? 0.2235 0.2452 0.2593 0.0024 0.0074 0.0150 681 LEU A CA 5210 C C . LEU A 688 ? 0.2433 0.2481 0.2555 0.0054 0.0166 0.0202 681 LEU A C 5211 O O . LEU A 688 ? 0.2618 0.2559 0.2749 0.0137 0.0195 0.0210 681 LEU A O 5212 C CB . LEU A 688 ? 0.2356 0.2487 0.2592 0.0070 0.0054 0.0226 681 LEU A CB 5213 C CG . LEU A 688 ? 0.2031 0.2447 0.3124 -0.0019 -0.0227 0.0133 681 LEU A CG 5214 C CD1 . LEU A 688 ? 0.2445 0.2327 0.2988 -0.0338 -0.0240 0.0748 681 LEU A CD1 5215 C CD2 . LEU A 688 ? 0.1531 0.2576 0.3165 -0.0085 -0.0607 0.0411 681 LEU A CD2 5216 N N . PRO A 689 ? 0.2696 0.2636 0.2553 -0.0073 0.0144 0.0210 682 PRO A N 5217 C CA . PRO A 689 ? 0.2841 0.2739 0.2389 -0.0094 0.0217 0.0204 682 PRO A CA 5218 C C . PRO A 689 ? 0.2909 0.2904 0.2239 -0.0031 0.0225 0.0256 682 PRO A C 5219 O O . PRO A 689 ? 0.2850 0.2758 0.2185 0.0092 0.0382 0.0280 682 PRO A O 5220 C CB . PRO A 689 ? 0.2954 0.2817 0.2392 -0.0239 0.0154 0.0134 682 PRO A CB 5221 C CG . PRO A 689 ? 0.3074 0.2644 0.2623 -0.0264 0.0210 0.0313 682 PRO A CG 5222 C CD . PRO A 689 ? 0.2747 0.2529 0.2470 -0.0166 0.0122 0.0295 682 PRO A CD 5223 N N . ASP A 690 ? 0.3050 0.3093 0.2211 0.0031 0.0217 0.0269 683 ASP A N 5224 C CA . ASP A 690 ? 0.3074 0.3156 0.2197 0.0099 0.0150 0.0282 683 ASP A CA 5225 C C . ASP A 690 ? 0.2789 0.2955 0.1911 0.0132 0.0089 0.0218 683 ASP A C 5226 O O . ASP A 690 ? 0.2628 0.2924 0.1576 0.0377 -0.0126 0.0086 683 ASP A O 5227 C CB . ASP A 690 ? 0.3436 0.3570 0.2355 0.0098 0.0178 0.0512 683 ASP A CB 5228 C CG . ASP A 690 ? 0.3830 0.4230 0.3092 0.0041 0.0118 0.0874 683 ASP A CG 5229 O OD1 . ASP A 690 ? 0.4012 0.4808 0.3521 0.0153 -0.0550 0.1287 683 ASP A OD1 5230 O OD2 . ASP A 690 ? 0.4930 0.4857 0.3994 -0.0574 0.0457 0.1113 683 ASP A OD2 5231 N N . ARG A 691 ? 0.2452 0.2792 0.1928 0.0093 -0.0092 0.0081 684 ARG A N 5232 C CA . ARG A 691 ? 0.2235 0.2627 0.1783 0.0042 0.0084 0.0000 684 ARG A CA 5233 C C . ARG A 691 ? 0.2034 0.2307 0.1852 0.0037 0.0069 -0.0032 684 ARG A C 5234 O O . ARG A 691 ? 0.2013 0.2191 0.1510 -0.0006 0.0315 -0.0175 684 ARG A O 5235 C CB . ARG A 691 ? 0.2127 0.2799 0.1909 0.0075 0.0101 0.0019 684 ARG A CB 5236 C CG . ARG A 691 ? 0.2048 0.2757 0.2040 -0.0007 0.0180 -0.0218 684 ARG A CG 5237 C CD . ARG A 691 ? 0.1807 0.2630 0.2215 -0.0216 0.0207 -0.0323 684 ARG A CD 5238 N NE . ARG A 691 ? 0.2007 0.2745 0.2380 -0.0256 0.0250 -0.0354 684 ARG A NE 5239 C CZ . ARG A 691 ? 0.2241 0.2591 0.2518 -0.0107 0.0152 -0.0398 684 ARG A CZ 5240 N NH1 . ARG A 691 ? 0.1793 0.2242 0.2172 -0.0016 0.0627 0.0021 684 ARG A NH1 5241 N NH2 . ARG A 691 ? 0.2303 0.2367 0.2292 -0.0341 0.0509 -0.0433 684 ARG A NH2 5242 N N . PRO A 692 ? 0.1937 0.2281 0.1930 0.0040 -0.0014 -0.0078 685 PRO A N 5243 C CA . PRO A 692 ? 0.1912 0.2330 0.1777 0.0000 -0.0033 -0.0107 685 PRO A CA 5244 C C . PRO A 692 ? 0.1974 0.2368 0.1897 -0.0002 -0.0151 -0.0168 685 PRO A C 5245 O O . PRO A 692 ? 0.1812 0.2572 0.1843 -0.0042 -0.0065 -0.0071 685 PRO A O 5246 C CB . PRO A 692 ? 0.2026 0.2554 0.2057 -0.0055 -0.0069 -0.0294 685 PRO A CB 5247 C CG . PRO A 692 ? 0.2158 0.2754 0.2140 -0.0119 0.0117 -0.0274 685 PRO A CG 5248 C CD . PRO A 692 ? 0.1910 0.2335 0.1906 -0.0026 0.0092 -0.0268 685 PRO A CD 5249 N N . PHE A 693 ? 0.1968 0.2179 0.1852 0.0094 -0.0130 -0.0015 686 PHE A N 5250 C CA . PHE A 693 ? 0.2008 0.2182 0.1957 -0.0081 -0.0120 -0.0080 686 PHE A CA 5251 C C . PHE A 693 ? 0.1885 0.2094 0.1895 0.0037 -0.0053 -0.0095 686 PHE A C 5252 O O . PHE A 693 ? 0.1906 0.2113 0.1970 -0.0016 -0.0129 0.0008 686 PHE A O 5253 C CB . PHE A 693 ? 0.1984 0.2071 0.1936 -0.0125 -0.0114 -0.0017 686 PHE A CB 5254 C CG . PHE A 693 ? 0.2014 0.2478 0.2133 -0.0172 -0.0131 -0.0313 686 PHE A CG 5255 C CD1 . PHE A 693 ? 0.1627 0.2271 0.1882 -0.0046 -0.0095 -0.0139 686 PHE A CD1 5256 C CD2 . PHE A 693 ? 0.1979 0.2220 0.2018 -0.0203 -0.0253 -0.0411 686 PHE A CD2 5257 C CE1 . PHE A 693 ? 0.1632 0.2060 0.1676 -0.0291 -0.0317 -0.0347 686 PHE A CE1 5258 C CE2 . PHE A 693 ? 0.1729 0.1911 0.2340 -0.0246 -0.0068 -0.0490 686 PHE A CE2 5259 C CZ . PHE A 693 ? 0.1736 0.1946 0.2168 -0.0396 -0.0020 -0.0783 686 PHE A CZ 5260 N N . TYR A 694 ? 0.1727 0.1975 0.1873 0.0117 0.0107 -0.0213 687 TYR A N 5261 C CA . TYR A 694 ? 0.1778 0.1903 0.1906 0.0087 0.0058 -0.0284 687 TYR A CA 5262 C C . TYR A 694 ? 0.1705 0.2159 0.1881 0.0067 0.0008 -0.0289 687 TYR A C 5263 O O . TYR A 694 ? 0.1997 0.2166 0.1893 0.0118 -0.0006 -0.0294 687 TYR A O 5264 C CB . TYR A 694 ? 0.1761 0.1947 0.1944 0.0201 0.0053 -0.0392 687 TYR A CB 5265 C CG . TYR A 694 ? 0.1938 0.1965 0.2007 0.0127 0.0009 -0.0420 687 TYR A CG 5266 C CD1 . TYR A 694 ? 0.2110 0.1972 0.1689 0.0516 -0.0098 -0.0320 687 TYR A CD1 5267 C CD2 . TYR A 694 ? 0.1790 0.2070 0.1624 0.0012 -0.0161 -0.0663 687 TYR A CD2 5268 C CE1 . TYR A 694 ? 0.2004 0.1949 0.1842 0.0143 -0.0223 -0.0348 687 TYR A CE1 5269 C CE2 . TYR A 694 ? 0.2447 0.2086 0.2135 -0.0132 -0.0265 -0.0246 687 TYR A CE2 5270 C CZ . TYR A 694 ? 0.2297 0.1847 0.1999 -0.0019 -0.0275 -0.0533 687 TYR A CZ 5271 O OH . TYR A 694 ? 0.1550 0.2315 0.1510 0.0434 0.0147 -0.0761 687 TYR A OH 5272 N N . ARG A 695 ? 0.1699 0.2227 0.1940 -0.0013 -0.0031 -0.0273 688 ARG A N 5273 C CA . ARG A 695 ? 0.1695 0.1958 0.1902 -0.0002 -0.0108 -0.0210 688 ARG A CA 5274 C C . ARG A 695 ? 0.1864 0.1869 0.1898 -0.0010 -0.0093 -0.0088 688 ARG A C 5275 O O . ARG A 695 ? 0.2209 0.1738 0.1709 0.0036 -0.0181 -0.0041 688 ARG A O 5276 C CB . ARG A 695 ? 0.1691 0.2084 0.1801 -0.0116 -0.0022 -0.0102 688 ARG A CB 5277 C CG . ARG A 695 ? 0.1721 0.2092 0.1761 -0.0140 -0.0157 -0.0299 688 ARG A CG 5278 C CD . ARG A 695 ? 0.2170 0.2962 0.2591 0.0533 0.0099 0.0272 688 ARG A CD 5279 N NE . ARG A 695 ? 0.2858 0.3152 0.2713 -0.0256 0.0277 -0.0275 688 ARG A NE 5280 C CZ . ARG A 695 ? 0.2889 0.3332 0.3062 0.0003 0.0234 0.0148 688 ARG A CZ 5281 N NH1 . ARG A 695 ? 0.2671 0.2579 0.2153 -0.0443 -0.0024 0.0118 688 ARG A NH1 5282 N NH2 . ARG A 695 ? 0.2006 0.2729 0.3551 0.0004 0.0660 0.0204 688 ARG A NH2 5283 N N . HIS A 696 ? 0.1692 0.1895 0.1987 -0.0055 -0.0151 -0.0064 689 HIS A N 5284 C CA . HIS A 696 ? 0.1866 0.1700 0.1696 -0.0061 -0.0177 -0.0223 689 HIS A CA 5285 C C . HIS A 696 ? 0.1981 0.1862 0.1829 -0.0062 -0.0071 -0.0206 689 HIS A C 5286 O O . HIS A 696 ? 0.2138 0.2200 0.2055 -0.0179 0.0113 -0.0178 689 HIS A O 5287 C CB . HIS A 696 ? 0.1880 0.1553 0.1747 0.0074 -0.0292 -0.0299 689 HIS A CB 5288 C CG . HIS A 696 ? 0.2076 0.1887 0.1554 0.0081 -0.0260 -0.0229 689 HIS A CG 5289 N ND1 . HIS A 696 ? 0.1844 0.2002 0.1543 -0.0030 -0.0217 -0.0299 689 HIS A ND1 5290 C CD2 . HIS A 696 ? 0.2187 0.1895 0.1900 0.0057 -0.0360 0.0109 689 HIS A CD2 5291 C CE1 . HIS A 696 ? 0.2242 0.2004 0.1563 0.0305 -0.0294 -0.0147 689 HIS A CE1 5292 N NE2 . HIS A 696 ? 0.2252 0.2065 0.1712 0.0060 -0.0107 -0.0241 689 HIS A NE2 5293 N N . VAL A 697 ? 0.1969 0.1757 0.2035 -0.0111 -0.0074 -0.0078 690 VAL A N 5294 C CA . VAL A 697 ? 0.1866 0.1860 0.2127 0.0011 -0.0106 -0.0081 690 VAL A CA 5295 C C . VAL A 697 ? 0.1934 0.1997 0.2138 0.0010 -0.0140 -0.0174 690 VAL A C 5296 O O . VAL A 697 ? 0.2068 0.2359 0.2197 0.0137 -0.0060 -0.0259 690 VAL A O 5297 C CB . VAL A 697 ? 0.1755 0.1723 0.2236 -0.0052 -0.0105 0.0000 690 VAL A CB 5298 C CG1 . VAL A 697 ? 0.1578 0.1522 0.1900 -0.0341 -0.0222 -0.0033 690 VAL A CG1 5299 C CG2 . VAL A 697 ? 0.1612 0.2086 0.1703 0.0060 -0.0320 -0.0087 690 VAL A CG2 5300 N N . ILE A 698 ? 0.2001 0.1926 0.2179 0.0155 -0.0282 -0.0247 691 ILE A N 5301 C CA . ILE A 698 ? 0.1848 0.2010 0.2140 0.0028 -0.0254 -0.0347 691 ILE A CA 5302 C C . ILE A 698 ? 0.1970 0.2223 0.2190 0.0013 -0.0233 -0.0311 691 ILE A C 5303 O O . ILE A 698 ? 0.1931 0.2298 0.2145 -0.0060 -0.0310 -0.0410 691 ILE A O 5304 C CB . ILE A 698 ? 0.1757 0.2114 0.2069 0.0023 -0.0205 -0.0331 691 ILE A CB 5305 C CG1 . ILE A 698 ? 0.1880 0.1774 0.2110 0.0116 -0.0100 -0.0352 691 ILE A CG1 5306 C CG2 . ILE A 698 ? 0.1668 0.1991 0.2187 0.0278 -0.0346 -0.0272 691 ILE A CG2 5307 C CD1 . ILE A 698 ? 0.1466 0.1892 0.2055 -0.0020 0.0196 -0.0406 691 ILE A CD1 5308 N N . TYR A 699 ? 0.2125 0.2101 0.2257 0.0090 -0.0360 -0.0171 692 TYR A N 5309 C CA . TYR A 699 ? 0.2186 0.2309 0.2310 0.0209 -0.0143 -0.0184 692 TYR A CA 5310 C C . TYR A 699 ? 0.2271 0.2372 0.2293 0.0163 -0.0126 -0.0149 692 TYR A C 5311 O O . TYR A 699 ? 0.2438 0.2693 0.2602 0.0304 -0.0220 -0.0190 692 TYR A O 5312 C CB . TYR A 699 ? 0.2105 0.2279 0.2277 0.0262 -0.0269 -0.0085 692 TYR A CB 5313 C CG . TYR A 699 ? 0.2411 0.2598 0.2599 0.0251 -0.0241 -0.0105 692 TYR A CG 5314 C CD1 . TYR A 699 ? 0.2352 0.2435 0.2617 0.0098 -0.0299 0.0047 692 TYR A CD1 5315 C CD2 . TYR A 699 ? 0.2080 0.1915 0.2362 0.0244 -0.0350 0.0083 692 TYR A CD2 5316 C CE1 . TYR A 699 ? 0.2816 0.2230 0.2679 0.0077 -0.0274 0.0092 692 TYR A CE1 5317 C CE2 . TYR A 699 ? 0.2404 0.2279 0.2335 0.0113 -0.0448 0.0012 692 TYR A CE2 5318 C CZ . TYR A 699 ? 0.2622 0.2420 0.2669 -0.0154 -0.0260 -0.0122 692 TYR A CZ 5319 O OH . TYR A 699 ? 0.2142 0.2654 0.2760 -0.0462 -0.0218 -0.0228 692 TYR A OH 5320 N N . ALA A 700 ? 0.2284 0.2040 0.2299 0.0187 -0.0107 -0.0153 693 ALA A N 5321 C CA . ALA A 700 ? 0.1971 0.2023 0.2218 0.0080 -0.0077 -0.0089 693 ALA A CA 5322 C C . ALA A 700 ? 0.2002 0.2067 0.2269 -0.0002 0.0005 -0.0135 693 ALA A C 5323 O O . ALA A 700 ? 0.2076 0.2185 0.2481 0.0148 0.0047 -0.0112 693 ALA A O 5324 C CB . ALA A 700 ? 0.1927 0.1895 0.2145 -0.0023 -0.0025 -0.0038 693 ALA A CB 5325 N N . PRO A 701 ? 0.1937 0.1996 0.2195 -0.0078 0.0131 -0.0096 694 PRO A N 5326 C CA . PRO A 701 ? 0.2012 0.2131 0.2187 -0.0046 0.0221 -0.0166 694 PRO A CA 5327 C C . PRO A 701 ? 0.2125 0.2252 0.2392 -0.0023 0.0246 -0.0150 694 PRO A C 5328 O O . PRO A 701 ? 0.2280 0.2565 0.2403 0.0143 0.0133 -0.0291 694 PRO A O 5329 C CB . PRO A 701 ? 0.1612 0.1905 0.2140 -0.0191 0.0294 -0.0187 694 PRO A CB 5330 C CG . PRO A 701 ? 0.1739 0.1825 0.2210 0.0099 0.0254 -0.0258 694 PRO A CG 5331 C CD . PRO A 701 ? 0.1875 0.1846 0.2068 -0.0228 0.0049 -0.0045 694 PRO A CD 5332 N N . SER A 702 ? 0.2031 0.2315 0.2405 0.0078 0.0364 -0.0290 695 SER A N 5333 C CA . SER A 702 ? 0.2061 0.2490 0.2570 0.0053 0.0412 -0.0233 695 SER A CA 5334 C C . SER A 702 ? 0.2360 0.2560 0.2673 0.0066 0.0439 -0.0184 695 SER A C 5335 O O . SER A 702 ? 0.2319 0.2622 0.2798 0.0049 0.0444 -0.0161 695 SER A O 5336 C CB . SER A 702 ? 0.2140 0.2530 0.2597 0.0012 0.0527 -0.0187 695 SER A CB 5337 O OG . SER A 702 ? 0.1815 0.2784 0.2731 0.0024 0.0737 -0.0621 695 SER A OG 5338 N N . SER A 703 ? 0.2522 0.2678 0.2710 0.0054 0.0420 -0.0198 696 SER A N 5339 C CA . SER A 703 ? 0.2480 0.2661 0.2641 0.0091 0.0418 -0.0127 696 SER A CA 5340 C C . SER A 703 ? 0.2551 0.2740 0.2669 -0.0025 0.0499 -0.0109 696 SER A C 5341 O O . SER A 703 ? 0.2567 0.2684 0.2656 -0.0084 0.0459 -0.0141 696 SER A O 5342 C CB . SER A 703 ? 0.2525 0.2546 0.2849 -0.0039 0.0522 -0.0038 696 SER A CB 5343 O OG A SER A 703 ? 0.2111 0.1619 0.1955 0.0180 0.0333 -0.0318 696 SER A OG 5344 O OG B SER A 703 ? 0.2776 0.3323 0.3211 0.0038 0.0542 0.0097 696 SER A OG 5345 N N . HIS A 704 ? 0.2303 0.2673 0.2566 0.0080 0.0444 -0.0078 697 HIS A N 5346 C CA . HIS A 704 ? 0.2594 0.2749 0.2678 -0.0031 0.0533 -0.0107 697 HIS A CA 5347 C C . HIS A 704 ? 0.2626 0.2761 0.2781 0.0030 0.0542 -0.0113 697 HIS A C 5348 O O . HIS A 704 ? 0.2962 0.2846 0.3029 0.0181 0.0575 -0.0097 697 HIS A O 5349 C CB . HIS A 704 ? 0.2495 0.2684 0.2759 -0.0073 0.0759 -0.0078 697 HIS A CB 5350 C CG . HIS A 704 ? 0.2699 0.2934 0.3061 -0.0046 0.0649 -0.0078 697 HIS A CG 5351 N ND1 . HIS A 704 ? 0.3133 0.3026 0.3085 -0.0241 0.1025 -0.0396 697 HIS A ND1 5352 C CD2 . HIS A 704 ? 0.3420 0.2866 0.3236 -0.0180 0.0633 -0.0217 697 HIS A CD2 5353 C CE1 . HIS A 704 ? 0.3438 0.3039 0.3681 -0.0063 0.0799 -0.0443 697 HIS A CE1 5354 N NE2 . HIS A 704 ? 0.3588 0.3107 0.2961 -0.0124 0.0665 -0.0309 697 HIS A NE2 5355 N N . ASN A 705 ? 0.2560 0.2753 0.2504 -0.0005 0.0308 -0.0066 698 ASN A N 5356 C CA . ASN A 705 ? 0.2369 0.2671 0.2650 -0.0097 0.0361 -0.0124 698 ASN A CA 5357 C C . ASN A 705 ? 0.2255 0.2475 0.2495 -0.0129 0.0327 -0.0133 698 ASN A C 5358 O O . ASN A 705 ? 0.2233 0.2264 0.2406 -0.0273 0.0159 -0.0048 698 ASN A O 5359 C CB . ASN A 705 ? 0.2388 0.2747 0.2562 0.0125 0.0369 -0.0242 698 ASN A CB 5360 C CG . ASN A 705 ? 0.2520 0.2727 0.2974 0.0068 0.0298 -0.0294 698 ASN A CG 5361 O OD1 . ASN A 705 ? 0.2306 0.2831 0.3019 0.0211 0.0568 -0.0384 698 ASN A OD1 5362 N ND2 . ASN A 705 ? 0.2213 0.2588 0.2972 0.0117 0.0438 -0.0462 698 ASN A ND2 5363 N N . LYS A 706 ? 0.2136 0.2494 0.2532 -0.0187 0.0459 -0.0107 699 LYS A N 5364 C CA . LYS A 706 ? 0.2077 0.2536 0.2477 -0.0289 0.0346 -0.0251 699 LYS A CA 5365 C C . LYS A 706 ? 0.2075 0.2455 0.2616 -0.0246 0.0340 -0.0307 699 LYS A C 5366 O O . LYS A 706 ? 0.2015 0.2588 0.2537 -0.0258 0.0412 -0.0412 699 LYS A O 5367 C CB . LYS A 706 ? 0.1978 0.2674 0.2619 -0.0406 0.0450 -0.0204 699 LYS A CB 5368 C CG . LYS A 706 ? 0.1901 0.2830 0.2709 -0.0486 0.0350 -0.0352 699 LYS A CG 5369 C CD . LYS A 706 ? 0.1655 0.2732 0.2797 -0.0273 -0.0161 -0.0533 699 LYS A CD 5370 C CE . LYS A 706 ? 0.1735 0.2841 0.2414 -0.0234 0.0080 -0.0600 699 LYS A CE 5371 N NZ . LYS A 706 ? 0.2031 0.2100 0.3029 0.0111 0.0215 -0.0774 699 LYS A NZ 5372 N N . TYR A 707 ? 0.2067 0.2283 0.2690 -0.0090 0.0202 -0.0309 700 TYR A N 5373 C CA . TYR A 707 ? 0.2195 0.2345 0.2787 0.0101 0.0104 -0.0363 700 TYR A CA 5374 C C . TYR A 707 ? 0.2279 0.2452 0.2749 0.0187 0.0186 -0.0381 700 TYR A C 5375 O O . TYR A 707 ? 0.2598 0.2687 0.2644 0.0264 0.0258 -0.0390 700 TYR A O 5376 C CB . TYR A 707 ? 0.2067 0.2282 0.2874 0.0240 0.0243 -0.0486 700 TYR A CB 5377 C CG . TYR A 707 ? 0.2139 0.2349 0.2770 0.0168 -0.0143 -0.0524 700 TYR A CG 5378 C CD1 . TYR A 707 ? 0.2169 0.2359 0.2341 0.0229 -0.0321 -0.0595 700 TYR A CD1 5379 C CD2 . TYR A 707 ? 0.2548 0.2558 0.2645 0.0107 -0.0207 -0.0714 700 TYR A CD2 5380 C CE1 . TYR A 707 ? 0.2654 0.2300 0.2690 0.0273 -0.0228 -0.0440 700 TYR A CE1 5381 C CE2 . TYR A 707 ? 0.2635 0.2761 0.2944 -0.0134 -0.0294 -0.0620 700 TYR A CE2 5382 C CZ . TYR A 707 ? 0.2722 0.2470 0.2911 0.0005 -0.0007 -0.0643 700 TYR A CZ 5383 O OH . TYR A 707 ? 0.2746 0.2347 0.3287 0.0225 0.0028 -0.0860 700 TYR A OH 5384 N N . ALA A 708 ? 0.2112 0.2355 0.2738 0.0136 0.0281 -0.0215 701 ALA A N 5385 C CA . ALA A 708 ? 0.2150 0.2467 0.2778 0.0084 0.0280 -0.0349 701 ALA A CA 5386 C C . ALA A 708 ? 0.2218 0.2565 0.2858 0.0084 0.0311 -0.0302 701 ALA A C 5387 O O . ALA A 708 ? 0.2113 0.2699 0.3041 0.0209 0.0256 -0.0470 701 ALA A O 5388 C CB . ALA A 708 ? 0.2156 0.2629 0.2782 -0.0008 0.0400 -0.0505 701 ALA A CB 5389 N N . GLY A 709 ? 0.2200 0.2321 0.3017 0.0013 0.0282 -0.0268 702 GLY A N 5390 C CA . GLY A 709 ? 0.2176 0.2380 0.3206 -0.0022 0.0336 -0.0134 702 GLY A CA 5391 C C . GLY A 709 ? 0.2120 0.2450 0.3290 -0.0019 0.0252 -0.0116 702 GLY A C 5392 O O . GLY A 709 ? 0.1757 0.2469 0.3444 -0.0073 0.0321 -0.0225 702 GLY A O 5393 N N . GLU A 710 ? 0.2037 0.2289 0.3015 0.0041 0.0201 -0.0103 703 GLU A N 5394 C CA . GLU A 710 ? 0.2021 0.2312 0.2786 -0.0118 0.0201 -0.0184 703 GLU A CA 5395 C C . GLU A 710 ? 0.1939 0.2235 0.2663 -0.0139 0.0112 -0.0231 703 GLU A C 5396 O O . GLU A 710 ? 0.1911 0.2290 0.2660 -0.0240 0.0264 -0.0496 703 GLU A O 5397 C CB . GLU A 710 ? 0.2211 0.2353 0.2760 -0.0121 0.0219 -0.0106 703 GLU A CB 5398 C CG . GLU A 710 ? 0.1916 0.2115 0.3115 -0.0080 0.0583 -0.0131 703 GLU A CG 5399 C CD . GLU A 710 ? 0.2418 0.2449 0.3154 -0.0226 0.0512 -0.0264 703 GLU A CD 5400 O OE1 . GLU A 710 ? 0.2451 0.2367 0.3052 -0.0036 0.0639 -0.0274 703 GLU A OE1 5401 O OE2 . GLU A 710 ? 0.2733 0.2414 0.3851 -0.0072 0.0184 -0.0665 703 GLU A OE2 5402 N N . SER A 711 ? 0.1823 0.2347 0.2379 -0.0183 -0.0039 -0.0226 704 SER A N 5403 C CA . SER A 711 ? 0.1856 0.2207 0.2433 -0.0132 -0.0058 -0.0261 704 SER A CA 5404 C C . SER A 711 ? 0.1836 0.2260 0.2422 -0.0088 -0.0052 -0.0235 704 SER A C 5405 O O . SER A 711 ? 0.2136 0.2236 0.2586 -0.0080 0.0000 -0.0053 704 SER A O 5406 C CB . SER A 711 ? 0.1598 0.2492 0.2584 -0.0206 -0.0154 -0.0261 704 SER A CB 5407 O OG . SER A 711 ? 0.1947 0.2524 0.2687 -0.0181 -0.0011 -0.0389 704 SER A OG 5408 N N . PHE A 712 ? 0.2055 0.1969 0.2429 -0.0127 -0.0103 -0.0215 705 PHE A N 5409 C CA . PHE A 712 ? 0.1959 0.1966 0.2364 -0.0125 0.0037 -0.0291 705 PHE A CA 5410 C C . PHE A 712 ? 0.1818 0.1983 0.2306 -0.0160 0.0086 -0.0219 705 PHE A C 5411 O O . PHE A 712 ? 0.1641 0.2084 0.2172 -0.0048 0.0306 -0.0237 705 PHE A O 5412 C CB . PHE A 712 ? 0.2125 0.1698 0.2318 -0.0095 -0.0060 -0.0333 705 PHE A CB 5413 C CG . PHE A 712 ? 0.2253 0.1863 0.2549 0.0050 -0.0093 -0.0323 705 PHE A CG 5414 C CD1 . PHE A 712 ? 0.1995 0.1836 0.2409 -0.0145 0.0010 -0.0452 705 PHE A CD1 5415 C CD2 . PHE A 712 ? 0.1984 0.1843 0.2354 0.0061 -0.0146 -0.0298 705 PHE A CD2 5416 C CE1 . PHE A 712 ? 0.2151 0.1788 0.2627 0.0259 -0.0456 -0.0265 705 PHE A CE1 5417 C CE2 . PHE A 712 ? 0.2486 0.1739 0.2821 0.0268 -0.0152 -0.0246 705 PHE A CE2 5418 C CZ . PHE A 712 ? 0.2193 0.1572 0.2757 -0.0149 -0.0184 0.0062 705 PHE A CZ 5419 N N . PRO A 713 ? 0.1796 0.1893 0.2338 -0.0138 0.0219 -0.0257 706 PRO A N 5420 C CA . PRO A 713 ? 0.1744 0.1962 0.2201 -0.0133 0.0157 -0.0226 706 PRO A CA 5421 C C . PRO A 713 ? 0.1974 0.1931 0.2340 -0.0109 0.0328 -0.0131 706 PRO A C 5422 O O . PRO A 713 ? 0.2074 0.2166 0.2572 -0.0027 0.0256 -0.0193 706 PRO A O 5423 C CB . PRO A 713 ? 0.1514 0.1796 0.1976 -0.0202 0.0303 -0.0128 706 PRO A CB 5424 C CG . PRO A 713 ? 0.1809 0.2032 0.2265 -0.0425 0.0121 -0.0262 706 PRO A CG 5425 C CD . PRO A 713 ? 0.1665 0.1831 0.2306 -0.0158 0.0203 -0.0219 706 PRO A CD 5426 N N . GLY A 714 ? 0.1872 0.1898 0.2527 -0.0085 0.0284 -0.0035 707 GLY A N 5427 C CA . GLY A 714 ? 0.1972 0.1935 0.2414 -0.0207 0.0237 -0.0003 707 GLY A CA 5428 C C . GLY A 714 ? 0.2065 0.2007 0.2489 -0.0202 0.0246 -0.0047 707 GLY A C 5429 O O . GLY A 714 ? 0.2351 0.1878 0.2470 -0.0370 0.0276 -0.0056 707 GLY A O 5430 N N . ILE A 715 ? 0.1906 0.1970 0.2451 -0.0167 0.0258 -0.0152 708 ILE A N 5431 C CA . ILE A 715 ? 0.2052 0.1937 0.2456 -0.0224 0.0304 -0.0111 708 ILE A CA 5432 C C . ILE A 715 ? 0.2217 0.2140 0.2450 -0.0296 0.0315 -0.0075 708 ILE A C 5433 O O . ILE A 715 ? 0.2156 0.2123 0.2296 -0.0487 0.0545 0.0081 708 ILE A O 5434 C CB . ILE A 715 ? 0.1991 0.1988 0.2309 -0.0240 0.0257 -0.0109 708 ILE A CB 5435 C CG1 . ILE A 715 ? 0.2188 0.1973 0.1970 -0.0371 0.0125 -0.0351 708 ILE A CG1 5436 C CG2 . ILE A 715 ? 0.2157 0.2073 0.2558 -0.0226 0.0280 -0.0143 708 ILE A CG2 5437 C CD1 . ILE A 715 ? 0.2109 0.2320 0.1768 -0.0240 -0.0187 -0.0453 708 ILE A CD1 5438 N N . TYR A 716 ? 0.2044 0.2018 0.2389 -0.0212 0.0179 -0.0076 709 TYR A N 5439 C CA . TYR A 716 ? 0.1963 0.2131 0.2488 -0.0216 0.0197 -0.0160 709 TYR A CA 5440 C C . TYR A 716 ? 0.2092 0.2216 0.2507 -0.0249 0.0293 -0.0066 709 TYR A C 5441 O O . TYR A 716 ? 0.2033 0.2223 0.2842 -0.0325 0.0213 -0.0307 709 TYR A O 5442 C CB . TYR A 716 ? 0.1937 0.2012 0.2352 -0.0171 0.0203 -0.0139 709 TYR A CB 5443 C CG . TYR A 716 ? 0.2128 0.2216 0.2529 -0.0172 0.0428 -0.0156 709 TYR A CG 5444 C CD1 . TYR A 716 ? 0.2225 0.2284 0.2793 -0.0042 0.0415 -0.0163 709 TYR A CD1 5445 C CD2 . TYR A 716 ? 0.2405 0.2357 0.2870 0.0000 0.0419 -0.0208 709 TYR A CD2 5446 C CE1 . TYR A 716 ? 0.2392 0.2108 0.3404 -0.0268 0.0623 -0.0139 709 TYR A CE1 5447 C CE2 . TYR A 716 ? 0.2185 0.2563 0.3093 -0.0148 0.0691 -0.0184 709 TYR A CE2 5448 C CZ . TYR A 716 ? 0.2383 0.2630 0.3111 -0.0026 0.0570 -0.0165 709 TYR A CZ 5449 O OH . TYR A 716 ? 0.1852 0.3027 0.3545 -0.0144 0.0633 -0.0006 709 TYR A OH 5450 N N . ASP A 717 ? 0.2024 0.2176 0.2572 -0.0241 0.0233 0.0017 710 ASP A N 5451 C CA . ASP A 717 ? 0.2219 0.2258 0.2567 -0.0229 0.0410 -0.0008 710 ASP A CA 5452 C C . ASP A 717 ? 0.2258 0.2341 0.2554 -0.0158 0.0424 0.0004 710 ASP A C 5453 O O . ASP A 717 ? 0.2246 0.2498 0.2386 -0.0171 0.0357 -0.0148 710 ASP A O 5454 C CB . ASP A 717 ? 0.2125 0.2211 0.2817 -0.0256 0.0316 0.0136 710 ASP A CB 5455 C CG . ASP A 717 ? 0.2227 0.2239 0.2785 -0.0234 0.0439 -0.0028 710 ASP A CG 5456 O OD1 . ASP A 717 ? 0.2156 0.2838 0.2942 -0.0481 0.0276 0.0018 710 ASP A OD1 5457 O OD2 . ASP A 717 ? 0.2160 0.2337 0.3478 -0.0232 0.0143 0.0026 710 ASP A OD2 5458 N N . ALA A 718 ? 0.2368 0.2112 0.2572 0.0039 0.0498 -0.0101 711 ALA A N 5459 C CA . ALA A 718 ? 0.2440 0.2291 0.2619 0.0013 0.0604 -0.0063 711 ALA A CA 5460 C C . ALA A 718 ? 0.2584 0.2290 0.2724 -0.0014 0.0534 -0.0096 711 ALA A C 5461 O O . ALA A 718 ? 0.2633 0.2313 0.2863 -0.0043 0.0513 0.0025 711 ALA A O 5462 C CB . ALA A 718 ? 0.2478 0.2201 0.2464 0.0156 0.0451 -0.0011 711 ALA A CB 5463 N N . LEU A 719 ? 0.2508 0.2301 0.2708 -0.0132 0.0461 -0.0179 712 LEU A N 5464 C CA . LEU A 719 ? 0.2514 0.2309 0.2760 -0.0145 0.0547 -0.0166 712 LEU A CA 5465 C C . LEU A 719 ? 0.2545 0.2523 0.2722 -0.0179 0.0608 -0.0076 712 LEU A C 5466 O O . LEU A 719 ? 0.2476 0.2409 0.2620 -0.0257 0.0672 -0.0195 712 LEU A O 5467 C CB . LEU A 719 ? 0.2393 0.2514 0.2972 -0.0201 0.0518 -0.0081 712 LEU A CB 5468 C CG . LEU A 719 ? 0.2333 0.2504 0.2891 -0.0296 0.0526 -0.0057 712 LEU A CG 5469 C CD1 . LEU A 719 ? 0.1896 0.2938 0.2873 -0.0352 0.0590 0.0284 712 LEU A CD1 5470 C CD2 . LEU A 719 ? 0.2783 0.2308 0.3328 0.0118 0.0669 0.0385 712 LEU A CD2 5471 N N . PHE A 720 ? 0.2633 0.2212 0.2755 -0.0175 0.0666 -0.0109 713 PHE A N 5472 C CA . PHE A 720 ? 0.2870 0.2612 0.2993 -0.0105 0.0812 0.0008 713 PHE A CA 5473 C C . PHE A 720 ? 0.2975 0.2656 0.2935 -0.0122 0.0853 -0.0082 713 PHE A C 5474 O O . PHE A 720 ? 0.2690 0.2556 0.2893 -0.0085 0.0867 -0.0068 713 PHE A O 5475 C CB . PHE A 720 ? 0.2883 0.2326 0.3066 -0.0047 0.0801 -0.0043 713 PHE A CB 5476 C CG . PHE A 720 ? 0.2993 0.2712 0.3261 0.0006 0.0866 -0.0152 713 PHE A CG 5477 C CD1 . PHE A 720 ? 0.2750 0.2610 0.3277 0.0215 0.0637 -0.0289 713 PHE A CD1 5478 C CD2 . PHE A 720 ? 0.3296 0.2589 0.2891 -0.0006 0.0929 -0.0129 713 PHE A CD2 5479 C CE1 . PHE A 720 ? 0.3362 0.2997 0.3344 0.0240 0.0542 -0.0412 713 PHE A CE1 5480 C CE2 . PHE A 720 ? 0.3222 0.2752 0.3504 0.0168 0.0671 -0.0094 713 PHE A CE2 5481 C CZ . PHE A 720 ? 0.3280 0.2936 0.3468 0.0222 0.0776 -0.0425 713 PHE A CZ 5482 N N . ASP A 721 ? 0.2950 0.2696 0.3059 -0.0098 0.0947 -0.0048 714 ASP A N 5483 C CA . ASP A 721 ? 0.3354 0.2976 0.3261 -0.0113 0.0958 0.0015 714 ASP A CA 5484 C C . ASP A 721 ? 0.3480 0.3099 0.3338 -0.0088 0.1001 0.0074 714 ASP A C 5485 O O . ASP A 721 ? 0.3480 0.2950 0.3468 -0.0078 0.0919 -0.0098 714 ASP A O 5486 C CB . ASP A 721 ? 0.3310 0.3035 0.3204 -0.0153 0.0982 -0.0079 714 ASP A CB 5487 C CG . ASP A 721 ? 0.3519 0.3531 0.3328 -0.0262 0.0945 0.0069 714 ASP A CG 5488 O OD1 . ASP A 721 ? 0.3966 0.4043 0.2835 -0.0454 0.1340 0.0087 714 ASP A OD1 5489 O OD2 . ASP A 721 ? 0.3932 0.4319 0.3671 -0.0076 0.0543 0.0271 714 ASP A OD2 5490 N N . ILE A 722 ? 0.3678 0.3075 0.3446 -0.0112 0.1042 0.0109 715 ILE A N 5491 C CA . ILE A 722 ? 0.3625 0.3208 0.3474 -0.0113 0.1070 0.0166 715 ILE A CA 5492 C C . ILE A 722 ? 0.4049 0.3504 0.3735 -0.0121 0.1067 0.0163 715 ILE A C 5493 O O . ILE A 722 ? 0.4000 0.3482 0.3805 -0.0073 0.1096 0.0097 715 ILE A O 5494 C CB . ILE A 722 ? 0.3481 0.3163 0.3396 -0.0038 0.1012 0.0194 715 ILE A CB 5495 C CG1 . ILE A 722 ? 0.3326 0.3034 0.3160 -0.0027 0.1115 0.0024 715 ILE A CG1 5496 C CG2 . ILE A 722 ? 0.3379 0.2841 0.3199 -0.0329 0.1044 0.0235 715 ILE A CG2 5497 C CD1 . ILE A 722 ? 0.3420 0.3025 0.2478 0.0338 0.0943 0.0329 715 ILE A CD1 5498 N N . GLU A 723 ? 0.4173 0.3885 0.3929 -0.0074 0.1169 0.0223 716 GLU A N 5499 C CA . GLU A 723 ? 0.4632 0.4371 0.4424 -0.0080 0.1256 0.0347 716 GLU A CA 5500 C C . GLU A 723 ? 0.4873 0.4581 0.4483 -0.0066 0.1224 0.0355 716 GLU A C 5501 O O . GLU A 723 ? 0.5032 0.4693 0.4619 -0.0024 0.1170 0.0344 716 GLU A O 5502 C CB . GLU A 723 ? 0.4619 0.4355 0.4496 -0.0027 0.1229 0.0407 716 GLU A CB 5503 C CG . GLU A 723 ? 0.4820 0.4626 0.4763 0.0000 0.1497 0.0301 716 GLU A CG 5504 C CD . GLU A 723 ? 0.4905 0.4653 0.4898 0.0095 0.1473 0.0260 716 GLU A CD 5505 O OE1 . GLU A 723 ? 0.4491 0.4179 0.4608 -0.0182 0.1521 0.0113 716 GLU A OE1 5506 O OE2 . GLU A 723 ? 0.4982 0.5092 0.5061 0.0074 0.1416 -0.0119 716 GLU A OE2 5507 N N . SER A 724 ? 0.5074 0.4651 0.4559 -0.0023 0.1183 0.0377 717 SER A N 5508 C CA . SER A 724 ? 0.5310 0.4851 0.4584 0.0053 0.1157 0.0345 717 SER A CA 5509 C C . SER A 724 ? 0.5439 0.4971 0.4549 0.0009 0.1080 0.0403 717 SER A C 5510 O O . SER A 724 ? 0.5677 0.4951 0.4636 -0.0019 0.1032 0.0197 717 SER A O 5511 C CB . SER A 724 ? 0.5359 0.4879 0.4576 0.0087 0.1119 0.0293 717 SER A CB 5512 O OG . SER A 724 ? 0.5382 0.4826 0.4269 0.0384 0.1348 0.0082 717 SER A OG 5513 N N . LYS A 725 ? 0.5404 0.4919 0.4286 0.0030 0.1161 0.0486 718 LYS A N 5514 C CA . LYS A 725 ? 0.5482 0.5023 0.4337 -0.0038 0.1024 0.0569 718 LYS A CA 5515 C C . LYS A 725 ? 0.5631 0.5116 0.4369 -0.0031 0.1016 0.0641 718 LYS A C 5516 O O . LYS A 725 ? 0.5517 0.5104 0.4387 -0.0052 0.0883 0.0754 718 LYS A O 5517 C CB . LYS A 725 ? 0.5272 0.4976 0.4242 -0.0063 0.1101 0.0597 718 LYS A CB 5518 C CG . LYS A 725 ? 0.5348 0.4893 0.4267 -0.0247 0.1151 0.0544 718 LYS A CG 5519 C CD . LYS A 725 ? 0.5785 0.5205 0.4364 -0.0569 0.1134 0.0587 718 LYS A CD 5520 C CE . LYS A 725 ? 0.5723 0.5373 0.4151 -0.1003 0.1402 0.0642 718 LYS A CE 5521 N NZ . LYS A 725 ? 0.5904 0.4887 0.3744 -0.1343 0.1402 0.0572 718 LYS A NZ 5522 N N . VAL A 726 ? 0.5856 0.5104 0.4342 -0.0012 0.0908 0.0613 719 VAL A N 5523 C CA . VAL A 726 ? 0.6012 0.5244 0.4432 0.0075 0.0908 0.0502 719 VAL A CA 5524 C C . VAL A 726 ? 0.5846 0.5154 0.4295 0.0024 0.0986 0.0545 719 VAL A C 5525 O O . VAL A 726 ? 0.5893 0.5267 0.4056 0.0063 0.1094 0.0547 719 VAL A O 5526 C CB . VAL A 726 ? 0.6193 0.5302 0.4500 0.0091 0.0825 0.0467 719 VAL A CB 5527 C CG1 . VAL A 726 ? 0.6208 0.5281 0.4651 0.0091 0.0783 0.0459 719 VAL A CG1 5528 C CG2 . VAL A 726 ? 0.6292 0.5489 0.4611 0.0184 0.0817 0.0317 719 VAL A CG2 5529 N N . ASP A 727 ? 0.5579 0.5045 0.4174 0.0027 0.0998 0.0477 720 ASP A N 5530 C CA . ASP A 727 ? 0.5341 0.4794 0.4032 -0.0054 0.0974 0.0468 720 ASP A CA 5531 C C . ASP A 727 ? 0.5069 0.4451 0.4063 -0.0127 0.0989 0.0462 720 ASP A C 5532 O O . ASP A 727 ? 0.4987 0.4213 0.3674 -0.0270 0.0926 0.0254 720 ASP A O 5533 C CB . ASP A 727 ? 0.5434 0.4970 0.4019 0.0033 0.0868 0.0434 720 ASP A CB 5534 C CG . ASP A 727 ? 0.5596 0.5169 0.4185 0.0028 0.0807 0.0437 720 ASP A CG 5535 O OD1 . ASP A 727 ? 0.5552 0.4992 0.4096 -0.0167 0.0767 0.0801 720 ASP A OD1 5536 O OD2 . ASP A 727 ? 0.5905 0.6099 0.4340 -0.0069 0.0432 0.0399 720 ASP A OD2 5537 N N . PRO A 728 ? 0.4909 0.4188 0.4028 -0.0172 0.1021 0.0563 721 PRO A N 5538 C CA . PRO A 728 ? 0.4656 0.4062 0.4066 -0.0169 0.0974 0.0643 721 PRO A CA 5539 C C . PRO A 728 ? 0.4395 0.3857 0.3948 -0.0252 0.0906 0.0696 721 PRO A C 5540 O O . PRO A 728 ? 0.4202 0.3663 0.3959 -0.0283 0.0780 0.0703 721 PRO A O 5541 C CB . PRO A 728 ? 0.4653 0.4129 0.4058 -0.0210 0.1005 0.0701 721 PRO A CB 5542 C CG . PRO A 728 ? 0.4878 0.4339 0.4132 -0.0185 0.1001 0.0605 721 PRO A CG 5543 C CD . PRO A 728 ? 0.4958 0.4304 0.4166 -0.0192 0.1011 0.0531 721 PRO A CD 5544 N N . SER A 729 ? 0.4218 0.3714 0.3875 -0.0093 0.0830 0.0646 722 SER A N 5545 C CA . SER A 729 ? 0.4439 0.3751 0.3829 0.0029 0.0672 0.0694 722 SER A CA 5546 C C . SER A 729 ? 0.4229 0.3664 0.3710 0.0054 0.0645 0.0574 722 SER A C 5547 O O . SER A 729 ? 0.4176 0.3372 0.3453 0.0197 0.0514 0.0580 722 SER A O 5548 C CB . SER A 729 ? 0.4459 0.3804 0.3963 0.0210 0.0653 0.0668 722 SER A CB 5549 O OG . SER A 729 ? 0.5141 0.4200 0.4389 0.0442 0.0400 0.0963 722 SER A OG 5550 N N . LYS A 730 ? 0.4142 0.3639 0.3489 -0.0065 0.0612 0.0513 723 LYS A N 5551 C CA . LYS A 730 ? 0.4017 0.3639 0.3472 -0.0246 0.0466 0.0434 723 LYS A CA 5552 C C . LYS A 730 ? 0.3661 0.3405 0.3186 -0.0227 0.0368 0.0299 723 LYS A C 5553 O O . LYS A 730 ? 0.3428 0.3161 0.2932 -0.0235 0.0154 0.0379 723 LYS A O 5554 C CB . LYS A 730 ? 0.4180 0.3944 0.3455 -0.0359 0.0487 0.0337 723 LYS A CB 5555 C CG . LYS A 730 ? 0.4673 0.4540 0.4216 -0.0635 0.0557 0.0268 723 LYS A CG 5556 C CD . LYS A 730 ? 0.5160 0.4749 0.4435 -0.0629 0.0399 0.0034 723 LYS A CD 5557 C CE . LYS A 730 ? 0.5271 0.4713 0.4430 -0.0670 0.0439 -0.0049 723 LYS A CE 5558 N NZ . LYS A 730 ? 0.5568 0.4810 0.4530 -0.0569 0.0345 -0.0177 723 LYS A NZ 5559 N N . ALA A 731 ? 0.3323 0.3115 0.2914 -0.0216 0.0306 0.0215 724 ALA A N 5560 C CA . ALA A 731 ? 0.3148 0.2874 0.2824 -0.0199 0.0394 0.0096 724 ALA A CA 5561 C C . ALA A 731 ? 0.3016 0.2783 0.2659 -0.0134 0.0545 0.0167 724 ALA A C 5562 O O . ALA A 731 ? 0.2919 0.2776 0.2697 -0.0290 0.0351 0.0014 724 ALA A O 5563 C CB . ALA A 731 ? 0.3164 0.2869 0.2533 -0.0076 0.0603 0.0051 724 ALA A CB 5564 N N . TRP A 732 ? 0.2701 0.2595 0.2627 -0.0146 0.0526 0.0051 725 TRP A N 5565 C CA . TRP A 732 ? 0.2731 0.2554 0.2741 -0.0202 0.0603 0.0210 725 TRP A CA 5566 C C . TRP A 732 ? 0.2681 0.2363 0.2709 -0.0188 0.0594 0.0248 725 TRP A C 5567 O O . TRP A 732 ? 0.2718 0.2326 0.2713 -0.0107 0.0380 0.0326 725 TRP A O 5568 C CB . TRP A 732 ? 0.2685 0.2484 0.2401 -0.0228 0.0722 0.0244 725 TRP A CB 5569 C CG . TRP A 732 ? 0.2765 0.2581 0.2998 -0.0240 0.0694 0.0310 725 TRP A CG 5570 C CD1 . TRP A 732 ? 0.2758 0.3022 0.3277 -0.0177 0.0763 -0.0080 725 TRP A CD1 5571 C CD2 . TRP A 732 ? 0.3099 0.2563 0.3240 -0.0126 0.0631 0.0286 725 TRP A CD2 5572 N NE1 . TRP A 732 ? 0.2817 0.2677 0.3280 -0.0030 0.0562 0.0182 725 TRP A NE1 5573 C CE2 . TRP A 732 ? 0.2976 0.2589 0.3465 -0.0227 0.0793 0.0465 725 TRP A CE2 5574 C CE3 . TRP A 732 ? 0.3204 0.2414 0.3309 -0.0119 0.0745 0.0677 725 TRP A CE3 5575 C CZ2 . TRP A 732 ? 0.3217 0.2388 0.3607 -0.0221 0.0626 0.0511 725 TRP A CZ2 5576 C CZ3 . TRP A 732 ? 0.3091 0.2447 0.3223 -0.0094 0.0802 0.0576 725 TRP A CZ3 5577 C CH2 . TRP A 732 ? 0.3178 0.2614 0.3370 -0.0168 0.0896 0.0576 725 TRP A CH2 5578 N N . GLY A 733 ? 0.2682 0.2420 0.2559 -0.0145 0.0489 0.0362 726 GLY A N 5579 C CA . GLY A 733 ? 0.2587 0.2319 0.2481 -0.0232 0.0536 0.0317 726 GLY A CA 5580 C C . GLY A 733 ? 0.2569 0.2426 0.2577 -0.0216 0.0355 0.0272 726 GLY A C 5581 O O . GLY A 733 ? 0.2663 0.2313 0.2782 -0.0252 0.0313 0.0363 726 GLY A O 5582 N N . GLU A 734 ? 0.2538 0.2542 0.2601 -0.0175 0.0265 0.0343 727 GLU A N 5583 C CA . GLU A 734 ? 0.2452 0.2455 0.2711 -0.0249 0.0231 0.0256 727 GLU A CA 5584 C C . GLU A 734 ? 0.2359 0.2398 0.2649 -0.0290 0.0268 0.0162 727 GLU A C 5585 O O . GLU A 734 ? 0.2074 0.2273 0.2548 -0.0339 0.0182 0.0057 727 GLU A O 5586 C CB . GLU A 734 ? 0.2528 0.2629 0.2771 -0.0227 0.0280 0.0179 727 GLU A CB 5587 C CG A GLU A 734 ? 0.2666 0.2647 0.2974 -0.0334 0.0334 0.0227 727 GLU A CG 5588 C CD A GLU A 734 ? 0.2968 0.3083 0.2928 -0.0336 0.0369 0.0080 727 GLU A CD 5589 O OE1 A GLU A 734 ? 0.3177 0.2976 0.3315 -0.0552 -0.0094 0.0013 727 GLU A OE1 5590 O OE2 A GLU A 734 ? 0.3245 0.3219 0.2618 -0.0584 0.0205 0.0019 727 GLU A OE2 5591 N N . VAL A 735 ? 0.2312 0.2301 0.2672 -0.0210 0.0305 0.0058 728 VAL A N 5592 C CA . VAL A 735 ? 0.2174 0.2178 0.2669 -0.0236 0.0321 0.0059 728 VAL A CA 5593 C C . VAL A 735 ? 0.2196 0.2215 0.2673 -0.0308 0.0362 0.0144 728 VAL A C 5594 O O . VAL A 735 ? 0.2143 0.2088 0.2844 -0.0524 0.0464 0.0285 728 VAL A O 5595 C CB . VAL A 735 ? 0.2113 0.2308 0.2529 -0.0128 0.0404 -0.0031 728 VAL A CB 5596 C CG1 . VAL A 735 ? 0.2026 0.2226 0.2286 -0.0267 0.0507 0.0024 728 VAL A CG1 5597 C CG2 . VAL A 735 ? 0.2320 0.1924 0.2616 0.0075 0.0356 0.0078 728 VAL A CG2 5598 N N . LYS A 736 ? 0.2190 0.2065 0.2762 -0.0322 0.0382 0.0165 729 LYS A N 5599 C CA . LYS A 736 ? 0.2245 0.2086 0.2602 -0.0375 0.0366 0.0188 729 LYS A CA 5600 C C . LYS A 736 ? 0.2300 0.2102 0.2424 -0.0404 0.0294 0.0193 729 LYS A C 5601 O O . LYS A 736 ? 0.2273 0.2073 0.1862 -0.0376 0.0319 0.0083 729 LYS A O 5602 C CB . LYS A 736 ? 0.2296 0.1965 0.2592 -0.0515 0.0329 0.0406 729 LYS A CB 5603 C CG . LYS A 736 ? 0.1865 0.2026 0.2640 -0.0439 0.0318 0.0299 729 LYS A CG 5604 C CD . LYS A 736 ? 0.2463 0.2017 0.4050 -0.0696 0.0439 0.0545 729 LYS A CD 5605 C CE . LYS A 736 ? 0.2783 0.2577 0.4125 -0.0281 0.0382 0.0732 729 LYS A CE 5606 N NZ . LYS A 736 ? 0.3415 0.3206 0.5168 -0.0436 0.0223 0.1255 729 LYS A NZ 5607 N N . ARG A 737 ? 0.2278 0.1963 0.2309 -0.0428 0.0174 0.0058 730 ARG A N 5608 C CA . ARG A 737 ? 0.1961 0.2075 0.2265 -0.0299 0.0113 0.0077 730 ARG A CA 5609 C C . ARG A 737 ? 0.1982 0.2064 0.2249 -0.0281 0.0037 0.0015 730 ARG A C 5610 O O . ARG A 737 ? 0.2088 0.2227 0.2444 -0.0148 -0.0006 0.0029 730 ARG A O 5611 C CB . ARG A 737 ? 0.2045 0.1969 0.2177 -0.0336 0.0047 0.0049 730 ARG A CB 5612 C CG . ARG A 737 ? 0.2050 0.2379 0.2062 -0.0411 -0.0067 0.0114 730 ARG A CG 5613 C CD . ARG A 737 ? 0.2483 0.2493 0.2986 -0.0489 0.0044 -0.0276 730 ARG A CD 5614 N NE . ARG A 737 ? 0.2759 0.2602 0.3018 -0.0218 0.0011 0.0208 730 ARG A NE 5615 C CZ . ARG A 737 ? 0.2686 0.2893 0.3585 -0.0363 0.0126 0.0218 730 ARG A CZ 5616 N NH1 . ARG A 737 ? 0.3079 0.3515 0.3430 -0.0567 -0.0266 0.0472 730 ARG A NH1 5617 N NH2 . ARG A 737 ? 0.2912 0.2738 0.3990 -0.0742 0.0221 0.0277 730 ARG A NH2 5618 N N . GLN A 738 ? 0.1843 0.1932 0.2220 -0.0212 -0.0090 -0.0014 731 GLN A N 5619 C CA . GLN A 738 ? 0.1877 0.1796 0.2301 -0.0262 -0.0030 -0.0013 731 GLN A CA 5620 C C . GLN A 738 ? 0.2045 0.1869 0.2272 -0.0179 0.0063 -0.0009 731 GLN A C 5621 O O . GLN A 738 ? 0.1866 0.1919 0.2291 -0.0039 -0.0038 0.0023 731 GLN A O 5622 C CB . GLN A 738 ? 0.1848 0.1770 0.2224 -0.0296 0.0059 -0.0114 731 GLN A CB 5623 C CG . GLN A 738 ? 0.2034 0.1853 0.2252 -0.0047 -0.0157 0.0016 731 GLN A CG 5624 C CD . GLN A 738 ? 0.2463 0.2598 0.2355 -0.0105 -0.0128 0.0095 731 GLN A CD 5625 O OE1 . GLN A 738 ? 0.2753 0.2387 0.2103 0.0020 -0.0308 -0.0133 731 GLN A OE1 5626 N NE2 . GLN A 738 ? 0.2697 0.2906 0.2462 -0.0191 -0.0312 0.0052 731 GLN A NE2 5627 N N . ILE A 739 ? 0.1902 0.1893 0.2367 -0.0356 0.0015 -0.0059 732 ILE A N 5628 C CA . ILE A 739 ? 0.1990 0.1977 0.2364 -0.0260 -0.0001 -0.0030 732 ILE A CA 5629 C C . ILE A 739 ? 0.1986 0.2070 0.2490 -0.0335 0.0101 0.0055 732 ILE A C 5630 O O . ILE A 739 ? 0.2146 0.2381 0.2705 -0.0399 0.0055 -0.0106 732 ILE A O 5631 C CB . ILE A 739 ? 0.1723 0.1904 0.2106 -0.0313 -0.0018 -0.0055 732 ILE A CB 5632 C CG1 . ILE A 739 ? 0.1960 0.2090 0.2401 -0.0360 -0.0031 0.0278 732 ILE A CG1 5633 C CG2 . ILE A 739 ? 0.1653 0.2123 0.2360 -0.0143 0.0038 -0.0249 732 ILE A CG2 5634 C CD1 . ILE A 739 ? 0.1917 0.1931 0.2548 -0.0580 0.0025 0.0390 732 ILE A CD1 5635 N N . TYR A 740 ? 0.1824 0.2011 0.2553 -0.0251 0.0083 0.0068 733 TYR A N 5636 C CA . TYR A 740 ? 0.2100 0.2139 0.2602 -0.0135 0.0099 0.0094 733 TYR A CA 5637 C C . TYR A 740 ? 0.1881 0.2024 0.2498 -0.0201 0.0057 0.0097 733 TYR A C 5638 O O . TYR A 740 ? 0.1660 0.1982 0.2393 -0.0247 0.0132 0.0152 733 TYR A O 5639 C CB . TYR A 740 ? 0.2108 0.2291 0.2679 0.0019 0.0099 0.0110 733 TYR A CB 5640 C CG . TYR A 740 ? 0.2642 0.2714 0.2924 0.0352 0.0029 -0.0120 733 TYR A CG 5641 C CD1 . TYR A 740 ? 0.2897 0.2843 0.2909 0.0571 0.0084 -0.0141 733 TYR A CD1 5642 C CD2 . TYR A 740 ? 0.2686 0.2937 0.2571 0.0138 0.0125 -0.0226 733 TYR A CD2 5643 C CE1 . TYR A 740 ? 0.2667 0.3132 0.2999 -0.0129 0.0016 -0.0318 733 TYR A CE1 5644 C CE2 . TYR A 740 ? 0.2659 0.2995 0.2655 -0.0175 0.0105 -0.0069 733 TYR A CE2 5645 C CZ . TYR A 740 ? 0.2784 0.3159 0.2715 -0.0105 0.0059 -0.0113 733 TYR A CZ 5646 O OH . TYR A 740 ? 0.2632 0.3171 0.2298 -0.0344 -0.0153 -0.0072 733 TYR A OH 5647 N N . VAL A 741 ? 0.1923 0.1943 0.2325 -0.0173 -0.0044 0.0006 734 VAL A N 5648 C CA . VAL A 741 ? 0.1922 0.1896 0.2258 -0.0266 -0.0137 0.0132 734 VAL A CA 5649 C C . VAL A 741 ? 0.2003 0.2022 0.2343 -0.0160 -0.0103 -0.0036 734 VAL A C 5650 O O . VAL A 741 ? 0.2061 0.2038 0.2477 -0.0073 -0.0044 -0.0067 734 VAL A O 5651 C CB . VAL A 741 ? 0.1830 0.1869 0.2038 -0.0248 -0.0152 0.0210 734 VAL A CB 5652 C CG1 . VAL A 741 ? 0.1859 0.1946 0.2143 -0.0477 -0.0149 0.0067 734 VAL A CG1 5653 C CG2 . VAL A 741 ? 0.1906 0.2058 0.1962 -0.0620 -0.0253 0.0291 734 VAL A CG2 5654 N N . ALA A 742 ? 0.1976 0.2013 0.2479 0.0015 -0.0212 -0.0097 735 ALA A N 5655 C CA . ALA A 742 ? 0.1939 0.1903 0.2323 0.0057 -0.0216 -0.0084 735 ALA A CA 5656 C C . ALA A 742 ? 0.1835 0.1886 0.2366 0.0081 -0.0176 -0.0113 735 ALA A C 5657 O O . ALA A 742 ? 0.1876 0.1986 0.2552 0.0178 -0.0388 -0.0139 735 ALA A O 5658 C CB . ALA A 742 ? 0.1926 0.1854 0.2203 0.0053 -0.0104 0.0077 735 ALA A CB 5659 N N . ALA A 743 ? 0.1827 0.1836 0.2419 0.0112 -0.0169 -0.0165 736 ALA A N 5660 C CA . ALA A 743 ? 0.1812 0.1789 0.2325 -0.0034 -0.0250 -0.0206 736 ALA A CA 5661 C C . ALA A 743 ? 0.1953 0.1926 0.2231 0.0001 -0.0300 -0.0149 736 ALA A C 5662 O O . ALA A 743 ? 0.1939 0.1945 0.2215 0.0000 -0.0409 -0.0152 736 ALA A O 5663 C CB . ALA A 743 ? 0.1791 0.1801 0.1910 -0.0066 -0.0414 0.0027 736 ALA A CB 5664 N N . PHE A 744 ? 0.1768 0.1998 0.2316 -0.0007 -0.0287 -0.0121 737 PHE A N 5665 C CA . PHE A 744 ? 0.1834 0.2043 0.2266 0.0026 -0.0234 -0.0051 737 PHE A CA 5666 C C . PHE A 744 ? 0.1886 0.1921 0.2265 0.0039 -0.0308 -0.0082 737 PHE A C 5667 O O . PHE A 744 ? 0.1835 0.1866 0.2303 0.0025 -0.0202 0.0021 737 PHE A O 5668 C CB . PHE A 744 ? 0.1777 0.2168 0.2066 -0.0056 -0.0178 -0.0107 737 PHE A CB 5669 C CG . PHE A 744 ? 0.2046 0.2324 0.2416 0.0042 -0.0154 -0.0005 737 PHE A CG 5670 C CD1 . PHE A 744 ? 0.1859 0.2559 0.2004 0.0438 -0.0218 -0.0001 737 PHE A CD1 5671 C CD2 . PHE A 744 ? 0.1978 0.2375 0.2441 -0.0229 -0.0354 0.0122 737 PHE A CD2 5672 C CE1 . PHE A 744 ? 0.1545 0.2000 0.2071 0.0391 -0.0285 0.0187 737 PHE A CE1 5673 C CE2 . PHE A 744 ? 0.1943 0.2043 0.2308 0.0132 0.0324 0.0053 737 PHE A CE2 5674 C CZ . PHE A 744 ? 0.1727 0.2012 0.2181 0.0430 -0.0318 -0.0062 737 PHE A CZ 5675 N N . THR A 745 ? 0.1862 0.1825 0.2354 0.0097 -0.0283 -0.0089 738 THR A N 5676 C CA . THR A 745 ? 0.2049 0.1826 0.2148 0.0008 -0.0253 -0.0097 738 THR A CA 5677 C C . THR A 745 ? 0.2130 0.1897 0.2379 0.0033 -0.0193 -0.0166 738 THR A C 5678 O O . THR A 745 ? 0.2087 0.2024 0.2198 -0.0081 -0.0153 -0.0047 738 THR A O 5679 C CB . THR A 745 ? 0.2262 0.1729 0.2075 -0.0049 -0.0274 -0.0021 738 THR A CB 5680 O OG1 . THR A 745 ? 0.1675 0.1864 0.1881 -0.0089 -0.0307 -0.0058 738 THR A OG1 5681 C CG2 . THR A 745 ? 0.2225 0.1623 0.2165 0.0049 -0.0329 0.0040 738 THR A CG2 5682 N N . VAL A 746 ? 0.2014 0.1888 0.2563 -0.0007 -0.0227 -0.0226 739 VAL A N 5683 C CA . VAL A 746 ? 0.1942 0.1876 0.2423 0.0032 -0.0328 -0.0235 739 VAL A CA 5684 C C . VAL A 746 ? 0.1907 0.1984 0.2494 -0.0053 -0.0346 -0.0141 739 VAL A C 5685 O O . VAL A 746 ? 0.1907 0.2118 0.2341 -0.0161 -0.0489 0.0111 739 VAL A O 5686 C CB . VAL A 746 ? 0.2025 0.1771 0.2366 -0.0100 -0.0315 -0.0300 739 VAL A CB 5687 C CG1 . VAL A 746 ? 0.1816 0.1960 0.2316 -0.0130 -0.0353 -0.0057 739 VAL A CG1 5688 C CG2 . VAL A 746 ? 0.1889 0.1604 0.2497 0.0152 -0.0044 -0.0284 739 VAL A CG2 5689 N N . GLN A 747 ? 0.1688 0.1950 0.2512 0.0161 -0.0299 -0.0163 740 GLN A N 5690 C CA . GLN A 747 ? 0.2108 0.1887 0.2399 0.0117 -0.0280 -0.0267 740 GLN A CA 5691 C C . GLN A 747 ? 0.1947 0.1970 0.2271 0.0132 -0.0316 -0.0309 740 GLN A C 5692 O O . GLN A 747 ? 0.1956 0.1921 0.2331 0.0142 -0.0211 -0.0309 740 GLN A O 5693 C CB . GLN A 747 ? 0.1908 0.1841 0.2047 0.0259 -0.0306 -0.0168 740 GLN A CB 5694 C CG . GLN A 747 ? 0.1989 0.1791 0.2555 0.0251 -0.0481 -0.0239 740 GLN A CG 5695 C CD . GLN A 747 ? 0.2564 0.1970 0.2576 0.0396 -0.0364 -0.0283 740 GLN A CD 5696 O OE1 . GLN A 747 ? 0.2097 0.2125 0.2987 0.0512 -0.0315 0.0050 740 GLN A OE1 5697 N NE2 . GLN A 747 ? 0.3104 0.1502 0.2689 0.0741 -0.0246 -0.0537 740 GLN A NE2 5698 N N . ALA A 748 ? 0.1976 0.1911 0.2169 0.0160 -0.0454 -0.0275 741 ALA A N 5699 C CA . ALA A 748 ? 0.2001 0.2069 0.2082 0.0103 -0.0410 -0.0271 741 ALA A CA 5700 C C . ALA A 748 ? 0.2169 0.2024 0.2081 0.0169 -0.0432 -0.0327 741 ALA A C 5701 O O . ALA A 748 ? 0.2351 0.2116 0.2265 0.0133 -0.0206 -0.0328 741 ALA A O 5702 C CB . ALA A 748 ? 0.1881 0.2074 0.1782 0.0051 -0.0465 -0.0375 741 ALA A CB 5703 N N . ALA A 749 ? 0.1971 0.1961 0.2035 0.0219 -0.0551 -0.0313 742 ALA A N 5704 C CA . ALA A 749 ? 0.2209 0.1906 0.2220 0.0291 -0.0496 -0.0321 742 ALA A CA 5705 C C . ALA A 749 ? 0.2275 0.1857 0.2098 0.0328 -0.0507 -0.0324 742 ALA A C 5706 O O . ALA A 749 ? 0.2283 0.1783 0.2322 0.0291 -0.0514 -0.0246 742 ALA A O 5707 C CB . ALA A 749 ? 0.2117 0.1690 0.2051 0.0424 -0.0508 -0.0414 742 ALA A CB 5708 N N . ALA A 750 ? 0.2393 0.1984 0.2233 0.0266 -0.0544 -0.0328 743 ALA A N 5709 C CA . ALA A 750 ? 0.2566 0.2060 0.2330 0.0273 -0.0416 -0.0352 743 ALA A CA 5710 C C . ALA A 750 ? 0.2523 0.2236 0.2329 0.0363 -0.0478 -0.0233 743 ALA A C 5711 O O . ALA A 750 ? 0.2619 0.2426 0.2246 0.0430 -0.0446 -0.0055 743 ALA A O 5712 C CB . ALA A 750 ? 0.2421 0.2104 0.2164 0.0123 -0.0405 -0.0290 743 ALA A CB 5713 N N . GLU A 751 ? 0.2471 0.1965 0.2245 0.0335 -0.0523 -0.0110 744 GLU A N 5714 C CA . GLU A 751 ? 0.2608 0.1908 0.2227 0.0490 -0.0540 -0.0156 744 GLU A CA 5715 C C . GLU A 751 ? 0.2535 0.2004 0.2032 0.0462 -0.0523 -0.0220 744 GLU A C 5716 O O . GLU A 751 ? 0.2606 0.1957 0.2214 0.0438 -0.0635 -0.0329 744 GLU A O 5717 C CB . GLU A 751 ? 0.2591 0.1898 0.2197 0.0527 -0.0570 -0.0146 744 GLU A CB 5718 C CG . GLU A 751 ? 0.2735 0.1931 0.2586 0.0514 -0.0455 0.0154 744 GLU A CG 5719 C CD . GLU A 751 ? 0.3055 0.2486 0.2902 0.0297 -0.0728 0.0252 744 GLU A CD 5720 O OE1 . GLU A 751 ? 0.3335 0.2984 0.3458 0.0202 -0.0562 0.0437 744 GLU A OE1 5721 O OE2 . GLU A 751 ? 0.3117 0.2214 0.2989 0.0333 -0.0708 -0.0208 744 GLU A OE2 5722 N N . THR A 752 ? 0.2588 0.1973 0.1989 0.0499 -0.0471 -0.0120 745 THR A N 5723 C CA . THR A 752 ? 0.2457 0.2123 0.2029 0.0513 -0.0386 -0.0257 745 THR A CA 5724 C C . THR A 752 ? 0.2701 0.2312 0.2128 0.0511 -0.0464 -0.0240 745 THR A C 5725 O O . THR A 752 ? 0.2693 0.2439 0.2010 0.0472 -0.0452 -0.0198 745 THR A O 5726 C CB . THR A 752 ? 0.2439 0.2126 0.1976 0.0549 -0.0320 -0.0262 745 THR A CB 5727 O OG1 . THR A 752 ? 0.2608 0.2196 0.2245 0.0610 -0.0473 -0.0239 745 THR A OG1 5728 C CG2 . THR A 752 ? 0.1892 0.1759 0.1913 0.0525 0.0042 -0.0444 745 THR A CG2 5729 N N . LEU A 753 ? 0.2801 0.2237 0.2212 0.0597 -0.0539 -0.0393 746 LEU A N 5730 C CA . LEU A 753 ? 0.2899 0.2251 0.2374 0.0683 -0.0601 -0.0398 746 LEU A CA 5731 C C . LEU A 753 ? 0.2937 0.2351 0.2312 0.0678 -0.0666 -0.0421 746 LEU A C 5732 O O . LEU A 753 ? 0.2939 0.2389 0.2271 0.0763 -0.0811 -0.0205 746 LEU A O 5733 C CB . LEU A 753 ? 0.2966 0.2235 0.2374 0.0766 -0.0518 -0.0358 746 LEU A CB 5734 C CG . LEU A 753 ? 0.3085 0.2287 0.2563 0.0534 -0.0233 -0.0526 746 LEU A CG 5735 C CD1 . LEU A 753 ? 0.2522 0.2410 0.2437 0.0961 -0.0944 -0.0673 746 LEU A CD1 5736 C CD2 . LEU A 753 ? 0.3684 0.2436 0.2225 0.0370 -0.0059 -0.0512 746 LEU A CD2 5737 N N . SER A 754 ? 0.2878 0.2383 0.2283 0.0742 -0.0737 -0.0437 747 SER A N 5738 C CA . SER A 754 ? 0.3093 0.2282 0.2297 0.0678 -0.0808 -0.0549 747 SER A CA 5739 C C . SER A 754 ? 0.3174 0.2357 0.2399 0.0765 -0.0848 -0.0580 747 SER A C 5740 O O . SER A 754 ? 0.3288 0.2285 0.2478 0.0584 -0.0803 -0.0550 747 SER A O 5741 C CB . SER A 754 ? 0.3290 0.2402 0.2211 0.0611 -0.0742 -0.0602 747 SER A CB 5742 O OG . SER A 754 ? 0.3750 0.2755 0.2562 0.0652 -0.0707 -0.0456 747 SER A OG 5743 N N . GLU A 755 ? 0.3235 0.2377 0.2361 0.0800 -0.0811 -0.0746 748 GLU A N 5744 C CA . GLU A 755 ? 0.3535 0.2690 0.2541 0.0734 -0.0778 -0.0763 748 GLU A CA 5745 C C . GLU A 755 ? 0.3451 0.2654 0.2448 0.0796 -0.0677 -0.0670 748 GLU A C 5746 O O . GLU A 755 ? 0.3158 0.2527 0.2521 0.0753 -0.0749 -0.0501 748 GLU A O 5747 C CB . GLU A 755 ? 0.3804 0.3025 0.2582 0.0778 -0.0645 -0.0851 748 GLU A CB 5748 C CG . GLU A 755 ? 0.4429 0.3359 0.3129 0.0851 -0.0935 -0.1106 748 GLU A CG 5749 C CD . GLU A 755 ? 0.6105 0.3973 0.3621 0.1018 -0.0715 -0.1161 748 GLU A CD 5750 O OE1 . GLU A 755 ? 0.6663 0.3750 0.4299 0.0602 -0.1010 -0.1669 748 GLU A OE1 5751 O OE2 . GLU A 755 ? 0.6840 0.4905 0.3830 0.1337 -0.0100 -0.0931 748 GLU A OE2 5752 N N . VAL A 756 ? 0.3413 0.2645 0.2370 0.0797 -0.0592 -0.0618 749 VAL A N 5753 C CA . VAL A 756 ? 0.3397 0.2555 0.2249 0.0882 -0.0422 -0.0590 749 VAL A CA 5754 C C . VAL A 756 ? 0.3548 0.2629 0.2311 0.0812 -0.0502 -0.0502 749 VAL A C 5755 O O . VAL A 756 ? 0.3592 0.2663 0.2057 0.0671 -0.0441 -0.0262 749 VAL A O 5756 C CB . VAL A 756 ? 0.3398 0.2468 0.2169 0.0927 -0.0399 -0.0620 749 VAL A CB 5757 C CG1 . VAL A 756 ? 0.2993 0.2322 0.2202 0.1026 -0.0238 -0.0602 749 VAL A CG1 5758 C CG2 . VAL A 756 ? 0.2892 0.2542 0.1838 0.1158 -0.0482 -0.0684 749 VAL A CG2 5759 N N . ALA A 757 ? 0.3641 0.2461 0.2477 0.0749 -0.0504 -0.0669 750 ALA A N 5760 C CA . ALA A 757 ? 0.3800 0.2661 0.2712 0.0824 -0.0854 -0.0839 750 ALA A CA 5761 C C . ALA A 757 ? 0.4127 0.2816 0.3276 0.0887 -0.0926 -0.0812 750 ALA A C 5762 O O . ALA A 757 ? 0.4390 0.2949 0.3950 0.0877 -0.1054 -0.0775 750 ALA A O 5763 C CB . ALA A 757 ? 0.3729 0.2555 0.2333 0.0896 -0.0709 -0.0892 750 ALA A CB 5764 O OXT . ALA A 757 ? 0.3969 0.2924 0.3269 0.0767 -0.1350 -0.0952 750 ALA A OXT 5765 ZN ZN . ZN B . ? 0.2200 0.2192 0.2696 0.0175 0.0127 -0.0165 801 ZN A ZN 5766 ZN ZN . ZN C . ? 0.2617 0.2611 0.2869 0.0266 0.0083 -0.0217 802 ZN A ZN 5767 CA CA . CA D . ? 0.2046 0.2193 0.2036 0.0027 0.0008 -0.0156 803 CA A CA 5768 CL CL . CL E . ? 0.3051 0.2914 0.3200 0.0134 -0.0065 -0.0472 804 CL A CL 5769 C C1 . NAG F . ? 0.4633 0.3555 0.5003 0.0426 0.0730 0.0158 805 NAG A C1 5770 C C2 . NAG F . ? 0.5295 0.4031 0.6048 0.0278 0.0839 -0.0037 805 NAG A C2 5771 C C3 . NAG F . ? 0.5142 0.4217 0.6330 0.0237 0.0948 0.0067 805 NAG A C3 5772 C C4 . NAG F . ? 0.5382 0.4056 0.6064 0.0265 0.0978 0.0351 805 NAG A C4 5773 C C5 . NAG F . ? 0.5098 0.4245 0.5346 0.0296 0.0758 0.0537 805 NAG A C5 5774 C C6 . NAG F . ? 0.5068 0.4527 0.5192 0.0129 0.0996 0.1015 805 NAG A C6 5775 C C7 . NAG F . ? 0.6039 0.4750 0.6504 0.0669 0.0716 -0.0398 805 NAG A C7 5776 C C8 . NAG F . ? 0.6083 0.4710 0.6421 0.0685 0.0964 -0.0829 805 NAG A C8 5777 N N2 . NAG F . ? 0.5838 0.4193 0.6180 0.0422 0.0936 -0.0522 805 NAG A N2 5778 O O3 . NAG F . ? 0.4727 0.4532 0.7025 0.0030 0.1271 -0.0095 805 NAG A O3 5779 O O4 . NAG F . ? 0.5780 0.4006 0.6741 0.0456 0.1060 0.0160 805 NAG A O4 5780 O O5 . NAG F . ? 0.4862 0.3495 0.4724 0.0435 0.0704 0.0630 805 NAG A O5 5781 O O6 . NAG F . ? 0.5328 0.5308 0.4809 -0.0046 0.1058 0.1684 805 NAG A O6 5782 O O7 . NAG F . ? 0.6743 0.4891 0.6825 0.0799 0.0494 -0.0485 805 NAG A O7 5783 C C1 . NAG G . ? 0.6387 0.4777 0.7368 0.0323 0.1207 0.0580 806 NAG A C1 5784 C C2 . NAG G . ? 0.6440 0.5146 0.7661 0.0236 0.1298 0.0481 806 NAG A C2 5785 C C3 . NAG G . ? 0.7022 0.5588 0.8134 0.0271 0.1365 0.0743 806 NAG A C3 5786 C C4 . NAG G . ? 0.7407 0.5663 0.8260 0.0403 0.1344 0.0657 806 NAG A C4 5787 C C5 . NAG G . ? 0.7494 0.5459 0.8160 0.0270 0.1384 0.0628 806 NAG A C5 5788 C C6 . NAG G . ? 0.7809 0.5601 0.8150 0.0261 0.1332 0.0454 806 NAG A C6 5789 C C7 . NAG G . ? 0.5707 0.5052 0.6882 0.0287 0.1217 0.0662 806 NAG A C7 5790 C C8 . NAG G . ? 0.5364 0.5031 0.6372 0.0070 0.1704 0.0189 806 NAG A C8 5791 N N2 . NAG G . ? 0.5633 0.4713 0.7434 0.0249 0.1403 0.0679 806 NAG A N2 5792 O O3 . NAG G . ? 0.7003 0.6277 0.8536 -0.0134 0.1356 0.0603 806 NAG A O3 5793 O O4 . NAG G . ? 0.7719 0.5917 0.8284 0.0463 0.1433 0.0747 806 NAG A O4 5794 O O5 . NAG G . ? 0.6852 0.5052 0.7895 0.0311 0.1257 0.0496 806 NAG A O5 5795 O O6 . NAG G . ? 0.8077 0.5275 0.7850 -0.0246 0.1697 0.0215 806 NAG A O6 5796 O O7 . NAG G . ? 0.5712 0.4611 0.6875 0.0559 0.1283 0.0957 806 NAG A O7 5797 C C1 . NAG H . ? 0.6099 0.5955 0.6862 -0.0269 -0.0826 -0.1948 807 NAG A C1 5798 C C2 . NAG H . ? 0.6045 0.6490 0.7257 -0.0364 -0.0759 -0.1942 807 NAG A C2 5799 C C3 . NAG H . ? 0.6559 0.7017 0.7727 -0.0311 -0.0806 -0.2063 807 NAG A C3 5800 C C4 . NAG H . ? 0.7311 0.7617 0.7911 -0.0172 -0.0654 -0.2133 807 NAG A C4 5801 C C5 . NAG H . ? 0.7392 0.7531 0.7958 -0.0080 -0.0675 -0.2140 807 NAG A C5 5802 C C6 . NAG H . ? 0.7993 0.7856 0.8072 0.0103 -0.0555 -0.2038 807 NAG A C6 5803 C C7 . NAG H . ? 0.5782 0.6691 0.7202 -0.0610 -0.0762 -0.1704 807 NAG A C7 5804 C C8 . NAG H . ? 0.5683 0.6702 0.7263 -0.0699 -0.0832 -0.1747 807 NAG A C8 5805 N N2 . NAG H . ? 0.5243 0.6439 0.7063 -0.0699 -0.0942 -0.1794 807 NAG A N2 5806 O O3 . NAG H . ? 0.5900 0.7174 0.8145 -0.0711 -0.1112 -0.1919 807 NAG A O3 5807 O O4 . NAG H . ? 0.7841 0.8109 0.8117 -0.0306 -0.0636 -0.2234 807 NAG A O4 5808 O O5 . NAG H . ? 0.6782 0.6976 0.7219 0.0100 -0.0511 -0.2165 807 NAG A O5 5809 O O6 . NAG H . ? 0.8324 0.7632 0.8899 0.0306 -0.0638 -0.1594 807 NAG A O6 5810 O O7 . NAG H . ? 0.5988 0.7138 0.7334 -0.0811 -0.0651 -0.1725 807 NAG A O7 5811 C C1 . NAG I . ? 0.6290 0.5142 0.5023 0.0659 0.0464 -0.2381 808 NAG A C1 5812 C C2 . NAG I . ? 0.6631 0.5424 0.5354 0.0820 0.0554 -0.2517 808 NAG A C2 5813 C C3 . NAG I . ? 0.6830 0.5563 0.5573 0.0817 0.0411 -0.2652 808 NAG A C3 5814 C C4 . NAG I . ? 0.7033 0.5805 0.5825 0.0768 0.0473 -0.2664 808 NAG A C4 5815 C C5 . NAG I . ? 0.6693 0.5651 0.5415 0.0686 0.0420 -0.2518 808 NAG A C5 5816 C C6 . NAG I . ? 0.6487 0.5569 0.5262 0.0711 0.0370 -0.2601 808 NAG A C6 5817 C C7 . NAG I . ? 0.7140 0.5843 0.6031 0.0603 0.0517 -0.1891 808 NAG A C7 5818 C C8 . NAG I . ? 0.7099 0.5757 0.6304 0.0625 0.0599 -0.1933 808 NAG A C8 5819 N N2 . NAG I . ? 0.6863 0.5556 0.5948 0.0634 0.0563 -0.2233 808 NAG A N2 5820 O O3 . NAG I . ? 0.6556 0.5908 0.4866 0.0712 0.0481 -0.2807 808 NAG A O3 5821 O O4 . NAG I . ? 0.8084 0.6705 0.6527 0.0879 0.0084 -0.2524 808 NAG A O4 5822 O O5 . NAG I . ? 0.6335 0.5178 0.4947 0.0775 0.0719 -0.2534 808 NAG A O5 5823 O O6 . NAG I . ? 0.6645 0.5423 0.5502 0.0371 0.0291 -0.2692 808 NAG A O6 5824 O O7 . NAG I . ? 0.7628 0.6117 0.5886 0.0560 0.0469 -0.1851 808 NAG A O7 5825 C C1 . NAG J . ? 0.8639 0.7290 0.7242 0.0611 -0.0125 -0.2592 809 NAG A C1 5826 C C2 . NAG J . ? 0.9044 0.7642 0.7422 0.0730 -0.0216 -0.2495 809 NAG A C2 5827 C C3 . NAG J . ? 0.9187 0.7843 0.7889 0.0647 -0.0197 -0.2393 809 NAG A C3 5828 C C4 . NAG J . ? 0.9338 0.7887 0.7974 0.0724 -0.0114 -0.2409 809 NAG A C4 5829 C C5 . NAG J . ? 0.9151 0.7684 0.7901 0.0766 -0.0060 -0.2495 809 NAG A C5 5830 C C6 . NAG J . ? 0.9230 0.7751 0.7959 0.0919 0.0030 -0.2433 809 NAG A C6 5831 C C7 . NAG J . ? 0.8928 0.7823 0.6794 0.0566 -0.0135 -0.2497 809 NAG A C7 5832 C C8 . NAG J . ? 0.8800 0.7561 0.6273 0.0445 -0.0246 -0.2677 809 NAG A C8 5833 N N2 . NAG J . ? 0.9054 0.7669 0.7047 0.0623 -0.0218 -0.2518 809 NAG A N2 5834 O O3 . NAG J . ? 0.9463 0.8055 0.7705 0.0595 -0.0252 -0.2398 809 NAG A O3 5835 O O4 . NAG J . ? 0.9398 0.8000 0.8304 0.0610 -0.0120 -0.2266 809 NAG A O4 5836 O O5 . NAG J . ? 0.8929 0.7493 0.7410 0.0843 -0.0134 -0.2628 809 NAG A O5 5837 O O6 . NAG J . ? 0.9250 0.7540 0.7907 0.1108 0.0099 -0.2562 809 NAG A O6 5838 O O7 . NAG J . ? 0.9060 0.8042 0.6494 0.0439 -0.0093 -0.2490 809 NAG A O7 5839 C C1 . NAG K . ? 1.0346 1.0357 0.7525 0.0596 0.1159 -0.0124 810 NAG A C1 5840 C C2 . NAG K . ? 1.1247 1.0679 0.8239 0.0731 0.1229 -0.0209 810 NAG A C2 5841 C C3 . NAG K . ? 1.1329 1.0944 0.8319 0.0706 0.1165 -0.0271 810 NAG A C3 5842 C C4 . NAG K . ? 1.1467 1.1106 0.8446 0.0712 0.1101 -0.0341 810 NAG A C4 5843 C C5 . NAG K . ? 1.1306 1.1056 0.8399 0.0671 0.1072 -0.0370 810 NAG A C5 5844 C C6 . NAG K . ? 1.1463 1.1062 0.8530 0.0639 0.0952 -0.0595 810 NAG A C6 5845 C C7 . NAG K . ? 1.1592 1.0759 0.8678 0.0357 0.1453 -0.0191 810 NAG A C7 5846 C C8 . NAG K . ? 1.1697 1.0709 0.8798 0.0311 0.1351 -0.0341 810 NAG A C8 5847 N N2 . NAG K . ? 1.1453 1.0716 0.8394 0.0501 0.1338 -0.0262 810 NAG A N2 5848 O O3 . NAG K . ? 1.1351 1.0935 0.8335 0.0807 0.1111 -0.0220 810 NAG A O3 5849 O O4 . NAG K . ? 1.1550 1.1309 0.8624 0.0623 0.1043 -0.0339 810 NAG A O4 5850 O O5 . NAG K . ? 1.1224 1.0714 0.7977 0.0661 0.1125 -0.0298 810 NAG A O5 5851 O O6 . NAG K . ? 1.1268 1.1049 0.8801 0.0602 0.0877 -0.0731 810 NAG A O6 5852 O O7 . NAG K . ? 1.1653 1.0658 0.8728 0.0286 0.1484 -0.0123 810 NAG A O7 5853 C C1 . NAG L . ? 0.3911 0.5052 0.6068 0.1063 -0.0448 -0.1078 811 NAG A C1 5854 C C2 . NAG L . ? 0.3441 0.5318 0.5996 0.1176 -0.0582 -0.1137 811 NAG A C2 5855 C C3 . NAG L . ? 0.3760 0.6062 0.6458 0.1618 -0.0400 -0.1285 811 NAG A C3 5856 C C4 . NAG L . ? 0.3668 0.6162 0.6665 0.1527 -0.0452 -0.1327 811 NAG A C4 5857 C C5 . NAG L . ? 0.4205 0.5965 0.6764 0.1137 -0.0386 -0.1277 811 NAG A C5 5858 C C6 . NAG L . ? 0.4538 0.5851 0.6751 0.0804 -0.0265 -0.1183 811 NAG A C6 5859 C C7 . NAG L . ? 0.3037 0.3896 0.4810 0.0745 -0.0420 -0.1103 811 NAG A C7 5860 C C8 . NAG L . ? 0.3091 0.3502 0.4425 0.0650 -0.0277 -0.1169 811 NAG A C8 5861 N N2 . NAG L . ? 0.3554 0.4514 0.5589 0.1151 -0.0530 -0.1070 811 NAG A N2 5862 O O3 . NAG L . ? 0.3493 0.6513 0.6266 0.2023 -0.0347 -0.1605 811 NAG A O3 5863 O O4 . NAG L . ? 0.3712 0.6418 0.7035 0.2294 -0.0442 -0.1616 811 NAG A O4 5864 O O5 . NAG L . ? 0.4505 0.5706 0.6444 0.0915 -0.0569 -0.1244 811 NAG A O5 5865 O O6 . NAG L . ? 0.4369 0.5858 0.6969 0.0197 0.0026 -0.0959 811 NAG A O6 5866 O O7 . NAG L . ? 0.2544 0.3875 0.4507 0.0533 -0.0840 -0.1072 811 NAG A O7 5867 C C1 . NAG M . ? 0.4393 0.3640 0.3242 0.0862 -0.1421 -0.0907 812 NAG A C1 5868 C C2 . NAG M . ? 0.4606 0.3862 0.3283 0.0909 -0.1268 -0.0785 812 NAG A C2 5869 C C3 . NAG M . ? 0.4617 0.3872 0.3635 0.0982 -0.1469 -0.0838 812 NAG A C3 5870 C C4 . NAG M . ? 0.5056 0.4074 0.3497 0.1103 -0.1683 -0.0987 812 NAG A C4 5871 C C5 . NAG M . ? 0.4629 0.4241 0.3499 0.1025 -0.1960 -0.0892 812 NAG A C5 5872 C C6 . NAG M . ? 0.5263 0.4598 0.3386 0.1052 -0.1985 -0.0493 812 NAG A C6 5873 C C7 . NAG M . ? 0.4819 0.4266 0.3822 0.0861 -0.1018 -0.0465 812 NAG A C7 5874 C C8 . NAG M . ? 0.4029 0.4073 0.3437 0.0908 -0.0938 -0.0753 812 NAG A C8 5875 N N2 . NAG M . ? 0.4185 0.4004 0.3456 0.0937 -0.1154 -0.0571 812 NAG A N2 5876 O O3 . NAG M . ? 0.4901 0.3915 0.3426 0.1013 -0.1421 -0.0652 812 NAG A O3 5877 O O4 . NAG M . ? 0.5429 0.4376 0.4351 0.1103 -0.1712 -0.1225 812 NAG A O4 5878 O O5 . NAG M . ? 0.4579 0.4158 0.3491 0.1062 -0.1607 -0.0730 812 NAG A O5 5879 O O6 . NAG M . ? 0.5102 0.5038 0.3346 0.1457 -0.2279 -0.0099 812 NAG A O6 5880 O O7 . NAG M . ? 0.5764 0.5125 0.4343 0.0628 -0.1110 -0.0006 812 NAG A O7 5881 C C1 . NAG N . ? 0.6205 0.5067 0.4632 0.1216 -0.1662 -0.1442 813 NAG A C1 5882 C C2 . NAG N . ? 0.6532 0.5411 0.5151 0.1062 -0.1543 -0.1598 813 NAG A C2 5883 C C3 . NAG N . ? 0.6881 0.5777 0.5469 0.0997 -0.1374 -0.1704 813 NAG A C3 5884 C C4 . NAG N . ? 0.6843 0.6212 0.5698 0.1119 -0.1456 -0.1503 813 NAG A C4 5885 C C5 . NAG N . ? 0.6661 0.6219 0.5413 0.1278 -0.1602 -0.1353 813 NAG A C5 5886 C C6 . NAG N . ? 0.6774 0.6901 0.5678 0.1331 -0.1554 -0.1206 813 NAG A C6 5887 C C7 . NAG N . ? 0.6622 0.5920 0.5918 0.0625 -0.1481 -0.1274 813 NAG A C7 5888 C C8 . NAG N . ? 0.6266 0.5153 0.5560 0.0452 -0.1363 -0.1239 813 NAG A C8 5889 N N2 . NAG N . ? 0.6525 0.5669 0.5427 0.0819 -0.1530 -0.1599 813 NAG A N2 5890 O O3 . NAG N . ? 0.6838 0.5564 0.5195 0.1062 -0.1215 -0.2291 813 NAG A O3 5891 O O4 . NAG N . ? 0.6988 0.7356 0.5711 0.0830 -0.0978 -0.1055 813 NAG A O4 5892 O O5 . NAG N . ? 0.6130 0.4996 0.5114 0.1495 -0.1834 -0.1431 813 NAG A O5 5893 O O6 . NAG N . ? 0.6748 0.7136 0.6280 0.1580 -0.1480 -0.1496 813 NAG A O6 5894 O O7 . NAG N . ? 0.7005 0.6489 0.6258 0.0740 -0.1254 -0.1201 813 NAG A O7 5895 C C1 . NAG O . ? 0.3440 0.2507 0.3667 0.0342 -0.0666 -0.0462 814 NAG A C1 5896 C C2 . NAG O . ? 0.3486 0.2380 0.3777 0.0261 -0.0761 -0.0531 814 NAG A C2 5897 C C3 . NAG O . ? 0.4168 0.2831 0.4213 0.0422 -0.0927 -0.0353 814 NAG A C3 5898 C C4 . NAG O . ? 0.4621 0.3400 0.4446 0.0547 -0.0891 -0.0590 814 NAG A C4 5899 C C5 . NAG O . ? 0.4861 0.3509 0.4567 0.0552 -0.1030 -0.0610 814 NAG A C5 5900 C C6 . NAG O . ? 0.5214 0.4036 0.4774 0.0618 -0.0989 -0.1058 814 NAG A C6 5901 C C7 . NAG O . ? 0.2913 0.2506 0.2937 0.0018 -0.0571 -0.0418 814 NAG A C7 5902 C C8 . NAG O . ? 0.2380 0.2281 0.2242 0.0164 -0.0622 -0.0449 814 NAG A C8 5903 N N2 . NAG O . ? 0.2882 0.2398 0.3366 -0.0204 -0.0801 -0.0058 814 NAG A N2 5904 O O3 . NAG O . ? 0.3607 0.2915 0.3956 0.0518 -0.0822 -0.0694 814 NAG A O3 5905 O O4 . NAG O . ? 0.5066 0.3794 0.5163 0.0346 -0.0702 -0.0447 814 NAG A O4 5906 O O5 . NAG O . ? 0.4081 0.3012 0.3748 0.0529 -0.0979 -0.0944 814 NAG A O5 5907 O O6 . NAG O . ? 0.5434 0.4982 0.6054 0.0104 -0.1039 -0.1133 814 NAG A O6 5908 O O7 . NAG O . ? 0.2882 0.2568 0.2561 0.0162 -0.0523 -0.0200 814 NAG A O7 5909 C C1 . NAG P . ? 0.5292 0.4120 0.5556 0.0611 -0.0742 -0.0087 815 NAG A C1 5910 C C2 . NAG P . ? 0.6096 0.4531 0.5746 0.0831 -0.0787 -0.0102 815 NAG A C2 5911 C C3 . NAG P . ? 0.6155 0.4556 0.5732 0.0938 -0.0619 0.0150 815 NAG A C3 5912 C C4 . NAG P . ? 0.5976 0.4717 0.5808 0.0675 -0.0539 0.0100 815 NAG A C4 5913 C C5 . NAG P . ? 0.5721 0.4701 0.5965 0.0483 -0.0544 0.0186 815 NAG A C5 5914 C C6 . NAG P . ? 0.5776 0.5503 0.6194 0.0279 -0.0477 0.0420 815 NAG A C6 5915 C C7 . NAG P . ? 0.6712 0.5510 0.6431 0.0999 -0.0781 -0.0300 815 NAG A C7 5916 C C8 . NAG P . ? 0.6818 0.5098 0.6551 0.0888 -0.0840 -0.0309 815 NAG A C8 5917 N N2 . NAG P . ? 0.6141 0.4848 0.6020 0.1070 -0.0715 -0.0047 815 NAG A N2 5918 O O3 . NAG P . ? 0.6562 0.4183 0.4846 0.0777 -0.0531 0.0466 815 NAG A O3 5919 O O4 . NAG P . ? 0.5993 0.4999 0.6016 0.0558 -0.0385 0.0217 815 NAG A O4 5920 O O5 . NAG P . ? 0.5216 0.4109 0.5678 0.0240 -0.0590 -0.0067 815 NAG A O5 5921 O O6 . NAG P . ? 0.6074 0.6594 0.6651 -0.0144 -0.0083 0.0624 815 NAG A O6 5922 O O7 . NAG P . ? 0.7242 0.6405 0.6434 0.1188 -0.0686 -0.0248 815 NAG A O7 5923 C C1 . BMA Q . ? 0.6155 0.4837 0.6545 0.0214 -0.0646 0.0259 816 BMA A C1 5924 C C2 . BMA Q . ? 0.6076 0.5068 0.6714 0.0166 -0.0585 0.0277 816 BMA A C2 5925 C C3 . BMA Q . ? 0.6069 0.5239 0.7171 0.0102 -0.0438 0.0438 816 BMA A C3 5926 C C4 . BMA Q . ? 0.6020 0.5224 0.7260 0.0102 -0.0588 0.0151 816 BMA A C4 5927 C C5 . BMA Q . ? 0.6259 0.5335 0.7255 0.0158 -0.0661 0.0053 816 BMA A C5 5928 C C6 . BMA Q . ? 0.6115 0.5660 0.7466 -0.0044 -0.0589 0.0169 816 BMA A C6 5929 O O2 . BMA Q . ? 0.5779 0.5201 0.6227 0.0241 -0.0700 0.0806 816 BMA A O2 5930 O O3 . BMA Q . ? 0.5680 0.5348 0.7268 0.0065 -0.0331 0.0513 816 BMA A O3 5931 O O4 . BMA Q . ? 0.6001 0.5149 0.7478 0.0242 -0.0573 0.0091 816 BMA A O4 5932 O O5 . BMA Q . ? 0.5823 0.4853 0.7007 -0.0037 -0.0791 0.0295 816 BMA A O5 5933 O O6 . BMA Q . ? 0.6409 0.5419 0.7591 -0.0105 -0.0545 0.0565 816 BMA A O6 5934 C C1 . MAN R . ? 0.6463 0.5734 0.7668 -0.0073 -0.0348 0.0637 817 MAN A C1 5935 C C2 . MAN R . ? 0.6729 0.5650 0.7595 -0.0106 -0.0460 0.0646 817 MAN A C2 5936 C C3 . MAN R . ? 0.6936 0.5854 0.7889 -0.0041 -0.0440 0.0488 817 MAN A C3 5937 C C4 . MAN R . ? 0.7034 0.6185 0.8041 -0.0106 -0.0337 0.0278 817 MAN A C4 5938 C C5 . MAN R . ? 0.6781 0.6238 0.7795 -0.0106 -0.0207 0.0247 817 MAN A C5 5939 C C6 . MAN R . ? 0.6694 0.6292 0.7875 -0.0180 -0.0306 0.0215 817 MAN A C6 5940 O O2 . MAN R . ? 0.6585 0.5918 0.7428 -0.0227 -0.0547 0.0866 817 MAN A O2 5941 O O3 . MAN R . ? 0.7072 0.5955 0.8133 -0.0174 -0.0649 0.0561 817 MAN A O3 5942 O O4 . MAN R . ? 0.7354 0.6679 0.8148 0.0041 -0.0198 0.0042 817 MAN A O4 5943 O O5 . MAN R . ? 0.6347 0.5767 0.7580 -0.0252 -0.0358 0.0555 817 MAN A O5 5944 O O6 . MAN R . ? 0.6663 0.6627 0.7446 -0.0094 0.0065 0.0348 817 MAN A O6 5945 O O4 . 29C S . ? 0.7277 0.6636 0.7075 0.0224 -0.0363 -0.0331 818 29C A O4 5946 C C4 . 29C S . ? 0.7186 0.6868 0.6944 0.0047 -0.0001 -0.0233 818 29C A C4 5947 C C4A . 29C S . ? 0.7113 0.6618 0.6884 -0.0122 0.0111 -0.0403 818 29C A C4A 5948 N N3 . 29C S . ? 0.7347 0.7165 0.7320 -0.0174 0.0090 -0.0150 818 29C A N3 5949 C C8A . 29C S . ? 0.7081 0.6899 0.6989 -0.0213 0.0108 -0.0342 818 29C A C8A 5950 N N5 . 29C S . ? 0.6716 0.6199 0.6704 -0.0179 0.0080 -0.0676 818 29C A N5 5951 C C2 . 29C S . ? 0.7438 0.7330 0.7455 -0.0286 0.0112 -0.0071 818 29C A C2 5952 N N8 . 29C S . ? 0.7117 0.6523 0.6778 -0.0507 0.0118 -0.0490 818 29C A N8 5953 N N1 . 29C S . ? 0.7306 0.7292 0.7330 -0.0266 0.0221 -0.0201 818 29C A N1 5954 C C6 . 29C S . ? 0.6669 0.6092 0.6491 -0.0399 0.0210 -0.0553 818 29C A C6 5955 N N2 . 29C S . ? 0.7607 0.7423 0.7647 -0.0576 0.0014 0.0000 818 29C A N2 5956 C C7 . 29C S . ? 0.7015 0.6216 0.6602 -0.0553 0.0039 -0.0514 818 29C A C7 5957 C C9 . 29C S . ? 0.6632 0.5961 0.6053 -0.0269 0.0251 -0.0377 818 29C A C9 5958 N N10 . 29C S . ? 0.6474 0.6208 0.6014 -0.0530 0.0508 -0.0169 818 29C A N10 5959 C CBP . 29C S . ? 0.6481 0.6554 0.6395 -0.0490 0.0088 -0.0047 818 29C A CBP 5960 C CAN . 29C S . ? 0.6612 0.6615 0.6561 -0.0266 0.0168 -0.0063 818 29C A CAN 5961 C CAO . 29C S . ? 0.6462 0.6626 0.6559 -0.0410 0.0011 -0.0068 818 29C A CAO 5962 C CAP . 29C S . ? 0.6433 0.6839 0.6828 -0.0207 -0.0101 -0.0051 818 29C A CAP 5963 C CAQ . 29C S . ? 0.6760 0.6866 0.6711 -0.0240 -0.0076 -0.0149 818 29C A CAQ 5964 C CBQ . 29C S . ? 0.6857 0.6980 0.6802 -0.0210 -0.0147 -0.0175 818 29C A CBQ 5965 C CBN . 29C S . ? 0.6771 0.7036 0.6725 -0.0142 -0.0254 -0.0016 818 29C A CBN 5966 O OAH . 29C S . ? 0.7172 0.7300 0.6884 -0.0179 -0.0020 -0.0316 818 29C A OAH 5967 N NBG . 29C S . ? 0.6649 0.6774 0.6600 -0.0248 -0.0266 0.0101 818 29C A NBG 5968 C CBX . 29C S . ? 0.5881 0.6164 0.6334 -0.0424 -0.0060 0.0271 818 29C A CBX 5969 C CBK . 29C S . ? 0.5896 0.6199 0.6087 -0.0398 -0.0019 0.0094 818 29C A CBK 5970 O OAE . 29C S . ? 0.5722 0.5852 0.6053 -0.0598 0.0078 0.0088 818 29C A OAE 5971 C CAX . 29C S . ? 0.5558 0.5385 0.6107 -0.0145 0.0015 0.0253 818 29C A CAX 5972 C CAU . 29C S . ? 0.4426 0.5140 0.5608 -0.0561 0.0425 0.0173 818 29C A CAU 5973 C CBM . 29C S . ? 0.3984 0.4456 0.5529 -0.0357 0.0025 -0.0202 818 29C A CBM 5974 O OAG . 29C S . ? 0.3825 0.4446 0.6147 -0.0585 0.0316 -0.0082 818 29C A OAG 5975 O OAL . 29C S . ? 0.4964 0.6130 0.5842 -0.0673 0.0066 -0.0094 818 29C A OAL 5976 N NBF . 29C S . ? 0.3290 0.4019 0.4679 -0.0350 0.0052 -0.0392 818 29C A NBF 5977 C CBW . 29C S . ? 0.3436 0.3746 0.3874 -0.0321 -0.0150 -0.0575 818 29C A CBW 5978 C CBJ . 29C S . ? 0.3653 0.4436 0.3951 0.0041 -0.0145 -0.0737 818 29C A CBJ 5979 O OAK . 29C S . ? 0.4218 0.4599 0.4022 0.0422 -0.0603 -0.0672 818 29C A OAK 5980 C CAW . 29C S . ? 0.2936 0.2826 0.3419 -0.0443 -0.0056 -0.0349 818 29C A CAW 5981 C CAT . 29C S . ? 0.2451 0.2700 0.2732 -0.0086 0.0226 -0.0587 818 29C A CAT 5982 C CBL . 29C S . ? 0.2654 0.2365 0.2644 0.0094 -0.0183 -0.0044 818 29C A CBL 5983 O OAF . 29C S . ? 0.2781 0.2474 0.2937 0.0474 0.0032 -0.0467 818 29C A OAF 5984 O OAD . 29C S . ? 0.2697 0.5396 0.4050 -0.0154 -0.0205 -0.1165 818 29C A OAD 5985 N N . 29C S . ? 0.2449 0.2509 0.2471 0.0199 -0.0013 -0.0132 818 29C A N 5986 C CA . 29C S . ? 0.2440 0.2410 0.2395 0.0172 -0.0052 -0.0292 818 29C A CA 5987 C C . 29C S . ? 0.2454 0.2380 0.2354 0.0161 -0.0104 -0.0223 818 29C A C 5988 O O . 29C S . ? 0.2631 0.2225 0.2280 0.0229 -0.0156 -0.0191 818 29C A O 5989 C CB . 29C S . ? 0.2407 0.2314 0.2296 0.0298 0.0000 -0.0250 818 29C A CB 5990 C CG . 29C S . ? 0.2526 0.2421 0.2682 0.0346 -0.0073 -0.0267 818 29C A CG 5991 C CD . 29C S . ? 0.2699 0.2769 0.3111 0.0260 -0.0168 -0.0345 818 29C A CD 5992 O OE2 . 29C S . ? 0.2933 0.2906 0.3255 -0.0201 -0.0008 -0.0409 818 29C A OE2 5993 O OE1 . 29C S . ? 0.2211 0.2698 0.3111 0.0154 -0.0153 -0.0614 818 29C A OE1 5994 O OXT . 29C S . ? 0.2542 0.2515 0.2187 0.0170 -0.0198 -0.0336 818 29C A OXT 5995 O O . HOH T . ? 0.1945 0.1949 0.1725 0.0193 -0.0138 0.0203 901 HOH A O 5996 O O . HOH T . ? 0.2136 0.2177 0.1851 0.0110 0.0238 -0.0273 902 HOH A O 5997 O O . HOH T . ? 0.2340 0.2339 0.1693 0.0620 -0.0508 0.0114 903 HOH A O 5998 O O . HOH T . ? 0.3185 0.2045 0.2526 0.0316 0.0426 -0.0218 904 HOH A O 5999 O O . HOH T . ? 0.1707 0.1798 0.2101 0.0677 0.0531 -0.0173 905 HOH A O 6000 O O . HOH T . ? 0.2297 0.1910 0.2186 0.0315 -0.0122 -0.0096 906 HOH A O 6001 O O . HOH T . ? 0.1214 0.1711 0.2214 0.0565 0.0064 -0.0087 907 HOH A O 6002 O O . HOH T . ? 0.1656 0.2376 0.2575 0.0267 0.0164 -0.0357 908 HOH A O 6003 O O . HOH T . ? 0.1313 0.2138 0.2185 0.0451 0.0110 -0.0262 909 HOH A O 6004 O O . HOH T . ? 0.1659 0.2190 0.1623 -0.0264 0.0111 0.0122 910 HOH A O 6005 O O . HOH T . ? 0.2022 0.2145 0.2298 0.0453 0.0198 0.0148 911 HOH A O 6006 O O . HOH T . ? 0.2604 0.2000 0.1876 0.0548 0.0241 0.0539 912 HOH A O 6007 O O . HOH T . ? 0.2498 0.2064 0.3207 0.0065 0.0545 0.0347 913 HOH A O 6008 O O . HOH T . ? 0.2691 0.2183 0.2716 -0.0226 -0.0310 -0.0376 914 HOH A O 6009 O O . HOH T . ? 0.2434 0.2314 0.2102 0.0381 0.0529 0.0235 915 HOH A O 6010 O O . HOH T . ? 0.1930 0.2165 0.2034 -0.0076 0.0482 -0.0163 916 HOH A O 6011 O O . HOH T . ? 0.2252 0.1885 0.2486 0.0039 0.0017 -0.0122 917 HOH A O 6012 O O . HOH T . ? 0.2804 0.1998 0.3000 0.0617 0.0727 -0.0511 918 HOH A O 6013 O O . HOH T . ? 0.2209 0.1738 0.2006 0.0079 -0.0043 -0.0168 919 HOH A O 6014 O O . HOH T . ? 0.3005 0.1745 0.1928 0.0458 0.0235 0.0376 920 HOH A O 6015 O O . HOH T . ? 0.2758 0.2277 0.2309 0.0258 -0.0188 -0.0305 921 HOH A O 6016 O O . HOH T . ? 0.3049 0.1748 0.2426 0.0487 -0.0824 -0.0475 922 HOH A O 6017 O O . HOH T . ? 0.2166 0.1878 0.3291 -0.0190 -0.0023 0.0144 923 HOH A O 6018 O O . HOH T . ? 0.2798 0.2246 0.2327 0.0099 0.0022 -0.0335 924 HOH A O 6019 O O . HOH T . ? 0.2525 0.2640 0.2386 0.0075 0.0729 -0.1110 925 HOH A O 6020 O O . HOH T . ? 0.2588 0.2389 0.3038 0.0484 -0.0873 -0.0704 926 HOH A O 6021 O O . HOH T . ? 0.2992 0.2184 0.1979 -0.0082 0.0441 0.0152 927 HOH A O 6022 O O . HOH T . ? 0.2664 0.2296 0.1602 -0.0401 0.0303 0.0297 928 HOH A O 6023 O O . HOH T . ? 0.2805 0.2658 0.3141 0.0654 0.1410 -0.0207 929 HOH A O 6024 O O . HOH T . ? 0.2421 0.2743 0.2503 0.0044 0.0179 -0.0486 930 HOH A O 6025 O O . HOH T . ? 0.2124 0.3026 0.2976 -0.0285 0.0477 -0.0442 931 HOH A O 6026 O O . HOH T . ? 0.2324 0.2256 0.1978 0.0252 0.0073 -0.0135 932 HOH A O 6027 O O . HOH T . ? 0.2869 0.2411 0.4117 0.0440 -0.0347 -0.0211 933 HOH A O 6028 O O . HOH T . ? 0.2465 0.2810 0.2042 0.0464 0.0045 0.0432 934 HOH A O 6029 O O . HOH T . ? 0.3067 0.3009 0.1230 0.0970 -0.0176 -0.0785 935 HOH A O 6030 O O . HOH T . ? 0.2564 0.2504 0.2020 0.0518 0.0373 -0.0270 936 HOH A O 6031 O O . HOH T . ? 0.2296 0.1524 0.2960 0.0389 -0.0229 0.0020 937 HOH A O 6032 O O . HOH T . ? 0.2393 0.2501 0.2402 0.0079 0.0065 -0.0355 938 HOH A O 6033 O O . HOH T . ? 0.3361 0.2732 0.1321 0.1013 -0.0685 -0.0609 939 HOH A O 6034 O O . HOH T . ? 0.2962 0.2795 0.3576 0.0879 0.0351 0.0083 940 HOH A O 6035 O O . HOH T . ? 0.2353 0.2235 0.2286 0.0123 -0.0378 -0.0499 941 HOH A O 6036 O O . HOH T . ? 0.2463 0.2967 0.2899 -0.0687 0.0265 0.0022 942 HOH A O 6037 O O . HOH T . ? 0.2572 0.2481 0.3544 -0.0001 0.0219 -0.0359 943 HOH A O 6038 O O . HOH T . ? 0.2677 0.1950 0.2830 0.0023 0.0227 -0.0429 944 HOH A O 6039 O O . HOH T . ? 0.3046 0.1602 0.2706 0.0197 -0.0651 -0.0550 945 HOH A O 6040 O O . HOH T . ? 0.2839 0.2274 0.3004 0.0204 -0.0058 -0.0189 946 HOH A O 6041 O O . HOH T . ? 0.2016 0.2422 0.1625 -0.0284 0.0426 -0.0467 947 HOH A O 6042 O O . HOH T . ? 0.2227 0.2748 0.3684 0.0186 0.0682 0.0027 948 HOH A O 6043 O O . HOH T . ? 0.2198 0.2352 0.2329 0.0047 -0.0044 -0.0290 949 HOH A O 6044 O O . HOH T . ? 0.2045 0.2950 0.2677 -0.0287 0.0384 0.0295 950 HOH A O 6045 O O . HOH T . ? 0.2705 0.2542 0.2449 0.0552 0.0128 -0.0788 951 HOH A O 6046 O O . HOH T . ? 0.2858 0.3232 0.2729 -0.0944 0.0130 -0.1191 952 HOH A O 6047 O O . HOH T . ? 0.3925 0.3710 0.2424 0.0426 0.0153 -0.0670 953 HOH A O 6048 O O . HOH T . ? 0.1960 0.2447 0.2379 0.0108 -0.0012 -0.0131 954 HOH A O 6049 O O . HOH T . ? 0.2805 0.2261 0.2052 0.0589 -0.0012 -0.0325 955 HOH A O 6050 O O . HOH T . ? 0.2371 0.2728 0.2229 0.0168 0.0355 -0.0779 956 HOH A O 6051 O O . HOH T . ? 0.2269 0.2166 0.1650 0.0136 -0.0015 -0.0253 957 HOH A O 6052 O O . HOH T . ? 0.2060 0.2536 0.2469 -0.0085 -0.0408 0.0629 958 HOH A O 6053 O O . HOH T . ? 0.3567 0.2755 0.1657 0.1325 -0.0401 0.0033 959 HOH A O 6054 O O . HOH T . ? 0.1647 0.2183 0.1815 -0.0018 -0.0517 -0.0356 960 HOH A O 6055 O O . HOH T . ? 0.2773 0.3025 0.2776 -0.0206 -0.0267 -0.0051 961 HOH A O 6056 O O . HOH T . ? 0.2001 0.2414 0.1995 0.0414 -0.0012 -0.0545 962 HOH A O 6057 O O . HOH T . ? 0.3674 0.2153 0.1860 0.0768 -0.0032 -0.0036 963 HOH A O 6058 O O . HOH T . ? 0.3096 0.2496 0.2793 0.0510 0.0557 0.0334 964 HOH A O 6059 O O . HOH T . ? 0.2378 0.2122 0.2217 0.0421 0.0390 0.0424 965 HOH A O 6060 O O . HOH T . ? 0.2782 0.2923 0.2146 0.0114 -0.0140 -0.0383 966 HOH A O 6061 O O . HOH T . ? 0.2247 0.3166 0.1978 0.0781 0.0539 -0.0031 967 HOH A O 6062 O O . HOH T . ? 0.2480 0.2425 0.1959 0.0614 -0.0131 -0.0525 968 HOH A O 6063 O O . HOH T . ? 0.2235 0.1961 0.3748 0.0135 0.0556 -0.0097 969 HOH A O 6064 O O . HOH T . ? 0.2780 0.3430 0.3585 0.0577 -0.1209 -0.0084 970 HOH A O 6065 O O . HOH T . ? 0.2456 0.2270 0.2833 -0.0353 0.0264 -0.0580 971 HOH A O 6066 O O . HOH T . ? 0.4549 0.3173 0.2263 0.0745 0.0145 0.0139 972 HOH A O 6067 O O . HOH T . ? 0.2950 0.2876 0.2733 0.0839 -0.0779 -0.0487 973 HOH A O 6068 O O . HOH T . ? 0.2676 0.2346 0.2639 0.0715 0.0157 -0.0549 974 HOH A O 6069 O O . HOH T . ? 0.2245 0.2818 0.2826 -0.1236 0.0135 0.0165 975 HOH A O 6070 O O . HOH T . ? 0.2894 0.3112 0.2224 0.1190 0.0415 -0.0643 976 HOH A O 6071 O O . HOH T . ? 0.2881 0.2946 0.3579 0.0195 -0.0913 0.0105 977 HOH A O 6072 O O . HOH T . ? 0.2531 0.4154 0.3979 0.0238 -0.0248 -0.0076 978 HOH A O 6073 O O . HOH T . ? 0.1869 0.2893 0.3775 0.0269 0.0445 -0.0478 979 HOH A O 6074 O O . HOH T . ? 0.3169 0.2253 0.2533 0.0491 0.0108 0.0059 980 HOH A O 6075 O O . HOH T . ? 0.3271 0.3138 0.1440 0.0515 -0.0762 -0.0449 981 HOH A O 6076 O O . HOH T . ? 0.4489 0.2737 0.2359 0.0609 -0.0004 -0.1025 982 HOH A O 6077 O O . HOH T . ? 0.3845 0.3475 0.2137 0.0256 -0.0255 0.0284 983 HOH A O 6078 O O . HOH T . ? 0.3483 0.2567 0.2762 0.0774 0.0192 -0.0266 984 HOH A O 6079 O O . HOH T . ? 0.2501 0.2521 0.2283 0.0261 0.0430 -0.0271 985 HOH A O 6080 O O . HOH T . ? 0.2953 0.3379 0.4018 -0.0058 0.0019 0.0051 986 HOH A O 6081 O O . HOH T . ? 0.2617 0.2812 0.2318 0.0784 -0.0524 -0.0136 987 HOH A O 6082 O O . HOH T . ? 0.2917 0.3642 0.5222 -0.0930 0.0359 0.0561 988 HOH A O 6083 O O . HOH T . ? 0.3736 0.2546 0.2547 0.0343 0.0607 -0.0209 989 HOH A O 6084 O O . HOH T . ? 0.3391 0.3098 0.3253 0.0629 0.0043 -0.0259 990 HOH A O 6085 O O . HOH T . ? 0.1879 0.3049 0.3147 0.0271 -0.0077 -0.0651 991 HOH A O 6086 O O . HOH T . ? 0.2478 0.2617 0.2626 -0.0023 -0.0961 0.0235 992 HOH A O 6087 O O . HOH T . ? 0.2759 0.3863 0.3196 0.0903 -0.0795 -0.0181 993 HOH A O 6088 O O . HOH T . ? 0.3655 0.2831 0.2157 -0.0593 0.0008 -0.0181 994 HOH A O 6089 O O . HOH T . ? 0.2722 0.2229 0.2713 -0.0745 -0.0167 -0.0716 995 HOH A O 6090 O O . HOH T . ? 0.3222 0.4167 0.2366 0.1452 -0.0913 -0.0322 996 HOH A O 6091 O O . HOH T . ? 0.2576 0.3921 0.3304 0.0765 -0.0091 0.0226 997 HOH A O 6092 O O . HOH T . ? 0.3393 0.2014 0.3092 0.0631 -0.1106 0.0210 998 HOH A O 6093 O O . HOH T . ? 0.4531 0.3550 0.2399 0.1674 -0.0667 0.0273 999 HOH A O 6094 O O . HOH T . ? 0.2760 0.2568 0.2045 0.0656 0.0141 -0.0337 1000 HOH A O 6095 O O . HOH T . ? 0.3012 0.3619 0.3166 0.0947 0.0467 -0.0335 1001 HOH A O 6096 O O . HOH T . ? 0.4102 0.4249 0.3622 0.1853 -0.0409 0.0020 1002 HOH A O 6097 O O . HOH T . ? 0.3629 0.2488 0.2515 0.0057 0.0504 -0.0065 1003 HOH A O 6098 O O . HOH T . ? 0.2507 0.4103 0.2554 0.0328 -0.0493 -0.0568 1004 HOH A O 6099 O O . HOH T . ? 0.3149 0.2816 0.3658 -0.0652 0.0700 0.0289 1005 HOH A O 6100 O O . HOH T . ? 0.3414 0.3190 0.3625 0.0411 -0.0047 -0.0454 1006 HOH A O 6101 O O . HOH T . ? 0.3035 0.1669 0.2619 0.0139 0.0035 0.0139 1007 HOH A O 6102 O O . HOH T . ? 0.2829 0.2728 0.2151 -0.0036 -0.0212 -0.0017 1008 HOH A O 6103 O O . HOH T . ? 0.2159 0.2716 0.4457 0.0073 0.0553 -0.1037 1009 HOH A O 6104 O O . HOH T . ? 0.3567 0.3423 0.3516 0.0314 -0.0337 -0.0646 1010 HOH A O 6105 O O . HOH T . ? 0.1558 0.3458 0.3165 -0.0301 -0.0202 -0.0157 1011 HOH A O 6106 O O . HOH T . ? 0.3323 0.4992 0.2248 0.2925 -0.0130 -0.1328 1012 HOH A O 6107 O O . HOH T . ? 0.3075 0.3016 0.3862 0.0734 -0.0231 -0.0108 1013 HOH A O 6108 O O . HOH T . ? 0.4304 0.2920 0.2234 0.0948 0.0722 -0.0217 1014 HOH A O 6109 O O . HOH T . ? 0.3617 0.3636 0.2619 -0.0269 0.0063 -0.0263 1015 HOH A O 6110 O O . HOH T . ? 0.2577 0.3558 0.3841 0.0528 -0.0731 -0.0400 1016 HOH A O 6111 O O . HOH T . ? 0.3355 0.3214 0.3165 -0.0485 0.0002 0.0213 1017 HOH A O 6112 O O . HOH T . ? 0.2720 0.2722 0.2716 -0.0314 0.1010 -0.0209 1018 HOH A O 6113 O O . HOH T . ? 0.2702 0.3487 0.3543 0.0577 0.0130 -0.0901 1019 HOH A O 6114 O O . HOH T . ? 0.3780 0.4059 0.2946 0.0132 0.0534 -0.1442 1020 HOH A O 6115 O O . HOH T . ? 0.3385 0.4391 0.2932 0.0604 -0.0587 -0.0450 1021 HOH A O 6116 O O . HOH T . ? 0.2988 0.4196 0.3563 0.1179 -0.1608 0.0270 1022 HOH A O 6117 O O . HOH T . ? 0.3313 0.2529 0.3550 -0.0224 0.0835 -0.0630 1023 HOH A O 6118 O O . HOH T . ? 0.4037 0.3091 0.3472 0.0237 -0.0103 -0.0320 1024 HOH A O 6119 O O . HOH T . ? 0.4350 0.3592 0.2887 0.0753 -0.0662 -0.1330 1025 HOH A O 6120 O O . HOH T . ? 0.3453 0.4201 0.4906 0.0897 -0.1414 0.0811 1026 HOH A O 6121 O O . HOH T . ? 0.3837 0.2376 0.4214 -0.0496 0.0552 0.1748 1027 HOH A O 6122 O O . HOH T . ? 0.5348 0.2898 0.3228 0.1120 0.0077 0.1077 1028 HOH A O 6123 O O . HOH T . ? 0.2192 0.2522 0.3473 -0.0198 0.0371 0.0000 1029 HOH A O 6124 O O . HOH T . ? 0.3002 0.1570 0.2928 0.0197 -0.0053 -0.0692 1030 HOH A O 6125 O O . HOH T . ? 0.3158 0.2458 0.3113 0.0059 -0.0367 -0.0697 1031 HOH A O 6126 O O . HOH T . ? 0.3256 0.2593 0.2709 -0.0137 -0.0633 0.0198 1032 HOH A O 6127 O O . HOH T . ? 0.4910 0.2996 0.3418 0.0656 0.0971 0.0198 1033 HOH A O 6128 O O . HOH T . ? 0.1880 0.2875 0.3226 -0.0110 -0.0020 -0.0963 1034 HOH A O 6129 O O . HOH T . ? 0.3425 0.4393 0.6699 0.1909 -0.1062 -0.1804 1035 HOH A O 6130 O O . HOH T . ? 0.4358 0.3360 0.2348 -0.0749 0.0131 -0.0567 1036 HOH A O 6131 O O . HOH T . ? 0.4730 0.3545 0.2816 0.0945 0.0773 -0.1309 1037 HOH A O 6132 O O . HOH T . ? 0.2644 0.3297 0.4028 -0.0133 0.0577 0.0200 1038 HOH A O 6133 O O . HOH T . ? 0.3954 0.3010 0.3317 0.0567 0.0090 -0.0136 1039 HOH A O 6134 O O . HOH T . ? 0.3025 0.3509 0.2569 0.0295 0.0071 0.0521 1040 HOH A O 6135 O O . HOH T . ? 0.3518 0.4353 0.2658 0.0467 0.0108 0.0447 1041 HOH A O 6136 O O . HOH T . ? 0.5226 0.3724 0.2642 0.0043 0.0214 0.0415 1042 HOH A O 6137 O O . HOH T . ? 0.3645 0.2572 0.3134 0.0587 -0.0160 -0.1008 1043 HOH A O 6138 O O . HOH T . ? 0.3656 0.3203 0.2551 0.1183 0.0392 0.0310 1044 HOH A O 6139 O O . HOH T . ? 0.2484 0.3950 0.3258 0.0046 0.0857 0.0087 1045 HOH A O 6140 O O . HOH T . ? 0.2143 0.3806 0.3340 -0.0210 -0.0103 0.0368 1046 HOH A O 6141 O O . HOH T . ? 0.2819 0.4566 0.5750 -0.0240 -0.0163 -0.1364 1047 HOH A O 6142 O O . HOH T . ? 0.4261 0.3217 0.3120 0.0944 -0.0930 -0.0423 1048 HOH A O 6143 O O . HOH T . ? 0.5564 0.3409 0.3733 0.0315 -0.0467 -0.1892 1049 HOH A O 6144 O O . HOH T . ? 0.3299 0.2286 0.3817 0.0239 -0.0333 0.0907 1050 HOH A O 6145 O O . HOH T . ? 0.3832 0.2840 0.3660 0.0291 0.0193 -0.1334 1051 HOH A O 6146 O O . HOH T . ? 0.4591 0.3282 0.4018 -0.0764 -0.0067 -0.1425 1052 HOH A O 6147 O O . HOH T . ? 0.3063 0.4032 0.5751 0.0568 -0.0455 -0.2048 1053 HOH A O 6148 O O . HOH T . ? 0.3706 0.4785 0.4320 0.0647 0.0616 -0.0276 1054 HOH A O 6149 O O . HOH T . ? 0.3676 0.3604 0.4387 -0.0231 -0.1129 -0.1979 1055 HOH A O 6150 O O . HOH T . ? 0.4606 0.3115 0.3319 0.0699 -0.0405 0.0350 1056 HOH A O 6151 O O . HOH T . ? 0.3111 0.3919 0.3146 -0.0932 0.0580 -0.0669 1057 HOH A O 6152 O O . HOH T . ? 0.3763 0.3030 0.4017 -0.0935 -0.0085 0.0092 1058 HOH A O 6153 O O . HOH T . ? 0.3668 0.5902 0.6560 -0.1047 -0.0664 -0.1085 1059 HOH A O 6154 O O . HOH T . ? 0.2770 0.2928 0.3490 0.0526 -0.0046 -0.0260 1060 HOH A O 6155 O O . HOH T . ? 0.4238 0.2570 0.3732 0.0563 0.0241 -0.1216 1061 HOH A O 6156 O O . HOH T . ? 0.2598 0.3526 0.5903 0.1403 0.1770 0.0605 1062 HOH A O 6157 O O . HOH T . ? 0.4671 0.2861 0.1775 0.1321 -0.0628 -0.0459 1063 HOH A O 6158 O O . HOH T . ? 0.3408 0.3570 0.5017 -0.0616 -0.0675 -0.0305 1064 HOH A O 6159 O O . HOH T . ? 0.3138 0.6104 0.3446 -0.0038 0.0332 0.0519 1065 HOH A O 6160 O O A HOH T . ? 0.2933 0.4111 0.2010 -0.0618 0.0042 -0.0209 1066 HOH A O 6161 O O B HOH T . ? 0.1668 0.1426 0.1771 -0.0139 0.1358 0.0363 1066 HOH A O 6162 O O . HOH T . ? 0.2861 0.2527 0.2011 0.0367 -0.0139 -0.0306 1067 HOH A O 6163 O O . HOH T . ? 0.2373 0.3193 0.1955 0.0640 0.0049 0.0189 1068 HOH A O 6164 O O . HOH T . ? 0.4786 0.4670 0.4053 0.1154 0.0982 -0.0390 1069 HOH A O 6165 O O . HOH T . ? 0.4535 0.3850 0.3293 -0.0386 0.1981 -0.0057 1070 HOH A O 6166 O O . HOH T . ? 0.3103 0.3805 0.4317 -0.0369 0.1440 -0.0926 1071 HOH A O 6167 O O . HOH T . ? 0.3680 0.3164 0.4218 -0.0041 0.0531 -0.0120 1072 HOH A O 6168 O O . HOH T . ? 0.7625 0.4739 0.6694 -0.0589 -0.3548 -0.0568 1073 HOH A O 6169 O O . HOH T . ? 0.2480 0.2970 0.4592 0.0053 0.0311 0.1040 1074 HOH A O 6170 O O . HOH T . ? 0.4603 0.0808 0.2891 0.0746 0.0146 0.0654 1075 HOH A O 6171 O O A HOH T . ? 0.3178 0.2855 0.4029 -0.0715 0.0193 0.0536 1076 HOH A O 6172 O O B HOH T . ? 0.2065 0.1408 0.2795 -0.0459 0.1660 -0.0252 1076 HOH A O 6173 O O . HOH T . ? 0.3824 0.3351 0.2758 0.1152 0.0137 -0.0170 1077 HOH A O 6174 O O . HOH T . ? 0.3276 0.3700 0.3659 -0.0866 0.0781 -0.1335 1078 HOH A O 6175 O O . HOH T . ? 0.7396 0.5601 0.2359 0.0574 0.0062 -0.0304 1079 HOH A O 6176 O O . HOH T . ? 0.3629 0.2839 0.3324 0.0290 0.0240 -0.0967 1080 HOH A O 6177 O O . HOH T . ? 0.3204 0.3224 0.3705 0.0961 -0.0872 0.0594 1081 HOH A O 6178 O O . HOH T . ? 0.6162 0.3933 0.2622 0.0711 -0.0363 -0.0655 1082 HOH A O 6179 O O . HOH T . ? 0.7308 0.4606 0.4747 -0.1186 -0.0432 -0.0840 1083 HOH A O 6180 O O . HOH T . ? 0.3922 0.5088 0.4410 0.2182 0.1665 -0.0667 1084 HOH A O 6181 O O . HOH T . ? 0.3763 0.3415 0.2781 0.0081 0.0408 -0.0470 1085 HOH A O 6182 O O . HOH T . ? 0.4212 0.3882 0.2629 -0.0794 0.0318 0.0422 1086 HOH A O 6183 O O . HOH T . ? 0.2812 0.3284 0.3667 0.0462 0.0579 -0.1212 1087 HOH A O 6184 O O . HOH T . ? 0.3132 0.4086 0.4897 -0.1407 0.0010 0.1047 1088 HOH A O 6185 O O . HOH T . ? 0.4484 0.4298 0.3181 0.1075 0.1508 0.0872 1089 HOH A O 6186 O O . HOH T . ? 0.3245 0.2924 0.4317 -0.0236 0.0672 -0.0143 1090 HOH A O 6187 O O . HOH T . ? 0.4044 0.4254 0.4857 0.0054 0.0024 -0.1296 1091 HOH A O 6188 O O . HOH T . ? 0.3394 0.3734 0.4958 0.0750 -0.0714 0.0307 1092 HOH A O 6189 O O . HOH T . ? 0.3431 0.4353 0.3847 0.0129 -0.1423 -0.0701 1093 HOH A O 6190 O O . HOH T . ? 0.2465 0.3078 0.2908 -0.0360 -0.0012 0.0329 1094 HOH A O 6191 O O . HOH T . ? 0.4638 0.3598 0.3241 0.0352 -0.1152 -0.0557 1095 HOH A O 6192 O O . HOH T . ? 0.4699 0.3635 0.3845 0.0965 -0.0881 -0.0678 1096 HOH A O 6193 O O . HOH T . ? 0.3105 0.3340 0.3038 -0.0605 -0.0335 0.0904 1097 HOH A O 6194 O O . HOH T . ? 0.3708 0.4774 0.4424 0.1975 0.0766 -0.0471 1098 HOH A O 6195 O O . HOH T . ? 0.2804 0.5772 0.5900 0.0087 -0.0581 0.1945 1099 HOH A O 6196 O O . HOH T . ? 0.5108 0.5061 0.4281 -0.2121 -0.0439 -0.1041 1100 HOH A O 6197 O O . HOH T . ? 0.5012 0.3794 0.5259 -0.0588 0.1292 0.0572 1101 HOH A O 6198 O O . HOH T . ? 0.3778 0.4776 0.4376 0.0333 0.1184 0.1093 1102 HOH A O 6199 O O . HOH T . ? 0.5269 0.3513 0.4716 -0.0508 0.0433 0.0920 1103 HOH A O 6200 O O . HOH T . ? 0.5652 0.3408 0.3828 -0.0583 -0.0778 -0.1208 1104 HOH A O 6201 O O . HOH T . ? 0.3034 0.3365 0.4296 -0.0216 0.0373 -0.0429 1105 HOH A O 6202 O O . HOH T . ? 0.2949 0.4825 0.3858 0.0044 -0.0665 0.0282 1106 HOH A O 6203 O O . HOH T . ? 0.3660 0.3490 0.5131 0.1595 0.0354 -0.1426 1107 HOH A O 6204 O O . HOH T . ? 0.4453 0.5370 0.4486 -0.1628 0.1345 -0.0176 1108 HOH A O 6205 O O . HOH T . ? 0.4687 0.6358 0.2799 0.1452 0.1561 0.2177 1109 HOH A O 6206 O O . HOH T . ? 0.2988 0.2977 0.2487 0.0232 -0.0236 -0.0179 1110 HOH A O 6207 O O . HOH T . ? 0.4781 0.4910 0.5137 0.1777 -0.0063 0.1007 1111 HOH A O 6208 O O . HOH T . ? 0.2900 0.4798 0.2988 0.0053 0.0218 -0.1201 1112 HOH A O 6209 O O . HOH T . ? 0.3523 0.5473 0.5344 -0.2272 -0.0889 0.0303 1113 HOH A O 6210 O O . HOH T . ? 0.6123 0.3342 0.5626 0.0129 -0.0306 0.0922 1114 HOH A O 6211 O O . HOH T . ? 0.2736 0.2154 0.2603 0.0368 -0.0266 -0.0049 1115 HOH A O 6212 O O . HOH T . ? 0.4244 0.4547 0.4155 -0.0153 0.1252 0.0192 1116 HOH A O 6213 O O . HOH T . ? 0.4335 0.5848 0.4623 0.0274 -0.1106 -0.1665 1117 HOH A O 6214 O O . HOH T . ? 0.4376 0.4563 0.3921 -0.0395 0.1186 -0.1376 1118 HOH A O 6215 O O . HOH T . ? 0.3522 0.4243 0.4622 -0.0675 -0.0038 -0.1544 1119 HOH A O 6216 O O . HOH T . ? 0.3848 0.6327 0.3494 -0.0628 0.0256 -0.1804 1120 HOH A O 6217 O O . HOH T . ? 0.3715 0.3134 0.4388 0.0083 -0.0069 0.0718 1121 HOH A O 6218 O O . HOH T . ? 0.3672 0.6960 0.4461 0.1860 0.0944 -0.0847 1122 HOH A O 6219 O O . HOH T . ? 0.3545 0.3807 0.2835 0.1026 0.0592 0.0630 1123 HOH A O 6220 O O . HOH T . ? 0.5094 0.3632 0.5122 0.0225 -0.0929 0.1797 1124 HOH A O 6221 O O . HOH T . ? 0.6090 0.4295 0.3474 0.0764 -0.0144 0.0241 1125 HOH A O 6222 O O . HOH T . ? 0.8283 0.3265 0.1845 0.2764 -0.1793 -0.0323 1126 HOH A O 6223 O O . HOH T . ? 0.3724 0.4068 0.5560 -0.0003 -0.0256 -0.0228 1127 HOH A O 6224 O O . HOH T . ? 0.6667 0.4282 0.2920 0.1989 0.0030 -0.0755 1128 HOH A O 6225 O O . HOH T . ? 0.5394 0.5251 0.2090 -0.0026 0.0559 0.0330 1129 HOH A O 6226 O O . HOH T . ? 0.2853 0.4307 0.4518 -0.0969 0.0370 -0.0562 1130 HOH A O 6227 O O . HOH T . ? 0.5228 0.5322 0.3552 0.0589 -0.1016 0.0131 1131 HOH A O 6228 O O . HOH T . ? 0.4712 0.4369 0.5300 0.0332 -0.1242 -0.0816 1132 HOH A O 6229 O O . HOH T . ? 0.3842 0.3048 0.4699 0.0330 0.0805 0.0565 1133 HOH A O 6230 O O . HOH T . ? 0.5274 0.3648 0.5914 -0.0051 -0.0667 0.2051 1134 HOH A O 6231 O O . HOH T . ? 0.3992 0.4573 0.2867 0.0059 0.1050 0.0018 1135 HOH A O 6232 O O . HOH T . ? 0.3706 0.6623 0.3303 0.0109 -0.0027 -0.0938 1136 HOH A O 6233 O O . HOH T . ? 0.3322 0.4084 0.4184 -0.0454 0.1389 -0.0388 1137 HOH A O 6234 O O . HOH T . ? 0.3217 0.7301 0.5896 0.0410 -0.0267 0.0050 1138 HOH A O 6235 O O . HOH T . ? 0.3790 0.2902 0.6840 -0.1141 0.1929 -0.1095 1139 HOH A O 6236 O O . HOH T . ? 0.2840 0.5909 0.6569 -0.0097 -0.0140 0.0361 1140 HOH A O 6237 O O . HOH T . ? 0.2180 0.2434 0.1962 0.0389 0.0016 -0.0305 1141 HOH A O 6238 O O . HOH T . ? 0.3138 0.3439 0.3928 -0.0042 0.1068 -0.1354 1142 HOH A O 6239 O O . HOH T . ? 0.3849 0.2310 0.2430 -0.0978 0.1532 0.0067 1143 HOH A O 6240 O O . HOH T . ? 0.2977 0.5558 0.3708 0.0499 -0.0172 -0.0848 1144 HOH A O 6241 O O . HOH T . ? 0.2342 0.4824 0.5139 -0.1013 0.0598 -0.0249 1145 HOH A O 6242 O O . HOH T . ? 0.4853 0.6414 0.3199 0.0786 -0.0128 -0.1802 1146 HOH A O 6243 O O . HOH T . ? 0.4582 0.4913 0.5458 0.0268 0.0632 -0.3458 1147 HOH A O 6244 O O . HOH T . ? 0.4698 0.4004 0.5596 -0.0891 0.0473 -0.0020 1148 HOH A O 6245 O O . HOH T . ? 0.3225 0.8464 0.3726 0.3224 0.1911 0.2389 1149 HOH A O 6246 O O . HOH T . ? 0.4057 0.4366 0.8970 0.0250 0.0585 0.1447 1150 HOH A O 6247 O O . HOH T . ? 0.3250 0.5155 0.8834 -0.0385 0.0215 0.1327 1151 HOH A O 6248 O O . HOH T . ? 0.6107 0.3358 0.3082 -0.0415 0.2039 0.0262 1152 HOH A O 6249 O O . HOH T . ? 0.4856 0.4761 0.4605 -0.0391 0.1124 -0.0027 1153 HOH A O 6250 O O . HOH T . ? 0.4475 0.4947 0.4732 0.0528 0.1678 -0.0660 1154 HOH A O 6251 O O . HOH T . ? 0.3885 0.3216 0.3806 0.0469 0.0525 -0.0345 1155 HOH A O 6252 O O . HOH T . ? 0.3572 0.5057 0.4401 0.1308 0.0131 0.0938 1156 HOH A O 6253 O O . HOH T . ? 0.5358 0.3355 0.3861 -0.0558 0.0232 0.0114 1157 HOH A O 6254 O O . HOH T . ? 0.1798 0.2762 0.0592 0.0060 -0.0380 0.0770 1158 HOH A O 6255 O O . HOH T . ? 0.3535 0.2708 0.2416 -0.0138 0.0352 -0.0207 1159 HOH A O 6256 O O . HOH T . ? 0.3787 0.4429 0.4684 -0.1080 0.1291 -0.1743 1160 HOH A O 6257 O O . HOH T . ? 0.4871 0.5547 0.3345 -0.0886 -0.0178 0.1339 1161 HOH A O 6258 O O . HOH T . ? 0.2868 0.6699 0.5521 0.1224 -0.0993 -0.1303 1162 HOH A O 6259 O O . HOH T . ? 0.3818 0.5397 0.3565 -0.1859 -0.0642 0.0992 1163 HOH A O 6260 O O . HOH T . ? 0.3226 0.4631 0.4534 -0.0588 0.0401 -0.0798 1164 HOH A O 6261 O O . HOH T . ? 0.5229 0.4265 0.4722 -0.0568 0.1598 0.0778 1165 HOH A O 6262 O O . HOH T . ? 0.4981 0.4461 0.2871 0.0659 0.0661 -0.0469 1166 HOH A O 6263 O O . HOH T . ? 0.6103 0.5136 0.2536 0.0554 -0.0576 0.0192 1167 HOH A O 6264 O O . HOH T . ? 0.6160 0.5553 0.5443 0.0371 -0.0646 -0.0908 1168 HOH A O 6265 O O . HOH T . ? 0.2612 0.3781 0.2998 0.0002 -0.0022 -0.0490 1169 HOH A O 6266 O O . HOH T . ? 0.3926 0.2784 0.4393 0.0166 0.0365 0.0674 1170 HOH A O 6267 O O . HOH T . ? 0.2966 0.5561 0.6132 0.0238 -0.1677 -0.0493 1171 HOH A O 6268 O O . HOH T . ? 0.5640 0.3178 0.4059 -0.0174 -0.0120 0.1505 1172 HOH A O 6269 O O . HOH T . ? 0.4538 0.5758 0.3673 0.2423 -0.0189 -0.1779 1173 HOH A O 6270 O O . HOH T . ? 0.3922 0.5569 0.3962 0.0811 -0.1476 -0.0047 1174 HOH A O 6271 O O . HOH T . ? 0.2785 0.3578 0.4317 -0.0763 0.0022 0.0672 1175 HOH A O 6272 O O . HOH T . ? 0.4931 0.5464 0.3557 0.0300 0.1370 0.0243 1176 HOH A O 6273 O O . HOH T . ? 0.5815 0.4493 0.3716 -0.0889 0.0254 -0.0074 1177 HOH A O 6274 O O . HOH T . ? 0.4043 0.3950 0.2599 0.0782 -0.0607 -0.0624 1178 HOH A O 6275 O O . HOH T . ? 0.8407 0.2826 0.4232 0.0136 -0.0919 0.0029 1179 HOH A O 6276 O O . HOH T . ? 0.4740 0.3352 0.4250 -0.0071 0.0054 0.0103 1180 HOH A O 6277 O O . HOH T . ? 0.4001 0.5263 0.4529 0.0773 -0.1295 -0.0921 1181 HOH A O 6278 O O . HOH T . ? 0.3874 0.6130 0.4924 0.0863 -0.1307 -0.1135 1182 HOH A O 6279 O O . HOH T . ? 0.4495 0.4419 0.5323 0.0654 -0.0471 0.0619 1183 HOH A O 6280 O O . HOH T . ? 0.2595 0.1819 0.1948 0.0312 0.0211 0.0197 1184 HOH A O 6281 O O . HOH T . ? 0.3660 0.4918 0.5074 -0.0509 0.1193 0.0727 1185 HOH A O 6282 O O A HOH T . ? 0.3392 0.2407 0.6525 0.0186 0.1238 0.0898 1186 HOH A O 6283 O O B HOH T . ? 0.0448 0.3265 0.1632 -0.0583 0.0359 -0.0114 1186 HOH A O 6284 O O . HOH T . ? 0.4907 0.3129 0.3430 -0.0079 -0.1215 0.0226 1187 HOH A O 6285 O O . HOH T . ? 0.5971 0.4698 0.3606 0.1679 -0.0458 -0.0587 1188 HOH A O 6286 O O . HOH T . ? 0.5618 0.6307 0.2924 0.0639 -0.0253 -0.1851 1189 HOH A O 6287 O O . HOH T . ? 0.3886 0.4042 0.4909 0.0861 -0.0381 0.1336 1190 HOH A O 6288 O O . HOH T . ? 0.4555 0.6122 0.2841 0.1567 -0.0800 -0.0593 1191 HOH A O 6289 O O . HOH T . ? 0.7297 0.3471 0.6072 0.0152 -0.0884 0.0780 1192 HOH A O 6290 O O . HOH T . ? 0.6772 0.3259 0.8559 -0.0867 -0.1239 -0.1162 1193 HOH A O 6291 O O . HOH T . ? 0.5875 0.3939 0.4861 -0.1472 -0.0640 -0.0122 1194 HOH A O 6292 O O . HOH T . ? 0.7558 0.4024 0.6400 -0.3389 -0.0562 0.1962 1195 HOH A O 6293 O O A HOH T . ? 0.3509 0.4182 0.4487 0.0747 -0.0683 0.0256 1196 HOH A O 6294 O O B HOH T . ? 0.2431 0.2084 0.1448 -0.1072 -0.0531 -0.0039 1196 HOH A O 6295 O O A HOH T . ? 0.3702 0.5088 0.3653 0.0751 -0.0964 -0.1619 1197 HOH A O 6296 O O B HOH T . ? 0.2503 0.1808 0.4812 -0.0726 -0.2839 0.2052 1197 HOH A O 6297 O O . HOH T . ? 0.4798 0.5162 0.6255 0.2340 0.1238 -0.0744 1198 HOH A O 6298 O O . HOH T . ? 0.5872 0.5500 0.2678 -0.1004 -0.1320 -0.0435 1199 HOH A O 6299 O O . HOH T . ? 0.3243 0.6486 0.5246 -0.1205 0.0961 -0.1121 1200 HOH A O 6300 O O . HOH T . ? 0.4128 0.2666 0.4023 0.1266 -0.2496 -0.0677 1201 HOH A O 6301 O O . HOH T . ? 0.3353 0.5447 0.4684 -0.0443 0.0877 0.0318 1202 HOH A O 6302 O O . HOH T . ? 0.5657 0.2409 0.6322 0.0909 0.0234 -0.1747 1203 HOH A O 6303 O O A HOH T . ? 0.4134 0.1705 0.3578 -0.0427 0.0156 0.0060 1204 HOH A O 6304 O O B HOH T . ? 0.0632 0.1645 0.0891 -0.0726 0.0491 -0.0942 1204 HOH A O 6305 O O . HOH T . ? 0.3888 0.4328 0.3028 0.0643 0.0368 0.0431 1205 HOH A O 6306 O O . HOH T . ? 0.4730 0.4423 0.4837 -0.0428 0.2469 -0.0825 1206 HOH A O 6307 O O . HOH T . ? 0.2993 0.3802 0.6098 0.0114 0.0266 0.0421 1207 HOH A O 6308 O O . HOH T . ? 0.2159 0.5009 0.3770 0.0207 0.0284 -0.0110 1208 HOH A O 6309 O O . HOH T . ? 0.3635 0.4644 0.6393 0.1573 0.0049 0.0346 1209 HOH A O 6310 O O . HOH T . ? 0.5041 0.5304 0.7108 0.2503 -0.0226 -0.1390 1210 HOH A O 6311 O O . HOH T . ? 0.3633 0.4013 0.3734 0.0010 -0.0042 0.0542 1211 HOH A O 6312 O O . HOH T . ? 0.2884 0.2986 0.3806 0.0825 -0.1984 0.1178 1212 HOH A O 6313 O O . HOH T . ? 0.3893 0.7418 0.5658 0.2251 -0.1268 -0.0909 1213 HOH A O 6314 O O . HOH T . ? 0.5110 0.5142 0.5140 0.2544 -0.0555 -0.1004 1214 HOH A O 6315 O O . HOH T . ? 0.3241 0.1539 0.2198 -0.0564 0.1918 0.0554 1215 HOH A O 6316 O O . HOH T . ? 0.1258 0.1506 0.4538 0.1022 -0.0038 0.0907 1216 HOH A O 6317 O O . HOH T . ? 0.5163 0.3864 0.5198 -0.0616 0.0944 -0.0324 1217 HOH A O 6318 O O . HOH T . ? 0.5500 0.3583 0.4681 0.0133 -0.0451 -0.0641 1218 HOH A O 6319 O O . HOH T . ? 0.6105 0.6326 0.3390 -0.0530 -0.1202 -0.1451 1219 HOH A O 6320 O O . HOH T . ? 0.5276 0.4791 0.4353 -0.1797 0.0959 0.0044 1220 HOH A O 6321 O O . HOH T . ? 0.1719 0.3209 0.3004 0.1398 0.0089 -0.0930 1221 HOH A O 6322 O O . HOH T . ? 0.6512 0.4369 0.5835 -0.1603 -0.0128 0.0078 1222 HOH A O 6323 O O . HOH T . ? 0.3381 0.3702 0.3226 -0.0276 0.0374 -0.0445 1223 HOH A O 6324 O O . HOH T . ? 0.7271 0.4990 0.3025 0.0765 0.0287 -0.1035 1224 HOH A O 6325 O O . HOH T . ? 0.5927 0.4477 0.6173 -0.1163 0.0997 0.0572 1225 HOH A O 6326 O O . HOH T . ? 0.4743 0.4712 0.4649 0.0423 -0.1362 0.0758 1226 HOH A O 6327 O O . HOH T . ? 0.5926 0.5474 0.3761 0.0802 0.0015 -0.0314 1227 HOH A O 6328 O O . HOH T . ? 0.2983 0.5784 0.7312 0.0680 -0.0430 0.0006 1228 HOH A O 6329 O O . HOH T . ? 0.5438 0.5453 0.6142 0.1351 -0.2183 0.0426 1229 HOH A O 6330 O O . HOH T . ? 0.4522 0.4567 0.5739 -0.1455 0.0630 -0.0370 1230 HOH A O 6331 O O . HOH T . ? 0.7719 0.4143 0.5998 0.0005 -0.1620 -0.1950 1231 HOH A O 6332 O O . HOH T . ? 0.5571 0.6198 0.4359 0.0361 0.0788 0.0654 1232 HOH A O 6333 O O . HOH T . ? 0.4144 0.5110 0.7019 -0.0376 0.1584 -0.0657 1233 HOH A O 6334 O O . HOH T . ? 0.6787 0.8520 0.3399 -0.0957 -0.0804 -0.2314 1234 HOH A O 6335 O O . HOH T . ? 0.4547 0.7552 0.5115 0.2084 -0.1121 -0.0967 1235 HOH A O 6336 O O . HOH T . ? 0.3585 0.6772 0.5367 0.0485 -0.0224 0.0463 1236 HOH A O 6337 O O . HOH T . ? 0.5446 0.5105 0.6387 0.2375 -0.0828 -0.0506 1237 HOH A O 6338 O O . HOH T . ? 0.4575 0.4319 0.3264 -0.0043 0.0195 -0.0672 1238 HOH A O 6339 O O . HOH T . ? 0.3477 0.5653 0.5518 0.0646 -0.0801 0.0706 1239 HOH A O 6340 O O . HOH T . ? 0.6777 0.3554 0.4869 -0.0090 -0.0382 -0.0464 1240 HOH A O 6341 O O . HOH T . ? 0.3542 0.3468 0.5739 -0.0237 0.0022 -0.1249 1241 HOH A O 6342 O O . HOH T . ? 0.3967 0.3215 0.4803 -0.0097 0.0313 0.0156 1242 HOH A O 6343 O O . HOH T . ? 0.4311 0.3812 0.3441 0.0359 -0.0600 0.0238 1243 HOH A O 6344 O O . HOH T . ? 0.4122 0.5113 0.5347 0.0177 -0.0185 0.0959 1244 HOH A O 6345 O O . HOH T . ? 0.4972 0.4624 0.0639 0.0528 0.0488 -0.0153 1245 HOH A O 6346 O O . HOH T . ? 0.5972 0.3939 0.2492 -0.0395 -0.0366 -0.0393 1246 HOH A O 6347 O O . HOH T . ? 0.4601 0.4435 0.3394 -0.0096 -0.1356 -0.0202 1247 HOH A O 6348 O O A HOH T . ? 0.1344 0.1162 0.4015 0.0232 -0.0315 -0.0283 1248 HOH A O 6349 O O B HOH T . ? 0.1521 0.6128 0.6018 0.0019 0.1114 0.2515 1248 HOH A O 6350 O O A HOH T . ? 0.2351 0.3465 0.4446 0.0366 0.0297 -0.1209 1249 HOH A O 6351 O O B HOH T . ? 0.1219 0.1992 0.2480 -0.1295 -0.0226 0.0246 1249 HOH A O 6352 O O . HOH T . ? 0.4124 0.5387 0.5232 0.1372 0.0778 0.0507 1250 HOH A O 6353 O O . HOH T . ? 0.2652 0.3768 0.3735 0.0322 -0.0352 -0.0108 1251 HOH A O 6354 O O . HOH T . ? 0.3129 0.3753 0.4238 0.0550 -0.0416 -0.1758 1252 HOH A O 6355 O O . HOH T . ? 0.5640 0.5661 0.7628 0.1225 -0.1732 -0.2018 1253 HOH A O 6356 O O . HOH T . ? 0.6411 0.5135 0.5827 0.0732 -0.2935 0.0867 1254 HOH A O 6357 O O . HOH T . ? 0.7953 0.5639 0.5900 0.1792 -0.0040 -0.1464 1255 HOH A O 6358 O O . HOH T . ? 0.3798 0.6979 0.3980 0.0667 -0.0049 -0.1255 1256 HOH A O 6359 O O . HOH T . ? 0.2853 0.4887 0.5219 -0.0514 0.1460 0.0273 1257 HOH A O 6360 O O . HOH T . ? 0.2308 0.5875 0.6710 0.0557 0.0776 -0.0703 1258 HOH A O 6361 O O . HOH T . ? 0.4014 0.3679 0.4322 -0.0218 0.0008 -0.0312 1259 HOH A O 6362 O O . HOH T . ? 0.2686 0.2456 0.2612 0.0344 0.0658 -0.0104 1260 HOH A O 6363 O O . HOH T . ? 0.4006 0.5869 0.5966 0.1102 0.0346 -0.2295 1261 HOH A O 6364 O O . HOH T . ? 0.5521 0.7000 0.2019 0.2530 -0.0887 0.0544 1262 HOH A O 6365 O O . HOH T . ? 0.3243 0.4667 0.3194 -0.0223 -0.0381 -0.0699 1263 HOH A O 6366 O O . HOH T . ? 0.4032 0.3888 0.3326 0.0293 -0.0118 -0.0098 1264 HOH A O 6367 O O . HOH T . ? 0.3311 0.4952 0.6518 0.0206 0.1386 0.1075 1265 HOH A O 6368 O O . HOH T . ? 0.5187 0.5044 0.4203 0.0527 0.0768 -0.1734 1266 HOH A O 6369 O O . HOH T . ? 0.5006 0.2643 0.6658 0.1068 -0.0641 -0.0287 1267 HOH A O 6370 O O . HOH T . ? 0.4396 0.4814 0.4596 0.0486 0.1071 0.0169 1268 HOH A O 6371 O O . HOH T . ? 0.4539 0.3307 0.7796 0.0460 -0.3820 0.0684 1269 HOH A O 6372 O O . HOH T . ? 0.3652 0.4589 0.2597 0.0591 0.1318 -0.0294 1270 HOH A O 6373 O O . HOH T . ? 0.6939 0.3167 0.5154 0.0777 0.1680 -0.0568 1271 HOH A O 6374 O O . HOH T . ? 0.5714 0.8617 0.3348 -0.1229 0.1678 -0.2627 1272 HOH A O 6375 O O . HOH T . ? 0.3041 0.7383 0.7188 -0.2333 0.0744 -0.1600 1273 HOH A O 6376 O O . HOH T . ? 0.3712 0.3118 0.3162 -0.0424 0.0350 -0.0811 1274 HOH A O 6377 O O . HOH T . ? 0.5649 0.6034 0.4279 -0.1106 0.1355 -0.1885 1275 HOH A O 6378 O O . HOH T . ? 0.5073 0.6042 0.3673 0.0563 -0.1011 -0.0576 1276 HOH A O 6379 O O . HOH T . ? 0.2454 0.5693 0.3567 -0.1298 0.0336 0.1052 1277 HOH A O 6380 O O . HOH T . ? 0.5565 0.5196 0.4881 -0.0587 0.2023 -0.1274 1278 HOH A O 6381 O O . HOH T . ? 0.4759 0.5696 0.6402 -0.0925 -0.0927 0.3214 1279 HOH A O 6382 O O . HOH T . ? 0.3796 0.5543 0.4282 0.1388 -0.0241 -0.0496 1280 HOH A O 6383 O O . HOH T . ? 0.5466 0.9192 0.5201 -0.1789 -0.1212 0.1741 1281 HOH A O 6384 O O . HOH T . ? 0.3799 0.4586 0.5272 0.0642 0.0678 0.0918 1282 HOH A O 6385 O O . HOH T . ? 0.7433 0.4709 0.5302 0.0590 0.3252 0.0807 1283 HOH A O 6386 O O . HOH T . ? 0.4836 0.4422 0.7126 0.1288 0.0083 -0.2058 1284 HOH A O 6387 O O . HOH T . ? 0.2591 0.5711 0.6763 0.0816 0.0053 0.0229 1285 HOH A O 6388 O O . HOH T . ? 0.5812 0.6913 0.5757 -0.0794 0.0901 0.2021 1286 HOH A O 6389 O O . HOH T . ? 0.2843 0.5615 0.5630 0.1984 0.0699 0.0016 1287 HOH A O 6390 O O . HOH T . ? 0.8175 0.3807 0.5161 -0.2148 -0.0753 -0.0592 1288 HOH A O 6391 O O . HOH T . ? 0.5863 0.4085 0.5533 0.0012 0.0233 -0.2589 1289 HOH A O 6392 O O . HOH T . ? 0.6198 0.7753 0.2935 0.0249 0.2266 0.0143 1290 HOH A O 6393 O O . HOH T . ? 0.2632 0.4804 0.7237 -0.0011 -0.1059 -0.0468 1291 HOH A O 6394 O O . HOH T . ? 0.3368 0.6849 0.8108 -0.0145 0.1938 -0.3247 1292 HOH A O 6395 O O . HOH T . ? 0.4590 0.6608 0.5420 0.0859 0.0240 -0.0396 1293 HOH A O 6396 O O . HOH T . ? 0.1910 0.3467 0.1433 0.0788 -0.0995 0.0608 1294 HOH A O 6397 O O . HOH T . ? 0.5613 0.5985 0.3360 0.1310 -0.1346 -0.0749 1295 HOH A O 6398 O O . HOH T . ? 0.5336 0.9102 0.3354 0.1525 0.0110 -0.0258 1296 HOH A O 6399 O O . HOH T . ? 0.5522 0.3798 0.4990 0.1495 -0.0183 -0.1129 1297 HOH A O 6400 O O . HOH T . ? 0.4940 0.6598 0.6907 0.1537 0.0625 -0.0231 1298 HOH A O 6401 O O . HOH T . ? 0.4824 0.5960 0.6045 0.3914 -0.0477 -0.0620 1299 HOH A O 6402 O O . HOH T . ? 0.4411 0.4412 0.4685 0.0004 0.0807 0.0064 1300 HOH A O 6403 O O . HOH T . ? 0.5684 0.7644 0.4599 0.1260 -0.1983 -0.1325 1301 HOH A O 6404 O O . HOH T . ? 0.7320 0.6978 0.2874 0.0769 -0.0297 0.2063 1302 HOH A O 6405 O O . HOH T . ? 0.5705 0.6364 0.3648 -0.0719 0.1236 -0.0598 1303 HOH A O 6406 O O . HOH T . ? 0.5036 0.3328 0.5373 -0.0444 0.0549 -0.0378 1304 HOH A O 6407 O O . HOH T . ? 0.3251 0.9073 0.6995 0.0480 -0.0432 -0.0346 1305 HOH A O 6408 O O . HOH T . ? 0.9657 0.4767 0.4212 0.2779 -0.0986 -0.0892 1306 HOH A O 6409 O O . HOH T . ? 0.3427 0.4632 0.6439 0.1684 -0.0916 -0.0514 1307 HOH A O 6410 O O . HOH T . ? 0.3254 0.5769 0.6753 0.1398 -0.0725 -0.1183 1308 HOH A O 6411 O O . HOH T . ? 0.2025 0.2376 0.2344 0.0358 0.0265 -0.0141 1309 HOH A O 6412 O O . HOH T . ? 0.6597 0.4826 0.0344 0.0279 0.0695 0.0293 1310 HOH A O 6413 O O . HOH T . ? 0.4987 0.7602 0.4212 -0.0965 0.0462 0.0018 1311 HOH A O 6414 O O . HOH T . ? 0.3149 0.1415 0.3051 -0.0039 -0.1089 0.0933 1312 HOH A O 6415 O O . HOH T . ? 0.1818 0.2175 0.4113 0.1274 0.0663 0.0003 1313 HOH A O 6416 O O . HOH T . ? 0.6767 0.7486 0.4777 -0.0171 -0.0071 0.1943 1314 HOH A O 6417 O O . HOH T . ? 0.4715 0.3846 0.5526 -0.0451 -0.0606 0.1707 1315 HOH A O 6418 O O . HOH T . ? 0.3452 0.6524 0.5751 0.0335 -0.0136 -0.1486 1316 HOH A O 6419 O O . HOH T . ? 0.2295 0.5938 0.5572 0.2205 0.0510 -0.1300 1317 HOH A O 6420 O O . HOH T . ? 0.4532 0.5833 0.6509 -0.0219 -0.2175 -0.2801 1318 HOH A O 6421 O O . HOH T . ? 0.4000 0.4396 0.3493 -0.0985 0.0538 0.0884 1319 HOH A O 6422 O O . HOH T . ? 0.3910 0.6201 0.8931 -0.0135 -0.0067 -0.1579 1320 HOH A O 6423 O O . HOH T . ? 0.4891 0.4657 0.7177 0.1232 0.0016 -0.0400 1321 HOH A O 6424 O O . HOH T . ? 0.2186 0.5670 0.6986 0.1400 -0.0478 -0.0823 1322 HOH A O 6425 O O . HOH T . ? 0.3829 0.7056 0.6892 0.0947 -0.1136 0.1093 1323 HOH A O 6426 O O . HOH T . ? 0.5920 0.7074 0.6862 -0.0451 -0.2541 -0.1601 1324 HOH A O 6427 O O . HOH T . ? 0.1177 0.4861 0.1705 0.1996 -0.0184 -0.1042 1325 HOH A O 6428 O O . HOH T . ? 0.1087 0.4586 0.3254 -0.0316 -0.0870 -0.0754 1326 HOH A O 6429 O O . HOH T . ? 0.6199 0.5092 0.2009 0.1521 -0.0257 -0.0062 1327 HOH A O 6430 O O . HOH T . ? 0.6561 0.5559 0.3647 -0.0361 0.1703 0.1854 1328 HOH A O 6431 O O . HOH T . ? 0.2457 0.5721 0.4466 0.0966 -0.0757 0.1240 1329 HOH A O 6432 O O . HOH T . ? 0.2731 0.4333 0.2276 -0.1190 0.0744 -0.0854 1330 HOH A O 6433 O O . HOH T . ? 0.6029 0.6503 0.3864 0.2319 -0.0963 -0.1273 1331 HOH A O 6434 O O . HOH T . ? 0.3326 0.2320 0.2228 0.0460 0.0114 -0.1394 1332 HOH A O 6435 O O . HOH T . ? 0.5645 0.2762 0.3511 -0.0118 -0.0357 -0.0074 1333 HOH A O 6436 O O . HOH T . ? 0.3795 0.4799 0.4025 -0.1197 -0.1417 0.0151 1334 HOH A O 6437 O O . HOH T . ? 0.2671 0.4216 0.3871 -0.1345 -0.0603 0.1860 1335 HOH A O 6438 O O . HOH T . ? 0.2614 0.4470 0.3466 0.0436 -0.1479 -0.1943 1336 HOH A O 6439 O O . HOH T . ? 0.4411 0.6392 0.5924 -0.0825 0.0750 -0.1133 1337 HOH A O 6440 O O . HOH T . ? 0.2962 0.3971 0.3493 -0.0347 0.2408 -0.2164 1338 HOH A O 6441 O O . HOH T . ? 0.2052 0.2941 0.2964 -0.0121 0.1399 -0.0254 1339 HOH A O 6442 O O . HOH T . ? 0.6594 0.6106 0.4065 0.0437 0.2345 0.1133 1340 HOH A O 6443 O O . HOH T . ? 0.0645 0.1189 0.2192 0.0055 0.0833 0.0509 1341 HOH A O 6444 O O . HOH T . ? 0.1074 0.1597 0.2177 -0.0758 0.1022 -0.1591 1342 HOH A O 6445 O O . HOH T . ? 0.3203 0.6481 0.0551 0.0486 -0.0876 -0.0628 1343 HOH A O 6446 O O . HOH T . ? 0.3077 0.2223 0.3552 0.0216 0.0166 -0.2157 1344 HOH A O 6447 O O . HOH T . ? 0.8322 0.3842 0.6412 -0.0776 0.1546 -0.1834 1345 HOH A O 6448 O O . HOH T . ? 0.3170 0.4894 0.4476 -0.2037 0.0023 -0.1349 1346 HOH A O 6449 O O . HOH T . ? 0.3696 0.4326 0.3916 0.0316 0.1012 -0.0247 1347 HOH A O 6450 O O . HOH T . ? 0.0609 0.2307 0.3560 0.0827 -0.0334 -0.1405 1348 HOH A O 6451 O O . HOH T . ? 0.1465 0.2605 0.2467 0.1456 0.1152 0.0564 1349 HOH A O 6452 O O . HOH T . ? 0.3999 0.4721 0.3737 0.0794 -0.1878 -0.0344 1350 HOH A O 6453 O O . HOH T . ? 0.8101 0.6782 0.4882 0.2736 0.0415 -0.2257 1351 HOH A O 6454 O O . HOH T . ? 0.2782 0.5600 0.3930 0.1810 -0.0215 0.0262 1352 HOH A O 6455 O O . HOH T . ? 0.4237 0.3736 0.7114 -0.0372 -0.1346 0.0272 1353 HOH A O 6456 O O . HOH T . ? 0.3435 0.8005 0.2885 0.0184 -0.1555 0.0031 1354 HOH A O 6457 O O . HOH T . ? 0.2196 0.2224 0.1932 0.0229 -0.0443 -0.1085 1355 HOH A O 6458 O O . HOH T . ? 0.7243 0.6037 0.3903 0.0899 -0.0100 0.0357 1356 HOH A O 6459 O O . HOH T . ? 0.1824 1.0180 0.7708 -0.0781 -0.0938 -0.0138 1357 HOH A O 6460 O O . HOH T . ? 0.4308 0.4968 0.3496 0.0334 0.0141 0.1343 1358 HOH A O 6461 O O . HOH T . ? 0.6825 0.8207 0.6146 0.0364 0.1527 0.2066 1359 HOH A O 6462 O O . HOH T . ? 0.4246 0.3079 0.2811 -0.0483 -0.2086 0.0480 1360 HOH A O 6463 O O . HOH T . ? 0.4959 0.3371 0.1348 0.0278 0.2161 0.0691 1361 HOH A O 6464 O O . HOH T . ? 0.4495 0.3022 0.6605 -0.0493 -0.1449 0.1640 1362 HOH A O 6465 O O . HOH T . ? 0.2617 0.3387 0.2461 -0.0358 0.0063 0.0246 1363 HOH A O 6466 O O . HOH T . ? 0.4474 0.2253 0.4629 0.1634 0.0458 0.0054 1364 HOH A O 6467 O O . HOH T . ? 0.6489 0.6073 0.4785 0.0436 -0.1145 -0.0301 1365 HOH A O 6468 O O . HOH T . ? 0.4469 0.4899 0.6471 0.0995 0.2367 0.2231 1366 HOH A O 6469 O O . HOH T . ? 0.6388 0.2977 0.8011 -0.0215 -0.0137 -0.1237 1367 HOH A O 6470 O O . HOH T . ? 0.4351 0.2149 0.5348 -0.0615 -0.1137 -0.0165 1368 HOH A O 6471 O O . HOH T . ? 0.4185 0.7547 0.5180 0.0275 -0.0039 -0.1264 1369 HOH A O 6472 O O . HOH T . ? 0.2759 0.6018 0.2431 -0.0882 0.0107 0.0755 1370 HOH A O 6473 O O . HOH T . ? 0.5115 0.5765 0.5724 0.0254 0.2668 0.0754 1371 HOH A O 6474 O O A HOH T . ? 0.0273 0.1126 0.0604 0.0132 -0.0084 -0.0553 1372 HOH A O 6475 O O B HOH T . ? 0.2162 0.2630 0.2957 -0.0992 -0.0478 0.1890 1372 HOH A O 6476 O O . HOH T . ? 0.3896 0.5392 0.2609 0.0533 -0.0479 -0.1168 1373 HOH A O 6477 O O . HOH T . ? 0.2159 0.2253 0.1968 0.0326 -0.0811 -0.0988 1374 HOH A O 6478 O O . HOH T . ? 0.3004 0.8671 0.3524 0.1822 -0.2472 -0.2309 1375 HOH A O 6479 O O . HOH T . ? 0.5302 0.7547 0.4600 0.0233 -0.0854 0.0335 1376 HOH A O 6480 O O . HOH T . ? 0.6505 0.4197 0.2930 0.0307 -0.0329 0.0184 1377 HOH A O 6481 O O . HOH T . ? 0.7381 1.0216 0.6576 0.2743 0.0545 0.1730 1378 HOH A O 6482 O O . HOH T . ? 0.5234 0.7126 0.5896 -0.0890 0.2280 -0.0375 1379 HOH A O 6483 O O . HOH T . ? 0.2408 0.5365 0.4809 0.0986 0.0893 0.1407 1380 HOH A O 6484 O O . HOH T . ? 0.6862 0.5082 0.6449 0.0415 -0.0413 -0.0043 1381 HOH A O 6485 O O . HOH T . ? 0.3261 0.9645 0.5723 -0.1603 0.0202 -0.1971 1382 HOH A O 6486 O O . HOH T . ? 0.3709 0.6745 0.4459 -0.0895 0.1417 0.0151 1383 HOH A O 6487 O O . HOH T . ? 0.5496 0.8787 1.0917 -0.0144 -0.0440 0.2761 1384 HOH A O 6488 O O . HOH T . ? 1.0387 0.4623 0.6793 -0.0148 -0.2762 0.0289 1385 HOH A O 6489 O O . HOH T . ? 0.4084 0.3630 0.3874 0.0484 -0.0043 -0.0310 1386 HOH A O 6490 O O . HOH T . ? 0.4233 0.2702 0.2695 -0.2363 0.1274 -0.0234 1387 HOH A O 6491 O O . HOH T . ? 0.4184 0.5535 0.5777 0.0380 0.0832 0.1462 1388 HOH A O 6492 O O . HOH T . ? 0.3285 0.1999 0.2831 -0.0905 -0.0196 0.1300 1389 HOH A O 6493 O O . HOH T . ? 0.3814 0.4264 0.5370 -0.0209 0.1073 0.1408 1390 HOH A O 6494 O O . HOH T . ? 0.7000 0.5964 0.2423 -0.0594 -0.1151 -0.2309 1391 HOH A O 6495 O O . HOH T . ? 0.5160 0.3876 0.4577 -0.0616 0.0339 -0.0215 1392 HOH A O 6496 O O . HOH T . ? 0.0646 0.0480 0.2333 0.0299 -0.0904 -0.0688 1393 HOH A O 6497 O O . HOH T . ? 0.2205 0.3989 0.6120 0.0191 -0.0810 0.0705 1394 HOH A O 6498 O O . HOH T . ? 0.7248 0.3161 0.2838 0.1014 -0.1278 0.1493 1395 HOH A O 6499 O O . HOH T . ? 0.3482 0.4268 0.2575 -0.0732 0.0681 0.0165 1396 HOH A O 6500 O O . HOH T . ? 0.3509 0.7591 0.7964 -0.1879 -0.2085 0.1410 1397 HOH A O 6501 O O . HOH T . ? 0.3502 0.5391 0.3440 -0.1050 0.0355 0.0441 1398 HOH A O 6502 O O . HOH T . ? 0.4792 0.7568 0.6967 -0.0340 0.1711 0.2593 1399 HOH A O 6503 O O . HOH T . ? 0.6470 0.7316 0.4389 -0.2403 -0.3465 0.1582 1400 HOH A O 6504 O O . HOH T . ? 0.4034 0.1583 0.2567 0.0945 -0.2716 -0.1308 1401 HOH A O 6505 O O . HOH T . ? 0.4516 0.4825 0.1749 -0.1810 0.1869 -0.2191 1402 HOH A O 6506 O O . HOH T . ? 0.5632 0.1598 0.4710 -0.0275 0.0848 -0.0862 1403 HOH A O 6507 O O . HOH T . ? 0.4871 0.4253 0.3805 -0.0942 -0.0180 0.1537 1404 HOH A O 6508 O O . HOH T . ? 0.4183 0.3039 0.8251 0.0433 0.0468 0.0613 1405 HOH A O 6509 O O . HOH T . ? 0.3296 0.5271 0.4861 -0.0252 -0.0701 0.0123 1406 HOH A O 6510 O O . HOH T . ? 0.2812 0.5682 0.0379 0.0165 0.0324 -0.0658 1407 HOH A O 6511 O O . HOH T . ? 0.7941 0.7645 0.3416 0.1955 0.1228 -0.0792 1408 HOH A O 6512 O O . HOH T . ? 0.3963 0.4870 0.3484 0.0072 0.0990 0.1892 1409 HOH A O 6513 O O . HOH T . ? 0.5104 0.8581 0.4020 -0.0302 -0.0956 0.1077 1410 HOH A O 6514 O O . HOH T . ? 0.5924 0.7705 0.9206 -0.2773 -0.0089 -0.0015 1411 HOH A O 6515 O O . HOH T . ? 0.5690 0.5618 0.9112 -0.2158 -0.0142 0.0611 1412 HOH A O 6516 O O . HOH T . ? 0.1648 0.2884 0.6436 -0.1173 0.0129 -0.2717 1413 HOH A O 6517 O O . HOH T . ? 0.2881 0.3051 0.3763 0.1401 0.1583 0.0156 1414 HOH A O 6518 O O . HOH T . ? 0.4462 0.6723 0.6065 0.1099 0.0049 -0.0689 1415 HOH A O 6519 O O . HOH T . ? 0.5162 0.2711 0.4546 0.0558 -0.1034 0.0000 1416 HOH A O 6520 O O . HOH T . ? 0.4756 0.3639 0.3775 -0.1947 -0.0660 0.1920 1417 HOH A O 6521 O O . HOH T . ? 0.5230 0.0415 0.5817 -0.0022 -0.1700 -0.0760 1418 HOH A O 6522 O O . HOH T . ? 0.5922 0.7945 0.5072 0.1200 -0.0680 -0.0469 1419 HOH A O 6523 O O . HOH T . ? 0.6674 0.4103 0.8694 0.1786 -0.2665 -0.1790 1420 HOH A O 6524 O O . HOH T . ? 0.2524 0.4349 0.1446 -0.0364 -0.1242 0.0683 1421 HOH A O # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 MET 1 -6 ? ? ? A . n A 1 2 LYS 2 -5 ? ? ? A . n A 1 3 LEU 3 -4 ? ? ? A . n A 1 4 CYS 4 -3 ? ? ? A . n A 1 5 ILE 5 -2 ? ? ? A . n A 1 6 LEU 6 -1 ? ? ? A . n A 1 7 LEU 7 0 ? ? ? A . n A 1 8 ALA 8 1 ? ? ? A . n A 1 9 VAL 9 2 ? ? ? A . n A 1 10 VAL 10 3 ? ? ? A . n A 1 11 ALA 11 4 ? ? ? A . n A 1 12 PHE 12 5 ? ? ? A . n A 1 13 VAL 13 6 ? ? ? A . n A 1 14 GLY 14 7 ? ? ? A . n A 1 15 LEU 15 8 ? ? ? A . n A 1 16 SER 16 9 ? ? ? A . n A 1 17 LEU 17 10 ? ? ? A . n A 1 18 GLY 18 11 ? ? ? A . n A 1 19 ARG 19 12 ? ? ? A . n A 1 20 SER 20 13 ? ? ? A . n A 1 21 GLY 21 14 ? ? ? A . n A 1 22 LEU 22 15 ? ? ? A . n A 1 23 ASN 23 16 ? ? ? A . n A 1 24 ASP 24 17 ? ? ? A . n A 1 25 ILE 25 18 ? ? ? A . n A 1 26 PHE 26 19 ? ? ? A . n A 1 27 GLU 27 20 ? ? ? A . n A 1 28 ALA 28 21 ? ? ? A . n A 1 29 GLN 29 22 ? ? ? A . n A 1 30 LYS 30 23 ? ? ? A . n A 1 31 ILE 31 24 ? ? ? A . n A 1 32 GLU 32 25 ? ? ? A . n A 1 33 TRP 33 26 ? ? ? A . n A 1 34 HIS 34 27 ? ? ? A . n A 1 35 GLU 35 28 ? ? ? A . n A 1 36 GLY 36 29 ? ? ? A . n A 1 37 SER 37 30 ? ? ? A . n A 1 38 GLY 38 31 ? ? ? A . n A 1 39 SER 39 32 ? ? ? A . n A 1 40 GLY 40 33 ? ? ? A . n A 1 41 SER 41 34 ? ? ? A . n A 1 42 GLU 42 35 ? ? ? A . n A 1 43 ASN 43 36 ? ? ? A . n A 1 44 LEU 44 37 ? ? ? A . n A 1 45 TYR 45 38 ? ? ? A . n A 1 46 PHE 46 39 ? ? ? A . n A 1 47 GLN 47 40 ? ? ? A . n A 1 48 GLY 48 41 ? ? ? A . n A 1 49 ARG 49 42 ? ? ? A . n A 1 50 SER 50 43 ? ? ? A . n A 1 51 LYS 51 44 ? ? ? A . n A 1 52 SER 52 45 ? ? ? A . n A 1 53 SER 53 46 ? ? ? A . n A 1 54 ASN 54 47 ? ? ? A . n A 1 55 GLU 55 48 ? ? ? A . n A 1 56 ALA 56 49 ? ? ? A . n A 1 57 THR 57 50 ? ? ? A . n A 1 58 ASN 58 51 ? ? ? A . n A 1 59 ILE 59 52 ? ? ? A . n A 1 60 THR 60 53 ? ? ? A . n A 1 61 PRO 61 54 ? ? ? A . n A 1 62 LYS 62 55 ? ? ? A . n A 1 63 HIS 63 56 56 HIS HIS A . n A 1 64 ASN 64 57 57 ASN ASN A . n A 1 65 MET 65 58 58 MET MET A . n A 1 66 LYS 66 59 59 LYS LYS A . n A 1 67 ALA 67 60 60 ALA ALA A . n A 1 68 PHE 68 61 61 PHE PHE A . n A 1 69 LEU 69 62 62 LEU LEU A . n A 1 70 ASP 70 63 63 ASP ASP A . n A 1 71 GLU 71 64 64 GLU GLU A . n A 1 72 LEU 72 65 65 LEU LEU A . n A 1 73 LYS 73 66 66 LYS LYS A . n A 1 74 ALA 74 67 67 ALA ALA A . n A 1 75 GLU 75 68 68 GLU GLU A . n A 1 76 ASN 76 69 69 ASN ASN A . n A 1 77 ILE 77 70 70 ILE ILE A . n A 1 78 LYS 78 71 71 LYS LYS A . n A 1 79 LYS 79 72 72 LYS LYS A . n A 1 80 PHE 80 73 73 PHE PHE A . n A 1 81 LEU 81 74 74 LEU LEU A . n A 1 82 TYR 82 75 75 TYR TYR A . n A 1 83 ASN 83 76 76 ASN ASN A . n A 1 84 PHE 84 77 77 PHE PHE A . n A 1 85 THR 85 78 78 THR THR A . n A 1 86 GLN 86 79 79 GLN GLN A . n A 1 87 ILE 87 80 80 ILE ILE A . n A 1 88 PRO 88 81 81 PRO PRO A . n A 1 89 HIS 89 82 82 HIS HIS A . n A 1 90 LEU 90 83 83 LEU LEU A . n A 1 91 ALA 91 84 84 ALA ALA A . n A 1 92 GLY 92 85 85 GLY GLY A . n A 1 93 THR 93 86 86 THR THR A . n A 1 94 GLU 94 87 87 GLU GLU A . n A 1 95 GLN 95 88 88 GLN GLN A . n A 1 96 ASN 96 89 89 ASN ASN A . n A 1 97 PHE 97 90 90 PHE PHE A . n A 1 98 GLN 98 91 91 GLN GLN A . n A 1 99 LEU 99 92 92 LEU LEU A . n A 1 100 ALA 100 93 93 ALA ALA A . n A 1 101 LYS 101 94 94 LYS LYS A . n A 1 102 GLN 102 95 95 GLN GLN A . n A 1 103 ILE 103 96 96 ILE ILE A . n A 1 104 GLN 104 97 97 GLN GLN A . n A 1 105 SER 105 98 98 SER SER A . n A 1 106 GLN 106 99 99 GLN GLN A . n A 1 107 TRP 107 100 100 TRP TRP A . n A 1 108 LYS 108 101 101 LYS LYS A . n A 1 109 GLU 109 102 102 GLU GLU A . n A 1 110 PHE 110 103 103 PHE PHE A . n A 1 111 GLY 111 104 104 GLY GLY A . n A 1 112 LEU 112 105 105 LEU LEU A . n A 1 113 ASP 113 106 106 ASP ASP A . n A 1 114 SER 114 107 107 SER SER A . n A 1 115 VAL 115 108 108 VAL VAL A . n A 1 116 GLU 116 109 109 GLU GLU A . n A 1 117 LEU 117 110 110 LEU LEU A . n A 1 118 ALA 118 111 111 ALA ALA A . n A 1 119 HIS 119 112 112 HIS HIS A . n A 1 120 TYR 120 113 113 TYR TYR A . n A 1 121 ASP 121 114 114 ASP ASP A . n A 1 122 VAL 122 115 115 VAL VAL A . n A 1 123 LEU 123 116 116 LEU LEU A . n A 1 124 LEU 124 117 117 LEU LEU A . n A 1 125 SER 125 118 118 SER SER A . n A 1 126 TYR 126 119 119 TYR TYR A . n A 1 127 PRO 127 120 120 PRO PRO A . n A 1 128 ASN 128 121 121 ASN ASN A . n A 1 129 LYS 129 122 122 LYS LYS A . n A 1 130 THR 130 123 123 THR THR A . n A 1 131 HIS 131 124 124 HIS HIS A . n A 1 132 PRO 132 125 125 PRO PRO A . n A 1 133 ASN 133 126 126 ASN ASN A . n A 1 134 TYR 134 127 127 TYR TYR A . n A 1 135 ILE 135 128 128 ILE ILE A . n A 1 136 SER 136 129 129 SER SER A . n A 1 137 ILE 137 130 130 ILE ILE A . n A 1 138 ILE 138 131 131 ILE ILE A . n A 1 139 ASN 139 132 132 ASN ASN A . n A 1 140 GLU 140 133 133 GLU GLU A . n A 1 141 ASP 141 134 134 ASP ASP A . n A 1 142 GLY 142 135 135 GLY GLY A . n A 1 143 ASN 143 136 136 ASN ASN A . n A 1 144 GLU 144 137 137 GLU GLU A . n A 1 145 ILE 145 138 138 ILE ILE A . n A 1 146 PHE 146 139 139 PHE PHE A . n A 1 147 ASN 147 140 140 ASN ASN A . n A 1 148 THR 148 141 141 THR THR A . n A 1 149 SER 149 142 142 SER SER A . n A 1 150 LEU 150 143 143 LEU LEU A . n A 1 151 PHE 151 144 144 PHE PHE A . n A 1 152 GLU 152 145 145 GLU GLU A . n A 1 153 PRO 153 146 146 PRO PRO A . n A 1 154 PRO 154 147 147 PRO PRO A . n A 1 155 PRO 155 148 148 PRO PRO A . n A 1 156 PRO 156 149 149 PRO PRO A . n A 1 157 GLY 157 150 150 GLY GLY A . n A 1 158 TYR 158 151 151 TYR TYR A . n A 1 159 GLU 159 152 152 GLU GLU A . n A 1 160 ASN 160 153 153 ASN ASN A . n A 1 161 VAL 161 154 154 VAL VAL A . n A 1 162 SER 162 155 155 SER SER A . n A 1 163 ASP 163 156 156 ASP ASP A . n A 1 164 ILE 164 157 157 ILE ILE A . n A 1 165 VAL 165 158 158 VAL VAL A . n A 1 166 PRO 166 159 159 PRO PRO A . n A 1 167 PRO 167 160 160 PRO PRO A . n A 1 168 PHE 168 161 161 PHE PHE A . n A 1 169 SER 169 162 162 SER SER A . n A 1 170 ALA 170 163 163 ALA ALA A . n A 1 171 PHE 171 164 164 PHE PHE A . n A 1 172 SER 172 165 165 SER SER A . n A 1 173 PRO 173 166 166 PRO PRO A . n A 1 174 GLN 174 167 167 GLN GLN A . n A 1 175 GLY 175 168 168 GLY GLY A . n A 1 176 MET 176 169 169 MET MET A . n A 1 177 PRO 177 170 170 PRO PRO A . n A 1 178 GLU 178 171 171 GLU GLU A . n A 1 179 GLY 179 172 172 GLY GLY A . n A 1 180 ASP 180 173 173 ASP ASP A . n A 1 181 LEU 181 174 174 LEU LEU A . n A 1 182 VAL 182 175 175 VAL VAL A . n A 1 183 TYR 183 176 176 TYR TYR A . n A 1 184 VAL 184 177 177 VAL VAL A . n A 1 185 ASN 185 178 178 ASN ASN A . n A 1 186 TYR 186 179 179 TYR TYR A . n A 1 187 ALA 187 180 180 ALA ALA A . n A 1 188 ARG 188 181 181 ARG ARG A . n A 1 189 THR 189 182 182 THR THR A . n A 1 190 GLU 190 183 183 GLU GLU A . n A 1 191 ASP 191 184 184 ASP ASP A . n A 1 192 PHE 192 185 185 PHE PHE A . n A 1 193 PHE 193 186 186 PHE PHE A . n A 1 194 LYS 194 187 187 LYS LYS A . n A 1 195 LEU 195 188 188 LEU LEU A . n A 1 196 GLU 196 189 189 GLU GLU A . n A 1 197 ARG 197 190 190 ARG ARG A . n A 1 198 ASP 198 191 191 ASP ASP A . n A 1 199 MET 199 192 192 MET MET A . n A 1 200 LYS 200 193 193 LYS LYS A . n A 1 201 ILE 201 194 194 ILE ILE A . n A 1 202 ASN 202 195 195 ASN ASN A . n A 1 203 CYS 203 196 196 CYS CYS A . n A 1 204 SER 204 197 197 SER SER A . n A 1 205 GLY 205 198 198 GLY GLY A . n A 1 206 LYS 206 199 199 LYS LYS A . n A 1 207 ILE 207 200 200 ILE ILE A . n A 1 208 VAL 208 201 201 VAL VAL A . n A 1 209 ILE 209 202 202 ILE ILE A . n A 1 210 ALA 210 203 203 ALA ALA A . n A 1 211 ARG 211 204 204 ARG ARG A . n A 1 212 TYR 212 205 205 TYR TYR A . n A 1 213 GLY 213 206 206 GLY GLY A . n A 1 214 LYS 214 207 207 LYS LYS A . n A 1 215 VAL 215 208 208 VAL VAL A . n A 1 216 PHE 216 209 209 PHE PHE A . n A 1 217 ARG 217 210 210 ARG ARG A . n A 1 218 GLY 218 211 211 GLY GLY A . n A 1 219 ASN 219 212 212 ASN ASN A . n A 1 220 LYS 220 213 213 LYS LYS A . n A 1 221 VAL 221 214 214 VAL VAL A . n A 1 222 LYS 222 215 215 LYS LYS A . n A 1 223 ASN 223 216 216 ASN ASN A . n A 1 224 ALA 224 217 217 ALA ALA A . n A 1 225 GLN 225 218 218 GLN GLN A . n A 1 226 LEU 226 219 219 LEU LEU A . n A 1 227 ALA 227 220 220 ALA ALA A . n A 1 228 GLY 228 221 221 GLY GLY A . n A 1 229 ALA 229 222 222 ALA ALA A . n A 1 230 LYS 230 223 223 LYS LYS A . n A 1 231 GLY 231 224 224 GLY GLY A . n A 1 232 VAL 232 225 225 VAL VAL A . n A 1 233 ILE 233 226 226 ILE ILE A . n A 1 234 LEU 234 227 227 LEU LEU A . n A 1 235 TYR 235 228 228 TYR TYR A . n A 1 236 SER 236 229 229 SER SER A . n A 1 237 ASP 237 230 230 ASP ASP A . n A 1 238 PRO 238 231 231 PRO PRO A . n A 1 239 ALA 239 232 232 ALA ALA A . n A 1 240 ASP 240 233 233 ASP ASP A . n A 1 241 TYR 241 234 234 TYR TYR A . n A 1 242 PHE 242 235 235 PHE PHE A . n A 1 243 ALA 243 236 236 ALA ALA A . n A 1 244 PRO 244 237 237 PRO PRO A . n A 1 245 GLY 245 238 238 GLY GLY A . n A 1 246 VAL 246 239 239 VAL VAL A . n A 1 247 LYS 247 240 240 LYS LYS A . n A 1 248 SER 248 241 241 SER SER A . n A 1 249 TYR 249 242 242 TYR TYR A . n A 1 250 PRO 250 243 243 PRO PRO A . n A 1 251 ASP 251 244 244 ASP ASP A . n A 1 252 GLY 252 245 245 GLY GLY A . n A 1 253 TRP 253 246 246 TRP TRP A . n A 1 254 ASN 254 247 247 ASN ASN A . n A 1 255 LEU 255 248 248 LEU LEU A . n A 1 256 PRO 256 249 249 PRO PRO A . n A 1 257 GLY 257 250 250 GLY GLY A . n A 1 258 GLY 258 251 251 GLY GLY A . n A 1 259 GLY 259 252 252 GLY GLY A . n A 1 260 VAL 260 253 253 VAL VAL A . n A 1 261 GLN 261 254 254 GLN GLN A . n A 1 262 ARG 262 255 255 ARG ARG A . n A 1 263 GLY 263 256 256 GLY GLY A . n A 1 264 ASN 264 257 257 ASN ASN A . n A 1 265 ILE 265 258 258 ILE ILE A . n A 1 266 LEU 266 259 259 LEU LEU A . n A 1 267 ASN 267 260 260 ASN ASN A . n A 1 268 LEU 268 261 261 LEU LEU A . n A 1 269 ASN 269 262 262 ASN ASN A . n A 1 270 GLY 270 263 263 GLY GLY A . n A 1 271 ALA 271 264 264 ALA ALA A . n A 1 272 GLY 272 265 265 GLY GLY A . n A 1 273 ASP 273 266 266 ASP ASP A . n A 1 274 PRO 274 267 267 PRO PRO A . n A 1 275 LEU 275 268 268 LEU LEU A . n A 1 276 THR 276 269 269 THR THR A . n A 1 277 PRO 277 270 270 PRO PRO A . n A 1 278 GLY 278 271 271 GLY GLY A . n A 1 279 TYR 279 272 272 TYR TYR A . n A 1 280 PRO 280 273 273 PRO PRO A . n A 1 281 ALA 281 274 274 ALA ALA A . n A 1 282 ASN 282 275 275 ASN ASN A . n A 1 283 GLU 283 276 276 GLU GLU A . n A 1 284 TYR 284 277 277 TYR TYR A . n A 1 285 ALA 285 278 278 ALA ALA A . n A 1 286 TYR 286 279 279 TYR TYR A . n A 1 287 ARG 287 280 280 ARG ARG A . n A 1 288 ARG 288 281 281 ARG ARG A . n A 1 289 GLY 289 282 282 GLY GLY A . n A 1 290 ILE 290 283 283 ILE ILE A . n A 1 291 ALA 291 284 284 ALA ALA A . n A 1 292 GLU 292 285 285 GLU GLU A . n A 1 293 ALA 293 286 286 ALA ALA A . n A 1 294 VAL 294 287 287 VAL VAL A . n A 1 295 GLY 295 288 288 GLY GLY A . n A 1 296 LEU 296 289 289 LEU LEU A . n A 1 297 PRO 297 290 290 PRO PRO A . n A 1 298 SER 298 291 291 SER SER A . n A 1 299 ILE 299 292 292 ILE ILE A . n A 1 300 PRO 300 293 293 PRO PRO A . n A 1 301 VAL 301 294 294 VAL VAL A . n A 1 302 HIS 302 295 295 HIS HIS A . n A 1 303 PRO 303 296 296 PRO PRO A . n A 1 304 ILE 304 297 297 ILE ILE A . n A 1 305 GLY 305 298 298 GLY GLY A . n A 1 306 TYR 306 299 299 TYR TYR A . n A 1 307 TYR 307 300 300 TYR TYR A . n A 1 308 ASP 308 301 301 ASP ASP A . n A 1 309 ALA 309 302 302 ALA ALA A . n A 1 310 GLN 310 303 303 GLN GLN A . n A 1 311 LYS 311 304 304 LYS LYS A . n A 1 312 LEU 312 305 305 LEU LEU A . n A 1 313 LEU 313 306 306 LEU LEU A . n A 1 314 GLU 314 307 307 GLU GLU A . n A 1 315 LYS 315 308 308 LYS LYS A . n A 1 316 MET 316 309 309 MET MET A . n A 1 317 GLY 317 310 310 GLY GLY A . n A 1 318 GLY 318 311 311 GLY GLY A . n A 1 319 SER 319 312 312 SER SER A . n A 1 320 ALA 320 313 313 ALA ALA A . n A 1 321 PRO 321 314 314 PRO PRO A . n A 1 322 PRO 322 315 315 PRO PRO A . n A 1 323 ASP 323 316 316 ASP ASP A . n A 1 324 SER 324 317 317 SER SER A . n A 1 325 SER 325 318 318 SER SER A . n A 1 326 TRP 326 319 319 TRP TRP A . n A 1 327 ARG 327 320 320 ARG ARG A . n A 1 328 GLY 328 321 321 GLY GLY A . n A 1 329 SER 329 322 322 SER SER A . n A 1 330 LEU 330 323 323 LEU LEU A . n A 1 331 LYS 331 324 324 LYS LYS A . n A 1 332 VAL 332 325 325 VAL VAL A . n A 1 333 PRO 333 326 326 PRO PRO A . n A 1 334 TYR 334 327 327 TYR TYR A . n A 1 335 ASN 335 328 328 ASN ASN A . n A 1 336 VAL 336 329 329 VAL VAL A . n A 1 337 GLY 337 330 330 GLY GLY A . n A 1 338 PRO 338 331 331 PRO PRO A . n A 1 339 GLY 339 332 332 GLY GLY A . n A 1 340 PHE 340 333 333 PHE PHE A . n A 1 341 THR 341 334 334 THR THR A . n A 1 342 GLY 342 335 335 GLY GLY A . n A 1 343 ASN 343 336 336 ASN ASN A . n A 1 344 PHE 344 337 337 PHE PHE A . n A 1 345 SER 345 338 338 SER SER A . n A 1 346 THR 346 339 339 THR THR A . n A 1 347 GLN 347 340 340 GLN GLN A . n A 1 348 LYS 348 341 341 LYS LYS A . n A 1 349 VAL 349 342 342 VAL VAL A . n A 1 350 LYS 350 343 343 LYS LYS A . n A 1 351 MET 351 344 344 MET MET A . n A 1 352 HIS 352 345 345 HIS HIS A . n A 1 353 ILE 353 346 346 ILE ILE A . n A 1 354 HIS 354 347 347 HIS HIS A . n A 1 355 SER 355 348 348 SER SER A . n A 1 356 THR 356 349 349 THR THR A . n A 1 357 ASN 357 350 350 ASN ASN A . n A 1 358 GLU 358 351 351 GLU GLU A . n A 1 359 VAL 359 352 352 VAL VAL A . n A 1 360 THR 360 353 353 THR THR A . n A 1 361 ARG 361 354 354 ARG ARG A . n A 1 362 ILE 362 355 355 ILE ILE A . n A 1 363 TYR 363 356 356 TYR TYR A . n A 1 364 ASN 364 357 357 ASN ASN A . n A 1 365 VAL 365 358 358 VAL VAL A . n A 1 366 ILE 366 359 359 ILE ILE A . n A 1 367 GLY 367 360 360 GLY GLY A . n A 1 368 THR 368 361 361 THR THR A . n A 1 369 LEU 369 362 362 LEU LEU A . n A 1 370 ARG 370 363 363 ARG ARG A . n A 1 371 GLY 371 364 364 GLY GLY A . n A 1 372 ALA 372 365 365 ALA ALA A . n A 1 373 VAL 373 366 366 VAL VAL A . n A 1 374 GLU 374 367 367 GLU GLU A . n A 1 375 PRO 375 368 368 PRO PRO A . n A 1 376 ASP 376 369 369 ASP ASP A . n A 1 377 ARG 377 370 370 ARG ARG A . n A 1 378 TYR 378 371 371 TYR TYR A . n A 1 379 VAL 379 372 372 VAL VAL A . n A 1 380 ILE 380 373 373 ILE ILE A . n A 1 381 LEU 381 374 374 LEU LEU A . n A 1 382 GLY 382 375 375 GLY GLY A . n A 1 383 GLY 383 376 376 GLY GLY A . n A 1 384 HIS 384 377 377 HIS HIS A . n A 1 385 ARG 385 378 378 ARG ARG A . n A 1 386 ASP 386 379 379 ASP ASP A . n A 1 387 SER 387 380 380 SER SER A . n A 1 388 TRP 388 381 381 TRP TRP A . n A 1 389 VAL 389 382 382 VAL VAL A . n A 1 390 PHE 390 383 383 PHE PHE A . n A 1 391 GLY 391 384 384 GLY GLY A . n A 1 392 GLY 392 385 385 GLY GLY A . n A 1 393 ILE 393 386 386 ILE ILE A . n A 1 394 ASP 394 387 387 ASP ASP A . n A 1 395 PRO 395 388 388 PRO PRO A . n A 1 396 GLN 396 389 389 GLN GLN A . n A 1 397 SER 397 390 390 SER SER A . n A 1 398 GLY 398 391 391 GLY GLY A . n A 1 399 ALA 399 392 392 ALA ALA A . n A 1 400 ALA 400 393 393 ALA ALA A . n A 1 401 VAL 401 394 394 VAL VAL A . n A 1 402 VAL 402 395 395 VAL VAL A . n A 1 403 HIS 403 396 396 HIS HIS A . n A 1 404 GLU 404 397 397 GLU GLU A . n A 1 405 ILE 405 398 398 ILE ILE A . n A 1 406 VAL 406 399 399 VAL VAL A . n A 1 407 ARG 407 400 400 ARG ARG A . n A 1 408 SER 408 401 401 SER SER A . n A 1 409 PHE 409 402 402 PHE PHE A . n A 1 410 GLY 410 403 403 GLY GLY A . n A 1 411 THR 411 404 404 THR THR A . n A 1 412 LEU 412 405 405 LEU LEU A . n A 1 413 LYS 413 406 406 LYS LYS A . n A 1 414 LYS 414 407 407 LYS LYS A . n A 1 415 GLU 415 408 408 GLU GLU A . n A 1 416 GLY 416 409 409 GLY GLY A . n A 1 417 TRP 417 410 410 TRP TRP A . n A 1 418 ARG 418 411 411 ARG ARG A . n A 1 419 PRO 419 412 412 PRO PRO A . n A 1 420 ARG 420 413 413 ARG ARG A . n A 1 421 ARG 421 414 414 ARG ARG A . n A 1 422 THR 422 415 415 THR THR A . n A 1 423 ILE 423 416 416 ILE ILE A . n A 1 424 LEU 424 417 417 LEU LEU A . n A 1 425 PHE 425 418 418 PHE PHE A . n A 1 426 ALA 426 419 419 ALA ALA A . n A 1 427 SER 427 420 420 SER SER A . n A 1 428 TRP 428 421 421 TRP TRP A . n A 1 429 ASP 429 422 422 ASP ASP A . n A 1 430 ALA 430 423 423 ALA ALA A . n A 1 431 ALA 431 424 424 ALA ALA A . n A 1 432 GLU 432 425 425 GLU GLU A . n A 1 433 PHE 433 426 426 PHE PHE A . n A 1 434 GLY 434 427 427 GLY GLY A . n A 1 435 LEU 435 428 428 LEU LEU A . n A 1 436 LEU 436 429 429 LEU LEU A . n A 1 437 GLY 437 430 430 GLY GLY A . n A 1 438 SER 438 431 431 SER SER A . n A 1 439 THR 439 432 432 THR THR A . n A 1 440 GLU 440 433 433 GLU GLU A . n A 1 441 TRP 441 434 434 TRP TRP A . n A 1 442 ALA 442 435 435 ALA ALA A . n A 1 443 GLU 443 436 436 GLU GLU A . n A 1 444 GLU 444 437 437 GLU GLU A . n A 1 445 ASN 445 438 438 ASN ASN A . n A 1 446 SER 446 439 439 SER SER A . n A 1 447 ARG 447 440 440 ARG ARG A . n A 1 448 LEU 448 441 441 LEU LEU A . n A 1 449 LEU 449 442 442 LEU LEU A . n A 1 450 GLN 450 443 443 GLN GLN A . n A 1 451 GLU 451 444 444 GLU GLU A . n A 1 452 ARG 452 445 445 ARG ARG A . n A 1 453 GLY 453 446 446 GLY GLY A . n A 1 454 VAL 454 447 447 VAL VAL A . n A 1 455 ALA 455 448 448 ALA ALA A . n A 1 456 TYR 456 449 449 TYR TYR A . n A 1 457 ILE 457 450 450 ILE ILE A . n A 1 458 ASN 458 451 451 ASN ASN A . n A 1 459 ALA 459 452 452 ALA ALA A . n A 1 460 ASP 460 453 453 ASP ASP A . n A 1 461 SER 461 454 454 SER SER A . n A 1 462 SER 462 455 455 SER SER A . n A 1 463 ILE 463 456 456 ILE ILE A . n A 1 464 GLU 464 457 457 GLU GLU A . n A 1 465 GLY 465 458 458 GLY GLY A . n A 1 466 ASN 466 459 459 ASN ASN A . n A 1 467 TYR 467 460 460 TYR TYR A . n A 1 468 THR 468 461 461 THR THR A . n A 1 469 LEU 469 462 462 LEU LEU A . n A 1 470 ARG 470 463 463 ARG ARG A . n A 1 471 VAL 471 464 464 VAL VAL A . n A 1 472 ASP 472 465 465 ASP ASP A . n A 1 473 CYS 473 466 466 CYS CYS A . n A 1 474 THR 474 467 467 THR THR A . n A 1 475 PRO 475 468 468 PRO PRO A . n A 1 476 LEU 476 469 469 LEU LEU A . n A 1 477 MET 477 470 470 MET MET A . n A 1 478 TYR 478 471 471 TYR TYR A . n A 1 479 SER 479 472 472 SER SER A . n A 1 480 LEU 480 473 473 LEU LEU A . n A 1 481 VAL 481 474 474 VAL VAL A . n A 1 482 HIS 482 475 475 HIS HIS A . n A 1 483 ASN 483 476 476 ASN ASN A . n A 1 484 LEU 484 477 477 LEU LEU A . n A 1 485 THR 485 478 478 THR THR A . n A 1 486 LYS 486 479 479 LYS LYS A . n A 1 487 GLU 487 480 480 GLU GLU A . n A 1 488 LEU 488 481 481 LEU LEU A . n A 1 489 LYS 489 482 482 LYS LYS A . n A 1 490 SER 490 483 483 SER SER A . n A 1 491 PRO 491 484 484 PRO PRO A . n A 1 492 ASP 492 485 485 ASP ASP A . n A 1 493 GLU 493 486 486 GLU GLU A . n A 1 494 GLY 494 487 487 GLY GLY A . n A 1 495 PHE 495 488 488 PHE PHE A . n A 1 496 GLU 496 489 489 GLU GLU A . n A 1 497 GLY 497 490 490 GLY GLY A . n A 1 498 LYS 498 491 491 LYS LYS A . n A 1 499 SER 499 492 492 SER SER A . n A 1 500 LEU 500 493 493 LEU LEU A . n A 1 501 TYR 501 494 494 TYR TYR A . n A 1 502 GLU 502 495 495 GLU GLU A . n A 1 503 SER 503 496 496 SER SER A . n A 1 504 TRP 504 497 497 TRP TRP A . n A 1 505 THR 505 498 498 THR THR A . n A 1 506 LYS 506 499 499 LYS LYS A . n A 1 507 LYS 507 500 500 LYS LYS A . n A 1 508 SER 508 501 501 SER SER A . n A 1 509 PRO 509 502 502 PRO PRO A . n A 1 510 SER 510 503 503 SER SER A . n A 1 511 PRO 511 504 504 PRO PRO A . n A 1 512 GLU 512 505 505 GLU GLU A . n A 1 513 PHE 513 506 506 PHE PHE A . n A 1 514 SER 514 507 507 SER SER A . n A 1 515 GLY 515 508 508 GLY GLY A . n A 1 516 MET 516 509 509 MET MET A . n A 1 517 PRO 517 510 510 PRO PRO A . n A 1 518 ARG 518 511 511 ARG ARG A . n A 1 519 ILE 519 512 512 ILE ILE A . n A 1 520 SER 520 513 513 SER SER A . n A 1 521 LYS 521 514 514 LYS LYS A . n A 1 522 LEU 522 515 515 LEU LEU A . n A 1 523 GLY 523 516 516 GLY GLY A . n A 1 524 SER 524 517 517 SER SER A . n A 1 525 GLY 525 518 518 GLY GLY A . n A 1 526 ASN 526 519 519 ASN ASN A . n A 1 527 ASP 527 520 520 ASP ASP A . n A 1 528 PHE 528 521 521 PHE PHE A . n A 1 529 GLU 529 522 522 GLU GLU A . n A 1 530 VAL 530 523 523 VAL VAL A . n A 1 531 PHE 531 524 524 PHE PHE A . n A 1 532 PHE 532 525 525 PHE PHE A . n A 1 533 GLN 533 526 526 GLN GLN A . n A 1 534 ARG 534 527 527 ARG ARG A . n A 1 535 LEU 535 528 528 LEU LEU A . n A 1 536 GLY 536 529 529 GLY GLY A . n A 1 537 ILE 537 530 530 ILE ILE A . n A 1 538 ALA 538 531 531 ALA ALA A . n A 1 539 SER 539 532 532 SER SER A . n A 1 540 GLY 540 533 533 GLY GLY A . n A 1 541 ARG 541 534 534 ARG ARG A . n A 1 542 ALA 542 535 535 ALA ALA A . n A 1 543 ARG 543 536 536 ARG ARG A . n A 1 544 TYR 544 537 537 TYR TYR A . n A 1 545 THR 545 538 538 THR THR A . n A 1 546 LYS 546 539 539 LYS LYS A . n A 1 547 ASN 547 540 540 ASN ASN A . n A 1 548 TRP 548 541 541 TRP TRP A . n A 1 549 GLU 549 542 542 GLU GLU A . n A 1 550 THR 550 543 543 THR THR A . n A 1 551 ASN 551 544 544 ASN ASN A . n A 1 552 LYS 552 545 545 LYS LYS A . n A 1 553 PHE 553 546 546 PHE PHE A . n A 1 554 SER 554 547 547 SER SER A . n A 1 555 GLY 555 548 548 GLY GLY A . n A 1 556 TYR 556 549 549 TYR TYR A . n A 1 557 PRO 557 550 550 PRO PRO A . n A 1 558 LEU 558 551 551 LEU LEU A . n A 1 559 TYR 559 552 552 TYR TYR A . n A 1 560 HIS 560 553 553 HIS HIS A . n A 1 561 SER 561 554 554 SER SER A . n A 1 562 VAL 562 555 555 VAL VAL A . n A 1 563 TYR 563 556 556 TYR TYR A . n A 1 564 GLU 564 557 557 GLU GLU A . n A 1 565 THR 565 558 558 THR THR A . n A 1 566 TYR 566 559 559 TYR TYR A . n A 1 567 GLU 567 560 560 GLU GLU A . n A 1 568 LEU 568 561 561 LEU LEU A . n A 1 569 VAL 569 562 562 VAL VAL A . n A 1 570 GLU 570 563 563 GLU GLU A . n A 1 571 LYS 571 564 564 LYS LYS A . n A 1 572 PHE 572 565 565 PHE PHE A . n A 1 573 TYR 573 566 566 TYR TYR A . n A 1 574 ASP 574 567 567 ASP ASP A . n A 1 575 PRO 575 568 568 PRO PRO A . n A 1 576 MET 576 569 569 MET MET A . n A 1 577 PHE 577 570 570 PHE PHE A . n A 1 578 LYS 578 571 571 LYS LYS A . n A 1 579 TYR 579 572 572 TYR TYR A . n A 1 580 HIS 580 573 573 HIS HIS A . n A 1 581 LEU 581 574 574 LEU LEU A . n A 1 582 THR 582 575 575 THR THR A . n A 1 583 VAL 583 576 576 VAL VAL A . n A 1 584 ALA 584 577 577 ALA ALA A . n A 1 585 GLN 585 578 578 GLN GLN A . n A 1 586 VAL 586 579 579 VAL VAL A . n A 1 587 ARG 587 580 580 ARG ARG A . n A 1 588 GLY 588 581 581 GLY GLY A . n A 1 589 GLY 589 582 582 GLY GLY A . n A 1 590 MET 590 583 583 MET MET A . n A 1 591 VAL 591 584 584 VAL VAL A . n A 1 592 PHE 592 585 585 PHE PHE A . n A 1 593 GLU 593 586 586 GLU GLU A . n A 1 594 LEU 594 587 587 LEU LEU A . n A 1 595 ALA 595 588 588 ALA ALA A . n A 1 596 ASN 596 589 589 ASN ASN A . n A 1 597 SER 597 590 590 SER SER A . n A 1 598 ILE 598 591 591 ILE ILE A . n A 1 599 VAL 599 592 592 VAL VAL A . n A 1 600 LEU 600 593 593 LEU LEU A . n A 1 601 PRO 601 594 594 PRO PRO A . n A 1 602 PHE 602 595 595 PHE PHE A . n A 1 603 ASP 603 596 596 ASP ASP A . n A 1 604 CYS 604 597 597 CYS CYS A . n A 1 605 ARG 605 598 598 ARG ARG A . n A 1 606 ASP 606 599 599 ASP ASP A . n A 1 607 TYR 607 600 600 TYR TYR A . n A 1 608 ALA 608 601 601 ALA ALA A . n A 1 609 VAL 609 602 602 VAL VAL A . n A 1 610 VAL 610 603 603 VAL VAL A . n A 1 611 LEU 611 604 604 LEU LEU A . n A 1 612 ARG 612 605 605 ARG ARG A . n A 1 613 LYS 613 606 606 LYS LYS A . n A 1 614 TYR 614 607 607 TYR TYR A . n A 1 615 ALA 615 608 608 ALA ALA A . n A 1 616 ASP 616 609 609 ASP ASP A . n A 1 617 LYS 617 610 610 LYS LYS A . n A 1 618 ILE 618 611 611 ILE ILE A . n A 1 619 TYR 619 612 612 TYR TYR A . n A 1 620 SER 620 613 613 SER SER A . n A 1 621 ILE 621 614 614 ILE ILE A . n A 1 622 SER 622 615 615 SER SER A . n A 1 623 MET 623 616 616 MET MET A . n A 1 624 LYS 624 617 617 LYS LYS A . n A 1 625 HIS 625 618 618 HIS HIS A . n A 1 626 PRO 626 619 619 PRO PRO A . n A 1 627 GLN 627 620 620 GLN GLN A . n A 1 628 GLU 628 621 621 GLU GLU A . n A 1 629 MET 629 622 622 MET MET A . n A 1 630 LYS 630 623 623 LYS LYS A . n A 1 631 THR 631 624 624 THR THR A . n A 1 632 TYR 632 625 625 TYR TYR A . n A 1 633 SER 633 626 626 SER SER A . n A 1 634 VAL 634 627 627 VAL VAL A . n A 1 635 SER 635 628 628 SER SER A . n A 1 636 PHE 636 629 629 PHE PHE A . n A 1 637 ASP 637 630 630 ASP ASP A . n A 1 638 SER 638 631 631 SER SER A . n A 1 639 LEU 639 632 632 LEU LEU A . n A 1 640 PHE 640 633 633 PHE PHE A . n A 1 641 SER 641 634 634 SER SER A . n A 1 642 ALA 642 635 635 ALA ALA A . n A 1 643 VAL 643 636 636 VAL VAL A . n A 1 644 LYS 644 637 637 LYS LYS A . n A 1 645 ASN 645 638 638 ASN ASN A . n A 1 646 PHE 646 639 639 PHE PHE A . n A 1 647 THR 647 640 640 THR THR A . n A 1 648 GLU 648 641 641 GLU GLU A . n A 1 649 ILE 649 642 642 ILE ILE A . n A 1 650 ALA 650 643 643 ALA ALA A . n A 1 651 SER 651 644 644 SER SER A . n A 1 652 LYS 652 645 645 LYS LYS A . n A 1 653 PHE 653 646 646 PHE PHE A . n A 1 654 SER 654 647 647 SER SER A . n A 1 655 GLU 655 648 648 GLU GLU A . n A 1 656 ARG 656 649 649 ARG ARG A . n A 1 657 LEU 657 650 650 LEU LEU A . n A 1 658 GLN 658 651 651 GLN GLN A . n A 1 659 ASP 659 652 652 ASP ASP A . n A 1 660 PHE 660 653 653 PHE PHE A . n A 1 661 ASP 661 654 ? ? ? A . n A 1 662 LYS 662 655 ? ? ? A . n A 1 663 SER 663 656 656 SER SER A . n A 1 664 ASN 664 657 657 ASN ASN A . n A 1 665 PRO 665 658 658 PRO PRO A . n A 1 666 ILE 666 659 659 ILE ILE A . n A 1 667 VAL 667 660 660 VAL VAL A . n A 1 668 LEU 668 661 661 LEU LEU A . n A 1 669 ARG 669 662 662 ARG ARG A . n A 1 670 MET 670 663 663 MET MET A . n A 1 671 MET 671 664 664 MET MET A . n A 1 672 ASN 672 665 665 ASN ASN A . n A 1 673 ASP 673 666 666 ASP ASP A . n A 1 674 GLN 674 667 667 GLN GLN A . n A 1 675 LEU 675 668 668 LEU LEU A . n A 1 676 MET 676 669 669 MET MET A . n A 1 677 PHE 677 670 670 PHE PHE A . n A 1 678 LEU 678 671 671 LEU LEU A . n A 1 679 GLU 679 672 672 GLU GLU A . n A 1 680 ARG 680 673 673 ARG ARG A . n A 1 681 ALA 681 674 674 ALA ALA A . n A 1 682 PHE 682 675 675 PHE PHE A . n A 1 683 ILE 683 676 676 ILE ILE A . n A 1 684 ASP 684 677 677 ASP ASP A . n A 1 685 PRO 685 678 678 PRO PRO A . n A 1 686 LEU 686 679 679 LEU LEU A . n A 1 687 GLY 687 680 680 GLY GLY A . n A 1 688 LEU 688 681 681 LEU LEU A . n A 1 689 PRO 689 682 682 PRO PRO A . n A 1 690 ASP 690 683 683 ASP ASP A . n A 1 691 ARG 691 684 684 ARG ARG A . n A 1 692 PRO 692 685 685 PRO PRO A . n A 1 693 PHE 693 686 686 PHE PHE A . n A 1 694 TYR 694 687 687 TYR TYR A . n A 1 695 ARG 695 688 688 ARG ARG A . n A 1 696 HIS 696 689 689 HIS HIS A . n A 1 697 VAL 697 690 690 VAL VAL A . n A 1 698 ILE 698 691 691 ILE ILE A . n A 1 699 TYR 699 692 692 TYR TYR A . n A 1 700 ALA 700 693 693 ALA ALA A . n A 1 701 PRO 701 694 694 PRO PRO A . n A 1 702 SER 702 695 695 SER SER A . n A 1 703 SER 703 696 696 SER SER A . n A 1 704 HIS 704 697 697 HIS HIS A . n A 1 705 ASN 705 698 698 ASN ASN A . n A 1 706 LYS 706 699 699 LYS LYS A . n A 1 707 TYR 707 700 700 TYR TYR A . n A 1 708 ALA 708 701 701 ALA ALA A . n A 1 709 GLY 709 702 702 GLY GLY A . n A 1 710 GLU 710 703 703 GLU GLU A . n A 1 711 SER 711 704 704 SER SER A . n A 1 712 PHE 712 705 705 PHE PHE A . n A 1 713 PRO 713 706 706 PRO PRO A . n A 1 714 GLY 714 707 707 GLY GLY A . n A 1 715 ILE 715 708 708 ILE ILE A . n A 1 716 TYR 716 709 709 TYR TYR A . n A 1 717 ASP 717 710 710 ASP ASP A . n A 1 718 ALA 718 711 711 ALA ALA A . n A 1 719 LEU 719 712 712 LEU LEU A . n A 1 720 PHE 720 713 713 PHE PHE A . n A 1 721 ASP 721 714 714 ASP ASP A . n A 1 722 ILE 722 715 715 ILE ILE A . n A 1 723 GLU 723 716 716 GLU GLU A . n A 1 724 SER 724 717 717 SER SER A . n A 1 725 LYS 725 718 718 LYS LYS A . n A 1 726 VAL 726 719 719 VAL VAL A . n A 1 727 ASP 727 720 720 ASP ASP A . n A 1 728 PRO 728 721 721 PRO PRO A . n A 1 729 SER 729 722 722 SER SER A . n A 1 730 LYS 730 723 723 LYS LYS A . n A 1 731 ALA 731 724 724 ALA ALA A . n A 1 732 TRP 732 725 725 TRP TRP A . n A 1 733 GLY 733 726 726 GLY GLY A . n A 1 734 GLU 734 727 727 GLU GLU A . n A 1 735 VAL 735 728 728 VAL VAL A . n A 1 736 LYS 736 729 729 LYS LYS A . n A 1 737 ARG 737 730 730 ARG ARG A . n A 1 738 GLN 738 731 731 GLN GLN A . n A 1 739 ILE 739 732 732 ILE ILE A . n A 1 740 TYR 740 733 733 TYR TYR A . n A 1 741 VAL 741 734 734 VAL VAL A . n A 1 742 ALA 742 735 735 ALA ALA A . n A 1 743 ALA 743 736 736 ALA ALA A . n A 1 744 PHE 744 737 737 PHE PHE A . n A 1 745 THR 745 738 738 THR THR A . n A 1 746 VAL 746 739 739 VAL VAL A . n A 1 747 GLN 747 740 740 GLN GLN A . n A 1 748 ALA 748 741 741 ALA ALA A . n A 1 749 ALA 749 742 742 ALA ALA A . n A 1 750 ALA 750 743 743 ALA ALA A . n A 1 751 GLU 751 744 744 GLU GLU A . n A 1 752 THR 752 745 745 THR THR A . n A 1 753 LEU 753 746 746 LEU LEU A . n A 1 754 SER 754 747 747 SER SER A . n A 1 755 GLU 755 748 748 GLU GLU A . n A 1 756 VAL 756 749 749 VAL VAL A . n A 1 757 ALA 757 750 750 ALA ALA A . n # _pdbx_molecule_features.prd_id PRD_001164 _pdbx_molecule_features.name 'N-(4-{[(2-AMINO-4-OXO-3,4-DIHYDROPTERIDIN-6-YL)METHYL]AMINO}BENZOYL)-L-GAMMA-GLUTAMYL-L-GAMMA-GLUTAMYL-L-GLUTAMIC ACID' _pdbx_molecule_features.type Peptide-like _pdbx_molecule_features.class Inhibitor _pdbx_molecule_features.details ? # _pdbx_molecule.instance_id 1 _pdbx_molecule.prd_id PRD_001164 _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 483 A ASN 476 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 83 A ASN 76 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 466 A ASN 459 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 645 A ASN 638 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 147 A ASN 140 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 128 A ASN 121 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 202 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)' 11980 ? 1 MORE -53 ? 1 'SSA (A^2)' 49310 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_565 -x,-y+1,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 130.1400000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id A _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 1411 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id T _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # 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 1309 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 106.3 ? 2 O ? T HOH . ? A HOH 1309 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 110.7 ? 3 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 121.0 ? 4 O ? T HOH . ? A HOH 1309 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 109.5 ? 5 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 106.3 ? 6 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 102.6 ? 7 O ? T HOH . ? A HOH 1309 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 95.9 ? 8 O ? T HOH . ? A HOH 1309 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 98.0 ? 9 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 96.2 ? 10 O ? T HOH . ? A HOH 1309 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 160.7 ? 11 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 91.9 ? 12 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 98.7 ? 13 O ? T HOH . ? A HOH 1309 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAF ? S 29C . ? A 29C 818 ? 1_555 76.1 ? 14 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAF ? S 29C . ? A 29C 818 ? 1_555 106.7 ? 15 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAF ? S 29C . ? A 29C 818 ? 1_555 156.7 ? 16 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAF ? S 29C . ? A 29C 818 ? 1_555 84.8 ? 17 O ? T HOH . ? A HOH 1309 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 89.5 ? 18 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 153.9 ? 19 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 57.7 ? 20 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 91.2 ? 21 OAF ? S 29C . ? A 29C 818 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 99.3 ? 22 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A TYR 279 ? A TYR 272 ? 1_555 80.5 ? 23 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 102.5 ? 24 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 73.7 ? 25 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 95.3 ? 26 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 144.6 ? 27 O ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 73.0 ? 28 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 93.7 ? 29 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 84.7 ? 30 O ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 150.2 ? 31 O ? T HOH . ? A HOH 906 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 130.6 ? 32 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 172.4 ? 33 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 93.2 ? 34 O ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 71.5 ? 35 O ? T HOH . ? A HOH 906 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 87.4 ? 36 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 89.8 ? 37 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 87.9 ? 38 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 136.6 ? 39 O ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 149.6 ? 40 O ? T HOH . ? A HOH 906 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 77.7 ? 41 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 54.3 ? 42 OG1 ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 99.6 ? # 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 2014-06-18 2 'Structure model' 1 1 2014-08-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 17.6124 _pdbx_refine_tls.origin_y 49.8180 _pdbx_refine_tls.origin_z 45.1536 _pdbx_refine_tls.T[1][1] 0.0102 _pdbx_refine_tls.T[2][2] 0.0115 _pdbx_refine_tls.T[3][3] 0.0204 _pdbx_refine_tls.T[1][2] 0.0044 _pdbx_refine_tls.T[1][3] 0.0005 _pdbx_refine_tls.T[2][3] -0.0119 _pdbx_refine_tls.L[1][1] 0.2273 _pdbx_refine_tls.L[2][2] 0.3755 _pdbx_refine_tls.L[3][3] 0.1583 _pdbx_refine_tls.L[1][2] -0.1004 _pdbx_refine_tls.L[1][3] -0.0005 _pdbx_refine_tls.L[2][3] 0.0114 _pdbx_refine_tls.S[1][1] -0.0165 _pdbx_refine_tls.S[2][2] 0.0238 _pdbx_refine_tls.S[3][3] -0.0073 _pdbx_refine_tls.S[1][2] 0.0156 _pdbx_refine_tls.S[1][3] -0.0165 _pdbx_refine_tls.S[2][3] -0.0646 _pdbx_refine_tls.S[2][1] -0.0001 _pdbx_refine_tls.S[3][1] 0.0148 _pdbx_refine_tls.S[3][2] 0.0245 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 56 A 750 ? . . . . ? 'X-RAY DIFFRACTION' 2 1 A 801 A 818 ? . . . . ? 'X-RAY DIFFRACTION' 3 1 A 901 A 1421 ? . . . . ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal BL-Control 'data collection' . ? 1 REFMAC refinement . ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 REFMAC phasing . ? 5 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 OE1 _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 GLU _pdbx_validate_symm_contact.auth_seq_id_1 276 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 D _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O2 _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 BMA _pdbx_validate_symm_contact.auth_seq_id_2 816 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 2_565 _pdbx_validate_symm_contact.dist 1.74 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 OE1 _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 GLU _pdbx_validate_rmsd_angle.auth_seq_id_1 425 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CD _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 GLU _pdbx_validate_rmsd_angle.auth_seq_id_2 425 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 OE2 _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 GLU _pdbx_validate_rmsd_angle.auth_seq_id_3 425 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 112.62 _pdbx_validate_rmsd_angle.angle_target_value 123.30 _pdbx_validate_rmsd_angle.angle_deviation -10.68 _pdbx_validate_rmsd_angle.angle_standard_deviation 1.20 _pdbx_validate_rmsd_angle.linker_flag N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASP A 156 ? ? 72.84 30.66 2 1 PHE A 164 ? ? 83.22 4.36 3 1 ASN A 178 ? ? 58.95 -127.08 4 1 LYS A 207 ? ? 78.59 -45.17 5 1 VAL A 382 ? ? -128.68 -105.10 6 1 ALA A 452 ? ? -153.70 60.35 7 1 ASP A 453 ? ? -84.41 -153.32 8 1 ASP A 567 ? ? -152.86 66.78 9 1 ASP A 683 ? ? 59.32 15.68 10 1 ASN A 698 ? ? -163.76 97.01 11 1 PHE A 705 ? ? 34.95 57.42 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A MET -6 ? A MET 1 2 1 Y 1 A LYS -5 ? A LYS 2 3 1 Y 1 A LEU -4 ? A LEU 3 4 1 Y 1 A CYS -3 ? A CYS 4 5 1 Y 1 A ILE -2 ? A ILE 5 6 1 Y 1 A LEU -1 ? A LEU 6 7 1 Y 1 A LEU 0 ? A LEU 7 8 1 Y 1 A ALA 1 ? A ALA 8 9 1 Y 1 A VAL 2 ? A VAL 9 10 1 Y 1 A VAL 3 ? A VAL 10 11 1 Y 1 A ALA 4 ? A ALA 11 12 1 Y 1 A PHE 5 ? A PHE 12 13 1 Y 1 A VAL 6 ? A VAL 13 14 1 Y 1 A GLY 7 ? A GLY 14 15 1 Y 1 A LEU 8 ? A LEU 15 16 1 Y 1 A SER 9 ? A SER 16 17 1 Y 1 A LEU 10 ? A LEU 17 18 1 Y 1 A GLY 11 ? A GLY 18 19 1 Y 1 A ARG 12 ? A ARG 19 20 1 Y 1 A SER 13 ? A SER 20 21 1 Y 1 A GLY 14 ? A GLY 21 22 1 Y 1 A LEU 15 ? A LEU 22 23 1 Y 1 A ASN 16 ? A ASN 23 24 1 Y 1 A ASP 17 ? A ASP 24 25 1 Y 1 A ILE 18 ? A ILE 25 26 1 Y 1 A PHE 19 ? A PHE 26 27 1 Y 1 A GLU 20 ? A GLU 27 28 1 Y 1 A ALA 21 ? A ALA 28 29 1 Y 1 A GLN 22 ? A GLN 29 30 1 Y 1 A LYS 23 ? A LYS 30 31 1 Y 1 A ILE 24 ? A ILE 31 32 1 Y 1 A GLU 25 ? A GLU 32 33 1 Y 1 A TRP 26 ? A TRP 33 34 1 Y 1 A HIS 27 ? A HIS 34 35 1 Y 1 A GLU 28 ? A GLU 35 36 1 Y 1 A GLY 29 ? A GLY 36 37 1 Y 1 A SER 30 ? A SER 37 38 1 Y 1 A GLY 31 ? A GLY 38 39 1 Y 1 A SER 32 ? A SER 39 40 1 Y 1 A GLY 33 ? A GLY 40 41 1 Y 1 A SER 34 ? A SER 41 42 1 Y 1 A GLU 35 ? A GLU 42 43 1 Y 1 A ASN 36 ? A ASN 43 44 1 Y 1 A LEU 37 ? A LEU 44 45 1 Y 1 A TYR 38 ? A TYR 45 46 1 Y 1 A PHE 39 ? A PHE 46 47 1 Y 1 A GLN 40 ? A GLN 47 48 1 Y 1 A GLY 41 ? A GLY 48 49 1 Y 1 A ARG 42 ? A ARG 49 50 1 Y 1 A SER 43 ? A SER 50 51 1 Y 1 A LYS 44 ? A LYS 51 52 1 Y 1 A SER 45 ? A SER 52 53 1 Y 1 A SER 46 ? A SER 53 54 1 Y 1 A ASN 47 ? A ASN 54 55 1 Y 1 A GLU 48 ? A GLU 55 56 1 Y 1 A ALA 49 ? A ALA 56 57 1 Y 1 A THR 50 ? A THR 57 58 1 Y 1 A ASN 51 ? A ASN 58 59 1 Y 1 A ILE 52 ? A ILE 59 60 1 Y 1 A THR 53 ? A THR 60 61 1 Y 1 A PRO 54 ? A PRO 61 62 1 Y 1 A LYS 55 ? A LYS 62 63 1 Y 1 A ASP 654 ? A ASP 661 64 1 Y 1 A LYS 655 ? A LYS 662 # 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 'N-(4-{[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-gamma-glutamyl-L-gamma-glutamyl-L-glutamic acid' 29C 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 1 801 801 ZN ZN A . C 2 ZN 1 802 802 ZN ZN A . D 3 CA 1 803 803 CA CA A . E 4 CL 1 804 804 CL CL A . F 5 NAG 1 805 805 NAG NAG A . G 5 NAG 2 806 806 NAG NAG A . H 5 NAG 1 807 807 NAG NAG A . I 5 NAG 1 808 808 NAG NAG A . J 5 NAG 2 809 809 NAG NAG A . K 5 NAG 1 810 810 NAG NAG A . L 5 NAG 1 811 811 NAG NAG A . M 5 NAG 1 812 812 NAG NAG A . N 5 NAG 2 813 813 NAG NAG A . O 5 NAG 1 814 814 NAG NAG A . P 5 NAG 2 815 815 NAG NAG A . Q 6 BMA 3 816 816 BMA BMA A . R 7 MAN 4 817 817 MAN MAN A . S 8 29C 1 818 818 29C 29C A . T 9 HOH 1 901 901 HOH HOH A . T 9 HOH 2 902 902 HOH HOH A . T 9 HOH 3 903 903 HOH HOH A . T 9 HOH 4 904 904 HOH HOH A . T 9 HOH 5 905 905 HOH HOH A . T 9 HOH 6 906 906 HOH HOH A . T 9 HOH 7 907 907 HOH HOH A . T 9 HOH 8 908 908 HOH HOH A . T 9 HOH 9 909 909 HOH HOH A . T 9 HOH 10 910 910 HOH HOH A . T 9 HOH 11 911 911 HOH HOH A . T 9 HOH 12 912 912 HOH HOH A . T 9 HOH 13 913 913 HOH HOH A . T 9 HOH 14 914 914 HOH HOH A . T 9 HOH 15 915 915 HOH HOH A . T 9 HOH 16 916 916 HOH HOH A . T 9 HOH 17 917 917 HOH HOH A . T 9 HOH 18 918 918 HOH HOH A . T 9 HOH 19 919 919 HOH HOH A . T 9 HOH 20 920 920 HOH HOH A . T 9 HOH 21 921 921 HOH HOH A . T 9 HOH 22 922 922 HOH HOH A . T 9 HOH 23 923 923 HOH HOH A . T 9 HOH 24 924 924 HOH HOH A . T 9 HOH 25 925 925 HOH HOH A . T 9 HOH 26 926 926 HOH HOH A . T 9 HOH 27 927 927 HOH HOH A . T 9 HOH 28 928 928 HOH HOH A . T 9 HOH 29 929 929 HOH HOH A . T 9 HOH 30 930 930 HOH HOH A . T 9 HOH 31 931 931 HOH HOH A . T 9 HOH 32 932 932 HOH HOH A . T 9 HOH 33 933 933 HOH HOH A . T 9 HOH 34 934 934 HOH HOH A . T 9 HOH 35 935 935 HOH HOH A . T 9 HOH 36 936 936 HOH HOH A . T 9 HOH 37 937 937 HOH HOH A . T 9 HOH 38 938 938 HOH HOH A . T 9 HOH 39 939 939 HOH HOH A . T 9 HOH 40 940 940 HOH HOH A . T 9 HOH 41 941 941 HOH HOH A . T 9 HOH 42 942 942 HOH HOH A . T 9 HOH 43 943 943 HOH HOH A . T 9 HOH 44 944 944 HOH HOH A . T 9 HOH 45 945 945 HOH HOH A . T 9 HOH 46 946 946 HOH HOH A . T 9 HOH 47 947 947 HOH HOH A . T 9 HOH 48 948 948 HOH HOH A . T 9 HOH 49 949 949 HOH HOH A . T 9 HOH 50 950 950 HOH HOH A . T 9 HOH 51 951 951 HOH HOH A . T 9 HOH 52 952 952 HOH HOH A . T 9 HOH 53 953 953 HOH HOH A . T 9 HOH 54 954 954 HOH HOH A . T 9 HOH 55 955 955 HOH HOH A . T 9 HOH 56 956 956 HOH HOH A . T 9 HOH 57 957 957 HOH HOH A . T 9 HOH 58 958 958 HOH HOH A . T 9 HOH 59 959 959 HOH HOH A . T 9 HOH 60 960 960 HOH HOH A . T 9 HOH 61 961 961 HOH HOH A . T 9 HOH 62 962 962 HOH HOH A . T 9 HOH 63 963 963 HOH HOH A . T 9 HOH 64 964 964 HOH HOH A . T 9 HOH 65 965 965 HOH HOH A . T 9 HOH 66 966 966 HOH HOH A . T 9 HOH 67 967 967 HOH HOH A . T 9 HOH 68 968 968 HOH HOH A . T 9 HOH 69 969 969 HOH HOH A . T 9 HOH 70 970 970 HOH HOH A . T 9 HOH 71 971 971 HOH HOH A . T 9 HOH 72 972 972 HOH HOH A . T 9 HOH 73 973 973 HOH HOH A . T 9 HOH 74 974 974 HOH HOH A . T 9 HOH 75 975 975 HOH HOH A . T 9 HOH 76 976 976 HOH HOH A . T 9 HOH 77 977 977 HOH HOH A . T 9 HOH 78 978 978 HOH HOH A . T 9 HOH 79 979 979 HOH HOH A . T 9 HOH 80 980 980 HOH HOH A . T 9 HOH 81 981 981 HOH HOH A . T 9 HOH 82 982 982 HOH HOH A . T 9 HOH 83 983 983 HOH HOH A . T 9 HOH 84 984 984 HOH HOH A . T 9 HOH 85 985 985 HOH HOH A . T 9 HOH 86 986 986 HOH HOH A . T 9 HOH 87 987 987 HOH HOH A . T 9 HOH 88 988 988 HOH HOH A . T 9 HOH 89 989 989 HOH HOH A . T 9 HOH 90 990 990 HOH HOH A . T 9 HOH 91 991 991 HOH HOH A . T 9 HOH 92 992 992 HOH HOH A . T 9 HOH 93 993 993 HOH HOH A . T 9 HOH 94 994 994 HOH HOH A . T 9 HOH 95 995 995 HOH HOH A . T 9 HOH 96 996 996 HOH HOH A . T 9 HOH 97 997 997 HOH HOH A . T 9 HOH 98 998 998 HOH HOH A . T 9 HOH 99 999 999 HOH HOH A . T 9 HOH 100 1000 1000 HOH HOH A . T 9 HOH 101 1001 1001 HOH HOH A . T 9 HOH 102 1002 1002 HOH HOH A . T 9 HOH 103 1003 1003 HOH HOH A . T 9 HOH 104 1004 1004 HOH HOH A . T 9 HOH 105 1005 1005 HOH HOH A . T 9 HOH 106 1006 1006 HOH HOH A . T 9 HOH 107 1007 1007 HOH HOH A . T 9 HOH 108 1008 1008 HOH HOH A . T 9 HOH 109 1009 1009 HOH HOH A . T 9 HOH 110 1010 1010 HOH HOH A . T 9 HOH 111 1011 1011 HOH HOH A . T 9 HOH 112 1012 1012 HOH HOH A . T 9 HOH 113 1013 1013 HOH HOH A . T 9 HOH 114 1014 1014 HOH HOH A . T 9 HOH 115 1015 1015 HOH HOH A . T 9 HOH 116 1016 1016 HOH HOH A . T 9 HOH 117 1017 1017 HOH HOH A . T 9 HOH 118 1018 1018 HOH HOH A . T 9 HOH 119 1019 1019 HOH HOH A . T 9 HOH 120 1020 1020 HOH HOH A . T 9 HOH 121 1021 1021 HOH HOH A . T 9 HOH 122 1022 1022 HOH HOH A . T 9 HOH 123 1023 1023 HOH HOH A . T 9 HOH 124 1024 1024 HOH HOH A . T 9 HOH 125 1025 1025 HOH HOH A . T 9 HOH 126 1026 1026 HOH HOH A . T 9 HOH 127 1027 1027 HOH HOH A . T 9 HOH 128 1028 1028 HOH HOH A . T 9 HOH 129 1029 1029 HOH HOH A . T 9 HOH 130 1030 1030 HOH HOH A . T 9 HOH 131 1031 1031 HOH HOH A . T 9 HOH 132 1032 1032 HOH HOH A . T 9 HOH 133 1033 1033 HOH HOH A . T 9 HOH 134 1034 1034 HOH HOH A . T 9 HOH 135 1035 1035 HOH HOH A . T 9 HOH 136 1036 1036 HOH HOH A . T 9 HOH 137 1037 1037 HOH HOH A . T 9 HOH 138 1038 1038 HOH HOH A . T 9 HOH 139 1039 1039 HOH HOH A . T 9 HOH 140 1040 1040 HOH HOH A . T 9 HOH 141 1041 1041 HOH HOH A . T 9 HOH 142 1042 1042 HOH HOH A . T 9 HOH 143 1043 1043 HOH HOH A . T 9 HOH 144 1044 1044 HOH HOH A . T 9 HOH 145 1045 1045 HOH HOH A . T 9 HOH 146 1046 1046 HOH HOH A . T 9 HOH 147 1047 1047 HOH HOH A . T 9 HOH 148 1048 1048 HOH HOH A . T 9 HOH 149 1049 1049 HOH HOH A . T 9 HOH 150 1050 1050 HOH HOH A . T 9 HOH 151 1051 1051 HOH HOH A . T 9 HOH 152 1052 1052 HOH HOH A . T 9 HOH 153 1053 1053 HOH HOH A . T 9 HOH 154 1054 1054 HOH HOH A . T 9 HOH 155 1055 1055 HOH HOH A . T 9 HOH 156 1056 1056 HOH HOH A . T 9 HOH 157 1057 1057 HOH HOH A . T 9 HOH 158 1058 1058 HOH HOH A . T 9 HOH 159 1059 1059 HOH HOH A . T 9 HOH 160 1060 1060 HOH HOH A . T 9 HOH 161 1061 1061 HOH HOH A . T 9 HOH 162 1062 1062 HOH HOH A . T 9 HOH 163 1063 1063 HOH HOH A . T 9 HOH 164 1064 1064 HOH HOH A . T 9 HOH 165 1065 1065 HOH HOH A . T 9 HOH 166 1066 1066 HOH HOH A . T 9 HOH 167 1067 1067 HOH HOH A . T 9 HOH 168 1068 1068 HOH HOH A . T 9 HOH 169 1069 1069 HOH HOH A . T 9 HOH 170 1070 1070 HOH HOH A . T 9 HOH 171 1071 1071 HOH HOH A . T 9 HOH 172 1072 1072 HOH HOH A . T 9 HOH 173 1073 1073 HOH HOH A . T 9 HOH 174 1074 1074 HOH HOH A . T 9 HOH 175 1075 1075 HOH HOH A . T 9 HOH 176 1076 1076 HOH HOH A . T 9 HOH 177 1077 1077 HOH HOH A . T 9 HOH 178 1078 1078 HOH HOH A . T 9 HOH 179 1079 1079 HOH HOH A . T 9 HOH 180 1080 1080 HOH HOH A . T 9 HOH 181 1081 1081 HOH HOH A . T 9 HOH 182 1082 1082 HOH HOH A . T 9 HOH 183 1083 1083 HOH HOH A . T 9 HOH 184 1084 1084 HOH HOH A . T 9 HOH 185 1085 1085 HOH HOH A . T 9 HOH 186 1086 1086 HOH HOH A . T 9 HOH 187 1087 1087 HOH HOH A . T 9 HOH 188 1088 1088 HOH HOH A . T 9 HOH 189 1089 1089 HOH HOH A . T 9 HOH 190 1090 1090 HOH HOH A . T 9 HOH 191 1091 1091 HOH HOH A . T 9 HOH 192 1092 1092 HOH HOH A . T 9 HOH 193 1093 1093 HOH HOH A . T 9 HOH 194 1094 1094 HOH HOH A . T 9 HOH 195 1095 1095 HOH HOH A . T 9 HOH 196 1096 1096 HOH HOH A . T 9 HOH 197 1097 1097 HOH HOH A . T 9 HOH 198 1098 1098 HOH HOH A . T 9 HOH 199 1099 1099 HOH HOH A . T 9 HOH 200 1100 1100 HOH HOH A . T 9 HOH 201 1101 1101 HOH HOH A . T 9 HOH 202 1102 1102 HOH HOH A . T 9 HOH 203 1103 1103 HOH HOH A . T 9 HOH 204 1104 1104 HOH HOH A . T 9 HOH 205 1105 1105 HOH HOH A . T 9 HOH 206 1106 1106 HOH HOH A . T 9 HOH 207 1107 1107 HOH HOH A . T 9 HOH 208 1108 1108 HOH HOH A . T 9 HOH 209 1109 1109 HOH HOH A . T 9 HOH 210 1110 1110 HOH HOH A . T 9 HOH 211 1111 1111 HOH HOH A . T 9 HOH 212 1112 1112 HOH HOH A . T 9 HOH 213 1113 1113 HOH HOH A . T 9 HOH 214 1114 1114 HOH HOH A . T 9 HOH 215 1115 1115 HOH HOH A . T 9 HOH 216 1116 1116 HOH HOH A . T 9 HOH 217 1117 1117 HOH HOH A . T 9 HOH 218 1118 1118 HOH HOH A . T 9 HOH 219 1119 1119 HOH HOH A . T 9 HOH 220 1120 1120 HOH HOH A . T 9 HOH 221 1121 1121 HOH HOH A . T 9 HOH 222 1122 1122 HOH HOH A . T 9 HOH 223 1123 1123 HOH HOH A . T 9 HOH 224 1124 1124 HOH HOH A . T 9 HOH 225 1125 1125 HOH HOH A . T 9 HOH 226 1126 1126 HOH HOH A . T 9 HOH 227 1127 1127 HOH HOH A . T 9 HOH 228 1128 1128 HOH HOH A . T 9 HOH 229 1129 1129 HOH HOH A . T 9 HOH 230 1130 1130 HOH HOH A . T 9 HOH 231 1131 1131 HOH HOH A . T 9 HOH 232 1132 1132 HOH HOH A . T 9 HOH 233 1133 1133 HOH HOH A . T 9 HOH 234 1134 1134 HOH HOH A . T 9 HOH 235 1135 1135 HOH HOH A . T 9 HOH 236 1136 1136 HOH HOH A . T 9 HOH 237 1137 1137 HOH HOH A . T 9 HOH 238 1138 1138 HOH HOH A . T 9 HOH 239 1139 1139 HOH HOH A . T 9 HOH 240 1140 1140 HOH HOH A . T 9 HOH 241 1141 1141 HOH HOH A . T 9 HOH 242 1142 1142 HOH HOH A . T 9 HOH 243 1143 1143 HOH HOH A . T 9 HOH 244 1144 1144 HOH HOH A . T 9 HOH 245 1145 1145 HOH HOH A . T 9 HOH 246 1146 1146 HOH HOH A . T 9 HOH 247 1147 1147 HOH HOH A . T 9 HOH 248 1148 1148 HOH HOH A . T 9 HOH 249 1149 1149 HOH HOH A . T 9 HOH 250 1150 1150 HOH HOH A . T 9 HOH 251 1151 1151 HOH HOH A . T 9 HOH 252 1152 1152 HOH HOH A . T 9 HOH 253 1153 1153 HOH HOH A . T 9 HOH 254 1154 1154 HOH HOH A . T 9 HOH 255 1155 1155 HOH HOH A . T 9 HOH 256 1156 1156 HOH HOH A . T 9 HOH 257 1157 1157 HOH HOH A . T 9 HOH 258 1158 1158 HOH HOH A . T 9 HOH 259 1159 1159 HOH HOH A . T 9 HOH 260 1160 1160 HOH HOH A . T 9 HOH 261 1161 1161 HOH HOH A . T 9 HOH 262 1162 1162 HOH HOH A . T 9 HOH 263 1163 1163 HOH HOH A . T 9 HOH 264 1164 1164 HOH HOH A . T 9 HOH 265 1165 1165 HOH HOH A . T 9 HOH 266 1166 1166 HOH HOH A . T 9 HOH 267 1167 1167 HOH HOH A . T 9 HOH 268 1168 1168 HOH HOH A . T 9 HOH 269 1169 1169 HOH HOH A . T 9 HOH 270 1170 1170 HOH HOH A . T 9 HOH 271 1171 1171 HOH HOH A . T 9 HOH 272 1172 1172 HOH HOH A . T 9 HOH 273 1173 1173 HOH HOH A . T 9 HOH 274 1174 1174 HOH HOH A . T 9 HOH 275 1175 1175 HOH HOH A . T 9 HOH 276 1176 1176 HOH HOH A . T 9 HOH 277 1177 1177 HOH HOH A . T 9 HOH 278 1178 1178 HOH HOH A . T 9 HOH 279 1179 1179 HOH HOH A . T 9 HOH 280 1180 1180 HOH HOH A . T 9 HOH 281 1181 1181 HOH HOH A . T 9 HOH 282 1182 1182 HOH HOH A . T 9 HOH 283 1183 1183 HOH HOH A . T 9 HOH 284 1184 1184 HOH HOH A . T 9 HOH 285 1185 1185 HOH HOH A . T 9 HOH 286 1186 1186 HOH HOH A . T 9 HOH 287 1187 1187 HOH HOH A . T 9 HOH 288 1188 1188 HOH HOH A . T 9 HOH 289 1189 1189 HOH HOH A . T 9 HOH 290 1190 1190 HOH HOH A . T 9 HOH 291 1191 1191 HOH HOH A . T 9 HOH 292 1192 1192 HOH HOH A . T 9 HOH 293 1193 1193 HOH HOH A . T 9 HOH 294 1194 1194 HOH HOH A . T 9 HOH 295 1195 1195 HOH HOH A . T 9 HOH 296 1196 1196 HOH HOH A . T 9 HOH 297 1197 1197 HOH HOH A . T 9 HOH 298 1198 1198 HOH HOH A . T 9 HOH 299 1199 1199 HOH HOH A . T 9 HOH 300 1200 1200 HOH HOH A . T 9 HOH 301 1201 1201 HOH HOH A . T 9 HOH 302 1202 1202 HOH HOH A . T 9 HOH 303 1203 1203 HOH HOH A . T 9 HOH 304 1204 1204 HOH HOH A . T 9 HOH 305 1205 1205 HOH HOH A . T 9 HOH 306 1206 1206 HOH HOH A . T 9 HOH 307 1207 1207 HOH HOH A . T 9 HOH 308 1208 1208 HOH HOH A . T 9 HOH 309 1209 1209 HOH HOH A . T 9 HOH 310 1210 1210 HOH HOH A . T 9 HOH 311 1211 1211 HOH HOH A . T 9 HOH 312 1212 1212 HOH HOH A . T 9 HOH 313 1213 1213 HOH HOH A . T 9 HOH 314 1214 1214 HOH HOH A . T 9 HOH 315 1215 1215 HOH HOH A . T 9 HOH 316 1216 1216 HOH HOH A . T 9 HOH 317 1217 1217 HOH HOH A . T 9 HOH 318 1218 1218 HOH HOH A . T 9 HOH 319 1219 1219 HOH HOH A . T 9 HOH 320 1220 1220 HOH HOH A . T 9 HOH 321 1221 1221 HOH HOH A . T 9 HOH 322 1222 1222 HOH HOH A . T 9 HOH 323 1223 1223 HOH HOH A . T 9 HOH 324 1224 1224 HOH HOH A . T 9 HOH 325 1225 1225 HOH HOH A . T 9 HOH 326 1226 1226 HOH HOH A . T 9 HOH 327 1227 1227 HOH HOH A . T 9 HOH 328 1228 1228 HOH HOH A . T 9 HOH 329 1229 1229 HOH HOH A . T 9 HOH 330 1230 1230 HOH HOH A . T 9 HOH 331 1231 1231 HOH HOH A . T 9 HOH 332 1232 1232 HOH HOH A . T 9 HOH 333 1233 1233 HOH HOH A . T 9 HOH 334 1234 1234 HOH HOH A . T 9 HOH 335 1235 1235 HOH HOH A . T 9 HOH 336 1236 1236 HOH HOH A . T 9 HOH 337 1237 1237 HOH HOH A . T 9 HOH 338 1238 1238 HOH HOH A . T 9 HOH 339 1239 1239 HOH HOH A . T 9 HOH 340 1240 1240 HOH HOH A . T 9 HOH 341 1241 1241 HOH HOH A . T 9 HOH 342 1242 1242 HOH HOH A . T 9 HOH 343 1243 1243 HOH HOH A . T 9 HOH 344 1244 1244 HOH HOH A . T 9 HOH 345 1245 1245 HOH HOH A . T 9 HOH 346 1246 1246 HOH HOH A . T 9 HOH 347 1247 1247 HOH HOH A . T 9 HOH 348 1248 1248 HOH HOH A . T 9 HOH 349 1249 1249 HOH HOH A . T 9 HOH 350 1250 1250 HOH HOH A . T 9 HOH 351 1251 1251 HOH HOH A . T 9 HOH 352 1252 1252 HOH HOH A . T 9 HOH 353 1253 1253 HOH HOH A . T 9 HOH 354 1254 1254 HOH HOH A . T 9 HOH 355 1255 1255 HOH HOH A . T 9 HOH 356 1256 1256 HOH HOH A . T 9 HOH 357 1257 1257 HOH HOH A . T 9 HOH 358 1258 1258 HOH HOH A . T 9 HOH 359 1259 1259 HOH HOH A . T 9 HOH 360 1260 1260 HOH HOH A . T 9 HOH 361 1261 1261 HOH HOH A . T 9 HOH 362 1262 1262 HOH HOH A . T 9 HOH 363 1263 1263 HOH HOH A . T 9 HOH 364 1264 1264 HOH HOH A . T 9 HOH 365 1265 1265 HOH HOH A . T 9 HOH 366 1266 1266 HOH HOH A . T 9 HOH 367 1267 1267 HOH HOH A . T 9 HOH 368 1268 1268 HOH HOH A . T 9 HOH 369 1269 1269 HOH HOH A . T 9 HOH 370 1270 1270 HOH HOH A . T 9 HOH 371 1271 1271 HOH HOH A . T 9 HOH 372 1272 1272 HOH HOH A . T 9 HOH 373 1273 1273 HOH HOH A . T 9 HOH 374 1274 1274 HOH HOH A . T 9 HOH 375 1275 1275 HOH HOH A . T 9 HOH 376 1276 1276 HOH HOH A . T 9 HOH 377 1277 1277 HOH HOH A . T 9 HOH 378 1278 1278 HOH HOH A . T 9 HOH 379 1279 1279 HOH HOH A . T 9 HOH 380 1280 1280 HOH HOH A . T 9 HOH 381 1281 1281 HOH HOH A . T 9 HOH 382 1282 1282 HOH HOH A . T 9 HOH 383 1283 1283 HOH HOH A . T 9 HOH 384 1284 1284 HOH HOH A . T 9 HOH 385 1285 1285 HOH HOH A . T 9 HOH 386 1286 1286 HOH HOH A . T 9 HOH 387 1287 1287 HOH HOH A . T 9 HOH 388 1288 1288 HOH HOH A . T 9 HOH 389 1289 1289 HOH HOH A . T 9 HOH 390 1290 1290 HOH HOH A . T 9 HOH 391 1291 1291 HOH HOH A . T 9 HOH 392 1292 1292 HOH HOH A . T 9 HOH 393 1293 1293 HOH HOH A . T 9 HOH 394 1294 1294 HOH HOH A . T 9 HOH 395 1295 1295 HOH HOH A . T 9 HOH 396 1296 1296 HOH HOH A . T 9 HOH 397 1297 1297 HOH HOH A . T 9 HOH 398 1298 1298 HOH HOH A . T 9 HOH 399 1299 1299 HOH HOH A . T 9 HOH 400 1300 1300 HOH HOH A . T 9 HOH 401 1301 1301 HOH HOH A . T 9 HOH 402 1302 1302 HOH HOH A . T 9 HOH 403 1303 1303 HOH HOH A . T 9 HOH 404 1304 1304 HOH HOH A . T 9 HOH 405 1305 1305 HOH HOH A . T 9 HOH 406 1306 1306 HOH HOH A . T 9 HOH 407 1307 1307 HOH HOH A . T 9 HOH 408 1308 1308 HOH HOH A . T 9 HOH 409 1309 1309 HOH HOH A . T 9 HOH 410 1310 1310 HOH HOH A . T 9 HOH 411 1311 1311 HOH HOH A . T 9 HOH 412 1312 1312 HOH HOH A . T 9 HOH 413 1313 1313 HOH HOH A . T 9 HOH 414 1314 1314 HOH HOH A . T 9 HOH 415 1315 1315 HOH HOH A . T 9 HOH 416 1316 1316 HOH HOH A . T 9 HOH 417 1317 1317 HOH HOH A . T 9 HOH 418 1318 1318 HOH HOH A . T 9 HOH 419 1319 1319 HOH HOH A . T 9 HOH 420 1320 1320 HOH HOH A . T 9 HOH 421 1321 1321 HOH HOH A . T 9 HOH 422 1322 1322 HOH HOH A . T 9 HOH 423 1323 1323 HOH HOH A . T 9 HOH 424 1324 1324 HOH HOH A . T 9 HOH 425 1325 1325 HOH HOH A . T 9 HOH 426 1326 1326 HOH HOH A . T 9 HOH 427 1327 1327 HOH HOH A . T 9 HOH 428 1328 1328 HOH HOH A . T 9 HOH 429 1329 1329 HOH HOH A . T 9 HOH 430 1330 1330 HOH HOH A . T 9 HOH 431 1331 1331 HOH HOH A . T 9 HOH 432 1332 1332 HOH HOH A . T 9 HOH 433 1333 1333 HOH HOH A . T 9 HOH 434 1334 1334 HOH HOH A . T 9 HOH 435 1335 1335 HOH HOH A . T 9 HOH 436 1336 1336 HOH HOH A . T 9 HOH 437 1337 1337 HOH HOH A . T 9 HOH 438 1338 1338 HOH HOH A . T 9 HOH 439 1339 1339 HOH HOH A . T 9 HOH 440 1340 1340 HOH HOH A . T 9 HOH 441 1341 1341 HOH HOH A . T 9 HOH 442 1342 1342 HOH HOH A . T 9 HOH 443 1343 1343 HOH HOH A . T 9 HOH 444 1344 1344 HOH HOH A . T 9 HOH 445 1345 1345 HOH HOH A . T 9 HOH 446 1346 1346 HOH HOH A . T 9 HOH 447 1347 1347 HOH HOH A . T 9 HOH 448 1348 1348 HOH HOH A . T 9 HOH 449 1349 1349 HOH HOH A . T 9 HOH 450 1350 1350 HOH HOH A . T 9 HOH 451 1351 1351 HOH HOH A . T 9 HOH 452 1352 1352 HOH HOH A . T 9 HOH 453 1353 1353 HOH HOH A . T 9 HOH 454 1354 1354 HOH HOH A . T 9 HOH 455 1355 1355 HOH HOH A . T 9 HOH 456 1356 1356 HOH HOH A . T 9 HOH 457 1357 1357 HOH HOH A . T 9 HOH 458 1358 1358 HOH HOH A . T 9 HOH 459 1359 1359 HOH HOH A . T 9 HOH 460 1360 1360 HOH HOH A . T 9 HOH 461 1361 1361 HOH HOH A . T 9 HOH 462 1362 1362 HOH HOH A . T 9 HOH 463 1363 1363 HOH HOH A . T 9 HOH 464 1364 1364 HOH HOH A . T 9 HOH 465 1365 1365 HOH HOH A . T 9 HOH 466 1366 1366 HOH HOH A . T 9 HOH 467 1367 1367 HOH HOH A . T 9 HOH 468 1368 1368 HOH HOH A . T 9 HOH 469 1369 1369 HOH HOH A . T 9 HOH 470 1370 1370 HOH HOH A . T 9 HOH 471 1371 1371 HOH HOH A . T 9 HOH 472 1372 1372 HOH HOH A . T 9 HOH 473 1373 1373 HOH HOH A . T 9 HOH 474 1374 1374 HOH HOH A . T 9 HOH 475 1375 1375 HOH HOH A . T 9 HOH 476 1376 1376 HOH HOH A . T 9 HOH 477 1377 1377 HOH HOH A . T 9 HOH 478 1378 1378 HOH HOH A . T 9 HOH 479 1379 1379 HOH HOH A . T 9 HOH 480 1380 1380 HOH HOH A . T 9 HOH 481 1381 1381 HOH HOH A . T 9 HOH 482 1382 1382 HOH HOH A . T 9 HOH 483 1383 1383 HOH HOH A . T 9 HOH 484 1384 1384 HOH HOH A . T 9 HOH 485 1385 1385 HOH HOH A . T 9 HOH 486 1386 1386 HOH HOH A . T 9 HOH 487 1387 1387 HOH HOH A . T 9 HOH 488 1388 1388 HOH HOH A . T 9 HOH 489 1389 1389 HOH HOH A . T 9 HOH 490 1390 1390 HOH HOH A . T 9 HOH 491 1391 1391 HOH HOH A . T 9 HOH 492 1392 1392 HOH HOH A . T 9 HOH 493 1393 1393 HOH HOH A . T 9 HOH 494 1394 1394 HOH HOH A . T 9 HOH 495 1395 1395 HOH HOH A . T 9 HOH 496 1396 1396 HOH HOH A . T 9 HOH 497 1397 1397 HOH HOH A . T 9 HOH 498 1398 1398 HOH HOH A . T 9 HOH 499 1399 1399 HOH HOH A . T 9 HOH 500 1400 1400 HOH HOH A . T 9 HOH 501 1401 1401 HOH HOH A . T 9 HOH 502 1402 1402 HOH HOH A . T 9 HOH 503 1403 1403 HOH HOH A . T 9 HOH 504 1404 1404 HOH HOH A . T 9 HOH 505 1405 1405 HOH HOH A . T 9 HOH 506 1406 1406 HOH HOH A . T 9 HOH 507 1407 1407 HOH HOH A . T 9 HOH 508 1408 1408 HOH HOH A . T 9 HOH 509 1409 1409 HOH HOH A . T 9 HOH 510 1410 1410 HOH HOH A . T 9 HOH 511 1411 1411 HOH HOH A . T 9 HOH 512 1412 1412 HOH HOH A . T 9 HOH 513 1413 1413 HOH HOH A . T 9 HOH 514 1414 1414 HOH HOH A . T 9 HOH 515 1415 1415 HOH HOH A . T 9 HOH 516 1416 1416 HOH HOH A . T 9 HOH 517 1417 1417 HOH HOH A . T 9 HOH 518 1418 1418 HOH HOH A . T 9 HOH 519 1419 1419 HOH HOH A . T 9 HOH 520 1420 1420 HOH HOH A . T 9 HOH 521 1421 1421 HOH HOH A . #