data_4MCS # _entry.id 4MCS # _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 4MCS RCSB RCSB081748 WWPDB D_1000081748 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4MCP . unspecified PDB 4MCQ . unspecified PDB 4MCR . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MCS _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 'Ptacek, J.' 1 'Barinka, C.' 2 'Sacha, P.' 3 'Navratil, M.' 4 # _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 4MCS _cell.length_a 101.547 _cell.length_b 130.395 _cell.length_c 158.980 _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 4MCS _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' 85055.977 1 3.4.17.21 H475Y 'Glutamate carboxypeptidase II, unp residues 44-750' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 11 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 5 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 6 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 7 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 8 non-polymer syn 'GLUTAMIC ACID' 147.129 1 ? ? ? ? 9 non-polymer syn 'ASPARTIC ACID' 133.103 1 ? ? ? ? 10 water nat water 18.015 584 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ;Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Membrane glutamate carboxypeptidase, mGCP, N-acetylated-alpha-linked acidic dipeptidase I, NAALADase I, Prostate-specific membrane antigen, PSM, PSMA, Pteroylpoly-gamma-glutamate carboxypeptidase ; # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;MKLCILLAVVAFVGLSLGRSGLNDIFEAQKIEWHEGSGSGSENLYFQGRSKSSNEATNITPKHNMKAFLDELKAENIKKF LYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYEN VSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPAD YFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSA PPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAA VVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSL VYNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYH SVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLF SAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALF DIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_seq_one_letter_code_can ;MKLCILLAVVAFVGLSLGRSGLNDIFEAQKIEWHEGSGSGSENLYFQGRSKSSNEATNITPKHNMKAFLDELKAENIKKF LYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYEN VSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPAD YFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSA PPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAA VVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSL VYNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYH 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 GLU 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 TYR 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 ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ;Schneider's S2 ; _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 4MCS _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 4MCS MET A 1 ? UNP Q04609 ? ? 'INITIATING METHIONINE' -6 1 1 4MCS LYS A 2 ? UNP Q04609 ? ? 'EXPRESSION TAG' -5 2 1 4MCS LEU A 3 ? UNP Q04609 ? ? 'EXPRESSION TAG' -4 3 1 4MCS CYS A 4 ? UNP Q04609 ? ? 'EXPRESSION TAG' -3 4 1 4MCS ILE A 5 ? UNP Q04609 ? ? 'EXPRESSION TAG' -2 5 1 4MCS LEU A 6 ? UNP Q04609 ? ? 'EXPRESSION TAG' -1 6 1 4MCS LEU A 7 ? UNP Q04609 ? ? 'EXPRESSION TAG' 0 7 1 4MCS ALA A 8 ? UNP Q04609 ? ? 'EXPRESSION TAG' 1 8 1 4MCS VAL A 9 ? UNP Q04609 ? ? 'EXPRESSION TAG' 2 9 1 4MCS VAL A 10 ? UNP Q04609 ? ? 'EXPRESSION TAG' 3 10 1 4MCS ALA A 11 ? UNP Q04609 ? ? 'EXPRESSION TAG' 4 11 1 4MCS PHE A 12 ? UNP Q04609 ? ? 'EXPRESSION TAG' 5 12 1 4MCS VAL A 13 ? UNP Q04609 ? ? 'EXPRESSION TAG' 6 13 1 4MCS GLY A 14 ? UNP Q04609 ? ? 'EXPRESSION TAG' 7 14 1 4MCS LEU A 15 ? UNP Q04609 ? ? 'EXPRESSION TAG' 8 15 1 4MCS SER A 16 ? UNP Q04609 ? ? 'EXPRESSION TAG' 9 16 1 4MCS LEU A 17 ? UNP Q04609 ? ? 'EXPRESSION TAG' 10 17 1 4MCS GLY A 18 ? UNP Q04609 ? ? 'EXPRESSION TAG' 11 18 1 4MCS ARG A 19 ? UNP Q04609 ? ? 'EXPRESSION TAG' 12 19 1 4MCS SER A 20 ? UNP Q04609 ? ? 'EXPRESSION TAG' 13 20 1 4MCS GLY A 21 ? UNP Q04609 ? ? 'EXPRESSION TAG' 14 21 1 4MCS LEU A 22 ? UNP Q04609 ? ? 'EXPRESSION TAG' 15 22 1 4MCS ASN A 23 ? UNP Q04609 ? ? 'EXPRESSION TAG' 16 23 1 4MCS ASP A 24 ? UNP Q04609 ? ? 'EXPRESSION TAG' 17 24 1 4MCS ILE A 25 ? UNP Q04609 ? ? 'EXPRESSION TAG' 18 25 1 4MCS PHE A 26 ? UNP Q04609 ? ? 'EXPRESSION TAG' 19 26 1 4MCS GLU A 27 ? UNP Q04609 ? ? 'EXPRESSION TAG' 20 27 1 4MCS ALA A 28 ? UNP Q04609 ? ? 'EXPRESSION TAG' 21 28 1 4MCS GLN A 29 ? UNP Q04609 ? ? 'EXPRESSION TAG' 22 29 1 4MCS LYS A 30 ? UNP Q04609 ? ? 'EXPRESSION TAG' 23 30 1 4MCS ILE A 31 ? UNP Q04609 ? ? 'EXPRESSION TAG' 24 31 1 4MCS GLU A 32 ? UNP Q04609 ? ? 'EXPRESSION TAG' 25 32 1 4MCS TRP A 33 ? UNP Q04609 ? ? 'EXPRESSION TAG' 26 33 1 4MCS HIS A 34 ? UNP Q04609 ? ? 'EXPRESSION TAG' 27 34 1 4MCS GLU A 35 ? UNP Q04609 ? ? 'EXPRESSION TAG' 28 35 1 4MCS GLY A 36 ? UNP Q04609 ? ? 'EXPRESSION TAG' 29 36 1 4MCS SER A 37 ? UNP Q04609 ? ? 'EXPRESSION TAG' 30 37 1 4MCS GLY A 38 ? UNP Q04609 ? ? 'EXPRESSION TAG' 31 38 1 4MCS SER A 39 ? UNP Q04609 ? ? 'EXPRESSION TAG' 32 39 1 4MCS GLY A 40 ? UNP Q04609 ? ? 'EXPRESSION TAG' 33 40 1 4MCS SER A 41 ? UNP Q04609 ? ? 'EXPRESSION TAG' 34 41 1 4MCS GLU A 42 ? UNP Q04609 ? ? 'EXPRESSION TAG' 35 42 1 4MCS ASN A 43 ? UNP Q04609 ? ? 'EXPRESSION TAG' 36 43 1 4MCS LEU A 44 ? UNP Q04609 ? ? 'EXPRESSION TAG' 37 44 1 4MCS TYR A 45 ? UNP Q04609 ? ? 'EXPRESSION TAG' 38 45 1 4MCS PHE A 46 ? UNP Q04609 ? ? 'EXPRESSION TAG' 39 46 1 4MCS GLN A 47 ? UNP Q04609 ? ? 'EXPRESSION TAG' 40 47 1 4MCS GLY A 48 ? UNP Q04609 ? ? 'EXPRESSION TAG' 41 48 1 4MCS ARG A 49 ? UNP Q04609 ? ? 'EXPRESSION TAG' 42 49 1 4MCS SER A 50 ? UNP Q04609 ? ? 'EXPRESSION TAG' 43 50 1 4MCS TYR A 482 ? UNP Q04609 HIS 475 'ENGINEERED MUTATION' 475 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 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 4MCS _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.09 _exptl_crystal.density_percent_sol 60.24 _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 2010-12-18 _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 4MCS _reflns.observed_criterion_sigma_I -3 _reflns.observed_criterion_sigma_F -3 _reflns.d_resolution_low 30 _reflns.d_resolution_high 1.83 _reflns.number_obs 86816 _reflns.number_all 86816 _reflns.percent_possible_obs 93.3 _reflns.pdbx_Rmerge_I_obs 0.067 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 16.5 _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 1.83 _reflns_shell.d_res_low 1.90 _reflns_shell.percent_possible_all 88.3 _reflns_shell.Rmerge_I_obs 0.429 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.1 _reflns_shell.pdbx_redundancy 2.9 _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 4MCS _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 84871 _refine.ls_number_reflns_all 84871 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 28.53 _refine.ls_d_res_high 1.83 _refine.ls_percent_reflns_obs 92.97 _refine.ls_R_factor_obs 0.15924 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.15858 _refine.ls_R_factor_R_free 0.19058 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 2.0 _refine.ls_number_reflns_R_free 1736 _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 0.952 _refine.B_iso_mean 31.482 _refine.aniso_B[1][1] 0.00 _refine.aniso_B[2][2] 0.00 _refine.aniso_B[3][3] 0.00 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct '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 0.099 _refine.pdbx_overall_ESU_R_Free 0.099 _refine.overall_SU_ML 0.067 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 4.916 _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 5501 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 199 _refine_hist.number_atoms_solvent 584 _refine_hist.number_atoms_total 6284 _refine_hist.d_res_high 1.83 _refine_hist.d_res_low 28.53 # 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 0.019 0.022 ? 6074 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.605 1.994 ? 8255 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.029 5.000 ? 717 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.528 23.868 ? 287 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.574 15.000 ? 1000 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 17.940 15.000 ? 36 'X-RAY DIFFRACTION' ? r_chiral_restr 0.120 0.200 ? 890 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.009 0.021 ? 4668 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 0.855 1.500 ? 3536 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.409 2.000 ? 5745 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.469 3.000 ? 2538 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 3.877 4.500 ? 2502 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.828 _refine_ls_shell.d_res_low 1.875 _refine_ls_shell.number_reflns_R_work 5750 _refine_ls_shell.R_factor_R_work 0.251 _refine_ls_shell.percent_reflns_obs 86.05 _refine_ls_shell.R_factor_R_free 0.284 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 122 _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 4MCS _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 4MCS _struct.title 'A high resolution structure of human glutamate carboxypeptidase II (GCPII) His475Tyr variant in complex with 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 4MCS _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'zinc metallopeptidase, GCPII, Prostate specific membrane antigen, folate hydrolase 1, FOLH1, HYDROLASE' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 2 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 2 ? I N N 2 ? J N N 2 ? K N N 2 ? L N N 2 ? M N N 3 ? N N N 4 ? O N N 5 ? P N N 5 ? Q N N 6 ? R N N 7 ? S N N 8 ? T N N 9 ? U N N 10 ? # _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 ? ASN A 445 ? LEU A 428 ASN A 438 1 ? 11 HELX_P HELX_P14 14 ASN A 445 ? ARG A 452 ? ASN A 438 ARG A 445 1 ? 8 HELX_P HELX_P15 15 MET A 477 ? LEU A 488 ? MET A 470 LEU A 481 1 ? 12 HELX_P HELX_P16 16 SER A 499 ? SER A 508 ? SER A 492 SER A 501 1 ? 10 HELX_P HELX_P17 17 PHE A 528 ? GLN A 533 ? PHE A 521 GLN A 526 1 ? 6 HELX_P HELX_P18 18 THR A 565 ? TYR A 573 ? THR A 558 TYR A 566 1 ? 9 HELX_P HELX_P19 19 PHE A 577 ? SER A 597 ? PHE A 570 SER A 590 1 ? 21 HELX_P HELX_P20 20 ASP A 603 ? MET A 623 ? ASP A 596 MET A 616 1 ? 21 HELX_P HELX_P21 21 HIS A 625 ? TYR A 632 ? HIS A 618 TYR A 625 1 ? 8 HELX_P HELX_P22 22 PHE A 636 ? PHE A 660 ? PHE A 629 PHE A 653 1 ? 25 HELX_P HELX_P23 23 ASN A 664 ? PHE A 682 ? ASN A 657 PHE A 675 1 ? 19 HELX_P HELX_P24 24 PHE A 712 ? PHE A 720 ? PHE A 705 PHE A 713 1 ? 9 HELX_P HELX_P25 25 ASP A 721 ? LYS A 725 ? ASP A 714 LYS A 718 5 ? 5 HELX_P HELX_P26 26 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 83 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 76 A NAG 801 1_555 ? ? ? ? ? ? ? 1.426 ? covale2 covale ? ? A ASN 483 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 476 A NAG 808 1_555 ? ? ? ? ? ? ? 1.427 ? covale3 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 808 A NAG 809 1_555 ? ? ? ? ? ? ? 1.431 ? covale4 covale ? ? K NAG . O4 ? ? ? 1_555 L NAG . C1 ? ? A NAG 810 A NAG 811 1_555 ? ? ? ? ? ? ? 1.433 ? covale5 covale ? ? L NAG . O4 ? ? ? 1_555 M BMA . C1 ? ? A NAG 811 A BMA 812 1_555 ? ? ? ? ? ? ? 1.438 ? covale6 covale ? ? A ASN 645 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 638 A NAG 810 1_555 ? ? ? ? ? ? ? 1.440 ? covale7 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 804 A NAG 805 1_555 ? ? ? ? ? ? ? 1.443 ? covale8 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 801 A NAG 802 1_555 ? ? ? ? ? ? ? 1.444 ? covale9 covale ? ? A ASN 202 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 195 A NAG 806 1_555 ? ? ? ? ? ? ? 1.450 ? covale10 covale ? ? M BMA . O3 ? ? ? 1_555 N MAN . C1 ? ? A BMA 812 A MAN 813 1_555 ? ? ? ? ? ? ? 1.450 ? covale11 covale ? ? A ASN 147 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 140 A NAG 804 1_555 ? ? ? ? ? ? ? 1.451 ? covale12 covale ? ? A ASN 466 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 459 A NAG 807 1_555 ? ? ? ? ? ? ? 1.454 ? covale13 covale ? ? A ASN 128 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 121 A NAG 803 1_555 ? ? ? ? ? ? ? 1.457 ? metalc1 metalc ? ? P ZN . ZN ? ? ? 1_555 U HOH . O ? ? A ZN 815 A HOH 1454 1_555 ? ? ? ? ? ? ? 1.847 ? metalc2 metalc ? ? A HIS 384 NE2 ? ? ? 1_555 P ZN . ZN ? ? A HIS 377 A ZN 815 1_555 ? ? ? ? ? ? ? 1.966 ? metalc3 metalc ? ? A ASP 394 OD1 ? ? ? 1_555 P ZN . ZN ? ? A ASP 387 A ZN 815 1_555 ? ? ? ? ? ? ? 1.983 ? metalc4 metalc ? ? A ASP 460 OD2 ? ? ? 1_555 P ZN . ZN ? ? A ASP 453 A ZN 815 1_555 ? ? ? ? ? ? ? 2.000 ? metalc5 metalc ? ? A HIS 560 NE2 ? ? ? 1_555 O ZN . ZN ? ? A HIS 553 A ZN 814 1_555 ? ? ? ? ? ? ? 2.033 ? metalc6 metalc ? ? A GLU 432 OE2 ? ? ? 1_555 O ZN . ZN ? ? A GLU 425 A ZN 814 1_555 ? ? ? ? ? ? ? 2.057 ? metalc7 metalc ? ? A ASP 394 OD2 ? ? ? 1_555 O ZN . ZN ? ? A ASP 387 A ZN 814 1_555 ? ? ? ? ? ? ? 2.083 ? metalc8 metalc ? ? O ZN . ZN ? ? ? 1_555 U HOH . O ? ? A ZN 814 A HOH 1454 1_555 ? ? ? ? ? ? ? 2.123 ? metalc9 metalc ? ? A GLU 443 OE2 ? ? ? 1_555 Q CA . CA ? ? A GLU 436 A CA 816 1_555 ? ? ? ? ? ? ? 2.291 ? metalc10 metalc ? ? A TYR 279 O ? ? ? 1_555 Q CA . CA ? ? A TYR 272 A CA 816 1_555 ? ? ? ? ? ? ? 2.300 ? metalc11 metalc ? ? Q CA . CA ? ? ? 1_555 U HOH . O ? ? A CA 816 A HOH 906 1_555 ? ? ? ? ? ? ? 2.408 ? metalc12 metalc ? ? A THR 276 O ? ? ? 1_555 Q CA . CA ? ? A THR 269 A CA 816 1_555 ? ? ? ? ? ? ? 2.413 ? metalc13 metalc ? ? A GLU 440 OE1 ? ? ? 1_555 Q CA . CA ? ? A GLU 433 A CA 816 1_555 ? ? ? ? ? ? ? 2.435 ? metalc14 metalc ? ? A GLU 432 OE1 ? ? ? 1_555 O ZN . ZN ? ? A GLU 425 A ZN 814 1_555 ? ? ? ? ? ? ? 2.442 ? metalc15 metalc ? ? A GLU 440 OE2 ? ? ? 1_555 Q CA . CA ? ? A GLU 433 A CA 816 1_555 ? ? ? ? ? ? ? 2.516 ? metalc16 metalc ? ? A THR 276 OG1 ? ? ? 1_555 Q CA . CA ? ? A THR 269 A CA 816 1_555 ? ? ? ? ? ? ? 2.528 ? # 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 9.86 2 GLY 337 A . ? GLY 330 A PRO 338 A ? PRO 331 A 1 -4.08 3 ASP 394 A . ? ASP 387 A PRO 395 A ? PRO 388 A 1 5.75 # 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 ALA A 700 ? N ALA A 693 O GLU A 710 ? O GLU A 703 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 801' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 802' AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 803' AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 804' AC5 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 805' AC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 806' AC7 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 807' AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 808' AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 809' BC1 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 810' BC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 811' BC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE BMA A 812' BC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE MAN A 813' BC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ZN A 814' BC6 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE ZN A 815' BC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 816' BC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CL A 817' BC9 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE GLU A 818' CC1 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE ASP A 819' # 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 9 ASN A 83 ? ASN A 76 . ? 1_555 ? 2 AC1 9 GLN A 102 ? GLN A 95 . ? 1_555 ? 3 AC1 9 GLN A 106 ? GLN A 99 . ? 1_555 ? 4 AC1 9 NAG C . ? NAG A 802 . ? 1_555 ? 5 AC1 9 HOH U . ? HOH A 1146 . ? 1_555 ? 6 AC1 9 HOH U . ? HOH A 1184 . ? 1_555 ? 7 AC1 9 HOH U . ? HOH A 1302 . ? 1_555 ? 8 AC1 9 HOH U . ? HOH A 1336 . ? 1_555 ? 9 AC1 9 HOH U . ? HOH A 1401 . ? 1_555 ? 10 AC2 3 NAG B . ? NAG A 801 . ? 1_555 ? 11 AC2 3 HOH U . ? HOH A 1155 . ? 1_555 ? 12 AC2 3 HOH U . ? HOH A 1401 . ? 1_555 ? 13 AC3 4 ASN A 128 ? ASN A 121 . ? 1_555 ? 14 AC3 4 HIS A 131 ? HIS A 124 . ? 1_555 ? 15 AC3 4 THR A 356 ? THR A 349 . ? 1_555 ? 16 AC3 4 HOH U . ? HOH A 1216 . ? 1_555 ? 17 AC4 6 TYR A 134 ? TYR A 127 . ? 1_555 ? 18 AC4 6 GLU A 144 ? GLU A 137 . ? 1_555 ? 19 AC4 6 ILE A 145 ? ILE A 138 . ? 1_555 ? 20 AC4 6 ASN A 147 ? ASN A 140 . ? 1_555 ? 21 AC4 6 NAG F . ? NAG A 805 . ? 1_555 ? 22 AC4 6 HOH U . ? HOH A 1360 . ? 1_555 ? 23 AC5 2 NAG E . ? NAG A 804 . ? 1_555 ? 24 AC5 2 HOH U . ? HOH A 1284 . ? 1_555 ? 25 AC6 2 ASN A 202 ? ASN A 195 . ? 1_555 ? 26 AC6 2 SER A 204 ? SER A 197 . ? 1_555 ? 27 AC7 9 TRP A 253 ? TRP A 246 . ? 1_555 ? 28 AC7 9 ASN A 466 ? ASN A 459 . ? 1_555 ? 29 AC7 9 PHE A 572 ? PHE A 565 . ? 1_555 ? 30 AC7 9 TYR A 573 ? TYR A 566 . ? 1_555 ? 31 AC7 9 HOH U . ? HOH A 977 . ? 1_555 ? 32 AC7 9 HOH U . ? HOH A 1171 . ? 1_555 ? 33 AC7 9 HOH U . ? HOH A 1217 . ? 1_555 ? 34 AC7 9 HOH U . ? HOH A 1275 . ? 1_555 ? 35 AC7 9 HOH U . ? HOH A 1369 . ? 1_555 ? 36 AC8 4 SER A 479 ? SER A 472 . ? 1_555 ? 37 AC8 4 ASN A 483 ? ASN A 476 . ? 1_555 ? 38 AC8 4 NAG J . ? NAG A 809 . ? 1_555 ? 39 AC8 4 HOH U . ? HOH A 1223 . ? 1_555 ? 40 AC9 3 GLN A 658 ? GLN A 651 . ? 1_555 ? 41 AC9 3 NAG I . ? NAG A 808 . ? 1_555 ? 42 AC9 3 HOH U . ? HOH A 1117 . ? 1_555 ? 43 BC1 9 TYR A 284 ? TYR A 277 . ? 2_565 ? 44 BC1 9 SER A 638 ? SER A 631 . ? 1_555 ? 45 BC1 9 SER A 641 ? SER A 634 . ? 1_555 ? 46 BC1 9 ASN A 645 ? ASN A 638 . ? 1_555 ? 47 BC1 9 GLN A 747 ? GLN A 740 . ? 1_555 ? 48 BC1 9 NAG L . ? NAG A 811 . ? 1_555 ? 49 BC1 9 HOH U . ? HOH A 1025 . ? 1_555 ? 50 BC1 9 HOH U . ? HOH A 1059 . ? 2_565 ? 51 BC1 9 HOH U . ? HOH A 1250 . ? 1_555 ? 52 BC2 3 GLU A 283 ? GLU A 276 . ? 2_565 ? 53 BC2 3 NAG K . ? NAG A 810 . ? 1_555 ? 54 BC2 3 BMA M . ? BMA A 812 . ? 1_555 ? 55 BC3 5 HIS A 119 ? HIS A 112 . ? 2_565 ? 56 BC3 5 GLU A 283 ? GLU A 276 . ? 2_565 ? 57 BC3 5 ARG A 361 ? ARG A 354 . ? 2_565 ? 58 BC3 5 NAG L . ? NAG A 811 . ? 1_555 ? 59 BC3 5 MAN N . ? MAN A 813 . ? 1_555 ? 60 BC4 8 PHE A 242 ? PHE A 235 . ? 7_555 ? 61 BC4 8 SER A 248 ? SER A 241 . ? 7_555 ? 62 BC4 8 GLU A 283 ? GLU A 276 . ? 2_565 ? 63 BC4 8 BMA M . ? BMA A 812 . ? 1_555 ? 64 BC4 8 HOH U . ? HOH A 1090 . ? 1_555 ? 65 BC4 8 HOH U . ? HOH A 1248 . ? 1_555 ? 66 BC4 8 HOH U . ? HOH A 1251 . ? 7_555 ? 67 BC4 8 HOH U . ? HOH A 1423 . ? 7_555 ? 68 BC5 6 ASP A 394 ? ASP A 387 . ? 1_555 ? 69 BC5 6 GLU A 432 ? GLU A 425 . ? 1_555 ? 70 BC5 6 HIS A 560 ? HIS A 553 . ? 1_555 ? 71 BC5 6 ZN P . ? ZN A 815 . ? 1_555 ? 72 BC5 6 ASP T . ? ASP A 819 . ? 1_555 ? 73 BC5 6 HOH U . ? HOH A 1454 . ? 1_555 ? 74 BC6 8 HIS A 384 ? HIS A 377 . ? 1_555 ? 75 BC6 8 ASP A 394 ? ASP A 387 . ? 1_555 ? 76 BC6 8 GLU A 431 ? GLU A 424 . ? 1_555 ? 77 BC6 8 GLU A 432 ? GLU A 425 . ? 1_555 ? 78 BC6 8 ASP A 460 ? ASP A 453 . ? 1_555 ? 79 BC6 8 ZN O . ? ZN A 814 . ? 1_555 ? 80 BC6 8 ASP T . ? ASP A 819 . ? 1_555 ? 81 BC6 8 HOH U . ? HOH A 1454 . ? 1_555 ? 82 BC7 5 THR A 276 ? THR A 269 . ? 1_555 ? 83 BC7 5 TYR A 279 ? TYR A 272 . ? 1_555 ? 84 BC7 5 GLU A 440 ? GLU A 433 . ? 1_555 ? 85 BC7 5 GLU A 443 ? GLU A 436 . ? 1_555 ? 86 BC7 5 HOH U . ? HOH A 906 . ? 1_555 ? 87 BC8 4 ASN A 458 ? ASN A 451 . ? 1_555 ? 88 BC8 4 ASP A 460 ? ASP A 453 . ? 1_555 ? 89 BC8 4 ARG A 541 ? ARG A 534 . ? 1_555 ? 90 BC8 4 ARG A 543 ? ARG A 536 . ? 1_555 ? 91 BC9 14 ARG A 217 ? ARG A 210 . ? 1_555 ? 92 BC9 14 ASN A 264 ? ASN A 257 . ? 1_555 ? 93 BC9 14 GLU A 431 ? GLU A 424 . ? 1_555 ? 94 BC9 14 GLU A 432 ? GLU A 425 . ? 1_555 ? 95 BC9 14 GLY A 434 ? GLY A 427 . ? 1_555 ? 96 BC9 14 LEU A 435 ? LEU A 428 . ? 1_555 ? 97 BC9 14 GLY A 525 ? GLY A 518 . ? 1_555 ? 98 BC9 14 TYR A 559 ? TYR A 552 . ? 1_555 ? 99 BC9 14 HIS A 560 ? HIS A 553 . ? 1_555 ? 100 BC9 14 LYS A 706 ? LYS A 699 . ? 1_555 ? 101 BC9 14 TYR A 707 ? TYR A 700 . ? 1_555 ? 102 BC9 14 ASP T . ? ASP A 819 . ? 1_555 ? 103 BC9 14 HOH U . ? HOH A 909 . ? 1_555 ? 104 BC9 14 HOH U . ? HOH A 1074 . ? 1_555 ? 105 CC1 16 ASP A 394 ? ASP A 387 . ? 1_555 ? 106 CC1 16 ASP A 460 ? ASP A 453 . ? 1_555 ? 107 CC1 16 GLY A 525 ? GLY A 518 . ? 1_555 ? 108 CC1 16 ASN A 526 ? ASN A 519 . ? 1_555 ? 109 CC1 16 ARG A 541 ? ARG A 534 . ? 1_555 ? 110 CC1 16 ARG A 543 ? ARG A 536 . ? 1_555 ? 111 CC1 16 TYR A 559 ? TYR A 552 . ? 1_555 ? 112 CC1 16 HIS A 560 ? HIS A 553 . ? 1_555 ? 113 CC1 16 ZN O . ? ZN A 814 . ? 1_555 ? 114 CC1 16 ZN P . ? ZN A 815 . ? 1_555 ? 115 CC1 16 GLU S . ? GLU A 818 . ? 1_555 ? 116 CC1 16 HOH U . ? HOH A 1070 . ? 1_555 ? 117 CC1 16 HOH U . ? HOH A 1416 . ? 1_555 ? 118 CC1 16 HOH U . ? HOH A 1435 . ? 1_555 ? 119 CC1 16 HOH U . ? HOH A 1437 . ? 1_555 ? 120 CC1 16 HOH U . ? HOH A 1454 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MCS _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 4MCS _atom_sites.fract_transf_matrix[1][1] 0.009848 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.007669 _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] 0.006290 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CA CL N O S ZN # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . LYS A 1 62 ? 16.869 45.619 82.579 1.00 61.75 ? 55 LYS A N 1 ATOM 2 C CA . LYS A 1 62 ? 16.311 46.748 81.773 1.00 60.13 ? 55 LYS A CA 1 ATOM 3 C C . LYS A 1 62 ? 15.866 46.370 80.368 1.00 57.96 ? 55 LYS A C 1 ATOM 4 O O . LYS A 1 62 ? 16.445 45.498 79.715 1.00 57.44 ? 55 LYS A O 1 ATOM 5 C CB . LYS A 1 62 ? 17.315 47.896 81.666 1.00 60.63 ? 55 LYS A CB 1 ATOM 6 C CG . LYS A 1 62 ? 17.240 48.912 82.788 1.00 63.54 ? 55 LYS A CG 1 ATOM 7 C CD . LYS A 1 62 ? 17.625 50.294 82.239 1.00 65.30 ? 55 LYS A CD 1 ATOM 8 C CE . LYS A 1 62 ? 18.266 51.167 83.286 1.00 65.06 ? 55 LYS A CE 1 ATOM 9 N NZ . LYS A 1 62 ? 19.063 50.377 84.277 1.00 67.02 ? 55 LYS A NZ 1 ATOM 10 N N . HIS A 1 63 ? 14.837 47.061 79.898 1.00 55.91 ? 56 HIS A N 1 ATOM 11 C CA . HIS A 1 63 ? 14.440 46.941 78.512 1.00 53.37 ? 56 HIS A CA 1 ATOM 12 C C . HIS A 1 63 ? 14.888 48.216 77.827 1.00 51.18 ? 56 HIS A C 1 ATOM 13 O O . HIS A 1 63 ? 14.189 49.234 77.887 1.00 52.04 ? 56 HIS A O 1 ATOM 14 C CB . HIS A 1 63 ? 12.933 46.747 78.394 1.00 53.64 ? 56 HIS A CB 1 ATOM 15 C CG . HIS A 1 63 ? 12.457 45.417 78.887 1.00 55.75 ? 56 HIS A CG 1 ATOM 16 N ND1 . HIS A 1 63 ? 11.389 45.286 79.751 1.00 58.29 ? 56 HIS A ND1 1 ATOM 17 C CD2 . HIS A 1 63 ? 12.903 44.161 78.639 1.00 55.99 ? 56 HIS A CD2 1 ATOM 18 C CE1 . HIS A 1 63 ? 11.201 44.003 80.017 1.00 61.38 ? 56 HIS A CE1 1 ATOM 19 N NE2 . HIS A 1 63 ? 12.103 43.300 79.349 1.00 60.65 ? 56 HIS A NE2 1 ATOM 20 N N . ASN A 1 64 ? 16.075 48.161 77.220 1.00 47.14 ? 57 ASN A N 1 ATOM 21 C CA . ASN A 1 64 ? 16.691 49.314 76.576 1.00 43.02 ? 57 ASN A CA 1 ATOM 22 C C . ASN A 1 64 ? 17.323 48.811 75.300 1.00 40.02 ? 57 ASN A C 1 ATOM 23 O O . ASN A 1 64 ? 17.118 47.645 74.931 1.00 37.51 ? 57 ASN A O 1 ATOM 24 C CB . ASN A 1 64 ? 17.722 50.010 77.493 1.00 43.49 ? 57 ASN A CB 1 ATOM 25 C CG . ASN A 1 64 ? 18.750 49.045 78.084 1.00 43.59 ? 57 ASN A CG 1 ATOM 26 O OD1 . ASN A 1 64 ? 18.985 47.945 77.571 1.00 40.44 ? 57 ASN A OD1 1 ATOM 27 N ND2 . ASN A 1 64 ? 19.362 49.459 79.202 1.00 44.90 ? 57 ASN A ND2 1 ATOM 28 N N . MET A 1 65 ? 18.076 49.663 74.607 1.00 38.42 ? 58 MET A N 1 ATOM 29 C CA . MET A 1 65 ? 18.572 49.182 73.324 1.00 37.61 ? 58 MET A CA 1 ATOM 30 C C . MET A 1 65 ? 19.546 48.012 73.510 1.00 37.18 ? 58 MET A C 1 ATOM 31 O O . MET A 1 65 ? 19.518 47.061 72.720 1.00 35.10 ? 58 MET A O 1 ATOM 32 C CB . MET A 1 65 ? 19.183 50.245 72.451 1.00 37.24 ? 58 MET A CB 1 ATOM 33 C CG . MET A 1 65 ? 19.151 49.750 71.013 1.00 40.06 ? 58 MET A CG 1 ATOM 34 S SD . MET A 1 65 ? 20.278 50.628 70.007 1.00 46.60 ? 58 MET A SD 1 ATOM 35 C CE . MET A 1 65 ? 19.510 52.169 69.978 1.00 39.70 ? 58 MET A CE 1 ATOM 36 N N . LYS A 1 66 ? 20.358 48.079 74.560 1.00 36.73 ? 59 LYS A N 1 ATOM 37 C CA . LYS A 1 66 ? 21.338 47.031 74.835 1.00 37.64 ? 59 LYS A CA 1 ATOM 38 C C . LYS A 1 66 ? 20.658 45.669 74.999 1.00 36.59 ? 59 LYS A C 1 ATOM 39 O O . LYS A 1 66 ? 21.157 44.668 74.504 1.00 36.35 ? 59 LYS A O 1 ATOM 40 C CB . LYS A 1 66 ? 22.188 47.354 76.084 1.00 38.87 ? 59 LYS A CB 1 ATOM 41 C CG . LYS A 1 66 ? 23.318 46.344 76.305 1.00 42.34 ? 59 LYS A CG 1 ATOM 42 C CD . LYS A 1 66 ? 24.103 46.633 77.614 1.00 49.50 ? 59 LYS A CD 1 ATOM 43 C CE . LYS A 1 66 ? 24.865 45.382 78.162 1.00 53.75 ? 59 LYS A CE 1 ATOM 44 N NZ . LYS A 1 66 ? 25.713 44.705 77.113 1.00 54.90 ? 59 LYS A NZ 1 ATOM 45 N N . ALA A 1 67 ? 19.532 45.636 75.707 1.00 36.39 ? 60 ALA A N 1 ATOM 46 C CA . ALA A 1 67 ? 18.757 44.403 75.829 1.00 36.59 ? 60 ALA A CA 1 ATOM 47 C C . ALA A 1 67 ? 18.324 43.880 74.461 1.00 34.77 ? 60 ALA A C 1 ATOM 48 O O . ALA A 1 67 ? 18.447 42.686 74.193 1.00 33.96 ? 60 ALA A O 1 ATOM 49 C CB . ALA A 1 67 ? 17.552 44.609 76.703 1.00 38.42 ? 60 ALA A CB 1 ATOM 50 N N . PHE A 1 68 ? 17.797 44.782 73.621 1.00 32.97 ? 61 PHE A N 1 ATOM 51 C CA . PHE A 1 68 ? 17.396 44.425 72.264 1.00 31.61 ? 61 PHE A CA 1 ATOM 52 C C . PHE A 1 68 ? 18.578 43.829 71.465 1.00 30.82 ? 61 PHE A C 1 ATOM 53 O O . PHE A 1 68 ? 18.477 42.733 70.885 1.00 30.36 ? 61 PHE A O 1 ATOM 54 C CB . PHE A 1 68 ? 16.771 45.619 71.520 1.00 30.10 ? 61 PHE A CB 1 ATOM 55 C CG . PHE A 1 68 ? 16.681 45.383 70.038 1.00 29.95 ? 61 PHE A CG 1 ATOM 56 C CD1 . PHE A 1 68 ? 15.706 44.525 69.522 1.00 28.32 ? 61 PHE A CD1 1 ATOM 57 C CD2 . PHE A 1 68 ? 17.647 45.919 69.180 1.00 29.90 ? 61 PHE A CD2 1 ATOM 58 C CE1 . PHE A 1 68 ? 15.670 44.237 68.155 1.00 28.51 ? 61 PHE A CE1 1 ATOM 59 C CE2 . PHE A 1 68 ? 17.631 45.634 67.810 1.00 27.22 ? 61 PHE A CE2 1 ATOM 60 C CZ . PHE A 1 68 ? 16.624 44.803 67.302 1.00 27.41 ? 61 PHE A CZ 1 ATOM 61 N N . LEU A 1 69 ? 19.671 44.578 71.415 1.00 30.09 ? 62 LEU A N 1 ATOM 62 C CA . LEU A 1 69 ? 20.864 44.185 70.694 1.00 31.19 ? 62 LEU A CA 1 ATOM 63 C C . LEU A 1 69 ? 21.470 42.856 71.167 1.00 33.08 ? 62 LEU A C 1 ATOM 64 O O . LEU A 1 69 ? 21.853 41.998 70.349 1.00 32.72 ? 62 LEU A O 1 ATOM 65 C CB . LEU A 1 69 ? 21.899 45.296 70.802 1.00 32.11 ? 62 LEU A CB 1 ATOM 66 C CG . LEU A 1 69 ? 21.521 46.635 70.149 1.00 30.40 ? 62 LEU A CG 1 ATOM 67 C CD1 . LEU A 1 69 ? 22.620 47.637 70.502 1.00 33.31 ? 62 LEU A CD1 1 ATOM 68 C CD2 . LEU A 1 69 ? 21.376 46.468 68.606 1.00 33.10 ? 62 LEU A CD2 1 ATOM 69 N N . ASP A 1 70 ? 21.542 42.669 72.485 1.00 34.82 ? 63 ASP A N 1 ATOM 70 C CA . ASP A 1 70 ? 22.141 41.448 73.045 1.00 37.10 ? 63 ASP A CA 1 ATOM 71 C C . ASP A 1 70 ? 21.356 40.179 72.722 1.00 36.30 ? 63 ASP A C 1 ATOM 72 O O . ASP A 1 70 ? 21.928 39.108 72.706 1.00 37.11 ? 63 ASP A O 1 ATOM 73 C CB . ASP A 1 70 ? 22.306 41.528 74.564 1.00 38.81 ? 63 ASP A CB 1 ATOM 74 C CG . ASP A 1 70 ? 23.432 42.453 74.998 1.00 42.35 ? 63 ASP A CG 1 ATOM 75 O OD1 . ASP A 1 70 ? 24.285 42.813 74.172 1.00 43.13 ? 63 ASP A OD1 1 ATOM 76 O OD2 . ASP A 1 70 ? 23.448 42.842 76.191 1.00 44.24 ? 63 ASP A OD2 1 ATOM 77 N N . GLU A 1 71 ? 20.053 40.297 72.506 1.00 35.26 ? 64 GLU A N 1 ATOM 78 C CA . GLU A 1 71 ? 19.215 39.150 72.207 1.00 34.95 ? 64 GLU A CA 1 ATOM 79 C C . GLU A 1 71 ? 19.423 38.593 70.764 1.00 33.42 ? 64 GLU A C 1 ATOM 80 O O . GLU A 1 71 ? 19.174 37.406 70.521 1.00 33.05 ? 64 GLU A O 1 ATOM 81 C CB . GLU A 1 71 ? 17.747 39.504 72.464 1.00 34.91 ? 64 GLU A CB 1 ATOM 82 C CG . GLU A 1 71 ? 16.744 38.380 72.190 1.00 36.82 ? 64 GLU A CG 1 ATOM 83 C CD . GLU A 1 71 ? 16.945 37.150 73.075 1.00 42.30 ? 64 GLU A CD 1 ATOM 84 O OE1 . GLU A 1 71 ? 17.289 37.316 74.258 1.00 41.12 ? 64 GLU A OE1 1 ATOM 85 O OE2 . GLU A 1 71 ? 16.755 36.010 72.583 1.00 41.88 ? 64 GLU A OE2 1 ATOM 86 N N . LEU A 1 72 ? 19.858 39.456 69.830 1.00 31.80 ? 65 LEU A N 1 ATOM 87 C CA . LEU A 1 72 ? 20.225 39.034 68.454 1.00 31.08 ? 65 LEU A CA 1 ATOM 88 C C . LEU A 1 72 ? 21.379 38.017 68.459 1.00 31.84 ? 65 LEU A C 1 ATOM 89 O O . LEU A 1 72 ? 22.392 38.263 69.101 1.00 30.99 ? 65 LEU A O 1 ATOM 90 C CB . LEU A 1 72 ? 20.622 40.245 67.595 1.00 30.03 ? 65 LEU A CB 1 ATOM 91 C CG . LEU A 1 72 ? 19.636 41.405 67.524 1.00 28.96 ? 65 LEU A CG 1 ATOM 92 C CD1 . LEU A 1 72 ? 20.350 42.639 66.929 1.00 27.74 ? 65 LEU A CD1 1 ATOM 93 C CD2 . LEU A 1 72 ? 18.410 40.966 66.635 1.00 26.64 ? 65 LEU A CD2 1 ATOM 94 N N . LYS A 1 73 ? 21.236 36.923 67.706 1.00 31.37 ? 66 LYS A N 1 ATOM 95 C CA . LYS A 1 73 ? 22.259 35.877 67.679 1.00 32.79 ? 66 LYS A CA 1 ATOM 96 C C . LYS A 1 73 ? 22.647 35.511 66.243 1.00 31.39 ? 66 LYS A C 1 ATOM 97 O O . LYS A 1 73 ? 21.773 35.264 65.427 1.00 30.66 ? 66 LYS A O 1 ATOM 98 C CB . LYS A 1 73 ? 21.742 34.625 68.404 1.00 34.26 ? 66 LYS A CB 1 ATOM 99 C CG . LYS A 1 73 ? 21.349 34.846 69.889 1.00 38.24 ? 66 LYS A CG 1 ATOM 100 C CD . LYS A 1 73 ? 22.565 35.215 70.737 1.00 43.63 ? 66 LYS A CD 1 ATOM 101 C CE . LYS A 1 73 ? 22.321 35.090 72.267 1.00 46.17 ? 66 LYS A CE 1 ATOM 102 N NZ . LYS A 1 73 ? 21.590 36.276 72.784 1.00 43.73 ? 66 LYS A NZ 1 ATOM 103 N N . ALA A 1 74 ? 23.949 35.482 65.953 1.00 31.54 ? 67 ALA A N 1 ATOM 104 C CA . ALA A 1 74 ? 24.476 35.061 64.653 1.00 30.92 ? 67 ALA A CA 1 ATOM 105 C C . ALA A 1 74 ? 23.944 33.669 64.316 1.00 31.45 ? 67 ALA A C 1 ATOM 106 O O . ALA A 1 74 ? 23.576 33.405 63.161 1.00 30.42 ? 67 ALA A O 1 ATOM 107 C CB . ALA A 1 74 ? 26.046 35.042 64.660 1.00 31.54 ? 67 ALA A CB 1 ATOM 108 N N . GLU A 1 75 ? 23.887 32.794 65.327 1.00 32.45 ? 68 GLU A N 1 ATOM 109 C CA . GLU A 1 75 ? 23.482 31.390 65.126 1.00 33.08 ? 68 GLU A CA 1 ATOM 110 C C . GLU A 1 75 ? 22.029 31.322 64.617 1.00 31.40 ? 68 GLU A C 1 ATOM 111 O O . GLU A 1 75 ? 21.719 30.498 63.757 1.00 30.35 ? 68 GLU A O 1 ATOM 112 C CB . GLU A 1 75 ? 23.667 30.539 66.424 1.00 34.81 ? 68 GLU A CB 1 ATOM 113 C CG A GLU A 1 75 ? 23.304 29.065 66.224 0.50 35.87 ? 68 GLU A CG 1 ATOM 114 C CG B GLU A 1 75 ? 22.615 30.920 67.570 0.50 37.38 ? 68 GLU A CG 1 ATOM 115 C CD A GLU A 1 75 ? 24.047 28.408 65.062 0.50 38.93 ? 68 GLU A CD 1 ATOM 116 C CD B GLU A 1 75 ? 23.091 30.886 69.065 0.50 42.13 ? 68 GLU A CD 1 ATOM 117 O OE1 A GLU A 1 75 ? 25.299 28.444 65.043 0.50 36.88 ? 68 GLU A OE1 1 ATOM 118 O OE1 B GLU A 1 75 ? 24.282 31.102 69.392 0.50 43.30 ? 68 GLU A OE1 1 ATOM 119 O OE2 A GLU A 1 75 ? 23.364 27.849 64.168 0.50 40.08 ? 68 GLU A OE2 1 ATOM 120 O OE2 B GLU A 1 75 ? 22.224 30.680 69.944 0.50 42.68 ? 68 GLU A OE2 1 ATOM 121 N N . ASN A 1 76 ? 21.151 32.181 65.161 1.00 30.73 ? 69 ASN A N 1 ATOM 122 C CA . ASN A 1 76 ? 19.766 32.255 64.664 1.00 30.27 ? 69 ASN A CA 1 ATOM 123 C C . ASN A 1 76 ? 19.666 32.724 63.222 1.00 28.96 ? 69 ASN A C 1 ATOM 124 O O . ASN A 1 76 ? 18.904 32.161 62.433 1.00 28.68 ? 69 ASN A O 1 ATOM 125 C CB . ASN A 1 76 ? 18.904 33.164 65.551 1.00 30.73 ? 69 ASN A CB 1 ATOM 126 C CG . ASN A 1 76 ? 18.588 32.524 66.913 1.00 32.57 ? 69 ASN A CG 1 ATOM 127 O OD1 . ASN A 1 76 ? 18.581 31.302 67.038 1.00 32.44 ? 69 ASN A OD1 1 ATOM 128 N ND2 . ASN A 1 76 ? 18.380 33.350 67.935 1.00 31.43 ? 69 ASN A ND2 1 ATOM 129 N N . ILE A 1 77 ? 20.408 33.771 62.883 1.00 27.92 ? 70 ILE A N 1 ATOM 130 C CA . ILE A 1 77 ? 20.369 34.310 61.512 1.00 26.16 ? 70 ILE A CA 1 ATOM 131 C C . ILE A 1 77 ? 20.827 33.208 60.537 1.00 26.29 ? 70 ILE A C 1 ATOM 132 O O . ILE A 1 77 ? 20.247 33.010 59.480 1.00 25.80 ? 70 ILE A O 1 ATOM 133 C CB . ILE A 1 77 ? 21.270 35.554 61.403 1.00 26.17 ? 70 ILE A CB 1 ATOM 134 C CG1 . ILE A 1 77 ? 20.717 36.686 62.315 1.00 25.79 ? 70 ILE A CG1 1 ATOM 135 C CG2 . ILE A 1 77 ? 21.357 36.048 59.933 1.00 24.24 ? 70 ILE A CG2 1 ATOM 136 C CD1 . ILE A 1 77 ? 21.717 37.844 62.602 1.00 26.73 ? 70 ILE A CD1 1 ATOM 137 N N . LYS A 1 78 ? 21.854 32.448 60.942 1.00 26.54 ? 71 LYS A N 1 ATOM 138 C CA . LYS A 1 78 ? 22.366 31.330 60.111 1.00 27.22 ? 71 LYS A CA 1 ATOM 139 C C . LYS A 1 78 ? 21.267 30.270 59.865 1.00 28.18 ? 71 LYS A C 1 ATOM 140 O O . LYS A 1 78 ? 21.053 29.832 58.725 1.00 28.79 ? 71 LYS A O 1 ATOM 141 C CB . LYS A 1 78 ? 23.593 30.708 60.814 1.00 27.85 ? 71 LYS A CB 1 ATOM 142 C CG . LYS A 1 78 ? 24.112 29.415 60.163 1.00 28.62 ? 71 LYS A CG 1 ATOM 143 C CD . LYS A 1 78 ? 25.440 28.962 60.839 1.00 31.30 ? 71 LYS A CD 1 ATOM 144 C CE . LYS A 1 78 ? 26.019 27.721 60.167 1.00 33.43 ? 71 LYS A CE 1 ATOM 145 N NZ . LYS A 1 78 ? 27.198 27.178 60.967 1.00 32.85 ? 71 LYS A NZ 1 ATOM 146 N N . LYS A 1 79 ? 20.609 29.828 60.939 1.00 29.21 ? 72 LYS A N 1 ATOM 147 C CA . LYS A 1 79 ? 19.485 28.880 60.851 1.00 30.16 ? 72 LYS A CA 1 ATOM 148 C C . LYS A 1 79 ? 18.360 29.378 59.939 1.00 27.73 ? 72 LYS A C 1 ATOM 149 O O . LYS A 1 79 ? 17.829 28.630 59.128 1.00 27.43 ? 72 LYS A O 1 ATOM 150 C CB . LYS A 1 79 ? 18.898 28.575 62.240 1.00 30.24 ? 72 LYS A CB 1 ATOM 151 C CG . LYS A 1 79 ? 19.924 27.935 63.164 1.00 38.31 ? 72 LYS A CG 1 ATOM 152 C CD . LYS A 1 79 ? 19.339 27.439 64.481 1.00 41.54 ? 72 LYS A CD 1 ATOM 153 C CE . LYS A 1 79 ? 20.378 26.585 65.213 1.00 48.00 ? 72 LYS A CE 1 ATOM 154 N NZ . LYS A 1 79 ? 19.984 26.433 66.643 1.00 49.29 ? 72 LYS A NZ 1 ATOM 155 N N . PHE A 1 80 ? 17.989 30.642 60.102 1.00 26.86 ? 73 PHE A N 1 ATOM 156 C CA . PHE A 1 80 ? 16.970 31.219 59.258 1.00 25.88 ? 73 PHE A CA 1 ATOM 157 C C . PHE A 1 80 ? 17.421 31.280 57.791 1.00 24.79 ? 73 PHE A C 1 ATOM 158 O O . PHE A 1 80 ? 16.638 31.001 56.887 1.00 24.79 ? 73 PHE A O 1 ATOM 159 C CB . PHE A 1 80 ? 16.577 32.626 59.744 1.00 25.06 ? 73 PHE A CB 1 ATOM 160 C CG . PHE A 1 80 ? 16.028 32.662 61.141 1.00 24.68 ? 73 PHE A CG 1 ATOM 161 C CD1 . PHE A 1 80 ? 15.308 31.574 61.671 1.00 26.67 ? 73 PHE A CD1 1 ATOM 162 C CD2 . PHE A 1 80 ? 16.163 33.812 61.894 1.00 22.63 ? 73 PHE A CD2 1 ATOM 163 C CE1 . PHE A 1 80 ? 14.793 31.633 62.962 1.00 29.61 ? 73 PHE A CE1 1 ATOM 164 C CE2 . PHE A 1 80 ? 15.612 33.906 63.173 1.00 24.40 ? 73 PHE A CE2 1 ATOM 165 C CZ . PHE A 1 80 ? 14.927 32.827 63.702 1.00 26.21 ? 73 PHE A CZ 1 ATOM 166 N N . LEU A 1 81 ? 18.658 31.687 57.551 1.00 25.15 ? 74 LEU A N 1 ATOM 167 C CA . LEU A 1 81 ? 19.113 31.761 56.156 1.00 25.10 ? 74 LEU A CA 1 ATOM 168 C C . LEU A 1 81 ? 19.032 30.380 55.520 1.00 25.29 ? 74 LEU A C 1 ATOM 169 O O . LEU A 1 81 ? 18.536 30.229 54.397 1.00 25.27 ? 74 LEU A O 1 ATOM 170 C CB . LEU A 1 81 ? 20.560 32.261 56.038 1.00 25.60 ? 74 LEU A CB 1 ATOM 171 C CG . LEU A 1 81 ? 21.046 32.353 54.595 1.00 24.03 ? 74 LEU A CG 1 ATOM 172 C CD1 . LEU A 1 81 ? 20.163 33.441 53.873 1.00 21.21 ? 74 LEU A CD1 1 ATOM 173 C CD2 . LEU A 1 81 ? 22.482 32.782 54.564 1.00 25.34 ? 74 LEU A CD2 1 ATOM 174 N N . TYR A 1 82 ? 19.553 29.372 56.220 1.00 25.33 ? 75 TYR A N 1 ATOM 175 C CA . TYR A 1 82 ? 19.457 28.014 55.721 1.00 27.03 ? 75 TYR A CA 1 ATOM 176 C C . TYR A 1 82 ? 17.998 27.659 55.399 1.00 27.32 ? 75 TYR A C 1 ATOM 177 O O . TYR A 1 82 ? 17.686 27.136 54.317 1.00 27.26 ? 75 TYR A O 1 ATOM 178 C CB . TYR A 1 82 ? 20.061 27.013 56.741 1.00 27.45 ? 75 TYR A CB 1 ATOM 179 C CG . TYR A 1 82 ? 19.973 25.597 56.214 1.00 30.30 ? 75 TYR A CG 1 ATOM 180 C CD1 . TYR A 1 82 ? 20.951 25.099 55.354 1.00 29.48 ? 75 TYR A CD1 1 ATOM 181 C CD2 . TYR A 1 82 ? 18.885 24.785 56.527 1.00 33.24 ? 75 TYR A CD2 1 ATOM 182 C CE1 . TYR A 1 82 ? 20.884 23.803 54.853 1.00 32.71 ? 75 TYR A CE1 1 ATOM 183 C CE2 . TYR A 1 82 ? 18.791 23.475 56.015 1.00 35.12 ? 75 TYR A CE2 1 ATOM 184 C CZ . TYR A 1 82 ? 19.801 23.002 55.184 1.00 35.52 ? 75 TYR A CZ 1 ATOM 185 O OH . TYR A 1 82 ? 19.734 21.723 54.674 1.00 40.42 ? 75 TYR A OH 1 ATOM 186 N N . ASN A 1 83 ? 17.101 27.945 56.337 1.00 27.56 ? 76 ASN A N 1 ATOM 187 C CA . ASN A 1 83 ? 15.680 27.663 56.153 1.00 27.05 ? 76 ASN A CA 1 ATOM 188 C C . ASN A 1 83 ? 15.027 28.330 54.933 1.00 26.33 ? 76 ASN A C 1 ATOM 189 O O . ASN A 1 83 ? 14.082 27.763 54.347 1.00 26.29 ? 76 ASN A O 1 ATOM 190 C CB . ASN A 1 83 ? 14.942 28.084 57.401 1.00 28.57 ? 76 ASN A CB 1 ATOM 191 C CG . ASN A 1 83 ? 13.480 27.699 57.379 1.00 29.64 ? 76 ASN A CG 1 ATOM 192 O OD1 . ASN A 1 83 ? 12.638 28.489 56.990 1.00 29.11 ? 76 ASN A OD1 1 ATOM 193 N ND2 . ASN A 1 83 ? 13.178 26.473 57.788 1.00 30.20 ? 76 ASN A ND2 1 ATOM 194 N N . PHE A 1 84 ? 15.507 29.525 54.575 1.00 24.15 ? 77 PHE A N 1 ATOM 195 C CA . PHE A 1 84 ? 14.860 30.349 53.536 1.00 23.65 ? 77 PHE A CA 1 ATOM 196 C C . PHE A 1 84 ? 15.384 30.074 52.131 1.00 24.37 ? 77 PHE A C 1 ATOM 197 O O . PHE A 1 84 ? 14.854 30.641 51.142 1.00 24.15 ? 77 PHE A O 1 ATOM 198 C CB . PHE A 1 84 ? 15.074 31.858 53.810 1.00 22.41 ? 77 PHE A CB 1 ATOM 199 C CG . PHE A 1 84 ? 14.337 32.411 55.008 1.00 23.15 ? 77 PHE A CG 1 ATOM 200 C CD1 . PHE A 1 84 ? 13.400 31.656 55.741 1.00 24.90 ? 77 PHE A CD1 1 ATOM 201 C CD2 . PHE A 1 84 ? 14.621 33.709 55.436 1.00 21.97 ? 77 PHE A CD2 1 ATOM 202 C CE1 . PHE A 1 84 ? 12.772 32.212 56.878 1.00 25.03 ? 77 PHE A CE1 1 ATOM 203 C CE2 . PHE A 1 84 ? 13.967 34.288 56.543 1.00 23.34 ? 77 PHE A CE2 1 ATOM 204 C CZ . PHE A 1 84 ? 13.023 33.536 57.271 1.00 24.44 ? 77 PHE A CZ 1 ATOM 205 N N . THR A 1 85 ? 16.442 29.231 52.027 1.00 24.74 ? 78 THR A N 1 ATOM 206 C CA . THR A 1 85 ? 17.197 29.106 50.784 1.00 24.73 ? 78 THR A CA 1 ATOM 207 C C . THR A 1 85 ? 17.322 27.688 50.200 1.00 24.94 ? 78 THR A C 1 ATOM 208 O O . THR A 1 85 ? 18.137 27.474 49.313 1.00 24.08 ? 78 THR A O 1 ATOM 209 C CB . THR A 1 85 ? 18.634 29.661 50.966 1.00 25.16 ? 78 THR A CB 1 ATOM 210 O OG1 . THR A 1 85 ? 19.283 28.947 52.015 1.00 23.12 ? 78 THR A OG1 1 ATOM 211 C CG2 . THR A 1 85 ? 18.577 31.158 51.346 1.00 24.47 ? 78 THR A CG2 1 ATOM 212 N N . GLN A 1 86 ? 16.496 26.751 50.666 1.00 25.24 ? 79 GLN A N 1 ATOM 213 C CA . GLN A 1 86 ? 16.582 25.348 50.215 1.00 28.23 ? 79 GLN A CA 1 ATOM 214 C C . GLN A 1 86 ? 15.873 25.107 48.883 1.00 28.35 ? 79 GLN A C 1 ATOM 215 O O . GLN A 1 86 ? 16.201 24.159 48.196 1.00 27.79 ? 79 GLN A O 1 ATOM 216 C CB . GLN A 1 86 ? 16.017 24.378 51.283 1.00 29.05 ? 79 GLN A CB 1 ATOM 217 C CG . GLN A 1 86 ? 16.805 24.434 52.575 1.00 32.65 ? 79 GLN A CG 1 ATOM 218 C CD . GLN A 1 86 ? 18.298 24.342 52.296 1.00 36.65 ? 79 GLN A CD 1 ATOM 219 O OE1 . GLN A 1 86 ? 18.772 23.274 51.900 1.00 41.56 ? 79 GLN A OE1 1 ATOM 220 N NE2 . GLN A 1 86 ? 19.040 25.464 52.445 1.00 35.42 ? 79 GLN A NE2 1 ATOM 221 N N . ILE A 1 87 ? 14.886 25.945 48.558 1.00 26.83 ? 80 ILE A N 1 ATOM 222 C CA . ILE A 1 87 ? 14.126 25.805 47.301 1.00 28.33 ? 80 ILE A CA 1 ATOM 223 C C . ILE A 1 87 ? 13.920 27.212 46.748 1.00 25.70 ? 80 ILE A C 1 ATOM 224 O O . ILE A 1 87 ? 14.028 28.167 47.506 1.00 25.68 ? 80 ILE A O 1 ATOM 225 C CB . ILE A 1 87 ? 12.727 25.149 47.539 1.00 29.64 ? 80 ILE A CB 1 ATOM 226 C CG1 . ILE A 1 87 ? 11.825 26.090 48.367 1.00 29.95 ? 80 ILE A CG1 1 ATOM 227 C CG2 . ILE A 1 87 ? 12.891 23.756 48.194 1.00 32.43 ? 80 ILE A CG2 1 ATOM 228 C CD1 . ILE A 1 87 ? 10.364 25.575 48.542 1.00 31.95 ? 80 ILE A CD1 1 ATOM 229 N N . PRO A 1 88 ? 13.637 27.347 45.433 1.00 25.61 ? 81 PRO A N 1 ATOM 230 C CA . PRO A 1 88 ? 13.391 28.708 44.894 1.00 24.64 ? 81 PRO A CA 1 ATOM 231 C C . PRO A 1 88 ? 12.133 29.337 45.465 1.00 24.36 ? 81 PRO A C 1 ATOM 232 O O . PRO A 1 88 ? 11.167 28.626 45.782 1.00 23.73 ? 81 PRO A O 1 ATOM 233 C CB . PRO A 1 88 ? 13.218 28.469 43.385 1.00 24.63 ? 81 PRO A CB 1 ATOM 234 C CG . PRO A 1 88 ? 14.037 27.157 43.144 1.00 27.03 ? 81 PRO A CG 1 ATOM 235 C CD . PRO A 1 88 ? 13.687 26.331 44.366 1.00 25.69 ? 81 PRO A CD 1 ATOM 236 N N . HIS A 1 89 ? 12.145 30.664 45.579 1.00 22.26 ? 82 HIS A N 1 ATOM 237 C CA . HIS A 1 89 ? 10.972 31.402 46.017 1.00 22.46 ? 82 HIS A CA 1 ATOM 238 C C . HIS A 1 89 ? 10.612 32.543 45.037 1.00 21.00 ? 82 HIS A C 1 ATOM 239 O O . HIS A 1 89 ? 10.555 33.739 45.416 1.00 20.51 ? 82 HIS A O 1 ATOM 240 C CB . HIS A 1 89 ? 11.178 31.941 47.452 1.00 21.31 ? 82 HIS A CB 1 ATOM 241 C CG . HIS A 1 89 ? 11.343 30.860 48.472 1.00 22.57 ? 82 HIS A CG 1 ATOM 242 N ND1 . HIS A 1 89 ? 12.570 30.541 49.016 1.00 22.04 ? 82 HIS A ND1 1 ATOM 243 C CD2 . HIS A 1 89 ? 10.448 29.995 49.017 1.00 20.94 ? 82 HIS A CD2 1 ATOM 244 C CE1 . HIS A 1 89 ? 12.419 29.536 49.873 1.00 22.14 ? 82 HIS A CE1 1 ATOM 245 N NE2 . HIS A 1 89 ? 11.143 29.178 49.880 1.00 21.68 ? 82 HIS A NE2 1 ATOM 246 N N . LEU A 1 90 ? 10.360 32.163 43.797 1.00 20.31 ? 83 LEU A N 1 ATOM 247 C CA . LEU A 1 90 ? 10.119 33.122 42.721 1.00 21.23 ? 83 LEU A CA 1 ATOM 248 C C . LEU A 1 90 ? 8.770 33.789 42.954 1.00 21.22 ? 83 LEU A C 1 ATOM 249 O O . LEU A 1 90 ? 7.804 33.121 43.326 1.00 20.27 ? 83 LEU A O 1 ATOM 250 C CB . LEU A 1 90 ? 10.148 32.384 41.350 1.00 21.04 ? 83 LEU A CB 1 ATOM 251 C CG . LEU A 1 90 ? 9.934 33.257 40.089 1.00 22.15 ? 83 LEU A CG 1 ATOM 252 C CD1 . LEU A 1 90 ? 11.106 34.195 39.977 1.00 19.47 ? 83 LEU A CD1 1 ATOM 253 C CD2 . LEU A 1 90 ? 9.893 32.256 38.753 1.00 19.83 ? 83 LEU A CD2 1 ATOM 254 N N . ALA A 1 91 ? 8.697 35.115 42.774 1.00 20.54 ? 84 ALA A N 1 ATOM 255 C CA . ALA A 1 91 ? 7.385 35.811 42.937 1.00 19.39 ? 84 ALA A CA 1 ATOM 256 C C . ALA A 1 91 ? 6.287 35.141 42.116 1.00 20.72 ? 84 ALA A C 1 ATOM 257 O O . ALA A 1 91 ? 6.488 34.759 40.945 1.00 20.76 ? 84 ALA A O 1 ATOM 258 C CB . ALA A 1 91 ? 7.484 37.266 42.530 1.00 18.13 ? 84 ALA A CB 1 ATOM 259 N N . GLY A 1 92 ? 5.110 35.055 42.723 1.00 20.49 ? 85 GLY A N 1 ATOM 260 C CA . GLY A 1 92 ? 3.903 34.483 42.072 1.00 22.99 ? 85 GLY A CA 1 ATOM 261 C C . GLY A 1 92 ? 3.847 32.973 42.026 1.00 24.64 ? 85 GLY A C 1 ATOM 262 O O . GLY A 1 92 ? 2.888 32.406 41.485 1.00 27.49 ? 85 GLY A O 1 ATOM 263 N N . THR A 1 93 ? 4.818 32.298 42.626 1.00 24.37 ? 86 THR A N 1 ATOM 264 C CA . THR A 1 93 ? 4.786 30.841 42.666 1.00 24.60 ? 86 THR A CA 1 ATOM 265 C C . THR A 1 93 ? 4.256 30.293 43.998 1.00 25.05 ? 86 THR A C 1 ATOM 266 O O . THR A 1 93 ? 4.282 30.959 45.037 1.00 24.52 ? 86 THR A O 1 ATOM 267 C CB . THR A 1 93 ? 6.194 30.189 42.347 1.00 24.58 ? 86 THR A CB 1 ATOM 268 O OG1 . THR A 1 93 ? 7.126 30.495 43.386 1.00 23.55 ? 86 THR A OG1 1 ATOM 269 C CG2 . THR A 1 93 ? 6.789 30.670 40.994 1.00 24.76 ? 86 THR A CG2 1 ATOM 270 N N . GLU A 1 94 ? 3.795 29.039 43.974 1.00 26.71 ? 87 GLU A N 1 ATOM 271 C CA . GLU A 1 94 ? 3.248 28.422 45.181 1.00 27.51 ? 87 GLU A CA 1 ATOM 272 C C . GLU A 1 94 ? 4.286 28.385 46.348 1.00 26.67 ? 87 GLU A C 1 ATOM 273 O O . GLU A 1 94 ? 3.941 28.606 47.530 1.00 25.57 ? 87 GLU A O 1 ATOM 274 C CB . GLU A 1 94 ? 2.787 26.991 44.851 1.00 28.95 ? 87 GLU A CB 1 ATOM 275 C CG . GLU A 1 94 ? 2.263 26.204 46.063 1.00 35.87 ? 87 GLU A CG 1 ATOM 276 C CD . GLU A 1 94 ? 0.952 26.751 46.656 1.00 46.30 ? 87 GLU A CD 1 ATOM 277 O OE1 . GLU A 1 94 ? 0.634 26.347 47.809 1.00 50.36 ? 87 GLU A OE1 1 ATOM 278 O OE2 . GLU A 1 94 ? 0.242 27.577 46.001 1.00 48.79 ? 87 GLU A OE2 1 ATOM 279 N N . GLN A 1 95 ? 5.527 28.037 46.015 1.00 25.86 ? 88 GLN A N 1 ATOM 280 C CA . GLN A 1 95 ? 6.581 27.971 47.021 1.00 27.16 ? 88 GLN A CA 1 ATOM 281 C C . GLN A 1 95 ? 6.769 29.318 47.743 1.00 25.59 ? 88 GLN A C 1 ATOM 282 O O . GLN A 1 95 ? 7.090 29.348 48.923 1.00 23.64 ? 88 GLN A O 1 ATOM 283 C CB . GLN A 1 95 ? 7.889 27.531 46.393 1.00 28.00 ? 88 GLN A CB 1 ATOM 284 C CG . GLN A 1 95 ? 7.812 26.102 45.776 1.00 33.15 ? 88 GLN A CG 1 ATOM 285 C CD . GLN A 1 95 ? 7.117 26.042 44.365 1.00 40.51 ? 88 GLN A CD 1 ATOM 286 O OE1 . GLN A 1 95 ? 6.795 27.079 43.724 1.00 34.48 ? 88 GLN A OE1 1 ATOM 287 N NE2 . GLN A 1 95 ? 6.909 24.799 43.878 1.00 46.17 ? 88 GLN A NE2 1 ATOM 288 N N . ASN A 1 96 ? 6.624 30.436 47.030 1.00 24.11 ? 89 ASN A N 1 ATOM 289 C CA . ASN A 1 96 ? 6.786 31.727 47.709 1.00 24.31 ? 89 ASN A CA 1 ATOM 290 C C . ASN A 1 96 ? 5.543 32.106 48.552 1.00 24.59 ? 89 ASN A C 1 ATOM 291 O O . ASN A 1 96 ? 5.637 32.880 49.516 1.00 24.34 ? 89 ASN A O 1 ATOM 292 C CB . ASN A 1 96 ? 7.064 32.870 46.718 1.00 23.39 ? 89 ASN A CB 1 ATOM 293 C CG . ASN A 1 96 ? 7.657 34.116 47.427 1.00 25.53 ? 89 ASN A CG 1 ATOM 294 O OD1 . ASN A 1 96 ? 8.424 33.983 48.383 1.00 22.27 ? 89 ASN A OD1 1 ATOM 295 N ND2 . ASN A 1 96 ? 7.334 35.295 46.934 1.00 24.54 ? 89 ASN A ND2 1 ATOM 296 N N . PHE A 1 97 ? 4.376 31.610 48.149 1.00 24.10 ? 90 PHE A N 1 ATOM 297 C CA . PHE A 1 97 ? 3.157 31.756 48.955 1.00 23.72 ? 90 PHE A CA 1 ATOM 298 C C . PHE A 1 97 ? 3.331 30.917 50.222 1.00 25.28 ? 90 PHE A C 1 ATOM 299 O O . PHE A 1 97 ? 3.040 31.393 51.324 1.00 22.71 ? 90 PHE A O 1 ATOM 300 C CB . PHE A 1 97 ? 1.906 31.313 48.163 1.00 24.53 ? 90 PHE A CB 1 ATOM 301 C CG . PHE A 1 97 ? 0.642 31.203 48.999 1.00 27.48 ? 90 PHE A CG 1 ATOM 302 C CD1 . PHE A 1 97 ? 0.149 32.293 49.729 1.00 27.71 ? 90 PHE A CD1 1 ATOM 303 C CD2 . PHE A 1 97 ? -0.030 29.979 49.093 1.00 35.89 ? 90 PHE A CD2 1 ATOM 304 C CE1 . PHE A 1 97 ? -1.046 32.206 50.458 1.00 30.51 ? 90 PHE A CE1 1 ATOM 305 C CE2 . PHE A 1 97 ? -1.228 29.856 49.866 1.00 39.17 ? 90 PHE A CE2 1 ATOM 306 C CZ . PHE A 1 97 ? -1.731 30.997 50.548 1.00 35.59 ? 90 PHE A CZ 1 ATOM 307 N N . GLN A 1 98 ? 3.873 29.699 50.096 1.00 24.58 ? 91 GLN A N 1 ATOM 308 C CA . GLN A 1 98 ? 4.112 28.883 51.314 1.00 27.26 ? 91 GLN A CA 1 ATOM 309 C C . GLN A 1 98 ? 5.102 29.526 52.297 1.00 25.99 ? 91 GLN A C 1 ATOM 310 O O . GLN A 1 98 ? 4.892 29.460 53.513 1.00 27.13 ? 91 GLN A O 1 ATOM 311 C CB . GLN A 1 98 ? 4.569 27.448 50.962 1.00 27.95 ? 91 GLN A CB 1 ATOM 312 C CG . GLN A 1 98 ? 3.481 26.595 50.261 1.00 33.38 ? 91 GLN A CG 1 ATOM 313 C CD . GLN A 1 98 ? 2.144 26.520 51.042 1.00 44.55 ? 91 GLN A CD 1 ATOM 314 O OE1 . GLN A 1 98 ? 2.116 26.462 52.292 1.00 49.62 ? 91 GLN A OE1 1 ATOM 315 N NE2 . GLN A 1 98 ? 1.031 26.484 50.298 1.00 45.80 ? 91 GLN A NE2 1 ATOM 316 N N . LEU A 1 99 ? 6.177 30.126 51.773 1.00 24.37 ? 92 LEU A N 1 ATOM 317 C CA . LEU A 1 99 ? 7.153 30.823 52.641 1.00 23.81 ? 92 LEU A CA 1 ATOM 318 C C . LEU A 1 99 ? 6.457 32.014 53.351 1.00 23.23 ? 92 LEU A C 1 ATOM 319 O O . LEU A 1 99 ? 6.663 32.212 54.536 1.00 23.44 ? 92 LEU A O 1 ATOM 320 C CB . LEU A 1 99 ? 8.356 31.335 51.838 1.00 22.12 ? 92 LEU A CB 1 ATOM 321 C CG . LEU A 1 99 ? 9.520 31.901 52.667 1.00 24.08 ? 92 LEU A CG 1 ATOM 322 C CD1 . LEU A 1 99 ? 10.013 30.927 53.778 1.00 23.70 ? 92 LEU A CD1 1 ATOM 323 C CD2 . LEU A 1 99 ? 10.667 32.339 51.783 1.00 21.05 ? 92 LEU A CD2 1 ATOM 324 N N . ALA A 1 100 ? 5.665 32.801 52.614 1.00 22.37 ? 93 ALA A N 1 ATOM 325 C CA . ALA A 1 100 ? 4.851 33.876 53.232 1.00 22.76 ? 93 ALA A CA 1 ATOM 326 C C . ALA A 1 100 ? 3.996 33.392 54.410 1.00 23.83 ? 93 ALA A C 1 ATOM 327 O O . ALA A 1 100 ? 3.960 34.016 55.501 1.00 24.28 ? 93 ALA A O 1 ATOM 328 C CB . ALA A 1 100 ? 3.959 34.558 52.187 1.00 21.57 ? 93 ALA A CB 1 ATOM 329 N N . LYS A 1 101 ? 3.305 32.281 54.220 1.00 25.16 ? 94 LYS A N 1 ATOM 330 C CA . LYS A 1 101 ? 2.485 31.737 55.330 1.00 25.33 ? 94 LYS A CA 1 ATOM 331 C C . LYS A 1 101 ? 3.363 31.295 56.510 1.00 25.56 ? 94 LYS A C 1 ATOM 332 O O . LYS A 1 101 ? 2.987 31.457 57.676 1.00 24.37 ? 94 LYS A O 1 ATOM 333 C CB . LYS A 1 101 ? 1.665 30.557 54.808 1.00 26.26 ? 94 LYS A CB 1 ATOM 334 C CG . LYS A 1 101 ? 0.535 30.978 53.875 1.00 31.08 ? 94 LYS A CG 1 ATOM 335 C CD . LYS A 1 101 ? -0.243 29.749 53.380 1.00 42.87 ? 94 LYS A CD 1 ATOM 336 C CE . LYS A 1 101 ? -1.186 29.185 54.459 1.00 49.77 ? 94 LYS A CE 1 ATOM 337 N NZ . LYS A 1 101 ? -1.566 27.721 54.251 1.00 53.94 ? 94 LYS A NZ 1 ATOM 338 N N . GLN A 1 102 ? 4.548 30.737 56.203 1.00 26.05 ? 95 GLN A N 1 ATOM 339 C CA . GLN A 1 102 ? 5.502 30.311 57.267 1.00 26.34 ? 95 GLN A CA 1 ATOM 340 C C . GLN A 1 102 ? 5.964 31.539 58.056 1.00 26.77 ? 95 GLN A C 1 ATOM 341 O O . GLN A 1 102 ? 6.004 31.541 59.271 1.00 25.11 ? 95 GLN A O 1 ATOM 342 C CB . GLN A 1 102 ? 6.728 29.605 56.671 1.00 26.75 ? 95 GLN A CB 1 ATOM 343 C CG . GLN A 1 102 ? 7.788 29.348 57.749 1.00 27.99 ? 95 GLN A CG 1 ATOM 344 C CD . GLN A 1 102 ? 9.137 28.949 57.200 1.00 27.82 ? 95 GLN A CD 1 ATOM 345 O OE1 . GLN A 1 102 ? 9.231 28.223 56.206 1.00 28.16 ? 95 GLN A OE1 1 ATOM 346 N NE2 . GLN A 1 102 ? 10.193 29.417 57.850 1.00 26.94 ? 95 GLN A NE2 1 ATOM 347 N N . ILE A 1 103 ? 6.306 32.602 57.339 1.00 26.06 ? 96 ILE A N 1 ATOM 348 C CA . ILE A 1 103 ? 6.788 33.805 57.990 1.00 26.99 ? 96 ILE A CA 1 ATOM 349 C C . ILE A 1 103 ? 5.662 34.422 58.835 1.00 26.37 ? 96 ILE A C 1 ATOM 350 O O . ILE A 1 103 ? 5.855 34.863 59.980 1.00 25.97 ? 96 ILE A O 1 ATOM 351 C CB . ILE A 1 103 ? 7.260 34.858 56.930 1.00 26.40 ? 96 ILE A CB 1 ATOM 352 C CG1 . ILE A 1 103 ? 8.372 34.321 56.033 1.00 29.74 ? 96 ILE A CG1 1 ATOM 353 C CG2 . ILE A 1 103 ? 7.667 36.190 57.627 1.00 25.93 ? 96 ILE A CG2 1 ATOM 354 C CD1 . ILE A 1 103 ? 9.655 34.078 56.681 1.00 29.87 ? 96 ILE A CD1 1 ATOM 355 N N . GLN A 1 104 ? 4.467 34.464 58.268 1.00 26.14 ? 97 GLN A N 1 ATOM 356 C CA . GLN A 1 104 ? 3.328 34.974 59.016 1.00 25.37 ? 97 GLN A CA 1 ATOM 357 C C . GLN A 1 104 ? 3.154 34.197 60.333 1.00 27.17 ? 97 GLN A C 1 ATOM 358 O O . GLN A 1 104 ? 3.007 34.810 61.409 1.00 27.05 ? 97 GLN A O 1 ATOM 359 C CB . GLN A 1 104 ? 2.069 34.906 58.149 1.00 25.29 ? 97 GLN A CB 1 ATOM 360 C CG . GLN A 1 104 ? 0.785 35.294 58.898 1.00 25.68 ? 97 GLN A CG 1 ATOM 361 C CD . GLN A 1 104 ? -0.502 35.044 58.094 1.00 28.51 ? 97 GLN A CD 1 ATOM 362 O OE1 . GLN A 1 104 ? -0.583 34.129 57.261 1.00 28.65 ? 97 GLN A OE1 1 ATOM 363 N NE2 . GLN A 1 104 ? -1.517 35.853 58.366 1.00 28.02 ? 97 GLN A NE2 1 ATOM 364 N N . SER A 1 105 ? 3.185 32.871 60.261 1.00 26.71 ? 98 SER A N 1 ATOM 365 C CA . SER A 1 105 ? 3.049 32.049 61.478 1.00 27.99 ? 98 SER A CA 1 ATOM 366 C C . SER A 1 105 ? 4.136 32.323 62.531 1.00 27.57 ? 98 SER A C 1 ATOM 367 O O . SER A 1 105 ? 3.838 32.461 63.723 1.00 27.52 ? 98 SER A O 1 ATOM 368 C CB . SER A 1 105 ? 3.042 30.550 61.128 1.00 27.51 ? 98 SER A CB 1 ATOM 369 O OG A SER A 1 105 ? 2.819 29.785 62.292 0.50 27.94 ? 98 SER A OG 1 ATOM 370 O OG B SER A 1 105 ? 1.747 30.206 60.707 0.50 31.36 ? 98 SER A OG 1 ATOM 371 N N . GLN A 1 106 ? 5.393 32.396 62.080 1.00 26.38 ? 99 GLN A N 1 ATOM 372 C CA . GLN A 1 106 ? 6.508 32.591 63.002 1.00 27.48 ? 99 GLN A CA 1 ATOM 373 C C . GLN A 1 106 ? 6.522 33.977 63.631 1.00 27.00 ? 99 GLN A C 1 ATOM 374 O O . GLN A 1 106 ? 6.786 34.119 64.817 1.00 28.47 ? 99 GLN A O 1 ATOM 375 C CB . GLN A 1 106 ? 7.831 32.331 62.283 1.00 26.00 ? 99 GLN A CB 1 ATOM 376 C CG . GLN A 1 106 ? 7.971 30.879 61.879 1.00 30.41 ? 99 GLN A CG 1 ATOM 377 C CD . GLN A 1 106 ? 9.349 30.602 61.240 1.00 32.74 ? 99 GLN A CD 1 ATOM 378 O OE1 . GLN A 1 106 ? 9.655 31.114 60.177 1.00 30.55 ? 99 GLN A OE1 1 ATOM 379 N NE2 . GLN A 1 106 ? 10.161 29.795 61.907 1.00 36.31 ? 99 GLN A NE2 1 ATOM 380 N N . TRP A 1 107 ? 6.290 35.018 62.835 1.00 25.83 ? 100 TRP A N 1 ATOM 381 C CA . TRP A 1 107 ? 6.115 36.360 63.402 1.00 26.15 ? 100 TRP A CA 1 ATOM 382 C C . TRP A 1 107 ? 5.039 36.430 64.495 1.00 26.99 ? 100 TRP A C 1 ATOM 383 O O . TRP A 1 107 ? 5.254 37.113 65.500 1.00 27.06 ? 100 TRP A O 1 ATOM 384 C CB . TRP A 1 107 ? 5.832 37.404 62.298 1.00 24.34 ? 100 TRP A CB 1 ATOM 385 C CG . TRP A 1 107 ? 7.043 37.724 61.506 1.00 23.34 ? 100 TRP A CG 1 ATOM 386 C CD1 . TRP A 1 107 ? 8.275 37.069 61.547 1.00 24.30 ? 100 TRP A CD1 1 ATOM 387 C CD2 . TRP A 1 107 ? 7.144 38.703 60.462 1.00 22.09 ? 100 TRP A CD2 1 ATOM 388 N NE1 . TRP A 1 107 ? 9.131 37.623 60.624 1.00 22.54 ? 100 TRP A NE1 1 ATOM 389 C CE2 . TRP A 1 107 ? 8.472 38.619 59.936 1.00 22.34 ? 100 TRP A CE2 1 ATOM 390 C CE3 . TRP A 1 107 ? 6.258 39.656 59.941 1.00 21.54 ? 100 TRP A CE3 1 ATOM 391 C CZ2 . TRP A 1 107 ? 8.934 39.466 58.905 1.00 22.94 ? 100 TRP A CZ2 1 ATOM 392 C CZ3 . TRP A 1 107 ? 6.696 40.494 58.914 1.00 20.95 ? 100 TRP A CZ3 1 ATOM 393 C CH2 . TRP A 1 107 ? 8.037 40.401 58.400 1.00 23.99 ? 100 TRP A CH2 1 ATOM 394 N N . LYS A 1 108 ? 3.918 35.723 64.313 1.00 28.39 ? 101 LYS A N 1 ATOM 395 C CA . LYS A 1 108 ? 2.893 35.595 65.379 1.00 31.45 ? 101 LYS A CA 1 ATOM 396 C C . LYS A 1 108 ? 3.478 34.912 66.625 1.00 31.75 ? 101 LYS A C 1 ATOM 397 O O . LYS A 1 108 ? 3.405 35.479 67.735 1.00 31.50 ? 101 LYS A O 1 ATOM 398 C CB . LYS A 1 108 ? 1.655 34.804 64.929 1.00 32.41 ? 101 LYS A CB 1 ATOM 399 C CG . LYS A 1 108 ? 0.743 35.558 64.007 1.00 38.66 ? 101 LYS A CG 1 ATOM 400 C CD . LYS A 1 108 ? -0.384 34.678 63.425 1.00 46.95 ? 101 LYS A CD 1 ATOM 401 C CE . LYS A 1 108 ? -1.337 35.555 62.574 1.00 49.96 ? 101 LYS A CE 1 ATOM 402 N NZ . LYS A 1 108 ? -2.421 34.739 61.952 1.00 54.63 ? 101 LYS A NZ 1 ATOM 403 N N . GLU A 1 109 ? 4.072 33.730 66.420 1.00 31.16 ? 102 GLU A N 1 ATOM 404 C CA A GLU A 1 109 ? 4.781 32.943 67.449 0.50 32.51 ? 102 GLU A CA 1 ATOM 405 C CA B GLU A 1 109 ? 4.668 33.026 67.547 0.50 32.67 ? 102 GLU A CA 1 ATOM 406 C C . GLU A 1 109 ? 5.773 33.863 68.190 1.00 32.18 ? 102 GLU A C 1 ATOM 407 O O . GLU A 1 109 ? 5.896 33.852 69.435 1.00 31.78 ? 102 GLU A O 1 ATOM 408 C CB A GLU A 1 109 ? 5.571 31.771 66.795 0.50 33.23 ? 102 GLU A CB 1 ATOM 409 C CB B GLU A 1 109 ? 5.171 31.639 67.156 0.50 33.41 ? 102 GLU A CB 1 ATOM 410 C CG A GLU A 1 109 ? 4.781 30.581 66.156 0.50 35.30 ? 102 GLU A CG 1 ATOM 411 C CG B GLU A 1 109 ? 5.313 30.655 68.324 0.50 38.21 ? 102 GLU A CG 1 ATOM 412 C CD A GLU A 1 109 ? 5.633 29.658 65.211 0.50 37.39 ? 102 GLU A CD 1 ATOM 413 C CD B GLU A 1 109 ? 6.651 30.731 69.049 0.50 42.99 ? 102 GLU A CD 1 ATOM 414 O OE1 A GLU A 1 109 ? 6.829 29.375 65.500 0.50 35.45 ? 102 GLU A OE1 1 ATOM 415 O OE1 B GLU A 1 109 ? 6.755 30.162 70.164 0.50 45.65 ? 102 GLU A OE1 1 ATOM 416 O OE2 A GLU A 1 109 ? 5.097 29.206 64.164 0.50 36.28 ? 102 GLU A OE2 1 ATOM 417 O OE2 B GLU A 1 109 ? 7.597 31.351 68.514 0.50 44.07 ? 102 GLU A OE2 1 ATOM 418 N N . PHE A 1 110 ? 6.526 34.640 67.403 1.00 29.88 ? 103 PHE A N 1 ATOM 419 C CA . PHE A 1 110 ? 7.580 35.524 67.970 1.00 30.13 ? 103 PHE A CA 1 ATOM 420 C C . PHE A 1 110 ? 7.015 36.632 68.902 1.00 30.57 ? 103 PHE A C 1 ATOM 421 O O . PHE A 1 110 ? 7.772 37.254 69.644 1.00 32.18 ? 103 PHE A O 1 ATOM 422 C CB . PHE A 1 110 ? 8.459 36.214 66.881 1.00 28.55 ? 103 PHE A CB 1 ATOM 423 C CG . PHE A 1 110 ? 9.365 35.275 66.066 1.00 30.16 ? 103 PHE A CG 1 ATOM 424 C CD1 . PHE A 1 110 ? 9.664 33.965 66.501 1.00 31.66 ? 103 PHE A CD1 1 ATOM 425 C CD2 . PHE A 1 110 ? 9.933 35.735 64.884 1.00 27.75 ? 103 PHE A CD2 1 ATOM 426 C CE1 . PHE A 1 110 ? 10.502 33.109 65.732 1.00 34.65 ? 103 PHE A CE1 1 ATOM 427 C CE2 . PHE A 1 110 ? 10.784 34.880 64.087 1.00 28.58 ? 103 PHE A CE2 1 ATOM 428 C CZ . PHE A 1 110 ? 11.066 33.577 64.518 1.00 31.62 ? 103 PHE A CZ 1 ATOM 429 N N . GLY A 1 111 ? 5.706 36.895 68.837 1.00 30.24 ? 104 GLY A N 1 ATOM 430 C CA . GLY A 1 111 ? 5.057 37.871 69.715 1.00 29.39 ? 104 GLY A CA 1 ATOM 431 C C . GLY A 1 111 ? 4.433 39.127 69.102 1.00 29.30 ? 104 GLY A C 1 ATOM 432 O O . GLY A 1 111 ? 3.902 39.962 69.848 1.00 30.35 ? 104 GLY A O 1 ATOM 433 N N . LEU A 1 112 ? 4.460 39.286 67.775 1.00 27.10 ? 105 LEU A N 1 ATOM 434 C CA . LEU A 1 112 ? 3.833 40.511 67.193 1.00 25.28 ? 105 LEU A CA 1 ATOM 435 C C . LEU A 1 112 ? 2.328 40.537 67.507 1.00 27.01 ? 105 LEU A C 1 ATOM 436 O O . LEU A 1 112 ? 1.697 39.472 67.655 1.00 28.39 ? 105 LEU A O 1 ATOM 437 C CB . LEU A 1 112 ? 4.068 40.579 65.668 1.00 24.47 ? 105 LEU A CB 1 ATOM 438 C CG . LEU A 1 112 ? 5.537 40.718 65.272 1.00 23.85 ? 105 LEU A CG 1 ATOM 439 C CD1 . LEU A 1 112 ? 5.653 41.065 63.759 1.00 21.09 ? 105 LEU A CD1 1 ATOM 440 C CD2 . LEU A 1 112 ? 6.274 41.786 66.126 1.00 24.11 ? 105 LEU A CD2 1 ATOM 441 N N . ASP A 1 113 ? 1.744 41.733 67.616 1.00 26.62 ? 106 ASP A N 1 ATOM 442 C CA . ASP A 1 113 ? 0.310 41.864 67.928 1.00 29.15 ? 106 ASP A CA 1 ATOM 443 C C . ASP A 1 113 ? -0.626 41.354 66.841 1.00 29.41 ? 106 ASP A C 1 ATOM 444 O O . ASP A 1 113 ? -1.673 40.749 67.152 1.00 30.03 ? 106 ASP A O 1 ATOM 445 C CB . ASP A 1 113 ? -0.031 43.330 68.264 1.00 28.80 ? 106 ASP A CB 1 ATOM 446 C CG . ASP A 1 113 ? 0.733 43.812 69.473 1.00 31.13 ? 106 ASP A CG 1 ATOM 447 O OD1 . ASP A 1 113 ? 0.595 43.206 70.555 1.00 29.71 ? 106 ASP A OD1 1 ATOM 448 O OD2 . ASP A 1 113 ? 1.503 44.764 69.357 1.00 28.39 ? 106 ASP A OD2 1 ATOM 449 N N . SER A 1 114 ? -0.263 41.622 65.591 1.00 27.19 ? 107 SER A N 1 ATOM 450 C CA A SER A 1 114 ? -0.999 41.088 64.438 0.50 27.16 ? 107 SER A CA 1 ATOM 451 C CA B SER A 1 114 ? -1.017 41.159 64.417 0.50 27.53 ? 107 SER A CA 1 ATOM 452 C C . SER A 1 114 ? -0.042 40.828 63.300 1.00 26.18 ? 107 SER A C 1 ATOM 453 O O . SER A 1 114 ? 0.959 41.505 63.158 1.00 25.79 ? 107 SER A O 1 ATOM 454 C CB A SER A 1 114 ? -2.108 42.033 63.936 0.50 26.33 ? 107 SER A CB 1 ATOM 455 C CB B SER A 1 114 ? -1.946 42.265 63.894 0.50 26.40 ? 107 SER A CB 1 ATOM 456 O OG A SER A 1 114 ? -1.619 43.291 63.520 0.50 24.92 ? 107 SER A OG 1 ATOM 457 O OG B SER A 1 114 ? -2.703 42.846 64.950 0.50 29.36 ? 107 SER A OG 1 ATOM 458 N N . VAL A 1 115 ? -0.373 39.837 62.481 1.00 26.07 ? 108 VAL A N 1 ATOM 459 C CA . VAL A 1 115 ? 0.443 39.553 61.285 1.00 25.99 ? 108 VAL A CA 1 ATOM 460 C C . VAL A 1 115 ? -0.549 39.135 60.194 1.00 26.59 ? 108 VAL A C 1 ATOM 461 O O . VAL A 1 115 ? -1.257 38.114 60.346 1.00 26.74 ? 108 VAL A O 1 ATOM 462 C CB . VAL A 1 115 ? 1.513 38.442 61.494 1.00 26.20 ? 108 VAL A CB 1 ATOM 463 C CG1 . VAL A 1 115 ? 2.456 38.463 60.252 1.00 23.68 ? 108 VAL A CG1 1 ATOM 464 C CG2 . VAL A 1 115 ? 2.340 38.657 62.813 1.00 25.10 ? 108 VAL A CG2 1 ATOM 465 N N . GLU A 1 116 ? -0.594 39.912 59.105 1.00 25.96 ? 109 GLU A N 1 ATOM 466 C CA A GLU A 1 116 ? -1.536 39.631 58.022 0.50 26.81 ? 109 GLU A CA 1 ATOM 467 C CA B GLU A 1 116 ? -1.544 39.717 58.007 0.50 26.03 ? 109 GLU A CA 1 ATOM 468 C C . GLU A 1 116 ? -0.818 39.459 56.687 1.00 25.81 ? 109 GLU A C 1 ATOM 469 O O . GLU A 1 116 ? 0.319 39.892 56.517 1.00 24.70 ? 109 GLU A O 1 ATOM 470 C CB A GLU A 1 116 ? -2.618 40.724 57.919 0.50 28.08 ? 109 GLU A CB 1 ATOM 471 C CB B GLU A 1 116 ? -2.393 40.989 57.842 0.50 26.45 ? 109 GLU A CB 1 ATOM 472 C CG A GLU A 1 116 ? -3.697 40.648 59.014 0.50 32.51 ? 109 GLU A CG 1 ATOM 473 C CG B GLU A 1 116 ? -1.558 42.243 57.757 0.50 26.42 ? 109 GLU A CG 1 ATOM 474 C CD A GLU A 1 116 ? -4.688 39.466 58.843 0.50 38.05 ? 109 GLU A CD 1 ATOM 475 C CD B GLU A 1 116 ? -2.380 43.528 57.852 0.50 28.67 ? 109 GLU A CD 1 ATOM 476 O OE1 A GLU A 1 116 ? -5.823 39.707 58.385 0.50 40.96 ? 109 GLU A OE1 1 ATOM 477 O OE1 B GLU A 1 116 ? -2.613 44.032 58.998 0.50 26.85 ? 109 GLU A OE1 1 ATOM 478 O OE2 A GLU A 1 116 ? -4.354 38.306 59.166 0.50 39.61 ? 109 GLU A OE2 1 ATOM 479 O OE2 B GLU A 1 116 ? -2.753 44.006 56.757 0.50 24.82 ? 109 GLU A OE2 1 ATOM 480 N N . LEU A 1 117 ? -1.477 38.783 55.762 1.00 24.51 ? 110 LEU A N 1 ATOM 481 C CA . LEU A 1 117 ? -1.026 38.840 54.384 1.00 23.72 ? 110 LEU A CA 1 ATOM 482 C C . LEU A 1 117 ? -1.829 39.934 53.653 1.00 24.16 ? 110 LEU A C 1 ATOM 483 O O . LEU A 1 117 ? -3.074 40.036 53.804 1.00 23.75 ? 110 LEU A O 1 ATOM 484 C CB . LEU A 1 117 ? -1.187 37.479 53.716 1.00 24.34 ? 110 LEU A CB 1 ATOM 485 C CG . LEU A 1 117 ? -0.465 36.293 54.369 1.00 26.82 ? 110 LEU A CG 1 ATOM 486 C CD1 . LEU A 1 117 ? -0.799 35.041 53.513 1.00 31.40 ? 110 LEU A CD1 1 ATOM 487 C CD2 . LEU A 1 117 ? 1.018 36.479 54.454 1.00 26.42 ? 110 LEU A CD2 1 ATOM 488 N N . ALA A 1 118 ? -1.139 40.763 52.875 1.00 23.05 ? 111 ALA A N 1 ATOM 489 C CA . ALA A 1 118 ? -1.781 41.749 52.023 1.00 23.12 ? 111 ALA A CA 1 ATOM 490 C C . ALA A 1 118 ? -1.424 41.275 50.622 1.00 23.95 ? 111 ALA A C 1 ATOM 491 O O . ALA A 1 118 ? -0.216 41.258 50.268 1.00 23.68 ? 111 ALA A O 1 ATOM 492 C CB . ALA A 1 118 ? -1.186 43.148 52.263 1.00 23.52 ? 111 ALA A CB 1 ATOM 493 N N . HIS A 1 119 ? -2.429 40.907 49.840 1.00 22.10 ? 112 HIS A N 1 ATOM 494 C CA . HIS A 1 119 ? -2.178 40.383 48.478 1.00 22.92 ? 112 HIS A CA 1 ATOM 495 C C . HIS A 1 119 ? -2.632 41.367 47.389 1.00 21.96 ? 112 HIS A C 1 ATOM 496 O O . HIS A 1 119 ? -3.486 42.214 47.652 1.00 20.98 ? 112 HIS A O 1 ATOM 497 C CB . HIS A 1 119 ? -2.844 39.017 48.272 1.00 22.78 ? 112 HIS A CB 1 ATOM 498 C CG . HIS A 1 119 ? -4.345 39.058 48.306 1.00 25.73 ? 112 HIS A CG 1 ATOM 499 N ND1 . HIS A 1 119 ? -5.073 38.730 49.435 1.00 31.14 ? 112 HIS A ND1 1 ATOM 500 C CD2 . HIS A 1 119 ? -5.255 39.406 47.358 1.00 26.81 ? 112 HIS A CD2 1 ATOM 501 C CE1 . HIS A 1 119 ? -6.364 38.839 49.174 1.00 29.94 ? 112 HIS A CE1 1 ATOM 502 N NE2 . HIS A 1 119 ? -6.503 39.255 47.925 1.00 29.32 ? 112 HIS A NE2 1 ATOM 503 N N . TYR A 1 120 ? -2.011 41.280 46.206 1.00 21.38 ? 113 TYR A N 1 ATOM 504 C CA . TYR A 1 120 ? -2.323 42.125 45.036 1.00 21.31 ? 113 TYR A CA 1 ATOM 505 C C . TYR A 1 120 ? -2.199 41.255 43.799 1.00 20.59 ? 113 TYR A C 1 ATOM 506 O O . TYR A 1 120 ? -1.494 40.233 43.839 1.00 20.94 ? 113 TYR A O 1 ATOM 507 C CB . TYR A 1 120 ? -1.367 43.354 44.939 1.00 19.57 ? 113 TYR A CB 1 ATOM 508 C CG . TYR A 1 120 ? -1.400 44.121 46.199 1.00 17.70 ? 113 TYR A CG 1 ATOM 509 C CD1 . TYR A 1 120 ? -2.432 45.066 46.448 1.00 18.59 ? 113 TYR A CD1 1 ATOM 510 C CD2 . TYR A 1 120 ? -0.481 43.835 47.226 1.00 18.55 ? 113 TYR A CD2 1 ATOM 511 C CE1 . TYR A 1 120 ? -2.486 45.729 47.689 1.00 19.72 ? 113 TYR A CE1 1 ATOM 512 C CE2 . TYR A 1 120 ? -0.568 44.464 48.443 1.00 20.78 ? 113 TYR A CE2 1 ATOM 513 C CZ . TYR A 1 120 ? -1.560 45.417 48.671 1.00 20.07 ? 113 TYR A CZ 1 ATOM 514 O OH . TYR A 1 120 ? -1.631 46.054 49.923 1.00 19.32 ? 113 TYR A OH 1 ATOM 515 N N . ASP A 1 121 ? -2.892 41.634 42.729 1.00 20.85 ? 114 ASP A N 1 ATOM 516 C CA . ASP A 1 121 ? -2.823 40.880 41.447 1.00 21.72 ? 114 ASP A CA 1 ATOM 517 C C . ASP A 1 121 ? -2.125 41.777 40.451 1.00 21.34 ? 114 ASP A C 1 ATOM 518 O O . ASP A 1 121 ? -2.728 42.737 39.925 1.00 21.45 ? 114 ASP A O 1 ATOM 519 C CB . ASP A 1 121 ? -4.238 40.458 40.966 1.00 23.34 ? 114 ASP A CB 1 ATOM 520 C CG . ASP A 1 121 ? -4.916 39.521 41.973 1.00 27.25 ? 114 ASP A CG 1 ATOM 521 O OD1 . ASP A 1 121 ? -4.250 38.536 42.391 1.00 26.09 ? 114 ASP A OD1 1 ATOM 522 O OD2 . ASP A 1 121 ? -6.047 39.816 42.396 1.00 28.52 ? 114 ASP A OD2 1 ATOM 523 N N . VAL A 1 122 ? -0.853 41.457 40.198 1.00 20.86 ? 115 VAL A N 1 ATOM 524 C CA . VAL A 1 122 ? 0.037 42.358 39.472 1.00 20.02 ? 115 VAL A CA 1 ATOM 525 C C . VAL A 1 122 ? 0.615 41.672 38.230 1.00 20.61 ? 115 VAL A C 1 ATOM 526 O O . VAL A 1 122 ? 0.697 40.423 38.165 1.00 20.71 ? 115 VAL A O 1 ATOM 527 C CB . VAL A 1 122 ? 1.202 42.881 40.376 1.00 19.64 ? 115 VAL A CB 1 ATOM 528 C CG1 . VAL A 1 122 ? 0.658 43.662 41.597 1.00 16.44 ? 115 VAL A CG1 1 ATOM 529 C CG2 . VAL A 1 122 ? 2.197 41.711 40.783 1.00 17.30 ? 115 VAL A CG2 1 ATOM 530 N N . LEU A 1 123 ? 1.064 42.495 37.279 1.00 19.40 ? 116 LEU A N 1 ATOM 531 C CA . LEU A 1 123 ? 1.682 41.938 36.078 1.00 19.98 ? 116 LEU A CA 1 ATOM 532 C C . LEU A 1 123 ? 3.053 41.357 36.398 1.00 20.29 ? 116 LEU A C 1 ATOM 533 O O . LEU A 1 123 ? 3.945 42.104 36.846 1.00 21.83 ? 116 LEU A O 1 ATOM 534 C CB . LEU A 1 123 ? 1.816 43.030 34.992 1.00 18.43 ? 116 LEU A CB 1 ATOM 535 C CG . LEU A 1 123 ? 2.135 42.407 33.598 1.00 20.73 ? 116 LEU A CG 1 ATOM 536 C CD1 . LEU A 1 123 ? 0.859 41.713 32.995 1.00 21.22 ? 116 LEU A CD1 1 ATOM 537 C CD2 . LEU A 1 123 ? 2.644 43.455 32.610 1.00 22.06 ? 116 LEU A CD2 1 ATOM 538 N N . LEU A 1 124 ? 3.221 40.049 36.152 1.00 20.86 ? 117 LEU A N 1 ATOM 539 C CA . LEU A 1 124 ? 4.549 39.391 36.215 1.00 20.80 ? 117 LEU A CA 1 ATOM 540 C C . LEU A 1 124 ? 4.912 38.850 34.831 1.00 21.41 ? 117 LEU A C 1 ATOM 541 O O . LEU A 1 124 ? 4.157 39.056 33.888 1.00 22.61 ? 117 LEU A O 1 ATOM 542 C CB . LEU A 1 124 ? 4.595 38.289 37.315 1.00 19.84 ? 117 LEU A CB 1 ATOM 543 C CG . LEU A 1 124 ? 4.255 38.714 38.777 1.00 20.40 ? 117 LEU A CG 1 ATOM 544 C CD1 . LEU A 1 124 ? 4.420 37.520 39.809 1.00 18.07 ? 117 LEU A CD1 1 ATOM 545 C CD2 . LEU A 1 124 ? 5.086 39.977 39.293 1.00 16.48 ? 117 LEU A CD2 1 ATOM 546 N N . SER A 1 125 ? 6.059 38.176 34.722 1.00 20.95 ? 118 SER A N 1 ATOM 547 C CA . SER A 1 125 ? 6.630 37.719 33.445 1.00 21.91 ? 118 SER A CA 1 ATOM 548 C C . SER A 1 125 ? 7.406 36.434 33.709 1.00 22.55 ? 118 SER A C 1 ATOM 549 O O . SER A 1 125 ? 8.176 36.353 34.672 1.00 21.45 ? 118 SER A O 1 ATOM 550 C CB . SER A 1 125 ? 7.573 38.782 32.862 1.00 22.97 ? 118 SER A CB 1 ATOM 551 O OG . SER A 1 125 ? 8.415 38.269 31.804 1.00 23.99 ? 118 SER A OG 1 ATOM 552 N N . TYR A 1 126 ? 7.170 35.431 32.864 1.00 22.64 ? 119 TYR A N 1 ATOM 553 C CA . TYR A 1 126 ? 7.819 34.138 32.990 1.00 23.67 ? 119 TYR A CA 1 ATOM 554 C C . TYR A 1 126 ? 8.179 33.571 31.628 1.00 25.00 ? 119 TYR A C 1 ATOM 555 O O . TYR A 1 126 ? 7.462 33.792 30.667 1.00 25.30 ? 119 TYR A O 1 ATOM 556 C CB . TYR A 1 126 ? 6.861 33.136 33.618 1.00 24.74 ? 119 TYR A CB 1 ATOM 557 C CG . TYR A 1 126 ? 6.370 33.514 34.999 1.00 25.26 ? 119 TYR A CG 1 ATOM 558 C CD1 . TYR A 1 126 ? 7.228 33.458 36.102 1.00 25.54 ? 119 TYR A CD1 1 ATOM 559 C CD2 . TYR A 1 126 ? 5.042 33.908 35.187 1.00 27.68 ? 119 TYR A CD2 1 ATOM 560 C CE1 . TYR A 1 126 ? 6.751 33.779 37.381 1.00 23.97 ? 119 TYR A CE1 1 ATOM 561 C CE2 . TYR A 1 126 ? 4.548 34.216 36.431 1.00 27.51 ? 119 TYR A CE2 1 ATOM 562 C CZ . TYR A 1 126 ? 5.411 34.136 37.534 1.00 26.68 ? 119 TYR A CZ 1 ATOM 563 O OH . TYR A 1 126 ? 4.910 34.434 38.763 1.00 25.20 ? 119 TYR A OH 1 ATOM 564 N N . PRO A 1 127 ? 9.276 32.805 31.556 1.00 26.05 ? 120 PRO A N 1 ATOM 565 C CA . PRO A 1 127 ? 9.547 32.071 30.312 1.00 27.44 ? 120 PRO A CA 1 ATOM 566 C C . PRO A 1 127 ? 8.462 31.046 30.037 1.00 29.83 ? 120 PRO A C 1 ATOM 567 O O . PRO A 1 127 ? 7.770 30.603 30.965 1.00 30.37 ? 120 PRO A O 1 ATOM 568 C CB . PRO A 1 127 ? 10.874 31.332 30.588 1.00 27.20 ? 120 PRO A CB 1 ATOM 569 C CG . PRO A 1 127 ? 11.504 32.063 31.805 1.00 27.14 ? 120 PRO A CG 1 ATOM 570 C CD . PRO A 1 127 ? 10.328 32.623 32.582 1.00 24.98 ? 120 PRO A CD 1 ATOM 571 N N . ASN A 1 128 ? 8.306 30.686 28.768 1.00 31.70 ? 121 ASN A N 1 ATOM 572 C CA . ASN A 1 128 ? 7.401 29.611 28.380 1.00 34.52 ? 121 ASN A CA 1 ATOM 573 C C . ASN A 1 128 ? 8.110 28.268 28.604 1.00 36.16 ? 121 ASN A C 1 ATOM 574 O O . ASN A 1 128 ? 9.136 27.975 27.970 1.00 35.92 ? 121 ASN A O 1 ATOM 575 C CB . ASN A 1 128 ? 7.001 29.783 26.925 1.00 35.01 ? 121 ASN A CB 1 ATOM 576 C CG . ASN A 1 128 ? 5.973 28.743 26.462 1.00 39.89 ? 121 ASN A CG 1 ATOM 577 O OD1 . ASN A 1 128 ? 6.056 27.585 26.832 1.00 42.44 ? 121 ASN A OD1 1 ATOM 578 N ND2 . ASN A 1 128 ? 5.009 29.165 25.642 1.00 45.91 ? 121 ASN A ND2 1 ATOM 579 N N . LYS A 1 129 ? 7.596 27.493 29.553 1.00 38.38 ? 122 LYS A N 1 ATOM 580 C CA . LYS A 1 129 ? 8.118 26.153 29.890 1.00 40.89 ? 122 LYS A CA 1 ATOM 581 C C . LYS A 1 129 ? 8.331 25.193 28.693 1.00 42.49 ? 122 LYS A C 1 ATOM 582 O O . LYS A 1 129 ? 9.281 24.402 28.685 1.00 43.03 ? 122 LYS A O 1 ATOM 583 C CB . LYS A 1 129 ? 7.193 25.497 30.929 1.00 42.20 ? 122 LYS A CB 1 ATOM 584 C CG . LYS A 1 129 ? 7.734 25.479 32.369 1.00 45.17 ? 122 LYS A CG 1 ATOM 585 C CD . LYS A 1 129 ? 8.362 24.085 32.654 1.00 51.25 ? 122 LYS A CD 1 ATOM 586 C CE . LYS A 1 129 ? 8.357 23.726 34.144 1.00 53.19 ? 122 LYS A CE 1 ATOM 587 N NZ . LYS A 1 129 ? 8.853 22.318 34.371 1.00 54.92 ? 122 LYS A NZ 1 ATOM 588 N N . THR A 1 130 ? 7.485 25.268 27.671 1.00 42.70 ? 123 THR A N 1 ATOM 589 C CA . THR A 1 130 ? 7.610 24.335 26.542 1.00 44.42 ? 123 THR A CA 1 ATOM 590 C C . THR A 1 130 ? 8.208 24.929 25.266 1.00 44.83 ? 123 THR A C 1 ATOM 591 O O . THR A 1 130 ? 8.287 24.254 24.249 1.00 46.32 ? 123 THR A O 1 ATOM 592 C CB . THR A 1 130 ? 6.248 23.679 26.184 1.00 45.26 ? 123 THR A CB 1 ATOM 593 O OG1 . THR A 1 130 ? 5.311 24.710 25.843 1.00 45.26 ? 123 THR A OG1 1 ATOM 594 C CG2 . THR A 1 130 ? 5.711 22.846 27.365 1.00 45.23 ? 123 THR A CG2 1 ATOM 595 N N . HIS A 1 131 ? 8.637 26.178 25.329 1.00 43.70 ? 124 HIS A N 1 ATOM 596 C CA . HIS A 1 131 ? 9.149 26.900 24.176 1.00 43.88 ? 124 HIS A CA 1 ATOM 597 C C . HIS A 1 131 ? 10.279 27.847 24.672 1.00 41.89 ? 124 HIS A C 1 ATOM 598 O O . HIS A 1 131 ? 10.052 29.041 24.840 1.00 40.65 ? 124 HIS A O 1 ATOM 599 C CB . HIS A 1 131 ? 7.993 27.716 23.620 1.00 44.79 ? 124 HIS A CB 1 ATOM 600 C CG . HIS A 1 131 ? 8.128 28.098 22.180 1.00 50.54 ? 124 HIS A CG 1 ATOM 601 N ND1 . HIS A 1 131 ? 8.664 27.258 21.225 1.00 57.36 ? 124 HIS A ND1 1 ATOM 602 C CD2 . HIS A 1 131 ? 7.715 29.205 21.516 1.00 54.17 ? 124 HIS A CD2 1 ATOM 603 C CE1 . HIS A 1 131 ? 8.627 27.853 20.043 1.00 58.48 ? 124 HIS A CE1 1 ATOM 604 N NE2 . HIS A 1 131 ? 8.054 29.036 20.191 1.00 57.88 ? 124 HIS A NE2 1 ATOM 605 N N . PRO A 1 132 ? 11.485 27.296 24.939 1.00 40.40 ? 125 PRO A N 1 ATOM 606 C CA . PRO A 1 132 ? 12.574 28.014 25.638 1.00 38.35 ? 125 PRO A CA 1 ATOM 607 C C . PRO A 1 132 ? 13.244 29.179 24.878 1.00 37.37 ? 125 PRO A C 1 ATOM 608 O O . PRO A 1 132 ? 13.364 29.173 23.638 1.00 37.56 ? 125 PRO A O 1 ATOM 609 C CB . PRO A 1 132 ? 13.583 26.900 25.973 1.00 39.62 ? 125 PRO A CB 1 ATOM 610 C CG . PRO A 1 132 ? 13.271 25.793 24.996 1.00 41.39 ? 125 PRO A CG 1 ATOM 611 C CD . PRO A 1 132 ? 11.810 25.871 24.717 1.00 41.49 ? 125 PRO A CD 1 ATOM 612 N N . ASN A 1 133 ? 13.645 30.200 25.641 1.00 34.35 ? 126 ASN A N 1 ATOM 613 C CA . ASN A 1 133 ? 14.339 31.360 25.091 1.00 32.96 ? 126 ASN A CA 1 ATOM 614 C C . ASN A 1 133 ? 15.780 30.984 24.781 1.00 32.52 ? 126 ASN A C 1 ATOM 615 O O . ASN A 1 133 ? 16.416 30.265 25.561 1.00 32.17 ? 126 ASN A O 1 ATOM 616 C CB . ASN A 1 133 ? 14.339 32.536 26.108 1.00 30.40 ? 126 ASN A CB 1 ATOM 617 C CG . ASN A 1 133 ? 12.951 32.958 26.503 1.00 31.76 ? 126 ASN A CG 1 ATOM 618 O OD1 . ASN A 1 133 ? 12.039 32.946 25.679 1.00 30.08 ? 126 ASN A OD1 1 ATOM 619 N ND2 . ASN A 1 133 ? 12.765 33.322 27.794 1.00 28.81 ? 126 ASN A ND2 1 ATOM 620 N N . TYR A 1 134 ? 16.288 31.443 23.645 1.00 32.48 ? 127 TYR A N 1 ATOM 621 C CA . TYR A 1 134 ? 17.726 31.272 23.343 1.00 33.10 ? 127 TYR A CA 1 ATOM 622 C C . TYR A 1 134 ? 18.110 32.193 22.193 1.00 33.23 ? 127 TYR A C 1 ATOM 623 O O . TYR A 1 134 ? 17.248 32.830 21.565 1.00 33.08 ? 127 TYR A O 1 ATOM 624 C CB . TYR A 1 134 ? 18.100 29.804 23.061 1.00 34.26 ? 127 TYR A CB 1 ATOM 625 C CG . TYR A 1 134 ? 17.604 29.277 21.720 1.00 35.83 ? 127 TYR A CG 1 ATOM 626 C CD1 . TYR A 1 134 ? 18.487 29.069 20.652 1.00 39.80 ? 127 TYR A CD1 1 ATOM 627 C CD2 . TYR A 1 134 ? 16.254 28.972 21.527 1.00 36.02 ? 127 TYR A CD2 1 ATOM 628 C CE1 . TYR A 1 134 ? 18.030 28.545 19.416 1.00 39.30 ? 127 TYR A CE1 1 ATOM 629 C CE2 . TYR A 1 134 ? 15.786 28.481 20.316 1.00 39.07 ? 127 TYR A CE2 1 ATOM 630 C CZ . TYR A 1 134 ? 16.674 28.264 19.264 1.00 41.90 ? 127 TYR A CZ 1 ATOM 631 O OH . TYR A 1 134 ? 16.183 27.786 18.066 1.00 42.79 ? 127 TYR A OH 1 ATOM 632 N N . ILE A 1 135 ? 19.412 32.274 21.938 1.00 33.89 ? 128 ILE A N 1 ATOM 633 C CA . ILE A 1 135 ? 19.951 33.091 20.875 1.00 33.88 ? 128 ILE A CA 1 ATOM 634 C C . ILE A 1 135 ? 20.810 32.171 19.996 1.00 35.51 ? 128 ILE A C 1 ATOM 635 O O . ILE A 1 135 ? 21.459 31.233 20.493 1.00 34.64 ? 128 ILE A O 1 ATOM 636 C CB . ILE A 1 135 ? 20.833 34.256 21.425 1.00 34.29 ? 128 ILE A CB 1 ATOM 637 C CG1 . ILE A 1 135 ? 20.037 35.179 22.369 1.00 31.39 ? 128 ILE A CG1 1 ATOM 638 C CG2 . ILE A 1 135 ? 21.484 35.068 20.277 1.00 34.32 ? 128 ILE A CG2 1 ATOM 639 C CD1 . ILE A 1 135 ? 20.912 35.929 23.381 1.00 29.43 ? 128 ILE A CD1 1 ATOM 640 N N . SER A 1 136 ? 20.768 32.434 18.695 1.00 36.24 ? 129 SER A N 1 ATOM 641 C CA . SER A 1 136 ? 21.599 31.733 17.713 1.00 38.29 ? 129 SER A CA 1 ATOM 642 C C . SER A 1 136 ? 22.447 32.656 16.873 1.00 39.24 ? 129 SER A C 1 ATOM 643 O O . SER A 1 136 ? 22.126 33.833 16.677 1.00 38.58 ? 129 SER A O 1 ATOM 644 C CB . SER A 1 136 ? 20.731 30.944 16.713 1.00 38.46 ? 129 SER A CB 1 ATOM 645 O OG . SER A 1 136 ? 19.886 30.024 17.367 1.00 41.22 ? 129 SER A OG 1 ATOM 646 N N . ILE A 1 137 ? 23.518 32.074 16.330 1.00 40.56 ? 130 ILE A N 1 ATOM 647 C CA . ILE A 1 137 ? 24.152 32.605 15.146 1.00 42.30 ? 130 ILE A CA 1 ATOM 648 C C . ILE A 1 137 ? 23.597 31.703 14.046 1.00 44.84 ? 130 ILE A C 1 ATOM 649 O O . ILE A 1 137 ? 23.587 30.477 14.166 1.00 44.00 ? 130 ILE A O 1 ATOM 650 C CB . ILE A 1 137 ? 25.688 32.482 15.183 1.00 43.52 ? 130 ILE A CB 1 ATOM 651 C CG1 . ILE A 1 137 ? 26.304 33.346 16.298 1.00 41.20 ? 130 ILE A CG1 1 ATOM 652 C CG2 . ILE A 1 137 ? 26.296 32.833 13.804 1.00 42.14 ? 130 ILE A CG2 1 ATOM 653 C CD1 . ILE A 1 137 ? 27.829 33.071 16.485 1.00 42.01 ? 130 ILE A CD1 1 ATOM 654 N N . ILE A 1 138 ? 23.116 32.343 12.995 1.00 47.97 ? 131 ILE A N 1 ATOM 655 C CA . ILE A 1 138 ? 22.412 31.681 11.917 1.00 51.46 ? 131 ILE A CA 1 ATOM 656 C C . ILE A 1 138 ? 23.183 31.951 10.609 1.00 53.99 ? 131 ILE A C 1 ATOM 657 O O . ILE A 1 138 ? 23.631 33.078 10.370 1.00 53.85 ? 131 ILE A O 1 ATOM 658 C CB . ILE A 1 138 ? 20.903 32.135 11.930 1.00 51.58 ? 131 ILE A CB 1 ATOM 659 C CG1 . ILE A 1 138 ? 20.010 31.130 11.198 1.00 54.73 ? 131 ILE A CG1 1 ATOM 660 C CG2 . ILE A 1 138 ? 20.710 33.591 11.446 1.00 52.15 ? 131 ILE A CG2 1 ATOM 661 C CD1 . ILE A 1 138 ? 18.487 31.392 11.424 1.00 56.32 ? 131 ILE A CD1 1 ATOM 662 N N . ASN A 1 139 ? 23.402 30.912 9.799 1.00 55.83 ? 132 ASN A N 1 ATOM 663 C CA . ASN A 1 139 ? 24.068 31.123 8.494 1.00 59.15 ? 132 ASN A CA 1 ATOM 664 C C . ASN A 1 139 ? 23.091 31.594 7.407 1.00 60.95 ? 132 ASN A C 1 ATOM 665 O O . ASN A 1 139 ? 21.887 31.702 7.666 1.00 60.43 ? 132 ASN A O 1 ATOM 666 C CB . ASN A 1 139 ? 24.899 29.903 8.053 1.00 59.75 ? 132 ASN A CB 1 ATOM 667 C CG . ASN A 1 139 ? 24.047 28.702 7.678 1.00 59.27 ? 132 ASN A CG 1 ATOM 668 O OD1 . ASN A 1 139 ? 22.856 28.822 7.393 1.00 58.43 ? 132 ASN A OD1 1 ATOM 669 N ND2 . ASN A 1 139 ? 24.666 27.529 7.685 1.00 57.74 ? 132 ASN A ND2 1 ATOM 670 N N . GLU A 1 140 ? 23.601 31.869 6.203 1.00 63.75 ? 133 GLU A N 1 ATOM 671 C CA . GLU A 1 140 ? 22.754 32.383 5.112 1.00 65.90 ? 133 GLU A CA 1 ATOM 672 C C . GLU A 1 140 ? 21.690 31.390 4.605 1.00 66.88 ? 133 GLU A C 1 ATOM 673 O O . GLU A 1 140 ? 20.701 31.800 3.994 1.00 67.37 ? 133 GLU A O 1 ATOM 674 C CB . GLU A 1 140 ? 23.603 32.890 3.949 1.00 67.48 ? 133 GLU A CB 1 ATOM 675 C CG . GLU A 1 140 ? 24.528 31.828 3.337 1.00 70.03 ? 133 GLU A CG 1 ATOM 676 C CD . GLU A 1 140 ? 25.339 32.365 2.169 1.00 71.61 ? 133 GLU A CD 1 ATOM 677 O OE1 . GLU A 1 140 ? 25.508 31.624 1.182 1.00 73.91 ? 133 GLU A OE1 1 ATOM 678 O OE2 . GLU A 1 140 ? 25.792 33.531 2.241 1.00 71.78 ? 133 GLU A OE2 1 ATOM 679 N N . ASP A 1 141 ? 21.902 30.099 4.863 1.00 67.46 ? 134 ASP A N 1 ATOM 680 C CA . ASP A 1 141 ? 20.890 29.067 4.609 1.00 68.40 ? 134 ASP A CA 1 ATOM 681 C C . ASP A 1 141 ? 19.816 29.063 5.701 1.00 67.16 ? 134 ASP A C 1 ATOM 682 O O . ASP A 1 141 ? 18.765 28.435 5.553 1.00 68.16 ? 134 ASP A O 1 ATOM 683 C CB . ASP A 1 141 ? 21.546 27.686 4.535 1.00 69.17 ? 134 ASP A CB 1 ATOM 684 C CG . ASP A 1 141 ? 22.591 27.590 3.433 1.00 71.95 ? 134 ASP A CG 1 ATOM 685 O OD1 . ASP A 1 141 ? 22.517 28.368 2.454 1.00 73.09 ? 134 ASP A OD1 1 ATOM 686 O OD2 . ASP A 1 141 ? 23.495 26.734 3.547 1.00 72.42 ? 134 ASP A OD2 1 ATOM 687 N N . GLY A 1 142 ? 20.088 29.760 6.799 1.00 64.80 ? 135 GLY A N 1 ATOM 688 C CA . GLY A 1 142 ? 19.192 29.750 7.938 1.00 62.87 ? 135 GLY A CA 1 ATOM 689 C C . GLY A 1 142 ? 19.443 28.596 8.898 1.00 61.33 ? 135 GLY A C 1 ATOM 690 O O . GLY A 1 142 ? 18.564 28.259 9.694 1.00 61.58 ? 135 GLY A O 1 ATOM 691 N N . ASN A 1 143 ? 20.633 28.001 8.843 1.00 60.01 ? 136 ASN A N 1 ATOM 692 C CA . ASN A 1 143 ? 21.026 26.998 9.831 1.00 58.04 ? 136 ASN A CA 1 ATOM 693 C C . ASN A 1 143 ? 21.561 27.661 11.089 1.00 55.12 ? 136 ASN A C 1 ATOM 694 O O . ASN A 1 143 ? 22.443 28.532 11.018 1.00 55.26 ? 136 ASN A O 1 ATOM 695 C CB . ASN A 1 143 ? 22.089 26.052 9.274 1.00 59.19 ? 136 ASN A CB 1 ATOM 696 C CG . ASN A 1 143 ? 21.623 25.319 8.040 1.00 62.93 ? 136 ASN A CG 1 ATOM 697 O OD1 . ASN A 1 143 ? 20.426 25.123 7.840 1.00 66.12 ? 136 ASN A OD1 1 ATOM 698 N ND2 . ASN A 1 143 ? 22.566 24.917 7.200 1.00 62.47 ? 136 ASN A ND2 1 ATOM 699 N N . GLU A 1 144 ? 21.021 27.255 12.234 1.00 51.86 ? 137 GLU A N 1 ATOM 700 C CA . GLU A 1 144 ? 21.481 27.786 13.522 1.00 48.42 ? 137 GLU A CA 1 ATOM 701 C C . GLU A 1 144 ? 22.722 27.005 13.907 1.00 47.55 ? 137 GLU A C 1 ATOM 702 O O . GLU A 1 144 ? 22.638 25.847 14.300 1.00 46.67 ? 137 GLU A O 1 ATOM 703 C CB . GLU A 1 144 ? 20.368 27.704 14.566 1.00 46.95 ? 137 GLU A CB 1 ATOM 704 C CG . GLU A 1 144 ? 19.126 28.514 14.153 1.00 45.80 ? 137 GLU A CG 1 ATOM 705 C CD . GLU A 1 144 ? 18.052 28.593 15.227 1.00 45.07 ? 137 GLU A CD 1 ATOM 706 O OE1 . GLU A 1 144 ? 18.040 27.758 16.157 1.00 42.65 ? 137 GLU A OE1 1 ATOM 707 O OE2 . GLU A 1 144 ? 17.200 29.496 15.122 1.00 43.70 ? 137 GLU A OE2 1 ATOM 708 N N . ILE A 1 145 ? 23.882 27.633 13.717 1.00 47.31 ? 138 ILE A N 1 ATOM 709 C CA . ILE A 1 145 ? 25.182 26.946 13.888 1.00 47.79 ? 138 ILE A CA 1 ATOM 710 C C . ILE A 1 145 ? 25.757 27.057 15.301 1.00 46.37 ? 138 ILE A C 1 ATOM 711 O O . ILE A 1 145 ? 26.719 26.368 15.642 1.00 46.26 ? 138 ILE A O 1 ATOM 712 C CB . ILE A 1 145 ? 26.239 27.395 12.834 1.00 49.21 ? 138 ILE A CB 1 ATOM 713 C CG1 . ILE A 1 145 ? 26.545 28.896 12.978 1.00 48.04 ? 138 ILE A CG1 1 ATOM 714 C CG2 . ILE A 1 145 ? 25.777 26.979 11.417 1.00 50.32 ? 138 ILE A CG2 1 ATOM 715 C CD1 . ILE A 1 145 ? 27.639 29.419 12.039 1.00 52.36 ? 138 ILE A CD1 1 ATOM 716 N N . PHE A 1 146 ? 25.154 27.921 16.117 1.00 43.93 ? 139 PHE A N 1 ATOM 717 C CA . PHE A 1 146 ? 25.521 28.053 17.509 1.00 42.87 ? 139 PHE A CA 1 ATOM 718 C C . PHE A 1 146 ? 24.272 28.459 18.268 1.00 40.38 ? 139 PHE A C 1 ATOM 719 O O . PHE A 1 146 ? 23.520 29.303 17.797 1.00 38.37 ? 139 PHE A O 1 ATOM 720 C CB . PHE A 1 146 ? 26.592 29.131 17.724 1.00 43.49 ? 139 PHE A CB 1 ATOM 721 C CG . PHE A 1 146 ? 26.757 29.517 19.168 1.00 44.15 ? 139 PHE A CG 1 ATOM 722 C CD1 . PHE A 1 146 ? 27.404 28.650 20.064 1.00 45.52 ? 139 PHE A CD1 1 ATOM 723 C CD2 . PHE A 1 146 ? 26.240 30.721 19.649 1.00 43.88 ? 139 PHE A CD2 1 ATOM 724 C CE1 . PHE A 1 146 ? 27.522 28.990 21.419 1.00 46.33 ? 139 PHE A CE1 1 ATOM 725 C CE2 . PHE A 1 146 ? 26.352 31.066 21.013 1.00 41.23 ? 139 PHE A CE2 1 ATOM 726 C CZ . PHE A 1 146 ? 27.004 30.208 21.889 1.00 41.82 ? 139 PHE A CZ 1 ATOM 727 N N . ASN A 1 147 ? 24.060 27.846 19.425 1.00 39.57 ? 140 ASN A N 1 ATOM 728 C CA . ASN A 1 147 ? 22.949 28.201 20.285 1.00 38.93 ? 140 ASN A CA 1 ATOM 729 C C . ASN A 1 147 ? 23.441 28.482 21.670 1.00 37.58 ? 140 ASN A C 1 ATOM 730 O O . ASN A 1 147 ? 24.300 27.745 22.180 1.00 37.03 ? 140 ASN A O 1 ATOM 731 C CB . ASN A 1 147 ? 21.963 27.044 20.381 1.00 40.29 ? 140 ASN A CB 1 ATOM 732 C CG . ASN A 1 147 ? 21.224 26.797 19.083 1.00 42.83 ? 140 ASN A CG 1 ATOM 733 O OD1 . ASN A 1 147 ? 21.058 27.710 18.271 1.00 42.88 ? 140 ASN A OD1 1 ATOM 734 N ND2 . ASN A 1 147 ? 20.768 25.556 18.888 1.00 46.04 ? 140 ASN A ND2 1 ATOM 735 N N . THR A 1 148 ? 22.893 29.537 22.289 1.00 35.46 ? 141 THR A N 1 ATOM 736 C CA . THR A 1 148 ? 23.187 29.829 23.690 1.00 34.96 ? 141 THR A CA 1 ATOM 737 C C . THR A 1 148 ? 22.463 28.806 24.593 1.00 35.45 ? 141 THR A C 1 ATOM 738 O O . THR A 1 148 ? 21.528 28.108 24.154 1.00 35.25 ? 141 THR A O 1 ATOM 739 C CB . THR A 1 148 ? 22.800 31.276 24.070 1.00 33.73 ? 141 THR A CB 1 ATOM 740 O OG1 . THR A 1 148 ? 21.393 31.463 23.863 1.00 33.54 ? 141 THR A OG1 1 ATOM 741 C CG2 . THR A 1 148 ? 23.549 32.281 23.228 1.00 33.27 ? 141 THR A CG2 1 ATOM 742 N N . SER A 1 149 ? 22.896 28.732 25.843 1.00 34.99 ? 142 SER A N 1 ATOM 743 C CA . SER A 1 149 ? 22.435 27.718 26.782 1.00 35.41 ? 142 SER A CA 1 ATOM 744 C C . SER A 1 149 ? 20.952 27.835 27.126 1.00 34.79 ? 142 SER A C 1 ATOM 745 O O . SER A 1 149 ? 20.384 28.932 27.121 1.00 34.65 ? 142 SER A O 1 ATOM 746 C CB . SER A 1 149 ? 23.252 27.853 28.081 1.00 35.68 ? 142 SER A CB 1 ATOM 747 O OG A SER A 1 149 ? 22.723 28.883 28.920 0.50 32.97 ? 142 SER A OG 1 ATOM 748 O OG B SER A 1 149 ? 23.835 26.621 28.441 0.50 37.99 ? 142 SER A OG 1 ATOM 749 N N . LEU A 1 150 ? 20.310 26.714 27.436 1.00 35.20 ? 143 LEU A N 1 ATOM 750 C CA . LEU A 1 150 ? 18.900 26.778 27.857 1.00 34.94 ? 143 LEU A CA 1 ATOM 751 C C . LEU A 1 150 ? 18.761 26.908 29.377 1.00 34.18 ? 143 LEU A C 1 ATOM 752 O O . LEU A 1 150 ? 17.651 27.174 29.885 1.00 32.05 ? 143 LEU A O 1 ATOM 753 C CB . LEU A 1 150 ? 18.104 25.570 27.343 1.00 36.88 ? 143 LEU A CB 1 ATOM 754 C CG . LEU A 1 150 ? 18.124 25.356 25.819 1.00 39.59 ? 143 LEU A CG 1 ATOM 755 C CD1 . LEU A 1 150 ? 17.285 24.150 25.454 1.00 43.90 ? 143 LEU A CD1 1 ATOM 756 C CD2 . LEU A 1 150 ? 17.636 26.601 25.098 1.00 41.07 ? 143 LEU A CD2 1 ATOM 757 N N . PHE A 1 151 ? 19.870 26.725 30.103 1.00 32.83 ? 144 PHE A N 1 ATOM 758 C CA . PHE A 1 151 ? 19.832 26.836 31.570 1.00 31.85 ? 144 PHE A CA 1 ATOM 759 C C . PHE A 1 151 ? 21.251 26.913 32.089 1.00 30.82 ? 144 PHE A C 1 ATOM 760 O O . PHE A 1 151 ? 22.164 26.507 31.384 1.00 31.76 ? 144 PHE A O 1 ATOM 761 C CB . PHE A 1 151 ? 19.094 25.645 32.201 1.00 31.89 ? 144 PHE A CB 1 ATOM 762 C CG . PHE A 1 151 ? 19.687 24.308 31.827 1.00 34.05 ? 144 PHE A CG 1 ATOM 763 C CD1 . PHE A 1 151 ? 20.621 23.689 32.656 1.00 36.24 ? 144 PHE A CD1 1 ATOM 764 C CD2 . PHE A 1 151 ? 19.324 23.680 30.641 1.00 36.72 ? 144 PHE A CD2 1 ATOM 765 C CE1 . PHE A 1 151 ? 21.170 22.479 32.325 1.00 38.44 ? 144 PHE A CE1 1 ATOM 766 C CE2 . PHE A 1 151 ? 19.870 22.463 30.289 1.00 40.48 ? 144 PHE A CE2 1 ATOM 767 C CZ . PHE A 1 151 ? 20.799 21.851 31.128 1.00 40.07 ? 144 PHE A CZ 1 ATOM 768 N N . GLU A 1 152 ? 21.439 27.418 33.311 1.00 29.30 ? 145 GLU A N 1 ATOM 769 C CA . GLU A 1 152 ? 22.770 27.367 33.978 1.00 28.94 ? 145 GLU A CA 1 ATOM 770 C C . GLU A 1 152 ? 23.004 25.967 34.546 1.00 29.17 ? 145 GLU A C 1 ATOM 771 O O . GLU A 1 152 ? 22.087 25.400 35.157 1.00 29.08 ? 145 GLU A O 1 ATOM 772 C CB . GLU A 1 152 ? 22.853 28.347 35.165 1.00 27.80 ? 145 GLU A CB 1 ATOM 773 C CG . GLU A 1 152 ? 22.497 29.808 34.862 1.00 26.85 ? 145 GLU A CG 1 ATOM 774 C CD . GLU A 1 152 ? 22.460 30.660 36.152 1.00 28.96 ? 145 GLU A CD 1 ATOM 775 O OE1 . GLU A 1 152 ? 21.361 30.747 36.715 1.00 27.85 ? 145 GLU A OE1 1 ATOM 776 O OE2 . GLU A 1 152 ? 23.519 31.202 36.589 1.00 26.69 ? 145 GLU A OE2 1 ATOM 777 N N . PRO A 1 153 ? 24.233 25.431 34.419 1.00 30.52 ? 146 PRO A N 1 ATOM 778 C CA . PRO A 1 153 ? 24.521 24.147 35.071 1.00 30.96 ? 146 PRO A CA 1 ATOM 779 C C . PRO A 1 153 ? 24.229 24.274 36.568 1.00 30.33 ? 146 PRO A C 1 ATOM 780 O O . PRO A 1 153 ? 24.783 25.163 37.244 1.00 30.90 ? 146 PRO A O 1 ATOM 781 C CB . PRO A 1 153 ? 26.016 23.955 34.809 1.00 32.92 ? 146 PRO A CB 1 ATOM 782 C CG . PRO A 1 153 ? 26.258 24.703 33.497 1.00 33.68 ? 146 PRO A CG 1 ATOM 783 C CD . PRO A 1 153 ? 25.387 25.925 33.645 1.00 31.32 ? 146 PRO A CD 1 ATOM 784 N N . PRO A 1 154 ? 23.307 23.466 37.086 1.00 30.35 ? 147 PRO A N 1 ATOM 785 C CA . PRO A 1 154 ? 22.993 23.704 38.481 1.00 29.78 ? 147 PRO A CA 1 ATOM 786 C C . PRO A 1 154 ? 24.151 23.328 39.431 1.00 30.88 ? 147 PRO A C 1 ATOM 787 O O . PRO A 1 154 ? 24.954 22.438 39.098 1.00 31.31 ? 147 PRO A O 1 ATOM 788 C CB . PRO A 1 154 ? 21.772 22.826 38.721 1.00 30.74 ? 147 PRO A CB 1 ATOM 789 C CG . PRO A 1 154 ? 21.809 21.811 37.661 1.00 31.67 ? 147 PRO A CG 1 ATOM 790 C CD . PRO A 1 154 ? 22.412 22.477 36.471 1.00 31.35 ? 147 PRO A CD 1 ATOM 791 N N . PRO A 1 155 ? 24.218 24.005 40.598 1.00 30.50 ? 148 PRO A N 1 ATOM 792 C CA . PRO A 1 155 ? 25.312 23.800 41.537 1.00 31.75 ? 148 PRO A CA 1 ATOM 793 C C . PRO A 1 155 ? 25.251 22.400 42.201 1.00 31.28 ? 148 PRO A C 1 ATOM 794 O O . PRO A 1 155 ? 24.171 21.781 42.252 1.00 30.97 ? 148 PRO A O 1 ATOM 795 C CB . PRO A 1 155 ? 25.110 24.932 42.568 1.00 30.00 ? 148 PRO A CB 1 ATOM 796 C CG . PRO A 1 155 ? 23.679 25.329 42.477 1.00 30.91 ? 148 PRO A CG 1 ATOM 797 C CD . PRO A 1 155 ? 23.239 25.004 41.063 1.00 30.92 ? 148 PRO A CD 1 ATOM 798 N N . PRO A 1 156 ? 26.391 21.914 42.736 1.00 32.51 ? 149 PRO A N 1 ATOM 799 C CA . PRO A 1 156 ? 26.473 20.598 43.374 1.00 32.09 ? 149 PRO A CA 1 ATOM 800 C C . PRO A 1 156 ? 25.368 20.313 44.414 1.00 32.95 ? 149 PRO A C 1 ATOM 801 O O . PRO A 1 156 ? 25.177 21.105 45.362 1.00 31.43 ? 149 PRO A O 1 ATOM 802 C CB . PRO A 1 156 ? 27.826 20.665 44.085 1.00 33.07 ? 149 PRO A CB 1 ATOM 803 C CG . PRO A 1 156 ? 28.663 21.541 43.202 1.00 32.72 ? 149 PRO A CG 1 ATOM 804 C CD . PRO A 1 156 ? 27.700 22.605 42.733 1.00 32.65 ? 149 PRO A CD 1 ATOM 805 N N . GLY A 1 157 ? 24.654 19.200 44.248 1.00 33.21 ? 150 GLY A N 1 ATOM 806 C CA . GLY A 1 157 ? 23.619 18.849 45.210 1.00 35.74 ? 150 GLY A CA 1 ATOM 807 C C . GLY A 1 157 ? 22.238 19.431 44.918 1.00 36.54 ? 150 GLY A C 1 ATOM 808 O O . GLY A 1 157 ? 21.270 19.046 45.581 1.00 37.88 ? 150 GLY A O 1 ATOM 809 N N . TYR A 1 158 ? 22.164 20.332 43.933 1.00 36.58 ? 151 TYR A N 1 ATOM 810 C CA . TYR A 1 158 ? 20.913 20.982 43.482 1.00 37.56 ? 151 TYR A CA 1 ATOM 811 C C . TYR A 1 158 ? 20.547 20.612 42.048 1.00 40.40 ? 151 TYR A C 1 ATOM 812 O O . TYR A 1 158 ? 19.649 21.239 41.452 1.00 40.72 ? 151 TYR A O 1 ATOM 813 C CB . TYR A 1 158 ? 21.090 22.488 43.448 1.00 35.46 ? 151 TYR A CB 1 ATOM 814 C CG . TYR A 1 158 ? 21.336 23.163 44.769 1.00 32.66 ? 151 TYR A CG 1 ATOM 815 C CD1 . TYR A 1 158 ? 20.281 23.723 45.480 1.00 31.99 ? 151 TYR A CD1 1 ATOM 816 C CD2 . TYR A 1 158 ? 22.618 23.266 45.298 1.00 29.79 ? 151 TYR A CD2 1 ATOM 817 C CE1 . TYR A 1 158 ? 20.477 24.366 46.667 1.00 29.54 ? 151 TYR A CE1 1 ATOM 818 C CE2 . TYR A 1 158 ? 22.834 23.915 46.507 1.00 28.02 ? 151 TYR A CE2 1 ATOM 819 C CZ . TYR A 1 158 ? 21.740 24.462 47.184 1.00 29.39 ? 151 TYR A CZ 1 ATOM 820 O OH . TYR A 1 158 ? 21.926 25.096 48.370 1.00 28.51 ? 151 TYR A OH 1 ATOM 821 N N . GLU A 1 159 ? 21.271 19.668 41.459 1.00 42.85 ? 152 GLU A N 1 ATOM 822 C CA . GLU A 1 159 ? 21.029 19.280 40.073 1.00 45.78 ? 152 GLU A CA 1 ATOM 823 C C . GLU A 1 159 ? 19.643 18.592 39.896 1.00 47.43 ? 152 GLU A C 1 ATOM 824 O O . GLU A 1 159 ? 19.207 18.395 38.767 1.00 48.79 ? 152 GLU A O 1 ATOM 825 C CB . GLU A 1 159 ? 22.190 18.435 39.471 1.00 46.93 ? 152 GLU A CB 1 ATOM 826 C CG . GLU A 1 159 ? 23.647 18.964 39.771 1.00 48.97 ? 152 GLU A CG 1 ATOM 827 C CD . GLU A 1 159 ? 24.270 18.384 41.065 1.00 49.30 ? 152 GLU A CD 1 ATOM 828 O OE1 . GLU A 1 159 ? 23.524 17.945 41.948 1.00 46.54 ? 152 GLU A OE1 1 ATOM 829 O OE2 . GLU A 1 159 ? 25.513 18.368 41.194 1.00 49.26 ? 152 GLU A OE2 1 ATOM 830 N N . ASN A 1 160 ? 18.951 18.266 41.001 1.00 48.30 ? 153 ASN A N 1 ATOM 831 C CA . ASN A 1 160 ? 17.590 17.677 40.958 1.00 48.67 ? 153 ASN A CA 1 ATOM 832 C C . ASN A 1 160 ? 16.519 18.612 41.565 1.00 48.05 ? 153 ASN A C 1 ATOM 833 O O . ASN A 1 160 ? 15.390 18.217 41.824 1.00 47.88 ? 153 ASN A O 1 ATOM 834 C CB . ASN A 1 160 ? 17.569 16.305 41.649 1.00 49.75 ? 153 ASN A CB 1 ATOM 835 C CG . ASN A 1 160 ? 16.297 15.519 41.370 1.00 50.88 ? 153 ASN A CG 1 ATOM 836 O OD1 . ASN A 1 160 ? 16.028 15.115 40.236 1.00 53.65 ? 153 ASN A OD1 1 ATOM 837 N ND2 . ASN A 1 160 ? 15.517 15.285 42.414 1.00 51.61 ? 153 ASN A ND2 1 ATOM 838 N N . VAL A 1 161 ? 16.879 19.861 41.805 1.00 47.53 ? 154 VAL A N 1 ATOM 839 C CA . VAL A 1 161 ? 15.871 20.809 42.225 1.00 46.38 ? 154 VAL A CA 1 ATOM 840 C C . VAL A 1 161 ? 14.997 21.160 40.996 1.00 46.56 ? 154 VAL A C 1 ATOM 841 O O . VAL A 1 161 ? 15.490 21.418 39.893 1.00 46.93 ? 154 VAL A O 1 ATOM 842 C CB . VAL A 1 161 ? 16.488 22.039 42.948 1.00 46.10 ? 154 VAL A CB 1 ATOM 843 C CG1 . VAL A 1 161 ? 15.396 23.066 43.340 1.00 44.37 ? 154 VAL A CG1 1 ATOM 844 C CG2 . VAL A 1 161 ? 17.237 21.568 44.196 1.00 47.19 ? 154 VAL A CG2 1 ATOM 845 N N . SER A 1 162 ? 13.690 21.098 41.179 1.00 46.30 ? 155 SER A N 1 ATOM 846 C CA . SER A 1 162 ? 12.803 21.523 40.110 1.00 46.47 ? 155 SER A CA 1 ATOM 847 C C . SER A 1 162 ? 12.399 23.018 40.262 1.00 44.31 ? 155 SER A C 1 ATOM 848 O O . SER A 1 162 ? 12.594 23.675 41.336 1.00 43.33 ? 155 SER A O 1 ATOM 849 C CB . SER A 1 162 ? 11.573 20.580 39.992 1.00 48.19 ? 155 SER A CB 1 ATOM 850 O OG . SER A 1 162 ? 10.847 20.554 41.219 1.00 51.33 ? 155 SER A OG 1 ATOM 851 N N . ASP A 1 163 ? 11.870 23.559 39.171 1.00 41.75 ? 156 ASP A N 1 ATOM 852 C CA . ASP A 1 163 ? 11.331 24.893 39.199 1.00 38.80 ? 156 ASP A CA 1 ATOM 853 C C . ASP A 1 163 ? 12.434 25.925 39.373 1.00 35.21 ? 156 ASP A C 1 ATOM 854 O O . ASP A 1 163 ? 12.199 26.952 39.981 1.00 34.11 ? 156 ASP A O 1 ATOM 855 C CB . ASP A 1 163 ? 10.265 25.033 40.315 1.00 40.46 ? 156 ASP A CB 1 ATOM 856 C CG . ASP A 1 163 ? 9.063 24.095 40.107 1.00 46.34 ? 156 ASP A CG 1 ATOM 857 O OD1 . ASP A 1 163 ? 8.734 23.790 38.933 1.00 52.00 ? 156 ASP A OD1 1 ATOM 858 O OD2 . ASP A 1 163 ? 8.454 23.650 41.111 1.00 51.64 ? 156 ASP A OD2 1 ATOM 859 N N . ILE A 1 164 ? 13.637 25.648 38.862 1.00 32.47 ? 157 ILE A N 1 ATOM 860 C CA . ILE A 1 164 ? 14.634 26.714 38.735 1.00 29.43 ? 157 ILE A CA 1 ATOM 861 C C . ILE A 1 164 ? 14.285 27.446 37.447 1.00 28.34 ? 157 ILE A C 1 ATOM 862 O O . ILE A 1 164 ? 14.332 26.857 36.354 1.00 28.88 ? 157 ILE A O 1 ATOM 863 C CB . ILE A 1 164 ? 16.087 26.172 38.690 1.00 29.20 ? 157 ILE A CB 1 ATOM 864 C CG1 . ILE A 1 164 ? 16.483 25.595 40.051 1.00 28.19 ? 157 ILE A CG1 1 ATOM 865 C CG2 . ILE A 1 164 ? 17.083 27.298 38.326 1.00 27.49 ? 157 ILE A CG2 1 ATOM 866 C CD1 . ILE A 1 164 ? 17.795 24.741 40.021 1.00 25.54 ? 157 ILE A CD1 1 ATOM 867 N N . VAL A 1 165 ? 13.863 28.694 37.563 1.00 26.21 ? 158 VAL A N 1 ATOM 868 C CA . VAL A 1 165 ? 13.547 29.461 36.376 1.00 25.21 ? 158 VAL A CA 1 ATOM 869 C C . VAL A 1 165 ? 14.830 29.683 35.571 1.00 24.94 ? 158 VAL A C 1 ATOM 870 O O . VAL A 1 165 ? 15.805 30.158 36.119 1.00 24.67 ? 158 VAL A O 1 ATOM 871 C CB . VAL A 1 165 ? 12.805 30.826 36.706 1.00 24.25 ? 158 VAL A CB 1 ATOM 872 C CG1 . VAL A 1 165 ? 13.807 31.957 37.232 1.00 22.89 ? 158 VAL A CG1 1 ATOM 873 C CG2 . VAL A 1 165 ? 12.072 31.295 35.473 1.00 25.63 ? 158 VAL A CG2 1 ATOM 874 N N . PRO A 1 166 ? 14.825 29.335 34.265 1.00 25.17 ? 159 PRO A N 1 ATOM 875 C CA . PRO A 1 166 ? 16.042 29.580 33.458 1.00 26.11 ? 159 PRO A CA 1 ATOM 876 C C . PRO A 1 166 ? 16.316 31.074 33.337 1.00 26.14 ? 159 PRO A C 1 ATOM 877 O O . PRO A 1 166 ? 15.391 31.874 33.514 1.00 24.95 ? 159 PRO A O 1 ATOM 878 C CB . PRO A 1 166 ? 15.706 28.987 32.054 1.00 26.82 ? 159 PRO A CB 1 ATOM 879 C CG . PRO A 1 166 ? 14.247 28.853 32.029 1.00 26.79 ? 159 PRO A CG 1 ATOM 880 C CD . PRO A 1 166 ? 13.743 28.711 33.475 1.00 25.49 ? 159 PRO A CD 1 ATOM 881 N N . PRO A 1 167 ? 17.565 31.451 32.990 1.00 25.45 ? 160 PRO A N 1 ATOM 882 C CA . PRO A 1 167 ? 17.830 32.879 32.805 1.00 25.47 ? 160 PRO A CA 1 ATOM 883 C C . PRO A 1 167 ? 16.889 33.511 31.764 1.00 24.60 ? 160 PRO A C 1 ATOM 884 O O . PRO A 1 167 ? 16.626 32.940 30.699 1.00 24.82 ? 160 PRO A O 1 ATOM 885 C CB . PRO A 1 167 ? 19.272 32.903 32.293 1.00 25.67 ? 160 PRO A CB 1 ATOM 886 C CG . PRO A 1 167 ? 19.884 31.597 32.893 1.00 26.66 ? 160 PRO A CG 1 ATOM 887 C CD . PRO A 1 167 ? 18.758 30.616 32.742 1.00 26.15 ? 160 PRO A CD 1 ATOM 888 N N . PHE A 1 168 ? 16.408 34.686 32.090 1.00 24.23 ? 161 PHE A N 1 ATOM 889 C CA . PHE A 1 168 ? 15.581 35.460 31.171 1.00 24.30 ? 161 PHE A CA 1 ATOM 890 C C . PHE A 1 168 ? 15.512 36.887 31.669 1.00 22.88 ? 161 PHE A C 1 ATOM 891 O O . PHE A 1 168 ? 15.869 37.172 32.818 1.00 21.68 ? 161 PHE A O 1 ATOM 892 C CB . PHE A 1 168 ? 14.166 34.872 31.074 1.00 23.80 ? 161 PHE A CB 1 ATOM 893 C CG . PHE A 1 168 ? 13.256 35.214 32.258 1.00 25.20 ? 161 PHE A CG 1 ATOM 894 C CD1 . PHE A 1 168 ? 12.101 35.981 32.053 1.00 22.77 ? 161 PHE A CD1 1 ATOM 895 C CD2 . PHE A 1 168 ? 13.496 34.699 33.547 1.00 23.88 ? 161 PHE A CD2 1 ATOM 896 C CE1 . PHE A 1 168 ? 11.228 36.276 33.092 1.00 20.45 ? 161 PHE A CE1 1 ATOM 897 C CE2 . PHE A 1 168 ? 12.627 34.991 34.611 1.00 23.74 ? 161 PHE A CE2 1 ATOM 898 C CZ . PHE A 1 168 ? 11.470 35.783 34.387 1.00 22.45 ? 161 PHE A CZ 1 ATOM 899 N N . SER A 1 169 ? 15.117 37.787 30.762 1.00 22.77 ? 162 SER A N 1 ATOM 900 C CA . SER A 1 169 ? 14.888 39.172 31.125 1.00 21.23 ? 162 SER A CA 1 ATOM 901 C C . SER A 1 169 ? 13.417 39.366 31.352 1.00 21.82 ? 162 SER A C 1 ATOM 902 O O . SER A 1 169 ? 12.637 39.323 30.410 1.00 22.65 ? 162 SER A O 1 ATOM 903 C CB . SER A 1 169 ? 15.399 40.115 30.023 1.00 23.83 ? 162 SER A CB 1 ATOM 904 O OG . SER A 1 169 ? 16.813 39.955 29.879 1.00 22.64 ? 162 SER A OG 1 ATOM 905 N N . ALA A 1 170 ? 13.037 39.626 32.604 1.00 20.25 ? 163 ALA A N 1 ATOM 906 C CA . ALA A 1 170 ? 11.598 39.720 32.912 1.00 20.61 ? 163 ALA A CA 1 ATOM 907 C C . ALA A 1 170 ? 11.001 40.941 32.224 1.00 21.37 ? 163 ALA A C 1 ATOM 908 O O . ALA A 1 170 ? 11.588 42.025 32.250 1.00 20.27 ? 163 ALA A O 1 ATOM 909 C CB . ALA A 1 170 ? 11.348 39.768 34.405 1.00 19.80 ? 163 ALA A CB 1 ATOM 910 N N . PHE A 1 171 ? 9.848 40.699 31.608 1.00 21.79 ? 164 PHE A N 1 ATOM 911 C CA . PHE A 1 171 ? 9.014 41.664 30.855 1.00 22.82 ? 164 PHE A CA 1 ATOM 912 C C . PHE A 1 171 ? 9.488 41.892 29.416 1.00 23.24 ? 164 PHE A C 1 ATOM 913 O O . PHE A 1 171 ? 8.874 42.696 28.703 1.00 23.51 ? 164 PHE A O 1 ATOM 914 C CB . PHE A 1 171 ? 8.821 42.982 31.601 1.00 21.24 ? 164 PHE A CB 1 ATOM 915 C CG . PHE A 1 171 ? 8.165 42.806 32.942 1.00 23.72 ? 164 PHE A CG 1 ATOM 916 C CD1 . PHE A 1 171 ? 6.770 42.589 33.020 1.00 20.72 ? 164 PHE A CD1 1 ATOM 917 C CD2 . PHE A 1 171 ? 8.937 42.792 34.098 1.00 20.49 ? 164 PHE A CD2 1 ATOM 918 C CE1 . PHE A 1 171 ? 6.124 42.430 34.249 1.00 21.65 ? 164 PHE A CE1 1 ATOM 919 C CE2 . PHE A 1 171 ? 8.335 42.612 35.329 1.00 20.67 ? 164 PHE A CE2 1 ATOM 920 C CZ . PHE A 1 171 ? 6.914 42.434 35.423 1.00 20.62 ? 164 PHE A CZ 1 ATOM 921 N N . SER A 1 172 ? 10.521 41.177 28.949 1.00 24.46 ? 165 SER A N 1 ATOM 922 C CA . SER A 1 172 ? 10.783 41.196 27.501 1.00 25.81 ? 165 SER A CA 1 ATOM 923 C C . SER A 1 172 ? 9.514 40.840 26.680 1.00 26.50 ? 165 SER A C 1 ATOM 924 O O . SER A 1 172 ? 8.757 39.912 27.041 1.00 26.43 ? 165 SER A O 1 ATOM 925 C CB . SER A 1 172 ? 11.899 40.213 27.094 1.00 26.36 ? 165 SER A CB 1 ATOM 926 O OG . SER A 1 172 ? 12.078 40.206 25.672 1.00 27.54 ? 165 SER A OG 1 ATOM 927 N N . PRO A 1 173 ? 9.268 41.581 25.576 1.00 26.96 ? 166 PRO A N 1 ATOM 928 C CA . PRO A 1 173 ? 8.264 41.096 24.653 1.00 28.03 ? 166 PRO A CA 1 ATOM 929 C C . PRO A 1 173 ? 8.759 39.863 23.901 1.00 29.59 ? 166 PRO A C 1 ATOM 930 O O . PRO A 1 173 ? 9.983 39.564 23.842 1.00 28.58 ? 166 PRO A O 1 ATOM 931 C CB . PRO A 1 173 ? 8.094 42.279 23.673 1.00 29.73 ? 166 PRO A CB 1 ATOM 932 C CG . PRO A 1 173 ? 9.453 42.895 23.628 1.00 28.30 ? 166 PRO A CG 1 ATOM 933 C CD . PRO A 1 173 ? 9.865 42.841 25.099 1.00 26.76 ? 166 PRO A CD 1 ATOM 934 N N . GLN A 1 174 ? 7.807 39.152 23.311 1.00 29.83 ? 167 GLN A N 1 ATOM 935 C CA . GLN A 1 174 ? 8.130 38.067 22.377 1.00 31.71 ? 167 GLN A CA 1 ATOM 936 C C . GLN A 1 174 ? 8.674 38.585 21.060 1.00 32.77 ? 167 GLN A C 1 ATOM 937 O O . GLN A 1 174 ? 8.339 39.686 20.639 1.00 33.94 ? 167 GLN A O 1 ATOM 938 C CB . GLN A 1 174 ? 6.885 37.238 22.110 1.00 32.27 ? 167 GLN A CB 1 ATOM 939 C CG . GLN A 1 174 ? 6.299 36.642 23.425 1.00 34.31 ? 167 GLN A CG 1 ATOM 940 C CD . GLN A 1 174 ? 4.992 35.891 23.215 1.00 41.30 ? 167 GLN A CD 1 ATOM 941 O OE1 . GLN A 1 174 ? 4.448 35.892 22.127 1.00 44.97 ? 167 GLN A OE1 1 ATOM 942 N NE2 . GLN A 1 174 ? 4.495 35.241 24.262 1.00 42.24 ? 167 GLN A NE2 1 ATOM 943 N N . GLY A 1 175 ? 9.511 37.790 20.408 1.00 34.11 ? 168 GLY A N 1 ATOM 944 C CA . GLY A 1 175 ? 9.923 38.096 19.047 1.00 35.05 ? 168 GLY A CA 1 ATOM 945 C C . GLY A 1 175 ? 11.016 37.154 18.629 1.00 36.31 ? 168 GLY A C 1 ATOM 946 O O . GLY A 1 175 ? 11.589 36.433 19.473 1.00 36.39 ? 168 GLY A O 1 ATOM 947 N N . MET A 1 176 ? 11.286 37.133 17.319 1.00 37.50 ? 169 MET A N 1 ATOM 948 C CA . MET A 1 176 ? 12.408 36.389 16.800 1.00 38.21 ? 169 MET A CA 1 ATOM 949 C C . MET A 1 176 ? 13.280 37.243 15.872 1.00 38.72 ? 169 MET A C 1 ATOM 950 O O . MET A 1 176 ? 13.585 36.826 14.729 1.00 40.01 ? 169 MET A O 1 ATOM 951 C CB . MET A 1 176 ? 11.910 35.108 16.119 1.00 40.28 ? 169 MET A CB 1 ATOM 952 C CG . MET A 1 176 ? 11.466 34.027 17.116 1.00 44.43 ? 169 MET A CG 1 ATOM 953 S SD . MET A 1 176 ? 10.878 32.540 16.248 1.00 61.48 ? 169 MET A SD 1 ATOM 954 C CE . MET A 1 176 ? 11.238 31.264 17.455 1.00 56.94 ? 169 MET A CE 1 ATOM 955 N N . PRO A 1 177 ? 13.714 38.424 16.334 1.00 37.65 ? 170 PRO A N 1 ATOM 956 C CA . PRO A 1 177 ? 14.469 39.296 15.441 1.00 38.61 ? 170 PRO A CA 1 ATOM 957 C C . PRO A 1 177 ? 15.835 38.688 15.023 1.00 40.27 ? 170 PRO A C 1 ATOM 958 O O . PRO A 1 177 ? 16.482 38.011 15.825 1.00 39.08 ? 170 PRO A O 1 ATOM 959 C CB . PRO A 1 177 ? 14.643 40.573 16.264 1.00 37.69 ? 170 PRO A CB 1 ATOM 960 C CG . PRO A 1 177 ? 14.685 40.076 17.692 1.00 36.04 ? 170 PRO A CG 1 ATOM 961 C CD . PRO A 1 177 ? 13.679 38.952 17.717 1.00 36.46 ? 170 PRO A CD 1 ATOM 962 N N . GLU A 1 178 ? 16.216 38.953 13.769 1.00 41.56 ? 171 GLU A N 1 ATOM 963 C CA . GLU A 1 178 ? 17.450 38.490 13.109 1.00 43.19 ? 171 GLU A CA 1 ATOM 964 C C . GLU A 1 178 ? 18.166 39.722 12.610 1.00 43.81 ? 171 GLU A C 1 ATOM 965 O O . GLU A 1 178 ? 17.521 40.601 12.013 1.00 45.06 ? 171 GLU A O 1 ATOM 966 C CB . GLU A 1 178 ? 17.104 37.687 11.858 1.00 44.49 ? 171 GLU A CB 1 ATOM 967 C CG A GLU A 1 178 ? 16.941 36.220 12.027 0.50 44.58 ? 171 GLU A CG 1 ATOM 968 C CD A GLU A 1 178 ? 16.658 35.553 10.703 0.50 45.65 ? 171 GLU A CD 1 ATOM 969 O OE1 A GLU A 1 178 ? 15.624 34.858 10.612 0.50 47.55 ? 171 GLU A OE1 1 ATOM 970 O OE2 A GLU A 1 178 ? 17.452 35.752 9.757 0.50 44.56 ? 171 GLU A OE2 1 ATOM 971 N N . GLY A 1 179 ? 19.473 39.817 12.831 1.00 43.22 ? 172 GLY A N 1 ATOM 972 C CA . GLY A 1 179 ? 20.186 41.025 12.411 1.00 43.32 ? 172 GLY A CA 1 ATOM 973 C C . GLY A 1 179 ? 21.669 40.983 12.688 1.00 42.94 ? 172 GLY A C 1 ATOM 974 O O . GLY A 1 179 ? 22.181 39.962 13.127 1.00 42.92 ? 172 GLY A O 1 ATOM 975 N N . ASP A 1 180 ? 22.348 42.102 12.451 1.00 42.67 ? 173 ASP A N 1 ATOM 976 C CA . ASP A 1 180 ? 23.801 42.210 12.710 1.00 42.90 ? 173 ASP A CA 1 ATOM 977 C C . ASP A 1 180 ? 24.026 42.803 14.094 1.00 40.89 ? 173 ASP A C 1 ATOM 978 O O . ASP A 1 180 ? 23.255 43.680 14.541 1.00 40.28 ? 173 ASP A O 1 ATOM 979 C CB . ASP A 1 180 ? 24.453 43.142 11.708 1.00 43.80 ? 173 ASP A CB 1 ATOM 980 C CG . ASP A 1 180 ? 24.444 42.588 10.292 1.00 47.20 ? 173 ASP A CG 1 ATOM 981 O OD1 . ASP A 1 180 ? 24.718 41.387 10.124 1.00 48.54 ? 173 ASP A OD1 1 ATOM 982 O OD2 . ASP A 1 180 ? 24.169 43.372 9.356 1.00 48.30 ? 173 ASP A OD2 1 ATOM 983 N N . LEU A 1 181 ? 25.093 42.347 14.754 1.00 39.69 ? 174 LEU A N 1 ATOM 984 C CA . LEU A 1 181 ? 25.409 42.800 16.096 1.00 38.54 ? 174 LEU A CA 1 ATOM 985 C C . LEU A 1 181 ? 26.127 44.139 16.098 1.00 39.04 ? 174 LEU A C 1 ATOM 986 O O . LEU A 1 181 ? 26.953 44.404 15.221 1.00 39.83 ? 174 LEU A O 1 ATOM 987 C CB . LEU A 1 181 ? 26.294 41.763 16.779 1.00 38.50 ? 174 LEU A CB 1 ATOM 988 C CG A LEU A 1 181 ? 26.157 41.233 18.209 0.50 36.48 ? 174 LEU A CG 1 ATOM 989 C CG B LEU A 1 181 ? 25.698 40.434 17.228 0.50 35.85 ? 174 LEU A CG 1 ATOM 990 C CD1 A LEU A 1 181 ? 24.716 41.091 18.687 0.50 34.52 ? 174 LEU A CD1 1 ATOM 991 C CD1 B LEU A 1 181 ? 26.785 39.627 17.918 0.50 32.66 ? 174 LEU A CD1 1 ATOM 992 C CD2 A LEU A 1 181 ? 26.893 39.890 18.278 0.50 34.39 ? 174 LEU A CD2 1 ATOM 993 C CD2 B LEU A 1 181 ? 24.512 40.642 18.150 0.50 33.91 ? 174 LEU A CD2 1 ATOM 994 N N . VAL A 1 182 ? 25.786 44.982 17.090 1.00 38.06 ? 175 VAL A N 1 ATOM 995 C CA . VAL A 1 182 ? 26.647 46.088 17.467 1.00 37.69 ? 175 VAL A CA 1 ATOM 996 C C . VAL A 1 182 ? 26.921 46.001 18.980 1.00 36.80 ? 175 VAL A C 1 ATOM 997 O O . VAL A 1 182 ? 26.004 45.779 19.787 1.00 35.79 ? 175 VAL A O 1 ATOM 998 C CB . VAL A 1 182 ? 26.048 47.476 17.085 1.00 38.67 ? 175 VAL A CB 1 ATOM 999 C CG1 . VAL A 1 182 ? 26.801 48.613 17.772 1.00 36.43 ? 175 VAL A CG1 1 ATOM 1000 C CG2 . VAL A 1 182 ? 26.093 47.665 15.590 1.00 38.12 ? 175 VAL A CG2 1 ATOM 1001 N N . TYR A 1 183 ? 28.190 46.171 19.337 1.00 36.68 ? 176 TYR A N 1 ATOM 1002 C CA . TYR A 1 183 ? 28.627 46.084 20.713 1.00 35.36 ? 176 TYR A CA 1 ATOM 1003 C C . TYR A 1 183 ? 28.660 47.499 21.282 1.00 35.01 ? 176 TYR A C 1 ATOM 1004 O O . TYR A 1 183 ? 29.293 48.392 20.719 1.00 35.11 ? 176 TYR A O 1 ATOM 1005 C CB . TYR A 1 183 ? 29.999 45.376 20.808 1.00 36.48 ? 176 TYR A CB 1 ATOM 1006 C CG . TYR A 1 183 ? 30.664 45.530 22.165 1.00 34.23 ? 176 TYR A CG 1 ATOM 1007 C CD1 . TYR A 1 183 ? 30.119 44.940 23.296 1.00 32.24 ? 176 TYR A CD1 1 ATOM 1008 C CD2 . TYR A 1 183 ? 31.858 46.259 22.304 1.00 34.13 ? 176 TYR A CD2 1 ATOM 1009 C CE1 . TYR A 1 183 ? 30.729 45.121 24.583 1.00 33.73 ? 176 TYR A CE1 1 ATOM 1010 C CE2 . TYR A 1 183 ? 32.479 46.420 23.550 1.00 33.68 ? 176 TYR A CE2 1 ATOM 1011 C CZ . TYR A 1 183 ? 31.910 45.855 24.683 1.00 33.84 ? 176 TYR A CZ 1 ATOM 1012 O OH . TYR A 1 183 ? 32.522 46.012 25.917 1.00 32.72 ? 176 TYR A OH 1 ATOM 1013 N N . VAL A 1 184 ? 27.968 47.695 22.405 1.00 33.54 ? 177 VAL A N 1 ATOM 1014 C CA . VAL A 1 184 ? 27.695 49.035 22.902 1.00 33.46 ? 177 VAL A CA 1 ATOM 1015 C C . VAL A 1 184 ? 28.286 49.244 24.303 1.00 32.37 ? 177 VAL A C 1 ATOM 1016 O O . VAL A 1 184 ? 27.815 50.102 25.051 1.00 32.13 ? 177 VAL A O 1 ATOM 1017 C CB . VAL A 1 184 ? 26.151 49.335 22.902 1.00 32.71 ? 177 VAL A CB 1 ATOM 1018 C CG1 . VAL A 1 184 ? 25.593 49.168 21.506 1.00 33.59 ? 177 VAL A CG1 1 ATOM 1019 C CG2 . VAL A 1 184 ? 25.407 48.376 23.859 1.00 32.49 ? 177 VAL A CG2 1 ATOM 1020 N N . ASN A 1 185 ? 29.317 48.464 24.646 1.00 32.96 ? 178 ASN A N 1 ATOM 1021 C CA . ASN A 1 185 ? 29.956 48.564 25.962 1.00 32.03 ? 178 ASN A CA 1 ATOM 1022 C C . ASN A 1 185 ? 28.895 48.315 27.057 1.00 30.95 ? 178 ASN A C 1 ATOM 1023 O O . ASN A 1 185 ? 28.214 47.273 27.015 1.00 30.17 ? 178 ASN A O 1 ATOM 1024 C CB . ASN A 1 185 ? 30.705 49.911 26.095 1.00 32.66 ? 178 ASN A CB 1 ATOM 1025 C CG . ASN A 1 185 ? 31.794 49.909 27.193 1.00 34.28 ? 178 ASN A CG 1 ATOM 1026 O OD1 . ASN A 1 185 ? 32.311 48.860 27.586 1.00 34.25 ? 178 ASN A OD1 1 ATOM 1027 N ND2 . ASN A 1 185 ? 32.128 51.107 27.699 1.00 32.89 ? 178 ASN A ND2 1 ATOM 1028 N N . TYR A 1 186 ? 28.739 49.240 28.016 1.00 30.49 ? 179 TYR A N 1 ATOM 1029 C CA . TYR A 1 186 ? 27.733 49.092 29.062 1.00 28.77 ? 179 TYR A CA 1 ATOM 1030 C C . TYR A 1 186 ? 26.358 49.628 28.695 1.00 28.00 ? 179 TYR A C 1 ATOM 1031 O O . TYR A 1 186 ? 25.450 49.688 29.578 1.00 26.90 ? 179 TYR A O 1 ATOM 1032 C CB . TYR A 1 186 ? 28.161 49.788 30.365 1.00 28.78 ? 179 TYR A CB 1 ATOM 1033 C CG . TYR A 1 186 ? 29.415 49.203 30.981 1.00 29.14 ? 179 TYR A CG 1 ATOM 1034 C CD1 . TYR A 1 186 ? 29.352 48.030 31.757 1.00 26.56 ? 179 TYR A CD1 1 ATOM 1035 C CD2 . TYR A 1 186 ? 30.666 49.838 30.818 1.00 29.46 ? 179 TYR A CD2 1 ATOM 1036 C CE1 . TYR A 1 186 ? 30.518 47.501 32.372 1.00 29.81 ? 179 TYR A CE1 1 ATOM 1037 C CE2 . TYR A 1 186 ? 31.823 49.318 31.418 1.00 30.04 ? 179 TYR A CE2 1 ATOM 1038 C CZ . TYR A 1 186 ? 31.741 48.150 32.193 1.00 30.56 ? 179 TYR A CZ 1 ATOM 1039 O OH . TYR A 1 186 ? 32.876 47.629 32.793 1.00 32.57 ? 179 TYR A OH 1 ATOM 1040 N N . ALA A 1 187 ? 26.193 50.057 27.436 1.00 27.77 ? 180 ALA A N 1 ATOM 1041 C CA . ALA A 1 187 ? 24.922 50.657 26.974 1.00 27.84 ? 180 ALA A CA 1 ATOM 1042 C C . ALA A 1 187 ? 24.468 51.854 27.807 1.00 27.81 ? 180 ALA A C 1 ATOM 1043 O O . ALA A 1 187 ? 23.241 52.065 27.993 1.00 27.23 ? 180 ALA A O 1 ATOM 1044 C CB . ALA A 1 187 ? 23.772 49.595 26.904 1.00 26.15 ? 180 ALA A CB 1 ATOM 1045 N N . ARG A 1 188 ? 25.433 52.597 28.355 1.00 27.89 ? 181 ARG A N 1 ATOM 1046 C CA . ARG A 1 188 ? 25.161 53.837 29.096 1.00 26.88 ? 181 ARG A CA 1 ATOM 1047 C C . ARG A 1 188 ? 24.852 54.978 28.102 1.00 27.88 ? 181 ARG A C 1 ATOM 1048 O O . ARG A 1 188 ? 25.160 54.893 26.903 1.00 28.02 ? 181 ARG A O 1 ATOM 1049 C CB . ARG A 1 188 ? 26.356 54.216 29.971 1.00 27.90 ? 181 ARG A CB 1 ATOM 1050 C CG . ARG A 1 188 ? 26.630 53.198 31.105 1.00 25.81 ? 181 ARG A CG 1 ATOM 1051 C CD . ARG A 1 188 ? 27.976 53.436 31.718 1.00 27.79 ? 181 ARG A CD 1 ATOM 1052 N NE . ARG A 1 188 ? 29.040 53.375 30.699 1.00 26.90 ? 181 ARG A NE 1 ATOM 1053 C CZ . ARG A 1 188 ? 30.336 53.571 30.923 1.00 32.23 ? 181 ARG A CZ 1 ATOM 1054 N NH1 . ARG A 1 188 ? 30.791 53.856 32.140 1.00 32.69 ? 181 ARG A NH1 1 ATOM 1055 N NH2 . ARG A 1 188 ? 31.190 53.492 29.906 1.00 29.49 ? 181 ARG A NH2 1 ATOM 1056 N N . THR A 1 189 ? 24.199 56.019 28.595 1.00 26.91 ? 182 THR A N 1 ATOM 1057 C CA . THR A 1 189 ? 23.983 57.208 27.795 1.00 27.59 ? 182 THR A CA 1 ATOM 1058 C C . THR A 1 189 ? 25.266 57.645 27.074 1.00 28.85 ? 182 THR A C 1 ATOM 1059 O O . THR A 1 189 ? 25.264 57.865 25.858 1.00 28.94 ? 182 THR A O 1 ATOM 1060 C CB . THR A 1 189 ? 23.436 58.350 28.653 1.00 27.79 ? 182 THR A CB 1 ATOM 1061 O OG1 . THR A 1 189 ? 22.186 57.920 29.188 1.00 25.72 ? 182 THR A OG1 1 ATOM 1062 C CG2 . THR A 1 189 ? 23.216 59.624 27.792 1.00 29.03 ? 182 THR A CG2 1 ATOM 1063 N N . GLU A 1 190 ? 26.365 57.755 27.816 1.00 29.71 ? 183 GLU A N 1 ATOM 1064 C CA . GLU A 1 190 ? 27.630 58.183 27.194 1.00 32.15 ? 183 GLU A CA 1 ATOM 1065 C C . GLU A 1 190 ? 28.180 57.173 26.184 1.00 32.71 ? 183 GLU A C 1 ATOM 1066 O O . GLU A 1 190 ? 28.920 57.551 25.249 1.00 33.08 ? 183 GLU A O 1 ATOM 1067 C CB . GLU A 1 190 ? 28.650 58.547 28.277 1.00 32.92 ? 183 GLU A CB 1 ATOM 1068 C CG . GLU A 1 190 ? 29.034 57.386 29.184 1.00 35.38 ? 183 GLU A CG 1 ATOM 1069 C CD . GLU A 1 190 ? 28.262 57.310 30.504 1.00 38.51 ? 183 GLU A CD 1 ATOM 1070 O OE1 . GLU A 1 190 ? 27.037 57.664 30.573 1.00 37.54 ? 183 GLU A OE1 1 ATOM 1071 O OE2 . GLU A 1 190 ? 28.909 56.868 31.480 1.00 36.68 ? 183 GLU A OE2 1 ATOM 1072 N N . ASP A 1 191 ? 27.805 55.892 26.319 1.00 31.80 ? 184 ASP A N 1 ATOM 1073 C CA . ASP A 1 191 ? 28.348 54.881 25.354 1.00 32.58 ? 184 ASP A CA 1 ATOM 1074 C C . ASP A 1 191 ? 27.646 55.092 24.015 1.00 32.95 ? 184 ASP A C 1 ATOM 1075 O O . ASP A 1 191 ? 28.248 55.022 22.942 1.00 31.56 ? 184 ASP A O 1 ATOM 1076 C CB . ASP A 1 191 ? 28.103 53.445 25.860 1.00 32.02 ? 184 ASP A CB 1 ATOM 1077 C CG . ASP A 1 191 ? 28.863 53.139 27.126 1.00 31.92 ? 184 ASP A CG 1 ATOM 1078 O OD1 . ASP A 1 191 ? 30.033 53.596 27.220 1.00 32.97 ? 184 ASP A OD1 1 ATOM 1079 O OD2 . ASP A 1 191 ? 28.313 52.425 28.010 1.00 29.18 ? 184 ASP A OD2 1 ATOM 1080 N N . PHE A 1 192 ? 26.344 55.383 24.089 1.00 31.99 ? 185 PHE A N 1 ATOM 1081 C CA . PHE A 1 192 ? 25.571 55.646 22.883 1.00 32.27 ? 185 PHE A CA 1 ATOM 1082 C C . PHE A 1 192 ? 25.932 56.983 22.264 1.00 33.50 ? 185 PHE A C 1 ATOM 1083 O O . PHE A 1 192 ? 25.936 57.092 21.038 1.00 34.14 ? 185 PHE A O 1 ATOM 1084 C CB . PHE A 1 192 ? 24.065 55.527 23.163 1.00 31.25 ? 185 PHE A CB 1 ATOM 1085 C CG . PHE A 1 192 ? 23.593 54.106 23.197 1.00 29.93 ? 185 PHE A CG 1 ATOM 1086 C CD1 . PHE A 1 192 ? 23.308 53.484 24.405 1.00 31.02 ? 185 PHE A CD1 1 ATOM 1087 C CD2 . PHE A 1 192 ? 23.459 53.373 22.010 1.00 31.58 ? 185 PHE A CD2 1 ATOM 1088 C CE1 . PHE A 1 192 ? 22.863 52.140 24.436 1.00 31.90 ? 185 PHE A CE1 1 ATOM 1089 C CE2 . PHE A 1 192 ? 23.059 52.033 22.022 1.00 29.94 ? 185 PHE A CE2 1 ATOM 1090 C CZ . PHE A 1 192 ? 22.747 51.405 23.255 1.00 31.38 ? 185 PHE A CZ 1 ATOM 1091 N N . PHE A 1 193 ? 26.250 57.992 23.090 1.00 34.39 ? 186 PHE A N 1 ATOM 1092 C CA . PHE A 1 193 ? 26.783 59.280 22.556 1.00 36.85 ? 186 PHE A CA 1 ATOM 1093 C C . PHE A 1 193 ? 28.050 59.000 21.738 1.00 38.63 ? 186 PHE A C 1 ATOM 1094 O O . PHE A 1 193 ? 28.237 59.541 20.633 1.00 40.21 ? 186 PHE A O 1 ATOM 1095 C CB . PHE A 1 193 ? 27.146 60.287 23.673 1.00 35.56 ? 186 PHE A CB 1 ATOM 1096 C CG . PHE A 1 193 ? 25.972 61.016 24.282 1.00 35.58 ? 186 PHE A CG 1 ATOM 1097 C CD1 . PHE A 1 193 ? 24.736 61.042 23.666 1.00 35.90 ? 186 PHE A CD1 1 ATOM 1098 C CD2 . PHE A 1 193 ? 26.139 61.725 25.476 1.00 34.64 ? 186 PHE A CD2 1 ATOM 1099 C CE1 . PHE A 1 193 ? 23.657 61.728 24.253 1.00 33.59 ? 186 PHE A CE1 1 ATOM 1100 C CE2 . PHE A 1 193 ? 25.086 62.437 26.062 1.00 32.06 ? 186 PHE A CE2 1 ATOM 1101 C CZ . PHE A 1 193 ? 23.839 62.429 25.444 1.00 31.80 ? 186 PHE A CZ 1 ATOM 1102 N N . LYS A 1 194 ? 28.933 58.172 22.297 1.00 38.91 ? 187 LYS A N 1 ATOM 1103 C CA . LYS A 1 194 ? 30.245 57.865 21.687 1.00 40.22 ? 187 LYS A CA 1 ATOM 1104 C C . LYS A 1 194 ? 30.082 57.147 20.344 1.00 41.58 ? 187 LYS A C 1 ATOM 1105 O O . LYS A 1 194 ? 30.781 57.474 19.365 1.00 43.02 ? 187 LYS A O 1 ATOM 1106 C CB . LYS A 1 194 ? 31.091 57.019 22.655 1.00 39.91 ? 187 LYS A CB 1 ATOM 1107 C CG . LYS A 1 194 ? 32.450 56.432 22.094 1.00 43.33 ? 187 LYS A CG 1 ATOM 1108 C CD . LYS A 1 194 ? 33.552 57.457 21.966 1.00 49.52 ? 187 LYS A CD 1 ATOM 1109 C CE . LYS A 1 194 ? 33.996 57.998 23.334 1.00 51.72 ? 187 LYS A CE 1 ATOM 1110 N NZ . LYS A 1 194 ? 34.987 59.104 23.122 1.00 57.81 ? 187 LYS A NZ 1 ATOM 1111 N N . LEU A 1 195 ? 29.151 56.191 20.303 1.00 41.03 ? 188 LEU A N 1 ATOM 1112 C CA . LEU A 1 195 ? 28.772 55.466 19.095 1.00 42.44 ? 188 LEU A CA 1 ATOM 1113 C C . LEU A 1 195 ? 28.198 56.343 17.998 1.00 43.55 ? 188 LEU A C 1 ATOM 1114 O O . LEU A 1 195 ? 28.713 56.328 16.879 1.00 43.61 ? 188 LEU A O 1 ATOM 1115 C CB . LEU A 1 195 ? 27.739 54.376 19.409 1.00 41.57 ? 188 LEU A CB 1 ATOM 1116 C CG . LEU A 1 195 ? 28.263 53.055 19.927 1.00 42.47 ? 188 LEU A CG 1 ATOM 1117 C CD1 . LEU A 1 195 ? 27.120 52.226 20.469 1.00 43.27 ? 188 LEU A CD1 1 ATOM 1118 C CD2 . LEU A 1 195 ? 29.004 52.299 18.847 1.00 40.80 ? 188 LEU A CD2 1 ATOM 1119 N N . GLU A 1 196 ? 27.131 57.085 18.321 1.00 42.43 ? 189 GLU A N 1 ATOM 1120 C CA A GLU A 1 196 ? 26.393 57.837 17.325 0.50 43.73 ? 189 GLU A CA 1 ATOM 1121 C CA B GLU A 1 196 ? 26.383 57.865 17.315 0.50 43.77 ? 189 GLU A CA 1 ATOM 1122 C C . GLU A 1 196 ? 27.094 59.144 16.926 1.00 44.88 ? 189 GLU A C 1 ATOM 1123 O O . GLU A 1 196 ? 27.209 59.463 15.731 1.00 46.32 ? 189 GLU A O 1 ATOM 1124 C CB A GLU A 1 196 ? 24.967 58.059 17.846 0.50 43.04 ? 189 GLU A CB 1 ATOM 1125 C CB B GLU A 1 196 ? 24.956 58.224 17.783 0.50 43.23 ? 189 GLU A CB 1 ATOM 1126 C CG A GLU A 1 196 ? 24.072 56.831 17.644 0.50 43.22 ? 189 GLU A CG 1 ATOM 1127 C CG B GLU A 1 196 ? 24.243 59.241 16.831 0.50 44.43 ? 189 GLU A CG 1 ATOM 1128 C CD A GLU A 1 196 ? 23.373 56.384 18.901 0.50 43.00 ? 189 GLU A CD 1 ATOM 1129 C CD B GLU A 1 196 ? 22.875 59.688 17.321 0.50 44.99 ? 189 GLU A CD 1 ATOM 1130 O OE1 A GLU A 1 196 ? 24.005 55.664 19.698 0.50 41.50 ? 189 GLU A OE1 1 ATOM 1131 O OE1 B GLU A 1 196 ? 21.982 58.829 17.452 0.50 46.06 ? 189 GLU A OE1 1 ATOM 1132 O OE2 A GLU A 1 196 ? 22.194 56.742 19.089 0.50 43.99 ? 189 GLU A OE2 1 ATOM 1133 O OE2 B GLU A 1 196 ? 22.684 60.897 17.567 0.50 43.20 ? 189 GLU A OE2 1 ATOM 1134 N N . ARG A 1 197 ? 27.564 59.886 17.928 1.00 44.67 ? 190 ARG A N 1 ATOM 1135 C CA . ARG A 1 197 ? 28.131 61.219 17.707 1.00 45.78 ? 190 ARG A CA 1 ATOM 1136 C C . ARG A 1 197 ? 29.577 61.191 17.235 1.00 46.90 ? 190 ARG A C 1 ATOM 1137 O O . ARG A 1 197 ? 29.915 61.891 16.269 1.00 48.60 ? 190 ARG A O 1 ATOM 1138 C CB . ARG A 1 197 ? 27.967 62.122 18.953 1.00 43.52 ? 190 ARG A CB 1 ATOM 1139 C CG . ARG A 1 197 ? 26.510 62.347 19.377 1.00 43.15 ? 190 ARG A CG 1 ATOM 1140 C CD . ARG A 1 197 ? 26.432 63.154 20.678 1.00 38.95 ? 190 ARG A CD 1 ATOM 1141 N NE . ARG A 1 197 ? 25.036 63.416 21.046 1.00 39.19 ? 190 ARG A NE 1 ATOM 1142 C CZ . ARG A 1 197 ? 24.659 64.236 22.026 1.00 37.62 ? 190 ARG A CZ 1 ATOM 1143 N NH1 . ARG A 1 197 ? 25.568 64.851 22.773 1.00 34.99 ? 190 ARG A NH1 1 ATOM 1144 N NH2 . ARG A 1 197 ? 23.368 64.414 22.283 1.00 37.42 ? 190 ARG A NH2 1 ATOM 1145 N N . ASP A 1 198 ? 30.413 60.390 17.908 1.00 47.41 ? 191 ASP A N 1 ATOM 1146 C CA . ASP A 1 198 ? 31.864 60.333 17.628 1.00 49.32 ? 191 ASP A CA 1 ATOM 1147 C C . ASP A 1 198 ? 32.242 59.290 16.578 1.00 50.13 ? 191 ASP A C 1 ATOM 1148 O O . ASP A 1 198 ? 32.966 59.589 15.639 1.00 51.82 ? 191 ASP A O 1 ATOM 1149 C CB . ASP A 1 198 ? 32.676 60.070 18.904 1.00 49.38 ? 191 ASP A CB 1 ATOM 1150 C CG . ASP A 1 198 ? 32.452 61.117 19.978 1.00 51.23 ? 191 ASP A CG 1 ATOM 1151 O OD1 . ASP A 1 198 ? 32.154 62.283 19.630 1.00 54.65 ? 191 ASP A OD1 1 ATOM 1152 O OD2 . ASP A 1 198 ? 32.571 60.777 21.181 1.00 53.97 ? 191 ASP A OD2 1 ATOM 1153 N N . MET A 1 199 ? 31.771 58.061 16.734 1.00 49.00 ? 192 MET A N 1 ATOM 1154 C CA . MET A 1 199 ? 32.148 57.005 15.795 1.00 50.03 ? 192 MET A CA 1 ATOM 1155 C C . MET A 1 199 ? 31.217 56.897 14.582 1.00 50.34 ? 192 MET A C 1 ATOM 1156 O O . MET A 1 199 ? 31.527 56.155 13.656 1.00 50.93 ? 192 MET A O 1 ATOM 1157 C CB . MET A 1 199 ? 32.213 55.645 16.487 1.00 49.17 ? 192 MET A CB 1 ATOM 1158 C CG . MET A 1 199 ? 33.122 55.568 17.684 1.00 49.71 ? 192 MET A CG 1 ATOM 1159 S SD . MET A 1 199 ? 32.937 53.943 18.444 1.00 48.22 ? 192 MET A SD 1 ATOM 1160 C CE . MET A 1 199 ? 34.018 52.988 17.366 1.00 49.51 ? 192 MET A CE 1 ATOM 1161 N N . LYS A 1 200 ? 30.072 57.588 14.611 1.00 49.43 ? 193 LYS A N 1 ATOM 1162 C CA . LYS A 1 200 ? 29.121 57.617 13.485 1.00 50.10 ? 193 LYS A CA 1 ATOM 1163 C C . LYS A 1 200 ? 28.545 56.231 13.194 1.00 49.89 ? 193 LYS A C 1 ATOM 1164 O O . LYS A 1 200 ? 28.346 55.861 12.039 1.00 50.38 ? 193 LYS A O 1 ATOM 1165 C CB . LYS A 1 200 ? 29.786 58.198 12.204 1.00 52.57 ? 193 LYS A CB 1 ATOM 1166 C CG . LYS A 1 200 ? 29.636 59.702 11.947 1.00 55.74 ? 193 LYS A CG 1 ATOM 1167 C CD . LYS A 1 200 ? 29.710 60.588 13.195 1.00 56.09 ? 193 LYS A CD 1 ATOM 1168 C CE . LYS A 1 200 ? 30.006 62.047 12.846 1.00 58.42 ? 193 LYS A CE 1 ATOM 1169 N NZ . LYS A 1 200 ? 29.214 62.996 13.699 1.00 57.29 ? 193 LYS A NZ 1 ATOM 1170 N N . ILE A 1 201 ? 28.282 55.449 14.240 1.00 48.61 ? 194 ILE A N 1 ATOM 1171 C CA . ILE A 1 201 ? 27.752 54.104 14.043 1.00 48.85 ? 194 ILE A CA 1 ATOM 1172 C C . ILE A 1 201 ? 26.251 54.111 14.319 1.00 48.33 ? 194 ILE A C 1 ATOM 1173 O O . ILE A 1 201 ? 25.806 54.698 15.285 1.00 46.98 ? 194 ILE A O 1 ATOM 1174 C CB . ILE A 1 201 ? 28.547 53.054 14.879 1.00 48.74 ? 194 ILE A CB 1 ATOM 1175 C CG1 . ILE A 1 201 ? 29.920 52.823 14.220 1.00 50.96 ? 194 ILE A CG1 1 ATOM 1176 C CG2 . ILE A 1 201 ? 27.800 51.725 14.957 1.00 48.96 ? 194 ILE A CG2 1 ATOM 1177 C CD1 . ILE A 1 201 ? 30.951 52.118 15.079 1.00 51.51 ? 194 ILE A CD1 1 ATOM 1178 N N . ASN A 1 202 ? 25.473 53.485 13.453 1.00 48.86 ? 195 ASN A N 1 ATOM 1179 C CA . ASN A 1 202 ? 24.031 53.606 13.518 1.00 49.04 ? 195 ASN A CA 1 ATOM 1180 C C . ASN A 1 202 ? 23.433 52.303 14.065 1.00 47.46 ? 195 ASN A C 1 ATOM 1181 O O . ASN A 1 202 ? 23.613 51.242 13.459 1.00 46.36 ? 195 ASN A O 1 ATOM 1182 C CB . ASN A 1 202 ? 23.492 53.959 12.120 1.00 51.79 ? 195 ASN A CB 1 ATOM 1183 C CG . ASN A 1 202 ? 22.001 54.255 12.120 1.00 56.20 ? 195 ASN A CG 1 ATOM 1184 O OD1 . ASN A 1 202 ? 21.327 54.097 13.138 1.00 54.69 ? 195 ASN A OD1 1 ATOM 1185 N ND2 . ASN A 1 202 ? 21.477 54.678 10.961 1.00 64.31 ? 195 ASN A ND2 1 ATOM 1186 N N . CYS A 1 203 ? 22.768 52.374 15.230 1.00 44.50 ? 196 CYS A N 1 ATOM 1187 C CA . CYS A 1 203 ? 22.179 51.166 15.814 1.00 44.08 ? 196 CYS A CA 1 ATOM 1188 C C . CYS A 1 203 ? 20.797 50.828 15.281 1.00 43.73 ? 196 CYS A C 1 ATOM 1189 O O . CYS A 1 203 ? 20.224 49.794 15.653 1.00 42.81 ? 196 CYS A O 1 ATOM 1190 C CB . CYS A 1 203 ? 22.108 51.241 17.354 1.00 42.26 ? 196 CYS A CB 1 ATOM 1191 S SG . CYS A 1 203 ? 23.703 51.247 18.129 1.00 43.82 ? 196 CYS A SG 1 ATOM 1192 N N . SER A 1 204 ? 20.245 51.688 14.432 1.00 44.56 ? 197 SER A N 1 ATOM 1193 C CA . SER A 1 204 ? 18.899 51.443 13.927 1.00 44.96 ? 197 SER A CA 1 ATOM 1194 C C . SER A 1 204 ? 18.808 50.077 13.215 1.00 45.32 ? 197 SER A C 1 ATOM 1195 O O . SER A 1 204 ? 19.586 49.788 12.287 1.00 47.54 ? 197 SER A O 1 ATOM 1196 C CB . SER A 1 204 ? 18.428 52.605 13.044 1.00 46.09 ? 197 SER A CB 1 ATOM 1197 O OG . SER A 1 204 ? 17.267 52.253 12.304 1.00 47.38 ? 197 SER A OG 1 ATOM 1198 N N . GLY A 1 205 ? 17.877 49.237 13.672 1.00 43.68 ? 198 GLY A N 1 ATOM 1199 C CA . GLY A 1 205 ? 17.658 47.901 13.112 1.00 43.41 ? 198 GLY A CA 1 ATOM 1200 C C . GLY A 1 205 ? 18.751 46.873 13.407 1.00 43.33 ? 198 GLY A C 1 ATOM 1201 O O . GLY A 1 205 ? 18.768 45.819 12.790 1.00 44.10 ? 198 GLY A O 1 ATOM 1202 N N . LYS A 1 206 ? 19.654 47.165 14.353 1.00 42.33 ? 199 LYS A N 1 ATOM 1203 C CA . LYS A 1 206 ? 20.734 46.232 14.725 1.00 41.62 ? 199 LYS A CA 1 ATOM 1204 C C . LYS A 1 206 ? 20.331 45.520 16.014 1.00 39.95 ? 199 LYS A C 1 ATOM 1205 O O . LYS A 1 206 ? 19.449 45.989 16.732 1.00 38.61 ? 199 LYS A O 1 ATOM 1206 C CB . LYS A 1 206 ? 22.062 46.956 14.994 1.00 41.64 ? 199 LYS A CB 1 ATOM 1207 C CG . LYS A 1 206 ? 22.591 47.845 13.872 1.00 44.80 ? 199 LYS A CG 1 ATOM 1208 C CD . LYS A 1 206 ? 22.849 47.080 12.609 1.00 49.02 ? 199 LYS A CD 1 ATOM 1209 C CE . LYS A 1 206 ? 23.239 48.053 11.523 1.00 52.35 ? 199 LYS A CE 1 ATOM 1210 N NZ . LYS A 1 206 ? 22.445 47.751 10.316 1.00 54.22 ? 199 LYS A NZ 1 ATOM 1211 N N . ILE A 1 207 ? 20.968 44.388 16.299 1.00 40.19 ? 200 ILE A N 1 ATOM 1212 C CA . ILE A 1 207 ? 20.848 43.764 17.623 1.00 39.17 ? 200 ILE A CA 1 ATOM 1213 C C . ILE A 1 207 ? 22.031 44.258 18.422 1.00 38.09 ? 200 ILE A C 1 ATOM 1214 O O . ILE A 1 207 ? 23.184 44.098 18.017 1.00 38.94 ? 200 ILE A O 1 ATOM 1215 C CB . ILE A 1 207 ? 20.835 42.223 17.558 1.00 40.23 ? 200 ILE A CB 1 ATOM 1216 C CG1 . ILE A 1 207 ? 19.572 41.757 16.825 1.00 40.71 ? 200 ILE A CG1 1 ATOM 1217 C CG2 . ILE A 1 207 ? 20.869 41.643 18.974 1.00 38.84 ? 200 ILE A CG2 1 ATOM 1218 C CD1 . ILE A 1 207 ? 19.511 40.274 16.600 1.00 39.39 ? 200 ILE A CD1 1 ATOM 1219 N N . VAL A 1 208 ? 21.746 44.878 19.552 1.00 34.99 ? 201 VAL A N 1 ATOM 1220 C CA . VAL A 1 208 ? 22.812 45.396 20.372 1.00 34.38 ? 201 VAL A CA 1 ATOM 1221 C C . VAL A 1 208 ? 23.250 44.344 21.418 1.00 33.06 ? 201 VAL A C 1 ATOM 1222 O O . VAL A 1 208 ? 22.432 43.655 22.019 1.00 32.56 ? 201 VAL A O 1 ATOM 1223 C CB . VAL A 1 208 ? 22.406 46.788 20.957 1.00 34.82 ? 201 VAL A CB 1 ATOM 1224 C CG1 A VAL A 1 208 ? 22.197 47.817 19.829 0.50 34.70 ? 201 VAL A CG1 1 ATOM 1225 C CG1 B VAL A 1 208 ? 22.644 46.902 22.475 0.50 31.56 ? 201 VAL A CG1 1 ATOM 1226 C CG2 A VAL A 1 208 ? 21.195 46.687 21.818 0.50 31.92 ? 201 VAL A CG2 1 ATOM 1227 C CG2 B VAL A 1 208 ? 23.023 47.929 20.121 0.50 35.29 ? 201 VAL A CG2 1 ATOM 1228 N N . ILE A 1 209 ? 24.550 44.200 21.600 1.00 32.29 ? 202 ILE A N 1 ATOM 1229 C CA . ILE A 1 209 ? 25.050 43.396 22.709 1.00 30.39 ? 202 ILE A CA 1 ATOM 1230 C C . ILE A 1 209 ? 25.784 44.304 23.695 1.00 30.66 ? 202 ILE A C 1 ATOM 1231 O O . ILE A 1 209 ? 26.684 45.092 23.323 1.00 31.82 ? 202 ILE A O 1 ATOM 1232 C CB . ILE A 1 209 ? 25.880 42.183 22.216 1.00 32.22 ? 202 ILE A CB 1 ATOM 1233 C CG1 . ILE A 1 209 ? 26.431 41.350 23.381 1.00 30.15 ? 202 ILE A CG1 1 ATOM 1234 C CG2 . ILE A 1 209 ? 27.046 42.617 21.240 1.00 30.76 ? 202 ILE A CG2 1 ATOM 1235 C CD1 . ILE A 1 209 ? 26.975 39.935 22.873 1.00 32.21 ? 202 ILE A CD1 1 ATOM 1236 N N . ALA A 1 210 ? 25.359 44.235 24.953 1.00 29.56 ? 203 ALA A N 1 ATOM 1237 C CA . ALA A 1 210 ? 25.923 45.094 25.976 1.00 29.71 ? 203 ALA A CA 1 ATOM 1238 C C . ALA A 1 210 ? 26.390 44.250 27.154 1.00 29.97 ? 203 ALA A C 1 ATOM 1239 O O . ALA A 1 210 ? 25.732 43.273 27.529 1.00 28.85 ? 203 ALA A O 1 ATOM 1240 C CB . ALA A 1 210 ? 24.842 46.119 26.466 1.00 28.05 ? 203 ALA A CB 1 ATOM 1241 N N . ARG A 1 211 ? 27.493 44.653 27.779 1.00 30.44 ? 204 ARG A N 1 ATOM 1242 C CA . ARG A 1 211 ? 27.817 44.048 29.059 1.00 29.98 ? 204 ARG A CA 1 ATOM 1243 C C . ARG A 1 211 ? 27.065 44.644 30.228 1.00 28.97 ? 204 ARG A C 1 ATOM 1244 O O . ARG A 1 211 ? 26.811 45.868 30.276 1.00 27.71 ? 204 ARG A O 1 ATOM 1245 C CB . ARG A 1 211 ? 29.308 44.083 29.329 1.00 31.29 ? 204 ARG A CB 1 ATOM 1246 C CG . ARG A 1 211 ? 29.956 45.441 29.144 1.00 32.66 ? 204 ARG A CG 1 ATOM 1247 C CD . ARG A 1 211 ? 31.408 45.277 29.577 1.00 36.12 ? 204 ARG A CD 1 ATOM 1248 N NE . ARG A 1 211 ? 32.251 46.439 29.284 1.00 35.32 ? 204 ARG A NE 1 ATOM 1249 C CZ . ARG A 1 211 ? 33.485 46.586 29.758 1.00 36.42 ? 204 ARG A CZ 1 ATOM 1250 N NH1 . ARG A 1 211 ? 33.991 45.687 30.598 1.00 33.17 ? 204 ARG A NH1 1 ATOM 1251 N NH2 . ARG A 1 211 ? 34.194 47.659 29.418 1.00 36.55 ? 204 ARG A NH2 1 ATOM 1252 N N . TYR A 1 212 ? 26.724 43.769 31.184 1.00 26.86 ? 205 TYR A N 1 ATOM 1253 C CA . TYR A 1 212 ? 26.122 44.176 32.431 1.00 26.06 ? 205 TYR A CA 1 ATOM 1254 C C . TYR A 1 212 ? 27.113 44.996 33.227 1.00 26.25 ? 205 TYR A C 1 ATOM 1255 O O . TYR A 1 212 ? 28.314 44.817 33.047 1.00 25.36 ? 205 TYR A O 1 ATOM 1256 C CB . TYR A 1 212 ? 25.792 42.925 33.235 1.00 25.45 ? 205 TYR A CB 1 ATOM 1257 C CG . TYR A 1 212 ? 24.420 42.313 33.060 1.00 26.88 ? 205 TYR A CG 1 ATOM 1258 C CD1 . TYR A 1 212 ? 24.279 40.941 32.736 1.00 25.71 ? 205 TYR A CD1 1 ATOM 1259 C CD2 . TYR A 1 212 ? 23.274 43.055 33.321 1.00 23.88 ? 205 TYR A CD2 1 ATOM 1260 C CE1 . TYR A 1 212 ? 23.046 40.339 32.670 1.00 25.33 ? 205 TYR A CE1 1 ATOM 1261 C CE2 . TYR A 1 212 ? 22.017 42.468 33.280 1.00 26.09 ? 205 TYR A CE2 1 ATOM 1262 C CZ . TYR A 1 212 ? 21.890 41.114 32.980 1.00 26.97 ? 205 TYR A CZ 1 ATOM 1263 O OH . TYR A 1 212 ? 20.612 40.554 32.950 1.00 22.60 ? 205 TYR A OH 1 ATOM 1264 N N . GLY A 1 213 ? 26.613 45.889 34.102 1.00 25.10 ? 206 GLY A N 1 ATOM 1265 C CA . GLY A 1 213 ? 27.484 46.594 35.064 1.00 25.48 ? 206 GLY A CA 1 ATOM 1266 C C . GLY A 1 213 ? 27.227 48.087 34.985 1.00 25.76 ? 206 GLY A C 1 ATOM 1267 O O . GLY A 1 213 ? 26.607 48.547 33.999 1.00 24.60 ? 206 GLY A O 1 ATOM 1268 N N . LYS A 1 214 ? 27.665 48.824 36.025 1.00 25.16 ? 207 LYS A N 1 ATOM 1269 C CA . LYS A 1 214 ? 27.656 50.314 36.050 1.00 26.16 ? 207 LYS A CA 1 ATOM 1270 C C . LYS A 1 214 ? 26.296 50.950 36.220 1.00 24.93 ? 207 LYS A C 1 ATOM 1271 O O . LYS A 1 214 ? 26.177 51.905 36.999 1.00 25.22 ? 207 LYS A O 1 ATOM 1272 C CB . LYS A 1 214 ? 28.288 50.959 34.811 1.00 27.64 ? 207 LYS A CB 1 ATOM 1273 C CG . LYS A 1 214 ? 29.675 50.395 34.442 1.00 31.27 ? 207 LYS A CG 1 ATOM 1274 C CD . LYS A 1 214 ? 30.744 50.916 35.367 1.00 36.79 ? 207 LYS A CD 1 ATOM 1275 C CE . LYS A 1 214 ? 32.105 50.335 34.966 1.00 38.27 ? 207 LYS A CE 1 ATOM 1276 N NZ . LYS A 1 214 ? 33.043 50.594 36.093 1.00 42.46 ? 207 LYS A NZ 1 ATOM 1277 N N . VAL A 1 215 ? 25.294 50.490 35.453 1.00 24.06 ? 208 VAL A N 1 ATOM 1278 C CA . VAL A 1 215 ? 23.942 51.079 35.590 1.00 22.88 ? 208 VAL A CA 1 ATOM 1279 C C . VAL A 1 215 ? 22.859 50.004 35.586 1.00 22.42 ? 208 VAL A C 1 ATOM 1280 O O . VAL A 1 215 ? 23.080 48.875 35.104 1.00 23.40 ? 208 VAL A O 1 ATOM 1281 C CB . VAL A 1 215 ? 23.636 52.137 34.451 1.00 22.45 ? 208 VAL A CB 1 ATOM 1282 C CG1 . VAL A 1 215 ? 24.683 53.279 34.419 1.00 22.69 ? 208 VAL A CG1 1 ATOM 1283 C CG2 . VAL A 1 215 ? 23.544 51.470 33.052 1.00 24.47 ? 208 VAL A CG2 1 ATOM 1284 N N . PHE A 1 216 ? 21.684 50.368 36.095 1.00 21.31 ? 209 PHE A N 1 ATOM 1285 C CA . PHE A 1 216 ? 20.532 49.473 36.081 1.00 21.47 ? 209 PHE A CA 1 ATOM 1286 C C . PHE A 1 216 ? 20.232 48.963 34.676 1.00 21.09 ? 209 PHE A C 1 ATOM 1287 O O . PHE A 1 216 ? 20.224 49.739 33.682 1.00 22.12 ? 209 PHE A O 1 ATOM 1288 C CB . PHE A 1 216 ? 19.315 50.190 36.656 1.00 19.55 ? 209 PHE A CB 1 ATOM 1289 C CG . PHE A 1 216 ? 18.035 49.402 36.544 1.00 21.38 ? 209 PHE A CG 1 ATOM 1290 C CD1 . PHE A 1 216 ? 17.909 48.186 37.223 1.00 21.71 ? 209 PHE A CD1 1 ATOM 1291 C CD2 . PHE A 1 216 ? 16.899 49.946 35.878 1.00 21.25 ? 209 PHE A CD2 1 ATOM 1292 C CE1 . PHE A 1 216 ? 16.710 47.434 37.154 1.00 21.46 ? 209 PHE A CE1 1 ATOM 1293 C CE2 . PHE A 1 216 ? 15.700 49.206 35.802 1.00 22.32 ? 209 PHE A CE2 1 ATOM 1294 C CZ . PHE A 1 216 ? 15.624 47.942 36.431 1.00 22.28 ? 209 PHE A CZ 1 ATOM 1295 N N . ARG A 1 217 ? 19.984 47.652 34.568 1.00 21.11 ? 210 ARG A N 1 ATOM 1296 C CA . ARG A 1 217 ? 19.844 47.060 33.212 1.00 21.03 ? 210 ARG A CA 1 ATOM 1297 C C . ARG A 1 217 ? 18.635 47.633 32.443 1.00 22.52 ? 210 ARG A C 1 ATOM 1298 O O . ARG A 1 217 ? 18.662 47.677 31.213 1.00 22.15 ? 210 ARG A O 1 ATOM 1299 C CB . ARG A 1 217 ? 19.730 45.534 33.297 1.00 21.54 ? 210 ARG A CB 1 ATOM 1300 C CG . ARG A 1 217 ? 18.440 45.072 34.053 1.00 19.85 ? 210 ARG A CG 1 ATOM 1301 C CD . ARG A 1 217 ? 18.422 43.514 34.244 1.00 21.54 ? 210 ARG A CD 1 ATOM 1302 N NE . ARG A 1 217 ? 19.179 43.071 35.429 1.00 21.98 ? 210 ARG A NE 1 ATOM 1303 C CZ . ARG A 1 217 ? 18.798 43.318 36.698 1.00 23.68 ? 210 ARG A CZ 1 ATOM 1304 N NH1 . ARG A 1 217 ? 17.674 43.980 36.965 1.00 21.87 ? 210 ARG A NH1 1 ATOM 1305 N NH2 . ARG A 1 217 ? 19.526 42.870 37.713 1.00 21.86 ? 210 ARG A NH2 1 ATOM 1306 N N . GLY A 1 218 ? 17.599 48.098 33.167 1.00 20.94 ? 211 GLY A N 1 ATOM 1307 C CA . GLY A 1 218 ? 16.446 48.768 32.528 1.00 21.71 ? 211 GLY A CA 1 ATOM 1308 C C . GLY A 1 218 ? 16.858 50.045 31.775 1.00 22.44 ? 211 GLY A C 1 ATOM 1309 O O . GLY A 1 218 ? 16.343 50.325 30.675 1.00 22.46 ? 211 GLY A O 1 ATOM 1310 N N . ASN A 1 219 ? 17.809 50.807 32.339 1.00 22.13 ? 212 ASN A N 1 ATOM 1311 C CA . ASN A 1 219 ? 18.335 51.958 31.600 1.00 23.00 ? 212 ASN A CA 1 ATOM 1312 C C . ASN A 1 219 ? 19.077 51.591 30.315 1.00 24.42 ? 212 ASN A C 1 ATOM 1313 O O . ASN A 1 219 ? 18.975 52.317 29.305 1.00 22.54 ? 212 ASN A O 1 ATOM 1314 C CB . ASN A 1 219 ? 19.251 52.797 32.491 1.00 23.54 ? 212 ASN A CB 1 ATOM 1315 C CG . ASN A 1 219 ? 18.482 53.451 33.603 1.00 25.16 ? 212 ASN A CG 1 ATOM 1316 O OD1 . ASN A 1 219 ? 18.341 52.892 34.710 1.00 26.33 ? 212 ASN A OD1 1 ATOM 1317 N ND2 . ASN A 1 219 ? 17.910 54.618 33.297 1.00 21.04 ? 212 ASN A ND2 1 ATOM 1318 N N . LYS A 1 220 ? 19.833 50.489 30.359 1.00 23.76 ? 213 LYS A N 1 ATOM 1319 C CA . LYS A 1 220 ? 20.497 49.971 29.139 1.00 24.33 ? 213 LYS A CA 1 ATOM 1320 C C . LYS A 1 220 ? 19.470 49.714 28.031 1.00 24.43 ? 213 LYS A C 1 ATOM 1321 O O . LYS A 1 220 ? 19.691 50.065 26.855 1.00 23.77 ? 213 LYS A O 1 ATOM 1322 C CB . LYS A 1 220 ? 21.264 48.655 29.437 1.00 24.55 ? 213 LYS A CB 1 ATOM 1323 C CG . LYS A 1 220 ? 22.322 48.753 30.560 1.00 23.96 ? 213 LYS A CG 1 ATOM 1324 C CD . LYS A 1 220 ? 23.033 47.408 30.750 1.00 24.49 ? 213 LYS A CD 1 ATOM 1325 C CE . LYS A 1 220 ? 23.895 47.359 32.000 1.00 25.22 ? 213 LYS A CE 1 ATOM 1326 N NZ . LYS A 1 220 ? 25.324 47.790 31.680 1.00 24.32 ? 213 LYS A NZ 1 ATOM 1327 N N . VAL A 1 221 ? 18.384 49.049 28.399 1.00 23.01 ? 214 VAL A N 1 ATOM 1328 C CA . VAL A 1 221 ? 17.390 48.635 27.433 1.00 24.47 ? 214 VAL A CA 1 ATOM 1329 C C . VAL A 1 221 ? 16.679 49.880 26.850 1.00 25.06 ? 214 VAL A C 1 ATOM 1330 O O . VAL A 1 221 ? 16.495 49.974 25.631 1.00 25.78 ? 214 VAL A O 1 ATOM 1331 C CB . VAL A 1 221 ? 16.395 47.596 28.041 1.00 24.49 ? 214 VAL A CB 1 ATOM 1332 C CG1 . VAL A 1 221 ? 15.217 47.362 27.060 1.00 24.71 ? 214 VAL A CG1 1 ATOM 1333 C CG2 . VAL A 1 221 ? 17.113 46.245 28.302 1.00 24.29 ? 214 VAL A CG2 1 ATOM 1334 N N . LYS A 1 222 ? 16.335 50.831 27.724 1.00 24.53 ? 215 LYS A N 1 ATOM 1335 C CA . LYS A 1 222 ? 15.728 52.091 27.283 1.00 24.87 ? 215 LYS A CA 1 ATOM 1336 C C . LYS A 1 222 ? 16.656 52.776 26.308 1.00 26.08 ? 215 LYS A C 1 ATOM 1337 O O . LYS A 1 222 ? 16.246 53.223 25.212 1.00 26.61 ? 215 LYS A O 1 ATOM 1338 C CB . LYS A 1 222 ? 15.496 53.010 28.483 1.00 24.44 ? 215 LYS A CB 1 ATOM 1339 C CG . LYS A 1 222 ? 14.928 54.395 28.051 1.00 27.35 ? 215 LYS A CG 1 ATOM 1340 C CD . LYS A 1 222 ? 14.535 55.236 29.297 1.00 29.65 ? 215 LYS A CD 1 ATOM 1341 C CE . LYS A 1 222 ? 14.228 56.694 28.913 1.00 37.51 ? 215 LYS A CE 1 ATOM 1342 N NZ . LYS A 1 222 ? 15.356 57.540 29.466 1.00 46.60 ? 215 LYS A NZ 1 ATOM 1343 N N . ASN A 1 223 ? 17.933 52.837 26.676 1.00 25.97 ? 216 ASN A N 1 ATOM 1344 C CA . ASN A 1 223 ? 18.924 53.487 25.798 1.00 26.99 ? 216 ASN A CA 1 ATOM 1345 C C . ASN A 1 223 ? 19.029 52.809 24.441 1.00 28.17 ? 216 ASN A C 1 ATOM 1346 O O . ASN A 1 223 ? 19.134 53.488 23.400 1.00 28.14 ? 216 ASN A O 1 ATOM 1347 C CB . ASN A 1 223 ? 20.306 53.579 26.454 1.00 25.36 ? 216 ASN A CB 1 ATOM 1348 C CG . ASN A 1 223 ? 20.301 54.445 27.717 1.00 27.63 ? 216 ASN A CG 1 ATOM 1349 O OD1 . ASN A 1 223 ? 19.349 55.205 27.975 1.00 28.92 ? 216 ASN A OD1 1 ATOM 1350 N ND2 . ASN A 1 223 ? 21.331 54.285 28.539 1.00 24.32 ? 216 ASN A ND2 1 ATOM 1351 N N . ALA A 1 224 ? 19.002 51.478 24.435 1.00 28.69 ? 217 ALA A N 1 ATOM 1352 C CA . ALA A 1 224 ? 19.121 50.719 23.152 1.00 29.55 ? 217 ALA A CA 1 ATOM 1353 C C . ALA A 1 224 ? 17.899 50.971 22.291 1.00 30.46 ? 217 ALA A C 1 ATOM 1354 O O . ALA A 1 224 ? 18.012 51.141 21.076 1.00 30.94 ? 217 ALA A O 1 ATOM 1355 C CB . ALA A 1 224 ? 19.271 49.215 23.423 1.00 28.66 ? 217 ALA A CB 1 ATOM 1356 N N . GLN A 1 225 ? 16.728 50.979 22.941 1.00 30.82 ? 218 GLN A N 1 ATOM 1357 C CA . GLN A 1 225 ? 15.444 51.204 22.267 1.00 32.33 ? 218 GLN A CA 1 ATOM 1358 C C . GLN A 1 225 ? 15.472 52.564 21.567 1.00 33.90 ? 218 GLN A C 1 ATOM 1359 O O . GLN A 1 225 ? 15.166 52.671 20.380 1.00 34.23 ? 218 GLN A O 1 ATOM 1360 C CB A GLN A 1 225 ? 14.306 51.197 23.286 0.65 31.93 ? 218 GLN A CB 1 ATOM 1361 C CB B GLN A 1 225 ? 14.286 51.093 23.280 0.35 30.99 ? 218 GLN A CB 1 ATOM 1362 C CG A GLN A 1 225 ? 13.502 49.952 23.271 0.65 33.81 ? 218 GLN A CG 1 ATOM 1363 C CG B GLN A 1 225 ? 12.878 51.108 22.684 0.35 29.43 ? 218 GLN A CG 1 ATOM 1364 C CD A GLN A 1 225 ? 12.439 49.898 24.366 0.65 37.14 ? 218 GLN A CD 1 ATOM 1365 C CD B GLN A 1 225 ? 11.780 50.870 23.730 0.35 28.30 ? 218 GLN A CD 1 ATOM 1366 O OE1 A GLN A 1 225 ? 12.267 48.863 25.001 0.65 37.06 ? 218 GLN A OE1 1 ATOM 1367 O OE1 B GLN A 1 225 ? 11.863 49.949 24.550 0.35 28.32 ? 218 GLN A OE1 1 ATOM 1368 N NE2 A GLN A 1 225 ? 11.719 51.010 24.582 0.65 37.10 ? 218 GLN A NE2 1 ATOM 1369 N NE2 B GLN A 1 225 ? 10.746 51.696 23.697 0.35 25.31 ? 218 GLN A NE2 1 ATOM 1370 N N . LEU A 1 226 ? 15.872 53.600 22.300 1.00 34.39 ? 219 LEU A N 1 ATOM 1371 C CA . LEU A 1 226 ? 15.926 54.949 21.741 1.00 35.83 ? 219 LEU A CA 1 ATOM 1372 C C . LEU A 1 226 ? 17.002 55.124 20.661 1.00 36.74 ? 219 LEU A C 1 ATOM 1373 O O . LEU A 1 226 ? 16.907 56.026 19.823 1.00 36.76 ? 219 LEU A O 1 ATOM 1374 C CB . LEU A 1 226 ? 16.030 56.007 22.862 1.00 35.28 ? 219 LEU A CB 1 ATOM 1375 C CG . LEU A 1 226 ? 14.799 56.159 23.782 1.00 39.08 ? 219 LEU A CG 1 ATOM 1376 C CD1 . LEU A 1 226 ? 15.006 57.227 24.884 1.00 39.36 ? 219 LEU A CD1 1 ATOM 1377 C CD2 . LEU A 1 226 ? 13.481 56.406 23.038 1.00 41.89 ? 219 LEU A CD2 1 ATOM 1378 N N . ALA A 1 227 ? 17.994 54.230 20.649 1.00 35.96 ? 220 ALA A N 1 ATOM 1379 C CA . ALA A 1 227 ? 18.981 54.182 19.598 1.00 36.69 ? 220 ALA A CA 1 ATOM 1380 C C . ALA A 1 227 ? 18.436 53.411 18.380 1.00 37.14 ? 220 ALA A C 1 ATOM 1381 O O . ALA A 1 227 ? 19.094 53.326 17.372 1.00 38.16 ? 220 ALA A O 1 ATOM 1382 C CB . ALA A 1 227 ? 20.243 53.544 20.111 1.00 36.69 ? 220 ALA A CB 1 ATOM 1383 N N . GLY A 1 228 ? 17.217 52.870 18.484 1.00 35.99 ? 221 GLY A N 1 ATOM 1384 C CA . GLY A 1 228 ? 16.609 52.160 17.355 1.00 35.68 ? 221 GLY A CA 1 ATOM 1385 C C . GLY A 1 228 ? 16.966 50.684 17.206 1.00 35.44 ? 221 GLY A C 1 ATOM 1386 O O . GLY A 1 228 ? 16.683 50.079 16.156 1.00 34.94 ? 221 GLY A O 1 ATOM 1387 N N . ALA A 1 229 ? 17.551 50.081 18.253 1.00 34.38 ? 222 ALA A N 1 ATOM 1388 C CA . ALA A 1 229 ? 17.931 48.664 18.212 1.00 34.03 ? 222 ALA A CA 1 ATOM 1389 C C . ALA A 1 229 ? 16.676 47.804 18.054 1.00 34.50 ? 222 ALA A C 1 ATOM 1390 O O . ALA A 1 229 ? 15.586 48.200 18.493 1.00 34.21 ? 222 ALA A O 1 ATOM 1391 C CB . ALA A 1 229 ? 18.703 48.277 19.459 1.00 33.40 ? 222 ALA A CB 1 ATOM 1392 N N . LYS A 1 230 ? 16.803 46.646 17.418 1.00 34.43 ? 223 LYS A N 1 ATOM 1393 C CA . LYS A 1 230 ? 15.666 45.754 17.344 1.00 33.65 ? 223 LYS A CA 1 ATOM 1394 C C . LYS A 1 230 ? 15.742 44.607 18.362 1.00 32.55 ? 223 LYS A C 1 ATOM 1395 O O . LYS A 1 230 ? 14.838 43.786 18.437 1.00 32.82 ? 223 LYS A O 1 ATOM 1396 C CB . LYS A 1 230 ? 15.452 45.276 15.899 1.00 36.47 ? 223 LYS A CB 1 ATOM 1397 C CG . LYS A 1 230 ? 16.375 44.253 15.399 1.00 38.81 ? 223 LYS A CG 1 ATOM 1398 C CD . LYS A 1 230 ? 15.852 43.829 14.010 1.00 41.65 ? 223 LYS A CD 1 ATOM 1399 C CE . LYS A 1 230 ? 16.936 43.353 13.154 1.00 45.66 ? 223 LYS A CE 1 ATOM 1400 N NZ . LYS A 1 230 ? 16.345 42.680 11.955 1.00 45.60 ? 223 LYS A NZ 1 ATOM 1401 N N . GLY A 1 231 ? 16.803 44.570 19.155 1.00 31.08 ? 224 GLY A N 1 ATOM 1402 C CA . GLY A 1 231 ? 16.883 43.632 20.297 1.00 29.93 ? 224 GLY A CA 1 ATOM 1403 C C . GLY A 1 231 ? 18.159 43.884 21.064 1.00 29.59 ? 224 GLY A C 1 ATOM 1404 O O . GLY A 1 231 ? 19.063 44.581 20.572 1.00 30.24 ? 224 GLY A O 1 ATOM 1405 N N . VAL A 1 232 ? 18.222 43.346 22.286 1.00 29.48 ? 225 VAL A N 1 ATOM 1406 C CA . VAL A 1 232 ? 19.331 43.580 23.196 1.00 28.64 ? 225 VAL A CA 1 ATOM 1407 C C . VAL A 1 232 ? 19.749 42.225 23.813 1.00 29.27 ? 225 VAL A C 1 ATOM 1408 O O . VAL A 1 232 ? 18.918 41.453 24.315 1.00 28.13 ? 225 VAL A O 1 ATOM 1409 C CB . VAL A 1 232 ? 18.956 44.511 24.378 1.00 28.22 ? 225 VAL A CB 1 ATOM 1410 C CG1 . VAL A 1 232 ? 20.172 44.763 25.257 1.00 26.90 ? 225 VAL A CG1 1 ATOM 1411 C CG2 . VAL A 1 232 ? 18.313 45.845 23.890 1.00 27.84 ? 225 VAL A CG2 1 ATOM 1412 N N . ILE A 1 233 ? 21.052 41.981 23.776 1.00 29.77 ? 226 ILE A N 1 ATOM 1413 C CA . ILE A 1 233 ? 21.670 40.849 24.440 1.00 29.26 ? 226 ILE A CA 1 ATOM 1414 C C . ILE A 1 233 ? 22.540 41.401 25.567 1.00 28.37 ? 226 ILE A C 1 ATOM 1415 O O . ILE A 1 233 ? 23.468 42.201 25.331 1.00 30.70 ? 226 ILE A O 1 ATOM 1416 C CB . ILE A 1 233 ? 22.505 40.049 23.432 1.00 31.17 ? 226 ILE A CB 1 ATOM 1417 C CG1 . ILE A 1 233 ? 21.574 39.495 22.327 1.00 31.38 ? 226 ILE A CG1 1 ATOM 1418 C CG2 . ILE A 1 233 ? 23.384 38.970 24.161 1.00 29.66 ? 226 ILE A CG2 1 ATOM 1419 C CD1 . ILE A 1 233 ? 22.305 38.842 21.156 1.00 29.63 ? 226 ILE A CD1 1 ATOM 1420 N N . LEU A 1 234 ? 22.234 40.979 26.782 1.00 27.07 ? 227 LEU A N 1 ATOM 1421 C CA . LEU A 1 234 ? 22.972 41.409 27.984 1.00 26.30 ? 227 LEU A CA 1 ATOM 1422 C C . LEU A 1 234 ? 23.907 40.258 28.387 1.00 26.84 ? 227 LEU A C 1 ATOM 1423 O O . LEU A 1 234 ? 23.474 39.106 28.364 1.00 26.42 ? 227 LEU A O 1 ATOM 1424 C CB . LEU A 1 234 ? 21.989 41.689 29.107 1.00 24.78 ? 227 LEU A CB 1 ATOM 1425 C CG . LEU A 1 234 ? 21.089 42.924 28.925 1.00 26.39 ? 227 LEU A CG 1 ATOM 1426 C CD1 . LEU A 1 234 ? 20.053 42.988 30.062 1.00 26.10 ? 227 LEU A CD1 1 ATOM 1427 C CD2 . LEU A 1 234 ? 21.967 44.214 28.844 1.00 25.69 ? 227 LEU A CD2 1 ATOM 1428 N N . TYR A 1 235 ? 25.176 40.538 28.704 1.00 26.77 ? 228 TYR A N 1 ATOM 1429 C CA . TYR A 1 235 ? 26.070 39.441 29.180 1.00 26.44 ? 228 TYR A CA 1 ATOM 1430 C C . TYR A 1 235 ? 26.950 39.896 30.319 1.00 26.36 ? 228 TYR A C 1 ATOM 1431 O O . TYR A 1 235 ? 27.180 41.112 30.482 1.00 27.00 ? 228 TYR A O 1 ATOM 1432 C CB . TYR A 1 235 ? 26.922 38.817 28.066 1.00 27.70 ? 228 TYR A CB 1 ATOM 1433 C CG . TYR A 1 235 ? 28.164 39.637 27.750 1.00 26.97 ? 228 TYR A CG 1 ATOM 1434 C CD1 . TYR A 1 235 ? 29.412 39.288 28.271 1.00 29.14 ? 228 TYR A CD1 1 ATOM 1435 C CD2 . TYR A 1 235 ? 28.075 40.778 26.946 1.00 28.22 ? 228 TYR A CD2 1 ATOM 1436 C CE1 . TYR A 1 235 ? 30.563 40.068 27.981 1.00 30.91 ? 228 TYR A CE1 1 ATOM 1437 C CE2 . TYR A 1 235 ? 29.206 41.568 26.657 1.00 26.75 ? 228 TYR A CE2 1 ATOM 1438 C CZ . TYR A 1 235 ? 30.424 41.219 27.186 1.00 31.48 ? 228 TYR A CZ 1 ATOM 1439 O OH . TYR A 1 235 ? 31.507 42.017 26.904 1.00 31.88 ? 228 TYR A OH 1 ATOM 1440 N N . SER A 1 236 ? 27.430 38.932 31.116 1.00 26.08 ? 229 SER A N 1 ATOM 1441 C CA . SER A 1 236 ? 28.349 39.245 32.216 1.00 25.06 ? 229 SER A CA 1 ATOM 1442 C C . SER A 1 236 ? 29.777 39.070 31.742 1.00 26.75 ? 229 SER A C 1 ATOM 1443 O O . SER A 1 236 ? 30.217 37.956 31.480 1.00 28.37 ? 229 SER A O 1 ATOM 1444 C CB . SER A 1 236 ? 28.059 38.336 33.417 1.00 25.72 ? 229 SER A CB 1 ATOM 1445 O OG . SER A 1 236 ? 26.697 38.516 33.825 1.00 24.77 ? 229 SER A OG 1 ATOM 1446 N N . ASP A 1 237 ? 30.513 40.168 31.662 1.00 27.65 ? 230 ASP A N 1 ATOM 1447 C CA . ASP A 1 237 ? 31.934 40.088 31.287 1.00 29.39 ? 230 ASP A CA 1 ATOM 1448 C C . ASP A 1 237 ? 32.777 39.752 32.522 1.00 29.74 ? 230 ASP A C 1 ATOM 1449 O O . ASP A 1 237 ? 32.593 40.362 33.577 1.00 28.93 ? 230 ASP A O 1 ATOM 1450 C CB . ASP A 1 237 ? 32.393 41.417 30.658 1.00 30.06 ? 230 ASP A CB 1 ATOM 1451 C CG . ASP A 1 237 ? 33.669 41.262 29.839 1.00 31.82 ? 230 ASP A CG 1 ATOM 1452 O OD1 . ASP A 1 237 ? 33.585 41.263 28.596 1.00 34.08 ? 230 ASP A OD1 1 ATOM 1453 O OD2 . ASP A 1 237 ? 34.746 41.072 30.441 1.00 31.96 ? 230 ASP A OD2 1 ATOM 1454 N N . PRO A 1 238 ? 33.739 38.820 32.387 1.00 31.65 ? 231 PRO A N 1 ATOM 1455 C CA . PRO A 1 238 ? 34.721 38.550 33.439 1.00 32.75 ? 231 PRO A CA 1 ATOM 1456 C C . PRO A 1 238 ? 35.372 39.821 33.992 1.00 33.24 ? 231 PRO A C 1 ATOM 1457 O O . PRO A 1 238 ? 35.719 39.867 35.162 1.00 33.38 ? 231 PRO A O 1 ATOM 1458 C CB . PRO A 1 238 ? 35.773 37.679 32.737 1.00 34.27 ? 231 PRO A CB 1 ATOM 1459 C CG . PRO A 1 238 ? 35.048 37.055 31.624 1.00 34.59 ? 231 PRO A CG 1 ATOM 1460 C CD . PRO A 1 238 ? 34.027 38.038 31.165 1.00 32.78 ? 231 PRO A CD 1 ATOM 1461 N N . ALA A 1 239 ? 35.505 40.869 33.184 1.00 34.18 ? 232 ALA A N 1 ATOM 1462 C CA . ALA A 1 239 ? 36.080 42.118 33.725 1.00 34.57 ? 232 ALA A CA 1 ATOM 1463 C C . ALA A 1 239 ? 35.301 42.686 34.921 1.00 33.98 ? 232 ALA A C 1 ATOM 1464 O O . ALA A 1 239 ? 35.877 43.251 35.862 1.00 33.70 ? 232 ALA A O 1 ATOM 1465 C CB . ALA A 1 239 ? 36.213 43.174 32.614 1.00 35.50 ? 232 ALA A CB 1 ATOM 1466 N N . ASP A 1 240 ? 33.990 42.493 34.885 1.00 32.32 ? 233 ASP A N 1 ATOM 1467 C CA . ASP A 1 240 ? 33.066 43.041 35.860 1.00 32.05 ? 233 ASP A CA 1 ATOM 1468 C C . ASP A 1 240 ? 32.584 42.012 36.895 1.00 31.84 ? 233 ASP A C 1 ATOM 1469 O O . ASP A 1 240 ? 32.187 42.406 38.021 1.00 32.89 ? 233 ASP A O 1 ATOM 1470 C CB . ASP A 1 240 ? 31.872 43.617 35.091 1.00 30.69 ? 233 ASP A CB 1 ATOM 1471 C CG . ASP A 1 240 ? 32.305 44.618 34.016 1.00 32.76 ? 233 ASP A CG 1 ATOM 1472 O OD1 . ASP A 1 240 ? 32.630 45.754 34.415 1.00 33.41 ? 233 ASP A OD1 1 ATOM 1473 O OD2 . ASP A 1 240 ? 32.363 44.261 32.796 1.00 32.52 ? 233 ASP A OD2 1 ATOM 1474 N N . TYR A 1 241 ? 32.566 40.727 36.518 1.00 30.78 ? 234 TYR A N 1 ATOM 1475 C CA . TYR A 1 241 ? 32.055 39.661 37.385 1.00 29.75 ? 234 TYR A CA 1 ATOM 1476 C C . TYR A 1 241 ? 33.040 38.533 37.730 1.00 31.56 ? 234 TYR A C 1 ATOM 1477 O O . TYR A 1 241 ? 32.621 37.478 38.224 1.00 31.81 ? 234 TYR A O 1 ATOM 1478 C CB . TYR A 1 241 ? 30.738 39.092 36.823 1.00 29.56 ? 234 TYR A CB 1 ATOM 1479 C CG . TYR A 1 241 ? 29.714 40.185 36.704 1.00 26.26 ? 234 TYR A CG 1 ATOM 1480 C CD1 . TYR A 1 241 ? 29.549 40.884 35.510 1.00 26.83 ? 234 TYR A CD1 1 ATOM 1481 C CD2 . TYR A 1 241 ? 28.985 40.580 37.816 1.00 26.06 ? 234 TYR A CD2 1 ATOM 1482 C CE1 . TYR A 1 241 ? 28.646 41.972 35.414 1.00 27.75 ? 234 TYR A CE1 1 ATOM 1483 C CE2 . TYR A 1 241 ? 28.056 41.633 37.750 1.00 28.28 ? 234 TYR A CE2 1 ATOM 1484 C CZ . TYR A 1 241 ? 27.893 42.332 36.545 1.00 28.77 ? 234 TYR A CZ 1 ATOM 1485 O OH . TYR A 1 241 ? 26.962 43.353 36.514 1.00 28.40 ? 234 TYR A OH 1 ATOM 1486 N N . PHE A 1 242 ? 34.332 38.746 37.492 1.00 32.65 ? 235 PHE A N 1 ATOM 1487 C CA . PHE A 1 242 ? 35.325 37.742 37.886 1.00 33.80 ? 235 PHE A CA 1 ATOM 1488 C C . PHE A 1 242 ? 36.527 38.412 38.544 1.00 35.32 ? 235 PHE A C 1 ATOM 1489 O O . PHE A 1 242 ? 37.366 39.003 37.868 1.00 36.54 ? 235 PHE A O 1 ATOM 1490 C CB . PHE A 1 242 ? 35.711 36.886 36.688 1.00 32.84 ? 235 PHE A CB 1 ATOM 1491 C CG . PHE A 1 242 ? 36.461 35.622 37.033 1.00 34.07 ? 235 PHE A CG 1 ATOM 1492 C CD1 . PHE A 1 242 ? 35.791 34.403 37.086 1.00 30.82 ? 235 PHE A CD1 1 ATOM 1493 C CD2 . PHE A 1 242 ? 37.865 35.640 37.227 1.00 33.10 ? 235 PHE A CD2 1 ATOM 1494 C CE1 . PHE A 1 242 ? 36.477 33.193 37.398 1.00 31.79 ? 235 PHE A CE1 1 ATOM 1495 C CE2 . PHE A 1 242 ? 38.578 34.457 37.528 1.00 35.52 ? 235 PHE A CE2 1 ATOM 1496 C CZ . PHE A 1 242 ? 37.894 33.219 37.609 1.00 36.12 ? 235 PHE A CZ 1 ATOM 1497 N N . ALA A 1 243 ? 36.587 38.338 39.870 1.00 36.19 ? 236 ALA A N 1 ATOM 1498 C CA . ALA A 1 243 ? 37.681 38.938 40.620 1.00 38.31 ? 236 ALA A CA 1 ATOM 1499 C C . ALA A 1 243 ? 38.972 38.167 40.402 1.00 40.81 ? 236 ALA A C 1 ATOM 1500 O O . ALA A 1 243 ? 38.999 36.950 40.541 1.00 41.22 ? 236 ALA A O 1 ATOM 1501 C CB . ALA A 1 243 ? 37.350 38.995 42.093 1.00 38.08 ? 236 ALA A CB 1 ATOM 1502 N N . PRO A 1 244 ? 40.055 38.877 40.063 1.00 42.91 ? 237 PRO A N 1 ATOM 1503 C CA . PRO A 1 244 ? 41.342 38.199 39.833 1.00 44.18 ? 237 PRO A CA 1 ATOM 1504 C C . PRO A 1 244 ? 41.777 37.345 41.044 1.00 44.39 ? 237 PRO A C 1 ATOM 1505 O O . PRO A 1 244 ? 41.649 37.790 42.189 1.00 44.30 ? 237 PRO A O 1 ATOM 1506 C CB . PRO A 1 244 ? 42.314 39.365 39.598 1.00 45.42 ? 237 PRO A CB 1 ATOM 1507 C CG . PRO A 1 244 ? 41.420 40.538 39.164 1.00 44.64 ? 237 PRO A CG 1 ATOM 1508 C CD . PRO A 1 244 ? 40.150 40.349 39.919 1.00 43.47 ? 237 PRO A CD 1 ATOM 1509 N N . GLY A 1 245 ? 42.236 36.118 40.784 1.00 44.96 ? 238 GLY A N 1 ATOM 1510 C CA . GLY A 1 245 ? 42.829 35.237 41.823 1.00 44.73 ? 238 GLY A CA 1 ATOM 1511 C C . GLY A 1 245 ? 41.837 34.474 42.707 1.00 43.88 ? 238 GLY A C 1 ATOM 1512 O O . GLY A 1 245 ? 42.249 33.741 43.615 1.00 44.23 ? 238 GLY A O 1 ATOM 1513 N N . VAL A 1 246 ? 40.539 34.631 42.452 1.00 40.90 ? 239 VAL A N 1 ATOM 1514 C CA . VAL A 1 246 ? 39.491 33.870 43.174 1.00 38.95 ? 239 VAL A CA 1 ATOM 1515 C C . VAL A 1 246 ? 38.863 32.849 42.238 1.00 38.34 ? 239 VAL A C 1 ATOM 1516 O O . VAL A 1 246 ? 38.777 33.086 41.051 1.00 37.69 ? 239 VAL A O 1 ATOM 1517 C CB . VAL A 1 246 ? 38.434 34.804 43.929 1.00 38.70 ? 239 VAL A CB 1 ATOM 1518 C CG1 A VAL A 1 246 ? 38.784 36.286 43.795 0.50 37.20 ? 239 VAL A CG1 1 ATOM 1519 C CG1 B VAL A 1 246 ? 37.179 34.020 44.363 0.50 35.71 ? 239 VAL A CG1 1 ATOM 1520 C CG2 A VAL A 1 246 ? 36.975 34.481 43.594 0.50 35.63 ? 239 VAL A CG2 1 ATOM 1521 C CG2 B VAL A 1 246 ? 39.081 35.547 45.101 0.50 37.69 ? 239 VAL A CG2 1 ATOM 1522 N N . LYS A 1 247 ? 38.468 31.702 42.782 1.00 38.87 ? 240 LYS A N 1 ATOM 1523 C CA . LYS A 1 247 ? 37.940 30.614 41.976 1.00 40.47 ? 240 LYS A CA 1 ATOM 1524 C C . LYS A 1 247 ? 36.445 30.758 41.695 1.00 39.53 ? 240 LYS A C 1 ATOM 1525 O O . LYS A 1 247 ? 35.726 31.380 42.469 1.00 37.43 ? 240 LYS A O 1 ATOM 1526 C CB . LYS A 1 247 ? 38.239 29.262 42.648 1.00 42.62 ? 240 LYS A CB 1 ATOM 1527 C CG . LYS A 1 247 ? 39.745 28.952 42.844 1.00 45.67 ? 240 LYS A CG 1 ATOM 1528 C CD . LYS A 1 247 ? 40.499 28.813 41.504 1.00 53.51 ? 240 LYS A CD 1 ATOM 1529 C CE . LYS A 1 247 ? 42.060 28.934 41.660 1.00 58.71 ? 240 LYS A CE 1 ATOM 1530 N NZ . LYS A 1 247 ? 42.501 30.396 41.753 1.00 61.05 ? 240 LYS A NZ 1 ATOM 1531 N N . SER A 1 248 ? 36.014 30.190 40.566 1.00 39.50 ? 241 SER A N 1 ATOM 1532 C CA . SER A 1 248 ? 34.604 30.033 40.199 1.00 38.42 ? 241 SER A CA 1 ATOM 1533 C C . SER A 1 248 ? 33.831 29.203 41.221 1.00 37.05 ? 241 SER A C 1 ATOM 1534 O O . SER A 1 248 ? 34.378 28.213 41.738 1.00 37.00 ? 241 SER A O 1 ATOM 1535 C CB . SER A 1 248 ? 34.544 29.224 38.892 1.00 40.53 ? 241 SER A CB 1 ATOM 1536 O OG . SER A 1 248 ? 34.768 30.031 37.758 1.00 44.35 ? 241 SER A OG 1 ATOM 1537 N N . TYR A 1 249 ? 32.550 29.546 41.449 1.00 34.10 ? 242 TYR A N 1 ATOM 1538 C CA . TYR A 1 249 ? 31.601 28.657 42.152 1.00 33.10 ? 242 TYR A CA 1 ATOM 1539 C C . TYR A 1 249 ? 31.650 27.254 41.533 1.00 33.79 ? 242 TYR A C 1 ATOM 1540 O O . TYR A 1 249 ? 31.595 27.151 40.310 1.00 33.48 ? 242 TYR A O 1 ATOM 1541 C CB . TYR A 1 249 ? 30.150 29.190 42.112 1.00 31.97 ? 242 TYR A CB 1 ATOM 1542 C CG . TYR A 1 249 ? 29.390 28.638 43.292 1.00 31.12 ? 242 TYR A CG 1 ATOM 1543 C CD1 . TYR A 1 249 ? 29.623 29.135 44.582 1.00 31.92 ? 242 TYR A CD1 1 ATOM 1544 C CD2 . TYR A 1 249 ? 28.543 27.538 43.147 1.00 32.08 ? 242 TYR A CD2 1 ATOM 1545 C CE1 . TYR A 1 249 ? 28.999 28.580 45.696 1.00 30.67 ? 242 TYR A CE1 1 ATOM 1546 C CE2 . TYR A 1 249 ? 27.912 26.987 44.236 1.00 33.98 ? 242 TYR A CE2 1 ATOM 1547 C CZ . TYR A 1 249 ? 28.146 27.533 45.512 1.00 33.95 ? 242 TYR A CZ 1 ATOM 1548 O OH . TYR A 1 249 ? 27.560 26.978 46.596 1.00 35.73 ? 242 TYR A OH 1 ATOM 1549 N N . PRO A 1 250 ? 31.698 26.181 42.358 1.00 34.52 ? 243 PRO A N 1 ATOM 1550 C CA . PRO A 1 250 ? 31.515 26.123 43.828 1.00 35.18 ? 243 PRO A CA 1 ATOM 1551 C C . PRO A 1 250 ? 32.813 26.237 44.662 1.00 36.53 ? 243 PRO A C 1 ATOM 1552 O O . PRO A 1 250 ? 32.759 26.077 45.884 1.00 38.02 ? 243 PRO A O 1 ATOM 1553 C CB . PRO A 1 250 ? 30.913 24.719 44.032 1.00 34.86 ? 243 PRO A CB 1 ATOM 1554 C CG . PRO A 1 250 ? 31.694 23.884 42.963 1.00 35.37 ? 243 PRO A CG 1 ATOM 1555 C CD . PRO A 1 250 ? 31.750 24.823 41.765 1.00 35.60 ? 243 PRO A CD 1 ATOM 1556 N N . ASP A 1 251 ? 33.947 26.493 44.031 1.00 36.35 ? 244 ASP A N 1 ATOM 1557 C CA . ASP A 1 251 ? 35.216 26.514 44.772 1.00 37.79 ? 244 ASP A CA 1 ATOM 1558 C C . ASP A 1 251 ? 35.617 27.899 45.257 1.00 37.38 ? 244 ASP A C 1 ATOM 1559 O O . ASP A 1 251 ? 36.567 28.034 46.007 1.00 36.97 ? 244 ASP A O 1 ATOM 1560 C CB . ASP A 1 251 ? 36.352 25.934 43.938 1.00 38.99 ? 244 ASP A CB 1 ATOM 1561 C CG . ASP A 1 251 ? 36.057 24.518 43.442 1.00 43.46 ? 244 ASP A CG 1 ATOM 1562 O OD1 . ASP A 1 251 ? 35.482 23.673 44.197 1.00 43.55 ? 244 ASP A OD1 1 ATOM 1563 O OD2 . ASP A 1 251 ? 36.414 24.269 42.276 1.00 47.40 ? 244 ASP A OD2 1 ATOM 1564 N N . GLY A 1 252 ? 34.886 28.922 44.814 1.00 35.94 ? 245 GLY A N 1 ATOM 1565 C CA . GLY A 1 252 ? 35.122 30.307 45.245 1.00 35.21 ? 245 GLY A CA 1 ATOM 1566 C C . GLY A 1 252 ? 33.869 31.084 44.913 1.00 34.14 ? 245 GLY A C 1 ATOM 1567 O O . GLY A 1 252 ? 32.829 30.495 44.540 1.00 33.65 ? 245 GLY A O 1 ATOM 1568 N N . TRP A 1 253 ? 33.945 32.403 45.043 1.00 32.96 ? 246 TRP A N 1 ATOM 1569 C CA . TRP A 1 253 ? 32.736 33.207 44.887 1.00 31.31 ? 246 TRP A CA 1 ATOM 1570 C C . TRP A 1 253 ? 32.585 33.870 43.518 1.00 30.89 ? 246 TRP A C 1 ATOM 1571 O O . TRP A 1 253 ? 31.694 34.742 43.339 1.00 28.67 ? 246 TRP A O 1 ATOM 1572 C CB . TRP A 1 253 ? 32.575 34.245 46.035 1.00 31.18 ? 246 TRP A CB 1 ATOM 1573 C CG . TRP A 1 253 ? 33.830 35.000 46.402 1.00 32.20 ? 246 TRP A CG 1 ATOM 1574 C CD1 . TRP A 1 253 ? 34.786 34.611 47.295 1.00 34.99 ? 246 TRP A CD1 1 ATOM 1575 C CD2 . TRP A 1 253 ? 34.263 36.275 45.885 1.00 34.33 ? 246 TRP A CD2 1 ATOM 1576 N NE1 . TRP A 1 253 ? 35.774 35.567 47.377 1.00 34.54 ? 246 TRP A NE1 1 ATOM 1577 C CE2 . TRP A 1 253 ? 35.483 36.595 46.526 1.00 34.18 ? 246 TRP A CE2 1 ATOM 1578 C CE3 . TRP A 1 253 ? 33.748 37.165 44.937 1.00 35.03 ? 246 TRP A CE3 1 ATOM 1579 C CZ2 . TRP A 1 253 ? 36.201 37.770 46.252 1.00 36.34 ? 246 TRP A CZ2 1 ATOM 1580 C CZ3 . TRP A 1 253 ? 34.455 38.365 44.675 1.00 35.15 ? 246 TRP A CZ3 1 ATOM 1581 C CH2 . TRP A 1 253 ? 35.681 38.644 45.329 1.00 35.78 ? 246 TRP A CH2 1 ATOM 1582 N N . ASN A 1 254 ? 33.396 33.439 42.543 1.00 29.78 ? 247 ASN A N 1 ATOM 1583 C CA . ASN A 1 254 ? 33.326 34.033 41.203 1.00 30.42 ? 247 ASN A CA 1 ATOM 1584 C C . ASN A 1 254 ? 32.276 33.412 40.302 1.00 30.00 ? 247 ASN A C 1 ATOM 1585 O O . ASN A 1 254 ? 31.855 32.257 40.513 1.00 29.86 ? 247 ASN A O 1 ATOM 1586 C CB . ASN A 1 254 ? 34.697 33.951 40.475 1.00 31.36 ? 247 ASN A CB 1 ATOM 1587 C CG . ASN A 1 254 ? 35.546 35.218 40.671 1.00 31.96 ? 247 ASN A CG 1 ATOM 1588 O OD1 . ASN A 1 254 ? 35.026 36.283 41.063 1.00 30.97 ? 247 ASN A OD1 1 ATOM 1589 N ND2 . ASN A 1 254 ? 36.877 35.098 40.431 1.00 31.34 ? 247 ASN A ND2 1 ATOM 1590 N N . LEU A 1 255 ? 31.894 34.175 39.273 1.00 28.90 ? 248 LEU A N 1 ATOM 1591 C CA . LEU A 1 255 ? 30.938 33.728 38.280 1.00 28.31 ? 248 LEU A CA 1 ATOM 1592 C C . LEU A 1 255 ? 31.560 32.746 37.278 1.00 29.00 ? 248 LEU A C 1 ATOM 1593 O O . LEU A 1 255 ? 32.531 33.087 36.604 1.00 30.49 ? 248 LEU A O 1 ATOM 1594 C CB . LEU A 1 255 ? 30.340 34.935 37.544 1.00 27.24 ? 248 LEU A CB 1 ATOM 1595 C CG . LEU A 1 255 ? 29.220 34.598 36.557 1.00 28.32 ? 248 LEU A CG 1 ATOM 1596 C CD1 . LEU A 1 255 ? 27.906 34.124 37.240 1.00 27.16 ? 248 LEU A CD1 1 ATOM 1597 C CD2 . LEU A 1 255 ? 28.999 35.873 35.707 1.00 28.38 ? 248 LEU A CD2 1 ATOM 1598 N N . PRO A 1 256 ? 31.001 31.517 37.179 1.00 29.05 ? 249 PRO A N 1 ATOM 1599 C CA . PRO A 1 256 ? 31.475 30.649 36.104 1.00 29.88 ? 249 PRO A CA 1 ATOM 1600 C C . PRO A 1 256 ? 30.985 31.074 34.711 1.00 30.06 ? 249 PRO A C 1 ATOM 1601 O O . PRO A 1 256 ? 30.023 31.853 34.585 1.00 29.47 ? 249 PRO A O 1 ATOM 1602 C CB . PRO A 1 256 ? 30.920 29.263 36.475 1.00 29.77 ? 249 PRO A CB 1 ATOM 1603 C CG . PRO A 1 256 ? 29.919 29.455 37.474 1.00 29.18 ? 249 PRO A CG 1 ATOM 1604 C CD . PRO A 1 256 ? 29.894 30.899 37.943 1.00 28.74 ? 249 PRO A CD 1 ATOM 1605 N N . GLY A 1 257 ? 31.632 30.523 33.682 1.00 30.96 ? 250 GLY A N 1 ATOM 1606 C CA . GLY A 1 257 ? 31.337 30.871 32.297 1.00 31.47 ? 250 GLY A CA 1 ATOM 1607 C C . GLY A 1 257 ? 29.915 30.555 31.875 1.00 30.86 ? 250 GLY A C 1 ATOM 1608 O O . GLY A 1 257 ? 29.410 31.161 30.935 1.00 30.72 ? 250 GLY A O 1 ATOM 1609 N N . GLY A 1 258 ? 29.280 29.609 32.574 1.00 30.41 ? 251 GLY A N 1 ATOM 1610 C CA . GLY A 1 258 ? 27.884 29.259 32.340 1.00 29.33 ? 251 GLY A CA 1 ATOM 1611 C C . GLY A 1 258 ? 26.880 30.048 33.191 1.00 28.80 ? 251 GLY A C 1 ATOM 1612 O O . GLY A 1 258 ? 25.685 29.973 32.945 1.00 27.89 ? 251 GLY A O 1 ATOM 1613 N N . GLY A 1 259 ? 27.360 30.806 34.181 1.00 28.58 ? 252 GLY A N 1 ATOM 1614 C CA . GLY A 1 259 ? 26.471 31.655 35.021 1.00 26.88 ? 252 GLY A CA 1 ATOM 1615 C C . GLY A 1 259 ? 25.843 32.823 34.265 1.00 26.60 ? 252 GLY A C 1 ATOM 1616 O O . GLY A 1 259 ? 26.436 33.390 33.325 1.00 25.93 ? 252 GLY A O 1 ATOM 1617 N N . VAL A 1 260 ? 24.641 33.176 34.677 1.00 25.93 ? 253 VAL A N 1 ATOM 1618 C CA . VAL A 1 260 ? 23.857 34.245 34.034 1.00 25.03 ? 253 VAL A CA 1 ATOM 1619 C C . VAL A 1 260 ? 23.088 35.051 35.079 1.00 24.86 ? 253 VAL A C 1 ATOM 1620 O O . VAL A 1 260 ? 22.491 34.497 36.024 1.00 24.01 ? 253 VAL A O 1 ATOM 1621 C CB . VAL A 1 260 ? 22.836 33.681 32.984 1.00 25.02 ? 253 VAL A CB 1 ATOM 1622 C CG1 . VAL A 1 260 ? 22.150 34.842 32.211 1.00 23.27 ? 253 VAL A CG1 1 ATOM 1623 C CG2 . VAL A 1 260 ? 23.500 32.680 31.988 1.00 27.38 ? 253 VAL A CG2 1 ATOM 1624 N N . GLN A 1 261 ? 23.098 36.369 34.911 1.00 22.95 ? 254 GLN A N 1 ATOM 1625 C CA . GLN A 1 261 ? 22.345 37.257 35.781 1.00 23.36 ? 254 GLN A CA 1 ATOM 1626 C C . GLN A 1 261 ? 20.913 37.445 35.264 1.00 22.80 ? 254 GLN A C 1 ATOM 1627 O O . GLN A 1 261 ? 20.725 38.019 34.191 1.00 23.97 ? 254 GLN A O 1 ATOM 1628 C CB . GLN A 1 261 ? 23.048 38.619 35.815 1.00 21.49 ? 254 GLN A CB 1 ATOM 1629 C CG . GLN A 1 261 ? 22.345 39.677 36.767 1.00 21.44 ? 254 GLN A CG 1 ATOM 1630 C CD . GLN A 1 261 ? 22.934 41.086 36.552 1.00 22.57 ? 254 GLN A CD 1 ATOM 1631 O OE1 . GLN A 1 261 ? 22.197 42.065 36.550 1.00 21.52 ? 254 GLN A OE1 1 ATOM 1632 N NE2 . GLN A 1 261 ? 24.266 41.173 36.342 1.00 19.86 ? 254 GLN A NE2 1 ATOM 1633 N N . ARG A 1 262 ? 19.911 36.969 36.017 1.00 22.22 ? 255 ARG A N 1 ATOM 1634 C CA . ARG A 1 262 ? 18.517 37.321 35.754 1.00 22.73 ? 255 ARG A CA 1 ATOM 1635 C C . ARG A 1 262 ? 18.215 38.788 36.129 1.00 21.77 ? 255 ARG A C 1 ATOM 1636 O O . ARG A 1 262 ? 19.028 39.452 36.787 1.00 20.79 ? 255 ARG A O 1 ATOM 1637 C CB . ARG A 1 262 ? 17.556 36.422 36.564 1.00 20.28 ? 255 ARG A CB 1 ATOM 1638 C CG . ARG A 1 262 ? 17.554 34.957 36.046 1.00 22.98 ? 255 ARG A CG 1 ATOM 1639 C CD . ARG A 1 262 ? 17.164 33.970 37.164 1.00 22.94 ? 255 ARG A CD 1 ATOM 1640 N NE . ARG A 1 262 ? 17.420 32.573 36.787 1.00 23.29 ? 255 ARG A NE 1 ATOM 1641 C CZ . ARG A 1 262 ? 18.626 32.017 36.742 1.00 24.95 ? 255 ARG A CZ 1 ATOM 1642 N NH1 . ARG A 1 262 ? 19.720 32.735 37.071 1.00 22.63 ? 255 ARG A NH1 1 ATOM 1643 N NH2 . ARG A 1 262 ? 18.733 30.743 36.414 1.00 23.16 ? 255 ARG A NH2 1 ATOM 1644 N N . GLY A 1 263 ? 17.035 39.276 35.738 1.00 21.23 ? 256 GLY A N 1 ATOM 1645 C CA . GLY A 1 263 ? 16.606 40.610 36.241 1.00 19.07 ? 256 GLY A CA 1 ATOM 1646 C C . GLY A 1 263 ? 15.609 41.300 35.318 1.00 20.44 ? 256 GLY A C 1 ATOM 1647 O O . GLY A 1 263 ? 15.678 41.158 34.072 1.00 20.33 ? 256 GLY A O 1 ATOM 1648 N N . ASN A 1 264 ? 14.679 42.071 35.917 1.00 19.59 ? 257 ASN A N 1 ATOM 1649 C CA . ASN A 1 264 ? 13.687 42.752 35.075 1.00 20.17 ? 257 ASN A CA 1 ATOM 1650 C C . ASN A 1 264 ? 14.343 43.923 34.340 1.00 20.17 ? 257 ASN A C 1 ATOM 1651 O O . ASN A 1 264 ? 15.350 44.462 34.785 1.00 19.87 ? 257 ASN A O 1 ATOM 1652 C CB . ASN A 1 264 ? 12.459 43.205 35.888 1.00 19.50 ? 257 ASN A CB 1 ATOM 1653 C CG . ASN A 1 264 ? 12.676 44.571 36.612 1.00 21.31 ? 257 ASN A CG 1 ATOM 1654 O OD1 . ASN A 1 264 ? 12.658 45.636 35.981 1.00 21.77 ? 257 ASN A OD1 1 ATOM 1655 N ND2 . ASN A 1 264 ? 12.882 44.530 37.931 1.00 18.89 ? 257 ASN A ND2 1 ATOM 1656 N N . ILE A 1 265 ? 13.732 44.322 33.230 1.00 19.49 ? 258 ILE A N 1 ATOM 1657 C CA . ILE A 1 265 ? 14.272 45.367 32.385 1.00 20.73 ? 258 ILE A CA 1 ATOM 1658 C C . ILE A 1 265 ? 13.223 46.457 32.188 1.00 20.97 ? 258 ILE A C 1 ATOM 1659 O O . ILE A 1 265 ? 13.184 47.098 31.145 1.00 22.73 ? 258 ILE A O 1 ATOM 1660 C CB . ILE A 1 265 ? 14.710 44.782 31.010 1.00 21.57 ? 258 ILE A CB 1 ATOM 1661 C CG1 . ILE A 1 265 ? 13.562 43.925 30.413 1.00 21.43 ? 258 ILE A CG1 1 ATOM 1662 C CG2 . ILE A 1 265 ? 15.999 43.980 31.164 1.00 22.88 ? 258 ILE A CG2 1 ATOM 1663 C CD1 . ILE A 1 265 ? 13.794 43.444 28.920 1.00 27.24 ? 258 ILE A CD1 1 ATOM 1664 N N . LEU A 1 266 ? 12.362 46.650 33.198 1.00 20.88 ? 259 LEU A N 1 ATOM 1665 C CA . LEU A 1 266 ? 11.314 47.704 33.132 1.00 21.36 ? 259 LEU A CA 1 ATOM 1666 C C . LEU A 1 266 ? 11.897 49.106 33.322 1.00 21.91 ? 259 LEU A C 1 ATOM 1667 O O . LEU A 1 266 ? 12.970 49.243 33.861 1.00 21.71 ? 259 LEU A O 1 ATOM 1668 C CB . LEU A 1 266 ? 10.286 47.486 34.245 1.00 19.86 ? 259 LEU A CB 1 ATOM 1669 C CG . LEU A 1 266 ? 9.433 46.211 34.122 1.00 19.85 ? 259 LEU A CG 1 ATOM 1670 C CD1 . LEU A 1 266 ? 8.589 46.120 35.391 1.00 19.67 ? 259 LEU A CD1 1 ATOM 1671 C CD2 . LEU A 1 266 ? 8.519 46.257 32.870 1.00 21.41 ? 259 LEU A CD2 1 ATOM 1672 N N . ASN A 1 267 ? 11.150 50.127 32.884 1.00 21.38 ? 260 ASN A N 1 ATOM 1673 C CA . ASN A 1 267 ? 11.398 51.526 33.242 1.00 20.35 ? 260 ASN A CA 1 ATOM 1674 C C . ASN A 1 267 ? 10.157 52.099 33.854 1.00 20.53 ? 260 ASN A C 1 ATOM 1675 O O . ASN A 1 267 ? 9.426 52.863 33.212 1.00 20.16 ? 260 ASN A O 1 ATOM 1676 C CB . ASN A 1 267 ? 11.813 52.295 31.974 1.00 22.18 ? 260 ASN A CB 1 ATOM 1677 C CG . ASN A 1 267 ? 13.288 52.032 31.642 1.00 23.25 ? 260 ASN A CG 1 ATOM 1678 O OD1 . ASN A 1 267 ? 14.157 52.672 32.220 1.00 25.42 ? 260 ASN A OD1 1 ATOM 1679 N ND2 . ASN A 1 267 ? 13.564 51.043 30.776 1.00 23.85 ? 260 ASN A ND2 1 ATOM 1680 N N . LEU A 1 268 ? 9.889 51.704 35.099 1.00 19.60 ? 261 LEU A N 1 ATOM 1681 C CA . LEU A 1 268 ? 8.658 52.042 35.745 1.00 19.09 ? 261 LEU A CA 1 ATOM 1682 C C . LEU A 1 268 ? 8.656 53.464 36.316 1.00 18.90 ? 261 LEU A C 1 ATOM 1683 O O . LEU A 1 268 ? 7.590 54.038 36.528 1.00 16.00 ? 261 LEU A O 1 ATOM 1684 C CB . LEU A 1 268 ? 8.440 51.086 36.961 1.00 18.71 ? 261 LEU A CB 1 ATOM 1685 C CG . LEU A 1 268 ? 8.032 49.643 36.604 1.00 17.95 ? 261 LEU A CG 1 ATOM 1686 C CD1 . LEU A 1 268 ? 7.898 48.775 37.916 1.00 17.78 ? 261 LEU A CD1 1 ATOM 1687 C CD2 . LEU A 1 268 ? 6.705 49.676 35.784 1.00 19.02 ? 261 LEU A CD2 1 ATOM 1688 N N . ASN A 1 269 ? 9.829 54.031 36.596 1.00 17.71 ? 262 ASN A N 1 ATOM 1689 C CA . ASN A 1 269 ? 9.888 55.383 37.247 1.00 19.21 ? 262 ASN A CA 1 ATOM 1690 C C . ASN A 1 269 ? 8.978 55.512 38.481 1.00 19.82 ? 262 ASN A C 1 ATOM 1691 O O . ASN A 1 269 ? 8.298 56.548 38.693 1.00 19.40 ? 262 ASN A O 1 ATOM 1692 C CB . ASN A 1 269 ? 9.591 56.472 36.182 1.00 19.80 ? 262 ASN A CB 1 ATOM 1693 C CG . ASN A 1 269 ? 10.689 56.527 35.132 1.00 23.49 ? 262 ASN A CG 1 ATOM 1694 O OD1 . ASN A 1 269 ? 11.872 56.350 35.472 1.00 24.59 ? 262 ASN A OD1 1 ATOM 1695 N ND2 . ASN A 1 269 ? 10.321 56.765 33.882 1.00 22.42 ? 262 ASN A ND2 1 ATOM 1696 N N . GLY A 1 270 ? 8.975 54.469 39.315 1.00 17.69 ? 263 GLY A N 1 ATOM 1697 C CA . GLY A 1 270 ? 8.222 54.545 40.571 1.00 17.70 ? 263 GLY A CA 1 ATOM 1698 C C . GLY A 1 270 ? 6.743 54.145 40.455 1.00 18.76 ? 263 GLY A C 1 ATOM 1699 O O . GLY A 1 270 ? 6.010 54.214 41.450 1.00 19.26 ? 263 GLY A O 1 ATOM 1700 N N . ALA A 1 271 ? 6.294 53.659 39.290 1.00 18.17 ? 264 ALA A N 1 ATOM 1701 C CA . ALA A 1 271 ? 4.825 53.399 39.125 1.00 17.46 ? 264 ALA A CA 1 ATOM 1702 C C . ALA A 1 271 ? 4.284 52.194 39.885 1.00 17.17 ? 264 ALA A C 1 ATOM 1703 O O . ALA A 1 271 ? 3.095 52.177 40.213 1.00 18.02 ? 264 ALA A O 1 ATOM 1704 C CB . ALA A 1 271 ? 4.448 53.233 37.601 1.00 16.53 ? 264 ALA A CB 1 ATOM 1705 N N . GLY A 1 272 ? 5.116 51.206 40.177 1.00 16.32 ? 265 GLY A N 1 ATOM 1706 C CA . GLY A 1 272 ? 4.595 49.954 40.722 1.00 17.99 ? 265 GLY A CA 1 ATOM 1707 C C . GLY A 1 272 ? 4.103 49.017 39.633 1.00 19.29 ? 265 GLY A C 1 ATOM 1708 O O . GLY A 1 272 ? 4.629 49.043 38.513 1.00 19.60 ? 265 GLY A O 1 ATOM 1709 N N . ASP A 1 273 ? 3.044 48.248 39.910 1.00 17.73 ? 266 ASP A N 1 ATOM 1710 C CA . ASP A 1 273 ? 2.444 47.362 38.885 1.00 18.73 ? 266 ASP A CA 1 ATOM 1711 C C . ASP A 1 273 ? 2.151 48.113 37.592 1.00 19.86 ? 266 ASP A C 1 ATOM 1712 O O . ASP A 1 273 ? 1.487 49.131 37.632 1.00 18.13 ? 266 ASP A O 1 ATOM 1713 C CB . ASP A 1 273 ? 1.142 46.796 39.432 1.00 18.99 ? 266 ASP A CB 1 ATOM 1714 C CG . ASP A 1 273 ? 0.271 46.151 38.364 1.00 21.05 ? 266 ASP A CG 1 ATOM 1715 O OD1 . ASP A 1 273 ? 0.792 45.370 37.522 1.00 19.27 ? 266 ASP A OD1 1 ATOM 1716 O OD2 . ASP A 1 273 ? -0.958 46.430 38.390 1.00 20.36 ? 266 ASP A OD2 1 ATOM 1717 N N . PRO A 1 274 ? 2.686 47.632 36.443 1.00 20.49 ? 267 PRO A N 1 ATOM 1718 C CA . PRO A 1 274 ? 2.566 48.354 35.193 1.00 20.52 ? 267 PRO A CA 1 ATOM 1719 C C . PRO A 1 274 ? 1.074 48.664 34.822 1.00 20.75 ? 267 PRO A C 1 ATOM 1720 O O . PRO A 1 274 ? 0.768 49.643 34.108 1.00 21.17 ? 267 PRO A O 1 ATOM 1721 C CB . PRO A 1 274 ? 3.127 47.326 34.177 1.00 20.59 ? 267 PRO A CB 1 ATOM 1722 C CG . PRO A 1 274 ? 4.227 46.622 34.892 1.00 21.64 ? 267 PRO A CG 1 ATOM 1723 C CD . PRO A 1 274 ? 3.699 46.542 36.362 1.00 20.24 ? 267 PRO A CD 1 ATOM 1724 N N . LEU A 1 275 ? 0.170 47.841 35.313 1.00 19.56 ? 268 LEU A N 1 ATOM 1725 C CA . LEU A 1 275 ? -1.257 47.994 34.896 1.00 19.64 ? 268 LEU A CA 1 ATOM 1726 C C . LEU A 1 275 ? -2.113 48.931 35.783 1.00 18.14 ? 268 LEU A C 1 ATOM 1727 O O . LEU A 1 275 ? -3.238 49.302 35.381 1.00 19.32 ? 268 LEU A O 1 ATOM 1728 C CB . LEU A 1 275 ? -1.903 46.613 34.836 1.00 21.06 ? 268 LEU A CB 1 ATOM 1729 C CG . LEU A 1 275 ? -1.224 45.596 33.885 1.00 21.66 ? 268 LEU A CG 1 ATOM 1730 C CD1 . LEU A 1 275 ? -2.088 44.333 33.877 1.00 23.99 ? 268 LEU A CD1 1 ATOM 1731 C CD2 . LEU A 1 275 ? -0.979 46.138 32.442 1.00 22.28 ? 268 LEU A CD2 1 ATOM 1732 N N . THR A 1 276 ? -1.608 49.323 36.951 1.00 19.14 ? 269 THR A N 1 ATOM 1733 C CA . THR A 1 276 ? -2.462 50.067 37.931 1.00 17.62 ? 269 THR A CA 1 ATOM 1734 C C . THR A 1 276 ? -1.768 51.284 38.568 1.00 18.46 ? 269 THR A C 1 ATOM 1735 O O . THR A 1 276 ? -1.793 51.463 39.811 1.00 18.96 ? 269 THR A O 1 ATOM 1736 C CB . THR A 1 276 ? -2.929 49.122 39.103 1.00 18.26 ? 269 THR A CB 1 ATOM 1737 O OG1 . THR A 1 276 ? -1.759 48.527 39.694 1.00 16.90 ? 269 THR A OG1 1 ATOM 1738 C CG2 . THR A 1 276 ? -3.944 47.983 38.611 1.00 17.12 ? 269 THR A CG2 1 ATOM 1739 N N . PRO A 1 277 ? -1.088 52.121 37.755 1.00 19.56 ? 270 PRO A N 1 ATOM 1740 C CA . PRO A 1 277 ? -0.289 53.189 38.408 1.00 18.53 ? 270 PRO A CA 1 ATOM 1741 C C . PRO A 1 277 ? -1.213 54.155 39.180 1.00 18.31 ? 270 PRO A C 1 ATOM 1742 O O . PRO A 1 277 ? -2.247 54.588 38.634 1.00 18.34 ? 270 PRO A O 1 ATOM 1743 C CB . PRO A 1 277 ? 0.363 53.932 37.217 1.00 20.26 ? 270 PRO A CB 1 ATOM 1744 C CG . PRO A 1 277 ? -0.625 53.679 36.063 1.00 20.50 ? 270 PRO A CG 1 ATOM 1745 C CD . PRO A 1 277 ? -1.011 52.200 36.283 1.00 20.67 ? 270 PRO A CD 1 ATOM 1746 N N . GLY A 1 278 ? -0.864 54.420 40.437 1.00 18.78 ? 271 GLY A N 1 ATOM 1747 C CA . GLY A 1 278 ? -1.590 55.330 41.326 1.00 18.25 ? 271 GLY A CA 1 ATOM 1748 C C . GLY A 1 278 ? -2.431 54.629 42.370 1.00 18.58 ? 271 GLY A C 1 ATOM 1749 O O . GLY A 1 278 ? -2.778 55.239 43.373 1.00 19.46 ? 271 GLY A O 1 ATOM 1750 N N . TYR A 1 279 ? -2.828 53.369 42.098 1.00 17.86 ? 272 TYR A N 1 ATOM 1751 C CA . TYR A 1 279 ? -3.888 52.720 42.881 1.00 18.86 ? 272 TYR A CA 1 ATOM 1752 C C . TYR A 1 279 ? -3.490 51.265 43.176 1.00 17.42 ? 272 TYR A C 1 ATOM 1753 O O . TYR A 1 279 ? -2.827 50.626 42.344 1.00 17.62 ? 272 TYR A O 1 ATOM 1754 C CB . TYR A 1 279 ? -5.230 52.803 42.130 1.00 17.95 ? 272 TYR A CB 1 ATOM 1755 C CG . TYR A 1 279 ? -5.548 54.238 41.744 1.00 19.17 ? 272 TYR A CG 1 ATOM 1756 C CD1 . TYR A 1 279 ? -6.158 55.126 42.659 1.00 17.56 ? 272 TYR A CD1 1 ATOM 1757 C CD2 . TYR A 1 279 ? -5.168 54.742 40.490 1.00 17.17 ? 272 TYR A CD2 1 ATOM 1758 C CE1 . TYR A 1 279 ? -6.351 56.450 42.320 1.00 15.39 ? 272 TYR A CE1 1 ATOM 1759 C CE2 . TYR A 1 279 ? -5.349 56.059 40.159 1.00 19.32 ? 272 TYR A CE2 1 ATOM 1760 C CZ . TYR A 1 279 ? -5.975 56.912 41.055 1.00 18.11 ? 272 TYR A CZ 1 ATOM 1761 O OH . TYR A 1 279 ? -6.170 58.236 40.675 1.00 16.68 ? 272 TYR A OH 1 ATOM 1762 N N . PRO A 1 280 ? -3.908 50.707 44.343 1.00 18.55 ? 273 PRO A N 1 ATOM 1763 C CA . PRO A 1 280 ? -3.486 49.305 44.579 1.00 19.59 ? 273 PRO A CA 1 ATOM 1764 C C . PRO A 1 280 ? -4.191 48.325 43.618 1.00 19.84 ? 273 PRO A C 1 ATOM 1765 O O . PRO A 1 280 ? -5.387 48.486 43.297 1.00 19.79 ? 273 PRO A O 1 ATOM 1766 C CB . PRO A 1 280 ? -3.949 49.008 46.028 1.00 19.80 ? 273 PRO A CB 1 ATOM 1767 C CG . PRO A 1 280 ? -5.052 50.032 46.319 1.00 18.94 ? 273 PRO A CG 1 ATOM 1768 C CD . PRO A 1 280 ? -4.659 51.274 45.480 1.00 19.65 ? 273 PRO A CD 1 ATOM 1769 N N . ALA A 1 281 ? -3.456 47.301 43.199 1.00 18.52 ? 274 ALA A N 1 ATOM 1770 C CA . ALA A 1 281 ? -3.980 46.261 42.303 1.00 18.24 ? 274 ALA A CA 1 ATOM 1771 C C . ALA A 1 281 ? -4.828 45.272 43.139 1.00 19.76 ? 274 ALA A C 1 ATOM 1772 O O . ALA A 1 281 ? -4.503 44.080 43.304 1.00 19.28 ? 274 ALA A O 1 ATOM 1773 C CB . ALA A 1 281 ? -2.816 45.563 41.627 1.00 20.09 ? 274 ALA A CB 1 ATOM 1774 N N . ASN A 1 282 ? -5.943 45.797 43.654 1.00 21.43 ? 275 ASN A N 1 ATOM 1775 C CA . ASN A 1 282 ? -6.810 45.035 44.501 1.00 23.12 ? 275 ASN A CA 1 ATOM 1776 C C . ASN A 1 282 ? -7.813 44.224 43.654 1.00 25.43 ? 275 ASN A C 1 ATOM 1777 O O . ASN A 1 282 ? -7.684 44.149 42.425 1.00 24.80 ? 275 ASN A O 1 ATOM 1778 C CB . ASN A 1 282 ? -7.476 45.967 45.538 1.00 24.63 ? 275 ASN A CB 1 ATOM 1779 C CG . ASN A 1 282 ? -8.352 47.015 44.904 1.00 23.32 ? 275 ASN A CG 1 ATOM 1780 O OD1 . ASN A 1 282 ? -8.849 46.836 43.787 1.00 23.29 ? 275 ASN A OD1 1 ATOM 1781 N ND2 . ASN A 1 282 ? -8.502 48.156 45.595 1.00 26.07 ? 275 ASN A ND2 1 ATOM 1782 N N A GLU A 1 283 ? -8.820 43.630 44.291 0.50 27.03 ? 276 GLU A N 1 ATOM 1783 N N B GLU A 1 283 ? -8.812 43.652 44.328 0.50 26.79 ? 276 GLU A N 1 ATOM 1784 C CA A GLU A 1 283 ? -9.710 42.716 43.556 0.50 28.57 ? 276 GLU A CA 1 ATOM 1785 C CA B GLU A 1 283 ? -9.787 42.769 43.682 0.50 28.31 ? 276 GLU A CA 1 ATOM 1786 C C A GLU A 1 283 ? -10.746 43.384 42.649 0.50 28.82 ? 276 GLU A C 1 ATOM 1787 C C B GLU A 1 283 ? -10.483 43.465 42.513 0.50 28.36 ? 276 GLU A C 1 ATOM 1788 O O A GLU A 1 283 ? -11.401 42.684 41.847 0.50 29.76 ? 276 GLU A O 1 ATOM 1789 O O B GLU A 1 283 ? -10.619 42.890 41.406 0.50 28.74 ? 276 GLU A O 1 ATOM 1790 C CB A GLU A 1 283 ? -10.395 41.715 44.502 0.50 30.10 ? 276 GLU A CB 1 ATOM 1791 C CB B GLU A 1 283 ? -10.842 42.295 44.712 0.50 29.40 ? 276 GLU A CB 1 ATOM 1792 C CG A GLU A 1 283 ? -9.704 40.366 44.547 0.50 32.65 ? 276 GLU A CG 1 ATOM 1793 C CG B GLU A 1 283 ? -11.131 40.799 44.669 0.50 32.36 ? 276 GLU A CG 1 ATOM 1794 C CD A GLU A 1 283 ? -10.167 39.387 43.453 0.50 36.50 ? 276 GLU A CD 1 ATOM 1795 C CD B GLU A 1 283 ? -10.031 39.959 45.348 0.50 34.78 ? 276 GLU A CD 1 ATOM 1796 O OE1 A GLU A 1 283 ? -10.870 39.783 42.497 0.50 37.03 ? 276 GLU A OE1 1 ATOM 1797 O OE1 B GLU A 1 283 ? -9.526 40.366 46.418 0.50 36.30 ? 276 GLU A OE1 1 ATOM 1798 O OE2 A GLU A 1 283 ? -9.820 38.198 43.565 0.50 38.61 ? 276 GLU A OE2 1 ATOM 1799 O OE2 B GLU A 1 283 ? -9.667 38.880 44.816 0.50 34.62 ? 276 GLU A OE2 1 ATOM 1800 N N . TYR A 1 284 ? -10.905 44.704 42.752 1.00 27.42 ? 277 TYR A N 1 ATOM 1801 C CA . TYR A 1 284 ? -11.801 45.413 41.800 1.00 28.43 ? 277 TYR A CA 1 ATOM 1802 C C . TYR A 1 284 ? -11.054 46.416 40.932 1.00 27.86 ? 277 TYR A C 1 ATOM 1803 O O . TYR A 1 284 ? -11.679 47.188 40.245 1.00 29.55 ? 277 TYR A O 1 ATOM 1804 C CB . TYR A 1 284 ? -12.998 46.085 42.521 1.00 26.45 ? 277 TYR A CB 1 ATOM 1805 C CG . TYR A 1 284 ? -12.560 47.055 43.583 1.00 27.60 ? 277 TYR A CG 1 ATOM 1806 C CD1 . TYR A 1 284 ? -12.350 48.413 43.271 1.00 29.50 ? 277 TYR A CD1 1 ATOM 1807 C CD2 . TYR A 1 284 ? -12.313 46.617 44.908 1.00 26.29 ? 277 TYR A CD2 1 ATOM 1808 C CE1 . TYR A 1 284 ? -11.940 49.328 44.252 1.00 27.86 ? 277 TYR A CE1 1 ATOM 1809 C CE2 . TYR A 1 284 ? -11.877 47.506 45.865 1.00 29.06 ? 277 TYR A CE2 1 ATOM 1810 C CZ . TYR A 1 284 ? -11.684 48.869 45.516 1.00 28.84 ? 277 TYR A CZ 1 ATOM 1811 O OH . TYR A 1 284 ? -11.243 49.762 46.494 1.00 29.06 ? 277 TYR A OH 1 ATOM 1812 N N . ALA A 1 285 ? -9.725 46.382 40.942 1.00 27.75 ? 278 ALA A N 1 ATOM 1813 C CA . ALA A 1 285 ? -8.909 47.363 40.225 1.00 28.88 ? 278 ALA A CA 1 ATOM 1814 C C . ALA A 1 285 ? -9.232 47.394 38.723 1.00 28.91 ? 278 ALA A C 1 ATOM 1815 O O . ALA A 1 285 ? -9.543 46.335 38.135 1.00 31.34 ? 278 ALA A O 1 ATOM 1816 C CB . ALA A 1 285 ? -7.436 47.030 40.409 1.00 28.58 ? 278 ALA A CB 1 ATOM 1817 N N . TYR A 1 286 ? -9.273 48.583 38.134 1.00 28.03 ? 279 TYR A N 1 ATOM 1818 C CA . TYR A 1 286 ? -9.376 48.680 36.658 1.00 27.69 ? 279 TYR A CA 1 ATOM 1819 C C . TYR A 1 286 ? -7.958 48.679 36.149 1.00 27.69 ? 279 TYR A C 1 ATOM 1820 O O . TYR A 1 286 ? -7.085 49.349 36.710 1.00 27.99 ? 279 TYR A O 1 ATOM 1821 C CB . TYR A 1 286 ? -10.113 49.961 36.169 1.00 30.12 ? 279 TYR A CB 1 ATOM 1822 C CG A TYR A 1 286 ? -10.464 49.942 34.689 0.50 25.74 ? 279 TYR A CG 1 ATOM 1823 C CG B TYR A 1 286 ? -9.422 50.629 34.932 0.50 29.47 ? 279 TYR A CG 1 ATOM 1824 C CD1 A TYR A 1 286 ? -11.551 49.221 34.209 0.50 26.80 ? 279 TYR A CD1 1 ATOM 1825 C CD1 B TYR A 1 286 ? -10.058 50.685 33.708 0.50 30.87 ? 279 TYR A CD1 1 ATOM 1826 C CD2 A TYR A 1 286 ? -9.672 50.640 33.778 0.50 24.81 ? 279 TYR A CD2 1 ATOM 1827 C CD2 B TYR A 1 286 ? -8.130 51.150 35.011 0.50 30.56 ? 279 TYR A CD2 1 ATOM 1828 C CE1 A TYR A 1 286 ? -11.851 49.202 32.850 0.50 27.33 ? 279 TYR A CE1 1 ATOM 1829 C CE1 B TYR A 1 286 ? -9.453 51.262 32.597 0.50 31.76 ? 279 TYR A CE1 1 ATOM 1830 C CE2 A TYR A 1 286 ? -9.955 50.617 32.425 0.50 26.60 ? 279 TYR A CE2 1 ATOM 1831 C CE2 B TYR A 1 286 ? -7.493 51.738 33.890 0.50 31.50 ? 279 TYR A CE2 1 ATOM 1832 C CZ A TYR A 1 286 ? -11.033 49.910 31.973 0.50 28.42 ? 279 TYR A CZ 1 ATOM 1833 C CZ B TYR A 1 286 ? -8.177 51.785 32.685 0.50 32.46 ? 279 TYR A CZ 1 ATOM 1834 O OH A TYR A 1 286 ? -11.279 49.908 30.628 0.50 32.29 ? 279 TYR A OH 1 ATOM 1835 O OH B TYR A 1 286 ? -7.604 52.362 31.561 0.50 34.39 ? 279 TYR A OH 1 ATOM 1836 N N . ARG A 1 287 ? -7.688 47.856 35.157 1.00 24.18 ? 280 ARG A N 1 ATOM 1837 C CA . ARG A 1 287 ? -6.322 47.706 34.663 1.00 24.53 ? 280 ARG A CA 1 ATOM 1838 C C . ARG A 1 287 ? -6.182 48.369 33.317 1.00 25.13 ? 280 ARG A C 1 ATOM 1839 O O . ARG A 1 287 ? -7.090 48.284 32.484 1.00 23.83 ? 280 ARG A O 1 ATOM 1840 C CB A ARG A 1 287 ? -5.963 46.220 34.570 0.65 25.33 ? 280 ARG A CB 1 ATOM 1841 C CB B ARG A 1 287 ? -6.012 46.231 34.467 0.35 23.73 ? 280 ARG A CB 1 ATOM 1842 C CG A ARG A 1 287 ? -5.263 45.662 35.835 0.65 25.85 ? 280 ARG A CG 1 ATOM 1843 C CG B ARG A 1 287 ? -5.964 45.481 35.752 0.35 20.02 ? 280 ARG A CG 1 ATOM 1844 C CD A ARG A 1 287 ? -6.134 44.759 36.673 0.65 33.01 ? 280 ARG A CD 1 ATOM 1845 C CD B ARG A 1 287 ? -5.389 44.090 35.582 0.35 12.04 ? 280 ARG A CD 1 ATOM 1846 N NE A ARG A 1 287 ? -5.467 44.291 37.902 0.65 30.46 ? 280 ARG A NE 1 ATOM 1847 N NE B ARG A 1 287 ? -5.100 43.594 36.906 0.35 10.07 ? 280 ARG A NE 1 ATOM 1848 C CZ A ARG A 1 287 ? -6.125 43.960 39.008 0.65 31.81 ? 280 ARG A CZ 1 ATOM 1849 C CZ B ARG A 1 287 ? -6.029 43.219 37.776 0.35 10.06 ? 280 ARG A CZ 1 ATOM 1850 N NH1 A ARG A 1 287 ? -7.462 44.049 39.047 0.65 34.11 ? 280 ARG A NH1 1 ATOM 1851 N NH1 B ARG A 1 287 ? -7.297 43.255 37.436 0.35 10.91 ? 280 ARG A NH1 1 ATOM 1852 N NH2 A ARG A 1 287 ? -5.470 43.556 40.080 0.65 28.10 ? 280 ARG A NH2 1 ATOM 1853 N NH2 B ARG A 1 287 ? -5.689 42.816 38.998 0.35 10.98 ? 280 ARG A NH2 1 ATOM 1854 N N . ARG A 1 288 ? -5.060 49.037 33.093 1.00 24.07 ? 281 ARG A N 1 ATOM 1855 C CA . ARG A 1 288 ? -4.744 49.470 31.735 1.00 26.76 ? 281 ARG A CA 1 ATOM 1856 C C . ARG A 1 288 ? -4.620 48.243 30.843 1.00 28.18 ? 281 ARG A C 1 ATOM 1857 O O . ARG A 1 288 ? -4.256 47.141 31.313 1.00 26.92 ? 281 ARG A O 1 ATOM 1858 C CB . ARG A 1 288 ? -3.417 50.190 31.703 1.00 25.56 ? 281 ARG A CB 1 ATOM 1859 C CG . ARG A 1 288 ? -3.452 51.495 32.471 1.00 27.37 ? 281 ARG A CG 1 ATOM 1860 C CD . ARG A 1 288 ? -2.137 52.193 32.321 1.00 28.95 ? 281 ARG A CD 1 ATOM 1861 N NE . ARG A 1 288 ? -2.242 53.523 32.911 1.00 30.89 ? 281 ARG A NE 1 ATOM 1862 C CZ . ARG A 1 288 ? -1.430 54.533 32.645 1.00 31.09 ? 281 ARG A CZ 1 ATOM 1863 N NH1 . ARG A 1 288 ? -0.468 54.398 31.756 1.00 32.49 ? 281 ARG A NH1 1 ATOM 1864 N NH2 . ARG A 1 288 ? -1.585 55.672 33.294 1.00 31.88 ? 281 ARG A NH2 1 ATOM 1865 N N . GLY A 1 289 ? -4.930 48.432 29.563 1.00 29.24 ? 282 GLY A N 1 ATOM 1866 C CA . GLY A 1 289 ? -4.587 47.407 28.582 1.00 32.05 ? 282 GLY A CA 1 ATOM 1867 C C . GLY A 1 289 ? -3.076 47.376 28.440 1.00 31.94 ? 282 GLY A C 1 ATOM 1868 O O . GLY A 1 289 ? -2.386 48.361 28.753 1.00 31.75 ? 282 GLY A O 1 ATOM 1869 N N . ILE A 1 290 ? -2.551 46.251 27.980 1.00 33.29 ? 283 ILE A N 1 ATOM 1870 C CA . ILE A 1 290 ? -1.088 46.055 27.841 1.00 33.71 ? 283 ILE A CA 1 ATOM 1871 C C . ILE A 1 290 ? -0.411 47.148 27.018 1.00 34.43 ? 283 ILE A C 1 ATOM 1872 O O . ILE A 1 290 ? 0.685 47.581 27.361 1.00 34.60 ? 283 ILE A O 1 ATOM 1873 C CB A ILE A 1 290 ? -0.772 44.613 27.311 0.65 34.90 ? 283 ILE A CB 1 ATOM 1874 C CB B ILE A 1 290 ? -0.689 44.678 27.225 0.35 34.36 ? 283 ILE A CB 1 ATOM 1875 C CG1 A ILE A 1 290 ? 0.626 44.146 27.724 0.65 35.33 ? 283 ILE A CG1 1 ATOM 1876 C CG1 B ILE A 1 290 ? -0.862 43.542 28.234 0.35 33.14 ? 283 ILE A CG1 1 ATOM 1877 C CG2 A ILE A 1 290 ? -1.026 44.490 25.784 0.65 35.94 ? 283 ILE A CG2 1 ATOM 1878 C CG2 B ILE A 1 290 ? 0.774 44.703 26.699 0.35 33.34 ? 283 ILE A CG2 1 ATOM 1879 C CD1 A ILE A 1 290 ? 0.764 43.905 29.222 0.65 33.44 ? 283 ILE A CD1 1 ATOM 1880 C CD1 B ILE A 1 290 ? 0.193 43.531 29.332 0.35 33.42 ? 283 ILE A CD1 1 ATOM 1881 N N . ALA A 1 291 ? -1.061 47.617 25.952 1.00 35.83 ? 284 ALA A N 1 ATOM 1882 C CA . ALA A 1 291 ? -0.479 48.674 25.119 1.00 36.14 ? 284 ALA A CA 1 ATOM 1883 C C . ALA A 1 291 ? -0.252 49.968 25.867 1.00 36.09 ? 284 ALA A C 1 ATOM 1884 O O . ALA A 1 291 ? 0.637 50.727 25.488 1.00 36.29 ? 284 ALA A O 1 ATOM 1885 C CB . ALA A 1 291 ? -1.335 48.934 23.841 1.00 38.21 ? 284 ALA A CB 1 ATOM 1886 N N . GLU A 1 292 ? -1.026 50.222 26.939 1.00 35.36 ? 285 GLU A N 1 ATOM 1887 C CA . GLU A 1 292 ? -0.864 51.437 27.747 1.00 34.29 ? 285 GLU A CA 1 ATOM 1888 C C . GLU A 1 292 ? -0.120 51.166 29.096 1.00 32.30 ? 285 GLU A C 1 ATOM 1889 O O . GLU A 1 292 ? -0.005 52.085 29.915 1.00 32.50 ? 285 GLU A O 1 ATOM 1890 C CB . GLU A 1 292 ? -2.213 52.144 28.012 1.00 34.60 ? 285 GLU A CB 1 ATOM 1891 C CG . GLU A 1 292 ? -2.949 52.752 26.765 1.00 39.17 ? 285 GLU A CG 1 ATOM 1892 C CD . GLU A 1 292 ? -3.492 51.696 25.797 1.00 47.96 ? 285 GLU A CD 1 ATOM 1893 O OE1 . GLU A 1 292 ? -4.069 50.680 26.252 1.00 49.24 ? 285 GLU A OE1 1 ATOM 1894 O OE2 . GLU A 1 292 ? -3.346 51.872 24.558 1.00 53.62 ? 285 GLU A OE2 1 ATOM 1895 N N . ALA A 1 293 ? 0.351 49.928 29.310 1.00 31.03 ? 286 ALA A N 1 ATOM 1896 C CA . ALA A 1 293 ? 1.071 49.563 30.550 1.00 30.33 ? 286 ALA A CA 1 ATOM 1897 C C . ALA A 1 293 ? 2.295 50.467 30.713 1.00 30.44 ? 286 ALA A C 1 ATOM 1898 O O . ALA A 1 293 ? 2.830 50.990 29.720 1.00 29.95 ? 286 ALA A O 1 ATOM 1899 C CB . ALA A 1 293 ? 1.477 48.111 30.568 1.00 29.71 ? 286 ALA A CB 1 ATOM 1900 N N . VAL A 1 294 ? 2.705 50.671 31.967 1.00 27.89 ? 287 VAL A N 1 ATOM 1901 C CA . VAL A 1 294 ? 3.856 51.517 32.228 1.00 27.55 ? 287 VAL A CA 1 ATOM 1902 C C . VAL A 1 294 ? 5.149 50.707 32.146 1.00 26.40 ? 287 VAL A C 1 ATOM 1903 O O . VAL A 1 294 ? 5.254 49.640 32.778 1.00 25.85 ? 287 VAL A O 1 ATOM 1904 C CB . VAL A 1 294 ? 3.788 52.179 33.633 1.00 26.26 ? 287 VAL A CB 1 ATOM 1905 C CG1 . VAL A 1 294 ? 5.068 53.009 33.894 1.00 25.20 ? 287 VAL A CG1 1 ATOM 1906 C CG2 . VAL A 1 294 ? 2.519 53.051 33.744 1.00 27.79 ? 287 VAL A CG2 1 ATOM 1907 N N . GLY A 1 295 ? 6.108 51.213 31.382 1.00 26.17 ? 288 GLY A N 1 ATOM 1908 C CA . GLY A 1 295 ? 7.506 50.796 31.515 1.00 25.86 ? 288 GLY A CA 1 ATOM 1909 C C . GLY A 1 295 ? 7.981 49.531 30.822 1.00 26.38 ? 288 GLY A C 1 ATOM 1910 O O . GLY A 1 295 ? 9.136 49.124 31.023 1.00 25.79 ? 288 GLY A O 1 ATOM 1911 N N . LEU A 1 296 ? 7.122 48.919 30.012 1.00 24.94 ? 289 LEU A N 1 ATOM 1912 C CA . LEU A 1 296 ? 7.508 47.722 29.227 1.00 26.87 ? 289 LEU A CA 1 ATOM 1913 C C . LEU A 1 296 ? 8.438 48.032 28.066 1.00 26.74 ? 289 LEU A C 1 ATOM 1914 O O . LEU A 1 296 ? 8.237 49.006 27.342 1.00 26.62 ? 289 LEU A O 1 ATOM 1915 C CB . LEU A 1 296 ? 6.273 46.993 28.670 1.00 27.76 ? 289 LEU A CB 1 ATOM 1916 C CG . LEU A 1 296 ? 5.406 46.079 29.577 1.00 30.00 ? 289 LEU A CG 1 ATOM 1917 C CD1 . LEU A 1 296 ? 5.216 46.500 30.998 1.00 35.63 ? 289 LEU A CD1 1 ATOM 1918 C CD2 . LEU A 1 296 ? 4.029 45.825 28.892 1.00 34.47 ? 289 LEU A CD2 1 ATOM 1919 N N . PRO A 1 297 ? 9.449 47.182 27.861 1.00 27.47 ? 290 PRO A N 1 ATOM 1920 C CA . PRO A 1 297 ? 10.345 47.345 26.707 1.00 28.59 ? 290 PRO A CA 1 ATOM 1921 C C . PRO A 1 297 ? 9.630 46.970 25.413 1.00 29.97 ? 290 PRO A C 1 ATOM 1922 O O . PRO A 1 297 ? 8.744 46.109 25.412 1.00 29.67 ? 290 PRO A O 1 ATOM 1923 C CB . PRO A 1 297 ? 11.499 46.367 27.003 1.00 29.03 ? 290 PRO A CB 1 ATOM 1924 C CG . PRO A 1 297 ? 10.927 45.333 27.913 1.00 29.00 ? 290 PRO A CG 1 ATOM 1925 C CD . PRO A 1 297 ? 9.739 45.962 28.644 1.00 27.58 ? 290 PRO A CD 1 ATOM 1926 N N . SER A 1 298 ? 10.032 47.598 24.318 1.00 30.54 ? 291 SER A N 1 ATOM 1927 C CA . SER A 1 298 ? 9.393 47.340 23.037 1.00 32.39 ? 291 SER A CA 1 ATOM 1928 C C . SER A 1 298 ? 10.202 46.393 22.139 1.00 31.54 ? 291 SER A C 1 ATOM 1929 O O . SER A 1 298 ? 9.744 46.022 21.042 1.00 31.69 ? 291 SER A O 1 ATOM 1930 C CB . SER A 1 298 ? 9.106 48.670 22.343 1.00 33.69 ? 291 SER A CB 1 ATOM 1931 O OG . SER A 1 298 ? 10.345 49.257 21.910 1.00 38.36 ? 291 SER A OG 1 ATOM 1932 N N . ILE A 1 299 ? 11.398 46.007 22.595 1.00 30.32 ? 292 ILE A N 1 ATOM 1933 C CA . ILE A 1 299 ? 12.272 45.073 21.837 1.00 29.98 ? 292 ILE A CA 1 ATOM 1934 C C . ILE A 1 299 ? 12.666 43.872 22.701 1.00 29.45 ? 292 ILE A C 1 ATOM 1935 O O . ILE A 1 299 ? 12.739 43.995 23.926 1.00 28.96 ? 292 ILE A O 1 ATOM 1936 C CB . ILE A 1 299 ? 13.528 45.776 21.273 1.00 29.74 ? 292 ILE A CB 1 ATOM 1937 C CG1 . ILE A 1 299 ? 14.338 46.472 22.388 1.00 28.72 ? 292 ILE A CG1 1 ATOM 1938 C CG2 . ILE A 1 299 ? 13.130 46.770 20.208 1.00 31.22 ? 292 ILE A CG2 1 ATOM 1939 C CD1 . ILE A 1 299 ? 15.628 47.131 21.868 1.00 29.01 ? 292 ILE A CD1 1 ATOM 1940 N N . PRO A 1 300 ? 12.859 42.687 22.093 1.00 29.50 ? 293 PRO A N 1 ATOM 1941 C CA . PRO A 1 300 ? 13.238 41.523 22.903 1.00 29.04 ? 293 PRO A CA 1 ATOM 1942 C C . PRO A 1 300 ? 14.633 41.678 23.525 1.00 28.65 ? 293 PRO A C 1 ATOM 1943 O O . PRO A 1 300 ? 15.518 42.324 22.918 1.00 28.70 ? 293 PRO A O 1 ATOM 1944 C CB . PRO A 1 300 ? 13.301 40.377 21.871 1.00 30.84 ? 293 PRO A CB 1 ATOM 1945 C CG . PRO A 1 300 ? 12.442 40.850 20.731 1.00 30.82 ? 293 PRO A CG 1 ATOM 1946 C CD . PRO A 1 300 ? 12.702 42.328 20.671 1.00 30.83 ? 293 PRO A CD 1 ATOM 1947 N N . VAL A 1 301 ? 14.812 41.055 24.698 1.00 26.96 ? 294 VAL A N 1 ATOM 1948 C CA . VAL A 1 301 ? 16.034 41.188 25.501 1.00 26.64 ? 294 VAL A CA 1 ATOM 1949 C C . VAL A 1 301 ? 16.292 39.830 26.165 1.00 26.55 ? 294 VAL A C 1 ATOM 1950 O O . VAL A 1 301 ? 15.345 39.151 26.596 1.00 26.15 ? 294 VAL A O 1 ATOM 1951 C CB . VAL A 1 301 ? 15.866 42.230 26.644 1.00 25.64 ? 294 VAL A CB 1 ATOM 1952 C CG1 . VAL A 1 301 ? 17.178 42.365 27.475 1.00 24.92 ? 294 VAL A CG1 1 ATOM 1953 C CG2 . VAL A 1 301 ? 15.360 43.604 26.126 1.00 25.70 ? 294 VAL A CG2 1 ATOM 1954 N N . HIS A 1 302 ? 17.560 39.432 26.266 1.00 26.24 ? 295 HIS A N 1 ATOM 1955 C CA . HIS A 1 302 ? 17.895 38.146 26.893 1.00 26.08 ? 295 HIS A CA 1 ATOM 1956 C C . HIS A 1 302 ? 19.320 38.202 27.451 1.00 26.17 ? 295 HIS A C 1 ATOM 1957 O O . HIS A 1 302 ? 20.199 38.820 26.802 1.00 25.43 ? 295 HIS A O 1 ATOM 1958 C CB . HIS A 1 302 ? 17.743 37.011 25.833 1.00 26.77 ? 295 HIS A CB 1 ATOM 1959 C CG . HIS A 1 302 ? 17.808 35.611 26.402 1.00 26.34 ? 295 HIS A CG 1 ATOM 1960 N ND1 . HIS A 1 302 ? 16.857 35.110 27.260 1.00 26.07 ? 295 HIS A ND1 1 ATOM 1961 C CD2 . HIS A 1 302 ? 18.720 34.619 26.246 1.00 26.77 ? 295 HIS A CD2 1 ATOM 1962 C CE1 . HIS A 1 302 ? 17.174 33.879 27.620 1.00 26.86 ? 295 HIS A CE1 1 ATOM 1963 N NE2 . HIS A 1 302 ? 18.297 33.548 27.009 1.00 26.17 ? 295 HIS A NE2 1 ATOM 1964 N N . PRO A 1 303 ? 19.553 37.624 28.662 1.00 25.14 ? 296 PRO A N 1 ATOM 1965 C CA . PRO A 1 303 ? 20.909 37.649 29.190 1.00 24.84 ? 296 PRO A CA 1 ATOM 1966 C C . PRO A 1 303 ? 21.610 36.327 29.007 1.00 26.21 ? 296 PRO A C 1 ATOM 1967 O O . PRO A 1 303 ? 20.955 35.279 28.945 1.00 27.10 ? 296 PRO A O 1 ATOM 1968 C CB . PRO A 1 303 ? 20.691 37.911 30.696 1.00 24.67 ? 296 PRO A CB 1 ATOM 1969 C CG . PRO A 1 303 ? 19.326 37.165 30.991 1.00 24.73 ? 296 PRO A CG 1 ATOM 1970 C CD . PRO A 1 303 ? 18.596 37.032 29.629 1.00 22.62 ? 296 PRO A CD 1 ATOM 1971 N N . ILE A 1 304 ? 22.946 36.383 28.925 1.00 26.39 ? 297 ILE A N 1 ATOM 1972 C CA . ILE A 1 304 ? 23.776 35.208 28.731 1.00 26.58 ? 297 ILE A CA 1 ATOM 1973 C C . ILE A 1 304 ? 25.057 35.319 29.584 1.00 26.94 ? 297 ILE A C 1 ATOM 1974 O O . ILE A 1 304 ? 25.418 36.426 30.062 1.00 26.18 ? 297 ILE A O 1 ATOM 1975 C CB . ILE A 1 304 ? 24.181 35.004 27.214 1.00 27.46 ? 297 ILE A CB 1 ATOM 1976 C CG1 . ILE A 1 304 ? 25.032 36.186 26.656 1.00 27.17 ? 297 ILE A CG1 1 ATOM 1977 C CG2 . ILE A 1 304 ? 22.937 34.696 26.315 1.00 26.83 ? 297 ILE A CG2 1 ATOM 1978 C CD1 . ILE A 1 304 ? 25.523 35.958 25.202 1.00 28.02 ? 297 ILE A CD1 1 ATOM 1979 N N . GLY A 1 305 ? 25.754 34.190 29.724 1.00 28.09 ? 298 GLY A N 1 ATOM 1980 C CA . GLY A 1 305 ? 27.073 34.145 30.403 1.00 28.46 ? 298 GLY A CA 1 ATOM 1981 C C . GLY A 1 305 ? 28.226 34.390 29.446 1.00 29.95 ? 298 GLY A C 1 ATOM 1982 O O . GLY A 1 305 ? 28.025 34.582 28.235 1.00 29.91 ? 298 GLY A O 1 ATOM 1983 N N . TYR A 1 306 ? 29.439 34.415 29.987 1.00 30.44 ? 299 TYR A N 1 ATOM 1984 C CA . TYR A 1 306 ? 30.579 34.814 29.171 1.00 31.48 ? 299 TYR A CA 1 ATOM 1985 C C . TYR A 1 306 ? 31.108 33.712 28.231 1.00 33.16 ? 299 TYR A C 1 ATOM 1986 O O . TYR A 1 306 ? 31.817 34.024 27.242 1.00 33.58 ? 299 TYR A O 1 ATOM 1987 C CB . TYR A 1 306 ? 31.678 35.486 29.999 1.00 31.59 ? 299 TYR A CB 1 ATOM 1988 C CG . TYR A 1 306 ? 32.266 34.724 31.178 1.00 29.27 ? 299 TYR A CG 1 ATOM 1989 C CD1 . TYR A 1 306 ? 31.850 35.005 32.492 1.00 32.84 ? 299 TYR A CD1 1 ATOM 1990 C CD2 . TYR A 1 306 ? 33.307 33.807 30.997 1.00 33.92 ? 299 TYR A CD2 1 ATOM 1991 C CE1 . TYR A 1 306 ? 32.402 34.337 33.586 1.00 31.76 ? 299 TYR A CE1 1 ATOM 1992 C CE2 . TYR A 1 306 ? 33.875 33.144 32.092 1.00 34.58 ? 299 TYR A CE2 1 ATOM 1993 C CZ . TYR A 1 306 ? 33.405 33.422 33.378 1.00 32.09 ? 299 TYR A CZ 1 ATOM 1994 O OH . TYR A 1 306 ? 33.947 32.780 34.477 1.00 31.55 ? 299 TYR A OH 1 ATOM 1995 N N . TYR A 1 307 ? 30.770 32.445 28.485 1.00 33.09 ? 300 TYR A N 1 ATOM 1996 C CA . TYR A 1 307 ? 31.121 31.407 27.475 1.00 34.27 ? 300 TYR A CA 1 ATOM 1997 C C . TYR A 1 307 ? 30.352 31.636 26.170 1.00 34.18 ? 300 TYR A C 1 ATOM 1998 O O . TYR A 1 307 ? 30.914 31.520 25.064 1.00 34.58 ? 300 TYR A O 1 ATOM 1999 C CB . TYR A 1 307 ? 30.807 29.985 27.954 1.00 34.42 ? 300 TYR A CB 1 ATOM 2000 C CG . TYR A 1 307 ? 31.721 29.401 28.999 1.00 37.33 ? 300 TYR A CG 1 ATOM 2001 C CD1 . TYR A 1 307 ? 33.037 29.856 29.156 1.00 37.44 ? 300 TYR A CD1 1 ATOM 2002 C CD2 . TYR A 1 307 ? 31.276 28.349 29.814 1.00 37.86 ? 300 TYR A CD2 1 ATOM 2003 C CE1 . TYR A 1 307 ? 33.873 29.301 30.098 1.00 39.22 ? 300 TYR A CE1 1 ATOM 2004 C CE2 . TYR A 1 307 ? 32.116 27.758 30.747 1.00 38.92 ? 300 TYR A CE2 1 ATOM 2005 C CZ . TYR A 1 307 ? 33.417 28.240 30.884 1.00 40.23 ? 300 TYR A CZ 1 ATOM 2006 O OH . TYR A 1 307 ? 34.250 27.682 31.828 1.00 43.09 ? 300 TYR A OH 1 ATOM 2007 N N . ASP A 1 308 ? 29.058 31.924 26.316 1.00 32.64 ? 301 ASP A N 1 ATOM 2008 C CA . ASP A 1 308 ? 28.175 32.200 25.191 1.00 33.25 ? 301 ASP A CA 1 ATOM 2009 C C . ASP A 1 308 ? 28.476 33.555 24.550 1.00 33.60 ? 301 ASP A C 1 ATOM 2010 O O . ASP A 1 308 ? 28.438 33.694 23.317 1.00 34.39 ? 301 ASP A O 1 ATOM 2011 C CB . ASP A 1 308 ? 26.705 32.164 25.654 1.00 31.25 ? 301 ASP A CB 1 ATOM 2012 C CG . ASP A 1 308 ? 26.178 30.729 25.825 1.00 32.06 ? 301 ASP A CG 1 ATOM 2013 O OD1 . ASP A 1 308 ? 26.800 29.808 25.289 1.00 36.42 ? 301 ASP A OD1 1 ATOM 2014 O OD2 . ASP A 1 308 ? 25.098 30.512 26.447 1.00 35.03 ? 301 ASP A OD2 1 ATOM 2015 N N . ALA A 1 309 ? 28.765 34.557 25.388 1.00 33.49 ? 302 ALA A N 1 ATOM 2016 C CA . ALA A 1 309 ? 29.104 35.883 24.896 1.00 33.33 ? 302 ALA A CA 1 ATOM 2017 C C . ALA A 1 309 ? 30.337 35.848 24.020 1.00 35.03 ? 302 ALA A C 1 ATOM 2018 O O . ALA A 1 309 ? 30.361 36.472 22.974 1.00 36.44 ? 302 ALA A O 1 ATOM 2019 C CB . ALA A 1 309 ? 29.320 36.842 26.045 1.00 32.75 ? 302 ALA A CB 1 ATOM 2020 N N . GLN A 1 310 ? 31.363 35.139 24.475 1.00 35.12 ? 303 GLN A N 1 ATOM 2021 C CA . GLN A 1 310 ? 32.598 34.971 23.697 1.00 37.62 ? 303 GLN A CA 1 ATOM 2022 C C . GLN A 1 310 ? 32.337 34.442 22.270 1.00 38.60 ? 303 GLN A C 1 ATOM 2023 O O . GLN A 1 310 ? 32.947 34.914 21.283 1.00 39.47 ? 303 GLN A O 1 ATOM 2024 C CB . GLN A 1 310 ? 33.572 34.065 24.447 1.00 37.34 ? 303 GLN A CB 1 ATOM 2025 C CG . GLN A 1 310 ? 34.793 33.747 23.556 1.00 42.35 ? 303 GLN A CG 1 ATOM 2026 C CD . GLN A 1 310 ? 36.118 33.576 24.291 1.00 48.45 ? 303 GLN A CD 1 ATOM 2027 O OE1 . GLN A 1 310 ? 37.136 33.273 23.659 1.00 52.91 ? 303 GLN A OE1 1 ATOM 2028 N NE2 . GLN A 1 310 ? 36.118 33.741 25.604 1.00 46.46 ? 303 GLN A NE2 1 ATOM 2029 N N . LYS A 1 311 ? 31.420 33.486 22.160 1.00 39.09 ? 304 LYS A N 1 ATOM 2030 C CA . LYS A 1 311 ? 31.034 32.928 20.872 1.00 40.54 ? 304 LYS A CA 1 ATOM 2031 C C . LYS A 1 311 ? 30.362 33.972 19.989 1.00 41.05 ? 304 LYS A C 1 ATOM 2032 O O . LYS A 1 311 ? 30.503 33.930 18.760 1.00 42.29 ? 304 LYS A O 1 ATOM 2033 C CB . LYS A 1 311 ? 30.104 31.726 21.058 1.00 40.80 ? 304 LYS A CB 1 ATOM 2034 C CG . LYS A 1 311 ? 30.778 30.534 21.666 1.00 42.16 ? 304 LYS A CG 1 ATOM 2035 C CD . LYS A 1 311 ? 31.752 29.922 20.662 1.00 48.33 ? 304 LYS A CD 1 ATOM 2036 C CE . LYS A 1 311 ? 32.984 29.488 21.406 1.00 52.46 ? 304 LYS A CE 1 ATOM 2037 N NZ . LYS A 1 311 ? 32.980 28.011 21.644 1.00 57.32 ? 304 LYS A NZ 1 ATOM 2038 N N . LEU A 1 312 ? 29.630 34.899 20.606 1.00 39.07 ? 305 LEU A N 1 ATOM 2039 C CA . LEU A 1 312 ? 28.961 35.953 19.847 1.00 39.81 ? 305 LEU A CA 1 ATOM 2040 C C . LEU A 1 312 ? 29.874 37.120 19.487 1.00 39.84 ? 305 LEU A C 1 ATOM 2041 O O . LEU A 1 312 ? 29.697 37.734 18.429 1.00 41.72 ? 305 LEU A O 1 ATOM 2042 C CB . LEU A 1 312 ? 27.720 36.485 20.583 1.00 36.59 ? 305 LEU A CB 1 ATOM 2043 C CG . LEU A 1 312 ? 26.554 35.536 20.891 1.00 37.35 ? 305 LEU A CG 1 ATOM 2044 C CD1 . LEU A 1 312 ? 25.368 36.264 21.591 1.00 36.58 ? 305 LEU A CD1 1 ATOM 2045 C CD2 . LEU A 1 312 ? 26.059 34.781 19.671 1.00 34.27 ? 305 LEU A CD2 1 ATOM 2046 N N . LEU A 1 313 ? 30.829 37.421 20.363 1.00 38.73 ? 306 LEU A N 1 ATOM 2047 C CA . LEU A 1 313 ? 31.731 38.551 20.174 1.00 38.92 ? 306 LEU A CA 1 ATOM 2048 C C . LEU A 1 313 ? 32.936 38.236 19.299 1.00 40.49 ? 306 LEU A C 1 ATOM 2049 O O . LEU A 1 313 ? 33.523 39.134 18.684 1.00 40.60 ? 306 LEU A O 1 ATOM 2050 C CB . LEU A 1 313 ? 32.257 39.010 21.503 1.00 37.39 ? 306 LEU A CB 1 ATOM 2051 C CG . LEU A 1 313 ? 31.188 39.590 22.450 1.00 35.92 ? 306 LEU A CG 1 ATOM 2052 C CD1 . LEU A 1 313 ? 31.765 39.661 23.867 1.00 36.47 ? 306 LEU A CD1 1 ATOM 2053 C CD2 . LEU A 1 313 ? 30.641 40.955 21.985 1.00 35.85 ? 306 LEU A CD2 1 ATOM 2054 N N . GLU A 1 314 ? 33.342 36.977 19.276 1.00 41.79 ? 307 GLU A N 1 ATOM 2055 C CA . GLU A 1 314 ? 34.654 36.648 18.692 1.00 43.69 ? 307 GLU A CA 1 ATOM 2056 C C . GLU A 1 314 ? 34.740 36.940 17.193 1.00 45.19 ? 307 GLU A C 1 ATOM 2057 O O . GLU A 1 314 ? 35.829 37.219 16.645 1.00 46.37 ? 307 GLU A O 1 ATOM 2058 C CB . GLU A 1 314 ? 35.036 35.209 19.021 1.00 44.01 ? 307 GLU A CB 1 ATOM 2059 C CG . GLU A 1 314 ? 34.116 34.182 18.439 1.00 46.45 ? 307 GLU A CG 1 ATOM 2060 C CD . GLU A 1 314 ? 34.525 32.767 18.789 1.00 50.31 ? 307 GLU A CD 1 ATOM 2061 O OE1 . GLU A 1 314 ? 35.430 32.576 19.638 1.00 51.57 ? 307 GLU A OE1 1 ATOM 2062 O OE2 . GLU A 1 314 ? 33.918 31.847 18.210 1.00 52.05 ? 307 GLU A OE2 1 ATOM 2063 N N . LYS A 1 315 ? 33.598 36.868 16.522 1.00 45.25 ? 308 LYS A N 1 ATOM 2064 C CA . LYS A 1 315 ? 33.577 37.057 15.077 1.00 46.65 ? 308 LYS A CA 1 ATOM 2065 C C . LYS A 1 315 ? 33.278 38.510 14.685 1.00 46.58 ? 308 LYS A C 1 ATOM 2066 O O . LYS A 1 315 ? 33.198 38.825 13.500 1.00 46.75 ? 308 LYS A O 1 ATOM 2067 C CB . LYS A 1 315 ? 32.539 36.122 14.447 1.00 47.54 ? 308 LYS A CB 1 ATOM 2068 C CG . LYS A 1 315 ? 32.975 34.645 14.330 1.00 49.88 ? 308 LYS A CG 1 ATOM 2069 C CD . LYS A 1 315 ? 31.760 33.746 14.069 1.00 52.33 ? 308 LYS A CD 1 ATOM 2070 C CE . LYS A 1 315 ? 32.169 32.347 13.606 1.00 54.73 ? 308 LYS A CE 1 ATOM 2071 N NZ . LYS A 1 315 ? 30.956 31.543 13.268 1.00 54.46 ? 308 LYS A NZ 1 ATOM 2072 N N . MET A 1 316 ? 33.091 39.389 15.679 1.00 45.07 ? 309 MET A N 1 ATOM 2073 C CA . MET A 1 316 ? 32.751 40.799 15.399 1.00 45.41 ? 309 MET A CA 1 ATOM 2074 C C . MET A 1 316 ? 33.780 41.609 14.593 1.00 46.47 ? 309 MET A C 1 ATOM 2075 O O . MET A 1 316 ? 34.963 41.604 14.903 1.00 47.26 ? 309 MET A O 1 ATOM 2076 C CB . MET A 1 316 ? 32.376 41.530 16.680 1.00 43.75 ? 309 MET A CB 1 ATOM 2077 C CG A MET A 1 316 ? 30.951 41.091 17.042 0.50 41.87 ? 309 MET A CG 1 ATOM 2078 C CG B MET A 1 316 ? 31.149 41.038 17.386 0.50 44.69 ? 309 MET A CG 1 ATOM 2079 S SD A MET A 1 316 ? 30.023 42.021 18.250 0.50 37.14 ? 309 MET A SD 1 ATOM 2080 S SD B MET A 1 316 ? 29.747 41.721 16.549 0.50 47.89 ? 309 MET A SD 1 ATOM 2081 C CE A MET A 1 316 ? 29.810 43.608 17.429 0.50 39.81 ? 309 MET A CE 1 ATOM 2082 C CE B MET A 1 316 ? 29.925 43.479 16.882 0.50 46.98 ? 309 MET A CE 1 ATOM 2083 N N . GLY A 1 317 ? 33.283 42.317 13.579 1.00 47.26 ? 310 GLY A N 1 ATOM 2084 C CA . GLY A 1 317 ? 34.102 43.147 12.692 1.00 49.42 ? 310 GLY A CA 1 ATOM 2085 C C . GLY A 1 317 ? 33.800 44.626 12.840 1.00 49.48 ? 310 GLY A C 1 ATOM 2086 O O . GLY A 1 317 ? 33.598 45.117 13.962 1.00 48.89 ? 310 GLY A O 1 ATOM 2087 N N . GLY A 1 318 ? 33.762 45.328 11.702 1.00 51.06 ? 311 GLY A N 1 ATOM 2088 C CA . GLY A 1 318 ? 33.568 46.774 11.672 1.00 50.60 ? 311 GLY A CA 1 ATOM 2089 C C . GLY A 1 318 ? 34.689 47.490 12.409 1.00 51.08 ? 311 GLY A C 1 ATOM 2090 O O . GLY A 1 318 ? 35.855 47.076 12.351 1.00 50.92 ? 311 GLY A O 1 ATOM 2091 N N . SER A 1 319 ? 34.323 48.554 13.113 1.00 49.70 ? 312 SER A N 1 ATOM 2092 C CA . SER A 1 319 ? 35.275 49.431 13.794 1.00 50.75 ? 312 SER A CA 1 ATOM 2093 C C . SER A 1 319 ? 35.864 48.835 15.060 1.00 49.85 ? 312 SER A C 1 ATOM 2094 O O . SER A 1 319 ? 35.160 48.138 15.808 1.00 48.95 ? 312 SER A O 1 ATOM 2095 C CB . SER A 1 319 ? 34.568 50.739 14.166 1.00 50.41 ? 312 SER A CB 1 ATOM 2096 O OG . SER A 1 319 ? 34.077 51.388 12.996 1.00 52.62 ? 312 SER A OG 1 ATOM 2097 N N . ALA A 1 320 ? 37.137 49.139 15.319 1.00 49.98 ? 313 ALA A N 1 ATOM 2098 C CA . ALA A 1 320 ? 37.800 48.796 16.585 1.00 49.27 ? 313 ALA A CA 1 ATOM 2099 C C . ALA A 1 320 ? 37.082 49.482 17.749 1.00 47.83 ? 313 ALA A C 1 ATOM 2100 O O . ALA A 1 320 ? 36.411 50.491 17.516 1.00 47.67 ? 313 ALA A O 1 ATOM 2101 C CB . ALA A 1 320 ? 39.241 49.249 16.548 1.00 50.52 ? 313 ALA A CB 1 ATOM 2102 N N . PRO A 1 321 ? 37.246 48.967 19.001 1.00 46.87 ? 314 PRO A N 1 ATOM 2103 C CA . PRO A 1 321 ? 36.703 49.711 20.175 1.00 45.64 ? 314 PRO A CA 1 ATOM 2104 C C . PRO A 1 321 ? 37.394 51.087 20.234 1.00 46.82 ? 314 PRO A C 1 ATOM 2105 O O . PRO A 1 321 ? 38.578 51.167 19.894 1.00 45.99 ? 314 PRO A O 1 ATOM 2106 C CB . PRO A 1 321 ? 37.114 48.863 21.386 1.00 44.68 ? 314 PRO A CB 1 ATOM 2107 C CG . PRO A 1 321 ? 38.209 47.924 20.882 1.00 45.82 ? 314 PRO A CG 1 ATOM 2108 C CD . PRO A 1 321 ? 38.047 47.781 19.387 1.00 47.18 ? 314 PRO A CD 1 ATOM 2109 N N . PRO A 1 322 ? 36.674 52.149 20.663 1.00 46.10 ? 315 PRO A N 1 ATOM 2110 C CA . PRO A 1 322 ? 37.297 53.487 20.586 1.00 47.41 ? 315 PRO A CA 1 ATOM 2111 C C . PRO A 1 322 ? 38.464 53.685 21.557 1.00 48.24 ? 315 PRO A C 1 ATOM 2112 O O . PRO A 1 322 ? 39.346 54.499 21.298 1.00 49.00 ? 315 PRO A O 1 ATOM 2113 C CB . PRO A 1 322 ? 36.136 54.440 20.920 1.00 46.21 ? 315 PRO A CB 1 ATOM 2114 C CG . PRO A 1 322 ? 35.173 53.582 21.746 1.00 44.10 ? 315 PRO A CG 1 ATOM 2115 C CD . PRO A 1 322 ? 35.263 52.223 21.103 1.00 44.49 ? 315 PRO A CD 1 ATOM 2116 N N . ASP A 1 323 ? 38.462 52.948 22.659 1.00 47.75 ? 316 ASP A N 1 ATOM 2117 C CA . ASP A 1 323 ? 39.532 52.993 23.657 1.00 49.30 ? 316 ASP A CA 1 ATOM 2118 C C . ASP A 1 323 ? 39.414 51.800 24.621 1.00 48.71 ? 316 ASP A C 1 ATOM 2119 O O . ASP A 1 323 ? 38.438 51.026 24.572 1.00 48.21 ? 316 ASP A O 1 ATOM 2120 C CB . ASP A 1 323 ? 39.567 54.356 24.413 1.00 49.07 ? 316 ASP A CB 1 ATOM 2121 C CG . ASP A 1 323 ? 38.345 54.594 25.306 1.00 49.62 ? 316 ASP A CG 1 ATOM 2122 O OD1 . ASP A 1 323 ? 38.030 53.761 26.178 1.00 52.99 ? 316 ASP A OD1 1 ATOM 2123 O OD2 . ASP A 1 323 ? 37.702 55.648 25.179 1.00 50.60 ? 316 ASP A OD2 1 ATOM 2124 N N . SER A 1 324 ? 40.382 51.689 25.528 1.00 49.06 ? 317 SER A N 1 ATOM 2125 C CA . SER A 1 324 ? 40.489 50.550 26.441 1.00 48.82 ? 317 SER A CA 1 ATOM 2126 C C . SER A 1 324 ? 39.301 50.408 27.435 1.00 46.55 ? 317 SER A C 1 ATOM 2127 O O . SER A 1 324 ? 39.030 49.300 27.908 1.00 46.77 ? 317 SER A O 1 ATOM 2128 C CB . SER A 1 324 ? 41.831 50.608 27.186 1.00 50.00 ? 317 SER A CB 1 ATOM 2129 O OG . SER A 1 324 ? 41.748 51.582 28.219 1.00 51.79 ? 317 SER A OG 1 ATOM 2130 N N . SER A 1 325 ? 38.595 51.501 27.737 1.00 44.83 ? 318 SER A N 1 ATOM 2131 C CA . SER A 1 325 ? 37.402 51.435 28.613 1.00 42.00 ? 318 SER A CA 1 ATOM 2132 C C . SER A 1 325 ? 36.223 50.662 27.985 1.00 40.89 ? 318 SER A C 1 ATOM 2133 O O . SER A 1 325 ? 35.213 50.378 28.660 1.00 39.83 ? 318 SER A O 1 ATOM 2134 C CB . SER A 1 325 ? 36.953 52.836 29.044 1.00 42.09 ? 318 SER A CB 1 ATOM 2135 O OG . SER A 1 325 ? 36.307 53.524 27.982 1.00 41.64 ? 318 SER A OG 1 ATOM 2136 N N . TRP A 1 326 ? 36.353 50.351 26.697 1.00 39.85 ? 319 TRP A N 1 ATOM 2137 C CA . TRP A 1 326 ? 35.395 49.534 25.959 1.00 39.38 ? 319 TRP A CA 1 ATOM 2138 C C . TRP A 1 326 ? 35.758 48.035 25.939 1.00 39.32 ? 319 TRP A C 1 ATOM 2139 O O . TRP A 1 326 ? 34.905 47.210 25.633 1.00 38.58 ? 319 TRP A O 1 ATOM 2140 C CB . TRP A 1 326 ? 35.190 50.069 24.524 1.00 40.11 ? 319 TRP A CB 1 ATOM 2141 C CG . TRP A 1 326 ? 34.218 51.236 24.481 1.00 37.28 ? 319 TRP A CG 1 ATOM 2142 C CD1 . TRP A 1 326 ? 34.327 52.427 25.162 1.00 36.16 ? 319 TRP A CD1 1 ATOM 2143 C CD2 . TRP A 1 326 ? 33.001 51.313 23.720 1.00 37.06 ? 319 TRP A CD2 1 ATOM 2144 N NE1 . TRP A 1 326 ? 33.236 53.231 24.879 1.00 37.62 ? 319 TRP A NE1 1 ATOM 2145 C CE2 . TRP A 1 326 ? 32.405 52.573 24.006 1.00 37.37 ? 319 TRP A CE2 1 ATOM 2146 C CE3 . TRP A 1 326 ? 32.349 50.435 22.829 1.00 37.31 ? 319 TRP A CE3 1 ATOM 2147 C CZ2 . TRP A 1 326 ? 31.182 52.980 23.436 1.00 33.65 ? 319 TRP A CZ2 1 ATOM 2148 C CZ3 . TRP A 1 326 ? 31.132 50.836 22.255 1.00 36.91 ? 319 TRP A CZ3 1 ATOM 2149 C CH2 . TRP A 1 326 ? 30.554 52.111 22.583 1.00 34.43 ? 319 TRP A CH2 1 ATOM 2150 N N . ARG A 1 327 ? 37.001 47.689 26.296 1.00 39.88 ? 320 ARG A N 1 ATOM 2151 C CA . ARG A 1 327 ? 37.450 46.294 26.297 1.00 40.57 ? 320 ARG A CA 1 ATOM 2152 C C . ARG A 1 327 ? 37.271 45.618 27.669 1.00 39.53 ? 320 ARG A C 1 ATOM 2153 O O . ARG A 1 327 ? 37.787 46.109 28.675 1.00 38.41 ? 320 ARG A O 1 ATOM 2154 C CB . ARG A 1 327 ? 38.923 46.199 25.866 1.00 41.55 ? 320 ARG A CB 1 ATOM 2155 C CG . ARG A 1 327 ? 39.162 46.274 24.361 1.00 45.91 ? 320 ARG A CG 1 ATOM 2156 C CD . ARG A 1 327 ? 40.653 46.002 24.009 1.00 53.39 ? 320 ARG A CD 1 ATOM 2157 N NE . ARG A 1 327 ? 41.441 47.128 24.501 1.00 61.14 ? 320 ARG A NE 1 ATOM 2158 C CZ . ARG A 1 327 ? 42.273 47.860 23.764 1.00 65.08 ? 320 ARG A CZ 1 ATOM 2159 N NH1 . ARG A 1 327 ? 42.494 47.554 22.483 1.00 67.66 ? 320 ARG A NH1 1 ATOM 2160 N NH2 . ARG A 1 327 ? 42.914 48.879 24.327 1.00 66.36 ? 320 ARG A NH2 1 ATOM 2161 N N . GLY A 1 328 ? 36.531 44.504 27.686 1.00 39.15 ? 321 GLY A N 1 ATOM 2162 C CA . GLY A 1 328 ? 36.448 43.593 28.851 1.00 38.25 ? 321 GLY A CA 1 ATOM 2163 C C . GLY A 1 328 ? 37.650 42.651 28.861 1.00 39.95 ? 321 GLY A C 1 ATOM 2164 O O . GLY A 1 328 ? 38.678 42.948 28.244 1.00 39.28 ? 321 GLY A O 1 ATOM 2165 N N . SER A 1 329 ? 37.519 41.516 29.549 1.00 39.22 ? 322 SER A N 1 ATOM 2166 C CA . SER A 1 329 ? 38.626 40.591 29.779 1.00 41.08 ? 322 SER A CA 1 ATOM 2167 C C . SER A 1 329 ? 38.612 39.342 28.905 1.00 40.88 ? 322 SER A C 1 ATOM 2168 O O . SER A 1 329 ? 39.494 38.524 29.023 1.00 42.43 ? 322 SER A O 1 ATOM 2169 C CB . SER A 1 329 ? 38.614 40.132 31.241 1.00 40.05 ? 322 SER A CB 1 ATOM 2170 O OG . SER A 1 329 ? 38.917 41.208 32.082 1.00 43.42 ? 322 SER A OG 1 ATOM 2171 N N . LEU A 1 330 ? 37.610 39.160 28.058 1.00 40.17 ? 323 LEU A N 1 ATOM 2172 C CA . LEU A 1 330 ? 37.603 37.972 27.187 1.00 41.08 ? 323 LEU A CA 1 ATOM 2173 C C . LEU A 1 330 ? 38.641 38.094 26.070 1.00 43.21 ? 323 LEU A C 1 ATOM 2174 O O . LEU A 1 330 ? 39.057 39.204 25.730 1.00 43.99 ? 323 LEU A O 1 ATOM 2175 C CB . LEU A 1 330 ? 36.223 37.772 26.560 1.00 39.96 ? 323 LEU A CB 1 ATOM 2176 C CG . LEU A 1 330 ? 35.027 37.503 27.488 1.00 37.50 ? 323 LEU A CG 1 ATOM 2177 C CD1 . LEU A 1 330 ? 33.749 37.685 26.671 1.00 35.46 ? 323 LEU A CD1 1 ATOM 2178 C CD2 . LEU A 1 330 ? 35.138 36.100 28.102 1.00 35.52 ? 323 LEU A CD2 1 ATOM 2179 N N . LYS A 1 331 ? 39.012 36.973 25.454 1.00 44.66 ? 324 LYS A N 1 ATOM 2180 C CA . LYS A 1 331 ? 39.996 36.997 24.357 1.00 47.43 ? 324 LYS A CA 1 ATOM 2181 C C . LYS A 1 331 ? 39.337 37.285 23.015 1.00 47.14 ? 324 LYS A C 1 ATOM 2182 O O . LYS A 1 331 ? 39.289 36.417 22.130 1.00 47.62 ? 324 LYS A O 1 ATOM 2183 C CB . LYS A 1 331 ? 40.805 35.690 24.298 1.00 49.08 ? 324 LYS A CB 1 ATOM 2184 C CG . LYS A 1 331 ? 41.570 35.346 25.591 1.00 53.56 ? 324 LYS A CG 1 ATOM 2185 C CD . LYS A 1 331 ? 41.955 36.599 26.422 1.00 58.90 ? 324 LYS A CD 1 ATOM 2186 C CE . LYS A 1 331 ? 43.363 36.467 27.029 1.00 62.84 ? 324 LYS A CE 1 ATOM 2187 N NZ . LYS A 1 331 ? 43.885 37.808 27.434 1.00 64.61 ? 324 LYS A NZ 1 ATOM 2188 N N . VAL A 1 332 ? 38.799 38.499 22.895 1.00 46.05 ? 325 VAL A N 1 ATOM 2189 C CA . VAL A 1 332 ? 38.158 38.977 21.671 1.00 45.85 ? 325 VAL A CA 1 ATOM 2190 C C . VAL A 1 332 ? 38.585 40.432 21.457 1.00 45.92 ? 325 VAL A C 1 ATOM 2191 O O . VAL A 1 332 ? 39.042 41.076 22.399 1.00 45.20 ? 325 VAL A O 1 ATOM 2192 C CB . VAL A 1 332 ? 36.613 38.833 21.707 1.00 44.70 ? 325 VAL A CB 1 ATOM 2193 C CG1 . VAL A 1 332 ? 36.202 37.354 21.831 1.00 45.35 ? 325 VAL A CG1 1 ATOM 2194 C CG2 . VAL A 1 332 ? 35.946 39.726 22.841 1.00 41.68 ? 325 VAL A CG2 1 ATOM 2195 N N . PRO A 1 333 ? 38.466 40.951 20.214 1.00 46.50 ? 326 PRO A N 1 ATOM 2196 C CA . PRO A 1 333 ? 38.944 42.326 20.006 1.00 46.54 ? 326 PRO A CA 1 ATOM 2197 C C . PRO A 1 333 ? 37.997 43.376 20.588 1.00 44.75 ? 326 PRO A C 1 ATOM 2198 O O . PRO A 1 333 ? 38.410 44.509 20.787 1.00 45.08 ? 326 PRO A O 1 ATOM 2199 C CB . PRO A 1 333 ? 39.018 42.463 18.475 1.00 48.67 ? 326 PRO A CB 1 ATOM 2200 C CG . PRO A 1 333 ? 38.032 41.422 17.931 1.00 49.17 ? 326 PRO A CG 1 ATOM 2201 C CD . PRO A 1 333 ? 37.916 40.335 18.983 1.00 47.86 ? 326 PRO A CD 1 ATOM 2202 N N . TYR A 1 334 ? 36.751 42.998 20.876 1.00 42.41 ? 327 TYR A N 1 ATOM 2203 C CA . TYR A 1 334 ? 35.738 43.982 21.298 1.00 40.94 ? 327 TYR A CA 1 ATOM 2204 C C . TYR A 1 334 ? 35.451 45.002 20.200 1.00 41.28 ? 327 TYR A C 1 ATOM 2205 O O . TYR A 1 334 ? 35.303 46.203 20.472 1.00 40.39 ? 327 TYR A O 1 ATOM 2206 C CB . TYR A 1 334 ? 36.133 44.659 22.624 1.00 40.35 ? 327 TYR A CB 1 ATOM 2207 C CG . TYR A 1 334 ? 35.994 43.706 23.796 1.00 39.40 ? 327 TYR A CG 1 ATOM 2208 C CD1 . TYR A 1 334 ? 34.748 43.509 24.401 1.00 37.16 ? 327 TYR A CD1 1 ATOM 2209 C CD2 . TYR A 1 334 ? 37.087 42.937 24.244 1.00 39.36 ? 327 TYR A CD2 1 ATOM 2210 C CE1 . TYR A 1 334 ? 34.590 42.624 25.460 1.00 35.25 ? 327 TYR A CE1 1 ATOM 2211 C CE2 . TYR A 1 334 ? 36.935 42.033 25.313 1.00 36.82 ? 327 TYR A CE2 1 ATOM 2212 C CZ . TYR A 1 334 ? 35.675 41.884 25.901 1.00 36.99 ? 327 TYR A CZ 1 ATOM 2213 O OH . TYR A 1 334 ? 35.504 41.024 26.961 1.00 34.74 ? 327 TYR A OH 1 ATOM 2214 N N . ASN A 1 335 ? 35.416 44.525 18.948 1.00 42.48 ? 328 ASN A N 1 ATOM 2215 C CA . ASN A 1 335 ? 35.022 45.376 17.831 1.00 42.96 ? 328 ASN A CA 1 ATOM 2216 C C . ASN A 1 335 ? 33.567 45.775 18.037 1.00 41.89 ? 328 ASN A C 1 ATOM 2217 O O . ASN A 1 335 ? 32.760 45.004 18.528 1.00 39.67 ? 328 ASN A O 1 ATOM 2218 C CB . ASN A 1 335 ? 35.202 44.679 16.490 1.00 43.56 ? 328 ASN A CB 1 ATOM 2219 C CG . ASN A 1 335 ? 36.660 44.437 16.143 1.00 45.46 ? 328 ASN A CG 1 ATOM 2220 O OD1 . ASN A 1 335 ? 37.557 45.156 16.605 1.00 45.74 ? 328 ASN A OD1 1 ATOM 2221 N ND2 . ASN A 1 335 ? 36.905 43.419 15.320 1.00 43.29 ? 328 ASN A ND2 1 ATOM 2222 N N . VAL A 1 336 ? 33.250 46.995 17.650 1.00 42.99 ? 329 VAL A N 1 ATOM 2223 C CA . VAL A 1 336 ? 31.926 47.540 17.863 1.00 42.72 ? 329 VAL A CA 1 ATOM 2224 C C . VAL A 1 336 ? 30.948 47.077 16.778 1.00 43.25 ? 329 VAL A C 1 ATOM 2225 O O . VAL A 1 336 ? 29.727 47.098 16.976 1.00 41.94 ? 329 VAL A O 1 ATOM 2226 C CB . VAL A 1 336 ? 32.010 49.061 17.918 1.00 43.10 ? 329 VAL A CB 1 ATOM 2227 C CG1 . VAL A 1 336 ? 30.606 49.664 18.057 1.00 44.08 ? 329 VAL A CG1 1 ATOM 2228 C CG2 . VAL A 1 336 ? 32.859 49.450 19.118 1.00 44.11 ? 329 VAL A CG2 1 ATOM 2229 N N . GLY A 1 337 ? 31.481 46.637 15.641 1.00 44.08 ? 330 GLY A N 1 ATOM 2230 C CA . GLY A 1 337 ? 30.627 46.178 14.542 1.00 44.98 ? 330 GLY A CA 1 ATOM 2231 C C . GLY A 1 337 ? 30.308 47.359 13.646 1.00 45.84 ? 330 GLY A C 1 ATOM 2232 O O . GLY A 1 337 ? 31.119 48.273 13.527 1.00 46.41 ? 330 GLY A O 1 ATOM 2233 N N . PRO A 1 338 ? 29.140 47.347 12.988 1.00 46.36 ? 331 PRO A N 1 ATOM 2234 C CA . PRO A 1 338 ? 28.113 46.297 12.933 1.00 46.03 ? 331 PRO A CA 1 ATOM 2235 C C . PRO A 1 338 ? 28.579 45.025 12.225 1.00 46.47 ? 331 PRO A C 1 ATOM 2236 O O . PRO A 1 338 ? 29.421 45.088 11.306 1.00 47.65 ? 331 PRO A O 1 ATOM 2237 C CB . PRO A 1 338 ? 27.007 46.947 12.093 1.00 46.51 ? 331 PRO A CB 1 ATOM 2238 C CG . PRO A 1 338 ? 27.797 47.860 11.122 1.00 49.13 ? 331 PRO A CG 1 ATOM 2239 C CD . PRO A 1 338 ? 28.825 48.470 12.073 1.00 47.99 ? 331 PRO A CD 1 ATOM 2240 N N . GLY A 1 339 ? 28.028 43.884 12.641 1.00 45.49 ? 332 GLY A N 1 ATOM 2241 C CA . GLY A 1 339 ? 28.230 42.618 11.923 1.00 46.71 ? 332 GLY A CA 1 ATOM 2242 C C . GLY A 1 339 ? 29.597 41.991 12.127 1.00 47.44 ? 332 GLY A C 1 ATOM 2243 O O . GLY A 1 339 ? 30.445 42.528 12.863 1.00 45.77 ? 332 GLY A O 1 ATOM 2244 N N . PHE A 1 340 ? 29.803 40.852 11.458 1.00 48.84 ? 333 PHE A N 1 ATOM 2245 C CA . PHE A 1 340 ? 30.993 40.009 11.642 1.00 50.30 ? 333 PHE A CA 1 ATOM 2246 C C . PHE A 1 340 ? 32.068 40.325 10.602 1.00 52.58 ? 333 PHE A C 1 ATOM 2247 O O . PHE A 1 340 ? 31.747 40.923 9.581 1.00 53.42 ? 333 PHE A O 1 ATOM 2248 C CB . PHE A 1 340 ? 30.605 38.525 11.559 1.00 49.81 ? 333 PHE A CB 1 ATOM 2249 C CG . PHE A 1 340 ? 29.690 38.067 12.672 1.00 49.25 ? 333 PHE A CG 1 ATOM 2250 C CD1 . PHE A 1 340 ? 28.633 37.201 12.405 1.00 49.52 ? 333 PHE A CD1 1 ATOM 2251 C CD2 . PHE A 1 340 ? 29.885 38.503 13.980 1.00 47.45 ? 333 PHE A CD2 1 ATOM 2252 C CE1 . PHE A 1 340 ? 27.793 36.762 13.422 1.00 48.25 ? 333 PHE A CE1 1 ATOM 2253 C CE2 . PHE A 1 340 ? 29.046 38.082 15.006 1.00 45.73 ? 333 PHE A CE2 1 ATOM 2254 C CZ . PHE A 1 340 ? 27.993 37.210 14.731 1.00 46.34 ? 333 PHE A CZ 1 ATOM 2255 N N . THR A 1 341 ? 33.328 39.941 10.858 1.00 54.29 ? 334 THR A N 1 ATOM 2256 C CA . THR A 1 341 ? 34.415 40.156 9.867 1.00 57.33 ? 334 THR A CA 1 ATOM 2257 C C . THR A 1 341 ? 34.245 39.288 8.625 1.00 59.31 ? 334 THR A C 1 ATOM 2258 O O . THR A 1 341 ? 33.621 38.218 8.683 1.00 58.80 ? 334 THR A O 1 ATOM 2259 C CB . THR A 1 341 ? 35.847 39.862 10.416 1.00 58.34 ? 334 THR A CB 1 ATOM 2260 O OG1 . THR A 1 341 ? 35.852 38.634 11.155 1.00 59.15 ? 334 THR A OG1 1 ATOM 2261 C CG2 . THR A 1 341 ? 36.369 40.991 11.288 1.00 58.27 ? 334 THR A CG2 1 ATOM 2262 N N . GLY A 1 342 ? 34.875 39.741 7.531 1.00 61.48 ? 335 GLY A N 1 ATOM 2263 C CA . GLY A 1 342 ? 34.807 39.142 6.193 1.00 63.88 ? 335 GLY A CA 1 ATOM 2264 C C . GLY A 1 342 ? 34.232 37.764 5.931 1.00 64.53 ? 335 GLY A C 1 ATOM 2265 O O . GLY A 1 342 ? 33.240 37.643 5.210 1.00 65.64 ? 335 GLY A O 1 ATOM 2266 N N . ASN A 1 343 ? 34.865 36.725 6.474 1.00 64.55 ? 336 ASN A N 1 ATOM 2267 C CA . ASN A 1 343 ? 34.453 35.331 6.228 1.00 65.11 ? 336 ASN A CA 1 ATOM 2268 C C . ASN A 1 343 ? 33.030 35.022 6.667 1.00 63.20 ? 336 ASN A C 1 ATOM 2269 O O . ASN A 1 343 ? 32.338 34.202 6.056 1.00 63.40 ? 336 ASN A O 1 ATOM 2270 C CB . ASN A 1 343 ? 35.387 34.357 6.959 1.00 65.75 ? 336 ASN A CB 1 ATOM 2271 C CG . ASN A 1 343 ? 36.731 34.211 6.290 1.00 70.16 ? 336 ASN A CG 1 ATOM 2272 O OD1 . ASN A 1 343 ? 37.090 34.965 5.371 1.00 74.14 ? 336 ASN A OD1 1 ATOM 2273 N ND2 . ASN A 1 343 ? 37.492 33.213 6.740 1.00 74.41 ? 336 ASN A ND2 1 ATOM 2274 N N . PHE A 1 344 ? 32.615 35.685 7.745 1.00 60.62 ? 337 PHE A N 1 ATOM 2275 C CA . PHE A 1 344 ? 31.340 35.423 8.394 1.00 58.66 ? 337 PHE A CA 1 ATOM 2276 C C . PHE A 1 344 ? 30.337 36.557 8.165 1.00 57.48 ? 337 PHE A C 1 ATOM 2277 O O . PHE A 1 344 ? 29.300 36.610 8.828 1.00 56.02 ? 337 PHE A O 1 ATOM 2278 C CB . PHE A 1 344 ? 31.571 35.213 9.895 1.00 56.92 ? 337 PHE A CB 1 ATOM 2279 C CG . PHE A 1 344 ? 32.747 34.318 10.212 1.00 58.48 ? 337 PHE A CG 1 ATOM 2280 C CD1 . PHE A 1 344 ? 33.948 34.858 10.674 1.00 59.35 ? 337 PHE A CD1 1 ATOM 2281 C CD2 . PHE A 1 344 ? 32.655 32.937 10.043 1.00 59.65 ? 337 PHE A CD2 1 ATOM 2282 C CE1 . PHE A 1 344 ? 35.045 34.030 10.967 1.00 60.62 ? 337 PHE A CE1 1 ATOM 2283 C CE2 . PHE A 1 344 ? 33.744 32.099 10.331 1.00 60.93 ? 337 PHE A CE2 1 ATOM 2284 C CZ . PHE A 1 344 ? 34.939 32.651 10.796 1.00 60.81 ? 337 PHE A CZ 1 ATOM 2285 N N . SER A 1 345 ? 30.632 37.442 7.212 1.00 57.78 ? 338 SER A N 1 ATOM 2286 C CA . SER A 1 345 ? 29.837 38.660 7.017 1.00 57.43 ? 338 SER A CA 1 ATOM 2287 C C . SER A 1 345 ? 28.373 38.366 6.716 1.00 56.56 ? 338 SER A C 1 ATOM 2288 O O . SER A 1 345 ? 27.505 39.224 6.943 1.00 56.40 ? 338 SER A O 1 ATOM 2289 C CB . SER A 1 345 ? 30.431 39.539 5.919 1.00 58.91 ? 338 SER A CB 1 ATOM 2290 O OG . SER A 1 345 ? 30.281 38.913 4.659 1.00 61.08 ? 338 SER A OG 1 ATOM 2291 N N . THR A 1 346 ? 28.104 37.147 6.257 1.00 56.28 ? 339 THR A N 1 ATOM 2292 C CA . THR A 1 346 ? 26.766 36.735 5.837 1.00 56.35 ? 339 THR A CA 1 ATOM 2293 C C . THR A 1 346 ? 26.012 36.018 6.948 1.00 54.76 ? 339 THR A C 1 ATOM 2294 O O . THR A 1 346 ? 24.824 35.705 6.806 1.00 55.27 ? 339 THR A O 1 ATOM 2295 C CB . THR A 1 346 ? 26.800 35.809 4.602 1.00 57.61 ? 339 THR A CB 1 ATOM 2296 O OG1 . THR A 1 346 ? 27.469 34.582 4.929 1.00 58.46 ? 339 THR A OG1 1 ATOM 2297 C CG2 . THR A 1 346 ? 27.512 36.488 3.440 1.00 59.85 ? 339 THR A CG2 1 ATOM 2298 N N . GLN A 1 347 ? 26.710 35.739 8.045 1.00 53.29 ? 340 GLN A N 1 ATOM 2299 C CA . GLN A 1 347 ? 26.067 35.185 9.228 1.00 50.51 ? 340 GLN A CA 1 ATOM 2300 C C . GLN A 1 347 ? 25.368 36.324 9.983 1.00 48.98 ? 340 GLN A C 1 ATOM 2301 O O . GLN A 1 347 ? 25.719 37.491 9.815 1.00 47.53 ? 340 GLN A O 1 ATOM 2302 C CB . GLN A 1 347 ? 27.071 34.442 10.109 1.00 49.71 ? 340 GLN A CB 1 ATOM 2303 C CG . GLN A 1 347 ? 27.645 33.181 9.428 1.00 52.45 ? 340 GLN A CG 1 ATOM 2304 C CD . GLN A 1 347 ? 28.798 32.522 10.186 1.00 53.09 ? 340 GLN A CD 1 ATOM 2305 O OE1 . GLN A 1 347 ? 29.174 32.938 11.280 1.00 53.62 ? 340 GLN A OE1 1 ATOM 2306 N NE2 . GLN A 1 347 ? 29.356 31.474 9.594 1.00 53.65 ? 340 GLN A NE2 1 ATOM 2307 N N . LYS A 1 348 ? 24.350 35.960 10.756 1.00 47.57 ? 341 LYS A N 1 ATOM 2308 C CA . LYS A 1 348 ? 23.543 36.899 11.523 1.00 46.72 ? 341 LYS A CA 1 ATOM 2309 C C . LYS A 1 348 ? 23.257 36.320 12.903 1.00 45.11 ? 341 LYS A C 1 ATOM 2310 O O . LYS A 1 348 ? 23.465 35.127 13.151 1.00 44.95 ? 341 LYS A O 1 ATOM 2311 C CB . LYS A 1 348 ? 22.216 37.183 10.800 1.00 47.75 ? 341 LYS A CB 1 ATOM 2312 C CG . LYS A 1 348 ? 22.345 37.994 9.488 1.00 51.51 ? 341 LYS A CG 1 ATOM 2313 C CD . LYS A 1 348 ? 20.943 38.432 9.013 1.00 57.30 ? 341 LYS A CD 1 ATOM 2314 C CE . LYS A 1 348 ? 20.938 39.820 8.374 1.00 59.70 ? 341 LYS A CE 1 ATOM 2315 N NZ . LYS A 1 348 ? 21.766 39.844 7.127 1.00 61.08 ? 341 LYS A NZ 1 ATOM 2316 N N . VAL A 1 349 ? 22.763 37.170 13.808 1.00 42.41 ? 342 VAL A N 1 ATOM 2317 C CA . VAL A 1 349 ? 22.355 36.701 15.119 1.00 41.01 ? 342 VAL A CA 1 ATOM 2318 C C . VAL A 1 349 ? 20.820 36.684 15.160 1.00 40.42 ? 342 VAL A C 1 ATOM 2319 O O . VAL A 1 349 ? 20.182 37.617 14.669 1.00 40.38 ? 342 VAL A O 1 ATOM 2320 C CB . VAL A 1 349 ? 22.947 37.586 16.215 1.00 40.40 ? 342 VAL A CB 1 ATOM 2321 C CG1 . VAL A 1 349 ? 22.266 37.322 17.572 1.00 38.80 ? 342 VAL A CG1 1 ATOM 2322 C CG2 . VAL A 1 349 ? 24.466 37.340 16.288 1.00 40.70 ? 342 VAL A CG2 1 ATOM 2323 N N . LYS A 1 350 ? 20.244 35.613 15.707 1.00 39.70 ? 343 LYS A N 1 ATOM 2324 C CA . LYS A 1 350 ? 18.796 35.504 15.857 1.00 39.33 ? 343 LYS A CA 1 ATOM 2325 C C . LYS A 1 350 ? 18.406 35.216 17.310 1.00 38.15 ? 343 LYS A C 1 ATOM 2326 O O . LYS A 1 350 ? 18.891 34.253 17.916 1.00 37.03 ? 343 LYS A O 1 ATOM 2327 C CB . LYS A 1 350 ? 18.237 34.400 14.950 1.00 40.84 ? 343 LYS A CB 1 ATOM 2328 C CG . LYS A 1 350 ? 16.701 34.257 14.986 1.00 41.61 ? 343 LYS A CG 1 ATOM 2329 C CD . LYS A 1 350 ? 16.242 33.201 13.965 1.00 45.29 ? 343 LYS A CD 1 ATOM 2330 C CE . LYS A 1 350 ? 14.709 33.111 13.947 1.00 45.54 ? 343 LYS A CE 1 ATOM 2331 N NZ . LYS A 1 350 ? 14.224 32.563 12.652 1.00 51.31 ? 343 LYS A NZ 1 ATOM 2332 N N . MET A 1 351 ? 17.496 36.030 17.838 1.00 36.54 ? 344 MET A N 1 ATOM 2333 C CA . MET A 1 351 ? 16.985 35.837 19.187 1.00 35.82 ? 344 MET A CA 1 ATOM 2334 C C . MET A 1 351 ? 15.693 35.021 19.074 1.00 36.50 ? 344 MET A C 1 ATOM 2335 O O . MET A 1 351 ? 15.000 35.124 18.064 1.00 37.51 ? 344 MET A O 1 ATOM 2336 C CB . MET A 1 351 ? 16.694 37.207 19.841 1.00 33.65 ? 344 MET A CB 1 ATOM 2337 C CG . MET A 1 351 ? 17.886 38.154 19.883 1.00 32.84 ? 344 MET A CG 1 ATOM 2338 S SD . MET A 1 351 ? 17.524 39.718 20.783 1.00 31.77 ? 344 MET A SD 1 ATOM 2339 C CE . MET A 1 351 ? 17.305 39.112 22.469 1.00 29.83 ? 344 MET A CE 1 ATOM 2340 N N . HIS A 1 352 ? 15.341 34.253 20.106 1.00 36.07 ? 345 HIS A N 1 ATOM 2341 C CA . HIS A 1 352 ? 14.029 33.601 20.136 1.00 36.09 ? 345 HIS A CA 1 ATOM 2342 C C . HIS A 1 352 ? 13.448 33.826 21.513 1.00 34.46 ? 345 HIS A C 1 ATOM 2343 O O . HIS A 1 352 ? 13.861 33.161 22.469 1.00 34.05 ? 345 HIS A O 1 ATOM 2344 C CB . HIS A 1 352 ? 14.119 32.100 19.902 1.00 37.02 ? 345 HIS A CB 1 ATOM 2345 C CG . HIS A 1 352 ? 15.065 31.699 18.815 1.00 39.35 ? 345 HIS A CG 1 ATOM 2346 N ND1 . HIS A 1 352 ? 16.434 31.757 18.968 1.00 42.55 ? 345 HIS A ND1 1 ATOM 2347 C CD2 . HIS A 1 352 ? 14.845 31.196 17.577 1.00 43.74 ? 345 HIS A CD2 1 ATOM 2348 C CE1 . HIS A 1 352 ? 17.020 31.328 17.859 1.00 42.84 ? 345 HIS A CE1 1 ATOM 2349 N NE2 . HIS A 1 352 ? 16.077 30.982 17.002 1.00 44.51 ? 345 HIS A NE2 1 ATOM 2350 N N . ILE A 1 353 ? 12.506 34.760 21.642 1.00 33.45 ? 346 ILE A N 1 ATOM 2351 C CA . ILE A 1 353 ? 11.994 35.044 22.988 1.00 31.86 ? 346 ILE A CA 1 ATOM 2352 C C . ILE A 1 353 ? 10.498 34.771 23.021 1.00 32.43 ? 346 ILE A C 1 ATOM 2353 O O . ILE A 1 353 ? 9.748 35.334 22.211 1.00 33.27 ? 346 ILE A O 1 ATOM 2354 C CB . ILE A 1 353 ? 12.310 36.494 23.439 1.00 31.62 ? 346 ILE A CB 1 ATOM 2355 C CG1 . ILE A 1 353 ? 13.801 36.815 23.255 1.00 30.67 ? 346 ILE A CG1 1 ATOM 2356 C CG2 . ILE A 1 353 ? 11.856 36.709 24.898 1.00 29.64 ? 346 ILE A CG2 1 ATOM 2357 C CD1 . ILE A 1 353 ? 14.828 35.918 24.110 1.00 32.63 ? 346 ILE A CD1 1 ATOM 2358 N N . HIS A 1 354 ? 10.067 33.913 23.948 1.00 31.90 ? 347 HIS A N 1 ATOM 2359 C CA . HIS A 1 354 ? 8.650 33.514 24.052 1.00 32.84 ? 347 HIS A CA 1 ATOM 2360 C C . HIS A 1 354 ? 8.043 33.686 25.455 1.00 31.37 ? 347 HIS A C 1 ATOM 2361 O O . HIS A 1 354 ? 7.003 33.076 25.767 1.00 29.91 ? 347 HIS A O 1 ATOM 2362 C CB . HIS A 1 354 ? 8.513 32.049 23.627 1.00 34.32 ? 347 HIS A CB 1 ATOM 2363 C CG . HIS A 1 354 ? 9.144 31.764 22.298 1.00 38.46 ? 347 HIS A CG 1 ATOM 2364 N ND1 . HIS A 1 354 ? 10.313 31.041 22.168 1.00 43.41 ? 347 HIS A ND1 1 ATOM 2365 C CD2 . HIS A 1 354 ? 8.804 32.163 21.048 1.00 42.53 ? 347 HIS A CD2 1 ATOM 2366 C CE1 . HIS A 1 354 ? 10.645 30.976 20.889 1.00 44.41 ? 347 HIS A CE1 1 ATOM 2367 N NE2 . HIS A 1 354 ? 9.745 31.647 20.189 1.00 45.83 ? 347 HIS A NE2 1 ATOM 2368 N N . SER A 1 355 ? 8.707 34.484 26.298 1.00 29.54 ? 348 SER A N 1 ATOM 2369 C CA . SER A 1 355 ? 8.193 34.796 27.641 1.00 28.51 ? 348 SER A CA 1 ATOM 2370 C C . SER A 1 355 ? 6.822 35.460 27.534 1.00 29.00 ? 348 SER A C 1 ATOM 2371 O O . SER A 1 355 ? 6.547 36.115 26.526 1.00 29.00 ? 348 SER A O 1 ATOM 2372 C CB . SER A 1 355 ? 9.148 35.757 28.349 1.00 27.28 ? 348 SER A CB 1 ATOM 2373 O OG . SER A 1 355 ? 10.431 35.156 28.446 1.00 27.61 ? 348 SER A OG 1 ATOM 2374 N N . THR A 1 356 ? 5.984 35.298 28.570 1.00 27.67 ? 349 THR A N 1 ATOM 2375 C CA . THR A 1 356 ? 4.651 35.903 28.598 1.00 28.69 ? 349 THR A CA 1 ATOM 2376 C C . THR A 1 356 ? 4.496 36.716 29.881 1.00 28.02 ? 349 THR A C 1 ATOM 2377 O O . THR A 1 356 ? 5.101 36.392 30.920 1.00 27.55 ? 349 THR A O 1 ATOM 2378 C CB . THR A 1 356 ? 3.538 34.847 28.563 1.00 29.25 ? 349 THR A CB 1 ATOM 2379 O OG1 . THR A 1 356 ? 3.699 33.977 29.687 1.00 34.22 ? 349 THR A OG1 1 ATOM 2380 C CG2 . THR A 1 356 ? 3.685 33.991 27.317 1.00 29.03 ? 349 THR A CG2 1 ATOM 2381 N N . ASN A 1 357 ? 3.724 37.788 29.777 1.00 26.63 ? 350 ASN A N 1 ATOM 2382 C CA . ASN A 1 357 ? 3.388 38.609 30.938 1.00 26.20 ? 350 ASN A CA 1 ATOM 2383 C C . ASN A 1 357 ? 2.021 38.138 31.411 1.00 27.77 ? 350 ASN A C 1 ATOM 2384 O O . ASN A 1 357 ? 1.096 37.870 30.605 1.00 28.20 ? 350 ASN A O 1 ATOM 2385 C CB . ASN A 1 357 ? 3.304 40.077 30.541 1.00 25.45 ? 350 ASN A CB 1 ATOM 2386 C CG . ASN A 1 357 ? 4.597 40.627 29.994 1.00 27.33 ? 350 ASN A CG 1 ATOM 2387 O OD1 . ASN A 1 357 ? 5.708 40.310 30.450 1.00 27.32 ? 350 ASN A OD1 1 ATOM 2388 N ND2 . ASN A 1 357 ? 4.459 41.491 28.990 1.00 32.31 ? 350 ASN A ND2 1 ATOM 2389 N N . GLU A 1 358 ? 1.861 37.968 32.707 1.00 26.08 ? 351 GLU A N 1 ATOM 2390 C CA . GLU A 1 358 ? 0.555 37.534 33.190 1.00 27.43 ? 351 GLU A CA 1 ATOM 2391 C C . GLU A 1 358 ? 0.281 38.059 34.563 1.00 25.02 ? 351 GLU A C 1 ATOM 2392 O O . GLU A 1 358 ? 1.180 38.127 35.385 1.00 22.71 ? 351 GLU A O 1 ATOM 2393 C CB . GLU A 1 358 ? 0.433 36.034 33.252 1.00 29.46 ? 351 GLU A CB 1 ATOM 2394 C CG . GLU A 1 358 ? 1.684 35.291 33.520 1.00 36.53 ? 351 GLU A CG 1 ATOM 2395 C CD . GLU A 1 358 ? 1.474 33.824 33.172 1.00 46.15 ? 351 GLU A CD 1 ATOM 2396 O OE1 . GLU A 1 358 ? 1.663 32.946 34.047 1.00 44.86 ? 351 GLU A OE1 1 ATOM 2397 O OE2 . GLU A 1 358 ? 1.033 33.570 32.023 1.00 54.45 ? 351 GLU A OE2 1 ATOM 2398 N N . VAL A 1 359 ? -0.974 38.434 34.766 1.00 24.74 ? 352 VAL A N 1 ATOM 2399 C CA . VAL A 1 359 ? -1.422 39.011 36.037 1.00 23.93 ? 352 VAL A CA 1 ATOM 2400 C C . VAL A 1 359 ? -1.457 37.838 37.048 1.00 24.24 ? 352 VAL A C 1 ATOM 2401 O O . VAL A 1 359 ? -2.073 36.792 36.782 1.00 23.27 ? 352 VAL A O 1 ATOM 2402 C CB . VAL A 1 359 ? -2.802 39.676 35.882 1.00 25.14 ? 352 VAL A CB 1 ATOM 2403 C CG1 . VAL A 1 359 ? -3.345 40.115 37.259 1.00 23.83 ? 352 VAL A CG1 1 ATOM 2404 C CG2 . VAL A 1 359 ? -2.692 40.893 34.912 1.00 25.48 ? 352 VAL A CG2 1 ATOM 2405 N N . THR A 1 360 ? -0.747 38.023 38.166 1.00 22.51 ? 353 THR A N 1 ATOM 2406 C CA . THR A 1 360 ? -0.402 36.944 39.099 1.00 22.62 ? 353 THR A CA 1 ATOM 2407 C C . THR A 1 360 ? -0.531 37.503 40.527 1.00 22.80 ? 353 THR A C 1 ATOM 2408 O O . THR A 1 360 ? -0.130 38.668 40.765 1.00 21.49 ? 353 THR A O 1 ATOM 2409 C CB . THR A 1 360 ? 1.029 36.437 38.819 1.00 22.21 ? 353 THR A CB 1 ATOM 2410 O OG1 . THR A 1 360 ? 1.128 36.093 37.414 1.00 24.19 ? 353 THR A OG1 1 ATOM 2411 C CG2 . THR A 1 360 ? 1.338 35.180 39.681 1.00 23.29 ? 353 THR A CG2 1 ATOM 2412 N N . ARG A 1 361 ? -1.097 36.702 41.448 1.00 22.29 ? 354 ARG A N 1 ATOM 2413 C CA . ARG A 1 361 ? -1.227 37.118 42.853 1.00 21.99 ? 354 ARG A CA 1 ATOM 2414 C C . ARG A 1 361 ? 0.124 37.085 43.585 1.00 21.58 ? 354 ARG A C 1 ATOM 2415 O O . ARG A 1 361 ? 0.922 36.145 43.429 1.00 21.91 ? 354 ARG A O 1 ATOM 2416 C CB . ARG A 1 361 ? -2.278 36.274 43.622 1.00 23.75 ? 354 ARG A CB 1 ATOM 2417 C CG . ARG A 1 361 ? -2.546 36.745 45.066 1.00 24.30 ? 354 ARG A CG 1 ATOM 2418 C CD . ARG A 1 361 ? -3.952 36.302 45.493 1.00 25.42 ? 354 ARG A CD 1 ATOM 2419 N NE . ARG A 1 361 ? -4.947 37.101 44.767 1.00 26.02 ? 354 ARG A NE 1 ATOM 2420 C CZ . ARG A 1 361 ? -6.258 37.058 44.996 1.00 29.99 ? 354 ARG A CZ 1 ATOM 2421 N NH1 . ARG A 1 361 ? -6.745 36.227 45.918 1.00 29.11 ? 354 ARG A NH1 1 ATOM 2422 N NH2 . ARG A 1 361 ? -7.083 37.840 44.303 1.00 31.16 ? 354 ARG A NH2 1 ATOM 2423 N N . ILE A 1 362 ? 0.354 38.129 44.374 1.00 19.72 ? 355 ILE A N 1 ATOM 2424 C CA . ILE A 1 362 ? 1.569 38.242 45.168 1.00 19.48 ? 355 ILE A CA 1 ATOM 2425 C C . ILE A 1 362 ? 1.139 38.533 46.601 1.00 20.60 ? 355 ILE A C 1 ATOM 2426 O O . ILE A 1 362 ? 0.021 38.982 46.826 1.00 21.10 ? 355 ILE A O 1 ATOM 2427 C CB . ILE A 1 362 ? 2.513 39.390 44.631 1.00 18.47 ? 355 ILE A CB 1 ATOM 2428 C CG1 . ILE A 1 362 ? 1.802 40.765 44.670 1.00 18.25 ? 355 ILE A CG1 1 ATOM 2429 C CG2 . ILE A 1 362 ? 3.053 38.990 43.234 1.00 16.47 ? 355 ILE A CG2 1 ATOM 2430 C CD1 . ILE A 1 362 ? 2.843 41.928 44.528 1.00 15.37 ? 355 ILE A CD1 1 ATOM 2431 N N . TYR A 1 363 ? 2.027 38.285 47.568 1.00 20.67 ? 356 TYR A N 1 ATOM 2432 C CA . TYR A 1 363 ? 1.608 38.353 48.960 1.00 19.62 ? 356 TYR A CA 1 ATOM 2433 C C . TYR A 1 363 ? 2.658 39.037 49.805 1.00 20.24 ? 356 TYR A C 1 ATOM 2434 O O . TYR A 1 363 ? 3.779 38.504 49.935 1.00 19.14 ? 356 TYR A O 1 ATOM 2435 C CB . TYR A 1 363 ? 1.439 36.944 49.558 1.00 19.84 ? 356 TYR A CB 1 ATOM 2436 C CG . TYR A 1 363 ? 0.400 36.104 48.884 1.00 21.12 ? 356 TYR A CG 1 ATOM 2437 C CD1 . TYR A 1 363 ? -0.927 36.094 49.362 1.00 22.63 ? 356 TYR A CD1 1 ATOM 2438 C CD2 . TYR A 1 363 ? 0.732 35.324 47.776 1.00 23.25 ? 356 TYR A CD2 1 ATOM 2439 C CE1 . TYR A 1 363 ? -1.916 35.312 48.718 1.00 24.37 ? 356 TYR A CE1 1 ATOM 2440 C CE2 . TYR A 1 363 ? -0.239 34.542 47.127 1.00 25.99 ? 356 TYR A CE2 1 ATOM 2441 C CZ . TYR A 1 363 ? -1.558 34.558 47.627 1.00 25.55 ? 356 TYR A CZ 1 ATOM 2442 O OH . TYR A 1 363 ? -2.505 33.817 46.985 1.00 29.02 ? 356 TYR A OH 1 ATOM 2443 N N . ASN A 1 364 ? 2.290 40.132 50.452 1.00 19.58 ? 357 ASN A N 1 ATOM 2444 C CA . ASN A 1 364 ? 3.197 40.731 51.447 1.00 19.80 ? 357 ASN A CA 1 ATOM 2445 C C . ASN A 1 364 ? 2.799 40.240 52.829 1.00 20.45 ? 357 ASN A C 1 ATOM 2446 O O . ASN A 1 364 ? 1.575 40.134 53.124 1.00 22.98 ? 357 ASN A O 1 ATOM 2447 C CB . ASN A 1 364 ? 3.092 42.272 51.489 1.00 18.81 ? 357 ASN A CB 1 ATOM 2448 C CG . ASN A 1 364 ? 3.408 42.931 50.159 1.00 21.01 ? 357 ASN A CG 1 ATOM 2449 O OD1 . ASN A 1 364 ? 4.331 42.534 49.430 1.00 19.89 ? 357 ASN A OD1 1 ATOM 2450 N ND2 . ASN A 1 364 ? 2.699 44.008 49.876 1.00 20.75 ? 357 ASN A ND2 1 ATOM 2451 N N . VAL A 1 365 ? 3.801 40.002 53.698 1.00 20.96 ? 358 VAL A N 1 ATOM 2452 C CA . VAL A 1 365 ? 3.490 39.776 55.108 1.00 20.41 ? 358 VAL A CA 1 ATOM 2453 C C . VAL A 1 365 ? 3.704 41.104 55.869 1.00 21.27 ? 358 VAL A C 1 ATOM 2454 O O . VAL A 1 365 ? 4.747 41.716 55.741 1.00 22.42 ? 358 VAL A O 1 ATOM 2455 C CB . VAL A 1 365 ? 4.361 38.675 55.773 1.00 21.22 ? 358 VAL A CB 1 ATOM 2456 C CG1 . VAL A 1 365 ? 3.755 38.338 57.157 1.00 21.54 ? 358 VAL A CG1 1 ATOM 2457 C CG2 . VAL A 1 365 ? 4.448 37.405 54.862 1.00 22.25 ? 358 VAL A CG2 1 ATOM 2458 N N . ILE A 1 366 ? 2.700 41.514 56.638 1.00 21.10 ? 359 ILE A N 1 ATOM 2459 C CA . ILE A 1 366 ? 2.714 42.806 57.353 1.00 20.48 ? 359 ILE A CA 1 ATOM 2460 C C . ILE A 1 366 ? 2.503 42.505 58.839 1.00 20.79 ? 359 ILE A C 1 ATOM 2461 O O . ILE A 1 366 ? 1.426 42.012 59.228 1.00 21.21 ? 359 ILE A O 1 ATOM 2462 C CB . ILE A 1 366 ? 1.597 43.797 56.835 1.00 19.87 ? 359 ILE A CB 1 ATOM 2463 C CG1 . ILE A 1 366 ? 1.700 43.995 55.297 1.00 19.52 ? 359 ILE A CG1 1 ATOM 2464 C CG2 . ILE A 1 366 ? 1.661 45.127 57.641 1.00 20.76 ? 359 ILE A CG2 1 ATOM 2465 C CD1 . ILE A 1 366 ? 3.020 44.680 54.874 1.00 21.37 ? 359 ILE A CD1 1 ATOM 2466 N N . GLY A 1 367 ? 3.559 42.719 59.628 1.00 20.42 ? 360 GLY A N 1 ATOM 2467 C CA . GLY A 1 367 ? 3.539 42.446 61.091 1.00 20.92 ? 360 GLY A CA 1 ATOM 2468 C C . GLY A 1 367 ? 3.461 43.763 61.857 1.00 21.51 ? 360 GLY A C 1 ATOM 2469 O O . GLY A 1 367 ? 4.065 44.727 61.444 1.00 21.66 ? 360 GLY A O 1 ATOM 2470 N N . THR A 1 368 ? 2.686 43.825 62.940 1.00 22.59 ? 361 THR A N 1 ATOM 2471 C CA . THR A 1 368 ? 2.492 45.092 63.692 1.00 23.86 ? 361 THR A CA 1 ATOM 2472 C C . THR A 1 368 ? 2.918 44.851 65.130 1.00 25.37 ? 361 THR A C 1 ATOM 2473 O O . THR A 1 368 ? 2.458 43.865 65.758 1.00 25.93 ? 361 THR A O 1 ATOM 2474 C CB . THR A 1 368 ? 0.988 45.503 63.721 1.00 24.54 ? 361 THR A CB 1 ATOM 2475 O OG1 . THR A 1 368 ? 0.545 45.732 62.398 1.00 22.14 ? 361 THR A OG1 1 ATOM 2476 C CG2 . THR A 1 368 ? 0.697 46.798 64.561 1.00 24.87 ? 361 THR A CG2 1 ATOM 2477 N N . LEU A 1 369 ? 3.756 45.760 65.672 1.00 24.64 ? 362 LEU A N 1 ATOM 2478 C CA . LEU A 1 369 ? 4.028 45.789 67.112 1.00 24.88 ? 362 LEU A CA 1 ATOM 2479 C C . LEU A 1 369 ? 3.496 47.149 67.615 1.00 24.68 ? 362 LEU A C 1 ATOM 2480 O O . LEU A 1 369 ? 4.154 48.155 67.388 1.00 24.85 ? 362 LEU A O 1 ATOM 2481 C CB . LEU A 1 369 ? 5.556 45.647 67.360 1.00 24.81 ? 362 LEU A CB 1 ATOM 2482 C CG . LEU A 1 369 ? 6.039 45.618 68.818 1.00 29.42 ? 362 LEU A CG 1 ATOM 2483 C CD1 . LEU A 1 369 ? 5.246 44.635 69.657 1.00 30.70 ? 362 LEU A CD1 1 ATOM 2484 C CD2 . LEU A 1 369 ? 7.550 45.290 68.842 1.00 29.04 ? 362 LEU A CD2 1 ATOM 2485 N N A ARG A 1 370 ? 2.312 47.178 68.238 0.40 23.52 ? 363 ARG A N 1 ATOM 2486 N N B ARG A 1 370 ? 2.335 47.170 68.269 0.40 23.89 ? 363 ARG A N 1 ATOM 2487 C CA A ARG A 1 370 ? 1.652 48.465 68.569 0.50 24.19 ? 363 ARG A CA 1 ATOM 2488 C CA B ARG A 1 370 ? 1.708 48.451 68.634 0.50 24.97 ? 363 ARG A CA 1 ATOM 2489 C C A ARG A 1 370 ? 2.456 49.278 69.605 0.40 23.86 ? 363 ARG A C 1 ATOM 2490 C C B ARG A 1 370 ? 2.537 49.275 69.616 0.40 24.28 ? 363 ARG A C 1 ATOM 2491 O O A ARG A 1 370 ? 2.892 48.729 70.597 0.40 23.28 ? 363 ARG A O 1 ATOM 2492 O O B ARG A 1 370 ? 3.036 48.753 70.595 0.40 23.79 ? 363 ARG A O 1 ATOM 2493 C CB A ARG A 1 370 ? 0.213 48.220 69.071 0.50 25.06 ? 363 ARG A CB 1 ATOM 2494 C CB B ARG A 1 370 ? 0.342 48.211 69.256 0.50 26.04 ? 363 ARG A CB 1 ATOM 2495 C CG A ARG A 1 370 ? -0.534 49.477 69.558 0.50 24.24 ? 363 ARG A CG 1 ATOM 2496 C CG B ARG A 1 370 ? -0.637 47.566 68.323 0.50 26.98 ? 363 ARG A CG 1 ATOM 2497 C CD A ARG A 1 370 ? -2.079 49.266 69.711 0.50 30.49 ? 363 ARG A CD 1 ATOM 2498 C CD B ARG A 1 370 ? -1.918 47.256 69.110 0.50 33.99 ? 363 ARG A CD 1 ATOM 2499 N NE A ARG A 1 370 ? -2.776 50.482 70.203 0.50 33.78 ? 363 ARG A NE 1 ATOM 2500 N NE B ARG A 1 370 ? -2.664 46.196 68.453 0.50 35.99 ? 363 ARG A NE 1 ATOM 2501 C CZ A ARG A 1 370 ? -3.626 51.245 69.484 0.50 32.40 ? 363 ARG A CZ 1 ATOM 2502 C CZ B ARG A 1 370 ? -3.241 45.195 69.089 0.50 36.77 ? 363 ARG A CZ 1 ATOM 2503 N NH1 A ARG A 1 370 ? -3.966 50.935 68.240 0.50 29.91 ? 363 ARG A NH1 1 ATOM 2504 N NH1 B ARG A 1 370 ? -3.165 45.110 70.410 0.50 39.44 ? 363 ARG A NH1 1 ATOM 2505 N NH2 A ARG A 1 370 ? -4.152 52.327 70.020 0.50 34.48 ? 363 ARG A NH2 1 ATOM 2506 N NH2 B ARG A 1 370 ? -3.882 44.280 68.396 0.50 37.47 ? 363 ARG A NH2 1 ATOM 2507 N N . GLY A 1 371 ? 2.697 50.559 69.310 1.00 23.78 ? 364 GLY A N 1 ATOM 2508 C CA . GLY A 1 371 ? 3.332 51.518 70.230 1.00 24.45 ? 364 GLY A CA 1 ATOM 2509 C C . GLY A 1 371 ? 2.538 51.735 71.532 1.00 26.08 ? 364 GLY A C 1 ATOM 2510 O O . GLY A 1 371 ? 1.301 51.755 71.530 1.00 27.40 ? 364 GLY A O 1 ATOM 2511 N N . ALA A 1 372 ? 3.269 51.855 72.637 1.00 27.01 ? 365 ALA A N 1 ATOM 2512 C CA . ALA A 1 372 ? 2.660 52.108 73.970 1.00 28.58 ? 365 ALA A CA 1 ATOM 2513 C C . ALA A 1 372 ? 2.125 53.525 74.092 1.00 29.68 ? 365 ALA A C 1 ATOM 2514 O O . ALA A 1 372 ? 1.111 53.765 74.769 1.00 30.41 ? 365 ALA A O 1 ATOM 2515 C CB . ALA A 1 372 ? 3.685 51.841 75.075 1.00 28.71 ? 365 ALA A CB 1 ATOM 2516 N N . VAL A 1 373 ? 2.797 54.477 73.440 1.00 28.46 ? 366 VAL A N 1 ATOM 2517 C CA . VAL A 1 373 ? 2.494 55.898 73.691 1.00 29.15 ? 366 VAL A CA 1 ATOM 2518 C C . VAL A 1 373 ? 2.020 56.609 72.404 1.00 27.50 ? 366 VAL A C 1 ATOM 2519 O O . VAL A 1 373 ? 1.081 57.401 72.435 1.00 26.47 ? 366 VAL A O 1 ATOM 2520 C CB . VAL A 1 373 ? 3.725 56.639 74.282 1.00 29.68 ? 366 VAL A CB 1 ATOM 2521 C CG1 . VAL A 1 373 ? 3.421 58.110 74.532 1.00 31.38 ? 366 VAL A CG1 1 ATOM 2522 C CG2 . VAL A 1 373 ? 4.182 55.986 75.592 1.00 32.07 ? 366 VAL A CG2 1 ATOM 2523 N N . GLU A 1 374 ? 2.681 56.328 71.274 1.00 25.55 ? 367 GLU A N 1 ATOM 2524 C CA . GLU A 1 374 ? 2.282 56.926 69.969 1.00 25.39 ? 367 GLU A CA 1 ATOM 2525 C C . GLU A 1 374 ? 2.024 55.815 68.952 1.00 23.70 ? 367 GLU A C 1 ATOM 2526 O O . GLU A 1 374 ? 2.801 55.647 68.005 1.00 22.71 ? 367 GLU A O 1 ATOM 2527 C CB . GLU A 1 374 ? 3.359 57.874 69.418 1.00 23.87 ? 367 GLU A CB 1 ATOM 2528 C CG . GLU A 1 374 ? 3.724 59.027 70.379 1.00 27.08 ? 367 GLU A CG 1 ATOM 2529 C CD . GLU A 1 374 ? 4.694 59.994 69.741 1.00 27.39 ? 367 GLU A CD 1 ATOM 2530 O OE1 . GLU A 1 374 ? 4.248 60.925 69.025 1.00 27.72 ? 367 GLU A OE1 1 ATOM 2531 O OE2 . GLU A 1 374 ? 5.920 59.838 69.960 1.00 29.69 ? 367 GLU A OE2 1 ATOM 2532 N N . PRO A 1 375 ? 0.916 55.074 69.135 1.00 24.51 ? 368 PRO A N 1 ATOM 2533 C CA . PRO A 1 375 ? 0.568 53.966 68.247 1.00 23.24 ? 368 PRO A CA 1 ATOM 2534 C C . PRO A 1 375 ? 0.270 54.449 66.827 1.00 22.42 ? 368 PRO A C 1 ATOM 2535 O O . PRO A 1 375 ? 0.354 53.658 65.912 1.00 21.56 ? 368 PRO A O 1 ATOM 2536 C CB . PRO A 1 375 ? -0.678 53.361 68.899 1.00 22.70 ? 368 PRO A CB 1 ATOM 2537 C CG . PRO A 1 375 ? -1.209 54.404 69.763 1.00 26.93 ? 368 PRO A CG 1 ATOM 2538 C CD . PRO A 1 375 ? -0.038 55.203 70.257 1.00 25.22 ? 368 PRO A CD 1 ATOM 2539 N N . ASP A 1 376 ? -0.056 55.745 66.665 1.00 23.19 ? 369 ASP A N 1 ATOM 2540 C CA . ASP A 1 376 ? -0.302 56.340 65.335 1.00 22.95 ? 369 ASP A CA 1 ATOM 2541 C C . ASP A 1 376 ? 0.946 56.958 64.718 1.00 22.17 ? 369 ASP A C 1 ATOM 2542 O O . ASP A 1 376 ? 0.824 57.835 63.851 1.00 20.57 ? 369 ASP A O 1 ATOM 2543 C CB . ASP A 1 376 ? -1.410 57.433 65.420 1.00 23.09 ? 369 ASP A CB 1 ATOM 2544 C CG . ASP A 1 376 ? -0.940 58.669 66.165 1.00 27.00 ? 369 ASP A CG 1 ATOM 2545 O OD1 . ASP A 1 376 ? 0.047 58.564 66.937 1.00 27.67 ? 369 ASP A OD1 1 ATOM 2546 O OD2 . ASP A 1 376 ? -1.544 59.755 65.988 1.00 29.89 ? 369 ASP A OD2 1 ATOM 2547 N N . ARG A 1 377 ? 2.133 56.464 65.093 1.00 21.69 ? 370 ARG A N 1 ATOM 2548 C CA . ARG A 1 377 ? 3.388 56.892 64.481 1.00 20.42 ? 370 ARG A CA 1 ATOM 2549 C C . ARG A 1 377 ? 4.057 55.596 64.106 1.00 21.23 ? 370 ARG A C 1 ATOM 2550 O O . ARG A 1 377 ? 4.153 54.679 64.958 1.00 21.42 ? 370 ARG A O 1 ATOM 2551 C CB . ARG A 1 377 ? 4.260 57.695 65.473 1.00 19.98 ? 370 ARG A CB 1 ATOM 2552 C CG . ARG A 1 377 ? 3.636 59.106 65.768 1.00 21.09 ? 370 ARG A CG 1 ATOM 2553 C CD . ARG A 1 377 ? 3.801 59.965 64.473 1.00 22.75 ? 370 ARG A CD 1 ATOM 2554 N NE . ARG A 1 377 ? 3.200 61.317 64.516 1.00 20.18 ? 370 ARG A NE 1 ATOM 2555 C CZ . ARG A 1 377 ? 1.955 61.620 64.115 1.00 21.80 ? 370 ARG A CZ 1 ATOM 2556 N NH1 . ARG A 1 377 ? 1.080 60.668 63.711 1.00 20.02 ? 370 ARG A NH1 1 ATOM 2557 N NH2 . ARG A 1 377 ? 1.576 62.910 64.121 1.00 21.17 ? 370 ARG A NH2 1 ATOM 2558 N N . TYR A 1 378 ? 4.449 55.483 62.835 1.00 19.19 ? 371 TYR A N 1 ATOM 2559 C CA . TYR A 1 378 ? 4.947 54.187 62.282 1.00 19.79 ? 371 TYR A CA 1 ATOM 2560 C C . TYR A 1 378 ? 6.403 54.215 61.898 1.00 19.46 ? 371 TYR A C 1 ATOM 2561 O O . TYR A 1 378 ? 6.812 55.042 61.070 1.00 20.79 ? 371 TYR A O 1 ATOM 2562 C CB . TYR A 1 378 ? 4.165 53.768 61.012 1.00 18.24 ? 371 TYR A CB 1 ATOM 2563 C CG . TYR A 1 378 ? 2.653 53.713 61.151 1.00 22.08 ? 371 TYR A CG 1 ATOM 2564 C CD1 . TYR A 1 378 ? 2.032 53.321 62.343 1.00 22.91 ? 371 TYR A CD1 1 ATOM 2565 C CD2 . TYR A 1 378 ? 1.840 54.032 60.076 1.00 18.59 ? 371 TYR A CD2 1 ATOM 2566 C CE1 . TYR A 1 378 ? 0.628 53.280 62.424 1.00 23.82 ? 371 TYR A CE1 1 ATOM 2567 C CE2 . TYR A 1 378 ? 0.449 53.974 60.142 1.00 20.24 ? 371 TYR A CE2 1 ATOM 2568 C CZ . TYR A 1 378 ? -0.155 53.576 61.297 1.00 22.92 ? 371 TYR A CZ 1 ATOM 2569 O OH . TYR A 1 378 ? -1.532 53.540 61.398 1.00 21.16 ? 371 TYR A OH 1 ATOM 2570 N N . VAL A 1 379 ? 7.194 53.312 62.495 1.00 20.14 ? 372 VAL A N 1 ATOM 2571 C CA . VAL A 1 379 ? 8.550 53.058 62.047 1.00 19.41 ? 372 VAL A CA 1 ATOM 2572 C C . VAL A 1 379 ? 8.499 51.700 61.324 1.00 19.29 ? 372 VAL A C 1 ATOM 2573 O O . VAL A 1 379 ? 8.051 50.677 61.875 1.00 19.67 ? 372 VAL A O 1 ATOM 2574 C CB . VAL A 1 379 ? 9.536 53.025 63.276 1.00 20.25 ? 372 VAL A CB 1 ATOM 2575 C CG1 . VAL A 1 379 ? 10.990 52.657 62.856 1.00 23.05 ? 372 VAL A CG1 1 ATOM 2576 C CG2 . VAL A 1 379 ? 9.493 54.359 63.980 1.00 21.40 ? 372 VAL A CG2 1 ATOM 2577 N N . ILE A 1 380 ? 8.942 51.711 60.064 1.00 18.78 ? 373 ILE A N 1 ATOM 2578 C CA . ILE A 1 380 ? 8.788 50.520 59.204 1.00 18.75 ? 373 ILE A CA 1 ATOM 2579 C C . ILE A 1 380 ? 10.141 49.882 58.905 1.00 18.97 ? 373 ILE A C 1 ATOM 2580 O O . ILE A 1 380 ? 11.081 50.551 58.480 1.00 20.45 ? 373 ILE A O 1 ATOM 2581 C CB . ILE A 1 380 ? 8.047 50.906 57.901 1.00 16.75 ? 373 ILE A CB 1 ATOM 2582 C CG1 . ILE A 1 380 ? 6.759 51.647 58.262 1.00 20.08 ? 373 ILE A CG1 1 ATOM 2583 C CG2 . ILE A 1 380 ? 7.844 49.623 56.975 1.00 16.09 ? 373 ILE A CG2 1 ATOM 2584 C CD1 . ILE A 1 380 ? 5.937 52.140 57.021 1.00 22.77 ? 373 ILE A CD1 1 ATOM 2585 N N . LEU A 1 381 ? 10.253 48.581 59.181 1.00 18.72 ? 374 LEU A N 1 ATOM 2586 C CA . LEU A 1 381 ? 11.381 47.783 58.724 1.00 18.60 ? 374 LEU A CA 1 ATOM 2587 C C . LEU A 1 381 ? 10.871 46.839 57.646 1.00 18.80 ? 374 LEU A C 1 ATOM 2588 O O . LEU A 1 381 ? 10.086 45.936 57.933 1.00 20.57 ? 374 LEU A O 1 ATOM 2589 C CB . LEU A 1 381 ? 12.027 47.023 59.900 1.00 18.52 ? 374 LEU A CB 1 ATOM 2590 C CG . LEU A 1 381 ? 13.136 46.007 59.566 1.00 20.90 ? 374 LEU A CG 1 ATOM 2591 C CD1 . LEU A 1 381 ? 14.362 46.747 58.982 1.00 18.72 ? 374 LEU A CD1 1 ATOM 2592 C CD2 . LEU A 1 381 ? 13.539 45.191 60.813 1.00 19.27 ? 374 LEU A CD2 1 ATOM 2593 N N . GLY A 1 382 ? 11.359 47.012 56.411 1.00 17.89 ? 375 GLY A N 1 ATOM 2594 C CA . GLY A 1 382 ? 10.778 46.271 55.272 1.00 18.40 ? 375 GLY A CA 1 ATOM 2595 C C . GLY A 1 382 ? 11.855 45.736 54.353 1.00 18.74 ? 375 GLY A C 1 ATOM 2596 O O . GLY A 1 382 ? 12.853 46.420 54.082 1.00 18.46 ? 375 GLY A O 1 ATOM 2597 N N . GLY A 1 383 ? 11.640 44.523 53.837 1.00 19.39 ? 376 GLY A N 1 ATOM 2598 C CA . GLY A 1 383 ? 12.569 43.993 52.848 1.00 18.88 ? 376 GLY A CA 1 ATOM 2599 C C . GLY A 1 383 ? 11.860 42.862 52.140 1.00 20.20 ? 376 GLY A C 1 ATOM 2600 O O . GLY A 1 383 ? 10.876 42.340 52.632 1.00 19.75 ? 376 GLY A O 1 ATOM 2601 N N . HIS A 1 384 ? 12.365 42.477 50.976 1.00 19.53 ? 377 HIS A N 1 ATOM 2602 C CA . HIS A 1 384 ? 11.628 41.475 50.167 1.00 18.85 ? 377 HIS A CA 1 ATOM 2603 C C . HIS A 1 384 ? 12.030 40.039 50.463 1.00 20.03 ? 377 HIS A C 1 ATOM 2604 O O . HIS A 1 384 ? 13.067 39.794 51.108 1.00 21.43 ? 377 HIS A O 1 ATOM 2605 C CB . HIS A 1 384 ? 11.732 41.841 48.671 1.00 17.99 ? 377 HIS A CB 1 ATOM 2606 C CG . HIS A 1 384 ? 13.039 41.498 47.997 1.00 15.43 ? 377 HIS A CG 1 ATOM 2607 N ND1 . HIS A 1 384 ? 13.134 40.414 47.158 1.00 17.68 ? 377 HIS A ND1 1 ATOM 2608 C CD2 . HIS A 1 384 ? 14.222 42.165 47.882 1.00 16.05 ? 377 HIS A CD2 1 ATOM 2609 C CE1 . HIS A 1 384 ? 14.332 40.404 46.568 1.00 14.76 ? 377 HIS A CE1 1 ATOM 2610 N NE2 . HIS A 1 384 ? 15.020 41.433 47.020 1.00 16.92 ? 377 HIS A NE2 1 ATOM 2611 N N . ARG A 1 385 ? 11.191 39.125 49.985 1.00 19.16 ? 378 ARG A N 1 ATOM 2612 C CA . ARG A 1 385 ? 11.242 37.710 50.270 1.00 20.11 ? 378 ARG A CA 1 ATOM 2613 C C . ARG A 1 385 ? 11.349 36.939 48.957 1.00 19.50 ? 378 ARG A C 1 ATOM 2614 O O . ARG A 1 385 ? 11.873 35.823 48.941 1.00 20.78 ? 378 ARG A O 1 ATOM 2615 C CB . ARG A 1 385 ? 9.919 37.306 50.963 1.00 19.51 ? 378 ARG A CB 1 ATOM 2616 C CG . ARG A 1 385 ? 9.792 35.818 51.327 1.00 20.38 ? 378 ARG A CG 1 ATOM 2617 C CD . ARG A 1 385 ? 8.385 35.473 51.834 1.00 22.12 ? 378 ARG A CD 1 ATOM 2618 N NE . ARG A 1 385 ? 7.372 35.561 50.741 1.00 20.92 ? 378 ARG A NE 1 ATOM 2619 C CZ . ARG A 1 385 ? 6.476 36.531 50.573 1.00 20.73 ? 378 ARG A CZ 1 ATOM 2620 N NH1 . ARG A 1 385 ? 6.398 37.564 51.421 1.00 20.44 ? 378 ARG A NH1 1 ATOM 2621 N NH2 . ARG A 1 385 ? 5.626 36.486 49.524 1.00 20.39 ? 378 ARG A NH2 1 ATOM 2622 N N . ASP A 1 386 ? 10.817 37.498 47.848 1.00 18.26 ? 379 ASP A N 1 ATOM 2623 C CA . ASP A 1 386 ? 10.833 36.761 46.553 1.00 18.40 ? 379 ASP A CA 1 ATOM 2624 C C . ASP A 1 386 ? 12.242 36.784 46.042 1.00 18.96 ? 379 ASP A C 1 ATOM 2625 O O . ASP A 1 386 ? 12.951 37.748 46.311 1.00 19.01 ? 379 ASP A O 1 ATOM 2626 C CB . ASP A 1 386 ? 9.933 37.425 45.517 1.00 16.98 ? 379 ASP A CB 1 ATOM 2627 C CG . ASP A 1 386 ? 10.387 38.861 45.196 1.00 18.92 ? 379 ASP A CG 1 ATOM 2628 O OD1 . ASP A 1 386 ? 10.411 39.749 46.118 1.00 19.20 ? 379 ASP A OD1 1 ATOM 2629 O OD2 . ASP A 1 386 ? 10.642 39.103 43.993 1.00 17.94 ? 379 ASP A OD2 1 ATOM 2630 N N . SER A 1 387 ? 12.655 35.739 45.336 1.00 19.07 ? 380 SER A N 1 ATOM 2631 C CA . SER A 1 387 ? 14.052 35.640 44.876 1.00 20.44 ? 380 SER A CA 1 ATOM 2632 C C . SER A 1 387 ? 14.039 35.163 43.426 1.00 20.92 ? 380 SER A C 1 ATOM 2633 O O . SER A 1 387 ? 13.032 34.591 42.967 1.00 20.83 ? 380 SER A O 1 ATOM 2634 C CB . SER A 1 387 ? 14.850 34.663 45.796 1.00 20.48 ? 380 SER A CB 1 ATOM 2635 O OG . SER A 1 387 ? 14.344 33.323 45.726 1.00 22.77 ? 380 SER A OG 1 ATOM 2636 N N . TRP A 1 388 ? 15.151 35.342 42.701 1.00 21.92 ? 381 TRP A N 1 ATOM 2637 C CA . TRP A 1 388 ? 15.194 34.784 41.348 1.00 21.51 ? 381 TRP A CA 1 ATOM 2638 C C . TRP A 1 388 ? 15.288 33.272 41.400 1.00 22.64 ? 381 TRP A C 1 ATOM 2639 O O . TRP A 1 388 ? 14.520 32.597 40.715 1.00 23.80 ? 381 TRP A O 1 ATOM 2640 C CB . TRP A 1 388 ? 16.318 35.419 40.475 1.00 21.79 ? 381 TRP A CB 1 ATOM 2641 C CG . TRP A 1 388 ? 15.846 36.771 39.940 1.00 21.60 ? 381 TRP A CG 1 ATOM 2642 C CD1 . TRP A 1 388 ? 16.363 38.016 40.239 1.00 22.32 ? 381 TRP A CD1 1 ATOM 2643 C CD2 . TRP A 1 388 ? 14.703 36.997 39.083 1.00 22.28 ? 381 TRP A CD2 1 ATOM 2644 N NE1 . TRP A 1 388 ? 15.635 39.012 39.573 1.00 22.25 ? 381 TRP A NE1 1 ATOM 2645 C CE2 . TRP A 1 388 ? 14.610 38.407 38.864 1.00 22.22 ? 381 TRP A CE2 1 ATOM 2646 C CE3 . TRP A 1 388 ? 13.781 36.136 38.435 1.00 21.08 ? 381 TRP A CE3 1 ATOM 2647 C CZ2 . TRP A 1 388 ? 13.599 38.977 38.071 1.00 22.63 ? 381 TRP A CZ2 1 ATOM 2648 C CZ3 . TRP A 1 388 ? 12.748 36.728 37.656 1.00 19.64 ? 381 TRP A CZ3 1 ATOM 2649 C CH2 . TRP A 1 388 ? 12.667 38.133 37.500 1.00 20.48 ? 381 TRP A CH2 1 ATOM 2650 N N . VAL A 1 389 ? 16.190 32.736 42.232 1.00 21.78 ? 382 VAL A N 1 ATOM 2651 C CA . VAL A 1 389 ? 16.286 31.283 42.430 1.00 22.04 ? 382 VAL A CA 1 ATOM 2652 C C . VAL A 1 389 ? 16.338 31.056 43.957 1.00 22.28 ? 382 VAL A C 1 ATOM 2653 O O . VAL A 1 389 ? 15.344 31.247 44.609 1.00 21.08 ? 382 VAL A O 1 ATOM 2654 C CB . VAL A 1 389 ? 17.457 30.613 41.634 1.00 22.04 ? 382 VAL A CB 1 ATOM 2655 C CG1 . VAL A 1 389 ? 17.292 29.063 41.640 1.00 22.50 ? 382 VAL A CG1 1 ATOM 2656 C CG2 . VAL A 1 389 ? 17.436 31.060 40.136 1.00 23.44 ? 382 VAL A CG2 1 ATOM 2657 N N . PHE A 1 390 ? 17.496 30.702 44.523 1.00 21.84 ? 383 PHE A N 1 ATOM 2658 C CA . PHE A 1 390 ? 17.564 30.341 45.942 1.00 21.82 ? 383 PHE A CA 1 ATOM 2659 C C . PHE A 1 390 ? 17.696 31.555 46.859 1.00 22.06 ? 383 PHE A C 1 ATOM 2660 O O . PHE A 1 390 ? 17.315 31.501 48.046 1.00 22.41 ? 383 PHE A O 1 ATOM 2661 C CB . PHE A 1 390 ? 18.726 29.366 46.181 1.00 21.85 ? 383 PHE A CB 1 ATOM 2662 C CG . PHE A 1 390 ? 18.581 28.115 45.387 1.00 23.92 ? 383 PHE A CG 1 ATOM 2663 C CD1 . PHE A 1 390 ? 17.583 27.180 45.726 1.00 24.51 ? 383 PHE A CD1 1 ATOM 2664 C CD2 . PHE A 1 390 ? 19.386 27.881 44.279 1.00 25.72 ? 383 PHE A CD2 1 ATOM 2665 C CE1 . PHE A 1 390 ? 17.409 26.003 44.965 1.00 25.24 ? 383 PHE A CE1 1 ATOM 2666 C CE2 . PHE A 1 390 ? 19.223 26.700 43.505 1.00 25.62 ? 383 PHE A CE2 1 ATOM 2667 C CZ . PHE A 1 390 ? 18.219 25.782 43.842 1.00 24.27 ? 383 PHE A CZ 1 ATOM 2668 N N . GLY A 1 391 ? 18.202 32.662 46.319 1.00 21.59 ? 384 GLY A N 1 ATOM 2669 C CA . GLY A 1 391 ? 18.228 33.911 47.121 1.00 21.24 ? 384 GLY A CA 1 ATOM 2670 C C . GLY A 1 391 ? 19.191 33.888 48.297 1.00 21.42 ? 384 GLY A C 1 ATOM 2671 O O . GLY A 1 391 ? 18.955 34.586 49.297 1.00 21.48 ? 384 GLY A O 1 ATOM 2672 N N . GLY A 1 392 ? 20.279 33.122 48.158 1.00 22.00 ? 385 GLY A N 1 ATOM 2673 C CA . GLY A 1 392 ? 21.279 32.913 49.217 1.00 21.84 ? 385 GLY A CA 1 ATOM 2674 C C . GLY A 1 392 ? 21.761 34.246 49.762 1.00 23.20 ? 385 GLY A C 1 ATOM 2675 O O . GLY A 1 392 ? 21.944 34.398 50.960 1.00 23.78 ? 385 GLY A O 1 ATOM 2676 N N . ILE A 1 393 ? 21.988 35.220 48.880 1.00 22.46 ? 386 ILE A N 1 ATOM 2677 C CA . ILE A 1 393 ? 22.288 36.576 49.365 1.00 22.79 ? 386 ILE A CA 1 ATOM 2678 C C . ILE A 1 393 ? 21.049 37.450 49.181 1.00 22.90 ? 386 ILE A C 1 ATOM 2679 O O . ILE A 1 393 ? 20.512 38.055 50.146 1.00 22.92 ? 386 ILE A O 1 ATOM 2680 C CB . ILE A 1 393 ? 23.510 37.172 48.666 1.00 22.31 ? 386 ILE A CB 1 ATOM 2681 C CG1 . ILE A 1 393 ? 24.804 36.474 49.185 1.00 24.46 ? 386 ILE A CG1 1 ATOM 2682 C CG2 . ILE A 1 393 ? 23.542 38.715 48.861 1.00 23.00 ? 386 ILE A CG2 1 ATOM 2683 C CD1 . ILE A 1 393 ? 26.026 36.786 48.308 1.00 27.05 ? 386 ILE A CD1 1 ATOM 2684 N N . ASP A 1 394 ? 20.577 37.471 47.945 1.00 21.97 ? 387 ASP A N 1 ATOM 2685 C CA . ASP A 1 394 ? 19.498 38.371 47.583 1.00 21.51 ? 387 ASP A CA 1 ATOM 2686 C C . ASP A 1 394 ? 18.145 37.641 47.419 1.00 20.15 ? 387 ASP A C 1 ATOM 2687 O O . ASP A 1 394 ? 17.938 36.950 46.419 1.00 21.69 ? 387 ASP A O 1 ATOM 2688 C CB . ASP A 1 394 ? 19.936 39.025 46.288 1.00 20.58 ? 387 ASP A CB 1 ATOM 2689 C CG . ASP A 1 394 ? 18.919 40.007 45.760 1.00 22.63 ? 387 ASP A CG 1 ATOM 2690 O OD1 . ASP A 1 394 ? 18.021 40.394 46.507 1.00 23.03 ? 387 ASP A OD1 1 ATOM 2691 O OD2 . ASP A 1 394 ? 19.049 40.389 44.579 1.00 23.14 ? 387 ASP A OD2 1 ATOM 2692 N N . PRO A 1 395 ? 17.206 37.801 48.367 1.00 20.06 ? 388 PRO A N 1 ATOM 2693 C CA . PRO A 1 395 ? 17.230 38.694 49.538 1.00 19.72 ? 388 PRO A CA 1 ATOM 2694 C C . PRO A 1 395 ? 17.440 37.991 50.878 1.00 21.31 ? 388 PRO A C 1 ATOM 2695 O O . PRO A 1 395 ? 17.354 38.639 51.913 1.00 21.14 ? 388 PRO A O 1 ATOM 2696 C CB . PRO A 1 395 ? 15.789 39.230 49.524 1.00 19.51 ? 388 PRO A CB 1 ATOM 2697 C CG . PRO A 1 395 ? 14.909 37.948 49.142 1.00 19.22 ? 388 PRO A CG 1 ATOM 2698 C CD . PRO A 1 395 ? 15.870 37.167 48.181 1.00 18.62 ? 388 PRO A CD 1 ATOM 2699 N N . GLN A 1 396 ? 17.611 36.666 50.892 1.00 20.66 ? 389 GLN A N 1 ATOM 2700 C CA . GLN A 1 396 ? 17.394 35.965 52.172 1.00 21.93 ? 389 GLN A CA 1 ATOM 2701 C C . GLN A 1 396 ? 18.453 36.323 53.232 1.00 21.62 ? 389 GLN A C 1 ATOM 2702 O O . GLN A 1 396 ? 18.157 36.224 54.408 1.00 22.58 ? 389 GLN A O 1 ATOM 2703 C CB . GLN A 1 396 ? 17.329 34.438 52.012 1.00 22.12 ? 389 GLN A CB 1 ATOM 2704 C CG . GLN A 1 396 ? 16.253 33.929 51.042 1.00 22.96 ? 389 GLN A CG 1 ATOM 2705 C CD . GLN A 1 396 ? 14.831 34.563 51.187 1.00 23.08 ? 389 GLN A CD 1 ATOM 2706 O OE1 . GLN A 1 396 ? 14.460 35.174 52.198 1.00 23.05 ? 389 GLN A OE1 1 ATOM 2707 N NE2 . GLN A 1 396 ? 14.017 34.343 50.166 1.00 19.80 ? 389 GLN A NE2 1 ATOM 2708 N N . SER A 1 397 ? 19.643 36.757 52.823 1.00 21.27 ? 390 SER A N 1 ATOM 2709 C CA . SER A 1 397 ? 20.585 37.319 53.841 1.00 22.64 ? 390 SER A CA 1 ATOM 2710 C C . SER A 1 397 ? 19.996 38.522 54.592 1.00 21.87 ? 390 SER A C 1 ATOM 2711 O O . SER A 1 397 ? 20.265 38.696 55.795 1.00 22.58 ? 390 SER A O 1 ATOM 2712 C CB . SER A 1 397 ? 21.965 37.660 53.276 1.00 23.72 ? 390 SER A CB 1 ATOM 2713 O OG . SER A 1 397 ? 21.882 38.744 52.411 1.00 24.37 ? 390 SER A OG 1 ATOM 2714 N N . GLY A 1 398 ? 19.132 39.281 53.905 1.00 20.73 ? 391 GLY A N 1 ATOM 2715 C CA . GLY A 1 398 ? 18.397 40.407 54.493 1.00 19.01 ? 391 GLY A CA 1 ATOM 2716 C C . GLY A 1 398 ? 17.206 39.908 55.307 1.00 20.56 ? 391 GLY A C 1 ATOM 2717 O O . GLY A 1 398 ? 17.042 40.305 56.468 1.00 21.58 ? 391 GLY A O 1 ATOM 2718 N N . ALA A 1 399 ? 16.396 39.020 54.711 1.00 20.20 ? 392 ALA A N 1 ATOM 2719 C CA . ALA A 1 399 ? 15.153 38.505 55.365 1.00 21.44 ? 392 ALA A CA 1 ATOM 2720 C C . ALA A 1 399 ? 15.410 37.743 56.660 1.00 21.61 ? 392 ALA A C 1 ATOM 2721 O O . ALA A 1 399 ? 14.630 37.856 57.605 1.00 20.96 ? 392 ALA A O 1 ATOM 2722 C CB . ALA A 1 399 ? 14.367 37.613 54.394 1.00 20.79 ? 392 ALA A CB 1 ATOM 2723 N N . ALA A 1 400 ? 16.516 36.987 56.704 1.00 21.64 ? 393 ALA A N 1 ATOM 2724 C CA . ALA A 1 400 ? 16.954 36.246 57.892 1.00 22.97 ? 393 ALA A CA 1 ATOM 2725 C C . ALA A 1 400 ? 17.298 37.204 59.033 1.00 23.65 ? 393 ALA A C 1 ATOM 2726 O O . ALA A 1 400 ? 17.025 36.931 60.202 1.00 23.02 ? 393 ALA A O 1 ATOM 2727 C CB . ALA A 1 400 ? 18.237 35.386 57.538 1.00 22.37 ? 393 ALA A CB 1 ATOM 2728 N N . VAL A 1 401 ? 17.915 38.328 58.672 1.00 23.65 ? 394 VAL A N 1 ATOM 2729 C CA . VAL A 1 401 ? 18.198 39.394 59.651 1.00 23.56 ? 394 VAL A CA 1 ATOM 2730 C C . VAL A 1 401 ? 16.883 40.027 60.163 1.00 23.76 ? 394 VAL A C 1 ATOM 2731 O O . VAL A 1 401 ? 16.715 40.250 61.374 1.00 21.81 ? 394 VAL A O 1 ATOM 2732 C CB . VAL A 1 401 ? 19.197 40.425 59.034 1.00 24.17 ? 394 VAL A CB 1 ATOM 2733 C CG1 . VAL A 1 401 ? 19.111 41.790 59.745 1.00 23.61 ? 394 VAL A CG1 1 ATOM 2734 C CG2 . VAL A 1 401 ? 20.624 39.867 59.138 1.00 21.99 ? 394 VAL A CG2 1 ATOM 2735 N N . VAL A 1 402 ? 15.957 40.326 59.251 1.00 22.84 ? 395 VAL A N 1 ATOM 2736 C CA . VAL A 1 402 ? 14.662 40.862 59.682 1.00 22.73 ? 395 VAL A CA 1 ATOM 2737 C C . VAL A 1 402 ? 13.988 39.869 60.680 1.00 22.67 ? 395 VAL A C 1 ATOM 2738 O O . VAL A 1 402 ? 13.475 40.272 61.738 1.00 22.54 ? 395 VAL A O 1 ATOM 2739 C CB . VAL A 1 402 ? 13.712 41.152 58.502 1.00 21.75 ? 395 VAL A CB 1 ATOM 2740 C CG1 . VAL A 1 402 ? 12.327 41.611 59.034 1.00 22.47 ? 395 VAL A CG1 1 ATOM 2741 C CG2 . VAL A 1 402 ? 14.327 42.239 57.569 1.00 24.09 ? 395 VAL A CG2 1 ATOM 2742 N N . HIS A 1 403 ? 14.007 38.589 60.321 1.00 22.77 ? 396 HIS A N 1 ATOM 2743 C CA . HIS A 1 403 ? 13.367 37.527 61.096 1.00 23.05 ? 396 HIS A CA 1 ATOM 2744 C C . HIS A 1 403 ? 13.937 37.539 62.512 1.00 24.78 ? 396 HIS A C 1 ATOM 2745 O O . HIS A 1 403 ? 13.170 37.505 63.479 1.00 26.10 ? 396 HIS A O 1 ATOM 2746 C CB . HIS A 1 403 ? 13.617 36.185 60.424 1.00 22.76 ? 396 HIS A CB 1 ATOM 2747 C CG . HIS A 1 403 ? 12.491 35.209 60.546 1.00 24.63 ? 396 HIS A CG 1 ATOM 2748 N ND1 . HIS A 1 403 ? 11.191 35.527 60.217 1.00 23.06 ? 396 HIS A ND1 1 ATOM 2749 C CD2 . HIS A 1 403 ? 12.485 33.901 60.898 1.00 25.68 ? 396 HIS A CD2 1 ATOM 2750 C CE1 . HIS A 1 403 ? 10.429 34.460 60.377 1.00 24.93 ? 396 HIS A CE1 1 ATOM 2751 N NE2 . HIS A 1 403 ? 11.196 33.457 60.769 1.00 28.44 ? 396 HIS A NE2 1 ATOM 2752 N N . GLU A 1 404 ? 15.262 37.618 62.653 1.00 24.62 ? 397 GLU A N 1 ATOM 2753 C CA . GLU A 1 404 ? 15.901 37.686 63.997 1.00 26.08 ? 397 GLU A CA 1 ATOM 2754 C C . GLU A 1 404 ? 15.574 38.981 64.744 1.00 26.12 ? 397 GLU A C 1 ATOM 2755 O O . GLU A 1 404 ? 15.398 38.982 65.977 1.00 26.98 ? 397 GLU A O 1 ATOM 2756 C CB . GLU A 1 404 ? 17.420 37.515 63.860 1.00 26.87 ? 397 GLU A CB 1 ATOM 2757 C CG . GLU A 1 404 ? 18.281 37.485 65.185 1.00 26.96 ? 397 GLU A CG 1 ATOM 2758 C CD . GLU A 1 404 ? 17.881 36.386 66.168 1.00 30.70 ? 397 GLU A CD 1 ATOM 2759 O OE1 . GLU A 1 404 ? 16.871 35.680 65.917 1.00 29.31 ? 397 GLU A OE1 1 ATOM 2760 O OE2 . GLU A 1 404 ? 18.576 36.233 67.213 1.00 31.00 ? 397 GLU A OE2 1 ATOM 2761 N N . ILE A 1 405 ? 15.518 40.092 64.009 1.00 25.17 ? 398 ILE A N 1 ATOM 2762 C CA . ILE A 1 405 ? 15.102 41.366 64.607 1.00 25.41 ? 398 ILE A CA 1 ATOM 2763 C C . ILE A 1 405 ? 13.684 41.282 65.171 1.00 24.94 ? 398 ILE A C 1 ATOM 2764 O O . ILE A 1 405 ? 13.470 41.693 66.296 1.00 25.32 ? 398 ILE A O 1 ATOM 2765 C CB . ILE A 1 405 ? 15.249 42.539 63.575 1.00 24.11 ? 398 ILE A CB 1 ATOM 2766 C CG1 . ILE A 1 405 ? 16.764 42.851 63.351 1.00 23.45 ? 398 ILE A CG1 1 ATOM 2767 C CG2 . ILE A 1 405 ? 14.439 43.803 64.030 1.00 22.39 ? 398 ILE A CG2 1 ATOM 2768 C CD1 . ILE A 1 405 ? 16.995 43.685 62.093 1.00 20.07 ? 398 ILE A CD1 1 ATOM 2769 N N . VAL A 1 406 ? 12.734 40.746 64.395 1.00 24.07 ? 399 VAL A N 1 ATOM 2770 C CA . VAL A 1 406 ? 11.372 40.478 64.899 1.00 24.32 ? 399 VAL A CA 1 ATOM 2771 C C . VAL A 1 406 ? 11.430 39.603 66.147 1.00 25.31 ? 399 VAL A C 1 ATOM 2772 O O . VAL A 1 406 ? 10.813 39.943 67.185 1.00 26.64 ? 399 VAL A O 1 ATOM 2773 C CB . VAL A 1 406 ? 10.435 39.825 63.834 1.00 23.44 ? 399 VAL A CB 1 ATOM 2774 C CG1 . VAL A 1 406 ? 9.061 39.489 64.434 1.00 24.68 ? 399 VAL A CG1 1 ATOM 2775 C CG2 . VAL A 1 406 ? 10.233 40.816 62.663 1.00 22.24 ? 399 VAL A CG2 1 ATOM 2776 N N . ARG A 1 407 ? 12.178 38.501 66.064 1.00 26.12 ? 400 ARG A N 1 ATOM 2777 C CA . ARG A 1 407 ? 12.296 37.615 67.227 1.00 26.75 ? 400 ARG A CA 1 ATOM 2778 C C . ARG A 1 407 ? 12.763 38.365 68.483 1.00 29.22 ? 400 ARG A C 1 ATOM 2779 O O . ARG A 1 407 ? 12.208 38.145 69.585 1.00 29.71 ? 400 ARG A O 1 ATOM 2780 C CB . ARG A 1 407 ? 13.213 36.408 66.953 1.00 27.61 ? 400 ARG A CB 1 ATOM 2781 C CG . ARG A 1 407 ? 13.032 35.250 67.983 1.00 26.58 ? 400 ARG A CG 1 ATOM 2782 C CD . ARG A 1 407 ? 14.195 34.204 67.886 1.00 28.55 ? 400 ARG A CD 1 ATOM 2783 N NE . ARG A 1 407 ? 15.474 34.873 68.166 1.00 31.16 ? 400 ARG A NE 1 ATOM 2784 C CZ . ARG A 1 407 ? 15.883 35.250 69.381 1.00 32.78 ? 400 ARG A CZ 1 ATOM 2785 N NH1 . ARG A 1 407 ? 17.044 35.872 69.533 1.00 30.18 ? 400 ARG A NH1 1 ATOM 2786 N NH2 . ARG A 1 407 ? 15.154 34.968 70.465 1.00 35.81 ? 400 ARG A NH2 1 ATOM 2787 N N . SER A 1 408 ? 13.785 39.209 68.349 1.00 28.89 ? 401 SER A N 1 ATOM 2788 C CA . SER A 1 408 ? 14.293 39.941 69.520 1.00 30.25 ? 401 SER A CA 1 ATOM 2789 C C . SER A 1 408 ? 13.279 40.953 70.060 1.00 30.72 ? 401 SER A C 1 ATOM 2790 O O . SER A 1 408 ? 13.039 40.979 71.267 1.00 31.45 ? 401 SER A O 1 ATOM 2791 C CB . SER A 1 408 ? 15.595 40.673 69.203 1.00 30.68 ? 401 SER A CB 1 ATOM 2792 O OG A SER A 1 408 ? 16.079 41.359 70.364 0.50 26.86 ? 401 SER A OG 1 ATOM 2793 O OG B SER A 1 408 ? 16.548 39.752 68.701 0.50 33.98 ? 401 SER A OG 1 ATOM 2794 N N . PHE A 1 409 ? 12.698 41.776 69.183 1.00 29.51 ? 402 PHE A N 1 ATOM 2795 C CA . PHE A 1 409 ? 11.638 42.696 69.619 1.00 28.94 ? 402 PHE A CA 1 ATOM 2796 C C . PHE A 1 409 ? 10.518 41.928 70.295 1.00 30.26 ? 402 PHE A C 1 ATOM 2797 O O . PHE A 1 409 ? 10.023 42.372 71.318 1.00 30.96 ? 402 PHE A O 1 ATOM 2798 C CB . PHE A 1 409 ? 11.047 43.539 68.478 1.00 28.09 ? 402 PHE A CB 1 ATOM 2799 C CG . PHE A 1 409 ? 11.843 44.761 68.127 1.00 27.34 ? 402 PHE A CG 1 ATOM 2800 C CD1 . PHE A 1 409 ? 12.010 45.783 69.056 1.00 28.38 ? 402 PHE A CD1 1 ATOM 2801 C CD2 . PHE A 1 409 ? 12.401 44.904 66.851 1.00 25.18 ? 402 PHE A CD2 1 ATOM 2802 C CE1 . PHE A 1 409 ? 12.711 46.940 68.724 1.00 27.74 ? 402 PHE A CE1 1 ATOM 2803 C CE2 . PHE A 1 409 ? 13.101 46.076 66.497 1.00 25.43 ? 402 PHE A CE2 1 ATOM 2804 C CZ . PHE A 1 409 ? 13.271 47.086 67.470 1.00 27.69 ? 402 PHE A CZ 1 ATOM 2805 N N . GLY A 1 410 ? 10.132 40.772 69.751 1.00 30.08 ? 403 GLY A N 1 ATOM 2806 C CA . GLY A 1 410 ? 9.081 39.955 70.344 1.00 31.40 ? 403 GLY A CA 1 ATOM 2807 C C . GLY A 1 410 ? 9.461 39.414 71.730 1.00 34.03 ? 403 GLY A C 1 ATOM 2808 O O . GLY A 1 410 ? 8.621 39.314 72.627 1.00 34.76 ? 403 GLY A O 1 ATOM 2809 N N . THR A 1 411 ? 10.733 39.100 71.924 1.00 34.61 ? 404 THR A N 1 ATOM 2810 C CA . THR A 1 411 ? 11.168 38.604 73.226 1.00 36.49 ? 404 THR A CA 1 ATOM 2811 C C . THR A 1 411 ? 10.943 39.691 74.288 1.00 37.99 ? 404 THR A C 1 ATOM 2812 O O . THR A 1 411 ? 10.433 39.411 75.375 1.00 39.81 ? 404 THR A O 1 ATOM 2813 C CB . THR A 1 411 ? 12.644 38.098 73.232 1.00 37.28 ? 404 THR A CB 1 ATOM 2814 O OG1 A THR A 1 411 ? 12.799 37.069 72.241 0.50 34.78 ? 404 THR A OG1 1 ATOM 2815 O OG1 B THR A 1 411 ? 13.573 39.196 73.320 0.50 38.12 ? 404 THR A OG1 1 ATOM 2816 C CG2 A THR A 1 411 ? 13.069 37.593 74.590 0.50 36.47 ? 404 THR A CG2 1 ATOM 2817 C CG2 B THR A 1 411 ? 12.950 37.195 72.043 0.50 35.45 ? 404 THR A CG2 1 ATOM 2818 N N . LEU A 1 412 ? 11.314 40.924 73.960 1.00 37.18 ? 405 LEU A N 1 ATOM 2819 C CA . LEU A 1 412 ? 11.134 42.044 74.867 1.00 38.29 ? 405 LEU A CA 1 ATOM 2820 C C . LEU A 1 412 ? 9.641 42.262 75.118 1.00 38.40 ? 405 LEU A C 1 ATOM 2821 O O . LEU A 1 412 ? 9.228 42.505 76.264 1.00 37.47 ? 405 LEU A O 1 ATOM 2822 C CB . LEU A 1 412 ? 11.771 43.325 74.290 1.00 38.61 ? 405 LEU A CB 1 ATOM 2823 C CG . LEU A 1 412 ? 13.233 43.688 74.605 1.00 40.64 ? 405 LEU A CG 1 ATOM 2824 C CD1 . LEU A 1 412 ? 14.195 42.553 74.303 1.00 43.79 ? 405 LEU A CD1 1 ATOM 2825 C CD2 . LEU A 1 412 ? 13.639 44.924 73.811 1.00 40.46 ? 405 LEU A CD2 1 ATOM 2826 N N . LYS A 1 413 ? 8.837 42.171 74.049 1.00 37.25 ? 406 LYS A N 1 ATOM 2827 C CA . LYS A 1 413 ? 7.393 42.319 74.195 1.00 37.85 ? 406 LYS A CA 1 ATOM 2828 C C . LYS A 1 413 ? 6.793 41.303 75.174 1.00 38.69 ? 406 LYS A C 1 ATOM 2829 O O . LYS A 1 413 ? 5.964 41.678 76.017 1.00 38.53 ? 406 LYS A O 1 ATOM 2830 C CB . LYS A 1 413 ? 6.663 42.235 72.851 1.00 37.54 ? 406 LYS A CB 1 ATOM 2831 C CG . LYS A 1 413 ? 5.225 42.659 73.005 1.00 41.73 ? 406 LYS A CG 1 ATOM 2832 C CD . LYS A 1 413 ? 4.335 41.961 72.045 1.00 47.12 ? 406 LYS A CD 1 ATOM 2833 C CE . LYS A 1 413 ? 3.024 41.612 72.708 1.00 50.83 ? 406 LYS A CE 1 ATOM 2834 N NZ . LYS A 1 413 ? 2.288 40.656 71.860 1.00 52.75 ? 406 LYS A NZ 1 ATOM 2835 N N . LYS A 1 414 ? 7.214 40.036 75.061 1.00 38.46 ? 407 LYS A N 1 ATOM 2836 C CA . LYS A 1 414 ? 6.747 38.986 75.981 1.00 40.68 ? 407 LYS A CA 1 ATOM 2837 C C . LYS A 1 414 ? 7.048 39.265 77.446 1.00 42.10 ? 407 LYS A C 1 ATOM 2838 O O . LYS A 1 414 ? 6.301 38.824 78.322 1.00 43.91 ? 407 LYS A O 1 ATOM 2839 C CB . LYS A 1 414 ? 7.232 37.595 75.564 1.00 40.57 ? 407 LYS A CB 1 ATOM 2840 C CG . LYS A 1 414 ? 6.528 37.105 74.303 1.00 42.72 ? 407 LYS A CG 1 ATOM 2841 C CD . LYS A 1 414 ? 7.132 35.829 73.750 1.00 45.08 ? 407 LYS A CD 1 ATOM 2842 C CE . LYS A 1 414 ? 6.360 35.370 72.528 1.00 46.49 ? 407 LYS A CE 1 ATOM 2843 N NZ . LYS A 1 414 ? 6.955 34.106 72.025 1.00 49.10 ? 407 LYS A NZ 1 ATOM 2844 N N . GLU A 1 415 ? 8.119 40.008 77.712 1.00 42.48 ? 408 GLU A N 1 ATOM 2845 C CA . GLU A 1 415 ? 8.472 40.431 79.092 1.00 44.76 ? 408 GLU A CA 1 ATOM 2846 C C . GLU A 1 415 ? 7.755 41.706 79.567 1.00 44.11 ? 408 GLU A C 1 ATOM 2847 O O . GLU A 1 415 ? 8.021 42.208 80.680 1.00 44.46 ? 408 GLU A O 1 ATOM 2848 C CB . GLU A 1 415 ? 9.976 40.645 79.209 1.00 45.77 ? 408 GLU A CB 1 ATOM 2849 C CG . GLU A 1 415 ? 10.813 39.444 78.793 1.00 50.82 ? 408 GLU A CG 1 ATOM 2850 C CD . GLU A 1 415 ? 12.297 39.661 79.040 1.00 58.92 ? 408 GLU A CD 1 ATOM 2851 O OE1 . GLU A 1 415 ? 12.853 40.700 78.588 1.00 61.54 ? 408 GLU A OE1 1 ATOM 2852 O OE2 . GLU A 1 415 ? 12.909 38.781 79.687 1.00 63.27 ? 408 GLU A OE2 1 ATOM 2853 N N . GLY A 1 416 ? 6.875 42.239 78.723 1.00 41.35 ? 409 GLY A N 1 ATOM 2854 C CA . GLY A 1 416 ? 6.034 43.377 79.079 1.00 41.34 ? 409 GLY A CA 1 ATOM 2855 C C . GLY A 1 416 ? 6.432 44.694 78.445 1.00 40.57 ? 409 GLY A C 1 ATOM 2856 O O . GLY A 1 416 ? 5.775 45.715 78.672 1.00 40.53 ? 409 GLY A O 1 ATOM 2857 N N . TRP A 1 417 ? 7.492 44.692 77.631 1.00 38.57 ? 410 TRP A N 1 ATOM 2858 C CA . TRP A 1 417 ? 7.941 45.942 77.016 1.00 37.38 ? 410 TRP A CA 1 ATOM 2859 C C . TRP A 1 417 ? 7.142 46.198 75.739 1.00 35.55 ? 410 TRP A C 1 ATOM 2860 O O . TRP A 1 417 ? 6.702 45.256 75.078 1.00 36.47 ? 410 TRP A O 1 ATOM 2861 C CB . TRP A 1 417 ? 9.437 45.868 76.705 1.00 38.38 ? 410 TRP A CB 1 ATOM 2862 C CG . TRP A 1 417 ? 10.051 46.998 75.863 1.00 37.64 ? 410 TRP A CG 1 ATOM 2863 C CD1 . TRP A 1 417 ? 10.609 48.163 76.324 1.00 39.20 ? 410 TRP A CD1 1 ATOM 2864 C CD2 . TRP A 1 417 ? 10.172 47.036 74.430 1.00 37.85 ? 410 TRP A CD2 1 ATOM 2865 N NE1 . TRP A 1 417 ? 11.080 48.910 75.273 1.00 36.58 ? 410 TRP A NE1 1 ATOM 2866 C CE2 . TRP A 1 417 ? 10.820 48.253 74.097 1.00 36.84 ? 410 TRP A CE2 1 ATOM 2867 C CE3 . TRP A 1 417 ? 9.791 46.167 73.401 1.00 36.87 ? 410 TRP A CE3 1 ATOM 2868 C CZ2 . TRP A 1 417 ? 11.130 48.603 72.771 1.00 34.05 ? 410 TRP A CZ2 1 ATOM 2869 C CZ3 . TRP A 1 417 ? 10.089 46.510 72.087 1.00 33.08 ? 410 TRP A CZ3 1 ATOM 2870 C CH2 . TRP A 1 417 ? 10.742 47.738 71.784 1.00 32.90 ? 410 TRP A CH2 1 ATOM 2871 N N . ARG A 1 418 ? 6.930 47.461 75.416 1.00 33.22 ? 411 ARG A N 1 ATOM 2872 C CA . ARG A 1 418 ? 6.524 47.852 74.042 1.00 31.90 ? 411 ARG A CA 1 ATOM 2873 C C . ARG A 1 418 ? 7.330 49.067 73.630 1.00 30.26 ? 411 ARG A C 1 ATOM 2874 O O . ARG A 1 418 ? 7.686 49.881 74.478 1.00 30.61 ? 411 ARG A O 1 ATOM 2875 C CB . ARG A 1 418 ? 5.063 48.301 73.966 1.00 32.20 ? 411 ARG A CB 1 ATOM 2876 C CG . ARG A 1 418 ? 4.029 47.243 74.238 1.00 34.95 ? 411 ARG A CG 1 ATOM 2877 C CD . ARG A 1 418 ? 2.600 47.743 73.934 1.00 33.16 ? 411 ARG A CD 1 ATOM 2878 N NE . ARG A 1 418 ? 1.755 46.560 73.897 1.00 34.03 ? 411 ARG A NE 1 ATOM 2879 C CZ . ARG A 1 418 ? 1.538 45.826 72.801 1.00 35.13 ? 411 ARG A CZ 1 ATOM 2880 N NH1 . ARG A 1 418 ? 2.026 46.212 71.613 1.00 29.54 ? 411 ARG A NH1 1 ATOM 2881 N NH2 . ARG A 1 418 ? 0.801 44.727 72.891 1.00 34.08 ? 411 ARG A NH2 1 ATOM 2882 N N . PRO A 1 419 ? 7.565 49.230 72.310 1.00 27.72 ? 412 PRO A N 1 ATOM 2883 C CA . PRO A 1 419 ? 8.179 50.460 71.867 1.00 26.45 ? 412 PRO A CA 1 ATOM 2884 C C . PRO A 1 419 ? 7.220 51.642 72.055 1.00 26.02 ? 412 PRO A C 1 ATOM 2885 O O . PRO A 1 419 ? 6.005 51.478 72.179 1.00 25.93 ? 412 PRO A O 1 ATOM 2886 C CB . PRO A 1 419 ? 8.411 50.234 70.342 1.00 24.19 ? 412 PRO A CB 1 ATOM 2887 C CG . PRO A 1 419 ? 7.376 49.203 69.949 1.00 25.23 ? 412 PRO A CG 1 ATOM 2888 C CD . PRO A 1 419 ? 7.193 48.325 71.200 1.00 25.91 ? 412 PRO A CD 1 ATOM 2889 N N . ARG A 1 420 ? 7.778 52.833 72.121 1.00 26.73 ? 413 ARG A N 1 ATOM 2890 C CA . ARG A 1 420 ? 6.951 54.031 72.253 1.00 26.01 ? 413 ARG A CA 1 ATOM 2891 C C . ARG A 1 420 ? 6.032 54.203 71.024 1.00 25.70 ? 413 ARG A C 1 ATOM 2892 O O . ARG A 1 420 ? 4.830 54.476 71.166 1.00 24.63 ? 413 ARG A O 1 ATOM 2893 C CB . ARG A 1 420 ? 7.838 55.240 72.373 1.00 26.19 ? 413 ARG A CB 1 ATOM 2894 C CG . ARG A 1 420 ? 7.064 56.576 72.395 1.00 28.13 ? 413 ARG A CG 1 ATOM 2895 C CD . ARG A 1 420 ? 8.031 57.753 72.297 1.00 28.36 ? 413 ARG A CD 1 ATOM 2896 N NE . ARG A 1 420 ? 7.270 59.003 72.224 1.00 30.73 ? 413 ARG A NE 1 ATOM 2897 C CZ . ARG A 1 420 ? 6.844 59.676 73.303 1.00 32.70 ? 413 ARG A CZ 1 ATOM 2898 N NH1 . ARG A 1 420 ? 7.134 59.222 74.525 1.00 27.19 ? 413 ARG A NH1 1 ATOM 2899 N NH2 . ARG A 1 420 ? 6.136 60.794 73.148 1.00 32.20 ? 413 ARG A NH2 1 ATOM 2900 N N . ARG A 1 421 ? 6.614 54.053 69.840 1.00 23.18 ? 414 ARG A N 1 ATOM 2901 C CA . ARG A 1 421 ? 5.871 54.173 68.537 1.00 22.56 ? 414 ARG A CA 1 ATOM 2902 C C . ARG A 1 421 ? 5.608 52.792 67.955 1.00 23.43 ? 414 ARG A C 1 ATOM 2903 O O . ARG A 1 421 ? 6.292 51.823 68.316 1.00 23.02 ? 414 ARG A O 1 ATOM 2904 C CB . ARG A 1 421 ? 6.684 54.988 67.543 1.00 21.69 ? 414 ARG A CB 1 ATOM 2905 C CG . ARG A 1 421 ? 7.198 56.358 68.098 1.00 21.85 ? 414 ARG A CG 1 ATOM 2906 C CD . ARG A 1 421 ? 7.818 57.296 67.010 1.00 22.95 ? 414 ARG A CD 1 ATOM 2907 N NE . ARG A 1 421 ? 8.036 58.557 67.700 1.00 23.80 ? 414 ARG A NE 1 ATOM 2908 C CZ . ARG A 1 421 ? 9.024 58.786 68.575 1.00 24.33 ? 414 ARG A CZ 1 ATOM 2909 N NH1 . ARG A 1 421 ? 10.008 57.898 68.723 1.00 23.80 ? 414 ARG A NH1 1 ATOM 2910 N NH2 . ARG A 1 421 ? 9.071 59.942 69.260 1.00 23.21 ? 414 ARG A NH2 1 ATOM 2911 N N . THR A 1 422 ? 4.623 52.684 67.057 1.00 22.09 ? 415 THR A N 1 ATOM 2912 C CA . THR A 1 422 ? 4.332 51.414 66.412 1.00 22.12 ? 415 THR A CA 1 ATOM 2913 C C . THR A 1 422 ? 5.463 51.047 65.446 1.00 21.92 ? 415 THR A C 1 ATOM 2914 O O . THR A 1 422 ? 5.955 51.919 64.694 1.00 20.61 ? 415 THR A O 1 ATOM 2915 C CB . THR A 1 422 ? 3.022 51.525 65.636 1.00 21.68 ? 415 THR A CB 1 ATOM 2916 O OG1 . THR A 1 422 ? 1.962 51.543 66.583 1.00 21.80 ? 415 THR A OG1 1 ATOM 2917 C CG2 . THR A 1 422 ? 2.822 50.336 64.691 1.00 20.02 ? 415 THR A CG2 1 ATOM 2918 N N . ILE A 1 423 ? 5.861 49.771 65.472 1.00 21.19 ? 416 ILE A N 1 ATOM 2919 C CA . ILE A 1 423 ? 6.766 49.260 64.465 1.00 21.31 ? 416 ILE A CA 1 ATOM 2920 C C . ILE A 1 423 ? 6.005 48.326 63.544 1.00 21.71 ? 416 ILE A C 1 ATOM 2921 O O . ILE A 1 423 ? 5.235 47.458 64.004 1.00 22.23 ? 416 ILE A O 1 ATOM 2922 C CB . ILE A 1 423 ? 8.017 48.536 65.081 1.00 21.24 ? 416 ILE A CB 1 ATOM 2923 C CG1 . ILE A 1 423 ? 8.740 49.427 66.091 1.00 20.78 ? 416 ILE A CG1 1 ATOM 2924 C CG2 . ILE A 1 423 ? 8.997 48.080 63.977 1.00 21.79 ? 416 ILE A CG2 1 ATOM 2925 C CD1 . ILE A 1 423 ? 9.841 48.657 66.906 1.00 19.43 ? 416 ILE A CD1 1 ATOM 2926 N N . LEU A 1 424 ? 6.160 48.577 62.239 1.00 20.75 ? 417 LEU A N 1 ATOM 2927 C CA . LEU A 1 424 ? 5.625 47.693 61.197 1.00 20.10 ? 417 LEU A CA 1 ATOM 2928 C C . LEU A 1 424 ? 6.782 46.946 60.567 1.00 20.10 ? 417 LEU A C 1 ATOM 2929 O O . LEU A 1 424 ? 7.840 47.542 60.240 1.00 21.27 ? 417 LEU A O 1 ATOM 2930 C CB . LEU A 1 424 ? 4.881 48.469 60.105 1.00 19.31 ? 417 LEU A CB 1 ATOM 2931 C CG . LEU A 1 424 ? 3.684 49.337 60.620 1.00 19.72 ? 417 LEU A CG 1 ATOM 2932 C CD1 . LEU A 1 424 ? 2.963 49.995 59.409 1.00 19.67 ? 417 LEU A CD1 1 ATOM 2933 C CD2 . LEU A 1 424 ? 2.649 48.546 61.513 1.00 21.28 ? 417 LEU A CD2 1 ATOM 2934 N N . PHE A 1 425 ? 6.574 45.650 60.391 1.00 19.27 ? 418 PHE A N 1 ATOM 2935 C CA . PHE A 1 425 ? 7.580 44.791 59.775 1.00 18.06 ? 418 PHE A CA 1 ATOM 2936 C C . PHE A 1 425 ? 6.966 44.241 58.506 1.00 18.43 ? 418 PHE A C 1 ATOM 2937 O O . PHE A 1 425 ? 5.768 43.815 58.490 1.00 19.77 ? 418 PHE A O 1 ATOM 2938 C CB . PHE A 1 425 ? 7.951 43.606 60.681 1.00 18.47 ? 418 PHE A CB 1 ATOM 2939 C CG . PHE A 1 425 ? 8.513 44.013 62.005 1.00 19.74 ? 418 PHE A CG 1 ATOM 2940 C CD1 . PHE A 1 425 ? 9.889 44.270 62.154 1.00 22.97 ? 418 PHE A CD1 1 ATOM 2941 C CD2 . PHE A 1 425 ? 7.664 44.161 63.104 1.00 23.41 ? 418 PHE A CD2 1 ATOM 2942 C CE1 . PHE A 1 425 ? 10.409 44.645 63.423 1.00 21.36 ? 418 PHE A CE1 1 ATOM 2943 C CE2 . PHE A 1 425 ? 8.167 44.547 64.339 1.00 23.34 ? 418 PHE A CE2 1 ATOM 2944 C CZ . PHE A 1 425 ? 9.553 44.735 64.519 1.00 23.08 ? 418 PHE A CZ 1 ATOM 2945 N N . ALA A 1 426 ? 7.747 44.287 57.438 1.00 18.71 ? 419 ALA A N 1 ATOM 2946 C CA . ALA A 1 426 ? 7.248 43.830 56.125 1.00 18.19 ? 419 ALA A CA 1 ATOM 2947 C C . ALA A 1 426 ? 8.196 42.841 55.439 1.00 18.94 ? 419 ALA A C 1 ATOM 2948 O O . ALA A 1 426 ? 9.399 43.073 55.341 1.00 19.76 ? 419 ALA A O 1 ATOM 2949 C CB . ALA A 1 426 ? 7.015 45.011 55.195 1.00 17.00 ? 419 ALA A CB 1 ATOM 2950 N N . SER A 1 427 ? 7.588 41.785 54.907 1.00 19.38 ? 420 SER A N 1 ATOM 2951 C CA . SER A 1 427 ? 8.180 40.847 54.000 1.00 19.00 ? 420 SER A CA 1 ATOM 2952 C C . SER A 1 427 ? 7.526 41.090 52.614 1.00 19.32 ? 420 SER A C 1 ATOM 2953 O O . SER A 1 427 ? 6.401 40.615 52.366 1.00 19.26 ? 420 SER A O 1 ATOM 2954 C CB . SER A 1 427 ? 7.840 39.422 54.481 1.00 19.71 ? 420 SER A CB 1 ATOM 2955 O OG . SER A 1 427 ? 8.327 38.416 53.567 1.00 19.10 ? 420 SER A OG 1 ATOM 2956 N N . TRP A 1 428 ? 8.201 41.854 51.733 1.00 18.86 ? 421 TRP A N 1 ATOM 2957 C CA . TRP A 1 428 ? 7.603 42.296 50.471 1.00 17.40 ? 421 TRP A CA 1 ATOM 2958 C C . TRP A 1 428 ? 7.706 41.183 49.423 1.00 19.45 ? 421 TRP A C 1 ATOM 2959 O O . TRP A 1 428 ? 8.704 40.417 49.397 1.00 17.56 ? 421 TRP A O 1 ATOM 2960 C CB . TRP A 1 428 ? 8.351 43.523 49.899 1.00 16.99 ? 421 TRP A CB 1 ATOM 2961 C CG . TRP A 1 428 ? 8.375 44.734 50.800 1.00 17.82 ? 421 TRP A CG 1 ATOM 2962 C CD1 . TRP A 1 428 ? 9.480 45.431 51.169 1.00 15.46 ? 421 TRP A CD1 1 ATOM 2963 C CD2 . TRP A 1 428 ? 7.229 45.443 51.384 1.00 15.77 ? 421 TRP A CD2 1 ATOM 2964 N NE1 . TRP A 1 428 ? 9.123 46.507 51.977 1.00 16.72 ? 421 TRP A NE1 1 ATOM 2965 C CE2 . TRP A 1 428 ? 7.752 46.541 52.106 1.00 15.29 ? 421 TRP A CE2 1 ATOM 2966 C CE3 . TRP A 1 428 ? 5.824 45.269 51.340 1.00 19.17 ? 421 TRP A CE3 1 ATOM 2967 C CZ2 . TRP A 1 428 ? 6.930 47.456 52.807 1.00 14.86 ? 421 TRP A CZ2 1 ATOM 2968 C CZ3 . TRP A 1 428 ? 4.993 46.161 52.072 1.00 18.30 ? 421 TRP A CZ3 1 ATOM 2969 C CH2 . TRP A 1 428 ? 5.559 47.243 52.806 1.00 17.09 ? 421 TRP A CH2 1 ATOM 2970 N N . ASP A 1 429 ? 6.684 41.114 48.558 1.00 18.71 ? 422 ASP A N 1 ATOM 2971 C CA . ASP A 1 429 ? 6.738 40.165 47.443 1.00 19.08 ? 422 ASP A CA 1 ATOM 2972 C C . ASP A 1 429 ? 7.056 40.958 46.166 1.00 18.58 ? 422 ASP A C 1 ATOM 2973 O O . ASP A 1 429 ? 6.870 42.197 46.121 1.00 19.59 ? 422 ASP A O 1 ATOM 2974 C CB . ASP A 1 429 ? 5.374 39.468 47.297 1.00 20.00 ? 422 ASP A CB 1 ATOM 2975 C CG . ASP A 1 429 ? 5.469 38.114 46.561 1.00 19.14 ? 422 ASP A CG 1 ATOM 2976 O OD1 . ASP A 1 429 ? 6.532 37.792 45.943 1.00 22.47 ? 422 ASP A OD1 1 ATOM 2977 O OD2 . ASP A 1 429 ? 4.473 37.350 46.630 1.00 20.01 ? 422 ASP A OD2 1 ATOM 2978 N N . ALA A 1 430 ? 7.481 40.219 45.129 1.00 18.39 ? 423 ALA A N 1 ATOM 2979 C CA . ALA A 1 430 ? 7.730 40.737 43.780 1.00 18.80 ? 423 ALA A CA 1 ATOM 2980 C C . ALA A 1 430 ? 8.677 41.945 43.692 1.00 16.96 ? 423 ALA A C 1 ATOM 2981 O O . ALA A 1 430 ? 8.560 42.758 42.793 1.00 18.54 ? 423 ALA A O 1 ATOM 2982 C CB . ALA A 1 430 ? 6.390 41.044 43.026 1.00 17.42 ? 423 ALA A CB 1 ATOM 2983 N N . GLU A 1 431 ? 9.595 42.077 44.622 1.00 19.19 ? 424 GLU A N 1 ATOM 2984 C CA . GLU A 1 431 ? 10.562 43.147 44.462 1.00 17.61 ? 424 GLU A CA 1 ATOM 2985 C C . GLU A 1 431 ? 11.320 42.933 43.163 1.00 18.39 ? 424 GLU A C 1 ATOM 2986 O O . GLU A 1 431 ? 11.626 43.923 42.417 1.00 19.68 ? 424 GLU A O 1 ATOM 2987 C CB . GLU A 1 431 ? 11.464 43.200 45.675 1.00 18.50 ? 424 GLU A CB 1 ATOM 2988 C CG . GLU A 1 431 ? 12.458 44.370 45.676 1.00 16.30 ? 424 GLU A CG 1 ATOM 2989 C CD . GLU A 1 431 ? 13.781 44.177 44.910 1.00 17.91 ? 424 GLU A CD 1 ATOM 2990 O OE1 . GLU A 1 431 ? 14.127 43.042 44.440 1.00 19.95 ? 424 GLU A OE1 1 ATOM 2991 O OE2 . GLU A 1 431 ? 14.501 45.228 44.733 1.00 17.87 ? 424 GLU A OE2 1 ATOM 2992 N N . GLU A 1 432 ? 11.600 41.670 42.825 1.00 18.18 ? 425 GLU A N 1 ATOM 2993 C CA . GLU A 1 432 ? 12.456 41.422 41.649 1.00 18.88 ? 425 GLU A CA 1 ATOM 2994 C C . GLU A 1 432 ? 11.791 41.841 40.355 1.00 18.74 ? 425 GLU A C 1 ATOM 2995 O O . GLU A 1 432 ? 12.473 42.056 39.353 1.00 19.86 ? 425 GLU A O 1 ATOM 2996 C CB . GLU A 1 432 ? 12.949 39.970 41.573 1.00 19.02 ? 425 GLU A CB 1 ATOM 2997 C CG . GLU A 1 432 ? 13.835 39.544 42.769 1.00 18.60 ? 425 GLU A CG 1 ATOM 2998 C CD . GLU A 1 432 ? 15.216 40.231 42.832 1.00 18.81 ? 425 GLU A CD 1 ATOM 2999 O OE1 . GLU A 1 432 ? 15.502 41.156 42.038 1.00 20.06 ? 425 GLU A OE1 1 ATOM 3000 O OE2 . GLU A 1 432 ? 16.022 39.852 43.691 1.00 17.86 ? 425 GLU A OE2 1 ATOM 3001 N N . PHE A 1 433 ? 10.464 41.956 40.383 1.00 19.17 ? 426 PHE A N 1 ATOM 3002 C CA . PHE A 1 433 ? 9.723 42.330 39.184 1.00 18.94 ? 426 PHE A CA 1 ATOM 3003 C C . PHE A 1 433 ? 9.350 43.773 39.122 1.00 18.51 ? 426 PHE A C 1 ATOM 3004 O O . PHE A 1 433 ? 8.521 44.180 38.271 1.00 18.13 ? 426 PHE A O 1 ATOM 3005 C CB . PHE A 1 433 ? 8.473 41.462 39.072 1.00 19.74 ? 426 PHE A CB 1 ATOM 3006 C CG . PHE A 1 433 ? 8.783 40.026 38.754 1.00 19.62 ? 426 PHE A CG 1 ATOM 3007 C CD1 . PHE A 1 433 ? 8.615 39.544 37.459 1.00 18.68 ? 426 PHE A CD1 1 ATOM 3008 C CD2 . PHE A 1 433 ? 9.202 39.149 39.776 1.00 18.82 ? 426 PHE A CD2 1 ATOM 3009 C CE1 . PHE A 1 433 ? 8.877 38.164 37.117 1.00 19.00 ? 426 PHE A CE1 1 ATOM 3010 C CE2 . PHE A 1 433 ? 9.478 37.776 39.489 1.00 19.53 ? 426 PHE A CE2 1 ATOM 3011 C CZ . PHE A 1 433 ? 9.316 37.275 38.140 1.00 20.48 ? 426 PHE A CZ 1 ATOM 3012 N N . GLY A 1 434 ? 9.944 44.593 40.007 1.00 17.92 ? 427 GLY A N 1 ATOM 3013 C CA . GLY A 1 434 ? 9.727 46.045 39.853 1.00 17.80 ? 427 GLY A CA 1 ATOM 3014 C C . GLY A 1 434 ? 9.271 46.731 41.142 1.00 18.27 ? 427 GLY A C 1 ATOM 3015 O O . GLY A 1 434 ? 8.523 47.722 41.096 1.00 17.64 ? 427 GLY A O 1 ATOM 3016 N N . LEU A 1 435 ? 9.704 46.201 42.270 1.00 16.40 ? 428 LEU A N 1 ATOM 3017 C CA . LEU A 1 435 ? 9.306 46.790 43.589 1.00 16.13 ? 428 LEU A CA 1 ATOM 3018 C C . LEU A 1 435 ? 7.744 46.714 43.735 1.00 15.83 ? 428 LEU A C 1 ATOM 3019 O O . LEU A 1 435 ? 7.133 47.596 44.319 1.00 15.72 ? 428 LEU A O 1 ATOM 3020 C CB . LEU A 1 435 ? 9.798 48.252 43.700 1.00 16.13 ? 428 LEU A CB 1 ATOM 3021 C CG . LEU A 1 435 ? 11.190 48.567 43.107 1.00 16.39 ? 428 LEU A CG 1 ATOM 3022 C CD1 . LEU A 1 435 ? 11.568 50.063 43.190 1.00 16.05 ? 428 LEU A CD1 1 ATOM 3023 C CD2 . LEU A 1 435 ? 12.296 47.667 43.754 1.00 15.66 ? 428 LEU A CD2 1 ATOM 3024 N N . LEU A 1 436 ? 7.128 45.647 43.229 1.00 15.96 ? 429 LEU A N 1 ATOM 3025 C CA . LEU A 1 436 ? 5.688 45.694 43.061 1.00 16.98 ? 429 LEU A CA 1 ATOM 3026 C C . LEU A 1 436 ? 4.962 45.570 44.388 1.00 17.33 ? 429 LEU A C 1 ATOM 3027 O O . LEU A 1 436 ? 3.953 46.212 44.594 1.00 17.82 ? 429 LEU A O 1 ATOM 3028 C CB . LEU A 1 436 ? 5.188 44.605 42.104 1.00 17.58 ? 429 LEU A CB 1 ATOM 3029 C CG . LEU A 1 436 ? 5.908 44.658 40.754 1.00 17.92 ? 429 LEU A CG 1 ATOM 3030 C CD1 . LEU A 1 436 ? 5.281 43.552 39.908 1.00 18.20 ? 429 LEU A CD1 1 ATOM 3031 C CD2 . LEU A 1 436 ? 5.768 46.016 40.030 1.00 17.44 ? 429 LEU A CD2 1 ATOM 3032 N N . GLY A 1 437 ? 5.423 44.654 45.237 1.00 17.87 ? 430 GLY A N 1 ATOM 3033 C CA . GLY A 1 437 ? 4.751 44.415 46.524 1.00 17.43 ? 430 GLY A CA 1 ATOM 3034 C C . GLY A 1 437 ? 4.782 45.613 47.469 1.00 17.93 ? 430 GLY A C 1 ATOM 3035 O O . GLY A 1 437 ? 3.737 45.984 48.004 1.00 17.60 ? 430 GLY A O 1 ATOM 3036 N N . SER A 1 438 ? 5.955 46.225 47.669 1.00 16.85 ? 431 SER A N 1 ATOM 3037 C CA . SER A 1 438 ? 6.064 47.422 48.539 1.00 16.97 ? 431 SER A CA 1 ATOM 3038 C C . SER A 1 438 ? 5.228 48.572 47.922 1.00 17.33 ? 431 SER A C 1 ATOM 3039 O O . SER A 1 438 ? 4.490 49.263 48.646 1.00 16.78 ? 431 SER A O 1 ATOM 3040 C CB . SER A 1 438 ? 7.536 47.851 48.661 1.00 17.24 ? 431 SER A CB 1 ATOM 3041 O OG . SER A 1 438 ? 8.127 48.149 47.381 1.00 17.48 ? 431 SER A OG 1 ATOM 3042 N N . THR A 1 439 ? 5.337 48.748 46.599 1.00 16.42 ? 432 THR A N 1 ATOM 3043 C CA . THR A 1 439 ? 4.672 49.874 45.935 1.00 16.91 ? 432 THR A CA 1 ATOM 3044 C C . THR A 1 439 ? 3.152 49.735 45.998 1.00 15.61 ? 432 THR A C 1 ATOM 3045 O O . THR A 1 439 ? 2.474 50.719 46.344 1.00 17.55 ? 432 THR A O 1 ATOM 3046 C CB . THR A 1 439 ? 5.147 50.099 44.489 1.00 17.30 ? 432 THR A CB 1 ATOM 3047 O OG1 . THR A 1 439 ? 6.577 50.235 44.527 1.00 18.69 ? 432 THR A OG1 1 ATOM 3048 C CG2 . THR A 1 439 ? 4.585 51.457 43.942 1.00 16.38 ? 432 THR A CG2 1 ATOM 3049 N N . GLU A 1 440 ? 2.602 48.550 45.711 1.00 15.25 ? 433 GLU A N 1 ATOM 3050 C CA . GLU A 1 440 ? 1.127 48.405 45.803 1.00 16.40 ? 433 GLU A CA 1 ATOM 3051 C C . GLU A 1 440 ? 0.621 48.631 47.221 1.00 16.61 ? 433 GLU A C 1 ATOM 3052 O O . GLU A 1 440 ? -0.438 49.252 47.415 1.00 17.55 ? 433 GLU A O 1 ATOM 3053 C CB . GLU A 1 440 ? 0.627 47.018 45.320 1.00 16.64 ? 433 GLU A CB 1 ATOM 3054 C CG . GLU A 1 440 ? 0.915 46.782 43.772 1.00 18.13 ? 433 GLU A CG 1 ATOM 3055 C CD . GLU A 1 440 ? 0.341 47.895 42.914 1.00 15.48 ? 433 GLU A CD 1 ATOM 3056 O OE1 . GLU A 1 440 ? -0.887 48.172 43.037 1.00 17.57 ? 433 GLU A OE1 1 ATOM 3057 O OE2 . GLU A 1 440 ? 1.124 48.545 42.162 1.00 18.02 ? 433 GLU A OE2 1 ATOM 3058 N N . TRP A 1 441 ? 1.331 48.071 48.194 1.00 16.10 ? 434 TRP A N 1 ATOM 3059 C CA . TRP A 1 441 ? 0.899 48.221 49.599 1.00 17.43 ? 434 TRP A CA 1 ATOM 3060 C C . TRP A 1 441 ? 0.957 49.722 49.977 1.00 17.44 ? 434 TRP A C 1 ATOM 3061 O O . TRP A 1 441 ? 0.068 50.225 50.600 1.00 17.26 ? 434 TRP A O 1 ATOM 3062 C CB . TRP A 1 441 ? 1.808 47.412 50.521 1.00 17.68 ? 434 TRP A CB 1 ATOM 3063 C CG . TRP A 1 441 ? 1.342 47.457 51.997 1.00 18.83 ? 434 TRP A CG 1 ATOM 3064 C CD1 . TRP A 1 441 ? 0.370 46.680 52.604 1.00 17.44 ? 434 TRP A CD1 1 ATOM 3065 C CD2 . TRP A 1 441 ? 1.867 48.325 52.988 1.00 20.29 ? 434 TRP A CD2 1 ATOM 3066 N NE1 . TRP A 1 441 ? 0.259 47.051 53.951 1.00 18.06 ? 434 TRP A NE1 1 ATOM 3067 C CE2 . TRP A 1 441 ? 1.182 48.037 54.217 1.00 21.43 ? 434 TRP A CE2 1 ATOM 3068 C CE3 . TRP A 1 441 ? 2.846 49.345 52.960 1.00 18.03 ? 434 TRP A CE3 1 ATOM 3069 C CZ2 . TRP A 1 441 ? 1.448 48.729 55.421 1.00 19.36 ? 434 TRP A CZ2 1 ATOM 3070 C CZ3 . TRP A 1 441 ? 3.148 50.031 54.204 1.00 19.68 ? 434 TRP A CZ3 1 ATOM 3071 C CH2 . TRP A 1 441 ? 2.423 49.720 55.397 1.00 20.36 ? 434 TRP A CH2 1 ATOM 3072 N N . ALA A 1 442 ? 1.995 50.437 49.548 1.00 17.13 ? 435 ALA A N 1 ATOM 3073 C CA . ALA A 1 442 ? 2.075 51.863 49.879 1.00 16.76 ? 435 ALA A CA 1 ATOM 3074 C C . ALA A 1 442 ? 1.012 52.683 49.145 1.00 16.56 ? 435 ALA A C 1 ATOM 3075 O O . ALA A 1 442 ? 0.499 53.653 49.692 1.00 15.91 ? 435 ALA A O 1 ATOM 3076 C CB . ALA A 1 442 ? 3.483 52.408 49.597 1.00 16.60 ? 435 ALA A CB 1 ATOM 3077 N N . GLU A 1 443 ? 0.645 52.274 47.932 1.00 16.30 ? 436 GLU A N 1 ATOM 3078 C CA . GLU A 1 443 ? -0.481 52.934 47.226 1.00 17.44 ? 436 GLU A CA 1 ATOM 3079 C C . GLU A 1 443 ? -1.789 52.699 47.977 1.00 18.17 ? 436 GLU A C 1 ATOM 3080 O O . GLU A 1 443 ? -2.629 53.605 48.093 1.00 17.96 ? 436 GLU A O 1 ATOM 3081 C CB . GLU A 1 443 ? -0.650 52.449 45.749 1.00 17.45 ? 436 GLU A CB 1 ATOM 3082 C CG . GLU A 1 443 ? 0.500 52.993 44.864 1.00 18.30 ? 436 GLU A CG 1 ATOM 3083 C CD . GLU A 1 443 ? 0.372 52.595 43.396 1.00 16.54 ? 436 GLU A CD 1 ATOM 3084 O OE1 . GLU A 1 443 ? 0.746 53.418 42.533 1.00 20.09 ? 436 GLU A OE1 1 ATOM 3085 O OE2 . GLU A 1 443 ? -0.086 51.466 43.120 1.00 18.47 ? 436 GLU A OE2 1 ATOM 3086 N N . GLU A 1 444 ? -1.959 51.482 48.499 1.00 17.76 ? 437 GLU A N 1 ATOM 3087 C CA . GLU A 1 444 ? -3.172 51.193 49.261 1.00 18.12 ? 437 GLU A CA 1 ATOM 3088 C C . GLU A 1 444 ? -3.233 52.053 50.547 1.00 17.43 ? 437 GLU A C 1 ATOM 3089 O O . GLU A 1 444 ? -4.288 52.591 50.922 1.00 18.20 ? 437 GLU A O 1 ATOM 3090 C CB . GLU A 1 444 ? -3.168 49.707 49.623 1.00 17.48 ? 437 GLU A CB 1 ATOM 3091 C CG . GLU A 1 444 ? -4.502 49.250 50.339 1.00 24.32 ? 437 GLU A CG 1 ATOM 3092 C CD . GLU A 1 444 ? -4.660 47.752 50.108 1.00 31.76 ? 437 GLU A CD 1 ATOM 3093 O OE1 . GLU A 1 444 ? -5.365 47.312 49.183 1.00 39.19 ? 437 GLU A OE1 1 ATOM 3094 O OE2 . GLU A 1 444 ? -3.937 47.032 50.764 1.00 30.73 ? 437 GLU A OE2 1 ATOM 3095 N N . ASN A 1 445 ? -2.090 52.185 51.210 1.00 16.63 ? 438 ASN A N 1 ATOM 3096 C CA . ASN A 1 445 ? -2.009 52.788 52.560 1.00 17.69 ? 438 ASN A CA 1 ATOM 3097 C C . ASN A 1 445 ? -1.435 54.201 52.579 1.00 16.73 ? 438 ASN A C 1 ATOM 3098 O O . ASN A 1 445 ? -1.069 54.735 53.636 1.00 16.44 ? 438 ASN A O 1 ATOM 3099 C CB . ASN A 1 445 ? -1.230 51.840 53.513 1.00 17.82 ? 438 ASN A CB 1 ATOM 3100 C CG . ASN A 1 445 ? -2.000 50.594 53.767 1.00 18.02 ? 438 ASN A CG 1 ATOM 3101 O OD1 . ASN A 1 445 ? -2.957 50.632 54.536 1.00 19.77 ? 438 ASN A OD1 1 ATOM 3102 N ND2 . ASN A 1 445 ? -1.631 49.483 53.106 1.00 19.06 ? 438 ASN A ND2 1 ATOM 3103 N N . SER A 1 446 ? -1.460 54.846 51.411 1.00 16.15 ? 439 SER A N 1 ATOM 3104 C CA . SER A 1 446 ? -0.728 56.105 51.271 1.00 17.95 ? 439 SER A CA 1 ATOM 3105 C C . SER A 1 446 ? -1.152 57.210 52.259 1.00 17.07 ? 439 SER A C 1 ATOM 3106 O O . SER A 1 446 ? -0.315 58.002 52.693 1.00 18.18 ? 439 SER A O 1 ATOM 3107 C CB . SER A 1 446 ? -0.832 56.679 49.827 1.00 17.80 ? 439 SER A CB 1 ATOM 3108 O OG . SER A 1 446 ? -2.162 56.990 49.507 1.00 18.85 ? 439 SER A OG 1 ATOM 3109 N N . ARG A 1 447 ? -2.444 57.316 52.548 1.00 17.81 ? 440 ARG A N 1 ATOM 3110 C CA . ARG A 1 447 ? -2.894 58.335 53.499 1.00 17.46 ? 440 ARG A CA 1 ATOM 3111 C C . ARG A 1 447 ? -2.365 58.083 54.927 1.00 19.41 ? 440 ARG A C 1 ATOM 3112 O O . ARG A 1 447 ? -2.017 59.045 55.654 1.00 18.98 ? 440 ARG A O 1 ATOM 3113 C CB . ARG A 1 447 ? -4.432 58.406 53.496 1.00 17.34 ? 440 ARG A CB 1 ATOM 3114 C CG . ARG A 1 447 ? -4.968 58.879 52.089 1.00 20.14 ? 440 ARG A CG 1 ATOM 3115 C CD . ARG A 1 447 ? -6.285 58.264 51.683 1.00 24.25 ? 440 ARG A CD 1 ATOM 3116 N NE . ARG A 1 447 ? -6.653 58.768 50.349 1.00 21.27 ? 440 ARG A NE 1 ATOM 3117 C CZ . ARG A 1 447 ? -6.210 58.316 49.183 1.00 23.54 ? 440 ARG A CZ 1 ATOM 3118 N NH1 . ARG A 1 447 ? -5.343 57.273 49.100 1.00 23.36 ? 440 ARG A NH1 1 ATOM 3119 N NH2 . ARG A 1 447 ? -6.613 58.960 48.094 1.00 17.46 ? 440 ARG A NH2 1 ATOM 3120 N N . LEU A 1 448 ? -2.364 56.821 55.349 1.00 18.74 ? 441 LEU A N 1 ATOM 3121 C CA . LEU A 1 448 ? -1.811 56.468 56.677 1.00 18.85 ? 441 LEU A CA 1 ATOM 3122 C C . LEU A 1 448 ? -0.306 56.792 56.717 1.00 19.83 ? 441 LEU A C 1 ATOM 3123 O O . LEU A 1 448 ? 0.195 57.415 57.644 1.00 18.65 ? 441 LEU A O 1 ATOM 3124 C CB . LEU A 1 448 ? -2.026 54.972 56.939 1.00 18.94 ? 441 LEU A CB 1 ATOM 3125 C CG . LEU A 1 448 ? -3.440 54.386 56.800 1.00 19.05 ? 441 LEU A CG 1 ATOM 3126 C CD1 . LEU A 1 448 ? -3.536 52.943 57.340 1.00 19.70 ? 441 LEU A CD1 1 ATOM 3127 C CD2 . LEU A 1 448 ? -4.494 55.248 57.499 1.00 22.59 ? 441 LEU A CD2 1 ATOM 3128 N N . LEU A 1 449 ? 0.382 56.413 55.653 1.00 18.70 ? 442 LEU A N 1 ATOM 3129 C CA . LEU A 1 449 ? 1.831 56.588 55.598 1.00 18.94 ? 442 LEU A CA 1 ATOM 3130 C C . LEU A 1 449 ? 2.223 58.051 55.552 1.00 18.94 ? 442 LEU A C 1 ATOM 3131 O O . LEU A 1 449 ? 3.197 58.461 56.177 1.00 21.26 ? 442 LEU A O 1 ATOM 3132 C CB . LEU A 1 449 ? 2.401 55.827 54.366 1.00 19.04 ? 442 LEU A CB 1 ATOM 3133 C CG . LEU A 1 449 ? 2.306 54.300 54.425 1.00 21.34 ? 442 LEU A CG 1 ATOM 3134 C CD1 . LEU A 1 449 ? 2.632 53.709 52.988 1.00 18.15 ? 442 LEU A CD1 1 ATOM 3135 C CD2 . LEU A 1 449 ? 3.267 53.660 55.490 1.00 22.81 ? 442 LEU A CD2 1 ATOM 3136 N N A GLN A 1 450 ? 1.466 58.803 54.741 0.50 18.99 ? 443 GLN A N 1 ATOM 3137 N N B GLN A 1 450 ? 1.501 58.859 54.801 0.50 18.70 ? 443 GLN A N 1 ATOM 3138 C CA A GLN A 1 450 ? 1.527 60.257 54.576 0.50 19.97 ? 443 GLN A CA 1 ATOM 3139 C CA B GLN A 1 450 ? 1.918 60.230 54.666 0.50 19.28 ? 443 GLN A CA 1 ATOM 3140 C C A GLN A 1 450 ? 1.635 60.932 55.944 0.50 18.98 ? 443 GLN A C 1 ATOM 3141 C C B GLN A 1 450 ? 1.605 61.063 55.935 0.50 18.54 ? 443 GLN A C 1 ATOM 3142 O O A GLN A 1 450 ? 2.589 61.665 56.264 0.50 18.06 ? 443 GLN A O 1 ATOM 3143 O O B GLN A 1 450 ? 2.241 62.099 56.153 0.50 17.31 ? 443 GLN A O 1 ATOM 3144 C CB A GLN A 1 450 ? 0.170 60.695 53.944 0.50 18.96 ? 443 GLN A CB 1 ATOM 3145 C CB B GLN A 1 450 ? 1.193 60.854 53.496 0.50 18.21 ? 443 GLN A CB 1 ATOM 3146 C CG A GLN A 1 450 ? 0.156 61.895 53.210 0.50 21.62 ? 443 GLN A CG 1 ATOM 3147 C CG B GLN A 1 450 ? 0.588 62.205 53.870 0.50 22.06 ? 443 GLN A CG 1 ATOM 3148 C CD A GLN A 1 450 ? -0.291 61.671 51.802 0.50 21.24 ? 443 GLN A CD 1 ATOM 3149 C CD B GLN A 1 450 ? 1.260 63.242 53.017 0.50 21.61 ? 443 GLN A CD 1 ATOM 3150 O OE1 A GLN A 1 450 ? -1.470 61.818 51.506 0.50 19.75 ? 443 GLN A OE1 1 ATOM 3151 O OE1 B GLN A 1 450 ? 1.536 64.398 53.419 0.50 18.61 ? 443 GLN A OE1 1 ATOM 3152 N NE2 A GLN A 1 450 ? 0.648 61.329 50.913 0.50 18.47 ? 443 GLN A NE2 1 ATOM 3153 N NE2 B GLN A 1 450 ? 1.579 62.792 51.803 0.50 22.10 ? 443 GLN A NE2 1 ATOM 3154 N N . GLU A 1 451 ? 0.624 60.648 56.747 1.00 18.70 ? 444 GLU A N 1 ATOM 3155 C CA . GLU A 1 451 ? 0.364 61.423 57.957 1.00 18.41 ? 444 GLU A CA 1 ATOM 3156 C C . GLU A 1 451 ? 0.996 60.791 59.187 1.00 17.70 ? 444 GLU A C 1 ATOM 3157 O O . GLU A 1 451 ? 1.116 61.471 60.200 1.00 18.64 ? 444 GLU A O 1 ATOM 3158 C CB . GLU A 1 451 ? -1.140 61.626 58.193 1.00 18.99 ? 444 GLU A CB 1 ATOM 3159 C CG . GLU A 1 451 ? -1.923 62.155 56.955 1.00 20.36 ? 444 GLU A CG 1 ATOM 3160 C CD . GLU A 1 451 ? -1.322 63.449 56.351 1.00 25.53 ? 444 GLU A CD 1 ATOM 3161 O OE1 . GLU A 1 451 ? -0.323 63.985 56.890 1.00 21.07 ? 444 GLU A OE1 1 ATOM 3162 O OE2 . GLU A 1 451 ? -1.848 63.928 55.306 1.00 23.74 ? 444 GLU A OE2 1 ATOM 3163 N N . ARG A 1 452 ? 1.383 59.515 59.082 1.00 16.52 ? 445 ARG A N 1 ATOM 3164 C CA . ARG A 1 452 ? 1.899 58.813 60.272 1.00 17.59 ? 445 ARG A CA 1 ATOM 3165 C C . ARG A 1 452 ? 3.303 58.194 60.151 1.00 18.48 ? 445 ARG A C 1 ATOM 3166 O O . ARG A 1 452 ? 3.797 57.715 61.129 1.00 20.27 ? 445 ARG A O 1 ATOM 3167 C CB . ARG A 1 452 ? 0.927 57.698 60.678 1.00 17.18 ? 445 ARG A CB 1 ATOM 3168 C CG . ARG A 1 452 ? -0.562 58.210 60.882 1.00 18.19 ? 445 ARG A CG 1 ATOM 3169 C CD . ARG A 1 452 ? -1.521 57.035 61.150 1.00 19.34 ? 445 ARG A CD 1 ATOM 3170 N NE . ARG A 1 452 ? -2.923 57.496 61.111 1.00 19.79 ? 445 ARG A NE 1 ATOM 3171 C CZ . ARG A 1 452 ? -3.967 56.691 61.085 1.00 19.22 ? 445 ARG A CZ 1 ATOM 3172 N NH1 . ARG A 1 452 ? -3.733 55.378 61.088 1.00 19.87 ? 445 ARG A NH1 1 ATOM 3173 N NH2 . ARG A 1 452 ? -5.227 57.195 61.033 1.00 19.36 ? 445 ARG A NH2 1 ATOM 3174 N N . GLY A 1 453 ? 3.916 58.228 58.970 1.00 18.73 ? 446 GLY A N 1 ATOM 3175 C CA . GLY A 1 453 ? 5.135 57.466 58.671 1.00 19.08 ? 446 GLY A CA 1 ATOM 3176 C C . GLY A 1 453 ? 6.321 58.260 59.194 1.00 20.06 ? 446 GLY A C 1 ATOM 3177 O O . GLY A 1 453 ? 6.664 59.358 58.691 1.00 20.64 ? 446 GLY A O 1 ATOM 3178 N N . VAL A 1 454 ? 6.963 57.716 60.223 1.00 18.74 ? 447 VAL A N 1 ATOM 3179 C CA . VAL A 1 454 ? 8.157 58.354 60.763 1.00 19.01 ? 447 VAL A CA 1 ATOM 3180 C C . VAL A 1 454 ? 9.373 58.082 59.890 1.00 19.90 ? 447 VAL A C 1 ATOM 3181 O O . VAL A 1 454 ? 10.113 59.006 59.525 1.00 19.28 ? 447 VAL A O 1 ATOM 3182 C CB . VAL A 1 454 ? 8.403 57.875 62.223 1.00 20.86 ? 447 VAL A CB 1 ATOM 3183 C CG1 . VAL A 1 454 ? 9.797 58.249 62.714 1.00 19.84 ? 447 VAL A CG1 1 ATOM 3184 C CG2 . VAL A 1 454 ? 7.298 58.474 63.129 1.00 22.20 ? 447 VAL A CG2 1 ATOM 3185 N N . ALA A 1 455 ? 9.603 56.793 59.594 1.00 19.45 ? 448 ALA A N 1 ATOM 3186 C CA . ALA A 1 455 ? 10.808 56.349 58.897 1.00 18.34 ? 448 ALA A CA 1 ATOM 3187 C C . ALA A 1 455 ? 10.578 54.974 58.292 1.00 18.80 ? 448 ALA A C 1 ATOM 3188 O O . ALA A 1 455 ? 9.749 54.167 58.791 1.00 19.44 ? 448 ALA A O 1 ATOM 3189 C CB . ALA A 1 455 ? 12.026 56.283 59.871 1.00 18.27 ? 448 ALA A CB 1 ATOM 3190 N N . TYR A 1 456 ? 11.348 54.698 57.233 1.00 18.30 ? 449 TYR A N 1 ATOM 3191 C CA . TYR A 1 456 ? 11.402 53.387 56.620 1.00 18.25 ? 449 TYR A CA 1 ATOM 3192 C C . TYR A 1 456 ? 12.873 52.962 56.563 1.00 18.35 ? 449 TYR A C 1 ATOM 3193 O O . TYR A 1 456 ? 13.746 53.665 56.035 1.00 19.39 ? 449 TYR A O 1 ATOM 3194 C CB . TYR A 1 456 ? 10.812 53.472 55.207 1.00 16.35 ? 449 TYR A CB 1 ATOM 3195 C CG . TYR A 1 456 ? 10.934 52.156 54.479 1.00 16.94 ? 449 TYR A CG 1 ATOM 3196 C CD1 . TYR A 1 456 ? 9.950 51.176 54.617 1.00 18.88 ? 449 TYR A CD1 1 ATOM 3197 C CD2 . TYR A 1 456 ? 12.041 51.869 53.705 1.00 18.86 ? 449 TYR A CD2 1 ATOM 3198 C CE1 . TYR A 1 456 ? 10.056 49.930 53.985 1.00 17.80 ? 449 TYR A CE1 1 ATOM 3199 C CE2 . TYR A 1 456 ? 12.160 50.611 53.037 1.00 19.26 ? 449 TYR A CE2 1 ATOM 3200 C CZ . TYR A 1 456 ? 11.143 49.665 53.192 1.00 19.22 ? 449 TYR A CZ 1 ATOM 3201 O OH . TYR A 1 456 ? 11.202 48.460 52.509 1.00 20.03 ? 449 TYR A OH 1 ATOM 3202 N N . ILE A 1 457 ? 13.140 51.787 57.097 1.00 18.88 ? 450 ILE A N 1 ATOM 3203 C CA . ILE A 1 457 ? 14.428 51.184 57.038 1.00 19.24 ? 450 ILE A CA 1 ATOM 3204 C C . ILE A 1 457 ? 14.300 49.937 56.106 1.00 20.22 ? 450 ILE A C 1 ATOM 3205 O O . ILE A 1 457 ? 13.523 49.017 56.392 1.00 19.24 ? 450 ILE A O 1 ATOM 3206 C CB . ILE A 1 457 ? 14.896 50.716 58.451 1.00 21.23 ? 450 ILE A CB 1 ATOM 3207 C CG1 . ILE A 1 457 ? 15.004 51.907 59.458 1.00 21.57 ? 450 ILE A CG1 1 ATOM 3208 C CG2 . ILE A 1 457 ? 16.282 49.994 58.354 1.00 18.58 ? 450 ILE A CG2 1 ATOM 3209 C CD1 . ILE A 1 457 ? 15.935 53.058 58.917 1.00 21.36 ? 450 ILE A CD1 1 ATOM 3210 N N . ASN A 1 458 ? 15.062 49.919 55.012 1.00 19.70 ? 451 ASN A N 1 ATOM 3211 C CA . ASN A 1 458 ? 15.059 48.806 54.089 1.00 18.78 ? 451 ASN A CA 1 ATOM 3212 C C . ASN A 1 458 ? 15.826 47.590 54.625 1.00 21.34 ? 451 ASN A C 1 ATOM 3213 O O . ASN A 1 458 ? 16.658 47.691 55.555 1.00 21.38 ? 451 ASN A O 1 ATOM 3214 C CB . ASN A 1 458 ? 15.662 49.224 52.739 1.00 19.72 ? 451 ASN A CB 1 ATOM 3215 C CG . ASN A 1 458 ? 15.083 48.420 51.568 1.00 21.44 ? 451 ASN A CG 1 ATOM 3216 O OD1 . ASN A 1 458 ? 13.867 48.314 51.423 1.00 19.47 ? 451 ASN A OD1 1 ATOM 3217 N ND2 . ASN A 1 458 ? 15.944 47.881 50.734 1.00 18.82 ? 451 ASN A ND2 1 ATOM 3218 N N . ALA A 1 459 ? 15.565 46.426 54.025 1.00 20.61 ? 452 ALA A N 1 ATOM 3219 C CA . ALA A 1 459 ? 16.242 45.214 54.520 1.00 20.39 ? 452 ALA A CA 1 ATOM 3220 C C . ALA A 1 459 ? 16.362 44.145 53.432 1.00 19.46 ? 452 ALA A C 1 ATOM 3221 O O . ALA A 1 459 ? 15.977 42.976 53.630 1.00 21.50 ? 452 ALA A O 1 ATOM 3222 C CB . ALA A 1 459 ? 15.484 44.614 55.771 1.00 19.59 ? 452 ALA A CB 1 ATOM 3223 N N . ASP A 1 460 ? 16.958 44.516 52.317 1.00 19.49 ? 453 ASP A N 1 ATOM 3224 C CA . ASP A 1 460 ? 17.398 43.512 51.339 1.00 18.80 ? 453 ASP A CA 1 ATOM 3225 C C . ASP A 1 460 ? 18.770 42.973 51.818 1.00 20.68 ? 453 ASP A C 1 ATOM 3226 O O . ASP A 1 460 ? 19.107 43.126 52.987 1.00 20.03 ? 453 ASP A O 1 ATOM 3227 C CB . ASP A 1 460 ? 17.461 44.144 49.950 1.00 18.89 ? 453 ASP A CB 1 ATOM 3228 C CG . ASP A 1 460 ? 17.325 43.113 48.809 1.00 21.33 ? 453 ASP A CG 1 ATOM 3229 O OD1 . ASP A 1 460 ? 17.467 41.919 49.077 1.00 22.48 ? 453 ASP A OD1 1 ATOM 3230 O OD2 . ASP A 1 460 ? 17.152 43.517 47.633 1.00 20.22 ? 453 ASP A OD2 1 ATOM 3231 N N . SER A 1 461 ? 19.486 42.275 50.937 1.00 20.60 ? 454 SER A N 1 ATOM 3232 C CA . SER A 1 461 ? 20.788 41.646 51.236 1.00 22.28 ? 454 SER A CA 1 ATOM 3233 C C . SER A 1 461 ? 21.605 42.361 52.330 1.00 21.98 ? 454 SER A C 1 ATOM 3234 O O . SER A 1 461 ? 21.840 43.571 52.270 1.00 21.25 ? 454 SER A O 1 ATOM 3235 C CB . SER A 1 461 ? 21.595 41.479 49.955 1.00 22.26 ? 454 SER A CB 1 ATOM 3236 O OG . SER A 1 461 ? 20.753 41.017 48.894 1.00 23.72 ? 454 SER A OG 1 ATOM 3237 N N . SER A 1 462 ? 21.941 41.610 53.373 1.00 22.83 ? 455 SER A N 1 ATOM 3238 C CA . SER A 1 462 ? 22.743 42.148 54.492 1.00 25.10 ? 455 SER A CA 1 ATOM 3239 C C . SER A 1 462 ? 24.231 42.203 54.131 1.00 25.19 ? 455 SER A C 1 ATOM 3240 O O . SER A 1 462 ? 24.995 42.959 54.718 1.00 25.85 ? 455 SER A O 1 ATOM 3241 C CB . SER A 1 462 ? 22.572 41.229 55.681 1.00 26.62 ? 455 SER A CB 1 ATOM 3242 O OG . SER A 1 462 ? 21.293 41.399 56.226 1.00 30.10 ? 455 SER A OG 1 ATOM 3243 N N . ILE A 1 463 ? 24.639 41.395 53.167 1.00 25.77 ? 456 ILE A N 1 ATOM 3244 C CA . ILE A 1 463 ? 26.056 41.361 52.768 1.00 27.37 ? 456 ILE A CA 1 ATOM 3245 C C . ILE A 1 463 ? 26.130 41.387 51.255 1.00 28.18 ? 456 ILE A C 1 ATOM 3246 O O . ILE A 1 463 ? 25.318 40.747 50.581 1.00 29.89 ? 456 ILE A O 1 ATOM 3247 C CB . ILE A 1 463 ? 26.778 40.077 53.307 1.00 28.10 ? 456 ILE A CB 1 ATOM 3248 C CG1 . ILE A 1 463 ? 25.929 38.812 53.013 1.00 29.04 ? 456 ILE A CG1 1 ATOM 3249 C CG2 . ILE A 1 463 ? 27.030 40.201 54.787 1.00 27.14 ? 456 ILE A CG2 1 ATOM 3250 C CD1 . ILE A 1 463 ? 26.741 37.589 52.634 1.00 35.03 ? 456 ILE A CD1 1 ATOM 3251 N N . GLU A 1 464 ? 27.106 42.097 50.705 1.00 28.06 ? 457 GLU A N 1 ATOM 3252 C CA . GLU A 1 464 ? 27.449 41.915 49.293 1.00 29.04 ? 457 GLU A CA 1 ATOM 3253 C C . GLU A 1 464 ? 28.967 41.814 49.192 1.00 29.75 ? 457 GLU A C 1 ATOM 3254 O O . GLU A 1 464 ? 29.556 41.884 48.111 1.00 30.49 ? 457 GLU A O 1 ATOM 3255 C CB . GLU A 1 464 ? 26.899 43.068 48.437 1.00 28.69 ? 457 GLU A CB 1 ATOM 3256 C CG . GLU A 1 464 ? 27.457 44.417 48.826 1.00 30.71 ? 457 GLU A CG 1 ATOM 3257 C CD . GLU A 1 464 ? 26.754 45.603 48.150 1.00 32.13 ? 457 GLU A CD 1 ATOM 3258 O OE1 . GLU A 1 464 ? 25.702 45.444 47.512 1.00 32.66 ? 457 GLU A OE1 1 ATOM 3259 O OE2 . GLU A 1 464 ? 27.276 46.714 48.275 1.00 34.06 ? 457 GLU A OE2 1 ATOM 3260 N N . GLY A 1 465 ? 29.600 41.639 50.353 1.00 29.84 ? 458 GLY A N 1 ATOM 3261 C CA . GLY A 1 465 ? 31.062 41.605 50.488 1.00 29.45 ? 458 GLY A CA 1 ATOM 3262 C C . GLY A 1 465 ? 31.348 41.474 51.981 1.00 30.27 ? 458 GLY A C 1 ATOM 3263 O O . GLY A 1 465 ? 30.416 41.381 52.777 1.00 30.34 ? 458 GLY A O 1 ATOM 3264 N N . ASN A 1 466 ? 32.606 41.531 52.382 1.00 29.41 ? 459 ASN A N 1 ATOM 3265 C CA . ASN A 1 466 ? 32.928 41.377 53.789 1.00 30.78 ? 459 ASN A CA 1 ATOM 3266 C C . ASN A 1 466 ? 33.955 42.414 54.234 1.00 31.07 ? 459 ASN A C 1 ATOM 3267 O O . ASN A 1 466 ? 34.683 42.210 55.180 1.00 31.78 ? 459 ASN A O 1 ATOM 3268 C CB . ASN A 1 466 ? 33.386 39.922 54.086 1.00 32.52 ? 459 ASN A CB 1 ATOM 3269 C CG . ASN A 1 466 ? 34.720 39.554 53.401 1.00 33.44 ? 459 ASN A CG 1 ATOM 3270 O OD1 . ASN A 1 466 ? 35.374 40.417 52.797 1.00 35.72 ? 459 ASN A OD1 1 ATOM 3271 N ND2 . ASN A 1 466 ? 35.127 38.267 53.497 1.00 41.32 ? 459 ASN A ND2 1 ATOM 3272 N N . TYR A 1 467 ? 33.979 43.546 53.543 1.00 30.79 ? 460 TYR A N 1 ATOM 3273 C CA . TYR A 1 467 ? 34.992 44.552 53.782 1.00 31.54 ? 460 TYR A CA 1 ATOM 3274 C C . TYR A 1 467 ? 34.578 45.587 54.841 1.00 30.97 ? 460 TYR A C 1 ATOM 3275 O O . TYR A 1 467 ? 35.280 45.758 55.847 1.00 30.57 ? 460 TYR A O 1 ATOM 3276 C CB . TYR A 1 467 ? 35.357 45.233 52.457 1.00 33.21 ? 460 TYR A CB 1 ATOM 3277 C CG . TYR A 1 467 ? 36.471 46.260 52.582 1.00 36.04 ? 460 TYR A CG 1 ATOM 3278 C CD1 . TYR A 1 467 ? 37.768 45.890 52.981 1.00 40.42 ? 460 TYR A CD1 1 ATOM 3279 C CD2 . TYR A 1 467 ? 36.228 47.595 52.270 1.00 39.52 ? 460 TYR A CD2 1 ATOM 3280 C CE1 . TYR A 1 467 ? 38.784 46.840 53.083 1.00 43.78 ? 460 TYR A CE1 1 ATOM 3281 C CE2 . TYR A 1 467 ? 37.232 48.551 52.364 1.00 41.38 ? 460 TYR A CE2 1 ATOM 3282 C CZ . TYR A 1 467 ? 38.485 48.178 52.772 1.00 45.25 ? 460 TYR A CZ 1 ATOM 3283 O OH . TYR A 1 467 ? 39.449 49.150 52.848 1.00 48.12 ? 460 TYR A OH 1 ATOM 3284 N N . THR A 1 468 ? 33.458 46.290 54.616 1.00 29.34 ? 461 THR A N 1 ATOM 3285 C CA . THR A 1 468 ? 33.060 47.335 55.556 1.00 29.14 ? 461 THR A CA 1 ATOM 3286 C C . THR A 1 468 ? 31.578 47.611 55.386 1.00 27.91 ? 461 THR A C 1 ATOM 3287 O O . THR A 1 468 ? 30.931 47.000 54.533 1.00 27.64 ? 461 THR A O 1 ATOM 3288 C CB . THR A 1 468 ? 33.903 48.650 55.409 1.00 29.85 ? 461 THR A CB 1 ATOM 3289 O OG1 . THR A 1 468 ? 33.674 49.502 56.538 1.00 29.93 ? 461 THR A OG1 1 ATOM 3290 C CG2 . THR A 1 468 ? 33.525 49.422 54.147 1.00 28.47 ? 461 THR A CG2 1 ATOM 3291 N N . LEU A 1 469 ? 31.054 48.498 56.227 1.00 27.88 ? 462 LEU A N 1 ATOM 3292 C CA . LEU A 1 469 ? 29.649 48.939 56.106 1.00 26.40 ? 462 LEU A CA 1 ATOM 3293 C C . LEU A 1 469 ? 29.402 49.849 54.938 1.00 25.86 ? 462 LEU A C 1 ATOM 3294 O O . LEU A 1 469 ? 30.288 50.606 54.546 1.00 26.56 ? 462 LEU A O 1 ATOM 3295 C CB . LEU A 1 469 ? 29.212 49.669 57.388 1.00 26.48 ? 462 LEU A CB 1 ATOM 3296 C CG . LEU A 1 469 ? 27.731 49.893 57.689 1.00 25.38 ? 462 LEU A CG 1 ATOM 3297 C CD1 . LEU A 1 469 ? 27.069 48.554 57.967 1.00 26.99 ? 462 LEU A CD1 1 ATOM 3298 C CD2 . LEU A 1 469 ? 27.729 50.814 58.973 1.00 25.97 ? 462 LEU A CD2 1 ATOM 3299 N N . ARG A 1 470 ? 28.186 49.781 54.396 1.00 24.33 ? 463 ARG A N 1 ATOM 3300 C CA . ARG A 1 470 ? 27.772 50.667 53.349 1.00 26.20 ? 463 ARG A CA 1 ATOM 3301 C C . ARG A 1 470 ? 26.405 51.183 53.810 1.00 25.52 ? 463 ARG A C 1 ATOM 3302 O O . ARG A 1 470 ? 25.472 50.384 54.044 1.00 26.05 ? 463 ARG A O 1 ATOM 3303 C CB . ARG A 1 470 ? 27.616 49.873 52.035 1.00 26.06 ? 463 ARG A CB 1 ATOM 3304 C CG . ARG A 1 470 ? 27.121 50.695 50.829 1.00 28.36 ? 463 ARG A CG 1 ATOM 3305 C CD . ARG A 1 470 ? 26.926 49.814 49.581 1.00 33.67 ? 463 ARG A CD 1 ATOM 3306 N NE . ARG A 1 470 ? 26.574 50.603 48.383 1.00 41.55 ? 463 ARG A NE 1 ATOM 3307 C CZ . ARG A 1 470 ? 26.322 50.100 47.167 1.00 43.40 ? 463 ARG A CZ 1 ATOM 3308 N NH1 . ARG A 1 470 ? 26.359 48.789 46.950 1.00 43.68 ? 463 ARG A NH1 1 ATOM 3309 N NH2 . ARG A 1 470 ? 26.020 50.907 46.151 1.00 43.47 ? 463 ARG A NH2 1 ATOM 3310 N N . VAL A 1 471 ? 26.264 52.505 53.898 1.00 25.14 ? 464 VAL A N 1 ATOM 3311 C CA . VAL A 1 471 ? 25.005 53.118 54.331 1.00 23.47 ? 464 VAL A CA 1 ATOM 3312 C C . VAL A 1 471 ? 24.552 54.159 53.317 1.00 23.84 ? 464 VAL A C 1 ATOM 3313 O O . VAL A 1 471 ? 25.346 54.998 52.911 1.00 24.60 ? 464 VAL A O 1 ATOM 3314 C CB . VAL A 1 471 ? 25.174 53.819 55.691 1.00 24.58 ? 464 VAL A CB 1 ATOM 3315 C CG1 . VAL A 1 471 ? 23.859 54.566 56.126 1.00 21.86 ? 464 VAL A CG1 1 ATOM 3316 C CG2 . VAL A 1 471 ? 25.577 52.815 56.750 1.00 24.36 ? 464 VAL A CG2 1 ATOM 3317 N N . ASP A 1 472 ? 23.286 54.062 52.892 1.00 21.76 ? 465 ASP A N 1 ATOM 3318 C CA . ASP A 1 472 ? 22.623 55.110 52.093 1.00 22.58 ? 465 ASP A CA 1 ATOM 3319 C C . ASP A 1 472 ? 21.405 55.523 52.888 1.00 21.22 ? 465 ASP A C 1 ATOM 3320 O O . ASP A 1 472 ? 20.602 54.689 53.258 1.00 20.90 ? 465 ASP A O 1 ATOM 3321 C CB . ASP A 1 472 ? 22.145 54.643 50.679 1.00 20.03 ? 465 ASP A CB 1 ATOM 3322 C CG . ASP A 1 472 ? 23.178 53.821 49.918 1.00 26.31 ? 465 ASP A CG 1 ATOM 3323 O OD1 . ASP A 1 472 ? 24.356 53.798 50.310 1.00 27.46 ? 465 ASP A OD1 1 ATOM 3324 O OD2 . ASP A 1 472 ? 22.802 53.185 48.883 1.00 28.03 ? 465 ASP A OD2 1 ATOM 3325 N N . CYS A 1 473 ? 21.233 56.828 53.091 1.00 22.56 ? 466 CYS A N 1 ATOM 3326 C CA . CYS A 1 473 ? 20.114 57.310 53.852 1.00 21.27 ? 466 CYS A CA 1 ATOM 3327 C C . CYS A 1 473 ? 19.917 58.799 53.659 1.00 21.76 ? 466 CYS A C 1 ATOM 3328 O O . CYS A 1 473 ? 20.813 59.510 53.218 1.00 22.29 ? 466 CYS A O 1 ATOM 3329 C CB . CYS A 1 473 ? 20.255 56.978 55.372 1.00 22.44 ? 466 CYS A CB 1 ATOM 3330 S SG . CYS A 1 473 ? 21.546 57.872 56.270 1.00 24.07 ? 466 CYS A SG 1 ATOM 3331 N N . THR A 1 474 ? 18.732 59.250 54.046 1.00 21.09 ? 467 THR A N 1 ATOM 3332 C CA . THR A 1 474 ? 18.477 60.657 54.188 1.00 20.72 ? 467 THR A CA 1 ATOM 3333 C C . THR A 1 474 ? 19.454 61.376 55.132 1.00 21.06 ? 467 THR A C 1 ATOM 3334 O O . THR A 1 474 ? 19.865 60.824 56.190 1.00 21.03 ? 467 THR A O 1 ATOM 3335 C CB . THR A 1 474 ? 17.032 60.917 54.675 1.00 20.03 ? 467 THR A CB 1 ATOM 3336 O OG1 . THR A 1 474 ? 16.869 62.321 54.835 1.00 18.79 ? 467 THR A OG1 1 ATOM 3337 C CG2 . THR A 1 474 ? 16.757 60.233 56.033 1.00 19.16 ? 467 THR A CG2 1 ATOM 3338 N N . PRO A 1 475 ? 19.848 62.623 54.788 1.00 21.14 ? 468 PRO A N 1 ATOM 3339 C CA . PRO A 1 475 ? 20.657 63.372 55.804 1.00 23.51 ? 468 PRO A CA 1 ATOM 3340 C C . PRO A 1 475 ? 20.044 63.418 57.239 1.00 24.45 ? 468 PRO A C 1 ATOM 3341 O O . PRO A 1 475 ? 20.790 63.578 58.242 1.00 24.41 ? 468 PRO A O 1 ATOM 3342 C CB . PRO A 1 475 ? 20.720 64.823 55.206 1.00 23.36 ? 468 PRO A CB 1 ATOM 3343 C CG . PRO A 1 475 ? 20.499 64.638 53.735 1.00 23.33 ? 468 PRO A CG 1 ATOM 3344 C CD . PRO A 1 475 ? 19.580 63.435 53.569 1.00 21.92 ? 468 PRO A CD 1 ATOM 3345 N N . LEU A 1 476 ? 18.710 63.304 57.334 1.00 22.92 ? 469 LEU A N 1 ATOM 3346 C CA . LEU A 1 476 ? 18.039 63.322 58.653 1.00 22.81 ? 469 LEU A CA 1 ATOM 3347 C C . LEU A 1 476 ? 18.471 62.173 59.571 1.00 22.28 ? 469 LEU A C 1 ATOM 3348 O O . LEU A 1 476 ? 18.365 62.292 60.801 1.00 23.17 ? 469 LEU A O 1 ATOM 3349 C CB . LEU A 1 476 ? 16.502 63.288 58.528 1.00 23.34 ? 469 LEU A CB 1 ATOM 3350 C CG . LEU A 1 476 ? 15.867 64.551 57.977 1.00 21.20 ? 469 LEU A CG 1 ATOM 3351 C CD1 . LEU A 1 476 ? 14.375 64.389 57.975 1.00 21.07 ? 469 LEU A CD1 1 ATOM 3352 C CD2 . LEU A 1 476 ? 16.296 65.780 58.815 1.00 19.83 ? 469 LEU A CD2 1 ATOM 3353 N N . MET A 1 477 ? 19.009 61.103 58.992 1.00 21.23 ? 470 MET A N 1 ATOM 3354 C CA . MET A 1 477 ? 19.470 59.968 59.782 1.00 21.88 ? 470 MET A CA 1 ATOM 3355 C C . MET A 1 477 ? 20.992 59.925 59.959 1.00 22.68 ? 470 MET A C 1 ATOM 3356 O O . MET A 1 477 ? 21.486 59.041 60.646 1.00 23.71 ? 470 MET A O 1 ATOM 3357 C CB . MET A 1 477 ? 18.967 58.624 59.169 1.00 23.24 ? 470 MET A CB 1 ATOM 3358 C CG . MET A 1 477 ? 17.493 58.340 59.398 1.00 22.05 ? 470 MET A CG 1 ATOM 3359 S SD . MET A 1 477 ? 17.147 56.819 58.448 1.00 26.51 ? 470 MET A SD 1 ATOM 3360 C CE . MET A 1 477 ? 15.373 56.987 58.302 1.00 25.91 ? 470 MET A CE 1 ATOM 3361 N N . TYR A 1 478 ? 21.758 60.869 59.395 1.00 22.62 ? 471 TYR A N 1 ATOM 3362 C CA . TYR A 1 478 ? 23.238 60.789 59.576 1.00 23.86 ? 471 TYR A CA 1 ATOM 3363 C C . TYR A 1 478 ? 23.698 60.650 61.029 1.00 25.71 ? 471 TYR A C 1 ATOM 3364 O O . TYR A 1 478 ? 24.521 59.782 61.372 1.00 26.85 ? 471 TYR A O 1 ATOM 3365 C CB . TYR A 1 478 ? 23.969 62.005 58.979 1.00 24.00 ? 471 TYR A CB 1 ATOM 3366 C CG . TYR A 1 478 ? 23.974 62.130 57.459 1.00 24.60 ? 471 TYR A CG 1 ATOM 3367 C CD1 . TYR A 1 478 ? 23.397 61.152 56.620 1.00 25.30 ? 471 TYR A CD1 1 ATOM 3368 C CD2 . TYR A 1 478 ? 24.567 63.249 56.857 1.00 25.24 ? 471 TYR A CD2 1 ATOM 3369 C CE1 . TYR A 1 478 ? 23.408 61.343 55.179 1.00 24.50 ? 471 TYR A CE1 1 ATOM 3370 C CE2 . TYR A 1 478 ? 24.578 63.434 55.493 1.00 27.85 ? 471 TYR A CE2 1 ATOM 3371 C CZ . TYR A 1 478 ? 24.012 62.483 54.647 1.00 27.17 ? 471 TYR A CZ 1 ATOM 3372 O OH . TYR A 1 478 ? 24.070 62.711 53.271 1.00 25.92 ? 471 TYR A OH 1 ATOM 3373 N N . SER A 1 479 ? 23.227 61.574 61.881 1.00 25.49 ? 472 SER A N 1 ATOM 3374 C CA . SER A 1 479 ? 23.672 61.604 63.278 1.00 24.66 ? 472 SER A CA 1 ATOM 3375 C C . SER A 1 479 ? 23.259 60.353 64.029 1.00 25.68 ? 472 SER A C 1 ATOM 3376 O O . SER A 1 479 ? 24.012 59.843 64.808 1.00 24.30 ? 472 SER A O 1 ATOM 3377 C CB . SER A 1 479 ? 23.125 62.846 63.967 1.00 25.96 ? 472 SER A CB 1 ATOM 3378 O OG A SER A 1 479 ? 23.677 63.991 63.311 0.50 28.90 ? 472 SER A OG 1 ATOM 3379 O OG B SER A 1 479 ? 23.636 62.981 65.298 0.50 22.42 ? 472 SER A OG 1 ATOM 3380 N N . LEU A 1 480 ? 22.033 59.889 63.832 1.00 23.87 ? 473 LEU A N 1 ATOM 3381 C CA . LEU A 1 480 ? 21.598 58.586 64.355 1.00 24.73 ? 473 LEU A CA 1 ATOM 3382 C C . LEU A 1 480 ? 22.608 57.466 63.962 1.00 26.09 ? 473 LEU A C 1 ATOM 3383 O O . LEU A 1 480 ? 23.021 56.653 64.798 1.00 26.75 ? 473 LEU A O 1 ATOM 3384 C CB . LEU A 1 480 ? 20.203 58.261 63.750 1.00 23.65 ? 473 LEU A CB 1 ATOM 3385 C CG . LEU A 1 480 ? 19.676 56.802 63.790 1.00 22.84 ? 473 LEU A CG 1 ATOM 3386 C CD1 . LEU A 1 480 ? 19.461 56.357 65.201 1.00 30.04 ? 473 LEU A CD1 1 ATOM 3387 C CD2 . LEU A 1 480 ? 18.429 56.689 63.010 1.00 27.63 ? 473 LEU A CD2 1 ATOM 3388 N N . VAL A 1 481 ? 23.005 57.427 62.689 1.00 25.47 ? 474 VAL A N 1 ATOM 3389 C CA . VAL A 1 481 ? 23.947 56.372 62.234 1.00 26.13 ? 474 VAL A CA 1 ATOM 3390 C C . VAL A 1 481 ? 25.346 56.514 62.814 1.00 26.57 ? 474 VAL A C 1 ATOM 3391 O O . VAL A 1 481 ? 25.946 55.524 63.264 1.00 27.95 ? 474 VAL A O 1 ATOM 3392 C CB . VAL A 1 481 ? 24.031 56.317 60.693 1.00 25.35 ? 474 VAL A CB 1 ATOM 3393 C CG1 . VAL A 1 481 ? 25.101 55.324 60.224 1.00 26.59 ? 474 VAL A CG1 1 ATOM 3394 C CG2 . VAL A 1 481 ? 22.654 55.940 60.112 1.00 26.81 ? 474 VAL A CG2 1 ATOM 3395 N N . TYR A 1 482 ? 25.888 57.720 62.803 1.00 27.06 ? 475 TYR A N 1 ATOM 3396 C CA . TYR A 1 482 ? 27.208 57.921 63.442 1.00 27.96 ? 475 TYR A CA 1 ATOM 3397 C C . TYR A 1 482 ? 27.140 57.485 64.899 1.00 29.41 ? 475 TYR A C 1 ATOM 3398 O O . TYR A 1 482 ? 28.030 56.752 65.392 1.00 28.88 ? 475 TYR A O 1 ATOM 3399 C CB . TYR A 1 482 ? 27.654 59.379 63.419 1.00 27.91 ? 475 TYR A CB 1 ATOM 3400 C CG . TYR A 1 482 ? 27.681 60.058 62.079 1.00 30.62 ? 475 TYR A CG 1 ATOM 3401 C CD1 . TYR A 1 482 ? 28.091 59.391 60.912 1.00 31.12 ? 475 TYR A CD1 1 ATOM 3402 C CD2 . TYR A 1 482 ? 27.345 61.412 61.994 1.00 34.38 ? 475 TYR A CD2 1 ATOM 3403 C CE1 . TYR A 1 482 ? 28.114 60.087 59.668 1.00 30.32 ? 475 TYR A CE1 1 ATOM 3404 C CE2 . TYR A 1 482 ? 27.379 62.099 60.798 1.00 33.11 ? 475 TYR A CE2 1 ATOM 3405 C CZ . TYR A 1 482 ? 27.751 61.431 59.637 1.00 32.28 ? 475 TYR A CZ 1 ATOM 3406 O OH . TYR A 1 482 ? 27.740 62.183 58.473 1.00 34.50 ? 475 TYR A OH 1 ATOM 3407 N N . ASN A 1 483 ? 26.112 57.947 65.610 1.00 28.16 ? 476 ASN A N 1 ATOM 3408 C CA . ASN A 1 483 ? 26.030 57.619 67.054 1.00 29.63 ? 476 ASN A CA 1 ATOM 3409 C C . ASN A 1 483 ? 25.859 56.133 67.337 1.00 29.42 ? 476 ASN A C 1 ATOM 3410 O O . ASN A 1 483 ? 26.519 55.574 68.234 1.00 30.99 ? 476 ASN A O 1 ATOM 3411 C CB . ASN A 1 483 ? 24.885 58.385 67.711 1.00 30.09 ? 476 ASN A CB 1 ATOM 3412 C CG . ASN A 1 483 ? 25.183 59.865 67.865 1.00 32.50 ? 476 ASN A CG 1 ATOM 3413 O OD1 . ASN A 1 483 ? 26.241 60.359 67.431 1.00 30.75 ? 476 ASN A OD1 1 ATOM 3414 N ND2 . ASN A 1 483 ? 24.258 60.581 68.505 1.00 32.30 ? 476 ASN A ND2 1 ATOM 3415 N N . LEU A 1 484 ? 24.993 55.481 66.567 1.00 29.07 ? 477 LEU A N 1 ATOM 3416 C CA . LEU A 1 484 ? 24.782 54.053 66.785 1.00 28.72 ? 477 LEU A CA 1 ATOM 3417 C C . LEU A 1 484 ? 26.045 53.265 66.475 1.00 28.02 ? 477 LEU A C 1 ATOM 3418 O O . LEU A 1 484 ? 26.412 52.396 67.237 1.00 27.41 ? 477 LEU A O 1 ATOM 3419 C CB . LEU A 1 484 ? 23.600 53.539 65.923 1.00 27.91 ? 477 LEU A CB 1 ATOM 3420 C CG . LEU A 1 484 ? 23.337 52.035 65.961 1.00 27.38 ? 477 LEU A CG 1 ATOM 3421 C CD1 . LEU A 1 484 ? 23.043 51.522 67.370 1.00 29.12 ? 477 LEU A CD1 1 ATOM 3422 C CD2 . LEU A 1 484 ? 22.181 51.690 65.013 1.00 26.31 ? 477 LEU A CD2 1 ATOM 3423 N N . THR A 1 485 ? 26.695 53.539 65.340 1.00 28.37 ? 478 THR A N 1 ATOM 3424 C CA . THR A 1 485 ? 27.904 52.767 64.964 1.00 28.67 ? 478 THR A CA 1 ATOM 3425 C C . THR A 1 485 ? 29.047 52.970 65.952 1.00 31.50 ? 478 THR A C 1 ATOM 3426 O O . THR A 1 485 ? 29.913 52.076 66.127 1.00 30.57 ? 478 THR A O 1 ATOM 3427 C CB . THR A 1 485 ? 28.338 53.003 63.495 1.00 28.55 ? 478 THR A CB 1 ATOM 3428 O OG1 . THR A 1 485 ? 28.679 54.380 63.294 1.00 27.07 ? 478 THR A OG1 1 ATOM 3429 C CG2 . THR A 1 485 ? 27.186 52.581 62.521 1.00 24.99 ? 478 THR A CG2 1 ATOM 3430 N N . LYS A 1 486 ? 29.021 54.092 66.680 1.00 33.03 ? 479 LYS A N 1 ATOM 3431 C CA . LYS A 1 486 ? 30.037 54.300 67.728 1.00 34.80 ? 479 LYS A CA 1 ATOM 3432 C C . LYS A 1 486 ? 29.830 53.383 68.933 1.00 36.00 ? 479 LYS A C 1 ATOM 3433 O O . LYS A 1 486 ? 30.770 53.123 69.681 1.00 36.94 ? 479 LYS A O 1 ATOM 3434 C CB . LYS A 1 486 ? 30.082 55.774 68.189 1.00 36.03 ? 479 LYS A CB 1 ATOM 3435 C CG . LYS A 1 486 ? 30.741 56.692 67.186 1.00 37.22 ? 479 LYS A CG 1 ATOM 3436 C CD . LYS A 1 486 ? 30.702 58.165 67.629 1.00 41.01 ? 479 LYS A CD 1 ATOM 3437 C CE . LYS A 1 486 ? 31.193 59.014 66.473 1.00 39.54 ? 479 LYS A CE 1 ATOM 3438 N NZ . LYS A 1 486 ? 30.957 60.463 66.673 1.00 42.05 ? 479 LYS A NZ 1 ATOM 3439 N N . GLU A 1 487 ? 28.611 52.881 69.101 1.00 35.94 ? 480 GLU A N 1 ATOM 3440 C CA . GLU A 1 487 ? 28.259 52.016 70.228 1.00 38.16 ? 480 GLU A CA 1 ATOM 3441 C C . GLU A 1 487 ? 28.273 50.537 69.883 1.00 37.46 ? 480 GLU A C 1 ATOM 3442 O O . GLU A 1 487 ? 28.065 49.723 70.774 1.00 39.47 ? 480 GLU A O 1 ATOM 3443 C CB . GLU A 1 487 ? 26.872 52.342 70.786 1.00 38.80 ? 480 GLU A CB 1 ATOM 3444 C CG . GLU A 1 487 ? 26.701 53.784 71.262 1.00 43.71 ? 480 GLU A CG 1 ATOM 3445 C CD . GLU A 1 487 ? 27.680 54.182 72.355 1.00 52.65 ? 480 GLU A CD 1 ATOM 3446 O OE1 . GLU A 1 487 ? 28.161 55.343 72.324 1.00 57.26 ? 480 GLU A OE1 1 ATOM 3447 O OE2 . GLU A 1 487 ? 27.982 53.342 73.238 1.00 56.01 ? 480 GLU A OE2 1 ATOM 3448 N N . LEU A 1 488 ? 28.519 50.204 68.616 1.00 35.14 ? 481 LEU A N 1 ATOM 3449 C CA . LEU A 1 488 ? 28.615 48.811 68.156 1.00 34.08 ? 481 LEU A CA 1 ATOM 3450 C C . LEU A 1 488 ? 30.067 48.347 67.964 1.00 34.83 ? 481 LEU A C 1 ATOM 3451 O O . LEU A 1 488 ? 30.934 49.129 67.575 1.00 35.03 ? 481 LEU A O 1 ATOM 3452 C CB . LEU A 1 488 ? 27.824 48.614 66.835 1.00 31.70 ? 481 LEU A CB 1 ATOM 3453 C CG . LEU A 1 488 ? 26.341 48.992 66.809 1.00 31.16 ? 481 LEU A CG 1 ATOM 3454 C CD1 . LEU A 1 488 ? 25.773 48.845 65.392 1.00 25.74 ? 481 LEU A CD1 1 ATOM 3455 C CD2 . LEU A 1 488 ? 25.545 48.120 67.821 1.00 31.86 ? 481 LEU A CD2 1 ATOM 3456 N N . LYS A 1 489 ? 30.317 47.073 68.217 1.00 35.30 ? 482 LYS A N 1 ATOM 3457 C CA . LYS A 1 489 ? 31.679 46.516 68.061 1.00 37.59 ? 482 LYS A CA 1 ATOM 3458 C C . LYS A 1 489 ? 31.948 46.252 66.587 1.00 36.62 ? 482 LYS A C 1 ATOM 3459 O O . LYS A 1 489 ? 31.044 45.814 65.871 1.00 37.01 ? 482 LYS A O 1 ATOM 3460 C CB . LYS A 1 489 ? 31.830 45.196 68.816 1.00 38.06 ? 482 LYS A CB 1 ATOM 3461 C CG . LYS A 1 489 ? 31.338 45.190 70.261 1.00 42.88 ? 482 LYS A CG 1 ATOM 3462 C CD . LYS A 1 489 ? 31.848 43.912 70.924 1.00 51.17 ? 482 LYS A CD 1 ATOM 3463 C CE . LYS A 1 489 ? 30.812 43.251 71.837 1.00 57.36 ? 482 LYS A CE 1 ATOM 3464 N NZ . LYS A 1 489 ? 30.517 44.027 73.090 1.00 60.39 ? 482 LYS A NZ 1 ATOM 3465 N N . SER A 1 490 ? 33.161 46.533 66.123 1.00 36.18 ? 483 SER A N 1 ATOM 3466 C CA . SER A 1 490 ? 33.509 46.180 64.754 1.00 35.64 ? 483 SER A CA 1 ATOM 3467 C C . SER A 1 490 ? 33.729 44.667 64.625 1.00 35.74 ? 483 SER A C 1 ATOM 3468 O O . SER A 1 490 ? 34.413 44.085 65.461 1.00 36.94 ? 483 SER A O 1 ATOM 3469 C CB . SER A 1 490 ? 34.771 46.907 64.291 1.00 36.55 ? 483 SER A CB 1 ATOM 3470 O OG . SER A 1 490 ? 35.177 46.432 63.003 1.00 36.16 ? 483 SER A OG 1 ATOM 3471 N N . PRO A 1 491 ? 33.176 44.029 63.565 1.00 34.72 ? 484 PRO A N 1 ATOM 3472 C CA . PRO A 1 491 ? 33.419 42.605 63.373 1.00 35.00 ? 484 PRO A CA 1 ATOM 3473 C C . PRO A 1 491 ? 34.684 42.350 62.531 1.00 36.30 ? 484 PRO A C 1 ATOM 3474 O O . PRO A 1 491 ? 35.010 41.190 62.265 1.00 36.09 ? 484 PRO A O 1 ATOM 3475 C CB . PRO A 1 491 ? 32.175 42.143 62.622 1.00 33.41 ? 484 PRO A CB 1 ATOM 3476 C CG . PRO A 1 491 ? 31.822 43.355 61.742 1.00 32.39 ? 484 PRO A CG 1 ATOM 3477 C CD . PRO A 1 491 ? 32.170 44.554 62.617 1.00 33.89 ? 484 PRO A CD 1 ATOM 3478 N N . ASP A 1 492 ? 35.401 43.423 62.163 1.00 36.84 ? 485 ASP A N 1 ATOM 3479 C CA . ASP A 1 492 ? 36.504 43.368 61.194 1.00 37.38 ? 485 ASP A CA 1 ATOM 3480 C C . ASP A 1 492 ? 37.807 42.860 61.822 1.00 39.24 ? 485 ASP A C 1 ATOM 3481 O O . ASP A 1 492 ? 38.170 43.237 62.946 1.00 39.95 ? 485 ASP A O 1 ATOM 3482 C CB . ASP A 1 492 ? 36.799 44.751 60.604 1.00 37.22 ? 485 ASP A CB 1 ATOM 3483 C CG . ASP A 1 492 ? 35.648 45.324 59.814 1.00 35.27 ? 485 ASP A CG 1 ATOM 3484 O OD1 . ASP A 1 492 ? 34.532 44.748 59.807 1.00 36.51 ? 485 ASP A OD1 1 ATOM 3485 O OD2 . ASP A 1 492 ? 35.864 46.377 59.183 1.00 34.87 ? 485 ASP A OD2 1 ATOM 3486 N N . GLU A 1 493 ? 38.512 42.027 61.069 1.00 40.30 ? 486 GLU A N 1 ATOM 3487 C CA . GLU A 1 493 ? 39.833 41.531 61.473 1.00 42.53 ? 486 GLU A CA 1 ATOM 3488 C C . GLU A 1 493 ? 40.785 42.735 61.650 1.00 42.53 ? 486 GLU A C 1 ATOM 3489 O O . GLU A 1 493 ? 40.818 43.623 60.804 1.00 41.84 ? 486 GLU A O 1 ATOM 3490 C CB . GLU A 1 493 ? 40.352 40.555 60.410 1.00 43.28 ? 486 GLU A CB 1 ATOM 3491 C CG . GLU A 1 493 ? 39.624 39.171 60.376 1.00 47.34 ? 486 GLU A CG 1 ATOM 3492 C CD . GLU A 1 493 ? 38.330 39.162 59.538 1.00 50.56 ? 486 GLU A CD 1 ATOM 3493 O OE1 . GLU A 1 493 ? 37.886 40.240 59.046 1.00 52.95 ? 486 GLU A OE1 1 ATOM 3494 O OE2 . GLU A 1 493 ? 37.727 38.069 59.381 1.00 50.37 ? 486 GLU A OE2 1 ATOM 3495 N N . GLY A 1 494 ? 41.550 42.780 62.740 1.00 44.17 ? 487 GLY A N 1 ATOM 3496 C CA . GLY A 1 494 ? 42.409 43.950 63.005 1.00 43.96 ? 487 GLY A CA 1 ATOM 3497 C C . GLY A 1 494 ? 41.722 45.088 63.764 1.00 44.28 ? 487 GLY A C 1 ATOM 3498 O O . GLY A 1 494 ? 42.389 46.025 64.204 1.00 45.65 ? 487 GLY A O 1 ATOM 3499 N N . PHE A 1 495 ? 40.396 45.035 63.915 1.00 41.84 ? 488 PHE A N 1 ATOM 3500 C CA . PHE A 1 495 ? 39.692 46.053 64.700 1.00 41.94 ? 488 PHE A CA 1 ATOM 3501 C C . PHE A 1 495 ? 38.973 45.460 65.915 1.00 42.57 ? 488 PHE A C 1 ATOM 3502 O O . PHE A 1 495 ? 37.964 46.005 66.358 1.00 40.83 ? 488 PHE A O 1 ATOM 3503 C CB . PHE A 1 495 ? 38.676 46.795 63.821 1.00 39.76 ? 488 PHE A CB 1 ATOM 3504 C CG . PHE A 1 495 ? 39.293 47.561 62.698 1.00 39.73 ? 488 PHE A CG 1 ATOM 3505 C CD1 . PHE A 1 495 ? 39.575 48.917 62.844 1.00 41.49 ? 488 PHE A CD1 1 ATOM 3506 C CD2 . PHE A 1 495 ? 39.600 46.928 61.488 1.00 40.60 ? 488 PHE A CD2 1 ATOM 3507 C CE1 . PHE A 1 495 ? 40.144 49.649 61.801 1.00 43.36 ? 488 PHE A CE1 1 ATOM 3508 C CE2 . PHE A 1 495 ? 40.178 47.645 60.432 1.00 41.54 ? 488 PHE A CE2 1 ATOM 3509 C CZ . PHE A 1 495 ? 40.446 49.013 60.590 1.00 43.92 ? 488 PHE A CZ 1 ATOM 3510 N N . GLU A 1 496 ? 39.451 44.330 66.432 1.00 43.59 ? 489 GLU A N 1 ATOM 3511 C CA . GLU A 1 496 ? 38.802 43.732 67.604 1.00 45.30 ? 489 GLU A CA 1 ATOM 3512 C C . GLU A 1 496 ? 38.976 44.696 68.781 1.00 46.22 ? 489 GLU A C 1 ATOM 3513 O O . GLU A 1 496 ? 40.063 45.224 68.990 1.00 47.19 ? 489 GLU A O 1 ATOM 3514 C CB . GLU A 1 496 ? 39.355 42.329 67.946 1.00 46.73 ? 489 GLU A CB 1 ATOM 3515 C CG . GLU A 1 496 ? 40.764 42.052 67.497 1.00 50.55 ? 489 GLU A CG 1 ATOM 3516 C CD . GLU A 1 496 ? 40.908 41.810 65.999 1.00 51.08 ? 489 GLU A CD 1 ATOM 3517 O OE1 . GLU A 1 496 ? 40.326 40.846 65.450 1.00 49.41 ? 489 GLU A OE1 1 ATOM 3518 O OE2 . GLU A 1 496 ? 41.653 42.594 65.376 1.00 53.43 ? 489 GLU A OE2 1 ATOM 3519 N N . GLY A 1 497 ? 37.900 44.955 69.511 1.00 45.29 ? 490 GLY A N 1 ATOM 3520 C CA . GLY A 1 497 ? 37.950 45.956 70.575 1.00 46.35 ? 490 GLY A CA 1 ATOM 3521 C C . GLY A 1 497 ? 37.681 47.376 70.090 1.00 44.99 ? 490 GLY A C 1 ATOM 3522 O O . GLY A 1 497 ? 37.630 48.309 70.894 1.00 46.70 ? 490 GLY A O 1 ATOM 3523 N N . LYS A 1 498 ? 37.501 47.553 68.786 1.00 42.57 ? 491 LYS A N 1 ATOM 3524 C CA . LYS A 1 498 ? 37.198 48.874 68.254 1.00 40.80 ? 491 LYS A CA 1 ATOM 3525 C C . LYS A 1 498 ? 35.751 48.940 67.843 1.00 38.32 ? 491 LYS A C 1 ATOM 3526 O O . LYS A 1 498 ? 35.100 47.912 67.669 1.00 37.26 ? 491 LYS A O 1 ATOM 3527 C CB . LYS A 1 498 ? 38.104 49.262 67.080 1.00 41.00 ? 491 LYS A CB 1 ATOM 3528 C CG . LYS A 1 498 ? 39.605 49.095 67.403 1.00 44.07 ? 491 LYS A CG 1 ATOM 3529 C CD . LYS A 1 498 ? 39.988 49.866 68.661 1.00 48.59 ? 491 LYS A CD 1 ATOM 3530 C CE . LYS A 1 498 ? 41.504 49.787 68.913 1.00 55.54 ? 491 LYS A CE 1 ATOM 3531 N NZ . LYS A 1 498 ? 42.173 50.373 67.708 1.00 58.47 ? 491 LYS A NZ 1 ATOM 3532 N N . SER A 1 499 ? 35.258 50.161 67.734 1.00 36.98 ? 492 SER A N 1 ATOM 3533 C CA . SER A 1 499 ? 33.860 50.381 67.313 1.00 35.54 ? 492 SER A CA 1 ATOM 3534 C C . SER A 1 499 ? 33.704 50.181 65.813 1.00 34.94 ? 492 SER A C 1 ATOM 3535 O O . SER A 1 499 ? 34.656 50.326 65.044 1.00 36.06 ? 492 SER A O 1 ATOM 3536 C CB . SER A 1 499 ? 33.433 51.793 67.698 1.00 35.20 ? 492 SER A CB 1 ATOM 3537 O OG . SER A 1 499 ? 33.989 52.713 66.788 1.00 35.24 ? 492 SER A OG 1 ATOM 3538 N N . LEU A 1 500 ? 32.473 49.885 65.399 1.00 33.74 ? 493 LEU A N 1 ATOM 3539 C CA . LEU A 1 500 ? 32.120 49.795 63.981 1.00 32.21 ? 493 LEU A CA 1 ATOM 3540 C C . LEU A 1 500 ? 32.368 51.162 63.327 1.00 32.10 ? 493 LEU A C 1 ATOM 3541 O O . LEU A 1 500 ? 32.839 51.223 62.178 1.00 30.43 ? 493 LEU A O 1 ATOM 3542 C CB . LEU A 1 500 ? 30.647 49.373 63.845 1.00 31.22 ? 493 LEU A CB 1 ATOM 3543 C CG . LEU A 1 500 ? 30.043 49.218 62.455 1.00 30.29 ? 493 LEU A CG 1 ATOM 3544 C CD1 . LEU A 1 500 ? 30.896 48.170 61.642 1.00 28.28 ? 493 LEU A CD1 1 ATOM 3545 C CD2 . LEU A 1 500 ? 28.563 48.809 62.539 1.00 27.34 ? 493 LEU A CD2 1 ATOM 3546 N N . TYR A 1 501 ? 32.091 52.250 64.068 1.00 31.99 ? 494 TYR A N 1 ATOM 3547 C CA . TYR A 1 501 ? 32.358 53.607 63.570 1.00 32.98 ? 494 TYR A CA 1 ATOM 3548 C C . TYR A 1 501 ? 33.830 53.739 63.170 1.00 33.41 ? 494 TYR A C 1 ATOM 3549 O O . TYR A 1 501 ? 34.133 54.294 62.115 1.00 33.03 ? 494 TYR A O 1 ATOM 3550 C CB . TYR A 1 501 ? 31.999 54.715 64.592 1.00 33.05 ? 494 TYR A CB 1 ATOM 3551 C CG . TYR A 1 501 ? 32.190 56.129 64.055 1.00 34.69 ? 494 TYR A CG 1 ATOM 3552 C CD1 . TYR A 1 501 ? 31.165 56.762 63.346 1.00 34.46 ? 494 TYR A CD1 1 ATOM 3553 C CD2 . TYR A 1 501 ? 33.415 56.828 64.249 1.00 37.89 ? 494 TYR A CD2 1 ATOM 3554 C CE1 . TYR A 1 501 ? 31.329 58.065 62.835 1.00 36.98 ? 494 TYR A CE1 1 ATOM 3555 C CE2 . TYR A 1 501 ? 33.591 58.130 63.749 1.00 37.75 ? 494 TYR A CE2 1 ATOM 3556 C CZ . TYR A 1 501 ? 32.532 58.742 63.051 1.00 37.18 ? 494 TYR A CZ 1 ATOM 3557 O OH . TYR A 1 501 ? 32.678 60.016 62.547 1.00 37.51 ? 494 TYR A OH 1 ATOM 3558 N N . GLU A 1 502 ? 34.740 53.280 64.028 1.00 34.98 ? 495 GLU A N 1 ATOM 3559 C CA . GLU A 1 502 ? 36.155 53.404 63.714 1.00 37.20 ? 495 GLU A CA 1 ATOM 3560 C C . GLU A 1 502 ? 36.565 52.634 62.439 1.00 36.56 ? 495 GLU A C 1 ATOM 3561 O O . GLU A 1 502 ? 37.244 53.181 61.560 1.00 36.56 ? 495 GLU A O 1 ATOM 3562 C CB . GLU A 1 502 ? 37.030 52.980 64.907 1.00 38.99 ? 495 GLU A CB 1 ATOM 3563 C CG . GLU A 1 502 ? 38.495 53.031 64.585 1.00 44.11 ? 495 GLU A CG 1 ATOM 3564 C CD . GLU A 1 502 ? 39.357 52.926 65.816 1.00 49.54 ? 495 GLU A CD 1 ATOM 3565 O OE1 . GLU A 1 502 ? 38.916 53.366 66.908 1.00 51.47 ? 495 GLU A OE1 1 ATOM 3566 O OE2 . GLU A 1 502 ? 40.469 52.387 65.689 1.00 53.74 ? 495 GLU A OE2 1 ATOM 3567 N N . SER A 1 503 ? 36.104 51.394 62.303 1.00 35.64 ? 496 SER A N 1 ATOM 3568 C CA . SER A 1 503 ? 36.570 50.583 61.176 1.00 35.55 ? 496 SER A CA 1 ATOM 3569 C C . SER A 1 503 ? 35.926 51.053 59.874 1.00 34.74 ? 496 SER A C 1 ATOM 3570 O O . SER A 1 503 ? 36.600 51.125 58.839 1.00 34.56 ? 496 SER A O 1 ATOM 3571 C CB . SER A 1 503 ? 36.366 49.077 61.419 1.00 35.55 ? 496 SER A CB 1 ATOM 3572 O OG . SER A 1 503 ? 35.000 48.724 61.518 1.00 31.75 ? 496 SER A OG 1 ATOM 3573 N N . TRP A 1 504 ? 34.648 51.420 59.950 1.00 33.22 ? 497 TRP A N 1 ATOM 3574 C CA . TRP A 1 504 ? 33.926 51.970 58.815 1.00 32.60 ? 497 TRP A CA 1 ATOM 3575 C C . TRP A 1 504 ? 34.551 53.293 58.362 1.00 33.50 ? 497 TRP A C 1 ATOM 3576 O O . TRP A 1 504 ? 34.741 53.516 57.155 1.00 33.33 ? 497 TRP A O 1 ATOM 3577 C CB . TRP A 1 504 ? 32.422 52.103 59.147 1.00 31.68 ? 497 TRP A CB 1 ATOM 3578 C CG . TRP A 1 504 ? 31.529 52.777 58.118 1.00 30.36 ? 497 TRP A CG 1 ATOM 3579 C CD1 . TRP A 1 504 ? 31.610 52.698 56.756 1.00 27.31 ? 497 TRP A CD1 1 ATOM 3580 C CD2 . TRP A 1 504 ? 30.379 53.593 58.406 1.00 30.30 ? 497 TRP A CD2 1 ATOM 3581 N NE1 . TRP A 1 504 ? 30.588 53.441 56.183 1.00 27.24 ? 497 TRP A NE1 1 ATOM 3582 C CE2 . TRP A 1 504 ? 29.827 54.001 57.173 1.00 29.80 ? 497 TRP A CE2 1 ATOM 3583 C CE3 . TRP A 1 504 ? 29.785 54.046 59.600 1.00 31.15 ? 497 TRP A CE3 1 ATOM 3584 C CZ2 . TRP A 1 504 ? 28.712 54.849 57.087 1.00 27.73 ? 497 TRP A CZ2 1 ATOM 3585 C CZ3 . TRP A 1 504 ? 28.657 54.861 59.518 1.00 27.45 ? 497 TRP A CZ3 1 ATOM 3586 C CH2 . TRP A 1 504 ? 28.126 55.255 58.260 1.00 28.68 ? 497 TRP A CH2 1 ATOM 3587 N N . THR A 1 505 ? 34.892 54.161 59.318 1.00 33.58 ? 498 THR A N 1 ATOM 3588 C CA . THR A 1 505 ? 35.434 55.469 58.956 1.00 34.42 ? 498 THR A CA 1 ATOM 3589 C C . THR A 1 505 ? 36.830 55.307 58.321 1.00 36.77 ? 498 THR A C 1 ATOM 3590 O O . THR A 1 505 ? 37.129 55.915 57.287 1.00 36.80 ? 498 THR A O 1 ATOM 3591 C CB . THR A 1 505 ? 35.417 56.454 60.167 1.00 35.07 ? 498 THR A CB 1 ATOM 3592 O OG1 A THR A 1 505 ? 34.060 56.739 60.512 0.50 29.40 ? 498 THR A OG1 1 ATOM 3593 C CG2 A THR A 1 505 ? 36.164 57.763 59.839 0.50 35.09 ? 498 THR A CG2 1 ATOM 3594 N N . LYS A 1 506 ? 37.640 54.422 58.891 1.00 38.22 ? 499 LYS A N 1 ATOM 3595 C CA . LYS A 1 506 ? 38.936 54.098 58.323 1.00 40.11 ? 499 LYS A CA 1 ATOM 3596 C C . LYS A 1 506 ? 38.859 53.489 56.899 1.00 39.50 ? 499 LYS A C 1 ATOM 3597 O O . LYS A 1 506 ? 39.620 53.884 56.011 1.00 39.88 ? 499 LYS A O 1 ATOM 3598 C CB . LYS A 1 506 ? 39.688 53.180 59.286 1.00 41.84 ? 499 LYS A CB 1 ATOM 3599 C CG . LYS A 1 506 ? 41.046 52.725 58.790 1.00 46.14 ? 499 LYS A CG 1 ATOM 3600 C CD . LYS A 1 506 ? 42.074 53.838 58.918 1.00 53.58 ? 499 LYS A CD 1 ATOM 3601 C CE . LYS A 1 506 ? 43.463 53.369 58.462 1.00 55.52 ? 499 LYS A CE 1 ATOM 3602 N NZ . LYS A 1 506 ? 44.350 54.551 58.508 1.00 59.44 ? 499 LYS A NZ 1 ATOM 3603 N N . LYS A 1 507 ? 37.932 52.557 56.671 1.00 38.28 ? 500 LYS A N 1 ATOM 3604 C CA . LYS A 1 507 ? 37.849 51.861 55.379 1.00 37.57 ? 500 LYS A CA 1 ATOM 3605 C C . LYS A 1 507 ? 37.059 52.598 54.296 1.00 36.85 ? 500 LYS A C 1 ATOM 3606 O O . LYS A 1 507 ? 37.217 52.311 53.116 1.00 36.49 ? 500 LYS A O 1 ATOM 3607 C CB . LYS A 1 507 ? 37.254 50.473 55.564 1.00 36.88 ? 500 LYS A CB 1 ATOM 3608 C CG . LYS A 1 507 ? 38.201 49.481 56.300 1.00 38.21 ? 500 LYS A CG 1 ATOM 3609 C CD . LYS A 1 507 ? 37.555 48.079 56.308 1.00 37.27 ? 500 LYS A CD 1 ATOM 3610 C CE . LYS A 1 507 ? 38.369 47.078 57.110 1.00 38.04 ? 500 LYS A CE 1 ATOM 3611 N NZ . LYS A 1 507 ? 37.668 45.749 57.089 1.00 38.15 ? 500 LYS A NZ 1 ATOM 3612 N N . SER A 1 508 ? 36.194 53.518 54.698 1.00 35.40 ? 501 SER A N 1 ATOM 3613 C CA . SER A 1 508 ? 35.314 54.199 53.756 1.00 35.84 ? 501 SER A CA 1 ATOM 3614 C C . SER A 1 508 ? 35.233 55.686 54.138 1.00 37.38 ? 501 SER A C 1 ATOM 3615 O O . SER A 1 508 ? 34.178 56.161 54.571 1.00 35.51 ? 501 SER A O 1 ATOM 3616 C CB . SER A 1 508 ? 33.940 53.545 53.846 1.00 34.59 ? 501 SER A CB 1 ATOM 3617 O OG . SER A 1 508 ? 33.118 53.983 52.811 1.00 36.17 ? 501 SER A OG 1 ATOM 3618 N N . PRO A 1 509 ? 36.370 56.424 54.020 1.00 39.12 ? 502 PRO A N 1 ATOM 3619 C CA . PRO A 1 509 ? 36.365 57.821 54.466 1.00 40.67 ? 502 PRO A CA 1 ATOM 3620 C C . PRO A 1 509 ? 35.441 58.678 53.601 1.00 41.17 ? 502 PRO A C 1 ATOM 3621 O O . PRO A 1 509 ? 35.354 58.473 52.374 1.00 40.53 ? 502 PRO A O 1 ATOM 3622 C CB . PRO A 1 509 ? 37.842 58.252 54.299 1.00 41.77 ? 502 PRO A CB 1 ATOM 3623 C CG . PRO A 1 509 ? 38.395 57.327 53.257 1.00 41.52 ? 502 PRO A CG 1 ATOM 3624 C CD . PRO A 1 509 ? 37.689 56.016 53.488 1.00 39.48 ? 502 PRO A CD 1 ATOM 3625 N N . SER A 1 510 ? 34.746 59.615 54.232 1.00 42.81 ? 503 SER A N 1 ATOM 3626 C CA . SER A 1 510 ? 33.909 60.565 53.487 1.00 45.03 ? 503 SER A CA 1 ATOM 3627 C C . SER A 1 510 ? 34.789 61.440 52.624 1.00 47.71 ? 503 SER A C 1 ATOM 3628 O O . SER A 1 510 ? 35.764 61.969 53.125 1.00 48.69 ? 503 SER A O 1 ATOM 3629 C CB . SER A 1 510 ? 33.152 61.486 54.427 1.00 44.87 ? 503 SER A CB 1 ATOM 3630 O OG . SER A 1 510 ? 32.516 62.503 53.651 1.00 45.51 ? 503 SER A OG 1 ATOM 3631 N N . PRO A 1 511 ? 34.452 61.599 51.335 1.00 49.48 ? 504 PRO A N 1 ATOM 3632 C CA . PRO A 1 511 ? 35.228 62.517 50.483 1.00 52.22 ? 504 PRO A CA 1 ATOM 3633 C C . PRO A 1 511 ? 34.842 63.972 50.724 1.00 54.02 ? 504 PRO A C 1 ATOM 3634 O O . PRO A 1 511 ? 35.719 64.855 50.738 1.00 55.11 ? 504 PRO A O 1 ATOM 3635 C CB . PRO A 1 511 ? 34.832 62.108 49.050 1.00 51.62 ? 504 PRO A CB 1 ATOM 3636 C CG . PRO A 1 511 ? 34.102 60.796 49.198 1.00 50.88 ? 504 PRO A CG 1 ATOM 3637 C CD . PRO A 1 511 ? 33.439 60.874 50.555 1.00 48.81 ? 504 PRO A CD 1 ATOM 3638 N N . GLU A 1 512 ? 33.541 64.210 50.915 1.00 55.19 ? 505 GLU A N 1 ATOM 3639 C CA . GLU A 1 512 ? 33.009 65.563 51.168 1.00 57.66 ? 505 GLU A CA 1 ATOM 3640 C C . GLU A 1 512 ? 33.292 66.099 52.575 1.00 58.60 ? 505 GLU A C 1 ATOM 3641 O O . GLU A 1 512 ? 33.541 67.296 52.750 1.00 59.92 ? 505 GLU A O 1 ATOM 3642 C CB . GLU A 1 512 ? 31.500 65.629 50.872 1.00 56.37 ? 505 GLU A CB 1 ATOM 3643 C CG . GLU A 1 512 ? 31.134 65.486 49.372 1.00 59.84 ? 505 GLU A CG 1 ATOM 3644 C CD . GLU A 1 512 ? 31.708 66.611 48.458 1.00 64.86 ? 505 GLU A CD 1 ATOM 3645 O OE1 . GLU A 1 512 ? 32.157 67.684 48.962 1.00 66.33 ? 505 GLU A OE1 1 ATOM 3646 O OE2 . GLU A 1 512 ? 31.709 66.409 47.215 1.00 65.46 ? 505 GLU A OE2 1 ATOM 3647 N N . PHE A 1 513 ? 33.257 65.214 53.569 1.00 59.06 ? 506 PHE A N 1 ATOM 3648 C CA . PHE A 1 513 ? 33.395 65.615 54.970 1.00 59.65 ? 506 PHE A CA 1 ATOM 3649 C C . PHE A 1 513 ? 34.555 64.881 55.588 1.00 60.29 ? 506 PHE A C 1 ATOM 3650 O O . PHE A 1 513 ? 34.435 63.725 55.996 1.00 60.11 ? 506 PHE A O 1 ATOM 3651 C CB . PHE A 1 513 ? 32.103 65.336 55.748 1.00 59.11 ? 506 PHE A CB 1 ATOM 3652 C CG . PHE A 1 513 ? 30.866 65.865 55.068 1.00 59.39 ? 506 PHE A CG 1 ATOM 3653 C CD1 . PHE A 1 513 ? 30.586 67.230 55.074 1.00 59.75 ? 506 PHE A CD1 1 ATOM 3654 C CD2 . PHE A 1 513 ? 29.997 65.000 54.399 1.00 60.12 ? 506 PHE A CD2 1 ATOM 3655 C CE1 . PHE A 1 513 ? 29.453 67.728 54.434 1.00 60.22 ? 506 PHE A CE1 1 ATOM 3656 C CE2 . PHE A 1 513 ? 28.839 65.486 53.759 1.00 60.16 ? 506 PHE A CE2 1 ATOM 3657 C CZ . PHE A 1 513 ? 28.567 66.857 53.773 1.00 60.35 ? 506 PHE A CZ 1 ATOM 3658 N N . SER A 1 514 ? 35.688 65.561 55.644 1.00 60.76 ? 507 SER A N 1 ATOM 3659 C CA . SER A 1 514 ? 36.901 64.970 56.187 1.00 61.45 ? 507 SER A CA 1 ATOM 3660 C C . SER A 1 514 ? 36.658 64.384 57.579 1.00 60.24 ? 507 SER A C 1 ATOM 3661 O O . SER A 1 514 ? 35.954 64.997 58.398 1.00 59.86 ? 507 SER A O 1 ATOM 3662 C CB . SER A 1 514 ? 38.025 66.018 56.232 1.00 63.40 ? 507 SER A CB 1 ATOM 3663 O OG . SER A 1 514 ? 38.164 66.633 54.957 1.00 64.95 ? 507 SER A OG 1 ATOM 3664 N N . GLY A 1 515 ? 37.215 63.191 57.816 1.00 58.89 ? 508 GLY A N 1 ATOM 3665 C CA . GLY A 1 515 ? 37.172 62.531 59.137 1.00 56.67 ? 508 GLY A CA 1 ATOM 3666 C C . GLY A 1 515 ? 35.917 61.711 59.462 1.00 53.68 ? 508 GLY A C 1 ATOM 3667 O O . GLY A 1 515 ? 35.893 60.994 60.459 1.00 53.20 ? 508 GLY A O 1 ATOM 3668 N N . MET A 1 516 ? 34.873 61.831 58.635 1.00 50.64 ? 509 MET A N 1 ATOM 3669 C CA . MET A 1 516 ? 33.615 61.080 58.791 1.00 47.33 ? 509 MET A CA 1 ATOM 3670 C C . MET A 1 516 ? 33.617 59.839 57.868 1.00 44.96 ? 509 MET A C 1 ATOM 3671 O O . MET A 1 516 ? 34.288 59.845 56.843 1.00 44.59 ? 509 MET A O 1 ATOM 3672 C CB . MET A 1 516 ? 32.457 61.963 58.348 1.00 46.29 ? 509 MET A CB 1 ATOM 3673 C CG . MET A 1 516 ? 32.526 63.407 58.845 1.00 48.99 ? 509 MET A CG 1 ATOM 3674 S SD . MET A 1 516 ? 32.317 63.384 60.630 1.00 51.00 ? 509 MET A SD 1 ATOM 3675 C CE . MET A 1 516 ? 30.573 62.970 60.620 1.00 49.55 ? 509 MET A CE 1 ATOM 3676 N N . PRO A 1 517 ? 32.808 58.806 58.179 1.00 42.40 ? 510 PRO A N 1 ATOM 3677 C CA . PRO A 1 517 ? 32.612 57.791 57.128 1.00 39.87 ? 510 PRO A CA 1 ATOM 3678 C C . PRO A 1 517 ? 31.717 58.281 56.010 1.00 37.69 ? 510 PRO A C 1 ATOM 3679 O O . PRO A 1 517 ? 30.863 59.162 56.220 1.00 37.18 ? 510 PRO A O 1 ATOM 3680 C CB . PRO A 1 517 ? 31.900 56.665 57.868 1.00 39.49 ? 510 PRO A CB 1 ATOM 3681 C CG . PRO A 1 517 ? 31.089 57.384 58.924 1.00 40.69 ? 510 PRO A CG 1 ATOM 3682 C CD . PRO A 1 517 ? 31.970 58.543 59.364 1.00 42.34 ? 510 PRO A CD 1 ATOM 3683 N N . ARG A 1 518 ? 31.870 57.689 54.832 1.00 34.90 ? 511 ARG A N 1 ATOM 3684 C CA . ARG A 1 518 ? 31.015 57.979 53.710 1.00 33.64 ? 511 ARG A CA 1 ATOM 3685 C C . ARG A 1 518 ? 29.570 57.472 53.914 1.00 31.86 ? 511 ARG A C 1 ATOM 3686 O O . ARG A 1 518 ? 29.352 56.304 54.249 1.00 30.33 ? 511 ARG A O 1 ATOM 3687 C CB . ARG A 1 518 ? 31.601 57.309 52.455 1.00 34.60 ? 511 ARG A CB 1 ATOM 3688 C CG . ARG A 1 518 ? 30.779 57.476 51.195 1.00 36.32 ? 511 ARG A CG 1 ATOM 3689 C CD . ARG A 1 518 ? 31.257 56.465 50.152 1.00 42.80 ? 511 ARG A CD 1 ATOM 3690 N NE . ARG A 1 518 ? 32.599 56.808 49.691 1.00 47.13 ? 511 ARG A NE 1 ATOM 3691 C CZ . ARG A 1 518 ? 32.851 57.613 48.650 1.00 50.77 ? 511 ARG A CZ 1 ATOM 3692 N NH1 . ARG A 1 518 ? 31.849 58.158 47.959 1.00 46.37 ? 511 ARG A NH1 1 ATOM 3693 N NH2 . ARG A 1 518 ? 34.105 57.875 48.295 1.00 48.85 ? 511 ARG A NH2 1 ATOM 3694 N N . ILE A 1 519 ? 28.607 58.356 53.697 1.00 29.87 ? 512 ILE A N 1 ATOM 3695 C CA . ILE A 1 519 ? 27.194 57.960 53.546 1.00 28.96 ? 512 ILE A CA 1 ATOM 3696 C C . ILE A 1 519 ? 26.687 58.434 52.191 1.00 29.66 ? 512 ILE A C 1 ATOM 3697 O O . ILE A 1 519 ? 26.824 59.612 51.839 1.00 30.60 ? 512 ILE A O 1 ATOM 3698 C CB . ILE A 1 519 ? 26.265 58.548 54.670 1.00 28.89 ? 512 ILE A CB 1 ATOM 3699 C CG1 . ILE A 1 519 ? 26.639 57.975 56.039 1.00 27.78 ? 512 ILE A CG1 1 ATOM 3700 C CG2 . ILE A 1 519 ? 24.755 58.199 54.345 1.00 25.46 ? 512 ILE A CG2 1 ATOM 3701 C CD1 . ILE A 1 519 ? 25.833 58.568 57.235 1.00 27.47 ? 512 ILE A CD1 1 ATOM 3702 N N . SER A 1 520 ? 26.107 57.525 51.421 1.00 29.45 ? 513 SER A N 1 ATOM 3703 C CA . SER A 1 520 ? 25.680 57.850 50.073 1.00 29.14 ? 513 SER A CA 1 ATOM 3704 C C . SER A 1 520 ? 24.240 58.312 50.049 1.00 29.02 ? 513 SER A C 1 ATOM 3705 O O . SER A 1 520 ? 23.491 58.091 51.000 1.00 26.98 ? 513 SER A O 1 ATOM 3706 C CB . SER A 1 520 ? 25.842 56.640 49.146 1.00 29.13 ? 513 SER A CB 1 ATOM 3707 O OG . SER A 1 520 ? 27.226 56.412 48.939 1.00 31.36 ? 513 SER A OG 1 ATOM 3708 N N . LYS A 1 521 ? 23.877 58.907 48.923 1.00 29.22 ? 514 LYS A N 1 ATOM 3709 C CA . LYS A 1 521 ? 22.511 59.296 48.614 1.00 29.72 ? 514 LYS A CA 1 ATOM 3710 C C . LYS A 1 521 ? 21.704 58.025 48.400 1.00 30.48 ? 514 LYS A C 1 ATOM 3711 O O . LYS A 1 521 ? 22.251 57.000 47.969 1.00 30.65 ? 514 LYS A O 1 ATOM 3712 C CB . LYS A 1 521 ? 22.508 60.127 47.314 1.00 28.61 ? 514 LYS A CB 1 ATOM 3713 C CG . LYS A 1 521 ? 23.218 61.481 47.473 1.00 29.68 ? 514 LYS A CG 1 ATOM 3714 C CD . LYS A 1 521 ? 22.942 62.420 46.253 1.00 31.22 ? 514 LYS A CD 1 ATOM 3715 C CE . LYS A 1 521 ? 23.747 62.000 45.064 1.00 30.42 ? 514 LYS A CE 1 ATOM 3716 N NZ . LYS A 1 521 ? 25.155 62.372 45.364 1.00 32.18 ? 514 LYS A NZ 1 ATOM 3717 N N . LEU A 1 522 ? 20.404 58.097 48.659 1.00 28.30 ? 515 LEU A N 1 ATOM 3718 C CA . LEU A 1 522 ? 19.501 57.027 48.249 1.00 28.79 ? 515 LEU A CA 1 ATOM 3719 C C . LEU A 1 522 ? 19.216 57.218 46.805 1.00 30.15 ? 515 LEU A C 1 ATOM 3720 O O . LEU A 1 522 ? 18.867 58.324 46.383 1.00 31.73 ? 515 LEU A O 1 ATOM 3721 C CB . LEU A 1 522 ? 18.177 57.066 49.015 1.00 26.01 ? 515 LEU A CB 1 ATOM 3722 C CG . LEU A 1 522 ? 18.250 56.543 50.444 1.00 23.69 ? 515 LEU A CG 1 ATOM 3723 C CD1 . LEU A 1 522 ? 16.965 57.010 51.180 1.00 20.59 ? 515 LEU A CD1 1 ATOM 3724 C CD2 . LEU A 1 522 ? 18.410 54.999 50.469 1.00 21.09 ? 515 LEU A CD2 1 ATOM 3725 N N . GLY A 1 523 ? 19.385 56.139 46.025 1.00 31.39 ? 516 GLY A N 1 ATOM 3726 C CA . GLY A 1 523 ? 18.883 56.137 44.657 1.00 30.13 ? 516 GLY A CA 1 ATOM 3727 C C . GLY A 1 523 ? 17.599 55.369 44.637 1.00 29.56 ? 516 GLY A C 1 ATOM 3728 O O . GLY A 1 523 ? 16.708 55.670 45.399 1.00 30.01 ? 516 GLY A O 1 ATOM 3729 N N . SER A 1 524 ? 17.459 54.417 43.704 1.00 27.82 ? 517 SER A N 1 ATOM 3730 C CA . SER A 1 524 ? 16.347 53.505 43.766 1.00 24.49 ? 517 SER A CA 1 ATOM 3731 C C . SER A 1 524 ? 16.781 52.086 43.377 1.00 22.19 ? 517 SER A C 1 ATOM 3732 O O . SER A 1 524 ? 17.952 51.711 43.532 1.00 22.55 ? 517 SER A O 1 ATOM 3733 C CB . SER A 1 524 ? 15.210 54.039 42.954 1.00 23.82 ? 517 SER A CB 1 ATOM 3734 O OG . SER A 1 524 ? 14.157 53.112 42.830 1.00 28.74 ? 517 SER A OG 1 ATOM 3735 N N . GLY A 1 525 ? 15.858 51.289 42.864 1.00 18.58 ? 518 GLY A N 1 ATOM 3736 C CA . GLY A 1 525 ? 16.183 49.886 42.564 1.00 18.95 ? 518 GLY A CA 1 ATOM 3737 C C . GLY A 1 525 ? 15.997 49.010 43.810 1.00 18.57 ? 518 GLY A C 1 ATOM 3738 O O . GLY A 1 525 ? 16.551 47.905 43.871 1.00 18.90 ? 518 GLY A O 1 ATOM 3739 N N . ASN A 1 526 ? 15.259 49.512 44.809 1.00 17.85 ? 519 ASN A N 1 ATOM 3740 C CA . ASN A 1 526 ? 14.891 48.656 45.937 1.00 18.91 ? 519 ASN A CA 1 ATOM 3741 C C . ASN A 1 526 ? 13.664 49.204 46.654 1.00 17.78 ? 519 ASN A C 1 ATOM 3742 O O . ASN A 1 526 ? 13.195 50.274 46.270 1.00 16.48 ? 519 ASN A O 1 ATOM 3743 C CB . ASN A 1 526 ? 16.076 48.444 46.864 1.00 19.17 ? 519 ASN A CB 1 ATOM 3744 C CG . ASN A 1 526 ? 16.160 47.001 47.320 1.00 20.81 ? 519 ASN A CG 1 ATOM 3745 O OD1 . ASN A 1 526 ? 15.311 46.553 48.084 1.00 19.89 ? 519 ASN A OD1 1 ATOM 3746 N ND2 . ASN A 1 526 ? 17.170 46.265 46.833 1.00 19.40 ? 519 ASN A ND2 1 ATOM 3747 N N . ASP A 1 527 ? 13.199 48.523 47.716 1.00 16.01 ? 520 ASP A N 1 ATOM 3748 C CA . ASP A 1 527 ? 11.806 48.709 48.174 1.00 17.79 ? 520 ASP A CA 1 ATOM 3749 C C . ASP A 1 527 ? 11.580 50.005 48.939 1.00 17.26 ? 520 ASP A C 1 ATOM 3750 O O . ASP A 1 527 ? 10.453 50.368 49.187 1.00 17.49 ? 520 ASP A O 1 ATOM 3751 C CB . ASP A 1 527 ? 11.367 47.515 49.043 1.00 16.53 ? 520 ASP A CB 1 ATOM 3752 C CG . ASP A 1 527 ? 10.973 46.307 48.181 1.00 19.21 ? 520 ASP A CG 1 ATOM 3753 O OD1 . ASP A 1 527 ? 10.251 46.498 47.184 1.00 18.29 ? 520 ASP A OD1 1 ATOM 3754 O OD2 . ASP A 1 527 ? 11.419 45.190 48.494 1.00 19.61 ? 520 ASP A OD2 1 ATOM 3755 N N . PHE A 1 528 ? 12.639 50.743 49.252 1.00 17.30 ? 521 PHE A N 1 ATOM 3756 C CA . PHE A 1 528 ? 12.431 52.050 49.895 1.00 18.99 ? 521 PHE A CA 1 ATOM 3757 C C . PHE A 1 528 ? 11.897 53.103 48.884 1.00 18.25 ? 521 PHE A C 1 ATOM 3758 O O . PHE A 1 528 ? 11.555 54.223 49.292 1.00 17.50 ? 521 PHE A O 1 ATOM 3759 C CB . PHE A 1 528 ? 13.763 52.537 50.516 1.00 19.70 ? 521 PHE A CB 1 ATOM 3760 C CG . PHE A 1 528 ? 14.843 52.726 49.490 1.00 20.84 ? 521 PHE A CG 1 ATOM 3761 C CD1 . PHE A 1 528 ? 14.903 53.912 48.733 1.00 22.90 ? 521 PHE A CD1 1 ATOM 3762 C CD2 . PHE A 1 528 ? 15.760 51.712 49.226 1.00 19.90 ? 521 PHE A CD2 1 ATOM 3763 C CE1 . PHE A 1 528 ? 15.888 54.060 47.751 1.00 19.81 ? 521 PHE A CE1 1 ATOM 3764 C CE2 . PHE A 1 528 ? 16.751 51.870 48.222 1.00 21.10 ? 521 PHE A CE2 1 ATOM 3765 C CZ . PHE A 1 528 ? 16.783 53.041 47.483 1.00 20.33 ? 521 PHE A CZ 1 ATOM 3766 N N . GLU A 1 529 ? 11.890 52.791 47.583 1.00 16.28 ? 522 GLU A N 1 ATOM 3767 C CA . GLU A 1 529 ? 11.625 53.846 46.573 1.00 17.72 ? 522 GLU A CA 1 ATOM 3768 C C . GLU A 1 529 ? 10.268 54.540 46.802 1.00 17.58 ? 522 GLU A C 1 ATOM 3769 O O . GLU A 1 529 ? 10.199 55.782 46.821 1.00 16.96 ? 522 GLU A O 1 ATOM 3770 C CB . GLU A 1 529 ? 11.657 53.265 45.125 1.00 16.79 ? 522 GLU A CB 1 ATOM 3771 C CG . GLU A 1 529 ? 11.511 54.388 44.038 1.00 19.91 ? 522 GLU A CG 1 ATOM 3772 C CD . GLU A 1 529 ? 11.341 53.807 42.612 1.00 20.36 ? 522 GLU A CD 1 ATOM 3773 O OE1 . GLU A 1 529 ? 10.364 53.129 42.337 1.00 25.88 ? 522 GLU A OE1 1 ATOM 3774 O OE2 . GLU A 1 529 ? 12.202 54.024 41.751 1.00 25.19 ? 522 GLU A OE2 1 ATOM 3775 N N . VAL A 1 530 ? 9.200 53.765 46.978 1.00 16.43 ? 523 VAL A N 1 ATOM 3776 C CA . VAL A 1 530 ? 7.872 54.404 47.097 1.00 15.59 ? 523 VAL A CA 1 ATOM 3777 C C . VAL A 1 530 ? 7.813 55.268 48.385 1.00 17.93 ? 523 VAL A C 1 ATOM 3778 O O . VAL A 1 530 ? 7.163 56.329 48.431 1.00 17.61 ? 523 VAL A O 1 ATOM 3779 C CB . VAL A 1 530 ? 6.732 53.362 47.063 1.00 18.03 ? 523 VAL A CB 1 ATOM 3780 C CG1 . VAL A 1 530 ? 6.786 52.355 48.338 1.00 14.83 ? 523 VAL A CG1 1 ATOM 3781 C CG2 . VAL A 1 530 ? 5.377 54.089 46.964 1.00 15.76 ? 523 VAL A CG2 1 ATOM 3782 N N . PHE A 1 531 ? 8.453 54.767 49.450 1.00 17.84 ? 524 PHE A N 1 ATOM 3783 C CA . PHE A 1 531 ? 8.398 55.488 50.740 1.00 17.62 ? 524 PHE A CA 1 ATOM 3784 C C . PHE A 1 531 ? 9.146 56.800 50.689 1.00 17.87 ? 524 PHE A C 1 ATOM 3785 O O . PHE A 1 531 ? 8.699 57.807 51.265 1.00 18.44 ? 524 PHE A O 1 ATOM 3786 C CB . PHE A 1 531 ? 8.975 54.614 51.862 1.00 17.67 ? 524 PHE A CB 1 ATOM 3787 C CG . PHE A 1 531 ? 8.171 53.344 52.041 1.00 17.93 ? 524 PHE A CG 1 ATOM 3788 C CD1 . PHE A 1 531 ? 6.950 53.381 52.752 1.00 19.83 ? 524 PHE A CD1 1 ATOM 3789 C CD2 . PHE A 1 531 ? 8.558 52.160 51.407 1.00 20.38 ? 524 PHE A CD2 1 ATOM 3790 C CE1 . PHE A 1 531 ? 6.144 52.208 52.875 1.00 23.49 ? 524 PHE A CE1 1 ATOM 3791 C CE2 . PHE A 1 531 ? 7.748 50.970 51.511 1.00 16.10 ? 524 PHE A CE2 1 ATOM 3792 C CZ . PHE A 1 531 ? 6.577 50.995 52.247 1.00 21.87 ? 524 PHE A CZ 1 ATOM 3793 N N . PHE A 1 532 ? 10.306 56.779 50.063 1.00 17.08 ? 525 PHE A N 1 ATOM 3794 C CA . PHE A 1 532 ? 11.176 57.974 50.025 1.00 17.63 ? 525 PHE A CA 1 ATOM 3795 C C . PHE A 1 532 ? 10.847 58.943 48.832 1.00 17.99 ? 525 PHE A C 1 ATOM 3796 O O . PHE A 1 532 ? 10.454 60.117 49.053 1.00 17.44 ? 525 PHE A O 1 ATOM 3797 C CB . PHE A 1 532 ? 12.646 57.512 49.971 1.00 16.18 ? 525 PHE A CB 1 ATOM 3798 C CG . PHE A 1 532 ? 13.624 58.625 50.185 1.00 17.99 ? 525 PHE A CG 1 ATOM 3799 C CD1 . PHE A 1 532 ? 13.614 59.320 51.396 1.00 18.31 ? 525 PHE A CD1 1 ATOM 3800 C CD2 . PHE A 1 532 ? 14.516 59.001 49.176 1.00 19.42 ? 525 PHE A CD2 1 ATOM 3801 C CE1 . PHE A 1 532 ? 14.534 60.376 51.649 1.00 20.66 ? 525 PHE A CE1 1 ATOM 3802 C CE2 . PHE A 1 532 ? 15.477 60.054 49.422 1.00 20.80 ? 525 PHE A CE2 1 ATOM 3803 C CZ . PHE A 1 532 ? 15.447 60.750 50.674 1.00 18.32 ? 525 PHE A CZ 1 ATOM 3804 N N . GLN A 1 533 ? 10.972 58.439 47.589 1.00 17.04 ? 526 GLN A N 1 ATOM 3805 C CA . GLN A 1 533 ? 10.879 59.325 46.421 1.00 16.95 ? 526 GLN A CA 1 ATOM 3806 C C . GLN A 1 533 ? 9.398 59.708 46.130 1.00 16.75 ? 526 GLN A C 1 ATOM 3807 O O . GLN A 1 533 ? 9.140 60.789 45.581 1.00 17.77 ? 526 GLN A O 1 ATOM 3808 C CB A GLN A 1 533 ? 11.391 58.506 45.187 0.65 17.29 ? 526 GLN A CB 1 ATOM 3809 C CB B GLN A 1 533 ? 11.628 58.839 45.169 0.35 16.56 ? 526 GLN A CB 1 ATOM 3810 C CG A GLN A 1 533 ? 12.829 57.865 45.365 0.65 20.44 ? 526 GLN A CG 1 ATOM 3811 C CG B GLN A 1 533 ? 13.150 58.995 45.279 0.35 13.69 ? 526 GLN A CG 1 ATOM 3812 C CD A GLN A 1 533 ? 13.859 58.948 45.405 0.65 20.03 ? 526 GLN A CD 1 ATOM 3813 C CD B GLN A 1 533 ? 13.792 57.723 45.793 0.35 10.49 ? 526 GLN A CD 1 ATOM 3814 O OE1 A GLN A 1 533 ? 13.485 60.105 45.351 0.65 22.91 ? 526 GLN A OE1 1 ATOM 3815 O OE1 B GLN A 1 533 ? 13.097 56.871 46.362 0.35 8.56 ? 526 GLN A OE1 1 ATOM 3816 N NE2 A GLN A 1 533 ? 15.162 58.600 45.519 0.65 18.41 ? 526 GLN A NE2 1 ATOM 3817 N NE2 B GLN A 1 533 ? 15.135 57.577 45.604 0.35 5.98 ? 526 GLN A NE2 1 ATOM 3818 N N . ARG A 1 534 ? 8.444 58.807 46.416 1.00 15.67 ? 527 ARG A N 1 ATOM 3819 C CA . ARG A 1 534 ? 7.038 59.179 46.182 1.00 15.95 ? 527 ARG A CA 1 ATOM 3820 C C . ARG A 1 534 ? 6.396 59.872 47.381 1.00 16.93 ? 527 ARG A C 1 ATOM 3821 O O . ARG A 1 534 ? 5.740 60.930 47.234 1.00 16.66 ? 527 ARG A O 1 ATOM 3822 C CB . ARG A 1 534 ? 6.162 57.975 45.727 1.00 16.00 ? 527 ARG A CB 1 ATOM 3823 C CG . ARG A 1 534 ? 4.802 58.454 45.143 1.00 16.13 ? 527 ARG A CG 1 ATOM 3824 C CD . ARG A 1 534 ? 3.710 57.325 45.057 1.00 16.28 ? 527 ARG A CD 1 ATOM 3825 N NE . ARG A 1 534 ? 4.053 56.286 44.067 1.00 16.26 ? 527 ARG A NE 1 ATOM 3826 C CZ . ARG A 1 534 ? 3.111 55.507 43.503 1.00 17.37 ? 527 ARG A CZ 1 ATOM 3827 N NH1 . ARG A 1 534 ? 1.793 55.739 43.766 1.00 15.28 ? 527 ARG A NH1 1 ATOM 3828 N NH2 . ARG A 1 534 ? 3.450 54.561 42.617 1.00 17.00 ? 527 ARG A NH2 1 ATOM 3829 N N . LEU A 1 535 ? 6.546 59.243 48.566 1.00 16.16 ? 528 LEU A N 1 ATOM 3830 C CA . LEU A 1 535 ? 5.827 59.706 49.745 1.00 16.13 ? 528 LEU A CA 1 ATOM 3831 C C . LEU A 1 535 ? 6.590 60.667 50.656 1.00 15.93 ? 528 LEU A C 1 ATOM 3832 O O . LEU A 1 535 ? 5.944 61.311 51.483 1.00 17.86 ? 528 LEU A O 1 ATOM 3833 C CB . LEU A 1 535 ? 5.290 58.522 50.608 1.00 15.87 ? 528 LEU A CB 1 ATOM 3834 C CG . LEU A 1 535 ? 4.344 57.593 49.815 1.00 17.55 ? 528 LEU A CG 1 ATOM 3835 C CD1 . LEU A 1 535 ? 3.909 56.408 50.739 1.00 18.84 ? 528 LEU A CD1 1 ATOM 3836 C CD2 . LEU A 1 535 ? 3.099 58.377 49.317 1.00 23.41 ? 528 LEU A CD2 1 ATOM 3837 N N . GLY A 1 536 ? 7.909 60.699 50.586 1.00 14.44 ? 529 GLY A N 1 ATOM 3838 C CA . GLY A 1 536 ? 8.709 61.660 51.409 1.00 15.67 ? 529 GLY A CA 1 ATOM 3839 C C . GLY A 1 536 ? 8.845 61.241 52.863 1.00 15.96 ? 529 GLY A C 1 ATOM 3840 O O . GLY A 1 536 ? 8.804 62.089 53.790 1.00 15.38 ? 529 GLY A O 1 ATOM 3841 N N . ILE A 1 537 ? 8.964 59.937 53.082 1.00 16.32 ? 530 ILE A N 1 ATOM 3842 C CA . ILE A 1 537 ? 9.188 59.422 54.441 1.00 16.77 ? 530 ILE A CA 1 ATOM 3843 C C . ILE A 1 537 ? 10.707 59.162 54.591 1.00 18.07 ? 530 ILE A C 1 ATOM 3844 O O . ILE A 1 537 ? 11.322 58.513 53.752 1.00 16.93 ? 530 ILE A O 1 ATOM 3845 C CB . ILE A 1 537 ? 8.397 58.119 54.670 1.00 16.41 ? 530 ILE A CB 1 ATOM 3846 C CG1 . ILE A 1 537 ? 6.894 58.406 54.627 1.00 18.16 ? 530 ILE A CG1 1 ATOM 3847 C CG2 . ILE A 1 537 ? 8.781 57.446 55.997 1.00 17.90 ? 530 ILE A CG2 1 ATOM 3848 C CD1 . ILE A 1 537 ? 6.097 57.130 54.256 1.00 19.37 ? 530 ILE A CD1 1 ATOM 3849 N N . ALA A 1 538 ? 11.297 59.713 55.652 1.00 16.93 ? 531 ALA A N 1 ATOM 3850 C CA . ALA A 1 538 ? 12.751 59.589 55.887 1.00 18.31 ? 531 ALA A CA 1 ATOM 3851 C C . ALA A 1 538 ? 13.155 58.090 55.758 1.00 19.53 ? 531 ALA A C 1 ATOM 3852 O O . ALA A 1 538 ? 12.535 57.212 56.420 1.00 19.52 ? 531 ALA A O 1 ATOM 3853 C CB . ALA A 1 538 ? 13.063 60.121 57.323 1.00 18.78 ? 531 ALA A CB 1 ATOM 3854 N N . SER A 1 539 ? 14.156 57.771 54.919 1.00 17.95 ? 532 SER A N 1 ATOM 3855 C CA . SER A 1 539 ? 14.477 56.362 54.702 1.00 18.05 ? 532 SER A CA 1 ATOM 3856 C C . SER A 1 539 ? 15.962 56.124 54.856 1.00 18.85 ? 532 SER A C 1 ATOM 3857 O O . SER A 1 539 ? 16.792 57.042 54.646 1.00 18.33 ? 532 SER A O 1 ATOM 3858 C CB . SER A 1 539 ? 14.016 55.918 53.285 1.00 18.66 ? 532 SER A CB 1 ATOM 3859 O OG . SER A 1 539 ? 12.587 55.914 53.180 1.00 18.38 ? 532 SER A OG 1 ATOM 3860 N N . GLY A 1 540 ? 16.316 54.879 55.155 1.00 18.93 ? 533 GLY A N 1 ATOM 3861 C CA . GLY A 1 540 ? 17.722 54.492 55.162 1.00 20.05 ? 533 GLY A CA 1 ATOM 3862 C C . GLY A 1 540 ? 17.932 53.018 54.833 1.00 20.60 ? 533 GLY A C 1 ATOM 3863 O O . GLY A 1 540 ? 16.983 52.213 54.875 1.00 18.96 ? 533 GLY A O 1 ATOM 3864 N N . ARG A 1 541 ? 19.193 52.660 54.589 1.00 19.83 ? 534 ARG A N 1 ATOM 3865 C CA . ARG A 1 541 ? 19.565 51.238 54.392 1.00 21.15 ? 534 ARG A CA 1 ATOM 3866 C C . ARG A 1 541 ? 21.036 51.061 54.791 1.00 20.80 ? 534 ARG A C 1 ATOM 3867 O O . ARG A 1 541 ? 21.787 52.026 54.721 1.00 21.02 ? 534 ARG A O 1 ATOM 3868 C CB . ARG A 1 541 ? 19.383 50.810 52.922 1.00 21.28 ? 534 ARG A CB 1 ATOM 3869 C CG . ARG A 1 541 ? 20.301 51.580 51.910 1.00 22.46 ? 534 ARG A CG 1 ATOM 3870 C CD . ARG A 1 541 ? 19.802 51.415 50.438 1.00 23.96 ? 534 ARG A CD 1 ATOM 3871 N NE . ARG A 1 541 ? 19.631 50.000 50.045 1.00 24.81 ? 534 ARG A NE 1 ATOM 3872 C CZ . ARG A 1 541 ? 19.691 49.536 48.786 1.00 25.52 ? 534 ARG A CZ 1 ATOM 3873 N NH1 . ARG A 1 541 ? 19.541 48.234 48.571 1.00 21.52 ? 534 ARG A NH1 1 ATOM 3874 N NH2 . ARG A 1 541 ? 19.891 50.353 47.751 1.00 22.74 ? 534 ARG A NH2 1 ATOM 3875 N N . ALA A 1 542 ? 21.434 49.827 55.165 1.00 20.54 ? 535 ALA A N 1 ATOM 3876 C CA . ALA A 1 542 ? 22.810 49.558 55.623 1.00 22.21 ? 535 ALA A CA 1 ATOM 3877 C C . ALA A 1 542 ? 23.108 48.099 55.302 1.00 21.49 ? 535 ALA A C 1 ATOM 3878 O O . ALA A 1 542 ? 22.225 47.237 55.485 1.00 22.29 ? 535 ALA A O 1 ATOM 3879 C CB . ALA A 1 542 ? 22.877 49.760 57.144 1.00 20.72 ? 535 ALA A CB 1 ATOM 3880 N N . ARG A 1 543 ? 24.309 47.804 54.812 1.00 22.39 ? 536 ARG A N 1 ATOM 3881 C CA . ARG A 1 543 ? 24.689 46.411 54.536 1.00 23.02 ? 536 ARG A CA 1 ATOM 3882 C C . ARG A 1 543 ? 26.207 46.341 54.605 1.00 23.89 ? 536 ARG A C 1 ATOM 3883 O O . ARG A 1 543 ? 26.837 47.374 54.557 1.00 24.33 ? 536 ARG A O 1 ATOM 3884 C CB A ARG A 1 543 ? 24.193 45.972 53.126 0.50 23.57 ? 536 ARG A CB 1 ATOM 3885 C CB B ARG A 1 543 ? 24.199 45.972 53.133 0.50 23.29 ? 536 ARG A CB 1 ATOM 3886 C CG A ARG A 1 543 ? 24.479 46.956 51.970 0.50 22.77 ? 536 ARG A CG 1 ATOM 3887 C CG B ARG A 1 543 ? 24.891 46.666 51.959 0.50 22.18 ? 536 ARG A CG 1 ATOM 3888 C CD A ARG A 1 543 ? 23.298 47.899 51.736 0.50 28.07 ? 536 ARG A CD 1 ATOM 3889 C CD B ARG A 1 543 ? 24.418 46.055 50.660 0.50 23.17 ? 536 ARG A CD 1 ATOM 3890 N NE A ARG A 1 543 ? 23.301 48.558 50.421 0.50 28.27 ? 536 ARG A NE 1 ATOM 3891 N NE B ARG A 1 543 ? 22.988 45.804 50.738 0.50 24.19 ? 536 ARG A NE 1 ATOM 3892 C CZ A ARG A 1 543 ? 23.434 49.869 50.256 0.50 24.64 ? 536 ARG A CZ 1 ATOM 3893 C CZ B ARG A 1 543 ? 22.199 45.554 49.707 0.50 23.01 ? 536 ARG A CZ 1 ATOM 3894 N NH1 A ARG A 1 543 ? 23.590 50.638 51.327 0.50 23.61 ? 536 ARG A NH1 1 ATOM 3895 N NH1 B ARG A 1 543 ? 20.928 45.335 49.922 0.50 19.22 ? 536 ARG A NH1 1 ATOM 3896 N NH2 A ARG A 1 543 ? 23.382 50.403 49.046 0.50 19.96 ? 536 ARG A NH2 1 ATOM 3897 N NH2 B ARG A 1 543 ? 22.687 45.530 48.472 0.50 26.37 ? 536 ARG A NH2 1 ATOM 3898 N N . TYR A 1 544 ? 26.785 45.151 54.716 1.00 24.38 ? 537 TYR A N 1 ATOM 3899 C CA . TYR A 1 544 ? 28.224 45.012 54.518 1.00 26.34 ? 537 TYR A CA 1 ATOM 3900 C C . TYR A 1 544 ? 28.510 44.899 53.023 1.00 26.68 ? 537 TYR A C 1 ATOM 3901 O O . TYR A 1 544 ? 27.698 44.339 52.273 1.00 25.55 ? 537 TYR A O 1 ATOM 3902 C CB . TYR A 1 544 ? 28.794 43.804 55.317 1.00 26.39 ? 537 TYR A CB 1 ATOM 3903 C CG . TYR A 1 544 ? 29.693 44.314 56.406 1.00 25.57 ? 537 TYR A CG 1 ATOM 3904 C CD1 . TYR A 1 544 ? 29.174 45.018 57.499 1.00 26.71 ? 537 TYR A CD1 1 ATOM 3905 C CD2 . TYR A 1 544 ? 31.085 44.140 56.318 1.00 25.49 ? 537 TYR A CD2 1 ATOM 3906 C CE1 . TYR A 1 544 ? 30.024 45.529 58.503 1.00 24.99 ? 537 TYR A CE1 1 ATOM 3907 C CE2 . TYR A 1 544 ? 31.925 44.632 57.308 1.00 26.41 ? 537 TYR A CE2 1 ATOM 3908 C CZ . TYR A 1 544 ? 31.383 45.336 58.386 1.00 27.18 ? 537 TYR A CZ 1 ATOM 3909 O OH . TYR A 1 544 ? 32.206 45.838 59.357 1.00 28.22 ? 537 TYR A OH 1 ATOM 3910 N N . THR A 1 545 ? 29.673 45.405 52.595 1.00 28.12 ? 538 THR A N 1 ATOM 3911 C CA . THR A 1 545 ? 29.983 45.486 51.172 1.00 28.62 ? 538 THR A CA 1 ATOM 3912 C C . THR A 1 545 ? 31.461 45.166 50.884 1.00 31.05 ? 538 THR A C 1 ATOM 3913 O O . THR A 1 545 ? 32.233 44.972 51.815 1.00 30.43 ? 538 THR A O 1 ATOM 3914 C CB . THR A 1 545 ? 29.629 46.898 50.608 1.00 28.85 ? 538 THR A CB 1 ATOM 3915 O OG1 . THR A 1 545 ? 29.697 46.880 49.174 1.00 30.54 ? 538 THR A OG1 1 ATOM 3916 C CG2 . THR A 1 545 ? 30.543 47.941 51.121 1.00 28.12 ? 538 THR A CG2 1 ATOM 3917 N N . LYS A 1 546 ? 31.796 45.121 49.591 1.00 32.59 ? 539 LYS A N 1 ATOM 3918 C CA . LYS A 1 546 ? 33.159 44.935 49.089 1.00 36.53 ? 539 LYS A CA 1 ATOM 3919 C C . LYS A 1 546 ? 33.973 46.234 49.113 1.00 37.86 ? 539 LYS A C 1 ATOM 3920 O O . LYS A 1 546 ? 33.445 47.297 49.446 1.00 37.53 ? 539 LYS A O 1 ATOM 3921 C CB . LYS A 1 546 ? 33.152 44.315 47.669 1.00 36.29 ? 539 LYS A CB 1 ATOM 3922 C CG . LYS A 1 546 ? 32.358 45.090 46.592 1.00 40.64 ? 539 LYS A CG 1 ATOM 3923 C CD . LYS A 1 546 ? 31.183 44.242 46.049 1.00 47.56 ? 539 LYS A CD 1 ATOM 3924 C CE . LYS A 1 546 ? 30.139 45.076 45.246 1.00 48.67 ? 539 LYS A CE 1 ATOM 3925 N NZ . LYS A 1 546 ? 30.519 45.359 43.809 1.00 49.45 ? 539 LYS A NZ 1 ATOM 3926 N N . ASN A 1 547 ? 35.253 46.140 48.759 1.00 40.19 ? 540 ASN A N 1 ATOM 3927 C CA . ASN A 1 547 ? 36.106 47.322 48.578 1.00 43.19 ? 540 ASN A CA 1 ATOM 3928 C C . ASN A 1 547 ? 35.737 48.136 47.320 1.00 43.69 ? 540 ASN A C 1 ATOM 3929 O O . ASN A 1 547 ? 35.419 47.556 46.257 1.00 45.49 ? 540 ASN A O 1 ATOM 3930 C CB . ASN A 1 547 ? 37.582 46.908 48.540 1.00 44.77 ? 540 ASN A CB 1 ATOM 3931 C CG . ASN A 1 547 ? 38.533 48.079 48.817 1.00 48.12 ? 540 ASN A CG 1 ATOM 3932 O OD1 . ASN A 1 547 ? 38.209 49.243 48.556 1.00 50.42 ? 540 ASN A OD1 1 ATOM 3933 N ND2 . ASN A 1 547 ? 39.716 47.772 49.357 1.00 50.76 ? 540 ASN A ND2 1 ATOM 3934 N N . ASN A 1 551 ? 32.851 49.346 40.919 1.00 52.79 ? 544 ASN A N 1 ATOM 3935 C CA . ASN A 1 551 ? 31.862 48.270 40.746 1.00 51.80 ? 544 ASN A CA 1 ATOM 3936 C C . ASN A 1 551 ? 30.593 48.348 41.611 1.00 49.15 ? 544 ASN A C 1 ATOM 3937 O O . ASN A 1 551 ? 29.812 47.380 41.641 1.00 48.32 ? 544 ASN A O 1 ATOM 3938 C CB . ASN A 1 551 ? 32.517 46.897 40.981 1.00 53.19 ? 544 ASN A CB 1 ATOM 3939 C CG . ASN A 1 551 ? 33.156 46.329 39.715 1.00 56.92 ? 544 ASN A CG 1 ATOM 3940 O OD1 . ASN A 1 551 ? 34.079 46.945 39.144 1.00 62.11 ? 544 ASN A OD1 1 ATOM 3941 N ND2 . ASN A 1 551 ? 32.676 45.151 39.269 1.00 54.84 ? 544 ASN A ND2 1 ATOM 3942 N N . LYS A 1 552 ? 30.407 49.465 42.323 1.00 46.88 ? 545 LYS A N 1 ATOM 3943 C CA . LYS A 1 552 ? 29.317 49.607 43.301 1.00 44.92 ? 545 LYS A CA 1 ATOM 3944 C C . LYS A 1 552 ? 27.879 49.322 42.779 1.00 42.82 ? 545 LYS A C 1 ATOM 3945 O O . LYS A 1 552 ? 27.032 48.786 43.523 1.00 42.25 ? 545 LYS A O 1 ATOM 3946 C CB . LYS A 1 552 ? 29.429 50.977 43.999 1.00 45.40 ? 545 LYS A CB 1 ATOM 3947 C CG . LYS A 1 552 ? 28.141 51.777 44.193 1.00 45.42 ? 545 LYS A CG 1 ATOM 3948 C CD . LYS A 1 552 ? 28.414 53.094 44.976 1.00 47.86 ? 545 LYS A CD 1 ATOM 3949 C CE . LYS A 1 552 ? 27.091 53.772 45.371 1.00 45.32 ? 545 LYS A CE 1 ATOM 3950 N NZ . LYS A 1 552 ? 27.253 55.008 46.157 1.00 46.23 ? 545 LYS A NZ 1 ATOM 3951 N N . PHE A 1 553 ? 27.613 49.655 41.521 1.00 40.17 ? 546 PHE A N 1 ATOM 3952 C CA . PHE A 1 553 ? 26.282 49.407 40.937 1.00 39.08 ? 546 PHE A CA 1 ATOM 3953 C C . PHE A 1 553 ? 26.201 48.112 40.110 1.00 38.73 ? 546 PHE A C 1 ATOM 3954 O O . PHE A 1 553 ? 25.146 47.819 39.558 1.00 39.02 ? 546 PHE A O 1 ATOM 3955 C CB . PHE A 1 553 ? 25.805 50.584 40.058 1.00 38.35 ? 546 PHE A CB 1 ATOM 3956 C CG . PHE A 1 553 ? 25.763 51.923 40.775 1.00 38.05 ? 546 PHE A CG 1 ATOM 3957 C CD1 . PHE A 1 553 ? 26.576 52.995 40.344 1.00 40.59 ? 546 PHE A CD1 1 ATOM 3958 C CD2 . PHE A 1 553 ? 24.936 52.110 41.885 1.00 38.24 ? 546 PHE A CD2 1 ATOM 3959 C CE1 . PHE A 1 553 ? 26.540 54.236 40.986 1.00 39.40 ? 546 PHE A CE1 1 ATOM 3960 C CE2 . PHE A 1 553 ? 24.886 53.350 42.541 1.00 36.84 ? 546 PHE A CE2 1 ATOM 3961 C CZ . PHE A 1 553 ? 25.695 54.408 42.093 1.00 37.85 ? 546 PHE A CZ 1 ATOM 3962 N N . SER A 1 554 ? 27.288 47.348 40.030 1.00 37.84 ? 547 SER A N 1 ATOM 3963 C CA . SER A 1 554 ? 27.342 46.164 39.132 1.00 37.76 ? 547 SER A CA 1 ATOM 3964 C C . SER A 1 554 ? 26.756 44.874 39.739 1.00 37.21 ? 547 SER A C 1 ATOM 3965 O O . SER A 1 554 ? 26.200 44.018 39.004 1.00 37.85 ? 547 SER A O 1 ATOM 3966 C CB . SER A 1 554 ? 28.775 45.929 38.668 1.00 38.69 ? 547 SER A CB 1 ATOM 3967 O OG . SER A 1 554 ? 29.234 47.076 37.965 1.00 39.08 ? 547 SER A OG 1 ATOM 3968 N N . GLY A 1 555 ? 26.840 44.774 41.077 1.00 35.47 ? 548 GLY A N 1 ATOM 3969 C CA . GLY A 1 555 ? 26.517 43.554 41.818 1.00 33.73 ? 548 GLY A CA 1 ATOM 3970 C C . GLY A 1 555 ? 27.778 42.710 42.026 1.00 32.96 ? 548 GLY A C 1 ATOM 3971 O O . GLY A 1 555 ? 28.813 42.873 41.297 1.00 33.74 ? 548 GLY A O 1 ATOM 3972 N N . TYR A 1 556 ? 27.711 41.825 43.021 1.00 29.62 ? 549 TYR A N 1 ATOM 3973 C CA . TYR A 1 556 ? 28.774 40.865 43.318 1.00 28.40 ? 549 TYR A CA 1 ATOM 3974 C C . TYR A 1 556 ? 28.736 39.763 42.204 1.00 26.82 ? 549 TYR A C 1 ATOM 3975 O O . TYR A 1 556 ? 27.776 39.701 41.434 1.00 27.13 ? 549 TYR A O 1 ATOM 3976 C CB . TYR A 1 556 ? 28.578 40.294 44.736 1.00 27.81 ? 549 TYR A CB 1 ATOM 3977 C CG . TYR A 1 556 ? 27.138 39.905 44.965 1.00 26.74 ? 549 TYR A CG 1 ATOM 3978 C CD1 . TYR A 1 556 ? 26.683 38.601 44.703 1.00 25.53 ? 549 TYR A CD1 1 ATOM 3979 C CD2 . TYR A 1 556 ? 26.218 40.868 45.412 1.00 23.79 ? 549 TYR A CD2 1 ATOM 3980 C CE1 . TYR A 1 556 ? 25.304 38.274 44.879 1.00 24.64 ? 549 TYR A CE1 1 ATOM 3981 C CE2 . TYR A 1 556 ? 24.897 40.547 45.597 1.00 22.08 ? 549 TYR A CE2 1 ATOM 3982 C CZ . TYR A 1 556 ? 24.451 39.247 45.326 1.00 20.56 ? 549 TYR A CZ 1 ATOM 3983 O OH . TYR A 1 556 ? 23.087 39.021 45.510 1.00 21.51 ? 549 TYR A OH 1 ATOM 3984 N N . PRO A 1 557 ? 29.786 38.939 42.078 1.00 26.24 ? 550 PRO A N 1 ATOM 3985 C CA . PRO A 1 557 ? 29.826 38.091 40.858 1.00 26.78 ? 550 PRO A CA 1 ATOM 3986 C C . PRO A 1 557 ? 28.601 37.185 40.640 1.00 26.22 ? 550 PRO A C 1 ATOM 3987 O O . PRO A 1 557 ? 28.138 37.048 39.491 1.00 26.94 ? 550 PRO A O 1 ATOM 3988 C CB . PRO A 1 557 ? 31.121 37.285 41.048 1.00 26.37 ? 550 PRO A CB 1 ATOM 3989 C CG . PRO A 1 557 ? 32.040 38.315 41.799 1.00 27.55 ? 550 PRO A CG 1 ATOM 3990 C CD . PRO A 1 557 ? 31.076 38.925 42.805 1.00 26.16 ? 550 PRO A CD 1 ATOM 3991 N N . LEU A 1 558 ? 28.085 36.577 41.711 1.00 25.67 ? 551 LEU A N 1 ATOM 3992 C CA . LEU A 1 558 ? 26.981 35.584 41.570 1.00 25.51 ? 551 LEU A CA 1 ATOM 3993 C C . LEU A 1 558 ? 25.563 36.172 41.654 1.00 24.69 ? 551 LEU A C 1 ATOM 3994 O O . LEU A 1 558 ? 24.580 35.443 41.736 1.00 24.32 ? 551 LEU A O 1 ATOM 3995 C CB . LEU A 1 558 ? 27.177 34.433 42.564 1.00 24.56 ? 551 LEU A CB 1 ATOM 3996 C CG . LEU A 1 558 ? 28.505 33.720 42.254 1.00 25.42 ? 551 LEU A CG 1 ATOM 3997 C CD1 . LEU A 1 558 ? 28.851 32.683 43.327 1.00 26.41 ? 551 LEU A CD1 1 ATOM 3998 C CD2 . LEU A 1 558 ? 28.506 33.018 40.868 1.00 21.89 ? 551 LEU A CD2 1 ATOM 3999 N N . TYR A 1 559 ? 25.479 37.501 41.581 1.00 24.39 ? 552 TYR A N 1 ATOM 4000 C CA . TYR A 1 559 ? 24.229 38.246 41.688 1.00 22.84 ? 552 TYR A CA 1 ATOM 4001 C C . TYR A 1 559 ? 23.166 37.743 40.710 1.00 22.46 ? 552 TYR A C 1 ATOM 4002 O O . TYR A 1 559 ? 23.424 37.703 39.501 1.00 23.73 ? 552 TYR A O 1 ATOM 4003 C CB . TYR A 1 559 ? 24.575 39.701 41.388 1.00 22.74 ? 552 TYR A CB 1 ATOM 4004 C CG . TYR A 1 559 ? 23.390 40.640 41.268 1.00 23.34 ? 552 TYR A CG 1 ATOM 4005 C CD1 . TYR A 1 559 ? 22.522 40.842 42.346 1.00 22.42 ? 552 TYR A CD1 1 ATOM 4006 C CD2 . TYR A 1 559 ? 23.181 41.356 40.090 1.00 22.80 ? 552 TYR A CD2 1 ATOM 4007 C CE1 . TYR A 1 559 ? 21.413 41.721 42.231 1.00 22.74 ? 552 TYR A CE1 1 ATOM 4008 C CE2 . TYR A 1 559 ? 22.094 42.293 39.979 1.00 21.41 ? 552 TYR A CE2 1 ATOM 4009 C CZ . TYR A 1 559 ? 21.254 42.441 41.034 1.00 21.10 ? 552 TYR A CZ 1 ATOM 4010 O OH . TYR A 1 559 ? 20.216 43.319 40.910 1.00 20.99 ? 552 TYR A OH 1 ATOM 4011 N N . HIS A 1 560 ? 22.012 37.320 41.233 1.00 21.62 ? 553 HIS A N 1 ATOM 4012 C CA . HIS A 1 560 ? 20.841 36.889 40.415 1.00 21.86 ? 553 HIS A CA 1 ATOM 4013 C C . HIS A 1 560 ? 21.108 35.640 39.569 1.00 22.87 ? 553 HIS A C 1 ATOM 4014 O O . HIS A 1 560 ? 20.393 35.365 38.564 1.00 22.42 ? 553 HIS A O 1 ATOM 4015 C CB . HIS A 1 560 ? 20.287 38.023 39.528 1.00 20.50 ? 553 HIS A CB 1 ATOM 4016 C CG . HIS A 1 560 ? 19.528 39.093 40.285 1.00 21.34 ? 553 HIS A CG 1 ATOM 4017 N ND1 . HIS A 1 560 ? 18.935 40.156 39.640 1.00 18.85 ? 553 HIS A ND1 1 ATOM 4018 C CD2 . HIS A 1 560 ? 19.285 39.276 41.608 1.00 20.61 ? 553 HIS A CD2 1 ATOM 4019 C CE1 . HIS A 1 560 ? 18.335 40.943 40.524 1.00 20.96 ? 553 HIS A CE1 1 ATOM 4020 N NE2 . HIS A 1 560 ? 18.536 40.435 41.726 1.00 18.69 ? 553 HIS A NE2 1 ATOM 4021 N N . SER A 1 561 ? 22.108 34.876 40.004 1.00 23.85 ? 554 SER A N 1 ATOM 4022 C CA . SER A 1 561 ? 22.458 33.599 39.410 1.00 22.71 ? 554 SER A CA 1 ATOM 4023 C C . SER A 1 561 ? 21.973 32.381 40.292 1.00 25.72 ? 554 SER A C 1 ATOM 4024 O O . SER A 1 561 ? 21.741 32.539 41.456 1.00 24.45 ? 554 SER A O 1 ATOM 4025 C CB . SER A 1 561 ? 23.975 33.489 39.160 1.00 23.81 ? 554 SER A CB 1 ATOM 4026 O OG A SER A 1 561 ? 24.690 33.263 40.374 0.50 21.70 ? 554 SER A OG 1 ATOM 4027 O OG B SER A 1 561 ? 24.381 32.137 38.968 0.50 23.64 ? 554 SER A OG 1 ATOM 4028 N N . VAL A 1 562 ? 21.832 31.208 39.657 1.00 22.98 ? 555 VAL A N 1 ATOM 4029 C CA . VAL A 1 562 ? 21.479 29.962 40.376 1.00 24.88 ? 555 VAL A CA 1 ATOM 4030 C C . VAL A 1 562 ? 22.504 29.643 41.494 1.00 25.24 ? 555 VAL A C 1 ATOM 4031 O O . VAL A 1 562 ? 22.188 28.886 42.421 1.00 26.19 ? 555 VAL A O 1 ATOM 4032 C CB . VAL A 1 562 ? 21.389 28.772 39.390 1.00 25.32 ? 555 VAL A CB 1 ATOM 4033 C CG1 . VAL A 1 562 ? 22.840 28.379 38.890 1.00 25.81 ? 555 VAL A CG1 1 ATOM 4034 C CG2 . VAL A 1 562 ? 20.689 27.514 40.037 1.00 23.56 ? 555 VAL A CG2 1 ATOM 4035 N N . TYR A 1 563 ? 23.707 30.222 41.382 1.00 24.75 ? 556 TYR A N 1 ATOM 4036 C CA . TYR A 1 563 ? 24.859 29.887 42.233 1.00 25.54 ? 556 TYR A CA 1 ATOM 4037 C C . TYR A 1 563 ? 24.809 30.679 43.536 1.00 25.33 ? 556 TYR A C 1 ATOM 4038 O O . TYR A 1 563 ? 25.604 30.406 44.454 1.00 25.36 ? 556 TYR A O 1 ATOM 4039 C CB . TYR A 1 563 ? 26.203 30.135 41.529 1.00 24.78 ? 556 TYR A CB 1 ATOM 4040 C CG . TYR A 1 563 ? 26.309 29.330 40.260 1.00 26.08 ? 556 TYR A CG 1 ATOM 4041 C CD1 . TYR A 1 563 ? 26.234 27.929 40.297 1.00 26.85 ? 556 TYR A CD1 1 ATOM 4042 C CD2 . TYR A 1 563 ? 26.461 29.952 39.032 1.00 25.08 ? 556 TYR A CD2 1 ATOM 4043 C CE1 . TYR A 1 563 ? 26.283 27.178 39.144 1.00 26.87 ? 556 TYR A CE1 1 ATOM 4044 C CE2 . TYR A 1 563 ? 26.536 29.194 37.845 1.00 28.24 ? 556 TYR A CE2 1 ATOM 4045 C CZ . TYR A 1 563 ? 26.412 27.825 37.908 1.00 28.25 ? 556 TYR A CZ 1 ATOM 4046 O OH . TYR A 1 563 ? 26.466 27.071 36.765 1.00 29.43 ? 556 TYR A OH 1 ATOM 4047 N N . GLU A 1 564 ? 23.855 31.606 43.634 1.00 24.47 ? 557 GLU A N 1 ATOM 4048 C CA . GLU A 1 564 ? 23.696 32.369 44.871 1.00 25.15 ? 557 GLU A CA 1 ATOM 4049 C C . GLU A 1 564 ? 22.940 31.515 45.885 1.00 24.60 ? 557 GLU A C 1 ATOM 4050 O O . GLU A 1 564 ? 21.712 31.489 45.889 1.00 25.40 ? 557 GLU A O 1 ATOM 4051 C CB . GLU A 1 564 ? 22.958 33.685 44.571 1.00 25.28 ? 557 GLU A CB 1 ATOM 4052 C CG . GLU A 1 564 ? 23.205 34.768 45.553 1.00 28.85 ? 557 GLU A CG 1 ATOM 4053 C CD . GLU A 1 564 ? 22.152 35.843 45.336 1.00 23.10 ? 557 GLU A CD 1 ATOM 4054 O OE1 . GLU A 1 564 ? 22.221 36.580 44.312 1.00 27.09 ? 557 GLU A OE1 1 ATOM 4055 O OE2 . GLU A 1 564 ? 21.232 35.809 46.135 1.00 27.30 ? 557 GLU A OE2 1 ATOM 4056 N N . THR A 1 565 ? 23.675 30.772 46.705 1.00 24.86 ? 558 THR A N 1 ATOM 4057 C CA . THR A 1 565 ? 23.101 29.738 47.567 1.00 24.88 ? 558 THR A CA 1 ATOM 4058 C C . THR A 1 565 ? 23.455 29.989 49.037 1.00 24.50 ? 558 THR A C 1 ATOM 4059 O O . THR A 1 565 ? 24.311 30.831 49.352 1.00 24.12 ? 558 THR A O 1 ATOM 4060 C CB . THR A 1 565 ? 23.686 28.349 47.195 1.00 25.65 ? 558 THR A CB 1 ATOM 4061 O OG1 . THR A 1 565 ? 25.112 28.402 47.270 1.00 27.41 ? 558 THR A OG1 1 ATOM 4062 C CG2 . THR A 1 565 ? 23.281 27.919 45.757 1.00 25.65 ? 558 THR A CG2 1 ATOM 4063 N N . TYR A 1 566 ? 22.818 29.237 49.932 1.00 24.37 ? 559 TYR A N 1 ATOM 4064 C CA . TYR A 1 566 ? 23.307 29.163 51.322 1.00 25.41 ? 559 TYR A CA 1 ATOM 4065 C C . TYR A 1 566 ? 24.830 28.887 51.416 1.00 26.64 ? 559 TYR A C 1 ATOM 4066 O O . TYR A 1 566 ? 25.555 29.521 52.219 1.00 26.90 ? 559 TYR A O 1 ATOM 4067 C CB . TYR A 1 566 ? 22.539 28.094 52.092 1.00 25.61 ? 559 TYR A CB 1 ATOM 4068 C CG . TYR A 1 566 ? 23.084 27.857 53.481 1.00 27.52 ? 559 TYR A CG 1 ATOM 4069 C CD1 . TYR A 1 566 ? 22.748 28.720 54.536 1.00 30.00 ? 559 TYR A CD1 1 ATOM 4070 C CD2 . TYR A 1 566 ? 23.953 26.788 53.741 1.00 30.96 ? 559 TYR A CD2 1 ATOM 4071 C CE1 . TYR A 1 566 ? 23.244 28.521 55.815 1.00 30.57 ? 559 TYR A CE1 1 ATOM 4072 C CE2 . TYR A 1 566 ? 24.485 26.587 55.028 1.00 32.83 ? 559 TYR A CE2 1 ATOM 4073 C CZ . TYR A 1 566 ? 24.117 27.466 56.059 1.00 31.61 ? 559 TYR A CZ 1 ATOM 4074 O OH . TYR A 1 566 ? 24.609 27.282 57.336 1.00 32.02 ? 559 TYR A OH 1 ATOM 4075 N N . GLU A 1 567 ? 25.311 27.915 50.635 1.00 26.08 ? 560 GLU A N 1 ATOM 4076 C CA . GLU A 1 567 ? 26.745 27.523 50.687 1.00 27.26 ? 560 GLU A CA 1 ATOM 4077 C C . GLU A 1 567 ? 27.667 28.643 50.294 1.00 26.66 ? 560 GLU A C 1 ATOM 4078 O O . GLU A 1 567 ? 28.767 28.751 50.862 1.00 27.26 ? 560 GLU A O 1 ATOM 4079 C CB . GLU A 1 567 ? 27.040 26.284 49.800 1.00 28.50 ? 560 GLU A CB 1 ATOM 4080 C CG . GLU A 1 567 ? 26.406 24.971 50.311 1.00 28.75 ? 560 GLU A CG 1 ATOM 4081 C CD . GLU A 1 567 ? 24.892 24.953 50.163 1.00 31.45 ? 560 GLU A CD 1 ATOM 4082 O OE1 . GLU A 1 567 ? 24.394 25.498 49.173 1.00 29.70 ? 560 GLU A OE1 1 ATOM 4083 O OE2 . GLU A 1 567 ? 24.193 24.372 51.023 1.00 31.54 ? 560 GLU A OE2 1 ATOM 4084 N N . LEU A 1 568 ? 27.262 29.438 49.304 1.00 24.58 ? 561 LEU A N 1 ATOM 4085 C CA . LEU A 1 568 ? 28.019 30.623 48.896 1.00 25.45 ? 561 LEU A CA 1 ATOM 4086 C C . LEU A 1 568 ? 28.292 31.483 50.132 1.00 25.93 ? 561 LEU A C 1 ATOM 4087 O O . LEU A 1 568 ? 29.434 31.947 50.363 1.00 26.41 ? 561 LEU A O 1 ATOM 4088 C CB . LEU A 1 568 ? 27.213 31.478 47.896 1.00 25.34 ? 561 LEU A CB 1 ATOM 4089 C CG . LEU A 1 568 ? 27.900 32.796 47.495 1.00 24.66 ? 561 LEU A CG 1 ATOM 4090 C CD1 . LEU A 1 568 ? 29.260 32.530 46.892 1.00 25.66 ? 561 LEU A CD1 1 ATOM 4091 C CD2 . LEU A 1 568 ? 26.981 33.607 46.512 1.00 23.66 ? 561 LEU A CD2 1 ATOM 4092 N N . VAL A 1 569 ? 27.229 31.724 50.911 1.00 25.70 ? 562 VAL A N 1 ATOM 4093 C CA . VAL A 1 569 ? 27.327 32.629 52.064 1.00 25.63 ? 562 VAL A CA 1 ATOM 4094 C C . VAL A 1 569 ? 28.161 31.965 53.185 1.00 26.73 ? 562 VAL A C 1 ATOM 4095 O O . VAL A 1 569 ? 29.139 32.537 53.688 1.00 27.78 ? 562 VAL A O 1 ATOM 4096 C CB . VAL A 1 569 ? 25.908 33.049 52.598 1.00 24.70 ? 562 VAL A CB 1 ATOM 4097 C CG1 . VAL A 1 569 ? 26.028 33.932 53.882 1.00 24.85 ? 562 VAL A CG1 1 ATOM 4098 C CG2 . VAL A 1 569 ? 25.123 33.883 51.555 1.00 25.19 ? 562 VAL A CG2 1 ATOM 4099 N N . GLU A 1 570 ? 27.769 30.747 53.567 1.00 27.64 ? 563 GLU A N 1 ATOM 4100 C CA . GLU A 1 570 ? 28.385 30.016 54.680 1.00 29.57 ? 563 GLU A CA 1 ATOM 4101 C C . GLU A 1 570 ? 29.856 29.706 54.444 1.00 30.94 ? 563 GLU A C 1 ATOM 4102 O O . GLU A 1 570 ? 30.660 29.738 55.384 1.00 31.09 ? 563 GLU A O 1 ATOM 4103 C CB . GLU A 1 570 ? 27.627 28.712 54.907 1.00 30.65 ? 563 GLU A CB 1 ATOM 4104 C CG . GLU A 1 570 ? 27.939 27.997 56.238 1.00 36.02 ? 563 GLU A CG 1 ATOM 4105 C CD . GLU A 1 570 ? 29.196 27.154 56.188 1.00 41.71 ? 563 GLU A CD 1 ATOM 4106 O OE1 . GLU A 1 570 ? 29.523 26.619 55.090 1.00 41.38 ? 563 GLU A OE1 1 ATOM 4107 O OE2 . GLU A 1 570 ? 29.846 27.036 57.255 1.00 42.63 ? 563 GLU A OE2 1 ATOM 4108 N N . LYS A 1 571 ? 30.208 29.361 53.201 1.00 30.22 ? 564 LYS A N 1 ATOM 4109 C CA . LYS A 1 571 ? 31.586 29.021 52.880 1.00 31.69 ? 564 LYS A CA 1 ATOM 4110 C C . LYS A 1 571 ? 32.472 30.238 52.614 1.00 32.08 ? 564 LYS A C 1 ATOM 4111 O O . LYS A 1 571 ? 33.609 30.246 53.040 1.00 32.35 ? 564 LYS A O 1 ATOM 4112 C CB . LYS A 1 571 ? 31.656 28.085 51.655 1.00 31.46 ? 564 LYS A CB 1 ATOM 4113 C CG . LYS A 1 571 ? 31.164 26.678 51.911 1.00 32.63 ? 564 LYS A CG 1 ATOM 4114 C CD . LYS A 1 571 ? 31.400 25.789 50.644 1.00 35.23 ? 564 LYS A CD 1 ATOM 4115 C CE . LYS A 1 571 ? 30.551 24.513 50.642 1.00 38.02 ? 564 LYS A CE 1 ATOM 4116 N NZ . LYS A 1 571 ? 30.840 23.690 51.817 1.00 45.01 ? 564 LYS A NZ 1 ATOM 4117 N N . PHE A 1 572 ? 31.965 31.210 51.848 1.00 31.12 ? 565 PHE A N 1 ATOM 4118 C CA . PHE A 1 572 ? 32.829 32.262 51.294 1.00 31.34 ? 565 PHE A CA 1 ATOM 4119 C C . PHE A 1 572 ? 32.568 33.662 51.797 1.00 31.36 ? 565 PHE A C 1 ATOM 4120 O O . PHE A 1 572 ? 33.490 34.462 51.815 1.00 34.03 ? 565 PHE A O 1 ATOM 4121 C CB . PHE A 1 572 ? 32.791 32.250 49.762 1.00 30.71 ? 565 PHE A CB 1 ATOM 4122 C CG . PHE A 1 572 ? 33.155 30.901 49.171 1.00 32.78 ? 565 PHE A CG 1 ATOM 4123 C CD1 . PHE A 1 572 ? 34.444 30.391 49.318 1.00 32.52 ? 565 PHE A CD1 1 ATOM 4124 C CD2 . PHE A 1 572 ? 32.203 30.139 48.487 1.00 30.12 ? 565 PHE A CD2 1 ATOM 4125 C CE1 . PHE A 1 572 ? 34.770 29.158 48.806 1.00 34.67 ? 565 PHE A CE1 1 ATOM 4126 C CE2 . PHE A 1 572 ? 32.533 28.875 47.947 1.00 32.78 ? 565 PHE A CE2 1 ATOM 4127 C CZ . PHE A 1 572 ? 33.805 28.388 48.114 1.00 33.64 ? 565 PHE A CZ 1 ATOM 4128 N N . TYR A 1 573 ? 31.335 33.999 52.178 1.00 30.38 ? 566 TYR A N 1 ATOM 4129 C CA . TYR A 1 573 ? 31.080 35.387 52.571 1.00 28.88 ? 566 TYR A CA 1 ATOM 4130 C C . TYR A 1 573 ? 31.183 35.617 54.075 1.00 28.83 ? 566 TYR A C 1 ATOM 4131 O O . TYR A 1 573 ? 31.793 36.602 54.509 1.00 29.63 ? 566 TYR A O 1 ATOM 4132 C CB . TYR A 1 573 ? 29.713 35.908 52.034 1.00 27.96 ? 566 TYR A CB 1 ATOM 4133 C CG . TYR A 1 573 ? 29.794 36.401 50.610 1.00 29.18 ? 566 TYR A CG 1 ATOM 4134 C CD1 . TYR A 1 573 ? 29.858 35.502 49.544 1.00 27.26 ? 566 TYR A CD1 1 ATOM 4135 C CD2 . TYR A 1 573 ? 29.846 37.778 50.325 1.00 31.67 ? 566 TYR A CD2 1 ATOM 4136 C CE1 . TYR A 1 573 ? 29.961 35.954 48.218 1.00 29.43 ? 566 TYR A CE1 1 ATOM 4137 C CE2 . TYR A 1 573 ? 29.948 38.246 49.019 1.00 30.74 ? 566 TYR A CE2 1 ATOM 4138 C CZ . TYR A 1 573 ? 30.011 37.320 47.973 1.00 31.58 ? 566 TYR A CZ 1 ATOM 4139 O OH . TYR A 1 573 ? 30.140 37.772 46.701 1.00 31.60 ? 566 TYR A OH 1 ATOM 4140 N N . ASP A 1 574 ? 30.568 34.744 54.877 1.00 28.02 ? 567 ASP A N 1 ATOM 4141 C CA . ASP A 1 574 ? 30.370 35.068 56.306 1.00 28.49 ? 567 ASP A CA 1 ATOM 4142 C C . ASP A 1 574 ? 30.205 33.801 57.142 1.00 28.66 ? 567 ASP A C 1 ATOM 4143 O O . ASP A 1 574 ? 29.159 33.600 57.757 1.00 28.50 ? 567 ASP A O 1 ATOM 4144 C CB . ASP A 1 574 ? 29.127 35.984 56.444 1.00 26.77 ? 567 ASP A CB 1 ATOM 4145 C CG . ASP A 1 574 ? 29.034 36.671 57.827 1.00 29.03 ? 567 ASP A CG 1 ATOM 4146 O OD1 . ASP A 1 574 ? 29.985 36.633 58.626 1.00 29.83 ? 567 ASP A OD1 1 ATOM 4147 O OD2 . ASP A 1 574 ? 27.972 37.217 58.119 1.00 26.83 ? 567 ASP A OD2 1 ATOM 4148 N N . PRO A 1 575 ? 31.249 32.950 57.194 1.00 30.72 ? 568 PRO A N 1 ATOM 4149 C CA . PRO A 1 575 ? 31.160 31.661 57.895 1.00 31.77 ? 568 PRO A CA 1 ATOM 4150 C C . PRO A 1 575 ? 30.661 31.756 59.343 1.00 32.58 ? 568 PRO A C 1 ATOM 4151 O O . PRO A 1 575 ? 29.922 30.861 59.807 1.00 33.06 ? 568 PRO A O 1 ATOM 4152 C CB . PRO A 1 575 ? 32.598 31.112 57.866 1.00 33.64 ? 568 PRO A CB 1 ATOM 4153 C CG . PRO A 1 575 ? 33.341 31.909 56.890 1.00 34.05 ? 568 PRO A CG 1 ATOM 4154 C CD . PRO A 1 575 ? 32.586 33.192 56.619 1.00 30.70 ? 568 PRO A CD 1 ATOM 4155 N N . MET A 1 576 ? 31.045 32.822 60.036 1.00 32.89 ? 569 MET A N 1 ATOM 4156 C CA A MET A 1 576 ? 30.689 32.957 61.453 0.50 33.61 ? 569 MET A CA 1 ATOM 4157 C CA B MET A 1 576 ? 30.720 33.011 61.455 0.50 33.92 ? 569 MET A CA 1 ATOM 4158 C C . MET A 1 576 ? 29.424 33.802 61.641 1.00 32.90 ? 569 MET A C 1 ATOM 4159 O O . MET A 1 576 ? 28.924 33.958 62.760 1.00 33.38 ? 569 MET A O 1 ATOM 4160 C CB A MET A 1 576 ? 31.869 33.504 62.266 0.50 34.90 ? 569 MET A CB 1 ATOM 4161 C CB B MET A 1 576 ? 31.868 33.735 62.157 0.50 35.41 ? 569 MET A CB 1 ATOM 4162 C CG A MET A 1 576 ? 33.075 32.556 62.330 0.50 37.17 ? 569 MET A CG 1 ATOM 4163 C CG B MET A 1 576 ? 33.250 33.165 61.849 0.50 38.54 ? 569 MET A CG 1 ATOM 4164 S SD A MET A 1 576 ? 32.605 30.882 62.795 0.50 40.56 ? 569 MET A SD 1 ATOM 4165 S SD B MET A 1 576 ? 34.428 33.554 63.145 0.50 47.36 ? 569 MET A SD 1 ATOM 4166 C CE A MET A 1 576 ? 32.394 31.041 64.569 0.50 41.30 ? 569 MET A CE 1 ATOM 4167 C CE B MET A 1 576 ? 35.254 35.031 62.531 0.50 43.75 ? 569 MET A CE 1 ATOM 4168 N N . PHE A 1 577 ? 28.896 34.312 60.536 1.00 30.56 ? 570 PHE A N 1 ATOM 4169 C CA . PHE A 1 577 ? 27.686 35.129 60.533 1.00 29.69 ? 570 PHE A CA 1 ATOM 4170 C C . PHE A 1 577 ? 27.849 36.374 61.382 1.00 29.06 ? 570 PHE A C 1 ATOM 4171 O O . PHE A 1 577 ? 26.876 36.964 61.821 1.00 28.97 ? 570 PHE A O 1 ATOM 4172 C CB . PHE A 1 577 ? 26.427 34.288 60.849 1.00 29.66 ? 570 PHE A CB 1 ATOM 4173 C CG . PHE A 1 577 ? 25.991 33.447 59.671 1.00 29.70 ? 570 PHE A CG 1 ATOM 4174 C CD1 . PHE A 1 577 ? 24.974 33.904 58.826 1.00 26.81 ? 570 PHE A CD1 1 ATOM 4175 C CD2 . PHE A 1 577 ? 26.673 32.244 59.346 1.00 29.84 ? 570 PHE A CD2 1 ATOM 4176 C CE1 . PHE A 1 577 ? 24.581 33.167 57.681 1.00 27.29 ? 570 PHE A CE1 1 ATOM 4177 C CE2 . PHE A 1 577 ? 26.290 31.514 58.172 1.00 30.76 ? 570 PHE A CE2 1 ATOM 4178 C CZ . PHE A 1 577 ? 25.225 31.979 57.363 1.00 27.90 ? 570 PHE A CZ 1 ATOM 4179 N N . LYS A 1 578 ? 29.098 36.806 61.546 1.00 29.20 ? 571 LYS A N 1 ATOM 4180 C CA . LYS A 1 578 ? 29.362 38.047 62.278 1.00 29.99 ? 571 LYS A CA 1 ATOM 4181 C C . LYS A 1 578 ? 29.017 39.311 61.469 1.00 28.35 ? 571 LYS A C 1 ATOM 4182 O O . LYS A 1 578 ? 28.699 40.332 62.049 1.00 27.01 ? 571 LYS A O 1 ATOM 4183 C CB . LYS A 1 578 ? 30.799 38.093 62.796 1.00 30.79 ? 571 LYS A CB 1 ATOM 4184 C CG . LYS A 1 578 ? 31.849 38.105 61.700 1.00 31.81 ? 571 LYS A CG 1 ATOM 4185 C CD . LYS A 1 578 ? 33.265 38.086 62.283 1.00 36.46 ? 571 LYS A CD 1 ATOM 4186 C CE . LYS A 1 578 ? 34.254 38.274 61.144 1.00 36.92 ? 571 LYS A CE 1 ATOM 4187 N NZ . LYS A 1 578 ? 35.621 38.467 61.677 1.00 41.49 ? 571 LYS A NZ 1 ATOM 4188 N N . TYR A 1 579 ? 29.127 39.264 60.145 1.00 27.62 ? 572 TYR A N 1 ATOM 4189 C CA . TYR A 1 579 ? 28.751 40.439 59.385 1.00 26.58 ? 572 TYR A CA 1 ATOM 4190 C C . TYR A 1 579 ? 27.230 40.553 59.386 1.00 26.28 ? 572 TYR A C 1 ATOM 4191 O O . TYR A 1 579 ? 26.681 41.669 59.546 1.00 25.41 ? 572 TYR A O 1 ATOM 4192 C CB . TYR A 1 579 ? 29.362 40.431 57.963 1.00 27.01 ? 572 TYR A CB 1 ATOM 4193 C CG . TYR A 1 579 ? 30.865 40.374 58.032 1.00 29.93 ? 572 TYR A CG 1 ATOM 4194 C CD1 . TYR A 1 579 ? 31.587 41.415 58.632 1.00 31.58 ? 572 TYR A CD1 1 ATOM 4195 C CD2 . TYR A 1 579 ? 31.565 39.266 57.571 1.00 33.67 ? 572 TYR A CD2 1 ATOM 4196 C CE1 . TYR A 1 579 ? 32.943 41.368 58.740 1.00 34.67 ? 572 TYR A CE1 1 ATOM 4197 C CE2 . TYR A 1 579 ? 32.957 39.201 57.699 1.00 35.51 ? 572 TYR A CE2 1 ATOM 4198 C CZ . TYR A 1 579 ? 33.632 40.257 58.265 1.00 36.45 ? 572 TYR A CZ 1 ATOM 4199 O OH . TYR A 1 579 ? 35.003 40.192 58.382 1.00 39.86 ? 572 TYR A OH 1 ATOM 4200 N N . HIS A 1 580 ? 26.538 39.425 59.218 1.00 24.81 ? 573 HIS A N 1 ATOM 4201 C CA . HIS A 1 580 ? 25.063 39.446 59.336 1.00 24.66 ? 573 HIS A CA 1 ATOM 4202 C C . HIS A 1 580 ? 24.638 39.997 60.705 1.00 25.09 ? 573 HIS A C 1 ATOM 4203 O O . HIS A 1 580 ? 23.741 40.815 60.796 1.00 24.81 ? 573 HIS A O 1 ATOM 4204 C CB . HIS A 1 580 ? 24.494 38.048 59.230 1.00 24.50 ? 573 HIS A CB 1 ATOM 4205 C CG . HIS A 1 580 ? 24.461 37.506 57.836 1.00 25.37 ? 573 HIS A CG 1 ATOM 4206 N ND1 . HIS A 1 580 ? 25.595 37.049 57.196 1.00 26.01 ? 573 HIS A ND1 1 ATOM 4207 C CD2 . HIS A 1 580 ? 23.429 37.300 56.982 1.00 26.15 ? 573 HIS A CD2 1 ATOM 4208 C CE1 . HIS A 1 580 ? 25.260 36.586 55.999 1.00 29.85 ? 573 HIS A CE1 1 ATOM 4209 N NE2 . HIS A 1 580 ? 23.951 36.717 55.849 1.00 28.31 ? 573 HIS A NE2 1 ATOM 4210 N N . LEU A 1 581 ? 25.278 39.516 61.772 1.00 25.83 ? 574 LEU A N 1 ATOM 4211 C CA . LEU A 1 581 ? 24.955 40.041 63.095 1.00 26.62 ? 574 LEU A CA 1 ATOM 4212 C C . LEU A 1 581 ? 25.189 41.556 63.198 1.00 26.80 ? 574 LEU A C 1 ATOM 4213 O O . LEU A 1 581 ? 24.328 42.268 63.700 1.00 26.58 ? 574 LEU A O 1 ATOM 4214 C CB . LEU A 1 581 ? 25.737 39.277 64.204 1.00 27.59 ? 574 LEU A CB 1 ATOM 4215 C CG . LEU A 1 581 ? 25.430 39.738 65.657 1.00 28.14 ? 574 LEU A CG 1 ATOM 4216 C CD1 . LEU A 1 581 ? 23.917 39.566 65.945 1.00 28.54 ? 574 LEU A CD1 1 ATOM 4217 C CD2 . LEU A 1 581 ? 26.265 38.904 66.664 1.00 26.98 ? 574 LEU A CD2 1 ATOM 4218 N N . THR A 1 582 ? 26.324 42.061 62.710 1.00 27.21 ? 575 THR A N 1 ATOM 4219 C CA . THR A 1 582 ? 26.596 43.523 62.737 1.00 26.12 ? 575 THR A CA 1 ATOM 4220 C C . THR A 1 582 ? 25.493 44.285 62.002 1.00 25.76 ? 575 THR A C 1 ATOM 4221 O O . THR A 1 582 ? 24.977 45.309 62.476 1.00 24.25 ? 575 THR A O 1 ATOM 4222 C CB . THR A 1 582 ? 28.023 43.792 62.188 1.00 27.09 ? 575 THR A CB 1 ATOM 4223 O OG1 . THR A 1 582 ? 28.983 43.274 63.142 1.00 27.85 ? 575 THR A OG1 1 ATOM 4224 C CG2 . THR A 1 582 ? 28.299 45.279 61.921 1.00 26.82 ? 575 THR A CG2 1 ATOM 4225 N N . VAL A 1 583 ? 25.068 43.745 60.877 1.00 24.98 ? 576 VAL A N 1 ATOM 4226 C CA . VAL A 1 583 ? 24.033 44.422 60.095 1.00 24.05 ? 576 VAL A CA 1 ATOM 4227 C C . VAL A 1 583 ? 22.650 44.338 60.779 1.00 23.94 ? 576 VAL A C 1 ATOM 4228 O O . VAL A 1 583 ? 21.851 45.294 60.698 1.00 24.06 ? 576 VAL A O 1 ATOM 4229 C CB . VAL A 1 583 ? 24.019 43.898 58.618 1.00 23.45 ? 576 VAL A CB 1 ATOM 4230 C CG1 . VAL A 1 583 ? 22.766 44.416 57.827 1.00 21.48 ? 576 VAL A CG1 1 ATOM 4231 C CG2 . VAL A 1 583 ? 25.302 44.300 57.882 1.00 24.51 ? 576 VAL A CG2 1 ATOM 4232 N N . ALA A 1 584 ? 22.369 43.226 61.464 1.00 24.15 ? 577 ALA A N 1 ATOM 4233 C CA . ALA A 1 584 ? 21.157 43.165 62.289 1.00 23.05 ? 577 ALA A CA 1 ATOM 4234 C C . ALA A 1 584 ? 21.229 44.214 63.409 1.00 23.60 ? 577 ALA A C 1 ATOM 4235 O O . ALA A 1 584 ? 20.272 44.922 63.666 1.00 22.52 ? 577 ALA A O 1 ATOM 4236 C CB . ALA A 1 584 ? 20.971 41.750 62.854 1.00 23.12 ? 577 ALA A CB 1 ATOM 4237 N N . GLN A 1 585 ? 22.387 44.365 64.040 1.00 23.98 ? 578 GLN A N 1 ATOM 4238 C CA . GLN A 1 585 ? 22.507 45.445 65.043 1.00 24.58 ? 578 GLN A CA 1 ATOM 4239 C C . GLN A 1 585 ? 22.311 46.874 64.487 1.00 24.34 ? 578 GLN A C 1 ATOM 4240 O O . GLN A 1 585 ? 21.691 47.720 65.149 1.00 25.03 ? 578 GLN A O 1 ATOM 4241 C CB . GLN A 1 585 ? 23.862 45.342 65.771 1.00 25.78 ? 578 GLN A CB 1 ATOM 4242 C CG . GLN A 1 585 ? 24.037 44.010 66.508 1.00 26.84 ? 578 GLN A CG 1 ATOM 4243 C CD . GLN A 1 585 ? 25.424 43.828 67.109 1.00 30.88 ? 578 GLN A CD 1 ATOM 4244 O OE1 . GLN A 1 585 ? 26.337 44.610 66.845 1.00 31.08 ? 578 GLN A OE1 1 ATOM 4245 N NE2 . GLN A 1 585 ? 25.599 42.760 67.902 1.00 32.89 ? 578 GLN A NE2 1 ATOM 4246 N N . VAL A 1 586 ? 22.832 47.147 63.292 1.00 23.55 ? 579 VAL A N 1 ATOM 4247 C CA . VAL A 1 586 ? 22.682 48.458 62.687 1.00 22.71 ? 579 VAL A CA 1 ATOM 4248 C C . VAL A 1 586 ? 21.189 48.662 62.300 1.00 22.44 ? 579 VAL A C 1 ATOM 4249 O O . VAL A 1 586 ? 20.578 49.627 62.720 1.00 22.57 ? 579 VAL A O 1 ATOM 4250 C CB . VAL A 1 586 ? 23.576 48.673 61.467 1.00 23.28 ? 579 VAL A CB 1 ATOM 4251 C CG1 . VAL A 1 586 ? 23.250 50.057 60.832 1.00 21.57 ? 579 VAL A CG1 1 ATOM 4252 C CG2 . VAL A 1 586 ? 25.118 48.629 61.835 1.00 22.46 ? 579 VAL A CG2 1 ATOM 4253 N N . ARG A 1 587 ? 20.612 47.761 61.511 1.00 21.57 ? 580 ARG A N 1 ATOM 4254 C CA . ARG A 1 587 ? 19.219 47.941 61.100 1.00 21.60 ? 580 ARG A CA 1 ATOM 4255 C C . ARG A 1 587 ? 18.276 47.939 62.312 1.00 22.50 ? 580 ARG A C 1 ATOM 4256 O O . ARG A 1 587 ? 17.390 48.801 62.436 1.00 22.63 ? 580 ARG A O 1 ATOM 4257 C CB . ARG A 1 587 ? 18.802 46.851 60.115 1.00 20.81 ? 580 ARG A CB 1 ATOM 4258 C CG . ARG A 1 587 ? 19.536 46.921 58.786 1.00 20.60 ? 580 ARG A CG 1 ATOM 4259 C CD . ARG A 1 587 ? 19.219 45.706 57.926 1.00 19.71 ? 580 ARG A CD 1 ATOM 4260 N NE . ARG A 1 587 ? 19.941 45.781 56.664 1.00 19.29 ? 580 ARG A NE 1 ATOM 4261 C CZ . ARG A 1 587 ? 19.855 44.863 55.694 1.00 21.80 ? 580 ARG A CZ 1 ATOM 4262 N NH1 . ARG A 1 587 ? 19.109 43.780 55.862 1.00 20.53 ? 580 ARG A NH1 1 ATOM 4263 N NH2 . ARG A 1 587 ? 20.517 45.050 54.556 1.00 18.01 ? 580 ARG A NH2 1 ATOM 4264 N N . GLY A 1 588 ? 18.439 46.947 63.186 1.00 22.51 ? 581 GLY A N 1 ATOM 4265 C CA . GLY A 1 588 ? 17.558 46.812 64.332 1.00 22.96 ? 581 GLY A CA 1 ATOM 4266 C C . GLY A 1 588 ? 17.766 47.970 65.316 1.00 23.22 ? 581 GLY A C 1 ATOM 4267 O O . GLY A 1 588 ? 16.794 48.529 65.866 1.00 22.08 ? 581 GLY A O 1 ATOM 4268 N N . GLY A 1 589 ? 19.027 48.381 65.481 1.00 23.18 ? 582 GLY A N 1 ATOM 4269 C CA . GLY A 1 589 ? 19.330 49.532 66.328 1.00 24.57 ? 582 GLY A CA 1 ATOM 4270 C C . GLY A 1 589 ? 18.717 50.828 65.845 1.00 24.41 ? 582 GLY A C 1 ATOM 4271 O O . GLY A 1 589 ? 18.182 51.643 66.673 1.00 24.01 ? 582 GLY A O 1 ATOM 4272 N N . MET A 1 590 ? 18.805 51.056 64.537 1.00 23.75 ? 583 MET A N 1 ATOM 4273 C CA . MET A 1 590 ? 18.153 52.236 63.933 1.00 22.41 ? 583 MET A CA 1 ATOM 4274 C C . MET A 1 590 ? 16.655 52.193 64.184 1.00 22.22 ? 583 MET A C 1 ATOM 4275 O O . MET A 1 590 ? 16.079 53.179 64.645 1.00 21.32 ? 583 MET A O 1 ATOM 4276 C CB . MET A 1 590 ? 18.439 52.346 62.426 1.00 22.93 ? 583 MET A CB 1 ATOM 4277 C CG . MET A 1 590 ? 19.878 52.702 62.143 1.00 25.07 ? 583 MET A CG 1 ATOM 4278 S SD . MET A 1 590 ? 20.241 52.689 60.362 1.00 26.21 ? 583 MET A SD 1 ATOM 4279 C CE . MET A 1 590 ? 19.487 54.237 59.811 1.00 22.90 ? 583 MET A CE 1 ATOM 4280 N N . VAL A 1 591 ? 16.022 51.045 63.938 1.00 20.81 ? 584 VAL A N 1 ATOM 4281 C CA . VAL A 1 591 ? 14.561 50.937 64.152 1.00 21.35 ? 584 VAL A CA 1 ATOM 4282 C C . VAL A 1 591 ? 14.218 51.208 65.626 1.00 23.22 ? 584 VAL A C 1 ATOM 4283 O O . VAL A 1 591 ? 13.248 51.935 65.917 1.00 22.11 ? 584 VAL A O 1 ATOM 4284 C CB . VAL A 1 591 ? 14.062 49.506 63.733 1.00 21.81 ? 584 VAL A CB 1 ATOM 4285 C CG1 . VAL A 1 591 ? 12.633 49.209 64.253 1.00 18.61 ? 584 VAL A CG1 1 ATOM 4286 C CG2 . VAL A 1 591 ? 14.141 49.349 62.229 1.00 22.18 ? 584 VAL A CG2 1 ATOM 4287 N N . PHE A 1 592 ? 14.993 50.597 66.539 1.00 22.80 ? 585 PHE A N 1 ATOM 4288 C CA . PHE A 1 592 ? 14.813 50.789 67.984 1.00 24.52 ? 585 PHE A CA 1 ATOM 4289 C C . PHE A 1 592 ? 14.852 52.285 68.366 1.00 24.83 ? 585 PHE A C 1 ATOM 4290 O O . PHE A 1 592 ? 13.971 52.767 69.094 1.00 25.14 ? 585 PHE A O 1 ATOM 4291 C CB . PHE A 1 592 ? 15.901 50.029 68.796 1.00 26.19 ? 585 PHE A CB 1 ATOM 4292 C CG . PHE A 1 592 ? 15.578 49.947 70.280 1.00 27.47 ? 585 PHE A CG 1 ATOM 4293 C CD1 . PHE A 1 592 ? 15.061 48.778 70.806 1.00 26.84 ? 585 PHE A CD1 1 ATOM 4294 C CD2 . PHE A 1 592 ? 15.703 51.069 71.100 1.00 28.83 ? 585 PHE A CD2 1 ATOM 4295 C CE1 . PHE A 1 592 ? 14.691 48.693 72.164 1.00 28.83 ? 585 PHE A CE1 1 ATOM 4296 C CE2 . PHE A 1 592 ? 15.348 51.007 72.492 1.00 29.09 ? 585 PHE A CE2 1 ATOM 4297 C CZ . PHE A 1 592 ? 14.844 49.811 73.008 1.00 30.02 ? 585 PHE A CZ 1 ATOM 4298 N N . GLU A 1 593 ? 15.889 53.018 67.947 1.00 24.43 ? 586 GLU A N 1 ATOM 4299 C CA A GLU A 1 593 ? 16.011 54.459 68.274 0.50 25.01 ? 586 GLU A CA 1 ATOM 4300 C CA B GLU A 1 593 ? 15.960 54.429 68.355 0.50 24.75 ? 586 GLU A CA 1 ATOM 4301 C C . GLU A 1 593 ? 14.833 55.243 67.719 1.00 23.87 ? 586 GLU A C 1 ATOM 4302 O O . GLU A 1 593 ? 14.246 56.109 68.387 1.00 24.41 ? 586 GLU A O 1 ATOM 4303 C CB A GLU A 1 593 ? 17.291 55.028 67.677 0.50 25.70 ? 586 GLU A CB 1 ATOM 4304 C CB B GLU A 1 593 ? 17.314 55.038 68.048 0.50 25.49 ? 586 GLU A CB 1 ATOM 4305 C CG A GLU A 1 593 ? 18.548 54.592 68.404 0.50 28.46 ? 586 GLU A CG 1 ATOM 4306 C CG B GLU A 1 593 ? 17.572 56.349 68.747 0.50 26.38 ? 586 GLU A CG 1 ATOM 4307 C CD A GLU A 1 593 ? 18.643 55.206 69.787 0.50 33.98 ? 586 GLU A CD 1 ATOM 4308 C CD B GLU A 1 593 ? 17.929 56.216 70.229 0.50 30.89 ? 586 GLU A CD 1 ATOM 4309 O OE1 A GLU A 1 593 ? 19.705 55.068 70.416 0.50 36.58 ? 586 GLU A OE1 1 ATOM 4310 O OE1 B GLU A 1 593 ? 18.044 55.082 70.779 0.50 30.91 ? 586 GLU A OE1 1 ATOM 4311 O OE2 A GLU A 1 593 ? 17.655 55.816 70.252 0.50 35.87 ? 586 GLU A OE2 1 ATOM 4312 O OE2 B GLU A 1 593 ? 18.083 57.286 70.851 0.50 34.97 ? 586 GLU A OE2 1 ATOM 4313 N N . LEU A 1 594 ? 14.504 54.942 66.468 1.00 22.78 ? 587 LEU A N 1 ATOM 4314 C CA . LEU A 1 594 ? 13.437 55.664 65.769 1.00 22.35 ? 587 LEU A CA 1 ATOM 4315 C C . LEU A 1 594 ? 12.088 55.422 66.448 1.00 22.91 ? 587 LEU A C 1 ATOM 4316 O O . LEU A 1 594 ? 11.249 56.351 66.541 1.00 22.17 ? 587 LEU A O 1 ATOM 4317 C CB . LEU A 1 594 ? 13.362 55.225 64.293 1.00 23.02 ? 587 LEU A CB 1 ATOM 4318 C CG . LEU A 1 594 ? 14.535 55.718 63.424 1.00 22.80 ? 587 LEU A CG 1 ATOM 4319 C CD1 . LEU A 1 594 ? 14.648 54.788 62.165 1.00 19.98 ? 587 LEU A CD1 1 ATOM 4320 C CD2 . LEU A 1 594 ? 14.197 57.149 63.009 1.00 24.33 ? 587 LEU A CD2 1 ATOM 4321 N N . ALA A 1 595 ? 11.884 54.181 66.910 1.00 21.96 ? 588 ALA A N 1 ATOM 4322 C CA . ALA A 1 595 ? 10.618 53.815 67.547 1.00 23.47 ? 588 ALA A CA 1 ATOM 4323 C C . ALA A 1 595 ? 10.557 54.154 69.039 1.00 24.22 ? 588 ALA A C 1 ATOM 4324 O O . ALA A 1 595 ? 9.463 54.150 69.600 1.00 24.65 ? 588 ALA A O 1 ATOM 4325 C CB . ALA A 1 595 ? 10.307 52.322 67.309 1.00 21.95 ? 588 ALA A CB 1 ATOM 4326 N N . ASN A 1 596 ? 11.708 54.403 69.681 1.00 25.06 ? 589 ASN A N 1 ATOM 4327 C CA . ASN A 1 596 ? 11.696 54.583 71.143 1.00 26.41 ? 589 ASN A CA 1 ATOM 4328 C C . ASN A 1 596 ? 12.201 55.907 71.669 1.00 27.86 ? 589 ASN A C 1 ATOM 4329 O O . ASN A 1 596 ? 11.887 56.293 72.823 1.00 29.12 ? 589 ASN A O 1 ATOM 4330 C CB . ASN A 1 596 ? 12.452 53.409 71.842 1.00 26.76 ? 589 ASN A CB 1 ATOM 4331 C CG A ASN A 1 596 ? 11.848 53.030 73.159 0.50 28.65 ? 589 ASN A CG 1 ATOM 4332 C CG B ASN A 1 596 ? 11.683 52.128 71.706 0.50 26.73 ? 589 ASN A CG 1 ATOM 4333 O OD1 A ASN A 1 596 ? 10.650 52.745 73.245 0.50 31.98 ? 589 ASN A OD1 1 ATOM 4334 O OD1 B ASN A 1 596 ? 11.983 51.293 70.847 0.50 30.99 ? 589 ASN A OD1 1 ATOM 4335 N ND2 A ASN A 1 596 ? 12.668 53.013 74.203 0.50 31.40 ? 589 ASN A ND2 1 ATOM 4336 N ND2 B ASN A 1 596 ? 10.610 52.015 72.456 0.50 24.30 ? 589 ASN A ND2 1 ATOM 4337 N N . SER A 1 597 ? 13.005 56.606 70.872 1.00 26.17 ? 590 SER A N 1 ATOM 4338 C CA . SER A 1 597 ? 13.598 57.849 71.391 1.00 26.91 ? 590 SER A CA 1 ATOM 4339 C C . SER A 1 597 ? 12.474 58.865 71.648 1.00 26.61 ? 590 SER A C 1 ATOM 4340 O O . SER A 1 597 ? 11.499 58.965 70.863 1.00 24.57 ? 590 SER A O 1 ATOM 4341 C CB . SER A 1 597 ? 14.659 58.401 70.417 1.00 28.20 ? 590 SER A CB 1 ATOM 4342 O OG . SER A 1 597 ? 15.157 59.658 70.861 1.00 29.52 ? 590 SER A OG 1 ATOM 4343 N N . ILE A 1 598 ? 12.558 59.597 72.757 1.00 25.92 ? 591 ILE A N 1 ATOM 4344 C CA . ILE A 1 598 ? 11.469 60.534 73.061 1.00 26.14 ? 591 ILE A CA 1 ATOM 4345 C C . ILE A 1 598 ? 11.345 61.615 72.002 1.00 25.47 ? 591 ILE A C 1 ATOM 4346 O O . ILE A 1 598 ? 10.238 61.882 71.448 1.00 24.13 ? 591 ILE A O 1 ATOM 4347 C CB . ILE A 1 598 ? 11.679 61.167 74.472 1.00 26.83 ? 591 ILE A CB 1 ATOM 4348 C CG1 A ILE A 1 598 ? 11.312 60.159 75.556 0.50 29.87 ? 591 ILE A CG1 1 ATOM 4349 C CG1 B ILE A 1 598 ? 11.799 60.060 75.530 0.50 30.21 ? 591 ILE A CG1 1 ATOM 4350 C CG2 A ILE A 1 598 ? 10.844 62.412 74.630 0.50 28.58 ? 591 ILE A CG2 1 ATOM 4351 C CG2 B ILE A 1 598 ? 10.489 61.988 74.833 0.50 28.75 ? 591 ILE A CG2 1 ATOM 4352 C CD1 A ILE A 1 598 ? 11.732 60.602 76.919 0.50 28.37 ? 591 ILE A CD1 1 ATOM 4353 C CD1 B ILE A 1 598 ? 10.583 59.124 75.583 0.50 30.40 ? 591 ILE A CD1 1 ATOM 4354 N N . VAL A 1 599 ? 12.482 62.226 71.707 1.00 25.84 ? 592 VAL A N 1 ATOM 4355 C CA . VAL A 1 599 ? 12.575 63.137 70.567 1.00 25.75 ? 592 VAL A CA 1 ATOM 4356 C C . VAL A 1 599 ? 13.054 62.315 69.365 1.00 25.76 ? 592 VAL A C 1 ATOM 4357 O O . VAL A 1 599 ? 14.039 61.600 69.466 1.00 26.26 ? 592 VAL A O 1 ATOM 4358 C CB . VAL A 1 599 ? 13.521 64.307 70.867 1.00 26.95 ? 592 VAL A CB 1 ATOM 4359 C CG1 . VAL A 1 599 ? 13.718 65.237 69.624 1.00 26.48 ? 592 VAL A CG1 1 ATOM 4360 C CG2 . VAL A 1 599 ? 12.980 65.129 72.079 1.00 28.57 ? 592 VAL A CG2 1 ATOM 4361 N N . LEU A 1 600 ? 12.347 62.405 68.233 1.00 25.02 ? 593 LEU A N 1 ATOM 4362 C CA . LEU A 1 600 ? 12.780 61.700 66.982 1.00 23.66 ? 593 LEU A CA 1 ATOM 4363 C C . LEU A 1 600 ? 14.274 61.987 66.742 1.00 24.02 ? 593 LEU A C 1 ATOM 4364 O O . LEU A 1 600 ? 14.701 63.142 66.878 1.00 24.73 ? 593 LEU A O 1 ATOM 4365 C CB . LEU A 1 600 ? 11.919 62.120 65.787 1.00 24.31 ? 593 LEU A CB 1 ATOM 4366 C CG . LEU A 1 600 ? 10.532 61.463 65.759 1.00 24.79 ? 593 LEU A CG 1 ATOM 4367 C CD1 . LEU A 1 600 ? 9.688 62.019 64.605 1.00 24.40 ? 593 LEU A CD1 1 ATOM 4368 C CD2 . LEU A 1 600 ? 10.708 59.917 65.638 1.00 24.51 ? 593 LEU A CD2 1 ATOM 4369 N N . PRO A 1 601 ? 15.077 60.939 66.430 1.00 23.04 ? 594 PRO A N 1 ATOM 4370 C CA . PRO A 1 601 ? 16.553 61.103 66.296 1.00 24.11 ? 594 PRO A CA 1 ATOM 4371 C C . PRO A 1 601 ? 16.971 61.603 64.865 1.00 23.43 ? 594 PRO A C 1 ATOM 4372 O O . PRO A 1 601 ? 17.741 60.912 64.153 1.00 24.52 ? 594 PRO A O 1 ATOM 4373 C CB . PRO A 1 601 ? 17.079 59.689 66.497 1.00 24.19 ? 594 PRO A CB 1 ATOM 4374 C CG . PRO A 1 601 ? 15.961 58.774 65.978 1.00 22.86 ? 594 PRO A CG 1 ATOM 4375 C CD . PRO A 1 601 ? 14.659 59.531 66.341 1.00 21.82 ? 594 PRO A CD 1 ATOM 4376 N N . PHE A 1 602 ? 16.442 62.755 64.476 1.00 23.38 ? 595 PHE A N 1 ATOM 4377 C CA . PHE A 1 602 ? 16.665 63.394 63.150 1.00 22.73 ? 595 PHE A CA 1 ATOM 4378 C C . PHE A 1 602 ? 17.364 64.706 63.454 1.00 24.52 ? 595 PHE A C 1 ATOM 4379 O O . PHE A 1 602 ? 16.946 65.445 64.379 1.00 26.18 ? 595 PHE A O 1 ATOM 4380 C CB . PHE A 1 602 ? 15.331 63.723 62.449 1.00 22.36 ? 595 PHE A CB 1 ATOM 4381 C CG . PHE A 1 602 ? 14.563 62.522 61.958 1.00 20.53 ? 595 PHE A CG 1 ATOM 4382 C CD1 . PHE A 1 602 ? 15.198 61.327 61.631 1.00 21.69 ? 595 PHE A CD1 1 ATOM 4383 C CD2 . PHE A 1 602 ? 13.188 62.639 61.730 1.00 22.35 ? 595 PHE A CD2 1 ATOM 4384 C CE1 . PHE A 1 602 ? 14.459 60.238 61.133 1.00 24.98 ? 595 PHE A CE1 1 ATOM 4385 C CE2 . PHE A 1 602 ? 12.442 61.565 61.238 1.00 23.79 ? 595 PHE A CE2 1 ATOM 4386 C CZ . PHE A 1 602 ? 13.047 60.383 60.931 1.00 21.38 ? 595 PHE A CZ 1 ATOM 4387 N N . ASP A 1 603 ? 18.428 65.018 62.730 1.00 24.23 ? 596 ASP A N 1 ATOM 4388 C CA . ASP A 1 603 ? 19.075 66.326 62.909 1.00 24.21 ? 596 ASP A CA 1 ATOM 4389 C C . ASP A 1 603 ? 18.914 67.152 61.624 1.00 24.15 ? 596 ASP A C 1 ATOM 4390 O O . ASP A 1 603 ? 19.611 66.897 60.619 1.00 24.22 ? 596 ASP A O 1 ATOM 4391 C CB . ASP A 1 603 ? 20.558 66.163 63.240 1.00 24.66 ? 596 ASP A CB 1 ATOM 4392 C CG . ASP A 1 603 ? 21.180 67.457 63.716 1.00 27.26 ? 596 ASP A CG 1 ATOM 4393 O OD1 . ASP A 1 603 ? 20.580 68.548 63.509 1.00 25.75 ? 596 ASP A OD1 1 ATOM 4394 O OD2 . ASP A 1 603 ? 22.252 67.411 64.341 1.00 31.02 ? 596 ASP A OD2 1 ATOM 4395 N N . CYS A 1 604 ? 17.945 68.064 61.622 1.00 23.63 ? 597 CYS A N 1 ATOM 4396 C CA . CYS A 1 604 ? 17.740 68.943 60.473 1.00 24.04 ? 597 CYS A CA 1 ATOM 4397 C C . CYS A 1 604 ? 18.979 69.699 60.011 1.00 24.31 ? 597 CYS A C 1 ATOM 4398 O O . CYS A 1 604 ? 19.059 70.037 58.822 1.00 24.72 ? 597 CYS A O 1 ATOM 4399 C CB . CYS A 1 604 ? 16.606 69.947 60.743 1.00 24.15 ? 597 CYS A CB 1 ATOM 4400 S SG . CYS A 1 604 ? 16.909 71.052 62.177 1.00 29.36 ? 597 CYS A SG 1 ATOM 4401 N N . ARG A 1 605 ? 19.922 69.989 60.914 1.00 24.23 ? 598 ARG A N 1 ATOM 4402 C CA . ARG A 1 605 ? 21.153 70.689 60.504 1.00 25.05 ? 598 ARG A CA 1 ATOM 4403 C C . ARG A 1 605 ? 21.961 69.899 59.455 1.00 25.14 ? 598 ARG A C 1 ATOM 4404 O O . ARG A 1 605 ? 22.599 70.495 58.578 1.00 25.18 ? 598 ARG A O 1 ATOM 4405 C CB . ARG A 1 605 ? 22.022 71.058 61.714 1.00 25.57 ? 598 ARG A CB 1 ATOM 4406 C CG . ARG A 1 605 ? 21.293 72.066 62.659 1.00 26.94 ? 598 ARG A CG 1 ATOM 4407 C CD . ARG A 1 605 ? 22.072 72.180 64.040 1.00 27.94 ? 598 ARG A CD 1 ATOM 4408 N NE . ARG A 1 605 ? 22.127 70.874 64.710 1.00 30.45 ? 598 ARG A NE 1 ATOM 4409 C CZ . ARG A 1 605 ? 22.774 70.648 65.855 1.00 36.11 ? 598 ARG A CZ 1 ATOM 4410 N NH1 . ARG A 1 605 ? 23.380 71.656 66.467 1.00 34.69 ? 598 ARG A NH1 1 ATOM 4411 N NH2 . ARG A 1 605 ? 22.807 69.424 66.388 1.00 31.60 ? 598 ARG A NH2 1 ATOM 4412 N N . ASP A 1 606 ? 21.934 68.568 59.531 1.00 24.08 ? 599 ASP A N 1 ATOM 4413 C CA . ASP A 1 606 ? 22.627 67.757 58.507 1.00 24.25 ? 599 ASP A CA 1 ATOM 4414 C C . ASP A 1 606 ? 22.023 67.949 57.109 1.00 23.84 ? 599 ASP A C 1 ATOM 4415 O O . ASP A 1 606 ? 22.747 67.917 56.091 1.00 23.77 ? 599 ASP A O 1 ATOM 4416 C CB . ASP A 1 606 ? 22.657 66.269 58.904 1.00 24.12 ? 599 ASP A CB 1 ATOM 4417 C CG . ASP A 1 606 ? 23.586 66.023 60.108 1.00 28.68 ? 599 ASP A CG 1 ATOM 4418 O OD1 . ASP A 1 606 ? 24.575 66.746 60.204 1.00 35.08 ? 599 ASP A OD1 1 ATOM 4419 O OD2 . ASP A 1 606 ? 23.307 65.183 60.978 1.00 29.55 ? 599 ASP A OD2 1 ATOM 4420 N N . TYR A 1 607 ? 20.711 68.187 57.051 1.00 22.40 ? 600 TYR A N 1 ATOM 4421 C CA . TYR A 1 607 ? 20.100 68.509 55.759 1.00 22.03 ? 600 TYR A CA 1 ATOM 4422 C C . TYR A 1 607 ? 20.641 69.840 55.236 1.00 22.28 ? 600 TYR A C 1 ATOM 4423 O O . TYR A 1 607 ? 20.932 69.973 54.046 1.00 22.45 ? 600 TYR A O 1 ATOM 4424 C CB . TYR A 1 607 ? 18.577 68.538 55.828 1.00 20.65 ? 600 TYR A CB 1 ATOM 4425 C CG . TYR A 1 607 ? 17.926 67.566 54.842 1.00 21.17 ? 600 TYR A CG 1 ATOM 4426 C CD1 . TYR A 1 607 ? 18.234 67.625 53.479 1.00 21.05 ? 600 TYR A CD1 1 ATOM 4427 C CD2 . TYR A 1 607 ? 16.956 66.638 55.267 1.00 20.49 ? 600 TYR A CD2 1 ATOM 4428 C CE1 . TYR A 1 607 ? 17.624 66.761 52.540 1.00 21.19 ? 600 TYR A CE1 1 ATOM 4429 C CE2 . TYR A 1 607 ? 16.339 65.751 54.348 1.00 22.45 ? 600 TYR A CE2 1 ATOM 4430 C CZ . TYR A 1 607 ? 16.682 65.837 52.977 1.00 22.89 ? 600 TYR A CZ 1 ATOM 4431 O OH . TYR A 1 607 ? 16.095 64.985 52.064 1.00 23.49 ? 600 TYR A OH 1 ATOM 4432 N N . ALA A 1 608 ? 20.792 70.825 56.115 1.00 22.56 ? 601 ALA A N 1 ATOM 4433 C CA . ALA A 1 608 ? 21.265 72.149 55.680 1.00 22.71 ? 601 ALA A CA 1 ATOM 4434 C C . ALA A 1 608 ? 22.669 72.044 55.064 1.00 23.66 ? 601 ALA A C 1 ATOM 4435 O O . ALA A 1 608 ? 22.958 72.640 54.017 1.00 23.74 ? 601 ALA A O 1 ATOM 4436 C CB . ALA A 1 608 ? 21.280 73.140 56.857 1.00 23.11 ? 601 ALA A CB 1 ATOM 4437 N N . VAL A 1 609 ? 23.530 71.276 55.714 1.00 24.18 ? 602 VAL A N 1 ATOM 4438 C CA . VAL A 1 609 ? 24.886 71.074 55.240 1.00 25.36 ? 602 VAL A CA 1 ATOM 4439 C C . VAL A 1 609 ? 24.891 70.422 53.810 1.00 25.82 ? 602 VAL A C 1 ATOM 4440 O O . VAL A 1 609 ? 25.583 70.937 52.898 1.00 26.13 ? 602 VAL A O 1 ATOM 4441 C CB . VAL A 1 609 ? 25.722 70.192 56.199 1.00 27.49 ? 602 VAL A CB 1 ATOM 4442 C CG1 . VAL A 1 609 ? 27.073 69.759 55.506 1.00 28.76 ? 602 VAL A CG1 1 ATOM 4443 C CG2 . VAL A 1 609 ? 26.089 70.992 57.480 1.00 30.50 ? 602 VAL A CG2 1 ATOM 4444 N N . VAL A 1 610 ? 24.105 69.362 53.597 1.00 23.45 ? 603 VAL A N 1 ATOM 4445 C CA . VAL A 1 610 ? 24.144 68.725 52.253 1.00 23.06 ? 603 VAL A CA 1 ATOM 4446 C C . VAL A 1 610 ? 23.465 69.592 51.180 1.00 22.76 ? 603 VAL A C 1 ATOM 4447 O O . VAL A 1 610 ? 23.896 69.577 50.037 1.00 22.40 ? 603 VAL A O 1 ATOM 4448 C CB . VAL A 1 610 ? 23.681 67.245 52.180 1.00 22.98 ? 603 VAL A CB 1 ATOM 4449 C CG1 . VAL A 1 610 ? 24.436 66.361 53.232 1.00 24.07 ? 603 VAL A CG1 1 ATOM 4450 C CG2 . VAL A 1 610 ? 22.232 67.154 52.369 1.00 25.12 ? 603 VAL A CG2 1 ATOM 4451 N N . LEU A 1 611 ? 22.419 70.326 51.552 1.00 21.29 ? 604 LEU A N 1 ATOM 4452 C CA . LEU A 1 611 ? 21.750 71.193 50.601 1.00 21.86 ? 604 LEU A CA 1 ATOM 4453 C C . LEU A 1 611 ? 22.732 72.210 50.020 1.00 23.11 ? 604 LEU A C 1 ATOM 4454 O O . LEU A 1 611 ? 22.647 72.519 48.828 1.00 23.21 ? 604 LEU A O 1 ATOM 4455 C CB . LEU A 1 611 ? 20.555 71.923 51.260 1.00 20.95 ? 604 LEU A CB 1 ATOM 4456 C CG . LEU A 1 611 ? 19.342 71.016 51.501 1.00 19.03 ? 604 LEU A CG 1 ATOM 4457 C CD1 . LEU A 1 611 ? 18.293 71.755 52.357 1.00 21.19 ? 604 LEU A CD1 1 ATOM 4458 C CD2 . LEU A 1 611 ? 18.712 70.521 50.167 1.00 19.64 ? 604 LEU A CD2 1 ATOM 4459 N N . ARG A 1 612 ? 23.671 72.705 50.845 1.00 24.05 ? 605 ARG A N 1 ATOM 4460 C CA . ARG A 1 612 ? 24.643 73.677 50.379 1.00 25.68 ? 605 ARG A CA 1 ATOM 4461 C C . ARG A 1 612 ? 25.600 72.989 49.405 1.00 25.61 ? 605 ARG A C 1 ATOM 4462 O O . ARG A 1 612 ? 25.911 73.535 48.336 1.00 25.78 ? 605 ARG A O 1 ATOM 4463 C CB . ARG A 1 612 ? 25.445 74.321 51.550 1.00 27.07 ? 605 ARG A CB 1 ATOM 4464 C CG . ARG A 1 612 ? 26.604 75.257 51.108 1.00 29.65 ? 605 ARG A CG 1 ATOM 4465 C CD . ARG A 1 612 ? 26.091 76.345 50.133 1.00 35.78 ? 605 ARG A CD 1 ATOM 4466 N NE . ARG A 1 612 ? 27.194 77.157 49.627 1.00 37.58 ? 605 ARG A NE 1 ATOM 4467 C CZ . ARG A 1 612 ? 27.592 78.289 50.194 1.00 42.87 ? 605 ARG A CZ 1 ATOM 4468 N NH1 . ARG A 1 612 ? 26.961 78.746 51.281 1.00 42.05 ? 605 ARG A NH1 1 ATOM 4469 N NH2 . ARG A 1 612 ? 28.621 78.951 49.686 1.00 43.42 ? 605 ARG A NH2 1 ATOM 4470 N N . LYS A 1 613 ? 26.073 71.805 49.776 1.00 24.85 ? 606 LYS A N 1 ATOM 4471 C CA A LYS A 1 613 ? 26.922 70.999 48.901 0.50 24.96 ? 606 LYS A CA 1 ATOM 4472 C CA B LYS A 1 613 ? 26.939 71.039 48.887 0.50 25.22 ? 606 LYS A CA 1 ATOM 4473 C C . LYS A 1 613 ? 26.226 70.750 47.535 1.00 24.07 ? 606 LYS A C 1 ATOM 4474 O O . LYS A 1 613 ? 26.818 70.918 46.469 1.00 24.46 ? 606 LYS A O 1 ATOM 4475 C CB A LYS A 1 613 ? 27.270 69.671 49.605 0.50 25.11 ? 606 LYS A CB 1 ATOM 4476 C CB B LYS A 1 613 ? 27.419 69.750 49.579 0.50 25.65 ? 606 LYS A CB 1 ATOM 4477 C CG A LYS A 1 613 ? 28.184 68.732 48.810 0.50 25.37 ? 606 LYS A CG 1 ATOM 4478 C CG B LYS A 1 613 ? 28.407 69.968 50.720 0.50 27.72 ? 606 LYS A CG 1 ATOM 4479 C CD A LYS A 1 613 ? 28.399 67.405 49.573 0.50 27.36 ? 606 LYS A CD 1 ATOM 4480 C CD B LYS A 1 613 ? 29.872 69.998 50.277 0.50 33.74 ? 606 LYS A CD 1 ATOM 4481 C CE A LYS A 1 613 ? 27.074 66.630 49.801 0.50 24.50 ? 606 LYS A CE 1 ATOM 4482 C CE B LYS A 1 613 ? 30.800 70.088 51.503 0.50 36.86 ? 606 LYS A CE 1 ATOM 4483 N NZ A LYS A 1 613 ? 27.305 65.312 50.437 0.50 22.51 ? 606 LYS A NZ 1 ATOM 4484 N NZ B LYS A 1 613 ? 29.945 69.793 52.706 0.50 35.94 ? 606 LYS A NZ 1 ATOM 4485 N N . TYR A 1 614 ? 24.958 70.367 47.564 1.00 21.96 ? 607 TYR A N 1 ATOM 4486 C CA . TYR A 1 614 ? 24.226 70.096 46.277 1.00 21.41 ? 607 TYR A CA 1 ATOM 4487 C C . TYR A 1 614 ? 23.990 71.375 45.467 1.00 20.12 ? 607 TYR A C 1 ATOM 4488 O O . TYR A 1 614 ? 23.997 71.326 44.248 1.00 22.21 ? 607 TYR A O 1 ATOM 4489 C CB . TYR A 1 614 ? 22.857 69.490 46.538 1.00 19.48 ? 607 TYR A CB 1 ATOM 4490 C CG . TYR A 1 614 ? 22.877 68.154 47.305 1.00 20.84 ? 607 TYR A CG 1 ATOM 4491 C CD1 . TYR A 1 614 ? 24.048 67.347 47.343 1.00 21.55 ? 607 TYR A CD1 1 ATOM 4492 C CD2 . TYR A 1 614 ? 21.759 67.733 47.993 1.00 22.03 ? 607 TYR A CD2 1 ATOM 4493 C CE1 . TYR A 1 614 ? 24.065 66.142 48.054 1.00 23.49 ? 607 TYR A CE1 1 ATOM 4494 C CE2 . TYR A 1 614 ? 21.753 66.526 48.707 1.00 21.49 ? 607 TYR A CE2 1 ATOM 4495 C CZ . TYR A 1 614 ? 22.918 65.739 48.725 1.00 25.98 ? 607 TYR A CZ 1 ATOM 4496 O OH . TYR A 1 614 ? 22.926 64.559 49.445 1.00 27.01 ? 607 TYR A OH 1 ATOM 4497 N N . ALA A 1 615 ? 23.770 72.497 46.135 1.00 19.63 ? 608 ALA A N 1 ATOM 4498 C CA . ALA A 1 615 ? 23.591 73.757 45.447 1.00 21.11 ? 608 ALA A CA 1 ATOM 4499 C C . ALA A 1 615 ? 24.870 74.171 44.734 1.00 23.36 ? 608 ALA A C 1 ATOM 4500 O O . ALA A 1 615 ? 24.849 74.600 43.564 1.00 23.18 ? 608 ALA A O 1 ATOM 4501 C CB . ALA A 1 615 ? 23.173 74.850 46.448 1.00 22.24 ? 608 ALA A CB 1 ATOM 4502 N N . ASP A 1 616 ? 25.994 74.087 45.450 1.00 24.25 ? 609 ASP A N 1 ATOM 4503 C CA . ASP A 1 616 ? 27.312 74.360 44.843 1.00 26.57 ? 609 ASP A CA 1 ATOM 4504 C C . ASP A 1 616 ? 27.555 73.463 43.604 1.00 26.48 ? 609 ASP A C 1 ATOM 4505 O O . ASP A 1 616 ? 28.069 73.920 42.560 1.00 26.84 ? 609 ASP A O 1 ATOM 4506 C CB . ASP A 1 616 ? 28.441 74.057 45.848 1.00 27.14 ? 609 ASP A CB 1 ATOM 4507 C CG . ASP A 1 616 ? 28.552 75.072 46.978 1.00 32.20 ? 609 ASP A CG 1 ATOM 4508 O OD1 . ASP A 1 616 ? 28.088 76.199 46.866 1.00 34.52 ? 609 ASP A OD1 1 ATOM 4509 O OD2 . ASP A 1 616 ? 29.185 74.728 47.999 1.00 38.14 ? 609 ASP A OD2 1 ATOM 4510 N N . LYS A 1 617 ? 27.228 72.181 43.751 1.00 24.30 ? 610 LYS A N 1 ATOM 4511 C CA . LYS A 1 617 ? 27.455 71.216 42.701 1.00 25.67 ? 610 LYS A CA 1 ATOM 4512 C C . LYS A 1 617 ? 26.618 71.530 41.431 1.00 25.28 ? 610 LYS A C 1 ATOM 4513 O O . LYS A 1 617 ? 27.138 71.534 40.304 1.00 24.85 ? 610 LYS A O 1 ATOM 4514 C CB . LYS A 1 617 ? 27.166 69.799 43.207 1.00 25.21 ? 610 LYS A CB 1 ATOM 4515 C CG . LYS A 1 617 ? 27.449 68.719 42.179 1.00 28.05 ? 610 LYS A CG 1 ATOM 4516 C CD . LYS A 1 617 ? 26.788 67.400 42.609 1.00 33.83 ? 610 LYS A CD 1 ATOM 4517 C CE . LYS A 1 617 ? 27.490 66.217 41.929 1.00 37.62 ? 610 LYS A CE 1 ATOM 4518 N NZ . LYS A 1 617 ? 26.848 64.914 42.326 1.00 36.37 ? 610 LYS A NZ 1 ATOM 4519 N N . ILE A 1 618 ? 25.334 71.810 41.622 1.00 24.60 ? 611 ILE A N 1 ATOM 4520 C CA . ILE A 1 618 ? 24.467 72.109 40.475 1.00 24.33 ? 611 ILE A CA 1 ATOM 4521 C C . ILE A 1 618 ? 24.816 73.457 39.805 1.00 25.55 ? 611 ILE A C 1 ATOM 4522 O O . ILE A 1 618 ? 24.838 73.567 38.571 1.00 25.57 ? 611 ILE A O 1 ATOM 4523 C CB . ILE A 1 618 ? 22.956 71.963 40.830 1.00 24.72 ? 611 ILE A CB 1 ATOM 4524 C CG1 . ILE A 1 618 ? 22.111 71.898 39.547 1.00 23.95 ? 611 ILE A CG1 1 ATOM 4525 C CG2 . ILE A 1 618 ? 22.460 73.132 41.758 1.00 23.87 ? 611 ILE A CG2 1 ATOM 4526 C CD1 . ILE A 1 618 ? 22.341 70.617 38.693 1.00 22.89 ? 611 ILE A CD1 1 ATOM 4527 N N . TYR A 1 619 ? 25.145 74.462 40.616 1.00 24.57 ? 612 TYR A N 1 ATOM 4528 C CA . TYR A 1 619 ? 25.640 75.723 40.090 1.00 26.35 ? 612 TYR A CA 1 ATOM 4529 C C . TYR A 1 619 ? 26.916 75.482 39.248 1.00 26.71 ? 612 TYR A C 1 ATOM 4530 O O . TYR A 1 619 ? 27.070 76.062 38.157 1.00 27.49 ? 612 TYR A O 1 ATOM 4531 C CB . TYR A 1 619 ? 25.898 76.716 41.239 1.00 27.06 ? 612 TYR A CB 1 ATOM 4532 C CG . TYR A 1 619 ? 26.832 77.833 40.840 1.00 29.76 ? 612 TYR A CG 1 ATOM 4533 C CD1 . TYR A 1 619 ? 26.346 78.978 40.220 1.00 33.02 ? 612 TYR A CD1 1 ATOM 4534 C CD2 . TYR A 1 619 ? 28.220 77.711 41.054 1.00 34.94 ? 612 TYR A CD2 1 ATOM 4535 C CE1 . TYR A 1 619 ? 27.211 80.017 39.852 1.00 38.40 ? 612 TYR A CE1 1 ATOM 4536 C CE2 . TYR A 1 619 ? 29.103 78.720 40.671 1.00 40.17 ? 612 TYR A CE2 1 ATOM 4537 C CZ . TYR A 1 619 ? 28.594 79.862 40.068 1.00 43.13 ? 612 TYR A CZ 1 ATOM 4538 O OH . TYR A 1 619 ? 29.467 80.851 39.703 1.00 51.66 ? 612 TYR A OH 1 ATOM 4539 N N . SER A 1 620 ? 27.803 74.612 39.725 1.00 27.39 ? 613 SER A N 1 ATOM 4540 C CA . SER A 1 620 ? 29.073 74.383 39.033 1.00 28.90 ? 613 SER A CA 1 ATOM 4541 C C . SER A 1 620 ? 28.844 73.712 37.668 1.00 29.15 ? 613 SER A C 1 ATOM 4542 O O . SER A 1 620 ? 29.550 74.016 36.702 1.00 30.23 ? 613 SER A O 1 ATOM 4543 C CB . SER A 1 620 ? 30.048 73.539 39.871 1.00 30.04 ? 613 SER A CB 1 ATOM 4544 O OG A SER A 1 620 ? 30.451 74.243 41.038 0.50 30.08 ? 613 SER A OG 1 ATOM 4545 O OG B SER A 1 620 ? 29.516 72.244 40.087 0.50 32.32 ? 613 SER A OG 1 ATOM 4546 N N . ILE A 1 621 ? 27.864 72.804 37.605 1.00 27.95 ? 614 ILE A N 1 ATOM 4547 C CA . ILE A 1 621 ? 27.454 72.210 36.330 1.00 27.14 ? 614 ILE A CA 1 ATOM 4548 C C . ILE A 1 621 ? 26.953 73.300 35.345 1.00 27.80 ? 614 ILE A C 1 ATOM 4549 O O . ILE A 1 621 ? 27.353 73.335 34.191 1.00 27.50 ? 614 ILE A O 1 ATOM 4550 C CB . ILE A 1 621 ? 26.369 71.118 36.557 1.00 26.76 ? 614 ILE A CB 1 ATOM 4551 C CG1 . ILE A 1 621 ? 26.998 69.887 37.243 1.00 26.65 ? 614 ILE A CG1 1 ATOM 4552 C CG2 . ILE A 1 621 ? 25.705 70.701 35.203 1.00 25.16 ? 614 ILE A CG2 1 ATOM 4553 C CD1 . ILE A 1 621 ? 25.920 68.899 37.798 1.00 28.10 ? 614 ILE A CD1 1 ATOM 4554 N N . SER A 1 622 ? 26.100 74.199 35.819 1.00 27.02 ? 615 SER A N 1 ATOM 4555 C CA . SER A 1 622 ? 25.542 75.253 34.973 1.00 27.46 ? 615 SER A CA 1 ATOM 4556 C C . SER A 1 622 ? 26.639 76.182 34.502 1.00 29.21 ? 615 SER A C 1 ATOM 4557 O O . SER A 1 622 ? 26.666 76.643 33.331 1.00 29.09 ? 615 SER A O 1 ATOM 4558 C CB . SER A 1 622 ? 24.471 76.037 35.750 1.00 26.59 ? 615 SER A CB 1 ATOM 4559 O OG . SER A 1 622 ? 23.812 76.961 34.902 1.00 26.34 ? 615 SER A OG 1 ATOM 4560 N N . MET A 1 623 ? 27.570 76.462 35.406 1.00 29.79 ? 616 MET A N 1 ATOM 4561 C CA . MET A 1 623 ? 28.656 77.386 35.085 1.00 32.03 ? 616 MET A CA 1 ATOM 4562 C C . MET A 1 623 ? 29.633 76.877 34.029 1.00 33.30 ? 616 MET A C 1 ATOM 4563 O O . MET A 1 623 ? 30.531 77.618 33.622 1.00 33.51 ? 616 MET A O 1 ATOM 4564 C CB . MET A 1 623 ? 29.378 77.853 36.336 1.00 32.28 ? 616 MET A CB 1 ATOM 4565 C CG . MET A 1 623 ? 28.619 79.016 36.988 1.00 38.20 ? 616 MET A CG 1 ATOM 4566 S SD . MET A 1 623 ? 28.609 80.587 35.996 1.00 47.65 ? 616 MET A SD 1 ATOM 4567 C CE . MET A 1 623 ? 30.340 80.832 35.590 1.00 41.88 ? 616 MET A CE 1 ATOM 4568 N N . LYS A 1 624 ? 29.452 75.641 33.555 1.00 33.83 ? 617 LYS A N 1 ATOM 4569 C CA . LYS A 1 624 ? 30.189 75.226 32.342 1.00 35.76 ? 617 LYS A CA 1 ATOM 4570 C C . LYS A 1 624 ? 29.659 75.967 31.101 1.00 35.39 ? 617 LYS A C 1 ATOM 4571 O O . LYS A 1 624 ? 30.260 75.880 30.044 1.00 36.01 ? 617 LYS A O 1 ATOM 4572 C CB . LYS A 1 624 ? 30.132 73.707 32.086 1.00 36.78 ? 617 LYS A CB 1 ATOM 4573 C CG . LYS A 1 624 ? 30.668 72.789 33.216 1.00 41.29 ? 617 LYS A CG 1 ATOM 4574 C CD . LYS A 1 624 ? 32.211 72.773 33.315 1.00 51.07 ? 617 LYS A CD 1 ATOM 4575 C CE . LYS A 1 624 ? 32.689 71.756 34.406 1.00 54.01 ? 617 LYS A CE 1 ATOM 4576 N NZ . LYS A 1 624 ? 32.425 72.193 35.832 1.00 54.12 ? 617 LYS A NZ 1 ATOM 4577 N N . HIS A 1 625 ? 28.522 76.665 31.221 1.00 33.56 ? 618 HIS A N 1 ATOM 4578 C CA . HIS A 1 625 ? 27.960 77.397 30.081 1.00 32.82 ? 618 HIS A CA 1 ATOM 4579 C C . HIS A 1 625 ? 27.794 78.884 30.417 1.00 32.91 ? 618 HIS A C 1 ATOM 4580 O O . HIS A 1 625 ? 26.664 79.391 30.484 1.00 30.86 ? 618 HIS A O 1 ATOM 4581 C CB . HIS A 1 625 ? 26.626 76.779 29.672 1.00 32.67 ? 618 HIS A CB 1 ATOM 4582 C CG . HIS A 1 625 ? 26.650 75.274 29.578 1.00 34.06 ? 618 HIS A CG 1 ATOM 4583 N ND1 . HIS A 1 625 ? 26.278 74.444 30.632 1.00 39.03 ? 618 HIS A ND1 1 ATOM 4584 C CD2 . HIS A 1 625 ? 26.969 74.457 28.553 1.00 32.51 ? 618 HIS A CD2 1 ATOM 4585 C CE1 . HIS A 1 625 ? 26.386 73.180 30.253 1.00 37.21 ? 618 HIS A CE1 1 ATOM 4586 N NE2 . HIS A 1 625 ? 26.787 73.162 28.990 1.00 40.15 ? 618 HIS A NE2 1 ATOM 4587 N N . PRO A 1 626 ? 28.921 79.600 30.627 1.00 33.39 ? 619 PRO A N 1 ATOM 4588 C CA . PRO A 1 626 ? 28.737 80.981 31.110 1.00 34.10 ? 619 PRO A CA 1 ATOM 4589 C C . PRO A 1 626 ? 28.063 81.926 30.129 1.00 34.95 ? 619 PRO A C 1 ATOM 4590 O O . PRO A 1 626 ? 27.290 82.784 30.587 1.00 34.42 ? 619 PRO A O 1 ATOM 4591 C CB . PRO A 1 626 ? 30.163 81.467 31.392 1.00 35.42 ? 619 PRO A CB 1 ATOM 4592 C CG . PRO A 1 626 ? 31.075 80.542 30.549 1.00 36.06 ? 619 PRO A CG 1 ATOM 4593 C CD . PRO A 1 626 ? 30.350 79.214 30.596 1.00 33.88 ? 619 PRO A CD 1 ATOM 4594 N N . GLN A 1 627 ? 28.336 81.792 28.821 1.00 35.14 ? 620 GLN A N 1 ATOM 4595 C CA . GLN A 1 627 ? 27.674 82.655 27.822 1.00 36.39 ? 620 GLN A CA 1 ATOM 4596 C C . GLN A 1 627 ? 26.137 82.549 27.896 1.00 34.06 ? 620 GLN A C 1 ATOM 4597 O O . GLN A 1 627 ? 25.431 83.581 27.876 1.00 32.33 ? 620 GLN A O 1 ATOM 4598 C CB . GLN A 1 627 ? 28.168 82.352 26.390 1.00 38.93 ? 620 GLN A CB 1 ATOM 4599 C CG . GLN A 1 627 ? 27.871 83.457 25.320 1.00 45.95 ? 620 GLN A CG 1 ATOM 4600 C CD . GLN A 1 627 ? 27.980 84.928 25.836 1.00 49.93 ? 620 GLN A CD 1 ATOM 4601 O OE1 . GLN A 1 627 ? 29.086 85.501 25.914 1.00 55.42 ? 620 GLN A OE1 1 ATOM 4602 N NE2 . GLN A 1 627 ? 26.815 85.537 26.183 1.00 46.23 ? 620 GLN A NE2 1 ATOM 4603 N N . GLU A 1 628 ? 25.628 81.316 27.968 1.00 32.08 ? 621 GLU A N 1 ATOM 4604 C CA . GLU A 1 628 ? 24.185 81.104 28.029 1.00 31.50 ? 621 GLU A CA 1 ATOM 4605 C C . GLU A 1 628 ? 23.579 81.632 29.319 1.00 30.25 ? 621 GLU A C 1 ATOM 4606 O O . GLU A 1 628 ? 22.456 82.167 29.325 1.00 30.74 ? 621 GLU A O 1 ATOM 4607 C CB . GLU A 1 628 ? 23.831 79.618 27.834 1.00 31.75 ? 621 GLU A CB 1 ATOM 4608 C CG . GLU A 1 628 ? 24.105 79.118 26.402 1.00 35.20 ? 621 GLU A CG 1 ATOM 4609 C CD . GLU A 1 628 ? 25.570 78.871 26.077 1.00 40.90 ? 621 GLU A CD 1 ATOM 4610 O OE1 . GLU A 1 628 ? 26.442 78.782 26.972 1.00 42.07 ? 621 GLU A OE1 1 ATOM 4611 O OE2 . GLU A 1 628 ? 25.865 78.781 24.875 1.00 47.11 ? 621 GLU A OE2 1 ATOM 4612 N N . MET A 1 629 ? 24.291 81.459 30.431 1.00 29.40 ? 622 MET A N 1 ATOM 4613 C CA . MET A 1 629 ? 23.822 81.989 31.706 1.00 27.82 ? 622 MET A CA 1 ATOM 4614 C C . MET A 1 629 ? 23.700 83.526 31.625 1.00 29.55 ? 622 MET A C 1 ATOM 4615 O O . MET A 1 629 ? 22.754 84.118 32.169 1.00 30.39 ? 622 MET A O 1 ATOM 4616 C CB . MET A 1 629 ? 24.770 81.543 32.820 1.00 27.84 ? 622 MET A CB 1 ATOM 4617 C CG . MET A 1 629 ? 24.591 80.013 33.214 1.00 25.10 ? 622 MET A CG 1 ATOM 4618 S SD . MET A 1 629 ? 25.591 79.633 34.704 1.00 29.52 ? 622 MET A SD 1 ATOM 4619 C CE . MET A 1 629 ? 24.652 80.530 35.998 1.00 24.91 ? 622 MET A CE 1 ATOM 4620 N N . LYS A 1 630 ? 24.634 84.153 30.915 1.00 30.46 ? 623 LYS A N 1 ATOM 4621 C CA . LYS A 1 630 ? 24.577 85.595 30.674 1.00 32.49 ? 623 LYS A CA 1 ATOM 4622 C C . LYS A 1 630 ? 23.386 85.952 29.772 1.00 32.33 ? 623 LYS A C 1 ATOM 4623 O O . LYS A 1 630 ? 22.559 86.807 30.133 1.00 30.51 ? 623 LYS A O 1 ATOM 4624 C CB . LYS A 1 630 ? 25.879 86.097 30.080 1.00 34.61 ? 623 LYS A CB 1 ATOM 4625 C CG . LYS A 1 630 ? 27.018 86.129 31.059 1.00 35.71 ? 623 LYS A CG 1 ATOM 4626 C CD . LYS A 1 630 ? 28.329 86.496 30.373 1.00 43.49 ? 623 LYS A CD 1 ATOM 4627 C CE . LYS A 1 630 ? 29.423 86.395 31.405 1.00 46.55 ? 623 LYS A CE 1 ATOM 4628 N NZ . LYS A 1 630 ? 30.640 85.649 30.982 1.00 53.07 ? 623 LYS A NZ 1 ATOM 4629 N N . THR A 1 631 ? 23.287 85.256 28.637 1.00 32.19 ? 624 THR A N 1 ATOM 4630 C CA . THR A 1 631 ? 22.262 85.546 27.638 1.00 34.26 ? 624 THR A CA 1 ATOM 4631 C C . THR A 1 631 ? 20.856 85.379 28.164 1.00 32.60 ? 624 THR A C 1 ATOM 4632 O O . THR A 1 631 ? 19.982 86.215 27.881 1.00 33.52 ? 624 THR A O 1 ATOM 4633 C CB . THR A 1 631 ? 22.464 84.709 26.359 1.00 35.08 ? 624 THR A CB 1 ATOM 4634 O OG1 . THR A 1 631 ? 23.743 85.046 25.826 1.00 38.77 ? 624 THR A OG1 1 ATOM 4635 C CG2 . THR A 1 631 ? 21.412 85.067 25.292 1.00 38.54 ? 624 THR A CG2 1 ATOM 4636 N N . TYR A 1 632 ? 20.635 84.320 28.938 1.00 30.02 ? 625 TYR A N 1 ATOM 4637 C CA . TYR A 1 632 ? 19.307 84.037 29.438 1.00 29.62 ? 625 TYR A CA 1 ATOM 4638 C C . TYR A 1 632 ? 19.076 84.447 30.887 1.00 28.78 ? 625 TYR A C 1 ATOM 4639 O O . TYR A 1 632 ? 18.025 84.108 31.428 1.00 28.07 ? 625 TYR A O 1 ATOM 4640 C CB . TYR A 1 632 ? 18.900 82.568 29.179 1.00 28.76 ? 625 TYR A CB 1 ATOM 4641 C CG . TYR A 1 632 ? 19.060 82.239 27.701 1.00 30.25 ? 625 TYR A CG 1 ATOM 4642 C CD1 . TYR A 1 632 ? 18.191 82.787 26.758 1.00 34.04 ? 625 TYR A CD1 1 ATOM 4643 C CD2 . TYR A 1 632 ? 20.084 81.402 27.253 1.00 32.37 ? 625 TYR A CD2 1 ATOM 4644 C CE1 . TYR A 1 632 ? 18.359 82.529 25.363 1.00 38.99 ? 625 TYR A CE1 1 ATOM 4645 C CE2 . TYR A 1 632 ? 20.258 81.121 25.874 1.00 37.90 ? 625 TYR A CE2 1 ATOM 4646 C CZ . TYR A 1 632 ? 19.381 81.685 24.939 1.00 40.10 ? 625 TYR A CZ 1 ATOM 4647 O OH . TYR A 1 632 ? 19.559 81.441 23.588 1.00 42.98 ? 625 TYR A OH 1 ATOM 4648 N N . SER A 1 633 ? 20.034 85.182 31.480 1.00 28.31 ? 626 SER A N 1 ATOM 4649 C CA . SER A 1 633 ? 19.902 85.704 32.861 1.00 28.19 ? 626 SER A CA 1 ATOM 4650 C C . SER A 1 633 ? 19.617 84.562 33.833 1.00 27.13 ? 626 SER A C 1 ATOM 4651 O O . SER A 1 633 ? 18.637 84.612 34.581 1.00 26.16 ? 626 SER A O 1 ATOM 4652 C CB . SER A 1 633 ? 18.803 86.787 32.965 1.00 27.87 ? 626 SER A CB 1 ATOM 4653 O OG . SER A 1 633 ? 19.145 87.857 32.100 1.00 32.10 ? 626 SER A OG 1 ATOM 4654 N N . VAL A 1 634 ? 20.460 83.523 33.800 1.00 26.79 ? 627 VAL A N 1 ATOM 4655 C CA . VAL A 1 634 ? 20.252 82.332 34.626 1.00 25.83 ? 627 VAL A CA 1 ATOM 4656 C C . VAL A 1 634 ? 20.971 82.567 35.950 1.00 27.17 ? 627 VAL A C 1 ATOM 4657 O O . VAL A 1 634 ? 22.221 82.632 35.995 1.00 29.78 ? 627 VAL A O 1 ATOM 4658 C CB . VAL A 1 634 ? 20.833 81.057 33.936 1.00 26.06 ? 627 VAL A CB 1 ATOM 4659 C CG1 . VAL A 1 634 ? 20.510 79.772 34.770 1.00 21.81 ? 627 VAL A CG1 1 ATOM 4660 C CG2 . VAL A 1 634 ? 20.309 80.951 32.500 1.00 24.92 ? 627 VAL A CG2 1 ATOM 4661 N N . SER A 1 635 ? 20.186 82.792 36.996 1.00 27.40 ? 628 SER A N 1 ATOM 4662 C CA . SER A 1 635 ? 20.737 82.997 38.332 1.00 28.14 ? 628 SER A CA 1 ATOM 4663 C C . SER A 1 635 ? 20.343 81.879 39.306 1.00 26.95 ? 628 SER A C 1 ATOM 4664 O O . SER A 1 635 ? 19.169 81.427 39.357 1.00 24.45 ? 628 SER A O 1 ATOM 4665 C CB . SER A 1 635 ? 20.308 84.340 38.919 1.00 29.37 ? 628 SER A CB 1 ATOM 4666 O OG . SER A 1 635 ? 21.018 84.511 40.141 1.00 30.89 ? 628 SER A OG 1 ATOM 4667 N N . PHE A 1 636 ? 21.335 81.418 40.069 1.00 26.30 ? 629 PHE A N 1 ATOM 4668 C CA . PHE A 1 636 ? 21.063 80.527 41.203 1.00 25.32 ? 629 PHE A CA 1 ATOM 4669 C C . PHE A 1 636 ? 20.862 81.275 42.550 1.00 24.85 ? 629 PHE A C 1 ATOM 4670 O O . PHE A 1 636 ? 20.758 80.614 43.615 1.00 23.88 ? 629 PHE A O 1 ATOM 4671 C CB . PHE A 1 636 ? 22.188 79.485 41.331 1.00 25.69 ? 629 PHE A CB 1 ATOM 4672 C CG . PHE A 1 636 ? 22.128 78.432 40.263 1.00 26.20 ? 629 PHE A CG 1 ATOM 4673 C CD1 . PHE A 1 636 ? 21.523 77.205 40.521 1.00 24.86 ? 629 PHE A CD1 1 ATOM 4674 C CD2 . PHE A 1 636 ? 22.660 78.686 38.984 1.00 27.92 ? 629 PHE A CD2 1 ATOM 4675 C CE1 . PHE A 1 636 ? 21.432 76.220 39.524 1.00 25.81 ? 629 PHE A CE1 1 ATOM 4676 C CE2 . PHE A 1 636 ? 22.604 77.722 37.992 1.00 25.41 ? 629 PHE A CE2 1 ATOM 4677 C CZ . PHE A 1 636 ? 21.990 76.473 38.267 1.00 25.26 ? 629 PHE A CZ 1 ATOM 4678 N N . ASP A 1 637 ? 20.791 82.612 42.513 1.00 24.35 ? 630 ASP A N 1 ATOM 4679 C CA . ASP A 1 637 ? 20.723 83.390 43.777 1.00 25.29 ? 630 ASP A CA 1 ATOM 4680 C C . ASP A 1 637 ? 19.547 82.931 44.632 1.00 24.18 ? 630 ASP A C 1 ATOM 4681 O O . ASP A 1 637 ? 19.677 82.838 45.857 1.00 25.74 ? 630 ASP A O 1 ATOM 4682 C CB . ASP A 1 637 ? 20.629 84.903 43.562 1.00 25.88 ? 630 ASP A CB 1 ATOM 4683 C CG . ASP A 1 637 ? 21.924 85.516 42.972 1.00 30.49 ? 630 ASP A CG 1 ATOM 4684 O OD1 . ASP A 1 637 ? 22.980 84.826 42.886 1.00 32.05 ? 630 ASP A OD1 1 ATOM 4685 O OD2 . ASP A 1 637 ? 21.875 86.707 42.602 1.00 32.93 ? 630 ASP A OD2 1 ATOM 4686 N N . SER A 1 638 ? 18.397 82.658 44.014 1.00 23.44 ? 631 SER A N 1 ATOM 4687 C CA . SER A 1 638 ? 17.226 82.217 44.821 1.00 23.19 ? 631 SER A CA 1 ATOM 4688 C C . SER A 1 638 ? 17.480 80.893 45.561 1.00 22.87 ? 631 SER A C 1 ATOM 4689 O O . SER A 1 638 ? 17.068 80.719 46.735 1.00 21.78 ? 631 SER A O 1 ATOM 4690 C CB . SER A 1 638 ? 15.926 82.120 43.996 1.00 22.85 ? 631 SER A CB 1 ATOM 4691 O OG . SER A 1 638 ? 16.066 81.167 42.953 1.00 23.21 ? 631 SER A OG 1 ATOM 4692 N N . LEU A 1 639 ? 18.146 79.964 44.885 1.00 22.45 ? 632 LEU A N 1 ATOM 4693 C CA . LEU A 1 639 ? 18.408 78.682 45.499 1.00 22.46 ? 632 LEU A CA 1 ATOM 4694 C C . LEU A 1 639 ? 19.413 78.836 46.656 1.00 22.82 ? 632 LEU A C 1 ATOM 4695 O O . LEU A 1 639 ? 19.235 78.263 47.716 1.00 21.58 ? 632 LEU A O 1 ATOM 4696 C CB . LEU A 1 639 ? 18.867 77.667 44.435 1.00 21.96 ? 632 LEU A CB 1 ATOM 4697 C CG . LEU A 1 639 ? 19.172 76.244 44.976 1.00 22.75 ? 632 LEU A CG 1 ATOM 4698 C CD1 . LEU A 1 639 ? 17.911 75.613 45.580 1.00 19.95 ? 632 LEU A CD1 1 ATOM 4699 C CD2 . LEU A 1 639 ? 19.729 75.343 43.878 1.00 21.88 ? 632 LEU A CD2 1 ATOM 4700 N N . PHE A 1 640 ? 20.456 79.628 46.458 1.00 23.32 ? 633 PHE A N 1 ATOM 4701 C CA . PHE A 1 640 ? 21.432 79.833 47.551 1.00 24.36 ? 633 PHE A CA 1 ATOM 4702 C C . PHE A 1 640 ? 20.795 80.572 48.730 1.00 25.30 ? 633 PHE A C 1 ATOM 4703 O O . PHE A 1 640 ? 21.039 80.233 49.903 1.00 25.33 ? 633 PHE A O 1 ATOM 4704 C CB . PHE A 1 640 ? 22.659 80.563 47.027 1.00 25.55 ? 633 PHE A CB 1 ATOM 4705 C CG . PHE A 1 640 ? 23.591 79.659 46.285 1.00 27.31 ? 633 PHE A CG 1 ATOM 4706 C CD1 . PHE A 1 640 ? 24.345 78.706 46.984 1.00 28.01 ? 633 PHE A CD1 1 ATOM 4707 C CD2 . PHE A 1 640 ? 23.726 79.749 44.908 1.00 29.42 ? 633 PHE A CD2 1 ATOM 4708 C CE1 . PHE A 1 640 ? 25.209 77.831 46.304 1.00 30.17 ? 633 PHE A CE1 1 ATOM 4709 C CE2 . PHE A 1 640 ? 24.592 78.881 44.224 1.00 31.04 ? 633 PHE A CE2 1 ATOM 4710 C CZ . PHE A 1 640 ? 25.326 77.917 44.936 1.00 29.36 ? 633 PHE A CZ 1 ATOM 4711 N N . SER A 1 641 ? 19.922 81.537 48.413 1.00 24.88 ? 634 SER A N 1 ATOM 4712 C CA . SER A 1 641 ? 19.120 82.241 49.445 1.00 24.99 ? 634 SER A CA 1 ATOM 4713 C C . SER A 1 641 ? 18.252 81.264 50.269 1.00 23.75 ? 634 SER A C 1 ATOM 4714 O O . SER A 1 641 ? 18.245 81.306 51.509 1.00 23.48 ? 634 SER A O 1 ATOM 4715 C CB . SER A 1 641 ? 18.237 83.330 48.786 1.00 24.71 ? 634 SER A CB 1 ATOM 4716 O OG . SER A 1 641 ? 17.408 83.939 49.752 1.00 25.18 ? 634 SER A OG 1 ATOM 4717 N N . ALA A 1 642 ? 17.528 80.369 49.586 1.00 22.03 ? 635 ALA A N 1 ATOM 4718 C CA . ALA A 1 642 ? 16.676 79.395 50.257 1.00 20.65 ? 635 ALA A CA 1 ATOM 4719 C C . ALA A 1 642 ? 17.514 78.460 51.154 1.00 21.54 ? 635 ALA A C 1 ATOM 4720 O O . ALA A 1 642 ? 17.107 78.146 52.291 1.00 21.78 ? 635 ALA A O 1 ATOM 4721 C CB . ALA A 1 642 ? 15.893 78.573 49.183 1.00 20.04 ? 635 ALA A CB 1 ATOM 4722 N N . VAL A 1 643 ? 18.700 78.065 50.662 1.00 21.28 ? 636 VAL A N 1 ATOM 4723 C CA . VAL A 1 643 ? 19.583 77.154 51.412 1.00 21.46 ? 636 VAL A CA 1 ATOM 4724 C C . VAL A 1 643 ? 20.139 77.868 52.675 1.00 23.36 ? 636 VAL A C 1 ATOM 4725 O O . VAL A 1 643 ? 20.216 77.282 53.789 1.00 22.48 ? 636 VAL A O 1 ATOM 4726 C CB . VAL A 1 643 ? 20.700 76.643 50.516 1.00 21.52 ? 636 VAL A CB 1 ATOM 4727 C CG1 . VAL A 1 643 ? 21.835 75.938 51.358 1.00 23.54 ? 636 VAL A CG1 1 ATOM 4728 C CG2 . VAL A 1 643 ? 20.135 75.701 49.428 1.00 22.92 ? 636 VAL A CG2 1 ATOM 4729 N N . LYS A 1 644 ? 20.534 79.120 52.498 1.00 23.84 ? 637 LYS A N 1 ATOM 4730 C CA . LYS A 1 644 ? 20.951 79.987 53.624 1.00 24.97 ? 637 LYS A CA 1 ATOM 4731 C C . LYS A 1 644 ? 19.832 80.111 54.659 1.00 24.59 ? 637 LYS A C 1 ATOM 4732 O O . LYS A 1 644 ? 20.073 79.988 55.850 1.00 24.43 ? 637 LYS A O 1 ATOM 4733 C CB . LYS A 1 644 ? 21.329 81.391 53.089 1.00 25.91 ? 637 LYS A CB 1 ATOM 4734 C CG . LYS A 1 644 ? 21.765 82.426 54.180 1.00 31.05 ? 637 LYS A CG 1 ATOM 4735 C CD . LYS A 1 644 ? 22.061 83.842 53.524 1.00 35.59 ? 637 LYS A CD 1 ATOM 4736 C CE . LYS A 1 644 ? 22.482 84.889 54.573 1.00 41.28 ? 637 LYS A CE 1 ATOM 4737 N NZ . LYS A 1 644 ? 21.256 85.297 55.360 1.00 42.26 ? 637 LYS A NZ 1 ATOM 4738 N N . ASN A 1 645 ? 18.599 80.369 54.206 1.00 24.00 ? 638 ASN A N 1 ATOM 4739 C CA . ASN A 1 645 ? 17.470 80.459 55.121 1.00 24.67 ? 638 ASN A CA 1 ATOM 4740 C C . ASN A 1 645 ? 17.202 79.126 55.819 1.00 24.42 ? 638 ASN A C 1 ATOM 4741 O O . ASN A 1 645 ? 16.961 79.117 57.028 1.00 24.10 ? 638 ASN A O 1 ATOM 4742 C CB . ASN A 1 645 ? 16.214 80.876 54.386 1.00 23.94 ? 638 ASN A CB 1 ATOM 4743 C CG . ASN A 1 645 ? 16.274 82.302 53.935 1.00 27.00 ? 638 ASN A CG 1 ATOM 4744 O OD1 . ASN A 1 645 ? 17.189 83.054 54.317 1.00 25.90 ? 638 ASN A OD1 1 ATOM 4745 N ND2 . ASN A 1 645 ? 15.306 82.704 53.134 1.00 27.10 ? 638 ASN A ND2 1 ATOM 4746 N N . PHE A 1 646 ? 17.250 78.011 55.066 1.00 22.83 ? 639 PHE A N 1 ATOM 4747 C CA . PHE A 1 646 ? 17.080 76.699 55.651 1.00 22.69 ? 639 PHE A CA 1 ATOM 4748 C C . PHE A 1 646 ? 18.148 76.512 56.763 1.00 23.03 ? 639 PHE A C 1 ATOM 4749 O O . PHE A 1 646 ? 17.848 76.031 57.859 1.00 23.63 ? 639 PHE A O 1 ATOM 4750 C CB . PHE A 1 646 ? 17.235 75.592 54.596 1.00 20.89 ? 639 PHE A CB 1 ATOM 4751 C CG . PHE A 1 646 ? 16.849 74.228 55.089 1.00 22.58 ? 639 PHE A CG 1 ATOM 4752 C CD1 . PHE A 1 646 ? 15.617 73.670 54.743 1.00 22.11 ? 639 PHE A CD1 1 ATOM 4753 C CD2 . PHE A 1 646 ? 17.706 73.503 55.915 1.00 20.66 ? 639 PHE A CD2 1 ATOM 4754 C CE1 . PHE A 1 646 ? 15.238 72.401 55.202 1.00 25.20 ? 639 PHE A CE1 1 ATOM 4755 C CE2 . PHE A 1 646 ? 17.347 72.250 56.418 1.00 22.23 ? 639 PHE A CE2 1 ATOM 4756 C CZ . PHE A 1 646 ? 16.088 71.680 56.052 1.00 22.57 ? 639 PHE A CZ 1 ATOM 4757 N N . THR A 1 647 ? 19.388 76.890 56.473 1.00 24.22 ? 640 THR A N 1 ATOM 4758 C CA . THR A 1 647 ? 20.480 76.757 57.477 1.00 24.58 ? 640 THR A CA 1 ATOM 4759 C C . THR A 1 647 ? 20.166 77.531 58.770 1.00 25.88 ? 640 THR A C 1 ATOM 4760 O O . THR A 1 647 ? 20.284 76.996 59.883 1.00 26.50 ? 640 THR A O 1 ATOM 4761 C CB . THR A 1 647 ? 21.821 77.180 56.874 1.00 25.44 ? 640 THR A CB 1 ATOM 4762 O OG1 . THR A 1 647 ? 22.001 76.467 55.637 1.00 25.18 ? 640 THR A OG1 1 ATOM 4763 C CG2 . THR A 1 647 ? 23.001 76.888 57.862 1.00 27.31 ? 640 THR A CG2 1 ATOM 4764 N N . GLU A 1 648 ? 19.764 78.789 58.611 1.00 26.13 ? 641 GLU A N 1 ATOM 4765 C CA . GLU A 1 648 ? 19.459 79.647 59.742 1.00 28.57 ? 641 GLU A CA 1 ATOM 4766 C C . GLU A 1 648 ? 18.278 79.125 60.544 1.00 27.21 ? 641 GLU A C 1 ATOM 4767 O O . GLU A 1 648 ? 18.325 79.061 61.783 1.00 26.65 ? 641 GLU A O 1 ATOM 4768 C CB . GLU A 1 648 ? 19.256 81.124 59.279 1.00 28.65 ? 641 GLU A CB 1 ATOM 4769 C CG . GLU A 1 648 ? 20.639 81.747 58.841 1.00 37.77 ? 641 GLU A CG 1 ATOM 4770 C CD . GLU A 1 648 ? 20.539 83.107 58.084 1.00 42.27 ? 641 GLU A CD 1 ATOM 4771 O OE1 . GLU A 1 648 ? 21.585 83.589 57.579 1.00 44.42 ? 641 GLU A OE1 1 ATOM 4772 O OE2 . GLU A 1 648 ? 19.433 83.682 58.001 1.00 46.50 ? 641 GLU A OE2 1 ATOM 4773 N N . ILE A 1 649 ? 17.191 78.778 59.845 1.00 25.64 ? 642 ILE A N 1 ATOM 4774 C CA . ILE A 1 649 ? 15.988 78.333 60.518 1.00 24.88 ? 642 ILE A CA 1 ATOM 4775 C C . ILE A 1 649 ? 16.172 76.984 61.197 1.00 24.78 ? 642 ILE A C 1 ATOM 4776 O O . ILE A 1 649 ? 15.672 76.765 62.328 1.00 24.45 ? 642 ILE A O 1 ATOM 4777 C CB . ILE A 1 649 ? 14.789 78.281 59.546 1.00 24.69 ? 642 ILE A CB 1 ATOM 4778 C CG1 . ILE A 1 649 ? 14.391 79.691 59.139 1.00 25.40 ? 642 ILE A CG1 1 ATOM 4779 C CG2 . ILE A 1 649 ? 13.592 77.523 60.144 1.00 24.29 ? 642 ILE A CG2 1 ATOM 4780 C CD1 . ILE A 1 649 ? 13.447 79.663 57.890 1.00 25.89 ? 642 ILE A CD1 1 ATOM 4781 N N . ALA A 1 650 ? 16.887 76.085 60.531 1.00 24.36 ? 643 ALA A N 1 ATOM 4782 C CA . ALA A 1 650 ? 17.228 74.800 61.151 1.00 25.81 ? 643 ALA A CA 1 ATOM 4783 C C . ALA A 1 650 ? 18.044 74.985 62.422 1.00 26.74 ? 643 ALA A C 1 ATOM 4784 O O . ALA A 1 650 ? 17.833 74.283 63.424 1.00 26.92 ? 643 ALA A O 1 ATOM 4785 C CB . ALA A 1 650 ? 17.990 73.834 60.122 1.00 26.34 ? 643 ALA A CB 1 ATOM 4786 N N . SER A 1 651 ? 18.999 75.909 62.397 1.00 28.49 ? 644 SER A N 1 ATOM 4787 C CA . SER A 1 651 ? 19.833 76.148 63.580 1.00 29.99 ? 644 SER A CA 1 ATOM 4788 C C . SER A 1 651 ? 18.945 76.646 64.745 1.00 29.88 ? 644 SER A C 1 ATOM 4789 O O . SER A 1 651 ? 19.091 76.216 65.902 1.00 30.89 ? 644 SER A O 1 ATOM 4790 C CB . SER A 1 651 ? 20.905 77.201 63.266 1.00 31.18 ? 644 SER A CB 1 ATOM 4791 O OG . SER A 1 651 ? 21.653 77.463 64.432 1.00 38.58 ? 644 SER A OG 1 ATOM 4792 N N . LYS A 1 652 ? 18.003 77.534 64.451 1.00 28.54 ? 645 LYS A N 1 ATOM 4793 C CA A LYS A 1 652 ? 17.106 78.045 65.487 0.50 29.10 ? 645 LYS A CA 1 ATOM 4794 C CA B LYS A 1 652 ? 17.112 78.044 65.489 0.50 29.21 ? 645 LYS A CA 1 ATOM 4795 C C . LYS A 1 652 ? 16.165 76.949 66.008 1.00 28.70 ? 645 LYS A C 1 ATOM 4796 O O . LYS A 1 652 ? 15.908 76.860 67.214 1.00 28.80 ? 645 LYS A O 1 ATOM 4797 C CB A LYS A 1 652 ? 16.318 79.254 64.975 0.50 28.86 ? 645 LYS A CB 1 ATOM 4798 C CB B LYS A 1 652 ? 16.348 79.273 64.986 0.50 29.12 ? 645 LYS A CB 1 ATOM 4799 C CG A LYS A 1 652 ? 17.170 80.534 64.866 0.50 31.28 ? 645 LYS A CG 1 ATOM 4800 C CG B LYS A 1 652 ? 17.256 80.516 64.846 0.50 31.87 ? 645 LYS A CG 1 ATOM 4801 C CD A LYS A 1 652 ? 17.655 81.005 66.238 0.50 33.32 ? 645 LYS A CD 1 ATOM 4802 C CD B LYS A 1 652 ? 16.514 81.730 64.298 0.50 34.00 ? 645 LYS A CD 1 ATOM 4803 C CE A LYS A 1 652 ? 18.647 82.161 66.115 0.50 36.60 ? 645 LYS A CE 1 ATOM 4804 C CE B LYS A 1 652 ? 17.444 82.943 64.185 0.50 38.44 ? 645 LYS A CE 1 ATOM 4805 N NZ A LYS A 1 652 ? 19.325 82.467 67.427 0.50 40.45 ? 645 LYS A NZ 1 ATOM 4806 N NZ B LYS A 1 652 ? 17.063 83.838 63.046 0.50 37.76 ? 645 LYS A NZ 1 ATOM 4807 N N . PHE A 1 653 ? 15.664 76.103 65.105 1.00 27.16 ? 646 PHE A N 1 ATOM 4808 C CA . PHE A 1 653 ? 14.797 74.994 65.509 1.00 26.59 ? 646 PHE A CA 1 ATOM 4809 C C . PHE A 1 653 ? 15.554 74.013 66.450 1.00 27.58 ? 646 PHE A C 1 ATOM 4810 O O . PHE A 1 653 ? 14.994 73.502 67.462 1.00 28.06 ? 646 PHE A O 1 ATOM 4811 C CB . PHE A 1 653 ? 14.307 74.242 64.259 1.00 26.57 ? 646 PHE A CB 1 ATOM 4812 C CG . PHE A 1 653 ? 13.454 73.032 64.575 1.00 25.62 ? 646 PHE A CG 1 ATOM 4813 C CD1 . PHE A 1 653 ? 12.082 73.168 64.803 1.00 22.07 ? 646 PHE A CD1 1 ATOM 4814 C CD2 . PHE A 1 653 ? 14.041 71.772 64.685 1.00 27.41 ? 646 PHE A CD2 1 ATOM 4815 C CE1 . PHE A 1 653 ? 11.308 72.062 65.107 1.00 24.96 ? 646 PHE A CE1 1 ATOM 4816 C CE2 . PHE A 1 653 ? 13.262 70.629 64.998 1.00 25.77 ? 646 PHE A CE2 1 ATOM 4817 C CZ . PHE A 1 653 ? 11.908 70.775 65.193 1.00 24.84 ? 646 PHE A CZ 1 ATOM 4818 N N . SER A 1 654 ? 16.804 73.732 66.103 1.00 26.45 ? 647 SER A N 1 ATOM 4819 C CA . SER A 1 654 ? 17.660 72.879 66.942 1.00 29.48 ? 647 SER A CA 1 ATOM 4820 C C . SER A 1 654 ? 17.778 73.421 68.377 1.00 31.02 ? 647 SER A C 1 ATOM 4821 O O . SER A 1 654 ? 17.760 72.642 69.345 1.00 32.52 ? 647 SER A O 1 ATOM 4822 C CB . SER A 1 654 ? 19.040 72.757 66.311 1.00 28.72 ? 647 SER A CB 1 ATOM 4823 O OG A SER A 1 654 ? 18.935 72.041 65.079 0.50 27.90 ? 647 SER A OG 1 ATOM 4824 O OG B SER A 1 654 ? 19.731 71.642 66.827 0.50 30.72 ? 647 SER A OG 1 ATOM 4825 N N . GLU A 1 655 ? 17.954 74.735 68.501 1.00 32.24 ? 648 GLU A N 1 ATOM 4826 C CA . GLU A 1 655 ? 18.017 75.402 69.808 1.00 34.67 ? 648 GLU A CA 1 ATOM 4827 C C . GLU A 1 655 ? 16.730 75.195 70.605 1.00 33.90 ? 648 GLU A C 1 ATOM 4828 O O . GLU A 1 655 ? 16.783 74.815 71.794 1.00 34.63 ? 648 GLU A O 1 ATOM 4829 C CB . GLU A 1 655 ? 18.277 76.901 69.643 1.00 36.16 ? 648 GLU A CB 1 ATOM 4830 C CG . GLU A 1 655 ? 19.682 77.217 69.177 1.00 42.95 ? 648 GLU A CG 1 ATOM 4831 C CD . GLU A 1 655 ? 19.909 78.708 68.844 1.00 51.24 ? 648 GLU A CD 1 ATOM 4832 O OE1 . GLU A 1 655 ? 19.151 79.609 69.305 1.00 52.08 ? 648 GLU A OE1 1 ATOM 4833 O OE2 . GLU A 1 655 ? 20.878 78.971 68.098 1.00 57.05 ? 648 GLU A OE2 1 ATOM 4834 N N . ARG A 1 656 ? 15.577 75.400 69.948 1.00 32.03 ? 649 ARG A N 1 ATOM 4835 C CA . ARG A 1 656 ? 14.296 75.166 70.622 1.00 32.02 ? 649 ARG A CA 1 ATOM 4836 C C . ARG A 1 656 ? 14.130 73.713 71.007 1.00 32.07 ? 649 ARG A C 1 ATOM 4837 O O . ARG A 1 656 ? 13.596 73.401 72.068 1.00 31.81 ? 649 ARG A O 1 ATOM 4838 C CB . ARG A 1 656 ? 13.105 75.672 69.784 1.00 31.65 ? 649 ARG A CB 1 ATOM 4839 C CG . ARG A 1 656 ? 13.200 77.152 69.466 1.00 32.56 ? 649 ARG A CG 1 ATOM 4840 C CD . ARG A 1 656 ? 11.838 77.737 69.043 1.00 31.78 ? 649 ARG A CD 1 ATOM 4841 N NE . ARG A 1 656 ? 11.254 76.944 67.967 1.00 29.60 ? 649 ARG A NE 1 ATOM 4842 C CZ . ARG A 1 656 ? 11.542 77.118 66.678 1.00 29.01 ? 649 ARG A CZ 1 ATOM 4843 N NH1 . ARG A 1 656 ? 12.433 78.053 66.320 1.00 28.57 ? 649 ARG A NH1 1 ATOM 4844 N NH2 . ARG A 1 656 ? 10.950 76.364 65.764 1.00 27.49 ? 649 ARG A NH2 1 ATOM 4845 N N . LEU A 1 657 ? 14.634 72.816 70.163 1.00 31.82 ? 650 LEU A N 1 ATOM 4846 C CA . LEU A 1 657 ? 14.522 71.389 70.419 1.00 34.25 ? 650 LEU A CA 1 ATOM 4847 C C . LEU A 1 657 ? 15.331 71.018 71.681 1.00 37.20 ? 650 LEU A C 1 ATOM 4848 O O . LEU A 1 657 ? 14.923 70.135 72.454 1.00 35.79 ? 650 LEU A O 1 ATOM 4849 C CB . LEU A 1 657 ? 15.013 70.606 69.196 1.00 33.20 ? 650 LEU A CB 1 ATOM 4850 C CG . LEU A 1 657 ? 14.627 69.154 69.069 1.00 34.03 ? 650 LEU A CG 1 ATOM 4851 C CD1 . LEU A 1 657 ? 13.102 69.045 68.796 1.00 28.02 ? 650 LEU A CD1 1 ATOM 4852 C CD2 . LEU A 1 657 ? 15.502 68.511 67.912 1.00 30.97 ? 650 LEU A CD2 1 ATOM 4853 N N . GLN A 1 658 ? 16.443 71.719 71.894 1.00 40.86 ? 651 GLN A N 1 ATOM 4854 C CA . GLN A 1 658 ? 17.257 71.552 73.106 1.00 46.45 ? 651 GLN A CA 1 ATOM 4855 C C . GLN A 1 658 ? 16.575 72.137 74.348 1.00 48.46 ? 651 GLN A C 1 ATOM 4856 O O . GLN A 1 658 ? 16.700 71.590 75.449 1.00 50.67 ? 651 GLN A O 1 ATOM 4857 C CB . GLN A 1 658 ? 18.619 72.250 72.949 1.00 47.69 ? 651 GLN A CB 1 ATOM 4858 C CG . GLN A 1 658 ? 19.553 71.623 71.904 1.00 52.01 ? 651 GLN A CG 1 ATOM 4859 C CD . GLN A 1 658 ? 20.379 70.456 72.441 1.00 58.71 ? 651 GLN A CD 1 ATOM 4860 O OE1 . GLN A 1 658 ? 20.365 69.366 71.873 1.00 61.79 ? 651 GLN A OE1 1 ATOM 4861 N NE2 . GLN A 1 658 ? 21.110 70.684 73.533 1.00 62.15 ? 651 GLN A NE2 1 ATOM 4862 N N . ASP A 1 659 ? 15.869 73.254 74.158 1.00 49.22 ? 652 ASP A N 1 ATOM 4863 C CA . ASP A 1 659 ? 15.419 74.150 75.229 1.00 50.98 ? 652 ASP A CA 1 ATOM 4864 C C . ASP A 1 659 ? 13.988 74.020 75.750 1.00 50.77 ? 652 ASP A C 1 ATOM 4865 O O . ASP A 1 659 ? 13.645 74.718 76.705 1.00 51.38 ? 652 ASP A O 1 ATOM 4866 C CB . ASP A 1 659 ? 15.606 75.615 74.801 1.00 51.86 ? 652 ASP A CB 1 ATOM 4867 C CG . ASP A 1 659 ? 17.080 76.043 74.764 1.00 56.57 ? 652 ASP A CG 1 ATOM 4868 O OD1 . ASP A 1 659 ? 17.340 77.201 74.345 1.00 61.07 ? 652 ASP A OD1 1 ATOM 4869 O OD2 . ASP A 1 659 ? 17.966 75.235 75.133 1.00 58.69 ? 652 ASP A OD2 1 ATOM 4870 N N . PHE A 1 660 ? 13.136 73.192 75.134 1.00 49.39 ? 653 PHE A N 1 ATOM 4871 C CA . PHE A 1 660 ? 11.801 72.911 75.730 1.00 49.24 ? 653 PHE A CA 1 ATOM 4872 C C . PHE A 1 660 ? 11.857 71.761 76.770 1.00 50.89 ? 653 PHE A C 1 ATOM 4873 O O . PHE A 1 660 ? 10.853 71.483 77.508 1.00 54.11 ? 653 PHE A O 1 ATOM 4874 C CB . PHE A 1 660 ? 10.777 72.607 74.616 1.00 47.26 ? 653 PHE A CB 1 ATOM 4875 C CG . PHE A 1 660 ? 10.796 71.184 74.151 1.00 42.14 ? 653 PHE A CG 1 ATOM 4876 C CD1 . PHE A 1 660 ? 9.806 70.305 74.546 1.00 39.13 ? 653 PHE A CD1 1 ATOM 4877 C CD2 . PHE A 1 660 ? 11.813 70.727 73.323 1.00 40.84 ? 653 PHE A CD2 1 ATOM 4878 C CE1 . PHE A 1 660 ? 9.815 68.985 74.124 1.00 43.08 ? 653 PHE A CE1 1 ATOM 4879 C CE2 . PHE A 1 660 ? 11.843 69.393 72.880 1.00 43.52 ? 653 PHE A CE2 1 ATOM 4880 C CZ . PHE A 1 660 ? 10.836 68.523 73.278 1.00 43.37 ? 653 PHE A CZ 1 ATOM 4881 N N A SER A 1 663 ? 8.918 69.044 80.106 0.50 27.50 ? 656 SER A N 1 ATOM 4882 N N B SER A 1 663 ? 8.326 66.455 79.093 0.50 26.09 ? 656 SER A N 1 ATOM 4883 C CA A SER A 1 663 ? 7.745 68.338 80.571 0.50 28.33 ? 656 SER A CA 1 ATOM 4884 C CA B SER A 1 663 ? 7.131 65.817 79.757 0.50 26.96 ? 656 SER A CA 1 ATOM 4885 C C A SER A 1 663 ? 6.464 68.465 79.677 0.50 27.56 ? 656 SER A C 1 ATOM 4886 C C B SER A 1 663 ? 5.742 66.495 79.509 0.50 28.05 ? 656 SER A C 1 ATOM 4887 O O A SER A 1 663 ? 5.419 67.901 80.018 0.50 27.90 ? 656 SER A O 1 ATOM 4888 O O B SER A 1 663 ? 4.726 66.185 80.187 0.50 27.97 ? 656 SER A O 1 ATOM 4889 C CB A SER A 1 663 ? 7.431 68.907 81.933 0.50 27.98 ? 656 SER A CB 1 ATOM 4890 C CB B SER A 1 663 ? 7.384 65.618 81.278 0.50 27.11 ? 656 SER A CB 1 ATOM 4891 O OG A SER A 1 663 ? 7.175 70.261 81.747 0.50 27.83 ? 656 SER A OG 1 ATOM 4892 O OG B SER A 1 663 ? 6.974 66.813 81.905 0.50 28.99 ? 656 SER A OG 1 ATOM 4893 N N A ASN A 1 664 ? 6.527 69.212 78.572 0.50 26.51 ? 657 ASN A N 1 ATOM 4894 N N B ASN A 1 664 ? 5.687 67.443 78.580 0.50 27.95 ? 657 ASN A N 1 ATOM 4895 C CA A ASN A 1 664 ? 5.332 69.480 77.756 0.50 26.08 ? 657 ASN A CA 1 ATOM 4896 C CA B ASN A 1 664 ? 4.395 68.015 78.150 0.50 29.98 ? 657 ASN A CA 1 ATOM 4897 C C A ASN A 1 664 ? 5.158 68.565 76.561 0.50 25.34 ? 657 ASN A C 1 ATOM 4898 C C B ASN A 1 664 ? 4.003 67.275 76.856 0.50 28.71 ? 657 ASN A C 1 ATOM 4899 O O A ASN A 1 664 ? 5.875 68.710 75.561 0.50 24.66 ? 657 ASN A O 1 ATOM 4900 O O B ASN A 1 664 ? 4.602 67.496 75.796 0.50 28.06 ? 657 ASN A O 1 ATOM 4901 C CB A ASN A 1 664 ? 5.331 70.907 77.238 0.50 26.24 ? 657 ASN A CB 1 ATOM 4902 C CB B ASN A 1 664 ? 4.507 69.555 77.965 0.50 30.41 ? 657 ASN A CB 1 ATOM 4903 C CG A ASN A 1 664 ? 3.987 71.303 76.678 0.50 25.55 ? 657 ASN A CG 1 ATOM 4904 C CG B ASN A 1 664 ? 3.149 70.250 77.642 0.50 32.77 ? 657 ASN A CG 1 ATOM 4905 O OD1 A ASN A 1 664 ? 3.300 70.493 76.060 0.50 25.39 ? 657 ASN A OD1 1 ATOM 4906 O OD1 B ASN A 1 664 ? 2.237 69.645 77.056 0.50 36.57 ? 657 ASN A OD1 1 ATOM 4907 N ND2 A ASN A 1 664 ? 3.594 72.525 76.921 0.50 28.87 ? 657 ASN A ND2 1 ATOM 4908 N ND2 B ASN A 1 664 ? 3.048 71.541 77.972 0.50 30.85 ? 657 ASN A ND2 1 ATOM 4909 N N A PRO A 1 665 ? 4.188 67.632 76.626 0.50 25.42 ? 658 PRO A N 1 ATOM 4910 N N B PRO A 1 665 ? 3.024 66.350 76.946 0.50 28.87 ? 658 PRO A N 1 ATOM 4911 C CA A PRO A 1 665 ? 4.117 66.692 75.506 0.50 24.44 ? 658 PRO A CA 1 ATOM 4912 C CA B PRO A 1 665 ? 2.753 65.447 75.815 0.50 27.65 ? 658 PRO A CA 1 ATOM 4913 C C A PRO A 1 665 ? 3.552 67.284 74.229 0.50 23.83 ? 658 PRO A C 1 ATOM 4914 C C B PRO A 1 665 ? 2.402 66.185 74.516 0.50 27.40 ? 658 PRO A C 1 ATOM 4915 O O A PRO A 1 665 ? 3.781 66.708 73.157 0.50 24.50 ? 658 PRO A O 1 ATOM 4916 O O B PRO A 1 665 ? 2.916 65.823 73.461 0.50 26.21 ? 658 PRO A O 1 ATOM 4917 C CB A PRO A 1 665 ? 3.162 65.601 76.016 0.50 23.69 ? 658 PRO A CB 1 ATOM 4918 C CB B PRO A 1 665 ? 1.557 64.617 76.288 0.50 28.94 ? 658 PRO A CB 1 ATOM 4919 C CG A PRO A 1 665 ? 2.223 66.364 76.910 0.50 24.57 ? 658 PRO A CG 1 ATOM 4920 C CG B PRO A 1 665 ? 1.486 64.819 77.770 0.50 29.03 ? 658 PRO A CG 1 ATOM 4921 C CD A PRO A 1 665 ? 3.134 67.370 77.628 0.50 26.64 ? 658 PRO A CD 1 ATOM 4922 C CD B PRO A 1 665 ? 2.174 66.079 78.121 0.50 29.06 ? 658 PRO A CD 1 ATOM 4923 N N A ILE A 1 666 ? 2.796 68.377 74.317 0.50 24.18 ? 659 ILE A N 1 ATOM 4924 N N B ILE A 1 666 ? 1.555 67.207 74.588 0.50 27.60 ? 659 ILE A N 1 ATOM 4925 C CA A ILE A 1 666 ? 2.251 68.973 73.088 0.50 23.08 ? 659 ILE A CA 1 ATOM 4926 C CA B ILE A 1 666 ? 1.183 67.908 73.361 0.50 27.74 ? 659 ILE A CA 1 ATOM 4927 C C A ILE A 1 666 ? 3.382 69.637 72.299 0.50 22.18 ? 659 ILE A C 1 ATOM 4928 C C B ILE A 1 666 ? 2.313 68.758 72.800 0.50 27.09 ? 659 ILE A C 1 ATOM 4929 O O A ILE A 1 666 ? 3.458 69.530 71.077 0.50 21.00 ? 659 ILE A O 1 ATOM 4930 O O B ILE A 1 666 ? 2.528 68.755 71.604 0.50 26.39 ? 659 ILE A O 1 ATOM 4931 C CB A ILE A 1 666 ? 1.141 70.037 73.287 0.50 24.14 ? 659 ILE A CB 1 ATOM 4932 C CB B ILE A 1 666 ? -0.185 68.583 73.426 0.50 28.19 ? 659 ILE A CB 1 ATOM 4933 C CG1 A ILE A 1 666 ? 0.142 69.674 74.401 0.50 26.05 ? 659 ILE A CG1 1 ATOM 4934 C CG1 B ILE A 1 666 ? -1.217 67.603 72.904 0.50 29.69 ? 659 ILE A CG1 1 ATOM 4935 C CG2 A ILE A 1 666 ? 0.436 70.293 71.903 0.50 21.29 ? 659 ILE A CG2 1 ATOM 4936 C CG2 B ILE A 1 666 ? -0.273 69.792 72.484 0.50 28.18 ? 659 ILE A CG2 1 ATOM 4937 C CD1 A ILE A 1 666 ? -0.789 68.520 74.038 0.50 26.60 ? 659 ILE A CD1 1 ATOM 4938 C CD1 B ILE A 1 666 ? -1.296 67.655 71.396 0.50 29.99 ? 659 ILE A CD1 1 ATOM 4939 N N A VAL A 1 667 ? 4.247 70.346 73.006 0.50 22.00 ? 660 VAL A N 1 ATOM 4940 N N B VAL A 1 667 ? 3.069 69.454 73.645 0.50 27.50 ? 660 VAL A N 1 ATOM 4941 C CA A VAL A 1 667 ? 5.382 70.978 72.358 0.50 22.33 ? 660 VAL A CA 1 ATOM 4942 C CA B VAL A 1 667 ? 4.233 70.191 73.124 0.50 26.63 ? 660 VAL A CA 1 ATOM 4943 C C A VAL A 1 667 ? 6.309 69.899 71.821 0.50 22.08 ? 660 VAL A C 1 ATOM 4944 C C B VAL A 1 667 ? 5.252 69.249 72.437 0.50 26.38 ? 660 VAL A C 1 ATOM 4945 O O A VAL A 1 667 ? 6.849 70.024 70.722 0.50 20.24 ? 660 VAL A O 1 ATOM 4946 O O B VAL A 1 667 ? 5.732 69.538 71.330 0.50 26.14 ? 660 VAL A O 1 ATOM 4947 C CB A VAL A 1 667 ? 6.146 71.892 73.321 0.50 22.90 ? 660 VAL A CB 1 ATOM 4948 C CB B VAL A 1 667 ? 4.919 71.090 74.204 0.50 27.40 ? 660 VAL A CB 1 ATOM 4949 C CG1 A VAL A 1 667 ? 7.437 72.391 72.679 0.50 22.36 ? 660 VAL A CG1 1 ATOM 4950 C CG1 B VAL A 1 667 ? 6.286 71.621 73.704 0.50 26.88 ? 660 VAL A CG1 1 ATOM 4951 C CG2 A VAL A 1 667 ? 5.258 73.039 73.692 0.50 23.73 ? 660 VAL A CG2 1 ATOM 4952 C CG2 B VAL A 1 667 ? 3.998 72.258 74.625 0.50 28.62 ? 660 VAL A CG2 1 ATOM 4953 N N A LEU A 1 668 ? 6.460 68.832 72.598 0.50 22.47 ? 661 LEU A N 1 ATOM 4954 N N B LEU A 1 668 ? 5.577 68.128 73.073 0.50 26.58 ? 661 LEU A N 1 ATOM 4955 C CA A LEU A 1 668 ? 7.297 67.708 72.185 0.50 22.73 ? 661 LEU A CA 1 ATOM 4956 C CA B LEU A 1 668 ? 6.478 67.157 72.455 0.50 26.23 ? 661 LEU A CA 1 ATOM 4957 C C A LEU A 1 668 ? 6.777 67.116 70.885 0.50 22.40 ? 661 LEU A C 1 ATOM 4958 C C B LEU A 1 668 ? 5.901 66.649 71.132 0.50 25.49 ? 661 LEU A C 1 ATOM 4959 O O A LEU A 1 668 ? 7.527 67.017 69.898 0.50 21.92 ? 661 LEU A O 1 ATOM 4960 O O B LEU A 1 668 ? 6.619 66.345 70.181 0.50 24.36 ? 661 LEU A O 1 ATOM 4961 C CB A LEU A 1 668 ? 7.394 66.636 73.298 0.50 23.36 ? 661 LEU A CB 1 ATOM 4962 C CB B LEU A 1 668 ? 6.753 65.996 73.422 0.50 26.99 ? 661 LEU A CB 1 ATOM 4963 C CG A LEU A 1 668 ? 7.959 65.238 72.928 0.50 22.83 ? 661 LEU A CG 1 ATOM 4964 C CG B LEU A 1 668 ? 7.490 64.754 72.882 0.50 25.71 ? 661 LEU A CG 1 ATOM 4965 C CD1 A LEU A 1 668 ? 9.415 65.304 72.522 0.50 18.20 ? 661 LEU A CD1 1 ATOM 4966 C CD1 B LEU A 1 668 ? 8.822 65.097 72.236 0.50 22.45 ? 661 LEU A CD1 1 ATOM 4967 C CD2 A LEU A 1 668 ? 7.809 64.247 74.095 0.50 21.58 ? 661 LEU A CD2 1 ATOM 4968 C CD2 B LEU A 1 668 ? 7.692 63.754 74.016 0.50 24.76 ? 661 LEU A CD2 1 ATOM 4969 N N A ARG A 1 669 ? 5.486 66.773 70.861 0.50 22.85 ? 662 ARG A N 1 ATOM 4970 N N B ARG A 1 669 ? 4.587 66.541 71.056 0.50 24.99 ? 662 ARG A N 1 ATOM 4971 C CA A ARG A 1 669 ? 4.886 66.126 69.703 0.50 22.37 ? 662 ARG A CA 1 ATOM 4972 C CA B ARG A 1 669 ? 4.004 66.066 69.802 0.50 24.35 ? 662 ARG A CA 1 ATOM 4973 C C A ARG A 1 669 ? 4.752 67.125 68.574 0.50 22.89 ? 662 ARG A C 1 ATOM 4974 C C B ARG A 1 669 ? 4.281 67.044 68.619 0.50 23.97 ? 662 ARG A C 1 ATOM 4975 O O A ARG A 1 669 ? 5.029 66.792 67.430 0.50 22.08 ? 662 ARG A O 1 ATOM 4976 O O B ARG A 1 669 ? 4.519 66.603 67.506 0.50 23.43 ? 662 ARG A O 1 ATOM 4977 C CB A ARG A 1 669 ? 3.511 65.546 70.020 0.50 22.18 ? 662 ARG A CB 1 ATOM 4978 C CB B ARG A 1 669 ? 2.518 65.747 70.009 0.50 24.45 ? 662 ARG A CB 1 ATOM 4979 C CG A ARG A 1 669 ? 2.696 65.247 68.767 0.50 21.23 ? 662 ARG A CG 1 ATOM 4980 C CG B ARG A 1 669 ? 1.799 65.229 68.774 0.50 22.49 ? 662 ARG A CG 1 ATOM 4981 C CD A ARG A 1 669 ? 3.033 63.903 68.161 0.50 19.88 ? 662 ARG A CD 1 ATOM 4982 C CD B ARG A 1 669 ? 1.888 63.713 68.595 0.50 26.99 ? 662 ARG A CD 1 ATOM 4983 N NE A ARG A 1 669 ? 1.864 63.471 67.416 0.50 23.17 ? 662 ARG A NE 1 ATOM 4984 N NE B ARG A 1 669 ? 0.733 63.315 67.779 0.50 26.75 ? 662 ARG A NE 1 ATOM 4985 C CZ A ARG A 1 669 ? 1.287 62.285 67.531 0.50 22.86 ? 662 ARG A CZ 1 ATOM 4986 C CZ B ARG A 1 669 ? 0.399 62.080 67.440 0.50 25.76 ? 662 ARG A CZ 1 ATOM 4987 N NH1 A ARG A 1 669 ? 1.824 61.324 68.292 0.50 23.29 ? 662 ARG A NH1 1 ATOM 4988 N NH1 B ARG A 1 669 ? 1.147 61.027 67.799 0.50 25.25 ? 662 ARG A NH1 1 ATOM 4989 N NH2 A ARG A 1 669 ? 0.190 62.061 66.828 0.50 23.30 ? 662 ARG A NH2 1 ATOM 4990 N NH2 B ARG A 1 669 ? -0.692 61.918 66.703 0.50 28.03 ? 662 ARG A NH2 1 ATOM 4991 N N . MET A 1 670 ? 4.347 68.352 68.907 1.00 24.48 ? 663 MET A N 1 ATOM 4992 C CA . MET A 1 670 ? 4.482 69.432 67.916 1.00 24.69 ? 663 MET A CA 1 ATOM 4993 C C . MET A 1 670 ? 5.870 69.393 67.288 1.00 25.45 ? 663 MET A C 1 ATOM 4994 O O . MET A 1 670 ? 6.002 69.398 66.050 1.00 24.50 ? 663 MET A O 1 ATOM 4995 C CB A MET A 1 670 ? 4.330 70.828 68.548 0.50 24.70 ? 663 MET A CB 1 ATOM 4996 C CB B MET A 1 670 ? 4.027 70.780 68.524 0.50 25.08 ? 663 MET A CB 1 ATOM 4997 C CG A MET A 1 670 ? 4.732 71.996 67.598 0.50 23.88 ? 663 MET A CG 1 ATOM 4998 C CG B MET A 1 670 ? 2.522 70.693 69.020 0.50 23.51 ? 663 MET A CG 1 ATOM 4999 S SD A MET A 1 670 ? 4.519 73.673 68.289 0.50 23.10 ? 663 MET A SD 1 ATOM 5000 S SD B MET A 1 670 ? 1.527 72.147 69.539 0.50 27.08 ? 663 MET A SD 1 ATOM 5001 C CE A MET A 1 670 ? 6.112 73.898 69.065 0.50 25.81 ? 663 MET A CE 1 ATOM 5002 C CE B MET A 1 670 ? 2.443 72.702 71.065 0.50 14.46 ? 663 MET A CE 1 ATOM 5003 N N . MET A 1 671 ? 6.919 69.341 68.127 1.00 24.98 ? 664 MET A N 1 ATOM 5004 C CA . MET A 1 671 ? 8.273 69.312 67.573 1.00 25.41 ? 664 MET A CA 1 ATOM 5005 C C . MET A 1 671 ? 8.611 68.007 66.835 1.00 24.30 ? 664 MET A C 1 ATOM 5006 O O . MET A 1 671 ? 9.323 68.031 65.838 1.00 24.13 ? 664 MET A O 1 ATOM 5007 C CB A MET A 1 671 ? 9.284 69.401 68.735 0.50 27.11 ? 664 MET A CB 1 ATOM 5008 C CB B MET A 1 671 ? 9.363 69.774 68.554 0.50 26.24 ? 664 MET A CB 1 ATOM 5009 C CG A MET A 1 671 ? 8.980 70.475 69.756 0.50 28.84 ? 664 MET A CG 1 ATOM 5010 C CG B MET A 1 671 ? 9.248 71.250 68.918 0.50 25.11 ? 664 MET A CG 1 ATOM 5011 S SD A MET A 1 671 ? 9.107 72.025 68.891 0.50 32.26 ? 664 MET A SD 1 ATOM 5012 S SD B MET A 1 671 ? 10.637 71.963 69.835 0.50 24.94 ? 664 MET A SD 1 ATOM 5013 C CE A MET A 1 671 ? 10.903 72.217 68.900 0.50 29.56 ? 664 MET A CE 1 ATOM 5014 C CE B MET A 1 671 ? 11.704 72.398 68.479 0.50 21.42 ? 664 MET A CE 1 ATOM 5015 N N . ASN A 1 672 ? 8.168 66.875 67.367 1.00 25.11 ? 665 ASN A N 1 ATOM 5016 C CA . ASN A 1 672 ? 8.371 65.603 66.675 1.00 24.58 ? 665 ASN A CA 1 ATOM 5017 C C . ASN A 1 672 ? 7.620 65.603 65.323 1.00 22.87 ? 665 ASN A C 1 ATOM 5018 O O . ASN A 1 672 ? 8.099 65.052 64.368 1.00 22.04 ? 665 ASN A O 1 ATOM 5019 C CB . ASN A 1 672 ? 7.849 64.462 67.510 1.00 25.17 ? 665 ASN A CB 1 ATOM 5020 C CG . ASN A 1 672 ? 8.894 63.944 68.488 1.00 26.48 ? 665 ASN A CG 1 ATOM 5021 O OD1 . ASN A 1 672 ? 10.110 64.119 68.249 1.00 25.87 ? 665 ASN A OD1 1 ATOM 5022 N ND2 . ASN A 1 672 ? 8.442 63.333 69.582 1.00 25.20 ? 665 ASN A ND2 1 ATOM 5023 N N . ASP A 1 673 ? 6.431 66.191 65.281 1.00 22.74 ? 666 ASP A N 1 ATOM 5024 C CA . ASP A 1 673 ? 5.740 66.358 63.993 1.00 21.92 ? 666 ASP A CA 1 ATOM 5025 C C . ASP A 1 673 ? 6.540 67.202 63.027 1.00 21.55 ? 666 ASP A C 1 ATOM 5026 O O . ASP A 1 673 ? 6.610 66.876 61.847 1.00 20.73 ? 666 ASP A O 1 ATOM 5027 C CB . ASP A 1 673 ? 4.318 66.945 64.155 1.00 21.66 ? 666 ASP A CB 1 ATOM 5028 C CG . ASP A 1 673 ? 3.321 65.917 64.649 1.00 25.01 ? 666 ASP A CG 1 ATOM 5029 O OD1 . ASP A 1 673 ? 3.738 64.746 64.797 1.00 25.85 ? 666 ASP A OD1 1 ATOM 5030 O OD2 . ASP A 1 673 ? 2.136 66.293 64.871 1.00 24.84 ? 666 ASP A OD2 1 ATOM 5031 N N . GLN A 1 674 ? 7.143 68.301 63.502 1.00 20.76 ? 667 GLN A N 1 ATOM 5032 C CA . GLN A 1 674 ? 7.995 69.105 62.623 1.00 21.14 ? 667 GLN A CA 1 ATOM 5033 C C . GLN A 1 674 ? 9.162 68.267 62.087 1.00 20.63 ? 667 GLN A C 1 ATOM 5034 O O . GLN A 1 674 ? 9.510 68.358 60.923 1.00 21.77 ? 667 GLN A O 1 ATOM 5035 C CB . GLN A 1 674 ? 8.512 70.372 63.340 1.00 20.59 ? 667 GLN A CB 1 ATOM 5036 C CG . GLN A 1 674 ? 7.346 71.398 63.493 1.00 22.55 ? 667 GLN A CG 1 ATOM 5037 C CD . GLN A 1 674 ? 7.795 72.645 64.227 1.00 24.12 ? 667 GLN A CD 1 ATOM 5038 O OE1 . GLN A 1 674 ? 7.885 72.657 65.452 1.00 26.15 ? 667 GLN A OE1 1 ATOM 5039 N NE2 . GLN A 1 674 ? 8.096 73.709 63.469 1.00 21.36 ? 667 GLN A NE2 1 ATOM 5040 N N . LEU A 1 675 ? 9.816 67.489 62.948 1.00 21.73 ? 668 LEU A N 1 ATOM 5041 C CA . LEU A 1 675 ? 10.851 66.568 62.453 1.00 21.07 ? 668 LEU A CA 1 ATOM 5042 C C . LEU A 1 675 ? 10.355 65.509 61.475 1.00 20.81 ? 668 LEU A C 1 ATOM 5043 O O . LEU A 1 675 ? 10.977 65.262 60.434 1.00 21.14 ? 668 LEU A O 1 ATOM 5044 C CB . LEU A 1 675 ? 11.505 65.868 63.652 1.00 22.40 ? 668 LEU A CB 1 ATOM 5045 C CG . LEU A 1 675 ? 12.385 66.834 64.470 1.00 24.99 ? 668 LEU A CG 1 ATOM 5046 C CD1 . LEU A 1 675 ? 12.777 66.150 65.753 1.00 25.82 ? 668 LEU A CD1 1 ATOM 5047 C CD2 . LEU A 1 675 ? 13.599 67.312 63.649 1.00 26.93 ? 668 LEU A CD2 1 ATOM 5048 N N . MET A 1 676 ? 9.206 64.916 61.774 1.00 21.62 ? 669 MET A N 1 ATOM 5049 C CA . MET A 1 676 ? 8.662 63.883 60.881 1.00 21.01 ? 669 MET A CA 1 ATOM 5050 C C . MET A 1 676 ? 8.285 64.453 59.511 1.00 20.81 ? 669 MET A C 1 ATOM 5051 O O . MET A 1 676 ? 8.553 63.829 58.482 1.00 19.18 ? 669 MET A O 1 ATOM 5052 C CB . MET A 1 676 ? 7.444 63.232 61.547 1.00 20.75 ? 669 MET A CB 1 ATOM 5053 C CG . MET A 1 676 ? 6.704 62.192 60.651 1.00 24.57 ? 669 MET A CG 1 ATOM 5054 S SD . MET A 1 676 ? 5.305 61.388 61.509 1.00 26.06 ? 669 MET A SD 1 ATOM 5055 C CE . MET A 1 676 ? 4.071 62.692 61.364 1.00 23.98 ? 669 MET A CE 1 ATOM 5056 N N . PHE A 1 677 ? 7.687 65.633 59.519 1.00 20.23 ? 670 PHE A N 1 ATOM 5057 C CA . PHE A 1 677 ? 7.156 66.232 58.260 1.00 19.88 ? 670 PHE A CA 1 ATOM 5058 C C . PHE A 1 677 ? 8.219 66.974 57.483 1.00 19.00 ? 670 PHE A C 1 ATOM 5059 O O . PHE A 1 677 ? 7.973 67.493 56.373 1.00 19.95 ? 670 PHE A O 1 ATOM 5060 C CB . PHE A 1 677 ? 5.963 67.119 58.568 1.00 18.43 ? 670 PHE A CB 1 ATOM 5061 C CG . PHE A 1 677 ? 4.668 66.349 58.825 1.00 21.54 ? 670 PHE A CG 1 ATOM 5062 C CD1 . PHE A 1 677 ? 4.171 65.416 57.879 1.00 19.65 ? 670 PHE A CD1 1 ATOM 5063 C CD2 . PHE A 1 677 ? 3.974 66.523 60.039 1.00 21.68 ? 670 PHE A CD2 1 ATOM 5064 C CE1 . PHE A 1 677 ? 2.979 64.684 58.124 1.00 18.30 ? 670 PHE A CE1 1 ATOM 5065 C CE2 . PHE A 1 677 ? 2.784 65.862 60.290 1.00 23.83 ? 670 PHE A CE2 1 ATOM 5066 C CZ . PHE A 1 677 ? 2.257 64.939 59.362 1.00 19.55 ? 670 PHE A CZ 1 ATOM 5067 N N . LEU A 1 678 ? 9.440 66.993 58.012 1.00 19.06 ? 671 LEU A N 1 ATOM 5068 C CA . LEU A 1 678 ? 10.496 67.716 57.302 1.00 19.49 ? 671 LEU A CA 1 ATOM 5069 C C . LEU A 1 678 ? 10.905 67.001 55.990 1.00 18.70 ? 671 LEU A C 1 ATOM 5070 O O . LEU A 1 678 ? 11.011 67.640 54.928 1.00 18.20 ? 671 LEU A O 1 ATOM 5071 C CB . LEU A 1 678 ? 11.737 67.963 58.220 1.00 19.27 ? 671 LEU A CB 1 ATOM 5072 C CG . LEU A 1 678 ? 12.907 68.636 57.498 1.00 21.23 ? 671 LEU A CG 1 ATOM 5073 C CD1 . LEU A 1 678 ? 12.474 70.032 56.957 1.00 22.34 ? 671 LEU A CD1 1 ATOM 5074 C CD2 . LEU A 1 678 ? 14.105 68.763 58.529 1.00 22.49 ? 671 LEU A CD2 1 ATOM 5075 N N . GLU A 1 679 ? 11.137 65.698 56.054 1.00 17.97 ? 672 GLU A N 1 ATOM 5076 C CA . GLU A 1 679 ? 11.312 64.950 54.781 1.00 17.73 ? 672 GLU A CA 1 ATOM 5077 C C . GLU A 1 679 ? 10.073 65.140 53.872 1.00 16.44 ? 672 GLU A C 1 ATOM 5078 O O . GLU A 1 679 ? 10.180 65.289 52.605 1.00 16.08 ? 672 GLU A O 1 ATOM 5079 C CB . GLU A 1 679 ? 11.496 63.450 55.063 1.00 16.83 ? 672 GLU A CB 1 ATOM 5080 C CG . GLU A 1 679 ? 12.100 62.750 53.809 1.00 16.43 ? 672 GLU A CG 1 ATOM 5081 C CD . GLU A 1 679 ? 13.623 63.036 53.707 1.00 22.33 ? 672 GLU A CD 1 ATOM 5082 O OE1 . GLU A 1 679 ? 14.350 62.637 54.642 1.00 18.61 ? 672 GLU A OE1 1 ATOM 5083 O OE2 . GLU A 1 679 ? 14.060 63.704 52.713 1.00 20.77 ? 672 GLU A OE2 1 ATOM 5084 N N . ARG A 1 680 ? 8.893 65.133 54.476 1.00 16.73 ? 673 ARG A N 1 ATOM 5085 C CA . ARG A 1 680 ? 7.651 65.254 53.681 1.00 15.30 ? 673 ARG A CA 1 ATOM 5086 C C . ARG A 1 680 ? 7.613 66.590 52.912 1.00 16.33 ? 673 ARG A C 1 ATOM 5087 O O . ARG A 1 680 ? 7.028 66.673 51.806 1.00 14.62 ? 673 ARG A O 1 ATOM 5088 C CB . ARG A 1 680 ? 6.391 65.164 54.596 1.00 17.33 ? 673 ARG A CB 1 ATOM 5089 C CG . ARG A 1 680 ? 5.177 64.520 53.853 1.00 17.25 ? 673 ARG A CG 1 ATOM 5090 C CD . ARG A 1 680 ? 5.350 62.938 53.993 1.00 20.22 ? 673 ARG A CD 1 ATOM 5091 N NE . ARG A 1 680 ? 4.949 62.462 55.358 1.00 18.17 ? 673 ARG A NE 1 ATOM 5092 C CZ . ARG A 1 680 ? 5.776 61.935 56.261 1.00 16.82 ? 673 ARG A CZ 1 ATOM 5093 N NH1 . ARG A 1 680 ? 7.109 61.798 56.031 1.00 16.58 ? 673 ARG A NH1 1 ATOM 5094 N NH2 . ARG A 1 680 ? 5.283 61.535 57.444 1.00 18.59 ? 673 ARG A NH2 1 ATOM 5095 N N . ALA A 1 681 ? 8.243 67.624 53.490 1.00 16.42 ? 674 ALA A N 1 ATOM 5096 C CA . ALA A 1 681 ? 8.189 68.979 52.917 1.00 17.68 ? 674 ALA A CA 1 ATOM 5097 C C . ALA A 1 681 ? 8.925 69.045 51.597 1.00 18.41 ? 674 ALA A C 1 ATOM 5098 O O . ALA A 1 681 ? 8.667 69.965 50.794 1.00 18.52 ? 674 ALA A O 1 ATOM 5099 C CB . ALA A 1 681 ? 8.773 70.007 53.909 1.00 17.83 ? 674 ALA A CB 1 ATOM 5100 N N . PHE A 1 682 ? 9.809 68.078 51.317 1.00 17.51 ? 675 PHE A N 1 ATOM 5101 C CA . PHE A 1 682 ? 10.522 68.094 50.018 1.00 18.05 ? 675 PHE A CA 1 ATOM 5102 C C . PHE A 1 682 ? 9.757 67.509 48.844 1.00 17.50 ? 675 PHE A C 1 ATOM 5103 O O . PHE A 1 682 ? 10.204 67.584 47.718 1.00 18.36 ? 675 PHE A O 1 ATOM 5104 C CB . PHE A 1 682 ? 11.877 67.430 50.143 1.00 18.72 ? 675 PHE A CB 1 ATOM 5105 C CG . PHE A 1 682 ? 12.809 68.177 51.028 1.00 18.21 ? 675 PHE A CG 1 ATOM 5106 C CD1 . PHE A 1 682 ? 13.247 69.444 50.675 1.00 18.01 ? 675 PHE A CD1 1 ATOM 5107 C CD2 . PHE A 1 682 ? 13.263 67.602 52.220 1.00 19.54 ? 675 PHE A CD2 1 ATOM 5108 C CE1 . PHE A 1 682 ? 14.165 70.159 51.543 1.00 16.51 ? 675 PHE A CE1 1 ATOM 5109 C CE2 . PHE A 1 682 ? 14.169 68.307 53.064 1.00 20.38 ? 675 PHE A CE2 1 ATOM 5110 C CZ . PHE A 1 682 ? 14.604 69.572 52.727 1.00 20.07 ? 675 PHE A CZ 1 ATOM 5111 N N . ILE A 1 683 ? 8.599 66.954 49.118 1.00 17.59 ? 676 ILE A N 1 ATOM 5112 C CA . ILE A 1 683 ? 7.702 66.415 48.066 1.00 17.03 ? 676 ILE A CA 1 ATOM 5113 C C . ILE A 1 683 ? 7.009 67.561 47.312 1.00 18.95 ? 676 ILE A C 1 ATOM 5114 O O . ILE A 1 683 ? 6.438 68.500 47.941 1.00 20.30 ? 676 ILE A O 1 ATOM 5115 C CB . ILE A 1 683 ? 6.639 65.530 48.781 1.00 16.27 ? 676 ILE A CB 1 ATOM 5116 C CG1 . ILE A 1 683 ? 7.339 64.299 49.374 1.00 15.23 ? 676 ILE A CG1 1 ATOM 5117 C CG2 . ILE A 1 683 ? 5.472 65.129 47.868 1.00 12.95 ? 676 ILE A CG2 1 ATOM 5118 C CD1 . ILE A 1 683 ? 8.051 63.407 48.284 1.00 15.03 ? 676 ILE A CD1 1 ATOM 5119 N N . ASP A 1 684 ? 7.017 67.489 45.977 1.00 18.18 ? 677 ASP A N 1 ATOM 5120 C CA . ASP A 1 684 ? 6.222 68.359 45.146 1.00 18.68 ? 677 ASP A CA 1 ATOM 5121 C C . ASP A 1 684 ? 5.073 67.522 44.620 1.00 18.53 ? 677 ASP A C 1 ATOM 5122 O O . ASP A 1 684 ? 5.311 66.500 43.967 1.00 18.06 ? 677 ASP A O 1 ATOM 5123 C CB . ASP A 1 684 ? 7.064 68.829 43.962 1.00 18.30 ? 677 ASP A CB 1 ATOM 5124 C CG . ASP A 1 684 ? 6.380 69.863 43.128 1.00 20.92 ? 677 ASP A CG 1 ATOM 5125 O OD1 . ASP A 1 684 ? 5.135 69.874 43.019 1.00 17.75 ? 677 ASP A OD1 1 ATOM 5126 O OD2 . ASP A 1 684 ? 7.127 70.673 42.542 1.00 20.21 ? 677 ASP A OD2 1 ATOM 5127 N N . PRO A 1 685 ? 3.846 67.911 44.929 1.00 20.07 ? 678 PRO A N 1 ATOM 5128 C CA . PRO A 1 685 ? 2.701 67.092 44.478 1.00 22.13 ? 678 PRO A CA 1 ATOM 5129 C C . PRO A 1 685 ? 2.552 67.018 42.945 1.00 22.69 ? 678 PRO A C 1 ATOM 5130 O O . PRO A 1 685 ? 1.867 66.160 42.447 1.00 25.74 ? 678 PRO A O 1 ATOM 5131 C CB . PRO A 1 685 ? 1.477 67.799 45.103 1.00 21.40 ? 678 PRO A CB 1 ATOM 5132 C CG . PRO A 1 685 ? 1.910 69.194 45.398 1.00 21.87 ? 678 PRO A CG 1 ATOM 5133 C CD . PRO A 1 685 ? 3.435 69.157 45.624 1.00 20.73 ? 678 PRO A CD 1 ATOM 5134 N N . LEU A 1 686 ? 3.235 67.871 42.199 1.00 22.10 ? 679 LEU A N 1 ATOM 5135 C CA . LEU A 1 686 ? 3.194 67.793 40.736 1.00 19.99 ? 679 LEU A CA 1 ATOM 5136 C C . LEU A 1 686 ? 4.245 66.820 40.138 1.00 20.70 ? 679 LEU A C 1 ATOM 5137 O O . LEU A 1 686 ? 4.211 66.550 38.928 1.00 19.47 ? 679 LEU A O 1 ATOM 5138 C CB . LEU A 1 686 ? 3.373 69.202 40.155 1.00 20.24 ? 679 LEU A CB 1 ATOM 5139 C CG . LEU A 1 686 ? 2.259 70.233 40.537 1.00 21.44 ? 679 LEU A CG 1 ATOM 5140 C CD1 . LEU A 1 686 ? 2.489 71.585 39.872 1.00 18.56 ? 679 LEU A CD1 1 ATOM 5141 C CD2 . LEU A 1 686 ? 0.818 69.737 40.159 1.00 22.74 ? 679 LEU A CD2 1 ATOM 5142 N N . GLY A 1 687 ? 5.152 66.333 40.995 1.00 21.06 ? 680 GLY A N 1 ATOM 5143 C CA . GLY A 1 687 ? 6.199 65.384 40.606 1.00 20.92 ? 680 GLY A CA 1 ATOM 5144 C C . GLY A 1 687 ? 7.248 66.038 39.718 1.00 22.34 ? 680 GLY A C 1 ATOM 5145 O O . GLY A 1 687 ? 7.179 67.224 39.428 1.00 22.83 ? 680 GLY A O 1 ATOM 5146 N N . LEU A 1 688 ? 8.229 65.255 39.279 1.00 21.07 ? 681 LEU A N 1 ATOM 5147 C CA . LEU A 1 688 ? 9.240 65.769 38.370 1.00 22.17 ? 681 LEU A CA 1 ATOM 5148 C C . LEU A 1 688 ? 8.757 65.588 36.929 1.00 22.70 ? 681 LEU A C 1 ATOM 5149 O O . LEU A 1 688 ? 7.819 64.773 36.656 1.00 22.43 ? 681 LEU A O 1 ATOM 5150 C CB . LEU A 1 688 ? 10.585 65.023 38.641 1.00 22.31 ? 681 LEU A CB 1 ATOM 5151 C CG . LEU A 1 688 ? 11.262 65.351 40.006 1.00 23.27 ? 681 LEU A CG 1 ATOM 5152 C CD1 . LEU A 1 688 ? 12.338 64.300 40.293 1.00 24.19 ? 681 LEU A CD1 1 ATOM 5153 C CD2 . LEU A 1 688 ? 11.821 66.823 40.085 1.00 22.99 ? 681 LEU A CD2 1 ATOM 5154 N N . PRO A 1 689 ? 9.349 66.358 35.977 1.00 24.60 ? 682 PRO A N 1 ATOM 5155 C CA . PRO A 1 689 ? 8.877 66.294 34.584 1.00 24.89 ? 682 PRO A CA 1 ATOM 5156 C C . PRO A 1 689 ? 8.788 64.879 34.028 1.00 25.17 ? 682 PRO A C 1 ATOM 5157 O O . PRO A 1 689 ? 9.793 64.154 34.002 1.00 26.23 ? 682 PRO A O 1 ATOM 5158 C CB . PRO A 1 689 ? 9.920 67.157 33.798 1.00 26.01 ? 682 PRO A CB 1 ATOM 5159 C CG . PRO A 1 689 ? 10.346 68.184 34.796 1.00 26.86 ? 682 PRO A CG 1 ATOM 5160 C CD . PRO A 1 689 ? 10.428 67.365 36.142 1.00 24.63 ? 682 PRO A CD 1 ATOM 5161 N N . ASP A 1 690 ? 7.584 64.504 33.593 1.00 25.88 ? 683 ASP A N 1 ATOM 5162 C CA . ASP A 1 690 ? 7.252 63.197 32.989 1.00 26.39 ? 683 ASP A CA 1 ATOM 5163 C C . ASP A 1 690 ? 7.543 62.033 33.914 1.00 23.94 ? 683 ASP A C 1 ATOM 5164 O O . ASP A 1 690 ? 7.502 60.886 33.481 1.00 22.91 ? 683 ASP A O 1 ATOM 5165 C CB . ASP A 1 690 ? 8.007 62.970 31.681 1.00 28.89 ? 683 ASP A CB 1 ATOM 5166 C CG . ASP A 1 690 ? 7.694 64.037 30.655 1.00 35.67 ? 683 ASP A CG 1 ATOM 5167 O OD1 . ASP A 1 690 ? 6.498 64.369 30.476 1.00 36.87 ? 683 ASP A OD1 1 ATOM 5168 O OD2 . ASP A 1 690 ? 8.656 64.543 30.065 1.00 41.26 ? 683 ASP A OD2 1 ATOM 5169 N N . ARG A 1 691 ? 7.808 62.331 35.182 1.00 22.87 ? 684 ARG A N 1 ATOM 5170 C CA . ARG A 1 691 ? 8.003 61.273 36.199 1.00 21.27 ? 684 ARG A CA 1 ATOM 5171 C C . ARG A 1 691 ? 7.127 61.604 37.440 1.00 20.36 ? 684 ARG A C 1 ATOM 5172 O O . ARG A 1 691 ? 7.633 61.988 38.531 1.00 19.04 ? 684 ARG A O 1 ATOM 5173 C CB . ARG A 1 691 ? 9.501 61.072 36.542 1.00 22.51 ? 684 ARG A CB 1 ATOM 5174 C CG . ARG A 1 691 ? 10.338 60.512 35.358 1.00 21.68 ? 684 ARG A CG 1 ATOM 5175 C CD . ARG A 1 691 ? 11.810 60.149 35.704 1.00 26.04 ? 684 ARG A CD 1 ATOM 5176 N NE . ARG A 1 691 ? 12.555 61.274 36.333 1.00 24.93 ? 684 ARG A NE 1 ATOM 5177 C CZ . ARG A 1 691 ? 13.735 61.183 36.970 1.00 25.92 ? 684 ARG A CZ 1 ATOM 5178 N NH1 . ARG A 1 691 ? 14.388 60.006 37.067 1.00 19.25 ? 684 ARG A NH1 1 ATOM 5179 N NH2 . ARG A 1 691 ? 14.320 62.304 37.470 1.00 22.50 ? 684 ARG A NH2 1 ATOM 5180 N N . PRO A 1 692 ? 5.826 61.407 37.293 1.00 19.49 ? 685 PRO A N 1 ATOM 5181 C CA . PRO A 1 692 ? 4.901 61.860 38.345 1.00 19.64 ? 685 PRO A CA 1 ATOM 5182 C C . PRO A 1 692 ? 5.041 61.147 39.702 1.00 18.48 ? 685 PRO A C 1 ATOM 5183 O O . PRO A 1 692 ? 4.646 61.724 40.710 1.00 18.34 ? 685 PRO A O 1 ATOM 5184 C CB . PRO A 1 692 ? 3.495 61.607 37.736 1.00 21.33 ? 685 PRO A CB 1 ATOM 5185 C CG . PRO A 1 692 ? 3.702 60.546 36.655 1.00 21.82 ? 685 PRO A CG 1 ATOM 5186 C CD . PRO A 1 692 ? 5.108 60.865 36.099 1.00 21.04 ? 685 PRO A CD 1 ATOM 5187 N N . PHE A 1 693 ? 5.626 59.955 39.722 1.00 17.67 ? 686 PHE A N 1 ATOM 5188 C CA . PHE A 1 693 ? 5.854 59.203 40.966 1.00 18.05 ? 686 PHE A CA 1 ATOM 5189 C C . PHE A 1 693 ? 7.178 59.473 41.659 1.00 17.07 ? 686 PHE A C 1 ATOM 5190 O O . PHE A 1 693 ? 7.418 59.013 42.790 1.00 17.31 ? 686 PHE A O 1 ATOM 5191 C CB . PHE A 1 693 ? 5.593 57.701 40.751 1.00 16.97 ? 686 PHE A CB 1 ATOM 5192 C CG . PHE A 1 693 ? 4.193 57.448 40.307 1.00 17.02 ? 686 PHE A CG 1 ATOM 5193 C CD1 . PHE A 1 693 ? 3.102 57.853 41.120 1.00 17.48 ? 686 PHE A CD1 1 ATOM 5194 C CD2 . PHE A 1 693 ? 3.948 56.879 39.062 1.00 18.12 ? 686 PHE A CD2 1 ATOM 5195 C CE1 . PHE A 1 693 ? 1.789 57.654 40.627 1.00 17.18 ? 686 PHE A CE1 1 ATOM 5196 C CE2 . PHE A 1 693 ? 2.661 56.683 38.589 1.00 17.85 ? 686 PHE A CE2 1 ATOM 5197 C CZ . PHE A 1 693 ? 1.599 57.062 39.382 1.00 17.87 ? 686 PHE A CZ 1 ATOM 5198 N N . TYR A 1 694 ? 8.010 60.274 41.004 1.00 16.29 ? 687 TYR A N 1 ATOM 5199 C CA . TYR A 1 694 ? 9.190 60.807 41.687 1.00 16.88 ? 687 TYR A CA 1 ATOM 5200 C C . TYR A 1 694 ? 8.883 62.256 42.056 1.00 16.56 ? 687 TYR A C 1 ATOM 5201 O O . TYR A 1 694 ? 8.969 63.149 41.222 1.00 18.06 ? 687 TYR A O 1 ATOM 5202 C CB . TYR A 1 694 ? 10.420 60.741 40.753 1.00 17.05 ? 687 TYR A CB 1 ATOM 5203 C CG . TYR A 1 694 ? 10.865 59.309 40.451 1.00 16.98 ? 687 TYR A CG 1 ATOM 5204 C CD1 . TYR A 1 694 ? 10.613 58.253 41.369 1.00 14.61 ? 687 TYR A CD1 1 ATOM 5205 C CD2 . TYR A 1 694 ? 11.581 59.018 39.289 1.00 19.83 ? 687 TYR A CD2 1 ATOM 5206 C CE1 . TYR A 1 694 ? 10.996 56.951 41.093 1.00 15.95 ? 687 TYR A CE1 1 ATOM 5207 C CE2 . TYR A 1 694 ? 12.004 57.686 38.995 1.00 20.94 ? 687 TYR A CE2 1 ATOM 5208 C CZ . TYR A 1 694 ? 11.727 56.684 39.931 1.00 19.25 ? 687 TYR A CZ 1 ATOM 5209 O OH . TYR A 1 694 ? 12.162 55.401 39.697 1.00 20.58 ? 687 TYR A OH 1 ATOM 5210 N N . ARG A 1 695 ? 8.541 62.479 43.329 1.00 16.97 ? 688 ARG A N 1 ATOM 5211 C CA . ARG A 1 695 ? 8.012 63.763 43.767 1.00 16.04 ? 688 ARG A CA 1 ATOM 5212 C C . ARG A 1 695 ? 9.013 64.491 44.697 1.00 17.57 ? 688 ARG A C 1 ATOM 5213 O O . ARG A 1 695 ? 8.761 65.654 45.086 1.00 17.11 ? 688 ARG A O 1 ATOM 5214 C CB . ARG A 1 695 ? 6.732 63.498 44.552 1.00 15.91 ? 688 ARG A CB 1 ATOM 5215 C CG . ARG A 1 695 ? 5.757 62.697 43.659 1.00 16.10 ? 688 ARG A CG 1 ATOM 5216 C CD . ARG A 1 695 ? 4.295 62.861 44.107 1.00 20.09 ? 688 ARG A CD 1 ATOM 5217 N NE . ARG A 1 695 ? 4.141 62.459 45.501 1.00 20.68 ? 688 ARG A NE 1 ATOM 5218 C CZ . ARG A 1 695 ? 3.103 62.768 46.288 1.00 25.36 ? 688 ARG A CZ 1 ATOM 5219 N NH1 . ARG A 1 695 ? 3.099 62.348 47.571 1.00 20.40 ? 688 ARG A NH1 1 ATOM 5220 N NH2 . ARG A 1 695 ? 2.080 63.497 45.806 1.00 20.61 ? 688 ARG A NH2 1 ATOM 5221 N N . HIS A 1 696 ? 10.090 63.816 45.082 1.00 16.76 ? 689 HIS A N 1 ATOM 5222 C CA . HIS A 1 696 ? 11.065 64.448 46.023 1.00 16.84 ? 689 HIS A CA 1 ATOM 5223 C C . HIS A 1 696 ? 11.911 65.416 45.169 1.00 17.36 ? 689 HIS A C 1 ATOM 5224 O O . HIS A 1 696 ? 12.412 65.038 44.128 1.00 16.30 ? 689 HIS A O 1 ATOM 5225 C CB . HIS A 1 696 ? 11.979 63.402 46.686 1.00 17.82 ? 689 HIS A CB 1 ATOM 5226 C CG . HIS A 1 696 ? 12.612 63.825 47.987 1.00 17.20 ? 689 HIS A CG 1 ATOM 5227 N ND1 . HIS A 1 696 ? 13.617 64.775 48.079 1.00 16.55 ? 689 HIS A ND1 1 ATOM 5228 C CD2 . HIS A 1 696 ? 12.451 63.333 49.242 1.00 18.37 ? 689 HIS A CD2 1 ATOM 5229 C CE1 . HIS A 1 696 ? 14.015 64.875 49.337 1.00 18.88 ? 689 HIS A CE1 1 ATOM 5230 N NE2 . HIS A 1 696 ? 13.320 64.014 50.067 1.00 18.22 ? 689 HIS A NE2 1 ATOM 5231 N N . VAL A 1 697 ? 12.084 66.651 45.618 1.00 17.05 ? 690 VAL A N 1 ATOM 5232 C CA . VAL A 1 697 ? 12.742 67.693 44.777 1.00 17.17 ? 690 VAL A CA 1 ATOM 5233 C C . VAL A 1 697 ? 14.258 67.665 45.024 1.00 18.87 ? 690 VAL A C 1 ATOM 5234 O O . VAL A 1 697 ? 15.050 68.138 44.212 1.00 18.49 ? 690 VAL A O 1 ATOM 5235 C CB . VAL A 1 697 ? 12.117 69.105 45.115 1.00 17.46 ? 690 VAL A CB 1 ATOM 5236 C CG1 . VAL A 1 697 ? 12.886 70.276 44.426 1.00 17.84 ? 690 VAL A CG1 1 ATOM 5237 C CG2 . VAL A 1 697 ? 10.620 69.154 44.676 1.00 17.42 ? 690 VAL A CG2 1 ATOM 5238 N N . ILE A 1 698 ? 14.674 67.075 46.136 1.00 17.67 ? 691 ILE A N 1 ATOM 5239 C CA . ILE A 1 698 ? 16.103 67.060 46.403 1.00 17.23 ? 691 ILE A CA 1 ATOM 5240 C C . ILE A 1 698 ? 16.764 65.855 45.804 1.00 18.01 ? 691 ILE A C 1 ATOM 5241 O O . ILE A 1 698 ? 17.900 65.949 45.365 1.00 19.52 ? 691 ILE A O 1 ATOM 5242 C CB . ILE A 1 698 ? 16.419 67.094 47.918 1.00 17.73 ? 691 ILE A CB 1 ATOM 5243 C CG1 . ILE A 1 698 ? 15.654 68.247 48.620 1.00 16.33 ? 691 ILE A CG1 1 ATOM 5244 C CG2 . ILE A 1 698 ? 17.959 67.278 48.212 1.00 19.12 ? 691 ILE A CG2 1 ATOM 5245 C CD1 . ILE A 1 698 ? 15.883 69.653 48.005 1.00 18.53 ? 691 ILE A CD1 1 ATOM 5246 N N . TYR A 1 699 ? 16.065 64.721 45.819 1.00 18.56 ? 692 TYR A N 1 ATOM 5247 C CA . TYR A 1 699 ? 16.643 63.445 45.402 1.00 18.66 ? 692 TYR A CA 1 ATOM 5248 C C . TYR A 1 699 ? 15.735 62.757 44.403 1.00 19.40 ? 692 TYR A C 1 ATOM 5249 O O . TYR A 1 699 ? 14.525 62.703 44.622 1.00 22.48 ? 692 TYR A O 1 ATOM 5250 C CB . TYR A 1 699 ? 16.722 62.497 46.624 1.00 18.22 ? 692 TYR A CB 1 ATOM 5251 C CG . TYR A 1 699 ? 17.741 62.942 47.649 1.00 19.88 ? 692 TYR A CG 1 ATOM 5252 C CD1 . TYR A 1 699 ? 19.114 62.959 47.320 1.00 21.57 ? 692 TYR A CD1 1 ATOM 5253 C CD2 . TYR A 1 699 ? 17.344 63.298 48.968 1.00 19.44 ? 692 TYR A CD2 1 ATOM 5254 C CE1 . TYR A 1 699 ? 20.054 63.341 48.272 1.00 20.71 ? 692 TYR A CE1 1 ATOM 5255 C CE2 . TYR A 1 699 ? 18.285 63.705 49.912 1.00 19.98 ? 692 TYR A CE2 1 ATOM 5256 C CZ . TYR A 1 699 ? 19.619 63.728 49.550 1.00 23.31 ? 692 TYR A CZ 1 ATOM 5257 O OH . TYR A 1 699 ? 20.545 64.064 50.508 1.00 23.61 ? 692 TYR A OH 1 ATOM 5258 N N . ALA A 1 700 ? 16.304 62.153 43.360 1.00 18.61 ? 693 ALA A N 1 ATOM 5259 C CA . ALA A 1 700 ? 15.525 61.180 42.569 1.00 18.18 ? 693 ALA A CA 1 ATOM 5260 C C . ALA A 1 700 ? 16.537 60.196 42.018 1.00 18.75 ? 693 ALA A C 1 ATOM 5261 O O . ALA A 1 700 ? 17.753 60.479 42.008 1.00 18.80 ? 693 ALA A O 1 ATOM 5262 C CB . ALA A 1 700 ? 14.773 61.885 41.402 1.00 18.91 ? 693 ALA A CB 1 ATOM 5263 N N . PRO A 1 701 ? 16.065 59.044 41.563 1.00 18.43 ? 694 PRO A N 1 ATOM 5264 C CA . PRO A 1 701 ? 16.940 58.088 40.915 1.00 20.15 ? 694 PRO A CA 1 ATOM 5265 C C . PRO A 1 701 ? 17.417 58.779 39.650 1.00 20.38 ? 694 PRO A C 1 ATOM 5266 O O . PRO A 1 701 ? 16.600 59.494 39.000 1.00 20.79 ? 694 PRO A O 1 ATOM 5267 C CB . PRO A 1 701 ? 15.970 56.961 40.502 1.00 19.20 ? 694 PRO A CB 1 ATOM 5268 C CG . PRO A 1 701 ? 14.877 57.065 41.517 1.00 17.87 ? 694 PRO A CG 1 ATOM 5269 C CD . PRO A 1 701 ? 14.680 58.552 41.644 1.00 17.51 ? 694 PRO A CD 1 ATOM 5270 N N . SER A 1 702 ? 18.689 58.590 39.302 1.00 20.41 ? 695 SER A N 1 ATOM 5271 C CA . SER A 1 702 ? 19.244 59.216 38.115 1.00 21.06 ? 695 SER A CA 1 ATOM 5272 C C . SER A 1 702 ? 18.458 58.756 36.881 1.00 21.82 ? 695 SER A C 1 ATOM 5273 O O . SER A 1 702 ? 18.150 57.570 36.761 1.00 20.99 ? 695 SER A O 1 ATOM 5274 C CB . SER A 1 702 ? 20.701 58.779 37.898 1.00 21.88 ? 695 SER A CB 1 ATOM 5275 O OG . SER A 1 702 ? 21.126 59.177 36.614 1.00 22.43 ? 695 SER A OG 1 ATOM 5276 N N . SER A 1 703 ? 18.183 59.675 35.935 1.00 21.78 ? 696 SER A N 1 ATOM 5277 C CA . SER A 1 703 ? 17.500 59.292 34.692 1.00 22.07 ? 696 SER A CA 1 ATOM 5278 C C . SER A 1 703 ? 18.323 58.351 33.800 1.00 23.22 ? 696 SER A C 1 ATOM 5279 O O . SER A 1 703 ? 17.780 57.710 32.865 1.00 23.14 ? 696 SER A O 1 ATOM 5280 C CB . SER A 1 703 ? 17.047 60.550 33.904 1.00 22.02 ? 696 SER A CB 1 ATOM 5281 O OG A SER A 1 703 ? 16.078 61.254 34.652 0.50 15.82 ? 696 SER A OG 1 ATOM 5282 O OG B SER A 1 703 ? 18.133 61.380 33.587 0.50 27.62 ? 696 SER A OG 1 ATOM 5283 N N . HIS A 1 704 ? 19.615 58.280 34.074 1.00 22.15 ? 697 HIS A N 1 ATOM 5284 C CA . HIS A 1 704 ? 20.514 57.395 33.339 1.00 23.09 ? 697 HIS A CA 1 ATOM 5285 C C . HIS A 1 704 ? 20.888 56.123 34.084 1.00 24.20 ? 697 HIS A C 1 ATOM 5286 O O . HIS A 1 704 ? 21.542 55.234 33.511 1.00 25.26 ? 697 HIS A O 1 ATOM 5287 C CB . HIS A 1 704 ? 21.791 58.184 33.013 1.00 24.50 ? 697 HIS A CB 1 ATOM 5288 C CG . HIS A 1 704 ? 21.499 59.494 32.363 1.00 26.97 ? 697 HIS A CG 1 ATOM 5289 N ND1 . HIS A 1 704 ? 21.294 59.611 31.004 1.00 25.59 ? 697 HIS A ND1 1 ATOM 5290 C CD2 . HIS A 1 704 ? 21.312 60.733 32.882 1.00 29.05 ? 697 HIS A CD2 1 ATOM 5291 C CE1 . HIS A 1 704 ? 21.005 60.864 30.711 1.00 30.07 ? 697 HIS A CE1 1 ATOM 5292 N NE2 . HIS A 1 704 ? 21.015 61.569 31.830 1.00 28.86 ? 697 HIS A NE2 1 ATOM 5293 N N . ASN A 1 705 ? 20.501 56.022 35.358 1.00 21.75 ? 698 ASN A N 1 ATOM 5294 C CA . ASN A 1 705 ? 20.867 54.838 36.170 1.00 21.80 ? 698 ASN A CA 1 ATOM 5295 C C . ASN A 1 705 ? 19.992 54.804 37.415 1.00 20.73 ? 698 ASN A C 1 ATOM 5296 O O . ASN A 1 705 ? 20.274 55.459 38.393 1.00 20.14 ? 698 ASN A O 1 ATOM 5297 C CB . ASN A 1 705 ? 22.364 54.901 36.577 1.00 23.08 ? 698 ASN A CB 1 ATOM 5298 C CG . ASN A 1 705 ? 22.762 53.808 37.551 1.00 22.56 ? 698 ASN A CG 1 ATOM 5299 O OD1 . ASN A 1 705 ? 22.025 52.837 37.742 1.00 21.36 ? 698 ASN A OD1 1 ATOM 5300 N ND2 . ASN A 1 705 ? 23.924 53.981 38.201 1.00 21.79 ? 698 ASN A ND2 1 ATOM 5301 N N . LYS A 1 706 ? 18.923 54.017 37.373 1.00 20.55 ? 699 LYS A N 1 ATOM 5302 C CA . LYS A 1 706 ? 17.966 53.954 38.479 1.00 19.34 ? 699 LYS A CA 1 ATOM 5303 C C . LYS A 1 706 ? 18.624 53.678 39.841 1.00 20.12 ? 699 LYS A C 1 ATOM 5304 O O . LYS A 1 706 ? 18.091 54.071 40.889 1.00 20.19 ? 699 LYS A O 1 ATOM 5305 C CB . LYS A 1 706 ? 16.964 52.831 38.155 1.00 21.07 ? 699 LYS A CB 1 ATOM 5306 C CG . LYS A 1 706 ? 15.786 52.815 39.072 1.00 22.36 ? 699 LYS A CG 1 ATOM 5307 C CD . LYS A 1 706 ? 14.803 51.734 38.579 1.00 21.86 ? 699 LYS A CD 1 ATOM 5308 C CE . LYS A 1 706 ? 13.458 51.917 39.310 1.00 22.09 ? 699 LYS A CE 1 ATOM 5309 N NZ . LYS A 1 706 ? 12.557 50.713 39.135 1.00 20.10 ? 699 LYS A NZ 1 ATOM 5310 N N . TYR A 1 707 ? 19.765 52.988 39.831 1.00 20.63 ? 700 TYR A N 1 ATOM 5311 C CA . TYR A 1 707 ? 20.420 52.649 41.104 1.00 21.24 ? 700 TYR A CA 1 ATOM 5312 C C . TYR A 1 707 ? 21.041 53.868 41.798 1.00 21.42 ? 700 TYR A C 1 ATOM 5313 O O . TYR A 1 707 ? 21.263 53.832 42.991 1.00 21.16 ? 700 TYR A O 1 ATOM 5314 C CB . TYR A 1 707 ? 21.552 51.641 40.891 1.00 20.79 ? 700 TYR A CB 1 ATOM 5315 C CG . TYR A 1 707 ? 21.112 50.217 40.520 1.00 21.52 ? 700 TYR A CG 1 ATOM 5316 C CD1 . TYR A 1 707 ? 19.992 49.619 41.137 1.00 23.35 ? 700 TYR A CD1 1 ATOM 5317 C CD2 . TYR A 1 707 ? 21.852 49.474 39.588 1.00 23.92 ? 700 TYR A CD2 1 ATOM 5318 C CE1 . TYR A 1 707 ? 19.566 48.283 40.764 1.00 21.36 ? 700 TYR A CE1 1 ATOM 5319 C CE2 . TYR A 1 707 ? 21.478 48.141 39.223 1.00 24.14 ? 700 TYR A CE2 1 ATOM 5320 C CZ . TYR A 1 707 ? 20.330 47.568 39.822 1.00 24.27 ? 700 TYR A CZ 1 ATOM 5321 O OH . TYR A 1 707 ? 19.998 46.292 39.450 1.00 20.85 ? 700 TYR A OH 1 ATOM 5322 N N . ALA A 1 708 ? 21.449 54.867 41.017 1.00 21.80 ? 701 ALA A N 1 ATOM 5323 C CA . ALA A 1 708 ? 22.173 56.033 41.580 1.00 22.65 ? 701 ALA A CA 1 ATOM 5324 C C . ALA A 1 708 ? 21.189 57.144 41.990 1.00 23.44 ? 701 ALA A C 1 ATOM 5325 O O . ALA A 1 708 ? 20.199 57.408 41.273 1.00 24.00 ? 701 ALA A O 1 ATOM 5326 C CB . ALA A 1 708 ? 23.211 56.568 40.545 1.00 23.10 ? 701 ALA A CB 1 ATOM 5327 N N . GLY A 1 709 ? 21.418 57.787 43.136 1.00 23.24 ? 702 GLY A N 1 ATOM 5328 C CA . GLY A 1 709 ? 20.611 58.961 43.452 1.00 24.49 ? 702 GLY A CA 1 ATOM 5329 C C . GLY A 1 709 ? 21.203 60.188 42.774 1.00 24.25 ? 702 GLY A C 1 ATOM 5330 O O . GLY A 1 709 ? 22.430 60.281 42.608 1.00 25.66 ? 702 GLY A O 1 ATOM 5331 N N . GLU A 1 710 ? 20.350 61.100 42.328 1.00 22.18 ? 703 GLU A N 1 ATOM 5332 C CA . GLU A 1 710 ? 20.831 62.361 41.764 1.00 22.78 ? 703 GLU A CA 1 ATOM 5333 C C . GLU A 1 710 ? 20.292 63.456 42.683 1.00 22.39 ? 703 GLU A C 1 ATOM 5334 O O . GLU A 1 710 ? 19.127 63.373 43.107 1.00 20.62 ? 703 GLU A O 1 ATOM 5335 C CB . GLU A 1 710 ? 20.305 62.555 40.338 1.00 23.50 ? 703 GLU A CB 1 ATOM 5336 C CG . GLU A 1 710 ? 20.880 63.825 39.615 1.00 24.12 ? 703 GLU A CG 1 ATOM 5337 C CD . GLU A 1 710 ? 22.398 63.812 39.644 1.00 26.73 ? 703 GLU A CD 1 ATOM 5338 O OE1 . GLU A 1 710 ? 22.980 63.061 38.840 1.00 25.71 ? 703 GLU A OE1 1 ATOM 5339 O OE2 . GLU A 1 710 ? 23.015 64.543 40.477 1.00 26.65 ? 703 GLU A OE2 1 ATOM 5340 N N . SER A 1 711 ? 21.116 64.473 42.962 1.00 21.07 ? 704 SER A N 1 ATOM 5341 C CA . SER A 1 711 ? 20.642 65.625 43.716 1.00 20.16 ? 704 SER A CA 1 ATOM 5342 C C . SER A 1 711 ? 20.116 66.757 42.817 1.00 19.81 ? 704 SER A C 1 ATOM 5343 O O . SER A 1 711 ? 20.589 66.915 41.703 1.00 20.89 ? 704 SER A O 1 ATOM 5344 C CB . SER A 1 711 ? 21.729 66.108 44.709 1.00 20.82 ? 704 SER A CB 1 ATOM 5345 O OG . SER A 1 711 ? 22.965 66.383 44.023 1.00 23.06 ? 704 SER A OG 1 ATOM 5346 N N . PHE A 1 712 ? 19.173 67.565 43.331 1.00 18.08 ? 705 PHE A N 1 ATOM 5347 C CA . PHE A 1 712 ? 18.393 68.558 42.491 1.00 17.55 ? 705 PHE A CA 1 ATOM 5348 C C . PHE A 1 712 ? 18.105 68.010 41.092 1.00 18.99 ? 705 PHE A C 1 ATOM 5349 O O . PHE A 1 712 ? 18.521 68.622 40.063 1.00 18.87 ? 705 PHE A O 1 ATOM 5350 C CB . PHE A 1 712 ? 19.107 69.917 42.421 1.00 17.94 ? 705 PHE A CB 1 ATOM 5351 C CG . PHE A 1 712 ? 19.079 70.653 43.759 1.00 18.68 ? 705 PHE A CG 1 ATOM 5352 C CD1 . PHE A 1 712 ? 17.830 70.939 44.367 1.00 18.02 ? 705 PHE A CD1 1 ATOM 5353 C CD2 . PHE A 1 712 ? 20.248 71.028 44.400 1.00 19.63 ? 705 PHE A CD2 1 ATOM 5354 C CE1 . PHE A 1 712 ? 17.759 71.612 45.568 1.00 19.17 ? 705 PHE A CE1 1 ATOM 5355 C CE2 . PHE A 1 712 ? 20.179 71.747 45.622 1.00 20.27 ? 705 PHE A CE2 1 ATOM 5356 C CZ . PHE A 1 712 ? 18.918 72.018 46.196 1.00 20.55 ? 705 PHE A CZ 1 ATOM 5357 N N . PRO A 1 713 ? 17.455 66.829 41.044 1.00 18.48 ? 706 PRO A N 1 ATOM 5358 C CA . PRO A 1 713 ? 17.267 66.106 39.764 1.00 18.12 ? 706 PRO A CA 1 ATOM 5359 C C . PRO A 1 713 ? 16.551 66.943 38.706 1.00 17.96 ? 706 PRO A C 1 ATOM 5360 O O . PRO A 1 713 ? 16.881 66.803 37.520 1.00 17.93 ? 706 PRO A O 1 ATOM 5361 C CB . PRO A 1 713 ? 16.400 64.882 40.157 1.00 15.44 ? 706 PRO A CB 1 ATOM 5362 C CG . PRO A 1 713 ? 15.693 65.348 41.481 1.00 16.75 ? 706 PRO A CG 1 ATOM 5363 C CD . PRO A 1 713 ? 16.798 66.137 42.174 1.00 18.60 ? 706 PRO A CD 1 ATOM 5364 N N . GLY A 1 714 ? 15.584 67.778 39.105 1.00 17.10 ? 707 GLY A N 1 ATOM 5365 C CA . GLY A 1 714 ? 14.857 68.594 38.096 1.00 17.97 ? 707 GLY A CA 1 ATOM 5366 C C . GLY A 1 714 ? 15.837 69.538 37.380 1.00 19.95 ? 707 GLY A C 1 ATOM 5367 O O . GLY A 1 714 ? 15.795 69.660 36.148 1.00 18.34 ? 707 GLY A O 1 ATOM 5368 N N . ILE A 1 715 ? 16.734 70.209 38.135 1.00 18.50 ? 708 ILE A N 1 ATOM 5369 C CA . ILE A 1 715 ? 17.701 71.102 37.465 1.00 19.65 ? 708 ILE A CA 1 ATOM 5370 C C . ILE A 1 715 ? 18.747 70.280 36.733 1.00 20.10 ? 708 ILE A C 1 ATOM 5371 O O . ILE A 1 715 ? 19.172 70.628 35.613 1.00 20.66 ? 708 ILE A O 1 ATOM 5372 C CB . ILE A 1 715 ? 18.462 71.989 38.518 1.00 19.05 ? 708 ILE A CB 1 ATOM 5373 C CG1 . ILE A 1 715 ? 17.443 72.730 39.426 1.00 20.34 ? 708 ILE A CG1 1 ATOM 5374 C CG2 . ILE A 1 715 ? 19.353 73.071 37.784 1.00 19.01 ? 708 ILE A CG2 1 ATOM 5375 C CD1 . ILE A 1 715 ? 18.113 73.546 40.600 1.00 23.00 ? 708 ILE A CD1 1 ATOM 5376 N N . TYR A 1 716 ? 19.171 69.184 37.345 1.00 19.91 ? 709 TYR A N 1 ATOM 5377 C CA . TYR A 1 716 ? 20.215 68.364 36.712 1.00 20.76 ? 709 TYR A CA 1 ATOM 5378 C C . TYR A 1 716 ? 19.772 67.884 35.305 1.00 20.84 ? 709 TYR A C 1 ATOM 5379 O O . TYR A 1 716 ? 20.521 68.039 34.325 1.00 21.23 ? 709 TYR A O 1 ATOM 5380 C CB . TYR A 1 716 ? 20.598 67.171 37.616 1.00 19.35 ? 709 TYR A CB 1 ATOM 5381 C CG . TYR A 1 716 ? 21.674 66.313 36.938 1.00 17.63 ? 709 TYR A CG 1 ATOM 5382 C CD1 . TYR A 1 716 ? 23.025 66.478 37.262 1.00 21.55 ? 709 TYR A CD1 1 ATOM 5383 C CD2 . TYR A 1 716 ? 21.335 65.414 35.905 1.00 21.36 ? 709 TYR A CD2 1 ATOM 5384 C CE1 . TYR A 1 716 ? 24.041 65.736 36.585 1.00 22.39 ? 709 TYR A CE1 1 ATOM 5385 C CE2 . TYR A 1 716 ? 22.338 64.665 35.229 1.00 21.55 ? 709 TYR A CE2 1 ATOM 5386 C CZ . TYR A 1 716 ? 23.678 64.830 35.601 1.00 25.01 ? 709 TYR A CZ 1 ATOM 5387 O OH . TYR A 1 716 ? 24.671 64.118 34.935 1.00 23.68 ? 709 TYR A OH 1 ATOM 5388 N N . ASP A 1 717 ? 18.563 67.309 35.201 1.00 21.16 ? 710 ASP A N 1 ATOM 5389 C CA . ASP A 1 717 ? 18.036 66.853 33.893 1.00 20.77 ? 710 ASP A CA 1 ATOM 5390 C C . ASP A 1 717 ? 17.795 67.995 32.925 1.00 21.73 ? 710 ASP A C 1 ATOM 5391 O O . ASP A 1 717 ? 18.048 67.844 31.730 1.00 23.00 ? 710 ASP A O 1 ATOM 5392 C CB . ASP A 1 717 ? 16.757 65.989 34.067 1.00 20.64 ? 710 ASP A CB 1 ATOM 5393 C CG . ASP A 1 717 ? 17.080 64.612 34.654 1.00 22.10 ? 710 ASP A CG 1 ATOM 5394 O OD1 . ASP A 1 717 ? 18.280 64.202 34.616 1.00 22.08 ? 710 ASP A OD1 1 ATOM 5395 O OD2 . ASP A 1 717 ? 16.158 63.945 35.127 1.00 24.01 ? 710 ASP A OD2 1 ATOM 5396 N N . ALA A 1 718 ? 17.387 69.155 33.430 1.00 21.32 ? 711 ALA A N 1 ATOM 5397 C CA . ALA A 1 718 ? 17.259 70.318 32.556 1.00 21.69 ? 711 ALA A CA 1 ATOM 5398 C C . ALA A 1 718 ? 18.610 70.737 31.956 1.00 22.77 ? 711 ALA A C 1 ATOM 5399 O O . ALA A 1 718 ? 18.669 71.183 30.793 1.00 22.45 ? 711 ALA A O 1 ATOM 5400 C CB . ALA A 1 718 ? 16.583 71.516 33.286 1.00 22.18 ? 711 ALA A CB 1 ATOM 5401 N N . LEU A 1 719 ? 19.678 70.613 32.734 1.00 20.95 ? 712 LEU A N 1 ATOM 5402 C CA . LEU A 1 719 ? 21.025 70.972 32.219 1.00 22.52 ? 712 LEU A CA 1 ATOM 5403 C C . LEU A 1 719 ? 21.724 69.890 31.419 1.00 23.82 ? 712 LEU A C 1 ATOM 5404 O O . LEU A 1 719 ? 22.718 70.166 30.732 1.00 24.38 ? 712 LEU A O 1 ATOM 5405 C CB . LEU A 1 719 ? 21.956 71.335 33.395 1.00 23.40 ? 712 LEU A CB 1 ATOM 5406 C CG . LEU A 1 719 ? 21.719 72.728 34.046 1.00 23.36 ? 712 LEU A CG 1 ATOM 5407 C CD1 . LEU A 1 719 ? 22.442 72.824 35.379 1.00 23.95 ? 712 LEU A CD1 1 ATOM 5408 C CD2 . LEU A 1 719 ? 22.238 73.812 33.088 1.00 26.14 ? 712 LEU A CD2 1 ATOM 5409 N N . PHE A 1 720 ? 21.254 68.665 31.562 1.00 24.27 ? 713 PHE A N 1 ATOM 5410 C CA . PHE A 1 720 ? 21.972 67.531 30.960 1.00 25.89 ? 713 PHE A CA 1 ATOM 5411 C C . PHE A 1 720 ? 21.969 67.616 29.440 1.00 26.76 ? 713 PHE A C 1 ATOM 5412 O O . PHE A 1 720 ? 20.912 67.686 28.803 1.00 26.14 ? 713 PHE A O 1 ATOM 5413 C CB . PHE A 1 720 ? 21.443 66.137 31.444 1.00 25.05 ? 713 PHE A CB 1 ATOM 5414 C CG . PHE A 1 720 ? 22.282 64.988 30.909 1.00 26.27 ? 713 PHE A CG 1 ATOM 5415 C CD1 . PHE A 1 720 ? 23.472 64.625 31.568 1.00 25.51 ? 713 PHE A CD1 1 ATOM 5416 C CD2 . PHE A 1 720 ? 21.938 64.349 29.719 1.00 27.53 ? 713 PHE A CD2 1 ATOM 5417 C CE1 . PHE A 1 720 ? 24.299 63.608 31.048 1.00 29.74 ? 713 PHE A CE1 1 ATOM 5418 C CE2 . PHE A 1 720 ? 22.740 63.320 29.188 1.00 26.93 ? 713 PHE A CE2 1 ATOM 5419 C CZ . PHE A 1 720 ? 23.934 62.949 29.861 1.00 30.28 ? 713 PHE A CZ 1 ATOM 5420 N N . ASP A 1 721 ? 23.166 67.625 28.864 1.00 27.48 ? 714 ASP A N 1 ATOM 5421 C CA . ASP A 1 721 ? 23.346 67.612 27.403 1.00 30.47 ? 714 ASP A CA 1 ATOM 5422 C C . ASP A 1 721 ? 22.689 68.854 26.789 1.00 30.58 ? 714 ASP A C 1 ATOM 5423 O O . ASP A 1 721 ? 22.208 68.808 25.654 1.00 31.09 ? 714 ASP A O 1 ATOM 5424 C CB . ASP A 1 721 ? 22.741 66.319 26.805 1.00 29.80 ? 714 ASP A CB 1 ATOM 5425 C CG . ASP A 1 721 ? 23.153 66.107 25.317 1.00 33.20 ? 714 ASP A CG 1 ATOM 5426 O OD1 . ASP A 1 721 ? 24.298 66.401 24.959 1.00 32.18 ? 714 ASP A OD1 1 ATOM 5427 O OD2 . ASP A 1 721 ? 22.316 65.649 24.516 1.00 35.66 ? 714 ASP A OD2 1 ATOM 5428 N N . ILE A 1 722 ? 22.668 69.967 27.538 1.00 30.47 ? 715 ILE A N 1 ATOM 5429 C CA . ILE A 1 722 ? 21.897 71.148 27.104 1.00 30.64 ? 715 ILE A CA 1 ATOM 5430 C C . ILE A 1 722 ? 22.425 71.774 25.804 1.00 33.56 ? 715 ILE A C 1 ATOM 5431 O O . ILE A 1 722 ? 21.633 72.334 25.002 1.00 34.03 ? 715 ILE A O 1 ATOM 5432 C CB . ILE A 1 722 ? 21.745 72.220 28.236 1.00 29.40 ? 715 ILE A CB 1 ATOM 5433 C CG1 . ILE A 1 722 ? 20.647 73.217 27.875 1.00 29.04 ? 715 ILE A CG1 1 ATOM 5434 C CG2 . ILE A 1 722 ? 23.063 72.870 28.610 1.00 30.80 ? 715 ILE A CG2 1 ATOM 5435 C CD1 . ILE A 1 722 ? 20.136 73.986 29.057 1.00 26.99 ? 715 ILE A CD1 1 ATOM 5436 N N . GLU A 1 723 ? 23.736 71.659 25.589 1.00 35.00 ? 716 GLU A N 1 ATOM 5437 C CA . GLU A 1 723 ? 24.370 72.224 24.400 1.00 39.46 ? 716 GLU A CA 1 ATOM 5438 C C . GLU A 1 723 ? 23.877 71.551 23.125 1.00 40.64 ? 716 GLU A C 1 ATOM 5439 O O . GLU A 1 723 ? 24.126 72.056 22.026 1.00 42.27 ? 716 GLU A O 1 ATOM 5440 C CB . GLU A 1 723 ? 25.910 72.210 24.486 1.00 39.83 ? 716 GLU A CB 1 ATOM 5441 C CG . GLU A 1 723 ? 26.581 70.815 24.471 1.00 42.89 ? 716 GLU A CG 1 ATOM 5442 C CD . GLU A 1 723 ? 26.550 70.048 25.831 1.00 45.26 ? 716 GLU A CD 1 ATOM 5443 O OE1 . GLU A 1 723 ? 25.752 70.366 26.767 1.00 39.34 ? 716 GLU A OE1 1 ATOM 5444 O OE2 . GLU A 1 723 ? 27.337 69.077 25.931 1.00 47.72 ? 716 GLU A OE2 1 ATOM 5445 N N . SER A 1 724 ? 23.149 70.446 23.268 1.00 40.02 ? 717 SER A N 1 ATOM 5446 C CA . SER A 1 724 ? 22.617 69.716 22.114 1.00 41.50 ? 717 SER A CA 1 ATOM 5447 C C . SER A 1 724 ? 21.187 70.079 21.787 1.00 41.98 ? 717 SER A C 1 ATOM 5448 O O . SER A 1 724 ? 20.700 69.685 20.736 1.00 43.31 ? 717 SER A O 1 ATOM 5449 C CB . SER A 1 724 ? 22.736 68.192 22.294 1.00 41.22 ? 717 SER A CB 1 ATOM 5450 O OG . SER A 1 724 ? 24.111 67.840 22.462 1.00 41.19 ? 717 SER A OG 1 ATOM 5451 N N . LYS A 1 725 ? 20.515 70.850 22.643 1.00 40.96 ? 718 LYS A N 1 ATOM 5452 C CA . LYS A 1 725 ? 19.098 71.172 22.401 1.00 40.98 ? 718 LYS A CA 1 ATOM 5453 C C . LYS A 1 725 ? 18.952 72.184 21.273 1.00 42.02 ? 718 LYS A C 1 ATOM 5454 O O . LYS A 1 725 ? 19.747 73.130 21.168 1.00 42.65 ? 718 LYS A O 1 ATOM 5455 C CB . LYS A 1 725 ? 18.401 71.700 23.665 1.00 39.46 ? 718 LYS A CB 1 ATOM 5456 C CG . LYS A 1 725 ? 18.324 70.706 24.827 1.00 40.70 ? 718 LYS A CG 1 ATOM 5457 C CD . LYS A 1 725 ? 17.630 69.384 24.442 1.00 44.67 ? 718 LYS A CD 1 ATOM 5458 C CE . LYS A 1 725 ? 17.785 68.307 25.559 1.00 43.19 ? 718 LYS A CE 1 ATOM 5459 N NZ . LYS A 1 725 ? 17.226 68.754 26.892 1.00 42.69 ? 718 LYS A NZ 1 ATOM 5460 N N . VAL A 1 726 ? 17.920 72.010 20.449 1.00 42.74 ? 719 VAL A N 1 ATOM 5461 C CA . VAL A 1 726 ? 17.802 72.820 19.212 1.00 44.23 ? 719 VAL A CA 1 ATOM 5462 C C . VAL A 1 726 ? 17.350 74.256 19.502 1.00 43.29 ? 719 VAL A C 1 ATOM 5463 O O . VAL A 1 726 ? 17.689 75.178 18.775 1.00 43.67 ? 719 VAL A O 1 ATOM 5464 C CB . VAL A 1 726 ? 16.870 72.150 18.146 1.00 45.11 ? 719 VAL A CB 1 ATOM 5465 C CG1 . VAL A 1 726 ? 16.956 72.886 16.828 1.00 48.71 ? 719 VAL A CG1 1 ATOM 5466 C CG2 . VAL A 1 726 ? 17.291 70.703 17.888 1.00 47.38 ? 719 VAL A CG2 1 ATOM 5467 N N . ASP A 1 727 ? 16.625 74.434 20.597 1.00 41.36 ? 720 ASP A N 1 ATOM 5468 C CA . ASP A 1 727 ? 16.080 75.737 20.977 1.00 40.56 ? 720 ASP A CA 1 ATOM 5469 C C . ASP A 1 727 ? 16.660 76.107 22.345 1.00 38.34 ? 720 ASP A C 1 ATOM 5470 O O . ASP A 1 727 ? 16.045 75.784 23.361 1.00 36.64 ? 720 ASP A O 1 ATOM 5471 C CB . ASP A 1 727 ? 14.561 75.599 21.111 1.00 40.10 ? 720 ASP A CB 1 ATOM 5472 C CG . ASP A 1 727 ? 13.867 76.924 21.352 1.00 42.34 ? 720 ASP A CG 1 ATOM 5473 O OD1 . ASP A 1 727 ? 14.548 77.923 21.661 1.00 43.92 ? 720 ASP A OD1 1 ATOM 5474 O OD2 . ASP A 1 727 ? 12.627 76.954 21.251 1.00 46.34 ? 720 ASP A OD2 1 ATOM 5475 N N . PRO A 1 728 ? 17.832 76.761 22.371 1.00 37.69 ? 721 PRO A N 1 ATOM 5476 C CA . PRO A 1 728 ? 18.503 77.067 23.633 1.00 36.96 ? 721 PRO A CA 1 ATOM 5477 C C . PRO A 1 728 ? 17.679 77.988 24.538 1.00 36.37 ? 721 PRO A C 1 ATOM 5478 O O . PRO A 1 728 ? 17.797 77.908 25.766 1.00 35.01 ? 721 PRO A O 1 ATOM 5479 C CB . PRO A 1 728 ? 19.811 77.750 23.204 1.00 38.33 ? 721 PRO A CB 1 ATOM 5480 C CG . PRO A 1 728 ? 19.698 78.042 21.747 1.00 40.00 ? 721 PRO A CG 1 ATOM 5481 C CD . PRO A 1 728 ? 18.645 77.120 21.194 1.00 39.68 ? 721 PRO A CD 1 ATOM 5482 N N . SER A 1 729 ? 16.859 78.857 23.944 1.00 35.85 ? 722 SER A N 1 ATOM 5483 C CA . SER A 1 729 ? 16.045 79.759 24.743 1.00 35.96 ? 722 SER A CA 1 ATOM 5484 C C . SER A 1 729 ? 15.060 78.981 25.589 1.00 33.53 ? 722 SER A C 1 ATOM 5485 O O . SER A 1 729 ? 14.885 79.255 26.793 1.00 31.93 ? 722 SER A O 1 ATOM 5486 C CB . SER A 1 729 ? 15.282 80.731 23.846 1.00 36.43 ? 722 SER A CB 1 ATOM 5487 O OG . SER A 1 729 ? 14.506 81.535 24.690 1.00 41.68 ? 722 SER A OG 1 ATOM 5488 N N . LYS A 1 730 ? 14.409 78.006 24.954 1.00 32.53 ? 723 LYS A N 1 ATOM 5489 C CA . LYS A 1 730 ? 13.467 77.149 25.643 1.00 32.40 ? 723 LYS A CA 1 ATOM 5490 C C . LYS A 1 730 ? 14.183 76.262 26.698 1.00 30.55 ? 723 LYS A C 1 ATOM 5491 O O . LYS A 1 730 ? 13.707 76.120 27.834 1.00 28.19 ? 723 LYS A O 1 ATOM 5492 C CB . LYS A 1 730 ? 12.721 76.303 24.596 1.00 32.99 ? 723 LYS A CB 1 ATOM 5493 C CG . LYS A 1 730 ? 11.607 75.443 25.180 1.00 39.24 ? 723 LYS A CG 1 ATOM 5494 C CD . LYS A 1 730 ? 10.831 74.691 24.068 1.00 46.42 ? 723 LYS A CD 1 ATOM 5495 C CE . LYS A 1 730 ? 9.939 73.584 24.670 1.00 48.22 ? 723 LYS A CE 1 ATOM 5496 N NZ . LYS A 1 730 ? 9.631 72.573 23.602 1.00 53.11 ? 723 LYS A NZ 1 ATOM 5497 N N . ALA A 1 731 ? 15.319 75.669 26.313 1.00 28.97 ? 724 ALA A N 1 ATOM 5498 C CA . ALA A 1 731 ? 16.077 74.801 27.218 1.00 27.85 ? 724 ALA A CA 1 ATOM 5499 C C . ALA A 1 731 ? 16.539 75.547 28.490 1.00 25.83 ? 724 ALA A C 1 ATOM 5500 O O . ALA A 1 731 ? 16.372 75.042 29.602 1.00 25.96 ? 724 ALA A O 1 ATOM 5501 C CB . ALA A 1 731 ? 17.313 74.215 26.486 1.00 27.43 ? 724 ALA A CB 1 ATOM 5502 N N . TRP A 1 732 ? 17.111 76.740 28.321 1.00 26.54 ? 725 TRP A N 1 ATOM 5503 C CA . TRP A 1 732 ? 17.533 77.533 29.475 1.00 26.03 ? 725 TRP A CA 1 ATOM 5504 C C . TRP A 1 732 ? 16.363 78.089 30.296 1.00 26.35 ? 725 TRP A C 1 ATOM 5505 O O . TRP A 1 732 ? 16.468 78.212 31.544 1.00 25.10 ? 725 TRP A O 1 ATOM 5506 C CB . TRP A 1 732 ? 18.550 78.600 29.042 1.00 26.76 ? 725 TRP A CB 1 ATOM 5507 C CG . TRP A 1 732 ? 19.894 77.951 28.767 1.00 27.09 ? 725 TRP A CG 1 ATOM 5508 C CD1 . TRP A 1 732 ? 20.442 77.616 27.529 1.00 30.04 ? 725 TRP A CD1 1 ATOM 5509 C CD2 . TRP A 1 732 ? 20.856 77.547 29.751 1.00 26.70 ? 725 TRP A CD2 1 ATOM 5510 N NE1 . TRP A 1 732 ? 21.682 77.007 27.708 1.00 29.21 ? 725 TRP A NE1 1 ATOM 5511 C CE2 . TRP A 1 732 ? 21.961 76.971 29.055 1.00 27.71 ? 725 TRP A CE2 1 ATOM 5512 C CE3 . TRP A 1 732 ? 20.883 77.591 31.169 1.00 26.14 ? 725 TRP A CE3 1 ATOM 5513 C CZ2 . TRP A 1 732 ? 23.087 76.479 29.719 1.00 28.03 ? 725 TRP A CZ2 1 ATOM 5514 C CZ3 . TRP A 1 732 ? 22.017 77.111 31.831 1.00 28.13 ? 725 TRP A CZ3 1 ATOM 5515 C CH2 . TRP A 1 732 ? 23.104 76.563 31.105 1.00 26.97 ? 725 TRP A CH2 1 ATOM 5516 N N . GLY A 1 733 ? 15.257 78.402 29.621 1.00 25.93 ? 726 GLY A N 1 ATOM 5517 C CA . GLY A 1 733 ? 13.994 78.729 30.331 1.00 25.06 ? 726 GLY A CA 1 ATOM 5518 C C . GLY A 1 733 ? 13.590 77.636 31.290 1.00 24.78 ? 726 GLY A C 1 ATOM 5519 O O . GLY A 1 733 ? 13.089 77.910 32.403 1.00 24.18 ? 726 GLY A O 1 ATOM 5520 N N . GLU A 1 734 ? 13.755 76.385 30.858 1.00 24.55 ? 727 GLU A N 1 ATOM 5521 C CA . GLU A 1 734 ? 13.310 75.265 31.678 1.00 23.37 ? 727 GLU A CA 1 ATOM 5522 C C . GLU A 1 734 ? 14.329 75.059 32.827 1.00 23.55 ? 727 GLU A C 1 ATOM 5523 O O . GLU A 1 734 ? 13.963 74.715 33.913 1.00 22.22 ? 727 GLU A O 1 ATOM 5524 C CB . GLU A 1 734 ? 13.105 74.003 30.820 1.00 23.68 ? 727 GLU A CB 1 ATOM 5525 C CG A GLU A 1 734 ? 12.795 72.742 31.671 1.00 25.37 ? 727 GLU A CG 1 ATOM 5526 C CD A GLU A 1 734 ? 11.435 72.785 32.383 1.00 27.26 ? 727 GLU A CD 1 ATOM 5527 O OE1 A GLU A 1 734 ? 10.609 73.695 32.098 1.00 26.21 ? 727 GLU A OE1 1 ATOM 5528 O OE2 A GLU A 1 734 ? 11.217 71.903 33.235 1.00 27.84 ? 727 GLU A OE2 1 ATOM 5529 N N . VAL A 1 735 ? 15.617 75.318 32.580 1.00 23.45 ? 728 VAL A N 1 ATOM 5530 C CA . VAL A 1 735 ? 16.593 75.344 33.702 1.00 23.31 ? 728 VAL A CA 1 ATOM 5531 C C . VAL A 1 735 ? 16.139 76.363 34.767 1.00 22.98 ? 728 VAL A C 1 ATOM 5532 O O . VAL A 1 735 ? 16.078 76.049 35.948 1.00 19.97 ? 728 VAL A O 1 ATOM 5533 C CB . VAL A 1 735 ? 18.034 75.653 33.196 1.00 24.31 ? 728 VAL A CB 1 ATOM 5534 C CG1 . VAL A 1 735 ? 19.021 75.973 34.381 1.00 24.56 ? 728 VAL A CG1 1 ATOM 5535 C CG2 . VAL A 1 735 ? 18.566 74.488 32.250 1.00 23.48 ? 728 VAL A CG2 1 ATOM 5536 N N . LYS A 1 736 ? 15.840 77.581 34.333 1.00 23.03 ? 729 LYS A N 1 ATOM 5537 C CA . LYS A 1 736 ? 15.364 78.623 35.259 1.00 23.32 ? 729 LYS A CA 1 ATOM 5538 C C . LYS A 1 736 ? 14.084 78.200 36.002 1.00 23.10 ? 729 LYS A C 1 ATOM 5539 O O . LYS A 1 736 ? 13.956 78.459 37.211 1.00 22.25 ? 729 LYS A O 1 ATOM 5540 C CB . LYS A 1 736 ? 15.131 79.931 34.527 1.00 24.08 ? 729 LYS A CB 1 ATOM 5541 C CG . LYS A 1 736 ? 16.450 80.591 34.036 1.00 23.43 ? 729 LYS A CG 1 ATOM 5542 C CD . LYS A 1 736 ? 16.132 81.846 33.174 1.00 27.24 ? 729 LYS A CD 1 ATOM 5543 C CE . LYS A 1 736 ? 15.658 83.009 34.039 1.00 30.35 ? 729 LYS A CE 1 ATOM 5544 N NZ . LYS A 1 736 ? 15.711 84.320 33.269 1.00 37.37 ? 729 LYS A NZ 1 ATOM 5545 N N . ARG A 1 737 ? 13.136 77.563 35.286 1.00 21.43 ? 730 ARG A N 1 ATOM 5546 C CA . ARG A 1 737 ? 11.946 77.061 35.970 1.00 20.53 ? 730 ARG A CA 1 ATOM 5547 C C . ARG A 1 737 ? 12.298 76.097 37.089 1.00 19.25 ? 730 ARG A C 1 ATOM 5548 O O . ARG A 1 737 ? 11.762 76.185 38.197 1.00 17.90 ? 730 ARG A O 1 ATOM 5549 C CB . ARG A 1 737 ? 10.972 76.391 34.961 1.00 20.41 ? 730 ARG A CB 1 ATOM 5550 C CG . ARG A 1 737 ? 9.624 76.125 35.635 1.00 22.48 ? 730 ARG A CG 1 ATOM 5551 C CD . ARG A 1 737 ? 8.580 75.598 34.609 1.00 25.49 ? 730 ARG A CD 1 ATOM 5552 N NE . ARG A 1 737 ? 8.762 74.170 34.386 1.00 27.38 ? 730 ARG A NE 1 ATOM 5553 C CZ . ARG A 1 737 ? 8.289 73.203 35.186 1.00 28.40 ? 730 ARG A CZ 1 ATOM 5554 N NH1 . ARG A 1 737 ? 7.612 73.482 36.314 1.00 29.42 ? 730 ARG A NH1 1 ATOM 5555 N NH2 . ARG A 1 737 ? 8.510 71.937 34.863 1.00 29.17 ? 730 ARG A NH2 1 ATOM 5556 N N . GLN A 1 738 ? 13.225 75.171 36.812 1.00 19.24 ? 731 GLN A N 1 ATOM 5557 C CA . GLN A 1 738 ? 13.610 74.175 37.800 1.00 19.69 ? 731 GLN A CA 1 ATOM 5558 C C . GLN A 1 738 ? 14.381 74.818 38.976 1.00 20.01 ? 731 GLN A C 1 ATOM 5559 O O . GLN A 1 738 ? 14.270 74.324 40.119 1.00 18.91 ? 731 GLN A O 1 ATOM 5560 C CB . GLN A 1 738 ? 14.485 73.081 37.108 1.00 18.87 ? 731 GLN A CB 1 ATOM 5561 C CG . GLN A 1 738 ? 13.626 72.222 36.083 1.00 18.45 ? 731 GLN A CG 1 ATOM 5562 C CD . GLN A 1 738 ? 12.468 71.465 36.757 1.00 23.13 ? 731 GLN A CD 1 ATOM 5563 O OE1 . GLN A 1 738 ? 12.554 71.049 37.928 1.00 21.72 ? 731 GLN A OE1 1 ATOM 5564 N NE2 . GLN A 1 738 ? 11.359 71.312 36.029 1.00 23.89 ? 731 GLN A NE2 1 ATOM 5565 N N . ILE A 1 739 ? 15.166 75.870 38.703 1.00 20.89 ? 732 ILE A N 1 ATOM 5566 C CA . ILE A 1 739 ? 15.798 76.591 39.808 1.00 20.84 ? 732 ILE A CA 1 ATOM 5567 C C . ILE A 1 739 ? 14.722 77.173 40.745 1.00 21.34 ? 732 ILE A C 1 ATOM 5568 O O . ILE A 1 739 ? 14.871 77.069 41.967 1.00 21.18 ? 732 ILE A O 1 ATOM 5569 C CB . ILE A 1 739 ? 16.776 77.706 39.315 1.00 20.66 ? 732 ILE A CB 1 ATOM 5570 C CG1 . ILE A 1 739 ? 17.997 77.076 38.605 1.00 19.62 ? 732 ILE A CG1 1 ATOM 5571 C CG2 . ILE A 1 739 ? 17.243 78.647 40.501 1.00 19.23 ? 732 ILE A CG2 1 ATOM 5572 C CD1 . ILE A 1 739 ? 18.780 78.137 37.742 1.00 21.28 ? 732 ILE A CD1 1 ATOM 5573 N N . TYR A 1 740 ? 13.678 77.777 40.170 1.00 21.41 ? 733 TYR A N 1 ATOM 5574 C CA . TYR A 1 740 ? 12.564 78.377 40.932 1.00 22.48 ? 733 TYR A CA 1 ATOM 5575 C C . TYR A 1 740 ? 11.835 77.290 41.754 1.00 21.53 ? 733 TYR A C 1 ATOM 5576 O O . TYR A 1 740 ? 11.515 77.490 42.941 1.00 20.57 ? 733 TYR A O 1 ATOM 5577 C CB . TYR A 1 740 ? 11.604 78.993 39.949 1.00 22.11 ? 733 TYR A CB 1 ATOM 5578 C CG . TYR A 1 740 ? 10.123 79.286 40.336 1.00 26.57 ? 733 TYR A CG 1 ATOM 5579 C CD1 . TYR A 1 740 ? 9.792 80.043 41.476 1.00 28.09 ? 733 TYR A CD1 1 ATOM 5580 C CD2 . TYR A 1 740 ? 9.059 78.814 39.499 1.00 24.06 ? 733 TYR A CD2 1 ATOM 5581 C CE1 . TYR A 1 740 ? 8.442 80.353 41.771 1.00 27.42 ? 733 TYR A CE1 1 ATOM 5582 C CE2 . TYR A 1 740 ? 7.728 79.122 39.752 1.00 23.23 ? 733 TYR A CE2 1 ATOM 5583 C CZ . TYR A 1 740 ? 7.424 79.910 40.893 1.00 27.39 ? 733 TYR A CZ 1 ATOM 5584 O OH . TYR A 1 740 ? 6.100 80.250 41.147 1.00 32.08 ? 733 TYR A OH 1 ATOM 5585 N N . VAL A 1 741 ? 11.562 76.171 41.130 1.00 20.19 ? 734 VAL A N 1 ATOM 5586 C CA . VAL A 1 741 ? 10.887 75.072 41.881 1.00 19.74 ? 734 VAL A CA 1 ATOM 5587 C C . VAL A 1 741 ? 11.739 74.589 43.052 1.00 20.51 ? 734 VAL A C 1 ATOM 5588 O O . VAL A 1 741 ? 11.253 74.415 44.182 1.00 20.74 ? 734 VAL A O 1 ATOM 5589 C CB . VAL A 1 741 ? 10.474 73.888 40.935 1.00 19.44 ? 734 VAL A CB 1 ATOM 5590 C CG1 . VAL A 1 741 ? 9.979 72.659 41.754 1.00 20.08 ? 734 VAL A CG1 1 ATOM 5591 C CG2 . VAL A 1 741 ? 9.352 74.338 39.925 1.00 19.45 ? 734 VAL A CG2 1 ATOM 5592 N N . ALA A 1 742 ? 13.037 74.430 42.796 1.00 19.54 ? 735 ALA A N 1 ATOM 5593 C CA . ALA A 1 742 ? 13.965 73.962 43.832 1.00 19.69 ? 735 ALA A CA 1 ATOM 5594 C C . ALA A 1 742 ? 14.110 74.991 44.980 1.00 19.23 ? 735 ALA A C 1 ATOM 5595 O O . ALA A 1 742 ? 14.039 74.603 46.149 1.00 18.47 ? 735 ALA A O 1 ATOM 5596 C CB . ALA A 1 742 ? 15.340 73.609 43.217 1.00 19.81 ? 735 ALA A CB 1 ATOM 5597 N N . ALA A 1 743 ? 14.287 76.271 44.648 1.00 19.04 ? 736 ALA A N 1 ATOM 5598 C CA . ALA A 1 743 ? 14.430 77.340 45.673 1.00 19.17 ? 736 ALA A CA 1 ATOM 5599 C C . ALA A 1 743 ? 13.132 77.419 46.493 1.00 19.96 ? 736 ALA A C 1 ATOM 5600 O O . ALA A 1 743 ? 13.159 77.480 47.720 1.00 19.29 ? 736 ALA A O 1 ATOM 5601 C CB . ALA A 1 743 ? 14.680 78.705 44.989 1.00 18.67 ? 736 ALA A CB 1 ATOM 5602 N N . PHE A 1 744 ? 12.008 77.445 45.804 1.00 18.52 ? 737 PHE A N 1 ATOM 5603 C CA . PHE A 1 744 ? 10.719 77.471 46.505 1.00 20.36 ? 737 PHE A CA 1 ATOM 5604 C C . PHE A 1 744 ? 10.572 76.282 47.480 1.00 18.58 ? 737 PHE A C 1 ATOM 5605 O O . PHE A 1 744 ? 10.180 76.464 48.645 1.00 19.70 ? 737 PHE A O 1 ATOM 5606 C CB . PHE A 1 744 ? 9.525 77.470 45.533 1.00 18.82 ? 737 PHE A CB 1 ATOM 5607 C CG . PHE A 1 744 ? 8.226 77.127 46.249 1.00 22.14 ? 737 PHE A CG 1 ATOM 5608 C CD1 . PHE A 1 744 ? 7.705 78.023 47.220 1.00 21.98 ? 737 PHE A CD1 1 ATOM 5609 C CD2 . PHE A 1 744 ? 7.600 75.890 46.032 1.00 20.78 ? 737 PHE A CD2 1 ATOM 5610 C CE1 . PHE A 1 744 ? 6.565 77.686 47.955 1.00 20.84 ? 737 PHE A CE1 1 ATOM 5611 C CE2 . PHE A 1 744 ? 6.415 75.539 46.772 1.00 20.73 ? 737 PHE A CE2 1 ATOM 5612 C CZ . PHE A 1 744 ? 5.895 76.452 47.711 1.00 20.29 ? 737 PHE A CZ 1 ATOM 5613 N N . THR A 1 745 ? 10.874 75.079 47.018 1.00 18.87 ? 738 THR A N 1 ATOM 5614 C CA . THR A 1 745 ? 10.627 73.884 47.877 1.00 18.72 ? 738 THR A CA 1 ATOM 5615 C C . THR A 1 745 ? 11.586 73.912 49.073 1.00 19.59 ? 738 THR A C 1 ATOM 5616 O O . THR A 1 745 ? 11.216 73.523 50.170 1.00 20.08 ? 738 THR A O 1 ATOM 5617 C CB . THR A 1 745 ? 10.856 72.588 47.063 1.00 20.04 ? 738 THR A CB 1 ATOM 5618 O OG1 . THR A 1 745 ? 10.042 72.638 45.888 1.00 18.17 ? 738 THR A OG1 1 ATOM 5619 C CG2 . THR A 1 745 ? 10.525 71.323 47.864 1.00 18.32 ? 738 THR A CG2 1 ATOM 5620 N N . VAL A 1 746 ? 12.827 74.352 48.841 1.00 19.61 ? 739 VAL A N 1 ATOM 5621 C CA . VAL A 1 746 ? 13.813 74.439 49.956 1.00 19.27 ? 739 VAL A CA 1 ATOM 5622 C C . VAL A 1 746 ? 13.337 75.436 51.003 1.00 19.93 ? 739 VAL A C 1 ATOM 5623 O O . VAL A 1 746 ? 13.348 75.138 52.227 1.00 18.12 ? 739 VAL A O 1 ATOM 5624 C CB . VAL A 1 746 ? 15.244 74.683 49.457 1.00 20.04 ? 739 VAL A CB 1 ATOM 5625 C CG1 . VAL A 1 746 ? 16.222 75.096 50.634 1.00 20.01 ? 739 VAL A CG1 1 ATOM 5626 C CG2 . VAL A 1 746 ? 15.752 73.446 48.675 1.00 19.21 ? 739 VAL A CG2 1 ATOM 5627 N N . GLN A 1 747 ? 12.901 76.599 50.530 1.00 20.78 ? 740 GLN A N 1 ATOM 5628 C CA . GLN A 1 747 ? 12.316 77.618 51.440 1.00 20.89 ? 740 GLN A CA 1 ATOM 5629 C C . GLN A 1 747 ? 11.074 77.105 52.157 1.00 19.56 ? 740 GLN A C 1 ATOM 5630 O O . GLN A 1 747 ? 10.920 77.351 53.376 1.00 20.92 ? 740 GLN A O 1 ATOM 5631 C CB . GLN A 1 747 ? 11.947 78.893 50.695 1.00 19.89 ? 740 GLN A CB 1 ATOM 5632 C CG . GLN A 1 747 ? 11.416 80.015 51.620 1.00 22.02 ? 740 GLN A CG 1 ATOM 5633 C CD . GLN A 1 747 ? 12.475 80.641 52.546 1.00 23.18 ? 740 GLN A CD 1 ATOM 5634 O OE1 . GLN A 1 747 ? 13.693 80.628 52.265 1.00 23.78 ? 740 GLN A OE1 1 ATOM 5635 N NE2 . GLN A 1 747 ? 12.004 81.219 53.662 1.00 23.85 ? 740 GLN A NE2 1 ATOM 5636 N N . ALA A 1 748 ? 10.169 76.460 51.415 1.00 18.30 ? 741 ALA A N 1 ATOM 5637 C CA . ALA A 1 748 ? 8.953 75.925 52.035 1.00 17.46 ? 741 ALA A CA 1 ATOM 5638 C C . ALA A 1 748 ? 9.279 74.874 53.077 1.00 17.56 ? 741 ALA A C 1 ATOM 5639 O O . ALA A 1 748 ? 8.636 74.835 54.136 1.00 18.40 ? 741 ALA A O 1 ATOM 5640 C CB . ALA A 1 748 ? 8.003 75.314 50.967 1.00 17.69 ? 741 ALA A CB 1 ATOM 5641 N N . ALA A 1 749 ? 10.234 74.006 52.773 1.00 16.85 ? 742 ALA A N 1 ATOM 5642 C CA . ALA A 1 749 ? 10.703 72.992 53.778 1.00 18.89 ? 742 ALA A CA 1 ATOM 5643 C C . ALA A 1 749 ? 11.263 73.698 55.005 1.00 19.21 ? 742 ALA A C 1 ATOM 5644 O O . ALA A 1 749 ? 10.974 73.298 56.139 1.00 19.79 ? 742 ALA A O 1 ATOM 5645 C CB . ALA A 1 749 ? 11.801 72.075 53.173 1.00 16.45 ? 742 ALA A CB 1 ATOM 5646 N N . ALA A 1 750 ? 12.106 74.711 54.786 1.00 19.99 ? 743 ALA A N 1 ATOM 5647 C CA . ALA A 1 750 ? 12.642 75.491 55.915 1.00 20.25 ? 743 ALA A CA 1 ATOM 5648 C C . ALA A 1 750 ? 11.521 76.041 56.781 1.00 20.75 ? 743 ALA A C 1 ATOM 5649 O O . ALA A 1 750 ? 11.600 75.992 58.015 1.00 19.80 ? 743 ALA A O 1 ATOM 5650 C CB . ALA A 1 750 ? 13.517 76.692 55.427 1.00 20.66 ? 743 ALA A CB 1 ATOM 5651 N N . GLU A 1 751 ? 10.486 76.581 56.144 1.00 19.79 ? 744 GLU A N 1 ATOM 5652 C CA . GLU A 1 751 ? 9.426 77.241 56.906 1.00 19.80 ? 744 GLU A CA 1 ATOM 5653 C C . GLU A 1 751 ? 8.586 76.259 57.760 1.00 19.22 ? 744 GLU A C 1 ATOM 5654 O O . GLU A 1 751 ? 7.939 76.687 58.707 1.00 20.87 ? 744 GLU A O 1 ATOM 5655 C CB . GLU A 1 751 ? 8.545 78.112 55.993 1.00 20.92 ? 744 GLU A CB 1 ATOM 5656 C CG . GLU A 1 751 ? 9.333 79.342 55.545 1.00 20.50 ? 744 GLU A CG 1 ATOM 5657 C CD . GLU A 1 751 ? 8.581 80.232 54.553 1.00 24.70 ? 744 GLU A CD 1 ATOM 5658 O OE1 . GLU A 1 751 ? 7.434 79.930 54.169 1.00 23.94 ? 744 GLU A OE1 1 ATOM 5659 O OE2 . GLU A 1 751 ? 9.172 81.265 54.174 1.00 23.78 ? 744 GLU A OE2 1 ATOM 5660 N N . THR A 1 752 ? 8.599 74.971 57.426 1.00 19.19 ? 745 THR A N 1 ATOM 5661 C CA . THR A 1 752 ? 7.980 73.959 58.319 1.00 19.78 ? 745 THR A CA 1 ATOM 5662 C C . THR A 1 752 ? 8.669 73.859 59.672 1.00 20.63 ? 745 THR A C 1 ATOM 5663 O O . THR A 1 752 ? 8.065 73.383 60.639 1.00 21.82 ? 745 THR A O 1 ATOM 5664 C CB . THR A 1 752 ? 7.847 72.548 57.720 1.00 19.84 ? 745 THR A CB 1 ATOM 5665 O OG1 . THR A 1 752 ? 9.141 71.910 57.710 1.00 20.04 ? 745 THR A OG1 1 ATOM 5666 C CG2 . THR A 1 752 ? 7.238 72.606 56.266 1.00 16.19 ? 745 THR A CG2 1 ATOM 5667 N N . LEU A 1 753 ? 9.888 74.387 59.760 1.00 20.78 ? 746 LEU A N 1 ATOM 5668 C CA . LEU A 1 753 ? 10.660 74.357 60.994 1.00 22.03 ? 746 LEU A CA 1 ATOM 5669 C C . LEU A 1 753 ? 10.583 75.693 61.734 1.00 23.17 ? 746 LEU A C 1 ATOM 5670 O O . LEU A 1 753 ? 11.133 75.825 62.831 1.00 23.56 ? 746 LEU A O 1 ATOM 5671 C CB . LEU A 1 753 ? 12.123 74.049 60.704 1.00 21.44 ? 746 LEU A CB 1 ATOM 5672 C CG . LEU A 1 753 ? 12.368 72.661 60.061 1.00 24.72 ? 746 LEU A CG 1 ATOM 5673 C CD1 . LEU A 1 753 ? 13.870 72.508 59.819 1.00 22.45 ? 746 LEU A CD1 1 ATOM 5674 C CD2 . LEU A 1 753 ? 11.841 71.504 60.970 1.00 21.64 ? 746 LEU A CD2 1 ATOM 5675 N N . SER A 1 754 ? 9.955 76.717 61.121 1.00 23.02 ? 747 SER A N 1 ATOM 5676 C CA . SER A 1 754 ? 9.823 77.987 61.815 1.00 23.12 ? 747 SER A CA 1 ATOM 5677 C C . SER A 1 754 ? 8.868 77.775 62.988 1.00 23.74 ? 747 SER A C 1 ATOM 5678 O O . SER A 1 754 ? 8.163 76.748 63.059 1.00 22.75 ? 747 SER A O 1 ATOM 5679 C CB . SER A 1 754 ? 9.258 79.053 60.881 1.00 23.47 ? 747 SER A CB 1 ATOM 5680 O OG . SER A 1 754 ? 10.129 79.164 59.764 1.00 25.90 ? 747 SER A OG 1 ATOM 5681 N N . GLU A 1 755 ? 8.811 78.751 63.886 1.00 23.90 ? 748 GLU A N 1 ATOM 5682 C CA . GLU A 1 755 ? 7.751 78.761 64.903 1.00 25.46 ? 748 GLU A CA 1 ATOM 5683 C C . GLU A 1 755 ? 6.401 78.670 64.191 1.00 24.89 ? 748 GLU A C 1 ATOM 5684 O O . GLU A 1 755 ? 6.194 79.276 63.115 1.00 24.73 ? 748 GLU A O 1 ATOM 5685 C CB . GLU A 1 755 ? 7.856 80.017 65.777 1.00 26.85 ? 748 GLU A CB 1 ATOM 5686 C CG . GLU A 1 755 ? 9.075 79.837 66.684 1.00 31.91 ? 748 GLU A CG 1 ATOM 5687 C CD . GLU A 1 755 ? 9.072 80.713 67.879 1.00 42.65 ? 748 GLU A CD 1 ATOM 5688 O OE1 . GLU A 1 755 ? 9.261 81.934 67.701 1.00 44.91 ? 748 GLU A OE1 1 ATOM 5689 O OE2 . GLU A 1 755 ? 8.913 80.160 68.981 1.00 44.81 ? 748 GLU A OE2 1 ATOM 5690 N N . VAL A 1 756 ? 5.514 77.848 64.755 1.00 24.18 ? 749 VAL A N 1 ATOM 5691 C CA . VAL A 1 756 ? 4.308 77.435 64.015 1.00 22.91 ? 749 VAL A CA 1 ATOM 5692 C C . VAL A 1 756 ? 3.252 78.549 63.987 1.00 24.03 ? 749 VAL A C 1 ATOM 5693 O O . VAL A 1 756 ? 2.329 78.514 63.186 1.00 23.64 ? 749 VAL A O 1 ATOM 5694 C CB . VAL A 1 756 ? 3.694 76.137 64.610 1.00 22.58 ? 749 VAL A CB 1 ATOM 5695 C CG1 . VAL A 1 756 ? 4.739 74.933 64.583 1.00 22.75 ? 749 VAL A CG1 1 ATOM 5696 C CG2 . VAL A 1 756 ? 3.164 76.369 66.078 1.00 23.81 ? 749 VAL A CG2 1 ATOM 5697 N N . ALA A 1 757 ? 3.364 79.508 64.909 1.00 24.86 ? 750 ALA A N 1 ATOM 5698 C CA . ALA A 1 757 ? 2.430 80.642 64.957 1.00 27.36 ? 750 ALA A CA 1 ATOM 5699 C C . ALA A 1 757 ? 3.115 81.805 65.642 1.00 30.29 ? 750 ALA A C 1 ATOM 5700 O O . ALA A 1 757 ? 2.780 82.965 65.369 1.00 32.20 ? 750 ALA A O 1 ATOM 5701 C CB . ALA A 1 757 ? 1.156 80.271 65.711 1.00 27.80 ? 750 ALA A CB 1 ATOM 5702 O OXT . ALA A 1 757 ? 3.993 81.562 66.492 1.00 30.82 ? 750 ALA A OXT 1 HETATM 5703 C C1 . NAG B 2 . ? 11.807 26.084 57.841 1.00 36.12 ? 801 NAG A C1 1 HETATM 5704 C C2 . NAG B 2 . ? 11.578 24.645 57.439 1.00 41.64 ? 801 NAG A C2 1 HETATM 5705 C C3 . NAG B 2 . ? 10.102 24.311 57.625 1.00 42.51 ? 801 NAG A C3 1 HETATM 5706 C C4 . NAG B 2 . ? 9.603 24.587 59.042 1.00 41.37 ? 801 NAG A C4 1 HETATM 5707 C C5 . NAG B 2 . ? 9.997 26.024 59.390 1.00 40.47 ? 801 NAG A C5 1 HETATM 5708 C C6 . NAG B 2 . ? 9.556 26.494 60.792 1.00 39.75 ? 801 NAG A C6 1 HETATM 5709 C C7 . NAG B 2 . ? 13.097 23.891 55.695 1.00 45.35 ? 801 NAG A C7 1 HETATM 5710 C C8 . NAG B 2 . ? 13.354 23.752 54.230 1.00 43.00 ? 801 NAG A C8 1 HETATM 5711 N N2 . NAG B 2 . ? 11.939 24.470 56.051 1.00 42.65 ? 801 NAG A N2 1 HETATM 5712 O O3 . NAG B 2 . ? 9.889 22.964 57.296 1.00 44.02 ? 801 NAG A O3 1 HETATM 5713 O O4 . NAG B 2 . ? 8.196 24.485 58.972 1.00 44.78 ? 801 NAG A O4 1 HETATM 5714 O O5 . NAG B 2 . ? 11.396 26.212 59.195 1.00 35.13 ? 801 NAG A O5 1 HETATM 5715 O O6 . NAG B 2 . ? 10.087 25.571 61.703 1.00 45.37 ? 801 NAG A O6 1 HETATM 5716 O O7 . NAG B 2 . ? 13.944 23.510 56.504 1.00 48.82 ? 801 NAG A O7 1 HETATM 5717 C C1 . NAG C 2 . ? 7.619 23.598 59.955 1.00 50.94 ? 802 NAG A C1 1 HETATM 5718 C C2 . NAG C 2 . ? 6.136 23.926 60.185 1.00 52.60 ? 802 NAG A C2 1 HETATM 5719 C C3 . NAG C 2 . ? 5.428 22.886 61.075 1.00 55.50 ? 802 NAG A C3 1 HETATM 5720 C C4 . NAG C 2 . ? 5.791 21.441 60.723 1.00 57.61 ? 802 NAG A C4 1 HETATM 5721 C C5 . NAG C 2 . ? 7.316 21.327 60.569 1.00 57.17 ? 802 NAG A C5 1 HETATM 5722 C C6 . NAG C 2 . ? 7.771 19.930 60.146 1.00 58.28 ? 802 NAG A C6 1 HETATM 5723 C C7 . NAG C 2 . ? 5.607 26.362 60.112 1.00 48.14 ? 802 NAG A C7 1 HETATM 5724 C C8 . NAG C 2 . ? 5.383 26.266 58.638 1.00 43.82 ? 802 NAG A C8 1 HETATM 5725 N N2 . NAG C 2 . ? 5.958 25.248 60.768 1.00 50.10 ? 802 NAG A N2 1 HETATM 5726 O O3 . NAG C 2 . ? 4.042 23.061 60.903 1.00 57.15 ? 802 NAG A O3 1 HETATM 5727 O O4 . NAG C 2 . ? 5.288 20.545 61.709 1.00 60.99 ? 802 NAG A O4 1 HETATM 5728 O O5 . NAG C 2 . ? 7.724 22.247 59.556 1.00 54.10 ? 802 NAG A O5 1 HETATM 5729 O O6 . NAG C 2 . ? 7.323 19.697 58.823 1.00 58.23 ? 802 NAG A O6 1 HETATM 5730 O O7 . NAG C 2 . ? 5.475 27.462 60.697 1.00 48.30 ? 802 NAG A O7 1 HETATM 5731 C C1 . NAG D 2 . ? 4.001 28.262 25.103 1.00 53.36 ? 803 NAG A C1 1 HETATM 5732 C C2 . NAG D 2 . ? 2.597 28.854 25.222 1.00 55.84 ? 803 NAG A C2 1 HETATM 5733 C C3 . NAG D 2 . ? 1.538 28.056 24.459 1.00 59.38 ? 803 NAG A C3 1 HETATM 5734 C C4 . NAG D 2 . ? 1.934 28.170 22.997 1.00 61.71 ? 803 NAG A C4 1 HETATM 5735 C C5 . NAG D 2 . ? 3.334 27.540 22.821 1.00 62.44 ? 803 NAG A C5 1 HETATM 5736 C C6 . NAG D 2 . ? 3.820 27.727 21.375 1.00 63.80 ? 803 NAG A C6 1 HETATM 5737 C C7 . NAG D 2 . ? 1.897 30.390 26.899 1.00 56.28 ? 803 NAG A C7 1 HETATM 5738 C C8 . NAG D 2 . ? 1.902 31.408 25.790 1.00 56.58 ? 803 NAG A C8 1 HETATM 5739 N N2 . NAG D 2 . ? 2.234 29.136 26.595 1.00 55.36 ? 803 NAG A N2 1 HETATM 5740 O O3 . NAG D 2 . ? 0.289 28.669 24.635 1.00 57.87 ? 803 NAG A O3 1 HETATM 5741 O O4 . NAG D 2 . ? 0.962 27.591 22.141 1.00 67.31 ? 803 NAG A O4 1 HETATM 5742 O O5 . NAG D 2 . ? 4.324 28.078 23.734 1.00 58.11 ? 803 NAG A O5 1 HETATM 5743 O O6 . NAG D 2 . ? 3.576 29.051 20.911 1.00 64.36 ? 803 NAG A O6 1 HETATM 5744 O O7 . NAG D 2 . ? 1.581 30.740 28.031 1.00 57.47 ? 803 NAG A O7 1 HETATM 5745 C C1 . NAG E 2 . ? 20.021 25.146 17.714 1.00 49.09 ? 804 NAG A C1 1 HETATM 5746 C C2 . NAG E 2 . ? 20.644 23.910 17.073 1.00 51.13 ? 804 NAG A C2 1 HETATM 5747 C C3 . NAG E 2 . ? 19.836 23.555 15.829 1.00 54.38 ? 804 NAG A C3 1 HETATM 5748 C C4 . NAG E 2 . ? 18.324 23.452 16.072 1.00 57.03 ? 804 NAG A C4 1 HETATM 5749 C C5 . NAG E 2 . ? 17.800 24.628 16.934 1.00 51.93 ? 804 NAG A C5 1 HETATM 5750 C C6 . NAG E 2 . ? 16.381 24.417 17.466 1.00 47.47 ? 804 NAG A C6 1 HETATM 5751 C C7 . NAG E 2 . ? 23.095 23.665 17.257 1.00 53.43 ? 804 NAG A C7 1 HETATM 5752 C C8 . NAG E 2 . ? 24.438 24.042 16.695 1.00 51.42 ? 804 NAG A C8 1 HETATM 5753 N N2 . NAG E 2 . ? 22.014 24.179 16.660 1.00 52.21 ? 804 NAG A N2 1 HETATM 5754 O O3 . NAG E 2 . ? 20.342 22.363 15.286 1.00 52.78 ? 804 NAG A O3 1 HETATM 5755 O O4 . NAG E 2 . ? 17.716 23.482 14.797 1.00 68.61 ? 804 NAG A O4 1 HETATM 5756 O O5 . NAG E 2 . ? 18.659 24.857 18.035 1.00 49.91 ? 804 NAG A O5 1 HETATM 5757 O O6 . NAG E 2 . ? 16.348 23.222 18.225 1.00 45.32 ? 804 NAG A O6 1 HETATM 5758 O O7 . NAG E 2 . ? 23.039 22.917 18.233 1.00 54.44 ? 804 NAG A O7 1 HETATM 5759 C C1 . NAG F 2 . ? 16.786 22.398 14.588 1.00 53.14 ? 805 NAG A C1 1 HETATM 5760 C C2 . NAG F 2 . ? 15.754 22.896 13.575 1.00 56.77 ? 805 NAG A C2 1 HETATM 5761 C C3 . NAG F 2 . ? 14.768 21.796 13.171 1.00 59.66 ? 805 NAG A C3 1 HETATM 5762 C C4 . NAG F 2 . ? 15.501 20.524 12.741 1.00 61.49 ? 805 NAG A C4 1 HETATM 5763 C C5 . NAG F 2 . ? 16.454 20.103 13.876 1.00 61.24 ? 805 NAG A C5 1 HETATM 5764 C C6 . NAG F 2 . ? 17.209 18.808 13.562 1.00 61.90 ? 805 NAG A C6 1 HETATM 5765 C C7 . NAG F 2 . ? 15.414 25.305 13.605 1.00 57.00 ? 805 NAG A C7 1 HETATM 5766 C C8 . NAG F 2 . ? 14.583 26.466 14.084 1.00 56.31 ? 805 NAG A C8 1 HETATM 5767 N N2 . NAG F 2 . ? 15.025 24.088 14.009 1.00 56.14 ? 805 NAG A N2 1 HETATM 5768 O O3 . NAG F 2 . ? 14.029 22.261 12.075 1.00 60.81 ? 805 NAG A O3 1 HETATM 5769 O O4 . NAG F 2 . ? 14.561 19.534 12.321 1.00 64.08 ? 805 NAG A O4 1 HETATM 5770 O O5 . NAG F 2 . ? 17.386 21.176 14.138 1.00 58.10 ? 805 NAG A O5 1 HETATM 5771 O O6 . NAG F 2 . ? 18.392 19.117 12.841 1.00 63.32 ? 805 NAG A O6 1 HETATM 5772 O O7 . NAG F 2 . ? 16.418 25.500 12.900 1.00 55.83 ? 805 NAG A O7 1 HETATM 5773 C C1 . NAG G 2 . ? 20.070 54.985 10.791 1.00 72.65 ? 806 NAG A C1 1 HETATM 5774 C C2 . NAG G 2 . ? 19.781 56.447 10.407 1.00 78.29 ? 806 NAG A C2 1 HETATM 5775 C C3 . NAG G 2 . ? 18.307 56.670 10.057 1.00 78.88 ? 806 NAG A C3 1 HETATM 5776 C C4 . NAG G 2 . ? 17.837 55.629 9.044 1.00 80.02 ? 806 NAG A C4 1 HETATM 5777 C C5 . NAG G 2 . ? 18.045 54.260 9.697 1.00 78.05 ? 806 NAG A C5 1 HETATM 5778 C C6 . NAG G 2 . ? 17.374 53.116 8.925 1.00 78.47 ? 806 NAG A C6 1 HETATM 5779 C C7 . NAG G 2 . ? 21.263 58.192 11.310 1.00 79.63 ? 806 NAG A C7 1 HETATM 5780 C C8 . NAG G 2 . ? 21.533 59.113 12.467 1.00 78.25 ? 806 NAG A C8 1 HETATM 5781 N N2 . NAG G 2 . ? 20.195 57.393 11.440 1.00 78.01 ? 806 NAG A N2 1 HETATM 5782 O O3 . NAG G 2 . ? 18.157 57.956 9.509 1.00 81.20 ? 806 NAG A O3 1 HETATM 5783 O O4 . NAG G 2 . ? 16.487 55.847 8.687 1.00 81.20 ? 806 NAG A O4 1 HETATM 5784 O O5 . NAG G 2 . ? 19.449 54.063 9.886 1.00 76.09 ? 806 NAG A O5 1 HETATM 5785 O O6 . NAG G 2 . ? 18.077 52.789 7.751 1.00 79.69 ? 806 NAG A O6 1 HETATM 5786 O O7 . NAG G 2 . ? 22.011 58.196 10.320 1.00 80.67 ? 806 NAG A O7 1 HETATM 5787 C C1 . NAG H 2 . ? 36.373 37.832 52.887 1.00 45.16 ? 807 NAG A C1 1 HETATM 5788 C C2 . NAG H 2 . ? 36.417 37.933 51.344 1.00 45.45 ? 807 NAG A C2 1 HETATM 5789 C C3 . NAG H 2 . ? 37.799 37.527 50.765 1.00 49.64 ? 807 NAG A C3 1 HETATM 5790 C C4 . NAG H 2 . ? 38.945 38.291 51.442 1.00 52.12 ? 807 NAG A C4 1 HETATM 5791 C C5 . NAG H 2 . ? 38.794 38.170 52.965 1.00 52.45 ? 807 NAG A C5 1 HETATM 5792 C C6 . NAG H 2 . ? 39.877 38.980 53.684 1.00 53.60 ? 807 NAG A C6 1 HETATM 5793 C C7 . NAG H 2 . ? 34.418 37.845 49.920 1.00 35.66 ? 807 NAG A C7 1 HETATM 5794 C C8 . NAG H 2 . ? 33.293 37.067 49.328 1.00 34.38 ? 807 NAG A C8 1 HETATM 5795 N N2 . NAG H 2 . ? 35.281 37.234 50.735 1.00 41.77 ? 807 NAG A N2 1 HETATM 5796 O O3 . NAG H 2 . ? 37.927 37.863 49.402 1.00 49.13 ? 807 NAG A O3 1 HETATM 5797 O O4 . NAG H 2 . ? 40.231 37.813 51.010 1.00 56.70 ? 807 NAG A O4 1 HETATM 5798 O O5 . NAG H 2 . ? 37.488 38.551 53.410 1.00 48.25 ? 807 NAG A O5 1 HETATM 5799 O O6 . NAG H 2 . ? 39.967 40.299 53.167 1.00 53.41 ? 807 NAG A O6 1 HETATM 5800 O O7 . NAG H 2 . ? 34.504 39.024 49.622 1.00 33.75 ? 807 NAG A O7 1 HETATM 5801 C C1 . NAG I 2 . ? 24.423 61.975 68.761 1.00 31.82 ? 808 NAG A C1 1 HETATM 5802 C C2 . NAG I 2 . ? 23.054 62.619 68.959 1.00 32.56 ? 808 NAG A C2 1 HETATM 5803 C C3 . NAG I 2 . ? 23.216 64.066 69.373 1.00 33.54 ? 808 NAG A C3 1 HETATM 5804 C C4 . NAG I 2 . ? 24.159 64.176 70.557 1.00 35.40 ? 808 NAG A C4 1 HETATM 5805 C C5 . NAG I 2 . ? 25.483 63.499 70.235 1.00 35.15 ? 808 NAG A C5 1 HETATM 5806 C C6 . NAG I 2 . ? 26.544 63.544 71.341 1.00 40.09 ? 808 NAG A C6 1 HETATM 5807 C C7 . NAG I 2 . ? 21.081 62.029 67.624 1.00 35.88 ? 808 NAG A C7 1 HETATM 5808 C C8 . NAG I 2 . ? 20.554 61.481 68.900 1.00 36.06 ? 808 NAG A C8 1 HETATM 5809 N N2 . NAG I 2 . ? 22.293 62.562 67.728 1.00 31.06 ? 808 NAG A N2 1 HETATM 5810 O O3 . NAG I 2 . ? 21.951 64.556 69.724 1.00 33.04 ? 808 NAG A O3 1 HETATM 5811 O O4 . NAG I 2 . ? 24.374 65.545 70.797 1.00 40.42 ? 808 NAG A O4 1 HETATM 5812 O O5 . NAG I 2 . ? 25.219 62.129 69.923 1.00 34.18 ? 808 NAG A O5 1 HETATM 5813 O O6 . NAG I 2 . ? 26.080 62.861 72.484 1.00 41.12 ? 808 NAG A O6 1 HETATM 5814 O O7 . NAG I 2 . ? 20.386 62.020 66.553 1.00 39.09 ? 808 NAG A O7 1 HETATM 5815 C C1 . NAG J 2 . ? 24.155 65.890 72.168 1.00 42.98 ? 809 NAG A C1 1 HETATM 5816 C C2 . NAG J 2 . ? 24.723 67.292 72.297 1.00 47.04 ? 809 NAG A C2 1 HETATM 5817 C C3 . NAG J 2 . ? 24.503 67.812 73.720 1.00 51.75 ? 809 NAG A C3 1 HETATM 5818 C C4 . NAG J 2 . ? 23.006 67.783 74.050 1.00 51.33 ? 809 NAG A C4 1 HETATM 5819 C C5 . NAG J 2 . ? 22.478 66.350 73.839 1.00 50.05 ? 809 NAG A C5 1 HETATM 5820 C C6 . NAG J 2 . ? 20.967 66.258 74.064 1.00 50.21 ? 809 NAG A C6 1 HETATM 5821 C C7 . NAG J 2 . ? 26.610 67.767 70.771 1.00 48.32 ? 809 NAG A C7 1 HETATM 5822 C C8 . NAG J 2 . ? 25.695 68.320 69.726 1.00 44.41 ? 809 NAG A C8 1 HETATM 5823 N N2 . NAG J 2 . ? 26.124 67.305 71.932 1.00 48.92 ? 809 NAG A N2 1 HETATM 5824 O O3 . NAG J 2 . ? 24.994 69.122 73.810 1.00 51.66 ? 809 NAG A O3 1 HETATM 5825 O O4 . NAG J 2 . ? 22.822 68.209 75.390 1.00 56.29 ? 809 NAG A O4 1 HETATM 5826 O O5 . NAG J 2 . ? 22.781 65.899 72.512 1.00 46.09 ? 809 NAG A O5 1 HETATM 5827 O O6 . NAG J 2 . ? 20.287 67.136 73.177 1.00 53.38 ? 809 NAG A O6 1 HETATM 5828 O O7 . NAG J 2 . ? 27.814 67.740 70.540 1.00 52.27 ? 809 NAG A O7 1 HETATM 5829 C C1 . NAG K 2 . ? 15.201 84.062 52.666 1.00 28.54 ? 810 NAG A C1 1 HETATM 5830 C C2 . NAG K 2 . ? 14.222 84.244 51.507 1.00 27.33 ? 810 NAG A C2 1 HETATM 5831 C C3 . NAG K 2 . ? 14.148 85.742 51.164 1.00 33.03 ? 810 NAG A C3 1 HETATM 5832 C C4 . NAG K 2 . ? 13.755 86.562 52.407 1.00 35.58 ? 810 NAG A C4 1 HETATM 5833 C C5 . NAG K 2 . ? 14.583 86.188 53.638 1.00 34.99 ? 810 NAG A C5 1 HETATM 5834 C C6 . NAG K 2 . ? 13.842 86.735 54.861 1.00 35.03 ? 810 NAG A C6 1 HETATM 5835 C C7 . NAG K 2 . ? 13.771 82.745 49.622 1.00 26.04 ? 810 NAG A C7 1 HETATM 5836 C C8 . NAG K 2 . ? 14.366 82.025 48.435 1.00 21.25 ? 810 NAG A C8 1 HETATM 5837 N N2 . NAG K 2 . ? 14.629 83.473 50.336 1.00 25.18 ? 810 NAG A N2 1 HETATM 5838 O O3 . NAG K 2 . ? 13.203 85.961 50.150 1.00 31.89 ? 810 NAG A O3 1 HETATM 5839 O O4 . NAG K 2 . ? 13.923 87.968 52.257 1.00 40.00 ? 810 NAG A O4 1 HETATM 5840 O O5 . NAG K 2 . ? 14.705 84.790 53.790 1.00 29.48 ? 810 NAG A O5 1 HETATM 5841 O O6 . NAG K 2 . ? 14.897 87.038 55.727 1.00 45.12 ? 810 NAG A O6 1 HETATM 5842 O O7 . NAG K 2 . ? 12.568 82.646 49.919 1.00 25.34 ? 810 NAG A O7 1 HETATM 5843 C C1 . NAG L 2 . ? 12.801 88.505 51.545 1.00 43.87 ? 811 NAG A C1 1 HETATM 5844 C C2 . NAG L 2 . ? 12.376 89.820 52.180 1.00 49.12 ? 811 NAG A C2 1 HETATM 5845 C C3 . NAG L 2 . ? 11.318 90.528 51.334 1.00 50.66 ? 811 NAG A C3 1 HETATM 5846 C C4 . NAG L 2 . ? 11.895 90.728 49.931 1.00 50.57 ? 811 NAG A C4 1 HETATM 5847 C C5 . NAG L 2 . ? 12.172 89.304 49.439 1.00 48.50 ? 811 NAG A C5 1 HETATM 5848 C C6 . NAG L 2 . ? 12.556 89.185 47.971 1.00 52.00 ? 811 NAG A C6 1 HETATM 5849 C C7 . NAG L 2 . ? 12.846 90.144 54.530 1.00 52.18 ? 811 NAG A C7 1 HETATM 5850 C C8 . NAG L 2 . ? 14.188 90.731 54.147 1.00 53.58 ? 811 NAG A C8 1 HETATM 5851 N N2 . NAG L 2 . ? 11.993 89.704 53.581 1.00 48.77 ? 811 NAG A N2 1 HETATM 5852 O O3 . NAG L 2 . ? 11.023 91.756 51.965 1.00 52.65 ? 811 NAG A O3 1 HETATM 5853 O O4 . NAG L 2 . ? 10.956 91.284 49.039 1.00 53.13 ? 811 NAG A O4 1 HETATM 5854 O O5 . NAG L 2 . ? 13.206 88.766 50.223 1.00 44.25 ? 811 NAG A O5 1 HETATM 5855 O O6 . NAG L 2 . ? 13.891 89.612 47.819 1.00 57.63 ? 811 NAG A O6 1 HETATM 5856 O O7 . NAG L 2 . ? 12.564 90.066 55.728 1.00 54.46 ? 811 NAG A O7 1 HETATM 5857 C C1 . BMA M 3 . ? 10.805 92.713 49.101 1.00 55.26 ? 812 BMA A C1 1 HETATM 5858 C C2 . BMA M 3 . ? 10.536 93.171 47.676 1.00 55.33 ? 812 BMA A C2 1 HETATM 5859 C C3 . BMA M 3 . ? 10.208 94.647 47.585 1.00 59.23 ? 812 BMA A C3 1 HETATM 5860 C C4 . BMA M 3 . ? 9.080 94.990 48.565 1.00 60.19 ? 812 BMA A C4 1 HETATM 5861 C C5 . BMA M 3 . ? 9.341 94.427 49.981 1.00 61.38 ? 812 BMA A C5 1 HETATM 5862 C C6 . BMA M 3 . ? 8.128 94.569 50.906 1.00 60.51 ? 812 BMA A C6 1 HETATM 5863 O O2 . BMA M 3 . ? 9.388 92.469 47.205 1.00 51.92 ? 812 BMA A O2 1 HETATM 5864 O O3 . BMA M 3 . ? 9.785 94.829 46.230 1.00 58.88 ? 812 BMA A O3 1 HETATM 5865 O O4 . BMA M 3 . ? 8.885 96.401 48.578 1.00 64.45 ? 812 BMA A O4 1 HETATM 5866 O O5 . BMA M 3 . ? 9.690 93.027 49.938 1.00 57.75 ? 812 BMA A O5 1 HETATM 5867 O O6 . BMA M 3 . ? 8.447 94.033 52.199 1.00 60.25 ? 812 BMA A O6 1 HETATM 5868 C C1 . MAN N 4 . ? 10.407 95.989 45.621 1.00 63.31 ? 813 MAN A C1 1 HETATM 5869 C C2 . MAN N 4 . ? 9.505 96.398 44.450 1.00 63.80 ? 813 MAN A C2 1 HETATM 5870 C C3 . MAN N 4 . ? 9.625 95.365 43.317 1.00 64.48 ? 813 MAN A C3 1 HETATM 5871 C C4 . MAN N 4 . ? 11.079 95.084 42.951 1.00 65.12 ? 813 MAN A C4 1 HETATM 5872 C C5 . MAN N 4 . ? 11.770 94.649 44.244 1.00 64.67 ? 813 MAN A C5 1 HETATM 5873 C C6 . MAN N 4 . ? 13.146 93.985 44.068 1.00 65.58 ? 813 MAN A C6 1 HETATM 5874 O O2 . MAN N 4 . ? 9.852 97.694 44.040 1.00 65.36 ? 813 MAN A O2 1 HETATM 5875 O O3 . MAN N 4 . ? 8.883 95.665 42.158 1.00 65.96 ? 813 MAN A O3 1 HETATM 5876 O O4 . MAN N 4 . ? 11.112 94.050 41.997 1.00 66.20 ? 813 MAN A O4 1 HETATM 5877 O O5 . MAN N 4 . ? 11.737 95.739 45.161 1.00 63.86 ? 813 MAN A O5 1 HETATM 5878 O O6 . MAN N 4 . ? 14.056 94.801 43.354 1.00 66.19 ? 813 MAN A O6 1 HETATM 5879 ZN ZN . ZN O 5 . ? 17.561 41.174 43.350 1.00 23.37 ? 814 ZN A ZN 1 HETATM 5880 ZN ZN . ZN P 5 . ? 16.814 41.965 46.417 1.00 20.16 ? 815 ZN A ZN 1 HETATM 5881 CA CA . CA Q 6 . ? -0.782 50.035 41.472 1.00 18.74 ? 816 CA A CA 1 HETATM 5882 CL CL . CL R 7 . ? 18.954 47.178 51.713 1.00 23.38 ? 817 CL A CL 1 HETATM 5883 N N . GLU S 8 . ? 16.406 45.145 42.910 1.00 20.87 ? 818 GLU A N 1 HETATM 5884 C CA . GLU S 8 . ? 15.950 44.553 41.597 1.00 21.35 ? 818 GLU A CA 1 HETATM 5885 C C . GLU S 8 . ? 17.077 44.667 40.574 1.00 22.94 ? 818 GLU A C 1 HETATM 5886 O O . GLU S 8 . ? 17.938 45.553 40.701 1.00 22.28 ? 818 GLU A O 1 HETATM 5887 C CB . GLU S 8 . ? 14.718 45.320 41.045 1.00 20.33 ? 818 GLU A CB 1 HETATM 5888 C CG . GLU S 8 . ? 14.973 46.851 40.928 1.00 20.51 ? 818 GLU A CG 1 HETATM 5889 C CD . GLU S 8 . ? 13.830 47.626 40.283 1.00 22.02 ? 818 GLU A CD 1 HETATM 5890 O OE1 . GLU S 8 . ? 12.994 47.027 39.565 1.00 21.76 ? 818 GLU A OE1 1 HETATM 5891 O OE2 . GLU S 8 . ? 13.772 48.857 40.485 1.00 22.76 ? 818 GLU A OE2 1 HETATM 5892 O OXT . GLU S 8 . ? 17.069 43.925 39.583 1.00 22.58 ? 818 GLU A OXT 1 HETATM 5893 N N . ASP T 9 . ? 21.813 44.930 45.449 1.00 46.01 ? 819 ASP A N 1 HETATM 5894 C CA . ASP T 9 . ? 21.180 45.840 44.467 1.00 43.76 ? 819 ASP A CA 1 HETATM 5895 C C . ASP T 9 . ? 20.119 46.740 45.120 1.00 42.38 ? 819 ASP A C 1 HETATM 5896 O O . ASP T 9 . ? 20.166 47.043 46.300 1.00 41.82 ? 819 ASP A O 1 HETATM 5897 C CB . ASP T 9 . ? 20.606 45.050 43.278 1.00 42.24 ? 819 ASP A CB 1 HETATM 5898 C CG . ASP T 9 . ? 19.347 44.237 43.637 1.00 39.18 ? 819 ASP A CG 1 HETATM 5899 O OD1 . ASP T 9 . ? 18.792 43.553 42.772 1.00 38.76 ? 819 ASP A OD1 1 HETATM 5900 O OD2 . ASP T 9 . ? 18.886 44.268 44.770 1.00 37.22 ? 819 ASP A OD2 1 HETATM 5901 O OXT . ASP T 9 . ? 19.202 47.196 44.441 1.00 42.03 ? 819 ASP A OXT 1 HETATM 5902 O O . HOH U 10 . ? 8.279 44.850 46.438 1.00 18.52 ? 901 HOH A O 1 HETATM 5903 O O . HOH U 10 . ? 6.893 58.443 37.497 1.00 18.57 ? 902 HOH A O 1 HETATM 5904 O O . HOH U 10 . ? 8.015 69.716 59.192 1.00 19.83 ? 903 HOH A O 1 HETATM 5905 O O . HOH U 10 . ? 13.733 44.763 49.765 1.00 17.86 ? 904 HOH A O 1 HETATM 5906 O O . HOH U 10 . ? 9.196 50.855 46.476 1.00 16.29 ? 905 HOH A O 1 HETATM 5907 O O . HOH U 10 . ? 0.993 50.562 39.932 1.00 18.18 ? 906 HOH A O 1 HETATM 5908 O O . HOH U 10 . ? 12.059 62.062 43.563 1.00 20.01 ? 907 HOH A O 1 HETATM 5909 O O . HOH U 10 . ? 13.608 29.956 40.161 1.00 24.54 ? 908 HOH A O 1 HETATM 5910 O O . HOH U 10 . ? 15.192 42.016 38.876 1.00 20.36 ? 909 HOH A O 1 HETATM 5911 O O . HOH U 10 . ? 9.602 60.991 57.703 1.00 18.33 ? 910 HOH A O 1 HETATM 5912 O O . HOH U 10 . ? 11.047 36.851 42.416 1.00 20.65 ? 911 HOH A O 1 HETATM 5913 O O . HOH U 10 . ? -5.490 59.886 59.776 1.00 20.72 ? 912 HOH A O 1 HETATM 5914 O O . HOH U 10 . ? 13.732 27.144 51.742 1.00 25.14 ? 913 HOH A O 1 HETATM 5915 O O . HOH U 10 . ? 7.422 71.980 45.251 1.00 21.58 ? 914 HOH A O 1 HETATM 5916 O O . HOH U 10 . ? 5.724 69.076 55.341 1.00 19.24 ? 915 HOH A O 1 HETATM 5917 O O . HOH U 10 . ? 16.869 37.230 44.034 1.00 20.99 ? 916 HOH A O 1 HETATM 5918 O O . HOH U 10 . ? -3.628 62.352 53.958 1.00 20.79 ? 917 HOH A O 1 HETATM 5919 O O . HOH U 10 . ? 29.464 36.254 44.310 1.00 23.94 ? 918 HOH A O 1 HETATM 5920 O O . HOH U 10 . ? 6.355 76.121 60.931 1.00 20.38 ? 919 HOH A O 1 HETATM 5921 O O . HOH U 10 . ? -3.488 60.301 61.795 1.00 20.64 ? 920 HOH A O 1 HETATM 5922 O O . HOH U 10 . ? 19.249 48.087 54.780 1.00 21.94 ? 921 HOH A O 1 HETATM 5923 O O . HOH U 10 . ? 4.011 70.564 64.485 1.00 23.76 ? 922 HOH A O 1 HETATM 5924 O O . HOH U 10 . ? 19.042 62.346 36.365 1.00 23.33 ? 923 HOH A O 1 HETATM 5925 O O . HOH U 10 . ? -7.092 51.681 51.532 1.00 21.53 ? 924 HOH A O 1 HETATM 5926 O O . HOH U 10 . ? 17.905 40.755 32.367 1.00 23.06 ? 925 HOH A O 1 HETATM 5927 O O . HOH U 10 . ? 20.080 61.675 62.873 1.00 23.37 ? 926 HOH A O 1 HETATM 5928 O O . HOH U 10 . ? -4.441 59.730 57.208 1.00 18.55 ? 927 HOH A O 1 HETATM 5929 O O . HOH U 10 . ? 3.525 72.214 43.510 1.00 18.12 ? 928 HOH A O 1 HETATM 5930 O O . HOH U 10 . ? 30.058 42.778 32.441 1.00 25.34 ? 929 HOH A O 1 HETATM 5931 O O . HOH U 10 . ? 23.976 46.209 34.838 1.00 23.87 ? 930 HOH A O 1 HETATM 5932 O O . HOH U 10 . ? 14.758 36.931 28.041 1.00 22.67 ? 931 HOH A O 1 HETATM 5933 O O . HOH U 10 . ? 18.538 33.646 43.622 1.00 26.00 ? 932 HOH A O 1 HETATM 5934 O O . HOH U 10 . ? 28.991 33.897 32.872 1.00 29.95 ? 933 HOH A O 1 HETATM 5935 O O . HOH U 10 . ? 6.006 75.566 54.193 1.00 21.66 ? 934 HOH A O 1 HETATM 5936 O O . HOH U 10 . ? 3.608 62.469 50.488 1.00 19.45 ? 935 HOH A O 1 HETATM 5937 O O . HOH U 10 . ? 14.662 32.148 48.161 1.00 23.12 ? 936 HOH A O 1 HETATM 5938 O O . HOH U 10 . ? 4.558 35.059 45.478 1.00 22.37 ? 937 HOH A O 1 HETATM 5939 O O . HOH U 10 . ? 0.237 57.030 45.751 1.00 22.25 ? 938 HOH A O 1 HETATM 5940 O O . HOH U 10 . ? -0.414 65.093 66.009 0.50 19.75 ? 939 HOH A O 1 HETATM 5941 O O . HOH U 10 . ? -0.261 43.514 60.921 1.00 25.59 ? 940 HOH A O 1 HETATM 5942 O O . HOH U 10 . ? 14.530 38.160 34.996 1.00 21.84 ? 941 HOH A O 1 HETATM 5943 O O . HOH U 10 . ? 22.162 88.178 32.344 1.00 32.10 ? 942 HOH A O 1 HETATM 5944 O O . HOH U 10 . ? 23.250 67.907 34.165 1.00 26.91 ? 943 HOH A O 1 HETATM 5945 O O . HOH U 10 . ? 23.166 68.941 43.003 1.00 22.35 ? 944 HOH A O 1 HETATM 5946 O O . HOH U 10 . ? 20.630 45.912 36.734 1.00 21.57 ? 945 HOH A O 1 HETATM 5947 O O . HOH U 10 . ? 24.520 37.353 32.634 1.00 25.27 ? 946 HOH A O 1 HETATM 5948 O O . HOH U 10 . ? 16.302 55.797 35.603 1.00 19.76 ? 947 HOH A O 1 HETATM 5949 O O . HOH U 10 . ? 25.814 37.131 38.129 1.00 25.38 ? 948 HOH A O 1 HETATM 5950 O O . HOH U 10 . ? 9.531 29.238 43.143 1.00 24.44 ? 949 HOH A O 1 HETATM 5951 O O . HOH U 10 . ? 27.526 31.187 28.875 1.00 30.60 ? 950 HOH A O 1 HETATM 5952 O O . HOH U 10 . ? 20.798 27.638 48.909 1.00 28.14 ? 951 HOH A O 1 HETATM 5953 O O . HOH U 10 . ? 10.262 31.083 26.714 1.00 31.19 ? 952 HOH A O 1 HETATM 5954 O O . HOH U 10 . ? 16.954 62.216 38.345 1.00 21.92 ? 953 HOH A O 1 HETATM 5955 O O . HOH U 10 . ? 19.391 36.246 43.361 1.00 24.69 ? 954 HOH A O 1 HETATM 5956 O O . HOH U 10 . ? 20.219 31.417 43.617 1.00 23.07 ? 955 HOH A O 1 HETATM 5957 O O . HOH U 10 . ? 8.042 50.441 40.796 1.00 19.12 ? 956 HOH A O 1 HETATM 5958 O O . HOH U 10 . ? -2.544 44.247 37.737 1.00 21.33 ? 957 HOH A O 1 HETATM 5959 O O . HOH U 10 . ? 6.502 60.974 67.159 1.00 24.42 ? 958 HOH A O 1 HETATM 5960 O O . HOH U 10 . ? 5.169 64.901 36.974 1.00 20.05 ? 959 HOH A O 1 HETATM 5961 O O . HOH U 10 . ? 14.724 81.072 38.151 1.00 26.08 ? 960 HOH A O 1 HETATM 5962 O O . HOH U 10 . ? 6.754 55.082 43.800 1.00 19.48 ? 961 HOH A O 1 HETATM 5963 O O . HOH U 10 . ? 14.021 40.973 53.546 1.00 19.87 ? 962 HOH A O 1 HETATM 5964 O O . HOH U 10 . ? 11.139 27.544 54.446 1.00 28.40 ? 963 HOH A O 1 HETATM 5965 O O . HOH U 10 . ? 22.929 44.521 36.819 1.00 24.54 ? 964 HOH A O 1 HETATM 5966 O O . HOH U 10 . ? 13.978 68.170 34.786 1.00 24.00 ? 965 HOH A O 1 HETATM 5967 O O . HOH U 10 . ? 4.436 67.240 51.485 1.00 23.07 ? 966 HOH A O 1 HETATM 5968 O O . HOH U 10 . ? 4.032 68.793 49.237 1.00 19.93 ? 967 HOH A O 1 HETATM 5969 O O . HOH U 10 . ? -4.491 55.347 51.803 1.00 23.30 ? 968 HOH A O 1 HETATM 5970 O O . HOH U 10 . ? 1.213 59.443 46.400 1.00 26.52 ? 969 HOH A O 1 HETATM 5971 O O . HOH U 10 . ? 2.643 33.210 45.343 1.00 24.83 ? 970 HOH A O 1 HETATM 5972 O O . HOH U 10 . ? -3.913 57.757 46.296 1.00 26.23 ? 971 HOH A O 1 HETATM 5973 O O . HOH U 10 . ? 11.109 63.576 58.313 1.00 28.83 ? 972 HOH A O 1 HETATM 5974 O O . HOH U 10 . ? 28.597 53.982 53.073 1.00 27.09 ? 973 HOH A O 1 HETATM 5975 O O . HOH U 10 . ? 13.750 71.580 40.503 1.00 24.35 ? 974 HOH A O 1 HETATM 5976 O O . HOH U 10 . ? 19.025 27.835 35.160 1.00 23.30 ? 975 HOH A O 1 HETATM 5977 O O . HOH U 10 . ? 13.406 77.920 63.538 1.00 32.04 ? 976 HOH A O 1 HETATM 5978 O O . HOH U 10 . ? 34.471 41.818 50.092 1.00 34.92 ? 977 HOH A O 1 HETATM 5979 O O . HOH U 10 . ? 26.500 39.085 36.413 1.00 28.04 ? 978 HOH A O 1 HETATM 5980 O O . HOH U 10 . ? -2.554 59.462 48.581 1.00 24.51 ? 979 HOH A O 1 HETATM 5981 O O . HOH U 10 . ? 8.731 74.773 66.691 1.00 26.09 ? 980 HOH A O 1 HETATM 5982 O O . HOH U 10 . ? 24.500 31.762 28.829 1.00 30.76 ? 981 HOH A O 1 HETATM 5983 O O . HOH U 10 . ? 5.565 62.849 65.037 1.00 26.82 ? 982 HOH A O 1 HETATM 5984 O O . HOH U 10 . ? 14.453 31.984 29.605 1.00 26.98 ? 983 HOH A O 1 HETATM 5985 O O . HOH U 10 . ? 12.122 35.140 53.758 1.00 24.76 ? 984 HOH A O 1 HETATM 5986 O O . HOH U 10 . ? 10.654 37.436 54.525 1.00 30.69 ? 985 HOH A O 1 HETATM 5987 O O . HOH U 10 . ? 21.177 63.694 60.993 1.00 24.04 ? 986 HOH A O 1 HETATM 5988 O O . HOH U 10 . ? 3.620 27.822 41.460 1.00 30.39 ? 987 HOH A O 1 HETATM 5989 O O . HOH U 10 . ? 19.457 60.363 50.057 1.00 28.33 ? 988 HOH A O 1 HETATM 5990 O O . HOH U 10 . ? 20.470 53.239 47.537 1.00 26.86 ? 989 HOH A O 1 HETATM 5991 O O . HOH U 10 . ? 31.098 40.144 46.665 1.00 29.51 ? 990 HOH A O 1 HETATM 5992 O O . HOH U 10 . ? 5.330 78.238 54.628 1.00 19.61 ? 991 HOH A O 1 HETATM 5993 O O . HOH U 10 . ? 32.211 35.431 59.244 1.00 34.73 ? 992 HOH A O 1 HETATM 5994 O O . HOH U 10 . ? 21.861 61.856 36.703 1.00 26.81 ? 993 HOH A O 1 HETATM 5995 O O . HOH U 10 . ? 16.309 72.368 29.664 1.00 29.10 ? 994 HOH A O 1 HETATM 5996 O O . HOH U 10 . ? 14.657 59.141 74.568 1.00 31.68 ? 995 HOH A O 1 HETATM 5997 O O . HOH U 10 . ? 29.468 70.524 46.071 1.00 31.00 ? 996 HOH A O 1 HETATM 5998 O O . HOH U 10 . ? -2.226 55.678 46.153 1.00 25.06 ? 997 HOH A O 1 HETATM 5999 O O . HOH U 10 . ? 24.069 40.843 69.441 1.00 33.41 ? 998 HOH A O 1 HETATM 6000 O O . HOH U 10 . ? 5.601 62.921 70.523 1.00 25.45 ? 999 HOH A O 1 HETATM 6001 O O . HOH U 10 . ? 16.780 68.396 64.299 1.00 27.04 ? 1000 HOH A O 1 HETATM 6002 O O . HOH U 10 . ? 25.108 33.056 67.939 1.00 33.85 ? 1001 HOH A O 1 HETATM 6003 O O . HOH U 10 . ? -6.381 58.780 38.066 1.00 25.30 ? 1002 HOH A O 1 HETATM 6004 O O . HOH U 10 . ? 15.012 61.973 73.177 1.00 29.97 ? 1003 HOH A O 1 HETATM 6005 O O . HOH U 10 . ? 0.338 31.507 58.241 1.00 32.24 ? 1004 HOH A O 1 HETATM 6006 O O . HOH U 10 . ? 18.383 55.525 30.563 1.00 29.41 ? 1005 HOH A O 1 HETATM 6007 O O . HOH U 10 . ? 9.005 69.244 40.959 1.00 20.60 ? 1006 HOH A O 1 HETATM 6008 O O . HOH U 10 . ? 12.204 37.126 28.713 1.00 25.59 ? 1007 HOH A O 1 HETATM 6009 O O . HOH U 10 . ? 0.552 33.404 43.466 1.00 28.80 ? 1008 HOH A O 1 HETATM 6010 O O . HOH U 10 . ? 1.081 63.352 42.975 1.00 34.64 ? 1009 HOH A O 1 HETATM 6011 O O . HOH U 10 . ? 33.985 48.074 58.871 1.00 33.53 ? 1010 HOH A O 1 HETATM 6012 O O . HOH U 10 . ? 17.258 81.728 37.334 1.00 35.13 ? 1011 HOH A O 1 HETATM 6013 O O . HOH U 10 . ? 15.099 69.094 41.623 1.00 31.64 ? 1012 HOH A O 1 HETATM 6014 O O . HOH U 10 . ? 16.555 26.292 34.706 1.00 31.64 ? 1013 HOH A O 1 HETATM 6015 O O . HOH U 10 . ? 23.161 55.300 31.415 1.00 25.70 ? 1014 HOH A O 1 HETATM 6016 O O . HOH U 10 . ? 17.744 82.794 41.273 1.00 35.83 ? 1015 HOH A O 1 HETATM 6017 O O . HOH U 10 . ? 24.071 75.242 54.651 1.00 30.22 ? 1016 HOH A O 1 HETATM 6018 O O . HOH U 10 . ? 23.181 67.794 40.741 1.00 27.55 ? 1017 HOH A O 1 HETATM 6019 O O . HOH U 10 . ? 8.088 51.880 43.001 1.00 24.11 ? 1018 HOH A O 1 HETATM 6020 O O . HOH U 10 . ? 30.054 27.165 33.787 1.00 33.03 ? 1019 HOH A O 1 HETATM 6021 O O . HOH U 10 . ? 6.186 38.883 26.463 1.00 31.55 ? 1020 HOH A O 1 HETATM 6022 O O . HOH U 10 . ? 18.786 69.221 65.613 1.00 35.05 ? 1021 HOH A O 1 HETATM 6023 O O . HOH U 10 . ? 25.958 59.200 46.644 1.00 41.01 ? 1022 HOH A O 1 HETATM 6024 O O . HOH U 10 . ? 21.729 74.757 60.544 1.00 31.60 ? 1023 HOH A O 1 HETATM 6025 O O . HOH U 10 . ? -2.147 34.076 40.602 1.00 27.62 ? 1024 HOH A O 1 HETATM 6026 O O . HOH U 10 . ? 13.476 82.981 55.751 1.00 30.13 ? 1025 HOH A O 1 HETATM 6027 O O . HOH U 10 . ? 25.814 35.682 68.217 1.00 32.86 ? 1026 HOH A O 1 HETATM 6028 O O . HOH U 10 . ? 23.865 73.400 59.386 1.00 33.85 ? 1027 HOH A O 1 HETATM 6029 O O . HOH U 10 . ? -1.357 61.746 62.319 1.00 27.63 ? 1028 HOH A O 1 HETATM 6030 O O . HOH U 10 . ? 10.257 36.271 70.123 1.00 37.33 ? 1029 HOH A O 1 HETATM 6031 O O . HOH U 10 . ? 14.035 57.691 35.184 1.00 22.22 ? 1030 HOH A O 1 HETATM 6032 O O . HOH U 10 . ? 13.674 29.567 28.555 1.00 28.45 ? 1031 HOH A O 1 HETATM 6033 O O . HOH U 10 . ? 36.828 42.659 65.168 1.00 35.72 ? 1032 HOH A O 1 HETATM 6034 O O . HOH U 10 . ? 10.912 29.148 40.459 1.00 27.04 ? 1033 HOH A O 1 HETATM 6035 O O . HOH U 10 . ? 11.919 41.103 55.447 1.00 25.87 ? 1034 HOH A O 1 HETATM 6036 O O . HOH U 10 . ? 19.272 63.753 32.142 1.00 29.15 ? 1035 HOH A O 1 HETATM 6037 O O . HOH U 10 . ? 12.566 53.544 35.919 1.00 24.88 ? 1036 HOH A O 1 HETATM 6038 O O . HOH U 10 . ? 23.393 56.695 45.014 1.00 42.66 ? 1037 HOH A O 1 HETATM 6039 O O . HOH U 10 . ? 21.892 61.411 51.600 1.00 35.55 ? 1038 HOH A O 1 HETATM 6040 O O . HOH U 10 . ? 25.813 27.352 24.424 1.00 36.78 ? 1039 HOH A O 1 HETATM 6041 O O . HOH U 10 . ? 25.607 56.193 37.507 1.00 26.38 ? 1040 HOH A O 1 HETATM 6042 O O . HOH U 10 . ? 20.332 31.546 26.362 1.00 35.08 ? 1041 HOH A O 1 HETATM 6043 O O . HOH U 10 . ? 30.832 52.612 52.860 1.00 30.50 ? 1042 HOH A O 1 HETATM 6044 O O . HOH U 10 . ? 6.598 76.796 67.439 1.00 28.45 ? 1043 HOH A O 1 HETATM 6045 O O . HOH U 10 . ? 10.500 55.751 75.202 1.00 35.57 ? 1044 HOH A O 1 HETATM 6046 O O . HOH U 10 . ? 21.439 32.580 28.652 1.00 30.79 ? 1045 HOH A O 1 HETATM 6047 O O . HOH U 10 . ? 25.288 70.777 31.193 1.00 36.09 ? 1046 HOH A O 1 HETATM 6048 O O . HOH U 10 . ? 19.119 69.729 28.616 1.00 30.41 ? 1047 HOH A O 1 HETATM 6049 O O . HOH U 10 . ? 23.524 79.160 50.573 1.00 30.03 ? 1048 HOH A O 1 HETATM 6050 O O . HOH U 10 . ? -9.740 46.218 34.298 1.00 35.33 ? 1049 HOH A O 1 HETATM 6051 O O . HOH U 10 . ? 29.224 40.517 64.871 1.00 34.50 ? 1050 HOH A O 1 HETATM 6052 O O . HOH U 10 . ? 11.671 27.888 29.216 1.00 34.37 ? 1051 HOH A O 1 HETATM 6053 O O . HOH U 10 . ? 25.261 63.487 49.770 1.00 29.29 ? 1052 HOH A O 1 HETATM 6054 O O . HOH U 10 . ? 16.207 29.116 28.125 1.00 32.56 ? 1053 HOH A O 1 HETATM 6055 O O . HOH U 10 . ? 13.690 80.072 67.913 1.00 35.51 ? 1054 HOH A O 1 HETATM 6056 O O . HOH U 10 . ? 4.856 31.716 30.420 1.00 39.89 ? 1055 HOH A O 1 HETATM 6057 O O . HOH U 10 . ? 14.237 81.548 40.794 1.00 35.60 ? 1056 HOH A O 1 HETATM 6058 O O . HOH U 10 . ? 10.220 81.150 63.503 1.00 31.69 ? 1057 HOH A O 1 HETATM 6059 O O . HOH U 10 . ? 4.136 63.609 72.775 1.00 33.54 ? 1058 HOH A O 1 HETATM 6060 O O . HOH U 10 . ? -10.481 48.616 48.590 1.00 31.18 ? 1059 HOH A O 1 HETATM 6061 O O . HOH U 10 . ? 21.769 84.242 47.174 1.00 32.90 ? 1060 HOH A O 1 HETATM 6062 O O . HOH U 10 . ? 18.032 21.297 38.803 1.00 47.23 ? 1061 HOH A O 1 HETATM 6063 O O . HOH U 10 . ? 27.506 54.378 50.617 1.00 40.91 ? 1062 HOH A O 1 HETATM 6064 O O . HOH U 10 . ? 20.844 50.626 76.064 1.00 44.39 ? 1063 HOH A O 1 HETATM 6065 O O . HOH U 10 . ? 7.562 38.748 29.297 1.00 29.86 ? 1064 HOH A O 1 HETATM 6066 O O . HOH U 10 . ? 38.244 34.599 26.511 1.00 39.36 ? 1065 HOH A O 1 HETATM 6067 O O . HOH U 10 . ? 4.685 62.252 75.089 1.00 28.67 ? 1066 HOH A O 1 HETATM 6068 O O . HOH U 10 . ? -1.724 32.549 44.772 1.00 38.50 ? 1067 HOH A O 1 HETATM 6069 O O . HOH U 10 . ? -12.898 47.588 37.645 1.00 33.67 ? 1068 HOH A O 1 HETATM 6070 O O . HOH U 10 . ? 29.284 50.391 39.184 1.00 35.61 ? 1069 HOH A O 1 HETATM 6071 O O . HOH U 10 . ? 19.279 49.654 45.015 1.00 25.87 ? 1070 HOH A O 1 HETATM 6072 O O . HOH U 10 . ? -10.101 43.992 47.121 1.00 34.04 ? 1071 HOH A O 1 HETATM 6073 O O . HOH U 10 . ? 29.971 25.263 47.482 1.00 41.49 ? 1072 HOH A O 1 HETATM 6074 O O . HOH U 10 . ? 29.359 54.537 34.739 1.00 31.90 ? 1073 HOH A O 1 HETATM 6075 O O . HOH U 10 . ? 11.750 47.840 37.358 1.00 20.43 ? 1074 HOH A O 1 HETATM 6076 O O . HOH U 10 . ? -0.808 58.258 43.352 1.00 20.97 ? 1075 HOH A O 1 HETATM 6077 O O . HOH U 10 . ? 22.698 58.597 24.419 1.00 38.30 ? 1076 HOH A O 1 HETATM 6078 O O . HOH U 10 . ? -2.807 38.564 63.317 1.00 35.38 ? 1077 HOH A O 1 HETATM 6079 O O . HOH U 10 . ? 11.650 38.610 56.698 1.00 31.01 ? 1078 HOH A O 1 HETATM 6080 O O . HOH U 10 . ? 25.594 67.347 30.073 1.00 30.68 ? 1079 HOH A O 1 HETATM 6081 O O . HOH U 10 . ? 16.629 69.336 20.890 1.00 52.85 ? 1080 HOH A O 1 HETATM 6082 O O . HOH U 10 . ? 11.992 63.906 35.565 1.00 29.18 ? 1081 HOH A O 1 HETATM 6083 O O . HOH U 10 . ? 25.159 66.142 40.263 1.00 38.49 ? 1082 HOH A O 1 HETATM 6084 O O . HOH U 10 . ? 31.913 55.290 26.393 1.00 42.57 ? 1083 HOH A O 1 HETATM 6085 O O . HOH U 10 . ? 18.172 31.071 29.197 1.00 27.64 ? 1084 HOH A O 1 HETATM 6086 O O . HOH U 10 . ? 28.997 26.096 36.125 1.00 32.23 ? 1085 HOH A O 1 HETATM 6087 O O . HOH U 10 . ? 16.675 79.829 21.133 1.00 41.28 ? 1086 HOH A O 1 HETATM 6088 O O . HOH U 10 . ? 20.074 25.768 36.818 1.00 30.83 ? 1087 HOH A O 1 HETATM 6089 O O . HOH U 10 . ? 28.218 45.445 68.953 1.00 34.53 ? 1088 HOH A O 1 HETATM 6090 O O . HOH U 10 . ? 18.033 52.571 75.072 1.00 39.67 ? 1089 HOH A O 1 HETATM 6091 O O . HOH U 10 . ? 12.856 93.936 40.184 1.00 56.59 ? 1090 HOH A O 1 HETATM 6092 O O . HOH U 10 . ? 0.739 33.641 36.624 1.00 39.69 ? 1091 HOH A O 1 HETATM 6093 O O . HOH U 10 . ? 30.538 48.812 47.215 1.00 51.71 ? 1092 HOH A O 1 HETATM 6094 O O . HOH U 10 . ? 25.795 25.526 20.114 1.00 41.63 ? 1093 HOH A O 1 HETATM 6095 O O . HOH U 10 . ? 35.039 51.130 31.429 1.00 45.22 ? 1094 HOH A O 1 HETATM 6096 O O . HOH U 10 . ? 20.596 30.339 29.890 1.00 33.23 ? 1095 HOH A O 1 HETATM 6097 O O . HOH U 10 . ? 12.974 69.710 32.738 1.00 32.14 ? 1096 HOH A O 1 HETATM 6098 O O . HOH U 10 . ? 24.615 29.678 30.516 1.00 35.37 ? 1097 HOH A O 1 HETATM 6099 O O . HOH U 10 . ? 26.621 40.179 13.564 1.00 41.17 ? 1098 HOH A O 1 HETATM 6100 O O . HOH U 10 . ? -2.668 32.960 55.980 1.00 40.18 ? 1099 HOH A O 1 HETATM 6101 O O . HOH U 10 . ? 24.255 82.337 42.406 1.00 37.21 ? 1100 HOH A O 1 HETATM 6102 O O . HOH U 10 . ? 29.208 79.220 27.544 1.00 40.97 ? 1101 HOH A O 1 HETATM 6103 O O . HOH U 10 . ? 10.552 27.285 51.514 1.00 36.76 ? 1102 HOH A O 1 HETATM 6104 O O . HOH U 10 . ? 5.178 40.257 23.221 1.00 35.67 ? 1103 HOH A O 1 HETATM 6105 O O . HOH U 10 . ? 36.124 43.162 57.507 1.00 34.87 ? 1104 HOH A O 1 HETATM 6106 O O . HOH U 10 . ? 36.930 52.473 68.453 1.00 44.42 ? 1105 HOH A O 1 HETATM 6107 O O . HOH U 10 . ? 9.963 70.057 38.654 1.00 32.60 ? 1106 HOH A O 1 HETATM 6108 O O . HOH U 10 . ? 22.870 65.483 66.108 1.00 35.15 ? 1107 HOH A O 1 HETATM 6109 O O . HOH U 10 . ? 27.280 57.225 70.395 1.00 38.30 ? 1108 HOH A O 1 HETATM 6110 O O . HOH U 10 . ? 6.978 76.029 37.685 1.00 28.71 ? 1109 HOH A O 1 HETATM 6111 O O . HOH U 10 . ? 34.837 41.496 19.688 1.00 52.70 ? 1110 HOH A O 1 HETATM 6112 O O . HOH U 10 . ? 39.682 43.898 58.317 1.00 35.04 ? 1111 HOH A O 1 HETATM 6113 O O . HOH U 10 . ? 26.790 16.875 39.869 1.00 45.80 ? 1112 HOH A O 1 HETATM 6114 O O . HOH U 10 . ? 27.991 72.344 53.152 1.00 42.79 ? 1113 HOH A O 1 HETATM 6115 O O . HOH U 10 . ? 9.697 26.531 44.073 1.00 45.97 ? 1114 HOH A O 1 HETATM 6116 O O . HOH U 10 . ? 5.069 31.715 24.568 1.00 40.18 ? 1115 HOH A O 1 HETATM 6117 O O . HOH U 10 . ? 30.881 41.550 40.516 1.00 34.21 ? 1116 HOH A O 1 HETATM 6118 O O . HOH U 10 . ? 23.278 68.606 69.104 0.50 32.26 ? 1117 HOH A O 1 HETATM 6119 O O . HOH U 10 . ? 26.393 60.362 30.618 1.00 42.14 ? 1118 HOH A O 1 HETATM 6120 O O . HOH U 10 . ? -1.714 46.291 55.827 1.00 30.66 ? 1119 HOH A O 1 HETATM 6121 O O . HOH U 10 . ? 1.788 31.208 64.899 1.00 41.75 ? 1120 HOH A O 1 HETATM 6122 O O . HOH U 10 . ? 21.737 25.385 23.786 1.00 46.62 ? 1121 HOH A O 1 HETATM 6123 O O . HOH U 10 . ? 0.755 66.279 62.982 1.00 49.03 ? 1122 HOH A O 1 HETATM 6124 O O . HOH U 10 . ? 23.963 61.643 34.778 1.00 34.60 ? 1123 HOH A O 1 HETATM 6125 O O . HOH U 10 . ? 11.184 76.910 28.533 1.00 35.64 ? 1124 HOH A O 1 HETATM 6126 O O . HOH U 10 . ? 26.296 23.566 45.842 1.00 38.41 ? 1125 HOH A O 1 HETATM 6127 O O . HOH U 10 . ? 20.674 44.100 11.506 1.00 44.78 ? 1126 HOH A O 1 HETATM 6128 O O . HOH U 10 . ? -3.882 37.633 56.658 1.00 34.20 ? 1127 HOH A O 1 HETATM 6129 O O . HOH U 10 . ? 16.122 67.745 72.589 1.00 48.94 ? 1128 HOH A O 1 HETATM 6130 O O . HOH U 10 . ? 11.613 48.876 29.622 1.00 26.81 ? 1129 HOH A O 1 HETATM 6131 O O . HOH U 10 . ? 5.385 66.255 33.938 1.00 39.76 ? 1130 HOH A O 1 HETATM 6132 O O . HOH U 10 . ? -2.883 38.057 32.696 1.00 32.50 ? 1131 HOH A O 1 HETATM 6133 O O . HOH U 10 . ? 24.365 77.993 53.097 1.00 42.62 ? 1132 HOH A O 1 HETATM 6134 O O . HOH U 10 . ? 20.968 74.587 23.722 1.00 41.04 ? 1133 HOH A O 1 HETATM 6135 O O . HOH U 10 . ? 10.204 51.926 40.024 1.00 19.47 ? 1134 HOH A O 1 HETATM 6136 O O . HOH U 10 . ? 30.872 84.221 28.564 1.00 43.74 ? 1135 HOH A O 1 HETATM 6137 O O . HOH U 10 . ? 0.410 63.183 48.119 1.00 40.10 ? 1136 HOH A O 1 HETATM 6138 O O . HOH U 10 . ? 26.572 66.243 26.230 1.00 40.96 ? 1137 HOH A O 1 HETATM 6139 O O . HOH U 10 . ? 14.740 23.065 37.745 1.00 40.75 ? 1138 HOH A O 1 HETATM 6140 O O . HOH U 10 . ? 31.564 46.872 36.932 1.00 44.37 ? 1139 HOH A O 1 HETATM 6141 O O . HOH U 10 . ? 28.362 64.053 23.142 1.00 49.38 ? 1140 HOH A O 1 HETATM 6142 O O . HOH U 10 . ? -4.285 53.389 37.230 1.00 30.79 ? 1141 HOH A O 1 HETATM 6143 O O . HOH U 10 . ? 28.801 44.655 65.467 1.00 44.11 ? 1142 HOH A O 1 HETATM 6144 O O . HOH U 10 . ? 8.441 82.677 52.068 1.00 32.73 ? 1143 HOH A O 1 HETATM 6145 O O . HOH U 10 . ? 33.075 30.247 24.422 1.00 47.75 ? 1144 HOH A O 1 HETATM 6146 O O . HOH U 10 . ? 15.023 52.750 34.883 1.00 28.91 ? 1145 HOH A O 1 HETATM 6147 O O . HOH U 10 . ? 15.226 24.804 58.698 1.00 40.22 ? 1146 HOH A O 1 HETATM 6148 O O . HOH U 10 . ? 4.181 43.859 76.093 1.00 46.57 ? 1147 HOH A O 1 HETATM 6149 O O . HOH U 10 . ? 9.322 52.352 75.192 1.00 38.88 ? 1148 HOH A O 1 HETATM 6150 O O . HOH U 10 . ? 18.876 66.050 28.010 1.00 37.93 ? 1149 HOH A O 1 HETATM 6151 O O . HOH U 10 . ? 17.979 32.426 70.670 1.00 40.52 ? 1150 HOH A O 1 HETATM 6152 O O . HOH U 10 . ? 13.960 50.436 19.053 1.00 36.90 ? 1151 HOH A O 1 HETATM 6153 O O . HOH U 10 . ? 12.243 22.743 37.079 1.00 58.02 ? 1152 HOH A O 1 HETATM 6154 O O . HOH U 10 . ? 21.876 51.978 45.019 1.00 39.12 ? 1153 HOH A O 1 HETATM 6155 O O . HOH U 10 . ? 17.806 65.461 30.371 1.00 30.72 ? 1154 HOH A O 1 HETATM 6156 O O . HOH U 10 . ? 3.374 27.498 57.392 1.00 49.58 ? 1155 HOH A O 1 HETATM 6157 O O . HOH U 10 . ? 22.256 58.770 69.771 1.00 57.64 ? 1156 HOH A O 1 HETATM 6158 O O . HOH U 10 . ? 38.130 41.833 57.544 1.00 48.91 ? 1157 HOH A O 1 HETATM 6159 O O . HOH U 10 . ? 26.048 24.945 57.463 1.00 42.38 ? 1158 HOH A O 1 HETATM 6160 O O . HOH U 10 . ? 29.372 69.980 39.695 1.00 41.78 ? 1159 HOH A O 1 HETATM 6161 O O . HOH U 10 . ? 3.734 27.428 54.684 1.00 37.69 ? 1160 HOH A O 1 HETATM 6162 O O . HOH U 10 . ? 15.054 81.804 28.399 1.00 44.67 ? 1161 HOH A O 1 HETATM 6163 O O . HOH U 10 . ? 23.729 45.547 39.299 1.00 38.10 ? 1162 HOH A O 1 HETATM 6164 O O . HOH U 10 . ? -4.468 54.067 34.614 1.00 33.09 ? 1163 HOH A O 1 HETATM 6165 O O . HOH U 10 . ? 21.367 75.309 66.910 1.00 47.80 ? 1164 HOH A O 1 HETATM 6166 O O . HOH U 10 . ? 34.313 32.717 27.456 1.00 46.42 ? 1165 HOH A O 1 HETATM 6167 O O . HOH U 10 . ? 21.163 88.578 44.272 1.00 38.82 ? 1166 HOH A O 1 HETATM 6168 O O . HOH U 10 . ? -4.037 37.276 51.297 1.00 42.84 ? 1167 HOH A O 1 HETATM 6169 O O . HOH U 10 . ? 33.911 28.936 34.329 1.00 45.54 ? 1168 HOH A O 1 HETATM 6170 O O . HOH U 10 . ? -5.865 41.643 44.524 1.00 33.37 ? 1169 HOH A O 1 HETATM 6171 O O . HOH U 10 . ? 13.919 65.468 36.001 1.00 43.43 ? 1170 HOH A O 1 HETATM 6172 O O . HOH U 10 . ? 33.738 40.178 47.405 1.00 41.98 ? 1171 HOH A O 1 HETATM 6173 O O . HOH U 10 . ? 11.945 50.120 36.407 1.00 20.64 ? 1172 HOH A O 1 HETATM 6174 O O . HOH U 10 . ? 31.209 31.873 17.364 1.00 48.43 ? 1173 HOH A O 1 HETATM 6175 O O . HOH U 10 . ? 30.327 59.925 25.326 1.00 43.52 ? 1174 HOH A O 1 HETATM 6176 O O . HOH U 10 . ? 5.265 53.427 77.689 1.00 45.59 ? 1175 HOH A O 1 HETATM 6177 O O . HOH U 10 . ? 12.437 43.646 17.301 1.00 40.55 ? 1176 HOH A O 1 HETATM 6178 O O . HOH U 10 . ? 26.689 69.514 29.044 1.00 45.30 ? 1177 HOH A O 1 HETATM 6179 O O . HOH U 10 . ? -5.077 41.875 50.597 1.00 37.82 ? 1178 HOH A O 1 HETATM 6180 O O . HOH U 10 . ? 36.327 43.502 49.062 1.00 45.45 ? 1179 HOH A O 1 HETATM 6181 O O . HOH U 10 . ? 19.595 58.412 68.644 1.00 48.02 ? 1180 HOH A O 1 HETATM 6182 O O . HOH U 10 . ? 13.477 28.046 17.164 1.00 53.91 ? 1181 HOH A O 1 HETATM 6183 O O . HOH U 10 . ? -3.479 47.380 53.182 1.00 35.61 ? 1182 HOH A O 1 HETATM 6184 O O . HOH U 10 . ? -7.312 48.152 48.245 1.00 35.32 ? 1183 HOH A O 1 HETATM 6185 O O . HOH U 10 . ? 10.018 24.352 54.303 1.00 51.68 ? 1184 HOH A O 1 HETATM 6186 O O . HOH U 10 . ? -0.826 32.519 60.762 1.00 46.55 ? 1185 HOH A O 1 HETATM 6187 O O . HOH U 10 . ? 16.209 79.629 69.268 1.00 50.90 ? 1186 HOH A O 1 HETATM 6188 O O . HOH U 10 . ? -8.861 41.569 48.016 1.00 53.29 ? 1187 HOH A O 1 HETATM 6189 O O . HOH U 10 . ? 19.765 56.103 23.064 1.00 37.71 ? 1188 HOH A O 1 HETATM 6190 O O . HOH U 10 . ? 32.732 42.874 20.214 1.00 45.46 ? 1189 HOH A O 1 HETATM 6191 O O . HOH U 10 . ? 21.356 24.128 51.338 1.00 39.21 ? 1190 HOH A O 1 HETATM 6192 O O . HOH U 10 . ? 16.736 63.598 69.009 1.00 46.19 ? 1191 HOH A O 1 HETATM 6193 O O . HOH U 10 . ? 28.465 24.863 53.432 0.50 39.16 ? 1192 HOH A O 1 HETATM 6194 O O . HOH U 10 . ? 29.343 28.275 59.487 1.00 53.50 ? 1193 HOH A O 1 HETATM 6195 O O . HOH U 10 . ? 27.238 20.250 40.003 1.00 38.84 ? 1194 HOH A O 1 HETATM 6196 O O . HOH U 10 . ? 4.909 27.682 30.658 1.00 47.10 ? 1195 HOH A O 1 HETATM 6197 O O . HOH U 10 . ? 5.813 82.083 54.269 1.00 32.43 ? 1196 HOH A O 1 HETATM 6198 O O . HOH U 10 . ? 8.397 29.428 33.317 1.00 43.02 ? 1197 HOH A O 1 HETATM 6199 O O . HOH U 10 . ? -1.189 51.600 72.493 1.00 39.34 ? 1198 HOH A O 1 HETATM 6200 O O . HOH U 10 . ? 39.202 31.379 45.574 1.00 48.80 ? 1199 HOH A O 1 HETATM 6201 O O . HOH U 10 . ? 37.277 61.668 55.046 0.50 36.61 ? 1200 HOH A O 1 HETATM 6202 O O . HOH U 10 . ? 8.911 56.738 43.750 1.00 29.80 ? 1201 HOH A O 1 HETATM 6203 O O . HOH U 10 . ? 23.138 75.911 25.702 1.00 40.30 ? 1202 HOH A O 1 HETATM 6204 O O . HOH U 10 . ? 6.009 68.590 37.134 1.00 35.77 ? 1203 HOH A O 1 HETATM 6205 O O . HOH U 10 . ? 12.383 27.688 21.567 1.00 47.62 ? 1204 HOH A O 1 HETATM 6206 O O . HOH U 10 . ? 38.796 55.249 62.241 1.00 54.64 ? 1205 HOH A O 1 HETATM 6207 O O . HOH U 10 . ? 12.846 71.898 80.168 1.00 44.63 ? 1206 HOH A O 1 HETATM 6208 O O . HOH U 10 . ? 11.610 81.515 60.708 1.00 48.88 ? 1207 HOH A O 1 HETATM 6209 O O . HOH U 10 . ? 1.373 37.062 68.794 1.00 40.25 ? 1208 HOH A O 1 HETATM 6210 O O . HOH U 10 . ? 5.217 72.556 80.010 1.00 55.56 ? 1209 HOH A O 1 HETATM 6211 O O . HOH U 10 . ? 28.967 58.223 48.219 1.00 40.75 ? 1210 HOH A O 1 HETATM 6212 O O . HOH U 10 . ? 12.929 32.953 70.978 1.00 42.61 ? 1211 HOH A O 1 HETATM 6213 O O . HOH U 10 . ? 14.808 73.358 23.781 1.00 54.93 ? 1212 HOH A O 1 HETATM 6214 O O . HOH U 10 . ? 18.795 40.750 76.011 1.00 40.22 ? 1213 HOH A O 1 HETATM 6215 O O . HOH U 10 . ? 20.242 46.105 79.048 1.00 49.16 ? 1214 HOH A O 1 HETATM 6216 O O . HOH U 10 . ? 5.869 56.376 35.845 1.00 30.13 ? 1215 HOH A O 1 HETATM 6217 O O . HOH U 10 . ? 1.942 33.808 24.443 1.00 54.82 ? 1216 HOH A O 1 HETATM 6218 O O . HOH U 10 . ? 37.138 40.336 55.620 1.00 42.23 ? 1217 HOH A O 1 HETATM 6219 O O . HOH U 10 . ? 23.495 60.419 39.760 1.00 36.39 ? 1218 HOH A O 1 HETATM 6220 O O . HOH U 10 . ? 30.773 71.822 43.687 1.00 39.82 ? 1219 HOH A O 1 HETATM 6221 O O . HOH U 10 . ? 8.509 74.927 75.554 1.00 39.54 ? 1220 HOH A O 1 HETATM 6222 O O . HOH U 10 . ? 3.063 38.603 27.295 1.00 41.23 ? 1221 HOH A O 1 HETATM 6223 O O . HOH U 10 . ? 38.707 38.771 35.276 1.00 48.24 ? 1222 HOH A O 1 HETATM 6224 O O . HOH U 10 . ? 18.378 59.855 70.187 1.00 49.42 ? 1223 HOH A O 1 HETATM 6225 O O . HOH U 10 . ? 38.428 43.314 55.301 1.00 46.95 ? 1224 HOH A O 1 HETATM 6226 O O . HOH U 10 . ? -0.986 57.090 74.009 1.00 49.62 ? 1225 HOH A O 1 HETATM 6227 O O . HOH U 10 . ? 26.924 31.064 64.049 1.00 54.21 ? 1226 HOH A O 1 HETATM 6228 O O . HOH U 10 . ? 25.298 86.078 42.629 1.00 34.89 ? 1227 HOH A O 1 HETATM 6229 O O . HOH U 10 . ? 12.062 56.531 31.555 1.00 35.97 ? 1228 HOH A O 1 HETATM 6230 O O . HOH U 10 . ? -14.182 42.551 41.563 1.00 46.60 ? 1229 HOH A O 1 HETATM 6231 O O . HOH U 10 . ? 22.099 80.909 22.896 1.00 45.44 ? 1230 HOH A O 1 HETATM 6232 O O . HOH U 10 . ? 40.576 45.373 19.736 1.00 53.03 ? 1231 HOH A O 1 HETATM 6233 O O . HOH U 10 . ? 10.769 36.997 76.482 1.00 46.94 ? 1232 HOH A O 1 HETATM 6234 O O . HOH U 10 . ? 13.775 55.217 32.920 1.00 33.80 ? 1233 HOH A O 1 HETATM 6235 O O . HOH U 10 . ? 28.202 53.714 37.274 1.00 36.92 ? 1234 HOH A O 1 HETATM 6236 O O . HOH U 10 . ? 28.424 61.376 68.410 1.00 46.27 ? 1235 HOH A O 1 HETATM 6237 O O . HOH U 10 . ? 26.105 32.233 6.214 0.50 43.36 ? 1236 HOH A O 1 HETATM 6238 O O . HOH U 10 . ? 24.569 23.081 53.265 1.00 45.41 ? 1237 HOH A O 1 HETATM 6239 O O . HOH U 10 . ? 15.342 25.654 30.074 1.00 39.61 ? 1238 HOH A O 1 HETATM 6240 O O . HOH U 10 . ? 30.343 61.702 22.841 1.00 50.87 ? 1239 HOH A O 1 HETATM 6241 O O . HOH U 10 . ? 7.757 57.778 33.542 1.00 51.69 ? 1240 HOH A O 1 HETATM 6242 O O . HOH U 10 . ? 6.582 42.840 27.321 1.00 34.92 ? 1241 HOH A O 1 HETATM 6243 O O . HOH U 10 . ? 35.163 44.190 68.189 1.00 52.12 ? 1242 HOH A O 1 HETATM 6244 O O . HOH U 10 . ? 30.952 35.706 16.982 1.00 48.62 ? 1243 HOH A O 1 HETATM 6245 O O . HOH U 10 . ? 37.143 26.062 48.118 1.00 49.95 ? 1244 HOH A O 1 HETATM 6246 O O . HOH U 10 . ? 12.124 29.099 19.404 1.00 43.97 ? 1245 HOH A O 1 HETATM 6247 O O . HOH U 10 . ? 26.999 28.542 28.409 1.00 50.03 ? 1246 HOH A O 1 HETATM 6248 O O . HOH U 10 . ? 15.922 55.129 72.486 1.00 55.28 ? 1247 HOH A O 1 HETATM 6249 O O . HOH U 10 . ? 6.334 95.907 42.231 1.00 53.95 ? 1248 HOH A O 1 HETATM 6250 O O . HOH U 10 . ? 9.538 75.209 69.547 1.00 49.86 ? 1249 HOH A O 1 HETATM 6251 O O . HOH U 10 . ? 10.545 84.357 51.333 1.00 32.79 ? 1250 HOH A O 1 HETATM 6252 O O . HOH U 10 . ? 40.898 32.422 39.421 1.00 41.22 ? 1251 HOH A O 1 HETATM 6253 O O . HOH U 10 . ? 30.162 76.000 43.324 1.00 49.28 ? 1252 HOH A O 1 HETATM 6254 O O . HOH U 10 . ? 0.821 64.025 38.311 1.00 47.46 ? 1253 HOH A O 1 HETATM 6255 O O . HOH U 10 . ? 25.316 65.218 44.742 1.00 35.49 ? 1254 HOH A O 1 HETATM 6256 O O . HOH U 10 . ? 25.192 56.942 32.291 1.00 38.10 ? 1255 HOH A O 1 HETATM 6257 O O . HOH U 10 . ? 32.550 84.913 32.612 1.00 49.67 ? 1256 HOH A O 1 HETATM 6258 O O . HOH U 10 . ? 39.395 57.528 57.805 1.00 64.52 ? 1257 HOH A O 1 HETATM 6259 O O . HOH U 10 . ? 8.889 54.503 31.211 1.00 32.63 ? 1258 HOH A O 1 HETATM 6260 O O . HOH U 10 . ? 24.050 24.652 30.447 1.00 41.12 ? 1259 HOH A O 1 HETATM 6261 O O . HOH U 10 . ? 6.100 44.925 25.599 1.00 46.88 ? 1260 HOH A O 1 HETATM 6262 O O . HOH U 10 . ? 5.018 64.014 76.906 1.00 43.46 ? 1261 HOH A O 1 HETATM 6263 O O . HOH U 10 . ? 17.369 25.981 59.633 1.00 35.80 ? 1262 HOH A O 1 HETATM 6264 O O . HOH U 10 . ? 0.246 29.993 44.885 1.00 51.52 ? 1263 HOH A O 1 HETATM 6265 O O . HOH U 10 . ? 2.579 63.607 40.584 1.00 34.11 ? 1264 HOH A O 1 HETATM 6266 O O . HOH U 10 . ? 10.038 24.228 44.747 1.00 53.26 ? 1265 HOH A O 1 HETATM 6267 O O . HOH U 10 . ? 23.272 58.897 21.458 1.00 51.40 ? 1266 HOH A O 1 HETATM 6268 O O . HOH U 10 . ? 21.398 24.141 27.427 1.00 54.44 ? 1267 HOH A O 1 HETATM 6269 O O . HOH U 10 . ? 13.884 61.566 32.996 1.00 48.39 ? 1268 HOH A O 1 HETATM 6270 O O . HOH U 10 . ? 42.262 34.877 37.744 1.00 58.84 ? 1269 HOH A O 1 HETATM 6271 O O . HOH U 10 . ? 29.304 73.229 49.962 1.00 46.01 ? 1270 HOH A O 1 HETATM 6272 O O . HOH U 10 . ? 18.283 87.095 25.614 0.50 41.02 ? 1271 HOH A O 1 HETATM 6273 O O . HOH U 10 . ? 22.290 83.748 49.792 1.00 39.30 ? 1272 HOH A O 1 HETATM 6274 O O . HOH U 10 . ? 24.270 82.551 24.504 1.00 44.40 ? 1273 HOH A O 1 HETATM 6275 O O . HOH U 10 . ? 29.519 30.536 15.034 1.00 54.04 ? 1274 HOH A O 1 HETATM 6276 O O . HOH U 10 . ? 36.087 34.740 51.160 1.00 47.93 ? 1275 HOH A O 1 HETATM 6277 O O . HOH U 10 . ? 24.552 83.374 45.626 1.00 47.61 ? 1276 HOH A O 1 HETATM 6278 O O . HOH U 10 . ? 26.283 62.440 65.510 1.00 41.20 ? 1277 HOH A O 1 HETATM 6279 O O . HOH U 10 . ? 6.881 26.939 40.602 1.00 54.18 ? 1278 HOH A O 1 HETATM 6280 O O . HOH U 10 . ? 24.636 68.305 63.148 1.00 40.97 ? 1279 HOH A O 1 HETATM 6281 O O . HOH U 10 . ? 30.830 72.329 47.876 1.00 47.29 ? 1280 HOH A O 1 HETATM 6282 O O . HOH U 10 . ? -5.060 44.664 30.920 1.00 39.66 ? 1281 HOH A O 1 HETATM 6283 O O . HOH U 10 . ? 27.025 65.104 35.145 1.00 42.12 ? 1282 HOH A O 1 HETATM 6284 O O . HOH U 10 . ? 17.723 64.882 67.265 1.00 43.03 ? 1283 HOH A O 1 HETATM 6285 O O . HOH U 10 . ? 19.235 24.950 12.458 1.00 53.06 ? 1284 HOH A O 1 HETATM 6286 O O . HOH U 10 . ? 33.832 53.332 32.025 1.00 43.70 ? 1285 HOH A O 1 HETATM 6287 O O . HOH U 10 . ? 30.905 70.491 37.249 1.00 49.35 ? 1286 HOH A O 1 HETATM 6288 O O . HOH U 10 . ? 1.199 60.237 43.655 1.00 28.03 ? 1287 HOH A O 1 HETATM 6289 O O . HOH U 10 . ? 2.984 65.042 50.940 1.00 25.39 ? 1288 HOH A O 1 HETATM 6290 O O . HOH U 10 . ? -8.260 49.709 50.028 1.00 34.13 ? 1289 HOH A O 1 HETATM 6291 O O . HOH U 10 . ? -4.188 58.326 36.284 1.00 38.13 ? 1290 HOH A O 1 HETATM 6292 O O . HOH U 10 . ? 9.388 28.792 38.255 1.00 42.53 ? 1291 HOH A O 1 HETATM 6293 O O . HOH U 10 . ? 15.061 25.032 32.584 1.00 37.17 ? 1292 HOH A O 1 HETATM 6294 O O . HOH U 10 . ? -1.881 63.606 48.968 1.00 31.29 ? 1293 HOH A O 1 HETATM 6295 O O . HOH U 10 . ? 28.946 25.980 31.642 1.00 45.31 ? 1294 HOH A O 1 HETATM 6296 O O . HOH U 10 . ? 26.858 65.045 29.048 1.00 41.21 ? 1295 HOH A O 1 HETATM 6297 O O . HOH U 10 . ? 25.529 68.400 32.729 1.00 36.44 ? 1296 HOH A O 1 HETATM 6298 O O . HOH U 10 . ? 29.816 67.912 45.610 1.00 39.62 ? 1297 HOH A O 1 HETATM 6299 O O . HOH U 10 . ? 29.292 62.032 27.068 1.00 50.09 ? 1298 HOH A O 1 HETATM 6300 O O . HOH U 10 . ? 27.416 66.289 46.280 1.00 37.24 ? 1299 HOH A O 1 HETATM 6301 O O . HOH U 10 . ? 34.740 35.955 58.304 1.00 43.44 ? 1300 HOH A O 1 HETATM 6302 O O . HOH U 10 . ? 24.504 79.680 55.277 1.00 41.36 ? 1301 HOH A O 1 HETATM 6303 O O . HOH U 10 . ? 11.694 24.924 51.939 1.00 50.47 ? 1302 HOH A O 1 HETATM 6304 O O . HOH U 10 . ? 21.391 56.708 25.250 1.00 34.23 ? 1303 HOH A O 1 HETATM 6305 O O . HOH U 10 . ? 36.071 38.148 57.386 1.00 46.42 ? 1304 HOH A O 1 HETATM 6306 O O . HOH U 10 . ? 28.312 36.255 67.521 1.00 41.10 ? 1305 HOH A O 1 HETATM 6307 O O . HOH U 10 . ? 29.642 38.053 66.175 1.00 45.59 ? 1306 HOH A O 1 HETATM 6308 O O . HOH U 10 . ? 13.664 80.730 63.019 1.00 42.65 ? 1307 HOH A O 1 HETATM 6309 O O . HOH U 10 . ? 11.931 73.716 81.744 1.00 53.58 ? 1308 HOH A O 1 HETATM 6310 O O . HOH U 10 . ? 35.053 49.226 33.372 1.00 44.63 ? 1309 HOH A O 1 HETATM 6311 O O . HOH U 10 . ? 37.802 41.731 37.086 1.00 49.38 ? 1310 HOH A O 1 HETATM 6312 O O . HOH U 10 . ? -3.585 32.499 53.460 1.00 48.39 ? 1311 HOH A O 1 HETATM 6313 O O . HOH U 10 . ? 31.434 51.502 50.301 1.00 48.11 ? 1312 HOH A O 1 HETATM 6314 O O . HOH U 10 . ? 4.833 50.162 28.317 1.00 39.17 ? 1313 HOH A O 1 HETATM 6315 O O . HOH U 10 . ? 25.386 71.808 60.823 1.00 46.87 ? 1314 HOH A O 1 HETATM 6316 O O . HOH U 10 . ? 23.631 74.632 65.620 1.00 43.44 ? 1315 HOH A O 1 HETATM 6317 O O . HOH U 10 . ? 14.511 70.288 30.228 1.00 40.07 ? 1316 HOH A O 1 HETATM 6318 O O . HOH U 10 . ? 11.037 27.358 32.042 1.00 50.71 ? 1317 HOH A O 1 HETATM 6319 O O . HOH U 10 . ? 16.594 84.952 41.019 1.00 40.56 ? 1318 HOH A O 1 HETATM 6320 O O . HOH U 10 . ? 28.978 64.099 68.717 1.00 51.31 ? 1319 HOH A O 1 HETATM 6321 O O . HOH U 10 . ? 31.210 70.242 41.650 1.00 37.36 ? 1320 HOH A O 1 HETATM 6322 O O . HOH U 10 . ? 27.299 65.362 38.255 1.00 41.69 ? 1321 HOH A O 1 HETATM 6323 O O . HOH U 10 . ? -5.393 34.236 47.606 1.00 39.73 ? 1322 HOH A O 1 HETATM 6324 O O . HOH U 10 . ? 12.813 50.438 27.460 1.00 34.14 ? 1323 HOH A O 1 HETATM 6325 O O . HOH U 10 . ? -5.533 43.957 47.390 1.00 36.58 ? 1324 HOH A O 1 HETATM 6326 O O . HOH U 10 . ? 13.531 81.750 66.017 1.00 46.08 ? 1325 HOH A O 1 HETATM 6327 O O . HOH U 10 . ? 7.922 26.468 54.774 1.00 52.09 ? 1326 HOH A O 1 HETATM 6328 O O . HOH U 10 . ? 31.750 50.334 11.857 1.00 49.16 ? 1327 HOH A O 1 HETATM 6329 O O . HOH U 10 . ? 17.998 58.355 29.827 1.00 43.68 ? 1328 HOH A O 1 HETATM 6330 O O . HOH U 10 . ? 20.715 79.592 65.824 1.00 48.60 ? 1329 HOH A O 1 HETATM 6331 O O . HOH U 10 . ? 5.279 30.357 36.904 1.00 54.95 ? 1330 HOH A O 1 HETATM 6332 O O . HOH U 10 . ? 1.348 31.983 67.464 1.00 48.75 ? 1331 HOH A O 1 HETATM 6333 O O . HOH U 10 . ? 28.695 29.877 62.103 1.00 49.18 ? 1332 HOH A O 1 HETATM 6334 O O . HOH U 10 . ? 16.110 83.038 57.727 1.00 51.62 ? 1333 HOH A O 1 HETATM 6335 O O . HOH U 10 . ? 27.760 67.543 33.732 1.00 42.77 ? 1334 HOH A O 1 HETATM 6336 O O . HOH U 10 . ? 18.407 24.725 61.628 1.00 52.08 ? 1335 HOH A O 1 HETATM 6337 O O . HOH U 10 . ? 12.445 28.687 60.647 1.00 38.96 ? 1336 HOH A O 1 HETATM 6338 O O . HOH U 10 . ? 10.826 41.289 17.614 1.00 43.01 ? 1337 HOH A O 1 HETATM 6339 O O . HOH U 10 . ? 23.930 58.299 36.900 1.00 49.76 ? 1338 HOH A O 1 HETATM 6340 O O . HOH U 10 . ? 21.434 73.649 69.102 1.00 50.70 ? 1339 HOH A O 1 HETATM 6341 O O . HOH U 10 . ? 32.608 27.743 56.432 1.00 49.89 ? 1340 HOH A O 1 HETATM 6342 O O . HOH U 10 . ? 19.083 54.272 73.046 1.00 45.82 ? 1341 HOH A O 1 HETATM 6343 O O . HOH U 10 . ? 10.182 39.044 15.615 1.00 54.79 ? 1342 HOH A O 1 HETATM 6344 O O . HOH U 10 . ? -9.248 46.555 32.014 0.50 34.57 ? 1343 HOH A O 1 HETATM 6345 O O . HOH U 10 . ? 27.358 62.249 29.084 1.00 39.36 ? 1344 HOH A O 1 HETATM 6346 O O . HOH U 10 . ? 30.089 42.255 66.564 1.00 39.43 ? 1345 HOH A O 1 HETATM 6347 O O . HOH U 10 . ? 27.216 25.843 22.277 1.00 50.65 ? 1346 HOH A O 1 HETATM 6348 O O . HOH U 10 . ? 29.018 64.525 25.822 1.00 40.94 ? 1347 HOH A O 1 HETATM 6349 O O . HOH U 10 . ? 6.473 81.884 62.611 1.00 30.63 ? 1348 HOH A O 1 HETATM 6350 O O . HOH U 10 . ? 35.692 31.873 53.712 1.00 47.10 ? 1349 HOH A O 1 HETATM 6351 O O . HOH U 10 . ? 28.288 56.762 34.201 1.00 45.79 ? 1350 HOH A O 1 HETATM 6352 O O . HOH U 10 . ? 26.184 74.873 56.029 1.00 52.30 ? 1351 HOH A O 1 HETATM 6353 O O . HOH U 10 . ? -9.321 45.788 48.585 1.00 41.23 ? 1352 HOH A O 1 HETATM 6354 O O . HOH U 10 . ? 24.670 60.118 32.483 1.00 49.57 ? 1353 HOH A O 1 HETATM 6355 O O . HOH U 10 . ? 32.270 58.035 26.596 1.00 50.08 ? 1354 HOH A O 1 HETATM 6356 O O . HOH U 10 . ? -3.731 47.035 24.916 1.00 43.55 ? 1355 HOH A O 1 HETATM 6357 O O . HOH U 10 . ? 40.298 45.664 16.997 1.00 53.80 ? 1356 HOH A O 1 HETATM 6358 O O . HOH U 10 . ? 24.470 81.777 50.348 1.00 54.06 ? 1357 HOH A O 1 HETATM 6359 O O . HOH U 10 . ? 15.250 57.389 32.069 1.00 42.47 ? 1358 HOH A O 1 HETATM 6360 O O . HOH U 10 . ? 13.963 54.908 37.414 1.00 39.02 ? 1359 HOH A O 1 HETATM 6361 O O . HOH U 10 . ? 19.887 22.481 12.601 1.00 56.61 ? 1360 HOH A O 1 HETATM 6362 O O . HOH U 10 . ? 22.660 55.257 69.701 1.00 52.40 ? 1361 HOH A O 1 HETATM 6363 O O . HOH U 10 . ? -10.543 43.652 38.436 1.00 51.56 ? 1362 HOH A O 1 HETATM 6364 O O . HOH U 10 . ? 15.586 30.032 12.934 1.00 48.50 ? 1363 HOH A O 1 HETATM 6365 O O . HOH U 10 . ? -4.973 36.720 40.400 1.00 49.58 ? 1364 HOH A O 1 HETATM 6366 O O . HOH U 10 . ? 1.803 66.569 37.391 1.00 48.34 ? 1365 HOH A O 1 HETATM 6367 O O . HOH U 10 . ? -5.592 50.806 28.365 1.00 45.05 ? 1366 HOH A O 1 HETATM 6368 O O . HOH U 10 . ? 31.887 74.239 44.044 1.00 53.89 ? 1367 HOH A O 1 HETATM 6369 O O . HOH U 10 . ? 34.072 55.086 68.201 1.00 49.72 ? 1368 HOH A O 1 HETATM 6370 O O . HOH U 10 . ? 37.799 42.052 52.832 1.00 44.80 ? 1369 HOH A O 1 HETATM 6371 O O . HOH U 10 . ? 21.348 43.317 78.006 1.00 52.48 ? 1370 HOH A O 1 HETATM 6372 O O . HOH U 10 . ? -12.680 45.956 35.556 1.00 47.29 ? 1371 HOH A O 1 HETATM 6373 O O . HOH U 10 . ? 17.786 61.078 30.484 1.00 46.88 ? 1372 HOH A O 1 HETATM 6374 O O . HOH U 10 . ? 28.398 42.049 68.529 1.00 44.91 ? 1373 HOH A O 1 HETATM 6375 O O . HOH U 10 . ? 17.095 20.917 51.731 1.00 47.92 ? 1374 HOH A O 1 HETATM 6376 O O . HOH U 10 . ? 20.233 57.799 27.567 1.00 38.33 ? 1375 HOH A O 1 HETATM 6377 O O . HOH U 10 . ? 32.568 41.818 67.440 1.00 55.11 ? 1376 HOH A O 1 HETATM 6378 O O . HOH U 10 . ? -0.287 41.079 71.514 1.00 55.83 ? 1377 HOH A O 1 HETATM 6379 O O . HOH U 10 . ? 16.065 68.175 29.448 1.00 44.08 ? 1378 HOH A O 1 HETATM 6380 O O . HOH U 10 . ? 24.536 22.029 31.369 1.00 48.07 ? 1379 HOH A O 1 HETATM 6381 O O . HOH U 10 . ? 25.113 25.126 26.086 1.00 55.73 ? 1380 HOH A O 1 HETATM 6382 O O . HOH U 10 . ? 13.964 69.120 75.697 1.00 46.64 ? 1381 HOH A O 1 HETATM 6383 O O . HOH U 10 . ? 8.044 29.914 36.388 1.00 54.03 ? 1382 HOH A O 1 HETATM 6384 O O . HOH U 10 . ? -8.794 43.610 35.096 1.00 47.05 ? 1383 HOH A O 1 HETATM 6385 O O . HOH U 10 . ? 1.821 41.174 27.233 1.00 44.99 ? 1384 HOH A O 1 HETATM 6386 O O . HOH U 10 . ? 31.966 74.867 36.446 1.00 49.98 ? 1385 HOH A O 1 HETATM 6387 O O . HOH U 10 . ? 33.687 54.291 28.349 1.00 46.73 ? 1386 HOH A O 1 HETATM 6388 O O . HOH U 10 . ? 9.631 47.290 80.238 1.00 55.92 ? 1387 HOH A O 1 HETATM 6389 O O . HOH U 10 . ? 8.820 22.748 46.683 1.00 54.43 ? 1388 HOH A O 1 HETATM 6390 O O . HOH U 10 . ? 17.633 56.917 27.083 1.00 44.44 ? 1389 HOH A O 1 HETATM 6391 O O . HOH U 10 . ? 30.408 25.903 38.317 1.00 44.28 ? 1390 HOH A O 1 HETATM 6392 O O . HOH U 10 . ? 18.027 24.102 36.139 1.00 50.24 ? 1391 HOH A O 1 HETATM 6393 O O . HOH U 10 . ? 19.808 30.583 70.768 1.00 56.44 ? 1392 HOH A O 1 HETATM 6394 O O . HOH U 10 . ? 31.522 55.155 35.232 0.50 35.30 ? 1393 HOH A O 1 HETATM 6395 O O . HOH U 10 . ? 35.748 33.905 55.053 1.00 43.75 ? 1394 HOH A O 1 HETATM 6396 O O . HOH U 10 . ? 26.303 62.622 47.960 1.00 42.12 ? 1395 HOH A O 1 HETATM 6397 O O . HOH U 10 . ? 5.659 32.191 73.864 0.50 41.83 ? 1396 HOH A O 1 HETATM 6398 O O . HOH U 10 . ? 17.372 66.627 70.751 1.00 47.19 ? 1397 HOH A O 1 HETATM 6399 O O . HOH U 10 . ? 3.431 48.936 26.722 1.00 47.20 ? 1398 HOH A O 1 HETATM 6400 O O . HOH U 10 . ? 7.400 49.276 77.820 0.50 40.14 ? 1399 HOH A O 1 HETATM 6401 O O . HOH U 10 . ? 15.112 78.815 72.183 1.00 55.08 ? 1400 HOH A O 1 HETATM 6402 O O . HOH U 10 . ? 6.535 24.363 56.658 1.00 57.77 ? 1401 HOH A O 1 HETATM 6403 O O . HOH U 10 . ? 25.683 63.226 38.693 1.00 44.90 ? 1402 HOH A O 1 HETATM 6404 O O . HOH U 10 . ? 10.087 82.849 56.284 1.00 54.47 ? 1403 HOH A O 1 HETATM 6405 O O . HOH U 10 . ? 33.066 54.721 70.401 0.50 31.58 ? 1404 HOH A O 1 HETATM 6406 O O . HOH U 10 . ? 39.013 39.007 64.837 1.00 52.72 ? 1405 HOH A O 1 HETATM 6407 O O . HOH U 10 . ? 14.307 40.843 12.404 0.50 33.48 ? 1406 HOH A O 1 HETATM 6408 O O . HOH U 10 . ? -1.253 53.560 23.987 1.00 65.39 ? 1407 HOH A O 1 HETATM 6409 O O . HOH U 10 . ? 25.398 69.381 60.768 1.00 50.16 ? 1408 HOH A O 1 HETATM 6410 O O . HOH U 10 . ? 40.506 47.691 29.201 1.00 60.44 ? 1409 HOH A O 1 HETATM 6411 O O . HOH U 10 . ? 21.419 54.458 16.515 1.00 52.56 ? 1410 HOH A O 1 HETATM 6412 O O . HOH U 10 . ? 25.799 25.735 46.601 1.00 40.81 ? 1411 HOH A O 1 HETATM 6413 O O . HOH U 10 . ? 12.418 25.070 33.122 1.00 45.94 ? 1412 HOH A O 1 HETATM 6414 O O . HOH U 10 . ? 6.023 53.667 30.148 1.00 31.50 ? 1413 HOH A O 1 HETATM 6415 O O . HOH U 10 . ? -0.118 60.643 48.427 1.00 35.17 ? 1414 HOH A O 1 HETATM 6416 O O . HOH U 10 . ? 10.063 75.960 30.842 1.00 40.54 ? 1415 HOH A O 1 HETATM 6417 O O . HOH U 10 . ? 23.135 45.312 41.542 1.00 42.29 ? 1416 HOH A O 1 HETATM 6418 O O . HOH U 10 . ? 8.090 56.660 75.739 1.00 30.65 ? 1417 HOH A O 1 HETATM 6419 O O . HOH U 10 . ? 6.722 53.931 75.574 1.00 36.28 ? 1418 HOH A O 1 HETATM 6420 O O . HOH U 10 . ? 11.346 52.569 28.053 1.00 43.99 ? 1419 HOH A O 1 HETATM 6421 O O . HOH U 10 . ? 29.428 61.171 53.561 1.00 45.12 ? 1420 HOH A O 1 HETATM 6422 O O . HOH U 10 . ? 24.573 20.812 33.691 1.00 46.97 ? 1421 HOH A O 1 HETATM 6423 O O . HOH U 10 . ? 23.231 61.259 20.080 1.00 48.62 ? 1422 HOH A O 1 HETATM 6424 O O . HOH U 10 . ? 36.014 31.148 34.192 1.00 55.45 ? 1423 HOH A O 1 HETATM 6425 O O . HOH U 10 . ? -1.991 41.288 30.318 1.00 59.16 ? 1424 HOH A O 1 HETATM 6426 O O . HOH U 10 . ? 38.879 35.224 19.749 0.50 38.38 ? 1425 HOH A O 1 HETATM 6427 O O . HOH U 10 . ? 36.536 46.647 31.808 1.00 43.30 ? 1426 HOH A O 1 HETATM 6428 O O . HOH U 10 . ? 22.873 48.106 42.679 1.00 50.50 ? 1427 HOH A O 1 HETATM 6429 O O . HOH U 10 . ? 20.106 81.487 62.596 1.00 57.41 ? 1428 HOH A O 1 HETATM 6430 O O . HOH U 10 . ? 3.950 64.233 34.933 1.00 38.23 ? 1429 HOH A O 1 HETATM 6431 O O . HOH U 10 . ? 13.918 59.260 33.040 1.00 51.94 ? 1430 HOH A O 1 HETATM 6432 O O . HOH U 10 . ? 20.243 64.299 25.596 1.00 53.29 ? 1431 HOH A O 1 HETATM 6433 O O . HOH U 10 . ? 20.445 61.920 27.243 1.00 46.08 ? 1432 HOH A O 1 HETATM 6434 O O . HOH U 10 . ? 38.221 34.435 48.485 1.00 50.08 ? 1433 HOH A O 1 HETATM 6435 O O . HOH U 10 . ? 11.555 54.669 26.335 1.00 55.59 ? 1434 HOH A O 1 HETATM 6436 O O . HOH U 10 . ? 23.690 43.985 44.393 1.00 53.15 ? 1435 HOH A O 1 HETATM 6437 O O . HOH U 10 . ? 24.107 53.625 46.338 1.00 48.44 ? 1436 HOH A O 1 HETATM 6438 O O . HOH U 10 . ? 20.321 43.430 47.328 1.00 35.48 ? 1437 HOH A O 1 HETATM 6439 O O . HOH U 10 . ? 33.527 49.830 50.453 1.00 48.41 ? 1438 HOH A O 1 HETATM 6440 O O . HOH U 10 . ? 28.030 71.230 32.792 1.00 53.18 ? 1439 HOH A O 1 HETATM 6441 O O . HOH U 10 . ? 23.152 88.544 41.287 1.00 41.79 ? 1440 HOH A O 1 HETATM 6442 O O . HOH U 10 . ? 17.342 59.239 44.963 1.00 38.00 ? 1441 HOH A O 1 HETATM 6443 O O . HOH U 10 . ? 25.853 57.185 34.709 1.00 41.09 ? 1442 HOH A O 1 HETATM 6444 O O . HOH U 10 . ? 29.078 24.320 40.135 1.00 51.79 ? 1443 HOH A O 1 HETATM 6445 O O . HOH U 10 . ? 23.539 75.233 62.679 1.00 55.28 ? 1444 HOH A O 1 HETATM 6446 O O . HOH U 10 . ? 0.314 63.752 61.411 1.00 37.87 ? 1445 HOH A O 1 HETATM 6447 O O . HOH U 10 . ? 29.217 60.799 50.236 1.00 47.25 ? 1446 HOH A O 1 HETATM 6448 O O . HOH U 10 . ? 11.314 49.718 19.490 1.00 56.67 ? 1447 HOH A O 1 HETATM 6449 O O . HOH U 10 . ? -7.550 41.873 41.116 1.00 33.00 ? 1448 HOH A O 1 HETATM 6450 O O . HOH U 10 . ? 23.411 78.489 22.892 1.00 47.55 ? 1449 HOH A O 1 HETATM 6451 O O . HOH U 10 . ? 20.733 57.148 20.830 1.00 49.35 ? 1450 HOH A O 1 HETATM 6452 O O . HOH U 10 . ? 15.608 86.223 35.349 1.00 43.31 ? 1451 HOH A O 1 HETATM 6453 O O . HOH U 10 . ? 10.918 53.488 21.864 1.00 54.31 ? 1452 HOH A O 1 HETATM 6454 O O . HOH U 10 . ? 29.745 35.234 64.908 1.00 56.12 ? 1453 HOH A O 1 HETATM 6455 O O . HOH U 10 . ? 16.813 42.636 44.696 1.00 20.46 ? 1454 HOH A O 1 HETATM 6456 O O . HOH U 10 . ? 41.542 39.083 20.747 1.00 60.15 ? 1455 HOH A O 1 HETATM 6457 O O . HOH U 10 . ? 21.813 50.870 11.031 1.00 58.83 ? 1456 HOH A O 1 HETATM 6458 O O . HOH U 10 . ? 6.653 25.417 20.742 1.00 65.35 ? 1457 HOH A O 1 HETATM 6459 O O . HOH U 10 . ? 16.991 57.617 72.985 1.00 48.74 ? 1458 HOH A O 1 HETATM 6460 O O . HOH U 10 . ? 14.801 60.401 77.121 1.00 48.97 ? 1459 HOH A O 1 HETATM 6461 O O . HOH U 10 . ? -1.725 46.733 71.925 1.00 59.01 ? 1460 HOH A O 1 HETATM 6462 O O . HOH U 10 . ? -4.387 43.083 66.737 1.00 52.94 ? 1461 HOH A O 1 HETATM 6463 O O . HOH U 10 . ? 29.300 61.382 56.387 1.00 45.02 ? 1462 HOH A O 1 HETATM 6464 O O . HOH U 10 . ? 35.124 60.878 62.313 1.00 43.13 ? 1463 HOH A O 1 HETATM 6465 O O . HOH U 10 . ? 24.205 61.121 51.343 1.00 49.29 ? 1464 HOH A O 1 HETATM 6466 O O . HOH U 10 . ? 26.850 63.156 52.490 1.00 53.53 ? 1465 HOH A O 1 HETATM 6467 O O . HOH U 10 . ? 24.827 63.518 42.293 1.00 46.77 ? 1466 HOH A O 1 HETATM 6468 O O . HOH U 10 . ? 32.653 53.251 37.230 1.00 62.86 ? 1467 HOH A O 1 HETATM 6469 O O . HOH U 10 . ? 23.859 53.760 71.815 1.00 68.87 ? 1468 HOH A O 1 HETATM 6470 O O . HOH U 10 . ? 12.144 23.176 43.898 1.00 51.35 ? 1469 HOH A O 1 HETATM 6471 O O . HOH U 10 . ? 0.283 31.718 41.098 1.00 46.52 ? 1470 HOH A O 1 HETATM 6472 O O . HOH U 10 . ? -4.220 29.700 52.971 1.00 62.34 ? 1471 HOH A O 1 HETATM 6473 O O . HOH U 10 . ? -2.123 46.510 62.768 1.00 41.62 ? 1472 HOH A O 1 HETATM 6474 O O . HOH U 10 . ? -4.844 45.912 57.772 1.00 37.48 ? 1473 HOH A O 1 HETATM 6475 O O . HOH U 10 . ? 27.922 30.803 6.710 1.00 57.60 ? 1474 HOH A O 1 HETATM 6476 O O . HOH U 10 . ? 17.674 25.511 21.216 1.00 54.90 ? 1475 HOH A O 1 HETATM 6477 O O . HOH U 10 . ? 18.423 22.666 49.064 1.00 55.77 ? 1476 HOH A O 1 HETATM 6478 O O . HOH U 10 . ? 17.389 17.763 44.763 1.00 62.61 ? 1477 HOH A O 1 HETATM 6479 O O . HOH U 10 . ? 7.802 35.193 18.718 1.00 63.66 ? 1478 HOH A O 1 HETATM 6480 O O . HOH U 10 . ? 31.320 57.300 31.390 1.00 52.72 ? 1479 HOH A O 1 HETATM 6481 O O . HOH U 10 . ? 8.641 50.661 25.412 1.00 50.62 ? 1480 HOH A O 1 HETATM 6482 O O . HOH U 10 . ? 0.484 58.075 35.540 1.00 46.48 ? 1481 HOH A O 1 HETATM 6483 O O . HOH U 10 . ? 42.842 53.191 25.182 1.00 57.64 ? 1482 HOH A O 1 HETATM 6484 O O . HOH U 10 . ? 35.410 42.303 40.172 1.00 53.70 ? 1483 HOH A O 1 HETATM 6485 O O . HOH U 10 . ? 40.522 62.617 57.739 1.00 74.57 ? 1484 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . LYS A 62 ? 1.0195 0.7800 0.5466 0.2399 -0.1067 0.0266 55 LYS A N 2 C CA . LYS A 62 ? 0.9874 0.7628 0.5345 0.2299 -0.1015 0.0209 55 LYS A CA 3 C C . LYS A 62 ? 0.9433 0.7349 0.5237 0.2166 -0.0900 0.0234 55 LYS A C 4 O O . LYS A 62 ? 0.9287 0.7260 0.5275 0.2132 -0.0919 0.0250 55 LYS A O 5 C CB . LYS A 62 ? 0.9868 0.7710 0.5455 0.2296 -0.1193 0.0084 55 LYS A CB 6 C CG . LYS A 62 ? 1.0370 0.8098 0.5673 0.2386 -0.1267 0.0033 55 LYS A CG 7 C CD . LYS A 62 ? 1.0479 0.8342 0.5989 0.2324 -0.1358 -0.0080 55 LYS A CD 8 C CE . LYS A 62 ? 1.0550 0.8317 0.5852 0.2422 -0.1524 -0.0166 55 LYS A CE 9 N NZ . LYS A 62 ? 1.0922 0.8545 0.5997 0.2542 -0.1642 -0.0149 55 LYS A NZ 10 N N . HIS A 63 ? 0.9126 0.7112 0.5003 0.2095 -0.0786 0.0233 56 HIS A N 11 C CA . HIS A 63 ? 0.8644 0.6792 0.4840 0.1969 -0.0699 0.0238 56 HIS A CA 12 C C . HIS A 63 ? 0.8251 0.6543 0.4649 0.1908 -0.0785 0.0135 56 HIS A C 13 O O . HIS A 63 ? 0.8366 0.6676 0.4728 0.1891 -0.0745 0.0109 56 HIS A O 14 C CB . HIS A 63 ? 0.8696 0.6827 0.4855 0.1928 -0.0507 0.0314 56 HIS A CB 15 C CG . HIS A 63 ? 0.9055 0.7059 0.5068 0.1969 -0.0404 0.0422 56 HIS A CG 16 N ND1 . HIS A 63 ? 0.9500 0.7376 0.5271 0.2019 -0.0278 0.0495 56 HIS A ND1 17 C CD2 . HIS A 63 ? 0.9071 0.7052 0.5150 0.1967 -0.0404 0.0471 56 HIS A CD2 18 C CE1 . HIS A 63 ? 0.9950 0.7726 0.5644 0.2043 -0.0203 0.0588 56 HIS A CE1 19 N NE2 . HIS A 63 ? 0.9775 0.7612 0.5654 0.2012 -0.0280 0.0574 56 HIS A NE2 20 N N . ASN A 64 ? 0.7638 0.6026 0.4245 0.1880 -0.0904 0.0079 57 ASN A N 21 C CA . ASN A 64 ? 0.7003 0.5523 0.3817 0.1825 -0.0997 -0.0017 57 ASN A CA 22 C C . ASN A 64 ? 0.6469 0.5134 0.3600 0.1739 -0.1003 -0.0029 57 ASN A C 23 O O . ASN A 64 ? 0.6139 0.4796 0.3315 0.1721 -0.0926 0.0035 57 ASN A O 24 C CB . ASN A 64 ? 0.7123 0.5585 0.3816 0.1910 -0.1175 -0.0095 57 ASN A CB 25 C CG . ASN A 64 ? 0.7186 0.5572 0.3802 0.1991 -0.1282 -0.0084 57 ASN A CG 26 O OD1 . ASN A 64 ? 0.6739 0.5154 0.3471 0.1969 -0.1246 -0.0037 57 ASN A OD1 27 N ND2 . ASN A 64 ? 0.7456 0.5737 0.3865 0.2093 -0.1419 -0.0130 57 ASN A ND2 28 N N . MET A 65 ? 0.6151 0.4942 0.3503 0.1686 -0.1088 -0.0110 58 MET A N 29 C CA . MET A 65 ? 0.5904 0.4831 0.3551 0.1601 -0.1071 -0.0116 58 MET A CA 30 C C . MET A 65 ? 0.5853 0.4750 0.3522 0.1651 -0.1138 -0.0099 58 MET A C 31 O O . MET A 65 ? 0.5528 0.4472 0.3335 0.1605 -0.1069 -0.0060 58 MET A O 32 C CB . MET A 65 ? 0.5728 0.4798 0.3623 0.1529 -0.1131 -0.0197 58 MET A CB 33 C CG . MET A 65 ? 0.5956 0.5154 0.4111 0.1430 -0.1048 -0.0180 58 MET A CG 34 S SD . MET A 65 ? 0.6629 0.5986 0.5090 0.1361 -0.1132 -0.0266 58 MET A SD 35 C CE . MET A 65 ? 0.5761 0.5134 0.4188 0.1323 -0.1110 -0.0300 58 MET A CE 36 N N . LYS A 66 ? 0.5873 0.4685 0.3398 0.1746 -0.1271 -0.0130 59 LYS A N 37 C CA . LYS A 66 ? 0.5997 0.4772 0.3532 0.1806 -0.1352 -0.0118 59 LYS A CA 38 C C . LYS A 66 ? 0.5940 0.4616 0.3346 0.1829 -0.1239 -0.0017 59 LYS A C 39 O O . LYS A 66 ? 0.5856 0.4561 0.3394 0.1818 -0.1235 0.0005 59 LYS A O 40 C CB . LYS A 66 ? 0.6245 0.4922 0.3601 0.1918 -0.1520 -0.0164 59 LYS A CB 41 C CG . LYS A 66 ? 0.6676 0.5332 0.4079 0.1979 -0.1622 -0.0162 59 LYS A CG 42 C CD . LYS A 66 ? 0.7688 0.6232 0.4888 0.2100 -0.1797 -0.0206 59 LYS A CD 43 C CE . LYS A 66 ? 0.8280 0.6736 0.5404 0.2192 -0.1874 -0.0169 59 LYS A CE 44 N NZ . LYS A 66 ? 0.8271 0.6864 0.5725 0.2137 -0.1885 -0.0182 59 LYS A NZ 45 N N . ALA A 67 ? 0.6038 0.4594 0.3193 0.1862 -0.1146 0.0043 60 ALA A N 46 C CA . ALA A 67 ? 0.6131 0.4593 0.3176 0.1873 -0.1020 0.0145 60 ALA A CA 47 C C . ALA A 67 ? 0.5774 0.4355 0.3078 0.1761 -0.0905 0.0168 60 ALA A C 48 O O . ALA A 67 ? 0.5664 0.4219 0.3018 0.1761 -0.0867 0.0218 60 ALA A O 49 C CB . ALA A 67 ? 0.6499 0.4833 0.3265 0.1913 -0.0922 0.0202 60 ALA A CB 50 N N . PHE A 68 ? 0.5457 0.4158 0.2913 0.1671 -0.0852 0.0132 61 PHE A N 51 C CA . PHE A 68 ? 0.5164 0.3982 0.2862 0.1565 -0.0754 0.0143 61 PHE A CA 52 C C . PHE A 68 ? 0.4958 0.3865 0.2885 0.1542 -0.0822 0.0109 61 PHE A C 53 O O . PHE A 68 ? 0.4870 0.3779 0.2886 0.1514 -0.0758 0.0151 61 PHE A O 54 C CB . PHE A 68 ? 0.4896 0.3827 0.2713 0.1482 -0.0710 0.0102 61 PHE A CB 55 C CG . PHE A 68 ? 0.4743 0.3807 0.2826 0.1378 -0.0648 0.0093 61 PHE A CG 56 C CD1 . PHE A 68 ? 0.4530 0.3584 0.2643 0.1332 -0.0520 0.0156 61 PHE A CD1 57 C CD2 . PHE A 68 ? 0.4621 0.3813 0.2925 0.1332 -0.0722 0.0021 61 PHE A CD2 58 C CE1 . PHE A 68 ? 0.4439 0.3606 0.2784 0.1243 -0.0472 0.0144 61 PHE A CE1 59 C CE2 . PHE A 68 ? 0.4168 0.3473 0.2699 0.1244 -0.0665 0.0014 61 PHE A CE2 60 C CZ . PHE A 68 ? 0.4195 0.3484 0.2736 0.1201 -0.0543 0.0073 61 PHE A CZ 61 N N . LEU A 69 ? 0.4807 0.3787 0.2838 0.1552 -0.0949 0.0030 62 LEU A N 62 C CA . LEU A 69 ? 0.4837 0.3912 0.3098 0.1533 -0.1018 -0.0011 62 LEU A CA 63 C C . LEU A 69 ? 0.5125 0.4112 0.3330 0.1606 -0.1055 0.0028 62 LEU A C 64 O O . LEU A 69 ? 0.5003 0.4044 0.3382 0.1573 -0.1027 0.0036 62 LEU A O 65 C CB . LEU A 69 ? 0.4897 0.4048 0.3256 0.1543 -0.1153 -0.0100 62 LEU A CB 66 C CG . LEU A 69 ? 0.4609 0.3864 0.3078 0.1463 -0.1127 -0.0148 62 LEU A CG 67 C CD1 . LEU A 69 ? 0.4938 0.4239 0.3479 0.1489 -0.1276 -0.0233 62 LEU A CD1 68 C CD2 . LEU A 69 ? 0.4822 0.4209 0.3543 0.1356 -0.1034 -0.0149 62 LEU A CD2 69 N N . ASP A 70 ? 0.5477 0.4321 0.3429 0.1709 -0.1116 0.0055 63 ASP A N 70 C CA . ASP A 70 ? 0.5827 0.4570 0.3700 0.1790 -0.1163 0.0096 63 ASP A CA 71 C C . ASP A 70 ? 0.5755 0.4433 0.3603 0.1768 -0.1028 0.0184 63 ASP A C 72 O O . ASP A 70 ? 0.5858 0.4497 0.3744 0.1804 -0.1051 0.0209 63 ASP A O 73 C CB . ASP A 70 ? 0.6196 0.4781 0.3768 0.1911 -0.1254 0.0112 63 ASP A CB 74 C CG . ASP A 70 ? 0.6617 0.5246 0.4226 0.1957 -0.1429 0.0021 63 ASP A CG 75 O OD1 . ASP A 70 ? 0.6574 0.5353 0.4460 0.1905 -0.1488 -0.0048 63 ASP A OD1 76 O OD2 . ASP A 70 ? 0.6980 0.5491 0.4335 0.2046 -0.1506 0.0017 63 ASP A OD2 77 N N . GLU A 71 ? 0.5649 0.4311 0.3437 0.1713 -0.0892 0.0230 64 GLU A N 78 C CA . GLU A 71 ? 0.5634 0.4235 0.3410 0.1685 -0.0760 0.0311 64 GLU A CA 79 C C . GLU A 71 ? 0.5301 0.4027 0.3367 0.1595 -0.0714 0.0290 64 GLU A C 80 O O . GLU A 71 ? 0.5267 0.3936 0.3354 0.1589 -0.0646 0.0345 64 GLU A O 81 C CB . GLU A 71 ? 0.5692 0.4243 0.3327 0.1655 -0.0633 0.0362 64 GLU A CB 82 C CG . GLU A 71 ? 0.5956 0.4443 0.3588 0.1620 -0.0489 0.0447 64 GLU A CG 83 C CD . GLU A 71 ? 0.6765 0.5083 0.4223 0.1707 -0.0490 0.0524 64 GLU A CD 84 O OE1 . GLU A 71 ? 0.6730 0.4935 0.3957 0.1806 -0.0560 0.0537 64 GLU A OE1 85 O OE2 . GLU A 71 ? 0.6690 0.4981 0.4238 0.1678 -0.0421 0.0569 64 GLU A OE2 86 N N . LEU A 72 ? 0.4973 0.3857 0.3250 0.1528 -0.0747 0.0213 65 LEU A N 87 C CA . LEU A 72 ? 0.4753 0.3758 0.3296 0.1452 -0.0717 0.0182 65 LEU A CA 88 C C . LEU A 72 ? 0.4830 0.3815 0.3452 0.1504 -0.0788 0.0176 65 LEU A C 89 O O . LEU A 72 ? 0.4733 0.3710 0.3332 0.1574 -0.0910 0.0142 65 LEU A O 90 C CB . LEU A 72 ? 0.4504 0.3669 0.3234 0.1385 -0.0751 0.0101 65 LEU A CB 91 C CG . LEU A 72 ? 0.4375 0.3574 0.3053 0.1334 -0.0699 0.0093 65 LEU A CG 92 C CD1 . LEU A 72 ? 0.4120 0.3456 0.2963 0.1293 -0.0767 0.0010 65 LEU A CD1 93 C CD2 . LEU A 72 ? 0.4057 0.3274 0.2788 0.1253 -0.0557 0.0135 65 LEU A CD2 94 N N . LYS A 73 ? 0.4735 0.3718 0.3465 0.1470 -0.0715 0.0204 66 LYS A N 95 C CA . LYS A 73 ? 0.4897 0.3854 0.3705 0.1521 -0.0772 0.0202 66 LYS A CA 96 C C . LYS A 73 ? 0.4591 0.3671 0.3664 0.1449 -0.0733 0.0159 66 LYS A C 97 O O . LYS A 73 ? 0.4474 0.3574 0.3599 0.1374 -0.0626 0.0176 66 LYS A O 98 C CB . LYS A 73 ? 0.5199 0.3984 0.3833 0.1577 -0.0723 0.0292 66 LYS A CB 99 C CG . LYS A 73 ? 0.5849 0.4488 0.4189 0.1661 -0.0751 0.0346 66 LYS A CG 100 C CD . LYS A 73 ? 0.6557 0.5181 0.4838 0.1756 -0.0909 0.0305 66 LYS A CD 101 C CE . LYS A 73 ? 0.7046 0.5488 0.5005 0.1862 -0.0945 0.0367 66 LYS A CE 102 N NZ . LYS A 73 ? 0.6789 0.5227 0.4596 0.1852 -0.0929 0.0359 66 LYS A NZ 103 N N . ALA A 74 ? 0.4529 0.3688 0.3764 0.1474 -0.0821 0.0102 67 ALA A N 104 C CA . ALA A 74 ? 0.4335 0.3601 0.3812 0.1420 -0.0788 0.0060 67 ALA A CA 105 C C . ALA A 74 ? 0.4437 0.3612 0.3901 0.1413 -0.0702 0.0113 67 ALA A C 106 O O . ALA A 74 ? 0.4244 0.3478 0.3835 0.1338 -0.0618 0.0098 67 ALA A O 107 C CB . ALA A 74 ? 0.4334 0.3674 0.3974 0.1473 -0.0903 0.0001 67 ALA A CB 108 N N . GLU A 75 ? 0.4667 0.3692 0.3969 0.1492 -0.0723 0.0175 68 GLU A N 109 C CA . GLU A 75 ? 0.4786 0.3707 0.4076 0.1496 -0.0650 0.0230 68 GLU A CA 110 C C . GLU A 75 ? 0.4592 0.3491 0.3844 0.1411 -0.0519 0.0267 68 GLU A C 111 O O . GLU A 75 ? 0.4426 0.3322 0.3781 0.1364 -0.0447 0.0270 68 GLU A O 112 C CB . GLU A 75 ? 0.5127 0.3874 0.4226 0.1602 -0.0698 0.0299 68 GLU A CB 113 C CG A GLU A 75 ? 0.5300 0.3930 0.4397 0.1607 -0.0625 0.0356 68 GLU A CG 114 C CG B GLU A 75 ? 0.5584 0.4209 0.4410 0.1627 -0.0667 0.0369 68 GLU A CG 115 C CD A GLU A 75 ? 0.5580 0.4293 0.4918 0.1580 -0.0621 0.0302 68 GLU A CD 116 C CD B GLU A 75 ? 0.6304 0.4799 0.4905 0.1747 -0.0766 0.0407 68 GLU A CD 117 O OE1 A GLU A 75 ? 0.5262 0.4037 0.4712 0.1630 -0.0716 0.0252 68 GLU A OE1 118 O OE1 B GLU A 75 ? 0.6425 0.4956 0.5070 0.1812 -0.0894 0.0361 68 GLU A OE1 119 O OE2 A GLU A 75 ? 0.5699 0.4412 0.5116 0.1509 -0.0521 0.0308 68 GLU A OE2 120 O OE2 B GLU A 75 ? 0.6496 0.4850 0.4869 0.1777 -0.0714 0.0485 68 GLU A OE2 121 N N . ASN A 76 ? 0.4561 0.3444 0.3670 0.1394 -0.0493 0.0291 69 ASN A N 122 C CA . ASN A 76 ? 0.4508 0.3390 0.3603 0.1312 -0.0376 0.0320 69 ASN A CA 123 C C . ASN A 76 ? 0.4225 0.3256 0.3519 0.1217 -0.0337 0.0256 69 ASN A C 124 O O . ASN A 76 ? 0.4170 0.3197 0.3530 0.1154 -0.0251 0.0267 69 ASN A O 125 C CB . ASN A 76 ? 0.4640 0.3484 0.3551 0.1319 -0.0358 0.0354 69 ASN A CB 126 C CG . ASN A 76 ? 0.5009 0.3676 0.3689 0.1402 -0.0352 0.0439 69 ASN A CG 127 O OD1 . ASN A 76 ? 0.5033 0.3595 0.3696 0.1428 -0.0322 0.0489 69 ASN A OD1 128 N ND2 . ASN A 76 ? 0.4940 0.3565 0.3437 0.1448 -0.0383 0.0455 69 ASN A ND2 129 N N . ILE A 77 ? 0.4021 0.3178 0.3407 0.1206 -0.0401 0.0188 70 ILE A N 130 C CA . ILE A 77 ? 0.3694 0.2989 0.3254 0.1119 -0.0365 0.0129 70 ILE A CA 131 C C . ILE A 77 ? 0.3657 0.2963 0.3367 0.1103 -0.0337 0.0108 70 ILE A C 132 O O . ILE A 77 ? 0.3556 0.2899 0.3347 0.1033 -0.0265 0.0093 70 ILE A O 133 C CB . ILE A 77 ? 0.3628 0.3044 0.3268 0.1120 -0.0443 0.0064 70 ILE A CB 134 C CG1 . ILE A 77 ? 0.3637 0.3036 0.3125 0.1132 -0.0466 0.0079 70 ILE A CG1 135 C CG2 . ILE A 77 ? 0.3279 0.2830 0.3099 0.1036 -0.0402 0.0006 70 ILE A CG2 136 C CD1 . ILE A 77 ? 0.3711 0.3196 0.3247 0.1156 -0.0568 0.0021 70 ILE A CD1 137 N N . LYS A 78 ? 0.3695 0.2958 0.3429 0.1175 -0.0397 0.0108 71 LYS A N 138 C CA . LYS A 78 ? 0.3736 0.2997 0.3607 0.1172 -0.0374 0.0087 71 LYS A CA 139 C C . LYS A 78 ? 0.3909 0.3064 0.3732 0.1139 -0.0282 0.0137 71 LYS A C 140 O O . LYS A 78 ? 0.3936 0.3127 0.3874 0.1083 -0.0225 0.0107 71 LYS A O 141 C CB . LYS A 78 ? 0.3826 0.3043 0.3711 0.1268 -0.0462 0.0088 71 LYS A CB 142 C CG . LYS A 78 ? 0.3894 0.3081 0.3899 0.1283 -0.0441 0.0076 71 LYS A CG 143 C CD . LYS A 78 ? 0.4229 0.3394 0.4270 0.1382 -0.0542 0.0068 71 LYS A CD 144 C CE . LYS A 78 ? 0.4462 0.3603 0.4635 0.1401 -0.0522 0.0050 71 LYS A CE 145 N NZ . LYS A 78 ? 0.4398 0.3495 0.4589 0.1507 -0.0623 0.0054 71 LYS A NZ 146 N N . LYS A 79 ? 0.4139 0.3160 0.3796 0.1178 -0.0268 0.0212 72 LYS A N 147 C CA . LYS A 79 ? 0.4310 0.3223 0.3923 0.1145 -0.0178 0.0268 72 LYS A CA 148 C C . LYS A 79 ? 0.3963 0.2945 0.3626 0.1046 -0.0100 0.0250 72 LYS A C 149 O O . LYS A 79 ? 0.3905 0.2867 0.3647 0.0996 -0.0039 0.0246 72 LYS A O 150 C CB . LYS A 79 ? 0.4438 0.3203 0.3848 0.1200 -0.0167 0.0357 72 LYS A CB 151 C CG . LYS A 79 ? 0.5515 0.4186 0.4855 0.1304 -0.0245 0.0383 72 LYS A CG 152 C CD . LYS A 79 ? 0.6052 0.4552 0.5178 0.1363 -0.0224 0.0479 72 LYS A CD 153 C CE . LYS A 79 ? 0.6923 0.5318 0.5995 0.1467 -0.0301 0.0505 72 LYS A CE 154 N NZ . LYS A 79 ? 0.7221 0.5458 0.6046 0.1540 -0.0302 0.0593 72 LYS A NZ 155 N N . PHE A 80 ? 0.3844 0.2901 0.3460 0.1021 -0.0107 0.0240 73 PHE A N 156 C CA . PHE A 80 ? 0.3680 0.2809 0.3345 0.0933 -0.0045 0.0221 73 PHE A CA 157 C C . PHE A 80 ? 0.3448 0.2687 0.3282 0.0879 -0.0041 0.0145 73 PHE A C 158 O O . PHE A 80 ? 0.3424 0.2675 0.3318 0.0814 0.0017 0.0133 73 PHE A O 159 C CB . PHE A 80 ? 0.3583 0.2771 0.3165 0.0924 -0.0060 0.0221 73 PHE A CB 160 C CG . PHE A 80 ? 0.3633 0.2712 0.3032 0.0975 -0.0053 0.0293 73 PHE A CG 161 C CD1 . PHE A 80 ? 0.3954 0.2899 0.3279 0.0989 0.0008 0.0365 73 PHE A CD1 162 C CD2 . PHE A 80 ? 0.3397 0.2505 0.2696 0.1006 -0.0099 0.0288 73 PHE A CD2 163 C CE1 . PHE A 80 ? 0.4421 0.3262 0.3564 0.1039 0.0025 0.0435 73 PHE A CE1 164 C CE2 . PHE A 80 ? 0.3718 0.2722 0.2830 0.1055 -0.0087 0.0352 73 PHE A CE2 165 C CZ . PHE A 80 ? 0.4019 0.2891 0.3049 0.1073 -0.0021 0.0427 73 PHE A CZ 166 N N . LEU A 81 ? 0.3442 0.2761 0.3350 0.0907 -0.0104 0.0093 74 LEU A N 167 C CA . LEU A 81 ? 0.3353 0.2772 0.3412 0.0860 -0.0090 0.0024 74 LEU A CA 168 C C . LEU A 81 ? 0.3378 0.2730 0.3500 0.0852 -0.0048 0.0021 74 LEU A C 169 O O . LEU A 81 ? 0.3344 0.2727 0.3531 0.0791 0.0000 -0.0010 74 LEU A O 170 C CB . LEU A 81 ? 0.3355 0.2866 0.3506 0.0897 -0.0157 -0.0026 74 LEU A CB 171 C CG . LEU A 81 ? 0.3073 0.2684 0.3371 0.0851 -0.0130 -0.0094 74 LEU A CG 172 C CD1 . LEU A 81 ? 0.2695 0.2380 0.2982 0.0773 -0.0090 -0.0110 74 LEU A CD1 173 C CD2 . LEU A 81 ? 0.3174 0.2872 0.3579 0.0890 -0.0189 -0.0138 74 LEU A CD2 174 N N . TYR A 82 ? 0.3424 0.2678 0.3522 0.0919 -0.0072 0.0053 75 TYR A N 175 C CA . TYR A 82 ? 0.3648 0.2821 0.3800 0.0916 -0.0035 0.0054 75 TYR A CA 176 C C . TYR A 82 ? 0.3714 0.2830 0.3835 0.0850 0.0038 0.0082 75 TYR A C 177 O O . TYR A 82 ? 0.3677 0.2798 0.3882 0.0801 0.0078 0.0044 75 TYR A O 178 C CB . TYR A 82 ? 0.3758 0.2810 0.3860 0.1002 -0.0071 0.0100 75 TYR A CB 179 C CG . TYR A 82 ? 0.4129 0.3089 0.4292 0.1000 -0.0032 0.0100 75 TYR A CG 180 C CD1 . TYR A 82 ? 0.3968 0.2969 0.4263 0.1015 -0.0045 0.0037 75 TYR A CD1 181 C CD2 . TYR A 82 ? 0.4564 0.3398 0.4665 0.0980 0.0023 0.0159 75 TYR A CD2 182 C CE1 . TYR A 82 ? 0.4388 0.3299 0.4739 0.1016 -0.0011 0.0031 75 TYR A CE1 183 C CE2 . TYR A 82 ? 0.4811 0.3553 0.4977 0.0974 0.0057 0.0155 75 TYR A CE2 184 C CZ . TYR A 82 ? 0.4809 0.3589 0.5095 0.0994 0.0036 0.0089 75 TYR A CZ 185 O OH . TYR A 82 ? 0.5441 0.4126 0.5789 0.0992 0.0067 0.0079 75 TYR A OH 186 N N . ASN A 83 ? 0.3802 0.2862 0.3807 0.0849 0.0057 0.0146 76 ASN A N 187 C CA . ASN A 83 ? 0.3758 0.2770 0.3748 0.0787 0.0127 0.0178 76 ASN A CA 188 C C . ASN A 83 ? 0.3606 0.2723 0.3673 0.0703 0.0155 0.0124 76 ASN A C 189 O O . ASN A 83 ? 0.3597 0.2680 0.3709 0.0649 0.0204 0.0124 76 ASN A O 190 C CB . ASN A 83 ? 0.4016 0.2971 0.3867 0.0806 0.0143 0.0253 76 ASN A CB 191 C CG . ASN A 83 ? 0.4172 0.3069 0.4019 0.0750 0.0221 0.0297 76 ASN A CG 192 O OD1 . ASN A 83 ? 0.4075 0.3045 0.3939 0.0692 0.0247 0.0283 76 ASN A OD1 193 N ND2 . ASN A 83 ? 0.4291 0.3055 0.4126 0.0766 0.0259 0.0349 76 ASN A ND2 194 N N . PHE A 84 ? 0.3285 0.2524 0.3366 0.0694 0.0121 0.0079 77 PHE A N 195 C CA . PHE A 84 ? 0.3173 0.2509 0.3300 0.0621 0.0143 0.0036 77 PHE A CA 196 C C . PHE A 84 ? 0.3212 0.2602 0.3445 0.0593 0.0145 -0.0036 77 PHE A C 197 O O . PHE A 84 ? 0.3151 0.2609 0.3415 0.0534 0.0163 -0.0075 77 PHE A O 198 C CB . PHE A 84 ? 0.2997 0.2433 0.3083 0.0623 0.0110 0.0027 77 PHE A CB 199 C CG . PHE A 84 ? 0.3141 0.2541 0.3114 0.0638 0.0116 0.0088 77 PHE A CG 200 C CD1 . PHE A 84 ? 0.3418 0.2709 0.3330 0.0642 0.0161 0.0153 77 PHE A CD1 201 C CD2 . PHE A 84 ? 0.2984 0.2454 0.2909 0.0651 0.0078 0.0081 77 PHE A CD2 202 C CE1 . PHE A 84 ? 0.3486 0.2743 0.3281 0.0663 0.0173 0.0210 77 PHE A CE1 203 C CE2 . PHE A 84 ? 0.3208 0.2643 0.3016 0.0671 0.0083 0.0131 77 PHE A CE2 204 C CZ . PHE A 84 ? 0.3406 0.2735 0.3144 0.0678 0.0134 0.0197 77 PHE A CZ 205 N N . THR A 85 ? 0.3253 0.2611 0.3535 0.0639 0.0127 -0.0057 78 THR A N 206 C CA . THR A 85 ? 0.3200 0.2619 0.3574 0.0627 0.0128 -0.0130 78 THR A CA 207 C C . THR A 85 ? 0.3236 0.2572 0.3668 0.0634 0.0150 -0.0153 78 THR A C 208 O O . THR A 85 ? 0.3091 0.2465 0.3593 0.0642 0.0150 -0.0212 78 THR A O 209 C CB . THR A 85 ? 0.3216 0.2712 0.3630 0.0678 0.0082 -0.0156 78 THR A CB 210 O OG1 . THR A 85 ? 0.2988 0.2410 0.3385 0.0750 0.0048 -0.0119 78 THR A OG1 211 C CG2 . THR A 85 ? 0.3112 0.2699 0.3484 0.0665 0.0057 -0.0148 78 THR A CG2 212 N N . GLN A 86 ? 0.3321 0.2542 0.3727 0.0628 0.0173 -0.0108 79 GLN A N 213 C CA . GLN A 86 ? 0.3713 0.2838 0.4174 0.0636 0.0192 -0.0127 79 GLN A CA 214 C C . GLN A 86 ? 0.3710 0.2843 0.4218 0.0570 0.0222 -0.0185 79 GLN A C 215 O O . GLN A 86 ? 0.3638 0.2720 0.4201 0.0577 0.0231 -0.0228 79 GLN A O 216 C CB . GLN A 86 ? 0.3878 0.2861 0.4296 0.0658 0.0207 -0.0051 79 GLN A CB 217 C CG . GLN A 86 ? 0.4366 0.3317 0.4721 0.0737 0.0170 0.0002 79 GLN A CG 218 C CD . GLN A 86 ? 0.4835 0.3835 0.5252 0.0794 0.0128 -0.0045 79 GLN A CD 219 O OE1 . GLN A 86 ? 0.5458 0.4395 0.5936 0.0818 0.0132 -0.0070 79 GLN A OE1 220 N NE2 . GLN A 86 ? 0.4643 0.3757 0.5056 0.0813 0.0088 -0.0064 79 GLN A NE2 221 N N . ILE A 87 ? 0.3506 0.2696 0.3990 0.0510 0.0234 -0.0186 80 ILE A N 222 C CA . ILE A 87 ? 0.3681 0.2880 0.4200 0.0447 0.0253 -0.0242 80 ILE A CA 223 C C . ILE A 87 ? 0.3317 0.2639 0.3808 0.0411 0.0245 -0.0266 80 ILE A C 224 O O . ILE A 87 ? 0.3310 0.2688 0.3759 0.0425 0.0232 -0.0228 80 ILE A O 225 C CB . ILE A 87 ? 0.3871 0.2984 0.4404 0.0401 0.0277 -0.0206 80 ILE A CB 226 C CG1 . ILE A 87 ? 0.3913 0.3065 0.4398 0.0378 0.0285 -0.0144 80 ILE A CG1 227 C CG2 . ILE A 87 ? 0.4262 0.3238 0.4819 0.0437 0.0290 -0.0170 80 ILE A CG2 228 C CD1 . ILE A 87 ? 0.4177 0.3263 0.4698 0.0326 0.0316 -0.0110 80 ILE A CD1 229 N N . PRO A 88 ? 0.3289 0.2645 0.3795 0.0369 0.0250 -0.0331 81 PRO A N 230 C CA . PRO A 88 ? 0.3142 0.2605 0.3613 0.0336 0.0243 -0.0349 81 PRO A CA 231 C C . PRO A 88 ? 0.3110 0.2587 0.3556 0.0297 0.0243 -0.0300 81 PRO A C 232 O O . PRO A 88 ? 0.3046 0.2452 0.3517 0.0274 0.0256 -0.0274 81 PRO A O 233 C CB . PRO A 88 ? 0.3137 0.2602 0.3616 0.0303 0.0248 -0.0425 81 PRO A CB 234 C CG . PRO A 88 ? 0.3454 0.2840 0.3975 0.0342 0.0258 -0.0459 81 PRO A CG 235 C CD . PRO A 88 ? 0.3306 0.2603 0.3851 0.0359 0.0259 -0.0395 81 PRO A CD 236 N N . HIS A 89 ? 0.2827 0.2395 0.3234 0.0290 0.0233 -0.0289 82 HIS A N 237 C CA . HIS A 89 ? 0.2851 0.2444 0.3236 0.0255 0.0234 -0.0250 82 HIS A CA 238 C C . HIS A 89 ? 0.2645 0.2325 0.3009 0.0216 0.0223 -0.0286 82 HIS A C 239 O O . HIS A 89 ? 0.2572 0.2319 0.2900 0.0215 0.0215 -0.0263 82 HIS A O 240 C CB . HIS A 89 ? 0.2718 0.2317 0.3060 0.0292 0.0231 -0.0184 82 HIS A CB 241 C CG . HIS A 89 ? 0.2909 0.2411 0.3252 0.0330 0.0243 -0.0138 82 HIS A CG 242 N ND1 . HIS A 89 ? 0.2853 0.2334 0.3184 0.0390 0.0226 -0.0131 82 HIS A ND1 243 C CD2 . HIS A 89 ? 0.2728 0.2142 0.3085 0.0319 0.0270 -0.0095 82 HIS A CD2 244 C CE1 . HIS A 89 ? 0.2902 0.2281 0.3226 0.0417 0.0240 -0.0083 82 HIS A CE1 245 N NE2 . HIS A 89 ? 0.2855 0.2189 0.3194 0.0373 0.0271 -0.0059 82 HIS A NE2 246 N N . LEU A 90 ? 0.2556 0.2226 0.2934 0.0186 0.0221 -0.0343 83 LEU A N 247 C CA . LEU A 90 ? 0.2661 0.2398 0.3005 0.0156 0.0209 -0.0382 83 LEU A CA 248 C C . LEU A 90 ? 0.2651 0.2414 0.2995 0.0117 0.0199 -0.0353 83 LEU A C 249 O O . LEU A 90 ? 0.2531 0.2246 0.2922 0.0096 0.0204 -0.0333 83 LEU A O 250 C CB . LEU A 90 ? 0.2650 0.2349 0.2994 0.0141 0.0206 -0.0453 83 LEU A CB 251 C CG . LEU A 90 ? 0.2793 0.2543 0.3079 0.0115 0.0193 -0.0498 83 LEU A CG 252 C CD1 . LEU A 90 ? 0.2443 0.2260 0.2691 0.0142 0.0208 -0.0498 83 LEU A CD1 253 C CD2 . LEU A 90 ? 0.2525 0.2210 0.2798 0.0107 0.0187 -0.0575 83 LEU A CD2 254 N N . ALA A 91 ? 0.2554 0.2393 0.2856 0.0108 0.0188 -0.0349 84 ALA A N 255 C CA . ALA A 91 ? 0.2396 0.2266 0.2705 0.0073 0.0177 -0.0324 84 ALA A CA 256 C C . ALA A 91 ? 0.2562 0.2398 0.2913 0.0032 0.0163 -0.0358 84 ALA A C 257 O O . ALA A 91 ? 0.2578 0.2395 0.2912 0.0023 0.0148 -0.0417 84 ALA A O 258 C CB . ALA A 91 ? 0.2228 0.2174 0.2483 0.0067 0.0163 -0.0328 84 ALA A CB 259 N N . GLY A 92 ? 0.2515 0.2345 0.2923 0.0008 0.0166 -0.0323 85 GLY A N 260 C CA . GLY A 92 ? 0.2817 0.2623 0.3294 -0.0035 0.0146 -0.0352 85 GLY A CA 261 C C . GLY A 92 ? 0.3033 0.2752 0.3576 -0.0042 0.0155 -0.0369 85 GLY A C 262 O O . GLY A 92 ? 0.3378 0.3072 0.3993 -0.0079 0.0134 -0.0399 85 GLY A O 263 N N . THR A 93 ? 0.3021 0.2690 0.3549 -0.0005 0.0182 -0.0351 86 THR A N 264 C CA . THR A 93 ? 0.3060 0.2636 0.3652 -0.0009 0.0194 -0.0362 86 THR A CA 265 C C . THR A 93 ? 0.3112 0.2640 0.3764 -0.0007 0.0233 -0.0289 86 THR A C 266 O O . THR A 93 ? 0.3046 0.2604 0.3665 0.0012 0.0256 -0.0228 86 THR A O 267 C CB . THR A 93 ? 0.3086 0.2618 0.3635 0.0032 0.0199 -0.0396 86 THR A CB 268 O OG1 . THR A 93 ? 0.2965 0.2509 0.3473 0.0079 0.0221 -0.0345 86 THR A OG1 269 C CG2 . THR A 93 ? 0.3118 0.2689 0.3598 0.0035 0.0173 -0.0467 86 THR A CG2 270 N N . GLU A 94 ? 0.3322 0.2765 0.4059 -0.0028 0.0243 -0.0295 87 GLU A N 271 C CA . GLU A 94 ? 0.3424 0.2808 0.4220 -0.0029 0.0289 -0.0222 87 GLU A CA 272 C C . GLU A 94 ? 0.3355 0.2706 0.4070 0.0031 0.0320 -0.0161 87 GLU A C 273 O O . GLU A 94 ? 0.3224 0.2565 0.3925 0.0045 0.0358 -0.0087 87 GLU A O 274 C CB . GLU A 94 ? 0.3604 0.2890 0.4506 -0.0058 0.0293 -0.0245 87 GLU A CB 275 C CG . GLU A 94 ? 0.4486 0.3691 0.5453 -0.0061 0.0350 -0.0165 87 GLU A CG 276 C CD . GLU A 94 ? 0.5767 0.5018 0.6804 -0.0097 0.0381 -0.0113 87 GLU A CD 277 O OE1 . GLU A 94 ? 0.6293 0.5488 0.7352 -0.0088 0.0441 -0.0033 87 GLU A OE1 278 O OE2 . GLU A 94 ? 0.6043 0.5384 0.7112 -0.0132 0.0349 -0.0148 87 GLU A OE2 279 N N . GLN A 95 ? 0.3277 0.2604 0.3943 0.0070 0.0304 -0.0195 88 GLN A N 280 C CA . GLN A 95 ? 0.3474 0.2772 0.4073 0.0132 0.0320 -0.0148 88 GLN A CA 281 C C . GLN A 95 ? 0.3274 0.2655 0.3794 0.0155 0.0318 -0.0109 88 GLN A C 282 O O . GLN A 95 ? 0.3053 0.2403 0.3522 0.0197 0.0336 -0.0048 88 GLN A O 283 C CB . GLN A 95 ? 0.3593 0.2875 0.4169 0.0168 0.0298 -0.0201 88 GLN A CB 284 C CG . GLN A 95 ? 0.4255 0.3438 0.4901 0.0155 0.0300 -0.0241 88 GLN A CG 285 C CD . GLN A 95 ? 0.5165 0.4369 0.5856 0.0100 0.0274 -0.0320 88 GLN A CD 286 O OE1 . GLN A 95 ? 0.4382 0.3675 0.5043 0.0076 0.0252 -0.0349 88 GLN A OE1 287 N NE2 . GLN A 95 ? 0.5891 0.5001 0.6649 0.0085 0.0272 -0.0357 88 GLN A NE2 288 N N . ASN A 96 ? 0.3061 0.2539 0.3561 0.0133 0.0293 -0.0146 89 ASN A N 289 C CA . ASN A 96 ? 0.3086 0.2635 0.3516 0.0154 0.0290 -0.0112 89 ASN A CA 290 C C . ASN A 96 ? 0.3115 0.2668 0.3559 0.0134 0.0320 -0.0053 89 ASN A C 291 O O . ASN A 96 ? 0.3098 0.2673 0.3475 0.0163 0.0329 -0.0008 89 ASN A O 292 C CB . ASN A 96 ? 0.2946 0.2592 0.3348 0.0139 0.0257 -0.0164 89 ASN A CB 293 C CG . ASN A 96 ? 0.3220 0.2929 0.3551 0.0172 0.0248 -0.0136 89 ASN A CG 294 O OD1 . ASN A 96 ? 0.2829 0.2509 0.3122 0.0219 0.0251 -0.0103 89 ASN A OD1 295 N ND2 . ASN A 96 ? 0.3075 0.2862 0.3387 0.0149 0.0232 -0.0153 89 ASN A ND2 296 N N . PHE A 97 ? 0.3029 0.2564 0.3561 0.0084 0.0334 -0.0059 90 PHE A N 297 C CA . PHE A 97 ? 0.2969 0.2501 0.3541 0.0064 0.0375 -0.0001 90 PHE A CA 298 C C . PHE A 97 ? 0.3209 0.2641 0.3755 0.0100 0.0423 0.0069 90 PHE A C 299 O O . PHE A 97 ? 0.2902 0.2331 0.3394 0.0124 0.0458 0.0131 90 PHE A O 300 C CB . PHE A 97 ? 0.3027 0.2563 0.3727 0.0000 0.0374 -0.0030 90 PHE A CB 301 C CG . PHE A 97 ? 0.3381 0.2904 0.4157 -0.0023 0.0428 0.0031 90 PHE A CG 302 C CD1 . PHE A 97 ? 0.3403 0.2985 0.4141 -0.0012 0.0451 0.0074 90 PHE A CD1 303 C CD2 . PHE A 97 ? 0.4433 0.3878 0.5322 -0.0054 0.0461 0.0047 90 PHE A CD2 304 C CE1 . PHE A 97 ? 0.3733 0.3307 0.4549 -0.0033 0.0510 0.0129 90 PHE A CE1 305 C CE2 . PHE A 97 ? 0.4823 0.4258 0.5800 -0.0078 0.0523 0.0108 90 PHE A CE2 306 C CZ . PHE A 97 ? 0.4359 0.3863 0.5297 -0.0066 0.0549 0.0149 90 PHE A CZ 307 N N . GLN A 98 ? 0.3141 0.2487 0.3710 0.0111 0.0425 0.0061 91 GLN A N 308 C CA . GLN A 98 ? 0.3529 0.2768 0.4058 0.0153 0.0468 0.0133 91 GLN A CA 309 C C . GLN A 98 ? 0.3413 0.2657 0.3805 0.0222 0.0458 0.0169 91 GLN A C 310 O O . GLN A 98 ? 0.3597 0.2783 0.3925 0.0255 0.0498 0.0243 91 GLN A O 311 C CB . GLN A 98 ? 0.3633 0.2772 0.4214 0.0156 0.0467 0.0115 91 GLN A CB 312 C CG . GLN A 98 ? 0.4285 0.3389 0.5010 0.0089 0.0483 0.0092 91 GLN A CG 313 C CD . GLN A 98 ? 0.5685 0.4767 0.6475 0.0056 0.0546 0.0161 91 GLN A CD 314 O OE1 . GLN A 98 ? 0.6367 0.5394 0.7091 0.0093 0.0598 0.0243 91 GLN A OE1 315 N NE2 . GLN A 98 ? 0.5786 0.4907 0.6708 -0.0009 0.0543 0.0127 91 GLN A NE2 316 N N . LEU A 99 ? 0.3202 0.2508 0.3550 0.0246 0.0405 0.0117 92 LEU A N 317 C CA . LEU A 99 ? 0.3163 0.2484 0.3397 0.0309 0.0383 0.0141 92 LEU A CA 318 C C . LEU A 99 ? 0.3093 0.2466 0.3267 0.0309 0.0398 0.0178 92 LEU A C 319 O O . LEU A 99 ? 0.3165 0.2497 0.3242 0.0358 0.0410 0.0232 92 LEU A O 320 C CB . LEU A 99 ? 0.2927 0.2321 0.3155 0.0324 0.0327 0.0074 92 LEU A CB 321 C CG . LEU A 99 ? 0.3202 0.2608 0.3340 0.0390 0.0293 0.0089 92 LEU A CG 322 C CD1 . LEU A 99 ? 0.3208 0.2501 0.3293 0.0451 0.0301 0.0144 92 LEU A CD1 323 C CD2 . LEU A 99 ? 0.2783 0.2265 0.2948 0.0397 0.0248 0.0022 92 LEU A CD2 324 N N . ALA A 100 ? 0.2937 0.2396 0.3164 0.0257 0.0396 0.0146 93 ALA A N 325 C CA . ALA A 100 ? 0.2985 0.2490 0.3172 0.0254 0.0416 0.0180 93 ALA A CA 326 C C . ALA A 100 ? 0.3153 0.2579 0.3319 0.0266 0.0484 0.0258 93 ALA A C 327 O O . ALA A 100 ? 0.3250 0.2664 0.3312 0.0308 0.0502 0.0305 93 ALA A O 328 C CB . ALA A 100 ? 0.2776 0.2371 0.3047 0.0193 0.0406 0.0136 93 ALA A CB 329 N N . LYS A 101 ? 0.3310 0.2677 0.3571 0.0232 0.0524 0.0275 94 LYS A N 330 C CA . LYS A 101 ? 0.3363 0.2646 0.3612 0.0241 0.0602 0.0357 94 LYS A CA 331 C C . LYS A 101 ? 0.3473 0.2653 0.3582 0.0316 0.0611 0.0413 94 LYS A C 332 O O . LYS A 101 ? 0.3371 0.2500 0.3389 0.0351 0.0662 0.0481 94 LYS A O 333 C CB . LYS A 101 ? 0.3448 0.2682 0.3846 0.0186 0.0638 0.0359 94 LYS A CB 334 C CG . LYS A 101 ? 0.3981 0.3307 0.4519 0.0115 0.0635 0.0317 94 LYS A CG 335 C CD . LYS A 101 ? 0.5439 0.4711 0.6136 0.0060 0.0663 0.0313 94 LYS A CD 336 C CE . LYS A 101 ? 0.6325 0.5523 0.7062 0.0055 0.0759 0.0402 94 LYS A CE 337 N NZ . LYS A 101 ? 0.6842 0.5943 0.7709 0.0017 0.0791 0.0413 94 LYS A NZ 338 N N . GLN A 102 ? 0.3553 0.2701 0.3642 0.0345 0.0561 0.0382 95 GLN A N 339 C CA . GLN A 102 ? 0.3666 0.2717 0.3623 0.0422 0.0554 0.0428 95 GLN A CA 340 C C . GLN A 102 ? 0.3752 0.2846 0.3570 0.0475 0.0523 0.0437 95 GLN A C 341 O O . GLN A 102 ? 0.3611 0.2629 0.3300 0.0530 0.0547 0.0500 95 GLN A O 342 C CB . GLN A 102 ? 0.3716 0.2746 0.3699 0.0444 0.0497 0.0382 95 GLN A CB 343 C CG . GLN A 102 ? 0.3945 0.2894 0.3794 0.0530 0.0472 0.0423 95 GLN A CG 344 C CD . GLN A 102 ? 0.3912 0.2868 0.3787 0.0560 0.0406 0.0370 95 GLN A CD 345 O OE1 . GLN A 102 ? 0.3918 0.2874 0.3904 0.0525 0.0403 0.0326 95 GLN A OE1 346 N NE2 . GLN A 102 ? 0.3832 0.2794 0.3609 0.0628 0.0352 0.0370 95 GLN A NE2 347 N N . ILE A 103 ? 0.3617 0.2827 0.3458 0.0457 0.0470 0.0373 96 ILE A N 348 C CA . ILE A 103 ? 0.3758 0.3011 0.3483 0.0502 0.0432 0.0371 96 ILE A CA 349 C C . ILE A 103 ? 0.3704 0.2948 0.3366 0.0503 0.0491 0.0423 96 ILE A C 350 O O . ILE A 103 ? 0.3717 0.2916 0.3235 0.0562 0.0493 0.0462 96 ILE A O 351 C CB . ILE A 103 ? 0.3622 0.3004 0.3405 0.0471 0.0372 0.0292 96 ILE A CB 352 C CG1 . ILE A 103 ? 0.4016 0.3416 0.3866 0.0470 0.0324 0.0237 96 ILE A CG1 353 C CG2 . ILE A 103 ? 0.3584 0.3009 0.3259 0.0512 0.0334 0.0289 96 ILE A CG2 354 C CD1 . ILE A 103 ? 0.4071 0.3427 0.3850 0.0539 0.0278 0.0242 96 ILE A CD1 355 N N . GLN A 104 ? 0.3625 0.2912 0.3396 0.0439 0.0539 0.0421 97 GLN A N 356 C CA . GLN A 104 ? 0.3540 0.2823 0.3276 0.0438 0.0606 0.0471 97 GLN A CA 357 C C . GLN A 104 ? 0.3849 0.2998 0.3475 0.0489 0.0671 0.0557 97 GLN A C 358 O O . GLN A 104 ? 0.3890 0.3008 0.3377 0.0539 0.0696 0.0598 97 GLN A O 359 C CB . GLN A 104 ? 0.3453 0.2798 0.3357 0.0359 0.0646 0.0456 97 GLN A CB 360 C CG . GLN A 104 ? 0.3504 0.2846 0.3404 0.0354 0.0728 0.0511 97 GLN A CG 361 C CD . GLN A 104 ? 0.3780 0.3178 0.3873 0.0277 0.0768 0.0500 97 GLN A CD 362 O OE1 . GLN A 104 ? 0.3760 0.3148 0.3977 0.0231 0.0758 0.0476 97 GLN A OE1 363 N NE2 . GLN A 104 ? 0.3691 0.3144 0.3811 0.0265 0.0811 0.0516 97 GLN A NE2 364 N N . SER A 105 ? 0.3802 0.2866 0.3480 0.0480 0.0700 0.0585 98 SER A N 365 C CA . SER A 105 ? 0.4048 0.2970 0.3617 0.0529 0.0766 0.0674 98 SER A CA 366 C C . SER A 105 ? 0.4087 0.2941 0.3447 0.0623 0.0719 0.0695 98 SER A C 367 O O . SER A 105 ? 0.4157 0.2932 0.3366 0.0675 0.0769 0.0761 98 SER A O 368 C CB . SER A 105 ? 0.3983 0.2818 0.3650 0.0504 0.0792 0.0694 98 SER A CB 369 O OG A SER A 105 ? 0.4120 0.2813 0.3682 0.0549 0.0865 0.0787 98 SER A OG 370 O OG B SER A 105 ? 0.4412 0.3266 0.4235 0.0433 0.0865 0.0708 98 SER A OG 371 N N . GLN A 106 ? 0.3927 0.2814 0.3282 0.0645 0.0624 0.0638 99 GLN A N 372 C CA . GLN A 106 ? 0.4144 0.2971 0.3325 0.0734 0.0564 0.0650 99 GLN A CA 373 C C . GLN A 106 ? 0.4108 0.2983 0.3165 0.0769 0.0538 0.0638 99 GLN A C 374 O O . GLN A 106 ? 0.4384 0.3173 0.3258 0.0844 0.0534 0.0682 99 GLN A O 375 C CB . GLN A 106 ? 0.3924 0.2788 0.3165 0.0744 0.0471 0.0586 99 GLN A CB 376 C CG . GLN A 106 ? 0.4479 0.3266 0.3807 0.0730 0.0492 0.0602 99 GLN A CG 377 C CD . GLN A 106 ? 0.4746 0.3565 0.4128 0.0750 0.0404 0.0540 99 GLN A CD 378 O OE1 . GLN A 106 ? 0.4394 0.3329 0.3885 0.0708 0.0364 0.0466 99 GLN A OE1 379 N NE2 . GLN A 106 ? 0.5259 0.3973 0.4562 0.0819 0.0377 0.0573 99 GLN A NE2 380 N N . TRP A 107 ? 0.3886 0.2893 0.3034 0.0719 0.0512 0.0577 100 TRP A N 381 C CA . TRP A 107 ? 0.3947 0.2997 0.2991 0.0745 0.0498 0.0567 100 TRP A CA 382 C C . TRP A 107 ? 0.4118 0.3091 0.3046 0.0772 0.0592 0.0641 100 TRP A C 383 O O . TRP A 107 ? 0.4198 0.3129 0.2952 0.0837 0.0576 0.0656 100 TRP A O 384 C CB . TRP A 107 ? 0.3625 0.2821 0.2800 0.0680 0.0471 0.0498 100 TRP A CB 385 C CG . TRP A 107 ? 0.3455 0.2724 0.2688 0.0675 0.0376 0.0426 100 TRP A CG 386 C CD1 . TRP A 107 ? 0.3594 0.2825 0.2812 0.0714 0.0317 0.0413 100 TRP A CD1 387 C CD2 . TRP A 107 ? 0.3222 0.2616 0.2556 0.0626 0.0335 0.0359 100 TRP A CD2 388 N NE1 . TRP A 107 ? 0.3309 0.2639 0.2616 0.0691 0.0247 0.0341 100 TRP A NE1 389 C CE2 . TRP A 107 ? 0.3228 0.2656 0.2602 0.0636 0.0258 0.0309 100 TRP A CE2 390 C CE3 . TRP A 107 ? 0.3104 0.2583 0.2496 0.0577 0.0356 0.0338 100 TRP A CE3 391 C CZ2 . TRP A 107 ? 0.3237 0.2775 0.2702 0.0598 0.0210 0.0242 100 TRP A CZ2 392 C CZ3 . TRP A 107 ? 0.2967 0.2550 0.2441 0.0541 0.0301 0.0273 100 TRP A CZ3 393 C CH2 . TRP A 107 ? 0.3332 0.2943 0.2839 0.0551 0.0232 0.0226 100 TRP A CH2 394 N N . LYS A 108 ? 0.4271 0.3221 0.3294 0.0724 0.0688 0.0686 101 LYS A N 395 C CA . LYS A 108 ? 0.4720 0.3585 0.3644 0.0749 0.0796 0.0768 101 LYS A CA 396 C C . LYS A 108 ? 0.4880 0.3586 0.3597 0.0837 0.0805 0.0835 101 LYS A C 397 O O . LYS A 108 ? 0.4933 0.3579 0.3456 0.0905 0.0824 0.0869 101 LYS A O 398 C CB . LYS A 108 ? 0.4785 0.3650 0.3878 0.0678 0.0898 0.0806 101 LYS A CB 399 C CG . LYS A 108 ? 0.5473 0.4476 0.4739 0.0604 0.0910 0.0759 101 LYS A CG 400 C CD . LYS A 108 ? 0.6454 0.5465 0.5920 0.0528 0.0991 0.0784 101 LYS A CD 401 C CE . LYS A 108 ? 0.6733 0.5885 0.6362 0.0463 0.0994 0.0736 101 LYS A CE 402 N NZ . LYS A 108 ? 0.7248 0.6418 0.7091 0.0387 0.1058 0.0750 101 LYS A NZ 403 N N . GLU A 109 ? 0.4816 0.3453 0.3568 0.0841 0.0788 0.0850 102 GLU A N 404 C CA A GLU A 109 ? 0.5100 0.3583 0.3670 0.0925 0.0780 0.0910 102 GLU A CA 405 C CA B GLU A 109 ? 0.5125 0.3605 0.3682 0.0927 0.0789 0.0915 102 GLU A CA 406 C C . GLU A 109 ? 0.5124 0.3600 0.3501 0.1009 0.0683 0.0881 102 GLU A C 407 O O . GLU A 109 ? 0.5190 0.3544 0.3341 0.1093 0.0697 0.0937 102 GLU A O 408 C CB A GLU A 109 ? 0.5166 0.3617 0.3841 0.0912 0.0734 0.0896 102 GLU A CB 409 C CB B GLU A 109 ? 0.5215 0.3625 0.3852 0.0918 0.0780 0.0932 102 GLU A CB 410 C CG A GLU A 109 ? 0.5380 0.3801 0.4232 0.0840 0.0818 0.0928 102 GLU A CG 411 C CG B GLU A 109 ? 0.5945 0.4167 0.4404 0.0993 0.0826 0.1028 102 GLU A CG 412 C CD A GLU A 109 ? 0.5598 0.4023 0.4583 0.0818 0.0754 0.0883 102 GLU A CD 413 C CD B GLU A 109 ? 0.6636 0.4790 0.4906 0.1092 0.0721 0.1021 102 GLU A CD 414 O OE1 A GLU A 109 ? 0.5399 0.3774 0.4295 0.0882 0.0676 0.0873 102 GLU A OE1 415 O OE1 B GLU A 109 ? 0.7092 0.5086 0.5166 0.1169 0.0751 0.1101 102 GLU A OE1 416 O OE2 A GLU A 109 ? 0.5374 0.3853 0.4557 0.0737 0.0779 0.0853 102 GLU A OE2 417 O OE2 B GLU A 109 ? 0.6724 0.4978 0.5040 0.1096 0.0608 0.0937 102 GLU A OE2 418 N N . PHE A 110 ? 0.4762 0.3363 0.3226 0.0987 0.0581 0.0791 103 PHE A N 419 C CA . PHE A 110 ? 0.4839 0.3447 0.3160 0.1058 0.0473 0.0749 103 PHE A CA 420 C C . PHE A 110 ? 0.4956 0.3548 0.3108 0.1099 0.0499 0.0763 103 PHE A C 421 O O . PHE A 110 ? 0.5225 0.3786 0.3216 0.1171 0.0420 0.0742 103 PHE A O 422 C CB . PHE A 110 ? 0.4541 0.3295 0.3012 0.1019 0.0369 0.0649 103 PHE A CB 423 C CG . PHE A 110 ? 0.4695 0.3463 0.3300 0.1002 0.0319 0.0621 103 PHE A CG 424 C CD1 . PHE A 110 ? 0.4943 0.3586 0.3499 0.1042 0.0335 0.0676 103 PHE A CD1 425 C CD2 . PHE A 110 ? 0.4289 0.3191 0.3061 0.0950 0.0258 0.0539 103 PHE A CD2 426 C CE1 . PHE A 110 ? 0.5274 0.3930 0.3959 0.1029 0.0289 0.0645 103 PHE A CE1 427 C CE2 . PHE A 110 ? 0.4347 0.3265 0.3246 0.0936 0.0217 0.0508 103 PHE A CE2 428 C CZ . PHE A 110 ? 0.4786 0.3584 0.3644 0.0976 0.0232 0.0559 103 PHE A CZ 429 N N . GLY A 111 ? 0.4891 0.3509 0.3088 0.1053 0.0605 0.0792 104 GLY A N 430 C CA . GLY A 111 ? 0.4841 0.3439 0.2884 0.1092 0.0647 0.0809 104 GLY A CA 431 C C . GLY A 111 ? 0.4749 0.3484 0.2899 0.1038 0.0649 0.0752 104 GLY A C 432 O O . GLY A 111 ? 0.4931 0.3647 0.2953 0.1075 0.0684 0.0763 104 GLY A O 433 N N . LEU A 112 ? 0.4351 0.3218 0.2725 0.0956 0.0616 0.0693 105 LEU A N 434 C CA . LEU A 112 ? 0.4048 0.3039 0.2517 0.0908 0.0617 0.0643 105 LEU A CA 435 C C . LEU A 112 ? 0.4264 0.3245 0.2751 0.0887 0.0746 0.0697 105 LEU A C 436 O O . LEU A 112 ? 0.4448 0.3366 0.2972 0.0872 0.0837 0.0762 105 LEU A O 437 C CB . LEU A 112 ? 0.3826 0.2948 0.2522 0.0824 0.0566 0.0577 105 LEU A CB 438 C CG . LEU A 112 ? 0.3735 0.2887 0.2438 0.0840 0.0445 0.0517 105 LEU A CG 439 C CD1 . LEU A 112 ? 0.3272 0.2560 0.2181 0.0759 0.0406 0.0450 105 LEU A CD1 440 C CD2 . LEU A 112 ? 0.3828 0.2962 0.2366 0.0910 0.0369 0.0488 105 LEU A CD2 441 N N . ASP A 113 ? 0.4200 0.3241 0.2672 0.0887 0.0759 0.0673 106 ASP A N 442 C CA . ASP A 113 ? 0.4510 0.3553 0.3011 0.0871 0.0882 0.0720 106 ASP A CA 443 C C . ASP A 113 ? 0.4429 0.3559 0.3185 0.0777 0.0938 0.0722 106 ASP A C 444 O O . ASP A 113 ? 0.4503 0.3598 0.3307 0.0762 0.1054 0.0785 106 ASP A O 445 C CB . ASP A 113 ? 0.4474 0.3564 0.2904 0.0897 0.0873 0.0684 106 ASP A CB 446 C CG . ASP A 113 ? 0.4891 0.3879 0.3055 0.0995 0.0827 0.0684 106 ASP A CG 447 O OD1 . ASP A 113 ? 0.4813 0.3672 0.2803 0.1057 0.0892 0.0752 106 ASP A OD1 448 O OD2 . ASP A 113 ? 0.4545 0.3573 0.2668 0.1012 0.0723 0.0618 106 ASP A OD2 449 N N . SER A 114 ? 0.4058 0.3299 0.2974 0.0717 0.0858 0.0654 107 SER A N 450 C CA A SER A 114 ? 0.3948 0.3268 0.3101 0.0629 0.0886 0.0644 107 SER A CA 451 C CA B SER A 114 ? 0.3993 0.3318 0.3148 0.0628 0.0885 0.0642 107 SER A CA 452 C C . SER A 114 ? 0.3774 0.3147 0.3023 0.0590 0.0787 0.0584 107 SER A C 453 O O . SER A 114 ? 0.3738 0.3137 0.2921 0.0613 0.0697 0.0534 107 SER A O 454 C CB A SER A 114 ? 0.3764 0.3193 0.3044 0.0586 0.0916 0.0620 107 SER A CB 455 C CB B SER A 114 ? 0.3776 0.3215 0.3041 0.0590 0.0896 0.0607 107 SER A CB 456 O OG A SER A 114 ? 0.3567 0.3073 0.2826 0.0590 0.0829 0.0554 107 SER A OG 457 O OG B SER A 114 ? 0.4197 0.3601 0.3356 0.0637 0.0975 0.0647 107 SER A OG 458 N N . VAL A 115 ? 0.3702 0.3089 0.3112 0.0530 0.0808 0.0587 108 VAL A N 459 C CA . VAL A 115 ? 0.3641 0.3082 0.3152 0.0490 0.0723 0.0526 108 VAL A CA 460 C C . VAL A 115 ? 0.3624 0.3131 0.3345 0.0408 0.0753 0.0510 108 VAL A C 461 O O . VAL A 115 ? 0.3634 0.3091 0.3431 0.0385 0.0825 0.0556 108 VAL A O 462 C CB . VAL A 115 ? 0.3718 0.3067 0.3168 0.0520 0.0695 0.0540 108 VAL A CB 463 C CG1 . VAL A 115 ? 0.3344 0.2765 0.2885 0.0487 0.0603 0.0465 108 VAL A CG1 464 C CG2 . VAL A 115 ? 0.3684 0.2941 0.2913 0.0611 0.0676 0.0571 108 VAL A CG2 465 N N . GLU A 116 ? 0.3477 0.3093 0.3293 0.0365 0.0695 0.0446 109 GLU A N 466 C CA A GLU A 116 ? 0.3498 0.3181 0.3505 0.0292 0.0707 0.0423 109 GLU A CA 467 C CA B GLU A 116 ? 0.3397 0.3086 0.3404 0.0292 0.0704 0.0420 109 GLU A CA 468 C C . GLU A 116 ? 0.3332 0.3063 0.3410 0.0254 0.0625 0.0355 109 GLU A C 469 O O . GLU A 116 ? 0.3216 0.2957 0.3212 0.0280 0.0560 0.0321 109 GLU A O 470 C CB A GLU A 116 ? 0.3610 0.3379 0.3678 0.0274 0.0727 0.0415 109 GLU A CB 471 C CB B GLU A 116 ? 0.3408 0.3188 0.3454 0.0279 0.0707 0.0403 109 GLU A CB 472 C CG A GLU A 116 ? 0.4185 0.3917 0.4247 0.0293 0.0833 0.0483 109 GLU A CG 473 C CG B GLU A 116 ? 0.3424 0.3246 0.3366 0.0309 0.0634 0.0360 109 GLU A CG 474 C CD A GLU A 116 ? 0.4840 0.4551 0.5066 0.0244 0.0905 0.0518 109 GLU A CD 475 C CD B GLU A 116 ? 0.3682 0.3572 0.3636 0.0310 0.0645 0.0352 109 GLU A CD 476 O OE1 A GLU A 116 ? 0.5130 0.4916 0.5515 0.0199 0.0931 0.0510 109 GLU A OE1 477 O OE1 B GLU A 116 ? 0.3501 0.3354 0.3345 0.0361 0.0690 0.0388 109 GLU A OE1 478 O OE2 A GLU A 116 ? 0.5074 0.4694 0.5282 0.0249 0.0935 0.0554 109 GLU A OE2 479 O OE2 B GLU A 116 ? 0.3130 0.3104 0.3194 0.0265 0.0606 0.0309 109 GLU A OE2 480 N N . LEU A 117 ? 0.3106 0.2863 0.3341 0.0194 0.0631 0.0336 110 LEU A N 481 C CA . LEU A 117 ? 0.2966 0.2779 0.3265 0.0156 0.0557 0.0266 110 LEU A CA 482 C C . LEU A 117 ? 0.2965 0.2880 0.3335 0.0123 0.0532 0.0231 110 LEU A C 483 O O . LEU A 117 ? 0.2871 0.2815 0.3337 0.0100 0.0577 0.0253 110 LEU A O 484 C CB . LEU A 117 ? 0.3021 0.2794 0.3433 0.0115 0.0562 0.0255 110 LEU A CB 485 C CG . LEU A 117 ? 0.3390 0.3054 0.3746 0.0146 0.0588 0.0291 110 LEU A CG 486 C CD1 . LEU A 117 ? 0.3933 0.3567 0.4428 0.0095 0.0588 0.0268 110 LEU A CD1 487 C CD2 . LEU A 117 ? 0.3386 0.3032 0.3618 0.0193 0.0534 0.0270 110 LEU A CD2 488 N N . ALA A 118 ? 0.2819 0.2788 0.3150 0.0122 0.0463 0.0180 111 ALA A N 489 C CA . ALA A 118 ? 0.2779 0.2835 0.3170 0.0092 0.0429 0.0144 111 ALA A CA 490 C C . ALA A 118 ? 0.2860 0.2933 0.3306 0.0053 0.0374 0.0087 111 ALA A C 491 O O . ALA A 118 ? 0.2854 0.2913 0.3227 0.0069 0.0337 0.0059 111 ALA A O 492 C CB . ALA A 118 ? 0.2854 0.2946 0.3136 0.0126 0.0396 0.0133 111 ALA A CB 493 N N . HIS A 119 ? 0.2573 0.2674 0.3147 0.0006 0.0368 0.0066 112 HIS A N 494 C CA . HIS A 119 ? 0.2661 0.2767 0.3278 -0.0027 0.0314 0.0008 112 HIS A CA 495 C C . HIS A 119 ? 0.2508 0.2688 0.3146 -0.0050 0.0258 -0.0035 112 HIS A C 496 O O . HIS A 119 ? 0.2356 0.2586 0.3029 -0.0051 0.0265 -0.0018 112 HIS A O 497 C CB . HIS A 119 ? 0.2616 0.2680 0.3357 -0.0063 0.0335 0.0007 112 HIS A CB 498 C CG . HIS A 119 ? 0.2929 0.3033 0.3814 -0.0098 0.0355 0.0020 112 HIS A CG 499 N ND1 . HIS A 119 ? 0.3601 0.3684 0.4544 -0.0093 0.0431 0.0081 112 HIS A ND1 500 C CD2 . HIS A 119 ? 0.3011 0.3178 0.3997 -0.0134 0.0310 -0.0019 112 HIS A CD2 501 C CE1 . HIS A 119 ? 0.3382 0.3518 0.4476 -0.0129 0.0436 0.0077 112 HIS A CE1 502 N NE2 . HIS A 119 ? 0.3276 0.3465 0.4399 -0.0154 0.0358 0.0015 112 HIS A NE2 503 N N . TYR A 120 ? 0.2444 0.2625 0.3051 -0.0063 0.0205 -0.0088 113 TYR A N 504 C CA . TYR A 120 ? 0.2420 0.2655 0.3023 -0.0081 0.0147 -0.0131 113 TYR A CA 505 C C . TYR A 120 ? 0.2330 0.2538 0.2956 -0.0108 0.0106 -0.0187 113 TYR A C 506 O O . TYR A 120 ? 0.2397 0.2548 0.3010 -0.0104 0.0122 -0.0195 113 TYR A O 507 C CB . TYR A 120 ? 0.2232 0.2492 0.2711 -0.0052 0.0128 -0.0134 113 TYR A CB 508 C CG . TYR A 120 ? 0.2002 0.2274 0.2449 -0.0022 0.0165 -0.0086 113 TYR A CG 509 C CD1 . TYR A 120 ? 0.2084 0.2406 0.2570 -0.0023 0.0166 -0.0069 113 TYR A CD1 510 C CD2 . TYR A 120 ? 0.2145 0.2375 0.2526 0.0012 0.0198 -0.0057 113 TYR A CD2 511 C CE1 . TYR A 120 ? 0.2240 0.2565 0.2688 0.0010 0.0204 -0.0027 113 TYR A CE1 512 C CE2 . TYR A 120 ? 0.2441 0.2671 0.2781 0.0044 0.0230 -0.0015 113 TYR A CE2 513 C CZ . TYR A 120 ? 0.2326 0.2602 0.2695 0.0043 0.0235 -0.0001 113 TYR A CZ 514 O OH . TYR A 120 ? 0.2252 0.2521 0.2567 0.0081 0.0270 0.0037 113 TYR A OH 515 N N . ASP A 121 ? 0.2341 0.2584 0.2997 -0.0132 0.0052 -0.0226 114 ASP A N 516 C CA . ASP A 121 ? 0.2460 0.2672 0.3118 -0.0155 0.0004 -0.0287 114 ASP A CA 517 C C . ASP A 121 ? 0.2451 0.2676 0.2981 -0.0141 -0.0035 -0.0319 114 ASP A C 518 O O . ASP A 121 ? 0.2453 0.2722 0.2973 -0.0145 -0.0075 -0.0326 114 ASP A O 519 C CB . ASP A 121 ? 0.2612 0.2842 0.3412 -0.0193 -0.0033 -0.0312 114 ASP A CB 520 C CG . ASP A 121 ? 0.3066 0.3278 0.4007 -0.0210 0.0019 -0.0276 114 ASP A CG 521 O OD1 . ASP A 121 ? 0.2945 0.3094 0.3874 -0.0205 0.0057 -0.0266 114 ASP A OD1 522 O OD2 . ASP A 121 ? 0.3173 0.3432 0.4230 -0.0225 0.0029 -0.0252 114 ASP A OD2 523 N N . VAL A 122 ? 0.2433 0.2620 0.2870 -0.0123 -0.0022 -0.0334 115 VAL A N 524 C CA . VAL A 122 ? 0.2366 0.2564 0.2677 -0.0105 -0.0037 -0.0351 115 VAL A CA 525 C C . VAL A 122 ? 0.2477 0.2628 0.2725 -0.0108 -0.0059 -0.0409 115 VAL A C 526 O O . VAL A 122 ? 0.2491 0.2594 0.2783 -0.0116 -0.0053 -0.0433 115 VAL A O 527 C CB . VAL A 122 ? 0.2333 0.2539 0.2587 -0.0074 0.0007 -0.0312 115 VAL A CB 528 C CG1 . VAL A 122 ? 0.1903 0.2147 0.2194 -0.0065 0.0028 -0.0259 115 VAL A CG1 529 C CG2 . VAL A 122 ? 0.2054 0.2209 0.2310 -0.0059 0.0042 -0.0316 115 VAL A CG2 530 N N . LEU A 123 ? 0.2357 0.2515 0.2496 -0.0099 -0.0080 -0.0429 116 LEU A N 531 C CA . LEU A 123 ? 0.2475 0.2585 0.2530 -0.0095 -0.0093 -0.0483 116 LEU A CA 532 C C . LEU A 123 ? 0.2532 0.2615 0.2561 -0.0074 -0.0041 -0.0482 116 LEU A C 533 O O . LEU A 123 ? 0.2730 0.2841 0.2722 -0.0055 -0.0007 -0.0451 116 LEU A O 534 C CB . LEU A 123 ? 0.2317 0.2435 0.2249 -0.0087 -0.0120 -0.0497 116 LEU A CB 535 C CG . LEU A 123 ? 0.2662 0.2719 0.2494 -0.0083 -0.0142 -0.0560 116 LEU A CG 536 C CD1 . LEU A 123 ? 0.2716 0.2748 0.2597 -0.0105 -0.0212 -0.0605 116 LEU A CD1 537 C CD2 . LEU A 123 ? 0.2882 0.2934 0.2565 -0.0067 -0.0143 -0.0563 116 LEU A CD2 538 N N . LEU A 124 ? 0.2614 0.2642 0.2670 -0.0076 -0.0038 -0.0519 117 LEU A N 539 C CA . LEU A 124 ? 0.2625 0.2622 0.2654 -0.0051 0.0005 -0.0531 117 LEU A CA 540 C C . LEU A 124 ? 0.2748 0.2692 0.2692 -0.0046 -0.0007 -0.0597 117 LEU A C 541 O O . LEU A 124 ? 0.2921 0.2853 0.2816 -0.0060 -0.0054 -0.0630 117 LEU A O 542 C CB . LEU A 124 ? 0.2479 0.2447 0.2610 -0.0049 0.0030 -0.0510 117 LEU A CB 543 C CG . LEU A 124 ? 0.2515 0.2521 0.2714 -0.0047 0.0050 -0.0443 117 LEU A CG 544 C CD1 . LEU A 124 ? 0.2209 0.2168 0.2485 -0.0038 0.0081 -0.0419 117 LEU A CD1 545 C CD2 . LEU A 124 ? 0.2018 0.2078 0.2163 -0.0023 0.0071 -0.0405 117 LEU A CD2 546 N N . SER A 125 ? 0.2708 0.2620 0.2631 -0.0023 0.0031 -0.0617 118 SER A N 547 C CA . SER A 125 ? 0.2878 0.2739 0.2704 -0.0008 0.0035 -0.0679 118 SER A CA 548 C C . SER A 125 ? 0.2959 0.2772 0.2834 0.0010 0.0067 -0.0702 118 SER A C 549 O O . SER A 125 ? 0.2794 0.2629 0.2727 0.0027 0.0106 -0.0664 118 SER A O 550 C CB . SER A 125 ? 0.3039 0.2930 0.2759 0.0010 0.0070 -0.0671 118 SER A CB 551 O OG . SER A 125 ? 0.3213 0.3056 0.2843 0.0033 0.0098 -0.0724 118 SER A OG 552 N N . TYR A 126 ? 0.3003 0.2744 0.2852 0.0008 0.0045 -0.0765 119 TYR A N 553 C CA . TYR A 126 ? 0.3139 0.2820 0.3032 0.0027 0.0071 -0.0795 119 TYR A CA 554 C C . TYR A 126 ? 0.3365 0.2979 0.3153 0.0044 0.0069 -0.0873 119 TYR A C 555 O O . TYR A 126 ? 0.3439 0.3029 0.3144 0.0031 0.0023 -0.0912 119 TYR A O 556 C CB . TYR A 126 ? 0.3249 0.2889 0.3259 0.0001 0.0040 -0.0793 119 TYR A CB 557 C CG . TYR A 126 ? 0.3265 0.2955 0.3376 -0.0013 0.0046 -0.0717 119 TYR A CG 558 C CD1 . TYR A 126 ? 0.3279 0.2988 0.3435 0.0011 0.0091 -0.0667 119 TYR A CD1 559 C CD2 . TYR A 126 ? 0.3547 0.3263 0.3707 -0.0049 0.0005 -0.0699 119 TYR A CD2 560 C CE1 . TYR A 126 ? 0.3046 0.2788 0.3274 0.0002 0.0098 -0.0599 119 TYR A CE1 561 C CE2 . TYR A 126 ? 0.3482 0.3238 0.3730 -0.0061 0.0019 -0.0631 119 TYR A CE2 562 C CZ . TYR A 126 ? 0.3367 0.3131 0.3638 -0.0033 0.0067 -0.0581 119 TYR A CZ 563 O OH . TYR A 126 ? 0.3149 0.2942 0.3485 -0.0040 0.0081 -0.0516 119 TYR A OH 564 N N . PRO A 127 ? 0.3510 0.3088 0.3299 0.0077 0.0115 -0.0898 120 PRO A N 565 C CA . PRO A 127 ? 0.3744 0.3243 0.3437 0.0097 0.0115 -0.0979 120 PRO A CA 566 C C . PRO A 127 ? 0.4061 0.3481 0.3790 0.0072 0.0051 -0.1030 120 PRO A C 567 O O . PRO A 127 ? 0.4086 0.3507 0.3945 0.0045 0.0028 -0.0998 120 PRO A O 568 C CB . PRO A 127 ? 0.3706 0.3187 0.3439 0.0138 0.0178 -0.0988 120 PRO A CB 569 C CG . PRO A 127 ? 0.3640 0.3211 0.3459 0.0143 0.0214 -0.0907 120 PRO A CG 570 C CD . PRO A 127 ? 0.3337 0.2945 0.3209 0.0103 0.0167 -0.0855 120 PRO A CD 571 N N . ASN A 128 ? 0.4360 0.3710 0.3974 0.0082 0.0024 -0.1108 121 ASN A N 572 C CA . ASN A 128 ? 0.4735 0.3999 0.4382 0.0062 -0.0040 -0.1171 121 ASN A CA 573 C C . ASN A 128 ? 0.4946 0.4137 0.4656 0.0085 -0.0006 -0.1204 121 ASN A C 574 O O . ASN A 128 ? 0.4957 0.4111 0.4578 0.0128 0.0040 -0.1246 121 ASN A O 575 C CB . ASN A 128 ? 0.4870 0.4081 0.4351 0.0069 -0.0089 -0.1246 121 ASN A CB 576 C CG . ASN A 128 ? 0.5505 0.4626 0.5024 0.0046 -0.0172 -0.1321 121 ASN A CG 577 O OD1 . ASN A 128 ? 0.5813 0.4876 0.5434 0.0043 -0.0168 -0.1344 121 ASN A OD1 578 N ND2 . ASN A 128 ? 0.6298 0.5407 0.5738 0.0029 -0.0252 -0.1358 121 ASN A ND2 579 N N . LYS A 129 ? 0.5181 0.4353 0.5049 0.0060 -0.0022 -0.1179 122 LYS A N 580 C CA . LYS A 129 ? 0.5499 0.4591 0.5446 0.0079 0.0002 -0.1202 122 LYS A CA 581 C C . LYS A 129 ? 0.5767 0.4748 0.5628 0.0102 -0.0015 -0.1308 122 LYS A C 582 O O . LYS A 129 ? 0.5850 0.4779 0.5716 0.0141 0.0030 -0.1333 122 LYS A O 583 C CB . LYS A 129 ? 0.5614 0.4686 0.5732 0.0038 -0.0024 -0.1163 122 LYS A CB 584 C CG . LYS A 129 ? 0.5943 0.5055 0.6164 0.0049 0.0030 -0.1073 122 LYS A CG 585 C CD . LYS A 129 ? 0.6723 0.5739 0.7011 0.0076 0.0055 -0.1094 122 LYS A CD 586 C CE . LYS A 129 ? 0.6925 0.5942 0.7341 0.0072 0.0084 -0.1008 122 LYS A CE 587 N NZ . LYS A 129 ? 0.7159 0.6067 0.7639 0.0098 0.0101 -0.1029 122 LYS A NZ 588 N N . THR A 130 ? 0.5834 0.4776 0.5611 0.0084 -0.0082 -0.1373 123 THR A N 589 C CA . THR A 130 ? 0.6122 0.4947 0.5807 0.0108 -0.0108 -0.1480 123 THR A CA 590 C C . THR A 130 ? 0.6251 0.5064 0.5715 0.0150 -0.0090 -0.1532 123 THR A C 591 O O . THR A 130 ? 0.6510 0.5222 0.5867 0.0175 -0.0112 -0.1625 123 THR A O 592 C CB . THR A 130 ? 0.6232 0.4987 0.5976 0.0063 -0.0208 -0.1539 123 THR A CB 593 O OG1 . THR A 130 ? 0.6228 0.5044 0.5923 0.0034 -0.0268 -0.1527 123 THR A OG1 594 C CG2 . THR A 130 ? 0.6159 0.4898 0.6125 0.0024 -0.0214 -0.1496 123 THR A CG2 595 N N . HIS A 131 ? 0.6100 0.5008 0.5493 0.0159 -0.0047 -0.1473 124 HIS A N 596 C CA . HIS A 131 ? 0.6195 0.5098 0.5377 0.0195 -0.0021 -0.1505 124 HIS A CA 597 C C . HIS A 131 ? 0.5909 0.4914 0.5091 0.0218 0.0074 -0.1427 124 HIS A C 598 O O . HIS A 131 ? 0.5734 0.4820 0.4890 0.0200 0.0074 -0.1368 124 HIS A O 599 C CB . HIS A 131 ? 0.6334 0.5252 0.5433 0.0165 -0.0104 -0.1511 124 HIS A CB 600 C CG . HIS A 131 ? 0.7162 0.6020 0.6018 0.0201 -0.0113 -0.1574 124 HIS A CG 601 N ND1 . HIS A 131 ? 0.8105 0.6854 0.6832 0.0245 -0.0097 -0.1664 124 HIS A ND1 602 C CD2 . HIS A 131 ? 0.7663 0.6546 0.6371 0.0201 -0.0143 -0.1561 124 HIS A CD2 603 C CE1 . HIS A 131 ? 0.8337 0.7046 0.6836 0.0273 -0.0110 -0.1701 124 HIS A CE1 604 N NE2 . HIS A 131 ? 0.8240 0.7026 0.6723 0.0247 -0.0139 -0.1638 124 HIS A NE2 605 N N . PRO A 132 ? 0.5708 0.4707 0.4934 0.0257 0.0153 -0.1428 125 PRO A N 606 C CA . PRO A 132 ? 0.5396 0.4496 0.4679 0.0274 0.0237 -0.1354 125 PRO A CA 607 C C . PRO A 132 ? 0.5305 0.4453 0.4441 0.0297 0.0296 -0.1340 125 PRO A C 608 O O . PRO A 132 ? 0.5408 0.4492 0.4368 0.0324 0.0309 -0.1401 125 PRO A O 609 C CB . PRO A 132 ? 0.5540 0.4601 0.4912 0.0314 0.0290 -0.1378 125 PRO A CB 610 C CG . PRO A 132 ? 0.5836 0.4767 0.5123 0.0330 0.0257 -0.1480 125 PRO A CG 611 C CD . PRO A 132 ? 0.5871 0.4767 0.5125 0.0283 0.0157 -0.1500 125 PRO A CD 612 N N . ASN A 133 ? 0.4863 0.4120 0.4068 0.0286 0.0333 -0.1257 126 ASN A N 613 C CA . ASN A 133 ? 0.4703 0.4014 0.3804 0.0302 0.0397 -0.1230 126 ASN A CA 614 C C . ASN A 133 ? 0.4648 0.3958 0.3750 0.0352 0.0496 -0.1254 126 ASN A C 615 O O . ASN A 133 ? 0.4549 0.3875 0.3799 0.0368 0.0519 -0.1247 126 ASN A O 616 C CB . ASN A 133 ? 0.4308 0.3734 0.3507 0.0272 0.0401 -0.1137 126 ASN A CB 617 C CG . ASN A 133 ? 0.4470 0.3909 0.3686 0.0226 0.0312 -0.1108 126 ASN A CG 618 O OD1 . ASN A 133 ? 0.4315 0.3696 0.3416 0.0214 0.0255 -0.1149 126 ASN A OD1 619 N ND2 . ASN A 133 ? 0.4023 0.3536 0.3385 0.0200 0.0297 -0.1040 126 ASN A ND2 620 N N . TYR A 134 ? 0.4704 0.3991 0.3643 0.0380 0.0555 -0.1280 127 TYR A N 621 C CA . TYR A 134 ? 0.4773 0.4077 0.3725 0.0428 0.0666 -0.1293 127 TYR A CA 622 C C . TYR A 134 ? 0.4853 0.4150 0.3619 0.0447 0.0735 -0.1294 127 TYR A C 623 O O . TYR A 134 ? 0.4899 0.4161 0.3508 0.0428 0.0689 -0.1293 127 TYR A O 624 C CB . TYR A 134 ? 0.4945 0.4161 0.3912 0.0469 0.0679 -0.1372 127 TYR A CB 625 C CG . TYR A 134 ? 0.5257 0.4345 0.4010 0.0491 0.0659 -0.1460 127 TYR A CG 626 C CD1 . TYR A 134 ? 0.5822 0.4859 0.4441 0.0545 0.0750 -0.1513 127 TYR A CD1 627 C CD2 . TYR A 134 ? 0.5326 0.4343 0.4014 0.0459 0.0547 -0.1493 127 TYR A CD2 628 C CE1 . TYR A 134 ? 0.5874 0.4780 0.4277 0.0572 0.0726 -0.1601 127 TYR A CE1 629 C CE2 . TYR A 134 ? 0.5819 0.4714 0.4311 0.0481 0.0515 -0.1580 127 TYR A CE2 630 C CZ . TYR A 134 ? 0.6249 0.5084 0.4587 0.0539 0.0603 -0.1635 127 TYR A CZ 631 O OH . TYR A 134 ? 0.6476 0.5180 0.4600 0.0565 0.0565 -0.1725 127 TYR A OH 632 N N . ILE A 135 ? 0.4918 0.4249 0.3707 0.0485 0.0847 -0.1293 128 ILE A N 633 C CA . ILE A 135 ? 0.4973 0.4297 0.3600 0.0506 0.0937 -0.1288 128 ILE A CA 634 C C . ILE A 135 ? 0.5229 0.4481 0.3780 0.0567 0.1023 -0.1363 128 ILE A C 635 O O . ILE A 135 ? 0.5065 0.4328 0.3767 0.0592 0.1045 -0.1390 128 ILE A O 636 C CB . ILE A 135 ? 0.4942 0.4392 0.3694 0.0492 0.1012 -0.1205 128 ILE A CB 637 C CG1 . ILE A 135 ? 0.4524 0.4046 0.3357 0.0436 0.0930 -0.1133 128 ILE A CG1 638 C CG2 . ILE A 135 ? 0.5004 0.4440 0.3593 0.0516 0.1124 -0.1197 128 ILE A CG2 639 C CD1 . ILE A 135 ? 0.4163 0.3814 0.3202 0.0421 0.0974 -0.1063 128 ILE A CD1 640 N N . SER A 136 ? 0.5430 0.4600 0.3738 0.0594 0.1067 -0.1397 129 SER A N 641 C CA . SER A 136 ? 0.5753 0.4847 0.3948 0.0657 0.1165 -0.1466 129 SER A CA 642 C C . SER A 136 ? 0.5907 0.5019 0.3982 0.0682 0.1298 -0.1435 129 SER A C 643 O O . SER A 136 ? 0.5844 0.4981 0.3831 0.0654 0.1299 -0.1375 129 SER A O 644 C CB . SER A 136 ? 0.5904 0.4843 0.3866 0.0681 0.1097 -0.1557 129 SER A CB 645 O OG . SER A 136 ? 0.6230 0.5137 0.4294 0.0657 0.0975 -0.1593 129 SER A OG 646 N N . ILE A 137 ? 0.6084 0.5174 0.4151 0.0739 0.1415 -0.1479 130 ILE A N 647 C CA . ILE A 137 ? 0.6385 0.5433 0.4254 0.0779 0.1544 -0.1481 130 ILE A CA 648 C C . ILE A 137 ? 0.6851 0.5731 0.4453 0.0825 0.1512 -0.1581 130 ILE A C 649 O O . ILE A 137 ? 0.6746 0.5573 0.4399 0.0850 0.1475 -0.1656 130 ILE A O 650 C CB . ILE A 137 ? 0.6461 0.5586 0.4488 0.0818 0.1701 -0.1474 130 ILE A CB 651 C CG1 . ILE A 137 ? 0.6017 0.5310 0.4326 0.0773 0.1727 -0.1382 130 ILE A CG1 652 C CG2 . ILE A 137 ? 0.6390 0.5443 0.4178 0.0869 0.1847 -0.1489 130 ILE A CG2 653 C CD1 . ILE A 137 ? 0.6019 0.5402 0.4541 0.0811 0.1864 -0.1383 130 ILE A CD1 654 N N . ILE A 138 ? 0.7373 0.6164 0.4687 0.0836 0.1518 -0.1582 131 ILE A N 655 C CA . ILE A 138 ? 0.7967 0.6592 0.4992 0.0876 0.1464 -0.1673 131 ILE A CA 656 C C . ILE A 138 ? 0.8400 0.6944 0.5169 0.0941 0.1615 -0.1691 131 ILE A C 657 O O . ILE A 138 ? 0.8380 0.6973 0.5104 0.0934 0.1711 -0.1612 131 ILE A O 658 C CB . ILE A 138 ? 0.8036 0.6617 0.4944 0.0830 0.1299 -0.1662 131 ILE A CB 659 C CG1 . ILE A 138 ? 0.8554 0.6979 0.5262 0.0858 0.1190 -0.1772 131 ILE A CG1 660 C CG2 . ILE A 138 ? 0.8159 0.6750 0.4902 0.0814 0.1330 -0.1582 131 ILE A CG2 661 C CD1 . ILE A 138 ? 0.8774 0.7177 0.5447 0.0806 0.1010 -0.1768 131 ILE A CD1 662 N N . ASN A 139 ? 0.8726 0.7148 0.5339 0.1006 0.1646 -0.1791 132 ASN A N 663 C CA . ASN A 139 ? 0.9271 0.7598 0.5605 0.1075 0.1792 -0.1813 132 ASN A CA 664 C C . ASN A 139 ? 0.9674 0.7855 0.5629 0.1091 0.1724 -0.1832 132 ASN A C 665 O O . ASN A 139 ? 0.9624 0.7783 0.5552 0.1048 0.1558 -0.1835 132 ASN A O 666 C CB . ASN A 139 ? 0.9373 0.7633 0.5695 0.1147 0.1882 -0.1908 132 ASN A CB 667 C CG . ASN A 139 ? 0.9409 0.7522 0.5589 0.1173 0.1750 -0.2027 132 ASN A CG 668 O OD1 . ASN A 139 ? 0.9388 0.7417 0.5396 0.1152 0.1608 -0.2050 132 ASN A OD1 669 N ND2 . ASN A 139 ? 0.9197 0.7277 0.5463 0.1220 0.1795 -0.2107 132 ASN A ND2 670 N N . GLU A 140 ? 1.0159 0.8239 0.5823 0.1154 0.1852 -0.1844 133 GLU A N 671 C CA . GLU A 140 ? 1.0610 0.8542 0.5887 0.1179 0.1796 -0.1857 133 GLU A CA 672 C C . GLU A 140 ? 1.0851 0.8629 0.5930 0.1205 0.1631 -0.1977 133 GLU A C 673 O O . GLU A 140 ? 1.1031 0.8709 0.5855 0.1207 0.1523 -0.1987 133 GLU A O 674 C CB . GLU A 140 ? 1.0928 0.8780 0.5929 0.1246 0.1984 -0.1838 133 GLU A CB 675 C CG . GLU A 140 ? 1.1300 0.9078 0.6231 0.1326 0.2110 -0.1929 133 GLU A CG 676 C CD . GLU A 140 ? 1.1623 0.9316 0.6267 0.1395 0.2307 -0.1905 133 GLU A CD 677 O OE1 . GLU A 140 ? 1.2055 0.9596 0.6430 0.1476 0.2355 -0.1999 133 GLU A OE1 678 O OE2 . GLU A 140 ? 1.1603 0.9378 0.6291 0.1368 0.2415 -0.1792 133 GLU A OE2 679 N N . ASP A 141 ? 1.0888 0.8646 0.6095 0.1225 0.1609 -0.2069 134 ASP A N 680 C CA . ASP A 141 ? 1.1085 0.8716 0.6187 0.1236 0.1440 -0.2184 134 ASP A CA 681 C C . ASP A 141 ? 1.0817 0.8534 0.6165 0.1151 0.1258 -0.2159 134 ASP A C 682 O O . ASP A 141 ? 1.0997 0.8623 0.6276 0.1142 0.1095 -0.2238 134 ASP A O 683 C CB . ASP A 141 ? 1.1178 0.8755 0.6347 0.1287 0.1490 -0.2288 134 ASP A CB 684 C CG . ASP A 141 ? 1.1643 0.9128 0.6566 0.1379 0.1674 -0.2323 134 ASP A CG 685 O OD1 . ASP A 141 ? 1.1922 0.9322 0.6524 0.1414 0.1725 -0.2300 134 ASP A OD1 686 O OD2 . ASP A 141 ? 1.1657 0.9152 0.6707 0.1418 0.1772 -0.2371 134 ASP A OD2 687 N N . GLY A 142 ? 1.0363 0.8253 0.6002 0.1088 0.1287 -0.2052 135 GLY A N 688 C CA . GLY A 142 ? 1.0003 0.7986 0.5898 0.1010 0.1137 -0.2021 135 GLY A CA 689 C C . GLY A 142 ? 0.9691 0.7725 0.5885 0.0993 0.1112 -0.2060 135 GLY A C 690 O O . GLY A 142 ? 0.9654 0.7721 0.6020 0.0939 0.0974 -0.2064 135 GLY A O 691 N N . ASN A 143 ? 0.9498 0.7540 0.5762 0.1041 0.1247 -0.2087 136 ASN A N 692 C CA . ASN A 143 ? 0.9127 0.7230 0.5694 0.1029 0.1239 -0.2108 136 ASN A CA 693 C C . ASN A 143 ? 0.8590 0.6881 0.5472 0.0976 0.1285 -0.1996 136 ASN A C 694 O O . ASN A 143 ? 0.8574 0.6947 0.5472 0.0985 0.1416 -0.1926 136 ASN A O 695 C CB . ASN A 143 ? 0.9310 0.7345 0.5834 0.1106 0.1361 -0.2187 136 ASN A CB 696 C CG . ASN A 143 ? 0.9955 0.7794 0.6162 0.1165 0.1318 -0.2308 136 ASN A CG 697 O OD1 . ASN A 143 ? 1.0422 0.8177 0.6520 0.1141 0.1162 -0.2354 136 ASN A OD1 698 N ND2 . ASN A 143 ? 0.9970 0.7735 0.6030 0.1244 0.1454 -0.2364 136 ASN A ND2 699 N N . GLU A 144 ? 0.8074 0.6428 0.5203 0.0923 0.1176 -0.1979 137 GLU A N 700 C CA . GLU A 144 ? 0.7481 0.6003 0.4910 0.0876 0.1202 -0.1880 137 GLU A CA 701 C C . GLU A 144 ? 0.7293 0.5859 0.4912 0.0917 0.1306 -0.1899 137 GLU A C 702 O O . GLU A 144 ? 0.7160 0.5682 0.4891 0.0927 0.1254 -0.1956 137 GLU A O 703 C CB . GLU A 144 ? 0.7227 0.5790 0.4820 0.0807 0.1050 -0.1851 137 GLU A CB 704 C CG . GLU A 144 ? 0.7153 0.5680 0.4568 0.0770 0.0946 -0.1833 137 GLU A CG 705 C CD . GLU A 144 ? 0.6981 0.5567 0.4575 0.0699 0.0811 -0.1792 137 GLU A CD 706 O OE1 . GLU A 144 ? 0.6592 0.5205 0.4405 0.0682 0.0774 -0.1799 137 GLU A OE1 707 O OE2 . GLU A 144 ? 0.6831 0.5432 0.4340 0.0664 0.0744 -0.1752 137 GLU A OE2 708 N N . ILE A 145 ? 0.7228 0.5870 0.4876 0.0944 0.1455 -0.1854 138 ILE A N 709 C CA . ILE A 145 ? 0.7221 0.5903 0.5031 0.0995 0.1571 -0.1879 138 ILE A CA 710 C C . ILE A 145 ? 0.6872 0.5712 0.5031 0.0962 0.1572 -0.1807 138 ILE A C 711 O O . ILE A 145 ? 0.6787 0.5664 0.5122 0.1001 0.1637 -0.1828 138 ILE A O 712 C CB . ILE A 145 ? 0.7453 0.6126 0.5118 0.1053 0.1748 -0.1883 138 ILE A CB 713 C CG1 . ILE A 145 ? 0.7255 0.6045 0.4952 0.1015 0.1816 -0.1774 138 ILE A CG1 714 C CG2 . ILE A 145 ? 0.7775 0.6264 0.5080 0.1105 0.1751 -0.1975 138 ILE A CG2 715 C CD1 . ILE A 145 ? 0.7836 0.6631 0.5425 0.1065 0.2004 -0.1762 138 ILE A CD1 716 N N . PHE A 146 ? 0.6504 0.5430 0.4756 0.0895 0.1494 -0.1725 139 PHE A N 717 C CA . PHE A 146 ? 0.6224 0.5286 0.4779 0.0861 0.1469 -0.1658 139 PHE A CA 718 C C . PHE A 146 ? 0.5893 0.4972 0.4474 0.0792 0.1327 -0.1611 139 PHE A C 719 O O . PHE A 146 ? 0.5703 0.4760 0.4115 0.0762 0.1294 -0.1587 139 PHE A O 720 C CB . PHE A 146 ? 0.6214 0.5415 0.4895 0.0858 0.1585 -0.1581 139 PHE A CB 721 C CG . PHE A 146 ? 0.6158 0.5496 0.5117 0.0814 0.1534 -0.1506 139 PHE A CG 722 C CD1 . PHE A 146 ? 0.6237 0.5622 0.5435 0.0836 0.1526 -0.1517 139 PHE A CD1 723 C CD2 . PHE A 146 ? 0.6095 0.5505 0.5069 0.0754 0.1488 -0.1425 139 PHE A CD2 724 C CE1 . PHE A 146 ? 0.6223 0.5723 0.5657 0.0801 0.1470 -0.1449 139 PHE A CE1 725 C CE2 . PHE A 146 ? 0.5640 0.5167 0.4856 0.0717 0.1434 -0.1360 139 PHE A CE2 726 C CZ . PHE A 146 ? 0.5626 0.5197 0.5065 0.0741 0.1425 -0.1372 139 PHE A CZ 727 N N . ASN A 147 ? 0.5711 0.4824 0.4497 0.0771 0.1247 -0.1599 140 ASN A N 728 C CA . ASN A 147 ? 0.5603 0.4743 0.4444 0.0707 0.1124 -0.1549 140 ASN A CA 729 C C . ASN A 147 ? 0.5302 0.4571 0.4404 0.0685 0.1117 -0.1474 140 ASN A C 730 O O . ASN A 147 ? 0.5168 0.4463 0.4437 0.0719 0.1152 -0.1487 140 ASN A O 731 C CB . ASN A 147 ? 0.5820 0.4849 0.4638 0.0699 0.1015 -0.1610 140 ASN A CB 732 C CG . ASN A 147 ? 0.6275 0.5168 0.4828 0.0713 0.0986 -0.1688 140 ASN A CG 733 O OD1 . ASN A 147 ? 0.6346 0.5232 0.4714 0.0711 0.1013 -0.1675 140 ASN A OD1 734 N ND2 . ASN A 147 ? 0.6728 0.5506 0.5257 0.0729 0.0926 -0.1768 140 ASN A ND2 735 N N . THR A 148 ? 0.4996 0.4341 0.4134 0.0631 0.1068 -0.1399 141 THR A N 736 C CA . THR A 148 ? 0.4820 0.4276 0.4187 0.0607 0.1041 -0.1329 141 THR A CA 737 C C . THR A 148 ? 0.4865 0.4275 0.4329 0.0593 0.0939 -0.1340 141 THR A C 738 O O . THR A 148 ? 0.4912 0.4214 0.4266 0.0586 0.0878 -0.1391 141 THR A O 739 C CB . THR A 148 ? 0.4635 0.4177 0.4001 0.0556 0.1020 -0.1249 141 THR A CB 740 O OG1 . THR A 148 ? 0.4678 0.4158 0.3906 0.0516 0.0927 -0.1251 141 THR A OG1 741 C CG2 . THR A 148 ? 0.4591 0.4175 0.3876 0.0567 0.1126 -0.1231 141 THR A CG2 742 N N . SER A 149 ? 0.4713 0.4199 0.4380 0.0591 0.0922 -0.1291 142 SER A N 743 C CA . SER A 149 ? 0.4746 0.4188 0.4519 0.0587 0.0846 -0.1292 142 SER A CA 744 C C . SER A 149 ? 0.4699 0.4101 0.4417 0.0531 0.0745 -0.1271 142 SER A C 745 O O . SER A 149 ? 0.4685 0.4135 0.4344 0.0491 0.0724 -0.1227 142 SER A O 746 C CB . SER A 149 ? 0.4676 0.4218 0.4661 0.0598 0.0849 -0.1232 142 SER A CB 747 O OG A SER A 149 ? 0.4296 0.3913 0.4316 0.0550 0.0799 -0.1157 142 SER A OG 748 O OG B SER A 149 ? 0.4947 0.4446 0.5040 0.0643 0.0854 -0.1264 142 SER A OG 749 N N . LEU A 150 ? 0.4770 0.4084 0.4518 0.0528 0.0685 -0.1300 143 LEU A N 750 C CA . LEU A 150 ? 0.4753 0.4037 0.4482 0.0474 0.0593 -0.1276 143 LEU A CA 751 C C . LEU A 150 ? 0.4585 0.3929 0.4472 0.0453 0.0555 -0.1197 143 LEU A C 752 O O . LEU A 150 ? 0.4315 0.3658 0.4205 0.0406 0.0491 -0.1161 143 LEU A O 753 C CB . LEU A 150 ? 0.5062 0.4212 0.4737 0.0472 0.0543 -0.1348 143 LEU A CB 754 C CG . LEU A 150 ? 0.5493 0.4562 0.4986 0.0496 0.0567 -0.1437 143 LEU A CG 755 C CD1 . LEU A 150 ? 0.6094 0.5030 0.5556 0.0490 0.0502 -0.1509 143 LEU A CD1 756 C CD2 . LEU A 150 ? 0.5719 0.4825 0.5060 0.0470 0.0563 -0.1422 143 LEU A CD2 757 N N . PHE A 151 ? 0.4354 0.3749 0.4370 0.0490 0.0593 -0.1171 144 PHE A N 758 C CA . PHE A 151 ? 0.4168 0.3613 0.4318 0.0480 0.0557 -0.1096 144 PHE A CA 759 C C . PHE A 151 ? 0.3973 0.3492 0.4243 0.0527 0.0605 -0.1077 144 PHE A C 760 O O . PHE A 151 ? 0.4094 0.3604 0.4368 0.0570 0.0664 -0.1127 144 PHE A O 761 C CB . PHE A 151 ? 0.4188 0.3536 0.4390 0.0473 0.0502 -0.1098 144 PHE A CB 762 C CG . PHE A 151 ? 0.4482 0.3740 0.4714 0.0520 0.0525 -0.1160 144 PHE A CG 763 C CD1 . PHE A 151 ? 0.4715 0.3979 0.5075 0.0567 0.0540 -0.1140 144 PHE A CD1 764 C CD2 . PHE A 151 ? 0.4886 0.4050 0.5015 0.0522 0.0528 -0.1242 144 PHE A CD2 765 C CE1 . PHE A 151 ? 0.5010 0.4189 0.5403 0.0614 0.0562 -0.1196 144 PHE A CE1 766 C CE2 . PHE A 151 ? 0.5383 0.4459 0.5537 0.0568 0.0550 -0.1304 144 PHE A CE2 767 C CZ . PHE A 151 ? 0.5284 0.4367 0.5574 0.0614 0.0570 -0.1280 144 PHE A CZ 768 N N . GLU A 152 ? 0.3724 0.3315 0.4093 0.0523 0.0579 -0.1007 145 GLU A N 769 C CA . GLU A 152 ? 0.3609 0.3266 0.4117 0.0572 0.0606 -0.0988 145 GLU A CA 770 C C . GLU A 152 ? 0.3640 0.3215 0.4228 0.0613 0.0586 -0.1001 145 GLU A C 771 O O . GLU A 152 ? 0.3656 0.3157 0.4235 0.0593 0.0533 -0.0978 145 GLU A O 772 C CB . GLU A 152 ? 0.3412 0.3161 0.3990 0.0557 0.0571 -0.0913 145 GLU A CB 773 C CG . GLU A 152 ? 0.3289 0.3115 0.3798 0.0511 0.0578 -0.0886 145 GLU A CG 774 C CD . GLU A 152 ? 0.3510 0.3408 0.4085 0.0498 0.0532 -0.0815 145 GLU A CD 775 O OE1 . GLU A 152 ? 0.3396 0.3261 0.3924 0.0465 0.0482 -0.0781 145 GLU A OE1 776 O OE2 . GLU A 152 ? 0.3159 0.3144 0.3837 0.0522 0.0546 -0.0798 145 GLU A OE2 777 N N . PRO A 153 ? 0.3774 0.3364 0.4455 0.0672 0.0629 -0.1032 146 PRO A N 778 C CA . PRO A 153 ? 0.3827 0.3340 0.4594 0.0717 0.0605 -0.1036 146 PRO A CA 779 C C . PRO A 153 ? 0.3724 0.3249 0.4551 0.0711 0.0540 -0.0957 146 PRO A C 780 O O . PRO A 153 ? 0.3740 0.3367 0.4631 0.0716 0.0530 -0.0913 146 PRO A O 781 C CB . PRO A 153 ? 0.4019 0.3590 0.4897 0.0780 0.0662 -0.1069 146 PRO A CB 782 C CG . PRO A 153 ? 0.4125 0.3746 0.4923 0.0766 0.0734 -0.1113 146 PRO A CG 783 C CD . PRO A 153 ? 0.3837 0.3509 0.4551 0.0701 0.0704 -0.1065 146 PRO A CD 784 N N . PRO A 154 ? 0.3770 0.3189 0.4572 0.0696 0.0495 -0.0938 147 PRO A N 785 C CA . PRO A 154 ? 0.3683 0.3113 0.4518 0.0690 0.0443 -0.0858 147 PRO A CA 786 C C . PRO A 154 ? 0.3776 0.3227 0.4730 0.0758 0.0428 -0.0832 147 PRO A C 787 O O . PRO A 154 ? 0.3820 0.3235 0.4840 0.0810 0.0452 -0.0875 147 PRO A O 788 C CB . PRO A 154 ? 0.3863 0.3166 0.4650 0.0660 0.0412 -0.0846 147 PRO A CB 789 C CG . PRO A 154 ? 0.4014 0.3230 0.4786 0.0673 0.0439 -0.0923 147 PRO A CG 790 C CD . PRO A 154 ? 0.3961 0.3254 0.4696 0.0676 0.0489 -0.0981 147 PRO A CD 791 N N . PRO A 155 ? 0.3701 0.3207 0.4680 0.0761 0.0387 -0.0765 148 PRO A N 792 C CA . PRO A 155 ? 0.3813 0.3348 0.4899 0.0826 0.0360 -0.0739 148 PRO A CA 793 C C . PRO A 155 ? 0.3791 0.3195 0.4899 0.0871 0.0333 -0.0721 148 PRO A C 794 O O . PRO A 155 ? 0.3812 0.3107 0.4849 0.0838 0.0326 -0.0707 148 PRO A O 795 C CB . PRO A 155 ? 0.3574 0.3181 0.4641 0.0808 0.0315 -0.0673 148 PRO A CB 796 C CG . PRO A 155 ? 0.3740 0.3312 0.4689 0.0739 0.0312 -0.0649 148 PRO A CG 797 C CD . PRO A 155 ? 0.3768 0.3308 0.4670 0.0705 0.0360 -0.0713 148 PRO A CD 798 N N . PRO A 156 ? 0.3908 0.3320 0.5122 0.0944 0.0315 -0.0719 149 PRO A N 799 C CA . PRO A 156 ? 0.3888 0.3174 0.5128 0.0995 0.0289 -0.0700 149 PRO A CA 800 C C . PRO A 156 ? 0.4062 0.3244 0.5213 0.0973 0.0250 -0.0624 149 PRO A C 801 O O . PRO A 156 ? 0.3867 0.3092 0.4981 0.0966 0.0212 -0.0564 149 PRO A O 802 C CB . PRO A 156 ? 0.3950 0.3303 0.5309 0.1072 0.0255 -0.0689 149 PRO A CB 803 C CG . PRO A 156 ? 0.3832 0.3331 0.5267 0.1066 0.0298 -0.0743 149 PRO A CG 804 C CD . PRO A 156 ? 0.3844 0.3390 0.5171 0.0983 0.0319 -0.0737 149 PRO A CD 805 N N . GLY A 157 ? 0.4151 0.3194 0.5270 0.0962 0.0261 -0.0628 150 GLY A N 806 C CA . GLY A 157 ? 0.4531 0.3469 0.5579 0.0941 0.0236 -0.0553 150 GLY A CA 807 C C . GLY A 157 ? 0.4660 0.3602 0.5621 0.0854 0.0251 -0.0541 150 GLY A C 808 O O . GLY A 157 ? 0.4876 0.3724 0.5790 0.0829 0.0243 -0.0485 150 GLY A O 809 N N . TYR A 158 ? 0.4635 0.3681 0.5580 0.0810 0.0274 -0.0592 151 TYR A N 810 C CA . TYR A 158 ? 0.4778 0.3843 0.5647 0.0730 0.0285 -0.0592 151 TYR A CA 811 C C . TYR A 158 ? 0.5152 0.4189 0.6007 0.0694 0.0316 -0.0674 151 TYR A C 812 O O . TYR A 158 ? 0.5202 0.4271 0.5998 0.0632 0.0322 -0.0688 151 TYR A O 813 C CB . TYR A 158 ? 0.4474 0.3682 0.5318 0.0708 0.0282 -0.0584 151 TYR A CB 814 C CG . TYR A 158 ? 0.4106 0.3359 0.4943 0.0733 0.0245 -0.0511 151 TYR A CG 815 C CD1 . TYR A 158 ? 0.4048 0.3293 0.4814 0.0692 0.0230 -0.0452 151 TYR A CD1 816 C CD2 . TYR A 158 ? 0.3703 0.3006 0.4607 0.0799 0.0223 -0.0506 151 TYR A CD2 817 C CE1 . TYR A 158 ? 0.3734 0.3012 0.4475 0.0717 0.0197 -0.0390 151 TYR A CE1 818 C CE2 . TYR A 158 ? 0.3473 0.2812 0.4360 0.0823 0.0179 -0.0446 151 TYR A CE2 819 C CZ . TYR A 158 ? 0.3683 0.3005 0.4479 0.0783 0.0168 -0.0388 151 TYR A CZ 820 O OH . TYR A 158 ? 0.3574 0.2922 0.4336 0.0810 0.0125 -0.0333 151 TYR A OH 821 N N . GLU A 159 ? 0.5464 0.4447 0.6368 0.0737 0.0335 -0.0730 152 GLU A N 822 C CA . GLU A 159 ? 0.5856 0.4805 0.6733 0.0714 0.0363 -0.0816 152 GLU A CA 823 C C . GLU A 159 ? 0.6116 0.4948 0.6957 0.0658 0.0350 -0.0820 152 GLU A C 824 O O . GLU A 159 ? 0.6311 0.5113 0.7113 0.0628 0.0360 -0.0890 152 GLU A O 825 C CB . GLU A 159 ? 0.5991 0.4909 0.6930 0.0780 0.0391 -0.0882 152 GLU A CB 826 C CG . GLU A 159 ? 0.6186 0.5219 0.7202 0.0842 0.0403 -0.0876 152 GLU A CG 827 C CD . GLU A 159 ? 0.6213 0.5208 0.7308 0.0904 0.0368 -0.0817 152 GLU A CD 828 O OE1 . GLU A 159 ? 0.5902 0.4808 0.6971 0.0892 0.0336 -0.0756 152 GLU A OE1 829 O OE2 . GLU A 159 ? 0.6160 0.5213 0.7343 0.0968 0.0373 -0.0829 152 GLU A OE2 830 N N . ASN A 160 ? 0.6243 0.5010 0.7097 0.0644 0.0327 -0.0744 153 ASN A N 831 C CA . ASN A 160 ? 0.6327 0.4993 0.7171 0.0585 0.0316 -0.0737 153 ASN A CA 832 C C . ASN A 160 ? 0.6243 0.4964 0.7049 0.0528 0.0304 -0.0672 153 ASN A C 833 O O . ASN A 160 ? 0.6241 0.4891 0.7059 0.0481 0.0298 -0.0645 153 ASN A O 834 C CB . ASN A 160 ? 0.6493 0.5011 0.7395 0.0615 0.0313 -0.0707 153 ASN A CB 835 C CG . ASN A 160 ? 0.6670 0.5072 0.7589 0.0555 0.0308 -0.0720 153 ASN A CG 836 O OD1 . ASN A 160 ? 0.7034 0.5398 0.7951 0.0532 0.0307 -0.0805 153 ASN A OD1 837 N ND2 . ASN A 160 ? 0.6776 0.5119 0.7714 0.0532 0.0306 -0.0636 153 ASN A ND2 838 N N . VAL A 161 ? 0.6146 0.4994 0.6917 0.0531 0.0302 -0.0646 154 VAL A N 839 C CA . VAL A 161 ? 0.5995 0.4900 0.6726 0.0478 0.0292 -0.0596 154 VAL A CA 840 C C . VAL A 161 ? 0.6021 0.4950 0.6719 0.0416 0.0289 -0.0659 154 VAL A C 841 O O . VAL A 161 ? 0.6064 0.5034 0.6731 0.0422 0.0297 -0.0730 154 VAL A O 842 C CB . VAL A 161 ? 0.5929 0.4952 0.6632 0.0501 0.0286 -0.0547 154 VAL A CB 843 C CG1 . VAL A 161 ? 0.5706 0.4786 0.6365 0.0447 0.0278 -0.0500 154 VAL A CG1 844 C CG2 . VAL A 161 ? 0.6072 0.5053 0.6802 0.0565 0.0276 -0.0487 154 VAL A CG2 845 N N . SER A 162 ? 0.5997 0.4890 0.6702 0.0359 0.0278 -0.0634 155 SER A N 846 C CA . SER A 162 ? 0.6020 0.4942 0.6695 0.0303 0.0264 -0.0689 155 SER A CA 847 C C . SER A 162 ? 0.5722 0.4767 0.6347 0.0274 0.0257 -0.0654 155 SER A C 848 O O . SER A 162 ? 0.5582 0.4680 0.6201 0.0290 0.0263 -0.0581 155 SER A O 849 C CB . SER A 162 ? 0.6253 0.5071 0.6986 0.0253 0.0249 -0.0700 155 SER A CB 850 O OG . SER A 162 ? 0.6642 0.5439 0.7419 0.0234 0.0257 -0.0610 155 SER A OG 851 N N . ASP A 163 ? 0.5398 0.4483 0.5978 0.0236 0.0241 -0.0709 156 ASP A N 852 C CA . ASP A 163 ? 0.5007 0.4193 0.5543 0.0205 0.0231 -0.0682 156 ASP A CA 853 C C . ASP A 163 ? 0.4533 0.3818 0.5024 0.0242 0.0248 -0.0664 156 ASP A C 854 O O . ASP A 163 ? 0.4375 0.3733 0.4849 0.0231 0.0244 -0.0612 156 ASP A O 855 C CB . ASP A 163 ? 0.5202 0.4385 0.5786 0.0172 0.0226 -0.0605 156 ASP A CB 856 C CG . ASP A 163 ? 0.5953 0.5049 0.6606 0.0125 0.0211 -0.0622 156 ASP A CG 857 O OD1 . ASP A 163 ? 0.6681 0.5750 0.7325 0.0103 0.0186 -0.0699 156 ASP A OD1 858 O OD2 . ASP A 163 ? 0.6618 0.5667 0.7335 0.0112 0.0224 -0.0559 156 ASP A OD2 859 N N . ILE A 164 ? 0.4190 0.3474 0.4670 0.0287 0.0268 -0.0707 157 ILE A N 860 C CA . ILE A 164 ? 0.3783 0.3170 0.4230 0.0312 0.0286 -0.0704 157 ILE A CA 861 C C . ILE A 164 ? 0.3658 0.3084 0.4025 0.0281 0.0285 -0.0756 157 ILE A C 862 O O . ILE A 164 ? 0.3755 0.3130 0.4087 0.0284 0.0291 -0.0825 157 ILE A O 863 C CB . ILE A 164 ? 0.3742 0.3123 0.4227 0.0373 0.0313 -0.0729 157 ILE A CB 864 C CG1 . ILE A 164 ? 0.3603 0.2950 0.4157 0.0411 0.0305 -0.0669 157 ILE A CG1 865 C CG2 . ILE A 164 ? 0.3495 0.2987 0.3960 0.0392 0.0337 -0.0736 157 ILE A CG2 866 C CD1 . ILE A 164 ? 0.3258 0.2575 0.3869 0.0475 0.0324 -0.0698 157 ILE A CD1 867 N N . VAL A 165 ? 0.3373 0.2880 0.3703 0.0254 0.0275 -0.0722 158 VAL A N 868 C CA . VAL A 165 ? 0.3265 0.2806 0.3508 0.0229 0.0273 -0.0764 158 VAL A CA 869 C C . VAL A 165 ? 0.3232 0.2804 0.3438 0.0266 0.0316 -0.0804 158 VAL A C 870 O O . VAL A 165 ? 0.3164 0.2799 0.3411 0.0294 0.0340 -0.0774 158 VAL A O 871 C CB . VAL A 165 ? 0.3126 0.2745 0.3339 0.0193 0.0253 -0.0715 158 VAL A CB 872 C CG1 . VAL A 165 ? 0.2921 0.2635 0.3138 0.0216 0.0277 -0.0674 158 VAL A CG1 873 C CG2 . VAL A 165 ? 0.3332 0.2950 0.3456 0.0162 0.0234 -0.0759 158 VAL A CG2 874 N N . PRO A 166 ? 0.3302 0.2829 0.3432 0.0267 0.0326 -0.0875 159 PRO A N 875 C CA . PRO A 166 ? 0.3424 0.2981 0.3514 0.0304 0.0381 -0.0912 159 PRO A CA 876 C C . PRO A 166 ? 0.3409 0.3064 0.3458 0.0292 0.0400 -0.0877 159 PRO A C 877 O O . PRO A 166 ? 0.3260 0.2943 0.3276 0.0254 0.0365 -0.0844 159 PRO A O 878 C CB . PRO A 166 ? 0.3577 0.3052 0.3562 0.0303 0.0382 -0.0994 159 PRO A CB 879 C CG . PRO A 166 ? 0.3595 0.3025 0.3556 0.0257 0.0318 -0.0995 159 PRO A CG 880 C CD . PRO A 166 ? 0.3386 0.2831 0.3464 0.0238 0.0289 -0.0926 159 PRO A CD 881 N N . PRO A 167 ? 0.3302 0.3008 0.3359 0.0325 0.0458 -0.0887 160 PRO A N 882 C CA . PRO A 167 ? 0.3287 0.3079 0.3309 0.0310 0.0480 -0.0855 160 PRO A CA 883 C C . PRO A 167 ? 0.3232 0.3001 0.3110 0.0277 0.0465 -0.0873 160 PRO A C 884 O O . PRO A 167 ? 0.3318 0.3015 0.3098 0.0283 0.0470 -0.0931 160 PRO A O 885 C CB . PRO A 167 ? 0.3290 0.3118 0.3342 0.0350 0.0555 -0.0880 160 PRO A CB 886 C CG . PRO A 167 ? 0.3392 0.3183 0.3554 0.0391 0.0555 -0.0898 160 PRO A CG 887 C CD . PRO A 167 ? 0.3380 0.3068 0.3489 0.0375 0.0508 -0.0926 160 PRO A CD 888 N N . PHE A 168 ? 0.3172 0.2998 0.3033 0.0247 0.0444 -0.0824 161 PHE A N 889 C CA . PHE A 168 ? 0.3229 0.3043 0.2958 0.0219 0.0427 -0.0832 161 PHE A CA 890 C C . PHE A 168 ? 0.3019 0.2913 0.2760 0.0197 0.0423 -0.0770 161 PHE A C 891 O O . PHE A 168 ? 0.2811 0.2762 0.2663 0.0199 0.0419 -0.0725 161 PHE A O 892 C CB . PHE A 168 ? 0.3201 0.2948 0.2894 0.0192 0.0357 -0.0852 161 PHE A CB 893 C CG . PHE A 168 ? 0.3338 0.3121 0.3113 0.0161 0.0305 -0.0796 161 PHE A CG 894 C CD1 . PHE A 168 ? 0.3046 0.2839 0.2766 0.0127 0.0258 -0.0780 161 PHE A CD1 895 C CD2 . PHE A 168 ? 0.3124 0.2921 0.3025 0.0170 0.0302 -0.0761 161 PHE A CD2 896 C CE1 . PHE A 168 ? 0.2717 0.2540 0.2512 0.0101 0.0218 -0.0731 161 PHE A CE1 897 C CE2 . PHE A 168 ? 0.3080 0.2899 0.3039 0.0145 0.0262 -0.0709 161 PHE A CE2 898 C CZ . PHE A 168 ? 0.2927 0.2762 0.2838 0.0109 0.0223 -0.0695 161 PHE A CZ 899 N N . SER A 169 ? 0.3046 0.2938 0.2667 0.0182 0.0426 -0.0771 162 SER A N 900 C CA . SER A 169 ? 0.2831 0.2786 0.2450 0.0158 0.0416 -0.0715 162 SER A CA 901 C C . SER A 169 ? 0.2919 0.2857 0.2511 0.0127 0.0341 -0.0702 162 SER A C 902 O O . SER A 169 ? 0.3080 0.2967 0.2560 0.0118 0.0313 -0.0732 162 SER A O 903 C CB . SER A 169 ? 0.3195 0.3156 0.2703 0.0162 0.0469 -0.0716 162 SER A CB 904 O OG . SER A 169 ? 0.3017 0.3006 0.2579 0.0191 0.0547 -0.0725 162 SER A OG 905 N N . ALA A 170 ? 0.2673 0.2654 0.2364 0.0113 0.0309 -0.0656 163 ALA A N 906 C CA . ALA A 170 ? 0.2723 0.2692 0.2412 0.0084 0.0244 -0.0642 163 ALA A CA 907 C C . ALA A 170 ? 0.2848 0.2831 0.2438 0.0067 0.0226 -0.0628 163 ALA A C 908 O O . ALA A 170 ? 0.2699 0.2727 0.2275 0.0068 0.0256 -0.0596 163 ALA A O 909 C CB . ALA A 170 ? 0.2570 0.2578 0.2375 0.0078 0.0225 -0.0594 163 ALA A CB 910 N N . PHE A 171 ? 0.2936 0.2876 0.2467 0.0051 0.0174 -0.0655 164 PHE A N 911 C CA . PHE A 171 ? 0.3101 0.3038 0.2531 0.0037 0.0137 -0.0650 164 PHE A CA 912 C C . PHE A 171 ? 0.3223 0.3113 0.2492 0.0054 0.0163 -0.0683 164 PHE A C 913 O O . PHE A 171 ? 0.3297 0.3173 0.2461 0.0049 0.0133 -0.0678 164 PHE A O 914 C CB . PHE A 171 ? 0.2867 0.2869 0.2334 0.0024 0.0132 -0.0588 164 PHE A CB 915 C CG . PHE A 171 ? 0.3126 0.3164 0.2722 0.0010 0.0103 -0.0556 164 PHE A CG 916 C CD1 . PHE A 171 ? 0.2740 0.2768 0.2365 -0.0010 0.0043 -0.0561 164 PHE A CD1 917 C CD2 . PHE A 171 ? 0.2672 0.2749 0.2363 0.0020 0.0137 -0.0523 164 PHE A CD2 918 C CE1 . PHE A 171 ? 0.2808 0.2866 0.2550 -0.0022 0.0028 -0.0529 164 PHE A CE1 919 C CE2 . PHE A 171 ? 0.2655 0.2753 0.2443 0.0012 0.0116 -0.0492 164 PHE A CE2 920 C CZ . PHE A 171 ? 0.2644 0.2733 0.2458 -0.0009 0.0067 -0.0492 164 PHE A CZ 921 N N . SER A 172 ? 0.3397 0.3256 0.2638 0.0079 0.0219 -0.0718 165 SER A N 922 C CA . SER A 172 ? 0.3647 0.3442 0.2716 0.0099 0.0242 -0.0759 165 SER A CA 923 C C . SER A 172 ? 0.3791 0.3519 0.2759 0.0092 0.0160 -0.0805 165 SER A C 924 O O . SER A 172 ? 0.3762 0.3471 0.2808 0.0079 0.0104 -0.0834 165 SER A O 925 C CB . SER A 172 ? 0.3731 0.3491 0.2791 0.0130 0.0307 -0.0804 165 SER A CB 926 O OG . SER A 172 ? 0.3967 0.3656 0.2841 0.0153 0.0332 -0.0846 165 SER A OG 927 N N . PRO A 173 ? 0.3920 0.3608 0.2715 0.0102 0.0150 -0.0810 166 PRO A N 928 C CA . PRO A 173 ? 0.4118 0.3730 0.2800 0.0105 0.0072 -0.0867 166 PRO A CA 929 C C . PRO A 173 ? 0.4367 0.3899 0.2976 0.0132 0.0093 -0.0942 166 PRO A C 930 O O . PRO A 173 ? 0.4239 0.3770 0.2847 0.0155 0.0182 -0.0947 166 PRO A O 931 C CB . PRO A 173 ? 0.4404 0.3988 0.2901 0.0118 0.0067 -0.0847 166 PRO A CB 932 C CG . PRO A 173 ? 0.4224 0.3833 0.2693 0.0133 0.0178 -0.0807 166 PRO A CG 933 C CD . PRO A 173 ? 0.3924 0.3626 0.2616 0.0112 0.0205 -0.0766 166 PRO A CD 934 N N . GLN A 174 ? 0.4437 0.3902 0.2992 0.0131 0.0009 -0.1004 167 GLN A N 935 C CA . GLN A 174 ? 0.4745 0.4113 0.3189 0.0161 0.0015 -0.1086 167 GLN A CA 936 C C . GLN A 174 ? 0.4983 0.4285 0.3183 0.0201 0.0059 -0.1103 167 GLN A C 937 O O . GLN A 174 ? 0.5167 0.4472 0.3255 0.0201 0.0043 -0.1066 167 GLN A O 938 C CB . GLN A 174 ? 0.4830 0.4142 0.3289 0.0146 -0.0097 -0.1150 167 GLN A CB 939 C CG . GLN A 174 ? 0.4985 0.4356 0.3693 0.0105 -0.0132 -0.1131 167 GLN A CG 940 C CD . GLN A 174 ? 0.5869 0.5195 0.4626 0.0083 -0.0244 -0.1189 167 GLN A CD 941 O OE1 . GLN A 174 ? 0.6407 0.5664 0.5016 0.0097 -0.0311 -0.1244 167 GLN A OE1 942 N NE2 . GLN A 174 ? 0.5906 0.5267 0.4873 0.0049 -0.0265 -0.1176 167 GLN A NE2 943 N N . GLY A 175 ? 0.5204 0.4439 0.3314 0.0236 0.0118 -0.1158 168 GLY A N 944 C CA . GLY A 175 ? 0.5439 0.4588 0.3291 0.0280 0.0157 -0.1186 168 GLY A CA 945 C C . GLY A 175 ? 0.5629 0.4727 0.3439 0.0318 0.0244 -0.1238 168 GLY A C 946 O O . GLY A 175 ? 0.5562 0.4705 0.3557 0.0310 0.0283 -0.1239 168 GLY A O 947 N N . MET A 176 ? 0.5897 0.4894 0.3457 0.0363 0.0274 -0.1284 169 MET A N 948 C CA . MET A 176 ? 0.6026 0.4971 0.3520 0.0407 0.0374 -0.1331 169 MET A CA 949 C C . MET A 176 ? 0.6168 0.5084 0.3459 0.0446 0.0487 -0.1301 169 MET A C 950 O O . MET A 176 ? 0.6442 0.5248 0.3512 0.0496 0.0524 -0.1361 169 MET A O 951 C CB . MET A 176 ? 0.6359 0.5187 0.3758 0.0432 0.0303 -0.1440 169 MET A CB 952 C CG . MET A 176 ? 0.6795 0.5652 0.4434 0.0398 0.0236 -0.1469 169 MET A CG 953 S SD . MET A 176 ? 0.9041 0.7748 0.6569 0.0425 0.0148 -0.1603 169 MET A SD 954 C CE . MET A 176 ? 0.8356 0.7102 0.6176 0.0404 0.0163 -0.1616 169 MET A CE 955 N N . PRO A 177 ? 0.5979 0.4985 0.3338 0.0425 0.0550 -0.1208 170 PRO A N 956 C CA . PRO A 177 ? 0.6176 0.5148 0.3345 0.0457 0.0659 -0.1173 170 PRO A CA 957 C C . PRO A 177 ? 0.6400 0.5352 0.3549 0.0500 0.0800 -0.1203 170 PRO A C 958 O O . PRO A 177 ? 0.6154 0.5174 0.3520 0.0493 0.0837 -0.1212 170 PRO A O 959 C CB . PRO A 177 ? 0.5973 0.5059 0.3286 0.0416 0.0688 -0.1070 170 PRO A CB 960 C CG . PRO A 177 ? 0.5628 0.4821 0.3242 0.0378 0.0657 -0.1059 170 PRO A CG 961 C CD . PRO A 177 ? 0.5698 0.4836 0.3317 0.0375 0.0538 -0.1135 170 PRO A CD 962 N N . GLU A 178 ? 0.6683 0.5538 0.3567 0.0547 0.0875 -0.1217 171 GLU A N 963 C CA . GLU A 178 ? 0.6928 0.5744 0.3736 0.0598 0.1020 -0.1248 171 GLU A CA 964 C C . GLU A 178 ? 0.7038 0.5865 0.3742 0.0607 0.1146 -0.1168 171 GLU A C 965 O O . GLU A 178 ? 0.7281 0.6049 0.3787 0.0607 0.1109 -0.1134 171 GLU A O 966 C CB . GLU A 178 ? 0.7242 0.5898 0.3763 0.0655 0.0993 -0.1343 171 GLU A CB 967 C CG A GLU A 178 ? 0.7242 0.5858 0.3836 0.0668 0.0934 -0.1440 171 GLU A CG 968 C CD A GLU A 178 ? 0.7537 0.5986 0.3822 0.0728 0.0913 -0.1535 171 GLU A CD 969 O OE1 A GLU A 178 ? 0.7812 0.6195 0.4058 0.0723 0.0771 -0.1606 171 GLU A OE1 970 O OE2 A GLU A 178 ? 0.7489 0.5871 0.3569 0.0781 0.1038 -0.1539 171 GLU A OE2 971 N N . GLY A 179 ? 0.6893 0.5792 0.3733 0.0615 0.1293 -0.1138 172 GLY A N 972 C CA . GLY A 179 ? 0.6924 0.5839 0.3696 0.0617 0.1420 -0.1056 172 GLY A CA 973 C C . GLY A 179 ? 0.6783 0.5787 0.3744 0.0625 0.1581 -0.1033 172 GLY A C 974 O O . GLY A 179 ? 0.6713 0.5756 0.3837 0.0638 0.1596 -0.1085 172 GLY A O 975 N N . ASP A 180 ? 0.6741 0.5777 0.3695 0.0616 0.1699 -0.0953 173 ASP A N 976 C CA . ASP A 180 ? 0.6668 0.5801 0.3828 0.0619 0.1858 -0.0923 173 ASP A CA 977 C C . ASP A 180 ? 0.6249 0.5540 0.3745 0.0558 0.1824 -0.0862 173 ASP A C 978 O O . ASP A 180 ? 0.6162 0.5474 0.3667 0.0514 0.1735 -0.0808 173 ASP A O 979 C CB . ASP A 180 ? 0.6857 0.5940 0.3844 0.0640 0.2014 -0.0866 173 ASP A CB 980 C CG . ASP A 180 ? 0.7455 0.6378 0.4098 0.0711 0.2078 -0.0924 173 ASP A CG 981 O OD1 . ASP A 180 ? 0.7635 0.6529 0.4277 0.0752 0.2089 -0.1008 173 ASP A OD1 982 O OD2 . ASP A 180 ? 0.7721 0.6541 0.4088 0.0728 0.2117 -0.0883 173 ASP A OD2 983 N N . LEU A 181 ? 0.5972 0.5369 0.3737 0.0558 0.1894 -0.0871 174 LEU A N 984 C CA . LEU A 181 ? 0.5671 0.5215 0.3757 0.0507 0.1859 -0.0823 174 LEU A CA 985 C C . LEU A 181 ? 0.5683 0.5293 0.3855 0.0478 0.1963 -0.0736 174 LEU A C 986 O O . LEU A 181 ? 0.5819 0.5401 0.3913 0.0504 0.2114 -0.0720 174 LEU A O 987 C CB . LEU A 181 ? 0.5553 0.5181 0.3891 0.0525 0.1886 -0.0869 174 LEU A CB 988 C CG A LEU A 181 ? 0.5176 0.4901 0.3783 0.0499 0.1773 -0.0880 174 LEU A CG 989 C CG B LEU A 181 ? 0.5219 0.4818 0.3582 0.0541 0.1770 -0.0945 174 LEU A CG 990 C CD1 A LEU A 181 ? 0.4967 0.4650 0.3498 0.0471 0.1605 -0.0890 174 LEU A CD1 991 C CD1 B LEU A 181 ? 0.4694 0.4386 0.3327 0.0560 0.1819 -0.0973 174 LEU A CD1 992 C CD2 A LEU A 181 ? 0.4873 0.4607 0.3588 0.0545 0.1812 -0.0951 174 LEU A CD2 993 C CD2 B LEU A 181 ? 0.4952 0.4569 0.3361 0.0494 0.1606 -0.0925 174 LEU A CD2 994 N N . VAL A 182 ? 0.5478 0.5170 0.3812 0.0423 0.1883 -0.0680 175 VAL A N 995 C CA . VAL A 182 ? 0.5336 0.5123 0.3859 0.0389 0.1969 -0.0607 175 VAL A CA 996 C C . VAL A 182 ? 0.5067 0.4993 0.3922 0.0354 0.1891 -0.0602 175 VAL A C 997 O O . VAL A 182 ? 0.4927 0.4861 0.3811 0.0334 0.1748 -0.0614 175 VAL A O 998 C CB . VAL A 182 ? 0.5528 0.5265 0.3899 0.0357 0.1962 -0.0531 175 VAL A CB 999 C CG1 . VAL A 182 ? 0.5125 0.4972 0.3742 0.0310 0.2015 -0.0459 175 VAL A CG1 1000 C CG2 . VAL A 182 ? 0.5604 0.5212 0.3668 0.0396 0.2071 -0.0524 175 VAL A CG2 1001 N N . TYR A 183 ? 0.4934 0.4965 0.4037 0.0349 0.1989 -0.0586 176 TYR A N 1002 C CA . TYR A 183 ? 0.4619 0.4779 0.4036 0.0325 0.1926 -0.0585 176 TYR A CA 1003 C C . TYR A 183 ? 0.4514 0.4736 0.4049 0.0271 0.1911 -0.0511 176 TYR A C 1004 O O . TYR A 183 ? 0.4522 0.4751 0.4066 0.0257 0.2026 -0.0463 176 TYR A O 1005 C CB . TYR A 183 ? 0.4659 0.4902 0.4297 0.0356 0.2027 -0.0618 176 TYR A CB 1006 C CG . TYR A 183 ? 0.4214 0.4598 0.4192 0.0332 0.1978 -0.0606 176 TYR A CG 1007 C CD1 . TYR A 183 ? 0.3923 0.4334 0.3990 0.0328 0.1833 -0.0631 176 TYR A CD1 1008 C CD2 . TYR A 183 ? 0.4089 0.4575 0.4300 0.0314 0.2078 -0.0571 176 TYR A CD2 1009 C CE1 . TYR A 183 ? 0.3972 0.4506 0.4336 0.0309 0.1780 -0.0619 176 TYR A CE1 1010 C CE2 . TYR A 183 ? 0.3887 0.4500 0.4410 0.0294 0.2022 -0.0565 176 TYR A CE2 1011 C CZ . TYR A 183 ? 0.3878 0.4512 0.4466 0.0294 0.1870 -0.0589 176 TYR A CZ 1012 O OH . TYR A 183 ? 0.3602 0.4352 0.4476 0.0280 0.1809 -0.0585 176 TYR A OH 1013 N N . VAL A 184 ? 0.4286 0.4547 0.3910 0.0240 0.1772 -0.0501 177 VAL A N 1014 C CA . VAL A 184 ? 0.4247 0.4539 0.3927 0.0191 0.1734 -0.0437 177 VAL A CA 1015 C C . VAL A 184 ? 0.3962 0.4381 0.3954 0.0166 0.1679 -0.0430 177 VAL A C 1016 O O . VAL A 184 ? 0.3906 0.4349 0.3951 0.0129 0.1599 -0.0394 177 VAL A O 1017 C CB . VAL A 184 ? 0.4253 0.4460 0.3716 0.0176 0.1613 -0.0425 177 VAL A CB 1018 C CG1 . VAL A 184 ? 0.4511 0.4588 0.3663 0.0204 0.1657 -0.0434 177 VAL A CG1 1019 C CG2 . VAL A 184 ? 0.4204 0.4425 0.3713 0.0183 0.1476 -0.0470 177 VAL A CG2 1020 N N . ASN A 185 ? 0.3944 0.4441 0.4138 0.0190 0.1719 -0.0467 178 ASN A N 1021 C CA . ASN A 185 ? 0.3689 0.4304 0.4177 0.0175 0.1661 -0.0467 178 ASN A CA 1022 C C . ASN A 185 ? 0.3562 0.4167 0.4028 0.0167 0.1498 -0.0476 178 ASN A C 1023 O O . ASN A 185 ? 0.3524 0.4072 0.3867 0.0194 0.1444 -0.0516 178 ASN A O 1024 C CB . ASN A 185 ? 0.3689 0.4373 0.4346 0.0134 0.1720 -0.0414 178 ASN A CB 1025 C CG . ASN A 185 ? 0.3736 0.4554 0.4733 0.0129 0.1698 -0.0426 178 ASN A CG 1026 O OD1 . ASN A 185 ? 0.3676 0.4540 0.4794 0.0165 0.1684 -0.0473 178 ASN A OD1 1027 N ND2 . ASN A 185 ? 0.3490 0.4365 0.4642 0.0085 0.1689 -0.0385 178 ASN A ND2 1028 N N . TYR A 186 ? 0.3450 0.4105 0.4029 0.0131 0.1424 -0.0441 179 TYR A N 1029 C CA . TYR A 186 ? 0.3245 0.3889 0.3797 0.0124 0.1282 -0.0445 179 TYR A CA 1030 C C . TYR A 186 ? 0.3255 0.3809 0.3572 0.0103 0.1231 -0.0419 179 TYR A C 1031 O O . TYR A 186 ? 0.3125 0.3672 0.3424 0.0093 0.1118 -0.0414 179 TYR A O 1032 C CB . TYR A 186 ? 0.3142 0.3875 0.3917 0.0101 0.1215 -0.0426 179 TYR A CB 1033 C CG . TYR A 186 ? 0.3071 0.3899 0.4098 0.0124 0.1229 -0.0456 179 TYR A CG 1034 C CD1 . TYR A 186 ? 0.2726 0.3563 0.3800 0.0160 0.1154 -0.0495 179 TYR A CD1 1035 C CD2 . TYR A 186 ? 0.3017 0.3926 0.4247 0.0111 0.1313 -0.0444 179 TYR A CD2 1036 C CE1 . TYR A 186 ? 0.3030 0.3955 0.4342 0.0187 0.1156 -0.0522 179 TYR A CE1 1037 C CE2 . TYR A 186 ? 0.2975 0.3979 0.4457 0.0135 0.1316 -0.0475 179 TYR A CE2 1038 C CZ . TYR A 186 ? 0.3027 0.4038 0.4544 0.0175 0.1234 -0.0514 179 TYR A CZ 1039 O OH . TYR A 186 ? 0.3170 0.4271 0.4933 0.0204 0.1229 -0.0544 179 TYR A OH 1040 N N . ALA A 187 ? 0.3307 0.3794 0.3449 0.0100 0.1313 -0.0400 180 ALA A N 1041 C CA . ALA A 187 ? 0.3420 0.3819 0.3336 0.0084 0.1266 -0.0373 180 ALA A CA 1042 C C . ALA A 187 ? 0.3387 0.3813 0.3366 0.0046 0.1194 -0.0327 180 ALA A C 1043 O O . ALA A 187 ? 0.3373 0.3750 0.3223 0.0037 0.1106 -0.0318 180 ALA A O 1044 C CB . ALA A 187 ? 0.3284 0.3614 0.3037 0.0107 0.1182 -0.0414 180 ALA A CB 1045 N N . ARG A 188 ? 0.3301 0.3807 0.3488 0.0024 0.1226 -0.0304 181 ARG A N 1046 C CA . ARG A 188 ? 0.3142 0.3670 0.3400 -0.0012 0.1169 -0.0263 181 ARG A CA 1047 C C . ARG A 188 ? 0.3341 0.3800 0.3450 -0.0034 0.1229 -0.0211 181 ARG A C 1048 O O . ARG A 188 ? 0.3414 0.3823 0.3406 -0.0023 0.1332 -0.0203 181 ARG A O 1049 C CB . ARG A 188 ? 0.3143 0.3775 0.3681 -0.0026 0.1180 -0.0263 181 ARG A CB 1050 C CG . ARG A 188 ? 0.2808 0.3505 0.3493 -0.0001 0.1104 -0.0309 181 ARG A CG 1051 C CD . ARG A 188 ? 0.2934 0.3731 0.3892 -0.0007 0.1128 -0.0316 181 ARG A CD 1052 N NE . ARG A 188 ? 0.2793 0.3612 0.3815 -0.0004 0.1266 -0.0315 181 ARG A NE 1053 C CZ . ARG A 188 ? 0.3354 0.4264 0.4626 -0.0010 0.1318 -0.0320 181 ARG A CZ 1054 N NH1 . ARG A 188 ? 0.3315 0.4304 0.4800 -0.0019 0.1236 -0.0331 181 ARG A NH1 1055 N NH2 . ARG A 188 ? 0.2990 0.3913 0.4299 -0.0006 0.1455 -0.0316 181 ARG A NH2 1056 N N . THR A 189 ? 0.3226 0.3671 0.3324 -0.0061 0.1163 -0.0176 182 THR A N 1057 C CA . THR A 189 ? 0.3372 0.3753 0.3356 -0.0083 0.1214 -0.0121 182 THR A CA 1058 C C . THR A 189 ? 0.3494 0.3894 0.3571 -0.0096 0.1356 -0.0096 182 THR A C 1059 O O . THR A 189 ? 0.3588 0.3912 0.3496 -0.0089 0.1447 -0.0067 182 THR A O 1060 C CB . THR A 189 ? 0.3376 0.3764 0.3416 -0.0113 0.1131 -0.0090 182 THR A CB 1061 O OG1 . THR A 189 ? 0.3157 0.3521 0.3094 -0.0099 0.1016 -0.0111 182 THR A OG1 1062 C CG2 . THR A 189 ? 0.3599 0.3910 0.3520 -0.0135 0.1186 -0.0028 182 THR A CG2 1063 N N . GLU A 190 ? 0.3481 0.3980 0.3825 -0.0112 0.1375 -0.0105 183 GLU A N 1064 C CA . GLU A 190 ? 0.3738 0.4267 0.4210 -0.0127 0.1514 -0.0081 183 GLU A CA 1065 C C . GLU A 190 ? 0.3838 0.4353 0.4236 -0.0092 0.1624 -0.0105 183 GLU A C 1066 O O . GLU A 190 ? 0.3891 0.4389 0.4286 -0.0098 0.1762 -0.0073 183 GLU A O 1067 C CB . GLU A 190 ? 0.3689 0.4333 0.4485 -0.0152 0.1494 -0.0092 183 GLU A CB 1068 C CG . GLU A 190 ? 0.3922 0.4652 0.4868 -0.0124 0.1428 -0.0154 183 GLU A CG 1069 C CD . GLU A 190 ? 0.4307 0.5053 0.5273 -0.0121 0.1270 -0.0176 183 GLU A CD 1070 O OE1 . GLU A 190 ? 0.4269 0.4944 0.5051 -0.0125 0.1199 -0.0158 183 GLU A OE1 1071 O OE2 . GLU A 190 ? 0.3979 0.4810 0.5149 -0.0111 0.1219 -0.0212 183 GLU A OE2 1072 N N . ASP A 191 ? 0.3746 0.4260 0.4074 -0.0054 0.1572 -0.0159 184 ASP A N 1073 C CA . ASP A 191 ? 0.3876 0.4371 0.4130 -0.0015 0.1677 -0.0190 184 ASP A CA 1074 C C . ASP A 191 ? 0.4070 0.4437 0.4012 -0.0002 0.1734 -0.0162 184 ASP A C 1075 O O . ASP A 191 ? 0.3932 0.4261 0.3795 0.0013 0.1868 -0.0151 184 ASP A O 1076 C CB . ASP A 191 ? 0.3795 0.4312 0.4056 0.0021 0.1600 -0.0256 184 ASP A CB 1077 C CG . ASP A 191 ? 0.3646 0.4281 0.4200 0.0018 0.1547 -0.0284 184 ASP A CG 1078 O OD1 . ASP A 191 ? 0.3679 0.4393 0.4453 0.0003 0.1623 -0.0271 184 ASP A OD1 1079 O OD2 . ASP A 191 ? 0.3290 0.3938 0.3857 0.0033 0.1432 -0.0318 184 ASP A OD2 1080 N N . PHE A 192 ? 0.4033 0.4328 0.3790 -0.0007 0.1629 -0.0151 185 PHE A N 1081 C CA . PHE A 192 ? 0.4213 0.4381 0.3665 0.0007 0.1659 -0.0125 185 PHE A CA 1082 C C . PHE A 192 ? 0.4393 0.4521 0.3814 -0.0019 0.1755 -0.0051 185 PHE A C 1083 O O . PHE A 192 ? 0.4575 0.4609 0.3784 0.0000 0.1849 -0.0027 185 PHE A O 1084 C CB . PHE A 192 ? 0.4158 0.4270 0.3445 0.0013 0.1514 -0.0138 185 PHE A CB 1085 C CG . PHE A 192 ? 0.4017 0.4119 0.3233 0.0048 0.1453 -0.0206 185 PHE A CG 1086 C CD1 . PHE A 192 ? 0.4083 0.4254 0.3449 0.0044 0.1347 -0.0243 185 PHE A CD1 1087 C CD2 . PHE A 192 ? 0.4330 0.4344 0.3324 0.0087 0.1507 -0.0234 185 PHE A CD2 1088 C CE1 . PHE A 192 ? 0.4219 0.4374 0.3526 0.0075 0.1294 -0.0305 185 PHE A CE1 1089 C CE2 . PHE A 192 ? 0.4146 0.4145 0.3085 0.0119 0.1452 -0.0302 185 PHE A CE2 1090 C CZ . PHE A 192 ? 0.4249 0.4319 0.3352 0.0111 0.1344 -0.0336 185 PHE A CZ 1091 N N . PHE A 193 ? 0.4415 0.4606 0.4043 -0.0062 0.1734 -0.0015 186 PHE A N 1092 C CA . PHE A 193 ? 0.4731 0.4890 0.4378 -0.0094 0.1839 0.0056 186 PHE A CA 1093 C C . PHE A 193 ? 0.4931 0.5107 0.4638 -0.0083 0.2012 0.0062 186 PHE A C 1094 O O . PHE A 193 ? 0.5211 0.5302 0.4764 -0.0080 0.2132 0.0114 186 PHE A O 1095 C CB . PHE A 193 ? 0.4451 0.4692 0.4366 -0.0144 0.1793 0.0081 186 PHE A CB 1096 C CG . PHE A 193 ? 0.4492 0.4694 0.4333 -0.0160 0.1659 0.0099 186 PHE A CG 1097 C CD1 . PHE A 193 ? 0.4665 0.4759 0.4217 -0.0137 0.1606 0.0112 186 PHE A CD1 1098 C CD2 . PHE A 193 ? 0.4273 0.4547 0.4341 -0.0196 0.1585 0.0103 186 PHE A CD2 1099 C CE1 . PHE A 193 ? 0.4397 0.4462 0.3900 -0.0150 0.1485 0.0128 186 PHE A CE1 1100 C CE2 . PHE A 193 ? 0.3978 0.4217 0.3985 -0.0208 0.1469 0.0119 186 PHE A CE2 1101 C CZ . PHE A 193 ? 0.4073 0.4209 0.3801 -0.0185 0.1422 0.0132 186 PHE A CZ 1102 N N . LYS A 194 ? 0.4853 0.5140 0.4790 -0.0076 0.2028 0.0012 187 LYS A N 1103 C CA . LYS A 194 ? 0.4964 0.5294 0.5022 -0.0066 0.2192 0.0010 187 LYS A CA 1104 C C . LYS A 194 ? 0.5268 0.5494 0.5036 -0.0016 0.2286 0.0000 187 LYS A C 1105 O O . LYS A 194 ? 0.5480 0.5667 0.5198 -0.0011 0.2448 0.0039 187 LYS A O 1106 C CB . LYS A 194 ? 0.4778 0.5248 0.5137 -0.0060 0.2161 -0.0049 187 LYS A CB 1107 C CG . LYS A 194 ? 0.5142 0.5672 0.5650 -0.0039 0.2321 -0.0067 187 LYS A CG 1108 C CD . LYS A 194 ? 0.5829 0.6417 0.6567 -0.0081 0.2447 -0.0014 187 LYS A CD 1109 C CE . LYS A 194 ? 0.5953 0.6664 0.7032 -0.0125 0.2351 -0.0021 187 LYS A CE 1110 N NZ . LYS A 194 ? 0.6638 0.7392 0.7934 -0.0173 0.2473 0.0034 187 LYS A NZ 1111 N N . LEU A 195 ? 0.5279 0.5454 0.4853 0.0021 0.2187 -0.0051 188 LEU A N 1112 C CA . LEU A 195 ? 0.5599 0.5660 0.4866 0.0072 0.2240 -0.0073 188 LEU A CA 1113 C C . LEU A 195 ? 0.5884 0.5805 0.4855 0.0075 0.2291 -0.0010 188 LEU A C 1114 O O . LEU A 195 ? 0.5963 0.5816 0.4789 0.0101 0.2438 0.0009 188 LEU A O 1115 C CB . LEU A 195 ? 0.5539 0.5574 0.4680 0.0102 0.2095 -0.0141 188 LEU A CB 1116 C CG . LEU A 195 ? 0.5572 0.5688 0.4874 0.0129 0.2079 -0.0216 188 LEU A CG 1117 C CD1 . LEU A 195 ? 0.5711 0.5804 0.4924 0.0143 0.1918 -0.0269 188 LEU A CD1 1118 C CD2 . LEU A 195 ? 0.5407 0.5483 0.4611 0.0175 0.2223 -0.0244 188 LEU A CD2 1119 N N . GLU A 196 ? 0.5790 0.5666 0.4666 0.0053 0.2172 0.0020 189 GLU A N 1120 C CA A GLU A 196 ? 0.6103 0.5837 0.4673 0.0064 0.2190 0.0074 189 GLU A CA 1121 C CA B GLU A 196 ? 0.6110 0.5841 0.4677 0.0063 0.2190 0.0076 189 GLU A CA 1122 C C . GLU A 196 ? 0.6240 0.5951 0.4860 0.0030 0.2321 0.0164 189 GLU A C 1123 O O . GLU A 196 ? 0.6538 0.6134 0.4925 0.0054 0.2437 0.0208 189 GLU A O 1124 C CB A GLU A 196 ? 0.6062 0.5762 0.4529 0.0057 0.2008 0.0068 189 GLU A CB 1125 C CB B GLU A 196 ? 0.6094 0.5784 0.4548 0.0054 0.2015 0.0079 189 GLU A CB 1126 C CG A GLU A 196 ? 0.6159 0.5816 0.4444 0.0100 0.1908 -0.0005 189 GLU A CG 1127 C CG B GLU A 196 ? 0.6388 0.5934 0.4556 0.0061 0.2028 0.0148 189 GLU A CG 1128 C CD A GLU A 196 ? 0.6053 0.5791 0.4491 0.0084 0.1746 -0.0051 189 GLU A CD 1129 C CD B GLU A 196 ? 0.6496 0.6011 0.4584 0.0052 0.1859 0.0153 189 GLU A CD 1130 O OE1 A GLU A 196 ? 0.5751 0.5595 0.4419 0.0078 0.1742 -0.0095 189 GLU A OE1 1131 O OE1 B GLU A 196 ? 0.6668 0.6173 0.4660 0.0078 0.1742 0.0093 189 GLU A OE1 1132 O OE2 A GLU A 196 ? 0.6230 0.5925 0.4559 0.0079 0.1625 -0.0043 189 GLU A OE2 1133 O OE2 B GLU A 196 ? 0.6261 0.5761 0.4390 0.0020 0.1845 0.0217 189 GLU A OE2 1134 N N . ARG A 197 ? 0.6079 0.5892 0.4999 -0.0022 0.2301 0.0189 190 ARG A N 1135 C CA . ARG A 197 ? 0.6199 0.5993 0.5200 -0.0063 0.2404 0.0274 190 ARG A CA 1136 C C . ARG A 197 ? 0.6272 0.6113 0.5433 -0.0069 0.2596 0.0293 190 ARG A C 1137 O O . ARG A 197 ? 0.6559 0.6311 0.5596 -0.0070 0.2737 0.0364 190 ARG A O 1138 C CB . ARG A 197 ? 0.5806 0.5677 0.5053 -0.0118 0.2296 0.0292 190 ARG A CB 1139 C CG . ARG A 197 ? 0.5830 0.5646 0.4918 -0.0114 0.2121 0.0286 190 ARG A CG 1140 C CD . ARG A 197 ? 0.5186 0.5084 0.4528 -0.0163 0.2020 0.0294 190 ARG A CD 1141 N NE . ARG A 197 ? 0.5284 0.5129 0.4476 -0.0156 0.1865 0.0291 190 ARG A NE 1142 C CZ . ARG A 197 ? 0.5028 0.4906 0.4357 -0.0190 0.1767 0.0304 190 ARG A CZ 1143 N NH1 . ARG A 197 ? 0.4571 0.4534 0.4188 -0.0234 0.1796 0.0316 190 ARG A NH1 1144 N NH2 . ARG A 197 ? 0.5067 0.4897 0.4252 -0.0178 0.1637 0.0301 190 ARG A NH2 1145 N N . ASP A 198 ? 0.6199 0.6177 0.5635 -0.0071 0.2604 0.0234 191 ASP A N 1146 C CA . ASP A 198 ? 0.6343 0.6395 0.6001 -0.0079 0.2780 0.0245 191 ASP A CA 1147 C C . ASP A 198 ? 0.6519 0.6525 0.6001 -0.0020 0.2902 0.0213 191 ASP A C 1148 O O . ASP A 198 ? 0.6764 0.6726 0.6197 -0.0013 0.3083 0.0259 191 ASP A O 1149 C CB . ASP A 198 ? 0.6154 0.6383 0.6225 -0.0110 0.2728 0.0198 191 ASP A CB 1150 C CG . ASP A 198 ? 0.6306 0.6585 0.6573 -0.0167 0.2616 0.0225 191 ASP A CG 1151 O OD1 . ASP A 198 ? 0.6796 0.6993 0.6974 -0.0198 0.2644 0.0298 191 ASP A OD1 1152 O OD2 . ASP A 198 ? 0.6536 0.6928 0.7039 -0.0180 0.2498 0.0173 191 ASP A OD2 1153 N N . MET A 199 ? 0.6405 0.6418 0.5794 0.0023 0.2810 0.0133 192 MET A N 1154 C CA . MET A 199 ? 0.6601 0.6571 0.5835 0.0083 0.2919 0.0091 192 MET A CA 1155 C C . MET A 199 ? 0.6851 0.6639 0.5634 0.0130 0.2929 0.0103 192 MET A C 1156 O O . MET A 199 ? 0.7004 0.6732 0.5615 0.0183 0.3034 0.0075 192 MET A O 1157 C CB . MET A 199 ? 0.6420 0.6479 0.5782 0.0111 0.2828 -0.0004 192 MET A CB 1158 C CG . MET A 199 ? 0.6288 0.6521 0.6075 0.0078 0.2804 -0.0027 192 MET A CG 1159 S SD . MET A 199 ? 0.6053 0.6353 0.5915 0.0120 0.2677 -0.0133 192 MET A SD 1160 C CE . MET A 199 ? 0.6227 0.6520 0.6062 0.0178 0.2872 -0.0169 192 MET A CE 1161 N N . LYS A 200 ? 0.6829 0.6530 0.5422 0.0116 0.2812 0.0137 193 LYS A N 1162 C CA . LYS A 200 ? 0.7115 0.6640 0.5279 0.0161 0.2803 0.0153 193 LYS A CA 1163 C C . LYS A 200 ? 0.7166 0.6649 0.5139 0.0219 0.2726 0.0061 193 LYS A C 1164 O O . LYS A 200 ? 0.7377 0.6731 0.5033 0.0273 0.2789 0.0052 193 LYS A O 1165 C CB . LYS A 200 ? 0.7523 0.6942 0.5509 0.0180 0.3010 0.0224 193 LYS A CB 1166 C CG . LYS A 200 ? 0.7968 0.7315 0.5895 0.0142 0.3053 0.0331 193 LYS A CG 1167 C CD . LYS A 200 ? 0.7861 0.7324 0.6124 0.0068 0.2970 0.0361 193 LYS A CD 1168 C CE . LYS A 200 ? 0.8174 0.7576 0.6444 0.0028 0.3073 0.0471 193 LYS A CE 1169 N NZ . LYS A 200 ? 0.8002 0.7414 0.6352 -0.0017 0.2921 0.0501 193 LYS A NZ 1170 N N . ILE A 201 ? 0.6908 0.6493 0.5068 0.0210 0.2591 -0.0007 194 ILE A N 1171 C CA . ILE A 201 ? 0.7000 0.6548 0.5011 0.0260 0.2514 -0.0096 194 ILE A CA 1172 C C . ILE A 201 ? 0.7009 0.6499 0.4855 0.0258 0.2322 -0.0113 194 ILE A C 1173 O O . ILE A 201 ? 0.6764 0.6318 0.4767 0.0213 0.2215 -0.0090 194 ILE A O 1174 C CB . ILE A 201 ? 0.6839 0.6527 0.5152 0.0262 0.2513 -0.0165 194 ILE A CB 1175 C CG1 . ILE A 201 ? 0.7086 0.6798 0.5476 0.0286 0.2717 -0.0161 194 ILE A CG1 1176 C CG2 . ILE A 201 ? 0.6915 0.6572 0.5113 0.0301 0.2394 -0.0255 194 ILE A CG2 1177 C CD1 . ILE A 201 ? 0.6984 0.6852 0.5735 0.0280 0.2741 -0.0208 194 ILE A CD1 1178 N N . ASN A 202 ? 0.7222 0.6588 0.4752 0.0308 0.2280 -0.0155 195 ASN A N 1179 C CA . ASN A 202 ? 0.7328 0.6624 0.4678 0.0308 0.2110 -0.0164 195 ASN A CA 1180 C C . ASN A 202 ? 0.7101 0.6432 0.4498 0.0324 0.1977 -0.0258 195 ASN A C 1181 O O . ASN A 202 ? 0.7017 0.6300 0.4295 0.0370 0.2011 -0.0323 195 ASN A O 1182 C CB . ASN A 202 ? 0.7869 0.6988 0.4819 0.0353 0.2144 -0.0138 195 ASN A CB 1183 C CG . ASN A 202 ? 0.8512 0.7559 0.5282 0.0354 0.1970 -0.0138 195 ASN A CG 1184 O OD1 . ASN A 202 ? 0.8238 0.7366 0.5176 0.0323 0.1827 -0.0164 195 ASN A OD1 1185 N ND2 . ASN A 202 ? 0.9706 0.8598 0.6129 0.0393 0.1981 -0.0110 195 ASN A ND2 1186 N N . CYS A 203 ? 0.6639 0.6052 0.4217 0.0285 0.1834 -0.0265 196 CYS A N 1187 C CA . CYS A 203 ? 0.6555 0.6001 0.4192 0.0295 0.1711 -0.0347 196 CYS A CA 1188 C C . CYS A 203 ? 0.6635 0.5971 0.4009 0.0320 0.1582 -0.0383 196 CYS A C 1189 O O . CYS A 203 ? 0.6505 0.5851 0.3908 0.0328 0.1480 -0.0452 196 CYS A O 1190 C CB . CYS A 203 ? 0.6174 0.5755 0.4125 0.0247 0.1619 -0.0343 196 CYS A CB 1191 S SG . CYS A 203 ? 0.6210 0.5933 0.4504 0.0226 0.1734 -0.0331 196 CYS A SG 1192 N N . SER A 204 ? 0.6857 0.6087 0.3984 0.0331 0.1581 -0.0337 197 SER A N 1193 C CA . SER A 204 ? 0.7021 0.6150 0.3909 0.0355 0.1447 -0.0371 197 SER A CA 1194 C C . SER A 204 ? 0.7146 0.6201 0.3872 0.0406 0.1437 -0.0464 197 SER A C 1195 O O . SER A 204 ? 0.7499 0.6487 0.4077 0.0446 0.1564 -0.0476 197 SER A O 1196 C CB . SER A 204 ? 0.7287 0.6304 0.3920 0.0368 0.1456 -0.0304 197 SER A CB 1197 O OG . SER A 204 ? 0.7579 0.6481 0.3942 0.0405 0.1341 -0.0346 197 SER A OG 1198 N N . GLY A 205 ? 0.6920 0.5988 0.3686 0.0403 0.1293 -0.0530 198 GLY A N 1199 C CA . GLY A 205 ? 0.6952 0.5950 0.3589 0.0445 0.1259 -0.0625 198 GLY A CA 1200 C C . GLY A 205 ? 0.6867 0.5925 0.3670 0.0456 0.1351 -0.0673 198 GLY A C 1201 O O . GLY A 205 ? 0.7032 0.6017 0.3707 0.0498 0.1353 -0.0750 198 GLY A O 1202 N N . LYS A 206 ? 0.6602 0.5789 0.3690 0.0421 0.1421 -0.0632 199 LYS A N 1203 C CA . LYS A 206 ? 0.6427 0.5683 0.3703 0.0432 0.1504 -0.0674 199 LYS A CA 1204 C C . LYS A 206 ? 0.6102 0.5451 0.3626 0.0402 0.1388 -0.0708 199 LYS A C 1205 O O . LYS A 206 ? 0.5896 0.5281 0.3490 0.0365 0.1275 -0.0681 199 LYS A O 1206 C CB . LYS A 206 ? 0.6339 0.5684 0.3798 0.0415 0.1653 -0.0611 199 LYS A CB 1207 C CG . LYS A 206 ? 0.6831 0.6100 0.4091 0.0435 0.1791 -0.0556 199 LYS A CG 1208 C CD . LYS A 206 ? 0.7492 0.6641 0.4491 0.0499 0.1872 -0.0610 199 LYS A CD 1209 C CE . LYS A 206 ? 0.8018 0.7078 0.4794 0.0519 0.2003 -0.0545 199 LYS A CE 1210 N NZ . LYS A 206 ? 0.8440 0.7329 0.4829 0.0573 0.1963 -0.0584 199 LYS A NZ 1211 N N . ILE A 207 ? 0.6078 0.5461 0.3730 0.0421 0.1419 -0.0766 200 ILE A N 1212 C CA . ILE A 207 ? 0.5828 0.5308 0.3746 0.0394 0.1335 -0.0784 200 ILE A CA 1213 C C . ILE A 207 ? 0.5562 0.5168 0.3742 0.0372 0.1423 -0.0735 200 ILE A C 1214 O O . ILE A 207 ? 0.5651 0.5273 0.3870 0.0398 0.1553 -0.0741 200 ILE A O 1215 C CB . ILE A 207 ? 0.5974 0.5416 0.3895 0.0427 0.1307 -0.0874 200 ILE A CB 1216 C CG1 . ILE A 207 ? 0.6157 0.5475 0.3836 0.0443 0.1200 -0.0928 200 ILE A CG1 1217 C CG2 . ILE A 207 ? 0.5669 0.5211 0.3873 0.0401 0.1239 -0.0881 200 ILE A CG2 1218 C CD1 . ILE A 207 ? 0.6017 0.5276 0.3671 0.0477 0.1172 -0.1021 200 ILE A CD1 1219 N N . VAL A 208 ? 0.5080 0.4774 0.3441 0.0327 0.1353 -0.0689 201 VAL A N 1220 C CA . VAL A 208 ? 0.4879 0.4691 0.3494 0.0305 0.1417 -0.0646 201 VAL A CA 1221 C C . VAL A 208 ? 0.4607 0.4496 0.3456 0.0311 0.1383 -0.0687 201 VAL A C 1222 O O . VAL A 208 ? 0.4540 0.4419 0.3409 0.0306 0.1271 -0.0717 201 VAL A O 1223 C CB . VAL A 208 ? 0.4900 0.4757 0.3572 0.0258 0.1373 -0.0571 201 VAL A CB 1224 C CG1 A VAL A 208 ? 0.4988 0.4763 0.3432 0.0259 0.1431 -0.0526 201 VAL A CG1 1225 C CG1 B VAL A 208 ? 0.4352 0.4329 0.3308 0.0226 0.1315 -0.0553 201 VAL A CG1 1226 C CG2 A VAL A 208 ? 0.4521 0.4387 0.3220 0.0234 0.1224 -0.0575 201 VAL A CG2 1227 C CG2 B VAL A 208 ? 0.4995 0.4831 0.3583 0.0254 0.1493 -0.0514 201 VAL A CG2 1228 N N . ILE A 209 ? 0.4427 0.4389 0.3451 0.0324 0.1481 -0.0687 202 ILE A N 1229 C CA . ILE A 209 ? 0.4078 0.4124 0.3345 0.0329 0.1444 -0.0712 202 ILE A CA 1230 C C . ILE A 209 ? 0.3990 0.4157 0.3503 0.0297 0.1456 -0.0658 202 ILE A C 1231 O O . ILE A 209 ? 0.4102 0.4311 0.3676 0.0290 0.1563 -0.0624 202 ILE A O 1232 C CB . ILE A 209 ? 0.4309 0.4337 0.3596 0.0380 0.1522 -0.0776 202 ILE A CB 1233 C CG1 . ILE A 209 ? 0.3934 0.4043 0.3475 0.0390 0.1481 -0.0799 202 ILE A CG1 1234 C CG2 . ILE A 209 ? 0.4126 0.4162 0.3396 0.0401 0.1689 -0.0763 202 ILE A CG2 1235 C CD1 . ILE A 209 ? 0.4214 0.4279 0.3744 0.0446 0.1533 -0.0873 202 ILE A CD1 1236 N N . ALA A 210 ? 0.3787 0.4006 0.3436 0.0276 0.1346 -0.0650 203 ALA A N 1237 C CA . ALA A 210 ? 0.3699 0.4023 0.3567 0.0246 0.1334 -0.0604 203 ALA A CA 1238 C C . ALA A 210 ? 0.3637 0.4030 0.3718 0.0262 0.1279 -0.0630 203 ALA A C 1239 O O . ALA A 210 ? 0.3521 0.3874 0.3563 0.0277 0.1202 -0.0663 203 ALA A O 1240 C CB . ALA A 210 ? 0.3513 0.3827 0.3318 0.0204 0.1242 -0.0557 203 ALA A CB 1241 N N . ARG A 211 ? 0.3586 0.4082 0.3898 0.0258 0.1312 -0.0613 204 ARG A N 1242 C CA . ARG A 211 ? 0.3442 0.4001 0.3947 0.0271 0.1237 -0.0627 204 ARG A CA 1243 C C . ARG A 211 ? 0.3297 0.3876 0.3835 0.0240 0.1120 -0.0593 204 ARG A C 1244 O O . ARG A 211 ? 0.3138 0.3731 0.3658 0.0203 0.1114 -0.0550 204 ARG A O 1245 C CB . ARG A 211 ? 0.3491 0.4152 0.4243 0.0287 0.1303 -0.0633 204 ARG A CB 1246 C CG . ARG A 211 ? 0.3612 0.4337 0.4460 0.0252 0.1369 -0.0589 204 ARG A CG 1247 C CD . ARG A 211 ? 0.3919 0.4754 0.5050 0.0271 0.1415 -0.0603 204 ARG A CD 1248 N NE . ARG A 211 ? 0.3750 0.4654 0.5014 0.0241 0.1500 -0.0568 204 ARG A NE 1249 C CZ . ARG A 211 ? 0.3759 0.4774 0.5302 0.0245 0.1529 -0.0574 204 ARG A CZ 1250 N NH1 . ARG A 211 ? 0.3276 0.4344 0.4983 0.0282 0.1469 -0.0611 204 ARG A NH1 1251 N NH2 . ARG A 211 ? 0.3717 0.4788 0.5381 0.0212 0.1613 -0.0541 204 ARG A NH2 1252 N N . TYR A 212 ? 0.3014 0.3589 0.3599 0.0258 0.1032 -0.0612 205 TYR A N 1253 C CA . TYR A 212 ? 0.2892 0.3486 0.3521 0.0239 0.0925 -0.0584 205 TYR A CA 1254 C C . TYR A 212 ? 0.2814 0.3508 0.3652 0.0230 0.0922 -0.0562 205 TYR A C 1255 O O . TYR A 212 ? 0.2630 0.3384 0.3619 0.0250 0.0986 -0.0579 205 TYR A O 1256 C CB . TYR A 212 ? 0.2817 0.3384 0.3468 0.0269 0.0853 -0.0609 205 TYR A CB 1257 C CG . TYR A 212 ? 0.3089 0.3562 0.3562 0.0263 0.0801 -0.0618 205 TYR A CG 1258 C CD1 . TYR A 212 ? 0.2976 0.3388 0.3404 0.0294 0.0804 -0.0661 205 TYR A CD1 1259 C CD2 . TYR A 212 ? 0.2749 0.3199 0.3123 0.0229 0.0742 -0.0585 205 TYR A CD2 1260 C CE1 . TYR A 212 ? 0.2998 0.3329 0.3294 0.0286 0.0750 -0.0672 205 TYR A CE1 1261 C CE2 . TYR A 212 ? 0.3097 0.3472 0.3342 0.0223 0.0688 -0.0594 205 TYR A CE2 1262 C CZ . TYR A 212 ? 0.3239 0.3556 0.3451 0.0249 0.0690 -0.0636 205 TYR A CZ 1263 O OH . TYR A 212 ? 0.2746 0.2991 0.2849 0.0238 0.0633 -0.0645 205 TYR A OH 1264 N N . GLY A 213 ? 0.2657 0.3369 0.3510 0.0203 0.0848 -0.0527 206 GLY A N 1265 C CA . GLY A 213 ? 0.2608 0.3409 0.3664 0.0198 0.0818 -0.0514 206 GLY A CA 1266 C C . GLY A 213 ? 0.2647 0.3459 0.3683 0.0153 0.0820 -0.0474 206 GLY A C 1267 O O . GLY A 213 ? 0.2570 0.3328 0.3448 0.0130 0.0867 -0.0457 206 GLY A O 1268 N N . LYS A 214 ? 0.2501 0.3373 0.3686 0.0143 0.0763 -0.0462 207 LYS A N 1269 C CA . LYS A 214 ? 0.2610 0.3503 0.3823 0.0100 0.0766 -0.0427 207 LYS A CA 1270 C C . LYS A 214 ? 0.2535 0.3363 0.3573 0.0077 0.0709 -0.0399 207 LYS A C 1271 O O . LYS A 214 ? 0.2548 0.3395 0.3638 0.0058 0.0652 -0.0380 207 LYS A O 1272 C CB . LYS A 214 ? 0.2788 0.3694 0.4020 0.0076 0.0886 -0.0413 207 LYS A CB 1273 C CG . LYS A 214 ? 0.3164 0.4138 0.4577 0.0097 0.0967 -0.0440 207 LYS A CG 1274 C CD . LYS A 214 ? 0.3743 0.4815 0.5420 0.0092 0.0933 -0.0446 207 LYS A CD 1275 C CE . LYS A 214 ? 0.3840 0.4987 0.5713 0.0116 0.1017 -0.0474 207 LYS A CE 1276 N NZ . LYS A 214 ? 0.4251 0.5494 0.6387 0.0122 0.0947 -0.0490 207 LYS A NZ 1277 N N . VAL A 215 ? 0.2516 0.3269 0.3356 0.0078 0.0725 -0.0397 208 VAL A N 1278 C CA . VAL A 215 ? 0.2438 0.3133 0.3122 0.0058 0.0669 -0.0370 208 VAL A CA 1279 C C . VAL A 215 ? 0.2447 0.3081 0.2989 0.0077 0.0628 -0.0386 208 VAL A C 1280 O O . VAL A 215 ? 0.2583 0.3200 0.3105 0.0101 0.0661 -0.0416 208 VAL A O 1281 C CB . VAL A 215 ? 0.2432 0.3091 0.3005 0.0025 0.0731 -0.0339 208 VAL A CB 1282 C CG1 . VAL A 215 ? 0.2395 0.3107 0.3116 0.0000 0.0780 -0.0318 208 VAL A CG1 1283 C CG2 . VAL A 215 ? 0.2752 0.3358 0.3186 0.0036 0.0811 -0.0352 208 VAL A CG2 1284 N N . PHE A 216 ? 0.2348 0.2948 0.2799 0.0065 0.0560 -0.0367 209 PHE A N 1285 C CA . PHE A 216 ? 0.2429 0.2972 0.2756 0.0076 0.0520 -0.0378 209 PHE A CA 1286 C C . PHE A 216 ? 0.2442 0.2931 0.2637 0.0076 0.0575 -0.0395 209 PHE A C 1287 O O . PHE A 216 ? 0.2606 0.3076 0.2722 0.0058 0.0624 -0.0380 209 PHE A O 1288 C CB . PHE A 216 ? 0.2217 0.2737 0.2472 0.0059 0.0454 -0.0350 209 PHE A CB 1289 C CG . PHE A 216 ? 0.2506 0.2970 0.2645 0.0063 0.0417 -0.0358 209 PHE A CG 1290 C CD1 . PHE A 216 ? 0.2541 0.2995 0.2712 0.0086 0.0387 -0.0377 209 PHE A CD1 1291 C CD2 . PHE A 216 ? 0.2547 0.2969 0.2556 0.0043 0.0404 -0.0344 209 PHE A CD2 1292 C CE1 . PHE A 216 ? 0.2555 0.2959 0.2640 0.0085 0.0355 -0.0384 209 PHE A CE1 1293 C CE2 . PHE A 216 ? 0.2725 0.3102 0.2651 0.0045 0.0365 -0.0355 209 PHE A CE2 1294 C CZ . PHE A 216 ? 0.2707 0.3077 0.2679 0.0064 0.0344 -0.0376 209 PHE A CZ 1295 N N . ARG A 217 ? 0.2467 0.2923 0.2628 0.0098 0.0567 -0.0427 210 ARG A N 1296 C CA . ARG A 217 ? 0.2517 0.2917 0.2554 0.0105 0.0619 -0.0455 210 ARG A CA 1297 C C . ARG A 217 ? 0.2783 0.3125 0.2649 0.0084 0.0599 -0.0441 210 ARG A C 1298 O O . ARG A 217 ? 0.2790 0.3089 0.2538 0.0086 0.0649 -0.0451 210 ARG A O 1299 C CB . ARG A 217 ? 0.2593 0.2960 0.2630 0.0132 0.0604 -0.0495 210 ARG A CB 1300 C CG . ARG A 217 ? 0.2403 0.2736 0.2403 0.0126 0.0519 -0.0491 210 ARG A CG 1301 C CD . ARG A 217 ? 0.2621 0.2918 0.2645 0.0152 0.0507 -0.0528 210 ARG A CD 1302 N NE . ARG A 217 ? 0.2615 0.2953 0.2783 0.0174 0.0491 -0.0523 210 ARG A NE 1303 C CZ . ARG A 217 ? 0.2806 0.3163 0.3027 0.0172 0.0432 -0.0492 210 ARG A CZ 1304 N NH1 . ARG A 217 ? 0.2603 0.2948 0.2758 0.0147 0.0390 -0.0465 210 ARG A NH1 1305 N NH2 . ARG A 217 ? 0.2528 0.2913 0.2862 0.0199 0.0414 -0.0489 210 ARG A NH2 1306 N N . GLY A 218 ? 0.2588 0.2929 0.2439 0.0068 0.0526 -0.0417 211 GLY A N 1307 C CA . GLY A 218 ? 0.2747 0.3042 0.2458 0.0050 0.0498 -0.0400 211 GLY A CA 1308 C C . GLY A 218 ? 0.2856 0.3151 0.2517 0.0035 0.0549 -0.0369 211 GLY A C 1309 O O . GLY A 218 ? 0.2928 0.3166 0.2438 0.0033 0.0562 -0.0367 211 GLY A O 1310 N N . ASN A 219 ? 0.2756 0.3107 0.2541 0.0027 0.0577 -0.0346 212 ASN A N 1311 C CA . ASN A 219 ? 0.2878 0.3226 0.2634 0.0012 0.0638 -0.0315 212 ASN A CA 1312 C C . ASN A 219 ? 0.3092 0.3409 0.2776 0.0024 0.0732 -0.0330 212 ASN A C 1313 O O . ASN A 219 ? 0.2911 0.3181 0.2472 0.0017 0.0777 -0.0306 212 ASN A O 1314 C CB . ASN A 219 ? 0.2866 0.3283 0.2794 -0.0001 0.0647 -0.0292 212 ASN A CB 1315 C CG . ASN A 219 ? 0.3055 0.3486 0.3017 -0.0013 0.0563 -0.0271 212 ASN A CG 1316 O OD1 . ASN A 219 ? 0.3167 0.3627 0.3207 -0.0001 0.0507 -0.0286 212 ASN A OD1 1317 N ND2 . ASN A 219 ? 0.2567 0.2969 0.2457 -0.0032 0.0554 -0.0237 212 ASN A ND2 1318 N N . LYS A 220 ? 0.2977 0.3316 0.2734 0.0046 0.0765 -0.0368 213 LYS A N 1319 C CA . LYS A 220 ? 0.3086 0.3391 0.2767 0.0066 0.0857 -0.0391 213 LYS A CA 1320 C C . LYS A 220 ? 0.3208 0.3418 0.2657 0.0074 0.0844 -0.0405 213 LYS A C 1321 O O . LYS A 220 ? 0.3185 0.3344 0.2501 0.0081 0.0915 -0.0396 213 LYS A O 1322 C CB . LYS A 220 ? 0.3068 0.3403 0.2856 0.0094 0.0877 -0.0437 213 LYS A CB 1323 C CG . LYS A 220 ? 0.2882 0.3312 0.2907 0.0094 0.0878 -0.0432 213 LYS A CG 1324 C CD . LYS A 220 ? 0.2913 0.3363 0.3029 0.0128 0.0896 -0.0478 213 LYS A CD 1325 C CE . LYS A 220 ? 0.2902 0.3438 0.3242 0.0135 0.0868 -0.0476 213 LYS A CE 1326 N NZ . LYS A 220 ? 0.2717 0.3319 0.3204 0.0136 0.0960 -0.0473 213 LYS A NZ 1327 N N . VAL A 221 ? 0.3051 0.3235 0.2455 0.0077 0.0755 -0.0428 214 VAL A N 1328 C CA . VAL A 221 ? 0.3329 0.3427 0.2538 0.0088 0.0726 -0.0452 214 VAL A CA 1329 C C . VAL A 221 ? 0.3463 0.3520 0.2536 0.0072 0.0711 -0.0410 214 VAL A C 1330 O O . VAL A 221 ? 0.3640 0.3623 0.2530 0.0086 0.0741 -0.0416 214 VAL A O 1331 C CB . VAL A 221 ? 0.3330 0.3416 0.2557 0.0090 0.0633 -0.0487 214 VAL A CB 1332 C CG1 . VAL A 221 ? 0.3450 0.3451 0.2484 0.0096 0.0585 -0.0512 214 VAL A CG1 1333 C CG2 . VAL A 221 ? 0.3270 0.3368 0.2588 0.0114 0.0658 -0.0533 214 VAL A CG2 1334 N N . LYS A 222 ? 0.3354 0.3455 0.2512 0.0048 0.0666 -0.0368 215 LYS A N 1335 C CA . LYS A 222 ? 0.3443 0.3509 0.2496 0.0034 0.0651 -0.0323 215 LYS A CA 1336 C C . LYS A 222 ? 0.3629 0.3666 0.2611 0.0036 0.0755 -0.0296 215 LYS A C 1337 O O . LYS A 222 ? 0.3786 0.3745 0.2578 0.0045 0.0770 -0.0281 215 LYS A O 1338 C CB . LYS A 222 ? 0.3325 0.3450 0.2511 0.0010 0.0603 -0.0285 215 LYS A CB 1339 C CG . LYS A 222 ? 0.3739 0.3825 0.2828 -0.0002 0.0591 -0.0236 215 LYS A CG 1340 C CD . LYS A 222 ? 0.3970 0.4108 0.3185 -0.0022 0.0531 -0.0207 215 LYS A CD 1341 C CE . LYS A 222 ? 0.5003 0.5103 0.4146 -0.0035 0.0533 -0.0155 215 LYS A CE 1342 N NZ . LYS A 222 ? 0.6089 0.6237 0.5378 -0.0055 0.0587 -0.0126 215 LYS A NZ 1343 N N . ASN A 223 ? 0.3544 0.3642 0.2679 0.0031 0.0829 -0.0289 216 ASN A N 1344 C CA . ASN A 223 ? 0.3693 0.3772 0.2791 0.0030 0.0944 -0.0259 216 ASN A CA 1345 C C . ASN A 223 ? 0.3933 0.3932 0.2838 0.0062 0.1007 -0.0287 216 ASN A C 1346 O O . ASN A 223 ? 0.4002 0.3934 0.2754 0.0067 0.1072 -0.0254 216 ASN A O 1347 C CB . ASN A 223 ? 0.3379 0.3548 0.2706 0.0019 0.1011 -0.0254 216 ASN A CB 1348 C CG . ASN A 223 ? 0.3586 0.3824 0.3088 -0.0009 0.0953 -0.0225 216 ASN A CG 1349 O OD1 . ASN A 223 ? 0.3778 0.3990 0.3220 -0.0024 0.0884 -0.0198 216 ASN A OD1 1350 N ND2 . ASN A 223 ? 0.3067 0.3390 0.2784 -0.0015 0.0973 -0.0235 216 ASN A ND2 1351 N N . ALA A 224 ? 0.4000 0.3997 0.2904 0.0086 0.0990 -0.0346 217 ALA A N 1352 C CA . ALA A 224 ? 0.4200 0.4114 0.2914 0.0121 0.1047 -0.0384 217 ALA A CA 1353 C C . ALA A 224 ? 0.4431 0.4243 0.2898 0.0131 0.0986 -0.0382 217 ALA A C 1354 O O . ALA A 224 ? 0.4588 0.4315 0.2853 0.0154 0.1047 -0.0377 217 ALA A O 1355 C CB . ALA A 224 ? 0.4061 0.3990 0.2837 0.0144 0.1028 -0.0452 217 ALA A CB 1356 N N . GLN A 225 ? 0.4467 0.4289 0.2953 0.0116 0.0864 -0.0386 218 GLN A N 1357 C CA . GLN A 225 ? 0.4753 0.4492 0.3038 0.0125 0.0783 -0.0389 218 GLN A CA 1358 C C . GLN A 225 ? 0.5013 0.4701 0.3167 0.0122 0.0826 -0.0325 218 GLN A C 1359 O O . GLN A 225 ? 0.5165 0.4753 0.3087 0.0148 0.0839 -0.0326 218 GLN A O 1360 C CB A GLN A 225 ? 0.4654 0.4436 0.3040 0.0104 0.0659 -0.0391 218 GLN A CB 1361 C CB B GLN A 225 ? 0.4535 0.4316 0.2921 0.0105 0.0657 -0.0396 218 GLN A CB 1362 C CG A GLN A 225 ? 0.4909 0.4667 0.3268 0.0116 0.0581 -0.0455 218 GLN A CG 1363 C CG B GLN A 225 ? 0.4418 0.4127 0.2636 0.0115 0.0557 -0.0411 218 GLN A CG 1364 C CD A GLN A 225 ? 0.5271 0.5080 0.3757 0.0093 0.0473 -0.0454 218 GLN A CD 1365 C CD B GLN A 225 ? 0.4215 0.3975 0.2562 0.0094 0.0444 -0.0422 218 GLN A CD 1366 O OE1 A GLN A 225 ? 0.5216 0.5053 0.3808 0.0091 0.0438 -0.0492 218 GLN A OE1 1367 O OE1 B GLN A 225 ? 0.4152 0.3963 0.2644 0.0087 0.0427 -0.0454 218 GLN A OE1 1368 N NE2 A GLN A 225 ? 0.5268 0.5084 0.3743 0.0078 0.0426 -0.0408 218 GLN A NE2 1369 N NE2 B GLN A 225 ? 0.3858 0.3603 0.2152 0.0087 0.0372 -0.0394 218 GLN A NE2 1370 N N . LEU A 226 ? 0.5005 0.4755 0.3305 0.0092 0.0849 -0.0269 219 LEU A N 1371 C CA . LEU A 226 ? 0.5236 0.4938 0.3437 0.0085 0.0891 -0.0203 219 LEU A CA 1372 C C . LEU A 226 ? 0.5407 0.5055 0.3498 0.0102 0.1031 -0.0182 219 LEU A C 1373 O O . LEU A 226 ? 0.5491 0.5059 0.3416 0.0108 0.1070 -0.0133 219 LEU A O 1374 C CB . LEU A 226 ? 0.5077 0.4855 0.3472 0.0047 0.0871 -0.0154 219 LEU A CB 1375 C CG . LEU A 226 ? 0.5527 0.5336 0.3983 0.0034 0.0739 -0.0159 219 LEU A CG 1376 C CD1 . LEU A 226 ? 0.5480 0.5356 0.4119 0.0002 0.0728 -0.0114 219 LEU A CD1 1377 C CD2 . LEU A 226 ? 0.5981 0.5704 0.4231 0.0052 0.0658 -0.0156 219 LEU A CD2 1378 N N . ALA A 227 ? 0.5267 0.4953 0.3442 0.0112 0.1109 -0.0220 220 ALA A N 1379 C CA . ALA A 227 ? 0.5411 0.5047 0.3481 0.0135 0.1248 -0.0211 220 ALA A CA 1380 C C . ALA A 227 ? 0.5602 0.5121 0.3388 0.0182 0.1238 -0.0256 220 ALA A C 1381 O O . ALA A 227 ? 0.5800 0.5255 0.3444 0.0210 0.1349 -0.0253 220 ALA A O 1382 C CB . ALA A 227 ? 0.5306 0.5035 0.3597 0.0131 0.1330 -0.0236 220 ALA A CB 1383 N N . GLY A 228 ? 0.5492 0.4983 0.3199 0.0191 0.1104 -0.0299 221 GLY A N 1384 C CA . GLY A 228 ? 0.5579 0.4955 0.3019 0.0235 0.1074 -0.0348 221 GLY A CA 1385 C C . GLY A 228 ? 0.5546 0.4921 0.2996 0.0262 0.1090 -0.0430 221 GLY A C 1386 O O . GLY A 228 ? 0.5596 0.4866 0.2813 0.0303 0.1087 -0.0476 221 GLY A O 1387 N N . ALA A 229 ? 0.5290 0.4773 0.2999 0.0242 0.1099 -0.0452 222 ALA A N 1388 C CA . ALA A 229 ? 0.5233 0.4719 0.2977 0.0267 0.1113 -0.0528 222 ALA A CA 1389 C C . ALA A 229 ? 0.5349 0.4775 0.2983 0.0280 0.0980 -0.0591 222 ALA A C 1390 O O . ALA A 229 ? 0.5305 0.4740 0.2952 0.0257 0.0867 -0.0576 222 ALA A O 1391 C CB . ALA A 229 ? 0.5011 0.4622 0.3058 0.0243 0.1132 -0.0531 222 ALA A CB 1392 N N . LYS A 230 ? 0.5395 0.4758 0.2927 0.0317 0.0993 -0.0663 223 LYS A N 1393 C CA . LYS A 230 ? 0.5336 0.4649 0.2800 0.0324 0.0864 -0.0729 223 LYS A CA 1394 C C . LYS A 230 ? 0.5098 0.4480 0.2788 0.0311 0.0824 -0.0776 223 LYS A C 1395 O O . LYS A 230 ? 0.5148 0.4497 0.2825 0.0311 0.0721 -0.0831 223 LYS A O 1396 C CB . LYS A 230 ? 0.5840 0.5012 0.3003 0.0375 0.0872 -0.0784 223 LYS A CB 1397 C CG . LYS A 230 ? 0.6161 0.5297 0.3288 0.0414 0.0963 -0.0843 223 LYS A CG 1398 C CD . LYS A 230 ? 0.6680 0.5663 0.3482 0.0464 0.0935 -0.0903 223 LYS A CD 1399 C CE . LYS A 230 ? 0.7249 0.6172 0.3927 0.0513 0.1072 -0.0934 223 LYS A CE 1400 N NZ . LYS A 230 ? 0.7392 0.6163 0.3770 0.0564 0.1020 -0.1013 223 LYS A NZ 1401 N N . GLY A 231 ? 0.4810 0.4285 0.2712 0.0299 0.0902 -0.0753 224 GLY A N 1402 C CA . GLY A 231 ? 0.4564 0.4111 0.2696 0.0285 0.0860 -0.0782 224 GLY A CA 1403 C C . GLY A 231 ? 0.4416 0.4065 0.2760 0.0276 0.0952 -0.0745 224 GLY A C 1404 O O . GLY A 231 ? 0.4504 0.4164 0.2820 0.0285 0.1060 -0.0710 224 GLY A O 1405 N N . VAL A 232 ? 0.4304 0.4029 0.2867 0.0260 0.0907 -0.0749 225 VAL A N 1406 C CA . VAL A 232 ? 0.4088 0.3917 0.2875 0.0251 0.0967 -0.0716 225 VAL A CA 1407 C C . VAL A 232 ? 0.4113 0.3963 0.3043 0.0270 0.0957 -0.0766 225 VAL A C 1408 O O . VAL A 232 ? 0.3968 0.3797 0.2922 0.0264 0.0866 -0.0794 225 VAL A O 1409 C CB . VAL A 232 ? 0.3960 0.3871 0.2891 0.0210 0.0905 -0.0656 225 VAL A CB 1410 C CG1 . VAL A 232 ? 0.3683 0.3696 0.2839 0.0204 0.0962 -0.0629 225 VAL A CG1 1411 C CG2 . VAL A 232 ? 0.3966 0.3849 0.2762 0.0189 0.0891 -0.0606 225 VAL A CG2 1412 N N . ILE A 233 ? 0.4128 0.4021 0.3162 0.0293 0.1055 -0.0774 226 ILE A N 1413 C CA . ILE A 233 ? 0.3997 0.3923 0.3195 0.0315 0.1057 -0.0811 226 ILE A CA 1414 C C . ILE A 233 ? 0.3766 0.3810 0.3201 0.0300 0.1075 -0.0764 226 ILE A C 1415 O O . ILE A 233 ? 0.4025 0.4121 0.3516 0.0298 0.1162 -0.0733 226 ILE A O 1416 C CB . ILE A 233 ? 0.4279 0.4156 0.3408 0.0362 0.1155 -0.0865 226 ILE A CB 1417 C CG1 . ILE A 233 ? 0.4433 0.4181 0.3309 0.0379 0.1122 -0.0918 226 ILE A CG1 1418 C CG2 . ILE A 233 ? 0.4004 0.3929 0.3336 0.0390 0.1171 -0.0897 226 ILE A CG2 1419 C CD1 . ILE A 233 ? 0.4275 0.3955 0.3028 0.0430 0.1224 -0.0974 226 ILE A CD1 1420 N N . LEU A 234 ? 0.3543 0.3624 0.3116 0.0290 0.0992 -0.0759 227 LEU A N 1421 C CA . LEU A 234 ? 0.3337 0.3523 0.3131 0.0280 0.0985 -0.0722 227 LEU A CA 1422 C C . LEU A 234 ? 0.3349 0.3559 0.3290 0.0319 0.1009 -0.0760 227 LEU A C 1423 O O . LEU A 234 ? 0.3329 0.3477 0.3229 0.0339 0.0973 -0.0802 227 LEU A O 1424 C CB . LEU A 234 ? 0.3128 0.3328 0.2959 0.0250 0.0876 -0.0689 227 LEU A CB 1425 C CG . LEU A 234 ? 0.3370 0.3562 0.3093 0.0213 0.0844 -0.0646 227 LEU A CG 1426 C CD1 . LEU A 234 ? 0.3318 0.3518 0.3080 0.0190 0.0738 -0.0623 227 LEU A CD1 1427 C CD2 . LEU A 234 ? 0.3237 0.3495 0.3027 0.0197 0.0910 -0.0603 227 LEU A CD2 1428 N N . TYR A 235 ? 0.3253 0.3550 0.3369 0.0331 0.1070 -0.0748 228 TYR A N 1429 C CA . TYR A 235 ? 0.3148 0.3474 0.3422 0.0373 0.1082 -0.0783 228 TYR A CA 1430 C C . TYR A 235 ? 0.3025 0.3460 0.3530 0.0371 0.1065 -0.0752 228 TYR A C 1431 O O . TYR A 235 ? 0.3069 0.3564 0.3625 0.0341 0.1078 -0.0710 228 TYR A O 1432 C CB . TYR A 235 ? 0.3325 0.3626 0.3571 0.0413 0.1192 -0.0830 228 TYR A CB 1433 C CG . TYR A 235 ? 0.3162 0.3551 0.3531 0.0414 0.1297 -0.0809 228 TYR A CG 1434 C CD1 . TYR A 235 ? 0.3331 0.3807 0.3933 0.0444 0.1333 -0.0820 228 TYR A CD1 1435 C CD2 . TYR A 235 ? 0.3360 0.3743 0.3620 0.0386 0.1360 -0.0776 228 TYR A CD2 1436 C CE1 . TYR A 235 ? 0.3479 0.4044 0.4221 0.0441 0.1433 -0.0801 228 TYR A CE1 1437 C CE2 . TYR A 235 ? 0.3105 0.3567 0.3489 0.0382 0.1464 -0.0752 228 TYR A CE2 1438 C CZ . TYR A 235 ? 0.3590 0.4146 0.4222 0.0407 0.1499 -0.0765 228 TYR A CZ 1439 O OH . TYR A 235 ? 0.3567 0.4205 0.4341 0.0399 0.1602 -0.0741 228 TYR A OH 1440 N N . SER A 236 ? 0.2937 0.3390 0.3580 0.0406 0.1031 -0.0773 229 SER A N 1441 C CA . SER A 236 ? 0.2699 0.3253 0.3567 0.0414 0.1005 -0.0752 229 SER A CA 1442 C C . SER A 236 ? 0.2839 0.3460 0.3861 0.0447 0.1102 -0.0777 229 SER A C 1443 O O . SER A 236 ? 0.3043 0.3639 0.4095 0.0491 0.1132 -0.0820 229 SER A O 1444 C CB . SER A 236 ? 0.2769 0.3304 0.3697 0.0437 0.0907 -0.0755 229 SER A CB 1445 O OG . SER A 236 ? 0.2715 0.3190 0.3506 0.0405 0.0828 -0.0729 229 SER A OG 1446 N N . ASP A 237 ? 0.2888 0.3595 0.4021 0.0425 0.1152 -0.0751 230 ASP A N 1447 C CA . ASP A 237 ? 0.3021 0.3807 0.4339 0.0453 0.1249 -0.0771 230 ASP A CA 1448 C C . ASP A 237 ? 0.2953 0.3825 0.4520 0.0482 0.1184 -0.0776 230 ASP A C 1449 O O . ASP A 237 ? 0.2815 0.3725 0.4450 0.0461 0.1093 -0.0745 230 ASP A O 1450 C CB . ASP A 237 ? 0.3076 0.3918 0.4425 0.0415 0.1337 -0.0738 230 ASP A CB 1451 C CG . ASP A 237 ? 0.3237 0.4135 0.4716 0.0443 0.1473 -0.0762 230 ASP A CG 1452 O OD1 . ASP A 237 ? 0.3594 0.4435 0.4918 0.0446 0.1578 -0.0770 230 ASP A OD1 1453 O OD2 . ASP A 237 ? 0.3137 0.4133 0.4871 0.0467 0.1474 -0.0774 230 ASP A OD2 1454 N N . PRO A 238 ? 0.3140 0.4041 0.4844 0.0534 0.1230 -0.0817 231 PRO A N 1455 C CA . PRO A 238 ? 0.3163 0.4155 0.5124 0.0568 0.1177 -0.0824 231 PRO A CA 1456 C C . PRO A 238 ? 0.3125 0.4230 0.5273 0.0535 0.1163 -0.0792 231 PRO A C 1457 O O . PRO A 238 ? 0.3073 0.4233 0.5374 0.0548 0.1067 -0.0786 231 PRO A O 1458 C CB . PRO A 238 ? 0.3308 0.4326 0.5385 0.0621 0.1277 -0.0871 231 PRO A CB 1459 C CG . PRO A 238 ? 0.3468 0.4371 0.5304 0.0627 0.1339 -0.0896 231 PRO A CG 1460 C CD . PRO A 238 ? 0.3324 0.4178 0.4952 0.0567 0.1341 -0.0860 231 PRO A CD 1461 N N . ALA A 239 ? 0.3240 0.4374 0.5370 0.0492 0.1253 -0.0771 232 ALA A N 1462 C CA . ALA A 239 ? 0.3195 0.4431 0.5509 0.0455 0.1235 -0.0741 232 ALA A CA 1463 C C . ALA A 239 ? 0.3139 0.4360 0.5408 0.0429 0.1094 -0.0710 232 ALA A C 1464 O O . ALA A 239 ? 0.3013 0.4315 0.5473 0.0424 0.1027 -0.0703 232 ALA A O 1465 C CB . ALA A 239 ? 0.3323 0.4570 0.5595 0.0410 0.1359 -0.0715 232 ALA A CB 1466 N N . ASP A 240 ? 0.3048 0.4162 0.5066 0.0415 0.1048 -0.0697 233 ASP A N 1467 C CA . ASP A 240 ? 0.3053 0.4137 0.4986 0.0389 0.0933 -0.0665 233 ASP A CA 1468 C C . ASP A 240 ? 0.3057 0.4091 0.4950 0.0428 0.0824 -0.0675 233 ASP A C 1469 O O . ASP A 240 ? 0.3188 0.4223 0.5083 0.0421 0.0719 -0.0653 233 ASP A O 1470 C CB . ASP A 240 ? 0.2990 0.3992 0.4677 0.0345 0.0961 -0.0639 233 ASP A CB 1471 C CG . ASP A 240 ? 0.3238 0.4270 0.4936 0.0310 0.1075 -0.0622 233 ASP A CG 1472 O OD1 . ASP A 240 ? 0.3263 0.4356 0.5074 0.0276 0.1060 -0.0596 233 ASP A OD1 1473 O OD2 . ASP A 240 ? 0.3254 0.4247 0.4852 0.0318 0.1180 -0.0637 233 ASP A OD2 1474 N N . TYR A 241 ? 0.2956 0.3938 0.4801 0.0469 0.0849 -0.0706 234 TYR A N 1475 C CA . TYR A 241 ? 0.2864 0.3782 0.4656 0.0505 0.0759 -0.0712 234 TYR A CA 1476 C C . TYR A 241 ? 0.3031 0.3974 0.4984 0.0569 0.0751 -0.0746 234 TYR A C 1477 O O . TYR A 241 ? 0.3107 0.3978 0.4998 0.0604 0.0697 -0.0753 234 TYR A O 1478 C CB . TYR A 241 ? 0.2962 0.3760 0.4508 0.0491 0.0764 -0.0712 234 TYR A CB 1479 C CG . TYR A 241 ? 0.2599 0.3375 0.4001 0.0435 0.0748 -0.0676 234 TYR A CG 1480 C CD1 . TYR A 241 ? 0.2704 0.3474 0.4014 0.0400 0.0833 -0.0673 234 TYR A CD1 1481 C CD2 . TYR A 241 ? 0.2593 0.3353 0.3955 0.0421 0.0649 -0.0643 234 TYR A CD2 1482 C CE1 . TYR A 241 ? 0.2868 0.3619 0.4054 0.0350 0.0814 -0.0637 234 TYR A CE1 1483 C CE2 . TYR A 241 ? 0.2919 0.3662 0.4161 0.0372 0.0633 -0.0610 234 TYR A CE2 1484 C CZ . TYR A 241 ? 0.3011 0.3751 0.4170 0.0336 0.0713 -0.0607 234 TYR A CZ 1485 O OH . TYR A 241 ? 0.3009 0.3728 0.4052 0.0293 0.0689 -0.0574 234 TYR A OH 1486 N N . PHE A 242 ? 0.3065 0.4109 0.5230 0.0587 0.0806 -0.0766 235 PHE A N 1487 C CA . PHE A 242 ? 0.3140 0.4219 0.5483 0.0652 0.0791 -0.0798 235 PHE A CA 1488 C C . PHE A 242 ? 0.3199 0.4408 0.5812 0.0661 0.0760 -0.0800 235 PHE A C 1489 O O . PHE A 242 ? 0.3275 0.4572 0.6034 0.0646 0.0849 -0.0811 235 PHE A O 1490 C CB . PHE A 242 ? 0.3029 0.4085 0.5363 0.0679 0.0906 -0.0839 235 PHE A CB 1491 C CG . PHE A 242 ? 0.3139 0.4197 0.5606 0.0752 0.0888 -0.0874 235 PHE A CG 1492 C CD1 . PHE A 242 ? 0.2814 0.3755 0.5139 0.0783 0.0858 -0.0888 235 PHE A CD1 1493 C CD2 . PHE A 242 ? 0.2884 0.4061 0.5630 0.0789 0.0906 -0.0896 235 PHE A CD2 1494 C CE1 . PHE A 242 ? 0.2900 0.3831 0.5344 0.0854 0.0841 -0.0919 235 PHE A CE1 1495 C CE2 . PHE A 242 ? 0.3147 0.4325 0.6022 0.0862 0.0888 -0.0930 235 PHE A CE2 1496 C CZ . PHE A 242 ? 0.3318 0.4369 0.6037 0.0896 0.0856 -0.0941 235 PHE A CZ 1497 N N . ALA A 243 ? 0.3286 0.4503 0.5961 0.0687 0.0634 -0.0789 236 ALA A N 1498 C CA . ALA A 243 ? 0.3430 0.4764 0.6359 0.0700 0.0580 -0.0795 236 ALA A CA 1499 C C . ALA A 243 ? 0.3644 0.5053 0.6809 0.0758 0.0619 -0.0836 236 ALA A C 1500 O O . ALA A 243 ? 0.3722 0.5076 0.6863 0.0814 0.0602 -0.0854 236 ALA A O 1501 C CB . ALA A 243 ? 0.3421 0.4726 0.6321 0.0720 0.0429 -0.0775 236 ALA A CB 1502 N N . PRO A 244 ? 0.3787 0.5322 0.7193 0.0744 0.0675 -0.0852 237 PRO A N 1503 C CA . PRO A 244 ? 0.3833 0.5455 0.7496 0.0800 0.0720 -0.0893 237 PRO A CA 1504 C C . PRO A 244 ? 0.3824 0.5447 0.7594 0.0873 0.0586 -0.0907 237 PRO A C 1505 O O . PRO A 244 ? 0.3808 0.5434 0.7588 0.0874 0.0456 -0.0891 237 PRO A O 1506 C CB . PRO A 244 ? 0.3858 0.5622 0.7777 0.0762 0.0770 -0.0896 237 PRO A CB 1507 C CG . PRO A 244 ? 0.3834 0.5559 0.7569 0.0680 0.0808 -0.0857 237 PRO A CG 1508 C CD . PRO A 244 ? 0.3813 0.5418 0.7284 0.0678 0.0698 -0.0831 237 PRO A CD 1509 N N . GLY A 245 ? 0.3883 0.5488 0.7710 0.0937 0.0618 -0.0938 238 GLY A N 1510 C CA . GLY A 245 ? 0.3808 0.5419 0.7766 0.1017 0.0502 -0.0955 238 GLY A CA 1511 C C . GLY A 245 ? 0.3828 0.5295 0.7550 0.1047 0.0392 -0.0928 238 GLY A C 1512 O O . GLY A 245 ? 0.3851 0.5304 0.7649 0.1115 0.0292 -0.0934 238 GLY A O 1513 N N . VAL A 246 ? 0.3580 0.4938 0.7020 0.0997 0.0412 -0.0897 239 VAL A N 1514 C CA . VAL A 246 ? 0.3459 0.4673 0.6667 0.1018 0.0330 -0.0869 239 VAL A CA 1515 C C . VAL A 246 ? 0.3471 0.4580 0.6517 0.1022 0.0419 -0.0881 239 VAL A C 1516 O O . VAL A 246 ? 0.3395 0.4519 0.6407 0.0984 0.0536 -0.0897 239 VAL A O 1517 C CB . VAL A 246 ? 0.3504 0.4671 0.6528 0.0966 0.0251 -0.0822 239 VAL A CB 1518 C CG1 A VAL A 246 ? 0.3240 0.4520 0.6374 0.0909 0.0265 -0.0820 239 VAL A CG1 1519 C CG1 B VAL A 246 ? 0.3264 0.4276 0.6028 0.0973 0.0208 -0.0789 239 VAL A CG1 1520 C CG2 A VAL A 246 ? 0.3257 0.4290 0.5990 0.0929 0.0280 -0.0794 239 VAL A CG2 1521 C CG2 B VAL A 246 ? 0.3300 0.4546 0.6474 0.0983 0.0132 -0.0816 239 VAL A CG2 1522 N N . LYS A 247 ? 0.3607 0.4605 0.6556 0.1071 0.0362 -0.0873 240 LYS A N 1523 C CA . LYS A 247 ? 0.3889 0.4779 0.6706 0.1082 0.0433 -0.0891 240 LYS A CA 1524 C C . LYS A 247 ? 0.3898 0.4679 0.6441 0.1020 0.0446 -0.0862 240 LYS A C 1525 O O . LYS A 247 ? 0.3675 0.4432 0.6114 0.0989 0.0374 -0.0820 240 LYS A O 1526 C CB . LYS A 247 ? 0.4173 0.4990 0.7029 0.1163 0.0370 -0.0897 240 LYS A CB 1527 C CG . LYS A 247 ? 0.4429 0.5351 0.7569 0.1234 0.0357 -0.0932 240 LYS A CG 1528 C CD . LYS A 247 ? 0.5355 0.6349 0.8625 0.1238 0.0496 -0.0986 240 LYS A CD 1529 C CE . LYS A 247 ? 0.5853 0.6998 0.9453 0.1291 0.0493 -0.1019 240 LYS A CE 1530 N NZ . LYS A 247 ? 0.6057 0.7344 0.9793 0.1239 0.0492 -0.1009 240 LYS A NZ 1531 N N . SER A 248 ? 0.3953 0.4668 0.6388 0.1007 0.0539 -0.0890 241 SER A N 1532 C CA . SER A 248 ? 0.3937 0.4535 0.6125 0.0960 0.0550 -0.0873 241 SER A CA 1533 C C . SER A 248 ? 0.3839 0.4318 0.5920 0.0982 0.0458 -0.0840 241 SER A C 1534 O O . SER A 248 ? 0.3815 0.4260 0.5982 0.1048 0.0421 -0.0848 241 SER A O 1535 C CB . SER A 248 ? 0.4243 0.4782 0.6371 0.0967 0.0652 -0.0923 241 SER A CB 1536 O OG . SER A 248 ? 0.4706 0.5312 0.6830 0.0929 0.0752 -0.0944 241 SER A OG 1537 N N . TYR A 249 ? 0.3550 0.3960 0.5446 0.0930 0.0429 -0.0803 242 TYR A N 1538 C CA . TYR A 249 ? 0.3511 0.3787 0.5278 0.0940 0.0371 -0.0772 242 TYR A CA 1539 C C . TYR A 249 ? 0.3632 0.3815 0.5391 0.0977 0.0412 -0.0811 242 TYR A C 1540 O O . TYR A 249 ? 0.3605 0.3784 0.5330 0.0957 0.0494 -0.0856 242 TYR A O 1541 C CB . TYR A 249 ? 0.3449 0.3670 0.5026 0.0871 0.0364 -0.0738 242 TYR A CB 1542 C CG . TYR A 249 ? 0.3404 0.3525 0.4896 0.0885 0.0287 -0.0688 242 TYR A CG 1543 C CD1 . TYR A 249 ? 0.3484 0.3635 0.5006 0.0907 0.0207 -0.0644 242 TYR A CD1 1544 C CD2 . TYR A 249 ? 0.3601 0.3592 0.4993 0.0883 0.0295 -0.0687 242 TYR A CD2 1545 C CE1 . TYR A 249 ? 0.3389 0.3439 0.4824 0.0929 0.0144 -0.0594 242 TYR A CE1 1546 C CE2 . TYR A 249 ? 0.3896 0.3791 0.5221 0.0899 0.0235 -0.0636 242 TYR A CE2 1547 C CZ . TYR A 249 ? 0.3878 0.3804 0.5218 0.0923 0.0163 -0.0587 242 TYR A CZ 1548 O OH . TYR A 249 ? 0.4164 0.3987 0.5424 0.0944 0.0112 -0.0534 242 TYR A OH 1549 N N . PRO A 250 ? 0.3748 0.3843 0.5522 0.1031 0.0357 -0.0794 243 PRO A N 1550 C CA . PRO A 250 ? 0.3850 0.3908 0.5608 0.1057 0.0258 -0.0735 243 PRO A CA 1551 C C . PRO A 250 ? 0.3935 0.4075 0.5868 0.1125 0.0199 -0.0732 243 PRO A C 1552 O O . PRO A 250 ? 0.4145 0.4242 0.6057 0.1160 0.0113 -0.0686 243 PRO A O 1553 C CB . PRO A 250 ? 0.3888 0.3788 0.5566 0.1084 0.0247 -0.0725 243 PRO A CB 1554 C CG . PRO A 250 ? 0.3920 0.3820 0.5696 0.1120 0.0316 -0.0794 243 PRO A CG 1555 C CD . PRO A 250 ? 0.3918 0.3915 0.5690 0.1067 0.0395 -0.0835 243 PRO A CD 1556 N N . ASP A 251 ? 0.3819 0.4071 0.5921 0.1145 0.0243 -0.0779 244 ASP A N 1557 C CA . ASP A 251 ? 0.3909 0.4244 0.6205 0.1212 0.0183 -0.0784 244 ASP A CA 1558 C C . ASP A 251 ? 0.3789 0.4251 0.6162 0.1187 0.0140 -0.0769 244 ASP A C 1559 O O . ASP A 251 ? 0.3663 0.4192 0.6189 0.1238 0.0071 -0.0770 244 ASP A O 1560 C CB . ASP A 251 ? 0.3980 0.4373 0.6459 0.1259 0.0249 -0.0845 244 ASP A CB 1561 C CG . ASP A 251 ? 0.4611 0.4874 0.7026 0.1291 0.0289 -0.0868 244 ASP A CG 1562 O OD1 . ASP A 251 ? 0.4699 0.4832 0.7015 0.1317 0.0229 -0.0832 244 ASP A OD1 1563 O OD2 . ASP A 251 ? 0.5085 0.5373 0.7549 0.1290 0.0384 -0.0922 244 ASP A OD2 1564 N N . GLY A 252 ? 0.3630 0.4121 0.5901 0.1109 0.0178 -0.0758 245 GLY A N 1565 C CA . GLY A 252 ? 0.3485 0.4083 0.5810 0.1077 0.0139 -0.0743 245 GLY A CA 1566 C C . GLY A 252 ? 0.3424 0.3988 0.5559 0.0997 0.0169 -0.0717 245 GLY A C 1567 O O . GLY A 252 ? 0.3452 0.3909 0.5422 0.0973 0.0201 -0.0707 245 GLY A O 1568 N N . TRP A 253 ? 0.3235 0.3887 0.5400 0.0955 0.0156 -0.0707 246 TRP A N 1569 C CA . TRP A 253 ? 0.3096 0.3715 0.5083 0.0884 0.0170 -0.0678 246 TRP A CA 1570 C C . TRP A 253 ? 0.3031 0.3700 0.5003 0.0824 0.0274 -0.0701 246 TRP A C 1571 O O . TRP A 253 ? 0.2796 0.3455 0.4642 0.0764 0.0284 -0.0678 246 TRP A O 1572 C CB . TRP A 253 ? 0.3076 0.3725 0.5044 0.0874 0.0078 -0.0642 246 TRP A CB 1573 C CG . TRP A 253 ? 0.3094 0.3868 0.5271 0.0894 0.0038 -0.0662 246 TRP A CG 1574 C CD1 . TRP A 253 ? 0.3392 0.4193 0.5707 0.0962 -0.0043 -0.0671 246 TRP A CD1 1575 C CD2 . TRP A 253 ? 0.3292 0.4178 0.5573 0.0845 0.0075 -0.0677 246 TRP A CD2 1576 N NE1 . TRP A 253 ? 0.3228 0.4157 0.5736 0.0957 -0.0065 -0.0694 246 TRP A NE1 1577 C CE2 . TRP A 253 ? 0.3169 0.4151 0.5664 0.0884 0.0010 -0.0697 246 TRP A CE2 1578 C CE3 . TRP A 253 ? 0.3394 0.4305 0.5611 0.0773 0.0154 -0.0675 246 TRP A CE3 1579 C CZ2 . TRP A 253 ? 0.3348 0.4452 0.6008 0.0848 0.0026 -0.0715 246 TRP A CZ2 1580 C CZ3 . TRP A 253 ? 0.3320 0.4346 0.5686 0.0740 0.0174 -0.0687 246 TRP A CZ3 1581 C CH2 . TRP A 253 ? 0.3293 0.4415 0.5885 0.0776 0.0112 -0.0708 246 TRP A CH2 1582 N N . ASN A 254 ? 0.2839 0.3549 0.4923 0.0841 0.0355 -0.0745 247 ASN A N 1583 C CA . ASN A 254 ? 0.2917 0.3666 0.4975 0.0791 0.0461 -0.0766 247 ASN A CA 1584 C C . ASN A 254 ? 0.2965 0.3606 0.4827 0.0767 0.0517 -0.0775 247 ASN A C 1585 O O . ASN A 254 ? 0.3002 0.3545 0.4797 0.0797 0.0494 -0.0779 247 ASN A O 1586 C CB . ASN A 254 ? 0.2934 0.3781 0.5198 0.0820 0.0539 -0.0809 247 ASN A CB 1587 C CG . ASN A 254 ? 0.2907 0.3888 0.5346 0.0798 0.0536 -0.0804 247 ASN A CG 1588 O OD1 . ASN A 254 ? 0.2798 0.3793 0.5175 0.0751 0.0497 -0.0772 247 ASN A OD1 1589 N ND2 . ASN A 254 ? 0.2718 0.3798 0.5391 0.0835 0.0577 -0.0838 247 ASN A ND2 1590 N N . LEU A 255 ? 0.2848 0.3505 0.4627 0.0714 0.0590 -0.0779 248 LEU A N 1591 C CA . LEU A 255 ? 0.2865 0.3429 0.4461 0.0688 0.0642 -0.0795 248 LEU A CA 1592 C C . LEU A 255 ? 0.2948 0.3490 0.4579 0.0727 0.0725 -0.0849 248 LEU A C 1593 O O . LEU A 255 ? 0.3074 0.3695 0.4816 0.0736 0.0802 -0.0874 248 LEU A O 1594 C CB . LEU A 255 ? 0.2759 0.3345 0.4245 0.0624 0.0684 -0.0779 248 LEU A CB 1595 C CG . LEU A 255 ? 0.2998 0.3485 0.4277 0.0595 0.0720 -0.0794 248 LEU A CG 1596 C CD1 . LEU A 255 ? 0.2926 0.3317 0.4075 0.0580 0.0640 -0.0769 248 LEU A CD1 1597 C CD2 . LEU A 255 ? 0.3016 0.3543 0.4221 0.0544 0.0776 -0.0782 248 LEU A CD2 1598 N N . PRO A 256 ? 0.3023 0.3452 0.4562 0.0750 0.0712 -0.0869 249 PRO A N 1599 C CA . PRO A 256 ? 0.3137 0.3533 0.4681 0.0784 0.0795 -0.0926 249 PRO A CA 1600 C C . PRO A 256 ? 0.3220 0.3589 0.4609 0.0744 0.0879 -0.0950 249 PRO A C 1601 O O . PRO A 256 ? 0.3197 0.3549 0.4450 0.0689 0.0860 -0.0922 249 PRO A O 1602 C CB . PRO A 256 ? 0.3184 0.3457 0.4669 0.0815 0.0746 -0.0938 249 PRO A CB 1603 C CG . PRO A 256 ? 0.3150 0.3380 0.4555 0.0785 0.0657 -0.0886 249 PRO A CG 1604 C CD . PRO A 256 ? 0.3055 0.3381 0.4481 0.0744 0.0632 -0.0842 249 PRO A CD 1605 N N . GLY A 257 ? 0.3333 0.3692 0.4737 0.0778 0.0970 -0.1004 250 GLY A N 1606 C CA . GLY A 257 ? 0.3459 0.3788 0.4710 0.0753 0.1058 -0.1031 250 GLY A CA 1607 C C . GLY A 257 ? 0.3498 0.3705 0.4522 0.0720 0.1022 -0.1039 250 GLY A C 1608 O O . GLY A 257 ? 0.3539 0.3723 0.4411 0.0686 0.1064 -0.1045 250 GLY A O 1609 N N . GLY A 258 ? 0.3475 0.3599 0.4481 0.0730 0.0942 -0.1039 251 GLY A N 1610 C CA . GLY A 258 ? 0.3435 0.3448 0.4260 0.0695 0.0894 -0.1044 251 GLY A CA 1611 C C . GLY A 258 ? 0.3378 0.3405 0.4158 0.0641 0.0813 -0.0982 251 GLY A C 1612 O O . GLY A 258 ? 0.3335 0.3286 0.3974 0.0605 0.0778 -0.0982 251 GLY A O 1613 N N . GLY A 259 ? 0.3279 0.3400 0.4181 0.0638 0.0783 -0.0932 252 GLY A N 1614 C CA . GLY A 259 ? 0.3071 0.3210 0.3930 0.0591 0.0712 -0.0873 252 GLY A CA 1615 C C . GLY A 259 ? 0.3070 0.3229 0.3805 0.0538 0.0737 -0.0861 252 GLY A C 1616 O O . GLY A 259 ? 0.2974 0.3177 0.3699 0.0537 0.0813 -0.0880 252 GLY A O 1617 N N . VAL A 260 ? 0.3027 0.3153 0.3669 0.0497 0.0675 -0.0828 253 VAL A N 1618 C CA . VAL A 260 ? 0.2954 0.3087 0.3469 0.0448 0.0683 -0.0813 253 VAL A CA 1619 C C . VAL A 260 ? 0.2923 0.3084 0.3437 0.0413 0.0613 -0.0755 253 VAL A C 1620 O O . VAL A 260 ? 0.2823 0.2945 0.3351 0.0415 0.0551 -0.0734 253 VAL A O 1621 C CB . VAL A 260 ? 0.3042 0.3074 0.3390 0.0432 0.0686 -0.0853 253 VAL A CB 1622 C CG1 . VAL A 260 ? 0.2861 0.2902 0.3075 0.0389 0.0696 -0.0839 253 VAL A CG1 1623 C CG2 . VAL A 260 ? 0.3364 0.3345 0.3694 0.0473 0.0750 -0.0920 253 VAL A CG2 1624 N N . GLN A 261 ? 0.2666 0.2890 0.3161 0.0383 0.0626 -0.0727 254 GLN A N 1625 C CA . GLN A 261 ? 0.2716 0.2963 0.3196 0.0350 0.0566 -0.0676 254 GLN A CA 1626 C C . GLN A 261 ? 0.2715 0.2903 0.3044 0.0311 0.0541 -0.0673 254 GLN A C 1627 O O . GLN A 261 ? 0.2898 0.3080 0.3130 0.0292 0.0577 -0.0686 254 GLN A O 1628 C CB . GLN A 261 ? 0.2428 0.2767 0.2969 0.0336 0.0591 -0.0650 254 GLN A CB 1629 C CG . GLN A 261 ? 0.2415 0.2783 0.2945 0.0304 0.0528 -0.0599 254 GLN A CG 1630 C CD . GLN A 261 ? 0.2520 0.2963 0.3091 0.0283 0.0559 -0.0579 254 GLN A CD 1631 O OE1 . GLN A 261 ? 0.2410 0.2854 0.2909 0.0249 0.0539 -0.0551 254 GLN A OE1 1632 N NE2 . GLN A 261 ? 0.2115 0.2619 0.2811 0.0303 0.0610 -0.0594 254 GLN A NE2 1633 N N . ARG A 262 ? 0.2664 0.2805 0.2973 0.0301 0.0480 -0.0655 255 ARG A N 1634 C CA . ARG A 262 ? 0.2777 0.2881 0.2976 0.0261 0.0445 -0.0644 255 ARG A CA 1635 C C . ARG A 262 ? 0.2640 0.2805 0.2826 0.0233 0.0427 -0.0599 255 ARG A C 1636 O O . ARG A 262 ? 0.2466 0.2696 0.2736 0.0242 0.0432 -0.0574 255 ARG A O 1637 C CB . ARG A 262 ? 0.2484 0.2528 0.2692 0.0257 0.0392 -0.0633 255 ARG A CB 1638 C CG . ARG A 262 ? 0.2856 0.2819 0.3057 0.0277 0.0402 -0.0682 255 ARG A CG 1639 C CD . ARG A 262 ? 0.2845 0.2759 0.3110 0.0288 0.0365 -0.0660 255 ARG A CD 1640 N NE . ARG A 262 ? 0.2909 0.2747 0.3192 0.0313 0.0378 -0.0705 255 ARG A NE 1641 C CZ . ARG A 262 ? 0.3097 0.2939 0.3444 0.0358 0.0410 -0.0728 255 ARG A CZ 1642 N NH1 . ARG A 262 ? 0.2753 0.2679 0.3165 0.0380 0.0432 -0.0710 255 ARG A NH1 1643 N NH2 . ARG A 262 ? 0.2892 0.2655 0.3251 0.0380 0.0419 -0.0770 255 ARG A NH2 1644 N N . GLY A 263 ? 0.2611 0.2753 0.2701 0.0199 0.0402 -0.0590 256 GLY A N 1645 C CA . GLY A 263 ? 0.2324 0.2514 0.2405 0.0174 0.0377 -0.0544 256 GLY A CA 1646 C C . GLY A 263 ? 0.2544 0.2714 0.2507 0.0143 0.0367 -0.0546 256 GLY A C 1647 O O . GLY A 263 ? 0.2569 0.2706 0.2446 0.0143 0.0398 -0.0580 256 GLY A O 1648 N N . ASN A 264 ? 0.2434 0.2621 0.2387 0.0120 0.0324 -0.0509 257 ASN A N 1649 C CA . ASN A 264 ? 0.2550 0.2718 0.2397 0.0094 0.0307 -0.0509 257 ASN A CA 1650 C C . ASN A 264 ? 0.2555 0.2753 0.2354 0.0089 0.0347 -0.0498 257 ASN A C 1651 O O . ASN A 264 ? 0.2476 0.2724 0.2349 0.0097 0.0376 -0.0480 257 ASN A O 1652 C CB . ASN A 264 ? 0.2458 0.2635 0.2315 0.0073 0.0252 -0.0474 257 ASN A CB 1653 C CG . ASN A 264 ? 0.2658 0.2892 0.2545 0.0068 0.0248 -0.0429 257 ASN A CG 1654 O OD1 . ASN A 264 ? 0.2730 0.2979 0.2561 0.0055 0.0257 -0.0419 257 ASN A OD1 1655 N ND2 . ASN A 264 ? 0.2316 0.2576 0.2285 0.0080 0.0234 -0.0403 257 ASN A ND2 1656 N N . ILE A 265 ? 0.2521 0.2684 0.2199 0.0076 0.0345 -0.0509 258 ILE A N 1657 C CA . ILE A 265 ? 0.2697 0.2871 0.2308 0.0073 0.0389 -0.0497 258 ILE A CA 1658 C C . ILE A 265 ? 0.2755 0.2923 0.2289 0.0051 0.0348 -0.0467 258 ILE A C 1659 O O . ILE A 265 ? 0.3024 0.3164 0.2445 0.0048 0.0369 -0.0465 258 ILE A O 1660 C CB . ILE A 265 ? 0.2856 0.2976 0.2361 0.0089 0.0439 -0.0540 258 ILE A CB 1661 C CG1 . ILE A 265 ? 0.2894 0.2944 0.2303 0.0088 0.0387 -0.0580 258 ILE A CG1 1662 C CG2 . ILE A 265 ? 0.2986 0.3125 0.2581 0.0115 0.0496 -0.0564 258 ILE A CG2 1663 C CD1 . ILE A 265 ? 0.3702 0.3682 0.2963 0.0107 0.0424 -0.0629 258 ILE A CD1 1664 N N . LEU A 266 ? 0.2716 0.2906 0.2309 0.0039 0.0292 -0.0444 259 LEU A N 1665 C CA . LEU A 266 ? 0.2795 0.2986 0.2335 0.0021 0.0249 -0.0415 259 LEU A CA 1666 C C . LEU A 266 ? 0.2848 0.3075 0.2401 0.0015 0.0274 -0.0374 259 LEU A C 1667 O O . LEU A 266 ? 0.2781 0.3046 0.2419 0.0020 0.0310 -0.0365 259 LEU A O 1668 C CB . LEU A 266 ? 0.2575 0.2783 0.2188 0.0013 0.0193 -0.0401 259 LEU A CB 1669 C CG . LEU A 266 ? 0.2585 0.2756 0.2201 0.0011 0.0159 -0.0435 259 LEU A CG 1670 C CD1 . LEU A 266 ? 0.2523 0.2718 0.2230 0.0004 0.0123 -0.0409 259 LEU A CD1 1671 C CD2 . LEU A 266 ? 0.2835 0.2960 0.2337 0.0003 0.0125 -0.0461 259 LEU A CD2 1672 N N . ASN A 267 ? 0.2811 0.3023 0.2287 0.0003 0.0250 -0.0351 260 ASN A N 1673 C CA . ASN A 267 ? 0.2664 0.2904 0.2163 -0.0005 0.0257 -0.0309 260 ASN A CA 1674 C C . ASN A 267 ? 0.2681 0.2930 0.2188 -0.0013 0.0194 -0.0287 260 ASN A C 1675 O O . ASN A 267 ? 0.2671 0.2894 0.2094 -0.0018 0.0171 -0.0273 260 ASN A O 1676 C CB . ASN A 267 ? 0.2944 0.3149 0.2331 -0.0007 0.0302 -0.0297 260 ASN A CB 1677 C CG . ASN A 267 ? 0.3066 0.3282 0.2486 -0.0001 0.0382 -0.0307 260 ASN A CG 1678 O OD1 . ASN A 267 ? 0.3293 0.3552 0.2812 -0.0007 0.0412 -0.0285 260 ASN A OD1 1679 N ND2 . ASN A 267 ? 0.3176 0.3356 0.2528 0.0013 0.0414 -0.0344 260 ASN A ND2 1680 N N . LEU A 268 ? 0.2520 0.2801 0.2126 -0.0011 0.0168 -0.0285 261 LEU A N 1681 C CA . LEU A 268 ? 0.2445 0.2736 0.2070 -0.0015 0.0116 -0.0268 261 LEU A CA 1682 C C . LEU A 268 ? 0.2407 0.2720 0.2052 -0.0018 0.0108 -0.0232 261 LEU A C 1683 O O . LEU A 268 ? 0.2043 0.2356 0.1678 -0.0020 0.0069 -0.0216 261 LEU A O 1684 C CB . LEU A 268 ? 0.2360 0.2671 0.2078 -0.0008 0.0102 -0.0274 261 LEU A CB 1685 C CG . LEU A 268 ? 0.2273 0.2556 0.1988 -0.0007 0.0095 -0.0308 261 LEU A CG 1686 C CD1 . LEU A 268 ? 0.2217 0.2513 0.2026 0.0000 0.0090 -0.0303 261 LEU A CD1 1687 C CD2 . LEU A 268 ? 0.2436 0.2695 0.2094 -0.0019 0.0051 -0.0319 261 LEU A CD2 1688 N N . ASN A 269 ? 0.2237 0.2569 0.1922 -0.0017 0.0143 -0.0221 262 ASN A N 1689 C CA . ASN A 269 ? 0.2411 0.2759 0.2127 -0.0021 0.0131 -0.0190 262 ASN A CA 1690 C C . ASN A 269 ? 0.2468 0.2833 0.2229 -0.0011 0.0088 -0.0180 262 ASN A C 1691 O O . ASN A 269 ? 0.2420 0.2782 0.2168 -0.0012 0.0062 -0.0159 262 ASN A O 1692 C CB . ASN A 269 ? 0.2526 0.2841 0.2154 -0.0031 0.0135 -0.0169 262 ASN A CB 1693 C CG . ASN A 269 ? 0.3014 0.3310 0.2601 -0.0038 0.0194 -0.0171 262 ASN A CG 1694 O OD1 . ASN A 269 ? 0.3118 0.3442 0.2783 -0.0039 0.0232 -0.0178 262 ASN A OD1 1695 N ND2 . ASN A 269 ? 0.2933 0.3182 0.2402 -0.0040 0.0202 -0.0165 262 ASN A ND2 1696 N N . GLY A 270 ? 0.2176 0.2554 0.1988 0.0000 0.0083 -0.0193 263 GLY A N 1697 C CA . GLY A 270 ? 0.2161 0.2551 0.2011 0.0012 0.0054 -0.0181 263 GLY A CA 1698 C C . GLY A 270 ? 0.2303 0.2686 0.2137 0.0009 0.0029 -0.0179 263 GLY A C 1699 O O . GLY A 270 ? 0.2354 0.2746 0.2218 0.0020 0.0014 -0.0166 263 GLY A O 1700 N N . ALA A 271 ? 0.2250 0.2614 0.2039 -0.0003 0.0025 -0.0195 264 ALA A N 1701 C CA . ALA A 271 ? 0.2160 0.2523 0.1952 -0.0008 -0.0007 -0.0197 264 ALA A CA 1702 C C . ALA A 271 ? 0.2099 0.2467 0.1956 -0.0005 -0.0007 -0.0204 264 ALA A C 1703 O O . ALA A 271 ? 0.2190 0.2569 0.2084 -0.0007 -0.0028 -0.0195 264 ALA A O 1704 C CB . ALA A 271 ? 0.2075 0.2410 0.1793 -0.0020 -0.0025 -0.0218 264 ALA A CB 1705 N N . GLY A 272 ? 0.1988 0.2347 0.1865 0.0000 0.0017 -0.0216 265 GLY A N 1706 C CA . GLY A 272 ? 0.2185 0.2534 0.2116 0.0000 0.0021 -0.0221 265 GLY A CA 1707 C C . GLY A 272 ? 0.2360 0.2685 0.2282 -0.0017 0.0006 -0.0254 265 GLY A C 1708 O O . GLY A 272 ? 0.2426 0.2734 0.2285 -0.0021 0.0006 -0.0278 265 GLY A O 1709 N N . ASP A 273 ? 0.2144 0.2466 0.2127 -0.0026 -0.0005 -0.0256 266 ASP A N 1710 C CA . ASP A 273 ? 0.2278 0.2575 0.2263 -0.0044 -0.0031 -0.0294 266 ASP A CA 1711 C C . ASP A 273 ? 0.2447 0.2741 0.2355 -0.0051 -0.0067 -0.0313 266 ASP A C 1712 O O . ASP A 273 ? 0.2220 0.2539 0.2126 -0.0051 -0.0090 -0.0293 266 ASP A O 1713 C CB . ASP A 273 ? 0.2274 0.2581 0.2358 -0.0058 -0.0044 -0.0286 266 ASP A CB 1714 C CG . ASP A 273 ? 0.2534 0.2824 0.2638 -0.0079 -0.0088 -0.0327 266 ASP A CG 1715 O OD1 . ASP A 273 ? 0.2337 0.2586 0.2396 -0.0083 -0.0094 -0.0366 266 ASP A OD1 1716 O OD2 . ASP A 273 ? 0.2416 0.2734 0.2585 -0.0091 -0.0119 -0.0322 266 ASP A OD2 1717 N N . PRO A 274 ? 0.2564 0.2821 0.2398 -0.0053 -0.0071 -0.0350 267 PRO A N 1718 C CA . PRO A 274 ? 0.2609 0.2848 0.2339 -0.0052 -0.0099 -0.0364 267 PRO A CA 1719 C C . PRO A 274 ? 0.2627 0.2877 0.2379 -0.0062 -0.0163 -0.0370 267 PRO A C 1720 O O . PRO A 274 ? 0.2706 0.2952 0.2383 -0.0057 -0.0194 -0.0364 267 PRO A O 1721 C CB . PRO A 274 ? 0.2656 0.2844 0.2320 -0.0051 -0.0093 -0.0413 267 PRO A CB 1722 C CG . PRO A 274 ? 0.2775 0.2963 0.2483 -0.0043 -0.0039 -0.0410 267 PRO A CG 1723 C CD . PRO A 274 ? 0.2546 0.2771 0.2373 -0.0047 -0.0036 -0.0374 267 PRO A CD 1724 N N . LEU A 275 ? 0.2435 0.2698 0.2298 -0.0076 -0.0182 -0.0380 268 LEU A N 1725 C CA . LEU A 275 ? 0.2424 0.2702 0.2334 -0.0087 -0.0248 -0.0393 268 LEU A CA 1726 C C . LEU A 275 ? 0.2187 0.2521 0.2182 -0.0084 -0.0253 -0.0351 268 LEU A C 1727 O O . LEU A 275 ? 0.2317 0.2672 0.2349 -0.0088 -0.0309 -0.0358 268 LEU A O 1728 C CB . LEU A 275 ? 0.2578 0.2841 0.2582 -0.0106 -0.0270 -0.0430 268 LEU A CB 1729 C CG . LEU A 275 ? 0.2702 0.2902 0.2626 -0.0106 -0.0274 -0.0482 268 LEU A CG 1730 C CD1 . LEU A 275 ? 0.2963 0.3149 0.3004 -0.0130 -0.0307 -0.0519 268 LEU A CD1 1731 C CD2 . LEU A 275 ? 0.2848 0.3007 0.2608 -0.0092 -0.0312 -0.0511 268 LEU A CD2 1732 N N . THR A 276 ? 0.2296 0.2654 0.2319 -0.0075 -0.0200 -0.0310 269 THR A N 1733 C CA . THR A 276 ? 0.2060 0.2466 0.2168 -0.0070 -0.0196 -0.0274 269 THR A CA 1734 C C . THR A 276 ? 0.2181 0.2598 0.2235 -0.0049 -0.0166 -0.0236 269 THR A C 1735 O O . THR A 276 ? 0.2220 0.2658 0.2327 -0.0039 -0.0129 -0.0207 269 THR A O 1736 C CB . THR A 276 ? 0.2092 0.2515 0.2329 -0.0078 -0.0160 -0.0260 269 THR A CB 1737 O OG1 . THR A 276 ? 0.1942 0.2336 0.2144 -0.0070 -0.0109 -0.0252 269 THR A OG1 1738 C CG2 . THR A 276 ? 0.1915 0.2336 0.2253 -0.0104 -0.0195 -0.0294 269 THR A CG2 1739 N N . PRO A 277 ? 0.2364 0.2759 0.2307 -0.0042 -0.0176 -0.0238 270 PRO A N 1740 C CA . PRO A 277 ? 0.2244 0.2644 0.2149 -0.0027 -0.0145 -0.0206 270 PRO A CA 1741 C C . PRO A 277 ? 0.2186 0.2620 0.2148 -0.0015 -0.0156 -0.0178 270 PRO A C 1742 O O . PRO A 277 ? 0.2180 0.2627 0.2159 -0.0015 -0.0200 -0.0181 270 PRO A O 1743 C CB . PRO A 277 ? 0.2514 0.2882 0.2302 -0.0025 -0.0157 -0.0211 270 PRO A CB 1744 C CG . PRO A 277 ? 0.2556 0.2911 0.2319 -0.0032 -0.0214 -0.0237 270 PRO A CG 1745 C CD . PRO A 277 ? 0.2549 0.2910 0.2394 -0.0046 -0.0214 -0.0265 270 PRO A CD 1746 N N . GLY A 278 ? 0.2232 0.2679 0.2223 -0.0001 -0.0119 -0.0155 271 GLY A N 1747 C CA . GLY A 278 ? 0.2142 0.2615 0.2176 0.0015 -0.0118 -0.0130 271 GLY A CA 1748 C C . GLY A 278 ? 0.2143 0.2641 0.2274 0.0019 -0.0093 -0.0120 271 GLY A C 1749 O O . GLY A 278 ? 0.2242 0.2754 0.2398 0.0040 -0.0073 -0.0098 271 GLY A O 1750 N N . TYR A 279 ? 0.2033 0.2532 0.2221 0.0000 -0.0093 -0.0136 272 TYR A N 1751 C CA . TYR A 279 ? 0.2113 0.2638 0.2414 -0.0001 -0.0071 -0.0125 272 TYR A CA 1752 C C . TYR A 279 ? 0.1930 0.2430 0.2257 -0.0014 -0.0039 -0.0131 272 TYR A C 1753 O O . TYR A 279 ? 0.1979 0.2452 0.2264 -0.0029 -0.0055 -0.0157 272 TYR A O 1754 C CB . TYR A 279 ? 0.1957 0.2517 0.2343 -0.0015 -0.0116 -0.0139 272 TYR A CB 1755 C CG . TYR A 279 ? 0.2119 0.2695 0.2469 0.0001 -0.0153 -0.0133 272 TYR A CG 1756 C CD1 . TYR A 279 ? 0.1891 0.2495 0.2285 0.0025 -0.0133 -0.0107 272 TYR A CD1 1757 C CD2 . TYR A 279 ? 0.1903 0.2456 0.2162 -0.0002 -0.0203 -0.0151 272 TYR A CD2 1758 C CE1 . TYR A 279 ? 0.1628 0.2236 0.1983 0.0042 -0.0166 -0.0101 272 TYR A CE1 1759 C CE2 . TYR A 279 ? 0.2191 0.2744 0.2405 0.0014 -0.0233 -0.0140 272 TYR A CE2 1760 C CZ . TYR A 279 ? 0.2009 0.2592 0.2279 0.0036 -0.0218 -0.0116 272 TYR A CZ 1761 O OH . TYR A 279 ? 0.1844 0.2422 0.2071 0.0054 -0.0251 -0.0105 272 TYR A OH 1762 N N . PRO A 280 ? 0.2050 0.2552 0.2443 -0.0007 0.0008 -0.0105 273 PRO A N 1763 C CA . PRO A 280 ? 0.2187 0.2655 0.2600 -0.0018 0.0037 -0.0107 273 PRO A CA 1764 C C . PRO A 280 ? 0.2189 0.2659 0.2688 -0.0053 0.0007 -0.0139 273 PRO A C 1765 O O . PRO A 280 ? 0.2139 0.2647 0.2732 -0.0067 -0.0016 -0.0145 273 PRO A O 1766 C CB . PRO A 280 ? 0.2199 0.2663 0.2660 0.0000 0.0099 -0.0066 273 PRO A CB 1767 C CG . PRO A 280 ? 0.2056 0.2568 0.2571 0.0009 0.0099 -0.0051 273 PRO A CG 1768 C CD . PRO A 280 ? 0.2166 0.2693 0.2605 0.0014 0.0045 -0.0071 273 PRO A CD 1769 N N . ALA A 281 ? 0.2045 0.2474 0.2517 -0.0064 0.0007 -0.0161 274 ALA A N 1770 C CA . ALA A 281 ? 0.1990 0.2407 0.2532 -0.0096 -0.0023 -0.0198 274 ALA A CA 1771 C C . ALA A 281 ? 0.2138 0.2552 0.2815 -0.0110 0.0017 -0.0176 274 ALA A C 1772 O O . ALA A 281 ? 0.2085 0.2453 0.2786 -0.0120 0.0041 -0.0179 274 ALA A O 1773 C CB . ALA A 281 ? 0.2269 0.2636 0.2727 -0.0097 -0.0031 -0.0229 274 ALA A CB 1774 N N . ASN A 282 ? 0.2303 0.2765 0.3072 -0.0111 0.0029 -0.0151 275 ASN A N 1775 C CA . ASN A 282 ? 0.2472 0.2937 0.3374 -0.0124 0.0080 -0.0122 275 ASN A CA 1776 C C . ASN A 282 ? 0.2710 0.3190 0.3760 -0.0165 0.0039 -0.0159 275 ASN A C 1777 O O . ASN A 282 ? 0.2642 0.3117 0.3663 -0.0180 -0.0031 -0.0211 275 ASN A O 1778 C CB . ASN A 282 ? 0.2639 0.3147 0.3572 -0.0100 0.0125 -0.0077 275 ASN A CB 1779 C CG . ASN A 282 ? 0.2434 0.3007 0.3418 -0.0102 0.0073 -0.0095 275 ASN A CG 1780 O OD1 . ASN A 282 ? 0.2404 0.2997 0.3448 -0.0128 0.0008 -0.0137 275 ASN A OD1 1781 N ND2 . ASN A 282 ? 0.2785 0.3386 0.3733 -0.0070 0.0097 -0.0066 275 ASN A ND2 1782 N N A GLU A 283 ? 0.2854 0.3352 0.4064 -0.0184 0.0082 -0.0135 276 GLU A N 1783 N N B GLU A 283 ? 0.2824 0.3321 0.4032 -0.0183 0.0084 -0.0134 276 GLU A N 1784 C CA A GLU A 283 ? 0.2992 0.3498 0.4363 -0.0228 0.0042 -0.0173 276 GLU A CA 1785 C CA B GLU A 283 ? 0.2955 0.3465 0.4334 -0.0227 0.0050 -0.0167 276 GLU A CA 1786 C C A GLU A 283 ? 0.2970 0.3545 0.4434 -0.0242 -0.0035 -0.0210 276 GLU A C 1787 C C B GLU A 283 ? 0.2930 0.3496 0.4349 -0.0237 -0.0043 -0.0215 276 GLU A C 1788 O O A GLU A 283 ? 0.3048 0.3628 0.4631 -0.0277 -0.0091 -0.0255 276 GLU A O 1789 O O B GLU A 283 ? 0.2974 0.3524 0.4421 -0.0263 -0.0115 -0.0272 276 GLU A O 1790 C CB A GLU A 283 ? 0.3138 0.3631 0.4667 -0.0250 0.0119 -0.0135 276 GLU A CB 1791 C CB B GLU A 283 ? 0.3025 0.3559 0.4584 -0.0242 0.0125 -0.0121 276 GLU A CB 1792 C CG A GLU A 283 ? 0.3494 0.3903 0.5005 -0.0264 0.0141 -0.0139 276 GLU A CG 1793 C CG B GLU A 283 ? 0.3371 0.3860 0.5062 -0.0282 0.0143 -0.0130 276 GLU A CG 1794 C CD A GLU A 283 ? 0.3948 0.4342 0.5577 -0.0310 0.0075 -0.0201 276 GLU A CD 1795 C CD B GLU A 283 ? 0.3745 0.4143 0.5324 -0.0268 0.0203 -0.0100 276 GLU A CD 1796 O OE1 A GLU A 283 ? 0.3976 0.4420 0.5671 -0.0327 -0.0004 -0.0249 276 GLU A OE1 1797 O OE1 B GLU A 283 ? 0.3978 0.4358 0.5454 -0.0230 0.0270 -0.0046 276 GLU A OE1 1798 O OE2 A GLU A 283 ? 0.4231 0.4555 0.5884 -0.0326 0.0099 -0.0203 276 GLU A OE2 1799 O OE2 B GLU A 283 ? 0.3739 0.4079 0.5333 -0.0291 0.0180 -0.0132 276 GLU A OE2 1800 N N . TYR A 284 ? 0.2794 0.3418 0.4206 -0.0214 -0.0045 -0.0195 277 TYR A N 1801 C CA . TYR A 284 ? 0.2880 0.3563 0.4359 -0.0220 -0.0131 -0.0231 277 TYR A CA 1802 C C . TYR A 284 ? 0.2874 0.3543 0.4166 -0.0194 -0.0194 -0.0254 277 TYR A C 1803 O O . TYR A 284 ? 0.3068 0.3777 0.4381 -0.0188 -0.0260 -0.0274 277 TYR A O 1804 C CB . TYR A 284 ? 0.2550 0.3312 0.4184 -0.0212 -0.0099 -0.0198 277 TYR A CB 1805 C CG . TYR A 284 ? 0.2731 0.3495 0.4259 -0.0171 -0.0029 -0.0146 277 TYR A CG 1806 C CD1 . TYR A 284 ? 0.3001 0.3785 0.4419 -0.0139 -0.0069 -0.0148 277 TYR A CD1 1807 C CD2 . TYR A 284 ? 0.2574 0.3311 0.4101 -0.0161 0.0075 -0.0094 277 TYR A CD2 1808 C CE1 . TYR A 284 ? 0.2826 0.3607 0.4149 -0.0100 -0.0011 -0.0106 277 TYR A CE1 1809 C CE2 . TYR A 284 ? 0.2965 0.3696 0.4379 -0.0118 0.0130 -0.0053 277 TYR A CE2 1810 C CZ . TYR A 284 ? 0.2961 0.3716 0.4278 -0.0090 0.0083 -0.0063 277 TYR A CZ 1811 O OH . TYR A 284 ? 0.3030 0.3773 0.4238 -0.0048 0.0134 -0.0027 277 TYR A OH 1812 N N . ALA A 285 ? 0.2938 0.3548 0.4056 -0.0178 -0.0172 -0.0250 278 ALA A N 1813 C CA . ALA A 285 ? 0.3146 0.3739 0.4087 -0.0154 -0.0213 -0.0262 278 ALA A CA 1814 C C . ALA A 285 ? 0.3160 0.3748 0.4076 -0.0165 -0.0311 -0.0318 278 ALA A C 1815 O O . ALA A 285 ? 0.3453 0.4020 0.4435 -0.0192 -0.0347 -0.0359 278 ALA A O 1816 C CB . ALA A 285 ? 0.3176 0.3708 0.3971 -0.0143 -0.0173 -0.0256 278 ALA A CB 1817 N N . TYR A 286 ? 0.3073 0.3674 0.3903 -0.0144 -0.0358 -0.0319 279 TYR A N 1818 C CA . TYR A 286 ? 0.3064 0.3640 0.3816 -0.0145 -0.0451 -0.0368 279 TYR A CA 1819 C C . TYR A 286 ? 0.3152 0.3661 0.3706 -0.0133 -0.0435 -0.0376 279 TYR A C 1820 O O . TYR A 286 ? 0.3223 0.3725 0.3688 -0.0115 -0.0380 -0.0339 279 TYR A O 1821 C CB . TYR A 286 ? 0.3362 0.3975 0.4105 -0.0123 -0.0514 -0.0364 279 TYR A CB 1822 C CG A TYR A 286 ? 0.2838 0.3424 0.3519 -0.0122 -0.0619 -0.0415 279 TYR A CG 1823 C CG B TYR A 286 ? 0.3367 0.3925 0.3904 -0.0103 -0.0568 -0.0382 279 TYR A CG 1824 C CD1 A TYR A 286 ? 0.2916 0.3526 0.3741 -0.0143 -0.0690 -0.0460 279 TYR A CD1 1825 C CD1 B TYR A 286 ? 0.3557 0.4101 0.4068 -0.0099 -0.0667 -0.0425 279 TYR A CD1 1826 C CD2 A TYR A 286 ? 0.2808 0.3338 0.3280 -0.0099 -0.0647 -0.0420 279 TYR A CD2 1827 C CD2 B TYR A 286 ? 0.3575 0.4089 0.3946 -0.0087 -0.0517 -0.0358 279 TYR A CD2 1828 C CE1 A TYR A 286 ? 0.3019 0.3595 0.3770 -0.0136 -0.0796 -0.0511 279 TYR A CE1 1829 C CE1 B TYR A 286 ? 0.3758 0.4241 0.4067 -0.0078 -0.0709 -0.0436 279 TYR A CE1 1830 C CE2 A TYR A 286 ? 0.3075 0.3567 0.3462 -0.0092 -0.0741 -0.0465 279 TYR A CE2 1831 C CE2 B TYR A 286 ? 0.3774 0.4233 0.3960 -0.0070 -0.0553 -0.0369 279 TYR A CE2 1832 C CZ A TYR A 286 ? 0.3256 0.3769 0.3774 -0.0108 -0.0819 -0.0512 279 TYR A CZ 1833 C CZ B TYR A 286 ? 0.3915 0.4356 0.4063 -0.0064 -0.0646 -0.0406 279 TYR A CZ 1834 O OH A TYR A 286 ? 0.3796 0.4263 0.4208 -0.0095 -0.0920 -0.0560 279 TYR A OH 1835 O OH B TYR A 286 ? 0.4245 0.4622 0.4196 -0.0043 -0.0678 -0.0413 279 TYR A OH 1836 N N . ARG A 287 ? 0.2743 0.3202 0.3239 -0.0144 -0.0476 -0.0425 280 ARG A N 1837 C CA . ARG A 287 ? 0.2867 0.3263 0.3189 -0.0134 -0.0450 -0.0435 280 ARG A CA 1838 C C . ARG A 287 ? 0.3007 0.3366 0.3172 -0.0116 -0.0513 -0.0461 280 ARG A C 1839 O O . ARG A 287 ? 0.2835 0.3194 0.3023 -0.0119 -0.0597 -0.0499 280 ARG A O 1840 C CB A ARG A 287 ? 0.2973 0.3326 0.3325 -0.0153 -0.0435 -0.0472 280 ARG A CB 1841 C CB B ARG A 287 ? 0.2772 0.3123 0.3120 -0.0153 -0.0442 -0.0475 280 ARG A CB 1842 C CG A ARG A 287 ? 0.3022 0.3374 0.3423 -0.0156 -0.0344 -0.0435 280 ARG A CG 1843 C CG B ARG A 287 ? 0.2255 0.2622 0.2729 -0.0167 -0.0371 -0.0446 280 ARG A CG 1844 C CD A ARG A 287 ? 0.3860 0.4235 0.4447 -0.0181 -0.0325 -0.0427 280 ARG A CD 1845 C CD B ARG A 287 ? 0.1263 0.1573 0.1737 -0.0181 -0.0354 -0.0479 280 ARG A CD 1846 N NE A ARG A 287 ? 0.3532 0.3897 0.4143 -0.0177 -0.0240 -0.0385 280 ARG A NE 1847 N NE B ARG A 287 ? 0.0985 0.1301 0.1539 -0.0184 -0.0276 -0.0436 280 ARG A NE 1848 C CZ A ARG A 287 ? 0.3647 0.4039 0.4396 -0.0187 -0.0196 -0.0349 280 ARG A CZ 1849 C CZ B ARG A 287 ? 0.0919 0.1268 0.1636 -0.0202 -0.0254 -0.0411 280 ARG A CZ 1850 N NH1 A ARG A 287 ? 0.3875 0.4315 0.4770 -0.0205 -0.0224 -0.0350 280 ARG A NH1 1851 N NH1 B ARG A 287 ? 0.0973 0.1359 0.1812 -0.0222 -0.0308 -0.0430 280 ARG A NH1 1852 N NH2 A ARG A 287 ? 0.3188 0.3558 0.3930 -0.0177 -0.0124 -0.0311 280 ARG A NH2 1853 N NH2 B ARG A 287 ? 0.1022 0.1365 0.1782 -0.0198 -0.0178 -0.0366 280 ARG A NH2 1854 N N . ARG A 288 ? 0.2937 0.3264 0.2945 -0.0097 -0.0476 -0.0441 281 ARG A N 1855 C CA . ARG A 288 ? 0.3353 0.3625 0.3187 -0.0079 -0.0522 -0.0465 281 ARG A CA 1856 C C . ARG A 288 ? 0.3567 0.3783 0.3355 -0.0088 -0.0554 -0.0528 281 ARG A C 1857 O O . ARG A 288 ? 0.3388 0.3596 0.3244 -0.0104 -0.0514 -0.0543 281 ARG A O 1858 C CB . ARG A 288 ? 0.3258 0.3502 0.2951 -0.0063 -0.0458 -0.0433 281 ARG A CB 1859 C CG . ARG A 288 ? 0.3466 0.3751 0.3182 -0.0052 -0.0433 -0.0377 281 ARG A CG 1860 C CD . ARG A 288 ? 0.3720 0.3973 0.3305 -0.0040 -0.0376 -0.0351 281 ARG A CD 1861 N NE . ARG A 288 ? 0.3951 0.4234 0.3551 -0.0029 -0.0365 -0.0303 281 ARG A NE 1862 C CZ . ARG A 288 ? 0.4020 0.4276 0.3516 -0.0018 -0.0336 -0.0274 281 ARG A CZ 1863 N NH1 . ARG A 288 ? 0.4259 0.4462 0.3624 -0.0014 -0.0311 -0.0285 281 ARG A NH1 1864 N NH2 . ARG A 288 ? 0.4101 0.4382 0.3629 -0.0009 -0.0329 -0.0235 281 ARG A NH2 1865 N N . GLY A 289 ? 0.3757 0.3927 0.3424 -0.0073 -0.0627 -0.0564 282 GLY A N 1866 C CA . GLY A 289 ? 0.4169 0.4267 0.3739 -0.0072 -0.0652 -0.0626 282 GLY A CA 1867 C C . GLY A 289 ? 0.4218 0.4270 0.3646 -0.0059 -0.0567 -0.0614 282 GLY A C 1868 O O . GLY A 289 ? 0.4209 0.4275 0.3579 -0.0047 -0.0511 -0.0562 282 GLY A O 1869 N N . ILE A 290 ? 0.4422 0.4420 0.3804 -0.0060 -0.0556 -0.0663 283 ILE A N 1870 C CA . ILE A 290 ? 0.4526 0.4485 0.3796 -0.0047 -0.0470 -0.0658 283 ILE A CA 1871 C C . ILE A 290 ? 0.4695 0.4617 0.3769 -0.0019 -0.0447 -0.0634 283 ILE A C 1872 O O . ILE A 290 ? 0.4724 0.4655 0.3766 -0.0013 -0.0364 -0.0597 283 ILE A O 1873 C CB A ILE A 290 ? 0.4705 0.4602 0.3951 -0.0048 -0.0473 -0.0726 283 ILE A CB 1874 C CB B ILE A 290 ? 0.4646 0.4537 0.3872 -0.0045 -0.0471 -0.0726 283 ILE A CB 1875 C CG1 A ILE A 290 ? 0.4767 0.4653 0.4000 -0.0042 -0.0374 -0.0715 283 ILE A CG1 1876 C CG1 B ILE A 290 ? 0.4418 0.4338 0.3835 -0.0072 -0.0452 -0.0735 283 ILE A CG1 1877 C CG2 A ILE A 290 ? 0.4926 0.4740 0.3990 -0.0026 -0.0543 -0.0786 283 ILE A CG2 1878 C CG2 B ILE A 290 ? 0.4585 0.4428 0.3653 -0.0021 -0.0390 -0.0726 283 ILE A CG2 1879 C CD1 A ILE A 290 ? 0.4447 0.4397 0.3861 -0.0061 -0.0324 -0.0673 283 ILE A CD1 1880 C CD1 B ILE A 290 ? 0.4422 0.4376 0.3899 -0.0072 -0.0354 -0.0687 283 ILE A CD1 1881 N N . ALA A 291 ? 0.4928 0.4807 0.3877 -0.0002 -0.0522 -0.0654 284 ALA A N 1882 C CA . ALA A 291 ? 0.5050 0.4881 0.3800 0.0025 -0.0499 -0.0625 284 ALA A CA 1883 C C . ALA A 291 ? 0.5012 0.4896 0.3805 0.0022 -0.0454 -0.0550 284 ALA A C 1884 O O . ALA A 291 ? 0.5089 0.4942 0.3756 0.0037 -0.0395 -0.0517 284 ALA A O 1885 C CB . ALA A 291 ? 0.5385 0.5150 0.3981 0.0050 -0.0600 -0.0659 284 ALA A CB 1886 N N . GLU A 292 ? 0.4832 0.4794 0.3807 0.0003 -0.0477 -0.0525 285 GLU A N 1887 C CA . GLU A 292 ? 0.4664 0.4676 0.3689 0.0002 -0.0438 -0.0459 285 GLU A CA 1888 C C . GLU A 292 ? 0.4347 0.4415 0.3510 -0.0015 -0.0358 -0.0433 285 GLU A C 1889 O O . GLU A 292 ? 0.4339 0.4450 0.3560 -0.0017 -0.0330 -0.0385 285 GLU A O 1890 C CB . GLU A 292 ? 0.4660 0.4714 0.3771 0.0003 -0.0515 -0.0443 285 GLU A CB 1891 C CG . GLU A 292 ? 0.5304 0.5304 0.4274 0.0028 -0.0602 -0.0454 285 GLU A CG 1892 C CD . GLU A 292 ? 0.6450 0.6403 0.5367 0.0033 -0.0678 -0.0525 285 GLU A CD 1893 O OE1 . GLU A 292 ? 0.6550 0.6540 0.5619 0.0010 -0.0706 -0.0563 285 GLU A OE1 1894 O OE2 . GLU A 292 ? 0.7262 0.7132 0.5977 0.0060 -0.0712 -0.0543 285 GLU A OE2 1895 N N . ALA A 293 ? 0.4173 0.4235 0.3382 -0.0025 -0.0328 -0.0467 286 ALA A N 1896 C CA . ALA A 293 ? 0.4030 0.4136 0.3358 -0.0036 -0.0260 -0.0445 286 ALA A CA 1897 C C . ALA A 293 ? 0.4062 0.4171 0.3331 -0.0027 -0.0189 -0.0404 286 ALA A C 1898 O O . ALA A 293 ? 0.4063 0.4127 0.3190 -0.0014 -0.0174 -0.0403 286 ALA A O 1899 C CB . ALA A 293 ? 0.3947 0.4031 0.3310 -0.0042 -0.0240 -0.0488 286 ALA A CB 1900 N N . VAL A 294 ? 0.3686 0.3845 0.3064 -0.0033 -0.0148 -0.0372 287 VAL A N 1901 C CA . VAL A 294 ? 0.3649 0.3817 0.3000 -0.0027 -0.0089 -0.0337 287 VAL A CA 1902 C C . VAL A 294 ? 0.3510 0.3665 0.2853 -0.0024 -0.0027 -0.0356 287 VAL A C 1903 O O . VAL A 294 ? 0.3408 0.3575 0.2836 -0.0026 -0.0019 -0.0375 287 VAL A O 1904 C CB . VAL A 294 ? 0.3429 0.3653 0.2894 -0.0031 -0.0078 -0.0297 287 VAL A CB 1905 C CG1 . VAL A 294 ? 0.3298 0.3529 0.2748 -0.0027 -0.0022 -0.0268 287 VAL A CG1 1906 C CG2 . VAL A 294 ? 0.3612 0.3852 0.3093 -0.0030 -0.0133 -0.0277 287 VAL A CG2 1907 N N . GLY A 295 ? 0.3522 0.3649 0.2769 -0.0016 0.0017 -0.0349 288 GLY A N 1908 C CA . GLY A 295 ? 0.3474 0.3607 0.2743 -0.0011 0.0087 -0.0355 288 GLY A CA 1909 C C . GLY A 295 ? 0.3567 0.3662 0.2794 -0.0001 0.0111 -0.0404 288 GLY A C 1910 O O . GLY A 295 ? 0.3474 0.3582 0.2742 0.0005 0.0169 -0.0410 288 GLY A O 1911 N N . LEU A 296 ? 0.3425 0.3474 0.2576 0.0000 0.0063 -0.0441 289 LEU A N 1912 C CA . LEU A 296 ? 0.3706 0.3705 0.2797 0.0013 0.0080 -0.0495 289 LEU A CA 1913 C C . LEU A 296 ? 0.3753 0.3705 0.2699 0.0031 0.0139 -0.0501 289 LEU A C 1914 O O . LEU A 296 ? 0.3786 0.3710 0.2615 0.0035 0.0134 -0.0478 289 LEU A O 1915 C CB . LEU A 296 ? 0.3845 0.3802 0.2898 0.0010 0.0001 -0.0539 289 LEU A CB 1916 C CG . LEU A 296 ? 0.4072 0.4054 0.3270 -0.0006 -0.0045 -0.0555 289 LEU A CG 1917 C CD1 . LEU A 296 ? 0.4714 0.4765 0.4056 -0.0020 -0.0040 -0.0507 289 LEU A CD1 1918 C CD2 . LEU A 296 ? 0.4662 0.4612 0.3823 -0.0013 -0.0134 -0.0590 289 LEU A CD2 1919 N N . PRO A 297 ? 0.3850 0.3788 0.2799 0.0044 0.0198 -0.0531 290 PRO A N 1920 C CA . PRO A 297 ? 0.4055 0.3944 0.2864 0.0065 0.0266 -0.0541 290 PRO A CA 1921 C C . PRO A 297 ? 0.4319 0.4121 0.2946 0.0081 0.0224 -0.0585 290 PRO A C 1922 O O . PRO A 297 ? 0.4285 0.4063 0.2925 0.0078 0.0153 -0.0628 290 PRO A O 1923 C CB . PRO A 297 ? 0.4077 0.3982 0.2971 0.0077 0.0332 -0.0567 290 PRO A CB 1924 C CG . PRO A 297 ? 0.4025 0.3949 0.3045 0.0068 0.0278 -0.0591 290 PRO A CG 1925 C CD . PRO A 297 ? 0.3814 0.3772 0.2891 0.0044 0.0204 -0.0558 290 PRO A CD 1926 N N . SER A 298 ? 0.4467 0.4214 0.2923 0.0099 0.0268 -0.0575 291 SER A N 1927 C CA . SER A 298 ? 0.4800 0.4453 0.3053 0.0122 0.0225 -0.0617 291 SER A CA 1928 C C . SER A 298 ? 0.4752 0.4339 0.2893 0.0152 0.0286 -0.0671 291 SER A C 1929 O O . SER A 298 ? 0.4862 0.4359 0.2818 0.0177 0.0250 -0.0717 291 SER A O 1930 C CB . SER A 298 ? 0.5028 0.4644 0.3130 0.0129 0.0220 -0.0569 291 SER A CB 1931 O OG . SER A 298 ? 0.5644 0.5248 0.3681 0.0140 0.0335 -0.0534 291 SER A OG 1932 N N . ILE A 299 ? 0.4547 0.4176 0.2796 0.0154 0.0376 -0.0668 292 ILE A N 1933 C CA . ILE A 299 ? 0.4549 0.4124 0.2716 0.0186 0.0447 -0.0720 292 ILE A CA 1934 C C . ILE A 299 ? 0.4406 0.4025 0.2756 0.0183 0.0451 -0.0756 292 ILE A C 1935 O O . ILE A 299 ? 0.4252 0.3954 0.2794 0.0158 0.0441 -0.0723 292 ILE A O 1936 C CB . ILE A 299 ? 0.4543 0.4115 0.2642 0.0203 0.0573 -0.0684 292 ILE A CB 1937 C CG1 . ILE A 299 ? 0.4307 0.3987 0.2617 0.0177 0.0627 -0.0624 292 ILE A CG1 1938 C CG2 . ILE A 299 ? 0.4829 0.4327 0.2704 0.0216 0.0572 -0.0656 292 ILE A CG2 1939 C CD1 . ILE A 299 ? 0.4353 0.4038 0.2631 0.0188 0.0757 -0.0589 292 ILE A CD1 1940 N N . PRO A 300 ? 0.4457 0.4010 0.2741 0.0209 0.0461 -0.0826 293 PRO A N 1941 C CA . PRO A 300 ? 0.4331 0.3916 0.2787 0.0209 0.0465 -0.0857 293 PRO A CA 1942 C C . PRO A 300 ? 0.4209 0.3869 0.2805 0.0214 0.0566 -0.0824 293 PRO A C 1943 O O . PRO A 300 ? 0.4239 0.3900 0.2765 0.0230 0.0656 -0.0803 293 PRO A O 1944 C CB . PRO A 300 ? 0.4638 0.4122 0.2957 0.0244 0.0469 -0.0940 293 PRO A CB 1945 C CG . PRO A 300 ? 0.4739 0.4141 0.2830 0.0253 0.0417 -0.0957 293 PRO A CG 1946 C CD . PRO A 300 ? 0.4741 0.4183 0.2788 0.0244 0.0462 -0.0880 293 PRO A CD 1947 N N . VAL A 301 ? 0.3910 0.3627 0.2703 0.0203 0.0549 -0.0821 294 VAL A N 1948 C CA . VAL A 301 ? 0.3788 0.3587 0.2747 0.0207 0.0620 -0.0790 294 VAL A CA 1949 C C . VAL A 301 ? 0.3733 0.3531 0.2821 0.0221 0.0607 -0.0829 294 VAL A C 1950 O O . VAL A 301 ? 0.3681 0.3452 0.2799 0.0208 0.0528 -0.0847 294 VAL A O 1951 C CB . VAL A 301 ? 0.3589 0.3475 0.2677 0.0175 0.0591 -0.0721 294 VAL A CB 1952 C CG1 . VAL A 301 ? 0.3411 0.3381 0.2676 0.0181 0.0655 -0.0694 294 VAL A CG1 1953 C CG2 . VAL A 301 ? 0.3637 0.3518 0.2607 0.0157 0.0583 -0.0678 294 VAL A CG2 1954 N N . HIS A 302 ? 0.3655 0.3482 0.2830 0.0247 0.0685 -0.0839 295 HIS A N 1955 C CA . HIS A 302 ? 0.3596 0.3418 0.2895 0.0266 0.0676 -0.0873 295 HIS A CA 1956 C C . HIS A 302 ? 0.3528 0.3428 0.2984 0.0287 0.0749 -0.0854 295 HIS A C 1957 O O . HIS A 302 ? 0.3437 0.3362 0.2863 0.0299 0.0835 -0.0846 295 HIS A O 1958 C CB . HIS A 302 ? 0.3760 0.3478 0.2931 0.0295 0.0682 -0.0950 295 HIS A CB 1959 C CG . HIS A 302 ? 0.3679 0.3368 0.2959 0.0311 0.0656 -0.0990 295 HIS A CG 1960 N ND1 . HIS A 302 ? 0.3624 0.3301 0.2980 0.0287 0.0570 -0.0982 295 HIS A ND1 1961 C CD2 . HIS A 302 ? 0.3725 0.3390 0.3053 0.0351 0.0709 -0.1034 295 HIS A CD2 1962 C CE1 . HIS A 302 ? 0.3707 0.3350 0.3149 0.0309 0.0570 -0.1016 295 HIS A CE1 1963 N NE2 . HIS A 302 ? 0.3627 0.3261 0.3054 0.0349 0.0650 -0.1050 295 HIS A NE2 1964 N N . PRO A 303 ? 0.3328 0.3267 0.2953 0.0290 0.0717 -0.0842 296 PRO A N 1965 C CA . PRO A 303 ? 0.3214 0.3228 0.2996 0.0314 0.0775 -0.0829 296 PRO A CA 1966 C C . PRO A 303 ? 0.3382 0.3360 0.3214 0.0357 0.0809 -0.0883 296 PRO A C 1967 O O . PRO A 303 ? 0.3535 0.3436 0.3324 0.0364 0.0765 -0.0921 296 PRO A O 1968 C CB . PRO A 303 ? 0.3126 0.3199 0.3048 0.0296 0.0708 -0.0780 296 PRO A CB 1969 C CG . PRO A 303 ? 0.3177 0.3177 0.3042 0.0280 0.0625 -0.0792 296 PRO A CG 1970 C CD . PRO A 303 ? 0.2997 0.2917 0.2678 0.0273 0.0628 -0.0834 296 PRO A CD 1971 N N . ILE A 304 ? 0.3351 0.3387 0.3287 0.0387 0.0889 -0.0887 297 ILE A N 1972 C CA . ILE A 304 ? 0.3362 0.3375 0.3362 0.0434 0.0933 -0.0937 297 ILE A CA 1973 C C . ILE A 304 ? 0.3300 0.3414 0.3519 0.0457 0.0963 -0.0915 297 ILE A C 1974 O O . ILE A 304 ? 0.3147 0.3349 0.3449 0.0435 0.0967 -0.0866 297 ILE A O 1975 C CB . ILE A 304 ? 0.3539 0.3496 0.3398 0.0462 0.1026 -0.0989 297 ILE A CB 1976 C CG1 . ILE A 304 ? 0.3477 0.3505 0.3342 0.0458 0.1122 -0.0959 297 ILE A CG1 1977 C CG2 . ILE A 304 ? 0.3572 0.3413 0.3207 0.0450 0.0984 -0.1026 297 ILE A CG2 1978 C CD1 . ILE A 304 ? 0.3651 0.3621 0.3373 0.0492 0.1229 -0.1006 297 ILE A CD1 1979 N N . GLY A 305 ? 0.3419 0.3519 0.3732 0.0503 0.0981 -0.0954 298 GLY A N 1980 C CA . GLY A 305 ? 0.3363 0.3557 0.3892 0.0535 0.1012 -0.0944 298 GLY A CA 1981 C C . GLY A 305 ? 0.3525 0.3763 0.4091 0.0561 0.1132 -0.0968 298 GLY A C 1982 O O . GLY A 305 ? 0.3589 0.3778 0.3995 0.0557 0.1197 -0.0991 298 GLY A O 1983 N N . TYR A 306 ? 0.3484 0.3817 0.4264 0.0588 0.1161 -0.0962 299 TYR A N 1984 C CA . TYR A 306 ? 0.3572 0.3968 0.4421 0.0607 0.1283 -0.0976 299 TYR A CA 1985 C C . TYR A 306 ? 0.3815 0.4154 0.4630 0.0662 0.1366 -0.1042 299 TYR A C 1986 O O . TYR A 306 ? 0.3865 0.4226 0.4666 0.0676 0.1486 -0.1058 299 TYR A O 1987 C CB . TYR A 306 ? 0.3455 0.3988 0.4558 0.0608 0.1289 -0.0943 299 TYR A CB 1988 C CG . TYR A 306 ? 0.3080 0.3655 0.4385 0.0647 0.1221 -0.0949 299 TYR A CG 1989 C CD1 . TYR A 306 ? 0.3505 0.4103 0.4868 0.0628 0.1104 -0.0908 299 TYR A CD1 1990 C CD2 . TYR A 306 ? 0.3616 0.4213 0.5059 0.0706 0.1275 -0.0993 299 TYR A CD2 1991 C CE1 . TYR A 306 ? 0.3301 0.3930 0.4833 0.0668 0.1038 -0.0910 299 TYR A CE1 1992 C CE2 . TYR A 306 ? 0.3624 0.4258 0.5254 0.0746 0.1206 -0.0996 299 TYR A CE2 1993 C CZ . TYR A 306 ? 0.3293 0.3940 0.4957 0.0727 0.1086 -0.0953 299 TYR A CZ 1994 O OH . TYR A 306 ? 0.3161 0.3835 0.4989 0.0771 0.1012 -0.0952 299 TYR A OH 1995 N N . TYR A 307 ? 0.3839 0.4099 0.4634 0.0694 0.1313 -0.1081 300 TYR A N 1996 C CA . TYR A 307 ? 0.4037 0.4221 0.4761 0.0745 0.1390 -0.1151 300 TYR A CA 1997 C C . TYR A 307 ? 0.4148 0.4235 0.4603 0.0728 0.1434 -0.1175 300 TYR A C 1998 O O . TYR A 307 ? 0.4230 0.4295 0.4614 0.0760 0.1545 -0.1214 300 TYR A O 1999 C CB . TYR A 307 ? 0.4080 0.4178 0.4820 0.0780 0.1319 -0.1190 300 TYR A CB 2000 C CG . TYR A 307 ? 0.4345 0.4509 0.5329 0.0821 0.1291 -0.1185 300 TYR A CG 2001 C CD1 . TYR A 307 ? 0.4247 0.4537 0.5439 0.0846 0.1357 -0.1174 300 TYR A CD1 2002 C CD2 . TYR A 307 ? 0.4427 0.4520 0.5437 0.0839 0.1199 -0.1192 300 TYR A CD2 2003 C CE1 . TYR A 307 ? 0.4378 0.4726 0.5795 0.0889 0.1322 -0.1174 300 TYR A CE1 2004 C CE2 . TYR A 307 ? 0.4476 0.4615 0.5695 0.0885 0.1169 -0.1187 300 TYR A CE2 2005 C CZ . TYR A 307 ? 0.4532 0.4800 0.5952 0.0912 0.1227 -0.1180 300 TYR A CZ 2006 O OH . TYR A 307 ? 0.4807 0.5125 0.6439 0.0961 0.1186 -0.1177 300 TYR A OH 2007 N N . ASP A 308 ? 0.4023 0.4051 0.4328 0.0681 0.1345 -0.1154 301 ASP A N 2008 C CA . ASP A 308 ? 0.4218 0.4152 0.4263 0.0662 0.1359 -0.1173 301 ASP A CA 2009 C C . ASP A 308 ? 0.4264 0.4253 0.4249 0.0638 0.1440 -0.1132 301 ASP A C 2010 O O . ASP A 308 ? 0.4447 0.4372 0.4245 0.0651 0.1516 -0.1159 301 ASP A O 2011 C CB . ASP A 308 ? 0.4020 0.3891 0.3961 0.0618 0.1232 -0.1157 301 ASP A CB 2012 C CG . ASP A 308 ? 0.4162 0.3932 0.4085 0.0640 0.1167 -0.1211 301 ASP A CG 2013 O OD1 . ASP A 308 ? 0.4729 0.4453 0.4655 0.0691 0.1223 -0.1271 301 ASP A OD1 2014 O OD2 . ASP A 308 ? 0.4559 0.4289 0.4460 0.0607 0.1063 -0.1196 301 ASP A OD2 2015 N N . ALA A 309 ? 0.4162 0.4262 0.4298 0.0603 0.1422 -0.1067 302 ALA A N 2016 C CA . ALA A 309 ? 0.4133 0.4288 0.4243 0.0576 0.1498 -0.1022 302 ALA A CA 2017 C C . ALA A 309 ? 0.4324 0.4508 0.4476 0.0617 0.1647 -0.1045 302 ALA A C 2018 O O . ALA A 309 ? 0.4565 0.4716 0.4563 0.0613 0.1734 -0.1037 302 ALA A O 2019 C CB . ALA A 309 ? 0.3958 0.4227 0.4256 0.0538 0.1450 -0.0957 302 ALA A CB 2020 N N . GLN A 310 ? 0.4244 0.4490 0.4610 0.0657 0.1678 -0.1070 303 GLN A N 2021 C CA . GLN A 310 ? 0.4524 0.4805 0.4963 0.0702 0.1825 -0.1098 303 GLN A CA 2022 C C . GLN A 310 ? 0.4778 0.4932 0.4954 0.0737 0.1906 -0.1153 303 GLN A C 2023 O O . GLN A 310 ? 0.4909 0.5065 0.5020 0.0752 0.2042 -0.1150 303 GLN A O 2024 C CB . GLN A 310 ? 0.4379 0.4730 0.5078 0.0747 0.1821 -0.1127 303 GLN A CB 2025 C CG . GLN A 310 ? 0.4981 0.5360 0.5750 0.0801 0.1979 -0.1165 303 GLN A CG 2026 C CD . GLN A 310 ? 0.5595 0.6111 0.6703 0.0830 0.2010 -0.1165 303 GLN A CD 2027 O OE1 . GLN A 310 ? 0.6118 0.6668 0.7316 0.0876 0.2137 -0.1197 303 GLN A OE1 2028 N NE2 . GLN A 310 ? 0.5256 0.5847 0.6550 0.0809 0.1895 -0.1132 303 GLN A NE2 2029 N N . LYS A 311 ? 0.4932 0.4970 0.4951 0.0750 0.1823 -0.1201 304 LYS A N 2030 C CA . LYS A 311 ? 0.5249 0.5152 0.5002 0.0784 0.1872 -0.1261 304 LYS A CA 2031 C C . LYS A 311 ? 0.5415 0.5263 0.4918 0.0752 0.1897 -0.1229 304 LYS A C 2032 O O . LYS A 311 ? 0.5666 0.5434 0.4967 0.0785 0.1994 -0.1262 304 LYS A O 2033 C CB . LYS A 311 ? 0.5349 0.5140 0.5010 0.0797 0.1758 -0.1319 304 LYS A CB 2034 C CG . LYS A 311 ? 0.5450 0.5259 0.5307 0.0842 0.1749 -0.1361 304 LYS A CG 2035 C CD . LYS A 311 ? 0.6252 0.6029 0.6080 0.0911 0.1887 -0.1424 304 LYS A CD 2036 C CE . LYS A 311 ? 0.6637 0.6524 0.6769 0.0947 0.1927 -0.1424 304 LYS A CE 2037 N NZ . LYS A 311 ? 0.7264 0.7075 0.7439 0.0996 0.1879 -0.1491 304 LYS A NZ 2038 N N . LEU A 312 ? 0.5151 0.5035 0.4659 0.0692 0.1810 -0.1167 305 LEU A N 2039 C CA . LEU A 312 ? 0.5336 0.5170 0.4619 0.0661 0.1823 -0.1130 305 LEU A CA 2040 C C . LEU A 312 ? 0.5294 0.5207 0.4636 0.0650 0.1953 -0.1072 305 LEU A C 2041 O O . LEU A 312 ? 0.5629 0.5474 0.4748 0.0653 0.2024 -0.1058 305 LEU A O 2042 C CB . LEU A 312 ? 0.4939 0.4771 0.4190 0.0604 0.1677 -0.1088 305 LEU A CB 2043 C CG . LEU A 312 ? 0.5091 0.4838 0.4262 0.0600 0.1541 -0.1133 305 LEU A CG 2044 C CD1 . LEU A 312 ? 0.4994 0.4755 0.4147 0.0541 0.1415 -0.1082 305 LEU A CD1 2045 C CD2 . LEU A 312 ? 0.4836 0.4439 0.3745 0.0638 0.1551 -0.1207 305 LEU A CD2 2046 N N . LEU A 313 ? 0.5010 0.5060 0.4646 0.0639 0.1981 -0.1038 306 LEU A N 2047 C CA . LEU A 313 ? 0.4968 0.5106 0.4712 0.0621 0.2098 -0.0980 306 LEU A CA 2048 C C . LEU A 313 ? 0.5152 0.5302 0.4931 0.0672 0.2270 -0.1008 306 LEU A C 2049 O O . LEU A 313 ? 0.5160 0.5337 0.4930 0.0663 0.2396 -0.0966 306 LEU A O 2050 C CB . LEU A 313 ? 0.4620 0.4903 0.4681 0.0587 0.2046 -0.0938 306 LEU A CB 2051 C CG . LEU A 313 ? 0.4435 0.4724 0.4486 0.0533 0.1894 -0.0896 306 LEU A CG 2052 C CD1 . LEU A 313 ? 0.4358 0.4776 0.4722 0.0518 0.1829 -0.0875 306 LEU A CD1 2053 C CD2 . LEU A 313 ? 0.4485 0.4749 0.4385 0.0486 0.1909 -0.0834 306 LEU A CD2 2054 N N . GLU A 314 ? 0.5303 0.5435 0.5137 0.0726 0.2282 -0.1077 307 GLU A N 2055 C CA . GLU A 314 ? 0.5492 0.5668 0.5439 0.0777 0.2446 -0.1104 307 GLU A CA 2056 C C . GLU A 314 ? 0.5805 0.5882 0.5480 0.0804 0.2592 -0.1109 307 GLU A C 2057 O O . GLU A 314 ? 0.5908 0.6037 0.5673 0.0828 0.2757 -0.1098 307 GLU A O 2058 C CB . GLU A 314 ? 0.5496 0.5667 0.5560 0.0833 0.2420 -0.1178 307 GLU A CB 2059 C CG . GLU A 314 ? 0.5947 0.5959 0.5740 0.0866 0.2361 -0.1248 307 GLU A CG 2060 C CD . GLU A 314 ? 0.6397 0.6400 0.6318 0.0922 0.2338 -0.1319 307 GLU A CD 2061 O OE1 . GLU A 314 ? 0.6413 0.6537 0.6641 0.0932 0.2344 -0.1311 307 GLU A OE1 2062 O OE2 . GLU A 314 ? 0.6732 0.6600 0.6444 0.0955 0.2308 -0.1386 307 GLU A OE2 2063 N N . LYS A 315 ? 0.5972 0.5905 0.5317 0.0804 0.2534 -0.1127 308 LYS A N 2064 C CA . LYS A 315 ? 0.6289 0.6105 0.5331 0.0838 0.2657 -0.1138 308 LYS A CA 2065 C C . LYS A 315 ? 0.6325 0.6133 0.5240 0.0791 0.2695 -0.1054 308 LYS A C 2066 O O . LYS A 315 ? 0.6473 0.6175 0.5113 0.0816 0.2795 -0.1049 308 LYS A O 2067 C CB . LYS A 315 ? 0.6560 0.6208 0.5294 0.0873 0.2573 -0.1214 308 LYS A CB 2068 C CG . LYS A 315 ? 0.6854 0.6465 0.5630 0.0939 0.2591 -0.1309 308 LYS A CG 2069 C CD . LYS A 315 ? 0.7295 0.6757 0.5830 0.0954 0.2454 -0.1380 308 LYS A CD 2070 C CE . LYS A 315 ? 0.7636 0.7022 0.6135 0.1028 0.2496 -0.1480 308 LYS A CE 2071 N NZ . LYS A 315 ? 0.7735 0.6967 0.5990 0.1039 0.2364 -0.1550 308 LYS A NZ 2072 N N . MET A 316 ? 0.6038 0.5946 0.5139 0.0726 0.2614 -0.0987 309 MET A N 2073 C CA . MET A 316 ? 0.6120 0.6019 0.5114 0.0678 0.2636 -0.0904 309 MET A CA 2074 C C . MET A 316 ? 0.6242 0.6164 0.5247 0.0685 0.2838 -0.0855 309 MET A C 2075 O O . MET A 316 ? 0.6208 0.6250 0.5496 0.0690 0.2938 -0.0847 309 MET A O 2076 C CB . MET A 316 ? 0.5805 0.5806 0.5009 0.0610 0.2507 -0.0850 309 MET A CB 2077 C CG A MET A 316 ? 0.5648 0.5569 0.4691 0.0597 0.2324 -0.0879 309 MET A CG 2078 C CG B MET A 316 ? 0.5959 0.5920 0.5102 0.0593 0.2315 -0.0878 309 MET A CG 2079 S SD A MET A 316 ? 0.4995 0.4976 0.4138 0.0523 0.2160 -0.0817 309 MET A SD 2080 S SD B MET A 316 ? 0.6539 0.6354 0.5301 0.0575 0.2253 -0.0853 309 MET A SD 2081 C CE A MET A 316 ? 0.5411 0.5346 0.4369 0.0491 0.2235 -0.0733 309 MET A CE 2082 C CE B MET A 316 ? 0.6363 0.6257 0.5228 0.0511 0.2286 -0.0744 309 MET A CE 2083 N N . GLY A 317 ? 0.6483 0.6289 0.5181 0.0686 0.2890 -0.0818 310 GLY A N 2084 C CA . GLY A 317 ? 0.6776 0.6574 0.5425 0.0692 0.3086 -0.0762 310 GLY A CA 2085 C C . GLY A 317 ? 0.6779 0.6593 0.5425 0.0628 0.3078 -0.0664 310 GLY A C 2086 O O . GLY A 317 ? 0.6595 0.6511 0.5468 0.0571 0.2965 -0.0632 310 GLY A O 2087 N N . GLY A 318 ? 0.7105 0.6811 0.5482 0.0642 0.3197 -0.0617 311 GLY A N 2088 C CA . GLY A 318 ? 0.7056 0.6759 0.5409 0.0587 0.3217 -0.0518 311 GLY A CA 2089 C C . GLY A 318 ? 0.6927 0.6797 0.5682 0.0538 0.3301 -0.0463 311 GLY A C 2090 O O . GLY A 318 ? 0.6809 0.6763 0.5775 0.0561 0.3434 -0.0483 311 GLY A O 2091 N N . SER A 319 ? 0.6698 0.6617 0.5566 0.0472 0.3218 -0.0398 312 SER A N 2092 C CA . SER A 319 ? 0.6662 0.6726 0.5895 0.0417 0.3284 -0.0340 312 SER A CA 2093 C C . SER A 319 ? 0.6361 0.6592 0.5985 0.0403 0.3205 -0.0387 312 SER A C 2094 O O . SER A 319 ? 0.6243 0.6482 0.5871 0.0408 0.3035 -0.0439 312 SER A O 2095 C CB . SER A 319 ? 0.6635 0.6681 0.5837 0.0354 0.3199 -0.0263 312 SER A CB 2096 O OG . SER A 319 ? 0.7084 0.6974 0.5932 0.0367 0.3276 -0.0210 312 SER A OG 2097 N N . ALA A 320 ? 0.6223 0.6584 0.6180 0.0386 0.3324 -0.0365 313 ALA A N 2098 C CA . ALA A 320 ? 0.5943 0.6472 0.6305 0.0368 0.3248 -0.0398 313 ALA A CA 2099 C C . ALA A 320 ? 0.5713 0.6285 0.6175 0.0308 0.3064 -0.0371 313 ALA A C 2100 O O . ALA A 320 ? 0.5771 0.6271 0.6069 0.0271 0.3044 -0.0311 313 ALA A O 2101 C CB . ALA A 320 ? 0.5948 0.6603 0.6641 0.0353 0.3414 -0.0368 313 ALA A CB 2102 N N . PRO A 321 ? 0.5464 0.6150 0.6192 0.0302 0.2933 -0.0414 314 PRO A N 2103 C CA . PRO A 321 ? 0.5250 0.5987 0.6102 0.0245 0.2771 -0.0386 314 PRO A CA 2104 C C . PRO A 321 ? 0.5311 0.6114 0.6364 0.0188 0.2856 -0.0314 314 PRO A C 2105 O O . PRO A 321 ? 0.5111 0.5990 0.6371 0.0192 0.3005 -0.0306 314 PRO A O 2106 C CB . PRO A 321 ? 0.4996 0.5851 0.6128 0.0260 0.2661 -0.0444 314 PRO A CB 2107 C CG . PRO A 321 ? 0.5082 0.5986 0.6339 0.0314 0.2793 -0.0490 314 PRO A CG 2108 C CD . PRO A 321 ? 0.5402 0.6178 0.6346 0.0348 0.2941 -0.0484 314 PRO A CD 2109 N N . PRO A 322 ? 0.5245 0.6020 0.6249 0.0136 0.2765 -0.0263 315 PRO A N 2110 C CA . PRO A 322 ? 0.5341 0.6159 0.6513 0.0080 0.2856 -0.0193 315 PRO A CA 2111 C C . PRO A 322 ? 0.5239 0.6228 0.6859 0.0053 0.2852 -0.0204 315 PRO A C 2112 O O . PRO A 322 ? 0.5252 0.6296 0.7067 0.0018 0.2976 -0.0160 315 PRO A O 2113 C CB . PRO A 322 ? 0.5270 0.6012 0.6275 0.0038 0.2732 -0.0148 315 PRO A CB 2114 C CG . PRO A 322 ? 0.5035 0.5767 0.5953 0.0061 0.2543 -0.0206 315 PRO A CG 2115 C CD . PRO A 322 ? 0.5141 0.5836 0.5925 0.0126 0.2593 -0.0265 315 PRO A CD 2116 N N . ASP A 323 ? 0.5096 0.6167 0.6877 0.0068 0.2709 -0.0263 316 ASP A N 2117 C CA . ASP A 323 ? 0.5100 0.6332 0.7299 0.0052 0.2679 -0.0285 316 ASP A CA 2118 C C . ASP A 323 ? 0.4982 0.6265 0.7258 0.0095 0.2534 -0.0358 316 ASP A C 2119 O O . ASP A 323 ? 0.5037 0.6228 0.7049 0.0128 0.2453 -0.0386 316 ASP A O 2120 C CB . ASP A 323 ? 0.4995 0.6274 0.7375 -0.0017 0.2614 -0.0239 316 ASP A CB 2121 C CG . ASP A 323 ? 0.5132 0.6358 0.7364 -0.0033 0.2418 -0.0241 316 ASP A CG 2122 O OD1 . ASP A 323 ? 0.5541 0.6795 0.7794 -0.0003 0.2281 -0.0293 316 ASP A OD1 2123 O OD2 . ASP A 323 ? 0.5322 0.6478 0.7425 -0.0074 0.2401 -0.0187 316 ASP A OD2 2124 N N . SER A 324 ? 0.4858 0.6283 0.7497 0.0093 0.2495 -0.0386 317 SER A N 2125 C CA . SER A 324 ? 0.4772 0.6253 0.7522 0.0138 0.2374 -0.0452 317 SER A CA 2126 C C . SER A 324 ? 0.4555 0.5980 0.7150 0.0135 0.2173 -0.0462 317 SER A C 2127 O O . SER A 324 ? 0.4600 0.6016 0.7153 0.0181 0.2085 -0.0510 317 SER A O 2128 C CB . SER A 324 ? 0.4722 0.6368 0.7908 0.0136 0.2373 -0.0475 317 SER A CB 2129 O OG . SER A 324 ? 0.4880 0.6576 0.8220 0.0085 0.2251 -0.0455 317 SER A OG 2130 N N . SER A 325 ? 0.4380 0.5764 0.6890 0.0084 0.2107 -0.0418 318 SER A N 2131 C CA . SER A 325 ? 0.4095 0.5421 0.6442 0.0081 0.1932 -0.0423 318 SER A CA 2132 C C . SER A 325 ? 0.4119 0.5313 0.6105 0.0112 0.1917 -0.0433 318 SER A C 2133 O O . SER A 325 ? 0.4045 0.5190 0.5896 0.0117 0.1780 -0.0444 318 SER A O 2134 C CB . SER A 325 ? 0.4109 0.5423 0.6459 0.0021 0.1874 -0.0374 318 SER A CB 2135 O OG . SER A 325 ? 0.4170 0.5379 0.6271 -0.0003 0.1959 -0.0324 318 SER A OG 2136 N N . TRP A 326 ? 0.4056 0.5192 0.5892 0.0132 0.2058 -0.0431 319 TRP A N 2137 C CA . TRP A 326 ? 0.4146 0.5159 0.5655 0.0167 0.2057 -0.0451 319 TRP A CA 2138 C C . TRP A 326 ? 0.4124 0.5149 0.5664 0.0228 0.2063 -0.0516 319 TRP A C 2139 O O . TRP A 326 ? 0.4141 0.5070 0.5445 0.0258 0.2021 -0.0545 319 TRP A O 2140 C CB . TRP A 326 ? 0.4350 0.5266 0.5622 0.0160 0.2197 -0.0412 319 TRP A CB 2141 C CG . TRP A 326 ? 0.4072 0.4916 0.5174 0.0113 0.2145 -0.0355 319 TRP A CG 2142 C CD1 . TRP A 326 ? 0.3861 0.4758 0.5120 0.0061 0.2103 -0.0311 319 TRP A CD1 2143 C CD2 . TRP A 326 ? 0.4208 0.4914 0.4956 0.0118 0.2126 -0.0339 319 TRP A CD2 2144 N NE1 . TRP A 326 ? 0.4158 0.4955 0.5180 0.0034 0.2062 -0.0267 319 TRP A NE1 2145 C CE2 . TRP A 326 ? 0.4267 0.4950 0.4978 0.0069 0.2072 -0.0283 319 TRP A CE2 2146 C CE3 . TRP A 326 ? 0.4371 0.4968 0.4834 0.0161 0.2143 -0.0371 319 TRP A CE3 2147 C CZ2 . TRP A 326 ? 0.3939 0.4499 0.4344 0.0063 0.2034 -0.0254 319 TRP A CZ2 2148 C CZ3 . TRP A 326 ? 0.4464 0.4938 0.4620 0.0154 0.2100 -0.0345 319 TRP A CZ3 2149 C CH2 . TRP A 326 ? 0.4162 0.4623 0.4297 0.0106 0.2044 -0.0286 319 TRP A CH2 2150 N N . ARG A 327 ? 0.4058 0.5199 0.5896 0.0247 0.2107 -0.0542 320 ARG A N 2151 C CA . ARG A 327 ? 0.4120 0.5277 0.6015 0.0309 0.2117 -0.0603 320 ARG A CA 2152 C C . ARG A 327 ? 0.3933 0.5132 0.5951 0.0327 0.1950 -0.0636 320 ARG A C 2153 O O . ARG A 327 ? 0.3677 0.4975 0.5943 0.0307 0.1881 -0.0626 320 ARG A O 2154 C CB . ARG A 327 ? 0.4124 0.5383 0.6277 0.0329 0.2264 -0.0616 320 ARG A CB 2155 C CG . ARG A 327 ? 0.4752 0.5947 0.6743 0.0342 0.2452 -0.0604 320 ARG A CG 2156 C CD . ARG A 327 ? 0.5569 0.6873 0.7841 0.0371 0.2601 -0.0623 320 ARG A CD 2157 N NE . ARG A 327 ? 0.6409 0.7834 0.8984 0.0319 0.2622 -0.0582 320 ARG A NE 2158 C CZ . ARG A 327 ? 0.6854 0.8323 0.9548 0.0297 0.2790 -0.0546 320 ARG A CZ 2159 N NH1 . ARG A 327 ? 0.7256 0.8661 0.9789 0.0329 0.2963 -0.0545 320 ARG A NH1 2160 N NH2 . ARG A 327 ? 0.6884 0.8462 0.9868 0.0245 0.2786 -0.0511 320 ARG A NH2 2161 N N . GLY A 328 ? 0.3974 0.5089 0.5812 0.0365 0.1886 -0.0673 321 GLY A N 2162 C CA . GLY A 328 ? 0.3817 0.4957 0.5757 0.0396 0.1751 -0.0708 321 GLY A CA 2163 C C . GLY A 328 ? 0.3933 0.5147 0.6096 0.0451 0.1808 -0.0754 321 GLY A C 2164 O O . GLY A 328 ? 0.3775 0.5059 0.6091 0.0454 0.1939 -0.0753 321 GLY A O 2165 N N . SER A 329 ? 0.3839 0.5037 0.6025 0.0495 0.1715 -0.0792 322 SER A N 2166 C CA . SER A 329 ? 0.3972 0.5243 0.6390 0.0552 0.1741 -0.0836 322 SER A CA 2167 C C . SER A 329 ? 0.4017 0.5208 0.6304 0.0607 0.1815 -0.0886 322 SER A C 2168 O O . SER A 329 ? 0.4137 0.5379 0.6604 0.0660 0.1842 -0.0925 322 SER A O 2169 C CB . SER A 329 ? 0.3784 0.5090 0.6339 0.0572 0.1581 -0.0845 322 SER A CB 2170 O OG . SER A 329 ? 0.4124 0.5520 0.6852 0.0532 0.1518 -0.0812 322 SER A OG 2171 N N . LEU A 330 ? 0.4074 0.5137 0.6052 0.0600 0.1840 -0.0889 323 LEU A N 2172 C CA . LEU A 330 ? 0.4261 0.5239 0.6106 0.0655 0.1909 -0.0943 323 LEU A CA 2173 C C . LEU A 330 ? 0.4496 0.5514 0.6408 0.0678 0.2092 -0.0958 323 LEU A C 2174 O O . LEU A 330 ? 0.4552 0.5631 0.6530 0.0640 0.2174 -0.0916 323 LEU A O 2175 C CB . LEU A 330 ? 0.4286 0.5113 0.5781 0.0640 0.1878 -0.0947 323 LEU A CB 2176 C CG . LEU A 330 ? 0.4031 0.4796 0.5420 0.0620 0.1713 -0.0937 323 LEU A CG 2177 C CD1 . LEU A 330 ? 0.3923 0.4560 0.4988 0.0593 0.1706 -0.0933 323 LEU A CD1 2178 C CD2 . LEU A 330 ? 0.3764 0.4504 0.5228 0.0673 0.1646 -0.0984 323 LEU A CD2 2179 N N . LYS A 331 ? 0.4703 0.5678 0.6585 0.0740 0.2162 -0.1015 324 LYS A N 2180 C CA . LYS A 331 ? 0.5027 0.6033 0.6961 0.0770 0.2348 -0.1032 324 LYS A CA 2181 C C . LYS A 331 ? 0.5143 0.6025 0.6741 0.0761 0.2446 -0.1028 324 LYS A C 2182 O O . LYS A 331 ? 0.5291 0.6079 0.6721 0.0812 0.2517 -0.1079 324 LYS A O 2183 C CB . LYS A 331 ? 0.5184 0.6206 0.7256 0.0848 0.2389 -0.1099 324 LYS A CB 2184 C CG . LYS A 331 ? 0.5596 0.6742 0.8011 0.0869 0.2294 -0.1106 324 LYS A CG 2185 C CD . LYS A 331 ? 0.6152 0.7430 0.8795 0.0811 0.2249 -0.1048 324 LYS A CD 2186 C CE . LYS A 331 ? 0.6464 0.7902 0.9509 0.0844 0.2267 -0.1064 324 LYS A CE 2187 N NZ . LYS A 331 ? 0.6574 0.8138 0.9835 0.0786 0.2273 -0.1013 324 LYS A NZ 2188 N N . VAL A 332 ? 0.5044 0.5916 0.6534 0.0699 0.2440 -0.0967 325 VAL A N 2189 C CA . VAL A 332 ? 0.5165 0.5921 0.6334 0.0686 0.2523 -0.0950 325 VAL A CA 2190 C C . VAL A 332 ? 0.5123 0.5949 0.6374 0.0633 0.2611 -0.0879 325 VAL A C 2191 O O . VAL A 332 ? 0.4902 0.5848 0.6420 0.0597 0.2562 -0.0845 325 VAL A O 2192 C CB . VAL A 332 ? 0.5165 0.5788 0.6031 0.0665 0.2388 -0.0952 325 VAL A CB 2193 C CG1 . VAL A 332 ? 0.5300 0.5843 0.6086 0.0716 0.2313 -0.1024 325 VAL A CG1 2194 C CG2 . VAL A 332 ? 0.4742 0.5413 0.5678 0.0599 0.2243 -0.0896 325 VAL A CG2 2195 N N . PRO A 333 ? 0.5301 0.6045 0.6321 0.0631 0.2742 -0.0857 326 PRO A N 2196 C CA . PRO A 333 ? 0.5253 0.6061 0.6369 0.0581 0.2837 -0.0785 326 PRO A CA 2197 C C . PRO A 333 ? 0.5056 0.5847 0.6097 0.0513 0.2713 -0.0726 326 PRO A C 2198 O O . PRO A 333 ? 0.5023 0.5887 0.6215 0.0465 0.2752 -0.0668 326 PRO A O 2199 C CB . PRO A 333 ? 0.5646 0.6348 0.6496 0.0608 0.3013 -0.0778 326 PRO A CB 2200 C CG . PRO A 333 ? 0.5873 0.6420 0.6387 0.0654 0.2952 -0.0838 326 PRO A CG 2201 C CD . PRO A 333 ? 0.5642 0.6231 0.6312 0.0675 0.2807 -0.0895 326 PRO A CD 2202 N N . TYR A 334 ? 0.4863 0.5561 0.5689 0.0510 0.2566 -0.0743 327 TYR A N 2203 C CA . TYR A 334 ? 0.4723 0.5390 0.5440 0.0451 0.2456 -0.0690 327 TYR A CA 2204 C C . TYR A 334 ? 0.4870 0.5454 0.5357 0.0428 0.2559 -0.0636 327 TYR A C 2205 O O . TYR A 334 ? 0.4734 0.5346 0.5266 0.0375 0.2543 -0.0573 327 TYR A O 2206 C CB . TYR A 334 ? 0.4499 0.5300 0.5531 0.0406 0.2370 -0.0658 327 TYR A CB 2207 C CG . TYR A 334 ? 0.4319 0.5162 0.5487 0.0427 0.2226 -0.0703 327 TYR A CG 2208 C CD1 . TYR A 334 ? 0.4108 0.4885 0.5124 0.0413 0.2070 -0.0706 327 TYR A CD1 2209 C CD2 . TYR A 334 ? 0.4191 0.5132 0.5630 0.0466 0.2250 -0.0743 327 TYR A CD2 2210 C CE1 . TYR A 334 ? 0.3822 0.4625 0.4946 0.0433 0.1945 -0.0741 327 TYR A CE1 2211 C CE2 . TYR A 334 ? 0.3826 0.4791 0.5370 0.0489 0.2116 -0.0781 327 TYR A CE2 2212 C CZ . TYR A 334 ? 0.3929 0.4819 0.5304 0.0472 0.1968 -0.0777 327 TYR A CZ 2213 O OH . TYR A 334 ? 0.3608 0.4513 0.5076 0.0495 0.1842 -0.0806 327 TYR A OH 2214 N N . ASN A 335 ? 0.5141 0.5619 0.5381 0.0473 0.2668 -0.0661 328 ASN A N 2215 C CA . ASN A 335 ? 0.5329 0.5701 0.5292 0.0463 0.2757 -0.0613 328 ASN A CA 2216 C C . ASN A 335 ? 0.5298 0.5582 0.5034 0.0432 0.2603 -0.0593 328 ASN A C 2217 O O . ASN A 335 ? 0.5048 0.5300 0.4722 0.0442 0.2464 -0.0638 328 ASN A O 2218 C CB . ASN A 335 ? 0.5525 0.5787 0.5239 0.0526 0.2889 -0.0652 328 ASN A CB 2219 C CG . ASN A 335 ? 0.5665 0.6011 0.5593 0.0557 0.3070 -0.0662 328 ASN A CG 2220 O OD1 . ASN A 335 ? 0.5560 0.6033 0.5785 0.0522 0.3133 -0.0618 328 ASN A OD1 2221 N ND2 . ASN A 335 ? 0.5463 0.5738 0.5247 0.0625 0.3154 -0.0724 328 ASN A ND2 2222 N N . VAL A 336 ? 0.5489 0.5733 0.5110 0.0394 0.2635 -0.0523 329 VAL A N 2223 C CA . VAL A 336 ? 0.5541 0.5712 0.4975 0.0362 0.2495 -0.0496 329 VAL A CA 2224 C C . VAL A 336 ? 0.5795 0.5802 0.4836 0.0402 0.2479 -0.0525 329 VAL A C 2225 O O . VAL A 336 ? 0.5703 0.5646 0.4585 0.0389 0.2338 -0.0531 329 VAL A O 2226 C CB . VAL A 336 ? 0.5566 0.5759 0.5050 0.0308 0.2532 -0.0409 329 VAL A CB 2227 C CG1 . VAL A 336 ? 0.5786 0.5897 0.5062 0.0280 0.2393 -0.0380 329 VAL A CG1 2228 C CG2 . VAL A 336 ? 0.5508 0.5862 0.5387 0.0268 0.2513 -0.0392 329 VAL A CG2 2229 N N . GLY A 337 ? 0.5974 0.5912 0.4860 0.0452 0.2621 -0.0548 330 GLY A N 2230 C CA . GLY A 337 ? 0.6272 0.6044 0.4771 0.0496 0.2609 -0.0583 330 GLY A CA 2231 C C . GLY A 337 ? 0.6495 0.6171 0.4751 0.0484 0.2676 -0.0509 330 GLY A C 2232 O O . GLY A 337 ? 0.6511 0.6236 0.4885 0.0460 0.2802 -0.0443 330 GLY A O 2233 N N . PRO A 338 ? 0.6721 0.6256 0.4638 0.0503 0.2593 -0.0520 331 PRO A N 2234 C CA . PRO A 338 ? 0.6762 0.6218 0.4507 0.0533 0.2450 -0.0601 331 PRO A CA 2235 C C . PRO A 338 ? 0.6871 0.6270 0.4513 0.0600 0.2524 -0.0685 331 PRO A C 2236 O O . PRO A 338 ? 0.7067 0.6424 0.4613 0.0638 0.2696 -0.0676 331 PRO A O 2237 C CB . PRO A 338 ? 0.6990 0.6301 0.4381 0.0539 0.2395 -0.0571 331 PRO A CB 2238 C CG . PRO A 338 ? 0.7378 0.6640 0.4648 0.0551 0.2585 -0.0501 331 PRO A CG 2239 C CD . PRO A 338 ? 0.7048 0.6476 0.4708 0.0499 0.2655 -0.0447 331 PRO A CD 2240 N N . GLY A 339 ? 0.6744 0.6134 0.4404 0.0616 0.2399 -0.0765 332 GLY A N 2241 C CA . GLY A 339 ? 0.6974 0.6281 0.4492 0.0682 0.2440 -0.0855 332 GLY A CA 2242 C C . GLY A 339 ? 0.6953 0.6354 0.4716 0.0708 0.2572 -0.0882 332 GLY A C 2243 O O . GLY A 339 ? 0.6594 0.6135 0.4660 0.0673 0.2629 -0.0831 332 GLY A O 2244 N N . PHE A 340 ? 0.7201 0.6522 0.4834 0.0773 0.2614 -0.0966 333 PHE A N 2245 C CA . PHE A 340 ? 0.7286 0.6683 0.5142 0.0809 0.2720 -0.1010 333 PHE A CA 2246 C C . PHE A 340 ? 0.7610 0.6984 0.5384 0.0851 0.2943 -0.0990 333 PHE A C 2247 O O . PHE A 340 ? 0.7857 0.7113 0.5324 0.0867 0.3003 -0.0960 333 PHE A O 2248 C CB . PHE A 340 ? 0.7275 0.6596 0.5052 0.0857 0.2639 -0.1118 333 PHE A CB 2249 C CG . PHE A 340 ? 0.7149 0.6505 0.5056 0.0817 0.2438 -0.1139 333 PHE A CG 2250 C CD1 . PHE A 340 ? 0.7292 0.6526 0.4996 0.0837 0.2310 -0.1213 333 PHE A CD1 2251 C CD2 . PHE A 340 ? 0.6764 0.6270 0.4994 0.0761 0.2378 -0.1087 333 PHE A CD2 2252 C CE1 . PHE A 340 ? 0.7079 0.6344 0.4911 0.0799 0.2137 -0.1229 333 PHE A CE1 2253 C CE2 . PHE A 340 ? 0.6501 0.6033 0.4839 0.0727 0.2204 -0.1102 333 PHE A CE2 2254 C CZ . PHE A 340 ? 0.6683 0.6096 0.4826 0.0745 0.2087 -0.1170 333 PHE A CZ 2255 N N . THR A 341 ? 0.7699 0.7181 0.5745 0.0871 0.3065 -0.1002 334 THR A N 2256 C CA . THR A 341 ? 0.8108 0.7574 0.6099 0.0916 0.3294 -0.0986 334 THR A CA 2257 C C . THR A 341 ? 0.8534 0.7830 0.6171 0.0998 0.3356 -0.1065 334 THR A C 2258 O O . THR A 341 ? 0.8526 0.7750 0.6065 0.1028 0.3236 -0.1151 334 THR A O 2259 C CB . THR A 341 ? 0.8048 0.7679 0.6439 0.0924 0.3414 -0.0990 334 THR A CB 2260 O OG1 . THR A 341 ? 0.8080 0.7753 0.6641 0.0946 0.3308 -0.1071 334 THR A OG1 2261 C CG2 . THR A 341 ? 0.7876 0.7668 0.6593 0.0852 0.3428 -0.0900 334 THR A CG2 2262 N N . GLY A 342 ? 0.8888 0.8121 0.6350 0.1036 0.3552 -0.1034 335 GLY A N 2263 C CA . GLY A 342 ? 0.9378 0.8434 0.6458 0.1119 0.3644 -0.1095 335 GLY A CA 2264 C C . GLY A 342 ? 0.9559 0.8500 0.6459 0.1178 0.3540 -0.1216 335 GLY A C 2265 O O . GLY A 342 ? 0.9878 0.8653 0.6406 0.1203 0.3457 -0.1250 335 GLY A O 2266 N N . ASN A 343 ? 0.9448 0.8471 0.6607 0.1203 0.3545 -0.1283 336 ASN A N 2267 C CA . ASN A 343 ? 0.9601 0.8516 0.6620 0.1262 0.3461 -0.1403 336 ASN A CA 2268 C C . ASN A 343 ? 0.9420 0.8266 0.6325 0.1227 0.3219 -0.1437 336 ASN A C 2269 O O . ASN A 343 ? 0.9587 0.8281 0.6219 0.1273 0.3144 -0.1524 336 ASN A O 2270 C CB . ASN A 343 ? 0.9522 0.8559 0.6902 0.1284 0.3493 -0.1455 336 ASN A CB 2271 C CG . ASN A 343 ? 1.0050 0.9115 0.7490 0.1347 0.3731 -0.1464 336 ASN A CG 2272 O OD1 . ASN A 343 ? 1.0633 0.9648 0.7886 0.1365 0.3894 -0.1415 336 ASN A OD1 2273 N ND2 . ASN A 343 ? 1.0476 0.9617 0.8178 0.1384 0.3759 -0.1527 336 ASN A ND2 2274 N N . PHE A 344 ? 0.8981 0.7943 0.6108 0.1146 0.3099 -0.1370 337 PHE A N 2275 C CA . PHE A 344 ? 0.8750 0.7684 0.5853 0.1104 0.2873 -0.1392 337 PHE A CA 2276 C C . PHE A 344 ? 0.8689 0.7570 0.5581 0.1058 0.2794 -0.1324 337 PHE A C 2277 O O . PHE A 344 ? 0.8493 0.7380 0.5412 0.1010 0.2614 -0.1320 337 PHE A O 2278 C CB . PHE A 344 ? 0.8333 0.7436 0.5855 0.1052 0.2785 -0.1374 337 PHE A CB 2279 C CG . PHE A 344 ? 0.8417 0.7602 0.6201 0.1095 0.2880 -0.1420 337 PHE A CG 2280 C CD1 . PHE A 344 ? 0.8371 0.7715 0.6462 0.1080 0.3006 -0.1361 337 PHE A CD1 2281 C CD2 . PHE A 344 ? 0.8608 0.7711 0.6342 0.1150 0.2839 -0.1524 337 PHE A CD2 2282 C CE1 . PHE A 344 ? 0.8420 0.7845 0.6767 0.1124 0.3090 -0.1405 337 PHE A CE1 2283 C CE2 . PHE A 344 ? 0.8665 0.7841 0.6643 0.1194 0.2925 -0.1568 337 PHE A CE2 2284 C CZ . PHE A 344 ? 0.8493 0.7833 0.6780 0.1182 0.3049 -0.1507 337 PHE A CZ 2285 N N . SER A 345 ? 0.8818 0.7639 0.5494 0.1076 0.2931 -0.1270 338 SER A N 2286 C CA . SER A 345 ? 0.8846 0.7626 0.5348 0.1032 0.2877 -0.1189 338 SER A CA 2287 C C . SER A 345 ? 0.8876 0.7519 0.5095 0.1036 0.2687 -0.1239 338 SER A C 2288 O O . SER A 345 ? 0.8875 0.7516 0.5036 0.0987 0.2581 -0.1181 338 SER A O 2289 C CB . SER A 345 ? 0.9130 0.7842 0.5411 0.1063 0.3068 -0.1128 338 SER A CB 2290 O OG . SER A 345 ? 0.9590 0.8122 0.5492 0.1144 0.3119 -0.1199 338 SER A OG 2291 N N . THR A 346 ? 0.8926 0.7462 0.4994 0.1091 0.2641 -0.1348 339 THR A N 2292 C CA . THR A 346 ? 0.9074 0.7468 0.4866 0.1103 0.2467 -0.1412 339 THR A CA 2293 C C . THR A 346 ? 0.8775 0.7233 0.4797 0.1057 0.2277 -0.1455 339 THR A C 2294 O O . THR A 346 ? 0.8924 0.7290 0.4786 0.1051 0.2113 -0.1503 339 THR A O 2295 C CB . THR A 346 ? 0.9405 0.7620 0.4863 0.1193 0.2513 -0.1516 339 THR A CB 2296 O OG1 . THR A 346 ? 0.9437 0.7688 0.5086 0.1224 0.2549 -0.1597 339 THR A OG1 2297 C CG2 . THR A 346 ? 0.9805 0.7937 0.4998 0.1246 0.2710 -0.1473 339 THR A CG2 2298 N N . GLN A 347 ? 0.8411 0.7024 0.4810 0.1026 0.2299 -0.1439 340 GLN A N 2299 C CA . GLN A 347 ? 0.7954 0.6640 0.4595 0.0977 0.2133 -0.1459 340 GLN A CA 2300 C C . GLN A 347 ? 0.7700 0.6470 0.4439 0.0901 0.2037 -0.1367 340 GLN A C 2301 O O . GLN A 347 ? 0.7510 0.6320 0.4230 0.0882 0.2123 -0.1281 340 GLN A O 2302 C CB . GLN A 347 ? 0.7698 0.6505 0.4684 0.0980 0.2188 -0.1476 340 GLN A CB 2303 C CG . GLN A 347 ? 0.8103 0.6820 0.5003 0.1058 0.2262 -0.1580 340 GLN A CG 2304 C CD . GLN A 347 ? 0.8031 0.6869 0.5268 0.1072 0.2340 -0.1592 340 GLN A CD 2305 O OE1 . GLN A 347 ? 0.7946 0.6936 0.5491 0.1024 0.2329 -0.1527 340 GLN A OE1 2306 N NE2 . GLN A 347 ? 0.8149 0.6913 0.5322 0.1143 0.2415 -0.1679 340 GLN A NE2 2307 N N . LYS A 348 ? 0.7487 0.6270 0.4317 0.0860 0.1861 -0.1387 341 LYS A N 2308 C CA . LYS A 348 ? 0.7325 0.6179 0.4247 0.0792 0.1752 -0.1312 341 LYS A CA 2309 C C . LYS A 348 ? 0.6985 0.5941 0.4213 0.0748 0.1639 -0.1319 341 LYS A C 2310 O O . LYS A 348 ? 0.6937 0.5881 0.4261 0.0771 0.1621 -0.1388 341 LYS A O 2311 C CB . LYS A 348 ? 0.7597 0.6325 0.4220 0.0792 0.1631 -0.1329 341 LYS A CB 2312 C CG . LYS A 348 ? 0.8219 0.6839 0.4511 0.0831 0.1727 -0.1302 341 LYS A CG 2313 C CD . LYS A 348 ? 0.9068 0.7588 0.5113 0.0822 0.1579 -0.1305 341 LYS A CD 2314 C CE . LYS A 348 ? 0.9449 0.7935 0.5299 0.0821 0.1643 -0.1217 341 LYS A CE 2315 N NZ . LYS A 348 ? 0.9747 0.8126 0.5333 0.0890 0.1808 -0.1227 341 LYS A NZ 2316 N N . VAL A 349 ? 0.6563 0.5612 0.3937 0.0686 0.1563 -0.1245 342 VAL A N 2317 C CA . VAL A 349 ? 0.6272 0.5404 0.3904 0.0644 0.1450 -0.1245 342 VAL A CA 2318 C C . VAL A 349 ? 0.6257 0.5326 0.3774 0.0615 0.1285 -0.1261 342 VAL A C 2319 O O . VAL A 349 ? 0.6321 0.5353 0.3668 0.0602 0.1255 -0.1224 342 VAL A O 2320 C CB . VAL A 349 ? 0.6054 0.5340 0.3953 0.0599 0.1483 -0.1157 342 VAL A CB 2321 C CG1 . VAL A 349 ? 0.5757 0.5114 0.3871 0.0553 0.1349 -0.1144 342 VAL A CG1 2322 C CG2 . VAL A 349 ? 0.6014 0.5371 0.4078 0.0630 0.1630 -0.1156 342 VAL A CG2 2323 N N . LYS A 350 ? 0.6139 0.5191 0.3752 0.0608 0.1181 -0.1317 343 LYS A N 2324 C CA . LYS A 350 ? 0.6126 0.5132 0.3682 0.0576 0.1024 -0.1335 343 LYS A CA 2325 C C . LYS A 350 ? 0.5853 0.4954 0.3687 0.0527 0.0938 -0.1309 343 LYS A C 2326 O O . LYS A 350 ? 0.5647 0.4771 0.3649 0.0537 0.0949 -0.1338 343 LYS A O 2327 C CB . LYS A 350 ? 0.6430 0.5292 0.3794 0.0614 0.0966 -0.1441 343 LYS A CB 2328 C CG . LYS A 350 ? 0.6565 0.5373 0.3870 0.0582 0.0799 -0.1468 343 LYS A CG 2329 C CD . LYS A 350 ? 0.7150 0.5806 0.4251 0.0625 0.0745 -0.1580 343 LYS A CD 2330 C CE . LYS A 350 ? 0.7212 0.5822 0.4268 0.0592 0.0575 -0.1609 343 LYS A CE 2331 N NZ . LYS A 350 ? 0.8089 0.6540 0.4864 0.0637 0.0522 -0.1707 343 LYS A NZ 2332 N N . MET A 351 ? 0.5622 0.4768 0.3491 0.0479 0.0852 -0.1254 344 MET A N 2333 C CA . MET A 351 ? 0.5426 0.4652 0.3530 0.0434 0.0768 -0.1225 344 MET A CA 2334 C C . MET A 351 ? 0.5557 0.4702 0.3610 0.0422 0.0638 -0.1285 344 MET A C 2335 O O . MET A 351 ? 0.5785 0.4840 0.3625 0.0435 0.0591 -0.1324 344 MET A O 2336 C CB . MET A 351 ? 0.5097 0.4416 0.3270 0.0391 0.0751 -0.1133 344 MET A CB 2337 C CG . MET A 351 ? 0.4954 0.4348 0.3174 0.0396 0.0872 -0.1071 344 MET A CG 2338 S SD . MET A 351 ? 0.4749 0.4248 0.3075 0.0343 0.0841 -0.0968 344 MET A SD 2339 C CE . MET A 351 ? 0.4380 0.3967 0.2988 0.0312 0.0767 -0.0955 344 MET A CE 2340 N N . HIS A 352 ? 0.5425 0.4601 0.3676 0.0397 0.0576 -0.1291 345 HIS A N 2341 C CA . HIS A 352 ? 0.5451 0.4567 0.3695 0.0374 0.0450 -0.1337 345 HIS A CA 2342 C C . HIS A 352 ? 0.5141 0.4349 0.3601 0.0323 0.0392 -0.1275 345 HIS A C 2343 O O . HIS A 352 ? 0.5016 0.4262 0.3660 0.0319 0.0408 -0.1264 345 HIS A O 2344 C CB . HIS A 352 ? 0.5593 0.4620 0.3850 0.0399 0.0436 -0.1425 345 HIS A CB 2345 C CG . HIS A 352 ? 0.5968 0.4920 0.4063 0.0458 0.0525 -0.1484 345 HIS A CG 2346 N ND1 . HIS A 352 ? 0.6334 0.5337 0.4494 0.0489 0.0649 -0.1460 345 HIS A ND1 2347 C CD2 . HIS A 352 ? 0.6639 0.5465 0.4514 0.0495 0.0509 -0.1569 345 HIS A CD2 2348 C CE1 . HIS A 352 ? 0.6457 0.5373 0.4445 0.0542 0.0715 -0.1525 345 HIS A CE1 2349 N NE2 . HIS A 352 ? 0.6768 0.5571 0.4570 0.0549 0.0632 -0.1592 345 HIS A NE2 2350 N N . ILE A 353 ? 0.5010 0.4250 0.3447 0.0289 0.0327 -0.1232 346 ILE A N 2351 C CA . ILE A 353 ? 0.4712 0.4042 0.3350 0.0245 0.0284 -0.1169 346 ILE A CA 2352 C C . ILE A 353 ? 0.4791 0.4088 0.3440 0.0213 0.0165 -0.1193 346 ILE A C 2353 O O . ILE A 353 ? 0.4958 0.4220 0.3463 0.0210 0.0110 -0.1207 346 ILE A O 2354 C CB . ILE A 353 ? 0.4642 0.4068 0.3304 0.0230 0.0324 -0.1082 346 ILE A CB 2355 C CG1 . ILE A 353 ? 0.4515 0.3972 0.3166 0.0261 0.0444 -0.1062 346 ILE A CG1 2356 C CG2 . ILE A 353 ? 0.4295 0.3806 0.3160 0.0191 0.0285 -0.1022 346 ILE A CG2 2357 C CD1 . ILE A 353 ? 0.4690 0.4184 0.3523 0.0277 0.0499 -0.1067 346 ILE A CD1 2358 N N . HIS A 354 ? 0.4662 0.3969 0.3488 0.0189 0.0124 -0.1196 347 HIS A N 2359 C CA . HIS A 354 ? 0.4773 0.4052 0.3650 0.0154 0.0016 -0.1221 347 HIS A CA 2360 C C . HIS A 354 ? 0.4493 0.3852 0.3574 0.0112 -0.0009 -0.1154 347 HIS A C 2361 O O . HIS A 354 ? 0.4281 0.3621 0.3460 0.0082 -0.0080 -0.1173 347 HIS A O 2362 C CB . HIS A 354 ? 0.4994 0.4171 0.3874 0.0165 -0.0014 -0.1309 347 HIS A CB 2363 C CG . HIS A 354 ? 0.5616 0.4704 0.4291 0.0212 0.0016 -0.1381 347 HIS A CG 2364 N ND1 . HIS A 354 ? 0.6257 0.5311 0.4925 0.0251 0.0098 -0.1410 347 HIS A ND1 2365 C CD2 . HIS A 354 ? 0.6225 0.5249 0.4685 0.0232 -0.0018 -0.1425 347 HIS A CD2 2366 C CE1 . HIS A 354 ? 0.6481 0.5453 0.4939 0.0292 0.0117 -0.1473 347 HIS A CE1 2367 N NE2 . HIS A 354 ? 0.6715 0.5664 0.5035 0.0282 0.0046 -0.1482 347 HIS A NE2 2368 N N . SER A 355 ? 0.4209 0.3656 0.3357 0.0111 0.0051 -0.1079 348 SER A N 2369 C CA . SER A 355 ? 0.3998 0.3520 0.3312 0.0078 0.0034 -0.1011 348 SER A CA 2370 C C . SER A 355 ? 0.4055 0.3597 0.3363 0.0046 -0.0045 -0.0999 348 SER A C 2371 O O . SER A 355 ? 0.4112 0.3634 0.3273 0.0054 -0.0073 -0.1019 348 SER A O 2372 C CB . SER A 355 ? 0.3803 0.3410 0.3150 0.0088 0.0103 -0.0940 348 SER A CB 2373 O OG . SER A 355 ? 0.3841 0.3438 0.3211 0.0120 0.0174 -0.0953 348 SER A OG 2374 N N . THR A 356 ? 0.3822 0.3401 0.3287 0.0013 -0.0080 -0.0964 349 THR A N 2375 C CA . THR A 356 ? 0.3932 0.3541 0.3426 -0.0017 -0.0152 -0.0949 349 THR A CA 2376 C C . THR A 356 ? 0.3779 0.3479 0.3386 -0.0033 -0.0129 -0.0865 349 THR A C 2377 O O . THR A 356 ? 0.3681 0.3403 0.3383 -0.0029 -0.0077 -0.0827 349 THR A O 2378 C CB . THR A 356 ? 0.3986 0.3549 0.3579 -0.0045 -0.0223 -0.0996 349 THR A CB 2379 O OG1 . THR A 356 ? 0.4562 0.4127 0.4312 -0.0056 -0.0188 -0.0971 349 THR A OG1 2380 C CG2 . THR A 356 ? 0.4028 0.3492 0.3507 -0.0026 -0.0253 -0.1088 349 THR A CG2 2381 N N . ASN A 357 ? 0.3596 0.3341 0.3180 -0.0046 -0.0168 -0.0838 350 ASN A N 2382 C CA . ASN A 357 ? 0.3481 0.3306 0.3166 -0.0061 -0.0155 -0.0765 350 ASN A CA 2383 C C . ASN A 357 ? 0.3631 0.3464 0.3456 -0.0095 -0.0210 -0.0767 350 ASN A C 2384 O O . ASN A 357 ? 0.3699 0.3502 0.3514 -0.0109 -0.0281 -0.0816 350 ASN A O 2385 C CB . ASN A 357 ? 0.3405 0.3271 0.2992 -0.0055 -0.0164 -0.0735 350 ASN A CB 2386 C CG . ASN A 357 ? 0.3690 0.3546 0.3145 -0.0026 -0.0105 -0.0730 350 ASN A CG 2387 O OD1 . ASN A 357 ? 0.3678 0.3540 0.3158 -0.0011 -0.0040 -0.0718 350 ASN A OD1 2388 N ND2 . ASN A 357 ? 0.4372 0.4214 0.3687 -0.0017 -0.0127 -0.0737 350 ASN A ND2 2389 N N . GLU A 358 ? 0.3359 0.3229 0.3319 -0.0107 -0.0179 -0.0716 351 GLU A N 2390 C CA . GLU A 358 ? 0.3478 0.3360 0.3584 -0.0140 -0.0218 -0.0712 351 GLU A CA 2391 C C . GLU A 358 ? 0.3117 0.3062 0.3325 -0.0147 -0.0181 -0.0637 351 GLU A C 2392 O O . GLU A 358 ? 0.2824 0.2778 0.3024 -0.0128 -0.0121 -0.0596 351 GLU A O 2393 C CB . GLU A 358 ? 0.3727 0.3544 0.3920 -0.0154 -0.0221 -0.0750 351 GLU A CB 2394 C CG . GLU A 358 ? 0.4647 0.4419 0.4811 -0.0129 -0.0162 -0.0751 351 GLU A CG 2395 C CD . GLU A 358 ? 0.5874 0.5563 0.6097 -0.0141 -0.0183 -0.0809 351 GLU A CD 2396 O OE1 . GLU A 358 ? 0.5687 0.5349 0.6009 -0.0145 -0.0145 -0.0785 351 GLU A OE1 2397 O OE2 . GLU A 358 ? 0.6956 0.6604 0.7127 -0.0148 -0.0244 -0.0878 351 GLU A OE2 2398 N N . VAL A 359 ? 0.3038 0.3025 0.3337 -0.0171 -0.0219 -0.0623 352 VAL A N 2399 C CA . VAL A 359 ? 0.2884 0.2931 0.3276 -0.0176 -0.0184 -0.0554 352 VAL A CA 2400 C C . VAL A 359 ? 0.2894 0.2909 0.3406 -0.0187 -0.0139 -0.0532 352 VAL A C 2401 O O . VAL A 359 ? 0.2753 0.2728 0.3357 -0.0212 -0.0163 -0.0566 352 VAL A O 2402 C CB . VAL A 359 ? 0.2994 0.3094 0.3462 -0.0196 -0.0237 -0.0551 352 VAL A CB 2403 C CG1 . VAL A 359 ? 0.2772 0.2928 0.3350 -0.0200 -0.0191 -0.0482 352 VAL A CG1 2404 C CG2 . VAL A 359 ? 0.3075 0.3196 0.3407 -0.0179 -0.0280 -0.0566 352 VAL A CG2 2405 N N . THR A 360 ? 0.2675 0.2700 0.3177 -0.0165 -0.0076 -0.0475 353 THR A N 2406 C CA . THR A 360 ? 0.2683 0.2661 0.3249 -0.0161 -0.0026 -0.0449 353 THR A CA 2407 C C . THR A 360 ? 0.2682 0.2698 0.3281 -0.0149 0.0023 -0.0373 353 THR A C 2408 O O . THR A 360 ? 0.2526 0.2589 0.3048 -0.0127 0.0030 -0.0348 353 THR A O 2409 C CB . THR A 360 ? 0.2678 0.2608 0.3151 -0.0132 -0.0005 -0.0472 353 THR A CB 2410 O OG1 . THR A 360 ? 0.2959 0.2854 0.3376 -0.0139 -0.0049 -0.0545 353 THR A OG1 2411 C CG2 . THR A 360 ? 0.2813 0.2680 0.3355 -0.0126 0.0037 -0.0450 353 THR A CG2 2412 N N . ARG A 361 ? 0.2591 0.2579 0.3297 -0.0161 0.0059 -0.0337 354 ARG A N 2413 C CA . ARG A 361 ? 0.2541 0.2549 0.3263 -0.0143 0.0114 -0.0265 354 ARG A CA 2414 C C . ARG A 361 ? 0.2532 0.2511 0.3156 -0.0100 0.0150 -0.0236 354 ARG A C 2415 O O . ARG A 361 ? 0.2599 0.2518 0.3205 -0.0089 0.0156 -0.0254 354 ARG A O 2416 C CB . ARG A 361 ? 0.2725 0.2708 0.3588 -0.0169 0.0151 -0.0229 354 ARG A CB 2417 C CG . ARG A 361 ? 0.2788 0.2787 0.3656 -0.0147 0.0214 -0.0152 354 ARG A CG 2418 C CD . ARG A 361 ? 0.2874 0.2880 0.3902 -0.0183 0.0244 -0.0124 354 ARG A CD 2419 N NE . ARG A 361 ? 0.2901 0.2985 0.3998 -0.0209 0.0197 -0.0155 354 ARG A NE 2420 C CZ . ARG A 361 ? 0.3341 0.3462 0.4591 -0.0240 0.0212 -0.0138 354 ARG A CZ 2421 N NH1 . ARG A 361 ? 0.3208 0.3290 0.4559 -0.0251 0.0282 -0.0089 354 ARG A NH1 2422 N NH2 . ARG A 361 ? 0.3445 0.3640 0.4753 -0.0257 0.0160 -0.0169 354 ARG A NH2 2423 N N . ILE A 362 ? 0.2302 0.2321 0.2867 -0.0073 0.0168 -0.0194 355 ILE A N 2424 C CA . ILE A 362 ? 0.2307 0.2306 0.2787 -0.0030 0.0193 -0.0166 355 ILE A CA 2425 C C . ILE A 362 ? 0.2448 0.2445 0.2931 -0.0010 0.0236 -0.0100 355 ILE A C 2426 O O . ILE A 362 ? 0.2482 0.2514 0.3020 -0.0028 0.0247 -0.0080 355 ILE A O 2427 C CB . ILE A 362 ? 0.2196 0.2243 0.2579 -0.0011 0.0164 -0.0190 355 ILE A CB 2428 C CG1 . ILE A 362 ? 0.2149 0.2263 0.2521 -0.0018 0.0151 -0.0177 355 ILE A CG1 2429 C CG2 . ILE A 362 ? 0.1954 0.1989 0.2316 -0.0024 0.0134 -0.0253 355 ILE A CG2 2430 C CD1 . ILE A 362 ? 0.1804 0.1954 0.2083 0.0005 0.0136 -0.0183 355 ILE A CD1 2431 N N . TYR A 363 ? 0.2492 0.2447 0.2912 0.0030 0.0261 -0.0066 356 TYR A N 2432 C CA . TYR A 363 ? 0.2372 0.2304 0.2779 0.0054 0.0308 -0.0002 356 TYR A CA 2433 C C . TYR A 363 ? 0.2488 0.2418 0.2782 0.0106 0.0304 0.0018 356 TYR A C 2434 O O . TYR A 363 ? 0.2376 0.2268 0.2628 0.0135 0.0294 0.0012 356 TYR A O 2435 C CB . TYR A 363 ? 0.2414 0.2260 0.2865 0.0056 0.0350 0.0031 356 TYR A CB 2436 C CG . TYR A 363 ? 0.2537 0.2371 0.3117 0.0004 0.0357 0.0013 356 TYR A CG 2437 C CD1 . TYR A 363 ? 0.2694 0.2538 0.3364 -0.0020 0.0398 0.0050 356 TYR A CD1 2438 C CD2 . TYR A 363 ? 0.2800 0.2612 0.3420 -0.0018 0.0322 -0.0043 356 TYR A CD2 2439 C CE1 . TYR A 363 ? 0.2869 0.2706 0.3683 -0.0072 0.0398 0.0029 356 TYR A CE1 2440 C CE2 . TYR A 363 ? 0.3111 0.2907 0.3855 -0.0067 0.0318 -0.0067 356 TYR A CE2 2441 C CZ . TYR A 363 ? 0.3016 0.2828 0.3863 -0.0094 0.0354 -0.0030 356 TYR A CZ 2442 O OH . TYR A 363 ? 0.3412 0.3215 0.4400 -0.0144 0.0343 -0.0057 356 TYR A OH 2443 N N . ASN A 364 ? 0.2406 0.2374 0.2658 0.0121 0.0311 0.0043 357 ASN A N 2444 C CA . ASN A 364 ? 0.2474 0.2428 0.2618 0.0174 0.0305 0.0065 357 ASN A CA 2445 C C . ASN A 364 ? 0.2593 0.2480 0.2697 0.0207 0.0357 0.0128 357 ASN A C 2446 O O . ASN A 364 ? 0.2896 0.2781 0.3052 0.0188 0.0403 0.0159 357 ASN A O 2447 C CB . ASN A 364 ? 0.2341 0.2361 0.2443 0.0180 0.0282 0.0057 357 ASN A CB 2448 C CG . ASN A 364 ? 0.2591 0.2673 0.2717 0.0150 0.0237 0.0003 357 ASN A CG 2449 O OD1 . ASN A 364 ? 0.2449 0.2529 0.2578 0.0146 0.0214 -0.0030 357 ASN A OD1 2450 N ND2 . ASN A 364 ? 0.2537 0.2672 0.2672 0.0134 0.0228 -0.0001 357 ASN A ND2 2451 N N . VAL A 365 ? 0.2706 0.2539 0.2718 0.0259 0.0350 0.0148 358 VAL A N 2452 C CA . VAL A 365 ? 0.2685 0.2448 0.2619 0.0302 0.0396 0.0211 358 VAL A CA 2453 C C . VAL A 365 ? 0.2821 0.2609 0.2650 0.0342 0.0377 0.0215 358 VAL A C 2454 O O . VAL A 365 ? 0.2973 0.2788 0.2758 0.0362 0.0321 0.0182 358 VAL A O 2455 C CB . VAL A 365 ? 0.2839 0.2508 0.2715 0.0346 0.0399 0.0238 358 VAL A CB 2456 C CG1 . VAL A 365 ? 0.2934 0.2519 0.2728 0.0384 0.0462 0.0311 358 VAL A CG1 2457 C CG2 . VAL A 365 ? 0.2943 0.2587 0.2923 0.0309 0.0402 0.0217 358 VAL A CG2 2458 N N . ILE A 366 ? 0.2812 0.2591 0.2611 0.0352 0.0427 0.0255 359 ILE A N 2459 C CA . ILE A 366 ? 0.2760 0.2558 0.2461 0.0388 0.0414 0.0256 359 ILE A CA 2460 C C . ILE A 366 ? 0.2872 0.2578 0.2450 0.0446 0.0465 0.0317 359 ILE A C 2461 O O . ILE A 366 ? 0.2926 0.2601 0.2532 0.0437 0.0542 0.0364 359 ILE A O 2462 C CB . ILE A 366 ? 0.2632 0.2510 0.2406 0.0350 0.0428 0.0242 359 ILE A CB 2463 C CG1 . ILE A 366 ? 0.2524 0.2480 0.2410 0.0293 0.0381 0.0186 359 ILE A CG1 2464 C CG2 . ILE A 366 ? 0.2778 0.2665 0.2444 0.0394 0.0414 0.0241 359 ILE A CG2 2465 C CD1 . ILE A 366 ? 0.2764 0.2749 0.2605 0.0306 0.0309 0.0141 359 ILE A CD1 2466 N N . GLY A 367 ? 0.2885 0.2543 0.2330 0.0506 0.0422 0.0317 360 GLY A N 2467 C CA . GLY A 367 ? 0.3034 0.2588 0.2323 0.0575 0.0459 0.0373 360 GLY A CA 2468 C C . GLY A 367 ? 0.3146 0.2708 0.2319 0.0617 0.0444 0.0365 360 GLY A C 2469 O O . GLY A 367 ? 0.3142 0.2764 0.2323 0.0613 0.0375 0.0312 360 GLY A O 2470 N N . THR A 368 ? 0.3339 0.2836 0.2405 0.0657 0.0513 0.0416 361 THR A N 2471 C CA . THR A 368 ? 0.3540 0.3037 0.2489 0.0700 0.0505 0.0406 361 THR A CA 2472 C C . THR A 368 ? 0.3842 0.3216 0.2578 0.0787 0.0512 0.0446 361 THR A C 2473 O O . THR A 368 ? 0.3961 0.3249 0.2643 0.0807 0.0589 0.0511 361 THR A O 2474 C CB . THR A 368 ? 0.3595 0.3126 0.2602 0.0676 0.0595 0.0431 361 THR A CB 2475 O OG1 . THR A 368 ? 0.3191 0.2831 0.2388 0.0600 0.0582 0.0395 361 THR A OG1 2476 C CG2 . THR A 368 ? 0.3683 0.3205 0.2561 0.0726 0.0598 0.0422 361 THR A CG2 2477 N N . LEU A 369 ? 0.3797 0.3156 0.2407 0.0839 0.0433 0.0408 362 LEU A N 2478 C CA . LEU A 369 ? 0.3944 0.3184 0.2324 0.0930 0.0433 0.0438 362 LEU A CA 2479 C C . LEU A 369 ? 0.3942 0.3195 0.2238 0.0957 0.0439 0.0415 362 LEU A C 2480 O O . LEU A 369 ? 0.3946 0.3247 0.2248 0.0959 0.0351 0.0353 362 LEU A O 2481 C CB . LEU A 369 ? 0.3972 0.3176 0.2277 0.0975 0.0318 0.0405 362 LEU A CB 2482 C CG . LEU A 369 ? 0.4683 0.3755 0.2738 0.1076 0.0292 0.0429 362 LEU A CG 2483 C CD1 . LEU A 369 ? 0.4924 0.3881 0.2860 0.1112 0.0402 0.0517 362 LEU A CD1 2484 C CD2 . LEU A 369 ? 0.4646 0.3701 0.2685 0.1109 0.0173 0.0394 362 LEU A CD2 2485 N N A ARG A 370 ? 0.3829 0.3043 0.2064 0.0974 0.0547 0.0464 363 ARG A N 2486 N N B ARG A 370 ? 0.3878 0.3088 0.2108 0.0977 0.0546 0.0465 363 ARG A N 2487 C CA A ARG A 370 ? 0.3922 0.3160 0.2109 0.0992 0.0565 0.0441 363 ARG A CA 2488 C CA B ARG A 370 ? 0.4027 0.3258 0.2200 0.0997 0.0562 0.0441 363 ARG A CA 2489 C C A ARG A 370 ? 0.3979 0.3139 0.1946 0.1077 0.0488 0.0407 363 ARG A C 2490 C C B ARG A 370 ? 0.4034 0.3193 0.1997 0.1079 0.0481 0.0405 363 ARG A C 2491 O O A ARG A 370 ? 0.4005 0.3051 0.1787 0.1147 0.0485 0.0440 363 ARG A O 2492 O O B ARG A 370 ? 0.4073 0.3117 0.1850 0.1149 0.0471 0.0434 363 ARG A O 2493 C CB A ARG A 370 ? 0.4046 0.3255 0.2220 0.0998 0.0707 0.0505 363 ARG A CB 2494 C CB B ARG A 370 ? 0.4190 0.3379 0.2325 0.1012 0.0701 0.0506 363 ARG A CB 2495 C CG A ARG A 370 ? 0.3960 0.3180 0.2067 0.1030 0.0741 0.0486 363 ARG A CG 2496 C CG B ARG A 370 ? 0.4207 0.3476 0.2568 0.0930 0.0781 0.0535 363 ARG A CG 2497 C CD A ARG A 370 ? 0.4723 0.3958 0.2903 0.1013 0.0889 0.0543 363 ARG A CD 2498 C CD B ARG A 370 ? 0.5126 0.4343 0.3444 0.0953 0.0926 0.0606 363 ARG A CD 2499 N NE A ARG A 370 ? 0.5158 0.4402 0.3273 0.1050 0.0923 0.0523 363 ARG A NE 2500 N NE B ARG A 370 ? 0.5302 0.4557 0.3813 0.0885 0.1002 0.0648 363 ARG A NE 2501 C CZ A ARG A 370 ? 0.4890 0.4243 0.3177 0.1003 0.0943 0.0496 363 ARG A CZ 2502 C CZ B ARG A 370 ? 0.5441 0.4613 0.3916 0.0899 0.1112 0.0726 363 ARG A CZ 2503 N NH1 A ARG A 370 ? 0.4456 0.3919 0.2986 0.0916 0.0936 0.0488 363 ARG A NH1 2504 N NH1 B ARG A 370 ? 0.5900 0.4945 0.4137 0.0984 0.1164 0.0774 363 ARG A NH1 2505 N NH2 A ARG A 370 ? 0.5181 0.4528 0.3391 0.1047 0.0970 0.0477 363 ARG A NH2 2506 N NH2 B ARG A 370 ? 0.5448 0.4662 0.4125 0.0830 0.1169 0.0755 363 ARG A NH2 2507 N N . GLY A 371 ? 0.3939 0.3161 0.1935 0.1070 0.0417 0.0341 364 GLY A N 2508 C CA . GLY A 371 ? 0.4108 0.3264 0.1916 0.1144 0.0340 0.0297 364 GLY A CA 2509 C C . GLY A 371 ? 0.4423 0.3472 0.2013 0.1223 0.0423 0.0335 364 GLY A C 2510 O O . GLY A 371 ? 0.4570 0.3637 0.2201 0.1207 0.0538 0.0373 364 GLY A O 2511 N N . ALA A 372 ? 0.4657 0.3591 0.2014 0.1311 0.0363 0.0324 365 ALA A N 2512 C CA . ALA A 372 ? 0.4981 0.3792 0.2085 0.1401 0.0431 0.0354 365 ALA A CA 2513 C C . ALA A 372 ? 0.5117 0.3957 0.2202 0.1413 0.0432 0.0303 365 ALA A C 2514 O O . ALA A 372 ? 0.5263 0.4052 0.2239 0.1454 0.0538 0.0335 365 ALA A O 2515 C CB . ALA A 372 ? 0.5128 0.3803 0.1977 0.1496 0.0348 0.0349 365 ALA A CB 2516 N N . VAL A 373 ? 0.4900 0.3818 0.2096 0.1379 0.0318 0.0224 366 VAL A N 2517 C CA . VAL A 373 ? 0.5002 0.3924 0.2149 0.1403 0.0295 0.0166 366 VAL A CA 2518 C C . VAL A 373 ? 0.4658 0.3724 0.2066 0.1312 0.0299 0.0136 366 VAL A C 2519 O O . VAL A 373 ? 0.4515 0.3602 0.1939 0.1314 0.0359 0.0129 366 VAL A O 2520 C CB . VAL A 373 ? 0.5137 0.3995 0.2143 0.1460 0.0146 0.0092 366 VAL A CB 2521 C CG1 . VAL A 373 ? 0.5369 0.4222 0.2329 0.1485 0.0120 0.0029 366 VAL A CG1 2522 C CG2 . VAL A 373 ? 0.5585 0.4290 0.2310 0.1560 0.0131 0.0119 366 VAL A CG2 2523 N N . GLU A 374 ? 0.4313 0.3474 0.1920 0.1235 0.0236 0.0119 367 GLU A N 2524 C CA . GLU A 374 ? 0.4169 0.3461 0.2015 0.1149 0.0236 0.0095 367 GLU A CA 2525 C C . GLU A 374 ? 0.3867 0.3238 0.1899 0.1073 0.0286 0.0140 367 GLU A C 2526 O O . GLU A 374 ? 0.3673 0.3111 0.1843 0.1017 0.0217 0.0115 367 GLU A O 2527 C CB . GLU A 374 ? 0.3937 0.3274 0.1858 0.1123 0.0105 0.0019 367 GLU A CB 2528 C CG . GLU A 374 ? 0.4426 0.3684 0.2178 0.1194 0.0037 -0.0037 367 GLU A CG 2529 C CD . GLU A 374 ? 0.4411 0.3721 0.2274 0.1157 -0.0081 -0.0109 367 GLU A CD 2530 O OE1 . GLU A 374 ? 0.4390 0.3766 0.2376 0.1113 -0.0077 -0.0133 367 GLU A OE1 2531 O OE2 . GLU A 374 ? 0.4721 0.4005 0.2553 0.1174 -0.0182 -0.0141 367 GLU A OE2 2532 N N . PRO A 375 ? 0.3970 0.3331 0.2009 0.1071 0.0408 0.0204 368 PRO A N 2533 C CA . PRO A 375 ? 0.3731 0.3154 0.1942 0.1003 0.0459 0.0247 368 PRO A CA 2534 C C . PRO A 375 ? 0.3508 0.3060 0.1949 0.0918 0.0438 0.0216 368 PRO A C 2535 O O . PRO A 375 ? 0.3333 0.2941 0.1917 0.0857 0.0439 0.0228 368 PRO A O 2536 C CB . PRO A 375 ? 0.3692 0.3073 0.1858 0.1026 0.0598 0.0316 368 PRO A CB 2537 C CG . PRO A 375 ? 0.4289 0.3624 0.2319 0.1087 0.0627 0.0301 368 PRO A CG 2538 C CD . PRO A 375 ? 0.4140 0.3421 0.2021 0.1138 0.0507 0.0241 368 PRO A CD 2539 N N . ASP A 376 ? 0.3586 0.3176 0.2049 0.0918 0.0416 0.0175 369 ASP A N 2540 C CA . ASP A 376 ? 0.3452 0.3153 0.2112 0.0845 0.0387 0.0145 369 ASP A CA 2541 C C . ASP A 376 ? 0.3333 0.3062 0.2027 0.0821 0.0270 0.0087 369 ASP A C 2542 O O . ASP A 376 ? 0.3071 0.2867 0.1875 0.0780 0.0237 0.0055 369 ASP A O 2543 C CB . ASP A 376 ? 0.3453 0.3181 0.2137 0.0856 0.0431 0.0135 369 ASP A CB 2544 C CG . ASP A 376 ? 0.4015 0.3685 0.2557 0.0914 0.0373 0.0087 369 ASP A CG 2545 O OD1 . ASP A 376 ? 0.4176 0.3768 0.2568 0.0961 0.0318 0.0071 369 ASP A OD1 2546 O OD2 . ASP A 376 ? 0.4358 0.4058 0.2941 0.0914 0.0376 0.0062 369 ASP A OD2 2547 N N . ARG A 377 ? 0.3315 0.2995 0.1929 0.0844 0.0209 0.0077 370 ARG A N 2548 C CA . ARG A 377 ? 0.3124 0.2838 0.1796 0.0818 0.0105 0.0026 370 ARG A CA 2549 C C . ARG A 377 ? 0.3208 0.2928 0.1928 0.0795 0.0097 0.0048 370 ARG A C 2550 O O . ARG A 377 ? 0.3294 0.2941 0.1902 0.0840 0.0123 0.0083 370 ARG A O 2551 C CB . ARG A 377 ? 0.3141 0.2782 0.1666 0.0882 0.0024 -0.0017 370 ARG A CB 2552 C CG . ARG A 377 ? 0.3297 0.2930 0.1783 0.0903 0.0025 -0.0048 370 ARG A CG 2553 C CD . ARG A 377 ? 0.3419 0.3143 0.2081 0.0833 -0.0016 -0.0082 370 ARG A CD 2554 N NE . ARG A 377 ? 0.3094 0.2819 0.1754 0.0842 -0.0019 -0.0110 370 ARG A NE 2555 C CZ . ARG A 377 ? 0.3263 0.3028 0.1988 0.0823 0.0050 -0.0089 370 ARG A CZ 2556 N NH1 . ARG A 377 ? 0.3001 0.2808 0.1797 0.0795 0.0132 -0.0038 370 ARG A NH1 2557 N NH2 . ARG A 377 ? 0.3184 0.2947 0.1912 0.0834 0.0034 -0.0120 370 ARG A NH2 2558 N N . TYR A 378 ? 0.2870 0.2671 0.1748 0.0728 0.0069 0.0031 371 TYR A N 2559 C CA . TYR A 378 ? 0.2917 0.2734 0.1866 0.0698 0.0074 0.0050 371 TYR A CA 2560 C C . TYR A 378 ? 0.2854 0.2691 0.1845 0.0688 -0.0013 0.0010 371 TYR A C 2561 O O . TYR A 378 ? 0.2971 0.2869 0.2057 0.0649 -0.0056 -0.0027 371 TYR A O 2562 C CB . TYR A 378 ? 0.2643 0.2537 0.1749 0.0626 0.0123 0.0066 371 TYR A CB 2563 C CG . TYR A 378 ? 0.3123 0.3022 0.2243 0.0621 0.0210 0.0103 371 TYR A CG 2564 C CD1 . TYR A 378 ? 0.3292 0.3118 0.2295 0.0674 0.0273 0.0145 371 TYR A CD1 2565 C CD2 . TYR A 378 ? 0.2611 0.2586 0.1865 0.0565 0.0231 0.0099 371 TYR A CD2 2566 C CE1 . TYR A 378 ? 0.3388 0.3229 0.2432 0.0666 0.0361 0.0179 371 TYR A CE1 2567 C CE2 . TYR A 378 ? 0.2800 0.2792 0.2097 0.0558 0.0306 0.0129 371 TYR A CE2 2568 C CZ . TYR A 378 ? 0.3191 0.3120 0.2395 0.0605 0.0374 0.0170 371 TYR A CZ 2569 O OH . TYR A 378 ? 0.2941 0.2892 0.2204 0.0599 0.0455 0.0201 371 TYR A OH 2570 N N . VAL A 379 ? 0.2981 0.2765 0.1907 0.0726 -0.0037 0.0021 372 VAL A N 2571 C CA . VAL A 379 ? 0.2855 0.2666 0.1852 0.0714 -0.0108 -0.0010 372 VAL A CA 2572 C C . VAL A 379 ? 0.2804 0.2635 0.1887 0.0679 -0.0064 0.0019 372 VAL A C 2573 O O . VAL A 379 ? 0.2895 0.2667 0.1912 0.0704 -0.0015 0.0064 372 VAL A O 2574 C CB . VAL A 379 ? 0.3031 0.2766 0.1897 0.0789 -0.0181 -0.0026 372 VAL A CB 2575 C CG1 . VAL A 379 ? 0.3342 0.3111 0.2302 0.0781 -0.0256 -0.0059 372 VAL A CG1 2576 C CG2 . VAL A 379 ? 0.3214 0.2923 0.1992 0.0824 -0.0224 -0.0060 372 VAL A CG2 2577 N N . ILE A 380 ? 0.2666 0.2574 0.1893 0.0620 -0.0079 -0.0006 373 ILE A N 2578 C CA . ILE A 380 ? 0.2625 0.2556 0.1941 0.0580 -0.0036 0.0013 373 ILE A CA 2579 C C . ILE A 380 ? 0.2631 0.2573 0.2003 0.0584 -0.0085 -0.0008 373 ILE A C 2580 O O . ILE A 380 ? 0.2781 0.2770 0.2217 0.0572 -0.0139 -0.0050 373 ILE A O 2581 C CB . ILE A 380 ? 0.2309 0.2315 0.1738 0.0511 -0.0003 0.0005 373 ILE A CB 2582 C CG1 . ILE A 380 ? 0.2748 0.2748 0.2133 0.0514 0.0037 0.0023 373 ILE A CG1 2583 C CG2 . ILE A 380 ? 0.2192 0.2213 0.1708 0.0470 0.0037 0.0019 373 ILE A CG2 2584 C CD1 . ILE A 380 ? 0.3030 0.3101 0.2520 0.0452 0.0060 0.0014 373 ILE A CD1 2585 N N . LEU A 381 ? 0.2622 0.2516 0.1974 0.0604 -0.0063 0.0020 374 LEU A N 2586 C CA . LEU A 381 ? 0.2577 0.2485 0.2004 0.0603 -0.0095 0.0002 374 LEU A CA 2587 C C . LEU A 381 ? 0.2564 0.2495 0.2082 0.0551 -0.0038 0.0014 374 LEU A C 2588 O O . LEU A 381 ? 0.2817 0.2696 0.2301 0.0556 0.0014 0.0056 374 LEU A O 2589 C CB . LEU A 381 ? 0.2628 0.2453 0.1955 0.0674 -0.0128 0.0022 374 LEU A CB 2590 C CG . LEU A 381 ? 0.2904 0.2732 0.2305 0.0684 -0.0157 0.0010 374 LEU A CG 2591 C CD1 . LEU A 381 ? 0.2563 0.2472 0.2075 0.0670 -0.0224 -0.0047 374 LEU A CD1 2592 C CD2 . LEU A 381 ? 0.2770 0.2499 0.2052 0.0761 -0.0184 0.0042 374 LEU A CD2 2593 N N . GLY A 382 ? 0.2386 0.2390 0.2021 0.0504 -0.0048 -0.0021 375 GLY A N 2594 C CA . GLY A 382 ? 0.2417 0.2443 0.2130 0.0452 0.0001 -0.0018 375 GLY A CA 2595 C C . GLY A 382 ? 0.2417 0.2478 0.2223 0.0437 -0.0015 -0.0052 375 GLY A C 2596 O O . GLY A 382 ? 0.2350 0.2459 0.2201 0.0437 -0.0055 -0.0086 375 GLY A O 2597 N N . GLY A 383 ? 0.2495 0.2532 0.2338 0.0421 0.0019 -0.0044 376 GLY A N 2598 C CA . GLY A 383 ? 0.2390 0.2460 0.2321 0.0406 0.0013 -0.0079 376 GLY A CA 2599 C C . GLY A 383 ? 0.2557 0.2599 0.2519 0.0376 0.0059 -0.0071 376 GLY A C 2600 O O . GLY A 383 ? 0.2529 0.2520 0.2454 0.0376 0.0089 -0.0035 376 GLY A O 2601 N N . HIS A 384 ? 0.2438 0.2510 0.2471 0.0350 0.0066 -0.0107 377 HIS A N 2602 C CA . HIS A 384 ? 0.2350 0.2396 0.2414 0.0317 0.0103 -0.0111 377 HIS A CA 2603 C C . HIS A 384 ? 0.2517 0.2497 0.2597 0.0345 0.0112 -0.0102 377 HIS A C 2604 O O . HIS A 384 ? 0.2700 0.2664 0.2777 0.0391 0.0086 -0.0100 377 HIS A O 2605 C CB . HIS A 384 ? 0.2207 0.2309 0.2317 0.0273 0.0110 -0.0155 377 HIS A CB 2606 C CG . HIS A 384 ? 0.1859 0.1982 0.2020 0.0284 0.0105 -0.0193 377 HIS A CG 2607 N ND1 . HIS A 384 ? 0.2141 0.2238 0.2336 0.0273 0.0127 -0.0218 377 HIS A ND1 2608 C CD2 . HIS A 384 ? 0.1909 0.2084 0.2103 0.0298 0.0087 -0.0215 377 HIS A CD2 2609 C CE1 . HIS A 384 ? 0.1745 0.1875 0.1985 0.0285 0.0127 -0.0252 377 HIS A CE1 2610 N NE2 . HIS A 384 ? 0.2000 0.2180 0.2249 0.0299 0.0104 -0.0249 377 HIS A NE2 2611 N N . ARG A 385 ? 0.2413 0.2352 0.2515 0.0316 0.0144 -0.0098 378 ARG A N 2612 C CA . ARG A 385 ? 0.2554 0.2415 0.2671 0.0335 0.0160 -0.0083 378 ARG A CA 2613 C C . ARG A 385 ? 0.2456 0.2316 0.2637 0.0305 0.0173 -0.0129 378 ARG A C 2614 O O . ARG A 385 ? 0.2627 0.2433 0.2835 0.0326 0.0178 -0.0135 378 ARG A O 2615 C CB . ARG A 385 ? 0.2505 0.2308 0.2597 0.0324 0.0194 -0.0033 378 ARG A CB 2616 C CG . ARG A 385 ? 0.2642 0.2349 0.2751 0.0338 0.0220 -0.0006 378 ARG A CG 2617 C CD . ARG A 385 ? 0.2878 0.2537 0.2987 0.0315 0.0264 0.0041 378 ARG A CD 2618 N NE . ARG A 385 ? 0.2688 0.2388 0.2870 0.0251 0.0276 0.0010 378 ARG A NE 2619 C CZ . ARG A 385 ? 0.2644 0.2403 0.2830 0.0220 0.0280 0.0011 378 ARG A CZ 2620 N NH1 . ARG A 385 ? 0.2620 0.2406 0.2740 0.0244 0.0278 0.0040 378 ARG A NH1 2621 N NH2 . ARG A 385 ? 0.2566 0.2355 0.2823 0.0167 0.0280 -0.0021 378 ARG A NH2 2622 N N . ASP A 386 ? 0.2276 0.2187 0.2474 0.0258 0.0177 -0.0162 379 ASP A N 2623 C CA . ASP A 386 ? 0.2284 0.2183 0.2522 0.0231 0.0186 -0.0211 379 ASP A CA 2624 C C . ASP A 386 ? 0.2340 0.2269 0.2595 0.0256 0.0179 -0.0249 379 ASP A C 2625 O O . ASP A 386 ? 0.2331 0.2316 0.2576 0.0272 0.0164 -0.0246 379 ASP A O 2626 C CB . ASP A 386 ? 0.2092 0.2033 0.2326 0.0181 0.0185 -0.0236 379 ASP A CB 2627 C CG . ASP A 386 ? 0.2322 0.2341 0.2524 0.0178 0.0170 -0.0247 379 ASP A CG 2628 O OD1 . ASP A 386 ? 0.2356 0.2403 0.2534 0.0194 0.0160 -0.0213 379 ASP A OD1 2629 O OD2 . ASP A 386 ? 0.2190 0.2237 0.2388 0.0159 0.0171 -0.0289 379 ASP A OD2 2630 N N . SER A 387 ? 0.2355 0.2247 0.2644 0.0259 0.0191 -0.0285 380 SER A N 2631 C CA . SER A 387 ? 0.2509 0.2427 0.2827 0.0289 0.0193 -0.0321 380 SER A CA 2632 C C . SER A 387 ? 0.2571 0.2480 0.2895 0.0265 0.0212 -0.0378 380 SER A C 2633 O O . SER A 387 ? 0.2579 0.2441 0.2893 0.0235 0.0216 -0.0389 380 SER A O 2634 C CB . SER A 387 ? 0.2521 0.2387 0.2872 0.0342 0.0186 -0.0302 380 SER A CB 2635 O OG . SER A 387 ? 0.2836 0.2613 0.3201 0.0340 0.0200 -0.0303 380 SER A OG 2636 N N . TRP A 388 ? 0.2678 0.2626 0.3021 0.0281 0.0227 -0.0417 381 TRP A N 2637 C CA . TRP A 388 ? 0.2638 0.2563 0.2970 0.0267 0.0250 -0.0473 381 TRP A CA 2638 C C . TRP A 388 ? 0.2798 0.2639 0.3164 0.0289 0.0256 -0.0490 381 TRP A C 2639 O O . TRP A 388 ? 0.2970 0.2754 0.3316 0.0264 0.0258 -0.0519 381 TRP A O 2640 C CB . TRP A 388 ? 0.2651 0.2640 0.2988 0.0278 0.0278 -0.0508 381 TRP A CB 2641 C CG . TRP A 388 ? 0.2627 0.2671 0.2906 0.0241 0.0278 -0.0502 381 TRP A CG 2642 C CD1 . TRP A 388 ? 0.2690 0.2808 0.2982 0.0241 0.0277 -0.0480 381 TRP A CD1 2643 C CD2 . TRP A 388 ? 0.2746 0.2769 0.2950 0.0201 0.0271 -0.0517 381 TRP A CD2 2644 N NE1 . TRP A 388 ? 0.2696 0.2837 0.2919 0.0204 0.0276 -0.0477 381 TRP A NE1 2645 C CE2 . TRP A 388 ? 0.2730 0.2815 0.2897 0.0181 0.0270 -0.0500 381 TRP A CE2 2646 C CE3 . TRP A 388 ? 0.2627 0.2584 0.2798 0.0182 0.0262 -0.0547 381 TRP A CE3 2647 C CZ2 . TRP A 388 ? 0.2808 0.2889 0.2899 0.0146 0.0259 -0.0507 381 TRP A CZ2 2648 C CZ3 . TRP A 388 ? 0.2468 0.2426 0.2568 0.0145 0.0245 -0.0557 381 TRP A CZ3 2649 C CH2 . TRP A 388 ? 0.2568 0.2587 0.2626 0.0129 0.0243 -0.0535 381 TRP A CH2 2650 N N . VAL A 389 ? 0.2675 0.2503 0.3095 0.0336 0.0253 -0.0474 382 VAL A N 2651 C CA . VAL A 389 ? 0.2727 0.2464 0.3182 0.0361 0.0256 -0.0482 382 VAL A CA 2652 C C . VAL A 389 ? 0.2762 0.2470 0.3234 0.0393 0.0233 -0.0419 382 VAL A C 2653 O O . VAL A 389 ? 0.2628 0.2314 0.3067 0.0371 0.0224 -0.0375 382 VAL A O 2654 C CB . VAL A 389 ? 0.2714 0.2446 0.3212 0.0396 0.0282 -0.0538 382 VAL A CB 2655 C CG1 . VAL A 389 ? 0.2800 0.2421 0.3325 0.0413 0.0284 -0.0554 382 VAL A CG1 2656 C CG2 . VAL A 389 ? 0.2896 0.2661 0.3349 0.0368 0.0310 -0.0596 382 VAL A CG2 2657 N N . PHE A 390 ? 0.2690 0.2398 0.3209 0.0448 0.0225 -0.0413 383 PHE A N 2658 C CA . PHE A 390 ? 0.2704 0.2364 0.3221 0.0487 0.0199 -0.0355 383 PHE A CA 2659 C C . PHE A 390 ? 0.2722 0.2448 0.3209 0.0496 0.0170 -0.0315 383 PHE A C 2660 O O . PHE A 390 ? 0.2796 0.2478 0.3241 0.0516 0.0151 -0.0260 383 PHE A O 2661 C CB . PHE A 390 ? 0.2699 0.2321 0.3279 0.0549 0.0192 -0.0368 383 PHE A CB 2662 C CG . PHE A 390 ? 0.2980 0.2523 0.3586 0.0546 0.0219 -0.0406 383 PHE A CG 2663 C CD1 . PHE A 390 ? 0.3098 0.2532 0.3681 0.0530 0.0224 -0.0378 383 PHE A CD1 2664 C CD2 . PHE A 390 ? 0.3181 0.2753 0.3835 0.0556 0.0242 -0.0472 383 PHE A CD2 2665 C CE1 . PHE A 390 ? 0.3208 0.2560 0.3821 0.0523 0.0244 -0.0419 383 PHE A CE1 2666 C CE2 . PHE A 390 ? 0.3192 0.2681 0.3861 0.0554 0.0265 -0.0516 383 PHE A CE2 2667 C CZ . PHE A 390 ? 0.3064 0.2442 0.3713 0.0536 0.0261 -0.0491 383 PHE A CZ 2668 N N . GLY A 391 ? 0.2625 0.2450 0.3128 0.0482 0.0170 -0.0343 384 GLY A N 2669 C CA . GLY A 391 ? 0.2570 0.2456 0.3044 0.0484 0.0140 -0.0311 384 GLY A CA 2670 C C . GLY A 391 ? 0.2584 0.2470 0.3082 0.0545 0.0097 -0.0287 384 GLY A C 2671 O O . GLY A 391 ? 0.2607 0.2498 0.3053 0.0556 0.0065 -0.0249 384 GLY A O 2672 N N . GLY A 392 ? 0.2635 0.2515 0.3209 0.0589 0.0092 -0.0313 385 GLY A N 2673 C CA . GLY A 392 ? 0.2604 0.2478 0.3214 0.0656 0.0043 -0.0296 385 GLY A CA 2674 C C . GLY A 392 ? 0.2745 0.2705 0.3364 0.0661 0.0001 -0.0292 385 GLY A C 2675 O O . GLY A 392 ? 0.2839 0.2774 0.3420 0.0704 -0.0050 -0.0258 385 GLY A O 2676 N N . ILE A 393 ? 0.2605 0.2658 0.3270 0.0621 0.0022 -0.0326 386 ILE A N 2677 C CA . ILE A 393 ? 0.2620 0.2747 0.3292 0.0616 -0.0015 -0.0322 386 ILE A CA 2678 C C . ILE A 393 ? 0.2665 0.2794 0.3242 0.0560 0.0005 -0.0302 386 ILE A C 2679 O O . ILE A 393 ? 0.2699 0.2810 0.3199 0.0565 -0.0028 -0.0268 386 ILE A O 2680 C CB . ILE A 393 ? 0.2479 0.2711 0.3285 0.0614 -0.0008 -0.0368 386 ILE A CB 2681 C CG1 . ILE A 393 ? 0.2713 0.2953 0.3627 0.0681 -0.0048 -0.0383 386 ILE A CG1 2682 C CG2 . ILE A 393 ? 0.2541 0.2847 0.3349 0.0586 -0.0032 -0.0366 386 ILE A CG2 2683 C CD1 . ILE A 393 ? 0.2952 0.3295 0.4027 0.0679 -0.0022 -0.0432 386 ILE A CD1 2684 N N . ASP A 394 ? 0.2542 0.2687 0.3118 0.0511 0.0058 -0.0326 387 ASP A N 2685 C CA . ASP A 394 ? 0.2502 0.2662 0.3006 0.0458 0.0075 -0.0315 387 ASP A CA 2686 C C . ASP A 394 ? 0.2381 0.2465 0.2809 0.0431 0.0101 -0.0295 387 ASP A C 2687 O O . ASP A 394 ? 0.2580 0.2642 0.3018 0.0411 0.0137 -0.0323 387 ASP A O 2688 C CB . ASP A 394 ? 0.2343 0.2576 0.2898 0.0422 0.0112 -0.0355 387 ASP A CB 2689 C CG . ASP A 394 ? 0.2621 0.2872 0.3106 0.0370 0.0128 -0.0347 387 ASP A CG 2690 O OD1 . ASP A 394 ? 0.2702 0.2928 0.3120 0.0362 0.0105 -0.0313 387 ASP A OD1 2691 O OD2 . ASP A 394 ? 0.2670 0.2957 0.3165 0.0339 0.0165 -0.0375 387 ASP A OD2 2692 N N . PRO A 395 ? 0.2408 0.2449 0.2761 0.0431 0.0085 -0.0250 388 PRO A N 2693 C CA . PRO A 395 ? 0.2375 0.2430 0.2686 0.0454 0.0045 -0.0219 388 PRO A CA 2694 C C . PRO A 395 ? 0.2613 0.2597 0.2886 0.0512 0.0014 -0.0182 388 PRO A C 2695 O O . PRO A 395 ? 0.2613 0.2591 0.2827 0.0536 -0.0018 -0.0155 388 PRO A O 2696 C CB . PRO A 395 ? 0.2377 0.2420 0.2615 0.0412 0.0065 -0.0194 388 PRO A CB 2697 C CG . PRO A 395 ? 0.2367 0.2337 0.2598 0.0394 0.0102 -0.0185 388 PRO A CG 2698 C CD . PRO A 395 ? 0.2264 0.2241 0.2568 0.0400 0.0114 -0.0232 388 PRO A CD 2699 N N . GLN A 396 ? 0.2546 0.2464 0.2837 0.0536 0.0026 -0.0177 389 GLN A N 2700 C CA . GLN A 396 ? 0.2762 0.2587 0.2983 0.0584 0.0009 -0.0127 389 GLN A CA 2701 C C . GLN A 396 ? 0.2723 0.2556 0.2934 0.0648 -0.0055 -0.0120 389 GLN A C 2702 O O . GLN A 396 ? 0.2898 0.2664 0.3014 0.0686 -0.0076 -0.0075 389 GLN A O 2703 C CB . GLN A 396 ? 0.2808 0.2546 0.3049 0.0598 0.0034 -0.0118 389 GLN A CB 2704 C CG . GLN A 396 ? 0.2918 0.2632 0.3171 0.0539 0.0089 -0.0128 389 GLN A CG 2705 C CD . GLN A 396 ? 0.2954 0.2669 0.3146 0.0492 0.0113 -0.0097 389 GLN A CD 2706 O OE1 . GLN A 396 ? 0.2977 0.2682 0.3097 0.0509 0.0101 -0.0056 389 GLN A OE1 2707 N NE2 . GLN A 396 ? 0.2526 0.2246 0.2749 0.0437 0.0147 -0.0120 389 GLN A NE2 2708 N N . SER A 397 ? 0.2619 0.2533 0.2927 0.0659 -0.0085 -0.0165 390 SER A N 2709 C CA . SER A 397 ? 0.2786 0.2720 0.3094 0.0714 -0.0158 -0.0165 390 SER A CA 2710 C C . SER A 397 ? 0.2717 0.2660 0.2930 0.0707 -0.0183 -0.0144 390 SER A C 2711 O O . SER A 397 ? 0.2844 0.2747 0.2985 0.0761 -0.0240 -0.0123 390 SER A O 2712 C CB . SER A 397 ? 0.2842 0.2873 0.3297 0.0723 -0.0185 -0.0218 390 SER A CB 2713 O OG . SER A 397 ? 0.2879 0.2998 0.3381 0.0666 -0.0160 -0.0247 390 SER A OG 2714 N N . GLY A 398 ? 0.2563 0.2547 0.2764 0.0644 -0.0140 -0.0149 391 GLY A N 2715 C CA . GLY A 398 ? 0.2374 0.2362 0.2486 0.0632 -0.0152 -0.0130 391 GLY A CA 2716 C C . GLY A 398 ? 0.2645 0.2537 0.2628 0.0644 -0.0124 -0.0074 391 GLY A C 2717 O O . GLY A 398 ? 0.2823 0.2671 0.2702 0.0684 -0.0156 -0.0047 391 GLY A O 2718 N N . ALA A 399 ? 0.2610 0.2464 0.2599 0.0612 -0.0064 -0.0059 392 ALA A N 2719 C CA . ALA A 399 ? 0.2829 0.2596 0.2721 0.0612 -0.0023 -0.0003 392 ALA A CA 2720 C C . ALA A 399 ? 0.2914 0.2580 0.2715 0.0682 -0.0044 0.0042 392 ALA A C 2721 O O . ALA A 399 ? 0.2891 0.2494 0.2578 0.0702 -0.0027 0.0090 392 ALA A O 2722 C CB . ALA A 399 ? 0.2735 0.2483 0.2681 0.0562 0.0036 -0.0003 392 ALA A CB 2723 N N . ALA A 400 ? 0.2909 0.2556 0.2756 0.0725 -0.0080 0.0028 393 ALA A N 2724 C CA . ALA A 400 ? 0.3138 0.2687 0.2900 0.0801 -0.0113 0.0068 393 ALA A CA 2725 C C . ALA A 400 ? 0.3261 0.2806 0.2919 0.0852 -0.0176 0.0075 393 ALA A C 2726 O O . ALA A 400 ? 0.3260 0.2706 0.2779 0.0905 -0.0184 0.0125 393 ALA A O 2727 C CB . ALA A 400 ? 0.3027 0.2580 0.2891 0.0836 -0.0150 0.0037 393 ALA A CB 2728 N N . VAL A 401 ? 0.3204 0.2852 0.2930 0.0836 -0.0221 0.0024 394 VAL A N 2729 C CA . VAL A 401 ? 0.3220 0.2872 0.2859 0.0875 -0.0286 0.0019 394 VAL A CA 2730 C C . VAL A 401 ? 0.3300 0.2915 0.2809 0.0858 -0.0241 0.0056 394 VAL A C 2731 O O . VAL A 401 ? 0.3128 0.2669 0.2488 0.0914 -0.0268 0.0087 394 VAL A O 2732 C CB . VAL A 401 ? 0.3212 0.2986 0.2984 0.0854 -0.0339 -0.0047 394 VAL A CB 2733 C CG1 . VAL A 401 ? 0.3159 0.2952 0.2857 0.0865 -0.0387 -0.0059 394 VAL A CG1 2734 C CG2 . VAL A 401 ? 0.2900 0.2689 0.2765 0.0904 -0.0406 -0.0075 394 VAL A CG2 2735 N N . VAL A 402 ? 0.3150 0.2815 0.2712 0.0786 -0.0175 0.0052 395 VAL A N 2736 C CA . VAL A 402 ? 0.3180 0.2815 0.2640 0.0769 -0.0127 0.0087 395 VAL A CA 2737 C C . VAL A 402 ? 0.3258 0.2766 0.2588 0.0812 -0.0085 0.0157 395 VAL A C 2738 O O . VAL A 402 ? 0.3309 0.2757 0.2496 0.0850 -0.0079 0.0192 395 VAL A O 2739 C CB . VAL A 402 ? 0.3005 0.2707 0.2552 0.0687 -0.0063 0.0075 395 VAL A CB 2740 C CG1 . VAL A 402 ? 0.3138 0.2807 0.2590 0.0676 -0.0011 0.0116 395 VAL A CG1 2741 C CG2 . VAL A 402 ? 0.3228 0.3043 0.2879 0.0648 -0.0099 0.0015 395 VAL A CG2 2742 N N . HIS A 403 ? 0.3269 0.2733 0.2649 0.0807 -0.0052 0.0177 396 HIS A N 2743 C CA . HIS A 403 ? 0.3377 0.2718 0.2660 0.0837 0.0000 0.0246 396 HIS A CA 2744 C C . HIS A 403 ? 0.3681 0.2932 0.2802 0.0929 -0.0053 0.0276 396 HIS A C 2745 O O . HIS A 403 ? 0.3927 0.3089 0.2900 0.0959 -0.0013 0.0333 396 HIS A O 2746 C CB . HIS A 403 ? 0.3318 0.2629 0.2699 0.0822 0.0022 0.0248 396 HIS A CB 2747 C CG . HIS A 403 ? 0.3590 0.2814 0.2951 0.0801 0.0108 0.0308 396 HIS A CG 2748 N ND1 . HIS A 403 ? 0.3376 0.2625 0.2761 0.0742 0.0177 0.0322 396 HIS A ND1 2749 C CD2 . HIS A 403 ? 0.3768 0.2882 0.3107 0.0828 0.0136 0.0354 396 HIS A CD2 2750 C CE1 . HIS A 403 ? 0.3641 0.2803 0.3027 0.0731 0.0245 0.0375 396 HIS A CE1 2751 N NE2 . HIS A 403 ? 0.4124 0.3200 0.3481 0.0781 0.0223 0.0395 396 HIS A NE2 2752 N N . GLU A 404 ? 0.3646 0.2918 0.2790 0.0974 -0.0144 0.0238 397 GLU A N 2753 C CA . GLU A 404 ? 0.3911 0.3098 0.2897 0.1068 -0.0214 0.0259 397 GLU A CA 2754 C C . GLU A 404 ? 0.3956 0.3150 0.2818 0.1087 -0.0239 0.0251 397 GLU A C 2755 O O . GLU A 404 ? 0.4164 0.3252 0.2834 0.1156 -0.0251 0.0293 397 GLU A O 2756 C CB . GLU A 404 ? 0.3969 0.3195 0.3044 0.1107 -0.0313 0.0210 397 GLU A CB 2757 C CG . GLU A 404 ? 0.4056 0.3198 0.2987 0.1211 -0.0411 0.0221 397 GLU A CG 2758 C CD . GLU A 404 ? 0.4643 0.3621 0.3401 0.1275 -0.0379 0.0302 397 GLU A CD 2759 O OE1 . GLU A 404 ? 0.4486 0.3413 0.3235 0.1236 -0.0275 0.0354 397 GLU A OE1 2760 O OE2 . GLU A 404 ? 0.4751 0.3646 0.3379 0.1365 -0.0459 0.0315 397 GLU A OE2 2761 N N . ILE A 405 ? 0.3763 0.3074 0.2725 0.1030 -0.0249 0.0197 398 ILE A N 2762 C CA . ILE A 405 ? 0.3824 0.3144 0.2683 0.1040 -0.0265 0.0186 398 ILE A CA 2763 C C . ILE A 405 ? 0.3835 0.3079 0.2561 0.1039 -0.0170 0.0249 398 ILE A C 2764 O O . ILE A 405 ? 0.3968 0.3135 0.2516 0.1098 -0.0183 0.0272 398 ILE A O 2765 C CB . ILE A 405 ? 0.3564 0.3023 0.2573 0.0972 -0.0283 0.0121 398 ILE A CB 2766 C CG1 . ILE A 405 ? 0.3422 0.2948 0.2540 0.0990 -0.0386 0.0059 398 ILE A CG1 2767 C CG2 . ILE A 405 ? 0.3376 0.2841 0.2290 0.0967 -0.0270 0.0118 398 ILE A CG2 2768 C CD1 . ILE A 405 ? 0.2890 0.2549 0.2186 0.0914 -0.0385 0.0004 398 ILE A CD1 2769 N N . VAL A 406 ? 0.3689 0.2952 0.2502 0.0974 -0.0077 0.0276 399 VAL A N 2770 C CA . VAL A 406 ? 0.3777 0.2968 0.2494 0.0970 0.0023 0.0341 399 VAL A CA 2771 C C . VAL A 406 ? 0.4012 0.3054 0.2550 0.1050 0.0035 0.0407 399 VAL A C 2772 O O . VAL A 406 ? 0.4264 0.3228 0.2629 0.1096 0.0069 0.0448 399 VAL A O 2773 C CB . VAL A 406 ? 0.3603 0.2834 0.2469 0.0888 0.0112 0.0357 399 VAL A CB 2774 C CG1 . VAL A 406 ? 0.3811 0.2967 0.2597 0.0886 0.0217 0.0427 399 VAL A CG1 2775 C CG2 . VAL A 406 ? 0.3356 0.2724 0.2367 0.0814 0.0103 0.0296 399 VAL A CG2 2776 N N . ARG A 407 ? 0.4119 0.3115 0.2689 0.1073 0.0009 0.0419 400 ARG A N 2777 C CA . ARG A 407 ? 0.4308 0.3151 0.2702 0.1154 0.0016 0.0486 400 ARG A CA 2778 C C . ARG A 407 ? 0.4712 0.3492 0.2898 0.1243 -0.0056 0.0484 400 ARG A C 2779 O O . ARG A 407 ? 0.4883 0.3537 0.2867 0.1301 -0.0009 0.0549 400 ARG A O 2780 C CB . ARG A 407 ? 0.4406 0.3212 0.2871 0.1175 -0.0021 0.0490 400 ARG A CB 2781 C CG . ARG A 407 ? 0.4388 0.3021 0.2688 0.1243 0.0018 0.0578 400 ARG A CG 2782 C CD . ARG A 407 ? 0.4636 0.3226 0.2985 0.1286 -0.0049 0.0573 400 ARG A CD 2783 N NE . ARG A 407 ? 0.4957 0.3593 0.3288 0.1341 -0.0182 0.0512 400 ARG A NE 2784 C CZ . ARG A 407 ? 0.5257 0.3810 0.3386 0.1432 -0.0250 0.0526 400 ARG A CZ 2785 N NH1 . ARG A 407 ? 0.4903 0.3511 0.3051 0.1474 -0.0376 0.0462 400 ARG A NH1 2786 N NH2 . ARG A 407 ? 0.5763 0.4172 0.3669 0.1484 -0.0192 0.0605 400 ARG A NH2 2787 N N . SER A 408 ? 0.4629 0.3487 0.2859 0.1258 -0.0167 0.0411 401 SER A N 2788 C CA . SER A 408 ? 0.4885 0.3683 0.2924 0.1343 -0.0252 0.0397 401 SER A CA 2789 C C . SER A 408 ? 0.4994 0.3776 0.2902 0.1344 -0.0200 0.0407 401 SER A C 2790 O O . SER A 408 ? 0.5204 0.3864 0.2881 0.1421 -0.0195 0.0448 401 SER A O 2791 C CB . SER A 408 ? 0.4872 0.3766 0.3018 0.1350 -0.0384 0.0311 401 SER A CB 2792 O OG A SER A 408 ? 0.4471 0.3300 0.2433 0.1435 -0.0476 0.0293 401 SER A OG 2793 O OG B SER A 408 ? 0.5240 0.4154 0.3516 0.1353 -0.0428 0.0299 401 SER A OG 2794 N N . PHE A 409 ? 0.4754 0.3655 0.2803 0.1263 -0.0162 0.0371 402 PHE A N 2795 C CA . PHE A 409 ? 0.4719 0.3610 0.2664 0.1260 -0.0102 0.0382 402 PHE A CA 2796 C C . PHE A 409 ? 0.4970 0.3747 0.2780 0.1282 0.0018 0.0472 402 PHE A C 2797 O O . PHE A 409 ? 0.5152 0.3846 0.2764 0.1338 0.0045 0.0499 402 PHE A O 2798 C CB . PHE A 409 ? 0.4503 0.3534 0.2633 0.1166 -0.0067 0.0339 402 PHE A CB 2799 C CG . PHE A 409 ? 0.4353 0.3478 0.2557 0.1154 -0.0168 0.0256 402 PHE A CG 2800 C CD1 . PHE A 409 ? 0.4548 0.3633 0.2599 0.1212 -0.0227 0.0229 402 PHE A CD1 2801 C CD2 . PHE A 409 ? 0.3963 0.3213 0.2388 0.1084 -0.0201 0.0205 402 PHE A CD2 2802 C CE1 . PHE A 409 ? 0.4412 0.3582 0.2545 0.1196 -0.0318 0.0153 402 PHE A CE1 2803 C CE2 . PHE A 409 ? 0.3940 0.3277 0.2445 0.1067 -0.0283 0.0134 402 PHE A CE2 2804 C CZ . PHE A 409 ? 0.4288 0.3582 0.2650 0.1123 -0.0345 0.0107 402 PHE A CZ 2805 N N . GLY A 410 ? 0.4917 0.3683 0.2830 0.1239 0.0093 0.0518 403 GLY A N 2806 C CA . GLY A 410 ? 0.5154 0.3810 0.2966 0.1253 0.0215 0.0608 403 GLY A CA 2807 C C . GLY A 410 ? 0.5630 0.4117 0.3182 0.1361 0.0200 0.0665 403 GLY A C 2808 O O . GLY A 410 ? 0.5815 0.4197 0.3195 0.1401 0.0289 0.0732 403 GLY A O 2809 N N . THR A 411 ? 0.5724 0.4181 0.3244 0.1414 0.0085 0.0640 404 THR A N 2810 C CA . THR A 411 ? 0.6103 0.4395 0.3367 0.1523 0.0054 0.0690 404 THR A CA 2811 C C . THR A 411 ? 0.6388 0.4625 0.3420 0.1591 0.0034 0.0680 404 THR A C 2812 O O . THR A 411 ? 0.6747 0.4837 0.3540 0.1660 0.0096 0.0750 404 THR A O 2813 C CB . THR A 411 ? 0.6201 0.4478 0.3485 0.1572 -0.0080 0.0657 404 THR A CB 2814 O OG1 A THR A 411 ? 0.5799 0.4121 0.3293 0.1512 -0.0052 0.0666 404 THR A OG1 2815 O OG1 B THR A 411 ? 0.6283 0.4632 0.3567 0.1599 -0.0215 0.0570 404 THR A OG1 2816 C CG2 A THR A 411 ? 0.6250 0.4348 0.3256 0.1692 -0.0120 0.0711 404 THR A CG2 2817 C CG2 B THR A 411 ? 0.5859 0.4213 0.3395 0.1502 -0.0070 0.0647 404 THR A CG2 2818 N N . LEU A 412 ? 0.6226 0.4573 0.3326 0.1571 -0.0047 0.0594 405 LEU A N 2819 C CA . LEU A 412 ? 0.6448 0.4752 0.3349 0.1629 -0.0075 0.0570 405 LEU A CA 2820 C C . LEU A 412 ? 0.6494 0.4770 0.3326 0.1608 0.0077 0.0625 405 LEU A C 2821 O O . LEU A 412 ? 0.6503 0.4656 0.3078 0.1686 0.0112 0.0661 405 LEU A O 2822 C CB . LEU A 412 ? 0.6397 0.4838 0.3432 0.1594 -0.0185 0.0464 405 LEU A CB 2823 C CG . LEU A 412 ? 0.6663 0.5106 0.3672 0.1652 -0.0358 0.0395 405 LEU A CG 2824 C CD1 . LEU A 412 ? 0.7032 0.5469 0.4135 0.1662 -0.0415 0.0406 405 LEU A CD1 2825 C CD2 . LEU A 412 ? 0.6527 0.5122 0.3724 0.1591 -0.0431 0.0300 405 LEU A CD2 2826 N N . LYS A 413 ? 0.6234 0.4621 0.3295 0.1506 0.0167 0.0630 406 LYS A N 2827 C CA . LYS A 413 ? 0.6321 0.4697 0.3360 0.1479 0.0315 0.0681 406 LYS A CA 2828 C C . LYS A 413 ? 0.6547 0.4758 0.3393 0.1537 0.0426 0.0787 406 LYS A C 2829 O O . LYS A 413 ? 0.6609 0.4746 0.3282 0.1580 0.0512 0.0827 406 LYS A O 2830 C CB . LYS A 413 ? 0.6138 0.4656 0.3467 0.1362 0.0384 0.0671 406 LYS A CB 2831 C CG . LYS A 413 ? 0.6667 0.5196 0.3991 0.1337 0.0516 0.0706 406 LYS A CG 2832 C CD . LYS A 413 ? 0.7250 0.5850 0.4803 0.1244 0.0615 0.0739 406 LYS A CD 2833 C CE . LYS A 413 ? 0.7769 0.6294 0.5248 0.1254 0.0772 0.0823 406 LYS A CE 2834 N NZ . LYS A 413 ? 0.7922 0.6493 0.5625 0.1169 0.0859 0.0861 406 LYS A NZ 2835 N N . LYS A 414 ? 0.6527 0.4679 0.3405 0.1539 0.0427 0.0833 407 LYS A N 2836 C CA . LYS A 414 ? 0.6926 0.4908 0.3621 0.1596 0.0528 0.0940 407 LYS A CA 2837 C C . LYS A 414 ? 0.7276 0.5097 0.3622 0.1721 0.0498 0.0967 407 LYS A C 2838 O O . LYS A 414 ? 0.7613 0.5299 0.3771 0.1769 0.0616 0.1055 407 LYS A O 2839 C CB . LYS A 414 ? 0.6891 0.4834 0.3688 0.1578 0.0523 0.0980 407 LYS A CB 2840 C CG . LYS A 414 ? 0.7024 0.5083 0.4123 0.1459 0.0603 0.0981 407 LYS A CG 2841 C CD . LYS A 414 ? 0.7291 0.5325 0.4512 0.1437 0.0578 0.0999 407 LYS A CD 2842 C CE . LYS A 414 ? 0.7339 0.5477 0.4845 0.1322 0.0656 0.0996 407 LYS A CE 2843 N NZ . LYS A 414 ? 0.7645 0.5748 0.5260 0.1306 0.0632 0.1011 407 LYS A NZ 2844 N N . GLU A 415 ? 0.7349 0.5182 0.3607 0.1775 0.0343 0.0890 408 GLU A N 2845 C CA . GLU A 415 ? 0.7801 0.5486 0.3718 0.1900 0.0289 0.0897 408 GLU A CA 2846 C C . GLU A 415 ? 0.7756 0.5451 0.3552 0.1918 0.0328 0.0866 408 GLU A C 2847 O O . GLU A 415 ? 0.7935 0.5513 0.3443 0.2021 0.0277 0.0858 408 GLU A O 2848 C CB . GLU A 415 ? 0.7939 0.5628 0.3823 0.1954 0.0094 0.0823 408 GLU A CB 2849 C CG . GLU A 415 ? 0.8545 0.6221 0.4540 0.1948 0.0040 0.0845 408 GLU A CG 2850 C CD . GLU A 415 ? 0.9587 0.7260 0.5540 0.2014 -0.0153 0.0774 408 GLU A CD 2851 O OE1 . GLU A 415 ? 0.9835 0.7636 0.5912 0.1985 -0.0258 0.0675 408 GLU A OE1 2852 O OE2 . GLU A 415 ? 1.0231 0.7773 0.6034 0.2094 -0.0200 0.0819 408 GLU A OE2 2853 N N . GLY A 416 ? 0.7287 0.5121 0.3300 0.1823 0.0409 0.0845 409 GLY A N 2854 C CA . GLY A 416 ? 0.7307 0.5159 0.3240 0.1832 0.0467 0.0823 409 GLY A CA 2855 C C . GLY A 416 ? 0.7115 0.5111 0.3186 0.1792 0.0358 0.0711 409 GLY A C 2856 O O . GLY A 416 ? 0.7119 0.5137 0.3140 0.1797 0.0396 0.0684 409 GLY A O 2857 N N . TRP A 417 ? 0.6768 0.4862 0.3022 0.1750 0.0227 0.0647 410 TRP A N 2858 C CA . TRP A 417 ? 0.6528 0.4753 0.2920 0.1710 0.0123 0.0543 410 TRP A CA 2859 C C . TRP A 417 ? 0.6147 0.4532 0.2829 0.1592 0.0201 0.0531 410 TRP A C 2860 O O . TRP A 417 ? 0.6201 0.4620 0.3036 0.1531 0.0283 0.0582 410 TRP A O 2861 C CB . TRP A 417 ? 0.6617 0.4880 0.3086 0.1718 -0.0044 0.0480 410 TRP A CB 2862 C CG . TRP A 417 ? 0.6407 0.4820 0.3075 0.1661 -0.0151 0.0377 410 TRP A CG 2863 C CD1 . TRP A 417 ? 0.6634 0.5043 0.3214 0.1704 -0.0263 0.0299 410 TRP A CD1 2864 C CD2 . TRP A 417 ? 0.6275 0.4851 0.3255 0.1552 -0.0154 0.0343 410 TRP A CD2 2865 N NE1 . TRP A 417 ? 0.6170 0.4730 0.2998 0.1626 -0.0331 0.0224 410 TRP A NE1 2866 C CE2 . TRP A 417 ? 0.6088 0.4752 0.3156 0.1534 -0.0264 0.0250 410 TRP A CE2 2867 C CE3 . TRP A 417 ? 0.6057 0.4706 0.3244 0.1470 -0.0075 0.0380 410 TRP A CE3 2868 C CZ2 . TRP A 417 ? 0.5591 0.4409 0.2937 0.1439 -0.0291 0.0201 410 TRP A CZ2 2869 C CZ3 . TRP A 417 ? 0.5438 0.4240 0.2891 0.1379 -0.0108 0.0326 410 TRP A CZ3 2870 C CH2 . TRP A 417 ? 0.5363 0.4247 0.2888 0.1365 -0.0211 0.0240 410 TRP A CH2 2871 N N . ARG A 418 ? 0.5799 0.4273 0.2549 0.1563 0.0174 0.0465 411 ARG A N 2872 C CA . ARG A 418 ? 0.5478 0.4119 0.2522 0.1452 0.0197 0.0432 411 ARG A CA 2873 C C . ARG A 418 ? 0.5216 0.3942 0.2338 0.1436 0.0068 0.0334 411 ARG A C 2874 O O . ARG A 418 ? 0.5340 0.4002 0.2286 0.1506 0.0000 0.0294 411 ARG A O 2875 C CB . ARG A 418 ? 0.5495 0.4167 0.2571 0.1420 0.0331 0.0460 411 ARG A CB 2876 C CG . ARG A 418 ? 0.5872 0.4482 0.2922 0.1417 0.0483 0.0557 411 ARG A CG 2877 C CD . ARG A 418 ? 0.5589 0.4266 0.2742 0.1370 0.0607 0.0574 411 ARG A CD 2878 N NE . ARG A 418 ? 0.5690 0.4337 0.2901 0.1343 0.0740 0.0661 411 ARG A NE 2879 C CZ . ARG A 418 ? 0.5718 0.4453 0.3174 0.1254 0.0765 0.0674 411 ARG A CZ 2880 N NH1 . ARG A 418 ? 0.4899 0.3764 0.2558 0.1184 0.0676 0.0606 411 ARG A NH1 2881 N NH2 . ARG A 418 ? 0.5587 0.4278 0.3083 0.1235 0.0883 0.0753 411 ARG A NH2 2882 N N . PRO A 419 ? 0.4760 0.3628 0.2145 0.1344 0.0039 0.0294 412 PRO A N 2883 C CA . PRO A 419 ? 0.4541 0.3493 0.2015 0.1321 -0.0062 0.0209 412 PRO A CA 2884 C C . PRO A 419 ? 0.4496 0.3461 0.1928 0.1321 -0.0014 0.0190 412 PRO A C 2885 O O . PRO A 419 ? 0.4497 0.3447 0.1905 0.1313 0.0108 0.0242 412 PRO A O 2886 C CB . PRO A 419 ? 0.4113 0.3206 0.1872 0.1219 -0.0068 0.0189 412 PRO A CB 2887 C CG . PRO A 419 ? 0.4221 0.3317 0.2046 0.1177 0.0059 0.0261 412 PRO A CG 2888 C CD . PRO A 419 ? 0.4432 0.3379 0.2031 0.1260 0.0107 0.0329 412 PRO A CD 2889 N N . ARG A 420 ? 0.4580 0.3568 0.2006 0.1332 -0.0111 0.0116 413 ARG A N 2890 C CA . ARG A 420 ? 0.4494 0.3495 0.1891 0.1332 -0.0076 0.0091 413 ARG A CA 2891 C C . ARG A 420 ? 0.4339 0.3463 0.1962 0.1237 0.0005 0.0103 413 ARG A C 2892 O O . ARG A 420 ? 0.4210 0.3332 0.1812 0.1236 0.0106 0.0132 413 ARG A O 2893 C CB . ARG A 420 ? 0.4517 0.3528 0.1906 0.1349 -0.0206 0.0004 413 ARG A CB 2894 C CG . ARG A 420 ? 0.4759 0.3788 0.2141 0.1345 -0.0181 -0.0031 413 ARG A CG 2895 C CD . ARG A 420 ? 0.4765 0.3818 0.2191 0.1343 -0.0316 -0.0120 413 ARG A CD 2896 N NE . ARG A 420 ? 0.5056 0.4127 0.2492 0.1334 -0.0290 -0.0152 413 ARG A NE 2897 C CZ . ARG A 420 ? 0.5409 0.4379 0.2636 0.1412 -0.0284 -0.0171 413 ARG A CZ 2898 N NH1 . ARG A 420 ? 0.4835 0.3678 0.1817 0.1504 -0.0306 -0.0160 413 ARG A NH1 2899 N NH2 . ARG A 420 ? 0.5328 0.4320 0.2585 0.1400 -0.0256 -0.0200 413 ARG A NH2 2900 N N . ARG A 421 ? 0.3913 0.3142 0.1750 0.1162 -0.0039 0.0080 414 ARG A N 2901 C CA . ARG A 421 ? 0.3722 0.3069 0.1778 0.1070 0.0020 0.0087 414 ARG A CA 2902 C C . ARG A 421 ? 0.3792 0.3163 0.1947 0.1028 0.0087 0.0142 414 ARG A C 2903 O O . ARG A 421 ? 0.3777 0.3093 0.1873 0.1057 0.0064 0.0164 414 ARG A O 2904 C CB . ARG A 421 ? 0.3527 0.2968 0.1745 0.1014 -0.0069 0.0022 414 ARG A CB 2905 C CG . ARG A 421 ? 0.3583 0.2997 0.1722 0.1053 -0.0158 -0.0042 414 ARG A CG 2906 C CD . ARG A 421 ? 0.3628 0.3140 0.1952 0.0988 -0.0228 -0.0100 414 ARG A CD 2907 N NE . ARG A 421 ? 0.3782 0.3249 0.2012 0.1030 -0.0293 -0.0153 414 ARG A NE 2908 C CZ . ARG A 421 ? 0.3908 0.3307 0.2027 0.1089 -0.0391 -0.0195 414 ARG A CZ 2909 N NH1 . ARG A 421 ? 0.3844 0.3232 0.1963 0.1105 -0.0445 -0.0192 414 ARG A NH1 2910 N NH2 . ARG A 421 ? 0.3816 0.3164 0.1837 0.1132 -0.0445 -0.0245 414 ARG A NH2 2911 N N . THR A 422 ? 0.3547 0.2994 0.1852 0.0961 0.0164 0.0164 415 THR A N 2912 C CA . THR A 422 ? 0.3505 0.2977 0.1922 0.0914 0.0223 0.0209 415 THR A CA 2913 C C . THR A 422 ? 0.3415 0.2947 0.1963 0.0870 0.0144 0.0175 415 THR A C 2914 O O . THR A 422 ? 0.3193 0.2800 0.1838 0.0834 0.0081 0.0122 415 THR A O 2915 C CB . THR A 422 ? 0.3376 0.2923 0.1935 0.0854 0.0308 0.0228 415 THR A CB 2916 O OG1 . THR A 422 ? 0.3448 0.2935 0.1898 0.0897 0.0400 0.0273 415 THR A OG1 2917 C CG2 . THR A 422 ? 0.3100 0.2691 0.1813 0.0791 0.0345 0.0256 415 THR A CG2 2918 N N . ILE A 423 ? 0.3335 0.2831 0.1885 0.0874 0.0154 0.0208 416 ILE A N 2919 C CA . ILE A 423 ? 0.3284 0.2839 0.1974 0.0829 0.0102 0.0181 416 ILE A CA 2920 C C . ILE A 423 ? 0.3275 0.2870 0.2102 0.0765 0.0177 0.0214 416 ILE A C 2921 O O . ILE A 423 ? 0.3373 0.2910 0.2159 0.0777 0.0257 0.0270 416 ILE A O 2922 C CB . ILE A 423 ? 0.3324 0.2812 0.1932 0.0883 0.0036 0.0181 416 ILE A CB 2923 C CG1 . ILE A 423 ? 0.3331 0.2769 0.1794 0.0952 -0.0047 0.0146 416 ILE A CG1 2924 C CG2 . ILE A 423 ? 0.3316 0.2876 0.2087 0.0836 -0.0014 0.0147 416 ILE A CG2 2925 C CD1 . ILE A 423 ? 0.3223 0.2578 0.1579 0.1021 -0.0113 0.0153 416 ILE A CD1 2926 N N . LEU A 424 ? 0.3068 0.2760 0.2056 0.0698 0.0154 0.0176 417 LEU A N 2927 C CA . LEU A 424 ? 0.2924 0.2658 0.2052 0.0636 0.0203 0.0191 417 LEU A CA 2928 C C . LEU A 424 ? 0.2898 0.2646 0.2094 0.0622 0.0153 0.0169 417 LEU A C 2929 O O . LEU A 424 ? 0.3024 0.2812 0.2246 0.0623 0.0080 0.0122 417 LEU A O 2930 C CB . LEU A 424 ? 0.2752 0.2579 0.2003 0.0573 0.0215 0.0166 417 LEU A CB 2931 C CG . LEU A 424 ? 0.2817 0.2646 0.2027 0.0584 0.0263 0.0183 417 LEU A CG 2932 C CD1 . LEU A 424 ? 0.2735 0.2657 0.2082 0.0521 0.0268 0.0158 417 LEU A CD1 2933 C CD2 . LEU A 424 ? 0.3057 0.2819 0.2209 0.0610 0.0357 0.0246 417 LEU A CD2 2934 N N . PHE A 425 ? 0.2791 0.2505 0.2024 0.0610 0.0196 0.0201 418 PHE A N 2935 C CA . PHE A 425 ? 0.2613 0.2333 0.1915 0.0599 0.0160 0.0182 418 PHE A CA 2936 C C . PHE A 425 ? 0.2595 0.2366 0.2039 0.0528 0.0199 0.0175 418 PHE A C 2937 O O . PHE A 425 ? 0.2760 0.2517 0.2233 0.0504 0.0267 0.0210 418 PHE A O 2938 C CB . PHE A 425 ? 0.2728 0.2346 0.1944 0.0652 0.0171 0.0225 418 PHE A CB 2939 C CG . PHE A 425 ? 0.2965 0.2514 0.2019 0.0730 0.0130 0.0236 418 PHE A CG 2940 C CD1 . PHE A 425 ? 0.3376 0.2934 0.2415 0.0765 0.0038 0.0195 418 PHE A CD1 2941 C CD2 . PHE A 425 ? 0.3500 0.2976 0.2416 0.0770 0.0182 0.0283 418 PHE A CD2 2942 C CE1 . PHE A 425 ? 0.3249 0.2736 0.2129 0.0843 -0.0012 0.0200 418 PHE A CE1 2943 C CE2 . PHE A 425 ? 0.3574 0.2976 0.2317 0.0849 0.0140 0.0290 418 PHE A CE2 2944 C CZ . PHE A 425 ? 0.3549 0.2951 0.2269 0.0887 0.0037 0.0248 418 PHE A CZ 2945 N N . ALA A 426 ? 0.2580 0.2412 0.2117 0.0496 0.0157 0.0128 419 ALA A N 2946 C CA . ALA A 426 ? 0.2458 0.2337 0.2117 0.0432 0.0182 0.0111 419 ALA A CA 2947 C C . ALA A 426 ? 0.2533 0.2408 0.2255 0.0424 0.0162 0.0088 419 ALA A C 2948 O O . ALA A 426 ? 0.2629 0.2524 0.2354 0.0444 0.0113 0.0057 419 ALA A O 2949 C CB . ALA A 426 ? 0.2259 0.2225 0.1973 0.0390 0.0163 0.0073 419 ALA A CB 2950 N N . SER A 427 ? 0.2574 0.2427 0.2359 0.0392 0.0203 0.0099 420 SER A N 2951 C CA . SER A 427 ? 0.2502 0.2354 0.2362 0.0373 0.0195 0.0071 420 SER A CA 2952 C C . SER A 427 ? 0.2493 0.2408 0.2440 0.0309 0.0203 0.0035 420 SER A C 2953 O O . SER A 427 ? 0.2474 0.2376 0.2465 0.0276 0.0240 0.0051 420 SER A O 2954 C CB . SER A 427 ? 0.2622 0.2384 0.2481 0.0385 0.0236 0.0112 420 SER A CB 2955 O OG . SER A 427 ? 0.2522 0.2274 0.2458 0.0366 0.0231 0.0082 420 SER A OG 2956 N N . TRP A 428 ? 0.2403 0.2385 0.2375 0.0293 0.0169 -0.0009 421 TRP A N 2957 C CA . TRP A 428 ? 0.2182 0.2220 0.2207 0.0240 0.0170 -0.0041 421 TRP A CA 2958 C C . TRP A 428 ? 0.2428 0.2449 0.2513 0.0213 0.0178 -0.0070 421 TRP A C 2959 O O . TRP A 428 ? 0.2194 0.2187 0.2288 0.0236 0.0172 -0.0083 421 TRP A O 2960 C CB . TRP A 428 ? 0.2111 0.2214 0.2128 0.0235 0.0136 -0.0075 421 TRP A CB 2961 C CG . TRP A 428 ? 0.2228 0.2349 0.2191 0.0260 0.0118 -0.0058 421 TRP A CG 2962 C CD1 . TRP A 428 ? 0.1931 0.2070 0.1872 0.0287 0.0083 -0.0072 421 TRP A CD1 2963 C CD2 . TRP A 428 ? 0.1980 0.2102 0.1909 0.0258 0.0133 -0.0030 421 TRP A CD2 2964 N NE1 . TRP A 428 ? 0.2106 0.2251 0.1993 0.0304 0.0071 -0.0056 421 TRP A NE1 2965 C CE2 . TRP A 428 ? 0.1933 0.2068 0.1809 0.0288 0.0104 -0.0030 421 TRP A CE2 2966 C CE3 . TRP A 428 ? 0.2404 0.2523 0.2357 0.0234 0.0167 -0.0009 421 TRP A CE3 2967 C CZ2 . TRP A 428 ? 0.1893 0.2029 0.1722 0.0299 0.0111 -0.0010 421 TRP A CZ2 2968 C CZ3 . TRP A 428 ? 0.2304 0.2430 0.2220 0.0246 0.0179 0.0015 421 TRP A CZ3 2969 C CH2 . TRP A 428 ? 0.2171 0.2302 0.2018 0.0280 0.0152 0.0014 421 TRP A CH2 2970 N N . ASP A 429 ? 0.2314 0.2351 0.2442 0.0168 0.0187 -0.0085 422 ASP A N 2971 C CA . ASP A 429 ? 0.2349 0.2370 0.2527 0.0142 0.0188 -0.0123 422 ASP A CA 2972 C C . ASP A 429 ? 0.2271 0.2348 0.2440 0.0119 0.0164 -0.0169 422 ASP A C 2973 O O . ASP A 429 ? 0.2391 0.2517 0.2533 0.0113 0.0151 -0.0165 422 ASP A O 2974 C CB . ASP A 429 ? 0.2456 0.2449 0.2691 0.0108 0.0207 -0.0112 422 ASP A CB 2975 C CG . ASP A 429 ? 0.2347 0.2290 0.2633 0.0091 0.0210 -0.0144 422 ASP A CG 2976 O OD1 . ASP A 429 ? 0.2777 0.2713 0.3047 0.0104 0.0198 -0.0180 422 ASP A OD1 2977 O OD2 . ASP A 429 ? 0.2450 0.2357 0.2797 0.0067 0.0227 -0.0132 422 ASP A OD2 2978 N N . ALA A 430 ? 0.2246 0.2307 0.2434 0.0107 0.0162 -0.0211 423 ALA A N 2979 C CA . ALA A 430 ? 0.2292 0.2388 0.2460 0.0086 0.0148 -0.0256 423 ALA A CA 2980 C C . ALA A 430 ? 0.2055 0.2203 0.2186 0.0100 0.0142 -0.0258 423 ALA A C 2981 O O . ALA A 430 ? 0.2254 0.2435 0.2356 0.0081 0.0134 -0.0277 423 ALA A O 2982 C CB . ALA A 430 ? 0.2111 0.2221 0.2286 0.0047 0.0133 -0.0267 423 ALA A CB 2983 N N . GLU A 431 ? 0.2334 0.2488 0.2468 0.0134 0.0143 -0.0239 424 GLU A N 2984 C CA . GLU A 431 ? 0.2122 0.2325 0.2242 0.0143 0.0136 -0.0248 424 GLU A CA 2985 C C . GLU A 431 ? 0.2216 0.2429 0.2341 0.0134 0.0151 -0.0291 424 GLU A C 2986 O O . GLU A 431 ? 0.2373 0.2625 0.2476 0.0119 0.0154 -0.0303 424 GLU A O 2987 C CB . GLU A 431 ? 0.2231 0.2434 0.2364 0.0184 0.0126 -0.0227 424 GLU A CB 2988 C CG . GLU A 431 ? 0.1931 0.2188 0.2073 0.0192 0.0112 -0.0236 424 GLU A CG 2989 C CD . GLU A 431 ? 0.2110 0.2393 0.2299 0.0198 0.0126 -0.0270 424 GLU A CD 2990 O OE1 . GLU A 431 ? 0.2370 0.2626 0.2582 0.0206 0.0144 -0.0291 424 GLU A OE1 2991 O OE2 . GLU A 431 ? 0.2082 0.2414 0.2292 0.0195 0.0122 -0.0277 424 GLU A OE2 2992 N N . GLU A 432 ? 0.2196 0.2369 0.2342 0.0142 0.0164 -0.0314 425 GLU A N 2993 C CA . GLU A 432 ? 0.2283 0.2461 0.2428 0.0141 0.0186 -0.0357 425 GLU A CA 2994 C C . GLU A 432 ? 0.2284 0.2463 0.2371 0.0109 0.0188 -0.0381 425 GLU A C 2995 O O . GLU A 432 ? 0.2430 0.2621 0.2492 0.0108 0.0211 -0.0410 425 GLU A O 2996 C CB . GLU A 432 ? 0.2305 0.2434 0.2485 0.0163 0.0200 -0.0381 425 GLU A CB 2997 C CG . GLU A 432 ? 0.2236 0.2361 0.2469 0.0204 0.0194 -0.0359 425 GLU A CG 2998 C CD . GLU A 432 ? 0.2229 0.2413 0.2502 0.0227 0.0199 -0.0367 425 GLU A CD 2999 O OE1 . GLU A 432 ? 0.2376 0.2607 0.2637 0.0208 0.0214 -0.0381 425 GLU A OE1 3000 O OE2 . GLU A 432 ? 0.2094 0.2276 0.2415 0.0265 0.0187 -0.0357 425 GLU A OE2 3001 N N . PHE A 433 ? 0.2349 0.2516 0.2417 0.0084 0.0166 -0.0369 426 PHE A N 3002 C CA . PHE A 433 ? 0.2341 0.2504 0.2351 0.0057 0.0155 -0.0392 426 PHE A CA 3003 C C . PHE A 433 ? 0.2284 0.2489 0.2258 0.0044 0.0141 -0.0369 426 PHE A C 3004 O O . PHE A 433 ? 0.2254 0.2455 0.2178 0.0023 0.0122 -0.0380 426 PHE A O 3005 C CB . PHE A 433 ? 0.2450 0.2571 0.2476 0.0037 0.0132 -0.0403 426 PHE A CB 3006 C CG . PHE A 433 ? 0.2447 0.2512 0.2495 0.0045 0.0143 -0.0438 426 PHE A CG 3007 C CD1 . PHE A 433 ? 0.2356 0.2385 0.2356 0.0035 0.0135 -0.0490 426 PHE A CD1 3008 C CD2 . PHE A 433 ? 0.2333 0.2374 0.2443 0.0067 0.0157 -0.0420 426 PHE A CD2 3009 C CE1 . PHE A 433 ? 0.2410 0.2378 0.2430 0.0043 0.0143 -0.0530 426 PHE A CE1 3010 C CE2 . PHE A 433 ? 0.2435 0.2415 0.2570 0.0076 0.0167 -0.0453 426 PHE A CE2 3011 C CZ . PHE A 433 ? 0.2581 0.2525 0.2675 0.0063 0.0160 -0.0511 426 PHE A CZ 3012 N N . GLY A 434 ? 0.2189 0.2432 0.2186 0.0058 0.0146 -0.0338 427 GLY A N 3013 C CA . GLY A 434 ? 0.2173 0.2451 0.2136 0.0046 0.0136 -0.0319 427 GLY A CA 3014 C C . GLY A 434 ? 0.2216 0.2516 0.2206 0.0053 0.0118 -0.0280 427 GLY A C 3015 O O . GLY A 434 ? 0.2140 0.2456 0.2105 0.0040 0.0100 -0.0263 427 GLY A O 3016 N N . LEU A 435 ? 0.1968 0.2262 0.2000 0.0076 0.0120 -0.0266 428 LEU A N 3017 C CA . LEU A 435 ? 0.1928 0.2232 0.1968 0.0091 0.0105 -0.0230 428 LEU A CA 3018 C C . LEU A 435 ? 0.1895 0.2187 0.1930 0.0074 0.0097 -0.0214 428 LEU A C 3019 O O . LEU A 435 ? 0.1879 0.2188 0.1905 0.0076 0.0086 -0.0190 428 LEU A O 3020 C CB . LEU A 435 ? 0.1920 0.2261 0.1947 0.0092 0.0095 -0.0222 428 LEU A CB 3021 C CG . LEU A 435 ? 0.1939 0.2303 0.1985 0.0094 0.0109 -0.0242 428 LEU A CG 3022 C CD1 . LEU A 435 ? 0.1885 0.2281 0.1930 0.0088 0.0099 -0.0232 428 LEU A CD1 3023 C CD2 . LEU A 435 ? 0.1830 0.2190 0.1927 0.0124 0.0114 -0.0251 428 LEU A CD2 3024 N N . LEU A 436 ? 0.1915 0.2179 0.1969 0.0059 0.0101 -0.0228 429 LEU A N 3025 C CA . LEU A 436 ? 0.2040 0.2304 0.2108 0.0037 0.0089 -0.0221 429 LEU A CA 3026 C C . LEU A 436 ? 0.2076 0.2333 0.2176 0.0049 0.0100 -0.0182 429 LEU A C 3027 O O . LEU A 436 ? 0.2126 0.2405 0.2238 0.0041 0.0094 -0.0165 429 LEU A O 3028 C CB . LEU A 436 ? 0.2118 0.2353 0.2206 0.0014 0.0083 -0.0254 429 LEU A CB 3029 C CG . LEU A 436 ? 0.2180 0.2412 0.2217 0.0008 0.0078 -0.0295 429 LEU A CG 3030 C CD1 . LEU A 436 ? 0.2223 0.2416 0.2274 -0.0010 0.0065 -0.0331 429 LEU A CD1 3031 C CD2 . LEU A 436 ? 0.2128 0.2390 0.2107 0.0000 0.0061 -0.0295 429 LEU A CD2 3032 N N . GLY A 437 ? 0.2151 0.2373 0.2265 0.0071 0.0120 -0.0168 430 GLY A N 3033 C CA . GLY A 437 ? 0.2097 0.2299 0.2226 0.0087 0.0140 -0.0126 430 GLY A CA 3034 C C . GLY A 437 ? 0.2166 0.2391 0.2253 0.0111 0.0137 -0.0099 430 GLY A C 3035 O O . GLY A 437 ? 0.2119 0.2350 0.2215 0.0110 0.0149 -0.0073 430 GLY A O 3036 N N . SER A 438 ? 0.2039 0.2275 0.2085 0.0134 0.0121 -0.0107 431 SER A N 3037 C CA . SER A 438 ? 0.2064 0.2315 0.2067 0.0158 0.0109 -0.0089 431 SER A CA 3038 C C . SER A 438 ? 0.2096 0.2387 0.2102 0.0134 0.0098 -0.0094 431 SER A C 3039 O O . SER A 438 ? 0.2029 0.2325 0.2020 0.0146 0.0102 -0.0072 431 SER A O 3040 C CB . SER A 438 ? 0.2101 0.2362 0.2085 0.0179 0.0086 -0.0106 431 SER A CB 3041 O OG . SER A 438 ? 0.2114 0.2407 0.2120 0.0153 0.0078 -0.0138 431 SER A OG 3042 N N . THR A 439 ? 0.1968 0.2282 0.1987 0.0104 0.0085 -0.0122 432 THR A N 3043 C CA . THR A 439 ? 0.2022 0.2368 0.2034 0.0085 0.0068 -0.0126 432 THR A CA 3044 C C . THR A 439 ? 0.1843 0.2195 0.1892 0.0072 0.0073 -0.0112 432 THR A C 3045 O O . THR A 439 ? 0.2083 0.2455 0.2129 0.0078 0.0067 -0.0097 432 THR A O 3046 C CB . THR A 439 ? 0.2073 0.2430 0.2070 0.0060 0.0054 -0.0155 432 THR A CB 3047 O OG1 . THR A 439 ? 0.2253 0.2611 0.2237 0.0073 0.0058 -0.0165 432 THR A OG1 3048 C CG2 . THR A 439 ? 0.1955 0.2336 0.1930 0.0049 0.0034 -0.0151 432 THR A CG2 3049 N N . GLU A 440 ? 0.1786 0.2123 0.1883 0.0055 0.0084 -0.0117 433 GLU A N 3050 C CA . GLU A 440 ? 0.1906 0.2257 0.2066 0.0041 0.0090 -0.0104 433 GLU A CA 3051 C C . GLU A 440 ? 0.1933 0.2279 0.2098 0.0067 0.0122 -0.0065 433 GLU A C 3052 O O . GLU A 440 ? 0.2031 0.2405 0.2231 0.0065 0.0126 -0.0051 433 GLU A O 3053 C CB . GLU A 440 ? 0.1922 0.2251 0.2147 0.0015 0.0096 -0.0118 433 GLU A CB 3054 C CG . GLU A 440 ? 0.2117 0.2445 0.2327 -0.0009 0.0060 -0.0165 433 GLU A CG 3055 C CD . GLU A 440 ? 0.1774 0.2138 0.1967 -0.0020 0.0022 -0.0177 433 GLU A CD 3056 O OE1 . GLU A 440 ? 0.2010 0.2401 0.2265 -0.0029 0.0012 -0.0166 433 GLU A OE1 3057 O OE2 . GLU A 440 ? 0.2120 0.2485 0.2239 -0.0018 0.0005 -0.0193 433 GLU A OE2 3058 N N . TRP A 441 ? 0.1893 0.2200 0.2024 0.0094 0.0147 -0.0046 434 TRP A N 3059 C CA . TRP A 441 ? 0.2074 0.2363 0.2185 0.0126 0.0183 -0.0007 434 TRP A CA 3060 C C . TRP A 441 ? 0.2085 0.2397 0.2142 0.0148 0.0166 -0.0005 434 TRP A C 3061 O O . TRP A 441 ? 0.2057 0.2378 0.2122 0.0161 0.0188 0.0015 434 TRP A O 3062 C CB . TRP A 441 ? 0.2141 0.2375 0.2200 0.0158 0.0202 0.0009 434 TRP A CB 3063 C CG . TRP A 441 ? 0.2313 0.2512 0.2328 0.0196 0.0244 0.0054 434 TRP A CG 3064 C CD1 . TRP A 441 ? 0.2133 0.2305 0.2186 0.0196 0.0299 0.0090 434 TRP A CD1 3065 C CD2 . TRP A 441 ? 0.2535 0.2717 0.2455 0.0241 0.0235 0.0063 434 TRP A CD2 3066 N NE1 . TRP A 441 ? 0.2251 0.2387 0.2222 0.0243 0.0331 0.0126 434 TRP A NE1 3067 C CE2 . TRP A 441 ? 0.2706 0.2845 0.2588 0.0273 0.0288 0.0107 434 TRP A CE2 3068 C CE3 . TRP A 441 ? 0.2263 0.2460 0.2127 0.0258 0.0188 0.0037 434 TRP A CE3 3069 C CZ2 . TRP A 441 ? 0.2492 0.2597 0.2265 0.0326 0.0291 0.0123 434 TRP A CZ2 3070 C CZ3 . TRP A 441 ? 0.2514 0.2678 0.2282 0.0308 0.0185 0.0050 434 TRP A CZ3 3071 C CH2 . TRP A 441 ? 0.2633 0.2751 0.2349 0.0343 0.0234 0.0091 434 TRP A CH2 3072 N N . ALA A 442 ? 0.2058 0.2380 0.2070 0.0151 0.0130 -0.0029 435 ALA A N 3073 C CA . ALA A 442 ? 0.2020 0.2357 0.1989 0.0169 0.0110 -0.0030 435 ALA A CA 3074 C C . ALA A 442 ? 0.1968 0.2345 0.1979 0.0147 0.0099 -0.0034 435 ALA A C 3075 O O . ALA A 442 ? 0.1889 0.2273 0.1884 0.0166 0.0100 -0.0024 435 ALA A O 3076 C CB . ALA A 442 ? 0.2013 0.2349 0.1943 0.0173 0.0077 -0.0053 435 ALA A CB 3077 N N . GLU A 443 ? 0.1911 0.2308 0.1971 0.0111 0.0085 -0.0051 436 GLU A N 3078 C CA . GLU A 443 ? 0.2029 0.2462 0.2134 0.0094 0.0067 -0.0055 436 GLU A CA 3079 C C . GLU A 443 ? 0.2096 0.2542 0.2266 0.0102 0.0100 -0.0031 436 GLU A C 3080 O O . GLU A 443 ? 0.2052 0.2525 0.2247 0.0111 0.0096 -0.0024 436 GLU A O 3081 C CB . GLU A 443 ? 0.2016 0.2461 0.2151 0.0058 0.0037 -0.0081 436 GLU A CB 3082 C CG . GLU A 443 ? 0.2151 0.2586 0.2216 0.0051 0.0011 -0.0102 436 GLU A CG 3083 C CD . GLU A 443 ? 0.1928 0.2363 0.1992 0.0023 -0.0015 -0.0128 436 GLU A CD 3084 O OE1 . GLU A 443 ? 0.2396 0.2829 0.2407 0.0018 -0.0038 -0.0137 436 GLU A OE1 3085 O OE2 . GLU A 443 ? 0.2158 0.2588 0.2269 0.0007 -0.0013 -0.0141 436 GLU A OE2 3086 N N . GLU A 444 ? 0.2038 0.2464 0.2243 0.0100 0.0137 -0.0017 437 GLU A N 3087 C CA . GLU A 444 ? 0.2056 0.2493 0.2333 0.0106 0.0182 0.0010 437 GLU A CA 3088 C C . GLU A 444 ? 0.1994 0.2418 0.2210 0.0151 0.0213 0.0036 437 GLU A C 3089 O O . GLU A 444 ? 0.2067 0.2517 0.2330 0.0162 0.0236 0.0050 437 GLU A O 3090 C CB . GLU A 444 ? 0.1974 0.2377 0.2288 0.0097 0.0221 0.0025 437 GLU A CB 3091 C CG . GLU A 444 ? 0.2805 0.3218 0.3217 0.0096 0.0279 0.0059 437 GLU A CG 3092 C CD . GLU A 444 ? 0.3729 0.4118 0.4218 0.0066 0.0300 0.0062 437 GLU A CD 3093 O OE1 . GLU A 444 ? 0.4623 0.5042 0.5223 0.0026 0.0276 0.0039 437 GLU A OE1 3094 O OE2 . GLU A 444 ? 0.3638 0.3970 0.4067 0.0083 0.0328 0.0080 437 GLU A OE2 3095 N N . ASN A 445 ? 0.1942 0.2323 0.2052 0.0180 0.0210 0.0038 438 ASN A N 3096 C CA . ASN A 445 ? 0.2114 0.2464 0.2143 0.0229 0.0238 0.0059 438 ASN A CA 3097 C C . ASN A 445 ? 0.2013 0.2367 0.1974 0.0248 0.0196 0.0038 438 ASN A C 3098 O O . ASN A 445 ? 0.2018 0.2335 0.1892 0.0291 0.0202 0.0044 438 ASN A O 3099 C CB . ASN A 445 ? 0.2175 0.2464 0.2131 0.0256 0.0264 0.0078 438 ASN A CB 3100 C CG . ASN A 445 ? 0.2184 0.2458 0.2204 0.0244 0.0321 0.0109 438 ASN A CG 3101 O OD1 . ASN A 445 ? 0.2401 0.2671 0.2437 0.0262 0.0376 0.0139 438 ASN A OD1 3102 N ND2 . ASN A 445 ? 0.2303 0.2568 0.2368 0.0214 0.0312 0.0101 438 ASN A ND2 3103 N N . SER A 446 ? 0.1914 0.2306 0.1915 0.0219 0.0152 0.0015 439 SER A N 3104 C CA . SER A 446 ? 0.2162 0.2549 0.2106 0.0229 0.0110 -0.0004 439 SER A CA 3105 C C . SER A 446 ? 0.2070 0.2443 0.1970 0.0270 0.0120 0.0002 439 SER A C 3106 O O . SER A 446 ? 0.2244 0.2590 0.2074 0.0292 0.0093 -0.0011 439 SER A O 3107 C CB . SER A 446 ? 0.2118 0.2540 0.2103 0.0193 0.0069 -0.0023 439 SER A CB 3108 O OG . SER A 446 ? 0.2218 0.2674 0.2270 0.0187 0.0074 -0.0015 439 SER A OG 3109 N N . ARG A 447 ? 0.2141 0.2535 0.2090 0.0280 0.0155 0.0019 440 ARG A N 3110 C CA . ARG A 447 ? 0.2116 0.2494 0.2021 0.0324 0.0171 0.0023 440 ARG A CA 3111 C C . ARG A 447 ? 0.2419 0.2737 0.2216 0.0371 0.0200 0.0033 440 ARG A C 3112 O O . ARG A 447 ? 0.2405 0.2687 0.2118 0.0409 0.0184 0.0020 440 ARG A O 3113 C CB . ARG A 447 ? 0.2057 0.2476 0.2055 0.0325 0.0210 0.0040 440 ARG A CB 3114 C CG . ARG A 447 ? 0.2362 0.2836 0.2454 0.0287 0.0165 0.0025 440 ARG A CG 3115 C CD . ARG A 447 ? 0.2820 0.3347 0.3045 0.0267 0.0190 0.0038 440 ARG A CD 3116 N NE . ARG A 447 ? 0.2409 0.2976 0.2697 0.0238 0.0132 0.0020 440 ARG A NE 3117 C CZ . ARG A 447 ? 0.2691 0.3264 0.2987 0.0199 0.0087 0.0004 440 ARG A CZ 3118 N NH1 . ARG A 447 ? 0.2689 0.3237 0.2949 0.0180 0.0094 0.0001 440 ARG A NH1 3119 N NH2 . ARG A 447 ? 0.1900 0.2499 0.2231 0.0185 0.0035 -0.0008 440 ARG A NH2 3120 N N . LEU A 448 ? 0.2342 0.2642 0.2135 0.0372 0.0241 0.0057 441 LEU A N 3121 C CA . LEU A 448 ? 0.2419 0.2650 0.2092 0.0420 0.0264 0.0070 441 LEU A CA 3122 C C . LEU A 448 ? 0.2579 0.2779 0.2174 0.0429 0.0199 0.0041 441 LEU A C 3123 O O . LEU A 448 ? 0.2480 0.2633 0.1972 0.0474 0.0181 0.0030 441 LEU A O 3124 C CB . LEU A 448 ? 0.2429 0.2642 0.2123 0.0413 0.0317 0.0104 441 LEU A CB 3125 C CG . LEU A 448 ? 0.2394 0.2643 0.2200 0.0393 0.0384 0.0134 441 LEU A CG 3126 C CD1 . LEU A 448 ? 0.2491 0.2698 0.2295 0.0394 0.0442 0.0173 441 LEU A CD1 3127 C CD2 . LEU A 448 ? 0.2842 0.3098 0.2643 0.0428 0.0430 0.0146 441 LEU A CD2 3128 N N . LEU A 449 ? 0.2407 0.2637 0.2061 0.0385 0.0162 0.0026 442 LEU A N 3129 C CA . LEU A 449 ? 0.2458 0.2669 0.2069 0.0388 0.0106 0.0000 442 LEU A CA 3130 C C . LEU A 449 ? 0.2464 0.2677 0.2053 0.0396 0.0059 -0.0029 442 LEU A C 3131 O O . LEU A 449 ? 0.2790 0.2969 0.2316 0.0423 0.0020 -0.0049 442 LEU A O 3132 C CB . LEU A 449 ? 0.2433 0.2679 0.2121 0.0339 0.0089 -0.0009 442 LEU A CB 3133 C CG . LEU A 449 ? 0.2722 0.2955 0.2429 0.0332 0.0125 0.0012 442 LEU A CG 3134 C CD1 . LEU A 449 ? 0.2278 0.2549 0.2069 0.0279 0.0110 -0.0004 442 LEU A CD1 3135 C CD2 . LEU A 449 ? 0.2956 0.3131 0.2579 0.0374 0.0120 0.0019 442 LEU A CD2 3136 N N A GLN A 450 ? 0.2437 0.2689 0.2088 0.0370 0.0058 -0.0032 443 GLN A N 3137 N N B GLN A 450 ? 0.2403 0.2652 0.2049 0.0373 0.0057 -0.0033 443 GLN A N 3138 C CA A GLN A 450 ? 0.2563 0.2815 0.2209 0.0374 0.0022 -0.0054 443 GLN A CA 3139 C CA B GLN A 450 ? 0.2482 0.2726 0.2115 0.0376 0.0012 -0.0059 443 GLN A CA 3140 C C A GLN A 450 ? 0.2488 0.2686 0.2036 0.0431 0.0017 -0.0064 443 GLN A C 3141 C C B GLN A 450 ? 0.2433 0.2630 0.1981 0.0431 0.0015 -0.0065 443 GLN A C 3142 O O A GLN A 450 ? 0.2395 0.2563 0.1901 0.0444 -0.0031 -0.0092 443 GLN A O 3143 O O B GLN A 450 ? 0.2295 0.2468 0.1812 0.0444 -0.0029 -0.0093 443 GLN A O 3144 C CB A GLN A 450 ? 0.2400 0.2690 0.2111 0.0358 0.0044 -0.0041 443 GLN A CB 3145 C CB B GLN A 450 ? 0.2308 0.2595 0.2016 0.0340 0.0007 -0.0058 443 GLN A CB 3146 C CG A GLN A 450 ? 0.2724 0.3026 0.2462 0.0343 0.0008 -0.0056 443 GLN A CG 3147 C CG B GLN A 450 ? 0.2807 0.3079 0.2496 0.0366 0.0000 -0.0066 443 GLN A CG 3148 C CD A GLN A 450 ? 0.2635 0.2983 0.2451 0.0297 0.0002 -0.0049 443 GLN A CD 3149 C CD B GLN A 450 ? 0.2741 0.3015 0.2452 0.0340 -0.0048 -0.0085 443 GLN A CD 3150 O OE1 A GLN A 450 ? 0.2419 0.2796 0.2287 0.0295 0.0017 -0.0038 443 GLN A OE1 3151 O OE1 B GLN A 450 ? 0.2383 0.2624 0.2063 0.0360 -0.0077 -0.0103 443 GLN A OE1 3152 N NE2 A GLN A 450 ? 0.2278 0.2633 0.2105 0.0262 -0.0020 -0.0058 443 GLN A NE2 3153 N NE2 B GLN A 450 ? 0.2777 0.3082 0.2538 0.0294 -0.0056 -0.0081 443 GLN A NE2 3154 N N . GLU A 451 ? 0.2470 0.2652 0.1984 0.0464 0.0070 -0.0041 444 GLU A N 3155 C CA . GLU A 451 ? 0.2481 0.2612 0.1898 0.0522 0.0077 -0.0050 444 GLU A CA 3156 C C . GLU A 451 ? 0.2454 0.2520 0.1750 0.0570 0.0080 -0.0046 444 GLU A C 3157 O O . GLU A 451 ? 0.2627 0.2636 0.1817 0.0622 0.0067 -0.0064 444 GLU A O 3158 C CB . GLU A 451 ? 0.2541 0.2688 0.1984 0.0540 0.0139 -0.0027 444 GLU A CB 3159 C CG . GLU A 451 ? 0.2651 0.2864 0.2220 0.0496 0.0133 -0.0027 444 GLU A CG 3160 C CD . GLU A 451 ? 0.3304 0.3514 0.2881 0.0483 0.0067 -0.0059 444 GLU A CD 3161 O OE1 . GLU A 451 ? 0.2781 0.2942 0.2282 0.0503 0.0025 -0.0085 444 GLU A OE1 3162 O OE2 . GLU A 451 ? 0.3036 0.3287 0.2697 0.0451 0.0054 -0.0057 444 GLU A OE2 3163 N N . ARG A 452 ? 0.2300 0.2369 0.1607 0.0555 0.0095 -0.0026 445 ARG A N 3164 C CA . ARG A 452 ? 0.2499 0.2499 0.1683 0.0606 0.0101 -0.0015 445 ARG A CA 3165 C C . ARG A 452 ? 0.2617 0.2607 0.1795 0.0598 0.0045 -0.0030 445 ARG A C 3166 O O . ARG A 452 ? 0.2900 0.2829 0.1972 0.0645 0.0037 -0.0025 445 ARG A O 3167 C CB . ARG A 452 ? 0.2454 0.2443 0.1630 0.0616 0.0188 0.0034 445 ARG A CB 3168 C CG . ARG A 452 ? 0.2569 0.2574 0.1769 0.0628 0.0256 0.0053 445 ARG A CG 3169 C CD . ARG A 452 ? 0.2704 0.2708 0.1933 0.0626 0.0348 0.0105 445 ARG A CD 3170 N NE . ARG A 452 ? 0.2724 0.2768 0.2025 0.0626 0.0411 0.0120 445 ARG A NE 3171 C CZ . ARG A 452 ? 0.2616 0.2685 0.2000 0.0610 0.0490 0.0160 445 ARG A CZ 3172 N NH1 . ARG A 452 ? 0.2701 0.2750 0.2096 0.0593 0.0516 0.0190 445 ARG A NH1 3173 N NH2 . ARG A 452 ? 0.2591 0.2704 0.2060 0.0611 0.0543 0.0169 445 ARG A NH2 3174 N N . GLY A 453 ? 0.2594 0.2640 0.1882 0.0544 0.0009 -0.0049 446 GLY A N 3175 C CA . GLY A 453 ? 0.2627 0.2678 0.1942 0.0530 -0.0028 -0.0059 446 GLY A CA 3176 C C . GLY A 453 ? 0.2776 0.2799 0.2046 0.0557 -0.0105 -0.0100 446 GLY A C 3177 O O . GLY A 453 ? 0.2822 0.2872 0.2145 0.0534 -0.0145 -0.0131 446 GLY A O 3178 N N . VAL A 454 ? 0.2659 0.2626 0.1835 0.0607 -0.0129 -0.0100 447 VAL A N 3179 C CA . VAL A 454 ? 0.2712 0.2653 0.1856 0.0636 -0.0213 -0.0144 447 VAL A CA 3180 C C . VAL A 454 ? 0.2766 0.2760 0.2032 0.0595 -0.0257 -0.0166 447 VAL A C 3181 O O . VAL A 454 ? 0.2655 0.2677 0.1991 0.0574 -0.0309 -0.0204 447 VAL A O 3182 C CB . VAL A 454 ? 0.3029 0.2882 0.2013 0.0713 -0.0232 -0.0138 447 VAL A CB 3183 C CG1 . VAL A 454 ? 0.2912 0.2744 0.1882 0.0741 -0.0332 -0.0186 447 VAL A CG1 3184 C CG2 . VAL A 454 ? 0.3260 0.3057 0.2115 0.0759 -0.0192 -0.0127 447 VAL A CG2 3185 N N . ALA A 455 ? 0.2695 0.2701 0.1992 0.0585 -0.0232 -0.0142 448 ALA A N 3186 C CA . ALA A 455 ? 0.2504 0.2555 0.1908 0.0558 -0.0267 -0.0162 448 ALA A CA 3187 C C . ALA A 455 ? 0.2544 0.2610 0.1988 0.0536 -0.0213 -0.0129 448 ALA A C 3188 O O . ALA A 455 ? 0.2664 0.2688 0.2034 0.0557 -0.0164 -0.0091 448 ALA A O 3189 C CB . ALA A 455 ? 0.2522 0.2535 0.1884 0.0610 -0.0346 -0.0191 448 ALA A CB 3190 N N . TYR A 456 ? 0.2422 0.2545 0.1986 0.0493 -0.0220 -0.0145 449 TYR A N 3191 C CA . TYR A 456 ? 0.2396 0.2531 0.2007 0.0475 -0.0183 -0.0126 449 TYR A CA 3192 C C . TYR A 456 ? 0.2381 0.2534 0.2058 0.0486 -0.0231 -0.0153 449 TYR A C 3193 O O . TYR A 456 ? 0.2466 0.2667 0.2233 0.0463 -0.0265 -0.0186 449 TYR A O 3194 C CB . TYR A 456 ? 0.2109 0.2299 0.1803 0.0411 -0.0137 -0.0123 449 TYR A CB 3195 C CG . TYR A 456 ? 0.2163 0.2364 0.1909 0.0390 -0.0104 -0.0113 449 TYR A CG 3196 C CD1 . TYR A 456 ? 0.2431 0.2600 0.2143 0.0392 -0.0056 -0.0079 449 TYR A CD1 3197 C CD2 . TYR A 456 ? 0.2363 0.2603 0.2197 0.0371 -0.0119 -0.0138 449 TYR A CD2 3198 C CE1 . TYR A 456 ? 0.2277 0.2446 0.2038 0.0374 -0.0028 -0.0073 449 TYR A CE1 3199 C CE2 . TYR A 456 ? 0.2399 0.2642 0.2276 0.0357 -0.0087 -0.0133 449 TYR A CE2 3200 C CZ . TYR A 456 ? 0.2420 0.2624 0.2256 0.0358 -0.0046 -0.0102 449 TYR A CZ 3201 O OH . TYR A 456 ? 0.2509 0.2709 0.2390 0.0342 -0.0017 -0.0101 449 TYR A OH 3202 N N . ILE A 457 ? 0.2472 0.2585 0.2114 0.0521 -0.0230 -0.0136 450 ILE A N 3203 C CA . ILE A 457 ? 0.2490 0.2619 0.2200 0.0536 -0.0270 -0.0156 450 ILE A CA 3204 C C . ILE A 457 ? 0.2589 0.2732 0.2360 0.0507 -0.0215 -0.0140 450 ILE A C 3205 O O . ILE A 457 ? 0.2502 0.2595 0.2210 0.0518 -0.0174 -0.0104 450 ILE A O 3206 C CB . ILE A 457 ? 0.2800 0.2857 0.2409 0.0611 -0.0321 -0.0149 450 ILE A CB 3207 C CG1 . ILE A 457 ? 0.2880 0.2908 0.2407 0.0648 -0.0383 -0.0171 450 ILE A CG1 3208 C CG2 . ILE A 457 ? 0.2427 0.2505 0.2125 0.0630 -0.0368 -0.0172 450 ILE A CG2 3209 C CD1 . ILE A 457 ? 0.2787 0.2887 0.2440 0.0617 -0.0436 -0.0223 450 ILE A CD1 3210 N N . ASN A 458 ? 0.2462 0.2668 0.2355 0.0470 -0.0212 -0.0168 451 ASN A N 3211 C CA . ASN A 458 ? 0.2322 0.2539 0.2271 0.0445 -0.0166 -0.0162 451 ASN A CA 3212 C C . ASN A 458 ? 0.2657 0.2838 0.2612 0.0490 -0.0186 -0.0158 451 ASN A C 3213 O O . ASN A 458 ? 0.2672 0.2837 0.2613 0.0539 -0.0246 -0.0168 451 ASN A O 3214 C CB . ASN A 458 ? 0.2378 0.2669 0.2443 0.0396 -0.0151 -0.0193 451 ASN A CB 3215 C CG . ASN A 458 ? 0.2587 0.2883 0.2673 0.0357 -0.0091 -0.0187 451 ASN A CG 3216 O OD1 . ASN A 458 ? 0.2365 0.2637 0.2396 0.0338 -0.0059 -0.0165 451 ASN A OD1 3217 N ND2 . ASN A 458 ? 0.2217 0.2544 0.2387 0.0346 -0.0077 -0.0210 451 ASN A ND2 3218 N N . ALA A 459 ? 0.2562 0.2728 0.2539 0.0477 -0.0141 -0.0146 452 ALA A N 3219 C CA . ALA A 459 ? 0.2548 0.2670 0.2529 0.0522 -0.0157 -0.0139 452 ALA A CA 3220 C C . ALA A 459 ? 0.2401 0.2533 0.2459 0.0495 -0.0112 -0.0148 452 ALA A C 3221 O O . ALA A 459 ? 0.2691 0.2760 0.2717 0.0510 -0.0087 -0.0123 452 ALA A O 3222 C CB . ALA A 459 ? 0.2522 0.2548 0.2371 0.0567 -0.0153 -0.0091 452 ALA A CB 3223 N N . ASP A 460 ? 0.2349 0.2551 0.2505 0.0460 -0.0102 -0.0185 453 ASP A N 3224 C CA . ASP A 460 ? 0.2233 0.2445 0.2464 0.0447 -0.0068 -0.0204 453 ASP A CA 3225 C C . ASP A 460 ? 0.2446 0.2663 0.2746 0.0498 -0.0110 -0.0221 453 ASP A C 3226 O O . ASP A 460 ? 0.2385 0.2576 0.2647 0.0545 -0.0164 -0.0209 453 ASP A O 3227 C CB . ASP A 460 ? 0.2202 0.2480 0.2493 0.0394 -0.0033 -0.0234 453 ASP A CB 3228 C CG . ASP A 460 ? 0.2506 0.2772 0.2825 0.0371 0.0016 -0.0249 453 ASP A CG 3229 O OD1 . ASP A 460 ? 0.2666 0.2884 0.2990 0.0399 0.0019 -0.0244 453 ASP A OD1 3230 O OD2 . ASP A 460 ? 0.2348 0.2650 0.2684 0.0329 0.0049 -0.0269 453 ASP A OD2 3231 N N . SER A 461 ? 0.2398 0.2640 0.2789 0.0493 -0.0085 -0.0248 454 SER A N 3232 C CA . SER A 461 ? 0.2577 0.2830 0.3057 0.0542 -0.0118 -0.0268 454 SER A CA 3233 C C . SER A 461 ? 0.2525 0.2801 0.3026 0.0584 -0.0195 -0.0272 454 SER A C 3234 O O . SER A 461 ? 0.2400 0.2735 0.2936 0.0562 -0.0215 -0.0289 454 SER A O 3235 C CB . SER A 461 ? 0.2512 0.2829 0.3114 0.0519 -0.0078 -0.0309 454 SER A CB 3236 O OG . SER A 461 ? 0.2718 0.3013 0.3282 0.0476 -0.0013 -0.0310 454 SER A OG 3237 N N . SER A 462 ? 0.2664 0.2881 0.3130 0.0646 -0.0243 -0.0256 455 SER A N 3238 C CA . SER A 462 ? 0.2945 0.3170 0.3419 0.0697 -0.0330 -0.0263 455 SER A CA 3239 C C . SER A 462 ? 0.2869 0.3178 0.3523 0.0712 -0.0363 -0.0310 455 SER A C 3240 O O . SER A 462 ? 0.2919 0.3270 0.3630 0.0735 -0.0433 -0.0332 455 SER A O 3241 C CB . SER A 462 ? 0.3210 0.3332 0.3571 0.0763 -0.0367 -0.0226 455 SER A CB 3242 O OG . SER A 462 ? 0.3728 0.3779 0.3930 0.0755 -0.0344 -0.0183 455 SER A OG 3243 N N . ILE A 463 ? 0.2902 0.3236 0.3652 0.0701 -0.0311 -0.0327 456 ILE A N 3244 C CA . ILE A 463 ? 0.3014 0.3433 0.3952 0.0717 -0.0329 -0.0370 456 ILE A CA 3245 C C . ILE A 463 ? 0.3067 0.3547 0.4093 0.0661 -0.0239 -0.0394 456 ILE A C 3246 O O . ILE A 463 ? 0.3324 0.3757 0.4275 0.0636 -0.0175 -0.0381 456 ILE A O 3247 C CB . ILE A 463 ? 0.3107 0.3483 0.4083 0.0789 -0.0368 -0.0369 456 ILE A CB 3248 C CG1 . ILE A 463 ? 0.3291 0.3574 0.4167 0.0789 -0.0309 -0.0339 456 ILE A CG1 3249 C CG2 . ILE A 463 ? 0.3024 0.3354 0.3934 0.0853 -0.0471 -0.0354 456 ILE A CG2 3250 C CD1 . ILE A 463 ? 0.4018 0.4295 0.4998 0.0827 -0.0296 -0.0358 456 ILE A CD1 3251 N N . GLU A 464 ? 0.2965 0.3544 0.4149 0.0643 -0.0234 -0.0430 457 GLU A N 3252 C CA . GLU A 464 ? 0.3041 0.3673 0.4319 0.0607 -0.0146 -0.0455 457 GLU A CA 3253 C C . GLU A 464 ? 0.3031 0.3749 0.4520 0.0637 -0.0162 -0.0493 457 GLU A C 3254 O O . GLU A 464 ? 0.3064 0.3848 0.4670 0.0612 -0.0091 -0.0519 457 GLU A O 3255 C CB . GLU A 464 ? 0.2995 0.3663 0.4243 0.0537 -0.0091 -0.0454 457 GLU A CB 3256 C CG . GLU A 464 ? 0.3198 0.3936 0.4534 0.0523 -0.0136 -0.0464 457 GLU A CG 3257 C CD . GLU A 464 ? 0.3391 0.4144 0.4670 0.0458 -0.0091 -0.0454 457 GLU A CD 3258 O OE1 . GLU A 464 ? 0.3517 0.4223 0.4669 0.0427 -0.0038 -0.0435 457 GLU A OE1 3259 O OE2 . GLU A 464 ? 0.3586 0.4396 0.4956 0.0439 -0.0115 -0.0465 457 GLU A OE2 3260 N N . GLY A 465 ? 0.3028 0.3744 0.4565 0.0695 -0.0256 -0.0496 458 GLY A N 3261 C CA . GLY A 465 ? 0.2878 0.3679 0.4631 0.0731 -0.0295 -0.0534 458 GLY A CA 3262 C C . GLY A 465 ? 0.3004 0.3766 0.4731 0.0798 -0.0419 -0.0527 458 GLY A C 3263 O O . GLY A 465 ? 0.3107 0.3775 0.4643 0.0812 -0.0455 -0.0492 458 GLY A O 3264 N N . ASN A 466 ? 0.2809 0.3643 0.4723 0.0839 -0.0486 -0.0561 459 ASN A N 3265 C CA . ASN A 466 ? 0.3007 0.3798 0.4888 0.0909 -0.0613 -0.0558 459 ASN A CA 3266 C C . ASN A 466 ? 0.2950 0.3839 0.5013 0.0914 -0.0698 -0.0599 459 ASN A C 3267 O O . ASN A 466 ? 0.3020 0.3910 0.5143 0.0979 -0.0808 -0.0616 459 ASN A O 3268 C CB . ASN A 466 ? 0.3237 0.3980 0.5137 0.0983 -0.0637 -0.0554 459 ASN A CB 3269 C CG . ASN A 466 ? 0.3228 0.4080 0.5397 0.0999 -0.0616 -0.0600 459 ASN A CG 3270 O OD1 . ASN A 466 ? 0.3417 0.4385 0.5769 0.0957 -0.0589 -0.0633 459 ASN A OD1 3271 N ND2 . ASN A 466 ? 0.4228 0.5041 0.6428 0.1062 -0.0624 -0.0599 459 ASN A ND2 3272 N N . TYR A 467 ? 0.2861 0.3827 0.5009 0.0844 -0.0649 -0.0614 460 TYR A N 3273 C CA . TYR A 467 ? 0.2853 0.3920 0.5210 0.0836 -0.0715 -0.0656 460 TYR A CA 3274 C C . TYR A 467 ? 0.2832 0.3858 0.5077 0.0837 -0.0815 -0.0656 460 TYR A C 3275 O O . TYR A 467 ? 0.2755 0.3791 0.5067 0.0889 -0.0940 -0.0683 460 TYR A O 3276 C CB . TYR A 467 ? 0.2972 0.4143 0.5501 0.0760 -0.0604 -0.0673 460 TYR A CB 3277 C CG . TYR A 467 ? 0.3207 0.4492 0.5992 0.0744 -0.0656 -0.0717 460 TYR A CG 3278 C CD1 . TYR A 467 ? 0.3657 0.5020 0.6678 0.0795 -0.0730 -0.0757 460 TYR A CD1 3279 C CD2 . TYR A 467 ? 0.3631 0.4947 0.6436 0.0675 -0.0631 -0.0718 460 TYR A CD2 3280 C CE1 . TYR A 467 ? 0.3960 0.5432 0.7239 0.0776 -0.0780 -0.0800 460 TYR A CE1 3281 C CE2 . TYR A 467 ? 0.3751 0.5168 0.6804 0.0654 -0.0676 -0.0757 460 TYR A CE2 3282 C CZ . TYR A 467 ? 0.4135 0.5631 0.7425 0.0702 -0.0750 -0.0799 460 TYR A CZ 3283 O OH . TYR A 467 ? 0.4377 0.5975 0.7929 0.0675 -0.0794 -0.0839 460 TYR A OH 3284 N N . THR A 468 ? 0.2697 0.3675 0.4772 0.0783 -0.0764 -0.0627 461 THR A N 3285 C CA . THR A 468 ? 0.2719 0.3659 0.4692 0.0784 -0.0850 -0.0630 461 THR A CA 3286 C C . THR A 468 ? 0.2672 0.3528 0.4403 0.0745 -0.0784 -0.0586 461 THR A C 3287 O O . THR A 468 ? 0.2669 0.3502 0.4329 0.0717 -0.0680 -0.0557 461 THR A O 3288 C CB . THR A 468 ? 0.2702 0.3744 0.4893 0.0742 -0.0885 -0.0675 461 THR A CB 3289 O OG1 . THR A 468 ? 0.2761 0.3754 0.4855 0.0762 -0.0996 -0.0688 461 THR A OG1 3290 C CG2 . THR A 468 ? 0.2498 0.3586 0.4732 0.0653 -0.0761 -0.0664 461 THR A CG2 3291 N N . LEU A 469 ? 0.2727 0.3533 0.4333 0.0748 -0.0849 -0.0585 462 LEU A N 3292 C CA . LEU A 469 ? 0.2633 0.3368 0.4029 0.0711 -0.0791 -0.0546 462 LEU A CA 3293 C C . LEU A 469 ? 0.2520 0.3315 0.3990 0.0627 -0.0701 -0.0547 462 LEU A C 3294 O O . LEU A 469 ? 0.2513 0.3395 0.4181 0.0596 -0.0709 -0.0580 462 LEU A O 3295 C CB . LEU A 469 ? 0.2717 0.3381 0.3962 0.0745 -0.0888 -0.0549 462 LEU A CB 3296 C CG . LEU A 469 ? 0.2693 0.3262 0.3689 0.0735 -0.0850 -0.0506 462 LEU A CG 3297 C CD1 . LEU A 469 ? 0.2977 0.3462 0.3813 0.0777 -0.0817 -0.0461 462 LEU A CD1 3298 C CD2 . LEU A 469 ? 0.2814 0.3334 0.3719 0.0775 -0.0963 -0.0529 462 LEU A CD2 3299 N N . ARG A 470 ? 0.2394 0.3140 0.3708 0.0592 -0.0617 -0.0508 463 ARG A N 3300 C CA . ARG A 470 ? 0.2610 0.3392 0.3950 0.0519 -0.0537 -0.0501 463 ARG A CA 3301 C C . ARG A 470 ? 0.2623 0.3323 0.3750 0.0511 -0.0538 -0.0471 463 ARG A C 3302 O O . ARG A 470 ? 0.2768 0.3396 0.3731 0.0532 -0.0514 -0.0438 463 ARG A O 3303 C CB . ARG A 470 ? 0.2579 0.3381 0.3942 0.0487 -0.0424 -0.0485 463 ARG A CB 3304 C CG . ARG A 470 ? 0.2861 0.3689 0.4225 0.0415 -0.0334 -0.0473 463 ARG A CG 3305 C CD . ARG A 470 ? 0.3534 0.4368 0.4890 0.0393 -0.0231 -0.0461 463 ARG A CD 3306 N NE . ARG A 470 ? 0.4525 0.5380 0.5879 0.0330 -0.0148 -0.0451 463 ARG A NE 3307 C CZ . ARG A 470 ? 0.4769 0.5624 0.6097 0.0304 -0.0056 -0.0442 463 ARG A CZ 3308 N NH1 . ARG A 470 ? 0.4818 0.5653 0.6125 0.0333 -0.0031 -0.0445 463 ARG A NH1 3309 N NH2 . ARG A 470 ? 0.4779 0.5646 0.6091 0.0252 0.0009 -0.0431 463 ARG A NH2 3310 N N . VAL A 471 ? 0.2567 0.3279 0.3705 0.0479 -0.0559 -0.0482 464 VAL A N 3311 C CA . VAL A 471 ? 0.2441 0.3082 0.3393 0.0473 -0.0560 -0.0458 464 VAL A CA 3312 C C . VAL A 471 ? 0.2470 0.3138 0.3447 0.0404 -0.0493 -0.0450 464 VAL A C 3313 O O . VAL A 471 ? 0.2495 0.3223 0.3627 0.0371 -0.0498 -0.0474 464 VAL A O 3314 C CB . VAL A 471 ? 0.2611 0.3213 0.3514 0.0517 -0.0670 -0.0482 464 VAL A CB 3315 C CG1 . VAL A 471 ? 0.2353 0.2883 0.3068 0.0511 -0.0663 -0.0459 464 VAL A CG1 3316 C CG2 . VAL A 471 ? 0.2615 0.3175 0.3465 0.0593 -0.0742 -0.0486 464 VAL A CG2 3317 N N . ASP A 472 ? 0.2270 0.2894 0.3103 0.0383 -0.0431 -0.0413 465 ASP A N 3318 C CA . ASP A 472 ? 0.2378 0.3008 0.3193 0.0326 -0.0380 -0.0400 465 ASP A CA 3319 C C . ASP A 472 ? 0.2287 0.2845 0.2928 0.0344 -0.0404 -0.0381 465 ASP A C 3320 O O . ASP A 472 ? 0.2305 0.2814 0.2821 0.0372 -0.0390 -0.0356 465 ASP A O 3321 C CB . ASP A 472 ? 0.2053 0.2698 0.2857 0.0283 -0.0279 -0.0375 465 ASP A CB 3322 C CG . ASP A 472 ? 0.2786 0.3487 0.3723 0.0279 -0.0240 -0.0390 465 ASP A CG 3323 O OD1 . ASP A 472 ? 0.2871 0.3615 0.3945 0.0299 -0.0284 -0.0419 465 ASP A OD1 3324 O OD2 . ASP A 472 ? 0.3015 0.3715 0.3920 0.0257 -0.0165 -0.0374 465 ASP A OD2 3325 N N . CYS A 473 ? 0.2460 0.3010 0.3101 0.0327 -0.0431 -0.0391 466 CYS A N 3326 C CA . CYS A 473 ? 0.2370 0.2855 0.2855 0.0347 -0.0451 -0.0377 466 CYS A CA 3327 C C . CYS A 473 ? 0.2425 0.2910 0.2933 0.0313 -0.0459 -0.0387 466 CYS A C 3328 O O . CYS A 473 ? 0.2429 0.2958 0.3080 0.0281 -0.0469 -0.0409 466 CYS A O 3329 C CB . CYS A 473 ? 0.2564 0.2997 0.2962 0.0416 -0.0532 -0.0391 466 CYS A CB 3330 S SG . CYS A 473 ? 0.2731 0.3177 0.3235 0.0441 -0.0645 -0.0449 466 CYS A SG 3331 N N . THR A 474 ? 0.2403 0.2834 0.2774 0.0322 -0.0454 -0.0369 467 THR A N 3332 C CA . THR A 474 ? 0.2364 0.2776 0.2733 0.0306 -0.0478 -0.0382 467 THR A CA 3333 C C . THR A 474 ? 0.2388 0.2792 0.2821 0.0331 -0.0571 -0.0429 467 THR A C 3334 O O . THR A 474 ? 0.2405 0.2787 0.2798 0.0385 -0.0634 -0.0449 467 THR A O 3335 C CB . THR A 474 ? 0.2351 0.2702 0.2555 0.0327 -0.0464 -0.0358 467 THR A CB 3336 O OG1 . THR A 474 ? 0.2200 0.2528 0.2409 0.0316 -0.0492 -0.0375 467 THR A OG1 3337 C CG2 . THR A 474 ? 0.2303 0.2599 0.2378 0.0395 -0.0504 -0.0360 467 THR A CG2 3338 N N . PRO A 475 ? 0.2360 0.2778 0.2894 0.0293 -0.0587 -0.0449 468 PRO A N 3339 C CA . PRO A 475 ? 0.2647 0.3048 0.3235 0.0319 -0.0687 -0.0501 468 PRO A CA 3340 C C . PRO A 475 ? 0.2852 0.3172 0.3262 0.0387 -0.0753 -0.0517 468 PRO A C 3341 O O . PRO A 475 ? 0.2850 0.3150 0.3274 0.0428 -0.0848 -0.0563 468 PRO A O 3342 C CB . PRO A 475 ? 0.2596 0.3000 0.3277 0.0265 -0.0679 -0.0510 468 PRO A CB 3343 C CG . PRO A 475 ? 0.2561 0.3008 0.3293 0.0208 -0.0577 -0.0466 468 PRO A CG 3344 C CD . PRO A 475 ? 0.2432 0.2871 0.3026 0.0230 -0.0522 -0.0428 468 PRO A CD 3345 N N . LEU A 476 ? 0.2729 0.3003 0.2976 0.0402 -0.0704 -0.0482 469 LEU A N 3346 C CA . LEU A 476 ? 0.2803 0.2996 0.2867 0.0469 -0.0747 -0.0490 469 LEU A CA 3347 C C . LEU A 476 ? 0.2767 0.2938 0.2760 0.0530 -0.0789 -0.0495 469 LEU A C 3348 O O . LEU A 476 ? 0.2946 0.3047 0.2808 0.0593 -0.0851 -0.0516 469 LEU A O 3349 C CB . LEU A 476 ? 0.2930 0.3086 0.2852 0.0472 -0.0672 -0.0446 469 LEU A CB 3350 C CG . LEU A 476 ? 0.2654 0.2804 0.2595 0.0434 -0.0647 -0.0444 469 LEU A CG 3351 C CD1 . LEU A 476 ? 0.2692 0.2811 0.2501 0.0447 -0.0582 -0.0404 469 LEU A CD1 3352 C CD2 . LEU A 476 ? 0.2497 0.2598 0.2438 0.0456 -0.0733 -0.0498 469 LEU A CD2 3353 N N . MET A 477 ? 0.2588 0.2812 0.2664 0.0516 -0.0760 -0.0477 470 MET A N 3354 C CA . MET A 477 ? 0.2697 0.2900 0.2717 0.0574 -0.0799 -0.0478 470 MET A CA 3355 C C . MET A 477 ? 0.2731 0.2978 0.2906 0.0582 -0.0884 -0.0524 470 MET A C 3356 O O . MET A 477 ? 0.2881 0.3108 0.3019 0.0635 -0.0931 -0.0529 470 MET A O 3357 C CB . MET A 477 ? 0.2873 0.3091 0.2864 0.0564 -0.0713 -0.0426 470 MET A CB 3358 C CG . MET A 477 ? 0.2799 0.2961 0.2619 0.0579 -0.0647 -0.0381 470 MET A CG 3359 S SD . MET A 477 ? 0.3342 0.3538 0.3191 0.0552 -0.0555 -0.0332 470 MET A SD 3360 C CE . MET A 477 ? 0.3320 0.3480 0.3043 0.0538 -0.0473 -0.0288 470 MET A CE 3361 N N . TYR A 478 ? 0.2645 0.2948 0.2999 0.0534 -0.0907 -0.0559 471 TYR A N 3362 C CA . TYR A 478 ? 0.2726 0.3081 0.3256 0.0541 -0.0988 -0.0605 471 TYR A CA 3363 C C . TYR A 478 ? 0.3011 0.3306 0.3451 0.0621 -0.1110 -0.0645 471 TYR A C 3364 O O . TYR A 478 ? 0.3132 0.3446 0.3621 0.0659 -0.1159 -0.0657 471 TYR A O 3365 C CB . TYR A 478 ? 0.2658 0.3068 0.3391 0.0482 -0.1006 -0.0641 471 TYR A CB 3366 C CG . TYR A 478 ? 0.2665 0.3147 0.3535 0.0403 -0.0898 -0.0609 471 TYR A CG 3367 C CD1 . TYR A 478 ? 0.2764 0.3264 0.3582 0.0387 -0.0798 -0.0558 471 TYR A CD1 3368 C CD2 . TYR A 478 ? 0.2673 0.3197 0.3720 0.0345 -0.0898 -0.0631 471 TYR A CD2 3369 C CE1 . TYR A 478 ? 0.2608 0.3165 0.3534 0.0318 -0.0701 -0.0531 471 TYR A CE1 3370 C CE2 . TYR A 478 ? 0.2950 0.3526 0.4102 0.0278 -0.0798 -0.0599 471 TYR A CE2 3371 C CZ . TYR A 478 ? 0.2882 0.3474 0.3967 0.0266 -0.0701 -0.0550 471 TYR A CZ 3372 O OH . TYR A 478 ? 0.2678 0.3315 0.3856 0.0203 -0.0605 -0.0522 471 TYR A OH 3373 N N . SER A 479 ? 0.3050 0.3270 0.3364 0.0650 -0.1165 -0.0671 472 SER A N 3374 C CA . SER A 479 ? 0.3001 0.3152 0.3214 0.0729 -0.1290 -0.0716 472 SER A CA 3375 C C . SER A 479 ? 0.3218 0.3305 0.3233 0.0802 -0.1285 -0.0680 472 SER A C 3376 O O . SER A 479 ? 0.3056 0.3122 0.3053 0.0861 -0.1376 -0.0705 472 SER A O 3377 C CB . SER A 479 ? 0.3229 0.3304 0.3327 0.0745 -0.1336 -0.0749 472 SER A CB 3378 O OG A SER A 479 ? 0.3514 0.3646 0.3820 0.0679 -0.1352 -0.0786 472 SER A OG 3379 O OG B SER A 479 ? 0.2838 0.2842 0.2839 0.0823 -0.1468 -0.0803 472 SER A OG 3380 N N . LEU A 480 ? 0.3052 0.3102 0.2914 0.0800 -0.1181 -0.0620 473 LEU A N 3381 C CA . LEU A 480 ? 0.3235 0.3229 0.2932 0.0856 -0.1152 -0.0573 473 LEU A CA 3382 C C . LEU A 480 ? 0.3340 0.3395 0.3177 0.0857 -0.1165 -0.0569 473 LEU A C 3383 O O . LEU A 480 ? 0.3468 0.3475 0.3221 0.0927 -0.1225 -0.0568 473 LEU A O 3384 C CB . LEU A 480 ? 0.3132 0.3116 0.2736 0.0823 -0.1017 -0.0508 473 LEU A CB 3385 C CG . LEU A 480 ? 0.3073 0.3027 0.2576 0.0848 -0.0948 -0.0447 473 LEU A CG 3386 C CD1 . LEU A 480 ? 0.4097 0.3938 0.3376 0.0940 -0.0995 -0.0437 473 LEU A CD1 3387 C CD2 . LEU A 480 ? 0.3686 0.3651 0.3159 0.0799 -0.0827 -0.0397 473 LEU A CD2 3388 N N . VAL A 481 ? 0.3157 0.3315 0.3204 0.0784 -0.1107 -0.0565 474 VAL A N 3389 C CA . VAL A 481 ? 0.3171 0.3392 0.3363 0.0785 -0.1109 -0.0562 474 VAL A CA 3390 C C . VAL A 481 ? 0.3174 0.3423 0.3496 0.0821 -0.1236 -0.0622 474 VAL A C 3391 O O . VAL A 481 ? 0.3354 0.3592 0.3672 0.0875 -0.1283 -0.0621 474 VAL A O 3392 C CB . VAL A 481 ? 0.2979 0.3298 0.3354 0.0700 -0.1008 -0.0545 474 VAL A CB 3393 C CG1 . VAL A 481 ? 0.3058 0.3445 0.3598 0.0703 -0.1011 -0.0551 474 VAL A CG1 3394 C CG2 . VAL A 481 ? 0.3216 0.3506 0.3462 0.0672 -0.0890 -0.0486 474 VAL A CG2 3395 N N . TYR A 482 ? 0.3183 0.3467 0.3631 0.0793 -0.1297 -0.0674 475 TYR A N 3396 C CA . TYR A 482 ? 0.3243 0.3554 0.3826 0.0829 -0.1433 -0.0738 475 TYR A CA 3397 C C . TYR A 482 ? 0.3536 0.3738 0.3899 0.0930 -0.1535 -0.0748 475 TYR A C 3398 O O . TYR A 482 ? 0.3452 0.3659 0.3859 0.0985 -0.1618 -0.0767 475 TYR A O 3399 C CB . TYR A 482 ? 0.3180 0.3522 0.3900 0.0789 -0.1494 -0.0797 475 TYR A CB 3400 C CG . TYR A 482 ? 0.3429 0.3859 0.4345 0.0691 -0.1399 -0.0787 475 TYR A CG 3401 C CD1 . TYR A 482 ? 0.3405 0.3928 0.4490 0.0643 -0.1308 -0.0759 475 TYR A CD1 3402 C CD2 . TYR A 482 ? 0.3907 0.4320 0.4835 0.0650 -0.1403 -0.0809 475 TYR A CD2 3403 C CE1 . TYR A 482 ? 0.3226 0.3820 0.4473 0.0556 -0.1218 -0.0748 475 TYR A CE1 3404 C CE2 . TYR A 482 ? 0.3668 0.4149 0.4763 0.0564 -0.1319 -0.0797 475 TYR A CE2 3405 C CZ . TYR A 482 ? 0.3482 0.4052 0.4729 0.0518 -0.1225 -0.0765 475 TYR A CZ 3406 O OH . TYR A 482 ? 0.3700 0.4323 0.5085 0.0436 -0.1139 -0.0750 475 TYR A OH 3407 N N . ASN A 483 ? 0.3492 0.3591 0.3613 0.0960 -0.1531 -0.0736 476 ASN A N 3408 C CA . ASN A 483 ? 0.3797 0.3778 0.3681 0.1063 -0.1626 -0.0745 476 ASN A CA 3409 C C . ASN A 483 ? 0.3829 0.3763 0.3585 0.1117 -0.1593 -0.0689 476 ASN A C 3410 O O . ASN A 483 ? 0.4066 0.3951 0.3757 0.1197 -0.1697 -0.0706 476 ASN A O 3411 C CB . ASN A 483 ? 0.3971 0.3848 0.3613 0.1084 -0.1607 -0.0739 476 ASN A CB 3412 C CG . ASN A 483 ? 0.4247 0.4132 0.3969 0.1060 -0.1684 -0.0809 476 ASN A CG 3413 O OD1 . ASN A 483 ? 0.3911 0.3884 0.3886 0.1020 -0.1747 -0.0860 476 ASN A OD1 3414 N ND2 . ASN A 483 ? 0.4322 0.4113 0.3836 0.1087 -0.1679 -0.0812 476 ASN A ND2 3415 N N . LEU A 484 ? 0.3791 0.3737 0.3515 0.1077 -0.1454 -0.0622 477 LEU A N 3416 C CA . LEU A 484 ? 0.3801 0.3698 0.3413 0.1123 -0.1414 -0.0566 477 LEU A CA 3417 C C . LEU A 484 ? 0.3623 0.3592 0.3432 0.1133 -0.1467 -0.0585 477 LEU A C 3418 O O . LEU A 484 ? 0.3598 0.3505 0.3312 0.1209 -0.1527 -0.0574 477 LEU A O 3419 C CB . LEU A 484 ? 0.3709 0.3613 0.3279 0.1068 -0.1256 -0.0497 477 LEU A CB 3420 C CG . LEU A 484 ? 0.3685 0.3544 0.3172 0.1100 -0.1199 -0.0436 477 LEU A CG 3421 C CD1 . LEU A 484 ? 0.4041 0.3760 0.3263 0.1199 -0.1247 -0.0410 477 LEU A CD1 3422 C CD2 . LEU A 484 ? 0.3546 0.3423 0.3025 0.1035 -0.1051 -0.0380 477 LEU A CD2 3423 N N . THR A 485 ? 0.3534 0.3630 0.3613 0.1059 -0.1439 -0.0609 478 THR A N 3424 C CA . THR A 485 ? 0.3476 0.3651 0.3765 0.1067 -0.1476 -0.0628 478 THR A CA 3425 C C . THR A 485 ? 0.3821 0.3988 0.4160 0.1136 -0.1642 -0.0689 478 THR A C 3426 O O . THR A 485 ? 0.3669 0.3854 0.4091 0.1183 -0.1698 -0.0695 478 THR A O 3427 C CB . THR A 485 ? 0.3323 0.3634 0.3887 0.0974 -0.1395 -0.0638 478 THR A CB 3428 O OG1 . THR A 485 ? 0.3073 0.3440 0.3771 0.0925 -0.1432 -0.0688 478 THR A OG1 3429 C CG2 . THR A 485 ? 0.2898 0.3206 0.3390 0.0917 -0.1237 -0.0575 478 THR A CG2 3430 N N . LYS A 486 ? 0.4049 0.4177 0.4321 0.1151 -0.1729 -0.0735 479 LYS A N 3431 C CA . LYS A 486 ? 0.4276 0.4379 0.4567 0.1225 -0.1903 -0.0798 479 LYS A CA 3432 C C . LYS A 486 ? 0.4563 0.4532 0.4581 0.1335 -0.1965 -0.0769 479 LYS A C 3433 O O . LYS A 486 ? 0.4680 0.4633 0.4723 0.1406 -0.2103 -0.0809 479 LYS A O 3434 C CB . LYS A 486 ? 0.4436 0.4525 0.4728 0.1213 -0.1987 -0.0862 479 LYS A CB 3435 C CG . LYS A 486 ? 0.4434 0.4659 0.5047 0.1119 -0.1973 -0.0906 479 LYS A CG 3436 C CD . LYS A 486 ? 0.4924 0.5123 0.5534 0.1104 -0.2050 -0.0967 479 LYS A CD 3437 C CE . LYS A 486 ? 0.4591 0.4918 0.5512 0.1000 -0.2000 -0.0992 479 LYS A CE 3438 N NZ . LYS A 486 ? 0.4917 0.5217 0.5839 0.0967 -0.2039 -0.1037 479 LYS A NZ 3439 N N . GLU A 487 ? 0.4671 0.4545 0.4438 0.1348 -0.1862 -0.0699 480 GLU A N 3440 C CA . GLU A 487 ? 0.5096 0.4826 0.4575 0.1450 -0.1897 -0.0658 480 GLU A CA 3441 C C . GLU A 487 ? 0.5007 0.4731 0.4492 0.1466 -0.1828 -0.0595 480 GLU A C 3442 O O . GLU A 487 ? 0.5376 0.4979 0.4639 0.1550 -0.1854 -0.0555 480 GLU A O 3443 C CB . GLU A 487 ? 0.5316 0.4927 0.4496 0.1465 -0.1824 -0.0615 480 GLU A CB 3444 C CG . GLU A 487 ? 0.5965 0.5553 0.5088 0.1462 -0.1888 -0.0674 480 GLU A CG 3445 C CD . GLU A 487 ? 0.7128 0.6666 0.6210 0.1544 -0.2076 -0.0747 480 GLU A CD 3446 O OE1 . GLU A 487 ? 0.7650 0.7238 0.6866 0.1515 -0.2157 -0.0822 480 GLU A OE1 3447 O OE2 . GLU A 487 ? 0.7638 0.7084 0.6560 0.1639 -0.2148 -0.0731 480 GLU A OE2 3448 N N . LEU A 488 ? 0.4592 0.4437 0.4321 0.1388 -0.1741 -0.0586 481 LEU A N 3449 C CA . LEU A 488 ? 0.4442 0.4292 0.4212 0.1397 -0.1676 -0.0536 481 LEU A CA 3450 C C . LEU A 488 ? 0.4427 0.4364 0.4441 0.1421 -0.1768 -0.0579 481 LEU A C 3451 O O . LEU A 488 ? 0.4335 0.4384 0.4588 0.1384 -0.1826 -0.0644 481 LEU A O 3452 C CB . LEU A 488 ? 0.4091 0.4005 0.3946 0.1301 -0.1508 -0.0494 481 LEU A CB 3453 C CG . LEU A 488 ? 0.4110 0.3960 0.3769 0.1266 -0.1401 -0.0448 481 LEU A CG 3454 C CD1 . LEU A 488 ? 0.3352 0.3285 0.3142 0.1169 -0.1258 -0.0421 481 LEU A CD1 3455 C CD2 . LEU A 488 ? 0.4347 0.4043 0.3713 0.1342 -0.1382 -0.0383 481 LEU A CD2 3456 N N . LYS A 489 ? 0.4521 0.4406 0.4486 0.1481 -0.1775 -0.0542 482 LYS A N 3457 C CA . LYS A 489 ? 0.4707 0.4671 0.4905 0.1513 -0.1860 -0.0581 482 LYS A CA 3458 C C . LYS A 489 ? 0.4447 0.4548 0.4918 0.1426 -0.1748 -0.0582 482 LYS A C 3459 O O . LYS A 489 ? 0.4521 0.4607 0.4931 0.1376 -0.1608 -0.0530 482 LYS A O 3460 C CB . LYS A 489 ? 0.4854 0.4706 0.4900 0.1612 -0.1903 -0.0536 482 LYS A CB 3461 C CG . LYS A 489 ? 0.5634 0.5316 0.5342 0.1706 -0.1982 -0.0511 482 LYS A CG 3462 C CD . LYS A 489 ? 0.6742 0.6333 0.6365 0.1808 -0.2048 -0.0478 482 LYS A CD 3463 C CE . LYS A 489 ? 0.7712 0.7113 0.6968 0.1873 -0.2005 -0.0395 482 LYS A CE 3464 N NZ . LYS A 489 ? 0.8224 0.7510 0.7211 0.1940 -0.2099 -0.0410 482 LYS A NZ 3465 N N . SER A 490 ? 0.4249 0.4480 0.5017 0.1408 -0.1807 -0.0643 483 SER A N 3466 C CA . SER A 490 ? 0.4056 0.4410 0.5074 0.1338 -0.1698 -0.0644 483 SER A CA 3467 C C . SER A 490 ? 0.4080 0.4401 0.5097 0.1387 -0.1669 -0.0606 483 SER A C 3468 O O . SER A 490 ? 0.4252 0.4529 0.5252 0.1476 -0.1783 -0.0615 483 SER A O 3469 C CB . SER A 490 ? 0.4009 0.4515 0.5361 0.1305 -0.1759 -0.0717 483 SER A CB 3470 O OG . SER A 490 ? 0.3846 0.4462 0.5429 0.1250 -0.1649 -0.0715 483 SER A OG 3471 N N . PRO A 491 ? 0.3938 0.4276 0.4977 0.1332 -0.1521 -0.0566 484 PRO A N 3472 C CA . PRO A 491 ? 0.3978 0.4285 0.5035 0.1375 -0.1491 -0.0536 484 PRO A CA 3473 C C . PRO A 491 ? 0.3986 0.4434 0.5373 0.1362 -0.1492 -0.0584 484 PRO A C 3474 O O . PRO A 491 ? 0.3945 0.4382 0.5384 0.1396 -0.1466 -0.0567 484 PRO A O 3475 C CB . PRO A 491 ? 0.3836 0.4093 0.4762 0.1316 -0.1336 -0.0478 484 PRO A CB 3476 C CG . PRO A 491 ? 0.3647 0.3998 0.4662 0.1217 -0.1264 -0.0502 484 PRO A CG 3477 C CD . PRO A 491 ? 0.3835 0.4197 0.4841 0.1236 -0.1384 -0.0544 484 PRO A CD 3478 N N . ASP A 492 ? 0.3937 0.4513 0.5546 0.1316 -0.1523 -0.0642 485 ASP A N 3479 C CA . ASP A 492 ? 0.3844 0.4570 0.5786 0.1285 -0.1493 -0.0687 485 ASP A CA 3480 C C . ASP A 492 ? 0.4010 0.4774 0.6123 0.1370 -0.1626 -0.0726 485 ASP A C 3481 O O . ASP A 492 ? 0.4129 0.4857 0.6193 0.1431 -0.1775 -0.0751 485 ASP A O 3482 C CB . ASP A 492 ? 0.3722 0.4567 0.5849 0.1203 -0.1474 -0.0731 485 ASP A CB 3483 C CG . ASP A 492 ? 0.3522 0.4350 0.5526 0.1115 -0.1342 -0.0698 485 ASP A CG 3484 O OD1 . ASP A 492 ? 0.3794 0.4518 0.5561 0.1115 -0.1272 -0.0643 485 ASP A OD1 3485 O OD2 . ASP A 492 ? 0.3390 0.4310 0.5546 0.1044 -0.1307 -0.0726 485 ASP A OD2 3486 N N . GLU A 493 ? 0.4053 0.4890 0.6368 0.1376 -0.1574 -0.0736 486 GLU A N 3487 C CA . GLU A 493 ? 0.4242 0.5140 0.6775 0.1452 -0.1688 -0.0778 486 GLU A CA 3488 C C . GLU A 493 ? 0.4117 0.5141 0.6899 0.1431 -0.1786 -0.0848 486 GLU A C 3489 O O . GLU A 493 ? 0.3946 0.5070 0.6878 0.1343 -0.1705 -0.0868 486 GLU A O 3490 C CB . GLU A 493 ? 0.4248 0.5218 0.6976 0.1446 -0.1584 -0.0778 486 GLU A CB 3491 C CG . GLU A 493 ? 0.4879 0.5716 0.7391 0.1485 -0.1517 -0.0717 486 GLU A CG 3492 C CD . GLU A 493 ? 0.5365 0.6148 0.7697 0.1405 -0.1358 -0.0670 486 GLU A CD 3493 O OE1 . GLU A 493 ? 0.5650 0.6483 0.7984 0.1322 -0.1300 -0.0678 486 GLU A OE1 3494 O OE2 . GLU A 493 ? 0.5421 0.6106 0.7608 0.1425 -0.1293 -0.0625 486 GLU A OE2 3495 N N . GLY A 494 ? 0.4313 0.5329 0.7140 0.1513 -0.1962 -0.0885 487 GLY A N 3496 C CA . GLY A 494 ? 0.4172 0.5298 0.7232 0.1494 -0.2070 -0.0956 487 GLY A CA 3497 C C . GLY A 494 ? 0.4305 0.5357 0.7159 0.1475 -0.2138 -0.0962 487 GLY A C 3498 O O . GLY A 494 ? 0.4406 0.5521 0.7415 0.1473 -0.2255 -0.1023 487 GLY A O 3499 N N . PHE A 495 ? 0.4154 0.5073 0.6670 0.1461 -0.2065 -0.0902 488 PHE A N 3500 C CA . PHE A 495 ? 0.4267 0.5102 0.6564 0.1454 -0.2127 -0.0907 488 PHE A CA 3501 C C . PHE A 495 ? 0.4531 0.5182 0.6459 0.1546 -0.2199 -0.0863 488 PHE A C 3502 O O . PHE A 495 ? 0.4431 0.4983 0.6097 0.1534 -0.2183 -0.0838 488 PHE A O 3503 C CB . PHE A 495 ? 0.4011 0.4855 0.6238 0.1348 -0.1973 -0.0878 488 PHE A CB 3504 C CG . PHE A 495 ? 0.3846 0.4850 0.6397 0.1256 -0.1901 -0.0916 488 PHE A CG 3505 C CD1 . PHE A 495 ? 0.4012 0.5071 0.6681 0.1211 -0.1961 -0.0966 488 PHE A CD1 3506 C CD2 . PHE A 495 ? 0.3864 0.4959 0.6601 0.1215 -0.1769 -0.0901 488 PHE A CD2 3507 C CE1 . PHE A 495 ? 0.4100 0.5302 0.7071 0.1124 -0.1887 -0.0996 488 PHE A CE1 3508 C CE2 . PHE A 495 ? 0.3838 0.5076 0.6866 0.1132 -0.1692 -0.0932 488 PHE A CE2 3509 C CZ . PHE A 495 ? 0.4083 0.5374 0.7230 0.1084 -0.1748 -0.0976 488 PHE A CZ 3510 N N . GLU A 496 ? 0.4687 0.5289 0.6586 0.1639 -0.2268 -0.0849 489 GLU A N 3511 C CA . GLU A 496 ? 0.5085 0.5502 0.6625 0.1731 -0.2333 -0.0801 489 GLU A CA 3512 C C . GLU A 496 ? 0.5255 0.5620 0.6684 0.1779 -0.2500 -0.0849 489 GLU A C 3513 O O . GLU A 496 ? 0.5268 0.5728 0.6934 0.1795 -0.2630 -0.0923 489 GLU A O 3514 C CB . GLU A 496 ? 0.5284 0.5650 0.6820 0.1827 -0.2383 -0.0776 489 GLU A CB 3515 C CG . GLU A 496 ? 0.5592 0.6109 0.7505 0.1842 -0.2443 -0.0833 489 GLU A CG 3516 C CD . GLU A 496 ? 0.5529 0.6179 0.7700 0.1753 -0.2277 -0.0831 489 GLU A CD 3517 O OE1 . GLU A 496 ? 0.5367 0.5964 0.7441 0.1744 -0.2151 -0.0773 489 GLU A OE1 3518 O OE2 . GLU A 496 ? 0.5672 0.6480 0.8149 0.1693 -0.2277 -0.0891 489 GLU A OE2 3519 N N . GLY A 497 ? 0.5302 0.5520 0.6383 0.1799 -0.2492 -0.0810 490 GLY A N 3520 C CA . GLY A 497 ? 0.5499 0.5659 0.6450 0.1839 -0.2637 -0.0858 490 GLY A CA 3521 C C . GLY A 497 ? 0.5266 0.5506 0.6320 0.1740 -0.2597 -0.0900 490 GLY A C 3522 O O . GLY A 497 ? 0.5535 0.5725 0.6481 0.1763 -0.2705 -0.0944 490 GLY A O 3523 N N . LYS A 498 ? 0.4856 0.5212 0.6107 0.1634 -0.2445 -0.0889 491 LYS A N 3524 C CA . LYS A 498 ? 0.4577 0.5002 0.5921 0.1538 -0.2395 -0.0920 491 LYS A CA 3525 C C . LYS A 498 ? 0.4366 0.4718 0.5475 0.1483 -0.2235 -0.0852 491 LYS A C 3526 O O . LYS A 498 ? 0.4305 0.4590 0.5262 0.1499 -0.2139 -0.0783 491 LYS A O 3527 C CB . LYS A 498 ? 0.4404 0.5016 0.6156 0.1453 -0.2349 -0.0963 491 LYS A CB 3528 C CG . LYS A 498 ? 0.4668 0.5373 0.6703 0.1506 -0.2500 -0.1031 491 LYS A CG 3529 C CD . LYS A 498 ? 0.5282 0.5931 0.7247 0.1569 -0.2698 -0.1095 491 LYS A CD 3530 C CE . LYS A 498 ? 0.6019 0.6776 0.8305 0.1613 -0.2855 -0.1170 491 LYS A CE 3531 N NZ . LYS A 498 ? 0.6193 0.7137 0.8883 0.1508 -0.2773 -0.1205 491 LYS A NZ 3532 N N . SER A 499 ? 0.4200 0.4561 0.5286 0.1423 -0.2214 -0.0873 492 SER A N 3533 C CA . SER A 499 ? 0.4106 0.4408 0.4990 0.1366 -0.2066 -0.0815 492 SER A CA 3534 C C . SER A 499 ? 0.3930 0.4340 0.5003 0.1270 -0.1904 -0.0787 492 SER A C 3535 O O . SER A 499 ? 0.3926 0.4469 0.5304 0.1227 -0.1900 -0.0824 492 SER A O 3536 C CB . SER A 499 ? 0.4097 0.4372 0.4904 0.1338 -0.2105 -0.0852 492 SER A CB 3537 O OG . SER A 499 ? 0.3957 0.4369 0.5061 0.1250 -0.2082 -0.0897 492 SER A OG 3538 N N . LEU A 500 ? 0.3860 0.4211 0.4748 0.1236 -0.1768 -0.0722 493 LEU A N 3539 C CA . LEU A 500 ? 0.3595 0.4029 0.4613 0.1144 -0.1612 -0.0694 493 LEU A CA 3540 C C . LEU A 500 ? 0.3484 0.4017 0.4691 0.1062 -0.1598 -0.0738 493 LEU A C 3541 O O . LEU A 500 ? 0.3157 0.3803 0.4598 0.0996 -0.1522 -0.0747 493 LEU A O 3542 C CB . LEU A 500 ? 0.3587 0.3925 0.4348 0.1129 -0.1492 -0.0622 493 LEU A CB 3543 C CG . LEU A 500 ? 0.3425 0.3822 0.4258 0.1042 -0.1334 -0.0589 493 LEU A CG 3544 C CD1 . LEU A 500 ? 0.3078 0.3552 0.4113 0.1040 -0.1296 -0.0590 493 LEU A CD1 3545 C CD2 . LEU A 500 ? 0.3174 0.3466 0.3747 0.1038 -0.1240 -0.0523 493 LEU A CD2 3546 N N . TYR A 501 ? 0.3520 0.4005 0.4626 0.1068 -0.1673 -0.0767 494 TYR A N 3547 C CA . TYR A 501 ? 0.3562 0.4125 0.4844 0.0995 -0.1674 -0.0811 494 TYR A CA 3548 C C . TYR A 501 ? 0.3457 0.4152 0.5085 0.0978 -0.1732 -0.0867 494 TYR A C 3549 O O . TYR A 501 ? 0.3302 0.4098 0.5147 0.0897 -0.1655 -0.0877 494 TYR A O 3550 C CB . TYR A 501 ? 0.3648 0.4131 0.4778 0.1019 -0.1772 -0.0846 494 TYR A CB 3551 C CG . TYR A 501 ? 0.3774 0.4326 0.5080 0.0940 -0.1766 -0.0887 494 TYR A CG 3552 C CD1 . TYR A 501 ? 0.3773 0.4314 0.5006 0.0871 -0.1647 -0.0852 494 TYR A CD1 3553 C CD2 . TYR A 501 ? 0.4069 0.4697 0.5628 0.0934 -0.1882 -0.0961 494 TYR A CD2 3554 C CE1 . TYR A 501 ? 0.4022 0.4617 0.5412 0.0799 -0.1638 -0.0884 494 TYR A CE1 3555 C CE2 . TYR A 501 ? 0.3977 0.4661 0.5706 0.0858 -0.1872 -0.0996 494 TYR A CE2 3556 C CZ . TYR A 501 ? 0.3944 0.4606 0.5577 0.0792 -0.1748 -0.0954 494 TYR A CZ 3557 O OH . TYR A 501 ? 0.3919 0.4625 0.5709 0.0718 -0.1733 -0.0982 494 TYR A OH 3558 N N . GLU A 502 ? 0.3640 0.4331 0.5319 0.1055 -0.1868 -0.0905 495 GLU A N 3559 C CA . GLU A 502 ? 0.3761 0.4583 0.5788 0.1043 -0.1931 -0.0962 495 GLU A CA 3560 C C . GLU A 502 ? 0.3575 0.4504 0.5811 0.0998 -0.1802 -0.0935 495 GLU A C 3561 O O . GLU A 502 ? 0.3440 0.4491 0.5959 0.0930 -0.1755 -0.0961 495 GLU A O 3562 C CB . GLU A 502 ? 0.3995 0.4789 0.6030 0.1144 -0.2112 -0.1007 495 GLU A CB 3563 C CG . GLU A 502 ? 0.4467 0.5406 0.6884 0.1135 -0.2177 -0.1067 495 GLU A CG 3564 C CD . GLU A 502 ? 0.5156 0.6069 0.7596 0.1230 -0.2381 -0.1126 495 GLU A CD 3565 O OE1 . GLU A 502 ? 0.5521 0.6316 0.7719 0.1282 -0.2488 -0.1142 495 GLU A OE1 3566 O OE2 . GLU A 502 ? 0.5571 0.6579 0.8268 0.1256 -0.2435 -0.1156 495 GLU A OE2 3567 N N . SER A 503 ? 0.3524 0.4402 0.5613 0.1033 -0.1735 -0.0882 496 SER A N 3568 C CA . SER A 503 ? 0.3418 0.4389 0.5700 0.1004 -0.1626 -0.0864 496 SER A CA 3569 C C . SER A 503 ? 0.3292 0.4305 0.5601 0.0904 -0.1461 -0.0833 496 SER A C 3570 O O . SER A 503 ? 0.3148 0.4275 0.5707 0.0852 -0.1385 -0.0846 496 SER A O 3571 C CB . SER A 503 ? 0.3489 0.4390 0.5627 0.1074 -0.1612 -0.0822 496 SER A CB 3572 O OG . SER A 503 ? 0.3151 0.3932 0.4981 0.1074 -0.1536 -0.0760 496 SER A OG 3573 N N . TRP A 504 ? 0.3216 0.4136 0.5270 0.0881 -0.1409 -0.0794 497 TRP A N 3574 C CA . TRP A 504 ? 0.3131 0.4076 0.5178 0.0793 -0.1268 -0.0765 497 TRP A CA 3575 C C . TRP A 504 ? 0.3138 0.4175 0.5414 0.0726 -0.1274 -0.0807 497 TRP A C 3576 O O . TRP A 504 ? 0.3039 0.4155 0.5470 0.0658 -0.1162 -0.0798 497 TRP A O 3577 C CB . TRP A 504 ? 0.3160 0.3984 0.4890 0.0792 -0.1230 -0.0718 497 TRP A CB 3578 C CG . TRP A 504 ? 0.3004 0.3837 0.4694 0.0708 -0.1105 -0.0688 497 TRP A CG 3579 C CD1 . TRP A 504 ? 0.2551 0.3457 0.4369 0.0643 -0.0982 -0.0673 497 TRP A CD1 3580 C CD2 . TRP A 504 ? 0.3088 0.3845 0.4579 0.0688 -0.1092 -0.0668 497 TRP A CD2 3581 N NE1 . TRP A 504 ? 0.2588 0.3465 0.4295 0.0585 -0.0903 -0.0644 497 TRP A NE1 3582 C CE2 . TRP A 504 ? 0.3004 0.3795 0.4522 0.0610 -0.0968 -0.0642 497 TRP A CE2 3583 C CE3 . TRP A 504 ? 0.3294 0.3955 0.4584 0.0733 -0.1176 -0.0672 497 TRP A CE3 3584 C CZ2 . TRP A 504 ? 0.2810 0.3548 0.4178 0.0574 -0.0929 -0.0619 497 TRP A CZ2 3585 C CZ3 . TRP A 504 ? 0.2893 0.3503 0.4033 0.0697 -0.1129 -0.0650 497 TRP A CZ3 3586 C CH2 . TRP A 504 ? 0.3020 0.3671 0.4206 0.0618 -0.1008 -0.0624 497 TRP A CH2 3587 N N . THR A 505 ? 0.3146 0.4168 0.5444 0.0748 -0.1404 -0.0853 498 THR A N 3588 C CA . THR A 505 ? 0.3155 0.4252 0.5669 0.0682 -0.1415 -0.0892 498 THR A CA 3589 C C . THR A 505 ? 0.3286 0.4523 0.6158 0.0661 -0.1407 -0.0927 498 THR A C 3590 O O . THR A 505 ? 0.3199 0.4518 0.6262 0.0585 -0.1312 -0.0925 498 THR A O 3591 C CB . THR A 505 ? 0.3282 0.4318 0.5724 0.0712 -0.1563 -0.0939 498 THR A CB 3592 O OG1 A THR A 505 ? 0.2706 0.3624 0.4838 0.0716 -0.1534 -0.0902 498 THR A OG1 3593 C CG2 A THR A 505 ? 0.3166 0.4285 0.5879 0.0646 -0.1588 -0.0988 498 THR A CG2 3594 N N . LYS A 506 ? 0.3434 0.4695 0.6390 0.0732 -0.1495 -0.0952 499 LYS A N 3595 C CA . LYS A 506 ? 0.3516 0.4912 0.6811 0.0723 -0.1483 -0.0983 499 LYS A CA 3596 C C . LYS A 506 ? 0.3396 0.4850 0.6761 0.0674 -0.1301 -0.0939 499 LYS A C 3597 O O . LYS A 506 ? 0.3315 0.4881 0.6953 0.0618 -0.1230 -0.0954 499 LYS A O 3598 C CB . LYS A 506 ? 0.3724 0.5118 0.7056 0.0820 -0.1620 -0.1014 499 LYS A CB 3599 C CG . LYS A 506 ? 0.4102 0.5637 0.7791 0.0824 -0.1617 -0.1048 499 LYS A CG 3600 C CD . LYS A 506 ? 0.4903 0.6542 0.8910 0.0788 -0.1700 -0.1114 499 LYS A CD 3601 C CE . LYS A 506 ? 0.4972 0.6761 0.9361 0.0795 -0.1697 -0.1149 499 LYS A CE 3602 N NZ . LYS A 506 ? 0.5330 0.7218 1.0035 0.0745 -0.1761 -0.1209 499 LYS A NZ 3603 N N . LYS A 507 ? 0.3350 0.4724 0.6468 0.0694 -0.1225 -0.0886 500 LYS A N 3604 C CA . LYS A 507 ? 0.3232 0.4647 0.6393 0.0659 -0.1065 -0.0851 500 LYS A CA 3605 C C . LYS A 507 ? 0.3167 0.4576 0.6259 0.0573 -0.0927 -0.0815 500 LYS A C 3606 O O . LYS A 507 ? 0.3073 0.4535 0.6255 0.0533 -0.0797 -0.0798 500 LYS A O 3607 C CB . LYS A 507 ? 0.3244 0.4577 0.6192 0.0719 -0.1047 -0.0815 500 LYS A CB 3608 C CG . LYS A 507 ? 0.3370 0.4722 0.6424 0.0806 -0.1151 -0.0843 500 LYS A CG 3609 C CD . LYS A 507 ? 0.3350 0.4613 0.6195 0.0855 -0.1108 -0.0799 500 LYS A CD 3610 C CE . LYS A 507 ? 0.3428 0.4687 0.6338 0.0948 -0.1216 -0.0820 500 LYS A CE 3611 N NZ . LYS A 507 ? 0.3545 0.4705 0.6246 0.0991 -0.1165 -0.0772 500 LYS A NZ 3612 N N . SER A 508 ? 0.3064 0.4401 0.5985 0.0549 -0.0955 -0.0804 501 SER A N 3613 C CA . SER A 508 ? 0.3160 0.4474 0.5983 0.0476 -0.0835 -0.0766 501 SER A CA 3614 C C . SER A 508 ? 0.3347 0.4653 0.6201 0.0436 -0.0892 -0.0787 501 SER A C 3615 O O . SER A 508 ? 0.3216 0.4430 0.5844 0.0435 -0.0911 -0.0768 501 SER A O 3616 C CB . SER A 508 ? 0.3146 0.4347 0.5649 0.0496 -0.0796 -0.0718 501 SER A CB 3617 O OG . SER A 508 ? 0.3381 0.4566 0.5796 0.0432 -0.0676 -0.0680 501 SER A OG 3618 N N . PRO A 509 ? 0.3438 0.4839 0.6586 0.0406 -0.0922 -0.0829 502 PRO A N 3619 C CA . PRO A 509 ? 0.3623 0.5011 0.6817 0.0371 -0.0989 -0.0856 502 PRO A CA 3620 C C . PRO A 509 ? 0.3738 0.5086 0.6820 0.0300 -0.0876 -0.0812 502 PRO A C 3621 O O . PRO A 509 ? 0.3635 0.5016 0.6748 0.0255 -0.0736 -0.0775 502 PRO A O 3622 C CB . PRO A 509 ? 0.3595 0.5108 0.7167 0.0347 -0.1020 -0.0905 502 PRO A CB 3623 C CG . PRO A 509 ? 0.3489 0.5085 0.7199 0.0338 -0.0900 -0.0885 502 PRO A CG 3624 C CD . PRO A 509 ? 0.3338 0.4863 0.6797 0.0402 -0.0893 -0.0855 502 PRO A CD 3625 N N . SER A 510 ? 0.4017 0.5288 0.6959 0.0293 -0.0938 -0.0818 503 SER A N 3626 C CA . SER A 510 ? 0.4341 0.5572 0.7193 0.0228 -0.0847 -0.0780 503 SER A CA 3627 C C . SER A 510 ? 0.4559 0.5874 0.7692 0.0156 -0.0785 -0.0788 503 SER A C 3628 O O . SER A 510 ? 0.4590 0.5959 0.7950 0.0152 -0.0872 -0.0839 503 SER A O 3629 C CB . SER A 510 ? 0.4408 0.5546 0.7095 0.0240 -0.0938 -0.0795 503 SER A CB 3630 O OG . SER A 510 ? 0.4511 0.5621 0.7160 0.0174 -0.0853 -0.0763 503 SER A OG 3631 N N . PRO A 511 ? 0.4784 0.6108 0.7905 0.0099 -0.0637 -0.0739 504 PRO A N 3632 C CA . PRO A 511 ? 0.5026 0.6416 0.8397 0.0027 -0.0564 -0.0737 504 PRO A CA 3633 C C . PRO A 511 ? 0.5277 0.6611 0.8634 -0.0015 -0.0601 -0.0741 504 PRO A C 3634 O O . PRO A 511 ? 0.5314 0.6698 0.8925 -0.0055 -0.0625 -0.0771 504 PRO A O 3635 C CB . PRO A 511 ? 0.4974 0.6368 0.8270 -0.0007 -0.0394 -0.0677 504 PRO A CB 3636 C CG . PRO A 511 ? 0.4971 0.6323 0.8036 0.0050 -0.0391 -0.0660 504 PRO A CG 3637 C CD . PRO A 511 ? 0.4793 0.6069 0.7684 0.0100 -0.0528 -0.0683 504 PRO A CD 3638 N N . GLU A 512 ? 0.5555 0.6786 0.8629 -0.0005 -0.0604 -0.0713 505 GLU A N 3639 C CA . GLU A 512 ? 0.5907 0.7069 0.8930 -0.0037 -0.0638 -0.0715 505 GLU A CA 3640 C C . GLU A 512 ? 0.6022 0.7158 0.9083 -0.0002 -0.0804 -0.0780 505 GLU A C 3641 O O . GLU A 512 ? 0.6155 0.7276 0.9333 -0.0040 -0.0844 -0.0805 505 GLU A O 3642 C CB . GLU A 512 ? 0.5879 0.6944 0.8596 -0.0035 -0.0583 -0.0663 505 GLU A CB 3643 C CG . GLU A 512 ? 0.6330 0.7402 0.9003 -0.0081 -0.0423 -0.0599 505 GLU A CG 3644 C CD . GLU A 512 ? 0.6895 0.7990 0.9759 -0.0156 -0.0344 -0.0580 505 GLU A CD 3645 O OE1 . GLU A 512 ? 0.7034 0.8125 1.0043 -0.0181 -0.0411 -0.0613 505 GLU A OE1 3646 O OE2 . GLU A 512 ? 0.6964 0.8078 0.9829 -0.0190 -0.0212 -0.0533 505 GLU A OE2 3647 N N . PHE A 513 ? 0.6119 0.7242 0.9076 0.0071 -0.0900 -0.0809 506 PHE A N 3648 C CA . PHE A 513 ? 0.6217 0.7295 0.9149 0.0118 -0.1064 -0.0871 506 PHE A CA 3649 C C . PHE A 513 ? 0.6215 0.7367 0.9324 0.0163 -0.1158 -0.0922 506 PHE A C 3650 O O . PHE A 513 ? 0.6235 0.7380 0.9223 0.0226 -0.1183 -0.0917 506 PHE A O 3651 C CB . PHE A 513 ? 0.6301 0.7267 0.8890 0.0176 -0.1102 -0.0856 506 PHE A CB 3652 C CG . PHE A 513 ? 0.6420 0.7320 0.8825 0.0139 -0.1001 -0.0800 506 PHE A CG 3653 C CD1 . PHE A 513 ? 0.6475 0.7328 0.8896 0.0099 -0.1014 -0.0810 506 PHE A CD1 3654 C CD2 . PHE A 513 ? 0.6577 0.7462 0.8805 0.0144 -0.0895 -0.0740 506 PHE A CD2 3655 C CE1 . PHE A 513 ? 0.6610 0.7402 0.8869 0.0069 -0.0925 -0.0758 506 PHE A CE1 3656 C CE2 . PHE A 513 ? 0.6654 0.7481 0.8720 0.0113 -0.0810 -0.0691 506 PHE A CE2 3657 C CZ . PHE A 513 ? 0.6689 0.7471 0.8770 0.0076 -0.0825 -0.0699 506 PHE A CZ 3658 N N . SER A 514 ? 0.6151 0.7373 0.9560 0.0130 -0.1212 -0.0971 507 SER A N 3659 C CA . SER A 514 ? 0.6138 0.7445 0.9766 0.0169 -0.1310 -0.1025 507 SER A CA 3660 C C . SER A 514 ? 0.6075 0.7312 0.9501 0.0265 -0.1461 -0.1063 507 SER A C 3661 O O . SER A 514 ? 0.6127 0.7261 0.9355 0.0289 -0.1540 -0.1081 507 SER A O 3662 C CB . SER A 514 ? 0.6247 0.7623 1.0220 0.0118 -0.1370 -0.1082 507 SER A CB 3663 O OG . SER A 514 ? 0.6374 0.7797 1.0507 0.0029 -0.1221 -0.1039 507 SER A OG 3664 N N . GLY A 515 ? 0.5873 0.7159 0.9340 0.0321 -0.1492 -0.1071 508 GLY A N 3665 C CA . GLY A 515 ? 0.5669 0.6893 0.8968 0.0418 -0.1639 -0.1105 508 GLY A CA 3666 C C . GLY A 515 ? 0.5452 0.6567 0.8374 0.0473 -0.1604 -0.1052 508 GLY A C 3667 O O . GLY A 515 ? 0.5459 0.6521 0.8233 0.0557 -0.1705 -0.1068 508 GLY A O 3668 N N . MET A 516 ? 0.5131 0.6209 0.7898 0.0427 -0.1464 -0.0990 509 MET A N 3669 C CA . MET A 516 ? 0.4854 0.5838 0.7290 0.0467 -0.1411 -0.0935 509 MET A CA 3670 C C . MET A 516 ? 0.4532 0.5567 0.6983 0.0462 -0.1292 -0.0885 509 MET A C 3671 O O . MET A 516 ? 0.4377 0.5509 0.7055 0.0409 -0.1210 -0.0879 509 MET A O 3672 C CB . MET A 516 ? 0.4795 0.5716 0.7075 0.0417 -0.1329 -0.0898 509 MET A CB 3673 C CG . MET A 516 ? 0.5132 0.6019 0.7461 0.0394 -0.1410 -0.0945 509 MET A CG 3674 S SD . MET A 516 ? 0.5496 0.6274 0.7607 0.0494 -0.1586 -0.0996 509 MET A SD 3675 C CE . MET A 516 ? 0.5471 0.6142 0.7210 0.0515 -0.1487 -0.0924 509 MET A CE 3676 N N . PRO A 517 ? 0.4313 0.5278 0.6517 0.0515 -0.1271 -0.0846 510 PRO A N 3677 C CA . PRO A 517 ? 0.3981 0.4982 0.6184 0.0496 -0.1140 -0.0796 510 PRO A CA 3678 C C . PRO A 517 ? 0.3731 0.4722 0.5866 0.0425 -0.1004 -0.0749 510 PRO A C 3679 O O . PRO A 517 ? 0.3735 0.4661 0.5731 0.0406 -0.1007 -0.0740 510 PRO A O 3680 C CB . PRO A 517 ? 0.4047 0.4960 0.5996 0.0570 -0.1164 -0.0768 510 PRO A CB 3681 C CG . PRO A 517 ? 0.4306 0.5115 0.6039 0.0599 -0.1241 -0.0776 510 PRO A CG 3682 C CD . PRO A 517 ? 0.4441 0.5287 0.6356 0.0586 -0.1346 -0.0840 510 PRO A CD 3683 N N . ARG A 518 ? 0.3330 0.4379 0.5548 0.0390 -0.0886 -0.0720 511 ARG A N 3684 C CA . ARG A 518 ? 0.3204 0.4239 0.5338 0.0330 -0.0757 -0.0673 511 ARG A CA 3685 C C . ARG A 518 ? 0.3110 0.4047 0.4947 0.0354 -0.0728 -0.0630 511 ARG A C 3686 O O . ARG A 518 ? 0.2961 0.3868 0.4694 0.0403 -0.0734 -0.0616 511 ARG A O 3687 C CB . ARG A 518 ? 0.3250 0.4364 0.5531 0.0300 -0.0644 -0.0657 511 ARG A CB 3688 C CG . ARG A 518 ? 0.3505 0.4601 0.5691 0.0245 -0.0510 -0.0610 511 ARG A CG 3689 C CD . ARG A 518 ? 0.4279 0.5431 0.6549 0.0239 -0.0410 -0.0597 511 ARG A CD 3690 N NE . ARG A 518 ? 0.4699 0.5952 0.7255 0.0212 -0.0388 -0.0624 511 ARG A NE 3691 C CZ . ARG A 518 ? 0.5111 0.6401 0.7776 0.0148 -0.0294 -0.0610 511 ARG A CZ 3692 N NH1 . ARG A 518 ? 0.4627 0.5859 0.7129 0.0108 -0.0222 -0.0569 511 ARG A NH1 3693 N NH2 . ARG A 518 ? 0.4745 0.6130 0.7686 0.0125 -0.0271 -0.0633 511 ARG A NH2 3694 N N . ILE A 519 ? 0.2914 0.3802 0.4631 0.0319 -0.0694 -0.0608 512 ILE A N 3695 C CA . ILE A 519 ? 0.2904 0.3718 0.4379 0.0324 -0.0637 -0.0561 512 ILE A CA 3696 C C . ILE A 519 ? 0.2987 0.3816 0.4465 0.0256 -0.0523 -0.0528 512 ILE A C 3697 O O . ILE A 519 ? 0.3076 0.3918 0.4632 0.0211 -0.0513 -0.0533 512 ILE A O 3698 C CB . ILE A 519 ? 0.2989 0.3714 0.4272 0.0356 -0.0708 -0.0563 512 ILE A CB 3699 C CG1 . ILE A 519 ? 0.2878 0.3567 0.4107 0.0432 -0.0818 -0.0590 512 ILE A CG1 3700 C CG2 . ILE A 519 ? 0.2648 0.3310 0.3714 0.0351 -0.0632 -0.0512 512 ILE A CG2 3701 C CD1 . ILE A 519 ? 0.2936 0.3531 0.3970 0.0473 -0.0890 -0.0597 512 ILE A CD1 3702 N N . SER A 520 ? 0.2993 0.3814 0.4382 0.0251 -0.0440 -0.0493 513 SER A N 3703 C CA . SER A 520 ? 0.2953 0.3784 0.4334 0.0194 -0.0334 -0.0463 513 SER A CA 3704 C C . SER A 520 ? 0.3026 0.3786 0.4213 0.0184 -0.0317 -0.0431 513 SER A C 3705 O O . SER A 520 ? 0.2832 0.3537 0.3880 0.0223 -0.0367 -0.0428 513 SER A O 3706 C CB . SER A 520 ? 0.2938 0.3796 0.4331 0.0194 -0.0254 -0.0449 513 SER A CB 3707 O OG . SER A 520 ? 0.3125 0.4060 0.4728 0.0194 -0.0251 -0.0477 513 SER A OG 3708 N N . LYS A 521 ? 0.3051 0.3815 0.4233 0.0133 -0.0241 -0.0407 514 LYS A N 3709 C CA . LYS A 521 ? 0.3190 0.3896 0.4205 0.0118 -0.0211 -0.0374 514 LYS A CA 3710 C C . LYS A 521 ? 0.3337 0.4019 0.4224 0.0140 -0.0177 -0.0354 514 LYS A C 3711 O O . LYS A 521 ? 0.3332 0.4044 0.4268 0.0147 -0.0144 -0.0359 514 LYS A O 3712 C CB . LYS A 521 ? 0.3033 0.3750 0.4086 0.0062 -0.0135 -0.0352 514 LYS A CB 3713 C CG . LYS A 521 ? 0.3119 0.3851 0.4305 0.0033 -0.0163 -0.0367 514 LYS A CG 3714 C CD . LYS A 521 ? 0.3321 0.4038 0.4501 -0.0019 -0.0086 -0.0334 514 LYS A CD 3715 C CE . LYS A 521 ? 0.3172 0.3937 0.4448 -0.0047 0.0002 -0.0323 514 LYS A CE 3716 N NZ . LYS A 521 ? 0.3301 0.4126 0.4800 -0.0059 -0.0017 -0.0353 514 LYS A NZ 3717 N N . LEU A 522 ? 0.3131 0.3758 0.3862 0.0148 -0.0181 -0.0332 515 LEU A N 3718 C CA . LEU A 522 ? 0.3238 0.3841 0.3859 0.0155 -0.0139 -0.0310 515 LEU A CA 3719 C C . LEU A 522 ? 0.3410 0.4022 0.4021 0.0111 -0.0065 -0.0291 515 LEU A C 3720 O O . LEU A 522 ? 0.3619 0.4220 0.4215 0.0082 -0.0054 -0.0279 515 LEU A O 3721 C CB . LEU A 522 ? 0.2953 0.3500 0.3429 0.0177 -0.0164 -0.0292 515 LEU A CB 3722 C CG . LEU A 522 ? 0.2681 0.3201 0.3117 0.0231 -0.0225 -0.0302 515 LEU A CG 3723 C CD1 . LEU A 522 ? 0.2352 0.2817 0.2654 0.0248 -0.0242 -0.0284 515 LEU A CD1 3724 C CD2 . LEU A 522 ? 0.2356 0.2873 0.2782 0.0257 -0.0208 -0.0297 515 LEU A CD2 3725 N N . GLY A 523 ? 0.3562 0.4186 0.4176 0.0109 -0.0016 -0.0291 516 GLY A N 3726 C CA . GLY A 523 ? 0.3424 0.4039 0.3983 0.0076 0.0050 -0.0274 516 GLY A CA 3727 C C . GLY A 523 ? 0.3408 0.3982 0.3839 0.0087 0.0052 -0.0260 516 GLY A C 3728 O O . GLY A 523 ? 0.3498 0.4043 0.3861 0.0099 0.0014 -0.0249 516 GLY A O 3729 N N . SER A 524 ? 0.3200 0.3768 0.3599 0.0081 0.0098 -0.0262 517 SER A N 3730 C CA . SER A 524 ? 0.2822 0.3354 0.3128 0.0092 0.0094 -0.0254 517 SER A CA 3731 C C . SER A 524 ? 0.2525 0.3056 0.2849 0.0105 0.0122 -0.0272 517 SER A C 3732 O O . SER A 524 ? 0.2529 0.3090 0.2946 0.0120 0.0127 -0.0290 517 SER A O 3733 C CB . SER A 524 ? 0.2776 0.3282 0.2990 0.0066 0.0109 -0.0237 517 SER A CB 3734 O OG . SER A 524 ? 0.3432 0.3908 0.3576 0.0070 0.0109 -0.0234 517 SER A OG 3735 N N . GLY A 525 ? 0.2104 0.2602 0.2352 0.0101 0.0137 -0.0270 518 GLY A N 3736 C CA . GLY A 525 ? 0.2150 0.2636 0.2412 0.0116 0.0159 -0.0289 518 GLY A CA 3737 C C . GLY A 525 ? 0.2106 0.2570 0.2376 0.0149 0.0123 -0.0284 518 GLY A C 3738 O O . GLY A 525 ? 0.2139 0.2595 0.2445 0.0170 0.0132 -0.0299 518 GLY A O 3739 N N . ASN A 526 ? 0.2033 0.2482 0.2266 0.0157 0.0086 -0.0262 519 ASN A N 3740 C CA . ASN A 526 ? 0.2185 0.2600 0.2399 0.0189 0.0062 -0.0249 519 ASN A CA 3741 C C . ASN A 526 ? 0.2072 0.2464 0.2218 0.0188 0.0042 -0.0222 519 ASN A C 3742 O O . ASN A 526 ? 0.1910 0.2317 0.2034 0.0164 0.0042 -0.0217 519 ASN A O 3743 C CB . ASN A 526 ? 0.2193 0.2620 0.2469 0.0227 0.0032 -0.0257 519 ASN A CB 3744 C CG . ASN A 526 ? 0.2415 0.2802 0.2690 0.0258 0.0032 -0.0255 519 ASN A CG 3745 O OD1 . ASN A 526 ? 0.2334 0.2675 0.2548 0.0273 0.0023 -0.0230 519 ASN A OD1 3746 N ND2 . ASN A 526 ? 0.2207 0.2610 0.2553 0.0269 0.0048 -0.0279 519 ASN A ND2 3747 N N . ASP A 527 ? 0.1871 0.2224 0.1985 0.0217 0.0029 -0.0202 520 ASP A N 3748 C CA . ASP A 527 ? 0.2126 0.2453 0.2179 0.0212 0.0032 -0.0175 520 ASP A CA 3749 C C . ASP A 527 ? 0.2066 0.2401 0.2087 0.0222 0.0005 -0.0164 520 ASP A C 3750 O O . ASP A 527 ? 0.2114 0.2437 0.2094 0.0217 0.0011 -0.0145 520 ASP A O 3751 C CB . ASP A 527 ? 0.1993 0.2267 0.2021 0.0239 0.0039 -0.0153 520 ASP A CB 3752 C CG . ASP A 527 ? 0.2330 0.2585 0.2381 0.0217 0.0070 -0.0161 520 ASP A CG 3753 O OD1 . ASP A 527 ? 0.2208 0.2478 0.2261 0.0181 0.0083 -0.0170 520 ASP A OD1 3754 O OD2 . ASP A 527 ? 0.2387 0.2608 0.2453 0.0240 0.0075 -0.0160 520 ASP A OD2 3755 N N . PHE A 528 ? 0.2055 0.2412 0.2105 0.0235 -0.0023 -0.0179 521 PHE A N 3756 C CA . PHE A 528 ? 0.2278 0.2637 0.2299 0.0242 -0.0052 -0.0175 521 PHE A CA 3757 C C . PHE A 528 ? 0.2174 0.2560 0.2199 0.0201 -0.0038 -0.0177 521 PHE A C 3758 O O . PHE A 528 ? 0.2088 0.2472 0.2089 0.0204 -0.0057 -0.0172 521 PHE A O 3759 C CB . PHE A 528 ? 0.2348 0.2723 0.2414 0.0267 -0.0096 -0.0197 521 PHE A CB 3760 C CG . PHE A 528 ? 0.2445 0.2868 0.2605 0.0239 -0.0086 -0.0221 521 PHE A CG 3761 C CD1 . PHE A 528 ? 0.2686 0.3137 0.2875 0.0204 -0.0078 -0.0227 521 PHE A CD1 3762 C CD2 . PHE A 528 ? 0.2300 0.2737 0.2521 0.0249 -0.0077 -0.0235 521 PHE A CD2 3763 C CE1 . PHE A 528 ? 0.2253 0.2745 0.2528 0.0178 -0.0055 -0.0244 521 PHE A CE1 3764 C CE2 . PHE A 528 ? 0.2406 0.2890 0.2720 0.0224 -0.0055 -0.0257 521 PHE A CE2 3765 C CZ . PHE A 528 ? 0.2292 0.2802 0.2629 0.0188 -0.0040 -0.0259 521 PHE A CZ 3766 N N . GLU A 529 ? 0.1911 0.2315 0.1960 0.0168 -0.0007 -0.0184 522 GLU A N 3767 C CA . GLU A 529 ? 0.2087 0.2509 0.2134 0.0134 0.0001 -0.0185 522 GLU A CA 3768 C C . GLU A 529 ? 0.2092 0.2500 0.2087 0.0130 -0.0006 -0.0165 522 GLU A C 3769 O O . GLU A 529 ? 0.2014 0.2426 0.2003 0.0124 -0.0021 -0.0162 522 GLU A O 3770 C CB . GLU A 529 ? 0.1966 0.2395 0.2017 0.0104 0.0036 -0.0194 522 GLU A CB 3771 C CG . GLU A 529 ? 0.2364 0.2803 0.2397 0.0074 0.0047 -0.0191 522 GLU A CG 3772 C CD . GLU A 529 ? 0.2433 0.2865 0.2437 0.0051 0.0078 -0.0200 522 GLU A CD 3773 O OE1 . GLU A 529 ? 0.3150 0.3564 0.3117 0.0048 0.0077 -0.0200 522 GLU A OE1 3774 O OE2 . GLU A 529 ? 0.3038 0.3479 0.3054 0.0038 0.0106 -0.0210 522 GLU A OE2 3775 N N . VAL A 530 ? 0.1961 0.2352 0.1929 0.0134 0.0005 -0.0152 523 VAL A N 3776 C CA . VAL A 530 ? 0.1866 0.2253 0.1804 0.0131 0.0002 -0.0135 523 VAL A CA 3777 C C . VAL A 530 ? 0.2174 0.2548 0.2087 0.0162 -0.0018 -0.0126 523 VAL A C 3778 O O . VAL A 530 ? 0.2139 0.2514 0.2035 0.0161 -0.0028 -0.0120 523 VAL A O 3779 C CB . VAL A 530 ? 0.2178 0.2555 0.2116 0.0127 0.0021 -0.0123 523 VAL A CB 3780 C CG1 . VAL A 530 ? 0.1785 0.2133 0.1716 0.0160 0.0032 -0.0110 523 VAL A CG1 3781 C CG2 . VAL A 530 ? 0.1891 0.2276 0.1821 0.0119 0.0018 -0.0109 523 VAL A CG2 3782 N N . PHE A 531 ? 0.2173 0.2528 0.2075 0.0195 -0.0027 -0.0128 524 PHE A N 3783 C CA . PHE A 531 ? 0.2167 0.2499 0.2026 0.0232 -0.0050 -0.0124 524 PHE A CA 3784 C C . PHE A 531 ? 0.2190 0.2532 0.2065 0.0228 -0.0084 -0.0143 524 PHE A C 3785 O O . PHE A 531 ? 0.2279 0.2605 0.2121 0.0243 -0.0101 -0.0142 524 PHE A O 3786 C CB . PHE A 531 ? 0.2194 0.2495 0.2024 0.0273 -0.0059 -0.0121 524 PHE A CB 3787 C CG . PHE A 531 ? 0.2240 0.2518 0.2052 0.0278 -0.0021 -0.0096 524 PHE A CG 3788 C CD1 . PHE A 531 ? 0.2504 0.2759 0.2269 0.0295 0.0003 -0.0070 524 PHE A CD1 3789 C CD2 . PHE A 531 ? 0.2536 0.2819 0.2389 0.0262 -0.0005 -0.0099 524 PHE A CD2 3790 C CE1 . PHE A 531 ? 0.2974 0.3209 0.2742 0.0294 0.0046 -0.0043 524 PHE A CE1 3791 C CE2 . PHE A 531 ? 0.2003 0.2261 0.1853 0.0262 0.0031 -0.0076 524 PHE A CE2 3792 C CZ . PHE A 531 ? 0.2754 0.2988 0.2567 0.0276 0.0056 -0.0048 524 PHE A CZ 3793 N N . PHE A 532 ? 0.2063 0.2428 0.1996 0.0209 -0.0092 -0.0161 525 PHE A N 3794 C CA . PHE A 532 ? 0.2116 0.2492 0.2088 0.0201 -0.0123 -0.0180 525 PHE A CA 3795 C C . PHE A 532 ? 0.2151 0.2541 0.2142 0.0160 -0.0106 -0.0174 525 PHE A C 3796 O O . PHE A 532 ? 0.2091 0.2466 0.2066 0.0162 -0.0124 -0.0172 525 PHE A O 3797 C CB . PHE A 532 ? 0.1900 0.2299 0.1946 0.0202 -0.0135 -0.0202 525 PHE A CB 3798 C CG . PHE A 532 ? 0.2106 0.2515 0.2212 0.0198 -0.0172 -0.0224 525 PHE A CG 3799 C CD1 . PHE A 532 ? 0.2168 0.2547 0.2240 0.0232 -0.0222 -0.0236 525 PHE A CD1 3800 C CD2 . PHE A 532 ? 0.2246 0.2690 0.2442 0.0161 -0.0155 -0.0233 525 PHE A CD2 3801 C CE1 . PHE A 532 ? 0.2441 0.2826 0.2580 0.0227 -0.0266 -0.0263 525 PHE A CE1 3802 C CE2 . PHE A 532 ? 0.2390 0.2845 0.2666 0.0154 -0.0190 -0.0255 525 PHE A CE2 3803 C CZ . PHE A 532 ? 0.2094 0.2519 0.2344 0.0186 -0.0250 -0.0272 525 PHE A CZ 3804 N N . GLN A 533 ? 0.2016 0.2427 0.2030 0.0129 -0.0073 -0.0170 526 GLN A N 3805 C CA . GLN A 533 ? 0.2001 0.2416 0.2021 0.0094 -0.0057 -0.0163 526 GLN A CA 3806 C C . GLN A 533 ? 0.2001 0.2400 0.1962 0.0091 -0.0055 -0.0143 526 GLN A C 3807 O O . GLN A 533 ? 0.2137 0.2526 0.2089 0.0076 -0.0059 -0.0134 526 GLN A O 3808 C CB A GLN A 533 ? 0.2032 0.2465 0.2071 0.0070 -0.0019 -0.0166 526 GLN A CB 3809 C CB B GLN A 533 ? 0.1935 0.2369 0.1987 0.0066 -0.0021 -0.0167 526 GLN A CB 3810 C CG A GLN A 533 ? 0.2399 0.2856 0.2511 0.0075 -0.0013 -0.0187 526 GLN A CG 3811 C CG B GLN A 533 ? 0.1535 0.1992 0.1673 0.0062 -0.0021 -0.0185 526 GLN A CG 3812 C CD A GLN A 533 ? 0.2318 0.2789 0.2502 0.0063 -0.0022 -0.0195 526 GLN A CD 3813 C CD B GLN A 533 ? 0.1113 0.1586 0.1284 0.0085 -0.0022 -0.0202 526 GLN A CD 3814 O OE1 A GLN A 533 ? 0.2694 0.3148 0.2862 0.0053 -0.0034 -0.0185 526 GLN A OE1 3815 O OE1 B GLN A 533 ? 0.0889 0.1347 0.1013 0.0107 -0.0030 -0.0197 526 GLN A OE1 3816 N NE2 A GLN A 533 ? 0.2074 0.2574 0.2347 0.0066 -0.0020 -0.0215 526 GLN A NE2 3817 N NE2 B GLN A 533 ? 0.0503 0.1006 0.0764 0.0080 -0.0013 -0.0219 526 GLN A NE2 3818 N N . ARG A 534 ? 0.1874 0.2271 0.1806 0.0104 -0.0048 -0.0136 527 ARG A N 3819 C CA . ARG A 534 ? 0.1923 0.2314 0.1823 0.0103 -0.0049 -0.0120 527 ARG A CA 3820 C C . ARG A 534 ? 0.2058 0.2434 0.1940 0.0133 -0.0066 -0.0114 527 ARG A C 3821 O O . ARG A 534 ? 0.2030 0.2398 0.1900 0.0133 -0.0077 -0.0106 527 ARG A O 3822 C CB . ARG A 534 ? 0.1928 0.2327 0.1824 0.0095 -0.0031 -0.0115 527 ARG A CB 3823 C CG . ARG A 534 ? 0.1947 0.2349 0.1830 0.0087 -0.0039 -0.0103 527 ARG A CG 3824 C CD . ARG A 534 ? 0.1956 0.2369 0.1857 0.0084 -0.0029 -0.0100 527 ARG A CD 3825 N NE . ARG A 534 ? 0.1954 0.2367 0.1856 0.0062 -0.0020 -0.0114 527 ARG A NE 3826 C CZ . ARG A 534 ? 0.2087 0.2506 0.2007 0.0049 -0.0023 -0.0119 527 ARG A CZ 3827 N NH1 . ARG A 534 ? 0.1808 0.2241 0.1757 0.0054 -0.0033 -0.0107 527 ARG A NH1 3828 N NH2 . ARG A 534 ? 0.2045 0.2455 0.1957 0.0032 -0.0017 -0.0137 527 ARG A NH2 3829 N N . LEU A 535 ? 0.1967 0.2334 0.1838 0.0163 -0.0066 -0.0117 528 LEU A N 3830 C CA . LEU A 535 ? 0.1982 0.2328 0.1817 0.0199 -0.0073 -0.0111 528 LEU A CA 3831 C C . LEU A 535 ? 0.1972 0.2293 0.1787 0.0224 -0.0106 -0.0128 528 LEU A C 3832 O O . LEU A 535 ? 0.2236 0.2534 0.2013 0.0253 -0.0112 -0.0126 528 LEU A O 3833 C CB . LEU A 535 ? 0.1961 0.2297 0.1773 0.0224 -0.0048 -0.0097 528 LEU A CB 3834 C CG . LEU A 535 ? 0.2155 0.2513 0.1999 0.0200 -0.0018 -0.0083 528 LEU A CG 3835 C CD1 . LEU A 535 ? 0.2328 0.2668 0.2159 0.0223 0.0012 -0.0066 528 LEU A CD1 3836 C CD2 . LEU A 535 ? 0.2886 0.3260 0.2746 0.0190 -0.0017 -0.0074 528 LEU A CD2 3837 N N . GLY A 536 ? 0.1771 0.2096 0.1618 0.0216 -0.0127 -0.0146 529 GLY A N 3838 C CA . GLY A 536 ? 0.1935 0.2236 0.1780 0.0236 -0.0169 -0.0170 529 GLY A CA 3839 C C . GLY A 536 ? 0.2002 0.2272 0.1788 0.0287 -0.0189 -0.0179 529 GLY A C 3840 O O . GLY A 536 ? 0.1955 0.2189 0.1697 0.0319 -0.0221 -0.0194 529 GLY A O 3841 N N . ILE A 537 ? 0.2051 0.2324 0.1825 0.0299 -0.0171 -0.0169 530 ILE A N 3842 C CA . ILE A 537 ? 0.2144 0.2378 0.1849 0.0351 -0.0190 -0.0173 530 ILE A CA 3843 C C . ILE A 537 ? 0.2289 0.2532 0.2042 0.0356 -0.0234 -0.0199 530 ILE A C 3844 O O . ILE A 537 ? 0.2109 0.2388 0.1934 0.0326 -0.0220 -0.0200 530 ILE A O 3845 C CB . ILE A 537 ? 0.2116 0.2339 0.1780 0.0364 -0.0143 -0.0141 530 ILE A CB 3846 C CG1 . ILE A 537 ? 0.2348 0.2568 0.1984 0.0362 -0.0102 -0.0117 530 ILE A CG1 3847 C CG2 . ILE A 537 ? 0.2348 0.2521 0.1930 0.0419 -0.0159 -0.0139 530 ILE A CG2 3848 C CD1 . ILE A 537 ? 0.2490 0.2723 0.2144 0.0347 -0.0049 -0.0087 530 ILE A CD1 3849 N N . ALA A 538 ? 0.2169 0.2378 0.1885 0.0395 -0.0289 -0.0225 531 ALA A N 3850 C CA . ALA A 538 ? 0.2320 0.2540 0.2096 0.0403 -0.0343 -0.0256 531 ALA A CA 3851 C C . ALA A 538 ? 0.2465 0.2698 0.2258 0.0410 -0.0323 -0.0241 531 ALA A C 3852 O O . ALA A 538 ? 0.2507 0.2700 0.2207 0.0445 -0.0302 -0.0216 531 ALA A O 3853 C CB . ALA A 538 ? 0.2426 0.2589 0.2120 0.0461 -0.0410 -0.0284 531 ALA A CB 3854 N N . SER A 539 ? 0.2210 0.2493 0.2118 0.0378 -0.0325 -0.0254 532 SER A N 3855 C CA . SER A 539 ? 0.2213 0.2506 0.2140 0.0384 -0.0301 -0.0242 532 SER A CA 3856 C C . SER A 539 ? 0.2273 0.2593 0.2293 0.0397 -0.0350 -0.0272 532 SER A C 3857 O O . SER A 539 ? 0.2165 0.2518 0.2279 0.0379 -0.0385 -0.0302 532 SER A O 3858 C CB . SER A 539 ? 0.2260 0.2592 0.2237 0.0332 -0.0235 -0.0224 532 SER A CB 3859 O OG . SER A 539 ? 0.2257 0.2567 0.2159 0.0324 -0.0194 -0.0195 532 SER A OG 3860 N N . GLY A 540 ? 0.2291 0.2599 0.2302 0.0426 -0.0350 -0.0264 533 GLY A N 3861 C CA . GLY A 540 ? 0.2385 0.2727 0.2504 0.0439 -0.0391 -0.0293 533 GLY A CA 3862 C C . GLY A 540 ? 0.2448 0.2792 0.2586 0.0448 -0.0358 -0.0277 533 GLY A C 3863 O O . GLY A 540 ? 0.2284 0.2587 0.2333 0.0454 -0.0314 -0.0244 533 GLY A O 3864 N N . ARG A 541 ? 0.2295 0.2682 0.2556 0.0452 -0.0382 -0.0303 534 ARG A N 3865 C CA . ARG A 541 ? 0.2454 0.2838 0.2741 0.0471 -0.0362 -0.0295 534 ARG A CA 3866 C C . ARG A 541 ? 0.2360 0.2778 0.2762 0.0505 -0.0426 -0.0329 534 ARG A C 3867 O O . ARG A 541 ? 0.2338 0.2805 0.2843 0.0490 -0.0463 -0.0361 534 ARG A O 3868 C CB . ARG A 541 ? 0.2436 0.2861 0.2787 0.0419 -0.0282 -0.0289 534 ARG A CB 3869 C CG . ARG A 541 ? 0.2510 0.3013 0.3009 0.0376 -0.0268 -0.0319 534 ARG A CG 3870 C CD . ARG A 541 ? 0.2690 0.3214 0.3197 0.0323 -0.0184 -0.0308 534 ARG A CD 3871 N NE . ARG A 541 ? 0.2812 0.3315 0.3300 0.0333 -0.0145 -0.0300 534 ARG A NE 3872 C CZ . ARG A 541 ? 0.2882 0.3407 0.3407 0.0302 -0.0084 -0.0305 534 ARG A CZ 3873 N NH1 . ARG A 541 ? 0.2392 0.2888 0.2897 0.0316 -0.0058 -0.0302 534 ARG A NH1 3874 N NH2 . ARG A 541 ? 0.2500 0.3067 0.3073 0.0259 -0.0046 -0.0314 534 ARG A NH2 3875 N N . ALA A 542 ? 0.2338 0.2729 0.2735 0.0548 -0.0439 -0.0322 535 ALA A N 3876 C CA . ALA A 542 ? 0.2503 0.2924 0.3011 0.0590 -0.0509 -0.0354 535 ALA A CA 3877 C C . ALA A 542 ? 0.2404 0.2816 0.2943 0.0611 -0.0478 -0.0343 535 ALA A C 3878 O O . ALA A 542 ? 0.2571 0.2913 0.2986 0.0624 -0.0441 -0.0305 535 ALA A O 3879 C CB . ALA A 542 ? 0.2372 0.2729 0.2771 0.0655 -0.0601 -0.0356 535 ALA A CB 3880 N N . ARG A 543 ? 0.2440 0.2918 0.3147 0.0612 -0.0487 -0.0374 536 ARG A N 3881 C CA . ARG A 543 ? 0.2511 0.2978 0.3257 0.0639 -0.0462 -0.0368 536 ARG A CA 3882 C C . ARG A 543 ? 0.2536 0.3073 0.3468 0.0667 -0.0517 -0.0409 536 ARG A C 3883 O O . ARG A 543 ? 0.2532 0.3135 0.3575 0.0648 -0.0550 -0.0440 536 ARG A O 3884 C CB A ARG A 543 ? 0.2567 0.3055 0.3334 0.0584 -0.0357 -0.0360 536 ARG A CB 3885 C CB B ARG A 543 ? 0.2531 0.3018 0.3298 0.0584 -0.0357 -0.0360 536 ARG A CB 3886 C CG A ARG A 543 ? 0.2400 0.2972 0.3279 0.0521 -0.0309 -0.0383 536 ARG A CG 3887 C CG B ARG A 543 ? 0.2306 0.2890 0.3231 0.0533 -0.0314 -0.0391 536 ARG A CG 3888 C CD A ARG A 543 ? 0.3115 0.3667 0.3883 0.0474 -0.0279 -0.0362 536 ARG A CD 3889 C CD B ARG A 543 ? 0.2435 0.3019 0.3349 0.0494 -0.0218 -0.0384 536 ARG A CD 3890 N NE A ARG A 543 ? 0.3099 0.3706 0.3933 0.0413 -0.0212 -0.0372 536 ARG A NE 3891 N NE B ARG A 543 ? 0.2644 0.3154 0.3391 0.0480 -0.0191 -0.0349 536 ARG A NE 3892 C CZ A ARG A 543 ? 0.2613 0.3259 0.3490 0.0380 -0.0219 -0.0381 536 ARG A CZ 3893 C CZ B ARG A 543 ? 0.2514 0.3012 0.3213 0.0439 -0.0120 -0.0340 536 ARG A CZ 3894 N NH1 A ARG A 543 ? 0.2488 0.3125 0.3357 0.0402 -0.0296 -0.0388 536 ARG A NH1 3895 N NH1 B ARG A 543 ? 0.2100 0.2534 0.2667 0.0430 -0.0107 -0.0310 536 ARG A NH1 3896 N NH2 A ARG A 543 ? 0.1994 0.2677 0.2912 0.0328 -0.0152 -0.0382 536 ARG A NH2 3897 N NH2 B ARG A 543 ? 0.2896 0.3443 0.3680 0.0408 -0.0063 -0.0363 536 ARG A NH2 3898 N N . TYR A 544 ? 0.2588 0.3111 0.3563 0.0713 -0.0527 -0.0410 537 TYR A N 3899 C CA . TYR A 544 ? 0.2738 0.3345 0.3924 0.0733 -0.0561 -0.0452 537 TYR A CA 3900 C C . TYR A 544 ? 0.2712 0.3393 0.4030 0.0679 -0.0460 -0.0467 537 TYR A C 3901 O O . TYR A 544 ? 0.2610 0.3254 0.3842 0.0651 -0.0378 -0.0445 537 TYR A O 3902 C CB . TYR A 544 ? 0.2762 0.3320 0.3945 0.0813 -0.0622 -0.0448 537 TYR A CB 3903 C CG . TYR A 544 ? 0.2631 0.3209 0.3876 0.0865 -0.0746 -0.0476 537 TYR A CG 3904 C CD1 . TYR A 544 ? 0.2846 0.3362 0.3937 0.0887 -0.0818 -0.0466 537 TYR A CD1 3905 C CD2 . TYR A 544 ? 0.2517 0.3180 0.3985 0.0893 -0.0793 -0.0519 537 TYR A CD2 3906 C CE1 . TYR A 544 ? 0.2607 0.3136 0.3750 0.0937 -0.0943 -0.0500 537 TYR A CE1 3907 C CE2 . TYR A 544 ? 0.2604 0.3288 0.4142 0.0940 -0.0919 -0.0551 537 TYR A CE2 3908 C CZ . TYR A 544 ? 0.2780 0.3395 0.4150 0.0961 -0.0996 -0.0543 537 TYR A CZ 3909 O OH . TYR A 544 ? 0.2886 0.3516 0.4317 0.1010 -0.1128 -0.0581 537 TYR A OH 3910 N N . THR A 545 ? 0.2790 0.3573 0.4319 0.0666 -0.0466 -0.0506 538 THR A N 3911 C CA . THR A 545 ? 0.2790 0.3644 0.4440 0.0614 -0.0363 -0.0520 538 THR A CA 3912 C C . THR A 545 ? 0.2986 0.3933 0.4879 0.0637 -0.0368 -0.0559 538 THR A C 3913 O O . THR A 545 ? 0.2874 0.3836 0.4851 0.0692 -0.0463 -0.0578 538 THR A O 3914 C CB . THR A 545 ? 0.2805 0.3696 0.4458 0.0545 -0.0326 -0.0519 538 THR A CB 3915 O OG1 . THR A 545 ? 0.2986 0.3920 0.4698 0.0496 -0.0214 -0.0521 538 THR A OG1 3916 C CG2 . THR A 545 ? 0.2638 0.3599 0.4448 0.0543 -0.0396 -0.0549 538 THR A CG2 3917 N N . LYS A 546 ? 0.3127 0.4133 0.5123 0.0598 -0.0265 -0.0571 539 LYS A N 3918 C CA . LYS A 546 ? 0.3509 0.4615 0.5753 0.0609 -0.0240 -0.0608 539 LYS A CA 3919 C C . LYS A 546 ? 0.3582 0.4786 0.6016 0.0576 -0.0264 -0.0632 539 LYS A C 3920 O O . LYS A 546 ? 0.3570 0.4757 0.5931 0.0542 -0.0295 -0.0620 539 LYS A O 3921 C CB . LYS A 546 ? 0.3470 0.4589 0.5728 0.0584 -0.0109 -0.0610 539 LYS A CB 3922 C CG . LYS A 546 ? 0.4058 0.5166 0.6214 0.0512 -0.0013 -0.0591 539 LYS A CG 3923 C CD . LYS A 546 ? 0.5039 0.6051 0.6980 0.0506 0.0042 -0.0568 539 LYS A CD 3924 C CE . LYS A 546 ? 0.5237 0.6219 0.7033 0.0441 0.0104 -0.0544 539 LYS A CE 3925 N NZ . LYS A 546 ? 0.5301 0.6329 0.7157 0.0402 0.0219 -0.0554 539 LYS A NZ 3926 N N . ASN A 547 ? 0.3759 0.5063 0.6446 0.0586 -0.0246 -0.0665 540 ASN A N 3927 C CA . ASN A 547 ? 0.4032 0.5439 0.6938 0.0545 -0.0246 -0.0689 540 ASN A CA 3928 C C . ASN A 547 ? 0.4097 0.5520 0.6982 0.0468 -0.0119 -0.0670 540 ASN A C 3929 O O . ASN A 547 ? 0.4356 0.5760 0.7167 0.0454 -0.0007 -0.0656 540 ASN A O 3930 C CB . ASN A 547 ? 0.4098 0.5613 0.7299 0.0580 -0.0257 -0.0730 540 ASN A CB 3931 C CG . ASN A 547 ? 0.4404 0.6021 0.7856 0.0553 -0.0306 -0.0760 540 ASN A CG 3932 O OD1 . ASN A 547 ? 0.4699 0.6321 0.8136 0.0491 -0.0280 -0.0748 540 ASN A OD1 3933 N ND2 . ASN A 547 ? 0.4631 0.6330 0.8325 0.0600 -0.0382 -0.0800 540 ASN A ND2 3934 N N . ASN A 551 ? 0.5491 0.6769 0.7797 0.0234 0.0487 -0.0550 544 ASN A N 3935 C CA . ASN A 551 ? 0.5468 0.6657 0.7558 0.0259 0.0487 -0.0546 544 ASN A CA 3936 C C . ASN A 551 ? 0.5221 0.6331 0.7121 0.0260 0.0393 -0.0525 544 ASN A C 3937 O O . ASN A 551 ? 0.5189 0.6229 0.6939 0.0283 0.0382 -0.0523 544 ASN A O 3938 C CB . ASN A 551 ? 0.5609 0.6815 0.7785 0.0317 0.0477 -0.0577 544 ASN A CB 3939 C CG . ASN A 551 ? 0.6054 0.7285 0.8286 0.0322 0.0602 -0.0595 544 ASN A CG 3940 O OD1 . ASN A 551 ? 0.6632 0.7939 0.9028 0.0301 0.0675 -0.0600 544 ASN A OD1 3941 N ND2 . ASN A 551 ? 0.5859 0.7022 0.7956 0.0351 0.0630 -0.0606 544 ASN A ND2 3942 N N . LYS A 552 ? 0.4925 0.6044 0.6841 0.0237 0.0329 -0.0511 545 LYS A N 3943 C CA . LYS A 552 ? 0.4752 0.5804 0.6511 0.0245 0.0238 -0.0493 545 LYS A CA 3944 C C . LYS A 552 ? 0.4594 0.5558 0.6114 0.0229 0.0267 -0.0468 545 LYS A C 3945 O O . LYS A 552 ? 0.4583 0.5487 0.5980 0.0253 0.0208 -0.0458 545 LYS A O 3946 C CB . LYS A 552 ? 0.4782 0.5860 0.6605 0.0220 0.0177 -0.0487 545 LYS A CB 3947 C CG . LYS A 552 ? 0.4869 0.5879 0.6508 0.0193 0.0151 -0.0457 545 LYS A CG 3948 C CD . LYS A 552 ? 0.5142 0.6177 0.6866 0.0175 0.0084 -0.0461 545 LYS A CD 3949 C CE . LYS A 552 ? 0.4905 0.5868 0.6443 0.0161 0.0046 -0.0434 545 LYS A CE 3950 N NZ . LYS A 552 ? 0.4998 0.5970 0.6596 0.0149 -0.0021 -0.0441 545 LYS A NZ 3951 N N . PHE A 553 ? 0.4284 0.5236 0.5741 0.0193 0.0357 -0.0456 546 PHE A N 3952 C CA . PHE A 553 ? 0.4243 0.5116 0.5488 0.0178 0.0379 -0.0437 546 PHE A CA 3953 C C . PHE A 553 ? 0.4231 0.5071 0.5413 0.0198 0.0436 -0.0455 546 PHE A C 3954 O O . PHE A 553 ? 0.4344 0.5120 0.5362 0.0187 0.0451 -0.0446 546 PHE A O 3955 C CB . PHE A 553 ? 0.4180 0.5039 0.5349 0.0129 0.0429 -0.0412 546 PHE A CB 3956 C CG . PHE A 553 ? 0.4121 0.4999 0.5336 0.0106 0.0376 -0.0394 546 PHE A CG 3957 C CD1 . PHE A 553 ? 0.4386 0.5312 0.5724 0.0074 0.0420 -0.0388 546 PHE A CD1 3958 C CD2 . PHE A 553 ? 0.4181 0.5025 0.5322 0.0117 0.0287 -0.0385 546 PHE A CD2 3959 C CE1 . PHE A 553 ? 0.4216 0.5152 0.5602 0.0051 0.0370 -0.0376 546 PHE A CE1 3960 C CE2 . PHE A 553 ? 0.3989 0.4843 0.5164 0.0099 0.0238 -0.0374 546 PHE A CE2 3961 C CZ . PHE A 553 ? 0.4060 0.4958 0.5360 0.0066 0.0275 -0.0372 546 PHE A CZ 3962 N N . SER A 554 ? 0.4058 0.4942 0.5375 0.0229 0.0463 -0.0483 547 SER A N 3963 C CA . SER A 554 ? 0.4075 0.4927 0.5344 0.0249 0.0527 -0.0506 547 SER A CA 3964 C C . SER A 554 ? 0.4050 0.4841 0.5245 0.0286 0.0473 -0.0515 547 SER A C 3965 O O . SER A 554 ? 0.4189 0.4920 0.5271 0.0291 0.0509 -0.0527 547 SER A O 3966 C CB . SER A 554 ? 0.4108 0.5033 0.5559 0.0267 0.0593 -0.0532 547 SER A CB 3967 O OG . SER A 554 ? 0.4124 0.5093 0.5631 0.0229 0.0660 -0.0519 547 SER A OG 3968 N N . GLY A 555 ? 0.3809 0.4608 0.5060 0.0311 0.0386 -0.0508 548 GLY A N 3969 C CA . GLY A 555 ? 0.3619 0.4365 0.4831 0.0353 0.0335 -0.0511 548 GLY A CA 3970 C C . GLY A 555 ? 0.3455 0.4242 0.4827 0.0401 0.0337 -0.0541 548 GLY A C 3971 O O . GLY A 555 ? 0.3487 0.4340 0.4990 0.0400 0.0400 -0.0564 548 GLY A O 3972 N N . TYR A 556 ? 0.3046 0.3793 0.4415 0.0445 0.0271 -0.0538 549 TYR A N 3973 C CA . TYR A 556 ? 0.2837 0.3607 0.4343 0.0500 0.0260 -0.0563 549 TYR A CA 3974 C C . TYR A 556 ? 0.2664 0.3392 0.4133 0.0509 0.0339 -0.0589 549 TYR A C 3975 O O . TYR A 556 ? 0.2770 0.3442 0.4093 0.0476 0.0380 -0.0585 549 TYR A O 3976 C CB . TYR A 556 ? 0.2788 0.3509 0.4266 0.0546 0.0162 -0.0544 549 TYR A CB 3977 C CG . TYR A 556 ? 0.2752 0.3371 0.4035 0.0531 0.0149 -0.0514 549 TYR A CG 3978 C CD1 . TYR A 556 ? 0.2649 0.3188 0.3863 0.0550 0.0171 -0.0518 549 TYR A CD1 3979 C CD2 . TYR A 556 ? 0.2419 0.3023 0.3597 0.0497 0.0118 -0.0483 549 TYR A CD2 3980 C CE1 . TYR A 556 ? 0.2619 0.3069 0.3672 0.0530 0.0163 -0.0489 549 TYR A CE1 3981 C CE2 . TYR A 556 ? 0.2282 0.2804 0.3303 0.0483 0.0113 -0.0456 549 TYR A CE2 3982 C CZ . TYR A 556 ? 0.2133 0.2580 0.3098 0.0498 0.0136 -0.0458 549 TYR A CZ 3983 O OH . TYR A 556 ? 0.2324 0.2696 0.3150 0.0476 0.0131 -0.0430 549 TYR A OH 3984 N N . PRO A 557 ? 0.2536 0.3293 0.4140 0.0554 0.0359 -0.0620 550 PRO A N 3985 C CA . PRO A 557 ? 0.2627 0.3351 0.4198 0.0559 0.0447 -0.0651 550 PRO A CA 3986 C C . PRO A 557 ? 0.2656 0.3263 0.4043 0.0554 0.0444 -0.0647 550 PRO A C 3987 O O . PRO A 557 ? 0.2792 0.3362 0.4081 0.0529 0.0511 -0.0665 550 PRO A O 3988 C CB . PRO A 557 ? 0.2499 0.3267 0.4254 0.0619 0.0450 -0.0682 550 PRO A CB 3989 C CG . PRO A 557 ? 0.2554 0.3430 0.4484 0.0620 0.0402 -0.0675 550 PRO A CG 3990 C CD . PRO A 557 ? 0.2432 0.3267 0.4239 0.0598 0.0315 -0.0634 550 PRO A CD 3991 N N . LEU A 558 ? 0.2622 0.3166 0.3964 0.0577 0.0369 -0.0624 551 LEU A N 3992 C CA . LEU A 558 ? 0.2686 0.3118 0.3886 0.0574 0.0367 -0.0620 551 LEU A CA 3993 C C . LEU A 558 ? 0.2650 0.3037 0.3693 0.0523 0.0347 -0.0587 551 LEU A C 3994 O O . LEU A 558 ? 0.2666 0.2965 0.3609 0.0517 0.0334 -0.0578 551 LEU A O 3995 C CB . LEU A 558 ? 0.2574 0.2947 0.3809 0.0630 0.0312 -0.0611 551 LEU A CB 3996 C CG . LEU A 558 ? 0.2619 0.3029 0.4007 0.0682 0.0341 -0.0651 551 LEU A CG 3997 C CD1 . LEU A 558 ? 0.2745 0.3104 0.4183 0.0745 0.0277 -0.0639 551 LEU A CD1 3998 C CD2 . LEU A 558 ? 0.2194 0.2570 0.3552 0.0678 0.0427 -0.0698 551 LEU A CD2 3999 N N . TYR A 559 ? 0.2594 0.3043 0.3630 0.0486 0.0348 -0.0571 552 TYR A N 4000 C CA . TYR A 559 ? 0.2448 0.2871 0.3356 0.0440 0.0328 -0.0540 552 TYR A CA 4001 C C . TYR A 559 ? 0.2467 0.2818 0.3246 0.0411 0.0363 -0.0553 552 TYR A C 4002 O O . TYR A 559 ? 0.2631 0.2989 0.3395 0.0400 0.0424 -0.0587 552 TYR A O 4003 C CB . TYR A 559 ? 0.2398 0.2902 0.3339 0.0407 0.0345 -0.0534 552 TYR A CB 4004 C CG . TYR A 559 ? 0.2521 0.3008 0.3339 0.0359 0.0334 -0.0506 552 TYR A CG 4005 C CD1 . TYR A 559 ? 0.2436 0.2890 0.3193 0.0356 0.0272 -0.0471 552 TYR A CD1 4006 C CD2 . TYR A 559 ? 0.2465 0.2967 0.3229 0.0321 0.0389 -0.0514 552 TYR A CD2 4007 C CE1 . TYR A 559 ? 0.2514 0.2956 0.3168 0.0315 0.0264 -0.0447 552 TYR A CE1 4008 C CE2 . TYR A 559 ? 0.2330 0.2817 0.2985 0.0279 0.0374 -0.0488 552 TYR A CE2 4009 C CZ . TYR A 559 ? 0.2313 0.2775 0.2926 0.0277 0.0312 -0.0457 552 TYR A CZ 4010 O OH . TYR A 559 ? 0.2334 0.2786 0.2854 0.0241 0.0300 -0.0435 552 TYR A OH 4011 N N . HIS A 560 ? 0.2414 0.2695 0.3106 0.0400 0.0325 -0.0530 553 HIS A N 4012 C CA . HIS A 560 ? 0.2505 0.2717 0.3083 0.0368 0.0343 -0.0542 553 HIS A CA 4013 C C . HIS A 560 ? 0.2650 0.2807 0.3230 0.0388 0.0380 -0.0589 553 HIS A C 4014 O O . HIS A 560 ? 0.2638 0.2748 0.3130 0.0363 0.0402 -0.0616 553 HIS A O 4015 C CB . HIS A 560 ? 0.2349 0.2590 0.2848 0.0322 0.0365 -0.0542 553 HIS A CB 4016 C CG . HIS A 560 ? 0.2460 0.2725 0.2923 0.0295 0.0324 -0.0498 553 HIS A CG 4017 N ND1 . HIS A 560 ? 0.2160 0.2446 0.2553 0.0256 0.0334 -0.0491 553 HIS A ND1 4018 C CD2 . HIS A 560 ? 0.2361 0.2626 0.2842 0.0307 0.0274 -0.0459 553 HIS A CD2 4019 C CE1 . HIS A 560 ? 0.2428 0.2729 0.2806 0.0243 0.0292 -0.0452 553 HIS A CE1 4020 N NE2 . HIS A 560 ? 0.2128 0.2417 0.2555 0.0273 0.0258 -0.0433 553 HIS A NE2 4021 N N . SER A 561 ? 0.2741 0.2900 0.3419 0.0436 0.0381 -0.0600 554 SER A N 4022 C CA . SER A 561 ? 0.2610 0.2711 0.3305 0.0465 0.0411 -0.0643 554 SER A CA 4023 C C . SER A 561 ? 0.3021 0.3031 0.3718 0.0488 0.0369 -0.0626 554 SER A C 4024 O O . SER A 561 ? 0.2858 0.2865 0.3565 0.0496 0.0323 -0.0579 554 SER A O 4025 C CB . SER A 561 ? 0.2689 0.2851 0.3506 0.0508 0.0449 -0.0673 554 SER A CB 4026 O OG A SER A 561 ? 0.2377 0.2563 0.3303 0.0551 0.0404 -0.0648 554 SER A OG 4027 O OG B SER A 561 ? 0.2674 0.2775 0.3530 0.0550 0.0464 -0.0707 554 SER A OG 4028 N N . VAL A 562 ? 0.2707 0.2637 0.3387 0.0500 0.0390 -0.0665 555 VAL A N 4029 C CA . VAL A 562 ? 0.2975 0.2810 0.3668 0.0523 0.0361 -0.0651 555 VAL A CA 4030 C C . VAL A 562 ? 0.2981 0.2832 0.3775 0.0582 0.0333 -0.0624 555 VAL A C 4031 O O . VAL A 562 ? 0.3126 0.2903 0.3921 0.0603 0.0299 -0.0590 555 VAL A O 4032 C CB . VAL A 562 ? 0.3064 0.2814 0.3739 0.0532 0.0392 -0.0709 555 VAL A CB 4033 C CG1 . VAL A 562 ? 0.3087 0.2870 0.3850 0.0585 0.0434 -0.0755 555 VAL A CG1 4034 C CG2 . VAL A 562 ? 0.2881 0.2512 0.3555 0.0539 0.0361 -0.0691 555 VAL A CG2 4035 N N . TYR A 563 ? 0.2860 0.2804 0.3740 0.0608 0.0348 -0.0640 556 TYR A N 4036 C CA . TYR A 563 ? 0.2912 0.2883 0.3909 0.0670 0.0321 -0.0630 556 TYR A CA 4037 C C . TYR A 563 ? 0.2872 0.2880 0.3872 0.0674 0.0260 -0.0574 556 TYR A C 4038 O O . TYR A 563 ? 0.2847 0.2862 0.3924 0.0728 0.0217 -0.0558 556 TYR A O 4039 C CB . TYR A 563 ? 0.2746 0.2807 0.3860 0.0697 0.0365 -0.0676 556 TYR A CB 4040 C CG . TYR A 563 ? 0.2930 0.2947 0.4029 0.0701 0.0431 -0.0735 556 TYR A CG 4041 C CD1 . TYR A 563 ? 0.3061 0.2975 0.4163 0.0736 0.0427 -0.0753 556 TYR A CD1 4042 C CD2 . TYR A 563 ? 0.2796 0.2864 0.3869 0.0673 0.0496 -0.0772 556 TYR A CD2 4043 C CE1 . TYR A 563 ? 0.3089 0.2952 0.4166 0.0742 0.0482 -0.0812 556 TYR A CE1 4044 C CE2 . TYR A 563 ? 0.3225 0.3242 0.4262 0.0682 0.0556 -0.0830 556 TYR A CE2 4045 C CZ . TYR A 563 ? 0.3260 0.3174 0.4297 0.0715 0.0546 -0.0852 556 TYR A CZ 4046 O OH . TYR A 563 ? 0.3444 0.3299 0.4438 0.0727 0.0601 -0.0915 556 TYR A OH 4047 N N . GLU A 564 ? 0.2788 0.2810 0.3698 0.0623 0.0251 -0.0546 557 GLU A N 4048 C CA . GLU A 564 ? 0.2872 0.2918 0.3764 0.0627 0.0194 -0.0495 557 GLU A CA 4049 C C . GLU A 564 ? 0.2861 0.2799 0.3686 0.0646 0.0159 -0.0449 557 GLU A C 4050 O O . GLU A 564 ? 0.3011 0.2895 0.3743 0.0606 0.0166 -0.0426 557 GLU A O 4051 C CB . GLU A 564 ? 0.2894 0.2992 0.3717 0.0568 0.0202 -0.0483 557 GLU A CB 4052 C CG . GLU A 564 ? 0.3323 0.3479 0.4159 0.0574 0.0153 -0.0451 557 GLU A CG 4053 C CD . GLU A 564 ? 0.2619 0.2793 0.3364 0.0517 0.0160 -0.0433 557 GLU A CD 4054 O OE1 . GLU A 564 ? 0.3104 0.3335 0.3855 0.0480 0.0199 -0.0458 557 GLU A OE1 4055 O OE2 . GLU A 564 ? 0.3195 0.3316 0.3860 0.0512 0.0133 -0.0393 557 GLU A OE2 4056 N N . THR A 565 ? 0.2888 0.2791 0.3764 0.0708 0.0124 -0.0436 558 THR A N 4057 C CA . THR A 565 ? 0.2951 0.2733 0.3768 0.0735 0.0102 -0.0393 558 THR A CA 4058 C C . THR A 565 ? 0.2912 0.2685 0.3710 0.0785 0.0036 -0.0344 558 THR A C 4059 O O . THR A 565 ? 0.2816 0.2677 0.3672 0.0806 0.0000 -0.0353 558 THR A O 4060 C CB . THR A 565 ? 0.3048 0.2765 0.3931 0.0777 0.0119 -0.0422 558 THR A CB 4061 O OG1 . THR A 565 ? 0.3208 0.2995 0.4210 0.0832 0.0098 -0.0449 558 THR A OG1 4062 C CG2 . THR A 565 ? 0.3053 0.2754 0.3935 0.0735 0.0181 -0.0476 558 THR A CG2 4063 N N . TYR A 566 ? 0.2960 0.2619 0.3678 0.0807 0.0020 -0.0292 559 TYR A N 4064 C CA . TYR A 566 ? 0.3113 0.2736 0.3803 0.0873 -0.0043 -0.0247 559 TYR A CA 4065 C C . TYR A 566 ? 0.3213 0.2881 0.4026 0.0940 -0.0085 -0.0279 559 TYR A C 4066 O O . TYR A 566 ? 0.3222 0.2940 0.4056 0.0981 -0.0149 -0.0272 559 TYR A O 4067 C CB . TYR A 566 ? 0.3219 0.2695 0.3816 0.0894 -0.0039 -0.0188 559 TYR A CB 4068 C CG . TYR A 566 ? 0.3497 0.2913 0.4046 0.0973 -0.0104 -0.0140 559 TYR A CG 4069 C CD1 . TYR A 566 ? 0.3846 0.3263 0.4287 0.0984 -0.0142 -0.0096 559 TYR A CD1 4070 C CD2 . TYR A 566 ? 0.3934 0.3289 0.4537 0.1042 -0.0131 -0.0141 559 TYR A CD2 4071 C CE1 . TYR A 566 ? 0.3961 0.3314 0.4337 0.1061 -0.0207 -0.0054 559 TYR A CE1 4072 C CE2 . TYR A 566 ? 0.4209 0.3505 0.4758 0.1122 -0.0201 -0.0097 559 TYR A CE2 4073 C CZ . TYR A 566 ? 0.4095 0.3389 0.4523 0.1131 -0.0239 -0.0054 559 TYR A CZ 4074 O OH . TYR A 566 ? 0.4196 0.3421 0.4547 0.1213 -0.0312 -0.0011 559 TYR A OH 4075 N N . GLU A 567 ? 0.3119 0.2768 0.4019 0.0955 -0.0053 -0.0317 560 GLU A N 4076 C CA . GLU A 567 ? 0.3211 0.2900 0.4246 0.1023 -0.0087 -0.0350 560 GLU A CA 4077 C C . GLU A 567 ? 0.3046 0.2887 0.4196 0.1015 -0.0098 -0.0394 560 GLU A C 4078 O O . GLU A 567 ? 0.3073 0.2963 0.4320 0.1074 -0.0157 -0.0403 560 GLU A O 4079 C CB . GLU A 567 ? 0.3361 0.3000 0.4468 0.1039 -0.0039 -0.0389 560 GLU A CB 4080 C CG . GLU A 567 ? 0.3472 0.2949 0.4501 0.1064 -0.0039 -0.0345 560 GLU A CG 4081 C CD . GLU A 567 ? 0.3880 0.3284 0.4783 0.0995 0.0003 -0.0314 560 GLU A CD 4082 O OE1 . GLU A 567 ? 0.3639 0.3102 0.4540 0.0929 0.0049 -0.0350 560 GLU A OE1 4083 O OE2 . GLU A 567 ? 0.3962 0.3248 0.4772 0.1008 -0.0008 -0.0253 560 GLU A OE2 4084 N N . LEU A 568 ? 0.2758 0.2672 0.3907 0.0945 -0.0042 -0.0422 561 LEU A N 4085 C CA . LEU A 568 ? 0.2787 0.2841 0.4038 0.0926 -0.0041 -0.0457 561 LEU A CA 4086 C C . LEU A 568 ? 0.2841 0.2929 0.4080 0.0952 -0.0126 -0.0427 561 LEU A C 4087 O O . LEU A 568 ? 0.2827 0.3005 0.4200 0.0985 -0.0169 -0.0452 561 LEU A O 4088 C CB . LEU A 568 ? 0.2779 0.2876 0.3972 0.0844 0.0021 -0.0471 561 LEU A CB 4089 C CG . LEU A 568 ? 0.2617 0.2849 0.3904 0.0818 0.0027 -0.0498 561 LEU A CG 4090 C CD1 . LEU A 568 ? 0.2657 0.2967 0.4123 0.0852 0.0051 -0.0548 561 LEU A CD1 4091 C CD2 . LEU A 568 ? 0.2510 0.2765 0.3714 0.0739 0.0088 -0.0504 561 LEU A CD2 4092 N N . VAL A 569 ? 0.2889 0.2905 0.3971 0.0936 -0.0148 -0.0376 562 VAL A N 4093 C CA . VAL A 569 ? 0.2888 0.2924 0.3925 0.0957 -0.0225 -0.0349 562 VAL A CA 4094 C C . VAL A 569 ? 0.3035 0.3023 0.4096 0.1047 -0.0308 -0.0332 562 VAL A C 4095 O O . VAL A 569 ? 0.3113 0.3174 0.4267 0.1084 -0.0378 -0.0352 562 VAL A O 4096 C CB . VAL A 569 ? 0.2855 0.2820 0.3708 0.0919 -0.0217 -0.0297 562 VAL A CB 4097 C CG1 . VAL A 569 ? 0.2893 0.2864 0.3681 0.0951 -0.0300 -0.0271 562 VAL A CG1 4098 C CG2 . VAL A 569 ? 0.2903 0.2926 0.3738 0.0834 -0.0151 -0.0314 562 VAL A CG2 4099 N N . GLU A 570 ? 0.3218 0.3081 0.4201 0.1082 -0.0303 -0.0297 563 GLU A N 4100 C CA . GLU A 570 ? 0.3493 0.3282 0.4461 0.1172 -0.0381 -0.0270 563 GLU A CA 4101 C C . GLU A 570 ? 0.3575 0.3440 0.4738 0.1226 -0.0419 -0.0319 563 GLU A C 4102 O O . GLU A 570 ? 0.3584 0.3451 0.4777 0.1296 -0.0512 -0.0314 563 GLU A O 4103 C CB . GLU A 570 ? 0.3718 0.3353 0.4575 0.1189 -0.0348 -0.0222 563 GLU A CB 4104 C CG . GLU A 570 ? 0.4463 0.3984 0.5240 0.1280 -0.0425 -0.0172 563 GLU A CG 4105 C CD . GLU A 570 ? 0.5133 0.4660 0.6053 0.1354 -0.0466 -0.0201 563 GLU A CD 4106 O OE1 . GLU A 570 ? 0.5036 0.4601 0.6085 0.1334 -0.0409 -0.0246 563 GLU A OE1 4107 O OE2 . GLU A 570 ? 0.5269 0.4760 0.6166 0.1434 -0.0559 -0.0180 563 GLU A OE2 4108 N N . LYS A 571 ? 0.3422 0.3344 0.4714 0.1198 -0.0348 -0.0367 564 LYS A N 4109 C CA . LYS A 571 ? 0.3515 0.3515 0.5010 0.1249 -0.0369 -0.0416 564 LYS A CA 4110 C C . LYS A 571 ? 0.3458 0.3620 0.5110 0.1230 -0.0389 -0.0462 564 LYS A C 4111 O O . LYS A 571 ? 0.3423 0.3645 0.5220 0.1289 -0.0457 -0.0485 564 LYS A O 4112 C CB . LYS A 571 ? 0.3465 0.3452 0.5033 0.1234 -0.0278 -0.0452 564 LYS A CB 4113 C CG . LYS A 571 ? 0.3697 0.3528 0.5173 0.1271 -0.0269 -0.0419 564 LYS A CG 4114 C CD . LYS A 571 ? 0.3996 0.3823 0.5567 0.1263 -0.0185 -0.0469 564 LYS A CD 4115 C CE . LYS A 571 ? 0.4441 0.4105 0.5900 0.1268 -0.0155 -0.0440 564 LYS A CE 4116 N NZ . LYS A 571 ? 0.5372 0.4930 0.6799 0.1349 -0.0228 -0.0393 564 LYS A NZ 4117 N N . PHE A 572 ? 0.3319 0.3549 0.4955 0.1149 -0.0327 -0.0476 565 PHE A N 4118 C CA . PHE A 572 ? 0.3238 0.3621 0.5047 0.1122 -0.0318 -0.0523 565 PHE A CA 4119 C C . PHE A 572 ? 0.3237 0.3673 0.5003 0.1084 -0.0362 -0.0512 565 PHE A C 4120 O O . PHE A 572 ? 0.3484 0.4034 0.5411 0.1086 -0.0395 -0.0544 565 PHE A O 4121 C CB . PHE A 572 ? 0.3119 0.3556 0.4992 0.1066 -0.0200 -0.0561 565 PHE A CB 4122 C CG . PHE A 572 ? 0.3377 0.3768 0.5309 0.1105 -0.0153 -0.0583 565 PHE A CG 4123 C CD1 . PHE A 572 ? 0.3263 0.3706 0.5385 0.1174 -0.0185 -0.0614 565 PHE A CD1 4124 C CD2 . PHE A 572 ? 0.3114 0.3408 0.4919 0.1076 -0.0081 -0.0577 565 PHE A CD2 4125 C CE1 . PHE A 572 ? 0.3534 0.3929 0.5708 0.1214 -0.0143 -0.0636 565 PHE A CE1 4126 C CE2 . PHE A 572 ? 0.3452 0.3693 0.5308 0.1114 -0.0041 -0.0602 565 PHE A CE2 4127 C CZ . PHE A 572 ? 0.3485 0.3774 0.5520 0.1184 -0.0070 -0.0631 565 PHE A CZ 4128 N N . TYR A 573 ? 0.3205 0.3564 0.4771 0.1049 -0.0359 -0.0469 566 TYR A N 4129 C CA . TYR A 573 ? 0.3011 0.3422 0.4540 0.1012 -0.0394 -0.0464 566 TYR A CA 4130 C C . TYR A 573 ? 0.3045 0.3409 0.4497 0.1069 -0.0511 -0.0438 566 TYR A C 4131 O O . TYR A 573 ? 0.3095 0.3535 0.4627 0.1073 -0.0577 -0.0460 566 TYR A O 4132 C CB . TYR A 573 ? 0.2957 0.3335 0.4331 0.0934 -0.0323 -0.0440 566 TYR A CB 4133 C CG . TYR A 573 ? 0.3054 0.3518 0.4516 0.0869 -0.0231 -0.0475 566 TYR A CG 4134 C CD1 . TYR A 573 ? 0.2800 0.3253 0.4302 0.0861 -0.0151 -0.0496 566 TYR A CD1 4135 C CD2 . TYR A 573 ? 0.3326 0.3876 0.4829 0.0818 -0.0224 -0.0488 566 TYR A CD2 4136 C CE1 . TYR A 573 ? 0.3031 0.3554 0.4595 0.0807 -0.0064 -0.0528 566 TYR A CE1 4137 C CE2 . TYR A 573 ? 0.3162 0.3783 0.4734 0.0762 -0.0137 -0.0514 566 TYR A CE2 4138 C CZ . TYR A 573 ? 0.3265 0.3871 0.4862 0.0759 -0.0056 -0.0534 566 TYR A CZ 4139 O OH . TYR A 573 ? 0.3231 0.3897 0.4878 0.0710 0.0030 -0.0559 566 TYR A OH 4140 N N . ASP A 574 ? 0.3041 0.3273 0.4330 0.1113 -0.0536 -0.0391 567 ASP A N 4141 C CA . ASP A 574 ? 0.3169 0.3334 0.4320 0.1161 -0.0633 -0.0356 567 ASP A CA 4142 C C . ASP A 574 ? 0.3276 0.3302 0.4309 0.1235 -0.0666 -0.0311 567 ASP A C 4143 O O . ASP A 574 ? 0.3361 0.3273 0.4193 0.1236 -0.0654 -0.0256 567 ASP A O 4144 C CB . ASP A 574 ? 0.3016 0.3154 0.4000 0.1102 -0.0602 -0.0327 567 ASP A CB 4145 C CG . ASP A 574 ? 0.3359 0.3452 0.4216 0.1145 -0.0700 -0.0307 567 ASP A CG 4146 O OD1 . ASP A 574 ? 0.3442 0.3542 0.4350 0.1214 -0.0802 -0.0322 567 ASP A OD1 4147 O OD2 . ASP A 574 ? 0.3149 0.3196 0.3848 0.1113 -0.0677 -0.0276 567 ASP A OD2 4148 N N . PRO A 575 ? 0.3493 0.3525 0.4654 0.1299 -0.0706 -0.0330 568 PRO A N 4149 C CA . PRO A 575 ? 0.3705 0.3599 0.4765 0.1372 -0.0732 -0.0285 568 PRO A CA 4150 C C . PRO A 575 ? 0.3920 0.3695 0.4761 0.1424 -0.0808 -0.0229 568 PRO A C 4151 O O . PRO A 575 ? 0.4084 0.3715 0.4761 0.1449 -0.0782 -0.0169 568 PRO A O 4152 C CB . PRO A 575 ? 0.3856 0.3807 0.5118 0.1440 -0.0793 -0.0327 568 PRO A CB 4153 C CG . PRO A 575 ? 0.3779 0.3897 0.5261 0.1392 -0.0765 -0.0393 568 PRO A CG 4154 C CD . PRO A 575 ? 0.3359 0.3529 0.4774 0.1309 -0.0727 -0.0394 568 PRO A CD 4155 N N . MET A 576 ? 0.3944 0.3771 0.4778 0.1441 -0.0895 -0.0247 569 MET A N 4156 C CA A MET A 576 ? 0.4146 0.3858 0.4763 0.1502 -0.0976 -0.0200 569 MET A CA 4157 C CA B MET A 576 ? 0.4182 0.3899 0.4804 0.1501 -0.0979 -0.0202 569 MET A CA 4158 C C . MET A 576 ? 0.4128 0.3807 0.4565 0.1443 -0.0925 -0.0169 569 MET A C 4159 O O . MET A 576 ? 0.4292 0.3867 0.4522 0.1486 -0.0968 -0.0126 569 MET A O 4160 C CB A MET A 576 ? 0.4267 0.4032 0.4962 0.1572 -0.1119 -0.0239 569 MET A CB 4161 C CB B MET A 576 ? 0.4317 0.4106 0.5030 0.1558 -0.1115 -0.0248 569 MET A CB 4162 C CG A MET A 576 ? 0.4499 0.4273 0.5348 0.1650 -0.1185 -0.0260 569 MET A CG 4163 C CG B MET A 576 ? 0.4608 0.4474 0.5561 0.1607 -0.1170 -0.0294 569 MET A CG 4164 S SD A MET A 576 ? 0.5049 0.4630 0.5729 0.1717 -0.1157 -0.0183 569 MET A SD 4165 S SD B MET A 576 ? 0.5711 0.5587 0.6694 0.1711 -0.1360 -0.0323 569 MET A SD 4166 C CE A MET A 576 ? 0.5285 0.4718 0.5687 0.1811 -0.1277 -0.0129 569 MET A CE 4167 C CE B MET A 576 ? 0.5097 0.5181 0.6345 0.1648 -0.1390 -0.0410 569 MET A CE 4168 N N . PHE A 577 ? 0.3779 0.3542 0.4290 0.1349 -0.0831 -0.0190 570 PHE A N 4169 C CA . PHE A 577 ? 0.3720 0.3468 0.4093 0.1287 -0.0775 -0.0167 570 PHE A CA 4170 C C . PHE A 577 ? 0.3652 0.3427 0.3963 0.1304 -0.0861 -0.0183 570 PHE A C 4171 O O . PHE A 577 ? 0.3711 0.3437 0.3858 0.1283 -0.0839 -0.0153 570 PHE A O 4172 C CB . PHE A 577 ? 0.3829 0.3433 0.4007 0.1285 -0.0703 -0.0094 570 PHE A CB 4173 C CG . PHE A 577 ? 0.3807 0.3413 0.4065 0.1230 -0.0599 -0.0094 570 PHE A CG 4174 C CD1 . PHE A 577 ? 0.3431 0.3073 0.3680 0.1142 -0.0509 -0.0095 570 PHE A CD1 4175 C CD2 . PHE A 577 ? 0.3800 0.3379 0.4157 0.1268 -0.0598 -0.0100 570 PHE A CD2 4176 C CE1 . PHE A 577 ? 0.3466 0.3112 0.3788 0.1090 -0.0420 -0.0103 570 PHE A CE1 4177 C CE2 . PHE A 577 ? 0.3890 0.3473 0.4324 0.1214 -0.0503 -0.0111 570 PHE A CE2 4178 C CZ . PHE A 577 ? 0.3526 0.3140 0.3935 0.1126 -0.0417 -0.0112 570 PHE A CZ 4179 N N . LYS A 578 ? 0.3591 0.3451 0.4051 0.1339 -0.0956 -0.0236 571 LYS A N 4180 C CA . LYS A 578 ? 0.3690 0.3584 0.4120 0.1352 -0.1047 -0.0264 571 LYS A CA 4181 C C . LYS A 578 ? 0.3419 0.3421 0.3929 0.1259 -0.0995 -0.0297 571 LYS A C 4182 O O . LYS A 578 ? 0.3282 0.3278 0.3700 0.1254 -0.1036 -0.0303 571 LYS A O 4183 C CB . LYS A 578 ? 0.3726 0.3672 0.4297 0.1422 -0.1179 -0.0311 571 LYS A CB 4184 C CG . LYS A 578 ? 0.3706 0.3801 0.4578 0.1388 -0.1162 -0.0369 571 LYS A CG 4185 C CD . LYS A 578 ? 0.4226 0.4373 0.5254 0.1462 -0.1298 -0.0415 571 LYS A CD 4186 C CE . LYS A 578 ? 0.4125 0.4435 0.5468 0.1418 -0.1265 -0.0474 571 LYS A CE 4187 N NZ . LYS A 578 ? 0.4616 0.5000 0.6147 0.1480 -0.1399 -0.0527 571 LYS A NZ 4188 N N . TYR A 579 ? 0.3239 0.3336 0.3917 0.1191 -0.0908 -0.0321 572 TYR A N 4189 C CA . TYR A 579 ? 0.3059 0.3244 0.3793 0.1107 -0.0856 -0.0345 572 TYR A CA 4190 C C . TYR A 579 ? 0.3115 0.3220 0.3648 0.1066 -0.0778 -0.0296 572 TYR A C 4191 O O . TYR A 579 ? 0.3022 0.3142 0.3490 0.1032 -0.0779 -0.0299 572 TYR A O 4192 C CB . TYR A 579 ? 0.2998 0.3304 0.3961 0.1050 -0.0786 -0.0385 572 TYR A CB 4193 C CG . TYR A 579 ? 0.3267 0.3659 0.4446 0.1091 -0.0862 -0.0434 572 TYR A CG 4194 C CD1 . TYR A 579 ? 0.3427 0.3879 0.4689 0.1106 -0.0961 -0.0472 572 TYR A CD1 4195 C CD2 . TYR A 579 ? 0.3693 0.4101 0.4997 0.1122 -0.0842 -0.0443 572 TYR A CD2 4196 C CE1 . TYR A 579 ? 0.3721 0.4255 0.5196 0.1144 -0.1037 -0.0518 572 TYR A CE1 4197 C CE2 . TYR A 579 ? 0.3828 0.4319 0.5344 0.1166 -0.0916 -0.0489 572 TYR A CE2 4198 C CZ . TYR A 579 ? 0.3894 0.4451 0.5501 0.1175 -0.1013 -0.0526 572 TYR A CZ 4199 O OH . TYR A 579 ? 0.4219 0.4866 0.6059 0.1217 -0.1090 -0.0573 572 TYR A OH 4200 N N . HIS A 580 ? 0.2987 0.3009 0.3431 0.1070 -0.0710 -0.0251 573 HIS A N 4201 C CA . HIS A 580 ? 0.3055 0.2998 0.3317 0.1037 -0.0640 -0.0201 573 HIS A CA 4202 C C . HIS A 580 ? 0.3199 0.3060 0.3270 0.1085 -0.0702 -0.0174 573 HIS A C 4203 O O . HIS A 580 ? 0.3197 0.3052 0.3174 0.1049 -0.0672 -0.0162 573 HIS A O 4204 C CB . HIS A 580 ? 0.3089 0.2936 0.3283 0.1050 -0.0578 -0.0155 573 HIS A CB 4205 C CG . HIS A 580 ? 0.3137 0.3037 0.3463 0.0992 -0.0495 -0.0175 573 HIS A CG 4206 N ND1 . HIS A 580 ? 0.3138 0.3104 0.3640 0.1005 -0.0507 -0.0217 573 HIS A ND1 4207 C CD2 . HIS A 580 ? 0.3248 0.3138 0.3550 0.0928 -0.0402 -0.0161 573 HIS A CD2 4208 C CE1 . HIS A 580 ? 0.3595 0.3583 0.4160 0.0952 -0.0420 -0.0228 573 HIS A CE1 4209 N NE2 . HIS A 580 ? 0.3456 0.3398 0.3901 0.0905 -0.0360 -0.0195 573 HIS A NE2 4210 N N . LEU A 581 ? 0.3338 0.3131 0.3346 0.1171 -0.0789 -0.0164 574 LEU A N 4211 C CA . LEU A 581 ? 0.3532 0.3239 0.3342 0.1226 -0.0854 -0.0142 574 LEU A CA 4212 C C . LEU A 581 ? 0.3515 0.3302 0.3364 0.1201 -0.0909 -0.0192 574 LEU A C 4213 O O . LEU A 581 ? 0.3552 0.3295 0.3250 0.1194 -0.0895 -0.0174 574 LEU A O 4214 C CB . LEU A 581 ? 0.3709 0.3328 0.3444 0.1331 -0.0953 -0.0128 574 LEU A CB 4215 C CG . LEU A 581 ? 0.3896 0.3405 0.3391 0.1401 -0.1024 -0.0104 574 LEU A CG 4216 C CD1 . LEU A 581 ? 0.4051 0.3456 0.3336 0.1382 -0.0920 -0.0034 574 LEU A CD1 4217 C CD2 . LEU A 581 ? 0.3804 0.3220 0.3224 0.1509 -0.1127 -0.0089 574 LEU A CD2 4218 N N . THR A 582 ? 0.3458 0.3362 0.3517 0.1188 -0.0965 -0.0254 575 THR A N 4219 C CA . THR A 582 ? 0.3273 0.3254 0.3395 0.1158 -0.1016 -0.0304 575 THR A CA 4220 C C . THR A 582 ? 0.3228 0.3238 0.3320 0.1073 -0.0917 -0.0293 575 THR A C 4221 O O . THR A 582 ? 0.3075 0.3067 0.3068 0.1066 -0.0936 -0.0298 575 THR A O 4222 C CB . THR A 582 ? 0.3265 0.3373 0.3655 0.1149 -0.1074 -0.0369 575 THR A CB 4223 O OG1 . THR A 582 ? 0.3372 0.3443 0.3764 0.1240 -0.1193 -0.0382 575 THR A OG1 4224 C CG2 . THR A 582 ? 0.3161 0.3363 0.3663 0.1098 -0.1103 -0.0420 575 THR A CG2 4225 N N . VAL A 583 ? 0.3095 0.3138 0.3258 0.1015 -0.0812 -0.0276 576 VAL A N 4226 C CA . VAL A 583 ? 0.2973 0.3047 0.3117 0.0937 -0.0723 -0.0266 576 VAL A CA 4227 C C . VAL A 583 ? 0.3070 0.3036 0.2988 0.0948 -0.0681 -0.0211 576 VAL A C 4228 O O . VAL A 583 ? 0.3101 0.3077 0.2963 0.0909 -0.0652 -0.0210 576 VAL A O 4229 C CB . VAL A 583 ? 0.2827 0.2969 0.3113 0.0873 -0.0629 -0.0271 576 VAL A CB 4230 C CG1 . VAL A 583 ? 0.2592 0.2743 0.2826 0.0799 -0.0537 -0.0252 576 VAL A CG1 4231 C CG2 . VAL A 583 ? 0.2846 0.3105 0.3359 0.0853 -0.0655 -0.0327 576 VAL A CG2 4232 N N . ALA A 584 ? 0.3173 0.3035 0.2966 0.1002 -0.0675 -0.0165 577 ALA A N 4233 C CA . ALA A 584 ? 0.3140 0.2896 0.2719 0.1022 -0.0639 -0.0111 577 ALA A CA 4234 C C . ALA A 584 ? 0.3263 0.2984 0.2717 0.1068 -0.0718 -0.0127 577 ALA A C 4235 O O . ALA A 584 ? 0.3171 0.2868 0.2515 0.1051 -0.0683 -0.0112 577 ALA A O 4236 C CB . ALA A 584 ? 0.3222 0.2866 0.2696 0.1076 -0.0619 -0.0056 577 ALA A CB 4237 N N . GLN A 585 ? 0.3301 0.3027 0.2783 0.1126 -0.0831 -0.0163 578 GLN A N 4238 C CA . GLN A 585 ? 0.3423 0.3119 0.2796 0.1167 -0.0917 -0.0190 578 GLN A CA 4239 C C . GLN A 585 ? 0.3334 0.3118 0.2793 0.1101 -0.0910 -0.0234 578 GLN A C 4240 O O . GLN A 585 ? 0.3484 0.3221 0.2802 0.1114 -0.0921 -0.0234 578 GLN A O 4241 C CB . GLN A 585 ? 0.3565 0.3255 0.2975 0.1242 -0.1053 -0.0230 578 GLN A CB 4242 C CG . GLN A 585 ? 0.3775 0.3356 0.3065 0.1322 -0.1073 -0.0183 578 GLN A CG 4243 C CD . GLN A 585 ? 0.4264 0.3850 0.3617 0.1396 -0.1213 -0.0225 578 GLN A CD 4244 O OE1 . GLN A 585 ? 0.4197 0.3885 0.3726 0.1379 -0.1289 -0.0292 578 GLN A OE1 4245 N NE2 . GLN A 585 ? 0.4600 0.4074 0.3820 0.1479 -0.1247 -0.0183 578 GLN A NE2 4246 N N . VAL A 586 ? 0.3121 0.3025 0.2802 0.1033 -0.0888 -0.0269 579 VAL A N 4247 C CA . VAL A 586 ? 0.2958 0.2941 0.2727 0.0969 -0.0875 -0.0304 579 VAL A CA 4248 C C . VAL A 586 ? 0.2968 0.2924 0.2632 0.0921 -0.0767 -0.0262 579 VAL A C 4249 O O . VAL A 586 ? 0.3024 0.2956 0.2594 0.0918 -0.0773 -0.0266 579 VAL A O 4250 C CB . VAL A 586 ? 0.2905 0.3014 0.2927 0.0909 -0.0865 -0.0344 579 VAL A CB 4251 C CG1 . VAL A 586 ? 0.2645 0.2817 0.2733 0.0840 -0.0839 -0.0369 579 VAL A CG1 4252 C CG2 . VAL A 586 ? 0.2737 0.2891 0.2904 0.0952 -0.0977 -0.0395 579 VAL A CG2 4253 N N . ARG A 587 ? 0.2849 0.2810 0.2536 0.0885 -0.0674 -0.0224 580 ARG A N 4254 C CA . ARG A 587 ? 0.2882 0.2828 0.2495 0.0838 -0.0579 -0.0188 580 ARG A CA 4255 C C . ARG A 587 ? 0.3106 0.2941 0.2499 0.0890 -0.0572 -0.0148 580 ARG A C 4256 O O . ARG A 587 ? 0.3149 0.2976 0.2470 0.0871 -0.0543 -0.0143 580 ARG A O 4257 C CB . ARG A 587 ? 0.2757 0.2716 0.2432 0.0797 -0.0492 -0.0159 580 ARG A CB 4258 C CG . ARG A 587 ? 0.2629 0.2693 0.2502 0.0741 -0.0476 -0.0196 580 ARG A CG 4259 C CD . ARG A 587 ? 0.2504 0.2564 0.2419 0.0715 -0.0402 -0.0173 580 ARG A CD 4260 N NE . ARG A 587 ? 0.2363 0.2516 0.2450 0.0668 -0.0383 -0.0210 580 ARG A NE 4261 C CZ . ARG A 587 ? 0.2656 0.2821 0.2804 0.0639 -0.0322 -0.0206 580 ARG A CZ 4262 N NH1 . ARG A 587 ? 0.2546 0.2637 0.2615 0.0651 -0.0282 -0.0168 580 ARG A NH1 4263 N NH2 . ARG A 587 ? 0.2102 0.2348 0.2391 0.0600 -0.0301 -0.0240 580 ARG A NH2 4264 N N . GLY A 588 ? 0.3173 0.2920 0.2456 0.0956 -0.0592 -0.0116 581 GLY A N 4265 C CA . GLY A 588 ? 0.3342 0.2974 0.2405 0.1010 -0.0572 -0.0070 581 GLY A CA 4266 C C . GLY A 588 ? 0.3422 0.3024 0.2376 0.1056 -0.0652 -0.0103 581 GLY A C 4267 O O . GLY A 588 ? 0.3343 0.2892 0.2153 0.1067 -0.0616 -0.0083 581 GLY A O 4268 N N . GLY A 589 ? 0.3377 0.3016 0.2411 0.1080 -0.0761 -0.0159 582 GLY A N 4269 C CA . GLY A 589 ? 0.3588 0.3204 0.2542 0.1119 -0.0852 -0.0203 582 GLY A CA 4270 C C . GLY A 589 ? 0.3535 0.3206 0.2531 0.1060 -0.0820 -0.0228 582 GLY A C 4271 O O . GLY A 589 ? 0.3558 0.3165 0.2399 0.1094 -0.0838 -0.0235 582 GLY A O 4272 N N . MET A 590 ? 0.3350 0.3128 0.2543 0.0978 -0.0776 -0.0243 583 MET A N 4273 C CA . MET A 590 ? 0.3147 0.2977 0.2388 0.0917 -0.0737 -0.0259 583 MET A CA 4274 C C . MET A 590 ? 0.3194 0.2964 0.2282 0.0917 -0.0646 -0.0209 583 MET A C 4275 O O . MET A 590 ? 0.3120 0.2861 0.2118 0.0926 -0.0650 -0.0220 583 MET A O 4276 C CB . MET A 590 ? 0.3103 0.3047 0.2561 0.0832 -0.0693 -0.0273 583 MET A CB 4277 C CG . MET A 590 ? 0.3292 0.3308 0.2924 0.0824 -0.0775 -0.0329 583 MET A CG 4278 S SD . MET A 590 ? 0.3316 0.3456 0.3185 0.0731 -0.0707 -0.0338 583 MET A SD 4279 C CE . MET A 590 ? 0.2882 0.3051 0.2765 0.0670 -0.0675 -0.0349 583 MET A CE 4280 N N . VAL A 591 ? 0.3033 0.2779 0.2093 0.0910 -0.0565 -0.0154 584 VAL A N 4281 C CA . VAL A 591 ? 0.3157 0.2854 0.2098 0.0906 -0.0470 -0.0104 584 VAL A CA 4282 C C . VAL A 591 ? 0.3506 0.3092 0.2224 0.0987 -0.0495 -0.0091 584 VAL A C 4283 O O . VAL A 591 ? 0.3401 0.2964 0.2033 0.0987 -0.0452 -0.0082 584 VAL A O 4284 C CB . VAL A 591 ? 0.3216 0.2896 0.2174 0.0889 -0.0388 -0.0048 584 VAL A CB 4285 C CG1 . VAL A 591 ? 0.2879 0.2489 0.1702 0.0901 -0.0295 0.0010 584 VAL A CG1 4286 C CG2 . VAL A 591 ? 0.3165 0.2946 0.2317 0.0808 -0.0351 -0.0062 584 VAL A CG2 4287 N N . PHE A 592 ? 0.3510 0.3023 0.2129 0.1059 -0.0561 -0.0089 585 PHE A N 4288 C CA . PHE A 592 ? 0.3846 0.3239 0.2229 0.1147 -0.0594 -0.0079 585 PHE A CA 4289 C C . PHE A 592 ? 0.3897 0.3295 0.2240 0.1157 -0.0655 -0.0136 585 PHE A C 4290 O O . PHE A 592 ? 0.4015 0.3344 0.2191 0.1192 -0.0617 -0.0120 585 PHE A O 4291 C CB . PHE A 592 ? 0.4106 0.3431 0.2412 0.1224 -0.0686 -0.0082 585 PHE A CB 4292 C CG . PHE A 592 ? 0.4411 0.3590 0.2437 0.1322 -0.0702 -0.0055 585 PHE A CG 4293 C CD1 . PHE A 592 ? 0.4410 0.3491 0.2296 0.1363 -0.0632 0.0019 585 PHE A CD1 4294 C CD2 . PHE A 592 ? 0.4639 0.3774 0.2539 0.1369 -0.0776 -0.0102 585 PHE A CD2 4295 C CE1 . PHE A 592 ? 0.4802 0.3738 0.2410 0.1455 -0.0631 0.0052 585 PHE A CE1 4296 C CE2 . PHE A 592 ? 0.4816 0.3804 0.2429 0.1466 -0.0784 -0.0077 585 PHE A CE2 4297 C CZ . PHE A 592 ? 0.5017 0.3906 0.2481 0.1509 -0.0708 0.0003 585 PHE A CZ 4298 N N . GLU A 593 ? 0.3773 0.3245 0.2262 0.1133 -0.0748 -0.0202 586 GLU A N 4299 C CA A GLU A 593 ? 0.3852 0.3326 0.2322 0.1139 -0.0813 -0.0261 586 GLU A CA 4300 C CA B GLU A 593 ? 0.3828 0.3294 0.2281 0.1145 -0.0811 -0.0259 586 GLU A CA 4301 C C . GLU A 593 ? 0.3690 0.3198 0.2181 0.1085 -0.0723 -0.0250 586 GLU A C 4302 O O . GLU A 593 ? 0.3820 0.3273 0.2181 0.1116 -0.0725 -0.0264 586 GLU A O 4303 C CB A GLU A 593 ? 0.3839 0.3405 0.2517 0.1103 -0.0910 -0.0328 586 GLU A CB 4304 C CB B GLU A 593 ? 0.3843 0.3378 0.2464 0.1127 -0.0928 -0.0330 586 GLU A CB 4305 C CG A GLU A 593 ? 0.4205 0.3738 0.2867 0.1167 -0.1030 -0.0359 586 GLU A CG 4306 C CG B GLU A 593 ? 0.3988 0.3489 0.2547 0.1158 -0.1019 -0.0394 586 GLU A CG 4307 C CD A GLU A 593 ? 0.5011 0.4434 0.3463 0.1254 -0.1121 -0.0393 586 GLU A CD 4308 C CD B GLU A 593 ? 0.4675 0.4052 0.3009 0.1265 -0.1111 -0.0410 586 GLU A CD 4309 O OE1 A GLU A 593 ? 0.5352 0.4750 0.3794 0.1309 -0.1241 -0.0432 586 GLU A OE1 4310 O OE1 B GLU A 593 ? 0.4737 0.4050 0.2956 0.1321 -0.1109 -0.0369 586 GLU A OE1 4311 O OE2 A GLU A 593 ? 0.5323 0.4686 0.3620 0.1270 -0.1075 -0.0383 586 GLU A OE2 4312 O OE2 B GLU A 593 ? 0.5227 0.4565 0.3493 0.1295 -0.1189 -0.0466 586 GLU A OE2 4313 N N . LEU A 594 ? 0.3466 0.3064 0.2124 0.1006 -0.0649 -0.0227 587 LEU A N 4314 C CA . LEU A 594 ? 0.3380 0.3022 0.2086 0.0949 -0.0570 -0.0217 587 LEU A CA 4315 C C . LEU A 594 ? 0.3534 0.3101 0.2068 0.0983 -0.0482 -0.0165 587 LEU A C 4316 O O . LEU A 594 ? 0.3456 0.3017 0.1949 0.0979 -0.0450 -0.0171 587 LEU A O 4317 C CB . LEU A 594 ? 0.3367 0.3111 0.2268 0.0864 -0.0511 -0.0200 587 LEU A CB 4318 C CG . LEU A 594 ? 0.3246 0.3077 0.2337 0.0816 -0.0575 -0.0250 587 LEU A CG 4319 C CD1 . LEU A 594 ? 0.2814 0.2719 0.2055 0.0756 -0.0517 -0.0226 587 LEU A CD1 4320 C CD2 . LEU A 594 ? 0.3412 0.3277 0.2555 0.0777 -0.0578 -0.0280 587 LEU A CD2 4321 N N . ALA A 595 ? 0.3464 0.2973 0.1906 0.1019 -0.0439 -0.0113 588 ALA A N 4322 C CA . ALA A 595 ? 0.3729 0.3166 0.2021 0.1050 -0.0342 -0.0056 588 ALA A CA 4323 C C . ALA A 595 ? 0.3946 0.3261 0.1995 0.1145 -0.0372 -0.0059 588 ALA A C 4324 O O . ALA A 595 ? 0.4061 0.3319 0.1982 0.1172 -0.0287 -0.0019 588 ALA A O 4325 C CB . ALA A 595 ? 0.3534 0.2958 0.1845 0.1038 -0.0267 0.0008 588 ALA A CB 4326 N N . ASN A 596 ? 0.4087 0.3362 0.2072 0.1197 -0.0491 -0.0106 589 ASN A N 4327 C CA . ASN A 596 ? 0.4388 0.3532 0.2114 0.1297 -0.0527 -0.0108 589 ASN A CA 4328 C C . ASN A 596 ? 0.4598 0.3720 0.2268 0.1331 -0.0632 -0.0185 589 ASN A C 4329 O O . ASN A 596 ? 0.4871 0.3882 0.2311 0.1410 -0.0643 -0.0192 589 ASN A O 4330 C CB . ASN A 596 ? 0.4496 0.3559 0.2111 0.1362 -0.0572 -0.0081 589 ASN A CB 4331 C CG A ASN A 596 ? 0.4880 0.3794 0.2209 0.1454 -0.0528 -0.0033 589 ASN A CG 4332 C CG B ASN A 596 ? 0.4508 0.3545 0.2103 0.1351 -0.0452 0.0004 589 ASN A CG 4333 O OD1 A ASN A 596 ? 0.5332 0.4219 0.2598 0.1448 -0.0400 0.0026 589 ASN A OD1 4334 O OD1 B ASN A 596 ? 0.4971 0.4073 0.2730 0.1299 -0.0435 0.0024 589 ASN A OD1 4335 N ND2 A ASN A 596 ? 0.5321 0.4136 0.2473 0.1543 -0.0633 -0.0058 589 ASN A ND2 4336 N ND2 B ASN A 596 ? 0.4290 0.3239 0.1704 0.1393 -0.0358 0.0056 589 ASN A ND2 4337 N N . SER A 597 ? 0.4285 0.3502 0.2153 0.1275 -0.0709 -0.0245 590 SER A N 4338 C CA . SER A 597 ? 0.4399 0.3591 0.2231 0.1305 -0.0821 -0.0324 590 SER A CA 4339 C C . SER A 597 ? 0.4405 0.3564 0.2141 0.1311 -0.0761 -0.0330 590 SER A C 4340 O O . SER A 597 ? 0.4095 0.3316 0.1925 0.1251 -0.0655 -0.0294 590 SER A O 4341 C CB . SER A 597 ? 0.4440 0.3746 0.2528 0.1235 -0.0903 -0.0382 590 SER A CB 4342 O OG . SER A 597 ? 0.4620 0.3902 0.2695 0.1256 -0.1006 -0.0458 590 SER A OG 4343 N N . ILE A 598 ? 0.4414 0.3472 0.1960 0.1388 -0.0826 -0.0374 591 ILE A N 4344 C CA . ILE A 598 ? 0.4489 0.3508 0.1935 0.1402 -0.0764 -0.0380 591 ILE A CA 4345 C C . ILE A 598 ? 0.4298 0.3420 0.1960 0.1318 -0.0764 -0.0417 591 ILE A C 4346 O O . ILE A 598 ? 0.4096 0.3259 0.1811 0.1277 -0.0658 -0.0384 591 ILE A O 4347 C CB . ILE A 598 ? 0.4708 0.3590 0.1897 0.1506 -0.0846 -0.0431 591 ILE A CB 4348 C CG1 A ILE A 598 ? 0.5222 0.3982 0.2144 0.1596 -0.0797 -0.0374 591 ILE A CG1 4349 C CG1 B ILE A 598 ? 0.5253 0.4021 0.2205 0.1595 -0.0844 -0.0388 591 ILE A CG1 4350 C CG2 A ILE A 598 ? 0.4954 0.3812 0.2092 0.1512 -0.0813 -0.0464 591 ILE A CG2 4351 C CG2 B ILE A 598 ? 0.5006 0.3840 0.2077 0.1529 -0.0765 -0.0431 591 ILE A CG2 4352 C CD1 A ILE A 598 ? 0.5167 0.3785 0.1825 0.1704 -0.0896 -0.0425 591 ILE A CD1 4353 C CD1 B ILE A 598 ? 0.5314 0.4057 0.2178 0.1600 -0.0679 -0.0290 591 ILE A CD1 4354 N N . VAL A 599 ? 0.4286 0.3449 0.2081 0.1293 -0.0882 -0.0483 592 VAL A N 4355 C CA . VAL A 599 ? 0.4164 0.3428 0.2190 0.1205 -0.0886 -0.0512 592 VAL A CA 4356 C C . VAL A 599 ? 0.4055 0.3433 0.2299 0.1127 -0.0860 -0.0478 592 VAL A C 4357 O O . VAL A 599 ? 0.4103 0.3491 0.2383 0.1138 -0.0922 -0.0484 592 VAL A O 4358 C CB . VAL A 599 ? 0.4309 0.3553 0.2377 0.1214 -0.1021 -0.0601 592 VAL A CB 4359 C CG1 . VAL A 599 ? 0.4131 0.3478 0.2452 0.1118 -0.1023 -0.0626 592 VAL A CG1 4360 C CG2 . VAL A 599 ? 0.4634 0.3753 0.2466 0.1298 -0.1045 -0.0640 592 VAL A CG2 4361 N N . LEU A 600 ? 0.3886 0.3348 0.2271 0.1052 -0.0769 -0.0443 593 LEU A N 4362 C CA . LEU A 600 ? 0.3609 0.3178 0.2199 0.0975 -0.0741 -0.0416 593 LEU A CA 4363 C C . LEU A 600 ? 0.3593 0.3204 0.2329 0.0955 -0.0852 -0.0472 593 LEU A C 4364 O O . LEU A 600 ? 0.3672 0.3275 0.2448 0.0951 -0.0925 -0.0530 593 LEU A O 4365 C CB . LEU A 600 ? 0.3623 0.3267 0.2343 0.0899 -0.0655 -0.0390 593 LEU A CB 4366 C CG . LEU A 600 ? 0.3714 0.3348 0.2354 0.0904 -0.0536 -0.0325 593 LEU A CG 4367 C CD1 . LEU A 600 ? 0.3599 0.3305 0.2367 0.0834 -0.0470 -0.0308 593 LEU A CD1 4368 C CD2 . LEU A 600 ? 0.3674 0.3319 0.2317 0.0903 -0.0499 -0.0276 593 LEU A CD2 4369 N N . PRO A 601 ? 0.3427 0.3080 0.2246 0.0945 -0.0868 -0.0457 594 PRO A N 4370 C CA . PRO A 601 ? 0.3499 0.3196 0.2466 0.0933 -0.0974 -0.0511 594 PRO A CA 4371 C C . PRO A 601 ? 0.3291 0.3101 0.2510 0.0838 -0.0952 -0.0521 594 PRO A C 4372 O O . PRO A 601 ? 0.3355 0.3237 0.2723 0.0803 -0.0950 -0.0513 594 PRO A O 4373 C CB . PRO A 601 ? 0.3515 0.3210 0.2464 0.0964 -0.0980 -0.0482 594 PRO A CB 4374 C CG . PRO A 601 ? 0.3358 0.3061 0.2264 0.0941 -0.0850 -0.0407 594 PRO A CG 4375 C CD . PRO A 601 ? 0.3289 0.2940 0.2059 0.0953 -0.0792 -0.0393 594 PRO A CD 4376 N N . PHE A 602 ? 0.3271 0.3089 0.2523 0.0801 -0.0931 -0.0534 595 PHE A N 4377 C CA . PHE A 602 ? 0.3091 0.2995 0.2548 0.0714 -0.0901 -0.0537 595 PHE A CA 4378 C C . PHE A 602 ? 0.3299 0.3188 0.2826 0.0711 -0.0994 -0.0603 595 PHE A C 4379 O O . PHE A 602 ? 0.3582 0.3391 0.2973 0.0758 -0.1034 -0.0633 595 PHE A O 4380 C CB . PHE A 602 ? 0.3051 0.2964 0.2480 0.0678 -0.0799 -0.0494 595 PHE A CB 4381 C CG . PHE A 602 ? 0.2823 0.2760 0.2216 0.0667 -0.0703 -0.0431 595 PHE A CG 4382 C CD1 . PHE A 602 ? 0.2936 0.2913 0.2390 0.0659 -0.0695 -0.0413 595 PHE A CD1 4383 C CD2 . PHE A 602 ? 0.3082 0.3007 0.2403 0.0659 -0.0621 -0.0392 595 PHE A CD2 4384 C CE1 . PHE A 602 ? 0.3355 0.3349 0.2786 0.0645 -0.0608 -0.0358 595 PHE A CE1 4385 C CE2 . PHE A 602 ? 0.3261 0.3209 0.2568 0.0643 -0.0536 -0.0338 595 PHE A CE2 4386 C CZ . PHE A 602 ? 0.2928 0.2908 0.2287 0.0635 -0.0529 -0.0321 595 PHE A CZ 4387 N N . ASP A 603 ? 0.3169 0.3130 0.2906 0.0658 -0.1027 -0.0629 596 ASP A N 4388 C CA . ASP A 603 ? 0.3138 0.3088 0.2972 0.0643 -0.1109 -0.0691 596 ASP A CA 4389 C C . ASP A 603 ? 0.3060 0.3065 0.3049 0.0559 -0.1046 -0.0674 596 ASP A C 4390 O O . ASP A 603 ? 0.2982 0.3069 0.3152 0.0501 -0.1015 -0.0661 596 ASP A O 4391 C CB . ASP A 603 ? 0.3138 0.3120 0.3109 0.0652 -0.1214 -0.0743 596 ASP A CB 4392 C CG . ASP A 603 ? 0.3453 0.3404 0.3499 0.0651 -0.1317 -0.0815 596 ASP A CG 4393 O OD1 . ASP A 603 ? 0.3276 0.3195 0.3311 0.0625 -0.1295 -0.0821 596 ASP A OD1 4394 O OD2 . ASP A 603 ? 0.3905 0.3859 0.4020 0.0680 -0.1427 -0.0869 596 ASP A OD2 4395 N N . CYS A 604 ? 0.3037 0.2993 0.2946 0.0555 -0.1016 -0.0669 597 CYS A N 4396 C CA . CYS A 604 ? 0.3035 0.3026 0.3070 0.0483 -0.0962 -0.0651 597 CYS A CA 4397 C C . CYS A 604 ? 0.2984 0.3015 0.3238 0.0431 -0.1013 -0.0690 597 CYS A C 4398 O O . CYS A 604 ? 0.2975 0.3056 0.3359 0.0363 -0.0951 -0.0661 597 CYS A O 4399 C CB . CYS A 604 ? 0.3113 0.3032 0.3030 0.0498 -0.0946 -0.0652 597 CYS A CB 4400 S SG . CYS A 604 ? 0.3832 0.3651 0.3670 0.0558 -0.1068 -0.0735 597 CYS A SG 4401 N N . ARG A 605 ? 0.2966 0.2975 0.3262 0.0461 -0.1124 -0.0754 598 ARG A N 4402 C CA . ARG A 605 ? 0.2976 0.3030 0.3509 0.0409 -0.1175 -0.0794 598 ARG A CA 4403 C C . ARG A 605 ? 0.2891 0.3051 0.3606 0.0357 -0.1120 -0.0762 598 ARG A C 4404 O O . ARG A 605 ? 0.2814 0.3023 0.3727 0.0290 -0.1096 -0.0761 598 ARG A O 4405 C CB . ARG A 605 ? 0.3049 0.3062 0.3601 0.0455 -0.1316 -0.0875 598 ARG A CB 4406 C CG . ARG A 605 ? 0.3316 0.3216 0.3703 0.0501 -0.1370 -0.0915 598 ARG A CG 4407 C CD . ARG A 605 ? 0.3475 0.3319 0.3819 0.0568 -0.1521 -0.0999 598 ARG A CD 4408 N NE . ARG A 605 ? 0.3840 0.3683 0.4046 0.0635 -0.1539 -0.0986 598 ARG A NE 4409 C CZ . ARG A 605 ? 0.4594 0.4392 0.4734 0.0703 -0.1662 -0.1045 598 ARG A CZ 4410 N NH1 . ARG A 605 ? 0.4410 0.4162 0.4610 0.0713 -0.1781 -0.1125 598 ARG A NH1 4411 N NH2 . ARG A 605 ? 0.4067 0.3860 0.4080 0.0762 -0.1670 -0.1023 598 ARG A NH2 4412 N N . ASP A 606 ? 0.2770 0.2960 0.3418 0.0387 -0.1094 -0.0735 599 ASP A N 4413 C CA . ASP A 606 ? 0.2707 0.2993 0.3512 0.0343 -0.1033 -0.0705 599 ASP A CA 4414 C C . ASP A 606 ? 0.2634 0.2951 0.3472 0.0278 -0.0912 -0.0647 599 ASP A C 4415 O O . ASP A 606 ? 0.2543 0.2931 0.3558 0.0222 -0.0863 -0.0633 599 ASP A O 4416 C CB . ASP A 606 ? 0.2716 0.3016 0.3431 0.0394 -0.1031 -0.0688 599 ASP A CB 4417 C CG . ASP A 606 ? 0.3294 0.3579 0.4023 0.0454 -0.1158 -0.0746 599 ASP A CG 4418 O OD1 . ASP A 606 ? 0.4037 0.4348 0.4941 0.0433 -0.1230 -0.0797 599 ASP A OD1 4419 O OD2 . ASP A 606 ? 0.3474 0.3713 0.4038 0.0521 -0.1189 -0.0743 599 ASP A OD2 4420 N N . TYR A 607 ? 0.2525 0.2788 0.3196 0.0287 -0.0864 -0.0613 600 TYR A N 4421 C CA . TYR A 607 ? 0.2464 0.2746 0.3157 0.0230 -0.0764 -0.0562 600 TYR A CA 4422 C C . TYR A 607 ? 0.2445 0.2726 0.3292 0.0175 -0.0771 -0.0578 600 TYR A C 4423 O O . TYR A 607 ? 0.2415 0.2740 0.3374 0.0117 -0.0701 -0.0546 600 TYR A O 4424 C CB . TYR A 607 ? 0.2373 0.2600 0.2873 0.0252 -0.0719 -0.0527 600 TYR A CB 4425 C CG . TYR A 607 ? 0.2440 0.2706 0.2895 0.0233 -0.0623 -0.0470 600 TYR A CG 4426 C CD1 . TYR A 607 ? 0.2372 0.2687 0.2938 0.0172 -0.0555 -0.0440 600 TYR A CD1 4427 C CD2 . TYR A 607 ? 0.2413 0.2659 0.2712 0.0275 -0.0599 -0.0445 600 TYR A CD2 4428 C CE1 . TYR A 607 ? 0.2397 0.2739 0.2913 0.0156 -0.0474 -0.0393 600 TYR A CE1 4429 C CE2 . TYR A 607 ? 0.2661 0.2939 0.2929 0.0255 -0.0517 -0.0398 600 TYR A CE2 4430 C CZ . TYR A 607 ? 0.2665 0.2991 0.3040 0.0196 -0.0460 -0.0375 600 TYR A CZ 4431 O OH . TYR A 607 ? 0.2745 0.3096 0.3082 0.0179 -0.0389 -0.0336 600 TYR A OH 4432 N N . ALA A 608 ? 0.2499 0.2724 0.3349 0.0194 -0.0856 -0.0627 601 ALA A N 4433 C CA . ALA A 608 ? 0.2471 0.2684 0.3471 0.0141 -0.0866 -0.0643 601 ALA A CA 4434 C C . ALA A 608 ? 0.2484 0.2777 0.3727 0.0090 -0.0860 -0.0653 601 ALA A C 4435 O O . ALA A 608 ? 0.2444 0.2758 0.3816 0.0027 -0.0797 -0.0624 601 ALA A O 4436 C CB . ALA A 608 ? 0.2559 0.2695 0.3526 0.0176 -0.0972 -0.0706 601 ALA A CB 4437 N N . VAL A 609 ? 0.2515 0.2851 0.3819 0.0121 -0.0923 -0.0691 602 VAL A N 4438 C CA . VAL A 609 ? 0.2556 0.2977 0.4102 0.0081 -0.0922 -0.0705 602 VAL A CA 4439 C C . VAL A 609 ? 0.2576 0.3063 0.4171 0.0035 -0.0791 -0.0640 602 VAL A C 4440 O O . VAL A 609 ? 0.2540 0.3067 0.4320 -0.0026 -0.0737 -0.0626 602 VAL A O 4441 C CB . VAL A 609 ? 0.2801 0.3258 0.4387 0.0133 -0.1015 -0.0754 602 VAL A CB 4442 C CG1 . VAL A 609 ? 0.2838 0.3403 0.4687 0.0092 -0.0990 -0.0759 602 VAL A CG1 4443 C CG2 . VAL A 609 ? 0.3195 0.3597 0.4794 0.0169 -0.1156 -0.0830 602 VAL A CG2 4444 N N . VAL A 610 ? 0.2331 0.2819 0.3760 0.0063 -0.0737 -0.0601 603 VAL A N 4445 C CA . VAL A 610 ? 0.2249 0.2793 0.3717 0.0023 -0.0620 -0.0547 603 VAL A CA 4446 C C . VAL A 610 ? 0.2233 0.2743 0.3668 -0.0026 -0.0536 -0.0499 603 VAL A C 4447 O O . VAL A 610 ? 0.2143 0.2692 0.3676 -0.0074 -0.0452 -0.0467 603 VAL A O 4448 C CB . VAL A 610 ? 0.2275 0.2839 0.3614 0.0060 -0.0583 -0.0522 603 VAL A CB 4449 C CG1 . VAL A 610 ? 0.2393 0.2985 0.3767 0.0113 -0.0668 -0.0566 603 VAL A CG1 4450 C CG2 . VAL A 610 ? 0.2644 0.3143 0.3757 0.0087 -0.0567 -0.0493 603 VAL A CG2 4451 N N . LEU A 611 ? 0.2121 0.2554 0.3414 -0.0011 -0.0559 -0.0494 604 LEU A N 4452 C CA . LEU A 611 ? 0.2218 0.2611 0.3476 -0.0052 -0.0491 -0.0449 604 LEU A CA 4453 C C . LEU A 611 ? 0.2305 0.2709 0.3766 -0.0112 -0.0473 -0.0451 604 LEU A C 4454 O O . LEU A 611 ? 0.2311 0.2713 0.3792 -0.0157 -0.0384 -0.0401 604 LEU A O 4455 C CB . LEU A 611 ? 0.2185 0.2494 0.3281 -0.0020 -0.0532 -0.0453 604 LEU A CB 4456 C CG . LEU A 611 ? 0.2014 0.2309 0.2907 0.0026 -0.0514 -0.0431 604 LEU A CG 4457 C CD1 . LEU A 611 ? 0.2360 0.2576 0.3116 0.0064 -0.0561 -0.0445 604 LEU A CD1 4458 C CD2 . LEU A 611 ? 0.2105 0.2418 0.2939 -0.0001 -0.0414 -0.0369 604 LEU A CD2 4459 N N . ARG A 612 ? 0.2371 0.2784 0.3983 -0.0112 -0.0557 -0.0508 605 ARG A N 4460 C CA . ARG A 612 ? 0.2499 0.2925 0.4332 -0.0172 -0.0544 -0.0514 605 ARG A CA 4461 C C . ARG A 612 ? 0.2410 0.2924 0.4396 -0.0209 -0.0459 -0.0489 605 ARG A C 4462 O O . ARG A 612 ? 0.2398 0.2915 0.4480 -0.0265 -0.0372 -0.0447 605 ARG A O 4463 C CB . ARG A 612 ? 0.2631 0.3049 0.4604 -0.0161 -0.0667 -0.0590 605 ARG A CB 4464 C CG . ARG A 612 ? 0.2859 0.3301 0.5107 -0.0228 -0.0657 -0.0602 605 ARG A CG 4465 C CD . ARG A 612 ? 0.3661 0.4038 0.5894 -0.0280 -0.0574 -0.0546 605 ARG A CD 4466 N NE . ARG A 612 ? 0.3793 0.4193 0.6292 -0.0348 -0.0546 -0.0546 605 ARG A NE 4467 C CZ . ARG A 612 ? 0.4433 0.4787 0.7066 -0.0370 -0.0620 -0.0591 605 ARG A CZ 4468 N NH1 . ARG A 612 ? 0.4395 0.4675 0.6903 -0.0324 -0.0728 -0.0640 605 ARG A NH1 4469 N NH2 . ARG A 612 ? 0.4406 0.4788 0.7301 -0.0436 -0.0586 -0.0588 605 ARG A NH2 4470 N N . LYS A 613 ? 0.2284 0.2865 0.4291 -0.0175 -0.0482 -0.0512 606 LYS A N 4471 C CA A LYS A 613 ? 0.2226 0.2893 0.4363 -0.0200 -0.0401 -0.0492 606 LYS A CA 4472 C CA B LYS A 613 ? 0.2257 0.2924 0.4399 -0.0202 -0.0400 -0.0491 606 LYS A CA 4473 C C . LYS A 613 ? 0.2160 0.2811 0.4172 -0.0224 -0.0271 -0.0420 606 LYS A C 4474 O O . LYS A 613 ? 0.2161 0.2842 0.4288 -0.0272 -0.0177 -0.0387 606 LYS A O 4475 C CB A LYS A 613 ? 0.2230 0.2953 0.4355 -0.0146 -0.0453 -0.0526 606 LYS A CB 4476 C CB B LYS A 613 ? 0.2286 0.3015 0.4443 -0.0151 -0.0453 -0.0528 606 LYS A CB 4477 C CG A LYS A 613 ? 0.2186 0.3001 0.4450 -0.0161 -0.0376 -0.0513 606 LYS A CG 4478 C CG B LYS A 613 ? 0.2482 0.3241 0.4808 -0.0133 -0.0575 -0.0600 606 LYS A CG 4479 C CD A LYS A 613 ? 0.2438 0.3292 0.4665 -0.0100 -0.0435 -0.0544 606 LYS A CD 4480 C CD B LYS A 613 ? 0.3112 0.3965 0.5741 -0.0174 -0.0550 -0.0617 606 LYS A CD 4481 C CE A LYS A 613 ? 0.2189 0.2985 0.4135 -0.0053 -0.0432 -0.0519 606 LYS A CE 4482 C CE B LYS A 613 ? 0.3443 0.4328 0.6233 -0.0146 -0.0692 -0.0695 606 LYS A CE 4483 N NZ A LYS A 613 ? 0.1937 0.2764 0.3850 0.0002 -0.0476 -0.0541 606 LYS A NZ 4484 N NZ B LYS A 613 ? 0.3430 0.4243 0.5982 -0.0074 -0.0796 -0.0723 606 LYS A NZ 4485 N N . TYR A 614 ? 0.1988 0.2589 0.3764 -0.0191 -0.0267 -0.0396 607 TYR A N 4486 C CA . TYR A 614 ? 0.1970 0.2550 0.3613 -0.0209 -0.0158 -0.0332 607 TYR A CA 4487 C C . TYR A 614 ? 0.1824 0.2346 0.3475 -0.0256 -0.0105 -0.0291 607 TYR A C 4488 O O . TYR A 614 ? 0.2096 0.2616 0.3727 -0.0286 -0.0005 -0.0243 607 TYR A O 4489 C CB . TYR A 614 ? 0.1818 0.2357 0.3224 -0.0164 -0.0174 -0.0319 607 TYR A CB 4490 C CG . TYR A 614 ? 0.1993 0.2572 0.3352 -0.0114 -0.0218 -0.0349 607 TYR A CG 4491 C CD1 . TYR A 614 ? 0.2008 0.2662 0.3515 -0.0111 -0.0215 -0.0373 607 TYR A CD1 4492 C CD2 . TYR A 614 ? 0.2218 0.2757 0.3396 -0.0068 -0.0259 -0.0350 607 TYR A CD2 4493 C CE1 . TYR A 614 ? 0.2261 0.2941 0.3720 -0.0062 -0.0258 -0.0397 607 TYR A CE1 4494 C CE2 . TYR A 614 ? 0.2159 0.2721 0.3286 -0.0021 -0.0295 -0.0371 607 TYR A CE2 4495 C CZ . TYR A 614 ? 0.2659 0.3289 0.3923 -0.0018 -0.0296 -0.0393 607 TYR A CZ 4496 O OH . TYR A 614 ? 0.2801 0.3446 0.4014 0.0030 -0.0333 -0.0411 607 TYR A OH 4497 N N . ALA A 615 ? 0.1775 0.2241 0.3443 -0.0260 -0.0170 -0.0310 608 ALA A N 4498 C CA . ALA A 615 ? 0.1977 0.2380 0.3664 -0.0303 -0.0127 -0.0272 608 ALA A CA 4499 C C . ALA A 615 ? 0.2174 0.2616 0.4086 -0.0361 -0.0060 -0.0259 608 ALA A C 4500 O O . ALA A 615 ? 0.2165 0.2576 0.4066 -0.0399 0.0037 -0.0201 608 ALA A O 4501 C CB . ALA A 615 ? 0.2146 0.2480 0.3821 -0.0291 -0.0222 -0.0306 608 ALA A CB 4502 N N . ASP A 616 ? 0.2196 0.2701 0.4315 -0.0366 -0.0115 -0.0313 609 ASP A N 4503 C CA . ASP A 616 ? 0.2387 0.2947 0.4758 -0.0421 -0.0051 -0.0306 609 ASP A CA 4504 C C . ASP A 616 ? 0.2368 0.2976 0.4715 -0.0432 0.0076 -0.0257 609 ASP A C 4505 O O . ASP A 616 ? 0.2384 0.2989 0.4823 -0.0481 0.0183 -0.0211 609 ASP A O 4506 C CB . ASP A 616 ? 0.2359 0.3001 0.4950 -0.0411 -0.0140 -0.0379 609 ASP A CB 4507 C CG . ASP A 616 ? 0.2986 0.3585 0.5660 -0.0410 -0.0262 -0.0435 609 ASP A CG 4508 O OD1 . ASP A 616 ? 0.3319 0.3835 0.5961 -0.0435 -0.0262 -0.0417 609 ASP A OD1 4509 O OD2 . ASP A 616 ? 0.3686 0.4334 0.6469 -0.0383 -0.0364 -0.0502 609 ASP A OD2 4510 N N . LYS A 617 ? 0.2120 0.2767 0.4346 -0.0386 0.0067 -0.0269 610 LYS A N 4511 C CA . LYS A 617 ? 0.2289 0.2979 0.4483 -0.0388 0.0174 -0.0235 610 LYS A CA 4512 C C . LYS A 617 ? 0.2327 0.2942 0.4335 -0.0405 0.0275 -0.0164 610 LYS A C 4513 O O . LYS A 617 ? 0.2253 0.2878 0.4308 -0.0437 0.0391 -0.0122 610 LYS A O 4514 C CB . LYS A 617 ? 0.2251 0.2984 0.4342 -0.0332 0.0131 -0.0266 610 LYS A CB 4515 C CG . LYS A 617 ? 0.2605 0.3382 0.4670 -0.0329 0.0235 -0.0241 610 LYS A CG 4516 C CD . LYS A 617 ? 0.3387 0.4175 0.5292 -0.0273 0.0193 -0.0260 610 LYS A CD 4517 C CE . LYS A 617 ? 0.3826 0.4679 0.5785 -0.0264 0.0270 -0.0261 610 LYS A CE 4518 N NZ . LYS A 617 ? 0.3718 0.4573 0.5527 -0.0212 0.0230 -0.0278 610 LYS A NZ 4519 N N . ILE A 618 ? 0.2336 0.2875 0.4136 -0.0382 0.0232 -0.0150 611 ILE A N 4520 C CA . ILE A 618 ? 0.2388 0.2853 0.4003 -0.0392 0.0310 -0.0085 611 ILE A CA 4521 C C . ILE A 618 ? 0.2534 0.2941 0.4231 -0.0444 0.0370 -0.0040 611 ILE A C 4522 O O . ILE A 618 ? 0.2569 0.2942 0.4203 -0.0465 0.0477 0.0016 611 ILE A O 4523 C CB . ILE A 618 ? 0.2534 0.2942 0.3915 -0.0349 0.0247 -0.0083 611 ILE A CB 4524 C CG1 . ILE A 618 ? 0.2521 0.2870 0.3706 -0.0350 0.0325 -0.0023 611 ILE A CG1 4525 C CG2 . ILE A 618 ? 0.2444 0.2793 0.3830 -0.0347 0.0158 -0.0100 611 ILE A CG2 4526 C CD1 . ILE A 618 ? 0.2392 0.2785 0.3519 -0.0339 0.0399 -0.0014 611 ILE A CD1 4527 N N . TYR A 619 ? 0.2368 0.2759 0.4207 -0.0463 0.0303 -0.0067 612 TYR A N 4528 C CA . TYR A 619 ? 0.2571 0.2911 0.4530 -0.0517 0.0358 -0.0030 612 TYR A CA 4529 C C . TYR A 619 ? 0.2535 0.2937 0.4677 -0.0558 0.0473 -0.0007 612 TYR A C 4530 O O . TYR A 619 ? 0.2654 0.3003 0.4785 -0.0594 0.0582 0.0056 612 TYR A O 4531 C CB . TYR A 619 ? 0.2616 0.2939 0.4727 -0.0529 0.0253 -0.0078 612 TYR A CB 4532 C CG . TYR A 619 ? 0.2893 0.3193 0.5219 -0.0593 0.0308 -0.0055 612 TYR A CG 4533 C CD1 . TYR A 619 ? 0.3364 0.3556 0.5624 -0.0620 0.0351 0.0002 612 TYR A CD1 4534 C CD2 . TYR A 619 ? 0.3425 0.3815 0.6034 -0.0626 0.0319 -0.0089 612 TYR A CD2 4535 C CE1 . TYR A 619 ? 0.3986 0.4151 0.6454 -0.0682 0.0407 0.0028 612 TYR A CE1 4536 C CE2 . TYR A 619 ? 0.4018 0.4393 0.6850 -0.0689 0.0376 -0.0066 612 TYR A CE2 4537 C CZ . TYR A 619 ? 0.4456 0.4715 0.7214 -0.0719 0.0423 -0.0005 612 TYR A CZ 4538 O OH . TYR A 619 ? 0.5468 0.5706 0.8452 -0.0784 0.0484 0.0019 612 TYR A OH 4539 N N . SER A 620 ? 0.2534 0.3041 0.4831 -0.0549 0.0454 -0.0057 613 SER A N 4540 C CA . SER A 620 ? 0.2633 0.3211 0.5136 -0.0585 0.0560 -0.0044 613 SER A CA 4541 C C . SER A 620 ? 0.2726 0.3287 0.5061 -0.0579 0.0692 0.0014 613 SER A C 4542 O O . SER A 620 ? 0.2834 0.3393 0.5259 -0.0618 0.0817 0.0060 613 SER A O 4543 C CB . SER A 620 ? 0.2668 0.3367 0.5377 -0.0570 0.0501 -0.0114 613 SER A CB 4544 O OG A SER A 620 ? 0.2609 0.3321 0.5497 -0.0580 0.0385 -0.0169 613 SER A OG 4545 O OG B SER A 620 ? 0.3002 0.3731 0.5545 -0.0513 0.0468 -0.0137 613 SER A OG 4546 N N . ILE A 621 ? 0.2660 0.3205 0.4753 -0.0529 0.0666 0.0011 614 ILE A N 4547 C CA . ILE A 621 ? 0.2635 0.3145 0.4529 -0.0517 0.0773 0.0062 614 ILE A CA 4548 C C . ILE A 621 ? 0.2799 0.3195 0.4567 -0.0545 0.0847 0.0137 614 ILE A C 4549 O O . ILE A 621 ? 0.2778 0.3150 0.4521 -0.0564 0.0974 0.0189 614 ILE A O 4550 C CB . ILE A 621 ? 0.2665 0.3171 0.4330 -0.0461 0.0710 0.0039 614 ILE A CB 4551 C CG1 . ILE A 621 ? 0.2578 0.3190 0.4356 -0.0433 0.0671 -0.0021 614 ILE A CG1 4552 C CG2 . ILE A 621 ? 0.2564 0.3008 0.3987 -0.0447 0.0803 0.0091 614 ILE A CG2 4553 C CD1 . ILE A 621 ? 0.2827 0.3434 0.4412 -0.0379 0.0586 -0.0051 614 ILE A CD1 4554 N N . SER A 622 ? 0.2751 0.3072 0.4440 -0.0543 0.0768 0.0144 615 SER A N 4555 C CA . SER A 622 ? 0.2890 0.3094 0.4450 -0.0563 0.0822 0.0215 615 SER A CA 4556 C C . SER A 622 ? 0.3047 0.3238 0.4811 -0.0622 0.0917 0.0253 615 SER A C 4557 O O . SER A 622 ? 0.3086 0.3201 0.4763 -0.0641 0.1031 0.0327 615 SER A O 4558 C CB . SER A 622 ? 0.2832 0.2968 0.4301 -0.0547 0.0707 0.0204 615 SER A CB 4559 O OG . SER A 622 ? 0.2889 0.2907 0.4210 -0.0556 0.0752 0.0274 615 SER A OG 4560 N N . MET A 623 ? 0.3005 0.3269 0.5045 -0.0649 0.0870 0.0205 616 MET A N 4561 C CA . MET A 623 ? 0.3210 0.3470 0.5489 -0.0711 0.0952 0.0234 616 MET A CA 4562 C C . MET A 623 ? 0.3328 0.3635 0.5689 -0.0733 0.1108 0.0271 616 MET A C 4563 O O . MET A 623 ? 0.3292 0.3593 0.5848 -0.0786 0.1198 0.0307 616 MET A O 4564 C CB . MET A 623 ? 0.3127 0.3449 0.5689 -0.0735 0.0851 0.0167 616 MET A CB 4565 C CG . MET A 623 ? 0.3924 0.4150 0.6439 -0.0740 0.0752 0.0162 616 MET A CG 4566 S SD . MET A 623 ? 0.5166 0.5252 0.7686 -0.0797 0.0856 0.0257 616 MET A SD 4567 C CE . MET A 623 ? 0.4290 0.4451 0.7171 -0.0868 0.0975 0.0271 616 MET A CE 4568 N N . LYS A 624 ? 0.3432 0.3778 0.5644 -0.0692 0.1145 0.0265 617 LYS A N 4569 C CA . LYS A 624 ? 0.3668 0.4028 0.5890 -0.0704 0.1311 0.0312 617 LYS A CA 4570 C C . LYS A 624 ? 0.3739 0.3962 0.5746 -0.0715 0.1418 0.0406 617 LYS A C 4571 O O . LYS A 624 ? 0.3824 0.4032 0.5827 -0.0730 0.1567 0.0457 617 LYS A O 4572 C CB . LYS A 624 ? 0.3813 0.4240 0.5920 -0.0655 0.1328 0.0280 617 LYS A CB 4573 C CG . LYS A 624 ? 0.4278 0.4838 0.6572 -0.0635 0.1231 0.0192 617 LYS A CG 4574 C CD . LYS A 624 ? 0.5364 0.6033 0.8006 -0.0671 0.1297 0.0172 617 LYS A CD 4575 C CE . LYS A 624 ? 0.5642 0.6437 0.8442 -0.0640 0.1193 0.0085 617 LYS A CE 4576 N NZ . LYS A 624 ? 0.5622 0.6430 0.8508 -0.0637 0.1022 0.0028 617 LYS A NZ 4577 N N . HIS A 625 ? 0.3605 0.3722 0.5422 -0.0703 0.1342 0.0429 618 HIS A N 4578 C CA . HIS A 625 ? 0.3631 0.3607 0.5231 -0.0707 0.1429 0.0519 618 HIS A CA 4579 C C . HIS A 625 ? 0.3644 0.3534 0.5325 -0.0745 0.1393 0.0551 618 HIS A C 4580 O O . HIS A 625 ? 0.3481 0.3276 0.4967 -0.0722 0.1319 0.0569 618 HIS A O 4581 C CB . HIS A 625 ? 0.3747 0.3663 0.5003 -0.0647 0.1381 0.0525 618 HIS A CB 4582 C CG . HIS A 625 ? 0.3918 0.3919 0.5101 -0.0606 0.1382 0.0477 618 HIS A CG 4583 N ND1 . HIS A 625 ? 0.4511 0.4597 0.5719 -0.0575 0.1256 0.0398 618 HIS A ND1 4584 C CD2 . HIS A 625 ? 0.3758 0.3762 0.4832 -0.0588 0.1495 0.0498 618 HIS A CD2 4585 C CE1 . HIS A 625 ? 0.4289 0.4428 0.5419 -0.0543 0.1290 0.0374 618 HIS A CE1 4586 N NE2 . HIS A 625 ? 0.4706 0.4796 0.5750 -0.0549 0.1432 0.0430 618 HIS A NE2 4587 N N . PRO A 626 ? 0.3596 0.3515 0.5575 -0.0805 0.1444 0.0557 619 PRO A N 4588 C CA . PRO A 626 ? 0.3682 0.3521 0.5753 -0.0840 0.1388 0.0573 619 PRO A CA 4589 C C . PRO A 626 ? 0.3916 0.3589 0.5773 -0.0843 0.1457 0.0670 619 PRO A C 4590 O O . PRO A 626 ? 0.3896 0.3486 0.5694 -0.0839 0.1364 0.0673 619 PRO A O 4591 C CB . PRO A 626 ? 0.3701 0.3609 0.6148 -0.0906 0.1444 0.0562 619 PRO A CB 4592 C CG . PRO A 626 ? 0.3737 0.3724 0.6239 -0.0910 0.1591 0.0580 619 PRO A CG 4593 C CD . PRO A 626 ? 0.3523 0.3558 0.5791 -0.0841 0.1533 0.0537 619 PRO A CD 4594 N N . GLN A 627 ? 0.3998 0.3617 0.5734 -0.0847 0.1613 0.0748 620 GLN A N 4595 C CA . GLN A 627 ? 0.4292 0.3741 0.5792 -0.0842 0.1679 0.0847 620 GLN A CA 4596 C C . GLN A 627 ? 0.4124 0.3500 0.5314 -0.0780 0.1560 0.0841 620 GLN A C 4597 O O . GLN A 627 ? 0.3977 0.3232 0.5075 -0.0779 0.1518 0.0882 620 GLN A O 4598 C CB . GLN A 627 ? 0.4671 0.4072 0.6046 -0.0843 0.1866 0.0927 620 GLN A CB 4599 C CG . GLN A 627 ? 0.5681 0.4897 0.6881 -0.0854 0.1967 0.1045 620 GLN A CG 4600 C CD . GLN A 627 ? 0.6148 0.5288 0.7533 -0.0907 0.1934 0.1072 620 GLN A CD 4601 O OE1 . GLN A 627 ? 0.6739 0.5902 0.8414 -0.0972 0.2019 0.1091 620 GLN A OE1 4602 N NE2 . GLN A 627 ? 0.5765 0.4811 0.6989 -0.0877 0.1810 0.1074 620 GLN A NE2 4603 N N . GLU A 628 ? 0.3900 0.3347 0.4941 -0.0728 0.1508 0.0790 621 GLU A N 4604 C CA . GLU A 628 ? 0.3935 0.3329 0.4704 -0.0670 0.1398 0.0779 621 GLU A CA 4605 C C . GLU A 628 ? 0.3742 0.3150 0.4600 -0.0666 0.1243 0.0723 621 GLU A C 4606 O O . GLU A 628 ? 0.3892 0.3209 0.4578 -0.0636 0.1170 0.0743 621 GLU A O 4607 C CB . GLU A 628 ? 0.3993 0.3464 0.4606 -0.0620 0.1380 0.0734 621 GLU A CB 4608 C CG . GLU A 628 ? 0.4507 0.3928 0.4936 -0.0606 0.1524 0.0794 621 GLU A CG 4609 C CD . GLU A 628 ? 0.5138 0.4626 0.5776 -0.0647 0.1665 0.0803 621 GLU A CD 4610 O OE1 . GLU A 628 ? 0.5147 0.4752 0.6084 -0.0682 0.1644 0.0749 621 GLU A OE1 4611 O OE2 . GLU A 628 ? 0.5993 0.5415 0.6492 -0.0642 0.1801 0.0867 621 GLU A OE2 4612 N N . MET A 629 ? 0.3508 0.3030 0.4632 -0.0691 0.1187 0.0649 622 MET A N 4613 C CA . MET A 629 ? 0.3274 0.2806 0.4490 -0.0687 0.1044 0.0591 622 MET A CA 4614 C C . MET A 629 ? 0.3521 0.2926 0.4778 -0.0719 0.1048 0.0644 622 MET A C 4615 O O . MET A 629 ? 0.3675 0.3019 0.4851 -0.0695 0.0946 0.0631 622 MET A O 4616 C CB . MET A 629 ? 0.3138 0.2807 0.4633 -0.0709 0.0993 0.0507 622 MET A CB 4617 C CG . MET A 629 ? 0.2772 0.2559 0.4203 -0.0663 0.0943 0.0441 622 MET A CG 4618 S SD . MET A 629 ? 0.3180 0.3110 0.4926 -0.0680 0.0853 0.0339 622 MET A SD 4619 C CE . MET A 629 ? 0.2620 0.2494 0.4348 -0.0660 0.0690 0.0293 622 MET A CE 4620 N N . LYS A 630 ? 0.3612 0.2972 0.4989 -0.0771 0.1173 0.0707 623 LYS A N 4621 C CA . LYS A 630 ? 0.3903 0.3128 0.5313 -0.0805 0.1198 0.0770 623 LYS A CA 4622 C C . LYS A 630 ? 0.4038 0.3120 0.5123 -0.0761 0.1209 0.0846 623 LYS A C 4623 O O . LYS A 630 ? 0.3859 0.2852 0.4881 -0.0745 0.1125 0.0852 623 LYS A O 4624 C CB . LYS A 630 ? 0.4105 0.3318 0.5725 -0.0872 0.1343 0.0824 623 LYS A CB 4625 C CG . LYS A 630 ? 0.4085 0.3416 0.6068 -0.0922 0.1312 0.0751 623 LYS A CG 4626 C CD . LYS A 630 ? 0.4995 0.4329 0.7199 -0.0989 0.1471 0.0807 623 LYS A CD 4627 C CE . LYS A 630 ? 0.5214 0.4684 0.7788 -0.1033 0.1421 0.0722 623 LYS A CE 4628 N NZ . LYS A 630 ? 0.5939 0.5526 0.8700 -0.1061 0.1541 0.0722 623 LYS A NZ 4629 N N . THR A 631 ? 0.4096 0.3159 0.4975 -0.0736 0.1304 0.0897 624 THR A N 4630 C CA . THR A 631 ? 0.4509 0.3433 0.5073 -0.0693 0.1322 0.0973 624 THR A CA 4631 C C . THR A 631 ? 0.4359 0.3275 0.4751 -0.0633 0.1174 0.0931 624 THR A C 4632 O O . THR A 631 ? 0.4568 0.3358 0.4810 -0.0610 0.1139 0.0979 624 THR A O 4633 C CB . THR A 631 ? 0.4683 0.3595 0.5052 -0.0673 0.1445 0.1023 624 THR A CB 4634 O OG1 . THR A 631 ? 0.5098 0.4000 0.5630 -0.0729 0.1598 0.1074 624 THR A OG1 4635 C CG2 . THR A 631 ? 0.5285 0.4040 0.5316 -0.0624 0.1457 0.1103 624 THR A CG2 4636 N N . TYR A 632 ? 0.3980 0.3027 0.4399 -0.0607 0.1090 0.0843 625 TYR A N 4637 C CA . TYR A 632 ? 0.3979 0.3031 0.4244 -0.0551 0.0959 0.0802 625 TYR A CA 4638 C C . TYR A 632 ? 0.3800 0.2900 0.4232 -0.0553 0.0835 0.0728 625 TYR A C 4639 O O . TYR A 632 ? 0.3737 0.2859 0.4066 -0.0506 0.0731 0.0686 625 TYR A O 4640 C CB . TYR A 632 ? 0.3891 0.3029 0.4005 -0.0507 0.0946 0.0765 625 TYR A CB 4641 C CG . TYR A 632 ? 0.4168 0.3238 0.4087 -0.0498 0.1064 0.0836 625 TYR A CG 4642 C CD1 . TYR A 632 ? 0.4776 0.3708 0.4448 -0.0465 0.1071 0.0908 625 TYR A CD1 4643 C CD2 . TYR A 632 ? 0.4393 0.3534 0.4371 -0.0518 0.1168 0.0832 625 TYR A CD2 4644 C CE1 . TYR A 632 ? 0.5497 0.4351 0.4965 -0.0452 0.1183 0.0977 625 TYR A CE1 4645 C CE2 . TYR A 632 ? 0.5181 0.4251 0.4965 -0.0505 0.1286 0.0897 625 TYR A CE2 4646 C CZ . TYR A 632 ? 0.5597 0.4520 0.5117 -0.0471 0.1290 0.0969 625 TYR A CZ 4647 O OH . TYR A 632 ? 0.6060 0.4901 0.5370 -0.0454 0.1404 0.1034 625 TYR A OH 4648 N N . SER A 633 ? 0.3655 0.2763 0.4338 -0.0606 0.0848 0.0714 626 SER A N 4649 C CA . SER A 633 ? 0.3577 0.2712 0.4420 -0.0609 0.0731 0.0643 626 SER A CA 4650 C C . SER A 633 ? 0.3397 0.2663 0.4247 -0.0574 0.0639 0.0551 626 SER A C 4651 O O . SER A 633 ? 0.3299 0.2563 0.4076 -0.0532 0.0533 0.0511 626 SER A O 4652 C CB . SER A 633 ? 0.3617 0.2626 0.4345 -0.0582 0.0663 0.0669 626 SER A CB 4653 O OG . SER A 633 ? 0.4195 0.3075 0.4926 -0.0617 0.0750 0.0757 626 SER A OG 4654 N N . VAL A 634 ? 0.3287 0.2666 0.4224 -0.0588 0.0684 0.0523 627 VAL A N 4655 C CA . VAL A 634 ? 0.3127 0.2626 0.4062 -0.0553 0.0609 0.0444 627 VAL A CA 4656 C C . VAL A 634 ? 0.3193 0.2758 0.4372 -0.0576 0.0536 0.0369 627 VAL A C 4657 O O . VAL A 634 ? 0.3435 0.3048 0.4829 -0.0623 0.0585 0.0359 627 VAL A O 4658 C CB . VAL A 634 ? 0.3138 0.2719 0.4044 -0.0553 0.0692 0.0447 627 VAL A CB 4659 C CG1 . VAL A 634 ? 0.2568 0.2263 0.3453 -0.0513 0.0612 0.0371 627 VAL A CG1 4660 C CG2 . VAL A 634 ? 0.3099 0.2598 0.3770 -0.0537 0.0777 0.0526 627 VAL A CG2 4661 N N . SER A 635 ? 0.3234 0.2793 0.4383 -0.0542 0.0419 0.0317 628 SER A N 4662 C CA . SER A 635 ? 0.3246 0.2856 0.4589 -0.0551 0.0333 0.0239 628 SER A CA 4663 C C . SER A 635 ? 0.3080 0.2784 0.4374 -0.0502 0.0248 0.0166 628 SER A C 4664 O O . SER A 635 ? 0.2832 0.2527 0.3931 -0.0453 0.0211 0.0167 628 SER A O 4665 C CB . SER A 635 ? 0.3424 0.2935 0.4798 -0.0553 0.0265 0.0231 628 SER A CB 4666 O OG . SER A 635 ? 0.3535 0.3095 0.5107 -0.0565 0.0185 0.0151 628 SER A OG 4667 N N . PHE A 636 ? 0.2907 0.2702 0.4383 -0.0516 0.0218 0.0106 629 PHE A N 4668 C CA . PHE A 636 ? 0.2766 0.2636 0.4216 -0.0470 0.0125 0.0033 629 PHE A CA 4669 C C . PHE A 636 ? 0.2698 0.2536 0.4206 -0.0452 0.0008 -0.0029 629 PHE A C 4670 O O . PHE A 636 ? 0.2561 0.2454 0.4057 -0.0413 -0.0071 -0.0093 629 PHE A O 4671 C CB . PHE A 636 ? 0.2727 0.2712 0.4318 -0.0483 0.0147 0.0000 629 PHE A CB 4672 C CG . PHE A 636 ? 0.2815 0.2840 0.4298 -0.0477 0.0239 0.0043 629 PHE A CG 4673 C CD1 . PHE A 636 ? 0.2673 0.2751 0.4021 -0.0430 0.0210 0.0019 629 PHE A CD1 4674 C CD2 . PHE A 636 ? 0.3032 0.3033 0.4542 -0.0518 0.0359 0.0108 629 PHE A CD2 4675 C CE1 . PHE A 636 ? 0.2820 0.2926 0.4061 -0.0423 0.0290 0.0053 629 PHE A CE1 4676 C CE2 . PHE A 636 ? 0.2744 0.2772 0.4138 -0.0509 0.0443 0.0143 629 PHE A CE2 4677 C CZ . PHE A 636 ? 0.2751 0.2833 0.4013 -0.0461 0.0404 0.0112 629 PHE A CZ 4678 N N . ASP A 637 ? 0.2650 0.2393 0.4206 -0.0476 0.0000 -0.0013 630 ASP A N 4679 C CA . ASP A 637 ? 0.2759 0.2463 0.4384 -0.0461 -0.0110 -0.0080 630 ASP A CA 4680 C C . ASP A 637 ? 0.2681 0.2385 0.4121 -0.0391 -0.0188 -0.0117 630 ASP A C 4681 O O . ASP A 637 ? 0.2859 0.2584 0.4337 -0.0363 -0.0279 -0.0191 630 ASP A O 4682 C CB . ASP A 637 ? 0.2857 0.2443 0.4534 -0.0492 -0.0108 -0.0053 630 ASP A CB 4683 C CG . ASP A 637 ? 0.3365 0.2946 0.5273 -0.0567 -0.0041 -0.0027 630 ASP A CG 4684 O OD1 . ASP A 637 ? 0.3481 0.3158 0.5537 -0.0594 -0.0009 -0.0042 630 ASP A OD1 4685 O OD2 . ASP A 637 ? 0.3694 0.3172 0.5643 -0.0597 -0.0020 0.0009 630 ASP A OD2 4686 N N . SER A 638 ? 0.2661 0.2339 0.3904 -0.0361 -0.0153 -0.0069 631 SER A N 4687 C CA . SER A 638 ? 0.2683 0.2365 0.3763 -0.0295 -0.0219 -0.0102 631 SER A CA 4688 C C . SER A 638 ? 0.2610 0.2393 0.3684 -0.0266 -0.0251 -0.0151 631 SER A C 4689 O O . SER A 638 ? 0.2488 0.2274 0.3513 -0.0220 -0.0329 -0.0207 631 SER A O 4690 C CB . SER A 638 ? 0.2716 0.2360 0.3605 -0.0268 -0.0180 -0.0042 631 SER A CB 4691 O OG . SER A 638 ? 0.2761 0.2458 0.3600 -0.0283 -0.0103 0.0002 631 SER A OG 4692 N N . LEU A 639 ? 0.2519 0.2376 0.3635 -0.0290 -0.0190 -0.0130 632 LEU A N 4693 C CA . LEU A 639 ? 0.2492 0.2438 0.3603 -0.0262 -0.0215 -0.0171 632 LEU A CA 4694 C C . LEU A 639 ? 0.2475 0.2450 0.3745 -0.0264 -0.0293 -0.0242 632 LEU A C 4695 O O . LEU A 639 ? 0.2324 0.2325 0.3547 -0.0218 -0.0362 -0.0293 632 LEU A O 4696 C CB . LEU A 639 ? 0.2405 0.2417 0.3520 -0.0285 -0.0128 -0.0131 632 LEU A CB 4697 C CG . LEU A 639 ? 0.2475 0.2578 0.3588 -0.0256 -0.0148 -0.0169 632 LEU A CG 4698 C CD1 . LEU A 639 ? 0.2183 0.2281 0.3115 -0.0199 -0.0190 -0.0181 632 LEU A CD1 4699 C CD2 . LEU A 639 ? 0.2339 0.2501 0.3474 -0.0281 -0.0057 -0.0134 632 LEU A CD2 4700 N N . PHE A 640 ? 0.2479 0.2443 0.3936 -0.0314 -0.0284 -0.0247 633 PHE A N 4701 C CA . PHE A 640 ? 0.2546 0.2536 0.4171 -0.0316 -0.0370 -0.0321 633 PHE A CA 4702 C C . PHE A 640 ? 0.2714 0.2630 0.4268 -0.0274 -0.0472 -0.0374 633 PHE A C 4703 O O . PHE A 640 ? 0.2708 0.2646 0.4270 -0.0236 -0.0561 -0.0442 633 PHE A O 4704 C CB . PHE A 640 ? 0.2616 0.2612 0.4478 -0.0385 -0.0334 -0.0313 633 PHE A CB 4705 C CG . PHE A 640 ? 0.2771 0.2862 0.4743 -0.0415 -0.0257 -0.0290 633 PHE A CG 4706 C CD1 . PHE A 640 ? 0.2799 0.2982 0.4861 -0.0395 -0.0306 -0.0345 633 PHE A CD1 4707 C CD2 . PHE A 640 ? 0.3037 0.3122 0.5018 -0.0458 -0.0135 -0.0215 633 PHE A CD2 4708 C CE1 . PHE A 640 ? 0.3005 0.3280 0.5176 -0.0418 -0.0233 -0.0326 633 PHE A CE1 4709 C CE2 . PHE A 640 ? 0.3180 0.3353 0.5258 -0.0481 -0.0057 -0.0197 633 PHE A CE2 4710 C CZ . PHE A 640 ? 0.2901 0.3172 0.5080 -0.0460 -0.0106 -0.0254 633 PHE A CZ 4711 N N . SER A 641 ? 0.2721 0.2545 0.4186 -0.0275 -0.0458 -0.0342 634 SER A N 4712 C CA . SER A 641 ? 0.2793 0.2539 0.4162 -0.0227 -0.0542 -0.0387 634 SER A CA 4713 C C . SER A 641 ? 0.2687 0.2461 0.3874 -0.0156 -0.0580 -0.0413 634 SER A C 4714 O O . SER A 641 ? 0.2669 0.2425 0.3827 -0.0112 -0.0667 -0.0479 634 SER A O 4715 C CB . SER A 641 ? 0.2814 0.2462 0.4111 -0.0236 -0.0506 -0.0336 634 SER A CB 4716 O OG . SER A 641 ? 0.2931 0.2506 0.4129 -0.0185 -0.0579 -0.0380 634 SER A OG 4717 N N . ALA A 642 ? 0.2498 0.2312 0.3559 -0.0143 -0.0513 -0.0360 635 ALA A N 4718 C CA . ALA A 642 ? 0.2368 0.2210 0.3267 -0.0082 -0.0534 -0.0375 635 ALA A CA 4719 C C . ALA A 642 ? 0.2443 0.2350 0.3391 -0.0061 -0.0585 -0.0429 635 ALA A C 4720 O O . ALA A 642 ? 0.2511 0.2405 0.3359 -0.0004 -0.0646 -0.0472 635 ALA A O 4721 C CB . ALA A 642 ? 0.2315 0.2193 0.3105 -0.0084 -0.0449 -0.0308 635 ALA A CB 4722 N N . VAL A 643 ? 0.2336 0.2308 0.3439 -0.0105 -0.0561 -0.0425 636 VAL A N 4723 C CA . VAL A 643 ? 0.2315 0.2353 0.3483 -0.0086 -0.0610 -0.0473 636 VAL A CA 4724 C C . VAL A 643 ? 0.2547 0.2544 0.3784 -0.0065 -0.0723 -0.0551 636 VAL A C 4725 O O . VAL A 643 ? 0.2453 0.2459 0.3628 -0.0012 -0.0796 -0.0601 636 VAL A O 4726 C CB . VAL A 643 ? 0.2242 0.2359 0.3573 -0.0138 -0.0552 -0.0451 636 VAL A CB 4727 C CG1 . VAL A 643 ? 0.2436 0.2619 0.3887 -0.0122 -0.0620 -0.0510 636 VAL A CG1 4728 C CG2 . VAL A 643 ? 0.2441 0.2597 0.3671 -0.0144 -0.0453 -0.0386 636 VAL A CG2 4729 N N . LYS A 644 ? 0.2583 0.2530 0.3944 -0.0106 -0.0739 -0.0562 637 LYS A N 4730 C CA . LYS A 644 ? 0.2724 0.2614 0.4146 -0.0088 -0.0850 -0.0639 637 LYS A CA 4731 C C . LYS A 644 ? 0.2772 0.2590 0.3980 -0.0015 -0.0905 -0.0670 637 LYS A C 4732 O O . LYS A 644 ? 0.2770 0.2570 0.3942 0.0032 -0.0998 -0.0737 637 LYS A O 4733 C CB . LYS A 644 ? 0.2811 0.2643 0.4388 -0.0149 -0.0840 -0.0633 637 LYS A CB 4734 C CG . LYS A 644 ? 0.3460 0.3221 0.5117 -0.0137 -0.0958 -0.0717 637 LYS A CG 4735 C CD . LYS A 644 ? 0.4004 0.3698 0.5818 -0.0203 -0.0935 -0.0700 637 LYS A CD 4736 C CE . LYS A 644 ? 0.4722 0.4338 0.6624 -0.0194 -0.1056 -0.0789 637 LYS A CE 4737 N NZ . LYS A 644 ? 0.4954 0.4473 0.6627 -0.0125 -0.1101 -0.0815 637 LYS A NZ 4738 N N . ASN A 645 ? 0.2760 0.2533 0.3824 -0.0003 -0.0846 -0.0621 638 ASN A N 4739 C CA . ASN A 645 ? 0.2931 0.2642 0.3798 0.0067 -0.0882 -0.0644 638 ASN A CA 4740 C C . ASN A 645 ? 0.2928 0.2687 0.3661 0.0124 -0.0892 -0.0653 638 ASN A C 4741 O O . ASN A 645 ? 0.2938 0.2653 0.3563 0.0186 -0.0961 -0.0706 638 ASN A O 4742 C CB . ASN A 645 ? 0.2888 0.2559 0.3649 0.0067 -0.0811 -0.0584 638 ASN A CB 4743 C CG . ASN A 645 ? 0.3271 0.2866 0.4121 0.0029 -0.0812 -0.0579 638 ASN A CG 4744 O OD1 . ASN A 645 ? 0.3097 0.2659 0.4084 0.0005 -0.0874 -0.0628 638 ASN A OD1 4745 N ND2 . ASN A 645 ? 0.3318 0.2880 0.4098 0.0023 -0.0750 -0.0521 638 ASN A ND2 4746 N N . PHE A 646 ? 0.2699 0.2540 0.3435 0.0105 -0.0822 -0.0603 639 PHE A N 4747 C CA . PHE A 646 ? 0.2703 0.2588 0.3331 0.0153 -0.0827 -0.0607 639 PHE A CA 4748 C C . PHE A 646 ? 0.2726 0.2614 0.3410 0.0180 -0.0928 -0.0678 639 PHE A C 4749 O O . PHE A 646 ? 0.2856 0.2718 0.3402 0.0246 -0.0977 -0.0710 639 PHE A O 4750 C CB . PHE A 646 ? 0.2433 0.2405 0.3097 0.0119 -0.0744 -0.0550 639 PHE A CB 4751 C CG . PHE A 646 ? 0.2677 0.2684 0.3217 0.0167 -0.0736 -0.0543 639 PHE A CG 4752 C CD1 . PHE A 646 ? 0.2663 0.2672 0.3065 0.0185 -0.0671 -0.0495 639 PHE A CD1 4753 C CD2 . PHE A 646 ? 0.2417 0.2451 0.2982 0.0196 -0.0796 -0.0584 639 PHE A CD2 4754 C CE1 . PHE A 646 ? 0.3081 0.3117 0.3377 0.0226 -0.0658 -0.0486 639 PHE A CE1 4755 C CE2 . PHE A 646 ? 0.2648 0.2703 0.3092 0.0243 -0.0788 -0.0574 639 PHE A CE2 4756 C CZ . PHE A 646 ? 0.2737 0.2791 0.3045 0.0256 -0.0714 -0.0523 639 PHE A CZ 4757 N N . THR A 647 ? 0.2798 0.2717 0.3686 0.0131 -0.0958 -0.0702 640 THR A N 4758 C CA . THR A 647 ? 0.2813 0.2741 0.3782 0.0155 -0.1065 -0.0775 640 THR A CA 4759 C C . THR A 647 ? 0.3048 0.2877 0.3907 0.0213 -0.1165 -0.0844 640 THR A C 4760 O O . THR A 647 ? 0.3168 0.2979 0.3922 0.0277 -0.1240 -0.0889 640 THR A O 4761 C CB . THR A 647 ? 0.2816 0.2796 0.4053 0.0086 -0.1076 -0.0789 640 THR A CB 4762 O OG1 . THR A 647 ? 0.2731 0.2794 0.4041 0.0039 -0.0969 -0.0723 640 THR A OG1 4763 C CG2 . THR A 647 ? 0.3009 0.3015 0.4351 0.0112 -0.1192 -0.0866 640 THR A CG2 4764 N N . GLU A 648 ? 0.3098 0.2856 0.3972 0.0193 -0.1166 -0.0850 641 GLU A N 4765 C CA . GLU A 648 ? 0.3475 0.3130 0.4250 0.0245 -0.1257 -0.0918 641 GLU A CA 4766 C C . GLU A 648 ? 0.3405 0.3015 0.3916 0.0327 -0.1246 -0.0913 641 GLU A C 4767 O O . GLU A 648 ? 0.3393 0.2948 0.3785 0.0395 -0.1331 -0.0974 641 GLU A O 4768 C CB . GLU A 648 ? 0.3479 0.3065 0.4339 0.0202 -0.1250 -0.0920 641 GLU A CB 4769 C CG . GLU A 648 ? 0.4532 0.4147 0.5672 0.0128 -0.1288 -0.0947 641 GLU A CG 4770 C CD . GLU A 648 ? 0.5082 0.4637 0.6339 0.0068 -0.1255 -0.0928 641 GLU A CD 4771 O OE1 . GLU A 648 ? 0.5267 0.4849 0.6760 0.0001 -0.1263 -0.0934 641 GLU A OE1 4772 O OE2 . GLU A 648 ? 0.5688 0.5170 0.6808 0.0090 -0.1221 -0.0904 641 GLU A OE2 4773 N N . ILE A 649 ? 0.3232 0.2860 0.3647 0.0323 -0.1142 -0.0841 642 ILE A N 4774 C CA . ILE A 649 ? 0.3226 0.2815 0.3412 0.0395 -0.1116 -0.0830 642 ILE A CA 4775 C C . ILE A 649 ? 0.3233 0.2860 0.3320 0.0443 -0.1130 -0.0832 642 ILE A C 4776 O O . ILE A 649 ? 0.3273 0.2839 0.3175 0.0519 -0.1163 -0.0861 642 ILE A O 4777 C CB . ILE A 649 ? 0.3211 0.2820 0.3348 0.0375 -0.1005 -0.0753 642 ILE A CB 4778 C CG1 . ILE A 649 ? 0.3308 0.2852 0.3491 0.0350 -0.1001 -0.0755 642 ILE A CG1 4779 C CG2 . ILE A 649 ? 0.3234 0.2830 0.3163 0.0442 -0.0963 -0.0731 642 ILE A CG2 4780 C CD1 . ILE A 649 ? 0.3359 0.2935 0.3541 0.0316 -0.0897 -0.0673 642 ILE A CD1 4781 N N . ALA A 650 ? 0.3112 0.2829 0.3311 0.0403 -0.1102 -0.0801 643 ALA A N 4782 C CA . ALA A 650 ? 0.3309 0.3059 0.3436 0.0446 -0.1123 -0.0804 643 ALA A CA 4783 C C . ALA A 650 ? 0.3452 0.3151 0.3554 0.0497 -0.1250 -0.0885 643 ALA A C 4784 O O . ALA A 650 ? 0.3544 0.3207 0.3475 0.0570 -0.1282 -0.0900 643 ALA A O 4785 C CB . ALA A 650 ? 0.3289 0.3149 0.3570 0.0390 -0.1073 -0.0761 643 ALA A CB 4786 N N . SER A 651 ? 0.3620 0.3311 0.3891 0.0462 -0.1325 -0.0939 644 SER A N 4787 C CA . SER A 651 ? 0.3830 0.3471 0.4093 0.0510 -0.1461 -0.1025 644 SER A CA 4788 C C . SER A 651 ? 0.3936 0.3457 0.3958 0.0591 -0.1502 -0.1064 644 SER A C 4789 O O . SER A 651 ? 0.4131 0.3601 0.4002 0.0667 -0.1578 -0.1107 644 SER A O 4790 C CB . SER A 651 ? 0.3895 0.3546 0.4405 0.0449 -0.1529 -0.1075 644 SER A CB 4791 O OG . SER A 651 ? 0.4852 0.4451 0.5352 0.0497 -0.1671 -0.1165 644 SER A OG 4792 N N . LYS A 652 ? 0.3799 0.3270 0.3773 0.0581 -0.1449 -0.1048 645 LYS A N 4793 C CA A LYS A 652 ? 0.3982 0.3340 0.3733 0.0658 -0.1474 -0.1084 645 LYS A CA 4794 C CA B LYS A 652 ? 0.3995 0.3354 0.3747 0.0658 -0.1475 -0.1084 645 LYS A CA 4795 C C . LYS A 652 ? 0.4011 0.3361 0.3530 0.0726 -0.1410 -0.1040 645 LYS A C 4796 O O . LYS A 652 ? 0.4119 0.3385 0.3436 0.0811 -0.1459 -0.1080 645 LYS A O 4797 C CB A LYS A 652 ? 0.3960 0.3271 0.3735 0.0630 -0.1428 -0.1075 645 LYS A CB 4798 C CB B LYS A 652 ? 0.3991 0.3302 0.3769 0.0630 -0.1431 -0.1077 645 LYS A CB 4799 C CG A LYS A 652 ? 0.4217 0.3491 0.4174 0.0585 -0.1513 -0.1138 645 LYS A CG 4800 C CG B LYS A 652 ? 0.4287 0.3565 0.4257 0.0582 -0.1517 -0.1139 645 LYS A CG 4801 C CD A LYS A 652 ? 0.4539 0.3714 0.4406 0.0652 -0.1650 -0.1240 645 LYS A CD 4802 C CD B LYS A 652 ? 0.4564 0.3788 0.4564 0.0553 -0.1472 -0.1125 645 LYS A CD 4803 C CE A LYS A 652 ? 0.4891 0.4039 0.4974 0.0600 -0.1744 -0.1307 645 LYS A CE 4804 C CE B LYS A 652 ? 0.5074 0.4258 0.5272 0.0503 -0.1556 -0.1186 645 LYS A CE 4805 N NZ A LYS A 652 ? 0.5427 0.4492 0.5447 0.0662 -0.1897 -0.1415 645 LYS A NZ 4806 N NZ B LYS A 652 ? 0.4947 0.4128 0.5270 0.0435 -0.1482 -0.1136 645 LYS A NZ 4807 N N . PHE A 653 ? 0.3780 0.3213 0.3325 0.0691 -0.1299 -0.0957 646 PHE A N 4808 C CA . PHE A 653 ? 0.3771 0.3204 0.3126 0.0745 -0.1231 -0.0909 646 PHE A CA 4809 C C . PHE A 653 ? 0.3929 0.3352 0.3198 0.0800 -0.1302 -0.0935 646 PHE A C 4810 O O . PHE A 653 ? 0.4087 0.3443 0.3131 0.0881 -0.1298 -0.0935 646 PHE A O 4811 C CB . PHE A 653 ? 0.3708 0.3239 0.3145 0.0686 -0.1114 -0.0823 646 PHE A CB 4812 C CG . PHE A 653 ? 0.3640 0.3179 0.2915 0.0731 -0.1040 -0.0770 646 PHE A CG 4813 C CD1 . PHE A 653 ? 0.3250 0.2749 0.2384 0.0766 -0.0966 -0.0741 646 PHE A CD1 4814 C CD2 . PHE A 653 ? 0.3852 0.3435 0.3125 0.0739 -0.1045 -0.0751 646 PHE A CD2 4815 C CE1 . PHE A 653 ? 0.3657 0.3164 0.2660 0.0804 -0.0894 -0.0692 646 PHE A CE1 4816 C CE2 . PHE A 653 ? 0.3693 0.3276 0.2822 0.0779 -0.0974 -0.0700 646 PHE A CE2 4817 C CZ . PHE A 653 ? 0.3631 0.3177 0.2631 0.0808 -0.0897 -0.0670 646 PHE A CZ 4818 N N . SER A 654 ? 0.3706 0.3192 0.3150 0.0760 -0.1360 -0.0954 647 SER A N 4819 C CA . SER A 654 ? 0.4110 0.3589 0.3501 0.0810 -0.1444 -0.0984 647 SER A CA 4820 C C . SER A 654 ? 0.4404 0.3763 0.3619 0.0897 -0.1556 -0.1062 647 SER A C 4821 O O . SER A 654 ? 0.4674 0.3981 0.3701 0.0974 -0.1588 -0.1067 647 SER A O 4822 C CB . SER A 654 ? 0.3898 0.3466 0.3546 0.0749 -0.1498 -0.1003 647 SER A CB 4823 O OG A SER A 654 ? 0.3719 0.3390 0.3488 0.0684 -0.1391 -0.0929 647 SER A OG 4824 O OG B SER A 654 ? 0.4155 0.3743 0.3771 0.0790 -0.1547 -0.1007 647 SER A OG 4825 N N . GLU A 655 ? 0.4555 0.3863 0.3831 0.0884 -0.1620 -0.1125 648 GLU A N 4826 C CA . GLU A 655 ? 0.4959 0.4143 0.4068 0.0964 -0.1730 -0.1208 648 GLU A CA 4827 C C . GLU A 655 ? 0.4992 0.4084 0.3801 0.1047 -0.1665 -0.1185 648 GLU A C 4828 O O . GLU A 655 ? 0.5187 0.4193 0.3778 0.1138 -0.1726 -0.1218 648 GLU A O 4829 C CB . GLU A 655 ? 0.5117 0.4262 0.4358 0.0926 -0.1791 -0.1273 648 GLU A CB 4830 C CG . GLU A 655 ? 0.5861 0.5072 0.5385 0.0858 -0.1881 -0.1316 648 GLU A CG 4831 C CD . GLU A 655 ? 0.6867 0.6045 0.6556 0.0805 -0.1924 -0.1368 648 GLU A CD 4832 O OE1 . GLU A 655 ? 0.7052 0.6128 0.6607 0.0841 -0.1928 -0.1400 648 GLU A OE1 4833 O OE2 . GLU A 655 ? 0.7487 0.6741 0.7449 0.0726 -0.1950 -0.1376 648 GLU A OE2 4834 N N . ARG A 656 ? 0.4753 0.3864 0.3549 0.1020 -0.1538 -0.1125 649 ARG A N 4835 C CA . ARG A 656 ? 0.4862 0.3901 0.3401 0.1093 -0.1459 -0.1095 649 ARG A CA 4836 C C . ARG A 656 ? 0.4910 0.3964 0.3310 0.1137 -0.1412 -0.1040 649 ARG A C 4837 O O . ARG A 656 ? 0.4990 0.3953 0.3141 0.1226 -0.1403 -0.1044 649 ARG A O 4838 C CB . ARG A 656 ? 0.4791 0.3859 0.3375 0.1052 -0.1337 -0.1043 649 ARG A CB 4839 C CG . ARG A 656 ? 0.4877 0.3912 0.3579 0.1017 -0.1382 -0.1095 649 ARG A CG 4840 C CD . ARG A 656 ? 0.4795 0.3817 0.3462 0.1013 -0.1275 -0.1056 649 ARG A CD 4841 N NE . ARG A 656 ? 0.4454 0.3584 0.3208 0.0958 -0.1158 -0.0963 649 ARG A NE 4842 C CZ . ARG A 656 ? 0.4279 0.3494 0.3248 0.0868 -0.1131 -0.0928 649 ARG A CZ 4843 N NH1 . ARG A 656 ? 0.4171 0.3380 0.3302 0.0819 -0.1208 -0.0974 649 ARG A NH1 4844 N NH2 . ARG A 656 ? 0.4040 0.3342 0.3061 0.0828 -0.1030 -0.0848 649 ARG A NH2 4845 N N . LEU A 657 ? 0.4789 0.3951 0.3347 0.1077 -0.1382 -0.0990 650 LEU A N 4846 C CA . LEU A 657 ? 0.5127 0.4306 0.3578 0.1111 -0.1335 -0.0934 650 LEU A CA 4847 C C . LEU A 657 ? 0.5579 0.4676 0.3876 0.1195 -0.1454 -0.0987 650 LEU A C 4848 O O . LEU A 657 ? 0.5492 0.4531 0.3575 0.1267 -0.1422 -0.0954 650 LEU A O 4849 C CB . LEU A 657 ? 0.4877 0.4187 0.3550 0.1027 -0.1291 -0.0881 650 LEU A CB 4850 C CG . LEU A 657 ? 0.4991 0.4337 0.3598 0.1037 -0.1205 -0.0805 650 LEU A CG 4851 C CD1 . LEU A 657 ? 0.4261 0.3604 0.2778 0.1036 -0.1068 -0.0741 650 LEU A CD1 4852 C CD2 . LEU A 657 ? 0.4482 0.3951 0.3331 0.0957 -0.1199 -0.0779 650 LEU A CD2 4853 N N . GLN A 658 ? 0.6013 0.5097 0.4414 0.1189 -0.1590 -0.1068 651 GLN A N 4854 C CA . GLN A 658 ? 0.6795 0.5794 0.5057 0.1272 -0.1727 -0.1133 651 GLN A CA 4855 C C . GLN A 658 ? 0.7198 0.6045 0.5168 0.1370 -0.1753 -0.1178 651 GLN A C 4856 O O . GLN A 658 ? 0.7586 0.6342 0.5324 0.1463 -0.1805 -0.1192 651 GLN A O 4857 C CB . GLN A 658 ? 0.6866 0.5898 0.5352 0.1232 -0.1871 -0.1216 651 GLN A CB 4858 C CG . GLN A 658 ? 0.7272 0.6446 0.6042 0.1149 -0.1867 -0.1186 651 GLN A CG 4859 C CD . GLN A 658 ? 0.8133 0.7314 0.6859 0.1199 -0.1938 -0.1185 651 GLN A CD 4860 O OE1 . GLN A 658 ? 0.8481 0.7737 0.7259 0.1175 -0.1860 -0.1115 651 GLN A OE1 4861 N NE2 . GLN A 658 ? 0.8627 0.7727 0.7260 0.1271 -0.2090 -0.1265 651 GLN A NE2 4862 N N . ASP A 659 ? 0.7301 0.6119 0.5279 0.1352 -0.1715 -0.1198 652 ASP A N 4863 C CA . ASP A 659 ? 0.7645 0.6322 0.5401 0.1434 -0.1763 -0.1265 652 ASP A CA 4864 C C . ASP A 659 ? 0.7730 0.6331 0.5228 0.1500 -0.1637 -0.1219 652 ASP A C 4865 O O . ASP A 659 ? 0.7917 0.6393 0.5211 0.1577 -0.1675 -0.1277 652 ASP A O 4866 C CB . ASP A 659 ? 0.7701 0.6375 0.5628 0.1381 -0.1816 -0.1331 652 ASP A CB 4867 C CG . ASP A 659 ? 0.8224 0.6921 0.6349 0.1347 -0.1977 -0.1412 652 ASP A CG 4868 O OD1 . ASP A 659 ? 0.8735 0.7434 0.7032 0.1293 -0.2022 -0.1463 652 ASP A OD1 4869 O OD2 . ASP A 659 ? 0.8488 0.7201 0.6610 0.1371 -0.2057 -0.1423 652 ASP A OD2 4870 N N . PHE A 660 ? 0.7526 0.6200 0.5039 0.1470 -0.1488 -0.1120 653 PHE A N 4871 C CA . PHE A 660 ? 0.7611 0.6215 0.4881 0.1538 -0.1365 -0.1072 653 PHE A CA 4872 C C . PHE A 660 ? 0.7931 0.6459 0.4945 0.1629 -0.1363 -0.1044 653 PHE A C 4873 O O . PHE A 660 ? 0.8446 0.6892 0.5218 0.1703 -0.1269 -0.1008 653 PHE A O 4874 C CB . PHE A 660 ? 0.7276 0.5990 0.4688 0.1466 -0.1207 -0.0981 653 PHE A CB 4875 C CG . PHE A 660 ? 0.6585 0.5380 0.4044 0.1436 -0.1137 -0.0897 653 PHE A CG 4876 C CD1 . PHE A 660 ? 0.6268 0.5038 0.3561 0.1481 -0.1016 -0.0825 653 PHE A CD1 4877 C CD2 . PHE A 660 ? 0.6314 0.5210 0.3992 0.1363 -0.1189 -0.0890 653 PHE A CD2 4878 C CE1 . PHE A 660 ? 0.6729 0.5567 0.4071 0.1452 -0.0953 -0.0749 653 PHE A CE1 4879 C CE2 . PHE A 660 ? 0.6615 0.5582 0.4337 0.1337 -0.1125 -0.0815 653 PHE A CE2 4880 C CZ . PHE A 660 ? 0.6663 0.5598 0.4217 0.1381 -0.1009 -0.0745 653 PHE A CZ 4881 N N A SER A 663 ? 0.5426 0.3614 0.1409 0.1951 -0.1015 -0.0849 656 SER A N 4882 N N B SER A 663 ? 0.5148 0.3485 0.1280 0.1871 -0.0806 -0.0648 656 SER A N 4883 C CA A SER A 663 ? 0.5607 0.3748 0.1406 0.2001 -0.0851 -0.0765 656 SER A CA 4884 C CA B SER A 663 ? 0.5354 0.3618 0.1272 0.1933 -0.0647 -0.0570 656 SER A CA 4885 C C A SER A 663 ? 0.5417 0.3664 0.1390 0.1932 -0.0686 -0.0702 656 SER A C 4886 C C B SER A 663 ? 0.5470 0.3762 0.1425 0.1918 -0.0509 -0.0551 656 SER A C 4887 O O A SER A 663 ? 0.5509 0.3728 0.1361 0.1968 -0.0540 -0.0631 656 SER A O 4888 O O B SER A 663 ? 0.5545 0.3766 0.1313 0.1980 -0.0378 -0.0499 656 SER A O 4889 C CB A SER A 663 ? 0.5733 0.3700 0.1195 0.2125 -0.0865 -0.0814 656 SER A CB 4890 C CB B SER A 663 ? 0.5557 0.3638 0.1105 0.2065 -0.0693 -0.0589 656 SER A CB 4891 O OG A SER A 663 ? 0.5689 0.3658 0.1224 0.2111 -0.0893 -0.0887 656 SER A OG 4892 O OG B SER A 663 ? 0.5872 0.3867 0.1274 0.2124 -0.0707 -0.0658 656 SER A OG 4893 N N A ASN A 664 ? 0.5153 0.3514 0.1404 0.1839 -0.0709 -0.0728 657 ASN A N 4894 N N B ASN A 664 ? 0.5347 0.3736 0.1535 0.1842 -0.0534 -0.0591 657 ASN A N 4895 C CA A ASN A 664 ? 0.5017 0.3469 0.1424 0.1782 -0.0574 -0.0681 657 ASN A CA 4896 C CA B ASN A 664 ? 0.5559 0.3998 0.1832 0.1816 -0.0408 -0.0568 657 ASN A CA 4897 C C A ASN A 664 ? 0.4794 0.3391 0.1443 0.1683 -0.0502 -0.0602 657 ASN A C 4898 C C B ASN A 664 ? 0.5256 0.3850 0.1801 0.1710 -0.0323 -0.0492 657 ASN A C 4899 O O A ASN A 664 ? 0.4598 0.3293 0.1478 0.1599 -0.0572 -0.0618 657 ASN A O 4900 O O B ASN A 664 ? 0.5060 0.3757 0.1843 0.1623 -0.0390 -0.0511 657 ASN A O 4901 C CB A ASN A 664 ? 0.4979 0.3459 0.1532 0.1743 -0.0630 -0.0752 657 ASN A CB 4902 C CB B ASN A 664 ? 0.5591 0.4025 0.1936 0.1807 -0.0487 -0.0658 657 ASN A CB 4903 C CG A ASN A 664 ? 0.4838 0.3378 0.1490 0.1715 -0.0495 -0.0712 657 ASN A CG 4904 C CG B ASN A 664 ? 0.5857 0.4327 0.2267 0.1796 -0.0364 -0.0641 657 ASN A CG 4905 O OD1 A ASN A 664 ? 0.4752 0.3381 0.1511 0.1669 -0.0382 -0.0630 657 ASN A OD1 4906 O OD1 B ASN A 664 ? 0.6272 0.4827 0.2796 0.1754 -0.0234 -0.0563 657 ASN A OD1 4907 N ND2 A ASN A 664 ? 0.5288 0.3776 0.1904 0.1745 -0.0508 -0.0771 657 ASN A ND2 4908 N ND2 B ASN A 664 ? 0.5651 0.4058 0.2010 0.1832 -0.0412 -0.0718 657 ASN A ND2 4909 N N A PRO A 665 ? 0.4814 0.3426 0.1417 0.1692 -0.0357 -0.0515 658 PRO A N 4910 N N B PRO A 665 ? 0.5285 0.3890 0.1792 0.1718 -0.0176 -0.0406 658 PRO A N 4911 C CA A PRO A 665 ? 0.4573 0.3314 0.1399 0.1600 -0.0304 -0.0447 658 PRO A CA 4912 C CA B PRO A 665 ? 0.5010 0.3745 0.1750 0.1625 -0.0108 -0.0335 658 PRO A CA 4913 C C A PRO A 665 ? 0.4365 0.3232 0.1454 0.1509 -0.0265 -0.0441 658 PRO A C 4914 C C B PRO A 665 ? 0.4842 0.3708 0.1859 0.1532 -0.0105 -0.0349 658 PRO A C 4915 O O A PRO A 665 ? 0.4346 0.3322 0.1640 0.1426 -0.0260 -0.0406 658 PRO A O 4916 O O B PRO A 665 ? 0.4590 0.3556 0.1812 0.1448 -0.0142 -0.0338 658 PRO A O 4917 C CB A PRO A 665 ? 0.4531 0.3240 0.1230 0.1640 -0.0158 -0.0360 658 PRO A CB 4918 C CB B PRO A 665 ? 0.5215 0.3923 0.1855 0.1660 0.0055 -0.0251 658 PRO A CB 4919 C CG A PRO A 665 ? 0.4733 0.3352 0.1248 0.1719 -0.0089 -0.0377 658 PRO A CG 4920 C CG B PRO A 665 ? 0.5388 0.3936 0.1704 0.1780 0.0063 -0.0270 658 PRO A CG 4921 C CD A PRO A 665 ? 0.5078 0.3596 0.1447 0.1779 -0.0234 -0.0475 658 PRO A CD 4922 C CD B PRO A 665 ? 0.5437 0.3926 0.1679 0.1816 -0.0068 -0.0371 658 PRO A CD 4923 N N A ILE A 666 ? 0.4418 0.3268 0.1499 0.1528 -0.0235 -0.0472 659 ILE A N 4924 N N B ILE A 666 ? 0.4870 0.3728 0.1886 0.1549 -0.0061 -0.0374 659 ILE A N 4925 C CA A ILE A 666 ? 0.4159 0.3123 0.1486 0.1446 -0.0204 -0.0465 659 ILE A CA 4926 C CA B ILE A 666 ? 0.4766 0.3739 0.2034 0.1467 -0.0058 -0.0382 659 ILE A CA 4927 C C A ILE A 666 ? 0.3976 0.2985 0.1465 0.1381 -0.0334 -0.0520 659 ILE A C 4928 C C B ILE A 666 ? 0.4640 0.3633 0.2018 0.1423 -0.0201 -0.0452 659 ILE A C 4929 O O A ILE A 666 ? 0.3716 0.2835 0.1425 0.1294 -0.0330 -0.0497 659 ILE A O 4930 O O B ILE A 666 ? 0.4442 0.3541 0.2041 0.1336 -0.0220 -0.0441 659 ILE A O 4931 C CB A ILE A 666 ? 0.4310 0.3250 0.1612 0.1479 -0.0141 -0.0484 659 ILE A CB 4932 C CB B ILE A 666 ? 0.4817 0.3797 0.2095 0.1489 0.0045 -0.0373 659 ILE A CB 4933 C CG1 A ILE A 666 ? 0.4649 0.3509 0.1740 0.1569 -0.0024 -0.0451 659 ILE A CG1 4934 C CG1 B ILE A 666 ? 0.4939 0.4006 0.2334 0.1450 0.0179 -0.0287 659 ILE A CG1 4935 C CG2 A ILE A 666 ? 0.3817 0.2889 0.1384 0.1390 -0.0091 -0.0452 659 ILE A CG2 4936 C CG2 B ILE A 666 ? 0.4732 0.3777 0.2198 0.1435 -0.0002 -0.0416 659 ILE A CG2 4937 C CD1 A ILE A 666 ? 0.4667 0.3602 0.1836 0.1539 0.0113 -0.0358 659 ILE A CD1 4938 C CD1 B ILE A 666 ? 0.4838 0.4042 0.2513 0.1345 0.0164 -0.0273 659 ILE A CD1 4939 N N A VAL A 667 ? 0.4019 0.2940 0.1400 0.1426 -0.0448 -0.0596 660 VAL A N 4940 N N B VAL A 667 ? 0.4776 0.3667 0.2005 0.1482 -0.0303 -0.0525 660 VAL A N 4941 C CA A VAL A 667 ? 0.3995 0.2953 0.1534 0.1368 -0.0571 -0.0650 660 VAL A CA 4942 C CA B VAL A 667 ? 0.4616 0.3530 0.1972 0.1435 -0.0441 -0.0590 660 VAL A CA 4943 C C A VAL A 667 ? 0.3906 0.2933 0.1549 0.1317 -0.0606 -0.0619 660 VAL A C 4944 C C B VAL A 667 ? 0.4514 0.3504 0.2004 0.1371 -0.0493 -0.0566 660 VAL A C 4945 O O A VAL A 667 ? 0.3570 0.2689 0.1429 0.1233 -0.0639 -0.0619 660 VAL A O 4946 O O B VAL A 667 ? 0.4382 0.3462 0.2089 0.1287 -0.0533 -0.0574 660 VAL A O 4947 C CB A VAL A 667 ? 0.4152 0.2995 0.1554 0.1431 -0.0694 -0.0742 660 VAL A CB 4948 C CB B VAL A 667 ? 0.4815 0.3601 0.1992 0.1511 -0.0555 -0.0680 660 VAL A CB 4949 C CG1 A VAL A 667 ? 0.4008 0.2894 0.1594 0.1366 -0.0822 -0.0795 660 VAL A CG1 4950 C CG1 B VAL A 667 ? 0.4690 0.3504 0.2017 0.1457 -0.0703 -0.0743 660 VAL A CG1 4951 C CG2 A VAL A 667 ? 0.4302 0.3082 0.1629 0.1473 -0.0661 -0.0777 660 VAL A CG2 4952 C CG2 B VAL A 667 ? 0.5017 0.3740 0.2114 0.1559 -0.0517 -0.0717 660 VAL A CG2 4953 N N A LEU A 668 ? 0.4024 0.3003 0.1509 0.1370 -0.0591 -0.0590 661 LEU A N 4954 N N B LEU A 668 ? 0.4596 0.3546 0.1955 0.1411 -0.0487 -0.0535 661 LEU A N 4955 C CA A LEU A 668 ? 0.4011 0.3045 0.1579 0.1332 -0.0619 -0.0558 661 LEU A CA 4956 C CA B LEU A 668 ? 0.4488 0.3508 0.1970 0.1357 -0.0526 -0.0509 661 LEU A CA 4957 C C A LEU A 668 ? 0.3858 0.3018 0.1632 0.1243 -0.0529 -0.0492 661 LEU A C 4958 C C B LEU A 668 ? 0.4279 0.3426 0.1978 0.1266 -0.0437 -0.0447 661 LEU A C 4959 O O A LEU A 668 ? 0.3705 0.2950 0.1671 0.1170 -0.0573 -0.0496 661 LEU A O 4960 O O B LEU A 668 ? 0.4048 0.3279 0.1926 0.1195 -0.0477 -0.0443 661 LEU A O 4961 C CB A LEU A 668 ? 0.4196 0.3142 0.1537 0.1413 -0.0606 -0.0529 661 LEU A CB 4962 C CB B LEU A 668 ? 0.4675 0.3617 0.1961 0.1425 -0.0521 -0.0477 661 LEU A CB 4963 C CG A LEU A 668 ? 0.4089 0.3086 0.1495 0.1383 -0.0600 -0.0476 661 LEU A CG 4964 C CG B LEU A 668 ? 0.4457 0.3462 0.1848 0.1382 -0.0536 -0.0436 661 LEU A CG 4965 C CD1 A LEU A 668 ? 0.3444 0.2484 0.0987 0.1346 -0.0732 -0.0525 661 LEU A CD1 4966 C CD1 B LEU A 668 ? 0.3965 0.3031 0.1532 0.1328 -0.0663 -0.0490 661 LEU A CD1 4967 C CD2 A LEU A 668 ? 0.4051 0.2941 0.1206 0.1471 -0.0567 -0.0437 661 LEU A CD2 4968 C CD2 B LEU A 668 ? 0.4448 0.3349 0.1607 0.1466 -0.0534 -0.0407 661 LEU A CD2 4969 N N A ARG A 669 ? 0.3924 0.3094 0.1663 0.1251 -0.0403 -0.0435 662 ARG A N 4970 N N B ARG A 669 ? 0.4214 0.3377 0.1902 0.1270 -0.0316 -0.0398 662 ARG A N 4971 C CA A ARG A 669 ? 0.3766 0.3048 0.1685 0.1174 -0.0317 -0.0373 662 ARG A CA 4972 C CA B ARG A 669 ? 0.4026 0.3306 0.1918 0.1186 -0.0242 -0.0344 662 ARG A CA 4973 C C A ARG A 669 ? 0.3741 0.3100 0.1854 0.1104 -0.0333 -0.0395 662 ARG A C 4974 C C B ARG A 669 ? 0.3882 0.3242 0.1980 0.1111 -0.0293 -0.0378 662 ARG A C 4975 O O A ARG A 669 ? 0.3549 0.3000 0.1839 0.1028 -0.0334 -0.0374 662 ARG A O 4976 O O B ARG A 669 ? 0.3727 0.3178 0.1996 0.1036 -0.0290 -0.0353 662 ARG A O 4977 C CB A ARG A 669 ? 0.3768 0.3041 0.1615 0.1202 -0.0182 -0.0310 662 ARG A CB 4978 C CB B ARG A 669 ? 0.4052 0.3335 0.1903 0.1208 -0.0105 -0.0288 662 ARG A CB 4979 C CG A ARG A 669 ? 0.3542 0.2931 0.1594 0.1122 -0.0103 -0.0261 662 ARG A CG 4980 C CG B ARG A 669 ? 0.3697 0.3096 0.1752 0.1128 -0.0031 -0.0235 662 ARG A CG 4981 C CD A ARG A 669 ? 0.3322 0.2768 0.1462 0.1074 -0.0084 -0.0213 662 ARG A CD 4982 C CD B ARG A 669 ? 0.4250 0.3677 0.2328 0.1105 0.0015 -0.0175 662 ARG A CD 4983 N NE A ARG A 669 ? 0.3673 0.3194 0.1935 0.1029 0.0018 -0.0160 662 ARG A NE 4984 N NE B ARG A 669 ? 0.4141 0.3653 0.2366 0.1054 0.0113 -0.0125 662 ARG A NE 4985 C CZ A ARG A 669 ? 0.3635 0.3163 0.1888 0.1029 0.0104 -0.0099 662 ARG A CZ 4986 C CZ B ARG A 669 ? 0.3983 0.3533 0.2270 0.1024 0.0178 -0.0068 662 ARG A CZ 4987 N NH1 A ARG A 669 ? 0.3753 0.3215 0.1878 0.1069 0.0102 -0.0078 662 ARG A NH1 4988 N NH1 B ARG A 669 ? 0.3955 0.3467 0.2171 0.1036 0.0161 -0.0048 662 ARG A NH1 4989 N NH2 A ARG A 669 ? 0.3623 0.3223 0.2007 0.0987 0.0186 -0.0061 662 ARG A NH2 4990 N NH2 B ARG A 669 ? 0.4197 0.3824 0.2627 0.0980 0.0255 -0.0034 662 ARG A NH2 4991 N N . MET A 670 ? 0.3972 0.3286 0.2041 0.1134 -0.0347 -0.0437 663 MET A N 4992 C CA . MET A 670 ? 0.3924 0.3291 0.2165 0.1072 -0.0388 -0.0467 663 MET A CA 4993 C C . MET A 670 ? 0.3965 0.3371 0.2331 0.1017 -0.0483 -0.0493 663 MET A C 4994 O O . MET A 670 ? 0.3756 0.3250 0.2303 0.0939 -0.0475 -0.0473 663 MET A O 4995 C CB A MET A 670 ? 0.3980 0.3265 0.2140 0.1120 -0.0431 -0.0529 663 MET A CB 4996 C CB B MET A 670 ? 0.4027 0.3318 0.2184 0.1122 -0.0405 -0.0518 663 MET A CB 4997 C CG A MET A 670 ? 0.3805 0.3126 0.2138 0.1058 -0.0492 -0.0566 663 MET A CG 4998 C CG B MET A 670 ? 0.3867 0.3137 0.1927 0.1173 -0.0286 -0.0481 663 MET A CG 4999 S SD A MET A 670 ? 0.3768 0.2987 0.2021 0.1111 -0.0544 -0.0641 663 MET A SD 5000 S SD B MET A 670 ? 0.4365 0.3569 0.2355 0.1231 -0.0261 -0.0523 663 MET A SD 5001 C CE A MET A 670 ? 0.4158 0.3302 0.2347 0.1135 -0.0689 -0.0719 663 MET A CE 5002 C CE B MET A 670 ? 0.2899 0.1949 0.0645 0.1324 -0.0363 -0.0607 663 MET A CE 5003 N N . MET A 671 ? 0.3958 0.3301 0.2230 0.1058 -0.0574 -0.0539 664 MET A N 5004 C CA . MET A 671 ? 0.3951 0.3338 0.2362 0.1007 -0.0665 -0.0567 664 MET A CA 5005 C C . MET A 671 ? 0.3751 0.3221 0.2260 0.0959 -0.0630 -0.0514 664 MET A C 5006 O O . MET A 671 ? 0.3646 0.3190 0.2331 0.0891 -0.0657 -0.0516 664 MET A O 5007 C CB A MET A 671 ? 0.4239 0.3539 0.2521 0.1072 -0.0774 -0.0628 664 MET A CB 5008 C CB B MET A 671 ? 0.4113 0.3419 0.2437 0.1058 -0.0789 -0.0641 664 MET A CB 5009 C CG A MET A 671 ? 0.4545 0.3737 0.2672 0.1141 -0.0814 -0.0686 664 MET A CG 5010 C CG B MET A 671 ? 0.4001 0.3241 0.2298 0.1079 -0.0841 -0.0705 664 MET A CG 5011 S SD A MET A 671 ? 0.4908 0.4128 0.3221 0.1077 -0.0856 -0.0731 664 MET A SD 5012 S SD B MET A 671 ? 0.4021 0.3179 0.2275 0.1120 -0.1006 -0.0805 664 MET A SD 5013 C CE A MET A 671 ? 0.4525 0.3751 0.2955 0.1051 -0.1005 -0.0797 664 MET A CE 5014 C CE B MET A 671 ? 0.3438 0.2700 0.1998 0.1010 -0.1058 -0.0818 664 MET A CE 5015 N N . ASN A 672 ? 0.3900 0.3350 0.2291 0.0999 -0.0571 -0.0468 665 ASN A N 5016 C CA . ASN A 672 ? 0.3780 0.3300 0.2259 0.0956 -0.0531 -0.0417 665 ASN A CA 5017 C C . ASN A 672 ? 0.3477 0.3092 0.2120 0.0879 -0.0454 -0.0376 665 ASN A C 5018 O O . ASN A 672 ? 0.3303 0.2990 0.2081 0.0820 -0.0452 -0.0358 665 ASN A O 5019 C CB . ASN A 672 ? 0.3925 0.3394 0.2244 0.1013 -0.0470 -0.0370 665 ASN A CB 5020 C CG . ASN A 672 ? 0.4154 0.3554 0.2351 0.1072 -0.0552 -0.0394 665 ASN A CG 5021 O OD1 . ASN A 672 ? 0.4037 0.3462 0.2328 0.1051 -0.0649 -0.0437 665 ASN A OD1 5022 N ND2 . ASN A 672 ? 0.4089 0.3402 0.2081 0.1147 -0.0515 -0.0367 665 ASN A ND2 5023 N N . ASP A 673 ? 0.3470 0.3078 0.2090 0.0885 -0.0391 -0.0362 666 ASP A N 5024 C CA . ASP A 673 ? 0.3287 0.2979 0.2061 0.0817 -0.0336 -0.0331 666 ASP A CA 5025 C C . ASP A 673 ? 0.3176 0.2911 0.2098 0.0757 -0.0398 -0.0363 666 ASP A C 5026 O O . ASP A 673 ? 0.3004 0.2814 0.2059 0.0693 -0.0375 -0.0337 666 ASP A O 5027 C CB . ASP A 673 ? 0.3272 0.2951 0.2007 0.0840 -0.0266 -0.0316 666 ASP A CB 5028 C CG . ASP A 673 ? 0.3724 0.3397 0.2380 0.0872 -0.0171 -0.0263 666 ASP A CG 5029 O OD1 . ASP A 673 ? 0.3837 0.3513 0.2469 0.0872 -0.0162 -0.0237 666 ASP A OD1 5030 O OD2 . ASP A 673 ? 0.3713 0.3379 0.2343 0.0896 -0.0105 -0.0248 666 ASP A OD2 5031 N N . GLN A 674 ? 0.3101 0.2784 0.2000 0.0777 -0.0474 -0.0419 667 GLN A N 5032 C CA . GLN A 674 ? 0.3088 0.2806 0.2138 0.0718 -0.0531 -0.0447 667 GLN A CA 5033 C C . GLN A 674 ? 0.2972 0.2745 0.2121 0.0677 -0.0560 -0.0443 667 GLN A C 5034 O O . GLN A 674 ? 0.3047 0.2884 0.2340 0.0612 -0.0552 -0.0430 667 GLN A O 5035 C CB . GLN A 674 ? 0.3055 0.2699 0.2068 0.0749 -0.0615 -0.0514 667 GLN A CB 5036 C CG . GLN A 674 ? 0.3334 0.2937 0.2295 0.0773 -0.0579 -0.0518 667 GLN A CG 5037 C CD . GLN A 674 ? 0.3575 0.3095 0.2493 0.0807 -0.0661 -0.0587 667 GLN A CD 5038 O OE1 . GLN A 674 ? 0.3909 0.3351 0.2674 0.0877 -0.0697 -0.0623 667 GLN A OE1 5039 N NE2 . GLN A 674 ? 0.3179 0.2708 0.2228 0.0757 -0.0693 -0.0606 667 GLN A NE2 5040 N N . LEU A 675 ? 0.3147 0.2891 0.2217 0.0720 -0.0598 -0.0455 668 LEU A N 5041 C CA . LEU A 675 ? 0.3012 0.2812 0.2179 0.0687 -0.0618 -0.0447 668 LEU A CA 5042 C C . LEU A 675 ? 0.2936 0.2805 0.2165 0.0643 -0.0534 -0.0388 668 LEU A C 5043 O O . LEU A 675 ? 0.2909 0.2844 0.2276 0.0586 -0.0531 -0.0381 668 LEU A O 5044 C CB . LEU A 675 ? 0.3238 0.2984 0.2288 0.0752 -0.0673 -0.0467 668 LEU A CB 5045 C CG . LEU A 675 ? 0.3593 0.3282 0.2620 0.0786 -0.0784 -0.0538 668 LEU A CG 5046 C CD1 . LEU A 675 ? 0.3775 0.3394 0.2641 0.0865 -0.0836 -0.0554 668 LEU A CD1 5047 C CD2 . LEU A 675 ? 0.3748 0.3500 0.2981 0.0723 -0.0843 -0.0571 668 LEU A CD2 5048 N N . MET A 676 ? 0.3076 0.2928 0.2207 0.0670 -0.0462 -0.0348 669 MET A N 5049 C CA . MET A 676 ? 0.2960 0.2872 0.2151 0.0630 -0.0387 -0.0296 669 MET A CA 5050 C C . MET A 676 ? 0.2870 0.2845 0.2190 0.0563 -0.0358 -0.0284 669 MET A C 5051 O O . MET A 676 ? 0.2612 0.2645 0.2028 0.0513 -0.0335 -0.0264 669 MET A O 5052 C CB . MET A 676 ? 0.2977 0.2856 0.2050 0.0671 -0.0315 -0.0256 669 MET A CB 5053 C CG . MET A 676 ? 0.3418 0.3355 0.2561 0.0629 -0.0237 -0.0204 669 MET A CG 5054 S SD . MET A 676 ? 0.3659 0.3556 0.2686 0.0676 -0.0146 -0.0156 669 MET A SD 5055 C CE . MET A 676 ? 0.3389 0.3294 0.2428 0.0676 -0.0115 -0.0161 669 MET A CE 5056 N N . PHE A 677 ? 0.2807 0.2761 0.2118 0.0566 -0.0360 -0.0297 670 PHE A N 5057 C CA . PHE A 677 ? 0.2714 0.2714 0.2125 0.0511 -0.0331 -0.0280 670 PHE A CA 5058 C C . PHE A 677 ? 0.2558 0.2579 0.2080 0.0464 -0.0378 -0.0304 670 PHE A C 5059 O O . PHE A 677 ? 0.2642 0.2694 0.2243 0.0418 -0.0359 -0.0289 670 PHE A O 5060 C CB . PHE A 677 ? 0.2557 0.2526 0.1917 0.0538 -0.0306 -0.0278 670 PHE A CB 5061 C CG . PHE A 677 ? 0.2965 0.2944 0.2273 0.0561 -0.0233 -0.0239 670 PHE A CG 5062 C CD1 . PHE A 677 ? 0.2682 0.2723 0.2061 0.0520 -0.0183 -0.0199 670 PHE A CD1 5063 C CD2 . PHE A 677 ? 0.3041 0.2963 0.2230 0.0626 -0.0212 -0.0243 670 PHE A CD2 5064 C CE1 . PHE A 677 ? 0.2515 0.2567 0.1868 0.0537 -0.0115 -0.0164 670 PHE A CE1 5065 C CE2 . PHE A 677 ? 0.3322 0.3255 0.2478 0.0646 -0.0136 -0.0205 670 PHE A CE2 5066 C CZ . PHE A 677 ? 0.2726 0.2726 0.1973 0.0601 -0.0087 -0.0165 670 PHE A CZ 5067 N N . LEU A 678 ? 0.2567 0.2572 0.2102 0.0475 -0.0439 -0.0340 671 LEU A N 5068 C CA . LEU A 678 ? 0.2572 0.2599 0.2232 0.0428 -0.0479 -0.0363 671 LEU A CA 5069 C C . LEU A 678 ? 0.2414 0.2511 0.2180 0.0369 -0.0439 -0.0333 671 LEU A C 5070 O O . LEU A 678 ? 0.2314 0.2434 0.2165 0.0320 -0.0424 -0.0323 671 LEU A O 5071 C CB . LEU A 678 ? 0.2551 0.2548 0.2221 0.0454 -0.0564 -0.0416 671 LEU A CB 5072 C CG . LEU A 678 ? 0.2736 0.2763 0.2564 0.0401 -0.0600 -0.0439 671 LEU A CG 5073 C CD1 . LEU A 678 ? 0.2872 0.2875 0.2740 0.0371 -0.0594 -0.0440 671 LEU A CD1 5074 C CD2 . LEU A 678 ? 0.2899 0.2901 0.2745 0.0433 -0.0694 -0.0496 671 LEU A CD2 5075 N N . GLU A 679 ? 0.2316 0.2440 0.2070 0.0377 -0.0421 -0.0319 672 GLU A N 5076 C CA . GLU A 679 ? 0.2238 0.2423 0.2073 0.0327 -0.0373 -0.0290 672 GLU A CA 5077 C C . GLU A 679 ? 0.2076 0.2272 0.1897 0.0302 -0.0317 -0.0254 672 GLU A C 5078 O O . GLU A 679 ? 0.1997 0.2226 0.1886 0.0253 -0.0290 -0.0238 672 GLU A O 5079 C CB . GLU A 679 ? 0.2129 0.2330 0.1936 0.0346 -0.0356 -0.0277 672 GLU A CB 5080 C CG . GLU A 679 ? 0.2025 0.2284 0.1932 0.0298 -0.0323 -0.0264 672 GLU A CG 5081 C CD . GLU A 679 ? 0.2727 0.3011 0.2745 0.0282 -0.0366 -0.0296 672 GLU A CD 5082 O OE1 . GLU A 679 ? 0.2261 0.2534 0.2273 0.0318 -0.0413 -0.0320 672 GLU A OE1 5083 O OE2 . GLU A 679 ? 0.2490 0.2800 0.2600 0.0234 -0.0351 -0.0296 672 GLU A OE2 5084 N N . ARG A 680 ? 0.2151 0.2320 0.1884 0.0336 -0.0298 -0.0241 673 ARG A N 5085 C CA . ARG A 680 ? 0.1965 0.2151 0.1696 0.0317 -0.0252 -0.0210 673 ARG A CA 5086 C C . ARG A 680 ? 0.2083 0.2261 0.1860 0.0287 -0.0264 -0.0212 673 ARG A C 5087 O O . ARG A 680 ? 0.1849 0.2050 0.1653 0.0256 -0.0235 -0.0187 673 ARG A O 5088 C CB . ARG A 680 ? 0.2261 0.2419 0.1904 0.0363 -0.0228 -0.0199 673 ARG A CB 5089 C CG . ARG A 680 ? 0.2232 0.2428 0.1892 0.0345 -0.0174 -0.0162 673 ARG A CG 5090 C CD . ARG A 680 ? 0.2605 0.2819 0.2257 0.0346 -0.0146 -0.0147 673 ARG A CD 5091 N NE . ARG A 680 ? 0.2388 0.2564 0.1953 0.0400 -0.0131 -0.0142 673 ARG A NE 5092 C CZ . ARG A 680 ? 0.2245 0.2389 0.1757 0.0432 -0.0152 -0.0154 673 ARG A CZ 5093 N NH1 . ARG A 680 ? 0.2198 0.2351 0.1750 0.0416 -0.0195 -0.0175 673 ARG A NH1 5094 N NH2 . ARG A 680 ? 0.2515 0.2616 0.1931 0.0483 -0.0131 -0.0143 673 ARG A NH2 5095 N N . ALA A 681 ? 0.2104 0.2245 0.1889 0.0299 -0.0311 -0.0244 674 ALA A N 5096 C CA . ALA A 681 ? 0.2257 0.2376 0.2083 0.0276 -0.0324 -0.0246 674 ALA A CA 5097 C C . ALA A 681 ? 0.2310 0.2459 0.2224 0.0219 -0.0309 -0.0230 674 ALA A C 5098 O O . ALA A 681 ? 0.2321 0.2454 0.2259 0.0193 -0.0302 -0.0215 674 ALA A O 5099 C CB . ALA A 681 ? 0.2297 0.2361 0.2117 0.0301 -0.0382 -0.0289 674 ALA A CB 5100 N N . PHE A 682 ? 0.2170 0.2358 0.2125 0.0200 -0.0299 -0.0231 675 PHE A N 5101 C CA . PHE A 682 ? 0.2202 0.2419 0.2235 0.0148 -0.0273 -0.0215 675 PHE A CA 5102 C C . PHE A 682 ? 0.2133 0.2375 0.2139 0.0126 -0.0223 -0.0178 675 PHE A C 5103 O O . PHE A 682 ? 0.2225 0.2479 0.2269 0.0088 -0.0196 -0.0162 675 PHE A O 5104 C CB . PHE A 682 ? 0.2252 0.2502 0.2358 0.0137 -0.0283 -0.0235 675 PHE A CB 5105 C CG . PHE A 682 ? 0.2175 0.2404 0.2337 0.0148 -0.0340 -0.0275 675 PHE A CG 5106 C CD1 . PHE A 682 ? 0.2134 0.2339 0.2367 0.0119 -0.0353 -0.0281 675 PHE A CD1 5107 C CD2 . PHE A 682 ? 0.2350 0.2578 0.2493 0.0188 -0.0384 -0.0306 675 PHE A CD2 5108 C CE1 . PHE A 682 ? 0.1929 0.2113 0.2230 0.0127 -0.0416 -0.0325 675 PHE A CE1 5109 C CE2 . PHE A 682 ? 0.2446 0.2652 0.2643 0.0201 -0.0451 -0.0351 675 PHE A CE2 5110 C CZ . PHE A 682 ? 0.2385 0.2571 0.2666 0.0169 -0.0468 -0.0362 675 PHE A CZ 5111 N N . ILE A 683 ? 0.2166 0.2410 0.2105 0.0151 -0.0211 -0.0166 676 ILE A N 5112 C CA . ILE A 683 ? 0.2097 0.2362 0.2012 0.0135 -0.0176 -0.0137 676 ILE A CA 5113 C C . ILE A 683 ? 0.2353 0.2591 0.2256 0.0123 -0.0177 -0.0117 676 ILE A C 5114 O O . ILE A 683 ? 0.2540 0.2746 0.2427 0.0147 -0.0200 -0.0122 676 ILE A O 5115 C CB . ILE A 683 ? 0.2012 0.2288 0.1880 0.0167 -0.0166 -0.0133 676 ILE A CB 5116 C CG1 . ILE A 683 ? 0.1873 0.2168 0.1745 0.0178 -0.0161 -0.0145 676 ILE A CG1 5117 C CG2 . ILE A 683 ? 0.1590 0.1886 0.1443 0.0156 -0.0143 -0.0108 676 ILE A CG2 5118 C CD1 . ILE A 683 ? 0.1824 0.2151 0.1734 0.0143 -0.0137 -0.0140 676 ILE A CD1 5119 N N . ASP A 684 ? 0.2252 0.2497 0.2155 0.0091 -0.0154 -0.0094 677 ASP A N 5120 C CA . ASP A 684 ? 0.2335 0.2552 0.2210 0.0084 -0.0156 -0.0070 677 ASP A CA 5121 C C . ASP A 684 ? 0.2319 0.2562 0.2158 0.0090 -0.0147 -0.0056 677 ASP A C 5122 O O . ASP A 684 ? 0.2254 0.2522 0.2086 0.0073 -0.0127 -0.0055 677 ASP A O 5123 C CB . ASP A 684 ? 0.2290 0.2487 0.2176 0.0047 -0.0136 -0.0051 677 ASP A CB 5124 C CG . ASP A 684 ? 0.2648 0.2801 0.2497 0.0043 -0.0142 -0.0022 677 ASP A CG 5125 O OD1 . ASP A 684 ? 0.2260 0.2413 0.2070 0.0064 -0.0157 -0.0012 677 ASP A OD1 5126 O OD2 . ASP A 684 ? 0.2566 0.2683 0.2430 0.0018 -0.0129 -0.0006 677 ASP A OD2 5127 N N . PRO A 685 ? 0.2521 0.2759 0.2346 0.0116 -0.0163 -0.0050 678 PRO A N 5128 C CA . PRO A 685 ? 0.2774 0.3044 0.2589 0.0121 -0.0159 -0.0041 678 PRO A CA 5129 C C . PRO A 685 ? 0.2859 0.3121 0.2641 0.0096 -0.0160 -0.0023 678 PRO A C 5130 O O . PRO A 685 ? 0.3238 0.3526 0.3014 0.0093 -0.0161 -0.0022 678 PRO A O 5131 C CB . PRO A 685 ? 0.2681 0.2946 0.2504 0.0154 -0.0176 -0.0038 678 PRO A CB 5132 C CG . PRO A 685 ? 0.2758 0.2974 0.2576 0.0162 -0.0193 -0.0039 678 PRO A CG 5133 C CD . PRO A 685 ? 0.2614 0.2818 0.2443 0.0141 -0.0186 -0.0053 678 PRO A CD 5134 N N . LEU A 686 ? 0.2805 0.3027 0.2563 0.0078 -0.0158 -0.0008 679 LEU A N 5135 C CA . LEU A 686 ? 0.2564 0.2766 0.2266 0.0059 -0.0154 0.0011 679 LEU A CA 5136 C C . LEU A 686 ? 0.2653 0.2868 0.2341 0.0033 -0.0119 0.0003 679 LEU A C 5137 O O . LEU A 686 ? 0.2524 0.2721 0.2150 0.0021 -0.0111 0.0015 679 LEU A O 5138 C CB . LEU A 686 ? 0.2625 0.2766 0.2297 0.0054 -0.0160 0.0038 679 LEU A CB 5139 C CG . LEU A 686 ? 0.2781 0.2902 0.2461 0.0084 -0.0197 0.0047 679 LEU A CG 5140 C CD1 . LEU A 686 ? 0.2452 0.2501 0.2096 0.0079 -0.0203 0.0078 679 LEU A CD1 5141 C CD2 . LEU A 686 ? 0.2941 0.3090 0.2608 0.0104 -0.0227 0.0049 679 LEU A CD2 5142 N N . GLY A 687 ? 0.2673 0.2913 0.2413 0.0029 -0.0101 -0.0016 680 GLY A N 5143 C CA . GLY A 687 ? 0.2648 0.2906 0.2395 0.0009 -0.0067 -0.0028 680 GLY A CA 5144 C C . GLY A 687 ? 0.2842 0.3069 0.2576 -0.0015 -0.0035 -0.0011 680 GLY A C 5145 O O . GLY A 687 ? 0.2923 0.3108 0.2641 -0.0019 -0.0041 0.0011 680 GLY A O 5146 N N . LEU A 688 ? 0.2673 0.2916 0.2417 -0.0031 0.0002 -0.0020 681 LEU A N 5147 C CA . LEU A 688 ? 0.2823 0.3038 0.2560 -0.0056 0.0046 -0.0002 681 LEU A CA 5148 C C . LEU A 688 ? 0.2941 0.3120 0.2564 -0.0059 0.0063 0.0017 681 LEU A C 5149 O O . LEU A 688 ? 0.2922 0.3109 0.2490 -0.0045 0.0038 0.0006 681 LEU A O 5150 C CB . LEU A 688 ? 0.2801 0.3056 0.2617 -0.0067 0.0082 -0.0024 681 LEU A CB 5151 C CG . LEU A 688 ? 0.2876 0.3159 0.2804 -0.0063 0.0059 -0.0045 681 LEU A CG 5152 C CD1 . LEU A 688 ? 0.2952 0.3283 0.2953 -0.0065 0.0082 -0.0071 681 LEU A CD1 5153 C CD2 . LEU A 688 ? 0.2834 0.3086 0.2814 -0.0081 0.0061 -0.0028 681 LEU A CD2 5154 N N . PRO A 689 ? 0.3211 0.3341 0.2792 -0.0076 0.0103 0.0048 682 PRO A N 5155 C CA . PRO A 689 ? 0.3310 0.3390 0.2755 -0.0072 0.0116 0.0070 682 PRO A CA 5156 C C . PRO A 689 ? 0.3357 0.3456 0.2748 -0.0066 0.0126 0.0043 682 PRO A C 5157 O O . PRO A 689 ? 0.3468 0.3595 0.2901 -0.0076 0.0172 0.0025 682 PRO A O 5158 C CB . PRO A 689 ? 0.3475 0.3505 0.2902 -0.0094 0.0180 0.0106 682 PRO A CB 5159 C CG . PRO A 689 ? 0.3540 0.3578 0.3086 -0.0106 0.0170 0.0112 682 PRO A CG 5160 C CD . PRO A 689 ? 0.3195 0.3310 0.2850 -0.0097 0.0137 0.0065 682 PRO A CD 5161 N N . ASP A 690 ? 0.3479 0.3565 0.2788 -0.0048 0.0079 0.0037 683 ASP A N 5162 C CA . ASP A 690 ? 0.3561 0.3654 0.2809 -0.0040 0.0073 0.0007 683 ASP A CA 5163 C C . ASP A 690 ? 0.3196 0.3353 0.2545 -0.0042 0.0075 -0.0030 683 ASP A C 5164 O O . ASP A 690 ? 0.3075 0.3236 0.2391 -0.0039 0.0080 -0.0058 683 ASP A O 5165 C CB . ASP A 690 ? 0.3931 0.3975 0.3069 -0.0045 0.0130 0.0015 683 ASP A CB 5166 C CG . ASP A 690 ? 0.4859 0.4825 0.3868 -0.0038 0.0130 0.0057 683 ASP A CG 5167 O OD1 . ASP A 690 ? 0.5036 0.4979 0.3990 -0.0021 0.0064 0.0064 683 ASP A OD1 5168 O OD2 . ASP A 690 ? 0.5592 0.5519 0.4564 -0.0050 0.0198 0.0085 683 ASP A OD2 5169 N N . ARG A 691 ? 0.3010 0.3207 0.2473 -0.0044 0.0069 -0.0032 684 ARG A N 5170 C CA . ARG A 691 ? 0.2760 0.3011 0.2312 -0.0040 0.0065 -0.0063 684 ARG A CA 5171 C C . ARG A 691 ? 0.2615 0.2890 0.2227 -0.0027 0.0017 -0.0063 684 ARG A C 5172 O O . ARG A 691 ? 0.2415 0.2712 0.2104 -0.0024 0.0017 -0.0064 684 ARG A O 5173 C CB . ARG A 691 ? 0.2883 0.3158 0.2510 -0.0051 0.0113 -0.0072 684 ARG A CB 5174 C CG . ARG A 691 ? 0.2801 0.3058 0.2376 -0.0059 0.0170 -0.0078 684 ARG A CG 5175 C CD . ARG A 691 ? 0.3308 0.3602 0.2982 -0.0067 0.0219 -0.0091 684 ARG A CD 5176 N NE . ARG A 691 ? 0.3133 0.3439 0.2898 -0.0079 0.0226 -0.0074 684 ARG A NE 5177 C CZ . ARG A 691 ? 0.3205 0.3552 0.3091 -0.0084 0.0247 -0.0088 684 ARG A CZ 5178 N NH1 . ARG A 691 ? 0.2333 0.2714 0.2264 -0.0076 0.0268 -0.0116 684 ARG A NH1 5179 N NH2 . ARG A 691 ? 0.2742 0.3095 0.2712 -0.0097 0.0245 -0.0075 684 ARG A NH2 5180 N N . PRO A 692 ? 0.2516 0.2789 0.2097 -0.0016 -0.0021 -0.0064 685 PRO A N 5181 C CA . PRO A 692 ? 0.2511 0.2804 0.2144 -0.0001 -0.0057 -0.0059 685 PRO A CA 5182 C C . PRO A 692 ? 0.2326 0.2658 0.2037 0.0008 -0.0053 -0.0076 685 PRO A C 5183 O O . PRO A 692 ? 0.2293 0.2633 0.2041 0.0023 -0.0069 -0.0070 685 PRO A O 5184 C CB . PRO A 692 ? 0.2739 0.3029 0.2336 0.0006 -0.0097 -0.0061 685 PRO A CB 5185 C CG . PRO A 692 ? 0.2824 0.3101 0.2363 -0.0004 -0.0087 -0.0079 685 PRO A CG 5186 C CD . PRO A 692 ? 0.2749 0.2999 0.2246 -0.0016 -0.0038 -0.0071 685 PRO A CD 5187 N N . PHE A 693 ? 0.2212 0.2559 0.1940 0.0003 -0.0031 -0.0095 686 PHE A N 5188 C CA . PHE A 693 ? 0.2231 0.2604 0.2020 0.0015 -0.0026 -0.0107 686 PHE A CA 5189 C C . PHE A 693 ? 0.2091 0.2471 0.1921 0.0018 -0.0010 -0.0112 686 PHE A C 5190 O O . PHE A 693 ? 0.2105 0.2498 0.1973 0.0035 -0.0013 -0.0120 686 PHE A O 5191 C CB . PHE A 693 ? 0.2090 0.2473 0.1885 0.0013 -0.0018 -0.0126 686 PHE A CB 5192 C CG . PHE A 693 ? 0.2100 0.2483 0.1882 0.0011 -0.0044 -0.0126 686 PHE A CG 5193 C CD1 . PHE A 693 ? 0.2141 0.2539 0.1959 0.0025 -0.0065 -0.0113 686 PHE A CD1 5194 C CD2 . PHE A 693 ? 0.2260 0.2627 0.1996 -0.0001 -0.0051 -0.0140 686 PHE A CD2 5195 C CE1 . PHE A 693 ? 0.2098 0.2504 0.1926 0.0022 -0.0092 -0.0115 686 PHE A CE1 5196 C CE2 . PHE A 693 ? 0.2226 0.2594 0.1960 -0.0002 -0.0086 -0.0145 686 PHE A CE2 5197 C CZ . PHE A 693 ? 0.2202 0.2594 0.1992 0.0007 -0.0107 -0.0132 686 PHE A CZ 5198 N N . TYR A 694 ? 0.2000 0.2367 0.1821 0.0003 0.0004 -0.0105 687 TYR A N 5199 C CA . TYR A 694 ? 0.2052 0.2427 0.1933 0.0003 0.0010 -0.0110 687 TYR A CA 5200 C C . TYR A 694 ? 0.2018 0.2373 0.1899 0.0006 -0.0012 -0.0094 687 TYR A C 5201 O O . TYR A 694 ? 0.2225 0.2554 0.2082 -0.0009 -0.0002 -0.0077 687 TYR A O 5202 C CB . TYR A 694 ? 0.2067 0.2444 0.1964 -0.0017 0.0052 -0.0112 687 TYR A CB 5203 C CG . TYR A 694 ? 0.2050 0.2445 0.1954 -0.0015 0.0077 -0.0132 687 TYR A CG 5204 C CD1 . TYR A 694 ? 0.1737 0.2148 0.1664 0.0004 0.0060 -0.0148 687 TYR A CD1 5205 C CD2 . TYR A 694 ? 0.2419 0.2808 0.2304 -0.0030 0.0123 -0.0135 687 TYR A CD2 5206 C CE1 . TYR A 694 ? 0.1901 0.2321 0.1837 0.0007 0.0081 -0.0166 687 TYR A CE1 5207 C CE2 . TYR A 694 ? 0.2554 0.2956 0.2446 -0.0025 0.0147 -0.0158 687 TYR A CE2 5208 C CZ . TYR A 694 ? 0.2324 0.2741 0.2247 -0.0006 0.0123 -0.0174 687 TYR A CZ 5209 O OH . TYR A 694 ? 0.2487 0.2910 0.2423 0.0000 0.0144 -0.0196 687 TYR A OH 5210 N N . ARG A 695 ? 0.2062 0.2420 0.1965 0.0029 -0.0041 -0.0101 688 ARG A N 5211 C CA . ARG A 695 ? 0.1955 0.2289 0.1851 0.0039 -0.0067 -0.0091 688 ARG A CA 5212 C C . ARG A 695 ? 0.2132 0.2460 0.2083 0.0045 -0.0085 -0.0107 688 ARG A C 5213 O O . ARG A 695 ? 0.2082 0.2383 0.2033 0.0052 -0.0108 -0.0104 688 ARG A O 5214 C CB . ARG A 695 ? 0.1944 0.2282 0.1816 0.0067 -0.0086 -0.0091 688 ARG A CB 5215 C CG . ARG A 695 ? 0.1974 0.2324 0.1816 0.0059 -0.0077 -0.0082 688 ARG A CG 5216 C CD . ARG A 695 ? 0.2481 0.2835 0.2316 0.0080 -0.0094 -0.0073 688 ARG A CD 5217 N NE . ARG A 695 ? 0.2547 0.2909 0.2399 0.0107 -0.0092 -0.0082 688 ARG A NE 5218 C CZ . ARG A 695 ? 0.3139 0.3502 0.2993 0.0134 -0.0098 -0.0076 688 ARG A CZ 5219 N NH1 . ARG A 695 ? 0.2513 0.2874 0.2364 0.0162 -0.0088 -0.0082 688 ARG A NH1 5220 N NH2 . ARG A 695 ? 0.2537 0.2899 0.2392 0.0136 -0.0111 -0.0064 688 ARG A NH2 5221 N N . HIS A 696 ? 0.2006 0.2357 0.2005 0.0045 -0.0080 -0.0126 689 HIS A N 5222 C CA . HIS A 696 ? 0.1996 0.2344 0.2058 0.0052 -0.0108 -0.0147 689 HIS A CA 5223 C C . HIS A 696 ? 0.2046 0.2385 0.2163 0.0017 -0.0091 -0.0139 689 HIS A C 5224 O O . HIS A 696 ? 0.1902 0.2256 0.2033 -0.0007 -0.0049 -0.0128 689 HIS A O 5225 C CB . HIS A 696 ? 0.2095 0.2473 0.2201 0.0067 -0.0115 -0.0170 689 HIS A CB 5226 C CG . HIS A 696 ? 0.2007 0.2377 0.2149 0.0092 -0.0164 -0.0198 689 HIS A CG 5227 N ND1 . HIS A 696 ? 0.1897 0.2265 0.2123 0.0077 -0.0185 -0.0214 689 HIS A ND1 5228 C CD2 . HIS A 696 ? 0.2171 0.2531 0.2277 0.0134 -0.0197 -0.0213 689 HIS A CD2 5229 C CE1 . HIS A 696 ? 0.2192 0.2550 0.2430 0.0109 -0.0238 -0.0244 689 HIS A CE1 5230 N NE2 . HIS A 696 ? 0.2139 0.2488 0.2293 0.0147 -0.0245 -0.0242 689 HIS A NE2 5231 N N . VAL A 697 ? 0.2006 0.2316 0.2154 0.0016 -0.0119 -0.0144 690 VAL A N 5232 C CA . VAL A 697 ? 0.2010 0.2301 0.2211 -0.0020 -0.0097 -0.0128 690 VAL A CA 5233 C C . VAL A 697 ? 0.2173 0.2495 0.2499 -0.0037 -0.0097 -0.0152 690 VAL A C 5234 O O . VAL A 697 ? 0.2103 0.2425 0.2496 -0.0072 -0.0060 -0.0138 690 VAL A O 5235 C CB . VAL A 697 ? 0.2071 0.2308 0.2253 -0.0014 -0.0129 -0.0122 690 VAL A CB 5236 C CG1 . VAL A 697 ? 0.2107 0.2313 0.2358 -0.0052 -0.0110 -0.0106 690 VAL A CG1 5237 C CG2 . VAL A 697 ? 0.2109 0.2323 0.2185 0.0000 -0.0126 -0.0095 690 VAL A CG2 5238 N N . ILE A 698 ? 0.2002 0.2349 0.2361 -0.0010 -0.0137 -0.0186 691 ILE A N 5239 C CA . ILE A 698 ? 0.1891 0.2271 0.2383 -0.0023 -0.0147 -0.0213 691 ILE A CA 5240 C C . ILE A 698 ? 0.1960 0.2391 0.2489 -0.0030 -0.0103 -0.0212 691 ILE A C 5241 O O . ILE A 698 ? 0.2103 0.2564 0.2749 -0.0057 -0.0077 -0.0217 691 ILE A O 5242 C CB . ILE A 698 ? 0.1946 0.2325 0.2465 0.0013 -0.0223 -0.0255 691 ILE A CB 5243 C CG1 . ILE A 698 ? 0.1807 0.2127 0.2270 0.0030 -0.0268 -0.0262 691 ILE A CG1 5244 C CG2 . ILE A 698 ? 0.2055 0.2470 0.2739 -0.0001 -0.0249 -0.0288 691 ILE A CG2 5245 C CD1 . ILE A 698 ? 0.2076 0.2363 0.2602 -0.0008 -0.0258 -0.0250 691 ILE A CD1 5246 N N . TYR A 699 ? 0.2058 0.2497 0.2497 -0.0007 -0.0093 -0.0206 692 TYR A N 5247 C CA . TYR A 699 ? 0.2048 0.2528 0.2514 -0.0006 -0.0059 -0.0212 692 TYR A CA 5248 C C . TYR A 699 ? 0.2179 0.2648 0.2541 -0.0012 -0.0012 -0.0186 692 TYR A C 5249 O O . TYR A 699 ? 0.2611 0.3053 0.2875 0.0003 -0.0029 -0.0175 692 TYR A O 5250 C CB . TYR A 699 ? 0.1990 0.2483 0.2450 0.0036 -0.0107 -0.0238 692 TYR A CB 5251 C CG . TYR A 699 ? 0.2161 0.2667 0.2723 0.0050 -0.0165 -0.0271 692 TYR A CG 5252 C CD1 . TYR A 699 ? 0.2310 0.2863 0.3022 0.0029 -0.0153 -0.0288 692 TYR A CD1 5253 C CD2 . TYR A 699 ? 0.2133 0.2607 0.2645 0.0087 -0.0233 -0.0289 692 TYR A CD2 5254 C CE1 . TYR A 699 ? 0.2159 0.2728 0.2979 0.0042 -0.0217 -0.0324 692 TYR A CE1 5255 C CE2 . TYR A 699 ? 0.2171 0.2651 0.2769 0.0103 -0.0297 -0.0326 692 TYR A CE2 5256 C CZ . TYR A 699 ? 0.2524 0.3053 0.3280 0.0079 -0.0293 -0.0344 692 TYR A CZ 5257 O OH . TYR A 699 ? 0.2526 0.3066 0.3379 0.0097 -0.0368 -0.0386 692 TYR A OH 5258 N N . ALA A 700 ? 0.2065 0.2555 0.2449 -0.0030 0.0044 -0.0181 693 ALA A N 5259 C CA . ALA A 700 ? 0.2048 0.2528 0.2332 -0.0027 0.0076 -0.0170 693 ALA A CA 5260 C C . ALA A 700 ? 0.2088 0.2603 0.2431 -0.0031 0.0120 -0.0184 693 ALA A C 5261 O O . ALA A 700 ? 0.2045 0.2591 0.2504 -0.0042 0.0137 -0.0195 693 ALA A O 5262 C CB . ALA A 700 ? 0.2182 0.2624 0.2378 -0.0050 0.0106 -0.0139 693 ALA A CB 5263 N N . PRO A 701 ? 0.2071 0.2581 0.2346 -0.0020 0.0139 -0.0188 694 PRO A N 5264 C CA . PRO A 701 ? 0.2268 0.2803 0.2585 -0.0021 0.0187 -0.0203 694 PRO A CA 5265 C C . PRO A 701 ? 0.2300 0.2827 0.2614 -0.0051 0.0251 -0.0185 694 PRO A C 5266 O O . PRO A 701 ? 0.2399 0.2884 0.2616 -0.0065 0.0257 -0.0160 694 PRO A O 5267 C CB . PRO A 701 ? 0.2191 0.2700 0.2402 -0.0009 0.0191 -0.0205 694 PRO A CB 5268 C CG . PRO A 701 ? 0.2043 0.2536 0.2210 0.0006 0.0134 -0.0199 694 PRO A CG 5269 C CD . PRO A 701 ? 0.2001 0.2482 0.2168 -0.0008 0.0117 -0.0180 694 PRO A CD 5270 N N . SER A 702 ? 0.2257 0.2820 0.2675 -0.0058 0.0299 -0.0196 695 SER A N 5271 C CA . SER A 702 ? 0.2342 0.2896 0.2762 -0.0085 0.0373 -0.0176 695 SER A CA 5272 C C . SER A 702 ? 0.2509 0.3013 0.2766 -0.0084 0.0412 -0.0164 695 SER A C 5273 O O . SER A 702 ? 0.2422 0.2923 0.2628 -0.0065 0.0409 -0.0186 695 SER A O 5274 C CB . SER A 702 ? 0.2381 0.2988 0.2942 -0.0087 0.0428 -0.0195 695 SER A CB 5275 O OG . SER A 702 ? 0.2465 0.3054 0.3001 -0.0109 0.0517 -0.0172 695 SER A OG 5276 N N . SER A 703 ? 0.2547 0.3005 0.2721 -0.0105 0.0449 -0.0131 696 SER A N 5277 C CA . SER A 703 ? 0.2659 0.3062 0.2665 -0.0100 0.0482 -0.0122 696 SER A CA 5278 C C . SER A 703 ? 0.2804 0.3215 0.2804 -0.0093 0.0558 -0.0140 696 SER A C 5279 O O . SER A 703 ? 0.2857 0.3222 0.2713 -0.0081 0.0576 -0.0147 696 SER A O 5280 C CB . SER A 703 ? 0.2704 0.3048 0.2613 -0.0118 0.0500 -0.0078 696 SER A CB 5281 O OG A SER A 703 ? 0.1928 0.2259 0.1822 -0.0117 0.0426 -0.0067 696 SER A OG 5282 O OG B SER A 703 ? 0.3382 0.3734 0.3378 -0.0141 0.0566 -0.0055 696 SER A OG 5283 N N . HIS A 704 ? 0.2598 0.3063 0.2753 -0.0098 0.0601 -0.0151 697 HIS A N 5284 C CA . HIS A 704 ? 0.2705 0.3187 0.2881 -0.0087 0.0679 -0.0171 697 HIS A CA 5285 C C . HIS A 704 ? 0.2798 0.3329 0.3067 -0.0062 0.0650 -0.0214 697 HIS A C 5286 O O . HIS A 704 ? 0.2924 0.3465 0.3206 -0.0047 0.0709 -0.0237 697 HIS A O 5287 C CB . HIS A 704 ? 0.2829 0.3343 0.3135 -0.0110 0.0760 -0.0152 697 HIS A CB 5288 C CG . HIS A 704 ? 0.3187 0.3646 0.3415 -0.0136 0.0790 -0.0103 697 HIS A CG 5289 N ND1 . HIS A 704 ? 0.3090 0.3480 0.3153 -0.0135 0.0863 -0.0078 697 HIS A ND1 5290 C CD2 . HIS A 704 ? 0.3436 0.3888 0.3713 -0.0159 0.0754 -0.0075 697 HIS A CD2 5291 C CE1 . HIS A 704 ? 0.3688 0.4031 0.3703 -0.0158 0.0871 -0.0031 697 HIS A CE1 5292 N NE2 . HIS A 704 ? 0.3477 0.3858 0.3627 -0.0174 0.0807 -0.0030 697 HIS A NE2 5293 N N . ASN A 705 ? 0.2460 0.3015 0.2787 -0.0053 0.0564 -0.0225 698 ASN A N 5294 C CA . ASN A 705 ? 0.2425 0.3018 0.2837 -0.0026 0.0532 -0.0261 698 ASN A CA 5295 C C . ASN A 705 ? 0.2295 0.2884 0.2696 -0.0015 0.0438 -0.0261 698 ASN A C 5296 O O . ASN A 705 ? 0.2179 0.2798 0.2673 -0.0017 0.0394 -0.0257 698 ASN A O 5297 C CB . ASN A 705 ? 0.2497 0.3162 0.3109 -0.0024 0.0560 -0.0275 698 ASN A CB 5298 C CG . ASN A 705 ? 0.2387 0.3090 0.3093 0.0008 0.0513 -0.0308 698 ASN A CG 5299 O OD1 . ASN A 705 ? 0.2275 0.2945 0.2892 0.0029 0.0481 -0.0320 698 ASN A OD1 5300 N ND2 . ASN A 705 ? 0.2206 0.2974 0.3098 0.0013 0.0506 -0.0321 698 ASN A ND2 5301 N N . LYS A 706 ? 0.2324 0.2874 0.2610 -0.0002 0.0408 -0.0268 699 LYS A N 5302 C CA . LYS A 706 ? 0.2182 0.2721 0.2444 0.0007 0.0331 -0.0264 699 LYS A CA 5303 C C . LYS A 706 ? 0.2228 0.2806 0.2610 0.0030 0.0287 -0.0277 699 LYS A C 5304 O O . LYS A 706 ? 0.2239 0.2813 0.2618 0.0037 0.0228 -0.0267 699 LYS A O 5305 C CB . LYS A 706 ? 0.2450 0.2948 0.2607 0.0019 0.0320 -0.0276 699 LYS A CB 5306 C CG . LYS A 706 ? 0.2633 0.3113 0.2750 0.0025 0.0256 -0.0265 699 LYS A CG 5307 C CD . LYS A 706 ? 0.2611 0.3052 0.2642 0.0029 0.0251 -0.0278 699 LYS A CD 5308 C CE . LYS A 706 ? 0.2658 0.3083 0.2650 0.0029 0.0198 -0.0261 699 LYS A CE 5309 N NZ . LYS A 706 ? 0.2431 0.2824 0.2381 0.0033 0.0186 -0.0275 699 LYS A NZ 5310 N N . TYR A 707 ? 0.2246 0.2860 0.2730 0.0044 0.0314 -0.0299 700 TYR A N 5311 C CA . TYR A 707 ? 0.2276 0.2923 0.2869 0.0072 0.0264 -0.0313 700 TYR A CA 5312 C C . TYR A 707 ? 0.2252 0.2936 0.2948 0.0062 0.0232 -0.0308 700 TYR A C 5313 O O . TYR A 707 ? 0.2198 0.2894 0.2946 0.0086 0.0169 -0.0317 700 TYR A O 5314 C CB . TYR A 707 ? 0.2174 0.2855 0.2868 0.0093 0.0297 -0.0341 700 TYR A CB 5315 C CG . TYR A 707 ? 0.2303 0.2947 0.2923 0.0113 0.0314 -0.0355 700 TYR A CG 5316 C CD1 . TYR A 707 ? 0.2582 0.3179 0.3109 0.0126 0.0267 -0.0347 700 TYR A CD1 5317 C CD2 . TYR A 707 ? 0.2593 0.3247 0.3247 0.0121 0.0378 -0.0378 700 TYR A CD2 5318 C CE1 . TYR A 707 ? 0.2364 0.2919 0.2833 0.0140 0.0281 -0.0362 700 TYR A CE1 5319 C CE2 . TYR A 707 ? 0.2657 0.3269 0.3246 0.0140 0.0391 -0.0397 700 TYR A CE2 5320 C CZ . TYR A 707 ? 0.2720 0.3281 0.3220 0.0148 0.0339 -0.0388 700 TYR A CZ 5321 O OH . TYR A 707 ? 0.2318 0.2835 0.2769 0.0163 0.0352 -0.0408 700 TYR A OH 5322 N N . ALA A 708 ? 0.2284 0.2982 0.3015 0.0030 0.0277 -0.0297 701 ALA A N 5323 C CA . ALA A 708 ? 0.2339 0.3072 0.3193 0.0016 0.0252 -0.0296 701 ALA A CA 5324 C C . ALA A 708 ? 0.2481 0.3174 0.3250 0.0001 0.0208 -0.0274 701 ALA A C 5325 O O . ALA A 708 ? 0.2609 0.3258 0.3249 -0.0013 0.0231 -0.0251 701 ALA A O 5326 C CB . ALA A 708 ? 0.2350 0.3119 0.3308 -0.0013 0.0333 -0.0292 701 ALA A CB 5327 N N . GLY A 709 ? 0.2429 0.3134 0.3266 0.0010 0.0140 -0.0284 702 GLY A N 5328 C CA . GLY A 709 ? 0.2621 0.3288 0.3393 -0.0002 0.0106 -0.0266 702 GLY A CA 5329 C C . GLY A 709 ? 0.2562 0.3238 0.3414 -0.0043 0.0145 -0.0253 702 GLY A C 5330 O O . GLY A 709 ? 0.2673 0.3397 0.3679 -0.0055 0.0170 -0.0267 702 GLY A O 5331 N N . GLU A 710 ? 0.2346 0.2975 0.3104 -0.0064 0.0155 -0.0225 703 GLU A N 5332 C CA . GLU A 710 ? 0.2401 0.3024 0.3228 -0.0102 0.0189 -0.0206 703 GLU A CA 5333 C C . GLU A 710 ? 0.2367 0.2956 0.3181 -0.0100 0.0118 -0.0207 703 GLU A C 5334 O O . GLU A 710 ? 0.2198 0.2750 0.2885 -0.0079 0.0079 -0.0201 703 GLU A O 5335 C CB . GLU A 710 ? 0.2544 0.3126 0.3257 -0.0124 0.0264 -0.0169 703 GLU A CB 5336 C CG . GLU A 710 ? 0.2606 0.3172 0.3385 -0.0165 0.0317 -0.0140 703 GLU A CG 5337 C CD . GLU A 710 ? 0.2849 0.3478 0.3829 -0.0181 0.0353 -0.0158 703 GLU A CD 5338 O OE1 . GLU A 710 ? 0.2704 0.3360 0.3703 -0.0182 0.0426 -0.0157 703 GLU A OE1 5339 O OE2 . GLU A 710 ? 0.2782 0.3435 0.3907 -0.0192 0.0306 -0.0175 703 GLU A OE2 5340 N N . SER A 711 ? 0.2150 0.2752 0.3101 -0.0123 0.0105 -0.0214 704 SER A N 5341 C CA . SER A 711 ? 0.2054 0.2614 0.2992 -0.0123 0.0043 -0.0217 704 SER A CA 5342 C C . SER A 711 ? 0.2046 0.2551 0.2927 -0.0156 0.0085 -0.0175 704 SER A C 5343 O O . SER A 711 ? 0.2173 0.2679 0.3083 -0.0187 0.0163 -0.0148 704 SER A O 5344 C CB . SER A 711 ? 0.2068 0.2662 0.3181 -0.0124 -0.0016 -0.0257 704 SER A CB 5345 O OG . SER A 711 ? 0.2279 0.2916 0.3565 -0.0162 0.0039 -0.0254 704 SER A OG 5346 N N . PHE A 712 ? 0.1873 0.2325 0.2673 -0.0146 0.0035 -0.0170 705 PHE A N 5347 C CA . PHE A 712 ? 0.1856 0.2243 0.2566 -0.0167 0.0067 -0.0127 705 PHE A CA 5348 C C . PHE A 712 ? 0.2074 0.2452 0.2687 -0.0178 0.0147 -0.0089 705 PHE A C 5349 O O . PHE A 712 ? 0.2062 0.2415 0.2692 -0.0211 0.0212 -0.0055 705 PHE A O 5350 C CB . PHE A 712 ? 0.1874 0.2236 0.2705 -0.0203 0.0073 -0.0119 705 PHE A CB 5351 C CG . PHE A 712 ? 0.1954 0.2300 0.2841 -0.0188 -0.0016 -0.0157 705 PHE A CG 5352 C CD1 . PHE A 712 ? 0.1931 0.2230 0.2687 -0.0155 -0.0069 -0.0159 705 PHE A CD1 5353 C CD2 . PHE A 712 ? 0.2006 0.2382 0.3070 -0.0202 -0.0049 -0.0193 705 PHE A CD2 5354 C CE1 . PHE A 712 ? 0.2075 0.2349 0.2859 -0.0135 -0.0147 -0.0196 705 PHE A CE1 5355 C CE2 . PHE A 712 ? 0.2085 0.2434 0.3182 -0.0184 -0.0139 -0.0233 705 PHE A CE2 5356 C CZ . PHE A 712 ? 0.2189 0.2484 0.3134 -0.0149 -0.0185 -0.0234 705 PHE A CZ 5357 N N . PRO A 713 ? 0.2038 0.2431 0.2549 -0.0151 0.0143 -0.0096 706 PRO A N 5358 C CA . PRO A 713 ? 0.2025 0.2413 0.2445 -0.0156 0.0210 -0.0073 706 PRO A CA 5359 C C . PRO A 713 ? 0.2066 0.2386 0.2371 -0.0171 0.0242 -0.0028 706 PRO A C 5360 O O . PRO A 713 ? 0.2081 0.2385 0.2344 -0.0186 0.0313 -0.0003 706 PRO A O 5361 C CB . PRO A 713 ? 0.1711 0.2114 0.2040 -0.0122 0.0176 -0.0092 706 PRO A CB 5362 C CG . PRO A 713 ? 0.1882 0.2275 0.2207 -0.0099 0.0097 -0.0108 706 PRO A CG 5363 C CD . PRO A 713 ? 0.2063 0.2471 0.2532 -0.0112 0.0077 -0.0125 706 PRO A CD 5364 N N . GLY A 714 ? 0.1990 0.2267 0.2238 -0.0162 0.0191 -0.0017 707 GLY A N 5365 C CA . GLY A 714 ? 0.2161 0.2368 0.2296 -0.0170 0.0214 0.0028 707 GLY A CA 5366 C C . GLY A 714 ? 0.2400 0.2577 0.2600 -0.0206 0.0277 0.0060 707 GLY A C 5367 O O . GLY A 714 ? 0.2243 0.2375 0.2351 -0.0217 0.0337 0.0099 707 GLY A O 5368 N N . ILE A 715 ? 0.2158 0.2353 0.2516 -0.0226 0.0265 0.0044 708 ILE A N 5369 C CA . ILE A 715 ? 0.2284 0.2452 0.2727 -0.0266 0.0331 0.0077 708 ILE A CA 5370 C C . ILE A 715 ? 0.2308 0.2523 0.2805 -0.0281 0.0414 0.0078 708 ILE A C 5371 O O . ILE A 715 ? 0.2400 0.2577 0.2872 -0.0304 0.0500 0.0121 708 ILE A O 5372 C CB . ILE A 715 ? 0.2142 0.2325 0.2769 -0.0285 0.0289 0.0051 708 ILE A CB 5373 C CG1 . ILE A 715 ? 0.2337 0.2477 0.2915 -0.0262 0.0201 0.0038 708 ILE A CG1 5374 C CG2 . ILE A 715 ? 0.2118 0.2261 0.2844 -0.0332 0.0362 0.0091 708 ILE A CG2 5375 C CD1 . ILE A 715 ? 0.2615 0.2763 0.3358 -0.0273 0.0143 0.0000 708 ILE A CD1 5376 N N . TYR A 716 ? 0.2237 0.2527 0.2801 -0.0265 0.0394 0.0032 709 TYR A N 5377 C CA . TYR A 716 ? 0.2305 0.2644 0.2935 -0.0275 0.0472 0.0028 709 TYR A CA 5378 C C . TYR A 716 ? 0.2390 0.2684 0.2843 -0.0268 0.0546 0.0062 709 TYR A C 5379 O O . TYR A 716 ? 0.2438 0.2719 0.2907 -0.0290 0.0641 0.0092 709 TYR A O 5380 C CB . TYR A 716 ? 0.2073 0.2493 0.2785 -0.0250 0.0429 -0.0026 709 TYR A CB 5381 C CG . TYR A 716 ? 0.1813 0.2284 0.2599 -0.0257 0.0512 -0.0033 709 TYR A CG 5382 C CD1 . TYR A 716 ? 0.2216 0.2749 0.3221 -0.0278 0.0535 -0.0051 709 TYR A CD1 5383 C CD2 . TYR A 716 ? 0.2340 0.2793 0.2982 -0.0242 0.0569 -0.0021 709 TYR A CD2 5384 C CE1 . TYR A 716 ? 0.2278 0.2861 0.3366 -0.0282 0.0622 -0.0056 709 TYR A CE1 5385 C CE2 . TYR A 716 ? 0.2329 0.2823 0.3035 -0.0245 0.0654 -0.0028 709 TYR A CE2 5386 C CZ . TYR A 716 ? 0.2670 0.3231 0.3601 -0.0264 0.0682 -0.0045 709 TYR A CZ 5387 O OH . TYR A 716 ? 0.2461 0.3067 0.3469 -0.0264 0.0771 -0.0052 709 TYR A OH 5388 N N . ASP A 717 ? 0.2495 0.2763 0.2779 -0.0238 0.0502 0.0058 710 ASP A N 5389 C CA . ASP A 717 ? 0.2524 0.2741 0.2624 -0.0227 0.0553 0.0084 710 ASP A CA 5390 C C . ASP A 717 ? 0.2708 0.2838 0.2710 -0.0243 0.0597 0.0142 710 ASP A C 5391 O O . ASP A 717 ? 0.2915 0.3004 0.2819 -0.0245 0.0677 0.0171 710 ASP A O 5392 C CB . ASP A 717 ? 0.2554 0.2767 0.2520 -0.0193 0.0484 0.0061 710 ASP A CB 5393 C CG . ASP A 717 ? 0.2694 0.2978 0.2723 -0.0176 0.0469 0.0012 710 ASP A CG 5394 O OD1 . ASP A 717 ? 0.2638 0.2968 0.2782 -0.0186 0.0522 -0.0001 710 ASP A OD1 5395 O OD2 . ASP A 717 ? 0.2953 0.3245 0.2924 -0.0153 0.0407 -0.0009 710 ASP A OD2 5396 N N . ALA A 718 ? 0.2659 0.2753 0.2689 -0.0252 0.0550 0.0161 711 ALA A N 5397 C CA . ALA A 718 ? 0.2761 0.2766 0.2713 -0.0268 0.0594 0.0221 711 ALA A CA 5398 C C . ALA A 718 ? 0.2865 0.2865 0.2921 -0.0304 0.0702 0.0251 711 ALA A C 5399 O O . ALA A 718 ? 0.2888 0.2812 0.2831 -0.0311 0.0778 0.0305 711 ALA A O 5400 C CB . ALA A 718 ? 0.2829 0.2793 0.2805 -0.0270 0.0521 0.0232 711 ALA A CB 5401 N N . LEU A 719 ? 0.2536 0.2615 0.2806 -0.0325 0.0709 0.0218 712 LEU A N 5402 C CA . LEU A 719 ? 0.2685 0.2777 0.3094 -0.0362 0.0815 0.0242 712 LEU A CA 5403 C C . LEU A 719 ? 0.2844 0.2973 0.3234 -0.0355 0.0906 0.0236 712 LEU A C 5404 O O . LEU A 719 ? 0.2890 0.3016 0.3357 -0.0382 0.1015 0.0266 712 LEU A O 5405 C CB . LEU A 719 ? 0.2683 0.2850 0.3358 -0.0389 0.0778 0.0205 712 LEU A CB 5406 C CG . LEU A 719 ? 0.2669 0.2788 0.3416 -0.0410 0.0721 0.0218 712 LEU A CG 5407 C CD1 . LEU A 719 ? 0.2641 0.2838 0.3620 -0.0422 0.0652 0.0161 712 LEU A CD1 5408 C CD2 . LEU A 719 ? 0.3039 0.3084 0.3808 -0.0450 0.0821 0.0285 712 LEU A CD2 5409 N N . PHE A 720 ? 0.2916 0.3083 0.3223 -0.0321 0.0865 0.0194 713 PHE A N 5410 C CA . PHE A 720 ? 0.3105 0.3315 0.3415 -0.0310 0.0943 0.0175 713 PHE A CA 5411 C C . PHE A 720 ? 0.3303 0.3431 0.3433 -0.0306 0.1050 0.0226 713 PHE A C 5412 O O . PHE A 720 ? 0.3327 0.3373 0.3233 -0.0285 0.1027 0.0249 713 PHE A O 5413 C CB . PHE A 720 ? 0.2999 0.3259 0.3256 -0.0272 0.0874 0.0118 713 PHE A CB 5414 C CG . PHE A 720 ? 0.3130 0.3436 0.3415 -0.0260 0.0952 0.0094 713 PHE A CG 5415 C CD1 . PHE A 720 ? 0.2924 0.3324 0.3442 -0.0270 0.0969 0.0060 713 PHE A CD1 5416 C CD2 . PHE A 720 ? 0.3375 0.3625 0.3460 -0.0237 0.1009 0.0104 713 PHE A CD2 5417 C CE1 . PHE A 720 ? 0.3431 0.3875 0.3990 -0.0256 0.1047 0.0038 713 PHE A CE1 5418 C CE2 . PHE A 720 ? 0.3280 0.3565 0.3387 -0.0223 0.1088 0.0079 713 PHE A CE2 5419 C CZ . PHE A 720 ? 0.3589 0.3974 0.3940 -0.0233 0.1111 0.0047 713 PHE A CZ 5420 N N . ASP A 721 ? 0.3353 0.3501 0.3584 -0.0326 0.1168 0.0243 714 ASP A N 5421 C CA . ASP A 721 ? 0.3814 0.3885 0.3876 -0.0319 0.1290 0.0289 714 ASP A CA 5422 C C . ASP A 721 ? 0.3919 0.3871 0.3828 -0.0329 0.1300 0.0359 714 ASP A C 5423 O O . ASP A 721 ? 0.4095 0.3952 0.3763 -0.0306 0.1348 0.0395 714 ASP A O 5424 C CB . ASP A 721 ? 0.3804 0.3858 0.3660 -0.0273 0.1281 0.0257 714 ASP A CB 5425 C CG . ASP A 721 ? 0.4314 0.4296 0.4003 -0.0260 0.1418 0.0292 714 ASP A CG 5426 O OD1 . ASP A 721 ? 0.4137 0.4139 0.3951 -0.0283 0.1537 0.0318 714 ASP A OD1 5427 O OD2 . ASP A 721 ? 0.4736 0.4641 0.4170 -0.0224 0.1405 0.0293 714 ASP A OD2 5428 N N . ILE A 722 ? 0.3861 0.3812 0.3904 -0.0360 0.1252 0.0376 715 ILE A N 5429 C CA . ILE A 722 ? 0.3969 0.3804 0.3869 -0.0365 0.1239 0.0438 715 ILE A CA 5430 C C . ILE A 722 ? 0.4402 0.4142 0.4206 -0.0378 0.1381 0.0515 715 ILE A C 5431 O O . ILE A 722 ? 0.4577 0.4197 0.4153 -0.0360 0.1384 0.0569 715 ILE A O 5432 C CB . ILE A 722 ? 0.3753 0.3599 0.3819 -0.0393 0.1152 0.0435 715 ILE A CB 5433 C CG1 . ILE A 722 ? 0.3806 0.3534 0.3692 -0.0382 0.1110 0.0487 715 ILE A CG1 5434 C CG2 . ILE A 722 ? 0.3822 0.3716 0.4162 -0.0443 0.1217 0.0444 715 ILE A CG2 5435 C CD1 . ILE A 722 ? 0.3507 0.3246 0.3502 -0.0391 0.0996 0.0466 715 ILE A CD1 5436 N N . GLU A 723 ? 0.4510 0.4301 0.4483 -0.0406 0.1498 0.0521 716 GLU A N 5437 C CA . GLU A 723 ? 0.5126 0.4834 0.5032 -0.0421 0.1652 0.0596 716 GLU A CA 5438 C C . GLU A 723 ? 0.5410 0.5030 0.4999 -0.0374 0.1708 0.0617 716 GLU A C 5439 O O . GLU A 723 ? 0.5697 0.5215 0.5148 -0.0374 0.1826 0.0687 716 GLU A O 5440 C CB . GLU A 723 ? 0.5051 0.4845 0.5237 -0.0462 0.1770 0.0595 716 GLU A CB 5441 C CG . GLU A 723 ? 0.5380 0.5280 0.5635 -0.0441 0.1810 0.0534 716 GLU A CG 5442 C CD . GLU A 723 ? 0.5577 0.5607 0.6013 -0.0435 0.1677 0.0445 716 GLU A CD 5443 O OE1 . GLU A 723 ? 0.4821 0.4856 0.5267 -0.0434 0.1538 0.0421 716 GLU A OE1 5444 O OE2 . GLU A 723 ? 0.5815 0.5939 0.6375 -0.0426 0.1717 0.0400 716 GLU A OE2 5445 N N . SER A 724 ? 0.5361 0.5013 0.4828 -0.0332 0.1620 0.0556 717 SER A N 5446 C CA . SER A 724 ? 0.5677 0.5248 0.4841 -0.0282 0.1653 0.0561 717 SER A CA 5447 C C . SER A 724 ? 0.5859 0.5324 0.4766 -0.0250 0.1552 0.0582 717 SER A C 5448 O O . SER A 724 ? 0.6147 0.5523 0.4783 -0.0209 0.1575 0.0596 717 SER A O 5449 C CB . SER A 724 ? 0.5608 0.5267 0.4785 -0.0254 0.1630 0.0481 717 SER A CB 5450 O OG . SER A 724 ? 0.5497 0.5249 0.4904 -0.0277 0.1734 0.0465 717 SER A OG 5451 N N . LYS A 725 ? 0.5703 0.5173 0.4687 -0.0265 0.1443 0.0585 718 LYS A N 5452 C CA . LYS A 725 ? 0.5810 0.5190 0.4571 -0.0232 0.1337 0.0600 718 LYS A CA 5453 C C . LYS A 725 ? 0.6060 0.5288 0.4617 -0.0224 0.1408 0.0690 718 LYS A C 5454 O O . LYS A 725 ? 0.6115 0.5312 0.4778 -0.0261 0.1501 0.0748 718 LYS A O 5455 C CB . LYS A 725 ? 0.5553 0.4982 0.4456 -0.0245 0.1203 0.0576 718 LYS A CB 5456 C CG . LYS A 725 ? 0.5611 0.5174 0.4676 -0.0244 0.1117 0.0491 718 LYS A CG 5457 C CD . LYS A 725 ? 0.6166 0.5739 0.5064 -0.0201 0.1071 0.0441 718 LYS A CD 5458 C CE . LYS A 725 ? 0.5876 0.5580 0.4951 -0.0203 0.1010 0.0362 718 LYS A CE 5459 N NZ . LYS A 725 ? 0.5748 0.5505 0.4966 -0.0214 0.0899 0.0340 718 LYS A NZ 5460 N N . VAL A 726 ? 0.6279 0.5409 0.4549 -0.0176 0.1359 0.0702 719 VAL A N 5461 C CA . VAL A 726 ? 0.6603 0.5573 0.4630 -0.0157 0.1433 0.0789 719 VAL A CA 5462 C C . VAL A 726 ? 0.6496 0.5395 0.4553 -0.0174 0.1390 0.0851 719 VAL A C 5463 O O . VAL A 726 ? 0.6613 0.5397 0.4582 -0.0181 0.1482 0.0934 719 VAL A O 5464 C CB . VAL A 726 ? 0.6858 0.5734 0.4545 -0.0092 0.1390 0.0780 719 VAL A CB 5465 C CG1 . VAL A 726 ? 0.7457 0.6165 0.4884 -0.0069 0.1486 0.0871 719 VAL A CG1 5466 C CG2 . VAL A 726 ? 0.7133 0.6075 0.4793 -0.0074 0.1427 0.0712 719 VAL A CG2 5467 N N . ASP A 727 ? 0.6186 0.5152 0.4376 -0.0180 0.1257 0.0810 720 ASP A N 5468 C CA . ASP A 727 ? 0.6094 0.4998 0.4318 -0.0191 0.1199 0.0856 720 ASP A CA 5469 C C . ASP A 727 ? 0.5666 0.4681 0.4219 -0.0242 0.1177 0.0822 720 ASP A C 5470 O O . ASP A 727 ? 0.5389 0.4490 0.4043 -0.0237 0.1060 0.0759 720 ASP A O 5471 C CB . ASP A 727 ? 0.6090 0.4974 0.4172 -0.0144 0.1046 0.0828 720 ASP A CB 5472 C CG . ASP A 727 ? 0.6401 0.5205 0.4481 -0.0142 0.0982 0.0877 720 ASP A CG 5473 O OD1 . ASP A 727 ? 0.6560 0.5340 0.4785 -0.0183 0.1041 0.0921 720 ASP A OD1 5474 O OD2 . ASP A 727 ? 0.6965 0.5732 0.4907 -0.0099 0.0871 0.0869 720 ASP A OD2 5475 N N . PRO A 728 ? 0.5530 0.4541 0.4247 -0.0291 0.1288 0.0862 721 PRO A N 5476 C CA . PRO A 728 ? 0.5296 0.4413 0.4331 -0.0339 0.1268 0.0824 721 PRO A CA 5477 C C . PRO A 728 ? 0.5204 0.4304 0.4308 -0.0341 0.1147 0.0819 721 PRO A C 5478 O O . PRO A 728 ? 0.4928 0.4129 0.4243 -0.0360 0.1076 0.0758 721 PRO A O 5479 C CB . PRO A 728 ? 0.5438 0.4523 0.4601 -0.0388 0.1418 0.0884 721 PRO A CB 5480 C CG . PRO A 728 ? 0.5789 0.4726 0.4681 -0.0364 0.1516 0.0968 721 PRO A CG 5481 C CD . PRO A 728 ? 0.5848 0.4762 0.4464 -0.0300 0.1445 0.0940 721 PRO A CD 5482 N N . SER A 729 ? 0.5243 0.4211 0.4165 -0.0317 0.1123 0.0880 722 SER A N 5483 C CA . SER A 729 ? 0.5246 0.4190 0.4225 -0.0314 0.1013 0.0876 722 SER A CA 5484 C C . SER A 729 ? 0.4906 0.3943 0.3888 -0.0280 0.0878 0.0796 722 SER A C 5485 O O . SER A 729 ? 0.4625 0.3727 0.3779 -0.0292 0.0799 0.0751 722 SER A O 5486 C CB . SER A 729 ? 0.5433 0.4214 0.4194 -0.0285 0.1010 0.0958 722 SER A CB 5487 O OG . SER A 729 ? 0.6077 0.4846 0.4911 -0.0279 0.0902 0.0946 722 SER A OG 5488 N N . LYS A 730 ? 0.4844 0.3884 0.3631 -0.0237 0.0854 0.0779 723 LYS A N 5489 C CA . LYS A 730 ? 0.4799 0.3927 0.3584 -0.0207 0.0737 0.0706 723 LYS A CA 5490 C C . LYS A 730 ? 0.4444 0.3719 0.3445 -0.0233 0.0734 0.0632 723 LYS A C 5491 O O . LYS A 730 ? 0.4082 0.3431 0.3198 -0.0228 0.0643 0.0578 723 LYS A O 5492 C CB . LYS A 730 ? 0.4972 0.4060 0.3504 -0.0159 0.0721 0.0707 723 LYS A CB 5493 C CG . LYS A 730 ? 0.5741 0.4906 0.4260 -0.0126 0.0600 0.0638 723 LYS A CG 5494 C CD . LYS A 730 ? 0.6751 0.5865 0.5019 -0.0080 0.0574 0.0638 723 LYS A CD 5495 C CE . LYS A 730 ? 0.6937 0.6150 0.5234 -0.0057 0.0471 0.0560 723 LYS A CE 5496 N NZ . LYS A 730 ? 0.7634 0.6816 0.5728 -0.0024 0.0472 0.0544 723 LYS A NZ 5497 N N . ALA A 731 ? 0.4215 0.3526 0.3266 -0.0256 0.0836 0.0629 724 ALA A N 5498 C CA . ALA A 731 ? 0.3961 0.3406 0.3212 -0.0277 0.0837 0.0562 724 ALA A CA 5499 C C . ALA A 731 ? 0.3606 0.3102 0.3104 -0.0312 0.0801 0.0541 724 ALA A C 5500 O O . ALA A 731 ? 0.3553 0.3141 0.3167 -0.0307 0.0723 0.0477 724 ALA A O 5501 C CB . ALA A 731 ? 0.3894 0.3359 0.3168 -0.0295 0.0967 0.0573 724 ALA A CB 5502 N N . TRP A 732 ? 0.3693 0.3123 0.3267 -0.0345 0.0856 0.0594 725 TRP A N 5503 C CA . TRP A 732 ? 0.3541 0.3006 0.3343 -0.0378 0.0815 0.0571 725 TRP A CA 5504 C C . TRP A 732 ? 0.3597 0.3040 0.3373 -0.0352 0.0692 0.0551 725 TRP A C 5505 O O . TRP A 732 ? 0.3362 0.2869 0.3304 -0.0361 0.0623 0.0497 725 TRP A O 5506 C CB . TRP A 732 ? 0.3617 0.3019 0.3529 -0.0426 0.0915 0.0630 725 TRP A CB 5507 C CG . TRP A 732 ? 0.3590 0.3065 0.3634 -0.0457 0.1022 0.0622 725 TRP A CG 5508 C CD1 . TRP A 732 ? 0.4011 0.3449 0.3953 -0.0460 0.1149 0.0671 725 TRP A CD1 5509 C CD2 . TRP A 732 ? 0.3414 0.3012 0.3717 -0.0485 0.1010 0.0560 725 TRP A CD2 5510 N NE1 . TRP A 732 ? 0.3808 0.3347 0.3944 -0.0488 0.1220 0.0640 725 TRP A NE1 5511 C CE2 . TRP A 732 ? 0.3508 0.3147 0.3872 -0.0505 0.1133 0.0573 725 TRP A CE2 5512 C CE3 . TRP A 732 ? 0.3257 0.2934 0.3740 -0.0490 0.0904 0.0491 725 TRP A CE3 5513 C CZ2 . TRP A 732 ? 0.3425 0.3183 0.4040 -0.0531 0.1149 0.0522 725 TRP A CZ2 5514 C CZ3 . TRP A 732 ? 0.3394 0.3182 0.4112 -0.0516 0.0916 0.0441 725 TRP A CZ3 5515 C CH2 . TRP A 732 ? 0.3208 0.3039 0.3999 -0.0537 0.1036 0.0456 725 TRP A CH2 5516 N N . GLY A 733 ? 0.3642 0.2995 0.3212 -0.0317 0.0662 0.0590 726 GLY A N 5517 C CA . GLY A 733 ? 0.3549 0.2893 0.3079 -0.0283 0.0544 0.0566 726 GLY A CA 5518 C C . GLY A 733 ? 0.3458 0.2918 0.3038 -0.0262 0.0469 0.0488 726 GLY A C 5519 O O . GLY A 733 ? 0.3344 0.2835 0.3006 -0.0251 0.0387 0.0449 726 GLY A O 5520 N N . GLU A 734 ? 0.3430 0.2947 0.2949 -0.0252 0.0499 0.0467 727 GLU A N 5521 C CA . GLU A 734 ? 0.3238 0.2854 0.2787 -0.0230 0.0432 0.0399 727 GLU A CA 5522 C C . GLU A 734 ? 0.3157 0.2864 0.2925 -0.0258 0.0432 0.0350 727 GLU A C 5523 O O . GLU A 734 ? 0.2947 0.2714 0.2781 -0.0243 0.0360 0.0300 727 GLU A O 5524 C CB . GLU A 734 ? 0.3316 0.2953 0.2726 -0.0210 0.0457 0.0391 727 GLU A CB 5525 C CG A GLU A 734 ? 0.3479 0.3219 0.2939 -0.0193 0.0401 0.0322 727 GLU A CG 5526 C CD A GLU A 734 ? 0.3725 0.3476 0.3156 -0.0161 0.0298 0.0299 727 GLU A CD 5527 O OE1 A GLU A 734 ? 0.3642 0.3321 0.2992 -0.0145 0.0264 0.0333 727 GLU A OE1 5528 O OE2 A GLU A 734 ? 0.3752 0.3582 0.3243 -0.0150 0.0256 0.0248 727 GLU A OE2 5529 N N . VAL A 735 ? 0.3104 0.2816 0.2988 -0.0297 0.0512 0.0367 728 VAL A N 5530 C CA . VAL A 735 ? 0.2986 0.2775 0.3095 -0.0323 0.0499 0.0321 728 VAL A CA 5531 C C . VAL A 735 ? 0.2927 0.2691 0.3111 -0.0321 0.0415 0.0304 728 VAL A C 5532 O O . VAL A 735 ? 0.2496 0.2323 0.2767 -0.0309 0.0345 0.0247 728 VAL A O 5533 C CB . VAL A 735 ? 0.3067 0.2859 0.3311 -0.0370 0.0602 0.0347 728 VAL A CB 5534 C CG1 . VAL A 735 ? 0.2991 0.2850 0.3490 -0.0399 0.0572 0.0300 728 VAL A CG1 5535 C CG2 . VAL A 735 ? 0.2971 0.2799 0.3150 -0.0366 0.0689 0.0352 728 VAL A CG2 5536 N N . LYS A 736 ? 0.2981 0.2646 0.3123 -0.0330 0.0424 0.0354 729 LYS A N 5537 C CA . LYS A 736 ? 0.3010 0.2637 0.3212 -0.0324 0.0348 0.0339 729 LYS A CA 5538 C C . LYS A 736 ? 0.3003 0.2656 0.3117 -0.0275 0.0253 0.0300 729 LYS A C 5539 O O . LYS A 736 ? 0.2857 0.2536 0.3059 -0.0265 0.0184 0.0252 729 LYS A O 5540 C CB . LYS A 736 ? 0.3166 0.2670 0.3311 -0.0336 0.0376 0.0406 729 LYS A CB 5541 C CG . LYS A 736 ? 0.3051 0.2522 0.3328 -0.0392 0.0469 0.0444 729 LYS A CG 5542 C CD . LYS A 736 ? 0.3609 0.2942 0.3799 -0.0400 0.0506 0.0523 729 LYS A CD 5543 C CE . LYS A 736 ? 0.3999 0.3274 0.4256 -0.0395 0.0426 0.0509 729 LYS A CE 5544 N NZ . LYS A 736 ? 0.4944 0.4081 0.5173 -0.0416 0.0476 0.0587 729 LYS A NZ 5545 N N . ARG A 737 ? 0.2851 0.2496 0.2793 -0.0243 0.0251 0.0318 730 ARG A N 5546 C CA . ARG A 737 ? 0.2745 0.2426 0.2626 -0.0200 0.0170 0.0281 730 ARG A CA 5547 C C . ARG A 737 ? 0.2517 0.2300 0.2496 -0.0195 0.0139 0.0216 730 ARG A C 5548 O O . ARG A 737 ? 0.2327 0.2131 0.2340 -0.0171 0.0073 0.0178 730 ARG A O 5549 C CB . ARG A 737 ? 0.2795 0.2462 0.2497 -0.0171 0.0172 0.0306 730 ARG A CB 5550 C CG . ARG A 737 ? 0.3063 0.2756 0.2720 -0.0128 0.0090 0.0276 730 ARG A CG 5551 C CD . ARG A 737 ? 0.3506 0.3179 0.2999 -0.0100 0.0078 0.0299 730 ARG A CD 5552 N NE . ARG A 737 ? 0.3731 0.3473 0.3199 -0.0100 0.0097 0.0271 730 ARG A NE 5553 C CZ . ARG A 737 ? 0.3822 0.3642 0.3326 -0.0083 0.0057 0.0223 730 ARG A CZ 5554 N NH1 . ARG A 737 ? 0.3923 0.3768 0.3487 -0.0063 0.0000 0.0196 730 ARG A NH1 5555 N NH2 . ARG A 737 ? 0.3912 0.3781 0.3389 -0.0085 0.0079 0.0202 730 ARG A NH2 5556 N N . GLN A 738 ? 0.2483 0.2323 0.2505 -0.0214 0.0190 0.0205 731 GLN A N 5557 C CA . GLN A 738 ? 0.2480 0.2411 0.2588 -0.0206 0.0162 0.0147 731 GLN A CA 5558 C C . GLN A 738 ? 0.2460 0.2408 0.2732 -0.0220 0.0127 0.0111 731 GLN A C 5559 O O . GLN A 738 ? 0.2291 0.2289 0.2603 -0.0197 0.0070 0.0062 731 GLN A O 5560 C CB . GLN A 738 ? 0.2355 0.2337 0.2474 -0.0222 0.0231 0.0146 731 GLN A CB 5561 C CG . GLN A 738 ? 0.2365 0.2335 0.2310 -0.0200 0.0249 0.0166 731 GLN A CG 5562 C CD . GLN A 738 ? 0.2965 0.2971 0.2851 -0.0163 0.0178 0.0132 731 GLN A CD 5563 O OE1 . GLN A 738 ? 0.2741 0.2801 0.2708 -0.0152 0.0136 0.0089 731 GLN A OE1 5564 N NE2 . GLN A 738 ? 0.3120 0.3090 0.2864 -0.0141 0.0164 0.0153 731 GLN A NE2 5565 N N . ILE A 739 ? 0.2557 0.2459 0.2920 -0.0256 0.0159 0.0135 732 ILE A N 5566 C CA . ILE A 739 ? 0.2498 0.2405 0.3015 -0.0269 0.0113 0.0096 732 ILE A CA 5567 C C . ILE A 739 ? 0.2592 0.2462 0.3055 -0.0232 0.0029 0.0073 732 ILE A C 5568 O O . ILE A 739 ? 0.2538 0.2441 0.3068 -0.0215 -0.0031 0.0018 732 ILE A O 5569 C CB . ILE A 739 ? 0.2451 0.2308 0.3090 -0.0318 0.0163 0.0128 732 ILE A CB 5570 C CG1 . ILE A 739 ? 0.2270 0.2181 0.3000 -0.0354 0.0248 0.0140 732 ILE A CG1 5571 C CG2 . ILE A 739 ? 0.2223 0.2066 0.3017 -0.0329 0.0095 0.0083 732 ILE A CG2 5572 C CD1 . ILE A 739 ? 0.2474 0.2321 0.3288 -0.0404 0.0328 0.0195 732 ILE A CD1 5573 N N . TYR A 740 ? 0.2663 0.2463 0.3006 -0.0216 0.0029 0.0114 733 TYR A N 5574 C CA . TYR A 740 ? 0.2830 0.2591 0.3119 -0.0178 -0.0040 0.0097 733 TYR A CA 5575 C C . TYR A 740 ? 0.2705 0.2534 0.2938 -0.0135 -0.0083 0.0055 733 TYR A C 5576 O O . TYR A 740 ? 0.2576 0.2408 0.2829 -0.0106 -0.0142 0.0012 733 TYR A O 5577 C CB . TYR A 740 ? 0.2849 0.2534 0.3015 -0.0167 -0.0025 0.0153 733 TYR A CB 5578 C CG . TYR A 740 ? 0.3455 0.3113 0.3527 -0.0118 -0.0082 0.0149 733 TYR A CG 5579 C CD1 . TYR A 740 ? 0.3640 0.3272 0.3758 -0.0094 -0.0141 0.0112 733 TYR A CD1 5580 C CD2 . TYR A 740 ? 0.3183 0.2839 0.3121 -0.0093 -0.0077 0.0181 733 TYR A CD2 5581 C CE1 . TYR A 740 ? 0.3590 0.3198 0.3630 -0.0047 -0.0184 0.0110 733 TYR A CE1 5582 C CE2 . TYR A 740 ? 0.3106 0.2742 0.2978 -0.0049 -0.0126 0.0180 733 TYR A CE2 5583 C CZ . TYR A 740 ? 0.3622 0.3235 0.3549 -0.0027 -0.0175 0.0146 733 TYR A CZ 5584 O OH . TYR A 740 ? 0.4240 0.3835 0.4113 0.0018 -0.0217 0.0146 733 TYR A OH 5585 N N . VAL A 741 ? 0.2546 0.2421 0.2704 -0.0129 -0.0053 0.0068 734 VAL A N 5586 C CA . VAL A 741 ? 0.2482 0.2419 0.2596 -0.0092 -0.0087 0.0032 734 VAL A CA 5587 C C . VAL A 741 ? 0.2530 0.2520 0.2740 -0.0090 -0.0113 -0.0019 734 VAL A C 5588 O O . VAL A 741 ? 0.2559 0.2562 0.2757 -0.0054 -0.0162 -0.0055 734 VAL A O 5589 C CB . VAL A 741 ? 0.2462 0.2436 0.2485 -0.0089 -0.0051 0.0053 734 VAL A CB 5590 C CG1 . VAL A 741 ? 0.2528 0.2568 0.2533 -0.0059 -0.0078 0.0016 734 VAL A CG1 5591 C CG2 . VAL A 741 ? 0.2521 0.2441 0.2428 -0.0078 -0.0048 0.0097 734 VAL A CG2 5592 N N . ALA A 742 ? 0.2366 0.2381 0.2675 -0.0125 -0.0081 -0.0023 735 ALA A N 5593 C CA . ALA A 742 ? 0.2332 0.2400 0.2746 -0.0122 -0.0111 -0.0073 735 ALA A CA 5594 C C . ALA A 742 ? 0.2267 0.2296 0.2744 -0.0111 -0.0176 -0.0111 735 ALA A C 5595 O O . ALA A 742 ? 0.2165 0.2215 0.2638 -0.0077 -0.0229 -0.0155 735 ALA A O 5596 C CB . ALA A 742 ? 0.2298 0.2406 0.2823 -0.0163 -0.0059 -0.0069 735 ALA A CB 5597 N N . ALA A 743 ? 0.2248 0.2214 0.2772 -0.0136 -0.0172 -0.0092 736 ALA A N 5598 C CA . ALA A 743 ? 0.2260 0.2178 0.2846 -0.0127 -0.0237 -0.0131 736 ALA A CA 5599 C C . ALA A 743 ? 0.2409 0.2299 0.2875 -0.0072 -0.0285 -0.0150 736 ALA A C 5600 O O . ALA A 743 ? 0.2322 0.2209 0.2795 -0.0040 -0.0345 -0.0201 736 ALA A O 5601 C CB . ALA A 743 ? 0.2203 0.2044 0.2848 -0.0166 -0.0214 -0.0098 736 ALA A CB 5602 N N . PHE A 744 ? 0.2270 0.2138 0.2627 -0.0059 -0.0259 -0.0108 737 PHE A N 5603 C CA . PHE A 744 ? 0.2542 0.2394 0.2799 -0.0006 -0.0294 -0.0121 737 PHE A CA 5604 C C . PHE A 744 ? 0.2308 0.2222 0.2529 0.0029 -0.0315 -0.0158 737 PHE A C 5605 O O . PHE A 744 ? 0.2466 0.2361 0.2655 0.0071 -0.0360 -0.0197 737 PHE A O 5606 C CB . PHE A 744 ? 0.2385 0.2221 0.2543 0.0002 -0.0264 -0.0071 737 PHE A CB 5607 C CG . PHE A 744 ? 0.2828 0.2678 0.2904 0.0056 -0.0290 -0.0086 737 PHE A CG 5608 C CD1 . PHE A 744 ? 0.2828 0.2628 0.2895 0.0093 -0.0333 -0.0115 737 PHE A CD1 5609 C CD2 . PHE A 744 ? 0.2655 0.2567 0.2672 0.0070 -0.0269 -0.0076 737 PHE A CD2 5610 C CE1 . PHE A 744 ? 0.2700 0.2516 0.2699 0.0144 -0.0346 -0.0130 737 PHE A CE1 5611 C CE2 . PHE A 744 ? 0.2663 0.2591 0.2622 0.0117 -0.0285 -0.0090 737 PHE A CE2 5612 C CZ . PHE A 744 ? 0.2625 0.2507 0.2575 0.0155 -0.0319 -0.0114 737 PHE A CZ 5613 N N . THR A 745 ? 0.2325 0.2303 0.2542 0.0016 -0.0280 -0.0146 738 THR A N 5614 C CA . THR A 745 ? 0.2303 0.2331 0.2475 0.0052 -0.0294 -0.0173 738 THR A CA 5615 C C . THR A 745 ? 0.2393 0.2423 0.2625 0.0065 -0.0344 -0.0225 738 THR A C 5616 O O . THR A 745 ? 0.2474 0.2505 0.2650 0.0109 -0.0376 -0.0254 738 THR A O 5617 C CB . THR A 745 ? 0.2453 0.2543 0.2618 0.0032 -0.0247 -0.0150 738 THR A CB 5618 O OG1 . THR A 745 ? 0.2240 0.2318 0.2345 0.0020 -0.0210 -0.0106 738 THR A OG1 5619 C CG2 . THR A 745 ? 0.2237 0.2369 0.2354 0.0067 -0.0255 -0.0170 738 THR A CG2 5620 N N . VAL A 746 ? 0.2356 0.2388 0.2705 0.0027 -0.0349 -0.0236 739 VAL A N 5621 C CA . VAL A 746 ? 0.2288 0.2322 0.2711 0.0038 -0.0409 -0.0292 739 VAL A CA 5622 C C . VAL A 746 ? 0.2407 0.2373 0.2789 0.0075 -0.0469 -0.0328 739 VAL A C 5623 O O . VAL A 746 ? 0.2196 0.2155 0.2532 0.0120 -0.0521 -0.0372 739 VAL A O 5624 C CB . VAL A 746 ? 0.2324 0.2383 0.2907 -0.0012 -0.0401 -0.0297 739 VAL A CB 5625 C CG1 . VAL A 746 ? 0.2291 0.2340 0.2971 -0.0001 -0.0482 -0.0362 739 VAL A CG1 5626 C CG2 . VAL A 746 ? 0.2184 0.2317 0.2795 -0.0033 -0.0344 -0.0273 739 VAL A CG2 5627 N N . GLN A 747 ? 0.2532 0.2440 0.2919 0.0059 -0.0462 -0.0309 740 GLN A N 5628 C CA . GLN A 747 ? 0.2587 0.2421 0.2927 0.0097 -0.0514 -0.0343 740 GLN A CA 5629 C C . GLN A 747 ? 0.2467 0.2299 0.2663 0.0158 -0.0515 -0.0347 740 GLN A C 5630 O O . GLN A 747 ? 0.2670 0.2463 0.2813 0.0206 -0.0566 -0.0394 740 GLN A O 5631 C CB . GLN A 747 ? 0.2475 0.2244 0.2839 0.0072 -0.0498 -0.0313 740 GLN A CB 5632 C CG . GLN A 747 ? 0.2785 0.2469 0.3111 0.0112 -0.0553 -0.0353 740 GLN A CG 5633 C CD . GLN A 747 ? 0.2914 0.2562 0.3329 0.0109 -0.0625 -0.0419 740 GLN A CD 5634 O OE1 . GLN A 747 ? 0.2937 0.2611 0.3485 0.0062 -0.0632 -0.0427 740 GLN A OE1 5635 N NE2 . GLN A 747 ? 0.3044 0.2628 0.3389 0.0162 -0.0681 -0.0469 740 GLN A NE2 5636 N N . ALA A 748 ? 0.2317 0.2184 0.2451 0.0158 -0.0460 -0.0299 741 ALA A N 5637 C CA . ALA A 748 ? 0.2247 0.2120 0.2267 0.0212 -0.0451 -0.0298 741 ALA A CA 5638 C C . ALA A 748 ? 0.2263 0.2166 0.2241 0.0245 -0.0470 -0.0328 741 ALA A C 5639 O O . ALA A 748 ? 0.2408 0.2284 0.2297 0.0300 -0.0486 -0.0352 741 ALA A O 5640 C CB . ALA A 748 ? 0.2274 0.2188 0.2259 0.0199 -0.0394 -0.0243 741 ALA A CB 5641 N N . ALA A 749 ? 0.2137 0.2092 0.2172 0.0217 -0.0462 -0.0326 742 ALA A N 5642 C CA . ALA A 749 ? 0.2400 0.2378 0.2399 0.0250 -0.0487 -0.0355 742 ALA A CA 5643 C C . ALA A 749 ? 0.2461 0.2383 0.2453 0.0284 -0.0561 -0.0414 742 ALA A C 5644 O O . ALA A 749 ? 0.2576 0.2476 0.2468 0.0340 -0.0585 -0.0439 742 ALA A O 5645 C CB . ALA A 749 ? 0.2041 0.2082 0.2128 0.0212 -0.0472 -0.0347 742 ALA A CB 5646 N N . ALA A 750 ? 0.2533 0.2431 0.2631 0.0251 -0.0598 -0.0437 743 ALA A N 5647 C CA . ALA A 750 ? 0.2585 0.2423 0.2685 0.0281 -0.0679 -0.0501 743 ALA A CA 5648 C C . ALA A 750 ? 0.2717 0.2486 0.2681 0.0340 -0.0691 -0.0518 743 ALA A C 5649 O O . ALA A 750 ? 0.2639 0.2365 0.2517 0.0395 -0.0743 -0.0565 743 ALA A O 5650 C CB . ALA A 750 ? 0.2596 0.2408 0.2845 0.0229 -0.0709 -0.0518 743 ALA A CB 5651 N N . GLU A 751 ? 0.2608 0.2361 0.2549 0.0333 -0.0644 -0.0482 744 GLU A N 5652 C CA . GLU A 751 ? 0.2668 0.2355 0.2499 0.0389 -0.0652 -0.0500 744 GLU A CA 5653 C C . GLU A 751 ? 0.2637 0.2335 0.2327 0.0451 -0.0625 -0.0495 744 GLU A C 5654 O O . GLU A 751 ? 0.2900 0.2540 0.2488 0.0509 -0.0639 -0.0524 744 GLU A O 5655 C CB . GLU A 751 ? 0.2808 0.2476 0.2664 0.0369 -0.0614 -0.0462 744 GLU A CB 5656 C CG . GLU A 751 ? 0.2733 0.2352 0.2702 0.0326 -0.0651 -0.0478 744 GLU A CG 5657 C CD . GLU A 751 ? 0.3267 0.2857 0.3260 0.0304 -0.0616 -0.0435 744 GLU A CD 5658 O OE1 . GLU A 751 ? 0.3183 0.2796 0.3115 0.0322 -0.0569 -0.0395 744 GLU A OE1 5659 O OE2 . GLU A 751 ? 0.3136 0.2677 0.3220 0.0268 -0.0639 -0.0442 744 GLU A OE2 5660 N N . THR A 752 ? 0.2612 0.2379 0.2298 0.0438 -0.0584 -0.0460 745 THR A N 5661 C CA . THR A 752 ? 0.2727 0.2500 0.2288 0.0494 -0.0560 -0.0455 745 THR A CA 5662 C C . THR A 752 ? 0.2878 0.2599 0.2358 0.0546 -0.0623 -0.0509 745 THR A C 5663 O O . THR A 752 ? 0.3084 0.2776 0.2430 0.0606 -0.0608 -0.0513 745 THR A O 5664 C CB . THR A 752 ? 0.2705 0.2554 0.2278 0.0471 -0.0504 -0.0408 745 THR A CB 5665 O OG1 . THR A 752 ? 0.2702 0.2580 0.2332 0.0449 -0.0538 -0.0422 745 THR A OG1 5666 C CG2 . THR A 752 ? 0.2200 0.2099 0.1851 0.0418 -0.0450 -0.0357 745 THR A CG2 5667 N N . LEU A 753 ? 0.2877 0.2581 0.2437 0.0524 -0.0695 -0.0553 746 LEU A N 5668 C CA . LEU A 753 ? 0.3073 0.2727 0.2568 0.0572 -0.0774 -0.0611 746 LEU A CA 5669 C C . LEU A 753 ? 0.3262 0.2824 0.2714 0.0606 -0.0834 -0.0670 746 LEU A C 5670 O O . LEU A 753 ? 0.3356 0.2859 0.2734 0.0654 -0.0910 -0.0728 746 LEU A O 5671 C CB . LEU A 753 ? 0.2940 0.2637 0.2567 0.0530 -0.0827 -0.0631 746 LEU A CB 5672 C CG . LEU A 753 ? 0.3313 0.3096 0.2982 0.0503 -0.0776 -0.0583 746 LEU A CG 5673 C CD1 . LEU A 753 ? 0.2962 0.2787 0.2780 0.0465 -0.0832 -0.0609 746 LEU A CD1 5674 C CD2 . LEU A 753 ? 0.2981 0.2751 0.2488 0.0566 -0.0756 -0.0569 746 LEU A CD2 5675 N N . SER A 754 ? 0.3235 0.2776 0.2733 0.0583 -0.0809 -0.0658 747 SER A N 5676 C CA . SER A 754 ? 0.3294 0.2741 0.2750 0.0618 -0.0863 -0.0715 747 SER A CA 5677 C C . SER A 754 ? 0.3457 0.2847 0.2714 0.0706 -0.0845 -0.0730 747 SER A C 5678 O O . SER A 754 ? 0.3345 0.2775 0.2521 0.0728 -0.0777 -0.0684 747 SER A O 5679 C CB . SER A 754 ? 0.3313 0.2748 0.2854 0.0579 -0.0831 -0.0691 747 SER A CB 5680 O OG . SER A 754 ? 0.3546 0.3032 0.3260 0.0499 -0.0833 -0.0668 747 SER A OG 5681 N N . GLU A 755 ? 0.3536 0.2828 0.2714 0.0756 -0.0902 -0.0793 748 GLU A N 5682 C CA . GLU A 755 ? 0.3819 0.3047 0.2806 0.0841 -0.0869 -0.0805 748 GLU A CA 5683 C C . GLU A 755 ? 0.3727 0.3002 0.2725 0.0833 -0.0764 -0.0739 748 GLU A C 5684 O O . GLU A 755 ? 0.3653 0.2958 0.2783 0.0778 -0.0744 -0.0711 748 GLU A O 5685 C CB . GLU A 755 ? 0.4056 0.3168 0.2975 0.0890 -0.0944 -0.0885 748 GLU A CB 5686 C CG . GLU A 755 ? 0.4728 0.3794 0.3599 0.0915 -0.1050 -0.0952 748 GLU A CG 5687 C CD . GLU A 755 ? 0.6177 0.5117 0.4908 0.0990 -0.1123 -0.1036 748 GLU A CD 5688 O OE1 . GLU A 755 ? 0.6454 0.5341 0.5269 0.0970 -0.1172 -0.1080 748 GLU A OE1 5689 O OE2 . GLU A 755 ? 0.6534 0.5422 0.5068 0.1068 -0.1131 -0.1057 748 GLU A OE2 5690 N N . VAL A 756 ? 0.3679 0.2962 0.2547 0.0885 -0.0695 -0.0710 749 VAL A N 5691 C CA . VAL A 756 ? 0.3482 0.2834 0.2387 0.0870 -0.0594 -0.0641 749 VAL A CA 5692 C C . VAL A 756 ? 0.3639 0.2950 0.2540 0.0898 -0.0567 -0.0650 749 VAL A C 5693 O O . VAL A 756 ? 0.3547 0.2914 0.2519 0.0876 -0.0502 -0.0600 749 VAL A O 5694 C CB . VAL A 756 ? 0.3469 0.2849 0.2259 0.0912 -0.0523 -0.0604 749 VAL A CB 5695 C CG1 . VAL A 756 ? 0.3473 0.2895 0.2273 0.0885 -0.0549 -0.0590 749 VAL A CG1 5696 C CG2 . VAL A 756 ? 0.3725 0.3007 0.2315 0.1010 -0.0514 -0.0642 749 VAL A CG2 5697 N N . ALA A 757 ? 0.3809 0.3017 0.2619 0.0952 -0.0618 -0.0716 750 ALA A N 5698 C CA . ALA A 757 ? 0.4144 0.3300 0.2948 0.0986 -0.0598 -0.0732 750 ALA A CA 5699 C C . ALA A 757 ? 0.4567 0.3610 0.3329 0.1014 -0.0691 -0.0815 750 ALA A C 5700 O O . ALA A 757 ? 0.4807 0.3803 0.3622 0.1014 -0.0705 -0.0835 750 ALA A O 5701 C CB . ALA A 757 ? 0.4246 0.3394 0.2922 0.1061 -0.0511 -0.0716 750 ALA A CB 5702 O OXT . ALA A 757 ? 0.4680 0.3676 0.3354 0.1040 -0.0755 -0.0864 750 ALA A OXT 5703 C C1 . NAG B . ? 0.5057 0.3763 0.4903 0.0712 0.0336 0.0394 801 NAG A C1 5704 C C2 . NAG B . ? 0.5762 0.4364 0.5693 0.0694 0.0372 0.0404 801 NAG A C2 5705 C C3 . NAG B . ? 0.5884 0.4428 0.5838 0.0637 0.0454 0.0457 801 NAG A C3 5706 C C4 . NAG B . ? 0.5813 0.4285 0.5621 0.0676 0.0495 0.0552 801 NAG A C4 5707 C C5 . NAG B . ? 0.5694 0.4274 0.5407 0.0704 0.0447 0.0531 801 NAG A C5 5708 C C6 . NAG B . ? 0.5680 0.4198 0.5225 0.0750 0.0480 0.0614 801 NAG A C6 5709 C C7 . NAG B . ? 0.6157 0.4817 0.6257 0.0695 0.0305 0.0275 801 NAG A C7 5710 C C8 . NAG B . ? 0.5794 0.4526 0.6018 0.0650 0.0293 0.0183 801 NAG A C8 5711 N N2 . NAG B . ? 0.5822 0.4497 0.5885 0.0652 0.0348 0.0315 801 NAG A N2 5712 O O3 . NAG B . ? 0.6082 0.4521 0.6121 0.0618 0.0486 0.0467 801 NAG A O3 5713 O O4 . NAG B . ? 0.6228 0.4688 0.6096 0.0609 0.0574 0.0584 801 NAG A O4 5714 O O5 . NAG B . ? 0.5006 0.3629 0.4710 0.0755 0.0363 0.0480 801 NAG A O5 5715 O O6 . NAG B . ? 0.6473 0.4846 0.5917 0.0823 0.0479 0.0677 801 NAG A O6 5716 O O7 . NAG B . ? 0.6639 0.5232 0.6675 0.0770 0.0274 0.0309 801 NAG A O7 5717 C C1 . NAG C . ? 0.7078 0.5386 0.6890 0.0629 0.0647 0.0682 802 NAG A C1 5718 C C2 . NAG C . ? 0.7271 0.5593 0.7119 0.0570 0.0733 0.0726 802 NAG A C2 5719 C C3 . NAG C . ? 0.7701 0.5862 0.7524 0.0578 0.0827 0.0830 802 NAG A C3 5720 C C4 . NAG C . ? 0.7980 0.6024 0.7885 0.0576 0.0827 0.0833 802 NAG A C4 5721 C C5 . NAG C . ? 0.7946 0.5988 0.7786 0.0645 0.0730 0.0786 802 NAG A C5 5722 C C6 . NAG C . ? 0.8095 0.6027 0.8021 0.0649 0.0722 0.0778 802 NAG A C6 5723 C C7 . NAG C . ? 0.6650 0.5199 0.6442 0.0546 0.0707 0.0676 802 NAG A C7 5724 C C8 . NAG C . ? 0.6010 0.4651 0.5984 0.0469 0.0681 0.0592 802 NAG A C8 5725 N N2 . NAG C . ? 0.6966 0.5368 0.6701 0.0591 0.0730 0.0736 802 NAG A N2 5726 O O3 . NAG C . ? 0.7862 0.6060 0.7792 0.0503 0.0905 0.0848 802 NAG A O3 5727 O O4 . NAG C . ? 0.8480 0.6359 0.8330 0.0597 0.0913 0.0940 802 NAG A O4 5728 O O5 . NAG C . ? 0.7480 0.5688 0.7386 0.0617 0.0661 0.0684 802 NAG A O5 5729 O O6 . NAG C . ? 0.8003 0.6004 0.8116 0.0566 0.0718 0.0698 802 NAG A O6 5730 O O7 . NAG C . ? 0.6687 0.5289 0.6375 0.0570 0.0706 0.0688 802 NAG A O7 5731 C C1 . NAG D . ? 0.7257 0.6284 0.6732 0.0007 -0.0344 -0.1438 803 NAG A C1 5732 C C2 . NAG D . ? 0.7527 0.6607 0.7080 -0.0037 -0.0430 -0.1420 803 NAG A C2 5733 C C3 . NAG D . ? 0.7996 0.6994 0.7572 -0.0059 -0.0540 -0.1513 803 NAG A C3 5734 C C4 . NAG D . ? 0.8401 0.7320 0.7724 -0.0013 -0.0568 -0.1594 803 NAG A C4 5735 C C5 . NAG D . ? 0.8545 0.7402 0.7776 0.0033 -0.0475 -0.1617 803 NAG A C5 5736 C C6 . NAG D . ? 0.8833 0.7612 0.7793 0.0085 -0.0483 -0.1691 803 NAG A C6 5737 C C7 . NAG D . ? 0.7463 0.6724 0.7196 -0.0082 -0.0402 -0.1265 803 NAG A C7 5738 C C8 . NAG D . ? 0.7566 0.6831 0.7098 -0.0058 -0.0435 -0.1288 803 NAG A C8 5739 N N2 . NAG D . ? 0.7374 0.6542 0.7117 -0.0073 -0.0401 -0.1329 803 NAG A N2 5740 O O3 . NAG D . ? 0.7752 0.6814 0.7421 -0.0099 -0.0615 -0.1490 803 NAG A O3 5741 O O4 . NAG D . ? 0.9142 0.7982 0.8449 -0.0026 -0.0685 -0.1689 803 NAG A O4 5742 O O5 . NAG D . ? 0.7954 0.6895 0.7227 0.0045 -0.0366 -0.1525 803 NAG A O5 5743 O O6 . NAG D . ? 0.8934 0.7765 0.7755 0.0093 -0.0501 -0.1656 803 NAG A O6 5744 O O7 . NAG D . ? 0.7541 0.6877 0.7415 -0.0107 -0.0376 -0.1189 803 NAG A O7 5745 C C1 . NAG E . ? 0.7242 0.5879 0.5531 0.0745 0.0878 -0.1856 804 NAG A C1 5746 C C2 . NAG E . ? 0.7553 0.6080 0.5791 0.0810 0.0926 -0.1955 804 NAG A C2 5747 C C3 . NAG E . ? 0.8106 0.6479 0.6075 0.0828 0.0868 -0.2051 804 NAG A C3 5748 C C4 . NAG E . ? 0.8457 0.6786 0.6422 0.0767 0.0709 -0.2060 804 NAG A C4 5749 C C5 . NAG E . ? 0.7731 0.6193 0.5804 0.0701 0.0670 -0.1948 804 NAG A C5 5750 C C6 . NAG E . ? 0.7148 0.5591 0.5296 0.0638 0.0523 -0.1946 804 NAG A C6 5751 C C7 . NAG E . ? 0.7749 0.6379 0.6172 0.0898 0.1150 -0.1940 804 NAG A C7 5752 C C8 . NAG E . ? 0.7485 0.6165 0.5885 0.0954 0.1309 -0.1936 804 NAG A C8 5753 N N2 . NAG E . ? 0.7679 0.6252 0.5903 0.0866 0.1076 -0.1949 804 NAG A N2 5754 O O3 . NAG E . ? 0.7955 0.6217 0.5880 0.0888 0.0903 -0.2148 804 NAG A O3 5755 O O4 . NAG E . ? 1.0057 0.8265 0.7744 0.0789 0.0667 -0.2136 804 NAG A O4 5756 O O5 . NAG E . ? 0.7357 0.5946 0.5659 0.0694 0.0738 -0.1868 804 NAG A O5 5757 O O6 . NAG E . ? 0.6823 0.5234 0.5162 0.0632 0.0489 -0.1971 804 NAG A O6 5758 O O7 . NAG E . ? 0.7806 0.6449 0.6430 0.0886 0.1097 -0.1933 804 NAG A O7 5773 C C1 . NAG G . ? 1.0855 0.9665 0.7082 0.0403 0.1820 -0.0110 806 NAG A C1 5774 C C2 . NAG G . ? 1.1639 1.0372 0.7735 0.0393 0.1839 -0.0009 806 NAG A C2 5775 C C3 . NAG G . ? 1.1827 1.0460 0.7685 0.0417 0.1672 -0.0016 806 NAG A C3 5776 C C4 . NAG G . ? 1.2111 1.0626 0.7665 0.0483 0.1630 -0.0095 806 NAG A C4 5777 C C5 . NAG G . ? 1.1760 1.0380 0.7516 0.0476 0.1594 -0.0193 806 NAG A C5 5778 C C6 . NAG G . ? 1.1930 1.0449 0.7436 0.0533 0.1509 -0.0288 806 NAG A C6 5779 C C7 . NAG G . ? 1.1634 1.0495 0.8126 0.0306 0.2020 0.0128 806 NAG A C7 5780 C C8 . NAG G . ? 1.1312 1.0292 0.8127 0.0238 0.2005 0.0179 806 NAG A C8 5781 N N2 . NAG G . ? 1.1463 1.0311 0.7865 0.0328 0.1859 0.0054 806 NAG A N2 5782 O O3 . NAG G . ? 1.2206 1.0744 0.7902 0.0419 0.1710 0.0077 806 NAG A O3 5783 O O4 . NAG G . ? 1.2360 1.0786 0.7704 0.0507 0.1470 -0.0104 806 NAG A O4 5784 O O5 . NAG G . ? 1.1427 1.0121 0.7362 0.0463 0.1763 -0.0182 806 NAG A O5 5785 O O6 . NAG G . ? 1.2208 1.0612 0.7458 0.0590 0.1644 -0.0299 806 NAG A O6 5786 O O7 . NAG G . ? 1.1846 1.0627 0.8177 0.0337 0.2175 0.0153 806 NAG A O7 5787 C C1 . NAG H . ? 0.4596 0.5509 0.7052 0.1085 -0.0602 -0.0642 807 NAG A C1 5788 C C2 . NAG H . ? 0.4577 0.5561 0.7128 0.1020 -0.0458 -0.0662 807 NAG A C2 5789 C C3 . NAG H . ? 0.4976 0.6071 0.7811 0.1051 -0.0431 -0.0709 807 NAG A C3 5790 C C4 . NAG H . ? 0.5178 0.6384 0.8240 0.1075 -0.0532 -0.0743 807 NAG A C4 5791 C C5 . NAG H . ? 0.5286 0.6412 0.8229 0.1138 -0.0686 -0.0724 807 NAG A C5 5792 C C6 . NAG H . ? 0.5326 0.6554 0.8483 0.1162 -0.0803 -0.0764 807 NAG A C6 5793 C C7 . NAG H . ? 0.3475 0.4352 0.5721 0.0919 -0.0284 -0.0620 807 NAG A C7 5794 C C8 . NAG H . ? 0.3410 0.4183 0.5467 0.0897 -0.0207 -0.0595 807 NAG A C8 5795 N N2 . NAG H . ? 0.4213 0.5094 0.6563 0.0994 -0.0370 -0.0632 807 NAG A N2 5796 O O3 . NAG H . ? 0.4857 0.6026 0.7782 0.0990 -0.0299 -0.0728 807 NAG A O3 5797 O O4 . NAG H . ? 0.5631 0.6940 0.8970 0.1112 -0.0514 -0.0786 807 NAG A O4 5798 O O5 . NAG H . ? 0.4884 0.5901 0.7547 0.1108 -0.0694 -0.0680 807 NAG A O5 5799 O O6 . NAG H . ? 0.5236 0.6559 0.8497 0.1084 -0.0762 -0.0782 807 NAG A O6 5800 O O7 . NAG H . ? 0.3190 0.4141 0.5492 0.0867 -0.0267 -0.0629 807 NAG A O7 5801 C C1 . NAG I . ? 0.4253 0.4028 0.3808 0.1073 -0.1752 -0.0879 808 NAG A C1 5802 C C2 . NAG I . ? 0.4441 0.4137 0.3794 0.1076 -0.1674 -0.0854 808 NAG A C2 5803 C C3 . NAG I . ? 0.4571 0.4231 0.3940 0.1074 -0.1761 -0.0929 808 NAG A C3 5804 C C4 . NAG I . ? 0.4846 0.4443 0.4158 0.1153 -0.1932 -0.1003 808 NAG A C4 5805 C C5 . NAG I . ? 0.4707 0.4399 0.4248 0.1141 -0.2001 -0.1021 808 NAG A C5 5806 C C6 . NAG I . ? 0.5355 0.4999 0.4876 0.1219 -0.2186 -0.1098 808 NAG A C6 5807 C C7 . NAG I . ? 0.4873 0.4604 0.4155 0.1000 -0.1412 -0.0727 808 NAG A C7 5808 C C8 . NAG I . ? 0.5032 0.4641 0.4028 0.1097 -0.1431 -0.0711 808 NAG A C8 5809 N N2 . NAG I . ? 0.4197 0.3964 0.3640 0.0994 -0.1528 -0.0795 808 NAG A N2 5810 O O3 . NAG I . ? 0.4607 0.4182 0.3762 0.1094 -0.1695 -0.0907 808 NAG A O3 5811 O O4 . NAG I . ? 0.5472 0.5045 0.4840 0.1139 -0.2013 -0.1077 808 NAG A O4 5812 O O5 . NAG I . ? 0.4595 0.4307 0.4084 0.1151 -0.1911 -0.0945 808 NAG A O5 5813 O O6 . NAG I . ? 0.5635 0.5151 0.4835 0.1324 -0.2214 -0.1078 808 NAG A O6 5814 O O7 . NAG I . ? 0.5235 0.5024 0.4593 0.0931 -0.1294 -0.0681 808 NAG A O7 5815 C C1 . NAG J . ? 0.5931 0.5364 0.5034 0.1236 -0.2110 -0.1124 809 NAG A C1 5816 C C2 . NAG J . ? 0.6402 0.5830 0.5641 0.1210 -0.2220 -0.1217 809 NAG A C2 5817 C C3 . NAG J . ? 0.7142 0.6417 0.6102 0.1311 -0.2331 -0.1280 809 NAG A C3 5818 C C4 . NAG J . ? 0.7220 0.6398 0.5882 0.1350 -0.2208 -0.1223 809 NAG A C4 5819 C C5 . NAG J . ? 0.7088 0.6284 0.5645 0.1366 -0.2090 -0.1123 809 NAG A C5 5820 C C6 . NAG J . ? 0.7218 0.6337 0.5520 0.1394 -0.1952 -0.1060 809 NAG A C6 5821 C C7 . NAG J . ? 0.6284 0.5935 0.6140 0.1068 -0.2277 -0.1266 809 NAG A C7 5822 C C8 . NAG J . ? 0.5760 0.5446 0.5666 0.0986 -0.2127 -0.1213 809 NAG A C8 5823 N N2 . NAG J . ? 0.6505 0.6034 0.6044 0.1172 -0.2319 -0.1266 809 NAG A N2 5824 O O3 . NAG J . ? 0.7089 0.6355 0.6182 0.1284 -0.2432 -0.1369 809 NAG A O3 5825 O O4 . NAG J . ? 0.7991 0.7020 0.6377 0.1451 -0.2305 -0.1281 809 NAG A O4 5826 O O5 . NAG J . ? 0.6444 0.5787 0.5279 0.1270 -0.2008 -0.1076 809 NAG A O5 5827 O O6 . NAG J . ? 0.7562 0.6733 0.5987 0.1313 -0.1860 -0.1048 809 NAG A O6 5828 O O7 . NAG J . ? 0.6671 0.6406 0.6781 0.1042 -0.2360 -0.1308 809 NAG A O7 5829 C C1 . NAG K . ? 0.3508 0.2985 0.4351 -0.0006 -0.0746 -0.0506 810 NAG A C1 5830 C C2 . NAG K . ? 0.3384 0.2844 0.4153 -0.0017 -0.0665 -0.0425 810 NAG A C2 5831 C C3 . NAG K . ? 0.4122 0.3476 0.4952 -0.0041 -0.0671 -0.0415 810 NAG A C3 5832 C C4 . NAG K . ? 0.4488 0.3757 0.5273 0.0010 -0.0755 -0.0487 810 NAG A C4 5833 C C5 . NAG K . ? 0.4391 0.3685 0.5215 0.0030 -0.0836 -0.0572 810 NAG A C5 5834 C C6 . NAG K . ? 0.4464 0.3678 0.5168 0.0103 -0.0905 -0.0637 810 NAG A C6 5835 C C7 . NAG K . ? 0.3208 0.2779 0.3904 -0.0050 -0.0527 -0.0308 810 NAG A C7 5836 C C8 . NAG K . ? 0.2563 0.2199 0.3310 -0.0100 -0.0452 -0.0254 810 NAG A C8 5837 N N2 . NAG K . ? 0.3073 0.2607 0.3884 -0.0063 -0.0587 -0.0363 810 NAG A N2 5838 O O3 . NAG K . ? 0.4013 0.3341 0.4762 -0.0043 -0.0607 -0.0342 810 NAG A O3 5839 O O4 . NAG K . ? 0.5053 0.4218 0.5924 -0.0015 -0.0776 -0.0493 810 NAG A O4 5840 O O5 . NAG K . ? 0.3678 0.3072 0.4448 0.0047 -0.0819 -0.0568 810 NAG A O5 5841 O O6 . NAG K . ? 0.5717 0.4908 0.6518 0.0097 -0.0992 -0.0716 810 NAG A O6 5842 O O7 . NAG K . ? 0.3170 0.2725 0.3731 0.0000 -0.0532 -0.0305 810 NAG A O7 5843 C C1 . NAG L . ? 0.5591 0.4702 0.6373 0.0000 -0.0729 -0.0434 811 NAG A C1 5844 C C2 . NAG L . ? 0.6300 0.5288 0.7074 0.0029 -0.0785 -0.0477 811 NAG A C2 5845 C C3 . NAG L . ? 0.6539 0.5460 0.7248 0.0039 -0.0739 -0.0411 811 NAG A C3 5846 C C4 . NAG L . ? 0.6496 0.5415 0.7301 -0.0034 -0.0671 -0.0329 811 NAG A C4 5847 C C5 . NAG L . ? 0.6200 0.5247 0.6980 -0.0052 -0.0620 -0.0296 811 NAG A C5 5848 C C6 . NAG L . ? 0.6624 0.5686 0.7447 -0.0111 -0.0536 -0.0209 811 NAG A C6 5849 C C7 . NAG L . ? 0.6712 0.5643 0.7469 0.0099 -0.0937 -0.0642 811 NAG A C7 5850 C C8 . NAG L . ? 0.6826 0.5739 0.7793 0.0020 -0.0955 -0.0649 811 NAG A C8 5851 N N2 . NAG L . ? 0.6293 0.5265 0.6972 0.0099 -0.0855 -0.0559 811 NAG A N2 5852 O O3 . NAG L . ? 0.6828 0.5631 0.7543 0.0067 -0.0794 -0.0457 811 NAG A O3 5853 O O4 . NAG L . ? 0.6865 0.5724 0.7598 -0.0024 -0.0628 -0.0260 811 NAG A O4 5854 O O5 . NAG L . ? 0.5613 0.4719 0.6480 -0.0065 -0.0661 -0.0359 811 NAG A O5 5855 O O6 . NAG L . ? 0.7282 0.6331 0.8282 -0.0177 -0.0532 -0.0217 811 NAG A O6 5856 O O7 . NAG L . ? 0.7040 0.5948 0.7701 0.0162 -0.0998 -0.0713 811 NAG A O7 5857 C C1 . BMA M . ? 0.7164 0.5889 0.7941 -0.0024 -0.0657 -0.0266 812 BMA A C1 5858 C C2 . BMA M . ? 0.7193 0.5867 0.7960 -0.0056 -0.0588 -0.0165 812 BMA A C2 5859 C C3 . BMA M . ? 0.7728 0.6254 0.8522 -0.0050 -0.0609 -0.0155 812 BMA A C3 5860 C C4 . BMA M . ? 0.7895 0.6383 0.8591 0.0032 -0.0668 -0.0212 812 BMA A C4 5861 C C5 . BMA M . ? 0.8027 0.6575 0.8719 0.0065 -0.0729 -0.0314 812 BMA A C5 5862 C C6 . BMA M . ? 0.7966 0.6490 0.8535 0.0154 -0.0768 -0.0363 812 BMA A C6 5863 O O2 . BMA M . ? 0.6794 0.5521 0.7412 -0.0011 -0.0557 -0.0121 812 BMA A O2 5864 O O3 . BMA M . ? 0.7713 0.6204 0.8454 -0.0066 -0.0543 -0.0054 812 BMA A O3 5865 O O4 . BMA M . ? 0.8469 0.6813 0.9206 0.0038 -0.0694 -0.0214 812 BMA A O4 5866 O O5 . BMA M . ? 0.7530 0.6215 0.8198 0.0052 -0.0702 -0.0309 812 BMA A O5 5867 O O6 . BMA M . ? 0.7924 0.6493 0.8472 0.0185 -0.0820 -0.0453 812 BMA A O6 5868 C C1 . MAN N . ? 0.8279 0.6649 0.9124 -0.0118 -0.0522 -0.0012 813 MAN A C1 5869 C C2 . MAN N . ? 0.8402 0.6702 0.9137 -0.0100 -0.0476 0.0084 813 MAN A C2 5870 C C3 . MAN N . ? 0.8483 0.6868 0.9147 -0.0125 -0.0401 0.0159 813 MAN A C3 5871 C C4 . MAN N . ? 0.8507 0.6929 0.9304 -0.0206 -0.0348 0.0173 813 MAN A C4 5872 C C5 . MAN N . ? 0.8387 0.6890 0.9293 -0.0212 -0.0405 0.0069 813 MAN A C5 5873 C C6 . MAN N . ? 0.8429 0.7017 0.9468 -0.0279 -0.0364 0.0065 813 MAN A C6 5874 O O2 . MAN N . ? 0.8620 0.6775 0.9435 -0.0133 -0.0467 0.0121 813 MAN A O2 5875 O O3 . MAN N . ? 0.8730 0.7050 0.9281 -0.0109 -0.0361 0.0249 813 MAN A O3 5876 O O4 . MAN N . ? 0.8644 0.7148 0.9358 -0.0219 -0.0281 0.0231 813 MAN A O4 5877 O O5 . MAN N . ? 0.8293 0.6699 0.9270 -0.0197 -0.0476 0.0008 813 MAN A O5 5878 O O6 . MAN N . ? 0.8489 0.6998 0.9660 -0.0348 -0.0311 0.0116 813 MAN A O6 5879 ZN ZN . ZN O . ? 0.2736 0.3017 0.3123 0.0271 0.0196 -0.0375 814 ZN A ZN 5880 ZN ZN . ZN P . ? 0.2354 0.2611 0.2694 0.0313 0.0102 -0.0291 815 ZN A ZN 5881 CA CA . CA Q . ? 0.2183 0.2599 0.2335 -0.0030 -0.0050 -0.0188 816 CA A CA 5882 CL CL . CL R . ? 0.2727 0.3093 0.3064 0.0429 -0.0167 -0.0257 817 CL A CL 5883 N N . GLU S . ? 0.2569 0.2693 0.2664 -0.0067 0.0114 0.0104 818 GLU A N 5884 C CA . GLU S . ? 0.2732 0.2679 0.2702 0.0006 0.0198 0.0059 818 GLU A CA 5885 C C . GLU S . ? 0.2931 0.2720 0.3062 0.0169 0.0336 0.0052 818 GLU A C 5886 O O . GLU S . ? 0.2721 0.2647 0.3095 0.0217 0.0381 0.0070 818 GLU A O 5887 C CB . GLU S . ? 0.2578 0.2682 0.2461 -0.0001 0.0214 -0.0056 818 GLU A CB 5888 C CG . GLU S . ? 0.2520 0.2719 0.2553 0.0104 0.0207 -0.0114 818 GLU A CG 5889 C CD . GLU S . ? 0.2700 0.2929 0.2737 0.0148 0.0095 -0.0235 818 GLU A CD 5890 O OE1 . GLU S . ? 0.2737 0.2875 0.2655 0.0103 0.0042 -0.0247 818 GLU A OE1 5891 O OE2 . GLU S . ? 0.2728 0.3015 0.2905 0.0232 -0.0004 -0.0318 818 GLU A OE2 5892 O OXT . GLU S . ? 0.3024 0.2555 0.2996 0.0211 0.0430 0.0004 818 GLU A OXT 5893 N N . ASP T . ? 0.5333 0.5204 0.6944 0.0032 -0.0646 0.0628 819 ASP A N 5894 C CA . ASP T . ? 0.5029 0.5141 0.6455 0.0099 -0.0275 0.0478 819 ASP A CA 5895 C C . ASP T . ? 0.5029 0.5161 0.5913 -0.0071 -0.0266 0.0438 819 ASP A C 5896 O O . ASP T . ? 0.5059 0.5099 0.5729 -0.0256 -0.0453 0.0510 819 ASP A O 5897 C CB . ASP T . ? 0.4892 0.4940 0.6217 0.0223 -0.0054 0.0344 819 ASP A CB 5898 C CG . ASP T . ? 0.4750 0.4586 0.5550 0.0080 -0.0148 0.0346 819 ASP A CG 5899 O OD1 . ASP T . ? 0.4793 0.4502 0.5429 0.0136 -0.0037 0.0266 819 ASP A OD1 5900 O OD2 . ASP T . ? 0.4621 0.4408 0.5113 -0.0142 -0.0319 0.0420 819 ASP A OD2 5901 O OXT . ASP T . ? 0.5020 0.5248 0.5699 -0.0023 -0.0079 0.0301 819 ASP A OXT 5902 O O . HOH U . ? 0.2249 0.2467 0.2320 0.0140 0.0117 -0.0165 901 HOH A O 5903 O O . HOH U . ? 0.2367 0.2685 0.2003 -0.0021 0.0024 -0.0123 902 HOH A O 5904 O O . HOH U . ? 0.2749 0.2627 0.2158 0.0541 -0.0474 -0.0389 903 HOH A O 5905 O O . HOH U . ? 0.2156 0.2370 0.2259 0.0317 0.0027 -0.0170 904 HOH A O 5906 O O . HOH U . ? 0.1944 0.2307 0.1938 0.0133 0.0044 -0.0162 905 HOH A O 5907 O O . HOH U . ? 0.2177 0.2558 0.2172 -0.0030 -0.0062 -0.0219 906 HOH A O 5908 O O . HOH U . ? 0.2375 0.2779 0.2446 0.0007 -0.0006 -0.0138 907 HOH A O 5909 O O . HOH U . ? 0.3113 0.2710 0.3499 0.0256 0.0257 -0.0572 908 HOH A O 5910 O O . HOH U . ? 0.2453 0.2694 0.2588 0.0151 0.0276 -0.0443 909 HOH A O 5911 O O . HOH U . ? 0.2455 0.2556 0.1952 0.0481 -0.0298 -0.0224 910 HOH A O 5912 O O . HOH U . ? 0.2552 0.2507 0.2787 0.0155 0.0192 -0.0368 911 HOH A O 5913 O O . HOH U . ? 0.2705 0.2901 0.2267 0.0596 0.0431 0.0092 912 HOH A O 5914 O O . HOH U . ? 0.3369 0.2515 0.3666 0.0547 0.0234 0.0001 913 HOH A O 5915 O O . HOH U . ? 0.2721 0.2809 0.2669 0.0062 -0.0198 -0.0066 914 HOH A O 5916 O O . HOH U . ? 0.2551 0.2596 0.2163 0.0404 -0.0304 -0.0253 915 HOH A O 5917 O O . HOH U . ? 0.2500 0.2580 0.2893 0.0326 0.0198 -0.0378 916 HOH A O 5918 O O . HOH U . ? 0.2564 0.2923 0.2410 0.0394 0.0113 -0.0013 917 HOH A O 5919 O O . HOH U . ? 0.2320 0.2907 0.3869 0.0677 0.0206 -0.0598 918 HOH A O 5920 O O . HOH U . ? 0.2961 0.2526 0.2254 0.0655 -0.0608 -0.0551 919 HOH A O 5921 O O . HOH U . ? 0.2868 0.2892 0.2080 0.0696 0.0378 0.0061 920 HOH A O 5922 O O . HOH U . ? 0.2618 0.2905 0.2812 0.0537 -0.0316 -0.0245 921 HOH A O 5923 O O . HOH U . ? 0.3574 0.3152 0.2301 0.0876 -0.0362 -0.0429 922 HOH A O 5924 O O . HOH U . ? 0.2691 0.3146 0.3025 -0.0153 0.0457 -0.0084 923 HOH A O 5925 O O . HOH U . ? 0.2383 0.2895 0.2899 0.0145 0.0338 0.0096 924 HOH A O 5926 O O . HOH U . ? 0.2922 0.3060 0.2780 0.0187 0.0536 -0.0641 925 HOH A O 5927 O O . HOH U . ? 0.3013 0.3050 0.2814 0.0712 -0.1047 -0.0590 926 HOH A O 5928 O O . HOH U . ? 0.2348 0.2631 0.2070 0.0482 0.0301 0.0056 927 HOH A O 5929 O O . HOH U . ? 0.2338 0.2412 0.2135 0.0110 -0.0211 0.0004 928 HOH A O 5930 O O . HOH U . ? 0.2557 0.3344 0.3724 0.0334 0.1094 -0.0659 929 HOH A O 5931 O O . HOH U . ? 0.2627 0.3230 0.3211 0.0169 0.0701 -0.0491 930 HOH A O 5932 O O . HOH U . ? 0.3182 0.2920 0.2511 0.0206 0.0445 -0.0890 931 HOH A O 5933 O O . HOH U . ? 0.3140 0.3079 0.3660 0.0418 0.0231 -0.0444 932 HOH A O 5934 O O . HOH U . ? 0.3341 0.3707 0.4331 0.0590 0.0947 -0.0902 933 HOH A O 5935 O O . HOH U . ? 0.2874 0.2711 0.2643 0.0360 -0.0437 -0.0318 934 HOH A O 5936 O O . HOH U . ? 0.2427 0.2743 0.2220 0.0238 -0.0090 -0.0099 935 HOH A O 5937 O O . HOH U . ? 0.2926 0.2581 0.3275 0.0423 0.0181 -0.0208 936 HOH A O 5938 O O . HOH U . ? 0.2752 0.2555 0.3191 0.0040 0.0226 -0.0190 937 HOH A O 5939 O O . HOH U . ? 0.2671 0.3122 0.2661 0.0099 -0.0024 -0.0072 938 HOH A O 5940 O O . HOH U . ? 0.3114 0.2761 0.1625 0.0970 0.0116 -0.0153 939 HOH A O 5941 O O . HOH U . ? 0.3526 0.3190 0.3006 0.0491 0.0647 0.0424 940 HOH A O 5942 O O . HOH U . ? 0.2776 0.2791 0.2729 0.0158 0.0331 -0.0625 941 HOH A O 5943 O O . HOH U . ? 0.3975 0.2958 0.5263 -0.0758 0.0903 0.0743 942 HOH A O 5944 O O . HOH U . ? 0.2997 0.3391 0.3833 -0.0337 0.0775 0.0077 943 HOH A O 5945 O O . HOH U . ? 0.2183 0.2745 0.3563 -0.0244 0.0100 -0.0203 944 HOH A O 5946 O O . HOH U . ? 0.2444 0.2938 0.2812 0.0150 0.0488 -0.0452 945 HOH A O 5947 O O . HOH U . ? 0.2957 0.3238 0.3407 0.0386 0.0797 -0.0769 946 HOH A O 5948 O O . HOH U . ? 0.2376 0.2801 0.2328 -0.0041 0.0395 -0.0207 947 HOH A O 5949 O O . HOH U . ? 0.2750 0.3188 0.3704 0.0454 0.0545 -0.0660 948 HOH A O 5950 O O . HOH U . ? 0.3108 0.2582 0.3593 0.0162 0.0233 -0.0391 949 HOH A O 5951 O O . HOH U . ? 0.3730 0.3733 0.4164 0.0638 0.1091 -0.1096 950 HOH A O 5952 O O . HOH U . ? 0.3519 0.3010 0.4160 0.0731 0.0108 -0.0287 951 HOH A O 5953 O O . HOH U . ? 0.4410 0.3713 0.3724 0.0164 0.0123 -0.1186 952 HOH A O 5954 O O . HOH U . ? 0.2547 0.2988 0.2793 -0.0113 0.0288 -0.0107 953 HOH A O 5955 O O . HOH U . ? 0.2908 0.3023 0.3447 0.0393 0.0229 -0.0443 954 HOH A O 5956 O O . HOH U . ? 0.2754 0.2613 0.3398 0.0508 0.0245 -0.0487 955 HOH A O 5957 O O . HOH U . ? 0.2332 0.2690 0.2240 0.0025 0.0076 -0.0231 956 HOH A O 5958 O O . HOH U . ? 0.2494 0.2777 0.2833 -0.0137 -0.0171 -0.0384 957 HOH A O 5959 O O . HOH U . ? 0.3820 0.3335 0.2121 0.0994 -0.0248 -0.0196 958 HOH A O 5960 O O . HOH U . ? 0.2634 0.2823 0.2160 -0.0008 -0.0058 0.0006 959 HOH A O 5961 O O . HOH U . ? 0.3308 0.2864 0.3736 -0.0310 0.0148 0.0255 960 HOH A O 5962 O O . HOH U . ? 0.2361 0.2766 0.2272 0.0058 0.0010 -0.0144 961 HOH A O 5963 O O . HOH U . ? 0.2548 0.2493 0.2507 0.0488 0.0007 -0.0060 962 HOH A O 5964 O O . HOH U . ? 0.3887 0.2901 0.4003 0.0536 0.0320 0.0197 963 HOH A O 5965 O O . HOH U . ? 0.2724 0.3280 0.3318 0.0208 0.0552 -0.0502 964 HOH A O 5966 O O . HOH U . ? 0.3072 0.3170 0.2876 -0.0171 0.0328 0.0107 965 HOH A O 5967 O O . HOH U . ? 0.2935 0.3134 0.2695 0.0277 -0.0195 -0.0150 966 HOH A O 5968 O O . HOH U . ? 0.2520 0.2714 0.2339 0.0219 -0.0203 -0.0119 967 HOH A O 5969 O O . HOH U . ? 0.2742 0.3203 0.2904 0.0227 0.0218 0.0048 968 HOH A O 5970 O O . HOH U . ? 0.3245 0.3667 0.3163 0.0129 -0.0049 -0.0069 969 HOH A O 5971 O O . HOH U . ? 0.3035 0.2745 0.3653 -0.0025 0.0249 -0.0187 970 HOH A O 5972 O O . HOH U . ? 0.3083 0.3619 0.3264 0.0123 -0.0021 -0.0042 971 HOH A O 5973 O O . HOH U . ? 0.3781 0.3845 0.3327 0.0491 -0.0436 -0.0315 972 HOH A O 5974 O O . HOH U . ? 0.2606 0.3493 0.4194 0.0419 -0.0582 -0.0554 973 HOH A O 5975 O O . HOH U . ? 0.2969 0.3091 0.3192 -0.0152 0.0058 0.0014 974 HOH A O 5976 O O . HOH U . ? 0.2977 0.2538 0.3337 0.0434 0.0448 -0.0894 975 HOH A O 5977 O O . HOH U . ? 0.4400 0.3801 0.3971 0.0629 -0.1132 -0.0880 976 HOH A O 5978 O O . HOH U . ? 0.3284 0.4342 0.5640 0.0780 -0.0330 -0.0633 977 HOH A O 5979 O O . HOH U . ? 0.3054 0.3594 0.4002 0.0400 0.0668 -0.0664 978 HOH A O 5980 O O . HOH U . ? 0.2933 0.3405 0.2973 0.0192 0.0010 -0.0029 979 HOH A O 5981 O O . HOH U . ? 0.3976 0.3264 0.2670 0.0935 -0.0857 -0.0759 980 HOH A O 5982 O O . HOH U . ? 0.3900 0.3772 0.4014 0.0536 0.0932 -0.1062 981 HOH A O 5983 O O . HOH U . ? 0.3974 0.3639 0.2578 0.0871 -0.0225 -0.0224 982 HOH A O 5984 O O . HOH U . ? 0.3690 0.3239 0.3323 0.0242 0.0368 -0.1007 983 HOH A O 5985 O O . HOH U . ? 0.3276 0.2872 0.3259 0.0495 0.0160 0.0051 984 HOH A O 5986 O O . HOH U . ? 0.4035 0.3710 0.3914 0.0467 0.0171 0.0083 985 HOH A O 5987 O O . HOH U . ? 0.2915 0.3087 0.3129 0.0566 -0.1044 -0.0640 986 HOH A O 5988 O O . HOH U . ? 0.3795 0.3174 0.4578 -0.0073 0.0169 -0.0456 987 HOH A O 5989 O O . HOH U . ? 0.3188 0.3744 0.3831 0.0155 -0.0275 -0.0338 988 HOH A O 5990 O O . HOH U . ? 0.2968 0.3598 0.3638 0.0204 -0.0069 -0.0323 989 HOH A O 5991 O O . HOH U . ? 0.2846 0.3686 0.4679 0.0656 0.0013 -0.0575 990 HOH A O 5992 O O . HOH U . ? 0.2662 0.2358 0.2429 0.0397 -0.0489 -0.0357 991 HOH A O 5993 O O . HOH U . ? 0.3973 0.4102 0.5119 0.1352 -0.0944 -0.0364 992 HOH A O 5994 O O . HOH U . ? 0.2972 0.3553 0.3658 -0.0168 0.0537 -0.0123 993 HOH A O 5995 O O . HOH U . ? 0.3922 0.3655 0.3479 -0.0268 0.0705 0.0383 994 HOH A O 5996 O O . HOH U . ? 0.5272 0.4179 0.2584 0.1536 -0.1078 -0.0448 995 HOH A O 5997 O O . HOH U . ? 0.2771 0.3620 0.5385 -0.0321 -0.0129 -0.0425 996 HOH A O 5998 O O . HOH U . ? 0.2964 0.3459 0.3098 0.0094 0.0004 -0.0057 997 HOH A O 5999 O O . HOH U . ? 0.4929 0.4091 0.3672 0.1591 -0.1149 -0.0023 998 HOH A O 6000 O O . HOH U . ? 0.4226 0.3461 0.1981 0.1218 -0.0268 -0.0266 999 HOH A O 6001 O O . HOH U . ? 0.3679 0.3436 0.3159 0.0717 -0.1103 -0.0718 1000 HOH A O 6002 O O . HOH U . ? 0.5001 0.3862 0.3998 0.1699 -0.0951 0.0202 1001 HOH A O 6003 O O . HOH U . ? 0.2994 0.3525 0.3093 0.0047 -0.0366 -0.0131 1002 HOH A O 6004 O O . HOH U . ? 0.4876 0.3941 0.2568 0.1402 -0.1165 -0.0587 1003 HOH A O 6005 O O . HOH U . ? 0.4320 0.3454 0.4475 0.0279 0.0814 0.0565 1004 HOH A O 6006 O O . HOH U . ? 0.3736 0.4040 0.3397 -0.0043 0.0705 -0.0200 1005 HOH A O 6007 O O . HOH U . ? 0.2598 0.2754 0.2476 -0.0036 -0.0045 0.0002 1006 HOH A O 6008 O O . HOH U . ? 0.3551 0.3274 0.2898 0.0143 0.0289 -0.0865 1007 HOH A O 6009 O O . HOH U . ? 0.3470 0.3240 0.4229 -0.0118 0.0181 -0.0271 1008 HOH A O 6010 O O . HOH U . ? 0.4321 0.4689 0.4149 0.0093 -0.0136 -0.0048 1009 HOH A O 6011 O O . HOH U . ? 0.3333 0.4186 0.5221 0.0936 -0.1211 -0.0690 1010 HOH A O 6012 O O . HOH U . ? 0.4364 0.3913 0.5070 -0.0415 0.0287 0.0295 1011 HOH A O 6013 O O . HOH U . ? 0.3804 0.4070 0.4148 -0.0133 0.0053 -0.0061 1012 HOH A O 6014 O O . HOH U . ? 0.4122 0.3488 0.4409 0.0368 0.0370 -0.0938 1013 HOH A O 6015 O O . HOH U . ? 0.2985 0.3517 0.3260 -0.0052 0.0914 -0.0226 1014 HOH A O 6016 O O . HOH U . ? 0.4320 0.3920 0.5374 -0.0395 0.0026 0.0093 1015 HOH A O 6017 O O . HOH U . ? 0.3198 0.3436 0.4845 -0.0026 -0.0924 -0.0712 1016 HOH A O 6018 O O . HOH U . ? 0.2877 0.3450 0.4140 -0.0262 0.0278 -0.0140 1017 HOH A O 6019 O O . HOH U . ? 0.2942 0.3329 0.2889 0.0053 0.0055 -0.0187 1018 HOH A O 6020 O O . HOH U . ? 0.3770 0.3803 0.4975 0.0836 0.0877 -0.1073 1019 HOH A O 6021 O O . HOH U . ? 0.4435 0.4065 0.3486 0.0045 -0.0075 -0.0914 1020 HOH A O 6022 O O . HOH U . ? 0.4681 0.4388 0.4245 0.0763 -0.1333 -0.0849 1021 HOH A O 6023 O O . HOH U . ? 0.4389 0.5282 0.5911 0.0051 -0.0089 -0.0409 1022 HOH A O 6024 O O . HOH U . ? 0.3757 0.3689 0.4558 0.0323 -0.1303 -0.0910 1023 HOH A O 6025 O O . HOH U . ? 0.3237 0.3107 0.4151 -0.0224 0.0028 -0.0411 1024 HOH A O 6026 O O . HOH U . ? 0.3848 0.3294 0.4303 0.0188 -0.0862 -0.0626 1025 HOH A O 6027 O O . HOH U . ? 0.4792 0.3844 0.3849 0.1679 -0.1095 0.0081 1026 HOH A O 6028 O O . HOH U . ? 0.3850 0.3979 0.5031 0.0248 -0.1278 -0.0892 1027 HOH A O 6029 O O . HOH U . ? 0.3843 0.3778 0.2876 0.0736 0.0225 -0.0019 1028 HOH A O 6030 O O . HOH U . ? 0.5944 0.4405 0.3835 0.1286 0.0226 0.0717 1029 HOH A O 6031 O O . HOH U . ? 0.2778 0.3124 0.2540 -0.0059 0.0323 -0.0152 1030 HOH A O 6032 O O . HOH U . ? 0.3958 0.3306 0.3543 0.0255 0.0314 -0.1142 1031 HOH A O 6033 O O . HOH U . ? 0.3899 0.4319 0.5353 0.1564 -0.1900 -0.0675 1032 HOH A O 6034 O O . HOH U . ? 0.3451 0.2949 0.3873 0.0174 0.0223 -0.0545 1033 HOH A O 6035 O O . HOH U . ? 0.3409 0.3241 0.3179 0.0513 0.0053 0.0035 1034 HOH A O 6036 O O . HOH U . ? 0.3595 0.3873 0.3608 -0.0195 0.0706 0.0034 1035 HOH A O 6037 O O . HOH U . ? 0.3120 0.3470 0.2863 -0.0014 0.0250 -0.0243 1036 HOH A O 6038 O O . HOH U . ? 0.4777 0.5567 0.5863 0.0073 0.0043 -0.0346 1037 HOH A O 6039 O O . HOH U . ? 0.3998 0.4602 0.4907 0.0178 -0.0422 -0.0423 1038 HOH A O 6040 O O . HOH U . ? 0.4919 0.4391 0.4662 0.0739 0.1160 -0.1411 1039 HOH A O 6041 O O . HOH U . ? 0.2686 0.3523 0.3814 -0.0049 0.0602 -0.0290 1040 HOH A O 6042 O O . HOH U . ? 0.4752 0.4322 0.4254 0.0448 0.0774 -0.1154 1041 HOH A O 6043 O O . HOH U . ? 0.2880 0.3895 0.4812 0.0466 -0.0605 -0.0602 1042 HOH A O 6044 O O . HOH U . ? 0.4376 0.3528 0.2903 0.1023 -0.0793 -0.0796 1043 HOH A O 6045 O O . HOH U . ? 0.5960 0.4701 0.2851 0.1583 -0.0531 -0.0109 1044 HOH A O 6046 O O . HOH U . ? 0.4031 0.3802 0.3863 0.0434 0.0776 -0.1030 1045 HOH A O 6047 O O . HOH U . ? 0.4170 0.4416 0.5125 -0.0454 0.1129 0.0259 1046 HOH A O 6048 O O . HOH U . ? 0.3992 0.3876 0.3687 -0.0285 0.0935 0.0328 1047 HOH A O 6049 O O . HOH U . ? 0.3134 0.3231 0.5042 -0.0264 -0.0625 -0.0525 1048 HOH A O 6050 O O . HOH U . ? 0.4059 0.4540 0.4823 -0.0193 -0.0598 -0.0512 1049 HOH A O 6051 O O . HOH U . ? 0.4392 0.4210 0.4506 0.1432 -0.1273 -0.0291 1050 HOH A O 6052 O O . HOH U . ? 0.4703 0.3931 0.4423 0.0199 0.0190 -0.1172 1051 HOH A O 6053 O O . HOH U . ? 0.2948 0.3715 0.4466 0.0045 -0.0371 -0.0467 1052 HOH A O 6054 O O . HOH U . ? 0.4469 0.3834 0.4067 0.0345 0.0457 -0.1176 1053 HOH A O 6055 O O . HOH U . ? 0.5120 0.4142 0.4231 0.0876 -0.1441 -0.1159 1054 HOH A O 6056 O O . HOH U . ? 0.5272 0.4736 0.5146 -0.0036 -0.0119 -0.1002 1055 HOH A O 6057 O O . HOH U . ? 0.4465 0.4051 0.5010 -0.0264 -0.0018 0.0132 1056 HOH A O 6058 O O . HOH U . ? 0.4479 0.3675 0.3886 0.0689 -0.1043 -0.0887 1057 HOH A O 6059 O O . HOH U . ? 0.5456 0.4492 0.2793 0.1382 -0.0171 -0.0265 1058 HOH A O 6060 O O . HOH U . ? 0.3353 0.4009 0.4485 -0.0024 0.0286 0.0043 1059 HOH A O 6061 O O . HOH U . ? 0.3630 0.3340 0.5530 -0.0427 -0.0393 -0.0300 1060 HOH A O 6062 O O . HOH U . ? 0.6076 0.5110 0.6756 0.0526 0.0344 -0.0825 1061 HOH A O 6063 O O . HOH U . ? 0.4368 0.5271 0.5903 0.0309 -0.0366 -0.0500 1062 HOH A O 6064 O O . HOH U . ? 0.6936 0.5682 0.4246 0.1832 -0.1488 -0.0277 1063 HOH A O 6065 O O . HOH U . ? 0.4070 0.3832 0.3440 0.0034 0.0038 -0.0804 1064 HOH A O 6066 O O . HOH U . ? 0.4091 0.4945 0.5917 0.0817 0.1964 -0.1095 1065 HOH A O 6067 O O . HOH U . ? 0.5074 0.3879 0.1940 0.1549 -0.0178 -0.0230 1066 HOH A O 6068 O O . HOH U . ? 0.4626 0.4371 0.5628 -0.0176 0.0246 -0.0191 1067 HOH A O 6069 O O . HOH U . ? 0.3569 0.4306 0.4916 -0.0200 -0.0480 -0.0378 1068 HOH A O 6070 O O . HOH U . ? 0.3613 0.4657 0.5260 0.0144 0.0568 -0.0462 1069 HOH A O 6071 O O . HOH U . ? 0.2911 0.3478 0.3440 0.0195 0.0085 -0.0318 1070 HOH A O 6072 O O . HOH U . ? 0.3684 0.4218 0.5029 -0.0151 0.0265 -0.0009 1071 HOH A O 6073 O O . HOH U . ? 0.4816 0.4619 0.6328 0.1117 0.0042 -0.0558 1072 HOH A O 6074 O O . HOH U . ? 0.3217 0.4201 0.4702 -0.0029 0.0949 -0.0333 1073 HOH A O 6075 O O . HOH U . ? 0.2532 0.2840 0.2390 0.0035 0.0205 -0.0345 1074 HOH A O 6076 O O . HOH U . ? 0.2507 0.2972 0.2486 0.0069 -0.0092 -0.0081 1075 HOH A O 6077 O O . HOH U . ? 0.5036 0.5132 0.4384 -0.0070 0.1361 -0.0017 1076 HOH A O 6078 O O . HOH U . ? 0.4860 0.4173 0.4407 0.0492 0.1039 0.0716 1077 HOH A O 6079 O O . HOH U . ? 0.4148 0.3790 0.3842 0.0575 0.0102 0.0120 1078 HOH A O 6080 O O . HOH U . ? 0.3518 0.3862 0.4277 -0.0369 0.1222 0.0186 1079 HOH A O 6081 O O . HOH U . ? 0.7550 0.6813 0.5717 -0.0111 0.1177 0.0538 1080 HOH A O 6082 O O . HOH U . ? 0.3727 0.3945 0.3411 -0.0099 0.0223 -0.0004 1081 HOH A O 6083 O O . HOH U . ? 0.4139 0.4849 0.5633 -0.0261 0.0365 -0.0173 1082 HOH A O 6084 O O . HOH U . ? 0.4781 0.5566 0.5826 -0.0050 0.1848 -0.0198 1083 HOH A O 6085 O O . HOH U . ? 0.3727 0.3312 0.3461 0.0365 0.0566 -0.1058 1084 HOH A O 6086 O O . HOH U . ? 0.3696 0.3618 0.4931 0.0843 0.0697 -0.0995 1085 HOH A O 6087 O O . HOH U . ? 0.6204 0.4858 0.4620 -0.0274 0.1293 0.1062 1086 HOH A O 6088 O O . HOH U . ? 0.3898 0.3365 0.4449 0.0518 0.0432 -0.0869 1087 HOH A O 6089 O O . HOH U . ? 0.4675 0.4307 0.4137 0.1540 -0.1611 -0.0387 1088 HOH A O 6090 O O . HOH U . ? 0.6311 0.5135 0.3625 0.1681 -0.1208 -0.0255 1089 HOH A O 6091 O O . HOH U . ? 0.7397 0.5887 0.8217 -0.0335 -0.0125 0.0349 1090 HOH A O 6092 O O . HOH U . ? 0.4932 0.4693 0.5454 -0.0167 -0.0081 -0.0634 1091 HOH A O 6093 O O . HOH U . ? 0.5543 0.6617 0.7486 0.0384 -0.0077 -0.0539 1092 HOH A O 6094 O O . HOH U . ? 0.5872 0.4968 0.4975 0.0871 0.1322 -0.1686 1093 HOH A O 6095 O O . HOH U . ? 0.4592 0.5848 0.6741 0.0084 0.1495 -0.0449 1094 HOH A O 6096 O O . HOH U . ? 0.4339 0.3993 0.4291 0.0446 0.0668 -0.1060 1095 HOH A O 6097 O O . HOH U . ? 0.4243 0.4177 0.3792 -0.0170 0.0364 0.0202 1096 HOH A O 6098 O O . HOH U . ? 0.4434 0.4245 0.4760 0.0582 0.0840 -0.1074 1097 HOH A O 6099 O O . HOH U . ? 0.6209 0.5526 0.3905 0.0676 0.2082 -0.1013 1098 HOH A O 6100 O O . HOH U . ? 0.5086 0.4512 0.5666 0.0099 0.0817 0.0460 1099 HOH A O 6101 O O . HOH U . ? 0.4029 0.3938 0.6168 -0.0594 0.0077 -0.0055 1100 HOH A O 6102 O O . HOH U . ? 0.4727 0.4502 0.6336 -0.0794 0.1792 0.0728 1101 HOH A O 6103 O O . HOH U . ? 0.4840 0.3961 0.5165 0.0411 0.0321 0.0049 1102 HOH A O 6104 O O . HOH U . ? 0.5168 0.4657 0.3727 0.0088 -0.0183 -0.0985 1103 HOH A O 6105 O O . HOH U . ? 0.3363 0.4280 0.5603 0.1085 -0.1103 -0.0673 1104 HOH A O 6106 O O . HOH U . ? 0.4982 0.5465 0.6429 0.1407 -0.2485 -0.1046 1105 HOH A O 6107 O O . HOH U . ? 0.4160 0.4245 0.3981 -0.0085 0.0036 0.0063 1106 HOH A O 6108 O O . HOH U . ? 0.4528 0.4416 0.4411 0.0825 -0.1542 -0.0881 1107 HOH A O 6109 O O . HOH U . ? 0.5095 0.4847 0.4607 0.1313 -0.1978 -0.0836 1108 HOH A O 6110 O O . HOH U . ? 0.3830 0.3586 0.3490 -0.0042 -0.0070 0.0205 1109 HOH A O 6111 O O . HOH U . ? 0.6461 0.6882 0.6678 0.0570 0.2479 -0.0826 1110 HOH A O 6112 O O . HOH U . ? 0.3058 0.4250 0.6005 0.1169 -0.1365 -0.0820 1111 HOH A O 6113 O O . HOH U . ? 0.5711 0.4695 0.6995 0.1051 0.0434 -0.0951 1112 HOH A O 6114 O O . HOH U . ? 0.4458 0.5056 0.6741 -0.0097 -0.0835 -0.0713 1113 HOH A O 6115 O O . HOH U . ? 0.5874 0.5135 0.6456 0.0196 0.0262 -0.0361 1114 HOH A O 6116 O O . HOH U . ? 0.5636 0.4837 0.4792 0.0053 -0.0251 -0.1309 1115 HOH A O 6117 O O . HOH U . ? 0.3431 0.4366 0.5200 0.0464 0.0489 -0.0625 1116 HOH A O 6118 O O . HOH U . ? 0.4333 0.3955 0.3966 0.0959 -0.1887 -0.1106 1117 HOH A O 6119 O O . HOH U . ? 0.4885 0.5488 0.5637 -0.0195 0.1178 -0.0066 1118 HOH A O 6120 O O . HOH U . ? 0.3863 0.3937 0.3849 0.0274 0.0475 0.0222 1119 HOH A O 6121 O O . HOH U . ? 0.6013 0.4620 0.5227 0.0656 0.0992 0.0920 1120 HOH A O 6122 O O . HOH U . ? 0.6407 0.5514 0.5790 0.0657 0.0863 -0.1531 1121 HOH A O 6123 O O . HOH U . ? 0.6648 0.6453 0.5528 0.0803 -0.0027 -0.0198 1122 HOH A O 6124 O O . HOH U . ? 0.3900 0.4522 0.4723 -0.0197 0.0748 -0.0104 1123 HOH A O 6125 O O . HOH U . ? 0.5080 0.4380 0.4081 -0.0164 0.0440 0.0567 1124 HOH A O 6126 O O . HOH U . ? 0.4643 0.4136 0.5814 0.0965 0.0174 -0.0552 1125 HOH A O 6127 O O . HOH U . ? 0.7187 0.6090 0.3736 0.0595 0.1592 -0.0855 1126 HOH A O 6128 O O . HOH U . ? 0.4285 0.3995 0.4715 0.0150 0.0799 0.0436 1127 HOH A O 6129 O O . HOH U . ? 0.7136 0.6234 0.5223 0.1291 -0.1454 -0.0893 1128 HOH A O 6130 O O . HOH U . ? 0.3646 0.3720 0.2820 0.0031 0.0319 -0.0432 1129 HOH A O 6131 O O . HOH U . ? 0.5261 0.5305 0.4538 -0.0017 -0.0029 0.0073 1130 HOH A O 6132 O O . HOH U . ? 0.4024 0.3977 0.4345 -0.0206 -0.0384 -0.0740 1131 HOH A O 6133 O O . HOH U . ? 0.4707 0.4863 0.6622 -0.0163 -0.0843 -0.0672 1132 HOH A O 6134 O O . HOH U . ? 0.5630 0.5001 0.4960 -0.0371 0.1447 0.0720 1133 HOH A O 6135 O O . HOH U . ? 0.2371 0.2756 0.2269 0.0022 0.0114 -0.0233 1134 HOH A O 6136 O O . HOH U . ? 0.4879 0.4451 0.7289 -0.1022 0.1835 0.0846 1135 HOH A O 6137 O O . HOH U . ? 0.4995 0.5371 0.4871 0.0201 -0.0083 -0.0060 1136 HOH A O 6138 O O . HOH U . ? 0.4991 0.5203 0.5367 -0.0334 0.1604 0.0271 1137 HOH A O 6139 O O . HOH U . ? 0.5286 0.4381 0.5817 0.0350 0.0291 -0.0827 1138 HOH A O 6140 O O . HOH U . ? 0.4645 0.5743 0.6470 0.0248 0.0809 -0.0556 1139 HOH A O 6141 O O . HOH U . ? 0.6149 0.6324 0.6286 -0.0262 0.1991 0.0273 1140 HOH A O 6142 O O . HOH U . ? 0.3718 0.4183 0.3795 -0.0039 -0.0296 -0.0234 1141 HOH A O 6143 O O . HOH U . ? 0.5580 0.5518 0.5661 0.1340 -0.1382 -0.0401 1142 HOH A O 6144 O O . HOH U . ? 0.4265 0.3751 0.4419 0.0209 -0.0578 -0.0348 1143 HOH A O 6145 O O . HOH U . ? 0.5808 0.5918 0.6415 0.0874 0.1722 -0.1298 1144 HOH A O 6146 O O . HOH U . ? 0.3603 0.3972 0.3407 -0.0005 0.0370 -0.0274 1145 HOH A O 6147 O O . HOH U . ? 0.5630 0.4228 0.5421 0.0913 0.0180 0.0378 1146 HOH A O 6148 O O . HOH U . ? 0.7588 0.5839 0.4267 0.1546 0.0627 0.0779 1147 HOH A O 6149 O O . HOH U . ? 0.6428 0.5089 0.3253 0.1581 -0.0273 0.0113 1148 HOH A O 6150 O O . HOH U . ? 0.4971 0.4954 0.4486 -0.0211 0.0932 0.0209 1149 HOH A O 6151 O O . HOH U . ? 0.6380 0.4651 0.4363 0.1632 -0.0386 0.0612 1150 HOH A O 6152 O O . HOH U . ? 0.5645 0.5097 0.3277 0.0210 0.0731 -0.0466 1151 HOH A O 6153 O O . HOH U . ? 0.7501 0.6517 0.8026 0.0244 0.0234 -0.0857 1152 HOH A O 6154 O O . HOH U . ? 0.4450 0.5149 0.5263 0.0171 0.0073 -0.0347 1153 HOH A O 6155 O O . HOH U . ? 0.3964 0.4060 0.3646 -0.0199 0.0729 0.0130 1154 HOH A O 6156 O O . HOH U . ? 0.6607 0.5443 0.6785 0.0335 0.0719 0.0532 1155 HOH A O 6157 O O . HOH U . ? 0.7782 0.7372 0.6744 0.1211 -0.1543 -0.0682 1156 HOH A O 6158 O O . HOH U . ? 0.4989 0.6008 0.7583 0.1184 -0.1179 -0.0723 1157 HOH A O 6159 O O . HOH U . ? 0.5515 0.4601 0.5984 0.1338 -0.0353 -0.0010 1158 HOH A O 6160 O O . HOH U . ? 0.4228 0.5034 0.6612 -0.0447 0.0509 -0.0152 1159 HOH A O 6161 O O . HOH U . ? 0.4982 0.3960 0.5377 0.0244 0.0612 0.0358 1160 HOH A O 6162 O O . HOH U . ? 0.6156 0.5187 0.5628 -0.0344 0.0731 0.0770 1161 HOH A O 6163 O O . HOH U . ? 0.4337 0.4990 0.5150 0.0222 0.0438 -0.0466 1162 HOH A O 6164 O O . HOH U . ? 0.4098 0.4496 0.3977 -0.0030 -0.0405 -0.0272 1163 HOH A O 6165 O O . HOH U . ? 0.6210 0.5726 0.6224 0.0703 -0.1781 -0.1200 1164 HOH A O 6166 O O . HOH U . ? 0.5313 0.5796 0.6525 0.0786 0.1603 -0.1122 1165 HOH A O 6167 O O . HOH U . ? 0.4481 0.3803 0.6463 -0.0567 -0.0196 -0.0079 1166 HOH A O 6168 O O . HOH U . ? 0.5175 0.5098 0.6002 -0.0038 0.0534 0.0173 1167 HOH A O 6169 O O . HOH U . ? 0.5029 0.5460 0.6811 0.0911 0.0992 -0.1057 1168 HOH A O 6170 O O . HOH U . ? 0.3798 0.4116 0.4763 -0.0163 0.0127 -0.0141 1169 HOH A O 6171 O O . HOH U . ? 0.5470 0.5696 0.5336 -0.0137 0.0280 0.0017 1170 HOH A O 6172 O O . HOH U . ? 0.4228 0.5235 0.6485 0.0734 -0.0068 -0.0632 1171 HOH A O 6173 O O . HOH U . ? 0.2579 0.2905 0.2357 0.0013 0.0223 -0.0312 1172 HOH A O 6174 O O . HOH U . ? 0.6549 0.6159 0.5692 0.0907 0.2113 -0.1413 1173 HOH A O 6175 O O . HOH U . ? 0.5085 0.5638 0.5809 -0.0186 0.1892 0.0024 1174 HOH A O 6176 O O . HOH U . ? 0.7556 0.5964 0.3801 0.1728 0.0125 0.0239 1175 HOH A O 6177 O O . HOH U . ? 0.6278 0.5477 0.3649 0.0323 0.0503 -0.0894 1176 HOH A O 6178 O O . HOH U . ? 0.5352 0.5613 0.6246 -0.0446 0.1394 0.0296 1177 HOH A O 6179 O O . HOH U . ? 0.4475 0.4667 0.5227 -0.0015 0.0438 0.0118 1178 HOH A O 6180 O O . HOH U . ? 0.4392 0.5686 0.7191 0.0715 -0.0274 -0.0693 1179 HOH A O 6181 O O . HOH U . ? 0.6608 0.6198 0.5437 0.1130 -0.1244 -0.0549 1180 HOH A O 6182 O O . HOH U . ? 0.7998 0.6582 0.5900 0.0507 0.0319 -0.1786 1181 HOH A O 6183 O O . HOH U . ? 0.4338 0.4593 0.4599 0.0167 0.0411 0.0149 1182 HOH A O 6184 O O . HOH U . ? 0.4037 0.4560 0.4822 -0.0004 0.0238 0.0018 1183 HOH A O 6185 O O . HOH U . ? 0.6882 0.5621 0.7132 0.0499 0.0413 0.0253 1184 HOH A O 6186 O O . HOH U . ? 0.6229 0.5295 0.6163 0.0360 0.0963 0.0709 1185 HOH A O 6187 O O . HOH U . ? 0.7057 0.6053 0.6227 0.0910 -0.1695 -0.1292 1186 HOH A O 6188 O O . HOH U . ? 0.6192 0.6568 0.7485 -0.0160 0.0353 0.0028 1187 HOH A O 6189 O O . HOH U . ? 0.5216 0.5130 0.3981 0.0022 0.1173 -0.0127 1188 HOH A O 6190 O O . HOH U . ? 0.5660 0.5996 0.5614 0.0481 0.2270 -0.0749 1189 HOH A O 6191 O O . HOH U . ? 0.5053 0.4182 0.5663 0.0899 0.0061 -0.0167 1190 HOH A O 6192 O O . HOH U . ? 0.6478 0.5954 0.5115 0.1080 -0.1191 -0.0655 1191 HOH A O 6193 O O . HOH U . ? 0.4796 0.4236 0.5847 0.1271 -0.0255 -0.0263 1192 HOH A O 6194 O O . HOH U . ? 0.6766 0.6182 0.7379 0.1487 -0.0687 -0.0103 1193 HOH A O 6195 O O . HOH U . ? 0.4717 0.4053 0.5987 0.0982 0.0441 -0.0898 1194 HOH A O 6196 O O . HOH U . ? 0.6193 0.5411 0.6290 -0.0041 -0.0128 -0.1118 1195 HOH A O 6197 O O . HOH U . ? 0.4316 0.3797 0.4206 0.0375 -0.0581 -0.0400 1196 HOH A O 6198 O O . HOH U . ? 0.5612 0.5028 0.5706 0.0057 0.0086 -0.0907 1197 HOH A O 6199 O O . HOH U . ? 0.6121 0.5137 0.3688 0.1240 0.0805 0.0477 1198 HOH A O 6200 O O . HOH U . ? 0.4820 0.5815 0.7905 0.1180 0.0089 -0.0836 1199 HOH A O 6201 O O . HOH U . ? 0.2965 0.4389 0.6555 0.0244 -0.1137 -0.0950 1200 HOH A O 6202 O O . HOH U . ? 0.3658 0.4073 0.3591 0.0054 0.0011 -0.0150 1201 HOH A O 6203 O O . HOH U . ? 0.5248 0.4782 0.5281 -0.0491 0.1482 0.0695 1202 HOH A O 6204 O O . HOH U . ? 0.4657 0.4734 0.4200 -0.0019 -0.0050 0.0077 1203 HOH A O 6205 O O . HOH U . ? 0.6848 0.5696 0.5547 0.0353 0.0214 -0.1586 1204 HOH A O 6206 O O . HOH U . ? 0.5560 0.6723 0.8477 0.0897 -0.1964 -0.1092 1205 HOH A O 6207 O O . HOH U . ? 0.7491 0.5650 0.3816 0.1907 -0.1617 -0.1196 1206 HOH A O 6208 O O . HOH U . ? 0.6469 0.5799 0.6303 0.0494 -0.1004 -0.0802 1207 HOH A O 6209 O O . HOH U . ? 0.6067 0.4742 0.4484 0.0914 0.0979 0.0916 1208 HOH A O 6210 O O . HOH U . ? 0.9007 0.7142 0.4961 0.1983 -0.0730 -0.0909 1209 HOH A O 6211 O O . HOH U . ? 0.4156 0.5201 0.6124 0.0118 -0.0225 -0.0506 1210 HOH A O 6212 O O . HOH U . ? 0.6747 0.4918 0.4525 0.1457 0.0078 0.0798 1211 HOH A O 6213 O O . HOH U . ? 0.7692 0.6936 0.6242 -0.0176 0.0910 0.0622 1212 HOH A O 6214 O O . HOH U . ? 0.6691 0.4942 0.3648 0.1943 -0.0899 0.0340 1213 HOH A O 6215 O O . HOH U . ? 0.8013 0.6207 0.4459 0.2151 -0.1388 0.0023 1214 HOH A O 6216 O O . HOH U . ? 0.3873 0.4161 0.3414 -0.0024 0.0005 -0.0169 1215 HOH A O 6217 O O . HOH U . ? 0.7433 0.6752 0.6644 -0.0019 -0.0458 -0.1258 1216 HOH A O 6218 O O . HOH U . ? 0.4192 0.5164 0.6690 0.1127 -0.0921 -0.0672 1217 HOH A O 6219 O O . HOH U . ? 0.4012 0.4752 0.5061 -0.0114 0.0381 -0.0226 1218 HOH A O 6220 O O . HOH U . ? 0.3779 0.4653 0.6695 -0.0451 0.0118 -0.0334 1219 HOH A O 6221 O O . HOH U . ? 0.6444 0.4981 0.3596 0.1567 -0.1102 -0.1046 1220 HOH A O 6222 O O . HOH U . ? 0.5568 0.5237 0.4859 -0.0026 -0.0262 -0.0918 1221 HOH A O 6223 O O . HOH U . ? 0.4697 0.6061 0.7571 0.0654 0.1150 -0.0860 1222 HOH A O 6224 O O . HOH U . ? 0.6955 0.6380 0.5440 0.1212 -0.1267 -0.0581 1223 HOH A O 6225 O O . HOH U . ? 0.4570 0.5794 0.7474 0.1018 -0.0973 -0.0758 1224 HOH A O 6226 O O . HOH U . ? 0.7565 0.6532 0.4757 0.1412 0.0604 0.0225 1225 HOH A O 6227 O O . HOH U . ? 0.7222 0.6374 0.7000 0.1569 -0.0845 0.0072 1226 HOH A O 6228 O O . HOH U . ? 0.3671 0.3356 0.6230 -0.0720 0.0049 -0.0045 1227 HOH A O 6229 O O . HOH U . ? 0.4720 0.4905 0.4042 -0.0040 0.0335 -0.0170 1228 HOH A O 6230 O O . HOH U . ? 0.4990 0.5703 0.7013 -0.0331 -0.0144 -0.0280 1229 HOH A O 6231 O O . HOH U . ? 0.6255 0.5181 0.5826 -0.0529 0.1678 0.1062 1230 HOH A O 6232 O O . HOH U . ? 0.5879 0.6876 0.7393 0.0465 0.3083 -0.0623 1231 HOH A O 6233 O O . HOH U . ? 0.7822 0.5629 0.4382 0.1768 0.0147 0.0905 1232 HOH A O 6234 O O . HOH U . ? 0.4336 0.4614 0.3890 -0.0036 0.0380 -0.0210 1233 HOH A O 6235 O O . HOH U . ? 0.3866 0.4842 0.5318 0.0016 0.0697 -0.0369 1234 HOH A O 6236 O O . HOH U . ? 0.5778 0.5787 0.6012 0.1060 -0.2029 -0.1010 1235 HOH A O 6237 O O . HOH U . ? 0.7448 0.5678 0.3346 0.1200 0.2208 -0.1772 1236 HOH A O 6238 O O . HOH U . ? 0.5819 0.4903 0.6531 0.1137 -0.0091 -0.0142 1237 HOH A O 6239 O O . HOH U . ? 0.5323 0.4498 0.5226 0.0344 0.0360 -0.1200 1238 HOH A O 6240 O O . HOH U . ? 0.6200 0.6544 0.6583 -0.0212 0.2153 0.0171 1239 HOH A O 6241 O O . HOH U . ? 0.6691 0.6898 0.6048 -0.0034 0.0093 -0.0140 1240 HOH A O 6242 O O . HOH U . ? 0.4819 0.4619 0.3829 0.0034 -0.0012 -0.0727 1241 HOH A O 6243 O O . HOH U . ? 0.6329 0.6427 0.7046 0.1674 -0.2103 -0.0649 1242 HOH A O 6244 O O . HOH U . ? 0.6571 0.6308 0.5591 0.0781 0.2204 -0.1198 1243 HOH A O 6245 O O . HOH U . ? 0.5357 0.5719 0.7903 0.1404 -0.0112 -0.0725 1244 HOH A O 6246 O O . HOH U . ? 0.6549 0.5335 0.4820 0.0389 0.0211 -0.1629 1245 HOH A O 6247 O O . HOH U . ? 0.6289 0.6081 0.6637 0.0701 0.1055 -0.1207 1246 HOH A O 6248 O O . HOH U . ? 0.8060 0.7155 0.5788 0.1427 -0.0982 -0.0292 1247 HOH A O 6249 O O . HOH U . ? 0.7292 0.5579 0.7625 0.0024 -0.0427 0.0259 1248 HOH A O 6250 O O . HOH U . ? 0.7184 0.6249 0.5509 0.1106 -0.1022 -0.0896 1249 HOH A O 6251 O O . HOH U . ? 0.4221 0.3618 0.4618 0.0105 -0.0611 -0.0356 1250 HOH A O 6252 O O . HOH U . ? 0.3667 0.4943 0.7050 0.1047 0.0731 -0.0984 1251 HOH A O 6253 O O . HOH U . ? 0.5027 0.5662 0.8034 -0.0579 0.0125 -0.0266 1252 HOH A O 6254 O O . HOH U . ? 0.6040 0.6322 0.5669 0.0049 -0.0191 -0.0020 1253 HOH A O 6255 O O . HOH U . ? 0.3696 0.4475 0.5314 -0.0147 0.0011 -0.0323 1254 HOH A O 6256 O O . HOH U . ? 0.4384 0.5040 0.5052 -0.0098 0.0967 -0.0197 1255 HOH A O 6257 O O . HOH U . ? 0.5212 0.5078 0.8582 -0.1111 0.1450 0.0564 1256 HOH A O 6258 O O . HOH U . ? 0.6457 0.7947 1.0110 0.0551 -0.1493 -0.1050 1257 HOH A O 6259 O O . HOH U . ? 0.4355 0.4495 0.3548 -0.0019 0.0169 -0.0240 1258 HOH A O 6260 O O . HOH U . ? 0.5277 0.4709 0.5634 0.0686 0.0767 -0.1241 1259 HOH A O 6261 O O . HOH U . ? 0.6447 0.6201 0.5164 0.0053 -0.0043 -0.0696 1260 HOH A O 6262 O O . HOH U . ? 0.7135 0.5741 0.3634 0.1697 -0.0295 -0.0349 1261 HOH A O 6263 O O . HOH U . ? 0.5067 0.3759 0.4774 0.1038 0.0028 0.0342 1262 HOH A O 6264 O O . HOH U . ? 0.6361 0.5898 0.7314 -0.0132 0.0273 -0.0209 1263 HOH A O 6265 O O . HOH U . ? 0.4305 0.4622 0.4032 0.0047 -0.0129 -0.0039 1264 HOH A O 6266 O O . HOH U . ? 0.6836 0.5902 0.7496 0.0233 0.0285 -0.0339 1265 HOH A O 6267 O O . HOH U . ? 0.6898 0.6800 0.5829 -0.0031 0.1608 0.0045 1266 HOH A O 6268 O O . HOH U . ? 0.7213 0.6383 0.7087 0.0619 0.0718 -0.1401 1267 HOH A O 6269 O O . HOH U . ? 0.6200 0.6411 0.5773 -0.0103 0.0392 -0.0032 1268 HOH A O 6270 O O . HOH U . ? 0.5714 0.7249 0.9394 0.0944 0.0958 -0.0992 1269 HOH A O 6271 O O . HOH U . ? 0.4694 0.5396 0.7391 -0.0273 -0.0550 -0.0601 1270 HOH A O 6272 O O . HOH U . ? 0.5813 0.4297 0.5476 -0.0528 0.1191 0.1155 1271 HOH A O 6273 O O . HOH U . ? 0.4406 0.4166 0.6358 -0.0351 -0.0613 -0.0472 1272 HOH A O 6274 O O . HOH U . ? 0.5846 0.4877 0.6146 -0.0675 0.1742 0.1052 1273 HOH A O 6275 O O . HOH U . ? 0.7611 0.6852 0.6068 0.0976 0.2065 -0.1572 1274 HOH A O 6276 O O . HOH U . ? 0.5004 0.5790 0.7416 0.1129 -0.0408 -0.0637 1275 HOH A O 6277 O O . HOH U . ? 0.5286 0.5176 0.7625 -0.0551 -0.0229 -0.0253 1276 HOH A O 6278 O O . HOH U . ? 0.5060 0.5178 0.5415 0.0841 -0.1652 -0.0889 1277 HOH A O 6279 O O . HOH U . ? 0.6883 0.6192 0.7509 0.0037 0.0184 -0.0538 1278 HOH A O 6280 O O . HOH U . ? 0.4929 0.5043 0.5595 0.0563 -0.1506 -0.0938 1279 HOH A O 6281 O O . HOH U . ? 0.4706 0.5562 0.7700 -0.0348 -0.0332 -0.0534 1280 HOH A O 6282 O O . HOH U . ? 0.4964 0.5127 0.4977 -0.0143 -0.0573 -0.0640 1281 HOH A O 6283 O O . HOH U . ? 0.4617 0.5327 0.6059 -0.0320 0.0854 -0.0054 1282 HOH A O 6284 O O . HOH U . ? 0.5890 0.5520 0.4940 0.0942 -0.1221 -0.0704 1283 HOH A O 6285 O O . HOH U . ? 0.8276 0.6434 0.5448 0.0903 0.0908 -0.2148 1284 HOH A O 6286 O O . HOH U . ? 0.4458 0.5654 0.6493 0.0000 0.1393 -0.0375 1285 HOH A O 6287 O O . HOH U . ? 0.5117 0.5941 0.7691 -0.0530 0.0807 -0.0057 1286 HOH A O 6288 O O . HOH U . ? 0.3449 0.3867 0.3333 0.0082 -0.0092 -0.0073 1287 HOH A O 6289 O O . HOH U . ? 0.3202 0.3472 0.2971 0.0268 -0.0128 -0.0110 1288 HOH A O 6290 O O . HOH U . ? 0.3878 0.4435 0.4652 0.0056 0.0320 0.0075 1289 HOH A O 6291 O O . HOH U . ? 0.4742 0.5165 0.4580 0.0025 -0.0357 -0.0150 1290 HOH A O 6292 O O . HOH U . ? 0.5440 0.4892 0.5827 0.0103 0.0179 -0.0657 1291 HOH A O 6293 O O . HOH U . ? 0.4928 0.4119 0.5075 0.0329 0.0328 -0.1080 1292 HOH A O 6294 O O . HOH U . ? 0.3851 0.4255 0.3780 0.0246 -0.0060 -0.0044 1293 HOH A O 6295 O O . HOH U . ? 0.5491 0.5323 0.6400 0.0830 0.0949 -0.1181 1294 HOH A O 6296 O O . HOH U . ? 0.4816 0.5252 0.5590 -0.0325 0.1370 0.0134 1295 HOH A O 6297 O O . HOH U . ? 0.4113 0.4541 0.5191 -0.0396 0.1001 0.0126 1296 HOH A O 6298 O O . HOH U . ? 0.3848 0.4806 0.6398 -0.0260 -0.0062 -0.0424 1297 HOH A O 6299 O O . HOH U . ? 0.5878 0.6427 0.6727 -0.0258 0.1680 0.0069 1298 HOH A O 6300 O O . HOH U . ? 0.3753 0.4613 0.5781 -0.0160 -0.0119 -0.0407 1299 HOH A O 6301 O O . HOH U . ? 0.4811 0.5210 0.6484 0.1363 -0.1006 -0.0484 1300 HOH A O 6302 O O . HOH U . ? 0.4591 0.4607 0.6518 -0.0112 -0.1073 -0.0814 1301 HOH A O 6303 O O . HOH U . ? 0.6632 0.5552 0.6991 0.0487 0.0323 0.0070 1302 HOH A O 6304 O O . HOH U . ? 0.4531 0.4650 0.3824 -0.0031 0.1188 -0.0113 1303 HOH A O 6305 O O . HOH U . ? 0.4963 0.5643 0.7029 0.1272 -0.1018 -0.0585 1304 HOH A O 6306 O O . HOH U . ? 0.5616 0.4902 0.5097 0.1699 -0.1280 -0.0061 1305 HOH A O 6307 O O . HOH U . ? 0.5936 0.5531 0.5852 0.1599 -0.1340 -0.0207 1306 HOH A O 6308 O O . HOH U . ? 0.5715 0.5006 0.5484 0.0569 -0.1203 -0.0947 1307 HOH A O 6309 O O . HOH U . ? 0.8836 0.6751 0.4770 0.2049 -0.1652 -0.1320 1308 HOH A O 6310 O O . HOH U . ? 0.4459 0.5763 0.6735 0.0164 0.1283 -0.0527 1309 HOH A O 6311 O O . HOH U . ? 0.4817 0.6246 0.7698 0.0530 0.0954 -0.0767 1310 HOH A O 6312 O O . HOH U . ? 0.5985 0.5524 0.6875 -0.0024 0.0727 0.0332 1311 HOH A O 6313 O O . HOH U . ? 0.5018 0.6132 0.7128 0.0407 -0.0378 -0.0585 1312 HOH A O 6314 O O . HOH U . ? 0.5322 0.5300 0.4260 0.0006 -0.0073 -0.0442 1313 HOH A O 6315 O O . HOH U . ? 0.5467 0.5652 0.6689 0.0336 -0.1436 -0.0966 1314 HOH A O 6316 O O . HOH U . ? 0.5422 0.5143 0.5937 0.0589 -0.1815 -0.1200 1315 HOH A O 6317 O O . HOH U . ? 0.5333 0.5149 0.4742 -0.0202 0.0559 0.0291 1316 HOH A O 6318 O O . HOH U . ? 0.6658 0.5929 0.6678 0.0161 0.0172 -0.1036 1317 HOH A O 6319 O O . HOH U . ? 0.5012 0.4413 0.5984 -0.0388 0.0000 0.0146 1318 HOH A O 6320 O O . HOH U . ? 0.6356 0.6357 0.6782 0.1003 -0.2179 -0.1148 1319 HOH A O 6321 O O . HOH U . ? 0.3462 0.4407 0.6325 -0.0454 0.0348 -0.0264 1320 HOH A O 6322 O O . HOH U . ? 0.4437 0.5243 0.6158 -0.0299 0.0592 -0.0150 1321 HOH A O 6323 O O . HOH U . ? 0.4644 0.4537 0.5912 -0.0213 0.0402 -0.0003 1322 HOH A O 6324 O O . HOH U . ? 0.4679 0.4680 0.3610 0.0044 0.0442 -0.0397 1323 HOH A O 6325 O O . HOH U . ? 0.4247 0.4604 0.5046 -0.0069 0.0245 -0.0017 1324 HOH A O 6326 O O . HOH U . ? 0.6339 0.5396 0.5772 0.0744 -0.1385 -0.1123 1325 HOH A O 6327 O O . HOH U . ? 0.6899 0.5784 0.7106 0.0420 0.0467 0.0297 1326 HOH A O 6328 O O . HOH U . ? 0.6986 0.6589 0.5103 0.0448 0.3077 -0.0289 1327 HOH A O 6329 O O . HOH U . ? 0.5601 0.5833 0.5160 -0.0084 0.0733 -0.0099 1328 HOH A O 6330 O O . HOH U . ? 0.6266 0.5640 0.6557 0.0568 -0.1781 -0.1274 1329 HOH A O 6331 O O . HOH U . ? 0.6979 0.6511 0.7387 -0.0043 0.0056 -0.0687 1330 HOH A O 6332 O O . HOH U . ? 0.7087 0.5534 0.5898 0.0793 0.1099 0.1048 1331 HOH A O 6333 O O . HOH U . ? 0.6379 0.5694 0.6613 0.1557 -0.0832 -0.0026 1332 HOH A O 6334 O O . HOH U . ? 0.6511 0.5949 0.7152 0.0193 -0.1066 -0.0793 1333 HOH A O 6335 O O . HOH U . ? 0.4696 0.5320 0.6233 -0.0409 0.1019 0.0049 1334 HOH A O 6336 O O . HOH U . ? 0.7269 0.5731 0.6785 0.1205 -0.0041 0.0445 1335 HOH A O 6337 O O . HOH U . ? 0.5530 0.4274 0.4997 0.0852 0.0255 0.0473 1336 HOH A O 6338 O O . HOH U . ? 0.6575 0.5719 0.4047 0.0315 0.0299 -0.1043 1337 HOH A O 6339 O O . HOH U . ? 0.5760 0.6487 0.6658 -0.0102 0.0593 -0.0221 1338 HOH A O 6340 O O . HOH U . ? 0.6746 0.6160 0.6354 0.0882 -0.1899 -0.1236 1339 HOH A O 6341 O O . HOH U . ? 0.5942 0.5721 0.7290 0.1486 -0.0643 -0.0315 1340 HOH A O 6342 O O . HOH U . ? 0.6811 0.5918 0.4677 0.1510 -0.1285 -0.0382 1341 HOH A O 6343 O O . HOH U . ? 0.8259 0.7159 0.5398 0.0388 0.0200 -0.1248 1342 HOH A O 6344 O O . HOH U . ? 0.4087 0.4477 0.4571 -0.0166 -0.0722 -0.0586 1343 HOH A O 6345 O O . HOH U . ? 0.4544 0.5085 0.5324 -0.0253 0.1376 0.0030 1344 HOH A O 6346 O O . HOH U . ? 0.5043 0.4857 0.5079 0.1511 -0.1504 -0.0365 1345 HOH A O 6347 O O . HOH U . ? 0.6775 0.6106 0.6361 0.0865 0.1342 -0.1572 1346 HOH A O 6348 O O . HOH U . ? 0.4823 0.5209 0.5522 -0.0320 0.1803 0.0210 1347 HOH A O 6349 O O . HOH U . ? 0.4392 0.3580 0.3664 0.0745 -0.0826 -0.0773 1348 HOH A O 6350 O O . HOH U . ? 0.5103 0.5563 0.7228 0.1331 -0.0598 -0.0550 1349 HOH A O 6351 O O . HOH U . ? 0.5061 0.5956 0.6381 -0.0098 0.0960 -0.0256 1350 HOH A O 6352 O O . HOH U . ? 0.5878 0.6192 0.7801 -0.0001 -0.1102 -0.0831 1351 HOH A O 6353 O O . HOH U . ? 0.4671 0.5203 0.5792 -0.0069 0.0322 0.0046 1352 HOH A O 6354 O O . HOH U . ? 0.5851 0.6450 0.6531 -0.0174 0.0943 -0.0103 1353 HOH A O 6355 O O . HOH U . ? 0.5669 0.6463 0.6894 -0.0149 0.1887 -0.0091 1354 HOH A O 6356 O O . HOH U . ? 0.5886 0.5750 0.4909 -0.0006 -0.0755 -0.0746 1355 HOH A O 6357 O O . HOH U . ? 0.6252 0.7009 0.7179 0.0509 0.3383 -0.0587 1356 HOH A O 6358 O O . HOH U . ? 0.6110 0.6094 0.8335 -0.0361 -0.0653 -0.0544 1357 HOH A O 6359 O O . HOH U . ? 0.5434 0.5700 0.5002 -0.0064 0.0484 -0.0146 1358 HOH A O 6360 O O . HOH U . ? 0.4833 0.5248 0.4745 -0.0017 0.0254 -0.0217 1359 HOH A O 6361 O O . HOH U . ? 0.8720 0.6743 0.6046 0.0967 0.0914 -0.2297 1360 HOH A O 6362 O O . HOH U . ? 0.7143 0.6718 0.6047 0.1278 -0.1465 -0.0553 1361 HOH A O 6363 O O . HOH U . ? 0.5922 0.6465 0.7204 -0.0261 -0.0330 -0.0396 1362 HOH A O 6364 O O . HOH U . ? 0.7691 0.6078 0.4657 0.0693 0.0614 -0.1840 1363 HOH A O 6365 O O . HOH U . ? 0.5899 0.5981 0.6957 -0.0267 -0.0042 -0.0386 1364 HOH A O 6366 O O . HOH U . ? 0.6220 0.6397 0.5748 0.0046 -0.0183 0.0033 1365 HOH A O 6367 O O . HOH U . ? 0.5831 0.5983 0.5302 -0.0026 -0.0717 -0.0524 1366 HOH A O 6368 O O . HOH U . ? 0.5442 0.6285 0.8748 -0.0546 0.0078 -0.0353 1367 HOH A O 6369 O O . HOH U . ? 0.5843 0.6184 0.6864 0.1264 -0.2292 -0.1010 1368 HOH A O 6370 O O . HOH U . ? 0.4302 0.5532 0.7187 0.0947 -0.0678 -0.0725 1369 HOH A O 6371 O O . HOH U . ? 0.8324 0.6555 0.5061 0.2136 -0.1369 0.0118 1370 HOH A O 6372 O O . HOH U . ? 0.5346 0.5990 0.6629 -0.0236 -0.0618 -0.0494 1371 HOH A O 6373 O O . HOH U . ? 0.5987 0.6200 0.5625 -0.0129 0.0703 -0.0016 1372 HOH A O 6374 O O . HOH U . ? 0.6024 0.5552 0.5485 0.1608 -0.1504 -0.0266 1373 HOH A O 6375 O O . HOH U . ? 0.6344 0.5017 0.6844 0.0769 0.0212 -0.0024 1374 HOH A O 6376 O O . HOH U . ? 0.4955 0.5154 0.4455 -0.0072 0.0985 -0.0095 1375 HOH A O 6377 O O . HOH U . ? 0.6929 0.6802 0.7208 0.1644 -0.1762 -0.0448 1376 HOH A O 6378 O O . HOH U . ? 0.8208 0.6880 0.6125 0.1079 0.1083 0.0910 1377 HOH A O 6379 O O . HOH U . ? 0.5805 0.5706 0.5237 -0.0203 0.0684 0.0244 1378 HOH A O 6380 O O . HOH U . ? 0.6154 0.5425 0.6686 0.0766 0.0730 -0.1283 1379 HOH A O 6381 O O . HOH U . ? 0.7290 0.6650 0.7235 0.0750 0.1006 -0.1433 1380 HOH A O 6382 O O . HOH U . ? 0.7224 0.5950 0.4545 0.1538 -0.1436 -0.0957 1381 HOH A O 6383 O O . HOH U . ? 0.6913 0.6414 0.7201 0.0044 0.0121 -0.0730 1382 HOH A O 6384 O O . HOH U . ? 0.5541 0.5942 0.6394 -0.0236 -0.0499 -0.0533 1383 HOH A O 6385 O O . HOH U . ? 0.6031 0.5797 0.5264 -0.0036 -0.0327 -0.0834 1384 HOH A O 6386 O O . HOH U . ? 0.5116 0.5780 0.8093 -0.0711 0.0938 0.0063 1385 HOH A O 6387 O O . HOH U . ? 0.5036 0.6059 0.6659 -0.0031 0.1763 -0.0281 1386 HOH A O 6388 O O . HOH U . ? 0.9244 0.7132 0.4869 0.2014 -0.0146 0.0460 1387 HOH A O 6389 O O . HOH U . ? 0.7022 0.5905 0.7753 0.0226 0.0338 -0.0205 1388 HOH A O 6390 O O . HOH U . ? 0.5874 0.5965 0.5043 -0.0037 0.0826 -0.0129 1389 HOH A O 6391 O O . HOH U . ? 0.5103 0.5111 0.6610 0.0925 0.0600 -0.0932 1390 HOH A O 6392 O O . HOH U . ? 0.6450 0.5709 0.6928 0.0462 0.0387 -0.0923 1391 HOH A O 6393 O O . HOH U . ? 0.8403 0.6575 0.6463 0.1739 -0.0509 0.0621 1392 HOH A O 6394 O O . HOH U . ? 0.3449 0.4586 0.5377 -0.0047 0.0992 -0.0350 1393 HOH A O 6395 O O . HOH U . ? 0.4669 0.5201 0.6753 0.1314 -0.0739 -0.0546 1394 HOH A O 6396 O O . HOH U . ? 0.4485 0.5346 0.6170 0.0000 -0.0226 -0.0441 1395 HOH A O 6397 O O . HOH U . ? 0.6938 0.4695 0.4261 0.1387 0.0869 0.1240 1396 HOH A O 6398 O O . HOH U . ? 0.6703 0.6016 0.5211 0.1160 -0.1433 -0.0843 1397 HOH A O 6399 O O . HOH U . ? 0.6415 0.6302 0.5215 0.0019 -0.0188 -0.0532 1398 HOH A O 6400 O O . HOH U . ? 0.6928 0.5189 0.3131 0.1764 0.0050 0.0393 1399 HOH A O 6401 O O . HOH U . ? 0.7879 0.6653 0.6393 0.1155 -0.1745 -0.1355 1400 HOH A O 6402 O O . HOH U . ? 0.7723 0.6317 0.7909 0.0434 0.0608 0.0476 1401 HOH A O 6403 O O . HOH U . ? 0.4959 0.5738 0.6360 -0.0216 0.0511 -0.0182 1402 HOH A O 6404 O O . HOH U . ? 0.7070 0.6465 0.7161 0.0321 -0.0784 -0.0581 1403 HOH A O 6405 O O . HOH U . ? 0.3836 0.3902 0.4261 0.1429 -0.2418 -0.0990 1404 HOH A O 6406 O O . HOH U . ? 0.5931 0.6369 0.7729 0.1747 -0.1950 -0.0658 1405 HOH A O 6407 O O . HOH U . ? 0.5852 0.4574 0.2294 0.0549 0.0727 -0.1161 1406 HOH A O 6408 O O . HOH U . ? 0.8877 0.8664 0.7304 0.0088 -0.0557 -0.0449 1407 HOH A O 6409 O O . HOH U . ? 0.5896 0.6157 0.7002 0.0392 -0.1376 -0.0905 1408 HOH A O 6410 O O . HOH U . ? 0.6126 0.7715 0.9123 0.0259 0.2002 -0.0601 1409 HOH A O 6411 O O . HOH U . ? 0.7602 0.7062 0.5306 0.0203 0.1656 -0.0158 1410 HOH A O 6412 O O . HOH U . ? 0.4927 0.4557 0.6021 0.0907 0.0135 -0.0498 1411 HOH A O 6413 O O . HOH U . ? 0.6040 0.5191 0.6224 0.0226 0.0223 -0.1042 1412 HOH A O 6414 O O . HOH U . ? 0.4275 0.4356 0.3336 -0.0008 0.0017 -0.0287 1413 HOH A O 6415 O O . HOH U . ? 0.4343 0.4758 0.4262 0.0191 -0.0033 -0.0052 1414 HOH A O 6416 O O . HOH U . ? 0.5575 0.5056 0.4772 -0.0139 0.0279 0.0444 1415 HOH A O 6417 O O . HOH U . ? 0.4871 0.5503 0.5694 0.0254 0.0305 -0.0440 1416 HOH A O 6418 O O . HOH U . ? 0.5413 0.4098 0.2132 0.1604 -0.0316 -0.0062 1417 HOH A O 6419 O O . HOH U . ? 0.6137 0.4791 0.2855 0.1578 -0.0059 0.0133 1418 HOH A O 6420 O O . HOH U . ? 0.5924 0.5942 0.4847 0.0016 0.0350 -0.0318 1419 HOH A O 6421 O O . HOH U . ? 0.4742 0.5670 0.6729 0.0228 -0.0744 -0.0657 1420 HOH A O 6422 O O . HOH U . ? 0.5961 0.5177 0.6706 0.0797 0.0636 -0.1194 1421 HOH A O 6423 O O . HOH U . ? 0.6675 0.6413 0.5382 -0.0057 0.1734 0.0191 1422 HOH A O 6424 O O . HOH U . ? 0.6066 0.6796 0.8203 0.0893 0.1096 -0.1032 1423 HOH A O 6425 O O . HOH U . ? 0.7554 0.7523 0.7401 -0.0135 -0.0444 -0.0742 1424 HOH A O 6426 O O . HOH U . ? 0.4372 0.4916 0.5293 0.0899 0.2700 -0.1170 1425 HOH A O 6427 O O . HOH U . ? 0.4254 0.5584 0.6612 0.0272 0.1489 -0.0611 1426 HOH A O 6428 O O . HOH U . ? 0.5884 0.6572 0.6730 0.0210 0.0230 -0.0397 1427 HOH A O 6429 O O . HOH U . ? 0.7228 0.6667 0.7917 0.0354 -0.1550 -0.1137 1428 HOH A O 6430 O O . HOH U . ? 0.5005 0.5150 0.4369 0.0000 -0.0092 0.0009 1429 HOH A O 6431 O O . HOH U . ? 0.6636 0.6888 0.6208 -0.0079 0.0389 -0.0097 1430 HOH A O 6432 O O . HOH U . ? 0.7002 0.6940 0.6306 -0.0176 0.1159 0.0201 1431 HOH A O 6433 O O . HOH U . ? 0.5955 0.6069 0.5485 -0.0151 0.1053 0.0070 1432 HOH A O 6434 O O . HOH U . ? 0.5028 0.6059 0.7941 0.1109 -0.0196 -0.0746 1433 HOH A O 6435 O O . HOH U . ? 0.7509 0.7429 0.6184 0.0021 0.0412 -0.0244 1434 HOH A O 6436 O O . HOH U . ? 0.6224 0.6831 0.7140 0.0350 0.0160 -0.0431 1435 HOH A O 6437 O O . HOH U . ? 0.5497 0.6298 0.6609 0.0179 -0.0019 -0.0385 1436 HOH A O 6438 O O . HOH U . ? 0.4168 0.4575 0.4738 0.0378 0.0033 -0.0331 1437 HOH A O 6439 O O . HOH U . ? 0.4912 0.6136 0.7345 0.0489 -0.0413 -0.0637 1438 HOH A O 6440 O O . HOH U . ? 0.6037 0.6489 0.7681 -0.0526 0.1134 0.0189 1439 HOH A O 6441 O O . HOH U . ? 0.4768 0.4118 0.6993 -0.0717 0.0114 0.0106 1440 HOH A O 6442 O O . HOH U . ? 0.4474 0.5030 0.4933 0.0037 0.0003 -0.0236 1441 HOH A O 6443 O O . HOH U . ? 0.4617 0.5389 0.5605 -0.0099 0.0820 -0.0231 1442 HOH A O 6444 O O . HOH U . ? 0.6154 0.5952 0.7572 0.0946 0.0466 -0.0860 1443 HOH A O 6445 O O . HOH U . ? 0.6745 0.6620 0.7638 0.0397 -0.1580 -0.1077 1444 HOH A O 6446 O O . HOH U . ? 0.5126 0.5064 0.4196 0.0704 0.0058 -0.0108 1445 HOH A O 6447 O O . HOH U . ? 0.4959 0.5966 0.7027 0.0110 -0.0433 -0.0563 1446 HOH A O 6448 O O . HOH U . ? 0.8159 0.7593 0.5779 0.0200 0.0460 -0.0532 1447 HOH A O 6449 O O . HOH U . ? 0.3684 0.4073 0.4779 -0.0232 -0.0083 -0.0290 1448 HOH A O 6450 O O . HOH U . ? 0.6400 0.5561 0.6103 -0.0522 0.1768 0.0954 1449 HOH A O 6451 O O . HOH U . ? 0.6830 0.6601 0.5318 0.0040 0.1392 -0.0050 1450 HOH A O 6452 O O . HOH U . ? 0.5629 0.4707 0.6118 -0.0428 0.0333 0.0513 1451 HOH A O 6453 O O . HOH U . ? 0.7684 0.7299 0.5650 0.0113 0.0435 -0.0322 1452 HOH A O 6454 O O . HOH U . ? 0.7242 0.6777 0.7302 0.1605 -0.1195 -0.0143 1453 HOH A O 6455 O O . HOH U . ? 0.2375 0.2679 0.2719 0.0264 0.0145 -0.0325 1454 HOH A O 6456 O O . HOH U . ? 0.6700 0.7705 0.8448 0.0754 0.2913 -0.0964 1455 HOH A O 6457 O O . HOH U . ? 0.8974 0.7918 0.5459 0.0473 0.1925 -0.0371 1456 HOH A O 6458 O O . HOH U . ? 0.9139 0.7722 0.7967 0.0196 -0.0300 -0.1809 1457 HOH A O 6459 O O . HOH U . ? 0.7212 0.6318 0.4988 0.1442 -0.1193 -0.0455 1458 HOH A O 6460 O O . HOH U . ? 0.7719 0.6360 0.4526 0.1731 -0.1237 -0.0546 1459 HOH A O 6461 O O . HOH U . ? 0.8565 0.7490 0.6366 0.1136 0.1026 0.0708 1460 HOH A O 6462 O O . HOH U . ? 0.7254 0.6572 0.6287 0.0702 0.1175 0.0750 1461 HOH A O 6463 O O . HOH U . ? 0.4832 0.5645 0.6626 0.0349 -0.1002 -0.0730 1462 HOH A O 6464 O O . HOH U . ? 0.4368 0.5261 0.6758 0.0671 -0.1870 -0.1094 1463 HOH A O 6465 O O . HOH U . ? 0.5596 0.6309 0.6822 0.0164 -0.0444 -0.0469 1464 HOH A O 6466 O O . HOH U . ? 0.5959 0.6751 0.7629 0.0142 -0.0616 -0.0577 1465 HOH A O 6467 O O . HOH U . ? 0.5186 0.5967 0.6616 -0.0154 0.0209 -0.0261 1466 HOH A O 6468 O O . HOH U . ? 0.6801 0.8061 0.9020 0.0038 0.0836 -0.0439 1467 HOH A O 6469 O O . HOH U . ? 0.9381 0.8779 0.8004 0.1475 -0.1660 -0.0554 1468 HOH A O 6470 O O . HOH U . ? 0.6610 0.5627 0.7271 0.0314 0.0278 -0.0424 1469 HOH A O 6471 O O . HOH U . ? 0.5720 0.5403 0.6551 -0.0169 0.0097 -0.0418 1470 HOH A O 6472 O O . HOH U . ? 0.7720 0.7099 0.8866 -0.0101 0.0774 0.0341 1471 HOH A O 6473 O O . HOH U . ? 0.5605 0.5303 0.4906 0.0579 0.0739 0.0443 1472 HOH A O 6474 O O . HOH U . ? 0.4699 0.4750 0.4791 0.0294 0.0695 0.0342 1473 HOH A O 6475 O O . HOH U . ? 0.9100 0.7427 0.5358 0.1259 0.2382 -0.1840 1474 HOH A O 6476 O O . HOH U . ? 0.7748 0.6564 0.6548 0.0565 0.0611 -0.1673 1475 HOH A O 6477 O O . HOH U . ? 0.7194 0.6179 0.7816 0.0721 0.0194 -0.0219 1476 HOH A O 6478 O O . HOH U . ? 0.8112 0.6718 0.8959 0.0639 0.0288 -0.0477 1477 HOH A O 6479 O O . HOH U . ? 0.9087 0.8079 0.7022 0.0262 -0.0086 -0.1386 1478 HOH A O 6480 O O . HOH U . ? 0.5814 0.6793 0.7422 -0.0136 0.1358 -0.0216 1479 HOH A O 6481 O O . HOH U . ? 0.6958 0.6787 0.5488 0.0059 0.0184 -0.0438 1480 HOH A O 6482 O O . HOH U . ? 0.5930 0.6237 0.5493 0.0000 -0.0203 -0.0143 1481 HOH A O 6483 O O . HOH U . ? 0.5660 0.7299 0.8939 0.0025 0.2745 -0.0333 1482 HOH A O 6484 O O . HOH U . ? 0.5519 0.6802 0.8080 0.0513 0.0594 -0.0701 1483 HOH A O 6485 O O . HOH U . ? 0.7493 0.9068 1.1771 0.0323 -0.1610 -0.1180 1484 HOH A O # _database_PDB_caveat.id 1 _database_PDB_caveat.text ;ATOM 'NE ARG 363 A' HAS OCCUPANCY 1.100 ; # 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 55 LYS LYS 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 GLU 431 424 424 GLU GLU 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 TYR 482 475 475 TYR TYR 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 ? ? ? A . n A 1 549 GLU 549 542 ? ? ? A . n A 1 550 THR 550 543 ? ? ? 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 # 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 83 A ASN 76 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 483 A ASN 476 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 645 A ASN 638 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 202 A ASN 195 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 147 A ASN 140 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 466 A ASN 459 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 128 A ASN 121 ? 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,U # 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)' 11690 ? 1 MORE 39 ? 1 'SSA (A^2)' 49320 ? # 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 130.3950000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? U HOH . ? A HOH 1454 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 112.6 ? 2 O ? U HOH . ? A HOH 1454 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 109.3 ? 3 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 109.1 ? 4 O ? U HOH . ? A HOH 1454 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 106.5 ? 5 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 100.2 ? 6 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? P ZN . ? A ZN 815 ? 1_555 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 119.0 ? 7 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 104.9 ? 8 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 89.5 ? 9 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 101.2 ? 10 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 O ? U HOH . ? A HOH 1454 ? 1_555 157.7 ? 11 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 O ? U HOH . ? A HOH 1454 ? 1_555 94.2 ? 12 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 O ? U HOH . ? A HOH 1454 ? 1_555 97.9 ? 13 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 88.4 ? 14 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 56.9 ? 15 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 156.4 ? 16 O ? U HOH . ? A HOH 1454 ? 1_555 ZN ? O ZN . ? A ZN 814 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 92.8 ? 17 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? A TYR 279 ? A TYR 272 ? 1_555 80.6 ? 18 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? U HOH . ? A HOH 906 ? 1_555 95.7 ? 19 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? U HOH . ? A HOH 906 ? 1_555 147.3 ? 20 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 104.6 ? 21 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 74.7 ? 22 O ? U HOH . ? A HOH 906 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 74.9 ? 23 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 91.6 ? 24 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 85.1 ? 25 O ? U HOH . ? A HOH 906 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 127.6 ? 26 O ? A THR 276 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 151.3 ? 27 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 86.7 ? 28 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 136.2 ? 29 O ? U HOH . ? A HOH 906 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 75.3 ? 30 O ? A THR 276 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 149.0 ? 31 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 53.4 ? 32 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 174.9 ? 33 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 94.4 ? 34 O ? U HOH . ? A HOH 906 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 88.0 ? 35 O ? A THR 276 ? A THR 269 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 73.0 ? 36 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 88.8 ? 37 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 CA ? Q CA . ? A CA 816 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 97.6 ? # 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' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] 'X-RAY DIFFRACTION' 1 ? refined 17.5911 49.9000 44.8240 0.0282 0.0801 0.0673 0.0173 0.0088 -0.0292 0.6218 1.1878 0.4326 -0.3097 0.0164 0.0834 -0.0576 0.0705 -0.0129 0.0329 -0.0366 -0.2182 -0.0132 0.0488 0.0852 'X-RAY DIFFRACTION' 2 ? refined 17.6273 45.7016 42.5201 0.0324 0.0420 0.0706 0.0079 0.0161 0.0144 4.2040 9.8389 6.8804 4.9122 4.2596 1.7353 0.2435 -0.2915 0.0481 -0.1895 -0.2614 -0.6511 0.0305 0.3649 -0.1057 # 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 55 A 750 ? . . . . ? 'X-RAY DIFFRACTION' 2 1 A 801 A 817 ? . . . . ? 'X-RAY DIFFRACTION' 3 2 A 818 A 819 ? . . . . ? # 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 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A GLY 508 ? ? O A HOH 1463 ? ? 2.01 2 1 NH2 A ARG 363 ? B O A HOH 1461 ? ? 2.11 3 1 OE1 A GLU 276 ? B O A HOH 1187 ? ? 2.11 4 1 OH A TYR 242 ? ? O A HOH 1411 ? ? 2.16 # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A SER 656 ? B 1_555 O A HOH 1261 ? ? 4_566 1.92 2 1 O A HOH 1122 ? ? 1_555 O A HOH 1445 ? ? 2_565 1.93 3 1 OG A SER 656 ? B 1_555 O A HOH 1261 ? ? 4_566 2.01 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 NE _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 ARG _pdbx_validate_rmsd_angle.auth_seq_id_1 440 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CZ _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 ARG _pdbx_validate_rmsd_angle.auth_seq_id_2 440 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 NH2 _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 ARG _pdbx_validate_rmsd_angle.auth_seq_id_3 440 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 117.02 _pdbx_validate_rmsd_angle.angle_target_value 120.30 _pdbx_validate_rmsd_angle.angle_deviation -3.28 _pdbx_validate_rmsd_angle.angle_standard_deviation 0.50 _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 PHE A 164 ? ? 81.92 3.73 2 1 ASN A 178 ? ? 58.08 -125.50 3 1 LYS A 207 ? ? 73.40 -47.04 4 1 VAL A 382 ? ? -132.15 -106.55 5 1 ALA A 452 ? ? -154.41 55.53 6 1 SER A 454 ? ? -28.67 122.79 7 1 SER A 517 ? ? -140.66 -153.09 8 1 ASP A 567 ? ? -156.42 63.30 9 1 ASP A 683 ? ? 59.23 11.88 10 1 ASN A 698 ? ? -164.40 97.58 11 1 PHE A 705 ? ? 35.81 56.06 # 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 TRP 541 ? A TRP 548 63 1 Y 1 A GLU 542 ? A GLU 549 64 1 Y 1 A THR 543 ? A THR 550 65 1 Y 1 A ASP 654 ? A ASP 661 66 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 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 ALPHA-D-MANNOSE MAN 5 'ZINC ION' ZN 6 'CALCIUM ION' CA 7 'CHLORIDE ION' CL 8 'GLUTAMIC ACID' GLU 9 'ASPARTIC ACID' ASP 10 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 801 1755 NAG NAG A . C 2 NAG 2 802 1756 NAG NAG A . D 2 NAG 1 803 1757 NAG NAG A . E 2 NAG 1 804 1758 NAG NAG A . F 2 NAG 2 805 1767 NAG NAG A . G 2 NAG 1 806 1759 NAG NAG A . H 2 NAG 1 807 1760 NAG NAG A . I 2 NAG 1 808 1761 NAG NAG A . J 2 NAG 2 809 1762 NAG NAG A . K 2 NAG 1 810 1763 NAG NAG A . L 2 NAG 2 811 1764 NAG NAG A . M 3 BMA 3 812 1765 BMA BMA A . N 4 MAN 4 813 1766 MAN MAN A . O 5 ZN 1 814 1751 ZN ZN A . P 5 ZN 1 815 1752 ZN ZN A . Q 6 CA 1 816 1753 CA CA A . R 7 CL 1 817 1754 CL CL A . S 8 GLU 1 818 1 GLU GLU A . T 9 ASP 1 819 2 ASP ASP A . U 10 HOH 1 901 1768 HOH HOH A . U 10 HOH 2 902 1769 HOH HOH A . U 10 HOH 3 903 1770 HOH HOH A . U 10 HOH 4 904 1771 HOH HOH A . U 10 HOH 5 905 1772 HOH HOH A . U 10 HOH 6 906 1773 HOH HOH A . U 10 HOH 7 907 1774 HOH HOH A . U 10 HOH 8 908 1775 HOH HOH A . U 10 HOH 9 909 1776 HOH HOH A . U 10 HOH 10 910 1777 HOH HOH A . U 10 HOH 11 911 1778 HOH HOH A . U 10 HOH 12 912 1779 HOH HOH A . U 10 HOH 13 913 1780 HOH HOH A . U 10 HOH 14 914 1781 HOH HOH A . U 10 HOH 15 915 1782 HOH HOH A . U 10 HOH 16 916 1783 HOH HOH A . U 10 HOH 17 917 1784 HOH HOH A . U 10 HOH 18 918 1785 HOH HOH A . U 10 HOH 19 919 1786 HOH HOH A . U 10 HOH 20 920 1787 HOH HOH A . U 10 HOH 21 921 1788 HOH HOH A . U 10 HOH 22 922 1789 HOH HOH A . U 10 HOH 23 923 1790 HOH HOH A . U 10 HOH 24 924 1791 HOH HOH A . U 10 HOH 25 925 1792 HOH HOH A . U 10 HOH 26 926 1793 HOH HOH A . U 10 HOH 27 927 1794 HOH HOH A . U 10 HOH 28 928 1795 HOH HOH A . U 10 HOH 29 929 1796 HOH HOH A . U 10 HOH 30 930 1797 HOH HOH A . U 10 HOH 31 931 1798 HOH HOH A . U 10 HOH 32 932 1799 HOH HOH A . U 10 HOH 33 933 1800 HOH HOH A . U 10 HOH 34 934 1801 HOH HOH A . U 10 HOH 35 935 1802 HOH HOH A . U 10 HOH 36 936 1803 HOH HOH A . U 10 HOH 37 937 1804 HOH HOH A . U 10 HOH 38 938 1805 HOH HOH A . U 10 HOH 39 939 1806 HOH HOH A . U 10 HOH 40 940 1807 HOH HOH A . U 10 HOH 41 941 1808 HOH HOH A . U 10 HOH 42 942 1809 HOH HOH A . U 10 HOH 43 943 1810 HOH HOH A . U 10 HOH 44 944 1811 HOH HOH A . U 10 HOH 45 945 1812 HOH HOH A . U 10 HOH 46 946 1813 HOH HOH A . U 10 HOH 47 947 1814 HOH HOH A . U 10 HOH 48 948 1815 HOH HOH A . U 10 HOH 49 949 1816 HOH HOH A . U 10 HOH 50 950 1817 HOH HOH A . U 10 HOH 51 951 1818 HOH HOH A . U 10 HOH 52 952 1819 HOH HOH A . U 10 HOH 53 953 1821 HOH HOH A . U 10 HOH 54 954 1822 HOH HOH A . U 10 HOH 55 955 1823 HOH HOH A . U 10 HOH 56 956 1824 HOH HOH A . U 10 HOH 57 957 1825 HOH HOH A . U 10 HOH 58 958 1826 HOH HOH A . U 10 HOH 59 959 1827 HOH HOH A . U 10 HOH 60 960 1828 HOH HOH A . U 10 HOH 61 961 1829 HOH HOH A . U 10 HOH 62 962 1830 HOH HOH A . U 10 HOH 63 963 1831 HOH HOH A . U 10 HOH 64 964 1832 HOH HOH A . U 10 HOH 65 965 1833 HOH HOH A . U 10 HOH 66 966 1834 HOH HOH A . U 10 HOH 67 967 1835 HOH HOH A . U 10 HOH 68 968 1836 HOH HOH A . U 10 HOH 69 969 1837 HOH HOH A . U 10 HOH 70 970 1838 HOH HOH A . U 10 HOH 71 971 1839 HOH HOH A . U 10 HOH 72 972 1840 HOH HOH A . U 10 HOH 73 973 1841 HOH HOH A . U 10 HOH 74 974 1842 HOH HOH A . U 10 HOH 75 975 1843 HOH HOH A . U 10 HOH 76 976 1844 HOH HOH A . U 10 HOH 77 977 1845 HOH HOH A . U 10 HOH 78 978 1846 HOH HOH A . U 10 HOH 79 979 1847 HOH HOH A . U 10 HOH 80 980 1848 HOH HOH A . U 10 HOH 81 981 1849 HOH HOH A . U 10 HOH 82 982 1850 HOH HOH A . U 10 HOH 83 983 1851 HOH HOH A . U 10 HOH 84 984 1852 HOH HOH A . U 10 HOH 85 985 1853 HOH HOH A . U 10 HOH 86 986 1854 HOH HOH A . U 10 HOH 87 987 1855 HOH HOH A . U 10 HOH 88 988 1857 HOH HOH A . U 10 HOH 89 989 1858 HOH HOH A . U 10 HOH 90 990 1859 HOH HOH A . U 10 HOH 91 991 1860 HOH HOH A . U 10 HOH 92 992 1861 HOH HOH A . U 10 HOH 93 993 1862 HOH HOH A . U 10 HOH 94 994 1863 HOH HOH A . U 10 HOH 95 995 1864 HOH HOH A . U 10 HOH 96 996 1865 HOH HOH A . U 10 HOH 97 997 1866 HOH HOH A . U 10 HOH 98 998 1867 HOH HOH A . U 10 HOH 99 999 1868 HOH HOH A . U 10 HOH 100 1000 1869 HOH HOH A . U 10 HOH 101 1001 1870 HOH HOH A . U 10 HOH 102 1002 1871 HOH HOH A . U 10 HOH 103 1003 1872 HOH HOH A . U 10 HOH 104 1004 1873 HOH HOH A . U 10 HOH 105 1005 1874 HOH HOH A . U 10 HOH 106 1006 1875 HOH HOH A . U 10 HOH 107 1007 1876 HOH HOH A . U 10 HOH 108 1008 1877 HOH HOH A . U 10 HOH 109 1009 1878 HOH HOH A . U 10 HOH 110 1010 1879 HOH HOH A . U 10 HOH 111 1011 1880 HOH HOH A . U 10 HOH 112 1012 1881 HOH HOH A . U 10 HOH 113 1013 1882 HOH HOH A . U 10 HOH 114 1014 1883 HOH HOH A . U 10 HOH 115 1015 1884 HOH HOH A . U 10 HOH 116 1016 1885 HOH HOH A . U 10 HOH 117 1017 1886 HOH HOH A . U 10 HOH 118 1018 1887 HOH HOH A . U 10 HOH 119 1019 1888 HOH HOH A . U 10 HOH 120 1020 1889 HOH HOH A . U 10 HOH 121 1021 1890 HOH HOH A . U 10 HOH 122 1022 1891 HOH HOH A . U 10 HOH 123 1023 1892 HOH HOH A . U 10 HOH 124 1024 1893 HOH HOH A . U 10 HOH 125 1025 1894 HOH HOH A . U 10 HOH 126 1026 1895 HOH HOH A . U 10 HOH 127 1027 1896 HOH HOH A . U 10 HOH 128 1028 1897 HOH HOH A . U 10 HOH 129 1029 1898 HOH HOH A . U 10 HOH 130 1030 1899 HOH HOH A . U 10 HOH 131 1031 1900 HOH HOH A . U 10 HOH 132 1032 1901 HOH HOH A . U 10 HOH 133 1033 1902 HOH HOH A . U 10 HOH 134 1034 1903 HOH HOH A . U 10 HOH 135 1035 1904 HOH HOH A . U 10 HOH 136 1036 1905 HOH HOH A . U 10 HOH 137 1037 1906 HOH HOH A . U 10 HOH 138 1038 1907 HOH HOH A . U 10 HOH 139 1039 1908 HOH HOH A . U 10 HOH 140 1040 1909 HOH HOH A . U 10 HOH 141 1041 1910 HOH HOH A . U 10 HOH 142 1042 1911 HOH HOH A . U 10 HOH 143 1043 1912 HOH HOH A . U 10 HOH 144 1044 1913 HOH HOH A . U 10 HOH 145 1045 1914 HOH HOH A . U 10 HOH 146 1046 1915 HOH HOH A . U 10 HOH 147 1047 1916 HOH HOH A . U 10 HOH 148 1048 1917 HOH HOH A . U 10 HOH 149 1049 1918 HOH HOH A . U 10 HOH 150 1050 1919 HOH HOH A . U 10 HOH 151 1051 1920 HOH HOH A . U 10 HOH 152 1052 1921 HOH HOH A . U 10 HOH 153 1053 1922 HOH HOH A . U 10 HOH 154 1054 1923 HOH HOH A . U 10 HOH 155 1055 1924 HOH HOH A . U 10 HOH 156 1056 1925 HOH HOH A . U 10 HOH 157 1057 1926 HOH HOH A . U 10 HOH 158 1058 1927 HOH HOH A . U 10 HOH 159 1059 1928 HOH HOH A . U 10 HOH 160 1060 1929 HOH HOH A . U 10 HOH 161 1061 1930 HOH HOH A . U 10 HOH 162 1062 1931 HOH HOH A . U 10 HOH 163 1063 1932 HOH HOH A . U 10 HOH 164 1064 1933 HOH HOH A . U 10 HOH 165 1065 1934 HOH HOH A . U 10 HOH 166 1066 1935 HOH HOH A . U 10 HOH 167 1067 1936 HOH HOH A . U 10 HOH 168 1068 1937 HOH HOH A . U 10 HOH 169 1069 1938 HOH HOH A . U 10 HOH 170 1070 1939 HOH HOH A . U 10 HOH 171 1071 1940 HOH HOH A . U 10 HOH 172 1072 1941 HOH HOH A . U 10 HOH 173 1073 1942 HOH HOH A . U 10 HOH 174 1074 1943 HOH HOH A . U 10 HOH 175 1075 1944 HOH HOH A . U 10 HOH 176 1076 1945 HOH HOH A . U 10 HOH 177 1077 1946 HOH HOH A . U 10 HOH 178 1078 1947 HOH HOH A . U 10 HOH 179 1079 1948 HOH HOH A . U 10 HOH 180 1080 1949 HOH HOH A . U 10 HOH 181 1081 1950 HOH HOH A . U 10 HOH 182 1082 1951 HOH HOH A . U 10 HOH 183 1083 1952 HOH HOH A . U 10 HOH 184 1084 1953 HOH HOH A . U 10 HOH 185 1085 1954 HOH HOH A . U 10 HOH 186 1086 1955 HOH HOH A . U 10 HOH 187 1087 1956 HOH HOH A . U 10 HOH 188 1088 1957 HOH HOH A . U 10 HOH 189 1089 1958 HOH HOH A . U 10 HOH 190 1090 1959 HOH HOH A . U 10 HOH 191 1091 1960 HOH HOH A . U 10 HOH 192 1092 1961 HOH HOH A . U 10 HOH 193 1093 1962 HOH HOH A . U 10 HOH 194 1094 1963 HOH HOH A . U 10 HOH 195 1095 1964 HOH HOH A . U 10 HOH 196 1096 1965 HOH HOH A . U 10 HOH 197 1097 1966 HOH HOH A . U 10 HOH 198 1098 1967 HOH HOH A . U 10 HOH 199 1099 1968 HOH HOH A . U 10 HOH 200 1100 1969 HOH HOH A . U 10 HOH 201 1101 1970 HOH HOH A . U 10 HOH 202 1102 1971 HOH HOH A . U 10 HOH 203 1103 1972 HOH HOH A . U 10 HOH 204 1104 1973 HOH HOH A . U 10 HOH 205 1105 1974 HOH HOH A . U 10 HOH 206 1106 1975 HOH HOH A . U 10 HOH 207 1107 1976 HOH HOH A . U 10 HOH 208 1108 1977 HOH HOH A . U 10 HOH 209 1109 1978 HOH HOH A . U 10 HOH 210 1110 1979 HOH HOH A . U 10 HOH 211 1111 1980 HOH HOH A . U 10 HOH 212 1112 1981 HOH HOH A . U 10 HOH 213 1113 1982 HOH HOH A . U 10 HOH 214 1114 1983 HOH HOH A . U 10 HOH 215 1115 1984 HOH HOH A . U 10 HOH 216 1116 1985 HOH HOH A . U 10 HOH 217 1117 1986 HOH HOH A . U 10 HOH 218 1118 1987 HOH HOH A . U 10 HOH 219 1119 1989 HOH HOH A . U 10 HOH 220 1120 1990 HOH HOH A . U 10 HOH 221 1121 1991 HOH HOH A . U 10 HOH 222 1122 1992 HOH HOH A . U 10 HOH 223 1123 1993 HOH HOH A . U 10 HOH 224 1124 1994 HOH HOH A . U 10 HOH 225 1125 1995 HOH HOH A . U 10 HOH 226 1126 1996 HOH HOH A . U 10 HOH 227 1127 1997 HOH HOH A . U 10 HOH 228 1128 1998 HOH HOH A . U 10 HOH 229 1129 1999 HOH HOH A . U 10 HOH 230 1130 2000 HOH HOH A . U 10 HOH 231 1131 2001 HOH HOH A . U 10 HOH 232 1132 2002 HOH HOH A . U 10 HOH 233 1133 2003 HOH HOH A . U 10 HOH 234 1134 2004 HOH HOH A . U 10 HOH 235 1135 2005 HOH HOH A . U 10 HOH 236 1136 2006 HOH HOH A . U 10 HOH 237 1137 2007 HOH HOH A . U 10 HOH 238 1138 2008 HOH HOH A . U 10 HOH 239 1139 2009 HOH HOH A . U 10 HOH 240 1140 2010 HOH HOH A . U 10 HOH 241 1141 2011 HOH HOH A . U 10 HOH 242 1142 2012 HOH HOH A . U 10 HOH 243 1143 2013 HOH HOH A . U 10 HOH 244 1144 2014 HOH HOH A . U 10 HOH 245 1145 2015 HOH HOH A . U 10 HOH 246 1146 2016 HOH HOH A . U 10 HOH 247 1147 2017 HOH HOH A . U 10 HOH 248 1148 2018 HOH HOH A . U 10 HOH 249 1149 2019 HOH HOH A . U 10 HOH 250 1150 2020 HOH HOH A . U 10 HOH 251 1151 2021 HOH HOH A . U 10 HOH 252 1152 2022 HOH HOH A . U 10 HOH 253 1153 2023 HOH HOH A . U 10 HOH 254 1154 2025 HOH HOH A . U 10 HOH 255 1155 2026 HOH HOH A . U 10 HOH 256 1156 2027 HOH HOH A . U 10 HOH 257 1157 2028 HOH HOH A . U 10 HOH 258 1158 2029 HOH HOH A . U 10 HOH 259 1159 2030 HOH HOH A . U 10 HOH 260 1160 2031 HOH HOH A . U 10 HOH 261 1161 2032 HOH HOH A . U 10 HOH 262 1162 2033 HOH HOH A . U 10 HOH 263 1163 2034 HOH HOH A . U 10 HOH 264 1164 2035 HOH HOH A . U 10 HOH 265 1165 2036 HOH HOH A . U 10 HOH 266 1166 2038 HOH HOH A . U 10 HOH 267 1167 2039 HOH HOH A . U 10 HOH 268 1168 2040 HOH HOH A . U 10 HOH 269 1169 2041 HOH HOH A . U 10 HOH 270 1170 2043 HOH HOH A . U 10 HOH 271 1171 2044 HOH HOH A . U 10 HOH 272 1172 2045 HOH HOH A . U 10 HOH 273 1173 2046 HOH HOH A . U 10 HOH 274 1174 2047 HOH HOH A . U 10 HOH 275 1175 2048 HOH HOH A . U 10 HOH 276 1176 2049 HOH HOH A . U 10 HOH 277 1177 2050 HOH HOH A . U 10 HOH 278 1178 2051 HOH HOH A . U 10 HOH 279 1179 2052 HOH HOH A . U 10 HOH 280 1180 2053 HOH HOH A . U 10 HOH 281 1181 2054 HOH HOH A . U 10 HOH 282 1182 2055 HOH HOH A . U 10 HOH 283 1183 2056 HOH HOH A . U 10 HOH 284 1184 2057 HOH HOH A . U 10 HOH 285 1185 2059 HOH HOH A . U 10 HOH 286 1186 2060 HOH HOH A . U 10 HOH 287 1187 2061 HOH HOH A . U 10 HOH 288 1188 2062 HOH HOH A . U 10 HOH 289 1189 2063 HOH HOH A . U 10 HOH 290 1190 2064 HOH HOH A . U 10 HOH 291 1191 2065 HOH HOH A . U 10 HOH 292 1192 2066 HOH HOH A . U 10 HOH 293 1193 2067 HOH HOH A . U 10 HOH 294 1194 2068 HOH HOH A . U 10 HOH 295 1195 2069 HOH HOH A . U 10 HOH 296 1196 2071 HOH HOH A . U 10 HOH 297 1197 2072 HOH HOH A . U 10 HOH 298 1198 2073 HOH HOH A . U 10 HOH 299 1199 2074 HOH HOH A . U 10 HOH 300 1200 2075 HOH HOH A . U 10 HOH 301 1201 2076 HOH HOH A . U 10 HOH 302 1202 2077 HOH HOH A . U 10 HOH 303 1203 2078 HOH HOH A . U 10 HOH 304 1204 2079 HOH HOH A . U 10 HOH 305 1205 2081 HOH HOH A . U 10 HOH 306 1206 2082 HOH HOH A . U 10 HOH 307 1207 2083 HOH HOH A . U 10 HOH 308 1208 2084 HOH HOH A . U 10 HOH 309 1209 2086 HOH HOH A . U 10 HOH 310 1210 2087 HOH HOH A . U 10 HOH 311 1211 2088 HOH HOH A . U 10 HOH 312 1212 2090 HOH HOH A . U 10 HOH 313 1213 2091 HOH HOH A . U 10 HOH 314 1214 2092 HOH HOH A . U 10 HOH 315 1215 2093 HOH HOH A . U 10 HOH 316 1216 2094 HOH HOH A . U 10 HOH 317 1217 2095 HOH HOH A . U 10 HOH 318 1218 2096 HOH HOH A . U 10 HOH 319 1219 2097 HOH HOH A . U 10 HOH 320 1220 2098 HOH HOH A . U 10 HOH 321 1221 2100 HOH HOH A . U 10 HOH 322 1222 2101 HOH HOH A . U 10 HOH 323 1223 2102 HOH HOH A . U 10 HOH 324 1224 2103 HOH HOH A . U 10 HOH 325 1225 2104 HOH HOH A . U 10 HOH 326 1226 2105 HOH HOH A . U 10 HOH 327 1227 2106 HOH HOH A . U 10 HOH 328 1228 2107 HOH HOH A . U 10 HOH 329 1229 2108 HOH HOH A . U 10 HOH 330 1230 2109 HOH HOH A . U 10 HOH 331 1231 2110 HOH HOH A . U 10 HOH 332 1232 2111 HOH HOH A . U 10 HOH 333 1233 2112 HOH HOH A . U 10 HOH 334 1234 2113 HOH HOH A . U 10 HOH 335 1235 2115 HOH HOH A . U 10 HOH 336 1236 2116 HOH HOH A . U 10 HOH 337 1237 2117 HOH HOH A . U 10 HOH 338 1238 2119 HOH HOH A . U 10 HOH 339 1239 2120 HOH HOH A . U 10 HOH 340 1240 2122 HOH HOH A . U 10 HOH 341 1241 2124 HOH HOH A . U 10 HOH 342 1242 2125 HOH HOH A . U 10 HOH 343 1243 2126 HOH HOH A . U 10 HOH 344 1244 2127 HOH HOH A . U 10 HOH 345 1245 2128 HOH HOH A . U 10 HOH 346 1246 2129 HOH HOH A . U 10 HOH 347 1247 2130 HOH HOH A . U 10 HOH 348 1248 2131 HOH HOH A . U 10 HOH 349 1249 2132 HOH HOH A . U 10 HOH 350 1250 2133 HOH HOH A . U 10 HOH 351 1251 2134 HOH HOH A . U 10 HOH 352 1252 2135 HOH HOH A . U 10 HOH 353 1253 2136 HOH HOH A . U 10 HOH 354 1254 2137 HOH HOH A . U 10 HOH 355 1255 2138 HOH HOH A . U 10 HOH 356 1256 2139 HOH HOH A . U 10 HOH 357 1257 2140 HOH HOH A . U 10 HOH 358 1258 2142 HOH HOH A . U 10 HOH 359 1259 2143 HOH HOH A . U 10 HOH 360 1260 2144 HOH HOH A . U 10 HOH 361 1261 2145 HOH HOH A . U 10 HOH 362 1262 2146 HOH HOH A . U 10 HOH 363 1263 2147 HOH HOH A . U 10 HOH 364 1264 2148 HOH HOH A . U 10 HOH 365 1265 2149 HOH HOH A . U 10 HOH 366 1266 2150 HOH HOH A . U 10 HOH 367 1267 2152 HOH HOH A . U 10 HOH 368 1268 2154 HOH HOH A . U 10 HOH 369 1269 2155 HOH HOH A . U 10 HOH 370 1270 2156 HOH HOH A . U 10 HOH 371 1271 2157 HOH HOH A . U 10 HOH 372 1272 2158 HOH HOH A . U 10 HOH 373 1273 2160 HOH HOH A . U 10 HOH 374 1274 2161 HOH HOH A . U 10 HOH 375 1275 2162 HOH HOH A . U 10 HOH 376 1276 2163 HOH HOH A . U 10 HOH 377 1277 2164 HOH HOH A . U 10 HOH 378 1278 2165 HOH HOH A . U 10 HOH 379 1279 2169 HOH HOH A . U 10 HOH 380 1280 2171 HOH HOH A . U 10 HOH 381 1281 2172 HOH HOH A . U 10 HOH 382 1282 2173 HOH HOH A . U 10 HOH 383 1283 2174 HOH HOH A . U 10 HOH 384 1284 2178 HOH HOH A . U 10 HOH 385 1285 2179 HOH HOH A . U 10 HOH 386 1286 2180 HOH HOH A . U 10 HOH 387 1287 2182 HOH HOH A . U 10 HOH 388 1288 2183 HOH HOH A . U 10 HOH 389 1289 2184 HOH HOH A . U 10 HOH 390 1290 2185 HOH HOH A . U 10 HOH 391 1291 2186 HOH HOH A . U 10 HOH 392 1292 2187 HOH HOH A . U 10 HOH 393 1293 2188 HOH HOH A . U 10 HOH 394 1294 2189 HOH HOH A . U 10 HOH 395 1295 2190 HOH HOH A . U 10 HOH 396 1296 2191 HOH HOH A . U 10 HOH 397 1297 2193 HOH HOH A . U 10 HOH 398 1298 2194 HOH HOH A . U 10 HOH 399 1299 2195 HOH HOH A . U 10 HOH 400 1300 2197 HOH HOH A . U 10 HOH 401 1301 2198 HOH HOH A . U 10 HOH 402 1302 2199 HOH HOH A . U 10 HOH 403 1303 2200 HOH HOH A . U 10 HOH 404 1304 2201 HOH HOH A . U 10 HOH 405 1305 2202 HOH HOH A . U 10 HOH 406 1306 2203 HOH HOH A . U 10 HOH 407 1307 2204 HOH HOH A . U 10 HOH 408 1308 2205 HOH HOH A . U 10 HOH 409 1309 2206 HOH HOH A . U 10 HOH 410 1310 2207 HOH HOH A . U 10 HOH 411 1311 2208 HOH HOH A . U 10 HOH 412 1312 2209 HOH HOH A . U 10 HOH 413 1313 2211 HOH HOH A . U 10 HOH 414 1314 2212 HOH HOH A . U 10 HOH 415 1315 2213 HOH HOH A . U 10 HOH 416 1316 2214 HOH HOH A . U 10 HOH 417 1317 2216 HOH HOH A . U 10 HOH 418 1318 2217 HOH HOH A . U 10 HOH 419 1319 2219 HOH HOH A . U 10 HOH 420 1320 2220 HOH HOH A . U 10 HOH 421 1321 2221 HOH HOH A . U 10 HOH 422 1322 2222 HOH HOH A . U 10 HOH 423 1323 2223 HOH HOH A . U 10 HOH 424 1324 2224 HOH HOH A . U 10 HOH 425 1325 2225 HOH HOH A . U 10 HOH 426 1326 2227 HOH HOH A . U 10 HOH 427 1327 2228 HOH HOH A . U 10 HOH 428 1328 2229 HOH HOH A . U 10 HOH 429 1329 2230 HOH HOH A . U 10 HOH 430 1330 2231 HOH HOH A . U 10 HOH 431 1331 2233 HOH HOH A . U 10 HOH 432 1332 2234 HOH HOH A . U 10 HOH 433 1333 2235 HOH HOH A . U 10 HOH 434 1334 2237 HOH HOH A . U 10 HOH 435 1335 2239 HOH HOH A . U 10 HOH 436 1336 2241 HOH HOH A . U 10 HOH 437 1337 2242 HOH HOH A . U 10 HOH 438 1338 2243 HOH HOH A . U 10 HOH 439 1339 2245 HOH HOH A . U 10 HOH 440 1340 2246 HOH HOH A . U 10 HOH 441 1341 2247 HOH HOH A . U 10 HOH 442 1342 2248 HOH HOH A . U 10 HOH 443 1343 2250 HOH HOH A . U 10 HOH 444 1344 2251 HOH HOH A . U 10 HOH 445 1345 2252 HOH HOH A . U 10 HOH 446 1346 2253 HOH HOH A . U 10 HOH 447 1347 2254 HOH HOH A . U 10 HOH 448 1348 2257 HOH HOH A . U 10 HOH 449 1349 2258 HOH HOH A . U 10 HOH 450 1350 2259 HOH HOH A . U 10 HOH 451 1351 2260 HOH HOH A . U 10 HOH 452 1352 2261 HOH HOH A . U 10 HOH 453 1353 2262 HOH HOH A . U 10 HOH 454 1354 2263 HOH HOH A . U 10 HOH 455 1355 2264 HOH HOH A . U 10 HOH 456 1356 2265 HOH HOH A . U 10 HOH 457 1357 2266 HOH HOH A . U 10 HOH 458 1358 2267 HOH HOH A . U 10 HOH 459 1359 2268 HOH HOH A . U 10 HOH 460 1360 2269 HOH HOH A . U 10 HOH 461 1361 2270 HOH HOH A . U 10 HOH 462 1362 2272 HOH HOH A . U 10 HOH 463 1363 2273 HOH HOH A . U 10 HOH 464 1364 2274 HOH HOH A . U 10 HOH 465 1365 2276 HOH HOH A . U 10 HOH 466 1366 2277 HOH HOH A . U 10 HOH 467 1367 2278 HOH HOH A . U 10 HOH 468 1368 2279 HOH HOH A . U 10 HOH 469 1369 2280 HOH HOH A . U 10 HOH 470 1370 2281 HOH HOH A . U 10 HOH 471 1371 2282 HOH HOH A . U 10 HOH 472 1372 2283 HOH HOH A . U 10 HOH 473 1373 2284 HOH HOH A . U 10 HOH 474 1374 2285 HOH HOH A . U 10 HOH 475 1375 2286 HOH HOH A . U 10 HOH 476 1376 2289 HOH HOH A . U 10 HOH 477 1377 2291 HOH HOH A . U 10 HOH 478 1378 2292 HOH HOH A . U 10 HOH 479 1379 2293 HOH HOH A . U 10 HOH 480 1380 2295 HOH HOH A . U 10 HOH 481 1381 2296 HOH HOH A . U 10 HOH 482 1382 2297 HOH HOH A . U 10 HOH 483 1383 2298 HOH HOH A . U 10 HOH 484 1384 2299 HOH HOH A . U 10 HOH 485 1385 2301 HOH HOH A . U 10 HOH 486 1386 2303 HOH HOH A . U 10 HOH 487 1387 2305 HOH HOH A . U 10 HOH 488 1388 2307 HOH HOH A . U 10 HOH 489 1389 2308 HOH HOH A . U 10 HOH 490 1390 2310 HOH HOH A . U 10 HOH 491 1391 2311 HOH HOH A . U 10 HOH 492 1392 2312 HOH HOH A . U 10 HOH 493 1393 2315 HOH HOH A . U 10 HOH 494 1394 2316 HOH HOH A . U 10 HOH 495 1395 2317 HOH HOH A . U 10 HOH 496 1396 2318 HOH HOH A . U 10 HOH 497 1397 2319 HOH HOH A . U 10 HOH 498 1398 2320 HOH HOH A . U 10 HOH 499 1399 2321 HOH HOH A . U 10 HOH 500 1400 2322 HOH HOH A . U 10 HOH 501 1401 2323 HOH HOH A . U 10 HOH 502 1402 2329 HOH HOH A . U 10 HOH 503 1403 2330 HOH HOH A . U 10 HOH 504 1404 2332 HOH HOH A . U 10 HOH 505 1405 2333 HOH HOH A . U 10 HOH 506 1406 2334 HOH HOH A . U 10 HOH 507 1407 2339 HOH HOH A . U 10 HOH 508 1408 2340 HOH HOH A . U 10 HOH 509 1409 2341 HOH HOH A . U 10 HOH 510 1410 2345 HOH HOH A . U 10 HOH 511 1411 2346 HOH HOH A . U 10 HOH 512 1412 2348 HOH HOH A . U 10 HOH 513 1413 2349 HOH HOH A . U 10 HOH 514 1414 2350 HOH HOH A . U 10 HOH 515 1415 2351 HOH HOH A . U 10 HOH 516 1416 2352 HOH HOH A . U 10 HOH 517 1417 2353 HOH HOH A . U 10 HOH 518 1418 2354 HOH HOH A . U 10 HOH 519 1419 2356 HOH HOH A . U 10 HOH 520 1420 2357 HOH HOH A . U 10 HOH 521 1421 2359 HOH HOH A . U 10 HOH 522 1422 2360 HOH HOH A . U 10 HOH 523 1423 2362 HOH HOH A . U 10 HOH 524 1424 2363 HOH HOH A . U 10 HOH 525 1425 2365 HOH HOH A . U 10 HOH 526 1426 2366 HOH HOH A . U 10 HOH 527 1427 2371 HOH HOH A . U 10 HOH 528 1428 2373 HOH HOH A . U 10 HOH 529 1429 2378 HOH HOH A . U 10 HOH 530 1430 2381 HOH HOH A . U 10 HOH 531 1431 2385 HOH HOH A . U 10 HOH 532 1432 2386 HOH HOH A . U 10 HOH 533 1433 2387 HOH HOH A . U 10 HOH 534 1434 2388 HOH HOH A . U 10 HOH 535 1435 2392 HOH HOH A . U 10 HOH 536 1436 2393 HOH HOH A . U 10 HOH 537 1437 2394 HOH HOH A . U 10 HOH 538 1438 2396 HOH HOH A . U 10 HOH 539 1439 2399 HOH HOH A . U 10 HOH 540 1440 2400 HOH HOH A . U 10 HOH 541 1441 2402 HOH HOH A . U 10 HOH 542 1442 2403 HOH HOH A . U 10 HOH 543 1443 2406 HOH HOH A . U 10 HOH 544 1444 2407 HOH HOH A . U 10 HOH 545 1445 2409 HOH HOH A . U 10 HOH 546 1446 2410 HOH HOH A . U 10 HOH 547 1447 2413 HOH HOH A . U 10 HOH 548 1448 2415 HOH HOH A . U 10 HOH 549 1449 2416 HOH HOH A . U 10 HOH 550 1450 2417 HOH HOH A . U 10 HOH 551 1451 2418 HOH HOH A . U 10 HOH 552 1452 2421 HOH HOH A . U 10 HOH 553 1453 2430 HOH HOH A . U 10 HOH 554 1454 2431 HOH HOH A . U 10 HOH 555 1455 2432 HOH HOH A . U 10 HOH 556 1456 2433 HOH HOH A . U 10 HOH 557 1457 2434 HOH HOH A . U 10 HOH 558 1458 2435 HOH HOH A . U 10 HOH 559 1459 2436 HOH HOH A . U 10 HOH 560 1460 2437 HOH HOH A . U 10 HOH 561 1461 2438 HOH HOH A . U 10 HOH 562 1462 2439 HOH HOH A . U 10 HOH 563 1463 2440 HOH HOH A . U 10 HOH 564 1464 2441 HOH HOH A . U 10 HOH 565 1465 2442 HOH HOH A . U 10 HOH 566 1466 2443 HOH HOH A . U 10 HOH 567 1467 2444 HOH HOH A . U 10 HOH 568 1468 2445 HOH HOH A . U 10 HOH 569 1469 2446 HOH HOH A . U 10 HOH 570 1470 2447 HOH HOH A . U 10 HOH 571 1471 2448 HOH HOH A . U 10 HOH 572 1472 2449 HOH HOH A . U 10 HOH 573 1473 2450 HOH HOH A . U 10 HOH 574 1474 2451 HOH HOH A . U 10 HOH 575 1475 2452 HOH HOH A . U 10 HOH 576 1476 2453 HOH HOH A . U 10 HOH 577 1477 2454 HOH HOH A . U 10 HOH 578 1478 2455 HOH HOH A . U 10 HOH 579 1479 2456 HOH HOH A . U 10 HOH 580 1480 2457 HOH HOH A . U 10 HOH 581 1481 2458 HOH HOH A . U 10 HOH 582 1482 2459 HOH HOH A . U 10 HOH 583 1483 2464 HOH HOH A . U 10 HOH 584 1484 2465 HOH HOH A . #