data_4MCR # _entry.id 4MCR # _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 4MCR RCSB RCSB081747 WWPDB D_1000081747 # 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 4MCS . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MCR _pdbx_database_status.recvd_initial_deposition_date 2013-08-21 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Navratil, M.' 1 'Barinka, C.' 2 'Lubkowski, J.' 3 # _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 4MCR _cell.length_a 101.491 _cell.length_b 129.830 _cell.length_c 158.811 _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 4MCR _symmetry.space_group_name_H-M 'I 2 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 23 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Glutamate carboxypeptidase 2' 84972.914 1 3.4.17.21 E424A 'Glutamate carboxypeptidase II, unp residues 44-750' ? 2 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 3 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 4 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 11 ? ? ? ? 6 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 7 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 8 non-polymer syn ;N-(4-{[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-gamma-glutamyl-L-gamma-glutamyl-L-gamma-glutamyl-L-glutamic acid ; 828.739 1 ? ? ? ? 9 water nat water 18.015 610 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ;Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Membrane glutamate carboxypeptidase, mGCP, N-acetylated-alpha-linked acidic dipeptidase I, NAALADase I, Prostate-specific membrane antigen, PSM, PSMA, Pteroylpoly-gamma-glutamate carboxypeptidase ; # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;MKLCILLAVVAFVGLSLGRSGLNDIFEAQKIEWHEGSGSGSENLYFQGRSKSSNEATNITPKHNMKAFLDELKAENIKKF LYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYEN VSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPAD YFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSA PPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAA VVHEIVRSFGTLKKEGWRPRRTILFASWDAAEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSL VHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYH SVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLF SAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALF DIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_seq_one_letter_code_can ;MKLCILLAVVAFVGLSLGRSGLNDIFEAQKIEWHEGSGSGSENLYFQGRSKSSNEATNITPKHNMKAFLDELKAENIKKF LYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYEN VSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPAD YFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSA PPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAA VVHEIVRSFGTLKKEGWRPRRTILFASWDAAEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSL VHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYH SVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLF SAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALF DIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 MET n 1 2 LYS n 1 3 LEU n 1 4 CYS n 1 5 ILE n 1 6 LEU n 1 7 LEU n 1 8 ALA n 1 9 VAL n 1 10 VAL n 1 11 ALA n 1 12 PHE n 1 13 VAL n 1 14 GLY n 1 15 LEU n 1 16 SER n 1 17 LEU n 1 18 GLY n 1 19 ARG n 1 20 SER n 1 21 GLY n 1 22 LEU n 1 23 ASN n 1 24 ASP n 1 25 ILE n 1 26 PHE n 1 27 GLU n 1 28 ALA n 1 29 GLN n 1 30 LYS n 1 31 ILE n 1 32 GLU n 1 33 TRP n 1 34 HIS n 1 35 GLU n 1 36 GLY n 1 37 SER n 1 38 GLY n 1 39 SER n 1 40 GLY n 1 41 SER n 1 42 GLU n 1 43 ASN n 1 44 LEU n 1 45 TYR n 1 46 PHE n 1 47 GLN n 1 48 GLY n 1 49 ARG n 1 50 SER n 1 51 LYS n 1 52 SER n 1 53 SER n 1 54 ASN n 1 55 GLU n 1 56 ALA n 1 57 THR n 1 58 ASN n 1 59 ILE n 1 60 THR n 1 61 PRO n 1 62 LYS n 1 63 HIS n 1 64 ASN n 1 65 MET n 1 66 LYS n 1 67 ALA n 1 68 PHE n 1 69 LEU n 1 70 ASP n 1 71 GLU n 1 72 LEU n 1 73 LYS n 1 74 ALA n 1 75 GLU n 1 76 ASN n 1 77 ILE n 1 78 LYS n 1 79 LYS n 1 80 PHE n 1 81 LEU n 1 82 TYR n 1 83 ASN n 1 84 PHE n 1 85 THR n 1 86 GLN n 1 87 ILE n 1 88 PRO n 1 89 HIS n 1 90 LEU n 1 91 ALA n 1 92 GLY n 1 93 THR n 1 94 GLU n 1 95 GLN n 1 96 ASN n 1 97 PHE n 1 98 GLN n 1 99 LEU n 1 100 ALA n 1 101 LYS n 1 102 GLN n 1 103 ILE n 1 104 GLN n 1 105 SER n 1 106 GLN n 1 107 TRP n 1 108 LYS n 1 109 GLU n 1 110 PHE n 1 111 GLY n 1 112 LEU n 1 113 ASP n 1 114 SER n 1 115 VAL n 1 116 GLU n 1 117 LEU n 1 118 ALA n 1 119 HIS n 1 120 TYR n 1 121 ASP n 1 122 VAL n 1 123 LEU n 1 124 LEU n 1 125 SER n 1 126 TYR n 1 127 PRO n 1 128 ASN n 1 129 LYS n 1 130 THR n 1 131 HIS n 1 132 PRO n 1 133 ASN n 1 134 TYR n 1 135 ILE n 1 136 SER n 1 137 ILE n 1 138 ILE n 1 139 ASN n 1 140 GLU n 1 141 ASP n 1 142 GLY n 1 143 ASN n 1 144 GLU n 1 145 ILE n 1 146 PHE n 1 147 ASN n 1 148 THR n 1 149 SER n 1 150 LEU n 1 151 PHE n 1 152 GLU n 1 153 PRO n 1 154 PRO n 1 155 PRO n 1 156 PRO n 1 157 GLY n 1 158 TYR n 1 159 GLU n 1 160 ASN n 1 161 VAL n 1 162 SER n 1 163 ASP n 1 164 ILE n 1 165 VAL n 1 166 PRO n 1 167 PRO n 1 168 PHE n 1 169 SER n 1 170 ALA n 1 171 PHE n 1 172 SER n 1 173 PRO n 1 174 GLN n 1 175 GLY n 1 176 MET n 1 177 PRO n 1 178 GLU n 1 179 GLY n 1 180 ASP n 1 181 LEU n 1 182 VAL n 1 183 TYR n 1 184 VAL n 1 185 ASN n 1 186 TYR n 1 187 ALA n 1 188 ARG n 1 189 THR n 1 190 GLU n 1 191 ASP n 1 192 PHE n 1 193 PHE n 1 194 LYS n 1 195 LEU n 1 196 GLU n 1 197 ARG n 1 198 ASP n 1 199 MET n 1 200 LYS n 1 201 ILE n 1 202 ASN n 1 203 CYS n 1 204 SER n 1 205 GLY n 1 206 LYS n 1 207 ILE n 1 208 VAL n 1 209 ILE n 1 210 ALA n 1 211 ARG n 1 212 TYR n 1 213 GLY n 1 214 LYS n 1 215 VAL n 1 216 PHE n 1 217 ARG n 1 218 GLY n 1 219 ASN n 1 220 LYS n 1 221 VAL n 1 222 LYS n 1 223 ASN n 1 224 ALA n 1 225 GLN n 1 226 LEU n 1 227 ALA n 1 228 GLY n 1 229 ALA n 1 230 LYS n 1 231 GLY n 1 232 VAL n 1 233 ILE n 1 234 LEU n 1 235 TYR n 1 236 SER n 1 237 ASP n 1 238 PRO n 1 239 ALA n 1 240 ASP n 1 241 TYR n 1 242 PHE n 1 243 ALA n 1 244 PRO n 1 245 GLY n 1 246 VAL n 1 247 LYS n 1 248 SER n 1 249 TYR n 1 250 PRO n 1 251 ASP n 1 252 GLY n 1 253 TRP n 1 254 ASN n 1 255 LEU n 1 256 PRO n 1 257 GLY n 1 258 GLY n 1 259 GLY n 1 260 VAL n 1 261 GLN n 1 262 ARG n 1 263 GLY n 1 264 ASN n 1 265 ILE n 1 266 LEU n 1 267 ASN n 1 268 LEU n 1 269 ASN n 1 270 GLY n 1 271 ALA n 1 272 GLY n 1 273 ASP n 1 274 PRO n 1 275 LEU n 1 276 THR n 1 277 PRO n 1 278 GLY n 1 279 TYR n 1 280 PRO n 1 281 ALA n 1 282 ASN n 1 283 GLU n 1 284 TYR n 1 285 ALA n 1 286 TYR n 1 287 ARG n 1 288 ARG n 1 289 GLY n 1 290 ILE n 1 291 ALA n 1 292 GLU n 1 293 ALA n 1 294 VAL n 1 295 GLY n 1 296 LEU n 1 297 PRO n 1 298 SER n 1 299 ILE n 1 300 PRO n 1 301 VAL n 1 302 HIS n 1 303 PRO n 1 304 ILE n 1 305 GLY n 1 306 TYR n 1 307 TYR n 1 308 ASP n 1 309 ALA n 1 310 GLN n 1 311 LYS n 1 312 LEU n 1 313 LEU n 1 314 GLU n 1 315 LYS n 1 316 MET n 1 317 GLY n 1 318 GLY n 1 319 SER n 1 320 ALA n 1 321 PRO n 1 322 PRO n 1 323 ASP n 1 324 SER n 1 325 SER n 1 326 TRP n 1 327 ARG n 1 328 GLY n 1 329 SER n 1 330 LEU n 1 331 LYS n 1 332 VAL n 1 333 PRO n 1 334 TYR n 1 335 ASN n 1 336 VAL n 1 337 GLY n 1 338 PRO n 1 339 GLY n 1 340 PHE n 1 341 THR n 1 342 GLY n 1 343 ASN n 1 344 PHE n 1 345 SER n 1 346 THR n 1 347 GLN n 1 348 LYS n 1 349 VAL n 1 350 LYS n 1 351 MET n 1 352 HIS n 1 353 ILE n 1 354 HIS n 1 355 SER n 1 356 THR n 1 357 ASN n 1 358 GLU n 1 359 VAL n 1 360 THR n 1 361 ARG n 1 362 ILE n 1 363 TYR n 1 364 ASN n 1 365 VAL n 1 366 ILE n 1 367 GLY n 1 368 THR n 1 369 LEU n 1 370 ARG n 1 371 GLY n 1 372 ALA n 1 373 VAL n 1 374 GLU n 1 375 PRO n 1 376 ASP n 1 377 ARG n 1 378 TYR n 1 379 VAL n 1 380 ILE n 1 381 LEU n 1 382 GLY n 1 383 GLY n 1 384 HIS n 1 385 ARG n 1 386 ASP n 1 387 SER n 1 388 TRP n 1 389 VAL n 1 390 PHE n 1 391 GLY n 1 392 GLY n 1 393 ILE n 1 394 ASP n 1 395 PRO n 1 396 GLN n 1 397 SER n 1 398 GLY n 1 399 ALA n 1 400 ALA n 1 401 VAL n 1 402 VAL n 1 403 HIS n 1 404 GLU n 1 405 ILE n 1 406 VAL n 1 407 ARG n 1 408 SER n 1 409 PHE n 1 410 GLY n 1 411 THR n 1 412 LEU n 1 413 LYS n 1 414 LYS n 1 415 GLU n 1 416 GLY n 1 417 TRP n 1 418 ARG n 1 419 PRO n 1 420 ARG n 1 421 ARG n 1 422 THR n 1 423 ILE n 1 424 LEU n 1 425 PHE n 1 426 ALA n 1 427 SER n 1 428 TRP n 1 429 ASP n 1 430 ALA n 1 431 ALA n 1 432 GLU n 1 433 PHE n 1 434 GLY n 1 435 LEU n 1 436 LEU n 1 437 GLY n 1 438 SER n 1 439 THR n 1 440 GLU n 1 441 TRP n 1 442 ALA n 1 443 GLU n 1 444 GLU n 1 445 ASN n 1 446 SER n 1 447 ARG n 1 448 LEU n 1 449 LEU n 1 450 GLN n 1 451 GLU n 1 452 ARG n 1 453 GLY n 1 454 VAL n 1 455 ALA n 1 456 TYR n 1 457 ILE n 1 458 ASN n 1 459 ALA n 1 460 ASP n 1 461 SER n 1 462 SER n 1 463 ILE n 1 464 GLU n 1 465 GLY n 1 466 ASN n 1 467 TYR n 1 468 THR n 1 469 LEU n 1 470 ARG n 1 471 VAL n 1 472 ASP n 1 473 CYS n 1 474 THR n 1 475 PRO n 1 476 LEU n 1 477 MET n 1 478 TYR n 1 479 SER n 1 480 LEU n 1 481 VAL n 1 482 HIS n 1 483 ASN n 1 484 LEU n 1 485 THR n 1 486 LYS n 1 487 GLU n 1 488 LEU n 1 489 LYS n 1 490 SER n 1 491 PRO n 1 492 ASP n 1 493 GLU n 1 494 GLY n 1 495 PHE n 1 496 GLU n 1 497 GLY n 1 498 LYS n 1 499 SER n 1 500 LEU n 1 501 TYR n 1 502 GLU n 1 503 SER n 1 504 TRP n 1 505 THR n 1 506 LYS n 1 507 LYS n 1 508 SER n 1 509 PRO n 1 510 SER n 1 511 PRO n 1 512 GLU n 1 513 PHE n 1 514 SER n 1 515 GLY n 1 516 MET n 1 517 PRO n 1 518 ARG n 1 519 ILE n 1 520 SER n 1 521 LYS n 1 522 LEU n 1 523 GLY n 1 524 SER n 1 525 GLY n 1 526 ASN n 1 527 ASP n 1 528 PHE n 1 529 GLU n 1 530 VAL n 1 531 PHE n 1 532 PHE n 1 533 GLN n 1 534 ARG n 1 535 LEU n 1 536 GLY n 1 537 ILE n 1 538 ALA n 1 539 SER n 1 540 GLY n 1 541 ARG n 1 542 ALA n 1 543 ARG n 1 544 TYR n 1 545 THR n 1 546 LYS n 1 547 ASN n 1 548 TRP n 1 549 GLU n 1 550 THR n 1 551 ASN n 1 552 LYS n 1 553 PHE n 1 554 SER n 1 555 GLY n 1 556 TYR n 1 557 PRO n 1 558 LEU n 1 559 TYR n 1 560 HIS n 1 561 SER n 1 562 VAL n 1 563 TYR n 1 564 GLU n 1 565 THR n 1 566 TYR n 1 567 GLU n 1 568 LEU n 1 569 VAL n 1 570 GLU n 1 571 LYS n 1 572 PHE n 1 573 TYR n 1 574 ASP n 1 575 PRO n 1 576 MET n 1 577 PHE n 1 578 LYS n 1 579 TYR n 1 580 HIS n 1 581 LEU n 1 582 THR n 1 583 VAL n 1 584 ALA n 1 585 GLN n 1 586 VAL n 1 587 ARG n 1 588 GLY n 1 589 GLY n 1 590 MET n 1 591 VAL n 1 592 PHE n 1 593 GLU n 1 594 LEU n 1 595 ALA n 1 596 ASN n 1 597 SER n 1 598 ILE n 1 599 VAL n 1 600 LEU n 1 601 PRO n 1 602 PHE n 1 603 ASP n 1 604 CYS n 1 605 ARG n 1 606 ASP n 1 607 TYR n 1 608 ALA n 1 609 VAL n 1 610 VAL n 1 611 LEU n 1 612 ARG n 1 613 LYS n 1 614 TYR n 1 615 ALA n 1 616 ASP n 1 617 LYS n 1 618 ILE n 1 619 TYR n 1 620 SER n 1 621 ILE n 1 622 SER n 1 623 MET n 1 624 LYS n 1 625 HIS n 1 626 PRO n 1 627 GLN n 1 628 GLU n 1 629 MET n 1 630 LYS n 1 631 THR n 1 632 TYR n 1 633 SER n 1 634 VAL n 1 635 SER n 1 636 PHE n 1 637 ASP n 1 638 SER n 1 639 LEU n 1 640 PHE n 1 641 SER n 1 642 ALA n 1 643 VAL n 1 644 LYS n 1 645 ASN n 1 646 PHE n 1 647 THR n 1 648 GLU n 1 649 ILE n 1 650 ALA n 1 651 SER n 1 652 LYS n 1 653 PHE n 1 654 SER n 1 655 GLU n 1 656 ARG n 1 657 LEU n 1 658 GLN n 1 659 ASP n 1 660 PHE n 1 661 ASP n 1 662 LYS n 1 663 SER n 1 664 ASN n 1 665 PRO n 1 666 ILE n 1 667 VAL n 1 668 LEU n 1 669 ARG n 1 670 MET n 1 671 MET n 1 672 ASN n 1 673 ASP n 1 674 GLN n 1 675 LEU n 1 676 MET n 1 677 PHE n 1 678 LEU n 1 679 GLU n 1 680 ARG n 1 681 ALA n 1 682 PHE n 1 683 ILE n 1 684 ASP n 1 685 PRO n 1 686 LEU n 1 687 GLY n 1 688 LEU n 1 689 PRO n 1 690 ASP n 1 691 ARG n 1 692 PRO n 1 693 PHE n 1 694 TYR n 1 695 ARG n 1 696 HIS n 1 697 VAL n 1 698 ILE n 1 699 TYR n 1 700 ALA n 1 701 PRO n 1 702 SER n 1 703 SER n 1 704 HIS n 1 705 ASN n 1 706 LYS n 1 707 TYR n 1 708 ALA n 1 709 GLY n 1 710 GLU n 1 711 SER n 1 712 PHE n 1 713 PRO n 1 714 GLY n 1 715 ILE n 1 716 TYR n 1 717 ASP n 1 718 ALA n 1 719 LEU n 1 720 PHE n 1 721 ASP n 1 722 ILE n 1 723 GLU n 1 724 SER n 1 725 LYS n 1 726 VAL n 1 727 ASP n 1 728 PRO n 1 729 SER n 1 730 LYS n 1 731 ALA n 1 732 TRP n 1 733 GLY n 1 734 GLU n 1 735 VAL n 1 736 LYS n 1 737 ARG n 1 738 GLN n 1 739 ILE n 1 740 TYR n 1 741 VAL n 1 742 ALA n 1 743 ALA n 1 744 PHE n 1 745 THR n 1 746 VAL n 1 747 GLN n 1 748 ALA n 1 749 ALA n 1 750 ALA n 1 751 GLU n 1 752 THR n 1 753 LEU n 1 754 SER n 1 755 GLU n 1 756 VAL n 1 757 ALA n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'FOLH1, FOLH, NAALAD1, PSM, PSMA, GIG27' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Drosophila Melanogaster' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7227 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ;Schneider's S2 ; _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code FOLH1_HUMAN _struct_ref.pdbx_db_accession Q04609 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;KSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKT HPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIA RYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGI AEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLR GAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQ ERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEV FFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVV LRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPD RPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _struct_ref.pdbx_align_begin 44 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4MCR _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 4MCR MET A 1 ? UNP Q04609 ? ? 'INITIATING METHIONINE' -6 1 1 4MCR LYS A 2 ? UNP Q04609 ? ? 'EXPRESSION TAG' -5 2 1 4MCR LEU A 3 ? UNP Q04609 ? ? 'EXPRESSION TAG' -4 3 1 4MCR CYS A 4 ? UNP Q04609 ? ? 'EXPRESSION TAG' -3 4 1 4MCR ILE A 5 ? UNP Q04609 ? ? 'EXPRESSION TAG' -2 5 1 4MCR LEU A 6 ? UNP Q04609 ? ? 'EXPRESSION TAG' -1 6 1 4MCR LEU A 7 ? UNP Q04609 ? ? 'EXPRESSION TAG' 0 7 1 4MCR ALA A 8 ? UNP Q04609 ? ? 'EXPRESSION TAG' 1 8 1 4MCR VAL A 9 ? UNP Q04609 ? ? 'EXPRESSION TAG' 2 9 1 4MCR VAL A 10 ? UNP Q04609 ? ? 'EXPRESSION TAG' 3 10 1 4MCR ALA A 11 ? UNP Q04609 ? ? 'EXPRESSION TAG' 4 11 1 4MCR PHE A 12 ? UNP Q04609 ? ? 'EXPRESSION TAG' 5 12 1 4MCR VAL A 13 ? UNP Q04609 ? ? 'EXPRESSION TAG' 6 13 1 4MCR GLY A 14 ? UNP Q04609 ? ? 'EXPRESSION TAG' 7 14 1 4MCR LEU A 15 ? UNP Q04609 ? ? 'EXPRESSION TAG' 8 15 1 4MCR SER A 16 ? UNP Q04609 ? ? 'EXPRESSION TAG' 9 16 1 4MCR LEU A 17 ? UNP Q04609 ? ? 'EXPRESSION TAG' 10 17 1 4MCR GLY A 18 ? UNP Q04609 ? ? 'EXPRESSION TAG' 11 18 1 4MCR ARG A 19 ? UNP Q04609 ? ? 'EXPRESSION TAG' 12 19 1 4MCR SER A 20 ? UNP Q04609 ? ? 'EXPRESSION TAG' 13 20 1 4MCR GLY A 21 ? UNP Q04609 ? ? 'EXPRESSION TAG' 14 21 1 4MCR LEU A 22 ? UNP Q04609 ? ? 'EXPRESSION TAG' 15 22 1 4MCR ASN A 23 ? UNP Q04609 ? ? 'EXPRESSION TAG' 16 23 1 4MCR ASP A 24 ? UNP Q04609 ? ? 'EXPRESSION TAG' 17 24 1 4MCR ILE A 25 ? UNP Q04609 ? ? 'EXPRESSION TAG' 18 25 1 4MCR PHE A 26 ? UNP Q04609 ? ? 'EXPRESSION TAG' 19 26 1 4MCR GLU A 27 ? UNP Q04609 ? ? 'EXPRESSION TAG' 20 27 1 4MCR ALA A 28 ? UNP Q04609 ? ? 'EXPRESSION TAG' 21 28 1 4MCR GLN A 29 ? UNP Q04609 ? ? 'EXPRESSION TAG' 22 29 1 4MCR LYS A 30 ? UNP Q04609 ? ? 'EXPRESSION TAG' 23 30 1 4MCR ILE A 31 ? UNP Q04609 ? ? 'EXPRESSION TAG' 24 31 1 4MCR GLU A 32 ? UNP Q04609 ? ? 'EXPRESSION TAG' 25 32 1 4MCR TRP A 33 ? UNP Q04609 ? ? 'EXPRESSION TAG' 26 33 1 4MCR HIS A 34 ? UNP Q04609 ? ? 'EXPRESSION TAG' 27 34 1 4MCR GLU A 35 ? UNP Q04609 ? ? 'EXPRESSION TAG' 28 35 1 4MCR GLY A 36 ? UNP Q04609 ? ? 'EXPRESSION TAG' 29 36 1 4MCR SER A 37 ? UNP Q04609 ? ? 'EXPRESSION TAG' 30 37 1 4MCR GLY A 38 ? UNP Q04609 ? ? 'EXPRESSION TAG' 31 38 1 4MCR SER A 39 ? UNP Q04609 ? ? 'EXPRESSION TAG' 32 39 1 4MCR GLY A 40 ? UNP Q04609 ? ? 'EXPRESSION TAG' 33 40 1 4MCR SER A 41 ? UNP Q04609 ? ? 'EXPRESSION TAG' 34 41 1 4MCR GLU A 42 ? UNP Q04609 ? ? 'EXPRESSION TAG' 35 42 1 4MCR ASN A 43 ? UNP Q04609 ? ? 'EXPRESSION TAG' 36 43 1 4MCR LEU A 44 ? UNP Q04609 ? ? 'EXPRESSION TAG' 37 44 1 4MCR TYR A 45 ? UNP Q04609 ? ? 'EXPRESSION TAG' 38 45 1 4MCR PHE A 46 ? UNP Q04609 ? ? 'EXPRESSION TAG' 39 46 1 4MCR GLN A 47 ? UNP Q04609 ? ? 'EXPRESSION TAG' 40 47 1 4MCR GLY A 48 ? UNP Q04609 ? ? 'EXPRESSION TAG' 41 48 1 4MCR ARG A 49 ? UNP Q04609 ? ? 'EXPRESSION TAG' 42 49 1 4MCR SER A 50 ? UNP Q04609 ? ? 'EXPRESSION TAG' 43 50 1 4MCR ALA A 431 ? UNP Q04609 GLU 424 'ENGINEERED MUTATION' 424 51 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight 29D non-polymer . ;N-(4-{[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-gamma-glutamyl-L-gamma-glutamyl-L-gamma-glutamyl-L-glutamic acid ; ? 'C34 H40 N10 O15' 828.739 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 4MCR _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.08 _exptl_crystal.density_percent_sol 60.04 _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 'MARMOSAIC 225 mm CCD' _diffrn_detector.pdbx_collection_date 2010-02-24 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Si(111), Rosenbaum-Rock double-crystal monochromator' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.00 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 22-BM' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 22-BM _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.00 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MCR _reflns.observed_criterion_sigma_I -3 _reflns.observed_criterion_sigma_F -3 _reflns.d_resolution_low 40.0 _reflns.d_resolution_high 1.65 _reflns.number_obs 114830 _reflns.number_all 114830 _reflns.percent_possible_obs 91.1 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.65 _reflns_shell.d_res_low 1.71 _reflns_shell.percent_possible_all 49.9 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4MCR _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 113362 _refine.ls_number_reflns_all 113490 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 29.48 _refine.ls_d_res_high 1.65 _refine.ls_percent_reflns_obs 91.17 _refine.ls_R_factor_obs 0.13296 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.13263 _refine.ls_R_factor_R_free 0.16715 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 1.0 _refine.ls_number_reflns_R_free 1140 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.976 _refine.correlation_coeff_Fo_to_Fc_free 0.965 _refine.B_iso_mean 26.132 _refine.aniso_B[1][1] 0.02 _refine.aniso_B[2][2] 0.01 _refine.aniso_B[3][3] -0.02 _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 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.080 _refine.pdbx_overall_ESU_R_Free 0.069 _refine.overall_SU_ML 0.041 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 2.688 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 5516 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 239 _refine_hist.number_atoms_solvent 610 _refine_hist.number_atoms_total 6365 _refine_hist.d_res_high 1.65 _refine_hist.d_res_low 29.48 # 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 0.011 0.020 ? 6276 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.384 1.996 ? 8523 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.738 5.000 ? 740 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 35.780 23.849 ? 291 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 13.296 15.000 ? 1012 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 14.312 15.000 ? 36 'X-RAY DIFFRACTION' ? r_chiral_restr 0.092 0.200 ? 906 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.007 0.021 ? 4870 '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 0.734 1.500 ? 3625 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.286 2.000 ? 5907 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.157 3.000 ? 2630 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 3.480 4.500 ? 2615 '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 2.566 3.000 ? 6276 'X-RAY DIFFRACTION' ? r_sphericity_free 26.849 5.000 ? 171 'X-RAY DIFFRACTION' ? r_sphericity_bonded 16.270 5.000 ? 6510 '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 1.650 _refine_ls_shell.d_res_low 1.693 _refine_ls_shell.number_reflns_R_work 4185 _refine_ls_shell.R_factor_R_work 0.221 _refine_ls_shell.percent_reflns_obs 46.72 _refine_ls_shell.R_factor_R_free 0.260 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 51 _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 4MCR _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 4MCR _struct.title ;A high resolution structure of human glutamate carboxypeptidase II (GCPII) in complex with folyltri-gamma-L-glutamic acid (pteroyltetra-gamma-L-glutamic acid) ; _struct.pdbx_descriptor 'Glutamate carboxypeptidase 2 (E.C.3.4.17.21)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4MCR _struct_keywords.pdbx_keywords 'hydrolase/hydrolase inhibitor' _struct_keywords.text 'hydrolase, metallopeptidase, hydrolase-hydrolase inhibitor complex' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 4 ? F N N 5 ? G N N 5 ? H N N 5 ? I N N 5 ? J N N 5 ? K N N 5 ? L N N 5 ? M N N 5 ? N N N 5 ? O N N 5 ? P N N 5 ? Q N N 6 ? R N N 7 ? S N N 8 ? T N N 9 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASN A 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 ? GLY A 111 ? THR A 86 GLY A 104 1 ? 19 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 ? ? P NAG . O4 ? ? ? 1_555 Q BMA . C1 ? ? A NAG 815 A BMA 816 1_555 ? ? ? ? ? ? ? 1.335 ? covale2 covale ? ? Q BMA . O3 ? ? ? 1_555 R MAN . C1 ? ? A BMA 816 A MAN 817 1_555 ? ? ? ? ? ? ? 1.345 ? covale3 covale ? ? A ASN 83 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 76 A NAG 805 1_555 ? ? ? ? ? ? ? 1.427 ? covale4 covale ? ? A ASN 483 ND2 ? ? ? 1_555 M NAG . C1 ? ? A ASN 476 A NAG 812 1_555 ? ? ? ? ? ? ? 1.437 ? covale5 covale ? ? A ASN 645 ND2 ? ? ? 1_555 O NAG . C1 ? ? A ASN 638 A NAG 814 1_555 ? ? ? ? ? ? ? 1.437 ? covale6 covale ? ? M NAG . O4 ? ? ? 1_555 N NAG . C1 ? ? A NAG 812 A NAG 813 1_555 ? ? ? ? ? ? ? 1.438 ? covale7 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 805 A NAG 806 1_555 ? ? ? ? ? ? ? 1.439 ? covale8 covale ? ? A ASN 147 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 140 A NAG 808 1_555 ? ? ? ? ? ? ? 1.440 ? covale9 covale ? ? O NAG . O4 ? ? ? 1_555 P NAG . C1 ? ? A NAG 814 A NAG 815 1_555 ? ? ? ? ? ? ? 1.441 ? covale10 covale ? ? A ASN 466 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 459 A NAG 811 1_555 ? ? ? ? ? ? ? 1.444 ? covale11 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 808 A NAG 809 1_555 ? ? ? ? ? ? ? 1.445 ? covale12 covale ? ? A ASN 128 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 121 A NAG 807 1_555 ? ? ? ? ? ? ? 1.447 ? covale13 covale ? ? A ASN 202 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 195 A NAG 810 1_555 ? ? ? ? ? ? ? 1.449 ? metalc1 metalc ? ? C ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 802 A HOH 1339 1_555 ? ? ? ? ? ? ? 1.968 ? metalc2 metalc ? ? B ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 801 A HOH 1339 1_555 ? ? ? ? ? ? ? 1.974 ? metalc3 metalc ? ? A ASP 394 OD1 ? ? ? 1_555 C ZN . ZN ? ? A ASP 387 A ZN 802 1_555 ? ? ? ? ? ? ? 1.980 ? metalc4 metalc ? ? A ASP 460 OD2 ? ? ? 1_555 C ZN . ZN ? ? A ASP 453 A ZN 802 1_555 ? ? ? ? ? ? ? 1.984 ? metalc5 metalc ? ? A ASP 394 OD2 ? ? ? 1_555 B ZN . ZN ? ? A ASP 387 A ZN 801 1_555 ? ? ? ? ? ? ? 2.024 ? metalc6 metalc ? ? A HIS 384 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 377 A ZN 802 1_555 ? ? ? ? ? ? ? 2.030 ? metalc7 metalc ? ? A HIS 560 NE2 ? ? ? 1_555 B ZN . ZN ? ? A HIS 553 A ZN 801 1_555 ? ? ? ? ? ? ? 2.041 ? metalc8 metalc ? ? A GLU 432 OE2 ? ? ? 1_555 B ZN . ZN ? ? A GLU 425 A ZN 801 1_555 ? ? ? ? ? ? ? 2.055 ? metalc9 metalc ? ? B ZN . ZN ? ? ? 1_555 S 29D . OAG ? ? A ZN 801 A 29D 818 1_555 ? ? ? ? ? ? ? 2.166 ? metalc10 metalc ? ? A GLU 432 OE1 ? ? ? 1_555 B ZN . ZN ? ? A GLU 425 A ZN 801 1_555 ? ? ? ? ? ? ? 2.175 ? metalc11 metalc ? ? A GLU 443 OE2 ? ? ? 1_555 D CA . CA ? ? A GLU 436 A CA 803 1_555 ? ? ? ? ? ? ? 2.310 ? metalc12 metalc ? ? A TYR 279 O ? ? ? 1_555 D CA . CA ? ? A TYR 272 A CA 803 1_555 ? ? ? ? ? ? ? 2.345 ? metalc13 metalc ? ? A GLU 440 OE1 ? ? ? 1_555 D CA . CA ? ? A GLU 433 A CA 803 1_555 ? ? ? ? ? ? ? 2.365 ? metalc14 metalc ? ? D CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 803 A HOH 906 1_555 ? ? ? ? ? ? ? 2.366 ? metalc15 metalc ? ? A THR 276 O ? ? ? 1_555 D CA . CA ? ? A THR 269 A CA 803 1_555 ? ? ? ? ? ? ? 2.369 ? metalc16 metalc ? ? A THR 276 OG1 ? ? ? 1_555 D CA . CA ? ? A THR 269 A CA 803 1_555 ? ? ? ? ? ? ? 2.400 ? metalc17 metalc ? ? A GLU 440 OE2 ? ? ? 1_555 D CA . CA ? ? A GLU 433 A CA 803 1_555 ? ? ? ? ? ? ? 2.415 ? # 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 9.29 2 GLY 337 A . ? GLY 330 A PRO 338 A ? PRO 331 A 1 2.35 3 ASP 394 A . ? ASP 387 A PRO 395 A ? PRO 388 A 1 6.11 # 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 ILE A 138 ? N ILE A 131 O LYS A 348 ? O LYS A 341 B 3 4 O VAL A 349 ? O VAL A 342 N GLY A 179 ? N GLY A 172 C 1 2 O ALA A 170 ? O ALA A 163 N GLY A 263 ? N GLY A 256 D 1 2 N VAL A 182 ? N VAL A 175 O ILE A 209 ? O ILE A 202 D 2 3 N ALA A 210 ? N ALA A 203 O ILE A 233 ? O ILE A 226 D 3 4 N LEU A 234 ? N LEU A 227 O HIS A 302 ? O HIS A 295 E 1 2 N SER A 702 ? N SER A 695 O ALA A 708 ? O ALA A 701 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ZN A 801' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ZN A 802' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 803' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CL A 804' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 805' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 806' AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 807' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 808' AC9 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 809' BC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 810' BC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 811' BC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 812' BC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 813' BC5 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 814' BC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 815' BC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE BMA A 816' BC8 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE MAN A 817' BC9 Software ? ? ? ? 29 'BINDING SITE FOR RESIDUE 29D A 818' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 ASP A 394 ? ASP A 387 . ? 1_555 ? 2 AC1 6 GLU A 432 ? GLU A 425 . ? 1_555 ? 3 AC1 6 HIS A 560 ? HIS A 553 . ? 1_555 ? 4 AC1 6 ZN C . ? ZN A 802 . ? 1_555 ? 5 AC1 6 29D S . ? 29D A 818 . ? 1_555 ? 6 AC1 6 HOH T . ? HOH A 1339 . ? 1_555 ? 7 AC2 6 HIS A 384 ? HIS A 377 . ? 1_555 ? 8 AC2 6 ASP A 394 ? ASP A 387 . ? 1_555 ? 9 AC2 6 GLU A 432 ? GLU A 425 . ? 1_555 ? 10 AC2 6 ASP A 460 ? ASP A 453 . ? 1_555 ? 11 AC2 6 ZN B . ? ZN A 801 . ? 1_555 ? 12 AC2 6 HOH T . ? HOH A 1339 . ? 1_555 ? 13 AC3 5 THR A 276 ? THR A 269 . ? 1_555 ? 14 AC3 5 TYR A 279 ? TYR A 272 . ? 1_555 ? 15 AC3 5 GLU A 440 ? GLU A 433 . ? 1_555 ? 16 AC3 5 GLU A 443 ? GLU A 436 . ? 1_555 ? 17 AC3 5 HOH T . ? HOH A 906 . ? 1_555 ? 18 AC4 4 ASN A 458 ? ASN A 451 . ? 1_555 ? 19 AC4 4 ASP A 460 ? ASP A 453 . ? 1_555 ? 20 AC4 4 ARG A 541 ? ARG A 534 . ? 1_555 ? 21 AC4 4 ARG A 543 ? ARG A 536 . ? 1_555 ? 22 AC5 6 ASN A 83 ? ASN A 76 . ? 1_555 ? 23 AC5 6 GLN A 102 ? GLN A 95 . ? 1_555 ? 24 AC5 6 GLN A 106 ? GLN A 99 . ? 1_555 ? 25 AC5 6 NAG G . ? NAG A 806 . ? 1_555 ? 26 AC5 6 HOH T . ? HOH A 1127 . ? 1_555 ? 27 AC5 6 HOH T . ? HOH A 1346 . ? 1_555 ? 28 AC6 3 NAG F . ? NAG A 805 . ? 1_555 ? 29 AC6 3 HOH T . ? HOH A 1491 . ? 1_555 ? 30 AC6 3 HOH T . ? HOH A 1495 . ? 1_555 ? 31 AC7 5 ASN A 128 ? ASN A 121 . ? 1_555 ? 32 AC7 5 THR A 130 ? THR A 123 . ? 1_555 ? 33 AC7 5 HIS A 131 ? HIS A 124 . ? 1_555 ? 34 AC7 5 THR A 356 ? THR A 349 . ? 1_555 ? 35 AC7 5 HOH T . ? HOH A 1294 . ? 1_555 ? 36 AC8 5 TYR A 134 ? TYR A 127 . ? 1_555 ? 37 AC8 5 GLU A 144 ? GLU A 137 . ? 1_555 ? 38 AC8 5 ILE A 145 ? ILE A 138 . ? 1_555 ? 39 AC8 5 ASN A 147 ? ASN A 140 . ? 1_555 ? 40 AC8 5 NAG J . ? NAG A 809 . ? 1_555 ? 41 AC9 2 NAG I . ? NAG A 808 . ? 1_555 ? 42 AC9 2 HOH T . ? HOH A 1400 . ? 1_555 ? 43 BC1 2 ASN A 202 ? ASN A 195 . ? 1_555 ? 44 BC1 2 SER A 204 ? SER A 197 . ? 1_555 ? 45 BC2 9 TRP A 253 ? TRP A 246 . ? 1_555 ? 46 BC2 9 ASN A 466 ? ASN A 459 . ? 1_555 ? 47 BC2 9 PHE A 572 ? PHE A 565 . ? 1_555 ? 48 BC2 9 TYR A 573 ? TYR A 566 . ? 1_555 ? 49 BC2 9 HOH T . ? HOH A 977 . ? 1_555 ? 50 BC2 9 HOH T . ? HOH A 1143 . ? 1_555 ? 51 BC2 9 HOH T . ? HOH A 1326 . ? 1_555 ? 52 BC2 9 HOH T . ? HOH A 1362 . ? 1_555 ? 53 BC2 9 HOH T . ? HOH A 1454 . ? 1_555 ? 54 BC3 6 SER A 479 ? SER A 472 . ? 1_555 ? 55 BC3 6 ASN A 483 ? ASN A 476 . ? 1_555 ? 56 BC3 6 PRO A 601 ? PRO A 594 . ? 1_555 ? 57 BC3 6 NAG N . ? NAG A 813 . ? 1_555 ? 58 BC3 6 HOH T . ? HOH A 1478 . ? 1_555 ? 59 BC3 6 HOH T . ? HOH A 1490 . ? 1_555 ? 60 BC4 2 NAG M . ? NAG A 812 . ? 1_555 ? 61 BC4 2 HOH T . ? HOH A 1275 . ? 1_555 ? 62 BC5 8 SER A 638 ? SER A 631 . ? 1_555 ? 63 BC5 8 SER A 641 ? SER A 634 . ? 1_555 ? 64 BC5 8 ASN A 645 ? ASN A 638 . ? 1_555 ? 65 BC5 8 GLN A 747 ? GLN A 740 . ? 1_555 ? 66 BC5 8 NAG P . ? NAG A 815 . ? 1_555 ? 67 BC5 8 HOH T . ? HOH A 1024 . ? 1_555 ? 68 BC5 8 HOH T . ? HOH A 1057 . ? 2_565 ? 69 BC5 8 HOH T . ? HOH A 1190 . ? 1_555 ? 70 BC6 3 GLU A 283 ? GLU A 276 . ? 2_565 ? 71 BC6 3 NAG O . ? NAG A 814 . ? 1_555 ? 72 BC6 3 BMA Q . ? BMA A 816 . ? 1_555 ? 73 BC7 5 HIS A 119 ? HIS A 112 . ? 2_565 ? 74 BC7 5 GLU A 283 ? GLU A 276 . ? 2_565 ? 75 BC7 5 ARG A 361 ? ARG A 354 . ? 2_565 ? 76 BC7 5 NAG P . ? NAG A 815 . ? 1_555 ? 77 BC7 5 MAN R . ? MAN A 817 . ? 1_555 ? 78 BC8 10 PHE A 242 ? PHE A 235 . ? 7_555 ? 79 BC8 10 LYS A 247 ? LYS A 240 . ? 7_555 ? 80 BC8 10 SER A 248 ? SER A 241 . ? 7_555 ? 81 BC8 10 GLU A 283 ? GLU A 276 . ? 2_565 ? 82 BC8 10 ARG A 361 ? ARG A 354 . ? 2_565 ? 83 BC8 10 BMA Q . ? BMA A 816 . ? 1_555 ? 84 BC8 10 HOH T . ? HOH A 1274 . ? 7_555 ? 85 BC8 10 HOH T . ? HOH A 1292 . ? 1_555 ? 86 BC8 10 HOH T . ? HOH A 1311 . ? 1_555 ? 87 BC8 10 HOH T . ? HOH A 1448 . ? 7_555 ? 88 BC9 29 ARG A 217 ? ARG A 210 . ? 1_555 ? 89 BC9 29 ASN A 264 ? ASN A 257 . ? 1_555 ? 90 BC9 29 ASP A 394 ? ASP A 387 . ? 1_555 ? 91 BC9 29 ALA A 431 ? ALA A 424 . ? 1_555 ? 92 BC9 29 GLU A 432 ? GLU A 425 . ? 1_555 ? 93 BC9 29 GLY A 434 ? GLY A 427 . ? 1_555 ? 94 BC9 29 ARG A 470 ? ARG A 463 . ? 1_555 ? 95 BC9 29 ARG A 518 ? ARG A 511 . ? 1_555 ? 96 BC9 29 SER A 520 ? SER A 513 . ? 1_555 ? 97 BC9 29 GLY A 525 ? GLY A 518 . ? 1_555 ? 98 BC9 29 ASN A 526 ? ASN A 519 . ? 1_555 ? 99 BC9 29 ARG A 541 ? ARG A 534 . ? 1_555 ? 100 BC9 29 ARG A 543 ? ARG A 536 . ? 1_555 ? 101 BC9 29 TRP A 548 ? TRP A 541 . ? 1_555 ? 102 BC9 29 GLU A 549 ? GLU A 542 . ? 1_555 ? 103 BC9 29 TYR A 559 ? TYR A 552 . ? 1_555 ? 104 BC9 29 HIS A 560 ? HIS A 553 . ? 1_555 ? 105 BC9 29 LYS A 706 ? LYS A 699 . ? 1_555 ? 106 BC9 29 TYR A 707 ? TYR A 700 . ? 1_555 ? 107 BC9 29 ALA A 708 ? ALA A 701 . ? 1_555 ? 108 BC9 29 ZN B . ? ZN A 801 . ? 1_555 ? 109 BC9 29 HOH T . ? HOH A 909 . ? 1_555 ? 110 BC9 29 HOH T . ? HOH A 1067 . ? 1_555 ? 111 BC9 29 HOH T . ? HOH A 1272 . ? 1_555 ? 112 BC9 29 HOH T . ? HOH A 1281 . ? 1_555 ? 113 BC9 29 HOH T . ? HOH A 1290 . ? 1_555 ? 114 BC9 29 HOH T . ? HOH A 1339 . ? 1_555 ? 115 BC9 29 HOH T . ? HOH A 1453 . ? 1_555 ? 116 BC9 29 HOH T . ? HOH A 1494 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MCR _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 4MCR _atom_sites.fract_transf_matrix[1][1] 0.009853 _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] 0.007702 _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] 0.006297 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CA CL N O S ZN # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . HIS A 1 63 ? 14.846 46.556 79.921 1.00 49.09 ? 56 HIS A N 1 ATOM 2 C CA . HIS A 1 63 ? 14.369 46.610 78.503 1.00 41.84 ? 56 HIS A CA 1 ATOM 3 C C . HIS A 1 63 ? 14.803 47.866 77.808 1.00 42.45 ? 56 HIS A C 1 ATOM 4 O O . HIS A 1 63 ? 14.092 48.873 77.812 1.00 50.98 ? 56 HIS A O 1 ATOM 5 C CB . HIS A 1 63 ? 12.850 46.492 78.426 1.00 43.88 ? 56 HIS A CB 1 ATOM 6 C CG . HIS A 1 63 ? 12.322 45.132 78.802 1.00 48.71 ? 56 HIS A CG 1 ATOM 7 N ND1 . HIS A 1 63 ? 11.200 44.970 79.528 1.00 47.58 ? 56 HIS A ND1 1 ATOM 8 C CD2 . HIS A 1 63 ? 12.810 43.854 78.532 1.00 46.86 ? 56 HIS A CD2 1 ATOM 9 C CE1 . HIS A 1 63 ? 10.975 43.654 79.711 1.00 53.50 ? 56 HIS A CE1 1 ATOM 10 N NE2 . HIS A 1 63 ? 11.962 42.973 79.100 1.00 51.92 ? 56 HIS A NE2 1 ATOM 11 N N . ASN A 1 64 ? 15.983 47.809 77.204 1.00 38.37 ? 57 ASN A N 1 ATOM 12 C CA . ASN A 1 64 ? 16.575 48.945 76.509 1.00 35.52 ? 57 ASN A CA 1 ATOM 13 C C . ASN A 1 64 ? 17.196 48.426 75.232 1.00 31.97 ? 57 ASN A C 1 ATOM 14 O O . ASN A 1 64 ? 17.066 47.232 74.915 1.00 32.04 ? 57 ASN A O 1 ATOM 15 C CB . ASN A 1 64 ? 17.637 49.618 77.389 1.00 31.83 ? 57 ASN A CB 1 ATOM 16 C CG . ASN A 1 64 ? 18.627 48.626 77.989 1.00 36.28 ? 57 ASN A CG 1 ATOM 17 O OD1 . ASN A 1 64 ? 18.762 47.478 77.529 1.00 36.20 ? 57 ASN A OD1 1 ATOM 18 N ND2 . ASN A 1 64 ? 19.335 49.067 79.025 1.00 37.95 ? 57 ASN A ND2 1 ATOM 19 N N . MET A 1 65 ? 17.874 49.293 74.485 1.00 30.91 ? 58 MET A N 1 ATOM 20 C CA . MET A 1 65 ? 18.423 48.816 73.223 1.00 29.67 ? 58 MET A CA 1 ATOM 21 C C . MET A 1 65 ? 19.441 47.690 73.402 1.00 30.31 ? 58 MET A C 1 ATOM 22 O O . MET A 1 65 ? 19.486 46.773 72.583 1.00 30.01 ? 58 MET A O 1 ATOM 23 C CB . MET A 1 65 ? 19.028 49.912 72.372 1.00 30.50 ? 58 MET A CB 1 ATOM 24 C CG . MET A 1 65 ? 19.128 49.421 70.924 1.00 34.20 ? 58 MET A CG 1 ATOM 25 S SD . MET A 1 65 ? 20.196 50.426 69.921 1.00 42.50 ? 58 MET A SD 1 ATOM 26 C CE . MET A 1 65 ? 19.242 51.902 69.803 1.00 36.24 ? 58 MET A CE 1 ATOM 27 N N . LYS A 1 66 ? 20.248 47.760 74.458 1.00 30.72 ? 59 LYS A N 1 ATOM 28 C CA . LYS A 1 66 ? 21.236 46.721 74.706 1.00 30.38 ? 59 LYS A CA 1 ATOM 29 C C . LYS A 1 66 ? 20.570 45.347 74.860 1.00 30.07 ? 59 LYS A C 1 ATOM 30 O O . LYS A 1 66 ? 21.077 44.351 74.341 1.00 30.44 ? 59 LYS A O 1 ATOM 31 C CB . LYS A 1 66 ? 22.085 47.042 75.941 1.00 29.42 ? 59 LYS A CB 1 ATOM 32 C CG . LYS A 1 66 ? 23.273 46.110 76.118 1.00 35.94 ? 59 LYS A CG 1 ATOM 33 C CD . LYS A 1 66 ? 24.059 46.468 77.376 1.00 43.71 ? 59 LYS A CD 1 ATOM 34 C CE . LYS A 1 66 ? 25.454 45.846 77.379 1.00 53.42 ? 59 LYS A CE 1 ATOM 35 N NZ . LYS A 1 66 ? 25.443 44.361 77.259 1.00 54.55 ? 59 LYS A NZ 1 ATOM 36 N N . ALA A 1 67 ? 19.438 45.297 75.568 1.00 29.40 ? 60 ALA A N 1 ATOM 37 C CA . ALA A 1 67 ? 18.708 44.035 75.733 1.00 30.38 ? 60 ALA A CA 1 ATOM 38 C C . ALA A 1 67 ? 18.275 43.530 74.361 1.00 27.18 ? 60 ALA A C 1 ATOM 39 O O . ALA A 1 67 ? 18.478 42.363 74.034 1.00 29.62 ? 60 ALA A O 1 ATOM 40 C CB . ALA A 1 67 ? 17.506 44.203 76.642 1.00 33.07 ? 60 ALA A CB 1 ATOM 41 N N . PHE A 1 68 ? 17.683 44.423 73.563 1.00 27.36 ? 61 PHE A N 1 ATOM 42 C CA . PHE A 1 68 ? 17.288 44.061 72.201 1.00 26.45 ? 61 PHE A CA 1 ATOM 43 C C . PHE A 1 68 ? 18.483 43.499 71.406 1.00 26.67 ? 61 PHE A C 1 ATOM 44 O O . PHE A 1 68 ? 18.405 42.409 70.828 1.00 26.15 ? 61 PHE A O 1 ATOM 45 C CB . PHE A 1 68 ? 16.637 45.241 71.445 1.00 25.55 ? 61 PHE A CB 1 ATOM 46 C CG . PHE A 1 68 ? 16.578 45.019 69.956 1.00 25.08 ? 61 PHE A CG 1 ATOM 47 C CD1 . PHE A 1 68 ? 15.635 44.153 69.397 1.00 25.49 ? 61 PHE A CD1 1 ATOM 48 C CD2 . PHE A 1 68 ? 17.510 45.625 69.113 1.00 24.11 ? 61 PHE A CD2 1 ATOM 49 C CE1 . PHE A 1 68 ? 15.620 43.910 68.020 1.00 23.73 ? 61 PHE A CE1 1 ATOM 50 C CE2 . PHE A 1 68 ? 17.495 45.393 67.742 1.00 22.94 ? 61 PHE A CE2 1 ATOM 51 C CZ . PHE A 1 68 ? 16.553 44.537 67.192 1.00 23.61 ? 61 PHE A CZ 1 ATOM 52 N N . LEU A 1 69 ? 19.589 44.244 71.397 1.00 26.68 ? 62 LEU A N 1 ATOM 53 C CA . LEU A 1 69 ? 20.758 43.873 70.609 1.00 27.43 ? 62 LEU A CA 1 ATOM 54 C C . LEU A 1 69 ? 21.385 42.559 71.067 1.00 27.57 ? 62 LEU A C 1 ATOM 55 O O . LEU A 1 69 ? 21.772 41.726 70.238 1.00 28.39 ? 62 LEU A O 1 ATOM 56 C CB . LEU A 1 69 ? 21.801 44.988 70.642 1.00 28.41 ? 62 LEU A CB 1 ATOM 57 C CG . LEU A 1 69 ? 21.400 46.291 69.945 1.00 23.57 ? 62 LEU A CG 1 ATOM 58 C CD1 . LEU A 1 69 ? 22.425 47.355 70.326 1.00 29.21 ? 62 LEU A CD1 1 ATOM 59 C CD2 . LEU A 1 69 ? 21.269 46.144 68.428 1.00 25.84 ? 62 LEU A CD2 1 ATOM 60 N N . ASP A 1 70 ? 21.469 42.373 72.380 1.00 27.52 ? 63 ASP A N 1 ATOM 61 C CA . ASP A 1 70 ? 22.090 41.178 72.943 1.00 30.67 ? 63 ASP A CA 1 ATOM 62 C C . ASP A 1 70 ? 21.331 39.904 72.588 1.00 29.34 ? 63 ASP A C 1 ATOM 63 O O . ASP A 1 70 ? 21.923 38.836 72.515 1.00 30.58 ? 63 ASP A O 1 ATOM 64 C CB . ASP A 1 70 ? 22.208 41.297 74.459 1.00 31.67 ? 63 ASP A CB 1 ATOM 65 C CG . ASP A 1 70 ? 23.352 42.196 74.891 1.00 34.37 ? 63 ASP A CG 1 ATOM 66 O OD1 . ASP A 1 70 ? 24.188 42.584 74.048 1.00 36.12 ? 63 ASP A OD1 1 ATOM 67 O OD2 . ASP A 1 70 ? 23.428 42.505 76.095 1.00 38.31 ? 63 ASP A OD2 1 ATOM 68 N N . GLU A 1 71 ? 20.025 40.025 72.376 1.00 28.37 ? 64 GLU A N 1 ATOM 69 C CA . GLU A 1 71 ? 19.174 38.874 72.087 1.00 29.43 ? 64 GLU A CA 1 ATOM 70 C C . GLU A 1 71 ? 19.380 38.330 70.667 1.00 27.69 ? 64 GLU A C 1 ATOM 71 O O . GLU A 1 71 ? 19.188 37.135 70.433 1.00 28.01 ? 64 GLU A O 1 ATOM 72 C CB . GLU A 1 71 ? 17.701 39.222 72.355 1.00 29.03 ? 64 GLU A CB 1 ATOM 73 C CG . GLU A 1 71 ? 16.687 38.116 72.072 1.00 32.18 ? 64 GLU A CG 1 ATOM 74 C CD . GLU A 1 71 ? 16.890 36.865 72.919 1.00 34.74 ? 64 GLU A CD 1 ATOM 75 O OE1 . GLU A 1 71 ? 17.267 36.988 74.104 1.00 34.34 ? 64 GLU A OE1 1 ATOM 76 O OE2 . GLU A 1 71 ? 16.681 35.747 72.396 1.00 32.90 ? 64 GLU A OE2 1 ATOM 77 N N . LEU A 1 72 ? 19.774 39.200 69.732 1.00 26.69 ? 65 LEU A N 1 ATOM 78 C CA . LEU A 1 72 ? 20.145 38.781 68.363 1.00 24.91 ? 65 LEU A CA 1 ATOM 79 C C . LEU A 1 72 ? 21.296 37.772 68.341 1.00 25.96 ? 65 LEU A C 1 ATOM 80 O O . LEU A 1 72 ? 22.325 37.996 68.982 1.00 27.03 ? 65 LEU A O 1 ATOM 81 C CB . LEU A 1 72 ? 20.551 40.004 67.530 1.00 23.56 ? 65 LEU A CB 1 ATOM 82 C CG . LEU A 1 72 ? 19.571 41.171 67.393 1.00 21.29 ? 65 LEU A CG 1 ATOM 83 C CD1 . LEU A 1 72 ? 20.302 42.377 66.809 1.00 22.71 ? 65 LEU A CD1 1 ATOM 84 C CD2 . LEU A 1 72 ? 18.381 40.783 66.506 1.00 22.00 ? 65 LEU A CD2 1 ATOM 85 N N . LYS A 1 73 ? 21.143 36.679 67.587 1.00 24.57 ? 66 LYS A N 1 ATOM 86 C CA . LYS A 1 73 ? 22.176 35.628 67.532 1.00 25.98 ? 66 LYS A CA 1 ATOM 87 C C . LYS A 1 73 ? 22.547 35.277 66.095 1.00 24.72 ? 66 LYS A C 1 ATOM 88 O O . LYS A 1 73 ? 21.675 35.046 65.257 1.00 25.45 ? 66 LYS A O 1 ATOM 89 C CB . LYS A 1 73 ? 21.720 34.341 68.252 1.00 26.69 ? 66 LYS A CB 1 ATOM 90 C CG . LYS A 1 73 ? 21.250 34.508 69.698 1.00 32.65 ? 66 LYS A CG 1 ATOM 91 C CD . LYS A 1 73 ? 22.396 34.861 70.630 1.00 40.64 ? 66 LYS A CD 1 ATOM 92 C CE . LYS A 1 73 ? 22.006 34.711 72.097 1.00 42.94 ? 66 LYS A CE 1 ATOM 93 N NZ . LYS A 1 73 ? 21.137 35.821 72.563 1.00 42.19 ? 66 LYS A NZ 1 ATOM 94 N N . ALA A 1 74 ? 23.844 35.221 65.831 1.00 26.39 ? 67 ALA A N 1 ATOM 95 C CA . ALA A 1 74 ? 24.365 34.809 64.537 1.00 25.89 ? 67 ALA A CA 1 ATOM 96 C C . ALA A 1 74 ? 23.849 33.425 64.159 1.00 24.31 ? 67 ALA A C 1 ATOM 97 O O . ALA A 1 74 ? 23.509 33.196 62.995 1.00 24.14 ? 67 ALA A O 1 ATOM 98 C CB . ALA A 1 74 ? 25.892 34.812 64.551 1.00 25.37 ? 67 ALA A CB 1 ATOM 99 N N . GLU A 1 75 ? 23.796 32.513 65.136 1.00 24.08 ? 68 GLU A N 1 ATOM 100 C CA . GLU A 1 75 ? 23.379 31.124 64.871 1.00 25.00 ? 68 GLU A CA 1 ATOM 101 C C . GLU A 1 75 ? 21.930 31.049 64.385 1.00 25.68 ? 68 GLU A C 1 ATOM 102 O O . GLU A 1 75 ? 21.594 30.202 63.540 1.00 24.89 ? 68 GLU A O 1 ATOM 103 C CB . GLU A 1 75 ? 23.584 30.234 66.101 1.00 28.06 ? 68 GLU A CB 1 ATOM 104 C CG . GLU A 1 75 ? 23.254 28.758 65.860 0.80 32.94 ? 68 GLU A CG 1 ATOM 105 C CD . GLU A 1 75 ? 24.098 28.087 64.774 0.80 41.11 ? 68 GLU A CD 1 ATOM 106 O OE1 . GLU A 1 75 ? 25.315 28.387 64.636 0.80 37.99 ? 68 GLU A OE1 1 ATOM 107 O OE2 . GLU A 1 75 ? 23.534 27.232 64.052 0.80 53.15 ? 68 GLU A OE2 1 ATOM 108 N N . ASN A 1 76 ? 21.079 31.934 64.905 1.00 23.62 ? 69 ASN A N 1 ATOM 109 C CA . ASN A 1 76 ? 19.684 32.002 64.435 1.00 23.33 ? 69 ASN A CA 1 ATOM 110 C C . ASN A 1 76 ? 19.561 32.499 63.010 1.00 22.53 ? 69 ASN A C 1 ATOM 111 O O . ASN A 1 76 ? 18.786 31.950 62.217 1.00 23.57 ? 69 ASN A O 1 ATOM 112 C CB . ASN A 1 76 ? 18.800 32.858 65.357 1.00 25.01 ? 69 ASN A CB 1 ATOM 113 C CG . ASN A 1 76 ? 18.564 32.202 66.703 1.00 26.01 ? 69 ASN A CG 1 ATOM 114 O OD1 . ASN A 1 76 ? 18.562 30.969 66.818 1.00 27.26 ? 69 ASN A OD1 1 ATOM 115 N ND2 . ASN A 1 76 ? 18.401 33.023 67.738 1.00 26.38 ? 69 ASN A ND2 1 ATOM 116 N N . ILE A 1 77 ? 20.323 33.541 62.689 1.00 21.74 ? 70 ILE A N 1 ATOM 117 C CA . ILE A 1 77 ? 20.333 34.100 61.325 1.00 20.53 ? 70 ILE A CA 1 ATOM 118 C C . ILE A 1 77 ? 20.762 32.996 60.349 1.00 22.13 ? 70 ILE A C 1 ATOM 119 O O . ILE A 1 77 ? 20.140 32.814 59.288 1.00 20.77 ? 70 ILE A O 1 ATOM 120 C CB . ILE A 1 77 ? 21.265 35.328 61.231 1.00 19.83 ? 70 ILE A CB 1 ATOM 121 C CG1 . ILE A 1 77 ? 20.766 36.440 62.182 1.00 21.64 ? 70 ILE A CG1 1 ATOM 122 C CG2 . ILE A 1 77 ? 21.322 35.860 59.800 1.00 20.14 ? 70 ILE A CG2 1 ATOM 123 C CD1 . ILE A 1 77 ? 21.707 37.613 62.356 1.00 23.21 ? 70 ILE A CD1 1 ATOM 124 N N . LYS A 1 78 ? 21.796 32.243 60.737 1.00 20.28 ? 71 LYS A N 1 ATOM 125 C CA . LYS A 1 78 ? 22.288 31.104 59.939 1.00 21.06 ? 71 LYS A CA 1 ATOM 126 C C . LYS A 1 78 ? 21.181 30.060 59.713 1.00 22.80 ? 71 LYS A C 1 ATOM 127 O O . LYS A 1 78 ? 20.932 29.663 58.568 1.00 21.98 ? 71 LYS A O 1 ATOM 128 C CB . LYS A 1 78 ? 23.516 30.463 60.618 1.00 21.92 ? 71 LYS A CB 1 ATOM 129 C CG . LYS A 1 78 ? 24.140 29.292 59.870 1.00 22.39 ? 71 LYS A CG 1 ATOM 130 C CD . LYS A 1 78 ? 25.386 28.829 60.619 1.00 24.96 ? 71 LYS A CD 1 ATOM 131 C CE . LYS A 1 78 ? 25.946 27.545 60.050 1.00 27.66 ? 71 LYS A CE 1 ATOM 132 N NZ . LYS A 1 78 ? 27.117 27.025 60.824 1.00 29.03 ? 71 LYS A NZ 1 ATOM 133 N N . LYS A 1 79 ? 20.528 29.622 60.796 1.00 22.77 ? 72 LYS A N 1 ATOM 134 C CA . LYS A 1 79 ? 19.409 28.655 60.712 1.00 22.68 ? 72 LYS A CA 1 ATOM 135 C C . LYS A 1 79 ? 18.281 29.151 59.788 1.00 21.56 ? 72 LYS A C 1 ATOM 136 O O . LYS A 1 79 ? 17.767 28.399 58.950 1.00 22.22 ? 72 LYS A O 1 ATOM 137 C CB . LYS A 1 79 ? 18.855 28.317 62.107 1.00 23.87 ? 72 LYS A CB 1 ATOM 138 C CG . LYS A 1 79 ? 19.788 27.448 62.927 0.50 23.19 ? 72 LYS A CG 1 ATOM 139 C CD . LYS A 1 79 ? 19.247 27.198 64.326 0.50 24.40 ? 72 LYS A CD 1 ATOM 140 C CE . LYS A 1 79 ? 20.305 26.541 65.199 0.20 24.64 ? 72 LYS A CE 1 ATOM 141 N NZ . LYS A 1 79 ? 19.813 26.301 66.582 0.20 26.12 ? 72 LYS A NZ 1 ATOM 142 N N . PHE A 1 80 ? 17.918 30.423 59.927 1.00 20.49 ? 73 PHE A N 1 ATOM 143 C CA . PHE A 1 80 ? 16.880 31.017 59.085 1.00 19.74 ? 73 PHE A CA 1 ATOM 144 C C . PHE A 1 80 ? 17.320 31.078 57.615 1.00 19.91 ? 73 PHE A C 1 ATOM 145 O O . PHE A 1 80 ? 16.540 30.749 56.706 1.00 19.19 ? 73 PHE A O 1 ATOM 146 C CB . PHE A 1 80 ? 16.494 32.413 59.600 1.00 20.09 ? 73 PHE A CB 1 ATOM 147 C CG . PHE A 1 80 ? 15.907 32.415 60.990 1.00 20.40 ? 73 PHE A CG 1 ATOM 148 C CD1 . PHE A 1 80 ? 15.223 31.300 61.498 1.00 21.09 ? 73 PHE A CD1 1 ATOM 149 C CD2 . PHE A 1 80 ? 16.011 33.560 61.796 1.00 21.27 ? 73 PHE A CD2 1 ATOM 150 C CE1 . PHE A 1 80 ? 14.679 31.327 62.786 1.00 23.85 ? 73 PHE A CE1 1 ATOM 151 C CE2 . PHE A 1 80 ? 15.461 33.591 63.076 1.00 23.00 ? 73 PHE A CE2 1 ATOM 152 C CZ . PHE A 1 80 ? 14.788 32.479 63.567 1.00 23.11 ? 73 PHE A CZ 1 ATOM 153 N N . LEU A 1 81 ? 18.565 31.484 57.369 1.00 19.77 ? 74 LEU A N 1 ATOM 154 C CA . LEU A 1 81 ? 19.039 31.559 55.993 1.00 18.58 ? 74 LEU A CA 1 ATOM 155 C C . LEU A 1 81 ? 18.984 30.187 55.339 1.00 19.71 ? 74 LEU A C 1 ATOM 156 O O . LEU A 1 81 ? 18.500 30.058 54.216 1.00 20.50 ? 74 LEU A O 1 ATOM 157 C CB . LEU A 1 81 ? 20.457 32.111 55.902 1.00 19.33 ? 74 LEU A CB 1 ATOM 158 C CG . LEU A 1 81 ? 20.958 32.277 54.455 1.00 17.18 ? 74 LEU A CG 1 ATOM 159 C CD1 . LEU A 1 81 ? 20.137 33.319 53.687 1.00 17.68 ? 74 LEU A CD1 1 ATOM 160 C CD2 . LEU A 1 81 ? 22.438 32.633 54.461 1.00 20.63 ? 74 LEU A CD2 1 ATOM 161 N N . TYR A 1 82 ? 19.489 29.170 56.037 1.00 18.65 ? 75 TYR A N 1 ATOM 162 C CA . TYR A 1 82 ? 19.410 27.809 55.517 1.00 20.67 ? 75 TYR A CA 1 ATOM 163 C C . TYR A 1 82 ? 17.944 27.456 55.193 1.00 21.30 ? 75 TYR A C 1 ATOM 164 O O . TYR A 1 82 ? 17.640 26.946 54.120 1.00 21.69 ? 75 TYR A O 1 ATOM 165 C CB . TYR A 1 82 ? 19.983 26.814 56.523 1.00 21.58 ? 75 TYR A CB 1 ATOM 166 C CG . TYR A 1 82 ? 19.934 25.408 56.001 1.00 23.01 ? 75 TYR A CG 1 ATOM 167 C CD1 . TYR A 1 82 ? 20.942 24.926 55.164 1.00 23.49 ? 75 TYR A CD1 1 ATOM 168 C CD2 . TYR A 1 82 ? 18.863 24.562 56.317 1.00 25.39 ? 75 TYR A CD2 1 ATOM 169 C CE1 . TYR A 1 82 ? 20.909 23.630 54.682 1.00 23.86 ? 75 TYR A CE1 1 ATOM 170 C CE2 . TYR A 1 82 ? 18.814 23.261 55.828 1.00 25.64 ? 75 TYR A CE2 1 ATOM 171 C CZ . TYR A 1 82 ? 19.839 22.808 55.008 1.00 25.38 ? 75 TYR A CZ 1 ATOM 172 O OH . TYR A 1 82 ? 19.801 21.532 54.508 1.00 31.60 ? 75 TYR A OH 1 ATOM 173 N N . ASN A 1 83 ? 17.046 27.741 56.132 1.00 20.17 ? 76 ASN A N 1 ATOM 174 C CA . ASN A 1 83 ? 15.616 27.441 55.975 1.00 20.20 ? 76 ASN A CA 1 ATOM 175 C C . ASN A 1 83 ? 14.961 28.102 54.762 1.00 20.10 ? 76 ASN A C 1 ATOM 176 O O . ASN A 1 83 ? 14.055 27.523 54.146 1.00 20.90 ? 76 ASN A O 1 ATOM 177 C CB . ASN A 1 83 ? 14.881 27.842 57.234 1.00 22.07 ? 76 ASN A CB 1 ATOM 178 C CG . ASN A 1 83 ? 13.415 27.503 57.186 1.00 21.84 ? 76 ASN A CG 1 ATOM 179 O OD1 . ASN A 1 83 ? 12.581 28.331 56.802 1.00 23.77 ? 76 ASN A OD1 1 ATOM 180 N ND2 . ASN A 1 83 ? 13.091 26.278 57.571 1.00 24.47 ? 76 ASN A ND2 1 ATOM 181 N N . PHE A 1 84 ? 15.428 29.299 54.423 1.00 19.54 ? 77 PHE A N 1 ATOM 182 C CA . PHE A 1 84 ? 14.800 30.122 53.382 1.00 17.81 ? 77 PHE A CA 1 ATOM 183 C C . PHE A 1 84 ? 15.345 29.852 51.985 1.00 18.64 ? 77 PHE A C 1 ATOM 184 O O . PHE A 1 84 ? 14.861 30.448 51.024 1.00 18.53 ? 77 PHE A O 1 ATOM 185 C CB . PHE A 1 84 ? 15.005 31.623 53.661 1.00 18.40 ? 77 PHE A CB 1 ATOM 186 C CG . PHE A 1 84 ? 14.287 32.162 54.876 1.00 18.45 ? 77 PHE A CG 1 ATOM 187 C CD1 . PHE A 1 84 ? 13.321 31.422 55.585 1.00 19.09 ? 77 PHE A CD1 1 ATOM 188 C CD2 . PHE A 1 84 ? 14.580 33.452 55.305 1.00 18.85 ? 77 PHE A CD2 1 ATOM 189 C CE1 . PHE A 1 84 ? 12.686 31.971 56.700 1.00 20.78 ? 77 PHE A CE1 1 ATOM 190 C CE2 . PHE A 1 84 ? 13.942 34.015 56.411 1.00 18.79 ? 77 PHE A CE2 1 ATOM 191 C CZ . PHE A 1 84 ? 12.987 33.274 57.113 1.00 19.01 ? 77 PHE A CZ 1 ATOM 192 N N . THR A 1 85 ? 16.358 28.984 51.861 1.00 19.22 ? 78 THR A N 1 ATOM 193 C CA . THR A 1 85 ? 17.115 28.910 50.612 1.00 19.82 ? 78 THR A CA 1 ATOM 194 C C . THR A 1 85 ? 17.227 27.494 50.027 1.00 19.92 ? 78 THR A C 1 ATOM 195 O O . THR A 1 85 ? 18.051 27.261 49.146 1.00 20.19 ? 78 THR A O 1 ATOM 196 C CB . THR A 1 85 ? 18.541 29.488 50.795 1.00 18.85 ? 78 THR A CB 1 ATOM 197 O OG1 . THR A 1 85 ? 19.198 28.763 51.839 1.00 19.25 ? 78 THR A OG1 1 ATOM 198 C CG2 . THR A 1 85 ? 18.494 31.006 51.133 1.00 18.64 ? 78 THR A CG2 1 ATOM 199 N N . GLN A 1 86 ? 16.390 26.563 50.494 1.00 19.61 ? 79 GLN A N 1 ATOM 200 C CA . GLN A 1 86 ? 16.486 25.174 50.046 1.00 22.71 ? 79 GLN A CA 1 ATOM 201 C C . GLN A 1 86 ? 15.808 24.932 48.707 1.00 22.53 ? 79 GLN A C 1 ATOM 202 O O . GLN A 1 86 ? 16.115 23.953 48.007 1.00 23.74 ? 79 GLN A O 1 ATOM 203 C CB . GLN A 1 86 ? 15.906 24.232 51.115 1.00 23.78 ? 79 GLN A CB 1 ATOM 204 C CG . GLN A 1 86 ? 16.725 24.238 52.390 1.00 25.14 ? 79 GLN A CG 1 ATOM 205 C CD . GLN A 1 86 ? 18.201 24.104 52.076 1.00 29.57 ? 79 GLN A CD 1 ATOM 206 O OE1 . GLN A 1 86 ? 18.649 23.045 51.608 1.00 32.90 ? 79 GLN A OE1 1 ATOM 207 N NE2 . GLN A 1 86 ? 18.971 25.183 52.306 1.00 28.23 ? 79 GLN A NE2 1 ATOM 208 N N . ILE A 1 87 ? 14.839 25.787 48.392 1.00 23.15 ? 80 ILE A N 1 ATOM 209 C CA . ILE A 1 87 ? 14.069 25.664 47.154 1.00 21.73 ? 80 ILE A CA 1 ATOM 210 C C . ILE A 1 87 ? 13.896 27.070 46.586 1.00 20.31 ? 80 ILE A C 1 ATOM 211 O O . ILE A 1 87 ? 14.005 28.052 47.337 1.00 20.24 ? 80 ILE A O 1 ATOM 212 C CB . ILE A 1 87 ? 12.681 24.995 47.381 1.00 24.04 ? 80 ILE A CB 1 ATOM 213 C CG1 . ILE A 1 87 ? 11.822 25.850 48.314 1.00 23.73 ? 80 ILE A CG1 1 ATOM 214 C CG2 . ILE A 1 87 ? 12.832 23.539 47.845 1.00 25.47 ? 80 ILE A CG2 1 ATOM 215 C CD1 . ILE A 1 87 ? 10.389 25.372 48.462 1.00 24.80 ? 80 ILE A CD1 1 ATOM 216 N N . PRO A 1 88 ? 13.615 27.188 45.274 1.00 19.83 ? 81 PRO A N 1 ATOM 217 C CA . PRO A 1 88 ? 13.347 28.526 44.726 1.00 18.82 ? 81 PRO A CA 1 ATOM 218 C C . PRO A 1 88 ? 12.082 29.152 45.304 1.00 19.54 ? 81 PRO A C 1 ATOM 219 O O . PRO A 1 88 ? 11.123 28.422 45.612 1.00 20.83 ? 81 PRO A O 1 ATOM 220 C CB . PRO A 1 88 ? 13.172 28.256 43.217 1.00 20.79 ? 81 PRO A CB 1 ATOM 221 C CG . PRO A 1 88 ? 13.916 26.973 42.979 1.00 21.24 ? 81 PRO A CG 1 ATOM 222 C CD . PRO A 1 88 ? 13.650 26.158 44.217 1.00 19.58 ? 81 PRO A CD 1 ATOM 223 N N . HIS A 1 89 ? 12.085 30.484 45.457 1.00 16.83 ? 82 HIS A N 1 ATOM 224 C CA . HIS A 1 89 ? 10.893 31.222 45.859 1.00 16.79 ? 82 HIS A CA 1 ATOM 225 C C . HIS A 1 89 ? 10.563 32.330 44.892 1.00 16.90 ? 82 HIS A C 1 ATOM 226 O O . HIS A 1 89 ? 10.482 33.511 45.274 1.00 17.50 ? 82 HIS A O 1 ATOM 227 C CB . HIS A 1 89 ? 11.054 31.767 47.287 1.00 17.83 ? 82 HIS A CB 1 ATOM 228 C CG . HIS A 1 89 ? 11.260 30.677 48.319 1.00 18.31 ? 82 HIS A CG 1 ATOM 229 N ND1 . HIS A 1 89 ? 12.478 30.386 48.832 1.00 18.92 ? 82 HIS A ND1 1 ATOM 230 C CD2 . HIS A 1 89 ? 10.361 29.767 48.886 1.00 17.80 ? 82 HIS A CD2 1 ATOM 231 C CE1 . HIS A 1 89 ? 12.358 29.357 49.709 1.00 20.20 ? 82 HIS A CE1 1 ATOM 232 N NE2 . HIS A 1 89 ? 11.062 28.980 49.742 1.00 19.04 ? 82 HIS A NE2 1 ATOM 233 N N . LEU A 1 90 ? 10.341 31.955 43.631 1.00 17.46 ? 83 LEU A N 1 ATOM 234 C CA . LEU A 1 90 ? 10.050 32.926 42.580 1.00 17.01 ? 83 LEU A CA 1 ATOM 235 C C . LEU A 1 90 ? 8.696 33.568 42.843 1.00 16.67 ? 83 LEU A C 1 ATOM 236 O O . LEU A 1 90 ? 7.747 32.877 43.244 1.00 18.06 ? 83 LEU A O 1 ATOM 237 C CB . LEU A 1 90 ? 10.032 32.222 41.211 1.00 17.27 ? 83 LEU A CB 1 ATOM 238 C CG . LEU A 1 90 ? 9.851 33.118 39.960 1.00 15.13 ? 83 LEU A CG 1 ATOM 239 C CD1 . LEU A 1 90 ? 11.031 34.063 39.787 1.00 17.38 ? 83 LEU A CD1 1 ATOM 240 C CD2 . LEU A 1 90 ? 9.760 32.144 38.746 1.00 17.20 ? 83 LEU A CD2 1 ATOM 241 N N . ALA A 1 91 ? 8.602 34.886 42.646 1.00 16.55 ? 84 ALA A N 1 ATOM 242 C CA . ALA A 1 91 ? 7.330 35.579 42.843 1.00 14.88 ? 84 ALA A CA 1 ATOM 243 C C . ALA A 1 91 ? 6.215 34.929 42.009 1.00 15.87 ? 84 ALA A C 1 ATOM 244 O O . ALA A 1 91 ? 6.418 34.544 40.828 1.00 16.48 ? 84 ALA A O 1 ATOM 245 C CB . ALA A 1 91 ? 7.456 37.040 42.477 1.00 16.62 ? 84 ALA A CB 1 ATOM 246 N N . GLY A 1 92 ? 5.057 34.796 42.643 1.00 16.27 ? 85 GLY A N 1 ATOM 247 C CA . GLY A 1 92 ? 3.848 34.254 41.999 1.00 17.40 ? 85 GLY A CA 1 ATOM 248 C C . GLY A 1 92 ? 3.784 32.753 41.956 1.00 18.14 ? 85 GLY A C 1 ATOM 249 O O . GLY A 1 92 ? 2.826 32.201 41.394 1.00 22.88 ? 85 GLY A O 1 ATOM 250 N N . THR A 1 93 ? 4.776 32.065 42.534 1.00 17.60 ? 86 THR A N 1 ATOM 251 C CA . THR A 1 93 ? 4.754 30.603 42.545 1.00 18.19 ? 86 THR A CA 1 ATOM 252 C C . THR A 1 93 ? 4.219 30.053 43.877 1.00 18.21 ? 86 THR A C 1 ATOM 253 O O . THR A 1 93 ? 4.248 30.743 44.896 1.00 19.57 ? 86 THR A O 1 ATOM 254 C CB . THR A 1 93 ? 6.162 29.987 42.265 1.00 19.51 ? 86 THR A CB 1 ATOM 255 O OG1 . THR A 1 93 ? 7.069 30.321 43.322 1.00 20.13 ? 86 THR A OG1 1 ATOM 256 C CG2 . THR A 1 93 ? 6.746 30.489 40.946 1.00 20.60 ? 86 THR A CG2 1 ATOM 257 N N . GLU A 1 94 ? 3.748 28.804 43.864 1.00 19.63 ? 87 GLU A N 1 ATOM 258 C CA . GLU A 1 94 ? 3.226 28.170 45.087 1.00 20.95 ? 87 GLU A CA 1 ATOM 259 C C . GLU A 1 94 ? 4.267 28.148 46.225 1.00 22.18 ? 87 GLU A C 1 ATOM 260 O O . GLU A 1 94 ? 3.926 28.397 47.394 1.00 21.83 ? 87 GLU A O 1 ATOM 261 C CB . GLU A 1 94 ? 2.708 26.753 44.804 1.00 25.36 ? 87 GLU A CB 1 ATOM 262 C CG . GLU A 1 94 ? 2.209 26.027 46.052 1.00 28.74 ? 87 GLU A CG 1 ATOM 263 C CD . GLU A 1 94 ? 0.895 26.581 46.618 0.80 36.98 ? 87 GLU A CD 1 ATOM 264 O OE1 . GLU A 1 94 ? 0.537 26.203 47.761 0.80 38.60 ? 87 GLU A OE1 1 ATOM 265 O OE2 . GLU A 1 94 ? 0.212 27.388 45.937 0.80 38.36 ? 87 GLU A OE2 1 ATOM 266 N N A GLN A 1 95 ? 5.516 27.865 45.860 0.40 21.47 ? 88 GLN A N 1 ATOM 267 N N B GLN A 1 95 ? 5.525 27.862 45.885 0.60 21.88 ? 88 GLN A N 1 ATOM 268 C CA A GLN A 1 95 ? 6.632 27.833 46.799 0.40 22.08 ? 88 GLN A CA 1 ATOM 269 C CA B GLN A 1 95 ? 6.590 27.788 46.892 0.60 23.38 ? 88 GLN A CA 1 ATOM 270 C C A GLN A 1 95 ? 6.735 29.124 47.609 0.40 20.16 ? 88 GLN A C 1 ATOM 271 C C B GLN A 1 95 ? 6.777 29.136 47.629 0.60 20.57 ? 88 GLN A C 1 ATOM 272 O O A GLN A 1 95 ? 6.926 29.094 48.829 0.40 19.86 ? 88 GLN A O 1 ATOM 273 O O B GLN A 1 95 ? 7.056 29.160 48.835 0.60 19.73 ? 88 GLN A O 1 ATOM 274 C CB A GLN A 1 95 ? 7.942 27.587 46.048 0.40 22.19 ? 88 GLN A CB 1 ATOM 275 C CB B GLN A 1 95 ? 7.917 27.274 46.284 0.60 25.10 ? 88 GLN A CB 1 ATOM 276 C CG A GLN A 1 95 ? 8.083 26.185 45.478 0.40 24.50 ? 88 GLN A CG 1 ATOM 277 C CG B GLN A 1 95 ? 7.899 25.852 45.692 0.60 29.31 ? 88 GLN A CG 1 ATOM 278 C CD A GLN A 1 95 ? 7.224 25.931 44.252 0.40 21.50 ? 88 GLN A CD 1 ATOM 279 C CD B GLN A 1 95 ? 9.162 25.510 44.871 0.60 33.60 ? 88 GLN A CD 1 ATOM 280 O OE1 A GLN A 1 95 ? 6.779 26.854 43.576 0.40 17.32 ? 88 GLN A OE1 1 ATOM 281 O OE1 B GLN A 1 95 ? 9.740 26.376 44.192 0.60 29.34 ? 88 GLN A OE1 1 ATOM 282 N NE2 A GLN A 1 95 ? 7.011 24.655 43.946 0.40 26.55 ? 88 GLN A NE2 1 ATOM 283 N NE2 B GLN A 1 95 ? 9.594 24.235 44.929 0.60 34.50 ? 88 GLN A NE2 1 ATOM 284 N N . ASN A 1 96 ? 6.593 30.257 46.928 1.00 18.00 ? 89 ASN A N 1 ATOM 285 C CA . ASN A 1 96 ? 6.717 31.554 47.591 1.00 17.80 ? 89 ASN A CA 1 ATOM 286 C C . ASN A 1 96 ? 5.475 31.928 48.434 1.00 19.97 ? 89 ASN A C 1 ATOM 287 O O . ASN A 1 96 ? 5.586 32.662 49.431 1.00 20.76 ? 89 ASN A O 1 ATOM 288 C CB . ASN A 1 96 ? 7.052 32.659 46.602 1.00 18.30 ? 89 ASN A CB 1 ATOM 289 C CG . ASN A 1 96 ? 7.625 33.881 47.303 1.00 19.09 ? 89 ASN A CG 1 ATOM 290 O OD1 . ASN A 1 96 ? 8.356 33.747 48.302 1.00 20.05 ? 89 ASN A OD1 1 ATOM 291 N ND2 . ASN A 1 96 ? 7.312 35.066 46.799 1.00 20.28 ? 89 ASN A ND2 1 ATOM 292 N N . PHE A 1 97 ? 4.301 31.438 48.036 1.00 19.83 ? 90 PHE A N 1 ATOM 293 C CA . PHE A 1 97 ? 3.098 31.548 48.880 1.00 20.23 ? 90 PHE A CA 1 ATOM 294 C C . PHE A 1 97 ? 3.292 30.714 50.134 1.00 20.18 ? 90 PHE A C 1 ATOM 295 O O . PHE A 1 97 ? 2.953 31.164 51.229 1.00 19.57 ? 90 PHE A O 1 ATOM 296 C CB A PHE A 1 97 ? 1.852 31.091 48.094 0.65 21.49 ? 90 PHE A CB 1 ATOM 297 C CB B PHE A 1 97 ? 1.842 31.074 48.138 0.35 19.56 ? 90 PHE A CB 1 ATOM 298 C CG A PHE A 1 97 ? 0.548 31.131 48.867 0.65 22.31 ? 90 PHE A CG 1 ATOM 299 C CG B PHE A 1 97 ? 0.648 30.851 49.034 0.35 18.53 ? 90 PHE A CG 1 ATOM 300 C CD1 A PHE A 1 97 ? 0.200 32.213 49.684 0.65 21.90 ? 90 PHE A CD1 1 ATOM 301 C CD1 B PHE A 1 97 ? -0.007 31.923 49.623 0.35 18.17 ? 90 PHE A CD1 1 ATOM 302 C CD2 A PHE A 1 97 ? -0.368 30.091 48.720 0.65 26.84 ? 90 PHE A CD2 1 ATOM 303 C CD2 B PHE A 1 97 ? 0.177 29.567 49.282 0.35 17.98 ? 90 PHE A CD2 1 ATOM 304 C CE1 A PHE A 1 97 ? -1.025 32.239 50.361 0.65 23.10 ? 90 PHE A CE1 1 ATOM 305 C CE1 B PHE A 1 97 ? -1.105 31.726 50.445 0.35 18.93 ? 90 PHE A CE1 1 ATOM 306 C CE2 A PHE A 1 97 ? -1.586 30.108 49.387 0.65 28.26 ? 90 PHE A CE2 1 ATOM 307 C CE2 B PHE A 1 97 ? -0.926 29.362 50.095 0.35 18.75 ? 90 PHE A CE2 1 ATOM 308 C CZ A PHE A 1 97 ? -1.919 31.183 50.211 0.65 27.62 ? 90 PHE A CZ 1 ATOM 309 C CZ B PHE A 1 97 ? -1.567 30.441 50.679 0.35 18.36 ? 90 PHE A CZ 1 ATOM 310 N N A GLN A 1 98 ? 3.810 29.491 50.002 0.60 19.49 ? 91 GLN A N 1 ATOM 311 N N B GLN A 1 98 ? 3.833 29.504 49.969 0.40 19.44 ? 91 GLN A N 1 ATOM 312 C CA A GLN A 1 98 ? 4.009 28.682 51.209 0.60 20.82 ? 91 GLN A CA 1 ATOM 313 C CA B GLN A 1 98 ? 4.083 28.610 51.101 0.40 20.76 ? 91 GLN A CA 1 ATOM 314 C C A GLN A 1 98 ? 4.995 29.360 52.168 0.60 19.85 ? 91 GLN A C 1 ATOM 315 C C B GLN A 1 98 ? 5.054 29.227 52.121 0.40 20.44 ? 91 GLN A C 1 ATOM 316 O O A GLN A 1 98 ? 4.770 29.388 53.381 0.60 19.77 ? 91 GLN A O 1 ATOM 317 O O B GLN A 1 98 ? 4.863 29.095 53.329 0.40 22.21 ? 91 GLN A O 1 ATOM 318 C CB A GLN A 1 98 ? 4.438 27.246 50.879 0.60 22.90 ? 91 GLN A CB 1 ATOM 319 C CB B GLN A 1 98 ? 4.544 27.228 50.602 0.40 21.70 ? 91 GLN A CB 1 ATOM 320 C CG A GLN A 1 98 ? 3.324 26.405 50.254 0.60 25.77 ? 91 GLN A CG 1 ATOM 321 C CG B GLN A 1 98 ? 3.394 26.458 49.950 0.40 24.46 ? 91 GLN A CG 1 ATOM 322 C CD A GLN A 1 98 ? 2.057 26.288 51.104 0.60 31.57 ? 91 GLN A CD 1 ATOM 323 C CD B GLN A 1 98 ? 3.800 25.166 49.248 0.40 28.26 ? 91 GLN A CD 1 ATOM 324 O OE1 A GLN A 1 98 ? 0.946 26.331 50.571 0.60 35.70 ? 91 GLN A OE1 1 ATOM 325 O OE1 B GLN A 1 98 ? 4.810 25.101 48.552 0.40 32.17 ? 91 GLN A OE1 1 ATOM 326 N NE2 A GLN A 1 98 ? 2.214 26.132 52.419 0.60 31.15 ? 91 GLN A NE2 1 ATOM 327 N NE2 B GLN A 1 98 ? 2.979 24.138 49.401 0.40 32.80 ? 91 GLN A NE2 1 ATOM 328 N N . LEU A 1 99 ? 6.070 29.930 51.626 1.00 20.11 ? 92 LEU A N 1 ATOM 329 C CA . LEU A 1 99 ? 7.028 30.630 52.489 1.00 18.85 ? 92 LEU A CA 1 ATOM 330 C C . LEU A 1 99 ? 6.366 31.817 53.193 1.00 19.45 ? 92 LEU A C 1 ATOM 331 O O . LEU A 1 99 ? 6.603 32.021 54.401 1.00 19.07 ? 92 LEU A O 1 ATOM 332 C CB . LEU A 1 99 ? 8.270 31.076 51.713 1.00 17.98 ? 92 LEU A CB 1 ATOM 333 C CG . LEU A 1 99 ? 9.400 31.670 52.571 1.00 17.64 ? 92 LEU A CG 1 ATOM 334 C CD1 . LEU A 1 99 ? 9.913 30.727 53.671 1.00 21.38 ? 92 LEU A CD1 1 ATOM 335 C CD2 . LEU A 1 99 ? 10.542 32.133 51.691 1.00 17.31 ? 92 LEU A CD2 1 ATOM 336 N N . ALA A 1 100 ? 5.548 32.590 52.458 1.00 18.31 ? 93 ALA A N 1 ATOM 337 C CA . ALA A 1 100 ? 4.764 33.679 53.081 1.00 18.09 ? 93 ALA A CA 1 ATOM 338 C C . ALA A 1 100 ? 3.951 33.181 54.282 1.00 19.45 ? 93 ALA A C 1 ATOM 339 O O . ALA A 1 100 ? 3.953 33.806 55.344 1.00 20.24 ? 93 ALA A O 1 ATOM 340 C CB . ALA A 1 100 ? 3.835 34.352 52.073 1.00 18.62 ? 93 ALA A CB 1 ATOM 341 N N . LYS A 1 101 ? 3.260 32.059 54.110 1.00 18.87 ? 94 LYS A N 1 ATOM 342 C CA . LYS A 1 101 ? 2.450 31.484 55.195 1.00 19.90 ? 94 LYS A CA 1 ATOM 343 C C . LYS A 1 101 ? 3.335 31.043 56.369 1.00 21.72 ? 94 LYS A C 1 ATOM 344 O O . LYS A 1 101 ? 2.972 31.212 57.548 1.00 21.90 ? 94 LYS A O 1 ATOM 345 C CB . LYS A 1 101 ? 1.610 30.321 54.660 1.00 21.62 ? 94 LYS A CB 1 ATOM 346 C CG . LYS A 1 101 ? 0.458 30.816 53.791 1.00 22.86 ? 94 LYS A CG 1 ATOM 347 C CD . LYS A 1 101 ? -0.535 29.704 53.515 1.00 30.24 ? 94 LYS A CD 1 ATOM 348 C CE . LYS A 1 101 ? -0.138 28.942 52.264 0.50 29.00 ? 94 LYS A CE 1 ATOM 349 N NZ . LYS A 1 101 ? -1.049 27.821 51.920 0.20 27.14 ? 94 LYS A NZ 1 ATOM 350 N N . GLN A 1 102 ? 4.508 30.497 56.055 1.00 21.68 ? 95 GLN A N 1 ATOM 351 C CA . GLN A 1 102 ? 5.437 30.100 57.118 1.00 21.57 ? 95 GLN A CA 1 ATOM 352 C C . GLN A 1 102 ? 5.890 31.328 57.914 1.00 20.99 ? 95 GLN A C 1 ATOM 353 O O . GLN A 1 102 ? 5.880 31.316 59.144 1.00 20.79 ? 95 GLN A O 1 ATOM 354 C CB . GLN A 1 102 ? 6.644 29.362 56.556 1.00 22.86 ? 95 GLN A CB 1 ATOM 355 C CG . GLN A 1 102 ? 7.669 29.036 57.632 1.00 24.49 ? 95 GLN A CG 1 ATOM 356 C CD . GLN A 1 102 ? 9.032 28.735 57.068 1.00 23.16 ? 95 GLN A CD 1 ATOM 357 O OE1 . GLN A 1 102 ? 9.166 28.005 56.070 1.00 23.30 ? 95 GLN A OE1 1 ATOM 358 N NE2 . GLN A 1 102 ? 10.061 29.282 57.701 1.00 24.00 ? 95 GLN A NE2 1 ATOM 359 N N . ILE A 1 103 ? 6.283 32.387 57.205 1.00 20.06 ? 96 ILE A N 1 ATOM 360 C CA . ILE A 1 103 ? 6.745 33.614 57.873 1.00 19.22 ? 96 ILE A CA 1 ATOM 361 C C . ILE A 1 103 ? 5.619 34.213 58.734 1.00 20.28 ? 96 ILE A C 1 ATOM 362 O O . ILE A 1 103 ? 5.839 34.611 59.886 1.00 20.16 ? 96 ILE A O 1 ATOM 363 C CB . ILE A 1 103 ? 7.271 34.647 56.840 1.00 19.93 ? 96 ILE A CB 1 ATOM 364 C CG1 A ILE A 1 103 ? 8.450 34.104 56.020 0.65 22.68 ? 96 ILE A CG1 1 ATOM 365 C CG1 B ILE A 1 103 ? 8.597 34.112 56.297 0.35 20.48 ? 96 ILE A CG1 1 ATOM 366 C CG2 . ILE A 1 103 ? 7.552 36.011 57.489 1.00 20.30 ? 96 ILE A CG2 1 ATOM 367 C CD1 A ILE A 1 103 ? 9.685 33.806 56.819 0.65 23.21 ? 96 ILE A CD1 1 ATOM 368 C CD1 B ILE A 1 103 ? 9.065 34.749 55.017 0.35 19.57 ? 96 ILE A CD1 1 ATOM 369 N N . GLN A 1 104 ? 4.417 34.269 58.172 1.00 20.25 ? 97 GLN A N 1 ATOM 370 C CA . GLN A 1 104 ? 3.253 34.763 58.909 1.00 20.81 ? 97 GLN A CA 1 ATOM 371 C C . GLN A 1 104 ? 3.100 33.978 60.220 1.00 22.05 ? 97 GLN A C 1 ATOM 372 O O . GLN A 1 104 ? 2.961 34.574 61.297 1.00 22.12 ? 97 GLN A O 1 ATOM 373 C CB . GLN A 1 104 ? 1.986 34.636 58.049 1.00 20.77 ? 97 GLN A CB 1 ATOM 374 C CG . GLN A 1 104 ? 0.696 35.038 58.778 1.00 22.65 ? 97 GLN A CG 1 ATOM 375 C CD . GLN A 1 104 ? -0.550 34.787 57.950 1.00 22.41 ? 97 GLN A CD 1 ATOM 376 O OE1 . GLN A 1 104 ? -0.595 33.858 57.128 1.00 24.93 ? 97 GLN A OE1 1 ATOM 377 N NE2 . GLN A 1 104 ? -1.571 35.603 58.165 1.00 23.25 ? 97 GLN A NE2 1 ATOM 378 N N . SER A 1 105 ? 3.150 32.651 60.134 1.00 22.91 ? 98 SER A N 1 ATOM 379 C CA . SER A 1 105 ? 2.977 31.816 61.329 1.00 23.10 ? 98 SER A CA 1 ATOM 380 C C . SER A 1 105 ? 4.086 32.072 62.355 1.00 23.66 ? 98 SER A C 1 ATOM 381 O O . SER A 1 105 ? 3.822 32.185 63.564 1.00 23.07 ? 98 SER A O 1 ATOM 382 C CB . SER A 1 105 ? 2.980 30.335 60.963 1.00 23.83 ? 98 SER A CB 1 ATOM 383 O OG A SER A 1 105 ? 2.804 29.560 62.122 0.50 22.07 ? 98 SER A OG 1 ATOM 384 O OG B SER A 1 105 ? 1.736 29.947 60.396 0.50 25.65 ? 98 SER A OG 1 ATOM 385 N N . GLN A 1 106 ? 5.325 32.157 61.874 1.00 22.38 ? 99 GLN A N 1 ATOM 386 C CA . GLN A 1 106 ? 6.457 32.363 62.775 1.00 23.16 ? 99 GLN A CA 1 ATOM 387 C C . GLN A 1 106 ? 6.432 33.730 63.429 1.00 21.82 ? 99 GLN A C 1 ATOM 388 O O . GLN A 1 106 ? 6.698 33.836 64.616 1.00 23.40 ? 99 GLN A O 1 ATOM 389 C CB . GLN A 1 106 ? 7.784 32.107 62.069 1.00 22.44 ? 99 GLN A CB 1 ATOM 390 C CG . GLN A 1 106 ? 7.956 30.633 61.746 1.00 23.97 ? 99 GLN A CG 1 ATOM 391 C CD . GLN A 1 106 ? 9.307 30.334 61.154 1.00 26.26 ? 99 GLN A CD 1 ATOM 392 O OE1 . GLN A 1 106 ? 9.633 30.825 60.091 1.00 27.14 ? 99 GLN A OE1 1 ATOM 393 N NE2 . GLN A 1 106 ? 10.096 29.518 61.842 1.00 35.78 ? 99 GLN A NE2 1 ATOM 394 N N . TRP A 1 107 ? 6.119 34.781 62.673 1.00 21.67 ? 100 TRP A N 1 ATOM 395 C CA . TRP A 1 107 ? 6.005 36.111 63.279 1.00 20.54 ? 100 TRP A CA 1 ATOM 396 C C . TRP A 1 107 ? 4.957 36.174 64.365 1.00 22.68 ? 100 TRP A C 1 ATOM 397 O O . TRP A 1 107 ? 5.152 36.867 65.368 1.00 23.57 ? 100 TRP A O 1 ATOM 398 C CB . TRP A 1 107 ? 5.728 37.160 62.218 1.00 20.44 ? 100 TRP A CB 1 ATOM 399 C CG . TRP A 1 107 ? 6.940 37.471 61.397 1.00 19.44 ? 100 TRP A CG 1 ATOM 400 C CD1 . TRP A 1 107 ? 8.188 36.829 61.419 1.00 20.33 ? 100 TRP A CD1 1 ATOM 401 C CD2 . TRP A 1 107 ? 7.043 38.483 60.363 1.00 18.06 ? 100 TRP A CD2 1 ATOM 402 N NE1 . TRP A 1 107 ? 9.035 37.392 60.506 1.00 20.27 ? 100 TRP A NE1 1 ATOM 403 C CE2 . TRP A 1 107 ? 8.403 38.379 59.819 1.00 19.96 ? 100 TRP A CE2 1 ATOM 404 C CE3 . TRP A 1 107 ? 6.158 39.438 59.828 1.00 17.82 ? 100 TRP A CE3 1 ATOM 405 C CZ2 . TRP A 1 107 ? 8.851 39.213 58.800 1.00 20.47 ? 100 TRP A CZ2 1 ATOM 406 C CZ3 . TRP A 1 107 ? 6.619 40.266 58.799 1.00 19.51 ? 100 TRP A CZ3 1 ATOM 407 C CH2 . TRP A 1 107 ? 7.940 40.169 58.312 1.00 19.52 ? 100 TRP A CH2 1 ATOM 408 N N . LYS A 1 108 ? 3.843 35.457 64.185 1.00 24.77 ? 101 LYS A N 1 ATOM 409 C CA . LYS A 1 108 ? 2.819 35.345 65.247 1.00 26.66 ? 101 LYS A CA 1 ATOM 410 C C . LYS A 1 108 ? 3.401 34.650 66.488 1.00 25.83 ? 101 LYS A C 1 ATOM 411 O O . LYS A 1 108 ? 3.268 35.161 67.612 1.00 26.90 ? 101 LYS A O 1 ATOM 412 C CB . LYS A 1 108 ? 1.578 34.575 64.770 1.00 29.38 ? 101 LYS A CB 1 ATOM 413 C CG . LYS A 1 108 ? 0.762 35.299 63.734 1.00 33.24 ? 101 LYS A CG 1 ATOM 414 C CD . LYS A 1 108 ? -0.336 34.426 63.157 1.00 39.92 ? 101 LYS A CD 1 ATOM 415 C CE . LYS A 1 108 ? -1.257 35.295 62.314 1.00 39.58 ? 101 LYS A CE 1 ATOM 416 N NZ . LYS A 1 108 ? -2.531 34.591 62.024 1.00 47.97 ? 101 LYS A NZ 1 ATOM 417 N N A GLU A 1 109 ? 4.022 33.489 66.261 0.60 25.94 ? 102 GLU A N 1 ATOM 418 N N B GLU A 1 109 ? 4.047 33.506 66.290 0.40 25.64 ? 102 GLU A N 1 ATOM 419 C CA A GLU A 1 109 ? 4.730 32.712 67.291 0.60 27.07 ? 102 GLU A CA 1 ATOM 420 C CA B GLU A 1 109 ? 4.653 32.770 67.400 0.40 25.70 ? 102 GLU A CA 1 ATOM 421 C C A GLU A 1 109 ? 5.684 33.620 68.074 0.60 26.47 ? 102 GLU A C 1 ATOM 422 C C B GLU A 1 109 ? 5.764 33.568 68.092 0.40 25.98 ? 102 GLU A C 1 ATOM 423 O O A GLU A 1 109 ? 5.715 33.590 69.313 0.60 26.50 ? 102 GLU A O 1 ATOM 424 O O B GLU A 1 109 ? 5.984 33.410 69.298 0.40 26.76 ? 102 GLU A O 1 ATOM 425 C CB A GLU A 1 109 ? 5.547 31.572 66.651 0.60 29.41 ? 102 GLU A CB 1 ATOM 426 C CB B GLU A 1 109 ? 5.184 31.417 66.931 0.40 26.37 ? 102 GLU A CB 1 ATOM 427 C CG A GLU A 1 109 ? 4.770 30.394 66.069 0.60 35.94 ? 102 GLU A CG 1 ATOM 428 C CG B GLU A 1 109 ? 6.065 30.723 67.957 0.40 28.65 ? 102 GLU A CG 1 ATOM 429 C CD A GLU A 1 109 ? 5.635 29.466 65.205 0.60 39.07 ? 102 GLU A CD 1 ATOM 430 C CD B GLU A 1 109 ? 5.294 30.295 69.189 0.40 33.46 ? 102 GLU A CD 1 ATOM 431 O OE1 A GLU A 1 109 ? 5.120 28.933 64.192 0.60 36.36 ? 102 GLU A OE1 1 ATOM 432 O OE1 B GLU A 1 109 ? 4.052 30.167 69.106 0.40 40.44 ? 102 GLU A OE1 1 ATOM 433 O OE2 A GLU A 1 109 ? 6.832 29.267 65.522 0.60 36.31 ? 102 GLU A OE2 1 ATOM 434 O OE2 B GLU A 1 109 ? 5.931 30.089 70.243 0.40 37.64 ? 102 GLU A OE2 1 ATOM 435 N N . PHE A 1 110 ? 6.441 34.431 67.330 1.00 25.54 ? 103 PHE A N 1 ATOM 436 C CA . PHE A 1 110 ? 7.492 35.307 67.874 1.00 24.93 ? 103 PHE A CA 1 ATOM 437 C C . PHE A 1 110 ? 6.913 36.394 68.780 1.00 24.77 ? 103 PHE A C 1 ATOM 438 O O . PHE A 1 110 ? 7.624 36.960 69.599 1.00 28.23 ? 103 PHE A O 1 ATOM 439 C CB . PHE A 1 110 ? 8.306 35.986 66.752 1.00 24.98 ? 103 PHE A CB 1 ATOM 440 C CG . PHE A 1 110 ? 9.226 35.059 65.970 1.00 24.34 ? 103 PHE A CG 1 ATOM 441 C CD1 . PHE A 1 110 ? 9.538 33.767 66.406 1.00 25.86 ? 103 PHE A CD1 1 ATOM 442 C CD2 . PHE A 1 110 ? 9.802 35.508 64.775 1.00 25.29 ? 103 PHE A CD2 1 ATOM 443 C CE1 . PHE A 1 110 ? 10.388 32.943 65.652 1.00 28.60 ? 103 PHE A CE1 1 ATOM 444 C CE2 . PHE A 1 110 ? 10.656 34.690 64.021 1.00 23.64 ? 103 PHE A CE2 1 ATOM 445 C CZ . PHE A 1 110 ? 10.949 33.402 64.461 1.00 27.43 ? 103 PHE A CZ 1 ATOM 446 N N . GLY A 1 111 ? 5.635 36.711 68.607 1.00 25.03 ? 104 GLY A N 1 ATOM 447 C CA . GLY A 1 111 ? 4.940 37.588 69.545 1.00 24.78 ? 104 GLY A CA 1 ATOM 448 C C . GLY A 1 111 ? 4.302 38.836 68.969 0.90 24.42 ? 104 GLY A C 1 ATOM 449 O O . GLY A 1 111 ? 3.770 39.657 69.724 1.00 25.43 ? 104 GLY A O 1 ATOM 450 N N . LEU A 1 112 ? 4.315 38.997 67.649 1.00 24.23 ? 105 LEU A N 1 ATOM 451 C CA . LEU A 1 112 ? 3.728 40.217 67.070 1.00 21.94 ? 105 LEU A CA 1 ATOM 452 C C . LEU A 1 112 ? 2.231 40.283 67.346 1.00 24.00 ? 105 LEU A C 1 ATOM 453 O O . LEU A 1 112 ? 1.578 39.250 67.528 1.00 26.79 ? 105 LEU A O 1 ATOM 454 C CB . LEU A 1 112 ? 4.004 40.318 65.560 1.00 21.70 ? 105 LEU A CB 1 ATOM 455 C CG . LEU A 1 112 ? 5.473 40.454 65.129 1.00 21.06 ? 105 LEU A CG 1 ATOM 456 C CD1 . LEU A 1 112 ? 5.548 40.854 63.660 1.00 23.09 ? 105 LEU A CD1 1 ATOM 457 C CD2 . LEU A 1 112 ? 6.191 41.483 66.017 1.00 22.70 ? 105 LEU A CD2 1 ATOM 458 N N . ASP A 1 113 ? 1.686 41.495 67.408 1.00 23.28 ? 106 ASP A N 1 ATOM 459 C CA . ASP A 1 113 ? 0.278 41.671 67.744 1.00 25.48 ? 106 ASP A CA 1 ATOM 460 C C . ASP A 1 113 ? -0.683 41.181 66.665 1.00 25.09 ? 106 ASP A C 1 ATOM 461 O O . ASP A 1 113 ? -1.719 40.578 66.963 1.00 26.99 ? 106 ASP A O 1 ATOM 462 C CB . ASP A 1 113 ? -0.007 43.132 68.084 1.00 25.39 ? 106 ASP A CB 1 ATOM 463 C CG . ASP A 1 113 ? 0.700 43.570 69.336 1.00 24.43 ? 106 ASP A CG 1 ATOM 464 O OD1 . ASP A 1 113 ? 0.448 42.957 70.402 1.00 28.01 ? 106 ASP A OD1 1 ATOM 465 O OD2 . ASP A 1 113 ? 1.508 44.518 69.250 1.00 26.21 ? 106 ASP A OD2 1 ATOM 466 N N . SER A 1 114 ? -0.343 41.472 65.422 1.00 23.82 ? 107 SER A N 1 ATOM 467 C CA . SER A 1 114 ? -1.118 41.010 64.287 1.00 23.68 ? 107 SER A CA 1 ATOM 468 C C . SER A 1 114 ? -0.141 40.686 63.169 1.00 21.21 ? 107 SER A C 1 ATOM 469 O O . SER A 1 114 ? 0.906 41.335 63.022 1.00 20.96 ? 107 SER A O 1 ATOM 470 C CB . SER A 1 114 ? -2.149 42.076 63.872 1.00 26.43 ? 107 SER A CB 1 ATOM 471 O OG A SER A 1 114 ? -1.532 43.258 63.418 0.50 21.40 ? 107 SER A OG 1 ATOM 472 O OG B SER A 1 114 ? -2.421 42.043 62.486 0.50 32.80 ? 107 SER A OG 1 ATOM 473 N N . VAL A 1 115 ? -0.449 39.651 62.394 1.00 21.61 ? 108 VAL A N 1 ATOM 474 C CA . VAL A 1 115 ? 0.357 39.358 61.214 1.00 21.00 ? 108 VAL A CA 1 ATOM 475 C C . VAL A 1 115 ? -0.598 38.918 60.106 1.00 21.67 ? 108 VAL A C 1 ATOM 476 O O . VAL A 1 115 ? -1.264 37.875 60.228 1.00 22.87 ? 108 VAL A O 1 ATOM 477 C CB . VAL A 1 115 ? 1.422 38.256 61.444 1.00 21.45 ? 108 VAL A CB 1 ATOM 478 C CG1 . VAL A 1 115 ? 2.362 38.203 60.235 1.00 21.05 ? 108 VAL A CG1 1 ATOM 479 C CG2 . VAL A 1 115 ? 2.226 38.515 62.721 1.00 19.94 ? 108 VAL A CG2 1 ATOM 480 N N . GLU A 1 116 ? -0.663 39.708 59.036 1.00 20.67 ? 109 GLU A N 1 ATOM 481 C CA . GLU A 1 116 ? -1.601 39.443 57.950 1.00 22.07 ? 109 GLU A CA 1 ATOM 482 C C . GLU A 1 116 ? -0.888 39.308 56.609 1.00 20.35 ? 109 GLU A C 1 ATOM 483 O O . GLU A 1 116 ? 0.222 39.826 56.421 1.00 23.56 ? 109 GLU A O 1 ATOM 484 C CB . GLU A 1 116 ? -2.643 40.585 57.855 1.00 27.67 ? 109 GLU A CB 1 ATOM 485 C CG . GLU A 1 116 ? -3.497 40.787 59.108 1.00 33.39 ? 109 GLU A CG 1 ATOM 486 C CD . GLU A 1 116 ? -4.384 39.594 59.437 0.80 40.55 ? 109 GLU A CD 1 ATOM 487 O OE1 . GLU A 1 116 ? -4.860 38.907 58.507 1.00 44.79 ? 109 GLU A OE1 1 ATOM 488 O OE2 . GLU A 1 116 ? -4.621 39.339 60.638 0.80 46.97 ? 109 GLU A OE2 1 ATOM 489 N N . LEU A 1 117 ? -1.515 38.603 55.671 1.00 19.63 ? 110 LEU A N 1 ATOM 490 C CA . LEU A 1 117 ? -1.071 38.660 54.275 1.00 18.88 ? 110 LEU A CA 1 ATOM 491 C C . LEU A 1 117 ? -1.860 39.745 53.557 1.00 20.96 ? 110 LEU A C 1 ATOM 492 O O . LEU A 1 117 ? -3.089 39.863 53.757 1.00 23.78 ? 110 LEU A O 1 ATOM 493 C CB . LEU A 1 117 ? -1.310 37.329 53.569 1.00 21.99 ? 110 LEU A CB 1 ATOM 494 C CG . LEU A 1 117 ? -0.607 36.101 54.126 1.00 23.81 ? 110 LEU A CG 1 ATOM 495 C CD1 . LEU A 1 117 ? -0.873 34.908 53.216 1.00 27.06 ? 110 LEU A CD1 1 ATOM 496 C CD2 . LEU A 1 117 ? 0.882 36.321 54.258 1.00 24.98 ? 110 LEU A CD2 1 ATOM 497 N N . ALA A 1 118 ? -1.156 40.548 52.764 1.00 18.94 ? 111 ALA A N 1 ATOM 498 C CA . ALA A 1 118 ? -1.758 41.551 51.886 1.00 17.59 ? 111 ALA A CA 1 ATOM 499 C C . ALA A 1 118 ? -1.451 41.069 50.492 1.00 19.05 ? 111 ALA A C 1 ATOM 500 O O . ALA A 1 118 ? -0.265 41.027 50.107 1.00 20.51 ? 111 ALA A O 1 ATOM 501 C CB . ALA A 1 118 ? -1.110 42.923 52.125 1.00 20.10 ? 111 ALA A CB 1 ATOM 502 N N . HIS A 1 119 ? -2.491 40.706 49.732 1.00 17.55 ? 112 HIS A N 1 ATOM 503 C CA . HIS A 1 119 ? -2.270 40.154 48.370 1.00 16.86 ? 112 HIS A CA 1 ATOM 504 C C . HIS A 1 119 ? -2.718 41.117 47.302 1.00 16.86 ? 112 HIS A C 1 ATOM 505 O O . HIS A 1 119 ? -3.600 41.942 47.545 1.00 17.39 ? 112 HIS A O 1 ATOM 506 C CB . HIS A 1 119 ? -2.938 38.785 48.183 1.00 18.80 ? 112 HIS A CB 1 ATOM 507 C CG . HIS A 1 119 ? -4.445 38.827 48.217 1.00 21.66 ? 112 HIS A CG 1 ATOM 508 N ND1 . HIS A 1 119 ? -5.159 38.565 49.337 1.00 25.23 ? 112 HIS A ND1 1 ATOM 509 C CD2 . HIS A 1 119 ? -5.370 39.128 47.220 1.00 22.49 ? 112 HIS A CD2 1 ATOM 510 C CE1 . HIS A 1 119 ? -6.482 38.677 49.063 1.00 26.40 ? 112 HIS A CE1 1 ATOM 511 N NE2 . HIS A 1 119 ? -6.609 39.027 47.767 1.00 24.56 ? 112 HIS A NE2 1 ATOM 512 N N . TYR A 1 120 ? -2.102 41.020 46.124 1.00 16.81 ? 113 TYR A N 1 ATOM 513 C CA . TYR A 1 120 ? -2.408 41.870 44.958 1.00 16.29 ? 113 TYR A CA 1 ATOM 514 C C . TYR A 1 120 ? -2.291 40.994 43.735 1.00 15.76 ? 113 TYR A C 1 ATOM 515 O O . TYR A 1 120 ? -1.573 39.984 43.761 1.00 17.50 ? 113 TYR A O 1 ATOM 516 C CB . TYR A 1 120 ? -1.435 43.080 44.860 1.00 15.68 ? 113 TYR A CB 1 ATOM 517 C CG . TYR A 1 120 ? -1.449 43.873 46.149 1.00 16.03 ? 113 TYR A CG 1 ATOM 518 C CD1 . TYR A 1 120 ? -2.457 44.815 46.408 1.00 16.27 ? 113 TYR A CD1 1 ATOM 519 C CD2 . TYR A 1 120 ? -0.537 43.580 47.167 1.00 16.84 ? 113 TYR A CD2 1 ATOM 520 C CE1 . TYR A 1 120 ? -2.503 45.476 47.638 1.00 18.51 ? 113 TYR A CE1 1 ATOM 521 C CE2 . TYR A 1 120 ? -0.579 44.226 48.391 1.00 16.27 ? 113 TYR A CE2 1 ATOM 522 C CZ . TYR A 1 120 ? -1.557 45.178 48.620 1.00 17.94 ? 113 TYR A CZ 1 ATOM 523 O OH . TYR A 1 120 ? -1.609 45.820 49.835 1.00 18.94 ? 113 TYR A OH 1 ATOM 524 N N . ASP A 1 121 ? -2.954 41.386 42.654 1.00 15.84 ? 114 ASP A N 1 ATOM 525 C CA . ASP A 1 121 ? -2.838 40.655 41.374 1.00 16.21 ? 114 ASP A CA 1 ATOM 526 C C . ASP A 1 121 ? -2.146 41.555 40.377 1.00 16.66 ? 114 ASP A C 1 ATOM 527 O O . ASP A 1 121 ? -2.760 42.523 39.885 1.00 17.73 ? 114 ASP A O 1 ATOM 528 C CB . ASP A 1 121 ? -4.227 40.211 40.874 1.00 17.38 ? 114 ASP A CB 1 ATOM 529 C CG . ASP A 1 121 ? -4.899 39.265 41.852 1.00 19.27 ? 114 ASP A CG 1 ATOM 530 O OD1 . ASP A 1 121 ? -4.239 38.291 42.252 1.00 20.67 ? 114 ASP A OD1 1 ATOM 531 O OD2 . ASP A 1 121 ? -6.062 39.492 42.228 1.00 24.03 ? 114 ASP A OD2 1 ATOM 532 N N . VAL A 1 122 ? -0.860 41.262 40.117 1.00 16.52 ? 115 VAL A N 1 ATOM 533 C CA . VAL A 1 122 ? 0.010 42.161 39.352 1.00 16.24 ? 115 VAL A CA 1 ATOM 534 C C . VAL A 1 122 ? 0.580 41.488 38.108 1.00 16.16 ? 115 VAL A C 1 ATOM 535 O O . VAL A 1 122 ? 0.596 40.256 38.016 1.00 16.19 ? 115 VAL A O 1 ATOM 536 C CB . VAL A 1 122 ? 1.189 42.683 40.221 1.00 14.40 ? 115 VAL A CB 1 ATOM 537 C CG1 . VAL A 1 122 ? 0.647 43.412 41.470 1.00 15.47 ? 115 VAL A CG1 1 ATOM 538 C CG2 . VAL A 1 122 ? 2.129 41.536 40.628 1.00 14.73 ? 115 VAL A CG2 1 ATOM 539 N N . LEU A 1 123 ? 1.065 42.290 37.159 1.00 14.19 ? 116 LEU A N 1 ATOM 540 C CA . LEU A 1 123 ? 1.642 41.715 35.954 1.00 14.51 ? 116 LEU A CA 1 ATOM 541 C C . LEU A 1 123 ? 3.023 41.144 36.277 1.00 15.94 ? 116 LEU A C 1 ATOM 542 O O . LEU A 1 123 ? 3.897 41.888 36.715 1.00 16.88 ? 116 LEU A O 1 ATOM 543 C CB . LEU A 1 123 ? 1.782 42.783 34.870 1.00 13.79 ? 116 LEU A CB 1 ATOM 544 C CG . LEU A 1 123 ? 2.065 42.193 33.469 1.00 15.40 ? 116 LEU A CG 1 ATOM 545 C CD1 . LEU A 1 123 ? 0.844 41.450 32.919 1.00 18.83 ? 116 LEU A CD1 1 ATOM 546 C CD2 . LEU A 1 123 ? 2.528 43.272 32.507 1.00 19.37 ? 116 LEU A CD2 1 ATOM 547 N N . LEU A 1 124 ? 3.209 39.838 36.053 1.00 16.07 ? 117 LEU A N 1 ATOM 548 C CA . LEU A 1 124 ? 4.528 39.186 36.165 1.00 16.11 ? 117 LEU A CA 1 ATOM 549 C C . LEU A 1 124 ? 4.891 38.642 34.786 1.00 16.60 ? 117 LEU A C 1 ATOM 550 O O . LEU A 1 124 ? 4.138 38.855 33.832 1.00 17.09 ? 117 LEU A O 1 ATOM 551 C CB . LEU A 1 124 ? 4.523 38.083 37.237 1.00 16.45 ? 117 LEU A CB 1 ATOM 552 C CG . LEU A 1 124 ? 4.203 38.542 38.672 1.00 14.46 ? 117 LEU A CG 1 ATOM 553 C CD1 . LEU A 1 124 ? 4.343 37.364 39.660 1.00 16.01 ? 117 LEU A CD1 1 ATOM 554 C CD2 . LEU A 1 124 ? 5.069 39.732 39.126 1.00 15.54 ? 117 LEU A CD2 1 ATOM 555 N N . SER A 1 125 ? 6.029 37.960 34.674 1.00 15.57 ? 118 SER A N 1 ATOM 556 C CA . SER A 1 125 ? 6.554 37.524 33.376 1.00 17.44 ? 118 SER A CA 1 ATOM 557 C C . SER A 1 125 ? 7.326 36.241 33.606 1.00 18.11 ? 118 SER A C 1 ATOM 558 O O . SER A 1 125 ? 8.115 36.156 34.558 1.00 18.95 ? 118 SER A O 1 ATOM 559 C CB . SER A 1 125 ? 7.507 38.597 32.827 1.00 17.61 ? 118 SER A CB 1 ATOM 560 O OG . SER A 1 125 ? 8.260 38.096 31.723 1.00 18.22 ? 118 SER A OG 1 ATOM 561 N N . TYR A 1 126 ? 7.094 35.241 32.751 1.00 19.62 ? 119 TYR A N 1 ATOM 562 C CA . TYR A 1 126 ? 7.767 33.958 32.897 1.00 17.69 ? 119 TYR A CA 1 ATOM 563 C C . TYR A 1 126 ? 8.122 33.362 31.549 1.00 19.84 ? 119 TYR A C 1 ATOM 564 O O . TYR A 1 126 ? 7.382 33.538 30.584 1.00 20.58 ? 119 TYR A O 1 ATOM 565 C CB . TYR A 1 126 ? 6.838 32.960 33.572 1.00 18.43 ? 119 TYR A CB 1 ATOM 566 C CG . TYR A 1 126 ? 6.320 33.334 34.933 1.00 18.18 ? 119 TYR A CG 1 ATOM 567 C CD1 . TYR A 1 126 ? 7.143 33.249 36.068 1.00 19.33 ? 119 TYR A CD1 1 ATOM 568 C CD2 . TYR A 1 126 ? 4.983 33.736 35.101 1.00 19.54 ? 119 TYR A CD2 1 ATOM 569 C CE1 . TYR A 1 126 ? 6.645 33.559 37.331 1.00 20.31 ? 119 TYR A CE1 1 ATOM 570 C CE2 . TYR A 1 126 ? 4.482 34.039 36.357 1.00 22.12 ? 119 TYR A CE2 1 ATOM 571 C CZ . TYR A 1 126 ? 5.323 33.942 37.464 1.00 20.76 ? 119 TYR A CZ 1 ATOM 572 O OH . TYR A 1 126 ? 4.831 34.229 38.708 1.00 19.65 ? 119 TYR A OH 1 ATOM 573 N N . PRO A 1 127 ? 9.218 32.592 31.488 1.00 19.14 ? 120 PRO A N 1 ATOM 574 C CA . PRO A 1 127 ? 9.465 31.853 30.249 1.00 21.23 ? 120 PRO A CA 1 ATOM 575 C C . PRO A 1 127 ? 8.372 30.827 29.974 1.00 22.60 ? 120 PRO A C 1 ATOM 576 O O . PRO A 1 127 ? 7.653 30.406 30.887 1.00 24.66 ? 120 PRO A O 1 ATOM 577 C CB . PRO A 1 127 ? 10.794 31.124 30.509 1.00 22.86 ? 120 PRO A CB 1 ATOM 578 C CG . PRO A 1 127 ? 11.415 31.823 31.672 1.00 21.48 ? 120 PRO A CG 1 ATOM 579 C CD . PRO A 1 127 ? 10.288 32.398 32.490 1.00 19.46 ? 120 PRO A CD 1 ATOM 580 N N . ASN A 1 128 ? 8.252 30.434 28.714 1.00 23.35 ? 121 ASN A N 1 ATOM 581 C CA . ASN A 1 128 ? 7.354 29.365 28.340 1.00 26.57 ? 121 ASN A CA 1 ATOM 582 C C . ASN A 1 128 ? 8.084 28.034 28.547 1.00 28.49 ? 121 ASN A C 1 ATOM 583 O O . ASN A 1 128 ? 9.105 27.779 27.902 1.00 27.51 ? 121 ASN A O 1 ATOM 584 C CB . ASN A 1 128 ? 6.920 29.554 26.891 1.00 26.83 ? 121 ASN A CB 1 ATOM 585 C CG . ASN A 1 128 ? 5.933 28.499 26.433 1.00 30.72 ? 121 ASN A CG 1 ATOM 586 O OD1 . ASN A 1 128 ? 5.984 27.349 26.869 1.00 34.53 ? 121 ASN A OD1 1 ATOM 587 N ND2 . ASN A 1 128 ? 5.031 28.881 25.547 1.00 32.79 ? 121 ASN A ND2 1 ATOM 588 N N . LYS A 1 129 ? 7.566 27.214 29.468 1.00 30.43 ? 122 LYS A N 1 ATOM 589 C CA . LYS A 1 129 ? 8.145 25.898 29.814 1.00 33.39 ? 122 LYS A CA 1 ATOM 590 C C . LYS A 1 129 ? 8.383 24.967 28.611 1.00 34.52 ? 122 LYS A C 1 ATOM 591 O O . LYS A 1 129 ? 9.343 24.180 28.601 1.00 38.07 ? 122 LYS A O 1 ATOM 592 C CB . LYS A 1 129 ? 7.267 25.184 30.863 1.00 37.96 ? 122 LYS A CB 1 ATOM 593 C CG . LYS A 1 129 ? 7.530 25.582 32.312 1.00 42.07 ? 122 LYS A CG 1 ATOM 594 C CD . LYS A 1 129 ? 8.512 24.638 32.997 0.40 41.37 ? 122 LYS A CD 1 ATOM 595 C CE . LYS A 1 129 ? 7.835 23.367 33.491 0.40 39.81 ? 122 LYS A CE 1 ATOM 596 N NZ . LYS A 1 129 ? 8.790 22.451 34.177 0.40 40.34 ? 122 LYS A NZ 1 ATOM 597 N N . THR A 1 130 ? 7.529 25.060 27.593 1.00 31.83 ? 123 THR A N 1 ATOM 598 C CA . THR A 1 130 ? 7.627 24.145 26.447 1.00 35.03 ? 123 THR A CA 1 ATOM 599 C C . THR A 1 130 ? 8.149 24.781 25.142 1.00 35.08 ? 123 THR A C 1 ATOM 600 O O . THR A 1 130 ? 8.178 24.135 24.094 1.00 40.08 ? 123 THR A O 1 ATOM 601 C CB . THR A 1 130 ? 6.295 23.410 26.201 1.00 41.31 ? 123 THR A CB 1 ATOM 602 O OG1 . THR A 1 130 ? 5.273 24.372 25.921 1.00 40.55 ? 123 THR A OG1 1 ATOM 603 C CG2 . THR A 1 130 ? 5.906 22.599 27.433 1.00 42.57 ? 123 THR A CG2 1 ATOM 604 N N . HIS A 1 131 ? 8.599 26.030 25.226 1.00 33.41 ? 124 HIS A N 1 ATOM 605 C CA . HIS A 1 131 ? 9.081 26.780 24.078 1.00 31.59 ? 124 HIS A CA 1 ATOM 606 C C . HIS A 1 131 ? 10.203 27.666 24.568 1.00 30.93 ? 124 HIS A C 1 ATOM 607 O O . HIS A 1 131 ? 10.004 28.860 24.755 1.00 30.10 ? 124 HIS A O 1 ATOM 608 C CB . HIS A 1 131 ? 7.927 27.620 23.535 1.00 32.97 ? 124 HIS A CB 1 ATOM 609 C CG . HIS A 1 131 ? 8.083 28.052 22.099 1.00 41.73 ? 124 HIS A CG 1 ATOM 610 N ND1 . HIS A 1 131 ? 9.022 27.542 21.277 0.70 46.71 ? 124 HIS A ND1 1 ATOM 611 C CD2 . HIS A 1 131 ? 7.341 28.955 21.336 1.00 47.30 ? 124 HIS A CD2 1 ATOM 612 C CE1 . HIS A 1 131 ? 8.905 28.106 20.057 0.70 48.99 ? 124 HIS A CE1 1 ATOM 613 N NE2 . HIS A 1 131 ? 7.876 28.970 20.094 0.70 47.88 ? 124 HIS A NE2 1 ATOM 614 N N . PRO A 1 132 ? 11.398 27.085 24.809 1.00 29.68 ? 125 PRO A N 1 ATOM 615 C CA . PRO A 1 132 ? 12.452 27.799 25.562 1.00 28.35 ? 125 PRO A CA 1 ATOM 616 C C . PRO A 1 132 ? 13.054 28.985 24.809 1.00 26.88 ? 125 PRO A C 1 ATOM 617 O O . PRO A 1 132 ? 13.090 28.997 23.579 1.00 30.99 ? 125 PRO A O 1 ATOM 618 C CB . PRO A 1 132 ? 13.527 26.720 25.803 1.00 35.62 ? 125 PRO A CB 1 ATOM 619 C CG . PRO A 1 132 ? 12.879 25.417 25.449 1.00 37.06 ? 125 PRO A CG 1 ATOM 620 C CD . PRO A 1 132 ? 11.829 25.730 24.427 1.00 34.11 ? 125 PRO A CD 1 ATOM 621 N N . ASN A 1 133 ? 13.490 29.991 25.567 1.00 25.01 ? 126 ASN A N 1 ATOM 622 C CA . ASN A 1 133 ? 14.199 31.146 25.005 1.00 24.41 ? 126 ASN A CA 1 ATOM 623 C C . ASN A 1 133 ? 15.631 30.766 24.670 1.00 26.60 ? 126 ASN A C 1 ATOM 624 O O . ASN A 1 133 ? 16.279 30.050 25.447 1.00 25.59 ? 126 ASN A O 1 ATOM 625 C CB . ASN A 1 133 ? 14.201 32.298 26.015 1.00 22.32 ? 126 ASN A CB 1 ATOM 626 C CG . ASN A 1 133 ? 12.802 32.744 26.375 1.00 23.50 ? 126 ASN A CG 1 ATOM 627 O OD1 . ASN A 1 133 ? 11.902 32.699 25.535 1.00 23.58 ? 126 ASN A OD1 1 ATOM 628 N ND2 . ASN A 1 133 ? 12.603 33.163 27.618 1.00 21.47 ? 126 ASN A ND2 1 ATOM 629 N N . TYR A 1 134 ? 16.117 31.222 23.514 1.00 25.25 ? 127 TYR A N 1 ATOM 630 C CA . TYR A 1 134 ? 17.535 31.044 23.161 1.00 24.69 ? 127 TYR A CA 1 ATOM 631 C C . TYR A 1 134 ? 17.931 31.971 22.022 1.00 26.54 ? 127 TYR A C 1 ATOM 632 O O . TYR A 1 134 ? 17.065 32.580 21.369 1.00 26.24 ? 127 TYR A O 1 ATOM 633 C CB . TYR A 1 134 ? 17.867 29.568 22.822 1.00 26.64 ? 127 TYR A CB 1 ATOM 634 C CG . TYR A 1 134 ? 17.327 29.061 21.497 1.00 28.33 ? 127 TYR A CG 1 ATOM 635 C CD1 . TYR A 1 134 ? 18.187 28.845 20.416 1.00 29.30 ? 127 TYR A CD1 1 ATOM 636 C CD2 . TYR A 1 134 ? 15.967 28.786 21.323 1.00 29.78 ? 127 TYR A CD2 1 ATOM 637 C CE1 . TYR A 1 134 ? 17.716 28.368 19.204 1.00 30.79 ? 127 TYR A CE1 1 ATOM 638 C CE2 . TYR A 1 134 ? 15.484 28.313 20.106 1.00 32.21 ? 127 TYR A CE2 1 ATOM 639 C CZ . TYR A 1 134 ? 16.363 28.108 19.051 1.00 30.46 ? 127 TYR A CZ 1 ATOM 640 O OH . TYR A 1 134 ? 15.906 27.651 17.840 1.00 33.97 ? 127 TYR A OH 1 ATOM 641 N N . ILE A 1 135 ? 19.243 32.080 21.799 1.00 24.67 ? 128 ILE A N 1 ATOM 642 C CA . ILE A 1 135 ? 19.811 32.909 20.732 1.00 25.81 ? 128 ILE A CA 1 ATOM 643 C C . ILE A 1 135 ? 20.637 31.995 19.843 1.00 26.35 ? 128 ILE A C 1 ATOM 644 O O . ILE A 1 135 ? 21.260 31.053 20.340 1.00 26.68 ? 128 ILE A O 1 ATOM 645 C CB . ILE A 1 135 ? 20.703 34.040 21.302 1.00 24.83 ? 128 ILE A CB 1 ATOM 646 C CG1 . ILE A 1 135 ? 19.877 34.984 22.198 1.00 24.30 ? 128 ILE A CG1 1 ATOM 647 C CG2 . ILE A 1 135 ? 21.345 34.850 20.176 1.00 26.90 ? 128 ILE A CG2 1 ATOM 648 C CD1 . ILE A 1 135 ? 20.712 35.762 23.201 1.00 24.89 ? 128 ILE A CD1 1 ATOM 649 N N . SER A 1 136 ? 20.630 32.266 18.534 1.00 27.83 ? 129 SER A N 1 ATOM 650 C CA . SER A 1 136 ? 21.419 31.499 17.559 1.00 28.81 ? 129 SER A CA 1 ATOM 651 C C . SER A 1 136 ? 22.308 32.393 16.728 1.00 31.47 ? 129 SER A C 1 ATOM 652 O O . SER A 1 136 ? 22.026 33.583 16.562 1.00 29.53 ? 129 SER A O 1 ATOM 653 C CB . SER A 1 136 ? 20.508 30.758 16.575 1.00 32.09 ? 129 SER A CB 1 ATOM 654 O OG . SER A 1 136 ? 19.684 29.839 17.249 1.00 34.30 ? 129 SER A OG 1 ATOM 655 N N . ILE A 1 137 ? 23.382 31.808 16.197 1.00 32.85 ? 130 ILE A N 1 ATOM 656 C CA . ILE A 1 137 ? 23.989 32.333 14.993 1.00 32.89 ? 130 ILE A CA 1 ATOM 657 C C . ILE A 1 137 ? 23.384 31.487 13.884 1.00 34.90 ? 130 ILE A C 1 ATOM 658 O O . ILE A 1 137 ? 23.334 30.253 13.972 1.00 34.68 ? 130 ILE A O 1 ATOM 659 C CB . ILE A 1 137 ? 25.526 32.245 14.994 1.00 31.86 ? 130 ILE A CB 1 ATOM 660 C CG1 . ILE A 1 137 ? 26.119 33.191 16.057 1.00 30.13 ? 130 ILE A CG1 1 ATOM 661 C CG2 . ILE A 1 137 ? 26.063 32.561 13.601 1.00 29.57 ? 130 ILE A CG2 1 ATOM 662 C CD1 . ILE A 1 137 ? 27.619 33.060 16.240 1.00 31.55 ? 130 ILE A CD1 1 ATOM 663 N N . ILE A 1 138 ? 22.899 32.161 12.853 1.00 36.76 ? 131 ILE A N 1 ATOM 664 C CA . ILE A 1 138 ? 22.201 31.489 11.765 1.00 38.41 ? 131 ILE A CA 1 ATOM 665 C C . ILE A 1 138 ? 22.997 31.750 10.478 1.00 40.84 ? 131 ILE A C 1 ATOM 666 O O . ILE A 1 138 ? 23.529 32.843 10.289 1.00 42.29 ? 131 ILE A O 1 ATOM 667 C CB . ILE A 1 138 ? 20.706 31.944 11.759 1.00 41.72 ? 131 ILE A CB 1 ATOM 668 C CG1 . ILE A 1 138 ? 19.826 31.010 10.931 1.00 47.03 ? 131 ILE A CG1 1 ATOM 669 C CG2 . ILE A 1 138 ? 20.539 33.413 11.368 1.00 43.34 ? 131 ILE A CG2 1 ATOM 670 C CD1 . ILE A 1 138 ? 18.358 31.068 11.324 1.00 48.63 ? 131 ILE A CD1 1 ATOM 671 N N . ASN A 1 139 ? 23.159 30.736 9.631 1.00 43.77 ? 132 ASN A N 1 ATOM 672 C CA . ASN A 1 139 ? 23.850 30.974 8.356 1.00 45.58 ? 132 ASN A CA 1 ATOM 673 C C . ASN A 1 139 ? 22.878 31.433 7.260 1.00 53.48 ? 132 ASN A C 1 ATOM 674 O O . ASN A 1 139 ? 21.667 31.523 7.505 1.00 54.27 ? 132 ASN A O 1 ATOM 675 C CB . ASN A 1 139 ? 24.728 29.784 7.926 1.00 49.57 ? 132 ASN A CB 1 ATOM 676 C CG . ASN A 1 139 ? 23.930 28.533 7.623 1.00 50.40 ? 132 ASN A CG 1 ATOM 677 O OD1 . ASN A 1 139 ? 22.745 28.590 7.291 1.00 50.46 ? 132 ASN A OD1 1 ATOM 678 N ND2 . ASN A 1 139 ? 24.590 27.384 7.726 1.00 46.38 ? 132 ASN A ND2 1 ATOM 679 N N . GLU A 1 140 ? 23.406 31.718 6.068 1.00 53.76 ? 133 GLU A N 1 ATOM 680 C CA . GLU A 1 140 ? 22.599 32.253 4.959 1.00 55.84 ? 133 GLU A CA 1 ATOM 681 C C . GLU A 1 140 ? 21.522 31.289 4.447 1.00 56.04 ? 133 GLU A C 1 ATOM 682 O O . GLU A 1 140 ? 20.610 31.701 3.730 1.00 57.53 ? 133 GLU A O 1 ATOM 683 C CB . GLU A 1 140 ? 23.493 32.719 3.809 1.00 57.27 ? 133 GLU A CB 1 ATOM 684 C CG . GLU A 1 140 ? 24.351 31.626 3.194 0.50 58.26 ? 133 GLU A CG 1 ATOM 685 C CD . GLU A 1 140 ? 25.183 32.126 2.031 1.00 66.33 ? 133 GLU A CD 1 ATOM 686 O OE1 . GLU A 1 140 ? 25.590 33.310 2.044 1.00 64.52 ? 133 GLU A OE1 1 ATOM 687 O OE2 . GLU A 1 140 ? 25.429 31.332 1.100 1.00 75.38 ? 133 GLU A OE2 1 ATOM 688 N N . ASP A 1 141 ? 21.637 30.016 4.825 1.00 57.15 ? 134 ASP A N 1 ATOM 689 C CA . ASP A 1 141 ? 20.639 28.995 4.497 1.00 55.60 ? 134 ASP A CA 1 ATOM 690 C C . ASP A 1 141 ? 19.582 28.833 5.595 1.00 56.63 ? 134 ASP A C 1 ATOM 691 O O . ASP A 1 141 ? 18.668 28.017 5.465 1.00 61.64 ? 134 ASP A O 1 ATOM 692 C CB . ASP A 1 141 ? 21.319 27.647 4.233 1.00 56.22 ? 134 ASP A CB 1 ATOM 693 C CG . ASP A 1 141 ? 22.331 27.710 3.105 0.70 57.11 ? 134 ASP A CG 1 ATOM 694 O OD1 . ASP A 1 141 ? 22.118 28.475 2.140 0.70 56.56 ? 134 ASP A OD1 1 ATOM 695 O OD2 . ASP A 1 141 ? 23.343 26.984 3.185 1.00 57.02 ? 134 ASP A OD2 1 ATOM 696 N N . GLY A 1 142 ? 19.711 29.603 6.673 1.00 50.47 ? 135 GLY A N 1 ATOM 697 C CA . GLY A 1 142 ? 18.781 29.513 7.792 1.00 54.33 ? 135 GLY A CA 1 ATOM 698 C C . GLY A 1 142 ? 19.099 28.424 8.808 1.00 51.76 ? 135 GLY A C 1 ATOM 699 O O . GLY A 1 142 ? 18.277 28.134 9.686 1.00 55.06 ? 135 GLY A O 1 ATOM 700 N N A ASN A 1 143 ? 20.278 27.818 8.684 0.70 43.20 ? 136 ASN A N 1 ATOM 701 N N B ASN A 1 143 ? 20.287 27.829 8.698 0.30 46.04 ? 136 ASN A N 1 ATOM 702 C CA A ASN A 1 143 ? 20.724 26.819 9.645 0.70 44.23 ? 136 ASN A CA 1 ATOM 703 C CA B ASN A 1 143 ? 20.744 26.793 9.630 0.30 44.81 ? 136 ASN A CA 1 ATOM 704 C C A ASN A 1 143 ? 21.265 27.494 10.897 0.70 43.73 ? 136 ASN A C 1 ATOM 705 C C B ASN A 1 143 ? 21.334 27.414 10.895 0.30 44.29 ? 136 ASN A C 1 ATOM 706 O O A ASN A 1 143 ? 22.111 28.389 10.819 0.70 42.32 ? 136 ASN A O 1 ATOM 707 O O B ASN A 1 143 ? 22.282 28.202 10.823 0.30 43.75 ? 136 ASN A O 1 ATOM 708 C CB A ASN A 1 143 ? 21.796 25.899 9.052 0.70 45.71 ? 136 ASN A CB 1 ATOM 709 C CB B ASN A 1 143 ? 21.776 25.887 8.949 0.30 44.56 ? 136 ASN A CB 1 ATOM 710 C CG A ASN A 1 143 ? 21.365 25.242 7.750 0.70 48.89 ? 136 ASN A CG 1 ATOM 711 C CG B ASN A 1 143 ? 22.122 24.655 9.770 0.30 43.13 ? 136 ASN A CG 1 ATOM 712 O OD1 A ASN A 1 143 ? 22.135 25.194 6.794 0.70 50.00 ? 136 ASN A OD1 1 ATOM 713 O OD1 B ASN A 1 143 ? 21.833 24.581 10.963 0.30 42.03 ? 136 ASN A OD1 1 ATOM 714 N ND2 A ASN A 1 143 ? 20.138 24.727 7.708 0.70 46.29 ? 136 ASN A ND2 1 ATOM 715 N ND2 B ASN A 1 143 ? 22.750 23.676 9.124 0.30 40.91 ? 136 ASN A ND2 1 ATOM 716 N N . GLU A 1 144 ? 20.767 27.056 12.047 1.00 42.06 ? 137 GLU A N 1 ATOM 717 C CA . GLU A 1 144 ? 21.221 27.580 13.334 1.00 40.79 ? 137 GLU A CA 1 ATOM 718 C C . GLU A 1 144 ? 22.471 26.814 13.749 1.00 37.67 ? 137 GLU A C 1 ATOM 719 O O . GLU A 1 144 ? 22.390 25.673 14.201 1.00 39.13 ? 137 GLU A O 1 ATOM 720 C CB . GLU A 1 144 ? 20.097 27.507 14.370 1.00 37.55 ? 137 GLU A CB 1 ATOM 721 C CG . GLU A 1 144 ? 18.961 28.472 14.038 1.00 38.51 ? 137 GLU A CG 1 ATOM 722 C CD . GLU A 1 144 ? 17.802 28.456 15.021 1.00 39.15 ? 137 GLU A CD 1 ATOM 723 O OE1 . GLU A 1 144 ? 17.754 27.584 15.917 1.00 36.03 ? 137 GLU A OE1 1 ATOM 724 O OE2 . GLU A 1 144 ? 16.924 29.338 14.890 1.00 39.10 ? 137 GLU A OE2 1 ATOM 725 N N . ILE A 1 145 ? 23.629 27.448 13.555 1.00 38.13 ? 138 ILE A N 1 ATOM 726 C CA . ILE A 1 145 ? 24.930 26.776 13.700 1.00 38.60 ? 138 ILE A CA 1 ATOM 727 C C . ILE A 1 145 ? 25.531 26.871 15.105 1.00 35.75 ? 138 ILE A C 1 ATOM 728 O O . ILE A 1 145 ? 26.502 26.166 15.427 1.00 39.45 ? 138 ILE A O 1 ATOM 729 C CB . ILE A 1 145 ? 25.965 27.248 12.638 1.00 36.61 ? 138 ILE A CB 1 ATOM 730 C CG1 . ILE A 1 145 ? 26.306 28.740 12.807 1.00 33.17 ? 138 ILE A CG1 1 ATOM 731 C CG2 . ILE A 1 145 ? 25.463 26.920 11.237 1.00 40.39 ? 138 ILE A CG2 1 ATOM 732 C CD1 . ILE A 1 145 ? 27.521 29.189 12.009 1.00 39.13 ? 138 ILE A CD1 1 ATOM 733 N N . PHE A 1 146 ? 24.953 27.740 15.924 1.00 32.53 ? 139 PHE A N 1 ATOM 734 C CA . PHE A 1 146 ? 25.315 27.866 17.322 1.00 33.30 ? 139 PHE A CA 1 ATOM 735 C C . PHE A 1 146 ? 24.089 28.295 18.092 1.00 31.64 ? 139 PHE A C 1 ATOM 736 O O . PHE A 1 146 ? 23.378 29.204 17.658 1.00 29.50 ? 139 PHE A O 1 ATOM 737 C CB . PHE A 1 146 ? 26.424 28.907 17.522 1.00 33.58 ? 139 PHE A CB 1 ATOM 738 C CG . PHE A 1 146 ? 26.580 29.345 18.950 1.00 32.95 ? 139 PHE A CG 1 ATOM 739 C CD1 . PHE A 1 146 ? 27.241 28.537 19.876 1.00 34.40 ? 139 PHE A CD1 1 ATOM 740 C CD2 . PHE A 1 146 ? 26.036 30.554 19.384 1.00 32.22 ? 139 PHE A CD2 1 ATOM 741 C CE1 . PHE A 1 146 ? 27.359 28.934 21.204 1.00 35.44 ? 139 PHE A CE1 1 ATOM 742 C CE2 . PHE A 1 146 ? 26.155 30.955 20.712 1.00 33.02 ? 139 PHE A CE2 1 ATOM 743 C CZ . PHE A 1 146 ? 26.815 30.142 21.621 1.00 33.68 ? 139 PHE A CZ 1 ATOM 744 N N . ASN A 1 147 ? 23.853 27.646 19.231 1.00 29.13 ? 140 ASN A N 1 ATOM 745 C CA . ASN A 1 147 ? 22.759 28.008 20.127 1.00 27.99 ? 140 ASN A CA 1 ATOM 746 C C . ASN A 1 147 ? 23.254 28.314 21.519 1.00 26.50 ? 140 ASN A C 1 ATOM 747 O O . ASN A 1 147 ? 24.081 27.574 22.056 1.00 28.20 ? 140 ASN A O 1 ATOM 748 C CB . ASN A 1 147 ? 21.773 26.855 20.243 1.00 31.06 ? 140 ASN A CB 1 ATOM 749 C CG . ASN A 1 147 ? 21.026 26.597 18.960 1.00 31.73 ? 140 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 147 ? 20.755 27.515 18.186 1.00 33.40 ? 140 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 147 ? 20.692 25.336 18.726 1.00 36.30 ? 140 ASN A ND2 1 ATOM 752 N N . THR A 1 148 ? 22.717 29.370 22.127 1.00 25.72 ? 141 THR A N 1 ATOM 753 C CA . THR A 1 148 ? 23.035 29.656 23.524 1.00 25.27 ? 141 THR A CA 1 ATOM 754 C C . THR A 1 148 ? 22.350 28.622 24.426 1.00 25.66 ? 141 THR A C 1 ATOM 755 O O . THR A 1 148 ? 21.436 27.910 23.989 1.00 27.34 ? 141 THR A O 1 ATOM 756 C CB . THR A 1 148 ? 22.674 31.098 23.933 1.00 24.49 ? 141 THR A CB 1 ATOM 757 O OG1 . THR A 1 148 ? 21.267 31.311 23.766 1.00 26.46 ? 141 THR A OG1 1 ATOM 758 C CG2 . THR A 1 148 ? 23.456 32.112 23.088 1.00 25.63 ? 141 THR A CG2 1 ATOM 759 N N . SER A 1 149 ? 22.810 28.532 25.670 1.00 27.13 ? 142 SER A N 1 ATOM 760 C CA . SER A 1 149 ? 22.352 27.512 26.607 1.00 24.83 ? 142 SER A CA 1 ATOM 761 C C . SER A 1 149 ? 20.873 27.681 26.971 1.00 24.23 ? 142 SER A C 1 ATOM 762 O O . SER A 1 149 ? 20.349 28.810 26.983 1.00 25.50 ? 142 SER A O 1 ATOM 763 C CB . SER A 1 149 ? 23.187 27.592 27.891 1.00 26.74 ? 142 SER A CB 1 ATOM 764 O OG A SER A 1 149 ? 22.698 28.612 28.762 0.50 22.28 ? 142 SER A OG 1 ATOM 765 O OG B SER A 1 149 ? 23.010 26.435 28.683 0.50 35.49 ? 142 SER A OG 1 ATOM 766 N N . LEU A 1 150 ? 20.210 26.569 27.288 1.00 23.85 ? 143 LEU A N 1 ATOM 767 C CA . LEU A 1 150 ? 18.811 26.619 27.754 1.00 24.58 ? 143 LEU A CA 1 ATOM 768 C C . LEU A 1 150 ? 18.661 26.736 29.273 1.00 25.20 ? 143 LEU A C 1 ATOM 769 O O . LEU A 1 150 ? 17.560 27.012 29.765 1.00 26.13 ? 143 LEU A O 1 ATOM 770 C CB . LEU A 1 150 ? 18.006 25.427 27.216 1.00 28.45 ? 143 LEU A CB 1 ATOM 771 C CG . LEU A 1 150 ? 17.994 25.248 25.691 1.00 29.98 ? 143 LEU A CG 1 ATOM 772 C CD1 . LEU A 1 150 ? 17.069 24.104 25.327 1.00 31.56 ? 143 LEU A CD1 1 ATOM 773 C CD2 . LEU A 1 150 ? 17.556 26.527 24.996 1.00 32.09 ? 143 LEU A CD2 1 ATOM 774 N N . PHE A 1 151 ? 19.767 26.561 30.003 1.00 24.08 ? 144 PHE A N 1 ATOM 775 C CA . PHE A 1 151 ? 19.765 26.664 31.473 1.00 23.62 ? 144 PHE A CA 1 ATOM 776 C C . PHE A 1 151 ? 21.189 26.779 31.985 1.00 23.84 ? 144 PHE A C 1 ATOM 777 O O . PHE A 1 151 ? 22.124 26.433 31.270 1.00 25.22 ? 144 PHE A O 1 ATOM 778 C CB . PHE A 1 151 ? 19.084 25.430 32.091 1.00 27.20 ? 144 PHE A CB 1 ATOM 779 C CG . PHE A 1 151 ? 19.770 24.124 31.758 1.00 28.72 ? 144 PHE A CG 1 ATOM 780 C CD1 . PHE A 1 151 ? 20.780 23.622 32.586 1.00 29.88 ? 144 PHE A CD1 1 ATOM 781 C CD2 . PHE A 1 151 ? 19.433 23.405 30.610 1.00 34.55 ? 144 PHE A CD2 1 ATOM 782 C CE1 . PHE A 1 151 ? 21.424 22.439 32.287 1.00 35.07 ? 144 PHE A CE1 1 ATOM 783 C CE2 . PHE A 1 151 ? 20.073 22.208 30.304 1.00 37.24 ? 144 PHE A CE2 1 ATOM 784 C CZ . PHE A 1 151 ? 21.069 21.725 31.145 1.00 36.89 ? 144 PHE A CZ 1 ATOM 785 N N . GLU A 1 152 ? 21.350 27.263 33.215 1.00 21.59 ? 145 GLU A N 1 ATOM 786 C CA . GLU A 1 152 ? 22.654 27.248 33.903 1.00 22.37 ? 145 GLU A CA 1 ATOM 787 C C . GLU A 1 152 ? 22.896 25.861 34.466 1.00 23.27 ? 145 GLU A C 1 ATOM 788 O O . GLU A 1 152 ? 21.982 25.279 35.070 1.00 22.81 ? 145 GLU A O 1 ATOM 789 C CB . GLU A 1 152 ? 22.659 28.194 35.099 1.00 23.05 ? 145 GLU A CB 1 ATOM 790 C CG . GLU A 1 152 ? 22.594 29.650 34.764 1.00 22.43 ? 145 GLU A CG 1 ATOM 791 C CD . GLU A 1 152 ? 22.535 30.492 36.029 1.00 21.06 ? 145 GLU A CD 1 ATOM 792 O OE1 . GLU A 1 152 ? 21.450 30.567 36.652 1.00 22.32 ? 145 GLU A OE1 1 ATOM 793 O OE2 . GLU A 1 152 ? 23.579 31.053 36.420 1.00 22.51 ? 145 GLU A OE2 1 ATOM 794 N N . PRO A 1 153 ? 24.123 25.329 34.296 1.00 22.35 ? 146 PRO A N 1 ATOM 795 C CA . PRO A 1 153 ? 24.458 24.059 34.952 1.00 23.38 ? 146 PRO A CA 1 ATOM 796 C C . PRO A 1 153 ? 24.176 24.188 36.461 1.00 23.44 ? 146 PRO A C 1 ATOM 797 O O . PRO A 1 153 ? 24.737 25.081 37.126 1.00 24.99 ? 146 PRO A O 1 ATOM 798 C CB . PRO A 1 153 ? 25.957 23.897 34.669 1.00 27.06 ? 146 PRO A CB 1 ATOM 799 C CG . PRO A 1 153 ? 26.225 24.733 33.464 1.00 27.47 ? 146 PRO A CG 1 ATOM 800 C CD . PRO A 1 153 ? 25.241 25.867 33.488 1.00 25.69 ? 146 PRO A CD 1 ATOM 801 N N . PRO A 1 154 ? 23.266 23.354 37.001 1.00 22.69 ? 147 PRO A N 1 ATOM 802 C CA . PRO A 1 154 ? 22.917 23.584 38.411 1.00 23.59 ? 147 PRO A CA 1 ATOM 803 C C . PRO A 1 154 ? 24.082 23.234 39.355 1.00 25.03 ? 147 PRO A C 1 ATOM 804 O O . PRO A 1 154 ? 24.919 22.377 39.019 1.00 24.60 ? 147 PRO A O 1 ATOM 805 C CB . PRO A 1 154 ? 21.709 22.665 38.636 1.00 25.65 ? 147 PRO A CB 1 ATOM 806 C CG . PRO A 1 154 ? 21.772 21.668 37.537 1.00 27.26 ? 147 PRO A CG 1 ATOM 807 C CD . PRO A 1 154 ? 22.377 22.372 36.365 1.00 23.92 ? 147 PRO A CD 1 ATOM 808 N N . PRO A 1 155 ? 24.149 23.899 40.520 1.00 24.49 ? 148 PRO A N 1 ATOM 809 C CA . PRO A 1 155 ? 25.296 23.647 41.397 1.00 24.91 ? 148 PRO A CA 1 ATOM 810 C C . PRO A 1 155 ? 25.256 22.268 42.079 1.00 25.10 ? 148 PRO A C 1 ATOM 811 O O . PRO A 1 155 ? 24.193 21.630 42.107 1.00 25.34 ? 148 PRO A O 1 ATOM 812 C CB . PRO A 1 155 ? 25.202 24.774 42.425 1.00 26.32 ? 148 PRO A CB 1 ATOM 813 C CG . PRO A 1 155 ? 23.774 25.180 42.452 1.00 25.00 ? 148 PRO A CG 1 ATOM 814 C CD . PRO A 1 155 ? 23.237 24.922 41.066 1.00 25.25 ? 148 PRO A CD 1 ATOM 815 N N . PRO A 1 156 ? 26.405 21.818 42.642 1.00 24.54 ? 149 PRO A N 1 ATOM 816 C CA . PRO A 1 156 ? 26.492 20.483 43.263 1.00 23.85 ? 149 PRO A CA 1 ATOM 817 C C . PRO A 1 156 ? 25.357 20.201 44.271 1.00 25.92 ? 149 PRO A C 1 ATOM 818 O O . PRO A 1 156 ? 25.125 20.997 45.194 1.00 24.84 ? 149 PRO A O 1 ATOM 819 C CB . PRO A 1 156 ? 27.853 20.517 43.967 1.00 25.95 ? 149 PRO A CB 1 ATOM 820 C CG . PRO A 1 156 ? 28.666 21.475 43.140 1.00 26.51 ? 149 PRO A CG 1 ATOM 821 C CD . PRO A 1 156 ? 27.689 22.546 42.728 1.00 26.39 ? 149 PRO A CD 1 ATOM 822 N N . GLY A 1 157 ? 24.654 19.083 44.075 1.00 24.55 ? 150 GLY A N 1 ATOM 823 C CA . GLY A 1 157 ? 23.589 18.687 44.982 1.00 26.80 ? 150 GLY A CA 1 ATOM 824 C C . GLY A 1 157 ? 22.236 19.323 44.707 1.00 30.06 ? 150 GLY A C 1 ATOM 825 O O . GLY A 1 157 ? 21.264 19.006 45.403 1.00 33.03 ? 150 GLY A O 1 ATOM 826 N N . TYR A 1 158 ? 22.178 20.210 43.702 1.00 29.37 ? 151 TYR A N 1 ATOM 827 C CA . TYR A 1 158 ? 20.930 20.875 43.259 1.00 30.63 ? 151 TYR A CA 1 ATOM 828 C C . TYR A 1 158 ? 20.555 20.524 41.818 1.00 34.05 ? 151 TYR A C 1 ATOM 829 O O . TYR A 1 158 ? 19.645 21.142 41.241 1.00 33.84 ? 151 TYR A O 1 ATOM 830 C CB . TYR A 1 158 ? 21.083 22.386 43.275 1.00 27.23 ? 151 TYR A CB 1 ATOM 831 C CG . TYR A 1 158 ? 21.295 23.046 44.603 1.00 26.50 ? 151 TYR A CG 1 ATOM 832 C CD1 . TYR A 1 158 ? 20.224 23.619 45.290 1.00 26.51 ? 151 TYR A CD1 1 ATOM 833 C CD2 . TYR A 1 158 ? 22.571 23.152 45.149 1.00 25.38 ? 151 TYR A CD2 1 ATOM 834 C CE1 . TYR A 1 158 ? 20.417 24.269 46.491 1.00 24.81 ? 151 TYR A CE1 1 ATOM 835 C CE2 . TYR A 1 158 ? 22.778 23.795 46.352 1.00 23.19 ? 151 TYR A CE2 1 ATOM 836 C CZ . TYR A 1 158 ? 21.697 24.354 47.012 1.00 23.78 ? 151 TYR A CZ 1 ATOM 837 O OH . TYR A 1 158 ? 21.896 24.995 48.191 1.00 23.45 ? 151 TYR A OH 1 ATOM 838 N N . GLU A 1 159 ? 21.270 19.568 41.226 1.00 32.72 ? 152 GLU A N 1 ATOM 839 C CA . GLU A 1 159 ? 21.028 19.161 39.842 1.00 34.77 ? 152 GLU A CA 1 ATOM 840 C C . GLU A 1 159 ? 19.659 18.477 39.644 0.75 35.21 ? 152 GLU A C 1 ATOM 841 O O . GLU A 1 159 ? 19.224 18.283 38.508 0.75 35.57 ? 152 GLU A O 1 ATOM 842 C CB . GLU A 1 159 ? 22.180 18.288 39.303 1.00 36.88 ? 152 GLU A CB 1 ATOM 843 C CG . GLU A 1 159 ? 23.583 18.849 39.544 1.00 41.88 ? 152 GLU A CG 1 ATOM 844 C CD . GLU A 1 159 ? 24.239 18.343 40.829 1.00 41.01 ? 152 GLU A CD 1 ATOM 845 O OE1 . GLU A 1 159 ? 23.537 17.884 41.755 1.00 38.32 ? 152 GLU A OE1 1 ATOM 846 O OE2 . GLU A 1 159 ? 25.486 18.409 40.922 1.00 43.49 ? 152 GLU A OE2 1 ATOM 847 N N . ASN A 1 160 ? 18.990 18.141 40.750 0.75 35.61 ? 153 ASN A N 1 ATOM 848 C CA . ASN A 1 160 ? 17.652 17.528 40.725 1.00 39.63 ? 153 ASN A CA 1 ATOM 849 C C . ASN A 1 160 ? 16.575 18.445 41.330 1.00 41.69 ? 153 ASN A C 1 ATOM 850 O O . ASN A 1 160 ? 15.412 18.054 41.491 1.00 41.39 ? 153 ASN A O 1 ATOM 851 C CB . ASN A 1 160 ? 17.675 16.176 41.446 1.00 41.05 ? 153 ASN A CB 1 ATOM 852 C CG . ASN A 1 160 ? 16.435 15.337 41.169 1.00 40.54 ? 153 ASN A CG 1 ATOM 853 O OD1 . ASN A 1 160 ? 16.073 15.095 40.012 1.00 43.19 ? 153 ASN A OD1 1 ATOM 854 N ND2 . ASN A 1 160 ? 15.785 14.878 42.234 1.00 45.47 ? 153 ASN A ND2 1 ATOM 855 N N . VAL A 1 161 ? 16.957 19.670 41.666 1.00 39.34 ? 154 VAL A N 1 ATOM 856 C CA . VAL A 1 161 ? 15.986 20.626 42.174 1.00 37.03 ? 154 VAL A CA 1 ATOM 857 C C . VAL A 1 161 ? 15.069 21.043 41.017 1.00 42.76 ? 154 VAL A C 1 ATOM 858 O O . VAL A 1 161 ? 15.526 21.380 39.916 1.00 41.16 ? 154 VAL A O 1 ATOM 859 C CB . VAL A 1 161 ? 16.653 21.822 42.903 1.00 37.77 ? 154 VAL A CB 1 ATOM 860 C CG1 . VAL A 1 161 ? 15.650 22.948 43.167 1.00 35.01 ? 154 VAL A CG1 1 ATOM 861 C CG2 . VAL A 1 161 ? 17.266 21.349 44.217 1.00 41.72 ? 154 VAL A CG2 1 ATOM 862 N N . SER A 1 162 ? 13.767 20.965 41.271 1.00 41.60 ? 155 SER A N 1 ATOM 863 C CA . SER A 1 162 ? 12.781 21.306 40.267 1.00 40.68 ? 155 SER A CA 1 ATOM 864 C C . SER A 1 162 ? 12.443 22.806 40.319 1.00 36.77 ? 155 SER A C 1 ATOM 865 O O . SER A 1 162 ? 12.640 23.509 41.350 1.00 35.90 ? 155 SER A O 1 ATOM 866 C CB . SER A 1 162 ? 11.515 20.443 40.443 1.00 43.24 ? 155 SER A CB 1 ATOM 867 O OG A SER A 1 162 ? 10.972 20.584 41.742 0.50 44.63 ? 155 SER A OG 1 ATOM 868 O OG B SER A 1 162 ? 10.983 20.044 39.191 0.50 41.06 ? 155 SER A OG 1 ATOM 869 N N . ASP A 1 163 ? 11.950 23.303 39.194 1.00 31.96 ? 156 ASP A N 1 ATOM 870 C CA . ASP A 1 163 ? 11.378 24.636 39.153 1.00 31.28 ? 156 ASP A CA 1 ATOM 871 C C . ASP A 1 163 ? 12.455 25.708 39.275 1.00 26.55 ? 156 ASP A C 1 ATOM 872 O O . ASP A 1 163 ? 12.185 26.782 39.818 1.00 26.33 ? 156 ASP A O 1 ATOM 873 C CB . ASP A 1 163 ? 10.346 24.851 40.289 1.00 34.87 ? 156 ASP A CB 1 ATOM 874 C CG . ASP A 1 163 ? 9.203 23.844 40.276 1.00 42.39 ? 156 ASP A CG 1 ATOM 875 O OD1 . ASP A 1 163 ? 8.601 23.597 39.202 1.00 46.28 ? 156 ASP A OD1 1 ATOM 876 O OD2 . ASP A 1 163 ? 8.891 23.310 41.365 1.00 51.63 ? 156 ASP A OD2 1 ATOM 877 N N . ILE A 1 164 ? 13.677 25.437 38.810 1.00 21.06 ? 157 ILE A N 1 ATOM 878 C CA . ILE A 1 164 ? 14.619 26.561 38.666 1.00 20.09 ? 157 ILE A CA 1 ATOM 879 C C . ILE A 1 164 ? 14.260 27.296 37.385 1.00 20.74 ? 157 ILE A C 1 ATOM 880 O O . ILE A 1 164 ? 14.278 26.698 36.291 1.00 22.26 ? 157 ILE A O 1 ATOM 881 C CB . ILE A 1 164 ? 16.090 26.075 38.610 1.00 20.06 ? 157 ILE A CB 1 ATOM 882 C CG1 . ILE A 1 164 ? 16.501 25.463 39.960 1.00 20.41 ? 157 ILE A CG1 1 ATOM 883 C CG2 . ILE A 1 164 ? 17.020 27.219 38.193 1.00 20.41 ? 157 ILE A CG2 1 ATOM 884 C CD1 . ILE A 1 164 ? 17.792 24.650 39.934 1.00 21.85 ? 157 ILE A CD1 1 ATOM 885 N N . VAL A 1 165 ? 13.888 28.569 37.499 1.00 18.76 ? 158 VAL A N 1 ATOM 886 C CA . VAL A 1 165 ? 13.509 29.320 36.311 1.00 19.60 ? 158 VAL A CA 1 ATOM 887 C C . VAL A 1 165 ? 14.752 29.508 35.427 1.00 19.36 ? 158 VAL A C 1 ATOM 888 O O . VAL A 1 165 ? 15.780 29.949 35.923 1.00 20.02 ? 158 VAL A O 1 ATOM 889 C CB . VAL A 1 165 ? 12.785 30.655 36.666 1.00 18.35 ? 158 VAL A CB 1 ATOM 890 C CG1 . VAL A 1 165 ? 13.769 31.749 37.136 1.00 18.65 ? 158 VAL A CG1 1 ATOM 891 C CG2 . VAL A 1 165 ? 11.961 31.127 35.461 1.00 20.03 ? 158 VAL A CG2 1 ATOM 892 N N . PRO A 1 166 ? 14.685 29.140 34.120 1.00 19.40 ? 159 PRO A N 1 ATOM 893 C CA . PRO A 1 166 ? 15.917 29.381 33.323 1.00 19.05 ? 159 PRO A CA 1 ATOM 894 C C . PRO A 1 166 ? 16.196 30.887 33.174 1.00 19.93 ? 159 PRO A C 1 ATOM 895 O O . PRO A 1 166 ? 15.274 31.709 33.363 1.00 19.34 ? 159 PRO A O 1 ATOM 896 C CB . PRO A 1 166 ? 15.582 28.762 31.957 1.00 21.86 ? 159 PRO A CB 1 ATOM 897 C CG . PRO A 1 166 ? 14.088 28.777 31.890 1.00 21.94 ? 159 PRO A CG 1 ATOM 898 C CD . PRO A 1 166 ? 13.607 28.552 33.307 1.00 20.77 ? 159 PRO A CD 1 ATOM 899 N N . PRO A 1 167 ? 17.453 31.260 32.858 1.00 19.26 ? 160 PRO A N 1 ATOM 900 C CA . PRO A 1 167 ? 17.756 32.694 32.669 1.00 18.75 ? 160 PRO A CA 1 ATOM 901 C C . PRO A 1 167 ? 16.825 33.328 31.630 1.00 17.88 ? 160 PRO A C 1 ATOM 902 O O . PRO A 1 167 ? 16.585 32.745 30.563 1.00 19.44 ? 160 PRO A O 1 ATOM 903 C CB . PRO A 1 167 ? 19.214 32.678 32.184 1.00 18.75 ? 160 PRO A CB 1 ATOM 904 C CG . PRO A 1 167 ? 19.764 31.422 32.795 1.00 19.30 ? 160 PRO A CG 1 ATOM 905 C CD . PRO A 1 167 ? 18.650 30.423 32.629 1.00 19.70 ? 160 PRO A CD 1 ATOM 906 N N . PHE A 1 168 ? 16.278 34.490 31.970 1.00 16.67 ? 161 PHE A N 1 ATOM 907 C CA . PHE A 1 168 ? 15.444 35.271 31.038 1.00 17.38 ? 161 PHE A CA 1 ATOM 908 C C . PHE A 1 168 ? 15.419 36.699 31.516 1.00 17.17 ? 161 PHE A C 1 ATOM 909 O O . PHE A 1 168 ? 15.745 36.973 32.675 1.00 17.80 ? 161 PHE A O 1 ATOM 910 C CB . PHE A 1 168 ? 14.010 34.704 30.940 1.00 17.94 ? 161 PHE A CB 1 ATOM 911 C CG . PHE A 1 168 ? 13.115 35.013 32.138 1.00 17.22 ? 161 PHE A CG 1 ATOM 912 C CD1 . PHE A 1 168 ? 11.935 35.786 31.986 1.00 16.08 ? 161 PHE A CD1 1 ATOM 913 C CD2 . PHE A 1 168 ? 13.389 34.466 33.400 1.00 17.98 ? 161 PHE A CD2 1 ATOM 914 C CE1 . PHE A 1 168 ? 11.093 36.041 33.075 1.00 16.19 ? 161 PHE A CE1 1 ATOM 915 C CE2 . PHE A 1 168 ? 12.547 34.732 34.495 1.00 17.70 ? 161 PHE A CE2 1 ATOM 916 C CZ . PHE A 1 168 ? 11.397 35.513 34.334 1.00 16.93 ? 161 PHE A CZ 1 ATOM 917 N N . SER A 1 169 ? 15.027 37.604 30.623 1.00 17.12 ? 162 SER A N 1 ATOM 918 C CA . SER A 1 169 ? 14.826 39.006 30.992 1.00 16.38 ? 162 SER A CA 1 ATOM 919 C C . SER A 1 169 ? 13.339 39.222 31.222 1.00 16.43 ? 162 SER A C 1 ATOM 920 O O . SER A 1 169 ? 12.553 39.221 30.271 1.00 17.58 ? 162 SER A O 1 ATOM 921 C CB . SER A 1 169 ? 15.340 39.914 29.874 1.00 17.56 ? 162 SER A CB 1 ATOM 922 O OG . SER A 1 169 ? 16.740 39.760 29.704 1.00 18.58 ? 162 SER A OG 1 ATOM 923 N N . ALA A 1 170 ? 12.937 39.419 32.474 1.00 17.40 ? 163 ALA A N 1 ATOM 924 C CA . ALA A 1 170 ? 11.494 39.533 32.777 1.00 16.25 ? 163 ALA A CA 1 ATOM 925 C C . ALA A 1 170 ? 10.900 40.755 32.076 1.00 17.04 ? 163 ALA A C 1 ATOM 926 O O . ALA A 1 170 ? 11.482 41.850 32.097 1.00 16.31 ? 163 ALA A O 1 ATOM 927 C CB . ALA A 1 170 ? 11.226 39.592 34.284 1.00 16.32 ? 163 ALA A CB 1 ATOM 928 N N . PHE A 1 171 ? 9.762 40.503 31.434 1.00 17.34 ? 164 PHE A N 1 ATOM 929 C CA . PHE A 1 171 ? 8.907 41.473 30.730 1.00 17.22 ? 164 PHE A CA 1 ATOM 930 C C . PHE A 1 171 ? 9.340 41.711 29.283 1.00 17.70 ? 164 PHE A C 1 ATOM 931 O O . PHE A 1 171 ? 8.730 42.522 28.582 1.00 18.64 ? 164 PHE A O 1 ATOM 932 C CB . PHE A 1 171 ? 8.712 42.780 31.513 1.00 17.03 ? 164 PHE A CB 1 ATOM 933 C CG . PHE A 1 171 ? 8.034 42.584 32.849 1.00 14.92 ? 164 PHE A CG 1 ATOM 934 C CD1 . PHE A 1 171 ? 6.634 42.414 32.934 1.00 16.37 ? 164 PHE A CD1 1 ATOM 935 C CD2 . PHE A 1 171 ? 8.790 42.561 34.033 1.00 14.52 ? 164 PHE A CD2 1 ATOM 936 C CE1 . PHE A 1 171 ? 6.009 42.236 34.170 1.00 15.42 ? 164 PHE A CE1 1 ATOM 937 C CE2 . PHE A 1 171 ? 8.173 42.391 35.272 1.00 14.58 ? 164 PHE A CE2 1 ATOM 938 C CZ . PHE A 1 171 ? 6.776 42.237 35.349 1.00 13.96 ? 164 PHE A CZ 1 ATOM 939 N N . SER A 1 172 ? 10.329 40.963 28.802 1.00 18.05 ? 165 SER A N 1 ATOM 940 C CA . SER A 1 172 ? 10.621 40.995 27.372 1.00 19.03 ? 165 SER A CA 1 ATOM 941 C C . SER A 1 172 ? 9.362 40.655 26.565 1.00 19.54 ? 165 SER A C 1 ATOM 942 O O . SER A 1 172 ? 8.615 39.728 26.917 1.00 20.77 ? 165 SER A O 1 ATOM 943 C CB . SER A 1 172 ? 11.706 39.979 26.985 1.00 19.59 ? 165 SER A CB 1 ATOM 944 O OG . SER A 1 172 ? 11.917 40.032 25.582 1.00 19.77 ? 165 SER A OG 1 ATOM 945 N N . PRO A 1 173 ? 9.119 41.396 25.473 1.00 20.09 ? 166 PRO A N 1 ATOM 946 C CA . PRO A 1 173 ? 8.098 40.909 24.557 1.00 20.73 ? 166 PRO A CA 1 ATOM 947 C C . PRO A 1 173 ? 8.582 39.664 23.826 1.00 21.61 ? 166 PRO A C 1 ATOM 948 O O . PRO A 1 173 ? 9.788 39.331 23.839 1.00 22.62 ? 166 PRO A O 1 ATOM 949 C CB . PRO A 1 173 ? 7.947 42.073 23.560 1.00 19.47 ? 166 PRO A CB 1 ATOM 950 C CG . PRO A 1 173 ? 9.298 42.746 23.574 1.00 20.92 ? 166 PRO A CG 1 ATOM 951 C CD . PRO A 1 173 ? 9.723 42.665 25.013 1.00 21.43 ? 166 PRO A CD 1 ATOM 952 N N . GLN A 1 174 ? 7.647 38.982 23.182 1.00 22.66 ? 167 GLN A N 1 ATOM 953 C CA . GLN A 1 174 ? 7.982 37.871 22.310 1.00 22.49 ? 167 GLN A CA 1 ATOM 954 C C . GLN A 1 174 ? 8.510 38.377 20.973 1.00 25.18 ? 167 GLN A C 1 ATOM 955 O O . GLN A 1 174 ? 8.175 39.474 20.533 1.00 26.41 ? 167 GLN A O 1 ATOM 956 C CB . GLN A 1 174 ? 6.746 37.014 22.082 1.00 23.34 ? 167 GLN A CB 1 ATOM 957 C CG . GLN A 1 174 ? 6.118 36.534 23.382 1.00 26.23 ? 167 GLN A CG 1 ATOM 958 C CD . GLN A 1 174 ? 4.915 35.645 23.163 1.00 31.64 ? 167 GLN A CD 1 ATOM 959 O OE1 . GLN A 1 174 ? 4.435 35.501 22.047 1.00 37.55 ? 167 GLN A OE1 1 ATOM 960 N NE2 . GLN A 1 174 ? 4.427 35.035 24.235 1.00 34.42 ? 167 GLN A NE2 1 ATOM 961 N N . GLY A 1 175 ? 9.338 37.570 20.328 1.00 25.19 ? 168 GLY A N 1 ATOM 962 C CA . GLY A 1 175 ? 9.807 37.890 18.980 1.00 26.66 ? 168 GLY A CA 1 ATOM 963 C C . GLY A 1 175 ? 10.889 36.934 18.563 1.00 26.75 ? 168 GLY A C 1 ATOM 964 O O . GLY A 1 175 ? 11.450 36.224 19.405 1.00 27.51 ? 168 GLY A O 1 ATOM 965 N N . MET A 1 176 ? 11.166 36.913 17.257 1.00 27.31 ? 169 MET A N 1 ATOM 966 C CA . MET A 1 176 ? 12.273 36.151 16.691 1.00 26.36 ? 169 MET A CA 1 ATOM 967 C C . MET A 1 176 ? 13.116 37.014 15.744 1.00 28.28 ? 169 MET A C 1 ATOM 968 O O . MET A 1 176 ? 13.395 36.604 14.597 1.00 30.65 ? 169 MET A O 1 ATOM 969 C CB . MET A 1 176 ? 11.753 34.898 15.983 1.00 30.51 ? 169 MET A CB 1 ATOM 970 C CG . MET A 1 176 ? 11.282 33.793 16.917 1.00 35.98 ? 169 MET A CG 1 ATOM 971 S SD . MET A 1 176 ? 10.734 32.381 15.944 1.00 56.89 ? 169 MET A SD 1 ATOM 972 C CE . MET A 1 176 ? 10.398 31.163 17.206 1.00 51.31 ? 169 MET A CE 1 ATOM 973 N N . PRO A 1 177 ? 13.545 38.208 16.217 1.00 28.29 ? 170 PRO A N 1 ATOM 974 C CA . PRO A 1 177 ? 14.302 39.111 15.342 1.00 29.88 ? 170 PRO A CA 1 ATOM 975 C C . PRO A 1 177 ? 15.636 38.507 14.895 1.00 31.81 ? 170 PRO A C 1 ATOM 976 O O . PRO A 1 177 ? 16.321 37.843 15.689 1.00 32.10 ? 170 PRO A O 1 ATOM 977 C CB . PRO A 1 177 ? 14.534 40.348 16.222 1.00 29.54 ? 170 PRO A CB 1 ATOM 978 C CG . PRO A 1 177 ? 14.482 39.834 17.620 1.00 28.68 ? 170 PRO A CG 1 ATOM 979 C CD . PRO A 1 177 ? 13.463 38.729 17.595 1.00 29.27 ? 170 PRO A CD 1 ATOM 980 N N A GLU A 1 178 ? 15.962 38.715 13.620 0.60 32.23 ? 171 GLU A N 1 ATOM 981 N N B GLU A 1 178 ? 15.998 38.751 13.637 0.40 31.90 ? 171 GLU A N 1 ATOM 982 C CA A GLU A 1 178 ? 17.228 38.284 13.037 0.60 32.52 ? 171 GLU A CA 1 ATOM 983 C CA B GLU A 1 178 ? 17.245 38.247 13.064 0.40 31.77 ? 171 GLU A CA 1 ATOM 984 C C A GLU A 1 178 ? 17.927 39.534 12.562 0.60 34.90 ? 171 GLU A C 1 ATOM 985 C C B GLU A 1 178 ? 17.993 39.376 12.370 0.40 33.43 ? 171 GLU A C 1 ATOM 986 O O A GLU A 1 178 ? 17.291 40.408 11.975 0.60 34.45 ? 171 GLU A O 1 ATOM 987 O O B GLU A 1 178 ? 17.460 40.003 11.454 0.40 31.64 ? 171 GLU A O 1 ATOM 988 C CB A GLU A 1 178 ? 17.005 37.378 11.819 0.60 35.79 ? 171 GLU A CB 1 ATOM 989 C CB B GLU A 1 178 ? 16.961 37.126 12.063 0.40 33.41 ? 171 GLU A CB 1 ATOM 990 C CG A GLU A 1 178 ? 15.991 36.267 12.010 0.60 39.21 ? 171 GLU A CG 1 ATOM 991 C CG B GLU A 1 178 ? 18.187 36.688 11.283 0.40 34.22 ? 171 GLU A CG 1 ATOM 992 C CD A GLU A 1 178 ? 15.761 35.449 10.753 0.60 39.94 ? 171 GLU A CD 1 ATOM 993 C CD B GLU A 1 178 ? 17.843 35.843 10.077 0.40 37.03 ? 171 GLU A CD 1 ATOM 994 O OE1 A GLU A 1 178 ? 14.835 34.610 10.761 0.60 43.20 ? 171 GLU A OE1 1 ATOM 995 O OE1 B GLU A 1 178 ? 18.186 36.252 8.949 0.40 40.23 ? 171 GLU A OE1 1 ATOM 996 O OE2 A GLU A 1 178 ? 16.494 35.638 9.754 0.60 41.59 ? 171 GLU A OE2 1 ATOM 997 O OE2 B GLU A 1 178 ? 17.222 34.776 10.257 0.40 40.22 ? 171 GLU A OE2 1 ATOM 998 N N . GLY A 1 179 ? 19.231 39.625 12.792 1.00 32.89 ? 172 GLY A N 1 ATOM 999 C CA . GLY A 1 179 ? 19.985 40.763 12.287 1.00 35.01 ? 172 GLY A CA 1 ATOM 1000 C C . GLY A 1 179 ? 21.471 40.735 12.544 1.00 32.44 ? 172 GLY A C 1 ATOM 1001 O O . GLY A 1 179 ? 22.028 39.725 12.974 1.00 33.20 ? 172 GLY A O 1 ATOM 1002 N N . ASP A 1 180 ? 22.105 41.867 12.265 1.00 30.91 ? 173 ASP A N 1 ATOM 1003 C CA . ASP A 1 180 ? 23.528 42.045 12.512 1.00 33.14 ? 173 ASP A CA 1 ATOM 1004 C C . ASP A 1 180 ? 23.737 42.641 13.892 1.00 29.86 ? 173 ASP A C 1 ATOM 1005 O O . ASP A 1 180 ? 22.995 43.535 14.314 1.00 28.47 ? 173 ASP A O 1 ATOM 1006 C CB . ASP A 1 180 ? 24.128 42.953 11.452 1.00 35.36 ? 173 ASP A CB 1 ATOM 1007 C CG . ASP A 1 180 ? 23.976 42.386 10.052 1.00 41.07 ? 173 ASP A CG 1 ATOM 1008 O OD1 . ASP A 1 180 ? 24.123 41.149 9.882 1.00 43.61 ? 173 ASP A OD1 1 ATOM 1009 O OD2 . ASP A 1 180 ? 23.701 43.177 9.119 1.00 38.97 ? 173 ASP A OD2 1 ATOM 1010 N N . LEU A 1 181 ? 24.758 42.147 14.584 1.00 29.20 ? 174 LEU A N 1 ATOM 1011 C CA . LEU A 1 181 ? 25.082 42.603 15.927 1.00 26.93 ? 174 LEU A CA 1 ATOM 1012 C C . LEU A 1 181 ? 25.840 43.929 15.925 1.00 28.93 ? 174 LEU A C 1 ATOM 1013 O O . LEU A 1 181 ? 26.713 44.157 15.088 1.00 29.59 ? 174 LEU A O 1 ATOM 1014 C CB . LEU A 1 181 ? 25.967 41.551 16.597 1.00 30.00 ? 174 LEU A CB 1 ATOM 1015 C CG A LEU A 1 181 ? 25.861 41.155 18.065 0.50 29.34 ? 174 LEU A CG 1 ATOM 1016 C CG B LEU A 1 181 ? 25.388 40.207 17.030 0.50 25.98 ? 174 LEU A CG 1 ATOM 1017 C CD1 A LEU A 1 181 ? 24.420 40.974 18.524 0.50 27.95 ? 174 LEU A CD1 1 ATOM 1018 C CD1 B LEU A 1 181 ? 26.490 39.368 17.656 0.50 27.23 ? 174 LEU A CD1 1 ATOM 1019 C CD2 A LEU A 1 181 ? 26.656 39.882 18.296 0.50 28.15 ? 174 LEU A CD2 1 ATOM 1020 C CD2 B LEU A 1 181 ? 24.220 40.371 17.992 0.50 25.45 ? 174 LEU A CD2 1 ATOM 1021 N N . VAL A 1 182 ? 25.515 44.788 16.886 1.00 27.44 ? 175 VAL A N 1 ATOM 1022 C CA . VAL A 1 182 ? 26.377 45.918 17.245 1.00 28.85 ? 175 VAL A CA 1 ATOM 1023 C C . VAL A 1 182 ? 26.715 45.783 18.731 1.00 26.31 ? 175 VAL A C 1 ATOM 1024 O O . VAL A 1 182 ? 25.826 45.549 19.558 1.00 27.47 ? 175 VAL A O 1 ATOM 1025 C CB . VAL A 1 182 ? 25.727 47.289 16.941 1.00 29.96 ? 175 VAL A CB 1 ATOM 1026 C CG1 . VAL A 1 182 ? 26.590 48.434 17.463 1.00 29.45 ? 175 VAL A CG1 1 ATOM 1027 C CG2 . VAL A 1 182 ? 25.507 47.444 15.449 1.00 32.29 ? 175 VAL A CG2 1 ATOM 1028 N N . TYR A 1 183 ? 28.004 45.878 19.054 1.00 26.19 ? 176 TYR A N 1 ATOM 1029 C CA . TYR A 1 183 ? 28.441 45.856 20.451 1.00 24.92 ? 176 TYR A CA 1 ATOM 1030 C C . TYR A 1 183 ? 28.459 47.280 21.023 1.00 25.80 ? 176 TYR A C 1 ATOM 1031 O O . TYR A 1 183 ? 29.098 48.175 20.453 1.00 27.18 ? 176 TYR A O 1 ATOM 1032 C CB . TYR A 1 183 ? 29.817 45.181 20.568 1.00 24.17 ? 176 TYR A CB 1 ATOM 1033 C CG . TYR A 1 183 ? 30.472 45.346 21.932 1.00 25.90 ? 176 TYR A CG 1 ATOM 1034 C CD1 . TYR A 1 183 ? 29.896 44.791 23.083 1.00 24.49 ? 176 TYR A CD1 1 ATOM 1035 C CD2 . TYR A 1 183 ? 31.664 46.057 22.067 1.00 24.61 ? 176 TYR A CD2 1 ATOM 1036 C CE1 . TYR A 1 183 ? 30.489 44.950 24.336 1.00 25.79 ? 176 TYR A CE1 1 ATOM 1037 C CE2 . TYR A 1 183 ? 32.268 46.218 23.308 1.00 27.14 ? 176 TYR A CE2 1 ATOM 1038 C CZ . TYR A 1 183 ? 31.686 45.656 24.438 1.00 24.94 ? 176 TYR A CZ 1 ATOM 1039 O OH . TYR A 1 183 ? 32.296 45.823 25.669 1.00 24.08 ? 176 TYR A OH 1 ATOM 1040 N N . VAL A 1 184 ? 27.741 47.470 22.138 1.00 24.24 ? 177 VAL A N 1 ATOM 1041 C CA . VAL A 1 184 ? 27.454 48.812 22.684 1.00 23.79 ? 177 VAL A CA 1 ATOM 1042 C C . VAL A 1 184 ? 28.060 49.041 24.069 1.00 23.85 ? 177 VAL A C 1 ATOM 1043 O O . VAL A 1 184 ? 27.593 49.893 24.832 1.00 24.30 ? 177 VAL A O 1 ATOM 1044 C CB . VAL A 1 184 ? 25.935 49.137 22.662 1.00 24.73 ? 177 VAL A CB 1 ATOM 1045 C CG1 . VAL A 1 184 ? 25.423 49.061 21.235 1.00 27.00 ? 177 VAL A CG1 1 ATOM 1046 C CG2 . VAL A 1 184 ? 25.131 48.180 23.551 1.00 24.16 ? 177 VAL A CG2 1 ATOM 1047 N N . ASN A 1 185 ? 29.102 48.268 24.390 1.00 23.71 ? 178 ASN A N 1 ATOM 1048 C CA . ASN A 1 185 ? 29.751 48.384 25.694 1.00 22.23 ? 178 ASN A CA 1 ATOM 1049 C C . ASN A 1 185 ? 28.699 48.162 26.800 1.00 21.87 ? 178 ASN A C 1 ATOM 1050 O O . ASN A 1 185 ? 27.983 47.158 26.765 1.00 23.09 ? 178 ASN A O 1 ATOM 1051 C CB . ASN A 1 185 ? 30.477 49.741 25.809 1.00 22.58 ? 178 ASN A CB 1 ATOM 1052 C CG . ASN A 1 185 ? 31.567 49.746 26.866 1.00 23.39 ? 178 ASN A CG 1 ATOM 1053 O OD1 . ASN A 1 185 ? 32.086 48.696 27.234 1.00 24.81 ? 178 ASN A OD1 1 ATOM 1054 N ND2 . ASN A 1 185 ? 31.907 50.937 27.374 1.00 23.16 ? 178 ASN A ND2 1 ATOM 1055 N N . TYR A 1 186 ? 28.578 49.083 27.757 1.00 21.68 ? 179 TYR A N 1 ATOM 1056 C CA . TYR A 1 186 ? 27.588 48.927 28.844 1.00 20.10 ? 179 TYR A CA 1 ATOM 1057 C C . TYR A 1 186 ? 26.194 49.459 28.498 1.00 21.60 ? 179 TYR A C 1 ATOM 1058 O O . TYR A 1 186 ? 25.307 49.464 29.369 1.00 20.64 ? 179 TYR A O 1 ATOM 1059 C CB . TYR A 1 186 ? 28.067 49.617 30.133 1.00 20.46 ? 179 TYR A CB 1 ATOM 1060 C CG . TYR A 1 186 ? 29.333 49.035 30.733 1.00 21.88 ? 179 TYR A CG 1 ATOM 1061 C CD1 . TYR A 1 186 ? 29.304 47.846 31.484 1.00 22.05 ? 179 TYR A CD1 1 ATOM 1062 C CD2 . TYR A 1 186 ? 30.567 49.695 30.583 1.00 21.64 ? 179 TYR A CD2 1 ATOM 1063 C CE1 . TYR A 1 186 ? 30.473 47.328 32.059 1.00 24.03 ? 179 TYR A CE1 1 ATOM 1064 C CE2 . TYR A 1 186 ? 31.733 49.184 31.149 1.00 23.84 ? 179 TYR A CE2 1 ATOM 1065 C CZ . TYR A 1 186 ? 31.684 48.013 31.891 1.00 22.64 ? 179 TYR A CZ 1 ATOM 1066 O OH . TYR A 1 186 ? 32.854 47.546 32.454 1.00 24.35 ? 179 TYR A OH 1 ATOM 1067 N N . ALA A 1 187 ? 25.999 49.885 27.240 1.00 21.14 ? 180 ALA A N 1 ATOM 1068 C CA . ALA A 1 187 ? 24.713 50.455 26.772 1.00 21.60 ? 180 ALA A CA 1 ATOM 1069 C C . ALA A 1 187 ? 24.271 51.660 27.616 1.00 20.91 ? 180 ALA A C 1 ATOM 1070 O O . ALA A 1 187 ? 23.075 51.929 27.764 1.00 20.68 ? 180 ALA A O 1 ATOM 1071 C CB . ALA A 1 187 ? 23.617 49.388 26.733 1.00 22.29 ? 180 ALA A CB 1 ATOM 1072 N N . ARG A 1 188 ? 25.245 52.377 28.175 1.00 20.94 ? 181 ARG A N 1 ATOM 1073 C CA . ARG A 1 188 ? 24.962 53.621 28.896 1.00 19.94 ? 181 ARG A CA 1 ATOM 1074 C C . ARG A 1 188 ? 24.663 54.756 27.918 1.00 20.56 ? 181 ARG A C 1 ATOM 1075 O O . ARG A 1 188 ? 25.025 54.689 26.745 1.00 21.59 ? 181 ARG A O 1 ATOM 1076 C CB . ARG A 1 188 ? 26.164 54.026 29.740 1.00 20.82 ? 181 ARG A CB 1 ATOM 1077 C CG . ARG A 1 188 ? 26.482 53.041 30.844 1.00 23.01 ? 181 ARG A CG 1 ATOM 1078 C CD . ARG A 1 188 ? 27.851 53.287 31.420 1.00 23.03 ? 181 ARG A CD 1 ATOM 1079 N NE . ARG A 1 188 ? 28.900 53.188 30.401 1.00 22.54 ? 181 ARG A NE 1 ATOM 1080 C CZ . ARG A 1 188 ? 30.199 53.343 30.634 1.00 24.27 ? 181 ARG A CZ 1 ATOM 1081 N NH1 . ARG A 1 188 ? 30.640 53.608 31.865 1.00 26.35 ? 181 ARG A NH1 1 ATOM 1082 N NH2 . ARG A 1 188 ? 31.058 53.239 29.628 1.00 26.66 ? 181 ARG A NH2 1 ATOM 1083 N N . THR A 1 189 ? 24.058 55.827 28.425 1.00 20.62 ? 182 THR A N 1 ATOM 1084 C CA . THR A 1 189 ? 23.777 56.997 27.601 1.00 20.56 ? 182 THR A CA 1 ATOM 1085 C C . THR A 1 189 ? 25.045 57.452 26.861 1.00 22.42 ? 182 THR A C 1 ATOM 1086 O O . THR A 1 189 ? 25.015 57.700 25.639 1.00 24.15 ? 182 THR A O 1 ATOM 1087 C CB . THR A 1 189 ? 23.200 58.127 28.466 1.00 20.63 ? 182 THR A CB 1 ATOM 1088 O OG1 . THR A 1 189 ? 21.929 57.703 28.995 1.00 21.26 ? 182 THR A OG1 1 ATOM 1089 C CG2 . THR A 1 189 ? 23.018 59.417 27.649 1.00 21.95 ? 182 THR A CG2 1 ATOM 1090 N N . GLU A 1 190 ? 26.165 57.540 27.585 1.00 24.27 ? 183 GLU A N 1 ATOM 1091 C CA . GLU A 1 190 ? 27.429 57.978 26.969 1.00 25.44 ? 183 GLU A CA 1 ATOM 1092 C C . GLU A 1 190 ? 28.002 56.977 25.954 1.00 25.06 ? 183 GLU A C 1 ATOM 1093 O O . GLU A 1 190 ? 28.711 57.368 25.017 1.00 26.71 ? 183 GLU A O 1 ATOM 1094 C CB . GLU A 1 190 ? 28.474 58.322 28.029 1.00 26.23 ? 183 GLU A CB 1 ATOM 1095 C CG . GLU A 1 190 ? 28.899 57.160 28.913 1.00 28.70 ? 183 GLU A CG 1 ATOM 1096 C CD . GLU A 1 190 ? 28.138 57.094 30.224 1.00 31.89 ? 183 GLU A CD 1 ATOM 1097 O OE1 . GLU A 1 190 ? 26.914 57.441 30.264 1.00 28.75 ? 183 GLU A OE1 1 ATOM 1098 O OE2 . GLU A 1 190 ? 28.784 56.681 31.219 1.00 31.13 ? 183 GLU A OE2 1 ATOM 1099 N N . ASP A 1 191 ? 27.687 55.693 26.125 1.00 24.18 ? 184 ASP A N 1 ATOM 1100 C CA . ASP A 1 191 ? 28.133 54.672 25.153 1.00 24.56 ? 184 ASP A CA 1 ATOM 1101 C C . ASP A 1 191 ? 27.396 54.879 23.837 1.00 25.34 ? 184 ASP A C 1 ATOM 1102 O O . ASP A 1 191 ? 27.993 54.791 22.759 1.00 25.91 ? 184 ASP A O 1 ATOM 1103 C CB . ASP A 1 191 ? 27.850 53.256 25.697 1.00 24.23 ? 184 ASP A CB 1 ATOM 1104 C CG . ASP A 1 191 ? 28.705 52.925 26.899 1.00 23.00 ? 184 ASP A CG 1 ATOM 1105 O OD1 . ASP A 1 191 ? 29.883 53.360 26.907 1.00 25.01 ? 184 ASP A OD1 1 ATOM 1106 O OD2 . ASP A 1 191 ? 28.212 52.247 27.823 1.00 21.77 ? 184 ASP A OD2 1 ATOM 1107 N N . PHE A 1 192 ? 26.093 55.167 23.929 1.00 23.61 ? 185 PHE A N 1 ATOM 1108 C CA . PHE A 1 192 ? 25.318 55.467 22.730 1.00 23.95 ? 185 PHE A CA 1 ATOM 1109 C C . PHE A 1 192 ? 25.699 56.806 22.111 1.00 24.05 ? 185 PHE A C 1 ATOM 1110 O O . PHE A 1 192 ? 25.732 56.922 20.880 1.00 26.61 ? 185 PHE A O 1 ATOM 1111 C CB . PHE A 1 192 ? 23.803 55.335 22.983 1.00 22.47 ? 185 PHE A CB 1 ATOM 1112 C CG . PHE A 1 192 ? 23.335 53.908 23.004 1.00 21.02 ? 185 PHE A CG 1 ATOM 1113 C CD1 . PHE A 1 192 ? 23.004 53.275 24.205 1.00 23.57 ? 185 PHE A CD1 1 ATOM 1114 C CD2 . PHE A 1 192 ? 23.239 53.185 21.816 1.00 21.63 ? 185 PHE A CD2 1 ATOM 1115 C CE1 . PHE A 1 192 ? 22.572 51.941 24.213 1.00 22.15 ? 185 PHE A CE1 1 ATOM 1116 C CE2 . PHE A 1 192 ? 22.827 51.854 21.821 1.00 21.91 ? 185 PHE A CE2 1 ATOM 1117 C CZ . PHE A 1 192 ? 22.499 51.228 23.018 1.00 22.09 ? 185 PHE A CZ 1 ATOM 1118 N N . PHE A 1 193 ? 25.988 57.818 22.936 1.00 25.09 ? 186 PHE A N 1 ATOM 1119 C CA . PHE A 1 193 ? 26.545 59.071 22.399 1.00 26.62 ? 186 PHE A CA 1 ATOM 1120 C C . PHE A 1 193 ? 27.799 58.775 21.562 1.00 29.38 ? 186 PHE A C 1 ATOM 1121 O O . PHE A 1 193 ? 27.933 59.256 20.425 1.00 30.18 ? 186 PHE A O 1 ATOM 1122 C CB . PHE A 1 193 ? 26.907 60.070 23.515 1.00 28.60 ? 186 PHE A CB 1 ATOM 1123 C CG . PHE A 1 193 ? 25.733 60.806 24.120 1.00 28.03 ? 186 PHE A CG 1 ATOM 1124 C CD1 . PHE A 1 193 ? 24.486 60.849 23.508 1.00 29.43 ? 186 PHE A CD1 1 ATOM 1125 C CD2 . PHE A 1 193 ? 25.909 61.499 25.315 1.00 29.07 ? 186 PHE A CD2 1 ATOM 1126 C CE1 . PHE A 1 193 ? 23.430 61.550 24.097 1.00 27.92 ? 186 PHE A CE1 1 ATOM 1127 C CE2 . PHE A 1 193 ? 24.868 62.203 25.908 1.00 27.05 ? 186 PHE A CE2 1 ATOM 1128 C CZ . PHE A 1 193 ? 23.622 62.234 25.293 1.00 25.75 ? 186 PHE A CZ 1 ATOM 1129 N N . LYS A 1 194 ? 28.715 57.976 22.117 1.00 28.65 ? 187 LYS A N 1 ATOM 1130 C CA . LYS A 1 194 ? 29.980 57.655 21.430 1.00 29.05 ? 187 LYS A CA 1 ATOM 1131 C C . LYS A 1 194 ? 29.728 56.941 20.092 1.00 31.67 ? 187 LYS A C 1 ATOM 1132 O O . LYS A 1 194 ? 30.368 57.258 19.089 1.00 34.32 ? 187 LYS A O 1 ATOM 1133 C CB . LYS A 1 194 ? 30.890 56.818 22.335 1.00 30.89 ? 187 LYS A CB 1 ATOM 1134 C CG . LYS A 1 194 ? 32.186 56.319 21.678 1.00 36.45 ? 187 LYS A CG 1 ATOM 1135 C CD . LYS A 1 194 ? 33.342 57.283 21.880 1.00 43.38 ? 187 LYS A CD 1 ATOM 1136 C CE . LYS A 1 194 ? 33.976 57.048 23.242 1.00 51.21 ? 187 LYS A CE 1 ATOM 1137 N NZ . LYS A 1 194 ? 34.688 58.253 23.739 1.00 61.32 ? 187 LYS A NZ 1 ATOM 1138 N N . LEU A 1 195 ? 28.799 55.983 20.078 1.00 30.31 ? 188 LEU A N 1 ATOM 1139 C CA . LEU A 1 195 ? 28.452 55.269 18.841 1.00 30.96 ? 188 LEU A CA 1 ATOM 1140 C C . LEU A 1 195 ? 27.886 56.168 17.753 1.00 33.20 ? 188 LEU A C 1 ATOM 1141 O O . LEU A 1 195 ? 28.437 56.210 16.654 1.00 33.73 ? 188 LEU A O 1 ATOM 1142 C CB . LEU A 1 195 ? 27.450 54.148 19.101 1.00 31.88 ? 188 LEU A CB 1 ATOM 1143 C CG . LEU A 1 195 ? 27.993 52.893 19.743 1.00 33.07 ? 188 LEU A CG 1 ATOM 1144 C CD1 . LEU A 1 195 ? 26.827 52.088 20.305 1.00 34.22 ? 188 LEU A CD1 1 ATOM 1145 C CD2 . LEU A 1 195 ? 28.803 52.100 18.730 1.00 35.87 ? 188 LEU A CD2 1 ATOM 1146 N N A GLU A 1 196 ? 26.794 56.878 18.047 0.60 34.63 ? 189 GLU A N 1 ATOM 1147 N N B GLU A 1 196 ? 26.795 56.874 18.064 0.40 33.96 ? 189 GLU A N 1 ATOM 1148 C CA A GLU A 1 196 ? 26.124 57.670 17.008 0.60 35.55 ? 189 GLU A CA 1 ATOM 1149 C CA B GLU A 1 196 ? 26.093 57.696 17.076 0.40 34.00 ? 189 GLU A CA 1 ATOM 1150 C C A GLU A 1 196 ? 26.802 58.999 16.698 0.60 35.77 ? 189 GLU A C 1 ATOM 1151 C C B GLU A 1 196 ? 26.868 58.952 16.711 0.40 34.76 ? 189 GLU A C 1 ATOM 1152 O O A GLU A 1 196 ? 26.919 59.365 15.524 0.60 34.99 ? 189 GLU A O 1 ATOM 1153 O O B GLU A 1 196 ? 27.109 59.219 15.531 0.40 34.49 ? 189 GLU A O 1 ATOM 1154 C CB A GLU A 1 196 ? 24.608 57.853 17.257 0.60 39.49 ? 189 GLU A CB 1 ATOM 1155 C CB B GLU A 1 196 ? 24.683 58.086 17.553 0.40 32.48 ? 189 GLU A CB 1 ATOM 1156 C CG A GLU A 1 196 ? 24.109 57.618 18.669 0.60 41.92 ? 189 GLU A CG 1 ATOM 1157 C CG B GLU A 1 196 ? 24.043 59.152 16.663 0.40 35.11 ? 189 GLU A CG 1 ATOM 1158 C CD A GLU A 1 196 ? 23.265 56.353 18.815 0.60 43.59 ? 189 GLU A CD 1 ATOM 1159 C CD B GLU A 1 196 ? 22.604 59.468 17.024 0.40 35.33 ? 189 GLU A CD 1 ATOM 1160 O OE1 A GLU A 1 196 ? 22.112 56.330 18.331 0.60 45.33 ? 189 GLU A OE1 1 ATOM 1161 O OE1 B GLU A 1 196 ? 21.742 58.583 16.868 0.40 33.13 ? 189 GLU A OE1 1 ATOM 1162 O OE2 A GLU A 1 196 ? 23.738 55.387 19.443 0.60 37.82 ? 189 GLU A OE2 1 ATOM 1163 O OE2 B GLU A 1 196 ? 22.330 60.614 17.439 0.40 34.38 ? 189 GLU A OE2 1 ATOM 1164 N N . ARG A 1 197 ? 27.257 59.713 17.729 1.00 33.27 ? 190 ARG A N 1 ATOM 1165 C CA . ARG A 1 197 ? 27.879 61.036 17.526 1.00 33.80 ? 190 ARG A CA 1 ATOM 1166 C C . ARG A 1 197 ? 29.331 61.005 17.058 1.00 34.96 ? 190 ARG A C 1 ATOM 1167 O O . ARG A 1 197 ? 29.687 61.728 16.121 1.00 37.52 ? 190 ARG A O 1 ATOM 1168 C CB . ARG A 1 197 ? 27.741 61.902 18.781 1.00 32.27 ? 190 ARG A CB 1 ATOM 1169 C CG . ARG A 1 197 ? 26.303 62.091 19.209 1.00 27.88 ? 190 ARG A CG 1 ATOM 1170 C CD . ARG A 1 197 ? 26.224 62.843 20.516 1.00 28.14 ? 190 ARG A CD 1 ATOM 1171 N NE . ARG A 1 197 ? 24.850 63.199 20.830 1.00 29.75 ? 190 ARG A NE 1 ATOM 1172 C CZ . ARG A 1 197 ? 24.493 63.956 21.867 1.00 27.48 ? 190 ARG A CZ 1 ATOM 1173 N NH1 . ARG A 1 197 ? 25.411 64.443 22.697 1.00 26.33 ? 190 ARG A NH1 1 ATOM 1174 N NH2 . ARG A 1 197 ? 23.219 64.236 22.069 1.00 29.75 ? 190 ARG A NH2 1 ATOM 1175 N N . ASP A 1 198 ? 30.162 60.187 17.707 1.00 34.18 ? 191 ASP A N 1 ATOM 1176 C CA . ASP A 1 198 ? 31.592 60.118 17.383 1.00 35.66 ? 191 ASP A CA 1 ATOM 1177 C C . ASP A 1 198 ? 31.923 59.083 16.311 1.00 36.47 ? 191 ASP A C 1 ATOM 1178 O O . ASP A 1 198 ? 32.614 59.392 15.332 1.00 37.48 ? 191 ASP A O 1 ATOM 1179 C CB . ASP A 1 198 ? 32.426 59.849 18.636 1.00 37.53 ? 191 ASP A CB 1 ATOM 1180 C CG . ASP A 1 198 ? 32.186 60.865 19.721 1.00 42.65 ? 191 ASP A CG 1 ATOM 1181 O OD1 . ASP A 1 198 ? 31.772 61.996 19.390 1.00 47.43 ? 191 ASP A OD1 1 ATOM 1182 O OD2 . ASP A 1 198 ? 32.410 60.531 20.903 0.80 46.43 ? 191 ASP A OD2 1 ATOM 1183 N N . MET A 1 199 ? 31.425 57.864 16.487 1.00 36.96 ? 192 MET A N 1 ATOM 1184 C CA . MET A 1 199 ? 31.776 56.764 15.588 1.00 35.90 ? 192 MET A CA 1 ATOM 1185 C C . MET A 1 199 ? 30.877 56.679 14.354 1.00 37.27 ? 192 MET A C 1 ATOM 1186 O O . MET A 1 199 ? 31.219 55.995 13.384 1.00 37.76 ? 192 MET A O 1 ATOM 1187 C CB . MET A 1 199 ? 31.759 55.435 16.348 1.00 35.57 ? 192 MET A CB 1 ATOM 1188 C CG . MET A 1 199 ? 32.742 55.368 17.503 1.00 38.45 ? 192 MET A CG 1 ATOM 1189 S SD . MET A 1 199 ? 32.768 53.732 18.253 1.00 38.09 ? 192 MET A SD 1 ATOM 1190 C CE . MET A 1 199 ? 33.879 52.874 17.121 1.00 39.81 ? 192 MET A CE 1 ATOM 1191 N N . LYS A 1 200 ? 29.734 57.364 14.400 1.00 36.05 ? 193 LYS A N 1 ATOM 1192 C CA . LYS A 1 200 ? 28.769 57.397 13.297 1.00 35.24 ? 193 LYS A CA 1 ATOM 1193 C C . LYS A 1 200 ? 28.265 55.998 12.952 1.00 39.91 ? 193 LYS A C 1 ATOM 1194 O O . LYS A 1 200 ? 28.137 55.632 11.781 1.00 42.86 ? 193 LYS A O 1 ATOM 1195 C CB . LYS A 1 200 ? 29.340 58.136 12.066 1.00 36.54 ? 193 LYS A CB 1 ATOM 1196 C CG . LYS A 1 200 ? 29.193 59.652 12.138 1.00 44.81 ? 193 LYS A CG 1 ATOM 1197 C CD . LYS A 1 200 ? 30.264 60.309 12.998 1.00 47.63 ? 193 LYS A CD 1 ATOM 1198 C CE . LYS A 1 200 ? 30.337 61.814 12.770 1.00 50.13 ? 193 LYS A CE 1 ATOM 1199 N NZ . LYS A 1 200 ? 29.143 62.544 13.284 1.00 51.42 ? 193 LYS A NZ 1 ATOM 1200 N N . ILE A 1 201 ? 27.991 55.220 13.999 1.00 37.23 ? 194 ILE A N 1 ATOM 1201 C CA . ILE A 1 201 ? 27.457 53.871 13.851 1.00 39.05 ? 194 ILE A CA 1 ATOM 1202 C C . ILE A 1 201 ? 25.965 53.911 14.187 1.00 36.58 ? 194 ILE A C 1 ATOM 1203 O O . ILE A 1 201 ? 25.560 54.445 15.220 1.00 39.38 ? 194 ILE A O 1 ATOM 1204 C CB . ILE A 1 201 ? 28.276 52.844 14.677 1.00 39.48 ? 194 ILE A CB 1 ATOM 1205 C CG1 . ILE A 1 201 ? 29.603 52.552 13.955 1.00 41.30 ? 194 ILE A CG1 1 ATOM 1206 C CG2 . ILE A 1 201 ? 27.497 51.547 14.897 1.00 37.22 ? 194 ILE A CG2 1 ATOM 1207 C CD1 . ILE A 1 201 ? 30.733 52.068 14.841 1.00 43.49 ? 194 ILE A CD1 1 ATOM 1208 N N . ASN A 1 202 ? 25.153 53.392 13.272 1.00 36.60 ? 195 ASN A N 1 ATOM 1209 C CA . ASN A 1 202 ? 23.698 53.470 13.374 1.00 38.10 ? 195 ASN A CA 1 ATOM 1210 C C . ASN A 1 202 ? 23.156 52.135 13.898 1.00 36.45 ? 195 ASN A C 1 ATOM 1211 O O . ASN A 1 202 ? 23.374 51.089 13.269 1.00 35.99 ? 195 ASN A O 1 ATOM 1212 C CB . ASN A 1 202 ? 23.131 53.837 11.983 1.00 42.59 ? 195 ASN A CB 1 ATOM 1213 C CG . ASN A 1 202 ? 21.619 54.035 11.968 1.00 48.05 ? 195 ASN A CG 1 ATOM 1214 O OD1 . ASN A 1 202 ? 20.938 53.839 12.972 1.00 41.43 ? 195 ASN A OD1 1 ATOM 1215 N ND2 . ASN A 1 202 ? 21.089 54.430 10.801 1.00 55.37 ? 195 ASN A ND2 1 ATOM 1216 N N . CYS A 1 203 ? 22.487 52.166 15.058 1.00 35.04 ? 196 CYS A N 1 ATOM 1217 C CA . CYS A 1 203 ? 21.939 50.949 15.654 1.00 33.57 ? 196 CYS A CA 1 ATOM 1218 C C . CYS A 1 203 ? 20.577 50.561 15.102 1.00 34.37 ? 196 CYS A C 1 ATOM 1219 O O . CYS A 1 203 ? 20.032 49.519 15.482 1.00 34.01 ? 196 CYS A O 1 ATOM 1220 C CB . CYS A 1 203 ? 21.861 51.061 17.186 1.00 36.33 ? 196 CYS A CB 1 ATOM 1221 S SG . CYS A 1 203 ? 23.479 51.018 17.973 1.00 36.69 ? 196 CYS A SG 1 ATOM 1222 N N . SER A 1 204 ? 20.026 51.381 14.208 1.00 33.98 ? 197 SER A N 1 ATOM 1223 C CA . SER A 1 204 ? 18.663 51.162 13.734 1.00 35.21 ? 197 SER A CA 1 ATOM 1224 C C . SER A 1 204 ? 18.511 49.826 13.008 1.00 35.15 ? 197 SER A C 1 ATOM 1225 O O . SER A 1 204 ? 19.185 49.569 12.007 1.00 39.65 ? 197 SER A O 1 ATOM 1226 C CB . SER A 1 204 ? 18.213 52.312 12.838 1.00 38.10 ? 197 SER A CB 1 ATOM 1227 O OG . SER A 1 204 ? 16.970 52.023 12.233 1.00 39.36 ? 197 SER A OG 1 ATOM 1228 N N . GLY A 1 205 ? 17.632 48.971 13.525 1.00 33.79 ? 198 GLY A N 1 ATOM 1229 C CA . GLY A 1 205 ? 17.391 47.666 12.910 1.00 32.38 ? 198 GLY A CA 1 ATOM 1230 C C . GLY A 1 205 ? 18.453 46.622 13.210 1.00 32.19 ? 198 GLY A C 1 ATOM 1231 O O . GLY A 1 205 ? 18.426 45.543 12.633 1.00 32.30 ? 198 GLY A O 1 ATOM 1232 N N . LYS A 1 206 ? 19.378 46.937 14.122 1.00 32.84 ? 199 LYS A N 1 ATOM 1233 C CA . LYS A 1 206 ? 20.436 46.006 14.534 1.00 30.64 ? 199 LYS A CA 1 ATOM 1234 C C . LYS A 1 206 ? 20.065 45.322 15.847 1.00 28.71 ? 199 LYS A C 1 ATOM 1235 O O . LYS A 1 206 ? 19.247 45.834 16.615 1.00 28.42 ? 199 LYS A O 1 ATOM 1236 C CB . LYS A 1 206 ? 21.761 46.747 14.717 1.00 30.35 ? 199 LYS A CB 1 ATOM 1237 C CG . LYS A 1 206 ? 22.229 47.527 13.497 1.00 31.13 ? 199 LYS A CG 1 ATOM 1238 C CD . LYS A 1 206 ? 22.800 46.601 12.435 1.00 35.74 ? 199 LYS A CD 1 ATOM 1239 C CE . LYS A 1 206 ? 23.312 47.395 11.248 1.00 42.37 ? 199 LYS A CE 1 ATOM 1240 N NZ . LYS A 1 206 ? 22.199 47.835 10.364 1.00 47.52 ? 199 LYS A NZ 1 ATOM 1241 N N . ILE A 1 207 ? 20.660 44.158 16.098 1.00 28.05 ? 200 ILE A N 1 ATOM 1242 C CA . ILE A 1 207 ? 20.576 43.551 17.426 1.00 28.09 ? 200 ILE A CA 1 ATOM 1243 C C . ILE A 1 207 ? 21.774 44.037 18.223 1.00 29.55 ? 200 ILE A C 1 ATOM 1244 O O . ILE A 1 207 ? 22.917 43.906 17.787 1.00 30.05 ? 200 ILE A O 1 ATOM 1245 C CB . ILE A 1 207 ? 20.516 42.014 17.359 1.00 27.81 ? 200 ILE A CB 1 ATOM 1246 C CG1 . ILE A 1 207 ? 19.181 41.593 16.732 1.00 29.03 ? 200 ILE A CG1 1 ATOM 1247 C CG2 . ILE A 1 207 ? 20.657 41.405 18.753 1.00 27.22 ? 200 ILE A CG2 1 ATOM 1248 C CD1 . ILE A 1 207 ? 19.137 40.143 16.324 1.00 31.70 ? 200 ILE A CD1 1 ATOM 1249 N N . VAL A 1 208 ? 21.518 44.627 19.383 1.00 24.95 ? 201 VAL A N 1 ATOM 1250 C CA . VAL A 1 208 ? 22.613 45.195 20.151 1.00 24.98 ? 201 VAL A CA 1 ATOM 1251 C C . VAL A 1 208 ? 23.051 44.174 21.199 1.00 24.98 ? 201 VAL A C 1 ATOM 1252 O O . VAL A 1 208 ? 22.223 43.490 21.784 1.00 25.56 ? 201 VAL A O 1 ATOM 1253 C CB . VAL A 1 208 ? 22.228 46.589 20.734 1.00 26.56 ? 201 VAL A CB 1 ATOM 1254 C CG1 A VAL A 1 208 ? 21.909 47.577 19.617 0.50 25.75 ? 201 VAL A CG1 1 ATOM 1255 C CG1 B VAL A 1 208 ? 22.512 46.730 22.227 0.50 26.44 ? 201 VAL A CG1 1 ATOM 1256 C CG2 A VAL A 1 208 ? 21.105 46.490 21.750 0.50 22.44 ? 201 VAL A CG2 1 ATOM 1257 C CG2 B VAL A 1 208 ? 22.807 47.714 19.886 0.50 28.06 ? 201 VAL A CG2 1 ATOM 1258 N N . ILE A 1 209 ? 24.359 44.033 21.386 1.00 23.24 ? 202 ILE A N 1 ATOM 1259 C CA . ILE A 1 209 ? 24.862 43.218 22.491 1.00 23.20 ? 202 ILE A CA 1 ATOM 1260 C C . ILE A 1 209 ? 25.583 44.122 23.486 1.00 23.33 ? 202 ILE A C 1 ATOM 1261 O O . ILE A 1 209 ? 26.469 44.906 23.110 1.00 23.87 ? 202 ILE A O 1 ATOM 1262 C CB . ILE A 1 209 ? 25.731 42.024 22.003 1.00 21.97 ? 202 ILE A CB 1 ATOM 1263 C CG1 . ILE A 1 209 ? 26.222 41.164 23.180 1.00 24.52 ? 202 ILE A CG1 1 ATOM 1264 C CG2 . ILE A 1 209 ? 26.898 42.495 21.121 1.00 22.33 ? 202 ILE A CG2 1 ATOM 1265 C CD1 . ILE A 1 209 ? 26.627 39.751 22.766 1.00 25.88 ? 202 ILE A CD1 1 ATOM 1266 N N . ALA A 1 210 ? 25.168 44.032 24.745 1.00 22.52 ? 203 ALA A N 1 ATOM 1267 C CA . ALA A 1 210 ? 25.687 44.909 25.789 1.00 21.68 ? 203 ALA A CA 1 ATOM 1268 C C . ALA A 1 210 ? 26.186 44.087 26.969 1.00 21.86 ? 203 ALA A C 1 ATOM 1269 O O . ALA A 1 210 ? 25.559 43.093 27.366 1.00 23.13 ? 203 ALA A O 1 ATOM 1270 C CB . ALA A 1 210 ? 24.598 45.872 26.250 1.00 21.84 ? 203 ALA A CB 1 ATOM 1271 N N . ARG A 1 211 ? 27.313 44.496 27.545 1.00 21.79 ? 204 ARG A N 1 ATOM 1272 C CA . ARG A 1 211 ? 27.707 43.873 28.816 1.00 21.28 ? 204 ARG A CA 1 ATOM 1273 C C . ARG A 1 211 ? 26.965 44.460 30.017 1.00 20.53 ? 204 ARG A C 1 ATOM 1274 O O . ARG A 1 211 ? 26.698 45.674 30.094 1.00 19.73 ? 204 ARG A O 1 ATOM 1275 C CB . ARG A 1 211 ? 29.218 43.873 29.025 1.00 24.12 ? 204 ARG A CB 1 ATOM 1276 C CG . ARG A 1 211 ? 29.901 45.197 28.807 1.00 24.75 ? 204 ARG A CG 1 ATOM 1277 C CD . ARG A 1 211 ? 31.320 45.064 29.310 1.00 24.82 ? 204 ARG A CD 1 ATOM 1278 N NE . ARG A 1 211 ? 32.126 46.232 28.972 1.00 25.52 ? 204 ARG A NE 1 ATOM 1279 C CZ . ARG A 1 211 ? 33.366 46.429 29.419 1.00 24.46 ? 204 ARG A CZ 1 ATOM 1280 N NH1 . ARG A 1 211 ? 33.927 45.552 30.248 1.00 25.16 ? 204 ARG A NH1 1 ATOM 1281 N NH2 . ARG A 1 211 ? 34.032 47.520 29.058 1.00 25.27 ? 204 ARG A NH2 1 ATOM 1282 N N . TYR A 1 212 ? 26.610 43.582 30.949 1.00 19.62 ? 205 TYR A N 1 ATOM 1283 C CA . TYR A 1 212 ? 26.003 44.009 32.192 1.00 18.35 ? 205 TYR A CA 1 ATOM 1284 C C . TYR A 1 212 ? 27.031 44.834 32.983 1.00 19.82 ? 205 TYR A C 1 ATOM 1285 O O . TYR A 1 212 ? 28.242 44.691 32.781 1.00 20.91 ? 205 TYR A O 1 ATOM 1286 C CB . TYR A 1 212 ? 25.667 42.765 32.990 1.00 19.73 ? 205 TYR A CB 1 ATOM 1287 C CG . TYR A 1 212 ? 24.306 42.144 32.845 1.00 18.88 ? 205 TYR A CG 1 ATOM 1288 C CD1 . TYR A 1 212 ? 24.181 40.749 32.660 1.00 18.77 ? 205 TYR A CD1 1 ATOM 1289 C CD2 . TYR A 1 212 ? 23.137 42.904 32.993 1.00 16.86 ? 205 TYR A CD2 1 ATOM 1290 C CE1 . TYR A 1 212 ? 22.928 40.143 32.611 1.00 18.30 ? 205 TYR A CE1 1 ATOM 1291 C CE2 . TYR A 1 212 ? 21.879 42.305 32.968 1.00 17.46 ? 205 TYR A CE2 1 ATOM 1292 C CZ . TYR A 1 212 ? 21.778 40.930 32.776 1.00 18.22 ? 205 TYR A CZ 1 ATOM 1293 O OH . TYR A 1 212 ? 20.538 40.342 32.788 1.00 17.92 ? 205 TYR A OH 1 ATOM 1294 N N . GLY A 1 213 ? 26.555 45.681 33.883 1.00 20.19 ? 206 GLY A N 1 ATOM 1295 C CA . GLY A 1 213 ? 27.447 46.459 34.742 1.00 22.10 ? 206 GLY A CA 1 ATOM 1296 C C . GLY A 1 213 ? 27.163 47.935 34.620 1.00 20.57 ? 206 GLY A C 1 ATOM 1297 O O . GLY A 1 213 ? 26.511 48.370 33.662 1.00 21.06 ? 206 GLY A O 1 ATOM 1298 N N . LYS A 1 214 ? 27.644 48.691 35.606 1.00 20.10 ? 207 LYS A N 1 ATOM 1299 C CA . LYS A 1 214 ? 27.601 50.177 35.625 1.00 19.68 ? 207 LYS A CA 1 ATOM 1300 C C . LYS A 1 214 ? 26.238 50.787 35.855 1.00 20.19 ? 207 LYS A C 1 ATOM 1301 O O . LYS A 1 214 ? 26.120 51.721 36.650 1.00 22.03 ? 207 LYS A O 1 ATOM 1302 C CB . LYS A 1 214 ? 28.216 50.806 34.360 1.00 20.86 ? 207 LYS A CB 1 ATOM 1303 C CG . LYS A 1 214 ? 29.661 50.397 34.043 1.00 24.24 ? 207 LYS A CG 1 ATOM 1304 C CD . LYS A 1 214 ? 30.633 50.678 35.178 1.00 29.11 ? 207 LYS A CD 1 ATOM 1305 C CE . LYS A 1 214 ? 32.027 50.190 34.801 1.00 29.31 ? 207 LYS A CE 1 ATOM 1306 N NZ . LYS A 1 214 ? 33.006 50.442 35.907 1.00 33.59 ? 207 LYS A NZ 1 ATOM 1307 N N . VAL A 1 215 ? 25.213 50.311 35.144 1.00 19.45 ? 208 VAL A N 1 ATOM 1308 C CA . VAL A 1 215 ? 23.870 50.902 35.264 1.00 18.86 ? 208 VAL A CA 1 ATOM 1309 C C . VAL A 1 215 ? 22.821 49.802 35.286 1.00 18.11 ? 208 VAL A C 1 ATOM 1310 O O . VAL A 1 215 ? 23.067 48.672 34.805 1.00 18.95 ? 208 VAL A O 1 ATOM 1311 C CB . VAL A 1 215 ? 23.538 51.940 34.133 1.00 18.94 ? 208 VAL A CB 1 ATOM 1312 C CG1 . VAL A 1 215 ? 24.572 53.078 34.084 1.00 19.69 ? 208 VAL A CG1 1 ATOM 1313 C CG2 . VAL A 1 215 ? 23.406 51.278 32.760 1.00 22.10 ? 208 VAL A CG2 1 ATOM 1314 N N . PHE A 1 216 ? 21.654 50.131 35.827 1.00 17.50 ? 209 PHE A N 1 ATOM 1315 C CA . PHE A 1 216 ? 20.495 49.227 35.796 1.00 15.63 ? 209 PHE A CA 1 ATOM 1316 C C . PHE A 1 216 ? 20.162 48.744 34.375 1.00 16.66 ? 209 PHE A C 1 ATOM 1317 O O . PHE A 1 216 ? 20.119 49.543 33.406 1.00 16.52 ? 209 PHE A O 1 ATOM 1318 C CB . PHE A 1 216 ? 19.289 49.947 36.428 1.00 15.65 ? 209 PHE A CB 1 ATOM 1319 C CG . PHE A 1 216 ? 18.004 49.185 36.335 1.00 14.30 ? 209 PHE A CG 1 ATOM 1320 C CD1 . PHE A 1 216 ? 17.884 47.931 36.953 1.00 15.07 ? 209 PHE A CD1 1 ATOM 1321 C CD2 . PHE A 1 216 ? 16.880 49.741 35.682 1.00 16.20 ? 209 PHE A CD2 1 ATOM 1322 C CE1 . PHE A 1 216 ? 16.685 47.206 36.900 1.00 18.14 ? 209 PHE A CE1 1 ATOM 1323 C CE2 . PHE A 1 216 ? 15.676 49.025 35.644 1.00 17.80 ? 209 PHE A CE2 1 ATOM 1324 C CZ . PHE A 1 216 ? 15.586 47.755 36.242 1.00 16.83 ? 209 PHE A CZ 1 ATOM 1325 N N . ARG A 1 217 ? 19.924 47.440 34.232 1.00 17.29 ? 210 ARG A N 1 ATOM 1326 C CA . ARG A 1 217 ? 19.700 46.862 32.884 1.00 16.66 ? 210 ARG A CA 1 ATOM 1327 C C . ARG A 1 217 ? 18.462 47.437 32.165 1.00 17.17 ? 210 ARG A C 1 ATOM 1328 O O . ARG A 1 217 ? 18.424 47.454 30.940 1.00 18.02 ? 210 ARG A O 1 ATOM 1329 C CB . ARG A 1 217 ? 19.640 45.331 32.951 1.00 16.11 ? 210 ARG A CB 1 ATOM 1330 C CG . ARG A 1 217 ? 18.401 44.824 33.706 1.00 14.84 ? 210 ARG A CG 1 ATOM 1331 C CD . ARG A 1 217 ? 18.398 43.293 33.887 1.00 14.53 ? 210 ARG A CD 1 ATOM 1332 N NE . ARG A 1 217 ? 19.175 42.879 35.062 1.00 15.20 ? 210 ARG A NE 1 ATOM 1333 C CZ . ARG A 1 217 ? 18.762 43.066 36.318 1.00 15.37 ? 210 ARG A CZ 1 ATOM 1334 N NH1 . ARG A 1 217 ? 17.586 43.662 36.548 1.00 15.27 ? 210 ARG A NH1 1 ATOM 1335 N NH2 . ARG A 1 217 ? 19.520 42.667 37.348 1.00 16.81 ? 210 ARG A NH2 1 ATOM 1336 N N . GLY A 1 218 ? 17.460 47.915 32.915 1.00 16.32 ? 211 GLY A N 1 ATOM 1337 C CA . GLY A 1 218 ? 16.303 48.566 32.289 1.00 18.49 ? 211 GLY A CA 1 ATOM 1338 C C . GLY A 1 218 ? 16.708 49.833 31.544 1.00 16.65 ? 211 GLY A C 1 ATOM 1339 O O . GLY A 1 218 ? 16.161 50.130 30.473 1.00 18.36 ? 211 GLY A O 1 ATOM 1340 N N . ASN A 1 219 ? 17.650 50.595 32.104 1.00 17.79 ? 212 ASN A N 1 ATOM 1341 C CA . ASN A 1 219 ? 18.169 51.765 31.387 1.00 17.41 ? 212 ASN A CA 1 ATOM 1342 C C . ASN A 1 219 ? 18.907 51.398 30.100 1.00 19.01 ? 212 ASN A C 1 ATOM 1343 O O . ASN A 1 219 ? 18.768 52.092 29.092 1.00 19.57 ? 212 ASN A O 1 ATOM 1344 C CB . ASN A 1 219 ? 19.076 52.621 32.270 1.00 17.92 ? 212 ASN A CB 1 ATOM 1345 C CG . ASN A 1 219 ? 18.316 53.271 33.402 1.00 19.26 ? 212 ASN A CG 1 ATOM 1346 O OD1 . ASN A 1 219 ? 18.233 52.708 34.500 1.00 19.91 ? 212 ASN A OD1 1 ATOM 1347 N ND2 . ASN A 1 219 ? 17.697 54.429 33.131 1.00 18.51 ? 212 ASN A ND2 1 ATOM 1348 N N . LYS A 1 220 ? 19.678 50.303 30.135 1.00 18.35 ? 213 LYS A N 1 ATOM 1349 C CA . LYS A 1 220 ? 20.363 49.792 28.936 1.00 17.72 ? 213 LYS A CA 1 ATOM 1350 C C . LYS A 1 220 ? 19.327 49.499 27.842 1.00 19.02 ? 213 LYS A C 1 ATOM 1351 O O . LYS A 1 220 ? 19.526 49.860 26.675 1.00 20.11 ? 213 LYS A O 1 ATOM 1352 C CB . LYS A 1 220 ? 21.123 48.495 29.253 1.00 18.20 ? 213 LYS A CB 1 ATOM 1353 C CG . LYS A 1 220 ? 22.236 48.589 30.305 1.00 17.75 ? 213 LYS A CG 1 ATOM 1354 C CD . LYS A 1 220 ? 22.836 47.200 30.534 1.00 17.96 ? 213 LYS A CD 1 ATOM 1355 C CE . LYS A 1 220 ? 23.827 47.156 31.696 1.00 17.85 ? 213 LYS A CE 1 ATOM 1356 N NZ . LYS A 1 220 ? 25.227 47.576 31.358 1.00 19.22 ? 213 LYS A NZ 1 ATOM 1357 N N . VAL A 1 221 ? 18.235 48.822 28.217 1.00 16.67 ? 214 VAL A N 1 ATOM 1358 C CA . VAL A 1 221 ? 17.208 48.455 27.243 1.00 18.44 ? 214 VAL A CA 1 ATOM 1359 C C . VAL A 1 221 ? 16.515 49.711 26.677 1.00 18.45 ? 214 VAL A C 1 ATOM 1360 O O . VAL A 1 221 ? 16.302 49.813 25.461 1.00 19.56 ? 214 VAL A O 1 ATOM 1361 C CB . VAL A 1 221 ? 16.199 47.419 27.813 1.00 18.35 ? 214 VAL A CB 1 ATOM 1362 C CG1 . VAL A 1 221 ? 15.038 47.179 26.840 1.00 20.62 ? 214 VAL A CG1 1 ATOM 1363 C CG2 . VAL A 1 221 ? 16.916 46.104 28.132 1.00 18.56 ? 214 VAL A CG2 1 ATOM 1364 N N . LYS A 1 222 ? 16.174 50.653 27.557 1.00 18.64 ? 215 LYS A N 1 ATOM 1365 C CA . LYS A 1 222 ? 15.569 51.918 27.130 1.00 19.86 ? 215 LYS A CA 1 ATOM 1366 C C . LYS A 1 222 ? 16.484 52.616 26.118 1.00 21.18 ? 215 LYS A C 1 ATOM 1367 O O . LYS A 1 222 ? 16.026 53.083 25.050 1.00 20.98 ? 215 LYS A O 1 ATOM 1368 C CB . LYS A 1 222 ? 15.349 52.837 28.324 1.00 18.57 ? 215 LYS A CB 1 ATOM 1369 C CG . LYS A 1 222 ? 14.782 54.189 27.923 1.00 22.40 ? 215 LYS A CG 1 ATOM 1370 C CD . LYS A 1 222 ? 14.401 55.003 29.151 1.00 21.78 ? 215 LYS A CD 1 ATOM 1371 C CE . LYS A 1 222 ? 13.998 56.416 28.763 1.00 30.33 ? 215 LYS A CE 1 ATOM 1372 N NZ . LYS A 1 222 ? 15.213 57.275 28.760 1.00 40.62 ? 215 LYS A NZ 1 ATOM 1373 N N . ASN A 1 223 ? 17.767 52.671 26.450 1.00 19.87 ? 216 ASN A N 1 ATOM 1374 C CA . ASN A 1 223 ? 18.742 53.343 25.587 1.00 19.56 ? 216 ASN A CA 1 ATOM 1375 C C . ASN A 1 223 ? 18.847 52.632 24.239 1.00 20.22 ? 216 ASN A C 1 ATOM 1376 O O . ASN A 1 223 ? 18.926 53.286 23.190 1.00 21.26 ? 216 ASN A O 1 ATOM 1377 C CB . ASN A 1 223 ? 20.113 53.386 26.259 1.00 19.46 ? 216 ASN A CB 1 ATOM 1378 C CG . ASN A 1 223 ? 20.133 54.242 27.515 1.00 20.91 ? 216 ASN A CG 1 ATOM 1379 O OD1 . ASN A 1 223 ? 19.191 55.001 27.789 1.00 22.88 ? 216 ASN A OD1 1 ATOM 1380 N ND2 . ASN A 1 223 ? 21.212 54.119 28.297 1.00 19.84 ? 216 ASN A ND2 1 ATOM 1381 N N . ALA A 1 224 ? 18.843 51.300 24.259 1.00 19.77 ? 217 ALA A N 1 ATOM 1382 C CA . ALA A 1 224 ? 18.918 50.524 23.002 1.00 21.17 ? 217 ALA A CA 1 ATOM 1383 C C . ALA A 1 224 ? 17.677 50.759 22.129 1.00 22.47 ? 217 ALA A C 1 ATOM 1384 O O . ALA A 1 224 ? 17.778 50.899 20.907 1.00 23.12 ? 217 ALA A O 1 ATOM 1385 C CB . ALA A 1 224 ? 19.107 49.030 23.302 1.00 22.97 ? 217 ALA A CB 1 ATOM 1386 N N . GLN A 1 225 ? 16.502 50.789 22.765 1.00 22.64 ? 218 GLN A N 1 ATOM 1387 C CA . GLN A 1 225 ? 15.246 51.042 22.051 1.00 24.75 ? 218 GLN A CA 1 ATOM 1388 C C . GLN A 1 225 ? 15.277 52.376 21.369 1.00 26.11 ? 218 GLN A C 1 ATOM 1389 O O . GLN A 1 225 ? 14.893 52.499 20.205 1.00 27.79 ? 218 GLN A O 1 ATOM 1390 C CB . GLN A 1 225 ? 14.088 51.080 23.025 1.00 27.14 ? 218 GLN A CB 1 ATOM 1391 C CG . GLN A 1 225 ? 13.471 49.738 23.199 1.00 31.21 ? 218 GLN A CG 1 ATOM 1392 C CD . GLN A 1 225 ? 12.269 49.735 24.135 1.00 33.29 ? 218 GLN A CD 1 ATOM 1393 O OE1 . GLN A 1 225 ? 12.099 48.788 24.867 1.00 36.61 ? 218 GLN A OE1 1 ATOM 1394 N NE2 . GLN A 1 225 ? 11.422 50.777 24.085 1.00 40.26 ? 218 GLN A NE2 1 ATOM 1395 N N . LEU A 1 226 ? 15.707 53.391 22.114 1.00 26.94 ? 219 LEU A N 1 ATOM 1396 C CA . LEU A 1 226 ? 15.733 54.747 21.582 1.00 27.32 ? 219 LEU A CA 1 ATOM 1397 C C . LEU A 1 226 ? 16.760 54.907 20.457 1.00 28.52 ? 219 LEU A C 1 ATOM 1398 O O . LEU A 1 226 ? 16.553 55.712 19.536 1.00 29.30 ? 219 LEU A O 1 ATOM 1399 C CB . LEU A 1 226 ? 15.881 55.767 22.717 1.00 27.45 ? 219 LEU A CB 1 ATOM 1400 C CG . LEU A 1 226 ? 14.620 55.843 23.616 1.00 33.16 ? 219 LEU A CG 1 ATOM 1401 C CD1 . LEU A 1 226 ? 14.803 56.804 24.779 1.00 39.01 ? 219 LEU A CD1 1 ATOM 1402 C CD2 . LEU A 1 226 ? 13.341 56.186 22.849 1.00 40.46 ? 219 LEU A CD2 1 ATOM 1403 N N . ALA A 1 227 ? 17.818 54.092 20.485 1.00 26.99 ? 220 ALA A N 1 ATOM 1404 C CA . ALA A 1 227 ? 18.775 54.003 19.372 1.00 27.11 ? 220 ALA A CA 1 ATOM 1405 C C . ALA A 1 227 ? 18.241 53.223 18.162 1.00 28.70 ? 220 ALA A C 1 ATOM 1406 O O . ALA A 1 227 ? 18.906 53.146 17.127 1.00 28.60 ? 220 ALA A O 1 ATOM 1407 C CB . ALA A 1 227 ? 20.083 53.391 19.852 1.00 25.65 ? 220 ALA A CB 1 ATOM 1408 N N . GLY A 1 228 ? 17.060 52.628 18.290 1.00 25.71 ? 221 GLY A N 1 ATOM 1409 C CA . GLY A 1 228 ? 16.436 51.934 17.167 1.00 26.59 ? 221 GLY A CA 1 ATOM 1410 C C . GLY A 1 228 ? 16.759 50.454 17.050 1.00 26.22 ? 221 GLY A C 1 ATOM 1411 O O . GLY A 1 228 ? 16.428 49.827 16.037 1.00 27.78 ? 221 GLY A O 1 ATOM 1412 N N . ALA A 1 229 ? 17.388 49.880 18.078 1.00 26.26 ? 222 ALA A N 1 ATOM 1413 C CA . ALA A 1 229 ? 17.716 48.442 18.074 1.00 26.30 ? 222 ALA A CA 1 ATOM 1414 C C . ALA A 1 229 ? 16.464 47.597 17.912 1.00 26.75 ? 222 ALA A C 1 ATOM 1415 O O . ALA A 1 229 ? 15.378 47.994 18.363 1.00 26.98 ? 222 ALA A O 1 ATOM 1416 C CB . ALA A 1 229 ? 18.431 48.055 19.364 1.00 25.83 ? 222 ALA A CB 1 ATOM 1417 N N . LYS A 1 230 ? 16.595 46.424 17.292 1.00 24.96 ? 223 LYS A N 1 ATOM 1418 C CA . LYS A 1 230 ? 15.445 45.530 17.240 1.00 26.22 ? 223 LYS A CA 1 ATOM 1419 C C . LYS A 1 230 ? 15.511 44.394 18.261 1.00 25.39 ? 223 LYS A C 1 ATOM 1420 O O . LYS A 1 230 ? 14.591 43.580 18.356 1.00 24.89 ? 223 LYS A O 1 ATOM 1421 C CB . LYS A 1 230 ? 15.170 45.037 15.819 1.00 30.77 ? 223 LYS A CB 1 ATOM 1422 C CG . LYS A 1 230 ? 16.167 44.061 15.249 1.00 31.74 ? 223 LYS A CG 1 ATOM 1423 C CD . LYS A 1 230 ? 15.607 43.566 13.921 1.00 36.37 ? 223 LYS A CD 1 ATOM 1424 C CE . LYS A 1 230 ? 16.670 42.969 13.041 1.00 37.13 ? 223 LYS A CE 1 ATOM 1425 N NZ . LYS A 1 230 ? 16.171 42.761 11.643 1.00 40.06 ? 223 LYS A NZ 1 ATOM 1426 N N . GLY A 1 231 ? 16.591 44.361 19.035 1.00 22.96 ? 224 GLY A N 1 ATOM 1427 C CA . GLY A 1 231 ? 16.721 43.381 20.107 1.00 23.78 ? 224 GLY A CA 1 ATOM 1428 C C . GLY A 1 231 ? 17.953 43.684 20.918 1.00 21.61 ? 224 GLY A C 1 ATOM 1429 O O . GLY A 1 231 ? 18.849 44.401 20.448 1.00 23.28 ? 224 GLY A O 1 ATOM 1430 N N . VAL A 1 232 ? 18.003 43.141 22.129 1.00 21.37 ? 225 VAL A N 1 ATOM 1431 C CA . VAL A 1 232 ? 19.134 43.361 23.028 1.00 19.93 ? 225 VAL A CA 1 ATOM 1432 C C . VAL A 1 232 ? 19.567 42.029 23.633 1.00 21.51 ? 225 VAL A C 1 ATOM 1433 O O . VAL A 1 232 ? 18.739 41.279 24.179 1.00 21.81 ? 225 VAL A O 1 ATOM 1434 C CB . VAL A 1 232 ? 18.788 44.292 24.207 1.00 20.15 ? 225 VAL A CB 1 ATOM 1435 C CG1 . VAL A 1 232 ? 20.026 44.525 25.077 1.00 22.33 ? 225 VAL A CG1 1 ATOM 1436 C CG2 . VAL A 1 232 ? 18.227 45.620 23.724 1.00 22.67 ? 225 VAL A CG2 1 ATOM 1437 N N . ILE A 1 233 ? 20.866 41.765 23.560 1.00 22.41 ? 226 ILE A N 1 ATOM 1438 C CA . ILE A 1 233 ? 21.478 40.630 24.241 1.00 22.38 ? 226 ILE A CA 1 ATOM 1439 C C . ILE A 1 233 ? 22.362 41.187 25.359 1.00 21.87 ? 226 ILE A C 1 ATOM 1440 O O . ILE A 1 233 ? 23.256 41.993 25.102 1.00 22.98 ? 226 ILE A O 1 ATOM 1441 C CB . ILE A 1 233 ? 22.310 39.777 23.261 1.00 22.33 ? 226 ILE A CB 1 ATOM 1442 C CG1 . ILE A 1 233 ? 21.414 39.258 22.119 1.00 22.22 ? 226 ILE A CG1 1 ATOM 1443 C CG2 . ILE A 1 233 ? 23.024 38.651 24.012 1.00 21.46 ? 226 ILE A CG2 1 ATOM 1444 C CD1 . ILE A 1 233 ? 22.183 38.733 20.908 1.00 24.33 ? 226 ILE A CD1 1 ATOM 1445 N N . LEU A 1 234 ? 22.090 40.769 26.595 1.00 20.55 ? 227 LEU A N 1 ATOM 1446 C CA . LEU A 1 234 ? 22.855 41.191 27.773 1.00 19.29 ? 227 LEU A CA 1 ATOM 1447 C C . LEU A 1 234 ? 23.769 40.043 28.160 1.00 19.04 ? 227 LEU A C 1 ATOM 1448 O O . LEU A 1 234 ? 23.346 38.883 28.105 1.00 20.89 ? 227 LEU A O 1 ATOM 1449 C CB . LEU A 1 234 ? 21.904 41.487 28.936 1.00 18.45 ? 227 LEU A CB 1 ATOM 1450 C CG . LEU A 1 234 ? 20.908 42.649 28.717 1.00 17.77 ? 227 LEU A CG 1 ATOM 1451 C CD1 . LEU A 1 234 ? 19.822 42.669 29.804 1.00 21.66 ? 227 LEU A CD1 1 ATOM 1452 C CD2 . LEU A 1 234 ? 21.659 43.984 28.661 1.00 20.48 ? 227 LEU A CD2 1 ATOM 1453 N N . TYR A 1 235 ? 25.018 40.332 28.526 1.00 18.88 ? 228 TYR A N 1 ATOM 1454 C CA . TYR A 1 235 ? 25.889 39.239 28.970 1.00 18.97 ? 228 TYR A CA 1 ATOM 1455 C C . TYR A 1 235 ? 26.788 39.707 30.113 1.00 21.16 ? 228 TYR A C 1 ATOM 1456 O O . TYR A 1 235 ? 27.025 40.915 30.286 1.00 20.16 ? 228 TYR A O 1 ATOM 1457 C CB . TYR A 1 235 ? 26.724 38.626 27.808 1.00 19.45 ? 228 TYR A CB 1 ATOM 1458 C CG . TYR A 1 235 ? 27.956 39.450 27.488 1.00 19.22 ? 228 TYR A CG 1 ATOM 1459 C CD1 . TYR A 1 235 ? 29.201 39.103 28.020 1.00 20.64 ? 228 TYR A CD1 1 ATOM 1460 C CD2 . TYR A 1 235 ? 27.870 40.593 26.684 1.00 20.84 ? 228 TYR A CD2 1 ATOM 1461 C CE1 . TYR A 1 235 ? 30.335 39.869 27.753 1.00 21.49 ? 228 TYR A CE1 1 ATOM 1462 C CE2 . TYR A 1 235 ? 28.996 41.367 26.409 1.00 21.88 ? 228 TYR A CE2 1 ATOM 1463 C CZ . TYR A 1 235 ? 30.219 41.008 26.948 1.00 22.34 ? 228 TYR A CZ 1 ATOM 1464 O OH . TYR A 1 235 ? 31.323 41.788 26.717 1.00 23.75 ? 228 TYR A OH 1 ATOM 1465 N N . SER A 1 236 ? 27.302 38.744 30.874 1.00 19.44 ? 229 SER A N 1 ATOM 1466 C CA . SER A 1 236 ? 28.218 39.034 31.981 1.00 20.12 ? 229 SER A CA 1 ATOM 1467 C C . SER A 1 236 ? 29.677 38.859 31.531 1.00 20.94 ? 229 SER A C 1 ATOM 1468 O O . SER A 1 236 ? 30.126 37.744 31.270 1.00 21.83 ? 229 SER A O 1 ATOM 1469 C CB . SER A 1 236 ? 27.865 38.127 33.179 1.00 19.97 ? 229 SER A CB 1 ATOM 1470 O OG . SER A 1 236 ? 26.521 38.341 33.586 1.00 22.73 ? 229 SER A OG 1 ATOM 1471 N N . ASP A 1 237 ? 30.419 39.961 31.429 1.00 20.01 ? 230 ASP A N 1 ATOM 1472 C CA . ASP A 1 237 ? 31.815 39.882 31.000 1.00 22.49 ? 230 ASP A CA 1 ATOM 1473 C C . ASP A 1 237 ? 32.679 39.571 32.232 1.00 22.26 ? 230 ASP A C 1 ATOM 1474 O O . ASP A 1 237 ? 32.453 40.150 33.296 1.00 22.48 ? 230 ASP A O 1 ATOM 1475 C CB . ASP A 1 237 ? 32.249 41.208 30.344 1.00 22.03 ? 230 ASP A CB 1 ATOM 1476 C CG . ASP A 1 237 ? 33.530 41.064 29.529 1.00 22.83 ? 230 ASP A CG 1 ATOM 1477 O OD1 . ASP A 1 237 ? 33.471 41.094 28.280 1.00 26.22 ? 230 ASP A OD1 1 ATOM 1478 O OD2 . ASP A 1 237 ? 34.599 40.899 30.135 1.00 24.20 ? 230 ASP A OD2 1 ATOM 1479 N N . PRO A 1 238 ? 33.656 38.653 32.103 1.00 24.54 ? 231 PRO A N 1 ATOM 1480 C CA . PRO A 1 238 ? 34.560 38.395 33.240 1.00 24.19 ? 231 PRO A CA 1 ATOM 1481 C C . PRO A 1 238 ? 35.236 39.658 33.785 1.00 26.78 ? 231 PRO A C 1 ATOM 1482 O O . PRO A 1 238 ? 35.509 39.728 34.989 1.00 24.46 ? 231 PRO A O 1 ATOM 1483 C CB . PRO A 1 238 ? 35.626 37.453 32.657 1.00 26.46 ? 231 PRO A CB 1 ATOM 1484 C CG . PRO A 1 238 ? 35.025 36.864 31.450 1.00 28.29 ? 231 PRO A CG 1 ATOM 1485 C CD . PRO A 1 238 ? 34.003 37.832 30.920 1.00 24.60 ? 231 PRO A CD 1 ATOM 1486 N N . ALA A 1 239 ? 35.485 40.653 32.927 1.00 25.50 ? 232 ALA A N 1 ATOM 1487 C CA . ALA A 1 239 ? 36.015 41.944 33.400 1.00 25.96 ? 232 ALA A CA 1 ATOM 1488 C C . ALA A 1 239 ? 35.204 42.505 34.589 1.00 25.93 ? 232 ALA A C 1 ATOM 1489 O O . ALA A 1 239 ? 35.755 43.100 35.533 1.00 27.50 ? 232 ALA A O 1 ATOM 1490 C CB . ALA A 1 239 ? 36.025 42.950 32.257 1.00 27.07 ? 232 ALA A CB 1 ATOM 1491 N N . ASP A 1 240 ? 33.897 42.294 34.543 1.00 26.10 ? 233 ASP A N 1 ATOM 1492 C CA . ASP A 1 240 ? 32.978 42.864 35.519 1.00 25.75 ? 233 ASP A CA 1 ATOM 1493 C C . ASP A 1 240 ? 32.465 41.856 36.542 1.00 26.06 ? 233 ASP A C 1 ATOM 1494 O O . ASP A 1 240 ? 31.951 42.261 37.588 1.00 29.39 ? 233 ASP A O 1 ATOM 1495 C CB . ASP A 1 240 ? 31.790 43.498 34.790 1.00 25.33 ? 233 ASP A CB 1 ATOM 1496 C CG . ASP A 1 240 ? 32.234 44.467 33.708 1.00 26.03 ? 233 ASP A CG 1 ATOM 1497 O OD1 . ASP A 1 240 ? 32.717 45.568 34.048 1.00 26.74 ? 233 ASP A OD1 1 ATOM 1498 O OD2 . ASP A 1 240 ? 32.125 44.104 32.523 1.00 23.17 ? 233 ASP A OD2 1 ATOM 1499 N N . TYR A 1 241 ? 32.597 40.559 36.247 1.00 24.26 ? 234 TYR A N 1 ATOM 1500 C CA . TYR A 1 241 ? 31.991 39.506 37.095 1.00 23.81 ? 234 TYR A CA 1 ATOM 1501 C C . TYR A 1 241 ? 32.946 38.372 37.471 1.00 25.51 ? 234 TYR A C 1 ATOM 1502 O O . TYR A 1 241 ? 32.505 37.317 37.950 1.00 24.36 ? 234 TYR A O 1 ATOM 1503 C CB . TYR A 1 241 ? 30.702 38.949 36.449 1.00 24.07 ? 234 TYR A CB 1 ATOM 1504 C CG . TYR A 1 241 ? 29.628 40.011 36.413 1.00 21.80 ? 234 TYR A CG 1 ATOM 1505 C CD1 . TYR A 1 241 ? 29.432 40.779 35.264 1.00 21.68 ? 234 TYR A CD1 1 ATOM 1506 C CD2 . TYR A 1 241 ? 28.882 40.322 37.563 1.00 21.02 ? 234 TYR A CD2 1 ATOM 1507 C CE1 . TYR A 1 241 ? 28.503 41.812 35.233 1.00 21.66 ? 234 TYR A CE1 1 ATOM 1508 C CE2 . TYR A 1 241 ? 27.933 41.336 37.543 1.00 23.66 ? 234 TYR A CE2 1 ATOM 1509 C CZ . TYR A 1 241 ? 27.745 42.072 36.374 1.00 22.35 ? 234 TYR A CZ 1 ATOM 1510 O OH . TYR A 1 241 ? 26.829 43.077 36.351 1.00 23.24 ? 234 TYR A OH 1 ATOM 1511 N N . PHE A 1 242 ? 34.247 38.589 37.274 1.00 24.92 ? 235 PHE A N 1 ATOM 1512 C CA . PHE A 1 242 ? 35.237 37.573 37.643 1.00 24.29 ? 235 PHE A CA 1 ATOM 1513 C C . PHE A 1 242 ? 36.404 38.277 38.314 1.00 26.78 ? 235 PHE A C 1 ATOM 1514 O O . PHE A 1 242 ? 37.250 38.867 37.641 1.00 28.66 ? 235 PHE A O 1 ATOM 1515 C CB . PHE A 1 242 ? 35.701 36.774 36.424 1.00 27.53 ? 235 PHE A CB 1 ATOM 1516 C CG . PHE A 1 242 ? 36.428 35.498 36.770 1.00 26.27 ? 235 PHE A CG 1 ATOM 1517 C CD1 . PHE A 1 242 ? 35.737 34.289 36.849 1.00 24.41 ? 235 PHE A CD1 1 ATOM 1518 C CD2 . PHE A 1 242 ? 37.803 35.503 37.015 1.00 27.55 ? 235 PHE A CD2 1 ATOM 1519 C CE1 . PHE A 1 242 ? 36.406 33.110 37.175 1.00 26.19 ? 235 PHE A CE1 1 ATOM 1520 C CE2 . PHE A 1 242 ? 38.480 34.322 37.333 1.00 27.79 ? 235 PHE A CE2 1 ATOM 1521 C CZ . PHE A 1 242 ? 37.778 33.123 37.404 1.00 28.38 ? 235 PHE A CZ 1 ATOM 1522 N N . ALA A 1 243 ? 36.419 38.249 39.642 1.00 26.83 ? 236 ALA A N 1 ATOM 1523 C CA . ALA A 1 243 ? 37.504 38.858 40.412 1.00 27.77 ? 236 ALA A CA 1 ATOM 1524 C C . ALA A 1 243 ? 38.803 38.090 40.200 1.00 30.06 ? 236 ALA A C 1 ATOM 1525 O O . ALA A 1 243 ? 38.817 36.867 40.307 1.00 29.23 ? 236 ALA A O 1 ATOM 1526 C CB . ALA A 1 243 ? 37.143 38.892 41.884 1.00 30.42 ? 236 ALA A CB 1 ATOM 1527 N N . PRO A 1 244 ? 39.903 38.807 39.902 1.00 34.47 ? 237 PRO A N 1 ATOM 1528 C CA . PRO A 1 244 ? 41.200 38.159 39.733 1.00 34.83 ? 237 PRO A CA 1 ATOM 1529 C C . PRO A 1 244 ? 41.572 37.326 40.964 1.00 33.69 ? 237 PRO A C 1 ATOM 1530 O O . PRO A 1 244 ? 41.388 37.781 42.101 1.00 34.68 ? 237 PRO A O 1 ATOM 1531 C CB . PRO A 1 244 ? 42.170 39.347 39.576 1.00 38.75 ? 237 PRO A CB 1 ATOM 1532 C CG . PRO A 1 244 ? 41.317 40.474 39.093 1.00 41.72 ? 237 PRO A CG 1 ATOM 1533 C CD . PRO A 1 244 ? 39.991 40.274 39.768 1.00 35.46 ? 237 PRO A CD 1 ATOM 1534 N N . GLY A 1 245 ? 42.055 36.106 40.732 1.00 32.98 ? 238 GLY A N 1 ATOM 1535 C CA . GLY A 1 245 ? 42.613 35.276 41.801 1.00 33.05 ? 238 GLY A CA 1 ATOM 1536 C C . GLY A 1 245 ? 41.637 34.470 42.637 1.00 35.03 ? 238 GLY A C 1 ATOM 1537 O O . GLY A 1 245 ? 42.045 33.809 43.601 1.00 40.96 ? 238 GLY A O 1 ATOM 1538 N N . VAL A 1 246 ? 40.355 34.517 42.273 1.00 33.03 ? 239 VAL A N 1 ATOM 1539 C CA . VAL A 1 246 ? 39.304 33.759 42.970 1.00 28.56 ? 239 VAL A CA 1 ATOM 1540 C C . VAL A 1 246 ? 38.728 32.740 41.987 1.00 27.63 ? 239 VAL A C 1 ATOM 1541 O O . VAL A 1 246 ? 38.652 33.002 40.783 1.00 30.43 ? 239 VAL A O 1 ATOM 1542 C CB . VAL A 1 246 ? 38.238 34.685 43.687 1.00 27.65 ? 239 VAL A CB 1 ATOM 1543 C CG1 A VAL A 1 246 ? 38.534 36.163 43.491 0.50 32.95 ? 239 VAL A CG1 1 ATOM 1544 C CG1 B VAL A 1 246 ? 37.126 33.867 44.330 0.50 23.94 ? 239 VAL A CG1 1 ATOM 1545 C CG2 A VAL A 1 246 ? 36.794 34.318 43.375 0.50 27.14 ? 239 VAL A CG2 1 ATOM 1546 C CG2 B VAL A 1 246 ? 38.904 35.604 44.710 0.50 25.59 ? 239 VAL A CG2 1 ATOM 1547 N N . LYS A 1 247 ? 38.390 31.562 42.497 1.00 29.20 ? 240 LYS A N 1 ATOM 1548 C CA . LYS A 1 247 ? 37.805 30.505 41.674 1.00 29.14 ? 240 LYS A CA 1 ATOM 1549 C C . LYS A 1 247 ? 36.312 30.714 41.407 1.00 28.91 ? 240 LYS A C 1 ATOM 1550 O O . LYS A 1 247 ? 35.631 31.355 42.190 1.00 27.82 ? 240 LYS A O 1 ATOM 1551 C CB . LYS A 1 247 ? 38.038 29.141 42.329 1.00 34.03 ? 240 LYS A CB 1 ATOM 1552 C CG . LYS A 1 247 ? 39.509 28.743 42.423 1.00 34.07 ? 240 LYS A CG 1 ATOM 1553 C CD . LYS A 1 247 ? 40.107 28.498 41.042 1.00 40.54 ? 240 LYS A CD 1 ATOM 1554 C CE . LYS A 1 247 ? 41.541 28.003 41.122 0.10 41.80 ? 240 LYS A CE 1 ATOM 1555 N NZ . LYS A 1 247 ? 42.241 28.202 39.822 1.00 45.50 ? 240 LYS A NZ 1 ATOM 1556 N N . SER A 1 248 ? 35.843 30.172 40.283 1.00 28.82 ? 241 SER A N 1 ATOM 1557 C CA . SER A 1 248 ? 34.418 30.056 39.956 1.00 27.26 ? 241 SER A CA 1 ATOM 1558 C C . SER A 1 248 ? 33.694 29.171 40.953 1.00 26.35 ? 241 SER A C 1 ATOM 1559 O O . SER A 1 248 ? 34.282 28.192 41.465 1.00 26.36 ? 241 SER A O 1 ATOM 1560 C CB . SER A 1 248 ? 34.270 29.363 38.598 1.00 33.22 ? 241 SER A CB 1 ATOM 1561 O OG . SER A 1 248 ? 34.693 30.177 37.545 1.00 37.41 ? 241 SER A OG 1 ATOM 1562 N N . TYR A 1 249 ? 32.410 29.470 41.179 1.00 24.83 ? 242 TYR A N 1 ATOM 1563 C CA . TYR A 1 249 ? 31.530 28.597 41.948 1.00 24.44 ? 242 TYR A CA 1 ATOM 1564 C C . TYR A 1 249 ? 31.547 27.194 41.336 1.00 24.85 ? 242 TYR A C 1 ATOM 1565 O O . TYR A 1 249 ? 31.468 27.071 40.120 1.00 27.89 ? 242 TYR A O 1 ATOM 1566 C CB . TYR A 1 249 ? 30.094 29.155 41.982 1.00 24.42 ? 242 TYR A CB 1 ATOM 1567 C CG . TYR A 1 249 ? 29.378 28.604 43.178 1.00 22.95 ? 242 TYR A CG 1 ATOM 1568 C CD1 . TYR A 1 249 ? 29.662 29.101 44.454 1.00 25.79 ? 242 TYR A CD1 1 ATOM 1569 C CD2 . TYR A 1 249 ? 28.508 27.510 43.059 1.00 27.26 ? 242 TYR A CD2 1 ATOM 1570 C CE1 . TYR A 1 249 ? 29.069 28.561 45.576 1.00 27.48 ? 242 TYR A CE1 1 ATOM 1571 C CE2 . TYR A 1 249 ? 27.906 26.957 44.182 1.00 27.61 ? 242 TYR A CE2 1 ATOM 1572 C CZ . TYR A 1 249 ? 28.194 27.497 45.431 1.00 26.50 ? 242 TYR A CZ 1 ATOM 1573 O OH . TYR A 1 249 ? 27.647 26.954 46.540 1.00 29.70 ? 242 TYR A OH 1 ATOM 1574 N N . PRO A 1 250 ? 31.607 26.125 42.161 1.00 27.21 ? 243 PRO A N 1 ATOM 1575 C CA . PRO A 1 250 ? 31.483 26.031 43.624 1.00 28.22 ? 243 PRO A CA 1 ATOM 1576 C C . PRO A 1 250 ? 32.786 26.187 44.421 1.00 29.09 ? 243 PRO A C 1 ATOM 1577 O O . PRO A 1 250 ? 32.765 26.079 45.650 1.00 30.87 ? 243 PRO A O 1 ATOM 1578 C CB . PRO A 1 250 ? 30.926 24.619 43.813 1.00 27.01 ? 243 PRO A CB 1 ATOM 1579 C CG . PRO A 1 250 ? 31.575 23.836 42.711 1.00 29.01 ? 243 PRO A CG 1 ATOM 1580 C CD . PRO A 1 250 ? 31.580 24.783 41.536 1.00 27.90 ? 243 PRO A CD 1 ATOM 1581 N N . ASP A 1 251 ? 33.894 26.438 43.739 1.00 26.85 ? 244 ASP A N 1 ATOM 1582 C CA . ASP A 1 251 ? 35.194 26.456 44.421 1.00 29.13 ? 244 ASP A CA 1 ATOM 1583 C C . ASP A 1 251 ? 35.597 27.838 44.907 1.00 28.97 ? 244 ASP A C 1 ATOM 1584 O O . ASP A 1 251 ? 36.556 27.982 45.659 1.00 29.28 ? 244 ASP A O 1 ATOM 1585 C CB . ASP A 1 251 ? 36.267 25.851 43.528 1.00 31.74 ? 244 ASP A CB 1 ATOM 1586 C CG . ASP A 1 251 ? 35.946 24.419 43.130 1.00 39.61 ? 244 ASP A CG 1 ATOM 1587 O OD1 . ASP A 1 251 ? 35.425 23.638 43.974 1.00 39.21 ? 244 ASP A OD1 1 ATOM 1588 O OD2 . ASP A 1 251 ? 36.204 24.086 41.962 1.00 48.91 ? 244 ASP A OD2 1 ATOM 1589 N N . GLY A 1 252 ? 34.851 28.846 44.479 1.00 28.86 ? 245 GLY A N 1 ATOM 1590 C CA . GLY A 1 252 ? 35.040 30.215 44.921 1.00 26.60 ? 245 GLY A CA 1 ATOM 1591 C C . GLY A 1 252 ? 33.774 30.976 44.626 1.00 26.16 ? 245 GLY A C 1 ATOM 1592 O O . GLY A 1 252 ? 32.757 30.383 44.254 1.00 28.05 ? 245 GLY A O 1 ATOM 1593 N N . TRP A 1 253 ? 33.836 32.293 44.777 1.00 24.58 ? 246 TRP A N 1 ATOM 1594 C CA . TRP A 1 253 ? 32.638 33.106 44.657 1.00 21.74 ? 246 TRP A CA 1 ATOM 1595 C C . TRP A 1 253 ? 32.500 33.804 43.318 1.00 23.34 ? 246 TRP A C 1 ATOM 1596 O O . TRP A 1 253 ? 31.637 34.685 43.149 1.00 22.08 ? 246 TRP A O 1 ATOM 1597 C CB . TRP A 1 253 ? 32.529 34.076 45.849 1.00 22.54 ? 246 TRP A CB 1 ATOM 1598 C CG . TRP A 1 253 ? 33.799 34.824 46.186 1.00 25.48 ? 246 TRP A CG 1 ATOM 1599 C CD1 . TRP A 1 253 ? 34.809 34.448 47.069 1.00 26.92 ? 246 TRP A CD1 1 ATOM 1600 C CD2 . TRP A 1 253 ? 34.210 36.132 45.667 1.00 25.01 ? 246 TRP A CD2 1 ATOM 1601 N NE1 . TRP A 1 253 ? 35.797 35.413 47.122 1.00 27.72 ? 246 TRP A NE1 1 ATOM 1602 C CE2 . TRP A 1 253 ? 35.492 36.449 46.305 1.00 26.97 ? 246 TRP A CE2 1 ATOM 1603 C CE3 . TRP A 1 253 ? 33.655 37.042 44.764 1.00 26.42 ? 246 TRP A CE3 1 ATOM 1604 C CZ2 . TRP A 1 253 ? 36.175 37.630 46.033 1.00 26.60 ? 246 TRP A CZ2 1 ATOM 1605 C CZ3 . TRP A 1 253 ? 34.345 38.229 44.500 1.00 27.49 ? 246 TRP A CZ3 1 ATOM 1606 C CH2 . TRP A 1 253 ? 35.585 38.514 45.119 1.00 26.10 ? 246 TRP A CH2 1 ATOM 1607 N N . ASN A 1 254 ? 33.314 33.399 42.338 1.00 22.44 ? 247 ASN A N 1 ATOM 1608 C CA . ASN A 1 254 ? 33.215 33.987 40.987 1.00 24.22 ? 247 ASN A CA 1 ATOM 1609 C C . ASN A 1 254 ? 32.125 33.342 40.140 1.00 22.70 ? 247 ASN A C 1 ATOM 1610 O O . ASN A 1 254 ? 31.690 32.206 40.431 1.00 25.59 ? 247 ASN A O 1 ATOM 1611 C CB . ASN A 1 254 ? 34.554 33.910 40.239 1.00 25.36 ? 247 ASN A CB 1 ATOM 1612 C CG . ASN A 1 254 ? 35.401 35.166 40.428 1.00 24.18 ? 247 ASN A CG 1 ATOM 1613 O OD1 . ASN A 1 254 ? 34.890 36.234 40.824 1.00 24.46 ? 247 ASN A OD1 1 ATOM 1614 N ND2 . ASN A 1 254 ? 36.696 35.055 40.127 1.00 24.08 ? 247 ASN A ND2 1 ATOM 1615 N N . LEU A 1 255 ? 31.713 34.062 39.093 1.00 23.01 ? 248 LEU A N 1 ATOM 1616 C CA . LEU A 1 255 ? 30.731 33.595 38.113 1.00 20.97 ? 248 LEU A CA 1 ATOM 1617 C C . LEU A 1 255 ? 31.401 32.687 37.093 1.00 23.56 ? 248 LEU A C 1 ATOM 1618 O O . LEU A 1 255 ? 32.364 33.112 36.432 1.00 23.92 ? 248 LEU A O 1 ATOM 1619 C CB . LEU A 1 255 ? 30.114 34.796 37.367 1.00 20.60 ? 248 LEU A CB 1 ATOM 1620 C CG . LEU A 1 255 ? 28.950 34.509 36.401 1.00 22.65 ? 248 LEU A CG 1 ATOM 1621 C CD1 . LEU A 1 255 ? 27.675 34.057 37.124 1.00 19.83 ? 248 LEU A CD1 1 ATOM 1622 C CD2 . LEU A 1 255 ? 28.690 35.750 35.542 1.00 25.34 ? 248 LEU A CD2 1 ATOM 1623 N N . PRO A 1 256 ? 30.894 31.436 36.949 1.00 21.98 ? 249 PRO A N 1 ATOM 1624 C CA . PRO A 1 256 ? 31.390 30.538 35.903 1.00 21.65 ? 249 PRO A CA 1 ATOM 1625 C C . PRO A 1 256 ? 30.882 30.968 34.534 1.00 20.87 ? 249 PRO A C 1 ATOM 1626 O O . PRO A 1 256 ? 29.946 31.770 34.457 1.00 21.05 ? 249 PRO A O 1 ATOM 1627 C CB . PRO A 1 256 ? 30.792 29.164 36.265 1.00 22.09 ? 249 PRO A CB 1 ATOM 1628 C CG . PRO A 1 256 ? 29.866 29.382 37.392 1.00 22.40 ? 249 PRO A CG 1 ATOM 1629 C CD . PRO A 1 256 ? 29.831 30.831 37.770 1.00 21.69 ? 249 PRO A CD 1 ATOM 1630 N N . GLY A 1 257 ? 31.479 30.430 33.467 1.00 21.75 ? 250 GLY A N 1 ATOM 1631 C CA . GLY A 1 257 ? 31.142 30.863 32.118 1.00 23.45 ? 250 GLY A CA 1 ATOM 1632 C C . GLY A 1 257 ? 29.736 30.493 31.684 1.00 21.72 ? 250 GLY A C 1 ATOM 1633 O O . GLY A 1 257 ? 29.213 31.070 30.728 1.00 22.78 ? 250 GLY A O 1 ATOM 1634 N N . GLY A 1 258 ? 29.133 29.528 32.381 1.00 21.03 ? 251 GLY A N 1 ATOM 1635 C CA . GLY A 1 258 ? 27.745 29.139 32.158 1.00 21.27 ? 251 GLY A CA 1 ATOM 1636 C C . GLY A 1 258 ? 26.756 29.883 33.041 1.00 19.95 ? 251 GLY A C 1 ATOM 1637 O O . GLY A 1 258 ? 25.544 29.755 32.859 1.00 20.99 ? 251 GLY A O 1 ATOM 1638 N N . GLY A 1 259 ? 27.263 30.686 33.979 1.00 20.49 ? 252 GLY A N 1 ATOM 1639 C CA . GLY A 1 259 ? 26.402 31.485 34.853 1.00 18.36 ? 252 GLY A CA 1 ATOM 1640 C C . GLY A 1 259 ? 25.725 32.635 34.126 1.00 19.27 ? 252 GLY A C 1 ATOM 1641 O O . GLY A 1 259 ? 26.300 33.231 33.208 1.00 20.62 ? 252 GLY A O 1 ATOM 1642 N N . VAL A 1 260 ? 24.495 32.943 34.529 1.00 18.53 ? 253 VAL A N 1 ATOM 1643 C CA . VAL A 1 260 ? 23.705 34.015 33.875 1.00 18.21 ? 253 VAL A CA 1 ATOM 1644 C C . VAL A 1 260 ? 22.931 34.819 34.914 1.00 18.57 ? 253 VAL A C 1 ATOM 1645 O O . VAL A 1 260 ? 22.316 34.253 35.827 1.00 20.09 ? 253 VAL A O 1 ATOM 1646 C CB . VAL A 1 260 ? 22.693 33.457 32.815 1.00 17.19 ? 253 VAL A CB 1 ATOM 1647 C CG1 . VAL A 1 260 ? 22.046 34.598 32.013 1.00 18.75 ? 253 VAL A CG1 1 ATOM 1648 C CG2 . VAL A 1 260 ? 23.363 32.441 31.884 1.00 18.61 ? 253 VAL A CG2 1 ATOM 1649 N N . GLN A 1 261 ? 22.935 36.139 34.737 1.00 17.15 ? 254 GLN A N 1 ATOM 1650 C CA . GLN A 1 261 ? 22.220 37.052 35.614 1.00 16.32 ? 254 GLN A CA 1 ATOM 1651 C C . GLN A 1 261 ? 20.794 37.264 35.119 1.00 17.89 ? 254 GLN A C 1 ATOM 1652 O O . GLN A 1 261 ? 20.577 37.856 34.044 1.00 19.53 ? 254 GLN A O 1 ATOM 1653 C CB . GLN A 1 261 ? 22.969 38.394 35.654 1.00 17.29 ? 254 GLN A CB 1 ATOM 1654 C CG . GLN A 1 261 ? 22.279 39.468 36.511 1.00 16.09 ? 254 GLN A CG 1 ATOM 1655 C CD . GLN A 1 261 ? 22.870 40.877 36.319 1.00 15.79 ? 254 GLN A CD 1 ATOM 1656 O OE1 . GLN A 1 261 ? 22.142 41.871 36.308 1.00 18.23 ? 254 GLN A OE1 1 ATOM 1657 N NE2 . GLN A 1 261 ? 24.190 40.961 36.192 1.00 18.78 ? 254 GLN A NE2 1 ATOM 1658 N N . ARG A 1 262 ? 19.818 36.781 35.896 1.00 17.60 ? 255 ARG A N 1 ATOM 1659 C CA . ARG A 1 262 ? 18.399 37.108 35.632 1.00 17.25 ? 255 ARG A CA 1 ATOM 1660 C C . ARG A 1 262 ? 18.105 38.564 35.993 1.00 17.45 ? 255 ARG A C 1 ATOM 1661 O O . ARG A 1 262 ? 18.889 39.192 36.700 1.00 16.57 ? 255 ARG A O 1 ATOM 1662 C CB . ARG A 1 262 ? 17.479 36.196 36.445 1.00 17.78 ? 255 ARG A CB 1 ATOM 1663 C CG . ARG A 1 262 ? 17.488 34.775 35.904 1.00 17.48 ? 255 ARG A CG 1 ATOM 1664 C CD . ARG A 1 262 ? 17.108 33.798 37.021 1.00 16.74 ? 255 ARG A CD 1 ATOM 1665 N NE . ARG A 1 262 ? 17.344 32.397 36.646 1.00 17.90 ? 255 ARG A NE 1 ATOM 1666 C CZ . ARG A 1 262 ? 18.549 31.821 36.606 1.00 17.89 ? 255 ARG A CZ 1 ATOM 1667 N NH1 . ARG A 1 262 ? 19.643 32.526 36.909 1.00 19.43 ? 255 ARG A NH1 1 ATOM 1668 N NH2 . ARG A 1 262 ? 18.669 30.540 36.246 1.00 18.63 ? 255 ARG A NH2 1 ATOM 1669 N N . GLY A 1 263 ? 16.969 39.094 35.542 1.00 16.81 ? 256 GLY A N 1 ATOM 1670 C CA . GLY A 1 263 ? 16.504 40.376 36.084 1.00 15.76 ? 256 GLY A CA 1 ATOM 1671 C C . GLY A 1 263 ? 15.520 41.057 35.164 1.00 16.08 ? 256 GLY A C 1 ATOM 1672 O O . GLY A 1 263 ? 15.581 40.883 33.938 1.00 15.88 ? 256 GLY A O 1 ATOM 1673 N N . ASN A 1 264 ? 14.625 41.848 35.747 1.00 15.54 ? 257 ASN A N 1 ATOM 1674 C CA . ASN A 1 264 ? 13.631 42.546 34.940 1.00 15.20 ? 257 ASN A CA 1 ATOM 1675 C C . ASN A 1 264 ? 14.260 43.722 34.187 1.00 14.96 ? 257 ASN A C 1 ATOM 1676 O O . ASN A 1 264 ? 15.309 44.265 34.589 1.00 15.99 ? 257 ASN A O 1 ATOM 1677 C CB . ASN A 1 264 ? 12.410 42.974 35.779 1.00 14.73 ? 257 ASN A CB 1 ATOM 1678 C CG . ASN A 1 264 ? 12.621 44.321 36.483 1.00 14.33 ? 257 ASN A CG 1 ATOM 1679 O OD1 . ASN A 1 264 ? 12.598 45.376 35.831 1.00 15.83 ? 257 ASN A OD1 1 ATOM 1680 N ND2 . ASN A 1 264 ? 12.822 44.298 37.812 1.00 16.56 ? 257 ASN A ND2 1 ATOM 1681 N N . ILE A 1 265 ? 13.603 44.103 33.091 1.00 14.91 ? 258 ILE A N 1 ATOM 1682 C CA . ILE A 1 265 ? 14.104 45.153 32.210 1.00 16.03 ? 258 ILE A CA 1 ATOM 1683 C C . ILE A 1 265 ? 13.053 46.253 32.036 1.00 15.65 ? 258 ILE A C 1 ATOM 1684 O O . ILE A 1 265 ? 13.015 46.920 31.006 1.00 17.97 ? 258 ILE A O 1 ATOM 1685 C CB . ILE A 1 265 ? 14.560 44.570 30.844 1.00 16.63 ? 258 ILE A CB 1 ATOM 1686 C CG1 . ILE A 1 265 ? 13.438 43.672 30.267 1.00 16.25 ? 258 ILE A CG1 1 ATOM 1687 C CG2 . ILE A 1 265 ? 15.868 43.790 31.012 1.00 17.13 ? 258 ILE A CG2 1 ATOM 1688 C CD1 . ILE A 1 265 ? 13.577 43.336 28.771 1.00 20.68 ? 258 ILE A CD1 1 ATOM 1689 N N . LEU A 1 266 ? 12.205 46.439 33.056 1.00 15.68 ? 259 LEU A N 1 ATOM 1690 C CA . LEU A 1 266 ? 11.201 47.507 33.052 1.00 14.92 ? 259 LEU A CA 1 ATOM 1691 C C . LEU A 1 266 ? 11.801 48.882 33.240 1.00 16.27 ? 259 LEU A C 1 ATOM 1692 O O . LEU A 1 266 ? 12.909 49.024 33.782 1.00 16.77 ? 259 LEU A O 1 ATOM 1693 C CB . LEU A 1 266 ? 10.182 47.306 34.185 1.00 16.01 ? 259 LEU A CB 1 ATOM 1694 C CG . LEU A 1 266 ? 9.331 46.035 34.066 1.00 15.13 ? 259 LEU A CG 1 ATOM 1695 C CD1 . LEU A 1 266 ? 8.528 45.915 35.351 1.00 17.16 ? 259 LEU A CD1 1 ATOM 1696 C CD2 . LEU A 1 266 ? 8.416 46.064 32.839 1.00 19.21 ? 259 LEU A CD2 1 ATOM 1697 N N . ASN A 1 267 ? 11.043 49.893 32.801 1.00 16.01 ? 260 ASN A N 1 ATOM 1698 C CA . ASN A 1 267 ? 11.326 51.294 33.163 1.00 14.90 ? 260 ASN A CA 1 ATOM 1699 C C . ASN A 1 267 ? 10.086 51.879 33.828 1.00 15.93 ? 260 ASN A C 1 ATOM 1700 O O . ASN A 1 267 ? 9.354 52.668 33.226 1.00 16.76 ? 260 ASN A O 1 ATOM 1701 C CB . ASN A 1 267 ? 11.751 52.075 31.927 1.00 17.38 ? 260 ASN A CB 1 ATOM 1702 C CG . ASN A 1 267 ? 13.193 51.780 31.548 1.00 17.71 ? 260 ASN A CG 1 ATOM 1703 O OD1 . ASN A 1 267 ? 14.115 52.401 32.074 1.00 20.75 ? 260 ASN A OD1 1 ATOM 1704 N ND2 . ASN A 1 267 ? 13.398 50.783 30.690 1.00 18.79 ? 260 ASN A ND2 1 ATOM 1705 N N . LEU A 1 268 ? 9.847 51.472 35.077 1.00 14.53 ? 261 LEU A N 1 ATOM 1706 C CA . LEU A 1 268 ? 8.614 51.835 35.774 1.00 14.97 ? 261 LEU A CA 1 ATOM 1707 C C . LEU A 1 268 ? 8.614 53.238 36.326 1.00 15.33 ? 261 LEU A C 1 ATOM 1708 O O . LEU A 1 268 ? 7.539 53.796 36.551 1.00 14.95 ? 261 LEU A O 1 ATOM 1709 C CB . LEU A 1 268 ? 8.369 50.880 36.951 1.00 15.31 ? 261 LEU A CB 1 ATOM 1710 C CG . LEU A 1 268 ? 8.003 49.444 36.564 1.00 14.87 ? 261 LEU A CG 1 ATOM 1711 C CD1 . LEU A 1 268 ? 7.972 48.626 37.872 1.00 16.00 ? 261 LEU A CD1 1 ATOM 1712 C CD2 . LEU A 1 268 ? 6.640 49.446 35.862 1.00 17.47 ? 261 LEU A CD2 1 ATOM 1713 N N . ASN A 1 269 ? 9.801 53.789 36.599 1.00 14.17 ? 262 ASN A N 1 ATOM 1714 C CA . ASN A 1 269 ? 9.897 55.126 37.251 1.00 14.53 ? 262 ASN A CA 1 ATOM 1715 C C . ASN A 1 269 ? 9.008 55.254 38.492 1.00 14.30 ? 262 ASN A C 1 ATOM 1716 O O . ASN A 1 269 ? 8.334 56.272 38.712 1.00 16.00 ? 262 ASN A O 1 ATOM 1717 C CB . ASN A 1 269 ? 9.589 56.248 36.251 1.00 16.36 ? 262 ASN A CB 1 ATOM 1718 C CG . ASN A 1 269 ? 10.607 56.303 35.149 1.00 18.64 ? 262 ASN A CG 1 ATOM 1719 O OD1 . ASN A 1 269 ? 11.788 56.065 35.389 1.00 20.50 ? 262 ASN A OD1 1 ATOM 1720 N ND2 . ASN A 1 269 ? 10.163 56.588 33.936 1.00 19.87 ? 262 ASN A ND2 1 ATOM 1721 N N . GLY A 1 270 ? 9.000 54.199 39.298 1.00 13.27 ? 263 GLY A N 1 ATOM 1722 C CA . GLY A 1 270 ? 8.238 54.217 40.545 1.00 13.71 ? 263 GLY A CA 1 ATOM 1723 C C . GLY A 1 270 ? 6.784 53.777 40.462 1.00 14.15 ? 263 GLY A C 1 ATOM 1724 O O . GLY A 1 270 ? 6.102 53.818 41.478 1.00 15.85 ? 263 GLY A O 1 ATOM 1725 N N . ALA A 1 271 ? 6.294 53.359 39.284 1.00 13.54 ? 264 ALA A N 1 ATOM 1726 C CA . ALA A 1 271 ? 4.845 53.127 39.130 1.00 13.47 ? 264 ALA A CA 1 ATOM 1727 C C . ALA A 1 271 ? 4.294 51.911 39.862 1.00 14.65 ? 264 ALA A C 1 ATOM 1728 O O . ALA A 1 271 ? 3.098 51.887 40.176 1.00 16.07 ? 264 ALA A O 1 ATOM 1729 C CB . ALA A 1 271 ? 4.450 53.080 37.645 1.00 13.24 ? 264 ALA A CB 1 ATOM 1730 N N . GLY A 1 272 ? 5.138 50.911 40.145 1.00 13.63 ? 265 GLY A N 1 ATOM 1731 C CA . GLY A 1 272 ? 4.592 49.637 40.664 1.00 14.33 ? 265 GLY A CA 1 ATOM 1732 C C . GLY A 1 272 ? 4.046 48.742 39.561 1.00 14.29 ? 265 GLY A C 1 ATOM 1733 O O . GLY A 1 272 ? 4.561 48.733 38.432 1.00 15.49 ? 265 GLY A O 1 ATOM 1734 N N . ASP A 1 273 ? 2.995 47.980 39.863 1.00 13.28 ? 266 ASP A N 1 ATOM 1735 C CA . ASP A 1 273 ? 2.391 47.100 38.845 1.00 14.49 ? 266 ASP A CA 1 ATOM 1736 C C . ASP A 1 273 ? 2.158 47.889 37.544 1.00 15.33 ? 266 ASP A C 1 ATOM 1737 O O . ASP A 1 273 ? 1.475 48.924 37.564 1.00 15.79 ? 266 ASP A O 1 ATOM 1738 C CB . ASP A 1 273 ? 1.053 46.593 39.395 1.00 15.34 ? 266 ASP A CB 1 ATOM 1739 C CG . ASP A 1 273 ? 0.199 45.916 38.339 1.00 15.27 ? 266 ASP A CG 1 ATOM 1740 O OD1 . ASP A 1 273 ? 0.731 45.140 37.499 1.00 17.09 ? 266 ASP A OD1 1 ATOM 1741 O OD2 . ASP A 1 273 ? -1.019 46.157 38.370 1.00 16.99 ? 266 ASP A OD2 1 ATOM 1742 N N . PRO A 1 274 ? 2.697 47.405 36.409 1.00 15.43 ? 267 PRO A N 1 ATOM 1743 C CA . PRO A 1 274 ? 2.530 48.126 35.139 1.00 17.01 ? 267 PRO A CA 1 ATOM 1744 C C . PRO A 1 274 ? 1.072 48.457 34.769 1.00 16.62 ? 267 PRO A C 1 ATOM 1745 O O . PRO A 1 274 ? 0.829 49.425 34.033 1.00 17.39 ? 267 PRO A O 1 ATOM 1746 C CB . PRO A 1 274 ? 3.117 47.146 34.109 1.00 16.92 ? 267 PRO A CB 1 ATOM 1747 C CG . PRO A 1 274 ? 4.163 46.396 34.869 1.00 18.66 ? 267 PRO A CG 1 ATOM 1748 C CD . PRO A 1 274 ? 3.607 46.250 36.284 1.00 16.89 ? 267 PRO A CD 1 ATOM 1749 N N . LEU A 1 275 ? 0.114 47.662 35.254 1.00 16.34 ? 268 LEU A N 1 ATOM 1750 C CA . LEU A 1 275 ? -1.284 47.818 34.847 1.00 16.48 ? 268 LEU A CA 1 ATOM 1751 C C . LEU A 1 275 ? -2.136 48.751 35.720 1.00 14.92 ? 268 LEU A C 1 ATOM 1752 O O . LEU A 1 275 ? -3.255 49.135 35.309 1.00 15.53 ? 268 LEU A O 1 ATOM 1753 C CB . LEU A 1 275 ? -1.976 46.450 34.751 1.00 15.59 ? 268 LEU A CB 1 ATOM 1754 C CG . LEU A 1 275 ? -1.274 45.426 33.841 1.00 16.92 ? 268 LEU A CG 1 ATOM 1755 C CD1 . LEU A 1 275 ? -2.120 44.176 33.786 1.00 20.76 ? 268 LEU A CD1 1 ATOM 1756 C CD2 . LEU A 1 275 ? -1.023 45.977 32.429 1.00 19.05 ? 268 LEU A CD2 1 ATOM 1757 N N . THR A 1 276 ? -1.601 49.169 36.874 1.00 13.41 ? 269 THR A N 1 ATOM 1758 C CA . THR A 1 276 ? -2.430 49.894 37.871 1.00 14.17 ? 269 THR A CA 1 ATOM 1759 C C . THR A 1 276 ? -1.707 51.084 38.527 1.00 13.49 ? 269 THR A C 1 ATOM 1760 O O . THR A 1 276 ? -1.757 51.237 39.772 1.00 15.45 ? 269 THR A O 1 ATOM 1761 C CB . THR A 1 276 ? -2.930 48.947 39.011 1.00 14.76 ? 269 THR A CB 1 ATOM 1762 O OG1 . THR A 1 276 ? -1.790 48.397 39.717 1.00 16.22 ? 269 THR A OG1 1 ATOM 1763 C CG2 . THR A 1 276 ? -3.897 47.819 38.460 1.00 13.55 ? 269 THR A CG2 1 ATOM 1764 N N . PRO A 1 277 ? -1.049 51.934 37.711 1.00 14.62 ? 270 PRO A N 1 ATOM 1765 C CA . PRO A 1 277 ? -0.276 53.016 38.325 1.00 14.55 ? 270 PRO A CA 1 ATOM 1766 C C . PRO A 1 277 ? -1.179 53.952 39.143 1.00 15.89 ? 270 PRO A C 1 ATOM 1767 O O . PRO A 1 277 ? -2.235 54.419 38.633 1.00 17.38 ? 270 PRO A O 1 ATOM 1768 C CB . PRO A 1 277 ? 0.311 53.759 37.114 1.00 14.05 ? 270 PRO A CB 1 ATOM 1769 C CG . PRO A 1 277 ? -0.613 53.406 35.960 1.00 14.96 ? 270 PRO A CG 1 ATOM 1770 C CD . PRO A 1 277 ? -0.995 51.982 36.231 1.00 15.72 ? 270 PRO A CD 1 ATOM 1771 N N . GLY A 1 278 ? -0.785 54.200 40.395 1.00 14.73 ? 271 GLY A N 1 ATOM 1772 C CA . GLY A 1 278 ? -1.523 55.106 41.294 1.00 15.66 ? 271 GLY A CA 1 ATOM 1773 C C . GLY A 1 278 ? -2.437 54.437 42.311 1.00 15.75 ? 271 GLY A C 1 ATOM 1774 O O . GLY A 1 278 ? -2.805 55.060 43.317 1.00 16.81 ? 271 GLY A O 1 ATOM 1775 N N . TYR A 1 279 ? -2.815 53.176 42.069 1.00 15.35 ? 272 TYR A N 1 ATOM 1776 C CA . TYR A 1 279 ? -3.877 52.512 42.851 1.00 15.31 ? 272 TYR A CA 1 ATOM 1777 C C . TYR A 1 279 ? -3.487 51.055 43.082 1.00 15.27 ? 272 TYR A C 1 ATOM 1778 O O . TYR A 1 279 ? -2.882 50.423 42.194 1.00 15.00 ? 272 TYR A O 1 ATOM 1779 C CB . TYR A 1 279 ? -5.229 52.608 42.109 1.00 14.92 ? 272 TYR A CB 1 ATOM 1780 C CG . TYR A 1 279 ? -5.522 54.026 41.707 1.00 15.19 ? 272 TYR A CG 1 ATOM 1781 C CD1 . TYR A 1 279 ? -6.093 54.920 42.615 1.00 15.86 ? 272 TYR A CD1 1 ATOM 1782 C CD2 . TYR A 1 279 ? -5.118 54.514 40.450 1.00 16.10 ? 272 TYR A CD2 1 ATOM 1783 C CE1 . TYR A 1 279 ? -6.316 56.240 42.271 1.00 15.13 ? 272 TYR A CE1 1 ATOM 1784 C CE2 . TYR A 1 279 ? -5.312 55.838 40.098 1.00 16.47 ? 272 TYR A CE2 1 ATOM 1785 C CZ . TYR A 1 279 ? -5.922 56.698 41.013 1.00 15.45 ? 272 TYR A CZ 1 ATOM 1786 O OH . TYR A 1 279 ? -6.121 58.013 40.688 1.00 16.79 ? 272 TYR A OH 1 ATOM 1787 N N . PRO A 1 280 ? -3.876 50.485 44.244 1.00 15.34 ? 273 PRO A N 1 ATOM 1788 C CA . PRO A 1 280 ? -3.514 49.087 44.509 1.00 16.31 ? 273 PRO A CA 1 ATOM 1789 C C . PRO A 1 280 ? -4.202 48.116 43.548 1.00 16.19 ? 273 PRO A C 1 ATOM 1790 O O . PRO A 1 280 ? -5.401 48.298 43.224 1.00 16.59 ? 273 PRO A O 1 ATOM 1791 C CB . PRO A 1 280 ? -4.021 48.854 45.949 1.00 15.39 ? 273 PRO A CB 1 ATOM 1792 C CG . PRO A 1 280 ? -5.139 49.870 46.129 1.00 15.70 ? 273 PRO A CG 1 ATOM 1793 C CD . PRO A 1 280 ? -4.642 51.081 45.353 1.00 14.48 ? 273 PRO A CD 1 ATOM 1794 N N . ALA A 1 281 ? -3.456 47.085 43.126 1.00 14.50 ? 274 ALA A N 1 ATOM 1795 C CA . ALA A 1 281 ? -3.983 46.043 42.249 1.00 14.85 ? 274 ALA A CA 1 ATOM 1796 C C . ALA A 1 281 ? -4.830 45.038 43.045 1.00 16.74 ? 274 ALA A C 1 ATOM 1797 O O . ALA A 1 281 ? -4.490 43.850 43.155 1.00 18.69 ? 274 ALA A O 1 ATOM 1798 C CB . ALA A 1 281 ? -2.834 45.357 41.523 1.00 16.10 ? 274 ALA A CB 1 ATOM 1799 N N . ASN A 1 282 ? -5.923 45.551 43.617 1.00 16.65 ? 275 ASN A N 1 ATOM 1800 C CA . ASN A 1 282 ? -6.841 44.776 44.450 1.00 18.94 ? 275 ASN A CA 1 ATOM 1801 C C . ASN A 1 282 ? -7.856 44.005 43.584 1.00 21.07 ? 275 ASN A C 1 ATOM 1802 O O . ASN A 1 282 ? -7.699 43.954 42.355 1.00 19.73 ? 275 ASN A O 1 ATOM 1803 C CB . ASN A 1 282 ? -7.515 45.695 45.492 1.00 20.76 ? 275 ASN A CB 1 ATOM 1804 C CG . ASN A 1 282 ? -8.319 46.814 44.861 1.00 22.14 ? 275 ASN A CG 1 ATOM 1805 O OD1 . ASN A 1 282 ? -8.829 46.672 43.744 1.00 20.86 ? 275 ASN A OD1 1 ATOM 1806 N ND2 . ASN A 1 282 ? -8.466 47.937 45.586 1.00 24.34 ? 275 ASN A ND2 1 ATOM 1807 N N A GLU A 1 283 ? -8.883 43.415 44.206 0.50 21.73 ? 276 GLU A N 1 ATOM 1808 N N B GLU A 1 283 ? -8.874 43.417 44.220 0.50 21.90 ? 276 GLU A N 1 ATOM 1809 C CA A GLU A 1 283 ? -9.789 42.507 43.491 0.50 23.52 ? 276 GLU A CA 1 ATOM 1810 C CA B GLU A 1 283 ? -9.830 42.558 43.526 0.50 24.06 ? 276 GLU A CA 1 ATOM 1811 C C A GLU A 1 283 ? -10.774 43.183 42.523 0.50 24.44 ? 276 GLU A C 1 ATOM 1812 C C B GLU A 1 283 ? -10.516 43.272 42.371 0.50 23.36 ? 276 GLU A C 1 ATOM 1813 O O A GLU A 1 283 ? -11.393 42.497 41.694 0.50 24.18 ? 276 GLU A O 1 ATOM 1814 O O B GLU A 1 283 ? -10.670 42.720 41.278 0.50 25.65 ? 276 GLU A O 1 ATOM 1815 C CB A GLU A 1 283 ? -10.567 41.623 44.479 0.50 25.89 ? 276 GLU A CB 1 ATOM 1816 C CB B GLU A 1 283 ? -10.912 42.076 44.501 0.50 26.16 ? 276 GLU A CB 1 ATOM 1817 C CG A GLU A 1 283 ? -11.475 40.607 43.814 0.50 30.64 ? 276 GLU A CG 1 ATOM 1818 C CG B GLU A 1 283 ? -11.117 40.585 44.471 0.50 31.46 ? 276 GLU A CG 1 ATOM 1819 C CD A GLU A 1 283 ? -10.736 39.334 43.439 0.50 29.46 ? 276 GLU A CD 1 ATOM 1820 C CD B GLU A 1 283 ? -9.896 39.857 44.970 0.50 32.91 ? 276 GLU A CD 1 ATOM 1821 O OE1 A GLU A 1 283 ? -10.131 38.706 44.333 0.50 33.68 ? 276 GLU A OE1 1 ATOM 1822 O OE1 B GLU A 1 283 ? -9.376 38.988 44.246 0.50 32.03 ? 276 GLU A OE1 1 ATOM 1823 O OE2 A GLU A 1 283 ? -10.760 38.963 42.253 0.50 30.64 ? 276 GLU A OE2 1 ATOM 1824 O OE2 B GLU A 1 283 ? -9.451 40.163 46.092 0.50 35.41 ? 276 GLU A OE2 1 ATOM 1825 N N . TYR A 1 284 ? -10.938 44.504 42.630 1.00 22.46 ? 277 TYR A N 1 ATOM 1826 C CA . TYR A 1 284 ? -11.818 45.222 41.693 1.00 23.09 ? 277 TYR A CA 1 ATOM 1827 C C . TYR A 1 284 ? -11.076 46.240 40.845 1.00 22.23 ? 277 TYR A C 1 ATOM 1828 O O . TYR A 1 284 ? -11.706 47.061 40.175 1.00 24.66 ? 277 TYR A O 1 ATOM 1829 C CB . TYR A 1 284 ? -12.997 45.871 42.441 1.00 23.09 ? 277 TYR A CB 1 ATOM 1830 C CG . TYR A 1 284 ? -12.542 46.838 43.497 1.00 23.15 ? 277 TYR A CG 1 ATOM 1831 C CD1 . TYR A 1 284 ? -12.299 48.184 43.177 1.00 24.47 ? 277 TYR A CD1 1 ATOM 1832 C CD2 . TYR A 1 284 ? -12.307 46.413 44.807 1.00 23.52 ? 277 TYR A CD2 1 ATOM 1833 C CE1 . TYR A 1 284 ? -11.857 49.078 44.137 1.00 25.12 ? 277 TYR A CE1 1 ATOM 1834 C CE2 . TYR A 1 284 ? -11.872 47.304 45.777 1.00 24.13 ? 277 TYR A CE2 1 ATOM 1835 C CZ . TYR A 1 284 ? -11.641 48.632 45.423 1.00 25.81 ? 277 TYR A CZ 1 ATOM 1836 O OH . TYR A 1 284 ? -11.204 49.526 46.361 1.00 27.45 ? 277 TYR A OH 1 ATOM 1837 N N . ALA A 1 285 ? -9.744 46.197 40.874 1.00 22.42 ? 278 ALA A N 1 ATOM 1838 C CA . ALA A 1 285 ? -8.929 47.145 40.115 1.00 23.46 ? 278 ALA A CA 1 ATOM 1839 C C . ALA A 1 285 ? -9.277 47.165 38.636 1.00 23.66 ? 278 ALA A C 1 ATOM 1840 O O . ALA A 1 285 ? -9.559 46.107 38.038 1.00 25.81 ? 278 ALA A O 1 ATOM 1841 C CB . ALA A 1 285 ? -7.446 46.835 40.303 1.00 25.15 ? 278 ALA A CB 1 ATOM 1842 N N . TYR A 1 286 ? -9.295 48.366 38.061 1.00 22.28 ? 279 TYR A N 1 ATOM 1843 C CA . TYR A 1 286 ? -9.348 48.506 36.609 1.00 23.16 ? 279 TYR A CA 1 ATOM 1844 C C . TYR A 1 286 ? -7.910 48.489 36.126 1.00 22.97 ? 279 TYR A C 1 ATOM 1845 O O . TYR A 1 286 ? -7.040 49.171 36.687 1.00 26.88 ? 279 TYR A O 1 ATOM 1846 C CB . TYR A 1 286 ? -10.089 49.782 36.139 1.00 28.06 ? 279 TYR A CB 1 ATOM 1847 C CG A TYR A 1 286 ? -10.469 49.716 34.669 0.50 25.39 ? 279 TYR A CG 1 ATOM 1848 C CG B TYR A 1 286 ? -9.460 50.435 34.874 0.50 28.77 ? 279 TYR A CG 1 ATOM 1849 C CD1 A TYR A 1 286 ? -11.545 48.939 34.226 0.50 25.58 ? 279 TYR A CD1 1 ATOM 1850 C CD1 B TYR A 1 286 ? -10.161 50.509 33.677 0.50 29.73 ? 279 TYR A CD1 1 ATOM 1851 C CD2 A TYR A 1 286 ? -9.725 50.407 33.722 0.50 26.49 ? 279 TYR A CD2 1 ATOM 1852 C CD2 B TYR A 1 286 ? -8.158 50.953 34.893 0.50 30.39 ? 279 TYR A CD2 1 ATOM 1853 C CE1 A TYR A 1 286 ? -11.872 48.876 32.880 0.50 28.70 ? 279 TYR A CE1 1 ATOM 1854 C CE1 B TYR A 1 286 ? -9.599 51.088 32.548 0.50 32.45 ? 279 TYR A CE1 1 ATOM 1855 C CE2 A TYR A 1 286 ? -10.046 50.347 32.381 0.50 27.80 ? 279 TYR A CE2 1 ATOM 1856 C CE2 B TYR A 1 286 ? -7.578 51.515 33.766 0.50 29.65 ? 279 TYR A CE2 1 ATOM 1857 C CZ A TYR A 1 286 ? -11.112 49.585 31.966 0.50 29.53 ? 279 TYR A CZ 1 ATOM 1858 C CZ B TYR A 1 286 ? -8.309 51.589 32.594 0.50 34.67 ? 279 TYR A CZ 1 ATOM 1859 O OH A TYR A 1 286 ? -11.393 49.539 30.628 0.50 35.34 ? 279 TYR A OH 1 ATOM 1860 O OH B TYR A 1 286 ? -7.760 52.168 31.464 0.50 37.09 ? 279 TYR A OH 1 ATOM 1861 N N . ARG A 1 287 ? -7.648 47.664 35.123 1.00 19.32 ? 280 ARG A N 1 ATOM 1862 C CA . ARG A 1 287 ? -6.292 47.498 34.608 1.00 19.58 ? 280 ARG A CA 1 ATOM 1863 C C . ARG A 1 287 ? -6.191 48.118 33.257 1.00 22.34 ? 280 ARG A C 1 ATOM 1864 O O . ARG A 1 287 ? -7.093 47.960 32.427 1.00 23.61 ? 280 ARG A O 1 ATOM 1865 C CB A ARG A 1 287 ? -5.965 46.001 34.494 0.65 21.04 ? 280 ARG A CB 1 ATOM 1866 C CB B ARG A 1 287 ? -5.961 46.031 34.474 0.35 17.94 ? 280 ARG A CB 1 ATOM 1867 C CG A ARG A 1 287 ? -5.297 45.366 35.715 0.65 24.24 ? 280 ARG A CG 1 ATOM 1868 C CG B ARG A 1 287 ? -6.008 45.332 35.798 0.35 13.57 ? 280 ARG A CG 1 ATOM 1869 C CD A ARG A 1 287 ? -6.264 44.862 36.768 0.65 29.36 ? 280 ARG A CD 1 ATOM 1870 C CD B ARG A 1 287 ? -5.512 43.917 35.663 0.35 11.08 ? 280 ARG A CD 1 ATOM 1871 N NE A ARG A 1 287 ? -5.559 44.306 37.932 0.65 27.48 ? 280 ARG A NE 1 ATOM 1872 N NE B ARG A 1 287 ? -5.203 43.439 36.990 0.35 12.38 ? 280 ARG A NE 1 ATOM 1873 C CZ A ARG A 1 287 ? -6.164 43.857 39.028 0.65 25.15 ? 280 ARG A CZ 1 ATOM 1874 C CZ B ARG A 1 287 ? -6.120 43.066 37.866 0.35 11.86 ? 280 ARG A CZ 1 ATOM 1875 N NH1 A ARG A 1 287 ? -7.484 43.891 39.124 0.65 28.91 ? 280 ARG A NH1 1 ATOM 1876 N NH1 B ARG A 1 287 ? -7.398 43.090 37.534 0.35 11.68 ? 280 ARG A NH1 1 ATOM 1877 N NH2 A ARG A 1 287 ? -5.457 43.385 40.039 0.65 22.84 ? 280 ARG A NH2 1 ATOM 1878 N NH2 B ARG A 1 287 ? -5.760 42.665 39.073 0.35 14.64 ? 280 ARG A NH2 1 ATOM 1879 N N . ARG A 1 288 ? -5.075 48.793 33.017 1.00 21.33 ? 281 ARG A N 1 ATOM 1880 C CA . ARG A 1 288 ? -4.720 49.202 31.666 1.00 22.14 ? 281 ARG A CA 1 ATOM 1881 C C . ARG A 1 288 ? -4.559 47.981 30.769 1.00 23.08 ? 281 ARG A C 1 ATOM 1882 O O . ARG A 1 288 ? -4.187 46.880 31.232 1.00 23.18 ? 281 ARG A O 1 ATOM 1883 C CB . ARG A 1 288 ? -3.398 49.940 31.695 1.00 21.53 ? 281 ARG A CB 1 ATOM 1884 C CG . ARG A 1 288 ? -3.496 51.265 32.406 1.00 21.60 ? 281 ARG A CG 1 ATOM 1885 C CD . ARG A 1 288 ? -2.187 51.994 32.340 1.00 23.45 ? 281 ARG A CD 1 ATOM 1886 N NE . ARG A 1 288 ? -2.342 53.345 32.882 1.00 25.82 ? 281 ARG A NE 1 ATOM 1887 C CZ . ARG A 1 288 ? -1.477 54.331 32.683 1.00 26.04 ? 281 ARG A CZ 1 ATOM 1888 N NH1 . ARG A 1 288 ? -0.404 54.125 31.939 1.00 25.12 ? 281 ARG A NH1 1 ATOM 1889 N NH2 . ARG A 1 288 ? -1.687 55.527 33.220 1.00 27.91 ? 281 ARG A NH2 1 ATOM 1890 N N . GLY A 1 289 ? -4.831 48.185 29.485 1.00 24.48 ? 282 GLY A N 1 ATOM 1891 C CA . GLY A 1 289 ? -4.465 47.216 28.464 1.00 27.91 ? 282 GLY A CA 1 ATOM 1892 C C . GLY A 1 289 ? -2.955 47.166 28.369 1.00 27.28 ? 282 GLY A C 1 ATOM 1893 O O . GLY A 1 289 ? -2.270 48.123 28.759 1.00 27.95 ? 282 GLY A O 1 ATOM 1894 N N . ILE A 1 290 ? -2.430 46.045 27.882 1.00 29.83 ? 283 ILE A N 1 ATOM 1895 C CA . ILE A 1 290 ? -0.987 45.868 27.766 1.00 29.62 ? 283 ILE A CA 1 ATOM 1896 C C . ILE A 1 290 ? -0.342 47.015 26.973 1.00 27.87 ? 283 ILE A C 1 ATOM 1897 O O . ILE A 1 290 ? 0.716 47.512 27.361 1.00 28.65 ? 283 ILE A O 1 ATOM 1898 C CB A ILE A 1 290 ? -0.646 44.452 27.227 0.65 29.61 ? 283 ILE A CB 1 ATOM 1899 C CB B ILE A 1 290 ? -0.592 44.503 27.128 0.35 27.23 ? 283 ILE A CB 1 ATOM 1900 C CG1 A ILE A 1 290 ? 0.788 44.062 27.579 0.65 31.30 ? 283 ILE A CG1 1 ATOM 1901 C CG1 B ILE A 1 290 ? -0.759 43.351 28.125 0.35 24.44 ? 283 ILE A CG1 1 ATOM 1902 C CG2 A ILE A 1 290 ? -0.984 44.304 25.746 0.65 34.13 ? 283 ILE A CG2 1 ATOM 1903 C CG2 B ILE A 1 290 ? 0.848 44.518 26.614 0.35 23.79 ? 283 ILE A CG2 1 ATOM 1904 C CD1 A ILE A 1 290 ? 0.939 43.673 29.035 0.65 26.80 ? 283 ILE A CD1 1 ATOM 1905 C CD1 B ILE A 1 290 ? 0.254 43.345 29.251 0.35 23.46 ? 283 ILE A CD1 1 ATOM 1906 N N . ALA A 1 291 ? -1.007 47.480 25.915 1.00 30.87 ? 284 ALA A N 1 ATOM 1907 C CA . ALA A 1 291 ? -0.471 48.561 25.074 1.00 31.32 ? 284 ALA A CA 1 ATOM 1908 C C . ALA A 1 291 ? -0.253 49.863 25.837 1.00 31.99 ? 284 ALA A C 1 ATOM 1909 O O . ALA A 1 291 ? 0.588 50.678 25.446 1.00 32.57 ? 284 ALA A O 1 ATOM 1910 C CB . ALA A 1 291 ? -1.373 48.804 23.877 1.00 36.53 ? 284 ALA A CB 1 ATOM 1911 N N . GLU A 1 292 ? -1.007 50.055 26.920 1.00 29.78 ? 285 GLU A N 1 ATOM 1912 C CA . GLU A 1 292 ? -0.905 51.264 27.743 1.00 29.61 ? 285 GLU A CA 1 ATOM 1913 C C . GLU A 1 292 ? -0.185 51.021 29.078 1.00 27.67 ? 285 GLU A C 1 ATOM 1914 O O . GLU A 1 292 ? -0.099 51.932 29.920 1.00 29.07 ? 285 GLU A O 1 ATOM 1915 C CB . GLU A 1 292 ? -2.292 51.866 28.009 1.00 30.50 ? 285 GLU A CB 1 ATOM 1916 C CG . GLU A 1 292 ? -2.992 52.444 26.779 1.00 32.00 ? 285 GLU A CG 1 ATOM 1917 C CD . GLU A 1 292 ? -3.491 51.383 25.800 1.00 41.73 ? 285 GLU A CD 1 ATOM 1918 O OE1 . GLU A 1 292 ? -4.060 50.352 26.235 1.00 41.78 ? 285 GLU A OE1 1 ATOM 1919 O OE2 . GLU A 1 292 ? -3.308 51.580 24.576 1.00 53.79 ? 285 GLU A OE2 1 ATOM 1920 N N . ALA A 1 293 ? 0.335 49.808 29.273 1.00 25.09 ? 286 ALA A N 1 ATOM 1921 C CA . ALA A 1 293 ? 1.008 49.455 30.521 1.00 23.29 ? 286 ALA A CA 1 ATOM 1922 C C . ALA A 1 293 ? 2.234 50.346 30.704 1.00 23.93 ? 286 ALA A C 1 ATOM 1923 O O . ALA A 1 293 ? 2.780 50.883 29.729 1.00 24.10 ? 286 ALA A O 1 ATOM 1924 C CB . ALA A 1 293 ? 1.406 47.990 30.539 1.00 23.67 ? 286 ALA A CB 1 ATOM 1925 N N . VAL A 1 294 ? 2.615 50.546 31.958 1.00 19.42 ? 287 VAL A N 1 ATOM 1926 C CA . VAL A 1 294 ? 3.786 51.360 32.277 1.00 19.20 ? 287 VAL A CA 1 ATOM 1927 C C . VAL A 1 294 ? 5.069 50.535 32.182 1.00 20.18 ? 287 VAL A C 1 ATOM 1928 O O . VAL A 1 294 ? 5.175 49.453 32.797 1.00 19.36 ? 287 VAL A O 1 ATOM 1929 C CB . VAL A 1 294 ? 3.711 52.016 33.689 1.00 19.23 ? 287 VAL A CB 1 ATOM 1930 C CG1 . VAL A 1 294 ? 4.957 52.877 33.936 1.00 19.44 ? 287 VAL A CG1 1 ATOM 1931 C CG2 . VAL A 1 294 ? 2.455 52.869 33.847 1.00 21.78 ? 287 VAL A CG2 1 ATOM 1932 N N . GLY A 1 295 ? 6.020 51.033 31.387 1.00 19.51 ? 288 GLY A N 1 ATOM 1933 C CA . GLY A 1 295 ? 7.406 50.616 31.523 1.00 20.18 ? 288 GLY A CA 1 ATOM 1934 C C . GLY A 1 295 ? 7.839 49.383 30.770 1.00 18.08 ? 288 GLY A C 1 ATOM 1935 O O . GLY A 1 295 ? 8.966 48.954 30.947 1.00 18.64 ? 288 GLY A O 1 ATOM 1936 N N . LEU A 1 296 ? 6.972 48.813 29.925 1.00 18.65 ? 289 LEU A N 1 ATOM 1937 C CA . LEU A 1 296 ? 7.364 47.586 29.206 1.00 18.63 ? 289 LEU A CA 1 ATOM 1938 C C . LEU A 1 296 ? 8.302 47.876 28.041 1.00 19.50 ? 289 LEU A C 1 ATOM 1939 O O . LEU A 1 296 ? 8.135 48.881 27.339 1.00 21.01 ? 289 LEU A O 1 ATOM 1940 C CB A LEU A 1 296 ? 6.134 46.834 28.673 0.65 18.88 ? 289 LEU A CB 1 ATOM 1941 C CB B LEU A 1 296 ? 6.140 46.794 28.723 0.35 19.46 ? 289 LEU A CB 1 ATOM 1942 C CG A LEU A 1 296 ? 5.009 46.465 29.647 0.65 18.78 ? 289 LEU A CG 1 ATOM 1943 C CG B LEU A 1 296 ? 5.583 45.728 29.676 0.35 19.84 ? 289 LEU A CG 1 ATOM 1944 C CD1 A LEU A 1 296 ? 3.857 45.898 28.840 0.65 18.31 ? 289 LEU A CD1 1 ATOM 1945 C CD1 B LEU A 1 296 ? 5.065 46.336 30.978 0.35 19.59 ? 289 LEU A CD1 1 ATOM 1946 C CD2 A LEU A 1 296 ? 5.490 45.454 30.685 0.65 23.63 ? 289 LEU A CD2 1 ATOM 1947 C CD2 B LEU A 1 296 ? 4.491 44.932 28.971 0.35 20.84 ? 289 LEU A CD2 1 ATOM 1948 N N . PRO A 1 297 ? 9.289 46.998 27.822 1.00 20.10 ? 290 PRO A N 1 ATOM 1949 C CA . PRO A 1 297 ? 10.177 47.145 26.664 1.00 20.92 ? 290 PRO A CA 1 ATOM 1950 C C . PRO A 1 297 ? 9.468 46.782 25.353 1.00 22.24 ? 290 PRO A C 1 ATOM 1951 O O . PRO A 1 297 ? 8.558 45.937 25.350 1.00 21.76 ? 290 PRO A O 1 ATOM 1952 C CB . PRO A 1 297 ? 11.304 46.147 26.962 1.00 23.36 ? 290 PRO A CB 1 ATOM 1953 C CG . PRO A 1 297 ? 10.672 45.113 27.835 1.00 22.85 ? 290 PRO A CG 1 ATOM 1954 C CD . PRO A 1 297 ? 9.611 45.809 28.638 1.00 22.26 ? 290 PRO A CD 1 ATOM 1955 N N A SER A 1 298 ? 9.900 47.408 24.260 0.60 22.39 ? 291 SER A N 1 ATOM 1956 N N B SER A 1 298 ? 9.884 47.396 24.247 0.40 22.59 ? 291 SER A N 1 ATOM 1957 C CA A SER A 1 298 ? 9.265 47.208 22.957 0.60 23.73 ? 291 SER A CA 1 ATOM 1958 C CA B SER A 1 298 ? 9.239 47.144 22.950 0.40 23.52 ? 291 SER A CA 1 ATOM 1959 C C A SER A 1 298 ? 10.005 46.188 22.083 0.60 22.63 ? 291 SER A C 1 ATOM 1960 C C B SER A 1 298 ? 10.052 46.245 22.032 0.40 22.44 ? 291 SER A C 1 ATOM 1961 O O A SER A 1 298 ? 9.499 45.781 21.034 0.60 23.88 ? 291 SER A O 1 ATOM 1962 O O B SER A 1 298 ? 9.658 46.000 20.888 0.40 22.84 ? 291 SER A O 1 ATOM 1963 C CB A SER A 1 298 ? 9.113 48.546 22.225 0.60 26.56 ? 291 SER A CB 1 ATOM 1964 C CB B SER A 1 298 ? 8.945 48.453 22.231 0.40 26.31 ? 291 SER A CB 1 ATOM 1965 O OG A SER A 1 298 ? 10.372 49.113 21.898 0.60 26.50 ? 291 SER A OG 1 ATOM 1966 O OG B SER A 1 298 ? 8.199 49.308 23.060 0.40 29.17 ? 291 SER A OG 1 ATOM 1967 N N . ILE A 1 299 ? 11.193 45.775 22.524 1.00 22.01 ? 292 ILE A N 1 ATOM 1968 C CA . ILE A 1 299 ? 12.058 44.873 21.743 1.00 21.47 ? 292 ILE A CA 1 ATOM 1969 C C . ILE A 1 299 ? 12.472 43.679 22.609 1.00 22.03 ? 292 ILE A C 1 ATOM 1970 O O . ILE A 1 299 ? 12.573 43.816 23.834 1.00 22.96 ? 292 ILE A O 1 ATOM 1971 C CB . ILE A 1 299 ? 13.298 45.608 21.148 1.00 21.92 ? 292 ILE A CB 1 ATOM 1972 C CG1 . ILE A 1 299 ? 14.161 46.259 22.253 1.00 23.41 ? 292 ILE A CG1 1 ATOM 1973 C CG2 . ILE A 1 299 ? 12.861 46.599 20.060 1.00 24.45 ? 292 ILE A CG2 1 ATOM 1974 C CD1 . ILE A 1 299 ? 15.385 46.995 21.731 1.00 25.69 ? 292 ILE A CD1 1 ATOM 1975 N N . PRO A 1 300 ? 12.696 42.503 21.989 1.00 21.49 ? 293 PRO A N 1 ATOM 1976 C CA . PRO A 1 300 ? 13.046 41.336 22.802 1.00 21.72 ? 293 PRO A CA 1 ATOM 1977 C C . PRO A 1 300 ? 14.446 41.461 23.412 1.00 21.08 ? 293 PRO A C 1 ATOM 1978 O O . PRO A 1 300 ? 15.332 42.096 22.809 1.00 20.78 ? 293 PRO A O 1 ATOM 1979 C CB . PRO A 1 300 ? 13.017 40.177 21.787 1.00 21.36 ? 293 PRO A CB 1 ATOM 1980 C CG . PRO A 1 300 ? 12.180 40.671 20.636 1.00 23.44 ? 293 PRO A CG 1 ATOM 1981 C CD . PRO A 1 300 ? 12.455 42.145 20.574 1.00 22.23 ? 293 PRO A CD 1 ATOM 1982 N N . VAL A 1 301 ? 14.638 40.859 24.588 1.00 19.40 ? 294 VAL A N 1 ATOM 1983 C CA . VAL A 1 301 ? 15.880 40.982 25.365 1.00 19.83 ? 294 VAL A CA 1 ATOM 1984 C C . VAL A 1 301 ? 16.137 39.637 26.026 1.00 20.69 ? 294 VAL A C 1 ATOM 1985 O O . VAL A 1 301 ? 15.179 38.973 26.475 1.00 20.13 ? 294 VAL A O 1 ATOM 1986 C CB . VAL A 1 301 ? 15.745 42.044 26.485 1.00 17.79 ? 294 VAL A CB 1 ATOM 1987 C CG1 . VAL A 1 301 ? 17.056 42.209 27.272 1.00 21.32 ? 294 VAL A CG1 1 ATOM 1988 C CG2 . VAL A 1 301 ? 15.297 43.393 25.911 1.00 20.89 ? 294 VAL A CG2 1 ATOM 1989 N N . HIS A 1 302 ? 17.413 39.236 26.099 1.00 18.98 ? 295 HIS A N 1 ATOM 1990 C CA . HIS A 1 302 ? 17.772 37.967 26.725 1.00 18.94 ? 295 HIS A CA 1 ATOM 1991 C C . HIS A 1 302 ? 19.170 38.035 27.292 1.00 20.06 ? 295 HIS A C 1 ATOM 1992 O O . HIS A 1 302 ? 20.066 38.636 26.658 1.00 20.01 ? 295 HIS A O 1 ATOM 1993 C CB . HIS A 1 302 ? 17.613 36.826 25.712 1.00 19.22 ? 295 HIS A CB 1 ATOM 1994 C CG . HIS A 1 302 ? 17.662 35.435 26.317 1.00 19.34 ? 295 HIS A CG 1 ATOM 1995 N ND1 . HIS A 1 302 ? 16.696 34.959 27.143 1.00 19.86 ? 295 HIS A ND1 1 ATOM 1996 C CD2 . HIS A 1 302 ? 18.586 34.403 26.154 1.00 20.52 ? 295 HIS A CD2 1 ATOM 1997 C CE1 . HIS A 1 302 ? 16.999 33.702 27.509 1.00 20.95 ? 295 HIS A CE1 1 ATOM 1998 N NE2 . HIS A 1 302 ? 18.155 33.356 26.901 1.00 21.27 ? 295 HIS A NE2 1 ATOM 1999 N N . PRO A 1 303 ? 19.390 37.433 28.489 1.00 19.20 ? 296 PRO A N 1 ATOM 2000 C CA . PRO A 1 303 ? 20.734 37.457 29.091 1.00 18.13 ? 296 PRO A CA 1 ATOM 2001 C C . PRO A 1 303 ? 21.476 36.136 28.882 1.00 18.98 ? 296 PRO A C 1 ATOM 2002 O O . PRO A 1 303 ? 20.838 35.064 28.820 1.00 20.77 ? 296 PRO A O 1 ATOM 2003 C CB . PRO A 1 303 ? 20.421 37.623 30.584 1.00 18.88 ? 296 PRO A CB 1 ATOM 2004 C CG . PRO A 1 303 ? 19.132 36.861 30.762 1.00 18.51 ? 296 PRO A CG 1 ATOM 2005 C CD . PRO A 1 303 ? 18.390 36.909 29.446 1.00 18.92 ? 296 PRO A CD 1 ATOM 2006 N N . ILE A 1 304 ? 22.802 36.220 28.761 1.00 19.64 ? 297 ILE A N 1 ATOM 2007 C CA . ILE A 1 304 ? 23.652 35.036 28.551 1.00 20.05 ? 297 ILE A CA 1 ATOM 2008 C C . ILE A 1 304 ? 24.941 35.136 29.378 1.00 21.05 ? 297 ILE A C 1 ATOM 2009 O O . ILE A 1 304 ? 25.287 36.223 29.878 1.00 20.87 ? 297 ILE A O 1 ATOM 2010 C CB . ILE A 1 304 ? 24.010 34.816 27.055 1.00 20.90 ? 297 ILE A CB 1 ATOM 2011 C CG1 . ILE A 1 304 ? 24.862 35.981 26.501 1.00 19.97 ? 297 ILE A CG1 1 ATOM 2012 C CG2 . ILE A 1 304 ? 22.759 34.565 26.212 1.00 20.69 ? 297 ILE A CG2 1 ATOM 2013 C CD1 . ILE A 1 304 ? 25.319 35.768 25.066 1.00 21.22 ? 297 ILE A CD1 1 ATOM 2014 N N . GLY A 1 305 ? 25.635 34.005 29.513 1.00 19.97 ? 298 GLY A N 1 ATOM 2015 C CA . GLY A 1 305 ? 26.915 33.949 30.204 1.00 21.40 ? 298 GLY A CA 1 ATOM 2016 C C . GLY A 1 305 ? 28.046 34.215 29.240 1.00 22.76 ? 298 GLY A C 1 ATOM 2017 O O . GLY A 1 305 ? 27.824 34.405 28.024 1.00 21.94 ? 298 GLY A O 1 ATOM 2018 N N . TYR A 1 306 ? 29.265 34.247 29.772 1.00 21.75 ? 299 TYR A N 1 ATOM 2019 C CA . TYR A 1 306 ? 30.400 34.640 28.947 1.00 22.08 ? 299 TYR A CA 1 ATOM 2020 C C . TYR A 1 306 ? 30.939 33.548 28.018 1.00 23.08 ? 299 TYR A C 1 ATOM 2021 O O . TYR A 1 306 ? 31.564 33.872 27.018 1.00 25.76 ? 299 TYR A O 1 ATOM 2022 C CB . TYR A 1 306 ? 31.509 35.354 29.742 1.00 23.32 ? 299 TYR A CB 1 ATOM 2023 C CG . TYR A 1 306 ? 32.118 34.618 30.925 1.00 24.70 ? 299 TYR A CG 1 ATOM 2024 C CD1 . TYR A 1 306 ? 31.675 34.877 32.226 1.00 23.74 ? 299 TYR A CD1 1 ATOM 2025 C CD2 . TYR A 1 306 ? 33.179 33.712 30.752 1.00 24.06 ? 299 TYR A CD2 1 ATOM 2026 C CE1 . TYR A 1 306 ? 32.242 34.244 33.322 1.00 21.39 ? 299 TYR A CE1 1 ATOM 2027 C CE2 . TYR A 1 306 ? 33.752 33.069 31.846 1.00 22.11 ? 299 TYR A CE2 1 ATOM 2028 C CZ . TYR A 1 306 ? 33.280 33.337 33.129 1.00 23.86 ? 299 TYR A CZ 1 ATOM 2029 O OH . TYR A 1 306 ? 33.841 32.699 34.227 1.00 22.41 ? 299 TYR A OH 1 ATOM 2030 N N . TYR A 1 307 ? 30.677 32.271 28.308 1.00 24.09 ? 300 TYR A N 1 ATOM 2031 C CA . TYR A 1 307 ? 30.981 31.229 27.301 1.00 23.90 ? 300 TYR A CA 1 ATOM 2032 C C . TYR A 1 307 ? 30.178 31.472 26.025 1.00 23.60 ? 300 TYR A C 1 ATOM 2033 O O . TYR A 1 307 ? 30.724 31.434 24.917 1.00 24.55 ? 300 TYR A O 1 ATOM 2034 C CB . TYR A 1 307 ? 30.662 29.826 27.815 1.00 25.10 ? 300 TYR A CB 1 ATOM 2035 C CG . TYR A 1 307 ? 31.580 29.280 28.876 1.00 26.98 ? 300 TYR A CG 1 ATOM 2036 C CD1 . TYR A 1 307 ? 32.884 29.773 29.044 1.00 27.71 ? 300 TYR A CD1 1 ATOM 2037 C CD2 . TYR A 1 307 ? 31.164 28.219 29.689 1.00 25.45 ? 300 TYR A CD2 1 ATOM 2038 C CE1 . TYR A 1 307 ? 33.733 29.246 30.009 1.00 28.27 ? 300 TYR A CE1 1 ATOM 2039 C CE2 . TYR A 1 307 ? 32.016 27.676 30.651 1.00 28.22 ? 300 TYR A CE2 1 ATOM 2040 C CZ . TYR A 1 307 ? 33.291 28.196 30.809 1.00 29.94 ? 300 TYR A CZ 1 ATOM 2041 O OH . TYR A 1 307 ? 34.134 27.650 31.760 1.00 32.55 ? 300 TYR A OH 1 ATOM 2042 N N . ASP A 1 308 ? 28.879 31.731 26.190 1.00 24.08 ? 301 ASP A N 1 ATOM 2043 C CA . ASP A 1 308 ? 28.006 32.009 25.054 1.00 25.29 ? 301 ASP A CA 1 ATOM 2044 C C . ASP A 1 308 ? 28.333 33.366 24.406 1.00 24.82 ? 301 ASP A C 1 ATOM 2045 O O . ASP A 1 308 ? 28.339 33.494 23.177 1.00 26.01 ? 301 ASP A O 1 ATOM 2046 C CB . ASP A 1 308 ? 26.543 31.969 25.491 1.00 24.17 ? 301 ASP A CB 1 ATOM 2047 C CG . ASP A 1 308 ? 25.998 30.541 25.618 1.00 24.38 ? 301 ASP A CG 1 ATOM 2048 O OD1 . ASP A 1 308 ? 26.603 29.589 25.066 1.00 26.92 ? 301 ASP A OD1 1 ATOM 2049 O OD2 . ASP A 1 308 ? 24.951 30.364 26.288 1.00 24.16 ? 301 ASP A OD2 1 ATOM 2050 N N . ALA A 1 309 ? 28.609 34.378 25.226 1.00 24.96 ? 302 ALA A N 1 ATOM 2051 C CA . ALA A 1 309 ? 28.958 35.704 24.692 1.00 24.44 ? 302 ALA A CA 1 ATOM 2052 C C . ALA A 1 309 ? 30.194 35.637 23.808 1.00 26.07 ? 302 ALA A C 1 ATOM 2053 O O . ALA A 1 309 ? 30.239 36.264 22.746 1.00 28.36 ? 302 ALA A O 1 ATOM 2054 C CB . ALA A 1 309 ? 29.167 36.702 25.818 1.00 24.23 ? 302 ALA A CB 1 ATOM 2055 N N . GLN A 1 310 ? 31.194 34.879 24.254 1.00 25.25 ? 303 GLN A N 1 ATOM 2056 C CA . GLN A 1 310 ? 32.415 34.685 23.481 1.00 27.07 ? 303 GLN A CA 1 ATOM 2057 C C . GLN A 1 310 ? 32.099 34.223 22.047 1.00 28.23 ? 303 GLN A C 1 ATOM 2058 O O . GLN A 1 310 ? 32.674 34.735 21.082 1.00 29.57 ? 303 GLN A O 1 ATOM 2059 C CB . GLN A 1 310 ? 33.304 33.664 24.170 1.00 28.48 ? 303 GLN A CB 1 ATOM 2060 C CG . GLN A 1 310 ? 34.567 33.348 23.386 1.00 34.50 ? 303 GLN A CG 1 ATOM 2061 C CD . GLN A 1 310 ? 35.795 33.878 24.075 1.00 40.79 ? 303 GLN A CD 1 ATOM 2062 O OE1 . GLN A 1 310 ? 36.583 34.623 23.493 0.80 50.55 ? 303 GLN A OE1 1 ATOM 2063 N NE2 . GLN A 1 310 ? 35.968 33.493 25.333 1.00 36.71 ? 303 GLN A NE2 1 ATOM 2064 N N . LYS A 1 311 ? 31.177 33.270 21.917 1.00 28.34 ? 304 LYS A N 1 ATOM 2065 C CA . LYS A 1 311 ? 30.815 32.733 20.604 1.00 28.54 ? 304 LYS A CA 1 ATOM 2066 C C . LYS A 1 311 ? 30.082 33.772 19.749 1.00 29.76 ? 304 LYS A C 1 ATOM 2067 O O . LYS A 1 311 ? 30.183 33.746 18.526 1.00 33.37 ? 304 LYS A O 1 ATOM 2068 C CB . LYS A 1 311 ? 29.977 31.456 20.746 1.00 31.31 ? 304 LYS A CB 1 ATOM 2069 C CG . LYS A 1 311 ? 30.653 30.329 21.534 1.00 32.92 ? 304 LYS A CG 1 ATOM 2070 C CD . LYS A 1 311 ? 31.895 29.767 20.838 1.00 37.53 ? 304 LYS A CD 1 ATOM 2071 C CE . LYS A 1 311 ? 31.526 28.903 19.648 1.00 45.14 ? 304 LYS A CE 1 ATOM 2072 N NZ . LYS A 1 311 ? 32.731 28.496 18.865 1.00 54.51 ? 304 LYS A NZ 1 ATOM 2073 N N . LEU A 1 312 ? 29.349 34.683 20.394 1.00 28.11 ? 305 LEU A N 1 ATOM 2074 C CA . LEU A 1 312 ? 28.687 35.787 19.677 1.00 28.23 ? 305 LEU A CA 1 ATOM 2075 C C . LEU A 1 312 ? 29.628 36.935 19.301 1.00 30.23 ? 305 LEU A C 1 ATOM 2076 O O . LEU A 1 312 ? 29.461 37.559 18.246 1.00 30.70 ? 305 LEU A O 1 ATOM 2077 C CB . LEU A 1 312 ? 27.493 36.324 20.477 1.00 27.16 ? 305 LEU A CB 1 ATOM 2078 C CG . LEU A 1 312 ? 26.353 35.321 20.730 1.00 27.47 ? 305 LEU A CG 1 ATOM 2079 C CD1 . LEU A 1 312 ? 25.207 36.010 21.465 1.00 28.85 ? 305 LEU A CD1 1 ATOM 2080 C CD2 . LEU A 1 312 ? 25.870 34.685 19.428 1.00 32.38 ? 305 LEU A CD2 1 ATOM 2081 N N . LEU A 1 313 ? 30.613 37.211 20.154 1.00 28.22 ? 306 LEU A N 1 ATOM 2082 C CA . LEU A 1 313 ? 31.511 38.339 19.937 1.00 28.01 ? 306 LEU A CA 1 ATOM 2083 C C . LEU A 1 313 ? 32.705 38.028 19.055 1.00 29.66 ? 306 LEU A C 1 ATOM 2084 O O . LEU A 1 313 ? 33.265 38.934 18.431 1.00 31.94 ? 306 LEU A O 1 ATOM 2085 C CB . LEU A 1 313 ? 32.038 38.866 21.261 1.00 27.23 ? 306 LEU A CB 1 ATOM 2086 C CG . LEU A 1 313 ? 30.965 39.396 22.219 1.00 26.30 ? 306 LEU A CG 1 ATOM 2087 C CD1 . LEU A 1 313 ? 31.573 39.708 23.582 1.00 29.70 ? 306 LEU A CD1 1 ATOM 2088 C CD2 . LEU A 1 313 ? 30.236 40.608 21.645 1.00 28.27 ? 306 LEU A CD2 1 ATOM 2089 N N . GLU A 1 314 ? 33.124 36.765 19.022 1.00 29.07 ? 307 GLU A N 1 ATOM 2090 C CA . GLU A 1 314 ? 34.409 36.442 18.419 1.00 30.51 ? 307 GLU A CA 1 ATOM 2091 C C . GLU A 1 314 ? 34.472 36.733 16.922 1.00 32.41 ? 307 GLU A C 1 ATOM 2092 O O . GLU A 1 314 ? 35.547 37.025 16.395 1.00 33.08 ? 307 GLU A O 1 ATOM 2093 C CB . GLU A 1 314 ? 34.802 35.006 18.730 1.00 30.50 ? 307 GLU A CB 1 ATOM 2094 C CG . GLU A 1 314 ? 33.908 33.949 18.127 1.00 33.25 ? 307 GLU A CG 1 ATOM 2095 C CD . GLU A 1 314 ? 34.312 32.557 18.563 1.00 37.09 ? 307 GLU A CD 1 ATOM 2096 O OE1 . GLU A 1 314 ? 35.197 32.428 19.442 1.00 37.46 ? 307 GLU A OE1 1 ATOM 2097 O OE2 . GLU A 1 314 ? 33.742 31.590 18.025 1.00 38.41 ? 307 GLU A OE2 1 ATOM 2098 N N . LYS A 1 315 ? 33.325 36.679 16.248 1.00 33.61 ? 308 LYS A N 1 ATOM 2099 C CA . LYS A 1 315 ? 33.281 36.906 14.801 1.00 35.55 ? 308 LYS A CA 1 ATOM 2100 C C . LYS A 1 315 ? 33.016 38.362 14.429 1.00 35.49 ? 308 LYS A C 1 ATOM 2101 O O . LYS A 1 315 ? 32.992 38.703 13.249 1.00 36.91 ? 308 LYS A O 1 ATOM 2102 C CB . LYS A 1 315 ? 32.230 36.009 14.136 1.00 35.92 ? 308 LYS A CB 1 ATOM 2103 C CG . LYS A 1 315 ? 32.625 34.545 14.017 1.00 37.13 ? 308 LYS A CG 1 ATOM 2104 C CD . LYS A 1 315 ? 31.412 33.699 13.682 1.00 36.66 ? 308 LYS A CD 1 ATOM 2105 C CE . LYS A 1 315 ? 31.797 32.248 13.465 1.00 39.81 ? 308 LYS A CE 1 ATOM 2106 N NZ . LYS A 1 315 ? 30.617 31.463 13.014 1.00 41.38 ? 308 LYS A NZ 1 ATOM 2107 N N . MET A 1 316 ? 32.821 39.221 15.428 1.00 34.63 ? 309 MET A N 1 ATOM 2108 C CA . MET A 1 316 ? 32.477 40.628 15.170 1.00 33.33 ? 309 MET A CA 1 ATOM 2109 C C . MET A 1 316 ? 33.505 41.420 14.343 1.00 34.35 ? 309 MET A C 1 ATOM 2110 O O . MET A 1 316 ? 34.711 41.371 14.609 1.00 34.79 ? 309 MET A O 1 ATOM 2111 C CB . MET A 1 316 ? 32.164 41.333 16.477 1.00 30.88 ? 309 MET A CB 1 ATOM 2112 C CG A MET A 1 316 ? 30.854 40.765 17.014 0.50 31.88 ? 309 MET A CG 1 ATOM 2113 C CG B MET A 1 316 ? 30.964 40.817 17.232 0.50 32.94 ? 309 MET A CG 1 ATOM 2114 S SD A MET A 1 316 ? 29.846 41.793 18.077 0.50 28.93 ? 309 MET A SD 1 ATOM 2115 S SD B MET A 1 316 ? 29.511 41.527 16.486 0.50 33.88 ? 309 MET A SD 1 ATOM 2116 C CE A MET A 1 316 ? 29.637 43.277 17.087 0.50 32.16 ? 309 MET A CE 1 ATOM 2117 C CE B MET A 1 316 ? 29.746 43.281 16.797 0.50 35.65 ? 309 MET A CE 1 ATOM 2118 N N . GLY A 1 317 ? 33.000 42.136 13.338 1.00 33.40 ? 310 GLY A N 1 ATOM 2119 C CA . GLY A 1 317 ? 33.824 42.947 12.440 1.00 35.57 ? 310 GLY A CA 1 ATOM 2120 C C . GLY A 1 317 ? 33.463 44.418 12.534 1.00 39.02 ? 310 GLY A C 1 ATOM 2121 O O . GLY A 1 317 ? 33.172 44.921 13.622 1.00 38.94 ? 310 GLY A O 1 ATOM 2122 N N . GLY A 1 318 ? 33.476 45.118 11.398 1.00 38.63 ? 311 GLY A N 1 ATOM 2123 C CA . GLY A 1 318 ? 33.203 46.558 11.399 1.00 38.68 ? 311 GLY A CA 1 ATOM 2124 C C . GLY A 1 318 ? 34.293 47.303 12.150 1.00 38.49 ? 311 GLY A C 1 ATOM 2125 O O . GLY A 1 318 ? 35.462 46.909 12.108 1.00 39.63 ? 311 GLY A O 1 ATOM 2126 N N . SER A 1 319 ? 33.905 48.361 12.859 1.00 35.47 ? 312 SER A N 1 ATOM 2127 C CA . SER A 1 319 ? 34.851 49.259 13.527 1.00 38.36 ? 312 SER A CA 1 ATOM 2128 C C . SER A 1 319 ? 35.496 48.656 14.771 1.00 37.81 ? 312 SER A C 1 ATOM 2129 O O . SER A 1 319 ? 34.853 47.910 15.510 1.00 38.40 ? 312 SER A O 1 ATOM 2130 C CB . SER A 1 319 ? 34.139 50.560 13.914 1.00 42.40 ? 312 SER A CB 1 ATOM 2131 O OG . SER A 1 319 ? 33.664 51.232 12.757 1.00 45.20 ? 312 SER A OG 1 ATOM 2132 N N . ALA A 1 320 ? 36.766 48.990 14.999 1.00 39.33 ? 313 ALA A N 1 ATOM 2133 C CA . ALA A 1 320 ? 37.471 48.607 16.229 1.00 37.74 ? 313 ALA A CA 1 ATOM 2134 C C . ALA A 1 320 ? 36.815 49.279 17.445 1.00 37.29 ? 313 ALA A C 1 ATOM 2135 O O . ALA A 1 320 ? 36.142 50.306 17.278 1.00 37.74 ? 313 ALA A O 1 ATOM 2136 C CB . ALA A 1 320 ? 38.936 49.007 16.126 1.00 38.53 ? 313 ALA A CB 1 ATOM 2137 N N . PRO A 1 321 ? 37.004 48.717 18.671 1.00 34.70 ? 314 PRO A N 1 ATOM 2138 C CA . PRO A 1 321 ? 36.493 49.458 19.844 1.00 35.44 ? 314 PRO A CA 1 ATOM 2139 C C . PRO A 1 321 ? 37.205 50.818 19.905 1.00 35.95 ? 314 PRO A C 1 ATOM 2140 O O . PRO A 1 321 ? 38.382 50.899 19.529 1.00 35.11 ? 314 PRO A O 1 ATOM 2141 C CB . PRO A 1 321 ? 36.887 48.574 21.038 1.00 33.97 ? 314 PRO A CB 1 ATOM 2142 C CG . PRO A 1 321 ? 38.017 47.716 20.538 1.00 33.58 ? 314 PRO A CG 1 ATOM 2143 C CD . PRO A 1 321 ? 37.791 47.526 19.060 1.00 36.56 ? 314 PRO A CD 1 ATOM 2144 N N . PRO A 1 322 ? 36.495 51.879 20.327 1.00 35.55 ? 315 PRO A N 1 ATOM 2145 C CA . PRO A 1 322 ? 37.048 53.246 20.289 1.00 35.29 ? 315 PRO A CA 1 ATOM 2146 C C . PRO A 1 322 ? 38.239 53.459 21.226 1.00 35.92 ? 315 PRO A C 1 ATOM 2147 O O . PRO A 1 322 ? 39.121 54.270 20.929 1.00 38.55 ? 315 PRO A O 1 ATOM 2148 C CB . PRO A 1 322 ? 35.852 54.119 20.711 1.00 33.96 ? 315 PRO A CB 1 ATOM 2149 C CG . PRO A 1 322 ? 34.979 53.200 21.499 1.00 35.06 ? 315 PRO A CG 1 ATOM 2150 C CD . PRO A 1 322 ? 35.106 51.869 20.815 1.00 34.54 ? 315 PRO A CD 1 ATOM 2151 N N . ASP A 1 323 ? 38.262 52.732 22.337 1.00 36.05 ? 316 ASP A N 1 ATOM 2152 C CA . ASP A 1 323 ? 39.357 52.801 23.309 1.00 37.77 ? 316 ASP A CA 1 ATOM 2153 C C . ASP A 1 323 ? 39.282 51.611 24.269 1.00 38.01 ? 316 ASP A C 1 ATOM 2154 O O . ASP A 1 323 ? 38.359 50.796 24.182 1.00 35.51 ? 316 ASP A O 1 ATOM 2155 C CB . ASP A 1 323 ? 39.365 54.151 24.067 1.00 38.15 ? 316 ASP A CB 1 ATOM 2156 C CG . ASP A 1 323 ? 38.110 54.383 24.893 1.00 38.86 ? 316 ASP A CG 1 ATOM 2157 O OD1 . ASP A 1 323 ? 37.837 53.589 25.810 1.00 40.24 ? 316 ASP A OD1 1 ATOM 2158 O OD2 . ASP A 1 323 ? 37.409 55.387 24.653 1.00 41.49 ? 316 ASP A OD2 1 ATOM 2159 N N . SER A 1 324 ? 40.239 51.524 25.191 1.00 37.42 ? 317 SER A N 1 ATOM 2160 C CA . SER A 1 324 ? 40.340 50.369 26.092 1.00 41.10 ? 317 SER A CA 1 ATOM 2161 C C . SER A 1 324 ? 39.158 50.185 27.065 1.00 38.95 ? 317 SER A C 1 ATOM 2162 O O . SER A 1 324 ? 38.912 49.066 27.525 1.00 37.53 ? 317 SER A O 1 ATOM 2163 C CB . SER A 1 324 ? 41.679 50.378 26.843 1.00 42.23 ? 317 SER A CB 1 ATOM 2164 O OG . SER A 1 324 ? 41.685 51.365 27.857 1.00 42.34 ? 317 SER A OG 1 ATOM 2165 N N . SER A 1 325 ? 38.423 51.266 27.357 1.00 37.37 ? 318 SER A N 1 ATOM 2166 C CA . SER A 1 325 ? 37.251 51.218 28.256 1.00 35.58 ? 318 SER A CA 1 ATOM 2167 C C . SER A 1 325 ? 36.063 50.467 27.642 1.00 33.68 ? 318 SER A C 1 ATOM 2168 O O . SER A 1 325 ? 35.062 50.198 28.318 1.00 33.45 ? 318 SER A O 1 ATOM 2169 C CB . SER A 1 325 ? 36.803 52.624 28.659 1.00 35.54 ? 318 SER A CB 1 ATOM 2170 O OG . SER A 1 325 ? 36.115 53.261 27.591 1.00 33.63 ? 318 SER A OG 1 ATOM 2171 N N . TRP A 1 326 ? 36.183 50.150 26.357 1.00 30.24 ? 319 TRP A N 1 ATOM 2172 C CA . TRP A 1 326 ? 35.205 49.341 25.639 1.00 29.04 ? 319 TRP A CA 1 ATOM 2173 C C . TRP A 1 326 ? 35.563 47.867 25.603 1.00 31.35 ? 319 TRP A C 1 ATOM 2174 O O . TRP A 1 326 ? 34.733 47.042 25.216 1.00 29.82 ? 319 TRP A O 1 ATOM 2175 C CB . TRP A 1 326 ? 35.017 49.894 24.223 1.00 32.31 ? 319 TRP A CB 1 ATOM 2176 C CG . TRP A 1 326 ? 34.033 51.042 24.187 1.00 27.41 ? 319 TRP A CG 1 ATOM 2177 C CD1 . TRP A 1 326 ? 34.114 52.263 24.861 1.00 28.09 ? 319 TRP A CD1 1 ATOM 2178 C CD2 . TRP A 1 326 ? 32.763 51.091 23.451 1.00 27.59 ? 319 TRP A CD2 1 ATOM 2179 N NE1 . TRP A 1 326 ? 33.012 53.048 24.593 1.00 29.31 ? 319 TRP A NE1 1 ATOM 2180 C CE2 . TRP A 1 326 ? 32.160 52.401 23.755 1.00 29.97 ? 319 TRP A CE2 1 ATOM 2181 C CE3 . TRP A 1 326 ? 32.093 50.217 22.594 1.00 25.54 ? 319 TRP A CE3 1 ATOM 2182 C CZ2 . TRP A 1 326 ? 30.935 52.788 23.225 1.00 27.21 ? 319 TRP A CZ2 1 ATOM 2183 C CZ3 . TRP A 1 326 ? 30.856 50.618 22.065 1.00 25.44 ? 319 TRP A CZ3 1 ATOM 2184 C CH2 . TRP A 1 326 ? 30.292 51.876 22.378 1.00 27.26 ? 319 TRP A CH2 1 ATOM 2185 N N . ARG A 1 327 ? 36.790 47.525 26.015 1.00 29.55 ? 320 ARG A N 1 ATOM 2186 C CA . ARG A 1 327 ? 37.268 46.130 25.998 1.00 29.96 ? 320 ARG A CA 1 ATOM 2187 C C . ARG A 1 327 ? 37.057 45.446 27.350 1.00 29.13 ? 320 ARG A C 1 ATOM 2188 O O . ARG A 1 327 ? 37.516 45.938 28.381 1.00 31.73 ? 320 ARG A O 1 ATOM 2189 C CB . ARG A 1 327 ? 38.761 46.057 25.631 1.00 31.69 ? 320 ARG A CB 1 ATOM 2190 C CG . ARG A 1 327 ? 39.080 46.268 24.163 1.00 34.19 ? 320 ARG A CG 1 ATOM 2191 C CD . ARG A 1 327 ? 40.537 45.911 23.823 1.00 43.96 ? 320 ARG A CD 1 ATOM 2192 N NE . ARG A 1 327 ? 41.036 46.803 22.791 1.00 58.65 ? 320 ARG A NE 1 ATOM 2193 C CZ . ARG A 1 327 ? 41.768 47.888 23.031 1.00 65.12 ? 320 ARG A CZ 1 ATOM 2194 N NH1 . ARG A 1 327 ? 42.118 48.204 24.274 1.00 67.90 ? 320 ARG A NH1 1 ATOM 2195 N NH2 . ARG A 1 327 ? 42.161 48.654 22.022 1.00 76.50 ? 320 ARG A NH2 1 ATOM 2196 N N . GLY A 1 328 ? 36.363 44.314 27.344 1.00 29.97 ? 321 GLY A N 1 ATOM 2197 C CA . GLY A 1 328 ? 36.306 43.436 28.518 1.00 28.15 ? 321 GLY A CA 1 ATOM 2198 C C . GLY A 1 328 ? 37.496 42.480 28.517 1.00 29.26 ? 321 GLY A C 1 ATOM 2199 O O . GLY A 1 328 ? 38.542 42.772 27.910 1.00 28.88 ? 321 GLY A O 1 ATOM 2200 N N . SER A 1 329 ? 37.332 41.332 29.177 1.00 28.30 ? 322 SER A N 1 ATOM 2201 C CA . SER A 1 329 ? 38.434 40.391 29.443 1.00 29.82 ? 322 SER A CA 1 ATOM 2202 C C . SER A 1 329 ? 38.453 39.157 28.568 1.00 31.07 ? 322 SER A C 1 ATOM 2203 O O . SER A 1 329 ? 39.372 38.339 28.670 1.00 31.84 ? 322 SER A O 1 ATOM 2204 C CB . SER A 1 329 ? 38.378 39.930 30.899 1.00 34.92 ? 322 SER A CB 1 ATOM 2205 O OG . SER A 1 329 ? 38.762 40.986 31.742 1.00 40.48 ? 322 SER A OG 1 ATOM 2206 N N . LEU A 1 330 ? 37.446 38.995 27.720 1.00 29.96 ? 323 LEU A N 1 ATOM 2207 C CA . LEU A 1 330 ? 37.415 37.828 26.842 1.00 29.48 ? 323 LEU A CA 1 ATOM 2208 C C . LEU A 1 330 ? 38.445 37.972 25.725 1.00 30.28 ? 323 LEU A C 1 ATOM 2209 O O . LEU A 1 330 ? 38.863 39.080 25.377 1.00 30.67 ? 323 LEU A O 1 ATOM 2210 C CB . LEU A 1 330 ? 36.014 37.627 26.256 1.00 29.03 ? 323 LEU A CB 1 ATOM 2211 C CG . LEU A 1 330 ? 34.872 37.372 27.236 1.00 27.95 ? 323 LEU A CG 1 ATOM 2212 C CD1 . LEU A 1 330 ? 33.568 37.575 26.495 1.00 28.99 ? 323 LEU A CD1 1 ATOM 2213 C CD2 . LEU A 1 330 ? 34.967 35.965 27.819 1.00 31.42 ? 323 LEU A CD2 1 ATOM 2214 N N . LYS A 1 331 ? 38.861 36.845 25.170 1.00 31.15 ? 324 LYS A N 1 ATOM 2215 C CA . LYS A 1 331 ? 39.852 36.858 24.107 1.00 33.88 ? 324 LYS A CA 1 ATOM 2216 C C . LYS A 1 331 ? 39.155 37.067 22.762 1.00 34.31 ? 324 LYS A C 1 ATOM 2217 O O . LYS A 1 331 ? 39.135 36.181 21.900 1.00 36.61 ? 324 LYS A O 1 ATOM 2218 C CB . LYS A 1 331 ? 40.705 35.584 24.169 1.00 34.80 ? 324 LYS A CB 1 ATOM 2219 C CG . LYS A 1 331 ? 41.408 35.383 25.517 1.00 42.69 ? 324 LYS A CG 1 ATOM 2220 C CD . LYS A 1 331 ? 42.502 36.422 25.786 1.00 46.56 ? 324 LYS A CD 1 ATOM 2221 C CE . LYS A 1 331 ? 43.008 36.360 27.220 0.10 40.52 ? 324 LYS A CE 1 ATOM 2222 N NZ . LYS A 1 331 ? 42.030 36.923 28.193 0.10 39.38 ? 324 LYS A NZ 1 ATOM 2223 N N . VAL A 1 332 ? 38.554 38.252 22.628 1.00 33.18 ? 325 VAL A N 1 ATOM 2224 C CA . VAL A 1 332 ? 37.887 38.708 21.411 1.00 33.09 ? 325 VAL A CA 1 ATOM 2225 C C . VAL A 1 332 ? 38.314 40.163 21.185 1.00 32.83 ? 325 VAL A C 1 ATOM 2226 O O . VAL A 1 332 ? 38.764 40.811 22.125 1.00 30.63 ? 325 VAL A O 1 ATOM 2227 C CB . VAL A 1 332 ? 36.343 38.624 21.527 1.00 32.19 ? 325 VAL A CB 1 ATOM 2228 C CG1 . VAL A 1 332 ? 35.891 37.183 21.751 1.00 31.12 ? 325 VAL A CG1 1 ATOM 2229 C CG2 . VAL A 1 332 ? 35.812 39.536 22.629 1.00 30.76 ? 325 VAL A CG2 1 ATOM 2230 N N . PRO A 1 333 ? 38.171 40.684 19.950 1.00 33.43 ? 326 PRO A N 1 ATOM 2231 C CA . PRO A 1 333 ? 38.625 42.061 19.709 1.00 33.23 ? 326 PRO A CA 1 ATOM 2232 C C . PRO A 1 333 ? 37.729 43.157 20.304 1.00 30.94 ? 326 PRO A C 1 ATOM 2233 O O . PRO A 1 333 ? 38.200 44.284 20.480 1.00 33.39 ? 326 PRO A O 1 ATOM 2234 C CB . PRO A 1 333 ? 38.642 42.166 18.179 1.00 35.15 ? 326 PRO A CB 1 ATOM 2235 C CG . PRO A 1 333 ? 37.646 41.153 17.715 1.00 37.62 ? 326 PRO A CG 1 ATOM 2236 C CD . PRO A 1 333 ? 37.683 40.032 18.717 1.00 35.38 ? 326 PRO A CD 1 ATOM 2237 N N . TYR A 1 334 ? 36.469 42.838 20.612 1.00 31.23 ? 327 TYR A N 1 ATOM 2238 C CA . TYR A 1 334 ? 35.483 43.840 21.058 1.00 30.13 ? 327 TYR A CA 1 ATOM 2239 C C . TYR A 1 334 ? 35.189 44.866 19.956 1.00 31.67 ? 327 TYR A C 1 ATOM 2240 O O . TYR A 1 334 ? 34.950 46.050 20.229 1.00 32.19 ? 327 TYR A O 1 ATOM 2241 C CB . TYR A 1 334 ? 35.900 44.510 22.376 1.00 28.91 ? 327 TYR A CB 1 ATOM 2242 C CG . TYR A 1 334 ? 35.760 43.553 23.528 1.00 28.42 ? 327 TYR A CG 1 ATOM 2243 C CD1 . TYR A 1 334 ? 34.521 43.367 24.159 1.00 26.37 ? 327 TYR A CD1 1 ATOM 2244 C CD2 . TYR A 1 334 ? 36.852 42.791 23.957 1.00 26.78 ? 327 TYR A CD2 1 ATOM 2245 C CE1 . TYR A 1 334 ? 34.382 42.458 25.192 1.00 25.41 ? 327 TYR A CE1 1 ATOM 2246 C CE2 . TYR A 1 334 ? 36.723 41.879 24.988 1.00 25.80 ? 327 TYR A CE2 1 ATOM 2247 C CZ . TYR A 1 334 ? 35.494 41.717 25.600 1.00 26.86 ? 327 TYR A CZ 1 ATOM 2248 O OH . TYR A 1 334 ? 35.375 40.819 26.629 1.00 25.48 ? 327 TYR A OH 1 ATOM 2249 N N . ASN A 1 335 ? 35.224 44.387 18.711 1.00 29.92 ? 328 ASN A N 1 ATOM 2250 C CA . ASN A 1 335 ? 34.798 45.178 17.567 1.00 31.86 ? 328 ASN A CA 1 ATOM 2251 C C . ASN A 1 335 ? 33.348 45.570 17.739 1.00 30.95 ? 328 ASN A C 1 ATOM 2252 O O . ASN A 1 335 ? 32.536 44.801 18.262 1.00 30.68 ? 328 ASN A O 1 ATOM 2253 C CB . ASN A 1 335 ? 34.988 44.406 16.266 1.00 32.61 ? 328 ASN A CB 1 ATOM 2254 C CG . ASN A 1 335 ? 36.446 44.270 15.886 1.00 32.93 ? 328 ASN A CG 1 ATOM 2255 O OD1 . ASN A 1 335 ? 37.269 45.103 16.271 1.00 34.19 ? 328 ASN A OD1 1 ATOM 2256 N ND2 . ASN A 1 335 ? 36.778 43.223 15.125 1.00 31.77 ? 328 ASN A ND2 1 ATOM 2257 N N . VAL A 1 336 ? 33.033 46.786 17.323 1.00 31.70 ? 329 VAL A N 1 ATOM 2258 C CA . VAL A 1 336 ? 31.710 47.336 17.549 1.00 32.51 ? 329 VAL A CA 1 ATOM 2259 C C . VAL A 1 336 ? 30.716 46.829 16.492 1.00 30.04 ? 329 VAL A C 1 ATOM 2260 O O . VAL A 1 336 ? 29.505 46.774 16.731 1.00 30.49 ? 329 VAL A O 1 ATOM 2261 C CB . VAL A 1 336 ? 31.760 48.879 17.616 1.00 34.94 ? 329 VAL A CB 1 ATOM 2262 C CG1 . VAL A 1 336 ? 30.366 49.462 17.510 1.00 37.52 ? 329 VAL A CG1 1 ATOM 2263 C CG2 . VAL A 1 336 ? 32.395 49.323 18.927 1.00 33.08 ? 329 VAL A CG2 1 ATOM 2264 N N . GLY A 1 337 ? 31.227 46.428 15.335 1.00 32.75 ? 330 GLY A N 1 ATOM 2265 C CA . GLY A 1 337 ? 30.359 46.051 14.233 1.00 34.66 ? 330 GLY A CA 1 ATOM 2266 C C . GLY A 1 337 ? 30.065 47.254 13.355 1.00 33.23 ? 330 GLY A C 1 ATOM 2267 O O . GLY A 1 337 ? 30.867 48.187 13.295 1.00 35.90 ? 330 GLY A O 1 ATOM 2268 N N . PRO A 1 338 ? 28.914 47.242 12.662 1.00 36.19 ? 331 PRO A N 1 ATOM 2269 C CA . PRO A 1 338 ? 27.903 46.189 12.723 1.00 36.42 ? 331 PRO A CA 1 ATOM 2270 C C . PRO A 1 338 ? 28.317 44.911 11.982 1.00 34.45 ? 331 PRO A C 1 ATOM 2271 O O . PRO A 1 338 ? 29.074 44.959 10.994 1.00 34.70 ? 331 PRO A O 1 ATOM 2272 C CB . PRO A 1 338 ? 26.704 46.827 12.021 1.00 38.87 ? 331 PRO A CB 1 ATOM 2273 C CG . PRO A 1 338 ? 27.325 47.734 11.008 1.00 41.73 ? 331 PRO A CG 1 ATOM 2274 C CD . PRO A 1 338 ? 28.592 48.253 11.634 1.00 38.82 ? 331 PRO A CD 1 ATOM 2275 N N . GLY A 1 339 ? 27.812 43.776 12.461 1.00 33.23 ? 332 GLY A N 1 ATOM 2276 C CA . GLY A 1 339 ? 27.981 42.498 11.762 1.00 37.02 ? 332 GLY A CA 1 ATOM 2277 C C . GLY A 1 339 ? 29.316 41.815 11.985 1.00 39.12 ? 332 GLY A C 1 ATOM 2278 O O . GLY A 1 339 ? 30.139 42.282 12.777 1.00 36.46 ? 332 GLY A O 1 ATOM 2279 N N . PHE A 1 340 ? 29.524 40.713 11.263 1.00 36.27 ? 333 PHE A N 1 ATOM 2280 C CA . PHE A 1 340 ? 30.693 39.845 11.444 1.00 39.39 ? 333 PHE A CA 1 ATOM 2281 C C . PHE A 1 340 ? 31.777 40.144 10.392 1.00 41.51 ? 333 PHE A C 1 ATOM 2282 O O . PHE A 1 340 ? 31.491 40.793 9.379 1.00 41.59 ? 333 PHE A O 1 ATOM 2283 C CB . PHE A 1 340 ? 30.283 38.359 11.375 1.00 36.58 ? 333 PHE A CB 1 ATOM 2284 C CG . PHE A 1 340 ? 29.399 37.887 12.516 1.00 35.36 ? 333 PHE A CG 1 ATOM 2285 C CD1 . PHE A 1 340 ? 28.399 36.948 12.277 1.00 34.49 ? 333 PHE A CD1 1 ATOM 2286 C CD2 . PHE A 1 340 ? 29.573 38.352 13.824 1.00 33.89 ? 333 PHE A CD2 1 ATOM 2287 C CE1 . PHE A 1 340 ? 27.591 36.485 13.305 1.00 38.05 ? 333 PHE A CE1 1 ATOM 2288 C CE2 . PHE A 1 340 ? 28.759 37.893 14.863 1.00 31.50 ? 333 PHE A CE2 1 ATOM 2289 C CZ . PHE A 1 340 ? 27.766 36.959 14.600 1.00 35.63 ? 333 PHE A CZ 1 ATOM 2290 N N . THR A 1 341 ? 33.010 39.683 10.629 1.00 40.43 ? 334 THR A N 1 ATOM 2291 C CA . THR A 1 341 ? 34.113 39.841 9.644 1.00 44.46 ? 334 THR A CA 1 ATOM 2292 C C . THR A 1 341 ? 33.847 39.098 8.327 1.00 48.45 ? 334 THR A C 1 ATOM 2293 O O . THR A 1 341 ? 33.008 38.197 8.272 1.00 52.29 ? 334 THR A O 1 ATOM 2294 C CB . THR A 1 341 ? 35.486 39.374 10.189 1.00 47.37 ? 334 THR A CB 1 ATOM 2295 O OG1 . THR A 1 341 ? 35.388 38.028 10.673 1.00 50.68 ? 334 THR A OG1 1 ATOM 2296 C CG2 . THR A 1 341 ? 35.992 40.285 11.295 1.00 47.02 ? 334 THR A CG2 1 ATOM 2297 N N . GLY A 1 342 ? 34.588 39.479 7.286 1.00 48.30 ? 335 GLY A N 1 ATOM 2298 C CA . GLY A 1 342 ? 34.429 38.961 5.920 1.00 52.70 ? 335 GLY A CA 1 ATOM 2299 C C . GLY A 1 342 ? 33.891 37.556 5.700 1.00 51.17 ? 335 GLY A C 1 ATOM 2300 O O . GLY A 1 342 ? 32.853 37.388 5.056 1.00 56.61 ? 335 GLY A O 1 ATOM 2301 N N . ASN A 1 343 ? 34.598 36.549 6.218 1.00 52.38 ? 336 ASN A N 1 ATOM 2302 C CA . ASN A 1 343 ? 34.217 35.135 6.047 1.00 55.01 ? 336 ASN A CA 1 ATOM 2303 C C . ASN A 1 343 ? 32.820 34.800 6.583 1.00 47.62 ? 336 ASN A C 1 ATOM 2304 O O . ASN A 1 343 ? 32.146 33.905 6.076 1.00 50.94 ? 336 ASN A O 1 ATOM 2305 C CB . ASN A 1 343 ? 35.248 34.205 6.713 1.00 58.40 ? 336 ASN A CB 1 ATOM 2306 C CG . ASN A 1 343 ? 36.588 34.177 5.988 1.00 65.94 ? 336 ASN A CG 1 ATOM 2307 O OD1 . ASN A 1 343 ? 36.805 34.890 5.003 1.00 73.46 ? 336 ASN A OD1 1 ATOM 2308 N ND2 . ASN A 1 343 ? 37.500 33.338 6.477 1.00 81.44 ? 336 ASN A ND2 1 ATOM 2309 N N . PHE A 1 344 ? 32.394 35.530 7.608 1.00 47.12 ? 337 PHE A N 1 ATOM 2310 C CA . PHE A 1 344 ? 31.151 35.223 8.294 1.00 44.00 ? 337 PHE A CA 1 ATOM 2311 C C . PHE A 1 344 ? 30.094 36.306 8.083 1.00 44.96 ? 337 PHE A C 1 ATOM 2312 O O . PHE A 1 344 ? 29.060 36.298 8.747 1.00 43.08 ? 337 PHE A O 1 ATOM 2313 C CB . PHE A 1 344 ? 31.422 35.025 9.793 1.00 44.57 ? 337 PHE A CB 1 ATOM 2314 C CG . PHE A 1 344 ? 32.621 34.155 10.086 1.00 44.74 ? 337 PHE A CG 1 ATOM 2315 C CD1 . PHE A 1 344 ? 33.818 34.722 10.520 1.00 47.36 ? 337 PHE A CD1 1 ATOM 2316 C CD2 . PHE A 1 344 ? 32.554 32.771 9.936 1.00 46.39 ? 337 PHE A CD2 1 ATOM 2317 C CE1 . PHE A 1 344 ? 34.921 33.928 10.796 1.00 48.56 ? 337 PHE A CE1 1 ATOM 2318 C CE2 . PHE A 1 344 ? 33.657 31.971 10.207 1.00 48.53 ? 337 PHE A CE2 1 ATOM 2319 C CZ . PHE A 1 344 ? 34.842 32.552 10.637 1.00 49.74 ? 337 PHE A CZ 1 ATOM 2320 N N . SER A 1 345 ? 30.343 37.215 7.142 1.00 42.77 ? 338 SER A N 1 ATOM 2321 C CA . SER A 1 345 ? 29.494 38.393 6.948 1.00 45.25 ? 338 SER A CA 1 ATOM 2322 C C . SER A 1 345 ? 28.047 38.083 6.551 1.00 47.66 ? 338 SER A C 1 ATOM 2323 O O . SER A 1 345 ? 27.166 38.925 6.741 1.00 49.34 ? 338 SER A O 1 ATOM 2324 C CB . SER A 1 345 ? 30.123 39.360 5.940 1.00 48.04 ? 338 SER A CB 1 ATOM 2325 O OG . SER A 1 345 ? 29.948 38.896 4.614 1.00 50.83 ? 338 SER A OG 1 ATOM 2326 N N . THR A 1 346 ? 27.798 36.891 6.011 1.00 44.01 ? 339 THR A N 1 ATOM 2327 C CA . THR A 1 346 ? 26.434 36.501 5.617 1.00 44.52 ? 339 THR A CA 1 ATOM 2328 C C . THR A 1 346 ? 25.674 35.793 6.741 1.00 44.35 ? 339 THR A C 1 ATOM 2329 O O . THR A 1 346 ? 24.469 35.540 6.630 1.00 42.96 ? 339 THR A O 1 ATOM 2330 C CB . THR A 1 346 ? 26.414 35.626 4.345 1.00 44.37 ? 339 THR A CB 1 ATOM 2331 O OG1 . THR A 1 346 ? 27.097 34.393 4.601 1.00 49.10 ? 339 THR A OG1 1 ATOM 2332 C CG2 . THR A 1 346 ? 27.060 36.353 3.181 1.00 49.28 ? 339 THR A CG2 1 ATOM 2333 N N . GLN A 1 347 ? 26.383 35.477 7.822 1.00 42.20 ? 340 GLN A N 1 ATOM 2334 C CA . GLN A 1 347 ? 25.743 34.958 9.027 1.00 39.15 ? 340 GLN A CA 1 ATOM 2335 C C . GLN A 1 347 ? 25.061 36.069 9.799 1.00 40.21 ? 340 GLN A C 1 ATOM 2336 O O . GLN A 1 347 ? 25.475 37.233 9.731 1.00 39.43 ? 340 GLN A O 1 ATOM 2337 C CB . GLN A 1 347 ? 26.759 34.242 9.910 1.00 36.19 ? 340 GLN A CB 1 ATOM 2338 C CG . GLN A 1 347 ? 27.281 32.986 9.237 1.00 40.37 ? 340 GLN A CG 1 ATOM 2339 C CD . GLN A 1 347 ? 28.411 32.292 9.972 1.00 41.36 ? 340 GLN A CD 1 ATOM 2340 O OE1 . GLN A 1 347 ? 28.886 32.740 11.013 1.00 41.35 ? 340 GLN A OE1 1 ATOM 2341 N NE2 . GLN A 1 347 ? 28.857 31.173 9.406 1.00 41.93 ? 340 GLN A NE2 1 ATOM 2342 N N . LYS A 1 348 ? 24.003 35.705 10.525 1.00 37.24 ? 341 LYS A N 1 ATOM 2343 C CA . LYS A 1 348 ? 23.272 36.659 11.346 1.00 35.28 ? 341 LYS A CA 1 ATOM 2344 C C . LYS A 1 348 ? 23.009 36.085 12.743 1.00 36.44 ? 341 LYS A C 1 ATOM 2345 O O . LYS A 1 348 ? 23.276 34.914 13.014 1.00 35.48 ? 341 LYS A O 1 ATOM 2346 C CB . LYS A 1 348 ? 21.952 37.093 10.677 1.00 38.79 ? 341 LYS A CB 1 ATOM 2347 C CG . LYS A 1 348 ? 22.055 37.400 9.193 1.00 44.56 ? 341 LYS A CG 1 ATOM 2348 C CD . LYS A 1 348 ? 21.580 38.797 8.834 1.00 49.47 ? 341 LYS A CD 1 ATOM 2349 C CE . LYS A 1 348 ? 22.162 39.200 7.481 0.90 53.06 ? 341 LYS A CE 1 ATOM 2350 N NZ . LYS A 1 348 ? 21.927 40.631 7.144 0.90 56.87 ? 341 LYS A NZ 1 ATOM 2351 N N . VAL A 1 349 ? 22.503 36.930 13.629 1.00 32.93 ? 342 VAL A N 1 ATOM 2352 C CA . VAL A 1 349 ? 22.114 36.497 14.966 1.00 32.30 ? 342 VAL A CA 1 ATOM 2353 C C . VAL A 1 349 ? 20.591 36.509 15.037 1.00 31.89 ? 342 VAL A C 1 ATOM 2354 O O . VAL A 1 349 ? 19.952 37.427 14.523 1.00 32.77 ? 342 VAL A O 1 ATOM 2355 C CB . VAL A 1 349 ? 22.776 37.371 16.057 1.00 29.37 ? 342 VAL A CB 1 ATOM 2356 C CG1 . VAL A 1 349 ? 22.155 37.121 17.431 1.00 29.49 ? 342 VAL A CG1 1 ATOM 2357 C CG2 . VAL A 1 349 ? 24.281 37.102 16.061 1.00 30.54 ? 342 VAL A CG2 1 ATOM 2358 N N . LYS A 1 350 ? 20.020 35.468 15.638 1.00 29.78 ? 343 LYS A N 1 ATOM 2359 C CA . LYS A 1 350 ? 18.573 35.343 15.735 1.00 29.59 ? 343 LYS A CA 1 ATOM 2360 C C . LYS A 1 350 ? 18.188 35.071 17.174 1.00 27.93 ? 343 LYS A C 1 ATOM 2361 O O . LYS A 1 350 ? 18.726 34.158 17.802 1.00 27.31 ? 343 LYS A O 1 ATOM 2362 C CB . LYS A 1 350 ? 18.051 34.221 14.818 1.00 30.71 ? 343 LYS A CB 1 ATOM 2363 C CG . LYS A 1 350 ? 16.535 34.040 14.866 1.00 29.68 ? 343 LYS A CG 1 ATOM 2364 C CD . LYS A 1 350 ? 16.060 33.011 13.846 1.00 35.18 ? 343 LYS A CD 1 ATOM 2365 C CE . LYS A 1 350 ? 14.542 33.027 13.754 1.00 37.63 ? 343 LYS A CE 1 ATOM 2366 N NZ . LYS A 1 350 ? 14.037 32.137 12.673 1.00 45.64 ? 343 LYS A NZ 1 ATOM 2367 N N . MET A 1 351 ? 17.268 35.877 17.697 1.00 26.62 ? 344 MET A N 1 ATOM 2368 C CA . MET A 1 351 ? 16.741 35.674 19.043 1.00 25.83 ? 344 MET A CA 1 ATOM 2369 C C . MET A 1 351 ? 15.445 34.867 18.939 1.00 28.27 ? 344 MET A C 1 ATOM 2370 O O . MET A 1 351 ? 14.754 34.946 17.925 1.00 28.92 ? 344 MET A O 1 ATOM 2371 C CB . MET A 1 351 ? 16.463 37.025 19.707 1.00 25.74 ? 344 MET A CB 1 ATOM 2372 C CG . MET A 1 351 ? 17.700 37.905 19.834 1.00 25.53 ? 344 MET A CG 1 ATOM 2373 S SD . MET A 1 351 ? 17.339 39.472 20.652 1.00 25.67 ? 344 MET A SD 1 ATOM 2374 C CE . MET A 1 351 ? 17.134 38.892 22.341 1.00 26.13 ? 344 MET A CE 1 ATOM 2375 N N . HIS A 1 352 ? 15.136 34.083 19.967 1.00 27.40 ? 345 HIS A N 1 ATOM 2376 C CA . HIS A 1 352 ? 13.851 33.386 20.061 1.00 26.88 ? 345 HIS A CA 1 ATOM 2377 C C . HIS A 1 352 ? 13.327 33.593 21.452 1.00 25.70 ? 345 HIS A C 1 ATOM 2378 O O . HIS A 1 352 ? 13.766 32.919 22.399 1.00 25.44 ? 345 HIS A O 1 ATOM 2379 C CB . HIS A 1 352 ? 13.983 31.882 19.805 1.00 26.63 ? 345 HIS A CB 1 ATOM 2380 C CG . HIS A 1 352 ? 14.912 31.509 18.673 1.00 30.62 ? 345 HIS A CG 1 ATOM 2381 N ND1 . HIS A 1 352 ? 16.256 31.580 18.779 1.00 30.24 ? 345 HIS A ND1 1 ATOM 2382 C CD2 . HIS A 1 352 ? 14.646 30.990 17.411 1.00 32.22 ? 345 HIS A CD2 1 ATOM 2383 C CE1 . HIS A 1 352 ? 16.823 31.162 17.629 1.00 32.27 ? 345 HIS A CE1 1 ATOM 2384 N NE2 . HIS A 1 352 ? 15.836 30.799 16.791 1.00 36.59 ? 345 HIS A NE2 1 ATOM 2385 N N . ILE A 1 353 ? 12.399 34.535 21.606 1.00 23.93 ? 346 ILE A N 1 ATOM 2386 C CA . ILE A 1 353 ? 11.849 34.855 22.926 1.00 24.30 ? 346 ILE A CA 1 ATOM 2387 C C . ILE A 1 353 ? 10.351 34.575 22.943 1.00 24.61 ? 346 ILE A C 1 ATOM 2388 O O . ILE A 1 353 ? 9.602 35.091 22.106 1.00 26.42 ? 346 ILE A O 1 ATOM 2389 C CB . ILE A 1 353 ? 12.143 36.317 23.346 1.00 24.02 ? 346 ILE A CB 1 ATOM 2390 C CG1 . ILE A 1 353 ? 13.631 36.672 23.153 1.00 24.62 ? 346 ILE A CG1 1 ATOM 2391 C CG2 . ILE A 1 353 ? 11.660 36.587 24.775 1.00 24.76 ? 346 ILE A CG2 1 ATOM 2392 C CD1 . ILE A 1 353 ? 14.625 35.816 23.927 1.00 25.79 ? 346 ILE A CD1 1 ATOM 2393 N N . HIS A 1 354 ? 9.928 33.766 23.912 1.00 24.04 ? 347 HIS A N 1 ATOM 2394 C CA . HIS A 1 354 ? 8.542 33.282 23.986 1.00 23.09 ? 347 HIS A CA 1 ATOM 2395 C C . HIS A 1 354 ? 7.920 33.458 25.357 1.00 22.43 ? 347 HIS A C 1 ATOM 2396 O O . HIS A 1 354 ? 6.845 32.912 25.648 1.00 23.47 ? 347 HIS A O 1 ATOM 2397 C CB . HIS A 1 354 ? 8.504 31.822 23.565 1.00 26.14 ? 347 HIS A CB 1 ATOM 2398 C CG . HIS A 1 354 ? 9.138 31.574 22.223 1.00 32.35 ? 347 HIS A CG 1 ATOM 2399 N ND1 . HIS A 1 354 ? 10.299 30.897 22.076 1.00 36.00 ? 347 HIS A ND1 1 ATOM 2400 C CD2 . HIS A 1 354 ? 8.759 31.985 20.951 1.00 35.44 ? 347 HIS A CD2 1 ATOM 2401 C CE1 . HIS A 1 354 ? 10.627 30.854 20.775 1.00 38.13 ? 347 HIS A CE1 1 ATOM 2402 N NE2 . HIS A 1 354 ? 9.684 31.518 20.085 1.00 41.90 ? 347 HIS A NE2 1 ATOM 2403 N N . SER A 1 355 ? 8.590 34.238 26.205 1.00 21.95 ? 348 SER A N 1 ATOM 2404 C CA . SER A 1 355 ? 8.081 34.571 27.536 1.00 19.54 ? 348 SER A CA 1 ATOM 2405 C C . SER A 1 355 ? 6.705 35.227 27.458 1.00 21.39 ? 348 SER A C 1 ATOM 2406 O O . SER A 1 355 ? 6.373 35.867 26.460 1.00 21.47 ? 348 SER A O 1 ATOM 2407 C CB . SER A 1 355 ? 9.049 35.532 28.243 1.00 19.67 ? 348 SER A CB 1 ATOM 2408 O OG . SER A 1 355 ? 10.344 34.948 28.313 1.00 21.32 ? 348 SER A OG 1 ATOM 2409 N N . THR A 1 356 ? 5.917 35.087 28.520 1.00 21.64 ? 349 THR A N 1 ATOM 2410 C CA . THR A 1 356 ? 4.584 35.697 28.557 1.00 21.56 ? 349 THR A CA 1 ATOM 2411 C C . THR A 1 356 ? 4.388 36.518 29.811 1.00 21.21 ? 349 THR A C 1 ATOM 2412 O O . THR A 1 356 ? 4.882 36.171 30.887 1.00 24.27 ? 349 THR A O 1 ATOM 2413 C CB . THR A 1 356 ? 3.473 34.642 28.512 1.00 24.98 ? 349 THR A CB 1 ATOM 2414 O OG1 . THR A 1 356 ? 3.617 33.777 29.639 1.00 28.20 ? 349 THR A OG1 1 ATOM 2415 C CG2 . THR A 1 356 ? 3.601 33.819 27.261 1.00 22.66 ? 349 THR A CG2 1 ATOM 2416 N N . ASN A 1 357 ? 3.675 37.619 29.661 1.00 20.70 ? 350 ASN A N 1 ATOM 2417 C CA . ASN A 1 357 ? 3.283 38.448 30.794 1.00 19.65 ? 350 ASN A CA 1 ATOM 2418 C C . ASN A 1 357 ? 1.944 37.915 31.275 1.00 20.77 ? 350 ASN A C 1 ATOM 2419 O O . ASN A 1 357 ? 1.048 37.641 30.457 1.00 23.26 ? 350 ASN A O 1 ATOM 2420 C CB . ASN A 1 357 ? 3.155 39.904 30.343 1.00 22.89 ? 350 ASN A CB 1 ATOM 2421 C CG . ASN A 1 357 ? 4.478 40.477 29.849 1.00 23.10 ? 350 ASN A CG 1 ATOM 2422 O OD1 . ASN A 1 357 ? 5.562 40.115 30.336 1.00 24.37 ? 350 ASN A OD1 1 ATOM 2423 N ND2 . ASN A 1 357 ? 4.400 41.395 28.891 1.00 27.40 ? 350 ASN A ND2 1 ATOM 2424 N N A GLU A 1 358 ? 1.816 37.775 32.591 0.60 20.51 ? 351 GLU A N 1 ATOM 2425 N N B GLU A 1 358 ? 1.798 37.716 32.579 0.40 20.94 ? 351 GLU A N 1 ATOM 2426 C CA A GLU A 1 358 ? 0.661 37.123 33.220 0.60 22.36 ? 351 GLU A CA 1 ATOM 2427 C CA B GLU A 1 358 ? 0.563 37.141 33.128 0.40 21.24 ? 351 GLU A CA 1 ATOM 2428 C C A GLU A 1 358 ? 0.296 37.874 34.490 0.60 20.37 ? 351 GLU A C 1 ATOM 2429 C C B GLU A 1 358 ? 0.262 37.784 34.468 0.40 19.81 ? 351 GLU A C 1 ATOM 2430 O O A GLU A 1 358 ? 1.155 38.083 35.346 0.60 19.21 ? 351 GLU A O 1 ATOM 2431 O O B GLU A 1 358 ? 1.130 37.833 35.337 0.40 19.06 ? 351 GLU A O 1 ATOM 2432 C CB A GLU A 1 358 ? 1.010 35.684 33.641 0.60 25.46 ? 351 GLU A CB 1 ATOM 2433 C CB B GLU A 1 358 ? 0.707 35.628 33.352 0.40 25.09 ? 351 GLU A CB 1 ATOM 2434 C CG A GLU A 1 358 ? 1.725 34.813 32.627 0.60 30.79 ? 351 GLU A CG 1 ATOM 2435 C CG B GLU A 1 358 ? 1.386 34.841 32.242 0.40 28.31 ? 351 GLU A CG 1 ATOM 2436 C CD A GLU A 1 358 ? 1.465 33.341 32.860 0.60 33.44 ? 351 GLU A CD 1 ATOM 2437 C CD B GLU A 1 358 ? 0.406 34.277 31.240 0.40 27.50 ? 351 GLU A CD 1 ATOM 2438 O OE1 A GLU A 1 358 ? 1.099 32.653 31.891 0.60 42.64 ? 351 GLU A OE1 1 ATOM 2439 O OE1 B GLU A 1 358 ? -0.816 34.441 31.450 0.40 33.81 ? 351 GLU A OE1 1 ATOM 2440 O OE2 A GLU A 1 358 ? 1.603 32.869 34.007 0.60 31.82 ? 351 GLU A OE2 1 ATOM 2441 O OE2 B GLU A 1 358 ? 0.861 33.659 30.248 0.40 30.57 ? 351 GLU A OE2 1 ATOM 2442 N N . VAL A 1 359 ? -0.966 38.266 34.633 1.00 20.84 ? 352 VAL A N 1 ATOM 2443 C CA . VAL A 1 359 ? -1.422 38.804 35.917 1.00 18.48 ? 352 VAL A CA 1 ATOM 2444 C C . VAL A 1 359 ? -1.448 37.632 36.911 1.00 17.50 ? 352 VAL A C 1 ATOM 2445 O O . VAL A 1 359 ? -2.081 36.578 36.662 1.00 19.14 ? 352 VAL A O 1 ATOM 2446 C CB . VAL A 1 359 ? -2.805 39.489 35.815 1.00 17.51 ? 352 VAL A CB 1 ATOM 2447 C CG1 . VAL A 1 359 ? -3.304 39.936 37.181 1.00 19.24 ? 352 VAL A CG1 1 ATOM 2448 C CG2 . VAL A 1 359 ? -2.712 40.714 34.933 1.00 20.16 ? 352 VAL A CG2 1 ATOM 2449 N N . THR A 1 360 ? -0.775 37.826 38.039 1.00 17.09 ? 353 THR A N 1 ATOM 2450 C CA . THR A 1 360 ? -0.492 36.739 38.995 1.00 17.33 ? 353 THR A CA 1 ATOM 2451 C C . THR A 1 360 ? -0.618 37.281 40.410 1.00 17.49 ? 353 THR A C 1 ATOM 2452 O O . THR A 1 360 ? -0.262 38.449 40.661 1.00 17.93 ? 353 THR A O 1 ATOM 2453 C CB . THR A 1 360 ? 0.935 36.208 38.776 1.00 18.55 ? 353 THR A CB 1 ATOM 2454 O OG1 . THR A 1 360 ? 1.110 35.890 37.387 1.00 19.64 ? 353 THR A OG1 1 ATOM 2455 C CG2 . THR A 1 360 ? 1.206 34.968 39.615 1.00 17.88 ? 353 THR A CG2 1 ATOM 2456 N N . ARG A 1 361 ? -1.104 36.439 41.336 1.00 17.43 ? 354 ARG A N 1 ATOM 2457 C CA . ARG A 1 361 ? -1.258 36.881 42.735 1.00 16.67 ? 354 ARG A CA 1 ATOM 2458 C C . ARG A 1 361 ? 0.079 36.861 43.474 1.00 16.68 ? 354 ARG A C 1 ATOM 2459 O O . ARG A 1 361 ? 0.868 35.910 43.337 1.00 19.00 ? 354 ARG A O 1 ATOM 2460 C CB . ARG A 1 361 ? -2.278 36.009 43.481 1.00 17.51 ? 354 ARG A CB 1 ATOM 2461 C CG . ARG A 1 361 ? -2.618 36.550 44.876 1.00 18.50 ? 354 ARG A CG 1 ATOM 2462 C CD . ARG A 1 361 ? -4.008 36.104 45.293 1.00 19.23 ? 354 ARG A CD 1 ATOM 2463 N NE . ARG A 1 361 ? -5.026 36.850 44.547 1.00 20.49 ? 354 ARG A NE 1 ATOM 2464 C CZ . ARG A 1 361 ? -6.322 36.806 44.793 1.00 21.38 ? 354 ARG A CZ 1 ATOM 2465 N NH1 . ARG A 1 361 ? -6.807 36.006 45.755 1.00 22.37 ? 354 ARG A NH1 1 ATOM 2466 N NH2 . ARG A 1 361 ? -7.141 37.561 44.062 1.00 25.04 ? 354 ARG A NH2 1 ATOM 2467 N N . ILE A 1 362 ? 0.311 37.899 44.272 1.00 15.07 ? 355 ILE A N 1 ATOM 2468 C CA . ILE A 1 362 ? 1.527 38.023 45.081 1.00 15.13 ? 355 ILE A CA 1 ATOM 2469 C C . ILE A 1 362 ? 1.072 38.315 46.515 1.00 16.15 ? 355 ILE A C 1 ATOM 2470 O O . ILE A 1 362 ? -0.066 38.781 46.710 1.00 16.91 ? 355 ILE A O 1 ATOM 2471 C CB . ILE A 1 362 ? 2.456 39.149 44.539 1.00 14.23 ? 355 ILE A CB 1 ATOM 2472 C CG1 . ILE A 1 362 ? 1.762 40.518 44.559 1.00 14.10 ? 355 ILE A CG1 1 ATOM 2473 C CG2 . ILE A 1 362 ? 2.910 38.790 43.113 1.00 15.71 ? 355 ILE A CG2 1 ATOM 2474 C CD1 . ILE A 1 362 ? 2.741 41.688 44.493 1.00 16.34 ? 355 ILE A CD1 1 ATOM 2475 N N . TYR A 1 363 ? 1.944 38.061 47.496 1.00 15.30 ? 356 TYR A N 1 ATOM 2476 C CA . TYR A 1 363 ? 1.550 38.111 48.908 1.00 15.59 ? 356 TYR A CA 1 ATOM 2477 C C . TYR A 1 363 ? 2.623 38.795 49.734 1.00 14.83 ? 356 TYR A C 1 ATOM 2478 O O . TYR A 1 363 ? 3.753 38.285 49.852 1.00 16.99 ? 356 TYR A O 1 ATOM 2479 C CB . TYR A 1 363 ? 1.387 36.690 49.457 1.00 15.66 ? 356 TYR A CB 1 ATOM 2480 C CG . TYR A 1 363 ? 0.348 35.859 48.758 1.00 17.61 ? 356 TYR A CG 1 ATOM 2481 C CD1 . TYR A 1 363 ? -0.964 35.846 49.217 1.00 19.54 ? 356 TYR A CD1 1 ATOM 2482 C CD2 . TYR A 1 363 ? 0.678 35.089 47.625 1.00 18.08 ? 356 TYR A CD2 1 ATOM 2483 C CE1 . TYR A 1 363 ? -1.936 35.083 48.581 1.00 20.27 ? 356 TYR A CE1 1 ATOM 2484 C CE2 . TYR A 1 363 ? -0.283 34.322 46.982 1.00 19.85 ? 356 TYR A CE2 1 ATOM 2485 C CZ . TYR A 1 363 ? -1.590 34.324 47.469 1.00 20.76 ? 356 TYR A CZ 1 ATOM 2486 O OH . TYR A 1 363 ? -2.570 33.591 46.834 1.00 22.76 ? 356 TYR A OH 1 ATOM 2487 N N . ASN A 1 364 ? 2.283 39.923 50.340 1.00 14.86 ? 357 ASN A N 1 ATOM 2488 C CA . ASN A 1 364 ? 3.179 40.536 51.347 1.00 16.61 ? 357 ASN A CA 1 ATOM 2489 C C . ASN A 1 364 ? 2.812 40.015 52.720 1.00 17.27 ? 357 ASN A C 1 ATOM 2490 O O . ASN A 1 364 ? 1.616 39.822 52.994 1.00 20.81 ? 357 ASN A O 1 ATOM 2491 C CB . ASN A 1 364 ? 3.007 42.061 51.386 1.00 15.79 ? 357 ASN A CB 1 ATOM 2492 C CG . ASN A 1 364 ? 3.357 42.744 50.079 1.00 15.97 ? 357 ASN A CG 1 ATOM 2493 O OD1 . ASN A 1 364 ? 4.240 42.309 49.324 1.00 15.87 ? 357 ASN A OD1 1 ATOM 2494 N ND2 . ASN A 1 364 ? 2.685 43.864 49.823 1.00 17.95 ? 357 ASN A ND2 1 ATOM 2495 N N . VAL A 1 365 ? 3.787 39.810 53.606 1.00 16.99 ? 358 VAL A N 1 ATOM 2496 C CA . VAL A 1 365 ? 3.422 39.532 55.013 1.00 16.65 ? 358 VAL A CA 1 ATOM 2497 C C . VAL A 1 365 ? 3.630 40.846 55.771 1.00 17.48 ? 358 VAL A C 1 ATOM 2498 O O . VAL A 1 365 ? 4.683 41.461 55.650 1.00 18.28 ? 358 VAL A O 1 ATOM 2499 C CB . VAL A 1 365 ? 4.274 38.423 55.658 1.00 15.64 ? 358 VAL A CB 1 ATOM 2500 C CG1 . VAL A 1 365 ? 3.699 38.044 57.038 1.00 16.97 ? 358 VAL A CG1 1 ATOM 2501 C CG2 . VAL A 1 365 ? 4.329 37.191 54.747 1.00 19.51 ? 358 VAL A CG2 1 ATOM 2502 N N . ILE A 1 366 ? 2.623 41.276 56.522 1.00 17.40 ? 359 ILE A N 1 ATOM 2503 C CA . ILE A 1 366 ? 2.689 42.544 57.281 1.00 17.86 ? 359 ILE A CA 1 ATOM 2504 C C . ILE A 1 366 ? 2.461 42.257 58.761 1.00 17.78 ? 359 ILE A C 1 ATOM 2505 O O . ILE A 1 366 ? 1.376 41.793 59.137 1.00 19.81 ? 359 ILE A O 1 ATOM 2506 C CB . ILE A 1 366 ? 1.620 43.563 56.792 1.00 17.30 ? 359 ILE A CB 1 ATOM 2507 C CG1 . ILE A 1 366 ? 1.654 43.744 55.252 1.00 17.86 ? 359 ILE A CG1 1 ATOM 2508 C CG2 . ILE A 1 366 ? 1.768 44.892 57.563 1.00 20.12 ? 359 ILE A CG2 1 ATOM 2509 C CD1 . ILE A 1 366 ? 2.913 44.400 54.728 1.00 19.11 ? 359 ILE A CD1 1 ATOM 2510 N N . GLY A 1 367 ? 3.493 42.491 59.583 1.00 18.87 ? 360 GLY A N 1 ATOM 2511 C CA . GLY A 1 367 ? 3.452 42.201 61.032 1.00 18.63 ? 360 GLY A CA 1 ATOM 2512 C C . GLY A 1 367 ? 3.386 43.525 61.767 1.00 18.02 ? 360 GLY A C 1 ATOM 2513 O O . GLY A 1 367 ? 4.035 44.484 61.350 1.00 20.29 ? 360 GLY A O 1 ATOM 2514 N N . THR A 1 368 ? 2.605 43.595 62.851 1.00 19.08 ? 361 THR A N 1 ATOM 2515 C CA . THR A 1 368 ? 2.456 44.850 63.619 1.00 19.38 ? 361 THR A CA 1 ATOM 2516 C C . THR A 1 368 ? 2.870 44.611 65.057 1.00 20.86 ? 361 THR A C 1 ATOM 2517 O O . THR A 1 368 ? 2.420 43.643 65.682 1.00 22.35 ? 361 THR A O 1 ATOM 2518 C CB . THR A 1 368 ? 0.990 45.347 63.585 1.00 21.26 ? 361 THR A CB 1 ATOM 2519 O OG1 . THR A 1 368 ? 0.608 45.578 62.225 1.00 22.83 ? 361 THR A OG1 1 ATOM 2520 C CG2 . THR A 1 368 ? 0.774 46.655 64.358 1.00 22.99 ? 361 THR A CG2 1 ATOM 2521 N N . LEU A 1 369 ? 3.709 45.501 65.586 1.00 20.62 ? 362 LEU A N 1 ATOM 2522 C CA . LEU A 1 369 ? 3.997 45.537 67.023 1.00 19.17 ? 362 LEU A CA 1 ATOM 2523 C C . LEU A 1 369 ? 3.507 46.906 67.489 1.00 20.46 ? 362 LEU A C 1 ATOM 2524 O O . LEU A 1 369 ? 4.181 47.911 67.254 1.00 21.39 ? 362 LEU A O 1 ATOM 2525 C CB . LEU A 1 369 ? 5.518 45.362 67.256 1.00 21.58 ? 362 LEU A CB 1 ATOM 2526 C CG . LEU A 1 369 ? 5.984 45.340 68.717 1.00 23.35 ? 362 LEU A CG 1 ATOM 2527 C CD1 . LEU A 1 369 ? 5.146 44.386 69.559 1.00 27.44 ? 362 LEU A CD1 1 ATOM 2528 C CD2 . LEU A 1 369 ? 7.471 44.999 68.800 1.00 25.27 ? 362 LEU A CD2 1 ATOM 2529 N N A ARG A 1 370 ? 2.334 46.927 68.134 0.50 20.99 ? 363 ARG A N 1 ATOM 2530 N N B ARG A 1 370 ? 2.331 46.945 68.120 0.50 20.79 ? 363 ARG A N 1 ATOM 2531 C CA A ARG A 1 370 ? 1.657 48.167 68.548 0.50 22.31 ? 363 ARG A CA 1 ATOM 2532 C CA B ARG A 1 370 ? 1.640 48.206 68.437 0.50 21.76 ? 363 ARG A CA 1 ATOM 2533 C C A ARG A 1 370 ? 2.513 48.998 69.505 0.50 21.14 ? 363 ARG A C 1 ATOM 2534 C C B ARG A 1 370 ? 2.356 49.017 69.533 0.50 20.86 ? 363 ARG A C 1 ATOM 2535 O O A ARG A 1 370 ? 3.137 48.454 70.421 0.50 21.88 ? 363 ARG A O 1 ATOM 2536 O O B ARG A 1 370 ? 2.731 48.470 70.575 0.50 22.37 ? 363 ARG A O 1 ATOM 2537 C CB A ARG A 1 370 ? 0.294 47.844 69.186 0.50 23.05 ? 363 ARG A CB 1 ATOM 2538 C CB B ARG A 1 370 ? 0.176 47.907 68.797 0.50 22.48 ? 363 ARG A CB 1 ATOM 2539 C CG A ARG A 1 370 ? -0.389 49.028 69.861 0.50 22.95 ? 363 ARG A CG 1 ATOM 2540 C CG B ARG A 1 370 ? -0.654 49.087 69.282 0.50 22.61 ? 363 ARG A CG 1 ATOM 2541 C CD A ARG A 1 370 ? -1.693 48.640 70.552 0.50 29.18 ? 363 ARG A CD 1 ATOM 2542 C CD B ARG A 1 370 ? -2.076 48.635 69.594 0.50 27.65 ? 363 ARG A CD 1 ATOM 2543 N NE A ARG A 1 370 ? -1.509 48.100 71.903 0.50 32.04 ? 363 ARG A NE 1 ATOM 2544 N NE B ARG A 1 370 ? -2.108 47.410 70.401 0.50 31.60 ? 363 ARG A NE 1 ATOM 2545 C CZ A ARG A 1 370 ? -1.835 46.865 72.274 0.50 33.15 ? 363 ARG A CZ 1 ATOM 2546 C CZ B ARG A 1 370 ? -2.371 46.196 69.918 0.50 29.26 ? 363 ARG A CZ 1 ATOM 2547 N NH1 A ARG A 1 370 ? -2.360 46.017 71.401 0.50 35.15 ? 363 ARG A NH1 1 ATOM 2548 N NH1 B ARG A 1 370 ? -2.637 46.031 68.624 0.50 28.46 ? 363 ARG A NH1 1 ATOM 2549 N NH2 A ARG A 1 370 ? -1.641 46.479 73.524 0.50 35.24 ? 363 ARG A NH2 1 ATOM 2550 N NH2 B ARG A 1 370 ? -2.376 45.147 70.728 0.50 33.16 ? 363 ARG A NH2 1 ATOM 2551 N N . GLY A 1 371 ? 2.576 50.306 69.266 1.00 21.05 ? 364 GLY A N 1 ATOM 2552 C CA . GLY A 1 371 ? 3.293 51.210 70.175 1.00 22.94 ? 364 GLY A CA 1 ATOM 2553 C C . GLY A 1 371 ? 2.521 51.462 71.461 1.00 22.98 ? 364 GLY A C 1 ATOM 2554 O O . GLY A 1 371 ? 1.293 51.532 71.448 1.00 24.54 ? 364 GLY A O 1 ATOM 2555 N N . ALA A 1 372 ? 3.248 51.600 72.568 1.00 25.31 ? 365 ALA A N 1 ATOM 2556 C CA . ALA A 1 372 ? 2.652 51.883 73.883 1.00 24.40 ? 365 ALA A CA 1 ATOM 2557 C C . ALA A 1 372 ? 2.147 53.316 74.041 1.00 24.51 ? 365 ALA A C 1 ATOM 2558 O O . ALA A 1 372 ? 1.177 53.567 74.790 1.00 26.44 ? 365 ALA A O 1 ATOM 2559 C CB . ALA A 1 372 ? 3.650 51.578 74.990 1.00 25.28 ? 365 ALA A CB 1 ATOM 2560 N N . VAL A 1 373 ? 2.812 54.265 73.381 1.00 24.18 ? 366 VAL A N 1 ATOM 2561 C CA . VAL A 1 373 ? 2.529 55.699 73.625 1.00 25.76 ? 366 VAL A CA 1 ATOM 2562 C C . VAL A 1 373 ? 2.027 56.387 72.349 1.00 24.82 ? 366 VAL A C 1 ATOM 2563 O O . VAL A 1 373 ? 1.057 57.134 72.373 1.00 26.28 ? 366 VAL A O 1 ATOM 2564 C CB . VAL A 1 373 ? 3.774 56.429 74.182 1.00 27.61 ? 366 VAL A CB 1 ATOM 2565 C CG1 . VAL A 1 373 ? 3.519 57.923 74.362 1.00 30.19 ? 366 VAL A CG1 1 ATOM 2566 C CG2 . VAL A 1 373 ? 4.220 55.807 75.499 1.00 30.60 ? 366 VAL A CG2 1 ATOM 2567 N N . GLU A 1 374 ? 2.699 56.125 71.232 1.00 21.50 ? 367 GLU A N 1 ATOM 2568 C CA . GLU A 1 374 ? 2.311 56.690 69.939 1.00 23.26 ? 367 GLU A CA 1 ATOM 2569 C C . GLU A 1 374 ? 2.025 55.570 68.944 1.00 20.23 ? 367 GLU A C 1 ATOM 2570 O O . GLU A 1 374 ? 2.797 55.382 67.988 1.00 21.04 ? 367 GLU A O 1 ATOM 2571 C CB . GLU A 1 374 ? 3.424 57.591 69.420 1.00 22.00 ? 367 GLU A CB 1 ATOM 2572 C CG . GLU A 1 374 ? 3.748 58.754 70.346 1.00 24.77 ? 367 GLU A CG 1 ATOM 2573 C CD . GLU A 1 374 ? 4.723 59.700 69.686 1.00 23.49 ? 367 GLU A CD 1 ATOM 2574 O OE1 . GLU A 1 374 ? 4.275 60.585 68.920 1.00 26.09 ? 367 GLU A OE1 1 ATOM 2575 O OE2 . GLU A 1 374 ? 5.937 59.561 69.928 1.00 27.23 ? 367 GLU A OE2 1 ATOM 2576 N N . PRO A 1 375 ? 0.923 54.812 69.159 1.00 22.62 ? 368 PRO A N 1 ATOM 2577 C CA . PRO A 1 375 ? 0.597 53.724 68.226 1.00 22.83 ? 368 PRO A CA 1 ATOM 2578 C C . PRO A 1 375 ? 0.274 54.220 66.815 1.00 20.84 ? 368 PRO A C 1 ATOM 2579 O O . PRO A 1 375 ? 0.390 53.452 65.871 1.00 21.12 ? 368 PRO A O 1 ATOM 2580 C CB . PRO A 1 375 ? -0.625 53.054 68.859 1.00 22.32 ? 368 PRO A CB 1 ATOM 2581 C CG . PRO A 1 375 ? -1.222 54.102 69.721 1.00 24.28 ? 368 PRO A CG 1 ATOM 2582 C CD . PRO A 1 375 ? -0.079 54.915 70.243 1.00 21.39 ? 368 PRO A CD 1 ATOM 2583 N N . ASP A 1 376 ? -0.075 55.504 66.673 1.00 21.13 ? 369 ASP A N 1 ATOM 2584 C CA . ASP A 1 376 ? -0.317 56.086 65.345 1.00 21.13 ? 369 ASP A CA 1 ATOM 2585 C C . ASP A 1 376 ? 0.940 56.668 64.676 1.00 19.21 ? 369 ASP A C 1 ATOM 2586 O O . ASP A 1 376 ? 0.835 57.538 63.804 1.00 18.20 ? 369 ASP A O 1 ATOM 2587 C CB . ASP A 1 376 ? -1.404 57.164 65.442 1.00 22.00 ? 369 ASP A CB 1 ATOM 2588 C CG . ASP A 1 376 ? -0.937 58.395 66.193 1.00 23.09 ? 369 ASP A CG 1 ATOM 2589 O OD1 . ASP A 1 376 ? 0.047 58.300 66.971 1.00 27.11 ? 369 ASP A OD1 1 ATOM 2590 O OD2 . ASP A 1 376 ? -1.536 59.476 65.975 1.00 27.09 ? 369 ASP A OD2 1 ATOM 2591 N N . ARG A 1 377 ? 2.119 56.188 65.081 1.00 18.62 ? 370 ARG A N 1 ATOM 2592 C CA . ARG A 1 377 ? 3.365 56.567 64.422 1.00 17.52 ? 370 ARG A CA 1 ATOM 2593 C C . ARG A 1 377 ? 4.028 55.275 64.028 1.00 17.25 ? 370 ARG A C 1 ATOM 2594 O O . ARG A 1 377 ? 4.179 54.386 64.870 1.00 17.17 ? 370 ARG A O 1 ATOM 2595 C CB . ARG A 1 377 ? 4.249 57.395 65.373 1.00 18.70 ? 370 ARG A CB 1 ATOM 2596 C CG . ARG A 1 377 ? 3.654 58.782 65.670 1.00 17.35 ? 370 ARG A CG 1 ATOM 2597 C CD . ARG A 1 377 ? 3.836 59.655 64.434 1.00 18.01 ? 370 ARG A CD 1 ATOM 2598 N NE . ARG A 1 377 ? 3.233 60.994 64.493 1.00 18.47 ? 370 ARG A NE 1 ATOM 2599 C CZ . ARG A 1 377 ? 2.000 61.322 64.074 1.00 17.49 ? 370 ARG A CZ 1 ATOM 2600 N NH1 . ARG A 1 377 ? 1.119 60.397 63.644 1.00 17.94 ? 370 ARG A NH1 1 ATOM 2601 N NH2 . ARG A 1 377 ? 1.628 62.602 64.106 1.00 18.33 ? 370 ARG A NH2 1 ATOM 2602 N N . TYR A 1 378 ? 4.412 55.157 62.757 1.00 17.49 ? 371 TYR A N 1 ATOM 2603 C CA . TYR A 1 378 ? 4.906 53.887 62.233 1.00 16.64 ? 371 TYR A CA 1 ATOM 2604 C C . TYR A 1 378 ? 6.372 53.950 61.865 1.00 16.90 ? 371 TYR A C 1 ATOM 2605 O O . TYR A 1 378 ? 6.791 54.792 61.039 1.00 18.81 ? 371 TYR A O 1 ATOM 2606 C CB . TYR A 1 378 ? 4.145 53.468 60.967 1.00 17.88 ? 371 TYR A CB 1 ATOM 2607 C CG . TYR A 1 378 ? 2.637 53.398 61.094 1.00 16.82 ? 371 TYR A CG 1 ATOM 2608 C CD1 . TYR A 1 378 ? 2.014 53.022 62.297 1.00 17.89 ? 371 TYR A CD1 1 ATOM 2609 C CD2 . TYR A 1 378 ? 1.830 53.679 59.999 1.00 15.89 ? 371 TYR A CD2 1 ATOM 2610 C CE1 . TYR A 1 378 ? 0.635 52.959 62.398 1.00 18.38 ? 371 TYR A CE1 1 ATOM 2611 C CE2 . TYR A 1 378 ? 0.454 53.631 60.091 1.00 18.67 ? 371 TYR A CE2 1 ATOM 2612 C CZ . TYR A 1 378 ? -0.143 53.258 61.288 1.00 18.37 ? 371 TYR A CZ 1 ATOM 2613 O OH . TYR A 1 378 ? -1.515 53.189 61.390 1.00 19.51 ? 371 TYR A OH 1 ATOM 2614 N N . VAL A 1 379 ? 7.135 53.014 62.419 1.00 16.60 ? 372 VAL A N 1 ATOM 2615 C CA . VAL A 1 379 ? 8.514 52.783 61.988 1.00 16.94 ? 372 VAL A CA 1 ATOM 2616 C C . VAL A 1 379 ? 8.471 51.433 61.283 1.00 16.48 ? 372 VAL A C 1 ATOM 2617 O O . VAL A 1 379 ? 8.031 50.425 61.865 1.00 17.68 ? 372 VAL A O 1 ATOM 2618 C CB . VAL A 1 379 ? 9.479 52.755 63.200 1.00 18.42 ? 372 VAL A CB 1 ATOM 2619 C CG1 . VAL A 1 379 ? 10.895 52.381 62.767 1.00 19.94 ? 372 VAL A CG1 1 ATOM 2620 C CG2 . VAL A 1 379 ? 9.503 54.112 63.883 1.00 18.58 ? 372 VAL A CG2 1 ATOM 2621 N N . ILE A 1 380 ? 8.926 51.417 60.030 1.00 15.92 ? 373 ILE A N 1 ATOM 2622 C CA . ILE A 1 380 ? 8.760 50.245 59.176 1.00 15.09 ? 373 ILE A CA 1 ATOM 2623 C C . ILE A 1 380 ? 10.108 49.609 58.872 1.00 15.84 ? 373 ILE A C 1 ATOM 2624 O O . ILE A 1 380 ? 11.042 50.287 58.427 1.00 16.77 ? 373 ILE A O 1 ATOM 2625 C CB . ILE A 1 380 ? 8.021 50.619 57.864 1.00 14.67 ? 373 ILE A CB 1 ATOM 2626 C CG1 . ILE A 1 380 ? 6.691 51.347 58.165 1.00 17.45 ? 373 ILE A CG1 1 ATOM 2627 C CG2 . ILE A 1 380 ? 7.840 49.366 56.959 1.00 15.81 ? 373 ILE A CG2 1 ATOM 2628 C CD1 . ILE A 1 380 ? 6.052 51.924 56.912 1.00 20.82 ? 373 ILE A CD1 1 ATOM 2629 N N . LEU A 1 381 ? 10.195 48.303 59.100 1.00 15.76 ? 374 LEU A N 1 ATOM 2630 C CA . LEU A 1 381 ? 11.339 47.510 58.666 1.00 15.76 ? 374 LEU A CA 1 ATOM 2631 C C . LEU A 1 381 ? 10.838 46.562 57.586 1.00 16.44 ? 374 LEU A C 1 ATOM 2632 O O . LEU A 1 381 ? 10.043 45.659 57.874 1.00 17.35 ? 374 LEU A O 1 ATOM 2633 C CB . LEU A 1 381 ? 11.950 46.723 59.850 1.00 16.68 ? 374 LEU A CB 1 ATOM 2634 C CG . LEU A 1 381 ? 13.091 45.741 59.521 1.00 14.97 ? 374 LEU A CG 1 ATOM 2635 C CD1 . LEU A 1 381 ? 14.297 46.505 58.961 1.00 18.04 ? 374 LEU A CD1 1 ATOM 2636 C CD2 . LEU A 1 381 ? 13.493 44.933 60.769 1.00 18.38 ? 374 LEU A CD2 1 ATOM 2637 N N . GLY A 1 382 ? 11.305 46.741 56.353 1.00 16.12 ? 375 GLY A N 1 ATOM 2638 C CA . GLY A 1 382 ? 10.769 45.926 55.237 1.00 15.24 ? 375 GLY A CA 1 ATOM 2639 C C . GLY A 1 382 ? 11.864 45.409 54.318 1.00 15.98 ? 375 GLY A C 1 ATOM 2640 O O . GLY A 1 382 ? 12.885 46.078 54.115 1.00 17.26 ? 375 GLY A O 1 ATOM 2641 N N . GLY A 1 383 ? 11.650 44.231 53.739 1.00 15.44 ? 376 GLY A N 1 ATOM 2642 C CA . GLY A 1 383 ? 12.589 43.703 52.739 1.00 15.85 ? 376 GLY A CA 1 ATOM 2643 C C . GLY A 1 383 ? 11.824 42.634 52.014 1.00 15.90 ? 376 GLY A C 1 ATOM 2644 O O . GLY A 1 383 ? 10.810 42.123 52.531 1.00 15.99 ? 376 GLY A O 1 ATOM 2645 N N . HIS A 1 384 ? 12.286 42.274 50.833 1.00 16.38 ? 377 HIS A N 1 ATOM 2646 C CA . HIS A 1 384 ? 11.525 41.293 50.048 1.00 14.86 ? 377 HIS A CA 1 ATOM 2647 C C . HIS A 1 384 ? 11.897 39.861 50.327 1.00 15.40 ? 377 HIS A C 1 ATOM 2648 O O . HIS A 1 384 ? 12.935 39.578 50.968 1.00 16.84 ? 377 HIS A O 1 ATOM 2649 C CB . HIS A 1 384 ? 11.554 41.642 48.555 1.00 14.17 ? 377 HIS A CB 1 ATOM 2650 C CG . HIS A 1 384 ? 12.839 41.299 47.846 1.00 14.48 ? 377 HIS A CG 1 ATOM 2651 N ND1 . HIS A 1 384 ? 12.965 40.199 47.047 1.00 14.90 ? 377 HIS A ND1 1 ATOM 2652 C CD2 . HIS A 1 384 ? 14.013 42.009 47.720 1.00 14.24 ? 377 HIS A CD2 1 ATOM 2653 C CE1 . HIS A 1 384 ? 14.182 40.203 46.466 1.00 14.10 ? 377 HIS A CE1 1 ATOM 2654 N NE2 . HIS A 1 384 ? 14.828 41.296 46.889 1.00 14.18 ? 377 HIS A NE2 1 ATOM 2655 N N . ARG A 1 385 ? 11.038 38.963 49.846 1.00 14.80 ? 378 ARG A N 1 ATOM 2656 C CA . ARG A 1 385 ? 11.095 37.532 50.123 1.00 15.12 ? 378 ARG A CA 1 ATOM 2657 C C . ARG A 1 385 ? 11.246 36.733 48.828 1.00 15.86 ? 378 ARG A C 1 ATOM 2658 O O . ARG A 1 385 ? 11.808 35.629 48.823 1.00 16.42 ? 378 ARG A O 1 ATOM 2659 C CB . ARG A 1 385 ? 9.796 37.126 50.835 1.00 17.03 ? 378 ARG A CB 1 ATOM 2660 C CG . ARG A 1 385 ? 9.699 35.646 51.216 1.00 17.49 ? 378 ARG A CG 1 ATOM 2661 C CD . ARG A 1 385 ? 8.295 35.286 51.719 1.00 16.74 ? 378 ARG A CD 1 ATOM 2662 N NE . ARG A 1 385 ? 7.284 35.324 50.646 1.00 17.17 ? 378 ARG A NE 1 ATOM 2663 C CZ . ARG A 1 385 ? 6.401 36.300 50.447 1.00 16.78 ? 378 ARG A CZ 1 ATOM 2664 N NH1 . ARG A 1 385 ? 6.332 37.353 51.265 1.00 15.51 ? 378 ARG A NH1 1 ATOM 2665 N NH2 . ARG A 1 385 ? 5.549 36.203 49.427 1.00 17.25 ? 378 ARG A NH2 1 ATOM 2666 N N . ASP A 1 386 ? 10.704 37.273 47.733 1.00 16.28 ? 379 ASP A N 1 ATOM 2667 C CA . ASP A 1 386 ? 10.761 36.574 46.445 1.00 14.94 ? 379 ASP A CA 1 ATOM 2668 C C . ASP A 1 386 ? 12.189 36.597 45.947 1.00 15.29 ? 379 ASP A C 1 ATOM 2669 O O . ASP A 1 386 ? 12.918 37.576 46.162 1.00 15.31 ? 379 ASP A O 1 ATOM 2670 C CB . ASP A 1 386 ? 9.851 37.247 45.407 1.00 15.04 ? 379 ASP A CB 1 ATOM 2671 C CG . ASP A 1 386 ? 10.294 38.660 45.072 1.00 14.98 ? 379 ASP A CG 1 ATOM 2672 O OD1 . ASP A 1 386 ? 10.362 39.534 45.987 1.00 15.52 ? 379 ASP A OD1 1 ATOM 2673 O OD2 . ASP A 1 386 ? 10.566 38.908 43.883 1.00 15.33 ? 379 ASP A OD2 1 ATOM 2674 N N . SER A 1 387 ? 12.591 35.521 45.281 1.00 15.63 ? 380 SER A N 1 ATOM 2675 C CA . SER A 1 387 ? 13.946 35.437 44.756 1.00 14.98 ? 380 SER A CA 1 ATOM 2676 C C . SER A 1 387 ? 13.904 34.988 43.303 1.00 16.17 ? 380 SER A C 1 ATOM 2677 O O . SER A 1 387 ? 12.868 34.466 42.830 1.00 18.16 ? 380 SER A O 1 ATOM 2678 C CB . SER A 1 387 ? 14.759 34.445 45.598 1.00 16.11 ? 380 SER A CB 1 ATOM 2679 O OG . SER A 1 387 ? 14.167 33.146 45.571 1.00 17.30 ? 380 SER A OG 1 ATOM 2680 N N . TRP A 1 388 ? 15.019 35.160 42.595 1.00 17.36 ? 381 TRP A N 1 ATOM 2681 C CA . TRP A 1 388 ? 15.104 34.603 41.238 1.00 15.43 ? 381 TRP A CA 1 ATOM 2682 C C . TRP A 1 388 ? 15.213 33.105 41.272 1.00 17.58 ? 381 TRP A C 1 ATOM 2683 O O . TRP A 1 388 ? 14.478 32.426 40.575 1.00 16.87 ? 381 TRP A O 1 ATOM 2684 C CB . TRP A 1 388 ? 16.233 35.240 40.398 1.00 16.58 ? 381 TRP A CB 1 ATOM 2685 C CG . TRP A 1 388 ? 15.764 36.561 39.834 1.00 15.91 ? 381 TRP A CG 1 ATOM 2686 C CD1 . TRP A 1 388 ? 16.272 37.841 40.087 1.00 16.19 ? 381 TRP A CD1 1 ATOM 2687 C CD2 . TRP A 1 388 ? 14.617 36.758 38.943 1.00 15.24 ? 381 TRP A CD2 1 ATOM 2688 N NE1 . TRP A 1 388 ? 15.531 38.801 39.407 1.00 17.05 ? 381 TRP A NE1 1 ATOM 2689 C CE2 . TRP A 1 388 ? 14.519 38.193 38.698 1.00 15.53 ? 381 TRP A CE2 1 ATOM 2690 C CE3 . TRP A 1 388 ? 13.680 35.885 38.317 1.00 14.75 ? 381 TRP A CE3 1 ATOM 2691 C CZ2 . TRP A 1 388 ? 13.510 38.733 37.900 1.00 16.16 ? 381 TRP A CZ2 1 ATOM 2692 C CZ3 . TRP A 1 388 ? 12.666 36.453 37.519 1.00 16.21 ? 381 TRP A CZ3 1 ATOM 2693 C CH2 . TRP A 1 388 ? 12.587 37.849 37.327 1.00 15.73 ? 381 TRP A CH2 1 ATOM 2694 N N . VAL A 1 389 ? 16.144 32.581 42.060 1.00 17.62 ? 382 VAL A N 1 ATOM 2695 C CA . VAL A 1 389 ? 16.246 31.125 42.273 1.00 17.76 ? 382 VAL A CA 1 ATOM 2696 C C . VAL A 1 389 ? 16.286 30.891 43.788 1.00 18.07 ? 382 VAL A C 1 ATOM 2697 O O . VAL A 1 389 ? 15.263 31.083 44.442 1.00 17.35 ? 382 VAL A O 1 ATOM 2698 C CB . VAL A 1 389 ? 17.386 30.415 41.483 1.00 17.10 ? 382 VAL A CB 1 ATOM 2699 C CG1 . VAL A 1 389 ? 17.176 28.885 41.523 1.00 17.14 ? 382 VAL A CG1 1 ATOM 2700 C CG2 . VAL A 1 389 ? 17.402 30.859 40.025 1.00 19.55 ? 382 VAL A CG2 1 ATOM 2701 N N . PHE A 1 390 ? 17.439 30.507 44.343 1.00 17.73 ? 383 PHE A N 1 ATOM 2702 C CA . PHE A 1 390 ? 17.530 30.204 45.780 1.00 17.52 ? 383 PHE A CA 1 ATOM 2703 C C . PHE A 1 390 ? 17.626 31.414 46.681 1.00 17.09 ? 383 PHE A C 1 ATOM 2704 O O . PHE A 1 390 ? 17.279 31.335 47.855 1.00 18.56 ? 383 PHE A O 1 ATOM 2705 C CB . PHE A 1 390 ? 18.666 29.209 46.053 1.00 17.65 ? 383 PHE A CB 1 ATOM 2706 C CG . PHE A 1 390 ? 18.516 27.942 45.257 1.00 18.87 ? 383 PHE A CG 1 ATOM 2707 C CD1 . PHE A 1 390 ? 17.506 27.008 45.570 1.00 18.96 ? 383 PHE A CD1 1 ATOM 2708 C CD2 . PHE A 1 390 ? 19.329 27.704 44.156 1.00 19.40 ? 383 PHE A CD2 1 ATOM 2709 C CE1 . PHE A 1 390 ? 17.355 25.844 44.815 1.00 20.45 ? 383 PHE A CE1 1 ATOM 2710 C CE2 . PHE A 1 390 ? 19.175 26.540 43.403 1.00 18.52 ? 383 PHE A CE2 1 ATOM 2711 C CZ . PHE A 1 390 ? 18.184 25.623 43.727 1.00 21.06 ? 383 PHE A CZ 1 ATOM 2712 N N . GLY A 1 391 ? 18.070 32.540 46.139 1.00 17.69 ? 384 GLY A N 1 ATOM 2713 C CA . GLY A 1 391 ? 18.106 33.780 46.938 1.00 16.41 ? 384 GLY A CA 1 ATOM 2714 C C . GLY A 1 391 ? 19.075 33.742 48.113 1.00 16.70 ? 384 GLY A C 1 ATOM 2715 O O . GLY A 1 391 ? 18.857 34.429 49.112 1.00 17.97 ? 384 GLY A O 1 ATOM 2716 N N . GLY A 1 392 ? 20.181 33.001 47.958 1.00 17.07 ? 385 GLY A N 1 ATOM 2717 C CA . GLY A 1 392 ? 21.168 32.818 49.037 1.00 18.42 ? 385 GLY A CA 1 ATOM 2718 C C . GLY A 1 392 ? 21.642 34.143 49.609 1.00 18.60 ? 385 GLY A C 1 ATOM 2719 O O . GLY A 1 392 ? 21.752 34.298 50.841 1.00 19.50 ? 385 GLY A O 1 ATOM 2720 N N . ILE A 1 393 ? 21.932 35.109 48.731 1.00 17.85 ? 386 ILE A N 1 ATOM 2721 C CA . ILE A 1 393 ? 22.213 36.469 49.223 1.00 16.52 ? 386 ILE A CA 1 ATOM 2722 C C . ILE A 1 393 ? 20.960 37.330 49.051 1.00 17.73 ? 386 ILE A C 1 ATOM 2723 O O . ILE A 1 393 ? 20.442 37.913 50.022 1.00 17.43 ? 386 ILE A O 1 ATOM 2724 C CB . ILE A 1 393 ? 23.438 37.092 48.498 1.00 15.91 ? 386 ILE A CB 1 ATOM 2725 C CG1 . ILE A 1 393 ? 24.732 36.372 48.955 1.00 18.94 ? 386 ILE A CG1 1 ATOM 2726 C CG2 . ILE A 1 393 ? 23.538 38.592 48.748 1.00 17.22 ? 386 ILE A CG2 1 ATOM 2727 C CD1 . ILE A 1 393 ? 25.960 36.722 48.138 1.00 21.31 ? 386 ILE A CD1 1 ATOM 2728 N N . ASP A 1 394 ? 20.460 37.386 47.820 1.00 17.78 ? 387 ASP A N 1 ATOM 2729 C CA . ASP A 1 394 ? 19.370 38.296 47.457 1.00 16.01 ? 387 ASP A CA 1 ATOM 2730 C C . ASP A 1 394 ? 18.058 37.498 47.305 1.00 16.85 ? 387 ASP A C 1 ATOM 2731 O O . ASP A 1 394 ? 17.881 36.816 46.293 1.00 17.57 ? 387 ASP A O 1 ATOM 2732 C CB . ASP A 1 394 ? 19.761 38.962 46.122 1.00 15.99 ? 387 ASP A CB 1 ATOM 2733 C CG . ASP A 1 394 ? 18.733 39.916 45.604 1.00 16.98 ? 387 ASP A CG 1 ATOM 2734 O OD1 . ASP A 1 394 ? 17.778 40.188 46.352 1.00 17.52 ? 387 ASP A OD1 1 ATOM 2735 O OD2 . ASP A 1 394 ? 18.872 40.386 44.431 1.00 18.47 ? 387 ASP A OD2 1 ATOM 2736 N N . PRO A 1 395 ? 17.114 37.617 48.262 1.00 16.23 ? 388 PRO A N 1 ATOM 2737 C CA . PRO A 1 395 ? 17.093 38.518 49.420 1.00 16.00 ? 388 PRO A CA 1 ATOM 2738 C C . PRO A 1 395 ? 17.274 37.808 50.750 1.00 15.80 ? 388 PRO A C 1 ATOM 2739 O O . PRO A 1 395 ? 17.137 38.456 51.803 1.00 16.95 ? 388 PRO A O 1 ATOM 2740 C CB . PRO A 1 395 ? 15.641 39.021 49.401 1.00 14.92 ? 388 PRO A CB 1 ATOM 2741 C CG . PRO A 1 395 ? 14.866 37.753 49.016 1.00 15.96 ? 388 PRO A CG 1 ATOM 2742 C CD . PRO A 1 395 ? 15.763 37.055 48.000 1.00 17.31 ? 388 PRO A CD 1 ATOM 2743 N N . GLN A 1 396 ? 17.507 36.493 50.744 1.00 16.72 ? 389 GLN A N 1 ATOM 2744 C CA . GLN A 1 396 ? 17.299 35.760 51.993 1.00 17.21 ? 389 GLN A CA 1 ATOM 2745 C C . GLN A 1 396 ? 18.328 36.102 53.083 1.00 17.97 ? 389 GLN A C 1 ATOM 2746 O O . GLN A 1 396 ? 18.028 35.950 54.257 1.00 17.64 ? 389 GLN A O 1 ATOM 2747 C CB . GLN A 1 396 ? 17.202 34.228 51.793 1.00 16.72 ? 389 GLN A CB 1 ATOM 2748 C CG . GLN A 1 396 ? 16.142 33.770 50.786 1.00 17.34 ? 389 GLN A CG 1 ATOM 2749 C CD . GLN A 1 396 ? 14.712 34.312 51.022 1.00 17.85 ? 389 GLN A CD 1 ATOM 2750 O OE1 . GLN A 1 396 ? 14.391 34.913 52.053 1.00 18.00 ? 389 GLN A OE1 1 ATOM 2751 N NE2 . GLN A 1 396 ? 13.850 34.087 50.043 1.00 19.34 ? 389 GLN A NE2 1 ATOM 2752 N N . SER A 1 397 ? 19.510 36.587 52.704 1.00 17.96 ? 390 SER A N 1 ATOM 2753 C CA . SER A 1 397 ? 20.476 37.051 53.714 1.00 18.36 ? 390 SER A CA 1 ATOM 2754 C C . SER A 1 397 ? 19.902 38.259 54.463 1.00 18.19 ? 390 SER A C 1 ATOM 2755 O O . SER A 1 397 ? 20.237 38.486 55.634 1.00 18.72 ? 390 SER A O 1 ATOM 2756 C CB . SER A 1 397 ? 21.849 37.386 53.101 1.00 18.91 ? 390 SER A CB 1 ATOM 2757 O OG . SER A 1 397 ? 21.757 38.534 52.278 1.00 17.65 ? 390 SER A OG 1 ATOM 2758 N N . GLY A 1 398 ? 19.050 39.020 53.774 1.00 16.55 ? 391 GLY A N 1 ATOM 2759 C CA . GLY A 1 398 ? 18.288 40.109 54.388 1.00 16.41 ? 391 GLY A CA 1 ATOM 2760 C C . GLY A 1 398 ? 17.087 39.619 55.169 1.00 17.00 ? 391 GLY A C 1 ATOM 2761 O O . GLY A 1 398 ? 16.867 40.043 56.308 1.00 17.69 ? 391 GLY A O 1 ATOM 2762 N N . ALA A 1 399 ? 16.281 38.754 54.554 1.00 16.07 ? 392 ALA A N 1 ATOM 2763 C CA . ALA A 1 399 ? 15.071 38.238 55.222 1.00 16.71 ? 392 ALA A CA 1 ATOM 2764 C C . ALA A 1 399 ? 15.365 37.475 56.506 1.00 17.08 ? 392 ALA A C 1 ATOM 2765 O O . ALA A 1 399 ? 14.576 37.569 57.466 1.00 17.11 ? 392 ALA A O 1 ATOM 2766 C CB . ALA A 1 399 ? 14.246 37.397 54.263 1.00 17.94 ? 392 ALA A CB 1 ATOM 2767 N N . ALA A 1 400 ? 16.479 36.725 56.535 1.00 18.60 ? 393 ALA A N 1 ATOM 2768 C CA . ALA A 1 400 ? 16.900 35.994 57.751 1.00 18.14 ? 393 ALA A CA 1 ATOM 2769 C C . ALA A 1 400 ? 17.204 36.969 58.870 1.00 19.25 ? 393 ALA A C 1 ATOM 2770 O O . ALA A 1 400 ? 16.921 36.691 60.044 1.00 19.09 ? 393 ALA A O 1 ATOM 2771 C CB . ALA A 1 400 ? 18.133 35.122 57.463 1.00 18.84 ? 393 ALA A CB 1 ATOM 2772 N N . VAL A 1 401 ? 17.795 38.109 58.496 1.00 18.45 ? 394 VAL A N 1 ATOM 2773 C CA . VAL A 1 401 ? 18.109 39.174 59.458 1.00 18.04 ? 394 VAL A CA 1 ATOM 2774 C C . VAL A 1 401 ? 16.816 39.805 59.989 1.00 17.98 ? 394 VAL A C 1 ATOM 2775 O O . VAL A 1 401 ? 16.679 40.022 61.207 1.00 18.67 ? 394 VAL A O 1 ATOM 2776 C CB . VAL A 1 401 ? 19.069 40.219 58.830 1.00 17.76 ? 394 VAL A CB 1 ATOM 2777 C CG1 . VAL A 1 401 ? 18.980 41.576 59.518 1.00 19.01 ? 394 VAL A CG1 1 ATOM 2778 C CG2 . VAL A 1 401 ? 20.500 39.688 58.846 1.00 20.06 ? 394 VAL A CG2 1 ATOM 2779 N N . VAL A 1 402 ? 15.866 40.100 59.091 1.00 17.22 ? 395 VAL A N 1 ATOM 2780 C CA . VAL A 1 402 ? 14.563 40.618 59.555 1.00 16.69 ? 395 VAL A CA 1 ATOM 2781 C C . VAL A 1 402 ? 13.913 39.613 60.521 1.00 18.25 ? 395 VAL A C 1 ATOM 2782 O O . VAL A 1 402 ? 13.392 39.997 61.567 1.00 17.67 ? 395 VAL A O 1 ATOM 2783 C CB . VAL A 1 402 ? 13.599 40.910 58.391 1.00 16.60 ? 395 VAL A CB 1 ATOM 2784 C CG1 . VAL A 1 402 ? 12.217 41.310 58.927 1.00 18.92 ? 395 VAL A CG1 1 ATOM 2785 C CG2 . VAL A 1 402 ? 14.165 42.029 57.513 1.00 19.08 ? 395 VAL A CG2 1 ATOM 2786 N N . HIS A 1 403 ? 13.957 38.329 60.173 1.00 19.12 ? 396 HIS A N 1 ATOM 2787 C CA . HIS A 1 403 ? 13.322 37.280 60.987 1.00 18.79 ? 396 HIS A CA 1 ATOM 2788 C C . HIS A 1 403 ? 13.871 37.282 62.396 1.00 21.04 ? 396 HIS A C 1 ATOM 2789 O O . HIS A 1 403 ? 13.104 37.253 63.380 1.00 23.09 ? 396 HIS A O 1 ATOM 2790 C CB . HIS A 1 403 ? 13.539 35.931 60.293 1.00 19.76 ? 396 HIS A CB 1 ATOM 2791 C CG . HIS A 1 403 ? 12.367 34.975 60.392 1.00 21.04 ? 396 HIS A CG 1 ATOM 2792 N ND1 . HIS A 1 403 ? 11.087 35.344 60.101 1.00 21.06 ? 396 HIS A ND1 1 ATOM 2793 C CD2 . HIS A 1 403 ? 12.325 33.607 60.694 1.00 21.48 ? 396 HIS A CD2 1 ATOM 2794 C CE1 . HIS A 1 403 ? 10.273 34.281 60.247 1.00 21.57 ? 396 HIS A CE1 1 ATOM 2795 N NE2 . HIS A 1 403 ? 11.029 33.215 60.611 1.00 22.83 ? 396 HIS A NE2 1 ATOM 2796 N N . GLU A 1 404 ? 15.195 37.346 62.521 1.00 20.35 ? 397 GLU A N 1 ATOM 2797 C CA . GLU A 1 404 ? 15.855 37.405 63.840 1.00 20.99 ? 397 GLU A CA 1 ATOM 2798 C C . GLU A 1 404 ? 15.538 38.704 64.606 1.00 20.51 ? 397 GLU A C 1 ATOM 2799 O O . GLU A 1 404 ? 15.398 38.695 65.844 1.00 22.13 ? 397 GLU A O 1 ATOM 2800 C CB . GLU A 1 404 ? 17.374 37.199 63.689 1.00 21.62 ? 397 GLU A CB 1 ATOM 2801 C CG . GLU A 1 404 ? 18.200 37.169 64.991 1.00 21.27 ? 397 GLU A CG 1 ATOM 2802 C CD . GLU A 1 404 ? 17.822 36.073 65.975 1.00 25.00 ? 397 GLU A CD 1 ATOM 2803 O OE1 . GLU A 1 404 ? 16.818 35.347 65.745 1.00 24.02 ? 397 GLU A OE1 1 ATOM 2804 O OE2 . GLU A 1 404 ? 18.546 35.945 67.002 1.00 25.61 ? 397 GLU A OE2 1 ATOM 2805 N N . ILE A 1 405 ? 15.433 39.820 63.874 1.00 20.08 ? 398 ILE A N 1 ATOM 2806 C CA . ILE A 1 405 ? 15.027 41.097 64.478 1.00 20.09 ? 398 ILE A CA 1 ATOM 2807 C C . ILE A 1 405 ? 13.611 41.005 65.054 1.00 20.54 ? 398 ILE A C 1 ATOM 2808 O O . ILE A 1 405 ? 13.369 41.420 66.190 1.00 21.46 ? 398 ILE A O 1 ATOM 2809 C CB . ILE A 1 405 ? 15.174 42.276 63.489 1.00 18.83 ? 398 ILE A CB 1 ATOM 2810 C CG1 . ILE A 1 405 ? 16.667 42.591 63.278 1.00 17.52 ? 398 ILE A CG1 1 ATOM 2811 C CG2 . ILE A 1 405 ? 14.398 43.513 63.970 1.00 19.35 ? 398 ILE A CG2 1 ATOM 2812 C CD1 . ILE A 1 405 ? 16.945 43.440 62.047 1.00 18.54 ? 398 ILE A CD1 1 ATOM 2813 N N . VAL A 1 406 ? 12.681 40.446 64.278 1.00 20.34 ? 399 VAL A N 1 ATOM 2814 C CA . VAL A 1 406 ? 11.300 40.222 64.771 1.00 21.51 ? 399 VAL A CA 1 ATOM 2815 C C . VAL A 1 406 ? 11.322 39.337 66.021 1.00 21.48 ? 399 VAL A C 1 ATOM 2816 O O . VAL A 1 406 ? 10.647 39.636 67.001 1.00 23.87 ? 399 VAL A O 1 ATOM 2817 C CB . VAL A 1 406 ? 10.370 39.587 63.709 1.00 19.99 ? 399 VAL A CB 1 ATOM 2818 C CG1 . VAL A 1 406 ? 9.002 39.247 64.313 1.00 20.89 ? 399 VAL A CG1 1 ATOM 2819 C CG2 . VAL A 1 406 ? 10.202 40.505 62.485 1.00 21.16 ? 399 VAL A CG2 1 ATOM 2820 N N . ARG A 1 407 ? 12.107 38.260 65.978 1.00 22.38 ? 400 ARG A N 1 ATOM 2821 C CA . ARG A 1 407 ? 12.214 37.345 67.104 1.00 22.43 ? 400 ARG A CA 1 ATOM 2822 C C . ARG A 1 407 ? 12.704 38.074 68.359 1.00 24.23 ? 400 ARG A C 1 ATOM 2823 O O . ARG A 1 407 ? 12.153 37.864 69.452 1.00 25.66 ? 400 ARG A O 1 ATOM 2824 C CB . ARG A 1 407 ? 13.112 36.143 66.776 1.00 22.81 ? 400 ARG A CB 1 ATOM 2825 C CG . ARG A 1 407 ? 12.955 34.993 67.772 1.00 22.95 ? 400 ARG A CG 1 ATOM 2826 C CD . ARG A 1 407 ? 14.117 33.981 67.721 1.00 24.33 ? 400 ARG A CD 1 ATOM 2827 N NE . ARG A 1 407 ? 15.401 34.622 68.021 1.00 25.48 ? 400 ARG A NE 1 ATOM 2828 C CZ . ARG A 1 407 ? 15.833 34.933 69.243 1.00 27.17 ? 400 ARG A CZ 1 ATOM 2829 N NH1 . ARG A 1 407 ? 16.999 35.543 69.393 1.00 27.82 ? 400 ARG A NH1 1 ATOM 2830 N NH2 . ARG A 1 407 ? 15.108 34.632 70.318 1.00 29.27 ? 400 ARG A NH2 1 ATOM 2831 N N . SER A 1 408 ? 13.708 38.944 68.204 1.00 23.37 ? 401 SER A N 1 ATOM 2832 C CA . SER A 1 408 ? 14.258 39.677 69.341 1.00 25.62 ? 401 SER A CA 1 ATOM 2833 C C . SER A 1 408 ? 13.256 40.679 69.922 1.00 25.33 ? 401 SER A C 1 ATOM 2834 O O . SER A 1 408 ? 13.034 40.699 71.146 1.00 26.50 ? 401 SER A O 1 ATOM 2835 C CB . SER A 1 408 ? 15.589 40.350 69.002 1.00 26.64 ? 401 SER A CB 1 ATOM 2836 O OG . SER A 1 408 ? 16.075 41.077 70.137 1.00 27.72 ? 401 SER A OG 1 ATOM 2837 N N . PHE A 1 409 ? 12.640 41.497 69.062 1.00 23.38 ? 402 PHE A N 1 ATOM 2838 C CA . PHE A 1 409 ? 11.599 42.405 69.529 1.00 24.58 ? 402 PHE A CA 1 ATOM 2839 C C . PHE A 1 409 ? 10.480 41.640 70.242 1.00 25.79 ? 402 PHE A C 1 ATOM 2840 O O . PHE A 1 409 ? 9.956 42.094 71.275 1.00 27.16 ? 402 PHE A O 1 ATOM 2841 C CB . PHE A 1 409 ? 11.024 43.208 68.366 1.00 24.08 ? 402 PHE A CB 1 ATOM 2842 C CG . PHE A 1 409 ? 11.813 44.441 68.007 1.00 22.00 ? 402 PHE A CG 1 ATOM 2843 C CD1 . PHE A 1 409 ? 11.964 45.482 68.929 1.00 21.68 ? 402 PHE A CD1 1 ATOM 2844 C CD2 . PHE A 1 409 ? 12.337 44.607 66.714 1.00 21.58 ? 402 PHE A CD2 1 ATOM 2845 C CE1 . PHE A 1 409 ? 12.653 46.647 68.587 1.00 22.76 ? 402 PHE A CE1 1 ATOM 2846 C CE2 . PHE A 1 409 ? 13.016 45.778 66.361 1.00 20.26 ? 402 PHE A CE2 1 ATOM 2847 C CZ . PHE A 1 409 ? 13.183 46.793 67.306 1.00 21.22 ? 402 PHE A CZ 1 ATOM 2848 N N . GLY A 1 410 ? 10.114 40.481 69.692 1.00 24.86 ? 403 GLY A N 1 ATOM 2849 C CA . GLY A 1 410 ? 9.083 39.626 70.280 1.00 25.93 ? 403 GLY A CA 1 ATOM 2850 C C . GLY A 1 410 ? 9.451 39.072 71.655 1.00 27.35 ? 403 GLY A C 1 ATOM 2851 O O . GLY A 1 410 ? 8.583 38.928 72.521 1.00 29.82 ? 403 GLY A O 1 ATOM 2852 N N . THR A 1 411 ? 10.729 38.755 71.868 1.00 28.70 ? 404 THR A N 1 ATOM 2853 C CA . THR A 1 411 ? 11.189 38.301 73.191 1.00 28.60 ? 404 THR A CA 1 ATOM 2854 C C . THR A 1 411 ? 10.949 39.401 74.227 1.00 29.82 ? 404 THR A C 1 ATOM 2855 O O . THR A 1 411 ? 10.457 39.126 75.325 1.00 32.04 ? 404 THR A O 1 ATOM 2856 C CB . THR A 1 411 ? 12.676 37.855 73.192 1.00 30.24 ? 404 THR A CB 1 ATOM 2857 O OG1 A THR A 1 411 ? 12.856 36.805 72.230 0.50 31.31 ? 404 THR A OG1 1 ATOM 2858 O OG1 B THR A 1 411 ? 13.545 38.996 73.169 0.50 31.26 ? 404 THR A OG1 1 ATOM 2859 C CG2 A THR A 1 411 ? 13.119 37.381 74.557 0.50 29.33 ? 404 THR A CG2 1 ATOM 2860 C CG2 B THR A 1 411 ? 12.987 36.920 72.024 0.50 30.04 ? 404 THR A CG2 1 ATOM 2861 N N . LEU A 1 412 ? 11.272 40.644 73.878 1.00 29.02 ? 405 LEU A N 1 ATOM 2862 C CA . LEU A 1 412 ? 11.065 41.762 74.802 1.00 29.23 ? 405 LEU A CA 1 ATOM 2863 C C . LEU A 1 412 ? 9.570 41.954 75.046 1.00 29.11 ? 405 LEU A C 1 ATOM 2864 O O . LEU A 1 412 ? 9.149 42.144 76.184 1.00 28.94 ? 405 LEU A O 1 ATOM 2865 C CB . LEU A 1 412 ? 11.680 43.072 74.269 1.00 31.30 ? 405 LEU A CB 1 ATOM 2866 C CG A LEU A 1 412 ? 13.174 43.149 73.955 0.50 31.52 ? 405 LEU A CG 1 ATOM 2867 C CG B LEU A 1 412 ? 13.159 43.358 74.563 0.50 30.11 ? 405 LEU A CG 1 ATOM 2868 C CD1 A LEU A 1 412 ? 13.483 44.451 73.234 0.50 29.73 ? 405 LEU A CD1 1 ATOM 2869 C CD1 B LEU A 1 412 ? 14.096 42.331 73.930 0.50 28.32 ? 405 LEU A CD1 1 ATOM 2870 C CD2 A LEU A 1 412 ? 14.010 43.017 75.219 0.50 32.91 ? 405 LEU A CD2 1 ATOM 2871 C CD2 B LEU A 1 412 ? 13.520 44.766 74.114 0.50 31.27 ? 405 LEU A CD2 1 ATOM 2872 N N . LYS A 1 413 ? 8.782 41.899 73.967 1.00 29.25 ? 406 LYS A N 1 ATOM 2873 C CA . LYS A 1 413 ? 7.327 42.016 74.050 1.00 29.05 ? 406 LYS A CA 1 ATOM 2874 C C . LYS A 1 413 ? 6.719 40.976 75.008 1.00 30.57 ? 406 LYS A C 1 ATOM 2875 O O . LYS A 1 413 ? 5.862 41.319 75.831 1.00 32.47 ? 406 LYS A O 1 ATOM 2876 C CB . LYS A 1 413 ? 6.721 41.898 72.648 1.00 31.32 ? 406 LYS A CB 1 ATOM 2877 C CG . LYS A 1 413 ? 5.310 42.439 72.514 1.00 37.15 ? 406 LYS A CG 1 ATOM 2878 C CD . LYS A 1 413 ? 4.289 41.328 72.643 1.00 39.69 ? 406 LYS A CD 1 ATOM 2879 C CE . LYS A 1 413 ? 2.967 41.732 72.021 1.00 39.42 ? 406 LYS A CE 1 ATOM 2880 N NZ . LYS A 1 413 ? 2.149 40.505 71.832 1.00 45.69 ? 406 LYS A NZ 1 ATOM 2881 N N . LYS A 1 414 ? 7.174 39.722 74.923 1.00 30.34 ? 407 LYS A N 1 ATOM 2882 C CA . LYS A 1 414 ? 6.666 38.655 75.814 1.00 32.95 ? 407 LYS A CA 1 ATOM 2883 C C . LYS A 1 414 ? 6.993 38.895 77.289 1.00 34.51 ? 407 LYS A C 1 ATOM 2884 O O . LYS A 1 414 ? 6.329 38.349 78.182 1.00 38.35 ? 407 LYS A O 1 ATOM 2885 C CB . LYS A 1 414 ? 7.139 37.269 75.355 1.00 34.23 ? 407 LYS A CB 1 ATOM 2886 C CG . LYS A 1 414 ? 6.471 36.823 74.062 1.00 34.32 ? 407 LYS A CG 1 ATOM 2887 C CD . LYS A 1 414 ? 6.961 35.471 73.583 1.00 36.35 ? 407 LYS A CD 1 ATOM 2888 C CE . LYS A 1 414 ? 6.334 35.120 72.243 1.00 34.02 ? 407 LYS A CE 1 ATOM 2889 N NZ . LYS A 1 414 ? 6.624 33.699 71.911 1.00 37.85 ? 407 LYS A NZ 1 ATOM 2890 N N . GLU A 1 415 ? 7.996 39.735 77.540 1.00 33.58 ? 408 GLU A N 1 ATOM 2891 C CA . GLU A 1 415 ? 8.367 40.131 78.905 1.00 36.04 ? 408 GLU A CA 1 ATOM 2892 C C . GLU A 1 415 ? 7.644 41.397 79.389 1.00 34.99 ? 408 GLU A C 1 ATOM 2893 O O . GLU A 1 415 ? 7.885 41.872 80.505 1.00 39.30 ? 408 GLU A O 1 ATOM 2894 C CB . GLU A 1 415 ? 9.885 40.296 79.025 1.00 37.07 ? 408 GLU A CB 1 ATOM 2895 C CG . GLU A 1 415 ? 10.674 39.015 78.773 1.00 42.60 ? 408 GLU A CG 1 ATOM 2896 C CD . GLU A 1 415 ? 12.175 39.206 78.894 0.75 46.64 ? 408 GLU A CD 1 ATOM 2897 O OE1 . GLU A 1 415 ? 12.893 38.189 78.982 0.50 48.04 ? 408 GLU A OE1 1 ATOM 2898 O OE2 . GLU A 1 415 ? 12.641 40.366 78.902 0.75 50.85 ? 408 GLU A OE2 1 ATOM 2899 N N . GLY A 1 416 ? 6.756 41.936 78.554 1.00 33.43 ? 409 GLY A N 1 ATOM 2900 C CA . GLY A 1 416 ? 5.924 43.074 78.934 1.00 34.36 ? 409 GLY A CA 1 ATOM 2901 C C . GLY A 1 416 ? 6.333 44.406 78.344 1.00 34.18 ? 409 GLY A C 1 ATOM 2902 O O . GLY A 1 416 ? 5.723 45.443 78.660 1.00 33.10 ? 409 GLY A O 1 ATOM 2903 N N . TRP A 1 417 ? 7.354 44.390 77.490 1.00 30.81 ? 410 TRP A N 1 ATOM 2904 C CA . TRP A 1 417 ? 7.827 45.605 76.850 1.00 30.27 ? 410 TRP A CA 1 ATOM 2905 C C . TRP A 1 417 ? 7.037 45.896 75.593 1.00 27.90 ? 410 TRP A C 1 ATOM 2906 O O . TRP A 1 417 ? 6.571 44.985 74.900 1.00 31.17 ? 410 TRP A O 1 ATOM 2907 C CB . TRP A 1 417 ? 9.320 45.478 76.548 1.00 31.77 ? 410 TRP A CB 1 ATOM 2908 C CG . TRP A 1 417 ? 9.930 46.599 75.729 1.00 31.54 ? 410 TRP A CG 1 ATOM 2909 C CD1 . TRP A 1 417 ? 10.492 47.785 76.197 1.00 33.33 ? 410 TRP A CD1 1 ATOM 2910 C CD2 . TRP A 1 417 ? 10.072 46.663 74.261 1.00 31.36 ? 410 TRP A CD2 1 ATOM 2911 N NE1 . TRP A 1 417 ? 10.960 48.550 75.157 1.00 31.31 ? 410 TRP A NE1 1 ATOM 2912 C CE2 . TRP A 1 417 ? 10.739 47.936 73.969 1.00 31.63 ? 410 TRP A CE2 1 ATOM 2913 C CE3 . TRP A 1 417 ? 9.725 45.822 73.197 1.00 30.69 ? 410 TRP A CE3 1 ATOM 2914 C CZ2 . TRP A 1 417 ? 11.043 48.325 72.671 1.00 26.54 ? 410 TRP A CZ2 1 ATOM 2915 C CZ3 . TRP A 1 417 ? 10.029 46.232 71.897 1.00 28.88 ? 410 TRP A CZ3 1 ATOM 2916 C CH2 . TRP A 1 417 ? 10.662 47.463 71.643 1.00 27.77 ? 410 TRP A CH2 1 ATOM 2917 N N . ARG A 1 418 ? 6.854 47.175 75.299 1.00 27.67 ? 411 ARG A N 1 ATOM 2918 C CA . ARG A 1 418 ? 6.400 47.590 73.972 1.00 26.64 ? 411 ARG A CA 1 ATOM 2919 C C . ARG A 1 418 ? 7.214 48.786 73.554 1.00 24.72 ? 411 ARG A C 1 ATOM 2920 O O . ARG A 1 418 ? 7.615 49.585 74.404 1.00 26.84 ? 411 ARG A O 1 ATOM 2921 C CB . ARG A 1 418 ? 4.935 48.041 73.986 1.00 29.01 ? 411 ARG A CB 1 ATOM 2922 C CG . ARG A 1 418 ? 3.934 46.918 73.989 1.00 32.35 ? 411 ARG A CG 1 ATOM 2923 C CD . ARG A 1 418 ? 2.505 47.426 73.844 1.00 30.98 ? 411 ARG A CD 1 ATOM 2924 N NE . ARG A 1 418 ? 1.666 46.243 73.784 1.00 31.66 ? 411 ARG A NE 1 ATOM 2925 C CZ . ARG A 1 418 ? 1.472 45.515 72.686 1.00 30.93 ? 411 ARG A CZ 1 ATOM 2926 N NH1 . ARG A 1 418 ? 2.006 45.891 71.518 1.00 26.12 ? 411 ARG A NH1 1 ATOM 2927 N NH2 . ARG A 1 418 ? 0.734 44.414 72.764 1.00 29.59 ? 411 ARG A NH2 1 ATOM 2928 N N . PRO A 1 419 ? 7.417 48.948 72.241 1.00 22.37 ? 412 PRO A N 1 ATOM 2929 C CA . PRO A 1 419 ? 8.073 50.172 71.798 1.00 23.84 ? 412 PRO A CA 1 ATOM 2930 C C . PRO A 1 419 ? 7.171 51.381 72.003 1.00 22.22 ? 412 PRO A C 1 ATOM 2931 O O . PRO A 1 419 ? 5.956 51.236 72.149 1.00 23.92 ? 412 PRO A O 1 ATOM 2932 C CB . PRO A 1 419 ? 8.319 49.925 70.307 1.00 21.90 ? 412 PRO A CB 1 ATOM 2933 C CG . PRO A 1 419 ? 7.249 48.953 69.904 1.00 21.79 ? 412 PRO A CG 1 ATOM 2934 C CD . PRO A 1 419 ? 6.975 48.101 71.113 1.00 21.50 ? 412 PRO A CD 1 ATOM 2935 N N . ARG A 1 420 ? 7.763 52.565 72.029 1.00 22.83 ? 413 ARG A N 1 ATOM 2936 C CA . ARG A 1 420 ? 6.974 53.796 72.147 1.00 22.21 ? 413 ARG A CA 1 ATOM 2937 C C . ARG A 1 420 ? 6.018 53.941 70.948 1.00 23.09 ? 413 ARG A C 1 ATOM 2938 O O . ARG A 1 420 ? 4.808 54.166 71.118 1.00 22.68 ? 413 ARG A O 1 ATOM 2939 C CB . ARG A 1 420 ? 7.891 55.008 72.262 1.00 21.07 ? 413 ARG A CB 1 ATOM 2940 C CG . ARG A 1 420 ? 7.135 56.324 72.357 1.00 23.10 ? 413 ARG A CG 1 ATOM 2941 C CD . ARG A 1 420 ? 8.042 57.526 72.194 1.00 26.62 ? 413 ARG A CD 1 ATOM 2942 N NE . ARG A 1 420 ? 7.252 58.761 72.171 1.00 27.98 ? 413 ARG A NE 1 ATOM 2943 C CZ . ARG A 1 420 ? 6.868 59.449 73.248 1.00 30.74 ? 413 ARG A CZ 1 ATOM 2944 N NH1 . ARG A 1 420 ? 7.201 59.046 74.477 1.00 28.79 ? 413 ARG A NH1 1 ATOM 2945 N NH2 . ARG A 1 420 ? 6.143 60.555 73.091 1.00 31.45 ? 413 ARG A NH2 1 ATOM 2946 N N . ARG A 1 421 ? 6.581 53.814 69.748 1.00 20.19 ? 414 ARG A N 1 ATOM 2947 C CA . ARG A 1 421 ? 5.822 53.916 68.484 1.00 19.50 ? 414 ARG A CA 1 ATOM 2948 C C . ARG A 1 421 ? 5.570 52.517 67.924 1.00 19.06 ? 414 ARG A C 1 ATOM 2949 O O . ARG A 1 421 ? 6.271 51.551 68.263 1.00 20.49 ? 414 ARG A O 1 ATOM 2950 C CB . ARG A 1 421 ? 6.596 54.755 67.449 1.00 19.89 ? 414 ARG A CB 1 ATOM 2951 C CG . ARG A 1 421 ? 7.061 56.119 67.988 1.00 19.92 ? 414 ARG A CG 1 ATOM 2952 C CD . ARG A 1 421 ? 7.788 57.002 66.963 1.00 20.55 ? 414 ARG A CD 1 ATOM 2953 N NE . ARG A 1 421 ? 7.999 58.272 67.651 1.00 21.18 ? 414 ARG A NE 1 ATOM 2954 C CZ . ARG A 1 421 ? 8.990 58.514 68.506 1.00 20.40 ? 414 ARG A CZ 1 ATOM 2955 N NH1 . ARG A 1 421 ? 9.957 57.613 68.685 1.00 18.48 ? 414 ARG A NH1 1 ATOM 2956 N NH2 . ARG A 1 421 ? 9.032 59.676 69.163 1.00 22.67 ? 414 ARG A NH2 1 ATOM 2957 N N . THR A 1 422 ? 4.580 52.414 67.054 1.00 18.12 ? 415 THR A N 1 ATOM 2958 C CA . THR A 1 422 ? 4.293 51.166 66.337 1.00 19.38 ? 415 THR A CA 1 ATOM 2959 C C . THR A 1 422 ? 5.437 50.794 65.372 1.00 19.42 ? 415 THR A C 1 ATOM 2960 O O . THR A 1 422 ? 5.984 51.648 64.650 1.00 19.65 ? 415 THR A O 1 ATOM 2961 C CB . THR A 1 422 ? 2.934 51.279 65.598 1.00 18.54 ? 415 THR A CB 1 ATOM 2962 O OG1 . THR A 1 422 ? 1.875 51.307 66.570 1.00 19.31 ? 415 THR A OG1 1 ATOM 2963 C CG2 . THR A 1 422 ? 2.706 50.108 64.607 1.00 18.65 ? 415 THR A CG2 1 ATOM 2964 N N . ILE A 1 423 ? 5.815 49.520 65.387 1.00 17.28 ? 416 ILE A N 1 ATOM 2965 C CA . ILE A 1 423 ? 6.764 49.002 64.416 1.00 17.79 ? 416 ILE A CA 1 ATOM 2966 C C . ILE A 1 423 ? 5.991 48.085 63.485 1.00 18.04 ? 416 ILE A C 1 ATOM 2967 O O . ILE A 1 423 ? 5.256 47.206 63.952 1.00 18.50 ? 416 ILE A O 1 ATOM 2968 C CB . ILE A 1 423 ? 7.929 48.213 65.075 1.00 17.01 ? 416 ILE A CB 1 ATOM 2969 C CG1 . ILE A 1 423 ? 8.665 49.076 66.119 1.00 18.49 ? 416 ILE A CG1 1 ATOM 2970 C CG2 . ILE A 1 423 ? 8.904 47.746 63.994 1.00 18.14 ? 416 ILE A CG2 1 ATOM 2971 C CD1 . ILE A 1 423 ? 9.695 48.308 66.928 1.00 19.92 ? 416 ILE A CD1 1 ATOM 2972 N N . LEU A 1 424 ? 6.142 48.326 62.177 1.00 16.57 ? 417 LEU A N 1 ATOM 2973 C CA . LEU A 1 424 ? 5.605 47.439 61.134 1.00 17.00 ? 417 LEU A CA 1 ATOM 2974 C C . LEU A 1 424 ? 6.754 46.686 60.514 1.00 17.14 ? 417 LEU A C 1 ATOM 2975 O O . LEU A 1 424 ? 7.797 47.282 60.203 1.00 18.07 ? 417 LEU A O 1 ATOM 2976 C CB . LEU A 1 424 ? 4.873 48.244 60.049 1.00 16.30 ? 417 LEU A CB 1 ATOM 2977 C CG . LEU A 1 424 ? 3.710 49.139 60.550 1.00 18.16 ? 417 LEU A CG 1 ATOM 2978 C CD1 . LEU A 1 424 ? 3.037 49.878 59.395 1.00 17.18 ? 417 LEU A CD1 1 ATOM 2979 C CD2 . LEU A 1 424 ? 2.692 48.343 61.365 1.00 19.17 ? 417 LEU A CD2 1 ATOM 2980 N N . PHE A 1 425 ? 6.554 45.383 60.335 1.00 17.42 ? 418 PHE A N 1 ATOM 2981 C CA . PHE A 1 425 ? 7.537 44.509 59.698 1.00 15.64 ? 418 PHE A CA 1 ATOM 2982 C C . PHE A 1 425 ? 6.928 43.981 58.416 1.00 16.30 ? 418 PHE A C 1 ATOM 2983 O O . PHE A 1 425 ? 5.760 43.570 58.399 1.00 17.70 ? 418 PHE A O 1 ATOM 2984 C CB . PHE A 1 425 ? 7.878 43.331 60.611 1.00 17.13 ? 418 PHE A CB 1 ATOM 2985 C CG . PHE A 1 425 ? 8.450 43.739 61.928 1.00 17.64 ? 418 PHE A CG 1 ATOM 2986 C CD1 . PHE A 1 425 ? 9.816 43.998 62.064 1.00 19.26 ? 418 PHE A CD1 1 ATOM 2987 C CD2 . PHE A 1 425 ? 7.619 43.879 63.054 1.00 19.40 ? 418 PHE A CD2 1 ATOM 2988 C CE1 . PHE A 1 425 ? 10.348 44.360 63.310 1.00 19.71 ? 418 PHE A CE1 1 ATOM 2989 C CE2 . PHE A 1 425 ? 8.152 44.238 64.289 1.00 20.07 ? 418 PHE A CE2 1 ATOM 2990 C CZ . PHE A 1 425 ? 9.513 44.481 64.414 1.00 20.18 ? 418 PHE A CZ 1 ATOM 2991 N N . ALA A 1 426 ? 7.706 43.996 57.335 1.00 16.45 ? 419 ALA A N 1 ATOM 2992 C CA . ALA A 1 426 ? 7.151 43.595 56.035 1.00 15.46 ? 419 ALA A CA 1 ATOM 2993 C C . ALA A 1 426 ? 8.071 42.620 55.310 1.00 15.97 ? 419 ALA A C 1 ATOM 2994 O O . ALA A 1 426 ? 9.282 42.820 55.263 1.00 17.21 ? 419 ALA A O 1 ATOM 2995 C CB . ALA A 1 426 ? 6.888 44.813 55.158 1.00 16.96 ? 419 ALA A CB 1 ATOM 2996 N N A SER A 1 427 ? 7.461 41.563 54.780 0.80 15.67 ? 420 SER A N 1 ATOM 2997 N N B SER A 1 427 ? 7.472 41.579 54.736 0.20 16.59 ? 420 SER A N 1 ATOM 2998 C CA A SER A 1 427 ? 8.091 40.621 53.873 0.80 15.33 ? 420 SER A CA 1 ATOM 2999 C CA B SER A 1 427 ? 8.173 40.650 53.858 0.20 16.23 ? 420 SER A CA 1 ATOM 3000 C C A SER A 1 427 ? 7.413 40.876 52.514 0.80 14.47 ? 420 SER A C 1 ATOM 3001 C C B SER A 1 427 ? 7.540 40.741 52.470 0.20 14.83 ? 420 SER A C 1 ATOM 3002 O O A SER A 1 427 ? 6.249 40.465 52.283 0.80 14.84 ? 420 SER A O 1 ATOM 3003 O O B SER A 1 427 ? 6.572 40.036 52.163 0.20 15.48 ? 420 SER A O 1 ATOM 3004 C CB A SER A 1 427 ? 7.837 39.191 54.382 0.80 14.19 ? 420 SER A CB 1 ATOM 3005 C CB B SER A 1 427 ? 8.066 39.226 54.390 0.20 18.43 ? 420 SER A CB 1 ATOM 3006 O OG A SER A 1 427 ? 8.290 38.205 53.455 0.80 12.30 ? 420 SER A OG 1 ATOM 3007 O OG B SER A 1 427 ? 7.006 38.540 53.754 0.20 20.99 ? 420 SER A OG 1 ATOM 3008 N N . TRP A 1 428 ? 8.098 41.623 51.647 1.00 14.24 ? 421 TRP A N 1 ATOM 3009 C CA . TRP A 1 428 ? 7.515 42.022 50.356 1.00 13.74 ? 421 TRP A CA 1 ATOM 3010 C C . TRP A 1 428 ? 7.620 40.943 49.317 1.00 14.90 ? 421 TRP A C 1 ATOM 3011 O O . TRP A 1 428 ? 8.585 40.169 49.299 1.00 16.53 ? 421 TRP A O 1 ATOM 3012 C CB . TRP A 1 428 ? 8.252 43.227 49.786 1.00 13.45 ? 421 TRP A CB 1 ATOM 3013 C CG . TRP A 1 428 ? 8.324 44.446 50.654 1.00 13.73 ? 421 TRP A CG 1 ATOM 3014 C CD1 . TRP A 1 428 ? 9.467 45.159 51.006 1.00 13.08 ? 421 TRP A CD1 1 ATOM 3015 C CD2 . TRP A 1 428 ? 7.198 45.176 51.267 1.00 13.63 ? 421 TRP A CD2 1 ATOM 3016 N NE1 . TRP A 1 428 ? 9.142 46.256 51.774 1.00 14.35 ? 421 TRP A NE1 1 ATOM 3017 C CE2 . TRP A 1 428 ? 7.785 46.313 51.976 1.00 14.00 ? 421 TRP A CE2 1 ATOM 3018 C CE3 . TRP A 1 428 ? 5.792 45.006 51.286 1.00 13.92 ? 421 TRP A CE3 1 ATOM 3019 C CZ2 . TRP A 1 428 ? 6.994 47.235 52.686 1.00 14.46 ? 421 TRP A CZ2 1 ATOM 3020 C CZ3 . TRP A 1 428 ? 5.017 45.934 51.991 1.00 15.13 ? 421 TRP A CZ3 1 ATOM 3021 C CH2 . TRP A 1 428 ? 5.617 47.017 52.703 1.00 15.84 ? 421 TRP A CH2 1 ATOM 3022 N N . ASP A 1 429 ? 6.639 40.912 48.409 1.00 15.23 ? 422 ASP A N 1 ATOM 3023 C CA . ASP A 1 429 ? 6.683 39.964 47.313 1.00 13.95 ? 422 ASP A CA 1 ATOM 3024 C C . ASP A 1 429 ? 6.984 40.740 46.029 1.00 14.31 ? 422 ASP A C 1 ATOM 3025 O O . ASP A 1 429 ? 6.825 41.994 45.973 1.00 15.37 ? 422 ASP A O 1 ATOM 3026 C CB . ASP A 1 429 ? 5.326 39.248 47.203 1.00 14.92 ? 422 ASP A CB 1 ATOM 3027 C CG . ASP A 1 429 ? 5.403 37.881 46.486 1.00 15.47 ? 422 ASP A CG 1 ATOM 3028 O OD1 . ASP A 1 429 ? 6.443 37.535 45.859 1.00 16.46 ? 422 ASP A OD1 1 ATOM 3029 O OD2 . ASP A 1 429 ? 4.377 37.164 46.540 1.00 17.09 ? 422 ASP A OD2 1 ATOM 3030 N N . ALA A 1 430 ? 7.378 39.988 45.004 1.00 14.52 ? 423 ALA A N 1 ATOM 3031 C CA . ALA A 1 430 ? 7.592 40.497 43.645 1.00 14.44 ? 423 ALA A CA 1 ATOM 3032 C C . ALA A 1 430 ? 8.535 41.707 43.551 1.00 14.00 ? 423 ALA A C 1 ATOM 3033 O O . ALA A 1 430 ? 8.441 42.521 42.616 1.00 15.08 ? 423 ALA A O 1 ATOM 3034 C CB . ALA A 1 430 ? 6.243 40.769 42.940 1.00 15.60 ? 423 ALA A CB 1 ATOM 3035 N N . ALA A 1 431 ? 9.471 41.841 44.479 1.00 14.26 ? 424 ALA A N 1 ATOM 3036 C CA . ALA A 1 431 ? 10.458 42.932 44.315 1.00 13.87 ? 424 ALA A CA 1 ATOM 3037 C C . ALA A 1 431 ? 11.264 42.731 43.039 1.00 14.68 ? 424 ALA A C 1 ATOM 3038 O O . ALA A 1 431 ? 11.642 43.718 42.371 1.00 14.86 ? 424 ALA A O 1 ATOM 3039 C CB . ALA A 1 431 ? 11.404 43.013 45.496 1.00 15.16 ? 424 ALA A CB 1 ATOM 3040 N N . GLU A 1 432 ? 11.558 41.473 42.707 1.00 15.23 ? 425 GLU A N 1 ATOM 3041 C CA . GLU A 1 432 ? 12.418 41.207 41.541 1.00 14.41 ? 425 GLU A CA 1 ATOM 3042 C C . GLU A 1 432 ? 11.714 41.602 40.239 1.00 14.63 ? 425 GLU A C 1 ATOM 3043 O O . GLU A 1 432 ? 12.368 41.771 39.185 1.00 15.23 ? 425 GLU A O 1 ATOM 3044 C CB . GLU A 1 432 ? 12.904 39.751 41.466 1.00 13.37 ? 425 GLU A CB 1 ATOM 3045 C CG . GLU A 1 432 ? 13.826 39.304 42.612 1.00 13.94 ? 425 GLU A CG 1 ATOM 3046 C CD . GLU A 1 432 ? 15.198 40.029 42.737 1.00 14.25 ? 425 GLU A CD 1 ATOM 3047 O OE1 . GLU A 1 432 ? 15.561 41.026 42.092 1.00 17.07 ? 425 GLU A OE1 1 ATOM 3048 O OE2 . GLU A 1 432 ? 16.041 39.630 43.544 1.00 16.48 ? 425 GLU A OE2 1 ATOM 3049 N N . PHE A 1 433 ? 10.391 41.765 40.301 1.00 14.44 ? 426 PHE A N 1 ATOM 3050 C CA . PHE A 1 433 ? 9.625 42.107 39.104 1.00 14.49 ? 426 PHE A CA 1 ATOM 3051 C C . PHE A 1 433 ? 9.265 43.583 39.037 1.00 14.59 ? 426 PHE A C 1 ATOM 3052 O O . PHE A 1 433 ? 8.394 43.984 38.246 1.00 14.81 ? 426 PHE A O 1 ATOM 3053 C CB . PHE A 1 433 ? 8.368 41.221 39.026 1.00 14.94 ? 426 PHE A CB 1 ATOM 3054 C CG . PHE A 1 433 ? 8.673 39.778 38.665 1.00 13.83 ? 426 PHE A CG 1 ATOM 3055 C CD1 . PHE A 1 433 ? 8.538 39.343 37.354 1.00 15.03 ? 426 PHE A CD1 1 ATOM 3056 C CD2 . PHE A 1 433 ? 9.083 38.847 39.657 1.00 16.20 ? 426 PHE A CD2 1 ATOM 3057 C CE1 . PHE A 1 433 ? 8.831 38.005 36.992 1.00 16.16 ? 426 PHE A CE1 1 ATOM 3058 C CE2 . PHE A 1 433 ? 9.362 37.507 39.323 1.00 15.02 ? 426 PHE A CE2 1 ATOM 3059 C CZ . PHE A 1 433 ? 9.225 37.083 37.976 1.00 16.55 ? 426 PHE A CZ 1 ATOM 3060 N N . GLY A 1 434 ? 9.954 44.397 39.836 1.00 14.15 ? 427 GLY A N 1 ATOM 3061 C CA . GLY A 1 434 ? 9.760 45.858 39.785 1.00 13.34 ? 427 GLY A CA 1 ATOM 3062 C C . GLY A 1 434 ? 9.256 46.471 41.078 1.00 13.93 ? 427 GLY A C 1 ATOM 3063 O O . GLY A 1 434 ? 8.525 47.464 41.046 1.00 15.07 ? 427 GLY A O 1 ATOM 3064 N N . LEU A 1 435 ? 9.660 45.913 42.218 1.00 12.41 ? 428 LEU A N 1 ATOM 3065 C CA . LEU A 1 435 ? 9.286 46.495 43.535 1.00 13.42 ? 428 LEU A CA 1 ATOM 3066 C C . LEU A 1 435 ? 7.762 46.470 43.660 1.00 12.80 ? 428 LEU A C 1 ATOM 3067 O O . LEU A 1 435 ? 7.151 47.378 44.212 1.00 13.95 ? 428 LEU A O 1 ATOM 3068 C CB . LEU A 1 435 ? 9.845 47.941 43.716 1.00 13.10 ? 428 LEU A CB 1 ATOM 3069 C CG . LEU A 1 435 ? 11.297 48.100 43.201 1.00 12.43 ? 428 LEU A CG 1 ATOM 3070 C CD1 . LEU A 1 435 ? 11.738 49.558 43.342 1.00 16.00 ? 428 LEU A CD1 1 ATOM 3071 C CD2 . LEU A 1 435 ? 12.271 47.167 43.935 1.00 15.65 ? 428 LEU A CD2 1 ATOM 3072 N N . LEU A 1 436 ? 7.144 45.410 43.148 1.00 13.72 ? 429 LEU A N 1 ATOM 3073 C CA . LEU A 1 436 ? 5.676 45.456 42.992 1.00 13.92 ? 429 LEU A CA 1 ATOM 3074 C C . LEU A 1 436 ? 4.925 45.333 44.315 1.00 14.49 ? 429 LEU A C 1 ATOM 3075 O O . LEU A 1 436 ? 3.930 46.030 44.532 1.00 14.81 ? 429 LEU A O 1 ATOM 3076 C CB . LEU A 1 436 ? 5.189 44.400 41.989 1.00 14.20 ? 429 LEU A CB 1 ATOM 3077 C CG . LEU A 1 436 ? 5.892 44.412 40.627 1.00 13.07 ? 429 LEU A CG 1 ATOM 3078 C CD1 . LEU A 1 436 ? 5.201 43.367 39.747 1.00 15.05 ? 429 LEU A CD1 1 ATOM 3079 C CD2 . LEU A 1 436 ? 5.795 45.799 39.966 1.00 16.62 ? 429 LEU A CD2 1 ATOM 3080 N N . GLY A 1 437 ? 5.375 44.435 45.185 1.00 14.44 ? 430 GLY A N 1 ATOM 3081 C CA . GLY A 1 437 ? 4.677 44.201 46.458 1.00 14.54 ? 430 GLY A CA 1 ATOM 3082 C C . GLY A 1 437 ? 4.708 45.412 47.383 1.00 13.54 ? 430 GLY A C 1 ATOM 3083 O O . GLY A 1 437 ? 3.679 45.797 47.953 1.00 15.02 ? 430 GLY A O 1 ATOM 3084 N N . SER A 1 438 ? 5.881 46.024 47.540 1.00 14.32 ? 431 SER A N 1 ATOM 3085 C CA . SER A 1 438 ? 6.011 47.182 48.424 1.00 13.86 ? 431 SER A CA 1 ATOM 3086 C C . SER A 1 438 ? 5.188 48.329 47.829 1.00 13.53 ? 431 SER A C 1 ATOM 3087 O O . SER A 1 438 ? 4.468 49.046 48.546 1.00 13.51 ? 431 SER A O 1 ATOM 3088 C CB . SER A 1 438 ? 7.487 47.585 48.570 1.00 13.61 ? 431 SER A CB 1 ATOM 3089 O OG . SER A 1 438 ? 8.069 47.933 47.313 1.00 14.37 ? 431 SER A OG 1 ATOM 3090 N N . THR A 1 439 ? 5.275 48.497 46.513 1.00 13.20 ? 432 THR A N 1 ATOM 3091 C CA . THR A 1 439 ? 4.602 49.643 45.878 1.00 13.57 ? 432 THR A CA 1 ATOM 3092 C C . THR A 1 439 ? 3.088 49.510 45.927 1.00 13.67 ? 432 THR A C 1 ATOM 3093 O O . THR A 1 439 ? 2.395 50.492 46.275 1.00 13.81 ? 432 THR A O 1 ATOM 3094 C CB . THR A 1 439 ? 5.086 49.852 44.424 1.00 13.77 ? 432 THR A CB 1 ATOM 3095 O OG1 . THR A 1 439 ? 6.512 50.018 44.434 1.00 15.34 ? 432 THR A OG1 1 ATOM 3096 C CG2 . THR A 1 439 ? 4.444 51.123 43.827 1.00 14.93 ? 432 THR A CG2 1 ATOM 3097 N N . GLU A 1 440 ? 2.556 48.318 45.621 1.00 13.80 ? 433 GLU A N 1 ATOM 3098 C CA . GLU A 1 440 ? 1.085 48.144 45.693 1.00 13.12 ? 433 GLU A CA 1 ATOM 3099 C C . GLU A 1 440 ? 0.565 48.378 47.124 1.00 13.57 ? 433 GLU A C 1 ATOM 3100 O O . GLU A 1 440 ? -0.470 49.019 47.319 1.00 15.20 ? 433 GLU A O 1 ATOM 3101 C CB . GLU A 1 440 ? 0.624 46.771 45.174 1.00 13.55 ? 433 GLU A CB 1 ATOM 3102 C CG . GLU A 1 440 ? 0.863 46.573 43.661 1.00 14.33 ? 433 GLU A CG 1 ATOM 3103 C CD . GLU A 1 440 ? 0.303 47.704 42.810 1.00 14.03 ? 433 GLU A CD 1 ATOM 3104 O OE1 . GLU A 1 440 ? -0.927 47.965 42.862 1.00 15.55 ? 433 GLU A OE1 1 ATOM 3105 O OE2 . GLU A 1 440 ? 1.054 48.369 42.045 1.00 15.79 ? 433 GLU A OE2 1 ATOM 3106 N N . TRP A 1 441 ? 1.273 47.850 48.117 1.00 14.31 ? 434 TRP A N 1 ATOM 3107 C CA . TRP A 1 441 ? 0.873 48.037 49.511 1.00 14.15 ? 434 TRP A CA 1 ATOM 3108 C C . TRP A 1 441 ? 0.930 49.502 49.915 1.00 14.19 ? 434 TRP A C 1 ATOM 3109 O O . TRP A 1 441 ? 0.029 49.990 50.593 1.00 14.09 ? 434 TRP A O 1 ATOM 3110 C CB . TRP A 1 441 ? 1.732 47.162 50.408 1.00 15.35 ? 434 TRP A CB 1 ATOM 3111 C CG . TRP A 1 441 ? 1.324 47.216 51.864 1.00 14.74 ? 434 TRP A CG 1 ATOM 3112 C CD1 . TRP A 1 441 ? 0.324 46.466 52.526 1.00 16.18 ? 434 TRP A CD1 1 ATOM 3113 C CD2 . TRP A 1 441 ? 1.907 48.084 52.888 1.00 16.63 ? 434 TRP A CD2 1 ATOM 3114 N NE1 . TRP A 1 441 ? 0.271 46.807 53.849 1.00 18.00 ? 434 TRP A NE1 1 ATOM 3115 C CE2 . TRP A 1 441 ? 1.186 47.783 54.138 1.00 17.39 ? 434 TRP A CE2 1 ATOM 3116 C CE3 . TRP A 1 441 ? 2.899 49.082 52.886 1.00 14.72 ? 434 TRP A CE3 1 ATOM 3117 C CZ2 . TRP A 1 441 ? 1.493 48.424 55.341 1.00 18.51 ? 434 TRP A CZ2 1 ATOM 3118 C CZ3 . TRP A 1 441 ? 3.219 49.716 54.127 1.00 15.75 ? 434 TRP A CZ3 1 ATOM 3119 C CH2 . TRP A 1 441 ? 2.509 49.399 55.313 1.00 16.36 ? 434 TRP A CH2 1 ATOM 3120 N N . ALA A 1 442 ? 1.971 50.218 49.476 1.00 13.63 ? 435 ALA A N 1 ATOM 3121 C CA . ALA A 1 442 ? 2.093 51.636 49.791 1.00 13.62 ? 435 ALA A CA 1 ATOM 3122 C C . ALA A 1 442 ? 0.998 52.425 49.073 1.00 13.95 ? 435 ALA A C 1 ATOM 3123 O O . ALA A 1 442 ? 0.474 53.383 49.623 1.00 14.08 ? 435 ALA A O 1 ATOM 3124 C CB . ALA A 1 442 ? 3.486 52.170 49.439 1.00 14.64 ? 435 ALA A CB 1 ATOM 3125 N N . GLU A 1 443 ? 0.640 52.013 47.849 1.00 13.43 ? 436 GLU A N 1 ATOM 3126 C CA . GLU A 1 443 ? -0.486 52.684 47.124 1.00 13.82 ? 436 GLU A CA 1 ATOM 3127 C C . GLU A 1 443 ? -1.797 52.465 47.878 1.00 14.18 ? 436 GLU A C 1 ATOM 3128 O O . GLU A 1 443 ? -2.613 53.399 48.025 1.00 15.25 ? 436 GLU A O 1 ATOM 3129 C CB . GLU A 1 443 ? -0.609 52.180 45.684 1.00 14.90 ? 436 GLU A CB 1 ATOM 3130 C CG . GLU A 1 443 ? 0.525 52.731 44.794 1.00 13.54 ? 436 GLU A CG 1 ATOM 3131 C CD . GLU A 1 443 ? 0.379 52.375 43.333 1.00 16.91 ? 436 GLU A CD 1 ATOM 3132 O OE1 . GLU A 1 443 ? 0.759 53.214 42.487 1.00 15.74 ? 436 GLU A OE1 1 ATOM 3133 O OE2 . GLU A 1 443 ? -0.137 51.274 43.039 1.00 16.61 ? 436 GLU A OE2 1 ATOM 3134 N N . GLU A 1 444 ? -1.994 51.252 48.373 1.00 14.65 ? 437 GLU A N 1 ATOM 3135 C CA . GLU A 1 444 ? -3.187 50.973 49.163 1.00 13.35 ? 437 GLU A CA 1 ATOM 3136 C C . GLU A 1 444 ? -3.239 51.826 50.440 1.00 14.61 ? 437 GLU A C 1 ATOM 3137 O O . GLU A 1 444 ? -4.298 52.334 50.806 1.00 16.12 ? 437 GLU A O 1 ATOM 3138 C CB . GLU A 1 444 ? -3.217 49.496 49.542 1.00 14.91 ? 437 GLU A CB 1 ATOM 3139 C CG . GLU A 1 444 ? -4.544 49.056 50.170 1.00 17.37 ? 437 GLU A CG 1 ATOM 3140 C CD . GLU A 1 444 ? -4.783 47.578 49.896 1.00 25.51 ? 437 GLU A CD 1 ATOM 3141 O OE1 . GLU A 1 444 ? -5.711 47.223 49.129 1.00 43.31 ? 437 GLU A OE1 1 ATOM 3142 O OE2 . GLU A 1 444 ? -4.000 46.782 50.399 1.00 26.50 ? 437 GLU A OE2 1 ATOM 3143 N N . ASN A 1 445 ? -2.091 51.975 51.098 1.00 14.20 ? 438 ASN A N 1 ATOM 3144 C CA . ASN A 1 445 ? -2.045 52.566 52.447 1.00 14.26 ? 438 ASN A CA 1 ATOM 3145 C C . ASN A 1 445 ? -1.451 53.963 52.470 1.00 14.63 ? 438 ASN A C 1 ATOM 3146 O O . ASN A 1 445 ? -1.027 54.445 53.528 1.00 14.17 ? 438 ASN A O 1 ATOM 3147 C CB . ASN A 1 445 ? -1.283 51.600 53.376 1.00 14.87 ? 438 ASN A CB 1 ATOM 3148 C CG . ASN A 1 445 ? -2.065 50.328 53.580 1.00 15.68 ? 438 ASN A CG 1 ATOM 3149 O OD1 . ASN A 1 445 ? -3.129 50.357 54.215 1.00 19.94 ? 438 ASN A OD1 1 ATOM 3150 N ND2 . ASN A 1 445 ? -1.602 49.224 52.999 1.00 17.71 ? 438 ASN A ND2 1 ATOM 3151 N N . SER A 1 446 ? -1.426 54.618 51.304 1.00 13.80 ? 439 SER A N 1 ATOM 3152 C CA . SER A 1 446 ? -0.688 55.883 51.168 1.00 12.76 ? 439 SER A CA 1 ATOM 3153 C C . SER A 1 446 ? -1.109 56.952 52.186 1.00 13.83 ? 439 SER A C 1 ATOM 3154 O O . SER A 1 446 ? -0.245 57.697 52.680 1.00 14.68 ? 439 SER A O 1 ATOM 3155 C CB . SER A 1 446 ? -0.836 56.434 49.725 1.00 13.67 ? 439 SER A CB 1 ATOM 3156 O OG . SER A 1 446 ? -2.180 56.730 49.451 1.00 15.85 ? 439 SER A OG 1 ATOM 3157 N N . ARG A 1 447 ? -2.408 57.034 52.496 1.00 13.97 ? 440 ARG A N 1 ATOM 3158 C CA . ARG A 1 447 ? -2.912 58.058 53.423 1.00 13.58 ? 440 ARG A CA 1 ATOM 3159 C C . ARG A 1 447 ? -2.408 57.794 54.839 1.00 14.58 ? 440 ARG A C 1 ATOM 3160 O O . ARG A 1 447 ? -2.038 58.736 55.564 1.00 15.15 ? 440 ARG A O 1 ATOM 3161 C CB . ARG A 1 447 ? -4.438 58.118 53.395 1.00 14.96 ? 440 ARG A CB 1 ATOM 3162 C CG . ARG A 1 447 ? -4.937 58.660 52.061 1.00 16.90 ? 440 ARG A CG 1 ATOM 3163 C CD . ARG A 1 447 ? -6.264 58.056 51.635 1.00 19.40 ? 440 ARG A CD 1 ATOM 3164 N NE . ARG A 1 447 ? -6.631 58.583 50.310 1.00 18.90 ? 440 ARG A NE 1 ATOM 3165 C CZ . ARG A 1 447 ? -6.205 58.136 49.134 1.00 17.60 ? 440 ARG A CZ 1 ATOM 3166 N NH1 . ARG A 1 447 ? -5.402 57.044 49.017 1.00 21.16 ? 440 ARG A NH1 1 ATOM 3167 N NH2 . ARG A 1 447 ? -6.623 58.788 48.050 1.00 16.49 ? 440 ARG A NH2 1 ATOM 3168 N N . LEU A 1 448 ? -2.395 56.525 55.240 1.00 14.67 ? 441 LEU A N 1 ATOM 3169 C CA . LEU A 1 448 ? -1.866 56.188 56.562 1.00 14.27 ? 441 LEU A CA 1 ATOM 3170 C C . LEU A 1 448 ? -0.365 56.481 56.617 1.00 15.33 ? 441 LEU A C 1 ATOM 3171 O O . LEU A 1 448 ? 0.145 57.039 57.600 1.00 16.16 ? 441 LEU A O 1 ATOM 3172 C CB . LEU A 1 448 ? -2.102 54.712 56.884 1.00 15.68 ? 441 LEU A CB 1 ATOM 3173 C CG . LEU A 1 448 ? -3.545 54.228 56.675 1.00 15.43 ? 441 LEU A CG 1 ATOM 3174 C CD1 . LEU A 1 448 ? -3.626 52.761 57.098 1.00 19.89 ? 441 LEU A CD1 1 ATOM 3175 C CD2 . LEU A 1 448 ? -4.538 55.061 57.471 1.00 16.82 ? 441 LEU A CD2 1 ATOM 3176 N N . LEU A 1 449 ? 0.337 56.120 55.550 1.00 15.11 ? 442 LEU A N 1 ATOM 3177 C CA . LEU A 1 449 ? 1.793 56.262 55.535 1.00 16.82 ? 442 LEU A CA 1 ATOM 3178 C C . LEU A 1 449 ? 2.206 57.721 55.510 1.00 16.18 ? 442 LEU A C 1 ATOM 3179 O O . LEU A 1 449 ? 3.149 58.120 56.207 1.00 18.96 ? 442 LEU A O 1 ATOM 3180 C CB . LEU A 1 449 ? 2.388 55.511 54.340 1.00 16.40 ? 442 LEU A CB 1 ATOM 3181 C CG . LEU A 1 449 ? 2.214 53.989 54.409 1.00 14.23 ? 442 LEU A CG 1 ATOM 3182 C CD1 . LEU A 1 449 ? 2.514 53.374 53.036 1.00 14.93 ? 442 LEU A CD1 1 ATOM 3183 C CD2 . LEU A 1 449 ? 3.094 53.367 55.495 1.00 20.02 ? 442 LEU A CD2 1 ATOM 3184 N N A GLN A 1 450 ? 1.554 58.545 54.713 0.60 16.90 ? 443 GLN A N 1 ATOM 3185 N N B GLN A 1 450 ? 1.466 58.492 54.697 0.40 16.72 ? 443 GLN A N 1 ATOM 3186 C CA A GLN A 1 450 ? 2.051 59.903 54.673 0.60 16.35 ? 443 GLN A CA 1 ATOM 3187 C CA B GLN A 1 450 ? 1.616 59.943 54.508 0.40 16.54 ? 443 GLN A CA 1 ATOM 3188 C C A GLN A 1 450 ? 1.704 60.686 55.955 0.60 16.48 ? 443 GLN A C 1 ATOM 3189 C C B GLN A 1 450 ? 1.572 60.710 55.816 0.40 16.15 ? 443 GLN A C 1 ATOM 3190 O O A GLN A 1 450 ? 2.465 61.568 56.337 0.60 16.03 ? 443 GLN A O 1 ATOM 3191 O O B GLN A 1 450 ? 2.371 61.614 56.053 0.40 15.84 ? 443 GLN A O 1 ATOM 3192 C CB A GLN A 1 450 ? 1.650 60.612 53.395 0.60 14.57 ? 443 GLN A CB 1 ATOM 3193 C CB B GLN A 1 450 ? 0.472 60.474 53.636 0.40 15.99 ? 443 GLN A CB 1 ATOM 3194 C CG A GLN A 1 450 ? 0.159 60.834 53.235 0.60 13.92 ? 443 GLN A CG 1 ATOM 3195 C CG B GLN A 1 450 ? 0.247 61.965 53.781 0.40 15.78 ? 443 GLN A CG 1 ATOM 3196 C CD A GLN A 1 450 ? -0.173 61.177 51.805 0.60 15.91 ? 443 GLN A CD 1 ATOM 3197 C CD B GLN A 1 450 ? 1.191 62.760 52.930 0.40 14.68 ? 443 GLN A CD 1 ATOM 3198 O OE1 A GLN A 1 450 ? 0.692 61.104 50.907 0.60 17.55 ? 443 GLN A OE1 1 ATOM 3199 O OE1 B GLN A 1 450 ? 1.659 62.249 51.910 0.40 14.68 ? 443 GLN A OE1 1 ATOM 3200 N NE2 A GLN A 1 450 ? -1.410 61.568 51.575 0.60 16.16 ? 443 GLN A NE2 1 ATOM 3201 N NE2 B GLN A 1 450 ? 1.478 64.021 53.329 0.40 9.80 ? 443 GLN A NE2 1 ATOM 3202 N N . GLU A 1 451 ? 0.612 60.338 56.657 1.00 15.27 ? 444 GLU A N 1 ATOM 3203 C CA . GLU A 1 451 ? 0.313 61.089 57.887 1.00 15.68 ? 444 GLU A CA 1 ATOM 3204 C C . GLU A 1 451 ? 0.950 60.506 59.138 1.00 16.22 ? 444 GLU A C 1 ATOM 3205 O O . GLU A 1 451 ? 1.073 61.217 60.153 1.00 16.12 ? 444 GLU A O 1 ATOM 3206 C CB . GLU A 1 451 ? -1.213 61.299 58.061 1.00 16.74 ? 444 GLU A CB 1 ATOM 3207 C CG . GLU A 1 451 ? -1.898 61.874 56.822 1.00 17.93 ? 444 GLU A CG 1 ATOM 3208 C CD . GLU A 1 451 ? -1.298 63.185 56.305 1.00 19.16 ? 444 GLU A CD 1 ATOM 3209 O OE1 . GLU A 1 451 ? -0.340 63.730 56.910 1.00 18.51 ? 444 GLU A OE1 1 ATOM 3210 O OE2 . GLU A 1 451 ? -1.783 63.672 55.256 1.00 20.79 ? 444 GLU A OE2 1 ATOM 3211 N N . ARG A 1 452 ? 1.398 59.244 59.052 1.00 14.37 ? 445 ARG A N 1 ATOM 3212 C CA . ARG A 1 452 ? 1.841 58.510 60.234 1.00 15.10 ? 445 ARG A CA 1 ATOM 3213 C C . ARG A 1 452 ? 3.253 57.909 60.111 1.00 15.61 ? 445 ARG A C 1 ATOM 3214 O O . ARG A 1 452 ? 3.785 57.411 61.087 1.00 16.97 ? 445 ARG A O 1 ATOM 3215 C CB . ARG A 1 452 ? 0.848 57.380 60.565 1.00 14.79 ? 445 ARG A CB 1 ATOM 3216 C CG . ARG A 1 452 ? -0.576 57.900 60.851 1.00 15.90 ? 445 ARG A CG 1 ATOM 3217 C CD . ARG A 1 452 ? -1.524 56.737 61.102 1.00 16.74 ? 445 ARG A CD 1 ATOM 3218 N NE . ARG A 1 452 ? -2.916 57.167 61.051 1.00 17.46 ? 445 ARG A NE 1 ATOM 3219 C CZ . ARG A 1 452 ? -3.952 56.342 61.035 1.00 16.12 ? 445 ARG A CZ 1 ATOM 3220 N NH1 . ARG A 1 452 ? -3.756 55.019 61.083 1.00 17.01 ? 445 ARG A NH1 1 ATOM 3221 N NH2 . ARG A 1 452 ? -5.187 56.850 60.946 1.00 16.23 ? 445 ARG A NH2 1 ATOM 3222 N N . GLY A 1 453 ? 3.832 57.937 58.917 1.00 16.62 ? 446 GLY A N 1 ATOM 3223 C CA . GLY A 1 453 ? 5.097 57.219 58.646 1.00 17.10 ? 446 GLY A CA 1 ATOM 3224 C C . GLY A 1 453 ? 6.295 58.003 59.160 1.00 16.32 ? 446 GLY A C 1 ATOM 3225 O O . GLY A 1 453 ? 6.639 59.087 58.641 1.00 17.86 ? 446 GLY A O 1 ATOM 3226 N N . VAL A 1 454 ? 6.954 57.448 60.170 1.00 16.12 ? 447 VAL A N 1 ATOM 3227 C CA . VAL A 1 454 ? 8.155 58.061 60.720 1.00 17.24 ? 447 VAL A CA 1 ATOM 3228 C C . VAL A 1 454 ? 9.388 57.761 59.845 1.00 17.59 ? 447 VAL A C 1 ATOM 3229 O O . VAL A 1 454 ? 10.152 58.679 59.453 1.00 16.64 ? 447 VAL A O 1 ATOM 3230 C CB . VAL A 1 454 ? 8.360 57.589 62.184 1.00 16.93 ? 447 VAL A CB 1 ATOM 3231 C CG1 . VAL A 1 454 ? 9.750 57.945 62.671 1.00 19.15 ? 447 VAL A CG1 1 ATOM 3232 C CG2 . VAL A 1 454 ? 7.273 58.186 63.093 1.00 20.10 ? 447 VAL A CG2 1 ATOM 3233 N N . ALA A 1 455 ? 9.587 56.474 59.526 1.00 16.36 ? 448 ALA A N 1 ATOM 3234 C CA . ALA A 1 455 ? 10.802 56.050 58.837 1.00 14.47 ? 448 ALA A CA 1 ATOM 3235 C C . ALA A 1 455 ? 10.585 54.686 58.240 1.00 15.31 ? 448 ALA A C 1 ATOM 3236 O O . ALA A 1 455 ? 9.746 53.895 58.745 1.00 17.14 ? 448 ALA A O 1 ATOM 3237 C CB . ALA A 1 455 ? 11.966 55.981 59.845 1.00 15.74 ? 448 ALA A CB 1 ATOM 3238 N N . TYR A 1 456 ? 11.364 54.411 57.190 1.00 16.57 ? 449 TYR A N 1 ATOM 3239 C CA . TYR A 1 456 ? 11.400 53.108 56.554 1.00 15.39 ? 449 TYR A CA 1 ATOM 3240 C C . TYR A 1 456 ? 12.869 52.659 56.504 1.00 15.57 ? 449 TYR A C 1 ATOM 3241 O O . TYR A 1 456 ? 13.731 53.373 55.966 1.00 16.63 ? 449 TYR A O 1 ATOM 3242 C CB . TYR A 1 456 ? 10.802 53.178 55.132 1.00 15.80 ? 449 TYR A CB 1 ATOM 3243 C CG . TYR A 1 456 ? 10.912 51.845 54.422 1.00 15.06 ? 449 TYR A CG 1 ATOM 3244 C CD1 . TYR A 1 456 ? 9.923 50.852 54.591 1.00 15.54 ? 449 TYR A CD1 1 ATOM 3245 C CD2 . TYR A 1 456 ? 12.004 51.559 53.601 1.00 14.85 ? 449 TYR A CD2 1 ATOM 3246 C CE1 . TYR A 1 456 ? 10.034 49.618 53.971 1.00 16.09 ? 449 TYR A CE1 1 ATOM 3247 C CE2 . TYR A 1 456 ? 12.126 50.328 52.961 1.00 15.91 ? 449 TYR A CE2 1 ATOM 3248 C CZ . TYR A 1 456 ? 11.128 49.367 53.140 1.00 16.38 ? 449 TYR A CZ 1 ATOM 3249 O OH . TYR A 1 456 ? 11.231 48.148 52.498 1.00 16.96 ? 449 TYR A OH 1 ATOM 3250 N N . ILE A 1 457 ? 13.141 51.483 57.066 1.00 15.21 ? 450 ILE A N 1 ATOM 3251 C CA . ILE A 1 457 ? 14.460 50.843 56.992 1.00 14.93 ? 450 ILE A CA 1 ATOM 3252 C C . ILE A 1 457 ? 14.306 49.614 56.089 1.00 15.58 ? 450 ILE A C 1 ATOM 3253 O O . ILE A 1 457 ? 13.508 48.713 56.371 1.00 16.82 ? 450 ILE A O 1 ATOM 3254 C CB . ILE A 1 457 ? 14.967 50.435 58.409 1.00 15.55 ? 450 ILE A CB 1 ATOM 3255 C CG1 . ILE A 1 457 ? 15.036 51.667 59.353 1.00 16.65 ? 450 ILE A CG1 1 ATOM 3256 C CG2 . ILE A 1 457 ? 16.306 49.684 58.332 1.00 17.62 ? 450 ILE A CG2 1 ATOM 3257 C CD1 . ILE A 1 457 ? 15.928 52.797 58.841 1.00 16.59 ? 450 ILE A CD1 1 ATOM 3258 N N . ASN A 1 458 ? 15.041 49.598 54.990 1.00 15.42 ? 451 ASN A N 1 ATOM 3259 C CA . ASN A 1 458 ? 15.007 48.467 54.075 1.00 15.22 ? 451 ASN A CA 1 ATOM 3260 C C . ASN A 1 458 ? 15.842 47.292 54.606 1.00 17.22 ? 451 ASN A C 1 ATOM 3261 O O . ASN A 1 458 ? 16.693 47.464 55.493 1.00 19.65 ? 451 ASN A O 1 ATOM 3262 C CB . ASN A 1 458 ? 15.578 48.895 52.719 1.00 15.84 ? 451 ASN A CB 1 ATOM 3263 C CG . ASN A 1 458 ? 15.015 48.082 51.569 1.00 15.44 ? 451 ASN A CG 1 ATOM 3264 O OD1 . ASN A 1 458 ? 13.802 47.908 51.453 1.00 18.28 ? 451 ASN A OD1 1 ATOM 3265 N ND2 . ASN A 1 458 ? 15.906 47.540 50.726 1.00 17.61 ? 451 ASN A ND2 1 ATOM 3266 N N . ALA A 1 459 ? 15.622 46.103 54.044 1.00 16.89 ? 452 ALA A N 1 ATOM 3267 C CA . ALA A 1 459 ? 16.347 44.916 54.514 1.00 17.52 ? 452 ALA A CA 1 ATOM 3268 C C . ALA A 1 459 ? 16.427 43.874 53.403 1.00 17.31 ? 452 ALA A C 1 ATOM 3269 O O . ALA A 1 459 ? 15.970 42.742 53.547 1.00 18.87 ? 452 ALA A O 1 ATOM 3270 C CB . ALA A 1 459 ? 15.676 44.355 55.776 1.00 18.43 ? 452 ALA A CB 1 ATOM 3271 N N . ASP A 1 460 ? 16.992 44.280 52.275 1.00 17.13 ? 453 ASP A N 1 ATOM 3272 C CA . ASP A 1 460 ? 17.384 43.298 51.249 1.00 16.40 ? 453 ASP A CA 1 ATOM 3273 C C . ASP A 1 460 ? 18.754 42.718 51.674 1.00 16.59 ? 453 ASP A C 1 ATOM 3274 O O . ASP A 1 460 ? 19.111 42.762 52.857 1.00 18.73 ? 453 ASP A O 1 ATOM 3275 C CB . ASP A 1 460 ? 17.402 43.936 49.852 1.00 17.82 ? 453 ASP A CB 1 ATOM 3276 C CG . ASP A 1 460 ? 17.266 42.909 48.718 1.00 18.67 ? 453 ASP A CG 1 ATOM 3277 O OD1 . ASP A 1 460 ? 17.299 41.690 48.994 1.00 22.11 ? 453 ASP A OD1 1 ATOM 3278 O OD2 . ASP A 1 460 ? 17.124 43.329 47.536 1.00 20.33 ? 453 ASP A OD2 1 ATOM 3279 N N . SER A 1 461 ? 19.502 42.188 50.715 1.00 17.56 ? 454 SER A N 1 ATOM 3280 C CA A SER A 1 461 ? 20.768 41.493 50.996 0.70 17.99 ? 454 SER A CA 1 ATOM 3281 C CA B SER A 1 461 ? 20.748 41.475 51.012 0.30 18.13 ? 454 SER A CA 1 ATOM 3282 C C . SER A 1 461 ? 21.595 42.112 52.128 1.00 18.13 ? 454 SER A C 1 ATOM 3283 O O . SER A 1 461 ? 21.902 43.315 52.109 1.00 18.50 ? 454 SER A O 1 ATOM 3284 C CB A SER A 1 461 ? 21.616 41.435 49.737 0.70 17.51 ? 454 SER A CB 1 ATOM 3285 C CB B SER A 1 461 ? 21.573 41.285 49.741 0.30 21.05 ? 454 SER A CB 1 ATOM 3286 O OG A SER A 1 461 ? 20.840 41.001 48.647 0.70 12.65 ? 454 SER A OG 1 ATOM 3287 O OG B SER A 1 461 ? 21.910 42.529 49.163 0.30 23.86 ? 454 SER A OG 1 ATOM 3288 N N . SER A 1 462 ? 21.969 41.292 53.107 1.00 18.17 ? 455 SER A N 1 ATOM 3289 C CA . SER A 1 462 ? 22.763 41.783 54.245 1.00 19.65 ? 455 SER A CA 1 ATOM 3290 C C . SER A 1 462 ? 24.241 41.907 53.913 1.00 19.50 ? 455 SER A C 1 ATOM 3291 O O . SER A 1 462 ? 24.980 42.616 54.587 1.00 20.22 ? 455 SER A O 1 ATOM 3292 C CB . SER A 1 462 ? 22.601 40.852 55.436 1.00 20.88 ? 455 SER A CB 1 ATOM 3293 O OG . SER A 1 462 ? 21.276 40.938 55.912 1.00 22.21 ? 455 SER A OG 1 ATOM 3294 N N . ILE A 1 463 ? 24.681 41.190 52.885 1.00 20.58 ? 456 ILE A N 1 ATOM 3295 C CA . ILE A 1 463 ? 26.093 41.162 52.517 1.00 20.97 ? 456 ILE A CA 1 ATOM 3296 C C . ILE A 1 463 ? 26.253 41.202 51.001 1.00 22.45 ? 456 ILE A C 1 ATOM 3297 O O . ILE A 1 463 ? 25.488 40.571 50.272 1.00 25.38 ? 456 ILE A O 1 ATOM 3298 C CB . ILE A 1 463 ? 26.778 39.873 53.044 1.00 22.91 ? 456 ILE A CB 1 ATOM 3299 C CG1 . ILE A 1 463 ? 25.925 38.621 52.696 1.00 26.78 ? 456 ILE A CG1 1 ATOM 3300 C CG2 . ILE A 1 463 ? 26.994 39.964 54.541 1.00 23.82 ? 456 ILE A CG2 1 ATOM 3301 C CD1 . ILE A 1 463 ? 26.719 37.385 52.421 1.00 32.45 ? 456 ILE A CD1 1 ATOM 3302 N N . GLU A 1 464 ? 27.250 41.937 50.529 1.00 23.07 ? 457 GLU A N 1 ATOM 3303 C CA . GLU A 1 464 ? 27.664 41.857 49.120 1.00 22.71 ? 457 GLU A CA 1 ATOM 3304 C C . GLU A 1 464 ? 29.195 41.788 49.107 1.00 23.83 ? 457 GLU A C 1 ATOM 3305 O O . GLU A 1 464 ? 29.828 41.953 48.069 1.00 23.97 ? 457 GLU A O 1 ATOM 3306 C CB . GLU A 1 464 ? 27.122 43.049 48.295 1.00 22.45 ? 457 GLU A CB 1 ATOM 3307 C CG . GLU A 1 464 ? 27.661 44.419 48.753 1.00 23.02 ? 457 GLU A CG 1 ATOM 3308 C CD . GLU A 1 464 ? 26.965 45.628 48.129 1.00 27.29 ? 457 GLU A CD 1 ATOM 3309 O OE1 . GLU A 1 464 ? 25.887 45.467 47.505 1.00 25.59 ? 457 GLU A OE1 1 ATOM 3310 O OE2 . GLU A 1 464 ? 27.495 46.765 48.281 1.00 26.55 ? 457 GLU A OE2 1 ATOM 3311 N N . GLY A 1 465 ? 29.761 41.517 50.286 1.00 23.49 ? 458 GLY A N 1 ATOM 3312 C CA . GLY A 1 465 ? 31.192 41.500 50.531 1.00 24.24 ? 458 GLY A CA 1 ATOM 3313 C C . GLY A 1 465 ? 31.432 41.331 52.024 1.00 24.24 ? 458 GLY A C 1 ATOM 3314 O O . GLY A 1 465 ? 30.482 41.203 52.812 1.00 26.16 ? 458 GLY A O 1 ATOM 3315 N N . ASN A 1 466 ? 32.698 41.325 52.423 1.00 23.92 ? 459 ASN A N 1 ATOM 3316 C CA . ASN A 1 466 ? 33.044 41.102 53.822 1.00 24.84 ? 459 ASN A CA 1 ATOM 3317 C C . ASN A 1 466 ? 34.065 42.121 54.324 1.00 24.97 ? 459 ASN A C 1 ATOM 3318 O O . ASN A 1 466 ? 34.809 41.856 55.263 1.00 26.82 ? 459 ASN A O 1 ATOM 3319 C CB . ASN A 1 466 ? 33.542 39.643 54.029 1.00 26.96 ? 459 ASN A CB 1 ATOM 3320 C CG . ASN A 1 466 ? 34.853 39.343 53.297 1.00 28.27 ? 459 ASN A CG 1 ATOM 3321 O OD1 . ASN A 1 466 ? 35.435 40.218 52.661 1.00 30.05 ? 459 ASN A OD1 1 ATOM 3322 N ND2 . ASN A 1 466 ? 35.329 38.094 53.391 1.00 34.57 ? 459 ASN A ND2 1 ATOM 3323 N N . TYR A 1 467 ? 34.087 43.293 53.696 1.00 24.58 ? 460 TYR A N 1 ATOM 3324 C CA . TYR A 1 467 ? 35.133 44.269 53.968 1.00 23.99 ? 460 TYR A CA 1 ATOM 3325 C C . TYR A 1 467 ? 34.693 45.302 55.006 1.00 24.65 ? 460 TYR A C 1 ATOM 3326 O O . TYR A 1 467 ? 35.377 45.503 56.009 1.00 26.08 ? 460 TYR A O 1 ATOM 3327 C CB . TYR A 1 467 ? 35.560 44.971 52.681 1.00 23.73 ? 460 TYR A CB 1 ATOM 3328 C CG . TYR A 1 467 ? 36.666 45.985 52.878 1.00 28.66 ? 460 TYR A CG 1 ATOM 3329 C CD1 . TYR A 1 467 ? 37.941 45.584 53.292 1.00 30.32 ? 460 TYR A CD1 1 ATOM 3330 C CD2 . TYR A 1 467 ? 36.441 47.338 52.646 1.00 30.49 ? 460 TYR A CD2 1 ATOM 3331 C CE1 . TYR A 1 467 ? 38.964 46.505 53.476 1.00 32.16 ? 460 TYR A CE1 1 ATOM 3332 C CE2 . TYR A 1 467 ? 37.454 48.270 52.819 1.00 31.47 ? 460 TYR A CE2 1 ATOM 3333 C CZ . TYR A 1 467 ? 38.710 47.849 53.231 1.00 35.95 ? 460 TYR A CZ 1 ATOM 3334 O OH . TYR A 1 467 ? 39.707 48.778 53.400 1.00 40.47 ? 460 TYR A OH 1 ATOM 3335 N N . THR A 1 468 ? 33.579 45.987 54.754 1.00 23.15 ? 461 THR A N 1 ATOM 3336 C CA . THR A 1 468 ? 33.146 47.030 55.685 1.00 22.12 ? 461 THR A CA 1 ATOM 3337 C C . THR A 1 468 ? 31.655 47.323 55.528 1.00 22.39 ? 461 THR A C 1 ATOM 3338 O O . THR A 1 468 ? 30.985 46.754 54.670 1.00 22.49 ? 461 THR A O 1 ATOM 3339 C CB . THR A 1 468 ? 33.999 48.333 55.554 1.00 22.83 ? 461 THR A CB 1 ATOM 3340 O OG1 . THR A 1 468 ? 33.820 49.158 56.718 1.00 25.00 ? 461 THR A OG1 1 ATOM 3341 C CG2 . THR A 1 468 ? 33.611 49.134 54.311 1.00 23.33 ? 461 THR A CG2 1 ATOM 3342 N N . LEU A 1 469 ? 31.140 48.198 56.384 1.00 21.87 ? 462 LEU A N 1 ATOM 3343 C CA . LEU A 1 469 ? 29.752 48.607 56.313 1.00 21.64 ? 462 LEU A CA 1 ATOM 3344 C C . LEU A 1 469 ? 29.495 49.542 55.149 1.00 21.96 ? 462 LEU A C 1 ATOM 3345 O O . LEU A 1 469 ? 30.379 50.313 54.756 1.00 22.97 ? 462 LEU A O 1 ATOM 3346 C CB . LEU A 1 469 ? 29.357 49.299 57.623 1.00 22.07 ? 462 LEU A CB 1 ATOM 3347 C CG . LEU A 1 469 ? 27.855 49.522 57.841 1.00 20.12 ? 462 LEU A CG 1 ATOM 3348 C CD1 . LEU A 1 469 ? 27.166 48.184 58.118 1.00 21.49 ? 462 LEU A CD1 1 ATOM 3349 C CD2 . LEU A 1 469 ? 27.700 50.476 59.014 1.00 21.35 ? 462 LEU A CD2 1 ATOM 3350 N N . ARG A 1 470 ? 28.286 49.449 54.607 1.00 19.41 ? 463 ARG A N 1 ATOM 3351 C CA . ARG A 1 470 ? 27.775 50.389 53.624 1.00 20.20 ? 463 ARG A CA 1 ATOM 3352 C C . ARG A 1 470 ? 26.435 50.894 54.152 1.00 19.67 ? 463 ARG A C 1 ATOM 3353 O O . ARG A 1 470 ? 25.576 50.091 54.522 1.00 20.30 ? 463 ARG A O 1 ATOM 3354 C CB . ARG A 1 470 ? 27.593 49.694 52.253 1.00 22.74 ? 463 ARG A CB 1 ATOM 3355 C CG . ARG A 1 470 ? 26.816 50.538 51.255 1.00 24.43 ? 463 ARG A CG 1 ATOM 3356 C CD . ARG A 1 470 ? 26.562 49.787 49.967 1.00 27.70 ? 463 ARG A CD 1 ATOM 3357 N NE . ARG A 1 470 ? 25.490 50.417 49.195 1.00 30.39 ? 463 ARG A NE 1 ATOM 3358 C CZ . ARG A 1 470 ? 24.826 49.811 48.208 1.00 33.56 ? 463 ARG A CZ 1 ATOM 3359 N NH1 . ARG A 1 470 ? 25.125 48.555 47.868 1.00 37.11 ? 463 ARG A NH1 1 ATOM 3360 N NH2 . ARG A 1 470 ? 23.852 50.451 47.561 1.00 35.09 ? 463 ARG A NH2 1 ATOM 3361 N N . VAL A 1 471 ? 26.262 52.216 54.216 1.00 18.86 ? 464 VAL A N 1 ATOM 3362 C CA . VAL A 1 471 ? 24.972 52.810 54.580 1.00 17.76 ? 464 VAL A CA 1 ATOM 3363 C C . VAL A 1 471 ? 24.581 53.825 53.500 1.00 18.46 ? 464 VAL A C 1 ATOM 3364 O O . VAL A 1 471 ? 25.417 54.646 53.104 1.00 19.78 ? 464 VAL A O 1 ATOM 3365 C CB . VAL A 1 471 ? 25.034 53.523 55.965 1.00 18.49 ? 464 VAL A CB 1 ATOM 3366 C CG1 . VAL A 1 471 ? 23.704 54.187 56.292 1.00 19.38 ? 464 VAL A CG1 1 ATOM 3367 C CG2 . VAL A 1 471 ? 25.445 52.557 57.087 1.00 21.12 ? 464 VAL A CG2 1 ATOM 3368 N N . ASP A 1 472 ? 23.341 53.738 53.003 1.00 17.72 ? 465 ASP A N 1 ATOM 3369 C CA . ASP A 1 472 ? 22.747 54.758 52.141 1.00 17.55 ? 465 ASP A CA 1 ATOM 3370 C C . ASP A 1 472 ? 21.483 55.212 52.883 1.00 17.88 ? 465 ASP A C 1 ATOM 3371 O O . ASP A 1 472 ? 20.650 54.385 53.254 1.00 17.42 ? 465 ASP A O 1 ATOM 3372 C CB . ASP A 1 472 ? 22.286 54.222 50.755 1.00 18.09 ? 465 ASP A CB 1 ATOM 3373 C CG . ASP A 1 472 ? 23.326 53.368 50.006 1.00 22.46 ? 465 ASP A CG 1 ATOM 3374 O OD1 . ASP A 1 472 ? 22.943 52.786 48.942 1.00 27.36 ? 465 ASP A OD1 1 ATOM 3375 O OD2 . ASP A 1 472 ? 24.507 53.291 50.389 1.00 22.62 ? 465 ASP A OD2 1 ATOM 3376 N N . CYS A 1 473 ? 21.325 56.511 53.097 1.00 18.25 ? 466 CYS A N 1 ATOM 3377 C CA . CYS A 1 473 ? 20.148 56.997 53.815 1.00 17.50 ? 466 CYS A CA 1 ATOM 3378 C C . CYS A 1 473 ? 19.942 58.480 53.625 1.00 16.86 ? 466 CYS A C 1 ATOM 3379 O O . CYS A 1 473 ? 20.812 59.189 53.107 1.00 20.58 ? 466 CYS A O 1 ATOM 3380 C CB . CYS A 1 473 ? 20.251 56.688 55.333 1.00 17.81 ? 466 CYS A CB 1 ATOM 3381 S SG . CYS A 1 473 ? 21.589 57.549 56.206 1.00 19.51 ? 466 CYS A SG 1 ATOM 3382 N N . THR A 1 474 ? 18.765 58.931 54.026 1.00 16.34 ? 467 THR A N 1 ATOM 3383 C CA . THR A 1 474 ? 18.475 60.342 54.144 1.00 15.97 ? 467 THR A CA 1 ATOM 3384 C C . THR A 1 474 ? 19.460 61.036 55.101 1.00 16.62 ? 467 THR A C 1 ATOM 3385 O O . THR A 1 474 ? 19.861 60.449 56.115 1.00 17.24 ? 467 THR A O 1 ATOM 3386 C CB . THR A 1 474 ? 17.030 60.579 54.639 1.00 16.19 ? 467 THR A CB 1 ATOM 3387 O OG1 . THR A 1 474 ? 16.859 61.981 54.850 1.00 16.37 ? 467 THR A OG1 1 ATOM 3388 C CG2 . THR A 1 474 ? 16.726 59.824 55.961 1.00 17.28 ? 467 THR A CG2 1 ATOM 3389 N N . PRO A 1 475 ? 19.828 62.298 54.805 1.00 16.54 ? 468 PRO A N 1 ATOM 3390 C CA . PRO A 1 475 ? 20.649 63.065 55.760 1.00 17.57 ? 468 PRO A CA 1 ATOM 3391 C C . PRO A 1 475 ? 20.035 63.087 57.162 1.00 18.18 ? 468 PRO A C 1 ATOM 3392 O O . PRO A 1 475 ? 20.768 63.213 58.141 1.00 18.41 ? 468 PRO A O 1 ATOM 3393 C CB . PRO A 1 475 ? 20.661 64.480 55.158 1.00 18.79 ? 468 PRO A CB 1 ATOM 3394 C CG . PRO A 1 475 ? 20.529 64.230 53.693 1.00 18.16 ? 468 PRO A CG 1 ATOM 3395 C CD . PRO A 1 475 ? 19.562 63.084 53.575 1.00 17.35 ? 468 PRO A CD 1 ATOM 3396 N N . LEU A 1 476 ? 18.704 62.962 57.255 1.00 17.80 ? 469 LEU A N 1 ATOM 3397 C CA . LEU A 1 476 ? 18.047 62.961 58.582 1.00 17.38 ? 469 LEU A CA 1 ATOM 3398 C C . LEU A 1 476 ? 18.509 61.838 59.504 1.00 18.02 ? 469 LEU A C 1 ATOM 3399 O O . LEU A 1 476 ? 18.407 61.968 60.715 1.00 20.51 ? 469 LEU A O 1 ATOM 3400 C CB . LEU A 1 476 ? 16.521 62.934 58.471 1.00 17.69 ? 469 LEU A CB 1 ATOM 3401 C CG . LEU A 1 476 ? 15.929 64.194 57.871 1.00 15.89 ? 469 LEU A CG 1 ATOM 3402 C CD1 . LEU A 1 476 ? 14.418 64.049 57.838 1.00 19.04 ? 469 LEU A CD1 1 ATOM 3403 C CD2 . LEU A 1 476 ? 16.335 65.421 58.709 1.00 17.27 ? 469 LEU A CD2 1 ATOM 3404 N N . MET A 1 477 ? 19.030 60.756 58.942 1.00 17.89 ? 470 MET A N 1 ATOM 3405 C CA . MET A 1 477 ? 19.510 59.635 59.755 1.00 17.88 ? 470 MET A CA 1 ATOM 3406 C C . MET A 1 477 ? 21.033 59.591 59.961 1.00 19.41 ? 470 MET A C 1 ATOM 3407 O O . MET A 1 477 ? 21.534 58.664 60.613 1.00 18.64 ? 470 MET A O 1 ATOM 3408 C CB . MET A 1 477 ? 19.026 58.290 59.158 1.00 18.38 ? 470 MET A CB 1 ATOM 3409 C CG . MET A 1 477 ? 17.532 58.037 59.279 1.00 20.27 ? 470 MET A CG 1 ATOM 3410 S SD . MET A 1 477 ? 17.193 56.494 58.413 1.00 23.32 ? 470 MET A SD 1 ATOM 3411 C CE . MET A 1 477 ? 15.412 56.555 58.265 1.00 22.95 ? 470 MET A CE 1 ATOM 3412 N N . TYR A 1 478 ? 21.787 60.560 59.426 1.00 18.32 ? 471 TYR A N 1 ATOM 3413 C CA . TYR A 1 478 ? 23.256 60.485 59.559 1.00 19.70 ? 471 TYR A CA 1 ATOM 3414 C C . TYR A 1 478 ? 23.710 60.386 61.015 1.00 20.37 ? 471 TYR A C 1 ATOM 3415 O O . TYR A 1 478 ? 24.554 59.544 61.369 1.00 20.36 ? 471 TYR A O 1 ATOM 3416 C CB . TYR A 1 478 ? 23.958 61.700 58.953 1.00 19.06 ? 471 TYR A CB 1 ATOM 3417 C CG . TYR A 1 478 ? 23.951 61.833 57.449 1.00 19.05 ? 471 TYR A CG 1 ATOM 3418 C CD1 . TYR A 1 478 ? 23.453 60.817 56.603 1.00 18.55 ? 471 TYR A CD1 1 ATOM 3419 C CD2 . TYR A 1 478 ? 24.440 62.998 56.862 1.00 20.48 ? 471 TYR A CD2 1 ATOM 3420 C CE1 . TYR A 1 478 ? 23.441 60.992 55.203 1.00 20.39 ? 471 TYR A CE1 1 ATOM 3421 C CE2 . TYR A 1 478 ? 24.437 63.175 55.490 1.00 20.10 ? 471 TYR A CE2 1 ATOM 3422 C CZ . TYR A 1 478 ? 23.949 62.179 54.663 1.00 21.22 ? 471 TYR A CZ 1 ATOM 3423 O OH . TYR A 1 478 ? 23.964 62.404 53.295 1.00 21.30 ? 471 TYR A OH 1 ATOM 3424 N N . SER A 1 479 ? 23.165 61.271 61.856 1.00 20.84 ? 472 SER A N 1 ATOM 3425 C CA . SER A 1 479 ? 23.601 61.350 63.257 1.00 22.19 ? 472 SER A CA 1 ATOM 3426 C C . SER A 1 479 ? 23.216 60.098 64.014 1.00 21.56 ? 472 SER A C 1 ATOM 3427 O O . SER A 1 479 ? 24.012 59.573 64.800 1.00 21.97 ? 472 SER A O 1 ATOM 3428 C CB . SER A 1 479 ? 23.033 62.598 63.923 1.00 22.30 ? 472 SER A CB 1 ATOM 3429 O OG A SER A 1 479 ? 23.711 63.747 63.417 0.50 26.17 ? 472 SER A OG 1 ATOM 3430 O OG B SER A 1 479 ? 23.495 62.722 65.268 0.50 19.39 ? 472 SER A OG 1 ATOM 3431 N N . LEU A 1 480 ? 22.008 59.601 63.746 1.00 21.41 ? 473 LEU A N 1 ATOM 3432 C CA . LEU A 1 480 ? 21.552 58.316 64.294 1.00 22.48 ? 473 LEU A CA 1 ATOM 3433 C C . LEU A 1 480 ? 22.540 57.193 63.950 1.00 21.68 ? 473 LEU A C 1 ATOM 3434 O O . LEU A 1 480 ? 22.923 56.388 64.826 1.00 21.52 ? 473 LEU A O 1 ATOM 3435 C CB . LEU A 1 480 ? 20.149 57.967 63.768 1.00 21.88 ? 473 LEU A CB 1 ATOM 3436 C CG . LEU A 1 480 ? 19.680 56.503 63.904 1.00 22.69 ? 473 LEU A CG 1 ATOM 3437 C CD1 . LEU A 1 480 ? 19.488 56.134 65.373 1.00 25.65 ? 473 LEU A CD1 1 ATOM 3438 C CD2 . LEU A 1 480 ? 18.380 56.324 63.155 1.00 25.97 ? 473 LEU A CD2 1 ATOM 3439 N N . VAL A 1 481 ? 22.934 57.123 62.678 1.00 20.20 ? 474 VAL A N 1 ATOM 3440 C CA . VAL A 1 481 ? 23.853 56.076 62.206 1.00 19.63 ? 474 VAL A CA 1 ATOM 3441 C C . VAL A 1 481 ? 25.248 56.217 62.839 1.00 20.56 ? 474 VAL A C 1 ATOM 3442 O O . VAL A 1 481 ? 25.821 55.222 63.307 1.00 22.70 ? 474 VAL A O 1 ATOM 3443 C CB . VAL A 1 481 ? 23.927 56.050 60.665 1.00 21.45 ? 474 VAL A CB 1 ATOM 3444 C CG1 . VAL A 1 481 ? 25.043 55.122 60.191 1.00 23.42 ? 474 VAL A CG1 1 ATOM 3445 C CG2 . VAL A 1 481 ? 22.595 55.589 60.081 1.00 22.44 ? 474 VAL A CG2 1 ATOM 3446 N N . HIS A 1 482 ? 25.787 57.438 62.878 1.00 21.52 ? 475 HIS A N 1 ATOM 3447 C CA . HIS A 1 482 ? 27.072 57.662 63.567 1.00 23.86 ? 475 HIS A CA 1 ATOM 3448 C C . HIS A 1 482 ? 26.995 57.202 65.009 1.00 22.19 ? 475 HIS A C 1 ATOM 3449 O O . HIS A 1 482 ? 27.850 56.435 65.476 1.00 22.88 ? 475 HIS A O 1 ATOM 3450 C CB . HIS A 1 482 ? 27.498 59.132 63.527 1.00 23.53 ? 475 HIS A CB 1 ATOM 3451 C CG . HIS A 1 482 ? 27.790 59.651 62.147 1.00 27.85 ? 475 HIS A CG 1 ATOM 3452 N ND1 . HIS A 1 482 ? 27.763 60.962 61.853 1.00 38.17 ? 475 HIS A ND1 1 ATOM 3453 C CD2 . HIS A 1 482 ? 28.068 58.989 60.956 1.00 28.93 ? 475 HIS A CD2 1 ATOM 3454 C CE1 . HIS A 1 482 ? 28.036 61.134 60.543 1.00 37.38 ? 475 HIS A CE1 1 ATOM 3455 N NE2 . HIS A 1 482 ? 28.221 59.928 59.997 1.00 29.70 ? 475 HIS A NE2 1 ATOM 3456 N N . ASN A 1 483 ? 25.959 57.642 65.721 1.00 22.45 ? 476 ASN A N 1 ATOM 3457 C CA . ASN A 1 483 ? 25.843 57.327 67.146 1.00 22.44 ? 476 ASN A CA 1 ATOM 3458 C C . ASN A 1 483 ? 25.681 55.850 67.417 1.00 23.41 ? 476 ASN A C 1 ATOM 3459 O O . ASN A 1 483 ? 26.339 55.300 68.312 1.00 25.72 ? 476 ASN A O 1 ATOM 3460 C CB . ASN A 1 483 ? 24.694 58.085 67.778 1.00 22.22 ? 476 ASN A CB 1 ATOM 3461 C CG . ASN A 1 483 ? 24.986 59.562 67.931 1.00 25.07 ? 476 ASN A CG 1 ATOM 3462 O OD1 . ASN A 1 483 ? 26.031 60.046 67.515 1.00 26.41 ? 476 ASN A OD1 1 ATOM 3463 N ND2 . ASN A 1 483 ? 24.045 60.288 68.526 1.00 24.94 ? 476 ASN A ND2 1 ATOM 3464 N N . LEU A 1 484 ? 24.818 55.203 66.645 1.00 23.45 ? 477 LEU A N 1 ATOM 3465 C CA . LEU A 1 484 ? 24.596 53.778 66.819 1.00 22.49 ? 477 LEU A CA 1 ATOM 3466 C C . LEU A 1 484 ? 25.872 52.976 66.560 1.00 23.24 ? 477 LEU A C 1 ATOM 3467 O O . LEU A 1 484 ? 26.249 52.127 67.377 1.00 23.68 ? 477 LEU A O 1 ATOM 3468 C CB . LEU A 1 484 ? 23.458 53.289 65.908 1.00 21.77 ? 477 LEU A CB 1 ATOM 3469 C CG . LEU A 1 484 ? 23.232 51.774 65.943 1.00 22.49 ? 477 LEU A CG 1 ATOM 3470 C CD1 . LEU A 1 484 ? 22.838 51.300 67.336 1.00 24.67 ? 477 LEU A CD1 1 ATOM 3471 C CD2 . LEU A 1 484 ? 22.171 51.396 64.914 1.00 22.25 ? 477 LEU A CD2 1 ATOM 3472 N N . THR A 1 485 ? 26.536 53.236 65.429 1.00 23.35 ? 478 THR A N 1 ATOM 3473 C CA . THR A 1 485 ? 27.749 52.458 65.067 1.00 25.05 ? 478 THR A CA 1 ATOM 3474 C C . THR A 1 485 ? 28.906 52.673 66.059 1.00 24.46 ? 478 THR A C 1 ATOM 3475 O O . THR A 1 485 ? 29.765 51.798 66.219 1.00 24.06 ? 478 THR A O 1 ATOM 3476 C CB . THR A 1 485 ? 28.211 52.681 63.594 1.00 23.25 ? 478 THR A CB 1 ATOM 3477 O OG1 . THR A 1 485 ? 28.564 54.056 63.382 1.00 22.99 ? 478 THR A OG1 1 ATOM 3478 C CG2 . THR A 1 485 ? 27.116 52.252 62.572 1.00 22.54 ? 478 THR A CG2 1 ATOM 3479 N N . LYS A 1 486 ? 28.918 53.810 66.760 1.00 25.65 ? 479 LYS A N 1 ATOM 3480 C CA . LYS A 1 486 ? 29.898 54.008 67.848 1.00 27.96 ? 479 LYS A CA 1 ATOM 3481 C C . LYS A 1 486 ? 29.661 53.083 69.045 1.00 27.32 ? 479 LYS A C 1 ATOM 3482 O O . LYS A 1 486 ? 30.586 52.836 69.829 1.00 29.29 ? 479 LYS A O 1 ATOM 3483 C CB . LYS A 1 486 ? 29.928 55.472 68.309 1.00 27.60 ? 479 LYS A CB 1 ATOM 3484 C CG . LYS A 1 486 ? 30.588 56.415 67.317 1.00 27.22 ? 479 LYS A CG 1 ATOM 3485 C CD . LYS A 1 486 ? 30.452 57.867 67.740 1.00 29.13 ? 479 LYS A CD 1 ATOM 3486 C CE . LYS A 1 486 ? 30.859 58.787 66.601 1.00 31.02 ? 479 LYS A CE 1 ATOM 3487 N NZ . LYS A 1 486 ? 30.820 60.226 66.995 1.00 34.26 ? 479 LYS A NZ 1 ATOM 3488 N N . GLU A 1 487 ? 28.443 52.561 69.170 1.00 28.61 ? 480 GLU A N 1 ATOM 3489 C CA . GLU A 1 487 ? 28.066 51.682 70.285 1.00 30.27 ? 480 GLU A CA 1 ATOM 3490 C C . GLU A 1 487 ? 28.081 50.208 69.906 1.00 30.05 ? 480 GLU A C 1 ATOM 3491 O O . GLU A 1 487 ? 27.864 49.357 70.760 1.00 34.58 ? 480 GLU A O 1 ATOM 3492 C CB . GLU A 1 487 ? 26.671 52.040 70.830 1.00 32.71 ? 480 GLU A CB 1 ATOM 3493 C CG . GLU A 1 487 ? 26.509 53.467 71.345 1.00 36.70 ? 480 GLU A CG 1 ATOM 3494 C CD . GLU A 1 487 ? 27.458 53.813 72.486 0.70 41.50 ? 480 GLU A CD 1 ATOM 3495 O OE1 . GLU A 1 487 ? 27.917 54.975 72.543 0.70 46.95 ? 480 GLU A OE1 1 ATOM 3496 O OE2 . GLU A 1 487 ? 27.753 52.926 73.324 0.70 45.29 ? 480 GLU A OE2 1 ATOM 3497 N N . LEU A 1 488 ? 28.310 49.912 68.629 1.00 27.70 ? 481 LEU A N 1 ATOM 3498 C CA . LEU A 1 488 ? 28.383 48.524 68.152 1.00 26.17 ? 481 LEU A CA 1 ATOM 3499 C C . LEU A 1 488 ? 29.825 48.046 68.015 1.00 27.69 ? 481 LEU A C 1 ATOM 3500 O O . LEU A 1 488 ? 30.721 48.831 67.709 1.00 28.24 ? 481 LEU A O 1 ATOM 3501 C CB . LEU A 1 488 ? 27.653 48.359 66.811 1.00 27.36 ? 481 LEU A CB 1 ATOM 3502 C CG . LEU A 1 488 ? 26.163 48.716 66.806 1.00 24.48 ? 481 LEU A CG 1 ATOM 3503 C CD1 . LEU A 1 488 ? 25.601 48.566 65.405 1.00 22.83 ? 481 LEU A CD1 1 ATOM 3504 C CD2 . LEU A 1 488 ? 25.410 47.849 67.817 1.00 25.21 ? 481 LEU A CD2 1 ATOM 3505 N N . LYS A 1 489 ? 30.035 46.752 68.233 1.00 26.68 ? 482 LYS A N 1 ATOM 3506 C CA . LYS A 1 489 ? 31.378 46.162 68.150 1.00 27.66 ? 482 LYS A CA 1 ATOM 3507 C C . LYS A 1 489 ? 31.745 45.937 66.680 1.00 28.71 ? 482 LYS A C 1 ATOM 3508 O O . LYS A 1 489 ? 30.909 45.478 65.900 1.00 29.51 ? 482 LYS A O 1 ATOM 3509 C CB . LYS A 1 489 ? 31.426 44.814 68.889 1.00 30.02 ? 482 LYS A CB 1 ATOM 3510 C CG . LYS A 1 489 ? 31.183 44.877 70.391 1.00 33.46 ? 482 LYS A CG 1 ATOM 3511 C CD . LYS A 1 489 ? 31.202 43.469 70.979 1.00 40.13 ? 482 LYS A CD 1 ATOM 3512 C CE . LYS A 1 489 ? 31.192 43.481 72.506 1.00 47.17 ? 482 LYS A CE 1 ATOM 3513 N NZ . LYS A 1 489 ? 29.862 43.823 73.086 0.20 43.97 ? 482 LYS A NZ 1 ATOM 3514 N N . SER A 1 490 ? 32.978 46.247 66.285 1.00 26.01 ? 483 SER A N 1 ATOM 3515 C CA . SER A 1 490 ? 33.398 45.880 64.919 1.00 27.55 ? 483 SER A CA 1 ATOM 3516 C C . SER A 1 490 ? 33.585 44.364 64.793 1.00 26.71 ? 483 SER A C 1 ATOM 3517 O O . SER A 1 490 ? 34.202 43.752 65.651 1.00 28.44 ? 483 SER A O 1 ATOM 3518 C CB . SER A 1 490 ? 34.685 46.586 64.495 1.00 28.05 ? 483 SER A CB 1 ATOM 3519 O OG . SER A 1 490 ? 35.079 46.115 63.209 1.00 28.47 ? 483 SER A OG 1 ATOM 3520 N N . PRO A 1 491 ? 33.052 43.755 63.718 1.00 25.70 ? 484 PRO A N 1 ATOM 3521 C CA . PRO A 1 491 ? 33.281 42.319 63.521 1.00 26.39 ? 484 PRO A CA 1 ATOM 3522 C C . PRO A 1 491 ? 34.570 42.052 62.738 1.00 28.17 ? 484 PRO A C 1 ATOM 3523 O O . PRO A 1 491 ? 34.905 40.893 62.477 1.00 27.72 ? 484 PRO A O 1 ATOM 3524 C CB . PRO A 1 491 ? 32.083 41.905 62.664 1.00 25.27 ? 484 PRO A CB 1 ATOM 3525 C CG . PRO A 1 491 ? 31.817 43.122 61.824 1.00 24.53 ? 484 PRO A CG 1 ATOM 3526 C CD . PRO A 1 491 ? 32.109 44.306 62.719 1.00 26.55 ? 484 PRO A CD 1 ATOM 3527 N N . ASP A 1 492 ? 35.272 43.115 62.346 1.00 29.19 ? 485 ASP A N 1 ATOM 3528 C CA . ASP A 1 492 ? 36.415 42.990 61.432 1.00 30.02 ? 485 ASP A CA 1 ATOM 3529 C C . ASP A 1 492 ? 37.680 42.478 62.117 1.00 30.06 ? 485 ASP A C 1 ATOM 3530 O O . ASP A 1 492 ? 38.011 42.884 63.246 1.00 30.09 ? 485 ASP A O 1 ATOM 3531 C CB . ASP A 1 492 ? 36.739 44.340 60.785 1.00 27.64 ? 485 ASP A CB 1 ATOM 3532 C CG . ASP A 1 492 ? 35.574 44.927 60.002 1.00 28.32 ? 485 ASP A CG 1 ATOM 3533 O OD1 . ASP A 1 492 ? 34.478 44.323 59.943 1.00 29.27 ? 485 ASP A OD1 1 ATOM 3534 O OD2 . ASP A 1 492 ? 35.761 46.020 59.444 1.00 27.76 ? 485 ASP A OD2 1 ATOM 3535 N N . GLU A 1 493 ? 38.402 41.612 61.407 1.00 32.10 ? 486 GLU A N 1 ATOM 3536 C CA . GLU A 1 493 ? 39.727 41.162 61.823 1.00 33.12 ? 486 GLU A CA 1 ATOM 3537 C C . GLU A 1 493 ? 40.640 42.387 61.944 1.00 33.04 ? 486 GLU A C 1 ATOM 3538 O O . GLU A 1 493 ? 40.642 43.265 61.077 1.00 33.82 ? 486 GLU A O 1 ATOM 3539 C CB . GLU A 1 493 ? 40.280 40.155 60.801 1.00 35.75 ? 486 GLU A CB 1 ATOM 3540 C CG . GLU A 1 493 ? 39.505 38.833 60.711 0.50 38.43 ? 486 GLU A CG 1 ATOM 3541 C CD . GLU A 1 493 ? 38.223 38.880 59.864 0.50 43.80 ? 486 GLU A CD 1 ATOM 3542 O OE1 . GLU A 1 493 ? 37.808 39.968 59.381 0.70 43.83 ? 486 GLU A OE1 1 ATOM 3543 O OE2 . GLU A 1 493 ? 37.609 37.800 59.681 1.00 46.49 ? 486 GLU A OE2 1 ATOM 3544 N N . GLY A 1 494 ? 41.389 42.468 63.037 1.00 34.80 ? 487 GLY A N 1 ATOM 3545 C CA . GLY A 1 494 ? 42.267 43.615 63.258 1.00 35.17 ? 487 GLY A CA 1 ATOM 3546 C C . GLY A 1 494 ? 41.611 44.762 64.006 1.00 36.39 ? 487 GLY A C 1 ATOM 3547 O O . GLY A 1 494 ? 42.298 45.692 64.441 1.00 39.27 ? 487 GLY A O 1 ATOM 3548 N N . PHE A 1 495 ? 40.289 44.702 64.160 1.00 33.96 ? 488 PHE A N 1 ATOM 3549 C CA . PHE A 1 495 ? 39.559 45.722 64.911 1.00 32.29 ? 488 PHE A CA 1 ATOM 3550 C C . PHE A 1 495 ? 38.824 45.107 66.100 1.00 34.01 ? 488 PHE A C 1 ATOM 3551 O O . PHE A 1 495 ? 37.811 45.644 66.544 1.00 33.79 ? 488 PHE A O 1 ATOM 3552 C CB . PHE A 1 495 ? 38.571 46.458 64.007 1.00 32.80 ? 488 PHE A CB 1 ATOM 3553 C CG . PHE A 1 495 ? 39.224 47.271 62.928 1.00 33.38 ? 488 PHE A CG 1 ATOM 3554 C CD1 . PHE A 1 495 ? 39.440 48.635 63.103 1.00 35.23 ? 488 PHE A CD1 1 ATOM 3555 C CD2 . PHE A 1 495 ? 39.611 46.677 61.723 1.00 35.36 ? 488 PHE A CD2 1 ATOM 3556 C CE1 . PHE A 1 495 ? 40.033 49.398 62.102 1.00 37.57 ? 488 PHE A CE1 1 ATOM 3557 C CE2 . PHE A 1 495 ? 40.207 47.434 60.722 1.00 37.11 ? 488 PHE A CE2 1 ATOM 3558 C CZ . PHE A 1 495 ? 40.421 48.796 60.914 1.00 37.63 ? 488 PHE A CZ 1 ATOM 3559 N N . GLU A 1 496 ? 39.325 43.989 66.627 1.00 35.52 ? 489 GLU A N 1 ATOM 3560 C CA . GLU A 1 496 ? 38.666 43.391 67.793 1.00 38.08 ? 489 GLU A CA 1 ATOM 3561 C C . GLU A 1 496 ? 38.754 44.328 68.995 1.00 34.40 ? 489 GLU A C 1 ATOM 3562 O O . GLU A 1 496 ? 39.804 44.910 69.276 1.00 36.61 ? 489 GLU A O 1 ATOM 3563 C CB . GLU A 1 496 ? 39.110 41.941 68.117 1.00 45.52 ? 489 GLU A CB 1 ATOM 3564 C CG . GLU A 1 496 ? 40.518 41.529 67.744 1.00 46.13 ? 489 GLU A CG 1 ATOM 3565 C CD . GLU A 1 496 ? 40.752 41.448 66.250 1.00 40.61 ? 489 GLU A CD 1 ATOM 3566 O OE1 . GLU A 1 496 ? 40.284 40.500 65.574 1.00 43.27 ? 489 GLU A OE1 1 ATOM 3567 O OE2 . GLU A 1 496 ? 41.438 42.352 65.756 1.00 42.99 ? 489 GLU A OE2 1 ATOM 3568 N N . GLY A 1 497 ? 37.619 44.538 69.650 1.00 36.66 ? 490 GLY A N 1 ATOM 3569 C CA . GLY A 1 497 ? 37.553 45.488 70.763 1.00 38.00 ? 490 GLY A CA 1 ATOM 3570 C C . GLY A 1 497 ? 37.370 46.942 70.341 1.00 36.53 ? 490 GLY A C 1 ATOM 3571 O O . GLY A 1 497 ? 37.303 47.838 71.191 1.00 38.41 ? 490 GLY A O 1 ATOM 3572 N N . LYS A 1 498 ? 37.294 47.180 69.034 1.00 34.50 ? 491 LYS A N 1 ATOM 3573 C CA . LYS A 1 498 ? 36.997 48.508 68.506 1.00 34.34 ? 491 LYS A CA 1 ATOM 3574 C C . LYS A 1 498 ? 35.538 48.597 68.067 1.00 32.32 ? 491 LYS A C 1 ATOM 3575 O O . LYS A 1 498 ? 34.876 47.576 67.849 1.00 32.16 ? 491 LYS A O 1 ATOM 3576 C CB . LYS A 1 498 ? 37.930 48.867 67.339 1.00 34.10 ? 491 LYS A CB 1 ATOM 3577 C CG . LYS A 1 498 ? 39.420 48.708 67.640 1.00 38.00 ? 491 LYS A CG 1 ATOM 3578 C CD . LYS A 1 498 ? 39.858 49.514 68.864 1.00 40.83 ? 491 LYS A CD 1 ATOM 3579 C CE . LYS A 1 498 ? 41.353 49.390 69.118 1.00 49.36 ? 491 LYS A CE 1 ATOM 3580 N NZ . LYS A 1 498 ? 42.141 50.090 68.066 1.00 54.13 ? 491 LYS A NZ 1 ATOM 3581 N N . SER A 1 499 ? 35.047 49.827 67.941 1.00 29.37 ? 492 SER A N 1 ATOM 3582 C CA . SER A 1 499 ? 33.676 50.081 67.496 1.00 27.82 ? 492 SER A CA 1 ATOM 3583 C C . SER A 1 499 ? 33.548 49.867 65.991 1.00 26.75 ? 492 SER A C 1 ATOM 3584 O O . SER A 1 499 ? 34.528 49.964 65.237 1.00 27.10 ? 492 SER A O 1 ATOM 3585 C CB . SER A 1 499 ? 33.254 51.507 67.856 1.00 28.43 ? 492 SER A CB 1 ATOM 3586 O OG . SER A 1 499 ? 33.817 52.440 66.955 1.00 30.30 ? 492 SER A OG 1 ATOM 3587 N N . LEU A 1 500 ? 32.331 49.575 65.562 1.00 26.04 ? 493 LEU A N 1 ATOM 3588 C CA . LEU A 1 500 ? 32.014 49.501 64.143 1.00 25.08 ? 493 LEU A CA 1 ATOM 3589 C C . LEU A 1 500 ? 32.247 50.876 63.489 1.00 26.09 ? 493 LEU A C 1 ATOM 3590 O O . LEU A 1 500 ? 32.715 50.948 62.347 1.00 25.64 ? 493 LEU A O 1 ATOM 3591 C CB . LEU A 1 500 ? 30.560 49.074 63.980 1.00 23.46 ? 493 LEU A CB 1 ATOM 3592 C CG . LEU A 1 500 ? 30.014 48.959 62.562 1.00 23.45 ? 493 LEU A CG 1 ATOM 3593 C CD1 . LEU A 1 500 ? 30.842 47.976 61.721 1.00 24.02 ? 493 LEU A CD1 1 ATOM 3594 C CD2 . LEU A 1 500 ? 28.539 48.582 62.587 1.00 22.76 ? 493 LEU A CD2 1 ATOM 3595 N N . TYR A 1 501 ? 31.931 51.960 64.207 1.00 25.03 ? 494 TYR A N 1 ATOM 3596 C CA . TYR A 1 501 ? 32.214 53.292 63.685 1.00 26.29 ? 494 TYR A CA 1 ATOM 3597 C C . TYR A 1 501 ? 33.703 53.430 63.306 1.00 27.32 ? 494 TYR A C 1 ATOM 3598 O O . TYR A 1 501 ? 34.033 53.960 62.235 1.00 27.70 ? 494 TYR A O 1 ATOM 3599 C CB . TYR A 1 501 ? 31.820 54.385 64.688 1.00 26.39 ? 494 TYR A CB 1 ATOM 3600 C CG . TYR A 1 501 ? 32.028 55.793 64.165 1.00 27.42 ? 494 TYR A CG 1 ATOM 3601 C CD1 . TYR A 1 501 ? 31.015 56.448 63.463 1.00 26.56 ? 494 TYR A CD1 1 ATOM 3602 C CD2 . TYR A 1 501 ? 33.240 56.469 64.364 1.00 28.49 ? 494 TYR A CD2 1 ATOM 3603 C CE1 . TYR A 1 501 ? 31.192 57.735 62.980 1.00 25.87 ? 494 TYR A CE1 1 ATOM 3604 C CE2 . TYR A 1 501 ? 33.428 57.761 63.884 1.00 27.24 ? 494 TYR A CE2 1 ATOM 3605 C CZ . TYR A 1 501 ? 32.396 58.387 63.194 1.00 26.28 ? 494 TYR A CZ 1 ATOM 3606 O OH . TYR A 1 501 ? 32.554 59.653 62.701 1.00 32.75 ? 494 TYR A OH 1 ATOM 3607 N N . GLU A 1 502 ? 34.589 52.958 64.179 1.00 26.28 ? 495 GLU A N 1 ATOM 3608 C CA . GLU A 1 502 ? 36.035 53.093 63.946 1.00 29.07 ? 495 GLU A CA 1 ATOM 3609 C C . GLU A 1 502 ? 36.476 52.311 62.707 1.00 27.09 ? 495 GLU A C 1 ATOM 3610 O O . GLU A 1 502 ? 37.201 52.845 61.866 1.00 28.43 ? 495 GLU A O 1 ATOM 3611 C CB . GLU A 1 502 ? 36.858 52.644 65.159 1.00 31.03 ? 495 GLU A CB 1 ATOM 3612 C CG . GLU A 1 502 ? 38.364 52.822 64.957 1.00 33.49 ? 495 GLU A CG 1 ATOM 3613 C CD . GLU A 1 502 ? 39.175 52.485 66.189 1.00 39.20 ? 495 GLU A CD 1 ATOM 3614 O OE1 . GLU A 1 502 ? 38.722 52.813 67.310 1.00 45.74 ? 495 GLU A OE1 1 ATOM 3615 O OE2 . GLU A 1 502 ? 40.277 51.909 66.038 1.00 47.76 ? 495 GLU A OE2 1 ATOM 3616 N N . SER A 1 503 ? 36.040 51.055 62.603 1.00 26.63 ? 496 SER A N 1 ATOM 3617 C CA . SER A 1 503 ? 36.485 50.205 61.493 1.00 26.79 ? 496 SER A CA 1 ATOM 3618 C C . SER A 1 503 ? 35.905 50.717 60.184 1.00 25.83 ? 496 SER A C 1 ATOM 3619 O O . SER A 1 503 ? 36.614 50.816 59.183 1.00 28.45 ? 496 SER A O 1 ATOM 3620 C CB . SER A 1 503 ? 36.172 48.718 61.716 1.00 26.63 ? 496 SER A CB 1 ATOM 3621 O OG . SER A 1 503 ? 34.790 48.453 61.754 1.00 26.88 ? 496 SER A OG 1 ATOM 3622 N N . TRP A 1 504 ? 34.619 51.067 60.209 1.00 25.95 ? 497 TRP A N 1 ATOM 3623 C CA . TRP A 1 504 ? 33.940 51.621 59.053 1.00 25.60 ? 497 TRP A CA 1 ATOM 3624 C C . TRP A 1 504 ? 34.565 52.921 58.598 1.00 26.42 ? 497 TRP A C 1 ATOM 3625 O O . TRP A 1 504 ? 34.800 53.123 57.399 1.00 27.15 ? 497 TRP A O 1 ATOM 3626 C CB . TRP A 1 504 ? 32.462 51.770 59.387 1.00 25.31 ? 497 TRP A CB 1 ATOM 3627 C CG . TRP A 1 504 ? 31.583 52.399 58.345 1.00 23.60 ? 497 TRP A CG 1 ATOM 3628 C CD1 . TRP A 1 504 ? 31.696 52.336 56.953 1.00 23.36 ? 497 TRP A CD1 1 ATOM 3629 C CD2 . TRP A 1 504 ? 30.389 53.190 58.604 1.00 23.43 ? 497 TRP A CD2 1 ATOM 3630 N NE1 . TRP A 1 504 ? 30.677 53.038 56.348 1.00 22.86 ? 497 TRP A NE1 1 ATOM 3631 C CE2 . TRP A 1 504 ? 29.857 53.588 57.292 1.00 24.10 ? 497 TRP A CE2 1 ATOM 3632 C CE3 . TRP A 1 504 ? 29.731 53.615 59.767 1.00 23.27 ? 497 TRP A CE3 1 ATOM 3633 C CZ2 . TRP A 1 504 ? 28.702 54.371 57.171 1.00 23.86 ? 497 TRP A CZ2 1 ATOM 3634 C CZ3 . TRP A 1 504 ? 28.583 54.398 59.635 1.00 23.62 ? 497 TRP A CZ3 1 ATOM 3635 C CH2 . TRP A 1 504 ? 28.081 54.771 58.361 1.00 22.40 ? 497 TRP A CH2 1 ATOM 3636 N N . THR A 1 505 ? 34.841 53.813 59.543 1.00 25.10 ? 498 THR A N 1 ATOM 3637 C CA . THR A 1 505 ? 35.455 55.094 59.226 1.00 28.27 ? 498 THR A CA 1 ATOM 3638 C C . THR A 1 505 ? 36.877 54.905 58.655 1.00 29.28 ? 498 THR A C 1 ATOM 3639 O O . THR A 1 505 ? 37.248 55.563 57.679 1.00 29.68 ? 498 THR A O 1 ATOM 3640 C CB . THR A 1 505 ? 35.467 56.000 60.468 1.00 27.73 ? 498 THR A CB 1 ATOM 3641 O OG1 A THR A 1 505 ? 34.112 56.336 60.809 1.00 28.90 ? 498 THR A OG1 1 ATOM 3642 C CG2 A THR A 1 505 ? 36.265 57.284 60.217 1.00 32.26 ? 498 THR A CG2 1 ATOM 3643 N N . LYS A 1 506 ? 37.658 54.003 59.248 1.00 28.56 ? 499 LYS A N 1 ATOM 3644 C CA . LYS A 1 506 ? 38.997 53.715 58.734 1.00 30.02 ? 499 LYS A CA 1 ATOM 3645 C C . LYS A 1 506 ? 38.920 53.167 57.293 1.00 30.35 ? 499 LYS A C 1 ATOM 3646 O O . LYS A 1 506 ? 39.645 53.627 56.417 1.00 32.45 ? 499 LYS A O 1 ATOM 3647 C CB . LYS A 1 506 ? 39.753 52.748 59.667 1.00 31.27 ? 499 LYS A CB 1 ATOM 3648 C CG . LYS A 1 506 ? 41.268 52.925 59.712 1.00 39.89 ? 499 LYS A CG 1 ATOM 3649 C CD . LYS A 1 506 ? 41.975 52.337 58.505 1.00 42.12 ? 499 LYS A CD 1 ATOM 3650 C CE . LYS A 1 506 ? 43.484 52.287 58.709 0.20 34.00 ? 499 LYS A CE 1 ATOM 3651 N NZ . LYS A 1 506 ? 44.108 53.635 58.617 0.20 26.84 ? 499 LYS A NZ 1 ATOM 3652 N N . LYS A 1 507 ? 38.013 52.224 57.047 1.00 29.10 ? 500 LYS A N 1 ATOM 3653 C CA . LYS A 1 507 ? 37.936 51.520 55.754 1.00 28.42 ? 500 LYS A CA 1 ATOM 3654 C C . LYS A 1 507 ? 37.209 52.271 54.643 1.00 29.09 ? 500 LYS A C 1 ATOM 3655 O O . LYS A 1 507 ? 37.489 52.047 53.457 1.00 31.36 ? 500 LYS A O 1 ATOM 3656 C CB . LYS A 1 507 ? 37.298 50.144 55.933 1.00 29.31 ? 500 LYS A CB 1 ATOM 3657 C CG . LYS A 1 507 ? 38.184 49.134 56.651 1.00 30.26 ? 500 LYS A CG 1 ATOM 3658 C CD . LYS A 1 507 ? 37.450 47.818 56.873 1.00 26.22 ? 500 LYS A CD 1 ATOM 3659 C CE . LYS A 1 507 ? 38.393 46.767 57.448 1.00 30.19 ? 500 LYS A CE 1 ATOM 3660 N NZ . LYS A 1 507 ? 37.753 45.422 57.521 1.00 28.94 ? 500 LYS A NZ 1 ATOM 3661 N N . SER A 1 508 ? 36.263 53.128 55.025 1.00 27.81 ? 501 SER A N 1 ATOM 3662 C CA . SER A 1 508 ? 35.439 53.856 54.076 1.00 28.23 ? 501 SER A CA 1 ATOM 3663 C C . SER A 1 508 ? 35.300 55.319 54.520 1.00 28.57 ? 501 SER A C 1 ATOM 3664 O O . SER A 1 508 ? 34.217 55.760 54.924 1.00 28.65 ? 501 SER A O 1 ATOM 3665 C CB . SER A 1 508 ? 34.073 53.169 53.962 1.00 28.94 ? 501 SER A CB 1 ATOM 3666 O OG . SER A 1 508 ? 33.365 53.626 52.832 1.00 32.87 ? 501 SER A OG 1 ATOM 3667 N N . PRO A 1 509 ? 36.411 56.084 54.451 1.00 30.16 ? 502 PRO A N 1 ATOM 3668 C CA . PRO A 1 509 ? 36.371 57.461 54.934 1.00 30.24 ? 502 PRO A CA 1 ATOM 3669 C C . PRO A 1 509 ? 35.450 58.326 54.094 1.00 32.42 ? 502 PRO A C 1 ATOM 3670 O O . PRO A 1 509 ? 35.345 58.147 52.872 1.00 31.83 ? 502 PRO A O 1 ATOM 3671 C CB . PRO A 1 509 ? 37.819 57.939 54.789 1.00 32.07 ? 502 PRO A CB 1 ATOM 3672 C CG . PRO A 1 509 ? 38.417 57.048 53.753 1.00 31.84 ? 502 PRO A CG 1 ATOM 3673 C CD . PRO A 1 509 ? 37.720 55.725 53.877 1.00 30.36 ? 502 PRO A CD 1 ATOM 3674 N N . SER A 1 510 ? 34.775 59.246 54.770 1.00 35.00 ? 503 SER A N 1 ATOM 3675 C CA . SER A 1 510 ? 33.996 60.278 54.115 1.00 38.81 ? 503 SER A CA 1 ATOM 3676 C C . SER A 1 510 ? 34.900 61.073 53.167 1.00 40.43 ? 503 SER A C 1 ATOM 3677 O O . SER A 1 510 ? 36.031 61.405 53.532 1.00 40.08 ? 503 SER A O 1 ATOM 3678 C CB . SER A 1 510 ? 33.402 61.205 55.176 1.00 36.58 ? 503 SER A CB 1 ATOM 3679 O OG . SER A 1 510 ? 33.192 62.492 54.651 1.00 41.65 ? 503 SER A OG 1 ATOM 3680 N N . PRO A 1 511 ? 34.416 61.364 51.942 1.00 41.84 ? 504 PRO A N 1 ATOM 3681 C CA . PRO A 1 511 ? 35.214 62.213 51.052 1.00 46.35 ? 504 PRO A CA 1 ATOM 3682 C C . PRO A 1 511 ? 35.292 63.675 51.536 1.00 49.16 ? 504 PRO A C 1 ATOM 3683 O O . PRO A 1 511 ? 36.281 64.361 51.261 1.00 53.89 ? 504 PRO A O 1 ATOM 3684 C CB . PRO A 1 511 ? 34.493 62.103 49.700 1.00 46.35 ? 504 PRO A CB 1 ATOM 3685 C CG . PRO A 1 511 ? 33.118 61.623 50.012 1.00 44.06 ? 504 PRO A CG 1 ATOM 3686 C CD . PRO A 1 511 ? 33.200 60.842 51.291 1.00 42.30 ? 504 PRO A CD 1 ATOM 3687 N N . GLU A 1 512 ? 34.276 64.129 52.273 1.00 54.63 ? 505 GLU A N 1 ATOM 3688 C CA . GLU A 1 512 ? 34.218 65.520 52.749 1.00 52.59 ? 505 GLU A CA 1 ATOM 3689 C C . GLU A 1 512 ? 34.917 65.756 54.091 1.00 54.17 ? 505 GLU A C 1 ATOM 3690 O O . GLU A 1 512 ? 35.574 66.784 54.273 1.00 57.95 ? 505 GLU A O 1 ATOM 3691 C CB . GLU A 1 512 ? 32.768 66.021 52.858 1.00 58.47 ? 505 GLU A CB 1 ATOM 3692 C CG . GLU A 1 512 ? 32.068 66.383 51.554 1.00 62.06 ? 505 GLU A CG 1 ATOM 3693 C CD . GLU A 1 512 ? 31.218 65.248 51.001 1.00 64.61 ? 505 GLU A CD 1 ATOM 3694 O OE1 . GLU A 1 512 ? 31.193 65.074 49.762 1.00 85.23 ? 505 GLU A OE1 1 ATOM 3695 O OE2 . GLU A 1 512 ? 30.567 64.534 51.798 1.00 61.37 ? 505 GLU A OE2 1 ATOM 3696 N N . PHE A 1 513 ? 34.763 64.828 55.036 1.00 46.96 ? 506 PHE A N 1 ATOM 3697 C CA . PHE A 1 513 ? 35.110 65.133 56.428 1.00 48.33 ? 506 PHE A CA 1 ATOM 3698 C C . PHE A 1 513 ? 36.045 64.127 57.069 1.00 47.92 ? 506 PHE A C 1 ATOM 3699 O O . PHE A 1 513 ? 35.821 62.914 57.001 1.00 48.52 ? 506 PHE A O 1 ATOM 3700 C CB . PHE A 1 513 ? 33.843 65.287 57.284 1.00 53.91 ? 506 PHE A CB 1 ATOM 3701 C CG . PHE A 1 513 ? 32.853 66.299 56.753 1.00 57.08 ? 506 PHE A CG 1 ATOM 3702 C CD1 . PHE A 1 513 ? 31.725 65.884 56.037 1.00 57.56 ? 506 PHE A CD1 1 ATOM 3703 C CD2 . PHE A 1 513 ? 33.030 67.666 56.990 1.00 57.87 ? 506 PHE A CD2 1 ATOM 3704 C CE1 . PHE A 1 513 ? 30.805 66.812 55.553 1.00 58.32 ? 506 PHE A CE1 1 ATOM 3705 C CE2 . PHE A 1 513 ? 32.113 68.596 56.506 1.00 58.34 ? 506 PHE A CE2 1 ATOM 3706 C CZ . PHE A 1 513 ? 31.001 68.168 55.787 1.00 60.18 ? 506 PHE A CZ 1 ATOM 3707 N N . SER A 1 514 ? 37.097 64.638 57.701 1.00 52.12 ? 507 SER A N 1 ATOM 3708 C CA . SER A 1 514 ? 38.049 63.789 58.406 1.00 54.60 ? 507 SER A CA 1 ATOM 3709 C C . SER A 1 514 ? 37.385 63.157 59.617 1.00 50.52 ? 507 SER A C 1 ATOM 3710 O O . SER A 1 514 ? 36.658 63.832 60.359 1.00 49.82 ? 507 SER A O 1 ATOM 3711 C CB . SER A 1 514 ? 39.287 64.584 58.844 1.00 60.15 ? 507 SER A CB 1 ATOM 3712 O OG . SER A 1 514 ? 40.317 64.485 57.877 1.00 68.04 ? 507 SER A OG 1 ATOM 3713 N N . GLY A 1 515 ? 37.618 61.856 59.790 1.00 42.62 ? 508 GLY A N 1 ATOM 3714 C CA . GLY A 1 515 ? 37.170 61.142 60.979 1.00 39.38 ? 508 GLY A CA 1 ATOM 3715 C C . GLY A 1 515 ? 35.703 60.761 60.938 1.00 35.32 ? 508 GLY A C 1 ATOM 3716 O O . GLY A 1 515 ? 35.147 60.355 61.960 1.00 36.97 ? 508 GLY A O 1 ATOM 3717 N N . MET A 1 516 ? 35.092 60.907 59.759 1.00 33.57 ? 509 MET A N 1 ATOM 3718 C CA . MET A 1 516 ? 33.711 60.473 59.475 1.00 32.94 ? 509 MET A CA 1 ATOM 3719 C C . MET A 1 516 ? 33.685 59.385 58.406 1.00 31.33 ? 509 MET A C 1 ATOM 3720 O O . MET A 1 516 ? 34.554 59.355 57.533 1.00 35.44 ? 509 MET A O 1 ATOM 3721 C CB . MET A 1 516 ? 32.884 61.634 58.928 1.00 32.26 ? 509 MET A CB 1 ATOM 3722 C CG . MET A 1 516 ? 33.100 62.939 59.660 1.00 43.32 ? 509 MET A CG 1 ATOM 3723 S SD . MET A 1 516 ? 31.947 63.031 61.017 1.00 56.96 ? 509 MET A SD 1 ATOM 3724 C CE . MET A 1 516 ? 30.510 63.610 60.124 1.00 55.78 ? 509 MET A CE 1 ATOM 3725 N N . PRO A 1 517 ? 32.680 58.495 58.453 1.00 30.79 ? 510 PRO A N 1 ATOM 3726 C CA . PRO A 1 517 ? 32.517 57.489 57.407 1.00 29.42 ? 510 PRO A CA 1 ATOM 3727 C C . PRO A 1 517 ? 31.694 57.984 56.217 1.00 29.32 ? 510 PRO A C 1 ATOM 3728 O O . PRO A 1 517 ? 30.896 58.914 56.350 1.00 29.84 ? 510 PRO A O 1 ATOM 3729 C CB . PRO A 1 517 ? 31.758 56.378 58.131 1.00 27.31 ? 510 PRO A CB 1 ATOM 3730 C CG . PRO A 1 517 ? 30.888 57.116 59.096 1.00 26.99 ? 510 PRO A CG 1 ATOM 3731 C CD . PRO A 1 517 ? 31.738 58.280 59.569 1.00 31.36 ? 510 PRO A CD 1 ATOM 3732 N N . ARG A 1 518 ? 31.890 57.352 55.064 1.00 26.50 ? 511 ARG A N 1 ATOM 3733 C CA . ARG A 1 518 ? 31.074 57.605 53.880 1.00 25.68 ? 511 ARG A CA 1 ATOM 3734 C C . ARG A 1 518 ? 29.644 57.097 54.084 1.00 24.02 ? 511 ARG A C 1 ATOM 3735 O O . ARG A 1 518 ? 29.435 55.949 54.465 1.00 24.69 ? 511 ARG A O 1 ATOM 3736 C CB . ARG A 1 518 ? 31.687 56.893 52.673 1.00 27.36 ? 511 ARG A CB 1 ATOM 3737 C CG . ARG A 1 518 ? 30.852 56.968 51.401 1.00 28.47 ? 511 ARG A CG 1 ATOM 3738 C CD . ARG A 1 518 ? 31.477 56.168 50.267 1.00 33.21 ? 511 ARG A CD 1 ATOM 3739 N NE . ARG A 1 518 ? 32.802 56.675 49.918 1.00 34.25 ? 511 ARG A NE 1 ATOM 3740 C CZ . ARG A 1 518 ? 33.039 57.671 49.060 1.00 36.33 ? 511 ARG A CZ 1 ATOM 3741 N NH1 . ARG A 1 518 ? 32.039 58.291 48.442 1.00 37.31 ? 511 ARG A NH1 1 ATOM 3742 N NH2 . ARG A 1 518 ? 34.287 58.051 48.817 1.00 43.24 ? 511 ARG A NH2 1 ATOM 3743 N N . ILE A 1 519 ? 28.663 57.957 53.835 1.00 23.34 ? 512 ILE A N 1 ATOM 3744 C CA . ILE A 1 519 ? 27.277 57.528 53.756 1.00 23.12 ? 512 ILE A CA 1 ATOM 3745 C C . ILE A 1 519 ? 26.754 58.064 52.438 1.00 23.34 ? 512 ILE A C 1 ATOM 3746 O O . ILE A 1 519 ? 26.851 59.279 52.175 1.00 27.09 ? 512 ILE A O 1 ATOM 3747 C CB . ILE A 1 519 ? 26.414 58.095 54.910 1.00 22.23 ? 512 ILE A CB 1 ATOM 3748 C CG1 . ILE A 1 519 ? 26.899 57.564 56.261 1.00 23.04 ? 512 ILE A CG1 1 ATOM 3749 C CG2 . ILE A 1 519 ? 24.934 57.769 54.671 1.00 22.49 ? 512 ILE A CG2 1 ATOM 3750 C CD1 . ILE A 1 519 ? 26.128 58.128 57.447 1.00 24.70 ? 512 ILE A CD1 1 ATOM 3751 N N . SER A 1 520 ? 26.199 57.180 51.617 1.00 22.17 ? 513 SER A N 1 ATOM 3752 C CA . SER A 1 520 ? 25.706 57.570 50.291 1.00 22.78 ? 513 SER A CA 1 ATOM 3753 C C . SER A 1 520 ? 24.255 58.008 50.281 1.00 21.44 ? 513 SER A C 1 ATOM 3754 O O . SER A 1 520 ? 23.487 57.690 51.189 1.00 21.55 ? 513 SER A O 1 ATOM 3755 C CB . SER A 1 520 ? 25.864 56.423 49.291 1.00 22.50 ? 513 SER A CB 1 ATOM 3756 O OG . SER A 1 520 ? 27.226 56.045 49.189 1.00 27.28 ? 513 SER A OG 1 ATOM 3757 N N A LYS A 1 521 ? 23.904 58.724 49.218 0.70 22.40 ? 514 LYS A N 1 ATOM 3758 N N B LYS A 1 521 ? 23.865 58.743 49.249 0.30 21.55 ? 514 LYS A N 1 ATOM 3759 C CA A LYS A 1 521 ? 22.511 59.021 48.870 0.70 21.13 ? 514 LYS A CA 1 ATOM 3760 C CA B LYS A 1 521 ? 22.456 59.068 49.067 0.30 19.04 ? 514 LYS A CA 1 ATOM 3761 C C A LYS A 1 521 ? 21.760 57.719 48.618 0.70 19.48 ? 514 LYS A C 1 ATOM 3762 C C B LYS A 1 521 ? 21.736 57.833 48.537 0.30 19.25 ? 514 LYS A C 1 ATOM 3763 O O A LYS A 1 521 ? 22.361 56.724 48.180 0.70 21.81 ? 514 LYS A O 1 ATOM 3764 O O B LYS A 1 521 ? 22.340 56.998 47.849 0.30 20.54 ? 514 LYS A O 1 ATOM 3765 C CB A LYS A 1 521 ? 22.465 59.859 47.575 0.70 22.09 ? 514 LYS A CB 1 ATOM 3766 C CB B LYS A 1 521 ? 22.296 60.220 48.081 0.30 18.23 ? 514 LYS A CB 1 ATOM 3767 C CG A LYS A 1 521 ? 23.246 61.167 47.648 0.70 25.48 ? 514 LYS A CG 1 ATOM 3768 C CG B LYS A 1 521 ? 22.644 59.843 46.652 0.30 15.22 ? 514 LYS A CG 1 ATOM 3769 C CD A LYS A 1 521 ? 22.928 62.126 46.502 0.70 26.97 ? 514 LYS A CD 1 ATOM 3770 C CD B LYS A 1 521 ? 22.512 61.046 45.734 0.30 16.62 ? 514 LYS A CD 1 ATOM 3771 C CE A LYS A 1 521 ? 23.515 61.689 45.172 0.70 28.45 ? 514 LYS A CE 1 ATOM 3772 C CE B LYS A 1 521 ? 23.547 62.113 46.065 0.30 16.39 ? 514 LYS A CE 1 ATOM 3773 N NZ A LYS A 1 521 ? 24.989 61.893 45.124 0.70 29.29 ? 514 LYS A NZ 1 ATOM 3774 N NZ B LYS A 1 521 ? 24.933 61.659 45.759 0.30 17.50 ? 514 LYS A NZ 1 ATOM 3775 N N . LEU A 1 522 ? 20.451 57.724 48.859 1.00 18.89 ? 515 LEU A N 1 ATOM 3776 C CA . LEU A 1 522 ? 19.612 56.630 48.378 1.00 19.41 ? 515 LEU A CA 1 ATOM 3777 C C . LEU A 1 522 ? 19.476 56.754 46.881 1.00 22.58 ? 515 LEU A C 1 ATOM 3778 O O . LEU A 1 522 ? 19.187 57.847 46.366 1.00 24.01 ? 515 LEU A O 1 ATOM 3779 C CB . LEU A 1 522 ? 18.220 56.665 48.997 1.00 18.98 ? 515 LEU A CB 1 ATOM 3780 C CG . LEU A 1 522 ? 18.256 56.182 50.452 1.00 20.33 ? 515 LEU A CG 1 ATOM 3781 C CD1 . LEU A 1 522 ? 16.961 56.607 51.130 1.00 20.08 ? 515 LEU A CD1 1 ATOM 3782 C CD2 . LEU A 1 522 ? 18.476 54.670 50.525 1.00 20.32 ? 515 LEU A CD2 1 ATOM 3783 N N . GLY A 1 523 ? 19.696 55.635 46.190 1.00 20.55 ? 516 GLY A N 1 ATOM 3784 C CA . GLY A 1 523 ? 19.332 55.525 44.771 1.00 21.33 ? 516 GLY A CA 1 ATOM 3785 C C . GLY A 1 523 ? 17.997 54.834 44.676 1.00 20.85 ? 516 GLY A C 1 ATOM 3786 O O . GLY A 1 523 ? 17.037 55.243 45.306 1.00 22.92 ? 516 GLY A O 1 ATOM 3787 N N . SER A 1 524 ? 17.929 53.775 43.873 1.00 19.98 ? 517 SER A N 1 ATOM 3788 C CA . SER A 1 524 ? 16.699 52.986 43.793 1.00 19.35 ? 517 SER A CA 1 ATOM 3789 C C . SER A 1 524 ? 17.029 51.582 43.328 1.00 17.61 ? 517 SER A C 1 ATOM 3790 O O . SER A 1 524 ? 18.189 51.137 43.490 1.00 19.81 ? 517 SER A O 1 ATOM 3791 C CB . SER A 1 524 ? 15.667 53.669 42.923 1.00 18.56 ? 517 SER A CB 1 ATOM 3792 O OG . SER A 1 524 ? 14.452 52.955 42.990 1.00 20.42 ? 517 SER A OG 1 ATOM 3793 N N . GLY A 1 525 ? 16.031 50.850 42.828 1.00 16.64 ? 518 GLY A N 1 ATOM 3794 C CA . GLY A 1 525 ? 16.221 49.426 42.587 1.00 17.17 ? 518 GLY A CA 1 ATOM 3795 C C . GLY A 1 525 ? 15.948 48.596 43.839 1.00 16.05 ? 518 GLY A C 1 ATOM 3796 O O . GLY A 1 525 ? 16.236 47.404 43.864 1.00 16.47 ? 518 GLY A O 1 ATOM 3797 N N . ASN A 1 526 ? 15.343 49.204 44.864 1.00 15.55 ? 519 ASN A N 1 ATOM 3798 C CA . ASN A 1 526 ? 14.960 48.443 46.053 1.00 16.07 ? 519 ASN A CA 1 ATOM 3799 C C . ASN A 1 526 ? 13.703 49.006 46.712 1.00 14.71 ? 519 ASN A C 1 ATOM 3800 O O . ASN A 1 526 ? 13.252 50.086 46.331 1.00 15.17 ? 519 ASN A O 1 ATOM 3801 C CB . ASN A 1 526 ? 16.134 48.243 47.026 1.00 16.71 ? 519 ASN A CB 1 ATOM 3802 C CG . ASN A 1 526 ? 16.219 46.802 47.481 1.00 19.73 ? 519 ASN A CG 1 ATOM 3803 O OD1 . ASN A 1 526 ? 15.266 46.291 48.105 1.00 22.06 ? 519 ASN A OD1 1 ATOM 3804 N ND2 . ASN A 1 526 ? 17.315 46.108 47.103 1.00 17.76 ? 519 ASN A ND2 1 ATOM 3805 N N . ASP A 1 527 ? 13.152 48.283 47.689 1.00 14.05 ? 520 ASP A N 1 ATOM 3806 C CA . ASP A 1 527 ? 11.768 48.516 48.142 1.00 14.35 ? 520 ASP A CA 1 ATOM 3807 C C . ASP A 1 527 ? 11.546 49.794 48.955 1.00 13.53 ? 520 ASP A C 1 ATOM 3808 O O . ASP A 1 527 ? 10.403 50.124 49.285 1.00 15.74 ? 520 ASP A O 1 ATOM 3809 C CB . ASP A 1 527 ? 11.257 47.299 48.938 1.00 14.43 ? 520 ASP A CB 1 ATOM 3810 C CG . ASP A 1 527 ? 10.923 46.110 48.040 1.00 15.79 ? 520 ASP A CG 1 ATOM 3811 O OD1 . ASP A 1 527 ? 10.154 46.312 47.073 1.00 16.28 ? 520 ASP A OD1 1 ATOM 3812 O OD2 . ASP A 1 527 ? 11.451 44.984 48.292 1.00 17.33 ? 520 ASP A OD2 1 ATOM 3813 N N . PHE A 1 528 ? 12.609 50.535 49.254 1.00 15.35 ? 521 PHE A N 1 ATOM 3814 C CA . PHE A 1 528 ? 12.436 51.867 49.857 1.00 15.48 ? 521 PHE A CA 1 ATOM 3815 C C . PHE A 1 528 ? 11.912 52.908 48.850 1.00 15.24 ? 521 PHE A C 1 ATOM 3816 O O . PHE A 1 528 ? 11.515 54.009 49.264 1.00 16.36 ? 521 PHE A O 1 ATOM 3817 C CB . PHE A 1 528 ? 13.756 52.389 50.468 1.00 16.77 ? 521 PHE A CB 1 ATOM 3818 C CG . PHE A 1 528 ? 14.876 52.475 49.476 1.00 15.13 ? 521 PHE A CG 1 ATOM 3819 C CD1 . PHE A 1 528 ? 14.984 53.571 48.578 1.00 15.52 ? 521 PHE A CD1 1 ATOM 3820 C CD2 . PHE A 1 528 ? 15.833 51.449 49.414 1.00 16.64 ? 521 PHE A CD2 1 ATOM 3821 C CE1 . PHE A 1 528 ? 16.038 53.604 47.644 1.00 15.57 ? 521 PHE A CE1 1 ATOM 3822 C CE2 . PHE A 1 528 ? 16.878 51.497 48.485 1.00 18.28 ? 521 PHE A CE2 1 ATOM 3823 C CZ . PHE A 1 528 ? 16.965 52.562 47.588 1.00 19.15 ? 521 PHE A CZ 1 ATOM 3824 N N . GLU A 1 529 ? 11.922 52.581 47.558 1.00 13.92 ? 522 GLU A N 1 ATOM 3825 C CA . GLU A 1 529 ? 11.656 53.594 46.515 1.00 13.82 ? 522 GLU A CA 1 ATOM 3826 C C . GLU A 1 529 ? 10.292 54.274 46.752 1.00 14.03 ? 522 GLU A C 1 ATOM 3827 O O . GLU A 1 529 ? 10.194 55.518 46.724 1.00 14.00 ? 522 GLU A O 1 ATOM 3828 C CB . GLU A 1 529 ? 11.723 53.002 45.085 1.00 13.64 ? 522 GLU A CB 1 ATOM 3829 C CG . GLU A 1 529 ? 11.630 54.094 43.985 1.00 13.66 ? 522 GLU A CG 1 ATOM 3830 C CD . GLU A 1 529 ? 11.482 53.503 42.579 1.00 14.89 ? 522 GLU A CD 1 ATOM 3831 O OE1 . GLU A 1 529 ? 10.494 52.801 42.351 1.00 19.70 ? 522 GLU A OE1 1 ATOM 3832 O OE2 . GLU A 1 529 ? 12.360 53.734 41.697 1.00 18.61 ? 522 GLU A OE2 1 ATOM 3833 N N . VAL A 1 530 ? 9.230 53.482 46.965 1.00 13.81 ? 523 VAL A N 1 ATOM 3834 C CA . VAL A 1 530 ? 7.887 54.093 47.084 1.00 15.34 ? 523 VAL A CA 1 ATOM 3835 C C . VAL A 1 530 ? 7.840 54.956 48.359 1.00 14.02 ? 523 VAL A C 1 ATOM 3836 O O . VAL A 1 530 ? 7.249 56.045 48.387 1.00 14.75 ? 523 VAL A O 1 ATOM 3837 C CB . VAL A 1 530 ? 6.757 53.042 47.025 1.00 13.62 ? 523 VAL A CB 1 ATOM 3838 C CG1 . VAL A 1 530 ? 6.813 52.079 48.246 1.00 14.83 ? 523 VAL A CG1 1 ATOM 3839 C CG2 . VAL A 1 530 ? 5.376 53.723 46.872 1.00 12.89 ? 523 VAL A CG2 1 ATOM 3840 N N . PHE A 1 531 ? 8.455 54.450 49.426 1.00 14.07 ? 524 PHE A N 1 ATOM 3841 C CA . PHE A 1 531 ? 8.441 55.181 50.694 1.00 14.93 ? 524 PHE A CA 1 ATOM 3842 C C . PHE A 1 531 ? 9.168 56.500 50.660 1.00 14.97 ? 524 PHE A C 1 ATOM 3843 O O . PHE A 1 531 ? 8.675 57.493 51.217 1.00 15.36 ? 524 PHE A O 1 ATOM 3844 C CB . PHE A 1 531 ? 8.996 54.288 51.796 1.00 14.49 ? 524 PHE A CB 1 ATOM 3845 C CG . PHE A 1 531 ? 8.166 53.042 51.971 1.00 15.12 ? 524 PHE A CG 1 ATOM 3846 C CD1 . PHE A 1 531 ? 6.946 53.103 52.661 1.00 17.47 ? 524 PHE A CD1 1 ATOM 3847 C CD2 . PHE A 1 531 ? 8.554 51.835 51.380 1.00 15.85 ? 524 PHE A CD2 1 ATOM 3848 C CE1 . PHE A 1 531 ? 6.161 51.956 52.813 1.00 18.08 ? 524 PHE A CE1 1 ATOM 3849 C CE2 . PHE A 1 531 ? 7.767 50.681 51.523 1.00 15.72 ? 524 PHE A CE2 1 ATOM 3850 C CZ . PHE A 1 531 ? 6.569 50.742 52.221 1.00 17.40 ? 524 PHE A CZ 1 ATOM 3851 N N . PHE A 1 532 ? 10.325 56.506 50.009 1.00 14.24 ? 525 PHE A N 1 ATOM 3852 C CA . PHE A 1 532 ? 11.215 57.677 50.018 1.00 14.97 ? 525 PHE A CA 1 ATOM 3853 C C . PHE A 1 532 ? 10.888 58.642 48.864 1.00 14.07 ? 525 PHE A C 1 ATOM 3854 O O . PHE A 1 532 ? 10.453 59.776 49.109 1.00 15.30 ? 525 PHE A O 1 ATOM 3855 C CB . PHE A 1 532 ? 12.672 57.219 49.950 1.00 14.09 ? 525 PHE A CB 1 ATOM 3856 C CG . PHE A 1 532 ? 13.659 58.334 50.175 1.00 14.84 ? 525 PHE A CG 1 ATOM 3857 C CD1 . PHE A 1 532 ? 13.631 59.073 51.377 1.00 16.03 ? 525 PHE A CD1 1 ATOM 3858 C CD2 . PHE A 1 532 ? 14.590 58.683 49.177 1.00 16.02 ? 525 PHE A CD2 1 ATOM 3859 C CE1 . PHE A 1 532 ? 14.541 60.110 51.598 1.00 15.88 ? 525 PHE A CE1 1 ATOM 3860 C CE2 . PHE A 1 532 ? 15.512 59.722 49.404 1.00 17.45 ? 525 PHE A CE2 1 ATOM 3861 C CZ . PHE A 1 532 ? 15.477 60.431 50.617 1.00 17.67 ? 525 PHE A CZ 1 ATOM 3862 N N . GLN A 1 533 ? 11.071 58.193 47.618 1.00 14.31 ? 526 GLN A N 1 ATOM 3863 C CA . GLN A 1 533 ? 10.887 59.065 46.453 1.00 13.95 ? 526 GLN A CA 1 ATOM 3864 C C . GLN A 1 533 ? 9.422 59.391 46.114 1.00 14.40 ? 526 GLN A C 1 ATOM 3865 O O . GLN A 1 533 ? 9.160 60.470 45.566 1.00 15.67 ? 526 GLN A O 1 ATOM 3866 C CB A GLN A 1 533 ? 11.462 58.327 45.220 0.50 15.76 ? 526 GLN A CB 1 ATOM 3867 C CB B GLN A 1 533 ? 11.712 58.645 45.224 0.50 12.66 ? 526 GLN A CB 1 ATOM 3868 C CG A GLN A 1 533 ? 12.746 57.530 45.455 0.50 17.37 ? 526 GLN A CG 1 ATOM 3869 C CG B GLN A 1 533 ? 13.216 58.769 45.417 0.50 10.57 ? 526 GLN A CG 1 ATOM 3870 C CD A GLN A 1 533 ? 13.921 58.456 45.465 0.50 19.72 ? 526 GLN A CD 1 ATOM 3871 C CD B GLN A 1 533 ? 13.875 57.439 45.816 0.50 9.57 ? 526 GLN A CD 1 ATOM 3872 O OE1 A GLN A 1 533 ? 13.726 59.655 45.345 0.50 22.20 ? 526 GLN A OE1 1 ATOM 3873 O OE1 B GLN A 1 533 ? 13.230 56.563 46.393 0.50 10.27 ? 526 GLN A OE1 1 ATOM 3874 N NE2 A GLN A 1 533 ? 15.140 57.923 45.595 0.50 21.49 ? 526 GLN A NE2 1 ATOM 3875 N NE2 B GLN A 1 533 ? 15.187 57.298 45.521 0.50 12.24 ? 526 GLN A NE2 1 ATOM 3876 N N . ARG A 1 534 ? 8.473 58.481 46.400 1.00 13.14 ? 527 ARG A N 1 ATOM 3877 C CA . ARG A 1 534 ? 7.074 58.838 46.163 1.00 12.95 ? 527 ARG A CA 1 ATOM 3878 C C . ARG A 1 534 ? 6.452 59.532 47.368 1.00 13.13 ? 527 ARG A C 1 ATOM 3879 O O . ARG A 1 534 ? 5.855 60.623 47.241 1.00 13.80 ? 527 ARG A O 1 ATOM 3880 C CB . ARG A 1 534 ? 6.198 57.653 45.714 1.00 13.26 ? 527 ARG A CB 1 ATOM 3881 C CG . ARG A 1 534 ? 4.850 58.152 45.154 1.00 12.97 ? 527 ARG A CG 1 ATOM 3882 C CD . ARG A 1 534 ? 3.778 57.060 45.050 1.00 14.46 ? 527 ARG A CD 1 ATOM 3883 N NE . ARG A 1 534 ? 4.115 56.023 44.061 1.00 12.94 ? 527 ARG A NE 1 ATOM 3884 C CZ . ARG A 1 534 ? 3.183 55.272 43.458 1.00 13.15 ? 527 ARG A CZ 1 ATOM 3885 N NH1 . ARG A 1 534 ? 1.883 55.485 43.728 1.00 13.89 ? 527 ARG A NH1 1 ATOM 3886 N NH2 . ARG A 1 534 ? 3.534 54.302 42.616 1.00 13.82 ? 527 ARG A NH2 1 ATOM 3887 N N . LEU A 1 535 ? 6.551 58.886 48.525 1.00 14.09 ? 528 LEU A N 1 ATOM 3888 C CA . LEU A 1 535 ? 5.821 59.365 49.720 1.00 12.46 ? 528 LEU A CA 1 ATOM 3889 C C . LEU A 1 535 ? 6.579 60.330 50.636 1.00 13.41 ? 528 LEU A C 1 ATOM 3890 O O . LEU A 1 535 ? 5.948 61.000 51.463 1.00 16.64 ? 528 LEU A O 1 ATOM 3891 C CB . LEU A 1 535 ? 5.284 58.177 50.534 1.00 13.26 ? 528 LEU A CB 1 ATOM 3892 C CG . LEU A 1 535 ? 4.277 57.265 49.795 1.00 13.45 ? 528 LEU A CG 1 ATOM 3893 C CD1 . LEU A 1 535 ? 3.873 56.098 50.712 1.00 16.37 ? 528 LEU A CD1 1 ATOM 3894 C CD2 . LEU A 1 535 ? 3.030 58.035 49.304 1.00 16.95 ? 528 LEU A CD2 1 ATOM 3895 N N . GLY A 1 536 ? 7.904 60.394 50.515 1.00 13.28 ? 529 GLY A N 1 ATOM 3896 C CA . GLY A 1 536 ? 8.702 61.327 51.340 1.00 13.53 ? 529 GLY A CA 1 ATOM 3897 C C . GLY A 1 536 ? 8.815 60.922 52.795 1.00 12.87 ? 529 GLY A C 1 ATOM 3898 O O . GLY A 1 536 ? 8.761 61.791 53.697 1.00 14.06 ? 529 GLY A O 1 ATOM 3899 N N . ILE A 1 537 ? 8.993 59.615 53.032 1.00 13.71 ? 530 ILE A N 1 ATOM 3900 C CA . ILE A 1 537 ? 9.225 59.093 54.384 1.00 13.52 ? 530 ILE A CA 1 ATOM 3901 C C . ILE A 1 537 ? 10.724 58.839 54.525 1.00 13.76 ? 530 ILE A C 1 ATOM 3902 O O . ILE A 1 537 ? 11.327 58.170 53.668 1.00 14.69 ? 530 ILE A O 1 ATOM 3903 C CB . ILE A 1 537 ? 8.417 57.779 54.642 1.00 13.99 ? 530 ILE A CB 1 ATOM 3904 C CG1 . ILE A 1 537 ? 6.901 58.075 54.615 1.00 14.19 ? 530 ILE A CG1 1 ATOM 3905 C CG2 . ILE A 1 537 ? 8.815 57.124 55.969 1.00 15.81 ? 530 ILE A CG2 1 ATOM 3906 C CD1 . ILE A 1 537 ? 6.060 56.835 54.379 1.00 15.87 ? 530 ILE A CD1 1 ATOM 3907 N N . ALA A 1 538 ? 11.326 59.394 55.586 1.00 14.28 ? 531 ALA A N 1 ATOM 3908 C CA . ALA A 1 538 ? 12.759 59.219 55.869 1.00 14.15 ? 531 ALA A CA 1 ATOM 3909 C C . ALA A 1 538 ? 13.138 57.744 55.762 1.00 15.51 ? 531 ALA A C 1 ATOM 3910 O O . ALA A 1 538 ? 12.514 56.895 56.415 1.00 16.36 ? 531 ALA A O 1 ATOM 3911 C CB . ALA A 1 538 ? 13.067 59.751 57.271 1.00 15.73 ? 531 ALA A CB 1 ATOM 3912 N N . SER A 1 539 ? 14.125 57.434 54.916 1.00 14.60 ? 532 SER A N 1 ATOM 3913 C CA . SER A 1 539 ? 14.464 56.031 54.628 1.00 14.99 ? 532 SER A CA 1 ATOM 3914 C C . SER A 1 539 ? 15.960 55.777 54.740 1.00 16.36 ? 532 SER A C 1 ATOM 3915 O O . SER A 1 539 ? 16.795 56.695 54.530 1.00 16.15 ? 532 SER A O 1 ATOM 3916 C CB . SER A 1 539 ? 13.961 55.619 53.229 1.00 15.62 ? 532 SER A CB 1 ATOM 3917 O OG . SER A 1 539 ? 12.548 55.670 53.162 1.00 16.21 ? 532 SER A OG 1 ATOM 3918 N N . GLY A 1 540 ? 16.314 54.531 55.059 1.00 15.37 ? 533 GLY A N 1 ATOM 3919 C CA . GLY A 1 540 ? 17.734 54.148 55.084 1.00 15.63 ? 533 GLY A CA 1 ATOM 3920 C C . GLY A 1 540 ? 17.914 52.660 54.810 1.00 16.29 ? 533 GLY A C 1 ATOM 3921 O O . GLY A 1 540 ? 16.957 51.874 54.830 1.00 17.22 ? 533 GLY A O 1 ATOM 3922 N N . ARG A 1 541 ? 19.155 52.285 54.560 1.00 16.65 ? 534 ARG A N 1 ATOM 3923 C CA . ARG A 1 541 ? 19.533 50.889 54.327 1.00 16.54 ? 534 ARG A CA 1 ATOM 3924 C C . ARG A 1 541 ? 20.997 50.708 54.757 1.00 18.00 ? 534 ARG A C 1 ATOM 3925 O O . ARG A 1 541 ? 21.777 51.673 54.774 1.00 18.56 ? 534 ARG A O 1 ATOM 3926 C CB . ARG A 1 541 ? 19.368 50.549 52.837 1.00 17.59 ? 534 ARG A CB 1 ATOM 3927 C CG . ARG A 1 541 ? 20.381 51.276 51.954 1.00 19.69 ? 534 ARG A CG 1 ATOM 3928 C CD . ARG A 1 541 ? 20.061 51.154 50.474 1.00 22.50 ? 534 ARG A CD 1 ATOM 3929 N NE . ARG A 1 541 ? 19.921 49.756 50.038 1.00 26.62 ? 534 ARG A NE 1 ATOM 3930 C CZ . ARG A 1 541 ? 19.980 49.362 48.772 1.00 25.46 ? 534 ARG A CZ 1 ATOM 3931 N NH1 . ARG A 1 541 ? 19.813 48.084 48.474 1.00 24.22 ? 534 ARG A NH1 1 ATOM 3932 N NH2 . ARG A 1 541 ? 20.180 50.253 47.797 1.00 26.96 ? 534 ARG A NH2 1 ATOM 3933 N N . ALA A 1 542 ? 21.363 49.482 55.111 1.00 17.11 ? 535 ALA A N 1 ATOM 3934 C CA . ALA A 1 542 ? 22.748 49.167 55.527 1.00 17.73 ? 535 ALA A CA 1 ATOM 3935 C C . ALA A 1 542 ? 23.053 47.728 55.199 1.00 18.30 ? 535 ALA A C 1 ATOM 3936 O O . ALA A 1 542 ? 22.173 46.865 55.286 1.00 19.15 ? 535 ALA A O 1 ATOM 3937 C CB . ALA A 1 542 ? 22.909 49.383 57.021 1.00 18.59 ? 535 ALA A CB 1 ATOM 3938 N N . ARG A 1 543 ? 24.299 47.467 54.817 1.00 18.51 ? 536 ARG A N 1 ATOM 3939 C CA . ARG A 1 543 ? 24.754 46.092 54.567 1.00 18.42 ? 536 ARG A CA 1 ATOM 3940 C C . ARG A 1 543 ? 26.249 46.049 54.639 1.00 20.01 ? 536 ARG A C 1 ATOM 3941 O O . ARG A 1 543 ? 26.912 47.110 54.672 1.00 20.57 ? 536 ARG A O 1 ATOM 3942 C CB . ARG A 1 543 ? 24.300 45.597 53.171 1.00 18.97 ? 536 ARG A CB 1 ATOM 3943 C CG . ARG A 1 543 ? 24.843 46.409 51.992 1.00 20.41 ? 536 ARG A CG 1 ATOM 3944 C CD . ARG A 1 543 ? 24.525 45.732 50.668 1.00 21.57 ? 536 ARG A CD 1 ATOM 3945 N NE . ARG A 1 543 ? 23.071 45.529 50.507 1.00 22.66 ? 536 ARG A NE 1 ATOM 3946 C CZ . ARG A 1 543 ? 22.431 45.384 49.355 1.00 23.79 ? 536 ARG A CZ 1 ATOM 3947 N NH1 . ARG A 1 543 ? 23.096 45.420 48.211 1.00 27.06 ? 536 ARG A NH1 1 ATOM 3948 N NH2 . ARG A 1 543 ? 21.105 45.192 49.350 1.00 21.93 ? 536 ARG A NH2 1 ATOM 3949 N N . TYR A 1 544 ? 26.798 44.836 54.664 1.00 20.12 ? 537 TYR A N 1 ATOM 3950 C CA . TYR A 1 544 ? 28.234 44.686 54.509 1.00 20.48 ? 537 TYR A CA 1 ATOM 3951 C C . TYR A 1 544 ? 28.585 44.640 53.028 1.00 21.35 ? 537 TYR A C 1 ATOM 3952 O O . TYR A 1 544 ? 27.822 44.111 52.213 1.00 21.14 ? 537 TYR A O 1 ATOM 3953 C CB . TYR A 1 544 ? 28.802 43.488 55.307 1.00 20.47 ? 537 TYR A CB 1 ATOM 3954 C CG . TYR A 1 544 ? 29.723 43.975 56.411 1.00 21.32 ? 537 TYR A CG 1 ATOM 3955 C CD1 . TYR A 1 544 ? 29.208 44.716 57.483 1.00 21.22 ? 537 TYR A CD1 1 ATOM 3956 C CD2 . TYR A 1 544 ? 31.103 43.753 56.360 1.00 21.04 ? 537 TYR A CD2 1 ATOM 3957 C CE1 . TYR A 1 544 ? 30.029 45.208 58.477 1.00 22.94 ? 537 TYR A CE1 1 ATOM 3958 C CE2 . TYR A 1 544 ? 31.947 44.241 57.363 1.00 21.93 ? 537 TYR A CE2 1 ATOM 3959 C CZ . TYR A 1 544 ? 31.396 44.971 58.420 1.00 22.40 ? 537 TYR A CZ 1 ATOM 3960 O OH . TYR A 1 544 ? 32.185 45.487 59.424 1.00 25.93 ? 537 TYR A OH 1 ATOM 3961 N N . THR A 1 545 ? 29.723 45.232 52.689 1.00 22.54 ? 538 THR A N 1 ATOM 3962 C CA . THR A 1 545 ? 30.102 45.419 51.284 1.00 22.89 ? 538 THR A CA 1 ATOM 3963 C C . THR A 1 545 ? 31.578 45.090 51.073 1.00 24.30 ? 538 THR A C 1 ATOM 3964 O O . THR A 1 545 ? 32.297 44.813 52.031 1.00 22.63 ? 538 THR A O 1 ATOM 3965 C CB . THR A 1 545 ? 29.787 46.859 50.807 1.00 23.29 ? 538 THR A CB 1 ATOM 3966 O OG1 . THR A 1 545 ? 29.859 46.916 49.375 1.00 24.00 ? 538 THR A OG1 1 ATOM 3967 C CG2 . THR A 1 545 ? 30.783 47.862 51.420 1.00 23.01 ? 538 THR A CG2 1 ATOM 3968 N N . LYS A 1 546 ? 32.005 45.108 49.811 1.00 26.45 ? 539 LYS A N 1 ATOM 3969 C CA . LYS A 1 546 ? 33.396 44.854 49.436 1.00 27.17 ? 539 LYS A CA 1 ATOM 3970 C C . LYS A 1 546 ? 34.233 46.137 49.536 1.00 28.15 ? 539 LYS A C 1 ATOM 3971 O O . LYS A 1 546 ? 33.702 47.217 49.851 1.00 27.28 ? 539 LYS A O 1 ATOM 3972 C CB . LYS A 1 546 ? 33.450 44.283 48.008 1.00 28.48 ? 539 LYS A CB 1 ATOM 3973 C CG . LYS A 1 546 ? 32.987 45.255 46.931 1.00 31.77 ? 539 LYS A CG 1 ATOM 3974 C CD . LYS A 1 546 ? 33.011 44.607 45.552 1.00 38.91 ? 539 LYS A CD 1 ATOM 3975 C CE . LYS A 1 546 ? 32.340 45.532 44.548 1.00 46.10 ? 539 LYS A CE 1 ATOM 3976 N NZ . LYS A 1 546 ? 32.055 44.872 43.252 0.50 44.55 ? 539 LYS A NZ 1 ATOM 3977 N N . ASN A 1 547 ? 35.533 45.998 49.277 1.00 30.35 ? 540 ASN A N 1 ATOM 3978 C CA . ASN A 1 547 ? 36.461 47.130 49.174 1.00 33.02 ? 540 ASN A CA 1 ATOM 3979 C C . ASN A 1 547 ? 36.368 47.736 47.776 1.00 37.42 ? 540 ASN A C 1 ATOM 3980 O O . ASN A 1 547 ? 36.900 47.171 46.811 1.00 42.12 ? 540 ASN A O 1 ATOM 3981 C CB . ASN A 1 547 ? 37.899 46.671 49.461 1.00 35.89 ? 540 ASN A CB 1 ATOM 3982 C CG . ASN A 1 547 ? 38.902 47.824 49.467 1.00 36.05 ? 540 ASN A CG 1 ATOM 3983 O OD1 . ASN A 1 547 ? 38.617 48.935 48.998 1.00 39.46 ? 540 ASN A OD1 1 ATOM 3984 N ND2 . ASN A 1 547 ? 40.092 47.559 50.004 1.00 38.68 ? 540 ASN A ND2 1 ATOM 3985 N N A TRP A 1 548 ? 35.715 48.903 47.705 0.50 37.24 ? 541 TRP A N 1 ATOM 3986 N N B TRP A 1 548 ? 35.692 48.870 47.652 0.50 37.57 ? 541 TRP A N 1 ATOM 3987 C CA A TRP A 1 548 ? 35.425 49.659 46.469 0.50 42.53 ? 541 TRP A CA 1 ATOM 3988 C CA B TRP A 1 548 ? 35.483 49.449 46.330 0.50 43.64 ? 541 TRP A CA 1 ATOM 3989 C C A TRP A 1 548 ? 36.637 50.255 45.801 0.50 47.75 ? 541 TRP A C 1 ATOM 3990 C C B TRP A 1 548 ? 36.753 49.976 45.706 0.50 46.48 ? 541 TRP A C 1 ATOM 3991 O O A TRP A 1 548 ? 36.572 50.672 44.644 0.50 49.60 ? 541 TRP A O 1 ATOM 3992 O O B TRP A 1 548 ? 36.856 50.036 44.479 0.50 53.27 ? 541 TRP A O 1 ATOM 3993 C CB A TRP A 1 548 ? 34.438 50.783 46.788 0.50 45.71 ? 541 TRP A CB 1 ATOM 3994 C CB B TRP A 1 548 ? 34.347 50.465 46.355 0.50 46.41 ? 541 TRP A CB 1 ATOM 3995 C CG A TRP A 1 548 ? 34.120 51.733 45.646 0.50 45.79 ? 541 TRP A CG 1 ATOM 3996 C CG B TRP A 1 548 ? 33.016 49.786 46.603 0.50 47.13 ? 541 TRP A CG 1 ATOM 3997 C CD1 A TRP A 1 548 ? 32.887 51.924 45.019 0.50 45.27 ? 541 TRP A CD1 1 ATOM 3998 C CD1 B TRP A 1 548 ? 32.423 49.500 47.833 0.50 43.32 ? 541 TRP A CD1 1 ATOM 3999 C CD2 A TRP A 1 548 ? 35.034 52.681 44.976 0.50 46.29 ? 541 TRP A CD2 1 ATOM 4000 C CD2 B TRP A 1 548 ? 32.088 49.237 45.596 0.50 49.02 ? 541 TRP A CD2 1 ATOM 4001 N NE1 A TRP A 1 548 ? 32.977 52.882 44.037 0.50 44.36 ? 541 TRP A NE1 1 ATOM 4002 N NE1 B TRP A 1 548 ? 31.228 48.853 47.662 0.50 35.68 ? 541 TRP A NE1 1 ATOM 4003 C CE2 A TRP A 1 548 ? 34.235 53.372 43.957 0.50 44.94 ? 541 TRP A CE2 1 ATOM 4004 C CE2 B TRP A 1 548 ? 30.966 48.664 46.345 0.50 49.63 ? 541 TRP A CE2 1 ATOM 4005 C CE3 A TRP A 1 548 ? 36.380 53.001 45.105 0.50 48.65 ? 541 TRP A CE3 1 ATOM 4006 C CE3 B TRP A 1 548 ? 32.071 49.179 44.206 0.50 47.39 ? 541 TRP A CE3 1 ATOM 4007 C CZ2 A TRP A 1 548 ? 34.782 54.336 43.125 0.50 44.45 ? 541 TRP A CZ2 1 ATOM 4008 C CZ2 B TRP A 1 548 ? 29.883 48.069 45.708 0.50 49.25 ? 541 TRP A CZ2 1 ATOM 4009 C CZ3 A TRP A 1 548 ? 36.919 53.977 44.261 0.50 50.29 ? 541 TRP A CZ3 1 ATOM 4010 C CZ3 B TRP A 1 548 ? 30.978 48.575 43.579 0.50 50.59 ? 541 TRP A CZ3 1 ATOM 4011 C CH2 A TRP A 1 548 ? 36.137 54.625 43.293 0.50 51.43 ? 541 TRP A CH2 1 ATOM 4012 C CH2 B TRP A 1 548 ? 29.913 48.032 44.314 0.50 49.47 ? 541 TRP A CH2 1 ATOM 4013 N N . GLU A 1 549 ? 37.742 50.320 46.537 1.00 47.14 ? 542 GLU A N 1 ATOM 4014 C CA . GLU A 1 549 ? 39.018 50.855 46.038 1.00 48.25 ? 542 GLU A CA 1 ATOM 4015 C C . GLU A 1 549 ? 39.809 49.795 45.267 1.00 54.36 ? 542 GLU A C 1 ATOM 4016 O O . GLU A 1 549 ? 40.418 50.087 44.231 1.00 65.00 ? 542 GLU A O 1 ATOM 4017 C CB . GLU A 1 549 ? 39.867 51.416 47.188 1.00 51.52 ? 542 GLU A CB 1 ATOM 4018 C CG . GLU A 1 549 ? 39.259 52.620 47.908 1.00 50.41 ? 542 GLU A CG 1 ATOM 4019 C CD . GLU A 1 549 ? 39.345 53.917 47.111 0.50 52.31 ? 542 GLU A CD 1 ATOM 4020 O OE1 . GLU A 1 549 ? 40.262 54.059 46.274 0.50 55.84 ? 542 GLU A OE1 1 ATOM 4021 O OE2 . GLU A 1 549 ? 38.495 54.807 47.329 0.50 54.14 ? 542 GLU A OE2 1 ATOM 4022 N N . THR A 1 550 ? 39.778 48.563 45.767 1.00 48.46 ? 543 THR A N 1 ATOM 4023 C CA . THR A 1 550 ? 40.573 47.478 45.196 1.00 53.21 ? 543 THR A CA 1 ATOM 4024 C C . THR A 1 550 ? 39.733 46.493 44.370 1.00 54.88 ? 543 THR A C 1 ATOM 4025 O O . THR A 1 550 ? 40.277 45.728 43.572 1.00 59.96 ? 543 THR A O 1 ATOM 4026 C CB . THR A 1 550 ? 41.377 46.726 46.289 1.00 53.81 ? 543 THR A CB 1 ATOM 4027 O OG1 . THR A 1 550 ? 40.476 46.123 47.230 1.00 52.81 ? 543 THR A OG1 1 ATOM 4028 C CG2 . THR A 1 550 ? 42.322 47.683 47.030 1.00 53.88 ? 543 THR A CG2 1 ATOM 4029 N N . ASN A 1 551 ? 38.415 46.512 44.554 1.00 50.79 ? 544 ASN A N 1 ATOM 4030 C CA . ASN A 1 551 ? 37.528 45.591 43.821 1.00 54.66 ? 544 ASN A CA 1 ATOM 4031 C C . ASN A 1 551 ? 36.714 46.308 42.755 1.00 57.32 ? 544 ASN A C 1 ATOM 4032 O O . ASN A 1 551 ? 35.666 46.906 43.048 1.00 61.51 ? 544 ASN A O 1 ATOM 4033 C CB . ASN A 1 551 ? 36.598 44.824 44.773 1.00 51.32 ? 544 ASN A CB 1 ATOM 4034 C CG . ASN A 1 551 ? 37.356 44.044 45.838 1.00 56.09 ? 544 ASN A CG 1 ATOM 4035 O OD1 . ASN A 1 551 ? 38.394 43.422 45.565 1.00 65.08 ? 544 ASN A OD1 1 ATOM 4036 N ND2 . ASN A 1 551 ? 36.832 44.063 47.064 1.00 46.41 ? 544 ASN A ND2 1 ATOM 4037 N N . LYS A 1 552 ? 37.201 46.232 41.517 1.00 53.28 ? 545 LYS A N 1 ATOM 4038 C CA . LYS A 1 552 ? 36.625 46.996 40.410 1.00 56.20 ? 545 LYS A CA 1 ATOM 4039 C C . LYS A 1 552 ? 35.541 46.254 39.610 0.50 49.74 ? 545 LYS A C 1 ATOM 4040 O O . LYS A 1 552 ? 35.019 46.774 38.620 0.60 48.75 ? 545 LYS A O 1 ATOM 4041 C CB . LYS A 1 552 ? 37.738 47.545 39.508 1.00 60.40 ? 545 LYS A CB 1 ATOM 4042 C CG . LYS A 1 552 ? 38.592 48.619 40.180 1.00 64.93 ? 545 LYS A CG 1 ATOM 4043 C CD . LYS A 1 552 ? 37.751 49.813 40.628 1.00 64.05 ? 545 LYS A CD 1 ATOM 4044 C CE . LYS A 1 552 ? 38.557 50.805 41.452 1.00 67.12 ? 545 LYS A CE 1 ATOM 4045 N NZ . LYS A 1 552 ? 37.700 51.923 41.945 1.00 60.72 ? 545 LYS A NZ 1 ATOM 4046 N N . PHE A 1 553 ? 35.198 45.047 40.058 1.00 46.81 ? 546 PHE A N 1 ATOM 4047 C CA . PHE A 1 553 ? 34.055 44.310 39.506 1.00 41.42 ? 546 PHE A CA 1 ATOM 4048 C C . PHE A 1 553 ? 32.714 44.894 40.002 1.00 43.83 ? 546 PHE A C 1 ATOM 4049 O O . PHE A 1 553 ? 32.683 45.736 40.912 1.00 39.18 ? 546 PHE A O 1 ATOM 4050 C CB . PHE A 1 553 ? 34.177 42.797 39.764 1.00 45.05 ? 546 PHE A CB 1 ATOM 4051 C CG . PHE A 1 553 ? 34.382 42.427 41.209 1.00 49.82 ? 546 PHE A CG 1 ATOM 4052 C CD1 . PHE A 1 553 ? 35.675 42.311 41.744 1.00 46.12 ? 546 PHE A CD1 1 ATOM 4053 C CD2 . PHE A 1 553 ? 33.286 42.164 42.034 1.00 41.86 ? 546 PHE A CD2 1 ATOM 4054 C CE1 . PHE A 1 553 ? 35.862 41.965 43.082 1.00 47.75 ? 546 PHE A CE1 1 ATOM 4055 C CE2 . PHE A 1 553 ? 33.463 41.818 43.368 1.00 43.96 ? 546 PHE A CE2 1 ATOM 4056 C CZ . PHE A 1 553 ? 34.754 41.724 43.895 1.00 46.99 ? 546 PHE A CZ 1 ATOM 4057 N N . SER A 1 554 ? 31.617 44.434 39.397 1.00 39.71 ? 547 SER A N 1 ATOM 4058 C CA . SER A 1 554 ? 30.294 45.041 39.547 1.00 41.50 ? 547 SER A CA 1 ATOM 4059 C C . SER A 1 554 ? 29.413 44.289 40.569 1.00 39.51 ? 547 SER A C 1 ATOM 4060 O O . SER A 1 554 ? 29.008 43.155 40.310 1.00 42.41 ? 547 SER A O 1 ATOM 4061 C CB . SER A 1 554 ? 29.622 45.052 38.161 1.00 39.01 ? 547 SER A CB 1 ATOM 4062 O OG . SER A 1 554 ? 28.370 45.707 38.196 1.00 50.73 ? 547 SER A OG 1 ATOM 4063 N N . GLY A 1 555 ? 29.114 44.911 41.717 1.00 40.13 ? 548 GLY A N 1 ATOM 4064 C CA . GLY A 1 555 ? 28.273 44.275 42.756 1.00 37.68 ? 548 GLY A CA 1 ATOM 4065 C C . GLY A 1 555 ? 28.946 43.024 43.289 0.75 34.68 ? 548 GLY A C 1 ATOM 4066 O O . GLY A 1 555 ? 30.140 43.048 43.576 1.00 38.98 ? 548 GLY A O 1 ATOM 4067 N N . TYR A 1 556 ? 28.212 41.914 43.398 1.00 29.71 ? 549 TYR A N 1 ATOM 4068 C CA . TYR A 1 556 ? 28.877 40.624 43.670 1.00 25.55 ? 549 TYR A CA 1 ATOM 4069 C C . TYR A 1 556 ? 28.694 39.680 42.470 1.00 22.91 ? 549 TYR A C 1 ATOM 4070 O O . TYR A 1 556 ? 27.635 39.710 41.821 1.00 21.30 ? 549 TYR A O 1 ATOM 4071 C CB . TYR A 1 556 ? 28.361 39.999 44.967 1.00 26.26 ? 549 TYR A CB 1 ATOM 4072 C CG . TYR A 1 556 ? 26.870 39.717 45.005 1.00 23.79 ? 549 TYR A CG 1 ATOM 4073 C CD1 . TYR A 1 556 ? 26.379 38.435 44.762 1.00 21.15 ? 549 TYR A CD1 1 ATOM 4074 C CD2 . TYR A 1 556 ? 25.950 40.741 45.294 1.00 20.51 ? 549 TYR A CD2 1 ATOM 4075 C CE1 . TYR A 1 556 ? 25.006 38.168 44.827 1.00 18.17 ? 549 TYR A CE1 1 ATOM 4076 C CE2 . TYR A 1 556 ? 24.586 40.489 45.343 1.00 20.71 ? 549 TYR A CE2 1 ATOM 4077 C CZ . TYR A 1 556 ? 24.116 39.211 45.090 1.00 19.20 ? 549 TYR A CZ 1 ATOM 4078 O OH . TYR A 1 556 ? 22.764 38.961 45.143 1.00 19.70 ? 549 TYR A OH 1 ATOM 4079 N N . PRO A 1 557 ? 29.698 38.832 42.179 1.00 20.05 ? 550 PRO A N 1 ATOM 4080 C CA . PRO A 1 557 ? 29.631 38.131 40.878 1.00 20.42 ? 550 PRO A CA 1 ATOM 4081 C C . PRO A 1 557 ? 28.439 37.216 40.615 1.00 18.29 ? 550 PRO A C 1 ATOM 4082 O O . PRO A 1 557 ? 28.015 37.095 39.470 1.00 19.65 ? 550 PRO A O 1 ATOM 4083 C CB . PRO A 1 557 ? 30.920 37.298 40.866 1.00 20.10 ? 550 PRO A CB 1 ATOM 4084 C CG . PRO A 1 557 ? 31.879 38.133 41.681 1.00 21.06 ? 550 PRO A CG 1 ATOM 4085 C CD . PRO A 1 557 ? 31.040 38.687 42.803 1.00 22.76 ? 550 PRO A CD 1 ATOM 4086 N N . LEU A 1 558 ? 27.910 36.565 41.651 1.00 18.24 ? 551 LEU A N 1 ATOM 4087 C CA . LEU A 1 558 ? 26.876 35.528 41.452 1.00 17.37 ? 551 LEU A CA 1 ATOM 4088 C C . LEU A 1 558 ? 25.450 36.059 41.562 1.00 17.38 ? 551 LEU A C 1 ATOM 4089 O O . LEU A 1 558 ? 24.476 35.289 41.571 1.00 19.25 ? 551 LEU A O 1 ATOM 4090 C CB . LEU A 1 558 ? 27.094 34.378 42.426 1.00 16.02 ? 551 LEU A CB 1 ATOM 4091 C CG . LEU A 1 558 ? 28.409 33.659 42.118 1.00 16.31 ? 551 LEU A CG 1 ATOM 4092 C CD1 . LEU A 1 558 ? 28.747 32.638 43.194 1.00 20.18 ? 551 LEU A CD1 1 ATOM 4093 C CD2 . LEU A 1 558 ? 28.373 32.995 40.749 1.00 19.24 ? 551 LEU A CD2 1 ATOM 4094 N N . TYR A 1 559 ? 25.346 37.384 41.638 1.00 17.46 ? 552 TYR A N 1 ATOM 4095 C CA . TYR A 1 559 ? 24.073 38.113 41.636 1.00 16.69 ? 552 TYR A CA 1 ATOM 4096 C C . TYR A 1 559 ? 23.051 37.569 40.627 1.00 17.01 ? 552 TYR A C 1 ATOM 4097 O O . TYR A 1 559 ? 23.326 37.514 39.414 1.00 17.85 ? 552 TYR A O 1 ATOM 4098 C CB . TYR A 1 559 ? 24.406 39.577 41.373 1.00 16.63 ? 552 TYR A CB 1 ATOM 4099 C CG . TYR A 1 559 ? 23.243 40.509 41.134 1.00 17.69 ? 552 TYR A CG 1 ATOM 4100 C CD1 . TYR A 1 559 ? 22.312 40.780 42.140 1.00 17.52 ? 552 TYR A CD1 1 ATOM 4101 C CD2 . TYR A 1 559 ? 23.113 41.168 39.913 1.00 18.10 ? 552 TYR A CD2 1 ATOM 4102 C CE1 . TYR A 1 559 ? 21.260 41.681 41.929 1.00 16.27 ? 552 TYR A CE1 1 ATOM 4103 C CE2 . TYR A 1 559 ? 22.080 42.067 39.692 1.00 16.57 ? 552 TYR A CE2 1 ATOM 4104 C CZ . TYR A 1 559 ? 21.150 42.312 40.693 1.00 16.96 ? 552 TYR A CZ 1 ATOM 4105 O OH . TYR A 1 559 ? 20.127 43.196 40.449 1.00 17.71 ? 552 TYR A OH 1 ATOM 4106 N N . HIS A 1 560 ? 21.889 37.146 41.133 1.00 16.62 ? 553 HIS A N 1 ATOM 4107 C CA . HIS A 1 560 ? 20.732 36.725 40.286 1.00 16.32 ? 553 HIS A CA 1 ATOM 4108 C C . HIS A 1 560 ? 20.977 35.475 39.461 1.00 17.19 ? 553 HIS A C 1 ATOM 4109 O O . HIS A 1 560 ? 20.265 35.210 38.473 1.00 18.24 ? 553 HIS A O 1 ATOM 4110 C CB . HIS A 1 560 ? 20.234 37.868 39.391 1.00 16.17 ? 553 HIS A CB 1 ATOM 4111 C CG . HIS A 1 560 ? 19.442 38.941 40.127 1.00 15.19 ? 553 HIS A CG 1 ATOM 4112 N ND1 . HIS A 1 560 ? 18.828 39.947 39.474 1.00 15.27 ? 553 HIS A ND1 1 ATOM 4113 C CD2 . HIS A 1 560 ? 19.187 39.142 41.482 1.00 15.96 ? 553 HIS A CD2 1 ATOM 4114 C CE1 . HIS A 1 560 ? 18.215 40.756 40.355 1.00 15.41 ? 553 HIS A CE1 1 ATOM 4115 N NE2 . HIS A 1 560 ? 18.411 40.252 41.580 1.00 15.49 ? 553 HIS A NE2 1 ATOM 4116 N N . SER A 1 561 ? 21.983 34.703 39.866 1.00 18.12 ? 554 SER A N 1 ATOM 4117 C CA . SER A 1 561 ? 22.305 33.413 39.245 1.00 16.22 ? 554 SER A CA 1 ATOM 4118 C C . SER A 1 561 ? 21.866 32.226 40.121 1.00 18.41 ? 554 SER A C 1 ATOM 4119 O O . SER A 1 561 ? 21.633 32.388 41.285 1.00 17.82 ? 554 SER A O 1 ATOM 4120 C CB . SER A 1 561 ? 23.820 33.345 38.998 1.00 15.21 ? 554 SER A CB 1 ATOM 4121 O OG A SER A 1 561 ? 24.551 33.023 40.167 0.50 17.45 ? 554 SER A OG 1 ATOM 4122 O OG B SER A 1 561 ? 24.297 32.029 38.815 0.50 18.54 ? 554 SER A OG 1 ATOM 4123 N N . VAL A 1 562 ? 21.765 31.047 39.507 1.00 16.75 ? 555 VAL A N 1 ATOM 4124 C CA . VAL A 1 562 ? 21.444 29.813 40.237 1.00 17.39 ? 555 VAL A CA 1 ATOM 4125 C C . VAL A 1 562 ? 22.480 29.530 41.343 1.00 18.97 ? 555 VAL A C 1 ATOM 4126 O O . VAL A 1 562 ? 22.194 28.782 42.293 1.00 20.21 ? 555 VAL A O 1 ATOM 4127 C CB . VAL A 1 562 ? 21.343 28.617 39.267 1.00 19.24 ? 555 VAL A CB 1 ATOM 4128 C CG1 . VAL A 1 562 ? 22.733 28.158 38.803 1.00 19.98 ? 555 VAL A CG1 1 ATOM 4129 C CG2 . VAL A 1 562 ? 20.581 27.463 39.905 1.00 18.42 ? 555 VAL A CG2 1 ATOM 4130 N N . TYR A 1 563 ? 23.673 30.131 41.224 1.00 17.33 ? 556 TYR A N 1 ATOM 4131 C CA . TYR A 1 563 ? 24.784 29.803 42.130 1.00 18.71 ? 556 TYR A CA 1 ATOM 4132 C C . TYR A 1 563 ? 24.706 30.553 43.444 1.00 20.45 ? 556 TYR A C 1 ATOM 4133 O O . TYR A 1 563 ? 25.493 30.281 44.356 1.00 21.45 ? 556 TYR A O 1 ATOM 4134 C CB . TYR A 1 563 ? 26.161 30.013 41.448 1.00 18.54 ? 556 TYR A CB 1 ATOM 4135 C CG . TYR A 1 563 ? 26.254 29.227 40.175 1.00 19.37 ? 556 TYR A CG 1 ATOM 4136 C CD1 . TYR A 1 563 ? 26.217 27.816 40.189 1.00 20.24 ? 556 TYR A CD1 1 ATOM 4137 C CD2 . TYR A 1 563 ? 26.329 29.871 38.949 1.00 19.15 ? 556 TYR A CD2 1 ATOM 4138 C CE1 . TYR A 1 563 ? 26.253 27.084 39.009 1.00 21.16 ? 556 TYR A CE1 1 ATOM 4139 C CE2 . TYR A 1 563 ? 26.379 29.138 37.758 1.00 19.24 ? 556 TYR A CE2 1 ATOM 4140 C CZ . TYR A 1 563 ? 26.354 27.752 37.798 1.00 21.25 ? 556 TYR A CZ 1 ATOM 4141 O OH . TYR A 1 563 ? 26.371 27.021 36.629 1.00 22.52 ? 556 TYR A OH 1 ATOM 4142 N N . GLU A 1 564 ? 23.756 31.492 43.536 1.00 18.98 ? 557 GLU A N 1 ATOM 4143 C CA . GLU A 1 564 ? 23.556 32.264 44.740 1.00 20.14 ? 557 GLU A CA 1 ATOM 4144 C C . GLU A 1 564 ? 22.793 31.405 45.748 1.00 19.52 ? 557 GLU A C 1 ATOM 4145 O O . GLU A 1 564 ? 21.566 31.413 45.791 1.00 21.47 ? 557 GLU A O 1 ATOM 4146 C CB . GLU A 1 564 ? 22.767 33.523 44.380 1.00 22.62 ? 557 GLU A CB 1 ATOM 4147 C CG . GLU A 1 564 ? 23.235 34.722 45.083 1.00 27.58 ? 557 GLU A CG 1 ATOM 4148 C CD . GLU A 1 564 ? 22.152 35.763 45.032 1.00 22.95 ? 557 GLU A CD 1 ATOM 4149 O OE1 . GLU A 1 564 ? 22.082 36.567 44.080 1.00 25.70 ? 557 GLU A OE1 1 ATOM 4150 O OE2 . GLU A 1 564 ? 21.322 35.691 45.914 1.00 20.25 ? 557 GLU A OE2 1 ATOM 4151 N N . THR A 1 565 ? 23.538 30.670 46.569 1.00 19.15 ? 558 THR A N 1 ATOM 4152 C CA . THR A 1 565 ? 22.985 29.630 47.430 1.00 18.87 ? 558 THR A CA 1 ATOM 4153 C C . THR A 1 565 ? 23.379 29.864 48.882 1.00 18.99 ? 558 THR A C 1 ATOM 4154 O O . THR A 1 565 ? 24.259 30.691 49.173 1.00 18.13 ? 558 THR A O 1 ATOM 4155 C CB . THR A 1 565 ? 23.577 28.262 47.041 1.00 19.79 ? 558 THR A CB 1 ATOM 4156 O OG1 . THR A 1 565 ? 25.009 28.355 47.070 1.00 21.13 ? 558 THR A OG1 1 ATOM 4157 C CG2 . THR A 1 565 ? 23.121 27.825 45.629 1.00 21.23 ? 558 THR A CG2 1 ATOM 4158 N N . TYR A 1 566 ? 22.771 29.085 49.782 1.00 19.28 ? 559 TYR A N 1 ATOM 4159 C CA . TYR A 1 566 ? 23.219 29.022 51.168 1.00 20.95 ? 559 TYR A CA 1 ATOM 4160 C C . TYR A 1 566 ? 24.727 28.737 51.245 1.00 20.04 ? 559 TYR A C 1 ATOM 4161 O O . TYR A 1 566 ? 25.441 29.379 52.010 1.00 20.70 ? 559 TYR A O 1 ATOM 4162 C CB . TYR A 1 566 ? 22.456 27.935 51.940 1.00 19.68 ? 559 TYR A CB 1 ATOM 4163 C CG . TYR A 1 566 ? 23.010 27.708 53.328 1.00 20.78 ? 559 TYR A CG 1 ATOM 4164 C CD1 . TYR A 1 566 ? 22.700 28.585 54.369 1.00 21.96 ? 559 TYR A CD1 1 ATOM 4165 C CD2 . TYR A 1 566 ? 23.872 26.633 53.596 1.00 22.45 ? 559 TYR A CD2 1 ATOM 4166 C CE1 . TYR A 1 566 ? 23.203 28.386 55.654 1.00 23.53 ? 559 TYR A CE1 1 ATOM 4167 C CE2 . TYR A 1 566 ? 24.397 26.433 54.875 1.00 24.38 ? 559 TYR A CE2 1 ATOM 4168 C CZ . TYR A 1 566 ? 24.064 27.314 55.898 1.00 24.72 ? 559 TYR A CZ 1 ATOM 4169 O OH . TYR A 1 566 ? 24.569 27.108 57.171 1.00 26.82 ? 559 TYR A OH 1 ATOM 4170 N N . GLU A 1 567 ? 25.214 27.789 50.440 1.00 19.39 ? 560 GLU A N 1 ATOM 4171 C CA . GLU A 1 567 ? 26.623 27.408 50.540 1.00 20.69 ? 560 GLU A CA 1 ATOM 4172 C C . GLU A 1 567 ? 27.558 28.548 50.146 1.00 20.50 ? 560 GLU A C 1 ATOM 4173 O O . GLU A 1 567 ? 28.639 28.699 50.721 1.00 22.60 ? 560 GLU A O 1 ATOM 4174 C CB . GLU A 1 567 ? 26.915 26.156 49.704 1.00 22.75 ? 560 GLU A CB 1 ATOM 4175 C CG . GLU A 1 567 ? 26.274 24.891 50.241 1.00 24.40 ? 560 GLU A CG 1 ATOM 4176 C CD . GLU A 1 567 ? 24.774 24.833 49.995 1.00 22.63 ? 560 GLU A CD 1 ATOM 4177 O OE1 . GLU A 1 567 ? 24.292 25.400 48.998 1.00 23.77 ? 560 GLU A OE1 1 ATOM 4178 O OE2 . GLU A 1 567 ? 24.069 24.214 50.802 1.00 25.60 ? 560 GLU A OE2 1 ATOM 4179 N N . LEU A 1 568 ? 27.144 29.344 49.166 1.00 20.05 ? 561 LEU A N 1 ATOM 4180 C CA . LEU A 1 568 ? 27.904 30.521 48.772 1.00 18.92 ? 561 LEU A CA 1 ATOM 4181 C C . LEU A 1 568 ? 28.189 31.401 49.981 1.00 19.75 ? 561 LEU A C 1 ATOM 4182 O O . LEU A 1 568 ? 29.333 31.833 50.187 1.00 21.27 ? 561 LEU A O 1 ATOM 4183 C CB . LEU A 1 568 ? 27.133 31.344 47.730 1.00 19.67 ? 561 LEU A CB 1 ATOM 4184 C CG . LEU A 1 568 ? 27.792 32.676 47.332 1.00 19.03 ? 561 LEU A CG 1 ATOM 4185 C CD1 . LEU A 1 568 ? 29.221 32.445 46.822 1.00 20.83 ? 561 LEU A CD1 1 ATOM 4186 C CD2 . LEU A 1 568 ? 26.925 33.425 46.319 1.00 21.16 ? 561 LEU A CD2 1 ATOM 4187 N N . VAL A 1 569 ? 27.139 31.688 50.754 1.00 19.23 ? 562 VAL A N 1 ATOM 4188 C CA . VAL A 1 569 ? 27.257 32.566 51.921 1.00 18.38 ? 562 VAL A CA 1 ATOM 4189 C C . VAL A 1 569 ? 28.085 31.892 53.049 1.00 21.03 ? 562 VAL A C 1 ATOM 4190 O O . VAL A 1 569 ? 29.040 32.481 53.584 1.00 21.87 ? 562 VAL A O 1 ATOM 4191 C CB . VAL A 1 569 ? 25.857 32.967 52.437 1.00 19.17 ? 562 VAL A CB 1 ATOM 4192 C CG1 . VAL A 1 569 ? 25.967 33.816 53.707 1.00 19.55 ? 562 VAL A CG1 1 ATOM 4193 C CG2 . VAL A 1 569 ? 25.098 33.748 51.363 1.00 21.50 ? 562 VAL A CG2 1 ATOM 4194 N N . GLU A 1 570 ? 27.710 30.662 53.402 1.00 21.63 ? 563 GLU A N 1 ATOM 4195 C CA . GLU A 1 570 ? 28.326 29.941 54.518 1.00 22.87 ? 563 GLU A CA 1 ATOM 4196 C C . GLU A 1 570 ? 29.804 29.622 54.256 1.00 24.02 ? 563 GLU A C 1 ATOM 4197 O O . GLU A 1 570 ? 30.625 29.673 55.169 1.00 26.40 ? 563 GLU A O 1 ATOM 4198 C CB . GLU A 1 570 ? 27.551 28.650 54.783 1.00 26.19 ? 563 GLU A CB 1 ATOM 4199 C CG . GLU A 1 570 ? 27.913 27.959 56.089 1.00 29.22 ? 563 GLU A CG 1 ATOM 4200 C CD . GLU A 1 570 ? 29.050 26.972 55.924 1.00 33.72 ? 563 GLU A CD 1 ATOM 4201 O OE1 . GLU A 1 570 ? 29.274 26.492 54.786 1.00 38.46 ? 563 GLU A OE1 1 ATOM 4202 O OE2 . GLU A 1 570 ? 29.730 26.676 56.933 1.00 37.95 ? 563 GLU A OE2 1 ATOM 4203 N N . LYS A 1 571 ? 30.139 29.312 53.006 1.00 23.11 ? 564 LYS A N 1 ATOM 4204 C CA . LYS A 1 571 ? 31.514 28.936 52.665 1.00 22.49 ? 564 LYS A CA 1 ATOM 4205 C C . LYS A 1 571 ? 32.422 30.140 52.403 1.00 23.84 ? 564 LYS A C 1 ATOM 4206 O O . LYS A 1 571 ? 33.570 30.137 52.830 1.00 27.04 ? 564 LYS A O 1 ATOM 4207 C CB . LYS A 1 571 ? 31.566 27.989 51.459 1.00 22.95 ? 564 LYS A CB 1 ATOM 4208 C CG . LYS A 1 571 ? 30.939 26.625 51.715 1.00 24.58 ? 564 LYS A CG 1 ATOM 4209 C CD . LYS A 1 571 ? 30.984 25.732 50.469 1.00 28.74 ? 564 LYS A CD 1 ATOM 4210 C CE . LYS A 1 571 ? 30.280 24.377 50.639 1.00 30.78 ? 564 LYS A CE 1 ATOM 4211 N NZ . LYS A 1 571 ? 30.801 23.663 51.826 1.00 36.11 ? 564 LYS A NZ 1 ATOM 4212 N N . PHE A 1 572 ? 31.906 31.152 51.704 1.00 23.64 ? 565 PHE A N 1 ATOM 4213 C CA . PHE A 1 572 ? 32.759 32.196 51.128 1.00 23.73 ? 565 PHE A CA 1 ATOM 4214 C C . PHE A 1 572 ? 32.555 33.591 51.708 1.00 25.63 ? 565 PHE A C 1 ATOM 4215 O O . PHE A 1 572 ? 33.521 34.343 51.833 1.00 32.67 ? 565 PHE A O 1 ATOM 4216 C CB . PHE A 1 572 ? 32.630 32.203 49.596 1.00 22.12 ? 565 PHE A CB 1 ATOM 4217 C CG . PHE A 1 572 ? 33.052 30.905 48.963 1.00 25.14 ? 565 PHE A CG 1 ATOM 4218 C CD1 . PHE A 1 572 ? 34.381 30.487 49.046 1.00 25.76 ? 565 PHE A CD1 1 ATOM 4219 C CD2 . PHE A 1 572 ? 32.127 30.086 48.296 1.00 24.09 ? 565 PHE A CD2 1 ATOM 4220 C CE1 . PHE A 1 572 ? 34.779 29.283 48.486 1.00 26.49 ? 565 PHE A CE1 1 ATOM 4221 C CE2 . PHE A 1 572 ? 32.525 28.871 47.732 1.00 27.18 ? 565 PHE A CE2 1 ATOM 4222 C CZ . PHE A 1 572 ? 33.848 28.475 47.824 1.00 28.83 ? 565 PHE A CZ 1 ATOM 4223 N N . TYR A 1 573 ? 31.322 33.947 52.067 1.00 22.49 ? 566 TYR A N 1 ATOM 4224 C CA . TYR A 1 573 ? 31.065 35.303 52.512 1.00 21.21 ? 566 TYR A CA 1 ATOM 4225 C C . TYR A 1 573 ? 31.143 35.494 54.020 1.00 22.96 ? 566 TYR A C 1 ATOM 4226 O O . TYR A 1 573 ? 31.778 36.443 54.498 1.00 23.41 ? 566 TYR A O 1 ATOM 4227 C CB . TYR A 1 573 ? 29.716 35.827 51.959 1.00 21.07 ? 566 TYR A CB 1 ATOM 4228 C CG . TYR A 1 573 ? 29.827 36.323 50.538 1.00 22.45 ? 566 TYR A CG 1 ATOM 4229 C CD1 . TYR A 1 573 ? 29.814 35.416 49.476 1.00 21.80 ? 566 TYR A CD1 1 ATOM 4230 C CD2 . TYR A 1 573 ? 29.969 37.697 50.247 1.00 22.45 ? 566 TYR A CD2 1 ATOM 4231 C CE1 . TYR A 1 573 ? 29.951 35.838 48.165 1.00 21.90 ? 566 TYR A CE1 1 ATOM 4232 C CE2 . TYR A 1 573 ? 30.108 38.135 48.929 1.00 24.80 ? 566 TYR A CE2 1 ATOM 4233 C CZ . TYR A 1 573 ? 30.105 37.190 47.897 1.00 22.57 ? 566 TYR A CZ 1 ATOM 4234 O OH . TYR A 1 573 ? 30.245 37.577 46.589 1.00 25.03 ? 566 TYR A OH 1 ATOM 4235 N N . ASP A 1 574 ? 30.497 34.614 54.780 1.00 20.48 ? 567 ASP A N 1 ATOM 4236 C CA . ASP A 1 574 ? 30.317 34.895 56.212 1.00 21.12 ? 567 ASP A CA 1 ATOM 4237 C C . ASP A 1 574 ? 30.146 33.609 57.011 1.00 21.60 ? 567 ASP A C 1 ATOM 4238 O O . ASP A 1 574 ? 29.077 33.385 57.589 1.00 22.73 ? 567 ASP A O 1 ATOM 4239 C CB . ASP A 1 574 ? 29.089 35.811 56.388 1.00 21.52 ? 567 ASP A CB 1 ATOM 4240 C CG . ASP A 1 574 ? 29.017 36.471 57.766 1.00 22.40 ? 567 ASP A CG 1 ATOM 4241 O OD1 . ASP A 1 574 ? 30.014 36.455 58.538 1.00 23.36 ? 567 ASP A OD1 1 ATOM 4242 O OD2 . ASP A 1 574 ? 27.936 37.024 58.074 1.00 21.40 ? 567 ASP A OD2 1 ATOM 4243 N N . PRO A 1 575 ? 31.200 32.763 57.067 1.00 23.59 ? 568 PRO A N 1 ATOM 4244 C CA . PRO A 1 575 ? 31.089 31.468 57.741 1.00 24.77 ? 568 PRO A CA 1 ATOM 4245 C C . PRO A 1 575 ? 30.575 31.534 59.175 1.00 25.24 ? 568 PRO A C 1 ATOM 4246 O O . PRO A 1 575 ? 29.841 30.634 59.601 1.00 28.15 ? 568 PRO A O 1 ATOM 4247 C CB . PRO A 1 575 ? 32.531 30.935 57.748 1.00 26.44 ? 568 PRO A CB 1 ATOM 4248 C CG . PRO A 1 575 ? 33.202 31.611 56.613 1.00 29.06 ? 568 PRO A CG 1 ATOM 4249 C CD . PRO A 1 575 ? 32.513 32.940 56.420 1.00 24.93 ? 568 PRO A CD 1 ATOM 4250 N N A MET A 1 576 ? 30.947 32.583 59.908 0.70 25.38 ? 569 MET A N 1 ATOM 4251 N N B MET A 1 576 ? 30.970 32.587 59.893 0.30 25.22 ? 569 MET A N 1 ATOM 4252 C CA A MET A 1 576 ? 30.558 32.728 61.316 0.70 26.19 ? 569 MET A CA 1 ATOM 4253 C CA B MET A 1 576 ? 30.621 32.782 61.299 0.30 25.28 ? 569 MET A CA 1 ATOM 4254 C C A MET A 1 576 ? 29.265 33.523 61.492 0.70 24.86 ? 569 MET A C 1 ATOM 4255 C C B MET A 1 576 ? 29.285 33.510 61.481 0.30 24.35 ? 569 MET A C 1 ATOM 4256 O O A MET A 1 576 ? 28.753 33.659 62.607 0.70 25.03 ? 569 MET A O 1 ATOM 4257 O O B MET A 1 576 ? 28.764 33.580 62.595 0.30 25.66 ? 569 MET A O 1 ATOM 4258 C CB A MET A 1 576 ? 31.696 33.377 62.117 0.70 28.01 ? 569 MET A CB 1 ATOM 4259 C CB B MET A 1 576 ? 31.741 33.559 62.014 0.30 26.01 ? 569 MET A CB 1 ATOM 4260 C CG A MET A 1 576 ? 32.997 32.573 62.120 0.70 35.51 ? 569 MET A CG 1 ATOM 4261 C CG B MET A 1 576 ? 33.135 32.956 61.849 0.30 27.74 ? 569 MET A CG 1 ATOM 4262 S SD A MET A 1 576 ? 32.749 30.845 62.572 0.70 42.68 ? 569 MET A SD 1 ATOM 4263 S SD B MET A 1 576 ? 34.410 33.750 62.860 0.30 29.91 ? 569 MET A SD 1 ATOM 4264 C CE A MET A 1 576 ? 32.297 30.958 64.304 0.70 39.37 ? 569 MET A CE 1 ATOM 4265 C CE B MET A 1 576 ? 35.399 34.584 61.621 0.30 30.51 ? 569 MET A CE 1 ATOM 4266 N N . PHE A 1 577 ? 28.737 34.044 60.387 1.00 23.67 ? 570 PHE A N 1 ATOM 4267 C CA . PHE A 1 577 ? 27.529 34.865 60.421 1.00 21.55 ? 570 PHE A CA 1 ATOM 4268 C C . PHE A 1 577 ? 27.686 36.121 61.270 1.00 22.01 ? 570 PHE A C 1 ATOM 4269 O O . PHE A 1 577 ? 26.707 36.720 61.724 1.00 23.36 ? 570 PHE A O 1 ATOM 4270 C CB . PHE A 1 577 ? 26.269 34.020 60.714 1.00 22.56 ? 570 PHE A CB 1 ATOM 4271 C CG . PHE A 1 577 ? 25.848 33.228 59.522 1.00 21.81 ? 570 PHE A CG 1 ATOM 4272 C CD1 . PHE A 1 577 ? 24.860 33.712 58.660 1.00 22.18 ? 570 PHE A CD1 1 ATOM 4273 C CD2 . PHE A 1 577 ? 26.516 32.044 59.191 1.00 24.23 ? 570 PHE A CD2 1 ATOM 4274 C CE1 . PHE A 1 577 ? 24.522 33.002 57.515 1.00 22.88 ? 570 PHE A CE1 1 ATOM 4275 C CE2 . PHE A 1 577 ? 26.188 31.343 58.039 1.00 24.32 ? 570 PHE A CE2 1 ATOM 4276 C CZ . PHE A 1 577 ? 25.187 31.820 57.206 1.00 22.51 ? 570 PHE A CZ 1 ATOM 4277 N N . LYS A 1 578 ? 28.941 36.533 61.439 1.00 22.22 ? 571 LYS A N 1 ATOM 4278 C CA . LYS A 1 578 ? 29.246 37.751 62.197 1.00 22.58 ? 571 LYS A CA 1 ATOM 4279 C C . LYS A 1 578 ? 28.932 39.031 61.437 1.00 20.97 ? 571 LYS A C 1 ATOM 4280 O O . LYS A 1 578 ? 28.570 40.027 62.051 1.00 21.98 ? 571 LYS A O 1 ATOM 4281 C CB . LYS A 1 578 ? 30.696 37.777 62.681 1.00 24.51 ? 571 LYS A CB 1 ATOM 4282 C CG . LYS A 1 578 ? 31.749 37.878 61.588 1.00 23.84 ? 571 LYS A CG 1 ATOM 4283 C CD . LYS A 1 578 ? 33.127 37.759 62.206 1.00 29.77 ? 571 LYS A CD 1 ATOM 4284 C CE . LYS A 1 578 ? 34.207 38.016 61.178 1.00 30.84 ? 571 LYS A CE 1 ATOM 4285 N NZ . LYS A 1 578 ? 35.546 38.113 61.836 1.00 34.12 ? 571 LYS A NZ 1 ATOM 4286 N N . TYR A 1 579 ? 29.112 39.036 60.120 1.00 21.88 ? 572 TYR A N 1 ATOM 4287 C CA . TYR A 1 579 ? 28.721 40.221 59.345 1.00 20.63 ? 572 TYR A CA 1 ATOM 4288 C C . TYR A 1 579 ? 27.199 40.347 59.311 1.00 20.41 ? 572 TYR A C 1 ATOM 4289 O O . TYR A 1 579 ? 26.664 41.452 59.437 1.00 20.59 ? 572 TYR A O 1 ATOM 4290 C CB . TYR A 1 579 ? 29.329 40.202 57.931 1.00 21.38 ? 572 TYR A CB 1 ATOM 4291 C CG . TYR A 1 579 ? 30.831 40.079 57.996 1.00 22.52 ? 572 TYR A CG 1 ATOM 4292 C CD1 . TYR A 1 579 ? 31.593 41.046 58.665 1.00 26.45 ? 572 TYR A CD1 1 ATOM 4293 C CD2 . TYR A 1 579 ? 31.491 38.986 57.440 1.00 25.04 ? 572 TYR A CD2 1 ATOM 4294 C CE1 . TYR A 1 579 ? 32.964 40.946 58.748 1.00 27.18 ? 572 TYR A CE1 1 ATOM 4295 C CE2 . TYR A 1 579 ? 32.880 38.869 57.536 1.00 26.40 ? 572 TYR A CE2 1 ATOM 4296 C CZ . TYR A 1 579 ? 33.604 39.848 58.184 1.00 27.33 ? 572 TYR A CZ 1 ATOM 4297 O OH . TYR A 1 579 ? 34.974 39.739 58.275 1.00 33.02 ? 572 TYR A OH 1 ATOM 4298 N N . HIS A 1 580 ? 26.504 39.220 59.146 1.00 21.42 ? 573 HIS A N 1 ATOM 4299 C CA . HIS A 1 580 ? 25.038 39.211 59.260 1.00 20.81 ? 573 HIS A CA 1 ATOM 4300 C C . HIS A 1 580 ? 24.603 39.749 60.599 1.00 20.69 ? 573 HIS A C 1 ATOM 4301 O O . HIS A 1 580 ? 23.682 40.558 60.675 1.00 19.81 ? 573 HIS A O 1 ATOM 4302 C CB . HIS A 1 580 ? 24.472 37.806 59.098 1.00 21.18 ? 573 HIS A CB 1 ATOM 4303 C CG . HIS A 1 580 ? 24.394 37.323 57.675 1.00 21.95 ? 573 HIS A CG 1 ATOM 4304 N ND1 . HIS A 1 580 ? 25.483 36.898 56.981 1.00 23.87 ? 573 HIS A ND1 1 ATOM 4305 C CD2 . HIS A 1 580 ? 23.291 37.131 56.840 1.00 23.49 ? 573 HIS A CD2 1 ATOM 4306 C CE1 . HIS A 1 580 ? 25.091 36.479 55.753 1.00 23.24 ? 573 HIS A CE1 1 ATOM 4307 N NE2 . HIS A 1 580 ? 23.750 36.614 55.671 1.00 26.00 ? 573 HIS A NE2 1 ATOM 4308 N N . LEU A 1 581 ? 25.241 39.290 61.671 1.00 20.72 ? 574 LEU A N 1 ATOM 4309 C CA . LEU A 1 581 ? 24.867 39.759 63.005 1.00 21.26 ? 574 LEU A CA 1 ATOM 4310 C C . LEU A 1 581 ? 25.064 41.270 63.152 1.00 21.23 ? 574 LEU A C 1 ATOM 4311 O O . LEU A 1 581 ? 24.186 41.973 63.681 1.00 20.46 ? 574 LEU A O 1 ATOM 4312 C CB . LEU A 1 581 ? 25.603 38.992 64.112 1.00 22.26 ? 574 LEU A CB 1 ATOM 4313 C CG . LEU A 1 581 ? 25.252 39.452 65.543 1.00 21.86 ? 574 LEU A CG 1 ATOM 4314 C CD1 . LEU A 1 581 ? 23.771 39.265 65.843 1.00 23.43 ? 574 LEU A CD1 1 ATOM 4315 C CD2 . LEU A 1 581 ? 26.095 38.669 66.544 1.00 23.56 ? 574 LEU A CD2 1 ATOM 4316 N N . THR A 1 582 ? 26.195 41.774 62.659 1.00 20.36 ? 575 THR A N 1 ATOM 4317 C CA . THR A 1 582 ? 26.474 43.225 62.681 1.00 21.66 ? 575 THR A CA 1 ATOM 4318 C C . THR A 1 582 ? 25.414 44.006 61.902 1.00 19.77 ? 575 THR A C 1 ATOM 4319 O O . THR A 1 582 ? 24.913 45.042 62.360 1.00 20.23 ? 575 THR A O 1 ATOM 4320 C CB . THR A 1 582 ? 27.900 43.510 62.157 1.00 21.19 ? 575 THR A CB 1 ATOM 4321 O OG1 . THR A 1 582 ? 28.863 42.983 63.093 1.00 24.66 ? 575 THR A OG1 1 ATOM 4322 C CG2 . THR A 1 582 ? 28.144 45.029 61.955 1.00 22.34 ? 575 THR A CG2 1 ATOM 4323 N N . VAL A 1 583 ? 25.027 43.485 60.742 1.00 19.61 ? 576 VAL A N 1 ATOM 4324 C CA . VAL A 1 583 ? 23.978 44.126 59.939 1.00 18.99 ? 576 VAL A CA 1 ATOM 4325 C C . VAL A 1 583 ? 22.626 44.079 60.664 1.00 18.73 ? 576 VAL A C 1 ATOM 4326 O O . VAL A 1 583 ? 21.867 45.059 60.621 1.00 19.55 ? 576 VAL A O 1 ATOM 4327 C CB . VAL A 1 583 ? 23.929 43.564 58.498 1.00 18.53 ? 576 VAL A CB 1 ATOM 4328 C CG1 . VAL A 1 583 ? 22.741 44.129 57.723 1.00 17.55 ? 576 VAL A CG1 1 ATOM 4329 C CG2 . VAL A 1 583 ? 25.227 43.908 57.767 1.00 20.31 ? 576 VAL A CG2 1 ATOM 4330 N N . ALA A 1 584 ? 22.327 42.972 61.351 1.00 18.60 ? 577 ALA A N 1 ATOM 4331 C CA . ALA A 1 584 ? 21.108 42.901 62.169 1.00 19.48 ? 577 ALA A CA 1 ATOM 4332 C C . ALA A 1 584 ? 21.123 43.956 63.288 1.00 19.23 ? 577 ALA A C 1 ATOM 4333 O O . ALA A 1 584 ? 20.110 44.599 63.576 1.00 18.53 ? 577 ALA A O 1 ATOM 4334 C CB . ALA A 1 584 ? 20.911 41.501 62.743 1.00 21.15 ? 577 ALA A CB 1 ATOM 4335 N N . GLN A 1 585 ? 22.283 44.140 63.906 1.00 20.04 ? 578 GLN A N 1 ATOM 4336 C CA . GLN A 1 585 ? 22.448 45.166 64.946 1.00 19.99 ? 578 GLN A CA 1 ATOM 4337 C C . GLN A 1 585 ? 22.293 46.583 64.400 1.00 20.09 ? 578 GLN A C 1 ATOM 4338 O O . GLN A 1 585 ? 21.682 47.447 65.062 1.00 20.89 ? 578 GLN A O 1 ATOM 4339 C CB . GLN A 1 585 ? 23.792 45.018 65.654 1.00 22.03 ? 578 GLN A CB 1 ATOM 4340 C CG . GLN A 1 585 ? 23.921 43.721 66.442 1.00 21.19 ? 578 GLN A CG 1 ATOM 4341 C CD . GLN A 1 585 ? 25.295 43.539 67.053 1.00 24.65 ? 578 GLN A CD 1 ATOM 4342 O OE1 . GLN A 1 585 ? 26.192 44.366 66.866 1.00 25.81 ? 578 GLN A OE1 1 ATOM 4343 N NE2 . GLN A 1 585 ? 25.471 42.439 67.783 1.00 27.02 ? 578 GLN A NE2 1 ATOM 4344 N N . VAL A 1 586 ? 22.829 46.834 63.203 1.00 18.99 ? 579 VAL A N 1 ATOM 4345 C CA . VAL A 1 586 ? 22.641 48.151 62.575 1.00 19.47 ? 579 VAL A CA 1 ATOM 4346 C C . VAL A 1 586 ? 21.165 48.385 62.206 1.00 19.00 ? 579 VAL A C 1 ATOM 4347 O O . VAL A 1 586 ? 20.561 49.378 62.634 1.00 18.77 ? 579 VAL A O 1 ATOM 4348 C CB . VAL A 1 586 ? 23.554 48.372 61.341 1.00 17.87 ? 579 VAL A CB 1 ATOM 4349 C CG1 . VAL A 1 586 ? 23.232 49.719 60.712 1.00 19.07 ? 579 VAL A CG1 1 ATOM 4350 C CG2 . VAL A 1 586 ? 25.031 48.325 61.746 1.00 19.12 ? 579 VAL A CG2 1 ATOM 4351 N N . ARG A 1 587 ? 20.574 47.480 61.424 1.00 18.35 ? 580 ARG A N 1 ATOM 4352 C CA . ARG A 1 587 ? 19.189 47.683 60.993 1.00 17.46 ? 580 ARG A CA 1 ATOM 4353 C C . ARG A 1 587 ? 18.232 47.679 62.189 1.00 18.34 ? 580 ARG A C 1 ATOM 4354 O O . ARG A 1 587 ? 17.346 48.539 62.299 1.00 18.67 ? 580 ARG A O 1 ATOM 4355 C CB . ARG A 1 587 ? 18.788 46.578 60.027 1.00 16.61 ? 580 ARG A CB 1 ATOM 4356 C CG . ARG A 1 587 ? 19.517 46.640 58.697 1.00 16.93 ? 580 ARG A CG 1 ATOM 4357 C CD . ARG A 1 587 ? 19.162 45.424 57.875 1.00 18.17 ? 580 ARG A CD 1 ATOM 4358 N NE . ARG A 1 587 ? 19.859 45.451 56.598 1.00 16.69 ? 580 ARG A NE 1 ATOM 4359 C CZ . ARG A 1 587 ? 19.852 44.470 55.694 1.00 17.36 ? 580 ARG A CZ 1 ATOM 4360 N NH1 . ARG A 1 587 ? 19.199 43.328 55.911 1.00 20.69 ? 580 ARG A NH1 1 ATOM 4361 N NH2 . ARG A 1 587 ? 20.537 44.625 54.566 1.00 16.76 ? 580 ARG A NH2 1 ATOM 4362 N N . GLY A 1 588 ? 18.401 46.699 63.075 1.00 19.07 ? 581 GLY A N 1 ATOM 4363 C CA . GLY A 1 588 ? 17.543 46.580 64.246 1.00 20.47 ? 581 GLY A CA 1 ATOM 4364 C C . GLY A 1 588 ? 17.711 47.737 65.216 1.00 18.80 ? 581 GLY A C 1 ATOM 4365 O O . GLY A 1 588 ? 16.725 48.255 65.742 1.00 19.63 ? 581 GLY A O 1 ATOM 4366 N N . GLY A 1 589 ? 18.960 48.146 65.444 1.00 20.41 ? 582 GLY A N 1 ATOM 4367 C CA . GLY A 1 589 ? 19.266 49.290 66.292 1.00 19.78 ? 582 GLY A CA 1 ATOM 4368 C C . GLY A 1 589 ? 18.649 50.578 65.787 1.00 20.36 ? 582 GLY A C 1 ATOM 4369 O O . GLY A 1 589 ? 18.118 51.361 66.580 1.00 20.60 ? 582 GLY A O 1 ATOM 4370 N N . MET A 1 590 ? 18.694 50.791 64.469 1.00 19.44 ? 583 MET A N 1 ATOM 4371 C CA . MET A 1 590 ? 18.071 51.967 63.858 1.00 18.80 ? 583 MET A CA 1 ATOM 4372 C C . MET A 1 590 ? 16.571 51.938 64.108 1.00 18.31 ? 583 MET A C 1 ATOM 4373 O O . MET A 1 590 ? 16.004 52.920 64.583 1.00 18.97 ? 583 MET A O 1 ATOM 4374 C CB . MET A 1 590 ? 18.367 52.040 62.357 1.00 18.78 ? 583 MET A CB 1 ATOM 4375 C CG . MET A 1 590 ? 19.816 52.412 62.090 1.00 19.77 ? 583 MET A CG 1 ATOM 4376 S SD . MET A 1 590 ? 20.221 52.399 60.344 1.00 22.14 ? 583 MET A SD 1 ATOM 4377 C CE . MET A 1 590 ? 19.499 53.957 59.791 1.00 21.91 ? 583 MET A CE 1 ATOM 4378 N N . VAL A 1 591 ? 15.950 50.786 63.849 1.00 17.75 ? 584 VAL A N 1 ATOM 4379 C CA . VAL A 1 591 ? 14.507 50.603 64.105 1.00 19.73 ? 584 VAL A CA 1 ATOM 4380 C C . VAL A 1 591 ? 14.182 50.850 65.585 1.00 19.62 ? 584 VAL A C 1 ATOM 4381 O O . VAL A 1 591 ? 13.226 51.588 65.886 1.00 19.51 ? 584 VAL A O 1 ATOM 4382 C CB . VAL A 1 591 ? 13.995 49.212 63.642 1.00 19.02 ? 584 VAL A CB 1 ATOM 4383 C CG1 . VAL A 1 591 ? 12.565 48.933 64.128 1.00 20.64 ? 584 VAL A CG1 1 ATOM 4384 C CG2 . VAL A 1 591 ? 14.112 49.068 62.116 1.00 19.44 ? 584 VAL A CG2 1 ATOM 4385 N N . PHE A 1 592 ? 14.981 50.270 66.496 1.00 18.85 ? 585 PHE A N 1 ATOM 4386 C CA . PHE A 1 592 ? 14.777 50.462 67.933 1.00 19.30 ? 585 PHE A CA 1 ATOM 4387 C C . PHE A 1 592 ? 14.782 51.948 68.304 1.00 20.46 ? 585 PHE A C 1 ATOM 4388 O O . PHE A 1 592 ? 13.859 52.427 68.974 1.00 20.74 ? 585 PHE A O 1 ATOM 4389 C CB . PHE A 1 592 ? 15.843 49.714 68.756 1.00 18.99 ? 585 PHE A CB 1 ATOM 4390 C CG . PHE A 1 592 ? 15.527 49.655 70.233 1.00 21.97 ? 585 PHE A CG 1 ATOM 4391 C CD1 . PHE A 1 592 ? 15.002 48.501 70.797 1.00 23.06 ? 585 PHE A CD1 1 ATOM 4392 C CD2 . PHE A 1 592 ? 15.719 50.777 71.053 1.00 22.97 ? 585 PHE A CD2 1 ATOM 4393 C CE1 . PHE A 1 592 ? 14.683 48.453 72.151 1.00 25.28 ? 585 PHE A CE1 1 ATOM 4394 C CE2 . PHE A 1 592 ? 15.406 50.737 72.405 1.00 24.64 ? 585 PHE A CE2 1 ATOM 4395 C CZ . PHE A 1 592 ? 14.895 49.567 72.960 1.00 27.23 ? 585 PHE A CZ 1 ATOM 4396 N N . GLU A 1 593 ? 15.812 52.679 67.873 1.00 20.93 ? 586 GLU A N 1 ATOM 4397 C CA . GLU A 1 593 ? 15.935 54.110 68.224 1.00 21.48 ? 586 GLU A CA 1 ATOM 4398 C C . GLU A 1 593 ? 14.793 54.923 67.602 1.00 21.03 ? 586 GLU A C 1 ATOM 4399 O O . GLU A 1 593 ? 14.205 55.789 68.251 1.00 23.07 ? 586 GLU A O 1 ATOM 4400 C CB . GLU A 1 593 ? 17.268 54.685 67.749 1.00 24.55 ? 586 GLU A CB 1 ATOM 4401 C CG . GLU A 1 593 ? 18.430 54.554 68.715 1.00 34.74 ? 586 GLU A CG 1 ATOM 4402 C CD . GLU A 1 593 ? 18.096 55.082 70.116 1.00 39.89 ? 586 GLU A CD 1 ATOM 4403 O OE1 . GLU A 1 593 ? 17.733 54.248 70.953 1.00 40.76 ? 586 GLU A OE1 1 ATOM 4404 O OE2 . GLU A 1 593 ? 18.138 56.313 70.378 1.00 45.24 ? 586 GLU A OE2 1 ATOM 4405 N N . LEU A 1 594 ? 14.486 54.651 66.339 1.00 20.10 ? 587 LEU A N 1 ATOM 4406 C CA . LEU A 1 594 ? 13.392 55.368 65.666 1.00 18.69 ? 587 LEU A CA 1 ATOM 4407 C C . LEU A 1 594 ? 12.050 55.121 66.365 1.00 20.29 ? 587 LEU A C 1 ATOM 4408 O O . LEU A 1 594 ? 11.224 56.038 66.494 1.00 21.16 ? 587 LEU A O 1 ATOM 4409 C CB . LEU A 1 594 ? 13.306 54.962 64.191 1.00 18.75 ? 587 LEU A CB 1 ATOM 4410 C CG . LEU A 1 594 ? 14.458 55.491 63.324 1.00 17.87 ? 587 LEU A CG 1 ATOM 4411 C CD1 . LEU A 1 594 ? 14.714 54.595 62.117 1.00 17.31 ? 587 LEU A CD1 1 ATOM 4412 C CD2 . LEU A 1 594 ? 14.187 56.931 62.907 1.00 18.20 ? 587 LEU A CD2 1 ATOM 4413 N N . ALA A 1 595 ? 11.855 53.897 66.859 1.00 19.95 ? 588 ALA A N 1 ATOM 4414 C CA . ALA A 1 595 ? 10.568 53.534 67.464 1.00 20.58 ? 588 ALA A CA 1 ATOM 4415 C C . ALA A 1 595 ? 10.478 53.856 68.941 1.00 20.59 ? 588 ALA A C 1 ATOM 4416 O O . ALA A 1 595 ? 9.379 53.908 69.488 1.00 22.03 ? 588 ALA A O 1 ATOM 4417 C CB . ALA A 1 595 ? 10.265 52.058 67.223 1.00 22.52 ? 588 ALA A CB 1 ATOM 4418 N N . ASN A 1 596 ? 11.614 54.101 69.588 1.00 22.07 ? 589 ASN A N 1 ATOM 4419 C CA . ASN A 1 596 ? 11.615 54.263 71.052 1.00 21.42 ? 589 ASN A CA 1 ATOM 4420 C C . ASN A 1 596 ? 12.117 55.577 71.612 1.00 23.61 ? 589 ASN A C 1 ATOM 4421 O O . ASN A 1 596 ? 11.789 55.921 72.755 1.00 25.89 ? 589 ASN A O 1 ATOM 4422 C CB . ASN A 1 596 ? 12.398 53.117 71.685 1.00 22.70 ? 589 ASN A CB 1 ATOM 4423 C CG A ASN A 1 596 ? 11.759 52.609 72.953 0.50 23.89 ? 589 ASN A CG 1 ATOM 4424 C CG B ASN A 1 596 ? 11.637 51.818 71.622 0.50 22.42 ? 589 ASN A CG 1 ATOM 4425 O OD1 A ASN A 1 596 ? 10.557 52.348 72.989 0.50 25.54 ? 589 ASN A OD1 1 ATOM 4426 O OD1 B ASN A 1 596 ? 11.984 50.913 70.863 0.50 27.64 ? 589 ASN A OD1 1 ATOM 4427 N ND2 A ASN A 1 596 ? 12.565 52.447 74.003 0.50 26.25 ? 589 ASN A ND2 1 ATOM 4428 N ND2 B ASN A 1 596 ? 10.574 51.727 72.403 0.50 22.15 ? 589 ASN A ND2 1 ATOM 4429 N N . SER A 1 597 ? 12.922 56.303 70.832 1.00 21.22 ? 590 SER A N 1 ATOM 4430 C CA . SER A 1 597 ? 13.484 57.574 71.305 1.00 22.79 ? 590 SER A CA 1 ATOM 4431 C C . SER A 1 597 ? 12.361 58.567 71.564 1.00 21.66 ? 590 SER A C 1 ATOM 4432 O O . SER A 1 597 ? 11.415 58.693 70.754 1.00 21.95 ? 590 SER A O 1 ATOM 4433 C CB . SER A 1 597 ? 14.483 58.144 70.285 1.00 25.81 ? 590 SER A CB 1 ATOM 4434 O OG . SER A 1 597 ? 15.109 59.316 70.799 1.00 27.45 ? 590 SER A OG 1 ATOM 4435 N N . ILE A 1 598 ? 12.444 59.277 72.681 1.00 20.13 ? 591 ILE A N 1 ATOM 4436 C CA . ILE A 1 598 ? 11.401 60.242 73.013 1.00 21.05 ? 591 ILE A CA 1 ATOM 4437 C C . ILE A 1 598 ? 11.287 61.320 71.933 1.00 21.51 ? 591 ILE A C 1 ATOM 4438 O O . ILE A 1 598 ? 10.185 61.589 71.399 1.00 23.03 ? 591 ILE A O 1 ATOM 4439 C CB . ILE A 1 598 ? 11.653 60.890 74.393 1.00 20.93 ? 591 ILE A CB 1 ATOM 4440 C CG1 . ILE A 1 598 ? 11.652 59.833 75.513 1.00 27.23 ? 591 ILE A CG1 1 ATOM 4441 C CG2 . ILE A 1 598 ? 10.625 61.984 74.632 1.00 23.95 ? 591 ILE A CG2 1 ATOM 4442 C CD1 . ILE A 1 598 ? 10.403 58.969 75.574 1.00 29.28 ? 591 ILE A CD1 1 ATOM 4443 N N . VAL A 1 599 ? 12.425 61.938 71.618 1.00 22.82 ? 592 VAL A N 1 ATOM 4444 C CA . VAL A 1 599 ? 12.518 62.846 70.475 1.00 22.75 ? 592 VAL A CA 1 ATOM 4445 C C . VAL A 1 599 ? 12.992 62.029 69.277 1.00 22.49 ? 592 VAL A C 1 ATOM 4446 O O . VAL A 1 599 ? 13.959 61.276 69.390 1.00 23.05 ? 592 VAL A O 1 ATOM 4447 C CB . VAL A 1 599 ? 13.478 64.013 70.757 1.00 22.91 ? 592 VAL A CB 1 ATOM 4448 C CG1 . VAL A 1 599 ? 13.584 64.918 69.537 1.00 25.28 ? 592 VAL A CG1 1 ATOM 4449 C CG2 . VAL A 1 599 ? 12.987 64.824 71.954 1.00 23.98 ? 592 VAL A CG2 1 ATOM 4450 N N . LEU A 1 600 ? 12.316 62.161 68.132 1.00 22.16 ? 593 LEU A N 1 ATOM 4451 C CA . LEU A 1 600 ? 12.749 61.424 66.926 1.00 21.56 ? 593 LEU A CA 1 ATOM 4452 C C . LEU A 1 600 ? 14.246 61.687 66.645 1.00 20.26 ? 593 LEU A C 1 ATOM 4453 O O . LEU A 1 600 ? 14.701 62.838 66.736 1.00 21.41 ? 593 LEU A O 1 ATOM 4454 C CB . LEU A 1 600 ? 11.872 61.781 65.715 1.00 21.77 ? 593 LEU A CB 1 ATOM 4455 C CG . LEU A 1 600 ? 10.488 61.120 65.711 1.00 23.00 ? 593 LEU A CG 1 ATOM 4456 C CD1 . LEU A 1 600 ? 9.625 61.683 64.590 1.00 22.64 ? 593 LEU A CD1 1 ATOM 4457 C CD2 . LEU A 1 600 ? 10.652 59.593 65.584 1.00 22.56 ? 593 LEU A CD2 1 ATOM 4458 N N . PRO A 1 601 ? 15.015 60.628 66.322 1.00 20.06 ? 594 PRO A N 1 ATOM 4459 C CA . PRO A 1 601 ? 16.482 60.759 66.198 1.00 22.13 ? 594 PRO A CA 1 ATOM 4460 C C . PRO A 1 601 ? 16.907 61.261 64.801 1.00 21.36 ? 594 PRO A C 1 ATOM 4461 O O . PRO A 1 601 ? 17.698 60.611 64.093 1.00 21.46 ? 594 PRO A O 1 ATOM 4462 C CB . PRO A 1 601 ? 16.972 59.325 66.457 1.00 20.62 ? 594 PRO A CB 1 ATOM 4463 C CG . PRO A 1 601 ? 15.855 58.483 65.879 1.00 20.70 ? 594 PRO A CG 1 ATOM 4464 C CD . PRO A 1 601 ? 14.592 59.210 66.285 1.00 20.88 ? 594 PRO A CD 1 ATOM 4465 N N . PHE A 1 602 ? 16.347 62.409 64.420 1.00 20.63 ? 595 PHE A N 1 ATOM 4466 C CA . PHE A 1 602 ? 16.630 63.060 63.145 1.00 18.95 ? 595 PHE A CA 1 ATOM 4467 C C . PHE A 1 602 ? 17.311 64.391 63.440 1.00 21.13 ? 595 PHE A C 1 ATOM 4468 O O . PHE A 1 602 ? 16.881 65.138 64.341 1.00 21.42 ? 595 PHE A O 1 ATOM 4469 C CB . PHE A 1 602 ? 15.338 63.385 62.388 1.00 18.98 ? 595 PHE A CB 1 ATOM 4470 C CG . PHE A 1 602 ? 14.564 62.183 61.887 1.00 18.90 ? 595 PHE A CG 1 ATOM 4471 C CD1 . PHE A 1 602 ? 15.176 60.965 61.558 1.00 19.67 ? 595 PHE A CD1 1 ATOM 4472 C CD2 . PHE A 1 602 ? 13.188 62.305 61.677 1.00 19.36 ? 595 PHE A CD2 1 ATOM 4473 C CE1 . PHE A 1 602 ? 14.402 59.906 61.046 1.00 20.12 ? 595 PHE A CE1 1 ATOM 4474 C CE2 . PHE A 1 602 ? 12.419 61.242 61.180 1.00 19.11 ? 595 PHE A CE2 1 ATOM 4475 C CZ . PHE A 1 602 ? 13.030 60.038 60.872 1.00 18.56 ? 595 PHE A CZ 1 ATOM 4476 N N . ASP A 1 603 ? 18.340 64.715 62.670 1.00 20.17 ? 596 ASP A N 1 ATOM 4477 C CA . ASP A 1 603 ? 19.025 66.000 62.836 1.00 20.56 ? 596 ASP A CA 1 ATOM 4478 C C . ASP A 1 603 ? 18.872 66.823 61.564 1.00 20.06 ? 596 ASP A C 1 ATOM 4479 O O . ASP A 1 603 ? 19.543 66.567 60.551 1.00 20.21 ? 596 ASP A O 1 ATOM 4480 C CB . ASP A 1 603 ? 20.494 65.822 63.217 1.00 21.14 ? 596 ASP A CB 1 ATOM 4481 C CG . ASP A 1 603 ? 21.130 67.131 63.689 1.00 22.88 ? 596 ASP A CG 1 ATOM 4482 O OD1 . ASP A 1 603 ? 20.599 68.219 63.385 1.00 23.72 ? 596 ASP A OD1 1 ATOM 4483 O OD2 . ASP A 1 603 ? 22.164 67.085 64.365 1.00 28.43 ? 596 ASP A OD2 1 ATOM 4484 N N . CYS A 1 604 ? 17.939 67.767 61.599 1.00 19.45 ? 597 CYS A N 1 ATOM 4485 C CA . CYS A 1 604 ? 17.648 68.585 60.427 1.00 19.74 ? 597 CYS A CA 1 ATOM 4486 C C . CYS A 1 604 ? 18.882 69.353 59.928 1.00 19.60 ? 597 CYS A C 1 ATOM 4487 O O . CYS A 1 604 ? 18.962 69.700 58.758 1.00 20.52 ? 597 CYS A O 1 ATOM 4488 C CB . CYS A 1 604 ? 16.509 69.571 60.736 1.00 18.98 ? 597 CYS A CB 1 ATOM 4489 S SG . CYS A 1 604 ? 16.811 70.702 62.137 1.00 25.26 ? 597 CYS A SG 1 ATOM 4490 N N . ARG A 1 605 ? 19.839 69.628 60.806 1.00 21.51 ? 598 ARG A N 1 ATOM 4491 C CA . ARG A 1 605 ? 21.025 70.396 60.390 1.00 22.23 ? 598 ARG A CA 1 ATOM 4492 C C . ARG A 1 605 ? 21.879 69.616 59.381 1.00 21.79 ? 598 ARG A C 1 ATOM 4493 O O . ARG A 1 605 ? 22.580 70.208 58.547 1.00 21.59 ? 598 ARG A O 1 ATOM 4494 C CB . ARG A 1 605 ? 21.867 70.804 61.599 1.00 22.04 ? 598 ARG A CB 1 ATOM 4495 C CG . ARG A 1 605 ? 21.112 71.682 62.587 1.00 21.61 ? 598 ARG A CG 1 ATOM 4496 C CD . ARG A 1 605 ? 21.910 71.834 63.884 1.00 23.44 ? 598 ARG A CD 1 ATOM 4497 N NE . ARG A 1 605 ? 22.049 70.544 64.576 1.00 26.18 ? 598 ARG A NE 1 ATOM 4498 C CZ . ARG A 1 605 ? 22.677 70.360 65.734 1.00 30.18 ? 598 ARG A CZ 1 ATOM 4499 N NH1 . ARG A 1 605 ? 23.255 71.379 66.367 1.00 28.83 ? 598 ARG A NH1 1 ATOM 4500 N NH2 . ARG A 1 605 ? 22.745 69.139 66.259 1.00 29.49 ? 598 ARG A NH2 1 ATOM 4501 N N . ASP A 1 606 ? 21.811 68.287 59.447 1.00 20.19 ? 599 ASP A N 1 ATOM 4502 C CA . ASP A 1 606 ? 22.544 67.461 58.485 1.00 19.71 ? 599 ASP A CA 1 ATOM 4503 C C . ASP A 1 606 ? 21.975 67.639 57.077 1.00 20.13 ? 599 ASP A C 1 ATOM 4504 O O . ASP A 1 606 ? 22.722 67.566 56.094 1.00 21.80 ? 599 ASP A O 1 ATOM 4505 C CB . ASP A 1 606 ? 22.537 65.998 58.917 1.00 20.71 ? 599 ASP A CB 1 ATOM 4506 C CG . ASP A 1 606 ? 23.520 65.742 60.058 1.00 25.05 ? 599 ASP A CG 1 ATOM 4507 O OD1 . ASP A 1 606 ? 24.607 66.355 60.048 1.00 32.62 ? 599 ASP A OD1 1 ATOM 4508 O OD2 . ASP A 1 606 ? 23.226 64.959 60.970 1.00 25.60 ? 599 ASP A OD2 1 ATOM 4509 N N . TYR A 1 607 ? 20.664 67.882 56.978 1.00 19.69 ? 600 TYR A N 1 ATOM 4510 C CA . TYR A 1 607 ? 20.052 68.168 55.664 1.00 18.42 ? 600 TYR A CA 1 ATOM 4511 C C . TYR A 1 607 ? 20.599 69.506 55.137 1.00 17.99 ? 600 TYR A C 1 ATOM 4512 O O . TYR A 1 607 ? 20.904 69.622 53.946 1.00 19.64 ? 600 TYR A O 1 ATOM 4513 C CB . TYR A 1 607 ? 18.511 68.193 55.719 1.00 18.18 ? 600 TYR A CB 1 ATOM 4514 C CG . TYR A 1 607 ? 17.878 67.239 54.723 1.00 16.50 ? 600 TYR A CG 1 ATOM 4515 C CD1 . TYR A 1 607 ? 18.246 67.275 53.360 1.00 17.48 ? 600 TYR A CD1 1 ATOM 4516 C CD2 . TYR A 1 607 ? 16.917 66.306 55.123 1.00 18.29 ? 600 TYR A CD2 1 ATOM 4517 C CE1 . TYR A 1 607 ? 17.665 66.414 52.429 1.00 16.46 ? 600 TYR A CE1 1 ATOM 4518 C CE2 . TYR A 1 607 ? 16.352 65.421 54.204 1.00 17.68 ? 600 TYR A CE2 1 ATOM 4519 C CZ . TYR A 1 607 ? 16.728 65.480 52.867 1.00 17.42 ? 600 TYR A CZ 1 ATOM 4520 O OH . TYR A 1 607 ? 16.147 64.622 51.989 1.00 17.65 ? 600 TYR A OH 1 ATOM 4521 N N . ALA A 1 608 ? 20.742 70.498 56.018 1.00 19.12 ? 601 ALA A N 1 ATOM 4522 C CA . ALA A 1 608 ? 21.229 71.824 55.608 1.00 18.72 ? 601 ALA A CA 1 ATOM 4523 C C . ALA A 1 608 ? 22.624 71.711 54.970 1.00 20.11 ? 601 ALA A C 1 ATOM 4524 O O . ALA A 1 608 ? 22.879 72.316 53.922 1.00 20.48 ? 601 ALA A O 1 ATOM 4525 C CB . ALA A 1 608 ? 21.268 72.784 56.792 1.00 18.15 ? 601 ALA A CB 1 ATOM 4526 N N . VAL A 1 609 ? 23.504 70.921 55.586 1.00 19.20 ? 602 VAL A N 1 ATOM 4527 C CA . VAL A 1 609 ? 24.857 70.714 55.062 1.00 20.91 ? 602 VAL A CA 1 ATOM 4528 C C . VAL A 1 609 ? 24.818 70.101 53.658 1.00 20.12 ? 602 VAL A C 1 ATOM 4529 O O . VAL A 1 609 ? 25.461 70.625 52.737 1.00 22.49 ? 602 VAL A O 1 ATOM 4530 C CB . VAL A 1 609 ? 25.732 69.852 56.004 1.00 22.56 ? 602 VAL A CB 1 ATOM 4531 C CG1 . VAL A 1 609 ? 27.099 69.544 55.371 1.00 24.19 ? 602 VAL A CG1 1 ATOM 4532 C CG2 . VAL A 1 609 ? 25.919 70.569 57.332 1.00 25.27 ? 602 VAL A CG2 1 ATOM 4533 N N . VAL A 1 610 ? 24.063 69.014 53.479 1.00 19.53 ? 603 VAL A N 1 ATOM 4534 C CA . VAL A 1 610 ? 24.053 68.359 52.151 1.00 19.91 ? 603 VAL A CA 1 ATOM 4535 C C . VAL A 1 610 ? 23.393 69.231 51.101 1.00 18.91 ? 603 VAL A C 1 ATOM 4536 O O . VAL A 1 610 ? 23.820 69.224 49.953 1.00 18.66 ? 603 VAL A O 1 ATOM 4537 C CB . VAL A 1 610 ? 23.528 66.894 52.117 1.00 21.43 ? 603 VAL A CB 1 ATOM 4538 C CG1 . VAL A 1 610 ? 24.279 66.019 53.132 1.00 22.76 ? 603 VAL A CG1 1 ATOM 4539 C CG2 . VAL A 1 610 ? 22.035 66.817 52.290 1.00 24.76 ? 603 VAL A CG2 1 ATOM 4540 N N . LEU A 1 611 ? 22.363 69.981 51.488 1.00 17.67 ? 604 LEU A N 1 ATOM 4541 C CA . LEU A 1 611 ? 21.690 70.851 50.523 1.00 17.27 ? 604 LEU A CA 1 ATOM 4542 C C . LEU A 1 611 ? 22.678 71.858 49.923 1.00 18.36 ? 604 LEU A C 1 ATOM 4543 O O . LEU A 1 611 ? 22.610 72.155 48.722 1.00 18.67 ? 604 LEU A O 1 ATOM 4544 C CB . LEU A 1 611 ? 20.488 71.573 51.155 1.00 17.26 ? 604 LEU A CB 1 ATOM 4545 C CG . LEU A 1 611 ? 19.248 70.681 51.420 1.00 16.20 ? 604 LEU A CG 1 ATOM 4546 C CD1 . LEU A 1 611 ? 18.244 71.404 52.315 1.00 20.41 ? 604 LEU A CD1 1 ATOM 4547 C CD2 . LEU A 1 611 ? 18.580 70.181 50.127 1.00 18.07 ? 604 LEU A CD2 1 ATOM 4548 N N . ARG A 1 612 ? 23.583 72.391 50.748 1.00 18.92 ? 605 ARG A N 1 ATOM 4549 C CA . ARG A 1 612 ? 24.586 73.313 50.234 1.00 20.18 ? 605 ARG A CA 1 ATOM 4550 C C . ARG A 1 612 ? 25.543 72.601 49.279 1.00 19.77 ? 605 ARG A C 1 ATOM 4551 O O . ARG A 1 612 ? 25.877 73.147 48.233 1.00 20.75 ? 605 ARG A O 1 ATOM 4552 C CB . ARG A 1 612 ? 25.352 74.014 51.364 1.00 21.49 ? 605 ARG A CB 1 ATOM 4553 C CG . ARG A 1 612 ? 26.450 74.946 50.874 1.00 22.77 ? 605 ARG A CG 1 ATOM 4554 C CD . ARG A 1 612 ? 25.937 76.074 49.960 1.00 25.41 ? 605 ARG A CD 1 ATOM 4555 N NE . ARG A 1 612 ? 27.089 76.865 49.511 1.00 28.81 ? 605 ARG A NE 1 ATOM 4556 C CZ . ARG A 1 612 ? 27.561 77.925 50.161 1.00 36.50 ? 605 ARG A CZ 1 ATOM 4557 N NH1 . ARG A 1 612 ? 26.966 78.348 51.280 1.00 38.64 ? 605 ARG A NH1 1 ATOM 4558 N NH2 . ARG A 1 612 ? 28.627 78.569 49.699 1.00 40.04 ? 605 ARG A NH2 1 ATOM 4559 N N . LYS A 1 613 ? 25.974 71.392 49.638 1.00 19.21 ? 606 LYS A N 1 ATOM 4560 C CA . LYS A 1 613 ? 26.845 70.595 48.770 1.00 19.66 ? 606 LYS A CA 1 ATOM 4561 C C . LYS A 1 613 ? 26.166 70.355 47.413 1.00 18.40 ? 606 LYS A C 1 ATOM 4562 O O . LYS A 1 613 ? 26.782 70.542 46.356 1.00 18.51 ? 606 LYS A O 1 ATOM 4563 C CB . LYS A 1 613 ? 27.198 69.264 49.466 1.00 21.41 ? 606 LYS A CB 1 ATOM 4564 C CG . LYS A 1 613 ? 28.039 68.291 48.665 1.00 26.53 ? 606 LYS A CG 1 ATOM 4565 C CD . LYS A 1 613 ? 28.328 67.014 49.458 1.00 31.34 ? 606 LYS A CD 1 ATOM 4566 C CE . LYS A 1 613 ? 27.106 66.123 49.642 1.00 35.98 ? 606 LYS A CE 1 ATOM 4567 N NZ . LYS A 1 613 ? 27.462 64.880 50.392 1.00 37.80 ? 606 LYS A NZ 1 ATOM 4568 N N . TYR A 1 614 ? 24.892 69.978 47.443 1.00 17.05 ? 607 TYR A N 1 ATOM 4569 C CA . TYR A 1 614 ? 24.148 69.714 46.196 1.00 16.16 ? 607 TYR A CA 1 ATOM 4570 C C . TYR A 1 614 ? 23.934 70.996 45.407 1.00 17.01 ? 607 TYR A C 1 ATOM 4571 O O . TYR A 1 614 ? 23.966 70.960 44.181 1.00 18.16 ? 607 TYR A O 1 ATOM 4572 C CB . TYR A 1 614 ? 22.790 69.072 46.481 1.00 16.21 ? 607 TYR A CB 1 ATOM 4573 C CG . TYR A 1 614 ? 22.847 67.758 47.235 1.00 17.57 ? 607 TYR A CG 1 ATOM 4574 C CD1 . TYR A 1 614 ? 23.983 66.921 47.181 1.00 19.00 ? 607 TYR A CD1 1 ATOM 4575 C CD2 . TYR A 1 614 ? 21.738 67.329 47.969 1.00 17.49 ? 607 TYR A CD2 1 ATOM 4576 C CE1 . TYR A 1 614 ? 24.019 65.707 47.883 1.00 19.39 ? 607 TYR A CE1 1 ATOM 4577 C CE2 . TYR A 1 614 ? 21.755 66.124 48.664 1.00 18.39 ? 607 TYR A CE2 1 ATOM 4578 C CZ . TYR A 1 614 ? 22.895 65.312 48.611 1.00 19.14 ? 607 TYR A CZ 1 ATOM 4579 O OH . TYR A 1 614 ? 22.912 64.131 49.302 1.00 20.37 ? 607 TYR A OH 1 ATOM 4580 N N . ALA A 1 615 ? 23.704 72.119 46.088 1.00 15.83 ? 608 ALA A N 1 ATOM 4581 C CA . ALA A 1 615 ? 23.541 73.395 45.376 1.00 17.40 ? 608 ALA A CA 1 ATOM 4582 C C . ALA A 1 615 ? 24.848 73.776 44.671 1.00 18.96 ? 608 ALA A C 1 ATOM 4583 O O . ALA A 1 615 ? 24.843 74.187 43.487 1.00 19.27 ? 608 ALA A O 1 ATOM 4584 C CB . ALA A 1 615 ? 23.092 74.484 46.331 1.00 19.52 ? 608 ALA A CB 1 ATOM 4585 N N . ASP A 1 616 ? 25.965 73.656 45.390 1.00 19.23 ? 609 ASP A N 1 ATOM 4586 C CA . ASP A 1 616 ? 27.294 73.887 44.790 1.00 21.32 ? 609 ASP A CA 1 ATOM 4587 C C . ASP A 1 616 ? 27.498 72.999 43.553 1.00 20.84 ? 609 ASP A C 1 ATOM 4588 O O . ASP A 1 616 ? 28.004 73.460 42.526 1.00 19.99 ? 609 ASP A O 1 ATOM 4589 C CB . ASP A 1 616 ? 28.428 73.636 45.797 1.00 22.70 ? 609 ASP A CB 1 ATOM 4590 C CG . ASP A 1 616 ? 28.513 74.694 46.886 1.00 26.26 ? 609 ASP A CG 1 ATOM 4591 O OD1 . ASP A 1 616 ? 28.001 75.814 46.718 1.00 28.97 ? 609 ASP A OD1 1 ATOM 4592 O OD2 . ASP A 1 616 ? 29.146 74.402 47.930 1.00 33.47 ? 609 ASP A OD2 1 ATOM 4593 N N . LYS A 1 617 ? 27.109 71.728 43.662 1.00 19.47 ? 610 LYS A N 1 ATOM 4594 C CA . LYS A 1 617 ? 27.310 70.779 42.583 1.00 20.15 ? 610 LYS A CA 1 ATOM 4595 C C . LYS A 1 617 ? 26.505 71.155 41.341 1.00 20.83 ? 610 LYS A C 1 ATOM 4596 O O . LYS A 1 617 ? 27.042 71.159 40.213 1.00 20.40 ? 610 LYS A O 1 ATOM 4597 C CB . LYS A 1 617 ? 26.945 69.361 43.046 1.00 20.64 ? 610 LYS A CB 1 ATOM 4598 C CG . LYS A 1 617 ? 27.186 68.285 42.003 1.00 23.77 ? 610 LYS A CG 1 ATOM 4599 C CD . LYS A 1 617 ? 26.620 66.969 42.505 1.00 28.37 ? 610 LYS A CD 1 ATOM 4600 C CE . LYS A 1 617 ? 27.019 65.812 41.618 1.00 35.93 ? 610 LYS A CE 1 ATOM 4601 N NZ . LYS A 1 617 ? 26.451 64.544 42.146 1.00 42.47 ? 610 LYS A NZ 1 ATOM 4602 N N . ILE A 1 618 ? 25.225 71.456 41.531 1.00 20.10 ? 611 ILE A N 1 ATOM 4603 C CA . ILE A 1 618 ? 24.375 71.749 40.374 1.00 18.92 ? 611 ILE A CA 1 ATOM 4604 C C . ILE A 1 618 ? 24.769 73.098 39.734 1.00 18.85 ? 611 ILE A C 1 ATOM 4605 O O . ILE A 1 618 ? 24.782 73.234 38.502 1.00 19.34 ? 611 ILE A O 1 ATOM 4606 C CB . ILE A 1 618 ? 22.859 71.644 40.720 1.00 19.02 ? 611 ILE A CB 1 ATOM 4607 C CG1 . ILE A 1 618 ? 22.019 71.582 39.435 1.00 19.42 ? 611 ILE A CG1 1 ATOM 4608 C CG2 . ILE A 1 618 ? 22.403 72.764 41.669 1.00 19.24 ? 611 ILE A CG2 1 ATOM 4609 C CD1 . ILE A 1 618 ? 22.179 70.288 38.676 1.00 19.09 ? 611 ILE A CD1 1 ATOM 4610 N N . TYR A 1 619 ? 25.134 74.076 40.564 1.00 19.00 ? 612 TYR A N 1 ATOM 4611 C CA . TYR A 1 619 ? 25.651 75.342 40.051 1.00 20.77 ? 612 TYR A CA 1 ATOM 4612 C C . TYR A 1 619 ? 26.913 75.091 39.190 1.00 21.84 ? 612 TYR A C 1 ATOM 4613 O O . TYR A 1 619 ? 27.066 75.650 38.105 1.00 21.50 ? 612 TYR A O 1 ATOM 4614 C CB . TYR A 1 619 ? 25.927 76.318 41.214 1.00 20.44 ? 612 TYR A CB 1 ATOM 4615 C CG . TYR A 1 619 ? 26.796 77.479 40.803 1.00 25.28 ? 612 TYR A CG 1 ATOM 4616 C CD1 . TYR A 1 619 ? 26.249 78.600 40.182 1.00 26.46 ? 612 TYR A CD1 1 ATOM 4617 C CD2 . TYR A 1 619 ? 28.181 77.421 40.989 1.00 29.31 ? 612 TYR A CD2 1 ATOM 4618 C CE1 . TYR A 1 619 ? 27.059 79.656 39.788 1.00 31.17 ? 612 TYR A CE1 1 ATOM 4619 C CE2 . TYR A 1 619 ? 29.002 78.462 40.600 1.00 32.66 ? 612 TYR A CE2 1 ATOM 4620 C CZ . TYR A 1 619 ? 28.440 79.572 40.000 1.00 38.13 ? 612 TYR A CZ 1 ATOM 4621 O OH . TYR A 1 619 ? 29.271 80.587 39.609 1.00 49.37 ? 612 TYR A OH 1 ATOM 4622 N N . SER A 1 620 ? 27.810 74.234 39.676 1.00 20.11 ? 613 SER A N 1 ATOM 4623 C CA . SER A 1 620 ? 29.039 73.934 38.945 1.00 22.48 ? 613 SER A CA 1 ATOM 4624 C C . SER A 1 620 ? 28.758 73.287 37.586 1.00 22.22 ? 613 SER A C 1 ATOM 4625 O O . SER A 1 620 ? 29.455 73.580 36.633 1.00 24.24 ? 613 SER A O 1 ATOM 4626 C CB . SER A 1 620 ? 29.976 73.082 39.784 1.00 22.91 ? 613 SER A CB 1 ATOM 4627 O OG A SER A 1 620 ? 30.367 73.808 40.934 0.50 23.22 ? 613 SER A OG 1 ATOM 4628 O OG B SER A 1 620 ? 29.512 71.760 39.854 0.50 25.78 ? 613 SER A OG 1 ATOM 4629 N N . ILE A 1 621 ? 27.733 72.425 37.502 1.00 20.66 ? 614 ILE A N 1 ATOM 4630 C CA . ILE A 1 621 ? 27.336 71.834 36.217 1.00 21.41 ? 614 ILE A CA 1 ATOM 4631 C C . ILE A 1 621 ? 26.873 72.933 35.255 1.00 22.15 ? 614 ILE A C 1 ATOM 4632 O O . ILE A 1 621 ? 27.310 73.004 34.098 1.00 22.60 ? 614 ILE A O 1 ATOM 4633 C CB . ILE A 1 621 ? 26.240 70.755 36.397 1.00 20.96 ? 614 ILE A CB 1 ATOM 4634 C CG1 . ILE A 1 621 ? 26.832 69.525 37.114 1.00 21.70 ? 614 ILE A CG1 1 ATOM 4635 C CG2 . ILE A 1 621 ? 25.627 70.344 35.052 1.00 22.13 ? 614 ILE A CG2 1 ATOM 4636 C CD1 . ILE A 1 621 ? 25.786 68.527 37.601 1.00 21.52 ? 614 ILE A CD1 1 ATOM 4637 N N . SER A 1 622 ? 26.001 73.805 35.753 1.00 19.72 ? 615 SER A N 1 ATOM 4638 C CA . SER A 1 622 ? 25.494 74.913 34.955 1.00 21.16 ? 615 SER A CA 1 ATOM 4639 C C . SER A 1 622 ? 26.602 75.846 34.472 1.00 22.62 ? 615 SER A C 1 ATOM 4640 O O . SER A 1 622 ? 26.556 76.334 33.323 1.00 24.12 ? 615 SER A O 1 ATOM 4641 C CB . SER A 1 622 ? 24.449 75.707 35.748 1.00 20.44 ? 615 SER A CB 1 ATOM 4642 O OG . SER A 1 622 ? 23.769 76.628 34.911 1.00 21.71 ? 615 SER A OG 1 ATOM 4643 N N A MET A 1 623 ? 27.591 76.079 35.328 0.70 22.35 ? 616 MET A N 1 ATOM 4644 N N B MET A 1 623 ? 27.590 76.095 35.343 0.30 23.10 ? 616 MET A N 1 ATOM 4645 C CA A MET A 1 623 ? 28.667 77.020 35.015 0.70 24.77 ? 616 MET A CA 1 ATOM 4646 C CA B MET A 1 623 ? 28.705 77.021 35.046 0.30 25.17 ? 616 MET A CA 1 ATOM 4647 C C A MET A 1 623 ? 29.648 76.518 33.957 0.70 25.90 ? 616 MET A C 1 ATOM 4648 C C B MET A 1 623 ? 29.680 76.499 33.985 0.30 26.22 ? 616 MET A C 1 ATOM 4649 O O A MET A 1 623 ? 30.581 77.238 33.585 0.70 28.30 ? 616 MET A O 1 ATOM 4650 O O B MET A 1 623 ? 30.648 77.184 33.645 0.30 28.53 ? 616 MET A O 1 ATOM 4651 C CB A MET A 1 623 ? 29.368 77.456 36.286 0.70 26.07 ? 616 MET A CB 1 ATOM 4652 C CB B MET A 1 623 ? 29.447 77.488 36.320 0.30 26.54 ? 616 MET A CB 1 ATOM 4653 C CG A MET A 1 623 ? 28.684 78.640 36.947 0.70 30.33 ? 616 MET A CG 1 ATOM 4654 C CG B MET A 1 623 ? 30.266 76.430 37.053 0.30 26.76 ? 616 MET A CG 1 ATOM 4655 S SD A MET A 1 623 ? 28.602 80.126 35.913 0.70 36.85 ? 616 MET A SD 1 ATOM 4656 S SD B MET A 1 623 ? 31.562 76.999 38.194 0.30 35.92 ? 616 MET A SD 1 ATOM 4657 C CE A MET A 1 623 ? 30.328 80.466 35.574 0.70 32.83 ? 616 MET A CE 1 ATOM 4658 C CE B MET A 1 623 ? 32.941 77.180 37.070 0.30 31.65 ? 616 MET A CE 1 ATOM 4659 N N . LYS A 1 624 ? 29.417 75.298 33.464 1.00 26.03 ? 617 LYS A N 1 ATOM 4660 C CA . LYS A 1 624 ? 30.086 74.805 32.250 1.00 28.52 ? 617 LYS A CA 1 ATOM 4661 C C . LYS A 1 624 ? 29.599 75.589 31.010 1.00 27.27 ? 617 LYS A C 1 ATOM 4662 O O . LYS A 1 624 ? 30.243 75.534 29.956 1.00 26.77 ? 617 LYS A O 1 ATOM 4663 C CB . LYS A 1 624 ? 29.848 73.299 32.028 1.00 32.88 ? 617 LYS A CB 1 ATOM 4664 C CG . LYS A 1 624 ? 30.562 72.353 32.987 1.00 33.32 ? 617 LYS A CG 1 ATOM 4665 C CD . LYS A 1 624 ? 32.080 72.446 32.894 0.25 33.95 ? 617 LYS A CD 1 ATOM 4666 C CE . LYS A 1 624 ? 32.751 71.381 33.747 0.25 36.97 ? 617 LYS A CE 1 ATOM 4667 N NZ . LYS A 1 624 ? 32.447 71.520 35.198 0.50 38.84 ? 617 LYS A NZ 1 ATOM 4668 N N . HIS A 1 625 ? 28.479 76.314 31.144 1.00 24.60 ? 618 HIS A N 1 ATOM 4669 C CA . HIS A 1 625 ? 27.868 77.082 30.040 1.00 24.51 ? 618 HIS A CA 1 ATOM 4670 C C . HIS A 1 625 ? 27.717 78.549 30.383 1.00 24.57 ? 618 HIS A C 1 ATOM 4671 O O . HIS A 1 625 ? 26.579 79.072 30.385 1.00 23.92 ? 618 HIS A O 1 ATOM 4672 C CB . HIS A 1 625 ? 26.494 76.497 29.701 1.00 25.22 ? 618 HIS A CB 1 ATOM 4673 C CG . HIS A 1 625 ? 26.471 74.984 29.649 1.00 27.09 ? 618 HIS A CG 1 ATOM 4674 N ND1 . HIS A 1 625 ? 26.726 74.296 28.520 1.00 28.41 ? 618 HIS A ND1 1 ATOM 4675 C CD2 . HIS A 1 625 ? 26.211 74.032 30.643 1.00 28.64 ? 618 HIS A CD2 1 ATOM 4676 C CE1 . HIS A 1 625 ? 26.641 72.972 28.768 1.00 29.73 ? 618 HIS A CE1 1 ATOM 4677 N NE2 . HIS A 1 625 ? 26.325 72.808 30.069 1.00 30.33 ? 618 HIS A NE2 1 ATOM 4678 N N . PRO A 1 626 ? 28.851 79.251 30.657 1.00 25.24 ? 619 PRO A N 1 ATOM 4679 C CA . PRO A 1 626 ? 28.733 80.629 31.138 1.00 25.91 ? 619 PRO A CA 1 ATOM 4680 C C . PRO A 1 626 ? 28.051 81.569 30.149 1.00 25.92 ? 619 PRO A C 1 ATOM 4681 O O . PRO A 1 626 ? 27.285 82.442 30.590 1.00 27.04 ? 619 PRO A O 1 ATOM 4682 C CB . PRO A 1 626 ? 30.189 81.067 31.394 1.00 28.91 ? 619 PRO A CB 1 ATOM 4683 C CG . PRO A 1 626 ? 31.030 80.106 30.611 1.00 29.40 ? 619 PRO A CG 1 ATOM 4684 C CD . PRO A 1 626 ? 30.258 78.816 30.581 1.00 27.75 ? 619 PRO A CD 1 ATOM 4685 N N A GLN A 1 627 ? 28.299 81.411 28.846 0.70 25.48 ? 620 GLN A N 1 ATOM 4686 N N B GLN A 1 627 ? 28.314 81.391 28.850 0.30 25.89 ? 620 GLN A N 1 ATOM 4687 C CA A GLN A 1 627 ? 27.669 82.321 27.875 0.70 26.09 ? 620 GLN A CA 1 ATOM 4688 C CA B GLN A 1 627 ? 27.708 82.222 27.797 0.30 26.39 ? 620 GLN A CA 1 ATOM 4689 C C A GLN A 1 627 ? 26.147 82.190 27.893 0.70 24.37 ? 620 GLN A C 1 ATOM 4690 C C B GLN A 1 627 ? 26.185 82.167 27.838 0.30 24.58 ? 620 GLN A C 1 ATOM 4691 O O A GLN A 1 627 ? 25.441 83.198 27.860 0.70 25.38 ? 620 GLN A O 1 ATOM 4692 O O B GLN A 1 627 ? 25.520 83.201 27.765 0.30 24.39 ? 620 GLN A O 1 ATOM 4693 C CB A GLN A 1 627 ? 28.211 82.153 26.447 0.70 29.09 ? 620 GLN A CB 1 ATOM 4694 C CB B GLN A 1 627 ? 28.196 81.800 26.403 0.30 27.35 ? 620 GLN A CB 1 ATOM 4695 C CG A GLN A 1 627 ? 27.641 83.173 25.463 0.70 32.90 ? 620 GLN A CG 1 ATOM 4696 C CG B GLN A 1 627 ? 29.649 82.137 26.118 0.30 28.01 ? 620 GLN A CG 1 ATOM 4697 C CD A GLN A 1 627 ? 27.813 84.622 25.925 0.70 37.38 ? 620 GLN A CD 1 ATOM 4698 C CD B GLN A 1 627 ? 30.046 81.866 24.679 0.30 31.89 ? 620 GLN A CD 1 ATOM 4699 O OE1 A GLN A 1 627 ? 26.831 85.317 26.221 0.70 33.59 ? 620 GLN A OE1 1 ATOM 4700 O OE1 B GLN A 1 627 ? 29.307 81.236 23.920 0.30 35.67 ? 620 GLN A OE1 1 ATOM 4701 N NE2 A GLN A 1 627 ? 29.062 85.078 26.010 0.70 43.17 ? 620 GLN A NE2 1 ATOM 4702 N NE2 B GLN A 1 627 ? 31.223 82.338 24.298 0.30 29.95 ? 620 GLN A NE2 1 ATOM 4703 N N . GLU A 1 628 ? 25.649 80.952 27.955 1.00 23.65 ? 621 GLU A N 1 ATOM 4704 C CA . GLU A 1 628 ? 24.212 80.734 28.007 1.00 22.89 ? 621 GLU A CA 1 ATOM 4705 C C . GLU A 1 628 ? 23.611 81.252 29.307 1.00 22.81 ? 621 GLU A C 1 ATOM 4706 O O . GLU A 1 628 ? 22.509 81.801 29.300 1.00 22.01 ? 621 GLU A O 1 ATOM 4707 C CB . GLU A 1 628 ? 23.850 79.264 27.801 1.00 24.52 ? 621 GLU A CB 1 ATOM 4708 C CG . GLU A 1 628 ? 24.127 78.752 26.399 1.00 29.89 ? 621 GLU A CG 1 ATOM 4709 C CD . GLU A 1 628 ? 25.604 78.658 26.054 1.00 32.30 ? 621 GLU A CD 1 ATOM 4710 O OE1 . GLU A 1 628 ? 26.449 78.392 26.934 1.00 32.53 ? 621 GLU A OE1 1 ATOM 4711 O OE2 . GLU A 1 628 ? 25.922 78.855 24.870 1.00 43.41 ? 621 GLU A OE2 1 ATOM 4712 N N . MET A 1 629 ? 24.329 81.091 30.421 1.00 21.89 ? 622 MET A N 1 ATOM 4713 C CA . MET A 1 629 ? 23.826 81.641 31.687 1.00 21.08 ? 622 MET A CA 1 ATOM 4714 C C . MET A 1 629 ? 23.707 83.173 31.611 1.00 21.97 ? 622 MET A C 1 ATOM 4715 O O . MET A 1 629 ? 22.750 83.740 32.157 1.00 21.00 ? 622 MET A O 1 ATOM 4716 C CB . MET A 1 629 ? 24.700 81.221 32.863 1.00 21.22 ? 622 MET A CB 1 ATOM 4717 C CG . MET A 1 629 ? 24.564 79.747 33.207 1.00 20.07 ? 622 MET A CG 1 ATOM 4718 S SD . MET A 1 629 ? 25.556 79.254 34.647 1.00 22.72 ? 622 MET A SD 1 ATOM 4719 C CE . MET A 1 629 ? 24.714 80.137 35.968 1.00 21.04 ? 622 MET A CE 1 ATOM 4720 N N . LYS A 1 630 ? 24.651 83.835 30.927 1.00 20.14 ? 623 LYS A N 1 ATOM 4721 C CA . LYS A 1 630 ? 24.556 85.292 30.713 1.00 21.96 ? 623 LYS A CA 1 ATOM 4722 C C . LYS A 1 630 ? 23.366 85.639 29.801 1.00 24.99 ? 623 LYS A C 1 ATOM 4723 O O . LYS A 1 630 ? 22.531 86.496 30.138 1.00 23.51 ? 623 LYS A O 1 ATOM 4724 C CB . LYS A 1 630 ? 25.865 85.858 30.133 1.00 24.80 ? 623 LYS A CB 1 ATOM 4725 C CG . LYS A 1 630 ? 27.060 85.701 31.063 1.00 23.62 ? 623 LYS A CG 1 ATOM 4726 C CD . LYS A 1 630 ? 28.357 86.160 30.410 1.00 27.90 ? 623 LYS A CD 1 ATOM 4727 C CE . LYS A 1 630 ? 29.482 86.048 31.427 1.00 34.54 ? 623 LYS A CE 1 ATOM 4728 N NZ . LYS A 1 630 ? 30.640 85.231 30.980 1.00 44.14 ? 623 LYS A NZ 1 ATOM 4729 N N . THR A 1 631 ? 23.281 84.948 28.662 1.00 23.64 ? 624 THR A N 1 ATOM 4730 C CA . THR A 1 631 ? 22.249 85.227 27.646 1.00 25.70 ? 624 THR A CA 1 ATOM 4731 C C . THR A 1 631 ? 20.842 85.068 28.188 1.00 24.52 ? 624 THR A C 1 ATOM 4732 O O . THR A 1 631 ? 19.976 85.921 27.946 1.00 25.79 ? 624 THR A O 1 ATOM 4733 C CB . THR A 1 631 ? 22.430 84.340 26.393 1.00 28.90 ? 624 THR A CB 1 ATOM 4734 O OG1 . THR A 1 631 ? 23.680 84.660 25.792 1.00 33.02 ? 624 THR A OG1 1 ATOM 4735 C CG2 . THR A 1 631 ? 21.312 84.600 25.355 1.00 31.90 ? 624 THR A CG2 1 ATOM 4736 N N . TYR A 1 632 ? 20.619 83.987 28.933 1.00 22.23 ? 625 TYR A N 1 ATOM 4737 C CA . TYR A 1 632 ? 19.277 83.669 29.420 1.00 23.35 ? 625 TYR A CA 1 ATOM 4738 C C . TYR A 1 632 ? 19.045 84.060 30.869 1.00 23.22 ? 625 TYR A C 1 ATOM 4739 O O . TYR A 1 632 ? 18.016 83.701 31.431 1.00 21.49 ? 625 TYR A O 1 ATOM 4740 C CB . TYR A 1 632 ? 18.931 82.188 29.162 1.00 21.34 ? 625 TYR A CB 1 ATOM 4741 C CG . TYR A 1 632 ? 19.064 81.868 27.690 1.00 25.37 ? 625 TYR A CG 1 ATOM 4742 C CD1 . TYR A 1 632 ? 18.187 82.429 26.758 1.00 27.37 ? 625 TYR A CD1 1 ATOM 4743 C CD2 . TYR A 1 632 ? 20.080 81.032 27.226 1.00 25.80 ? 625 TYR A CD2 1 ATOM 4744 C CE1 . TYR A 1 632 ? 18.320 82.166 25.401 1.00 29.27 ? 625 TYR A CE1 1 ATOM 4745 C CE2 . TYR A 1 632 ? 20.216 80.749 25.873 1.00 28.07 ? 625 TYR A CE2 1 ATOM 4746 C CZ . TYR A 1 632 ? 19.333 81.327 24.968 1.00 30.94 ? 625 TYR A CZ 1 ATOM 4747 O OH . TYR A 1 632 ? 19.450 81.072 23.628 1.00 33.64 ? 625 TYR A OH 1 ATOM 4748 N N . SER A 1 633 ? 19.997 84.806 31.452 1.00 22.66 ? 626 SER A N 1 ATOM 4749 C CA . SER A 1 633 ? 19.883 85.313 32.825 1.00 21.44 ? 626 SER A CA 1 ATOM 4750 C C . SER A 1 633 ? 19.585 84.179 33.803 1.00 20.41 ? 626 SER A C 1 ATOM 4751 O O . SER A 1 633 ? 18.613 84.228 34.567 1.00 20.15 ? 626 SER A O 1 ATOM 4752 C CB A SER A 1 633 ? 18.803 86.400 32.931 0.65 21.29 ? 626 SER A CB 1 ATOM 4753 C CB B SER A 1 633 ? 18.790 86.379 32.891 0.35 22.60 ? 626 SER A CB 1 ATOM 4754 O OG A SER A 1 633 ? 19.170 87.548 32.186 0.65 19.15 ? 626 SER A OG 1 ATOM 4755 O OG B SER A 1 633 ? 18.983 87.203 34.011 0.35 23.47 ? 626 SER A OG 1 ATOM 4756 N N . VAL A 1 634 ? 20.425 83.150 33.771 1.00 19.59 ? 627 VAL A N 1 ATOM 4757 C CA . VAL A 1 634 ? 20.207 81.946 34.580 1.00 20.05 ? 627 VAL A CA 1 ATOM 4758 C C . VAL A 1 634 ? 20.923 82.185 35.909 1.00 22.47 ? 627 VAL A C 1 ATOM 4759 O O . VAL A 1 634 ? 22.159 82.237 35.958 1.00 22.61 ? 627 VAL A O 1 ATOM 4760 C CB . VAL A 1 634 ? 20.777 80.692 33.880 1.00 20.86 ? 627 VAL A CB 1 ATOM 4761 C CG1 . VAL A 1 634 ? 20.504 79.430 34.703 1.00 20.47 ? 627 VAL A CG1 1 ATOM 4762 C CG2 . VAL A 1 634 ? 20.175 80.540 32.487 1.00 21.77 ? 627 VAL A CG2 1 ATOM 4763 N N . SER A 1 635 ? 20.143 82.377 36.968 1.00 22.10 ? 628 SER A N 1 ATOM 4764 C CA . SER A 1 635 ? 20.697 82.630 38.298 1.00 23.23 ? 628 SER A CA 1 ATOM 4765 C C . SER A 1 635 ? 20.295 81.543 39.284 1.00 21.27 ? 628 SER A C 1 ATOM 4766 O O . SER A 1 635 ? 19.129 81.121 39.330 1.00 20.60 ? 628 SER A O 1 ATOM 4767 C CB . SER A 1 635 ? 20.203 83.960 38.837 1.00 26.63 ? 628 SER A CB 1 ATOM 4768 O OG . SER A 1 635 ? 20.793 84.184 40.102 1.00 29.08 ? 628 SER A OG 1 ATOM 4769 N N . PHE A 1 636 ? 21.265 81.130 40.096 1.00 21.22 ? 629 PHE A N 1 ATOM 4770 C CA . PHE A 1 636 ? 21.022 80.181 41.186 1.00 20.59 ? 629 PHE A CA 1 ATOM 4771 C C . PHE A 1 636 ? 20.821 80.908 42.533 1.00 19.37 ? 629 PHE A C 1 ATOM 4772 O O . PHE A 1 636 ? 20.740 80.266 43.570 1.00 19.33 ? 629 PHE A O 1 ATOM 4773 C CB . PHE A 1 636 ? 22.159 79.146 41.276 1.00 20.57 ? 629 PHE A CB 1 ATOM 4774 C CG . PHE A 1 636 ? 22.081 78.079 40.222 1.00 20.19 ? 629 PHE A CG 1 ATOM 4775 C CD1 . PHE A 1 636 ? 21.523 76.832 40.509 1.00 19.22 ? 629 PHE A CD1 1 ATOM 4776 C CD2 . PHE A 1 636 ? 22.548 78.322 38.934 1.00 20.56 ? 629 PHE A CD2 1 ATOM 4777 C CE1 . PHE A 1 636 ? 21.423 75.850 39.527 1.00 20.07 ? 629 PHE A CE1 1 ATOM 4778 C CE2 . PHE A 1 636 ? 22.452 77.347 37.947 1.00 20.29 ? 629 PHE A CE2 1 ATOM 4779 C CZ . PHE A 1 636 ? 21.890 76.104 38.247 1.00 18.77 ? 629 PHE A CZ 1 ATOM 4780 N N . ASP A 1 637 ? 20.722 82.235 42.498 1.00 19.31 ? 630 ASP A N 1 ATOM 4781 C CA . ASP A 1 637 ? 20.632 83.038 43.727 1.00 20.15 ? 630 ASP A CA 1 ATOM 4782 C C . ASP A 1 637 ? 19.489 82.565 44.610 1.00 19.97 ? 630 ASP A C 1 ATOM 4783 O O . ASP A 1 637 ? 19.658 82.445 45.836 1.00 21.19 ? 630 ASP A O 1 ATOM 4784 C CB . ASP A 1 637 ? 20.485 84.529 43.429 1.00 21.60 ? 630 ASP A CB 1 ATOM 4785 C CG . ASP A 1 637 ? 21.783 85.153 42.878 1.00 24.18 ? 630 ASP A CG 1 ATOM 4786 O OD1 . ASP A 1 637 ? 22.835 84.468 42.856 1.00 26.58 ? 630 ASP A OD1 1 ATOM 4787 O OD2 . ASP A 1 637 ? 21.762 86.337 42.459 1.00 27.83 ? 630 ASP A OD2 1 ATOM 4788 N N . SER A 1 638 ? 18.336 82.300 43.995 1.00 19.18 ? 631 SER A N 1 ATOM 4789 C CA . SER A 1 638 ? 17.159 81.848 44.769 1.00 16.64 ? 631 SER A CA 1 ATOM 4790 C C . SER A 1 638 ? 17.431 80.541 45.499 1.00 17.74 ? 631 SER A C 1 ATOM 4791 O O . SER A 1 638 ? 17.017 80.384 46.654 1.00 17.89 ? 631 SER A O 1 ATOM 4792 C CB . SER A 1 638 ? 15.888 81.743 43.905 1.00 18.41 ? 631 SER A CB 1 ATOM 4793 O OG . SER A 1 638 ? 16.042 80.784 42.857 1.00 20.06 ? 631 SER A OG 1 ATOM 4794 N N . LEU A 1 639 ? 18.104 79.602 44.834 1.00 16.19 ? 632 LEU A N 1 ATOM 4795 C CA . LEU A 1 639 ? 18.371 78.313 45.458 1.00 16.27 ? 632 LEU A CA 1 ATOM 4796 C C . LEU A 1 639 ? 19.364 78.465 46.627 1.00 16.78 ? 632 LEU A C 1 ATOM 4797 O O . LEU A 1 639 ? 19.146 77.919 47.705 1.00 17.37 ? 632 LEU A O 1 ATOM 4798 C CB . LEU A 1 639 ? 18.906 77.315 44.440 1.00 18.16 ? 632 LEU A CB 1 ATOM 4799 C CG . LEU A 1 639 ? 19.168 75.900 44.970 1.00 15.94 ? 632 LEU A CG 1 ATOM 4800 C CD1 . LEU A 1 639 ? 17.922 75.238 45.553 1.00 16.70 ? 632 LEU A CD1 1 ATOM 4801 C CD2 . LEU A 1 639 ? 19.734 75.040 43.854 1.00 17.68 ? 632 LEU A CD2 1 ATOM 4802 N N . PHE A 1 640 ? 20.435 79.227 46.428 1.00 17.54 ? 633 PHE A N 1 ATOM 4803 C CA . PHE A 1 640 ? 21.376 79.451 47.528 1.00 17.95 ? 633 PHE A CA 1 ATOM 4804 C C . PHE A 1 640 ? 20.729 80.205 48.701 1.00 18.25 ? 633 PHE A C 1 ATOM 4805 O O . PHE A 1 640 ? 21.002 79.908 49.868 1.00 21.24 ? 633 PHE A O 1 ATOM 4806 C CB . PHE A 1 640 ? 22.625 80.157 47.002 1.00 19.40 ? 633 PHE A CB 1 ATOM 4807 C CG . PHE A 1 640 ? 23.545 79.234 46.248 1.00 20.37 ? 633 PHE A CG 1 ATOM 4808 C CD1 . PHE A 1 640 ? 24.336 78.308 46.943 1.00 22.23 ? 633 PHE A CD1 1 ATOM 4809 C CD2 . PHE A 1 640 ? 23.623 79.271 44.856 1.00 22.76 ? 633 PHE A CD2 1 ATOM 4810 C CE1 . PHE A 1 640 ? 25.174 77.437 46.257 1.00 23.14 ? 633 PHE A CE1 1 ATOM 4811 C CE2 . PHE A 1 640 ? 24.488 78.415 44.169 1.00 22.81 ? 633 PHE A CE2 1 ATOM 4812 C CZ . PHE A 1 640 ? 25.245 77.489 44.870 1.00 21.89 ? 633 PHE A CZ 1 ATOM 4813 N N . SER A 1 641 ? 19.854 81.157 48.384 1.00 18.89 ? 634 SER A N 1 ATOM 4814 C CA . SER A 1 641 ? 19.095 81.867 49.410 1.00 18.39 ? 634 SER A CA 1 ATOM 4815 C C . SER A 1 641 ? 18.241 80.897 50.234 1.00 17.19 ? 634 SER A C 1 ATOM 4816 O O . SER A 1 641 ? 18.230 80.958 51.479 1.00 19.28 ? 634 SER A O 1 ATOM 4817 C CB . SER A 1 641 ? 18.199 82.930 48.788 1.00 19.26 ? 634 SER A CB 1 ATOM 4818 O OG . SER A 1 641 ? 17.445 83.593 49.790 1.00 20.60 ? 634 SER A OG 1 ATOM 4819 N N . ALA A 1 642 ? 17.522 80.019 49.542 1.00 17.19 ? 635 ALA A N 1 ATOM 4820 C CA . ALA A 1 642 ? 16.672 79.021 50.207 1.00 15.75 ? 635 ALA A CA 1 ATOM 4821 C C . ALA A 1 642 ? 17.514 78.113 51.100 1.00 18.24 ? 635 ALA A C 1 ATOM 4822 O O . ALA A 1 642 ? 17.127 77.820 52.245 1.00 18.42 ? 635 ALA A O 1 ATOM 4823 C CB . ALA A 1 642 ? 15.900 78.206 49.173 1.00 16.83 ? 635 ALA A CB 1 ATOM 4824 N N . VAL A 1 643 ? 18.669 77.677 50.582 1.00 17.41 ? 636 VAL A N 1 ATOM 4825 C CA . VAL A 1 643 ? 19.579 76.804 51.368 1.00 17.40 ? 636 VAL A CA 1 ATOM 4826 C C . VAL A 1 643 ? 20.115 77.543 52.607 1.00 19.01 ? 636 VAL A C 1 ATOM 4827 O O . VAL A 1 643 ? 20.173 76.971 53.696 1.00 18.55 ? 636 VAL A O 1 ATOM 4828 C CB . VAL A 1 643 ? 20.708 76.237 50.487 1.00 18.44 ? 636 VAL A CB 1 ATOM 4829 C CG1 . VAL A 1 643 ? 21.752 75.512 51.319 1.00 18.44 ? 636 VAL A CG1 1 ATOM 4830 C CG2 . VAL A 1 643 ? 20.089 75.290 49.443 1.00 18.07 ? 636 VAL A CG2 1 ATOM 4831 N N . LYS A 1 644 ? 20.505 78.809 52.436 1.00 19.17 ? 637 LYS A N 1 ATOM 4832 C CA . LYS A 1 644 ? 20.948 79.637 53.554 1.00 19.96 ? 637 LYS A CA 1 ATOM 4833 C C . LYS A 1 644 ? 19.828 79.749 54.597 1.00 20.04 ? 637 LYS A C 1 ATOM 4834 O O . LYS A 1 644 ? 20.061 79.589 55.794 1.00 20.24 ? 637 LYS A O 1 ATOM 4835 C CB . LYS A 1 644 ? 21.367 81.033 53.044 1.00 21.49 ? 637 LYS A CB 1 ATOM 4836 C CG . LYS A 1 644 ? 21.707 82.038 54.136 1.00 26.64 ? 637 LYS A CG 1 ATOM 4837 C CD . LYS A 1 644 ? 22.225 83.363 53.551 1.00 29.99 ? 637 LYS A CD 1 ATOM 4838 C CE . LYS A 1 644 ? 22.590 84.374 54.626 1.00 32.97 ? 637 LYS A CE 1 ATOM 4839 N NZ . LYS A 1 644 ? 21.385 84.969 55.275 1.00 40.12 ? 637 LYS A NZ 1 ATOM 4840 N N . ASN A 1 645 ? 18.601 79.999 54.142 1.00 18.68 ? 638 ASN A N 1 ATOM 4841 C CA . ASN A 1 645 ? 17.461 80.092 55.059 1.00 19.64 ? 638 ASN A CA 1 ATOM 4842 C C . ASN A 1 645 ? 17.188 78.773 55.785 1.00 19.00 ? 638 ASN A C 1 ATOM 4843 O O . ASN A 1 645 ? 16.946 78.759 57.011 1.00 19.62 ? 638 ASN A O 1 ATOM 4844 C CB . ASN A 1 645 ? 16.220 80.525 54.310 1.00 18.26 ? 638 ASN A CB 1 ATOM 4845 C CG . ASN A 1 645 ? 16.278 81.971 53.885 1.00 19.57 ? 638 ASN A CG 1 ATOM 4846 O OD1 . ASN A 1 645 ? 17.171 82.738 54.308 1.00 21.54 ? 638 ASN A OD1 1 ATOM 4847 N ND2 . ASN A 1 645 ? 15.307 82.372 53.051 1.00 20.84 ? 638 ASN A ND2 1 ATOM 4848 N N . PHE A 1 646 ? 17.248 77.671 55.036 1.00 18.32 ? 639 PHE A N 1 ATOM 4849 C CA . PHE A 1 646 ? 17.091 76.341 55.625 1.00 17.46 ? 639 PHE A CA 1 ATOM 4850 C C . PHE A 1 646 ? 18.129 76.161 56.750 1.00 19.85 ? 639 PHE A C 1 ATOM 4851 O O . PHE A 1 646 ? 17.794 75.677 57.849 1.00 19.59 ? 639 PHE A O 1 ATOM 4852 C CB . PHE A 1 646 ? 17.256 75.245 54.568 1.00 17.47 ? 639 PHE A CB 1 ATOM 4853 C CG . PHE A 1 646 ? 16.829 73.870 55.048 1.00 18.34 ? 639 PHE A CG 1 ATOM 4854 C CD1 . PHE A 1 646 ? 15.601 73.321 54.644 1.00 18.52 ? 639 PHE A CD1 1 ATOM 4855 C CD2 . PHE A 1 646 ? 17.653 73.111 55.880 1.00 17.40 ? 639 PHE A CD2 1 ATOM 4856 C CE1 . PHE A 1 646 ? 15.209 72.057 55.087 1.00 19.09 ? 639 PHE A CE1 1 ATOM 4857 C CE2 . PHE A 1 646 ? 17.265 71.849 56.327 1.00 17.61 ? 639 PHE A CE2 1 ATOM 4858 C CZ . PHE A 1 646 ? 16.034 71.320 55.944 1.00 17.70 ? 639 PHE A CZ 1 ATOM 4859 N N . THR A 1 647 ? 19.378 76.557 56.479 1.00 19.80 ? 640 THR A N 1 ATOM 4860 C CA . THR A 1 647 ? 20.477 76.403 57.453 1.00 21.15 ? 640 THR A CA 1 ATOM 4861 C C . THR A 1 647 ? 20.162 77.173 58.744 1.00 21.71 ? 640 THR A C 1 ATOM 4862 O O . THR A 1 647 ? 20.282 76.628 59.847 1.00 22.85 ? 640 THR A O 1 ATOM 4863 C CB . THR A 1 647 ? 21.831 76.812 56.832 1.00 19.16 ? 640 THR A CB 1 ATOM 4864 O OG1 . THR A 1 647 ? 22.016 76.065 55.619 1.00 21.21 ? 640 THR A OG1 1 ATOM 4865 C CG2 . THR A 1 647 ? 23.006 76.524 57.782 1.00 21.66 ? 640 THR A CG2 1 ATOM 4866 N N A GLU A 1 648 ? 19.727 78.418 58.570 0.70 20.40 ? 641 GLU A N 1 ATOM 4867 N N B GLU A 1 648 ? 19.734 78.431 58.626 0.30 21.03 ? 641 GLU A N 1 ATOM 4868 C CA A GLU A 1 648 ? 19.408 79.279 59.693 0.70 22.71 ? 641 GLU A CA 1 ATOM 4869 C CA B GLU A 1 648 ? 19.452 79.232 59.828 0.30 22.71 ? 641 GLU A CA 1 ATOM 4870 C C A GLU A 1 648 ? 18.243 78.741 60.521 0.70 21.99 ? 641 GLU A C 1 ATOM 4871 C C B GLU A 1 648 ? 18.164 78.866 60.567 0.30 22.21 ? 641 GLU A C 1 ATOM 4872 O O A GLU A 1 648 ? 18.365 78.594 61.750 0.70 22.37 ? 641 GLU A O 1 ATOM 4873 O O B GLU A 1 648 ? 18.095 79.015 61.793 0.30 23.90 ? 641 GLU A O 1 ATOM 4874 C CB A GLU A 1 648 ? 19.182 80.718 59.213 0.70 22.74 ? 641 GLU A CB 1 ATOM 4875 C CB B GLU A 1 648 ? 19.484 80.736 59.542 0.30 22.08 ? 641 GLU A CB 1 ATOM 4876 C CG A GLU A 1 648 ? 20.459 81.336 58.649 0.70 27.71 ? 641 GLU A CG 1 ATOM 4877 C CG B GLU A 1 648 ? 18.814 81.585 60.622 0.30 23.43 ? 641 GLU A CG 1 ATOM 4878 C CD A GLU A 1 648 ? 20.293 82.743 58.100 0.70 30.20 ? 641 GLU A CD 1 ATOM 4879 C CD B GLU A 1 648 ? 19.575 81.653 61.947 0.30 27.86 ? 641 GLU A CD 1 ATOM 4880 O OE1 A GLU A 1 648 ? 21.316 83.320 57.671 0.70 35.58 ? 641 GLU A OE1 1 ATOM 4881 O OE1 B GLU A 1 648 ? 20.619 80.982 62.125 0.30 29.76 ? 641 GLU A OE1 1 ATOM 4882 O OE2 A GLU A 1 648 ? 19.160 83.276 58.099 0.70 37.70 ? 641 GLU A OE2 1 ATOM 4883 O OE2 B GLU A 1 648 ? 19.114 82.396 62.837 0.30 32.20 ? 641 GLU A OE2 1 ATOM 4884 N N . ILE A 1 649 ? 17.152 78.396 59.837 1.00 21.28 ? 642 ILE A N 1 ATOM 4885 C CA . ILE A 1 649 ? 15.916 77.932 60.480 1.00 22.25 ? 642 ILE A CA 1 ATOM 4886 C C . ILE A 1 649 ? 16.178 76.586 61.172 1.00 20.70 ? 642 ILE A C 1 ATOM 4887 O O . ILE A 1 649 ? 15.744 76.375 62.304 1.00 22.22 ? 642 ILE A O 1 ATOM 4888 C CB . ILE A 1 649 ? 14.718 77.873 59.507 1.00 21.44 ? 642 ILE A CB 1 ATOM 4889 C CG1 . ILE A 1 649 ? 14.329 79.292 59.069 1.00 18.79 ? 642 ILE A CG1 1 ATOM 4890 C CG2 . ILE A 1 649 ? 13.524 77.191 60.163 1.00 21.53 ? 642 ILE A CG2 1 ATOM 4891 C CD1 . ILE A 1 649 ? 13.413 79.335 57.846 1.00 20.77 ? 642 ILE A CD1 1 ATOM 4892 N N . ALA A 1 650 ? 16.899 75.694 60.498 1.00 20.18 ? 643 ALA A N 1 ATOM 4893 C CA . ALA A 1 650 ? 17.268 74.402 61.098 1.00 21.58 ? 643 ALA A CA 1 ATOM 4894 C C . ALA A 1 650 ? 18.067 74.606 62.390 1.00 23.60 ? 643 ALA A C 1 ATOM 4895 O O . ALA A 1 650 ? 17.814 73.923 63.404 1.00 23.04 ? 643 ALA A O 1 ATOM 4896 C CB . ALA A 1 650 ? 18.052 73.543 60.094 1.00 23.70 ? 643 ALA A CB 1 ATOM 4897 N N . SER A 1 651 ? 19.018 75.543 62.367 1.00 23.18 ? 644 SER A N 1 ATOM 4898 C CA . SER A 1 651 ? 19.834 75.811 63.557 1.00 24.33 ? 644 SER A CA 1 ATOM 4899 C C . SER A 1 651 ? 18.952 76.280 64.717 1.00 23.93 ? 644 SER A C 1 ATOM 4900 O O . SER A 1 651 ? 19.133 75.833 65.850 1.00 24.66 ? 644 SER A O 1 ATOM 4901 C CB . SER A 1 651 ? 20.928 76.837 63.267 1.00 27.84 ? 644 SER A CB 1 ATOM 4902 O OG . SER A 1 651 ? 21.623 77.166 64.466 0.90 33.38 ? 644 SER A OG 1 ATOM 4903 N N . LYS A 1 652 ? 17.999 77.167 64.431 1.00 23.67 ? 645 LYS A N 1 ATOM 4904 C CA . LYS A 1 652 ? 17.098 77.663 65.463 1.00 25.27 ? 645 LYS A CA 1 ATOM 4905 C C . LYS A 1 652 ? 16.145 76.570 65.986 1.00 24.86 ? 645 LYS A C 1 ATOM 4906 O O . LYS A 1 652 ? 15.926 76.454 67.204 1.00 23.80 ? 645 LYS A O 1 ATOM 4907 C CB . LYS A 1 652 ? 16.342 78.912 64.985 1.00 25.87 ? 645 LYS A CB 1 ATOM 4908 C CG . LYS A 1 652 ? 17.222 80.158 64.861 1.00 28.50 ? 645 LYS A CG 1 ATOM 4909 C CD . LYS A 1 652 ? 17.746 80.648 66.208 1.00 34.55 ? 645 LYS A CD 1 ATOM 4910 C CE . LYS A 1 652 ? 18.761 81.768 66.064 0.20 31.04 ? 645 LYS A CE 1 ATOM 4911 N NZ . LYS A 1 652 ? 19.311 82.134 67.398 0.20 26.03 ? 645 LYS A NZ 1 ATOM 4912 N N . PHE A 1 653 ? 15.613 75.756 65.077 1.00 23.24 ? 646 PHE A N 1 ATOM 4913 C CA . PHE A 1 653 ? 14.801 74.613 65.458 1.00 22.48 ? 646 PHE A CA 1 ATOM 4914 C C . PHE A 1 653 ? 15.580 73.675 66.404 1.00 23.61 ? 646 PHE A C 1 ATOM 4915 O O . PHE A 1 653 ? 15.045 73.227 67.428 1.00 24.91 ? 646 PHE A O 1 ATOM 4916 C CB . PHE A 1 653 ? 14.330 73.846 64.206 1.00 21.76 ? 646 PHE A CB 1 ATOM 4917 C CG . PHE A 1 653 ? 13.499 72.638 64.520 1.00 22.31 ? 646 PHE A CG 1 ATOM 4918 C CD1 . PHE A 1 653 ? 12.127 72.755 64.732 1.00 23.97 ? 646 PHE A CD1 1 ATOM 4919 C CD2 . PHE A 1 653 ? 14.095 71.375 64.621 1.00 23.26 ? 646 PHE A CD2 1 ATOM 4920 C CE1 . PHE A 1 653 ? 11.364 71.638 65.035 1.00 23.53 ? 646 PHE A CE1 1 ATOM 4921 C CE2 . PHE A 1 653 ? 13.335 70.257 64.939 1.00 24.68 ? 646 PHE A CE2 1 ATOM 4922 C CZ . PHE A 1 653 ? 11.972 70.383 65.131 1.00 23.44 ? 646 PHE A CZ 1 ATOM 4923 N N . SER A 1 654 ? 16.834 73.380 66.062 1.00 23.37 ? 647 SER A N 1 ATOM 4924 C CA . SER A 1 654 ? 17.668 72.506 66.880 1.00 25.87 ? 647 SER A CA 1 ATOM 4925 C C . SER A 1 654 ? 17.838 73.052 68.303 1.00 27.81 ? 647 SER A C 1 ATOM 4926 O O . SER A 1 654 ? 17.799 72.281 69.270 1.00 27.59 ? 647 SER A O 1 ATOM 4927 C CB . SER A 1 654 ? 19.028 72.304 66.223 1.00 25.26 ? 647 SER A CB 1 ATOM 4928 O OG A SER A 1 654 ? 18.872 71.674 64.960 0.50 25.88 ? 647 SER A OG 1 ATOM 4929 O OG B SER A 1 654 ? 19.747 71.257 66.842 0.50 26.10 ? 647 SER A OG 1 ATOM 4930 N N . GLU A 1 655 ? 18.015 74.372 68.414 1.00 26.17 ? 648 GLU A N 1 ATOM 4931 C CA . GLU A 1 655 ? 18.087 75.059 69.711 1.00 28.56 ? 648 GLU A CA 1 ATOM 4932 C C . GLU A 1 655 ? 16.812 74.834 70.538 1.00 29.84 ? 648 GLU A C 1 ATOM 4933 O O . GLU A 1 655 ? 16.889 74.460 71.710 1.00 29.39 ? 648 GLU A O 1 ATOM 4934 C CB . GLU A 1 655 ? 18.316 76.562 69.519 1.00 30.42 ? 648 GLU A CB 1 ATOM 4935 C CG . GLU A 1 655 ? 19.728 76.968 69.125 1.00 38.26 ? 648 GLU A CG 1 ATOM 4936 C CD . GLU A 1 655 ? 19.872 78.468 68.882 0.80 44.37 ? 648 GLU A CD 1 ATOM 4937 O OE1 . GLU A 1 655 ? 19.052 79.261 69.395 1.00 44.59 ? 648 GLU A OE1 1 ATOM 4938 O OE2 . GLU A 1 655 ? 20.814 78.861 68.165 0.80 54.52 ? 648 GLU A OE2 1 ATOM 4939 N N . ARG A 1 656 ? 15.647 75.041 69.912 1.00 26.84 ? 649 ARG A N 1 ATOM 4940 C CA . ARG A 1 656 ? 14.357 74.825 70.579 1.00 28.02 ? 649 ARG A CA 1 ATOM 4941 C C . ARG A 1 656 ? 14.154 73.368 70.968 1.00 27.40 ? 649 ARG A C 1 ATOM 4942 O O . ARG A 1 656 ? 13.613 73.083 72.038 1.00 28.14 ? 649 ARG A O 1 ATOM 4943 C CB . ARG A 1 656 ? 13.190 75.293 69.709 1.00 26.41 ? 649 ARG A CB 1 ATOM 4944 C CG . ARG A 1 656 ? 13.204 76.778 69.401 1.00 27.39 ? 649 ARG A CG 1 ATOM 4945 C CD . ARG A 1 656 ? 11.824 77.285 68.986 1.00 25.82 ? 649 ARG A CD 1 ATOM 4946 N NE . ARG A 1 656 ? 11.277 76.558 67.846 1.00 26.11 ? 649 ARG A NE 1 ATOM 4947 C CZ . ARG A 1 656 ? 11.625 76.778 66.580 1.00 26.26 ? 649 ARG A CZ 1 ATOM 4948 N NH1 . ARG A 1 656 ? 12.544 77.698 66.291 1.00 26.45 ? 649 ARG A NH1 1 ATOM 4949 N NH2 . ARG A 1 656 ? 11.066 76.077 65.603 1.00 26.05 ? 649 ARG A NH2 1 ATOM 4950 N N . LEU A 1 657 ? 14.612 72.455 70.110 1.00 27.30 ? 650 LEU A N 1 ATOM 4951 C CA . LEU A 1 657 ? 14.439 71.018 70.333 1.00 29.79 ? 650 LEU A CA 1 ATOM 4952 C C . LEU A 1 657 ? 15.156 70.576 71.604 1.00 31.87 ? 650 LEU A C 1 ATOM 4953 O O . LEU A 1 657 ? 14.738 69.638 72.290 1.00 36.10 ? 650 LEU A O 1 ATOM 4954 C CB . LEU A 1 657 ? 14.975 70.230 69.141 1.00 31.59 ? 650 LEU A CB 1 ATOM 4955 C CG . LEU A 1 657 ? 14.552 68.773 69.009 1.00 30.08 ? 650 LEU A CG 1 ATOM 4956 C CD1 . LEU A 1 657 ? 13.059 68.669 68.728 1.00 29.12 ? 650 LEU A CD1 1 ATOM 4957 C CD2 . LEU A 1 657 ? 15.372 68.105 67.902 1.00 29.82 ? 650 LEU A CD2 1 ATOM 4958 N N . GLN A 1 658 ? 16.249 71.239 71.920 1.00 35.11 ? 651 GLN A N 1 ATOM 4959 C CA . GLN A 1 658 ? 16.943 70.858 73.125 1.00 42.04 ? 651 GLN A CA 1 ATOM 4960 C C . GLN A 1 658 ? 16.586 71.726 74.326 1.00 41.20 ? 651 GLN A C 1 ATOM 4961 O O . GLN A 1 658 ? 16.874 71.362 75.459 1.00 55.20 ? 651 GLN A O 1 ATOM 4962 C CB . GLN A 1 658 ? 18.437 70.737 72.882 1.00 44.04 ? 651 GLN A CB 1 ATOM 4963 C CG . GLN A 1 658 ? 19.125 71.960 72.317 1.00 47.60 ? 651 GLN A CG 1 ATOM 4964 C CD . GLN A 1 658 ? 20.525 71.637 71.822 1.00 65.13 ? 651 GLN A CD 1 ATOM 4965 O OE1 . GLN A 1 658 ? 21.374 72.527 71.720 1.00 81.09 ? 651 GLN A OE1 1 ATOM 4966 N NE2 . GLN A 1 658 ? 20.778 70.354 71.515 1.00 58.68 ? 651 GLN A NE2 1 ATOM 4967 N N . ASP A 1 659 ? 15.931 72.861 74.072 1.00 41.61 ? 652 ASP A N 1 ATOM 4968 C CA . ASP A 1 659 ? 15.517 73.790 75.134 1.00 45.80 ? 652 ASP A CA 1 ATOM 4969 C C . ASP A 1 659 ? 14.105 73.598 75.697 1.00 44.63 ? 652 ASP A C 1 ATOM 4970 O O . ASP A 1 659 ? 13.747 74.300 76.624 1.00 40.70 ? 652 ASP A O 1 ATOM 4971 C CB . ASP A 1 659 ? 15.628 75.256 74.670 1.00 44.77 ? 652 ASP A CB 1 ATOM 4972 C CG . ASP A 1 659 ? 17.045 75.794 74.717 0.80 47.17 ? 652 ASP A CG 1 ATOM 4973 O OD1 . ASP A 1 659 ? 17.226 76.976 74.346 0.80 56.58 ? 652 ASP A OD1 1 ATOM 4974 O OD2 . ASP A 1 659 ? 17.971 75.055 75.120 0.80 49.75 ? 652 ASP A OD2 1 ATOM 4975 N N . PHE A 1 660 ? 13.293 72.699 75.141 1.00 50.56 ? 653 PHE A N 1 ATOM 4976 C CA . PHE A 1 660 ? 11.927 72.510 75.652 1.00 45.09 ? 653 PHE A CA 1 ATOM 4977 C C . PHE A 1 660 ? 11.826 71.370 76.686 1.00 48.09 ? 653 PHE A C 1 ATOM 4978 O O . PHE A 1 660 ? 10.797 71.373 77.537 1.00 66.57 ? 653 PHE A O 1 ATOM 4979 C CB . PHE A 1 660 ? 10.949 72.294 74.481 1.00 41.07 ? 653 PHE A CB 1 ATOM 4980 C CG . PHE A 1 660 ? 10.833 70.868 74.036 1.00 36.24 ? 653 PHE A CG 1 ATOM 4981 C CD1 . PHE A 1 660 ? 9.765 70.087 74.456 1.00 34.52 ? 653 PHE A CD1 1 ATOM 4982 C CD2 . PHE A 1 660 ? 11.788 70.303 73.197 1.00 35.20 ? 653 PHE A CD2 1 ATOM 4983 C CE1 . PHE A 1 660 ? 9.649 68.773 74.040 1.00 33.71 ? 653 PHE A CE1 1 ATOM 4984 C CE2 . PHE A 1 660 ? 11.682 68.984 72.785 1.00 39.07 ? 653 PHE A CE2 1 ATOM 4985 C CZ . PHE A 1 660 ? 10.611 68.219 73.210 1.00 39.34 ? 653 PHE A CZ 1 ATOM 4986 N N A SER A 1 663 ? 8.939 68.813 79.825 0.50 22.39 ? 656 SER A N 1 ATOM 4987 N N B SER A 1 663 ? 8.045 66.194 78.887 0.50 25.11 ? 656 SER A N 1 ATOM 4988 C CA A SER A 1 663 ? 7.805 68.109 80.404 0.50 21.78 ? 656 SER A CA 1 ATOM 4989 C CA B SER A 1 663 ? 6.937 65.716 79.739 0.50 22.99 ? 656 SER A CA 1 ATOM 4990 C C A SER A 1 663 ? 6.511 68.222 79.570 0.50 21.45 ? 656 SER A C 1 ATOM 4991 C C B SER A 1 663 ? 5.572 66.269 79.406 0.50 21.80 ? 656 SER A C 1 ATOM 4992 O O A SER A 1 663 ? 5.470 67.679 79.953 0.50 20.92 ? 656 SER A O 1 ATOM 4993 O O B SER A 1 663 ? 4.569 65.881 80.006 0.50 25.09 ? 656 SER A O 1 ATOM 4994 C CB A SER A 1 663 ? 7.525 68.707 81.767 0.50 16.91 ? 656 SER A CB 1 ATOM 4995 C CB B SER A 1 663 ? 7.209 66.001 81.203 0.50 22.46 ? 656 SER A CB 1 ATOM 4996 O OG A SER A 1 663 ? 7.067 70.016 81.573 0.50 16.42 ? 656 SER A OG 1 ATOM 4997 O OG B SER A 1 663 ? 7.596 64.798 81.727 0.50 17.09 ? 656 SER A OG 1 ATOM 4998 N N A ASN A 1 664 ? 6.556 68.949 78.457 0.50 20.64 ? 657 ASN A N 1 ATOM 4999 N N B ASN A 1 664 ? 5.545 67.204 78.474 0.50 20.91 ? 657 ASN A N 1 ATOM 5000 C CA A ASN A 1 664 ? 5.357 69.196 77.655 0.50 20.64 ? 657 ASN A CA 1 ATOM 5001 C CA B ASN A 1 664 ? 4.305 67.778 78.013 0.50 23.72 ? 657 ASN A CA 1 ATOM 5002 C C A ASN A 1 664 ? 5.236 68.273 76.447 0.50 20.85 ? 657 ASN A C 1 ATOM 5003 C C B ASN A 1 664 ? 3.890 67.049 76.733 0.50 24.36 ? 657 ASN A C 1 ATOM 5004 O O A ASN A 1 664 ? 5.972 68.419 75.467 0.50 20.00 ? 657 ASN A O 1 ATOM 5005 O O B ASN A 1 664 ? 4.410 67.330 75.657 0.50 22.82 ? 657 ASN A O 1 ATOM 5006 C CB A ASN A 1 664 ? 5.323 70.645 77.186 0.50 22.74 ? 657 ASN A CB 1 ATOM 5007 C CB B ASN A 1 664 ? 4.527 69.272 77.779 0.50 24.39 ? 657 ASN A CB 1 ATOM 5008 C CG A ASN A 1 664 ? 3.964 71.048 76.665 0.50 22.49 ? 657 ASN A CG 1 ATOM 5009 C CG B ASN A 1 664 ? 3.259 70.002 77.414 0.50 27.23 ? 657 ASN A CG 1 ATOM 5010 O OD1 A ASN A 1 664 ? 3.317 70.298 75.931 0.50 23.30 ? 657 ASN A OD1 1 ATOM 5011 O OD1 B ASN A 1 664 ? 2.407 69.471 76.706 0.50 33.18 ? 657 ASN A OD1 1 ATOM 5012 N ND2 A ASN A 1 664 ? 3.520 72.235 77.042 0.50 26.52 ? 657 ASN A ND2 1 ATOM 5013 N ND2 B ASN A 1 664 ? 3.136 71.238 77.883 0.50 29.92 ? 657 ASN A ND2 1 ATOM 5014 N N A PRO A 1 665 ? 4.290 67.320 76.502 0.50 19.52 ? 658 PRO A N 1 ATOM 5015 N N B PRO A 1 665 ? 2.961 66.082 76.847 0.50 26.13 ? 658 PRO A N 1 ATOM 5016 C CA A PRO A 1 665 ? 4.164 66.328 75.432 0.50 19.35 ? 658 PRO A CA 1 ATOM 5017 C CA B PRO A 1 665 ? 2.624 65.256 75.688 0.50 24.80 ? 658 PRO A CA 1 ATOM 5018 C C A PRO A 1 665 ? 3.592 66.891 74.118 0.50 19.39 ? 658 PRO A C 1 ATOM 5019 C C B PRO A 1 665 ? 2.360 66.027 74.390 0.50 25.06 ? 658 PRO A C 1 ATOM 5020 O O A PRO A 1 665 ? 3.810 66.296 73.065 0.50 18.71 ? 658 PRO A O 1 ATOM 5021 O O B PRO A 1 665 ? 2.950 65.691 73.367 0.50 24.73 ? 658 PRO A O 1 ATOM 5022 C CB A PRO A 1 665 ? 3.193 65.303 76.037 0.50 19.27 ? 658 PRO A CB 1 ATOM 5023 C CB B PRO A 1 665 ? 1.373 64.510 76.150 0.50 25.79 ? 658 PRO A CB 1 ATOM 5024 C CG A PRO A 1 665 ? 2.301 66.155 76.887 0.50 20.51 ? 658 PRO A CG 1 ATOM 5025 C CG B PRO A 1 665 ? 1.581 64.363 77.617 0.50 24.16 ? 658 PRO A CG 1 ATOM 5026 C CD A PRO A 1 665 ? 3.237 67.158 77.526 0.50 19.53 ? 658 PRO A CD 1 ATOM 5027 C CD B PRO A 1 665 ? 2.232 65.653 78.055 0.50 24.20 ? 658 PRO A CD 1 ATOM 5028 N N A ILE A 1 666 ? 2.854 68.001 74.178 0.50 18.75 ? 659 ILE A N 1 ATOM 5029 N N B ILE A 1 666 ? 1.499 67.046 74.407 0.50 24.89 ? 659 ILE A N 1 ATOM 5030 C CA A ILE A 1 666 ? 2.325 68.626 72.963 0.50 20.54 ? 659 ILE A CA 1 ATOM 5031 C CA B ILE A 1 666 ? 1.191 67.741 73.148 0.50 25.06 ? 659 ILE A CA 1 ATOM 5032 C C A ILE A 1 666 ? 3.445 69.335 72.210 0.50 19.08 ? 659 ILE A C 1 ATOM 5033 C C B ILE A 1 666 ? 2.356 68.576 72.636 0.50 23.74 ? 659 ILE A C 1 ATOM 5034 O O A ILE A 1 666 ? 3.552 69.216 71.002 0.50 18.44 ? 659 ILE A O 1 ATOM 5035 O O B ILE A 1 666 ? 2.564 68.680 71.435 0.50 23.53 ? 659 ILE A O 1 ATOM 5036 C CB A ILE A 1 666 ? 1.217 69.667 73.235 0.50 22.03 ? 659 ILE A CB 1 ATOM 5037 C CB B ILE A 1 666 ? -0.105 68.577 73.210 0.50 24.17 ? 659 ILE A CB 1 ATOM 5038 C CG1 A ILE A 1 666 ? 0.126 69.106 74.154 0.50 25.85 ? 659 ILE A CG1 1 ATOM 5039 C CG1 B ILE A 1 666 ? -1.298 67.632 73.259 0.50 28.80 ? 659 ILE A CG1 1 ATOM 5040 C CG2 A ILE A 1 666 ? 0.636 70.157 71.915 0.50 20.22 ? 659 ILE A CG2 1 ATOM 5041 C CG2 B ILE A 1 666 ? -0.220 69.490 72.004 0.50 28.44 ? 659 ILE A CG2 1 ATOM 5042 C CD1 A ILE A 1 666 ? -0.426 67.771 73.708 0.50 30.42 ? 659 ILE A CD1 1 ATOM 5043 C CD1 B ILE A 1 666 ? -0.988 66.284 72.652 0.50 26.88 ? 659 ILE A CD1 1 ATOM 5044 N N A VAL A 1 667 ? 4.265 70.093 72.929 0.50 18.42 ? 660 VAL A N 1 ATOM 5045 N N B VAL A 1 667 ? 3.130 69.174 73.535 0.50 22.84 ? 660 VAL A N 1 ATOM 5046 C CA A VAL A 1 667 ? 5.431 70.716 72.303 0.50 19.99 ? 660 VAL A CA 1 ATOM 5047 C CA B VAL A 1 667 ? 4.300 69.922 73.065 0.50 20.63 ? 660 VAL A CA 1 ATOM 5048 C C A VAL A 1 667 ? 6.378 69.644 71.767 0.50 20.23 ? 660 VAL A C 1 ATOM 5049 C C B VAL A 1 667 ? 5.301 68.974 72.387 0.50 19.25 ? 660 VAL A C 1 ATOM 5050 O O A VAL A 1 667 ? 6.946 69.788 70.681 0.50 20.46 ? 660 VAL A O 1 ATOM 5051 O O B VAL A 1 667 ? 5.862 69.291 71.330 0.50 20.38 ? 660 VAL A O 1 ATOM 5052 C CB A VAL A 1 667 ? 6.172 71.629 73.288 0.50 19.24 ? 660 VAL A CB 1 ATOM 5053 C CB B VAL A 1 667 ? 4.977 70.738 74.183 0.50 20.56 ? 660 VAL A CB 1 ATOM 5054 C CG1 A VAL A 1 667 ? 7.473 72.130 72.675 0.50 20.32 ? 660 VAL A CG1 1 ATOM 5055 C CG1 B VAL A 1 667 ? 6.315 71.298 73.702 0.50 22.11 ? 660 VAL A CG1 1 ATOM 5056 C CG2 A VAL A 1 667 ? 5.259 72.776 73.689 0.50 19.85 ? 660 VAL A CG2 1 ATOM 5057 C CG2 B VAL A 1 667 ? 4.061 71.864 74.635 0.50 21.55 ? 660 VAL A CG2 1 ATOM 5058 N N A LEU A 1 668 ? 6.544 68.569 72.536 0.50 20.19 ? 661 LEU A N 1 ATOM 5059 N N B LEU A 1 668 ? 5.510 67.805 72.981 0.50 18.34 ? 661 LEU A N 1 ATOM 5060 C CA A LEU A 1 668 ? 7.326 67.420 72.090 0.50 18.69 ? 661 LEU A CA 1 ATOM 5061 C CA B LEU A 1 668 ? 6.435 66.821 72.416 0.50 20.11 ? 661 LEU A CA 1 ATOM 5062 C C A LEU A 1 668 ? 6.773 66.839 70.798 0.50 20.67 ? 661 LEU A C 1 ATOM 5063 C C B LEU A 1 668 ? 5.912 66.325 71.078 0.50 20.19 ? 661 LEU A C 1 ATOM 5064 O O A LEU A 1 668 ? 7.491 66.754 69.799 0.50 17.80 ? 661 LEU A O 1 ATOM 5065 O O B LEU A 1 668 ? 6.672 66.046 70.145 0.50 21.60 ? 661 LEU A O 1 ATOM 5066 C CB A LEU A 1 668 ? 7.379 66.341 73.181 0.50 19.43 ? 661 LEU A CB 1 ATOM 5067 C CB B LEU A 1 668 ? 6.639 65.650 73.381 0.50 19.20 ? 661 LEU A CB 1 ATOM 5068 C CG A LEU A 1 668 ? 7.907 64.963 72.766 0.50 18.34 ? 661 LEU A CG 1 ATOM 5069 C CG B LEU A 1 668 ? 7.493 64.464 72.893 0.50 21.70 ? 661 LEU A CG 1 ATOM 5070 C CD1 A LEU A 1 668 ? 9.331 65.026 72.238 0.50 19.48 ? 661 LEU A CD1 1 ATOM 5071 C CD1 B LEU A 1 668 ? 8.928 64.853 72.556 0.50 20.62 ? 661 LEU A CD1 1 ATOM 5072 C CD2 A LEU A 1 668 ? 7.813 64.002 73.939 0.50 17.12 ? 661 LEU A CD2 1 ATOM 5073 C CD2 B LEU A 1 668 ? 7.478 63.378 73.951 0.50 22.49 ? 661 LEU A CD2 1 ATOM 5074 N N A ARG A 1 669 ? 5.502 66.435 70.821 0.50 20.56 ? 662 ARG A N 1 ATOM 5075 N N B ARG A 1 669 ? 4.599 66.223 70.976 0.50 19.66 ? 662 ARG A N 1 ATOM 5076 C CA A ARG A 1 669 ? 4.872 65.835 69.645 0.50 20.82 ? 662 ARG A CA 1 ATOM 5077 C CA B ARG A 1 669 ? 4.007 65.804 69.720 0.50 20.11 ? 662 ARG A CA 1 ATOM 5078 C C A ARG A 1 669 ? 4.777 66.835 68.520 0.50 20.39 ? 662 ARG A C 1 ATOM 5079 C C B ARG A 1 669 ? 4.287 66.774 68.549 0.50 21.14 ? 662 ARG A C 1 ATOM 5080 O O A ARG A 1 669 ? 5.029 66.480 67.377 0.50 18.08 ? 662 ARG A O 1 ATOM 5081 O O B ARG A 1 669 ? 4.444 66.330 67.419 0.50 20.08 ? 662 ARG A O 1 ATOM 5082 C CB A ARG A 1 669 ? 3.481 65.272 69.953 0.50 20.01 ? 662 ARG A CB 1 ATOM 5083 C CB B ARG A 1 669 ? 2.512 65.536 69.910 0.50 17.81 ? 662 ARG A CB 1 ATOM 5084 C CG A ARG A 1 669 ? 2.658 64.940 68.708 0.50 17.91 ? 662 ARG A CG 1 ATOM 5085 C CG B ARG A 1 669 ? 1.816 65.040 68.668 0.50 19.65 ? 662 ARG A CG 1 ATOM 5086 C CD A ARG A 1 669 ? 2.943 63.556 68.122 0.50 15.73 ? 662 ARG A CD 1 ATOM 5087 C CD B ARG A 1 669 ? 1.883 63.533 68.493 0.50 25.18 ? 662 ARG A CD 1 ATOM 5088 N NE A ARG A 1 669 ? 1.722 63.114 67.460 0.50 19.23 ? 662 ARG A NE 1 ATOM 5089 N NE B ARG A 1 669 ? 0.773 63.140 67.626 0.50 24.39 ? 662 ARG A NE 1 ATOM 5090 C CZ A ARG A 1 669 ? 1.229 61.881 67.470 0.50 20.34 ? 662 ARG A CZ 1 ATOM 5091 C CZ B ARG A 1 669 ? 0.416 61.899 67.335 0.50 24.63 ? 662 ARG A CZ 1 ATOM 5092 N NH1 A ARG A 1 669 ? 1.868 60.879 68.074 0.50 20.40 ? 662 ARG A NH1 1 ATOM 5093 N NH1 B ARG A 1 669 ? 1.091 60.859 67.824 0.50 27.50 ? 662 ARG A NH1 1 ATOM 5094 N NH2 A ARG A 1 669 ? 0.077 61.660 66.854 0.50 21.36 ? 662 ARG A NH2 1 ATOM 5095 N NH2 B ARG A 1 669 ? -0.621 61.708 66.530 0.50 23.63 ? 662 ARG A NH2 1 ATOM 5096 N N . MET A 1 670 ? 4.397 68.079 68.831 1.00 22.47 ? 663 MET A N 1 ATOM 5097 C CA . MET A 1 670 ? 4.494 69.139 67.794 1.00 22.06 ? 663 MET A CA 1 ATOM 5098 C C . MET A 1 670 ? 5.896 69.131 67.173 1.00 22.49 ? 663 MET A C 1 ATOM 5099 O O . MET A 1 670 ? 6.037 69.154 65.956 1.00 21.26 ? 663 MET A O 1 ATOM 5100 C CB A MET A 1 670 ? 4.284 70.544 68.380 0.50 21.59 ? 663 MET A CB 1 ATOM 5101 C CB B MET A 1 670 ? 3.996 70.493 68.355 0.50 23.90 ? 663 MET A CB 1 ATOM 5102 C CG A MET A 1 670 ? 4.755 71.689 67.464 0.50 20.81 ? 663 MET A CG 1 ATOM 5103 C CG B MET A 1 670 ? 2.531 70.408 68.852 0.50 24.99 ? 663 MET A CG 1 ATOM 5104 S SD A MET A 1 670 ? 4.569 73.318 68.225 0.50 18.65 ? 663 MET A SD 1 ATOM 5105 S SD B MET A 1 670 ? 1.579 71.866 69.390 0.50 25.11 ? 663 MET A SD 1 ATOM 5106 C CE A MET A 1 670 ? 2.917 73.123 68.860 0.50 27.87 ? 663 MET A CE 1 ATOM 5107 C CE B MET A 1 670 ? 2.483 72.318 70.892 0.50 19.75 ? 663 MET A CE 1 ATOM 5108 N N . MET A 1 671 ? 6.940 69.049 68.009 1.00 23.25 ? 664 MET A N 1 ATOM 5109 C CA . MET A 1 671 ? 8.306 69.015 67.490 1.00 21.84 ? 664 MET A CA 1 ATOM 5110 C C . MET A 1 671 ? 8.600 67.705 66.770 1.00 21.09 ? 664 MET A C 1 ATOM 5111 O O . MET A 1 671 ? 9.287 67.704 65.752 1.00 22.74 ? 664 MET A O 1 ATOM 5112 C CB A MET A 1 671 ? 9.305 69.087 68.668 0.50 23.74 ? 664 MET A CB 1 ATOM 5113 C CB B MET A 1 671 ? 9.365 69.414 68.533 0.50 21.74 ? 664 MET A CB 1 ATOM 5114 C CG A MET A 1 671 ? 9.005 70.146 69.715 0.50 25.36 ? 664 MET A CG 1 ATOM 5115 C CG B MET A 1 671 ? 9.289 70.900 68.865 0.50 18.07 ? 664 MET A CG 1 ATOM 5116 S SD A MET A 1 671 ? 9.035 71.715 68.860 0.50 28.99 ? 664 MET A SD 1 ATOM 5117 S SD B MET A 1 671 ? 10.702 71.634 69.712 0.50 19.84 ? 664 MET A SD 1 ATOM 5118 C CE A MET A 1 671 ? 10.733 72.204 69.149 0.50 29.32 ? 664 MET A CE 1 ATOM 5119 C CE B MET A 1 671 ? 11.711 72.123 68.315 0.50 21.02 ? 664 MET A CE 1 ATOM 5120 N N . ASN A 1 672 ? 8.091 66.596 67.304 1.00 22.24 ? 665 ASN A N 1 ATOM 5121 C CA . ASN A 1 672 ? 8.255 65.302 66.624 1.00 20.24 ? 665 ASN A CA 1 ATOM 5122 C C . ASN A 1 672 ? 7.558 65.316 65.271 1.00 20.91 ? 665 ASN A C 1 ATOM 5123 O O . ASN A 1 672 ? 8.088 64.780 64.303 1.00 21.10 ? 665 ASN A O 1 ATOM 5124 C CB . ASN A 1 672 ? 7.772 64.127 67.484 1.00 20.68 ? 665 ASN A CB 1 ATOM 5125 C CG . ASN A 1 672 ? 8.853 63.636 68.442 1.00 21.52 ? 665 ASN A CG 1 ATOM 5126 O OD1 . ASN A 1 672 ? 10.052 63.792 68.168 1.00 22.18 ? 665 ASN A OD1 1 ATOM 5127 N ND2 . ASN A 1 672 ? 8.448 63.030 69.548 1.00 21.52 ? 665 ASN A ND2 1 ATOM 5128 N N . ASP A 1 673 ? 6.390 65.953 65.199 1.00 19.96 ? 666 ASP A N 1 ATOM 5129 C CA . ASP A 1 673 ? 5.681 66.069 63.906 1.00 19.33 ? 666 ASP A CA 1 ATOM 5130 C C . ASP A 1 673 ? 6.496 66.937 62.936 1.00 18.73 ? 666 ASP A C 1 ATOM 5131 O O . ASP A 1 673 ? 6.592 66.624 61.753 1.00 18.35 ? 666 ASP A O 1 ATOM 5132 C CB . ASP A 1 673 ? 4.254 66.642 64.049 1.00 20.82 ? 666 ASP A CB 1 ATOM 5133 C CG . ASP A 1 673 ? 3.266 65.634 64.614 1.00 21.66 ? 666 ASP A CG 1 ATOM 5134 O OD1 . ASP A 1 673 ? 3.638 64.449 64.803 1.00 22.60 ? 666 ASP A OD1 1 ATOM 5135 O OD2 . ASP A 1 673 ? 2.108 66.037 64.867 1.00 21.69 ? 666 ASP A OD2 1 ATOM 5136 N N . GLN A 1 674 ? 7.113 68.009 63.436 1.00 17.17 ? 667 GLN A N 1 ATOM 5137 C CA . GLN A 1 674 ? 7.988 68.813 62.565 1.00 18.35 ? 667 GLN A CA 1 ATOM 5138 C C . GLN A 1 674 ? 9.154 67.966 62.024 1.00 17.96 ? 667 GLN A C 1 ATOM 5139 O O . GLN A 1 674 ? 9.488 68.042 60.840 1.00 19.91 ? 667 GLN A O 1 ATOM 5140 C CB . GLN A 1 674 ? 8.490 70.073 63.272 1.00 16.88 ? 667 GLN A CB 1 ATOM 5141 C CG . GLN A 1 674 ? 7.358 71.093 63.460 1.00 17.40 ? 667 GLN A CG 1 ATOM 5142 C CD . GLN A 1 674 ? 7.826 72.330 64.189 1.00 18.19 ? 667 GLN A CD 1 ATOM 5143 O OE1 . GLN A 1 674 ? 7.917 72.321 65.405 1.00 22.30 ? 667 GLN A OE1 1 ATOM 5144 N NE2 . GLN A 1 674 ? 8.095 73.424 63.443 1.00 18.32 ? 667 GLN A NE2 1 ATOM 5145 N N . LEU A 1 675 ? 9.754 67.154 62.889 1.00 19.60 ? 668 LEU A N 1 ATOM 5146 C CA . LEU A 1 675 ? 10.807 66.222 62.462 1.00 18.32 ? 668 LEU A CA 1 ATOM 5147 C C . LEU A 1 675 ? 10.315 65.202 61.433 1.00 18.31 ? 668 LEU A C 1 ATOM 5148 O O . LEU A 1 675 ? 10.972 64.956 60.391 1.00 20.72 ? 668 LEU A O 1 ATOM 5149 C CB . LEU A 1 675 ? 11.419 65.514 63.686 1.00 19.75 ? 668 LEU A CB 1 ATOM 5150 C CG . LEU A 1 675 ? 12.300 66.463 64.521 1.00 22.69 ? 668 LEU A CG 1 ATOM 5151 C CD1 . LEU A 1 675 ? 12.751 65.807 65.814 1.00 26.40 ? 668 LEU A CD1 1 ATOM 5152 C CD2 . LEU A 1 675 ? 13.491 66.967 63.705 1.00 25.88 ? 668 LEU A CD2 1 ATOM 5153 N N . MET A 1 676 ? 9.140 64.641 61.701 1.00 19.27 ? 669 MET A N 1 ATOM 5154 C CA . MET A 1 676 ? 8.577 63.601 60.836 1.00 18.67 ? 669 MET A CA 1 ATOM 5155 C C . MET A 1 676 ? 8.201 64.144 59.467 1.00 17.63 ? 669 MET A C 1 ATOM 5156 O O . MET A 1 676 ? 8.441 63.496 58.426 1.00 17.84 ? 669 MET A O 1 ATOM 5157 C CB . MET A 1 676 ? 7.343 62.988 61.497 1.00 18.68 ? 669 MET A CB 1 ATOM 5158 C CG . MET A 1 676 ? 6.691 61.913 60.624 1.00 20.51 ? 669 MET A CG 1 ATOM 5159 S SD . MET A 1 676 ? 5.295 61.129 61.432 1.00 23.51 ? 669 MET A SD 1 ATOM 5160 C CE . MET A 1 676 ? 4.054 62.423 61.301 1.00 21.36 ? 669 MET A CE 1 ATOM 5161 N N . PHE A 1 677 ? 7.581 65.324 59.462 1.00 16.79 ? 670 PHE A N 1 ATOM 5162 C CA . PHE A 1 677 ? 7.101 65.907 58.198 1.00 16.28 ? 670 PHE A CA 1 ATOM 5163 C C . PHE A 1 677 ? 8.190 66.654 57.435 1.00 16.66 ? 670 PHE A C 1 ATOM 5164 O O . PHE A 1 677 ? 7.931 67.184 56.354 1.00 16.93 ? 670 PHE A O 1 ATOM 5165 C CB . PHE A 1 677 ? 5.865 66.795 58.445 1.00 15.75 ? 670 PHE A CB 1 ATOM 5166 C CG . PHE A 1 677 ? 4.613 66.019 58.734 1.00 16.66 ? 670 PHE A CG 1 ATOM 5167 C CD1 . PHE A 1 677 ? 4.120 65.082 57.804 1.00 17.26 ? 670 PHE A CD1 1 ATOM 5168 C CD2 . PHE A 1 677 ? 3.883 66.248 59.917 1.00 18.50 ? 670 PHE A CD2 1 ATOM 5169 C CE1 . PHE A 1 677 ? 2.949 64.378 58.054 1.00 16.99 ? 670 PHE A CE1 1 ATOM 5170 C CE2 . PHE A 1 677 ? 2.697 65.548 60.174 1.00 16.98 ? 670 PHE A CE2 1 ATOM 5171 C CZ . PHE A 1 677 ? 2.221 64.611 59.237 1.00 18.07 ? 670 PHE A CZ 1 ATOM 5172 N N . LEU A 1 678 ? 9.415 66.695 57.974 1.00 17.07 ? 671 LEU A N 1 ATOM 5173 C CA . LEU A 1 678 ? 10.506 67.389 57.267 1.00 15.97 ? 671 LEU A CA 1 ATOM 5174 C C . LEU A 1 678 ? 10.868 66.685 55.942 1.00 14.94 ? 671 LEU A C 1 ATOM 5175 O O . LEU A 1 678 ? 10.901 67.320 54.883 1.00 15.87 ? 671 LEU A O 1 ATOM 5176 C CB . LEU A 1 678 ? 11.738 67.598 58.166 1.00 17.83 ? 671 LEU A CB 1 ATOM 5177 C CG . LEU A 1 678 ? 12.892 68.362 57.497 1.00 17.43 ? 671 LEU A CG 1 ATOM 5178 C CD1 . LEU A 1 678 ? 12.517 69.734 56.932 1.00 20.35 ? 671 LEU A CD1 1 ATOM 5179 C CD2 . LEU A 1 678 ? 14.026 68.489 58.522 1.00 20.10 ? 671 LEU A CD2 1 ATOM 5180 N N . GLU A 1 679 ? 11.137 65.382 55.988 1.00 15.22 ? 672 GLU A N 1 ATOM 5181 C CA . GLU A 1 679 ? 11.322 64.630 54.735 1.00 14.93 ? 672 GLU A CA 1 ATOM 5182 C C . GLU A 1 679 ? 10.107 64.814 53.802 1.00 14.45 ? 672 GLU A C 1 ATOM 5183 O O . GLU A 1 679 ? 10.252 64.979 52.556 1.00 14.38 ? 672 GLU A O 1 ATOM 5184 C CB . GLU A 1 679 ? 11.523 63.139 55.014 1.00 14.82 ? 672 GLU A CB 1 ATOM 5185 C CG . GLU A 1 679 ? 12.097 62.431 53.810 1.00 14.58 ? 672 GLU A CG 1 ATOM 5186 C CD . GLU A 1 679 ? 13.596 62.704 53.690 1.00 17.09 ? 672 GLU A CD 1 ATOM 5187 O OE1 . GLU A 1 679 ? 14.354 62.283 54.583 1.00 17.33 ? 672 GLU A OE1 1 ATOM 5188 O OE2 . GLU A 1 679 ? 14.010 63.367 52.725 1.00 16.00 ? 672 GLU A OE2 1 ATOM 5189 N N . ARG A 1 680 ? 8.919 64.830 54.409 1.00 13.96 ? 673 ARG A N 1 ATOM 5190 C CA . ARG A 1 680 ? 7.662 64.936 53.649 1.00 14.50 ? 673 ARG A CA 1 ATOM 5191 C C . ARG A 1 680 ? 7.624 66.261 52.881 1.00 14.32 ? 673 ARG A C 1 ATOM 5192 O O . ARG A 1 680 ? 7.029 66.343 51.793 1.00 14.09 ? 673 ARG A O 1 ATOM 5193 C CB . ARG A 1 680 ? 6.424 64.800 54.560 1.00 14.42 ? 673 ARG A CB 1 ATOM 5194 C CG . ARG A 1 680 ? 5.212 64.165 53.822 1.00 13.55 ? 673 ARG A CG 1 ATOM 5195 C CD . ARG A 1 680 ? 5.305 62.630 53.958 1.00 15.25 ? 673 ARG A CD 1 ATOM 5196 N NE . ARG A 1 680 ? 4.934 62.159 55.310 1.00 13.26 ? 673 ARG A NE 1 ATOM 5197 C CZ . ARG A 1 680 ? 5.758 61.628 56.225 1.00 13.70 ? 673 ARG A CZ 1 ATOM 5198 N NH1 . ARG A 1 680 ? 7.086 61.496 56.011 1.00 14.78 ? 673 ARG A NH1 1 ATOM 5199 N NH2 . ARG A 1 680 ? 5.237 61.217 57.379 1.00 16.59 ? 673 ARG A NH2 1 ATOM 5200 N N . ALA A 1 681 ? 8.283 67.287 53.431 1.00 13.90 ? 674 ALA A N 1 ATOM 5201 C CA . ALA A 1 681 ? 8.212 68.611 52.831 1.00 13.51 ? 674 ALA A CA 1 ATOM 5202 C C . ALA A 1 681 ? 8.935 68.698 51.509 1.00 13.63 ? 674 ALA A C 1 ATOM 5203 O O . ALA A 1 681 ? 8.660 69.623 50.731 1.00 15.41 ? 674 ALA A O 1 ATOM 5204 C CB . ALA A 1 681 ? 8.733 69.645 53.803 1.00 14.79 ? 674 ALA A CB 1 ATOM 5205 N N . PHE A 1 682 ? 9.839 67.752 51.229 1.00 14.91 ? 675 PHE A N 1 ATOM 5206 C CA . PHE A 1 682 ? 10.571 67.767 49.940 1.00 13.80 ? 675 PHE A CA 1 ATOM 5207 C C . PHE A 1 682 ? 9.773 67.180 48.793 1.00 14.31 ? 675 PHE A C 1 ATOM 5208 O O . PHE A 1 682 ? 10.212 67.222 47.661 1.00 15.41 ? 675 PHE A O 1 ATOM 5209 C CB . PHE A 1 682 ? 11.915 67.058 50.092 1.00 13.84 ? 675 PHE A CB 1 ATOM 5210 C CG . PHE A 1 682 ? 12.845 67.802 51.001 1.00 14.68 ? 675 PHE A CG 1 ATOM 5211 C CD1 . PHE A 1 682 ? 13.286 69.088 50.657 1.00 15.68 ? 675 PHE A CD1 1 ATOM 5212 C CD2 . PHE A 1 682 ? 13.252 67.253 52.209 1.00 15.47 ? 675 PHE A CD2 1 ATOM 5213 C CE1 . PHE A 1 682 ? 14.152 69.806 51.494 1.00 15.91 ? 675 PHE A CE1 1 ATOM 5214 C CE2 . PHE A 1 682 ? 14.112 67.972 53.072 1.00 16.45 ? 675 PHE A CE2 1 ATOM 5215 C CZ . PHE A 1 682 ? 14.569 69.255 52.709 1.00 17.05 ? 675 PHE A CZ 1 ATOM 5216 N N . ILE A 1 683 ? 8.596 66.650 49.092 1.00 15.06 ? 676 ILE A N 1 ATOM 5217 C CA . ILE A 1 683 ? 7.683 66.105 48.078 1.00 14.13 ? 676 ILE A CA 1 ATOM 5218 C C . ILE A 1 683 ? 6.968 67.235 47.310 1.00 14.50 ? 676 ILE A C 1 ATOM 5219 O O . ILE A 1 683 ? 6.414 68.171 47.906 1.00 16.94 ? 676 ILE A O 1 ATOM 5220 C CB . ILE A 1 683 ? 6.651 65.135 48.746 1.00 12.58 ? 676 ILE A CB 1 ATOM 5221 C CG1 . ILE A 1 683 ? 7.409 63.912 49.329 1.00 12.97 ? 676 ILE A CG1 1 ATOM 5222 C CG2 . ILE A 1 683 ? 5.525 64.731 47.766 1.00 15.38 ? 676 ILE A CG2 1 ATOM 5223 C CD1 . ILE A 1 683 ? 8.193 63.100 48.292 1.00 12.93 ? 676 ILE A CD1 1 ATOM 5224 N N . ASP A 1 684 ? 6.970 67.130 45.986 1.00 14.58 ? 677 ASP A N 1 ATOM 5225 C CA . ASP A 1 684 ? 6.190 68.020 45.124 1.00 15.65 ? 677 ASP A CA 1 ATOM 5226 C C . ASP A 1 684 ? 5.023 67.186 44.597 1.00 15.56 ? 677 ASP A C 1 ATOM 5227 O O . ASP A 1 684 ? 5.251 66.190 43.915 1.00 15.88 ? 677 ASP A O 1 ATOM 5228 C CB . ASP A 1 684 ? 7.056 68.489 43.954 1.00 16.49 ? 677 ASP A CB 1 ATOM 5229 C CG . ASP A 1 684 ? 6.374 69.533 43.086 1.00 15.36 ? 677 ASP A CG 1 ATOM 5230 O OD1 . ASP A 1 684 ? 5.124 69.562 43.002 1.00 17.14 ? 677 ASP A OD1 1 ATOM 5231 O OD2 . ASP A 1 684 ? 7.120 70.324 42.455 1.00 16.83 ? 677 ASP A OD2 1 ATOM 5232 N N . PRO A 1 685 ? 3.772 67.567 44.919 1.00 17.17 ? 678 PRO A N 1 ATOM 5233 C CA . PRO A 1 685 ? 2.642 66.738 44.479 1.00 19.35 ? 678 PRO A CA 1 ATOM 5234 C C . PRO A 1 685 ? 2.511 66.655 42.945 1.00 18.60 ? 678 PRO A C 1 ATOM 5235 O O . PRO A 1 685 ? 1.800 65.796 42.429 1.00 24.17 ? 678 PRO A O 1 ATOM 5236 C CB . PRO A 1 685 ? 1.411 67.442 45.103 1.00 20.85 ? 678 PRO A CB 1 ATOM 5237 C CG . PRO A 1 685 ? 1.847 68.833 45.380 1.00 22.53 ? 678 PRO A CG 1 ATOM 5238 C CD . PRO A 1 685 ? 3.336 68.799 45.619 1.00 18.41 ? 678 PRO A CD 1 ATOM 5239 N N . LEU A 1 686 ? 3.202 67.518 42.212 1.00 17.63 ? 679 LEU A N 1 ATOM 5240 C CA . LEU A 1 686 ? 3.168 67.441 40.741 1.00 16.17 ? 679 LEU A CA 1 ATOM 5241 C C . LEU A 1 686 ? 4.222 66.491 40.141 1.00 17.51 ? 679 LEU A C 1 ATOM 5242 O O . LEU A 1 686 ? 4.209 66.228 38.939 1.00 17.69 ? 679 LEU A O 1 ATOM 5243 C CB . LEU A 1 686 ? 3.338 68.840 40.155 1.00 16.93 ? 679 LEU A CB 1 ATOM 5244 C CG . LEU A 1 686 ? 2.215 69.820 40.537 1.00 18.14 ? 679 LEU A CG 1 ATOM 5245 C CD1 . LEU A 1 686 ? 2.450 71.169 39.873 1.00 18.91 ? 679 LEU A CD1 1 ATOM 5246 C CD2 . LEU A 1 686 ? 0.824 69.283 40.174 1.00 21.84 ? 679 LEU A CD2 1 ATOM 5247 N N . GLY A 1 687 ? 5.113 65.975 40.986 1.00 16.40 ? 680 GLY A N 1 ATOM 5248 C CA . GLY A 1 687 ? 6.172 65.052 40.563 1.00 18.02 ? 680 GLY A CA 1 ATOM 5249 C C . GLY A 1 687 ? 7.221 65.733 39.698 1.00 16.63 ? 680 GLY A C 1 ATOM 5250 O O . GLY A 1 687 ? 7.153 66.927 39.426 1.00 18.50 ? 680 GLY A O 1 ATOM 5251 N N . LEU A 1 688 ? 8.203 64.958 39.271 1.00 16.31 ? 681 LEU A N 1 ATOM 5252 C CA . LEU A 1 688 ? 9.212 65.432 38.324 1.00 16.92 ? 681 LEU A CA 1 ATOM 5253 C C . LEU A 1 688 ? 8.741 65.247 36.876 1.00 16.61 ? 681 LEU A C 1 ATOM 5254 O O . LEU A 1 688 ? 7.851 64.458 36.612 1.00 18.54 ? 681 LEU A O 1 ATOM 5255 C CB . LEU A 1 688 ? 10.523 64.686 38.608 1.00 17.78 ? 681 LEU A CB 1 ATOM 5256 C CG . LEU A 1 688 ? 11.178 65.071 39.951 1.00 17.00 ? 681 LEU A CG 1 ATOM 5257 C CD1 . LEU A 1 688 ? 12.231 64.030 40.282 1.00 20.12 ? 681 LEU A CD1 1 ATOM 5258 C CD2 . LEU A 1 688 ? 11.791 66.493 39.923 1.00 21.09 ? 681 LEU A CD2 1 ATOM 5259 N N . PRO A 1 689 ? 9.309 66.009 35.931 1.00 20.00 ? 682 PRO A N 1 ATOM 5260 C CA . PRO A 1 689 ? 8.832 65.955 34.545 1.00 19.44 ? 682 PRO A CA 1 ATOM 5261 C C . PRO A 1 689 ? 8.737 64.534 33.974 1.00 19.91 ? 682 PRO A C 1 ATOM 5262 O O . PRO A 1 689 ? 9.726 63.793 33.922 1.00 19.93 ? 682 PRO A O 1 ATOM 5263 C CB . PRO A 1 689 ? 9.853 66.839 33.788 1.00 20.76 ? 682 PRO A CB 1 ATOM 5264 C CG . PRO A 1 689 ? 10.335 67.789 34.846 1.00 21.81 ? 682 PRO A CG 1 ATOM 5265 C CD . PRO A 1 689 ? 10.428 66.953 36.091 1.00 20.49 ? 682 PRO A CD 1 ATOM 5266 N N . ASP A 1 690 ? 7.523 64.161 33.571 1.00 18.87 ? 683 ASP A N 1 ATOM 5267 C CA . ASP A 1 690 ? 7.228 62.846 32.983 1.00 21.11 ? 683 ASP A CA 1 ATOM 5268 C C . ASP A 1 690 ? 7.485 61.656 33.906 1.00 18.01 ? 683 ASP A C 1 ATOM 5269 O O . ASP A 1 690 ? 7.436 60.495 33.473 1.00 18.08 ? 683 ASP A O 1 ATOM 5270 C CB . ASP A 1 690 ? 7.944 62.646 31.632 1.00 23.85 ? 683 ASP A CB 1 ATOM 5271 C CG . ASP A 1 690 ? 7.596 63.724 30.621 1.00 32.35 ? 683 ASP A CG 1 ATOM 5272 O OD1 . ASP A 1 690 ? 6.402 64.042 30.441 1.00 34.06 ? 683 ASP A OD1 1 ATOM 5273 O OD2 . ASP A 1 690 ? 8.533 64.252 29.991 1.00 38.17 ? 683 ASP A OD2 1 ATOM 5274 N N . ARG A 1 691 ? 7.706 61.936 35.187 1.00 15.91 ? 684 ARG A N 1 ATOM 5275 C CA . ARG A 1 691 ? 7.937 60.873 36.189 1.00 15.35 ? 684 ARG A CA 1 ATOM 5276 C C . ARG A 1 691 ? 7.103 61.222 37.432 1.00 14.88 ? 684 ARG A C 1 ATOM 5277 O O . ARG A 1 691 ? 7.627 61.618 38.488 1.00 14.12 ? 684 ARG A O 1 ATOM 5278 C CB . ARG A 1 691 ? 9.441 60.727 36.516 1.00 15.35 ? 684 ARG A CB 1 ATOM 5279 C CG . ARG A 1 691 ? 10.266 60.264 35.300 1.00 16.01 ? 684 ARG A CG 1 ATOM 5280 C CD . ARG A 1 691 ? 11.703 59.836 35.635 1.00 15.34 ? 684 ARG A CD 1 ATOM 5281 N NE . ARG A 1 691 ? 12.478 60.961 36.200 1.00 16.58 ? 684 ARG A NE 1 ATOM 5282 C CZ . ARG A 1 691 ? 13.633 60.858 36.860 1.00 17.68 ? 684 ARG A CZ 1 ATOM 5283 N NH1 . ARG A 1 691 ? 14.211 59.662 37.023 1.00 17.00 ? 684 ARG A NH1 1 ATOM 5284 N NH2 . ARG A 1 691 ? 14.225 61.964 37.352 1.00 19.11 ? 684 ARG A NH2 1 ATOM 5285 N N . PRO A 1 692 ? 5.788 61.019 37.325 1.00 14.80 ? 685 PRO A N 1 ATOM 5286 C CA . PRO A 1 692 ? 4.892 61.516 38.368 1.00 15.62 ? 685 PRO A CA 1 ATOM 5287 C C . PRO A 1 692 ? 5.053 60.821 39.705 1.00 14.69 ? 685 PRO A C 1 ATOM 5288 O O . PRO A 1 692 ? 4.577 61.368 40.703 1.00 15.36 ? 685 PRO A O 1 ATOM 5289 C CB . PRO A 1 692 ? 3.487 61.241 37.797 1.00 17.75 ? 685 PRO A CB 1 ATOM 5290 C CG . PRO A 1 692 ? 3.688 60.139 36.816 1.00 17.45 ? 685 PRO A CG 1 ATOM 5291 C CD . PRO A 1 692 ? 5.045 60.428 36.203 1.00 16.35 ? 685 PRO A CD 1 ATOM 5292 N N . PHE A 1 693 ? 5.691 59.640 39.735 1.00 13.88 ? 686 PHE A N 1 ATOM 5293 C CA . PHE A 1 693 ? 5.885 58.910 40.991 1.00 13.84 ? 686 PHE A CA 1 ATOM 5294 C C . PHE A 1 693 ? 7.244 59.171 41.641 1.00 13.73 ? 686 PHE A C 1 ATOM 5295 O O . PHE A 1 693 ? 7.513 58.682 42.739 1.00 15.32 ? 686 PHE A O 1 ATOM 5296 C CB . PHE A 1 693 ? 5.590 57.406 40.824 1.00 13.84 ? 686 PHE A CB 1 ATOM 5297 C CG . PHE A 1 693 ? 4.192 57.153 40.323 1.00 13.27 ? 686 PHE A CG 1 ATOM 5298 C CD1 . PHE A 1 693 ? 3.075 57.544 41.093 1.00 15.67 ? 686 PHE A CD1 1 ATOM 5299 C CD2 . PHE A 1 693 ? 3.976 56.599 39.038 1.00 16.12 ? 686 PHE A CD2 1 ATOM 5300 C CE1 . PHE A 1 693 ? 1.776 57.333 40.616 1.00 15.04 ? 686 PHE A CE1 1 ATOM 5301 C CE2 . PHE A 1 693 ? 2.678 56.403 38.566 1.00 15.76 ? 686 PHE A CE2 1 ATOM 5302 C CZ . PHE A 1 693 ? 1.586 56.768 39.357 1.00 16.46 ? 686 PHE A CZ 1 ATOM 5303 N N . TYR A 1 694 ? 8.056 59.996 40.995 1.00 13.22 ? 687 TYR A N 1 ATOM 5304 C CA . TYR A 1 694 ? 9.279 60.505 41.632 1.00 12.74 ? 687 TYR A CA 1 ATOM 5305 C C . TYR A 1 694 ? 8.953 61.924 42.022 1.00 13.94 ? 687 TYR A C 1 ATOM 5306 O O . TYR A 1 694 ? 8.987 62.855 41.169 1.00 16.26 ? 687 TYR A O 1 ATOM 5307 C CB . TYR A 1 694 ? 10.471 60.430 40.668 1.00 14.14 ? 687 TYR A CB 1 ATOM 5308 C CG . TYR A 1 694 ? 10.936 59.003 40.384 1.00 13.88 ? 687 TYR A CG 1 ATOM 5309 C CD1 . TYR A 1 694 ? 10.661 57.943 41.282 1.00 15.08 ? 687 TYR A CD1 1 ATOM 5310 C CD2 . TYR A 1 694 ? 11.664 58.715 39.223 1.00 16.12 ? 687 TYR A CD2 1 ATOM 5311 C CE1 . TYR A 1 694 ? 11.109 56.643 41.015 1.00 14.94 ? 687 TYR A CE1 1 ATOM 5312 C CE2 . TYR A 1 694 ? 12.103 57.414 38.940 1.00 15.17 ? 687 TYR A CE2 1 ATOM 5313 C CZ . TYR A 1 694 ? 11.827 56.387 39.840 1.00 14.92 ? 687 TYR A CZ 1 ATOM 5314 O OH . TYR A 1 694 ? 12.302 55.116 39.574 1.00 16.80 ? 687 TYR A OH 1 ATOM 5315 N N A ARG A 1 695 ? 8.641 62.118 43.303 0.70 12.62 ? 688 ARG A N 1 ATOM 5316 N N B ARG A 1 695 ? 8.590 62.094 43.296 0.30 13.07 ? 688 ARG A N 1 ATOM 5317 C CA A ARG A 1 695 ? 8.081 63.396 43.763 0.70 13.03 ? 688 ARG A CA 1 ATOM 5318 C CA B ARG A 1 695 ? 8.017 63.347 43.798 0.30 13.70 ? 688 ARG A CA 1 ATOM 5319 C C A ARG A 1 695 ? 9.043 64.181 44.630 0.70 13.18 ? 688 ARG A C 1 ATOM 5320 C C B ARG A 1 695 ? 8.947 64.103 44.758 0.30 13.36 ? 688 ARG A C 1 ATOM 5321 O O A ARG A 1 695 ? 8.829 65.370 44.877 0.70 13.72 ? 688 ARG A O 1 ATOM 5322 O O B ARG A 1 695 ? 8.619 65.209 45.180 0.30 13.69 ? 688 ARG A O 1 ATOM 5323 C CB A ARG A 1 695 ? 6.764 63.144 44.515 0.70 11.60 ? 688 ARG A CB 1 ATOM 5324 C CB B ARG A 1 695 ? 6.648 63.087 44.471 0.30 13.12 ? 688 ARG A CB 1 ATOM 5325 C CG A ARG A 1 695 ? 5.787 62.377 43.612 0.70 12.41 ? 688 ARG A CG 1 ATOM 5326 C CG B ARG A 1 695 ? 5.582 62.459 43.555 0.30 13.67 ? 688 ARG A CG 1 ATOM 5327 C CD A ARG A 1 695 ? 4.339 62.559 44.045 0.70 14.00 ? 688 ARG A CD 1 ATOM 5328 C CD B ARG A 1 695 ? 4.310 62.080 44.331 0.30 12.98 ? 688 ARG A CD 1 ATOM 5329 N NE A ARG A 1 695 ? 4.161 62.133 45.434 0.70 14.21 ? 688 ARG A NE 1 ATOM 5330 N NE B ARG A 1 695 ? 3.275 61.345 43.576 0.30 12.07 ? 688 ARG A NE 1 ATOM 5331 C CZ A ARG A 1 695 ? 3.117 62.422 46.210 0.70 14.66 ? 688 ARG A CZ 1 ATOM 5332 C CZ B ARG A 1 695 ? 2.241 60.720 44.165 0.30 9.46 ? 688 ARG A CZ 1 ATOM 5333 N NH1 A ARG A 1 695 ? 3.121 61.974 47.473 0.70 12.01 ? 688 ARG A NH1 1 ATOM 5334 N NH1 B ARG A 1 695 ? 1.316 60.050 43.489 0.30 5.87 ? 688 ARG A NH1 1 ATOM 5335 N NH2 A ARG A 1 695 ? 2.072 63.160 45.740 0.70 15.97 ? 688 ARG A NH2 1 ATOM 5336 N NH2 B ARG A 1 695 ? 2.156 60.733 45.475 0.30 11.50 ? 688 ARG A NH2 1 ATOM 5337 N N . HIS A 1 696 ? 10.092 63.504 45.106 1.00 13.83 ? 689 HIS A N 1 ATOM 5338 C CA . HIS A 1 696 ? 11.071 64.134 45.997 1.00 13.35 ? 689 HIS A CA 1 ATOM 5339 C C . HIS A 1 696 ? 11.922 65.072 45.164 1.00 13.70 ? 689 HIS A C 1 ATOM 5340 O O . HIS A 1 696 ? 12.478 64.687 44.134 1.00 14.51 ? 689 HIS A O 1 ATOM 5341 C CB . HIS A 1 696 ? 11.913 63.047 46.668 1.00 14.04 ? 689 HIS A CB 1 ATOM 5342 C CG . HIS A 1 696 ? 12.599 63.485 47.938 1.00 14.39 ? 689 HIS A CG 1 ATOM 5343 N ND1 . HIS A 1 696 ? 13.561 64.462 47.971 1.00 13.94 ? 689 HIS A ND1 1 ATOM 5344 C CD2 . HIS A 1 696 ? 12.452 63.033 49.238 1.00 15.22 ? 689 HIS A CD2 1 ATOM 5345 C CE1 . HIS A 1 696 ? 14.010 64.598 49.244 1.00 14.10 ? 689 HIS A CE1 1 ATOM 5346 N NE2 . HIS A 1 696 ? 13.322 63.740 50.022 1.00 15.08 ? 689 HIS A NE2 1 ATOM 5347 N N . VAL A 1 697 ? 11.994 66.329 45.578 1.00 14.01 ? 690 VAL A N 1 ATOM 5348 C CA . VAL A 1 697 ? 12.672 67.365 44.778 1.00 13.05 ? 690 VAL A CA 1 ATOM 5349 C C . VAL A 1 697 ? 14.198 67.322 44.980 1.00 15.05 ? 690 VAL A C 1 ATOM 5350 O O . VAL A 1 697 ? 14.960 67.792 44.125 1.00 15.03 ? 690 VAL A O 1 ATOM 5351 C CB . VAL A 1 697 ? 12.074 68.761 45.084 1.00 12.78 ? 690 VAL A CB 1 ATOM 5352 C CG1 . VAL A 1 697 ? 12.894 69.876 44.402 1.00 15.86 ? 690 VAL A CG1 1 ATOM 5353 C CG2 . VAL A 1 697 ? 10.621 68.820 44.627 1.00 15.55 ? 690 VAL A CG2 1 ATOM 5354 N N . ILE A 1 698 ? 14.653 66.764 46.102 1.00 14.62 ? 691 ILE A N 1 ATOM 5355 C CA . ILE A 1 698 ? 16.106 66.723 46.357 1.00 14.65 ? 691 ILE A CA 1 ATOM 5356 C C . ILE A 1 698 ? 16.739 65.480 45.733 1.00 14.56 ? 691 ILE A C 1 ATOM 5357 O O . ILE A 1 698 ? 17.847 65.550 45.226 1.00 15.18 ? 691 ILE A O 1 ATOM 5358 C CB . ILE A 1 698 ? 16.442 66.751 47.879 1.00 14.43 ? 691 ILE A CB 1 ATOM 5359 C CG1 . ILE A 1 698 ? 15.681 67.885 48.604 1.00 14.78 ? 691 ILE A CG1 1 ATOM 5360 C CG2 . ILE A 1 698 ? 17.951 66.940 48.115 1.00 16.84 ? 691 ILE A CG2 1 ATOM 5361 C CD1 . ILE A 1 698 ? 15.835 69.262 47.977 1.00 16.14 ? 691 ILE A CD1 1 ATOM 5362 N N . TYR A 1 699 ? 16.044 64.338 45.807 1.00 15.74 ? 692 TYR A N 1 ATOM 5363 C CA . TYR A 1 699 ? 16.590 63.049 45.372 1.00 14.81 ? 692 TYR A CA 1 ATOM 5364 C C . TYR A 1 699 ? 15.645 62.332 44.422 1.00 16.79 ? 692 TYR A C 1 ATOM 5365 O O . TYR A 1 699 ? 14.468 62.151 44.756 1.00 18.86 ? 692 TYR A O 1 ATOM 5366 C CB . TYR A 1 699 ? 16.745 62.135 46.597 1.00 15.25 ? 692 TYR A CB 1 ATOM 5367 C CG . TYR A 1 699 ? 17.780 62.579 47.601 1.00 15.85 ? 692 TYR A CG 1 ATOM 5368 C CD1 . TYR A 1 699 ? 19.147 62.604 47.261 1.00 18.64 ? 692 TYR A CD1 1 ATOM 5369 C CD2 . TYR A 1 699 ? 17.402 62.906 48.909 1.00 16.69 ? 692 TYR A CD2 1 ATOM 5370 C CE1 . TYR A 1 699 ? 20.106 62.971 48.188 1.00 17.95 ? 692 TYR A CE1 1 ATOM 5371 C CE2 . TYR A 1 699 ? 18.349 63.277 49.858 1.00 16.36 ? 692 TYR A CE2 1 ATOM 5372 C CZ . TYR A 1 699 ? 19.703 63.298 49.489 1.00 19.09 ? 692 TYR A CZ 1 ATOM 5373 O OH . TYR A 1 699 ? 20.677 63.635 50.390 1.00 20.28 ? 692 TYR A OH 1 ATOM 5374 N N . ALA A 1 700 ? 16.157 61.860 43.284 1.00 14.91 ? 693 ALA A N 1 ATOM 5375 C CA . ALA A 1 700 ? 15.409 60.886 42.463 1.00 14.16 ? 693 ALA A CA 1 ATOM 5376 C C . ALA A 1 700 ? 16.405 59.873 41.940 1.00 15.76 ? 693 ALA A C 1 ATOM 5377 O O . ALA A 1 700 ? 17.617 60.147 41.916 1.00 16.39 ? 693 ALA A O 1 ATOM 5378 C CB . ALA A 1 700 ? 14.700 61.567 41.298 1.00 15.12 ? 693 ALA A CB 1 ATOM 5379 N N . PRO A 1 701 ? 15.916 58.693 41.531 1.00 14.99 ? 694 PRO A N 1 ATOM 5380 C CA . PRO A 1 701 ? 16.805 57.762 40.822 1.00 15.17 ? 694 PRO A CA 1 ATOM 5381 C C . PRO A 1 701 ? 17.311 58.449 39.543 1.00 15.75 ? 694 PRO A C 1 ATOM 5382 O O . PRO A 1 701 ? 16.538 59.172 38.895 1.00 16.55 ? 694 PRO A O 1 ATOM 5383 C CB . PRO A 1 701 ? 15.870 56.589 40.481 1.00 15.90 ? 694 PRO A CB 1 ATOM 5384 C CG . PRO A 1 701 ? 14.799 56.682 41.540 1.00 15.28 ? 694 PRO A CG 1 ATOM 5385 C CD . PRO A 1 701 ? 14.544 58.163 41.633 1.00 14.94 ? 694 PRO A CD 1 ATOM 5386 N N . SER A 1 702 ? 18.594 58.282 39.214 1.00 16.02 ? 695 SER A N 1 ATOM 5387 C CA . SER A 1 702 ? 19.153 58.878 38.010 1.00 16.62 ? 695 SER A CA 1 ATOM 5388 C C . SER A 1 702 ? 18.350 58.449 36.793 1.00 16.06 ? 695 SER A C 1 ATOM 5389 O O . SER A 1 702 ? 18.047 57.265 36.630 1.00 18.31 ? 695 SER A O 1 ATOM 5390 C CB . SER A 1 702 ? 20.611 58.458 37.826 1.00 17.05 ? 695 SER A CB 1 ATOM 5391 O OG . SER A 1 702 ? 21.094 58.863 36.551 1.00 18.89 ? 695 SER A OG 1 ATOM 5392 N N . SER A 1 703 ? 18.044 59.397 35.911 1.00 16.63 ? 696 SER A N 1 ATOM 5393 C CA . SER A 1 703 ? 17.348 59.062 34.650 1.00 17.50 ? 696 SER A CA 1 ATOM 5394 C C . SER A 1 703 ? 18.191 58.176 33.719 1.00 16.39 ? 696 SER A C 1 ATOM 5395 O O . SER A 1 703 ? 17.664 57.623 32.744 1.00 19.29 ? 696 SER A O 1 ATOM 5396 C CB . SER A 1 703 ? 16.936 60.340 33.905 1.00 17.25 ? 696 SER A CB 1 ATOM 5397 O OG A SER A 1 703 ? 15.980 61.052 34.654 0.50 12.38 ? 696 SER A OG 1 ATOM 5398 O OG B SER A 1 703 ? 18.044 61.118 33.532 0.50 25.98 ? 696 SER A OG 1 ATOM 5399 N N . HIS A 1 704 ? 19.482 58.049 34.024 1.00 16.66 ? 697 HIS A N 1 ATOM 5400 C CA . HIS A 1 704 ? 20.419 57.208 33.235 1.00 17.28 ? 697 HIS A CA 1 ATOM 5401 C C . HIS A 1 704 ? 20.766 55.906 33.919 1.00 18.59 ? 697 HIS A C 1 ATOM 5402 O O . HIS A 1 704 ? 21.407 55.017 33.325 1.00 21.19 ? 697 HIS A O 1 ATOM 5403 C CB . HIS A 1 704 ? 21.680 58.020 32.931 1.00 19.95 ? 697 HIS A CB 1 ATOM 5404 C CG . HIS A 1 704 ? 21.363 59.313 32.235 1.00 20.26 ? 697 HIS A CG 1 ATOM 5405 N ND1 . HIS A 1 704 ? 21.145 59.368 30.915 1.00 22.16 ? 697 HIS A ND1 1 ATOM 5406 C CD2 . HIS A 1 704 ? 21.094 60.587 32.734 1.00 21.78 ? 697 HIS A CD2 1 ATOM 5407 C CE1 . HIS A 1 704 ? 20.795 60.617 30.564 1.00 23.16 ? 697 HIS A CE1 1 ATOM 5408 N NE2 . HIS A 1 704 ? 20.769 61.368 31.676 1.00 21.90 ? 697 HIS A NE2 1 ATOM 5409 N N . ASN A 1 705 ? 20.334 55.759 35.169 1.00 17.10 ? 698 ASN A N 1 ATOM 5410 C CA . ASN A 1 705 ? 20.719 54.580 35.957 1.00 18.28 ? 698 ASN A CA 1 ATOM 5411 C C . ASN A 1 705 ? 19.873 54.553 37.207 1.00 16.79 ? 698 ASN A C 1 ATOM 5412 O O . ASN A 1 705 ? 20.208 55.198 38.206 1.00 16.22 ? 698 ASN A O 1 ATOM 5413 C CB . ASN A 1 705 ? 22.201 54.639 36.357 1.00 19.72 ? 698 ASN A CB 1 ATOM 5414 C CG . ASN A 1 705 ? 22.599 53.508 37.295 1.00 18.64 ? 698 ASN A CG 1 ATOM 5415 O OD1 . ASN A 1 705 ? 21.866 52.527 37.426 1.00 19.37 ? 698 ASN A OD1 1 ATOM 5416 N ND2 . ASN A 1 705 ? 23.750 53.642 37.965 1.00 19.75 ? 698 ASN A ND2 1 ATOM 5417 N N . LYS A 1 706 ? 18.788 53.780 37.161 1.00 17.00 ? 699 LYS A N 1 ATOM 5418 C CA . LYS A 1 706 ? 17.851 53.670 38.289 1.00 17.17 ? 699 LYS A CA 1 ATOM 5419 C C . LYS A 1 706 ? 18.540 53.378 39.629 1.00 17.17 ? 699 LYS A C 1 ATOM 5420 O O . LYS A 1 706 ? 18.064 53.798 40.686 1.00 16.41 ? 699 LYS A O 1 ATOM 5421 C CB . LYS A 1 706 ? 16.863 52.545 37.987 1.00 18.09 ? 699 LYS A CB 1 ATOM 5422 C CG . LYS A 1 706 ? 15.706 52.455 38.962 1.00 18.90 ? 699 LYS A CG 1 ATOM 5423 C CD . LYS A 1 706 ? 14.703 51.411 38.489 1.00 17.74 ? 699 LYS A CD 1 ATOM 5424 C CE . LYS A 1 706 ? 13.428 51.558 39.311 1.00 15.94 ? 699 LYS A CE 1 ATOM 5425 N NZ . LYS A 1 706 ? 12.525 50.404 38.987 1.00 17.30 ? 699 LYS A NZ 1 ATOM 5426 N N . TYR A 1 707 ? 19.648 52.639 39.605 1.00 17.69 ? 700 TYR A N 1 ATOM 5427 C CA . TYR A 1 707 ? 20.323 52.323 40.860 1.00 17.90 ? 700 TYR A CA 1 ATOM 5428 C C . TYR A 1 707 ? 20.916 53.511 41.590 1.00 18.68 ? 700 TYR A C 1 ATOM 5429 O O . TYR A 1 707 ? 21.024 53.458 42.799 1.00 19.40 ? 700 TYR A O 1 ATOM 5430 C CB . TYR A 1 707 ? 21.452 51.336 40.645 1.00 17.93 ? 700 TYR A CB 1 ATOM 5431 C CG . TYR A 1 707 ? 21.043 49.949 40.212 1.00 15.92 ? 700 TYR A CG 1 ATOM 5432 C CD1 . TYR A 1 707 ? 19.906 49.314 40.741 1.00 17.65 ? 700 TYR A CD1 1 ATOM 5433 C CD2 . TYR A 1 707 ? 21.844 49.225 39.300 1.00 18.64 ? 700 TYR A CD2 1 ATOM 5434 C CE1 . TYR A 1 707 ? 19.563 48.015 40.353 1.00 17.29 ? 700 TYR A CE1 1 ATOM 5435 C CE2 . TYR A 1 707 ? 21.501 47.917 38.904 1.00 17.51 ? 700 TYR A CE2 1 ATOM 5436 C CZ . TYR A 1 707 ? 20.366 47.322 39.436 1.00 16.60 ? 700 TYR A CZ 1 ATOM 5437 O OH . TYR A 1 707 ? 20.042 46.034 39.047 1.00 18.34 ? 700 TYR A OH 1 ATOM 5438 N N . ALA A 1 708 ? 21.362 54.530 40.847 1.00 18.25 ? 701 ALA A N 1 ATOM 5439 C CA . ALA A 1 708 ? 22.107 55.645 41.422 1.00 18.13 ? 701 ALA A CA 1 ATOM 5440 C C . ALA A 1 708 ? 21.156 56.763 41.840 1.00 18.62 ? 701 ALA A C 1 ATOM 5441 O O . ALA A 1 708 ? 20.188 57.038 41.145 1.00 19.33 ? 701 ALA A O 1 ATOM 5442 C CB . ALA A 1 708 ? 23.081 56.176 40.384 1.00 19.85 ? 701 ALA A CB 1 ATOM 5443 N N . GLY A 1 709 ? 21.424 57.431 42.959 1.00 18.10 ? 702 GLY A N 1 ATOM 5444 C CA . GLY A 1 709 ? 20.624 58.625 43.254 1.00 17.92 ? 702 GLY A CA 1 ATOM 5445 C C . GLY A 1 709 ? 21.200 59.835 42.554 1.00 17.41 ? 702 GLY A C 1 ATOM 5446 O O . GLY A 1 709 ? 22.420 59.921 42.350 1.00 19.98 ? 702 GLY A O 1 ATOM 5447 N N . GLU A 1 710 ? 20.317 60.748 42.151 1.00 16.06 ? 703 GLU A N 1 ATOM 5448 C CA . GLU A 1 710 ? 20.712 62.054 41.634 1.00 15.99 ? 703 GLU A CA 1 ATOM 5449 C C . GLU A 1 710 ? 20.163 63.130 42.581 1.00 16.05 ? 703 GLU A C 1 ATOM 5450 O O . GLU A 1 710 ? 19.039 63.018 43.060 1.00 16.70 ? 703 GLU A O 1 ATOM 5451 C CB . GLU A 1 710 ? 20.197 62.258 40.189 1.00 16.92 ? 703 GLU A CB 1 ATOM 5452 C CG . GLU A 1 710 ? 20.817 63.488 39.519 1.00 17.25 ? 703 GLU A CG 1 ATOM 5453 C CD . GLU A 1 710 ? 22.356 63.451 39.588 1.00 19.22 ? 703 GLU A CD 1 ATOM 5454 O OE1 . GLU A 1 710 ? 22.961 62.681 38.810 1.00 20.00 ? 703 GLU A OE1 1 ATOM 5455 O OE2 . GLU A 1 710 ? 22.964 64.170 40.443 1.00 21.02 ? 703 GLU A OE2 1 ATOM 5456 N N . SER A 1 711 ? 20.971 64.151 42.865 1.00 15.97 ? 704 SER A N 1 ATOM 5457 C CA . SER A 1 711 ? 20.516 65.285 43.676 1.00 15.17 ? 704 SER A CA 1 ATOM 5458 C C . SER A 1 711 ? 20.031 66.407 42.781 1.00 15.31 ? 704 SER A C 1 ATOM 5459 O O . SER A 1 711 ? 20.522 66.554 41.646 1.00 16.33 ? 704 SER A O 1 ATOM 5460 C CB . SER A 1 711 ? 21.640 65.773 44.619 1.00 15.77 ? 704 SER A CB 1 ATOM 5461 O OG . SER A 1 711 ? 22.848 66.096 43.898 1.00 18.67 ? 704 SER A OG 1 ATOM 5462 N N . PHE A 1 712 ? 19.077 67.203 43.288 1.00 15.21 ? 705 PHE A N 1 ATOM 5463 C CA . PHE A 1 712 ? 18.354 68.201 42.454 1.00 15.47 ? 705 PHE A CA 1 ATOM 5464 C C . PHE A 1 712 ? 18.078 67.647 41.039 1.00 15.43 ? 705 PHE A C 1 ATOM 5465 O O . PHE A 1 712 ? 18.472 68.262 40.036 1.00 14.18 ? 705 PHE A O 1 ATOM 5466 C CB . PHE A 1 712 ? 19.109 69.549 42.419 1.00 14.73 ? 705 PHE A CB 1 ATOM 5467 C CG . PHE A 1 712 ? 19.052 70.295 43.742 1.00 13.69 ? 705 PHE A CG 1 ATOM 5468 C CD1 . PHE A 1 712 ? 17.809 70.604 44.337 1.00 15.52 ? 705 PHE A CD1 1 ATOM 5469 C CD2 . PHE A 1 712 ? 20.223 70.660 44.411 1.00 14.39 ? 705 PHE A CD2 1 ATOM 5470 C CE1 . PHE A 1 712 ? 17.741 71.279 45.560 1.00 16.53 ? 705 PHE A CE1 1 ATOM 5471 C CE2 . PHE A 1 712 ? 20.160 71.343 45.638 1.00 15.83 ? 705 PHE A CE2 1 ATOM 5472 C CZ . PHE A 1 712 ? 18.913 71.646 46.223 1.00 17.04 ? 705 PHE A CZ 1 ATOM 5473 N N . PRO A 1 713 ? 17.376 66.494 40.966 1.00 14.80 ? 706 PRO A N 1 ATOM 5474 C CA . PRO A 1 713 ? 17.227 65.791 39.690 1.00 14.09 ? 706 PRO A CA 1 ATOM 5475 C C . PRO A 1 713 ? 16.512 66.624 38.635 1.00 14.92 ? 706 PRO A C 1 ATOM 5476 O O . PRO A 1 713 ? 16.795 66.472 37.453 1.00 16.47 ? 706 PRO A O 1 ATOM 5477 C CB . PRO A 1 713 ? 16.361 64.552 40.059 1.00 14.40 ? 706 PRO A CB 1 ATOM 5478 C CG . PRO A 1 713 ? 15.672 64.936 41.343 1.00 15.04 ? 706 PRO A CG 1 ATOM 5479 C CD . PRO A 1 713 ? 16.730 65.747 42.063 1.00 14.48 ? 706 PRO A CD 1 ATOM 5480 N N . GLY A 1 714 ? 15.562 67.460 39.049 1.00 14.82 ? 707 GLY A N 1 ATOM 5481 C CA . GLY A 1 714 ? 14.840 68.296 38.080 1.00 16.64 ? 707 GLY A CA 1 ATOM 5482 C C . GLY A 1 714 ? 15.796 69.227 37.348 1.00 15.94 ? 707 GLY A C 1 ATOM 5483 O O . GLY A 1 714 ? 15.756 69.347 36.103 1.00 16.06 ? 707 GLY A O 1 ATOM 5484 N N . ILE A 1 715 ? 16.677 69.888 38.105 1.00 14.98 ? 708 ILE A N 1 ATOM 5485 C CA . ILE A 1 715 ? 17.661 70.787 37.472 1.00 14.96 ? 708 ILE A CA 1 ATOM 5486 C C . ILE A 1 715 ? 18.699 69.962 36.712 1.00 15.97 ? 708 ILE A C 1 ATOM 5487 O O . ILE A 1 715 ? 19.112 70.336 35.603 1.00 17.21 ? 708 ILE A O 1 ATOM 5488 C CB . ILE A 1 715 ? 18.400 71.674 38.507 1.00 14.24 ? 708 ILE A CB 1 ATOM 5489 C CG1 . ILE A 1 715 ? 17.397 72.344 39.488 1.00 16.65 ? 708 ILE A CG1 1 ATOM 5490 C CG2 . ILE A 1 715 ? 19.250 72.721 37.773 1.00 16.99 ? 708 ILE A CG2 1 ATOM 5491 C CD1 . ILE A 1 715 ? 18.102 73.101 40.625 1.00 16.34 ? 708 ILE A CD1 1 ATOM 5492 N N . TYR A 1 716 ? 19.137 68.847 37.308 1.00 16.15 ? 709 TYR A N 1 ATOM 5493 C CA . TYR A 1 716 ? 20.145 68.012 36.666 1.00 15.99 ? 709 TYR A CA 1 ATOM 5494 C C . TYR A 1 716 ? 19.682 67.588 35.267 1.00 16.66 ? 709 TYR A C 1 ATOM 5495 O O . TYR A 1 716 ? 20.416 67.751 34.277 1.00 16.90 ? 709 TYR A O 1 ATOM 5496 C CB . TYR A 1 716 ? 20.511 66.783 37.516 1.00 16.90 ? 709 TYR A CB 1 ATOM 5497 C CG . TYR A 1 716 ? 21.599 65.967 36.842 1.00 15.92 ? 709 TYR A CG 1 ATOM 5498 C CD1 . TYR A 1 716 ? 22.947 66.154 37.170 1.00 17.47 ? 709 TYR A CD1 1 ATOM 5499 C CD2 . TYR A 1 716 ? 21.275 65.035 35.826 1.00 16.45 ? 709 TYR A CD2 1 ATOM 5500 C CE1 . TYR A 1 716 ? 23.962 65.417 36.534 1.00 17.99 ? 709 TYR A CE1 1 ATOM 5501 C CE2 . TYR A 1 716 ? 22.270 64.305 35.180 1.00 18.86 ? 709 TYR A CE2 1 ATOM 5502 C CZ . TYR A 1 716 ? 23.615 64.500 35.544 1.00 19.66 ? 709 TYR A CZ 1 ATOM 5503 O OH . TYR A 1 716 ? 24.620 63.794 34.926 1.00 20.92 ? 709 TYR A OH 1 ATOM 5504 N N . ASP A 1 717 ? 18.471 67.042 35.186 1.00 16.38 ? 710 ASP A N 1 ATOM 5505 C CA . ASP A 1 717 ? 17.955 66.564 33.904 1.00 15.99 ? 710 ASP A CA 1 ATOM 5506 C C . ASP A 1 717 ? 17.746 67.726 32.930 1.00 16.75 ? 710 ASP A C 1 ATOM 5507 O O . ASP A 1 717 ? 17.981 67.577 31.720 1.00 17.57 ? 710 ASP A O 1 ATOM 5508 C CB . ASP A 1 717 ? 16.672 65.742 34.101 1.00 17.04 ? 710 ASP A CB 1 ATOM 5509 C CG . ASP A 1 717 ? 16.954 64.336 34.614 1.00 17.30 ? 710 ASP A CG 1 ATOM 5510 O OD1 . ASP A 1 717 ? 18.125 63.878 34.537 1.00 19.17 ? 710 ASP A OD1 1 ATOM 5511 O OD2 . ASP A 1 717 ? 16.001 63.680 35.085 1.00 19.62 ? 710 ASP A OD2 1 ATOM 5512 N N . ALA A 1 718 ? 17.346 68.891 33.432 1.00 16.73 ? 711 ALA A N 1 ATOM 5513 C CA . ALA A 1 718 ? 17.187 70.058 32.547 1.00 16.72 ? 711 ALA A CA 1 ATOM 5514 C C . ALA A 1 718 ? 18.543 70.484 31.938 1.00 18.78 ? 711 ALA A C 1 ATOM 5515 O O . ALA A 1 718 ? 18.613 70.939 30.780 1.00 18.56 ? 711 ALA A O 1 ATOM 5516 C CB . ALA A 1 718 ? 16.543 71.223 33.298 1.00 18.04 ? 711 ALA A CB 1 ATOM 5517 N N . LEU A 1 719 ? 19.624 70.309 32.701 1.00 18.29 ? 712 LEU A N 1 ATOM 5518 C CA . LEU A 1 719 ? 20.979 70.674 32.219 1.00 17.67 ? 712 LEU A CA 1 ATOM 5519 C C . LEU A 1 719 ? 21.677 69.598 31.380 1.00 18.28 ? 712 LEU A C 1 ATOM 5520 O O . LEU A 1 719 ? 22.623 69.888 30.634 1.00 20.41 ? 712 LEU A O 1 ATOM 5521 C CB . LEU A 1 719 ? 21.889 71.014 33.397 1.00 17.22 ? 712 LEU A CB 1 ATOM 5522 C CG . LEU A 1 719 ? 21.634 72.374 34.039 1.00 16.55 ? 712 LEU A CG 1 ATOM 5523 C CD1 . LEU A 1 719 ? 22.370 72.419 35.370 1.00 20.85 ? 712 LEU A CD1 1 ATOM 5524 C CD2 . LEU A 1 719 ? 22.136 73.479 33.111 1.00 18.80 ? 712 LEU A CD2 1 ATOM 5525 N N . PHE A 1 720 ? 21.231 68.358 31.520 1.00 19.13 ? 713 PHE A N 1 ATOM 5526 C CA . PHE A 1 720 ? 21.939 67.249 30.906 1.00 19.11 ? 713 PHE A CA 1 ATOM 5527 C C . PHE A 1 720 ? 21.932 67.348 29.386 1.00 20.88 ? 713 PHE A C 1 ATOM 5528 O O . PHE A 1 720 ? 20.849 67.455 28.770 1.00 21.68 ? 713 PHE A O 1 ATOM 5529 C CB . PHE A 1 720 ? 21.355 65.893 31.335 1.00 20.51 ? 713 PHE A CB 1 ATOM 5530 C CG . PHE A 1 720 ? 22.160 64.728 30.806 1.00 21.37 ? 713 PHE A CG 1 ATOM 5531 C CD1 . PHE A 1 720 ? 23.345 64.339 31.453 1.00 21.93 ? 713 PHE A CD1 1 ATOM 5532 C CD2 . PHE A 1 720 ? 21.794 64.083 29.628 1.00 20.86 ? 713 PHE A CD2 1 ATOM 5533 C CE1 . PHE A 1 720 ? 24.118 63.297 30.953 1.00 23.06 ? 713 PHE A CE1 1 ATOM 5534 C CE2 . PHE A 1 720 ? 22.586 63.051 29.109 1.00 22.08 ? 713 PHE A CE2 1 ATOM 5535 C CZ . PHE A 1 720 ? 23.737 62.654 29.777 1.00 21.56 ? 713 PHE A CZ 1 ATOM 5536 N N . ASP A 1 721 ? 23.135 67.309 28.800 1.00 22.03 ? 714 ASP A N 1 ATOM 5537 C CA . ASP A 1 721 ? 23.325 67.346 27.339 1.00 21.61 ? 714 ASP A CA 1 ATOM 5538 C C . ASP A 1 721 ? 22.652 68.581 26.732 1.00 22.62 ? 714 ASP A C 1 ATOM 5539 O O . ASP A 1 721 ? 22.203 68.548 25.587 1.00 24.53 ? 714 ASP A O 1 ATOM 5540 C CB . ASP A 1 721 ? 22.758 66.049 26.709 1.00 21.63 ? 714 ASP A CB 1 ATOM 5541 C CG . ASP A 1 721 ? 23.167 65.868 25.245 1.00 25.25 ? 714 ASP A CG 1 ATOM 5542 O OD1 . ASP A 1 721 ? 24.336 66.156 24.901 1.00 26.70 ? 714 ASP A OD1 1 ATOM 5543 O OD2 . ASP A 1 721 ? 22.323 65.422 24.431 1.00 25.61 ? 714 ASP A OD2 1 ATOM 5544 N N . ILE A 1 722 ? 22.599 69.678 27.489 1.00 22.90 ? 715 ILE A N 1 ATOM 5545 C CA . ILE A 1 722 ? 21.813 70.845 27.062 1.00 22.52 ? 715 ILE A CA 1 ATOM 5546 C C . ILE A 1 722 ? 22.371 71.475 25.784 1.00 24.83 ? 715 ILE A C 1 ATOM 5547 O O . ILE A 1 722 ? 21.599 72.041 24.985 1.00 25.35 ? 715 ILE A O 1 ATOM 5548 C CB . ILE A 1 722 ? 21.662 71.897 28.190 1.00 21.71 ? 715 ILE A CB 1 ATOM 5549 C CG1 . ILE A 1 722 ? 20.655 72.987 27.800 1.00 19.44 ? 715 ILE A CG1 1 ATOM 5550 C CG2 . ILE A 1 722 ? 23.013 72.508 28.551 1.00 23.09 ? 715 ILE A CG2 1 ATOM 5551 C CD1 . ILE A 1 722 ? 20.075 73.726 28.995 1.00 21.39 ? 715 ILE A CD1 1 ATOM 5552 N N . GLU A 1 723 ? 23.692 71.343 25.580 1.00 26.44 ? 716 GLU A N 1 ATOM 5553 C CA . GLU A 1 723 ? 24.360 71.929 24.423 1.00 29.10 ? 716 GLU A CA 1 ATOM 5554 C C . GLU A 1 723 ? 23.900 71.273 23.119 1.00 32.19 ? 716 GLU A C 1 ATOM 5555 O O . GLU A 1 723 ? 24.146 71.804 22.037 1.00 34.06 ? 716 GLU A O 1 ATOM 5556 C CB . GLU A 1 723 ? 25.895 71.876 24.574 1.00 32.18 ? 716 GLU A CB 1 ATOM 5557 C CG . GLU A 1 723 ? 26.515 70.488 24.453 1.00 32.83 ? 716 GLU A CG 1 ATOM 5558 C CD . GLU A 1 723 ? 26.542 69.683 25.749 1.00 34.76 ? 716 GLU A CD 1 ATOM 5559 O OE1 . GLU A 1 723 ? 25.794 69.975 26.722 1.00 29.69 ? 716 GLU A OE1 1 ATOM 5560 O OE2 . GLU A 1 723 ? 27.335 68.720 25.782 1.00 38.72 ? 716 GLU A OE2 1 ATOM 5561 N N . SER A 1 724 ? 23.211 70.138 23.229 1.00 30.53 ? 717 SER A N 1 ATOM 5562 C CA . SER A 1 724 ? 22.686 69.429 22.058 1.00 34.32 ? 717 SER A CA 1 ATOM 5563 C C . SER A 1 724 ? 21.249 69.798 21.702 1.00 31.12 ? 717 SER A C 1 ATOM 5564 O O . SER A 1 724 ? 20.749 69.371 20.661 1.00 36.93 ? 717 SER A O 1 ATOM 5565 C CB . SER A 1 724 ? 22.806 67.911 22.251 1.00 33.69 ? 717 SER A CB 1 ATOM 5566 O OG . SER A 1 724 ? 24.176 67.547 22.377 1.00 33.00 ? 717 SER A OG 1 ATOM 5567 N N . LYS A 1 725 ? 20.592 70.596 22.545 1.00 33.20 ? 718 LYS A N 1 ATOM 5568 C CA . LYS A 1 725 ? 19.180 70.931 22.344 1.00 31.18 ? 718 LYS A CA 1 ATOM 5569 C C . LYS A 1 725 ? 19.011 71.954 21.222 1.00 36.23 ? 718 LYS A C 1 ATOM 5570 O O . LYS A 1 725 ? 19.786 72.915 21.108 1.00 35.98 ? 718 LYS A O 1 ATOM 5571 C CB . LYS A 1 725 ? 18.521 71.436 23.647 1.00 27.50 ? 718 LYS A CB 1 ATOM 5572 C CG . LYS A 1 725 ? 18.484 70.439 24.802 1.00 31.97 ? 718 LYS A CG 1 ATOM 5573 C CD . LYS A 1 725 ? 17.747 69.159 24.449 1.00 37.24 ? 718 LYS A CD 1 ATOM 5574 C CE . LYS A 1 725 ? 17.879 68.120 25.559 1.00 39.62 ? 718 LYS A CE 1 ATOM 5575 N NZ . LYS A 1 725 ? 17.154 68.521 26.801 1.00 39.73 ? 718 LYS A NZ 1 ATOM 5576 N N . VAL A 1 726 ? 17.992 71.741 20.396 1.00 36.92 ? 719 VAL A N 1 ATOM 5577 C CA . VAL A 1 726 ? 17.799 72.536 19.178 1.00 38.40 ? 719 VAL A CA 1 ATOM 5578 C C . VAL A 1 726 ? 17.358 73.971 19.492 1.00 37.06 ? 719 VAL A C 1 ATOM 5579 O O . VAL A 1 726 ? 17.717 74.918 18.770 1.00 36.47 ? 719 VAL A O 1 ATOM 5580 C CB . VAL A 1 726 ? 16.823 71.816 18.215 1.00 43.06 ? 719 VAL A CB 1 ATOM 5581 C CG1 . VAL A 1 726 ? 16.349 72.735 17.100 1.00 46.60 ? 719 VAL A CG1 1 ATOM 5582 C CG2 . VAL A 1 726 ? 17.502 70.586 17.623 1.00 46.86 ? 719 VAL A CG2 1 ATOM 5583 N N . ASP A 1 727 ? 16.604 74.121 20.578 1.00 36.50 ? 720 ASP A N 1 ATOM 5584 C CA . ASP A 1 727 ? 16.061 75.412 21.010 1.00 35.75 ? 720 ASP A CA 1 ATOM 5585 C C . ASP A 1 727 ? 16.659 75.791 22.378 1.00 32.60 ? 720 ASP A C 1 ATOM 5586 O O . ASP A 1 727 ? 16.076 75.466 23.421 1.00 29.24 ? 720 ASP A O 1 ATOM 5587 C CB . ASP A 1 727 ? 14.532 75.309 21.088 1.00 33.01 ? 720 ASP A CB 1 ATOM 5588 C CG . ASP A 1 727 ? 13.851 76.635 21.407 1.00 36.05 ? 720 ASP A CG 1 ATOM 5589 O OD1 . ASP A 1 727 ? 14.524 77.618 21.788 1.00 34.20 ? 720 ASP A OD1 1 ATOM 5590 O OD2 . ASP A 1 727 ? 12.610 76.688 21.280 1.00 44.89 ? 720 ASP A OD2 1 ATOM 5591 N N . PRO A 1 728 ? 17.830 76.461 22.381 1.00 31.22 ? 721 PRO A N 1 ATOM 5592 C CA . PRO A 1 728 ? 18.473 76.791 23.658 1.00 30.50 ? 721 PRO A CA 1 ATOM 5593 C C . PRO A 1 728 ? 17.626 77.692 24.565 1.00 27.31 ? 721 PRO A C 1 ATOM 5594 O O . PRO A 1 728 ? 17.665 77.532 25.789 1.00 27.71 ? 721 PRO A O 1 ATOM 5595 C CB . PRO A 1 728 ? 19.770 77.496 23.238 1.00 31.48 ? 721 PRO A CB 1 ATOM 5596 C CG . PRO A 1 728 ? 19.562 77.908 21.817 1.00 35.26 ? 721 PRO A CG 1 ATOM 5597 C CD . PRO A 1 728 ? 18.670 76.853 21.233 1.00 34.41 ? 721 PRO A CD 1 ATOM 5598 N N . SER A 1 729 ? 16.861 78.616 23.982 1.00 27.70 ? 722 SER A N 1 ATOM 5599 C CA . SER A 1 729 ? 15.971 79.470 24.783 1.00 27.97 ? 722 SER A CA 1 ATOM 5600 C C . SER A 1 729 ? 14.992 78.643 25.619 1.00 26.84 ? 722 SER A C 1 ATOM 5601 O O . SER A 1 729 ? 14.857 78.861 26.830 1.00 25.46 ? 722 SER A O 1 ATOM 5602 C CB . SER A 1 729 ? 15.202 80.449 23.897 1.00 31.08 ? 722 SER A CB 1 ATOM 5603 O OG . SER A 1 729 ? 14.402 81.289 24.707 1.00 35.38 ? 722 SER A OG 1 ATOM 5604 N N . LYS A 1 730 ? 14.320 77.695 24.965 1.00 25.10 ? 723 LYS A N 1 ATOM 5605 C CA . LYS A 1 730 ? 13.413 76.780 25.633 1.00 25.78 ? 723 LYS A CA 1 ATOM 5606 C C . LYS A 1 730 ? 14.142 75.926 26.672 1.00 24.63 ? 723 LYS A C 1 ATOM 5607 O O . LYS A 1 730 ? 13.644 75.736 27.784 1.00 22.49 ? 723 LYS A O 1 ATOM 5608 C CB . LYS A 1 730 ? 12.702 75.890 24.598 1.00 28.66 ? 723 LYS A CB 1 ATOM 5609 C CG . LYS A 1 730 ? 11.584 75.010 25.154 1.00 34.56 ? 723 LYS A CG 1 ATOM 5610 C CD . LYS A 1 730 ? 10.936 74.175 24.045 1.00 42.16 ? 723 LYS A CD 1 ATOM 5611 C CE . LYS A 1 730 ? 9.936 73.163 24.598 1.00 44.68 ? 723 LYS A CE 1 ATOM 5612 N NZ . LYS A 1 730 ? 9.402 72.281 23.524 0.50 46.78 ? 723 LYS A NZ 1 ATOM 5613 N N . ALA A 1 731 ? 15.313 75.407 26.308 1.00 22.38 ? 724 ALA A N 1 ATOM 5614 C CA . ALA A 1 731 ? 16.038 74.494 27.195 1.00 21.33 ? 724 ALA A CA 1 ATOM 5615 C C . ALA A 1 731 ? 16.482 75.239 28.466 1.00 20.63 ? 724 ALA A C 1 ATOM 5616 O O . ALA A 1 731 ? 16.311 74.745 29.579 1.00 20.41 ? 724 ALA A O 1 ATOM 5617 C CB . ALA A 1 731 ? 17.250 73.915 26.478 1.00 21.25 ? 724 ALA A CB 1 ATOM 5618 N N . TRP A 1 732 ? 17.057 76.428 28.302 1.00 20.88 ? 725 TRP A N 1 ATOM 5619 C CA . TRP A 1 732 ? 17.488 77.217 29.480 1.00 19.76 ? 725 TRP A CA 1 ATOM 5620 C C . TRP A 1 732 ? 16.328 77.764 30.278 1.00 20.25 ? 725 TRP A C 1 ATOM 5621 O O . TRP A 1 732 ? 16.407 77.923 31.510 1.00 17.99 ? 725 TRP A O 1 ATOM 5622 C CB . TRP A 1 732 ? 18.462 78.311 29.041 1.00 19.03 ? 725 TRP A CB 1 ATOM 5623 C CG . TRP A 1 732 ? 19.805 77.681 28.772 1.00 19.84 ? 725 TRP A CG 1 ATOM 5624 C CD1 . TRP A 1 732 ? 20.363 77.328 27.537 1.00 20.23 ? 725 TRP A CD1 1 ATOM 5625 C CD2 . TRP A 1 732 ? 20.769 77.237 29.773 1.00 20.53 ? 725 TRP A CD2 1 ATOM 5626 N NE1 . TRP A 1 732 ? 21.593 76.731 27.708 1.00 21.97 ? 725 TRP A NE1 1 ATOM 5627 C CE2 . TRP A 1 732 ? 21.897 76.650 29.028 1.00 21.16 ? 725 TRP A CE2 1 ATOM 5628 C CE3 . TRP A 1 732 ? 20.825 77.276 31.176 1.00 20.18 ? 725 TRP A CE3 1 ATOM 5629 C CZ2 . TRP A 1 732 ? 23.023 76.139 29.674 1.00 22.17 ? 725 TRP A CZ2 1 ATOM 5630 C CZ3 . TRP A 1 732 ? 21.972 76.749 31.812 1.00 21.87 ? 725 TRP A CZ3 1 ATOM 5631 C CH2 . TRP A 1 732 ? 23.039 76.196 31.073 1.00 22.23 ? 725 TRP A CH2 1 ATOM 5632 N N . GLY A 1 733 ? 15.221 78.034 29.597 1.00 20.10 ? 726 GLY A N 1 ATOM 5633 C CA . GLY A 1 733 ? 13.978 78.396 30.293 1.00 20.03 ? 726 GLY A CA 1 ATOM 5634 C C . GLY A 1 733 ? 13.550 77.303 31.258 1.00 18.57 ? 726 GLY A C 1 ATOM 5635 O O . GLY A 1 733 ? 13.113 77.589 32.393 1.00 18.40 ? 726 GLY A O 1 ATOM 5636 N N . GLU A 1 734 ? 13.681 76.046 30.821 1.00 18.44 ? 727 GLU A N 1 ATOM 5637 C CA . GLU A 1 734 ? 13.312 74.915 31.656 1.00 18.00 ? 727 GLU A CA 1 ATOM 5638 C C . GLU A 1 734 ? 14.311 74.742 32.817 1.00 17.84 ? 727 GLU A C 1 ATOM 5639 O O . GLU A 1 734 ? 13.918 74.382 33.921 1.00 17.59 ? 727 GLU A O 1 ATOM 5640 C CB . GLU A 1 734 ? 13.149 73.641 30.810 1.00 19.50 ? 727 GLU A CB 1 ATOM 5641 C CG A GLU A 1 734 ? 12.799 72.395 31.621 1.00 20.28 ? 727 GLU A CG 1 ATOM 5642 C CD A GLU A 1 734 ? 11.449 72.445 32.353 1.00 22.12 ? 727 GLU A CD 1 ATOM 5643 O OE1 A GLU A 1 734 ? 10.608 73.358 32.111 1.00 23.72 ? 727 GLU A OE1 1 ATOM 5644 O OE2 A GLU A 1 734 ? 11.227 71.532 33.180 1.00 23.04 ? 727 GLU A OE2 1 ATOM 5645 N N . VAL A 1 735 ? 15.603 74.996 32.572 1.00 16.67 ? 728 VAL A N 1 ATOM 5646 C CA . VAL A 1 735 ? 16.582 75.041 33.686 1.00 16.96 ? 728 VAL A CA 1 ATOM 5647 C C . VAL A 1 735 ? 16.125 76.054 34.746 1.00 16.01 ? 728 VAL A C 1 ATOM 5648 O O . VAL A 1 735 ? 16.078 75.726 35.933 1.00 16.77 ? 728 VAL A O 1 ATOM 5649 C CB . VAL A 1 735 ? 18.018 75.373 33.212 1.00 16.82 ? 728 VAL A CB 1 ATOM 5650 C CG1 . VAL A 1 735 ? 18.933 75.600 34.422 1.00 19.27 ? 728 VAL A CG1 1 ATOM 5651 C CG2 . VAL A 1 735 ? 18.554 74.278 32.270 1.00 18.19 ? 728 VAL A CG2 1 ATOM 5652 N N A LYS A 1 736 ? 15.755 77.261 34.310 0.50 16.39 ? 729 LYS A N 1 ATOM 5653 N N B LYS A 1 736 ? 15.782 77.267 34.316 0.50 16.55 ? 729 LYS A N 1 ATOM 5654 C CA A LYS A 1 736 ? 15.294 78.316 35.239 0.50 16.29 ? 729 LYS A CA 1 ATOM 5655 C CA B LYS A 1 736 ? 15.312 78.289 35.262 0.50 16.61 ? 729 LYS A CA 1 ATOM 5656 C C A LYS A 1 736 ? 13.994 77.949 35.974 0.50 16.75 ? 729 LYS A C 1 ATOM 5657 C C B LYS A 1 736 ? 14.063 77.808 36.016 0.50 16.81 ? 729 LYS A C 1 ATOM 5658 O O A LYS A 1 736 ? 13.805 78.316 37.141 0.50 15.85 ? 729 LYS A O 1 ATOM 5659 O O B LYS A 1 736 ? 13.988 77.930 37.244 0.50 15.79 ? 729 LYS A O 1 ATOM 5660 C CB A LYS A 1 736 ? 15.134 79.645 34.510 0.50 16.13 ? 729 LYS A CB 1 ATOM 5661 C CB B LYS A 1 736 ? 15.059 79.615 34.551 0.50 16.58 ? 729 LYS A CB 1 ATOM 5662 C CG A LYS A 1 736 ? 16.463 80.230 34.056 0.50 15.90 ? 729 LYS A CG 1 ATOM 5663 C CG B LYS A 1 736 ? 16.331 80.212 33.962 0.50 17.60 ? 729 LYS A CG 1 ATOM 5664 C CD A LYS A 1 736 ? 16.296 81.461 33.175 0.50 16.06 ? 729 LYS A CD 1 ATOM 5665 C CD B LYS A 1 736 ? 16.110 81.590 33.353 0.50 19.49 ? 729 LYS A CD 1 ATOM 5666 C CE A LYS A 1 736 ? 15.687 82.649 33.913 0.50 16.82 ? 729 LYS A CE 1 ATOM 5667 C CE B LYS A 1 736 ? 15.420 81.503 31.997 0.50 22.69 ? 729 LYS A CE 1 ATOM 5668 N NZ A LYS A 1 736 ? 15.694 83.883 33.067 0.50 19.41 ? 729 LYS A NZ 1 ATOM 5669 N NZ B LYS A 1 736 ? 15.573 82.750 31.193 0.50 26.46 ? 729 LYS A NZ 1 ATOM 5670 N N . ARG A 1 737 ? 13.104 77.234 35.288 1.00 15.21 ? 730 ARG A N 1 ATOM 5671 C CA . ARG A 1 737 ? 11.909 76.704 35.929 1.00 15.95 ? 730 ARG A CA 1 ATOM 5672 C C . ARG A 1 737 ? 12.268 75.713 37.050 1.00 15.48 ? 730 ARG A C 1 ATOM 5673 O O . ARG A 1 737 ? 11.700 75.775 38.137 1.00 15.56 ? 730 ARG A O 1 ATOM 5674 C CB . ARG A 1 737 ? 10.940 76.058 34.932 1.00 15.75 ? 730 ARG A CB 1 ATOM 5675 C CG . ARG A 1 737 ? 9.585 75.787 35.586 1.00 16.69 ? 730 ARG A CG 1 ATOM 5676 C CD . ARG A 1 737 ? 8.611 75.203 34.579 1.00 20.36 ? 730 ARG A CD 1 ATOM 5677 N NE . ARG A 1 737 ? 8.840 73.786 34.341 1.00 18.98 ? 730 ARG A NE 1 ATOM 5678 C CZ . ARG A 1 737 ? 8.348 72.810 35.105 1.00 22.30 ? 730 ARG A CZ 1 ATOM 5679 N NH1 . ARG A 1 737 ? 7.617 73.105 36.179 1.00 23.18 ? 730 ARG A NH1 1 ATOM 5680 N NH2 . ARG A 1 737 ? 8.584 71.540 34.796 1.00 23.45 ? 730 ARG A NH2 1 ATOM 5681 N N . GLN A 1 738 ? 13.201 74.806 36.772 1.00 15.73 ? 731 GLN A N 1 ATOM 5682 C CA . GLN A 1 738 ? 13.609 73.808 37.760 1.00 14.87 ? 731 GLN A CA 1 ATOM 5683 C C . GLN A 1 738 ? 14.344 74.445 38.935 1.00 15.19 ? 731 GLN A C 1 ATOM 5684 O O . GLN A 1 738 ? 14.217 73.979 40.066 1.00 16.24 ? 731 GLN A O 1 ATOM 5685 C CB . GLN A 1 738 ? 14.435 72.696 37.096 1.00 14.94 ? 731 GLN A CB 1 ATOM 5686 C CG . GLN A 1 738 ? 13.577 71.910 36.092 1.00 13.69 ? 731 GLN A CG 1 ATOM 5687 C CD . GLN A 1 738 ? 12.427 71.174 36.759 1.00 17.17 ? 731 GLN A CD 1 ATOM 5688 O OE1 . GLN A 1 738 ? 12.538 70.740 37.917 1.00 18.33 ? 731 GLN A OE1 1 ATOM 5689 N NE2 . GLN A 1 738 ? 11.327 70.982 36.018 1.00 19.90 ? 731 GLN A NE2 1 ATOM 5690 N N . ILE A 1 739 ? 15.097 75.513 38.673 1.00 16.29 ? 732 ILE A N 1 ATOM 5691 C CA . ILE A 1 739 ? 15.748 76.238 39.787 1.00 15.23 ? 732 ILE A CA 1 ATOM 5692 C C . ILE A 1 739 ? 14.674 76.817 40.713 1.00 15.73 ? 732 ILE A C 1 ATOM 5693 O O . ILE A 1 739 ? 14.772 76.706 41.935 1.00 17.12 ? 732 ILE A O 1 ATOM 5694 C CB . ILE A 1 739 ? 16.683 77.371 39.297 1.00 15.05 ? 732 ILE A CB 1 ATOM 5695 C CG1 . ILE A 1 739 ? 17.877 76.772 38.539 1.00 15.23 ? 732 ILE A CG1 1 ATOM 5696 C CG2 . ILE A 1 739 ? 17.175 78.253 40.467 1.00 16.13 ? 732 ILE A CG2 1 ATOM 5697 C CD1 . ILE A 1 739 ? 18.706 77.798 37.767 1.00 17.77 ? 732 ILE A CD1 1 ATOM 5698 N N . TYR A 1 740 ? 13.674 77.460 40.119 1.00 15.78 ? 733 TYR A N 1 ATOM 5699 C CA . TYR A 1 740 ? 12.539 78.018 40.871 1.00 16.27 ? 733 TYR A CA 1 ATOM 5700 C C . TYR A 1 740 ? 11.852 76.946 41.703 1.00 16.09 ? 733 TYR A C 1 ATOM 5701 O O . TYR A 1 740 ? 11.599 77.153 42.900 1.00 15.51 ? 733 TYR A O 1 ATOM 5702 C CB . TYR A 1 740 ? 11.550 78.639 39.888 1.00 16.78 ? 733 TYR A CB 1 ATOM 5703 C CG . TYR A 1 740 ? 10.078 78.916 40.304 1.00 18.82 ? 733 TYR A CG 1 ATOM 5704 C CD1 . TYR A 1 740 ? 9.751 79.680 41.438 1.00 21.98 ? 733 TYR A CD1 1 ATOM 5705 C CD2 . TYR A 1 740 ? 9.004 78.492 39.459 1.00 18.37 ? 733 TYR A CD2 1 ATOM 5706 C CE1 . TYR A 1 740 ? 8.403 79.987 41.740 1.00 20.10 ? 733 TYR A CE1 1 ATOM 5707 C CE2 . TYR A 1 740 ? 7.689 78.808 39.732 1.00 16.95 ? 733 TYR A CE2 1 ATOM 5708 C CZ . TYR A 1 740 ? 7.381 79.566 40.871 1.00 19.52 ? 733 TYR A CZ 1 ATOM 5709 O OH . TYR A 1 740 ? 6.044 79.906 41.147 1.00 23.74 ? 733 TYR A OH 1 ATOM 5710 N N . VAL A 1 741 ? 11.535 75.811 41.090 1.00 14.52 ? 734 VAL A N 1 ATOM 5711 C CA . VAL A 1 741 ? 10.854 74.729 41.842 1.00 14.41 ? 734 VAL A CA 1 ATOM 5712 C C . VAL A 1 741 ? 11.711 74.252 43.026 1.00 15.03 ? 734 VAL A C 1 ATOM 5713 O O . VAL A 1 741 ? 11.214 74.060 44.147 1.00 15.83 ? 734 VAL A O 1 ATOM 5714 C CB . VAL A 1 741 ? 10.470 73.553 40.904 1.00 13.94 ? 734 VAL A CB 1 ATOM 5715 C CG1 . VAL A 1 741 ? 9.998 72.357 41.720 1.00 16.53 ? 734 VAL A CG1 1 ATOM 5716 C CG2 . VAL A 1 741 ? 9.377 74.023 39.921 1.00 17.01 ? 734 VAL A CG2 1 ATOM 5717 N N . ALA A 1 742 ? 13.004 74.088 42.786 1.00 14.78 ? 735 ALA A N 1 ATOM 5718 C CA . ALA A 1 742 ? 13.926 73.602 43.828 1.00 14.53 ? 735 ALA A CA 1 ATOM 5719 C C . ALA A 1 742 ? 14.080 74.640 44.931 1.00 14.83 ? 735 ALA A C 1 ATOM 5720 O O . ALA A 1 742 ? 14.017 74.286 46.126 1.00 14.91 ? 735 ALA A O 1 ATOM 5721 C CB . ALA A 1 742 ? 15.283 73.228 43.237 1.00 16.13 ? 735 ALA A CB 1 ATOM 5722 N N . ALA A 1 743 ? 14.291 75.910 44.555 1.00 13.76 ? 736 ALA A N 1 ATOM 5723 C CA . ALA A 1 743 ? 14.413 76.984 45.582 1.00 14.35 ? 736 ALA A CA 1 ATOM 5724 C C . ALA A 1 743 ? 13.124 77.073 46.415 1.00 15.16 ? 736 ALA A C 1 ATOM 5725 O O . ALA A 1 743 ? 13.159 77.165 47.639 1.00 15.84 ? 736 ALA A O 1 ATOM 5726 C CB . ALA A 1 743 ? 14.693 78.333 44.929 1.00 15.57 ? 736 ALA A CB 1 ATOM 5727 N N . PHE A 1 744 ? 11.983 77.045 45.735 1.00 15.13 ? 737 PHE A N 1 ATOM 5728 C CA . PHE A 1 744 ? 10.721 77.107 46.455 1.00 14.61 ? 737 PHE A CA 1 ATOM 5729 C C . PHE A 1 744 ? 10.586 75.933 47.420 1.00 15.06 ? 737 PHE A C 1 ATOM 5730 O O . PHE A 1 744 ? 10.200 76.116 48.582 1.00 14.96 ? 737 PHE A O 1 ATOM 5731 C CB . PHE A 1 744 ? 9.524 77.128 45.505 1.00 15.32 ? 737 PHE A CB 1 ATOM 5732 C CG . PHE A 1 744 ? 8.236 76.788 46.198 1.00 16.55 ? 737 PHE A CG 1 ATOM 5733 C CD1 . PHE A 1 744 ? 7.694 77.664 47.165 1.00 16.74 ? 737 PHE A CD1 1 ATOM 5734 C CD2 . PHE A 1 744 ? 7.621 75.558 45.974 1.00 16.10 ? 737 PHE A CD2 1 ATOM 5735 C CE1 . PHE A 1 744 ? 6.525 77.307 47.864 1.00 17.67 ? 737 PHE A CE1 1 ATOM 5736 C CE2 . PHE A 1 744 ? 6.431 75.209 46.646 1.00 16.59 ? 737 PHE A CE2 1 ATOM 5737 C CZ . PHE A 1 744 ? 5.891 76.082 47.585 1.00 16.60 ? 737 PHE A CZ 1 ATOM 5738 N N . THR A 1 745 ? 10.899 74.734 46.947 1.00 14.14 ? 738 THR A N 1 ATOM 5739 C CA . THR A 1 745 ? 10.701 73.540 47.791 1.00 13.92 ? 738 THR A CA 1 ATOM 5740 C C . THR A 1 745 ? 11.613 73.570 49.010 1.00 14.78 ? 738 THR A C 1 ATOM 5741 O O . THR A 1 745 ? 11.171 73.227 50.128 1.00 15.63 ? 738 THR A O 1 ATOM 5742 C CB . THR A 1 745 ? 10.901 72.242 46.995 1.00 13.79 ? 738 THR A CB 1 ATOM 5743 O OG1 . THR A 1 745 ? 10.028 72.271 45.864 1.00 15.71 ? 738 THR A OG1 1 ATOM 5744 C CG2 . THR A 1 745 ? 10.574 71.051 47.863 1.00 14.84 ? 738 THR A CG2 1 ATOM 5745 N N . VAL A 1 746 ? 12.871 73.983 48.818 1.00 14.83 ? 739 VAL A N 1 ATOM 5746 C CA . VAL A 1 746 ? 13.812 74.074 49.954 1.00 14.81 ? 739 VAL A CA 1 ATOM 5747 C C . VAL A 1 746 ? 13.312 75.095 50.975 1.00 13.97 ? 739 VAL A C 1 ATOM 5748 O O . VAL A 1 746 ? 13.316 74.817 52.176 1.00 16.27 ? 739 VAL A O 1 ATOM 5749 C CB . VAL A 1 746 ? 15.264 74.370 49.494 1.00 14.00 ? 739 VAL A CB 1 ATOM 5750 C CG1 . VAL A 1 746 ? 16.226 74.669 50.673 1.00 16.90 ? 739 VAL A CG1 1 ATOM 5751 C CG2 . VAL A 1 746 ? 15.766 73.177 48.678 1.00 15.32 ? 739 VAL A CG2 1 ATOM 5752 N N . GLN A 1 747 ? 12.870 76.260 50.502 1.00 15.48 ? 740 GLN A N 1 ATOM 5753 C CA . GLN A 1 747 ? 12.315 77.284 51.403 1.00 15.03 ? 740 GLN A CA 1 ATOM 5754 C C . GLN A 1 747 ? 11.060 76.767 52.129 1.00 15.21 ? 740 GLN A C 1 ATOM 5755 O O . GLN A 1 747 ? 10.895 76.991 53.328 1.00 14.83 ? 740 GLN A O 1 ATOM 5756 C CB . GLN A 1 747 ? 11.970 78.564 50.641 1.00 15.61 ? 740 GLN A CB 1 ATOM 5757 C CG . GLN A 1 747 ? 11.446 79.690 51.545 1.00 16.86 ? 740 GLN A CG 1 ATOM 5758 C CD . GLN A 1 747 ? 12.493 80.269 52.491 1.00 17.15 ? 740 GLN A CD 1 ATOM 5759 O OE1 . GLN A 1 747 ? 13.701 80.214 52.227 1.00 19.85 ? 740 GLN A OE1 1 ATOM 5760 N NE2 . GLN A 1 747 ? 12.025 80.865 53.595 1.00 19.92 ? 740 GLN A NE2 1 ATOM 5761 N N . ALA A 1 748 ? 10.181 76.086 51.399 1.00 15.12 ? 741 ALA A N 1 ATOM 5762 C CA . ALA A 1 748 ? 8.940 75.577 51.992 1.00 15.27 ? 741 ALA A CA 1 ATOM 5763 C C . ALA A 1 748 ? 9.274 74.542 53.056 1.00 15.23 ? 741 ALA A C 1 ATOM 5764 O O . ALA A 1 748 ? 8.685 74.544 54.147 1.00 15.72 ? 741 ALA A O 1 ATOM 5765 C CB . ALA A 1 748 ? 8.019 74.989 50.916 1.00 14.71 ? 741 ALA A CB 1 ATOM 5766 N N . ALA A 1 749 ? 10.243 73.679 52.771 1.00 15.13 ? 742 ALA A N 1 ATOM 5767 C CA . ALA A 1 749 ? 10.662 72.682 53.760 1.00 14.35 ? 742 ALA A CA 1 ATOM 5768 C C . ALA A 1 749 ? 11.241 73.389 54.988 1.00 15.93 ? 742 ALA A C 1 ATOM 5769 O O . ALA A 1 749 ? 10.943 73.007 56.140 1.00 16.07 ? 742 ALA A O 1 ATOM 5770 C CB . ALA A 1 749 ? 11.699 71.735 53.148 1.00 14.90 ? 742 ALA A CB 1 ATOM 5771 N N . ALA A 1 750 ? 12.083 74.404 54.757 1.00 16.15 ? 743 ALA A N 1 ATOM 5772 C CA . ALA A 1 750 ? 12.655 75.180 55.879 1.00 17.49 ? 743 ALA A CA 1 ATOM 5773 C C . ALA A 1 750 ? 11.535 75.727 56.760 1.00 17.09 ? 743 ALA A C 1 ATOM 5774 O O . ALA A 1 750 ? 11.589 75.658 58.000 1.00 17.36 ? 743 ALA A O 1 ATOM 5775 C CB . ALA A 1 750 ? 13.514 76.342 55.372 1.00 16.80 ? 743 ALA A CB 1 ATOM 5776 N N . GLU A 1 751 ? 10.512 76.273 56.116 1.00 16.99 ? 744 GLU A N 1 ATOM 5777 C CA . GLU A 1 751 ? 9.440 76.932 56.858 1.00 17.49 ? 744 GLU A CA 1 ATOM 5778 C C . GLU A 1 751 ? 8.613 75.989 57.724 1.00 16.59 ? 744 GLU A C 1 ATOM 5779 O O . GLU A 1 751 ? 8.003 76.442 58.690 1.00 17.88 ? 744 GLU A O 1 ATOM 5780 C CB . GLU A 1 751 ? 8.571 77.790 55.934 1.00 17.63 ? 744 GLU A CB 1 ATOM 5781 C CG . GLU A 1 751 ? 9.366 79.009 55.469 1.00 18.55 ? 744 GLU A CG 1 ATOM 5782 C CD . GLU A 1 751 ? 8.615 79.897 54.498 1.00 21.68 ? 744 GLU A CD 1 ATOM 5783 O OE1 . GLU A 1 751 ? 7.489 79.541 54.055 1.00 22.42 ? 744 GLU A OE1 1 ATOM 5784 O OE2 . GLU A 1 751 ? 9.162 80.966 54.172 1.00 22.46 ? 744 GLU A OE2 1 ATOM 5785 N N . THR A 1 752 ? 8.623 74.689 57.411 1.00 17.30 ? 745 THR A N 1 ATOM 5786 C CA . THR A 1 752 ? 7.976 73.696 58.285 1.00 16.39 ? 745 THR A CA 1 ATOM 5787 C C . THR A 1 752 ? 8.681 73.567 59.642 1.00 17.36 ? 745 THR A C 1 ATOM 5788 O O . THR A 1 752 ? 8.086 73.037 60.581 1.00 18.28 ? 745 THR A O 1 ATOM 5789 C CB . THR A 1 752 ? 7.835 72.281 57.660 1.00 15.95 ? 745 THR A CB 1 ATOM 5790 O OG1 . THR A 1 752 ? 9.117 71.606 57.647 1.00 17.56 ? 745 THR A OG1 1 ATOM 5791 C CG2 . THR A 1 752 ? 7.209 72.349 56.244 1.00 16.24 ? 745 THR A CG2 1 ATOM 5792 N N . LEU A 1 753 ? 9.933 74.050 59.732 1.00 17.30 ? 746 LEU A N 1 ATOM 5793 C CA . LEU A 1 753 ? 10.709 74.029 60.976 1.00 17.62 ? 746 LEU A CA 1 ATOM 5794 C C . LEU A 1 753 ? 10.645 75.344 61.752 1.00 18.81 ? 746 LEU A C 1 ATOM 5795 O O . LEU A 1 753 ? 11.119 75.422 62.886 1.00 20.34 ? 746 LEU A O 1 ATOM 5796 C CB . LEU A 1 753 ? 12.171 73.688 60.684 1.00 17.70 ? 746 LEU A CB 1 ATOM 5797 C CG . LEU A 1 753 ? 12.422 72.353 59.997 1.00 17.35 ? 746 LEU A CG 1 ATOM 5798 C CD1 . LEU A 1 753 ? 13.916 72.185 59.743 1.00 19.60 ? 746 LEU A CD1 1 ATOM 5799 C CD2 . LEU A 1 753 ? 11.885 71.195 60.844 1.00 19.21 ? 746 LEU A CD2 1 ATOM 5800 N N . SER A 1 754 ? 10.097 76.394 61.134 1.00 19.19 ? 747 SER A N 1 ATOM 5801 C CA . SER A 1 754 ? 9.870 77.660 61.856 1.00 19.99 ? 747 SER A CA 1 ATOM 5802 C C . SER A 1 754 ? 8.883 77.433 63.012 1.00 20.00 ? 747 SER A C 1 ATOM 5803 O O . SER A 1 754 ? 8.163 76.425 63.047 1.00 20.48 ? 747 SER A O 1 ATOM 5804 C CB . SER A 1 754 ? 9.304 78.708 60.906 1.00 20.30 ? 747 SER A CB 1 ATOM 5805 O OG . SER A 1 754 ? 10.198 78.956 59.837 1.00 22.85 ? 747 SER A OG 1 ATOM 5806 N N . GLU A 1 755 ? 8.835 78.368 63.957 1.00 21.47 ? 748 GLU A N 1 ATOM 5807 C CA . GLU A 1 755 ? 7.763 78.339 64.961 1.00 22.64 ? 748 GLU A CA 1 ATOM 5808 C C . GLU A 1 755 ? 6.400 78.288 64.250 1.00 22.52 ? 748 GLU A C 1 ATOM 5809 O O . GLU A 1 755 ? 6.195 78.945 63.227 1.00 22.31 ? 748 GLU A O 1 ATOM 5810 C CB . GLU A 1 755 ? 7.882 79.520 65.910 1.00 24.78 ? 748 GLU A CB 1 ATOM 5811 C CG . GLU A 1 755 ? 9.161 79.391 66.733 1.00 29.56 ? 748 GLU A CG 1 ATOM 5812 C CD . GLU A 1 755 ? 9.224 80.308 67.915 1.00 35.88 ? 748 GLU A CD 1 ATOM 5813 O OE1 . GLU A 1 755 ? 9.602 81.481 67.734 1.00 42.30 ? 748 GLU A OE1 1 ATOM 5814 O OE2 . GLU A 1 755 ? 8.932 79.837 69.028 1.00 44.45 ? 748 GLU A OE2 1 ATOM 5815 N N . VAL A 1 756 ? 5.503 77.456 64.764 1.00 22.29 ? 749 VAL A N 1 ATOM 5816 C CA . VAL A 1 756 ? 4.267 77.103 64.045 1.00 21.79 ? 749 VAL A CA 1 ATOM 5817 C C . VAL A 1 756 ? 3.204 78.221 64.066 1.00 22.12 ? 749 VAL A C 1 ATOM 5818 O O . VAL A 1 756 ? 2.280 78.217 63.255 1.00 22.81 ? 749 VAL A O 1 ATOM 5819 C CB . VAL A 1 756 ? 3.669 75.772 64.576 1.00 21.85 ? 749 VAL A CB 1 ATOM 5820 C CG1 . VAL A 1 756 ? 4.680 74.644 64.465 1.00 23.10 ? 749 VAL A CG1 1 ATOM 5821 C CG2 . VAL A 1 756 ? 3.175 75.931 66.021 1.00 22.13 ? 749 VAL A CG2 1 ATOM 5822 N N . ALA A 1 757 ? 3.349 79.176 64.983 1.00 22.04 ? 750 ALA A N 1 ATOM 5823 C CA . ALA A 1 757 ? 2.405 80.302 65.141 1.00 23.24 ? 750 ALA A CA 1 ATOM 5824 C C . ALA A 1 757 ? 2.997 81.321 66.086 0.70 25.06 ? 750 ALA A C 1 ATOM 5825 O O . ALA A 1 757 ? 2.425 82.390 66.289 0.70 28.86 ? 750 ALA A O 1 ATOM 5826 C CB . ALA A 1 757 ? 1.071 79.825 65.686 1.00 25.60 ? 750 ALA A CB 1 ATOM 5827 O OXT . ALA A 1 757 ? 4.032 81.076 66.695 0.70 24.88 ? 750 ALA A OXT 1 HETATM 5828 ZN ZN . ZN B 2 . ? 17.446 41.083 43.175 1.00 17.06 ? 801 ZN A ZN 1 HETATM 5829 ZN ZN . ZN C 2 . ? 16.691 41.842 46.296 1.00 18.94 ? 802 ZN A ZN 1 HETATM 5830 CA CA . CA D 3 . ? -0.774 49.800 41.378 1.00 15.28 ? 803 CA A CA 1 HETATM 5831 CL CL . CL E 4 . ? 19.061 46.838 51.607 1.00 22.06 ? 804 CL A CL 1 HETATM 5832 C C1 . NAG F 5 . ? 11.730 25.852 57.616 1.00 28.10 ? 805 NAG A C1 1 HETATM 5833 C C2 . NAG F 5 . ? 11.494 24.422 57.150 1.00 33.13 ? 805 NAG A C2 1 HETATM 5834 C C3 . NAG F 5 . ? 10.025 24.057 57.351 1.00 35.51 ? 805 NAG A C3 1 HETATM 5835 C C4 . NAG F 5 . ? 9.537 24.354 58.771 1.00 35.20 ? 805 NAG A C4 1 HETATM 5836 C C5 . NAG F 5 . ? 9.920 25.792 59.144 1.00 33.82 ? 805 NAG A C5 1 HETATM 5837 C C6 . NAG F 5 . ? 9.566 26.150 60.584 1.00 37.17 ? 805 NAG A C6 1 HETATM 5838 C C7 . NAG F 5 . ? 12.985 23.733 55.362 1.00 40.06 ? 805 NAG A C7 1 HETATM 5839 C C8 . NAG F 5 . ? 13.254 23.722 53.895 1.00 41.91 ? 805 NAG A C8 1 HETATM 5840 N N2 . NAG F 5 . ? 11.861 24.335 55.752 1.00 36.12 ? 805 NAG A N2 1 HETATM 5841 O O3 . NAG F 5 . ? 9.869 22.693 57.071 1.00 40.32 ? 805 NAG A O3 1 HETATM 5842 O O4 . NAG F 5 . ? 8.128 24.258 58.779 1.00 36.84 ? 805 NAG A O4 1 HETATM 5843 O O5 . NAG F 5 . ? 11.308 25.990 58.953 1.00 28.93 ? 805 NAG A O5 1 HETATM 5844 O O6 . NAG F 5 . ? 10.181 25.209 61.428 1.00 38.03 ? 805 NAG A O6 1 HETATM 5845 O O7 . NAG F 5 . ? 13.792 23.215 56.132 1.00 49.62 ? 805 NAG A O7 1 HETATM 5846 C C1 . NAG G 5 . ? 7.645 23.381 59.812 1.00 38.98 ? 806 NAG A C1 1 HETATM 5847 C C2 . NAG G 5 . ? 6.165 23.691 60.051 1.00 41.66 ? 806 NAG A C2 1 HETATM 5848 C C3 . NAG G 5 . ? 5.498 22.669 60.978 1.00 47.17 ? 806 NAG A C3 1 HETATM 5849 C C4 . NAG G 5 . ? 5.859 21.219 60.632 1.00 48.96 ? 806 NAG A C4 1 HETATM 5850 C C5 . NAG G 5 . ? 7.375 21.086 60.423 1.00 47.00 ? 806 NAG A C5 1 HETATM 5851 C C6 . NAG G 5 . ? 7.776 19.693 59.951 1.00 51.71 ? 806 NAG A C6 1 HETATM 5852 C C7 . NAG G 5 . ? 5.621 26.132 59.902 1.00 40.10 ? 806 NAG A C7 1 HETATM 5853 C C8 . NAG G 5 . ? 5.421 26.012 58.426 1.00 35.51 ? 806 NAG A C8 1 HETATM 5854 N N2 . NAG G 5 . ? 5.964 25.033 60.593 1.00 39.03 ? 806 NAG A N2 1 HETATM 5855 O O3 . NAG G 5 . ? 4.099 22.844 60.880 1.00 52.23 ? 806 NAG A O3 1 HETATM 5856 O O4 . NAG G 5 . ? 5.380 20.320 61.631 1.00 58.11 ? 806 NAG A O4 1 HETATM 5857 O O5 . NAG G 5 . ? 7.816 22.022 59.444 1.00 43.42 ? 806 NAG A O5 1 HETATM 5858 O O6 . NAG G 5 . ? 7.462 19.558 58.580 1.00 55.48 ? 806 NAG A O6 1 HETATM 5859 O O7 . NAG G 5 . ? 5.458 27.242 60.436 1.00 44.98 ? 806 NAG A O7 1 HETATM 5860 C C1 . NAG H 5 . ? 4.093 27.889 25.068 1.00 38.79 ? 807 NAG A C1 1 HETATM 5861 C C2 . NAG H 5 . ? 2.699 28.476 24.931 1.00 42.10 ? 807 NAG A C2 1 HETATM 5862 C C3 . NAG H 5 . ? 1.695 27.540 24.263 1.00 46.83 ? 807 NAG A C3 1 HETATM 5863 C C4 . NAG H 5 . ? 2.298 26.714 23.120 1.00 54.89 ? 807 NAG A C4 1 HETATM 5864 C C5 . NAG H 5 . ? 3.695 26.174 23.485 1.00 53.74 ? 807 NAG A C5 1 HETATM 5865 C C6 . NAG H 5 . ? 4.295 25.303 22.357 1.00 56.17 ? 807 NAG A C6 1 HETATM 5866 C C7 . NAG H 5 . ? 1.922 30.082 26.583 1.00 46.70 ? 807 NAG A C7 1 HETATM 5867 C C8 . NAG H 5 . ? 1.945 31.114 25.498 1.00 43.39 ? 807 NAG A C8 1 HETATM 5868 N N2 . NAG H 5 . ? 2.278 28.843 26.270 1.00 39.95 ? 807 NAG A N2 1 HETATM 5869 O O3 . NAG H 5 . ? 0.663 28.347 23.749 1.00 55.27 ? 807 NAG A O3 1 HETATM 5870 O O4 . NAG H 5 . ? 1.403 25.669 22.742 1.00 68.23 ? 807 NAG A O4 1 HETATM 5871 O O5 . NAG H 5 . ? 4.536 27.264 23.888 1.00 45.22 ? 807 NAG A O5 1 HETATM 5872 O O6 . NAG H 5 . ? 5.661 25.560 22.061 1.00 67.26 ? 807 NAG A O6 1 HETATM 5873 O O7 . NAG H 5 . ? 1.575 30.399 27.714 1.00 56.19 ? 807 NAG A O7 1 HETATM 5874 C C1 . NAG I 5 . ? 19.957 24.941 17.553 1.00 38.41 ? 808 NAG A C1 1 HETATM 5875 C C2 . NAG I 5 . ? 20.571 23.729 16.862 1.00 38.77 ? 808 NAG A C2 1 HETATM 5876 C C3 . NAG I 5 . ? 19.722 23.339 15.652 1.00 41.92 ? 808 NAG A C3 1 HETATM 5877 C C4 . NAG I 5 . ? 18.209 23.282 15.948 1.00 43.51 ? 808 NAG A C4 1 HETATM 5878 C C5 . NAG I 5 . ? 17.723 24.458 16.824 1.00 42.20 ? 808 NAG A C5 1 HETATM 5879 C C6 . NAG I 5 . ? 16.300 24.304 17.386 1.00 42.21 ? 808 NAG A C6 1 HETATM 5880 C C7 . NAG I 5 . ? 23.007 23.519 17.086 1.00 44.06 ? 808 NAG A C7 1 HETATM 5881 C C8 . NAG I 5 . ? 24.370 23.845 16.543 1.00 42.99 ? 808 NAG A C8 1 HETATM 5882 N N2 . NAG I 5 . ? 21.943 23.991 16.432 1.00 39.53 ? 808 NAG A N2 1 HETATM 5883 O O3 . NAG I 5 . ? 20.195 22.105 15.142 1.00 41.14 ? 808 NAG A O3 1 HETATM 5884 O O4 . NAG I 5 . ? 17.543 23.291 14.697 1.00 50.43 ? 808 NAG A O4 1 HETATM 5885 O O5 . NAG I 5 . ? 18.608 24.676 17.912 1.00 40.78 ? 808 NAG A O5 1 HETATM 5886 O O6 . NAG I 5 . ? 16.149 23.097 18.112 1.00 40.44 ? 808 NAG A O6 1 HETATM 5887 O O7 . NAG I 5 . ? 22.917 22.842 18.105 1.00 46.83 ? 808 NAG A O7 1 HETATM 5888 C C1 . NAG J 5 . ? 16.549 22.250 14.567 1.00 52.32 ? 809 NAG A C1 1 HETATM 5889 C C2 . NAG J 5 . ? 15.543 22.723 13.511 1.00 53.78 ? 809 NAG A C2 1 HETATM 5890 C C3 . NAG J 5 . ? 14.534 21.637 13.136 1.00 57.64 ? 809 NAG A C3 1 HETATM 5891 C C4 . NAG J 5 . ? 15.219 20.293 12.868 1.00 62.82 ? 809 NAG A C4 1 HETATM 5892 C C5 . NAG J 5 . ? 16.144 19.947 14.048 1.00 59.31 ? 809 NAG A C5 1 HETATM 5893 C C6 . NAG J 5 . ? 16.854 18.603 13.878 1.00 64.79 ? 809 NAG A C6 1 HETATM 5894 C C7 . NAG J 5 . ? 15.250 25.163 13.647 1.00 52.27 ? 809 NAG A C7 1 HETATM 5895 C C8 . NAG J 5 . ? 14.427 26.286 14.200 1.00 46.58 ? 809 NAG A C8 1 HETATM 5896 N N2 . NAG J 5 . ? 14.852 23.925 13.966 1.00 50.82 ? 809 NAG A N2 1 HETATM 5897 O O3 . NAG J 5 . ? 13.838 22.047 11.981 1.00 59.66 ? 809 NAG A O3 1 HETATM 5898 O O4 . NAG J 5 . ? 14.248 19.289 12.623 1.00 69.81 ? 809 NAG A O4 1 HETATM 5899 O O5 . NAG J 5 . ? 17.104 20.985 14.237 1.00 55.17 ? 809 NAG A O5 1 HETATM 5900 O O6 . NAG J 5 . ? 18.076 18.778 13.194 1.00 62.58 ? 809 NAG A O6 1 HETATM 5901 O O7 . NAG J 5 . ? 16.234 25.418 12.945 1.00 55.46 ? 809 NAG A O7 1 HETATM 5902 C C1 . NAG K 5 . ? 19.678 54.654 10.559 1.00 57.68 ? 810 NAG A C1 1 HETATM 5903 C C2 . NAG K 5 . ? 19.250 56.060 10.142 1.00 66.57 ? 810 NAG A C2 1 HETATM 5904 C C3 . NAG K 5 . ? 17.748 56.063 9.892 1.00 71.06 ? 810 NAG A C3 1 HETATM 5905 C C4 . NAG K 5 . ? 17.445 55.150 8.710 1.00 70.75 ? 810 NAG A C4 1 HETATM 5906 C C5 . NAG K 5 . ? 17.967 53.725 8.926 1.00 67.18 ? 810 NAG A C5 1 HETATM 5907 C C6 . NAG K 5 . ? 18.235 53.088 7.557 1.00 63.62 ? 810 NAG A C6 1 HETATM 5908 C C7 . NAG K 5 . ? 20.751 57.756 11.121 1.00 71.84 ? 810 NAG A C7 1 HETATM 5909 C C8 . NAG K 5 . ? 20.955 58.720 12.255 1.00 67.87 ? 810 NAG A C8 1 HETATM 5910 N N2 . NAG K 5 . ? 19.620 57.039 11.154 1.00 71.02 ? 810 NAG A N2 1 HETATM 5911 O O3 . NAG K 5 . ? 17.292 57.367 9.612 1.00 81.24 ? 810 NAG A O3 1 HETATM 5912 O O4 . NAG K 5 . ? 16.054 55.115 8.470 1.00 77.45 ? 810 NAG A O4 1 HETATM 5913 O O5 . NAG K 5 . ? 19.146 53.606 9.738 1.00 65.31 ? 810 NAG A O5 1 HETATM 5914 O O6 . NAG K 5 . ? 17.857 51.729 7.543 1.00 62.84 ? 810 NAG A O6 1 HETATM 5915 O O7 . NAG K 5 . ? 21.606 57.665 10.234 1.00 80.59 ? 810 NAG A O7 1 HETATM 5916 C C1 . NAG L 5 . ? 36.562 37.737 52.729 1.00 36.02 ? 811 NAG A C1 1 HETATM 5917 C C2 . NAG L 5 . ? 36.572 37.813 51.197 1.00 35.51 ? 811 NAG A C2 1 HETATM 5918 C C3 . NAG L 5 . ? 37.910 37.328 50.598 1.00 42.57 ? 811 NAG A C3 1 HETATM 5919 C C4 . NAG L 5 . ? 39.123 37.982 51.277 1.00 43.65 ? 811 NAG A C4 1 HETATM 5920 C C5 . NAG L 5 . ? 38.972 37.932 52.802 1.00 41.99 ? 811 NAG A C5 1 HETATM 5921 C C6 . NAG L 5 . ? 40.109 38.709 53.480 1.00 42.52 ? 811 NAG A C6 1 HETATM 5922 C C7 . NAG L 5 . ? 34.530 37.626 49.883 1.00 27.64 ? 811 NAG A C7 1 HETATM 5923 C C8 . NAG L 5 . ? 33.431 36.758 49.346 1.00 28.05 ? 811 NAG A C8 1 HETATM 5924 N N2 . NAG L 5 . ? 35.454 37.062 50.651 1.00 31.94 ? 811 NAG A N2 1 HETATM 5925 O O3 . NAG L 5 . ? 37.952 37.625 49.216 1.00 47.28 ? 811 NAG A O3 1 HETATM 5926 O O4 . NAG L 5 . ? 40.378 37.405 50.876 1.00 48.10 ? 811 NAG A O4 1 HETATM 5927 O O5 . NAG L 5 . ? 37.706 38.432 53.228 1.00 39.42 ? 811 NAG A O5 1 HETATM 5928 O O6 . NAG L 5 . ? 40.075 40.081 53.115 1.00 43.52 ? 811 NAG A O6 1 HETATM 5929 O O7 . NAG L 5 . ? 34.546 38.815 49.595 1.00 27.25 ? 811 NAG A O7 1 HETATM 5930 C C1 . NAG M 5 . ? 24.225 61.695 68.753 1.00 25.23 ? 812 NAG A C1 1 HETATM 5931 C C2 . NAG M 5 . ? 22.847 62.320 68.945 1.00 26.09 ? 812 NAG A C2 1 HETATM 5932 C C3 . NAG M 5 . ? 23.081 63.763 69.363 1.00 27.18 ? 812 NAG A C3 1 HETATM 5933 C C4 . NAG M 5 . ? 24.044 63.891 70.555 1.00 28.34 ? 812 NAG A C4 1 HETATM 5934 C C5 . NAG M 5 . ? 25.364 63.159 70.289 1.00 28.29 ? 812 NAG A C5 1 HETATM 5935 C C6 . NAG M 5 . ? 26.351 63.114 71.464 1.00 32.82 ? 812 NAG A C6 1 HETATM 5936 C C7 . NAG M 5 . ? 20.813 61.722 67.597 1.00 34.53 ? 812 NAG A C7 1 HETATM 5937 C C8 . NAG M 5 . ? 20.187 61.218 68.860 1.00 35.21 ? 812 NAG A C8 1 HETATM 5938 N N2 . NAG M 5 . ? 22.048 62.232 67.713 1.00 27.86 ? 812 NAG A N2 1 HETATM 5939 O O3 . NAG M 5 . ? 21.849 64.377 69.670 1.00 28.34 ? 812 NAG A O3 1 HETATM 5940 O O4 . NAG M 5 . ? 24.301 65.261 70.732 1.00 30.83 ? 812 NAG A O4 1 HETATM 5941 O O5 . NAG M 5 . ? 25.053 61.828 69.914 1.00 28.28 ? 812 NAG A O5 1 HETATM 5942 O O6 . NAG M 5 . ? 25.726 62.679 72.656 1.00 35.21 ? 812 NAG A O6 1 HETATM 5943 O O7 . NAG M 5 . ? 20.157 61.664 66.519 1.00 37.31 ? 812 NAG A O7 1 HETATM 5944 C C1 . NAG N 5 . ? 24.087 65.693 72.087 1.00 33.46 ? 813 NAG A C1 1 HETATM 5945 C C2 . NAG N 5 . ? 24.672 67.101 72.173 1.00 38.10 ? 813 NAG A C2 1 HETATM 5946 C C3 . NAG N 5 . ? 24.438 67.694 73.560 1.00 39.74 ? 813 NAG A C3 1 HETATM 5947 C C4 . NAG N 5 . ? 22.963 67.601 73.970 1.00 38.66 ? 813 NAG A C4 1 HETATM 5948 C C5 . NAG N 5 . ? 22.460 66.168 73.768 1.00 37.24 ? 813 NAG A C5 1 HETATM 5949 C C6 . NAG N 5 . ? 20.959 66.054 74.016 1.00 43.66 ? 813 NAG A C6 1 HETATM 5950 C C7 . NAG N 5 . ? 26.636 67.391 70.678 1.00 42.55 ? 813 NAG A C7 1 HETATM 5951 C C8 . NAG N 5 . ? 25.774 67.823 69.524 1.00 32.62 ? 813 NAG A C8 1 HETATM 5952 N N2 . NAG N 5 . ? 26.092 67.070 71.860 1.00 41.57 ? 813 NAG A N2 1 HETATM 5953 O O3 . NAG N 5 . ? 24.872 69.036 73.567 1.00 43.82 ? 813 NAG A O3 1 HETATM 5954 O O4 . NAG N 5 . ? 22.835 67.948 75.336 1.00 43.18 ? 813 NAG A O4 1 HETATM 5955 O O5 . NAG N 5 . ? 22.714 65.737 72.438 1.00 34.06 ? 813 NAG A O5 1 HETATM 5956 O O6 . NAG N 5 . ? 20.276 66.970 73.177 1.00 49.65 ? 813 NAG A O6 1 HETATM 5957 O O7 . NAG N 5 . ? 27.851 67.328 70.507 1.00 53.27 ? 813 NAG A O7 1 HETATM 5958 C C1 . NAG O 5 . ? 15.222 83.742 52.625 1.00 22.76 ? 814 NAG A C1 1 HETATM 5959 C C2 . NAG O 5 . ? 14.199 83.875 51.497 1.00 22.13 ? 814 NAG A C2 1 HETATM 5960 C C3 . NAG O 5 . ? 14.018 85.354 51.167 1.00 26.52 ? 814 NAG A C3 1 HETATM 5961 C C4 . NAG O 5 . ? 13.650 86.167 52.429 1.00 28.34 ? 814 NAG A C4 1 HETATM 5962 C C5 . NAG O 5 . ? 14.581 85.854 53.604 1.00 28.80 ? 814 NAG A C5 1 HETATM 5963 C C6 . NAG O 5 . ? 14.060 86.463 54.919 1.00 32.54 ? 814 NAG A C6 1 HETATM 5964 C C7 . NAG O 5 . ? 13.747 82.359 49.632 1.00 20.23 ? 814 NAG A C7 1 HETATM 5965 C C8 . NAG O 5 . ? 14.328 81.603 48.475 1.00 20.54 ? 814 NAG A C8 1 HETATM 5966 N N2 . NAG O 5 . ? 14.609 83.094 50.340 1.00 20.24 ? 814 NAG A N2 1 HETATM 5967 O O3 . NAG O 5 . ? 12.993 85.458 50.210 1.00 26.85 ? 814 NAG A O3 1 HETATM 5968 O O4 . NAG O 5 . ? 13.784 87.563 52.231 1.00 33.76 ? 814 NAG A O4 1 HETATM 5969 O O5 . NAG O 5 . ? 14.719 84.454 53.744 1.00 26.16 ? 814 NAG A O5 1 HETATM 5970 O O6 . NAG O 5 . ? 15.101 86.605 55.877 1.00 45.23 ? 814 NAG A O6 1 HETATM 5971 O O7 . NAG O 5 . ? 12.523 82.289 49.876 1.00 20.71 ? 814 NAG A O7 1 HETATM 5972 C C1 . NAG P 5 . ? 12.639 88.081 51.525 1.00 32.53 ? 815 NAG A C1 1 HETATM 5973 C C2 . NAG P 5 . ? 12.089 89.337 52.186 1.00 36.75 ? 815 NAG A C2 1 HETATM 5974 C C3 . NAG P 5 . ? 11.058 90.036 51.301 1.00 35.09 ? 815 NAG A C3 1 HETATM 5975 C C4 . NAG P 5 . ? 11.619 90.198 49.889 1.00 35.01 ? 815 NAG A C4 1 HETATM 5976 C C5 . NAG P 5 . ? 11.972 88.806 49.369 1.00 36.49 ? 815 NAG A C5 1 HETATM 5977 C C6 . NAG P 5 . ? 12.407 88.760 47.908 1.00 44.76 ? 815 NAG A C6 1 HETATM 5978 C C7 . NAG P 5 . ? 12.135 89.355 54.637 1.00 44.46 ? 815 NAG A C7 1 HETATM 5979 C C8 . NAG P 5 . ? 13.457 90.075 54.587 1.00 38.27 ? 815 NAG A C8 1 HETATM 5980 N N2 . NAG P 5 . ? 11.527 89.027 53.486 1.00 42.24 ? 815 NAG A N2 1 HETATM 5981 O O3 . NAG P 5 . ? 10.764 91.306 51.857 1.00 34.95 ? 815 NAG A O3 1 HETATM 5982 O O4 . NAG P 5 . ? 10.682 90.829 49.039 1.00 33.88 ? 815 NAG A O4 1 HETATM 5983 O O5 . NAG P 5 . ? 13.019 88.324 50.194 1.00 34.52 ? 815 NAG A O5 1 HETATM 5984 O O6 . NAG P 5 . ? 13.728 89.237 47.784 1.00 57.89 ? 815 NAG A O6 1 HETATM 5985 O O7 . NAG P 5 . ? 11.646 89.068 55.730 1.00 63.47 ? 815 NAG A O7 1 HETATM 5986 C C1 . BMA Q 6 . ? 10.742 92.152 48.874 1.00 35.74 ? 816 BMA A C1 1 HETATM 5987 C C2 . BMA Q 6 . ? 10.418 92.527 47.430 1.00 34.63 ? 816 BMA A C2 1 HETATM 5988 C C3 . BMA Q 6 . ? 10.137 94.016 47.371 1.00 32.75 ? 816 BMA A C3 1 HETATM 5989 C C4 . BMA Q 6 . ? 9.030 94.381 48.381 1.00 36.30 ? 816 BMA A C4 1 HETATM 5990 C C5 . BMA Q 6 . ? 9.335 93.846 49.788 1.00 37.02 ? 816 BMA A C5 1 HETATM 5991 C C6 . BMA Q 6 . ? 8.196 94.040 50.780 1.00 38.47 ? 816 BMA A C6 1 HETATM 5992 O O2 . BMA Q 6 . ? 9.260 91.803 46.982 1.00 35.47 ? 816 BMA A O2 1 HETATM 5993 O O3 . BMA Q 6 . ? 9.746 94.345 46.031 1.00 31.96 ? 816 BMA A O3 1 HETATM 5994 O O4 . BMA Q 6 . ? 8.872 95.793 48.391 1.00 37.81 ? 816 BMA A O4 1 HETATM 5995 O O5 . BMA Q 6 . ? 9.614 92.441 49.721 1.00 32.57 ? 816 BMA A O5 1 HETATM 5996 O O6 . BMA Q 6 . ? 8.656 93.634 52.076 1.00 40.36 ? 816 BMA A O6 1 HETATM 5997 C C1 . MAN R 7 . ? 10.392 95.339 45.395 1.00 40.19 ? 817 MAN A C1 1 HETATM 5998 C C2 . MAN R 7 . ? 9.527 95.755 44.197 1.00 40.20 ? 817 MAN A C2 1 HETATM 5999 C C3 . MAN R 7 . ? 9.662 94.743 43.047 1.00 43.79 ? 817 MAN A C3 1 HETATM 6000 C C4 . MAN R 7 . ? 11.129 94.392 42.757 1.00 49.21 ? 817 MAN A C4 1 HETATM 6001 C C5 . MAN R 7 . ? 11.849 94.034 44.068 1.00 47.13 ? 817 MAN A C5 1 HETATM 6002 C C6 . MAN R 7 . ? 13.309 93.596 43.898 1.00 52.23 ? 817 MAN A C6 1 HETATM 6003 O O2 . MAN R 7 . ? 9.956 97.025 43.790 1.00 46.06 ? 817 MAN A O2 1 HETATM 6004 O O3 . MAN R 7 . ? 9.010 95.185 41.873 1.00 48.34 ? 817 MAN A O3 1 HETATM 6005 O O4 . MAN R 7 . ? 11.196 93.315 41.841 1.00 53.83 ? 817 MAN A O4 1 HETATM 6006 O O5 . MAN R 7 . ? 11.735 95.124 44.975 1.00 39.99 ? 817 MAN A O5 1 HETATM 6007 O O6 . MAN R 7 . ? 14.093 94.683 43.461 1.00 47.57 ? 817 MAN A O6 1 HETATM 6008 O O4 . 29D S 8 . ? 35.644 53.303 49.187 1.00 99.68 ? 818 29D A O4 1 HETATM 6009 C C4 . 29D S 8 . ? 34.980 54.070 48.275 1.00 89.59 ? 818 29D A C4 1 HETATM 6010 C C4A . 29D S 8 . ? 33.592 53.969 48.115 1.00 84.24 ? 818 29D A C4A 1 HETATM 6011 N N3 . 29D S 8 . ? 35.677 54.949 47.511 1.00 89.54 ? 818 29D A N3 1 HETATM 6012 C C8A . 29D S 8 . ? 32.978 54.787 47.157 1.00 81.90 ? 818 29D A C8A 1 HETATM 6013 N N5 . 29D S 8 . ? 32.842 53.102 48.859 1.00 80.74 ? 818 29D A N5 1 HETATM 6014 C C2 . 29D S 8 . ? 35.055 55.731 46.591 1.00 83.87 ? 818 29D A C2 1 HETATM 6015 N N8 . 29D S 8 . ? 31.645 54.718 46.972 1.00 71.42 ? 818 29D A N8 1 HETATM 6016 N N1 . 29D S 8 . ? 33.712 55.651 46.415 1.00 83.40 ? 818 29D A N1 1 HETATM 6017 C C6 . 29D S 8 . ? 31.497 53.027 48.675 1.00 74.18 ? 818 29D A C6 1 HETATM 6018 N N2 . 29D S 8 . ? 35.781 56.597 45.841 1.00 90.70 ? 818 29D A N2 1 HETATM 6019 C C7 . 29D S 8 . ? 30.929 53.874 47.718 1.00 72.40 ? 818 29D A C7 1 HETATM 6020 C C9 . 29D S 8 . ? 30.624 52.068 49.493 1.00 67.75 ? 818 29D A C9 1 HETATM 6021 N N10 . 29D S 8 . ? 29.558 51.405 48.722 1.00 85.41 ? 818 29D A N10 1 HETATM 6022 C CBX . 29D S 8 . ? 29.101 51.996 47.591 1.00 105.54 ? 818 29D A CBX 1 HETATM 6023 C CAQ . 29D S 8 . ? 28.166 53.029 47.696 1.00 101.89 ? 818 29D A CAQ 1 HETATM 6024 C CAR . 29D S 8 . ? 29.603 51.617 46.336 1.00 91.85 ? 818 29D A CAR 1 HETATM 6025 C CAS . 29D S 8 . ? 27.729 53.677 46.545 1.00 118.45 ? 818 29D A CAS 1 HETATM 6026 C CAT . 29D S 8 . ? 29.164 52.269 45.183 1.00 119.38 ? 818 29D A CAT 1 HETATM 6027 C CBY . 29D S 8 . ? 28.220 53.297 45.291 1.00 123.84 ? 818 29D A CBY 1 HETATM 6028 C CBV . 29D S 8 . ? 27.730 54.037 44.074 1.00 117.48 ? 818 29D A CBV 1 HETATM 6029 O OAJ . 29D S 8 . ? 27.311 55.177 44.253 1.00 120.77 ? 818 29D A OAJ 1 HETATM 6030 N NBM . 29D S 8 . ? 27.788 53.458 42.862 1.00 127.09 ? 818 29D A NBM 1 HETATM 6031 C CCG . 29D S 8 . ? 27.358 54.041 41.571 1.00 102.88 ? 818 29D A CCG 1 HETATM 6032 C CBR . 29D S 8 . ? 27.754 55.488 41.353 1.00 113.14 ? 818 29D A CBR 1 HETATM 6033 O OAO . 29D S 8 . ? 28.930 55.718 40.991 1.00 122.26 ? 818 29D A OAO 1 HETATM 6034 C CBC . 29D S 8 . ? 25.843 53.824 41.362 1.00 72.58 ? 818 29D A CBC 1 HETATM 6035 C CAY . 29D S 8 . ? 24.944 53.912 42.603 1.00 60.09 ? 818 29D A CAY 1 HETATM 6036 C CBU . 29D S 8 . ? 24.831 52.579 43.314 1.00 87.58 ? 818 29D A CBU 1 HETATM 6037 O OAI . 29D S 8 . ? 24.415 52.519 44.467 1.00 107.34 ? 818 29D A OAI 1 HETATM 6038 O OAF . 29D S 8 . ? 26.915 56.406 41.531 1.00 103.38 ? 818 29D A OAF 1 HETATM 6039 N NBL . 29D S 8 . ? 25.223 51.516 42.614 1.00 88.69 ? 818 29D A NBL 1 HETATM 6040 C CCF . 29D S 8 . ? 25.173 50.175 43.153 1.00 69.70 ? 818 29D A CCF 1 HETATM 6041 C CBQ . 29D S 8 . ? 26.551 49.574 43.201 1.00 80.68 ? 818 29D A CBQ 1 HETATM 6042 O OAN . 29D S 8 . ? 27.161 49.368 42.125 1.00 99.49 ? 818 29D A OAN 1 HETATM 6043 C CBB . 29D S 8 . ? 24.232 49.491 42.170 1.00 47.54 ? 818 29D A CBB 1 HETATM 6044 C CAX . 29D S 8 . ? 23.810 48.136 42.700 1.00 44.65 ? 818 29D A CAX 1 HETATM 6045 C CBT . 29D S 8 . ? 22.474 48.120 43.439 1.00 37.03 ? 818 29D A CBT 1 HETATM 6046 O OAH . 29D S 8 . ? 22.078 49.045 44.142 1.00 38.16 ? 818 29D A OAH 1 HETATM 6047 O OAE . 29D S 8 . ? 27.038 49.317 44.328 1.00 80.54 ? 818 29D A OAE 1 HETATM 6048 N NBK . 29D S 8 . ? 21.777 47.001 43.278 1.00 32.83 ? 818 29D A NBK 1 HETATM 6049 C CCE . 29D S 8 . ? 20.481 46.734 43.915 1.00 27.29 ? 818 29D A CCE 1 HETATM 6050 C CBP . 29D S 8 . ? 20.720 46.365 45.344 1.00 33.16 ? 818 29D A CBP 1 HETATM 6051 O OAM . 29D S 8 . ? 21.748 45.700 45.620 1.00 38.92 ? 818 29D A OAM 1 HETATM 6052 C CBA . 29D S 8 . ? 19.875 45.512 43.222 1.00 21.22 ? 818 29D A CBA 1 HETATM 6053 C CAW . 29D S 8 . ? 18.648 44.894 43.921 1.00 20.23 ? 818 29D A CAW 1 HETATM 6054 C CBS . 29D S 8 . ? 17.883 44.138 42.828 1.00 16.94 ? 818 29D A CBS 1 HETATM 6055 O OAG . 29D S 8 . ? 18.196 42.976 42.435 1.00 19.05 ? 818 29D A OAG 1 HETATM 6056 O OAD . 29D S 8 . ? 19.877 46.739 46.190 1.00 35.52 ? 818 29D A OAD 1 HETATM 6057 N N . 29D S 8 . ? 16.794 44.831 42.400 1.00 16.90 ? 818 29D A N 1 HETATM 6058 C CA . 29D S 8 . ? 16.046 44.268 41.266 1.00 16.37 ? 818 29D A CA 1 HETATM 6059 C C . 29D S 8 . ? 16.970 44.367 40.075 1.00 17.07 ? 818 29D A C 1 HETATM 6060 O O . 29D S 8 . ? 17.870 45.267 40.049 1.00 17.44 ? 818 29D A O 1 HETATM 6061 C CB . 29D S 8 . ? 14.748 45.048 40.949 1.00 16.30 ? 818 29D A CB 1 HETATM 6062 C CG . 29D S 8 . ? 15.041 46.516 40.658 1.00 17.70 ? 818 29D A CG 1 HETATM 6063 C CD . 29D S 8 . ? 13.832 47.285 40.152 1.00 17.59 ? 818 29D A CD 1 HETATM 6064 O OE2 . 29D S 8 . ? 12.942 46.707 39.465 1.00 17.02 ? 818 29D A OE2 1 HETATM 6065 O OE1 . 29D S 8 . ? 13.774 48.502 40.430 1.00 17.19 ? 818 29D A OE1 1 HETATM 6066 O OXT . 29D S 8 . ? 16.813 43.543 39.137 1.00 17.31 ? 818 29D A OXT 1 HETATM 6067 O O . HOH T 9 . ? 8.243 44.595 46.344 1.00 14.40 ? 901 HOH A O 1 HETATM 6068 O O . HOH T 9 . ? 6.886 58.151 37.536 1.00 16.70 ? 902 HOH A O 1 HETATM 6069 O O . HOH T 9 . ? 7.929 69.425 59.101 1.00 16.62 ? 903 HOH A O 1 HETATM 6070 O O . HOH T 9 . ? 13.589 44.634 49.771 1.00 19.44 ? 904 HOH A O 1 HETATM 6071 O O . HOH T 9 . ? 9.216 50.559 46.404 1.00 15.98 ? 905 HOH A O 1 HETATM 6072 O O . HOH T 9 . ? 0.931 50.358 39.835 1.00 15.39 ? 906 HOH A O 1 HETATM 6073 O O . HOH T 9 . ? 12.010 61.804 43.489 1.00 16.70 ? 907 HOH A O 1 HETATM 6074 O O . HOH T 9 . ? 13.603 29.797 40.065 1.00 18.43 ? 908 HOH A O 1 HETATM 6075 O O . HOH T 9 . ? 15.048 41.663 38.639 1.00 15.94 ? 909 HOH A O 1 HETATM 6076 O O . HOH T 9 . ? 9.624 60.714 57.617 1.00 15.61 ? 910 HOH A O 1 HETATM 6077 O O . HOH T 9 . ? 10.863 36.642 42.295 1.00 16.35 ? 911 HOH A O 1 HETATM 6078 O O . HOH T 9 . ? -5.439 59.602 59.745 1.00 17.57 ? 912 HOH A O 1 HETATM 6079 O O . HOH T 9 . ? 13.710 26.973 51.562 1.00 20.83 ? 913 HOH A O 1 HETATM 6080 O O . HOH T 9 . ? 7.426 71.668 45.171 1.00 17.71 ? 914 HOH A O 1 HETATM 6081 O O . HOH T 9 . ? 5.751 68.767 55.306 1.00 16.63 ? 915 HOH A O 1 HETATM 6082 O O . HOH T 9 . ? 16.849 37.002 43.896 1.00 16.15 ? 916 HOH A O 1 HETATM 6083 O O . HOH T 9 . ? -3.609 62.072 53.924 1.00 17.88 ? 917 HOH A O 1 HETATM 6084 O O . HOH T 9 . ? 29.376 36.076 44.330 1.00 19.32 ? 918 HOH A O 1 HETATM 6085 O O . HOH T 9 . ? 6.422 75.829 60.923 1.00 16.82 ? 919 HOH A O 1 HETATM 6086 O O . HOH T 9 . ? -3.455 59.977 61.760 1.00 18.33 ? 920 HOH A O 1 HETATM 6087 O O . HOH T 9 . ? 19.283 47.634 54.660 1.00 18.84 ? 921 HOH A O 1 HETATM 6088 O O . HOH T 9 . ? 3.964 70.324 64.401 1.00 20.29 ? 922 HOH A O 1 HETATM 6089 O O . HOH T 9 . ? 18.955 62.058 36.337 1.00 17.67 ? 923 HOH A O 1 HETATM 6090 O O . HOH T 9 . ? -7.024 51.479 51.456 1.00 19.32 ? 924 HOH A O 1 HETATM 6091 O O . HOH T 9 . ? 17.806 40.449 32.192 1.00 18.46 ? 925 HOH A O 1 HETATM 6092 O O . HOH T 9 . ? 19.986 61.347 62.880 1.00 21.26 ? 926 HOH A O 1 HETATM 6093 O O . HOH T 9 . ? -4.406 59.382 57.140 1.00 18.25 ? 927 HOH A O 1 HETATM 6094 O O . HOH T 9 . ? 3.513 71.825 43.492 1.00 16.32 ? 928 HOH A O 1 HETATM 6095 O O . HOH T 9 . ? 29.891 42.602 32.068 1.00 23.19 ? 929 HOH A O 1 HETATM 6096 O O . HOH T 9 . ? 23.830 46.006 34.581 1.00 19.31 ? 930 HOH A O 1 HETATM 6097 O O . HOH T 9 . ? 14.665 36.724 27.899 1.00 17.97 ? 931 HOH A O 1 HETATM 6098 O O . HOH T 9 . ? 18.490 33.518 43.445 1.00 19.13 ? 932 HOH A O 1 HETATM 6099 O O . HOH T 9 . ? 28.879 33.814 32.671 1.00 20.63 ? 933 HOH A O 1 HETATM 6100 O O . HOH T 9 . ? 5.979 75.197 54.060 1.00 19.81 ? 934 HOH A O 1 HETATM 6101 O O . HOH T 9 . ? 3.637 62.129 50.466 1.00 19.29 ? 935 HOH A O 1 HETATM 6102 O O . HOH T 9 . ? 14.572 32.022 48.061 1.00 18.55 ? 936 HOH A O 1 HETATM 6103 O O . HOH T 9 . ? 4.663 34.856 45.356 1.00 19.37 ? 937 HOH A O 1 HETATM 6104 O O . HOH T 9 . ? 0.277 56.794 45.672 1.00 20.34 ? 938 HOH A O 1 HETATM 6105 O O . HOH T 9 . ? -0.354 43.351 60.661 1.00 25.72 ? 939 HOH A O 1 HETATM 6106 O O . HOH T 9 . ? 14.356 37.994 34.795 1.00 18.22 ? 940 HOH A O 1 HETATM 6107 O O . HOH T 9 . ? 22.141 87.833 32.428 1.00 25.28 ? 941 HOH A O 1 HETATM 6108 O O . HOH T 9 . ? 23.160 67.617 34.169 1.00 20.33 ? 942 HOH A O 1 HETATM 6109 O O . HOH T 9 . ? 23.063 68.560 42.965 1.00 20.83 ? 943 HOH A O 1 HETATM 6110 O O . HOH T 9 . ? 20.567 45.667 36.339 1.00 16.67 ? 944 HOH A O 1 HETATM 6111 O O . HOH T 9 . ? 24.370 37.154 32.462 1.00 21.05 ? 945 HOH A O 1 HETATM 6112 O O . HOH T 9 . ? 16.131 55.549 35.435 1.00 17.02 ? 946 HOH A O 1 HETATM 6113 O O . HOH T 9 . ? 25.643 37.036 38.040 1.00 20.01 ? 947 HOH A O 1 HETATM 6114 O O . HOH T 9 . ? 9.552 29.094 43.009 1.00 19.63 ? 948 HOH A O 1 HETATM 6115 O O . HOH T 9 . ? 27.477 31.021 28.688 1.00 23.70 ? 949 HOH A O 1 HETATM 6116 O O . HOH T 9 . ? 20.689 27.485 48.691 1.00 21.21 ? 950 HOH A O 1 HETATM 6117 O O . HOH T 9 . ? 10.096 30.876 26.695 1.00 26.19 ? 951 HOH A O 1 HETATM 6118 O O . HOH T 9 . ? 29.038 60.464 57.460 1.00 30.13 ? 952 HOH A O 1 HETATM 6119 O O . HOH T 9 . ? 16.860 61.859 38.243 1.00 17.06 ? 953 HOH A O 1 HETATM 6120 O O . HOH T 9 . ? 19.312 36.081 43.168 1.00 19.42 ? 954 HOH A O 1 HETATM 6121 O O . HOH T 9 . ? 20.158 31.268 43.430 1.00 20.81 ? 955 HOH A O 1 HETATM 6122 O O . HOH T 9 . ? 7.966 50.210 40.873 1.00 16.86 ? 956 HOH A O 1 HETATM 6123 O O . HOH T 9 . ? -2.599 44.065 37.658 1.00 17.79 ? 957 HOH A O 1 HETATM 6124 O O . HOH T 9 . ? 6.478 60.706 67.078 1.00 22.40 ? 958 HOH A O 1 HETATM 6125 O O . HOH T 9 . ? 5.140 64.521 37.014 1.00 18.94 ? 959 HOH A O 1 HETATM 6126 O O . HOH T 9 . ? 14.651 80.685 38.150 1.00 22.01 ? 960 HOH A O 1 HETATM 6127 O O . HOH T 9 . ? 6.766 54.779 43.843 1.00 18.45 ? 961 HOH A O 1 HETATM 6128 O O . HOH T 9 . ? 13.917 40.740 53.422 1.00 19.19 ? 962 HOH A O 1 HETATM 6129 O O . HOH T 9 . ? 11.142 27.388 54.247 1.00 23.16 ? 963 HOH A O 1 HETATM 6130 O O . HOH T 9 . ? 22.980 44.345 36.560 1.00 20.15 ? 964 HOH A O 1 HETATM 6131 O O . HOH T 9 . ? 13.852 67.824 34.763 1.00 21.85 ? 965 HOH A O 1 HETATM 6132 O O . HOH T 9 . ? 4.366 66.868 51.450 1.00 19.33 ? 966 HOH A O 1 HETATM 6133 O O . HOH T 9 . ? 4.041 68.493 49.219 1.00 20.31 ? 967 HOH A O 1 HETATM 6134 O O . HOH T 9 . ? -4.503 55.100 51.755 1.00 21.10 ? 968 HOH A O 1 HETATM 6135 O O . HOH T 9 . ? 1.270 59.134 46.409 1.00 23.77 ? 969 HOH A O 1 HETATM 6136 O O . HOH T 9 . ? 2.589 33.031 45.285 1.00 21.21 ? 970 HOH A O 1 HETATM 6137 O O . HOH T 9 . ? -3.939 57.514 46.363 1.00 23.64 ? 971 HOH A O 1 HETATM 6138 O O . HOH T 9 . ? 11.137 63.263 58.173 1.00 22.82 ? 972 HOH A O 1 HETATM 6139 O O . HOH T 9 . ? 28.565 53.713 53.180 1.00 21.17 ? 973 HOH A O 1 HETATM 6140 O O . HOH T 9 . ? 13.718 71.239 40.472 1.00 19.19 ? 974 HOH A O 1 HETATM 6141 O O . HOH T 9 . ? 18.900 27.635 34.987 1.00 20.70 ? 975 HOH A O 1 HETATM 6142 O O . HOH T 9 . ? 13.382 77.680 63.500 1.00 29.27 ? 976 HOH A O 1 HETATM 6143 O O . HOH T 9 . ? 34.478 41.659 50.186 1.00 26.74 ? 977 HOH A O 1 HETATM 6144 O O . HOH T 9 . ? 26.334 38.853 36.180 1.00 21.51 ? 978 HOH A O 1 HETATM 6145 O O . HOH T 9 . ? -2.583 59.172 48.463 1.00 22.07 ? 979 HOH A O 1 HETATM 6146 O O . HOH T 9 . ? 8.773 74.498 66.610 1.00 23.84 ? 980 HOH A O 1 HETATM 6147 O O . HOH T 9 . ? 24.277 31.627 28.611 1.00 23.59 ? 981 HOH A O 1 HETATM 6148 O O . HOH T 9 . ? 5.591 62.598 64.979 1.00 24.21 ? 982 HOH A O 1 HETATM 6149 O O . HOH T 9 . ? 14.315 31.787 29.398 1.00 22.66 ? 983 HOH A O 1 HETATM 6150 O O . HOH T 9 . ? 12.061 34.900 53.579 1.00 21.56 ? 984 HOH A O 1 HETATM 6151 O O . HOH T 9 . ? 10.567 37.216 54.380 1.00 26.73 ? 985 HOH A O 1 HETATM 6152 O O . HOH T 9 . ? 21.115 63.357 60.955 1.00 21.93 ? 986 HOH A O 1 HETATM 6153 O O . HOH T 9 . ? 3.539 27.537 41.317 1.00 25.91 ? 987 HOH A O 1 HETATM 6154 O O . HOH T 9 . ? 19.268 60.008 50.149 1.00 23.57 ? 988 HOH A O 1 HETATM 6155 O O . HOH T 9 . ? 20.754 53.109 47.434 1.00 22.45 ? 989 HOH A O 1 HETATM 6156 O O . HOH T 9 . ? 31.252 40.073 46.396 1.00 24.05 ? 990 HOH A O 1 HETATM 6157 O O . HOH T 9 . ? 5.500 77.867 54.424 1.00 21.36 ? 991 HOH A O 1 HETATM 6158 O O . HOH T 9 . ? 32.262 35.062 59.173 1.00 28.46 ? 992 HOH A O 1 HETATM 6159 O O . HOH T 9 . ? 21.754 61.489 36.641 1.00 20.36 ? 993 HOH A O 1 HETATM 6160 O O . HOH T 9 . ? 16.212 72.005 29.649 1.00 20.04 ? 994 HOH A O 1 HETATM 6161 O O . HOH T 9 . ? 14.689 58.842 74.471 1.00 27.69 ? 995 HOH A O 1 HETATM 6162 O O . HOH T 9 . ? 29.418 70.058 45.957 1.00 26.18 ? 996 HOH A O 1 HETATM 6163 O O . HOH T 9 . ? -2.157 55.441 46.142 1.00 19.33 ? 997 HOH A O 1 HETATM 6164 O O . HOH T 9 . ? 23.985 40.530 69.417 1.00 28.48 ? 998 HOH A O 1 HETATM 6165 O O . HOH T 9 . ? 5.682 62.704 70.431 1.00 25.00 ? 999 HOH A O 1 HETATM 6166 O O . HOH T 9 . ? 16.746 68.080 64.257 1.00 23.50 ? 1000 HOH A O 1 HETATM 6167 O O . HOH T 9 . ? 25.075 32.697 67.696 1.00 30.34 ? 1001 HOH A O 1 HETATM 6168 O O . HOH T 9 . ? -6.321 58.606 38.021 1.00 25.87 ? 1002 HOH A O 1 HETATM 6169 O O . HOH T 9 . ? 14.962 61.672 73.070 1.00 26.71 ? 1003 HOH A O 1 HETATM 6170 O O . HOH T 9 . ? 0.262 31.232 58.170 1.00 26.38 ? 1004 HOH A O 1 HETATM 6171 O O . HOH T 9 . ? 18.242 55.361 30.372 1.00 26.26 ? 1005 HOH A O 1 HETATM 6172 O O . HOH T 9 . ? 8.930 68.857 40.901 1.00 21.25 ? 1006 HOH A O 1 HETATM 6173 O O . HOH T 9 . ? 12.045 36.879 28.574 1.00 19.85 ? 1007 HOH A O 1 HETATM 6174 O O . HOH T 9 . ? 0.449 33.260 43.326 1.00 21.78 ? 1008 HOH A O 1 HETATM 6175 O O . HOH T 9 . ? 1.167 63.037 42.971 0.30 8.13 ? 1009 HOH A O 1 HETATM 6176 O O . HOH T 9 . ? 33.925 47.813 59.199 1.00 26.55 ? 1010 HOH A O 1 HETATM 6177 O O . HOH T 9 . ? 17.242 81.547 37.310 1.00 25.26 ? 1011 HOH A O 1 HETATM 6178 O O . HOH T 9 . ? 15.131 68.902 41.504 1.00 28.78 ? 1012 HOH A O 1 HETATM 6179 O O . HOH T 9 . ? 16.429 26.117 34.629 1.00 23.60 ? 1013 HOH A O 1 HETATM 6180 O O . HOH T 9 . ? 23.171 55.171 31.175 1.00 24.64 ? 1014 HOH A O 1 HETATM 6181 O O . HOH T 9 . ? 17.637 82.391 41.128 1.00 29.77 ? 1015 HOH A O 1 HETATM 6182 O O . HOH T 9 . ? 24.046 74.880 54.463 1.00 25.14 ? 1016 HOH A O 1 HETATM 6183 O O . HOH T 9 . ? 23.032 67.350 40.506 1.00 24.55 ? 1017 HOH A O 1 HETATM 6184 O O . HOH T 9 . ? 8.284 51.552 43.285 1.00 24.67 ? 1018 HOH A O 1 HETATM 6185 O O . HOH T 9 . ? 29.943 27.054 33.624 1.00 24.01 ? 1019 HOH A O 1 HETATM 6186 O O . HOH T 9 . ? 6.150 38.609 26.371 1.00 26.07 ? 1020 HOH A O 1 HETATM 6187 O O . HOH T 9 . ? 18.870 68.889 65.689 1.00 28.92 ? 1021 HOH A O 1 HETATM 6188 O O . HOH T 9 . ? 21.810 74.368 60.628 1.00 27.03 ? 1022 HOH A O 1 HETATM 6189 O O . HOH T 9 . ? -2.262 33.884 40.537 1.00 23.98 ? 1023 HOH A O 1 HETATM 6190 O O . HOH T 9 . ? 13.607 82.594 55.739 1.00 27.18 ? 1024 HOH A O 1 HETATM 6191 O O . HOH T 9 . ? 25.726 35.490 68.102 1.00 27.51 ? 1025 HOH A O 1 HETATM 6192 O O . HOH T 9 . ? 23.771 72.964 59.295 1.00 28.81 ? 1026 HOH A O 1 HETATM 6193 O O . HOH T 9 . ? -1.320 61.505 62.245 1.00 27.27 ? 1027 HOH A O 1 HETATM 6194 O O . HOH T 9 . ? 10.115 35.913 69.943 1.00 29.71 ? 1028 HOH A O 1 HETATM 6195 O O . HOH T 9 . ? 14.042 57.414 35.089 1.00 19.53 ? 1029 HOH A O 1 HETATM 6196 O O . HOH T 9 . ? 13.490 29.368 28.418 1.00 23.77 ? 1030 HOH A O 1 HETATM 6197 O O . HOH T 9 . ? 10.852 28.956 40.376 1.00 22.14 ? 1031 HOH A O 1 HETATM 6198 O O . HOH T 9 . ? 11.751 40.865 55.354 1.00 20.07 ? 1032 HOH A O 1 HETATM 6199 O O . HOH T 9 . ? 19.153 63.573 32.097 1.00 28.50 ? 1033 HOH A O 1 HETATM 6200 O O . HOH T 9 . ? 12.560 53.309 35.841 1.00 22.45 ? 1034 HOH A O 1 HETATM 6201 O O . HOH T 9 . ? 23.574 56.931 44.575 1.00 43.02 ? 1035 HOH A O 1 HETATM 6202 O O . HOH T 9 . ? 21.924 61.159 51.681 1.00 26.07 ? 1036 HOH A O 1 HETATM 6203 O O . HOH T 9 . ? 25.754 27.173 24.213 1.00 28.11 ? 1037 HOH A O 1 HETATM 6204 O O . HOH T 9 . ? 25.403 55.966 37.307 1.00 27.77 ? 1038 HOH A O 1 HETATM 6205 O O . HOH T 9 . ? 20.091 31.330 26.173 1.00 29.44 ? 1039 HOH A O 1 HETATM 6206 O O . HOH T 9 . ? 30.956 52.386 53.008 1.00 25.72 ? 1040 HOH A O 1 HETATM 6207 O O . HOH T 9 . ? 6.543 76.181 67.254 1.00 28.74 ? 1041 HOH A O 1 HETATM 6208 O O . HOH T 9 . ? 10.506 55.407 75.191 1.00 30.62 ? 1042 HOH A O 1 HETATM 6209 O O . HOH T 9 . ? 21.248 32.364 28.569 1.00 23.82 ? 1043 HOH A O 1 HETATM 6210 O O . HOH T 9 . ? 25.319 70.436 31.231 1.00 24.58 ? 1044 HOH A O 1 HETATM 6211 O O . HOH T 9 . ? 19.045 69.458 28.430 1.00 25.41 ? 1045 HOH A O 1 HETATM 6212 O O . HOH T 9 . ? 23.501 78.793 50.518 1.00 26.07 ? 1046 HOH A O 1 HETATM 6213 O O . HOH T 9 . ? -9.695 45.950 34.217 1.00 34.70 ? 1047 HOH A O 1 HETATM 6214 O O . HOH T 9 . ? 29.089 40.229 64.816 1.00 27.11 ? 1048 HOH A O 1 HETATM 6215 O O . HOH T 9 . ? 11.519 27.661 29.227 1.00 30.49 ? 1049 HOH A O 1 HETATM 6216 O O . HOH T 9 . ? 25.304 63.239 49.888 1.00 28.09 ? 1050 HOH A O 1 HETATM 6217 O O . HOH T 9 . ? 16.188 29.028 27.978 1.00 25.86 ? 1051 HOH A O 1 HETATM 6218 O O . HOH T 9 . ? 13.792 79.705 67.886 1.00 31.96 ? 1052 HOH A O 1 HETATM 6219 O O . HOH T 9 . ? 4.974 31.536 30.186 1.00 39.39 ? 1053 HOH A O 1 HETATM 6220 O O . HOH T 9 . ? 14.348 81.188 40.817 1.00 35.47 ? 1054 HOH A O 1 HETATM 6221 O O . HOH T 9 . ? 10.280 80.892 63.583 1.00 29.74 ? 1055 HOH A O 1 HETATM 6222 O O . HOH T 9 . ? 4.134 63.351 72.673 1.00 27.32 ? 1056 HOH A O 1 HETATM 6223 O O . HOH T 9 . ? -10.414 48.537 48.584 1.00 27.23 ? 1057 HOH A O 1 HETATM 6224 O O . HOH T 9 . ? 21.690 83.877 47.215 1.00 32.30 ? 1058 HOH A O 1 HETATM 6225 O O . HOH T 9 . ? 18.121 21.188 38.847 1.00 39.33 ? 1059 HOH A O 1 HETATM 6226 O O . HOH T 9 . ? 27.255 53.932 50.744 1.00 24.42 ? 1060 HOH A O 1 HETATM 6227 O O . HOH T 9 . ? 7.471 38.499 29.276 1.00 24.81 ? 1061 HOH A O 1 HETATM 6228 O O . HOH T 9 . ? 38.060 34.282 26.309 1.00 37.04 ? 1062 HOH A O 1 HETATM 6229 O O . HOH T 9 . ? 4.789 61.979 75.125 1.00 27.24 ? 1063 HOH A O 1 HETATM 6230 O O . HOH T 9 . ? -1.744 32.176 44.677 1.00 32.81 ? 1064 HOH A O 1 HETATM 6231 O O . HOH T 9 . ? -10.158 43.713 46.989 1.00 32.21 ? 1065 HOH A O 1 HETATM 6232 O O . HOH T 9 . ? 29.342 54.365 34.478 1.00 29.87 ? 1066 HOH A O 1 HETATM 6233 O O . HOH T 9 . ? 11.708 47.519 37.308 1.00 17.91 ? 1067 HOH A O 1 HETATM 6234 O O . HOH T 9 . ? -0.725 58.054 43.304 1.00 20.48 ? 1068 HOH A O 1 HETATM 6235 O O . HOH T 9 . ? 22.579 58.343 24.230 1.00 28.59 ? 1069 HOH A O 1 HETATM 6236 O O . HOH T 9 . ? -2.943 38.502 63.116 1.00 35.38 ? 1070 HOH A O 1 HETATM 6237 O O . HOH T 9 . ? 11.641 38.290 56.600 1.00 29.34 ? 1071 HOH A O 1 HETATM 6238 O O . HOH T 9 . ? 25.599 66.823 30.062 1.00 25.45 ? 1072 HOH A O 1 HETATM 6239 O O . HOH T 9 . ? 16.539 69.189 20.735 1.00 41.91 ? 1073 HOH A O 1 HETATM 6240 O O . HOH T 9 . ? 11.996 63.608 35.497 1.00 27.40 ? 1074 HOH A O 1 HETATM 6241 O O . HOH T 9 . ? 25.183 65.741 40.015 1.00 36.94 ? 1075 HOH A O 1 HETATM 6242 O O . HOH T 9 . ? 31.686 55.184 26.101 1.00 35.83 ? 1076 HOH A O 1 HETATM 6243 O O . HOH T 9 . ? 18.005 30.879 29.036 1.00 22.97 ? 1077 HOH A O 1 HETATM 6244 O O . HOH T 9 . ? 28.895 26.036 36.032 1.00 28.27 ? 1078 HOH A O 1 HETATM 6245 O O . HOH T 9 . ? 16.724 79.535 21.058 1.00 39.32 ? 1079 HOH A O 1 HETATM 6246 O O . HOH T 9 . ? 19.947 25.537 36.780 1.00 23.00 ? 1080 HOH A O 1 HETATM 6247 O O . HOH T 9 . ? 27.897 45.092 68.976 1.00 28.04 ? 1081 HOH A O 1 HETATM 6248 O O . HOH T 9 . ? 17.759 52.189 75.082 1.00 35.26 ? 1082 HOH A O 1 HETATM 6249 O O . HOH T 9 . ? 0.398 33.461 36.430 1.00 38.55 ? 1083 HOH A O 1 HETATM 6250 O O . HOH T 9 . ? 25.569 25.465 19.933 1.00 29.67 ? 1084 HOH A O 1 HETATM 6251 O O . HOH T 9 . ? 20.563 30.140 29.801 1.00 28.90 ? 1085 HOH A O 1 HETATM 6252 O O . HOH T 9 . ? 12.838 69.329 32.628 1.00 27.15 ? 1086 HOH A O 1 HETATM 6253 O O . HOH T 9 . ? 24.544 29.433 30.323 1.00 27.05 ? 1087 HOH A O 1 HETATM 6254 O O . HOH T 9 . ? -2.657 32.619 55.842 0.60 25.01 ? 1088 HOH A O 1 HETATM 6255 O O . HOH T 9 . ? 24.098 82.072 42.228 1.00 34.85 ? 1089 HOH A O 1 HETATM 6256 O O . HOH T 9 . ? 29.247 78.903 27.461 1.00 32.45 ? 1090 HOH A O 1 HETATM 6257 O O . HOH T 9 . ? 10.425 27.025 51.552 1.00 25.88 ? 1091 HOH A O 1 HETATM 6258 O O . HOH T 9 . ? 4.970 40.063 23.174 1.00 29.96 ? 1092 HOH A O 1 HETATM 6259 O O . HOH T 9 . ? 36.099 42.782 57.648 1.00 30.99 ? 1093 HOH A O 1 HETATM 6260 O O . HOH T 9 . ? 36.673 52.000 68.861 1.00 30.19 ? 1094 HOH A O 1 HETATM 6261 O O . HOH T 9 . ? 9.910 69.698 38.513 1.00 27.00 ? 1095 HOH A O 1 HETATM 6262 O O . HOH T 9 . ? 22.741 65.208 66.111 1.00 33.20 ? 1096 HOH A O 1 HETATM 6263 O O . HOH T 9 . ? 26.997 56.874 70.496 1.00 31.59 ? 1097 HOH A O 1 HETATM 6264 O O . HOH T 9 . ? 6.954 75.671 37.666 1.00 23.60 ? 1098 HOH A O 1 HETATM 6265 O O . HOH T 9 . ? 39.729 43.695 58.531 1.00 34.50 ? 1099 HOH A O 1 HETATM 6266 O O . HOH T 9 . ? 26.830 16.710 40.136 1.00 44.57 ? 1100 HOH A O 1 HETATM 6267 O O . HOH T 9 . ? 27.954 71.787 52.668 1.00 35.28 ? 1101 HOH A O 1 HETATM 6268 O O . HOH T 9 . ? 4.975 31.324 24.427 1.00 33.68 ? 1102 HOH A O 1 HETATM 6269 O O . HOH T 9 . ? 26.298 60.129 30.551 1.00 34.67 ? 1103 HOH A O 1 HETATM 6270 O O . HOH T 9 . ? -1.714 45.973 55.683 1.00 35.26 ? 1104 HOH A O 1 HETATM 6271 O O . HOH T 9 . ? 1.626 30.870 64.723 0.80 29.46 ? 1105 HOH A O 1 HETATM 6272 O O . HOH T 9 . ? 21.429 25.085 23.755 1.00 32.67 ? 1106 HOH A O 1 HETATM 6273 O O . HOH T 9 . ? 23.866 61.245 34.675 1.00 26.07 ? 1107 HOH A O 1 HETATM 6274 O O . HOH T 9 . ? 11.111 76.500 28.505 1.00 29.37 ? 1108 HOH A O 1 HETATM 6275 O O . HOH T 9 . ? 26.314 23.430 45.630 1.00 31.20 ? 1109 HOH A O 1 HETATM 6276 O O . HOH T 9 . ? 20.381 43.941 11.334 1.00 37.22 ? 1110 HOH A O 1 HETATM 6277 O O A HOH T 9 . ? -3.977 37.229 56.363 0.70 29.66 ? 1111 HOH A O 1 HETATM 6278 O O B HOH T 9 . ? -4.590 35.334 55.733 0.30 30.09 ? 1111 HOH A O 1 HETATM 6279 O O . HOH T 9 . ? 16.031 67.186 72.541 1.00 41.89 ? 1112 HOH A O 1 HETATM 6280 O O . HOH T 9 . ? 11.486 48.746 29.547 1.00 19.76 ? 1113 HOH A O 1 HETATM 6281 O O . HOH T 9 . ? 5.365 65.986 33.804 1.00 36.75 ? 1114 HOH A O 1 HETATM 6282 O O . HOH T 9 . ? -2.878 37.813 32.524 1.00 28.96 ? 1115 HOH A O 1 HETATM 6283 O O . HOH T 9 . ? 24.229 77.569 52.981 1.00 32.65 ? 1116 HOH A O 1 HETATM 6284 O O . HOH T 9 . ? 20.871 74.331 23.657 1.00 32.80 ? 1117 HOH A O 1 HETATM 6285 O O . HOH T 9 . ? 10.138 51.605 39.997 1.00 15.63 ? 1118 HOH A O 1 HETATM 6286 O O . HOH T 9 . ? 30.664 84.005 28.501 1.00 34.60 ? 1119 HOH A O 1 HETATM 6287 O O . HOH T 9 . ? 0.450 63.066 48.126 1.00 32.16 ? 1120 HOH A O 1 HETATM 6288 O O . HOH T 9 . ? 26.520 66.006 26.242 1.00 29.60 ? 1121 HOH A O 1 HETATM 6289 O O . HOH T 9 . ? -4.314 53.122 37.192 1.00 30.33 ? 1122 HOH A O 1 HETATM 6290 O O . HOH T 9 . ? 28.556 44.348 65.457 1.00 34.16 ? 1123 HOH A O 1 HETATM 6291 O O . HOH T 9 . ? 8.394 82.291 51.945 1.00 29.23 ? 1124 HOH A O 1 HETATM 6292 O O . HOH T 9 . ? 32.959 29.961 24.288 1.00 38.29 ? 1125 HOH A O 1 HETATM 6293 O O . HOH T 9 . ? 14.921 52.535 34.695 1.00 22.72 ? 1126 HOH A O 1 HETATM 6294 O O . HOH T 9 . ? 15.164 24.473 58.404 1.00 35.37 ? 1127 HOH A O 1 HETATM 6295 O O . HOH T 9 . ? 4.243 43.573 75.886 1.00 36.95 ? 1128 HOH A O 1 HETATM 6296 O O . HOH T 9 . ? 9.080 51.995 75.205 1.00 43.36 ? 1129 HOH A O 1 HETATM 6297 O O . HOH T 9 . ? 18.783 65.921 27.881 1.00 32.75 ? 1130 HOH A O 1 HETATM 6298 O O . HOH T 9 . ? 17.930 32.095 70.467 1.00 33.14 ? 1131 HOH A O 1 HETATM 6299 O O . HOH T 9 . ? 13.838 50.222 18.894 1.00 30.85 ? 1132 HOH A O 1 HETATM 6300 O O . HOH T 9 . ? 17.641 65.179 30.390 1.00 27.14 ? 1133 HOH A O 1 HETATM 6301 O O . HOH T 9 . ? 25.915 24.832 57.492 1.00 33.02 ? 1134 HOH A O 1 HETATM 6302 O O . HOH T 9 . ? 29.243 69.575 39.557 1.00 34.79 ? 1135 HOH A O 1 HETATM 6303 O O . HOH T 9 . ? 3.621 27.176 54.629 1.00 31.41 ? 1136 HOH A O 1 HETATM 6304 O O . HOH T 9 . ? 14.970 81.477 28.321 1.00 35.92 ? 1137 HOH A O 1 HETATM 6305 O O . HOH T 9 . ? -4.527 53.774 34.612 1.00 33.69 ? 1138 HOH A O 1 HETATM 6306 O O . HOH T 9 . ? 21.541 75.140 67.002 1.00 40.02 ? 1139 HOH A O 1 HETATM 6307 O O . HOH T 9 . ? 21.308 88.337 44.331 1.00 29.45 ? 1140 HOH A O 1 HETATM 6308 O O . HOH T 9 . ? -4.343 36.993 51.356 1.00 45.77 ? 1141 HOH A O 1 HETATM 6309 O O . HOH T 9 . ? 13.859 65.074 35.775 1.00 37.39 ? 1142 HOH A O 1 HETATM 6310 O O . HOH T 9 . ? 33.893 40.173 47.341 1.00 33.83 ? 1143 HOH A O 1 HETATM 6311 O O . HOH T 9 . ? 11.949 49.938 36.343 1.00 17.31 ? 1144 HOH A O 1 HETATM 6312 O O . HOH T 9 . ? 31.043 31.735 16.968 0.80 28.91 ? 1145 HOH A O 1 HETATM 6313 O O . HOH T 9 . ? 30.133 59.657 25.009 0.50 23.57 ? 1146 HOH A O 1 HETATM 6314 O O . HOH T 9 . ? 12.176 43.583 17.176 1.00 31.85 ? 1147 HOH A O 1 HETATM 6315 O O . HOH T 9 . ? 26.639 69.163 29.065 1.00 29.79 ? 1148 HOH A O 1 HETATM 6316 O O . HOH T 9 . ? -5.092 41.929 50.504 1.00 36.57 ? 1149 HOH A O 1 HETATM 6317 O O . HOH T 9 . ? 36.651 43.281 49.501 1.00 40.84 ? 1150 HOH A O 1 HETATM 6318 O O . HOH T 9 . ? -3.348 46.996 53.095 1.00 35.85 ? 1151 HOH A O 1 HETATM 6319 O O A HOH T 9 . ? -6.478 42.208 46.738 0.50 28.20 ? 1152 HOH A O 1 HETATM 6320 O O B HOH T 9 . ? -5.598 43.814 47.347 0.50 27.14 ? 1152 HOH A O 1 HETATM 6321 O O . HOH T 9 . ? -0.807 32.301 60.613 1.00 41.04 ? 1153 HOH A O 1 HETATM 6322 O O . HOH T 9 . ? 16.137 79.222 69.260 1.00 41.05 ? 1154 HOH A O 1 HETATM 6323 O O . HOH T 9 . ? -8.776 41.381 48.063 1.00 37.25 ? 1155 HOH A O 1 HETATM 6324 O O . HOH T 9 . ? 19.648 55.914 22.941 1.00 30.38 ? 1156 HOH A O 1 HETATM 6325 O O . HOH T 9 . ? 32.418 42.737 19.993 1.00 33.92 ? 1157 HOH A O 1 HETATM 6326 O O . HOH T 9 . ? 21.327 23.992 51.062 1.00 37.25 ? 1158 HOH A O 1 HETATM 6327 O O . HOH T 9 . ? 27.269 20.209 39.875 1.00 30.00 ? 1159 HOH A O 1 HETATM 6328 O O . HOH T 9 . ? 5.578 81.526 53.919 1.00 33.44 ? 1160 HOH A O 1 HETATM 6329 O O . HOH T 9 . ? 8.271 29.272 33.425 1.00 39.43 ? 1161 HOH A O 1 HETATM 6330 O O . HOH T 9 . ? -1.066 51.440 72.529 0.50 21.21 ? 1162 HOH A O 1 HETATM 6331 O O . HOH T 9 . ? 9.008 56.455 43.775 1.00 17.41 ? 1163 HOH A O 1 HETATM 6332 O O . HOH T 9 . ? 23.006 75.591 25.550 1.00 33.85 ? 1164 HOH A O 1 HETATM 6333 O O . HOH T 9 . ? 6.001 68.228 37.106 1.00 32.42 ? 1165 HOH A O 1 HETATM 6334 O O . HOH T 9 . ? 38.742 55.043 62.453 1.00 42.13 ? 1166 HOH A O 1 HETATM 6335 O O . HOH T 9 . ? 12.969 71.708 80.013 1.00 39.60 ? 1167 HOH A O 1 HETATM 6336 O O . HOH T 9 . ? 11.717 80.879 61.172 1.00 35.09 ? 1168 HOH A O 1 HETATM 6337 O O . HOH T 9 . ? 1.416 36.869 68.668 1.00 33.13 ? 1169 HOH A O 1 HETATM 6338 O O . HOH T 9 . ? 12.981 32.786 70.824 1.00 34.76 ? 1170 HOH A O 1 HETATM 6339 O O . HOH T 9 . ? 18.788 40.275 75.907 1.00 35.14 ? 1171 HOH A O 1 HETATM 6340 O O . HOH T 9 . ? 20.097 45.591 79.023 1.00 37.12 ? 1172 HOH A O 1 HETATM 6341 O O . HOH T 9 . ? 5.797 56.093 35.872 1.00 20.75 ? 1173 HOH A O 1 HETATM 6342 O O . HOH T 9 . ? 23.338 59.984 39.595 1.00 27.45 ? 1174 HOH A O 1 HETATM 6343 O O . HOH T 9 . ? 30.618 71.323 43.632 1.00 34.33 ? 1175 HOH A O 1 HETATM 6344 O O . HOH T 9 . ? 8.582 74.759 75.387 1.00 35.12 ? 1176 HOH A O 1 HETATM 6345 O O . HOH T 9 . ? 2.892 38.341 26.990 1.00 35.96 ? 1177 HOH A O 1 HETATM 6346 O O . HOH T 9 . ? 38.479 43.008 55.492 1.00 40.32 ? 1178 HOH A O 1 HETATM 6347 O O . HOH T 9 . ? 25.337 85.720 42.704 1.00 28.71 ? 1179 HOH A O 1 HETATM 6348 O O . HOH T 9 . ? 11.858 56.331 31.454 1.00 36.28 ? 1180 HOH A O 1 HETATM 6349 O O . HOH T 9 . ? 21.924 80.643 22.832 1.00 37.65 ? 1181 HOH A O 1 HETATM 6350 O O . HOH T 9 . ? 13.605 55.026 32.757 1.00 28.39 ? 1182 HOH A O 1 HETATM 6351 O O . HOH T 9 . ? 28.219 53.393 37.121 0.50 27.02 ? 1183 HOH A O 1 HETATM 6352 O O . HOH T 9 . ? 24.914 23.052 53.012 1.00 37.92 ? 1184 HOH A O 1 HETATM 6353 O O . HOH T 9 . ? 25.226 66.430 56.681 1.00 33.44 ? 1185 HOH A O 1 HETATM 6354 O O . HOH T 9 . ? 15.293 25.456 29.904 0.50 25.48 ? 1186 HOH A O 1 HETATM 6355 O O . HOH T 9 . ? 6.454 42.717 27.145 1.00 33.90 ? 1187 HOH A O 1 HETATM 6356 O O . HOH T 9 . ? 35.038 43.841 68.324 1.00 42.12 ? 1188 HOH A O 1 HETATM 6357 O O . HOH T 9 . ? 9.601 74.765 69.481 0.35 22.19 ? 1189 HOH A O 1 HETATM 6358 O O . HOH T 9 . ? 10.488 84.018 51.211 1.00 33.79 ? 1190 HOH A O 1 HETATM 6359 O O . HOH T 9 . ? 25.084 64.655 44.491 0.50 19.52 ? 1191 HOH A O 1 HETATM 6360 O O . HOH T 9 . ? 25.013 56.779 32.223 1.00 36.39 ? 1192 HOH A O 1 HETATM 6361 O O . HOH T 9 . ? 39.246 57.406 58.182 1.00 38.52 ? 1193 HOH A O 1 HETATM 6362 O O . HOH T 9 . ? 8.719 54.410 31.341 1.00 30.85 ? 1194 HOH A O 1 HETATM 6363 O O . HOH T 9 . ? 23.657 24.391 30.297 1.00 41.31 ? 1195 HOH A O 1 HETATM 6364 O O . HOH T 9 . ? 5.996 44.768 25.607 1.00 38.71 ? 1196 HOH A O 1 HETATM 6365 O O . HOH T 9 . ? 17.383 25.764 59.401 1.00 29.33 ? 1197 HOH A O 1 HETATM 6366 O O . HOH T 9 . ? 2.514 63.169 40.592 1.00 31.91 ? 1198 HOH A O 1 HETATM 6367 O O . HOH T 9 . ? 22.736 58.696 21.393 1.00 39.02 ? 1199 HOH A O 1 HETATM 6368 O O . HOH T 9 . ? -4.213 44.010 27.137 1.00 46.91 ? 1200 HOH A O 1 HETATM 6369 O O . HOH T 9 . ? 21.224 23.951 26.903 0.50 28.14 ? 1201 HOH A O 1 HETATM 6370 O O . HOH T 9 . ? 22.173 83.349 49.914 1.00 38.81 ? 1202 HOH A O 1 HETATM 6371 O O . HOH T 9 . ? 24.923 67.942 63.115 0.40 23.60 ? 1203 HOH A O 1 HETATM 6372 O O . HOH T 9 . ? -5.133 44.400 30.857 1.00 40.72 ? 1204 HOH A O 1 HETATM 6373 O O . HOH T 9 . ? 26.936 64.768 34.724 0.40 22.50 ? 1205 HOH A O 1 HETATM 6374 O O . HOH T 9 . ? 17.650 64.354 67.299 0.50 24.95 ? 1206 HOH A O 1 HETATM 6375 O O . HOH T 9 . ? 33.600 53.354 31.688 1.00 39.71 ? 1207 HOH A O 1 HETATM 6376 O O . HOH T 9 . ? 2.922 64.736 50.930 1.00 26.38 ? 1208 HOH A O 1 HETATM 6377 O O . HOH T 9 . ? 4.048 71.779 36.204 1.00 32.02 ? 1209 HOH A O 1 HETATM 6378 O O . HOH T 9 . ? 9.351 28.597 37.965 1.00 34.70 ? 1210 HOH A O 1 HETATM 6379 O O . HOH T 9 . ? 15.171 24.839 32.433 1.00 37.67 ? 1211 HOH A O 1 HETATM 6380 O O . HOH T 9 . ? -1.820 63.434 48.906 1.00 31.16 ? 1212 HOH A O 1 HETATM 6381 O O . HOH T 9 . ? 28.972 25.709 31.427 1.00 35.29 ? 1213 HOH A O 1 HETATM 6382 O O . HOH T 9 . ? 26.736 64.672 28.735 1.00 34.19 ? 1214 HOH A O 1 HETATM 6383 O O . HOH T 9 . ? 25.523 67.905 32.647 1.00 27.68 ? 1215 HOH A O 1 HETATM 6384 O O . HOH T 9 . ? 29.577 67.261 45.429 1.00 39.34 ? 1216 HOH A O 1 HETATM 6385 O O . HOH T 9 . ? 34.937 35.541 58.316 1.00 45.16 ? 1217 HOH A O 1 HETATM 6386 O O . HOH T 9 . ? 21.097 56.481 25.143 1.00 30.97 ? 1218 HOH A O 1 HETATM 6387 O O . HOH T 9 . ? 28.331 35.786 67.284 0.50 27.85 ? 1219 HOH A O 1 HETATM 6388 O O . HOH T 9 . ? 29.613 37.731 66.195 1.00 38.81 ? 1220 HOH A O 1 HETATM 6389 O O . HOH T 9 . ? 13.958 80.385 62.925 1.00 36.65 ? 1221 HOH A O 1 HETATM 6390 O O . HOH T 9 . ? 12.068 73.546 81.589 0.40 20.03 ? 1222 HOH A O 1 HETATM 6391 O O . HOH T 9 . ? 34.932 49.123 33.081 0.50 22.59 ? 1223 HOH A O 1 HETATM 6392 O O . HOH T 9 . ? 14.810 69.844 81.801 1.00 38.80 ? 1224 HOH A O 1 HETATM 6393 O O . HOH T 9 . ? 4.826 50.036 28.261 1.00 31.81 ? 1225 HOH A O 1 HETATM 6394 O O . HOH T 9 . ? 23.506 74.358 65.492 1.00 38.75 ? 1226 HOH A O 1 HETATM 6395 O O . HOH T 9 . ? 16.506 84.646 40.886 1.00 40.15 ? 1227 HOH A O 1 HETATM 6396 O O . HOH T 9 . ? -1.959 44.425 58.691 1.00 42.28 ? 1228 HOH A O 1 HETATM 6397 O O . HOH T 9 . ? -5.453 34.031 47.559 1.00 35.06 ? 1229 HOH A O 1 HETATM 6398 O O . HOH T 9 . ? 12.468 50.186 27.344 1.00 28.41 ? 1230 HOH A O 1 HETATM 6399 O O . HOH T 9 . ? 17.936 58.163 29.787 1.00 35.34 ? 1231 HOH A O 1 HETATM 6400 O O . HOH T 9 . ? 16.633 70.854 79.145 0.50 26.51 ? 1232 HOH A O 1 HETATM 6401 O O . HOH T 9 . ? 15.833 82.296 57.599 1.00 44.93 ? 1233 HOH A O 1 HETATM 6402 O O . HOH T 9 . ? 10.844 41.022 17.425 1.00 36.03 ? 1234 HOH A O 1 HETATM 6403 O O . HOH T 9 . ? 19.021 53.903 73.066 1.00 46.99 ? 1235 HOH A O 1 HETATM 6404 O O . HOH T 9 . ? 25.993 74.343 58.282 1.00 39.62 ? 1236 HOH A O 1 HETATM 6405 O O . HOH T 9 . ? 30.041 42.068 66.482 1.00 37.74 ? 1237 HOH A O 1 HETATM 6406 O O . HOH T 9 . ? 28.664 64.281 25.511 1.00 34.48 ? 1238 HOH A O 1 HETATM 6407 O O . HOH T 9 . ? 26.374 74.628 55.609 1.00 40.97 ? 1239 HOH A O 1 HETATM 6408 O O . HOH T 9 . ? -9.304 45.698 48.591 1.00 41.56 ? 1240 HOH A O 1 HETATM 6409 O O . HOH T 9 . ? 24.583 59.787 32.394 1.00 40.17 ? 1241 HOH A O 1 HETATM 6410 O O . HOH T 9 . ? -3.504 46.503 24.923 1.00 39.42 ? 1242 HOH A O 1 HETATM 6411 O O . HOH T 9 . ? -10.689 43.509 38.545 1.00 43.22 ? 1243 HOH A O 1 HETATM 6412 O O . HOH T 9 . ? 1.893 66.509 37.269 1.00 46.97 ? 1244 HOH A O 1 HETATM 6413 O O . HOH T 9 . ? -5.560 50.769 28.495 1.00 39.68 ? 1245 HOH A O 1 HETATM 6414 O O . HOH T 9 . ? 28.198 41.656 68.693 1.00 46.16 ? 1246 HOH A O 1 HETATM 6415 O O . HOH T 9 . ? 19.863 57.753 27.381 1.00 36.27 ? 1247 HOH A O 1 HETATM 6416 O O . HOH T 9 . ? 13.944 68.542 75.390 1.00 34.32 ? 1248 HOH A O 1 HETATM 6417 O O . HOH T 9 . ? 33.453 54.262 28.056 0.50 29.70 ? 1249 HOH A O 1 HETATM 6418 O O . HOH T 9 . ? 30.529 25.802 38.104 1.00 38.73 ? 1250 HOH A O 1 HETATM 6419 O O . HOH T 9 . ? 35.674 33.706 54.648 0.80 41.04 ? 1251 HOH A O 1 HETATM 6420 O O . HOH T 9 . ? 38.761 38.519 64.816 0.50 31.15 ? 1252 HOH A O 1 HETATM 6421 O O . HOH T 9 . ? 5.883 53.601 30.091 1.00 29.11 ? 1253 HOH A O 1 HETATM 6422 O O . HOH T 9 . ? -0.079 60.260 48.389 1.00 29.13 ? 1254 HOH A O 1 HETATM 6423 O O . HOH T 9 . ? 9.897 75.729 30.966 1.00 36.15 ? 1255 HOH A O 1 HETATM 6424 O O . HOH T 9 . ? 7.981 56.341 75.697 1.00 29.77 ? 1256 HOH A O 1 HETATM 6425 O O . HOH T 9 . ? 6.733 53.645 75.436 1.00 31.30 ? 1257 HOH A O 1 HETATM 6426 O O . HOH T 9 . ? 11.319 52.513 28.012 1.00 38.74 ? 1258 HOH A O 1 HETATM 6427 O O . HOH T 9 . ? 29.734 60.714 52.916 1.00 37.15 ? 1259 HOH A O 1 HETATM 6428 O O . HOH T 9 . ? 36.451 46.429 31.575 0.50 24.10 ? 1260 HOH A O 1 HETATM 6429 O O . HOH T 9 . ? 3.815 63.760 34.794 1.00 37.45 ? 1261 HOH A O 1 HETATM 6430 O O . HOH T 9 . ? 17.419 58.992 44.814 1.00 22.36 ? 1262 HOH A O 1 HETATM 6431 O O . HOH T 9 . ? 26.813 30.935 63.625 1.00 42.43 ? 1263 HOH A O 1 HETATM 6432 O O . HOH T 9 . ? 29.464 28.031 59.259 1.00 45.05 ? 1264 HOH A O 1 HETATM 6433 O O . HOH T 9 . ? 12.577 28.519 60.609 1.00 45.28 ? 1265 HOH A O 1 HETATM 6434 O O . HOH T 9 . ? -6.678 44.824 49.606 1.00 47.90 ? 1266 HOH A O 1 HETATM 6435 O O . HOH T 9 . ? -7.583 41.631 40.897 1.00 34.33 ? 1267 HOH A O 1 HETATM 6436 O O . HOH T 9 . ? -6.098 41.462 44.212 1.00 35.06 ? 1268 HOH A O 1 HETATM 6437 O O . HOH T 9 . ? 42.239 34.853 37.689 1.00 47.71 ? 1269 HOH A O 1 HETATM 6438 O O . HOH T 9 . ? 34.226 32.616 27.277 1.00 33.73 ? 1270 HOH A O 1 HETATM 6439 O O . HOH T 9 . ? 26.477 42.069 40.871 1.00 28.50 ? 1271 HOH A O 1 HETATM 6440 O O . HOH T 9 . ? 22.440 45.255 40.976 1.00 24.00 ? 1272 HOH A O 1 HETATM 6441 O O . HOH T 9 . ? 25.830 25.764 46.337 1.00 33.22 ? 1273 HOH A O 1 HETATM 6442 O O . HOH T 9 . ? 37.526 28.548 38.930 1.00 44.32 ? 1274 HOH A O 1 HETATM 6443 O O . HOH T 9 . ? 23.406 68.565 69.018 1.00 44.60 ? 1275 HOH A O 1 HETATM 6444 O O . HOH T 9 . ? -12.804 47.342 37.572 1.00 30.29 ? 1276 HOH A O 1 HETATM 6445 O O . HOH T 9 . ? 24.131 45.469 38.742 1.00 27.91 ? 1277 HOH A O 1 HETATM 6446 O O . HOH T 9 . ? 24.934 47.903 37.572 0.75 37.06 ? 1278 HOH A O 1 HETATM 6447 O O . HOH T 9 . ? 26.214 40.002 13.369 1.00 31.72 ? 1279 HOH A O 1 HETATM 6448 O O . HOH T 9 . ? 20.767 50.265 76.121 1.00 35.60 ? 1280 HOH A O 1 HETATM 6449 O O . HOH T 9 . ? 19.435 49.779 45.376 1.00 40.15 ? 1281 HOH A O 1 HETATM 6450 O O . HOH T 9 . ? -0.122 63.629 61.961 1.00 45.21 ? 1282 HOH A O 1 HETATM 6451 O O . HOH T 9 . ? 25.731 43.605 38.624 1.00 37.54 ? 1283 HOH A O 1 HETATM 6452 O O . HOH T 9 . ? 34.518 41.203 19.210 1.00 34.79 ? 1284 HOH A O 1 HETATM 6453 O O . HOH T 9 . ? 34.324 45.836 70.018 0.35 22.41 ? 1285 HOH A O 1 HETATM 6454 O O . HOH T 9 . ? 16.673 63.293 68.896 0.50 23.75 ? 1286 HOH A O 1 HETATM 6455 O O . HOH T 9 . ? 34.809 50.988 30.918 1.00 39.99 ? 1287 HOH A O 1 HETATM 6456 O O . HOH T 9 . ? 24.291 43.690 42.226 1.00 29.89 ? 1288 HOH A O 1 HETATM 6457 O O . HOH T 9 . ? 11.691 28.992 19.040 1.00 42.69 ? 1289 HOH A O 1 HETATM 6458 O O . HOH T 9 . ? 21.703 51.998 44.981 1.00 39.56 ? 1290 HOH A O 1 HETATM 6459 O O . HOH T 9 . ? 28.671 48.200 38.122 1.00 40.56 ? 1291 HOH A O 1 HETATM 6460 O O . HOH T 9 . ? 9.861 97.165 40.114 1.00 32.55 ? 1292 HOH A O 1 HETATM 6461 O O . HOH T 9 . ? 30.753 35.430 16.732 1.00 36.62 ? 1293 HOH A O 1 HETATM 6462 O O . HOH T 9 . ? 2.193 33.324 24.154 1.00 50.81 ? 1294 HOH A O 1 HETATM 6463 O O . HOH T 9 . ? 20.956 79.467 65.413 0.25 22.20 ? 1295 HOH A O 1 HETATM 6464 O O . HOH T 9 . ? 26.066 59.473 47.297 1.00 40.90 ? 1296 HOH A O 1 HETATM 6465 O O . HOH T 9 . ? 35.265 56.014 51.346 1.00 39.06 ? 1297 HOH A O 1 HETATM 6466 O O A HOH T 9 . ? 15.112 57.284 32.113 0.50 24.71 ? 1298 HOH A O 1 HETATM 6467 O O B HOH T 9 . ? 13.745 58.819 32.580 0.50 25.86 ? 1298 HOH A O 1 HETATM 6468 O O . HOH T 9 . ? 25.626 62.959 38.664 1.00 33.38 ? 1299 HOH A O 1 HETATM 6469 O O . HOH T 9 . ? 36.773 48.402 29.961 1.00 40.63 ? 1300 HOH A O 1 HETATM 6470 O O . HOH T 9 . ? 25.359 74.498 21.978 1.00 47.70 ? 1301 HOH A O 1 HETATM 6471 O O . HOH T 9 . ? 34.446 36.208 54.865 1.00 39.72 ? 1302 HOH A O 1 HETATM 6472 O O . HOH T 9 . ? 31.024 69.587 41.679 1.00 38.09 ? 1303 HOH A O 1 HETATM 6473 O O . HOH T 9 . ? 30.281 75.588 43.191 1.00 50.66 ? 1304 HOH A O 1 HETATM 6474 O O . HOH T 9 . ? 13.270 27.897 17.008 1.00 39.88 ? 1305 HOH A O 1 HETATM 6475 O O . HOH T 9 . ? 33.849 28.887 34.110 1.00 39.83 ? 1306 HOH A O 1 HETATM 6476 O O . HOH T 9 . ? 14.110 54.684 37.369 0.50 19.71 ? 1307 HOH A O 1 HETATM 6477 O O . HOH T 9 . ? 22.291 80.408 57.328 0.25 14.84 ? 1308 HOH A O 1 HETATM 6478 O O . HOH T 9 . ? 21.903 58.527 69.764 1.00 60.75 ? 1309 HOH A O 1 HETATM 6479 O O . HOH T 9 . ? 12.118 27.582 21.454 1.00 41.03 ? 1310 HOH A O 1 HETATM 6480 O O . HOH T 9 . ? 14.506 96.355 45.505 1.00 41.10 ? 1311 HOH A O 1 HETATM 6481 O O A HOH T 9 . ? 37.093 41.799 37.708 0.50 27.26 ? 1312 HOH A O 1 HETATM 6482 O O B HOH T 9 . ? 38.451 43.128 38.721 0.50 35.72 ? 1312 HOH A O 1 HETATM 6483 O O . HOH T 9 . ? 13.889 61.455 32.954 1.00 34.61 ? 1313 HOH A O 1 HETATM 6484 O O . HOH T 9 . ? 29.275 72.571 50.038 1.00 40.94 ? 1314 HOH A O 1 HETATM 6485 O O . HOH T 9 . ? 40.483 45.187 19.523 1.00 43.52 ? 1315 HOH A O 1 HETATM 6486 O O . HOH T 9 . ? 7.639 26.664 54.215 1.00 49.79 ? 1316 HOH A O 1 HETATM 6487 O O . HOH T 9 . ? 40.212 41.444 26.174 1.00 42.72 ? 1317 HOH A O 1 HETATM 6488 O O . HOH T 9 . ? 28.669 29.556 61.988 1.00 36.64 ? 1318 HOH A O 1 HETATM 6489 O O . HOH T 9 . ? 32.777 54.257 70.632 1.00 47.35 ? 1319 HOH A O 1 HETATM 6490 O O . HOH T 9 . ? 14.050 40.503 12.256 1.00 41.92 ? 1320 HOH A O 1 HETATM 6491 O O . HOH T 9 . ? 29.981 25.305 47.323 1.00 37.42 ? 1321 HOH A O 1 HETATM 6492 O O . HOH T 9 . ? 10.590 36.547 76.392 1.00 38.20 ? 1322 HOH A O 1 HETATM 6493 O O . HOH T 9 . ? 27.950 67.093 52.865 1.00 45.19 ? 1323 HOH A O 1 HETATM 6494 O O . HOH T 9 . ? 9.068 41.896 19.616 1.00 50.39 ? 1324 HOH A O 1 HETATM 6495 O O . HOH T 9 . ? 7.938 34.468 19.260 1.00 57.67 ? 1325 HOH A O 1 HETATM 6496 O O . HOH T 9 . ? 36.072 34.306 50.792 1.00 44.01 ? 1326 HOH A O 1 HETATM 6497 O O . HOH T 9 . ? 27.150 63.169 63.285 1.00 51.05 ? 1327 HOH A O 1 HETATM 6498 O O . HOH T 9 . ? 29.260 30.480 14.975 1.00 37.65 ? 1328 HOH A O 1 HETATM 6499 O O . HOH T 9 . ? 33.986 54.766 68.045 1.00 43.32 ? 1329 HOH A O 1 HETATM 6500 O O . HOH T 9 . ? 40.430 42.663 23.441 1.00 48.83 ? 1330 HOH A O 1 HETATM 6501 O O . HOH T 9 . ? 7.471 57.406 33.632 1.00 39.31 ? 1331 HOH A O 1 HETATM 6502 O O . HOH T 9 . ? 31.344 50.158 11.469 1.00 38.62 ? 1332 HOH A O 1 HETATM 6503 O O . HOH T 9 . ? 23.284 78.211 23.045 1.00 39.44 ? 1333 HOH A O 1 HETATM 6504 O O . HOH T 9 . ? 21.193 42.183 45.958 1.00 37.15 ? 1334 HOH A O 1 HETATM 6505 O O . HOH T 9 . ? 42.615 30.973 41.031 1.00 50.80 ? 1335 HOH A O 1 HETATM 6506 O O . HOH T 9 . ? 7.262 81.577 62.610 1.00 40.79 ? 1336 HOH A O 1 HETATM 6507 O O . HOH T 9 . ? 24.385 79.339 55.380 1.00 43.72 ? 1337 HOH A O 1 HETATM 6508 O O . HOH T 9 . ? 27.515 65.708 55.235 1.00 36.55 ? 1338 HOH A O 1 HETATM 6509 O O . HOH T 9 . ? 16.674 42.413 44.413 1.00 17.57 ? 1339 HOH A O 1 HETATM 6510 O O . HOH T 9 . ? 14.895 41.104 77.575 0.50 39.28 ? 1340 HOH A O 1 HETATM 6511 O O . HOH T 9 . ? 15.596 39.413 75.783 0.50 39.95 ? 1341 HOH A O 1 HETATM 6512 O O . HOH T 9 . ? 12.316 50.783 76.229 1.00 50.38 ? 1342 HOH A O 1 HETATM 6513 O O . HOH T 9 . ? 25.153 43.208 71.426 0.30 25.88 ? 1343 HOH A O 1 HETATM 6514 O O . HOH T 9 . ? 23.659 31.114 69.507 0.50 28.44 ? 1344 HOH A O 1 HETATM 6515 O O . HOH T 9 . ? 18.471 24.175 61.109 1.00 56.29 ? 1345 HOH A O 1 HETATM 6516 O O . HOH T 9 . ? 11.635 24.692 51.628 0.50 27.37 ? 1346 HOH A O 1 HETATM 6517 O O . HOH T 9 . ? 12.368 22.723 43.963 0.40 23.13 ? 1347 HOH A O 1 HETATM 6518 O O . HOH T 9 . ? 9.062 53.231 79.416 0.70 40.93 ? 1348 HOH A O 1 HETATM 6519 O O . HOH T 9 . ? 22.560 55.133 69.795 1.00 51.61 ? 1349 HOH A O 1 HETATM 6520 O O . HOH T 9 . ? -0.519 30.648 62.909 0.70 38.19 ? 1350 HOH A O 1 HETATM 6521 O O . HOH T 9 . ? 15.291 29.821 12.726 0.50 32.07 ? 1351 HOH A O 1 HETATM 6522 O O . HOH T 9 . ? 5.728 32.601 21.189 1.00 61.86 ? 1352 HOH A O 1 HETATM 6523 O O . HOH T 9 . ? 20.231 61.812 27.032 1.00 40.61 ? 1353 HOH A O 1 HETATM 6524 O O . HOH T 9 . ? 20.411 60.021 24.690 1.00 44.10 ? 1354 HOH A O 1 HETATM 6525 O O . HOH T 9 . ? 38.758 30.959 45.222 0.60 34.31 ? 1355 HOH A O 1 HETATM 6526 O O . HOH T 9 . ? 33.083 21.697 40.496 0.50 35.36 ? 1356 HOH A O 1 HETATM 6527 O O . HOH T 9 . ? 26.990 28.284 28.284 1.00 39.47 ? 1357 HOH A O 1 HETATM 6528 O O . HOH T 9 . ? -7.323 48.146 47.927 0.75 30.25 ? 1358 HOH A O 1 HETATM 6529 O O . HOH T 9 . ? 42.572 53.013 24.740 1.00 51.45 ? 1359 HOH A O 1 HETATM 6530 O O . HOH T 9 . ? 31.357 29.295 11.070 1.00 47.55 ? 1360 HOH A O 1 HETATM 6531 O O . HOH T 9 . ? 26.079 32.117 5.917 0.80 51.15 ? 1361 HOH A O 1 HETATM 6532 O O . HOH T 9 . ? 37.908 41.707 52.822 1.00 40.71 ? 1362 HOH A O 1 HETATM 6533 O O . HOH T 9 . ? 40.575 44.918 50.727 1.00 46.31 ? 1363 HOH A O 1 HETATM 6534 O O . HOH T 9 . ? 30.875 41.164 40.068 1.00 40.47 ? 1364 HOH A O 1 HETATM 6535 O O . HOH T 9 . ? 25.552 71.358 60.721 1.00 47.93 ? 1365 HOH A O 1 HETATM 6536 O O . HOH T 9 . ? 30.594 76.517 48.887 1.00 55.35 ? 1366 HOH A O 1 HETATM 6537 O O . HOH T 9 . ? 24.942 59.374 43.367 0.50 34.03 ? 1367 HOH A O 1 HETATM 6538 O O . HOH T 9 . ? 24.686 62.701 42.263 0.50 27.94 ? 1368 HOH A O 1 HETATM 6539 O O . HOH T 9 . ? 9.722 47.187 80.159 1.00 58.62 ? 1369 HOH A O 1 HETATM 6540 O O . HOH T 9 . ? 16.067 29.207 65.514 0.50 42.92 ? 1370 HOH A O 1 HETATM 6541 O O . HOH T 9 . ? 13.432 30.611 66.399 0.50 27.51 ? 1371 HOH A O 1 HETATM 6542 O O . HOH T 9 . ? 0.020 29.798 44.771 0.50 30.19 ? 1372 HOH A O 1 HETATM 6543 O O . HOH T 9 . ? -3.784 32.450 53.217 0.50 30.63 ? 1373 HOH A O 1 HETATM 6544 O O . HOH T 9 . ? -4.191 29.457 52.769 0.50 32.14 ? 1374 HOH A O 1 HETATM 6545 O O . HOH T 9 . ? -4.630 34.248 51.529 0.50 40.62 ? 1375 HOH A O 1 HETATM 6546 O O . HOH T 9 . ? 1.726 40.802 27.095 1.00 40.29 ? 1376 HOH A O 1 HETATM 6547 O O . HOH T 9 . ? 3.312 48.695 26.604 1.00 39.44 ? 1377 HOH A O 1 HETATM 6548 O O . HOH T 9 . ? 8.123 30.189 36.029 0.50 25.81 ? 1378 HOH A O 1 HETATM 6549 O O . HOH T 9 . ? 5.301 30.059 37.051 0.60 35.82 ? 1379 HOH A O 1 HETATM 6550 O O . HOH T 9 . ? 10.947 27.228 31.993 0.50 24.50 ? 1380 HOH A O 1 HETATM 6551 O O . HOH T 9 . ? 17.515 61.054 30.497 0.50 25.75 ? 1381 HOH A O 1 HETATM 6552 O O . HOH T 9 . ? 15.071 61.187 30.612 0.50 30.76 ? 1382 HOH A O 1 HETATM 6553 O O . HOH T 9 . ? 13.262 65.091 31.695 0.50 32.40 ? 1383 HOH A O 1 HETATM 6554 O O . HOH T 9 . ? 14.471 69.822 30.147 0.70 25.20 ? 1384 HOH A O 1 HETATM 6555 O O . HOH T 9 . ? 16.056 67.839 29.293 0.50 26.37 ? 1385 HOH A O 1 HETATM 6556 O O . HOH T 9 . ? 14.790 72.968 23.905 0.50 26.41 ? 1386 HOH A O 1 HETATM 6557 O O . HOH T 9 . ? 15.138 71.865 21.890 0.50 26.95 ? 1387 HOH A O 1 HETATM 6558 O O . HOH T 9 . ? 20.086 64.223 25.387 0.50 27.68 ? 1388 HOH A O 1 HETATM 6559 O O . HOH T 9 . ? 29.110 61.798 26.813 1.00 36.18 ? 1389 HOH A O 1 HETATM 6560 O O . HOH T 9 . ? 27.139 61.922 28.843 0.50 22.61 ? 1390 HOH A O 1 HETATM 6561 O O . HOH T 9 . ? 31.963 57.914 26.446 0.25 21.24 ? 1391 HOH A O 1 HETATM 6562 O O . HOH T 9 . ? 31.442 56.984 31.174 0.50 32.09 ? 1392 HOH A O 1 HETATM 6563 O O . HOH T 9 . ? 8.307 50.464 25.247 1.00 43.47 ? 1393 HOH A O 1 HETATM 6564 O O . HOH T 9 . ? 6.577 52.454 27.815 0.50 31.40 ? 1394 HOH A O 1 HETATM 6565 O O . HOH T 9 . ? 10.541 54.723 29.477 0.40 22.61 ? 1395 HOH A O 1 HETATM 6566 O O . HOH T 9 . ? 11.335 54.614 26.178 0.50 28.80 ? 1396 HOH A O 1 HETATM 6567 O O . HOH T 9 . ? 17.219 56.607 26.739 0.40 24.84 ? 1397 HOH A O 1 HETATM 6568 O O . HOH T 9 . ? 29.185 60.410 50.070 0.40 36.71 ? 1398 HOH A O 1 HETATM 6569 O O . HOH T 9 . ? 29.020 57.863 48.516 0.30 17.50 ? 1399 HOH A O 1 HETATM 6570 O O . HOH T 9 . ? 19.094 24.856 12.247 1.00 47.12 ? 1400 HOH A O 1 HETATM 6571 O O . HOH T 9 . ? 18.630 15.244 38.334 0.25 23.77 ? 1401 HOH A O 1 HETATM 6572 O O . HOH T 9 . ? 10.081 38.946 15.399 0.40 27.21 ? 1402 HOH A O 1 HETATM 6573 O O . HOH T 9 . ? 30.866 54.643 10.623 0.50 36.17 ? 1403 HOH A O 1 HETATM 6574 O O . HOH T 9 . ? 26.425 52.027 11.086 0.50 34.28 ? 1404 HOH A O 1 HETATM 6575 O O . HOH T 9 . ? 23.576 55.252 8.909 1.00 78.87 ? 1405 HOH A O 1 HETATM 6576 O O . HOH T 9 . ? 21.312 54.417 16.250 0.50 27.22 ? 1406 HOH A O 1 HETATM 6577 O O . HOH T 9 . ? 32.318 46.363 36.649 0.50 27.70 ? 1407 HOH A O 1 HETATM 6578 O O . HOH T 9 . ? 38.745 38.710 35.105 0.40 24.63 ? 1408 HOH A O 1 HETATM 6579 O O . HOH T 9 . ? 34.985 20.930 44.081 1.00 40.34 ? 1409 HOH A O 1 HETATM 6580 O O . HOH T 9 . ? -14.205 42.418 41.502 0.60 39.22 ? 1410 HOH A O 1 HETATM 6581 O O . HOH T 9 . ? -8.268 49.416 50.024 1.00 29.92 ? 1411 HOH A O 1 HETATM 6582 O O . HOH T 9 . ? 16.111 85.753 29.436 0.50 30.35 ? 1412 HOH A O 1 HETATM 6583 O O . HOH T 9 . ? -8.789 43.160 34.939 0.50 26.00 ? 1413 HOH A O 1 HETATM 6584 O O . HOH T 9 . ? 1.419 55.851 30.915 0.20 19.19 ? 1414 HOH A O 1 HETATM 6585 O O . HOH T 9 . ? 29.269 28.496 24.511 0.30 20.21 ? 1415 HOH A O 1 HETATM 6586 O O . HOH T 9 . ? 37.703 51.116 13.272 1.00 44.23 ? 1416 HOH A O 1 HETATM 6587 O O . HOH T 9 . ? 37.501 52.511 16.430 1.00 50.08 ? 1417 HOH A O 1 HETATM 6588 O O . HOH T 9 . ? 40.830 50.118 19.438 0.40 26.75 ? 1418 HOH A O 1 HETATM 6589 O O . HOH T 9 . ? 39.975 45.252 16.265 0.50 27.79 ? 1419 HOH A O 1 HETATM 6590 O O . HOH T 9 . ? 29.483 34.261 5.515 0.50 38.62 ? 1420 HOH A O 1 HETATM 6591 O O . HOH T 9 . ? 36.060 37.705 57.002 0.80 41.86 ? 1421 HOH A O 1 HETATM 6592 O O . HOH T 9 . ? 36.138 41.445 47.128 0.40 21.18 ? 1422 HOH A O 1 HETATM 6593 O O . HOH T 9 . ? 36.546 42.296 65.356 1.00 30.78 ? 1423 HOH A O 1 HETATM 6594 O O . HOH T 9 . ? 43.362 39.593 64.313 1.00 54.16 ? 1424 HOH A O 1 HETATM 6595 O O . HOH T 9 . ? 29.544 68.954 52.630 0.70 30.98 ? 1425 HOH A O 1 HETATM 6596 O O . HOH T 9 . ? 28.393 73.389 54.674 0.60 38.26 ? 1426 HOH A O 1 HETATM 6597 O O . HOH T 9 . ? 30.145 71.726 56.431 0.50 43.13 ? 1427 HOH A O 1 HETATM 6598 O O . HOH T 9 . ? 36.850 59.386 63.833 0.50 26.66 ? 1428 HOH A O 1 HETATM 6599 O O . HOH T 9 . ? 37.096 56.611 64.139 1.00 37.44 ? 1429 HOH A O 1 HETATM 6600 O O . HOH T 9 . ? 40.019 56.753 60.783 0.70 37.12 ? 1430 HOH A O 1 HETATM 6601 O O . HOH T 9 . ? 27.913 24.320 53.403 1.00 73.93 ? 1431 HOH A O 1 HETATM 6602 O O . HOH T 9 . ? 32.530 27.648 56.251 0.50 25.53 ? 1432 HOH A O 1 HETATM 6603 O O . HOH T 9 . ? 35.766 31.533 53.488 0.20 16.24 ? 1433 HOH A O 1 HETATM 6604 O O . HOH T 9 . ? 24.240 82.166 24.467 1.00 41.05 ? 1434 HOH A O 1 HETATM 6605 O O . HOH T 9 . ? -0.038 58.865 76.558 0.70 49.24 ? 1435 HOH A O 1 HETATM 6606 O O . HOH T 9 . ? 8.162 69.633 36.832 0.80 29.20 ? 1436 HOH A O 1 HETATM 6607 O O . HOH T 9 . ? 10.516 82.583 56.233 0.40 26.87 ? 1437 HOH A O 1 HETATM 6608 O O . HOH T 9 . ? 15.039 52.283 75.926 0.50 34.14 ? 1438 HOH A O 1 HETATM 6609 O O . HOH T 9 . ? 2.074 26.817 61.804 1.00 61.35 ? 1439 HOH A O 1 HETATM 6610 O O . HOH T 9 . ? 1.238 31.798 67.478 0.70 31.27 ? 1440 HOH A O 1 HETATM 6611 O O . HOH T 9 . ? -0.710 37.313 66.009 0.40 36.90 ? 1441 HOH A O 1 HETATM 6612 O O . HOH T 9 . ? 19.276 18.428 43.807 1.00 48.52 ? 1442 HOH A O 1 HETATM 6613 O O . HOH T 9 . ? 18.406 22.505 48.777 1.00 43.99 ? 1443 HOH A O 1 HETATM 6614 O O . HOH T 9 . ? 18.339 19.465 46.856 0.40 32.08 ? 1444 HOH A O 1 HETATM 6615 O O . HOH T 9 . ? 28.052 63.745 22.893 1.00 42.42 ? 1445 HOH A O 1 HETATM 6616 O O . HOH T 9 . ? 37.959 33.994 48.485 0.30 25.25 ? 1446 HOH A O 1 HETATM 6617 O O . HOH T 9 . ? 45.364 28.810 38.779 0.30 16.07 ? 1447 HOH A O 1 HETATM 6618 O O . HOH T 9 . ? 44.470 30.703 37.164 0.50 29.71 ? 1448 HOH A O 1 HETATM 6619 O O . HOH T 9 . ? 44.257 32.416 34.841 0.60 41.53 ? 1449 HOH A O 1 HETATM 6620 O O A HOH T 9 . ? 32.477 26.303 34.016 0.50 30.11 ? 1450 HOH A O 1 HETATM 6621 O O B HOH T 9 . ? 33.406 26.598 35.810 0.50 29.83 ? 1450 HOH A O 1 HETATM 6622 O O . HOH T 9 . ? 21.589 50.511 11.005 1.00 45.72 ? 1451 HOH A O 1 HETATM 6623 O O . HOH T 9 . ? -0.979 57.057 74.007 1.00 48.36 ? 1452 HOH A O 1 HETATM 6624 O O . HOH T 9 . ? 23.178 43.692 44.344 0.35 18.63 ? 1453 HOH A O 1 HETATM 6625 O O . HOH T 9 . ? 37.042 39.938 55.696 0.50 29.60 ? 1454 HOH A O 1 HETATM 6626 O O . HOH T 9 . ? 26.049 62.160 65.745 1.00 38.09 ? 1455 HOH A O 1 HETATM 6627 O O . HOH T 9 . ? 27.138 64.525 60.312 0.60 41.20 ? 1456 HOH A O 1 HETATM 6628 O O . HOH T 9 . ? 28.216 63.410 57.785 0.50 40.06 ? 1457 HOH A O 1 HETATM 6629 O O . HOH T 9 . ? 21.800 56.314 67.628 0.25 15.25 ? 1458 HOH A O 1 HETATM 6630 O O . HOH T 9 . ? 30.750 61.291 64.351 0.30 18.83 ? 1459 HOH A O 1 HETATM 6631 O O . HOH T 9 . ? 28.514 60.864 68.672 0.30 19.26 ? 1460 HOH A O 1 HETATM 6632 O O . HOH T 9 . ? 28.822 63.683 68.860 1.00 43.68 ? 1461 HOH A O 1 HETATM 6633 O O . HOH T 9 . ? 26.468 64.560 67.311 0.50 37.72 ? 1462 HOH A O 1 HETATM 6634 O O . HOH T 9 . ? 27.117 66.826 63.730 0.30 27.38 ? 1463 HOH A O 1 HETATM 6635 O O . HOH T 9 . ? 31.394 48.764 71.562 0.35 34.53 ? 1464 HOH A O 1 HETATM 6636 O O . HOH T 9 . ? 32.495 41.191 67.378 0.30 15.11 ? 1465 HOH A O 1 HETATM 6637 O O . HOH T 9 . ? 42.606 48.291 65.483 0.30 33.56 ? 1466 HOH A O 1 HETATM 6638 O O . HOH T 9 . ? 26.896 63.233 47.219 0.35 30.83 ? 1467 HOH A O 1 HETATM 6639 O O . HOH T 9 . ? 27.255 65.678 46.089 1.00 32.22 ? 1468 HOH A O 1 HETATM 6640 O O . HOH T 9 . ? 28.597 66.905 38.781 0.40 24.60 ? 1469 HOH A O 1 HETATM 6641 O O . HOH T 9 . ? 28.356 65.909 36.387 1.00 39.50 ? 1470 HOH A O 1 HETATM 6642 O O . HOH T 9 . ? 30.770 70.238 37.126 1.00 53.47 ? 1471 HOH A O 1 HETATM 6643 O O . HOH T 9 . ? 32.068 74.086 36.077 1.00 47.80 ? 1472 HOH A O 1 HETATM 6644 O O . HOH T 9 . ? 33.400 73.658 41.434 0.50 34.70 ? 1473 HOH A O 1 HETATM 6645 O O . HOH T 9 . ? 31.019 24.452 54.532 0.30 22.35 ? 1474 HOH A O 1 HETATM 6646 O O . HOH T 9 . ? 29.671 34.504 64.939 1.00 44.90 ? 1475 HOH A O 1 HETATM 6647 O O . HOH T 9 . ? 28.272 38.778 69.466 1.00 47.99 ? 1476 HOH A O 1 HETATM 6648 O O . HOH T 9 . ? 19.397 58.054 68.563 0.50 34.26 ? 1477 HOH A O 1 HETATM 6649 O O . HOH T 9 . ? 18.072 59.532 70.207 0.50 27.77 ? 1478 HOH A O 1 HETATM 6650 O O . HOH T 9 . ? 15.530 78.231 71.951 0.50 28.44 ? 1479 HOH A O 1 HETATM 6651 O O . HOH T 9 . ? 14.118 71.956 25.581 0.50 31.37 ? 1480 HOH A O 1 HETATM 6652 O O . HOH T 9 . ? 12.204 80.942 69.791 0.40 27.64 ? 1481 HOH A O 1 HETATM 6653 O O . HOH T 9 . ? 13.818 81.402 65.676 0.35 22.70 ? 1482 HOH A O 1 HETATM 6654 O O . HOH T 9 . ? 7.960 82.786 60.250 0.40 27.64 ? 1483 HOH A O 1 HETATM 6655 O O . HOH T 9 . ? -0.254 64.531 66.003 0.50 15.09 ? 1484 HOH A O 1 HETATM 6656 O O . HOH T 9 . ? 21.509 73.232 68.956 0.70 38.64 ? 1485 HOH A O 1 HETATM 6657 O O . HOH T 9 . ? 23.033 60.928 19.946 0.65 31.44 ? 1486 HOH A O 1 HETATM 6658 O O . HOH T 9 . ? 20.569 56.909 20.490 1.00 45.56 ? 1487 HOH A O 1 HETATM 6659 O O . HOH T 9 . ? 18.354 59.078 19.263 0.55 36.52 ? 1488 HOH A O 1 HETATM 6660 O O . HOH T 9 . ? 9.437 59.230 31.383 0.20 19.52 ? 1489 HOH A O 1 HETATM 6661 O O . HOH T 9 . ? 21.223 67.022 69.993 1.00 53.93 ? 1490 HOH A O 1 HETATM 6662 O O . HOH T 9 . ? 3.110 27.317 57.226 0.40 30.54 ? 1491 HOH A O 1 HETATM 6663 O O . HOH T 9 . ? 3.394 28.958 21.057 1.00 55.09 ? 1492 HOH A O 1 HETATM 6664 O O . HOH T 9 . ? 31.831 48.637 37.827 1.00 47.04 ? 1493 HOH A O 1 HETATM 6665 O O . HOH T 9 . ? 24.949 51.488 39.598 1.00 36.30 ? 1494 HOH A O 1 HETATM 6666 O O . HOH T 9 . ? 6.537 25.184 63.248 1.00 56.76 ? 1495 HOH A O 1 HETATM 6667 O O . HOH T 9 . ? -5.914 46.479 56.095 1.00 62.94 ? 1496 HOH A O 1 HETATM 6668 O O . HOH T 9 . ? 9.269 81.141 58.489 1.00 43.07 ? 1497 HOH A O 1 HETATM 6669 O O . HOH T 9 . ? -8.298 48.715 30.045 1.00 47.89 ? 1498 HOH A O 1 HETATM 6670 O O . HOH T 9 . ? 3.945 46.494 25.087 1.00 53.32 ? 1499 HOH A O 1 HETATM 6671 O O . HOH T 9 . ? 36.238 38.912 14.652 0.25 10.87 ? 1500 HOH A O 1 HETATM 6672 O O . HOH T 9 . ? 25.484 81.805 53.117 1.00 52.76 ? 1501 HOH A O 1 HETATM 6673 O O . HOH T 9 . ? 28.032 81.003 51.716 1.00 60.09 ? 1502 HOH A O 1 HETATM 6674 O O . HOH T 9 . ? 12.610 25.173 20.537 0.60 42.98 ? 1503 HOH A O 1 HETATM 6675 O O . HOH T 9 . ? 18.648 21.667 59.821 0.80 57.42 ? 1504 HOH A O 1 HETATM 6676 O O . HOH T 9 . ? 22.928 79.327 60.176 0.50 27.44 ? 1505 HOH A O 1 HETATM 6677 O O . HOH T 9 . ? 25.294 47.605 73.029 1.00 64.12 ? 1506 HOH A O 1 HETATM 6678 O O . HOH T 9 . ? -2.341 43.450 56.119 1.00 51.45 ? 1507 HOH A O 1 HETATM 6679 O O . HOH T 9 . ? 30.109 61.261 22.645 1.00 45.86 ? 1508 HOH A O 1 HETATM 6680 O O . HOH T 9 . ? 17.289 65.943 70.534 1.00 45.06 ? 1509 HOH A O 1 HETATM 6681 O O . HOH T 9 . ? 6.935 24.841 49.813 1.00 54.86 ? 1510 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . HIS A 63 ? 0.8333 0.6751 0.3567 -0.1475 -0.0833 -0.0728 56 HIS A N 2 C CA . HIS A 63 ? 0.6608 0.5519 0.3769 0.1155 -0.0459 0.0429 56 HIS A CA 3 C C . HIS A 63 ? 0.6441 0.5264 0.4424 0.1794 -0.0057 0.0566 56 HIS A C 4 O O . HIS A 63 ? 0.6889 0.5635 0.6845 0.2192 -0.0717 0.0225 56 HIS A O 5 C CB . HIS A 63 ? 0.6869 0.5404 0.4400 0.1239 -0.1509 0.0569 56 HIS A CB 6 C CG . HIS A 63 ? 0.8027 0.5605 0.4872 0.1052 -0.1091 0.0805 56 HIS A CG 7 N ND1 . HIS A 63 ? 0.7812 0.5903 0.4361 0.1443 -0.1124 0.1108 56 HIS A ND1 8 C CD2 . HIS A 63 ? 0.8218 0.5837 0.3749 0.1160 -0.0433 -0.0075 56 HIS A CD2 9 C CE1 . HIS A 63 ? 0.8307 0.5993 0.6026 0.1289 -0.0540 0.0776 56 HIS A CE1 10 N NE2 . HIS A 63 ? 0.8902 0.6167 0.4656 0.1199 -0.0330 0.0506 56 HIS A NE2 11 N N . ASN A 64 ? 0.6393 0.4717 0.3468 0.2009 -0.0351 0.0282 57 ASN A N 12 C CA . ASN A 64 ? 0.5898 0.4968 0.2627 0.1467 -0.0265 -0.0368 57 ASN A CA 13 C C . ASN A 64 ? 0.5330 0.4319 0.2496 0.1905 -0.0576 -0.0003 57 ASN A C 14 O O . ASN A 64 ? 0.5298 0.4207 0.2667 0.1894 -0.0474 -0.0104 57 ASN A O 15 C CB . ASN A 64 ? 0.5518 0.4172 0.2403 0.1857 -0.0290 -0.0425 57 ASN A CB 16 C CG . ASN A 64 ? 0.6101 0.4940 0.2743 0.1757 -0.1079 -0.0048 57 ASN A CG 17 O OD1 . ASN A 64 ? 0.5837 0.5349 0.2565 0.1742 -0.0845 -0.0453 57 ASN A OD1 18 N ND2 . ASN A 64 ? 0.6683 0.4982 0.2752 0.1410 -0.0914 -0.0448 57 ASN A ND2 19 N N . MET A 65 ? 0.4739 0.4241 0.2762 0.1960 -0.0461 -0.0411 58 MET A N 20 C CA . MET A 65 ? 0.5029 0.3844 0.2400 0.2134 -0.0561 -0.0214 58 MET A CA 21 C C . MET A 65 ? 0.5137 0.3608 0.2770 0.2013 -0.0867 -0.0238 58 MET A C 22 O O . MET A 65 ? 0.4693 0.3799 0.2908 0.1570 -0.0684 -0.0559 58 MET A O 23 C CB . MET A 65 ? 0.5256 0.4099 0.2233 0.1803 -0.0766 -0.0066 58 MET A CB 24 C CG . MET A 65 ? 0.5734 0.4364 0.2896 0.1940 -0.0300 -0.0867 58 MET A CG 25 S SD . MET A 65 ? 0.5736 0.6269 0.4142 0.1660 -0.0603 -0.0095 58 MET A SD 26 C CE . MET A 65 ? 0.4445 0.5630 0.3693 0.1059 -0.1392 -0.1173 58 MET A CE 27 N N . LYS A 66 ? 0.4953 0.3709 0.3008 0.1852 -0.0893 -0.0400 59 LYS A N 28 C CA . LYS A 66 ? 0.4770 0.3996 0.2774 0.1613 -0.1661 0.0150 59 LYS A CA 29 C C . LYS A 66 ? 0.4995 0.3958 0.2471 0.1552 -0.1149 -0.0115 59 LYS A C 30 O O . LYS A 66 ? 0.4859 0.4011 0.2692 0.1779 -0.0854 0.0263 59 LYS A O 31 C CB . LYS A 66 ? 0.4535 0.4036 0.2605 0.1709 -0.1485 -0.0171 59 LYS A CB 32 C CG . LYS A 66 ? 0.5006 0.4286 0.4362 0.2007 -0.1376 0.0245 59 LYS A CG 33 C CD . LYS A 66 ? 0.5804 0.5630 0.5175 0.2054 -0.1932 -0.0049 59 LYS A CD 34 C CE . LYS A 66 ? 0.6163 0.5531 0.8601 0.2386 -0.2124 -0.0440 59 LYS A CE 35 N NZ . LYS A 66 ? 0.6432 0.5481 0.8811 0.2356 -0.3043 0.0132 59 LYS A NZ 36 N N . ALA A 67 ? 0.5151 0.3904 0.2115 0.1433 -0.1117 -0.0185 60 ALA A N 37 C CA . ALA A 67 ? 0.5145 0.4251 0.2147 0.1035 -0.0675 -0.0173 60 ALA A CA 38 C C . ALA A 67 ? 0.4446 0.3778 0.2102 0.1448 -0.0722 0.0043 60 ALA A C 39 O O . ALA A 67 ? 0.4792 0.3781 0.2680 0.1218 -0.0499 0.0007 60 ALA A O 40 C CB . ALA A 67 ? 0.5125 0.4610 0.2827 0.1484 -0.0420 -0.0519 60 ALA A CB 41 N N . PHE A 68 ? 0.4479 0.3933 0.1982 0.1412 -0.0896 0.0068 61 PHE A N 42 C CA . PHE A 68 ? 0.4209 0.3864 0.1976 0.1588 -0.0899 0.0092 61 PHE A CA 43 C C . PHE A 68 ? 0.4615 0.3358 0.2158 0.1361 -0.0602 0.0040 61 PHE A C 44 O O . PHE A 68 ? 0.4058 0.3201 0.2673 0.1311 -0.0794 0.0094 61 PHE A O 45 C CB . PHE A 68 ? 0.4211 0.3405 0.2091 0.1453 -0.0243 0.0166 61 PHE A CB 46 C CG . PHE A 68 ? 0.4278 0.3201 0.2050 0.1216 -0.0423 0.0115 61 PHE A CG 47 C CD1 . PHE A 68 ? 0.4047 0.3420 0.2218 0.1232 -0.0439 0.0090 61 PHE A CD1 48 C CD2 . PHE A 68 ? 0.4168 0.2892 0.2099 0.1070 -0.0495 0.0320 61 PHE A CD2 49 C CE1 . PHE A 68 ? 0.4141 0.2697 0.2178 0.1017 -0.0370 0.0213 61 PHE A CE1 50 C CE2 . PHE A 68 ? 0.3894 0.2665 0.2156 0.1005 -0.0580 0.0159 61 PHE A CE2 51 C CZ . PHE A 68 ? 0.3909 0.3076 0.1985 0.0956 -0.0691 0.0103 61 PHE A CZ 52 N N . LEU A 69 ? 0.4126 0.3558 0.2452 0.1508 -0.0784 0.0125 62 LEU A N 53 C CA . LEU A 69 ? 0.4536 0.3158 0.2726 0.1416 -0.0425 0.0035 62 LEU A CA 54 C C . LEU A 69 ? 0.4506 0.3412 0.2556 0.1449 -0.0752 0.0225 62 LEU A C 55 O O . LEU A 69 ? 0.4774 0.3243 0.2768 0.1346 -0.1108 0.0130 62 LEU A O 56 C CB . LEU A 69 ? 0.5140 0.2950 0.2701 0.1191 -0.0303 0.0368 62 LEU A CB 57 C CG . LEU A 69 ? 0.3742 0.3128 0.2086 0.1422 -0.0923 -0.0031 62 LEU A CG 58 C CD1 . LEU A 69 ? 0.5451 0.3165 0.2480 0.0463 -0.0583 -0.0264 62 LEU A CD1 59 C CD2 . LEU A 69 ? 0.4797 0.3094 0.1924 0.1218 -0.0177 0.0161 62 LEU A CD2 60 N N . ASP A 70 ? 0.4606 0.3210 0.2638 0.1421 -0.0570 0.0336 63 ASP A N 61 C CA . ASP A 70 ? 0.5359 0.3361 0.2933 0.1504 -0.0858 0.0405 63 ASP A CA 62 C C . ASP A 70 ? 0.4802 0.3463 0.2882 0.1666 -0.0836 -0.0131 63 ASP A C 63 O O . ASP A 70 ? 0.4547 0.3635 0.3436 0.1740 -0.0939 0.0108 63 ASP A O 64 C CB . ASP A 70 ? 0.5167 0.4029 0.2837 0.1655 -0.0684 0.0406 63 ASP A CB 65 C CG . ASP A 70 ? 0.5617 0.4490 0.2951 0.1355 -0.0994 0.0303 63 ASP A CG 66 O OD1 . ASP A 70 ? 0.5490 0.4464 0.3770 0.0706 -0.0874 0.0324 63 ASP A OD1 67 O OD2 . ASP A 70 ? 0.6556 0.4678 0.3321 0.1533 -0.2087 0.0013 63 ASP A OD2 68 N N . GLU A 71 ? 0.4589 0.3659 0.2529 0.1523 -0.0606 0.0012 64 GLU A N 69 C CA . GLU A 71 ? 0.4946 0.3483 0.2752 0.1406 -0.0395 0.0062 64 GLU A CA 70 C C . GLU A 71 ? 0.4426 0.3325 0.2770 0.1645 -0.0049 0.0249 64 GLU A C 71 O O . GLU A 71 ? 0.4540 0.3355 0.2746 0.1079 -0.0458 0.0312 64 GLU A O 72 C CB . GLU A 71 ? 0.4666 0.3755 0.2610 0.1322 -0.0454 0.0092 64 GLU A CB 73 C CG . GLU A 71 ? 0.5318 0.3772 0.3134 0.0935 -0.0240 0.0238 64 GLU A CG 74 C CD . GLU A 71 ? 0.6221 0.4309 0.2667 0.0867 -0.0687 0.0280 64 GLU A CD 75 O OE1 . GLU A 71 ? 0.6036 0.4805 0.2206 0.0477 -0.0017 -0.0008 64 GLU A OE1 76 O OE2 . GLU A 71 ? 0.5418 0.4184 0.2897 0.1031 0.0351 0.0126 64 GLU A OE2 77 N N . LEU A 72 ? 0.4358 0.3170 0.2612 0.1462 -0.0417 0.0215 65 LEU A N 78 C CA . LEU A 72 ? 0.4092 0.2708 0.2665 0.1595 -0.0144 0.0556 65 LEU A CA 79 C C . LEU A 72 ? 0.3684 0.3181 0.2999 0.1567 -0.0678 0.0047 65 LEU A C 80 O O . LEU A 72 ? 0.4237 0.3386 0.2645 0.1688 -0.0900 -0.0038 65 LEU A O 81 C CB . LEU A 72 ? 0.3638 0.2762 0.2549 0.1598 -0.0322 0.0683 65 LEU A CB 82 C CG . LEU A 72 ? 0.3181 0.2633 0.2275 0.1342 -0.0497 0.0662 65 LEU A CG 83 C CD1 . LEU A 72 ? 0.3342 0.2722 0.2566 0.1044 -0.0414 0.0452 65 LEU A CD1 84 C CD2 . LEU A 72 ? 0.3061 0.3090 0.2208 0.1085 -0.0372 0.0408 65 LEU A CD2 85 N N . LYS A 73 ? 0.3514 0.2711 0.3109 0.1266 -0.0585 0.0178 66 LYS A N 86 C CA . LYS A 73 ? 0.4198 0.2800 0.2873 0.1524 -0.0144 0.0341 66 LYS A CA 87 C C . LYS A 73 ? 0.3933 0.2736 0.2723 0.1280 -0.0346 0.0394 66 LYS A C 88 O O . LYS A 73 ? 0.3980 0.2798 0.2892 0.1379 -0.0377 -0.0038 66 LYS A O 89 C CB . LYS A 73 ? 0.4344 0.2926 0.2871 0.1104 -0.0355 0.0415 66 LYS A CB 90 C CG . LYS A 73 ? 0.5310 0.4162 0.2932 0.1325 -0.0052 0.0365 66 LYS A CG 91 C CD . LYS A 73 ? 0.5951 0.5979 0.3512 0.0962 -0.0401 0.0475 66 LYS A CD 92 C CE . LYS A 73 ? 0.6984 0.5268 0.4062 0.1987 0.0814 0.0459 66 LYS A CE 93 N NZ . LYS A 73 ? 0.6933 0.4666 0.4429 0.2063 0.0818 0.1236 66 LYS A NZ 94 N N . ALA A 74 ? 0.3982 0.3084 0.2960 0.1492 -0.0381 0.0275 67 ALA A N 95 C CA . ALA A 74 ? 0.3431 0.2974 0.3431 0.1290 -0.0377 -0.0365 67 ALA A CA 96 C C . ALA A 74 ? 0.3350 0.2659 0.3224 0.1329 -0.0484 0.0135 67 ALA A C 97 O O . ALA A 74 ? 0.3272 0.2518 0.3379 0.0990 -0.0493 0.0042 67 ALA A O 98 C CB . ALA A 74 ? 0.3301 0.3260 0.3076 0.1338 -0.0756 -0.0195 67 ALA A CB 99 N N . GLU A 75 ? 0.3350 0.2524 0.3272 0.1436 0.0017 0.0083 68 GLU A N 100 C CA . GLU A 75 ? 0.3771 0.2593 0.3135 0.1353 -0.0498 0.0295 68 GLU A CA 101 C C . GLU A 75 ? 0.3786 0.2829 0.3142 0.1262 -0.0368 0.0117 68 GLU A C 102 O O . GLU A 75 ? 0.3797 0.2617 0.3042 0.1222 -0.0224 0.0243 68 GLU A O 103 C CB . GLU A 75 ? 0.4593 0.2478 0.3589 0.0976 -0.0692 0.0634 68 GLU A CB 104 C CG . GLU A 75 ? 0.5430 0.2754 0.4328 0.0929 -0.0477 0.0241 68 GLU A CG 105 C CD . GLU A 75 ? 0.6081 0.4439 0.5099 0.0251 0.0212 -0.0653 68 GLU A CD 106 O OE1 . GLU A 75 ? 0.5206 0.3959 0.5267 0.1643 -0.0115 0.0141 68 GLU A OE1 107 O OE2 . GLU A 75 ? 0.9269 0.4293 0.6632 -0.0402 0.0912 -0.1926 68 GLU A OE2 108 N N . ASN A 76 ? 0.3703 0.2432 0.2836 0.1151 0.0026 0.0596 69 ASN A N 109 C CA . ASN A 76 ? 0.3653 0.2420 0.2789 0.1531 0.0024 0.0306 69 ASN A CA 110 C C . ASN A 76 ? 0.3396 0.2394 0.2767 0.1136 -0.0044 0.0283 69 ASN A C 111 O O . ASN A 76 ? 0.3417 0.2504 0.3032 0.0900 -0.0143 0.0083 69 ASN A O 112 C CB . ASN A 76 ? 0.4364 0.2571 0.2566 0.1121 0.0252 -0.0044 69 ASN A CB 113 C CG . ASN A 76 ? 0.4459 0.2499 0.2922 0.1375 -0.0054 0.0512 69 ASN A CG 114 O OD1 . ASN A 76 ? 0.4816 0.2417 0.3122 0.1070 0.0362 0.0417 69 ASN A OD1 115 N ND2 . ASN A 76 ? 0.4195 0.3296 0.2532 0.1426 -0.0445 0.0390 69 ASN A ND2 116 N N . ILE A 77 ? 0.3486 0.2315 0.2456 0.1038 -0.0076 0.0174 70 ILE A N 117 C CA . ILE A 77 ? 0.3257 0.1932 0.2608 0.0794 -0.0052 0.0361 70 ILE A CA 118 C C . ILE A 77 ? 0.3333 0.2364 0.2708 0.1046 -0.0069 0.0238 70 ILE A C 119 O O . ILE A 77 ? 0.2708 0.2290 0.2894 0.0665 0.0028 0.0100 70 ILE A O 120 C CB . ILE A 77 ? 0.3053 0.1908 0.2573 0.0827 0.0112 0.0295 70 ILE A CB 121 C CG1 . ILE A 77 ? 0.3048 0.2280 0.2893 0.0899 0.0134 0.0006 70 ILE A CG1 122 C CG2 . ILE A 77 ? 0.2888 0.2495 0.2266 0.1005 0.0257 0.0118 70 ILE A CG2 123 C CD1 . ILE A 77 ? 0.3192 0.2320 0.3304 0.0950 -0.0794 -0.0168 70 ILE A CD1 124 N N . LYS A 78 ? 0.2951 0.2171 0.2582 0.0882 -0.0067 0.0123 71 LYS A N 125 C CA . LYS A 78 ? 0.3165 0.1960 0.2877 0.1154 -0.0284 0.0189 71 LYS A CA 126 C C . LYS A 78 ? 0.3216 0.2668 0.2778 0.0869 -0.0151 0.0122 71 LYS A C 127 O O . LYS A 78 ? 0.3145 0.2302 0.2903 0.0591 -0.0147 -0.0031 71 LYS A O 128 C CB . LYS A 78 ? 0.2967 0.2251 0.3110 0.1298 -0.0105 0.0156 71 LYS A CB 129 C CG . LYS A 78 ? 0.2989 0.2291 0.3224 0.1570 -0.0658 -0.0002 71 LYS A CG 130 C CD . LYS A 78 ? 0.3440 0.2577 0.3464 0.1709 -0.0825 0.0618 71 LYS A CD 131 C CE . LYS A 78 ? 0.3331 0.3143 0.4035 0.1359 -0.0271 -0.0073 71 LYS A CE 132 N NZ . LYS A 78 ? 0.3801 0.3288 0.3940 0.1416 -0.0385 0.0462 71 LYS A NZ 133 N N . LYS A 79 ? 0.3285 0.2412 0.2954 0.0813 -0.0056 0.0173 72 LYS A N 134 C CA . LYS A 79 ? 0.3336 0.2552 0.2728 0.0796 -0.0038 0.0563 72 LYS A CA 135 C C . LYS A 79 ? 0.3163 0.2225 0.2802 0.0871 -0.0068 0.0198 72 LYS A C 136 O O . LYS A 79 ? 0.3156 0.2280 0.3004 0.0758 -0.0034 0.0122 72 LYS A O 137 C CB . LYS A 79 ? 0.3596 0.2864 0.2608 0.0856 -0.0012 0.0708 72 LYS A CB 138 C CG . LYS A 79 ? 0.3378 0.2543 0.2890 0.0834 0.0024 0.0542 72 LYS A CG 139 C CD . LYS A 79 ? 0.3860 0.2619 0.2791 0.0048 -0.0100 0.0707 72 LYS A CD 140 C CE . LYS A 79 ? 0.4037 0.2184 0.3138 0.0486 0.0035 0.0652 72 LYS A CE 141 N NZ . LYS A 79 ? 0.4658 0.2147 0.3116 0.0421 -0.0113 0.1099 72 LYS A NZ 142 N N . PHE A 80 ? 0.2910 0.2248 0.2624 0.0976 0.0061 0.0294 73 PHE A N 143 C CA . PHE A 80 ? 0.3016 0.1923 0.2561 0.1049 0.0113 0.0313 73 PHE A CA 144 C C . PHE A 80 ? 0.2618 0.2372 0.2574 0.0502 0.0043 0.0187 73 PHE A C 145 O O . PHE A 80 ? 0.2416 0.2222 0.2651 0.0516 0.0089 0.0246 73 PHE A O 146 C CB . PHE A 80 ? 0.2793 0.2207 0.2632 0.0954 0.0346 -0.0090 73 PHE A CB 147 C CG . PHE A 80 ? 0.3116 0.2114 0.2518 0.0999 0.0201 0.0435 73 PHE A CG 148 C CD1 . PHE A 80 ? 0.3241 0.2200 0.2571 0.0893 0.0225 0.0443 73 PHE A CD1 149 C CD2 . PHE A 80 ? 0.2973 0.2501 0.2606 0.0952 -0.0107 0.0113 73 PHE A CD2 150 C CE1 . PHE A 80 ? 0.3821 0.2604 0.2636 0.1010 0.0451 -0.0369 73 PHE A CE1 151 C CE2 . PHE A 80 ? 0.3296 0.2498 0.2945 0.1077 0.0241 0.0322 73 PHE A CE2 152 C CZ . PHE A 80 ? 0.3561 0.2207 0.3010 0.0778 -0.0414 0.0102 73 PHE A CZ 153 N N . LEU A 81 ? 0.2646 0.2317 0.2548 0.0567 0.0158 0.0286 74 LEU A N 154 C CA . LEU A 81 ? 0.2551 0.1975 0.2533 0.0581 0.0095 0.0102 74 LEU A CA 155 C C . LEU A 81 ? 0.2708 0.1945 0.2833 0.0781 -0.0121 0.0185 74 LEU A C 156 O O . LEU A 81 ? 0.2871 0.2151 0.2766 0.0469 0.0004 0.0042 74 LEU A O 157 C CB . LEU A 81 ? 0.2648 0.2226 0.2471 0.0379 0.0188 0.0404 74 LEU A CB 158 C CG . LEU A 81 ? 0.2108 0.2110 0.2310 0.0743 -0.0141 0.0244 74 LEU A CG 159 C CD1 . LEU A 81 ? 0.2481 0.1368 0.2867 0.0738 -0.0137 0.0114 74 LEU A CD1 160 C CD2 . LEU A 81 ? 0.2087 0.3055 0.2693 0.0488 -0.0370 -0.0063 74 LEU A CD2 161 N N . TYR A 82 ? 0.2566 0.1811 0.2706 0.0592 -0.0136 0.0223 75 TYR A N 162 C CA . TYR A 82 ? 0.2858 0.1763 0.3231 0.0756 -0.0312 0.0239 75 TYR A CA 163 C C . TYR A 82 ? 0.2830 0.2311 0.2951 0.0632 -0.0054 0.0173 75 TYR A C 164 O O . TYR A 82 ? 0.3097 0.2307 0.2836 0.0251 0.0141 0.0261 75 TYR A O 165 C CB . TYR A 82 ? 0.3201 0.1761 0.3237 0.0836 0.0096 0.0446 75 TYR A CB 166 C CG . TYR A 82 ? 0.3193 0.1887 0.3662 0.0759 0.0273 0.0101 75 TYR A CG 167 C CD1 . TYR A 82 ? 0.3437 0.2094 0.3392 0.1133 0.0167 0.0107 75 TYR A CD1 168 C CD2 . TYR A 82 ? 0.3456 0.2113 0.4079 0.0644 0.0268 -0.0048 75 TYR A CD2 169 C CE1 . TYR A 82 ? 0.3465 0.2148 0.3451 0.0556 -0.0259 0.0158 75 TYR A CE1 170 C CE2 . TYR A 82 ? 0.3404 0.2119 0.4219 0.0624 0.0001 -0.0094 75 TYR A CE2 171 C CZ . TYR A 82 ? 0.3641 0.2230 0.3772 0.0721 0.0013 0.0238 75 TYR A CZ 172 O OH . TYR A 82 ? 0.4908 0.2391 0.4705 0.0001 -0.0060 -0.0003 75 TYR A OH 173 N N . ASN A 83 ? 0.2799 0.1995 0.2869 0.0542 0.0037 0.0407 76 ASN A N 174 C CA . ASN A 83 ? 0.2825 0.2036 0.2811 0.0649 0.0107 0.0199 76 ASN A CA 175 C C . ASN A 83 ? 0.2796 0.2050 0.2791 0.0500 0.0189 0.0244 76 ASN A C 176 O O . ASN A 83 ? 0.2953 0.2001 0.2985 0.0244 0.0086 0.0373 76 ASN A O 177 C CB . ASN A 83 ? 0.2928 0.2389 0.3068 0.0329 0.0482 0.0336 76 ASN A CB 178 C CG . ASN A 83 ? 0.3028 0.2174 0.3093 0.0358 0.0622 0.0363 76 ASN A CG 179 O OD1 . ASN A 83 ? 0.2869 0.2409 0.3753 0.0212 0.0376 0.0628 76 ASN A OD1 180 N ND2 . ASN A 83 ? 0.3779 0.2429 0.3088 0.0229 0.1013 0.0659 76 ASN A ND2 181 N N . PHE A 84 ? 0.2829 0.1834 0.2759 0.0680 0.0163 0.0190 77 PHE A N 182 C CA . PHE A 84 ? 0.2485 0.1654 0.2627 0.0538 0.0174 0.0116 77 PHE A CA 183 C C . PHE A 84 ? 0.2487 0.1815 0.2780 0.0598 0.0229 0.0161 77 PHE A C 184 O O . PHE A 84 ? 0.2335 0.1871 0.2831 0.0556 0.0087 -0.0026 77 PHE A O 185 C CB . PHE A 84 ? 0.2785 0.1687 0.2517 0.0413 0.0220 0.0092 77 PHE A CB 186 C CG . PHE A 84 ? 0.2416 0.1874 0.2720 0.0325 0.0282 0.0120 77 PHE A CG 187 C CD1 . PHE A 84 ? 0.2218 0.2423 0.2610 0.0327 0.0245 0.0220 77 PHE A CD1 188 C CD2 . PHE A 84 ? 0.2594 0.2046 0.2519 0.0541 0.0084 -0.0283 77 PHE A CD2 189 C CE1 . PHE A 84 ? 0.3243 0.2114 0.2536 0.0459 0.0178 0.0131 77 PHE A CE1 190 C CE2 . PHE A 84 ? 0.2574 0.2247 0.2317 0.0450 0.0381 0.0051 77 PHE A CE2 191 C CZ . PHE A 84 ? 0.2663 0.2163 0.2394 0.0294 0.0175 0.0278 77 PHE A CZ 192 N N . THR A 85 ? 0.2412 0.1998 0.2893 0.0583 0.0293 -0.0173 78 THR A N 193 C CA . THR A 85 ? 0.2582 0.2000 0.2948 0.0563 0.0252 -0.0177 78 THR A CA 194 C C . THR A 85 ? 0.2681 0.1901 0.2987 0.0374 0.0075 -0.0115 78 THR A C 195 O O . THR A 85 ? 0.2551 0.2146 0.2971 0.0477 -0.0092 -0.0267 78 THR A O 196 C CB . THR A 85 ? 0.2712 0.1710 0.2740 0.0558 -0.0274 -0.0110 78 THR A CB 197 O OG1 . THR A 85 ? 0.2383 0.2018 0.2911 0.0554 0.0052 0.0120 78 THR A OG1 198 C CG2 . THR A 85 ? 0.2615 0.1744 0.2722 0.0539 -0.0156 -0.0144 78 THR A CG2 199 N N . GLN A 86 ? 0.2923 0.1669 0.2857 0.0399 0.0189 -0.0047 79 GLN A N 200 C CA . GLN A 86 ? 0.3406 0.1818 0.3403 0.0304 0.0054 -0.0217 79 GLN A CA 201 C C . GLN A 86 ? 0.3293 0.1866 0.3400 0.0353 0.0069 -0.0362 79 GLN A C 202 O O . GLN A 86 ? 0.3352 0.2219 0.3449 0.0664 0.0142 -0.0546 79 GLN A O 203 C CB . GLN A 86 ? 0.3620 0.1961 0.3454 0.0415 -0.0073 0.0095 79 GLN A CB 204 C CG . GLN A 86 ? 0.3282 0.2440 0.3827 0.0645 -0.0322 -0.0280 79 GLN A CG 205 C CD . GLN A 86 ? 0.3618 0.2945 0.4671 0.1334 0.0167 -0.0440 79 GLN A CD 206 O OE1 . GLN A 86 ? 0.4740 0.3033 0.4725 0.1459 -0.0184 -0.0606 79 GLN A OE1 207 N NE2 . GLN A 86 ? 0.3813 0.3580 0.3330 0.1282 -0.0672 -0.0407 79 GLN A NE2 208 N N . ILE A 87 ? 0.3143 0.2385 0.3267 0.0236 -0.0045 0.0082 80 ILE A N 209 C CA . ILE A 87 ? 0.2655 0.2138 0.3464 0.0322 -0.0134 0.0026 80 ILE A CA 210 C C . ILE A 87 ? 0.2686 0.2012 0.3017 0.0279 0.0279 -0.0117 80 ILE A C 211 O O . ILE A 87 ? 0.2526 0.2103 0.3059 0.0180 -0.0166 -0.0134 80 ILE A O 212 C CB . ILE A 87 ? 0.3020 0.2314 0.3799 0.0191 0.0416 0.0188 80 ILE A CB 213 C CG1 . ILE A 87 ? 0.2286 0.2900 0.3830 0.0143 0.0600 0.0226 80 ILE A CG1 214 C CG2 . ILE A 87 ? 0.2900 0.2451 0.4326 -0.0037 -0.0288 0.0366 80 ILE A CG2 215 C CD1 . ILE A 87 ? 0.2313 0.3087 0.4019 -0.0173 -0.0315 0.0302 80 ILE A CD1 216 N N . PRO A 88 ? 0.2525 0.1909 0.3100 0.0579 0.0167 -0.0294 81 PRO A N 217 C CA . PRO A 88 ? 0.2495 0.2075 0.2580 0.0454 0.0134 -0.0105 81 PRO A CA 218 C C . PRO A 88 ? 0.2420 0.1794 0.3208 0.0355 0.0148 -0.0168 81 PRO A C 219 O O . PRO A 88 ? 0.2546 0.1979 0.3388 0.0302 0.0101 -0.0021 81 PRO A O 220 C CB . PRO A 88 ? 0.2829 0.2391 0.2676 0.0722 -0.0011 -0.0540 81 PRO A CB 221 C CG . PRO A 88 ? 0.2704 0.2133 0.3230 0.0557 0.0443 -0.0025 81 PRO A CG 222 C CD . PRO A 88 ? 0.2804 0.1882 0.2753 0.0559 -0.0059 -0.0198 81 PRO A CD 223 N N . HIS A 89 ? 0.1955 0.1720 0.2718 0.0418 -0.0027 -0.0103 82 HIS A N 224 C CA . HIS A 89 ? 0.2170 0.1753 0.2454 0.0354 0.0264 -0.0103 82 HIS A CA 225 C C . HIS A 89 ? 0.2235 0.1787 0.2397 0.0285 0.0125 -0.0125 82 HIS A C 226 O O . HIS A 89 ? 0.2290 0.1842 0.2516 0.0278 -0.0060 -0.0197 82 HIS A O 227 C CB . HIS A 89 ? 0.2330 0.2070 0.2372 0.0525 0.0102 0.0015 82 HIS A CB 228 C CG . HIS A 89 ? 0.2424 0.1829 0.2703 0.0550 0.0055 0.0113 82 HIS A CG 229 N ND1 . HIS A 89 ? 0.2528 0.2214 0.2447 0.0490 -0.0119 -0.0050 82 HIS A ND1 230 C CD2 . HIS A 89 ? 0.2109 0.2104 0.2547 0.0549 0.0101 -0.0030 82 HIS A CD2 231 C CE1 . HIS A 89 ? 0.2416 0.2044 0.3213 0.0275 0.0190 0.0159 82 HIS A CE1 232 N NE2 . HIS A 89 ? 0.2341 0.1983 0.2910 0.0374 -0.0308 -0.0115 82 HIS A NE2 233 N N . LEU A 90 ? 0.2172 0.1959 0.2502 0.0062 0.0077 -0.0090 83 LEU A N 234 C CA . LEU A 90 ? 0.2297 0.1986 0.2180 0.0274 0.0018 -0.0337 83 LEU A CA 235 C C . LEU A 90 ? 0.2136 0.1676 0.2520 0.0107 -0.0032 -0.0197 83 LEU A C 236 O O . LEU A 90 ? 0.2176 0.1949 0.2735 0.0052 -0.0036 -0.0018 83 LEU A O 237 C CB . LEU A 90 ? 0.2377 0.2054 0.2128 -0.0082 0.0179 -0.0386 83 LEU A CB 238 C CG . LEU A 90 ? 0.2389 0.1192 0.2168 -0.0147 -0.0198 -0.0791 83 LEU A CG 239 C CD1 . LEU A 90 ? 0.2295 0.1652 0.2654 -0.0325 -0.0339 -0.0275 83 LEU A CD1 240 C CD2 . LEU A 90 ? 0.2610 0.2021 0.1902 0.0099 -0.0407 -0.1013 83 LEU A CD2 241 N N . ALA A 91 ? 0.2184 0.1657 0.2444 0.0286 -0.0120 -0.0254 84 ALA A N 242 C CA . ALA A 91 ? 0.1979 0.1457 0.2215 0.0027 0.0041 -0.0411 84 ALA A CA 243 C C . ALA A 91 ? 0.1816 0.1758 0.2456 0.0011 -0.0091 -0.0165 84 ALA A C 244 O O . ALA A 91 ? 0.1437 0.2072 0.2752 0.0040 0.0225 -0.0314 84 ALA A O 245 C CB . ALA A 91 ? 0.2133 0.1536 0.2643 -0.0014 0.0367 -0.0162 84 ALA A CB 246 N N . GLY A 92 ? 0.1648 0.1861 0.2671 0.0004 -0.0191 -0.0008 85 GLY A N 247 C CA . GLY A 92 ? 0.1986 0.1873 0.2752 -0.0258 -0.0191 -0.0420 85 GLY A CA 248 C C . GLY A 92 ? 0.1951 0.1854 0.3085 -0.0088 -0.0212 -0.0119 85 GLY A C 249 O O . GLY A 92 ? 0.2363 0.2374 0.3953 -0.0261 -0.0556 -0.0211 85 GLY A O 250 N N . THR A 93 ? 0.2168 0.1816 0.2700 0.0097 -0.0012 -0.0203 86 THR A N 251 C CA . THR A 93 ? 0.2201 0.1733 0.2974 0.0050 0.0364 0.0002 86 THR A CA 252 C C . THR A 93 ? 0.2006 0.1844 0.3067 0.0015 0.0238 -0.0127 86 THR A C 253 O O . THR A 93 ? 0.2412 0.1780 0.3242 0.0197 0.0176 -0.0206 86 THR A O 254 C CB . THR A 93 ? 0.2271 0.2051 0.3089 0.0199 0.0326 -0.0186 86 THR A CB 255 O OG1 . THR A 93 ? 0.2382 0.2096 0.3170 0.0155 0.0260 -0.0143 86 THR A OG1 256 C CG2 . THR A 93 ? 0.2563 0.2528 0.2733 -0.0217 0.0189 -0.0345 86 THR A CG2 257 N N . GLU A 94 ? 0.2203 0.1853 0.3399 -0.0167 0.0169 0.0121 87 GLU A N 258 C CA . GLU A 94 ? 0.2666 0.1974 0.3320 -0.0219 0.0162 0.0107 87 GLU A CA 259 C C . GLU A 94 ? 0.2646 0.2240 0.3541 -0.0055 0.0246 -0.0199 87 GLU A C 260 O O . GLU A 94 ? 0.2779 0.2046 0.3468 0.0138 0.0306 0.0050 87 GLU A O 261 C CB . GLU A 94 ? 0.3433 0.2229 0.3972 -0.0748 0.0173 0.0063 87 GLU A CB 262 C CG . GLU A 94 ? 0.4112 0.2725 0.4081 -0.0984 0.0519 -0.0158 87 GLU A CG 263 C CD . GLU A 94 ? 0.4120 0.4628 0.5299 -0.0459 0.0841 0.0260 87 GLU A CD 264 O OE1 . GLU A 94 ? 0.5021 0.5163 0.4480 -0.1125 0.0331 -0.0349 87 GLU A OE1 265 O OE2 . GLU A 94 ? 0.4168 0.5065 0.5341 -0.0179 0.0967 0.0225 87 GLU A OE2 266 N N A GLN A 95 ? 0.2620 0.1948 0.3587 0.0069 0.0215 -0.0078 88 GLN A N 267 N N B GLN A 95 ? 0.2607 0.1976 0.3729 0.0088 0.0201 -0.0085 88 GLN A N 268 C CA A GLN A 95 ? 0.2661 0.2169 0.3558 0.0122 0.0258 -0.0145 88 GLN A CA 269 C CA B GLN A 95 ? 0.2740 0.2281 0.3860 0.0080 0.0150 -0.0161 88 GLN A CA 270 C C A GLN A 95 ? 0.2524 0.1914 0.3221 0.0312 0.0458 0.0089 88 GLN A C 271 C C B GLN A 95 ? 0.2576 0.1965 0.3273 0.0350 0.0454 0.0126 88 GLN A C 272 O O A GLN A 95 ? 0.2251 0.2088 0.3206 0.0344 0.0515 0.0168 88 GLN A O 273 O O B GLN A 95 ? 0.2409 0.1821 0.3266 0.0212 0.0429 0.0176 88 GLN A O 274 C CB A GLN A 95 ? 0.2828 0.2083 0.3518 0.0674 0.0215 -0.0303 88 GLN A CB 275 C CB B GLN A 95 ? 0.3080 0.2239 0.4217 0.0552 0.0279 -0.0137 88 GLN A CB 276 C CG A GLN A 95 ? 0.3579 0.2173 0.3553 0.0665 0.0119 -0.0434 88 GLN A CG 277 C CG B GLN A 95 ? 0.3938 0.2442 0.4755 0.0157 -0.0128 -0.0423 88 GLN A CG 278 C CD A GLN A 95 ? 0.2992 0.1826 0.3351 0.1074 0.0251 -0.0240 88 GLN A CD 279 C CD B GLN A 95 ? 0.4104 0.2931 0.5731 0.0317 0.0359 0.0098 88 GLN A CD 280 O OE1 A GLN A 95 ? 0.2878 0.1136 0.2565 0.1064 0.0716 -0.0686 88 GLN A OE1 281 O OE1 B GLN A 95 ? 0.3990 0.2521 0.4637 0.0650 -0.0095 -0.0175 88 GLN A OE1 282 N NE2 A GLN A 95 ? 0.4072 0.2063 0.3950 0.0689 0.0286 -0.0485 88 GLN A NE2 283 N NE2 B GLN A 95 ? 0.4439 0.2492 0.6177 -0.0575 -0.0355 0.0210 88 GLN A NE2 284 N N . ASN A 96 ? 0.2198 0.1650 0.2988 0.0261 0.0521 -0.0129 89 ASN A N 285 C CA . ASN A 96 ? 0.2202 0.1606 0.2952 0.0039 0.0557 -0.0017 89 ASN A CA 286 C C . ASN A 96 ? 0.2314 0.2134 0.3139 -0.0060 0.0642 -0.0229 89 ASN A C 287 O O . ASN A 96 ? 0.2354 0.2555 0.2978 -0.0232 0.0471 -0.0343 89 ASN A O 288 C CB . ASN A 96 ? 0.2454 0.1575 0.2924 -0.0192 0.0351 -0.0035 89 ASN A CB 289 C CG . ASN A 96 ? 0.2853 0.1640 0.2757 -0.0003 0.0147 -0.0124 89 ASN A CG 290 O OD1 . ASN A 96 ? 0.2606 0.2280 0.2731 0.0135 0.0271 -0.0270 89 ASN A OD1 291 N ND2 . ASN A 96 ? 0.2984 0.1863 0.2857 0.0327 0.0238 0.0130 89 ASN A ND2 292 N N . PHE A 97 ? 0.2284 0.2106 0.3141 -0.0009 0.0412 0.0162 90 PHE A N 293 C CA . PHE A 97 ? 0.2408 0.2438 0.2838 -0.0154 0.0502 0.0163 90 PHE A CA 294 C C . PHE A 97 ? 0.2572 0.1986 0.3110 0.0191 0.0424 0.0149 90 PHE A C 295 O O . PHE A 97 ? 0.2391 0.2029 0.3016 0.0110 0.0579 0.0055 90 PHE A O 296 C CB A PHE A 97 ? 0.2244 0.2608 0.3311 -0.0004 0.0377 0.0239 90 PHE A CB 297 C CB B PHE A 97 ? 0.2123 0.2269 0.3037 0.0075 0.0477 0.0287 90 PHE A CB 298 C CG A PHE A 97 ? 0.2681 0.2319 0.3475 -0.0152 0.0684 0.0252 90 PHE A CG 299 C CG B PHE A 97 ? 0.2225 0.1719 0.3095 -0.0123 0.0477 0.0235 90 PHE A CG 300 C CD1 A PHE A 97 ? 0.2500 0.2303 0.3515 0.0053 0.0742 0.0260 90 PHE A CD1 301 C CD1 B PHE A 97 ? 0.2115 0.1824 0.2965 -0.0059 0.0575 0.0286 90 PHE A CD1 302 C CD2 A PHE A 97 ? 0.2877 0.2723 0.4596 -0.0451 0.0861 0.0264 90 PHE A CD2 303 C CD2 B PHE A 97 ? 0.1947 0.1698 0.3186 -0.0020 0.0389 0.0347 90 PHE A CD2 304 C CE1 A PHE A 97 ? 0.2573 0.2434 0.3770 -0.0027 0.0776 0.0201 90 PHE A CE1 305 C CE1 B PHE A 97 ? 0.2169 0.1858 0.3165 -0.0520 0.0561 0.0214 90 PHE A CE1 306 C CE2 A PHE A 97 ? 0.3072 0.3006 0.4658 -0.0090 0.1049 -0.0293 90 PHE A CE2 307 C CE2 B PHE A 97 ? 0.2310 0.1923 0.2888 0.0074 0.0508 0.0391 90 PHE A CE2 308 C CZ A PHE A 97 ? 0.2943 0.2758 0.4790 -0.0171 0.0917 -0.0339 90 PHE A CZ 309 C CZ B PHE A 97 ? 0.2652 0.1530 0.2792 -0.0069 0.0275 0.0409 90 PHE A CZ 310 N N A GLN A 98 ? 0.2466 0.1890 0.3049 0.0040 0.0448 0.0097 91 GLN A N 311 N N B GLN A 98 ? 0.2434 0.1919 0.3033 0.0051 0.0492 0.0110 91 GLN A N 312 C CA A GLN A 98 ? 0.2805 0.1826 0.3279 0.0060 0.0201 0.0178 91 GLN A CA 313 C CA B GLN A 98 ? 0.2784 0.1811 0.3290 0.0023 0.0283 0.0175 91 GLN A CA 314 C C A GLN A 98 ? 0.2613 0.1797 0.3132 0.0071 0.0476 0.0135 91 GLN A C 315 C C B GLN A 98 ? 0.2656 0.2012 0.3098 -0.0010 0.0495 0.0174 91 GLN A C 316 O O A GLN A 98 ? 0.2400 0.1815 0.3293 0.0278 0.0596 0.0208 91 GLN A O 317 O O B GLN A 98 ? 0.2838 0.2417 0.3185 0.0177 0.0596 0.0284 91 GLN A O 318 C CB A GLN A 98 ? 0.3249 0.1947 0.3502 0.0065 0.0445 -0.0091 91 GLN A CB 319 C CB B GLN A 98 ? 0.2834 0.1968 0.3442 0.0091 0.0634 0.0089 91 GLN A CB 320 C CG A GLN A 98 ? 0.3288 0.2605 0.3897 -0.0198 0.0177 -0.0012 91 GLN A CG 321 C CG B GLN A 98 ? 0.3259 0.2323 0.3708 -0.0262 0.0272 0.0287 91 GLN A CG 322 C CD A GLN A 98 ? 0.3561 0.3899 0.4534 -0.0250 0.0439 0.0497 91 GLN A CD 323 C CD B GLN A 98 ? 0.3765 0.2491 0.4481 0.0102 0.0440 0.0188 91 GLN A CD 324 O OE1 A GLN A 98 ? 0.3350 0.4541 0.5673 -0.0319 0.0578 0.0431 91 GLN A OE1 325 O OE1 B GLN A 98 ? 0.3326 0.3327 0.5568 -0.0221 0.0429 0.1067 91 GLN A OE1 326 N NE2 A GLN A 98 ? 0.3827 0.3277 0.4730 -0.0573 -0.0091 0.0445 91 GLN A NE2 327 N NE2 B GLN A 98 ? 0.3962 0.3567 0.4932 -0.0583 0.0142 0.0545 91 GLN A NE2 328 N N . LEU A 99 ? 0.2504 0.1836 0.3298 -0.0052 0.0351 0.0079 92 LEU A N 329 C CA . LEU A 99 ? 0.2334 0.1928 0.2900 -0.0028 0.0760 0.0031 92 LEU A CA 330 C C . LEU A 99 ? 0.2675 0.1961 0.2753 0.0471 0.0427 0.0243 92 LEU A C 331 O O . LEU A 99 ? 0.2530 0.2075 0.2639 0.0282 0.0587 0.0179 92 LEU A O 332 C CB . LEU A 99 ? 0.2193 0.2067 0.2572 0.0151 0.0867 -0.0169 92 LEU A CB 333 C CG . LEU A 99 ? 0.2178 0.2044 0.2481 0.0437 0.0434 0.0381 92 LEU A CG 334 C CD1 . LEU A 99 ? 0.2951 0.2171 0.2999 0.0454 -0.0087 0.0565 92 LEU A CD1 335 C CD2 . LEU A 99 ? 0.2182 0.2149 0.2245 0.0130 0.0367 0.0190 92 LEU A CD2 336 N N . ALA A 100 ? 0.2333 0.1829 0.2794 0.0261 0.0290 0.0270 93 ALA A N 337 C CA . ALA A 100 ? 0.2505 0.1940 0.2427 0.0404 0.0399 0.0430 93 ALA A CA 338 C C . ALA A 100 ? 0.2739 0.1895 0.2756 0.0309 0.0538 0.0439 93 ALA A C 339 O O . ALA A 100 ? 0.2725 0.2238 0.2727 0.0480 0.0752 0.0304 93 ALA A O 340 C CB . ALA A 100 ? 0.2230 0.1985 0.2858 0.0568 0.0283 0.0398 93 ALA A CB 341 N N . LYS A 101 ? 0.2296 0.2093 0.2780 0.0142 0.0508 0.0478 94 LYS A N 342 C CA . LYS A 101 ? 0.2698 0.1949 0.2912 0.0039 0.0649 0.0541 94 LYS A CA 343 C C . LYS A 101 ? 0.2864 0.2270 0.3119 0.0451 0.0605 0.0505 94 LYS A C 344 O O . LYS A 101 ? 0.3150 0.2164 0.3006 0.0558 0.0397 0.0476 94 LYS A O 345 C CB . LYS A 101 ? 0.2451 0.2247 0.3516 0.0009 0.0580 0.0286 94 LYS A CB 346 C CG . LYS A 101 ? 0.3067 0.2400 0.3218 -0.0206 0.0422 0.0823 94 LYS A CG 347 C CD . LYS A 101 ? 0.3632 0.3072 0.4786 -0.0420 0.0273 0.0087 94 LYS A CD 348 C CE . LYS A 101 ? 0.3558 0.3068 0.4392 -0.0157 0.0650 0.0460 94 LYS A CE 349 N NZ . LYS A 101 ? 0.2704 0.3233 0.4373 -0.0210 0.1083 0.0537 94 LYS A NZ 350 N N . GLN A 102 ? 0.3014 0.2298 0.2924 0.0707 0.0429 0.0269 95 GLN A N 351 C CA . GLN A 102 ? 0.2983 0.1937 0.3275 0.0699 0.0272 0.0280 95 GLN A CA 352 C C . GLN A 102 ? 0.2995 0.2078 0.2899 0.0360 0.0419 0.0501 95 GLN A C 353 O O . GLN A 102 ? 0.2673 0.2265 0.2958 0.0597 0.0627 0.0442 95 GLN A O 354 C CB . GLN A 102 ? 0.3174 0.2284 0.3226 0.0993 0.0293 0.0269 95 GLN A CB 355 C CG . GLN A 102 ? 0.3218 0.2542 0.3544 0.0860 0.0163 0.0233 95 GLN A CG 356 C CD . GLN A 102 ? 0.3353 0.2380 0.3063 0.0364 0.0594 0.0243 95 GLN A CD 357 O OE1 . GLN A 102 ? 0.3286 0.2167 0.3399 0.0661 0.0341 0.0073 95 GLN A OE1 358 N NE2 . GLN A 102 ? 0.3129 0.2271 0.3717 0.0612 0.0337 0.0192 95 GLN A NE2 359 N N . ILE A 103 ? 0.2922 0.1764 0.2932 0.0567 0.0579 0.0413 96 ILE A N 360 C CA . ILE A 103 ? 0.2733 0.1792 0.2777 0.0678 0.0491 0.0402 96 ILE A CA 361 C C . ILE A 103 ? 0.2847 0.2385 0.2472 0.0567 0.0573 0.0342 96 ILE A C 362 O O . ILE A 103 ? 0.2890 0.2341 0.2428 0.0492 0.0244 0.0232 96 ILE A O 363 C CB . ILE A 103 ? 0.2977 0.1790 0.2802 0.0424 0.0746 0.0219 96 ILE A CB 364 C CG1 A ILE A 103 ? 0.2747 0.2736 0.3132 0.0578 0.0503 -0.0177 96 ILE A CG1 365 C CG1 B ILE A 103 ? 0.2851 0.2313 0.2615 0.0364 0.0703 0.0203 96 ILE A CG1 366 C CG2 . ILE A 103 ? 0.2825 0.2057 0.2828 0.0289 0.0361 0.0072 96 ILE A CG2 367 C CD1 A ILE A 103 ? 0.2997 0.2247 0.3573 0.0596 0.0162 0.0245 96 ILE A CD1 368 C CD1 B ILE A 103 ? 0.3109 0.1792 0.2533 0.0076 0.0689 -0.0014 96 ILE A CD1 369 N N . GLN A 104 ? 0.2641 0.2153 0.2901 0.0485 0.0611 0.0344 97 GLN A N 370 C CA . GLN A 104 ? 0.2590 0.2703 0.2612 0.0652 0.0511 0.0448 97 GLN A CA 371 C C . GLN A 104 ? 0.3127 0.2397 0.2850 0.0545 0.0665 0.0482 97 GLN A C 372 O O . GLN A 104 ? 0.3034 0.2616 0.2753 0.0444 0.0404 0.0444 97 GLN A O 373 C CB . GLN A 104 ? 0.2383 0.2538 0.2971 0.0705 0.0513 0.0630 97 GLN A CB 374 C CG . GLN A 104 ? 0.2768 0.2811 0.3027 0.0761 0.0696 0.0391 97 GLN A CG 375 C CD . GLN A 104 ? 0.2529 0.2405 0.3579 0.0716 0.0640 0.0497 97 GLN A CD 376 O OE1 . GLN A 104 ? 0.3029 0.2956 0.3486 0.0507 0.0395 0.0246 97 GLN A OE1 377 N NE2 . GLN A 104 ? 0.2471 0.2838 0.3523 0.0936 0.0458 0.0673 97 GLN A NE2 378 N N . SER A 105 ? 0.3366 0.2324 0.3014 0.0665 0.0364 0.0818 98 SER A N 379 C CA . SER A 105 ? 0.3450 0.2331 0.2996 0.0327 0.0750 0.0685 98 SER A CA 380 C C . SER A 105 ? 0.3457 0.2460 0.3071 0.0450 0.0687 0.0664 98 SER A C 381 O O . SER A 105 ? 0.3206 0.2543 0.3013 0.0572 0.0797 0.0811 98 SER A O 382 C CB . SER A 105 ? 0.3475 0.2300 0.3278 -0.0274 0.0496 0.0807 98 SER A CB 383 O OG A SER A 105 ? 0.3161 0.2374 0.2847 0.0434 0.0169 0.0822 98 SER A OG 384 O OG B SER A 105 ? 0.3077 0.3063 0.3605 -0.0036 0.1079 -0.0247 98 SER A OG 385 N N . GLN A 106 ? 0.3287 0.1892 0.3322 0.0585 0.0596 0.0613 99 GLN A N 386 C CA . GLN A 106 ? 0.3347 0.2537 0.2913 0.0589 0.0743 0.0451 99 GLN A CA 387 C C . GLN A 106 ? 0.3454 0.2230 0.2606 0.0656 0.0650 0.0754 99 GLN A C 388 O O . GLN A 106 ? 0.3537 0.2760 0.2591 0.0622 0.0629 0.0592 99 GLN A O 389 C CB . GLN A 106 ? 0.3191 0.2233 0.3103 0.0789 0.0602 0.0507 99 GLN A CB 390 C CG . GLN A 106 ? 0.3413 0.2253 0.3441 0.0760 0.0576 0.0508 99 GLN A CG 391 C CD . GLN A 106 ? 0.3872 0.2537 0.3568 0.0886 0.0976 0.0560 99 GLN A CD 392 O OE1 . GLN A 106 ? 0.3525 0.3181 0.3606 0.0501 0.1543 0.0340 99 GLN A OE1 393 N NE2 . GLN A 106 ? 0.4296 0.4222 0.5076 0.1254 0.0085 0.1107 99 GLN A NE2 394 N N . TRP A 107 ? 0.3253 0.2279 0.2701 0.0881 0.0616 0.0635 100 TRP A N 395 C CA . TRP A 107 ? 0.3420 0.2066 0.2316 0.0830 0.0659 0.0823 100 TRP A CA 396 C C . TRP A 107 ? 0.3474 0.2643 0.2499 0.0815 0.0781 0.0618 100 TRP A C 397 O O . TRP A 107 ? 0.3654 0.2467 0.2833 0.0716 0.0702 0.0631 100 TRP A O 398 C CB . TRP A 107 ? 0.3719 0.2175 0.1870 0.0819 0.0585 0.0643 100 TRP A CB 399 C CG . TRP A 107 ? 0.3101 0.1992 0.2293 0.0786 0.0212 0.0516 100 TRP A CG 400 C CD1 . TRP A 107 ? 0.2924 0.2404 0.2396 0.0544 0.0393 0.0051 100 TRP A CD1 401 C CD2 . TRP A 107 ? 0.2930 0.1831 0.2097 0.0514 0.0168 0.0336 100 TRP A CD2 402 N NE1 . TRP A 107 ? 0.2806 0.2331 0.2561 0.0856 0.0342 0.0428 100 TRP A NE1 403 C CE2 . TRP A 107 ? 0.3100 0.1998 0.2484 0.0730 0.0082 0.0251 100 TRP A CE2 404 C CE3 . TRP A 107 ? 0.2613 0.1849 0.2307 0.0471 0.0175 0.0391 100 TRP A CE3 405 C CZ2 . TRP A 107 ? 0.3154 0.2147 0.2474 0.0407 -0.0035 0.0232 100 TRP A CZ2 406 C CZ3 . TRP A 107 ? 0.3049 0.2331 0.2031 0.0221 0.0315 0.0215 100 TRP A CZ3 407 C CH2 . TRP A 107 ? 0.2769 0.2008 0.2637 0.0493 0.0034 -0.0071 100 TRP A CH2 408 N N . LYS A 108 ? 0.3812 0.2575 0.3021 0.0534 0.0964 0.1009 101 LYS A N 409 C CA . LYS A 108 ? 0.4000 0.3277 0.2853 0.0684 0.1030 0.1061 101 LYS A CA 410 C C . LYS A 108 ? 0.4077 0.2912 0.2825 0.0872 0.1019 0.0964 101 LYS A C 411 O O . LYS A 108 ? 0.3983 0.3110 0.3124 0.0924 0.1086 0.0660 101 LYS A O 412 C CB . LYS A 108 ? 0.4035 0.3536 0.3592 0.0821 0.0643 0.0941 101 LYS A CB 413 C CG . LYS A 108 ? 0.4296 0.4416 0.3917 0.0882 0.0144 0.0616 101 LYS A CG 414 C CD . LYS A 108 ? 0.4526 0.4675 0.5964 -0.0164 0.0303 0.1386 101 LYS A CD 415 C CE . LYS A 108 ? 0.4601 0.5336 0.5100 -0.0251 0.0185 0.1436 101 LYS A CE 416 N NZ . LYS A 108 ? 0.3947 0.7207 0.7069 -0.0033 -0.0083 0.2099 101 LYS A NZ 417 N N A GLU A 109 ? 0.3865 0.2852 0.3138 0.0828 0.0942 0.0988 102 GLU A N 418 N N B GLU A 109 ? 0.3923 0.2834 0.2984 0.0835 0.0885 0.0998 102 GLU A N 419 C CA A GLU A 109 ? 0.4203 0.3127 0.2954 0.1033 0.0808 0.0845 102 GLU A CA 420 C CA B GLU A 109 ? 0.4137 0.2751 0.2876 0.1092 0.0830 0.0786 102 GLU A CA 421 C C A GLU A 109 ? 0.4065 0.3065 0.2926 0.1032 0.0911 0.0967 102 GLU A C 422 C C B GLU A 109 ? 0.4128 0.2889 0.2853 0.0982 0.0852 0.0970 102 GLU A C 423 O O A GLU A 109 ? 0.4055 0.3055 0.2955 0.1023 0.0735 0.0874 102 GLU A O 424 O O B GLU A 109 ? 0.4261 0.2999 0.2908 0.0963 0.0590 0.0808 102 GLU A O 425 C CB A GLU A 109 ? 0.4812 0.3069 0.3294 0.1137 0.0676 0.0607 102 GLU A CB 426 C CB B GLU A 109 ? 0.4299 0.2478 0.3240 0.0883 0.0442 0.0658 102 GLU A CB 427 C CG A GLU A 109 ? 0.5180 0.4332 0.4140 0.0568 0.0474 0.0315 102 GLU A CG 428 C CG B GLU A 109 ? 0.5195 0.2124 0.3566 0.1184 0.0403 0.1035 102 GLU A CG 429 C CD A GLU A 109 ? 0.5352 0.4551 0.4941 0.1333 -0.0177 -0.0168 102 GLU A CD 430 C CD B GLU A 109 ? 0.5193 0.3629 0.3890 0.1170 0.0624 0.1065 102 GLU A CD 431 O OE1 A GLU A 109 ? 0.6705 0.2755 0.4354 0.1222 -0.0224 0.0280 102 GLU A OE1 432 O OE1 B GLU A 109 ? 0.5403 0.3723 0.6236 0.0502 0.0207 0.1153 102 GLU A OE1 433 O OE2 A GLU A 109 ? 0.5213 0.3817 0.4765 0.1497 0.0108 0.0207 102 GLU A OE2 434 O OE2 B GLU A 109 ? 0.6538 0.3597 0.4165 0.1641 0.0287 0.1918 102 GLU A OE2 435 N N . PHE A 110 ? 0.4344 0.2552 0.2806 0.1017 0.0621 0.1084 103 PHE A N 436 C CA . PHE A 110 ? 0.4058 0.2648 0.2763 0.1125 0.0884 0.0785 103 PHE A CA 437 C C . PHE A 110 ? 0.4011 0.3077 0.2320 0.0937 0.0989 0.0746 103 PHE A C 438 O O . PHE A 110 ? 0.4095 0.3604 0.3024 0.1354 0.0520 0.0367 103 PHE A O 439 C CB . PHE A 110 ? 0.4183 0.3061 0.2247 0.0946 0.0785 0.0557 103 PHE A CB 440 C CG . PHE A 110 ? 0.3745 0.2923 0.2578 0.0962 0.0372 0.0302 103 PHE A CG 441 C CD1 . PHE A 110 ? 0.3864 0.3028 0.2931 0.1209 0.0306 0.0334 103 PHE A CD1 442 C CD2 . PHE A 110 ? 0.3763 0.3216 0.2630 0.1042 0.0600 0.0246 103 PHE A CD2 443 C CE1 . PHE A 110 ? 0.4341 0.3495 0.3029 0.1053 0.0680 0.0163 103 PHE A CE1 444 C CE2 . PHE A 110 ? 0.3546 0.2813 0.2621 0.0952 0.0314 0.0189 103 PHE A CE2 445 C CZ . PHE A 110 ? 0.4185 0.3067 0.3168 0.0933 0.0207 0.0542 103 PHE A CZ 446 N N . GLY A 111 ? 0.4207 0.2608 0.2695 0.1170 0.0707 0.0756 104 GLY A N 447 C CA . GLY A 111 ? 0.4531 0.2598 0.2285 0.0907 0.0812 0.0731 104 GLY A CA 448 C C . GLY A 111 ? 0.4054 0.2842 0.2379 0.1024 0.0435 0.0505 104 GLY A C 449 O O . GLY A 111 ? 0.4075 0.3052 0.2535 0.0980 0.0860 0.0403 104 GLY A O 450 N N . LEU A 112 ? 0.4272 0.2525 0.2409 0.0995 0.0747 0.0685 105 LEU A N 451 C CA . LEU A 112 ? 0.3950 0.2443 0.1942 0.0598 0.0619 0.0900 105 LEU A CA 452 C C . LEU A 112 ? 0.4115 0.2446 0.2556 0.0911 0.0785 0.0707 105 LEU A C 453 O O . LEU A 112 ? 0.4052 0.2779 0.3345 0.0669 0.1209 0.0716 105 LEU A O 454 C CB . LEU A 112 ? 0.3606 0.2546 0.2093 0.0778 0.1183 0.0739 105 LEU A CB 455 C CG . LEU A 112 ? 0.3198 0.2501 0.2300 0.0566 0.0717 0.0541 105 LEU A CG 456 C CD1 . LEU A 112 ? 0.3813 0.2530 0.2427 0.0976 0.0456 0.0691 105 LEU A CD1 457 C CD2 . LEU A 112 ? 0.4057 0.2619 0.1948 0.1037 0.0475 0.0184 105 LEU A CD2 458 N N . ASP A 113 ? 0.3833 0.2470 0.2541 0.0876 0.0685 0.0668 106 ASP A N 459 C CA . ASP A 113 ? 0.4097 0.2980 0.2602 0.0821 0.1014 0.0462 106 ASP A CA 460 C C . ASP A 113 ? 0.3944 0.2902 0.2685 0.0536 0.0897 0.0945 106 ASP A C 461 O O . ASP A 113 ? 0.3760 0.3532 0.2959 0.0492 0.1570 0.0488 106 ASP A O 462 C CB . ASP A 113 ? 0.4293 0.2755 0.2597 0.0683 0.1129 0.0611 106 ASP A CB 463 C CG . ASP A 113 ? 0.4437 0.2836 0.2007 0.0841 0.1465 0.0624 106 ASP A CG 464 O OD1 . ASP A 113 ? 0.5100 0.3063 0.2479 0.0173 0.1351 0.1047 106 ASP A OD1 465 O OD2 . ASP A 113 ? 0.4566 0.2846 0.2546 0.0848 0.0565 0.0520 106 ASP A OD2 466 N N . SER A 114 ? 0.3702 0.3081 0.2265 0.0887 0.0762 0.0429 107 SER A N 467 C CA . SER A 114 ? 0.3403 0.2887 0.2706 0.0685 0.0948 0.0110 107 SER A CA 468 C C . SER A 114 ? 0.3206 0.2205 0.2646 0.0686 0.0874 0.0324 107 SER A C 469 O O . SER A 114 ? 0.2772 0.2658 0.2532 0.0615 0.0648 0.0391 107 SER A O 470 C CB . SER A 114 ? 0.3622 0.3473 0.2946 0.0562 0.0465 0.0904 107 SER A CB 471 O OG A SER A 114 ? 0.3309 0.2639 0.2180 0.1331 0.0880 0.0444 107 SER A OG 472 O OG B SER A 114 ? 0.4420 0.4858 0.3182 0.1108 0.0568 0.0475 107 SER A OG 473 N N . VAL A 115 ? 0.3171 0.2624 0.2416 0.0601 0.0641 0.0285 108 VAL A N 474 C CA . VAL A 115 ? 0.3093 0.2467 0.2417 0.0650 0.0730 0.0328 108 VAL A CA 475 C C . VAL A 115 ? 0.3003 0.2640 0.2588 0.0365 0.0491 0.0628 108 VAL A C 476 O O . VAL A 115 ? 0.3078 0.2839 0.2772 0.0152 0.0720 0.0367 108 VAL A O 477 C CB . VAL A 115 ? 0.2898 0.2882 0.2369 0.0660 0.0351 0.0418 108 VAL A CB 478 C CG1 . VAL A 115 ? 0.2744 0.2604 0.2649 0.0514 0.0383 0.0194 108 VAL A CG1 479 C CG2 . VAL A 115 ? 0.2945 0.2585 0.2046 0.0639 0.0456 0.0549 108 VAL A CG2 480 N N . GLU A 116 ? 0.2671 0.2665 0.2518 0.0458 0.0890 0.0589 109 GLU A N 481 C CA . GLU A 116 ? 0.2952 0.2798 0.2632 0.0552 0.0643 0.0442 109 GLU A CA 482 C C . GLU A 116 ? 0.2593 0.2440 0.2696 0.0291 0.0685 0.0306 109 GLU A C 483 O O . GLU A 116 ? 0.2939 0.3205 0.2806 -0.0249 0.0471 0.0188 109 GLU A O 484 C CB . GLU A 116 ? 0.3325 0.3398 0.3788 0.1065 0.0532 -0.0008 109 GLU A CB 485 C CG . GLU A 116 ? 0.4052 0.4786 0.3848 0.0587 0.0812 0.0298 109 GLU A CG 486 C CD . GLU A 116 ? 0.4620 0.5986 0.4800 -0.0186 0.0882 0.0370 109 GLU A CD 487 O OE1 . GLU A 116 ? 0.5262 0.6523 0.5233 0.0117 0.1196 -0.0470 109 GLU A OE1 488 O OE2 . GLU A 116 ? 0.4561 0.8614 0.4670 -0.0679 0.0663 0.0167 109 GLU A OE2 489 N N . LEU A 117 ? 0.2347 0.2512 0.2600 0.0238 0.0515 0.0598 110 LEU A N 490 C CA . LEU A 117 ? 0.2339 0.2180 0.2654 0.0428 0.0630 0.0447 110 LEU A CA 491 C C . LEU A 117 ? 0.2326 0.2765 0.2871 0.0590 0.0576 0.0711 110 LEU A C 492 O O . LEU A 117 ? 0.2250 0.3341 0.3444 0.0295 0.0440 0.1106 110 LEU A O 493 C CB . LEU A 117 ? 0.2881 0.2261 0.3213 0.0453 0.0324 0.0277 110 LEU A CB 494 C CG . LEU A 117 ? 0.3092 0.2200 0.3752 0.0422 -0.0140 0.0156 110 LEU A CG 495 C CD1 . LEU A 117 ? 0.4006 0.2614 0.3661 0.0720 -0.0117 -0.0342 110 LEU A CD1 496 C CD2 . LEU A 117 ? 0.2959 0.2674 0.3855 0.0295 0.0202 -0.0359 110 LEU A CD2 497 N N . ALA A 118 ? 0.2621 0.2019 0.2556 0.0277 0.0254 0.0285 111 ALA A N 498 C CA . ALA A 118 ? 0.2359 0.2029 0.2294 0.0085 0.0124 0.0126 111 ALA A CA 499 C C . ALA A 118 ? 0.2478 0.2377 0.2382 -0.0014 0.0238 0.0159 111 ALA A C 500 O O . ALA A 118 ? 0.2643 0.2759 0.2390 0.0271 0.0462 0.0191 111 ALA A O 501 C CB . ALA A 118 ? 0.2976 0.2203 0.2456 -0.0235 0.0360 -0.0044 111 ALA A CB 502 N N . HIS A 119 ? 0.2246 0.2165 0.2256 0.0031 0.0320 0.0154 112 HIS A N 503 C CA . HIS A 119 ? 0.2291 0.1836 0.2275 0.0210 0.0435 0.0163 112 HIS A CA 504 C C . HIS A 119 ? 0.2028 0.2011 0.2365 0.0178 0.0291 0.0205 112 HIS A C 505 O O . HIS A 119 ? 0.2147 0.2320 0.2141 0.0300 0.0449 0.0162 112 HIS A O 506 C CB . HIS A 119 ? 0.2175 0.2155 0.2811 -0.0064 0.0276 0.0255 112 HIS A CB 507 C CG . HIS A 119 ? 0.2209 0.2717 0.3302 0.0027 0.0403 0.0136 112 HIS A CG 508 N ND1 . HIS A 119 ? 0.2243 0.3729 0.3612 -0.0139 0.0518 0.0394 112 HIS A ND1 509 C CD2 . HIS A 119 ? 0.2296 0.2995 0.3252 0.0108 0.0225 0.0042 112 HIS A CD2 510 C CE1 . HIS A 119 ? 0.2370 0.3666 0.3992 0.0294 0.0337 0.0200 112 HIS A CE1 511 N NE2 . HIS A 119 ? 0.2226 0.3178 0.3927 0.0013 0.0280 -0.0230 112 HIS A NE2 512 N N . TYR A 120 ? 0.2037 0.2081 0.2269 0.0046 0.0139 0.0208 113 TYR A N 513 C CA . TYR A 120 ? 0.2268 0.1832 0.2090 -0.0032 0.0146 0.0072 113 TYR A CA 514 C C . TYR A 120 ? 0.1771 0.1907 0.2310 -0.0182 0.0332 -0.0070 113 TYR A C 515 O O . TYR A 120 ? 0.2306 0.1985 0.2357 0.0018 0.0175 -0.0112 113 TYR A O 516 C CB . TYR A 120 ? 0.1968 0.1914 0.2075 0.0002 0.0269 -0.0017 113 TYR A CB 517 C CG . TYR A 120 ? 0.2165 0.1787 0.2136 0.0375 0.0403 -0.0041 113 TYR A CG 518 C CD1 . TYR A 120 ? 0.2255 0.1627 0.2299 0.0360 0.0472 0.0098 113 TYR A CD1 519 C CD2 . TYR A 120 ? 0.2163 0.2088 0.2145 0.0085 0.0191 -0.0034 113 TYR A CD2 520 C CE1 . TYR A 120 ? 0.2733 0.2005 0.2293 -0.0068 0.0147 0.0044 113 TYR A CE1 521 C CE2 . TYR A 120 ? 0.1996 0.2140 0.2046 0.0170 0.0220 0.0043 113 TYR A CE2 522 C CZ . TYR A 120 ? 0.2752 0.1956 0.2106 0.0365 0.0336 -0.0094 113 TYR A CZ 523 O OH . TYR A 120 ? 0.2960 0.2271 0.1965 -0.0039 0.0204 -0.0098 113 TYR A OH 524 N N . ASP A 121 ? 0.1849 0.1972 0.2194 -0.0001 0.0252 -0.0148 114 ASP A N 525 C CA . ASP A 121 ? 0.1927 0.1950 0.2281 -0.0258 0.0071 -0.0228 114 ASP A CA 526 C C . ASP A 121 ? 0.1826 0.2043 0.2461 -0.0180 0.0168 -0.0124 114 ASP A C 527 O O . ASP A 121 ? 0.2265 0.1941 0.2530 0.0014 0.0140 -0.0419 114 ASP A O 528 C CB . ASP A 121 ? 0.1669 0.2062 0.2872 -0.0239 0.0205 0.0103 114 ASP A CB 529 C CG . ASP A 121 ? 0.2132 0.2272 0.2916 -0.0239 0.0090 0.0381 114 ASP A CG 530 O OD1 . ASP A 121 ? 0.2385 0.2086 0.3383 -0.0299 -0.0051 0.0452 114 ASP A OD1 531 O OD2 . ASP A 121 ? 0.2498 0.3465 0.3167 0.0117 0.0238 0.0389 114 ASP A OD2 532 N N . VAL A 122 ? 0.1953 0.1950 0.2373 -0.0234 0.0147 -0.0221 115 VAL A N 533 C CA . VAL A 122 ? 0.1989 0.1965 0.2216 -0.0227 0.0206 -0.0357 115 VAL A CA 534 C C . VAL A 122 ? 0.2019 0.2032 0.2087 -0.0038 0.0206 -0.0158 115 VAL A C 535 O O . VAL A 122 ? 0.1799 0.2083 0.2268 0.0052 0.0099 -0.0219 115 VAL A O 536 C CB . VAL A 122 ? 0.1833 0.1586 0.2051 0.0035 0.0138 -0.0179 115 VAL A CB 537 C CG1 . VAL A 122 ? 0.2017 0.1939 0.1919 -0.0005 0.0215 -0.0265 115 VAL A CG1 538 C CG2 . VAL A 122 ? 0.1477 0.2012 0.2106 0.0194 0.0212 -0.0118 115 VAL A CG2 539 N N . LEU A 123 ? 0.1655 0.2033 0.1702 0.0152 0.0230 -0.0242 116 LEU A N 540 C CA . LEU A 123 ? 0.1857 0.1861 0.1795 0.0320 0.0143 -0.0368 116 LEU A CA 541 C C . LEU A 123 ? 0.1847 0.1933 0.2274 0.0184 0.0046 -0.0324 116 LEU A C 542 O O . LEU A 123 ? 0.2134 0.2059 0.2219 0.0116 -0.0017 -0.0443 116 LEU A O 543 C CB . LEU A 123 ? 0.1869 0.1822 0.1548 0.0331 0.0212 -0.0361 116 LEU A CB 544 C CG . LEU A 123 ? 0.2302 0.1874 0.1676 -0.0219 0.0417 -0.0531 116 LEU A CG 545 C CD1 . LEU A 123 ? 0.2442 0.2122 0.2588 -0.0221 -0.0128 -0.0364 116 LEU A CD1 546 C CD2 . LEU A 123 ? 0.3098 0.2102 0.2158 -0.0420 -0.0158 0.0056 116 LEU A CD2 547 N N . LEU A 124 ? 0.1924 0.1882 0.2299 0.0168 0.0157 -0.0257 117 LEU A N 548 C CA . LEU A 124 ? 0.1987 0.2056 0.2075 0.0215 0.0278 -0.0265 117 LEU A CA 549 C C . LEU A 124 ? 0.2097 0.2088 0.2119 0.0286 0.0171 -0.0334 117 LEU A C 550 O O . LEU A 124 ? 0.1731 0.2535 0.2227 0.0238 0.0020 -0.0507 117 LEU A O 551 C CB . LEU A 124 ? 0.2114 0.2023 0.2111 0.0050 0.0019 -0.0257 117 LEU A CB 552 C CG . LEU A 124 ? 0.2015 0.1310 0.2167 -0.0159 0.0141 -0.0265 117 LEU A CG 553 C CD1 . LEU A 124 ? 0.2004 0.1805 0.2272 0.0108 0.0330 0.0063 117 LEU A CD1 554 C CD2 . LEU A 124 ? 0.1991 0.1812 0.2098 -0.0281 0.0128 -0.0697 117 LEU A CD2 555 N N . SER A 125 ? 0.1760 0.2089 0.2064 0.0025 0.0436 -0.0383 118 SER A N 556 C CA . SER A 125 ? 0.2302 0.2191 0.2131 0.0053 0.0371 -0.0483 118 SER A CA 557 C C . SER A 125 ? 0.2206 0.2305 0.2369 0.0168 0.0273 -0.0625 118 SER A C 558 O O . SER A 125 ? 0.2389 0.2204 0.2606 0.0055 0.0143 -0.0521 118 SER A O 559 C CB . SER A 125 ? 0.2111 0.2523 0.2057 0.0104 0.0478 -0.0318 118 SER A CB 560 O OG . SER A 125 ? 0.2187 0.2604 0.2128 0.0204 0.0417 -0.0507 118 SER A OG 561 N N . TYR A 126 ? 0.2650 0.1945 0.2859 0.0188 0.0509 -0.0610 119 TYR A N 562 C CA . TYR A 126 ? 0.2344 0.1937 0.2439 0.0139 0.0262 -0.0463 119 TYR A CA 563 C C . TYR A 126 ? 0.2490 0.2385 0.2662 0.0238 0.0246 -0.0653 119 TYR A C 564 O O . TYR A 126 ? 0.2466 0.2499 0.2854 0.0053 0.0128 -0.0628 119 TYR A O 565 C CB . TYR A 126 ? 0.2309 0.2262 0.2431 0.0115 0.0380 -0.0573 119 TYR A CB 566 C CG . TYR A 126 ? 0.2261 0.2446 0.2200 -0.0028 0.0130 -0.0546 119 TYR A CG 567 C CD1 . TYR A 126 ? 0.2414 0.2643 0.2286 0.0040 -0.0019 -0.0798 119 TYR A CD1 568 C CD2 . TYR A 126 ? 0.2329 0.2687 0.2408 -0.0005 0.0160 -0.0543 119 TYR A CD2 569 C CE1 . TYR A 126 ? 0.2650 0.2355 0.2709 0.0148 0.0391 -0.0631 119 TYR A CE1 570 C CE2 . TYR A 126 ? 0.2897 0.3038 0.2466 0.0193 -0.0056 -0.1043 119 TYR A CE2 571 C CZ . TYR A 126 ? 0.2451 0.2807 0.2626 0.0033 0.0000 -0.0976 119 TYR A CZ 572 O OH . TYR A 126 ? 0.2016 0.2758 0.2692 0.0170 0.0177 -0.0786 119 TYR A OH 573 N N . PRO A 127 ? 0.2278 0.2218 0.2775 0.0093 0.0261 -0.0742 120 PRO A N 574 C CA . PRO A 127 ? 0.2703 0.2353 0.3011 0.0100 -0.0055 -0.1137 120 PRO A CA 575 C C . PRO A 127 ? 0.2837 0.2611 0.3137 -0.0125 0.0288 -0.1176 120 PRO A C 576 O O . PRO A 127 ? 0.3034 0.2555 0.3780 -0.0165 0.0475 -0.0970 120 PRO A O 577 C CB . PRO A 127 ? 0.2667 0.2671 0.3345 0.0208 -0.0127 -0.0986 120 PRO A CB 578 C CG . PRO A 127 ? 0.2455 0.2572 0.3131 0.0697 0.0071 -0.1266 120 PRO A CG 579 C CD . PRO A 127 ? 0.2328 0.2420 0.2646 0.0397 0.0138 -0.0948 120 PRO A CD 580 N N . ASN A 128 ? 0.3288 0.2479 0.3104 -0.0246 0.0046 -0.1231 121 ASN A N 581 C CA . ASN A 128 ? 0.3458 0.2805 0.3831 -0.0409 -0.0366 -0.1240 121 ASN A CA 582 C C . ASN A 128 ? 0.3816 0.3005 0.4002 -0.0150 0.0116 -0.1256 121 ASN A C 583 O O . ASN A 128 ? 0.3099 0.2798 0.4554 0.0015 -0.0317 -0.1451 121 ASN A O 584 C CB . ASN A 128 ? 0.3480 0.2959 0.3751 -0.0258 -0.0559 -0.1585 121 ASN A CB 585 C CG . ASN A 128 ? 0.3836 0.3286 0.4547 -0.0633 -0.0712 -0.1382 121 ASN A CG 586 O OD1 . ASN A 128 ? 0.3678 0.3690 0.5752 -0.0284 -0.1226 -0.0739 121 ASN A OD1 587 N ND2 . ASN A 128 ? 0.3759 0.3875 0.4825 -0.0656 -0.1175 -0.1873 121 ASN A ND2 588 N N . LYS A 129 ? 0.3281 0.3175 0.5104 -0.0492 0.0205 -0.0920 122 LYS A N 589 C CA . LYS A 129 ? 0.4363 0.3411 0.4911 -0.0409 -0.0202 -0.0767 122 LYS A CA 590 C C . LYS A 129 ? 0.4722 0.3261 0.5133 0.0067 -0.0281 -0.0772 122 LYS A C 591 O O . LYS A 129 ? 0.4705 0.3305 0.6453 0.0102 -0.0487 -0.1070 122 LYS A O 592 C CB . LYS A 129 ? 0.5798 0.3880 0.4744 -0.0234 0.0497 -0.0768 122 LYS A CB 593 C CG . LYS A 129 ? 0.6026 0.5011 0.4948 -0.0179 -0.0530 -0.0596 122 LYS A CG 594 C CD . LYS A 129 ? 0.4740 0.4912 0.6066 0.0041 0.0192 -0.0603 122 LYS A CD 595 C CE . LYS A 129 ? 0.4829 0.4346 0.5951 0.0405 0.0082 -0.0726 122 LYS A CE 596 N NZ . LYS A 129 ? 0.4529 0.4929 0.5867 0.0223 0.0000 -0.0465 122 LYS A NZ 597 N N . THR A 130 ? 0.3660 0.3076 0.5356 -0.0555 -0.0163 -0.1056 123 THR A N 598 C CA . THR A 130 ? 0.4281 0.3784 0.5245 -0.0071 0.0174 -0.1266 123 THR A CA 599 C C . THR A 130 ? 0.4784 0.3627 0.4915 -0.0180 0.0469 -0.1762 123 THR A C 600 O O . THR A 130 ? 0.5982 0.4599 0.4645 -0.0838 0.0017 -0.1798 123 THR A O 601 C CB . THR A 130 ? 0.4575 0.4590 0.6530 -0.0502 -0.0147 -0.0642 123 THR A CB 602 O OG1 . THR A 130 ? 0.3794 0.5045 0.6565 -0.0423 -0.0772 -0.1890 123 THR A OG1 603 C CG2 . THR A 130 ? 0.4642 0.5186 0.6346 -0.0928 0.0431 -0.0728 123 THR A CG2 604 N N . HIS A 131 ? 0.4289 0.3683 0.4722 -0.0300 0.0175 -0.1499 124 HIS A N 605 C CA . HIS A 131 ? 0.4038 0.3623 0.4338 -0.0165 -0.0183 -0.1657 124 HIS A CA 606 C C . HIS A 131 ? 0.3957 0.3262 0.4532 -0.0107 -0.0117 -0.1580 124 HIS A C 607 O O . HIS A 131 ? 0.4010 0.3397 0.4028 0.0181 0.0253 -0.1523 124 HIS A O 608 C CB . HIS A 131 ? 0.4272 0.4019 0.4233 -0.0451 -0.0782 -0.1532 124 HIS A CB 609 C CG . HIS A 131 ? 0.5839 0.5283 0.4730 -0.0056 -0.0066 -0.1039 124 HIS A CG 610 N ND1 . HIS A 131 ? 0.5887 0.6459 0.5399 0.0777 -0.0490 -0.1537 124 HIS A ND1 611 C CD2 . HIS A 131 ? 0.6288 0.6296 0.5387 0.0454 -0.0386 -0.0749 124 HIS A CD2 612 C CE1 . HIS A 131 ? 0.6055 0.6593 0.5964 0.0587 0.0384 -0.0663 124 HIS A CE1 613 N NE2 . HIS A 131 ? 0.6518 0.5927 0.5748 0.0576 -0.0006 -0.0973 124 HIS A NE2 614 N N . PRO A 132 ? 0.3904 0.3298 0.4073 -0.0100 -0.0183 -0.1569 125 PRO A N 615 C CA . PRO A 132 ? 0.3650 0.2748 0.4374 -0.0036 -0.0091 -0.1420 125 PRO A CA 616 C C . PRO A 132 ? 0.3221 0.3156 0.3834 -0.0197 -0.0061 -0.1590 125 PRO A C 617 O O . PRO A 132 ? 0.3910 0.3963 0.3901 -0.0083 0.0027 -0.1403 125 PRO A O 618 C CB . PRO A 132 ? 0.4490 0.3476 0.5566 0.0379 -0.0374 -0.0852 125 PRO A CB 619 C CG . PRO A 132 ? 0.4851 0.3726 0.5503 0.0286 -0.0766 -0.1177 125 PRO A CG 620 C CD . PRO A 132 ? 0.4935 0.3469 0.4555 0.0257 -0.0493 -0.1821 125 PRO A CD 621 N N . ASN A 133 ? 0.3160 0.2818 0.3522 -0.0178 -0.0161 -0.1259 126 ASN A N 622 C CA . ASN A 133 ? 0.3062 0.3132 0.3080 0.0115 0.0455 -0.1252 126 ASN A CA 623 C C . ASN A 133 ? 0.3302 0.3572 0.3230 0.0441 0.0792 -0.1240 126 ASN A C 624 O O . ASN A 133 ? 0.2984 0.3632 0.3105 -0.0085 0.0558 -0.1255 126 ASN A O 625 C CB . ASN A 133 ? 0.2822 0.2724 0.2934 0.0298 0.0188 -0.0993 126 ASN A CB 626 C CG . ASN A 133 ? 0.2809 0.3252 0.2867 0.0243 0.0088 -0.1320 126 ASN A CG 627 O OD1 . ASN A 133 ? 0.2934 0.3399 0.2625 -0.0092 0.0014 -0.0680 126 ASN A OD1 628 N ND2 . ASN A 133 ? 0.2575 0.2712 0.2869 0.0381 0.0344 -0.1068 126 ASN A ND2 629 N N . TYR A 134 ? 0.2984 0.3494 0.3115 0.0121 0.0855 -0.1506 127 TYR A N 630 C CA . TYR A 134 ? 0.3103 0.3263 0.3012 0.0503 0.0903 -0.1285 127 TYR A CA 631 C C . TYR A 134 ? 0.3226 0.3492 0.3363 0.0277 0.0544 -0.0921 127 TYR A C 632 O O . TYR A 134 ? 0.2970 0.3828 0.3172 0.0313 0.0508 -0.1036 127 TYR A O 633 C CB . TYR A 134 ? 0.3606 0.3309 0.3205 0.0564 0.0664 -0.1392 127 TYR A CB 634 C CG . TYR A 134 ? 0.3862 0.3332 0.3570 0.0196 0.0612 -0.1503 127 TYR A CG 635 C CD1 . TYR A 134 ? 0.4199 0.3686 0.3246 0.0984 0.0382 -0.1522 127 TYR A CD1 636 C CD2 . TYR A 134 ? 0.4043 0.3720 0.3552 0.0063 0.0147 -0.1471 127 TYR A CD2 637 C CE1 . TYR A 134 ? 0.4161 0.3863 0.3674 0.0054 0.0325 -0.1704 127 TYR A CE1 638 C CE2 . TYR A 134 ? 0.4544 0.3961 0.3734 -0.0009 0.0423 -0.2042 127 TYR A CE2 639 C CZ . TYR A 134 ? 0.4155 0.3676 0.3740 -0.0017 0.0387 -0.1746 127 TYR A CZ 640 O OH . TYR A 134 ? 0.4435 0.4248 0.4223 -0.0222 0.0283 -0.2108 127 TYR A OH 641 N N . ILE A 135 ? 0.3134 0.3546 0.2692 0.0094 0.0502 -0.1142 128 ILE A N 642 C CA . ILE A 135 ? 0.3593 0.3361 0.2852 -0.0112 0.0568 -0.1233 128 ILE A CA 643 C C . ILE A 135 ? 0.3464 0.3505 0.3041 -0.0070 0.0530 -0.1319 128 ILE A C 644 O O . ILE A 135 ? 0.3623 0.3296 0.3217 -0.0061 0.0773 -0.1215 128 ILE A O 645 C CB . ILE A 135 ? 0.3368 0.3281 0.2785 0.0066 0.0745 -0.1410 128 ILE A CB 646 C CG1 . ILE A 135 ? 0.3076 0.3275 0.2882 0.0046 0.0498 -0.1632 128 ILE A CG1 647 C CG2 . ILE A 135 ? 0.3524 0.3593 0.3101 -0.0680 0.0432 -0.1143 128 ILE A CG2 648 C CD1 . ILE A 135 ? 0.3559 0.3168 0.2727 -0.0231 0.0375 -0.1252 128 ILE A CD1 649 N N . SER A 136 ? 0.3963 0.3676 0.2933 -0.0020 0.1012 -0.1290 129 SER A N 650 C CA . SER A 136 ? 0.3903 0.3826 0.3216 0.0287 0.0879 -0.1448 129 SER A CA 651 C C . SER A 136 ? 0.3778 0.4295 0.3884 0.0512 0.1285 -0.1353 129 SER A C 652 O O . SER A 136 ? 0.3593 0.4445 0.3182 0.0417 0.1633 -0.1153 129 SER A O 653 C CB . SER A 136 ? 0.4747 0.4051 0.3393 0.0000 0.0891 -0.1818 129 SER A CB 654 O OG . SER A 136 ? 0.4339 0.4489 0.4201 -0.0012 0.0661 -0.1704 129 SER A OG 655 N N . ILE A 137 ? 0.4296 0.4731 0.3452 0.0526 0.1721 -0.1744 130 ILE A N 656 C CA . ILE A 137 ? 0.4555 0.4596 0.3343 0.0352 0.0930 -0.1116 130 ILE A CA 657 C C . ILE A 137 ? 0.5081 0.4834 0.3344 0.0572 0.0933 -0.1400 130 ILE A C 658 O O . ILE A 137 ? 0.5167 0.4590 0.3417 0.0529 0.1097 -0.1549 130 ILE A O 659 C CB . ILE A 137 ? 0.4461 0.4457 0.3185 0.0032 0.1461 -0.1034 130 ILE A CB 660 C CG1 . ILE A 137 ? 0.3804 0.4110 0.3532 0.0404 0.1428 -0.1154 130 ILE A CG1 661 C CG2 . ILE A 137 ? 0.3438 0.4828 0.2968 0.0353 0.1142 -0.1029 130 ILE A CG2 662 C CD1 . ILE A 137 ? 0.4045 0.4318 0.3623 0.1141 0.0935 -0.1100 130 ILE A CD1 663 N N . ILE A 138 ? 0.5360 0.5026 0.3579 0.0287 0.0652 -0.1282 131 ILE A N 664 C CA . ILE A 138 ? 0.5680 0.5738 0.3176 0.0587 0.0881 -0.1610 131 ILE A CA 665 C C . ILE A 138 ? 0.6516 0.5398 0.3602 0.0660 0.1260 -0.1497 131 ILE A C 666 O O . ILE A 138 ? 0.6866 0.5652 0.3549 0.0529 0.0874 -0.1615 131 ILE A O 667 C CB . ILE A 138 ? 0.5557 0.5438 0.4856 0.0469 0.0314 -0.0986 131 ILE A CB 668 C CG1 . ILE A 138 ? 0.5764 0.6764 0.5340 0.0011 0.0611 -0.1341 131 ILE A CG1 669 C CG2 . ILE A 138 ? 0.6325 0.5359 0.4782 0.0315 0.0643 -0.1440 131 ILE A CG2 670 C CD1 . ILE A 138 ? 0.6421 0.6650 0.5404 -0.0180 0.2082 -0.0536 131 ILE A CD1 671 N N . ASN A 139 ? 0.7058 0.5903 0.3668 0.0120 0.1652 -0.1771 132 ASN A N 672 C CA . ASN A 139 ? 0.6861 0.6525 0.3929 0.0597 0.1790 -0.1662 132 ASN A CA 673 C C . ASN A 139 ? 0.7736 0.7743 0.4839 0.0717 0.1020 -0.1547 132 ASN A C 674 O O . ASN A 139 ? 0.8067 0.8691 0.3860 0.0651 0.1729 -0.1642 132 ASN A O 675 C CB . ASN A 139 ? 0.7227 0.6205 0.5400 0.0534 0.1814 -0.1758 132 ASN A CB 676 C CG . ASN A 139 ? 0.7613 0.6742 0.4794 0.0170 0.0810 -0.1552 132 ASN A CG 677 O OD1 . ASN A 139 ? 0.7721 0.6836 0.4613 0.0396 0.0663 -0.1466 132 ASN A OD1 678 N ND2 . ASN A 139 ? 0.6853 0.6735 0.4032 -0.0294 0.1608 -0.1215 132 ASN A ND2 679 N N . GLU A 140 ? 0.8483 0.7384 0.4560 0.0148 0.0876 -0.1620 133 GLU A N 680 C CA . GLU A 140 ? 0.8340 0.7753 0.5124 0.0505 0.0941 -0.1502 133 GLU A CA 681 C C . GLU A 140 ? 0.8561 0.7734 0.4996 0.0906 -0.0295 -0.1570 133 GLU A C 682 O O . GLU A 140 ? 0.9285 0.8053 0.4520 0.0804 -0.0673 -0.1180 133 GLU A O 683 C CB . GLU A 140 ? 0.8642 0.8505 0.4612 0.0651 0.0801 -0.1098 133 GLU A CB 684 C CG . GLU A 140 ? 0.9519 0.8127 0.4490 0.0349 0.0974 -0.1671 133 GLU A CG 685 C CD . GLU A 140 ? 1.0666 0.8870 0.5663 0.0118 0.1935 -0.1412 133 GLU A CD 686 O OE1 . GLU A 140 ? 1.1253 0.9693 0.3569 -0.0953 0.2228 -0.0493 133 GLU A OE1 687 O OE2 . GLU A 140 ? 1.2667 0.8612 0.7359 0.1904 0.2598 -0.1710 133 GLU A OE2 688 N N . ASP A 141 ? 0.9407 0.7381 0.4925 0.0189 0.0098 -0.1816 134 ASP A N 689 C CA . ASP A 141 ? 0.8143 0.7807 0.5173 0.0549 0.0118 -0.1508 134 ASP A CA 690 C C . ASP A 141 ? 0.8233 0.7852 0.5431 -0.0178 0.0129 -0.1757 134 ASP A C 691 O O . ASP A 141 ? 0.9222 0.8754 0.5442 -0.0820 -0.1791 -0.1678 134 ASP A O 692 C CB . ASP A 141 ? 0.8289 0.7752 0.5319 0.0481 0.0798 -0.1840 134 ASP A CB 693 C CG . ASP A 141 ? 0.8776 0.7728 0.5194 0.0740 0.0884 -0.1483 134 ASP A CG 694 O OD1 . ASP A 141 ? 0.8594 0.9138 0.3756 0.1155 0.0282 -0.2012 134 ASP A OD1 695 O OD2 . ASP A 141 ? 0.9010 0.7661 0.4993 0.0686 0.0370 -0.1706 134 ASP A OD2 696 N N . GLY A 142 ? 0.7241 0.7592 0.4341 0.0665 0.0646 -0.1279 135 GLY A N 697 C CA . GLY A 142 ? 0.7081 0.8107 0.5455 0.0566 0.1079 -0.0708 135 GLY A CA 698 C C . GLY A 142 ? 0.6991 0.7696 0.4978 0.0824 0.0685 -0.1274 135 GLY A C 699 O O . GLY A 142 ? 0.6955 0.8581 0.5381 -0.0077 0.0463 -0.0761 135 GLY A O 700 N N A ASN A 143 ? 0.6965 0.6053 0.3393 0.0417 0.0673 -0.2088 136 ASN A N 701 N N B ASN A 143 ? 0.7014 0.6440 0.4037 0.0548 0.0704 -0.1782 136 ASN A N 702 C CA A ASN A 143 ? 0.6636 0.6027 0.4141 0.0492 0.0371 -0.2004 136 ASN A CA 703 C CA B ASN A 143 ? 0.6575 0.6081 0.4370 0.0609 0.0626 -0.1941 136 ASN A CA 704 C C A ASN A 143 ? 0.6390 0.6075 0.4147 0.0503 0.0722 -0.2241 136 ASN A C 705 C C B ASN A 143 ? 0.6345 0.6085 0.4397 0.0555 0.0712 -0.1970 136 ASN A C 706 O O A ASN A 143 ? 0.6451 0.5923 0.3704 0.0433 0.0728 -0.1728 136 ASN A O 707 O O B ASN A 143 ? 0.6282 0.6129 0.4210 0.0454 0.0719 -0.1666 136 ASN A O 708 C CB A ASN A 143 ? 0.7129 0.6468 0.3770 0.0350 0.1287 -0.2220 136 ASN A CB 709 C CB B ASN A 143 ? 0.6854 0.6078 0.3998 0.0508 0.0979 -0.1906 136 ASN A CB 710 C CG A ASN A 143 ? 0.6847 0.7260 0.4469 -0.0328 0.0527 -0.2254 136 ASN A CG 711 C CG B ASN A 143 ? 0.6203 0.5525 0.4658 0.0756 0.0731 -0.2305 136 ASN A CG 712 O OD1 A ASN A 143 ? 0.7220 0.7313 0.4463 -0.1420 0.0816 -0.1726 136 ASN A OD1 713 O OD1 B ASN A 143 ? 0.6216 0.4989 0.4764 -0.0286 0.0646 -0.2376 136 ASN A OD1 714 N ND2 A ASN A 143 ? 0.6685 0.6832 0.4069 -0.0281 0.0679 -0.1420 136 ASN A ND2 715 N ND2 B ASN A 143 ? 0.5654 0.5478 0.4410 0.0674 0.1080 -0.1904 136 ASN A ND2 716 N N . GLU A 144 ? 0.5691 0.6030 0.4259 0.0552 0.0285 -0.1984 137 GLU A N 717 C CA . GLU A 144 ? 0.5726 0.5818 0.3954 0.0311 0.0645 -0.1747 137 GLU A CA 718 C C . GLU A 144 ? 0.5586 0.5117 0.3606 0.0119 0.0552 -0.1627 137 GLU A C 719 O O . GLU A 144 ? 0.5422 0.5203 0.4240 -0.0118 0.0738 -0.1380 137 GLU A O 720 C CB . GLU A 144 ? 0.5992 0.5124 0.3149 0.0426 0.0471 -0.2039 137 GLU A CB 721 C CG . GLU A 144 ? 0.5159 0.5871 0.3602 0.0237 0.0359 -0.2158 137 GLU A CG 722 C CD . GLU A 144 ? 0.5632 0.5242 0.4002 0.0470 0.0674 -0.1789 137 GLU A CD 723 O OE1 . GLU A 144 ? 0.5049 0.4803 0.3835 0.0011 0.0798 -0.1874 137 GLU A OE1 724 O OE2 . GLU A 144 ? 0.5956 0.5093 0.3804 0.0478 0.0426 -0.2120 137 GLU A OE2 725 N N . ILE A 145 ? 0.5529 0.4957 0.4001 0.0285 0.1045 -0.1501 138 ILE A N 726 C CA . ILE A 145 ? 0.5481 0.5201 0.3985 0.0200 0.0856 -0.1134 138 ILE A CA 727 C C . ILE A 145 ? 0.5222 0.4434 0.3925 0.1156 0.1069 -0.2100 138 ILE A C 728 O O . ILE A 145 ? 0.4508 0.5439 0.5041 0.1058 0.1055 -0.1755 138 ILE A O 729 C CB . ILE A 145 ? 0.5256 0.4980 0.3671 0.0491 0.1140 -0.1707 138 ILE A CB 730 C CG1 . ILE A 145 ? 0.4025 0.4762 0.3815 0.0571 0.1195 -0.0953 138 ILE A CG1 731 C CG2 . ILE A 145 ? 0.5708 0.5946 0.3690 0.0657 0.1111 -0.2112 138 ILE A CG2 732 C CD1 . ILE A 145 ? 0.4605 0.5101 0.5158 0.0247 0.1692 -0.1081 138 ILE A CD1 733 N N . PHE A 146 ? 0.4387 0.4072 0.3900 0.0283 0.1237 -0.1992 139 PHE A N 734 C CA . PHE A 146 ? 0.4055 0.4734 0.3864 0.0257 0.1104 -0.1349 139 PHE A CA 735 C C . PHE A 146 ? 0.4096 0.4199 0.3727 0.0324 0.0919 -0.1362 139 PHE A C 736 O O . PHE A 146 ? 0.4407 0.3703 0.3096 0.0366 0.1050 -0.1487 139 PHE A O 737 C CB . PHE A 146 ? 0.4160 0.4389 0.4207 0.0179 0.1440 -0.1649 139 PHE A CB 738 C CG . PHE A 146 ? 0.4345 0.3985 0.4187 -0.0086 0.1213 -0.1460 139 PHE A CG 739 C CD1 . PHE A 146 ? 0.4397 0.4030 0.4643 -0.0487 0.0671 -0.1333 139 PHE A CD1 740 C CD2 . PHE A 146 ? 0.3766 0.4122 0.4353 -0.0208 0.1564 -0.1606 139 PHE A CD2 741 C CE1 . PHE A 146 ? 0.4506 0.4652 0.4306 -0.0200 0.0749 -0.0867 139 PHE A CE1 742 C CE2 . PHE A 146 ? 0.4119 0.4115 0.4312 -0.0219 0.0726 -0.1498 139 PHE A CE2 743 C CZ . PHE A 146 ? 0.4111 0.4335 0.4348 -0.0608 0.0932 -0.0933 139 PHE A CZ 744 N N . ASN A 147 ? 0.3903 0.3613 0.3551 0.0298 0.0935 -0.1575 140 ASN A N 745 C CA . ASN A 147 ? 0.3891 0.3388 0.3353 0.0220 0.0856 -0.1755 140 ASN A CA 746 C C . ASN A 147 ? 0.3435 0.3261 0.3370 0.0329 0.0755 -0.1389 140 ASN A C 747 O O . ASN A 147 ? 0.3836 0.2876 0.4000 0.0268 0.1005 -0.1119 140 ASN A O 748 C CB . ASN A 147 ? 0.4616 0.3575 0.3609 -0.0054 0.0616 -0.1344 140 ASN A CB 749 C CG . ASN A 147 ? 0.4934 0.3592 0.3527 0.0132 0.0614 -0.1821 140 ASN A CG 750 O OD1 . ASN A 147 ? 0.4619 0.3926 0.4144 0.0173 0.0665 -0.1473 140 ASN A OD1 751 N ND2 . ASN A 147 ? 0.5740 0.3874 0.4177 -0.0654 0.0891 -0.2024 140 ASN A ND2 752 N N . THR A 148 ? 0.3333 0.3031 0.3406 0.0254 0.0893 -0.1190 141 THR A N 753 C CA . THR A 148 ? 0.3363 0.2859 0.3377 0.0265 0.0897 -0.1076 141 THR A CA 754 C C . THR A 148 ? 0.3258 0.3205 0.3286 0.0354 0.0825 -0.1055 141 THR A C 755 O O . THR A 148 ? 0.3731 0.3045 0.3610 0.0212 0.0734 -0.1124 141 THR A O 756 C CB . THR A 148 ? 0.3325 0.3006 0.2974 0.0301 0.1107 -0.1121 141 THR A CB 757 O OG1 . THR A 148 ? 0.3554 0.3032 0.3467 0.0599 0.0924 -0.0853 141 THR A OG1 758 C CG2 . THR A 148 ? 0.3583 0.3127 0.3027 0.0368 0.0860 -0.0760 141 THR A CG2 759 N N . SER A 149 ? 0.3580 0.3290 0.3436 0.0552 0.0548 -0.0914 142 SER A N 760 C CA . SER A 149 ? 0.2926 0.3002 0.3504 0.0273 0.0453 -0.0942 142 SER A CA 761 C C . SER A 149 ? 0.3049 0.2856 0.3299 0.0327 0.0733 -0.1019 142 SER A C 762 O O . SER A 149 ? 0.3081 0.3083 0.3522 0.0512 0.0702 -0.0803 142 SER A O 763 C CB . SER A 149 ? 0.3631 0.2947 0.3580 0.0343 0.0266 -0.1076 142 SER A CB 764 O OG A SER A 149 ? 0.2977 0.2989 0.2498 0.0172 0.0289 -0.0747 142 SER A OG 765 O OG B SER A 149 ? 0.4785 0.4101 0.4597 0.0372 0.0364 0.0045 142 SER A OG 766 N N . LEU A 150 ? 0.3006 0.2971 0.3082 0.0368 0.0595 -0.0828 143 LEU A N 767 C CA . LEU A 150 ? 0.2920 0.3054 0.3366 0.0290 0.0381 -0.1007 143 LEU A CA 768 C C . LEU A 150 ? 0.3092 0.2996 0.3486 0.0465 0.0513 -0.0918 143 LEU A C 769 O O . LEU A 150 ? 0.2969 0.3525 0.3431 0.0552 0.0585 -0.0673 143 LEU A O 770 C CB . LEU A 150 ? 0.3341 0.3694 0.3775 -0.0265 -0.0472 -0.0755 143 LEU A CB 771 C CG . LEU A 150 ? 0.4184 0.3411 0.3795 -0.0275 -0.0129 -0.0724 143 LEU A CG 772 C CD1 . LEU A 150 ? 0.4182 0.4102 0.3703 -0.0554 -0.0421 -0.0845 143 LEU A CD1 773 C CD2 . LEU A 150 ? 0.4541 0.3829 0.3821 0.0357 -0.0391 -0.0771 143 LEU A CD2 774 N N . PHE A 151 ? 0.3077 0.2729 0.3342 0.0182 0.0381 -0.0961 144 PHE A N 775 C CA . PHE A 151 ? 0.3012 0.2675 0.3287 0.0082 0.0033 -0.0883 144 PHE A CA 776 C C . PHE A 151 ? 0.2854 0.2806 0.3398 0.0317 0.0237 -0.0768 144 PHE A C 777 O O . PHE A 151 ? 0.3273 0.3158 0.3150 0.0409 0.0313 -0.0681 144 PHE A O 778 C CB . PHE A 151 ? 0.3563 0.3072 0.3699 0.0180 0.0442 -0.0377 144 PHE A CB 779 C CG . PHE A 151 ? 0.4096 0.2756 0.4060 0.0101 -0.0110 -0.0645 144 PHE A CG 780 C CD1 . PHE A 151 ? 0.4094 0.3197 0.4060 0.0534 0.0020 -0.0620 144 PHE A CD1 781 C CD2 . PHE A 151 ? 0.5352 0.3449 0.4324 0.0652 -0.0808 -0.0668 144 PHE A CD2 782 C CE1 . PHE A 151 ? 0.5813 0.2881 0.4628 0.0509 -0.0148 -0.1245 144 PHE A CE1 783 C CE2 . PHE A 151 ? 0.5134 0.4057 0.4957 0.0796 -0.0283 -0.1339 144 PHE A CE2 784 C CZ . PHE A 151 ? 0.5578 0.3992 0.4445 0.0573 -0.0489 -0.1261 144 PHE A CZ 785 N N . GLU A 152 ? 0.2568 0.2465 0.3169 0.0260 0.0194 -0.0560 145 GLU A N 786 C CA . GLU A 152 ? 0.2707 0.2332 0.3460 0.0337 0.0104 -0.0947 145 GLU A CA 787 C C . GLU A 152 ? 0.2689 0.2636 0.3517 0.0436 0.0229 -0.0521 145 GLU A C 788 O O . GLU A 152 ? 0.2612 0.2569 0.3484 0.0246 0.0126 -0.0536 145 GLU A O 789 C CB . GLU A 152 ? 0.3144 0.2255 0.3357 0.0403 0.0579 -0.0856 145 GLU A CB 790 C CG . GLU A 152 ? 0.3031 0.2276 0.3215 0.0646 0.0583 -0.0690 145 GLU A CG 791 C CD . GLU A 152 ? 0.2820 0.2108 0.3072 0.0538 0.0494 -0.0491 145 GLU A CD 792 O OE1 . GLU A 152 ? 0.2683 0.2526 0.3269 0.0528 0.0486 -0.0227 145 GLU A OE1 793 O OE2 . GLU A 152 ? 0.2887 0.2327 0.3339 0.0382 0.0579 -0.0488 145 GLU A OE2 794 N N . PRO A 153 ? 0.2591 0.2655 0.3246 0.0275 0.0514 -0.0877 146 PRO A N 795 C CA . PRO A 153 ? 0.2326 0.2879 0.3678 0.0462 0.0092 -0.0768 146 PRO A CA 796 C C . PRO A 153 ? 0.2596 0.2542 0.3767 0.0428 0.0057 -0.0565 146 PRO A C 797 O O . PRO A 153 ? 0.2898 0.3271 0.3323 0.0284 -0.0178 -0.0841 146 PRO A O 798 C CB . PRO A 153 ? 0.2608 0.3623 0.4048 0.0402 0.0817 -0.0462 146 PRO A CB 799 C CG . PRO A 153 ? 0.3208 0.3110 0.4120 0.0568 0.0568 -0.0387 146 PRO A CG 800 C CD . PRO A 153 ? 0.2507 0.2992 0.4262 0.0207 0.0587 -0.0543 146 PRO A CD 801 N N . PRO A 154 ? 0.2573 0.2418 0.3629 0.0420 0.0053 -0.0715 147 PRO A N 802 C CA . PRO A 154 ? 0.2630 0.2808 0.3521 0.0358 0.0046 -0.0443 147 PRO A CA 803 C C . PRO A 154 ? 0.3038 0.2563 0.3909 0.0375 -0.0123 -0.0407 147 PRO A C 804 O O . PRO A 154 ? 0.2420 0.3109 0.3815 0.0569 -0.0489 -0.0358 147 PRO A O 805 C CB . PRO A 154 ? 0.2953 0.2490 0.4300 0.0395 0.0085 -0.0465 147 PRO A CB 806 C CG . PRO A 154 ? 0.3546 0.3182 0.3629 -0.0058 0.0081 -0.0484 147 PRO A CG 807 C CD . PRO A 154 ? 0.2571 0.2403 0.4113 -0.0096 0.0177 -0.0375 147 PRO A CD 808 N N . PRO A 155 ? 0.2925 0.2769 0.3609 0.0324 -0.0348 -0.0185 148 PRO A N 809 C CA . PRO A 155 ? 0.2961 0.2620 0.3882 0.0227 -0.0578 -0.0323 148 PRO A CA 810 C C . PRO A 155 ? 0.2918 0.2423 0.4192 0.0560 -0.0392 -0.0466 148 PRO A C 811 O O . PRO A 155 ? 0.3124 0.2373 0.4132 0.0516 -0.0385 -0.0273 148 PRO A O 812 C CB . PRO A 155 ? 0.3420 0.2457 0.4123 0.0250 -0.0479 -0.0456 148 PRO A CB 813 C CG . PRO A 155 ? 0.3335 0.2368 0.3793 0.0166 -0.0614 -0.0451 148 PRO A CG 814 C CD . PRO A 155 ? 0.3542 0.2393 0.3659 0.0270 -0.0439 -0.0601 148 PRO A CD 815 N N . PRO A 156 ? 0.2861 0.2446 0.4015 0.0721 -0.0117 -0.0329 149 PRO A N 816 C CA . PRO A 156 ? 0.2705 0.2622 0.3732 0.0727 -0.0301 -0.0202 149 PRO A CA 817 C C . PRO A 156 ? 0.2696 0.2814 0.4335 0.0726 -0.0215 -0.0140 149 PRO A C 818 O O . PRO A 156 ? 0.2350 0.3132 0.3956 0.1095 -0.0088 0.0076 149 PRO A O 819 C CB . PRO A 156 ? 0.2424 0.3146 0.4288 0.0433 -0.0204 -0.0328 149 PRO A CB 820 C CG . PRO A 156 ? 0.2910 0.3053 0.4108 0.0549 -0.0269 -0.0255 149 PRO A CG 821 C CD . PRO A 156 ? 0.3117 0.2974 0.3934 0.0470 -0.0203 -0.0002 149 PRO A CD 822 N N . GLY A 157 ? 0.2863 0.2455 0.4008 0.0822 -0.0294 0.0075 150 GLY A N 823 C CA . GLY A 157 ? 0.2590 0.2766 0.4825 0.0291 -0.0373 0.0135 150 GLY A CA 824 C C . GLY A 157 ? 0.3025 0.3253 0.5140 0.1050 -0.0028 0.0029 150 GLY A C 825 O O . GLY A 157 ? 0.2650 0.4160 0.5737 0.0774 -0.0191 0.0034 150 GLY A O 826 N N . TYR A 158 ? 0.3067 0.2858 0.5233 0.0877 -0.0124 -0.0208 151 TYR A N 827 C CA . TYR A 158 ? 0.3478 0.2657 0.5500 0.0861 -0.0657 -0.0484 151 TYR A CA 828 C C . TYR A 158 ? 0.3980 0.3539 0.5417 0.1245 -0.0237 -0.0734 151 TYR A C 829 O O . TYR A 158 ? 0.3499 0.3269 0.6090 0.0273 -0.0309 0.0036 151 TYR A O 830 C CB . TYR A 158 ? 0.2895 0.2619 0.4831 0.1236 -0.0220 -0.0641 151 TYR A CB 831 C CG . TYR A 158 ? 0.3225 0.2415 0.4428 0.0670 0.0159 -0.0189 151 TYR A CG 832 C CD1 . TYR A 158 ? 0.3140 0.2414 0.4516 0.0649 0.0157 -0.0215 151 TYR A CD1 833 C CD2 . TYR A 158 ? 0.2897 0.2549 0.4195 0.0697 0.0354 -0.0253 151 TYR A CD2 834 C CE1 . TYR A 158 ? 0.2956 0.2672 0.3796 0.0877 0.0387 0.0147 151 TYR A CE1 835 C CE2 . TYR A 158 ? 0.2899 0.2117 0.3795 0.0801 0.0399 0.0005 151 TYR A CE2 836 C CZ . TYR A 158 ? 0.2902 0.2664 0.3467 0.0865 0.0428 0.0065 151 TYR A CZ 837 O OH . TYR A 158 ? 0.2802 0.2327 0.3781 0.0766 0.0355 -0.0195 151 TYR A OH 838 N N . GLU A 159 ? 0.4253 0.2476 0.5701 0.1017 -0.0447 -0.0687 152 GLU A N 839 C CA . GLU A 159 ? 0.3864 0.3608 0.5736 0.0522 -0.0306 -0.0540 152 GLU A CA 840 C C . GLU A 159 ? 0.3875 0.3719 0.5783 0.0294 -0.0016 -0.0554 152 GLU A C 841 O O . GLU A 159 ? 0.3018 0.3951 0.6546 0.0003 -0.0868 -0.0442 152 GLU A O 842 C CB . GLU A 159 ? 0.3912 0.4006 0.6094 0.0327 -0.0293 -0.1593 152 GLU A CB 843 C CG . GLU A 159 ? 0.3767 0.5023 0.7121 0.0195 -0.0076 -0.0758 152 GLU A CG 844 C CD . GLU A 159 ? 0.4711 0.4297 0.6571 -0.0473 0.0066 -0.1171 152 GLU A CD 845 O OE1 . GLU A 159 ? 0.4991 0.3829 0.5738 -0.0345 -0.0123 -0.1011 152 GLU A OE1 846 O OE2 . GLU A 159 ? 0.4869 0.4734 0.6921 -0.0034 -0.0479 -0.1503 152 GLU A OE2 847 N N . ASN A 160 ? 0.3696 0.3230 0.6604 0.0584 0.0250 0.0048 153 ASN A N 848 C CA . ASN A 160 ? 0.4011 0.3529 0.7516 0.0327 0.0355 -0.0148 153 ASN A CA 849 C C . ASN A 160 ? 0.3920 0.3982 0.7938 0.0196 0.0368 -0.0489 153 ASN A C 850 O O . ASN A 160 ? 0.4585 0.3377 0.7764 -0.0631 0.0250 0.0269 153 ASN A O 851 C CB . ASN A 160 ? 0.4168 0.4131 0.7297 -0.0503 -0.0035 0.0296 153 ASN A CB 852 C CG . ASN A 160 ? 0.3896 0.4566 0.6939 -0.0107 -0.0256 -0.0156 153 ASN A CG 853 O OD1 . ASN A 160 ? 0.4032 0.5158 0.7221 0.0573 -0.0340 -0.0692 153 ASN A OD1 854 N ND2 . ASN A 160 ? 0.4304 0.6041 0.6931 -0.0500 -0.0150 -0.0141 153 ASN A ND2 855 N N . VAL A 161 ? 0.4128 0.3406 0.7413 0.0993 -0.0142 -0.0200 154 VAL A N 856 C CA . VAL A 161 ? 0.3594 0.3980 0.6496 0.0552 0.0494 -0.0580 154 VAL A CA 857 C C . VAL A 161 ? 0.4679 0.5017 0.6549 0.0309 0.0370 -0.0044 154 VAL A C 858 O O . VAL A 161 ? 0.4244 0.4874 0.6519 0.0049 -0.0536 0.0576 154 VAL A O 859 C CB . VAL A 161 ? 0.3403 0.3990 0.6957 0.0483 0.0350 -0.0427 154 VAL A CB 860 C CG1 . VAL A 161 ? 0.4508 0.2253 0.6541 0.0119 0.0503 -0.0138 154 VAL A CG1 861 C CG2 . VAL A 161 ? 0.3778 0.5686 0.6385 -0.0436 0.0012 -0.1340 154 VAL A CG2 862 N N . SER A 162 ? 0.3859 0.4109 0.7836 0.0397 -0.1237 -0.0437 155 SER A N 863 C CA . SER A 162 ? 0.5151 0.3303 0.7001 -0.0238 -0.1173 0.0200 155 SER A CA 864 C C . SER A 162 ? 0.4579 0.3553 0.5839 -0.0099 -0.1035 -0.0103 155 SER A C 865 O O . SER A 162 ? 0.4909 0.2831 0.5900 -0.0141 -0.0239 0.0088 155 SER A O 866 C CB . SER A 162 ? 0.4845 0.5800 0.5781 -0.0640 0.0148 -0.0496 155 SER A CB 867 O OG A SER A 162 ? 0.4342 0.6173 0.6441 0.0070 0.1273 -0.0138 155 SER A OG 868 O OG B SER A 162 ? 0.3723 0.5242 0.6635 -0.1471 -0.0433 -0.0776 155 SER A OG 869 N N . ASP A 163 ? 0.4141 0.2849 0.5151 -0.0514 -0.0663 -0.0006 156 ASP A N 870 C CA . ASP A 163 ? 0.3891 0.2898 0.5094 -0.0138 -0.0313 -0.0070 156 ASP A CA 871 C C . ASP A 163 ? 0.2883 0.3006 0.4199 0.0157 0.0355 0.0065 156 ASP A C 872 O O . ASP A 163 ? 0.2656 0.3240 0.4107 -0.0050 -0.0072 -0.0193 156 ASP A O 873 C CB . ASP A 163 ? 0.4178 0.3381 0.5688 -0.0102 0.0124 -0.0068 156 ASP A CB 874 C CG . ASP A 163 ? 0.5254 0.4945 0.5905 -0.1111 -0.0222 -0.0144 156 ASP A CG 875 O OD1 . ASP A 163 ? 0.4128 0.6215 0.7241 -0.1546 -0.0952 -0.0246 156 ASP A OD1 876 O OD2 . ASP A 163 ? 0.7173 0.6987 0.5455 -0.1945 0.0436 -0.0663 156 ASP A OD2 877 N N . ILE A 164 ? 0.2473 0.2130 0.3397 -0.0059 -0.0280 0.0047 157 ILE A N 878 C CA . ILE A 164 ? 0.2125 0.2238 0.3268 0.0178 0.0107 -0.0303 157 ILE A CA 879 C C . ILE A 164 ? 0.2597 0.1943 0.3339 0.0375 0.0129 -0.0523 157 ILE A C 880 O O . ILE A 164 ? 0.3134 0.2141 0.3181 0.0507 -0.0163 -0.0514 157 ILE A O 881 C CB . ILE A 164 ? 0.2002 0.2521 0.3097 0.0304 0.0278 -0.0331 157 ILE A CB 882 C CG1 . ILE A 164 ? 0.2024 0.2279 0.3449 0.0506 -0.0056 -0.0318 157 ILE A CG1 883 C CG2 . ILE A 164 ? 0.2512 0.2154 0.3088 0.0170 0.0011 -0.0582 157 ILE A CG2 884 C CD1 . ILE A 164 ? 0.2145 0.2600 0.3555 0.0731 -0.0202 -0.0607 157 ILE A CD1 885 N N . VAL A 165 ? 0.2096 0.1877 0.3156 0.0219 0.0400 -0.0230 158 VAL A N 886 C CA . VAL A 165 ? 0.2353 0.2186 0.2906 0.0351 0.0193 -0.0474 158 VAL A CA 887 C C . VAL A 165 ? 0.2590 0.2033 0.2733 0.0080 0.0246 -0.0566 158 VAL A C 888 O O . VAL A 165 ? 0.2064 0.2238 0.3304 0.0109 0.0296 -0.0330 158 VAL A O 889 C CB . VAL A 165 ? 0.2459 0.1892 0.2620 0.0127 -0.0014 -0.0567 158 VAL A CB 890 C CG1 . VAL A 165 ? 0.2421 0.1687 0.2977 0.0051 0.0548 -0.0489 158 VAL A CG1 891 C CG2 . VAL A 165 ? 0.2420 0.2244 0.2947 0.0306 -0.0230 -0.0471 158 VAL A CG2 892 N N . PRO A 166 ? 0.2417 0.2290 0.2664 0.0070 0.0529 -0.0681 159 PRO A N 893 C CA . PRO A 166 ? 0.2441 0.2078 0.2717 0.0069 0.0535 -0.0708 159 PRO A CA 894 C C . PRO A 166 ? 0.2392 0.2137 0.3041 0.0142 0.0238 -0.0595 159 PRO A C 895 O O . PRO A 166 ? 0.2079 0.2292 0.2976 0.0124 0.0380 -0.0491 159 PRO A O 896 C CB . PRO A 166 ? 0.2681 0.2786 0.2837 -0.0046 0.0318 -0.0909 159 PRO A CB 897 C CG . PRO A 166 ? 0.2670 0.3404 0.2262 -0.0077 0.0476 -0.0898 159 PRO A CG 898 C CD . PRO A 166 ? 0.2727 0.2655 0.2506 -0.0373 0.0574 -0.0420 159 PRO A CD 899 N N . PRO A 167 ? 0.2412 0.1908 0.2997 0.0234 0.0233 -0.0494 160 PRO A N 900 C CA . PRO A 167 ? 0.2155 0.1983 0.2983 0.0112 0.0169 -0.0309 160 PRO A CA 901 C C . PRO A 167 ? 0.2275 0.1931 0.2587 0.0191 0.0321 -0.0517 160 PRO A C 902 O O . PRO A 167 ? 0.2478 0.2116 0.2789 0.0300 0.0096 -0.0607 160 PRO A O 903 C CB . PRO A 167 ? 0.2247 0.2108 0.2768 0.0561 0.0218 -0.0576 160 PRO A CB 904 C CG . PRO A 167 ? 0.2328 0.1858 0.3145 0.0030 0.0156 -0.0265 160 PRO A CG 905 C CD . PRO A 167 ? 0.1926 0.2466 0.3092 0.0071 0.0285 -0.0487 160 PRO A CD 906 N N . PHE A 168 ? 0.1855 0.2078 0.2398 0.0352 0.0357 -0.0346 161 PHE A N 907 C CA . PHE A 168 ? 0.2078 0.2015 0.2509 0.0225 0.0209 -0.0475 161 PHE A CA 908 C C . PHE A 168 ? 0.2174 0.2035 0.2311 0.0157 0.0242 -0.0466 161 PHE A C 909 O O . PHE A 168 ? 0.2282 0.2164 0.2314 0.0231 0.0090 -0.0491 161 PHE A O 910 C CB . PHE A 168 ? 0.2039 0.2335 0.2439 0.0068 0.0493 -0.0512 161 PHE A CB 911 C CG . PHE A 168 ? 0.2259 0.2175 0.2108 0.0326 0.0192 -0.0788 161 PHE A CG 912 C CD1 . PHE A 168 ? 0.2299 0.1571 0.2240 0.0029 0.0091 -0.0722 161 PHE A CD1 913 C CD2 . PHE A 168 ? 0.2352 0.2309 0.2167 0.0080 0.0168 -0.0525 161 PHE A CD2 914 C CE1 . PHE A 168 ? 0.2158 0.1944 0.2049 0.0326 -0.0106 -0.0575 161 PHE A CE1 915 C CE2 . PHE A 168 ? 0.2203 0.2173 0.2347 0.0357 0.0081 -0.0645 161 PHE A CE2 916 C CZ . PHE A 168 ? 0.1997 0.1970 0.2463 0.0057 -0.0157 -0.0151 161 PHE A CZ 917 N N . SER A 169 ? 0.2143 0.1883 0.2476 0.0127 0.0213 -0.0384 162 SER A N 918 C CA . SER A 169 ? 0.2111 0.1931 0.2182 0.0033 0.0502 -0.0484 162 SER A CA 919 C C . SER A 169 ? 0.2027 0.2132 0.2080 0.0048 0.0159 -0.0468 162 SER A C 920 O O . SER A 169 ? 0.2136 0.2318 0.2224 0.0135 -0.0058 -0.0558 162 SER A O 921 C CB . SER A 169 ? 0.2067 0.2301 0.2303 -0.0019 -0.0013 0.0072 162 SER A CB 922 O OG . SER A 169 ? 0.2362 0.2279 0.2418 0.0307 0.0440 -0.0410 162 SER A OG 923 N N . ALA A 170 ? 0.2019 0.2389 0.2203 0.0040 0.0428 -0.0477 163 ALA A N 924 C CA . ALA A 170 ? 0.1941 0.2239 0.1991 0.0192 0.0207 -0.0148 163 ALA A CA 925 C C . ALA A 170 ? 0.2259 0.2008 0.2207 0.0039 0.0230 -0.0251 163 ALA A C 926 O O . ALA A 170 ? 0.1752 0.2167 0.2275 -0.0084 0.0378 -0.0573 163 ALA A O 927 C CB . ALA A 170 ? 0.2098 0.2085 0.2015 0.0059 0.0278 -0.0321 163 ALA A CB 928 N N . PHE A 171 ? 0.2198 0.2391 0.1997 0.0096 0.0226 -0.0034 164 PHE A N 929 C CA . PHE A 171 ? 0.2576 0.2044 0.1920 0.0344 0.0185 -0.0408 164 PHE A CA 930 C C . PHE A 171 ? 0.2529 0.2176 0.2021 0.0187 0.0172 -0.0263 164 PHE A C 931 O O . PHE A 171 ? 0.2729 0.2308 0.2046 0.0420 0.0046 -0.0304 164 PHE A O 932 C CB . PHE A 171 ? 0.2330 0.2215 0.1923 0.0110 0.0206 -0.0541 164 PHE A CB 933 C CG . PHE A 171 ? 0.1905 0.1963 0.1800 0.0069 0.0008 -0.0349 164 PHE A CG 934 C CD1 . PHE A 171 ? 0.1896 0.2346 0.1976 0.0066 -0.0024 0.0077 164 PHE A CD1 935 C CD2 . PHE A 171 ? 0.2059 0.1961 0.1496 0.0148 0.0117 -0.0285 164 PHE A CD2 936 C CE1 . PHE A 171 ? 0.2105 0.2220 0.1533 -0.0132 -0.0250 -0.0351 164 PHE A CE1 937 C CE2 . PHE A 171 ? 0.1644 0.2066 0.1827 -0.0035 0.0381 -0.0372 164 PHE A CE2 938 C CZ . PHE A 171 ? 0.1526 0.1746 0.2030 -0.0108 -0.0460 -0.0340 164 PHE A CZ 939 N N . SER A 172 ? 0.2608 0.2248 0.2003 0.0153 0.0220 -0.0499 165 SER A N 940 C CA . SER A 172 ? 0.2717 0.2507 0.2006 0.0412 0.0126 -0.0570 165 SER A CA 941 C C . SER A 172 ? 0.2577 0.2657 0.2188 0.0299 0.0158 -0.0552 165 SER A C 942 O O . SER A 172 ? 0.2846 0.2898 0.2147 0.0119 -0.0168 -0.0394 165 SER A O 943 C CB . SER A 172 ? 0.2686 0.2693 0.2064 0.0534 0.0447 -0.0272 165 SER A CB 944 O OG . SER A 172 ? 0.2773 0.2673 0.2062 0.0335 0.0005 -0.0365 165 SER A OG 945 N N . PRO A 173 ? 0.2490 0.2877 0.2265 0.0172 -0.0074 -0.0580 166 PRO A N 946 C CA . PRO A 173 ? 0.2967 0.2859 0.2050 0.0062 -0.0235 -0.0577 166 PRO A CA 947 C C . PRO A 173 ? 0.2823 0.2932 0.2456 0.0049 -0.0201 -0.0731 166 PRO A C 948 O O . PRO A 173 ? 0.2787 0.3274 0.2533 0.0137 -0.0038 -0.0828 166 PRO A O 949 C CB . PRO A 173 ? 0.2340 0.3026 0.2031 -0.0034 -0.0446 -0.0424 166 PRO A CB 950 C CG . PRO A 173 ? 0.2455 0.3103 0.2391 -0.0078 -0.0132 -0.0723 166 PRO A CG 951 C CD . PRO A 173 ? 0.3152 0.2736 0.2252 0.0139 -0.0008 -0.0484 166 PRO A CD 952 N N . GLN A 174 ? 0.2943 0.3200 0.2466 0.0309 -0.0400 -0.1144 167 GLN A N 953 C CA . GLN A 174 ? 0.3123 0.3177 0.2244 0.0206 0.0078 -0.1045 167 GLN A CA 954 C C . GLN A 174 ? 0.3613 0.3219 0.2733 0.0068 0.0228 -0.0912 167 GLN A C 955 O O . GLN A 174 ? 0.3644 0.3565 0.2822 0.0117 0.0126 -0.0456 167 GLN A O 956 C CB . GLN A 174 ? 0.3026 0.3391 0.2450 0.0226 -0.0055 -0.0960 167 GLN A CB 957 C CG . GLN A 174 ? 0.3602 0.3560 0.2802 -0.0220 0.0104 -0.0716 167 GLN A CG 958 C CD . GLN A 174 ? 0.3970 0.4868 0.3181 -0.0746 -0.0403 -0.0956 167 GLN A CD 959 O OE1 . GLN A 174 ? 0.5229 0.5587 0.3450 -0.0747 -0.1055 -0.0659 167 GLN A OE1 960 N NE2 . GLN A 174 ? 0.4645 0.4530 0.3900 -0.0331 0.0072 -0.0510 167 GLN A NE2 961 N N . GLY A 175 ? 0.3286 0.3805 0.2476 0.0091 0.0424 -0.0918 168 GLY A N 962 C CA . GLY A 175 ? 0.3792 0.4050 0.2287 0.0490 0.0636 -0.1230 168 GLY A CA 963 C C . GLY A 175 ? 0.3464 0.4036 0.2660 0.0379 0.0343 -0.1025 168 GLY A C 964 O O . GLY A 175 ? 0.3839 0.3978 0.2635 0.0340 0.0403 -0.0937 168 GLY A O 965 N N . MET A 176 ? 0.3646 0.4328 0.2402 0.0304 -0.0144 -0.1358 169 MET A N 966 C CA . MET A 176 ? 0.3919 0.3948 0.2150 0.0229 -0.0095 -0.1328 169 MET A CA 967 C C . MET A 176 ? 0.3866 0.4446 0.2431 0.0203 -0.0162 -0.1340 169 MET A C 968 O O . MET A 176 ? 0.4238 0.4809 0.2598 0.0219 -0.0001 -0.1481 169 MET A O 969 C CB . MET A 176 ? 0.4802 0.3964 0.2824 -0.0040 -0.0041 -0.1505 169 MET A CB 970 C CG . MET A 176 ? 0.4835 0.5508 0.3328 -0.0039 0.0401 -0.0785 169 MET A CG 971 S SD . MET A 176 ? 0.8470 0.5927 0.7216 -0.1799 0.0099 -0.1296 169 MET A SD 972 C CE . MET A 176 ? 0.7076 0.7149 0.5268 0.0545 0.1154 -0.1082 169 MET A CE 973 N N . PRO A 177 ? 0.3845 0.4072 0.2831 0.0288 0.0197 -0.1070 170 PRO A N 974 C CA . PRO A 177 ? 0.4586 0.4426 0.2338 0.0472 0.0445 -0.0958 170 PRO A CA 975 C C . PRO A 177 ? 0.4669 0.4678 0.2737 0.0597 0.0440 -0.1049 170 PRO A C 976 O O . PRO A 177 ? 0.4754 0.4120 0.3321 0.0740 0.0875 -0.0386 170 PRO A O 977 C CB . PRO A 177 ? 0.4606 0.4185 0.2432 0.0552 0.0106 -0.0907 170 PRO A CB 978 C CG . PRO A 177 ? 0.4000 0.4171 0.2723 0.0261 0.0473 -0.0569 170 PRO A CG 979 C CD . PRO A 177 ? 0.4197 0.4229 0.2694 0.0033 0.0062 -0.1091 170 PRO A CD 980 N N A GLU A 178 ? 0.4669 0.4581 0.2996 0.0532 0.0965 -0.0821 171 GLU A N 981 N N B GLU A 178 ? 0.4651 0.4485 0.2983 0.0552 0.0911 -0.0948 171 GLU A N 982 C CA A GLU A 178 ? 0.4848 0.4657 0.2850 0.0636 0.1005 -0.0863 171 GLU A CA 983 C CA B GLU A 178 ? 0.4775 0.4606 0.2691 0.0570 0.0950 -0.0988 171 GLU A CA 984 C C A GLU A 178 ? 0.4823 0.5011 0.3425 0.0261 0.0570 -0.0701 171 GLU A C 985 C C B GLU A 178 ? 0.4727 0.4795 0.3178 0.0274 0.0499 -0.0784 171 GLU A C 986 O O A GLU A 178 ? 0.5058 0.4956 0.3076 0.0007 0.0463 -0.0597 171 GLU A O 987 O O B GLU A 178 ? 0.3974 0.5150 0.2896 -0.0004 0.0221 -0.1032 171 GLU A O 988 C CB A GLU A 178 ? 0.5655 0.4740 0.3202 0.0327 -0.0061 -0.0786 171 GLU A CB 989 C CB B GLU A 178 ? 0.4800 0.4494 0.3400 0.0142 0.0716 -0.1036 171 GLU A CB 990 C CG A GLU A 178 ? 0.5696 0.5135 0.4065 0.0248 0.0116 -0.0827 171 GLU A CG 991 C CG B GLU A 178 ? 0.5021 0.4840 0.3140 0.0321 0.0921 -0.0765 171 GLU A CG 992 C CD A GLU A 178 ? 0.6069 0.5796 0.3310 0.0748 0.0412 -0.0669 171 GLU A CD 993 C CD B GLU A 178 ? 0.5295 0.5376 0.3396 0.0174 0.0633 -0.0894 171 GLU A CD 994 O OE1 A GLU A 178 ? 0.6843 0.6288 0.3283 0.0162 0.0788 -0.0379 171 GLU A OE1 995 O OE1 B GLU A 178 ? 0.6004 0.6645 0.2634 0.0128 0.1215 -0.1912 171 GLU A OE1 996 O OE2 A GLU A 178 ? 0.5243 0.5938 0.4620 0.1856 0.1294 -0.1250 171 GLU A OE2 997 O OE2 B GLU A 178 ? 0.5956 0.4957 0.4368 0.0484 0.0564 -0.0574 171 GLU A OE2 998 N N . GLY A 179 ? 0.5016 0.5046 0.2433 0.0136 0.0325 -0.0711 172 GLY A N 999 C CA . GLY A 179 ? 0.4555 0.5449 0.3297 0.0148 0.0679 -0.0493 172 GLY A CA 1000 C C . GLY A 179 ? 0.4420 0.4507 0.3400 0.0463 0.1110 -0.0865 172 GLY A C 1001 O O . GLY A 179 ? 0.4399 0.4582 0.3630 0.0188 0.1024 -0.0349 172 GLY A O 1002 N N . ASP A 180 ? 0.4559 0.4549 0.2637 0.0508 0.1290 -0.0753 173 ASP A N 1003 C CA . ASP A 180 ? 0.4862 0.4750 0.2979 0.0431 0.0979 -0.0705 173 ASP A CA 1004 C C . ASP A 180 ? 0.4203 0.4176 0.2964 0.0414 0.1179 -0.0731 173 ASP A C 1005 O O . ASP A 180 ? 0.4223 0.3938 0.2657 0.0604 0.0857 -0.0636 173 ASP A O 1006 C CB . ASP A 180 ? 0.5112 0.5075 0.3245 0.0454 0.1424 -0.0656 173 ASP A CB 1007 C CG . ASP A 180 ? 0.6864 0.5681 0.3059 0.0594 0.1318 -0.0509 173 ASP A CG 1008 O OD1 . ASP A 180 ? 0.7632 0.6007 0.2931 0.0209 0.1966 -0.0796 173 ASP A OD1 1009 O OD2 . ASP A 180 ? 0.5630 0.5882 0.3293 0.1221 0.1558 -0.0324 173 ASP A OD2 1010 N N . LEU A 181 ? 0.4231 0.4112 0.2750 0.0182 0.1255 -0.0364 174 LEU A N 1011 C CA . LEU A 181 ? 0.3464 0.3966 0.2802 0.0165 0.1297 -0.0449 174 LEU A CA 1012 C C . LEU A 181 ? 0.4248 0.3749 0.2994 0.0489 0.1075 -0.0657 174 LEU A C 1013 O O . LEU A 181 ? 0.4230 0.3877 0.3134 0.0482 0.1087 -0.0327 174 LEU A O 1014 C CB . LEU A 181 ? 0.4109 0.4037 0.3251 0.0305 0.0992 -0.0354 174 LEU A CB 1015 C CG A LEU A 181 ? 0.3643 0.4318 0.3185 0.0548 0.1557 -0.0589 174 LEU A CG 1016 C CG B LEU A 181 ? 0.3556 0.3964 0.2351 0.0128 0.1404 -0.0727 174 LEU A CG 1017 C CD1 A LEU A 181 ? 0.3647 0.3986 0.2984 0.0587 0.1737 -0.0402 174 LEU A CD1 1018 C CD1 B LEU A 181 ? 0.3760 0.3993 0.2593 0.0105 0.1053 -0.0875 174 LEU A CD1 1019 C CD2 A LEU A 181 ? 0.3840 0.4207 0.2647 0.0439 0.1213 -0.0275 174 LEU A CD2 1020 C CD2 B LEU A 181 ? 0.3300 0.3633 0.2734 0.0161 0.1412 -0.0585 174 LEU A CD2 1021 N N . VAL A 182 ? 0.3965 0.3918 0.2543 0.0337 0.1235 -0.0498 175 VAL A N 1022 C CA . VAL A 182 ? 0.4147 0.3759 0.3053 0.0482 0.1081 -0.0576 175 VAL A CA 1023 C C . VAL A 182 ? 0.3548 0.3367 0.3080 0.0007 0.1102 -0.0446 175 VAL A C 1024 O O . VAL A 182 ? 0.3870 0.3550 0.3014 -0.0096 0.1236 -0.0116 175 VAL A O 1025 C CB . VAL A 182 ? 0.4557 0.3547 0.3276 -0.0064 0.0765 -0.0032 175 VAL A CB 1026 C CG1 . VAL A 182 ? 0.4193 0.3222 0.3775 0.0016 0.0929 -0.0073 175 VAL A CG1 1027 C CG2 . VAL A 182 ? 0.4529 0.4409 0.3328 0.0098 0.0926 0.0181 175 VAL A CG2 1028 N N . TYR A 183 ? 0.3296 0.3507 0.3149 0.0056 0.1028 0.0038 176 TYR A N 1029 C CA . TYR A 183 ? 0.3042 0.3520 0.2905 0.0465 0.1246 -0.0536 176 TYR A CA 1030 C C . TYR A 183 ? 0.3166 0.3480 0.3154 0.0274 0.1392 -0.0324 176 TYR A C 1031 O O . TYR A 183 ? 0.3664 0.3312 0.3349 0.0262 0.1155 -0.0261 176 TYR A O 1032 C CB . TYR A 183 ? 0.3105 0.2960 0.3118 0.0345 0.0837 0.0254 176 TYR A CB 1033 C CG . TYR A 183 ? 0.3327 0.3458 0.3055 0.0313 0.1106 -0.0591 176 TYR A CG 1034 C CD1 . TYR A 183 ? 0.2883 0.3175 0.3245 0.0169 0.0788 -0.0230 176 TYR A CD1 1035 C CD2 . TYR A 183 ? 0.2942 0.2906 0.3501 0.0734 0.0635 -0.0220 176 TYR A CD2 1036 C CE1 . TYR A 183 ? 0.3066 0.3274 0.3460 0.0416 0.0784 -0.0704 176 TYR A CE1 1037 C CE2 . TYR A 183 ? 0.3429 0.3605 0.3277 0.0175 0.1034 -0.0372 176 TYR A CE2 1038 C CZ . TYR A 183 ? 0.3187 0.3080 0.3210 0.0243 0.0930 -0.0526 176 TYR A CZ 1039 O OH . TYR A 183 ? 0.3054 0.2827 0.3267 0.0019 0.1123 -0.0456 176 TYR A OH 1040 N N . VAL A 184 ? 0.3256 0.2881 0.3070 0.0266 0.1355 -0.0581 177 VAL A N 1041 C CA . VAL A 184 ? 0.3299 0.2909 0.2829 0.0287 0.1216 -0.0353 177 VAL A CA 1042 C C . VAL A 184 ? 0.2994 0.2904 0.3161 0.0050 0.1051 -0.0318 177 VAL A C 1043 O O . VAL A 184 ? 0.3282 0.2926 0.3022 0.0312 0.1075 -0.0148 177 VAL A O 1044 C CB . VAL A 184 ? 0.3100 0.3298 0.2998 -0.0005 0.1132 0.0081 177 VAL A CB 1045 C CG1 . VAL A 184 ? 0.3428 0.3429 0.3400 -0.0252 0.0658 0.0218 177 VAL A CG1 1046 C CG2 . VAL A 184 ? 0.2578 0.3342 0.3259 0.0043 0.1196 -0.0083 177 VAL A CG2 1047 N N . ASN A 185 ? 0.2890 0.2990 0.3127 -0.0145 0.0813 0.0176 178 ASN A N 1048 C CA . ASN A 185 ? 0.2807 0.2687 0.2951 -0.0070 0.0919 -0.0244 178 ASN A CA 1049 C C . ASN A 185 ? 0.2583 0.2824 0.2902 -0.0062 0.0810 -0.0423 178 ASN A C 1050 O O . ASN A 185 ? 0.2665 0.2907 0.3200 -0.0167 0.0751 -0.0286 178 ASN A O 1051 C CB . ASN A 185 ? 0.2819 0.2645 0.3113 -0.0067 0.0886 -0.0164 178 ASN A CB 1052 C CG . ASN A 185 ? 0.2663 0.2729 0.3493 -0.0025 0.0983 -0.0319 178 ASN A CG 1053 O OD1 . ASN A 185 ? 0.2501 0.3197 0.3727 0.0293 0.1075 -0.0086 178 ASN A OD1 1054 N ND2 . ASN A 185 ? 0.2637 0.2809 0.3353 -0.0232 0.0880 -0.0295 178 ASN A ND2 1055 N N . TYR A 186 ? 0.2470 0.2757 0.3008 0.0317 0.1098 -0.0372 179 TYR A N 1056 C CA . TYR A 186 ? 0.2347 0.2802 0.2487 -0.0271 0.0753 -0.0431 179 TYR A CA 1057 C C . TYR A 186 ? 0.2555 0.2889 0.2763 -0.0020 0.0733 -0.0307 179 TYR A C 1058 O O . TYR A 186 ? 0.2403 0.2714 0.2724 -0.0096 0.0676 -0.0197 179 TYR A O 1059 C CB . TYR A 186 ? 0.2479 0.2736 0.2557 -0.0067 0.0387 -0.0323 179 TYR A CB 1060 C CG . TYR A 186 ? 0.2214 0.2892 0.3206 0.0064 0.0624 -0.0150 179 TYR A CG 1061 C CD1 . TYR A 186 ? 0.2243 0.2475 0.3658 0.0065 0.0672 -0.0374 179 TYR A CD1 1062 C CD2 . TYR A 186 ? 0.1967 0.3012 0.3241 0.0255 0.0605 -0.0321 179 TYR A CD2 1063 C CE1 . TYR A 186 ? 0.2037 0.3116 0.3977 -0.0019 0.0781 -0.0247 179 TYR A CE1 1064 C CE2 . TYR A 186 ? 0.2315 0.2927 0.3815 0.0332 0.0452 -0.0153 179 TYR A CE2 1065 C CZ . TYR A 186 ? 0.1856 0.2908 0.3838 0.0240 0.0880 -0.0168 179 TYR A CZ 1066 O OH . TYR A 186 ? 0.2130 0.2973 0.4146 0.0080 0.0448 -0.0258 179 TYR A OH 1067 N N . ALA A 187 ? 0.2536 0.2632 0.2862 -0.0087 0.0730 -0.0274 180 ALA A N 1068 C CA . ALA A 187 ? 0.2673 0.2619 0.2913 -0.0050 0.0737 -0.0421 180 ALA A CA 1069 C C . ALA A 187 ? 0.2564 0.2733 0.2647 -0.0002 0.0666 -0.0361 180 ALA A C 1070 O O . ALA A 187 ? 0.2442 0.2739 0.2674 -0.0082 0.0627 -0.0282 180 ALA A O 1071 C CB . ALA A 187 ? 0.2830 0.2646 0.2992 -0.0180 0.0664 -0.0392 180 ALA A CB 1072 N N . ARG A 188 ? 0.2539 0.2517 0.2897 -0.0153 0.0856 -0.0549 181 ARG A N 1073 C CA . ARG A 188 ? 0.2556 0.2380 0.2637 0.0176 0.0801 -0.0292 181 ARG A CA 1074 C C . ARG A 188 ? 0.2566 0.2434 0.2809 0.0090 0.0902 -0.0249 181 ARG A C 1075 O O . ARG A 188 ? 0.2842 0.2486 0.2873 -0.0003 0.1018 -0.0205 181 ARG A O 1076 C CB . ARG A 188 ? 0.2654 0.2626 0.2629 -0.0028 0.0786 -0.0269 181 ARG A CB 1077 C CG . ARG A 188 ? 0.2692 0.2904 0.3144 0.0213 0.0301 0.0005 181 ARG A CG 1078 C CD . ARG A 188 ? 0.2548 0.3196 0.3006 -0.0534 0.0708 -0.0326 181 ARG A CD 1079 N NE . ARG A 188 ? 0.2541 0.2434 0.3589 -0.0439 0.0969 -0.0029 181 ARG A NE 1080 C CZ . ARG A 188 ? 0.2615 0.3062 0.3543 -0.0124 0.0651 -0.0258 181 ARG A CZ 1081 N NH1 . ARG A 188 ? 0.3455 0.2942 0.3612 -0.0309 0.0532 -0.0545 181 ARG A NH1 1082 N NH2 . ARG A 188 ? 0.2383 0.3290 0.4457 -0.0458 0.1172 -0.0199 181 ARG A NH2 1083 N N . THR A 189 ? 0.3015 0.1986 0.2833 -0.0091 0.0979 -0.0227 182 THR A N 1084 C CA . THR A 189 ? 0.2935 0.2187 0.2688 0.0156 0.0869 -0.0156 182 THR A CA 1085 C C . THR A 189 ? 0.3158 0.2285 0.3074 -0.0089 0.0882 0.0096 182 THR A C 1086 O O . THR A 189 ? 0.3533 0.2661 0.2979 0.0213 0.0840 -0.0155 182 THR A O 1087 C CB . THR A 189 ? 0.2744 0.2259 0.2833 0.0268 0.1225 0.0073 182 THR A CB 1088 O OG1 . THR A 189 ? 0.2902 0.2601 0.2572 -0.0009 0.1076 0.0068 182 THR A OG1 1089 C CG2 . THR A 189 ? 0.3097 0.2239 0.3002 0.0331 0.0813 0.0171 182 THR A CG2 1090 N N . GLU A 190 ? 0.3103 0.2795 0.3321 -0.0268 0.0954 0.0007 183 GLU A N 1091 C CA . GLU A 190 ? 0.3287 0.2885 0.3492 -0.0171 0.1212 -0.0129 183 GLU A CA 1092 C C . GLU A 190 ? 0.3148 0.2879 0.3492 -0.0038 0.1218 -0.0163 183 GLU A C 1093 O O . GLU A 190 ? 0.3702 0.2966 0.3481 -0.0423 0.1117 -0.0091 183 GLU A O 1094 C CB . GLU A 190 ? 0.3050 0.2973 0.3943 -0.0333 0.0922 -0.0081 183 GLU A CB 1095 C CG . GLU A 190 ? 0.3356 0.3624 0.3924 -0.0350 0.0855 0.0214 183 GLU A CG 1096 C CD . GLU A 190 ? 0.3888 0.4426 0.3800 0.0263 0.0726 0.0199 183 GLU A CD 1097 O OE1 . GLU A 190 ? 0.3337 0.3309 0.4277 -0.0652 0.0619 -0.0028 183 GLU A OE1 1098 O OE2 . GLU A 190 ? 0.4092 0.4001 0.3733 0.0096 0.0152 0.0033 183 GLU A OE2 1099 N N . ASP A 191 ? 0.3035 0.2757 0.3396 0.0338 0.1194 -0.0296 184 ASP A N 1100 C CA . ASP A 191 ? 0.3696 0.2513 0.3120 0.0107 0.1081 -0.0196 184 ASP A CA 1101 C C . ASP A 191 ? 0.3303 0.3234 0.3088 -0.0067 0.1334 -0.0289 184 ASP A C 1102 O O . ASP A 191 ? 0.3596 0.3191 0.3055 0.0067 0.1444 0.0057 184 ASP A O 1103 C CB . ASP A 191 ? 0.3093 0.2518 0.3592 0.0233 0.0850 0.0091 184 ASP A CB 1104 C CG . ASP A 191 ? 0.2680 0.2868 0.3189 -0.0025 0.1218 0.0056 184 ASP A CG 1105 O OD1 . ASP A 191 ? 0.2544 0.2857 0.4101 -0.0009 0.1308 0.0312 184 ASP A OD1 1106 O OD2 . ASP A 191 ? 0.2539 0.2489 0.3242 0.0165 0.1017 0.0186 184 ASP A OD2 1107 N N . PHE A 192 ? 0.3217 0.2578 0.3175 0.0057 0.1212 -0.0266 185 PHE A N 1108 C CA . PHE A 192 ? 0.2720 0.2986 0.3391 -0.0003 0.1133 0.0040 185 PHE A CA 1109 C C . PHE A 192 ? 0.3152 0.3184 0.2800 -0.0019 0.1293 0.0088 185 PHE A C 1110 O O . PHE A 192 ? 0.3957 0.3267 0.2884 0.0047 0.1599 0.0092 185 PHE A O 1111 C CB . PHE A 192 ? 0.2843 0.2993 0.2700 -0.0479 0.1412 -0.0245 185 PHE A CB 1112 C CG . PHE A 192 ? 0.2524 0.2766 0.2695 -0.0021 0.1289 -0.0222 185 PHE A CG 1113 C CD1 . PHE A 192 ? 0.2903 0.3095 0.2956 -0.0112 0.1231 0.0094 185 PHE A CD1 1114 C CD2 . PHE A 192 ? 0.2753 0.2739 0.2723 0.0035 0.1038 -0.0184 185 PHE A CD2 1115 C CE1 . PHE A 192 ? 0.2924 0.2978 0.2511 0.0056 0.0934 -0.0307 185 PHE A CE1 1116 C CE2 . PHE A 192 ? 0.2819 0.2900 0.2607 -0.0197 0.0898 -0.0302 185 PHE A CE2 1117 C CZ . PHE A 192 ? 0.2815 0.3048 0.2530 0.0014 0.0902 -0.0206 185 PHE A CZ 1118 N N . PHE A 193 ? 0.3420 0.3251 0.2859 -0.0502 0.1200 0.0287 186 PHE A N 1119 C CA . PHE A 193 ? 0.3972 0.2847 0.3295 -0.0253 0.1170 0.0201 186 PHE A CA 1120 C C . PHE A 193 ? 0.3913 0.3818 0.3430 -0.0054 0.1044 -0.0019 186 PHE A C 1121 O O . PHE A 193 ? 0.4349 0.3229 0.3889 0.0282 0.1644 0.0406 186 PHE A O 1122 C CB . PHE A 193 ? 0.4169 0.3126 0.3571 -0.0198 0.1272 -0.0239 186 PHE A CB 1123 C CG . PHE A 193 ? 0.3690 0.3312 0.3649 -0.0197 0.1055 0.0192 186 PHE A CG 1124 C CD1 . PHE A 193 ? 0.3738 0.3562 0.3879 0.0249 0.0964 -0.0093 186 PHE A CD1 1125 C CD2 . PHE A 193 ? 0.4255 0.3243 0.3545 0.0128 0.1305 0.0026 186 PHE A CD2 1126 C CE1 . PHE A 193 ? 0.3735 0.3075 0.3795 0.0166 0.0798 -0.0046 186 PHE A CE1 1127 C CE2 . PHE A 193 ? 0.3358 0.3304 0.3612 0.0025 0.1064 0.0293 186 PHE A CE2 1128 C CZ . PHE A 193 ? 0.3876 0.2466 0.3439 0.0464 0.0687 0.0536 186 PHE A CZ 1129 N N . LYS A 194 ? 0.3641 0.3308 0.3934 0.0294 0.1446 -0.0219 187 LYS A N 1130 C CA . LYS A 194 ? 0.3704 0.3809 0.3525 -0.0333 0.1936 0.0270 187 LYS A CA 1131 C C . LYS A 194 ? 0.3807 0.4211 0.4014 -0.0080 0.1935 -0.0099 187 LYS A C 1132 O O . LYS A 194 ? 0.4232 0.4746 0.4061 -0.0345 0.1966 0.0204 187 LYS A O 1133 C CB . LYS A 194 ? 0.3257 0.4111 0.4366 0.0196 0.1546 -0.0205 187 LYS A CB 1134 C CG . LYS A 194 ? 0.3573 0.4704 0.5572 0.0372 0.1823 -0.0688 187 LYS A CG 1135 C CD . LYS A 194 ? 0.4636 0.5293 0.6553 -0.0174 0.0579 -0.0443 187 LYS A CD 1136 C CE . LYS A 194 ? 0.6502 0.6445 0.6507 -0.0472 0.0091 -0.1043 187 LYS A CE 1137 N NZ . LYS A 194 ? 0.7327 0.5263 1.0705 -0.0345 0.0379 -0.1211 187 LYS A NZ 1138 N N . LEU A 195 ? 0.3724 0.3640 0.4150 0.0064 0.1587 -0.0137 188 LEU A N 1139 C CA . LEU A 195 ? 0.4353 0.4017 0.3392 -0.0503 0.1919 0.0297 188 LEU A CA 1140 C C . LEU A 195 ? 0.4194 0.4451 0.3969 -0.0250 0.1578 0.0258 188 LEU A C 1141 O O . LEU A 195 ? 0.4558 0.4200 0.4054 -0.0170 0.1848 -0.0685 188 LEU A O 1142 C CB . LEU A 195 ? 0.3930 0.4071 0.4111 -0.0311 0.2043 0.0383 188 LEU A CB 1143 C CG . LEU A 195 ? 0.3879 0.4627 0.4055 0.0130 0.2286 0.0671 188 LEU A CG 1144 C CD1 . LEU A 195 ? 0.4053 0.4465 0.4484 -0.0214 0.2315 0.0202 188 LEU A CD1 1145 C CD2 . LEU A 195 ? 0.5093 0.3782 0.4752 0.0701 0.1479 -0.0393 188 LEU A CD2 1146 N N A GLU A 196 ? 0.4593 0.4451 0.4114 0.0018 0.1322 -0.0390 189 GLU A N 1147 N N B GLU A 196 ? 0.4557 0.4381 0.3964 -0.0042 0.1433 -0.0274 189 GLU A N 1148 C CA A GLU A 196 ? 0.4435 0.4455 0.4614 0.0129 0.1675 0.0024 189 GLU A CA 1149 C CA B GLU A 196 ? 0.4259 0.4348 0.4310 0.0129 0.1774 -0.0074 189 GLU A CA 1150 C C A GLU A 196 ? 0.5078 0.4409 0.4103 0.0027 0.1696 -0.0043 189 GLU A C 1151 C C B GLU A 196 ? 0.4903 0.4322 0.3981 0.0015 0.1807 -0.0047 189 GLU A C 1152 O O A GLU A 196 ? 0.5819 0.3688 0.3787 0.0336 0.1413 -0.0363 189 GLU A O 1153 O O B GLU A 196 ? 0.5442 0.3853 0.3807 0.0081 0.1866 -0.0346 189 GLU A O 1154 C CB A GLU A 196 ? 0.4473 0.5213 0.5318 0.0340 0.1708 -0.0476 189 GLU A CB 1155 C CB B GLU A 196 ? 0.4272 0.4191 0.3877 -0.0052 0.1869 -0.0405 189 GLU A CB 1156 C CG A GLU A 196 ? 0.5866 0.5018 0.5043 -0.0199 0.0766 0.0796 189 GLU A CG 1157 C CG B GLU A 196 ? 0.4530 0.4473 0.4334 -0.0271 0.1963 0.0251 189 GLU A CG 1158 C CD A GLU A 196 ? 0.5817 0.4590 0.6153 -0.0160 -0.0074 0.0497 189 GLU A CD 1159 C CD B GLU A 196 ? 0.4382 0.4122 0.4917 0.0159 0.1298 0.0059 189 GLU A CD 1160 O OE1 A GLU A 196 ? 0.4938 0.4989 0.7295 -0.0308 0.0822 0.0603 189 GLU A OE1 1161 O OE1 B GLU A 196 ? 0.4485 0.4308 0.3792 -0.0067 0.1413 0.0327 189 GLU A OE1 1162 O OE2 A GLU A 196 ? 0.6087 0.4390 0.3889 -0.0403 0.1025 0.0427 189 GLU A OE2 1163 O OE2 B GLU A 196 ? 0.4154 0.4571 0.4337 0.0248 0.1369 -0.0391 189 GLU A OE2 1164 N N . ARG A 197 ? 0.4768 0.4217 0.3653 0.0075 0.1732 0.0152 190 ARG A N 1165 C CA . ARG A 197 ? 0.4939 0.4292 0.3611 -0.0130 0.1877 -0.0159 190 ARG A CA 1166 C C . ARG A 197 ? 0.4972 0.4195 0.4113 0.0035 0.2056 0.0292 190 ARG A C 1167 O O . ARG A 197 ? 0.5251 0.4541 0.4462 0.0291 0.2138 0.0714 190 ARG A O 1168 C CB . ARG A 197 ? 0.4549 0.4026 0.3685 0.0246 0.1764 -0.0228 190 ARG A CB 1169 C CG . ARG A 197 ? 0.4352 0.3086 0.3152 0.0103 0.1430 0.0027 190 ARG A CG 1170 C CD . ARG A 197 ? 0.4385 0.2801 0.3506 0.0413 0.1137 -0.0178 190 ARG A CD 1171 N NE . ARG A 197 ? 0.4603 0.3324 0.3376 0.0236 0.1635 -0.0393 190 ARG A NE 1172 C CZ . ARG A 197 ? 0.4201 0.2958 0.3280 0.0010 0.1180 -0.0394 190 ARG A CZ 1173 N NH1 . ARG A 197 ? 0.3878 0.2921 0.3205 -0.0203 0.1245 -0.0140 190 ARG A NH1 1174 N NH2 . ARG A 197 ? 0.4278 0.3289 0.3736 0.0180 0.0987 -0.0105 190 ARG A NH2 1175 N N . ASP A 198 ? 0.5160 0.3953 0.3873 0.0019 0.1977 0.0092 191 ASP A N 1176 C CA . ASP A 198 ? 0.5132 0.4017 0.4397 0.0115 0.1814 0.0228 191 ASP A CA 1177 C C . ASP A 198 ? 0.5025 0.4628 0.4201 -0.0101 0.2528 0.0171 191 ASP A C 1178 O O . ASP A 198 ? 0.5688 0.4127 0.4425 -0.0488 0.2721 0.0266 191 ASP A O 1179 C CB . ASP A 198 ? 0.5238 0.4640 0.4381 0.0209 0.1850 0.0202 191 ASP A CB 1180 C CG . ASP A 198 ? 0.6517 0.4651 0.5037 -0.0472 0.1403 -0.0255 191 ASP A CG 1181 O OD1 . ASP A 198 ? 0.6755 0.4894 0.6369 0.0598 0.1036 -0.1249 191 ASP A OD1 1182 O OD2 . ASP A 198 ? 0.6237 0.6275 0.5127 -0.1556 0.1356 0.0293 191 ASP A OD2 1183 N N . MET A 199 ? 0.5432 0.4361 0.4247 -0.0055 0.2071 -0.0156 192 MET A N 1184 C CA . MET A 199 ? 0.5304 0.4299 0.4035 -0.0180 0.2422 0.0113 192 MET A CA 1185 C C . MET A 199 ? 0.5442 0.4883 0.3832 0.0378 0.2426 0.0154 192 MET A C 1186 O O . MET A 199 ? 0.5452 0.4511 0.4384 -0.0149 0.2593 -0.0211 192 MET A O 1187 C CB . MET A 199 ? 0.5172 0.4377 0.3964 0.0234 0.2017 0.0331 192 MET A CB 1188 C CG . MET A 199 ? 0.5317 0.4401 0.4888 -0.0464 0.1463 0.0092 192 MET A CG 1189 S SD . MET A 199 ? 0.4455 0.4699 0.5317 0.0393 0.1555 0.0357 192 MET A SD 1190 C CE . MET A 199 ? 0.4622 0.4879 0.5626 0.0930 0.1743 0.0427 192 MET A CE 1191 N N . LYS A 200 ? 0.5016 0.4576 0.4106 -0.0194 0.2286 0.0188 193 LYS A N 1192 C CA . LYS A 200 ? 0.4867 0.4751 0.3771 -0.0079 0.2354 0.0610 193 LYS A CA 1193 C C . LYS A 200 ? 0.6051 0.5295 0.3816 -0.0164 0.2356 -0.0003 193 LYS A C 1194 O O . LYS A 200 ? 0.6349 0.6409 0.3524 0.0029 0.1750 0.0557 193 LYS A O 1195 C CB . LYS A 200 ? 0.4959 0.5242 0.3682 0.0262 0.2140 0.0956 193 LYS A CB 1196 C CG . LYS A 200 ? 0.7197 0.5407 0.4419 -0.0830 0.0874 0.1676 193 LYS A CG 1197 C CD . LYS A 200 ? 0.7430 0.6266 0.4399 -0.0777 0.1078 0.0913 193 LYS A CD 1198 C CE . LYS A 200 ? 0.6705 0.6211 0.6131 -0.0468 0.1929 0.0819 193 LYS A CE 1199 N NZ . LYS A 200 ? 0.7548 0.6421 0.5566 -0.0155 0.2720 0.1819 193 LYS A NZ 1200 N N . ILE A 201 ? 0.4898 0.4600 0.4644 0.0251 0.2433 0.0251 194 ILE A N 1201 C CA . ILE A 201 ? 0.5198 0.4995 0.4643 -0.0150 0.2280 0.0663 194 ILE A CA 1202 C C . ILE A 201 ? 0.5239 0.4980 0.3678 -0.0273 0.2219 0.0304 194 ILE A C 1203 O O . ILE A 201 ? 0.5529 0.5671 0.3760 -0.0151 0.2551 0.0248 194 ILE A O 1204 C CB . ILE A 201 ? 0.5526 0.5361 0.4112 -0.0435 0.2269 0.1081 194 ILE A CB 1205 C CG1 . ILE A 201 ? 0.5388 0.5890 0.4414 0.0439 0.1777 0.0705 194 ILE A CG1 1206 C CG2 . ILE A 201 ? 0.6037 0.5120 0.2985 -0.0513 0.1578 0.0481 194 ILE A CG2 1207 C CD1 . ILE A 201 ? 0.6876 0.5852 0.3796 -0.0053 0.1125 0.1122 194 ILE A CD1 1208 N N . ASN A 202 ? 0.5527 0.4899 0.3480 -0.0046 0.2345 0.0030 195 ASN A N 1209 C CA . ASN A 202 ? 0.5356 0.5208 0.3909 0.0180 0.1042 0.0766 195 ASN A CA 1210 C C . ASN A 202 ? 0.5356 0.5165 0.3329 0.0054 0.1482 -0.0107 195 ASN A C 1211 O O . ASN A 202 ? 0.5650 0.5051 0.2971 0.0017 0.1311 -0.0055 195 ASN A O 1212 C CB . ASN A 202 ? 0.6121 0.6516 0.3545 -0.0278 0.1184 0.1040 195 ASN A CB 1213 C CG . ASN A 202 ? 0.6546 0.7373 0.4335 0.1066 0.1402 0.0531 195 ASN A CG 1214 O OD1 . ASN A 202 ? 0.6767 0.4872 0.4103 0.0831 0.0893 0.1371 195 ASN A OD1 1215 N ND2 . ASN A 202 ? 0.8553 0.7656 0.4827 0.0667 0.1177 0.1939 195 ASN A ND2 1216 N N . CYS A 203 ? 0.5068 0.4837 0.3406 0.0117 0.1477 0.0396 196 CYS A N 1217 C CA . CYS A 203 ? 0.5001 0.4677 0.3074 -0.0023 0.1587 -0.0065 196 CYS A CA 1218 C C . CYS A 203 ? 0.5080 0.5068 0.2909 0.0565 0.1152 0.0315 196 CYS A C 1219 O O . CYS A 203 ? 0.5162 0.4786 0.2974 0.0780 0.0796 0.0345 196 CYS A O 1220 C CB . CYS A 203 ? 0.5095 0.5561 0.3149 0.0078 0.1398 0.0580 196 CYS A CB 1221 S SG . CYS A 203 ? 0.5247 0.5038 0.3655 0.0673 0.1063 -0.0180 196 CYS A SG 1222 N N . SER A 204 ? 0.5131 0.4834 0.2944 0.0775 0.1132 0.0000 197 SER A N 1223 C CA . SER A 204 ? 0.5273 0.4985 0.3120 0.0428 0.0778 0.0248 197 SER A CA 1224 C C . SER A 204 ? 0.5115 0.5221 0.3018 0.0462 0.0996 0.0096 197 SER A C 1225 O O . SER A 204 ? 0.5975 0.5927 0.3162 0.0537 0.1248 -0.0484 197 SER A O 1226 C CB . SER A 204 ? 0.5310 0.5158 0.4007 -0.0187 0.0305 0.0848 197 SER A CB 1227 O OG . SER A 204 ? 0.4904 0.5838 0.4213 0.0370 0.0494 0.0297 197 SER A OG 1228 N N . GLY A 205 ? 0.5120 0.4928 0.2790 0.0424 0.0735 -0.0267 198 GLY A N 1229 C CA . GLY A 205 ? 0.5012 0.4571 0.2719 0.0338 0.0330 0.0081 198 GLY A CA 1230 C C . GLY A 205 ? 0.4891 0.4540 0.2798 0.0471 0.1146 -0.0781 198 GLY A C 1231 O O . GLY A 205 ? 0.5220 0.4553 0.2496 0.0447 0.0191 -0.0725 198 GLY A O 1232 N N . LYS A 206 ? 0.4804 0.5080 0.2593 0.0440 0.1105 0.0146 199 LYS A N 1233 C CA . LYS A 206 ? 0.4709 0.4306 0.2624 0.0157 0.1019 0.0067 199 LYS A CA 1234 C C . LYS A 206 ? 0.4539 0.4107 0.2259 0.0506 0.0948 -0.0309 199 LYS A C 1235 O O . LYS A 206 ? 0.4114 0.4014 0.2667 0.0514 0.0689 -0.0676 199 LYS A O 1236 C CB . LYS A 206 ? 0.4399 0.4711 0.2420 0.0330 0.1117 -0.0383 199 LYS A CB 1237 C CG . LYS A 206 ? 0.4480 0.4598 0.2749 0.0678 0.1080 -0.0105 199 LYS A CG 1238 C CD . LYS A 206 ? 0.5332 0.5583 0.2662 0.0407 0.1634 -0.0377 199 LYS A CD 1239 C CE . LYS A 206 ? 0.6196 0.6684 0.3218 0.0119 0.0628 0.1021 199 LYS A CE 1240 N NZ . LYS A 206 ? 0.7184 0.6975 0.3895 0.1220 0.0036 0.0813 199 LYS A NZ 1241 N N . ILE A 207 ? 0.3797 0.4137 0.2724 0.0444 0.1012 -0.0109 200 ILE A N 1242 C CA . ILE A 207 ? 0.4160 0.3780 0.2732 0.0476 0.0570 -0.0181 200 ILE A CA 1243 C C . ILE A 207 ? 0.4231 0.4103 0.2893 0.0435 0.0725 -0.0761 200 ILE A C 1244 O O . ILE A 207 ? 0.4173 0.4277 0.2967 -0.0054 0.0801 -0.0551 200 ILE A O 1245 C CB . ILE A 207 ? 0.4091 0.3812 0.2660 -0.0240 0.0654 -0.0014 200 ILE A CB 1246 C CG1 . ILE A 207 ? 0.4660 0.3941 0.2427 0.0267 -0.0242 -0.0386 200 ILE A CG1 1247 C CG2 . ILE A 207 ? 0.4173 0.3588 0.2580 0.0163 0.0770 -0.0050 200 ILE A CG2 1248 C CD1 . ILE A 207 ? 0.4380 0.4136 0.3525 0.0723 0.0166 -0.0994 200 ILE A CD1 1249 N N . VAL A 208 ? 0.3812 0.3393 0.2272 -0.0010 0.0532 -0.0180 201 VAL A N 1250 C CA . VAL A 208 ? 0.3426 0.3602 0.2464 0.0275 0.0530 -0.0210 201 VAL A CA 1251 C C . VAL A 208 ? 0.3241 0.3266 0.2982 0.0378 0.0495 -0.0234 201 VAL A C 1252 O O . VAL A 208 ? 0.3450 0.3396 0.2865 0.0362 0.0601 -0.0187 201 VAL A O 1253 C CB . VAL A 208 ? 0.3764 0.3519 0.2808 -0.0112 0.0611 -0.0244 201 VAL A CB 1254 C CG1 A VAL A 208 ? 0.3356 0.3176 0.3251 -0.0664 0.0159 -0.0039 201 VAL A CG1 1255 C CG1 B VAL A 208 ? 0.3636 0.3876 0.2533 0.0339 0.1161 -0.0188 201 VAL A CG1 1256 C CG2 A VAL A 208 ? 0.3314 0.2701 0.2508 -0.0060 0.0454 -0.0210 201 VAL A CG2 1257 C CG2 B VAL A 208 ? 0.3455 0.4097 0.3108 0.0067 0.1003 0.0124 201 VAL A CG2 1258 N N . ILE A 209 ? 0.3047 0.2871 0.2909 0.0304 0.0853 -0.0553 202 ILE A N 1259 C CA . ILE A 209 ? 0.3136 0.2823 0.2854 0.0098 0.0778 -0.0547 202 ILE A CA 1260 C C . ILE A 209 ? 0.3044 0.3021 0.2797 -0.0014 0.0898 -0.0427 202 ILE A C 1261 O O . ILE A 209 ? 0.3089 0.3258 0.2720 -0.0006 0.1165 -0.0088 202 ILE A O 1262 C CB . ILE A 209 ? 0.2861 0.2992 0.2494 0.0064 0.1328 -0.0322 202 ILE A CB 1263 C CG1 . ILE A 209 ? 0.3354 0.2858 0.3102 0.0268 0.0820 -0.0286 202 ILE A CG1 1264 C CG2 . ILE A 209 ? 0.2463 0.3262 0.2757 0.0088 0.1209 -0.0250 202 ILE A CG2 1265 C CD1 . ILE A 209 ? 0.3612 0.3262 0.2956 0.0513 0.1243 -0.0441 202 ILE A CD1 1266 N N . ALA A 210 ? 0.3144 0.2863 0.2546 0.0244 0.0677 -0.0626 203 ALA A N 1267 C CA . ALA A 210 ? 0.2876 0.2715 0.2643 0.0562 0.0587 -0.0622 203 ALA A CA 1268 C C . ALA A 210 ? 0.2593 0.3009 0.2701 0.0239 0.0492 -0.0394 203 ALA A C 1269 O O . ALA A 210 ? 0.2650 0.2873 0.3263 0.0103 0.0340 -0.0480 203 ALA A O 1270 C CB . ALA A 210 ? 0.2522 0.2988 0.2788 0.0526 0.0953 -0.0381 203 ALA A CB 1271 N N . ARG A 211 ? 0.2445 0.2896 0.2938 0.0239 0.0607 -0.0471 204 ARG A N 1272 C CA . ARG A 211 ? 0.2437 0.2749 0.2897 0.0112 0.0621 -0.0461 204 ARG A CA 1273 C C . ARG A 211 ? 0.2064 0.2600 0.3137 0.0058 0.0784 -0.0237 204 ARG A C 1274 O O . ARG A 211 ? 0.2159 0.2437 0.2898 -0.0103 0.0576 -0.0259 204 ARG A O 1275 C CB . ARG A 211 ? 0.2560 0.2757 0.3844 -0.0032 0.0402 -0.0067 204 ARG A CB 1276 C CG . ARG A 211 ? 0.2062 0.3235 0.4106 -0.0449 0.0345 0.0060 204 ARG A CG 1277 C CD . ARG A 211 ? 0.2099 0.3739 0.3591 -0.0641 0.0569 0.0357 204 ARG A CD 1278 N NE . ARG A 211 ? 0.2061 0.3297 0.4336 -0.0547 0.0874 -0.0158 204 ARG A NE 1279 C CZ . ARG A 211 ? 0.2107 0.3159 0.4027 -0.0363 0.0724 -0.0160 204 ARG A CZ 1280 N NH1 . ARG A 211 ? 0.2336 0.2933 0.4288 -0.0116 0.0844 -0.0065 204 ARG A NH1 1281 N NH2 . ARG A 211 ? 0.2416 0.3185 0.4001 -0.0379 0.1234 -0.0283 204 ARG A NH2 1282 N N . TYR A 212 ? 0.2073 0.2670 0.2710 0.0284 0.0828 -0.0299 205 TYR A N 1283 C CA . TYR A 212 ? 0.2203 0.2265 0.2504 -0.0119 0.0772 -0.0206 205 TYR A CA 1284 C C . TYR A 212 ? 0.2256 0.2649 0.2623 0.0050 0.0639 -0.0355 205 TYR A C 1285 O O . TYR A 212 ? 0.2221 0.2794 0.2927 0.0149 0.0365 -0.0565 205 TYR A O 1286 C CB . TYR A 212 ? 0.2185 0.2361 0.2949 -0.0039 0.0716 0.0109 205 TYR A CB 1287 C CG . TYR A 212 ? 0.2198 0.1827 0.3148 0.0185 0.0613 -0.0164 205 TYR A CG 1288 C CD1 . TYR A 212 ? 0.2393 0.1867 0.2869 0.0066 0.0325 -0.0293 205 TYR A CD1 1289 C CD2 . TYR A 212 ? 0.1569 0.2605 0.2231 0.0062 0.0327 -0.0053 205 TYR A CD2 1290 C CE1 . TYR A 212 ? 0.2166 0.2071 0.2716 0.0272 0.0720 -0.0190 205 TYR A CE1 1291 C CE2 . TYR A 212 ? 0.1868 0.2168 0.2596 -0.0083 0.0447 -0.0003 205 TYR A CE2 1292 C CZ . TYR A 212 ? 0.1865 0.2199 0.2857 0.0178 0.0360 -0.0135 205 TYR A CZ 1293 O OH . TYR A 212 ? 0.1926 0.2451 0.2431 0.0147 0.0594 -0.0372 205 TYR A OH 1294 N N . GLY A 213 ? 0.2650 0.2096 0.2926 0.0274 0.0279 -0.0424 206 GLY A N 1295 C CA . GLY A 213 ? 0.2553 0.2326 0.3515 0.0144 0.0277 -0.0545 206 GLY A CA 1296 C C . GLY A 213 ? 0.2198 0.2415 0.3203 0.0027 0.0356 -0.0362 206 GLY A C 1297 O O . GLY A 213 ? 0.2259 0.2436 0.3306 -0.0011 0.0403 -0.0048 206 GLY A O 1298 N N . LYS A 214 ? 0.1978 0.2387 0.3270 -0.0086 0.0458 -0.0530 207 LYS A N 1299 C CA . LYS A 214 ? 0.1962 0.2267 0.3248 -0.0085 0.0497 -0.0486 207 LYS A CA 1300 C C . LYS A 214 ? 0.2025 0.2476 0.3170 -0.0009 0.0411 -0.0519 207 LYS A C 1301 O O . LYS A 214 ? 0.2182 0.2812 0.3377 -0.0111 0.0186 -0.0888 207 LYS A O 1302 C CB . LYS A 214 ? 0.1868 0.2656 0.3400 0.0157 0.0742 -0.0257 207 LYS A CB 1303 C CG . LYS A 214 ? 0.1789 0.3155 0.4265 0.0155 0.0670 -0.0539 207 LYS A CG 1304 C CD . LYS A 214 ? 0.2437 0.3875 0.4748 0.0092 0.0227 -0.0762 207 LYS A CD 1305 C CE . LYS A 214 ? 0.1851 0.4791 0.4492 -0.0345 -0.0129 -0.0799 207 LYS A CE 1306 N NZ . LYS A 214 ? 0.2243 0.6057 0.4461 -0.0255 -0.0153 -0.0987 207 LYS A NZ 1307 N N . VAL A 215 ? 0.2085 0.2373 0.2931 -0.0033 0.0375 -0.0132 208 VAL A N 1308 C CA . VAL A 215 ? 0.1966 0.2340 0.2859 -0.0218 0.0511 -0.0125 208 VAL A CA 1309 C C . VAL A 215 ? 0.1901 0.2301 0.2679 -0.0164 0.0429 -0.0229 208 VAL A C 1310 O O . VAL A 215 ? 0.2118 0.2340 0.2742 0.0083 0.0287 -0.0378 208 VAL A O 1311 C CB . VAL A 215 ? 0.1990 0.2444 0.2761 -0.0165 0.0601 -0.0137 208 VAL A CB 1312 C CG1 . VAL A 215 ? 0.2009 0.2631 0.2839 -0.0265 0.0357 -0.0193 208 VAL A CG1 1313 C CG2 . VAL A 215 ? 0.2355 0.2921 0.3120 -0.0308 0.0187 -0.0409 208 VAL A CG2 1314 N N . PHE A 216 ? 0.1896 0.2276 0.2477 -0.0201 0.0339 -0.0226 209 PHE A N 1315 C CA . PHE A 216 ? 0.1555 0.2176 0.2205 -0.0040 0.0573 -0.0409 209 PHE A CA 1316 C C . PHE A 216 ? 0.2021 0.1986 0.2322 -0.0008 0.0268 -0.0189 209 PHE A C 1317 O O . PHE A 216 ? 0.1988 0.2135 0.2151 -0.0009 0.0294 -0.0116 209 PHE A O 1318 C CB . PHE A 216 ? 0.1413 0.2183 0.2349 -0.0044 0.0530 -0.0384 209 PHE A CB 1319 C CG . PHE A 216 ? 0.1566 0.2043 0.1821 -0.0096 0.0381 -0.0208 209 PHE A CG 1320 C CD1 . PHE A 216 ? 0.1782 0.1907 0.2035 -0.0151 0.0108 -0.0140 209 PHE A CD1 1321 C CD2 . PHE A 216 ? 0.1309 0.2589 0.2255 -0.0114 0.0380 -0.0256 209 PHE A CD2 1322 C CE1 . PHE A 216 ? 0.1716 0.2571 0.2604 -0.0219 0.0318 -0.0224 209 PHE A CE1 1323 C CE2 . PHE A 216 ? 0.2006 0.2504 0.2250 -0.0639 0.0221 -0.0228 209 PHE A CE2 1324 C CZ . PHE A 216 ? 0.1924 0.2247 0.2221 0.0002 0.0282 -0.0439 209 PHE A CZ 1325 N N . ARG A 217 ? 0.2258 0.1976 0.2336 -0.0065 0.0120 -0.0619 210 ARG A N 1326 C CA . ARG A 217 ? 0.2281 0.1965 0.2081 0.0076 0.0290 -0.0341 210 ARG A CA 1327 C C . ARG A 217 ? 0.2220 0.2153 0.2151 0.0125 0.0382 -0.0387 210 ARG A C 1328 O O . ARG A 217 ? 0.2390 0.2290 0.2164 0.0108 0.0287 -0.0191 210 ARG A O 1329 C CB . ARG A 217 ? 0.1854 0.1950 0.2315 -0.0066 0.0667 -0.0166 210 ARG A CB 1330 C CG . ARG A 217 ? 0.2003 0.1712 0.1924 -0.0198 0.0673 -0.0315 210 ARG A CG 1331 C CD . ARG A 217 ? 0.2068 0.1672 0.1781 0.0054 0.0063 -0.0336 210 ARG A CD 1332 N NE . ARG A 217 ? 0.2255 0.1811 0.1709 0.0041 0.0098 -0.0171 210 ARG A NE 1333 C CZ . ARG A 217 ? 0.1705 0.2205 0.1930 0.0363 0.0304 -0.0125 210 ARG A CZ 1334 N NH1 . ARG A 217 ? 0.1787 0.1717 0.2294 0.0338 0.0196 -0.0344 210 ARG A NH1 1335 N NH2 . ARG A 217 ? 0.2531 0.2012 0.1842 0.0124 -0.0001 -0.0130 210 ARG A NH2 1336 N N . GLY A 218 ? 0.2123 0.1856 0.2220 0.0125 0.0411 -0.0133 211 GLY A N 1337 C CA . GLY A 218 ? 0.2088 0.2177 0.2760 -0.0078 0.0215 0.0136 211 GLY A CA 1338 C C . GLY A 218 ? 0.1978 0.2188 0.2158 0.0051 0.0413 -0.0010 211 GLY A C 1339 O O . GLY A 218 ? 0.2445 0.2365 0.2166 0.0025 0.0267 -0.0050 211 GLY A O 1340 N N . ASN A 219 ? 0.2237 0.2091 0.2431 0.0039 0.0300 -0.0049 212 ASN A N 1341 C CA . ASN A 219 ? 0.2324 0.2162 0.2126 -0.0285 0.0378 -0.0240 212 ASN A CA 1342 C C . ASN A 219 ? 0.2599 0.2359 0.2264 0.0305 0.0435 -0.0160 212 ASN A C 1343 O O . ASN A 219 ? 0.2648 0.2220 0.2565 0.0127 0.0678 0.0069 212 ASN A O 1344 C CB . ASN A 219 ? 0.2460 0.2115 0.2234 -0.0066 -0.0008 -0.0229 212 ASN A CB 1345 C CG . ASN A 219 ? 0.2729 0.2242 0.2345 0.0024 0.0198 -0.0125 212 ASN A CG 1346 O OD1 . ASN A 219 ? 0.3139 0.2062 0.2361 0.0023 0.0221 -0.0058 212 ASN A OD1 1347 N ND2 . ASN A 219 ? 0.2436 0.2096 0.2500 0.0097 0.0185 -0.0354 212 ASN A ND2 1348 N N . LYS A 220 ? 0.2307 0.2189 0.2474 0.0120 0.0711 -0.0362 213 LYS A N 1349 C CA . LYS A 220 ? 0.2362 0.2271 0.2100 0.0079 0.0465 -0.0365 213 LYS A CA 1350 C C . LYS A 220 ? 0.2456 0.2492 0.2277 0.0053 0.0396 -0.0064 213 LYS A C 1351 O O . LYS A 220 ? 0.2633 0.2730 0.2276 0.0010 0.0495 -0.0001 213 LYS A O 1352 C CB . LYS A 220 ? 0.2293 0.2281 0.2339 -0.0006 0.0362 -0.0210 213 LYS A CB 1353 C CG . LYS A 220 ? 0.2184 0.2138 0.2420 -0.0025 0.0259 -0.0163 213 LYS A CG 1354 C CD . LYS A 220 ? 0.2204 0.2345 0.2272 0.0205 0.0389 -0.0175 213 LYS A CD 1355 C CE . LYS A 220 ? 0.1986 0.2431 0.2363 -0.0148 0.0451 0.0134 213 LYS A CE 1356 N NZ . LYS A 220 ? 0.2106 0.2369 0.2827 -0.0325 0.0563 -0.0186 213 LYS A NZ 1357 N N . VAL A 221 ? 0.2135 0.2196 0.2002 0.0346 0.0650 -0.0271 214 VAL A N 1358 C CA . VAL A 221 ? 0.2226 0.2471 0.2307 0.0170 0.0503 -0.0052 214 VAL A CA 1359 C C . VAL A 221 ? 0.2499 0.2533 0.1975 0.0138 0.0569 -0.0094 214 VAL A C 1360 O O . VAL A 221 ? 0.2679 0.2777 0.1974 0.0039 0.0191 -0.0021 214 VAL A O 1361 C CB . VAL A 221 ? 0.2306 0.2322 0.2342 0.0020 0.0361 -0.0119 214 VAL A CB 1362 C CG1 . VAL A 221 ? 0.2331 0.2930 0.2572 0.0034 0.0265 -0.0047 214 VAL A CG1 1363 C CG2 . VAL A 221 ? 0.2397 0.2441 0.2212 0.0092 0.0101 -0.0178 214 VAL A CG2 1364 N N . LYS A 222 ? 0.2498 0.2404 0.2179 0.0177 0.0365 -0.0258 215 LYS A N 1365 C CA . LYS A 222 ? 0.3105 0.2501 0.1939 0.0265 0.0781 -0.0075 215 LYS A CA 1366 C C . LYS A 222 ? 0.2772 0.3019 0.2256 -0.0078 0.0626 -0.0041 215 LYS A C 1367 O O . LYS A 222 ? 0.2733 0.2954 0.2284 0.0174 0.0492 -0.0125 215 LYS A O 1368 C CB . LYS A 222 ? 0.2424 0.2377 0.2252 0.0494 0.0489 -0.0277 215 LYS A CB 1369 C CG . LYS A 222 ? 0.3383 0.2299 0.2827 0.0526 0.0688 -0.0241 215 LYS A CG 1370 C CD . LYS A 222 ? 0.2771 0.2898 0.2607 0.0618 0.0809 -0.0248 215 LYS A CD 1371 C CE . LYS A 222 ? 0.4399 0.3006 0.4118 0.0033 0.0686 0.0412 215 LYS A CE 1372 N NZ . LYS A 222 ? 0.4854 0.4496 0.6083 -0.0474 0.0953 0.0468 215 LYS A NZ 1373 N N . ASN A 223 ? 0.2645 0.2656 0.2246 -0.0054 0.0723 -0.0100 216 ASN A N 1374 C CA . ASN A 223 ? 0.2600 0.2946 0.1885 -0.0051 0.0820 -0.0290 216 ASN A CA 1375 C C . ASN A 223 ? 0.3061 0.2788 0.1833 0.0080 0.0763 -0.0206 216 ASN A C 1376 O O . ASN A 223 ? 0.3160 0.3033 0.1882 0.0085 0.0824 0.0000 216 ASN A O 1377 C CB . ASN A 223 ? 0.2433 0.2648 0.2313 -0.0018 0.0709 -0.0247 216 ASN A CB 1378 C CG . ASN A 223 ? 0.2685 0.3191 0.2068 -0.0050 0.0636 -0.0215 216 ASN A CG 1379 O OD1 . ASN A 223 ? 0.2881 0.3032 0.2778 -0.0084 0.0525 -0.0365 216 ASN A OD1 1380 N ND2 . ASN A 223 ? 0.2567 0.2870 0.2101 -0.0067 0.0597 -0.0184 216 ASN A ND2 1381 N N . ALA A 224 ? 0.2720 0.2819 0.1972 -0.0026 0.0792 -0.0291 217 ALA A N 1382 C CA . ALA A 224 ? 0.3161 0.2731 0.2150 0.0207 0.0603 -0.0402 217 ALA A CA 1383 C C . ALA A 224 ? 0.2997 0.3249 0.2292 0.0085 0.0698 -0.0254 217 ALA A C 1384 O O . ALA A 224 ? 0.2929 0.3401 0.2454 0.0139 0.0425 -0.0032 217 ALA A O 1385 C CB . ALA A 224 ? 0.3506 0.2643 0.2578 0.0193 0.0597 -0.0499 217 ALA A CB 1386 N N . GLN A 225 ? 0.3082 0.2958 0.2560 0.0414 0.0836 -0.0154 218 GLN A N 1387 C CA . GLN A 225 ? 0.3123 0.3663 0.2617 0.0227 0.0753 -0.0394 218 GLN A CA 1388 C C . GLN A 225 ? 0.3469 0.3905 0.2546 0.0357 0.0415 -0.0137 218 GLN A C 1389 O O . GLN A 225 ? 0.3970 0.4015 0.2571 0.0741 0.0238 -0.0299 218 GLN A O 1390 C CB . GLN A 225 ? 0.3760 0.4297 0.2254 -0.0041 0.1050 -0.0566 218 GLN A CB 1391 C CG . GLN A 225 ? 0.4325 0.4855 0.2675 -0.0803 0.1144 -0.0381 218 GLN A CG 1392 C CD . GLN A 225 ? 0.4787 0.5325 0.2533 -0.0351 0.1431 -0.0647 218 GLN A CD 1393 O OE1 . GLN A 225 ? 0.4842 0.5696 0.3371 -0.0689 0.0671 0.0012 218 GLN A OE1 1394 N NE2 . GLN A 225 ? 0.5029 0.5756 0.4508 -0.0487 0.1784 -0.0477 218 GLN A NE2 1395 N N . LEU A 226 ? 0.4042 0.3541 0.2651 0.0426 0.0063 -0.0056 219 LEU A N 1396 C CA . LEU A 226 ? 0.4003 0.3457 0.2917 0.0529 0.0265 -0.0164 219 LEU A CA 1397 C C . LEU A 226 ? 0.4358 0.3614 0.2863 0.0379 0.0282 0.0320 219 LEU A C 1398 O O . LEU A 226 ? 0.4724 0.3555 0.2853 0.0540 0.0391 0.0441 219 LEU A O 1399 C CB . LEU A 226 ? 0.4674 0.3512 0.2242 0.0813 0.0140 0.0027 219 LEU A CB 1400 C CG . LEU A 226 ? 0.4312 0.4890 0.3397 0.0714 0.0158 -0.0325 219 LEU A CG 1401 C CD1 . LEU A 226 ? 0.6175 0.4568 0.4079 0.0358 -0.0331 -0.0557 219 LEU A CD1 1402 C CD2 . LEU A 226 ? 0.4237 0.6617 0.4518 0.1139 0.0405 0.0247 219 LEU A CD2 1403 N N . ALA A 227 ? 0.3893 0.3575 0.2784 0.0206 0.0466 0.0322 220 ALA A N 1404 C CA . ALA A 227 ? 0.4210 0.3649 0.2439 0.0413 0.0437 0.0102 220 ALA A CA 1405 C C . ALA A 227 ? 0.4143 0.4194 0.2568 0.0089 0.0651 -0.0050 220 ALA A C 1406 O O . ALA A 227 ? 0.4271 0.3985 0.2610 0.0115 0.0694 0.0126 220 ALA A O 1407 C CB . ALA A 227 ? 0.3118 0.3804 0.2823 0.0062 0.1071 -0.0164 220 ALA A CB 1408 N N . GLY A 228 ? 0.4117 0.3481 0.2167 0.0182 0.0356 -0.0009 221 GLY A N 1409 C CA . GLY A 228 ? 0.3923 0.3682 0.2496 0.0215 0.0334 -0.0238 221 GLY A CA 1410 C C . GLY A 228 ? 0.3833 0.3678 0.2450 0.0133 0.0503 -0.0155 221 GLY A C 1411 O O . GLY A 228 ? 0.4333 0.3989 0.2231 0.0301 0.0598 -0.0116 221 GLY A O 1412 N N . ALA A 229 ? 0.3833 0.3662 0.2480 0.0358 0.0465 -0.0299 222 ALA A N 1413 C CA . ALA A 229 ? 0.3824 0.3627 0.2540 0.0283 0.0565 -0.0341 222 ALA A CA 1414 C C . ALA A 229 ? 0.4172 0.3596 0.2396 0.0273 0.0400 -0.0569 222 ALA A C 1415 O O . ALA A 229 ? 0.3728 0.3945 0.2575 -0.0009 0.0467 0.0026 222 ALA A O 1416 C CB . ALA A 229 ? 0.3905 0.3377 0.2530 0.0275 0.0528 -0.0160 222 ALA A CB 1417 N N . LYS A 230 ? 0.4090 0.3636 0.1758 0.0274 0.0561 -0.0318 223 LYS A N 1418 C CA . LYS A 230 ? 0.3955 0.3617 0.2388 0.0295 0.0521 -0.0285 223 LYS A CA 1419 C C . LYS A 230 ? 0.3630 0.3553 0.2465 0.0219 0.0462 -0.0332 223 LYS A C 1420 O O . LYS A 230 ? 0.3471 0.3122 0.2862 0.0405 0.0518 -0.0430 223 LYS A O 1421 C CB . LYS A 230 ? 0.4401 0.4678 0.2612 -0.0178 0.0746 -0.0731 223 LYS A CB 1422 C CG . LYS A 230 ? 0.4764 0.4720 0.2576 0.0303 0.0535 -0.0651 223 LYS A CG 1423 C CD . LYS A 230 ? 0.5158 0.5711 0.2947 -0.0142 -0.0012 -0.0637 223 LYS A CD 1424 C CE . LYS A 230 ? 0.5789 0.5752 0.2566 -0.0014 -0.0033 -0.0833 223 LYS A CE 1425 N NZ . LYS A 230 ? 0.6168 0.6884 0.2167 0.0121 0.0712 -0.1585 223 LYS A NZ 1426 N N . GLY A 231 ? 0.3303 0.3269 0.2151 0.0590 0.0584 -0.0125 224 GLY A N 1427 C CA . GLY A 231 ? 0.3255 0.3458 0.2320 -0.0184 0.0106 -0.0083 224 GLY A CA 1428 C C . GLY A 231 ? 0.2809 0.3168 0.2231 0.0086 0.0427 -0.0239 224 GLY A C 1429 O O . GLY A 231 ? 0.3252 0.3513 0.2078 -0.0095 0.0745 -0.0158 224 GLY A O 1430 N N . VAL A 232 ? 0.3026 0.2855 0.2238 0.0362 0.0441 -0.0375 225 VAL A N 1431 C CA . VAL A 232 ? 0.2813 0.2603 0.2153 0.0330 0.0376 -0.0399 225 VAL A CA 1432 C C . VAL A 232 ? 0.3023 0.2719 0.2430 0.0312 0.0716 -0.0226 225 VAL A C 1433 O O . VAL A 232 ? 0.2907 0.2634 0.2742 0.0004 0.0378 -0.0309 225 VAL A O 1434 C CB . VAL A 232 ? 0.2755 0.2578 0.2323 0.0645 0.0414 -0.0369 225 VAL A CB 1435 C CG1 . VAL A 232 ? 0.2912 0.2935 0.2636 -0.0063 0.0359 -0.0417 225 VAL A CG1 1436 C CG2 . VAL A 232 ? 0.3579 0.2714 0.2318 0.0770 -0.0027 -0.0401 225 VAL A CG2 1437 N N . ILE A 233 ? 0.3137 0.2766 0.2611 0.0413 0.0282 -0.0539 226 ILE A N 1438 C CA . ILE A 233 ? 0.2993 0.2994 0.2512 0.0451 0.0416 -0.0518 226 ILE A CA 1439 C C . ILE A 233 ? 0.3038 0.2795 0.2473 0.0239 0.0501 -0.0503 226 ILE A C 1440 O O . ILE A 233 ? 0.3182 0.3119 0.2427 0.0018 0.0448 -0.0362 226 ILE A O 1441 C CB . ILE A 233 ? 0.3230 0.2660 0.2591 0.0537 0.0296 -0.0614 226 ILE A CB 1442 C CG1 . ILE A 233 ? 0.3390 0.2996 0.2056 0.0559 0.0513 -0.0722 226 ILE A CG1 1443 C CG2 . ILE A 233 ? 0.2856 0.2596 0.2699 0.0676 0.0804 -0.0440 226 ILE A CG2 1444 C CD1 . ILE A 233 ? 0.3547 0.3183 0.2513 0.0747 0.0717 -0.0899 226 ILE A CD1 1445 N N . LEU A 234 ? 0.2613 0.2709 0.2483 0.0364 0.0456 -0.0375 227 LEU A N 1446 C CA . LEU A 234 ? 0.2393 0.2349 0.2587 0.0598 0.0559 -0.0468 227 LEU A CA 1447 C C . LEU A 234 ? 0.2122 0.2414 0.2697 0.0411 0.0403 -0.0304 227 LEU A C 1448 O O . LEU A 234 ? 0.2530 0.2576 0.2831 0.0192 0.0345 -0.0345 227 LEU A O 1449 C CB . LEU A 234 ? 0.2226 0.2260 0.2524 0.0443 0.0621 -0.0308 227 LEU A CB 1450 C CG . LEU A 234 ? 0.2239 0.2076 0.2434 0.0341 0.0573 -0.0179 227 LEU A CG 1451 C CD1 . LEU A 234 ? 0.2503 0.2846 0.2880 0.0602 0.0864 -0.0187 227 LEU A CD1 1452 C CD2 . LEU A 234 ? 0.3002 0.1907 0.2872 0.0249 0.0458 -0.0242 227 LEU A CD2 1453 N N . TYR A 235 ? 0.2030 0.2495 0.2645 0.0332 0.0493 -0.0405 228 TYR A N 1454 C CA . TYR A 235 ? 0.2217 0.2385 0.2603 0.0395 0.0496 -0.0459 228 TYR A CA 1455 C C . TYR A 235 ? 0.2466 0.2611 0.2960 0.0219 0.0261 -0.0520 228 TYR A C 1456 O O . TYR A 235 ? 0.2172 0.2654 0.2833 0.0348 0.0296 -0.0491 228 TYR A O 1457 C CB . TYR A 235 ? 0.1774 0.2585 0.3028 0.0136 0.0819 -0.0389 228 TYR A CB 1458 C CG . TYR A 235 ? 0.1975 0.2415 0.2911 0.0020 0.0967 -0.0578 228 TYR A CG 1459 C CD1 . TYR A 235 ? 0.2235 0.2630 0.2977 -0.0255 0.0452 -0.0664 228 TYR A CD1 1460 C CD2 . TYR A 235 ? 0.2503 0.2392 0.3020 -0.0010 0.0807 -0.0631 228 TYR A CD2 1461 C CE1 . TYR A 235 ? 0.2544 0.2478 0.3141 -0.0370 0.0661 -0.0510 228 TYR A CE1 1462 C CE2 . TYR A 235 ? 0.2497 0.2901 0.2915 -0.0004 0.1113 -0.0774 228 TYR A CE2 1463 C CZ . TYR A 235 ? 0.2579 0.3123 0.2785 -0.0050 0.1118 -0.0344 228 TYR A CZ 1464 O OH . TYR A 235 ? 0.2514 0.3312 0.3196 -0.0107 0.1073 -0.0450 228 TYR A OH 1465 N N . SER A 236 ? 0.2111 0.2621 0.2652 0.0242 0.0730 -0.0408 229 SER A N 1466 C CA . SER A 236 ? 0.2206 0.2681 0.2756 0.0218 0.0562 -0.0184 229 SER A CA 1467 C C . SER A 236 ? 0.2190 0.2540 0.3224 0.0096 0.0540 -0.0469 229 SER A C 1468 O O . SER A 236 ? 0.2411 0.2773 0.3108 0.0278 0.0873 -0.0547 229 SER A O 1469 C CB . SER A 236 ? 0.2348 0.2401 0.2839 0.0157 0.0455 -0.0282 229 SER A CB 1470 O OG . SER A 236 ? 0.2622 0.2499 0.3515 0.0315 0.0684 -0.0094 229 SER A OG 1471 N N . ASP A 237 ? 0.1781 0.2700 0.3119 0.0031 0.0507 -0.0300 230 ASP A N 1472 C CA . ASP A 237 ? 0.1995 0.2984 0.3564 -0.0141 0.0800 -0.0333 230 ASP A CA 1473 C C . ASP A 237 ? 0.1931 0.2837 0.3690 -0.0026 0.0833 -0.0270 230 ASP A C 1474 O O . ASP A 237 ? 0.1784 0.3121 0.3637 0.0301 0.0787 -0.0218 230 ASP A O 1475 C CB . ASP A 237 ? 0.2193 0.2834 0.3343 0.0036 0.0879 -0.0487 230 ASP A CB 1476 C CG . ASP A 237 ? 0.2177 0.2910 0.3586 -0.0222 0.1002 -0.0277 230 ASP A CG 1477 O OD1 . ASP A 237 ? 0.2519 0.3641 0.3802 -0.0115 0.0649 -0.0079 230 ASP A OD1 1478 O OD2 . ASP A 237 ? 0.2408 0.3227 0.3560 -0.0120 0.1073 -0.0303 230 ASP A OD2 1479 N N . PRO A 238 ? 0.2334 0.2957 0.4031 0.0227 0.0775 -0.0606 231 PRO A N 1480 C CA . PRO A 238 ? 0.2438 0.2818 0.3932 0.0124 0.0663 -0.0500 231 PRO A CA 1481 C C . PRO A 238 ? 0.2796 0.3313 0.4066 -0.0331 0.0484 -0.0452 231 PRO A C 1482 O O . PRO A 238 ? 0.2091 0.3114 0.4089 0.0150 -0.0113 -0.0480 231 PRO A O 1483 C CB . PRO A 238 ? 0.3033 0.3055 0.3964 0.0292 0.0872 -0.0752 231 PRO A CB 1484 C CG . PRO A 238 ? 0.2867 0.3369 0.4511 0.0597 0.0001 -0.0583 231 PRO A CG 1485 C CD . PRO A 238 ? 0.2356 0.2942 0.4046 0.0634 0.0653 -0.0616 231 PRO A CD 1486 N N . ALA A 239 ? 0.2286 0.3162 0.4240 -0.0249 0.0818 -0.0556 232 ALA A N 1487 C CA . ALA A 239 ? 0.2419 0.2877 0.4564 -0.0136 0.0961 -0.0490 232 ALA A CA 1488 C C . ALA A 239 ? 0.2755 0.2955 0.4139 -0.0274 0.0579 -0.0840 232 ALA A C 1489 O O . ALA A 239 ? 0.2048 0.3639 0.4759 -0.0414 0.0149 -0.0815 232 ALA A O 1490 C CB . ALA A 239 ? 0.2635 0.3510 0.4138 -0.0288 0.0908 -0.0471 232 ALA A CB 1491 N N . ASP A 240 ? 0.2702 0.2612 0.4603 0.0470 0.0608 -0.0267 233 ASP A N 1492 C CA . ASP A 240 ? 0.2659 0.3041 0.4082 0.0106 0.0697 -0.0235 233 ASP A CA 1493 C C . ASP A 240 ? 0.2974 0.2947 0.3981 0.0104 0.0424 -0.0187 233 ASP A C 1494 O O . ASP A 240 ? 0.3528 0.3125 0.4513 0.0266 0.0636 -0.0607 233 ASP A O 1495 C CB . ASP A 240 ? 0.3003 0.2751 0.3870 0.0015 0.0473 -0.0229 233 ASP A CB 1496 C CG . ASP A 240 ? 0.2869 0.3185 0.3834 -0.0255 0.0423 -0.0166 233 ASP A CG 1497 O OD1 . ASP A 240 ? 0.2526 0.3042 0.4593 -0.0077 0.0360 -0.0271 233 ASP A OD1 1498 O OD2 . ASP A 240 ? 0.2400 0.2614 0.3788 -0.0340 0.0447 -0.0085 233 ASP A OD2 1499 N N . TYR A 241 ? 0.2276 0.2812 0.4128 0.0413 0.0242 -0.0134 234 TYR A N 1500 C CA . TYR A 241 ? 0.2005 0.2874 0.4166 0.0200 0.0461 -0.0223 234 TYR A CA 1501 C C . TYR A 241 ? 0.2084 0.2957 0.4650 0.0213 0.0438 -0.0117 234 TYR A C 1502 O O . TYR A 241 ? 0.2452 0.2848 0.3954 0.0410 -0.0088 0.0094 234 TYR A O 1503 C CB . TYR A 241 ? 0.2080 0.3287 0.3778 0.0473 0.0084 -0.0192 234 TYR A CB 1504 C CG . TYR A 241 ? 0.2244 0.2582 0.3458 0.0170 0.0374 -0.0638 234 TYR A CG 1505 C CD1 . TYR A 241 ? 0.2299 0.2587 0.3351 0.0101 0.0447 -0.0459 234 TYR A CD1 1506 C CD2 . TYR A 241 ? 0.2218 0.2538 0.3229 -0.0022 0.0303 -0.0877 234 TYR A CD2 1507 C CE1 . TYR A 241 ? 0.2247 0.2708 0.3272 0.0148 0.0072 -0.0791 234 TYR A CE1 1508 C CE2 . TYR A 241 ? 0.2859 0.2823 0.3305 0.0302 -0.0197 -0.0412 234 TYR A CE2 1509 C CZ . TYR A 241 ? 0.2472 0.2468 0.3550 0.0203 0.0428 -0.0334 234 TYR A CZ 1510 O OH . TYR A 241 ? 0.2760 0.2608 0.3461 0.0470 0.0244 -0.0103 234 TYR A OH 1511 N N . PHE A 242 ? 0.1874 0.3243 0.4351 0.0418 0.0161 -0.0169 235 PHE A N 1512 C CA . PHE A 242 ? 0.1838 0.3043 0.4346 0.0457 0.0524 -0.0417 235 PHE A CA 1513 C C . PHE A 242 ? 0.2168 0.3355 0.4649 0.0235 0.0258 -0.0221 235 PHE A C 1514 O O . PHE A 242 ? 0.2294 0.3669 0.4925 -0.0224 0.0467 -0.0464 235 PHE A O 1515 C CB . PHE A 242 ? 0.2741 0.3159 0.4558 0.0718 0.0438 -0.0567 235 PHE A CB 1516 C CG . PHE A 242 ? 0.2618 0.2937 0.4423 0.0459 0.0192 -0.0532 235 PHE A CG 1517 C CD1 . PHE A 242 ? 0.2360 0.3035 0.3879 0.0357 0.0677 -0.0710 235 PHE A CD1 1518 C CD2 . PHE A 242 ? 0.2504 0.3423 0.4538 0.0755 0.0657 -0.0361 235 PHE A CD2 1519 C CE1 . PHE A 242 ? 0.2320 0.3280 0.4350 0.0253 0.0176 -0.0610 235 PHE A CE1 1520 C CE2 . PHE A 242 ? 0.2843 0.3198 0.4515 0.0461 0.0507 -0.0282 235 PHE A CE2 1521 C CZ . PHE A 242 ? 0.2267 0.3775 0.4739 0.0178 0.0525 -0.0359 235 PHE A CZ 1522 N N . ALA A 243 ? 0.2245 0.3415 0.4531 0.0314 0.0404 -0.0518 236 ALA A N 1523 C CA . ALA A 243 ? 0.2608 0.3212 0.4731 0.0208 0.0247 -0.0682 236 ALA A CA 1524 C C . ALA A 243 ? 0.2644 0.3475 0.5303 0.0186 0.0329 -0.0778 236 ALA A C 1525 O O . ALA A 243 ? 0.2647 0.3422 0.5036 0.0330 0.0052 -0.0724 236 ALA A O 1526 C CB . ALA A 243 ? 0.2782 0.4026 0.4750 0.0341 0.0257 -0.0480 236 ALA A CB 1527 N N . PRO A 244 ? 0.2901 0.3926 0.6268 -0.0067 0.0296 -0.0712 237 PRO A N 1528 C CA . PRO A 244 ? 0.2901 0.3895 0.6437 0.0029 -0.0024 -0.0554 237 PRO A CA 1529 C C . PRO A 244 ? 0.2882 0.3901 0.6015 0.0130 0.0324 -0.0632 237 PRO A C 1530 O O . PRO A 244 ? 0.2884 0.4267 0.6025 -0.0122 -0.0081 -0.0965 237 PRO A O 1531 C CB . PRO A 244 ? 0.2958 0.4465 0.7300 -0.0182 0.0472 -0.0228 237 PRO A CB 1532 C CG . PRO A 244 ? 0.3380 0.4961 0.7510 -0.0092 0.0785 0.0236 237 PRO A CG 1533 C CD . PRO A 244 ? 0.2848 0.4039 0.6585 -0.0493 0.0057 0.0182 237 PRO A CD 1534 N N . GLY A 245 ? 0.2207 0.3764 0.6558 0.0049 0.0154 -0.0494 238 GLY A N 1535 C CA . GLY A 245 ? 0.2742 0.3723 0.6090 0.0334 -0.0077 -0.0822 238 GLY A CA 1536 C C . GLY A 245 ? 0.2894 0.4444 0.5970 0.0515 -0.0111 -0.0469 238 GLY A C 1537 O O . GLY A 245 ? 0.3345 0.5208 0.7010 0.0446 -0.1081 -0.0123 238 GLY A O 1538 N N . VAL A 246 ? 0.2639 0.3924 0.5983 0.0639 0.0281 -0.0779 239 VAL A N 1539 C CA . VAL A 246 ? 0.2268 0.3166 0.5415 0.0821 0.0122 -0.1236 239 VAL A CA 1540 C C . VAL A 246 ? 0.2130 0.3134 0.5233 0.0804 0.0150 -0.1044 239 VAL A C 1541 O O . VAL A 246 ? 0.2906 0.3399 0.5256 0.0382 -0.0283 -0.1276 239 VAL A O 1542 C CB . VAL A 246 ? 0.2395 0.3001 0.5108 0.0745 0.0230 -0.1093 239 VAL A CB 1543 C CG1 A VAL A 246 ? 0.3255 0.3303 0.5958 0.0761 0.0446 -0.0265 239 VAL A CG1 1544 C CG1 B VAL A 246 ? 0.1633 0.2962 0.4500 0.0540 -0.0418 -0.1468 239 VAL A CG1 1545 C CG2 A VAL A 246 ? 0.2611 0.2873 0.4826 0.0739 -0.0186 -0.0784 239 VAL A CG2 1546 C CG2 B VAL A 246 ? 0.2092 0.3193 0.4437 0.0474 0.0139 -0.0816 239 VAL A CG2 1547 N N . LYS A 247 ? 0.2698 0.3183 0.5211 0.0742 0.0716 -0.1323 240 LYS A N 1548 C CA . LYS A 247 ? 0.2187 0.3251 0.5632 0.0874 -0.0194 -0.1050 240 LYS A CA 1549 C C . LYS A 247 ? 0.2165 0.3563 0.5254 0.0828 0.0045 -0.0728 240 LYS A C 1550 O O . LYS A 247 ? 0.2022 0.3261 0.5285 0.0613 0.0157 -0.0780 240 LYS A O 1551 C CB . LYS A 247 ? 0.2322 0.4233 0.6372 0.0944 -0.0883 -0.0098 240 LYS A CB 1552 C CG . LYS A 247 ? 0.1965 0.4492 0.6488 0.0861 0.0468 -0.1162 240 LYS A CG 1553 C CD . LYS A 247 ? 0.3644 0.5731 0.6025 0.1080 -0.0057 -0.1128 240 LYS A CD 1554 C CE . LYS A 247 ? 0.3678 0.5214 0.6988 0.1011 -0.0141 -0.0789 240 LYS A CE 1555 N NZ . LYS A 247 ? 0.4913 0.4796 0.7577 0.1079 0.0295 -0.0007 240 LYS A NZ 1556 N N . SER A 248 ? 0.2441 0.3058 0.5448 0.0061 -0.0218 -0.0298 241 SER A N 1557 C CA . SER A 248 ? 0.2381 0.2943 0.5033 0.0205 -0.0208 -0.0420 241 SER A CA 1558 C C . SER A 248 ? 0.2523 0.3135 0.4352 0.0726 0.0144 -0.0701 241 SER A C 1559 O O . SER A 248 ? 0.2371 0.2893 0.4751 0.0541 0.0230 -0.0447 241 SER A O 1560 C CB . SER A 248 ? 0.3326 0.4546 0.4748 -0.0509 0.0321 -0.0353 241 SER A CB 1561 O OG . SER A 248 ? 0.3881 0.4918 0.5415 0.0121 0.0333 0.0465 241 SER A OG 1562 N N . TYR A 249 ? 0.2369 0.2572 0.4492 0.0276 0.0042 -0.0606 242 TYR A N 1563 C CA . TYR A 249 ? 0.2422 0.2411 0.4453 0.0644 0.0366 -0.0498 242 TYR A CA 1564 C C . TYR A 249 ? 0.2492 0.2712 0.4236 0.0316 0.0654 -0.0726 242 TYR A C 1565 O O . TYR A 249 ? 0.3022 0.3121 0.4451 0.0305 0.0179 -0.0558 242 TYR A O 1566 C CB . TYR A 249 ? 0.2387 0.2796 0.4094 0.0745 -0.0067 -0.0307 242 TYR A CB 1567 C CG . TYR A 249 ? 0.2337 0.2179 0.4202 0.1203 -0.0060 -0.0074 242 TYR A CG 1568 C CD1 . TYR A 249 ? 0.2822 0.2904 0.4071 0.0975 0.0633 -0.0438 242 TYR A CD1 1569 C CD2 . TYR A 249 ? 0.2579 0.3150 0.4628 0.0633 0.0039 -0.0424 242 TYR A CD2 1570 C CE1 . TYR A 249 ? 0.3726 0.2926 0.3787 0.0711 0.0370 -0.0260 242 TYR A CE1 1571 C CE2 . TYR A 249 ? 0.3228 0.2910 0.4352 0.1041 -0.0253 -0.0180 242 TYR A CE2 1572 C CZ . TYR A 249 ? 0.2476 0.3488 0.4104 0.0964 0.0931 -0.0622 242 TYR A CZ 1573 O OH . TYR A 249 ? 0.3913 0.3034 0.4335 0.0884 0.1077 -0.0271 242 TYR A OH 1574 N N . PRO A 250 ? 0.3324 0.2563 0.4449 0.0977 0.0292 -0.0819 243 PRO A N 1575 C CA . PRO A 250 ? 0.3289 0.2987 0.4444 0.0539 -0.0248 -0.0447 243 PRO A CA 1576 C C . PRO A 250 ? 0.3107 0.3220 0.4723 0.0756 -0.0102 -0.0560 243 PRO A C 1577 O O . PRO A 250 ? 0.3896 0.3198 0.4634 0.1376 -0.0939 -0.0736 243 PRO A O 1578 C CB . PRO A 250 ? 0.3432 0.2484 0.4345 0.0953 0.0191 -0.0761 243 PRO A CB 1579 C CG . PRO A 250 ? 0.4121 0.2589 0.4311 0.0772 0.0642 -0.0581 243 PRO A CG 1580 C CD . PRO A 250 ? 0.3974 0.2460 0.4164 0.0892 0.0206 -0.0691 243 PRO A CD 1581 N N . ASP A 251 ? 0.2674 0.2562 0.4966 0.0736 -0.0206 -0.0418 244 ASP A N 1582 C CA . ASP A 251 ? 0.3001 0.2973 0.5092 0.0918 -0.0393 -0.1084 244 ASP A CA 1583 C C . ASP A 251 ? 0.2730 0.3037 0.5240 0.0742 -0.0681 -0.0720 244 ASP A C 1584 O O . ASP A 251 ? 0.2790 0.3146 0.5186 0.0968 -0.0777 -0.1083 244 ASP A O 1585 C CB . ASP A 251 ? 0.2748 0.3474 0.5835 0.1167 -0.0247 -0.0952 244 ASP A CB 1586 C CG . ASP A 251 ? 0.5093 0.4001 0.5955 0.0339 0.0185 -0.1487 244 ASP A CG 1587 O OD1 . ASP A 251 ? 0.4453 0.3749 0.6697 0.1408 -0.0538 -0.0594 244 ASP A OD1 1588 O OD2 . ASP A 251 ? 0.7199 0.5087 0.6295 0.0558 0.1014 -0.1659 244 ASP A OD2 1589 N N . GLY A 252 ? 0.2945 0.2872 0.5147 0.0600 -0.1042 -0.0595 245 GLY A N 1590 C CA . GLY A 252 ? 0.2484 0.2887 0.4735 0.0883 -0.0583 -0.0781 245 GLY A CA 1591 C C . GLY A 252 ? 0.2554 0.2653 0.4732 0.0738 -0.0456 -0.0485 245 GLY A C 1592 O O . GLY A 252 ? 0.2915 0.2897 0.4844 0.0357 -0.0463 -0.0729 245 GLY A O 1593 N N . TRP A 253 ? 0.2564 0.2564 0.4212 0.0755 0.0044 -0.0471 246 TRP A N 1594 C CA . TRP A 253 ? 0.2144 0.2535 0.3579 0.0479 -0.0039 -0.0581 246 TRP A CA 1595 C C . TRP A 253 ? 0.2313 0.2773 0.3783 0.0373 0.0161 -0.0585 246 TRP A C 1596 O O . TRP A 253 ? 0.2166 0.2838 0.3385 0.0474 0.0462 -0.0511 246 TRP A O 1597 C CB . TRP A 253 ? 0.1889 0.2821 0.3853 0.0707 -0.0143 -0.0770 246 TRP A CB 1598 C CG . TRP A 253 ? 0.2353 0.3019 0.4306 0.0302 -0.0180 -0.0446 246 TRP A CG 1599 C CD1 . TRP A 253 ? 0.2351 0.3505 0.4372 0.0270 -0.0378 -0.0764 246 TRP A CD1 1600 C CD2 . TRP A 253 ? 0.2210 0.2811 0.4481 0.0604 0.0107 -0.0466 246 TRP A CD2 1601 N NE1 . TRP A 253 ? 0.2740 0.3318 0.4472 0.0077 -0.0341 -0.0350 246 TRP A NE1 1602 C CE2 . TRP A 253 ? 0.2634 0.3080 0.4533 0.0412 -0.0113 -0.0531 246 TRP A CE2 1603 C CE3 . TRP A 253 ? 0.2391 0.3240 0.4406 0.0403 -0.0269 -0.0239 246 TRP A CE3 1604 C CZ2 . TRP A 253 ? 0.2761 0.2901 0.4443 0.0432 -0.0177 -0.0665 246 TRP A CZ2 1605 C CZ3 . TRP A 253 ? 0.2146 0.3376 0.4922 0.0149 -0.0286 -0.0462 246 TRP A CZ3 1606 C CH2 . TRP A 253 ? 0.2120 0.3540 0.4255 0.0974 -0.0497 -0.1169 246 TRP A CH2 1607 N N . ASN A 254 ? 0.2025 0.2807 0.3695 0.0362 0.0040 -0.0684 247 ASN A N 1608 C CA . ASN A 254 ? 0.2057 0.3443 0.3700 -0.0081 0.0042 -0.0564 247 ASN A CA 1609 C C . ASN A 254 ? 0.2441 0.2334 0.3849 0.0223 -0.0146 -0.0896 247 ASN A C 1610 O O . ASN A 254 ? 0.2685 0.3332 0.3706 0.0139 0.0081 0.0327 247 ASN A O 1611 C CB . ASN A 254 ? 0.2011 0.3224 0.4400 0.0071 0.0207 -0.0820 247 ASN A CB 1612 C CG . ASN A 254 ? 0.2200 0.2771 0.4214 0.0280 0.0138 -0.0638 247 ASN A CG 1613 O OD1 . ASN A 254 ? 0.2281 0.2736 0.4275 0.0515 0.0161 -0.0284 247 ASN A OD1 1614 N ND2 . ASN A 254 ? 0.2002 0.3141 0.4006 0.0369 -0.0394 -0.0467 247 ASN A ND2 1615 N N . LEU A 255 ? 0.2245 0.2973 0.3525 0.0581 0.0189 -0.0673 248 LEU A N 1616 C CA . LEU A 255 ? 0.2117 0.2335 0.3514 0.0495 0.0225 -0.0545 248 LEU A CA 1617 C C . LEU A 255 ? 0.2727 0.2487 0.3734 0.0313 0.0485 -0.0655 248 LEU A C 1618 O O . LEU A 255 ? 0.2395 0.2802 0.3892 0.0370 0.0381 -0.0533 248 LEU A O 1619 C CB . LEU A 255 ? 0.1888 0.2456 0.3483 0.0578 0.0337 -0.0404 248 LEU A CB 1620 C CG . LEU A 255 ? 0.2676 0.2583 0.3346 0.0286 0.0130 -0.0144 248 LEU A CG 1621 C CD1 . LEU A 255 ? 0.1996 0.2348 0.3189 0.0306 -0.0242 -0.0704 248 LEU A CD1 1622 C CD2 . LEU A 255 ? 0.3526 0.2447 0.3655 0.0784 -0.0172 -0.0319 248 LEU A CD2 1623 N N . PRO A 256 ? 0.2601 0.2463 0.3287 0.0253 0.0295 -0.0574 249 PRO A N 1624 C CA . PRO A 256 ? 0.2441 0.2182 0.3601 0.0480 0.0461 -0.0490 249 PRO A CA 1625 C C . PRO A 256 ? 0.2458 0.2079 0.3390 0.0231 0.0599 -0.0519 249 PRO A C 1626 O O . PRO A 256 ? 0.2092 0.2375 0.3528 0.0128 0.0407 -0.0850 249 PRO A O 1627 C CB . PRO A 256 ? 0.2633 0.2372 0.3387 0.0147 0.0689 -0.0545 249 PRO A CB 1628 C CG . PRO A 256 ? 0.2044 0.2450 0.4018 0.0354 0.0792 -0.0687 249 PRO A CG 1629 C CD . PRO A 256 ? 0.2408 0.2175 0.3658 0.0412 0.0509 -0.0321 249 PRO A CD 1630 N N . GLY A 257 ? 0.2447 0.2499 0.3316 0.0262 0.0500 -0.0611 250 GLY A N 1631 C CA . GLY A 257 ? 0.2432 0.3154 0.3321 0.0135 0.0644 -0.0488 250 GLY A CA 1632 C C . GLY A 257 ? 0.2463 0.2574 0.3214 0.0317 0.0391 -0.0549 250 GLY A C 1633 O O . GLY A 257 ? 0.2663 0.2599 0.3391 0.0145 0.0490 -0.0259 250 GLY A O 1634 N N . GLY A 258 ? 0.2180 0.2798 0.3010 0.0240 0.0645 -0.0680 251 GLY A N 1635 C CA . GLY A 258 ? 0.2278 0.2789 0.3013 0.0423 0.0347 -0.0741 251 GLY A CA 1636 C C . GLY A 258 ? 0.2329 0.2508 0.2744 0.0356 0.0356 -0.0638 251 GLY A C 1637 O O . GLY A 258 ? 0.2359 0.2705 0.2911 0.0513 0.0479 -0.0632 251 GLY A O 1638 N N . GLY A 259 ? 0.2636 0.2166 0.2982 0.0594 0.0420 -0.0715 252 GLY A N 1639 C CA . GLY A 259 ? 0.1883 0.2256 0.2837 0.0302 0.0532 -0.0520 252 GLY A CA 1640 C C . GLY A 259 ? 0.2042 0.2264 0.3015 0.0402 0.0545 -0.0666 252 GLY A C 1641 O O . GLY A 259 ? 0.2486 0.2340 0.3008 0.0346 0.0505 -0.0565 252 GLY A O 1642 N N . VAL A 260 ? 0.2006 0.2065 0.2970 0.0557 0.0512 -0.0664 253 VAL A N 1643 C CA . VAL A 260 ? 0.1994 0.1989 0.2934 0.0538 0.0445 -0.0678 253 VAL A CA 1644 C C . VAL A 260 ? 0.2366 0.1889 0.2799 0.0257 0.0663 -0.0562 253 VAL A C 1645 O O . VAL A 260 ? 0.2370 0.2289 0.2972 0.0222 0.0449 -0.0265 253 VAL A O 1646 C CB . VAL A 260 ? 0.1981 0.1760 0.2787 0.0742 0.0395 -0.0577 253 VAL A CB 1647 C CG1 . VAL A 260 ? 0.1917 0.2155 0.3051 0.0392 0.0269 -0.0108 253 VAL A CG1 1648 C CG2 . VAL A 260 ? 0.2356 0.2136 0.2576 0.0427 0.0757 -0.0725 253 VAL A CG2 1649 N N . GLN A 261 ? 0.2064 0.1670 0.2779 0.0251 0.0192 -0.0761 254 GLN A N 1650 C CA . GLN A 261 ? 0.1833 0.1796 0.2569 0.0007 0.0380 -0.0658 254 GLN A CA 1651 C C . GLN A 261 ? 0.1967 0.2263 0.2568 0.0171 0.0411 -0.0382 254 GLN A C 1652 O O . GLN A 261 ? 0.2565 0.2216 0.2636 0.0126 0.0417 -0.0445 254 GLN A O 1653 C CB . GLN A 261 ? 0.2299 0.1764 0.2505 -0.0080 0.0317 -0.0739 254 GLN A CB 1654 C CG . GLN A 261 ? 0.1852 0.1606 0.2655 0.0113 0.0255 -0.0553 254 GLN A CG 1655 C CD . GLN A 261 ? 0.2009 0.1941 0.2046 -0.0052 0.0204 -0.0328 254 GLN A CD 1656 O OE1 . GLN A 261 ? 0.1961 0.2477 0.2488 0.0223 0.0043 -0.0332 254 GLN A OE1 1657 N NE2 . GLN A 261 ? 0.1925 0.2522 0.2686 0.0347 0.0217 -0.0374 254 GLN A NE2 1658 N N . ARG A 262 ? 0.1900 0.2255 0.2530 0.0034 0.0362 -0.0617 255 ARG A N 1659 C CA . ARG A 262 ? 0.1957 0.1914 0.2680 0.0049 0.0345 -0.0493 255 ARG A CA 1660 C C . ARG A 262 ? 0.1931 0.1992 0.2704 0.0243 0.0342 -0.0579 255 ARG A C 1661 O O . ARG A 262 ? 0.1781 0.2089 0.2423 0.0213 0.0224 -0.0403 255 ARG A O 1662 C CB . ARG A 262 ? 0.2132 0.1684 0.2938 0.0151 0.0591 -0.0475 255 ARG A CB 1663 C CG . ARG A 262 ? 0.2322 0.1701 0.2617 0.0225 0.0397 -0.0459 255 ARG A CG 1664 C CD . ARG A 262 ? 0.2344 0.1630 0.2387 0.0209 0.0448 -0.0517 255 ARG A CD 1665 N NE . ARG A 262 ? 0.2147 0.1700 0.2952 0.0488 0.0173 -0.0553 255 ARG A NE 1666 C CZ . ARG A 262 ? 0.1861 0.1879 0.3057 0.0212 0.0220 -0.0462 255 ARG A CZ 1667 N NH1 . ARG A 262 ? 0.1958 0.2169 0.3256 0.0119 -0.0290 -0.0093 255 ARG A NH1 1668 N NH2 . ARG A 262 ? 0.2425 0.1964 0.2689 0.0062 -0.0089 -0.0557 255 ARG A NH2 1669 N N . GLY A 263 ? 0.2118 0.1856 0.2414 0.0237 0.0313 -0.0475 256 GLY A N 1670 C CA . GLY A 263 ? 0.1904 0.1839 0.2246 0.0361 0.0014 -0.0456 256 GLY A CA 1671 C C . GLY A 263 ? 0.1895 0.2092 0.2121 0.0212 0.0095 -0.0482 256 GLY A C 1672 O O . GLY A 263 ? 0.1904 0.2076 0.2053 0.0099 0.0316 -0.0435 256 GLY A O 1673 N N . ASN A 264 ? 0.1576 0.1981 0.2347 0.0254 0.0167 -0.0166 257 ASN A N 1674 C CA . ASN A 264 ? 0.1688 0.2127 0.1957 0.0331 0.0270 -0.0085 257 ASN A CA 1675 C C . ASN A 264 ? 0.1696 0.1992 0.1995 0.0181 0.0179 -0.0298 257 ASN A C 1676 O O . ASN A 264 ? 0.1797 0.1949 0.2328 0.0000 0.0294 -0.0190 257 ASN A O 1677 C CB . ASN A 264 ? 0.1801 0.1692 0.2103 0.0106 0.0369 -0.0523 257 ASN A CB 1678 C CG . ASN A 264 ? 0.1889 0.1725 0.1830 0.0027 -0.0036 -0.0379 257 ASN A CG 1679 O OD1 . ASN A 264 ? 0.1914 0.2024 0.2074 0.0107 0.0234 -0.0120 257 ASN A OD1 1680 N ND2 . ASN A 264 ? 0.1900 0.2545 0.1844 0.0226 0.0058 -0.0310 257 ASN A ND2 1681 N N . ILE A 265 ? 0.1807 0.2037 0.1819 0.0116 0.0283 -0.0097 258 ILE A N 1682 C CA . ILE A 265 ? 0.2152 0.2084 0.1855 0.0124 0.0415 -0.0043 258 ILE A CA 1683 C C . ILE A 265 ? 0.1947 0.2140 0.1858 0.0050 0.0463 -0.0156 258 ILE A C 1684 O O . ILE A 265 ? 0.2313 0.2416 0.2099 0.0355 0.0389 0.0038 258 ILE A O 1685 C CB . ILE A 265 ? 0.2090 0.2194 0.2034 0.0156 -0.0079 -0.0470 258 ILE A CB 1686 C CG1 . ILE A 265 ? 0.2254 0.2214 0.1707 -0.0294 0.0043 -0.0309 258 ILE A CG1 1687 C CG2 . ILE A 265 ? 0.2128 0.2312 0.2068 0.0332 0.0172 -0.0154 258 ILE A CG2 1688 C CD1 . ILE A 265 ? 0.2565 0.3194 0.2098 0.0237 0.0518 -0.0789 258 ILE A CD1 1689 N N . LEU A 266 ? 0.1906 0.1955 0.2096 0.0292 0.0542 -0.0299 259 LEU A N 1690 C CA . LEU A 266 ? 0.1934 0.1731 0.2003 0.0183 0.0408 -0.0050 259 LEU A CA 1691 C C . LEU A 266 ? 0.2014 0.1917 0.2248 0.0025 0.0099 -0.0010 259 LEU A C 1692 O O . LEU A 266 ? 0.2002 0.2188 0.2179 0.0268 0.0131 -0.0155 259 LEU A O 1693 C CB . LEU A 266 ? 0.1937 0.2004 0.2142 -0.0039 0.0480 -0.0083 259 LEU A CB 1694 C CG . LEU A 266 ? 0.2210 0.1809 0.1727 0.0062 0.0323 -0.0101 259 LEU A CG 1695 C CD1 . LEU A 266 ? 0.1653 0.2632 0.2232 0.0062 0.0642 -0.0083 259 LEU A CD1 1696 C CD2 . LEU A 266 ? 0.2200 0.2727 0.2370 0.0001 -0.0094 -0.0273 259 LEU A CD2 1697 N N . ASN A 267 ? 0.2140 0.1647 0.2295 0.0076 0.0352 -0.0082 260 ASN A N 1698 C CA . ASN A 267 ? 0.2253 0.1710 0.1697 -0.0035 0.0417 -0.0126 260 ASN A CA 1699 C C . ASN A 267 ? 0.2156 0.2030 0.1867 0.0099 0.0316 0.0102 260 ASN A C 1700 O O . ASN A 267 ? 0.2138 0.2124 0.2105 0.0122 0.0269 0.0078 260 ASN A O 1701 C CB . ASN A 267 ? 0.2350 0.2269 0.1983 -0.0077 0.0668 -0.0008 260 ASN A CB 1702 C CG . ASN A 267 ? 0.2306 0.2499 0.1923 -0.0036 0.0598 -0.0102 260 ASN A CG 1703 O OD1 . ASN A 267 ? 0.2830 0.2793 0.2260 -0.0079 0.0187 -0.0257 260 ASN A OD1 1704 N ND2 . ASN A 267 ? 0.2800 0.2723 0.1617 0.0154 0.0583 -0.0133 260 ASN A ND2 1705 N N . LEU A 268 ? 0.1998 0.1986 0.1535 -0.0215 0.0195 -0.0248 261 LEU A N 1706 C CA . LEU A 268 ? 0.2166 0.1885 0.1635 -0.0168 0.0253 -0.0056 261 LEU A CA 1707 C C . LEU A 268 ? 0.2003 0.1921 0.1900 -0.0098 0.0202 -0.0032 261 LEU A C 1708 O O . LEU A 268 ? 0.1807 0.2014 0.1858 -0.0030 -0.0065 -0.0119 261 LEU A O 1709 C CB . LEU A 268 ? 0.2243 0.1740 0.1834 -0.0399 0.0056 0.0089 261 LEU A CB 1710 C CG . LEU A 268 ? 0.2096 0.1689 0.1865 -0.0265 0.0016 0.0000 261 LEU A CG 1711 C CD1 . LEU A 268 ? 0.2397 0.1875 0.1807 -0.0009 0.0115 0.0031 261 LEU A CD1 1712 C CD2 . LEU A 268 ? 0.1918 0.2304 0.2414 -0.0408 0.0088 0.0010 261 LEU A CD2 1713 N N . ASN A 269 ? 0.1759 0.1900 0.1724 0.0047 0.0032 -0.0101 262 ASN A N 1714 C CA . ASN A 269 ? 0.2175 0.1860 0.1483 -0.0081 0.0130 0.0017 262 ASN A CA 1715 C C . ASN A 269 ? 0.1823 0.1880 0.1729 -0.0080 0.0175 0.0074 262 ASN A C 1716 O O . ASN A 269 ? 0.2259 0.1975 0.1845 -0.0132 0.0074 0.0039 262 ASN A O 1717 C CB . ASN A 269 ? 0.2310 0.2067 0.1837 -0.0084 0.0144 0.0230 262 ASN A CB 1718 C CG . ASN A 269 ? 0.2586 0.2608 0.1888 0.0049 0.0275 -0.0011 262 ASN A CG 1719 O OD1 . ASN A 269 ? 0.2504 0.2891 0.2392 -0.0105 0.0375 0.0174 262 ASN A OD1 1720 N ND2 . ASN A 269 ? 0.3144 0.2856 0.1548 -0.0101 0.0341 -0.0063 262 ASN A ND2 1721 N N . GLY A 270 ? 0.1747 0.1935 0.1360 -0.0109 0.0105 0.0144 263 GLY A N 1722 C CA . GLY A 270 ? 0.1544 0.1946 0.1717 -0.0059 0.0302 -0.0035 263 GLY A CA 1723 C C . GLY A 270 ? 0.1666 0.2148 0.1562 -0.0143 -0.0044 -0.0156 263 GLY A C 1724 O O . GLY A 270 ? 0.1946 0.2217 0.1857 -0.0248 0.0199 -0.0234 263 GLY A O 1725 N N . ALA A 271 ? 0.1611 0.1779 0.1754 -0.0165 -0.0152 -0.0221 264 ALA A N 1726 C CA . ALA A 271 ? 0.1677 0.2003 0.1436 -0.0133 -0.0135 0.0005 264 ALA A CA 1727 C C . ALA A 271 ? 0.1862 0.1937 0.1766 0.0011 0.0012 0.0019 264 ALA A C 1728 O O . ALA A 271 ? 0.1950 0.2224 0.1931 -0.0048 0.0148 -0.0084 264 ALA A O 1729 C CB . ALA A 271 ? 0.1595 0.2115 0.1319 -0.0171 -0.0038 -0.0188 264 ALA A CB 1730 N N . GLY A 272 ? 0.2010 0.1729 0.1438 0.0091 0.0096 -0.0187 265 GLY A N 1731 C CA . GLY A 272 ? 0.2029 0.1706 0.1709 -0.0102 -0.0060 -0.0159 265 GLY A CA 1732 C C . GLY A 272 ? 0.1762 0.1878 0.1789 -0.0085 -0.0101 -0.0110 265 GLY A C 1733 O O . GLY A 272 ? 0.1790 0.2161 0.1933 -0.0204 0.0024 -0.0174 265 GLY A O 1734 N N . ASP A 273 ? 0.1762 0.1678 0.1605 -0.0040 -0.0172 -0.0141 266 ASP A N 1735 C CA . ASP A 273 ? 0.1828 0.1897 0.1778 -0.0283 -0.0096 -0.0192 266 ASP A CA 1736 C C . ASP A 273 ? 0.2011 0.2004 0.1808 -0.0024 0.0139 -0.0195 266 ASP A C 1737 O O . ASP A 273 ? 0.2058 0.2006 0.1934 0.0065 -0.0068 -0.0003 266 ASP A O 1738 C CB . ASP A 273 ? 0.1447 0.2197 0.2182 -0.0166 -0.0024 -0.0521 266 ASP A CB 1739 C CG . ASP A 273 ? 0.1840 0.2063 0.1896 -0.0288 -0.0048 -0.0262 266 ASP A CG 1740 O OD1 . ASP A 273 ? 0.1881 0.2149 0.2461 -0.0083 0.0374 -0.0165 266 ASP A OD1 1741 O OD2 . ASP A 273 ? 0.1922 0.2262 0.2269 -0.0005 -0.0040 -0.0218 266 ASP A OD2 1742 N N . PRO A 274 ? 0.1881 0.2189 0.1792 0.0054 -0.0045 -0.0264 267 PRO A N 1743 C CA . PRO A 274 ? 0.2157 0.2426 0.1878 0.0122 0.0135 -0.0170 267 PRO A CA 1744 C C . PRO A 274 ? 0.2057 0.2228 0.2028 -0.0133 0.0112 -0.0194 267 PRO A C 1745 O O . PRO A 274 ? 0.1988 0.2396 0.2221 -0.0186 0.0132 0.0028 267 PRO A O 1746 C CB . PRO A 274 ? 0.2057 0.2289 0.2083 0.0134 -0.0056 -0.0334 267 PRO A CB 1747 C CG . PRO A 274 ? 0.2713 0.2512 0.1861 0.0407 0.0126 0.0080 267 PRO A CG 1748 C CD . PRO A 274 ? 0.2268 0.2134 0.2016 0.0149 0.0417 -0.0321 267 PRO A CD 1749 N N . LEU A 275 ? 0.2114 0.2353 0.1740 -0.0207 0.0091 -0.0232 268 LEU A N 1750 C CA . LEU A 275 ? 0.2041 0.1872 0.2348 -0.0143 0.0171 -0.0449 268 LEU A CA 1751 C C . LEU A 275 ? 0.1796 0.1899 0.1974 -0.0045 -0.0014 -0.0421 268 LEU A C 1752 O O . LEU A 275 ? 0.1890 0.2170 0.1840 -0.0121 0.0026 -0.0245 268 LEU A O 1753 C CB . LEU A 275 ? 0.1885 0.1841 0.2194 -0.0121 -0.0074 -0.0671 268 LEU A CB 1754 C CG . LEU A 275 ? 0.2203 0.2248 0.1977 0.0016 0.0347 -0.0528 268 LEU A CG 1755 C CD1 . LEU A 275 ? 0.2638 0.2556 0.2690 -0.0310 -0.0253 -0.0486 268 LEU A CD1 1756 C CD2 . LEU A 275 ? 0.2286 0.2883 0.2069 0.0078 0.0372 -0.0314 268 LEU A CD2 1757 N N . THR A 276 ? 0.1730 0.1783 0.1581 -0.0081 0.0277 -0.0165 269 THR A N 1758 C CA . THR A 276 ? 0.1940 0.1806 0.1636 -0.0133 0.0268 -0.0318 269 THR A CA 1759 C C . THR A 276 ? 0.1589 0.1865 0.1668 -0.0094 -0.0049 -0.0061 269 THR A C 1760 O O . THR A 276 ? 0.2024 0.2152 0.1694 -0.0110 0.0072 -0.0216 269 THR A O 1761 C CB . THR A 276 ? 0.1868 0.1923 0.1815 -0.0507 -0.0190 -0.0070 269 THR A CB 1762 O OG1 . THR A 276 ? 0.2018 0.2309 0.1836 -0.0065 0.0026 -0.0068 269 THR A OG1 1763 C CG2 . THR A 276 ? 0.1283 0.2084 0.1781 -0.0225 -0.0115 -0.0286 269 THR A CG2 1764 N N . PRO A 277 ? 0.1997 0.1969 0.1587 -0.0172 0.0070 -0.0114 270 PRO A N 1765 C CA . PRO A 277 ? 0.2157 0.1816 0.1554 -0.0301 0.0211 -0.0021 270 PRO A CA 1766 C C . PRO A 277 ? 0.1989 0.2194 0.1851 -0.0089 0.0070 -0.0095 270 PRO A C 1767 O O . PRO A 277 ? 0.2049 0.2369 0.2184 0.0036 0.0059 -0.0086 270 PRO A O 1768 C CB . PRO A 277 ? 0.1853 0.2183 0.1301 -0.0072 0.0079 0.0121 270 PRO A CB 1769 C CG . PRO A 277 ? 0.2159 0.1952 0.1570 -0.0325 0.0047 -0.0232 270 PRO A CG 1770 C CD . PRO A 277 ? 0.2289 0.2027 0.1656 -0.0147 0.0058 0.0018 270 PRO A CD 1771 N N . GLY A 278 ? 0.1883 0.1959 0.1752 -0.0094 0.0120 -0.0181 271 GLY A N 1772 C CA . GLY A 278 ? 0.2132 0.1758 0.2058 -0.0055 0.0281 -0.0182 271 GLY A CA 1773 C C . GLY A 278 ? 0.2112 0.1936 0.1937 -0.0042 0.0198 -0.0211 271 GLY A C 1774 O O . GLY A 278 ? 0.2251 0.2170 0.1964 -0.0252 0.0376 -0.0301 271 GLY A O 1775 N N . TYR A 279 ? 0.1912 0.1827 0.2091 -0.0061 0.0123 -0.0061 272 TYR A N 1776 C CA . TYR A 279 ? 0.1899 0.1819 0.2099 -0.0034 0.0020 0.0056 272 TYR A CA 1777 C C . TYR A 279 ? 0.2048 0.1779 0.1972 0.0102 0.0227 -0.0033 272 TYR A C 1778 O O . TYR A 279 ? 0.1873 0.2005 0.1820 0.0030 0.0001 -0.0209 272 TYR A O 1779 C CB . TYR A 279 ? 0.1783 0.1860 0.2025 0.0169 0.0127 0.0040 272 TYR A CB 1780 C CG . TYR A 279 ? 0.1958 0.1938 0.1874 0.0106 0.0090 0.0050 272 TYR A CG 1781 C CD1 . TYR A 279 ? 0.1758 0.1807 0.2458 0.0195 0.0011 -0.0088 272 TYR A CD1 1782 C CD2 . TYR A 279 ? 0.2036 0.2131 0.1950 0.0047 0.0217 0.0055 272 TYR A CD2 1783 C CE1 . TYR A 279 ? 0.1706 0.1931 0.2111 0.0168 0.0077 0.0172 272 TYR A CE1 1784 C CE2 . TYR A 279 ? 0.1904 0.2060 0.2291 0.0407 0.0214 -0.0220 272 TYR A CE2 1785 C CZ . TYR A 279 ? 0.1980 0.2120 0.1770 0.0234 0.0122 -0.0199 272 TYR A CZ 1786 O OH . TYR A 279 ? 0.2253 0.2164 0.1960 0.0301 0.0238 -0.0239 272 TYR A OH 1787 N N . PRO A 280 ? 0.2063 0.1977 0.1787 0.0239 0.0092 -0.0116 273 PRO A N 1788 C CA . PRO A 280 ? 0.2346 0.1839 0.2010 0.0022 0.0195 -0.0034 273 PRO A CA 1789 C C . PRO A 280 ? 0.1918 0.1889 0.2341 0.0119 0.0168 -0.0113 273 PRO A C 1790 O O . PRO A 280 ? 0.1923 0.1990 0.2391 -0.0172 0.0181 -0.0280 273 PRO A O 1791 C CB . PRO A 280 ? 0.1721 0.2118 0.2005 0.0295 0.0320 -0.0082 273 PRO A CB 1792 C CG . PRO A 280 ? 0.2136 0.1396 0.2433 0.0213 0.0308 0.0133 273 PRO A CG 1793 C CD . PRO A 280 ? 0.1924 0.1694 0.1882 0.0120 0.0367 0.0079 273 PRO A CD 1794 N N . ALA A 281 ? 0.2033 0.1603 0.1870 -0.0076 0.0304 -0.0096 274 ALA A N 1795 C CA . ALA A 281 ? 0.1715 0.1897 0.2030 -0.0041 0.0432 -0.0303 274 ALA A CA 1796 C C . ALA A 281 ? 0.1909 0.2096 0.2354 -0.0038 0.0343 -0.0049 274 ALA A C 1797 O O . ALA A 281 ? 0.2221 0.2191 0.2689 -0.0051 0.0182 -0.0099 274 ALA A O 1798 C CB . ALA A 281 ? 0.1726 0.2272 0.2117 0.0017 0.0533 -0.0429 274 ALA A CB 1799 N N . ASN A 282 ? 0.1767 0.2145 0.2413 0.0034 0.0290 -0.0131 275 ASN A N 1800 C CA . ASN A 282 ? 0.1862 0.2393 0.2940 -0.0082 0.0493 -0.0042 275 ASN A CA 1801 C C . ASN A 282 ? 0.2182 0.2452 0.3369 -0.0166 0.0276 -0.0121 275 ASN A C 1802 O O . ASN A 282 ? 0.1810 0.2332 0.3355 -0.0121 0.0068 -0.0171 275 ASN A O 1803 C CB . ASN A 282 ? 0.2094 0.2508 0.3285 -0.0184 0.0552 -0.0316 275 ASN A CB 1804 C CG . ASN A 282 ? 0.2499 0.2714 0.3198 -0.0139 0.0406 -0.0279 275 ASN A CG 1805 O OD1 . ASN A 282 ? 0.2201 0.2466 0.3257 0.0037 0.0404 -0.0433 275 ASN A OD1 1806 N ND2 . ASN A 282 ? 0.2477 0.3012 0.3756 -0.0713 0.0452 -0.0785 275 ASN A ND2 1807 N N A GLU A 283 ? 0.1904 0.2752 0.3597 -0.0023 0.0051 0.0191 276 GLU A N 1808 N N B GLU A 283 ? 0.1918 0.2817 0.3585 -0.0024 0.0074 0.0201 276 GLU A N 1809 C CA A GLU A 283 ? 0.2199 0.2702 0.4033 -0.0328 0.0206 0.0165 276 GLU A CA 1810 C CA B GLU A 283 ? 0.2152 0.2893 0.4093 -0.0368 0.0231 0.0159 276 GLU A CA 1811 C C A GLU A 283 ? 0.2664 0.2713 0.3908 -0.0268 0.0022 0.0024 276 GLU A C 1812 C C B GLU A 283 ? 0.2503 0.2578 0.3794 -0.0270 0.0422 -0.0040 276 GLU A C 1813 O O A GLU A 283 ? 0.2143 0.3137 0.3907 0.0150 0.0052 -0.0432 276 GLU A O 1814 O O B GLU A 283 ? 0.2861 0.3042 0.3840 -0.0245 0.0880 -0.0336 276 GLU A O 1815 C CB A GLU A 283 ? 0.3096 0.2521 0.4220 -0.0502 0.0520 0.0174 276 GLU A CB 1816 C CB B GLU A 283 ? 0.2440 0.3465 0.4034 -0.0487 0.0310 0.0389 276 GLU A CB 1817 C CG A GLU A 283 ? 0.3426 0.3666 0.4548 -0.0134 -0.0257 -0.0516 276 GLU A CG 1818 C CG B GLU A 283 ? 0.3415 0.3560 0.4978 -0.0137 0.0061 -0.0912 276 GLU A CG 1819 C CD A GLU A 283 ? 0.3585 0.3278 0.4329 -0.0329 0.0232 -0.0317 276 GLU A CD 1820 C CD B GLU A 283 ? 0.2888 0.4537 0.5077 -0.0247 -0.0021 -0.0995 276 GLU A CD 1821 O OE1 A GLU A 283 ? 0.2913 0.4683 0.5198 -0.0184 -0.0044 0.0020 276 GLU A OE1 1822 O OE1 B GLU A 283 ? 0.2248 0.4534 0.5386 -0.0240 0.0233 -0.0945 276 GLU A OE1 1823 O OE2 A GLU A 283 ? 0.2997 0.4037 0.4605 -0.0998 -0.0845 -0.0834 276 GLU A OE2 1824 O OE2 B GLU A 283 ? 0.2417 0.5558 0.5477 -0.0940 0.0078 -0.1327 276 GLU A OE2 1825 N N . TYR A 284 ? 0.1839 0.2732 0.3960 0.0154 0.0356 -0.0002 277 TYR A N 1826 C CA . TYR A 284 ? 0.2174 0.2846 0.3753 -0.0035 0.0151 0.0065 277 TYR A CA 1827 C C . TYR A 284 ? 0.2272 0.2693 0.3482 -0.0117 -0.0035 -0.0132 277 TYR A C 1828 O O . TYR A 284 ? 0.2466 0.3133 0.3769 -0.0118 -0.0082 0.0074 277 TYR A O 1829 C CB . TYR A 284 ? 0.2418 0.2779 0.3577 0.0060 -0.0014 -0.0379 277 TYR A CB 1830 C CG . TYR A 284 ? 0.2539 0.2501 0.3754 -0.0311 0.0252 -0.0355 277 TYR A CG 1831 C CD1 . TYR A 284 ? 0.2688 0.2597 0.4012 -0.0332 0.0388 -0.0264 277 TYR A CD1 1832 C CD2 . TYR A 284 ? 0.2171 0.2891 0.3872 -0.0059 0.0286 -0.0401 277 TYR A CD2 1833 C CE1 . TYR A 284 ? 0.3041 0.2730 0.3770 -0.0257 0.0572 -0.0490 277 TYR A CE1 1834 C CE2 . TYR A 284 ? 0.2953 0.2736 0.3479 -0.0228 0.0775 -0.0511 277 TYR A CE2 1835 C CZ . TYR A 284 ? 0.3428 0.2570 0.3806 0.0160 0.0630 -0.0494 277 TYR A CZ 1836 O OH . TYR A 284 ? 0.3716 0.2321 0.4391 -0.0001 0.0251 -0.0345 277 TYR A OH 1837 N N . ALA A 285 ? 0.2222 0.3073 0.3221 -0.0070 0.0141 0.0000 278 ALA A N 1838 C CA . ALA A 285 ? 0.2192 0.3317 0.3403 -0.0024 -0.0228 0.0318 278 ALA A CA 1839 C C . ALA A 285 ? 0.2702 0.2978 0.3308 0.0093 -0.0106 -0.0054 278 ALA A C 1840 O O . ALA A 285 ? 0.3032 0.3059 0.3715 0.0309 -0.0057 -0.0160 278 ALA A O 1841 C CB . ALA A 285 ? 0.2041 0.4232 0.3282 -0.0219 -0.0497 0.0759 278 ALA A CB 1842 N N . TYR A 286 ? 0.2350 0.3069 0.3045 0.0188 0.0027 0.0029 279 TYR A N 1843 C CA . TYR A 286 ? 0.2970 0.2679 0.3150 0.0407 0.0021 -0.0135 279 TYR A CA 1844 C C . TYR A 286 ? 0.2888 0.3081 0.2758 -0.0203 0.0051 -0.0405 279 TYR A C 1845 O O . TYR A 286 ? 0.3526 0.2946 0.3740 -0.0687 0.0522 -0.0993 279 TYR A O 1846 C CB . TYR A 286 ? 0.3804 0.3301 0.3556 0.0978 0.0141 0.0155 279 TYR A CB 1847 C CG A TYR A 286 ? 0.2792 0.3190 0.3665 0.0744 -0.0510 -0.0020 279 TYR A CG 1848 C CG B TYR A 286 ? 0.3972 0.3129 0.3828 0.0702 0.0191 0.0134 279 TYR A CG 1849 C CD1 A TYR A 286 ? 0.2471 0.3656 0.3591 0.0719 -0.0048 -0.0078 279 TYR A CD1 1850 C CD1 B TYR A 286 ? 0.4192 0.3180 0.3924 0.1455 0.0096 -0.0436 279 TYR A CD1 1851 C CD2 A TYR A 286 ? 0.3391 0.3109 0.3565 0.1234 0.0140 -0.0156 279 TYR A CD2 1852 C CD2 B TYR A 286 ? 0.4041 0.3468 0.4036 0.0520 -0.0052 -0.0558 279 TYR A CD2 1853 C CE1 A TYR A 286 ? 0.3108 0.4025 0.3769 0.0123 -0.0140 -0.0853 279 TYR A CE1 1854 C CE1 B TYR A 286 ? 0.4466 0.3800 0.4064 0.0990 -0.0171 -0.0062 279 TYR A CE1 1855 C CE2 A TYR A 286 ? 0.3796 0.3197 0.3567 0.0739 0.0154 -0.0176 279 TYR A CE2 1856 C CE2 B TYR A 286 ? 0.4245 0.2804 0.4214 0.1979 -0.0170 0.0287 279 TYR A CE2 1857 C CZ A TYR A 286 ? 0.3763 0.3611 0.3845 0.0810 -0.0291 -0.0127 279 TYR A CZ 1858 C CZ B TYR A 286 ? 0.4567 0.4590 0.4016 0.0862 -0.0151 -0.0402 279 TYR A CZ 1859 O OH A TYR A 286 ? 0.4903 0.4508 0.4017 0.1802 -0.0779 0.0757 279 TYR A OH 1860 O OH B TYR A 286 ? 0.4886 0.5712 0.3494 0.1536 -0.0036 -0.0458 279 TYR A OH 1861 N N . ARG A 287 ? 0.2103 0.2406 0.2829 0.0286 0.0009 -0.0229 280 ARG A N 1862 C CA . ARG A 287 ? 0.2047 0.2419 0.2971 -0.0001 -0.0004 -0.0185 280 ARG A CA 1863 C C . ARG A 287 ? 0.2489 0.3084 0.2914 -0.0003 -0.0283 -0.0219 280 ARG A C 1864 O O . ARG A 287 ? 0.2180 0.3705 0.3084 -0.0185 -0.0292 -0.0307 280 ARG A O 1865 C CB A ARG A 287 ? 0.2205 0.2625 0.3162 0.0319 -0.0010 -0.0350 280 ARG A CB 1866 C CB B ARG A 287 ? 0.1789 0.2459 0.2566 0.0161 0.0084 -0.0151 280 ARG A CB 1867 C CG A ARG A 287 ? 0.2512 0.3775 0.2923 -0.0178 -0.0290 -0.0204 280 ARG A CG 1868 C CG B ARG A 287 ? 0.1191 0.1348 0.2617 0.0063 0.0168 -0.0268 280 ARG A CG 1869 C CD A ARG A 287 ? 0.2900 0.5036 0.3218 -0.0728 -0.0425 0.0096 280 ARG A CD 1870 C CD B ARG A 287 ? 0.0530 0.1404 0.2272 0.0079 0.0073 -0.0490 280 ARG A CD 1871 N NE A ARG A 287 ? 0.2405 0.4576 0.3457 -0.0157 0.0011 0.0202 280 ARG A NE 1872 N NE B ARG A 287 ? 0.1188 0.1208 0.2309 0.0252 -0.0060 -0.0651 280 ARG A NE 1873 C CZ A ARG A 287 ? 0.2086 0.3828 0.3642 -0.0168 -0.0220 0.0403 280 ARG A CZ 1874 C CZ B ARG A 287 ? 0.0904 0.1360 0.2240 0.0328 -0.0275 -0.0359 280 ARG A CZ 1875 N NH1 A ARG A 287 ? 0.1884 0.4506 0.4595 -0.0583 -0.0787 0.0884 280 ARG A NH1 1876 N NH1 B ARG A 287 ? 0.0783 0.1631 0.2021 0.0046 -0.0076 -0.0624 280 ARG A NH1 1877 N NH2 A ARG A 287 ? 0.2306 0.2658 0.3711 -0.0182 -0.0219 0.0358 280 ARG A NH2 1878 N NH2 B ARG A 287 ? 0.1002 0.2124 0.2434 0.0416 -0.0872 -0.0400 280 ARG A NH2 1879 N N . ARG A 288 ? 0.2442 0.2906 0.2756 0.0095 -0.0035 -0.0250 281 ARG A N 1880 C CA . ARG A 288 ? 0.2660 0.3044 0.2705 -0.0114 -0.0199 -0.0213 281 ARG A CA 1881 C C . ARG A 288 ? 0.2900 0.3151 0.2716 -0.0342 -0.0314 -0.0344 281 ARG A C 1882 O O . ARG A 288 ? 0.2897 0.3123 0.2786 0.0026 -0.0430 -0.0660 281 ARG A O 1883 C CB . ARG A 288 ? 0.2801 0.2926 0.2451 -0.0336 -0.0017 -0.0354 281 ARG A CB 1884 C CG . ARG A 288 ? 0.2789 0.2962 0.2456 -0.0638 0.0023 -0.0401 281 ARG A CG 1885 C CD . ARG A 288 ? 0.2569 0.3431 0.2908 -0.0512 -0.0263 -0.0650 281 ARG A CD 1886 N NE . ARG A 288 ? 0.3326 0.3133 0.3350 -0.0085 -0.0306 -0.0471 281 ARG A NE 1887 C CZ . ARG A 288 ? 0.3293 0.3304 0.3296 0.0056 0.0516 0.0093 281 ARG A CZ 1888 N NH1 . ARG A 288 ? 0.2934 0.3808 0.2800 0.0233 0.0131 0.0189 281 ARG A NH1 1889 N NH2 . ARG A 288 ? 0.3707 0.3248 0.3647 -0.0303 0.0226 -0.0010 281 ARG A NH2 1890 N N . GLY A 289 ? 0.2896 0.3731 0.2673 -0.0314 -0.0591 -0.0482 282 GLY A N 1891 C CA . GLY A 289 ? 0.3765 0.3926 0.2911 -0.0532 -0.0176 -0.0607 282 GLY A CA 1892 C C . GLY A 289 ? 0.3801 0.3874 0.2691 -0.0226 -0.0307 -0.0744 282 GLY A C 1893 O O . GLY A 289 ? 0.3531 0.4056 0.3030 -0.0550 -0.0159 -0.0504 282 GLY A O 1894 N N . ILE A 290 ? 0.3907 0.3981 0.3444 0.0016 -0.0353 -0.0859 283 ILE A N 1895 C CA . ILE A 290 ? 0.3864 0.3899 0.3489 0.0022 -0.0514 -0.1061 283 ILE A CA 1896 C C . ILE A 290 ? 0.3453 0.4310 0.2826 0.0201 -0.0070 -0.0981 283 ILE A C 1897 O O . ILE A 290 ? 0.3581 0.4868 0.2436 -0.0068 -0.0255 -0.0718 283 ILE A O 1898 C CB A ILE A 290 ? 0.3735 0.4265 0.3248 0.0192 -0.0210 -0.1269 283 ILE A CB 1899 C CB B ILE A 290 ? 0.3514 0.3963 0.2866 0.0162 -0.0277 -0.0843 283 ILE A CB 1900 C CG1 A ILE A 290 ? 0.4442 0.4288 0.3162 0.0649 -0.1009 -0.0771 283 ILE A CG1 1901 C CG1 B ILE A 290 ? 0.2663 0.3751 0.2870 0.0386 -0.0483 -0.0799 283 ILE A CG1 1902 C CG2 A ILE A 290 ? 0.4535 0.5182 0.3248 0.0036 -0.0394 -0.1027 283 ILE A CG2 1903 C CG2 B ILE A 290 ? 0.3392 0.3513 0.2133 0.0212 -0.0583 -0.0775 283 ILE A CG2 1904 C CD1 A ILE A 290 ? 0.3269 0.3863 0.3049 0.0306 -0.0697 -0.0550 283 ILE A CD1 1905 C CD1 B ILE A 290 ? 0.2460 0.3500 0.2952 0.0490 -0.0426 -0.0756 283 ILE A CD1 1906 N N . ALA A 291 ? 0.3988 0.4435 0.3306 0.0081 -0.0376 -0.0567 284 ALA A N 1907 C CA . ALA A 291 ? 0.4091 0.4680 0.3128 0.0212 0.0050 -0.0561 284 ALA A CA 1908 C C . ALA A 291 ? 0.4249 0.4362 0.3542 -0.0467 0.0000 -0.0135 284 ALA A C 1909 O O . ALA A 291 ? 0.3833 0.5651 0.2890 -0.0594 0.0964 -0.0506 284 ALA A O 1910 C CB . ALA A 291 ? 0.5339 0.5470 0.3070 0.0651 -0.0339 -0.0566 284 ALA A CB 1911 N N . GLU A 292 ? 0.3923 0.4510 0.2880 0.0098 -0.0609 -0.0019 285 GLU A N 1912 C CA . GLU A 292 ? 0.3894 0.4263 0.3092 0.0178 -0.0224 -0.0057 285 GLU A CA 1913 C C . GLU A 292 ? 0.3769 0.3880 0.2864 -0.0189 -0.0168 -0.0288 285 GLU A C 1914 O O . GLU A 292 ? 0.3979 0.3881 0.3182 -0.0277 -0.0121 -0.0381 285 GLU A O 1915 C CB . GLU A 292 ? 0.3545 0.4812 0.3231 0.0439 -0.0790 0.0512 285 GLU A CB 1916 C CG . GLU A 292 ? 0.4283 0.4575 0.3298 0.0862 -0.1013 0.0352 285 GLU A CG 1917 C CD . GLU A 292 ? 0.5689 0.5615 0.4552 -0.0277 -0.0689 -0.0052 285 GLU A CD 1918 O OE1 . GLU A 292 ? 0.4644 0.5852 0.5376 -0.0150 -0.0368 0.0133 285 GLU A OE1 1919 O OE2 . GLU A 292 ? 0.7882 0.7875 0.4680 0.0115 -0.0922 0.0517 285 GLU A OE2 1920 N N . ALA A 293 ? 0.3126 0.4004 0.2399 -0.0494 0.0125 0.0099 286 ALA A N 1921 C CA . ALA A 293 ? 0.2584 0.3740 0.2524 -0.0577 -0.0011 -0.0325 286 ALA A CA 1922 C C . ALA A 293 ? 0.2721 0.4040 0.2330 -0.0698 -0.0177 -0.0217 286 ALA A C 1923 O O . ALA A 293 ? 0.2668 0.4178 0.2311 -0.0535 0.0027 -0.0214 286 ALA A O 1924 C CB . ALA A 293 ? 0.2792 0.3598 0.2601 -0.0251 0.0224 -0.0304 286 ALA A CB 1925 N N . VAL A 294 ? 0.2356 0.2802 0.2217 -0.0128 -0.0034 -0.0749 287 VAL A N 1926 C CA . VAL A 294 ? 0.2202 0.2694 0.2400 -0.0045 -0.0061 -0.0479 287 VAL A CA 1927 C C . VAL A 294 ? 0.2371 0.2693 0.2603 -0.0001 0.0115 -0.0304 287 VAL A C 1928 O O . VAL A 294 ? 0.2158 0.2729 0.2469 -0.0156 0.0085 -0.0206 287 VAL A O 1929 C CB . VAL A 294 ? 0.2096 0.2743 0.2468 0.0041 0.0274 -0.0575 287 VAL A CB 1930 C CG1 . VAL A 294 ? 0.1930 0.2960 0.2495 0.0045 0.0075 -0.0319 287 VAL A CG1 1931 C CG2 . VAL A 294 ? 0.2211 0.3056 0.3008 0.0353 0.0432 0.0107 287 VAL A CG2 1932 N N . GLY A 295 ? 0.2140 0.2910 0.2363 0.0040 0.0102 -0.0567 288 GLY A N 1933 C CA . GLY A 295 ? 0.2418 0.2522 0.2725 0.0226 -0.0054 -0.0705 288 GLY A CA 1934 C C . GLY A 295 ? 0.2332 0.2489 0.2045 0.0012 0.0197 -0.0484 288 GLY A C 1935 O O . GLY A 295 ? 0.2447 0.2463 0.2169 0.0127 -0.0036 -0.0274 288 GLY A O 1936 N N . LEU A 296 ? 0.2393 0.2734 0.1956 -0.0013 0.0162 -0.0528 289 LEU A N 1937 C CA . LEU A 296 ? 0.2585 0.2330 0.2161 -0.0154 0.0145 -0.0259 289 LEU A CA 1938 C C . LEU A 296 ? 0.2534 0.2679 0.2195 0.0016 0.0177 -0.0287 289 LEU A C 1939 O O . LEU A 296 ? 0.2732 0.2864 0.2385 0.0256 0.0438 -0.0036 289 LEU A O 1940 C CB A LEU A 296 ? 0.2343 0.2602 0.2228 -0.0176 0.0105 -0.0021 289 LEU A CB 1941 C CB B LEU A 296 ? 0.2434 0.2632 0.2326 -0.0205 0.0172 -0.0283 289 LEU A CB 1942 C CG A LEU A 296 ? 0.2497 0.2527 0.2109 -0.0112 0.0127 -0.0068 289 LEU A CG 1943 C CG B LEU A 296 ? 0.2750 0.2730 0.2055 -0.0426 0.0161 -0.0457 289 LEU A CG 1944 C CD1 A LEU A 296 ? 0.1972 0.2405 0.2578 0.0287 0.0065 -0.0198 289 LEU A CD1 1945 C CD1 B LEU A 296 ? 0.2719 0.2365 0.2358 -0.0256 0.0221 -0.0611 289 LEU A CD1 1946 C CD2 A LEU A 296 ? 0.2846 0.3259 0.2870 0.0138 -0.0297 0.0379 289 LEU A CD2 1947 C CD2 B LEU A 296 ? 0.2673 0.2256 0.2989 -0.0609 0.0104 -0.0207 289 LEU A CD2 1948 N N . PRO A 297 ? 0.2507 0.2898 0.2232 0.0133 -0.0014 -0.0274 290 PRO A N 1949 C CA . PRO A 297 ? 0.2696 0.3164 0.2088 0.0156 0.0055 -0.0346 290 PRO A CA 1950 C C . PRO A 297 ? 0.2948 0.3266 0.2236 0.0023 0.0074 -0.0364 290 PRO A C 1951 O O . PRO A 297 ? 0.2609 0.3176 0.2480 0.0030 -0.0082 -0.0516 290 PRO A O 1952 C CB . PRO A 297 ? 0.2939 0.3362 0.2574 0.0381 0.0327 -0.0109 290 PRO A CB 1953 C CG . PRO A 297 ? 0.2862 0.3156 0.2662 0.0299 0.0174 -0.0283 290 PRO A CG 1954 C CD . PRO A 297 ? 0.3046 0.2661 0.2750 0.0398 -0.0005 -0.0304 290 PRO A CD 1955 N N A SER A 298 ? 0.3151 0.3039 0.2316 0.0037 0.0182 -0.0322 291 SER A N 1956 N N B SER A 298 ? 0.3233 0.3109 0.2239 0.0069 0.0144 -0.0359 291 SER A N 1957 C CA A SER A 298 ? 0.3348 0.3241 0.2425 0.0318 0.0030 -0.0533 291 SER A CA 1958 C CA B SER A 298 ? 0.3384 0.3258 0.2294 0.0289 0.0066 -0.0568 291 SER A CA 1959 C C A SER A 298 ? 0.3091 0.3227 0.2281 0.0147 0.0315 -0.0399 291 SER A C 1960 C C B SER A 298 ? 0.3130 0.3126 0.2270 0.0096 0.0238 -0.0460 291 SER A C 1961 O O A SER A 298 ? 0.2976 0.3381 0.2716 0.0397 0.0118 -0.0636 291 SER A O 1962 O O B SER A 298 ? 0.3184 0.3109 0.2383 0.0311 0.0005 -0.0252 291 SER A O 1963 C CB A SER A 298 ? 0.3448 0.3304 0.3338 0.0031 0.0367 -0.0147 291 SER A CB 1964 C CB B SER A 298 ? 0.4028 0.3231 0.2736 0.0204 0.0332 -0.0373 291 SER A CB 1965 O OG A SER A 298 ? 0.3702 0.2868 0.3498 -0.0026 0.0801 0.0101 291 SER A OG 1966 O OG B SER A 298 ? 0.4786 0.3917 0.2380 0.0422 0.0484 -0.0524 291 SER A OG 1967 N N . ILE A 299 ? 0.3085 0.2899 0.2378 0.0159 0.0581 -0.0148 292 ILE A N 1968 C CA . ILE A 299 ? 0.3199 0.2916 0.2043 0.0181 0.0105 -0.0556 292 ILE A CA 1969 C C . ILE A 299 ? 0.3199 0.2914 0.2254 0.0148 0.0067 -0.0570 292 ILE A C 1970 O O . ILE A 299 ? 0.3678 0.2828 0.2215 0.0071 0.0208 -0.0370 292 ILE A O 1971 C CB . ILE A 299 ? 0.3182 0.3189 0.1956 0.0213 0.0077 -0.0232 292 ILE A CB 1972 C CG1 . ILE A 299 ? 0.3231 0.3232 0.2430 0.0040 0.0216 -0.0528 292 ILE A CG1 1973 C CG2 . ILE A 299 ? 0.3408 0.3462 0.2418 0.0465 0.0113 -0.0078 292 ILE A CG2 1974 C CD1 . ILE A 299 ? 0.3048 0.3881 0.2831 0.0220 0.0358 -0.0519 292 ILE A CD1 1975 N N . PRO A 300 ? 0.3058 0.2830 0.2276 0.0341 -0.0210 -0.0503 293 PRO A N 1976 C CA . PRO A 300 ? 0.3127 0.2686 0.2440 0.0046 0.0143 -0.0552 293 PRO A CA 1977 C C . PRO A 300 ? 0.3089 0.2823 0.2094 0.0157 0.0058 -0.0304 293 PRO A C 1978 O O . PRO A 300 ? 0.2696 0.2847 0.2353 0.0368 0.0256 -0.0307 293 PRO A O 1979 C CB . PRO A 300 ? 0.2942 0.3093 0.2080 0.0139 0.0028 -0.0756 293 PRO A CB 1980 C CG . PRO A 300 ? 0.3030 0.2889 0.2985 0.0347 -0.0103 -0.0168 293 PRO A CG 1981 C CD . PRO A 300 ? 0.3389 0.2818 0.2236 -0.0073 0.0002 -0.0609 293 PRO A CD 1982 N N . VAL A 301 ? 0.2658 0.2752 0.1960 0.0086 0.0435 -0.0226 294 VAL A N 1983 C CA . VAL A 301 ? 0.2900 0.2423 0.2210 0.0195 0.0231 -0.0748 294 VAL A CA 1984 C C . VAL A 301 ? 0.2610 0.2611 0.2639 0.0353 0.0334 -0.0568 294 VAL A C 1985 O O . VAL A 301 ? 0.2601 0.2714 0.2331 0.0326 0.0057 -0.0525 294 VAL A O 1986 C CB . VAL A 301 ? 0.2430 0.2326 0.2002 0.0387 0.0118 -0.0637 294 VAL A CB 1987 C CG1 . VAL A 301 ? 0.2356 0.2588 0.3155 0.0103 -0.0093 -0.0558 294 VAL A CG1 1988 C CG2 . VAL A 301 ? 0.3222 0.2506 0.2208 0.0142 -0.0070 -0.0113 294 VAL A CG2 1989 N N . HIS A 302 ? 0.2547 0.2539 0.2123 0.0176 0.0209 -0.0727 295 HIS A N 1990 C CA . HIS A 302 ? 0.2446 0.2385 0.2363 0.0325 0.0279 -0.0850 295 HIS A CA 1991 C C . HIS A 302 ? 0.2385 0.2787 0.2447 0.0097 0.0291 -0.0538 295 HIS A C 1992 O O . HIS A 302 ? 0.2145 0.2716 0.2741 0.0430 0.0413 -0.0288 295 HIS A O 1993 C CB . HIS A 302 ? 0.2630 0.2476 0.2196 0.0086 0.0284 -0.0775 295 HIS A CB 1994 C CG . HIS A 302 ? 0.2704 0.2536 0.2106 0.0234 0.0227 -0.0785 295 HIS A CG 1995 N ND1 . HIS A 302 ? 0.2568 0.2496 0.2479 0.0213 0.0285 -0.0683 295 HIS A ND1 1996 C CD2 . HIS A 302 ? 0.3028 0.2160 0.2607 0.0341 0.0147 -0.0714 295 HIS A CD2 1997 C CE1 . HIS A 302 ? 0.2649 0.2318 0.2991 0.0272 0.0454 -0.0823 295 HIS A CE1 1998 N NE2 . HIS A 302 ? 0.2629 0.2709 0.2742 0.0001 0.0594 -0.0787 295 HIS A NE2 1999 N N . PRO A 303 ? 0.2461 0.2576 0.2255 0.0007 0.0301 -0.0649 296 PRO A N 2000 C CA . PRO A 303 ? 0.2134 0.2302 0.2452 0.0418 0.0531 -0.0596 296 PRO A CA 2001 C C . PRO A 303 ? 0.2271 0.2301 0.2638 0.0404 0.0358 -0.0582 296 PRO A C 2002 O O . PRO A 303 ? 0.2653 0.2369 0.2868 0.0255 0.0354 -0.0404 296 PRO A O 2003 C CB . PRO A 303 ? 0.2448 0.2407 0.2316 0.0083 0.0245 -0.0560 296 PRO A CB 2004 C CG . PRO A 303 ? 0.2226 0.2414 0.2392 0.0238 0.0198 -0.0561 296 PRO A CG 2005 C CD . PRO A 303 ? 0.2475 0.2408 0.2304 0.0071 0.0227 -0.0549 296 PRO A CD 2006 N N . ILE A 304 ? 0.2382 0.2593 0.2486 0.0351 0.0660 -0.0628 297 ILE A N 2007 C CA . ILE A 304 ? 0.2339 0.2356 0.2922 0.0222 0.0525 -0.0586 297 ILE A CA 2008 C C . ILE A 304 ? 0.2358 0.2558 0.3080 0.0118 0.0517 -0.0655 297 ILE A C 2009 O O . ILE A 304 ? 0.2360 0.2487 0.3083 0.0206 0.0300 -0.0617 297 ILE A O 2010 C CB . ILE A 304 ? 0.2519 0.2624 0.2796 -0.0166 0.0526 -0.0571 297 ILE A CB 2011 C CG1 . ILE A 304 ? 0.2497 0.2672 0.2417 0.0027 0.0852 -0.0576 297 ILE A CG1 2012 C CG2 . ILE A 304 ? 0.2864 0.2593 0.2402 0.0099 0.0294 -0.0599 297 ILE A CG2 2013 C CD1 . ILE A 304 ? 0.2765 0.2784 0.2512 0.0258 0.0938 -0.0693 297 ILE A CD1 2014 N N . GLY A 305 ? 0.1994 0.2580 0.3014 -0.0029 0.0653 -0.0153 298 GLY A N 2015 C CA . GLY A 305 ? 0.2072 0.2863 0.3194 0.0453 0.0567 -0.0249 298 GLY A CA 2016 C C . GLY A 305 ? 0.2333 0.3072 0.3241 0.0118 0.0643 -0.0615 298 GLY A C 2017 O O . GLY A 305 ? 0.2687 0.2573 0.3075 0.0288 0.0806 -0.0634 298 GLY A O 2018 N N . TYR A 306 ? 0.1953 0.2352 0.3956 0.0557 0.0797 -0.0666 299 TYR A N 2019 C CA . TYR A 306 ? 0.2165 0.2976 0.3246 0.0288 0.0728 -0.0843 299 TYR A CA 2020 C C . TYR A 306 ? 0.2478 0.2734 0.3556 0.0308 0.0632 -0.0927 299 TYR A C 2021 O O . TYR A 306 ? 0.2860 0.3186 0.3742 0.0293 0.0977 -0.0862 299 TYR A O 2022 C CB . TYR A 306 ? 0.2760 0.2812 0.3288 -0.0220 0.0611 -0.0649 299 TYR A CB 2023 C CG . TYR A 306 ? 0.2656 0.2857 0.3872 0.0225 0.0392 -0.0573 299 TYR A CG 2024 C CD1 . TYR A 306 ? 0.2411 0.2803 0.3803 -0.0291 0.0585 -0.0100 299 TYR A CD1 2025 C CD2 . TYR A 306 ? 0.2680 0.2652 0.3807 0.0079 -0.0015 -0.0710 299 TYR A CD2 2026 C CE1 . TYR A 306 ? 0.2074 0.2205 0.3847 -0.0041 0.0422 -0.0525 299 TYR A CE1 2027 C CE2 . TYR A 306 ? 0.2064 0.2561 0.3775 0.0093 0.0380 -0.0387 299 TYR A CE2 2028 C CZ . TYR A 306 ? 0.2469 0.2702 0.3895 0.0377 0.0577 -0.0506 299 TYR A CZ 2029 O OH . TYR A 306 ? 0.2235 0.2857 0.3421 0.0021 0.0436 -0.0684 299 TYR A OH 2030 N N . TYR A 307 ? 0.2743 0.2771 0.3636 0.0353 0.0366 -0.0920 300 TYR A N 2031 C CA . TYR A 307 ? 0.2614 0.2769 0.3699 0.0279 0.0755 -0.0784 300 TYR A CA 2032 C C . TYR A 307 ? 0.2664 0.2688 0.3612 0.0312 0.0940 -0.0820 300 TYR A C 2033 O O . TYR A 307 ? 0.2513 0.3346 0.3467 0.0549 0.0632 -0.0843 300 TYR A O 2034 C CB . TYR A 307 ? 0.2925 0.2489 0.4122 0.0302 0.0394 -0.0768 300 TYR A CB 2035 C CG . TYR A 307 ? 0.3107 0.2885 0.4257 0.0770 0.0711 -0.0558 300 TYR A CG 2036 C CD1 . TYR A 307 ? 0.3084 0.3674 0.3768 0.0651 0.1105 -0.0719 300 TYR A CD1 2037 C CD2 . TYR A 307 ? 0.2966 0.3024 0.3677 0.0430 0.0802 -0.0635 300 TYR A CD2 2038 C CE1 . TYR A 307 ? 0.2900 0.3833 0.4008 0.0858 0.1006 -0.0784 300 TYR A CE1 2039 C CE2 . TYR A 307 ? 0.3138 0.3299 0.4283 0.1173 0.0383 -0.1138 300 TYR A CE2 2040 C CZ . TYR A 307 ? 0.3316 0.3818 0.4243 0.0949 0.0494 -0.0592 300 TYR A CZ 2041 O OH . TYR A 307 ? 0.3905 0.4202 0.4258 0.1606 0.0542 -0.0522 300 TYR A OH 2042 N N . ASP A 308 ? 0.2506 0.2628 0.4014 0.0356 0.0691 -0.0520 301 ASP A N 2043 C CA . ASP A 308 ? 0.2662 0.3208 0.3738 0.0012 0.0833 -0.0477 301 ASP A CA 2044 C C . ASP A 308 ? 0.2911 0.2909 0.3609 0.0423 0.0945 -0.0813 301 ASP A C 2045 O O . ASP A 308 ? 0.3209 0.3223 0.3450 0.0212 0.1061 -0.0967 301 ASP A O 2046 C CB . ASP A 308 ? 0.2572 0.3298 0.3311 0.0149 0.0751 -0.0353 301 ASP A CB 2047 C CG . ASP A 308 ? 0.2811 0.3061 0.3390 0.0403 0.0781 -0.0546 301 ASP A CG 2048 O OD1 . ASP A 308 ? 0.2716 0.3166 0.4345 0.0700 0.0693 -0.0469 301 ASP A OD1 2049 O OD2 . ASP A 308 ? 0.2505 0.2945 0.3727 0.0199 0.0462 -0.0410 301 ASP A OD2 2050 N N . ALA A 309 ? 0.2714 0.3062 0.3704 0.0170 0.0810 -0.0855 302 ALA A N 2051 C CA . ALA A 309 ? 0.2924 0.3049 0.3311 -0.0072 0.1161 -0.0890 302 ALA A CA 2052 C C . ALA A 309 ? 0.3152 0.3345 0.3407 0.0782 0.1236 -0.0889 302 ALA A C 2053 O O . ALA A 309 ? 0.3631 0.3407 0.3737 0.0222 0.0922 -0.0623 302 ALA A O 2054 C CB . ALA A 309 ? 0.2917 0.2672 0.3614 0.0106 0.0978 -0.0911 302 ALA A CB 2055 N N . GLN A 310 ? 0.2974 0.3157 0.3461 0.0740 0.1218 -0.0961 303 GLN A N 2056 C CA . GLN A 310 ? 0.3283 0.3372 0.3627 0.0602 0.1458 -0.1117 303 GLN A CA 2057 C C . GLN A 310 ? 0.3358 0.3750 0.3618 0.0502 0.0974 -0.0933 303 GLN A C 2058 O O . GLN A 310 ? 0.3288 0.4045 0.3902 0.0560 0.0925 -0.0706 303 GLN A O 2059 C CB . GLN A 310 ? 0.2853 0.3903 0.4065 0.0568 0.1161 -0.0810 303 GLN A CB 2060 C CG . GLN A 310 ? 0.3204 0.5577 0.4324 0.0647 0.1437 -0.0941 303 GLN A CG 2061 C CD . GLN A 310 ? 0.3167 0.7002 0.5326 -0.0170 0.1276 -0.0281 303 GLN A CD 2062 O OE1 . GLN A 310 ? 0.5321 0.7874 0.6012 -0.1428 0.0534 0.0657 303 GLN A OE1 2063 N NE2 . GLN A 310 ? 0.2945 0.5487 0.5515 0.1094 0.1129 -0.0260 303 GLN A NE2 2064 N N . LYS A 311 ? 0.3299 0.3714 0.3751 0.0565 0.1038 -0.0834 304 LYS A N 2065 C CA . LYS A 311 ? 0.3372 0.3636 0.3835 0.0470 0.1244 -0.0985 304 LYS A CA 2066 C C . LYS A 311 ? 0.3766 0.3616 0.3926 0.0605 0.1419 -0.1120 304 LYS A C 2067 O O . LYS A 311 ? 0.4414 0.4235 0.4029 0.0867 0.1424 -0.0638 304 LYS A O 2068 C CB . LYS A 311 ? 0.3986 0.3431 0.4478 0.0413 0.1148 -0.1254 304 LYS A CB 2069 C CG . LYS A 311 ? 0.4175 0.3988 0.4342 0.0457 0.1481 -0.0475 304 LYS A CG 2070 C CD . LYS A 311 ? 0.4712 0.4780 0.4765 0.0259 0.2150 -0.0690 304 LYS A CD 2071 C CE . LYS A 311 ? 0.5890 0.5941 0.5320 0.0364 0.1334 -0.1200 304 LYS A CE 2072 N NZ . LYS A 311 ? 0.6109 0.6176 0.8424 0.1641 0.1567 -0.1066 304 LYS A NZ 2073 N N . LEU A 312 ? 0.3194 0.3411 0.4073 0.0526 0.1405 -0.0948 305 LEU A N 2074 C CA . LEU A 312 ? 0.3161 0.4086 0.3476 0.0475 0.1565 -0.0720 305 LEU A CA 2075 C C . LEU A 312 ? 0.4092 0.3731 0.3663 0.0224 0.1095 -0.0561 305 LEU A C 2076 O O . LEU A 312 ? 0.3634 0.4292 0.3736 0.0153 0.1311 -0.0259 305 LEU A O 2077 C CB . LEU A 312 ? 0.2962 0.3323 0.4034 0.0626 0.1390 -0.0835 305 LEU A CB 2078 C CG . LEU A 312 ? 0.3614 0.3390 0.3430 0.0281 0.0993 -0.0999 305 LEU A CG 2079 C CD1 . LEU A 312 ? 0.3748 0.3739 0.3472 0.0220 0.1157 -0.1234 305 LEU A CD1 2080 C CD2 . LEU A 312 ? 0.4548 0.4379 0.3375 0.0070 0.0728 -0.1099 305 LEU A CD2 2081 N N . LEU A 313 ? 0.3301 0.3899 0.3522 0.0343 0.1312 -0.0447 306 LEU A N 2082 C CA . LEU A 313 ? 0.3493 0.3890 0.3257 0.0186 0.1646 -0.0873 306 LEU A CA 2083 C C . LEU A 313 ? 0.3880 0.3837 0.3550 0.0678 0.1740 -0.1123 306 LEU A C 2084 O O . LEU A 313 ? 0.3876 0.4183 0.4074 0.0488 0.1601 -0.0657 306 LEU A O 2085 C CB . LEU A 313 ? 0.3777 0.3349 0.3217 0.0447 0.1515 -0.0995 306 LEU A CB 2086 C CG . LEU A 313 ? 0.3364 0.3098 0.3531 0.0529 0.1546 -0.0673 306 LEU A CG 2087 C CD1 . LEU A 313 ? 0.3619 0.4137 0.3527 0.0347 0.1512 -0.1227 306 LEU A CD1 2088 C CD2 . LEU A 313 ? 0.3418 0.3292 0.4028 0.0505 0.1737 -0.0146 306 LEU A CD2 2089 N N . GLU A 314 ? 0.3457 0.3885 0.3702 0.0718 0.1537 -0.0830 307 GLU A N 2090 C CA . GLU A 314 ? 0.3680 0.3813 0.4099 0.0687 0.1912 -0.0719 307 GLU A CA 2091 C C . GLU A 314 ? 0.4065 0.4135 0.4114 0.0529 0.1784 -0.0769 307 GLU A C 2092 O O . GLU A 314 ? 0.3945 0.4242 0.4381 0.0464 0.1764 -0.0449 307 GLU A O 2093 C CB . GLU A 314 ? 0.3059 0.4009 0.4518 0.0811 0.1221 -0.0621 307 GLU A CB 2094 C CG . GLU A 314 ? 0.4116 0.3821 0.4696 0.0398 0.1444 -0.0617 307 GLU A CG 2095 C CD . GLU A 314 ? 0.4629 0.3957 0.5506 0.0790 0.1293 -0.0882 307 GLU A CD 2096 O OE1 . GLU A 314 ? 0.5331 0.4386 0.4515 0.0354 0.1681 -0.0001 307 GLU A OE1 2097 O OE2 . GLU A 314 ? 0.5421 0.3830 0.5340 0.0812 0.1080 -0.0874 307 GLU A OE2 2098 N N . LYS A 315 ? 0.4449 0.4203 0.4118 0.0316 0.1612 -0.0718 308 LYS A N 2099 C CA . LYS A 315 ? 0.4996 0.4434 0.4075 0.0153 0.1280 -0.0895 308 LYS A CA 2100 C C . LYS A 315 ? 0.4789 0.4649 0.4045 0.0569 0.1681 -0.0932 308 LYS A C 2101 O O . LYS A 315 ? 0.5276 0.4725 0.4022 0.0685 0.1542 -0.0905 308 LYS A O 2102 C CB . LYS A 315 ? 0.4478 0.4606 0.4562 0.0259 0.1271 -0.1046 308 LYS A CB 2103 C CG . LYS A 315 ? 0.4971 0.4537 0.4599 0.0300 0.0644 -0.1063 308 LYS A CG 2104 C CD . LYS A 315 ? 0.5007 0.4732 0.4187 0.0131 0.1018 -0.1518 308 LYS A CD 2105 C CE . LYS A 315 ? 0.5453 0.4853 0.4819 0.0415 0.0821 -0.1464 308 LYS A CE 2106 N NZ . LYS A 315 ? 0.5890 0.4654 0.5176 -0.0191 0.1554 -0.1254 308 LYS A NZ 2107 N N . MET A 316 ? 0.4638 0.4390 0.4127 0.0472 0.2135 -0.0780 309 MET A N 2108 C CA . MET A 316 ? 0.4036 0.4571 0.4056 0.0314 0.2352 -0.0618 309 MET A CA 2109 C C . MET A 316 ? 0.4543 0.4693 0.3815 -0.0028 0.2024 -0.0209 309 MET A C 2110 O O . MET A 316 ? 0.4156 0.4804 0.4258 0.0420 0.2342 -0.0233 309 MET A O 2111 C CB . MET A 316 ? 0.4005 0.4103 0.3624 0.0248 0.2088 -0.0228 309 MET A CB 2112 C CG A MET A 316 ? 0.4112 0.4638 0.3361 0.0164 0.2057 -0.0065 309 MET A CG 2113 C CG B MET A 316 ? 0.4065 0.4750 0.3697 0.0225 0.2004 0.0226 309 MET A CG 2114 S SD A MET A 316 ? 0.4083 0.3505 0.3403 0.0249 0.1080 -0.0367 309 MET A SD 2115 S SD B MET A 316 ? 0.3919 0.4662 0.4291 0.0071 0.1460 -0.0175 309 MET A SD 2116 C CE A MET A 316 ? 0.4674 0.3621 0.3921 0.0160 0.1003 -0.0136 309 MET A CE 2117 C CE B MET A 316 ? 0.4394 0.4675 0.4475 -0.0036 0.1064 -0.0094 309 MET A CE 2118 N N . GLY A 317 ? 0.4912 0.4035 0.3742 0.0192 0.1856 -0.0736 310 GLY A N 2119 C CA . GLY A 317 ? 0.4560 0.4790 0.4162 0.0377 0.2112 -0.0161 310 GLY A CA 2120 C C . GLY A 317 ? 0.5650 0.4901 0.4272 0.0207 0.2128 -0.0032 310 GLY A C 2121 O O . GLY A 317 ? 0.5426 0.5134 0.4234 0.0214 0.2222 0.0098 310 GLY A O 2122 N N . GLY A 318 ? 0.5463 0.5201 0.4014 0.0282 0.2333 -0.0028 311 GLY A N 2123 C CA . GLY A 318 ? 0.5381 0.4959 0.4356 -0.0095 0.2221 0.0028 311 GLY A CA 2124 C C . GLY A 318 ? 0.5312 0.4701 0.4609 0.0165 0.2302 -0.0277 311 GLY A C 2125 O O . GLY A 318 ? 0.5298 0.4700 0.5057 0.0237 0.2509 0.0119 311 GLY A O 2126 N N . SER A 319 ? 0.4829 0.4733 0.3912 0.0401 0.2736 0.0156 312 SER A N 2127 C CA . SER A 319 ? 0.5391 0.4584 0.4598 0.0555 0.2105 -0.0319 312 SER A CA 2128 C C . SER A 319 ? 0.4637 0.4734 0.4994 0.0527 0.2120 -0.0335 312 SER A C 2129 O O . SER A 319 ? 0.4997 0.4686 0.4905 0.0036 0.1942 -0.0588 312 SER A O 2130 C CB . SER A 319 ? 0.5571 0.5025 0.5514 0.1224 0.2080 0.0076 312 SER A CB 2131 O OG . SER A 319 ? 0.6247 0.5724 0.5201 0.1102 0.1920 -0.0116 312 SER A OG 2132 N N . ALA A 320 ? 0.4891 0.4745 0.5305 0.0031 0.2061 -0.0158 313 ALA A N 2133 C CA . ALA A 320 ? 0.4457 0.4925 0.4955 0.0296 0.2350 -0.0538 313 ALA A CA 2134 C C . ALA A 320 ? 0.4284 0.5147 0.4736 0.0301 0.2359 -0.0252 313 ALA A C 2135 O O . ALA A 320 ? 0.4781 0.4997 0.4559 0.0116 0.2240 0.0272 313 ALA A O 2136 C CB . ALA A 320 ? 0.4728 0.4568 0.5344 -0.0230 0.2389 0.0323 313 ALA A CB 2137 N N . PRO A 321 ? 0.3740 0.4506 0.4938 0.0018 0.2904 -0.0006 314 PRO A N 2138 C CA . PRO A 321 ? 0.4161 0.4424 0.4880 0.0061 0.2477 -0.0213 314 PRO A CA 2139 C C . PRO A 321 ? 0.4021 0.4491 0.5147 -0.0085 0.2231 -0.0101 314 PRO A C 2140 O O . PRO A 321 ? 0.3881 0.4356 0.5102 -0.0542 0.1908 0.0324 314 PRO A O 2141 C CB . PRO A 321 ? 0.3697 0.4520 0.4690 -0.0011 0.2620 -0.0132 314 PRO A CB 2142 C CG . PRO A 321 ? 0.3952 0.4113 0.4693 -0.0005 0.2261 -0.0672 314 PRO A CG 2143 C CD . PRO A 321 ? 0.4732 0.4405 0.4752 0.0007 0.2149 0.0162 314 PRO A CD 2144 N N . PRO A 322 ? 0.4270 0.4343 0.4892 -0.0139 0.2089 -0.0065 315 PRO A N 2145 C CA . PRO A 322 ? 0.3820 0.4555 0.5033 -0.0261 0.2342 -0.0018 315 PRO A CA 2146 C C . PRO A 322 ? 0.3532 0.4791 0.5324 -0.0566 0.2270 0.0365 315 PRO A C 2147 O O . PRO A 322 ? 0.3906 0.4792 0.5949 -0.0719 0.2459 0.0381 315 PRO A O 2148 C CB . PRO A 322 ? 0.3548 0.4229 0.5124 -0.0079 0.1803 0.0069 315 PRO A CB 2149 C CG . PRO A 322 ? 0.4384 0.4196 0.4740 -0.0172 0.1995 -0.0019 315 PRO A CG 2150 C CD . PRO A 322 ? 0.4193 0.4118 0.4810 0.0426 0.2163 0.0179 315 PRO A CD 2151 N N . ASP A 323 ? 0.3999 0.4569 0.5129 -0.0177 0.1787 0.0084 316 ASP A N 2152 C CA . ASP A 323 ? 0.3660 0.4652 0.6036 -0.0320 0.1625 0.0059 316 ASP A CA 2153 C C . ASP A 323 ? 0.3728 0.4517 0.6194 -0.0199 0.1146 0.0123 316 ASP A C 2154 O O . ASP A 323 ? 0.3369 0.4503 0.5617 -0.0159 0.1365 0.0592 316 ASP A O 2155 C CB . ASP A 323 ? 0.4389 0.4240 0.5864 -0.0256 0.1525 0.0405 316 ASP A CB 2156 C CG . ASP A 323 ? 0.3805 0.4613 0.6345 -0.0280 0.1138 0.0285 316 ASP A CG 2157 O OD1 . ASP A 323 ? 0.4276 0.5156 0.5854 -0.0068 0.1315 0.0251 316 ASP A OD1 2158 O OD2 . ASP A 323 ? 0.4596 0.4760 0.6407 0.0060 0.1323 0.0525 316 ASP A OD2 2159 N N . SER A 324 ? 0.2914 0.5311 0.5992 -0.0039 0.1702 -0.0029 317 SER A N 2160 C CA . SER A 324 ? 0.4103 0.5360 0.6152 -0.0451 0.1186 0.0111 317 SER A CA 2161 C C . SER A 324 ? 0.3905 0.4832 0.6062 -0.0095 0.1195 -0.0168 317 SER A C 2162 O O . SER A 324 ? 0.3313 0.4752 0.6193 -0.0317 0.0491 -0.0169 317 SER A O 2163 C CB . SER A 324 ? 0.4265 0.5511 0.6266 -0.0017 0.0898 -0.0200 317 SER A CB 2164 O OG . SER A 324 ? 0.4339 0.4804 0.6942 -0.0771 0.0009 -0.0231 317 SER A OG 2165 N N . SER A 325 ? 0.3791 0.4267 0.6141 -0.0738 0.1018 -0.0483 318 SER A N 2166 C CA . SER A 325 ? 0.3616 0.4201 0.5700 -0.0560 0.0932 -0.0552 318 SER A CA 2167 C C . SER A 325 ? 0.3108 0.4577 0.5110 -0.0412 0.1336 -0.0558 318 SER A C 2168 O O . SER A 325 ? 0.3362 0.4370 0.4976 -0.0705 0.1202 -0.0194 318 SER A O 2169 C CB . SER A 325 ? 0.3320 0.4244 0.5936 -0.0558 0.0639 -0.0404 318 SER A CB 2170 O OG . SER A 325 ? 0.3256 0.3684 0.5838 -0.0284 0.0964 -0.0431 318 SER A OG 2171 N N . TRP A 326 ? 0.3200 0.3428 0.4861 -0.0543 0.1532 -0.0194 319 TRP A N 2172 C CA . TRP A 326 ? 0.2776 0.3662 0.4592 -0.0107 0.1612 -0.0205 319 TRP A CA 2173 C C . TRP A 326 ? 0.3106 0.3780 0.5024 0.0198 0.1592 -0.0511 319 TRP A C 2174 O O . TRP A 326 ? 0.3102 0.3561 0.4664 0.0221 0.1475 -0.0409 319 TRP A O 2175 C CB . TRP A 326 ? 0.3478 0.4083 0.4712 0.0362 0.1412 0.0058 319 TRP A CB 2176 C CG . TRP A 326 ? 0.2804 0.3695 0.3912 -0.0035 0.1725 -0.0059 319 TRP A CG 2177 C CD1 . TRP A 326 ? 0.2853 0.3659 0.4161 -0.0165 0.2011 -0.0019 319 TRP A CD1 2178 C CD2 . TRP A 326 ? 0.2772 0.3441 0.4268 -0.0101 0.1580 -0.0141 319 TRP A CD2 2179 N NE1 . TRP A 326 ? 0.3388 0.3481 0.4265 -0.0018 0.1180 -0.0101 319 TRP A NE1 2180 C CE2 . TRP A 326 ? 0.3284 0.3614 0.4489 0.0181 0.1124 -0.0102 319 TRP A CE2 2181 C CE3 . TRP A 326 ? 0.2429 0.3790 0.3483 0.0113 0.1476 -0.0020 319 TRP A CE3 2182 C CZ2 . TRP A 326 ? 0.2964 0.3677 0.3695 -0.0207 0.1210 -0.0069 319 TRP A CZ2 2183 C CZ3 . TRP A 326 ? 0.2315 0.3311 0.4038 0.0126 0.1245 -0.0097 319 TRP A CZ3 2184 C CH2 . TRP A 326 ? 0.3084 0.3231 0.4039 -0.0012 0.1279 -0.0311 319 TRP A CH2 2185 N N . ARG A 327 ? 0.2983 0.3871 0.4371 0.0300 0.1700 -0.0576 320 ARG A N 2186 C CA . ARG A 327 ? 0.3061 0.3636 0.4685 -0.0060 0.1452 -0.0002 320 ARG A CA 2187 C C . ARG A 327 ? 0.3154 0.3533 0.4379 -0.0115 0.1333 -0.0292 320 ARG A C 2188 O O . ARG A 327 ? 0.3236 0.4107 0.4714 -0.0556 0.1150 -0.0420 320 ARG A O 2189 C CB . ARG A 327 ? 0.2952 0.4207 0.4881 -0.0101 0.1330 -0.0410 320 ARG A CB 2190 C CG . ARG A 327 ? 0.2862 0.5230 0.4897 -0.0631 0.1348 -0.0956 320 ARG A CG 2191 C CD . ARG A 327 ? 0.3751 0.7092 0.5859 -0.0389 0.3105 -0.0853 320 ARG A CD 2192 N NE . ARG A 327 ? 0.6500 0.7844 0.7937 -0.0729 0.1507 0.0995 320 ARG A NE 2193 C CZ . ARG A 327 ? 0.6632 0.9298 0.8813 -0.1216 0.1136 -0.0316 320 ARG A CZ 2194 N NH1 . ARG A 327 ? 0.7450 0.9756 0.8591 -0.0205 0.1595 -0.1432 320 ARG A NH1 2195 N NH2 . ARG A 327 ? 0.6875 1.1682 1.0508 -0.1101 0.2942 0.0766 320 ARG A NH2 2196 N N . GLY A 328 ? 0.2759 0.3926 0.4702 -0.0072 0.1125 -0.0218 321 GLY A N 2197 C CA . GLY A 328 ? 0.2535 0.3565 0.4593 0.0107 0.1489 -0.0210 321 GLY A CA 2198 C C . GLY A 328 ? 0.2569 0.3723 0.4824 0.0189 0.1132 -0.0521 321 GLY A C 2199 O O . GLY A 328 ? 0.2819 0.3507 0.4644 0.0206 0.1091 -0.0145 321 GLY A O 2200 N N . SER A 329 ? 0.2469 0.3568 0.4716 0.0055 0.1465 -0.0576 322 SER A N 2201 C CA . SER A 329 ? 0.3055 0.3366 0.4910 0.0082 0.1032 -0.0589 322 SER A CA 2202 C C . SER A 329 ? 0.2941 0.3850 0.5015 0.0560 0.1236 -0.0814 322 SER A C 2203 O O . SER A 329 ? 0.2556 0.4024 0.5518 0.0410 0.0782 -0.0615 322 SER A O 2204 C CB . SER A 329 ? 0.4272 0.4122 0.4872 0.1076 0.0184 -0.0444 322 SER A CB 2205 O OG . SER A 329 ? 0.4177 0.5454 0.5747 0.0741 0.0251 -0.1053 322 SER A OG 2206 N N . LEU A 330 ? 0.2873 0.3715 0.4792 0.0302 0.1392 -0.0906 323 LEU A N 2207 C CA . LEU A 330 ? 0.2667 0.3870 0.4664 0.0135 0.1602 -0.0951 323 LEU A CA 2208 C C . LEU A 330 ? 0.2981 0.3959 0.4562 0.0580 0.1584 -0.0384 323 LEU A C 2209 O O . LEU A 330 ? 0.2481 0.4240 0.4930 -0.0057 0.0799 -0.0358 323 LEU A O 2210 C CB . LEU A 330 ? 0.2659 0.3931 0.4440 0.0407 0.1475 -0.0468 323 LEU A CB 2211 C CG . LEU A 330 ? 0.2647 0.3472 0.4499 0.0446 0.1500 -0.0525 323 LEU A CG 2212 C CD1 . LEU A 330 ? 0.2740 0.3812 0.4463 0.0485 0.1280 -0.0671 323 LEU A CD1 2213 C CD2 . LEU A 330 ? 0.3633 0.3582 0.4719 0.0455 0.1176 -0.0305 323 LEU A CD2 2214 N N . LYS A 331 ? 0.2591 0.4228 0.5015 0.0579 0.1532 -0.0739 324 LYS A N 2215 C CA . LYS A 331 ? 0.3419 0.4597 0.4854 0.1211 0.1795 -0.0420 324 LYS A CA 2216 C C . LYS A 331 ? 0.4183 0.4252 0.4600 0.0828 0.1960 -0.0972 324 LYS A C 2217 O O . LYS A 331 ? 0.5069 0.4120 0.4719 -0.0027 0.2228 -0.0934 324 LYS A O 2218 C CB . LYS A 331 ? 0.3419 0.4239 0.5562 0.1035 0.1815 -0.0965 324 LYS A CB 2219 C CG . LYS A 331 ? 0.3896 0.6096 0.6228 0.0280 0.1451 0.0065 324 LYS A CG 2220 C CD . LYS A 331 ? 0.4718 0.5929 0.7044 -0.0039 0.0293 0.0533 324 LYS A CD 2221 C CE . LYS A 331 ? 0.4024 0.5243 0.6126 0.0220 0.1548 -0.0133 324 LYS A CE 2222 N NZ . LYS A 331 ? 0.3656 0.5125 0.6181 0.0067 0.1605 0.0101 324 LYS A NZ 2223 N N . VAL A 332 ? 0.2842 0.4435 0.5327 0.0459 0.1354 -0.0031 325 VAL A N 2224 C CA . VAL A 332 ? 0.4020 0.4035 0.4514 0.0206 0.1493 -0.0690 325 VAL A CA 2225 C C . VAL A 332 ? 0.4033 0.4063 0.4375 0.0149 0.1944 -0.0623 325 VAL A C 2226 O O . VAL A 332 ? 0.2669 0.4190 0.4776 0.0158 0.1322 -0.0081 325 VAL A O 2227 C CB . VAL A 332 ? 0.3855 0.4070 0.4304 0.0125 0.1606 -0.0810 325 VAL A CB 2228 C CG1 . VAL A 332 ? 0.3815 0.3777 0.4231 0.0471 0.1203 -0.1186 325 VAL A CG1 2229 C CG2 . VAL A 332 ? 0.3842 0.3827 0.4016 0.0070 0.1695 -0.0477 325 VAL A CG2 2230 N N . PRO A 333 ? 0.4336 0.3939 0.4426 0.0356 0.2044 -0.0504 326 PRO A N 2231 C CA . PRO A 333 ? 0.3913 0.4198 0.4512 0.0350 0.1965 -0.0603 326 PRO A CA 2232 C C . PRO A 333 ? 0.3826 0.4048 0.3881 0.0134 0.2006 -0.0481 326 PRO A C 2233 O O . PRO A 333 ? 0.3372 0.4323 0.4990 -0.0102 0.1788 -0.0270 326 PRO A O 2234 C CB . PRO A 333 ? 0.4383 0.4314 0.4655 0.0287 0.2091 0.0027 326 PRO A CB 2235 C CG . PRO A 333 ? 0.4818 0.4700 0.4775 0.0370 0.1646 -0.0371 326 PRO A CG 2236 C CD . PRO A 333 ? 0.4589 0.4065 0.4788 -0.0057 0.1684 -0.0454 326 PRO A CD 2237 N N . TYR A 334 ? 0.3385 0.4288 0.4190 0.0615 0.1679 -0.0749 327 TYR A N 2238 C CA . TYR A 334 ? 0.3756 0.3731 0.3961 0.0443 0.1820 -0.0387 327 TYR A CA 2239 C C . TYR A 334 ? 0.3559 0.4198 0.4274 0.0214 0.1822 -0.0134 327 TYR A C 2240 O O . TYR A 334 ? 0.3977 0.4023 0.4228 0.0017 0.1564 -0.0081 327 TYR A O 2241 C CB . TYR A 334 ? 0.3338 0.3754 0.3892 0.0055 0.1677 -0.0130 327 TYR A CB 2242 C CG . TYR A 334 ? 0.3221 0.3735 0.3840 0.0385 0.1713 -0.0228 327 TYR A CG 2243 C CD1 . TYR A 334 ? 0.2971 0.2985 0.4062 0.0359 0.1472 -0.0370 327 TYR A CD1 2244 C CD2 . TYR A 334 ? 0.3259 0.3380 0.3535 0.0056 0.1063 -0.0424 327 TYR A CD2 2245 C CE1 . TYR A 334 ? 0.2558 0.3283 0.3812 0.0179 0.1464 -0.0207 327 TYR A CE1 2246 C CE2 . TYR A 334 ? 0.2826 0.3217 0.3760 0.0079 0.1143 -0.0298 327 TYR A CE2 2247 C CZ . TYR A 334 ? 0.2717 0.3332 0.4157 0.0293 0.1228 -0.0189 327 TYR A CZ 2248 O OH . TYR A 334 ? 0.2389 0.3283 0.4007 0.0089 0.1008 -0.0135 327 TYR A OH 2249 N N . ASN A 335 ? 0.3007 0.4313 0.4047 -0.0232 0.1739 -0.0040 328 ASN A N 2250 C CA . ASN A 335 ? 0.3720 0.4299 0.4083 0.0278 0.1639 -0.0274 328 ASN A CA 2251 C C . ASN A 335 ? 0.3649 0.3953 0.4156 0.0286 0.1722 -0.0547 328 ASN A C 2252 O O . ASN A 335 ? 0.4220 0.3631 0.3803 0.0510 0.1790 -0.0138 328 ASN A O 2253 C CB . ASN A 335 ? 0.3597 0.4791 0.4000 0.0248 0.2032 -0.0385 328 ASN A CB 2254 C CG . ASN A 335 ? 0.3647 0.4387 0.4478 0.0631 0.1996 -0.0690 328 ASN A CG 2255 O OD1 . ASN A 335 ? 0.4055 0.4853 0.4080 -0.0042 0.2038 -0.0476 328 ASN A OD1 2256 N ND2 . ASN A 335 ? 0.4127 0.4285 0.3658 0.0214 0.2254 -0.0511 328 ASN A ND2 2257 N N . VAL A 336 ? 0.3609 0.4251 0.4182 -0.0056 0.1466 -0.0110 329 VAL A N 2258 C CA . VAL A 336 ? 0.4186 0.3988 0.4176 0.0499 0.1686 -0.0736 329 VAL A CA 2259 C C . VAL A 336 ? 0.4122 0.3593 0.3697 0.0497 0.1845 -0.0322 329 VAL A C 2260 O O . VAL A 336 ? 0.4053 0.4115 0.3413 0.0274 0.1949 -0.0310 329 VAL A O 2261 C CB . VAL A 336 ? 0.4864 0.3998 0.4412 0.0523 0.1024 -0.1249 329 VAL A CB 2262 C CG1 . VAL A 336 ? 0.4659 0.4961 0.4635 0.0202 0.1252 -0.0108 329 VAL A CG1 2263 C CG2 . VAL A 336 ? 0.4427 0.3308 0.4831 0.0065 0.0727 -0.0675 329 VAL A CG2 2264 N N . GLY A 337 ? 0.4338 0.4377 0.3727 0.0688 0.1642 -0.0808 330 GLY A N 2265 C CA . GLY A 337 ? 0.4948 0.4521 0.3697 0.0298 0.1334 -0.0352 330 GLY A CA 2266 C C . GLY A 337 ? 0.5142 0.4592 0.2890 0.0376 0.1597 -0.0539 330 GLY A C 2267 O O . GLY A 337 ? 0.5050 0.4762 0.3828 0.0353 0.1365 -0.0227 330 GLY A O 2268 N N . PRO A 338 ? 0.5036 0.4770 0.3945 0.0401 0.1415 0.0121 331 PRO A N 2269 C CA . PRO A 338 ? 0.5242 0.4361 0.4233 0.0489 0.1476 -0.0115 331 PRO A CA 2270 C C . PRO A 338 ? 0.4487 0.5202 0.3399 0.0407 0.2034 -0.0502 331 PRO A C 2271 O O . PRO A 338 ? 0.4832 0.5116 0.3237 0.0449 0.2071 -0.0528 331 PRO A O 2272 C CB . PRO A 338 ? 0.4925 0.5619 0.4224 0.0234 0.1517 0.0321 331 PRO A CB 2273 C CG . PRO A 338 ? 0.5779 0.5874 0.4202 0.0056 0.1160 0.0450 331 PRO A CG 2274 C CD . PRO A 338 ? 0.5261 0.5316 0.4172 0.0275 0.1473 0.0493 331 PRO A CD 2275 N N . GLY A 339 ? 0.5105 0.4883 0.2635 0.0703 0.1809 -0.0589 332 GLY A N 2276 C CA . GLY A 339 ? 0.5581 0.4649 0.3833 0.0908 0.1289 -0.0783 332 GLY A CA 2277 C C . GLY A 339 ? 0.5239 0.5043 0.4581 0.0696 0.1468 -0.1059 332 GLY A C 2278 O O . GLY A 339 ? 0.5106 0.4808 0.3936 0.0245 0.2095 -0.0993 332 GLY A O 2279 N N . PHE A 340 ? 0.5275 0.4824 0.3683 0.0233 0.2164 -0.0638 333 PHE A N 2280 C CA . PHE A 340 ? 0.5097 0.5426 0.4441 0.0164 0.2367 -0.0021 333 PHE A CA 2281 C C . PHE A 340 ? 0.5554 0.6117 0.4098 0.0097 0.2508 -0.0338 333 PHE A C 2282 O O . PHE A 340 ? 0.5832 0.5415 0.4552 0.0579 0.2296 -0.0431 333 PHE A O 2283 C CB . PHE A 340 ? 0.4457 0.5302 0.4138 0.0409 0.2228 -0.0739 333 PHE A CB 2284 C CG . PHE A 340 ? 0.4956 0.4531 0.3946 0.0092 0.1994 -0.0776 333 PHE A CG 2285 C CD1 . PHE A 340 ? 0.4664 0.4786 0.3653 0.0304 0.2372 -0.1702 333 PHE A CD1 2286 C CD2 . PHE A 340 ? 0.4508 0.5003 0.3363 0.0567 0.2390 -0.0477 333 PHE A CD2 2287 C CE1 . PHE A 340 ? 0.4755 0.5821 0.3880 -0.0311 0.1862 -0.0674 333 PHE A CE1 2288 C CE2 . PHE A 340 ? 0.3248 0.4529 0.4190 0.0685 0.1964 0.0136 333 PHE A CE2 2289 C CZ . PHE A 340 ? 0.4918 0.4751 0.3866 0.0050 0.1504 -0.0431 333 PHE A CZ 2290 N N . THR A 341 ? 0.5719 0.5423 0.4219 0.0374 0.2438 -0.0732 334 THR A N 2291 C CA . THR A 341 ? 0.5937 0.6532 0.4422 0.0212 0.2589 -0.0380 334 THR A CA 2292 C C . THR A 341 ? 0.6736 0.7103 0.4570 -0.0493 0.2326 -0.0441 334 THR A C 2293 O O . THR A 341 ? 0.7781 0.7581 0.4506 -0.1279 0.2268 -0.1492 334 THR A O 2294 C CB . THR A 341 ? 0.6087 0.6853 0.5057 0.0321 0.2532 -0.0597 334 THR A CB 2295 O OG1 . THR A 341 ? 0.5547 0.6935 0.6774 0.1017 0.2984 0.0162 334 THR A OG1 2296 C CG2 . THR A 341 ? 0.5721 0.6692 0.5453 0.1248 0.2405 -0.1243 334 THR A CG2 2297 N N . GLY A 342 ? 0.6266 0.7157 0.4926 0.0112 0.2441 -0.0091 335 GLY A N 2298 C CA . GLY A 342 ? 0.7167 0.7606 0.5250 -0.0646 0.2400 -0.0236 335 GLY A CA 2299 C C . GLY A 342 ? 0.6912 0.7224 0.5304 -0.0071 0.2466 0.0171 335 GLY A C 2300 O O . GLY A 342 ? 0.5806 0.9151 0.6552 0.0407 0.2607 0.1612 335 GLY A O 2301 N N . ASN A 343 ? 0.7121 0.7286 0.5495 0.0879 0.3510 0.0203 336 ASN A N 2302 C CA . ASN A 343 ? 0.7016 0.7511 0.6373 0.0501 0.3301 0.0080 336 ASN A CA 2303 C C . ASN A 343 ? 0.6816 0.6235 0.5040 0.0248 0.2792 -0.1172 336 ASN A C 2304 O O . ASN A 343 ? 0.8042 0.6777 0.4532 0.0026 0.1684 -0.1393 336 ASN A O 2305 C CB . ASN A 343 ? 0.7777 0.7922 0.6490 0.0604 0.2761 0.0401 336 ASN A CB 2306 C CG . ASN A 343 ? 0.7660 0.9329 0.8063 0.1454 0.2701 -0.0580 336 ASN A CG 2307 O OD1 . ASN A 343 ? 1.0699 0.8333 0.8880 0.0548 0.2397 -0.0396 336 ASN A OD1 2308 N ND2 . ASN A 343 ? 1.0231 1.0649 1.0060 0.1386 -0.0446 0.0240 336 ASN A ND2 2309 N N . PHE A 344 ? 0.6648 0.6622 0.4630 0.0629 0.2672 -0.0824 337 PHE A N 2310 C CA . PHE A 344 ? 0.6179 0.6164 0.4373 0.0645 0.2156 -0.0861 337 PHE A CA 2311 C C . PHE A 344 ? 0.6069 0.6125 0.4885 0.0680 0.2344 -0.0876 337 PHE A C 2312 O O . PHE A 344 ? 0.6595 0.5968 0.3805 0.0761 0.2362 -0.0962 337 PHE A O 2313 C CB . PHE A 344 ? 0.7015 0.5584 0.4332 0.0494 0.1509 -0.1465 337 PHE A CB 2314 C CG . PHE A 344 ? 0.6204 0.6775 0.4020 0.0689 0.2552 -0.1095 337 PHE A CG 2315 C CD1 . PHE A 344 ? 0.6438 0.6436 0.5118 0.0578 0.2013 -0.0668 337 PHE A CD1 2316 C CD2 . PHE A 344 ? 0.6218 0.6735 0.4671 0.0730 0.1876 -0.1398 337 PHE A CD2 2317 C CE1 . PHE A 344 ? 0.6074 0.6563 0.5811 0.0807 0.2414 -0.1005 337 PHE A CE1 2318 C CE2 . PHE A 344 ? 0.6491 0.6058 0.5890 0.1039 0.2091 -0.1855 337 PHE A CE2 2319 C CZ . PHE A 344 ? 0.6721 0.6581 0.5597 0.1044 0.1289 -0.1118 337 PHE A CZ 2320 N N . SER A 345 ? 0.6275 0.5750 0.4224 0.0714 0.1830 -0.1233 338 SER A N 2321 C CA . SER A 345 ? 0.6534 0.6352 0.4306 0.0668 0.1758 -0.0375 338 SER A CA 2322 C C . SER A 345 ? 0.7193 0.6680 0.4234 0.0187 0.1318 -0.0278 338 SER A C 2323 O O . SER A 345 ? 0.7836 0.7541 0.3370 0.0567 0.1775 -0.0124 338 SER A O 2324 C CB . SER A 345 ? 0.6579 0.7063 0.4610 0.0200 0.2076 -0.0356 338 SER A CB 2325 O OG . SER A 345 ? 0.6912 0.7307 0.5094 -0.1118 0.1328 -0.0137 338 SER A OG 2326 N N . THR A 346 ? 0.6767 0.6506 0.3448 0.0498 0.2083 -0.0364 339 THR A N 2327 C CA . THR A 346 ? 0.7321 0.6323 0.3270 0.0227 0.1596 -0.1082 339 THR A CA 2328 C C . THR A 346 ? 0.6518 0.6140 0.4190 0.0212 0.1269 -0.0492 339 THR A C 2329 O O . THR A 346 ? 0.6213 0.5800 0.4307 -0.0040 0.2076 -0.0415 339 THR A O 2330 C CB . THR A 346 ? 0.6880 0.6274 0.3702 0.0404 0.1975 -0.1489 339 THR A CB 2331 O OG1 . THR A 346 ? 0.7540 0.7150 0.3964 0.0925 0.1638 -0.0798 339 THR A OG1 2332 C CG2 . THR A 346 ? 0.8208 0.6255 0.4260 -0.0387 0.1228 -0.0497 339 THR A CG2 2333 N N . GLN A 347 ? 0.6331 0.6060 0.3641 0.0580 0.1557 -0.0923 340 GLN A N 2334 C CA . GLN A 347 ? 0.5910 0.5286 0.3676 0.0510 0.1434 -0.1115 340 GLN A CA 2335 C C . GLN A 347 ? 0.5546 0.5402 0.4328 0.0687 0.1654 -0.0972 340 GLN A C 2336 O O . GLN A 347 ? 0.5943 0.5212 0.3823 0.0615 0.1439 -0.1408 340 GLN A O 2337 C CB . GLN A 347 ? 0.5074 0.4560 0.4117 0.0778 0.1929 -0.0872 340 GLN A CB 2338 C CG . GLN A 347 ? 0.5875 0.4958 0.4503 0.0859 0.1222 -0.1906 340 GLN A CG 2339 C CD . GLN A 347 ? 0.6095 0.4309 0.5310 0.1133 0.1375 -0.1787 340 GLN A CD 2340 O OE1 . GLN A 347 ? 0.5329 0.5658 0.4721 0.0574 0.1713 -0.0812 340 GLN A OE1 2341 N NE2 . GLN A 347 ? 0.6348 0.4928 0.4654 0.1646 0.1365 -0.2211 340 GLN A NE2 2342 N N . LYS A 348 ? 0.5710 0.4980 0.3458 0.0920 0.1682 -0.1193 341 LYS A N 2343 C CA . LYS A 348 ? 0.5396 0.4988 0.3019 0.0713 0.1785 -0.1081 341 LYS A CA 2344 C C . LYS A 348 ? 0.5838 0.4865 0.3142 0.0633 0.1418 -0.0919 341 LYS A C 2345 O O . LYS A 348 ? 0.5402 0.4578 0.3499 0.0532 0.1339 -0.1252 341 LYS A O 2346 C CB . LYS A 348 ? 0.5613 0.5647 0.3475 0.0613 0.1109 -0.1145 341 LYS A CB 2347 C CG . LYS A 348 ? 0.7278 0.6025 0.3625 0.1059 0.1020 -0.0699 341 LYS A CG 2348 C CD . LYS A 348 ? 0.8592 0.5861 0.4343 0.0812 0.1125 -0.0566 341 LYS A CD 2349 C CE . LYS A 348 ? 0.8568 0.6715 0.4874 0.0530 0.1106 0.0364 341 LYS A CE 2350 N NZ . LYS A 348 ? 0.8501 0.6410 0.6698 0.0037 0.0801 -0.0205 341 LYS A NZ 2351 N N . VAL A 349 ? 0.4607 0.4657 0.3246 0.0460 0.1323 -0.0785 342 VAL A N 2352 C CA . VAL A 349 ? 0.4429 0.4845 0.2996 0.0201 0.1194 -0.0997 342 VAL A CA 2353 C C . VAL A 349 ? 0.4437 0.4377 0.3300 0.0385 0.0959 -0.0741 342 VAL A C 2354 O O . VAL A 349 ? 0.4347 0.4303 0.3800 0.0668 0.0825 -0.0982 342 VAL A O 2355 C CB . VAL A 349 ? 0.4209 0.4169 0.2780 0.0356 0.0920 -0.0504 342 VAL A CB 2356 C CG1 . VAL A 349 ? 0.4614 0.3889 0.2702 0.0721 0.0922 -0.0656 342 VAL A CG1 2357 C CG2 . VAL A 349 ? 0.4146 0.4583 0.2875 0.0160 0.1319 -0.0364 342 VAL A CG2 2358 N N . LYS A 350 ? 0.4046 0.3693 0.3574 0.0181 0.0702 -0.1286 343 LYS A N 2359 C CA . LYS A 350 ? 0.4115 0.3979 0.3148 0.0180 0.0744 -0.0902 343 LYS A CA 2360 C C . LYS A 350 ? 0.3871 0.3710 0.3031 0.0498 0.0871 -0.1294 343 LYS A C 2361 O O . LYS A 350 ? 0.3269 0.4155 0.2950 0.0532 0.1035 -0.0840 343 LYS A O 2362 C CB . LYS A 350 ? 0.4099 0.4294 0.3276 -0.0130 0.0564 -0.0952 343 LYS A CB 2363 C CG . LYS A 350 ? 0.4009 0.4165 0.3101 0.0000 0.0086 -0.1218 343 LYS A CG 2364 C CD . LYS A 350 ? 0.5392 0.4688 0.3285 -0.0562 -0.0077 -0.1288 343 LYS A CD 2365 C CE . LYS A 350 ? 0.5486 0.5180 0.3631 -0.0602 0.0084 -0.1235 343 LYS A CE 2366 N NZ . LYS A 350 ? 0.7048 0.5545 0.4745 -0.0417 -0.0868 -0.1671 343 LYS A NZ 2367 N N . MET A 351 ? 0.3685 0.3409 0.3021 0.0477 0.0781 -0.1168 344 MET A N 2368 C CA . MET A 351 ? 0.3662 0.3390 0.2762 0.0420 0.0495 -0.1210 344 MET A CA 2369 C C . MET A 351 ? 0.4046 0.3812 0.2884 0.0047 0.0277 -0.0922 344 MET A C 2370 O O . MET A 351 ? 0.3621 0.4507 0.2858 0.0182 0.0348 -0.0617 344 MET A O 2371 C CB . MET A 351 ? 0.3710 0.3137 0.2932 0.0208 0.0409 -0.1127 344 MET A CB 2372 C CG . MET A 351 ? 0.4015 0.3404 0.2279 -0.0114 0.0151 -0.1042 344 MET A CG 2373 S SD . MET A 351 ? 0.3789 0.3294 0.2671 0.0288 0.0410 -0.0688 344 MET A SD 2374 C CE . MET A 351 ? 0.3768 0.4102 0.2056 0.0335 0.0482 -0.1273 344 MET A CE 2375 N N . HIS A 352 ? 0.3756 0.3510 0.3142 0.0100 0.0736 -0.0941 345 HIS A N 2376 C CA . HIS A 352 ? 0.3574 0.3567 0.3072 0.0130 0.0270 -0.1056 345 HIS A CA 2377 C C . HIS A 352 ? 0.3543 0.3198 0.3024 0.0234 0.0292 -0.0910 345 HIS A C 2378 O O . HIS A 352 ? 0.2727 0.3680 0.3256 0.0330 0.0215 -0.0989 345 HIS A O 2379 C CB . HIS A 352 ? 0.3563 0.3481 0.3072 0.0430 0.0434 -0.1093 345 HIS A CB 2380 C CG . HIS A 352 ? 0.4213 0.4351 0.3070 0.0548 0.0650 -0.0809 345 HIS A CG 2381 N ND1 . HIS A 352 ? 0.4179 0.4056 0.3253 0.0307 0.1148 -0.0873 345 HIS A ND1 2382 C CD2 . HIS A 352 ? 0.4897 0.4042 0.3302 0.0690 0.0533 -0.1075 345 HIS A CD2 2383 C CE1 . HIS A 352 ? 0.4983 0.4225 0.3050 0.0458 0.0732 -0.1388 345 HIS A CE1 2384 N NE2 . HIS A 352 ? 0.4722 0.4922 0.4259 -0.0013 0.0661 -0.1232 345 HIS A NE2 2385 N N . ILE A 353 ? 0.3194 0.3294 0.2601 0.0163 0.0215 -0.1089 346 ILE A N 2386 C CA . ILE A 353 ? 0.3212 0.3201 0.2817 0.0345 0.0397 -0.1031 346 ILE A CA 2387 C C . ILE A 353 ? 0.3347 0.3494 0.2509 0.0037 0.0251 -0.0936 346 ILE A C 2388 O O . ILE A 353 ? 0.3285 0.3817 0.2936 0.0371 0.0163 -0.0696 346 ILE A O 2389 C CB . ILE A 353 ? 0.3448 0.3176 0.2500 0.0366 0.0323 -0.0867 346 ILE A CB 2390 C CG1 . ILE A 353 ? 0.3412 0.2838 0.3103 0.0205 -0.0153 -0.0291 346 ILE A CG1 2391 C CG2 . ILE A 353 ? 0.4109 0.2752 0.2546 0.0431 0.0424 -0.0992 346 ILE A CG2 2392 C CD1 . ILE A 353 ? 0.3712 0.2898 0.3188 0.0196 -0.0344 -0.0216 346 ILE A CD1 2393 N N . HIS A 354 ? 0.3187 0.3335 0.2613 -0.0089 0.0342 -0.0864 347 HIS A N 2394 C CA . HIS A 354 ? 0.3080 0.3296 0.2395 -0.0026 -0.0107 -0.1086 347 HIS A CA 2395 C C . HIS A 354 ? 0.3040 0.2942 0.2541 -0.0111 0.0035 -0.1099 347 HIS A C 2396 O O . HIS A 354 ? 0.2807 0.3229 0.2878 -0.0120 -0.0243 -0.0901 347 HIS A O 2397 C CB . HIS A 354 ? 0.3846 0.3254 0.2830 0.0067 -0.0159 -0.1152 347 HIS A CB 2398 C CG . HIS A 354 ? 0.4529 0.4424 0.3335 0.0287 0.0284 -0.1485 347 HIS A CG 2399 N ND1 . HIS A 354 ? 0.4653 0.5147 0.3875 0.0263 0.0825 -0.1460 347 HIS A ND1 2400 C CD2 . HIS A 354 ? 0.4817 0.5103 0.3545 0.0183 -0.0201 -0.1525 347 HIS A CD2 2401 C CE1 . HIS A 354 ? 0.5837 0.4872 0.3775 0.0762 0.0499 -0.1952 347 HIS A CE1 2402 N NE2 . HIS A 354 ? 0.5189 0.6552 0.4178 0.0285 0.0350 -0.1529 347 HIS A NE2 2403 N N . SER A 355 ? 0.3062 0.2885 0.2391 0.0037 -0.0181 -0.0969 348 SER A N 2404 C CA . SER A 355 ? 0.2225 0.2643 0.2555 0.0119 -0.0047 -0.1241 348 SER A CA 2405 C C . SER A 355 ? 0.2512 0.2828 0.2787 0.0259 -0.0114 -0.0782 348 SER A C 2406 O O . SER A 355 ? 0.2448 0.3148 0.2560 0.0189 -0.0093 -0.0759 348 SER A O 2407 C CB . SER A 355 ? 0.2304 0.2735 0.2434 -0.0045 -0.0104 -0.1052 348 SER A CB 2408 O OG . SER A 355 ? 0.2623 0.2526 0.2952 0.0211 0.0180 -0.0627 348 SER A OG 2409 N N . THR A 356 ? 0.2617 0.2736 0.2868 0.0187 0.0064 -0.0838 349 THR A N 2410 C CA . THR A 356 ? 0.2578 0.2755 0.2857 0.0222 0.0012 -0.1072 349 THR A CA 2411 C C . THR A 356 ? 0.2715 0.2717 0.2626 0.0314 -0.0027 -0.0892 349 THR A C 2412 O O . THR A 356 ? 0.3444 0.2833 0.2944 0.0709 -0.0053 -0.0557 349 THR A O 2413 C CB . THR A 356 ? 0.3903 0.2765 0.2821 -0.0313 -0.0068 -0.1039 349 THR A CB 2414 O OG1 . THR A 356 ? 0.3145 0.3778 0.3789 -0.0094 0.0387 -0.0246 349 THR A OG1 2415 C CG2 . THR A 356 ? 0.2338 0.3205 0.3065 -0.0172 -0.0100 -0.1416 349 THR A CG2 2416 N N . ASN A 357 ? 0.2660 0.2526 0.2676 0.0163 0.0187 -0.0691 350 ASN A N 2417 C CA . ASN A 357 ? 0.2747 0.2445 0.2274 0.0012 0.0144 -0.0581 350 ASN A CA 2418 C C . ASN A 357 ? 0.2613 0.2739 0.2537 -0.0173 -0.0187 -0.0521 350 ASN A C 2419 O O . ASN A 357 ? 0.2666 0.3678 0.2493 -0.0452 -0.0198 -0.0759 350 ASN A O 2420 C CB . ASN A 357 ? 0.3228 0.2468 0.3001 -0.0238 0.0384 -0.0539 350 ASN A CB 2421 C CG . ASN A 357 ? 0.3164 0.2961 0.2652 -0.0161 0.0289 -0.0326 350 ASN A CG 2422 O OD1 . ASN A 357 ? 0.3670 0.3179 0.2409 -0.0166 0.0071 -0.0204 350 ASN A OD1 2423 N ND2 . ASN A 357 ? 0.4255 0.3496 0.2658 -0.0331 0.0190 -0.0051 350 ASN A ND2 2424 N N A GLU A 358 ? 0.2650 0.2590 0.2552 -0.0261 0.0299 -0.0490 351 GLU A N 2425 N N B GLU A 358 ? 0.2683 0.2710 0.2563 -0.0303 0.0253 -0.0549 351 GLU A N 2426 C CA A GLU A 358 ? 0.2871 0.2787 0.2836 -0.0471 0.0309 -0.0517 351 GLU A CA 2427 C CA B GLU A 358 ? 0.2683 0.2618 0.2767 -0.0337 0.0157 -0.0523 351 GLU A CA 2428 C C A GLU A 358 ? 0.2296 0.2553 0.2887 -0.0301 0.0263 -0.0470 351 GLU A C 2429 C C B GLU A 358 ? 0.2313 0.2405 0.2807 -0.0227 0.0212 -0.0454 351 GLU A C 2430 O O A GLU A 358 ? 0.2156 0.2540 0.2600 0.0146 0.0146 -0.0183 351 GLU A O 2431 O O B GLU A 358 ? 0.2337 0.2293 0.2611 -0.0077 0.0147 -0.0145 351 GLU A O 2432 C CB A GLU A 358 ? 0.3855 0.2535 0.3282 -0.0534 0.0224 -0.0579 351 GLU A CB 2433 C CB B GLU A 358 ? 0.3861 0.2430 0.3239 -0.0380 0.0215 -0.0796 351 GLU A CB 2434 C CG A GLU A 358 ? 0.4327 0.3528 0.3845 0.0092 0.0435 -0.0434 351 GLU A CG 2435 C CG B GLU A 358 ? 0.3865 0.3683 0.3208 -0.0127 0.0299 -0.0749 351 GLU A CG 2436 C CD A GLU A 358 ? 0.5051 0.3444 0.4210 0.0052 -0.0157 -0.0272 351 GLU A CD 2437 C CD B GLU A 358 ? 0.3664 0.2894 0.3888 -0.0170 0.0118 -0.0722 351 GLU A CD 2438 O OE1 A GLU A 358 ? 0.5979 0.5243 0.4979 -0.0830 -0.0499 -0.0652 351 GLU A OE1 2439 O OE1 B GLU A 358 ? 0.3775 0.4018 0.5053 0.0087 0.0230 -0.1145 351 GLU A OE1 2440 O OE2 A GLU A 358 ? 0.4818 0.3569 0.3699 -0.0832 -0.0452 -0.0715 351 GLU A OE2 2441 O OE2 B GLU A 358 ? 0.4179 0.3914 0.3521 0.0297 0.0740 -0.0128 351 GLU A OE2 2442 N N . VAL A 359 ? 0.2584 0.2435 0.2896 0.0027 0.0363 -0.0413 352 VAL A N 2443 C CA . VAL A 359 ? 0.2375 0.2073 0.2573 0.0132 0.0252 -0.0316 352 VAL A CA 2444 C C . VAL A 359 ? 0.2144 0.1826 0.2677 -0.0208 0.0246 -0.0490 352 VAL A C 2445 O O . VAL A 359 ? 0.2370 0.2070 0.2829 -0.0586 0.0003 -0.0333 352 VAL A O 2446 C CB . VAL A 359 ? 0.2234 0.2020 0.2397 -0.0211 0.0051 -0.0243 352 VAL A CB 2447 C CG1 . VAL A 359 ? 0.3083 0.2019 0.2207 -0.0001 0.0004 -0.0249 352 VAL A CG1 2448 C CG2 . VAL A 359 ? 0.2719 0.2241 0.2698 -0.0284 0.0293 0.0166 352 VAL A CG2 2449 N N . THR A 360 ? 0.1973 0.1974 0.2546 -0.0162 0.0275 -0.0097 353 THR A N 2450 C CA . THR A 360 ? 0.2208 0.1944 0.2432 -0.0112 0.0111 -0.0175 353 THR A CA 2451 C C . THR A 360 ? 0.2300 0.1865 0.2477 -0.0170 0.0395 -0.0059 353 THR A C 2452 O O . THR A 360 ? 0.2213 0.1821 0.2777 -0.0029 -0.0098 -0.0080 353 THR A O 2453 C CB . THR A 360 ? 0.2294 0.2352 0.2401 0.0125 0.0059 -0.0088 353 THR A CB 2454 O OG1 . THR A 360 ? 0.2471 0.2329 0.2661 0.0004 0.0236 -0.0374 353 THR A OG1 2455 C CG2 . THR A 360 ? 0.1964 0.2166 0.2661 0.0085 0.0170 -0.0086 353 THR A CG2 2456 N N . ARG A 361 ? 0.2025 0.2216 0.2381 -0.0109 0.0415 0.0058 354 ARG A N 2457 C CA . ARG A 361 ? 0.1899 0.1985 0.2447 -0.0157 0.0341 -0.0010 354 ARG A CA 2458 C C . ARG A 361 ? 0.1963 0.1849 0.2523 -0.0103 0.0197 -0.0104 354 ARG A C 2459 O O . ARG A 361 ? 0.2436 0.1958 0.2823 0.0071 0.0038 -0.0163 354 ARG A O 2460 C CB . ARG A 361 ? 0.1944 0.2100 0.2608 -0.0187 0.0714 -0.0192 354 ARG A CB 2461 C CG . ARG A 361 ? 0.2030 0.2493 0.2504 -0.0185 0.0636 0.0000 354 ARG A CG 2462 C CD . ARG A 361 ? 0.1795 0.2355 0.3155 -0.0117 0.0324 0.0371 354 ARG A CD 2463 N NE . ARG A 361 ? 0.2062 0.2198 0.3525 0.0155 0.0242 0.0017 354 ARG A NE 2464 C CZ . ARG A 361 ? 0.2164 0.2595 0.3361 -0.0106 0.0179 0.0357 354 ARG A CZ 2465 N NH1 . ARG A 361 ? 0.2371 0.2457 0.3671 -0.0446 0.0525 0.0265 354 ARG A NH1 2466 N NH2 . ARG A 361 ? 0.2590 0.3126 0.3795 0.0357 0.0076 0.0563 354 ARG A NH2 2467 N N . ILE A 362 ? 0.1753 0.1765 0.2208 -0.0272 0.0090 0.0212 355 ILE A N 2468 C CA . ILE A 362 ? 0.1697 0.1981 0.2069 -0.0175 0.0248 -0.0035 355 ILE A CA 2469 C C . ILE A 362 ? 0.1879 0.2136 0.2121 0.0020 0.0331 0.0008 355 ILE A C 2470 O O . ILE A 362 ? 0.1884 0.2060 0.2481 0.0059 0.0075 0.0098 355 ILE A O 2471 C CB . ILE A 362 ? 0.1715 0.1424 0.2265 0.0145 0.0298 0.0022 355 ILE A CB 2472 C CG1 . ILE A 362 ? 0.1897 0.1257 0.2202 0.0022 -0.0121 0.0035 355 ILE A CG1 2473 C CG2 . ILE A 362 ? 0.2031 0.1743 0.2192 0.0077 0.0218 -0.0165 355 ILE A CG2 2474 C CD1 . ILE A 362 ? 0.2152 0.1547 0.2510 -0.0230 0.0000 -0.0335 355 ILE A CD1 2475 N N . TYR A 363 ? 0.1951 0.1796 0.2066 -0.0144 0.0289 0.0021 356 TYR A N 2476 C CA . TYR A 363 ? 0.2306 0.1643 0.1974 -0.0131 0.0144 0.0074 356 TYR A CA 2477 C C . TYR A 363 ? 0.1886 0.1642 0.2107 -0.0028 0.0335 -0.0036 356 TYR A C 2478 O O . TYR A 363 ? 0.2031 0.2184 0.2240 0.0120 0.0240 -0.0005 356 TYR A O 2479 C CB . TYR A 363 ? 0.1932 0.1685 0.2331 -0.0104 0.0102 0.0283 356 TYR A CB 2480 C CG . TYR A 363 ? 0.2163 0.1902 0.2623 -0.0306 0.0308 0.0030 356 TYR A CG 2481 C CD1 . TYR A 363 ? 0.1843 0.2151 0.3430 -0.0175 0.0050 0.0549 356 TYR A CD1 2482 C CD2 . TYR A 363 ? 0.2332 0.1790 0.2744 -0.0114 0.0168 -0.0003 356 TYR A CD2 2483 C CE1 . TYR A 363 ? 0.2723 0.1933 0.3046 -0.0161 -0.0167 0.0321 356 TYR A CE1 2484 C CE2 . TYR A 363 ? 0.2479 0.2052 0.3011 -0.0436 0.0143 0.0267 356 TYR A CE2 2485 C CZ . TYR A 363 ? 0.2446 0.1910 0.3529 -0.0438 0.0186 0.0188 356 TYR A CZ 2486 O OH . TYR A 363 ? 0.2633 0.2444 0.3569 -0.0435 -0.0398 0.0280 356 TYR A OH 2487 N N . ASN A 364 ? 0.1881 0.1659 0.2105 0.0051 0.0372 -0.0084 357 ASN A N 2488 C CA . ASN A 364 ? 0.2320 0.1769 0.2219 -0.0070 0.0107 0.0101 357 ASN A CA 2489 C C . ASN A 364 ? 0.2386 0.1844 0.2329 0.0364 0.0233 0.0358 357 ASN A C 2490 O O . ASN A 364 ? 0.2448 0.2571 0.2886 -0.0072 0.0114 0.0662 357 ASN A O 2491 C CB . ASN A 364 ? 0.2170 0.1717 0.2110 0.0314 0.0181 0.0213 357 ASN A CB 2492 C CG . ASN A 364 ? 0.1864 0.1824 0.2379 0.0223 0.0324 0.0172 357 ASN A CG 2493 O OD1 . ASN A 364 ? 0.1878 0.1998 0.2152 0.0357 0.0165 0.0067 357 ASN A OD1 2494 N ND2 . ASN A 364 ? 0.1975 0.2000 0.2845 0.0431 0.0165 0.0299 357 ASN A ND2 2495 N N . VAL A 365 ? 0.2339 0.2059 0.2057 0.0261 0.0381 0.0315 358 VAL A N 2496 C CA . VAL A 365 ? 0.2496 0.1853 0.1976 0.0517 0.0425 0.0360 358 VAL A CA 2497 C C . VAL A 365 ? 0.2589 0.2010 0.2039 0.0387 0.0481 0.0306 358 VAL A C 2498 O O . VAL A 365 ? 0.2615 0.1863 0.2467 0.0181 0.0169 0.0061 358 VAL A O 2499 C CB . VAL A 365 ? 0.2581 0.1672 0.1689 0.0465 0.0540 0.0307 358 VAL A CB 2500 C CG1 . VAL A 365 ? 0.2682 0.2021 0.1745 0.0522 0.0572 0.0536 358 VAL A CG1 2501 C CG2 . VAL A 365 ? 0.3050 0.1849 0.2514 0.0495 0.0278 -0.0130 358 VAL A CG2 2502 N N . ILE A 366 ? 0.2409 0.1932 0.2270 0.0496 0.0433 0.0225 359 ILE A N 2503 C CA . ILE A 366 ? 0.2743 0.1892 0.2152 0.0622 0.0370 0.0294 359 ILE A CA 2504 C C . ILE A 366 ? 0.2582 0.2050 0.2122 0.0588 0.0421 0.0164 359 ILE A C 2505 O O . ILE A 366 ? 0.2946 0.2422 0.2157 0.0420 0.0521 0.0321 359 ILE A O 2506 C CB . ILE A 366 ? 0.2774 0.1955 0.1844 0.0690 0.0379 0.0236 359 ILE A CB 2507 C CG1 . ILE A 366 ? 0.2247 0.2518 0.2020 0.0420 0.0892 0.0675 359 ILE A CG1 2508 C CG2 . ILE A 366 ? 0.3306 0.1955 0.2381 0.0151 0.0360 0.0122 359 ILE A CG2 2509 C CD1 . ILE A 366 ? 0.2142 0.2644 0.2473 0.0169 0.0703 0.0564 359 ILE A CD1 2510 N N . GLY A 367 ? 0.3053 0.2296 0.1820 0.0603 0.0183 0.0325 360 GLY A N 2511 C CA . GLY A 367 ? 0.3000 0.2308 0.1769 0.0677 0.0401 0.0078 360 GLY A CA 2512 C C . GLY A 367 ? 0.2995 0.2194 0.1657 0.0545 0.0256 0.0166 360 GLY A C 2513 O O . GLY A 367 ? 0.3370 0.2387 0.1953 0.0251 0.0362 -0.0060 360 GLY A O 2514 N N . THR A 368 ? 0.2977 0.2228 0.2044 0.0693 0.0435 0.0032 361 THR A N 2515 C CA . THR A 368 ? 0.3107 0.2256 0.1998 0.0637 0.0357 0.0023 361 THR A CA 2516 C C . THR A 368 ? 0.3261 0.2589 0.2075 0.0696 0.0490 0.0298 361 THR A C 2517 O O . THR A 368 ? 0.3706 0.2483 0.2300 0.0531 0.0451 0.0452 361 THR A O 2518 C CB . THR A 368 ? 0.3333 0.2477 0.2266 0.0915 0.0359 -0.0046 361 THR A CB 2519 O OG1 . THR A 368 ? 0.3528 0.2844 0.2300 0.0734 0.0288 0.0457 361 THR A OG1 2520 C CG2 . THR A 368 ? 0.3617 0.2684 0.2434 0.0507 0.0658 -0.0207 361 THR A CG2 2521 N N . LEU A 369 ? 0.3272 0.2694 0.1867 0.0808 0.0185 0.0299 362 LEU A N 2522 C CA . LEU A 369 ? 0.3015 0.2608 0.1660 0.1155 0.0515 0.0447 362 LEU A CA 2523 C C . LEU A 369 ? 0.3438 0.2667 0.1665 0.1007 0.0664 0.0317 362 LEU A C 2524 O O . LEU A 369 ? 0.3498 0.2566 0.2062 0.1016 0.0601 0.0279 362 LEU A O 2525 C CB . LEU A 369 ? 0.3332 0.2904 0.1962 0.1186 -0.0038 0.0497 362 LEU A CB 2526 C CG . LEU A 369 ? 0.3408 0.3380 0.2082 0.1016 -0.0156 0.0912 362 LEU A CG 2527 C CD1 . LEU A 369 ? 0.4151 0.4051 0.2221 0.0717 -0.0031 0.1276 362 LEU A CD1 2528 C CD2 . LEU A 369 ? 0.3399 0.3911 0.2288 0.1362 0.0527 0.0120 362 LEU A CD2 2529 N N A ARG A 370 ? 0.3379 0.2728 0.1865 0.1167 0.0675 0.0333 363 ARG A N 2530 N N B ARG A 370 ? 0.3375 0.2672 0.1851 0.1204 0.0670 0.0271 363 ARG A N 2531 C CA A ARG A 370 ? 0.3694 0.2713 0.2067 0.1260 0.0476 0.0305 363 ARG A CA 2532 C CA B ARG A 370 ? 0.3599 0.2605 0.2062 0.1252 0.0472 0.0308 363 ARG A CA 2533 C C A ARG A 370 ? 0.3684 0.2722 0.1624 0.1398 0.0589 0.0338 363 ARG A C 2534 C C B ARG A 370 ? 0.3692 0.2561 0.1672 0.1467 0.0682 0.0230 363 ARG A C 2535 O O A ARG A 370 ? 0.3607 0.3160 0.1542 0.1172 0.0606 0.0638 363 ARG A O 2536 O O B ARG A 370 ? 0.3942 0.2940 0.1617 0.1369 0.0386 0.0154 363 ARG A O 2537 C CB A ARG A 370 ? 0.3600 0.2897 0.2258 0.1529 0.0589 0.0364 363 ARG A CB 2538 C CB B ARG A 370 ? 0.3418 0.2866 0.2258 0.1527 0.0613 0.0346 363 ARG A CB 2539 C CG A ARG A 370 ? 0.3594 0.3134 0.1990 0.1345 0.0697 0.0113 363 ARG A CG 2540 C CG B ARG A 370 ? 0.3744 0.2792 0.2053 0.1295 0.1053 0.0229 363 ARG A CG 2541 C CD A ARG A 370 ? 0.4164 0.3976 0.2947 0.0544 0.1013 0.0043 363 ARG A CD 2542 C CD B ARG A 370 ? 0.3603 0.3774 0.3128 0.0982 0.0281 0.0558 363 ARG A CD 2543 N NE A ARG A 370 ? 0.4420 0.3957 0.3795 0.1384 0.0760 0.0810 363 ARG A NE 2544 N NE B ARG A 370 ? 0.4457 0.3572 0.3975 0.0796 0.0981 0.0549 363 ARG A NE 2545 C CZ A ARG A 370 ? 0.4250 0.4293 0.4053 0.0711 0.0622 0.0564 363 ARG A CZ 2546 C CZ B ARG A 370 ? 0.4109 0.3959 0.3049 0.0840 0.0989 0.0284 363 ARG A CZ 2547 N NH1 A ARG A 370 ? 0.5112 0.4031 0.4210 0.1466 0.1441 -0.0565 363 ARG A NH1 2548 N NH1 B ARG A 370 ? 0.3660 0.4596 0.2557 0.1350 0.1233 0.0755 363 ARG A NH1 2549 N NH2 A ARG A 370 ? 0.4757 0.4221 0.4409 0.0642 0.0015 0.0703 363 ARG A NH2 2550 N NH2 B ARG A 370 ? 0.4721 0.4062 0.3815 0.1130 0.0981 0.0586 363 ARG A NH2 2551 N N . GLY A 371 ? 0.3596 0.2764 0.1635 0.0994 0.0671 0.0264 364 GLY A N 2552 C CA . GLY A 371 ? 0.4060 0.2998 0.1655 0.1035 0.0491 0.0037 364 GLY A CA 2553 C C . GLY A 371 ? 0.4090 0.2981 0.1660 0.1059 0.0579 0.0389 364 GLY A C 2554 O O . GLY A 371 ? 0.4125 0.3153 0.2043 0.1379 0.0316 0.0264 364 GLY A O 2555 N N . ALA A 372 ? 0.4534 0.3296 0.1786 0.1214 0.0354 0.0281 365 ALA A N 2556 C CA . ALA A 372 ? 0.4318 0.3126 0.1824 0.1465 0.0359 0.0364 365 ALA A CA 2557 C C . ALA A 372 ? 0.4302 0.3229 0.1781 0.1489 0.0646 0.0178 365 ALA A C 2558 O O . ALA A 372 ? 0.4748 0.3406 0.1891 0.1634 0.0947 0.0038 365 ALA A O 2559 C CB . ALA A 372 ? 0.4137 0.3568 0.1898 0.1488 0.0389 0.0562 365 ALA A CB 2560 N N . VAL A 373 ? 0.4392 0.3134 0.1659 0.1605 0.0348 0.0377 366 VAL A N 2561 C CA . VAL A 373 ? 0.4792 0.3046 0.1949 0.1322 0.0259 0.0092 366 VAL A CA 2562 C C . VAL A 373 ? 0.4146 0.3472 0.1811 0.1517 0.0552 0.0068 366 VAL A C 2563 O O . VAL A 373 ? 0.4578 0.3633 0.1775 0.1834 0.0747 0.0018 366 VAL A O 2564 C CB . VAL A 373 ? 0.5036 0.3401 0.2054 0.1431 -0.0275 -0.0113 366 VAL A CB 2565 C CG1 . VAL A 373 ? 0.5295 0.3429 0.2747 0.1218 -0.0696 -0.0658 366 VAL A CG1 2566 C CG2 . VAL A 373 ? 0.5904 0.3644 0.2078 0.0671 -0.0866 -0.0098 366 VAL A CG2 2567 N N . GLU A 374 ? 0.3755 0.3101 0.1311 0.1241 0.0166 0.0075 367 GLU A N 2568 C CA . GLU A 374 ? 0.4481 0.2944 0.1410 0.1266 0.0385 0.0238 367 GLU A CA 2569 C C . GLU A 374 ? 0.3465 0.2765 0.1453 0.1511 0.0137 0.0278 367 GLU A C 2570 O O . GLU A 374 ? 0.3832 0.2827 0.1335 0.1284 0.0236 0.0276 367 GLU A O 2571 C CB . GLU A 374 ? 0.4126 0.2867 0.1363 0.1021 0.0406 -0.0501 367 GLU A CB 2572 C CG . GLU A 374 ? 0.4936 0.2655 0.1819 0.0876 0.0472 -0.0501 367 GLU A CG 2573 C CD . GLU A 374 ? 0.4220 0.2560 0.2145 0.0972 -0.0048 -0.0157 367 GLU A CD 2574 O OE1 . GLU A 374 ? 0.4146 0.3476 0.2289 0.1199 -0.0720 -0.0044 367 GLU A OE1 2575 O OE2 . GLU A 374 ? 0.4087 0.3783 0.2474 0.1057 0.0543 0.0192 367 GLU A OE2 2576 N N . PRO A 375 ? 0.4008 0.2943 0.1643 0.1264 0.0679 0.0256 368 PRO A N 2577 C CA . PRO A 375 ? 0.3965 0.2853 0.1854 0.1127 0.0282 0.0273 368 PRO A CA 2578 C C . PRO A 375 ? 0.3661 0.2501 0.1755 0.1006 0.0041 0.0010 368 PRO A C 2579 O O . PRO A 375 ? 0.3579 0.2690 0.1755 0.1040 0.0323 -0.0005 368 PRO A O 2580 C CB . PRO A 375 ? 0.3843 0.2665 0.1971 0.1197 0.0261 0.0497 368 PRO A CB 2581 C CG . PRO A 375 ? 0.4007 0.2976 0.2239 0.0946 0.0339 0.0077 368 PRO A CG 2582 C CD . PRO A 375 ? 0.3433 0.2909 0.1782 0.1072 0.0626 0.0431 368 PRO A CD 2583 N N . ASP A 376 ? 0.3303 0.2733 0.1990 0.1224 0.0160 0.0285 369 ASP A N 2584 C CA . ASP A 376 ? 0.3184 0.2631 0.2212 0.1174 0.0303 0.0469 369 ASP A CA 2585 C C . ASP A 376 ? 0.3103 0.2376 0.1820 0.0962 0.0144 0.0000 369 ASP A C 2586 O O . ASP A 376 ? 0.3000 0.2419 0.1495 0.0915 0.0181 -0.0081 369 ASP A O 2587 C CB . ASP A 376 ? 0.3471 0.2151 0.2736 0.1182 0.0137 0.0518 369 ASP A CB 2588 C CG . ASP A 376 ? 0.3680 0.2673 0.2418 0.1189 0.0572 0.0255 369 ASP A CG 2589 O OD1 . ASP A 376 ? 0.3979 0.2744 0.3575 0.1290 0.0245 -0.0123 369 ASP A OD1 2590 O OD2 . ASP A 376 ? 0.4136 0.2719 0.3435 0.1426 0.0821 0.0382 369 ASP A OD2 2591 N N . ARG A 377 ? 0.3001 0.2286 0.1786 0.0870 0.0140 -0.0042 370 ARG A N 2592 C CA . ARG A 377 ? 0.2793 0.2175 0.1690 0.0829 0.0002 -0.0145 370 ARG A CA 2593 C C . ARG A 377 ? 0.2990 0.2145 0.1418 0.0866 0.0019 -0.0018 370 ARG A C 2594 O O . ARG A 377 ? 0.2724 0.2198 0.1600 0.0948 -0.0005 0.0118 370 ARG A O 2595 C CB . ARG A 377 ? 0.3126 0.2040 0.1937 0.0716 -0.0182 -0.0138 370 ARG A CB 2596 C CG . ARG A 377 ? 0.2998 0.1930 0.1665 0.0713 0.0032 0.0242 370 ARG A CG 2597 C CD . ARG A 377 ? 0.3216 0.2192 0.1434 0.1119 0.0091 0.0192 370 ARG A CD 2598 N NE . ARG A 377 ? 0.3141 0.2036 0.1840 0.0996 -0.0290 0.0157 370 ARG A NE 2599 C CZ . ARG A 377 ? 0.2830 0.2210 0.1605 0.0888 0.0147 -0.0345 370 ARG A CZ 2600 N NH1 . ARG A 377 ? 0.3035 0.2476 0.1305 0.0595 -0.0087 0.0155 370 ARG A NH1 2601 N NH2 . ARG A 377 ? 0.3381 0.2182 0.1399 0.0858 0.0132 -0.0092 370 ARG A NH2 2602 N N . TYR A 378 ? 0.2944 0.2171 0.1528 0.0698 0.0207 -0.0220 371 TYR A N 2603 C CA . TYR A 378 ? 0.2603 0.2078 0.1639 0.0801 0.0103 0.0009 371 TYR A CA 2604 C C . TYR A 378 ? 0.2623 0.2193 0.1602 0.0909 0.0204 -0.0032 371 TYR A C 2605 O O . TYR A 378 ? 0.2850 0.2296 0.2001 0.0481 -0.0065 0.0111 371 TYR A O 2606 C CB . TYR A 378 ? 0.2694 0.2356 0.1741 0.0567 -0.0013 0.0057 371 TYR A CB 2607 C CG . TYR A 378 ? 0.2578 0.2259 0.1551 0.0663 -0.0011 0.0320 371 TYR A CG 2608 C CD1 . TYR A 378 ? 0.2433 0.2539 0.1825 0.0357 0.0237 0.0210 371 TYR A CD1 2609 C CD2 . TYR A 378 ? 0.2604 0.1937 0.1494 0.0617 -0.0039 0.0303 371 TYR A CD2 2610 C CE1 . TYR A 378 ? 0.2537 0.2287 0.2156 0.0776 0.0093 0.0212 371 TYR A CE1 2611 C CE2 . TYR A 378 ? 0.2625 0.2419 0.2047 0.0640 0.0279 0.0006 371 TYR A CE2 2612 C CZ . TYR A 378 ? 0.2596 0.2373 0.2010 0.0634 0.0108 0.0140 371 TYR A CZ 2613 O OH . TYR A 378 ? 0.2592 0.2450 0.2368 0.0559 0.0194 0.0239 371 TYR A OH 2614 N N . VAL A 379 ? 0.2666 0.2243 0.1398 0.0892 0.0106 -0.0043 372 VAL A N 2615 C CA . VAL A 379 ? 0.2560 0.2058 0.1818 0.0794 -0.0002 -0.0261 372 VAL A CA 2616 C C . VAL A 379 ? 0.2662 0.2136 0.1463 0.0664 0.0086 -0.0173 372 VAL A C 2617 O O . VAL A 379 ? 0.2617 0.2217 0.1881 0.0535 -0.0141 -0.0150 372 VAL A O 2618 C CB . VAL A 379 ? 0.2692 0.2183 0.2122 0.0945 -0.0229 -0.0122 372 VAL A CB 2619 C CG1 . VAL A 379 ? 0.2705 0.2610 0.2258 0.1119 -0.0131 -0.0063 372 VAL A CG1 2620 C CG2 . VAL A 379 ? 0.2791 0.2454 0.1815 0.1003 -0.0274 -0.0360 372 VAL A CG2 2621 N N . ILE A 380 ? 0.2614 0.2068 0.1366 0.0715 -0.0114 -0.0237 373 ILE A N 2622 C CA . ILE A 380 ? 0.2309 0.2008 0.1413 0.0559 -0.0104 -0.0132 373 ILE A CA 2623 C C . ILE A 380 ? 0.2454 0.1947 0.1616 0.0564 0.0049 0.0015 373 ILE A C 2624 O O . ILE A 380 ? 0.2490 0.1956 0.1923 0.0454 -0.0050 -0.0025 373 ILE A O 2625 C CB . ILE A 380 ? 0.2276 0.1882 0.1413 0.0670 -0.0015 -0.0020 373 ILE A CB 2626 C CG1 . ILE A 380 ? 0.2255 0.2474 0.1899 0.0781 -0.0100 0.0227 373 ILE A CG1 2627 C CG2 . ILE A 380 ? 0.2241 0.2017 0.1747 0.0335 -0.0285 -0.0152 373 ILE A CG2 2628 C CD1 . ILE A 380 ? 0.2570 0.3197 0.2143 0.1048 -0.0325 0.0336 373 ILE A CD1 2629 N N . LEU A 381 ? 0.2214 0.1816 0.1958 0.0748 -0.0201 0.0053 374 LEU A N 2630 C CA . LEU A 381 ? 0.2305 0.2013 0.1670 0.0646 -0.0005 -0.0063 374 LEU A CA 2631 C C . LEU A 381 ? 0.2379 0.2134 0.1732 0.0426 -0.0058 0.0015 374 LEU A C 2632 O O . LEU A 381 ? 0.2558 0.1944 0.2088 0.0531 -0.0005 0.0083 374 LEU A O 2633 C CB . LEU A 381 ? 0.2140 0.2159 0.2037 0.0690 -0.0145 0.0111 374 LEU A CB 2634 C CG . LEU A 381 ? 0.2159 0.1945 0.1584 0.0654 -0.0350 0.0314 374 LEU A CG 2635 C CD1 . LEU A 381 ? 0.2406 0.2564 0.1882 0.0561 0.0178 0.0100 374 LEU A CD1 2636 C CD2 . LEU A 381 ? 0.2908 0.2372 0.1700 0.0810 -0.0458 0.0540 374 LEU A CD2 2637 N N . GLY A 382 ? 0.2525 0.2056 0.1544 0.0676 -0.0145 -0.0138 375 GLY A N 2638 C CA . GLY A 382 ? 0.2335 0.1996 0.1458 0.0385 0.0159 -0.0225 375 GLY A CA 2639 C C . GLY A 382 ? 0.1960 0.2050 0.2059 0.0467 0.0114 -0.0216 375 GLY A C 2640 O O . GLY A 382 ? 0.2400 0.2039 0.2118 0.0288 0.0494 -0.0182 375 GLY A O 2641 N N . GLY A 383 ? 0.1945 0.2032 0.1887 0.0532 0.0204 -0.0202 376 GLY A N 2642 C CA . GLY A 383 ? 0.2272 0.2050 0.1701 0.0352 0.0098 -0.0503 376 GLY A CA 2643 C C . GLY A 383 ? 0.2153 0.1846 0.2042 0.0173 0.0037 -0.0175 376 GLY A C 2644 O O . GLY A 383 ? 0.2129 0.2107 0.1838 0.0158 0.0055 -0.0087 376 GLY A O 2645 N N . HIS A 384 ? 0.2392 0.1891 0.1939 0.0187 -0.0213 -0.0242 377 HIS A N 2646 C CA . HIS A 384 ? 0.2259 0.1590 0.1794 0.0113 -0.0087 -0.0061 377 HIS A CA 2647 C C . HIS A 384 ? 0.2038 0.1778 0.2033 0.0160 0.0026 0.0140 377 HIS A C 2648 O O . HIS A 384 ? 0.2178 0.1990 0.2229 0.0353 -0.0015 0.0170 377 HIS A O 2649 C CB . HIS A 384 ? 0.1804 0.1782 0.1798 0.0312 0.0362 -0.0089 377 HIS A CB 2650 C CG . HIS A 384 ? 0.1751 0.1806 0.1943 0.0318 0.0315 -0.0090 377 HIS A CG 2651 N ND1 . HIS A 384 ? 0.1560 0.1927 0.2174 0.0406 0.0178 -0.0143 377 HIS A ND1 2652 C CD2 . HIS A 384 ? 0.1308 0.2081 0.2020 0.0647 0.0093 -0.0093 377 HIS A CD2 2653 C CE1 . HIS A 384 ? 0.1444 0.1992 0.1919 0.0319 -0.0073 -0.0134 377 HIS A CE1 2654 N NE2 . HIS A 384 ? 0.2026 0.1683 0.1676 0.0360 0.0258 -0.0169 377 HIS A NE2 2655 N N . ARG A 385 ? 0.1970 0.1575 0.2076 0.0104 0.0149 0.0095 378 ARG A N 2656 C CA . ARG A 385 ? 0.2083 0.1644 0.2017 0.0124 0.0240 0.0127 378 ARG A CA 2657 C C . ARG A 385 ? 0.2171 0.1717 0.2137 0.0245 0.0142 0.0065 378 ARG A C 2658 O O . ARG A 385 ? 0.2205 0.1806 0.2228 0.0392 0.0156 0.0012 378 ARG A O 2659 C CB . ARG A 385 ? 0.2135 0.1892 0.2442 0.0129 0.0400 0.0300 378 ARG A CB 2660 C CG . ARG A 385 ? 0.2361 0.1944 0.2340 0.0125 0.0533 0.0296 378 ARG A CG 2661 C CD . ARG A 385 ? 0.1722 0.2218 0.2420 0.0253 -0.0052 0.0197 378 ARG A CD 2662 N NE . ARG A 385 ? 0.2169 0.2179 0.2174 0.0215 -0.0036 0.0295 378 ARG A NE 2663 C CZ . ARG A 385 ? 0.2177 0.1786 0.2410 0.0072 -0.0092 -0.0084 378 ARG A CZ 2664 N NH1 . ARG A 385 ? 0.2216 0.1718 0.1958 0.0228 0.0313 0.0110 378 ARG A NH1 2665 N NH2 . ARG A 385 ? 0.2295 0.1973 0.2283 -0.0162 -0.0138 0.0172 378 ARG A NH2 2666 N N . ASP A 386 ? 0.2088 0.2033 0.2064 0.0367 0.0053 -0.0063 379 ASP A N 2667 C CA . ASP A 386 ? 0.1761 0.1887 0.2027 0.0440 0.0083 -0.0097 379 ASP A CA 2668 C C . ASP A 386 ? 0.1907 0.1772 0.2129 0.0181 0.0197 -0.0245 379 ASP A C 2669 O O . ASP A 386 ? 0.1782 0.1833 0.2202 0.0117 0.0160 -0.0112 379 ASP A O 2670 C CB . ASP A 386 ? 0.1693 0.1777 0.2242 0.0349 0.0058 0.0071 379 ASP A CB 2671 C CG . ASP A 386 ? 0.1951 0.1839 0.1899 0.0217 0.0151 -0.0085 379 ASP A CG 2672 O OD1 . ASP A 386 ? 0.1838 0.1613 0.2444 0.0159 -0.0063 -0.0229 379 ASP A OD1 2673 O OD2 . ASP A 386 ? 0.1789 0.2022 0.2014 0.0151 0.0315 -0.0173 379 ASP A OD2 2674 N N . SER A 387 ? 0.1783 0.1902 0.2251 0.0458 0.0183 -0.0239 380 SER A N 2675 C CA . SER A 387 ? 0.1763 0.1757 0.2168 0.0260 0.0181 -0.0284 380 SER A CA 2676 C C . SER A 387 ? 0.1842 0.2098 0.2201 0.0200 0.0154 -0.0274 380 SER A C 2677 O O . SER A 387 ? 0.1960 0.2253 0.2686 -0.0080 0.0206 -0.0236 380 SER A O 2678 C CB . SER A 387 ? 0.1994 0.1771 0.2355 0.0205 -0.0001 -0.0137 380 SER A CB 2679 O OG . SER A 387 ? 0.2326 0.1813 0.2434 0.0239 0.0189 -0.0051 380 SER A OG 2680 N N . TRP A 388 ? 0.2285 0.2266 0.2044 0.0151 0.0468 -0.0257 381 TRP A N 2681 C CA . TRP A 388 ? 0.2038 0.1782 0.2039 0.0134 0.0220 -0.0306 381 TRP A CA 2682 C C . TRP A 388 ? 0.2200 0.1881 0.2598 0.0170 0.0129 -0.0347 381 TRP A C 2683 O O . TRP A 388 ? 0.2066 0.2211 0.2130 0.0175 0.0068 -0.0175 381 TRP A O 2684 C CB . TRP A 388 ? 0.1779 0.1969 0.2550 -0.0018 0.0112 0.0000 381 TRP A CB 2685 C CG . TRP A 388 ? 0.1752 0.1886 0.2404 0.0077 0.0173 -0.0140 381 TRP A CG 2686 C CD1 . TRP A 388 ? 0.1903 0.1824 0.2422 0.0202 0.0261 -0.0153 381 TRP A CD1 2687 C CD2 . TRP A 388 ? 0.1747 0.1827 0.2215 -0.0101 0.0127 -0.0300 381 TRP A CD2 2688 N NE1 . TRP A 388 ? 0.1809 0.2186 0.2482 0.0203 -0.0051 -0.0234 381 TRP A NE1 2689 C CE2 . TRP A 388 ? 0.2060 0.1928 0.1911 -0.0047 0.0118 -0.0209 381 TRP A CE2 2690 C CE3 . TRP A 388 ? 0.1620 0.2147 0.1835 -0.0040 0.0052 -0.0312 381 TRP A CE3 2691 C CZ2 . TRP A 388 ? 0.1950 0.2274 0.1916 0.0036 0.0203 -0.0294 381 TRP A CZ2 2692 C CZ3 . TRP A 388 ? 0.2165 0.1867 0.2125 0.0076 0.0101 0.0069 381 TRP A CZ3 2693 C CH2 . TRP A 388 ? 0.2097 0.1775 0.2104 -0.0036 0.0553 -0.0240 381 TRP A CH2 2694 N N . VAL A 389 ? 0.2192 0.1846 0.2656 0.0263 0.0300 -0.0060 382 VAL A N 2695 C CA . VAL A 389 ? 0.2474 0.1815 0.2459 0.0458 0.0298 -0.0174 382 VAL A CA 2696 C C . VAL A 389 ? 0.2141 0.2260 0.2462 0.0495 0.0156 -0.0218 382 VAL A C 2697 O O . VAL A 389 ? 0.1901 0.2066 0.2622 0.0380 0.0148 -0.0080 382 VAL A O 2698 C CB . VAL A 389 ? 0.2003 0.1810 0.2682 0.0269 0.0361 0.0044 382 VAL A CB 2699 C CG1 . VAL A 389 ? 0.1928 0.1732 0.2852 0.0389 -0.0227 -0.0495 382 VAL A CG1 2700 C CG2 . VAL A 389 ? 0.2417 0.2610 0.2398 0.0286 0.0403 -0.0401 382 VAL A CG2 2701 N N . PHE A 390 ? 0.2379 0.1812 0.2546 0.0249 -0.0285 -0.0308 383 PHE A N 2702 C CA . PHE A 390 ? 0.2421 0.1622 0.2614 0.0443 0.0129 -0.0204 383 PHE A CA 2703 C C . PHE A 390 ? 0.2109 0.1842 0.2540 0.0241 -0.0021 -0.0285 383 PHE A C 2704 O O . PHE A 390 ? 0.2472 0.2144 0.2433 0.0085 0.0019 -0.0046 383 PHE A O 2705 C CB . PHE A 390 ? 0.2233 0.1749 0.2721 0.0432 0.0122 -0.0222 383 PHE A CB 2706 C CG . PHE A 390 ? 0.2459 0.1796 0.2914 0.0521 -0.0142 -0.0360 383 PHE A CG 2707 C CD1 . PHE A 390 ? 0.2523 0.1658 0.3022 0.0637 -0.0259 -0.0224 383 PHE A CD1 2708 C CD2 . PHE A 390 ? 0.2181 0.1930 0.3259 0.0771 -0.0091 -0.0421 383 PHE A CD2 2709 C CE1 . PHE A 390 ? 0.2429 0.2180 0.3159 0.0641 -0.0443 -0.0634 383 PHE A CE1 2710 C CE2 . PHE A 390 ? 0.2401 0.1708 0.2927 0.0519 -0.0209 -0.0083 383 PHE A CE2 2711 C CZ . PHE A 390 ? 0.2618 0.2068 0.3314 0.0291 -0.0052 0.0046 383 PHE A CZ 2712 N N . GLY A 391 ? 0.2432 0.1715 0.2572 0.0112 -0.0214 -0.0360 384 GLY A N 2713 C CA . GLY A 391 ? 0.1861 0.1787 0.2586 0.0243 -0.0116 -0.0436 384 GLY A CA 2714 C C . GLY A 391 ? 0.2148 0.1761 0.2435 0.0458 -0.0031 -0.0132 384 GLY A C 2715 O O . GLY A 391 ? 0.2194 0.2215 0.2417 0.0380 -0.0204 -0.0270 384 GLY A O 2716 N N . GLY A 392 ? 0.1951 0.1673 0.2859 0.0367 -0.0230 -0.0111 385 GLY A N 2717 C CA . GLY A 392 ? 0.2309 0.1880 0.2806 0.0248 -0.0294 0.0067 385 GLY A CA 2718 C C . GLY A 392 ? 0.2421 0.1909 0.2734 0.0323 0.0044 -0.0119 385 GLY A C 2719 O O . GLY A 392 ? 0.2386 0.2348 0.2674 0.0327 -0.0023 -0.0117 385 GLY A O 2720 N N . ILE A 393 ? 0.1942 0.1614 0.3226 0.0343 0.0266 -0.0153 386 ILE A N 2721 C CA . ILE A 393 ? 0.1849 0.1754 0.2671 0.0368 0.0140 -0.0367 386 ILE A CA 2722 C C . ILE A 393 ? 0.2143 0.2041 0.2552 0.0603 0.0108 -0.0219 386 ILE A C 2723 O O . ILE A 393 ? 0.2183 0.2022 0.2417 0.0608 0.0232 -0.0124 386 ILE A O 2724 C CB . ILE A 393 ? 0.1661 0.1642 0.2742 0.0421 0.0064 -0.0250 386 ILE A CB 2725 C CG1 . ILE A 393 ? 0.1736 0.2464 0.2993 0.0779 0.0191 -0.0293 386 ILE A CG1 2726 C CG2 . ILE A 393 ? 0.1898 0.1779 0.2865 0.0420 0.0047 -0.0417 386 ILE A CG2 2727 C CD1 . ILE A 393 ? 0.1765 0.2824 0.3505 0.0331 0.0038 0.0047 386 ILE A CD1 2728 N N . ASP A 394 ? 0.1984 0.2075 0.2695 0.0539 -0.0146 0.0030 387 ASP A N 2729 C CA . ASP A 394 ? 0.1853 0.1858 0.2373 0.0501 0.0112 -0.0041 387 ASP A CA 2730 C C . ASP A 394 ? 0.1921 0.2042 0.2436 0.0381 0.0082 -0.0189 387 ASP A C 2731 O O . ASP A 394 ? 0.2199 0.1848 0.2626 0.0399 0.0070 -0.0242 387 ASP A O 2732 C CB . ASP A 394 ? 0.1838 0.1900 0.2334 0.0369 0.0019 0.0060 387 ASP A CB 2733 C CG . ASP A 394 ? 0.2104 0.2118 0.2229 0.0436 -0.0034 0.0060 387 ASP A CG 2734 O OD1 . ASP A 394 ? 0.2250 0.2140 0.2267 0.0391 0.0129 -0.0014 387 ASP A OD1 2735 O OD2 . ASP A 394 ? 0.2460 0.2352 0.2204 0.0302 0.0272 0.0154 387 ASP A OD2 2736 N N . PRO A 395 ? 0.1966 0.1934 0.2266 0.0353 -0.0012 -0.0169 388 PRO A N 2737 C CA . PRO A 395 ? 0.1958 0.1938 0.2183 0.0539 0.0072 -0.0119 388 PRO A CA 2738 C C . PRO A 395 ? 0.1940 0.1751 0.2310 0.0421 -0.0107 -0.0058 388 PRO A C 2739 O O . PRO A 395 ? 0.2272 0.1853 0.2311 0.0407 0.0165 -0.0095 388 PRO A O 2740 C CB . PRO A 395 ? 0.1797 0.1576 0.2293 0.0301 0.0031 -0.0096 388 PRO A CB 2741 C CG . PRO A 395 ? 0.2200 0.1777 0.2084 0.0185 -0.0023 -0.0263 388 PRO A CG 2742 C CD . PRO A 395 ? 0.2016 0.2114 0.2444 0.0230 0.0115 -0.0241 388 PRO A CD 2743 N N . GLN A 396 ? 0.2139 0.1750 0.2462 0.0452 -0.0097 -0.0062 389 GLN A N 2744 C CA . GLN A 396 ? 0.2484 0.1725 0.2330 0.0183 -0.0119 -0.0059 389 GLN A CA 2745 C C . GLN A 396 ? 0.2488 0.2032 0.2305 0.0300 -0.0093 -0.0004 389 GLN A C 2746 O O . GLN A 396 ? 0.2620 0.1838 0.2244 0.0523 0.0068 0.0085 389 GLN A O 2747 C CB . GLN A 396 ? 0.2455 0.1767 0.2130 0.0336 0.0077 -0.0184 389 GLN A CB 2748 C CG . GLN A 396 ? 0.1905 0.2164 0.2517 0.0347 -0.0042 -0.0097 389 GLN A CG 2749 C CD . GLN A 396 ? 0.2118 0.2141 0.2521 0.0474 0.0221 -0.0078 389 GLN A CD 2750 O OE1 . GLN A 396 ? 0.2070 0.2058 0.2708 0.0201 0.0100 -0.0214 389 GLN A OE1 2751 N NE2 . GLN A 396 ? 0.2252 0.2253 0.2842 0.0358 0.0104 -0.0150 389 GLN A NE2 2752 N N . SER A 397 ? 0.2247 0.1904 0.2670 0.0520 -0.0139 -0.0135 390 SER A N 2753 C CA . SER A 397 ? 0.2260 0.2082 0.2632 0.0255 0.0083 -0.0207 390 SER A CA 2754 C C . SER A 397 ? 0.2441 0.2132 0.2337 0.0597 -0.0126 -0.0044 390 SER A C 2755 O O . SER A 397 ? 0.2486 0.2304 0.2322 0.0622 -0.0199 -0.0160 390 SER A O 2756 C CB . SER A 397 ? 0.2243 0.2188 0.2753 0.0469 0.0265 0.0376 390 SER A CB 2757 O OG . SER A 397 ? 0.2213 0.2143 0.2350 0.0471 0.0013 0.0123 390 SER A OG 2758 N N . GLY A 398 ? 0.2124 0.1914 0.2249 0.0497 -0.0041 -0.0068 391 GLY A N 2759 C CA . GLY A 398 ? 0.2031 0.1994 0.2209 0.0556 -0.0042 -0.0021 391 GLY A CA 2760 C C . GLY A 398 ? 0.2316 0.1996 0.2146 0.0400 -0.0027 0.0008 391 GLY A C 2761 O O . GLY A 398 ? 0.2400 0.2206 0.2115 0.0318 -0.0088 0.0051 391 GLY A O 2762 N N . ALA A 399 ? 0.2085 0.1781 0.2237 0.0385 0.0073 0.0196 392 ALA A N 2763 C CA . ALA A 399 ? 0.2185 0.1970 0.2192 0.0250 -0.0021 0.0131 392 ALA A CA 2764 C C . ALA A 399 ? 0.2388 0.2002 0.2097 0.0522 0.0028 -0.0033 392 ALA A C 2765 O O . ALA A 399 ? 0.2238 0.2104 0.2158 0.0564 0.0171 0.0230 392 ALA A O 2766 C CB . ALA A 399 ? 0.2488 0.1905 0.2422 0.0150 -0.0019 -0.0085 392 ALA A CB 2767 N N . ALA A 400 ? 0.2469 0.2109 0.2489 0.0608 -0.0294 0.0298 393 ALA A N 2768 C CA . ALA A 400 ? 0.2559 0.2076 0.2258 0.0884 -0.0276 0.0078 393 ALA A CA 2769 C C . ALA A 400 ? 0.2947 0.2137 0.2229 0.0627 -0.0031 0.0167 393 ALA A C 2770 O O . ALA A 400 ? 0.2839 0.2324 0.2088 0.0628 -0.0096 0.0135 393 ALA A O 2771 C CB . ALA A 400 ? 0.2541 0.2126 0.2489 0.0954 -0.0355 0.0075 393 ALA A CB 2772 N N . VAL A 401 ? 0.2661 0.2067 0.2281 0.0472 -0.0304 -0.0055 394 VAL A N 2773 C CA . VAL A 401 ? 0.2602 0.1878 0.2372 0.0616 0.0003 -0.0046 394 VAL A CA 2774 C C . VAL A 401 ? 0.2514 0.2240 0.2074 0.0777 -0.0165 0.0105 394 VAL A C 2775 O O . VAL A 401 ? 0.2846 0.2243 0.2002 0.0796 0.0133 0.0197 394 VAL A O 2776 C CB . VAL A 401 ? 0.2253 0.2013 0.2480 0.0478 -0.0033 -0.0173 394 VAL A CB 2777 C CG1 . VAL A 401 ? 0.2766 0.2076 0.2378 0.0485 -0.0058 -0.0230 394 VAL A CG1 2778 C CG2 . VAL A 401 ? 0.2346 0.2482 0.2794 0.0811 -0.0047 -0.0394 394 VAL A CG2 2779 N N . VAL A 402 ? 0.2364 0.2062 0.2117 0.0691 -0.0155 0.0132 395 VAL A N 2780 C CA . VAL A 402 ? 0.2359 0.1978 0.2001 0.0716 -0.0134 0.0242 395 VAL A CA 2781 C C . VAL A 402 ? 0.2831 0.2043 0.2057 0.0598 0.0036 0.0213 395 VAL A C 2782 O O . VAL A 402 ? 0.2472 0.1930 0.2310 0.0477 0.0218 0.0173 395 VAL A O 2783 C CB . VAL A 402 ? 0.2050 0.2183 0.2073 0.0739 -0.0047 0.0363 395 VAL A CB 2784 C CG1 . VAL A 402 ? 0.2463 0.2187 0.2538 0.1072 0.0111 -0.0346 395 VAL A CG1 2785 C CG2 . VAL A 402 ? 0.2727 0.2278 0.2245 0.0405 -0.0106 0.0452 395 VAL A CG2 2786 N N . HIS A 403 ? 0.2881 0.1961 0.2423 0.0499 0.0053 0.0331 396 HIS A N 2787 C CA . HIS A 403 ? 0.3041 0.1773 0.2325 0.0640 0.0193 0.0308 396 HIS A CA 2788 C C . HIS A 403 ? 0.3210 0.2236 0.2547 0.0681 0.0116 0.0188 396 HIS A C 2789 O O . HIS A 403 ? 0.3482 0.2619 0.2671 0.0912 0.0244 0.0501 396 HIS A O 2790 C CB . HIS A 403 ? 0.2897 0.1972 0.2638 0.0546 0.0236 0.0014 396 HIS A CB 2791 C CG . HIS A 403 ? 0.2956 0.2207 0.2829 0.0509 0.0250 0.0112 396 HIS A CG 2792 N ND1 . HIS A 403 ? 0.2922 0.2372 0.2706 0.0474 0.0508 0.0254 396 HIS A ND1 2793 C CD2 . HIS A 403 ? 0.3234 0.2377 0.2549 0.0347 0.0650 0.0365 396 HIS A CD2 2794 C CE1 . HIS A 403 ? 0.3095 0.1929 0.3170 0.0594 0.0622 0.0207 396 HIS A CE1 2795 N NE2 . HIS A 403 ? 0.3007 0.2208 0.3459 0.0746 0.0444 0.0207 396 HIS A NE2 2796 N N . GLU A 404 ? 0.3150 0.2237 0.2345 0.0716 -0.0124 0.0425 397 GLU A N 2797 C CA . GLU A 404 ? 0.3238 0.2481 0.2254 0.0883 -0.0071 0.0249 397 GLU A CA 2798 C C . GLU A 404 ? 0.3261 0.2374 0.2155 0.0811 -0.0155 0.0332 397 GLU A C 2799 O O . GLU A 404 ? 0.3289 0.2780 0.2338 0.0861 0.0266 0.0338 397 GLU A O 2800 C CB . GLU A 404 ? 0.3222 0.2738 0.2252 0.1054 -0.0245 -0.0006 397 GLU A CB 2801 C CG . GLU A 404 ? 0.3398 0.2401 0.2281 0.0570 -0.0350 0.0350 397 GLU A CG 2802 C CD . GLU A 404 ? 0.3748 0.3155 0.2594 0.0595 -0.0196 0.0721 397 GLU A CD 2803 O OE1 . GLU A 404 ? 0.3673 0.2712 0.2739 0.0969 0.0028 0.0162 397 GLU A OE1 2804 O OE2 . GLU A 404 ? 0.4422 0.2957 0.2352 0.0686 -0.0169 0.0137 397 GLU A OE2 2805 N N . ILE A 405 ? 0.3170 0.2105 0.2353 0.0849 -0.0164 0.0176 398 ILE A N 2806 C CA . ILE A 405 ? 0.3058 0.2159 0.2415 0.0905 -0.0152 0.0160 398 ILE A CA 2807 C C . ILE A 405 ? 0.3384 0.2256 0.2164 0.0710 0.0119 0.0325 398 ILE A C 2808 O O . ILE A 405 ? 0.3576 0.2464 0.2111 0.0837 -0.0116 0.0194 398 ILE A O 2809 C CB . ILE A 405 ? 0.2920 0.2073 0.2161 0.0897 0.0096 0.0029 398 ILE A CB 2810 C CG1 . ILE A 405 ? 0.3066 0.1886 0.1702 0.0340 -0.0032 0.0091 398 ILE A CG1 2811 C CG2 . ILE A 405 ? 0.2787 0.2165 0.2397 0.0960 -0.0066 -0.0045 398 ILE A CG2 2812 C CD1 . ILE A 405 ? 0.2913 0.2104 0.2024 0.0383 -0.0293 0.0530 398 ILE A CD1 2813 N N . VAL A 406 ? 0.3003 0.2367 0.2356 0.0773 0.0017 0.0339 399 VAL A N 2814 C CA . VAL A 406 ? 0.3365 0.2720 0.2087 0.0680 0.0351 0.0531 399 VAL A CA 2815 C C . VAL A 406 ? 0.3481 0.2545 0.2132 0.0917 0.0068 0.0484 399 VAL A C 2816 O O . VAL A 406 ? 0.3531 0.2974 0.2562 0.0834 0.0280 0.0318 399 VAL A O 2817 C CB . VAL A 406 ? 0.3011 0.2628 0.1954 0.0665 0.0354 0.0526 399 VAL A CB 2818 C CG1 . VAL A 406 ? 0.3245 0.2576 0.2117 0.0635 0.0698 0.0276 399 VAL A CG1 2819 C CG2 . VAL A 406 ? 0.3490 0.2412 0.2136 0.0949 -0.0031 0.0452 399 VAL A CG2 2820 N N . ARG A 407 ? 0.3779 0.2641 0.2082 0.1120 0.0441 0.0584 400 ARG A N 2821 C CA . ARG A 407 ? 0.3643 0.2523 0.2356 0.1114 0.0092 0.0656 400 ARG A CA 2822 C C . ARG A 407 ? 0.4146 0.2867 0.2192 0.1142 0.0220 0.0518 400 ARG A C 2823 O O . ARG A 407 ? 0.4253 0.3184 0.2310 0.1073 0.0224 0.0506 400 ARG A O 2824 C CB . ARG A 407 ? 0.4089 0.2328 0.2247 0.1136 0.0364 0.0799 400 ARG A CB 2825 C CG . ARG A 407 ? 0.3974 0.2232 0.2513 0.1126 0.0097 0.0938 400 ARG A CG 2826 C CD . ARG A 407 ? 0.3915 0.2785 0.2542 0.1319 -0.0093 0.1003 400 ARG A CD 2827 N NE . ARG A 407 ? 0.4140 0.3199 0.2342 0.1074 0.0147 0.0718 400 ARG A NE 2828 C CZ . ARG A 407 ? 0.4195 0.3565 0.2560 0.1391 -0.0132 0.0637 400 ARG A CZ 2829 N NH1 . ARG A 407 ? 0.4159 0.3727 0.2683 0.1332 -0.0012 0.0613 400 ARG A NH1 2830 N NH2 . ARG A 407 ? 0.4754 0.3312 0.3055 0.1099 0.0210 0.0659 400 ARG A NH2 2831 N N . SER A 408 ? 0.3807 0.2836 0.2236 0.1228 0.0109 0.0363 401 SER A N 2832 C CA . SER A 408 ? 0.4128 0.3087 0.2518 0.1054 -0.0016 0.0138 401 SER A CA 2833 C C . SER A 408 ? 0.4221 0.3036 0.2365 0.1181 -0.0012 0.0502 401 SER A C 2834 O O . SER A 408 ? 0.4499 0.3204 0.2365 0.1181 -0.0038 0.0357 401 SER A O 2835 C CB . SER A 408 ? 0.3966 0.3747 0.2408 0.0973 -0.0211 0.0183 401 SER A CB 2836 O OG . SER A 408 ? 0.4019 0.3698 0.2813 0.1387 -0.0020 -0.0044 401 SER A OG 2837 N N . PHE A 409 ? 0.3696 0.3149 0.2036 0.1105 -0.0009 0.0316 402 PHE A N 2838 C CA . PHE A 409 ? 0.4294 0.2838 0.2206 0.1232 -0.0086 0.0417 402 PHE A CA 2839 C C . PHE A 409 ? 0.4377 0.3119 0.2302 0.1335 0.0298 0.0219 402 PHE A C 2840 O O . PHE A 409 ? 0.4398 0.3533 0.2388 0.1265 0.0305 0.0007 402 PHE A O 2841 C CB . PHE A 409 ? 0.3865 0.2801 0.2481 0.1102 -0.0388 0.0438 402 PHE A CB 2842 C CG . PHE A 409 ? 0.3839 0.2713 0.1805 0.1109 -0.0222 0.0151 402 PHE A CG 2843 C CD1 . PHE A 409 ? 0.3459 0.2936 0.1842 0.0935 -0.0576 0.0032 402 PHE A CD1 2844 C CD2 . PHE A 409 ? 0.3384 0.2693 0.2122 0.0870 -0.0009 0.0448 402 PHE A CD2 2845 C CE1 . PHE A 409 ? 0.4051 0.2913 0.1682 0.0940 -0.0309 0.0337 402 PHE A CE1 2846 C CE2 . PHE A 409 ? 0.2882 0.2711 0.2102 0.0685 -0.0371 -0.0033 402 PHE A CE2 2847 C CZ . PHE A 409 ? 0.3287 0.2982 0.1792 0.0956 -0.0393 0.0015 402 PHE A CZ 2848 N N . GLY A 410 ? 0.4269 0.2963 0.2214 0.1330 0.0421 0.0385 403 GLY A N 2849 C CA . GLY A 410 ? 0.4323 0.3067 0.2461 0.1133 0.0417 0.0589 403 GLY A CA 2850 C C . GLY A 410 ? 0.4884 0.3030 0.2478 0.1218 0.0384 0.0537 403 GLY A C 2851 O O . GLY A 410 ? 0.4908 0.3518 0.2904 0.0956 0.0596 0.0228 403 GLY A O 2852 N N . THR A 411 ? 0.4857 0.3421 0.2623 0.1140 0.0490 0.0728 404 THR A N 2853 C CA . THR A 411 ? 0.4948 0.3139 0.2779 0.1509 0.0278 0.0670 404 THR A CA 2854 C C . THR A 411 ? 0.5109 0.3776 0.2443 0.1196 0.0267 0.0542 404 THR A C 2855 O O . THR A 411 ? 0.5320 0.4383 0.2468 0.1763 0.0386 0.0681 404 THR A O 2856 C CB . THR A 411 ? 0.4984 0.3495 0.3009 0.1443 0.0487 0.0585 404 THR A CB 2857 O OG1 A THR A 411 ? 0.5403 0.3451 0.3041 0.1456 0.0124 0.0488 404 THR A OG1 2858 O OG1 B THR A 411 ? 0.5223 0.3643 0.3012 0.1324 0.0168 -0.0020 404 THR A OG1 2859 C CG2 A THR A 411 ? 0.4523 0.3647 0.2972 0.1722 0.0798 0.0872 404 THR A CG2 2860 C CG2 B THR A 411 ? 0.5398 0.3616 0.2397 0.1265 0.0014 0.0648 404 THR A CG2 2861 N N . LEU A 412 ? 0.4911 0.3536 0.2578 0.1445 0.0177 0.0528 405 LEU A N 2862 C CA . LEU A 412 ? 0.5125 0.3765 0.2214 0.1495 0.0756 0.0681 405 LEU A CA 2863 C C . LEU A 412 ? 0.5058 0.3798 0.2202 0.1282 0.0549 0.0744 405 LEU A C 2864 O O . LEU A 412 ? 0.5179 0.3778 0.2036 0.1364 0.0484 0.0508 405 LEU A O 2865 C CB . LEU A 412 ? 0.5231 0.3863 0.2797 0.0837 -0.0152 0.0610 405 LEU A CB 2866 C CG A LEU A 412 ? 0.5190 0.4124 0.2661 0.0876 0.0011 0.0528 405 LEU A CG 2867 C CG B LEU A 412 ? 0.4743 0.3828 0.2868 0.1500 0.0297 0.0375 405 LEU A CG 2868 C CD1 A LEU A 412 ? 0.4977 0.4217 0.2100 0.0995 -0.0267 0.0530 405 LEU A CD1 2869 C CD1 B LEU A 412 ? 0.4662 0.3527 0.2570 0.1435 0.0224 0.0599 405 LEU A CD1 2870 C CD2 A LEU A 412 ? 0.5095 0.4356 0.3054 0.0718 -0.0186 0.0991 405 LEU A CD2 2871 C CD2 B LEU A 412 ? 0.4686 0.3910 0.3284 0.1697 0.0375 0.0555 405 LEU A CD2 2872 N N . LYS A 413 ? 0.5032 0.3494 0.2588 0.1398 0.0222 0.0700 406 LYS A N 2873 C CA . LYS A 413 ? 0.5054 0.3842 0.2140 0.1280 0.0608 0.0836 406 LYS A CA 2874 C C . LYS A 413 ? 0.5142 0.3656 0.2816 0.1621 0.0756 0.1052 406 LYS A C 2875 O O . LYS A 413 ? 0.5548 0.3911 0.2876 0.1494 0.0865 0.0626 406 LYS A O 2876 C CB . LYS A 413 ? 0.5443 0.3896 0.2558 0.1134 0.0163 0.0491 406 LYS A CB 2877 C CG . LYS A 413 ? 0.5551 0.3973 0.4592 0.1166 0.0796 0.0616 406 LYS A CG 2878 C CD . LYS A 413 ? 0.5545 0.4854 0.4680 0.0967 0.0200 0.0385 406 LYS A CD 2879 C CE . LYS A 413 ? 0.5443 0.4556 0.4978 0.1260 0.0152 -0.0235 406 LYS A CE 2880 N NZ . LYS A 413 ? 0.5968 0.5810 0.5580 0.0144 0.0383 0.0132 406 LYS A NZ 2881 N N . LYS A 414 ? 0.5023 0.3586 0.2916 0.1493 0.0480 0.0787 407 LYS A N 2882 C CA . LYS A 414 ? 0.5548 0.3960 0.3011 0.1480 0.0664 0.0958 407 LYS A CA 2883 C C . LYS A 414 ? 0.5967 0.4127 0.3016 0.1489 0.0221 0.1422 407 LYS A C 2884 O O . LYS A 414 ? 0.7167 0.4757 0.2643 0.1136 0.0484 0.1055 407 LYS A O 2885 C CB . LYS A 414 ? 0.5552 0.4047 0.3407 0.1502 0.0643 0.0787 407 LYS A CB 2886 C CG . LYS A 414 ? 0.5817 0.4210 0.3012 0.0922 0.1436 0.0980 407 LYS A CG 2887 C CD . LYS A 414 ? 0.6423 0.4243 0.3146 0.1155 0.0499 0.0634 407 LYS A CD 2888 C CE . LYS A 414 ? 0.6111 0.4042 0.2773 0.1039 0.0879 0.0939 407 LYS A CE 2889 N NZ . LYS A 414 ? 0.6601 0.4552 0.3227 0.1190 0.0719 0.0466 407 LYS A NZ 2890 N N . GLU A 415 ? 0.6089 0.3679 0.2988 0.1556 0.0643 0.0776 408 GLU A N 2891 C CA . GLU A 415 ? 0.6346 0.4251 0.3096 0.1671 0.0016 0.0749 408 GLU A CA 2892 C C . GLU A 415 ? 0.5906 0.4847 0.2540 0.1641 0.0410 0.0626 408 GLU A C 2893 O O . GLU A 415 ? 0.7261 0.4783 0.2887 0.1246 0.0054 0.0445 408 GLU A O 2894 C CB . GLU A 415 ? 0.6343 0.4414 0.3327 0.1652 0.0233 0.0266 408 GLU A CB 2895 C CG . GLU A 415 ? 0.6461 0.4779 0.4944 0.2083 -0.0723 -0.0207 408 GLU A CG 2896 C CD . GLU A 415 ? 0.6631 0.5073 0.6014 0.2005 -0.0384 0.0118 408 GLU A CD 2897 O OE1 . GLU A 415 ? 0.6128 0.5463 0.6662 0.1897 -0.2000 0.1260 408 GLU A OE1 2898 O OE2 . GLU A 415 ? 0.8002 0.5458 0.5860 0.1351 -0.1426 0.0330 408 GLU A OE2 2899 N N . GLY A 416 ? 0.6223 0.4213 0.2265 0.1818 0.0687 0.0697 409 GLY A N 2900 C CA . GLY A 416 ? 0.6581 0.4087 0.2385 0.1742 0.0377 0.0486 409 GLY A CA 2901 C C . GLY A 416 ? 0.5865 0.4183 0.2937 0.1538 0.0598 0.0347 409 GLY A C 2902 O O . GLY A 416 ? 0.5563 0.4382 0.2630 0.1539 0.0763 0.0406 409 GLY A O 2903 N N . TRP A 417 ? 0.5751 0.3841 0.2113 0.1352 0.0177 0.0549 410 TRP A N 2904 C CA . TRP A 417 ? 0.5355 0.3986 0.2160 0.1846 0.0228 0.0933 410 TRP A CA 2905 C C . TRP A 417 ? 0.5004 0.3475 0.2123 0.1697 0.0297 0.0811 410 TRP A C 2906 O O . TRP A 417 ? 0.5784 0.3504 0.2552 0.1307 0.0226 0.0833 410 TRP A O 2907 C CB . TRP A 417 ? 0.5261 0.4251 0.2558 0.1683 0.0077 0.0760 410 TRP A CB 2908 C CG . TRP A 417 ? 0.5110 0.3975 0.2897 0.1690 -0.0432 0.0864 410 TRP A CG 2909 C CD1 . TRP A 417 ? 0.5007 0.4138 0.3518 0.1519 -0.0739 0.0782 410 TRP A CD1 2910 C CD2 . TRP A 417 ? 0.5112 0.3889 0.2912 0.1664 0.0023 0.0368 410 TRP A CD2 2911 N NE1 . TRP A 417 ? 0.4774 0.4100 0.3020 0.1460 -0.0824 0.0550 410 TRP A NE1 2912 C CE2 . TRP A 417 ? 0.5243 0.3934 0.2838 0.1649 -0.0407 0.0676 410 TRP A CE2 2913 C CE3 . TRP A 417 ? 0.5075 0.3718 0.2864 0.1645 -0.0157 0.0632 410 TRP A CE3 2914 C CZ2 . TRP A 417 ? 0.3884 0.3394 0.2806 0.1878 0.0272 0.0096 410 TRP A CZ2 2915 C CZ3 . TRP A 417 ? 0.4522 0.3763 0.2687 0.1778 -0.0564 0.0679 410 TRP A CZ3 2916 C CH2 . TRP A 417 ? 0.4055 0.3760 0.2734 0.1837 0.0044 0.0219 410 TRP A CH2 2917 N N . ARG A 418 ? 0.5148 0.3281 0.2081 0.1916 0.0258 0.0461 411 ARG A N 2918 C CA . ARG A 418 ? 0.4558 0.3333 0.2230 0.1623 0.0227 0.0764 411 ARG A CA 2919 C C . ARG A 418 ? 0.4104 0.3543 0.1746 0.1414 0.0007 0.0414 411 ARG A C 2920 O O . ARG A 418 ? 0.4920 0.3378 0.1900 0.1546 -0.0127 0.0267 411 ARG A O 2921 C CB . ARG A 418 ? 0.4299 0.4096 0.2625 0.1391 0.0219 0.0497 411 ARG A CB 2922 C CG . ARG A 418 ? 0.4904 0.4082 0.3305 0.1352 0.0071 0.0286 411 ARG A CG 2923 C CD . ARG A 418 ? 0.4957 0.4001 0.2810 0.1516 -0.0039 -0.0288 411 ARG A CD 2924 N NE . ARG A 418 ? 0.5457 0.4176 0.2395 0.1251 -0.0001 0.0362 411 ARG A NE 2925 C CZ . ARG A 418 ? 0.5059 0.4026 0.2665 0.0788 0.0361 0.0121 411 ARG A CZ 2926 N NH1 . ARG A 418 ? 0.4632 0.2865 0.2425 0.1236 -0.0097 0.0384 411 ARG A NH1 2927 N NH2 . ARG A 418 ? 0.4696 0.3576 0.2970 0.0947 0.0533 0.0750 411 ARG A NH2 2928 N N . PRO A 419 ? 0.3759 0.3053 0.1688 0.1421 0.0149 0.0169 412 PRO A N 2929 C CA . PRO A 419 ? 0.4447 0.2919 0.1689 0.1323 0.0096 0.0090 412 PRO A CA 2930 C C . PRO A 419 ? 0.4042 0.2929 0.1469 0.1204 0.0021 0.0119 412 PRO A C 2931 O O . PRO A 419 ? 0.3977 0.3098 0.2014 0.1315 0.0073 0.0346 412 PRO A O 2932 C CB . PRO A 419 ? 0.4049 0.2694 0.1574 0.1205 0.0068 0.0181 412 PRO A CB 2933 C CG . PRO A 419 ? 0.3999 0.2891 0.1389 0.1096 -0.0319 0.0503 412 PRO A CG 2934 C CD . PRO A 419 ? 0.4082 0.2857 0.1228 0.1246 0.0061 0.0321 412 PRO A CD 2935 N N . ARG A 420 ? 0.4173 0.2748 0.1751 0.1241 -0.0076 0.0129 413 ARG A N 2936 C CA . ARG A 420 ? 0.3941 0.2854 0.1641 0.1292 -0.0057 0.0119 413 ARG A CA 2937 C C . ARG A 420 ? 0.3836 0.3313 0.1625 0.1154 -0.0024 -0.0044 413 ARG A C 2938 O O . ARG A 420 ? 0.3804 0.3395 0.1417 0.1193 -0.0110 0.0093 413 ARG A O 2939 C CB . ARG A 420 ? 0.3597 0.2808 0.1601 0.1419 0.0320 -0.0215 413 ARG A CB 2940 C CG . ARG A 420 ? 0.4157 0.2551 0.2070 0.1359 -0.0288 -0.0591 413 ARG A CG 2941 C CD . ARG A 420 ? 0.4597 0.2919 0.2598 0.1147 0.0515 -0.0184 413 ARG A CD 2942 N NE . ARG A 420 ? 0.4852 0.3293 0.2486 0.1498 0.0063 -0.0572 413 ARG A NE 2943 C CZ . ARG A 420 ? 0.5795 0.3813 0.2070 0.1759 -0.0271 -0.0513 413 ARG A CZ 2944 N NH1 . ARG A 420 ? 0.5605 0.3652 0.1681 0.1687 -0.0147 -0.0834 413 ARG A NH1 2945 N NH2 . ARG A 420 ? 0.4979 0.3991 0.2977 0.1715 -0.0616 -0.1086 413 ARG A NH2 2946 N N . ARG A 421 ? 0.3646 0.2873 0.1150 0.1169 -0.0425 -0.0104 414 ARG A N 2947 C CA . ARG A 421 ? 0.3567 0.2594 0.1246 0.0986 -0.0493 0.0037 414 ARG A CA 2948 C C . ARG A 421 ? 0.3462 0.2573 0.1204 0.1134 -0.0132 0.0027 414 ARG A C 2949 O O . ARG A 421 ? 0.3468 0.2686 0.1628 0.1151 -0.0297 0.0159 414 ARG A O 2950 C CB . ARG A 421 ? 0.3544 0.2346 0.1664 0.0660 -0.0459 -0.0315 414 ARG A CB 2951 C CG . ARG A 421 ? 0.3715 0.2177 0.1676 0.0782 -0.0439 -0.0232 414 ARG A CG 2952 C CD . ARG A 421 ? 0.3509 0.2673 0.1624 0.0723 -0.0218 -0.0298 414 ARG A CD 2953 N NE . ARG A 421 ? 0.3723 0.2698 0.1624 0.1129 -0.0297 -0.0415 414 ARG A NE 2954 C CZ . ARG A 421 ? 0.3307 0.2163 0.2279 0.0882 -0.0387 -0.0018 414 ARG A CZ 2955 N NH1 . ARG A 421 ? 0.3007 0.2715 0.1299 0.1092 0.0162 -0.0008 414 ARG A NH1 2956 N NH2 . ARG A 421 ? 0.3999 0.2549 0.2063 0.1168 -0.0609 -0.0280 414 ARG A NH2 2957 N N . THR A 422 ? 0.3242 0.2403 0.1239 0.0998 -0.0093 -0.0139 415 THR A N 2958 C CA . THR A 422 ? 0.3288 0.2556 0.1520 0.0808 -0.0019 -0.0260 415 THR A CA 2959 C C . THR A 422 ? 0.3227 0.2316 0.1835 0.0877 0.0095 0.0009 415 THR A C 2960 O O . THR A 422 ? 0.3152 0.2585 0.1728 0.0985 0.0109 0.0106 415 THR A O 2961 C CB . THR A 422 ? 0.2987 0.2424 0.1630 0.0952 0.0201 -0.0093 415 THR A CB 2962 O OG1 . THR A 422 ? 0.2810 0.2718 0.1808 0.0917 0.0244 0.0246 415 THR A OG1 2963 C CG2 . THR A 422 ? 0.3341 0.2228 0.1516 0.0907 0.0297 0.0025 415 THR A CG2 2964 N N . ILE A 423 ? 0.2707 0.2340 0.1515 0.1039 0.0143 0.0141 416 ILE A N 2965 C CA . ILE A 423 ? 0.2820 0.2510 0.1427 0.0894 0.0204 0.0158 416 ILE A CA 2966 C C . ILE A 423 ? 0.2869 0.2484 0.1501 0.0753 0.0189 0.0269 416 ILE A C 2967 O O . ILE A 423 ? 0.3049 0.2417 0.1561 0.0846 0.0132 0.0221 416 ILE A O 2968 C CB . ILE A 423 ? 0.2559 0.2480 0.1423 0.0973 0.0196 -0.0162 416 ILE A CB 2969 C CG1 . ILE A 423 ? 0.2987 0.2462 0.1576 0.0951 -0.0176 0.0203 416 ILE A CG1 2970 C CG2 . ILE A 423 ? 0.2656 0.2467 0.1769 0.0955 0.0537 0.0090 416 ILE A CG2 2971 C CD1 . ILE A 423 ? 0.3018 0.2737 0.1814 0.0879 -0.0459 0.0233 416 ILE A CD1 2972 N N . LEU A 424 ? 0.2827 0.2156 0.1313 0.0870 -0.0101 0.0110 417 LEU A N 2973 C CA . LEU A 424 ? 0.2728 0.1973 0.1757 0.0731 -0.0024 0.0145 417 LEU A CA 2974 C C . LEU A 424 ? 0.2653 0.2076 0.1781 0.0515 0.0241 0.0137 417 LEU A C 2975 O O . LEU A 424 ? 0.2803 0.1881 0.2180 0.0414 0.0301 0.0112 417 LEU A O 2976 C CB . LEU A 424 ? 0.2342 0.2066 0.1783 0.0745 0.0112 0.0282 417 LEU A CB 2977 C CG . LEU A 424 ? 0.2416 0.2364 0.2120 0.0859 0.0448 0.0462 417 LEU A CG 2978 C CD1 . LEU A 424 ? 0.2401 0.2109 0.2016 0.0314 0.0259 0.0495 417 LEU A CD1 2979 C CD2 . LEU A 424 ? 0.1928 0.2896 0.2460 0.0730 0.0443 0.0401 417 LEU A CD2 2980 N N . PHE A 425 ? 0.2590 0.1983 0.2046 0.0688 0.0297 0.0082 418 PHE A N 2981 C CA . PHE A 425 ? 0.2624 0.1838 0.1477 0.0592 0.0164 0.0167 418 PHE A CA 2982 C C . PHE A 425 ? 0.2521 0.2142 0.1528 0.0433 0.0126 0.0253 418 PHE A C 2983 O O . PHE A 425 ? 0.2656 0.2361 0.1706 0.0325 0.0058 -0.0015 418 PHE A O 2984 C CB . PHE A 425 ? 0.2828 0.1944 0.1733 0.0536 0.0145 0.0335 418 PHE A CB 2985 C CG . PHE A 425 ? 0.2899 0.2182 0.1619 0.0680 0.0168 0.0198 418 PHE A CG 2986 C CD1 . PHE A 425 ? 0.3029 0.2105 0.2184 0.0499 0.0023 0.0232 418 PHE A CD1 2987 C CD2 . PHE A 425 ? 0.3046 0.2451 0.1874 0.0403 0.0453 0.0245 418 PHE A CD2 2988 C CE1 . PHE A 425 ? 0.3169 0.2190 0.2128 0.0961 0.0108 -0.0061 418 PHE A CE1 2989 C CE2 . PHE A 425 ? 0.3051 0.2581 0.1993 0.0795 0.0125 0.0337 418 PHE A CE2 2990 C CZ . PHE A 425 ? 0.3124 0.2319 0.2224 0.0769 0.0190 0.0277 418 PHE A CZ 2991 N N . ALA A 426 ? 0.2471 0.2239 0.1538 0.0509 0.0147 0.0132 419 ALA A N 2992 C CA . ALA A 426 ? 0.2565 0.1776 0.1531 0.0426 0.0199 0.0194 419 ALA A CA 2993 C C . ALA A 426 ? 0.2368 0.1835 0.1862 0.0434 0.0157 0.0148 419 ALA A C 2994 O O . ALA A 426 ? 0.2464 0.1909 0.2165 0.0218 0.0121 -0.0162 419 ALA A O 2995 C CB . ALA A 426 ? 0.2582 0.2014 0.1845 0.0413 0.0075 0.0425 419 ALA A CB 2996 N N A SER A 427 ? 0.2429 0.1590 0.1935 0.0478 0.0284 0.0063 420 SER A N 2997 N N B SER A 427 ? 0.2519 0.1769 0.2015 0.0388 0.0215 0.0097 420 SER A N 2998 C CA A SER A 427 ? 0.2374 0.1488 0.1961 0.0475 0.0293 0.0125 420 SER A CA 2999 C CA B SER A 427 ? 0.2365 0.1811 0.1988 0.0351 0.0195 0.0092 420 SER A CA 3000 C C A SER A 427 ? 0.1940 0.1638 0.1918 0.0242 0.0298 0.0057 420 SER A C 3001 C C B SER A 427 ? 0.2090 0.1638 0.1905 0.0297 0.0307 0.0107 420 SER A C 3002 O O A SER A 427 ? 0.1953 0.1815 0.1869 0.0263 0.0080 0.0253 420 SER A O 3003 O O B SER A 427 ? 0.2357 0.1511 0.2011 0.0287 0.0148 -0.0030 420 SER A O 3004 C CB A SER A 427 ? 0.2107 0.1313 0.1970 0.0308 0.0394 -0.0207 420 SER A CB 3005 C CB B SER A 427 ? 0.2452 0.1879 0.2668 0.0241 0.0053 0.0276 420 SER A CB 3006 O OG A SER A 427 ? 0.1632 0.1219 0.1820 0.0502 0.0354 -0.0064 420 SER A OG 3007 O OG B SER A 427 ? 0.2585 0.2738 0.2651 -0.0079 0.0016 0.0244 420 SER A OG 3008 N N . TRP A 428 ? 0.2130 0.1639 0.1641 0.0383 0.0181 0.0150 421 TRP A N 3009 C CA . TRP A 428 ? 0.2127 0.1436 0.1655 0.0172 0.0047 0.0117 421 TRP A CA 3010 C C . TRP A 428 ? 0.2229 0.1678 0.1754 0.0093 -0.0068 -0.0026 421 TRP A C 3011 O O . TRP A 428 ? 0.2264 0.1998 0.2019 0.0152 -0.0045 -0.0122 421 TRP A O 3012 C CB . TRP A 428 ? 0.2121 0.1446 0.1543 0.0059 0.0211 -0.0053 421 TRP A CB 3013 C CG . TRP A 428 ? 0.1988 0.1515 0.1712 0.0187 0.0055 -0.0077 421 TRP A CG 3014 C CD1 . TRP A 428 ? 0.1843 0.1575 0.1550 0.0236 0.0107 0.0058 421 TRP A CD1 3015 C CD2 . TRP A 428 ? 0.1777 0.1827 0.1574 0.0000 0.0345 0.0065 421 TRP A CD2 3016 N NE1 . TRP A 428 ? 0.2060 0.1911 0.1482 0.0540 0.0147 -0.0003 421 TRP A NE1 3017 C CE2 . TRP A 428 ? 0.1960 0.1787 0.1570 0.0206 0.0320 -0.0003 421 TRP A CE2 3018 C CE3 . TRP A 428 ? 0.1842 0.1725 0.1722 0.0397 0.0343 0.0492 421 TRP A CE3 3019 C CZ2 . TRP A 428 ? 0.1951 0.1801 0.1740 0.0562 0.0008 0.0129 421 TRP A CZ2 3020 C CZ3 . TRP A 428 ? 0.2102 0.1722 0.1925 0.0185 0.0230 -0.0033 421 TRP A CZ3 3021 C CH2 . TRP A 428 ? 0.2116 0.1825 0.2078 -0.0080 0.0058 0.0130 421 TRP A CH2 3022 N N . ASP A 429 ? 0.2206 0.1770 0.1811 0.0073 -0.0136 -0.0132 422 ASP A N 3023 C CA . ASP A 429 ? 0.1870 0.1675 0.1754 -0.0105 -0.0025 -0.0099 422 ASP A CA 3024 C C . ASP A 429 ? 0.1833 0.1661 0.1942 -0.0118 0.0194 -0.0088 422 ASP A C 3025 O O . ASP A 429 ? 0.2249 0.1770 0.1818 -0.0053 0.0105 -0.0111 422 ASP A O 3026 C CB . ASP A 429 ? 0.1736 0.1664 0.2269 -0.0062 0.0141 -0.0234 422 ASP A CB 3027 C CG . ASP A 429 ? 0.1856 0.1547 0.2472 0.0106 0.0173 -0.0064 422 ASP A CG 3028 O OD1 . ASP A 429 ? 0.1772 0.2061 0.2420 0.0239 -0.0007 0.0080 422 ASP A OD1 3029 O OD2 . ASP A 429 ? 0.1905 0.1902 0.2687 -0.0043 -0.0024 -0.0219 422 ASP A OD2 3030 N N . ALA A 430 ? 0.1755 0.1906 0.1853 0.0002 0.0229 -0.0047 423 ALA A N 3031 C CA . ALA A 430 ? 0.1770 0.1808 0.1909 -0.0076 0.0208 0.0105 423 ALA A CA 3032 C C . ALA A 430 ? 0.1707 0.1675 0.1937 -0.0027 0.0065 -0.0222 423 ALA A C 3033 O O . ALA A 430 ? 0.1869 0.1857 0.2002 -0.0050 0.0097 -0.0138 423 ALA A O 3034 C CB . ALA A 430 ? 0.1797 0.2166 0.1963 -0.0073 0.0033 -0.0076 423 ALA A CB 3035 N N . ALA A 431 ? 0.1877 0.1634 0.1907 0.0151 0.0049 -0.0225 424 ALA A N 3036 C CA . ALA A 431 ? 0.1797 0.1775 0.1696 0.0004 0.0072 -0.0127 424 ALA A CA 3037 C C . ALA A 431 ? 0.1936 0.1772 0.1869 0.0201 0.0125 -0.0211 424 ALA A C 3038 O O . ALA A 431 ? 0.1898 0.1852 0.1893 0.0197 0.0273 -0.0230 424 ALA A O 3039 C CB . ALA A 431 ? 0.2038 0.1903 0.1816 0.0247 -0.0105 -0.0368 424 ALA A CB 3040 N N . GLU A 432 ? 0.2081 0.1771 0.1934 0.0141 0.0178 -0.0303 425 GLU A N 3041 C CA . GLU A 432 ? 0.1816 0.1644 0.2012 0.0327 0.0210 -0.0288 425 GLU A CA 3042 C C . GLU A 432 ? 0.1812 0.1735 0.2009 0.0249 0.0150 -0.0271 425 GLU A C 3043 O O . GLU A 432 ? 0.1911 0.1840 0.2034 0.0204 0.0238 -0.0382 425 GLU A O 3044 C CB . GLU A 432 ? 0.1716 0.1558 0.1804 0.0214 0.0097 -0.0090 425 GLU A CB 3045 C CG . GLU A 432 ? 0.1447 0.1714 0.2136 -0.0084 -0.0252 -0.0110 425 GLU A CG 3046 C CD . GLU A 432 ? 0.1483 0.1713 0.2217 -0.0260 0.0096 -0.0600 425 GLU A CD 3047 O OE1 . GLU A 432 ? 0.2017 0.1837 0.2632 0.0199 0.0268 -0.0092 425 GLU A OE1 3048 O OE2 . GLU A 432 ? 0.2004 0.1827 0.2430 0.0396 0.0064 -0.0190 425 GLU A OE2 3049 N N . PHE A 433 ? 0.1787 0.1611 0.2086 0.0017 0.0176 -0.0409 426 PHE A N 3050 C CA . PHE A 433 ? 0.1850 0.1589 0.2065 -0.0184 0.0140 -0.0316 426 PHE A CA 3051 C C . PHE A 433 ? 0.1842 0.1751 0.1948 0.0141 0.0160 -0.0398 426 PHE A C 3052 O O . PHE A 433 ? 0.1958 0.1821 0.1846 -0.0051 0.0140 -0.0226 426 PHE A O 3053 C CB . PHE A 433 ? 0.1794 0.1651 0.2232 -0.0193 0.0081 -0.0338 426 PHE A CB 3054 C CG . PHE A 433 ? 0.1466 0.1659 0.2130 -0.0066 0.0324 -0.0246 426 PHE A CG 3055 C CD1 . PHE A 433 ? 0.1544 0.1968 0.2197 0.0075 0.0568 -0.0348 426 PHE A CD1 3056 C CD2 . PHE A 433 ? 0.1956 0.1773 0.2424 0.0042 -0.0019 -0.0123 426 PHE A CD2 3057 C CE1 . PHE A 433 ? 0.1954 0.1622 0.2563 0.0068 0.0152 -0.0081 426 PHE A CE1 3058 C CE2 . PHE A 433 ? 0.1641 0.1969 0.2095 -0.0077 0.0272 -0.0447 426 PHE A CE2 3059 C CZ . PHE A 433 ? 0.2262 0.2044 0.1979 -0.0237 0.0009 -0.0123 426 PHE A CZ 3060 N N . GLY A 434 ? 0.1948 0.1579 0.1849 -0.0046 0.0203 -0.0261 427 GLY A N 3061 C CA . GLY A 434 ? 0.1888 0.1629 0.1549 0.0174 0.0110 -0.0212 427 GLY A CA 3062 C C . GLY A 434 ? 0.1728 0.1845 0.1718 0.0115 0.0205 -0.0207 427 GLY A C 3063 O O . GLY A 434 ? 0.1836 0.1904 0.1984 0.0125 -0.0014 -0.0099 427 GLY A O 3064 N N . LEU A 435 ? 0.1381 0.1768 0.1565 -0.0111 0.0070 -0.0225 428 LEU A N 3065 C CA . LEU A 435 ? 0.1502 0.1813 0.1783 -0.0339 0.0287 -0.0301 428 LEU A CA 3066 C C . LEU A 435 ? 0.1453 0.1657 0.1752 0.0072 0.0075 -0.0229 428 LEU A C 3067 O O . LEU A 435 ? 0.1579 0.1885 0.1835 0.0166 0.0155 -0.0303 428 LEU A O 3068 C CB . LEU A 435 ? 0.1236 0.1721 0.2017 -0.0166 0.0224 -0.0050 428 LEU A CB 3069 C CG . LEU A 435 ? 0.1062 0.1646 0.2015 0.0095 0.0118 -0.0161 428 LEU A CG 3070 C CD1 . LEU A 435 ? 0.2056 0.1659 0.2364 -0.0007 0.0424 -0.0124 428 LEU A CD1 3071 C CD2 . LEU A 435 ? 0.1995 0.1911 0.2038 0.0198 -0.0262 0.0028 428 LEU A CD2 3072 N N . LEU A 436 ? 0.1660 0.1936 0.1615 -0.0329 -0.0114 0.0009 429 LEU A N 3073 C CA . LEU A 436 ? 0.1614 0.1905 0.1770 -0.0042 0.0173 -0.0200 429 LEU A CA 3074 C C . LEU A 436 ? 0.1797 0.1843 0.1865 0.0116 0.0234 -0.0010 429 LEU A C 3075 O O . LEU A 436 ? 0.1749 0.1934 0.1942 0.0280 0.0007 -0.0017 429 LEU A O 3076 C CB . LEU A 436 ? 0.1830 0.2043 0.1520 -0.0026 0.0226 -0.0247 429 LEU A CB 3077 C CG . LEU A 436 ? 0.1933 0.1602 0.1432 -0.0146 0.0173 -0.0203 429 LEU A CG 3078 C CD1 . LEU A 436 ? 0.1725 0.1955 0.2036 -0.0110 0.0022 -0.0597 429 LEU A CD1 3079 C CD2 . LEU A 436 ? 0.2326 0.1838 0.2148 -0.0204 -0.0183 0.0155 429 LEU A CD2 3080 N N . GLY A 437 ? 0.1559 0.2271 0.1656 0.0019 -0.0041 0.0094 430 GLY A N 3081 C CA . GLY A 437 ? 0.1939 0.1839 0.1744 0.0302 0.0285 -0.0185 430 GLY A CA 3082 C C . GLY A 437 ? 0.1753 0.1611 0.1779 0.0127 0.0205 -0.0028 430 GLY A C 3083 O O . GLY A 437 ? 0.1729 0.1830 0.2145 0.0157 0.0155 -0.0116 430 GLY A O 3084 N N . SER A 438 ? 0.1921 0.1681 0.1838 0.0081 0.0075 -0.0099 431 SER A N 3085 C CA . SER A 438 ? 0.1739 0.1613 0.1911 0.0072 -0.0123 -0.0093 431 SER A CA 3086 C C . SER A 438 ? 0.1775 0.1663 0.1702 0.0182 0.0164 -0.0034 431 SER A C 3087 O O . SER A 438 ? 0.1726 0.1597 0.1808 0.0278 0.0203 0.0021 431 SER A O 3088 C CB . SER A 438 ? 0.1672 0.1813 0.1684 0.0112 0.0192 0.0236 431 SER A CB 3089 O OG . SER A 438 ? 0.2032 0.1925 0.1500 0.0101 0.0096 0.0152 431 SER A OG 3090 N N . THR A 439 ? 0.1653 0.1672 0.1690 0.0189 -0.0114 0.0076 432 THR A N 3091 C CA . THR A 439 ? 0.1770 0.1870 0.1517 0.0172 -0.0084 0.0223 432 THR A CA 3092 C C . THR A 439 ? 0.1799 0.1729 0.1664 0.0140 0.0136 -0.0023 432 THR A C 3093 O O . THR A 439 ? 0.1708 0.1755 0.1784 0.0105 0.0129 -0.0044 432 THR A O 3094 C CB . THR A 439 ? 0.1687 0.1875 0.1670 0.0221 0.0134 0.0234 432 THR A CB 3095 O OG1 . THR A 439 ? 0.1773 0.2002 0.2053 0.0018 0.0206 -0.0077 432 THR A OG1 3096 C CG2 . THR A 439 ? 0.2305 0.1729 0.1635 0.0321 -0.0044 0.0133 432 THR A CG2 3097 N N . GLU A 440 ? 0.1628 0.1813 0.1802 0.0046 0.0011 -0.0052 433 GLU A N 3098 C CA . GLU A 440 ? 0.1606 0.1734 0.1642 -0.0171 0.0110 -0.0150 433 GLU A CA 3099 C C . GLU A 440 ? 0.1713 0.1674 0.1769 0.0101 0.0197 -0.0169 433 GLU A C 3100 O O . GLU A 440 ? 0.1903 0.1788 0.2083 0.0315 0.0222 -0.0007 433 GLU A O 3101 C CB . GLU A 440 ? 0.1810 0.1693 0.1643 0.0152 -0.0056 -0.0344 433 GLU A CB 3102 C CG . GLU A 440 ? 0.1891 0.1977 0.1576 0.0156 0.0002 0.0073 433 GLU A CG 3103 C CD . GLU A 440 ? 0.1779 0.1643 0.1908 0.0112 -0.0148 -0.0057 433 GLU A CD 3104 O OE1 . GLU A 440 ? 0.1749 0.2017 0.2142 0.0302 0.0011 -0.0226 433 GLU A OE1 3105 O OE2 . GLU A 440 ? 0.1808 0.1981 0.2210 -0.0103 0.0051 -0.0114 433 GLU A OE2 3106 N N . TRP A 441 ? 0.1886 0.1819 0.1728 0.0073 0.0195 -0.0070 434 TRP A N 3107 C CA . TRP A 441 ? 0.2110 0.1624 0.1640 0.0314 0.0056 0.0124 434 TRP A CA 3108 C C . TRP A 441 ? 0.1657 0.1784 0.1950 0.0168 0.0288 -0.0016 434 TRP A C 3109 O O . TRP A 441 ? 0.1993 0.1804 0.1555 0.0342 0.0228 0.0038 434 TRP A O 3110 C CB . TRP A 441 ? 0.2213 0.2003 0.1614 0.0346 -0.0025 0.0186 434 TRP A CB 3111 C CG . TRP A 441 ? 0.1830 0.1956 0.1815 0.0115 0.0276 0.0168 434 TRP A CG 3112 C CD1 . TRP A 441 ? 0.2152 0.1986 0.2006 0.0419 0.0364 0.0584 434 TRP A CD1 3113 C CD2 . TRP A 441 ? 0.2305 0.2080 0.1931 0.0318 0.0000 0.0102 434 TRP A CD2 3114 N NE1 . TRP A 441 ? 0.2605 0.1953 0.2281 0.0386 0.0323 0.0292 434 TRP A NE1 3115 C CE2 . TRP A 441 ? 0.2468 0.2062 0.2077 0.0425 0.0091 0.0125 434 TRP A CE2 3116 C CE3 . TRP A 441 ? 0.2096 0.1986 0.1508 0.0390 -0.0252 -0.0120 434 TRP A CE3 3117 C CZ2 . TRP A 441 ? 0.2639 0.2158 0.2233 0.0337 0.0027 -0.0067 434 TRP A CZ2 3118 C CZ3 . TRP A 441 ? 0.2540 0.2166 0.1278 0.0423 -0.0258 0.0055 434 TRP A CZ3 3119 C CH2 . TRP A 441 ? 0.1984 0.2389 0.1840 0.0458 -0.0018 0.0181 434 TRP A CH2 3120 N N . ALA A 442 ? 0.1903 0.1599 0.1675 -0.0072 0.0213 0.0046 435 ALA A N 3121 C CA . ALA A 442 ? 0.1613 0.1666 0.1894 0.0124 0.0367 0.0040 435 ALA A CA 3122 C C . ALA A 442 ? 0.1880 0.1793 0.1627 0.0159 0.0107 -0.0126 435 ALA A C 3123 O O . ALA A 442 ? 0.1714 0.1862 0.1772 0.0317 0.0199 -0.0046 435 ALA A O 3124 C CB . ALA A 442 ? 0.1526 0.2085 0.1950 -0.0053 0.0305 -0.0081 435 ALA A CB 3125 N N . GLU A 443 ? 0.1730 0.1750 0.1621 0.0038 -0.0173 0.0002 436 GLU A N 3126 C CA . GLU A 443 ? 0.1573 0.1940 0.1734 0.0343 0.0182 0.0023 436 GLU A CA 3127 C C . GLU A 443 ? 0.1744 0.1798 0.1845 0.0128 0.0274 0.0033 436 GLU A C 3128 O O . GLU A 443 ? 0.1807 0.1970 0.2014 0.0297 0.0198 0.0091 436 GLU A O 3129 C CB . GLU A 443 ? 0.1956 0.1908 0.1795 -0.0217 0.0388 -0.0097 436 GLU A CB 3130 C CG . GLU A 443 ? 0.1518 0.2096 0.1531 0.0013 0.0189 0.0001 436 GLU A CG 3131 C CD . GLU A 443 ? 0.2380 0.2171 0.1873 -0.0334 0.0050 -0.0266 436 GLU A CD 3132 O OE1 . GLU A 443 ? 0.2025 0.1946 0.2008 -0.0185 0.0229 -0.0290 436 GLU A OE1 3133 O OE2 . GLU A 443 ? 0.2062 0.1936 0.2312 -0.0046 -0.0026 -0.0389 436 GLU A OE2 3134 N N . GLU A 444 ? 0.1877 0.1912 0.1776 0.0069 0.0319 0.0094 437 GLU A N 3135 C CA . GLU A 444 ? 0.1766 0.1620 0.1683 -0.0089 0.0221 0.0133 437 GLU A CA 3136 C C . GLU A 444 ? 0.1854 0.1737 0.1959 0.0138 0.0151 -0.0039 437 GLU A C 3137 O O . GLU A 444 ? 0.2047 0.2069 0.2006 0.0247 0.0356 -0.0056 437 GLU A O 3138 C CB . GLU A 444 ? 0.1764 0.1657 0.2244 -0.0227 0.0427 0.0378 437 GLU A CB 3139 C CG . GLU A 444 ? 0.1782 0.1803 0.3015 -0.0178 0.0711 0.0277 437 GLU A CG 3140 C CD . GLU A 444 ? 0.3119 0.1961 0.4609 -0.0636 0.0189 0.0608 437 GLU A CD 3141 O OE1 . GLU A 444 ? 0.5509 0.4702 0.6244 -0.1690 -0.0513 -0.0311 437 GLU A OE1 3142 O OE2 . GLU A 444 ? 0.3300 0.2517 0.4250 0.0248 0.1347 0.0922 437 GLU A OE2 3143 N N . ASN A 445 ? 0.2022 0.1589 0.1781 0.0114 0.0031 0.0067 438 ASN A N 3144 C CA . ASN A 445 ? 0.2204 0.1548 0.1665 0.0389 -0.0023 0.0263 438 ASN A CA 3145 C C . ASN A 445 ? 0.2226 0.1800 0.1530 0.0072 0.0013 0.0194 438 ASN A C 3146 O O . ASN A 445 ? 0.1999 0.1868 0.1514 0.0330 0.0102 0.0117 438 ASN A O 3147 C CB . ASN A 445 ? 0.2180 0.1787 0.1683 0.0525 0.0067 0.0316 438 ASN A CB 3148 C CG . ASN A 445 ? 0.2218 0.1780 0.1959 0.0495 0.0516 0.0391 438 ASN A CG 3149 O OD1 . ASN A 445 ? 0.2415 0.1949 0.3210 0.0137 0.1009 0.0248 438 ASN A OD1 3150 N ND2 . ASN A 445 ? 0.2337 0.1776 0.2615 0.0500 0.0634 0.0320 438 ASN A ND2 3151 N N . SER A 446 ? 0.2045 0.1519 0.1677 0.0115 0.0179 0.0232 439 SER A N 3152 C CA . SER A 446 ? 0.1983 0.1637 0.1227 -0.0008 0.0333 0.0118 439 SER A CA 3153 C C . SER A 446 ? 0.1845 0.1824 0.1584 0.0088 0.0320 -0.0083 439 SER A C 3154 O O . SER A 446 ? 0.2051 0.2009 0.1515 0.0130 0.0182 -0.0183 439 SER A O 3155 C CB . SER A 446 ? 0.1737 0.1981 0.1475 0.0169 -0.0190 0.0378 439 SER A CB 3156 O OG . SER A 446 ? 0.1808 0.2193 0.2019 0.0400 0.0131 -0.0063 439 SER A OG 3157 N N . ARG A 447 ? 0.1980 0.1776 0.1550 0.0353 0.0235 0.0147 440 ARG A N 3158 C CA . ARG A 447 ? 0.1970 0.1740 0.1448 0.0196 0.0007 -0.0015 440 ARG A CA 3159 C C . ARG A 447 ? 0.2216 0.1801 0.1522 0.0221 0.0017 0.0185 440 ARG A C 3160 O O . ARG A 447 ? 0.2373 0.1865 0.1517 0.0210 -0.0270 0.0166 440 ARG A O 3161 C CB . ARG A 447 ? 0.2063 0.2064 0.1557 0.0621 0.0148 0.0101 440 ARG A CB 3162 C CG . ARG A 447 ? 0.2178 0.2284 0.1957 0.0353 -0.0328 0.0271 440 ARG A CG 3163 C CD . ARG A 447 ? 0.2617 0.2320 0.2432 0.0070 -0.0593 0.0489 440 ARG A CD 3164 N NE . ARG A 447 ? 0.2747 0.2357 0.2076 0.0249 -0.0602 0.0084 440 ARG A NE 3165 C CZ . ARG A 447 ? 0.2101 0.2087 0.2497 0.0134 -0.0656 -0.0199 440 ARG A CZ 3166 N NH1 . ARG A 447 ? 0.2287 0.2295 0.3457 0.0241 -0.0357 -0.0553 440 ARG A NH1 3167 N NH2 . ARG A 447 ? 0.2217 0.2246 0.1800 -0.0121 -0.0071 -0.0122 440 ARG A NH2 3168 N N . LEU A 448 ? 0.1993 0.1874 0.1703 0.0539 0.0252 0.0300 441 LEU A N 3169 C CA . LEU A 448 ? 0.2114 0.1684 0.1623 0.0289 0.0174 0.0231 441 LEU A CA 3170 C C . LEU A 448 ? 0.2177 0.1980 0.1667 0.0381 0.0214 0.0019 441 LEU A C 3171 O O . LEU A 448 ? 0.2400 0.2274 0.1466 0.0419 0.0166 -0.0018 441 LEU A O 3172 C CB . LEU A 448 ? 0.2199 0.1722 0.2036 0.0214 0.0214 0.0453 441 LEU A CB 3173 C CG . LEU A 448 ? 0.1807 0.1920 0.2134 0.0617 0.0508 -0.0057 441 LEU A CG 3174 C CD1 . LEU A 448 ? 0.2884 0.2247 0.2424 0.0229 0.0186 0.0442 441 LEU A CD1 3175 C CD2 . LEU A 448 ? 0.2425 0.2183 0.1780 0.0665 0.0830 -0.0091 441 LEU A CD2 3176 N N . LEU A 449 ? 0.2188 0.1932 0.1621 0.0401 0.0385 0.0282 442 LEU A N 3177 C CA . LEU A 449 ? 0.2337 0.2294 0.1759 0.0269 0.0213 -0.0042 442 LEU A CA 3178 C C . LEU A 449 ? 0.2410 0.2294 0.1441 0.0155 0.0138 0.0044 442 LEU A C 3179 O O . LEU A 449 ? 0.2387 0.2773 0.2041 0.0104 0.0173 -0.0087 442 LEU A O 3180 C CB . LEU A 449 ? 0.2502 0.1872 0.1857 0.0368 0.0092 -0.0180 442 LEU A CB 3181 C CG . LEU A 449 ? 0.2431 0.1773 0.1202 0.0532 0.0092 -0.0161 442 LEU A CG 3182 C CD1 . LEU A 449 ? 0.2115 0.2310 0.1247 0.0083 0.0235 -0.0349 442 LEU A CD1 3183 C CD2 . LEU A 449 ? 0.3033 0.2916 0.1657 0.0473 -0.0256 0.0289 442 LEU A CD2 3184 N N A GLN A 450 ? 0.2682 0.1791 0.1945 0.0249 0.0228 0.0069 443 GLN A N 3185 N N B GLN A 450 ? 0.2550 0.1984 0.1816 0.0247 0.0199 0.0071 443 GLN A N 3186 C CA A GLN A 450 ? 0.2581 0.2037 0.1592 0.0041 0.0076 0.0071 443 GLN A CA 3187 C CA B GLN A 450 ? 0.2558 0.2063 0.1662 0.0206 -0.0095 0.0069 443 GLN A CA 3188 C C A GLN A 450 ? 0.2316 0.2141 0.1802 0.0074 0.0256 -0.0098 443 GLN A C 3189 C C B GLN A 450 ? 0.2341 0.2116 0.1677 0.0231 0.0268 0.0023 443 GLN A C 3190 O O A GLN A 450 ? 0.2331 0.2225 0.1532 0.0058 0.0085 -0.0079 443 GLN A O 3191 O O B GLN A 450 ? 0.2371 0.2083 0.1562 0.0296 -0.0114 0.0114 443 GLN A O 3192 C CB A GLN A 450 ? 0.1971 0.1984 0.1581 -0.0154 0.0242 0.0224 443 GLN A CB 3193 C CB B GLN A 450 ? 0.2393 0.2039 0.1641 0.0016 0.0002 0.0287 443 GLN A CB 3194 C CG A GLN A 450 ? 0.2114 0.1425 0.1748 0.0458 0.0123 0.0082 443 GLN A CG 3195 C CG B GLN A 450 ? 0.2077 0.2157 0.1761 0.0110 -0.0099 0.0109 443 GLN A CG 3196 C CD A GLN A 450 ? 0.2030 0.2291 0.1724 0.0282 0.0223 0.0230 443 GLN A CD 3197 C CD B GLN A 450 ? 0.2303 0.1289 0.1984 -0.0186 -0.0296 -0.0145 443 GLN A CD 3198 O OE1 A GLN A 450 ? 0.1429 0.2686 0.2551 -0.0006 0.0428 -0.0009 443 GLN A OE1 3199 O OE1 B GLN A 450 ? 0.2013 0.1637 0.1927 -0.0136 0.0045 0.0194 443 GLN A OE1 3200 N NE2 A GLN A 450 ? 0.1804 0.2425 0.1909 0.0150 0.0251 0.0040 443 GLN A NE2 3201 N NE2 B GLN A 450 ? 0.1120 0.0765 0.1837 -0.0062 -0.0763 0.0621 443 GLN A NE2 3202 N N . GLU A 451 ? 0.2296 0.2035 0.1468 0.0330 0.0161 0.0152 444 GLU A N 3203 C CA . GLU A 451 ? 0.2154 0.2232 0.1571 0.0558 0.0242 0.0137 444 GLU A CA 3204 C C . GLU A 451 ? 0.2755 0.1946 0.1460 0.0332 0.0174 0.0135 444 GLU A C 3205 O O . GLU A 451 ? 0.2767 0.2216 0.1139 0.0589 0.0118 0.0217 444 GLU A O 3206 C CB . GLU A 451 ? 0.1979 0.2434 0.1945 0.0532 -0.0180 0.0328 444 GLU A CB 3207 C CG . GLU A 451 ? 0.2418 0.2375 0.2020 0.0311 -0.0257 0.0479 444 GLU A CG 3208 C CD . GLU A 451 ? 0.2808 0.2273 0.2197 0.0111 -0.0503 0.0219 444 GLU A CD 3209 O OE1 . GLU A 451 ? 0.2627 0.2114 0.2291 0.0153 -0.0417 0.0128 444 GLU A OE1 3210 O OE2 . GLU A 451 ? 0.3431 0.1960 0.2507 0.0031 -0.0696 0.0464 444 GLU A OE2 3211 N N . ARG A 452 ? 0.1911 0.2078 0.1470 0.0474 0.0258 0.0274 445 ARG A N 3212 C CA . ARG A 452 ? 0.2189 0.2093 0.1455 0.0432 0.0305 0.0347 445 ARG A CA 3213 C C . ARG A 452 ? 0.2072 0.2279 0.1577 0.0394 -0.0079 0.0118 445 ARG A C 3214 O O . ARG A 452 ? 0.2236 0.2235 0.1974 0.0429 -0.0244 0.0219 445 ARG A O 3215 C CB . ARG A 452 ? 0.1933 0.2256 0.1430 0.0400 0.0099 0.0200 445 ARG A CB 3216 C CG . ARG A 452 ? 0.2140 0.2104 0.1796 0.0483 0.0431 0.0399 445 ARG A CG 3217 C CD . ARG A 452 ? 0.2182 0.2236 0.1939 0.0253 0.0249 0.0583 445 ARG A CD 3218 N NE . ARG A 452 ? 0.2323 0.2326 0.1982 0.0329 0.0490 0.0635 445 ARG A NE 3219 C CZ . ARG A 452 ? 0.2084 0.2069 0.1971 0.0562 0.0774 0.0451 445 ARG A CZ 3220 N NH1 . ARG A 452 ? 0.2645 0.2018 0.1800 0.0452 0.0439 0.0470 445 ARG A NH1 3221 N NH2 . ARG A 452 ? 0.2263 0.2114 0.1789 0.0724 0.0406 0.0456 445 ARG A NH2 3222 N N . GLY A 453 ? 0.2184 0.2317 0.1811 0.0495 0.0206 -0.0219 446 GLY A N 3223 C CA . GLY A 453 ? 0.2014 0.2641 0.1839 0.0519 0.0014 -0.0067 446 GLY A CA 3224 C C . GLY A 453 ? 0.2326 0.2245 0.1627 0.0509 -0.0169 0.0025 446 GLY A C 3225 O O . GLY A 453 ? 0.2448 0.2295 0.2042 0.0268 -0.0266 0.0026 446 GLY A O 3226 N N . VAL A 454 ? 0.2285 0.2504 0.1335 0.0625 0.0000 -0.0139 447 VAL A N 3227 C CA . VAL A 454 ? 0.2590 0.2414 0.1545 0.0529 -0.0308 -0.0001 447 VAL A CA 3228 C C . VAL A 454 ? 0.2641 0.2112 0.1930 0.0524 -0.0186 -0.0079 447 VAL A C 3229 O O . VAL A 454 ? 0.2374 0.2061 0.1888 0.0566 -0.0316 0.0026 447 VAL A O 3230 C CB . VAL A 454 ? 0.2460 0.2633 0.1339 0.0695 -0.0107 -0.0136 447 VAL A CB 3231 C CG1 . VAL A 454 ? 0.2919 0.2365 0.1990 0.0149 -0.0325 -0.0312 447 VAL A CG1 3232 C CG2 . VAL A 454 ? 0.2762 0.2892 0.1983 0.0857 0.0243 -0.0125 447 VAL A CG2 3233 N N . ALA A 455 ? 0.2335 0.2148 0.1732 0.0716 -0.0155 -0.0172 448 ALA A N 3234 C CA . ALA A 455 ? 0.1993 0.2017 0.1487 0.0576 -0.0455 -0.0235 448 ALA A CA 3235 C C . ALA A 455 ? 0.2220 0.2016 0.1578 0.0410 -0.0180 -0.0205 448 ALA A C 3236 O O . ALA A 455 ? 0.2531 0.2122 0.1859 0.0425 -0.0094 -0.0086 448 ALA A O 3237 C CB . ALA A 455 ? 0.2159 0.2353 0.1466 0.0674 -0.0581 -0.0068 448 ALA A CB 3238 N N . TYR A 456 ? 0.2667 0.1877 0.1750 0.0577 -0.0121 -0.0350 449 TYR A N 3239 C CA . TYR A 456 ? 0.2220 0.2002 0.1624 0.0636 -0.0182 -0.0330 449 TYR A CA 3240 C C . TYR A 456 ? 0.2075 0.1949 0.1891 0.0416 -0.0328 -0.0058 449 TYR A C 3241 O O . TYR A 456 ? 0.2138 0.2168 0.2013 0.0430 -0.0302 -0.0076 449 TYR A O 3242 C CB . TYR A 456 ? 0.2359 0.1961 0.1683 0.0398 -0.0212 -0.0193 449 TYR A CB 3243 C CG . TYR A 456 ? 0.2212 0.2014 0.1492 0.0237 0.0027 -0.0237 449 TYR A CG 3244 C CD1 . TYR A 456 ? 0.2518 0.1736 0.1650 0.0170 -0.0102 -0.0159 449 TYR A CD1 3245 C CD2 . TYR A 456 ? 0.1806 0.1939 0.1895 0.0185 -0.0174 -0.0339 449 TYR A CD2 3246 C CE1 . TYR A 456 ? 0.2350 0.1959 0.1803 0.0343 -0.0214 -0.0354 449 TYR A CE1 3247 C CE2 . TYR A 456 ? 0.2563 0.1594 0.1885 0.0070 -0.0232 -0.0118 449 TYR A CE2 3248 C CZ . TYR A 456 ? 0.2306 0.1842 0.2076 0.0157 0.0018 -0.0077 449 TYR A CZ 3249 O OH . TYR A 456 ? 0.2521 0.1890 0.2031 0.0474 -0.0005 -0.0056 449 TYR A OH 3250 N N . ILE A 457 ? 0.2034 0.2042 0.1700 0.0452 -0.0433 0.0013 450 ILE A N 3251 C CA . ILE A 457 ? 0.2216 0.1810 0.1645 0.0522 -0.0494 -0.0191 450 ILE A CA 3252 C C . ILE A 457 ? 0.2310 0.1904 0.1703 0.0430 -0.0127 -0.0233 450 ILE A C 3253 O O . ILE A 457 ? 0.2668 0.1902 0.1819 0.0321 0.0011 -0.0134 450 ILE A O 3254 C CB . ILE A 457 ? 0.2291 0.2085 0.1530 0.0539 -0.0310 -0.0129 450 ILE A CB 3255 C CG1 . ILE A 457 ? 0.2445 0.1792 0.2088 0.0214 0.0169 -0.0180 450 ILE A CG1 3256 C CG2 . ILE A 457 ? 0.2423 0.1828 0.2443 0.0624 -0.0309 -0.0242 450 ILE A CG2 3257 C CD1 . ILE A 457 ? 0.2582 0.1678 0.2042 0.0187 -0.0404 0.0044 450 ILE A CD1 3258 N N . ASN A 458 ? 0.2411 0.1918 0.1529 0.0457 -0.0148 -0.0376 451 ASN A N 3259 C CA . ASN A 458 ? 0.2483 0.1637 0.1660 0.0333 0.0019 -0.0253 451 ASN A CA 3260 C C . ASN A 458 ? 0.2697 0.1944 0.1901 0.0429 -0.0148 -0.0102 451 ASN A C 3261 O O . ASN A 458 ? 0.2757 0.2144 0.2562 0.0313 -0.0337 -0.0520 451 ASN A O 3262 C CB . ASN A 458 ? 0.2520 0.1947 0.1551 0.0208 0.0139 -0.0340 451 ASN A CB 3263 C CG . ASN A 458 ? 0.2227 0.2012 0.1626 0.0212 0.0021 -0.0218 451 ASN A CG 3264 O OD1 . ASN A 458 ? 0.2470 0.2527 0.1947 0.0259 -0.0076 -0.0292 451 ASN A OD1 3265 N ND2 . ASN A 458 ? 0.2761 0.2112 0.1817 0.0495 0.0378 -0.0044 451 ASN A ND2 3266 N N . ALA A 459 ? 0.2478 0.1714 0.2224 0.0575 0.0001 -0.0032 452 ALA A N 3267 C CA . ALA A 459 ? 0.3015 0.1715 0.1924 0.0600 0.0019 0.0047 452 ALA A CA 3268 C C . ALA A 459 ? 0.2508 0.2031 0.2037 0.0531 -0.0056 -0.0073 452 ALA A C 3269 O O . ALA A 459 ? 0.2578 0.2326 0.2264 0.0250 0.0191 0.0000 452 ALA A O 3270 C CB . ALA A 459 ? 0.2738 0.2032 0.2229 0.0193 0.0133 0.0157 452 ALA A CB 3271 N N . ASP A 460 ? 0.2458 0.2095 0.1955 0.0334 0.0015 -0.0139 453 ASP A N 3272 C CA . ASP A 460 ? 0.2110 0.1968 0.2152 0.0605 -0.0024 -0.0096 453 ASP A CA 3273 C C . ASP A 460 ? 0.2080 0.1908 0.2312 0.0384 -0.0156 -0.0107 453 ASP A C 3274 O O . ASP A 460 ? 0.2461 0.2140 0.2514 0.0272 -0.0294 -0.0135 453 ASP A O 3275 C CB . ASP A 460 ? 0.2444 0.2136 0.2189 0.0312 -0.0293 -0.0103 453 ASP A CB 3276 C CG . ASP A 460 ? 0.2451 0.2220 0.2420 0.0328 -0.0233 -0.0173 453 ASP A CG 3277 O OD1 . ASP A 460 ? 0.2858 0.2403 0.3138 0.0315 -0.0349 -0.0023 453 ASP A OD1 3278 O OD2 . ASP A 460 ? 0.2864 0.2501 0.2358 -0.0123 -0.0240 -0.0276 453 ASP A OD2 3279 N N . SER A 461 ? 0.1933 0.2177 0.2560 0.0507 -0.0124 -0.0275 454 SER A N 3280 C CA A SER A 461 ? 0.2081 0.2441 0.2310 0.0598 -0.0377 -0.0231 454 SER A CA 3281 C CA B SER A 461 ? 0.2108 0.2337 0.2443 0.0563 -0.0360 -0.0218 454 SER A CA 3282 C C . SER A 461 ? 0.2250 0.2217 0.2419 0.0410 -0.0277 -0.0270 454 SER A C 3283 O O . SER A 461 ? 0.2319 0.2276 0.2431 0.0346 -0.0133 -0.0006 454 SER A O 3284 C CB A SER A 461 ? 0.2289 0.2302 0.2059 0.0198 -0.0491 -0.0305 454 SER A CB 3285 C CB B SER A 461 ? 0.2749 0.2474 0.2772 0.0526 0.0095 -0.0128 454 SER A CB 3286 O OG A SER A 461 ? 0.1232 0.1601 0.1971 0.0342 -0.0327 -0.0157 454 SER A OG 3287 O OG B SER A 461 ? 0.2961 0.2668 0.3433 0.0199 0.0224 0.0003 454 SER A OG 3288 N N . SER A 462 ? 0.2021 0.2455 0.2425 0.0535 -0.0334 -0.0220 455 SER A N 3289 C CA . SER A 462 ? 0.2400 0.2639 0.2424 0.0245 -0.0445 -0.0132 455 SER A CA 3290 C C . SER A 462 ? 0.2259 0.2426 0.2722 0.0494 -0.0400 -0.0296 455 SER A C 3291 O O . SER A 462 ? 0.2657 0.2352 0.2672 0.0405 -0.0333 -0.0377 455 SER A O 3292 C CB . SER A 462 ? 0.2460 0.2943 0.2529 0.0281 -0.0203 0.0061 455 SER A CB 3293 O OG . SER A 462 ? 0.2460 0.2875 0.3100 0.0709 -0.0295 -0.0312 455 SER A OG 3294 N N . ILE A 463 ? 0.2562 0.2604 0.2653 0.0384 -0.0395 -0.0232 456 ILE A N 3295 C CA . ILE A 463 ? 0.2453 0.2659 0.2854 0.0430 -0.0538 -0.0474 456 ILE A CA 3296 C C . ILE A 463 ? 0.2738 0.2789 0.3001 0.0244 -0.0324 -0.0188 456 ILE A C 3297 O O . ILE A 463 ? 0.2963 0.3354 0.3324 0.0119 -0.0541 -0.0454 456 ILE A O 3298 C CB . ILE A 463 ? 0.3105 0.2528 0.3070 0.0495 -0.0436 -0.0327 456 ILE A CB 3299 C CG1 . ILE A 463 ? 0.3576 0.2775 0.3824 0.0427 -0.0284 -0.0288 456 ILE A CG1 3300 C CG2 . ILE A 463 ? 0.3426 0.2468 0.3154 0.0550 -0.0615 -0.0064 456 ILE A CG2 3301 C CD1 . ILE A 463 ? 0.3931 0.3916 0.4481 0.0996 0.0124 -0.0471 456 ILE A CD1 3302 N N . GLU A 464 ? 0.2857 0.2717 0.3191 0.0217 -0.0223 -0.0442 457 GLU A N 3303 C CA . GLU A 464 ? 0.2698 0.2723 0.3207 0.0257 -0.0142 -0.0218 457 GLU A CA 3304 C C . GLU A 464 ? 0.2723 0.3041 0.3289 0.0612 -0.0179 -0.0186 457 GLU A C 3305 O O . GLU A 464 ? 0.2502 0.3368 0.3237 0.0502 -0.0189 -0.0576 457 GLU A O 3306 C CB . GLU A 464 ? 0.2981 0.2744 0.2804 0.0217 -0.0727 -0.0509 457 GLU A CB 3307 C CG . GLU A 464 ? 0.2850 0.2635 0.3260 0.0092 -0.0194 -0.0352 457 GLU A CG 3308 C CD . GLU A 464 ? 0.3082 0.3212 0.4072 0.0288 -0.0573 -0.0210 457 GLU A CD 3309 O OE1 . GLU A 464 ? 0.3198 0.3169 0.3354 0.0166 -0.0536 -0.0307 457 GLU A OE1 3310 O OE2 . GLU A 464 ? 0.3212 0.3282 0.3593 0.0315 -0.0590 -0.0222 457 GLU A OE2 3311 N N . GLY A 465 ? 0.2681 0.2951 0.3294 0.0628 -0.0303 -0.0583 458 GLY A N 3312 C CA . GLY A 465 ? 0.2779 0.2765 0.3665 0.0817 -0.0551 -0.0846 458 GLY A CA 3313 C C . GLY A 465 ? 0.2426 0.3168 0.3614 0.0687 -0.0508 -0.0711 458 GLY A C 3314 O O . GLY A 465 ? 0.3120 0.3315 0.3502 0.0570 -0.0266 -0.0718 458 GLY A O 3315 N N . ASN A 466 ? 0.2393 0.2971 0.3723 0.0879 -0.0535 -0.0511 459 ASN A N 3316 C CA . ASN A 466 ? 0.2854 0.2850 0.3732 0.0572 -0.0641 -0.0462 459 ASN A CA 3317 C C . ASN A 466 ? 0.2721 0.2876 0.3889 0.0581 -0.0619 -0.0410 459 ASN A C 3318 O O . ASN A 466 ? 0.3117 0.3102 0.3971 0.0687 -0.0780 -0.0465 459 ASN A O 3319 C CB . ASN A 466 ? 0.3290 0.2782 0.4170 0.0642 -0.0591 -0.0614 459 ASN A CB 3320 C CG . ASN A 466 ? 0.3208 0.3548 0.3984 0.0678 -0.0767 -0.0879 459 ASN A CG 3321 O OD1 . ASN A 466 ? 0.3722 0.3635 0.4060 0.1227 -0.0444 -0.0300 459 ASN A OD1 3322 N ND2 . ASN A 466 ? 0.4549 0.3947 0.4639 0.0956 0.0026 -0.0531 459 ASN A ND2 3323 N N . TYR A 467 ? 0.2790 0.2518 0.4029 0.0387 -0.0489 -0.0736 460 TYR A N 3324 C CA . TYR A 467 ? 0.2405 0.2554 0.4156 0.0592 -0.0408 -0.0879 460 TYR A CA 3325 C C . TYR A 467 ? 0.2631 0.2805 0.3928 0.0773 -0.0351 -0.0723 460 TYR A C 3326 O O . TYR A 467 ? 0.2612 0.3133 0.4164 0.0852 -0.0623 -0.0668 460 TYR A O 3327 C CB . TYR A 467 ? 0.2368 0.2687 0.3959 0.0519 -0.0396 -0.1086 460 TYR A CB 3328 C CG . TYR A 467 ? 0.2913 0.3149 0.4826 0.0079 -0.0186 -0.1032 460 TYR A CG 3329 C CD1 . TYR A 467 ? 0.3275 0.3591 0.4653 0.0087 -0.0730 -0.1044 460 TYR A CD1 3330 C CD2 . TYR A 467 ? 0.3645 0.3456 0.4484 0.0374 0.0134 -0.0931 460 TYR A CD2 3331 C CE1 . TYR A 467 ? 0.3083 0.4127 0.5007 0.0032 -0.0400 -0.1116 460 TYR A CE1 3332 C CE2 . TYR A 467 ? 0.3913 0.3559 0.4481 0.0182 0.0129 -0.0819 460 TYR A CE2 3333 C CZ . TYR A 467 ? 0.3816 0.4123 0.5720 -0.0329 -0.0311 -0.1179 460 TYR A CZ 3334 O OH . TYR A 467 ? 0.4060 0.5828 0.5488 -0.1122 -0.0069 -0.1517 460 TYR A OH 3335 N N . THR A 468 ? 0.2351 0.2787 0.3657 0.0570 -0.0180 -0.0483 461 THR A N 3336 C CA . THR A 468 ? 0.2132 0.2481 0.3791 0.0679 -0.0499 -0.0574 461 THR A CA 3337 C C . THR A 468 ? 0.2280 0.2742 0.3484 0.0912 -0.0587 -0.0669 461 THR A C 3338 O O . THR A 468 ? 0.2331 0.2659 0.3552 0.0728 -0.0470 -0.0733 461 THR A O 3339 C CB . THR A 468 ? 0.2538 0.2602 0.3534 0.0494 -0.0500 -0.0666 461 THR A CB 3340 O OG1 . THR A 468 ? 0.2882 0.2893 0.3724 0.0517 -0.0884 -0.0901 461 THR A OG1 3341 C CG2 . THR A 468 ? 0.2264 0.2800 0.3800 0.0671 -0.0366 -0.0133 461 THR A CG2 3342 N N . LEU A 469 ? 0.2272 0.2585 0.3452 0.0745 -0.0402 -0.0619 462 LEU A N 3343 C CA . LEU A 469 ? 0.2377 0.2830 0.3014 0.0961 -0.0142 -0.0372 462 LEU A CA 3344 C C . LEU A 469 ? 0.2311 0.2744 0.3286 0.0509 -0.0416 -0.0307 462 LEU A C 3345 O O . LEU A 469 ? 0.2338 0.2756 0.3631 0.0449 -0.0319 -0.0183 462 LEU A O 3346 C CB . LEU A 469 ? 0.2172 0.2733 0.3481 0.0738 -0.0038 -0.0962 462 LEU A CB 3347 C CG . LEU A 469 ? 0.2058 0.2251 0.3334 0.0753 -0.0317 -0.0746 462 LEU A CG 3348 C CD1 . LEU A 469 ? 0.2022 0.2814 0.3325 0.0426 -0.0024 -0.0537 462 LEU A CD1 3349 C CD2 . LEU A 469 ? 0.2770 0.2654 0.2688 0.0702 -0.0301 -0.0572 462 LEU A CD2 3350 N N . ARG A 470 ? 0.2214 0.2233 0.2925 0.0566 -0.0347 -0.0284 463 ARG A N 3351 C CA . ARG A 470 ? 0.2239 0.2393 0.3043 0.0722 -0.0662 -0.0516 463 ARG A CA 3352 C C . ARG A 470 ? 0.2119 0.2135 0.3218 0.0550 -0.0583 -0.0287 463 ARG A C 3353 O O . ARG A 470 ? 0.2091 0.2381 0.3239 0.0655 -0.0092 -0.0369 463 ARG A O 3354 C CB . ARG A 470 ? 0.2711 0.2998 0.2930 0.0802 -0.0648 -0.0544 463 ARG A CB 3355 C CG . ARG A 470 ? 0.2757 0.3416 0.3107 0.0637 -0.0938 -0.0596 463 ARG A CG 3356 C CD . ARG A 470 ? 0.3460 0.4076 0.2986 0.0520 -0.0593 -0.0938 463 ARG A CD 3357 N NE . ARG A 470 ? 0.3509 0.4360 0.3676 0.0978 -0.0281 -0.0830 463 ARG A NE 3358 C CZ . ARG A 470 ? 0.4715 0.3757 0.4278 0.1088 -0.1311 -0.0414 463 ARG A CZ 3359 N NH1 . ARG A 470 ? 0.5404 0.3995 0.4698 0.1570 -0.0358 -0.0692 463 ARG A NH1 3360 N NH2 . ARG A 470 ? 0.4260 0.3757 0.5312 0.1234 -0.0668 0.0410 463 ARG A NH2 3361 N N . VAL A 471 ? 0.1929 0.2101 0.3134 0.0525 -0.0686 -0.0579 464 VAL A N 3362 C CA . VAL A 471 ? 0.2180 0.1971 0.2594 0.0684 -0.0384 -0.0348 464 VAL A CA 3363 C C . VAL A 471 ? 0.2165 0.2062 0.2783 0.0456 -0.0399 -0.0295 464 VAL A C 3364 O O . VAL A 471 ? 0.2343 0.2283 0.2888 0.0191 -0.0316 -0.0391 464 VAL A O 3365 C CB . VAL A 471 ? 0.2105 0.2310 0.2609 0.0973 -0.0457 -0.0441 464 VAL A CB 3366 C CG1 . VAL A 471 ? 0.2085 0.2397 0.2879 0.0918 -0.0215 -0.0364 464 VAL A CG1 3367 C CG2 . VAL A 471 ? 0.2862 0.2655 0.2505 0.0501 -0.0646 -0.0280 464 VAL A CG2 3368 N N . ASP A 472 ? 0.2114 0.2015 0.2601 0.0617 -0.0416 -0.0237 465 ASP A N 3369 C CA . ASP A 472 ? 0.1969 0.2184 0.2515 0.0666 -0.0331 -0.0243 465 ASP A CA 3370 C C . ASP A 472 ? 0.2251 0.2106 0.2435 0.0393 -0.0132 -0.0529 465 ASP A C 3371 O O . ASP A 472 ? 0.2123 0.2383 0.2112 0.0404 -0.0188 -0.0389 465 ASP A O 3372 C CB . ASP A 472 ? 0.2320 0.2125 0.2428 0.0119 -0.0344 -0.0177 465 ASP A CB 3373 C CG . ASP A 472 ? 0.2464 0.3033 0.3035 0.0288 -0.0249 -0.0500 465 ASP A CG 3374 O OD1 . ASP A 472 ? 0.3753 0.3497 0.3145 0.0368 -0.0119 -0.0657 465 ASP A OD1 3375 O OD2 . ASP A 472 ? 0.2405 0.3147 0.3042 0.0392 -0.0090 -0.0564 465 ASP A OD2 3376 N N . CYS A 473 ? 0.2344 0.2059 0.2528 0.0526 -0.0206 -0.0353 466 CYS A N 3377 C CA . CYS A 473 ? 0.2181 0.2084 0.2384 0.0427 -0.0239 -0.0155 466 CYS A CA 3378 C C . CYS A 473 ? 0.2088 0.2059 0.2257 0.0341 -0.0429 -0.0266 466 CYS A C 3379 O O . CYS A 473 ? 0.2667 0.2176 0.2974 0.0403 -0.0037 -0.0266 466 CYS A O 3380 C CB . CYS A 473 ? 0.2426 0.1990 0.2349 0.0233 -0.0554 -0.0132 466 CYS A CB 3381 S SG . CYS A 473 ? 0.2370 0.2473 0.2570 0.0326 -0.0565 -0.0311 466 CYS A SG 3382 N N . THR A 474 ? 0.2258 0.1879 0.2068 0.0367 -0.0281 -0.0292 467 THR A N 3383 C CA . THR A 474 ? 0.2096 0.1846 0.2124 0.0264 -0.0411 -0.0208 467 THR A CA 3384 C C . THR A 474 ? 0.2258 0.1991 0.2063 0.0270 -0.0433 -0.0257 467 THR A C 3385 O O . THR A 474 ? 0.2197 0.2161 0.2192 0.0269 -0.0511 -0.0266 467 THR A O 3386 C CB . THR A 474 ? 0.2158 0.1860 0.2131 0.0327 -0.0412 -0.0038 467 THR A CB 3387 O OG1 . THR A 474 ? 0.2166 0.2019 0.2035 0.0320 -0.0459 -0.0234 467 THR A OG1 3388 C CG2 . THR A 474 ? 0.2240 0.2318 0.2007 0.0236 -0.0150 -0.0132 467 THR A CG2 3389 N N . PRO A 475 ? 0.2258 0.1961 0.2063 0.0203 -0.0541 -0.0156 468 PRO A N 3390 C CA . PRO A 475 ? 0.2445 0.1981 0.2247 0.0218 -0.0617 -0.0242 468 PRO A CA 3391 C C . PRO A 475 ? 0.2356 0.2156 0.2394 0.0276 -0.0548 -0.0205 468 PRO A C 3392 O O . PRO A 475 ? 0.2359 0.2401 0.2232 0.0408 -0.0466 -0.0337 468 PRO A O 3393 C CB . PRO A 475 ? 0.2878 0.2061 0.2199 0.0233 -0.0675 -0.0188 468 PRO A CB 3394 C CG . PRO A 475 ? 0.2594 0.2235 0.2068 -0.0191 -0.0463 0.0023 468 PRO A CG 3395 C CD . PRO A 475 ? 0.2227 0.2232 0.2132 -0.0023 -0.0762 -0.0028 468 PRO A CD 3396 N N . LEU A 476 ? 0.2260 0.1964 0.2538 0.0225 -0.0297 -0.0292 469 LEU A N 3397 C CA . LEU A 476 ? 0.2127 0.2343 0.2133 0.0589 -0.0692 -0.0177 469 LEU A CA 3398 C C . LEU A 476 ? 0.2502 0.2063 0.2279 0.0418 -0.0535 -0.0156 469 LEU A C 3399 O O . LEU A 476 ? 0.2993 0.2624 0.2175 0.0869 -0.0649 -0.0322 469 LEU A O 3400 C CB . LEU A 476 ? 0.2151 0.2157 0.2412 0.0719 -0.0540 -0.0159 469 LEU A CB 3401 C CG . LEU A 476 ? 0.2301 0.1690 0.2045 0.0510 -0.0711 -0.0455 469 LEU A CG 3402 C CD1 . LEU A 476 ? 0.2293 0.2532 0.2406 0.0501 -0.0374 -0.0117 469 LEU A CD1 3403 C CD2 . LEU A 476 ? 0.2833 0.1835 0.1893 0.0649 -0.0564 -0.0686 469 LEU A CD2 3404 N N . MET A 477 ? 0.2139 0.2303 0.2352 0.0408 -0.0469 -0.0337 470 MET A N 3405 C CA . MET A 477 ? 0.2383 0.2091 0.2319 0.0545 -0.0699 -0.0486 470 MET A CA 3406 C C . MET A 477 ? 0.2481 0.2238 0.2654 0.0529 -0.0721 -0.0260 470 MET A C 3407 O O . MET A 477 ? 0.2562 0.2005 0.2515 0.0590 -0.0547 -0.0311 470 MET A O 3408 C CB . MET A 477 ? 0.2467 0.2143 0.2374 0.0283 -0.0923 -0.0187 470 MET A CB 3409 C CG . MET A 477 ? 0.2458 0.2781 0.2459 0.0614 -0.0711 -0.0168 470 MET A CG 3410 S SD . MET A 477 ? 0.2757 0.2712 0.3388 0.0262 -0.0698 -0.0170 470 MET A SD 3411 C CE . MET A 477 ? 0.2569 0.3257 0.2891 0.0474 -0.0838 -0.0265 470 MET A CE 3412 N N . TYR A 478 ? 0.2355 0.2243 0.2363 0.0348 -0.0831 -0.0471 471 TYR A N 3413 C CA . TYR A 478 ? 0.2459 0.2508 0.2518 0.0343 -0.0828 -0.0391 471 TYR A CA 3414 C C . TYR A 478 ? 0.2719 0.2500 0.2520 0.0662 -0.0793 -0.0472 471 TYR A C 3415 O O . TYR A 478 ? 0.2539 0.2549 0.2645 0.0624 -0.0746 -0.0191 471 TYR A O 3416 C CB . TYR A 478 ? 0.2187 0.2478 0.2575 0.0178 -0.0809 -0.0454 471 TYR A CB 3417 C CG . TYR A 478 ? 0.2629 0.2171 0.2438 0.0332 -0.0741 -0.0538 471 TYR A CG 3418 C CD1 . TYR A 478 ? 0.2311 0.2211 0.2523 0.0485 -0.0861 -0.0575 471 TYR A CD1 3419 C CD2 . TYR A 478 ? 0.2664 0.2407 0.2709 0.0229 -0.0737 -0.0267 471 TYR A CD2 3420 C CE1 . TYR A 478 ? 0.2753 0.2310 0.2682 0.0727 -0.0517 -0.0170 471 TYR A CE1 3421 C CE2 . TYR A 478 ? 0.2273 0.2770 0.2592 0.0335 -0.0669 -0.0240 471 TYR A CE2 3422 C CZ . TYR A 478 ? 0.2958 0.2431 0.2672 0.0430 -0.0698 -0.0190 471 TYR A CZ 3423 O OH . TYR A 478 ? 0.2864 0.2536 0.2692 0.0361 -0.0617 -0.0038 471 TYR A OH 3424 N N . SER A 479 ? 0.2741 0.2394 0.2781 0.0533 -0.0906 -0.0709 472 SER A N 3425 C CA . SER A 479 ? 0.3342 0.2486 0.2602 0.0470 -0.0811 -0.0653 472 SER A CA 3426 C C . SER A 479 ? 0.3088 0.2640 0.2464 0.0732 -0.0949 -0.0482 472 SER A C 3427 O O . SER A 479 ? 0.3100 0.2673 0.2572 0.0985 -0.0834 -0.0548 472 SER A O 3428 C CB . SER A 479 ? 0.3500 0.2495 0.2475 0.0632 -0.1202 -0.0729 472 SER A CB 3429 O OG A SER A 479 ? 0.4145 0.2633 0.3163 0.0911 -0.0988 -0.0366 472 SER A OG 3430 O OG B SER A 479 ? 0.2523 0.2317 0.2526 0.0583 -0.1096 -0.1018 472 SER A OG 3431 N N . LEU A 480 ? 0.3081 0.2309 0.2742 0.0911 -0.0955 -0.0620 473 LEU A N 3432 C CA . LEU A 480 ? 0.3088 0.2585 0.2866 0.0788 -0.0707 -0.0400 473 LEU A CA 3433 C C . LEU A 480 ? 0.3076 0.2635 0.2524 0.0845 -0.0673 -0.0321 473 LEU A C 3434 O O . LEU A 480 ? 0.2962 0.2620 0.2594 0.1055 -0.0751 -0.0484 473 LEU A O 3435 C CB . LEU A 480 ? 0.2860 0.2643 0.2808 0.0970 -0.0687 -0.0202 473 LEU A CB 3436 C CG . LEU A 480 ? 0.3099 0.2895 0.2625 0.0605 -0.0618 -0.0280 473 LEU A CG 3437 C CD1 . LEU A 480 ? 0.3806 0.3037 0.2901 0.0562 -0.0213 -0.0232 473 LEU A CD1 3438 C CD2 . LEU A 480 ? 0.2749 0.3348 0.3770 0.0421 -0.0481 -0.0392 473 LEU A CD2 3439 N N . VAL A 481 ? 0.2809 0.2408 0.2455 0.0902 -0.0744 -0.0723 474 VAL A N 3440 C CA . VAL A 481 ? 0.2569 0.2378 0.2511 0.0973 -0.0729 -0.0431 474 VAL A CA 3441 C C . VAL A 481 ? 0.2684 0.2655 0.2472 0.0998 -0.0709 -0.0615 474 VAL A C 3442 O O . VAL A 481 ? 0.3007 0.2752 0.2863 0.1011 -0.0800 -0.0356 474 VAL A O 3443 C CB . VAL A 481 ? 0.2645 0.2975 0.2528 0.1136 -0.0761 -0.0970 474 VAL A CB 3444 C CG1 . VAL A 481 ? 0.2817 0.3426 0.2652 0.1360 -0.0200 -0.0488 474 VAL A CG1 3445 C CG2 . VAL A 481 ? 0.3000 0.2927 0.2599 0.0707 -0.0815 -0.0622 474 VAL A CG2 3446 N N . HIS A 482 ? 0.2760 0.2698 0.2719 0.0866 -0.0888 -0.0643 475 HIS A N 3447 C CA . HIS A 482 ? 0.3432 0.2939 0.2692 0.0540 -0.1462 -0.0487 475 HIS A CA 3448 C C . HIS A 482 ? 0.3040 0.2761 0.2627 0.1060 -0.1259 -0.0546 475 HIS A C 3449 O O . HIS A 482 ? 0.3187 0.3020 0.2484 0.1189 -0.1113 -0.0270 475 HIS A O 3450 C CB . HIS A 482 ? 0.2885 0.2646 0.3408 0.0951 -0.1433 -0.0547 475 HIS A CB 3451 C CG . HIS A 482 ? 0.3633 0.3299 0.3648 0.1069 -0.1231 -0.0171 475 HIS A CG 3452 N ND1 . HIS A 482 ? 0.6495 0.3573 0.4433 -0.0200 -0.0705 0.0072 475 HIS A ND1 3453 C CD2 . HIS A 482 ? 0.3219 0.3825 0.3945 0.0689 -0.0918 -0.0458 475 HIS A CD2 3454 C CE1 . HIS A 482 ? 0.5680 0.4266 0.4257 0.0031 -0.0248 -0.0817 475 HIS A CE1 3455 N NE2 . HIS A 482 ? 0.3427 0.3646 0.4210 0.0200 -0.1482 -0.0458 475 HIS A NE2 3456 N N . ASN A 483 ? 0.3249 0.2759 0.2520 0.0787 -0.1007 -0.0557 476 ASN A N 3457 C CA . ASN A 483 ? 0.3182 0.2899 0.2446 0.1190 -0.1009 -0.0562 476 ASN A CA 3458 C C . ASN A 483 ? 0.3255 0.2973 0.2666 0.1013 -0.0988 -0.0635 476 ASN A C 3459 O O . ASN A 483 ? 0.3718 0.3270 0.2781 0.1110 -0.1155 -0.0465 476 ASN A O 3460 C CB . ASN A 483 ? 0.3288 0.2759 0.2395 0.1137 -0.1163 -0.1076 476 ASN A CB 3461 C CG . ASN A 483 ? 0.3384 0.2893 0.3248 0.0775 -0.0936 -0.0943 476 ASN A CG 3462 O OD1 . ASN A 483 ? 0.3339 0.3092 0.3603 0.0975 -0.0859 -0.0903 476 ASN A OD1 3463 N ND2 . ASN A 483 ? 0.4029 0.2633 0.2815 0.1002 -0.0974 -0.1055 476 ASN A ND2 3464 N N . LEU A 484 ? 0.3446 0.2652 0.2811 0.0897 -0.0892 -0.0745 477 LEU A N 3465 C CA . LEU A 484 ? 0.3302 0.2652 0.2591 0.0751 -0.1194 -0.0723 477 LEU A CA 3466 C C . LEU A 484 ? 0.3178 0.2961 0.2690 0.0809 -0.1294 -0.0606 477 LEU A C 3467 O O . LEU A 484 ? 0.3393 0.2947 0.2658 0.1189 -0.1032 -0.0595 477 LEU A O 3468 C CB . LEU A 484 ? 0.2972 0.2879 0.2419 0.0727 -0.1031 -0.0764 477 LEU A CB 3469 C CG . LEU A 484 ? 0.3242 0.3007 0.2295 0.0766 -0.1040 -0.0602 477 LEU A CG 3470 C CD1 . LEU A 484 ? 0.3699 0.3237 0.2438 0.0944 -0.0925 -0.0480 477 LEU A CD1 3471 C CD2 . LEU A 484 ? 0.3180 0.2836 0.2436 0.0864 -0.1232 -0.0446 477 LEU A CD2 3472 N N . THR A 485 ? 0.2931 0.3155 0.2785 0.0891 -0.1204 -0.0816 478 THR A N 3473 C CA . THR A 485 ? 0.3272 0.3091 0.3152 0.1172 -0.1085 -0.0796 478 THR A CA 3474 C C . THR A 485 ? 0.3332 0.2735 0.3224 0.1363 -0.1135 -0.0653 478 THR A C 3475 O O . THR A 485 ? 0.3157 0.2740 0.3242 0.1367 -0.1316 -0.0595 478 THR A O 3476 C CB . THR A 485 ? 0.2949 0.2871 0.3013 0.0837 -0.1593 -0.0542 478 THR A CB 3477 O OG1 . THR A 485 ? 0.2931 0.2789 0.3013 0.0737 -0.0896 -0.0748 478 THR A OG1 3478 C CG2 . THR A 485 ? 0.2470 0.3031 0.3062 0.0561 -0.1460 -0.0231 478 THR A CG2 3479 N N . LYS A 486 ? 0.3698 0.3162 0.2883 0.1402 -0.1180 -0.1007 479 LYS A N 3480 C CA . LYS A 486 ? 0.4080 0.3239 0.3304 0.1261 -0.1636 -0.0706 479 LYS A CA 3481 C C . LYS A 486 ? 0.3900 0.3379 0.3100 0.1557 -0.1619 -0.0795 479 LYS A C 3482 O O . LYS A 486 ? 0.3908 0.3787 0.3434 0.1589 -0.1796 -0.0786 479 LYS A O 3483 C CB . LYS A 486 ? 0.4177 0.3246 0.3060 0.0964 -0.1213 -0.0872 479 LYS A CB 3484 C CG . LYS A 486 ? 0.3706 0.3237 0.3399 0.1306 -0.1207 -0.0745 479 LYS A CG 3485 C CD . LYS A 486 ? 0.3921 0.3107 0.4038 0.1092 -0.1426 -0.0671 479 LYS A CD 3486 C CE . LYS A 486 ? 0.4956 0.3159 0.3669 0.1203 -0.0865 -0.0943 479 LYS A CE 3487 N NZ . LYS A 486 ? 0.4483 0.3514 0.5018 0.0605 -0.1289 -0.1685 479 LYS A NZ 3488 N N . GLU A 487 ? 0.4199 0.3430 0.3242 0.1426 -0.1230 -0.1031 480 GLU A N 3489 C CA . GLU A 487 ? 0.4483 0.3342 0.3673 0.1406 -0.1247 -0.0876 480 GLU A CA 3490 C C . GLU A 487 ? 0.4863 0.3308 0.3245 0.1393 -0.1089 -0.0567 480 GLU A C 3491 O O . GLU A 487 ? 0.5857 0.3533 0.3749 0.1384 -0.1163 -0.0196 480 GLU A O 3492 C CB . GLU A 487 ? 0.4705 0.3828 0.3894 0.1444 -0.0766 -0.0724 480 GLU A CB 3493 C CG . GLU A 487 ? 0.5956 0.3552 0.4435 0.1317 -0.1505 -0.0378 480 GLU A CG 3494 C CD . GLU A 487 ? 0.6801 0.4635 0.4330 0.1313 -0.1444 -0.1198 480 GLU A CD 3495 O OE1 . GLU A 487 ? 0.6367 0.4784 0.6687 0.1031 -0.1107 -0.0137 480 GLU A OE1 3496 O OE2 . GLU A 487 ? 0.7654 0.5243 0.4310 0.1974 -0.1011 -0.0932 480 GLU A OE2 3497 N N . LEU A 488 ? 0.3904 0.3381 0.3237 0.1201 -0.1355 -0.1012 481 LEU A N 3498 C CA . LEU A 488 ? 0.3828 0.3037 0.3077 0.1406 -0.1600 -0.0380 481 LEU A CA 3499 C C . LEU A 488 ? 0.3524 0.3465 0.3529 0.1275 -0.1673 -0.0361 481 LEU A C 3500 O O . LEU A 488 ? 0.3820 0.3434 0.3476 0.0967 -0.1425 -0.0300 481 LEU A O 3501 C CB . LEU A 488 ? 0.3317 0.3868 0.3208 0.1098 -0.1587 -0.0596 481 LEU A CB 3502 C CG . LEU A 488 ? 0.3460 0.3242 0.2598 0.1096 -0.1419 -0.0321 481 LEU A CG 3503 C CD1 . LEU A 488 ? 0.2778 0.3177 0.2717 0.1196 -0.1477 -0.0462 481 LEU A CD1 3504 C CD2 . LEU A 488 ? 0.3712 0.3259 0.2605 0.0693 -0.1313 -0.0302 481 LEU A CD2 3505 N N . LYS A 489 ? 0.3590 0.3449 0.3096 0.1450 -0.1457 -0.0543 482 LYS A N 3506 C CA . LYS A 489 ? 0.3615 0.3507 0.3385 0.1650 -0.1444 -0.0427 482 LYS A CA 3507 C C . LYS A 489 ? 0.3666 0.3732 0.3508 0.1291 -0.1184 -0.0499 482 LYS A C 3508 O O . LYS A 489 ? 0.3804 0.4099 0.3310 0.0966 -0.0875 -0.0898 482 LYS A O 3509 C CB . LYS A 489 ? 0.4235 0.3620 0.3549 0.1301 -0.1422 -0.0277 482 LYS A CB 3510 C CG . LYS A 489 ? 0.4241 0.4729 0.3742 0.2051 -0.1249 0.0422 482 LYS A CG 3511 C CD . LYS A 489 ? 0.5716 0.5108 0.4423 0.1763 -0.1864 0.0826 482 LYS A CD 3512 C CE . LYS A 489 ? 0.6451 0.6901 0.4568 0.1414 -0.1544 0.1077 482 LYS A CE 3513 N NZ . LYS A 489 ? 0.6432 0.5828 0.4445 0.1656 -0.1604 0.0855 482 LYS A NZ 3514 N N . SER A 490 ? 0.3242 0.3230 0.3410 0.1496 -0.1203 -0.0807 483 SER A N 3515 C CA . SER A 490 ? 0.3857 0.3249 0.3360 0.1100 -0.1249 -0.0917 483 SER A CA 3516 C C . SER A 490 ? 0.3275 0.3220 0.3653 0.1214 -0.1426 -0.0471 483 SER A C 3517 O O . SER A 490 ? 0.3187 0.3671 0.3948 0.1388 -0.1424 -0.0194 483 SER A O 3518 C CB . SER A 490 ? 0.3479 0.3635 0.3543 0.1614 -0.0953 -0.0540 483 SER A CB 3519 O OG . SER A 490 ? 0.3492 0.3526 0.3798 0.1061 -0.1212 -0.0835 483 SER A OG 3520 N N . PRO A 491 ? 0.2997 0.3008 0.3759 0.1219 -0.1305 -0.0656 484 PRO A N 3521 C CA . PRO A 491 ? 0.3036 0.3093 0.3895 0.1254 -0.1285 -0.0822 484 PRO A CA 3522 C C . PRO A 491 ? 0.2962 0.3091 0.4649 0.1450 -0.1177 -0.0494 484 PRO A C 3523 O O . PRO A 491 ? 0.3012 0.3064 0.4453 0.1227 -0.0953 -0.0840 484 PRO A O 3524 C CB . PRO A 491 ? 0.2821 0.3052 0.3727 0.1271 -0.1335 -0.0455 484 PRO A CB 3525 C CG . PRO A 491 ? 0.3011 0.2714 0.3594 0.0867 -0.0895 -0.0576 484 PRO A CG 3526 C CD . PRO A 491 ? 0.2914 0.3301 0.3871 0.0897 -0.1525 -0.0750 484 PRO A CD 3527 N N . ASP A 492 ? 0.3117 0.3293 0.4680 0.1142 -0.1065 -0.0736 485 ASP A N 3528 C CA . ASP A 492 ? 0.3149 0.3568 0.4687 0.1230 -0.1016 -0.0489 485 ASP A CA 3529 C C . ASP A 492 ? 0.3344 0.3573 0.4504 0.1080 -0.1373 -0.0813 485 ASP A C 3530 O O . ASP A 492 ? 0.3138 0.3857 0.4436 0.0993 -0.1397 -0.0707 485 ASP A O 3531 C CB . ASP A 492 ? 0.3290 0.3305 0.3906 0.0762 -0.1265 -0.0747 485 ASP A CB 3532 C CG . ASP A 492 ? 0.3372 0.3117 0.4268 0.0771 -0.1342 -0.0744 485 ASP A CG 3533 O OD1 . ASP A 492 ? 0.3160 0.3425 0.4533 0.0967 -0.1444 -0.0587 485 ASP A OD1 3534 O OD2 . ASP A 492 ? 0.3511 0.3339 0.3696 0.0660 -0.0726 -0.0818 485 ASP A OD2 3535 N N . GLU A 493 ? 0.3287 0.4017 0.4890 0.1280 -0.1285 -0.0924 486 GLU A N 3536 C CA . GLU A 493 ? 0.3362 0.3896 0.5324 0.1434 -0.1260 -0.1201 486 GLU A CA 3537 C C . GLU A 493 ? 0.3117 0.4363 0.5073 0.1398 -0.1609 -0.0857 486 GLU A C 3538 O O . GLU A 493 ? 0.3827 0.4133 0.4890 0.1088 -0.1466 -0.1051 486 GLU A O 3539 C CB . GLU A 493 ? 0.3879 0.4024 0.5680 0.1092 -0.0153 -0.1263 486 GLU A CB 3540 C CG . GLU A 493 ? 0.3729 0.4506 0.6364 0.0832 -0.0860 -0.2079 486 GLU A CG 3541 C CD . GLU A 493 ? 0.4331 0.5836 0.6476 0.0685 -0.1253 -0.2172 486 GLU A CD 3542 O OE1 . GLU A 493 ? 0.4501 0.6023 0.6131 -0.0018 -0.0598 -0.2191 486 GLU A OE1 3543 O OE2 . GLU A 493 ? 0.4973 0.5227 0.7464 0.0980 -0.0293 -0.2185 486 GLU A OE2 3544 N N . GLY A 494 ? 0.3169 0.4807 0.5243 0.1446 -0.1719 -0.1185 487 GLY A N 3545 C CA . GLY A 494 ? 0.3943 0.4095 0.5323 0.1437 -0.1505 -0.0744 487 GLY A CA 3546 C C . GLY A 494 ? 0.3696 0.4489 0.5638 0.1486 -0.1305 -0.0796 487 GLY A C 3547 O O . GLY A 494 ? 0.3526 0.5529 0.5864 0.1210 -0.1591 -0.0935 487 GLY A O 3548 N N . PHE A 495 ? 0.3462 0.4020 0.5421 0.1666 -0.1438 -0.0680 488 PHE A N 3549 C CA . PHE A 495 ? 0.3271 0.4127 0.4869 0.1730 -0.1922 -0.0626 488 PHE A CA 3550 C C . PHE A 495 ? 0.3905 0.4475 0.4540 0.1752 -0.2250 -0.0600 488 PHE A C 3551 O O . PHE A 495 ? 0.4560 0.4193 0.4084 0.1603 -0.1980 -0.1295 488 PHE A O 3552 C CB . PHE A 495 ? 0.3490 0.4623 0.4347 0.1454 -0.2193 -0.0687 488 PHE A CB 3553 C CG . PHE A 495 ? 0.3416 0.4402 0.4862 0.1503 -0.1993 -0.0523 488 PHE A CG 3554 C CD1 . PHE A 495 ? 0.3384 0.4531 0.5470 0.1369 -0.1789 -0.0509 488 PHE A CD1 3555 C CD2 . PHE A 495 ? 0.3472 0.4899 0.5062 0.1130 -0.1774 -0.0892 488 PHE A CD2 3556 C CE1 . PHE A 495 ? 0.4245 0.4341 0.5689 0.1458 -0.1144 -0.0747 488 PHE A CE1 3557 C CE2 . PHE A 495 ? 0.4017 0.4590 0.5491 0.1025 -0.1447 -0.0864 488 PHE A CE2 3558 C CZ . PHE A 495 ? 0.4394 0.4590 0.5312 0.0960 -0.1503 -0.1023 488 PHE A CZ 3559 N N . GLU A 496 ? 0.3691 0.4404 0.5399 0.1974 -0.1826 -0.0458 489 GLU A N 3560 C CA . GLU A 496 ? 0.5152 0.4539 0.4775 0.1783 -0.1753 -0.0582 489 GLU A CA 3561 C C . GLU A 496 ? 0.4071 0.4145 0.4854 0.1922 -0.2198 -0.0498 489 GLU A C 3562 O O . GLU A 496 ? 0.4546 0.5806 0.3558 0.1038 -0.1892 -0.0757 489 GLU A O 3563 C CB . GLU A 496 ? 0.5315 0.5061 0.6918 0.1626 -0.1645 0.0729 489 GLU A CB 3564 C CG . GLU A 496 ? 0.5948 0.5867 0.5711 0.1634 -0.1281 0.1420 489 GLU A CG 3565 C CD . GLU A 496 ? 0.5150 0.4848 0.5429 0.1821 -0.2671 0.0713 489 GLU A CD 3566 O OE1 . GLU A 496 ? 0.4959 0.5328 0.6152 0.0944 -0.2221 0.0607 489 GLU A OE1 3567 O OE2 . GLU A 496 ? 0.5179 0.5115 0.6038 0.1727 -0.1165 -0.0263 489 GLU A OE2 3568 N N . GLY A 497 ? 0.4648 0.4546 0.4733 0.1565 -0.1477 -0.0787 490 GLY A N 3569 C CA . GLY A 497 ? 0.5336 0.4302 0.4796 0.1680 -0.1352 -0.0739 490 GLY A CA 3570 C C . GLY A 497 ? 0.5107 0.4227 0.4542 0.1565 -0.1662 -0.0812 490 GLY A C 3571 O O . GLY A 497 ? 0.5176 0.5142 0.4275 0.1866 -0.1546 -0.1089 490 GLY A O 3572 N N . LYS A 498 ? 0.4529 0.4101 0.4475 0.1630 -0.2092 -0.0593 491 LYS A N 3573 C CA . LYS A 498 ? 0.3696 0.3912 0.5437 0.1825 -0.1789 -0.0740 491 LYS A CA 3574 C C . LYS A 498 ? 0.3763 0.3725 0.4792 0.1470 -0.1763 -0.0812 491 LYS A C 3575 O O . LYS A 498 ? 0.3817 0.3523 0.4878 0.1409 -0.1859 -0.0508 491 LYS A O 3576 C CB . LYS A 498 ? 0.3810 0.4038 0.5108 0.1462 -0.1818 -0.1010 491 LYS A CB 3577 C CG . LYS A 498 ? 0.3838 0.4999 0.5601 0.1504 -0.2217 -0.0731 491 LYS A CG 3578 C CD . LYS A 498 ? 0.4590 0.5065 0.5859 0.1523 -0.2102 -0.0723 491 LYS A CD 3579 C CE . LYS A 498 ? 0.4089 0.6518 0.8148 0.1055 -0.0765 -0.0427 491 LYS A CE 3580 N NZ . LYS A 498 ? 0.3122 0.8195 0.9249 -0.0161 -0.0504 -0.0768 491 LYS A NZ 3581 N N . SER A 499 ? 0.3479 0.3718 0.3961 0.1476 -0.1902 -0.0681 492 SER A N 3582 C CA . SER A 499 ? 0.3397 0.3360 0.3813 0.1622 -0.1646 -0.0622 492 SER A CA 3583 C C . SER A 499 ? 0.2956 0.3261 0.3945 0.1441 -0.1778 -0.0678 492 SER A C 3584 O O . SER A 499 ? 0.3097 0.3076 0.4121 0.1313 -0.1400 -0.1013 492 SER A O 3585 C CB . SER A 499 ? 0.3689 0.3275 0.3836 0.1314 -0.1220 -0.0700 492 SER A CB 3586 O OG . SER A 499 ? 0.3963 0.3500 0.4047 0.1203 -0.1511 -0.0535 492 SER A OG 3587 N N . LEU A 500 ? 0.3313 0.3175 0.3407 0.1244 -0.1976 -0.0911 493 LEU A N 3588 C CA . LEU A 500 ? 0.2972 0.3244 0.3310 0.1014 -0.1810 -0.0608 493 LEU A CA 3589 C C . LEU A 500 ? 0.3288 0.3019 0.3606 0.0988 -0.1277 -0.0885 493 LEU A C 3590 O O . LEU A 500 ? 0.3208 0.2735 0.3798 0.0986 -0.1105 -0.0711 493 LEU A O 3591 C CB . LEU A 500 ? 0.2680 0.2972 0.3260 0.1203 -0.1523 -0.0818 493 LEU A CB 3592 C CG . LEU A 500 ? 0.2808 0.3148 0.2951 0.1217 -0.1105 -0.0976 493 LEU A CG 3593 C CD1 . LEU A 500 ? 0.3322 0.2746 0.3056 0.1241 -0.0810 -0.0799 493 LEU A CD1 3594 C CD2 . LEU A 500 ? 0.2556 0.3250 0.2839 0.1482 -0.0847 -0.0148 493 LEU A CD2 3595 N N . TYR A 501 ? 0.2767 0.2927 0.3816 0.0941 -0.1651 -0.0977 494 TYR A N 3596 C CA . TYR A 501 ? 0.3013 0.2959 0.4017 0.0928 -0.1067 -0.1166 494 TYR A CA 3597 C C . TYR A 501 ? 0.2882 0.3384 0.4114 0.0914 -0.1363 -0.1146 494 TYR A C 3598 O O . TYR A 501 ? 0.2944 0.3457 0.4125 0.0687 -0.1456 -0.1141 494 TYR A O 3599 C CB . TYR A 501 ? 0.3404 0.2943 0.3679 0.1224 -0.1146 -0.0921 494 TYR A CB 3600 C CG . TYR A 501 ? 0.3198 0.3206 0.4014 0.0922 -0.1152 -0.0913 494 TYR A CG 3601 C CD1 . TYR A 501 ? 0.3320 0.3065 0.3707 0.1078 -0.1078 -0.1042 494 TYR A CD1 3602 C CD2 . TYR A 501 ? 0.3365 0.3412 0.4047 0.0678 -0.0987 -0.0855 494 TYR A CD2 3603 C CE1 . TYR A 501 ? 0.2637 0.3297 0.3893 0.1024 -0.1104 -0.0818 494 TYR A CE1 3604 C CE2 . TYR A 501 ? 0.3290 0.3202 0.3858 0.1016 -0.1186 -0.0793 494 TYR A CE2 3605 C CZ . TYR A 501 ? 0.3140 0.3120 0.3723 0.0840 -0.1350 -0.1126 494 TYR A CZ 3606 O OH . TYR A 501 ? 0.4151 0.2997 0.5293 0.0694 -0.1217 -0.1149 494 TYR A OH 3607 N N . GLU A 502 ? 0.3182 0.3085 0.3718 0.0844 -0.1283 -0.1172 495 GLU A N 3608 C CA . GLU A 502 ? 0.3096 0.3779 0.4168 0.1110 -0.1504 -0.1269 495 GLU A CA 3609 C C . GLU A 502 ? 0.3061 0.3282 0.3947 0.1016 -0.1268 -0.0969 495 GLU A C 3610 O O . GLU A 502 ? 0.3022 0.3762 0.4016 0.0748 -0.1261 -0.0920 495 GLU A O 3611 C CB . GLU A 502 ? 0.2954 0.4346 0.4488 0.0592 -0.1685 -0.0768 495 GLU A CB 3612 C CG . GLU A 502 ? 0.3009 0.4665 0.5048 0.0782 -0.1590 -0.0783 495 GLU A CG 3613 C CD . GLU A 502 ? 0.3971 0.5519 0.5403 0.1182 -0.1901 -0.0594 495 GLU A CD 3614 O OE1 . GLU A 502 ? 0.4919 0.7255 0.5205 0.0708 -0.2134 -0.1413 495 GLU A OE1 3615 O OE2 . GLU A 502 ? 0.3564 0.8200 0.6382 0.1417 -0.1574 -0.1258 495 GLU A OE2 3616 N N . SER A 503 ? 0.2890 0.3337 0.3889 0.0935 -0.1521 -0.1057 496 SER A N 3617 C CA . SER A 503 ? 0.2992 0.3128 0.4058 0.0798 -0.1166 -0.1001 496 SER A CA 3618 C C . SER A 503 ? 0.2535 0.3007 0.4273 0.0700 -0.1155 -0.0857 496 SER A C 3619 O O . SER A 503 ? 0.2965 0.3352 0.4493 0.0641 -0.0761 -0.0914 496 SER A O 3620 C CB . SER A 503 ? 0.2986 0.3257 0.3874 0.1009 -0.1133 -0.0691 496 SER A CB 3621 O OG . SER A 503 ? 0.3191 0.3205 0.3816 0.0995 -0.1128 -0.0764 496 SER A OG 3622 N N . TRP A 504 ? 0.2681 0.3119 0.4060 0.0984 -0.1003 -0.0907 497 TRP A N 3623 C CA . TRP A 504 ? 0.2654 0.2915 0.4157 0.0739 -0.0832 -0.0507 497 TRP A CA 3624 C C . TRP A 504 ? 0.2887 0.2902 0.4248 0.0462 -0.1017 -0.1010 497 TRP A C 3625 O O . TRP A 504 ? 0.2894 0.3004 0.4415 0.0494 -0.0945 -0.0823 497 TRP A O 3626 C CB . TRP A 504 ? 0.2584 0.2863 0.4167 0.0879 -0.0952 -0.0505 497 TRP A CB 3627 C CG . TRP A 504 ? 0.2670 0.2708 0.3586 0.0518 -0.0900 -0.0732 497 TRP A CG 3628 C CD1 . TRP A 504 ? 0.2471 0.2915 0.3487 0.0090 -0.1046 -0.0411 497 TRP A CD1 3629 C CD2 . TRP A 504 ? 0.2696 0.2673 0.3530 0.0439 -0.0526 -0.0560 497 TRP A CD2 3630 N NE1 . TRP A 504 ? 0.2211 0.2799 0.3676 0.0366 -0.0507 -0.0366 497 TRP A NE1 3631 C CE2 . TRP A 504 ? 0.2598 0.2981 0.3578 0.0384 -0.0590 -0.0600 497 TRP A CE2 3632 C CE3 . TRP A 504 ? 0.2694 0.2671 0.3477 0.0546 -0.0528 -0.0720 497 TRP A CE3 3633 C CZ2 . TRP A 504 ? 0.2465 0.2871 0.3730 0.0188 -0.0654 -0.0639 497 TRP A CZ2 3634 C CZ3 . TRP A 504 ? 0.2794 0.2735 0.3444 0.0672 -0.0791 -0.0315 497 TRP A CZ3 3635 C CH2 . TRP A 504 ? 0.2149 0.2915 0.3445 0.0560 -0.1114 -0.0612 497 TRP A CH2 3636 N N . THR A 505 ? 0.2398 0.2955 0.4184 0.0375 -0.1230 -0.0918 498 THR A N 3637 C CA . THR A 505 ? 0.2887 0.3252 0.4599 -0.0016 -0.0782 -0.1200 498 THR A CA 3638 C C . THR A 505 ? 0.2909 0.3416 0.4799 0.0648 -0.0886 -0.0812 498 THR A C 3639 O O . THR A 505 ? 0.2915 0.3526 0.4836 0.0391 -0.0555 -0.0820 498 THR A O 3640 C CB . THR A 505 ? 0.3075 0.3113 0.4346 0.0325 -0.1160 -0.1087 498 THR A CB 3641 O OG1 A THR A 505 ? 0.3396 0.3366 0.4218 0.0717 -0.1159 -0.1189 498 THR A OG1 3642 C CG2 A THR A 505 ? 0.3706 0.3421 0.5129 -0.0022 -0.0895 -0.1058 498 THR A CG2 3643 N N . LYS A 506 ? 0.2834 0.3171 0.4845 0.0651 -0.0997 -0.1213 499 LYS A N 3644 C CA . LYS A 506 ? 0.2667 0.3710 0.5028 0.0692 -0.1139 -0.1039 499 LYS A CA 3645 C C . LYS A 506 ? 0.2655 0.3855 0.5019 0.0476 -0.0688 -0.0941 499 LYS A C 3646 O O . LYS A 506 ? 0.3457 0.3725 0.5145 0.0188 -0.0662 -0.0797 499 LYS A O 3647 C CB . LYS A 506 ? 0.3377 0.3409 0.5094 0.0539 -0.0988 -0.0833 499 LYS A CB 3648 C CG . LYS A 506 ? 0.3383 0.5583 0.6190 0.1396 -0.0502 -0.0795 499 LYS A CG 3649 C CD . LYS A 506 ? 0.4219 0.5981 0.5802 0.1143 -0.0746 -0.0950 499 LYS A CD 3650 C CE . LYS A 506 ? 0.4048 0.4457 0.4411 0.1100 -0.0843 -0.0943 499 LYS A CE 3651 N NZ . LYS A 506 ? 0.1453 0.4533 0.4209 0.1570 -0.1012 -0.1098 499 LYS A NZ 3652 N N . LYS A 507 ? 0.3252 0.3022 0.4782 0.0649 -0.0852 -0.1149 500 LYS A N 3653 C CA . LYS A 507 ? 0.2954 0.3334 0.4507 0.0386 -0.0625 -0.0892 500 LYS A CA 3654 C C . LYS A 507 ? 0.2832 0.3580 0.4638 0.0382 -0.0547 -0.0845 500 LYS A C 3655 O O . LYS A 507 ? 0.3318 0.4103 0.4494 0.0629 -0.0346 -0.0878 500 LYS A O 3656 C CB . LYS A 507 ? 0.3283 0.3118 0.4735 0.0494 -0.0509 -0.0973 500 LYS A CB 3657 C CG . LYS A 507 ? 0.2864 0.3348 0.5284 0.0342 -0.0470 -0.0533 500 LYS A CG 3658 C CD . LYS A 507 ? 0.2664 0.2992 0.4306 0.0525 -0.0722 -0.0623 500 LYS A CD 3659 C CE . LYS A 507 ? 0.3201 0.3285 0.4982 0.0922 -0.0735 -0.0561 500 LYS A CE 3660 N NZ . LYS A 507 ? 0.2907 0.3469 0.4619 0.0763 -0.0506 0.0134 500 LYS A NZ 3661 N N . SER A 508 ? 0.2548 0.3156 0.4863 0.0254 -0.1045 -0.0973 501 SER A N 3662 C CA . SER A 508 ? 0.2555 0.3406 0.4765 0.0098 -0.0710 -0.0614 501 SER A CA 3663 C C . SER A 508 ? 0.2295 0.3583 0.4975 0.0138 -0.1035 -0.0692 501 SER A C 3664 O O . SER A 508 ? 0.2884 0.3292 0.4709 0.0416 -0.0539 -0.0645 501 SER A O 3665 C CB . SER A 508 ? 0.2261 0.3736 0.4998 0.0372 -0.0990 -0.0605 501 SER A CB 3666 O OG . SER A 508 ? 0.3614 0.3567 0.5305 0.0198 -0.1096 -0.0238 501 SER A OG 3667 N N . PRO A 509 ? 0.2665 0.3368 0.5427 -0.0119 -0.0749 -0.0950 502 PRO A N 3668 C CA . PRO A 509 ? 0.2569 0.3285 0.5632 -0.0170 -0.0873 -0.0822 502 PRO A CA 3669 C C . PRO A 509 ? 0.2947 0.3559 0.5812 0.0017 -0.0712 -0.0446 502 PRO A C 3670 O O . PRO A 509 ? 0.2409 0.3575 0.6109 0.0079 -0.0604 -0.0618 502 PRO A O 3671 C CB . PRO A 509 ? 0.2555 0.3601 0.6028 -0.0175 -0.0724 -0.0738 502 PRO A CB 3672 C CG . PRO A 509 ? 0.2696 0.3639 0.5762 -0.0449 -0.0443 -0.0682 502 PRO A CG 3673 C CD . PRO A 509 ? 0.2486 0.3393 0.5654 -0.0120 -0.0758 -0.0951 502 PRO A CD 3674 N N . SER A 510 ? 0.3464 0.3436 0.6398 -0.0027 -0.0507 -0.0557 503 SER A N 3675 C CA . SER A 510 ? 0.4461 0.3854 0.6432 0.0426 -0.0487 -0.0415 503 SER A CA 3676 C C . SER A 510 ? 0.4190 0.4580 0.6590 0.0230 -0.0537 -0.0329 503 SER A C 3677 O O . SER A 510 ? 0.4422 0.3859 0.6946 -0.0103 -0.0519 0.0086 503 SER A O 3678 C CB . SER A 510 ? 0.3648 0.3921 0.6330 0.0101 -0.0520 -0.0748 503 SER A CB 3679 O OG . SER A 510 ? 0.4141 0.4705 0.6979 0.0569 -0.0635 -0.0013 503 SER A OG 3680 N N . PRO A 511 ? 0.5287 0.3984 0.6627 0.0516 -0.0720 -0.0179 504 PRO A N 3681 C CA . PRO A 511 ? 0.5339 0.5234 0.7037 -0.0205 -0.0485 -0.0499 504 PRO A CA 3682 C C . PRO A 511 ? 0.5214 0.5149 0.8315 0.0002 -0.0401 -0.0376 504 PRO A C 3683 O O . PRO A 511 ? 0.6763 0.5715 0.7996 -0.0984 0.0253 0.0132 504 PRO A O 3684 C CB . PRO A 511 ? 0.5008 0.5811 0.6792 -0.0045 -0.0510 0.0636 504 PRO A CB 3685 C CG . PRO A 511 ? 0.4753 0.5519 0.6468 0.0358 -0.0893 -0.0362 504 PRO A CG 3686 C CD . PRO A 511 ? 0.4642 0.4500 0.6929 0.0734 -0.0365 -0.0134 504 PRO A CD 3687 N N . GLU A 512 ? 0.6787 0.5524 0.8442 0.0800 0.0098 -0.0500 505 GLU A N 3688 C CA . GLU A 512 ? 0.6131 0.6011 0.7836 -0.0853 -0.0489 -0.1202 505 GLU A CA 3689 C C . GLU A 512 ? 0.6191 0.6507 0.7882 -0.0704 -0.0756 -0.0622 505 GLU A C 3690 O O . GLU A 512 ? 0.8046 0.5811 0.8159 -0.0990 -0.0299 -0.0043 505 GLU A O 3691 C CB . GLU A 512 ? 0.6333 0.7802 0.8079 0.0198 -0.0861 -0.0646 505 GLU A CB 3692 C CG . GLU A 512 ? 0.6155 0.9152 0.8271 -0.0622 -0.0671 -0.0018 505 GLU A CG 3693 C CD . GLU A 512 ? 0.7544 0.8195 0.8807 -0.0279 0.0099 -0.0508 505 GLU A CD 3694 O OE1 . GLU A 512 ? 1.0898 1.2752 0.8734 0.1126 0.0878 -0.1004 505 GLU A OE1 3695 O OE2 . GLU A 512 ? 0.6583 0.6414 1.0320 0.1373 0.1236 -0.0118 505 GLU A OE2 3696 N N . PHE A 513 ? 0.5455 0.4597 0.7789 0.0363 -0.1142 -0.1226 506 PHE A N 3697 C CA . PHE A 513 ? 0.5327 0.5117 0.7917 0.0087 -0.1081 -0.0408 506 PHE A CA 3698 C C . PHE A 513 ? 0.4702 0.6015 0.7490 -0.0385 -0.1771 -0.0216 506 PHE A C 3699 O O . PHE A 513 ? 0.6036 0.5530 0.6866 0.0421 -0.2059 -0.0388 506 PHE A O 3700 C CB . PHE A 513 ? 0.6068 0.5806 0.8609 0.0694 -0.0663 -0.0865 506 PHE A CB 3701 C CG . PHE A 513 ? 0.5676 0.6420 0.9591 0.0689 -0.0883 -0.0289 506 PHE A CG 3702 C CD1 . PHE A 513 ? 0.5750 0.7180 0.8937 0.0692 -0.1040 -0.0351 506 PHE A CD1 3703 C CD2 . PHE A 513 ? 0.5942 0.6674 0.9370 0.0061 -0.1191 -0.0760 506 PHE A CD2 3704 C CE1 . PHE A 513 ? 0.6191 0.6822 0.9144 0.0302 -0.1587 0.0093 506 PHE A CE1 3705 C CE2 . PHE A 513 ? 0.6538 0.5630 0.9998 0.0328 -0.1153 -0.1818 506 PHE A CE2 3706 C CZ . PHE A 513 ? 0.6541 0.7077 0.9245 0.0700 -0.1934 -0.0503 506 PHE A CZ 3707 N N . SER A 514 ? 0.5725 0.6816 0.7262 -0.0830 -0.1913 -0.0259 507 SER A N 3708 C CA . SER A 514 ? 0.5230 0.6990 0.8525 -0.0463 -0.1543 0.0063 507 SER A CA 3709 C C . SER A 514 ? 0.5410 0.5521 0.8262 0.0278 -0.1257 -0.0235 507 SER A C 3710 O O . SER A 514 ? 0.5717 0.5941 0.7269 0.0513 -0.1300 -0.0052 507 SER A O 3711 C CB . SER A 514 ? 0.4931 0.7520 1.0402 -0.0830 -0.1042 -0.0516 507 SER A CB 3712 O OG . SER A 514 ? 0.5664 0.9393 1.0794 -0.1979 -0.0724 -0.2059 507 SER A OG 3713 N N . GLY A 515 ? 0.3531 0.4849 0.7813 -0.0477 -0.1578 -0.0487 508 GLY A N 3714 C CA . GLY A 515 ? 0.4159 0.4149 0.6652 -0.0713 -0.1680 -0.1359 508 GLY A CA 3715 C C . GLY A 515 ? 0.3732 0.3511 0.6176 0.0022 -0.1434 -0.1533 508 GLY A C 3716 O O . GLY A 515 ? 0.3963 0.4132 0.5952 0.0304 -0.1757 -0.0990 508 GLY A O 3717 N N . MET A 516 ? 0.3694 0.3473 0.5587 0.0447 -0.1182 -0.1542 509 MET A N 3718 C CA . MET A 516 ? 0.3360 0.3815 0.5340 0.0269 -0.0701 -0.1284 509 MET A CA 3719 C C . MET A 516 ? 0.3108 0.3123 0.5671 0.0311 -0.0911 -0.1032 509 MET A C 3720 O O . MET A 516 ? 0.4032 0.3319 0.6112 0.0122 -0.0358 -0.0550 509 MET A O 3721 C CB . MET A 516 ? 0.3336 0.3361 0.5558 -0.0071 -0.0759 -0.1128 509 MET A CB 3722 C CG . MET A 516 ? 0.4794 0.4378 0.7287 -0.0260 -0.0546 -0.2260 509 MET A CG 3723 S SD . MET A 516 ? 0.6191 0.6971 0.8480 -0.0609 0.0794 -0.2909 509 MET A SD 3724 C CE . MET A 516 ? 0.8257 0.5314 0.7621 -0.0243 -0.0439 -0.0871 509 MET A CE 3725 N N . PRO A 517 ? 0.3260 0.3378 0.5058 0.0088 -0.0752 -0.1018 510 PRO A N 3726 C CA . PRO A 517 ? 0.3231 0.3130 0.4816 0.0154 -0.0802 -0.0873 510 PRO A CA 3727 C C . PRO A 517 ? 0.3327 0.3437 0.4376 0.0208 -0.0451 -0.0814 510 PRO A C 3728 O O . PRO A 517 ? 0.3534 0.3347 0.4456 0.0294 -0.0776 -0.0476 510 PRO A O 3729 C CB . PRO A 517 ? 0.2884 0.3136 0.4355 0.0086 -0.0602 -0.1145 510 PRO A CB 3730 C CG . PRO A 517 ? 0.3144 0.2961 0.4148 0.0260 -0.0797 -0.1185 510 PRO A CG 3731 C CD . PRO A 517 ? 0.3163 0.3621 0.5131 -0.0080 -0.0842 -0.1265 510 PRO A CD 3732 N N . ARG A 518 ? 0.2376 0.3435 0.4256 -0.0008 -0.0574 -0.0822 511 ARG A N 3733 C CA . ARG A 518 ? 0.2656 0.3222 0.3878 0.0285 -0.0386 -0.0589 511 ARG A CA 3734 C C . ARG A 518 ? 0.2641 0.3060 0.3423 0.0525 -0.0595 -0.0623 511 ARG A C 3735 O O . ARG A 518 ? 0.2709 0.2937 0.3732 0.0533 -0.0490 -0.0631 511 ARG A O 3736 C CB . ARG A 518 ? 0.2766 0.3673 0.3954 0.0056 -0.0146 -0.0544 511 ARG A CB 3737 C CG . ARG A 518 ? 0.2272 0.4266 0.4279 0.0256 -0.0387 -0.0503 511 ARG A CG 3738 C CD . ARG A 518 ? 0.3220 0.4676 0.4721 0.0647 0.0320 -0.0174 511 ARG A CD 3739 N NE . ARG A 518 ? 0.3086 0.4620 0.5305 0.0394 -0.0091 -0.0398 511 ARG A NE 3740 C CZ . ARG A 518 ? 0.2883 0.5370 0.5550 0.0327 -0.0068 0.0058 511 ARG A CZ 3741 N NH1 . ARG A 518 ? 0.3465 0.5142 0.5568 0.0859 0.0057 0.0374 511 ARG A NH1 3742 N NH2 . ARG A 518 ? 0.2252 0.7122 0.7052 0.0687 0.0092 -0.0428 511 ARG A NH2 3743 N N . ILE A 519 ? 0.2483 0.2773 0.3610 0.0539 -0.0300 -0.0777 512 ILE A N 3744 C CA . ILE A 519 ? 0.2449 0.2922 0.3413 0.0544 -0.0179 -0.0436 512 ILE A CA 3745 C C . ILE A 519 ? 0.2529 0.2664 0.3672 0.0429 -0.0466 -0.0287 512 ILE A C 3746 O O . ILE A 519 ? 0.3421 0.2606 0.4265 0.0314 -0.0449 0.0155 512 ILE A O 3747 C CB . ILE A 519 ? 0.2056 0.3068 0.3320 0.0176 -0.0309 -0.0694 512 ILE A CB 3748 C CG1 . ILE A 519 ? 0.2699 0.2720 0.3332 0.0273 -0.0070 -0.0560 512 ILE A CG1 3749 C CG2 . ILE A 519 ? 0.2158 0.2755 0.3632 0.0147 -0.0397 -0.0570 512 ILE A CG2 3750 C CD1 . ILE A 519 ? 0.2796 0.3475 0.3111 0.0239 -0.0210 -0.0995 512 ILE A CD1 3751 N N . SER A 520 ? 0.2343 0.2660 0.3421 0.0222 -0.0109 -0.0198 513 SER A N 3752 C CA . SER A 520 ? 0.2319 0.2741 0.3595 0.0435 -0.0125 0.0127 513 SER A CA 3753 C C . SER A 520 ? 0.2241 0.2756 0.3146 0.0375 -0.0307 -0.0116 513 SER A C 3754 O O . SER A 520 ? 0.2124 0.2568 0.3495 0.0279 -0.0134 -0.0278 513 SER A O 3755 C CB . SER A 520 ? 0.2403 0.2947 0.3197 0.0476 0.0182 0.0144 513 SER A CB 3756 O OG . SER A 520 ? 0.2472 0.3891 0.4001 0.0593 0.0576 0.0317 513 SER A OG 3757 N N A LYS A 521 ? 0.2132 0.2773 0.3603 0.0386 -0.0156 0.0294 514 LYS A N 3758 N N B LYS A 521 ? 0.2129 0.2693 0.3365 0.0347 -0.0127 0.0106 514 LYS A N 3759 C CA A LYS A 521 ? 0.2188 0.2492 0.3347 0.0071 -0.0661 0.0203 514 LYS A CA 3760 C CA B LYS A 521 ? 0.2086 0.2324 0.2824 0.0187 -0.0291 -0.0049 514 LYS A CA 3761 C C A LYS A 521 ? 0.2194 0.2348 0.2857 0.0306 -0.0151 -0.0309 514 LYS A C 3762 C C B LYS A 521 ? 0.2167 0.2328 0.2819 0.0260 -0.0068 -0.0306 514 LYS A C 3763 O O A LYS A 521 ? 0.2511 0.2388 0.3388 0.0456 0.0191 -0.0189 514 LYS A O 3764 O O B LYS A 521 ? 0.2554 0.2243 0.3004 0.0421 0.0277 -0.0076 514 LYS A O 3765 C CB A LYS A 521 ? 0.2253 0.2678 0.3459 0.0269 -0.0789 0.0379 514 LYS A CB 3766 C CB B LYS A 521 ? 0.2122 0.2251 0.2554 0.0320 -0.0141 -0.0195 514 LYS A CB 3767 C CG A LYS A 521 ? 0.2753 0.3001 0.3925 -0.0009 -0.0582 -0.0037 514 LYS A CG 3768 C CG B LYS A 521 ? 0.1292 0.2042 0.2448 0.0400 -0.0252 -0.0243 514 LYS A CG 3769 C CD A LYS A 521 ? 0.3225 0.3439 0.3581 0.0322 -0.0059 0.0037 514 LYS A CD 3770 C CD B LYS A 521 ? 0.1819 0.2215 0.2278 0.0291 -0.0307 -0.0209 514 LYS A CD 3771 C CE A LYS A 521 ? 0.2733 0.4189 0.3886 0.0383 0.0004 -0.0364 514 LYS A CE 3772 C CE B LYS A 521 ? 0.1719 0.2344 0.2162 0.0235 -0.0143 -0.0172 514 LYS A CE 3773 N NZ A LYS A 521 ? 0.2655 0.4366 0.4107 0.0585 -0.0055 0.0188 514 LYS A NZ 3774 N NZ B LYS A 521 ? 0.1661 0.2736 0.2249 0.0319 -0.0299 -0.0029 514 LYS A NZ 3775 N N . LEU A 522 ? 0.2187 0.2358 0.2632 -0.0191 -0.0184 -0.0425 515 LEU A N 3776 C CA . LEU A 522 ? 0.2152 0.2632 0.2591 -0.0160 -0.0011 -0.0857 515 LEU A CA 3777 C C . LEU A 522 ? 0.3101 0.2677 0.2802 0.0127 -0.0055 -0.0257 515 LEU A C 3778 O O . LEU A 522 ? 0.3522 0.2554 0.3043 -0.0157 -0.0274 -0.0195 515 LEU A O 3779 C CB . LEU A 522 ? 0.2153 0.2767 0.2289 -0.0078 -0.0005 -0.0475 515 LEU A CB 3780 C CG . LEU A 522 ? 0.2578 0.2635 0.2509 0.0332 -0.0138 0.0034 515 LEU A CG 3781 C CD1 . LEU A 522 ? 0.2529 0.2978 0.2120 0.0096 -0.0062 0.0042 515 LEU A CD1 3782 C CD2 . LEU A 522 ? 0.2427 0.2478 0.2815 -0.0034 -0.0456 0.0302 515 LEU A CD2 3783 N N . GLY A 523 ? 0.2409 0.2644 0.2754 -0.0252 -0.0382 -0.0496 516 GLY A N 3784 C CA . GLY A 523 ? 0.3090 0.2498 0.2516 -0.0561 -0.0082 -0.0417 516 GLY A CA 3785 C C . GLY A 523 ? 0.2839 0.2577 0.2503 -0.0168 0.0159 -0.0440 516 GLY A C 3786 O O . GLY A 523 ? 0.3396 0.2245 0.3065 0.0029 0.0602 -0.0378 516 GLY A O 3787 N N . SER A 524 ? 0.2788 0.2261 0.2541 -0.0523 0.0120 -0.0287 517 SER A N 3788 C CA . SER A 524 ? 0.2346 0.2302 0.2703 -0.0015 0.0066 -0.0346 517 SER A CA 3789 C C . SER A 524 ? 0.2260 0.2256 0.2172 -0.0095 0.0166 -0.0296 517 SER A C 3790 O O . SER A 524 ? 0.2363 0.2393 0.2770 -0.0001 0.0185 -0.0442 517 SER A O 3791 C CB . SER A 524 ? 0.2538 0.2225 0.2289 0.0126 0.0133 -0.0115 517 SER A CB 3792 O OG . SER A 524 ? 0.2309 0.2587 0.2861 0.0390 0.0249 0.0044 517 SER A OG 3793 N N . GLY A 525 ? 0.2317 0.1937 0.2066 0.0102 0.0045 -0.0356 518 GLY A N 3794 C CA . GLY A 525 ? 0.2568 0.1838 0.2117 -0.0024 0.0441 -0.0320 518 GLY A CA 3795 C C . GLY A 525 ? 0.2232 0.1945 0.1921 0.0241 0.0089 -0.0286 518 GLY A C 3796 O O . GLY A 525 ? 0.2147 0.2007 0.2102 0.0154 0.0059 -0.0210 518 GLY A O 3797 N N . ASN A 526 ? 0.2127 0.1865 0.1916 0.0005 0.0264 -0.0195 519 ASN A N 3798 C CA . ASN A 526 ? 0.1910 0.2313 0.1880 0.0268 0.0156 -0.0088 519 ASN A CA 3799 C C . ASN A 526 ? 0.1796 0.1827 0.1967 0.0094 0.0136 -0.0033 519 ASN A C 3800 O O . ASN A 526 ? 0.1891 0.1874 0.1996 0.0167 0.0076 -0.0003 519 ASN A O 3801 C CB . ASN A 526 ? 0.2161 0.1976 0.2211 0.0093 -0.0088 -0.0011 519 ASN A CB 3802 C CG . ASN A 526 ? 0.2609 0.2127 0.2758 0.0564 0.0158 0.0013 519 ASN A CG 3803 O OD1 . ASN A 526 ? 0.2891 0.2543 0.2946 0.0110 0.0050 -0.0190 519 ASN A OD1 3804 N ND2 . ASN A 526 ? 0.2102 0.2735 0.1912 0.0307 0.0115 -0.0226 519 ASN A ND2 3805 N N . ASP A 527 ? 0.1559 0.1968 0.1811 -0.0046 0.0124 -0.0186 520 ASP A N 3806 C CA . ASP A 527 ? 0.1764 0.1635 0.2053 0.0088 0.0418 -0.0050 520 ASP A CA 3807 C C . ASP A 527 ? 0.1738 0.1728 0.1674 0.0158 0.0023 -0.0068 520 ASP A C 3808 O O . ASP A 527 ? 0.1897 0.1927 0.2156 0.0255 0.0172 -0.0301 520 ASP A O 3809 C CB . ASP A 527 ? 0.1941 0.1690 0.1848 -0.0001 0.0164 0.0099 520 ASP A CB 3810 C CG . ASP A 527 ? 0.2065 0.1890 0.2043 0.0114 0.0109 -0.0122 520 ASP A CG 3811 O OD1 . ASP A 527 ? 0.2391 0.1876 0.1918 -0.0041 0.0035 -0.0100 520 ASP A OD1 3812 O OD2 . ASP A 527 ? 0.2503 0.1929 0.2152 0.0198 0.0038 -0.0126 520 ASP A OD2 3813 N N . PHE A 528 ? 0.1940 0.1890 0.2001 0.0052 -0.0083 -0.0134 521 PHE A N 3814 C CA . PHE A 528 ? 0.2033 0.1802 0.2046 0.0269 -0.0239 -0.0071 521 PHE A CA 3815 C C . PHE A 528 ? 0.2113 0.1894 0.1781 0.0315 -0.0105 -0.0098 521 PHE A C 3816 O O . PHE A 528 ? 0.2427 0.1847 0.1940 0.0391 0.0024 -0.0021 521 PHE A O 3817 C CB . PHE A 528 ? 0.1854 0.2237 0.2281 0.0093 -0.0037 -0.0099 521 PHE A CB 3818 C CG . PHE A 528 ? 0.1975 0.1871 0.1903 -0.0116 -0.0119 0.0062 521 PHE A CG 3819 C CD1 . PHE A 528 ? 0.1922 0.2097 0.1876 -0.0257 0.0101 0.0116 521 PHE A CD1 3820 C CD2 . PHE A 528 ? 0.1841 0.2123 0.2359 -0.0038 -0.0102 -0.0410 521 PHE A CD2 3821 C CE1 . PHE A 528 ? 0.1734 0.2380 0.1801 -0.0289 -0.0003 -0.0150 521 PHE A CE1 3822 C CE2 . PHE A 528 ? 0.2501 0.2147 0.2297 -0.0135 0.0162 -0.0029 521 PHE A CE2 3823 C CZ . PHE A 528 ? 0.2606 0.2303 0.2366 -0.0032 0.0088 0.0121 521 PHE A CZ 3824 N N . GLU A 529 ? 0.1834 0.1772 0.1681 0.0186 -0.0117 0.0060 522 GLU A N 3825 C CA . GLU A 529 ? 0.2080 0.1745 0.1424 0.0204 0.0103 -0.0094 522 GLU A CA 3826 C C . GLU A 529 ? 0.1812 0.1709 0.1808 0.0075 -0.0135 -0.0132 522 GLU A C 3827 O O . GLU A 529 ? 0.1567 0.1679 0.2074 -0.0150 0.0199 -0.0062 522 GLU A O 3828 C CB . GLU A 529 ? 0.2171 0.1727 0.1284 0.0233 0.0155 -0.0020 522 GLU A CB 3829 C CG . GLU A 529 ? 0.2093 0.1814 0.1282 0.0364 0.0337 -0.0044 522 GLU A CG 3830 C CD . GLU A 529 ? 0.2072 0.2013 0.1571 0.0220 0.0173 -0.0322 522 GLU A CD 3831 O OE1 . GLU A 529 ? 0.2593 0.2461 0.2429 0.0120 -0.0329 -0.0069 522 GLU A OE1 3832 O OE2 . GLU A 529 ? 0.2379 0.2479 0.2210 0.0065 0.0469 -0.0204 522 GLU A OE2 3833 N N . VAL A 530 ? 0.1710 0.2028 0.1508 0.0039 0.0093 -0.0164 523 VAL A N 3834 C CA . VAL A 530 ? 0.1943 0.2046 0.1838 0.0056 0.0189 -0.0311 523 VAL A CA 3835 C C . VAL A 530 ? 0.1943 0.1886 0.1498 0.0082 0.0045 -0.0029 523 VAL A C 3836 O O . VAL A 530 ? 0.2148 0.1817 0.1638 0.0166 -0.0285 0.0096 523 VAL A O 3837 C CB . VAL A 530 ? 0.1466 0.2076 0.1630 0.0204 0.0219 0.0131 523 VAL A CB 3838 C CG1 . VAL A 530 ? 0.2047 0.1999 0.1588 -0.0127 0.0023 0.0157 523 VAL A CG1 3839 C CG2 . VAL A 530 ? 0.1226 0.2065 0.1606 0.0124 0.0177 -0.0191 523 VAL A CG2 3840 N N . PHE A 531 ? 0.1805 0.1934 0.1606 -0.0147 -0.0276 -0.0114 524 PHE A N 3841 C CA . PHE A 531 ? 0.2392 0.1742 0.1538 0.0049 -0.0090 -0.0011 524 PHE A CA 3842 C C . PHE A 531 ? 0.1946 0.1897 0.1842 0.0110 0.0055 -0.0050 524 PHE A C 3843 O O . PHE A 531 ? 0.2401 0.1716 0.1718 0.0006 -0.0019 -0.0073 524 PHE A O 3844 C CB . PHE A 531 ? 0.2084 0.1574 0.1845 0.0182 0.0265 0.0232 524 PHE A CB 3845 C CG . PHE A 531 ? 0.2094 0.1669 0.1981 -0.0055 0.0130 0.0117 524 PHE A CG 3846 C CD1 . PHE A 531 ? 0.2114 0.1744 0.2778 0.0008 0.0301 0.0152 524 PHE A CD1 3847 C CD2 . PHE A 531 ? 0.2535 0.1634 0.1852 -0.0049 -0.0081 0.0133 524 PHE A CD2 3848 C CE1 . PHE A 531 ? 0.2472 0.1660 0.2738 -0.0104 0.0382 0.0068 524 PHE A CE1 3849 C CE2 . PHE A 531 ? 0.2050 0.1903 0.2020 -0.0073 0.0284 0.0344 524 PHE A CE2 3850 C CZ . PHE A 531 ? 0.2177 0.2212 0.2220 0.0494 0.0441 -0.0019 524 PHE A CZ 3851 N N . PHE A 532 ? 0.1895 0.1917 0.1597 -0.0113 0.0001 -0.0043 525 PHE A N 3852 C CA . PHE A 532 ? 0.1864 0.1846 0.1975 0.0052 -0.0122 0.0112 525 PHE A CA 3853 C C . PHE A 532 ? 0.2018 0.1746 0.1581 0.0226 -0.0067 -0.0118 525 PHE A C 3854 O O . PHE A 532 ? 0.2263 0.1854 0.1692 0.0425 -0.0113 -0.0132 525 PHE A O 3855 C CB . PHE A 532 ? 0.1737 0.1807 0.1807 -0.0033 -0.0269 -0.0183 525 PHE A CB 3856 C CG . PHE A 532 ? 0.1496 0.1944 0.2198 -0.0108 -0.0105 -0.0131 525 PHE A CG 3857 C CD1 . PHE A 532 ? 0.1985 0.1838 0.2268 0.0115 -0.0237 -0.0033 525 PHE A CD1 3858 C CD2 . PHE A 532 ? 0.2157 0.1906 0.2022 0.0020 -0.0027 0.0113 525 PHE A CD2 3859 C CE1 . PHE A 532 ? 0.2011 0.1855 0.2165 0.0136 -0.0290 0.0033 525 PHE A CE1 3860 C CE2 . PHE A 532 ? 0.2429 0.1890 0.2310 -0.0076 -0.0128 -0.0255 525 PHE A CE2 3861 C CZ . PHE A 532 ? 0.2450 0.2139 0.2124 0.0088 0.0079 -0.0122 525 PHE A CZ 3862 N N . GLN A 533 ? 0.2016 0.1805 0.1615 0.0289 -0.0013 -0.0109 526 GLN A N 3863 C CA . GLN A 533 ? 0.1791 0.1901 0.1605 0.0191 0.0017 -0.0168 526 GLN A CA 3864 C C . GLN A 533 ? 0.1861 0.1767 0.1840 0.0131 -0.0100 -0.0103 526 GLN A C 3865 O O . GLN A 533 ? 0.2108 0.1934 0.1912 0.0027 -0.0242 0.0075 526 GLN A O 3866 C CB A GLN A 533 ? 0.1958 0.2427 0.1604 0.0360 0.0256 -0.0067 526 GLN A CB 3867 C CB B GLN A 533 ? 0.1355 0.1837 0.1616 0.0422 -0.0027 0.0038 526 GLN A CB 3868 C CG A GLN A 533 ? 0.2137 0.2245 0.2217 0.0240 -0.0096 0.0050 526 GLN A CG 3869 C CG B GLN A 533 ? 0.1393 0.1154 0.1469 0.0061 -0.0091 -0.0097 526 GLN A CG 3870 C CD A GLN A 533 ? 0.2449 0.2457 0.2584 0.0005 -0.0129 -0.0145 526 GLN A CD 3871 C CD B GLN A 533 ? 0.1068 0.1154 0.1411 0.0125 0.0063 -0.0179 526 GLN A CD 3872 O OE1 A GLN A 533 ? 0.2721 0.2530 0.3184 0.0470 -0.0214 0.0206 526 GLN A OE1 3873 O OE1 B GLN A 533 ? 0.1295 0.1098 0.1505 0.0200 -0.0071 0.0003 526 GLN A OE1 3874 N NE2 A GLN A 533 ? 0.2559 0.2963 0.2641 0.0210 -0.0162 -0.0132 526 GLN A NE2 3875 N NE2 B GLN A 533 ? 0.1204 0.1662 0.1782 -0.0069 0.0423 -0.0045 526 GLN A NE2 3876 N N . ARG A 534 ? 0.1583 0.1881 0.1526 0.0082 0.0022 -0.0299 527 ARG A N 3877 C CA . ARG A 534 ? 0.1731 0.1806 0.1382 0.0077 -0.0079 -0.0188 527 ARG A CA 3878 C C . ARG A 534 ? 0.1803 0.1703 0.1484 0.0092 0.0033 -0.0121 527 ARG A C 3879 O O . ARG A 534 ? 0.1945 0.1788 0.1509 0.0275 -0.0095 -0.0185 527 ARG A O 3880 C CB . ARG A 534 ? 0.1400 0.1759 0.1877 0.0091 -0.0241 -0.0057 527 ARG A CB 3881 C CG . ARG A 534 ? 0.1393 0.1573 0.1959 -0.0042 -0.0418 -0.0204 527 ARG A CG 3882 C CD . ARG A 534 ? 0.1958 0.1768 0.1767 -0.0361 -0.0058 -0.0477 527 ARG A CD 3883 N NE . ARG A 534 ? 0.1786 0.1793 0.1335 0.0045 -0.0200 -0.0213 527 ARG A NE 3884 C CZ . ARG A 534 ? 0.1861 0.1836 0.1298 -0.0231 0.0125 -0.0221 527 ARG A CZ 3885 N NH1 . ARG A 534 ? 0.1890 0.1855 0.1530 -0.0102 0.0149 0.0106 527 ARG A NH1 3886 N NH2 . ARG A 534 ? 0.2210 0.1584 0.1456 -0.0138 0.0220 -0.0057 527 ARG A NH2 3887 N N . LEU A 535 ? 0.1899 0.1986 0.1467 0.0123 -0.0165 -0.0057 528 LEU A N 3888 C CA . LEU A 535 ? 0.1581 0.1711 0.1442 -0.0213 -0.0085 -0.0059 528 LEU A CA 3889 C C . LEU A 535 ? 0.1971 0.1710 0.1414 0.0031 -0.0289 -0.0114 528 LEU A C 3890 O O . LEU A 535 ? 0.2331 0.2068 0.1923 0.0032 -0.0044 -0.0358 528 LEU A O 3891 C CB . LEU A 535 ? 0.1811 0.1706 0.1519 -0.0118 -0.0044 0.0048 528 LEU A CB 3892 C CG . LEU A 535 ? 0.1576 0.1927 0.1605 0.0006 -0.0217 0.0078 528 LEU A CG 3893 C CD1 . LEU A 535 ? 0.2127 0.1965 0.2128 -0.0016 0.0083 0.0178 528 LEU A CD1 3894 C CD2 . LEU A 535 ? 0.1759 0.2374 0.2305 0.0428 -0.0018 0.0185 528 LEU A CD2 3895 N N . GLY A 536 ? 0.1935 0.1595 0.1513 0.0065 -0.0148 -0.0122 529 GLY A N 3896 C CA . GLY A 536 ? 0.2002 0.1834 0.1305 0.0143 -0.0468 0.0001 529 GLY A CA 3897 C C . GLY A 536 ? 0.1907 0.1705 0.1277 0.0245 -0.0291 -0.0006 529 GLY A C 3898 O O . GLY A 536 ? 0.1848 0.1983 0.1511 0.0167 -0.0352 -0.0165 529 GLY A O 3899 N N . ILE A 537 ? 0.2048 0.1722 0.1437 0.0144 -0.0226 0.0056 530 ILE A N 3900 C CA . ILE A 537 ? 0.2047 0.1664 0.1424 0.0124 -0.0440 -0.0053 530 ILE A CA 3901 C C . ILE A 537 ? 0.2053 0.1733 0.1441 0.0295 -0.0314 -0.0211 530 ILE A C 3902 O O . ILE A 537 ? 0.1839 0.1911 0.1830 0.0380 -0.0005 -0.0052 530 ILE A O 3903 C CB . ILE A 537 ? 0.1786 0.1964 0.1563 0.0054 -0.0362 0.0196 530 ILE A CB 3904 C CG1 . ILE A 537 ? 0.1764 0.1540 0.2087 0.0090 -0.0220 -0.0146 530 ILE A CG1 3905 C CG2 . ILE A 537 ? 0.2430 0.2020 0.1555 0.0170 -0.0369 0.0208 530 ILE A CG2 3906 C CD1 . ILE A 537 ? 0.1849 0.1816 0.2362 -0.0186 -0.0045 -0.0099 530 ILE A CD1 3907 N N . ALA A 538 ? 0.1751 0.2030 0.1642 0.0123 -0.0541 -0.0093 531 ALA A N 3908 C CA . ALA A 538 ? 0.1816 0.1938 0.1623 0.0428 -0.0497 -0.0308 531 ALA A CA 3909 C C . ALA A 538 ? 0.2178 0.1950 0.1762 0.0415 -0.0192 -0.0085 531 ALA A C 3910 O O . ALA A 538 ? 0.2288 0.2172 0.1754 0.0379 -0.0027 -0.0053 531 ALA A O 3911 C CB . ALA A 538 ? 0.2038 0.2385 0.1554 0.0103 -0.0240 -0.0424 531 ALA A CB 3912 N N . SER A 539 ? 0.1965 0.1825 0.1755 0.0598 -0.0338 -0.0166 532 SER A N 3913 C CA . SER A 539 ? 0.2124 0.1955 0.1616 0.0620 -0.0353 -0.0259 532 SER A CA 3914 C C . SER A 539 ? 0.2023 0.1992 0.2200 0.0462 -0.0346 0.0013 532 SER A C 3915 O O . SER A 539 ? 0.1940 0.2081 0.2113 0.0400 -0.0261 -0.0364 532 SER A O 3916 C CB . SER A 539 ? 0.2143 0.2308 0.1481 0.0368 -0.0418 0.0008 532 SER A CB 3917 O OG . SER A 539 ? 0.2253 0.2140 0.1765 0.0315 -0.0136 0.0089 532 SER A OG 3918 N N . GLY A 540 ? 0.1773 0.1993 0.2072 0.0527 -0.0384 -0.0065 533 GLY A N 3919 C CA . GLY A 540 ? 0.1836 0.1783 0.2319 0.0673 -0.0070 -0.0106 533 GLY A CA 3920 C C . GLY A 540 ? 0.2093 0.1812 0.2281 0.0529 -0.0217 -0.0153 533 GLY A C 3921 O O . GLY A 540 ? 0.2037 0.2102 0.2401 0.0433 -0.0220 -0.0352 533 GLY A O 3922 N N . ARG A 541 ? 0.2022 0.1943 0.2361 0.0561 -0.0263 -0.0204 534 ARG A N 3923 C CA . ARG A 541 ? 0.2030 0.1984 0.2267 0.0525 -0.0259 -0.0434 534 ARG A CA 3924 C C . ARG A 541 ? 0.2110 0.2142 0.2584 0.0460 -0.0336 -0.0119 534 ARG A C 3925 O O . ARG A 541 ? 0.2249 0.2109 0.2693 0.0334 -0.0360 -0.0082 534 ARG A O 3926 C CB . ARG A 541 ? 0.2230 0.2182 0.2268 0.0137 -0.0294 -0.0259 534 ARG A CB 3927 C CG . ARG A 541 ? 0.2816 0.2508 0.2158 -0.0140 -0.0113 -0.0177 534 ARG A CG 3928 C CD . ARG A 541 ? 0.3606 0.2686 0.2255 -0.0375 -0.0271 -0.0379 534 ARG A CD 3929 N NE . ARG A 541 ? 0.4057 0.2916 0.3141 -0.0954 0.0084 -0.0734 534 ARG A NE 3930 C CZ . ARG A 541 ? 0.3862 0.2617 0.3192 -0.0076 0.0696 -0.0625 534 ARG A CZ 3931 N NH1 . ARG A 541 ? 0.3605 0.2454 0.3142 0.0157 0.0021 -0.0580 534 ARG A NH1 3932 N NH2 . ARG A 541 ? 0.3359 0.3255 0.3630 0.0146 0.0611 0.0048 534 ARG A NH2 3933 N N . ALA A 542 ? 0.2074 0.2205 0.2222 0.0622 -0.0482 -0.0037 535 ALA A N 3934 C CA . ALA A 542 ? 0.2070 0.2227 0.2437 0.0639 -0.0444 -0.0335 535 ALA A CA 3935 C C . ALA A 542 ? 0.2083 0.2168 0.2701 0.0503 -0.0204 -0.0239 535 ALA A C 3936 O O . ALA A 542 ? 0.1957 0.2184 0.3135 0.0345 -0.0277 -0.0275 535 ALA A O 3937 C CB . ALA A 542 ? 0.2560 0.2132 0.2368 0.0331 -0.0578 -0.0491 535 ALA A CB 3938 N N . ARG A 543 ? 0.2066 0.2104 0.2860 0.0676 -0.0188 -0.0316 536 ARG A N 3939 C CA . ARG A 543 ? 0.2305 0.2119 0.2573 0.0616 -0.0512 -0.0620 536 ARG A CA 3940 C C . ARG A 543 ? 0.2319 0.2155 0.3129 0.0538 -0.0418 -0.0371 536 ARG A C 3941 O O . ARG A 543 ? 0.2170 0.2315 0.3328 0.0536 -0.0668 -0.0408 536 ARG A O 3942 C CB . ARG A 543 ? 0.2564 0.2101 0.2540 0.0340 -0.0604 -0.0452 536 ARG A CB 3943 C CG . ARG A 543 ? 0.2603 0.2629 0.2522 0.0102 -0.0527 -0.0343 536 ARG A CG 3944 C CD . ARG A 543 ? 0.2404 0.3424 0.2366 0.0297 -0.0649 -0.0289 536 ARG A CD 3945 N NE . ARG A 543 ? 0.2229 0.3131 0.3246 0.0416 -0.0123 -0.0261 536 ARG A NE 3946 C CZ . ARG A 543 ? 0.2423 0.3395 0.3220 0.0394 0.0083 -0.0290 536 ARG A CZ 3947 N NH1 . ARG A 543 ? 0.2789 0.4186 0.3307 0.0309 0.0282 -0.0303 536 ARG A NH1 3948 N NH2 . ARG A 543 ? 0.2383 0.2671 0.3277 0.0243 0.0065 -0.0078 536 ARG A NH2 3949 N N . TYR A 544 ? 0.2202 0.2332 0.3110 0.0757 -0.0676 -0.0403 537 TYR A N 3950 C CA . TYR A 544 ? 0.2329 0.2455 0.2995 0.0892 -0.0196 -0.0073 537 TYR A CA 3951 C C . TYR A 544 ? 0.2535 0.2531 0.3047 0.0673 -0.0315 -0.0505 537 TYR A C 3952 O O . TYR A 544 ? 0.2151 0.2823 0.3059 0.0489 -0.0269 -0.0476 537 TYR A O 3953 C CB . TYR A 544 ? 0.2349 0.2353 0.3073 0.0842 -0.0677 -0.0157 537 TYR A CB 3954 C CG . TYR A 544 ? 0.2490 0.2507 0.3101 0.0735 -0.0465 -0.0536 537 TYR A CG 3955 C CD1 . TYR A 544 ? 0.3077 0.2356 0.2626 0.0419 -0.0691 -0.0639 537 TYR A CD1 3956 C CD2 . TYR A 544 ? 0.2362 0.2494 0.3135 0.0477 -0.0992 -0.0538 537 TYR A CD2 3957 C CE1 . TYR A 544 ? 0.2856 0.2827 0.3031 0.0459 -0.0976 -0.0503 537 TYR A CE1 3958 C CE2 . TYR A 544 ? 0.2817 0.2556 0.2960 0.0250 -0.0989 -0.0553 537 TYR A CE2 3959 C CZ . TYR A 544 ? 0.2785 0.2530 0.3194 0.0512 -0.0867 -0.0451 537 TYR A CZ 3960 O OH . TYR A 544 ? 0.3486 0.2715 0.3651 0.0426 -0.1255 -0.0487 537 TYR A OH 3961 N N . THR A 545 ? 0.2530 0.2647 0.3386 0.0722 -0.0041 -0.0361 538 THR A N 3962 C CA . THR A 545 ? 0.2497 0.2789 0.3408 0.0571 0.0173 -0.0382 538 THR A CA 3963 C C . THR A 545 ? 0.2496 0.3035 0.3702 0.0628 -0.0158 -0.0567 538 THR A C 3964 O O . THR A 545 ? 0.2102 0.3066 0.3430 0.0884 0.0134 -0.0657 538 THR A O 3965 C CB . THR A 545 ? 0.2834 0.2759 0.3253 0.0221 -0.0481 -0.0386 538 THR A CB 3966 O OG1 . THR A 545 ? 0.2562 0.3144 0.3411 0.0490 0.0041 0.0108 538 THR A OG1 3967 C CG2 . THR A 545 ? 0.2720 0.2468 0.3554 0.0113 -0.0219 -0.0281 538 THR A CG2 3968 N N . LYS A 546 ? 0.2817 0.3190 0.4041 0.0223 0.0529 -0.0755 539 LYS A N 3969 C CA . LYS A 546 ? 0.2626 0.3414 0.4282 0.0264 0.0034 -0.0940 539 LYS A CA 3970 C C . LYS A 546 ? 0.3120 0.3421 0.4153 0.0079 -0.0074 -0.0527 539 LYS A C 3971 O O . LYS A 546 ? 0.2658 0.3503 0.4201 0.0042 0.0249 -0.0357 539 LYS A O 3972 C CB . LYS A 546 ? 0.2922 0.3714 0.4184 0.0366 -0.0054 -0.0946 539 LYS A CB 3973 C CG . LYS A 546 ? 0.3290 0.4509 0.4272 0.0610 -0.0277 -0.0884 539 LYS A CG 3974 C CD . LYS A 546 ? 0.4988 0.4849 0.4944 0.0731 -0.0726 -0.1390 539 LYS A CD 3975 C CE . LYS A 546 ? 0.6157 0.6317 0.5042 -0.0018 -0.0879 -0.0011 539 LYS A CE 3976 N NZ . LYS A 546 ? 0.5450 0.6170 0.5307 -0.0619 -0.0569 -0.0219 539 LYS A NZ 3977 N N . ASN A 547 ? 0.3012 0.3637 0.4881 -0.0062 -0.0054 -0.0427 540 ASN A N 3978 C CA . ASN A 547 ? 0.3169 0.3930 0.5445 -0.0275 0.0220 -0.0659 540 ASN A CA 3979 C C . ASN A 547 ? 0.3669 0.4566 0.5982 -0.0127 0.0175 -0.0161 540 ASN A C 3980 O O . ASN A 547 ? 0.4135 0.5689 0.6180 0.0592 0.0073 -0.0483 540 ASN A O 3981 C CB . ASN A 547 ? 0.3378 0.4818 0.5441 -0.0265 -0.0222 -0.0744 540 ASN A CB 3982 C CG . ASN A 547 ? 0.3184 0.4823 0.5688 -0.0167 0.0195 -0.0595 540 ASN A CG 3983 O OD1 . ASN A 547 ? 0.4329 0.4769 0.5892 -0.0577 -0.0128 -0.0558 540 ASN A OD1 3984 N ND2 . ASN A 547 ? 0.3387 0.5518 0.5788 -0.0446 -0.0153 -0.0532 540 ASN A ND2 3985 N N A TRP A 548 ? 0.3124 0.4631 0.6393 -0.0146 0.0402 -0.0376 541 TRP A N 3986 N N B TRP A 548 ? 0.3154 0.4671 0.6450 -0.0116 0.0454 -0.0151 541 TRP A N 3987 C CA A TRP A 548 ? 0.3939 0.5603 0.6618 0.0192 0.0200 -0.0137 541 TRP A CA 3988 C CA B TRP A 548 ? 0.4229 0.5647 0.6704 0.0148 0.0090 0.0104 541 TRP A CA 3989 C C A TRP A 548 ? 0.4467 0.6721 0.6952 -0.0739 -0.0050 0.0233 541 TRP A C 3990 C C B TRP A 548 ? 0.4619 0.6312 0.6729 -0.0502 -0.0134 0.0377 541 TRP A C 3991 O O A TRP A 548 ? 0.4320 0.7564 0.6961 -0.1811 0.1037 0.0512 541 TRP A O 3992 O O B TRP A 548 ? 0.6452 0.6866 0.6920 -0.0920 0.0933 0.0342 541 TRP A O 3993 C CB A TRP A 548 ? 0.4606 0.5766 0.6993 0.0568 0.0293 -0.0303 541 TRP A CB 3994 C CB B TRP A 548 ? 0.4432 0.6086 0.7112 0.0497 0.0118 0.0785 541 TRP A CB 3995 C CG A TRP A 548 ? 0.5049 0.5288 0.7060 0.0493 0.0405 -0.0450 541 TRP A CG 3996 C CG B TRP A 548 ? 0.4726 0.6302 0.6878 -0.0084 -0.0344 0.0048 541 TRP A CG 3997 C CD1 A TRP A 548 ? 0.4964 0.5550 0.6685 -0.0193 0.0384 -0.0315 541 TRP A CD1 3998 C CD1 B TRP A 548 ? 0.3972 0.5785 0.6702 0.0197 -0.0228 -0.0707 541 TRP A CD1 3999 C CD2 A TRP A 548 ? 0.4866 0.5546 0.7176 0.0214 0.0287 -0.0527 541 TRP A CD2 4000 C CD2 B TRP A 548 ? 0.5051 0.7111 0.6463 0.0058 -0.0562 0.0225 541 TRP A CD2 4001 N NE1 A TRP A 548 ? 0.4706 0.5782 0.6366 0.0410 -0.0154 -0.0136 541 TRP A NE1 4002 N NE1 B TRP A 548 ? 0.4124 0.3141 0.6291 0.0229 0.0619 -0.0295 541 TRP A NE1 4003 C CE2 A TRP A 548 ? 0.4969 0.5441 0.6665 0.0035 0.0142 -0.0689 541 TRP A CE2 4004 C CE2 B TRP A 548 ? 0.5380 0.6920 0.6556 -0.0128 -0.0195 0.0030 541 TRP A CE2 4005 C CE3 A TRP A 548 ? 0.4716 0.6273 0.7494 0.0570 0.0167 -0.0492 541 TRP A CE3 4006 C CE3 B TRP A 548 ? 0.4685 0.6895 0.6426 0.0820 0.0084 -0.0828 541 TRP A CE3 4007 C CZ2 A TRP A 548 ? 0.4797 0.5874 0.6218 0.0240 0.0297 -0.0569 541 TRP A CZ2 4008 C CZ2 B TRP A 548 ? 0.5314 0.7152 0.6244 0.0730 -0.1196 0.0792 541 TRP A CZ2 4009 C CZ3 A TRP A 548 ? 0.5019 0.6116 0.7971 0.0220 0.0048 -0.0390 541 TRP A CZ3 4010 C CZ3 B TRP A 548 ? 0.5440 0.7074 0.6707 0.0416 -0.0196 -0.0551 541 TRP A CZ3 4011 C CH2 A TRP A 548 ? 0.5063 0.6831 0.7644 -0.0287 0.0462 0.0434 541 TRP A CH2 4012 C CH2 B TRP A 548 ? 0.4504 0.7771 0.6521 0.0652 -0.1033 0.0258 541 TRP A CH2 4013 N N . GLU A 549 ? 0.4357 0.6229 0.7324 -0.0659 -0.0150 0.0157 542 GLU A N 4014 C CA . GLU A 549 ? 0.4533 0.6393 0.7405 -0.0642 0.0246 -0.0263 542 GLU A CA 4015 C C . GLU A 549 ? 0.6115 0.6215 0.8323 0.0294 0.0353 0.0100 542 GLU A C 4016 O O . GLU A 549 ? 0.7087 0.8458 0.9152 -0.1118 0.0872 0.0343 542 GLU A O 4017 C CB . GLU A 549 ? 0.6229 0.6041 0.7304 -0.0516 -0.0108 -0.0550 542 GLU A CB 4018 C CG . GLU A 549 ? 0.5896 0.5997 0.7257 0.0031 -0.1784 -0.0850 542 GLU A CG 4019 C CD . GLU A 549 ? 0.5929 0.6301 0.7644 -0.0131 -0.0071 -0.0596 542 GLU A CD 4020 O OE1 . GLU A 549 ? 0.5689 0.7179 0.8347 -0.0460 0.0044 0.0041 542 GLU A OE1 4021 O OE2 . GLU A 549 ? 0.6716 0.5545 0.8309 0.0271 -0.0776 0.0231 542 GLU A OE2 4022 N N . THR A 550 ? 0.4871 0.5979 0.7563 -0.0240 -0.0319 -0.0138 543 THR A N 4023 C CA . THR A 550 ? 0.5336 0.6696 0.8184 -0.0035 -0.0023 -0.0723 543 THR A CA 4024 C C . THR A 550 ? 0.5006 0.7170 0.8677 -0.0438 0.0367 -0.1048 543 THR A C 4025 O O . THR A 550 ? 0.4759 0.9176 0.8845 0.0061 0.2046 -0.0629 543 THR A O 4026 C CB . THR A 550 ? 0.5132 0.7099 0.8213 -0.0325 0.0057 -0.0532 543 THR A CB 4027 O OG1 . THR A 550 ? 0.4505 0.7074 0.8485 0.1068 0.0284 0.0270 543 THR A OG1 4028 C CG2 . THR A 550 ? 0.3143 0.8998 0.8328 -0.0704 -0.0003 -0.0083 543 THR A CG2 4029 N N . ASN A 551 ? 0.4630 0.6335 0.8331 0.0621 -0.0363 -0.0445 544 ASN A N 4030 C CA . ASN A 551 ? 0.6357 0.6618 0.7793 0.0143 -0.0651 -0.0386 544 ASN A CA 4031 C C . ASN A 551 ? 0.6298 0.7663 0.7817 0.0529 -0.0828 -0.0637 544 ASN A C 4032 O O . ASN A 551 ? 0.6138 0.7215 1.0015 0.0778 -0.1252 -0.1328 544 ASN A O 4033 C CB . ASN A 551 ? 0.5936 0.5746 0.7816 0.0674 -0.0219 -0.0605 544 ASN A CB 4034 C CG . ASN A 551 ? 0.6429 0.6872 0.8008 0.1157 0.0329 -0.0278 544 ASN A CG 4035 O OD1 . ASN A 551 ? 0.6182 0.8451 1.0094 0.1710 0.0187 -0.0208 544 ASN A OD1 4036 N ND2 . ASN A 551 ? 0.3382 0.5973 0.8277 0.1013 0.0395 -0.0035 544 ASN A ND2 4037 N N . LYS A 552 ? 0.5339 0.6951 0.7951 -0.0917 -0.0523 -0.0620 545 LYS A N 4038 C CA . LYS A 552 ? 0.6154 0.7238 0.7961 -0.1173 -0.0294 0.0033 545 LYS A CA 4039 C C . LYS A 552 ? 0.5490 0.6272 0.7137 -0.0221 -0.0143 -0.0220 545 LYS A C 4040 O O . LYS A 552 ? 0.5639 0.5846 0.7035 -0.1200 -0.0317 0.0088 545 LYS A O 4041 C CB . LYS A 552 ? 0.6724 0.7956 0.8268 -0.0891 0.0423 -0.0044 545 LYS A CB 4042 C CG . LYS A 552 ? 0.8345 0.6736 0.9586 -0.0520 0.0934 -0.1116 545 LYS A CG 4043 C CD . LYS A 552 ? 0.7928 0.6729 0.9677 0.0239 0.0013 -0.0225 545 LYS A CD 4044 C CE . LYS A 552 ? 0.9291 0.6712 0.9497 0.0359 0.0360 -0.1135 545 LYS A CE 4045 N NZ . LYS A 552 ? 0.7883 0.6559 0.8628 -0.0208 0.1193 0.0356 545 LYS A NZ 4046 N N . PHE A 553 ? 0.4493 0.6508 0.6782 -0.0416 -0.0399 -0.0313 546 PHE A N 4047 C CA . PHE A 553 ? 0.4527 0.5536 0.5674 0.0143 0.0185 -0.1170 546 PHE A CA 4048 C C . PHE A 553 ? 0.4491 0.5416 0.6746 0.0256 -0.0155 -0.1126 546 PHE A C 4049 O O . PHE A 553 ? 0.4187 0.4891 0.5806 0.0017 0.0249 -0.0910 546 PHE A O 4050 C CB . PHE A 553 ? 0.5304 0.5600 0.6211 -0.0376 -0.0454 -0.0819 546 PHE A CB 4051 C CG . PHE A 553 ? 0.5614 0.6751 0.6562 0.0226 -0.0197 -0.0219 546 PHE A CG 4052 C CD1 . PHE A 553 ? 0.5830 0.4707 0.6985 0.1169 0.0041 -0.0728 546 PHE A CD1 4053 C CD2 . PHE A 553 ? 0.4879 0.4164 0.6859 -0.0204 -0.0450 -0.0931 546 PHE A CD2 4054 C CE1 . PHE A 553 ? 0.4904 0.5905 0.7333 0.0785 -0.0467 0.0129 546 PHE A CE1 4055 C CE2 . PHE A 553 ? 0.5369 0.3947 0.7384 -0.0713 -0.0552 -0.0126 546 PHE A CE2 4056 C CZ . PHE A 553 ? 0.5599 0.5358 0.6894 0.0695 -0.0327 0.0798 546 PHE A CZ 4057 N N . SER A 554 ? 0.4153 0.4650 0.6282 0.0042 0.0315 -0.0624 547 SER A N 4058 C CA . SER A 554 ? 0.3970 0.5548 0.6249 0.0097 -0.0516 0.0419 547 SER A CA 4059 C C . SER A 554 ? 0.4658 0.4749 0.5603 0.0630 0.0500 -0.0640 547 SER A C 4060 O O . SER A 554 ? 0.4796 0.4644 0.6670 -0.0208 0.0828 -0.0389 547 SER A O 4061 C CB . SER A 554 ? 0.4555 0.4433 0.5833 -0.0048 -0.0728 -0.0990 547 SER A CB 4062 O OG . SER A 554 ? 0.5251 0.6249 0.7773 0.0883 -0.0588 -0.0678 547 SER A OG 4063 N N . GLY A 555 ? 0.5783 0.4060 0.5402 0.0475 0.0504 -0.0532 548 GLY A N 4064 C CA . GLY A 555 ? 0.5098 0.3814 0.5405 0.0027 -0.0017 -0.0618 548 GLY A CA 4065 C C . GLY A 555 ? 0.3838 0.3737 0.5599 -0.0390 0.0133 -0.0438 548 GLY A C 4066 O O . GLY A 555 ? 0.4561 0.4635 0.5612 -0.0493 -0.0849 0.0389 548 GLY A O 4067 N N . TYR A 556 ? 0.3436 0.2861 0.4990 0.0481 0.0460 -0.0371 549 TYR A N 4068 C CA . TYR A 556 ? 0.3098 0.2744 0.3864 0.0098 0.0123 -0.0628 549 TYR A CA 4069 C C . TYR A 556 ? 0.2384 0.2756 0.3563 0.0434 0.0049 -0.0537 549 TYR A C 4070 O O . TYR A 556 ? 0.2257 0.2091 0.3744 0.0130 -0.0035 -0.0532 549 TYR A O 4071 C CB . TYR A 556 ? 0.2512 0.3904 0.3560 0.0063 -0.0084 -0.0454 549 TYR A CB 4072 C CG . TYR A 556 ? 0.2469 0.3004 0.3564 0.0168 0.0173 -0.0660 549 TYR A CG 4073 C CD1 . TYR A 556 ? 0.1926 0.2936 0.3173 -0.0176 0.0230 0.0014 549 TYR A CD1 4074 C CD2 . TYR A 556 ? 0.1997 0.3086 0.2708 0.0210 0.0112 -0.0530 549 TYR A CD2 4075 C CE1 . TYR A 556 ? 0.1646 0.2574 0.2683 0.0243 0.0312 -0.0272 549 TYR A CE1 4076 C CE2 . TYR A 556 ? 0.2103 0.2708 0.3055 0.0127 0.0314 -0.0467 549 TYR A CE2 4077 C CZ . TYR A 556 ? 0.2047 0.2404 0.2843 0.0266 0.0406 -0.0265 549 TYR A CZ 4078 O OH . TYR A 556 ? 0.2189 0.2420 0.2876 0.0345 0.0513 -0.0084 549 TYR A OH 4079 N N . PRO A 557 ? 0.1977 0.2378 0.3263 0.0077 0.0238 -0.0301 550 PRO A N 4080 C CA . PRO A 557 ? 0.2182 0.2245 0.3330 0.0142 0.0002 -0.0300 550 PRO A CA 4081 C C . PRO A 557 ? 0.1534 0.2414 0.2999 0.0386 0.0227 -0.0229 550 PRO A C 4082 O O . PRO A 557 ? 0.2458 0.2125 0.2884 0.0045 0.0327 -0.0319 550 PRO A O 4083 C CB . PRO A 557 ? 0.1765 0.2246 0.3624 0.0012 -0.0014 -0.0299 550 PRO A CB 4084 C CG . PRO A 557 ? 0.2142 0.2504 0.3355 0.0097 -0.0006 -0.0691 550 PRO A CG 4085 C CD . PRO A 557 ? 0.2148 0.2867 0.3630 0.0596 0.0140 -0.0532 550 PRO A CD 4086 N N . LEU A 558 ? 0.1851 0.2017 0.3060 0.0362 0.0179 -0.0092 551 LEU A N 4087 C CA . LEU A 558 ? 0.1768 0.1917 0.2912 0.0451 -0.0059 -0.0256 551 LEU A CA 4088 C C . LEU A 558 ? 0.1809 0.2071 0.2720 0.0402 0.0293 -0.0401 551 LEU A C 4089 O O . LEU A 558 ? 0.2168 0.2068 0.3075 0.0314 0.0177 -0.0347 551 LEU A O 4090 C CB . LEU A 558 ? 0.1533 0.1766 0.2787 0.0531 -0.0064 -0.0340 551 LEU A CB 4091 C CG . LEU A 558 ? 0.1777 0.1998 0.2420 0.0588 0.0350 -0.0513 551 LEU A CG 4092 C CD1 . LEU A 558 ? 0.2493 0.2684 0.2488 0.0594 0.0588 0.0032 551 LEU A CD1 4093 C CD2 . LEU A 558 ? 0.2412 0.2110 0.2788 0.0417 0.0142 -0.0910 551 LEU A CD2 4094 N N . TYR A 559 ? 0.1710 0.2013 0.2909 0.0542 0.0251 -0.0363 552 TYR A N 4095 C CA . TYR A 559 ? 0.1747 0.1796 0.2796 0.0462 0.0112 -0.0198 552 TYR A CA 4096 C C . TYR A 559 ? 0.1731 0.2092 0.2636 0.0387 0.0242 -0.0331 552 TYR A C 4097 O O . TYR A 559 ? 0.1748 0.2318 0.2713 0.0234 0.0213 -0.0321 552 TYR A O 4098 C CB . TYR A 559 ? 0.1812 0.1754 0.2752 0.0429 0.0074 -0.0126 552 TYR A CB 4099 C CG . TYR A 559 ? 0.2022 0.1823 0.2874 0.0585 0.0261 -0.0234 552 TYR A CG 4100 C CD1 . TYR A 559 ? 0.1843 0.1983 0.2831 0.0304 0.0248 -0.0509 552 TYR A CD1 4101 C CD2 . TYR A 559 ? 0.2182 0.2028 0.2666 0.0147 -0.0117 -0.0231 552 TYR A CD2 4102 C CE1 . TYR A 559 ? 0.1964 0.1905 0.2311 0.0258 -0.0144 -0.0591 552 TYR A CE1 4103 C CE2 . TYR A 559 ? 0.2208 0.1976 0.2110 0.0284 -0.0132 -0.0590 552 TYR A CE2 4104 C CZ . TYR A 559 ? 0.2277 0.1834 0.2331 0.0362 -0.0020 -0.0534 552 TYR A CZ 4105 O OH . TYR A 559 ? 0.2125 0.2212 0.2389 0.0329 0.0246 -0.0356 552 TYR A OH 4106 N N . HIS A 560 ? 0.1651 0.1896 0.2765 0.0343 0.0004 -0.0136 553 HIS A N 4107 C CA . HIS A 560 ? 0.2056 0.1668 0.2477 0.0264 -0.0048 -0.0290 553 HIS A CA 4108 C C . HIS A 560 ? 0.1921 0.1861 0.2749 0.0489 0.0180 -0.0389 553 HIS A C 4109 O O . HIS A 560 ? 0.2342 0.1988 0.2599 0.0471 0.0273 -0.0492 553 HIS A O 4110 C CB . HIS A 560 ? 0.1913 0.1728 0.2500 0.0542 0.0003 -0.0394 553 HIS A CB 4111 C CG . HIS A 560 ? 0.1712 0.1830 0.2228 0.0446 0.0007 -0.0382 553 HIS A CG 4112 N ND1 . HIS A 560 ? 0.1913 0.1669 0.2218 0.0316 0.0186 -0.0213 553 HIS A ND1 4113 C CD2 . HIS A 560 ? 0.1582 0.1960 0.2520 0.0334 0.0320 -0.0343 553 HIS A CD2 4114 C CE1 . HIS A 560 ? 0.1678 0.2214 0.1963 0.0129 -0.0026 -0.0436 553 HIS A CE1 4115 N NE2 . HIS A 560 ? 0.1942 0.1833 0.2107 0.0294 -0.0024 -0.0226 553 HIS A NE2 4116 N N . SER A 561 ? 0.2070 0.2036 0.2778 0.0671 0.0252 -0.0307 554 SER A N 4117 C CA . SER A 561 ? 0.1966 0.1277 0.2917 0.0050 0.0174 -0.0021 554 SER A CA 4118 C C . SER A 561 ? 0.2152 0.2008 0.2833 0.0079 0.0245 0.0023 554 SER A C 4119 O O . SER A 561 ? 0.2025 0.2111 0.2633 0.0373 0.0123 -0.0003 554 SER A O 4120 C CB . SER A 561 ? 0.2038 0.1533 0.2207 0.0188 0.0390 -0.0215 554 SER A CB 4121 O OG A SER A 561 ? 0.2039 0.1917 0.2672 0.0130 0.0112 -0.0311 554 SER A OG 4122 O OG B SER A 561 ? 0.2303 0.1701 0.3040 0.0364 0.0079 -0.0519 554 SER A OG 4123 N N . VAL A 562 ? 0.1877 0.1528 0.2959 0.0301 0.0060 -0.0023 555 VAL A N 4124 C CA . VAL A 562 ? 0.2081 0.1594 0.2930 0.0353 0.0064 -0.0125 555 VAL A CA 4125 C C . VAL A 562 ? 0.1940 0.2177 0.3090 0.0204 0.0019 0.0000 555 VAL A C 4126 O O . VAL A 562 ? 0.2041 0.2493 0.3144 0.0237 0.0307 -0.0062 555 VAL A O 4127 C CB . VAL A 562 ? 0.2241 0.2020 0.3048 0.0182 0.0060 -0.0450 555 VAL A CB 4128 C CG1 . VAL A 562 ? 0.2278 0.2284 0.3030 0.0413 0.0119 -0.0221 555 VAL A CG1 4129 C CG2 . VAL A 562 ? 0.2331 0.2370 0.2297 0.0064 0.0169 -0.0272 555 VAL A CG2 4130 N N . TYR A 563 ? 0.1726 0.1874 0.2983 0.0392 0.0389 -0.0262 556 TYR A N 4131 C CA . TYR A 563 ? 0.1733 0.2275 0.3100 0.0528 0.0264 -0.0457 556 TYR A CA 4132 C C . TYR A 563 ? 0.2193 0.2370 0.3206 0.0507 0.0136 -0.0458 556 TYR A C 4133 O O . TYR A 563 ? 0.2613 0.2332 0.3204 0.0573 0.0066 -0.0351 556 TYR A O 4134 C CB . TYR A 563 ? 0.1919 0.2224 0.2901 0.0614 0.0395 -0.0583 556 TYR A CB 4135 C CG . TYR A 563 ? 0.2429 0.2039 0.2889 0.0495 -0.0272 -0.0629 556 TYR A CG 4136 C CD1 . TYR A 563 ? 0.2502 0.2079 0.3109 0.0706 0.0160 -0.0743 556 TYR A CD1 4137 C CD2 . TYR A 563 ? 0.2037 0.2423 0.2813 0.0025 0.0421 -0.0678 556 TYR A CD2 4138 C CE1 . TYR A 563 ? 0.2543 0.2491 0.3004 0.0705 -0.0021 -0.0744 556 TYR A CE1 4139 C CE2 . TYR A 563 ? 0.1872 0.2349 0.3088 0.0377 -0.0303 -0.0915 556 TYR A CE2 4140 C CZ . TYR A 563 ? 0.2398 0.2397 0.3279 0.0533 0.0135 -0.0684 556 TYR A CZ 4141 O OH . TYR A 563 ? 0.2496 0.2780 0.3278 0.0458 -0.0138 -0.0783 556 TYR A OH 4142 N N . GLU A 564 ? 0.2061 0.2230 0.2921 0.0399 0.0424 -0.0450 557 GLU A N 4143 C CA . GLU A 564 ? 0.2467 0.2153 0.3032 0.0757 0.0316 -0.0386 557 GLU A CA 4144 C C . GLU A 564 ? 0.2259 0.2330 0.2827 0.0658 0.0166 -0.0385 557 GLU A C 4145 O O . GLU A 564 ? 0.2362 0.2799 0.2994 0.0753 0.0088 -0.0228 557 GLU A O 4146 C CB . GLU A 564 ? 0.3539 0.1984 0.3071 0.0799 0.0607 -0.0347 557 GLU A CB 4147 C CG . GLU A 564 ? 0.3341 0.2284 0.4851 0.0526 0.0302 -0.0505 557 GLU A CG 4148 C CD . GLU A 564 ? 0.2808 0.2206 0.3703 0.0473 0.0241 -0.0230 557 GLU A CD 4149 O OE1 . GLU A 564 ? 0.3938 0.2447 0.3379 0.0500 0.0865 -0.0236 557 GLU A OE1 4150 O OE2 . GLU A 564 ? 0.3224 0.2057 0.2413 0.0789 -0.0383 -0.0139 557 GLU A OE2 4151 N N . THR A 565 ? 0.2489 0.1989 0.2797 0.0378 0.0221 -0.0259 558 THR A N 4152 C CA . THR A 565 ? 0.2338 0.2100 0.2731 0.0376 0.0072 -0.0199 558 THR A CA 4153 C C . THR A 565 ? 0.2401 0.1883 0.2931 0.0630 0.0102 -0.0291 558 THR A C 4154 O O . THR A 565 ? 0.2122 0.2073 0.2693 0.0593 0.0105 -0.0282 558 THR A O 4155 C CB . THR A 565 ? 0.2636 0.2054 0.2826 0.0335 -0.0188 -0.0385 558 THR A CB 4156 O OG1 . THR A 565 ? 0.2706 0.2168 0.3152 0.0432 0.0217 -0.0397 558 THR A OG1 4157 C CG2 . THR A 565 ? 0.3197 0.2101 0.2767 0.0239 -0.0176 -0.0428 558 THR A CG2 4158 N N . TYR A 566 ? 0.2384 0.2215 0.2727 0.0748 0.0115 -0.0065 559 TYR A N 4159 C CA . TYR A 566 ? 0.2591 0.2377 0.2989 0.0558 0.0006 0.0042 559 TYR A CA 4160 C C . TYR A 566 ? 0.2631 0.2029 0.2953 0.0727 0.0080 -0.0213 559 TYR A C 4161 O O . TYR A 566 ? 0.2436 0.2290 0.3139 0.0356 0.0085 -0.0181 559 TYR A O 4162 C CB . TYR A 566 ? 0.2427 0.2170 0.2876 0.0623 0.0094 -0.0008 559 TYR A CB 4163 C CG . TYR A 566 ? 0.2570 0.2197 0.3128 0.0575 -0.0339 -0.0080 559 TYR A CG 4164 C CD1 . TYR A 566 ? 0.3005 0.2522 0.2815 0.0307 -0.0108 0.0060 559 TYR A CD1 4165 C CD2 . TYR A 566 ? 0.2834 0.2459 0.3237 0.0728 -0.0286 0.0091 559 TYR A CD2 4166 C CE1 . TYR A 566 ? 0.3139 0.2643 0.3156 0.0457 -0.0570 0.0161 559 TYR A CE1 4167 C CE2 . TYR A 566 ? 0.3163 0.2882 0.3217 0.0827 -0.0344 -0.0031 559 TYR A CE2 4168 C CZ . TYR A 566 ? 0.3134 0.2767 0.3491 0.0687 -0.0401 -0.0217 559 TYR A CZ 4169 O OH . TYR A 566 ? 0.3281 0.3446 0.3464 0.0512 -0.0247 -0.0013 559 TYR A OH 4170 N N . GLU A 567 ? 0.2423 0.2031 0.2911 0.1052 0.0231 0.0009 560 GLU A N 4171 C CA . GLU A 567 ? 0.2218 0.2264 0.3380 0.0746 0.0311 -0.0346 560 GLU A CA 4172 C C . GLU A 567 ? 0.2426 0.2158 0.3204 0.0847 0.0112 -0.0354 560 GLU A C 4173 O O . GLU A 567 ? 0.2652 0.2666 0.3267 0.0511 0.0025 -0.0355 560 GLU A O 4174 C CB . GLU A 567 ? 0.2578 0.2222 0.3844 0.0605 0.0094 -0.0537 560 GLU A CB 4175 C CG . GLU A 567 ? 0.2636 0.2411 0.4220 0.0667 0.0099 -0.0022 560 GLU A CG 4176 C CD . GLU A 567 ? 0.2658 0.2431 0.3508 0.0472 0.0022 -0.0216 560 GLU A CD 4177 O OE1 . GLU A 567 ? 0.2597 0.2549 0.3885 0.0481 0.0205 0.0313 560 GLU A OE1 4178 O OE2 . GLU A 567 ? 0.2968 0.2926 0.3832 0.0130 0.0135 -0.0100 560 GLU A OE2 4179 N N . LEU A 568 ? 0.2373 0.2179 0.3066 0.0770 0.0150 -0.0227 561 LEU A N 4180 C CA . LEU A 568 ? 0.2275 0.2028 0.2884 0.0701 -0.0372 -0.0277 561 LEU A CA 4181 C C . LEU A 568 ? 0.2206 0.2407 0.2888 0.0706 0.0050 -0.0566 561 LEU A C 4182 O O . LEU A 568 ? 0.2410 0.2754 0.2915 0.0657 -0.0188 -0.0172 561 LEU A O 4183 C CB . LEU A 568 ? 0.2144 0.2249 0.3078 0.0522 -0.0394 0.0091 561 LEU A CB 4184 C CG . LEU A 568 ? 0.2076 0.2389 0.2765 0.0415 -0.0135 -0.0063 561 LEU A CG 4185 C CD1 . LEU A 568 ? 0.2228 0.2626 0.3057 0.0748 -0.0197 -0.0466 561 LEU A CD1 4186 C CD2 . LEU A 568 ? 0.2896 0.2485 0.2657 0.0402 -0.0158 0.0218 561 LEU A CD2 4187 N N . VAL A 569 ? 0.2154 0.2314 0.2836 0.0636 0.0051 -0.0476 562 VAL A N 4188 C CA . VAL A 569 ? 0.2142 0.1974 0.2867 0.0758 0.0015 -0.0428 562 VAL A CA 4189 C C . VAL A 569 ? 0.2365 0.2354 0.3268 0.0716 -0.0299 -0.0267 562 VAL A C 4190 O O . VAL A 569 ? 0.2477 0.2615 0.3214 0.0717 -0.0356 -0.0370 562 VAL A O 4191 C CB . VAL A 569 ? 0.1993 0.2466 0.2825 0.0854 -0.0124 -0.0489 562 VAL A CB 4192 C CG1 . VAL A 569 ? 0.2049 0.2232 0.3146 0.0235 -0.0011 -0.0720 562 VAL A CG1 4193 C CG2 . VAL A 569 ? 0.2611 0.2469 0.3089 0.0426 -0.0254 -0.0060 562 VAL A CG2 4194 N N . GLU A 570 ? 0.2765 0.2271 0.3183 0.0876 0.0059 -0.0167 563 GLU A N 4195 C CA . GLU A 570 ? 0.2608 0.2642 0.3436 0.0966 -0.0186 -0.0163 563 GLU A CA 4196 C C . GLU A 570 ? 0.2777 0.2750 0.3599 0.1128 -0.0235 -0.0496 563 GLU A C 4197 O O . GLU A 570 ? 0.3320 0.3299 0.3408 0.1198 -0.0304 -0.0598 563 GLU A O 4198 C CB . GLU A 570 ? 0.3327 0.3038 0.3584 0.0568 -0.0193 0.0339 563 GLU A CB 4199 C CG . GLU A 570 ? 0.3892 0.3455 0.3755 0.1138 -0.0680 0.0088 563 GLU A CG 4200 C CD . GLU A 570 ? 0.4181 0.4155 0.4474 0.1543 -0.0876 0.0066 563 GLU A CD 4201 O OE1 . GLU A 570 ? 0.5714 0.3920 0.4978 0.1553 -0.0723 -0.0446 563 GLU A OE1 4202 O OE2 . GLU A 570 ? 0.5001 0.4345 0.5071 0.1754 -0.1357 0.0567 563 GLU A OE2 4203 N N . LYS A 571 ? 0.3055 0.2266 0.3459 0.0663 0.0023 -0.0382 564 LYS A N 4204 C CA . LYS A 571 ? 0.2701 0.2384 0.3459 0.0611 -0.0459 -0.0474 564 LYS A CA 4205 C C . LYS A 571 ? 0.2598 0.2777 0.3680 0.0674 -0.0264 -0.0413 564 LYS A C 4206 O O . LYS A 571 ? 0.2664 0.3223 0.4386 0.0695 -0.0713 -0.0037 564 LYS A O 4207 C CB . LYS A 571 ? 0.2934 0.2229 0.3557 0.0863 0.0083 -0.0473 564 LYS A CB 4208 C CG . LYS A 571 ? 0.2999 0.2294 0.4045 0.0665 0.0308 -0.0435 564 LYS A CG 4209 C CD . LYS A 571 ? 0.4405 0.2378 0.4136 0.0562 0.0147 -0.0477 564 LYS A CD 4210 C CE . LYS A 571 ? 0.4737 0.2565 0.4392 0.0587 0.0225 0.0166 564 LYS A CE 4211 N NZ . LYS A 571 ? 0.5577 0.2806 0.5337 0.0850 -0.0173 0.0235 564 LYS A NZ 4212 N N . PHE A 572 ? 0.2833 0.2485 0.3664 0.0719 -0.0110 -0.0497 565 PHE A N 4213 C CA . PHE A 572 ? 0.3019 0.2311 0.3684 0.0758 -0.0355 -0.0475 565 PHE A CA 4214 C C . PHE A 572 ? 0.2545 0.2590 0.4601 0.1042 -0.0089 -0.0796 565 PHE A C 4215 O O . PHE A 572 ? 0.3035 0.3606 0.5772 0.0654 -0.0024 -0.0816 565 PHE A O 4216 C CB . PHE A 572 ? 0.2105 0.2722 0.3577 0.0603 0.0226 -0.0504 565 PHE A CB 4217 C CG . PHE A 572 ? 0.2729 0.2720 0.4100 0.1016 -0.0096 -0.0436 565 PHE A CG 4218 C CD1 . PHE A 572 ? 0.2689 0.3052 0.4044 0.0967 -0.0277 -0.1035 565 PHE A CD1 4219 C CD2 . PHE A 572 ? 0.2837 0.2789 0.3526 0.1027 0.0099 -0.0513 565 PHE A CD2 4220 C CE1 . PHE A 572 ? 0.2809 0.2886 0.4369 0.0839 -0.0135 -0.1039 565 PHE A CE1 4221 C CE2 . PHE A 572 ? 0.3278 0.2821 0.4228 0.0930 -0.0366 -0.0802 565 PHE A CE2 4222 C CZ . PHE A 572 ? 0.2929 0.3477 0.4546 0.0580 -0.0359 -0.1036 565 PHE A CZ 4223 N N . TYR A 573 ? 0.2529 0.2494 0.3522 0.0928 -0.0203 -0.0582 566 TYR A N 4224 C CA . TYR A 573 ? 0.2392 0.2356 0.3308 0.0904 -0.0304 -0.0399 566 TYR A CA 4225 C C . TYR A 573 ? 0.2873 0.2667 0.3183 0.0539 -0.0292 -0.0270 566 TYR A C 4226 O O . TYR A 573 ? 0.2589 0.2964 0.3340 0.0401 -0.0006 -0.0333 566 TYR A O 4227 C CB . TYR A 573 ? 0.2265 0.2567 0.3174 0.1055 -0.0252 -0.0651 566 TYR A CB 4228 C CG . TYR A 573 ? 0.2360 0.2518 0.3649 0.0662 0.0174 -0.0394 566 TYR A CG 4229 C CD1 . TYR A 573 ? 0.2433 0.2640 0.3211 0.0533 -0.0316 -0.0290 566 TYR A CD1 4230 C CD2 . TYR A 573 ? 0.2376 0.2566 0.3588 0.0605 0.0111 -0.0430 566 TYR A CD2 4231 C CE1 . TYR A 573 ? 0.2281 0.2768 0.3270 0.0856 -0.0487 0.0057 566 TYR A CE1 4232 C CE2 . TYR A 573 ? 0.3228 0.2822 0.3373 0.0714 -0.0268 -0.0529 566 TYR A CE2 4233 C CZ . TYR A 573 ? 0.2837 0.2594 0.3142 0.0426 -0.0448 -0.0323 566 TYR A CZ 4234 O OH . TYR A 573 ? 0.3204 0.3063 0.3244 0.0485 -0.0238 -0.0291 566 TYR A OH 4235 N N . ASP A 574 ? 0.2368 0.2196 0.3215 0.0847 -0.0355 -0.0500 567 ASP A N 4236 C CA . ASP A 574 ? 0.2423 0.2548 0.3053 0.0946 -0.0443 -0.0221 567 ASP A CA 4237 C C . ASP A 574 ? 0.2635 0.2604 0.2968 0.0991 -0.0809 -0.0210 567 ASP A C 4238 O O . ASP A 574 ? 0.2859 0.2705 0.3072 0.0979 -0.0670 -0.0297 567 ASP A O 4239 C CB . ASP A 574 ? 0.2779 0.2274 0.3121 0.1048 -0.0287 -0.0330 567 ASP A CB 4240 C CG . ASP A 574 ? 0.2693 0.2635 0.3181 0.0708 -0.0317 -0.0438 567 ASP A CG 4241 O OD1 . ASP A 574 ? 0.3176 0.2934 0.2766 0.0644 -0.0371 -0.0522 567 ASP A OD1 4242 O OD2 . ASP A 574 ? 0.2584 0.2481 0.3065 0.0760 -0.0715 -0.0419 567 ASP A OD2 4243 N N . PRO A 575 ? 0.2901 0.2639 0.3420 0.1178 -0.0403 -0.0345 568 PRO A N 4244 C CA . PRO A 575 ? 0.3212 0.2715 0.3483 0.1307 -0.0409 -0.0117 568 PRO A CA 4245 C C . PRO A 575 ? 0.3223 0.2894 0.3470 0.1244 -0.0415 -0.0355 568 PRO A C 4246 O O . PRO A 575 ? 0.3709 0.3136 0.3849 0.1225 -0.0625 0.0056 568 PRO A O 4247 C CB . PRO A 575 ? 0.3186 0.3182 0.3677 0.1496 -0.0190 0.0243 568 PRO A CB 4248 C CG . PRO A 575 ? 0.3567 0.3306 0.4167 0.1332 -0.0233 0.0496 568 PRO A CG 4249 C CD . PRO A 575 ? 0.2530 0.2944 0.3999 0.1010 -0.0433 -0.0376 568 PRO A CD 4250 N N A MET A 576 ? 0.3592 0.2583 0.3464 0.1587 -0.0750 -0.0298 569 MET A N 4251 N N B MET A 576 ? 0.3422 0.2709 0.3450 0.1374 -0.0661 -0.0239 569 MET A N 4252 C CA A MET A 576 ? 0.3376 0.3090 0.3482 0.1305 -0.0584 -0.0183 569 MET A CA 4253 C CA B MET A 576 ? 0.3226 0.2974 0.3403 0.1210 -0.0690 -0.0179 569 MET A CA 4254 C C A MET A 576 ? 0.3375 0.2915 0.3153 0.1229 -0.0710 0.0003 569 MET A C 4255 C C B MET A 576 ? 0.3221 0.2864 0.3165 0.1172 -0.0738 -0.0058 569 MET A C 4256 O O A MET A 576 ? 0.3132 0.3109 0.3269 0.1300 -0.0673 -0.0098 569 MET A O 4257 O O B MET A 576 ? 0.3239 0.3236 0.3273 0.1189 -0.0637 -0.0249 569 MET A O 4258 C CB A MET A 576 ? 0.3496 0.3626 0.3520 0.1263 -0.0749 -0.0237 569 MET A CB 4259 C CB B MET A 576 ? 0.3288 0.3211 0.3383 0.1183 -0.0764 -0.0279 569 MET A CB 4260 C CG A MET A 576 ? 0.3831 0.4628 0.5033 0.1783 -0.0540 -0.1092 569 MET A CG 4261 C CG B MET A 576 ? 0.3188 0.3759 0.3591 0.1311 -0.1191 0.0049 569 MET A CG 4262 S SD A MET A 576 ? 0.5239 0.5663 0.5314 0.2291 -0.0888 0.0378 569 MET A SD 4263 S SD B MET A 576 ? 0.3263 0.4563 0.3537 0.1199 -0.1210 -0.0127 569 MET A SD 4264 C CE A MET A 576 ? 0.5217 0.5305 0.4435 0.2103 -0.1833 0.0239 569 MET A CE 4265 C CE B MET A 576 ? 0.4011 0.3290 0.4292 0.1550 -0.1109 0.0581 569 MET A CE 4266 N N . PHE A 577 ? 0.3154 0.2630 0.3207 0.1153 -0.0829 -0.0146 570 PHE A N 4267 C CA . PHE A 577 ? 0.2857 0.2485 0.2846 0.0848 -0.0515 -0.0176 570 PHE A CA 4268 C C . PHE A 577 ? 0.3040 0.2695 0.2627 0.0845 -0.0495 -0.0202 570 PHE A C 4269 O O . PHE A 577 ? 0.2855 0.2811 0.3207 0.0991 -0.0607 -0.0218 570 PHE A O 4270 C CB . PHE A 577 ? 0.2554 0.2690 0.3327 0.1019 -0.0185 -0.0460 570 PHE A CB 4271 C CG . PHE A 577 ? 0.2404 0.3020 0.2861 0.0642 -0.0361 -0.0115 570 PHE A CG 4272 C CD1 . PHE A 577 ? 0.2679 0.2825 0.2920 0.0726 -0.0396 -0.0062 570 PHE A CD1 4273 C CD2 . PHE A 577 ? 0.2939 0.2789 0.3476 0.0467 -0.0346 -0.0223 570 PHE A CD2 4274 C CE1 . PHE A 577 ? 0.3050 0.2762 0.2878 0.0302 -0.0335 0.0014 570 PHE A CE1 4275 C CE2 . PHE A 577 ? 0.3016 0.2998 0.3226 0.0888 -0.0500 -0.0148 570 PHE A CE2 4276 C CZ . PHE A 577 ? 0.2990 0.3004 0.2557 0.0474 -0.0545 -0.0145 570 PHE A CZ 4277 N N . LYS A 578 ? 0.2928 0.2731 0.2782 0.0959 -0.0650 -0.0281 571 LYS A N 4278 C CA . LYS A 578 ? 0.2972 0.2506 0.3099 0.0766 -0.0703 -0.0198 571 LYS A CA 4279 C C . LYS A 578 ? 0.2605 0.2527 0.2834 0.1037 -0.0884 -0.0387 571 LYS A C 4280 O O . LYS A 578 ? 0.2870 0.2581 0.2897 0.1186 -0.0326 -0.0316 571 LYS A O 4281 C CB . LYS A 578 ? 0.2943 0.3471 0.2895 0.1070 -0.0832 -0.0081 571 LYS A CB 4282 C CG . LYS A 578 ? 0.2807 0.3116 0.3135 0.1177 -0.0703 -0.0440 571 LYS A CG 4283 C CD . LYS A 578 ? 0.2914 0.3908 0.4489 0.0828 -0.1164 -0.0177 571 LYS A CD 4284 C CE . LYS A 578 ? 0.3388 0.3877 0.4452 0.0790 -0.1054 -0.0224 571 LYS A CE 4285 N NZ . LYS A 578 ? 0.3407 0.4272 0.5282 0.1191 -0.1277 -0.0261 571 LYS A NZ 4286 N N . TYR A 579 ? 0.2803 0.2722 0.2785 0.0828 -0.0936 -0.0179 572 TYR A N 4287 C CA . TYR A 579 ? 0.2520 0.2597 0.2719 0.1016 -0.0469 -0.0173 572 TYR A CA 4288 C C . TYR A 579 ? 0.2541 0.2465 0.2749 0.0899 -0.0462 -0.0261 572 TYR A C 4289 O O . TYR A 579 ? 0.2388 0.2412 0.3023 0.0789 -0.0519 -0.0474 572 TYR A O 4290 C CB . TYR A 579 ? 0.2636 0.2613 0.2871 0.1140 -0.0341 -0.0594 572 TYR A CB 4291 C CG . TYR A 579 ? 0.2598 0.2547 0.3410 0.0755 -0.0526 -0.0316 572 TYR A CG 4292 C CD1 . TYR A 579 ? 0.2912 0.3188 0.3947 0.0471 -0.1068 -0.0367 572 TYR A CD1 4293 C CD2 . TYR A 579 ? 0.2660 0.3110 0.3742 0.1270 -0.0362 -0.0269 572 TYR A CD2 4294 C CE1 . TYR A 579 ? 0.2784 0.3657 0.3883 0.0632 -0.0430 -0.0246 572 TYR A CE1 4295 C CE2 . TYR A 579 ? 0.2562 0.3529 0.3937 0.0858 -0.0427 -0.0316 572 TYR A CE2 4296 C CZ . TYR A 579 ? 0.3036 0.3496 0.3850 0.0878 -0.0636 -0.0101 572 TYR A CZ 4297 O OH . TYR A 579 ? 0.3073 0.4892 0.4580 0.0606 -0.1199 0.0195 572 TYR A OH 4298 N N . HIS A 580 ? 0.2757 0.2488 0.2891 0.0786 -0.0410 -0.0169 573 HIS A N 4299 C CA . HIS A 580 ? 0.2711 0.2515 0.2680 0.0725 -0.0445 -0.0326 573 HIS A CA 4300 C C . HIS A 580 ? 0.2768 0.2533 0.2560 0.0872 -0.0629 -0.0260 573 HIS A C 4301 O O . HIS A 580 ? 0.2715 0.2579 0.2230 0.0933 -0.0635 -0.0065 573 HIS A O 4302 C CB . HIS A 580 ? 0.2830 0.2536 0.2681 0.0506 -0.0693 -0.0329 573 HIS A CB 4303 C CG . HIS A 580 ? 0.3079 0.2540 0.2719 0.0830 -0.0418 -0.0329 573 HIS A CG 4304 N ND1 . HIS A 580 ? 0.3353 0.2724 0.2992 0.0960 -0.0374 -0.0577 573 HIS A ND1 4305 C CD2 . HIS A 580 ? 0.3156 0.2703 0.3065 0.0628 -0.0523 -0.0340 573 HIS A CD2 4306 C CE1 . HIS A 580 ? 0.3159 0.2535 0.3133 0.1028 -0.0694 -0.0189 573 HIS A CE1 4307 N NE2 . HIS A 580 ? 0.3132 0.3339 0.3406 0.0992 -0.0345 -0.0573 573 HIS A NE2 4308 N N . LEU A 581 ? 0.2947 0.2570 0.2352 0.0454 -0.0608 -0.0095 574 LEU A N 4309 C CA . LEU A 581 ? 0.2984 0.2562 0.2530 0.0937 -0.0501 -0.0134 574 LEU A CA 4310 C C . LEU A 581 ? 0.2913 0.2595 0.2558 0.0909 -0.0412 -0.0189 574 LEU A C 4311 O O . LEU A 581 ? 0.2606 0.2463 0.2704 0.1013 -0.0606 -0.0183 574 LEU A O 4312 C CB . LEU A 581 ? 0.3400 0.2821 0.2237 0.0903 -0.0522 -0.0071 574 LEU A CB 4313 C CG . LEU A 581 ? 0.2884 0.3224 0.2194 0.1049 -0.0630 -0.0118 574 LEU A CG 4314 C CD1 . LEU A 581 ? 0.2980 0.3119 0.2803 0.1074 -0.0426 -0.0131 574 LEU A CD1 4315 C CD2 . LEU A 581 ? 0.3154 0.3010 0.2788 0.0827 -0.0987 0.0121 574 LEU A CD2 4316 N N . THR A 582 ? 0.2927 0.2569 0.2239 0.0662 -0.0656 -0.0141 575 THR A N 4317 C CA . THR A 582 ? 0.2961 0.2498 0.2771 0.0789 -0.0535 -0.0006 575 THR A CA 4318 C C . THR A 582 ? 0.2681 0.2334 0.2495 0.0616 -0.0573 -0.0254 575 THR A C 4319 O O . THR A 582 ? 0.2550 0.2563 0.2572 0.0891 -0.0627 -0.0175 575 THR A O 4320 C CB . THR A 582 ? 0.2738 0.2518 0.2793 0.0820 -0.0652 -0.0150 575 THR A CB 4321 O OG1 . THR A 582 ? 0.3306 0.2773 0.3289 0.1209 -0.1036 -0.0216 575 THR A OG1 4322 C CG2 . THR A 582 ? 0.3211 0.2428 0.2847 0.0909 -0.0764 -0.0298 575 THR A CG2 4323 N N . VAL A 583 ? 0.2525 0.2615 0.2311 0.0844 -0.0567 -0.0108 576 VAL A N 4324 C CA . VAL A 583 ? 0.2500 0.2375 0.2338 0.0716 -0.0624 -0.0043 576 VAL A CA 4325 C C . VAL A 583 ? 0.2699 0.2269 0.2146 0.0963 -0.0523 -0.0029 576 VAL A C 4326 O O . VAL A 583 ? 0.2537 0.2426 0.2464 0.0997 -0.0241 -0.0162 576 VAL A O 4327 C CB . VAL A 583 ? 0.2077 0.2606 0.2354 0.0770 -0.0741 -0.0084 576 VAL A CB 4328 C CG1 . VAL A 583 ? 0.2173 0.2493 0.2000 0.0906 -0.0659 -0.0138 576 VAL A CG1 4329 C CG2 . VAL A 583 ? 0.2478 0.2792 0.2447 0.0523 -0.0337 -0.0413 576 VAL A CG2 4330 N N . ALA A 584 ? 0.2735 0.2365 0.1968 0.0744 -0.0753 -0.0063 577 ALA A N 4331 C CA . ALA A 584 ? 0.3203 0.2029 0.2168 0.0844 -0.0329 -0.0081 577 ALA A CA 4332 C C . ALA A 584 ? 0.2843 0.2115 0.2347 0.0842 -0.0620 -0.0221 577 ALA A C 4333 O O . ALA A 584 ? 0.2700 0.2317 0.2021 0.0869 -0.0565 -0.0042 577 ALA A O 4334 C CB . ALA A 584 ? 0.3533 0.2123 0.2378 0.0576 -0.0621 0.0228 577 ALA A CB 4335 N N . GLN A 585 ? 0.2918 0.2419 0.2277 0.0980 -0.0806 -0.0120 578 GLN A N 4336 C CA . GLN A 585 ? 0.2779 0.2371 0.2444 0.1175 -0.0533 -0.0285 578 GLN A CA 4337 C C . GLN A 585 ? 0.2886 0.2480 0.2266 0.0994 -0.0622 -0.0135 578 GLN A C 4338 O O . GLN A 585 ? 0.3193 0.2379 0.2365 0.1081 -0.0598 -0.0191 578 GLN A O 4339 C CB . GLN A 585 ? 0.3186 0.2590 0.2592 0.1325 -0.0945 0.0076 578 GLN A CB 4340 C CG . GLN A 585 ? 0.3677 0.2742 0.1631 0.1058 -0.0932 -0.0038 578 GLN A CG 4341 C CD . GLN A 585 ? 0.3562 0.2920 0.2881 0.0809 -0.1078 -0.0072 578 GLN A CD 4342 O OE1 . GLN A 585 ? 0.3633 0.2935 0.3236 0.0729 -0.0964 -0.0069 578 GLN A OE1 4343 N NE2 . GLN A 585 ? 0.3891 0.3247 0.3128 0.1005 -0.1664 0.0176 578 GLN A NE2 4344 N N . VAL A 586 ? 0.2796 0.2311 0.2107 0.0768 -0.0959 -0.0121 579 VAL A N 4345 C CA . VAL A 586 ? 0.2563 0.2293 0.2540 0.0761 -0.0706 0.0005 579 VAL A CA 4346 C C . VAL A 586 ? 0.2557 0.2199 0.2463 0.0742 -0.0713 -0.0254 579 VAL A C 4347 O O . VAL A 586 ? 0.2562 0.2245 0.2324 0.0629 -0.0380 -0.0191 579 VAL A O 4348 C CB . VAL A 586 ? 0.2226 0.2386 0.2176 0.0613 -0.1061 -0.0047 579 VAL A CB 4349 C CG1 . VAL A 586 ? 0.2639 0.2311 0.2293 0.0783 -0.0548 -0.0001 579 VAL A CG1 4350 C CG2 . VAL A 586 ? 0.2270 0.2588 0.2403 0.0906 -0.1133 -0.0033 579 VAL A CG2 4351 N N . ARG A 587 ? 0.2424 0.2381 0.2165 0.0764 -0.0583 -0.0305 580 ARG A N 4352 C CA . ARG A 587 ? 0.2365 0.2275 0.1994 0.0496 -0.0478 -0.0383 580 ARG A CA 4353 C C . ARG A 587 ? 0.2693 0.2312 0.1962 0.0944 -0.0380 -0.0076 580 ARG A C 4354 O O . ARG A 587 ? 0.2790 0.1864 0.2439 0.0789 -0.0215 -0.0105 580 ARG A O 4355 C CB . ARG A 587 ? 0.2242 0.2303 0.1763 0.0403 -0.0546 -0.0364 580 ARG A CB 4356 C CG . ARG A 587 ? 0.2742 0.1999 0.1691 0.0603 -0.0420 -0.0155 580 ARG A CG 4357 C CD . ARG A 587 ? 0.2971 0.2079 0.1853 0.0605 -0.0183 -0.0369 580 ARG A CD 4358 N NE . ARG A 587 ? 0.2272 0.2190 0.1876 0.0369 -0.0275 -0.0171 580 ARG A NE 4359 C CZ . ARG A 587 ? 0.2431 0.1749 0.2416 0.0451 0.0103 -0.0205 580 ARG A CZ 4360 N NH1 . ARG A 587 ? 0.2875 0.1962 0.3022 0.0041 0.0316 -0.0417 580 ARG A NH1 4361 N NH2 . ARG A 587 ? 0.1991 0.2375 0.2002 0.0586 -0.0277 -0.0143 580 ARG A NH2 4362 N N . GLY A 588 ? 0.2990 0.2286 0.1969 0.0705 -0.0298 0.0006 581 GLY A N 4363 C CA . GLY A 588 ? 0.3265 0.2451 0.2062 0.0752 0.0027 -0.0280 581 GLY A CA 4364 C C . GLY A 588 ? 0.3051 0.2309 0.1782 0.0882 -0.0301 0.0010 581 GLY A C 4365 O O . GLY A 588 ? 0.2971 0.2479 0.2008 0.0925 -0.0176 -0.0068 581 GLY A O 4366 N N . GLY A 589 ? 0.3158 0.2555 0.2041 0.0903 -0.0489 -0.0136 582 GLY A N 4367 C CA . GLY A 589 ? 0.3280 0.2440 0.1792 0.0990 -0.0665 -0.0112 582 GLY A CA 4368 C C . GLY A 589 ? 0.3375 0.2447 0.1914 0.0978 -0.0428 -0.0066 582 GLY A C 4369 O O . GLY A 589 ? 0.3249 0.2550 0.2025 0.1200 -0.0742 -0.0281 582 GLY A O 4370 N N . MET A 590 ? 0.3003 0.2469 0.1911 0.0710 -0.0545 -0.0244 583 MET A N 4371 C CA . MET A 590 ? 0.2854 0.2543 0.1745 0.0751 -0.0374 -0.0069 583 MET A CA 4372 C C . MET A 590 ? 0.2846 0.2221 0.1888 0.0768 -0.0309 -0.0187 583 MET A C 4373 O O . MET A 590 ? 0.2881 0.2408 0.1917 0.0974 -0.0377 -0.0160 583 MET A O 4374 C CB . MET A 590 ? 0.2811 0.2579 0.1744 0.0629 -0.0319 -0.0302 583 MET A CB 4375 C CG . MET A 590 ? 0.2692 0.2670 0.2147 0.0868 -0.0537 -0.0104 583 MET A CG 4376 S SD . MET A 590 ? 0.3075 0.2875 0.2461 0.0688 -0.0309 0.0084 583 MET A SD 4377 C CE . MET A 590 ? 0.2471 0.2841 0.3010 0.0547 -0.0228 0.0461 583 MET A CE 4378 N N . VAL A 591 ? 0.2805 0.2232 0.1705 0.0648 -0.0430 -0.0136 584 VAL A N 4379 C CA . VAL A 591 ? 0.2939 0.2401 0.2153 0.0773 -0.0226 -0.0182 584 VAL A CA 4380 C C . VAL A 591 ? 0.2911 0.2555 0.1986 0.1072 -0.0423 0.0046 584 VAL A C 4381 O O . VAL A 591 ? 0.2925 0.2329 0.2155 0.0959 -0.0278 -0.0125 584 VAL A O 4382 C CB . VAL A 591 ? 0.2873 0.2459 0.1895 0.0723 -0.0426 -0.0325 584 VAL A CB 4383 C CG1 . VAL A 591 ? 0.3076 0.2608 0.2158 0.0542 -0.0409 0.0240 584 VAL A CG1 4384 C CG2 . VAL A 591 ? 0.2942 0.2639 0.1804 0.0671 -0.0404 -0.0061 584 VAL A CG2 4385 N N . PHE A 592 ? 0.2937 0.2510 0.1712 0.0790 -0.0583 -0.0085 585 PHE A N 4386 C CA . PHE A 592 ? 0.3250 0.2409 0.1673 0.1329 -0.0561 0.0086 585 PHE A CA 4387 C C . PHE A 592 ? 0.3155 0.2589 0.2028 0.1076 -0.0555 -0.0187 585 PHE A C 4388 O O . PHE A 592 ? 0.3420 0.2552 0.1905 0.0967 -0.0372 -0.0171 585 PHE A O 4389 C CB . PHE A 592 ? 0.3240 0.2419 0.1555 0.1382 -0.0418 0.0166 585 PHE A CB 4390 C CG . PHE A 592 ? 0.3589 0.3193 0.1565 0.1296 -0.0570 -0.0037 585 PHE A CG 4391 C CD1 . PHE A 592 ? 0.3501 0.3274 0.1985 0.1591 -0.0701 0.0357 585 PHE A CD1 4392 C CD2 . PHE A 592 ? 0.3779 0.2987 0.1961 0.1299 -0.0463 -0.0043 585 PHE A CD2 4393 C CE1 . PHE A 592 ? 0.4082 0.3447 0.2075 0.1366 -0.0555 0.0149 585 PHE A CE1 4394 C CE2 . PHE A 592 ? 0.4124 0.3334 0.1901 0.1112 -0.0602 0.0226 585 PHE A CE2 4395 C CZ . PHE A 592 ? 0.4349 0.2933 0.3063 0.1472 -0.0134 0.0072 585 PHE A CZ 4396 N N . GLU A 593 ? 0.3314 0.2520 0.2118 0.1015 -0.0629 0.0049 586 GLU A N 4397 C CA . GLU A 593 ? 0.3673 0.2543 0.1943 0.1119 -0.0622 -0.0091 586 GLU A CA 4398 C C . GLU A 593 ? 0.3589 0.2578 0.1821 0.1071 -0.0534 0.0029 586 GLU A C 4399 O O . GLU A 593 ? 0.3892 0.3023 0.1850 0.1118 -0.0523 -0.0215 586 GLU A O 4400 C CB . GLU A 593 ? 0.3809 0.3044 0.2475 0.0777 -0.0579 -0.0160 586 GLU A CB 4401 C CG . GLU A 593 ? 0.4884 0.5701 0.2612 0.0601 -0.1027 -0.0392 586 GLU A CG 4402 C CD . GLU A 593 ? 0.7509 0.5353 0.2294 0.0327 -0.1569 -0.0814 586 GLU A CD 4403 O OE1 . GLU A 593 ? 0.6412 0.5520 0.3554 0.0562 -0.1254 -0.0537 586 GLU A OE1 4404 O OE2 . GLU A 593 ? 0.6586 0.5608 0.4994 0.0864 -0.2086 0.0171 586 GLU A OE2 4405 N N . LEU A 594 ? 0.3365 0.2354 0.1918 0.1148 -0.0701 -0.0033 587 LEU A N 4406 C CA . LEU A 594 ? 0.3130 0.2388 0.1582 0.1056 -0.0518 -0.0098 587 LEU A CA 4407 C C . LEU A 594 ? 0.3483 0.2568 0.1657 0.1006 -0.0357 -0.0187 587 LEU A C 4408 O O . LEU A 594 ? 0.3655 0.2467 0.1914 0.1039 -0.0373 -0.0334 587 LEU A O 4409 C CB . LEU A 594 ? 0.3109 0.2462 0.1550 0.0862 -0.0206 -0.0125 587 LEU A CB 4410 C CG . LEU A 594 ? 0.3170 0.1962 0.1655 0.0967 0.0002 -0.0166 587 LEU A CG 4411 C CD1 . LEU A 594 ? 0.2679 0.2352 0.1545 0.0859 -0.0396 -0.0337 587 LEU A CD1 4412 C CD2 . LEU A 594 ? 0.3050 0.2182 0.1682 0.1008 -0.0286 0.0038 587 LEU A CD2 4413 N N . ALA A 595 ? 0.3448 0.2585 0.1546 0.0835 -0.0303 0.0036 588 ALA A N 4414 C CA . ALA A 595 ? 0.3568 0.2676 0.1572 0.0839 -0.0423 -0.0084 588 ALA A CA 4415 C C . ALA A 595 ? 0.3546 0.2631 0.1646 0.1044 0.0031 -0.0072 588 ALA A C 4416 O O . ALA A 595 ? 0.3437 0.3243 0.1690 0.1239 0.0210 -0.0450 588 ALA A O 4417 C CB . ALA A 595 ? 0.3782 0.2561 0.2212 0.0867 -0.0414 -0.0251 588 ALA A CB 4418 N N . ASN A 596 ? 0.3806 0.3029 0.1550 0.1137 -0.0148 -0.0083 589 ASN A N 4419 C CA . ASN A 596 ? 0.3889 0.2715 0.1531 0.1486 -0.0457 -0.0084 589 ASN A CA 4420 C C . ASN A 596 ? 0.4109 0.3035 0.1827 0.1344 -0.0443 -0.0188 589 ASN A C 4421 O O . ASN A 596 ? 0.4527 0.3399 0.1912 0.1200 -0.0239 -0.0342 589 ASN A O 4422 C CB . ASN A 596 ? 0.4168 0.2713 0.1743 0.1488 -0.0160 0.0281 589 ASN A CB 4423 C CG A ASN A 596 ? 0.4156 0.3211 0.1709 0.1177 -0.0304 0.0233 589 ASN A CG 4424 C CG B ASN A 596 ? 0.3520 0.2962 0.2035 0.1452 -0.0230 -0.0027 589 ASN A CG 4425 O OD1 A ASN A 596 ? 0.4278 0.2782 0.2643 0.0917 -0.0618 -0.0054 589 ASN A OD1 4426 O OD1 B ASN A 596 ? 0.4259 0.3571 0.2670 0.0953 -0.0238 -0.0911 589 ASN A OD1 4427 N ND2 A ASN A 596 ? 0.4316 0.3483 0.2173 0.0985 -0.0751 -0.0023 589 ASN A ND2 4428 N ND2 B ASN A 596 ? 0.3882 0.2927 0.1606 0.1953 -0.0082 0.0000 589 ASN A ND2 4429 N N . SER A 597 ? 0.3470 0.2624 0.1968 0.1467 -0.0259 -0.0330 590 SER A N 4430 C CA . SER A 597 ? 0.3805 0.2946 0.1908 0.1366 -0.0491 -0.0409 590 SER A CA 4431 C C . SER A 597 ? 0.3736 0.3033 0.1458 0.1330 -0.0530 -0.0573 590 SER A C 4432 O O . SER A 597 ? 0.3780 0.2664 0.1896 0.1423 -0.0798 -0.0436 590 SER A O 4433 C CB . SER A 597 ? 0.4620 0.3099 0.2087 0.0726 -0.0206 -0.0608 590 SER A CB 4434 O OG . SER A 597 ? 0.4216 0.3201 0.3011 0.1299 -0.0660 -0.0744 590 SER A OG 4435 N N . ILE A 598 ? 0.3637 0.2497 0.1512 0.1206 -0.0201 -0.0434 591 ILE A N 4436 C CA . ILE A 598 ? 0.4042 0.2597 0.1356 0.1506 -0.0300 -0.0551 591 ILE A CA 4437 C C . ILE A 598 ? 0.3791 0.2578 0.1801 0.1414 -0.0555 -0.0450 591 ILE A C 4438 O O . ILE A 598 ? 0.4024 0.2892 0.1834 0.1614 -0.0661 -0.0259 591 ILE A O 4439 C CB . ILE A 598 ? 0.3673 0.3018 0.1261 0.1315 -0.0273 -0.0566 591 ILE A CB 4440 C CG1 . ILE A 598 ? 0.4033 0.3285 0.3025 0.0897 0.0008 0.0197 591 ILE A CG1 4441 C CG2 . ILE A 598 ? 0.3509 0.3054 0.2534 0.1319 -0.0649 -0.0528 591 ILE A CG2 4442 C CD1 . ILE A 598 ? 0.4560 0.3899 0.2664 0.0316 -0.0958 -0.0442 591 ILE A CD1 4443 N N . VAL A 599 ? 0.3723 0.3107 0.1841 0.1422 -0.0540 -0.0268 592 VAL A N 4444 C CA . VAL A 599 ? 0.3941 0.3134 0.1566 0.1224 -0.0379 -0.0344 592 VAL A CA 4445 C C . VAL A 599 ? 0.3751 0.3112 0.1682 0.1219 -0.0550 -0.0446 592 VAL A C 4446 O O . VAL A 599 ? 0.3907 0.3184 0.1666 0.1234 -0.0584 -0.0249 592 VAL A O 4447 C CB . VAL A 599 ? 0.3784 0.3160 0.1758 0.1158 -0.0027 -0.0182 592 VAL A CB 4448 C CG1 . VAL A 599 ? 0.4479 0.3003 0.2124 0.1050 -0.0451 0.0150 592 VAL A CG1 4449 C CG2 . VAL A 599 ? 0.3612 0.3598 0.1901 0.1285 -0.0330 -0.0490 592 VAL A CG2 4450 N N . LEU A 600 ? 0.4034 0.2902 0.1482 0.1109 -0.0457 -0.0481 593 LEU A N 4451 C CA . LEU A 600 ? 0.3482 0.3117 0.1591 0.1177 -0.0409 -0.0533 593 LEU A CA 4452 C C . LEU A 600 ? 0.3397 0.2667 0.1634 0.1129 -0.0537 -0.0230 593 LEU A C 4453 O O . LEU A 600 ? 0.3549 0.2724 0.1862 0.0876 -0.0270 -0.0439 593 LEU A O 4454 C CB . LEU A 600 ? 0.3683 0.3098 0.1488 0.1063 -0.0462 -0.0544 593 LEU A CB 4455 C CG . LEU A 600 ? 0.3922 0.2719 0.2095 0.0961 -0.0683 -0.0620 593 LEU A CG 4456 C CD1 . LEU A 600 ? 0.3303 0.3179 0.2118 0.1164 -0.0408 -0.0555 593 LEU A CD1 4457 C CD2 . LEU A 600 ? 0.4121 0.2644 0.1806 0.0754 -0.0268 -0.0499 593 LEU A CD2 4458 N N . PRO A 601 ? 0.3422 0.2448 0.1751 0.0973 -0.0373 -0.0262 594 PRO A N 4459 C CA . PRO A 601 ? 0.3464 0.2494 0.2447 0.1055 -0.0415 0.0082 594 PRO A CA 4460 C C . PRO A 601 ? 0.3307 0.2673 0.2133 0.1073 -0.0488 -0.0249 594 PRO A C 4461 O O . PRO A 601 ? 0.3330 0.2501 0.2322 0.1131 -0.0415 -0.0207 594 PRO A O 4462 C CB . PRO A 601 ? 0.3216 0.2419 0.2199 0.0972 -0.0818 -0.0263 594 PRO A CB 4463 C CG . PRO A 601 ? 0.2891 0.2627 0.2346 0.0750 -0.0411 -0.0402 594 PRO A CG 4464 C CD . PRO A 601 ? 0.3632 0.2299 0.2003 0.1133 -0.0135 -0.0277 594 PRO A CD 4465 N N . PHE A 602 ? 0.3225 0.2502 0.2107 0.0764 -0.0744 -0.0065 595 PHE A N 4466 C CA . PHE A 602 ? 0.2805 0.2329 0.2065 0.0782 -0.0668 -0.0151 595 PHE A CA 4467 C C . PHE A 602 ? 0.3210 0.2631 0.2187 0.0690 -0.0700 -0.0674 595 PHE A C 4468 O O . PHE A 602 ? 0.3420 0.2737 0.1979 0.0690 -0.0283 -0.0492 595 PHE A O 4469 C CB . PHE A 602 ? 0.2711 0.2460 0.2039 0.0537 -0.0804 -0.0474 595 PHE A CB 4470 C CG . PHE A 602 ? 0.2974 0.2522 0.1685 0.0541 -0.0565 -0.0634 595 PHE A CG 4471 C CD1 . PHE A 602 ? 0.2822 0.2451 0.2200 0.0565 -0.0686 -0.0489 595 PHE A CD1 4472 C CD2 . PHE A 602 ? 0.2871 0.2477 0.2007 0.0457 -0.0986 -0.0503 595 PHE A CD2 4473 C CE1 . PHE A 602 ? 0.2968 0.2723 0.1951 0.0258 -0.0958 0.0004 595 PHE A CE1 4474 C CE2 . PHE A 602 ? 0.3455 0.2147 0.1659 0.0428 -0.0385 -0.0536 595 PHE A CE2 4475 C CZ . PHE A 602 ? 0.3029 0.2391 0.1630 0.0702 -0.0167 -0.0191 595 PHE A CZ 4476 N N . ASP A 603 ? 0.2908 0.2591 0.2163 0.0705 -0.0778 -0.0356 596 ASP A N 4477 C CA . ASP A 603 ? 0.3008 0.2668 0.2133 0.0618 -0.1064 -0.0467 596 ASP A CA 4478 C C . ASP A 603 ? 0.2813 0.2330 0.2476 0.0608 -0.0620 -0.0270 596 ASP A C 4479 O O . ASP A 603 ? 0.2883 0.2559 0.2236 0.0510 -0.0681 -0.0469 596 ASP A O 4480 C CB . ASP A 603 ? 0.3018 0.2683 0.2330 0.0713 -0.0954 -0.0373 596 ASP A CB 4481 C CG . ASP A 603 ? 0.3190 0.2817 0.2683 0.0713 -0.1108 -0.0502 596 ASP A CG 4482 O OD1 . ASP A 603 ? 0.3271 0.2796 0.2943 0.0750 -0.1496 -0.0540 596 ASP A OD1 4483 O OD2 . ASP A 603 ? 0.3818 0.3815 0.3168 0.0865 -0.1727 -0.0698 596 ASP A OD2 4484 N N . CYS A 604 ? 0.2867 0.1974 0.2546 0.0442 -0.1101 -0.0484 597 CYS A N 4485 C CA . CYS A 604 ? 0.2476 0.2482 0.2539 0.0721 -0.0786 -0.0320 597 CYS A CA 4486 C C . CYS A 604 ? 0.2702 0.2239 0.2505 0.0626 -0.0730 -0.0617 597 CYS A C 4487 O O . CYS A 604 ? 0.2740 0.2699 0.2357 0.0368 -0.1035 -0.0460 597 CYS A O 4488 C CB . CYS A 604 ? 0.2587 0.2372 0.2251 0.0842 -0.0636 -0.0224 597 CYS A CB 4489 S SG . CYS A 604 ? 0.3459 0.3236 0.2903 0.0879 -0.0805 -0.0827 597 CYS A SG 4490 N N . ARG A 605 ? 0.2695 0.2568 0.2909 0.0585 -0.0872 -0.0751 598 ARG A N 4491 C CA . ARG A 605 ? 0.2968 0.2585 0.2891 0.0383 -0.0805 -0.0865 598 ARG A CA 4492 C C . ARG A 605 ? 0.2985 0.2357 0.2936 0.0597 -0.0698 -0.0520 598 ARG A C 4493 O O . ARG A 605 ? 0.2509 0.2546 0.3146 0.0456 -0.1087 -0.0252 598 ARG A O 4494 C CB . ARG A 605 ? 0.3283 0.2515 0.2576 0.0475 -0.0633 -0.1011 598 ARG A CB 4495 C CG . ARG A 605 ? 0.2855 0.2927 0.2429 0.0644 -0.0948 -0.1171 598 ARG A CG 4496 C CD . ARG A 605 ? 0.3285 0.3146 0.2472 0.0778 -0.1259 -0.0660 598 ARG A CD 4497 N NE . ARG A 605 ? 0.3695 0.3235 0.3014 0.0703 -0.0697 -0.0433 598 ARG A NE 4498 C CZ . ARG A 605 ? 0.4815 0.3364 0.3287 0.0020 -0.1347 -0.0755 598 ARG A CZ 4499 N NH1 . ARG A 605 ? 0.4239 0.4194 0.2520 -0.0038 -0.1742 -0.1052 598 ARG A NH1 4500 N NH2 . ARG A 605 ? 0.4483 0.3818 0.2904 0.0949 -0.0584 -0.0258 598 ARG A NH2 4501 N N . ASP A 606 ? 0.2699 0.2273 0.2699 0.0589 -0.1009 -0.0707 599 ASP A N 4502 C CA . ASP A 606 ? 0.2590 0.2172 0.2727 0.0619 -0.0760 -0.0354 599 ASP A CA 4503 C C . ASP A 606 ? 0.2481 0.2398 0.2769 0.0429 -0.0791 -0.0400 599 ASP A C 4504 O O . ASP A 606 ? 0.2764 0.2699 0.2819 0.0781 -0.0680 -0.0409 599 ASP A O 4505 C CB . ASP A 606 ? 0.2738 0.2275 0.2854 0.0604 -0.0836 -0.0138 599 ASP A CB 4506 C CG . ASP A 606 ? 0.2745 0.3169 0.3604 0.0304 -0.1280 0.0122 599 ASP A CG 4507 O OD1 . ASP A 606 ? 0.3096 0.4274 0.5022 0.0066 -0.1530 0.1073 599 ASP A OD1 4508 O OD2 . ASP A 606 ? 0.3459 0.2873 0.3392 0.0491 -0.0997 -0.0093 599 ASP A OD2 4509 N N . TYR A 607 ? 0.2388 0.2319 0.2772 0.0413 -0.0814 -0.0549 600 TYR A N 4510 C CA . TYR A 607 ? 0.2101 0.2154 0.2741 0.0321 -0.0645 -0.0205 600 TYR A CA 4511 C C . TYR A 607 ? 0.2045 0.2026 0.2762 0.0330 -0.0542 -0.0624 600 TYR A C 4512 O O . TYR A 607 ? 0.2300 0.2271 0.2891 0.0062 -0.0664 -0.0416 600 TYR A O 4513 C CB . TYR A 607 ? 0.2206 0.2459 0.2243 0.0183 -0.0709 -0.0596 600 TYR A CB 4514 C CG . TYR A 607 ? 0.2000 0.1974 0.2295 0.0152 -0.0570 -0.0430 600 TYR A CG 4515 C CD1 . TYR A 607 ? 0.2600 0.2077 0.1965 0.0107 -0.0782 -0.0600 600 TYR A CD1 4516 C CD2 . TYR A 607 ? 0.2571 0.1973 0.2404 0.0059 -0.0395 -0.0560 600 TYR A CD2 4517 C CE1 . TYR A 607 ? 0.2064 0.2269 0.1921 -0.0183 -0.0840 -0.0294 600 TYR A CE1 4518 C CE2 . TYR A 607 ? 0.2330 0.2426 0.1958 0.0078 -0.0456 -0.0410 600 TYR A CE2 4519 C CZ . TYR A 607 ? 0.2438 0.2091 0.2088 0.0000 -0.0420 -0.0337 600 TYR A CZ 4520 O OH . TYR A 607 ? 0.2194 0.2640 0.1871 0.0065 -0.0651 -0.0343 600 TYR A OH 4521 N N . ALA A 608 ? 0.2104 0.2119 0.3040 -0.0008 -0.0825 -0.0703 601 ALA A N 4522 C CA . ALA A 608 ? 0.2381 0.2082 0.2649 -0.0034 -0.0530 -0.0745 601 ALA A CA 4523 C C . ALA A 608 ? 0.2277 0.2305 0.3058 0.0312 -0.0728 -0.0550 601 ALA A C 4524 O O . ALA A 608 ? 0.2337 0.2418 0.3026 0.0220 -0.0656 -0.0488 601 ALA A O 4525 C CB . ALA A 608 ? 0.2305 0.1999 0.2591 0.0404 -0.1043 -0.0696 601 ALA A CB 4526 N N . VAL A 609 ? 0.2383 0.2098 0.2812 0.0263 -0.0897 -0.0752 602 VAL A N 4527 C CA . VAL A 609 ? 0.2367 0.2586 0.2989 0.0327 -0.0952 -0.0440 602 VAL A CA 4528 C C . VAL A 609 ? 0.2290 0.2218 0.3134 0.0257 -0.0854 -0.0483 602 VAL A C 4529 O O . VAL A 609 ? 0.2654 0.2740 0.3149 0.0140 -0.0773 -0.0467 602 VAL A O 4530 C CB . VAL A 609 ? 0.2031 0.3260 0.3278 0.0479 -0.1154 -0.0413 602 VAL A CB 4531 C CG1 . VAL A 609 ? 0.2978 0.3499 0.2711 0.1049 -0.0643 -0.0214 602 VAL A CG1 4532 C CG2 . VAL A 609 ? 0.2804 0.3544 0.3252 0.0565 -0.1022 -0.0576 602 VAL A CG2 4533 N N . VAL A 610 ? 0.2149 0.2073 0.3196 0.0281 -0.0877 -0.0681 603 VAL A N 4534 C CA . VAL A 610 ? 0.2326 0.2303 0.2937 0.0278 -0.0928 -0.0401 603 VAL A CA 4535 C C . VAL A 610 ? 0.1996 0.2195 0.2994 0.0172 -0.0693 -0.0363 603 VAL A C 4536 O O . VAL A 610 ? 0.1942 0.2191 0.2956 0.0083 -0.0622 -0.0323 603 VAL A O 4537 C CB . VAL A 610 ? 0.2406 0.2307 0.3428 0.0266 -0.0810 0.0212 603 VAL A CB 4538 C CG1 . VAL A 610 ? 0.2910 0.2428 0.3309 0.0391 -0.1083 0.0113 603 VAL A CG1 4539 C CG2 . VAL A 610 ? 0.2682 0.2916 0.3807 0.0046 -0.0627 0.0199 603 VAL A CG2 4540 N N . LEU A 611 ? 0.1983 0.1961 0.2769 0.0204 -0.0576 -0.0222 604 LEU A N 4541 C CA . LEU A 611 ? 0.1611 0.1871 0.3080 0.0169 -0.0645 -0.0214 604 LEU A CA 4542 C C . LEU A 611 ? 0.1905 0.2102 0.2968 -0.0010 -0.0474 -0.0447 604 LEU A C 4543 O O . LEU A 611 ? 0.1859 0.2195 0.3039 -0.0191 -0.0634 -0.0264 604 LEU A O 4544 C CB . LEU A 611 ? 0.1604 0.2071 0.2882 -0.0024 -0.0223 -0.0108 604 LEU A CB 4545 C CG . LEU A 611 ? 0.1372 0.2253 0.2530 -0.0199 -0.0612 -0.0408 604 LEU A CG 4546 C CD1 . LEU A 611 ? 0.2425 0.2641 0.2686 0.0082 -0.0296 -0.0349 604 LEU A CD1 4547 C CD2 . LEU A 611 ? 0.1795 0.2535 0.2534 -0.0341 -0.0675 -0.0195 604 LEU A CD2 4548 N N . ARG A 612 ? 0.1670 0.2159 0.3357 -0.0069 -0.0522 -0.0421 605 ARG A N 4549 C CA . ARG A 612 ? 0.2013 0.2262 0.3391 -0.0332 -0.0615 -0.0568 605 ARG A CA 4550 C C . ARG A 612 ? 0.2083 0.2052 0.3376 -0.0090 -0.0574 -0.0348 605 ARG A C 4551 O O . ARG A 612 ? 0.1903 0.2417 0.3563 -0.0032 -0.0252 -0.0232 605 ARG A O 4552 C CB . ARG A 612 ? 0.2524 0.2089 0.3549 -0.0531 -0.0891 -0.0387 605 ARG A CB 4553 C CG . ARG A 612 ? 0.2259 0.2458 0.3932 -0.0381 -0.0925 -0.0060 605 ARG A CG 4554 C CD . ARG A 612 ? 0.2929 0.2351 0.4371 -0.0113 -0.0747 -0.0124 605 ARG A CD 4555 N NE . ARG A 612 ? 0.2913 0.3260 0.4774 -0.0551 -0.0397 -0.0996 605 ARG A NE 4556 C CZ . ARG A 612 ? 0.4017 0.3405 0.6445 -0.1330 0.0082 -0.1287 605 ARG A CZ 4557 N NH1 . ARG A 612 ? 0.4476 0.3753 0.6451 -0.0630 0.0396 -0.1052 605 ARG A NH1 4558 N NH2 . ARG A 612 ? 0.3984 0.4505 0.6721 -0.1013 0.0441 0.0041 605 ARG A NH2 4559 N N . LYS A 613 ? 0.1851 0.2124 0.3322 0.0018 -0.0662 -0.0278 606 LYS A N 4560 C CA . LYS A 613 ? 0.2174 0.2023 0.3271 0.0246 -0.0617 -0.0062 606 LYS A CA 4561 C C . LYS A 613 ? 0.1740 0.2123 0.3129 -0.0076 -0.0298 -0.0012 606 LYS A C 4562 O O . LYS A 613 ? 0.1519 0.2331 0.3182 -0.0037 -0.0172 -0.0006 606 LYS A O 4563 C CB . LYS A 613 ? 0.2337 0.2161 0.3634 0.0462 -0.0317 0.0258 606 LYS A CB 4564 C CG . LYS A 613 ? 0.3370 0.2801 0.3908 0.0523 -0.0271 -0.0216 606 LYS A CG 4565 C CD . LYS A 613 ? 0.3856 0.3389 0.4659 0.0284 0.0128 0.0484 606 LYS A CD 4566 C CE . LYS A 613 ? 0.4589 0.3525 0.5554 -0.0230 -0.0487 0.0020 606 LYS A CE 4567 N NZ . LYS A 613 ? 0.4044 0.3645 0.6671 0.0160 -0.0765 0.0180 606 LYS A NZ 4568 N N . TYR A 614 ? 0.1565 0.2106 0.2807 -0.0027 -0.0675 -0.0174 607 TYR A N 4569 C CA . TYR A 614 ? 0.1432 0.1949 0.2756 -0.0217 -0.0477 -0.0114 607 TYR A CA 4570 C C . TYR A 614 ? 0.1567 0.1999 0.2896 -0.0026 -0.0283 -0.0107 607 TYR A C 4571 O O . TYR A 614 ? 0.2018 0.2018 0.2860 -0.0051 -0.0459 0.0023 607 TYR A O 4572 C CB . TYR A 614 ? 0.1539 0.1902 0.2718 -0.0174 -0.0008 -0.0060 607 TYR A CB 4573 C CG . TYR A 614 ? 0.1961 0.1795 0.2916 -0.0077 -0.0427 -0.0200 607 TYR A CG 4574 C CD1 . TYR A 614 ? 0.2171 0.1692 0.3356 0.0034 -0.0351 0.0026 607 TYR A CD1 4575 C CD2 . TYR A 614 ? 0.2032 0.1791 0.2822 -0.0098 -0.0225 -0.0171 607 TYR A CD2 4576 C CE1 . TYR A 614 ? 0.2098 0.2284 0.2985 0.0243 -0.0439 0.0391 607 TYR A CE1 4577 C CE2 . TYR A 614 ? 0.2004 0.2138 0.2845 0.0386 -0.0675 0.0149 607 TYR A CE2 4578 C CZ . TYR A 614 ? 0.2093 0.2186 0.2991 0.0404 -0.0252 0.0187 607 TYR A CZ 4579 O OH . TYR A 614 ? 0.2222 0.2257 0.3259 0.0059 -0.0580 0.0253 607 TYR A OH 4580 N N . ALA A 615 ? 0.1500 0.1682 0.2833 -0.0203 -0.0524 -0.0002 608 ALA A N 4581 C CA . ALA A 615 ? 0.1873 0.1494 0.3244 -0.0075 -0.0309 -0.0149 608 ALA A CA 4582 C C . ALA A 615 ? 0.1769 0.2232 0.3200 0.0001 -0.0345 -0.0313 608 ALA A C 4583 O O . ALA A 615 ? 0.1363 0.2399 0.3560 -0.0060 -0.0398 0.0029 608 ALA A O 4584 C CB . ALA A 615 ? 0.2504 0.1664 0.3247 0.0064 -0.0178 -0.0228 608 ALA A CB 4585 N N . ASP A 616 ? 0.1636 0.2310 0.3357 0.0088 -0.0365 -0.0343 609 ASP A N 4586 C CA . ASP A 616 ? 0.1733 0.2773 0.3592 0.0035 -0.0286 -0.0360 609 ASP A CA 4587 C C . ASP A 616 ? 0.2052 0.2334 0.3529 -0.0181 -0.0260 -0.0133 609 ASP A C 4588 O O . ASP A 616 ? 0.1661 0.2554 0.3378 -0.0015 -0.0089 -0.0129 609 ASP A O 4589 C CB . ASP A 616 ? 0.2008 0.2617 0.3997 -0.0019 -0.0606 -0.0267 609 ASP A CB 4590 C CG . ASP A 616 ? 0.2410 0.3134 0.4432 -0.0158 -0.0915 -0.0478 609 ASP A CG 4591 O OD1 . ASP A 616 ? 0.2389 0.3269 0.5346 0.0171 -0.1398 -0.0878 609 ASP A OD1 4592 O OD2 . ASP A 616 ? 0.3426 0.5145 0.4144 -0.0703 -0.1054 -0.0455 609 ASP A OD2 4593 N N . LYS A 617 ? 0.1738 0.2222 0.3437 -0.0135 -0.0334 -0.0223 610 LYS A N 4594 C CA . LYS A 617 ? 0.2152 0.2130 0.3372 -0.0103 -0.0271 -0.0104 610 LYS A CA 4595 C C . LYS A 617 ? 0.1987 0.2484 0.3442 -0.0057 -0.0202 -0.0059 610 LYS A C 4596 O O . LYS A 617 ? 0.2035 0.2458 0.3257 0.0002 -0.0383 -0.0116 610 LYS A O 4597 C CB . LYS A 617 ? 0.2493 0.2027 0.3322 -0.0045 -0.0115 0.0020 610 LYS A CB 4598 C CG . LYS A 617 ? 0.2947 0.2358 0.3725 0.0227 0.0187 -0.0070 610 LYS A CG 4599 C CD . LYS A 617 ? 0.4099 0.2509 0.4170 0.0238 0.0876 0.0029 610 LYS A CD 4600 C CE . LYS A 617 ? 0.5626 0.3015 0.5011 0.0428 0.0710 -0.0591 610 LYS A CE 4601 N NZ . LYS A 617 ? 0.6556 0.3857 0.5721 0.0095 0.0608 0.0333 610 LYS A NZ 4602 N N . ILE A 618 ? 0.1879 0.2319 0.3438 -0.0099 -0.0640 -0.0104 611 ILE A N 4603 C CA . ILE A 618 ? 0.1792 0.2220 0.3176 -0.0217 -0.0338 0.0256 611 ILE A CA 4604 C C . ILE A 618 ? 0.1927 0.1995 0.3239 -0.0301 -0.0116 -0.0084 611 ILE A C 4605 O O . ILE A 618 ? 0.2091 0.2040 0.3215 -0.0245 -0.0158 -0.0149 611 ILE A O 4606 C CB . ILE A 618 ? 0.1736 0.2507 0.2983 -0.0016 -0.0218 -0.0206 611 ILE A CB 4607 C CG1 . ILE A 618 ? 0.2301 0.2260 0.2814 -0.0106 -0.0092 -0.0347 611 ILE A CG1 4608 C CG2 . ILE A 618 ? 0.1912 0.2124 0.3274 -0.0086 -0.0276 -0.0087 611 ILE A CG2 4609 C CD1 . ILE A 618 ? 0.2086 0.2436 0.2729 0.0064 -0.0052 -0.0549 611 ILE A CD1 4610 N N . TYR A 619 ? 0.1941 0.1835 0.3439 -0.0349 -0.0126 -0.0048 612 TYR A N 4611 C CA . TYR A 619 ? 0.2133 0.2026 0.3733 -0.0586 -0.0090 -0.0110 612 TYR A CA 4612 C C . TYR A 619 ? 0.2250 0.2339 0.3706 -0.0299 -0.0100 0.0163 612 TYR A C 4613 O O . TYR A 619 ? 0.2148 0.2220 0.3799 -0.0288 -0.0046 0.0167 612 TYR A O 4614 C CB . TYR A 619 ? 0.2047 0.1837 0.3883 -0.0664 -0.0189 -0.0100 612 TYR A CB 4615 C CG . TYR A 619 ? 0.2603 0.2276 0.4726 -0.0945 0.0158 0.0107 612 TYR A CG 4616 C CD1 . TYR A 619 ? 0.3267 0.2756 0.4028 -0.0800 0.0487 0.0357 612 TYR A CD1 4617 C CD2 . TYR A 619 ? 0.2744 0.3325 0.5067 -0.1167 -0.0145 -0.0159 612 TYR A CD2 4618 C CE1 . TYR A 619 ? 0.4058 0.2662 0.5122 -0.1255 0.0073 0.0417 612 TYR A CE1 4619 C CE2 . TYR A 619 ? 0.3307 0.3222 0.5879 -0.1236 0.0268 -0.0287 612 TYR A CE2 4620 C CZ . TYR A 619 ? 0.4316 0.3787 0.6384 -0.1220 -0.0176 0.0480 612 TYR A CZ 4621 O OH . TYR A 619 ? 0.5833 0.5780 0.7142 -0.2564 0.1240 0.0120 612 TYR A OH 4622 N N . SER A 620 ? 0.1802 0.2051 0.3786 -0.0144 0.0080 -0.0207 613 SER A N 4623 C CA . SER A 620 ? 0.1966 0.2673 0.3900 -0.0185 0.0023 -0.0261 613 SER A CA 4624 C C . SER A 620 ? 0.2250 0.2368 0.3821 -0.0347 0.0295 -0.0090 613 SER A C 4625 O O . SER A 620 ? 0.2037 0.3299 0.3874 -0.0481 0.0135 0.0199 613 SER A O 4626 C CB . SER A 620 ? 0.2281 0.2673 0.3750 -0.0205 -0.0014 -0.0027 613 SER A CB 4627 O OG A SER A 620 ? 0.2015 0.3069 0.3736 0.0005 -0.0306 -0.0220 613 SER A OG 4628 O OG B SER A 620 ? 0.2848 0.2703 0.4244 0.0021 0.0120 -0.0170 613 SER A OG 4629 N N . ILE A 621 ? 0.1864 0.2169 0.3817 -0.0122 0.0223 -0.0121 614 ILE A N 4630 C CA . ILE A 621 ? 0.2148 0.2170 0.3816 -0.0344 0.0084 0.0089 614 ILE A CA 4631 C C . ILE A 621 ? 0.2439 0.2192 0.3782 -0.0032 0.0490 0.0052 614 ILE A C 4632 O O . ILE A 621 ? 0.2332 0.2324 0.3927 -0.0066 0.0428 0.0023 614 ILE A O 4633 C CB . ILE A 621 ? 0.2394 0.1942 0.3626 -0.0409 0.0029 0.0002 614 ILE A CB 4634 C CG1 . ILE A 621 ? 0.2501 0.1984 0.3757 -0.0419 0.0156 0.0176 614 ILE A CG1 4635 C CG2 . ILE A 621 ? 0.2144 0.2667 0.3595 -0.0221 0.0043 0.0091 614 ILE A CG2 4636 C CD1 . ILE A 621 ? 0.2629 0.1838 0.3708 -0.0386 0.0596 -0.0161 614 ILE A CD1 4637 N N . SER A 622 ? 0.1773 0.2032 0.3686 -0.0110 0.0128 0.0052 615 SER A N 4638 C CA . SER A 622 ? 0.2346 0.1883 0.3810 -0.0134 0.0311 0.0188 615 SER A CA 4639 C C . SER A 622 ? 0.2294 0.2349 0.3951 -0.0105 0.0626 0.0170 615 SER A C 4640 O O . SER A 622 ? 0.2755 0.2403 0.4006 -0.0161 0.0876 0.0390 615 SER A O 4641 C CB . SER A 622 ? 0.2181 0.1895 0.3687 -0.0074 0.0268 0.0248 615 SER A CB 4642 O OG . SER A 622 ? 0.2306 0.2432 0.3508 0.0031 0.0198 0.0252 615 SER A OG 4643 N N A MET A 623 ? 0.2127 0.2066 0.4295 -0.0320 0.0457 0.0252 616 MET A N 4644 N N B MET A 623 ? 0.2311 0.2260 0.4204 -0.0322 0.0496 0.0239 616 MET A N 4645 C CA A MET A 623 ? 0.2281 0.2597 0.4532 -0.0544 0.0453 0.0616 616 MET A CA 4646 C CA B MET A 623 ? 0.2415 0.2694 0.4455 -0.0521 0.0533 0.0405 616 MET A CA 4647 C C A MET A 623 ? 0.2381 0.3134 0.4324 -0.0744 0.0424 0.0533 616 MET A C 4648 C C B MET A 623 ? 0.2567 0.3098 0.4295 -0.0549 0.0563 0.0459 616 MET A C 4649 O O A MET A 623 ? 0.2277 0.4179 0.4293 -0.0790 0.0595 0.0990 616 MET A O 4650 O O B MET A 623 ? 0.2423 0.4120 0.4295 -0.0672 0.0579 0.0821 616 MET A O 4651 C CB A MET A 623 ? 0.2532 0.2657 0.4713 -0.0516 0.0464 0.0443 616 MET A CB 4652 C CB B MET A 623 ? 0.2717 0.2882 0.4481 -0.0368 0.0624 0.0079 616 MET A CB 4653 C CG A MET A 623 ? 0.3413 0.2685 0.5423 -0.0398 0.0401 0.0216 616 MET A CG 4654 C CG B MET A 623 ? 0.2821 0.2740 0.4604 -0.0734 0.0443 0.0258 616 MET A CG 4655 S SD A MET A 623 ? 0.4191 0.3477 0.6333 -0.0024 -0.0355 0.1071 616 MET A SD 4656 S SD B MET A 623 ? 0.3380 0.5141 0.5125 -0.0847 -0.0057 -0.0173 616 MET A SD 4657 C CE A MET A 623 ? 0.3876 0.2912 0.5685 -0.0322 -0.0924 0.1666 616 MET A CE 4658 C CE B MET A 623 ? 0.2635 0.4417 0.4973 -0.0068 -0.0348 -0.0051 616 MET A CE 4659 N N . LYS A 624 ? 0.2660 0.2890 0.4337 0.0040 0.0455 0.0439 617 LYS A N 4660 C CA . LYS A 624 ? 0.3140 0.3554 0.4139 -0.0332 0.0505 0.0527 617 LYS A CA 4661 C C . LYS A 624 ? 0.2758 0.3363 0.4239 -0.0116 0.0926 0.0623 617 LYS A C 4662 O O . LYS A 624 ? 0.2881 0.2945 0.4344 0.0006 0.1176 0.0409 617 LYS A O 4663 C CB . LYS A 624 ? 0.4764 0.3534 0.4196 0.0146 0.0948 0.0516 617 LYS A CB 4664 C CG . LYS A 624 ? 0.3276 0.4637 0.4746 0.0066 0.0866 0.0800 617 LYS A CG 4665 C CD . LYS A 624 ? 0.3252 0.4176 0.5471 -0.0174 0.0595 0.0193 617 LYS A CD 4666 C CE . LYS A 624 ? 0.3399 0.4722 0.5926 0.0106 0.0429 0.0374 617 LYS A CE 4667 N NZ . LYS A 624 ? 0.2635 0.6026 0.6094 -0.0335 0.0450 0.0573 617 LYS A NZ 4668 N N . HIS A 625 ? 0.2976 0.2568 0.3801 -0.0197 0.0811 0.0194 618 HIS A N 4669 C CA . HIS A 625 ? 0.2668 0.2376 0.4266 -0.0319 0.0777 0.0407 618 HIS A CA 4670 C C . HIS A 625 ? 0.2687 0.2480 0.4169 -0.0324 0.0891 0.0430 618 HIS A C 4671 O O . HIS A 625 ? 0.2493 0.2689 0.3905 -0.0397 0.1171 0.0049 618 HIS A O 4672 C CB . HIS A 625 ? 0.2853 0.2531 0.4197 -0.0250 0.0140 0.0542 618 HIS A CB 4673 C CG . HIS A 625 ? 0.2985 0.2664 0.4643 -0.0141 0.0465 0.0064 618 HIS A CG 4674 N ND1 . HIS A 625 ? 0.3706 0.3050 0.4036 0.0000 0.0184 0.0356 618 HIS A ND1 4675 C CD2 . HIS A 625 ? 0.3417 0.2677 0.4787 0.0099 -0.0077 0.0218 618 HIS A CD2 4676 C CE1 . HIS A 625 ? 0.3358 0.2927 0.5009 -0.0092 0.0198 -0.0031 618 HIS A CE1 4677 N NE2 . HIS A 625 ? 0.3326 0.3179 0.5019 0.0080 0.0409 -0.0221 618 HIS A NE2 4678 N N . PRO A 626 ? 0.2879 0.2616 0.4093 -0.0455 0.1091 0.0503 619 PRO A N 4679 C CA . PRO A 626 ? 0.2757 0.2370 0.4715 -0.0774 0.0850 0.0528 619 PRO A CA 4680 C C . PRO A 626 ? 0.2784 0.2526 0.4536 -0.0723 0.0981 0.0604 619 PRO A C 4681 O O . PRO A 626 ? 0.3248 0.2454 0.4571 -0.0410 0.0741 0.0499 619 PRO A O 4682 C CB . PRO A 626 ? 0.2647 0.3574 0.4761 -0.0402 0.0518 -0.0093 619 PRO A CB 4683 C CG . PRO A 626 ? 0.3174 0.2748 0.5248 -0.0568 0.0965 0.0024 619 PRO A CG 4684 C CD . PRO A 626 ? 0.2507 0.3056 0.4979 -0.0698 0.0918 0.0478 619 PRO A CD 4685 N N A GLN A 627 ? 0.2783 0.2444 0.4452 -0.0444 0.0811 0.0473 620 GLN A N 4686 N N B GLN A 627 ? 0.2807 0.2531 0.4498 -0.0536 0.0857 0.0492 620 GLN A N 4687 C CA A GLN A 627 ? 0.3321 0.2448 0.4142 -0.0625 0.1044 0.0726 620 GLN A CA 4688 C CA B GLN A 627 ? 0.3136 0.2638 0.4252 -0.0677 0.1020 0.0649 620 GLN A CA 4689 C C A GLN A 627 ? 0.3291 0.2357 0.3613 -0.0510 0.0818 0.0589 620 GLN A C 4690 C C B GLN A 627 ? 0.3132 0.2440 0.3767 -0.0584 0.0856 0.0621 620 GLN A C 4691 O O A GLN A 627 ? 0.3627 0.2507 0.3508 -0.0310 0.0585 0.0512 620 GLN A O 4692 O O B GLN A 627 ? 0.3412 0.2470 0.3382 -0.0458 0.0758 0.0459 620 GLN A O 4693 C CB A GLN A 627 ? 0.4028 0.2661 0.4363 -0.0184 0.1370 0.0896 620 GLN A CB 4694 C CB B GLN A 627 ? 0.3018 0.3019 0.4355 -0.0548 0.1196 0.0684 620 GLN A CB 4695 C CG A GLN A 627 ? 0.4814 0.3273 0.4412 0.0259 0.1067 0.0801 620 GLN A CG 4696 C CG B GLN A 627 ? 0.3197 0.2701 0.4743 -0.1005 0.1210 0.0685 620 GLN A CG 4697 C CD A GLN A 627 ? 0.4361 0.3110 0.6729 -0.0263 0.1488 0.0928 620 GLN A CD 4698 C CD B GLN A 627 ? 0.3400 0.3745 0.4971 -0.0968 0.1354 0.0473 620 GLN A CD 4699 O OE1 A GLN A 627 ? 0.4776 0.2749 0.5235 0.0344 0.1087 0.1054 620 GLN A OE1 4700 O OE1 B GLN A 627 ? 0.4404 0.4071 0.5078 -0.0692 0.0817 0.0092 620 GLN A OE1 4701 N NE2 A GLN A 627 ? 0.3985 0.5755 0.6659 -0.0170 0.2196 0.2914 620 GLN A NE2 4702 N NE2 B GLN A 627 ? 0.3705 0.3547 0.4125 -0.0771 0.1782 0.0874 620 GLN A NE2 4703 N N . GLU A 628 ? 0.3221 0.2325 0.3438 -0.0571 0.0647 0.0418 621 GLU A N 4704 C CA . GLU A 628 ? 0.3091 0.1985 0.3620 -0.0396 0.0779 0.0544 621 GLU A CA 4705 C C . GLU A 628 ? 0.3048 0.2134 0.3483 -0.0507 0.0614 0.0663 621 GLU A C 4706 O O . GLU A 628 ? 0.3308 0.2032 0.3020 -0.0183 -0.0128 0.0559 621 GLU A O 4707 C CB . GLU A 628 ? 0.3463 0.2066 0.3788 -0.0349 0.0327 0.0404 621 GLU A CB 4708 C CG . GLU A 628 ? 0.4206 0.3105 0.4042 -0.0536 0.0826 0.0174 621 GLU A CG 4709 C CD . GLU A 628 ? 0.4327 0.3740 0.4204 -0.1271 0.1164 0.1254 621 GLU A CD 4710 O OE1 . GLU A 628 ? 0.4836 0.3209 0.4315 -0.0035 0.1068 0.0332 621 GLU A OE1 4711 O OE2 . GLU A 628 ? 0.5907 0.6472 0.4114 -0.0967 0.1968 0.0231 621 GLU A OE2 4712 N N . MET A 629 ? 0.3162 0.1699 0.3457 -0.0322 0.0474 0.0281 622 MET A N 4713 C CA . MET A 629 ? 0.2796 0.1898 0.3316 0.0022 0.0635 0.0673 622 MET A CA 4714 C C . MET A 629 ? 0.2840 0.1836 0.3670 -0.0363 0.0748 0.0629 622 MET A C 4715 O O . MET A 629 ? 0.2318 0.1917 0.3745 -0.0363 0.0164 0.0323 622 MET A O 4716 C CB . MET A 629 ? 0.2663 0.2034 0.3363 -0.0199 0.0538 0.0628 622 MET A CB 4717 C CG . MET A 629 ? 0.2544 0.1816 0.3266 -0.0083 0.0443 0.0266 622 MET A CG 4718 S SD . MET A 629 ? 0.2430 0.2482 0.3719 -0.0007 0.0388 0.0470 622 MET A SD 4719 C CE . MET A 629 ? 0.2450 0.2366 0.3178 -0.0110 -0.0059 0.0226 622 MET A CE 4720 N N . LYS A 630 ? 0.2600 0.1853 0.3200 -0.0425 0.0567 0.0426 623 LYS A N 4721 C CA . LYS A 630 ? 0.2754 0.1989 0.3602 -0.0519 0.0679 0.0653 623 LYS A CA 4722 C C . LYS A 630 ? 0.3084 0.2543 0.3867 -0.0161 0.0412 0.0565 623 LYS A C 4723 O O . LYS A 630 ? 0.3168 0.2057 0.3706 -0.0457 0.0279 0.0465 623 LYS A O 4724 C CB . LYS A 630 ? 0.2778 0.2512 0.4133 -0.0604 0.0951 0.0428 623 LYS A CB 4725 C CG . LYS A 630 ? 0.2756 0.2328 0.3889 -0.0796 0.0881 0.0282 623 LYS A CG 4726 C CD . LYS A 630 ? 0.2903 0.3037 0.4661 -0.0980 0.1255 -0.0115 623 LYS A CD 4727 C CE . LYS A 630 ? 0.3147 0.4088 0.5888 -0.0618 0.0547 -0.0894 623 LYS A CE 4728 N NZ . LYS A 630 ? 0.5161 0.5608 0.6001 0.0104 0.1717 -0.1602 623 LYS A NZ 4729 N N . THR A 631 ? 0.2838 0.2266 0.3877 -0.0235 0.0399 0.0582 624 THR A N 4730 C CA . THR A 631 ? 0.3408 0.2869 0.3488 -0.0489 0.0239 0.0638 624 THR A CA 4731 C C . THR A 631 ? 0.3455 0.2245 0.3616 -0.0227 0.0256 0.0702 624 THR A C 4732 O O . THR A 631 ? 0.3656 0.2428 0.3715 -0.0070 0.0061 0.0855 624 THR A O 4733 C CB . THR A 631 ? 0.3536 0.3662 0.3781 -0.0234 0.0320 0.0503 624 THR A CB 4734 O OG1 . THR A 631 ? 0.4069 0.4525 0.3950 -0.0274 0.0947 0.1018 624 THR A OG1 4735 C CG2 . THR A 631 ? 0.4072 0.4179 0.3869 -0.0144 -0.0098 0.0333 624 THR A CG2 4736 N N . TYR A 632 ? 0.3100 0.2174 0.3170 -0.0341 0.0193 0.0563 625 TYR A N 4737 C CA . TYR A 632 ? 0.3224 0.2096 0.3552 -0.0648 0.0188 0.0418 625 TYR A CA 4738 C C . TYR A 632 ? 0.2967 0.2317 0.3537 -0.0508 0.0248 0.0496 625 TYR A C 4739 O O . TYR A 632 ? 0.2729 0.2258 0.3175 -0.0258 0.0041 0.0565 625 TYR A O 4740 C CB . TYR A 632 ? 0.2652 0.1941 0.3513 -0.0336 -0.0094 0.0281 625 TYR A CB 4741 C CG . TYR A 632 ? 0.3748 0.2392 0.3498 -0.0295 0.0152 0.0423 625 TYR A CG 4742 C CD1 . TYR A 632 ? 0.4125 0.2665 0.3608 0.0121 0.0232 0.0493 625 TYR A CD1 4743 C CD2 . TYR A 632 ? 0.3644 0.2461 0.3695 -0.0450 0.0318 0.0376 625 TYR A CD2 4744 C CE1 . TYR A 632 ? 0.4325 0.3186 0.3608 0.0339 0.0120 0.0477 625 TYR A CE1 4745 C CE2 . TYR A 632 ? 0.4241 0.2641 0.3783 -0.0464 0.0179 0.0131 625 TYR A CE2 4746 C CZ . TYR A 632 ? 0.4741 0.3430 0.3584 0.0419 0.0399 0.0222 625 TYR A CZ 4747 O OH . TYR A 632 ? 0.5069 0.4021 0.3689 0.0000 0.0098 0.0022 625 TYR A OH 4748 N N . SER A 633 ? 0.3321 0.1861 0.3425 -0.0295 -0.0060 0.0463 626 SER A N 4749 C CA . SER A 633 ? 0.2765 0.1929 0.3450 -0.0091 0.0158 0.0409 626 SER A CA 4750 C C . SER A 633 ? 0.2516 0.1979 0.3259 -0.0251 0.0206 0.0234 626 SER A C 4751 O O . SER A 633 ? 0.1965 0.2162 0.3526 -0.0229 0.0113 0.0121 626 SER A O 4752 C CB A SER A 633 ? 0.3223 0.1485 0.3380 -0.0076 0.0186 0.0589 626 SER A CB 4753 C CB B SER A 633 ? 0.3014 0.1852 0.3719 -0.0042 0.0234 0.0376 626 SER A CB 4754 O OG A SER A 633 ? 0.2195 0.1653 0.3426 0.0110 0.0197 0.0772 626 SER A OG 4755 O OG B SER A 633 ? 0.2286 0.2974 0.3656 -0.0458 0.0647 0.0061 626 SER A OG 4756 N N . VAL A 634 ? 0.2589 0.1581 0.3271 -0.0311 0.0192 0.0235 627 VAL A N 4757 C CA . VAL A 634 ? 0.2696 0.1673 0.3246 -0.0394 0.0116 0.0302 627 VAL A CA 4758 C C . VAL A 634 ? 0.2639 0.2464 0.3432 -0.0263 -0.0040 0.0201 627 VAL A C 4759 O O . VAL A 634 ? 0.2454 0.2985 0.3149 0.0098 -0.0138 0.0001 627 VAL A O 4760 C CB . VAL A 634 ? 0.3170 0.1679 0.3077 -0.0181 0.0111 0.0344 627 VAL A CB 4761 C CG1 . VAL A 634 ? 0.2536 0.2084 0.3156 -0.0807 0.0109 0.0477 627 VAL A CG1 4762 C CG2 . VAL A 634 ? 0.2707 0.2316 0.3246 -0.0506 -0.0051 0.0255 627 VAL A CG2 4763 N N . SER A 635 ? 0.2632 0.2409 0.3354 -0.0329 -0.0078 0.0351 628 SER A N 4764 C CA . SER A 635 ? 0.3082 0.2392 0.3351 -0.0420 0.0236 0.0081 628 SER A CA 4765 C C . SER A 635 ? 0.2596 0.2084 0.3401 -0.0547 -0.0143 0.0007 628 SER A C 4766 O O . SER A 635 ? 0.2308 0.2503 0.3014 -0.0549 -0.0080 0.0046 628 SER A O 4767 C CB . SER A 635 ? 0.4092 0.2372 0.3653 -0.0517 -0.0186 -0.0053 628 SER A CB 4768 O OG . SER A 635 ? 0.4721 0.2773 0.3553 -0.1169 0.0137 -0.0219 628 SER A OG 4769 N N . PHE A 636 ? 0.2512 0.2051 0.3497 -0.0380 -0.0134 -0.0226 629 PHE A N 4770 C CA . PHE A 636 ? 0.2581 0.1930 0.3310 -0.0163 0.0038 -0.0219 629 PHE A CA 4771 C C . PHE A 636 ? 0.2069 0.2008 0.3282 -0.0280 -0.0036 -0.0242 629 PHE A C 4772 O O . PHE A 636 ? 0.1800 0.2188 0.3356 -0.0214 0.0036 -0.0096 629 PHE A O 4773 C CB . PHE A 636 ? 0.2001 0.2119 0.3695 -0.0388 -0.0049 -0.0281 629 PHE A CB 4774 C CG . PHE A 636 ? 0.2256 0.2083 0.3331 -0.0308 -0.0321 -0.0054 629 PHE A CG 4775 C CD1 . PHE A 636 ? 0.1987 0.2028 0.3287 -0.0282 -0.0261 -0.0086 629 PHE A CD1 4776 C CD2 . PHE A 636 ? 0.2136 0.2236 0.3439 -0.0452 -0.0153 -0.0203 629 PHE A CD2 4777 C CE1 . PHE A 636 ? 0.2278 0.2159 0.3187 0.0140 0.0066 -0.0071 629 PHE A CE1 4778 C CE2 . PHE A 636 ? 0.2167 0.1971 0.3569 -0.0103 -0.0115 -0.0309 629 PHE A CE2 4779 C CZ . PHE A 636 ? 0.1978 0.2081 0.3069 0.0003 -0.0234 0.0012 629 PHE A CZ 4780 N N . ASP A 637 ? 0.1813 0.2028 0.3496 -0.0147 -0.0011 -0.0177 630 ASP A N 4781 C CA . ASP A 637 ? 0.2012 0.2255 0.3388 -0.0355 -0.0129 -0.0097 630 ASP A CA 4782 C C . ASP A 637 ? 0.1825 0.2196 0.3564 -0.0290 -0.0168 -0.0158 630 ASP A C 4783 O O . ASP A 637 ? 0.2043 0.2340 0.3667 -0.0172 -0.0205 -0.0462 630 ASP A O 4784 C CB . ASP A 637 ? 0.2445 0.2114 0.3645 -0.0549 -0.0260 -0.0268 630 ASP A CB 4785 C CG . ASP A 637 ? 0.2780 0.2269 0.4137 -0.0624 0.0020 -0.0015 630 ASP A CG 4786 O OD1 . ASP A 637 ? 0.2420 0.3248 0.4430 -0.0799 -0.0108 0.0396 630 ASP A OD1 4787 O OD2 . ASP A 637 ? 0.3477 0.2301 0.4794 -0.1043 0.0104 0.0040 630 ASP A OD2 4788 N N . SER A 638 ? 0.1799 0.1941 0.3546 -0.0311 -0.0262 -0.0093 631 SER A N 4789 C CA . SER A 638 ? 0.1837 0.1722 0.2761 0.0044 -0.0220 -0.0180 631 SER A CA 4790 C C . SER A 638 ? 0.2159 0.1746 0.2835 -0.0044 -0.0256 -0.0263 631 SER A C 4791 O O . SER A 638 ? 0.2114 0.1957 0.2723 0.0011 -0.0206 -0.0211 631 SER A O 4792 C CB . SER A 638 ? 0.1726 0.2186 0.3084 -0.0025 -0.0216 -0.0377 631 SER A CB 4793 O OG . SER A 638 ? 0.2236 0.2292 0.3091 -0.0089 -0.0327 -0.0320 631 SER A OG 4794 N N . LEU A 639 ? 0.1770 0.1633 0.2748 0.0032 -0.0375 -0.0235 632 LEU A N 4795 C CA . LEU A 639 ? 0.2054 0.1452 0.2676 -0.0004 -0.0527 -0.0457 632 LEU A CA 4796 C C . LEU A 639 ? 0.1782 0.1772 0.2819 -0.0317 -0.0460 -0.0196 632 LEU A C 4797 O O . LEU A 639 ? 0.2118 0.1687 0.2792 -0.0113 -0.0766 0.0089 632 LEU A O 4798 C CB . LEU A 639 ? 0.2535 0.1494 0.2868 0.0136 -0.0017 -0.0305 632 LEU A CB 4799 C CG . LEU A 639 ? 0.1895 0.1512 0.2647 0.0062 -0.0105 -0.0222 632 LEU A CG 4800 C CD1 . LEU A 639 ? 0.2412 0.1496 0.2438 -0.0321 0.0046 -0.0198 632 LEU A CD1 4801 C CD2 . LEU A 639 ? 0.1972 0.1846 0.2898 0.0195 0.0222 -0.0331 632 LEU A CD2 4802 N N . PHE A 640 ? 0.1806 0.1554 0.3303 -0.0369 -0.0671 -0.0424 633 PHE A N 4803 C CA . PHE A 640 ? 0.1813 0.1922 0.3081 -0.0353 -0.0580 -0.0329 633 PHE A CA 4804 C C . PHE A 640 ? 0.1898 0.1862 0.3172 -0.0205 -0.0593 -0.0289 633 PHE A C 4805 O O . PHE A 640 ? 0.2603 0.2179 0.3286 -0.0013 -0.0446 -0.0248 633 PHE A O 4806 C CB . PHE A 640 ? 0.1756 0.1962 0.3651 -0.0245 -0.0407 -0.0281 633 PHE A CB 4807 C CG . PHE A 640 ? 0.2170 0.1970 0.3598 0.0102 -0.0623 -0.0415 633 PHE A CG 4808 C CD1 . PHE A 640 ? 0.2232 0.1995 0.4219 0.0175 -0.0569 -0.0248 633 PHE A CD1 4809 C CD2 . PHE A 640 ? 0.2188 0.2619 0.3840 0.0167 -0.0176 -0.0436 633 PHE A CD2 4810 C CE1 . PHE A 640 ? 0.2242 0.2362 0.4188 0.0015 -0.0275 -0.0315 633 PHE A CE1 4811 C CE2 . PHE A 640 ? 0.2033 0.2628 0.4003 0.0398 -0.0532 -0.0365 633 PHE A CE2 4812 C CZ . PHE A 640 ? 0.1649 0.2553 0.4112 -0.0022 -0.0536 -0.0191 633 PHE A CZ 4813 N N . SER A 641 ? 0.2101 0.1716 0.3359 -0.0044 -0.0166 -0.0424 634 SER A N 4814 C CA . SER A 641 ? 0.2048 0.1701 0.3236 0.0053 -0.0309 -0.0505 634 SER A CA 4815 C C . SER A 641 ? 0.1865 0.1668 0.2998 -0.0020 -0.0578 -0.0456 634 SER A C 4816 O O . SER A 641 ? 0.2098 0.2162 0.3063 -0.0077 -0.0677 -0.0598 634 SER A O 4817 C CB . SER A 641 ? 0.2776 0.1557 0.2984 0.0064 -0.0497 -0.0526 634 SER A CB 4818 O OG . SER A 641 ? 0.2526 0.2261 0.3040 0.0207 -0.0651 -0.0581 634 SER A OG 4819 N N . ALA A 642 ? 0.1994 0.1591 0.2943 -0.0051 -0.0452 -0.0478 635 ALA A N 4820 C CA . ALA A 642 ? 0.1767 0.1368 0.2846 -0.0172 -0.0852 -0.0434 635 ALA A CA 4821 C C . ALA A 642 ? 0.2045 0.1922 0.2963 0.0183 -0.0760 -0.0319 635 ALA A C 4822 O O . ALA A 642 ? 0.2164 0.2078 0.2756 -0.0027 -0.0656 -0.0627 635 ALA A O 4823 C CB . ALA A 642 ? 0.2046 0.1878 0.2467 -0.0294 -0.0702 -0.0568 635 ALA A CB 4824 N N . VAL A 643 ? 0.1845 0.1991 0.2779 0.0123 -0.0885 -0.0328 636 VAL A N 4825 C CA . VAL A 643 ? 0.2012 0.1846 0.2753 0.0193 -0.0750 -0.0213 636 VAL A CA 4826 C C . VAL A 643 ? 0.2411 0.1850 0.2961 -0.0134 -0.0867 -0.0164 636 VAL A C 4827 O O . VAL A 643 ? 0.2085 0.2211 0.2748 0.0158 -0.0856 0.0021 636 VAL A O 4828 C CB . VAL A 643 ? 0.2198 0.1849 0.2958 0.0436 -0.0942 -0.0467 636 VAL A CB 4829 C CG1 . VAL A 643 ? 0.1961 0.2328 0.2714 0.0014 -0.0864 -0.0048 636 VAL A CG1 4830 C CG2 . VAL A 643 ? 0.2308 0.1678 0.2876 -0.0109 -0.0442 -0.0433 636 VAL A CG2 4831 N N . LYS A 644 ? 0.2416 0.1749 0.3116 -0.0215 -0.0860 -0.0439 637 LYS A N 4832 C CA . LYS A 644 ? 0.2334 0.1871 0.3378 -0.0201 -0.0825 -0.0690 637 LYS A CA 4833 C C . LYS A 644 ? 0.2338 0.2156 0.3118 0.0022 -0.1059 -0.0430 637 LYS A C 4834 O O . LYS A 644 ? 0.2085 0.2313 0.3291 0.0278 -0.1298 -0.0601 637 LYS A O 4835 C CB . LYS A 644 ? 0.2802 0.2010 0.3353 -0.0386 -0.1013 -0.0429 637 LYS A CB 4836 C CG . LYS A 644 ? 0.3854 0.2381 0.3886 -0.0513 -0.1200 -0.0788 637 LYS A CG 4837 C CD . LYS A 644 ? 0.4556 0.2578 0.4261 -0.0719 -0.1037 -0.0681 637 LYS A CD 4838 C CE . LYS A 644 ? 0.5162 0.2614 0.4749 -0.0149 -0.1237 -0.0998 637 LYS A CE 4839 N NZ . LYS A 644 ? 0.5706 0.3942 0.5594 0.0064 -0.0910 -0.1168 637 LYS A NZ 4840 N N . ASN A 645 ? 0.2133 0.2059 0.2905 -0.0039 -0.0925 -0.0640 638 ASN A N 4841 C CA . ASN A 645 ? 0.2338 0.2197 0.2926 0.0321 -0.0929 -0.0473 638 ASN A CA 4842 C C . ASN A 645 ? 0.2395 0.2154 0.2668 0.0142 -0.0833 -0.0593 638 ASN A C 4843 O O . ASN A 645 ? 0.2413 0.2458 0.2581 0.0418 -0.0716 -0.0696 638 ASN A O 4844 C CB . ASN A 645 ? 0.2289 0.2081 0.2568 0.0302 -0.0887 -0.0528 638 ASN A CB 4845 C CG . ASN A 645 ? 0.2265 0.1985 0.3185 0.0050 -0.1162 -0.0772 638 ASN A CG 4846 O OD1 . ASN A 645 ? 0.2768 0.1815 0.3600 -0.0002 -0.1583 -0.0722 638 ASN A OD1 4847 N ND2 . ASN A 645 ? 0.2385 0.2376 0.3154 0.0506 -0.0865 -0.0265 638 ASN A ND2 4848 N N . PHE A 646 ? 0.2358 0.1974 0.2627 0.0493 -0.1154 -0.0439 639 PHE A N 4849 C CA . PHE A 646 ? 0.2394 0.1759 0.2480 0.0100 -0.0714 -0.0678 639 PHE A CA 4850 C C . PHE A 646 ? 0.2449 0.2362 0.2730 0.0086 -0.0880 -0.0704 639 PHE A C 4851 O O . PHE A 646 ? 0.2525 0.2292 0.2624 0.0130 -0.0891 -0.0523 639 PHE A O 4852 C CB . PHE A 646 ? 0.2283 0.1955 0.2399 -0.0296 -0.0769 -0.0818 639 PHE A CB 4853 C CG . PHE A 646 ? 0.2424 0.1971 0.2571 0.0025 -0.0721 -0.0479 639 PHE A CG 4854 C CD1 . PHE A 646 ? 0.2535 0.2257 0.2242 -0.0074 -0.0727 -0.0538 639 PHE A CD1 4855 C CD2 . PHE A 646 ? 0.2440 0.1840 0.2332 0.0083 -0.0606 -0.0628 639 PHE A CD2 4856 C CE1 . PHE A 646 ? 0.2375 0.2249 0.2629 0.0195 -0.0899 -0.0206 639 PHE A CE1 4857 C CE2 . PHE A 646 ? 0.2431 0.1965 0.2293 0.0033 -0.0671 -0.0397 639 PHE A CE2 4858 C CZ . PHE A 646 ? 0.2285 0.2424 0.2016 0.0241 -0.0829 -0.0457 639 PHE A CZ 4859 N N . THR A 647 ? 0.2271 0.2394 0.2856 0.0136 -0.1071 -0.0889 640 THR A N 4860 C CA . THR A 647 ? 0.2519 0.2430 0.3084 0.0153 -0.1233 -0.0842 640 THR A CA 4861 C C . THR A 647 ? 0.2845 0.2278 0.3126 0.0380 -0.1399 -0.0787 640 THR A C 4862 O O . THR A 647 ? 0.2881 0.2527 0.3273 0.0336 -0.1210 -0.0432 640 THR A O 4863 C CB . THR A 647 ? 0.2036 0.2413 0.2828 0.0290 -0.1432 -0.1031 640 THR A CB 4864 O OG1 . THR A 647 ? 0.2520 0.2522 0.3016 0.0041 -0.0753 -0.0998 640 THR A OG1 4865 C CG2 . THR A 647 ? 0.1414 0.3454 0.3361 0.0265 -0.1229 -0.0797 640 THR A CG2 4866 N N A GLU A 648 ? 0.2415 0.2165 0.3168 0.0353 -0.1259 -0.0855 641 GLU A N 4867 N N B GLU A 648 ? 0.2574 0.2218 0.3195 0.0335 -0.1226 -0.0844 641 GLU A N 4868 C CA A GLU A 648 ? 0.3051 0.2366 0.3211 0.0337 -0.1349 -0.0977 641 GLU A CA 4869 C CA B GLU A 648 ? 0.3089 0.2199 0.3340 0.0294 -0.1113 -0.0908 641 GLU A CA 4870 C C A GLU A 648 ? 0.3024 0.2283 0.3047 0.0271 -0.1293 -0.0965 641 GLU A C 4871 C C B GLU A 648 ? 0.2956 0.2336 0.3146 0.0236 -0.1258 -0.0839 641 GLU A C 4872 O O A GLU A 648 ? 0.2954 0.2416 0.3129 0.0457 -0.1443 -0.0715 641 GLU A O 4873 O O B GLU A 648 ? 0.3254 0.2664 0.3160 0.0134 -0.0997 -0.0775 641 GLU A O 4874 C CB A GLU A 648 ? 0.3162 0.2372 0.3104 -0.0099 -0.1553 -0.0642 641 GLU A CB 4875 C CB B GLU A 648 ? 0.2945 0.2212 0.3232 0.0303 -0.1145 -0.0731 641 GLU A CB 4876 C CG A GLU A 648 ? 0.3488 0.2985 0.4055 0.0109 -0.0932 -0.0743 641 GLU A CG 4877 C CG B GLU A 648 ? 0.3566 0.1322 0.4012 0.0247 -0.0996 -0.1010 641 GLU A CG 4878 C CD A GLU A 648 ? 0.3601 0.3143 0.4728 0.0348 -0.1410 -0.0430 641 GLU A CD 4879 C CD B GLU A 648 ? 0.4037 0.2372 0.4176 0.0459 -0.1211 -0.1156 641 GLU A CD 4880 O OE1 A GLU A 648 ? 0.5465 0.2978 0.5073 -0.0794 -0.0786 -0.0641 641 GLU A OE1 4881 O OE1 B GLU A 648 ? 0.3296 0.2801 0.5210 -0.0008 -0.1941 -0.2249 641 GLU A OE1 4882 O OE2 A GLU A 648 ? 0.4588 0.3734 0.6000 0.1430 0.0096 0.0347 641 GLU A OE2 4883 O OE2 B GLU A 648 ? 0.5177 0.2881 0.4175 0.0606 -0.0929 -0.1247 641 GLU A OE2 4884 N N . ILE A 649 ? 0.2810 0.2120 0.3155 0.0369 -0.1131 -0.0990 642 ILE A N 4885 C CA . ILE A 649 ? 0.3128 0.2399 0.2926 0.0035 -0.1303 -0.0783 642 ILE A CA 4886 C C . ILE A 649 ? 0.2884 0.2219 0.2762 0.0376 -0.1196 -0.0999 642 ILE A C 4887 O O . ILE A 649 ? 0.3095 0.2680 0.2666 0.0066 -0.1169 -0.0742 642 ILE A O 4888 C CB . ILE A 649 ? 0.2839 0.2429 0.2876 0.0421 -0.1152 -0.0604 642 ILE A CB 4889 C CG1 . ILE A 649 ? 0.2339 0.2413 0.2385 0.0521 -0.1129 -0.0706 642 ILE A CG1 4890 C CG2 . ILE A 649 ? 0.2699 0.2759 0.2723 0.0297 -0.1380 -0.0747 642 ILE A CG2 4891 C CD1 . ILE A 649 ? 0.2465 0.3010 0.2416 0.0160 -0.1194 -0.0824 642 ILE A CD1 4892 N N . ALA A 650 ? 0.2803 0.2080 0.2784 0.0729 -0.1250 -0.0767 643 ALA A N 4893 C CA . ALA A 650 ? 0.3293 0.2126 0.2781 0.0715 -0.0960 -0.0619 643 ALA A CA 4894 C C . ALA A 650 ? 0.3078 0.2874 0.3013 0.0471 -0.0982 -0.0804 643 ALA A C 4895 O O . ALA A 650 ? 0.3221 0.2574 0.2959 0.0581 -0.1501 -0.0920 643 ALA A O 4896 C CB . ALA A 650 ? 0.3970 0.2277 0.2757 0.0847 -0.0727 -0.0711 643 ALA A CB 4897 N N . SER A 651 ? 0.3389 0.2664 0.2752 0.0445 -0.1518 -0.1053 644 SER A N 4898 C CA . SER A 651 ? 0.3612 0.2945 0.2684 0.0425 -0.1459 -0.1343 644 SER A CA 4899 C C . SER A 651 ? 0.3281 0.2829 0.2980 0.0655 -0.1305 -0.0769 644 SER A C 4900 O O . SER A 651 ? 0.3403 0.2984 0.2982 0.0608 -0.0977 -0.0854 644 SER A O 4901 C CB . SER A 651 ? 0.3378 0.4170 0.3029 0.0174 -0.1372 -0.1119 644 SER A CB 4902 O OG . SER A 651 ? 0.4341 0.5004 0.3336 0.0592 -0.1947 -0.0958 644 SER A OG 4903 N N . LYS A 652 ? 0.3175 0.2678 0.3138 0.0593 -0.1331 -0.0901 645 LYS A N 4904 C CA . LYS A 652 ? 0.3578 0.2684 0.3339 0.0718 -0.1167 -0.0771 645 LYS A CA 4905 C C . LYS A 652 ? 0.3461 0.3090 0.2892 0.0619 -0.1386 -0.0995 645 LYS A C 4906 O O . LYS A 652 ? 0.3387 0.2795 0.2861 0.0496 -0.1326 -0.1177 645 LYS A O 4907 C CB . LYS A 652 ? 0.4132 0.2502 0.3194 0.0698 -0.1138 -0.0581 645 LYS A CB 4908 C CG . LYS A 652 ? 0.3947 0.3291 0.3590 0.0078 -0.1038 -0.1086 645 LYS A CG 4909 C CD . LYS A 652 ? 0.4930 0.4442 0.3755 -0.0109 -0.1438 -0.0800 645 LYS A CD 4910 C CE . LYS A 652 ? 0.4870 0.3096 0.3826 0.0296 -0.1390 -0.1680 645 LYS A CE 4911 N NZ . LYS A 652 ? 0.3521 0.2408 0.3957 -0.0151 -0.1297 -0.1361 645 LYS A NZ 4912 N N . PHE A 653 ? 0.3254 0.2647 0.2929 0.0701 -0.1334 -0.0896 646 PHE A N 4913 C CA . PHE A 653 ? 0.3640 0.2395 0.2507 0.0679 -0.1667 -0.0953 646 PHE A CA 4914 C C . PHE A 653 ? 0.3458 0.2797 0.2712 0.0867 -0.1423 -0.0718 646 PHE A C 4915 O O . PHE A 653 ? 0.3730 0.3112 0.2620 0.0950 -0.1240 -0.1082 646 PHE A O 4916 C CB . PHE A 653 ? 0.3367 0.2715 0.2185 0.0559 -0.1483 -0.0809 646 PHE A CB 4917 C CG . PHE A 653 ? 0.3633 0.2559 0.2283 0.0649 -0.1392 -0.0707 646 PHE A CG 4918 C CD1 . PHE A 653 ? 0.3574 0.2893 0.2639 0.0576 -0.1596 -0.0471 646 PHE A CD1 4919 C CD2 . PHE A 653 ? 0.3332 0.2672 0.2831 0.0697 -0.0899 -0.0640 646 PHE A CD2 4920 C CE1 . PHE A 653 ? 0.3634 0.2702 0.2603 0.0706 -0.1543 -0.0624 646 PHE A CE1 4921 C CE2 . PHE A 653 ? 0.3768 0.2910 0.2697 0.0353 -0.0932 -0.0418 646 PHE A CE2 4922 C CZ . PHE A 653 ? 0.3715 0.2803 0.2388 0.0960 -0.1117 -0.0515 646 PHE A CZ 4923 N N . SER A 654 ? 0.3479 0.2745 0.2652 0.0836 -0.1365 -0.0980 647 SER A N 4924 C CA . SER A 654 ? 0.3934 0.3131 0.2765 0.0947 -0.1234 -0.0616 647 SER A CA 4925 C C . SER A 654 ? 0.4060 0.3478 0.3028 0.1048 -0.1490 -0.0875 647 SER A C 4926 O O . SER A 654 ? 0.3467 0.4265 0.2749 0.1133 -0.1389 -0.0731 647 SER A O 4927 C CB . SER A 654 ? 0.3623 0.3042 0.2930 0.1514 -0.1513 -0.0707 647 SER A CB 4928 O OG A SER A 654 ? 0.3448 0.3422 0.2960 0.1143 -0.1197 -0.0893 647 SER A OG 4929 O OG B SER A 654 ? 0.4405 0.2964 0.2546 0.1048 -0.0793 0.0446 647 SER A OG 4930 N N . GLU A 655 ? 0.3432 0.3430 0.3081 0.1052 -0.1396 -0.1365 648 GLU A N 4931 C CA . GLU A 655 ? 0.4108 0.3647 0.3094 0.1210 -0.1352 -0.1415 648 GLU A CA 4932 C C . GLU A 655 ? 0.3996 0.4285 0.3057 0.0913 -0.1748 -0.0936 648 GLU A C 4933 O O . GLU A 655 ? 0.3679 0.4802 0.2686 0.1175 -0.1631 -0.1091 648 GLU A O 4934 C CB . GLU A 655 ? 0.4440 0.3655 0.3461 0.0271 -0.1582 -0.1698 648 GLU A CB 4935 C CG . GLU A 655 ? 0.4817 0.4866 0.4853 0.0323 -0.1225 -0.0831 648 GLU A CG 4936 C CD . GLU A 655 ? 0.5316 0.4622 0.6919 0.0238 -0.0849 -0.1394 648 GLU A CD 4937 O OE1 . GLU A 655 ? 0.4677 0.5923 0.6341 -0.0274 -0.0387 -0.1676 648 GLU A OE1 4938 O OE2 . GLU A 655 ? 0.5573 0.6106 0.9035 -0.0680 -0.0528 -0.1126 648 GLU A OE2 4939 N N . ARG A 656 ? 0.4093 0.3511 0.2592 0.1389 -0.1712 -0.1438 649 ARG A N 4940 C CA . ARG A 656 ? 0.4146 0.3686 0.2812 0.1187 -0.1843 -0.1077 649 ARG A CA 4941 C C . ARG A 656 ? 0.4140 0.3711 0.2559 0.1025 -0.1512 -0.1295 649 ARG A C 4942 O O . ARG A 656 ? 0.3899 0.4264 0.2529 0.0911 -0.1408 -0.1307 649 ARG A O 4943 C CB . ARG A 656 ? 0.3863 0.3384 0.2786 0.0987 -0.1725 -0.1058 649 ARG A CB 4944 C CG . ARG A 656 ? 0.3812 0.3332 0.3262 0.1525 -0.1705 -0.0959 649 ARG A CG 4945 C CD . ARG A 656 ? 0.3396 0.3431 0.2981 0.0958 -0.1616 -0.1065 649 ARG A CD 4946 N NE . ARG A 656 ? 0.3826 0.3485 0.2610 0.1072 -0.1434 -0.1029 649 ARG A NE 4947 C CZ . ARG A 656 ? 0.3886 0.3139 0.2951 0.0977 -0.0908 -0.0777 649 ARG A CZ 4948 N NH1 . ARG A 656 ? 0.3793 0.3057 0.3200 0.0855 -0.1396 -0.0784 649 ARG A NH1 4949 N NH2 . ARG A 656 ? 0.3903 0.2867 0.3127 0.0652 -0.0799 -0.0774 649 ARG A NH2 4950 N N . LEU A 657 ? 0.3943 0.3775 0.2654 0.1343 -0.1380 -0.1236 650 LEU A N 4951 C CA . LEU A 657 ? 0.4569 0.3957 0.2789 0.1735 -0.0775 -0.1071 650 LEU A CA 4952 C C . LEU A 657 ? 0.5069 0.4224 0.2814 0.1802 -0.0779 -0.1109 650 LEU A C 4953 O O . LEU A 657 ? 0.5471 0.4871 0.3372 0.1764 -0.0559 -0.0468 650 LEU A O 4954 C CB . LEU A 657 ? 0.5245 0.3231 0.3524 0.1669 0.0045 -0.1065 650 LEU A CB 4955 C CG . LEU A 657 ? 0.4348 0.3989 0.3091 0.1260 -0.0538 -0.1586 650 LEU A CG 4956 C CD1 . LEU A 657 ? 0.4264 0.4691 0.2109 0.1796 -0.0818 -0.0930 650 LEU A CD1 4957 C CD2 . LEU A 657 ? 0.4319 0.4196 0.2813 0.1233 -0.0405 -0.1336 650 LEU A CD2 4958 N N . GLN A 658 ? 0.4748 0.5645 0.2946 0.1833 -0.1295 -0.1131 651 GLN A N 4959 C CA . GLN A 658 ? 0.5946 0.6152 0.3873 0.1658 -0.1878 -0.0221 651 GLN A CA 4960 C C . GLN A 658 ? 0.5853 0.6152 0.3649 0.0874 -0.2909 -0.1096 651 GLN A C 4961 O O . GLN A 658 ? 0.6587 0.9799 0.4587 0.0276 -0.2402 0.1561 651 GLN A O 4962 C CB . GLN A 658 ? 0.5222 0.5640 0.5868 0.1456 -0.3148 0.1069 651 GLN A CB 4963 C CG . GLN A 658 ? 0.6232 0.6712 0.5141 0.1645 -0.2520 0.1971 651 GLN A CG 4964 C CD . GLN A 658 ? 0.7245 0.7714 0.9788 0.1318 -0.0905 -0.1079 651 GLN A CD 4965 O OE1 . GLN A 658 ? 0.8311 1.0393 1.2106 -0.0408 -0.1156 -0.1556 651 GLN A OE1 4966 N NE2 . GLN A 658 ? 0.4867 0.6806 1.0619 0.0447 -0.1803 -0.0865 651 GLN A NE2 4967 N N . ASP A 659 ? 0.5399 0.6455 0.3955 0.1146 -0.2070 -0.1283 652 ASP A N 4968 C CA . ASP A 659 ? 0.6832 0.6550 0.4017 0.0011 -0.1117 -0.1642 652 ASP A CA 4969 C C . ASP A 659 ? 0.6031 0.6382 0.4544 0.0107 -0.1402 -0.2066 652 ASP A C 4970 O O . ASP A 659 ? 0.5151 0.6016 0.4296 -0.0227 -0.1604 -0.1829 652 ASP A O 4971 C CB . ASP A 659 ? 0.6894 0.6739 0.3376 0.0542 -0.0959 -0.1682 652 ASP A CB 4972 C CG . ASP A 659 ? 0.7240 0.5855 0.4825 0.0536 -0.1890 -0.1630 652 ASP A CG 4973 O OD1 . ASP A 659 ? 0.9459 0.5313 0.6724 0.1066 -0.0227 -0.1874 652 ASP A OD1 4974 O OD2 . ASP A 659 ? 0.6862 0.7358 0.4682 0.1005 -0.1430 -0.0995 652 ASP A OD2 4975 N N . PHE A 660 ? 0.6773 0.6465 0.5973 -0.0055 -0.1262 -0.2914 653 PHE A N 4976 C CA . PHE A 660 ? 0.6020 0.6410 0.4700 0.0057 -0.1610 -0.2765 653 PHE A CA 4977 C C . PHE A 660 ? 0.7310 0.7651 0.3310 0.1568 -0.0924 -0.2682 653 PHE A C 4978 O O . PHE A 660 ? 0.8355 1.2198 0.4739 0.1747 -0.0706 -0.7306 653 PHE A O 4979 C CB . PHE A 660 ? 0.5364 0.5498 0.4743 0.1211 -0.1392 -0.2249 653 PHE A CB 4980 C CG . PHE A 660 ? 0.5438 0.5122 0.3208 0.1299 -0.1596 -0.1345 653 PHE A CG 4981 C CD1 . PHE A 660 ? 0.5992 0.4256 0.2867 0.2099 -0.1016 -0.0881 653 PHE A CD1 4982 C CD2 . PHE A 660 ? 0.5533 0.4517 0.3322 0.0904 -0.1691 -0.1357 653 PHE A CD2 4983 C CE1 . PHE A 660 ? 0.6439 0.3598 0.2768 0.1306 -0.0327 0.0430 653 PHE A CE1 4984 C CE2 . PHE A 660 ? 0.6624 0.4284 0.3936 0.0849 0.0118 -0.1140 653 PHE A CE2 4985 C CZ . PHE A 660 ? 0.6926 0.3586 0.4432 0.1201 0.0101 -0.0684 653 PHE A CZ 4986 N N A SER A 663 ? 0.2176 0.4214 0.2114 0.0990 -0.1451 -0.0765 656 SER A N 4987 N N B SER A 663 ? 0.4909 0.2409 0.2222 0.1913 -0.1245 0.0164 656 SER A N 4988 C CA A SER A 663 ? 0.4048 0.3333 0.0892 0.1553 -0.0217 -0.0397 656 SER A CA 4989 C CA B SER A 663 ? 0.4752 0.2626 0.1355 0.2051 -0.0855 -0.0220 656 SER A CA 4990 C C A SER A 663 ? 0.4265 0.3188 0.0695 0.1165 -0.0411 -0.0488 656 SER A C 4991 C C B SER A 663 ? 0.4383 0.2887 0.1014 0.1737 -0.0692 -0.0420 656 SER A C 4992 O O A SER A 663 ? 0.3747 0.3258 0.0943 0.1524 -0.0703 0.0001 656 SER A O 4993 O O B SER A 663 ? 0.4772 0.3786 0.0973 0.1229 -0.1062 0.0148 656 SER A O 4994 C CB A SER A 663 ? 0.1580 0.3923 0.0918 0.1635 0.0281 -0.0229 656 SER A CB 4995 C CB B SER A 663 ? 0.3217 0.3476 0.1840 0.0976 -0.1946 0.0306 656 SER A CB 4996 O OG A SER A 663 ? 0.2776 0.2986 0.0475 0.0058 0.0721 -0.0189 656 SER A OG 4997 O OG B SER A 663 ? 0.3184 0.2211 0.1098 -0.0046 -0.1371 -0.0118 656 SER A OG 4998 N N A ASN A 664 ? 0.3847 0.2616 0.1378 0.1200 -0.0856 -0.0018 657 ASN A N 4999 N N B ASN A 664 ? 0.4187 0.3191 0.0567 0.1470 -0.1111 -0.0440 657 ASN A N 5000 C CA A ASN A 664 ? 0.3836 0.2755 0.1251 0.1076 -0.0824 -0.0258 657 ASN A CA 5001 C CA B ASN A 664 ? 0.4382 0.3074 0.1554 0.1827 -0.0822 -0.0206 657 ASN A CA 5002 C C A ASN A 664 ? 0.3804 0.3131 0.0983 0.0995 -0.0656 -0.0254 657 ASN A C 5003 C C B ASN A 664 ? 0.4161 0.3494 0.1600 0.1299 -0.0575 -0.0336 657 ASN A C 5004 O O A ASN A 664 ? 0.3751 0.2628 0.1219 0.0230 -0.0449 -0.0597 657 ASN A O 5005 O O B ASN A 664 ? 0.3251 0.3318 0.2099 0.0721 -0.0640 -0.0008 657 ASN A O 5006 C CB A ASN A 664 ? 0.4146 0.2729 0.1763 0.1181 -0.0896 -0.0248 657 ASN A CB 5007 C CB B ASN A 664 ? 0.4444 0.3039 0.1782 0.1996 -0.0892 0.0394 657 ASN A CB 5008 C CG A ASN A 664 ? 0.4076 0.2785 0.1682 0.1539 -0.0411 -0.0091 657 ASN A CG 5009 C CG B ASN A 664 ? 0.4484 0.3443 0.2416 0.2455 -0.0716 -0.0501 657 ASN A CG 5010 O OD1 A ASN A 664 ? 0.3702 0.3386 0.1763 0.1289 -0.0360 -0.0129 657 ASN A OD1 5011 O OD1 B ASN A 664 ? 0.5004 0.4409 0.3194 0.1546 -0.0596 -0.0676 657 ASN A OD1 5012 N ND2 A ASN A 664 ? 0.4535 0.2874 0.2666 0.1439 -0.0017 -0.0492 657 ASN A ND2 5013 N ND2 B ASN A 664 ? 0.5127 0.3697 0.2542 0.2185 -0.0624 -0.1024 657 ASN A ND2 5014 N N A PRO A 665 ? 0.3263 0.3061 0.1092 0.1140 -0.0608 -0.0364 658 PRO A N 5015 N N B PRO A 665 ? 0.4747 0.3687 0.1492 0.0975 0.0079 -0.0336 658 PRO A N 5016 C CA A PRO A 665 ? 0.3221 0.2939 0.1191 0.1269 -0.0416 -0.0377 658 PRO A CA 5017 C CA B PRO A 665 ? 0.4134 0.3685 0.1603 0.0645 -0.0096 -0.0216 658 PRO A CA 5018 C C A PRO A 665 ? 0.3495 0.2816 0.1057 0.1178 -0.0280 -0.0306 658 PRO A C 5019 C C B PRO A 665 ? 0.4189 0.3615 0.1715 0.1164 -0.0174 -0.0253 658 PRO A C 5020 O O A PRO A 665 ? 0.3126 0.2823 0.1160 0.0926 -0.0431 -0.0457 658 PRO A O 5021 O O B PRO A 665 ? 0.4911 0.3059 0.1426 0.1550 -0.0231 0.0031 658 PRO A O 5022 C CB A PRO A 665 ? 0.3282 0.2604 0.1435 0.1382 -0.0421 -0.0210 658 PRO A CB 5023 C CB B PRO A 665 ? 0.4680 0.3636 0.1480 0.0533 0.0071 0.0230 658 PRO A CB 5024 C CG A PRO A 665 ? 0.3586 0.2701 0.1505 0.1116 -0.0276 -0.0569 658 PRO A CG 5025 C CG B PRO A 665 ? 0.3915 0.3824 0.1438 0.0913 0.0021 -0.0083 658 PRO A CG 5026 C CD A PRO A 665 ? 0.3854 0.2805 0.0761 0.1102 -0.0590 -0.0242 658 PRO A CD 5027 C CD B PRO A 665 ? 0.4345 0.3583 0.1267 0.1238 -0.0142 -0.0366 658 PRO A CD 5028 N N A ILE A 666 ? 0.3328 0.2760 0.1035 0.1069 -0.0347 -0.0378 659 ILE A N 5029 N N B ILE A 666 ? 0.4025 0.3624 0.1808 0.1089 -0.0352 -0.0280 659 ILE A N 5030 C CA A ILE A 666 ? 0.3678 0.2758 0.1365 0.1058 -0.0208 0.0059 659 ILE A CA 5031 C CA B ILE A 666 ? 0.4125 0.3415 0.1982 0.1380 -0.0274 -0.0269 659 ILE A CA 5032 C C A ILE A 666 ? 0.3373 0.2645 0.1228 0.1177 -0.0345 -0.0183 659 ILE A C 5033 C C B ILE A 666 ? 0.4199 0.3156 0.1663 0.1146 -0.0381 -0.0453 659 ILE A C 5034 O O A ILE A 666 ? 0.3283 0.2534 0.1187 0.0824 -0.0787 -0.0363 659 ILE A O 5035 O O B ILE A 666 ? 0.4061 0.3267 0.1610 0.1115 -0.0557 -0.0576 659 ILE A O 5036 C CB A ILE A 666 ? 0.3827 0.2895 0.1646 0.1216 -0.0056 0.0451 659 ILE A CB 5037 C CB B ILE A 666 ? 0.4052 0.3446 0.1683 0.1322 -0.0518 -0.0741 659 ILE A CB 5038 C CG1 A ILE A 666 ? 0.3627 0.3745 0.2450 0.0792 0.0073 0.0144 659 ILE A CG1 5039 C CG1 B ILE A 666 ? 0.4126 0.4038 0.2776 0.1318 -0.0304 -0.0424 659 ILE A CG1 5040 C CG2 A ILE A 666 ? 0.3605 0.2410 0.1667 0.1085 -0.0508 -0.0142 659 ILE A CG2 5041 C CG2 B ILE A 666 ? 0.4663 0.3558 0.2583 0.1759 -0.0665 -0.0221 659 ILE A CG2 5042 C CD1 A ILE A 666 ? 0.4236 0.3413 0.3907 0.1053 -0.0859 0.0370 659 ILE A CD1 5043 C CD1 B ILE A 666 ? 0.3811 0.3773 0.2630 0.1800 -0.0579 0.0053 659 ILE A CD1 5044 N N A VAL A 667 ? 0.3384 0.2473 0.1141 0.1111 -0.0225 -0.0255 660 VAL A N 5045 N N B VAL A 667 ? 0.3666 0.3238 0.1772 0.1534 -0.0479 -0.0453 660 VAL A N 5046 C CA A VAL A 667 ? 0.3631 0.2528 0.1435 0.0925 -0.0278 -0.0601 660 VAL A CA 5047 C CA B VAL A 667 ? 0.3598 0.2800 0.1440 0.1508 -0.0315 -0.0159 660 VAL A CA 5048 C C A VAL A 667 ? 0.3467 0.2789 0.1427 0.1299 -0.0463 -0.0190 660 VAL A C 5049 C C B VAL A 667 ? 0.3477 0.2714 0.1120 0.1358 -0.0559 -0.0387 660 VAL A C 5050 O O A VAL A 667 ? 0.3751 0.2837 0.1185 0.1229 -0.0519 -0.0757 660 VAL A O 5051 O O B VAL A 667 ? 0.3180 0.3416 0.1146 0.1342 -0.0720 -0.0041 660 VAL A O 5052 C CB A VAL A 667 ? 0.3568 0.2802 0.0938 0.1082 -0.0465 -0.0439 660 VAL A CB 5053 C CB B VAL A 667 ? 0.3442 0.2725 0.1641 0.1615 -0.0185 -0.0305 660 VAL A CB 5054 C CG1 A VAL A 667 ? 0.3473 0.3392 0.0853 0.0777 -0.0957 -0.0617 660 VAL A CG1 5055 C CG1 B VAL A 667 ? 0.3740 0.2946 0.1713 0.1239 -0.0299 0.0444 660 VAL A CG1 5056 C CG2 A VAL A 667 ? 0.3944 0.2514 0.1084 0.0837 -0.0369 -0.0864 660 VAL A CG2 5057 C CG2 B VAL A 667 ? 0.3709 0.2334 0.2144 0.1597 -0.0413 -0.0389 660 VAL A CG2 5058 N N A LEU A 668 ? 0.3560 0.2457 0.1654 0.1359 -0.0422 -0.0244 661 LEU A N 5059 N N B LEU A 668 ? 0.3080 0.2655 0.1233 0.1293 -0.0508 -0.0347 661 LEU A N 5060 C CA A LEU A 668 ? 0.3243 0.2586 0.1273 0.1285 -0.0561 -0.0308 661 LEU A CA 5061 C CA B LEU A 668 ? 0.3679 0.2573 0.1386 0.1410 -0.0376 -0.0422 661 LEU A CA 5062 C C A LEU A 668 ? 0.3539 0.2979 0.1336 0.1163 -0.0428 -0.0564 661 LEU A C 5063 C C B LEU A 668 ? 0.3424 0.2729 0.1515 0.1168 -0.0472 -0.0353 661 LEU A C 5064 O O A LEU A 668 ? 0.3236 0.2519 0.1007 0.1234 -0.0638 0.0112 661 LEU A O 5065 O O B LEU A 668 ? 0.3778 0.2881 0.1545 0.1347 -0.0352 -0.0372 661 LEU A O 5066 C CB A LEU A 668 ? 0.3451 0.2418 0.1512 0.1486 -0.0679 -0.0232 661 LEU A CB 5067 C CB B LEU A 668 ? 0.3474 0.2699 0.1119 0.1396 -0.0473 -0.0430 661 LEU A CB 5068 C CG A LEU A 668 ? 0.3122 0.2427 0.1417 0.1308 -0.0513 -0.0268 661 LEU A CG 5069 C CG B LEU A 668 ? 0.3334 0.2895 0.2015 0.1514 -0.0107 -0.0244 661 LEU A CG 5070 C CD1 A LEU A 668 ? 0.3137 0.2718 0.1547 0.1335 -0.0351 -0.0404 661 LEU A CD1 5071 C CD1 B LEU A 668 ? 0.3367 0.3231 0.1237 0.1220 -0.0311 -0.0846 661 LEU A CD1 5072 C CD2 A LEU A 668 ? 0.3421 0.1884 0.1197 0.1229 -0.1156 -0.0494 661 LEU A CD2 5073 C CD2 B LEU A 668 ? 0.3664 0.2885 0.1997 0.1902 -0.0309 -0.0208 661 LEU A CD2 5074 N N A ARG A 669 ? 0.3335 0.2791 0.1686 0.1268 -0.0778 -0.0360 662 ARG A N 5075 N N B ARG A 669 ? 0.3347 0.2754 0.1368 0.1711 -0.0663 -0.0429 662 ARG A N 5076 C CA A ARG A 669 ? 0.3604 0.2899 0.1406 0.1357 -0.0659 -0.0342 662 ARG A CA 5077 C CA B ARG A 669 ? 0.3389 0.2810 0.1442 0.1233 -0.0629 -0.0409 662 ARG A CA 5078 C C A ARG A 669 ? 0.3632 0.2709 0.1403 0.1259 -0.0807 -0.0462 662 ARG A C 5079 C C B ARG A 669 ? 0.4082 0.2593 0.1357 0.1328 -0.0781 -0.0506 662 ARG A C 5080 O O A ARG A 669 ? 0.3052 0.2590 0.1225 0.0922 -0.0998 -0.0356 662 ARG A O 5081 O O B ARG A 669 ? 0.3603 0.2730 0.1293 0.0984 -0.0320 -0.0377 662 ARG A O 5082 C CB A ARG A 669 ? 0.3605 0.2703 0.1292 0.1282 -0.0700 -0.0541 662 ARG A CB 5083 C CB B ARG A 669 ? 0.3248 0.2475 0.1043 0.1584 -0.0682 -0.0233 662 ARG A CB 5084 C CG A ARG A 669 ? 0.3199 0.2416 0.1187 0.1366 -0.0511 -0.0558 662 ARG A CG 5085 C CG B ARG A 669 ? 0.2673 0.3257 0.1536 0.1346 -0.0710 -0.0651 662 ARG A CG 5086 C CD A ARG A 669 ? 0.2541 0.2799 0.0636 0.1335 -0.0185 -0.0833 662 ARG A CD 5087 C CD B ARG A 669 ? 0.4217 0.3419 0.1931 0.0719 -0.0604 -0.0689 662 ARG A CD 5088 N NE A ARG A 669 ? 0.2995 0.2906 0.1404 0.0959 -0.0281 -0.0771 662 ARG A NE 5089 N NE B ARG A 669 ? 0.3257 0.3732 0.2277 0.0860 -0.0269 -0.0415 662 ARG A NE 5090 C CZ A ARG A 669 ? 0.3417 0.2851 0.1458 0.0800 -0.0283 -0.0395 662 ARG A CZ 5091 C CZ B ARG A 669 ? 0.3934 0.3339 0.2083 0.1025 0.0311 -0.0387 662 ARG A CZ 5092 N NH1 A ARG A 669 ? 0.3127 0.3056 0.1565 0.1055 -0.0285 -0.0535 662 ARG A NH1 5093 N NH1 B ARG A 669 ? 0.3817 0.3612 0.3017 0.0898 0.0151 0.0086 662 ARG A NH1 5094 N NH2 A ARG A 669 ? 0.2927 0.3279 0.1908 0.0666 0.0077 -0.0151 662 ARG A NH2 5095 N NH2 B ARG A 669 ? 0.3267 0.2953 0.2755 0.1675 0.0381 0.0120 662 ARG A NH2 5096 N N . MET A 670 ? 0.4145 0.2556 0.1834 0.1265 -0.1184 -0.0322 663 MET A N 5097 C CA . MET A 670 ? 0.3947 0.2491 0.1941 0.1169 -0.0834 -0.0436 663 MET A CA 5098 C C . MET A 670 ? 0.3912 0.2796 0.1838 0.1161 -0.0965 -0.0640 663 MET A C 5099 O O . MET A 670 ? 0.3446 0.2846 0.1785 0.0987 -0.1141 -0.0706 663 MET A O 5100 C CB A MET A 670 ? 0.3680 0.2507 0.2015 0.1514 -0.0669 -0.0353 663 MET A CB 5101 C CB B MET A 670 ? 0.4183 0.2681 0.2215 0.1371 -0.0438 -0.0430 663 MET A CB 5102 C CG A MET A 670 ? 0.3393 0.2499 0.2014 0.1355 -0.0390 -0.0642 663 MET A CG 5103 C CG B MET A 670 ? 0.4140 0.2924 0.2429 0.1246 -0.0483 -0.0588 663 MET A CG 5104 S SD A MET A 670 ? 0.2693 0.2455 0.1939 0.1013 -0.0882 -0.0683 663 MET A SD 5105 S SD B MET A 670 ? 0.4025 0.3600 0.1914 0.1420 -0.0644 -0.0928 663 MET A SD 5106 C CE A MET A 670 ? 0.3665 0.3688 0.3234 0.0542 0.0119 -0.0267 663 MET A CE 5107 C CE B MET A 670 ? 0.3756 0.2665 0.1083 0.2290 -0.0695 0.0100 663 MET A CE 5108 N N . MET A 671 ? 0.3824 0.2623 0.2386 0.1461 -0.1175 -0.0671 664 MET A N 5109 C CA . MET A 671 ? 0.3585 0.2717 0.1997 0.1129 -0.1208 -0.0651 664 MET A CA 5110 C C . MET A 671 ? 0.3412 0.2724 0.1875 0.0918 -0.1055 -0.0701 664 MET A C 5111 O O . MET A 671 ? 0.3988 0.2683 0.1969 0.1026 -0.1079 -0.0559 664 MET A O 5112 C CB A MET A 671 ? 0.3642 0.3182 0.2194 0.1141 -0.1318 -0.0896 664 MET A CB 5113 C CB B MET A 671 ? 0.3640 0.2658 0.1963 0.1162 -0.1005 -0.1371 664 MET A CB 5114 C CG A MET A 671 ? 0.3839 0.2923 0.2874 0.1324 -0.0604 -0.0778 664 MET A CG 5115 C CG B MET A 671 ? 0.2888 0.2182 0.1796 0.0960 -0.1184 -0.0377 664 MET A CG 5116 S SD A MET A 671 ? 0.4627 0.2900 0.3485 0.0327 -0.0955 -0.0695 664 MET A SD 5117 S SD B MET A 671 ? 0.3212 0.2505 0.1821 0.0664 -0.1159 -0.0651 664 MET A SD 5118 C CE A MET A 671 ? 0.4140 0.3266 0.3734 0.0783 -0.1167 0.0110 664 MET A CE 5119 C CE B MET A 671 ? 0.3087 0.3225 0.1673 0.1209 -0.1058 -0.0758 664 MET A CE 5120 N N . ASN A 672 ? 0.3868 0.2673 0.1908 0.1166 -0.1159 -0.0558 665 ASN A N 5121 C CA . ASN A 672 ? 0.3535 0.2531 0.1623 0.1144 -0.0932 -0.0340 665 ASN A CA 5122 C C . ASN A 672 ? 0.3479 0.2939 0.1524 0.0951 -0.0784 -0.0244 665 ASN A C 5123 O O . ASN A 672 ? 0.3892 0.2494 0.1630 0.0994 -0.0775 -0.0210 665 ASN A O 5124 C CB . ASN A 672 ? 0.3560 0.2550 0.1747 0.1165 -0.0947 -0.0359 665 ASN A CB 5125 C CG . ASN A 672 ? 0.3391 0.2948 0.1838 0.0960 -0.0935 -0.0231 665 ASN A CG 5126 O OD1 . ASN A 672 ? 0.3518 0.2876 0.2033 0.1161 -0.0731 -0.0106 665 ASN A OD1 5127 N ND2 . ASN A 672 ? 0.3647 0.2685 0.1843 0.1099 -0.0450 -0.0392 665 ASN A ND2 5128 N N . ASP A 673 ? 0.3387 0.2384 0.1811 0.0783 -0.0906 -0.0197 666 ASP A N 5129 C CA . ASP A 673 ? 0.3258 0.2556 0.1530 0.0650 -0.0673 -0.0108 666 ASP A CA 5130 C C . ASP A 673 ? 0.3116 0.2347 0.1651 0.0462 -0.0475 -0.0428 666 ASP A C 5131 O O . ASP A 673 ? 0.3015 0.2340 0.1614 0.0457 -0.0589 -0.0285 666 ASP A O 5132 C CB . ASP A 673 ? 0.3334 0.2736 0.1837 0.0642 -0.0593 -0.0062 666 ASP A CB 5133 C CG . ASP A 673 ? 0.3075 0.2877 0.2275 0.0651 -0.0504 -0.0245 666 ASP A CG 5134 O OD1 . ASP A 673 ? 0.3912 0.2718 0.1956 0.0496 -0.0420 0.0056 666 ASP A OD1 5135 O OD2 . ASP A 673 ? 0.3529 0.3003 0.1706 0.1010 -0.0603 -0.0246 666 ASP A OD2 5136 N N . GLN A 674 ? 0.2465 0.2309 0.1749 0.0599 -0.0659 -0.0270 667 GLN A N 5137 C CA . GLN A 674 ? 0.3007 0.2127 0.1837 0.0500 -0.0511 -0.0506 667 GLN A CA 5138 C C . GLN A 674 ? 0.2875 0.2150 0.1797 0.0636 -0.0773 -0.0550 667 GLN A C 5139 O O . GLN A 674 ? 0.3072 0.2464 0.2026 0.0814 -0.0546 -0.0328 667 GLN A O 5140 C CB . GLN A 674 ? 0.2528 0.1958 0.1926 0.0825 -0.0763 -0.0510 667 GLN A CB 5141 C CG . GLN A 674 ? 0.2526 0.1804 0.2280 0.0738 -0.0742 -0.0519 667 GLN A CG 5142 C CD . GLN A 674 ? 0.3159 0.1997 0.1755 0.0618 -0.0518 -0.0567 667 GLN A CD 5143 O OE1 . GLN A 674 ? 0.3695 0.2902 0.1873 0.0446 -0.0777 -0.0413 667 GLN A OE1 5144 N NE2 . GLN A 674 ? 0.2893 0.2326 0.1740 0.0420 -0.0606 -0.0248 667 GLN A NE2 5145 N N . LEU A 675 ? 0.2896 0.2128 0.2421 0.0752 -0.0723 -0.0306 668 LEU A N 5146 C CA . LEU A 675 ? 0.2832 0.2030 0.2098 0.0810 -0.0947 -0.0386 668 LEU A CA 5147 C C . LEU A 675 ? 0.2611 0.2442 0.1904 0.0601 -0.0905 -0.0324 668 LEU A C 5148 O O . LEU A 675 ? 0.2915 0.2637 0.2318 0.0634 -0.0714 -0.0345 668 LEU A O 5149 C CB . LEU A 675 ? 0.2881 0.2478 0.2145 0.0846 -0.1237 -0.0408 668 LEU A CB 5150 C CG . LEU A 675 ? 0.3329 0.2888 0.2403 0.0803 -0.1063 -0.0987 668 LEU A CG 5151 C CD1 . LEU A 675 ? 0.3432 0.3327 0.3269 0.1343 -0.1651 -0.0616 668 LEU A CD1 5152 C CD2 . LEU A 675 ? 0.3326 0.2709 0.3796 0.0625 -0.1021 -0.0927 668 LEU A CD2 5153 N N . MET A 676 ? 0.3032 0.2179 0.2109 0.0415 -0.0971 -0.0019 669 MET A N 5154 C CA . MET A 676 ? 0.2947 0.2274 0.1872 0.0395 -0.0694 -0.0142 669 MET A CA 5155 C C . MET A 676 ? 0.2667 0.2263 0.1766 0.0666 -0.0742 -0.0386 669 MET A C 5156 O O . MET A 676 ? 0.2865 0.2145 0.1768 0.0631 -0.0710 -0.0224 669 MET A O 5157 C CB . MET A 676 ? 0.2764 0.2400 0.1933 0.0340 -0.0452 -0.0446 669 MET A CB 5158 C CG . MET A 676 ? 0.3178 0.2370 0.2243 0.0318 -0.0322 -0.0627 669 MET A CG 5159 S SD . MET A 676 ? 0.3537 0.2533 0.2861 0.0562 0.0187 -0.0063 669 MET A SD 5160 C CE . MET A 676 ? 0.3052 0.2854 0.2208 0.0556 -0.0146 0.0026 669 MET A CE 5161 N N . PHE A 677 ? 0.2678 0.2010 0.1691 0.0503 -0.0741 -0.0132 670 PHE A N 5162 C CA . PHE A 677 ? 0.2335 0.2178 0.1672 0.0673 -0.0481 -0.0097 670 PHE A CA 5163 C C . PHE A 677 ? 0.2327 0.2135 0.1867 0.0453 -0.0482 -0.0222 670 PHE A C 5164 O O . PHE A 677 ? 0.2528 0.2122 0.1782 0.0313 -0.0447 -0.0356 670 PHE A O 5165 C CB . PHE A 677 ? 0.2149 0.2243 0.1590 0.0536 -0.0202 -0.0138 670 PHE A CB 5166 C CG . PHE A 677 ? 0.2365 0.2100 0.1864 0.0481 -0.0179 -0.0539 670 PHE A CG 5167 C CD1 . PHE A 677 ? 0.2383 0.2393 0.1779 0.0195 -0.0390 -0.0396 670 PHE A CD1 5168 C CD2 . PHE A 677 ? 0.2617 0.2684 0.1727 0.0158 0.0090 -0.0126 670 PHE A CD2 5169 C CE1 . PHE A 677 ? 0.2215 0.2690 0.1550 0.0421 0.0509 -0.0275 670 PHE A CE1 5170 C CE2 . PHE A 677 ? 0.2368 0.2324 0.1758 0.0316 0.0126 -0.0525 670 PHE A CE2 5171 C CZ . PHE A 677 ? 0.2746 0.2653 0.1466 0.0497 0.0435 -0.0831 670 PHE A CZ 5172 N N . LEU A 678 ? 0.2418 0.2261 0.1806 0.0353 -0.0477 -0.0273 671 LEU A N 5173 C CA . LEU A 678 ? 0.2035 0.2275 0.1758 0.0349 -0.0636 -0.0413 671 LEU A CA 5174 C C . LEU A 678 ? 0.2107 0.1916 0.1654 0.0352 -0.0519 -0.0230 671 LEU A C 5175 O O . LEU A 678 ? 0.2261 0.2000 0.1770 0.0298 -0.0443 -0.0201 671 LEU A O 5176 C CB . LEU A 678 ? 0.2067 0.2563 0.2142 0.0124 -0.0773 -0.0433 671 LEU A CB 5177 C CG . LEU A 678 ? 0.2163 0.2423 0.2034 0.0173 -0.1043 0.0042 671 LEU A CG 5178 C CD1 . LEU A 678 ? 0.2566 0.2365 0.2799 0.0495 -0.0673 -0.0031 671 LEU A CD1 5179 C CD2 . LEU A 678 ? 0.2471 0.2946 0.2217 0.0196 -0.1274 -0.0434 671 LEU A CD2 5180 N N . GLU A 679 ? 0.2143 0.1922 0.1718 0.0260 -0.0381 -0.0372 672 GLU A N 5181 C CA . GLU A 679 ? 0.2249 0.1697 0.1725 0.0619 -0.0411 -0.0211 672 GLU A CA 5182 C C . GLU A 679 ? 0.2038 0.1936 0.1514 0.0184 -0.0327 -0.0064 672 GLU A C 5183 O O . GLU A 679 ? 0.2057 0.1870 0.1537 0.0314 -0.0253 0.0002 672 GLU A O 5184 C CB . GLU A 679 ? 0.2148 0.1615 0.1866 0.0477 -0.0262 -0.0142 672 GLU A CB 5185 C CG . GLU A 679 ? 0.1829 0.1770 0.1938 0.0218 -0.0243 -0.0274 672 GLU A CG 5186 C CD . GLU A 679 ? 0.1887 0.2071 0.2533 0.0253 -0.0171 0.0111 672 GLU A CD 5187 O OE1 . GLU A 679 ? 0.2340 0.2114 0.2128 0.0267 -0.0194 -0.0013 672 GLU A OE1 5188 O OE2 . GLU A 679 ? 0.2172 0.2070 0.1836 0.0098 -0.0216 -0.0393 672 GLU A OE2 5189 N N . ARG A 680 ? 0.1981 0.1830 0.1492 0.0517 -0.0457 -0.0137 673 ARG A N 5190 C CA . ARG A 680 ? 0.1622 0.1929 0.1956 0.0285 -0.0335 0.0045 673 ARG A CA 5191 C C . ARG A 680 ? 0.1942 0.1913 0.1584 0.0004 -0.0356 -0.0047 673 ARG A C 5192 O O . ARG A 680 ? 0.2169 0.1648 0.1535 0.0123 -0.0327 -0.0028 673 ARG A O 5193 C CB . ARG A 680 ? 0.1708 0.2205 0.1564 0.0212 -0.0370 -0.0443 673 ARG A CB 5194 C CG . ARG A 680 ? 0.1757 0.1582 0.1807 0.0414 -0.0738 -0.0058 673 ARG A CG 5195 C CD . ARG A 680 ? 0.2509 0.1635 0.1650 0.0401 0.0013 0.0276 673 ARG A CD 5196 N NE . ARG A 680 ? 0.2221 0.1541 0.1273 0.0241 -0.0217 -0.0105 673 ARG A NE 5197 C CZ . ARG A 680 ? 0.1918 0.1756 0.1532 0.0591 0.0058 0.0002 673 ARG A CZ 5198 N NH1 . ARG A 680 ? 0.1885 0.1839 0.1889 0.0557 0.0070 -0.0021 673 ARG A NH1 5199 N NH2 . ARG A 680 ? 0.2949 0.1914 0.1441 0.0017 0.0036 -0.0220 673 ARG A NH2 5200 N N . ALA A 681 ? 0.1945 0.1471 0.1862 0.0322 -0.0062 -0.0164 674 ALA A N 5201 C CA . ALA A 681 ? 0.2163 0.1492 0.1477 0.0082 -0.0239 -0.0210 674 ALA A CA 5202 C C . ALA A 681 ? 0.1942 0.1639 0.1596 0.0218 -0.0279 -0.0149 674 ALA A C 5203 O O . ALA A 681 ? 0.2242 0.1938 0.1673 0.0359 -0.0139 0.0136 674 ALA A O 5204 C CB . ALA A 681 ? 0.2216 0.1556 0.1846 -0.0013 -0.0312 -0.0378 674 ALA A CB 5205 N N . PHE A 682 ? 0.1996 0.1848 0.1821 0.0124 -0.0109 -0.0361 675 PHE A N 5206 C CA . PHE A 682 ? 0.1641 0.1914 0.1685 0.0263 -0.0262 -0.0279 675 PHE A CA 5207 C C . PHE A 682 ? 0.1817 0.1907 0.1713 0.0154 -0.0319 -0.0171 675 PHE A C 5208 O O . PHE A 682 ? 0.1862 0.2171 0.1821 0.0046 -0.0170 -0.0289 675 PHE A O 5209 C CB . PHE A 682 ? 0.1598 0.1802 0.1857 0.0139 -0.0348 -0.0323 675 PHE A CB 5210 C CG . PHE A 682 ? 0.1844 0.1876 0.1857 0.0020 -0.0462 -0.0296 675 PHE A CG 5211 C CD1 . PHE A 682 ? 0.1936 0.1798 0.2220 0.0087 -0.0188 -0.0214 675 PHE A CD1 5212 C CD2 . PHE A 682 ? 0.1987 0.2211 0.1677 0.0223 -0.0522 -0.0436 675 PHE A CD2 5213 C CE1 . PHE A 682 ? 0.2015 0.2340 0.1690 0.0276 -0.0278 -0.0359 675 PHE A CE1 5214 C CE2 . PHE A 682 ? 0.1804 0.2050 0.2396 0.0130 -0.0518 -0.0639 675 PHE A CE2 5215 C CZ . PHE A 682 ? 0.1995 0.2414 0.2069 0.0219 -0.0299 0.0053 675 PHE A CZ 5216 N N . ILE A 683 ? 0.1886 0.2005 0.1830 0.0060 -0.0074 -0.0230 676 ILE A N 5217 C CA . ILE A 683 ? 0.1820 0.1847 0.1699 0.0118 -0.0283 0.0130 676 ILE A CA 5218 C C . ILE A 683 ? 0.1956 0.1908 0.1642 0.0316 -0.0233 -0.0033 676 ILE A C 5219 O O . ILE A 683 ? 0.2296 0.2234 0.1904 0.0439 -0.0140 -0.0234 676 ILE A O 5220 C CB . ILE A 683 ? 0.1504 0.1763 0.1512 0.0132 -0.0302 -0.0094 676 ILE A CB 5221 C CG1 . ILE A 683 ? 0.1889 0.1486 0.1554 0.0379 0.0238 -0.0271 676 ILE A CG1 5222 C CG2 . ILE A 683 ? 0.1929 0.2340 0.1574 0.0004 -0.0440 -0.0224 676 ILE A CG2 5223 C CD1 . ILE A 683 ? 0.1908 0.1858 0.1145 0.0013 0.0125 -0.0567 676 ILE A CD1 5224 N N . ASP A 684 ? 0.2020 0.1914 0.1606 0.0360 -0.0182 -0.0008 677 ASP A N 5225 C CA . ASP A 684 ? 0.2094 0.1957 0.1892 0.0419 -0.0161 0.0088 677 ASP A CA 5226 C C . ASP A 684 ? 0.2145 0.2065 0.1702 0.0142 0.0020 0.0127 677 ASP A C 5227 O O . ASP A 684 ? 0.2051 0.2057 0.1924 -0.0069 -0.0114 0.0064 677 ASP A O 5228 C CB . ASP A 684 ? 0.2423 0.1842 0.1997 0.0151 -0.0104 0.0100 677 ASP A CB 5229 C CG . ASP A 684 ? 0.2160 0.1758 0.1917 0.0120 0.0019 0.0066 677 ASP A CG 5230 O OD1 . ASP A 684 ? 0.2396 0.2272 0.1843 0.0280 -0.0154 -0.0070 677 ASP A OD1 5231 O OD2 . ASP A 684 ? 0.2106 0.2263 0.2025 -0.0013 0.0104 0.0224 677 ASP A OD2 5232 N N . PRO A 685 ? 0.2266 0.2328 0.1929 0.0355 -0.0206 0.0046 678 PRO A N 5233 C CA . PRO A 685 ? 0.2329 0.3098 0.1924 0.0061 0.0224 -0.0135 678 PRO A CA 5234 C C . PRO A 685 ? 0.2443 0.2602 0.2019 -0.0132 -0.0094 -0.0028 678 PRO A C 5235 O O . PRO A 685 ? 0.3223 0.3289 0.2671 -0.1108 -0.0164 0.0179 678 PRO A O 5236 C CB . PRO A 685 ? 0.2219 0.3130 0.2571 0.0488 -0.0025 -0.0014 678 PRO A CB 5237 C CG . PRO A 685 ? 0.2139 0.3485 0.2936 0.0235 -0.0289 -0.0219 678 PRO A CG 5238 C CD . PRO A 685 ? 0.1904 0.2795 0.2294 0.0618 0.0313 -0.0141 678 PRO A CD 5239 N N . LEU A 686 ? 0.2312 0.2437 0.1949 0.0239 0.0023 0.0117 679 LEU A N 5240 C CA . LEU A 686 ? 0.2151 0.2072 0.1918 0.0177 -0.0105 -0.0120 679 LEU A CA 5241 C C . LEU A 686 ? 0.2142 0.2522 0.1987 0.0291 -0.0064 -0.0096 679 LEU A C 5242 O O . LEU A 686 ? 0.2136 0.2719 0.1866 0.0434 -0.0280 -0.0002 679 LEU A O 5243 C CB . LEU A 686 ? 0.2261 0.2160 0.2009 0.0304 0.0075 0.0179 679 LEU A CB 5244 C CG . LEU A 686 ? 0.2349 0.2147 0.2394 0.0302 -0.0141 -0.0139 679 LEU A CG 5245 C CD1 . LEU A 686 ? 0.2881 0.2107 0.2196 -0.0159 -0.0404 -0.0192 679 LEU A CD1 5246 C CD2 . LEU A 686 ? 0.2166 0.2824 0.3308 0.0419 -0.0139 -0.0062 679 LEU A CD2 5247 N N . GLY A 687 ? 0.1896 0.2194 0.2140 0.0166 -0.0001 0.0051 680 GLY A N 5248 C CA . GLY A 687 ? 0.1836 0.2638 0.2370 0.0204 0.0371 0.0020 680 GLY A CA 5249 C C . GLY A 687 ? 0.1950 0.2071 0.2298 0.0135 0.0129 0.0000 680 GLY A C 5250 O O . GLY A 687 ? 0.2211 0.2145 0.2671 0.0032 0.0413 0.0144 680 GLY A O 5251 N N . LEU A 688 ? 0.1603 0.2134 0.2460 0.0072 0.0253 -0.0050 681 LEU A N 5252 C CA . LEU A 688 ? 0.1995 0.2286 0.2147 0.0140 0.0097 0.0209 681 LEU A CA 5253 C C . LEU A 688 ? 0.2013 0.2100 0.2197 0.0204 0.0243 0.0103 681 LEU A C 5254 O O . LEU A 688 ? 0.2433 0.2352 0.2258 -0.0054 -0.0025 0.0378 681 LEU A O 5255 C CB . LEU A 688 ? 0.2102 0.2249 0.2402 0.0245 -0.0167 0.0060 681 LEU A CB 5256 C CG . LEU A 688 ? 0.1976 0.1956 0.2525 0.0019 -0.0086 -0.0001 681 LEU A CG 5257 C CD1 . LEU A 688 ? 0.2283 0.2297 0.3062 0.0082 -0.0412 0.0241 681 LEU A CD1 5258 C CD2 . LEU A 688 ? 0.2061 0.2351 0.3598 -0.0336 -0.0312 0.0243 681 LEU A CD2 5259 N N . PRO A 689 ? 0.2616 0.2589 0.2392 -0.0313 0.0025 0.0355 682 PRO A N 5260 C CA . PRO A 689 ? 0.2550 0.2677 0.2158 -0.0290 0.0256 0.0430 682 PRO A CA 5261 C C . PRO A 689 ? 0.2532 0.2752 0.2278 -0.0002 0.0108 0.0356 682 PRO A C 5262 O O . PRO A 689 ? 0.2278 0.2694 0.2598 -0.0095 0.0135 0.0365 682 PRO A O 5263 C CB . PRO A 689 ? 0.2575 0.2624 0.2687 -0.0472 0.0125 0.0499 682 PRO A CB 5264 C CG . PRO A 689 ? 0.2924 0.3012 0.2349 -0.0234 -0.0002 0.0531 682 PRO A CG 5265 C CD . PRO A 689 ? 0.2550 0.2423 0.2811 -0.0378 0.0158 0.0676 682 PRO A CD 5266 N N . ASP A 690 ? 0.2588 0.2571 0.2010 -0.0002 0.0023 0.0553 683 ASP A N 5267 C CA . ASP A 690 ? 0.3160 0.2813 0.2047 -0.0306 0.0031 0.0336 683 ASP A CA 5268 C C . ASP A 690 ? 0.2589 0.2425 0.1828 -0.0002 -0.0141 0.0035 683 ASP A C 5269 O O . ASP A 690 ? 0.2385 0.2652 0.1830 0.0016 -0.0195 -0.0218 683 ASP A O 5270 C CB . ASP A 690 ? 0.3544 0.3552 0.1964 0.0008 0.0134 0.0401 683 ASP A CB 5271 C CG . ASP A 690 ? 0.3977 0.4656 0.3658 0.0192 0.0250 0.1556 683 ASP A CG 5272 O OD1 . ASP A 690 ? 0.4108 0.5420 0.3412 0.0498 0.0170 0.1286 683 ASP A OD1 5273 O OD2 . ASP A 690 ? 0.4731 0.5742 0.4027 -0.0409 0.0579 0.1842 683 ASP A OD2 5274 N N . ARG A 691 ? 0.2035 0.2318 0.1689 -0.0082 -0.0032 0.0290 684 ARG A N 5275 C CA . ARG A 691 ? 0.1998 0.2223 0.1610 0.0056 0.0041 0.0132 684 ARG A CA 5276 C C . ARG A 691 ? 0.1857 0.2166 0.1630 -0.0143 -0.0002 0.0000 684 ARG A C 5277 O O . ARG A 691 ? 0.1867 0.1879 0.1616 -0.0163 -0.0143 0.0130 684 ARG A O 5278 C CB . ARG A 691 ? 0.1785 0.2332 0.1714 -0.0108 0.0191 0.0038 684 ARG A CB 5279 C CG . ARG A 691 ? 0.1635 0.2324 0.2121 0.0132 0.0308 -0.0138 684 ARG A CG 5280 C CD . ARG A 691 ? 0.1579 0.2117 0.2130 -0.0176 -0.0177 -0.0258 684 ARG A CD 5281 N NE . ARG A 691 ? 0.2102 0.2130 0.2067 -0.0477 0.0291 -0.0353 684 ARG A NE 5282 C CZ . ARG A 691 ? 0.2284 0.2020 0.2410 0.0012 0.0237 0.0166 684 ARG A CZ 5283 N NH1 . ARG A 691 ? 0.2250 0.1987 0.2220 0.0267 0.0329 0.0334 684 ARG A NH1 5284 N NH2 . ARG A 691 ? 0.2754 0.2207 0.2297 -0.0250 0.0543 -0.0140 684 ARG A NH2 5285 N N . PRO A 692 ? 0.1757 0.2048 0.1819 0.0085 -0.0001 -0.0131 685 PRO A N 5286 C CA . PRO A 692 ? 0.1949 0.2314 0.1670 0.0133 0.0000 -0.0153 685 PRO A CA 5287 C C . PRO A 692 ? 0.1903 0.2012 0.1666 -0.0075 -0.0017 -0.0133 685 PRO A C 5288 O O . PRO A 692 ? 0.2109 0.1930 0.1797 0.0086 0.0067 -0.0079 685 PRO A O 5289 C CB . PRO A 692 ? 0.2189 0.2580 0.1973 -0.0026 -0.0201 -0.0560 685 PRO A CB 5290 C CG . PRO A 692 ? 0.1959 0.2611 0.2060 -0.0296 -0.0044 -0.0603 685 PRO A CG 5291 C CD . PRO A 692 ? 0.1919 0.2622 0.1672 -0.0041 -0.0086 -0.0141 685 PRO A CD 5292 N N . PHE A 693 ? 0.1777 0.1963 0.1534 -0.0120 0.0086 -0.0055 686 PHE A N 5293 C CA . PHE A 693 ? 0.1687 0.1740 0.1831 -0.0239 -0.0292 0.0050 686 PHE A CA 5294 C C . PHE A 693 ? 0.1470 0.1970 0.1775 -0.0020 -0.0184 0.0003 686 PHE A C 5295 O O . PHE A 693 ? 0.1837 0.2151 0.1831 -0.0106 -0.0160 0.0102 686 PHE A O 5296 C CB . PHE A 693 ? 0.1552 0.1809 0.1895 -0.0341 -0.0237 -0.0042 686 PHE A CB 5297 C CG . PHE A 693 ? 0.1481 0.1833 0.1728 -0.0141 -0.0252 0.0091 686 PHE A CG 5298 C CD1 . PHE A 693 ? 0.1779 0.1841 0.2332 -0.0241 0.0077 0.0065 686 PHE A CD1 5299 C CD2 . PHE A 693 ? 0.1989 0.2093 0.2041 -0.0322 -0.0224 -0.0283 686 PHE A CD2 5300 C CE1 . PHE A 693 ? 0.1883 0.1735 0.2097 -0.0194 -0.0054 0.0006 686 PHE A CE1 5301 C CE2 . PHE A 693 ? 0.1776 0.2106 0.2103 -0.0319 0.0038 0.0084 686 PHE A CE2 5302 C CZ . PHE A 693 ? 0.2034 0.2222 0.1998 -0.0335 0.0165 -0.0040 686 PHE A CZ 5303 N N . TYR A 694 ? 0.1486 0.1815 0.1722 0.0040 -0.0084 -0.0185 687 TYR A N 5304 C CA . TYR A 694 ? 0.1511 0.1878 0.1450 0.0031 -0.0065 -0.0168 687 TYR A CA 5305 C C . TYR A 694 ? 0.1809 0.1910 0.1577 0.0000 0.0044 -0.0125 687 TYR A C 5306 O O . TYR A 694 ? 0.2385 0.2004 0.1790 0.0029 0.0226 -0.0067 687 TYR A O 5307 C CB . TYR A 694 ? 0.1674 0.1928 0.1770 0.0157 0.0100 -0.0246 687 TYR A CB 5308 C CG . TYR A 694 ? 0.1785 0.1760 0.1726 0.0063 -0.0044 -0.0126 687 TYR A CG 5309 C CD1 . TYR A 694 ? 0.2212 0.1729 0.1788 0.0287 -0.0121 -0.0061 687 TYR A CD1 5310 C CD2 . TYR A 694 ? 0.2307 0.1966 0.1851 0.0430 0.0023 -0.0505 687 TYR A CD2 5311 C CE1 . TYR A 694 ? 0.1792 0.1777 0.2107 0.0143 0.0060 -0.0271 687 TYR A CE1 5312 C CE2 . TYR A 694 ? 0.2213 0.1658 0.1891 0.0131 -0.0049 -0.0169 687 TYR A CE2 5313 C CZ . TYR A 694 ? 0.2082 0.1721 0.1866 -0.0085 -0.0093 -0.0266 687 TYR A CZ 5314 O OH . TYR A 694 ? 0.2135 0.2010 0.2237 0.0172 -0.0002 -0.0476 687 TYR A OH 5315 N N A ARG A 695 ? 0.1420 0.1754 0.1620 -0.0092 -0.0002 -0.0351 688 ARG A N 5316 N N B ARG A 695 ? 0.1540 0.1802 0.1624 -0.0059 0.0016 -0.0271 688 ARG A N 5317 C CA A ARG A 695 ? 0.1266 0.1740 0.1941 -0.0067 0.0070 -0.0268 688 ARG A CA 5318 C CA B ARG A 695 ? 0.1502 0.1785 0.1918 -0.0013 0.0030 -0.0229 688 ARG A CA 5319 C C A ARG A 695 ? 0.1655 0.1725 0.1626 0.0019 -0.0209 -0.0088 688 ARG A C 5320 C C B ARG A 695 ? 0.1610 0.1696 0.1769 0.0066 -0.0088 -0.0085 688 ARG A C 5321 O O A ARG A 695 ? 0.1778 0.1745 0.1688 0.0002 -0.0172 -0.0169 688 ARG A O 5322 O O B ARG A 695 ? 0.1867 0.1718 0.1615 -0.0019 0.0155 -0.0131 688 ARG A O 5323 C CB A ARG A 695 ? 0.1312 0.1733 0.1363 -0.0301 -0.0130 -0.0195 688 ARG A CB 5324 C CB B ARG A 695 ? 0.1501 0.1829 0.1654 -0.0182 -0.0088 -0.0215 688 ARG A CB 5325 C CG A ARG A 695 ? 0.1361 0.2104 0.1250 -0.0306 -0.0217 -0.0232 688 ARG A CG 5326 C CG B ARG A 695 ? 0.1620 0.1975 0.1597 -0.0129 -0.0140 -0.0359 688 ARG A CG 5327 C CD A ARG A 695 ? 0.1621 0.2187 0.1512 0.0104 0.0188 0.0279 688 ARG A CD 5328 C CD B ARG A 695 ? 0.1497 0.1648 0.1786 0.0000 -0.0100 -0.0509 688 ARG A CD 5329 N NE A ARG A 695 ? 0.1985 0.2225 0.1189 -0.0199 -0.0078 -0.0060 688 ARG A NE 5330 N NE B ARG A 695 ? 0.1303 0.1846 0.1438 0.0078 -0.0135 -0.0368 688 ARG A NE 5331 C CZ A ARG A 695 ? 0.1644 0.2168 0.1757 0.0124 -0.0053 0.0596 688 ARG A CZ 5332 C CZ B ARG A 695 ? 0.1123 0.1448 0.1022 0.0064 -0.0332 -0.0713 688 ARG A CZ 5333 N NH1 A ARG A 695 ? 0.1350 0.1746 0.1465 -0.0339 0.0140 0.0289 688 ARG A NH1 5334 N NH1 B ARG A 695 ? 0.0509 0.1044 0.0674 0.0352 -0.0123 -0.0502 688 ARG A NH1 5335 N NH2 A ARG A 695 ? 0.1267 0.2702 0.2098 0.0009 -0.0124 0.0831 688 ARG A NH2 5336 N NH2 B ARG A 695 ? 0.1366 0.1927 0.1074 0.0324 0.0232 -0.0497 688 ARG A NH2 5337 N N . HIS A 696 ? 0.1561 0.1868 0.1823 0.0076 -0.0097 -0.0026 689 HIS A N 5338 C CA . HIS A 696 ? 0.1809 0.1528 0.1736 0.0027 -0.0213 0.0130 689 HIS A CA 5339 C C . HIS A 696 ? 0.1762 0.1613 0.1828 -0.0087 -0.0053 -0.0150 689 HIS A C 5340 O O . HIS A 696 ? 0.2040 0.1767 0.1707 -0.0130 -0.0029 0.0046 689 HIS A O 5341 C CB . HIS A 696 ? 0.2027 0.1651 0.1656 0.0259 -0.0378 -0.0129 689 HIS A CB 5342 C CG . HIS A 696 ? 0.1880 0.1861 0.1727 -0.0013 -0.0403 -0.0007 689 HIS A CG 5343 N ND1 . HIS A 696 ? 0.1843 0.1886 0.1566 -0.0018 -0.0332 -0.0304 689 HIS A ND1 5344 C CD2 . HIS A 696 ? 0.2124 0.2145 0.1511 0.0092 -0.0231 -0.0297 689 HIS A CD2 5345 C CE1 . HIS A 696 ? 0.1705 0.1920 0.1732 0.0049 -0.0525 -0.0143 689 HIS A CE1 5346 N NE2 . HIS A 696 ? 0.1776 0.1838 0.2113 0.0185 -0.0251 -0.0258 689 HIS A NE2 5347 N N . VAL A 697 ? 0.1892 0.1406 0.2025 -0.0173 -0.0112 0.0014 690 VAL A N 5348 C CA . VAL A 697 ? 0.1581 0.1440 0.1936 -0.0058 -0.0157 -0.0075 690 VAL A CA 5349 C C . VAL A 697 ? 0.1691 0.1997 0.2030 -0.0133 -0.0338 0.0026 690 VAL A C 5350 O O . VAL A 697 ? 0.1460 0.2189 0.2060 0.0082 -0.0146 -0.0132 690 VAL A O 5351 C CB . VAL A 697 ? 0.1447 0.1397 0.2009 -0.0166 -0.0110 -0.0055 690 VAL A CB 5352 C CG1 . VAL A 697 ? 0.1669 0.1714 0.2642 -0.0478 0.0043 0.0130 690 VAL A CG1 5353 C CG2 . VAL A 697 ? 0.1584 0.2008 0.2315 0.0408 -0.0324 -0.0165 690 VAL A CG2 5354 N N . ILE A 698 ? 0.1933 0.1777 0.1845 -0.0077 -0.0445 -0.0227 691 ILE A N 5355 C CA . ILE A 698 ? 0.1838 0.1857 0.1871 0.0078 -0.0368 -0.0376 691 ILE A CA 5356 C C . ILE A 698 ? 0.1656 0.1853 0.2022 0.0052 -0.0096 -0.0209 691 ILE A C 5357 O O . ILE A 698 ? 0.1868 0.1989 0.1909 -0.0096 0.0041 -0.0284 691 ILE A O 5358 C CB . ILE A 698 ? 0.1674 0.2041 0.1766 0.0103 -0.0251 -0.0379 691 ILE A CB 5359 C CG1 . ILE A 698 ? 0.2038 0.1503 0.2074 0.0240 -0.0262 -0.0075 691 ILE A CG1 5360 C CG2 . ILE A 698 ? 0.1833 0.2113 0.2451 -0.0078 -0.0598 -0.0260 691 ILE A CG2 5361 C CD1 . ILE A 698 ? 0.2224 0.1566 0.2341 0.0161 -0.0109 0.0006 691 ILE A CD1 5362 N N . TYR A 699 ? 0.2092 0.1739 0.2149 0.0042 -0.0216 -0.0355 692 TYR A N 5363 C CA . TYR A 699 ? 0.1884 0.1820 0.1924 0.0216 -0.0236 -0.0170 692 TYR A CA 5364 C C . TYR A 699 ? 0.2065 0.2245 0.2067 -0.0041 -0.0121 -0.0353 692 TYR A C 5365 O O . TYR A 699 ? 0.1963 0.2819 0.2384 0.0135 -0.0257 -0.0459 692 TYR A O 5366 C CB . TYR A 699 ? 0.1770 0.1943 0.2080 0.0142 -0.0327 -0.0077 692 TYR A CB 5367 C CG . TYR A 699 ? 0.1986 0.1924 0.2111 0.0192 -0.0288 -0.0290 692 TYR A CG 5368 C CD1 . TYR A 699 ? 0.2014 0.2466 0.2601 -0.0079 -0.0432 0.0009 692 TYR A CD1 5369 C CD2 . TYR A 699 ? 0.2350 0.2053 0.1938 -0.0154 -0.0463 -0.0291 692 TYR A CD2 5370 C CE1 . TYR A 699 ? 0.2465 0.1906 0.2446 -0.0095 -0.0441 -0.0145 692 TYR A CE1 5371 C CE2 . TYR A 699 ? 0.2233 0.1980 0.2001 -0.0151 -0.0611 -0.0106 692 TYR A CE2 5372 C CZ . TYR A 699 ? 0.2427 0.2454 0.2371 -0.0288 -0.0328 -0.0161 692 TYR A CZ 5373 O OH . TYR A 699 ? 0.2799 0.2328 0.2577 -0.0349 -0.0560 -0.0025 692 TYR A OH 5374 N N . ALA A 700 ? 0.2060 0.1951 0.1651 0.0005 -0.0336 -0.0157 693 ALA A N 5375 C CA . ALA A 700 ? 0.1667 0.1703 0.2009 0.0094 -0.0163 -0.0161 693 ALA A CA 5376 C C . ALA A 700 ? 0.1871 0.1801 0.2314 0.0132 0.0003 -0.0219 693 ALA A C 5377 O O . ALA A 700 ? 0.2050 0.1971 0.2206 -0.0164 -0.0031 -0.0331 693 ALA A O 5378 C CB . ALA A 700 ? 0.2054 0.1713 0.1976 -0.0130 -0.0164 0.0097 693 ALA A CB 5379 N N . PRO A 701 ? 0.1601 0.1909 0.2183 -0.0003 0.0068 -0.0234 694 PRO A N 5380 C CA . PRO A 701 ? 0.1981 0.1833 0.1949 -0.0023 0.0286 -0.0292 694 PRO A CA 5381 C C . PRO A 701 ? 0.1823 0.1899 0.2260 -0.0092 0.0197 -0.0132 694 PRO A C 5382 O O . PRO A 701 ? 0.1956 0.2466 0.1865 -0.0018 0.0079 -0.0232 694 PRO A O 5383 C CB . PRO A 701 ? 0.1948 0.2151 0.1942 -0.0225 0.0313 -0.0115 694 PRO A CB 5384 C CG . PRO A 701 ? 0.1864 0.1669 0.2270 0.0088 0.0379 -0.0469 694 PRO A CG 5385 C CD . PRO A 701 ? 0.1904 0.1560 0.2212 -0.0325 0.0016 -0.0282 694 PRO A CD 5386 N N . SER A 702 ? 0.1926 0.2056 0.2104 -0.0032 0.0409 -0.0408 695 SER A N 5387 C CA . SER A 702 ? 0.1866 0.2246 0.2203 -0.0101 0.0116 -0.0132 695 SER A CA 5388 C C . SER A 702 ? 0.1814 0.2057 0.2231 -0.0076 0.0211 -0.0152 695 SER A C 5389 O O . SER A 702 ? 0.2317 0.1978 0.2661 -0.0193 0.0217 -0.0191 695 SER A O 5390 C CB . SER A 702 ? 0.1941 0.2333 0.2203 0.0040 0.0358 -0.0189 695 SER A CB 5391 O OG . SER A 702 ? 0.2070 0.2415 0.2692 -0.0029 0.0720 -0.0235 695 SER A OG 5392 N N . SER A 703 ? 0.1897 0.2241 0.2178 -0.0112 0.0068 -0.0045 696 SER A N 5393 C CA . SER A 703 ? 0.2426 0.2078 0.2145 0.0323 -0.0034 -0.0314 696 SER A CA 5394 C C . SER A 703 ? 0.2036 0.2169 0.2021 -0.0148 0.0467 -0.0064 696 SER A C 5395 O O . SER A 703 ? 0.2739 0.2413 0.2175 0.0159 0.0181 -0.0339 696 SER A O 5396 C CB . SER A 703 ? 0.2127 0.2232 0.2195 0.0153 0.0370 0.0020 696 SER A CB 5397 O OG A SER A 703 ? 0.1945 0.1151 0.1608 -0.0062 0.0272 0.0047 696 SER A OG 5398 O OG B SER A 703 ? 0.2540 0.3700 0.3629 -0.0504 0.0393 -0.0087 696 SER A OG 5399 N N . HIS A 704 ? 0.1955 0.2235 0.2139 0.0168 0.0533 0.0095 697 HIS A N 5400 C CA . HIS A 704 ? 0.2054 0.2206 0.2305 0.0061 0.0704 0.0090 697 HIS A CA 5401 C C . HIS A 704 ? 0.2361 0.2251 0.2450 -0.0014 0.0600 0.0163 697 HIS A C 5402 O O . HIS A 704 ? 0.2898 0.2530 0.2622 0.0164 0.0607 0.0033 697 HIS A O 5403 C CB . HIS A 704 ? 0.2312 0.2458 0.2810 -0.0135 0.0777 0.0322 697 HIS A CB 5404 C CG . HIS A 704 ? 0.2600 0.2270 0.2825 0.0188 0.0764 0.0078 697 HIS A CG 5405 N ND1 . HIS A 704 ? 0.3391 0.2218 0.2810 0.0205 0.0571 0.0073 697 HIS A ND1 5406 C CD2 . HIS A 704 ? 0.2925 0.2284 0.3066 -0.0250 0.0870 -0.0031 697 HIS A CD2 5407 C CE1 . HIS A 704 ? 0.3558 0.2107 0.3133 0.0246 0.0759 -0.0101 697 HIS A CE1 5408 N NE2 . HIS A 704 ? 0.2889 0.2719 0.2713 -0.0329 0.1080 -0.0063 697 HIS A NE2 5409 N N . ASN A 705 ? 0.2209 0.2136 0.2152 0.0046 0.0357 0.0006 698 ASN A N 5410 C CA . ASN A 705 ? 0.2124 0.2330 0.2489 0.0038 0.0457 0.0194 698 ASN A CA 5411 C C . ASN A 705 ? 0.2036 0.2032 0.2309 -0.0076 0.0336 0.0007 698 ASN A C 5412 O O . ASN A 705 ? 0.1803 0.1965 0.2394 0.0044 0.0277 -0.0131 698 ASN A O 5413 C CB . ASN A 705 ? 0.2306 0.2431 0.2755 -0.0114 0.0236 -0.0118 698 ASN A CB 5414 C CG . ASN A 705 ? 0.2069 0.2495 0.2518 -0.0052 0.0196 -0.0236 698 ASN A CG 5415 O OD1 . ASN A 705 ? 0.2043 0.2449 0.2867 0.0113 0.0548 -0.0181 698 ASN A OD1 5416 N ND2 . ASN A 705 ? 0.2091 0.2758 0.2655 0.0173 0.0017 -0.0361 698 ASN A ND2 5417 N N . LYS A 706 ? 0.1827 0.2174 0.2457 -0.0007 0.0374 -0.0018 699 LYS A N 5418 C CA . LYS A 706 ? 0.2040 0.2278 0.2204 -0.0210 0.0274 -0.0235 699 LYS A CA 5419 C C . LYS A 706 ? 0.2062 0.2114 0.2346 -0.0131 0.0187 -0.0345 699 LYS A C 5420 O O . LYS A 706 ? 0.1827 0.2276 0.2131 -0.0076 0.0202 -0.0181 699 LYS A O 5421 C CB . LYS A 706 ? 0.1802 0.2727 0.2342 -0.0447 0.0318 -0.0196 699 LYS A CB 5422 C CG . LYS A 706 ? 0.1728 0.2820 0.2632 -0.0553 0.0405 -0.0486 699 LYS A CG 5423 C CD . LYS A 706 ? 0.1729 0.2379 0.2631 -0.0444 0.0420 -0.0268 699 LYS A CD 5424 C CE . LYS A 706 ? 0.1572 0.2094 0.2388 -0.0127 0.0224 -0.0233 699 LYS A CE 5425 N NZ . LYS A 706 ? 0.1856 0.1977 0.2739 -0.0151 0.0121 -0.0163 699 LYS A NZ 5426 N N . TYR A 707 ? 0.2021 0.2229 0.2471 -0.0058 0.0165 -0.0009 700 TYR A N 5427 C CA . TYR A 707 ? 0.2190 0.2024 0.2586 -0.0080 -0.0208 -0.0480 700 TYR A CA 5428 C C . TYR A 707 ? 0.2637 0.1987 0.2474 -0.0312 0.0013 -0.0317 700 TYR A C 5429 O O . TYR A 707 ? 0.2594 0.2369 0.2407 0.0091 0.0272 -0.0402 700 TYR A O 5430 C CB . TYR A 707 ? 0.2191 0.2062 0.2558 0.0036 0.0044 -0.0212 700 TYR A CB 5431 C CG . TYR A 707 ? 0.1729 0.1979 0.2338 0.0060 -0.0051 -0.0232 700 TYR A CG 5432 C CD1 . TYR A 707 ? 0.2256 0.2024 0.2424 -0.0133 0.0322 -0.0310 700 TYR A CD1 5433 C CD2 . TYR A 707 ? 0.2572 0.1835 0.2673 0.0224 0.0237 -0.0378 700 TYR A CD2 5434 C CE1 . TYR A 707 ? 0.2136 0.2035 0.2396 -0.0070 -0.0044 -0.0276 700 TYR A CE1 5435 C CE2 . TYR A 707 ? 0.1805 0.2142 0.2705 -0.0318 -0.0095 -0.0303 700 TYR A CE2 5436 C CZ . TYR A 707 ? 0.1800 0.2184 0.2320 -0.0041 -0.0111 -0.0145 700 TYR A CZ 5437 O OH . TYR A 707 ? 0.2267 0.2044 0.2655 0.0236 0.0208 -0.0269 700 TYR A OH 5438 N N . ALA A 708 ? 0.2173 0.1939 0.2821 -0.0149 0.0008 -0.0093 701 ALA A N 5439 C CA . ALA A 708 ? 0.2140 0.2041 0.2705 0.0054 0.0110 -0.0406 701 ALA A CA 5440 C C . ALA A 708 ? 0.2207 0.2221 0.2645 0.0201 0.0033 -0.0350 701 ALA A C 5441 O O . ALA A 708 ? 0.2326 0.2416 0.2600 0.0234 -0.0067 -0.0240 701 ALA A O 5442 C CB . ALA A 708 ? 0.2172 0.2333 0.3034 -0.0051 0.0363 -0.0364 701 ALA A CB 5443 N N . GLY A 709 ? 0.2392 0.2005 0.2479 0.0304 0.0119 -0.0248 702 GLY A N 5444 C CA . GLY A 709 ? 0.2431 0.1875 0.2502 0.0231 0.0225 0.0032 702 GLY A CA 5445 C C . GLY A 709 ? 0.1850 0.2087 0.2677 -0.0051 -0.0065 -0.0023 702 GLY A C 5446 O O . GLY A 709 ? 0.1825 0.2438 0.3326 0.0024 -0.0086 0.0045 702 GLY A O 5447 N N . GLU A 710 ? 0.1787 0.1769 0.2545 -0.0173 -0.0042 -0.0073 703 GLU A N 5448 C CA . GLU A 710 ? 0.1982 0.1762 0.2331 -0.0087 0.0057 -0.0159 703 GLU A CA 5449 C C . GLU A 710 ? 0.1657 0.1912 0.2528 -0.0077 0.0112 -0.0205 703 GLU A C 5450 O O . GLU A 710 ? 0.1754 0.2007 0.2581 -0.0098 0.0208 -0.0532 703 GLU A O 5451 C CB . GLU A 710 ? 0.1864 0.2235 0.2328 -0.0323 0.0377 0.0168 703 GLU A CB 5452 C CG . GLU A 710 ? 0.1966 0.2009 0.2580 -0.0419 0.0293 0.0082 703 GLU A CG 5453 C CD . GLU A 710 ? 0.1979 0.2413 0.2911 -0.0034 0.0343 -0.0158 703 GLU A CD 5454 O OE1 . GLU A 710 ? 0.2747 0.2110 0.2740 0.0056 0.0298 -0.0004 703 GLU A OE1 5455 O OE2 . GLU A 710 ? 0.1804 0.2773 0.3408 -0.0311 0.0431 -0.0370 703 GLU A OE2 5456 N N . SER A 711 ? 0.1972 0.2026 0.2067 -0.0082 -0.0205 -0.0400 704 SER A N 5457 C CA . SER A 711 ? 0.1673 0.1810 0.2279 0.0082 -0.0461 -0.0332 704 SER A CA 5458 C C . SER A 711 ? 0.1669 0.1909 0.2237 -0.0084 -0.0224 -0.0160 704 SER A C 5459 O O . SER A 711 ? 0.1848 0.1966 0.2390 0.0177 -0.0109 -0.0300 704 SER A O 5460 C CB . SER A 711 ? 0.1309 0.2302 0.2378 -0.0318 -0.0243 -0.0219 704 SER A CB 5461 O OG . SER A 711 ? 0.1634 0.2567 0.2891 -0.0325 0.0129 -0.0175 704 SER A OG 5462 N N . PHE A 712 ? 0.1624 0.1900 0.2253 -0.0040 -0.0371 -0.0115 705 PHE A N 5463 C CA . PHE A 712 ? 0.2163 0.1541 0.2174 -0.0127 -0.0289 -0.0103 705 PHE A CA 5464 C C . PHE A 712 ? 0.1923 0.1865 0.2072 -0.0157 -0.0111 -0.0027 705 PHE A C 5465 O O . PHE A 712 ? 0.1413 0.1901 0.2073 -0.0278 -0.0143 0.0035 705 PHE A O 5466 C CB . PHE A 712 ? 0.2007 0.1493 0.2096 -0.0096 -0.0141 -0.0267 705 PHE A CB 5467 C CG . PHE A 712 ? 0.1638 0.1608 0.1956 -0.0086 -0.0175 -0.0174 705 PHE A CG 5468 C CD1 . PHE A 712 ? 0.1892 0.1658 0.2347 0.0252 -0.0063 -0.0178 705 PHE A CD1 5469 C CD2 . PHE A 712 ? 0.1900 0.1507 0.2057 0.0009 -0.0502 -0.0149 705 PHE A CD2 5470 C CE1 . PHE A 712 ? 0.2026 0.1817 0.2435 0.0176 -0.0208 -0.0182 705 PHE A CE1 5471 C CE2 . PHE A 712 ? 0.1919 0.1931 0.2163 0.0229 -0.0247 -0.0364 705 PHE A CE2 5472 C CZ . PHE A 712 ? 0.1798 0.1780 0.2893 0.0184 -0.0285 -0.0020 705 PHE A CZ 5473 N N . PRO A 713 ? 0.1778 0.1761 0.2083 -0.0073 -0.0074 -0.0233 706 PRO A N 5474 C CA . PRO A 713 ? 0.1790 0.1638 0.1923 -0.0263 -0.0210 -0.0111 706 PRO A CA 5475 C C . PRO A 713 ? 0.1984 0.1684 0.2001 -0.0086 0.0046 0.0026 706 PRO A C 5476 O O . PRO A 713 ? 0.2132 0.2009 0.2116 0.0046 0.0162 -0.0015 706 PRO A O 5477 C CB . PRO A 713 ? 0.1695 0.1950 0.1824 -0.0400 0.0133 -0.0096 706 PRO A CB 5478 C CG . PRO A 713 ? 0.1758 0.2085 0.1868 -0.0422 -0.0059 -0.0452 706 PRO A CG 5479 C CD . PRO A 713 ? 0.1556 0.1942 0.2003 -0.0296 -0.0223 -0.0173 706 PRO A CD 5480 N N . GLY A 714 ? 0.1796 0.1711 0.2123 -0.0106 -0.0194 -0.0102 707 GLY A N 5481 C CA . GLY A 714 ? 0.2072 0.1913 0.2336 0.0056 0.0081 0.0239 707 GLY A CA 5482 C C . GLY A 714 ? 0.2102 0.1754 0.2199 -0.0230 -0.0106 0.0015 707 GLY A C 5483 O O . GLY A 714 ? 0.1927 0.2041 0.2130 -0.0191 0.0396 -0.0041 707 GLY A O 5484 N N . ILE A 715 ? 0.1749 0.1732 0.2210 -0.0286 -0.0046 0.0049 708 ILE A N 5485 C CA . ILE A 715 ? 0.1927 0.1571 0.2184 -0.0477 0.0033 -0.0200 708 ILE A CA 5486 C C . ILE A 715 ? 0.1956 0.1917 0.2192 -0.0368 0.0062 -0.0030 708 ILE A C 5487 O O . ILE A 715 ? 0.2368 0.2008 0.2160 -0.0297 0.0216 -0.0045 708 ILE A O 5488 C CB . ILE A 715 ? 0.1589 0.1731 0.2089 -0.0419 0.0079 -0.0202 708 ILE A CB 5489 C CG1 . ILE A 715 ? 0.2149 0.2150 0.2025 -0.0247 -0.0036 -0.0574 708 ILE A CG1 5490 C CG2 . ILE A 715 ? 0.2351 0.1569 0.2534 -0.0621 -0.0037 0.0032 708 ILE A CG2 5491 C CD1 . ILE A 715 ? 0.1950 0.1978 0.2279 -0.0364 -0.0069 -0.0630 708 ILE A CD1 5492 N N . TYR A 716 ? 0.2177 0.1794 0.2163 -0.0208 0.0079 -0.0192 709 TYR A N 5493 C CA . TYR A 716 ? 0.1925 0.1771 0.2377 -0.0144 -0.0001 -0.0117 709 TYR A CA 5494 C C . TYR A 716 ? 0.2056 0.1960 0.2312 -0.0248 0.0150 -0.0111 709 TYR A C 5495 O O . TYR A 716 ? 0.2305 0.1954 0.2161 -0.0182 0.0041 -0.0135 709 TYR A O 5496 C CB . TYR A 716 ? 0.2149 0.1833 0.2438 0.0029 0.0257 -0.0079 709 TYR A CB 5497 C CG . TYR A 716 ? 0.1894 0.1880 0.2274 -0.0172 0.0323 -0.0101 709 TYR A CG 5498 C CD1 . TYR A 716 ? 0.1795 0.2051 0.2792 0.0063 0.0437 -0.0041 709 TYR A CD1 5499 C CD2 . TYR A 716 ? 0.2233 0.1601 0.2415 -0.0124 0.0470 -0.0144 709 TYR A CD2 5500 C CE1 . TYR A 716 ? 0.2272 0.2000 0.2562 0.0040 0.0687 -0.0113 709 TYR A CE1 5501 C CE2 . TYR A 716 ? 0.2154 0.2159 0.2850 0.0174 0.0622 -0.0009 709 TYR A CE2 5502 C CZ . TYR A 716 ? 0.2299 0.2045 0.3126 0.0072 0.0428 -0.0295 709 TYR A CZ 5503 O OH . TYR A 716 ? 0.2126 0.2534 0.3288 0.0191 0.0588 -0.0026 709 TYR A OH 5504 N N . ASP A 717 ? 0.1953 0.2060 0.2209 -0.0223 0.0026 0.0033 710 ASP A N 5505 C CA . ASP A 717 ? 0.2015 0.1991 0.2068 -0.0204 0.0273 -0.0023 710 ASP A CA 5506 C C . ASP A 717 ? 0.2188 0.2097 0.2077 0.0032 0.0328 0.0008 710 ASP A C 5507 O O . ASP A 717 ? 0.2379 0.2297 0.1998 -0.0181 0.0396 0.0088 710 ASP A O 5508 C CB . ASP A 717 ? 0.2223 0.1819 0.2432 -0.0345 0.0140 0.0184 710 ASP A CB 5509 C CG . ASP A 717 ? 0.2143 0.1984 0.2445 -0.0183 0.0469 0.0274 710 ASP A CG 5510 O OD1 . ASP A 717 ? 0.2379 0.2250 0.2651 0.0029 0.0043 -0.0045 710 ASP A OD1 5511 O OD2 . ASP A 717 ? 0.2228 0.2083 0.3143 -0.0367 0.0524 0.0137 710 ASP A OD2 5512 N N . ALA A 718 ? 0.2295 0.1792 0.2266 -0.0308 0.0070 -0.0130 711 ALA A N 5513 C CA . ALA A 718 ? 0.2202 0.1983 0.2168 -0.0055 0.0280 -0.0066 711 ALA A CA 5514 C C . ALA A 718 ? 0.2349 0.2301 0.2483 -0.0281 0.0303 0.0217 711 ALA A C 5515 O O . ALA A 718 ? 0.2473 0.2163 0.2415 -0.0463 0.0317 0.0199 711 ALA A O 5516 C CB . ALA A 718 ? 0.2162 0.1958 0.2731 0.0100 0.0309 -0.0114 711 ALA A CB 5517 N N . LEU A 719 ? 0.2299 0.1948 0.2701 -0.0267 0.0270 -0.0034 712 LEU A N 5518 C CA . LEU A 719 ? 0.2261 0.1877 0.2574 -0.0313 0.0361 -0.0201 712 LEU A CA 5519 C C . LEU A 719 ? 0.2170 0.1947 0.2826 -0.0247 0.0551 -0.0137 712 LEU A C 5520 O O . LEU A 719 ? 0.2762 0.2394 0.2596 -0.0236 0.0605 0.0062 712 LEU A O 5521 C CB . LEU A 719 ? 0.2151 0.1741 0.2650 -0.0235 0.0331 -0.0224 712 LEU A CB 5522 C CG . LEU A 719 ? 0.2353 0.1611 0.2321 -0.0366 0.0294 -0.0133 712 LEU A CG 5523 C CD1 . LEU A 719 ? 0.2446 0.2646 0.2830 -0.0536 -0.0127 -0.0451 712 LEU A CD1 5524 C CD2 . LEU A 719 ? 0.2581 0.1795 0.2764 -0.0334 0.0347 0.0177 712 LEU A CD2 5525 N N . PHE A 720 ? 0.2377 0.1835 0.3053 -0.0124 0.0336 -0.0115 713 PHE A N 5526 C CA . PHE A 720 ? 0.2531 0.1778 0.2950 -0.0383 0.0822 0.0075 713 PHE A CA 5527 C C . PHE A 720 ? 0.2721 0.2258 0.2955 -0.0393 0.0598 -0.0107 713 PHE A C 5528 O O . PHE A 720 ? 0.2761 0.2543 0.2931 -0.0210 0.0480 -0.0167 713 PHE A O 5529 C CB . PHE A 720 ? 0.2560 0.1732 0.3500 -0.0271 0.1009 0.0241 713 PHE A CB 5530 C CG . PHE A 720 ? 0.2812 0.2195 0.3113 0.0101 0.0760 -0.0125 713 PHE A CG 5531 C CD1 . PHE A 720 ? 0.2757 0.2357 0.3218 0.0016 0.0746 -0.0058 713 PHE A CD1 5532 C CD2 . PHE A 720 ? 0.2874 0.1653 0.3397 -0.0287 0.0785 -0.0209 713 PHE A CD2 5533 C CE1 . PHE A 720 ? 0.2907 0.2432 0.3421 0.0382 0.0302 0.0025 713 PHE A CE1 5534 C CE2 . PHE A 720 ? 0.2913 0.2230 0.3244 0.0365 0.0715 0.0117 713 PHE A CE2 5535 C CZ . PHE A 720 ? 0.2357 0.2487 0.3347 -0.0345 0.0793 -0.0060 713 PHE A CZ 5536 N N . ASP A 721 ? 0.2955 0.2484 0.2931 -0.0206 0.0798 -0.0232 714 ASP A N 5537 C CA . ASP A 721 ? 0.3020 0.2304 0.2887 -0.0273 0.0658 -0.0069 714 ASP A CA 5538 C C . ASP A 721 ? 0.2992 0.2564 0.3036 -0.0069 0.0860 0.0029 714 ASP A C 5539 O O . ASP A 721 ? 0.3327 0.2888 0.3104 -0.0028 0.0769 -0.0097 714 ASP A O 5540 C CB . ASP A 721 ? 0.2728 0.2323 0.3164 -0.0227 0.0851 -0.0375 714 ASP A CB 5541 C CG . ASP A 721 ? 0.3295 0.3108 0.3189 -0.0459 0.0905 -0.0234 714 ASP A CG 5542 O OD1 . ASP A 721 ? 0.3419 0.3214 0.3509 -0.0374 0.1340 -0.0474 714 ASP A OD1 5543 O OD2 . ASP A 721 ? 0.3724 0.3265 0.2740 -0.0049 0.0672 -0.0300 714 ASP A OD2 5544 N N . ILE A 722 ? 0.3308 0.2231 0.3163 -0.0096 0.0522 0.0159 715 ILE A N 5545 C CA . ILE A 722 ? 0.3236 0.2363 0.2958 0.0173 0.0652 0.0097 715 ILE A CA 5546 C C . ILE A 722 ? 0.3562 0.2658 0.3215 -0.0038 0.0782 0.0168 715 ILE A C 5547 O O . ILE A 722 ? 0.3964 0.2814 0.2851 -0.0055 0.1056 0.0475 715 ILE A O 5548 C CB . ILE A 722 ? 0.2974 0.2278 0.2996 0.0418 0.0568 0.0068 715 ILE A CB 5549 C CG1 . ILE A 722 ? 0.2584 0.2256 0.2546 0.0226 0.0822 0.0072 715 ILE A CG1 5550 C CG2 . ILE A 722 ? 0.3050 0.2544 0.3178 -0.0040 0.0894 0.0129 715 ILE A CG2 5551 C CD1 . ILE A 722 ? 0.3185 0.2739 0.2202 0.0050 0.0692 -0.0101 715 ILE A CD1 5552 N N . GLU A 723 ? 0.3705 0.3151 0.3187 -0.0291 0.1322 0.0120 716 GLU A N 5553 C CA . GLU A 723 ? 0.3799 0.3545 0.3712 -0.0342 0.1287 0.0599 716 GLU A CA 5554 C C . GLU A 723 ? 0.4891 0.3820 0.3518 -0.0255 0.1013 0.0694 716 GLU A C 5555 O O . GLU A 723 ? 0.5522 0.3634 0.3782 0.0525 0.1215 0.1023 716 GLU A O 5556 C CB . GLU A 723 ? 0.3758 0.3851 0.4616 -0.0045 0.1169 0.0400 716 GLU A CB 5557 C CG . GLU A 723 ? 0.3900 0.4195 0.4377 0.0106 0.1422 0.0516 716 GLU A CG 5558 C CD . GLU A 723 ? 0.4263 0.4407 0.4536 0.0022 0.1356 0.0659 716 GLU A CD 5559 O OE1 . GLU A 723 ? 0.3522 0.3396 0.4361 -0.0601 0.1148 0.0560 716 GLU A OE1 5560 O OE2 . GLU A 723 ? 0.4679 0.4930 0.5102 0.0223 0.0757 0.0031 716 GLU A OE2 5561 N N . SER A 724 ? 0.4425 0.3473 0.3700 0.0176 0.1208 0.0592 717 SER A N 5562 C CA . SER A 724 ? 0.4882 0.3648 0.4510 0.0159 0.0532 0.0466 717 SER A CA 5563 C C . SER A 724 ? 0.4694 0.3590 0.3541 -0.0196 0.0906 0.0291 717 SER A C 5564 O O . SER A 724 ? 0.5987 0.4072 0.3970 0.0021 0.0783 -0.0938 717 SER A O 5565 C CB . SER A 724 ? 0.5150 0.3690 0.3958 0.0595 0.0636 0.0233 717 SER A CB 5566 O OG . SER A 724 ? 0.4883 0.3715 0.3937 0.0124 0.1732 0.0479 717 SER A OG 5567 N N . LYS A 725 ? 0.4924 0.4260 0.3430 0.0268 0.1241 0.0405 718 LYS A N 5568 C CA . LYS A 725 ? 0.4750 0.3747 0.3347 0.0188 0.1054 0.0054 718 LYS A CA 5569 C C . LYS A 725 ? 0.5402 0.4491 0.3870 -0.0049 0.0713 0.0533 718 LYS A C 5570 O O . LYS A 725 ? 0.5255 0.4497 0.3916 -0.0040 0.0358 0.0927 718 LYS A O 5571 C CB . LYS A 725 ? 0.3915 0.3528 0.3004 0.0116 0.0985 0.0516 718 LYS A CB 5572 C CG . LYS A 725 ? 0.4828 0.3742 0.3574 -0.0881 0.0815 0.0883 718 LYS A CG 5573 C CD . LYS A 725 ? 0.5884 0.4402 0.3865 -0.1149 -0.0704 0.0705 718 LYS A CD 5574 C CE . LYS A 725 ? 0.6399 0.4731 0.3921 -0.1652 0.0772 0.0997 718 LYS A CE 5575 N NZ . LYS A 725 ? 0.5669 0.4972 0.4454 -0.1273 0.0166 0.0091 718 LYS A NZ 5576 N N . VAL A 726 ? 0.5840 0.4216 0.3969 0.0347 0.0192 0.0409 719 VAL A N 5577 C CA . VAL A 726 ? 0.5997 0.4254 0.4339 0.0457 -0.0158 0.0509 719 VAL A CA 5578 C C . VAL A 726 ? 0.5742 0.4055 0.4282 -0.0266 0.0776 0.0506 719 VAL A C 5579 O O . VAL A 726 ? 0.6179 0.4401 0.3274 0.0277 0.1512 0.0296 719 VAL A O 5580 C CB . VAL A 726 ? 0.7412 0.4648 0.4301 0.0235 -0.0513 -0.0154 719 VAL A CB 5581 C CG1 . VAL A 726 ? 0.7607 0.4636 0.5460 0.0636 -0.0617 -0.0003 719 VAL A CG1 5582 C CG2 . VAL A 726 ? 0.8327 0.4770 0.4707 0.0372 -0.0653 -0.0332 719 VAL A CG2 5583 N N . ASP A 727 ? 0.5560 0.4378 0.3928 -0.0135 0.0289 -0.0219 720 ASP A N 5584 C CA . ASP A 727 ? 0.5077 0.4354 0.4151 -0.0134 0.0321 -0.0098 720 ASP A CA 5585 C C . ASP A 727 ? 0.4898 0.3972 0.3516 -0.0435 0.0824 0.0334 720 ASP A C 5586 O O . ASP A 727 ? 0.4388 0.3620 0.3100 -0.0651 0.0352 0.0029 720 ASP A O 5587 C CB . ASP A 727 ? 0.5025 0.4569 0.2945 0.0025 0.0291 0.0134 720 ASP A CB 5588 C CG . ASP A 727 ? 0.5074 0.4526 0.4098 -0.0144 0.0470 0.0382 720 ASP A CG 5589 O OD1 . ASP A 727 ? 0.5062 0.4758 0.3175 -0.0051 -0.0485 0.0497 720 ASP A OD1 5590 O OD2 . ASP A 727 ? 0.5445 0.7110 0.4499 -0.0439 -0.0801 0.0083 720 ASP A OD2 5591 N N . PRO A 728 ? 0.4838 0.3636 0.3385 -0.0270 0.0662 0.0475 721 PRO A N 5592 C CA . PRO A 728 ? 0.4314 0.3382 0.3891 -0.0086 0.0479 0.0374 721 PRO A CA 5593 C C . PRO A 728 ? 0.3647 0.3260 0.3467 -0.0394 0.0455 0.0640 721 PRO A C 5594 O O . PRO A 728 ? 0.3706 0.3462 0.3359 -0.0214 0.0505 0.0720 721 PRO A O 5595 C CB . PRO A 728 ? 0.4184 0.4045 0.3729 -0.0101 0.0598 0.0617 721 PRO A CB 5596 C CG . PRO A 728 ? 0.4975 0.4446 0.3974 -0.0767 0.0531 0.0846 721 PRO A CG 5597 C CD . PRO A 728 ? 0.4871 0.3915 0.4285 -0.0643 0.1001 0.0519 721 PRO A CD 5598 N N . SER A 729 ? 0.3995 0.3226 0.3301 0.0072 0.0378 0.0257 722 SER A N 5599 C CA . SER A 729 ? 0.3991 0.3252 0.3383 0.0277 0.0554 0.0759 722 SER A CA 5600 C C . SER A 729 ? 0.3841 0.3116 0.3241 0.0079 0.0498 0.0291 722 SER A C 5601 O O . SER A 729 ? 0.3862 0.2811 0.3000 -0.0288 0.0023 0.0360 722 SER A O 5602 C CB . SER A 729 ? 0.4599 0.3363 0.3847 0.0887 0.0615 0.0855 722 SER A CB 5603 O OG . SER A 729 ? 0.5361 0.3717 0.4361 0.0938 0.0323 0.0563 722 SER A OG 5604 N N . LYS A 730 ? 0.3740 0.2708 0.3085 -0.0030 0.0209 0.0683 723 LYS A N 5605 C CA . LYS A 730 ? 0.3640 0.3016 0.3137 -0.0390 0.0031 0.0416 723 LYS A CA 5606 C C . LYS A 730 ? 0.3282 0.3075 0.2999 -0.0193 0.0123 0.0088 723 LYS A C 5607 O O . LYS A 730 ? 0.2708 0.3004 0.2834 -0.0277 0.0014 0.0174 723 LYS A O 5608 C CB . LYS A 730 ? 0.4201 0.3887 0.2800 -0.0580 0.0090 -0.0059 723 LYS A CB 5609 C CG . LYS A 730 ? 0.4087 0.4934 0.4109 -0.0903 -0.0346 0.0404 723 LYS A CG 5610 C CD . LYS A 730 ? 0.5566 0.5400 0.5050 -0.1271 -0.0188 -0.0621 723 LYS A CD 5611 C CE . LYS A 730 ? 0.5780 0.5446 0.5747 -0.1275 -0.0654 -0.0039 723 LYS A CE 5612 N NZ . LYS A 730 ? 0.7326 0.4435 0.6011 -0.0878 -0.0582 -0.0223 723 LYS A NZ 5613 N N . ALA A 731 ? 0.2750 0.2896 0.2858 -0.0517 0.0159 0.0160 724 ALA A N 5614 C CA . ALA A 731 ? 0.2745 0.2560 0.2796 -0.0200 0.0363 -0.0067 724 ALA A CA 5615 C C . ALA A 731 ? 0.2960 0.2273 0.2604 -0.0139 0.0522 0.0043 724 ALA A C 5616 O O . ALA A 731 ? 0.2735 0.2374 0.2645 -0.0228 0.0308 0.0159 724 ALA A O 5617 C CB . ALA A 731 ? 0.2994 0.2578 0.2498 -0.0071 0.0500 -0.0281 724 ALA A CB 5618 N N . TRP A 732 ? 0.2757 0.2368 0.2805 -0.0232 0.0353 -0.0063 725 TRP A N 5619 C CA . TRP A 732 ? 0.2479 0.2033 0.2994 -0.0431 0.0454 0.0103 725 TRP A CA 5620 C C . TRP A 732 ? 0.2612 0.2483 0.2596 -0.0239 0.0303 0.0101 725 TRP A C 5621 O O . TRP A 732 ? 0.2296 0.2209 0.2329 0.0099 0.0304 0.0414 725 TRP A O 5622 C CB . TRP A 732 ? 0.2245 0.2263 0.2719 -0.0252 0.0608 0.0450 725 TRP A CB 5623 C CG . TRP A 732 ? 0.2338 0.2245 0.2953 -0.0257 0.0567 0.0219 725 TRP A CG 5624 C CD1 . TRP A 732 ? 0.2312 0.2400 0.2974 -0.0310 0.0495 -0.0012 725 TRP A CD1 5625 C CD2 . TRP A 732 ? 0.2742 0.1928 0.3128 -0.0238 0.0329 0.0369 725 TRP A CD2 5626 N NE1 . TRP A 732 ? 0.2522 0.2454 0.3369 -0.0238 0.0084 0.0126 725 TRP A NE1 5627 C CE2 . TRP A 732 ? 0.2628 0.2208 0.3201 -0.0224 0.0540 0.0637 725 TRP A CE2 5628 C CE3 . TRP A 732 ? 0.2928 0.1581 0.3157 -0.0541 0.0303 0.0522 725 TRP A CE3 5629 C CZ2 . TRP A 732 ? 0.2975 0.2090 0.3357 -0.0275 0.0055 0.0382 725 TRP A CZ2 5630 C CZ3 . TRP A 732 ? 0.2525 0.2258 0.3524 -0.0071 0.0436 0.0114 725 TRP A CZ3 5631 C CH2 . TRP A 732 ? 0.2801 0.2460 0.3183 -0.0236 0.0752 0.0465 725 TRP A CH2 5632 N N . GLY A 733 ? 0.2658 0.2434 0.2544 0.0055 0.0119 0.0029 726 GLY A N 5633 C CA . GLY A 733 ? 0.2697 0.2357 0.2554 -0.0224 0.0339 0.0021 726 GLY A CA 5634 C C . GLY A 733 ? 0.2220 0.2337 0.2498 -0.0247 0.0019 0.0053 726 GLY A C 5635 O O . GLY A 733 ? 0.2249 0.2345 0.2396 -0.0079 -0.0118 0.0342 726 GLY A O 5636 N N . GLU A 734 ? 0.2350 0.2174 0.2482 -0.0110 0.0016 0.0381 727 GLU A N 5637 C CA . GLU A 734 ? 0.2446 0.1880 0.2510 -0.0137 0.0072 0.0150 727 GLU A CA 5638 C C . GLU A 734 ? 0.2147 0.2201 0.2431 -0.0250 0.0304 0.0212 727 GLU A C 5639 O O . GLU A 734 ? 0.2249 0.2090 0.2344 -0.0439 0.0487 0.0012 727 GLU A O 5640 C CB . GLU A 734 ? 0.2801 0.1961 0.2647 -0.0403 0.0325 0.0097 727 GLU A CB 5641 C CG A GLU A 734 ? 0.2969 0.2031 0.2706 -0.0250 0.0196 0.0240 727 GLU A CG 5642 C CD A GLU A 734 ? 0.2780 0.2520 0.3105 -0.0164 0.0095 0.0131 727 GLU A CD 5643 O OE1 A GLU A 734 ? 0.2946 0.2526 0.3539 -0.0072 -0.0107 0.0075 727 GLU A OE1 5644 O OE2 A GLU A 734 ? 0.2702 0.3144 0.2906 -0.0671 -0.0288 0.0272 727 GLU A OE2 5645 N N . VAL A 735 ? 0.1961 0.1793 0.2577 -0.0192 0.0125 -0.0098 728 VAL A N 5646 C CA . VAL A 735 ? 0.1901 0.2070 0.2473 -0.0211 0.0282 -0.0053 728 VAL A CA 5647 C C . VAL A 735 ? 0.1917 0.1778 0.2388 -0.0358 0.0004 0.0043 728 VAL A C 5648 O O . VAL A 735 ? 0.1939 0.2062 0.2368 -0.0355 0.0145 0.0197 728 VAL A O 5649 C CB . VAL A 735 ? 0.1667 0.2092 0.2630 0.0010 0.0185 -0.0100 728 VAL A CB 5650 C CG1 . VAL A 735 ? 0.2067 0.2437 0.2818 -0.0242 0.0046 -0.0102 728 VAL A CG1 5651 C CG2 . VAL A 735 ? 0.2592 0.1549 0.2768 -0.0143 0.0203 0.0044 728 VAL A CG2 5652 N N A LYS A 736 ? 0.1903 0.1732 0.2592 -0.0265 0.0176 0.0050 729 LYS A N 5653 N N B LYS A 736 ? 0.1903 0.1769 0.2616 -0.0255 0.0199 0.0090 729 LYS A N 5654 C CA A LYS A 736 ? 0.2083 0.1666 0.2439 -0.0195 0.0221 0.0220 729 LYS A CA 5655 C CA B LYS A 736 ? 0.2069 0.1778 0.2463 -0.0212 0.0207 0.0201 729 LYS A CA 5656 C C A LYS A 736 ? 0.2045 0.1906 0.2412 -0.0443 0.0091 -0.0018 729 LYS A C 5657 C C B LYS A 736 ? 0.2015 0.1992 0.2377 -0.0480 0.0016 0.0043 729 LYS A C 5658 O O A LYS A 736 ? 0.1920 0.1890 0.2209 -0.0262 0.0016 0.0182 729 LYS A O 5659 O O B LYS A 736 ? 0.1723 0.2062 0.2214 -0.0373 -0.0310 0.0301 729 LYS A O 5660 C CB A LYS A 736 ? 0.1905 0.1696 0.2526 -0.0408 0.0268 0.0366 729 LYS A CB 5661 C CB B LYS A 736 ? 0.1960 0.1806 0.2532 -0.0475 0.0279 0.0391 729 LYS A CB 5662 C CG A LYS A 736 ? 0.1903 0.1570 0.2565 -0.0409 0.0233 0.0494 729 LYS A CG 5663 C CG B LYS A 736 ? 0.1860 0.2074 0.2751 -0.0579 0.0202 0.0406 729 LYS A CG 5664 C CD A LYS A 736 ? 0.1854 0.1621 0.2626 -0.0064 -0.0202 0.0434 729 LYS A CD 5665 C CD B LYS A 736 ? 0.2129 0.2236 0.3037 -0.0461 0.0046 0.0567 729 LYS A CD 5666 C CE A LYS A 736 ? 0.1918 0.1444 0.3028 -0.0237 0.0210 0.0479 729 LYS A CE 5667 C CE B LYS A 736 ? 0.2659 0.2815 0.3145 -0.0482 -0.0167 0.0549 729 LYS A CE 5668 N NZ A LYS A 736 ? 0.2060 0.1864 0.3451 -0.0019 -0.0326 0.0900 729 LYS A NZ 5669 N NZ B LYS A 736 ? 0.3033 0.3033 0.3987 -0.0514 0.0894 0.0797 729 LYS A NZ 5670 N N . ARG A 737 ? 0.1743 0.1683 0.2350 -0.0200 -0.0148 0.0214 730 ARG A N 5671 C CA . ARG A 737 ? 0.1938 0.1864 0.2257 -0.0582 -0.0229 0.0159 730 ARG A CA 5672 C C . ARG A 737 ? 0.1943 0.1798 0.2140 -0.0374 -0.0192 -0.0075 730 ARG A C 5673 O O . ARG A 737 ? 0.2042 0.1789 0.2082 -0.0167 -0.0088 -0.0107 730 ARG A O 5674 C CB . ARG A 737 ? 0.1668 0.2208 0.2107 -0.0598 0.0071 -0.0113 730 ARG A CB 5675 C CG . ARG A 737 ? 0.1797 0.2316 0.2228 -0.0652 0.0177 -0.0083 730 ARG A CG 5676 C CD . ARG A 737 ? 0.2481 0.2388 0.2866 -0.0767 -0.0214 -0.0303 730 ARG A CD 5677 N NE . ARG A 737 ? 0.2244 0.2426 0.2538 -0.0284 -0.0031 0.0069 730 ARG A NE 5678 C CZ . ARG A 737 ? 0.2949 0.2609 0.2913 -0.0357 -0.0062 0.0336 730 ARG A CZ 5679 N NH1 . ARG A 737 ? 0.2305 0.3155 0.3345 -0.0328 -0.0040 0.0243 730 ARG A NH1 5680 N NH2 . ARG A 737 ? 0.3073 0.2629 0.3205 -0.0220 -0.0035 0.0215 730 ARG A NH2 5681 N N . GLN A 738 ? 0.1936 0.1759 0.2279 -0.0229 -0.0324 0.0042 731 GLN A N 5682 C CA . GLN A 738 ? 0.2097 0.1561 0.1989 -0.0061 -0.0236 -0.0167 731 GLN A CA 5683 C C . GLN A 738 ? 0.1861 0.1746 0.2162 -0.0270 -0.0212 -0.0091 731 GLN A C 5684 O O . GLN A 738 ? 0.2018 0.2045 0.2106 -0.0178 -0.0089 0.0004 731 GLN A O 5685 C CB . GLN A 738 ? 0.1951 0.1709 0.2016 -0.0232 -0.0153 -0.0388 731 GLN A CB 5686 C CG . GLN A 738 ? 0.1484 0.1666 0.2050 -0.0230 -0.0332 -0.0016 731 GLN A CG 5687 C CD . GLN A 738 ? 0.1972 0.2199 0.2352 -0.0281 0.0022 0.0183 731 GLN A CD 5688 O OE1 . GLN A 738 ? 0.2443 0.2100 0.2420 -0.0362 0.0067 0.0066 731 GLN A OE1 5689 N NE2 . GLN A 738 ? 0.1995 0.2885 0.2678 -0.0266 -0.0083 0.0049 731 GLN A NE2 5690 N N . ILE A 739 ? 0.1966 0.1767 0.2454 -0.0421 -0.0245 -0.0204 732 ILE A N 5691 C CA . ILE A 739 ? 0.1711 0.1730 0.2343 -0.0416 -0.0099 -0.0225 732 ILE A CA 5692 C C . ILE A 739 ? 0.1739 0.1937 0.2299 -0.0309 -0.0021 0.0120 732 ILE A C 5693 O O . ILE A 739 ? 0.1954 0.2251 0.2298 -0.0350 -0.0195 -0.0066 732 ILE A O 5694 C CB . ILE A 739 ? 0.1823 0.1771 0.2123 -0.0445 0.0061 -0.0206 732 ILE A CB 5695 C CG1 . ILE A 739 ? 0.1494 0.1792 0.2501 -0.0462 0.0098 -0.0031 732 ILE A CG1 5696 C CG2 . ILE A 739 ? 0.1724 0.2161 0.2243 -0.0505 0.0044 -0.0405 732 ILE A CG2 5697 C CD1 . ILE A 739 ? 0.2041 0.2155 0.2555 -0.0731 0.0066 0.0227 732 ILE A CD1 5698 N N . TYR A 740 ? 0.1521 0.2036 0.2439 -0.0243 -0.0236 -0.0143 733 TYR A N 5699 C CA . TYR A 740 ? 0.1784 0.2211 0.2185 -0.0178 -0.0006 0.0099 733 TYR A CA 5700 C C . TYR A 740 ? 0.2099 0.1786 0.2229 -0.0327 -0.0247 0.0000 733 TYR A C 5701 O O . TYR A 740 ? 0.1687 0.1957 0.2249 -0.0213 0.0118 -0.0063 733 TYR A O 5702 C CB . TYR A 740 ? 0.2012 0.1949 0.2412 0.0281 0.0069 0.0193 733 TYR A CB 5703 C CG . TYR A 740 ? 0.2125 0.2231 0.2793 0.0142 0.0045 -0.0063 733 TYR A CG 5704 C CD1 . TYR A 740 ? 0.2664 0.2693 0.2991 0.0309 0.0290 -0.0105 733 TYR A CD1 5705 C CD2 . TYR A 740 ? 0.2217 0.2320 0.2442 -0.0166 0.0144 0.0171 733 TYR A CD2 5706 C CE1 . TYR A 740 ? 0.2115 0.2416 0.3104 -0.0411 -0.0085 0.0060 733 TYR A CE1 5707 C CE2 . TYR A 740 ? 0.2082 0.2129 0.2229 -0.0059 -0.0382 0.0210 733 TYR A CE2 5708 C CZ . TYR A 740 ? 0.2319 0.2364 0.2734 -0.0455 0.0136 -0.0029 733 TYR A CZ 5709 O OH . TYR A 740 ? 0.2425 0.3039 0.3556 -0.0296 -0.0021 -0.0004 733 TYR A OH 5710 N N . VAL A 741 ? 0.1630 0.1690 0.2197 -0.0170 -0.0202 -0.0012 734 VAL A N 5711 C CA . VAL A 741 ? 0.1859 0.1618 0.1996 -0.0313 -0.0414 0.0097 734 VAL A CA 5712 C C . VAL A 741 ? 0.1812 0.1888 0.2010 -0.0165 -0.0235 0.0115 734 VAL A C 5713 O O . VAL A 741 ? 0.1756 0.2135 0.2123 -0.0152 0.0027 -0.0015 734 VAL A O 5714 C CB . VAL A 741 ? 0.1783 0.1437 0.2077 -0.0327 -0.0471 0.0193 734 VAL A CB 5715 C CG1 . VAL A 741 ? 0.2315 0.1848 0.2117 -0.0487 -0.0021 0.0227 734 VAL A CG1 5716 C CG2 . VAL A 741 ? 0.1592 0.2526 0.2343 -0.0166 -0.0472 0.0254 734 VAL A CG2 5717 N N . ALA A 742 ? 0.1733 0.1789 0.2092 -0.0115 -0.0334 -0.0105 735 ALA A N 5718 C CA . ALA A 742 ? 0.1865 0.1737 0.1917 0.0102 -0.0168 -0.0016 735 ALA A CA 5719 C C . ALA A 742 ? 0.1968 0.1568 0.2097 -0.0176 -0.0224 0.0007 735 ALA A C 5720 O O . ALA A 742 ? 0.1891 0.1795 0.1979 -0.0022 -0.0375 0.0014 735 ALA A O 5721 C CB . ALA A 742 ? 0.1781 0.2036 0.2311 0.0089 -0.0135 -0.0155 735 ALA A CB 5722 N N . ALA A 743 ? 0.1602 0.1414 0.2211 -0.0155 -0.0023 -0.0190 736 ALA A N 5723 C CA . ALA A 743 ? 0.1704 0.1541 0.2207 -0.0317 0.0016 -0.0286 736 ALA A CA 5724 C C . ALA A 743 ? 0.1589 0.1954 0.2214 -0.0053 -0.0294 -0.0247 736 ALA A C 5725 O O . ALA A 743 ? 0.1838 0.1981 0.2198 -0.0108 -0.0260 -0.0230 736 ALA A O 5726 C CB . ALA A 743 ? 0.2018 0.1688 0.2209 -0.0273 -0.0113 -0.0021 736 ALA A CB 5727 N N . PHE A 744 ? 0.1544 0.1899 0.2303 -0.0176 -0.0387 -0.0028 737 PHE A N 5728 C CA . PHE A 744 ? 0.1648 0.1872 0.2031 0.0071 -0.0370 0.0081 737 PHE A CA 5729 C C . PHE A 744 ? 0.1846 0.1772 0.2102 -0.0028 -0.0311 -0.0072 737 PHE A C 5730 O O . PHE A 744 ? 0.1856 0.1846 0.1979 -0.0037 -0.0208 0.0000 737 PHE A O 5731 C CB . PHE A 744 ? 0.1461 0.2065 0.2295 -0.0135 -0.0365 0.0036 737 PHE A CB 5732 C CG . PHE A 744 ? 0.1854 0.2306 0.2127 -0.0006 0.0004 0.0036 737 PHE A CG 5733 C CD1 . PHE A 744 ? 0.1508 0.2504 0.2347 0.0541 0.0054 0.0155 737 PHE A CD1 5734 C CD2 . PHE A 744 ? 0.1466 0.2445 0.2203 -0.0232 -0.0212 0.0473 737 PHE A CD2 5735 C CE1 . PHE A 744 ? 0.1687 0.2282 0.2744 0.0299 0.0140 0.0503 737 PHE A CE1 5736 C CE2 . PHE A 744 ? 0.1582 0.2509 0.2211 0.0159 0.0136 0.0382 737 PHE A CE2 5737 C CZ . PHE A 744 ? 0.1556 0.2524 0.2227 0.0351 -0.0234 0.0140 737 PHE A CZ 5738 N N . THR A 745 ? 0.1562 0.1614 0.2194 -0.0051 -0.0366 -0.0019 738 THR A N 5739 C CA . THR A 745 ? 0.1899 0.1500 0.1889 0.0167 -0.0227 -0.0135 738 THR A CA 5740 C C . THR A 745 ? 0.1828 0.1781 0.2006 0.0029 -0.0284 -0.0056 738 THR A C 5741 O O . THR A 745 ? 0.2156 0.1938 0.1845 0.0025 -0.0233 -0.0101 738 THR A O 5742 C CB . THR A 745 ? 0.2000 0.1304 0.1935 -0.0134 -0.0269 -0.0044 738 THR A CB 5743 O OG1 . THR A 745 ? 0.2051 0.1998 0.1920 -0.0119 -0.0194 -0.0164 738 THR A OG1 5744 C CG2 . THR A 745 ? 0.2204 0.1517 0.1914 -0.0223 -0.0035 0.0057 738 THR A CG2 5745 N N . VAL A 746 ? 0.1769 0.1684 0.2180 0.0026 -0.0563 -0.0171 739 VAL A N 5746 C CA . VAL A 746 ? 0.1629 0.1901 0.2097 -0.0111 -0.0483 -0.0429 739 VAL A CA 5747 C C . VAL A 746 ? 0.1483 0.1703 0.2120 -0.0088 -0.0494 -0.0331 739 VAL A C 5748 O O . VAL A 746 ? 0.1972 0.2070 0.2140 -0.0012 -0.0443 -0.0124 739 VAL A O 5749 C CB . VAL A 746 ? 0.1553 0.1878 0.1888 0.0018 -0.0488 -0.0362 739 VAL A CB 5750 C CG1 . VAL A 746 ? 0.1989 0.2278 0.2153 0.0078 -0.0840 -0.0297 739 VAL A CG1 5751 C CG2 . VAL A 746 ? 0.1775 0.1674 0.2370 0.0235 -0.0316 -0.0258 739 VAL A CG2 5752 N N . GLN A 747 ? 0.1657 0.1855 0.2370 0.0047 -0.0451 -0.0298 740 GLN A N 5753 C CA . GLN A 747 ? 0.1923 0.1512 0.2275 0.0119 -0.0442 -0.0139 740 GLN A CA 5754 C C . GLN A 747 ? 0.1926 0.1811 0.2039 0.0167 -0.0409 -0.0317 740 GLN A C 5755 O O . GLN A 747 ? 0.1752 0.2046 0.1836 -0.0056 -0.0565 -0.0167 740 GLN A O 5756 C CB . GLN A 747 ? 0.2337 0.1410 0.2183 0.0227 -0.0280 -0.0200 740 GLN A CB 5757 C CG . GLN A 747 ? 0.2575 0.1780 0.2050 0.0247 -0.0361 -0.0452 740 GLN A CG 5758 C CD . GLN A 747 ? 0.2329 0.1707 0.2477 0.0420 -0.0484 -0.0315 740 GLN A CD 5759 O OE1 . GLN A 747 ? 0.2218 0.2375 0.2948 0.0271 -0.0810 -0.0429 740 GLN A OE1 5760 N NE2 . GLN A 747 ? 0.2854 0.1887 0.2824 0.0381 -0.0422 -0.0733 740 GLN A NE2 5761 N N . ALA A 748 ? 0.1760 0.1869 0.2114 0.0037 -0.0431 -0.0200 741 ALA A N 5762 C CA . ALA A 748 ? 0.1819 0.1958 0.2024 -0.0174 -0.0628 -0.0087 741 ALA A CA 5763 C C . ALA A 748 ? 0.2000 0.1842 0.1944 0.0096 -0.0381 -0.0194 741 ALA A C 5764 O O . ALA A 748 ? 0.1932 0.2023 0.2016 0.0214 -0.0245 -0.0429 741 ALA A O 5765 C CB . ALA A 748 ? 0.1970 0.2201 0.1418 -0.0149 -0.0322 -0.0264 741 ALA A CB 5766 N N . ALA A 749 ? 0.2044 0.1630 0.2073 0.0068 -0.0539 -0.0140 742 ALA A N 5767 C CA . ALA A 749 ? 0.1953 0.1619 0.1880 0.0382 -0.0418 -0.0276 742 ALA A CA 5768 C C . ALA A 749 ? 0.2080 0.2004 0.1969 0.0129 -0.0550 -0.0260 742 ALA A C 5769 O O . ALA A 749 ? 0.2211 0.2024 0.1869 0.0290 -0.0687 -0.0276 742 ALA A O 5770 C CB . ALA A 749 ? 0.2008 0.1534 0.2119 0.0442 -0.0305 -0.0265 742 ALA A CB 5771 N N . ALA A 750 ? 0.2230 0.1682 0.2222 0.0273 -0.0782 -0.0385 743 ALA A N 5772 C CA . ALA A 750 ? 0.2334 0.2041 0.2267 0.0100 -0.0745 -0.0487 743 ALA A CA 5773 C C . ALA A 750 ? 0.2212 0.2191 0.2087 0.0127 -0.0675 -0.0136 743 ALA A C 5774 O O . ALA A 750 ? 0.2258 0.2304 0.2031 0.0356 -0.0855 -0.0296 743 ALA A O 5775 C CB . ALA A 750 ? 0.1847 0.2146 0.2389 0.0126 -0.0742 -0.0224 743 ALA A CB 5776 N N . GLU A 751 ? 0.2189 0.1895 0.2370 0.0207 -0.0652 -0.0181 744 GLU A N 5777 C CA . GLU A 751 ? 0.2569 0.2032 0.2042 0.0508 -0.0648 -0.0233 744 GLU A CA 5778 C C . GLU A 751 ? 0.2361 0.1970 0.1972 0.0314 -0.0817 -0.0441 744 GLU A C 5779 O O . GLU A 751 ? 0.2634 0.2011 0.2147 0.0439 -0.0665 -0.0407 744 GLU A O 5780 C CB . GLU A 751 ? 0.2465 0.1879 0.2354 0.0490 -0.0466 -0.0068 744 GLU A CB 5781 C CG . GLU A 751 ? 0.2795 0.1759 0.2493 0.0139 -0.0467 -0.0172 744 GLU A CG 5782 C CD . GLU A 751 ? 0.3164 0.2155 0.2919 0.0125 -0.0752 -0.0044 744 GLU A CD 5783 O OE1 . GLU A 751 ? 0.2571 0.3096 0.2848 0.0322 -0.0196 0.0169 744 GLU A OE1 5784 O OE2 . GLU A 751 ? 0.3106 0.2043 0.3383 0.0281 -0.0385 -0.0013 744 GLU A OE2 5785 N N . THR A 752 ? 0.2488 0.1922 0.2162 0.0474 -0.0920 -0.0248 745 THR A N 5786 C CA . THR A 752 ? 0.2503 0.1958 0.1765 0.0318 -0.0792 -0.0437 745 THR A CA 5787 C C . THR A 752 ? 0.2563 0.2145 0.1885 0.0344 -0.0897 -0.0354 745 THR A C 5788 O O . THR A 752 ? 0.2734 0.2453 0.1755 0.0403 -0.0742 -0.0439 745 THR A O 5789 C CB . THR A 752 ? 0.2381 0.1945 0.1731 0.0440 -0.0784 -0.0488 745 THR A CB 5790 O OG1 . THR A 752 ? 0.2610 0.2005 0.2056 0.0540 -0.0639 -0.0361 745 THR A OG1 5791 C CG2 . THR A 752 ? 0.1972 0.2511 0.1687 0.0163 -0.0582 -0.0219 745 THR A CG2 5792 N N . LEU A 753 ? 0.2657 0.1957 0.1958 0.0326 -0.0826 -0.0634 746 LEU A N 5793 C CA . LEU A 753 ? 0.2515 0.2048 0.2131 0.0638 -0.0884 -0.0326 746 LEU A CA 5794 C C . LEU A 753 ? 0.2711 0.2201 0.2233 0.0577 -0.0946 -0.0461 746 LEU A C 5795 O O . LEU A 753 ? 0.3092 0.2500 0.2137 0.0688 -0.0951 -0.0591 746 LEU A O 5796 C CB . LEU A 753 ? 0.2495 0.2162 0.2069 0.0709 -0.0918 -0.0428 746 LEU A CB 5797 C CG . LEU A 753 ? 0.2522 0.2049 0.2021 0.0819 -0.0692 -0.0296 746 LEU A CG 5798 C CD1 . LEU A 753 ? 0.2528 0.2504 0.2411 0.0768 -0.0676 -0.0701 746 LEU A CD1 5799 C CD2 . LEU A 753 ? 0.2644 0.1963 0.2692 0.0501 -0.0672 -0.0227 746 LEU A CD2 5800 N N . SER A 754 ? 0.3072 0.1965 0.2251 0.0655 -0.0920 -0.0550 747 SER A N 5801 C CA . SER A 754 ? 0.3295 0.2057 0.2241 0.0728 -0.0763 -0.0697 747 SER A CA 5802 C C . SER A 754 ? 0.3133 0.2036 0.2429 0.0864 -0.0916 -0.0656 747 SER A C 5803 O O . SER A 754 ? 0.3041 0.2281 0.2459 0.0580 -0.0718 -0.0439 747 SER A O 5804 C CB . SER A 754 ? 0.3294 0.2236 0.2183 0.0634 -0.0630 -0.0525 747 SER A CB 5805 O OG . SER A 754 ? 0.3648 0.2424 0.2610 0.0586 -0.0544 -0.0520 747 SER A OG 5806 N N . GLU A 755 ? 0.3240 0.2549 0.2369 0.1133 -0.0981 -0.0840 748 GLU A N 5807 C CA . GLU A 755 ? 0.3437 0.2714 0.2448 0.0687 -0.0864 -0.0781 748 GLU A CA 5808 C C . GLU A 755 ? 0.3370 0.2459 0.2724 0.0892 -0.0856 -0.0818 748 GLU A C 5809 O O . GLU A 755 ? 0.3189 0.2497 0.2790 0.0736 -0.0569 -0.0463 748 GLU A O 5810 C CB . GLU A 755 ? 0.3670 0.3051 0.2694 0.0798 -0.0961 -0.1065 748 GLU A CB 5811 C CG . GLU A 755 ? 0.4225 0.3664 0.3342 0.0706 -0.1638 -0.0901 748 GLU A CG 5812 C CD . GLU A 755 ? 0.6110 0.3912 0.3607 0.0564 -0.0112 -0.1148 748 GLU A CD 5813 O OE1 . GLU A 755 ? 0.6730 0.4089 0.5251 -0.0287 -0.0558 -0.1708 748 GLU A OE1 5814 O OE2 . GLU A 755 ? 0.7564 0.5984 0.3338 0.0276 -0.0195 -0.0964 748 GLU A OE2 5815 N N . VAL A 756 ? 0.3177 0.2743 0.2547 0.0962 -0.0547 -0.0931 749 VAL A N 5816 C CA . VAL A 756 ? 0.3293 0.2608 0.2375 0.0863 -0.0677 -0.0644 749 VAL A CA 5817 C C . VAL A 756 ? 0.3289 0.2591 0.2521 0.0851 -0.0982 -0.0689 749 VAL A C 5818 O O . VAL A 756 ? 0.3455 0.2923 0.2286 0.0838 -0.0973 -0.0421 749 VAL A O 5819 C CB . VAL A 756 ? 0.3199 0.2604 0.2498 0.0866 -0.0682 -0.0769 749 VAL A CB 5820 C CG1 . VAL A 756 ? 0.3577 0.2664 0.2534 0.1140 -0.0910 -0.0475 749 VAL A CG1 5821 C CG2 . VAL A 756 ? 0.3078 0.2845 0.2482 0.0961 -0.0583 -0.0635 749 VAL A CG2 5822 N N . ALA A 757 ? 0.3397 0.2410 0.2567 0.0782 -0.0442 -0.0728 750 ALA A N 5823 C CA . ALA A 757 ? 0.3361 0.2464 0.3005 0.0782 -0.0734 -0.0865 750 ALA A CA 5824 C C . ALA A 757 ? 0.3483 0.2636 0.3402 0.0805 -0.0787 -0.1147 750 ALA A C 5825 O O . ALA A 757 ? 0.3698 0.2563 0.4701 0.0785 -0.1132 -0.1329 750 ALA A O 5826 C CB . ALA A 757 ? 0.3219 0.3071 0.3433 0.1150 -0.0509 -0.0590 750 ALA A CB 5827 O OXT . ALA A 757 ? 0.3446 0.2573 0.3434 0.0808 -0.0929 -0.1492 750 ALA A OXT 5828 ZN ZN . ZN B . ? 0.2098 0.2068 0.2315 0.0220 0.0047 -0.0172 801 ZN A ZN 5829 ZN ZN . ZN C . ? 0.2412 0.2211 0.2571 0.0247 0.0115 -0.0231 802 ZN A ZN 5830 CA CA . CA D . ? 0.1954 0.1949 0.1900 -0.0042 0.0062 -0.0178 803 CA A CA 5831 CL CL . CL E . ? 0.2883 0.2532 0.2966 -0.0065 0.0034 -0.0229 804 CL A CL 5832 C C1 . NAG F . ? 0.3707 0.2931 0.4038 0.0051 0.0861 0.0328 805 NAG A C1 5833 C C2 . NAG F . ? 0.4275 0.3092 0.5220 0.0112 0.1262 -0.0130 805 NAG A C2 5834 C C3 . NAG F . ? 0.4384 0.3582 0.5526 -0.0216 0.1274 -0.0257 805 NAG A C3 5835 C C4 . NAG F . ? 0.4542 0.3656 0.5175 0.0106 0.1440 0.0494 805 NAG A C4 5836 C C5 . NAG F . ? 0.4263 0.3994 0.4591 -0.0162 0.0929 0.0478 805 NAG A C5 5837 C C6 . NAG F . ? 0.5137 0.4274 0.4711 -0.0040 0.1197 0.0597 805 NAG A C6 5838 C C7 . NAG F . ? 0.5044 0.4879 0.5297 0.0778 0.1404 0.0235 805 NAG A C7 5839 C C8 . NAG F . ? 0.5967 0.4601 0.5355 0.0351 0.1640 -0.0886 805 NAG A C8 5840 N N2 . NAG F . ? 0.4912 0.3392 0.5416 -0.0003 0.1502 -0.0317 805 NAG A N2 5841 O O3 . NAG F . ? 0.4621 0.3873 0.6825 -0.0651 0.1738 -0.0954 805 NAG A O3 5842 O O4 . NAG F . ? 0.4757 0.3345 0.5896 -0.0275 0.1334 0.0520 805 NAG A O4 5843 O O5 . NAG F . ? 0.3965 0.3235 0.3789 0.0814 0.0635 0.0813 805 NAG A O5 5844 O O6 . NAG F . ? 0.4030 0.5993 0.4424 -0.0267 0.0892 0.1266 805 NAG A O6 5845 O O7 . NAG F . ? 0.6280 0.5394 0.7178 0.1589 0.0889 0.0363 805 NAG A O7 5846 C C1 . NAG G . ? 0.5096 0.3740 0.5974 -0.0445 0.1529 0.0690 806 NAG A C1 5847 C C2 . NAG G . ? 0.5531 0.3732 0.6565 -0.0051 0.1808 0.0128 806 NAG A C2 5848 C C3 . NAG G . ? 0.6211 0.4332 0.7377 0.0205 0.1841 0.1056 806 NAG A C3 5849 C C4 . NAG G . ? 0.6500 0.4815 0.7285 0.0524 0.2191 0.0189 806 NAG A C4 5850 C C5 . NAG G . ? 0.6260 0.4140 0.7455 -0.0796 0.2698 0.0934 806 NAG A C5 5851 C C6 . NAG G . ? 0.8006 0.4814 0.6827 -0.0139 0.2457 0.0449 806 NAG A C6 5852 C C7 . NAG G . ? 0.4876 0.4612 0.5747 0.0252 0.0441 0.0717 806 NAG A C7 5853 C C8 . NAG G . ? 0.4211 0.4289 0.4990 -0.0117 0.1754 -0.0018 806 NAG A C8 5854 N N2 . NAG G . ? 0.4872 0.3589 0.6370 0.0442 0.1985 0.0498 806 NAG A N2 5855 O O3 . NAG G . ? 0.5817 0.5272 0.8754 -0.1111 0.2839 0.0128 806 NAG A O3 5856 O O4 . NAG G . ? 0.9172 0.5222 0.7683 0.0831 0.1859 0.1128 806 NAG A O4 5857 O O5 . NAG G . ? 0.5520 0.4113 0.6863 -0.0176 0.2382 0.0831 806 NAG A O5 5858 O O6 . NAG G . ? 0.9797 0.4014 0.7269 -0.1166 0.2204 -0.0897 806 NAG A O6 5859 O O7 . NAG G . ? 0.5681 0.4279 0.7128 -0.0241 0.0604 0.0841 806 NAG A O7 5860 C C1 . NAG H . ? 0.4545 0.4374 0.5819 -0.0893 -0.1510 -0.2783 807 NAG A C1 5861 C C2 . NAG H . ? 0.4877 0.5167 0.5952 -0.0468 -0.1211 -0.1798 807 NAG A C2 5862 C C3 . NAG H . ? 0.4993 0.5420 0.7380 -0.0448 -0.1670 -0.1907 807 NAG A C3 5863 C C4 . NAG H . ? 0.5861 0.7088 0.7904 -0.0259 -0.1023 -0.2443 807 NAG A C4 5864 C C5 . NAG H . ? 0.5762 0.6494 0.8162 -0.0809 -0.1599 -0.2490 807 NAG A C5 5865 C C6 . NAG H . ? 0.6291 0.6216 0.8832 -0.0077 -0.1422 -0.2251 807 NAG A C6 5866 C C7 . NAG H . ? 0.5224 0.5772 0.6745 -0.0348 -0.0159 -0.1324 807 NAG A C7 5867 C C8 . NAG H . ? 0.4577 0.5387 0.6519 -0.0568 -0.0551 -0.1384 807 NAG A C8 5868 N N2 . NAG H . ? 0.3324 0.5234 0.6618 -0.1158 -0.0208 -0.1575 807 NAG A N2 5869 O O3 . NAG H . ? 0.4410 0.7430 0.9158 0.0007 -0.3173 -0.2093 807 NAG A O3 5870 O O4 . NAG H . ? 0.7633 0.7394 1.0897 -0.1551 -0.0250 -0.2558 807 NAG A O4 5871 O O5 . NAG H . ? 0.4742 0.6587 0.5853 -0.0398 -0.0863 -0.2555 807 NAG A O5 5872 O O6 . NAG H . ? 0.7666 0.7057 1.0829 0.1033 0.1326 0.0840 807 NAG A O6 5873 O O7 . NAG H . ? 0.5990 0.8351 0.7006 -0.0748 0.0249 -0.1631 807 NAG A O7 5874 C C1 . NAG I . ? 0.5694 0.4475 0.4423 0.0275 0.0394 -0.1973 808 NAG A C1 5875 C C2 . NAG I . ? 0.5557 0.4247 0.4927 0.0341 0.0475 -0.1913 808 NAG A C2 5876 C C3 . NAG I . ? 0.5962 0.4761 0.5202 0.0328 0.0342 -0.2424 808 NAG A C3 5877 C C4 . NAG I . ? 0.6088 0.4873 0.5571 0.0205 0.0550 -0.2132 808 NAG A C4 5878 C C5 . NAG I . ? 0.6017 0.4751 0.5265 0.0067 0.0265 -0.2088 808 NAG A C5 5879 C C6 . NAG I . ? 0.5375 0.4915 0.5747 0.0139 -0.0324 -0.2380 808 NAG A C6 5880 C C7 . NAG I . ? 0.5379 0.5929 0.5432 0.0306 0.0733 -0.0813 808 NAG A C7 5881 C C8 . NAG I . ? 0.5344 0.6063 0.4927 0.0578 0.0998 -0.1095 808 NAG A C8 5882 N N2 . NAG I . ? 0.5834 0.4594 0.4591 0.0359 0.0358 -0.2093 808 NAG A N2 5883 O O3 . NAG I . ? 0.6385 0.4689 0.4554 0.0062 0.1390 -0.2068 808 NAG A O3 5884 O O4 . NAG I . ? 0.7274 0.5614 0.6271 0.0092 -0.0066 -0.2674 808 NAG A O4 5885 O O5 . NAG I . ? 0.5673 0.4061 0.5759 0.0209 0.0223 -0.1904 808 NAG A O5 5886 O O6 . NAG I . ? 0.5355 0.4805 0.5205 -0.0109 0.0381 -0.2954 808 NAG A O6 5887 O O7 . NAG I . ? 0.6341 0.5732 0.5720 0.0209 0.0243 -0.0625 808 NAG A O7 5888 C C1 . NAG J . ? 0.6976 0.6218 0.6682 -0.0022 -0.1078 -0.3312 809 NAG A C1 5889 C C2 . NAG J . ? 0.7571 0.5976 0.6885 0.0726 -0.0954 -0.2878 809 NAG A C2 5890 C C3 . NAG J . ? 0.7121 0.6547 0.8232 0.0411 -0.1193 -0.2259 809 NAG A C3 5891 C C4 . NAG J . ? 0.8351 0.6672 0.8843 0.0577 -0.0735 -0.2475 809 NAG A C4 5892 C C5 . NAG J . ? 0.8243 0.6236 0.8055 0.0285 -0.0724 -0.3411 809 NAG A C5 5893 C C6 . NAG J . ? 0.8187 0.6639 0.9788 0.0917 -0.0142 -0.2468 809 NAG A C6 5894 C C7 . NAG J . ? 0.7093 0.6583 0.6181 0.0519 -0.0075 -0.2302 809 NAG A C7 5895 C C8 . NAG J . ? 0.6700 0.6173 0.4822 -0.0031 -0.0035 -0.2455 809 NAG A C8 5896 N N2 . NAG J . ? 0.7256 0.5908 0.6144 0.0379 -0.0888 -0.2957 809 NAG A N2 5897 O O3 . NAG J . ? 0.7939 0.7314 0.7415 -0.0999 -0.1830 -0.3277 809 NAG A O3 5898 O O4 . NAG J . ? 0.7446 0.7286 1.1789 0.0328 -0.0374 -0.1764 809 NAG A O4 5899 O O5 . NAG J . ? 0.7525 0.6437 0.6997 0.0560 -0.1530 -0.2610 809 NAG A O5 5900 O O6 . NAG J . ? 0.8589 0.6337 0.8848 0.0774 -0.0150 -0.3056 809 NAG A O6 5901 O O7 . NAG J . ? 0.7279 0.7351 0.6439 -0.0162 0.0534 -0.3322 809 NAG A O7 5902 C C1 . NAG K . ? 0.8642 0.8411 0.4861 0.0480 0.0705 0.1636 810 NAG A C1 5903 C C2 . NAG K . ? 0.9385 0.8083 0.7822 0.1082 0.0064 0.0211 810 NAG A C2 5904 C C3 . NAG K . ? 0.9342 0.9179 0.8477 0.1081 0.0682 -0.0181 810 NAG A C3 5905 C C4 . NAG K . ? 0.9572 0.9310 0.7999 0.1095 0.0538 0.0003 810 NAG A C4 5906 C C5 . NAG K . ? 0.8915 0.9255 0.7356 0.0709 -0.0048 0.0121 810 NAG A C5 5907 C C6 . NAG K . ? 0.8612 0.8263 0.7295 -0.0443 -0.0499 -0.0440 810 NAG A C6 5908 C C7 . NAG K . ? 1.0283 0.9715 0.7296 0.0322 0.0776 0.0166 810 NAG A C7 5909 C C8 . NAG K . ? 0.9253 0.9478 0.7055 0.0426 -0.0149 0.0359 810 NAG A C8 5910 N N2 . NAG K . ? 0.9903 0.9753 0.7328 0.0550 0.1030 -0.0327 810 NAG A N2 5911 O O3 . NAG K . ? 1.2346 0.8199 1.0321 0.0739 0.1382 -0.0343 810 NAG A O3 5912 O O4 . NAG K . ? 0.9017 1.1510 0.8898 -0.1442 0.2821 -0.0708 810 NAG A O4 5913 O O5 . NAG K . ? 1.1038 0.8584 0.5191 0.0172 -0.0828 0.2348 810 NAG A O5 5914 O O6 . NAG K . ? 0.7749 0.9466 0.6660 -0.2581 -0.0840 -0.0757 810 NAG A O6 5915 O O7 . NAG K . ? 1.0729 1.2069 0.7820 -0.0011 0.1354 0.2396 810 NAG A O7 5916 C C1 . NAG L . ? 0.3939 0.4048 0.5697 0.1383 -0.0650 -0.1740 811 NAG A C1 5917 C C2 . NAG L . ? 0.3241 0.4716 0.5532 0.1403 -0.1234 -0.0775 811 NAG A C2 5918 C C3 . NAG L . ? 0.3858 0.6194 0.6122 0.1690 -0.0606 -0.1502 811 NAG A C3 5919 C C4 . NAG L . ? 0.3579 0.6414 0.6592 0.1687 -0.0825 -0.1196 811 NAG A C4 5920 C C5 . NAG L . ? 0.3830 0.5664 0.6460 0.1188 -0.0974 -0.1837 811 NAG A C5 5921 C C6 . NAG L . ? 0.4211 0.5211 0.6732 0.1294 -0.2039 -0.1089 811 NAG A C6 5922 C C7 . NAG L . ? 0.3304 0.3045 0.4150 0.0739 -0.0185 -0.1035 811 NAG A C7 5923 C C8 . NAG L . ? 0.3126 0.3245 0.4285 0.0321 0.0335 -0.0961 811 NAG A C8 5924 N N2 . NAG L . ? 0.3709 0.3304 0.5121 0.1154 -0.0507 -0.0944 811 NAG A N2 5925 O O3 . NAG L . ? 0.4166 0.7882 0.5915 0.2149 -0.0246 -0.1419 811 NAG A O3 5926 O O4 . NAG L . ? 0.3195 0.7695 0.7382 0.2153 -0.1844 -0.1711 811 NAG A O4 5927 O O5 . NAG L . ? 0.3979 0.5352 0.5646 0.1331 -0.1253 -0.1193 811 NAG A O5 5928 O O6 . NAG L . ? 0.3686 0.5364 0.7484 0.0344 -0.0670 -0.1249 811 NAG A O6 5929 O O7 . NAG L . ? 0.2914 0.2905 0.4534 0.0487 -0.0755 -0.0852 811 NAG A O7 5930 C C1 . NAG M . ? 0.3950 0.2698 0.2935 0.1019 -0.1433 -0.1018 812 NAG A C1 5931 C C2 . NAG M . ? 0.4113 0.3271 0.2529 0.1191 -0.1228 -0.1185 812 NAG A C2 5932 C C3 . NAG M . ? 0.3982 0.3028 0.3315 0.1293 -0.0930 -0.1079 812 NAG A C3 5933 C C4 . NAG M . ? 0.4392 0.3062 0.3310 0.1376 -0.1103 -0.1255 812 NAG A C4 5934 C C5 . NAG M . ? 0.3967 0.3299 0.3480 0.1346 -0.1482 -0.1174 812 NAG A C5 5935 C C6 . NAG M . ? 0.4992 0.4398 0.3079 0.0940 -0.1496 -0.0740 812 NAG A C6 5936 C C7 . NAG M . ? 0.4528 0.5280 0.3311 0.0539 -0.1534 -0.0873 812 NAG A C7 5937 C C8 . NAG M . ? 0.4153 0.5208 0.4015 0.0156 -0.1829 -0.0153 812 NAG A C8 5938 N N2 . NAG M . ? 0.3551 0.4195 0.2837 0.1313 -0.1363 -0.0778 812 NAG A N2 5939 O O3 . NAG M . ? 0.3880 0.3520 0.3364 0.1413 -0.1072 -0.0965 812 NAG A O3 5940 O O4 . NAG M . ? 0.4900 0.3378 0.3433 0.1007 -0.0994 -0.1446 812 NAG A O4 5941 O O5 . NAG M . ? 0.4172 0.3627 0.2945 0.1231 -0.1441 -0.1192 812 NAG A O5 5942 O O6 . NAG M . ? 0.5487 0.4452 0.3438 0.1311 -0.1365 -0.0459 812 NAG A O6 5943 O O7 . NAG M . ? 0.4471 0.5887 0.3818 0.0998 -0.1804 -0.1148 812 NAG A O7 5944 C C1 . NAG N . ? 0.5050 0.4086 0.3575 0.0835 -0.1160 -0.2026 813 NAG A C1 5945 C C2 . NAG N . ? 0.5233 0.4325 0.4917 0.0521 -0.0714 -0.2077 813 NAG A C2 5946 C C3 . NAG N . ? 0.5685 0.5105 0.4307 0.0055 -0.1261 -0.1740 813 NAG A C3 5947 C C4 . NAG N . ? 0.5631 0.4981 0.4076 0.0636 -0.1092 -0.2041 813 NAG A C4 5948 C C5 . NAG N . ? 0.5153 0.5073 0.3921 0.0752 -0.1479 -0.2386 813 NAG A C5 5949 C C6 . NAG N . ? 0.5301 0.7174 0.4115 0.0637 -0.0618 -0.1146 813 NAG A C6 5950 C C7 . NAG N . ? 0.5622 0.5728 0.4814 0.0095 -0.1492 -0.1698 813 NAG A C7 5951 C C8 . NAG N . ? 0.3026 0.4236 0.5131 -0.1180 -0.0681 -0.0484 813 NAG A C8 5952 N N2 . NAG N . ? 0.5356 0.5057 0.5381 0.0346 -0.0862 -0.1899 813 NAG A N2 5953 O O3 . NAG N . ? 0.6185 0.4799 0.5665 0.0310 -0.1428 -0.2638 813 NAG A O3 5954 O O4 . NAG N . ? 0.5743 0.6979 0.3681 0.0276 -0.0737 -0.1432 813 NAG A O4 5955 O O5 . NAG N . ? 0.5111 0.4367 0.3462 0.1296 -0.1543 -0.1420 813 NAG A O5 5956 O O6 . NAG N . ? 0.5663 0.6481 0.6717 0.1000 -0.0993 -0.1433 813 NAG A O6 5957 O O7 . NAG N . ? 0.5985 0.7412 0.6843 -0.0568 -0.1389 -0.1346 813 NAG A O7 5958 C C1 . NAG O . ? 0.3203 0.2089 0.3354 0.0586 -0.0841 -0.0730 814 NAG A C1 5959 C C2 . NAG O . ? 0.3051 0.2092 0.3265 0.0334 -0.0797 -0.0612 814 NAG A C2 5960 C C3 . NAG O . ? 0.4092 0.2285 0.3699 0.0771 -0.1260 -0.0610 814 NAG A C3 5961 C C4 . NAG O . ? 0.3983 0.2879 0.3904 0.0746 -0.1397 -0.1061 814 NAG A C4 5962 C C5 . NAG O . ? 0.4327 0.2966 0.3649 0.0873 -0.1215 -0.0634 814 NAG A C5 5963 C C6 . NAG O . ? 0.4847 0.3135 0.4379 0.1428 -0.1134 -0.1666 814 NAG A C6 5964 C C7 . NAG O . ? 0.2345 0.2331 0.3010 0.0111 -0.0625 -0.0482 814 NAG A C7 5965 C C8 . NAG O . ? 0.2697 0.2163 0.2942 0.0274 -0.0405 -0.0305 814 NAG A C8 5966 N N2 . NAG O . ? 0.2621 0.1979 0.3090 0.0124 -0.0774 -0.0344 814 NAG A N2 5967 O O3 . NAG O . ? 0.3612 0.3047 0.3542 0.0818 -0.0877 -0.0589 814 NAG A O3 5968 O O4 . NAG O . ? 0.4873 0.3308 0.4645 0.0977 -0.1516 -0.0109 814 NAG A O4 5969 O O5 . NAG O . ? 0.3957 0.2854 0.3125 0.0706 -0.1133 -0.0987 814 NAG A O5 5970 O O6 . NAG O . ? 0.5628 0.5496 0.6061 0.0155 -0.1663 -0.0835 814 NAG A O6 5971 O O7 . NAG O . ? 0.2124 0.2834 0.2911 0.0135 -0.0858 -0.0170 814 NAG A O7 5972 C C1 . NAG P . ? 0.4503 0.3166 0.4690 0.1201 -0.1085 0.0368 815 NAG A C1 5973 C C2 . NAG P . ? 0.5927 0.3425 0.4611 0.1045 -0.1075 0.0071 815 NAG A C2 5974 C C3 . NAG P . ? 0.5265 0.3441 0.4625 0.1254 -0.0835 -0.0254 815 NAG A C3 5975 C C4 . NAG P . ? 0.4603 0.3854 0.4842 0.1567 -0.0622 0.0117 815 NAG A C4 5976 C C5 . NAG P . ? 0.4885 0.3771 0.5205 0.1631 -0.0609 0.0354 815 NAG A C5 5977 C C6 . NAG P . ? 0.4420 0.7345 0.5239 0.0771 -0.1119 0.0929 815 NAG A C6 5978 C C7 . NAG P . ? 0.6431 0.4640 0.5819 0.1162 -0.0608 -0.0891 815 NAG A C7 5979 C C8 . NAG P . ? 0.6671 0.3318 0.4550 0.0763 -0.1076 -0.0954 815 NAG A C8 5980 N N2 . NAG P . ? 0.6859 0.3938 0.5251 0.1460 -0.0582 0.0242 815 NAG A N2 5981 O O3 . NAG P . ? 0.5855 0.2902 0.4519 0.0281 0.0301 0.0018 815 NAG A O3 5982 O O4 . NAG P . ? 0.4572 0.4377 0.3922 0.1150 0.0131 0.0887 815 NAG A O4 5983 O O5 . NAG P . ? 0.4564 0.3664 0.4886 0.0612 -0.1051 -0.0153 815 NAG A O5 5984 O O6 . NAG P . ? 0.5882 0.7888 0.8225 -0.0528 0.0297 0.1611 815 NAG A O6 5985 O O7 . NAG P . ? 0.9187 0.9168 0.5759 0.0945 0.0399 -0.1205 815 NAG A O7 5986 C C1 . BMA Q . ? 0.4942 0.4263 0.4372 0.0845 -0.0006 0.0690 816 BMA A C1 5987 C C2 . BMA Q . ? 0.4257 0.4274 0.4624 0.0044 -0.0461 0.0568 816 BMA A C2 5988 C C3 . BMA Q . ? 0.3638 0.4298 0.4506 0.0002 0.0117 0.1492 816 BMA A C3 5989 C C4 . BMA Q . ? 0.4632 0.4429 0.4730 0.0450 0.0031 0.0055 816 BMA A C4 5990 C C5 . BMA Q . ? 0.5248 0.4043 0.4774 0.0348 0.0147 -0.0060 816 BMA A C5 5991 C C6 . BMA Q . ? 0.4720 0.5144 0.4751 0.0012 0.0145 -0.0518 816 BMA A C6 5992 O O2 . BMA Q . ? 0.3326 0.5509 0.4641 0.0549 -0.0897 0.1075 816 BMA A O2 5993 O O3 . BMA Q . ? 0.2940 0.4661 0.4539 -0.0067 -0.0264 0.1206 816 BMA A O3 5994 O O4 . BMA Q . ? 0.3792 0.3987 0.6584 0.0241 -0.0012 0.0570 816 BMA A O4 5995 O O5 . BMA Q . ? 0.3447 0.3751 0.5177 0.0372 -0.0631 0.0058 816 BMA A O5 5996 O O6 . BMA Q . ? 0.4168 0.5359 0.5807 -0.0358 -0.0257 0.0874 816 BMA A O6 5997 C C1 . MAN R . ? 0.4725 0.4968 0.5575 -0.0367 -0.0282 0.1951 817 MAN A C1 5998 C C2 . MAN R . ? 0.5450 0.4243 0.5581 -0.0273 -0.1067 0.0950 817 MAN A C2 5999 C C3 . MAN R . ? 0.5667 0.4516 0.6452 0.0615 -0.0676 0.0575 817 MAN A C3 6000 C C4 . MAN R . ? 0.5357 0.6148 0.7193 -0.0257 -0.0490 0.0188 817 MAN A C4 6001 C C5 . MAN R . ? 0.4880 0.6450 0.6577 -0.0464 0.0125 0.0286 817 MAN A C5 6002 C C6 . MAN R . ? 0.5289 0.6033 0.8522 0.0097 -0.0427 0.0287 817 MAN A C6 6003 O O2 . MAN R . ? 0.5723 0.5606 0.6170 -0.0943 -0.0195 0.1848 817 MAN A O2 6004 O O3 . MAN R . ? 0.5800 0.5847 0.6719 -0.0630 -0.2204 -0.0189 817 MAN A O3 6005 O O4 . MAN R . ? 0.5910 0.7262 0.7279 0.1170 -0.1234 -0.0351 817 MAN A O4 6006 O O5 . MAN R . ? 0.4256 0.5088 0.5848 -0.0866 -0.0881 0.1203 817 MAN A O5 6007 O O6 . MAN R . ? 0.5354 0.5565 0.7155 0.0786 0.0888 0.0173 817 MAN A O6 6008 O O4 . 29D S . ? 1.5125 0.8666 1.4081 0.3413 -0.1422 -0.1001 818 29D A O4 6009 C C4 . 29D S . ? 1.2778 0.9858 1.1403 0.0592 -0.0161 -0.0061 818 29D A C4 6010 C C4A . 29D S . ? 1.2390 0.8787 1.0829 0.0619 0.0897 -0.1331 818 29D A C4A 6011 N N3 . 29D S . ? 1.2868 0.9688 1.1465 -0.0096 -0.0153 -0.0626 818 29D A N3 6012 C C8A . 29D S . ? 1.1276 0.9278 1.0561 0.0568 0.1058 -0.1383 818 29D A C8A 6013 N N5 . 29D S . ? 1.1179 0.8574 1.0924 0.0056 0.0987 -0.2576 818 29D A N5 6014 C C2 . 29D S . ? 1.2234 0.8591 1.1041 -0.0594 0.0772 -0.0568 818 29D A C2 6015 N N8 . 29D S . ? 1.1818 0.6757 0.8560 -0.0320 -0.0164 -0.2322 818 29D A N8 6016 N N1 . 29D S . ? 1.1971 0.8770 1.0946 0.0953 0.2428 -0.2040 818 29D A N1 6017 C C6 . 29D S . ? 1.1016 0.7557 0.9612 -0.0617 0.0322 -0.2309 818 29D A C6 6018 N N2 . 29D S . ? 1.2562 0.9456 1.2442 -0.1017 0.1379 -0.0191 818 29D A N2 6019 C C7 . 29D S . ? 0.9319 0.7987 1.0200 -0.1456 -0.0505 -0.2218 818 29D A C7 6020 C C9 . 29D S . ? 1.2296 0.6510 0.6933 0.0420 0.2231 -0.3752 818 29D A C9 6021 N N10 . 29D S . ? 1.1083 0.9469 1.1899 -0.2842 0.1402 0.1496 818 29D A N10 6022 C CBX . 29D S . ? 1.4242 1.2957 1.2900 0.1137 0.0343 0.1393 818 29D A CBX 6023 C CAQ . 29D S . ? 1.4155 1.3218 1.1337 0.1257 0.1117 -0.0311 818 29D A CAQ 6024 C CAR . 29D S . ? 1.1028 1.1575 1.2295 0.1406 -0.1553 0.0227 818 29D A CAR 6025 C CAS . 29D S . ? 1.6781 1.5651 1.2572 0.1674 -0.1524 -0.0254 818 29D A CAS 6026 C CAT . 29D S . ? 1.7575 1.5878 1.1903 0.1605 -0.3433 0.0274 818 29D A CAT 6027 C CBY . 29D S . ? 1.7697 1.6888 1.2468 0.1675 -0.2603 -0.0722 818 29D A CBY 6028 C CBV . 29D S . ? 1.6478 1.4515 1.3642 0.0201 -0.2752 -0.0238 818 29D A CBV 6029 O OAJ . 29D S . ? 1.7014 1.3856 1.5017 -0.0616 -0.3150 -0.1867 818 29D A OAJ 6030 N NBM . 29D S . ? 1.7244 1.7951 1.3089 -0.0560 -0.0724 -0.0094 818 29D A NBM 6031 C CCG . 29D S . ? 1.1605 1.3075 1.4409 -0.1927 0.0424 0.0572 818 29D A CCG 6032 C CBR . 29D S . ? 1.3844 1.2790 1.6353 -0.0629 0.1574 0.2367 818 29D A CBR 6033 O OAO . 29D S . ? 1.4782 1.3919 1.7750 0.0028 0.3916 0.2382 818 29D A OAO 6034 C CBC . 29D S . ? 1.0255 0.8914 0.8405 0.1107 0.0255 0.0040 818 29D A CBC 6035 C CAY . 29D S . ? 0.5933 0.8292 0.8604 0.1311 -0.0272 0.0072 818 29D A CAY 6036 C CBU . 29D S . ? 1.2176 0.9215 1.1883 -0.2416 0.0106 0.0245 818 29D A CBU 6037 O OAI . 29D S . ? 1.5646 1.3715 1.1424 -0.3659 0.0515 -0.0720 818 29D A OAI 6038 O OAF . 29D S . ? 1.1072 1.2606 1.5599 -0.1117 -0.1223 0.2442 818 29D A OAF 6039 N NBL . 29D S . ? 1.0686 0.9745 1.3267 -0.1184 0.0358 0.0217 818 29D A NBL 6040 C CCF . 29D S . ? 0.8396 0.8736 0.9350 -0.0320 -0.1268 -0.0963 818 29D A CCF 6041 C CBQ . 29D S . ? 0.8894 1.1788 0.9971 0.0876 0.0800 0.1117 818 29D A CBQ 6042 O OAN . 29D S . ? 1.3636 1.4240 0.9926 0.1211 0.2155 0.1165 818 29D A OAN 6043 C CBB . 29D S . ? 0.5847 0.5164 0.7052 0.1103 -0.0624 0.0740 818 29D A CBB 6044 C CAX . 29D S . ? 0.3863 0.6740 0.6360 -0.2503 0.0442 0.0092 818 29D A CAX 6045 C CBT . 29D S . ? 0.3750 0.4700 0.5617 0.0053 -0.0139 -0.0313 818 29D A CBT 6046 O OAH . 29D S . ? 0.4373 0.4798 0.5326 -0.0405 -0.0249 -0.0340 818 29D A OAH 6047 O OAE . 29D S . ? 0.7956 1.4483 0.8162 -0.2200 0.2325 0.2115 818 29D A OAE 6048 N NBK . 29D S . ? 0.3443 0.4211 0.4820 0.0134 0.0281 -0.0495 818 29D A NBK 6049 C CCE . 29D S . ? 0.3053 0.3594 0.3720 -0.0477 -0.0369 -0.1103 818 29D A CCE 6050 C CBP . 29D S . ? 0.3861 0.5089 0.3648 -0.0054 -0.0074 -0.1028 818 29D A CBP 6051 O OAM . 29D S . ? 0.4680 0.6212 0.3896 0.0428 -0.1055 -0.0558 818 29D A OAM 6052 C CBA . 29D S . ? 0.3019 0.2575 0.2467 -0.0270 -0.0373 -0.0283 818 29D A CBA 6053 C CAW . 29D S . ? 0.2212 0.2567 0.2906 0.0069 -0.0244 -0.0903 818 29D A CAW 6054 C CBS . 29D S . ? 0.2381 0.1820 0.2233 -0.0008 -0.0748 0.0234 818 29D A CBS 6055 O OAG . 29D S . ? 0.2407 0.2298 0.2530 0.0335 -0.0077 -0.0266 818 29D A OAG 6056 O OAD . 29D S . ? 0.3350 0.6330 0.3814 -0.0644 -0.0122 -0.2088 818 29D A OAD 6057 N N . 29D S . ? 0.2014 0.2073 0.2334 0.0324 -0.0166 -0.0257 818 29D A N 6058 C CA . 29D S . ? 0.1896 0.2147 0.2175 0.0183 -0.0166 -0.0080 818 29D A CA 6059 C C . 29D S . ? 0.2150 0.2025 0.2311 -0.0005 -0.0061 -0.0178 818 29D A C 6060 O O . 29D S . ? 0.2277 0.1919 0.2430 0.0066 0.0109 0.0062 818 29D A O 6061 C CB . 29D S . ? 0.2058 0.1914 0.2221 0.0257 -0.0099 0.0090 818 29D A CB 6062 C CG . 29D S . ? 0.2367 0.1867 0.2489 0.0399 -0.0173 0.0049 818 29D A CG 6063 C CD . 29D S . ? 0.2167 0.2063 0.2450 0.0173 -0.0265 0.0012 818 29D A CD 6064 O OE2 . 29D S . ? 0.1988 0.2082 0.2395 0.0176 0.0022 -0.0277 818 29D A OE2 6065 O OE1 . 29D S . ? 0.2142 0.1914 0.2475 0.0122 -0.0084 -0.0003 818 29D A OE1 6066 O OXT . 29D S . ? 0.2195 0.2274 0.2107 0.0046 0.0231 -0.0263 818 29D A OXT 6067 O O . HOH T . ? 0.1717 0.1660 0.2093 0.0342 0.0488 -0.0042 901 HOH A O 6068 O O . HOH T . ? 0.2294 0.1920 0.2130 0.0008 0.0267 0.0004 902 HOH A O 6069 O O . HOH T . ? 0.2431 0.2099 0.1783 0.0555 -0.0614 -0.0220 903 HOH A O 6070 O O . HOH T . ? 0.2492 0.2233 0.2659 0.0224 0.0139 -0.0017 904 HOH A O 6071 O O . HOH T . ? 0.2204 0.1967 0.1899 0.0105 -0.0173 -0.0237 905 HOH A O 6072 O O . HOH T . ? 0.1916 0.1914 0.2018 -0.0085 0.0053 0.0206 906 HOH A O 6073 O O . HOH T . ? 0.2315 0.1979 0.2052 0.0197 0.0034 -0.0309 907 HOH A O 6074 O O . HOH T . ? 0.2226 0.2000 0.2773 0.0153 0.0260 -0.0060 908 HOH A O 6075 O O . HOH T . ? 0.1973 0.1862 0.2218 0.0276 -0.0131 -0.0248 909 HOH A O 6076 O O . HOH T . ? 0.2170 0.2176 0.1584 0.0318 -0.0099 -0.0076 910 HOH A O 6077 O O . HOH T . ? 0.2157 0.2004 0.2050 0.0043 0.0261 -0.0130 911 HOH A O 6078 O O . HOH T . ? 0.2692 0.2064 0.1919 0.0161 0.0387 0.0529 912 HOH A O 6079 O O . HOH T . ? 0.2664 0.2274 0.2975 0.0746 0.0072 0.0092 913 HOH A O 6080 O O . HOH T . ? 0.1968 0.2520 0.2239 -0.0093 -0.0379 -0.0269 914 HOH A O 6081 O O . HOH T . ? 0.1875 0.2561 0.1880 0.0266 0.0424 0.0486 915 HOH A O 6082 O O . HOH T . ? 0.1946 0.1998 0.2190 0.0133 -0.0098 -0.0202 916 HOH A O 6083 O O . HOH T . ? 0.2135 0.2413 0.2246 0.0090 -0.0060 0.0132 917 HOH A O 6084 O O . HOH T . ? 0.2143 0.2383 0.2814 0.0220 -0.0058 -0.0425 918 HOH A O 6085 O O . HOH T . ? 0.2151 0.2168 0.2069 0.0281 -0.0289 -0.0294 919 HOH A O 6086 O O . HOH T . ? 0.2655 0.2225 0.2083 0.0449 0.0718 0.0458 920 HOH A O 6087 O O . HOH T . ? 0.2252 0.1865 0.3040 0.0494 -0.0512 -0.0077 921 HOH A O 6088 O O . HOH T . ? 0.2747 0.2372 0.2587 0.0357 -0.0530 -0.0096 922 HOH A O 6089 O O . HOH T . ? 0.2355 0.1839 0.2517 -0.0036 0.0243 0.0010 923 HOH A O 6090 O O . HOH T . ? 0.2489 0.2204 0.2647 -0.0003 -0.0077 -0.0089 924 HOH A O 6091 O O . HOH T . ? 0.2315 0.2580 0.2116 -0.0079 0.0408 -0.0453 925 HOH A O 6092 O O . HOH T . ? 0.3321 0.2627 0.2127 0.0661 -0.0525 -0.0503 926 HOH A O 6093 O O . HOH T . ? 0.2556 0.2288 0.2089 -0.0072 0.0680 0.0124 927 HOH A O 6094 O O . HOH T . ? 0.2036 0.2234 0.1929 0.0164 0.0276 0.0209 928 HOH A O 6095 O O . HOH T . ? 0.3019 0.2512 0.3278 0.0301 0.0663 0.0124 929 HOH A O 6096 O O . HOH T . ? 0.2327 0.2388 0.2620 0.0187 0.0633 -0.0216 930 HOH A O 6097 O O . HOH T . ? 0.2069 0.2665 0.2093 -0.0023 0.0260 -0.0570 931 HOH A O 6098 O O . HOH T . ? 0.2450 0.2405 0.2412 0.0301 0.0151 -0.0176 932 HOH A O 6099 O O . HOH T . ? 0.2210 0.2438 0.3188 0.0051 0.0417 -0.0185 933 HOH A O 6100 O O . HOH T . ? 0.2173 0.2951 0.2403 0.0295 0.0169 0.0153 934 HOH A O 6101 O O . HOH T . ? 0.3339 0.2396 0.1594 0.0832 -0.0556 -0.0307 935 HOH A O 6102 O O . HOH T . ? 0.2242 0.2260 0.2543 0.0413 0.0270 -0.0150 936 HOH A O 6103 O O . HOH T . ? 0.2337 0.2299 0.2721 0.0248 0.0011 0.0092 937 HOH A O 6104 O O . HOH T . ? 0.2470 0.3041 0.2217 0.0366 -0.0149 -0.0354 938 HOH A O 6105 O O . HOH T . ? 0.2949 0.3091 0.3731 0.0940 0.0520 -0.0079 939 HOH A O 6106 O O . HOH T . ? 0.2061 0.2229 0.2630 -0.0022 0.0238 -0.0349 940 HOH A O 6107 O O . HOH T . ? 0.2260 0.3225 0.4119 -0.0796 0.0182 -0.0311 941 HOH A O 6108 O O . HOH T . ? 0.2034 0.2334 0.3356 -0.0365 0.0248 0.0275 942 HOH A O 6109 O O . HOH T . ? 0.2510 0.2215 0.3188 -0.0188 0.0043 -0.0404 943 HOH A O 6110 O O . HOH T . ? 0.2157 0.1946 0.2230 0.0115 0.0100 -0.0326 944 HOH A O 6111 O O . HOH T . ? 0.2908 0.2149 0.2940 0.0264 0.0277 -0.0336 945 HOH A O 6112 O O . HOH T . ? 0.2009 0.2381 0.2076 -0.0372 0.0004 -0.0422 946 HOH A O 6113 O O . HOH T . ? 0.2283 0.2594 0.2723 0.0303 0.0220 -0.0127 947 HOH A O 6114 O O . HOH T . ? 0.2211 0.2341 0.2906 0.0290 -0.0001 -0.0271 948 HOH A O 6115 O O . HOH T . ? 0.2479 0.3545 0.2981 0.0616 0.0761 -0.0243 949 HOH A O 6116 O O . HOH T . ? 0.2130 0.2837 0.3089 0.0568 0.0015 -0.0407 950 HOH A O 6117 O O . HOH T . ? 0.3763 0.3404 0.2782 -0.0330 0.0308 -0.1273 951 HOH A O 6118 O O . HOH T . ? 0.4159 0.3823 0.3463 0.0394 0.0125 -0.0108 952 HOH A O 6119 O O . HOH T . ? 0.1922 0.2128 0.2432 0.0188 -0.0133 -0.0151 953 HOH A O 6120 O O . HOH T . ? 0.2376 0.2322 0.2677 0.0236 0.0150 0.0006 954 HOH A O 6121 O O . HOH T . ? 0.1911 0.2803 0.3190 -0.0100 0.0084 -0.0626 955 HOH A O 6122 O O . HOH T . ? 0.2026 0.2013 0.2364 0.0050 0.0197 -0.0170 956 HOH A O 6123 O O . HOH T . ? 0.2237 0.2421 0.2100 -0.0058 -0.0349 -0.0185 957 HOH A O 6124 O O . HOH T . ? 0.4008 0.2462 0.2040 0.0894 -0.0259 0.0161 958 HOH A O 6125 O O . HOH T . ? 0.1942 0.2851 0.2401 -0.0347 0.0197 0.0101 959 HOH A O 6126 O O . HOH T . ? 0.2214 0.2787 0.3360 -0.0416 -0.0015 0.0241 960 HOH A O 6127 O O . HOH T . ? 0.2427 0.2705 0.1878 0.0409 0.0369 -0.0450 961 HOH A O 6128 O O . HOH T . ? 0.2750 0.2058 0.2481 0.0471 -0.0267 0.0363 962 HOH A O 6129 O O . HOH T . ? 0.2939 0.2686 0.3172 0.0247 0.0261 0.0035 963 HOH A O 6130 O O . HOH T . ? 0.2558 0.2429 0.2669 0.0111 0.0517 -0.0132 964 HOH A O 6131 O O . HOH T . ? 0.2711 0.2720 0.2869 0.0042 -0.0194 -0.0028 965 HOH A O 6132 O O . HOH T . ? 0.2576 0.2772 0.1994 0.0815 -0.0067 -0.0199 966 HOH A O 6133 O O . HOH T . ? 0.2734 0.2748 0.2235 0.0681 0.0140 -0.0473 967 HOH A O 6134 O O . HOH T . ? 0.2058 0.2421 0.3539 -0.0031 0.0593 -0.0269 968 HOH A O 6135 O O . HOH T . ? 0.3068 0.2900 0.3060 -0.0270 -0.1086 0.0341 969 HOH A O 6136 O O . HOH T . ? 0.2587 0.2259 0.3211 0.0053 0.0154 0.0070 970 HOH A O 6137 O O . HOH T . ? 0.3722 0.2420 0.2839 0.0579 0.0732 0.0037 971 HOH A O 6138 O O . HOH T . ? 0.3358 0.2872 0.2438 0.0563 -0.0024 -0.0305 972 HOH A O 6139 O O . HOH T . ? 0.2536 0.2415 0.3093 0.0124 0.0000 -0.0175 973 HOH A O 6140 O O . HOH T . ? 0.2036 0.2542 0.2711 -0.0454 -0.0346 -0.0190 974 HOH A O 6141 O O . HOH T . ? 0.2762 0.2332 0.2769 0.0921 0.0389 -0.0572 975 HOH A O 6142 O O . HOH T . ? 0.3499 0.4267 0.3355 0.0694 -0.1297 -0.0766 976 HOH A O 6143 O O . HOH T . ? 0.2150 0.3640 0.4369 0.0445 -0.0461 -0.0554 977 HOH A O 6144 O O . HOH T . ? 0.2236 0.2638 0.3296 0.0589 0.0289 -0.0291 978 HOH A O 6145 O O . HOH T . ? 0.2870 0.2602 0.2912 0.0579 0.0229 0.0269 979 HOH A O 6146 O O . HOH T . ? 0.4353 0.2723 0.1980 0.0269 -0.0870 -0.0322 980 HOH A O 6147 O O . HOH T . ? 0.2996 0.2790 0.3177 0.0193 0.0774 -0.0336 981 HOH A O 6148 O O . HOH T . ? 0.3361 0.3169 0.2666 0.0538 -0.0116 0.0209 982 HOH A O 6149 O O . HOH T . ? 0.2979 0.2585 0.3045 0.0041 0.0375 -0.0789 983 HOH A O 6150 O O . HOH T . ? 0.2880 0.2492 0.2818 0.0535 0.0169 0.0008 984 HOH A O 6151 O O . HOH T . ? 0.3039 0.3284 0.3832 0.0844 -0.0091 -0.0426 985 HOH A O 6152 O O . HOH T . ? 0.3014 0.2470 0.2846 0.0553 -0.0558 -0.0567 986 HOH A O 6153 O O . HOH T . ? 0.3687 0.3118 0.3039 -0.0793 0.0109 -0.0082 987 HOH A O 6154 O O . HOH T . ? 0.3266 0.2641 0.3046 0.0504 0.0016 -0.0144 988 HOH A O 6155 O O . HOH T . ? 0.3043 0.2719 0.2767 0.0417 -0.0763 -0.0170 989 HOH A O 6156 O O . HOH T . ? 0.2379 0.2955 0.3803 0.0234 0.0307 -0.0791 990 HOH A O 6157 O O . HOH T . ? 0.2418 0.2867 0.2828 0.0492 -0.0640 -0.0035 991 HOH A O 6158 O O . HOH T . ? 0.3403 0.3446 0.3963 0.1061 -0.0877 -0.1222 992 HOH A O 6159 O O . HOH T . ? 0.2557 0.2386 0.2791 -0.0264 -0.0070 0.0092 993 HOH A O 6160 O O . HOH T . ? 0.2590 0.2564 0.2459 -0.0290 -0.0153 -0.0176 994 HOH A O 6161 O O . HOH T . ? 0.3607 0.4102 0.2812 0.1351 -0.0470 0.0491 995 HOH A O 6162 O O . HOH T . ? 0.2200 0.3582 0.4163 0.0173 -0.0603 0.0440 996 HOH A O 6163 O O . HOH T . ? 0.2049 0.2594 0.2701 0.0353 -0.0215 0.0011 997 HOH A O 6164 O O . HOH T . ? 0.4107 0.3748 0.2966 0.1490 -0.0510 0.0107 998 HOH A O 6165 O O . HOH T . ? 0.4361 0.2901 0.2236 0.1325 -0.0747 -0.0583 999 HOH A O 6166 O O . HOH T . ? 0.3474 0.3483 0.1971 0.0876 -0.0046 -0.0111 1000 HOH A O 6167 O O . HOH T . ? 0.4886 0.3613 0.3028 0.1417 -0.1018 0.0236 1001 HOH A O 6168 O O . HOH T . ? 0.4498 0.3038 0.2290 -0.0312 -0.0349 0.0015 1002 HOH A O 6169 O O . HOH T . ? 0.3660 0.3623 0.2864 0.0336 -0.0565 0.0098 1003 HOH A O 6170 O O . HOH T . ? 0.2682 0.3551 0.3787 -0.0030 0.0711 0.0500 1004 HOH A O 6171 O O . HOH T . ? 0.3807 0.3393 0.2777 0.1098 0.0561 -0.0071 1005 HOH A O 6172 O O . HOH T . ? 0.2811 0.2331 0.2930 0.0034 0.0561 -0.0089 1006 HOH A O 6173 O O . HOH T . ? 0.2648 0.2946 0.1948 0.0461 0.0108 -0.0093 1007 HOH A O 6174 O O . HOH T . ? 0.2172 0.2317 0.3783 -0.0026 0.0167 -0.0136 1008 HOH A O 6175 O O . HOH T . ? 0.0309 0.2397 0.0380 0.0088 0.0056 0.0465 1009 HOH A O 6176 O O . HOH T . ? 0.2761 0.3107 0.4218 0.0182 -0.0195 -0.0903 1010 HOH A O 6177 O O . HOH T . ? 0.2167 0.3625 0.3804 -0.0548 -0.0311 -0.0752 1011 HOH A O 6178 O O . HOH T . ? 0.3439 0.4661 0.2833 0.2091 -0.0285 -0.1151 1012 HOH A O 6179 O O . HOH T . ? 0.2768 0.2388 0.3810 0.0582 0.0361 -0.0643 1013 HOH A O 6180 O O . HOH T . ? 0.3655 0.3025 0.2681 0.0639 0.1059 -0.0010 1014 HOH A O 6181 O O . HOH T . ? 0.3645 0.4951 0.2711 -0.0418 -0.0260 0.0705 1015 HOH A O 6182 O O . HOH T . ? 0.2729 0.3294 0.3527 -0.0281 -0.0490 -0.0923 1016 HOH A O 6183 O O . HOH T . ? 0.3220 0.3210 0.2897 -0.0218 -0.0057 -0.0129 1017 HOH A O 6184 O O . HOH T . ? 0.3329 0.2683 0.3359 -0.0430 0.0835 0.0148 1018 HOH A O 6185 O O . HOH T . ? 0.2610 0.2492 0.4018 0.0235 0.0334 -0.0420 1019 HOH A O 6186 O O . HOH T . ? 0.3483 0.3343 0.3077 0.0206 -0.0019 -0.0665 1020 HOH A O 6187 O O . HOH T . ? 0.3530 0.3771 0.3685 0.0711 -0.0943 -0.1066 1021 HOH A O 6188 O O . HOH T . ? 0.3422 0.3341 0.3506 0.1012 -0.0817 -0.0067 1022 HOH A O 6189 O O . HOH T . ? 0.3511 0.2652 0.2946 -0.0991 0.0109 -0.0511 1023 HOH A O 6190 O O . HOH T . ? 0.4207 0.3378 0.2739 -0.0099 -0.0069 -0.1406 1024 HOH A O 6191 O O . HOH T . ? 0.4386 0.3260 0.2804 0.0702 -0.0929 0.0004 1025 HOH A O 6192 O O . HOH T . ? 0.3353 0.3765 0.3825 0.1269 -0.0716 -0.0411 1026 HOH A O 6193 O O . HOH T . ? 0.3639 0.2623 0.4100 0.0105 -0.0340 0.1333 1027 HOH A O 6194 O O . HOH T . ? 0.4599 0.3712 0.2976 0.0709 -0.0146 0.0809 1028 HOH A O 6195 O O . HOH T . ? 0.2405 0.2316 0.2699 -0.0103 0.0123 -0.0228 1029 HOH A O 6196 O O . HOH T . ? 0.3282 0.2637 0.3112 -0.0184 0.0377 -0.0375 1030 HOH A O 6197 O O . HOH T . ? 0.2441 0.2906 0.3064 0.0077 0.0004 -0.0736 1031 HOH A O 6198 O O . HOH T . ? 0.2425 0.2936 0.2262 0.0066 -0.0494 0.0629 1032 HOH A O 6199 O O . HOH T . ? 0.4686 0.2477 0.3664 0.0634 0.1554 0.0495 1033 HOH A O 6200 O O . HOH T . ? 0.2312 0.2644 0.3571 -0.0109 0.0489 -0.0702 1034 HOH A O 6201 O O . HOH T . ? 0.4325 0.5644 0.6374 0.2076 -0.1942 -0.1828 1035 HOH A O 6202 O O . HOH T . ? 0.4160 0.2997 0.2748 -0.0513 0.0303 0.0002 1036 HOH A O 6203 O O . HOH T . ? 0.3081 0.3571 0.4027 0.0474 -0.0009 -0.0861 1037 HOH A O 6204 O O . HOH T . ? 0.2484 0.3500 0.4568 -0.0302 0.0232 -0.0163 1038 HOH A O 6205 O O . HOH T . ? 0.4048 0.3313 0.3824 0.1133 0.0810 -0.0436 1039 HOH A O 6206 O O . HOH T . ? 0.2078 0.4162 0.3531 0.0162 -0.0168 0.0654 1040 HOH A O 6207 O O . HOH T . ? 0.3902 0.4907 0.2108 0.0956 -0.0439 0.0335 1041 HOH A O 6208 O O . HOH T . ? 0.4842 0.3641 0.3147 0.0887 0.0446 0.0496 1042 HOH A O 6209 O O . HOH T . ? 0.3499 0.2493 0.3058 0.0203 0.0005 -0.0551 1043 HOH A O 6210 O O . HOH T . ? 0.2855 0.2760 0.3723 -0.0043 0.0220 0.0164 1044 HOH A O 6211 O O . HOH T . ? 0.3436 0.3277 0.2941 0.0112 0.0464 -0.0141 1045 HOH A O 6212 O O . HOH T . ? 0.1757 0.4015 0.4130 0.0325 -0.0953 -0.0100 1046 HOH A O 6213 O O . HOH T . ? 0.3018 0.5677 0.4490 -0.0386 -0.0401 -0.2059 1047 HOH A O 6214 O O . HOH T . ? 0.3924 0.3351 0.3024 0.0841 -0.0721 -0.0285 1048 HOH A O 6215 O O . HOH T . ? 0.3673 0.3132 0.4780 -0.0761 0.0155 -0.0515 1049 HOH A O 6216 O O . HOH T . ? 0.2138 0.3186 0.5348 0.0292 -0.0810 0.1210 1050 HOH A O 6217 O O . HOH T . ? 0.3293 0.2846 0.3687 0.0386 0.0247 -0.0966 1051 HOH A O 6218 O O . HOH T . ? 0.4639 0.3456 0.4048 -0.0219 -0.1046 -0.1101 1052 HOH A O 6219 O O . HOH T . ? 0.3235 0.4199 0.7529 0.0291 -0.1264 -0.1534 1053 HOH A O 6220 O O . HOH T . ? 0.5355 0.4908 0.3214 0.1526 0.0126 -0.0167 1054 HOH A O 6221 O O . HOH T . ? 0.3838 0.3066 0.4394 -0.0096 -0.0286 -0.1650 1055 HOH A O 6222 O O . HOH T . ? 0.4848 0.3605 0.1925 0.1332 -0.0134 -0.0119 1056 HOH A O 6223 O O . HOH T . ? 0.3886 0.3138 0.3320 -0.0164 0.0933 -0.0242 1057 HOH A O 6224 O O . HOH T . ? 0.3761 0.3191 0.5318 -0.0727 -0.0571 -0.0569 1058 HOH A O 6225 O O . HOH T . ? 0.4823 0.3799 0.6322 -0.0514 0.0389 -0.0267 1059 HOH A O 6226 O O . HOH T . ? 0.2465 0.2833 0.3980 0.0330 0.0505 0.0137 1060 HOH A O 6227 O O . HOH T . ? 0.3505 0.3035 0.2885 -0.0058 0.0308 -0.0535 1061 HOH A O 6228 O O . HOH T . ? 0.3353 0.3541 0.7177 0.0323 0.0692 0.0039 1062 HOH A O 6229 O O . HOH T . ? 0.5602 0.3411 0.1335 0.1571 -0.0102 -0.0598 1063 HOH A O 6230 O O . HOH T . ? 0.4679 0.3546 0.4241 -0.0973 -0.0181 -0.0811 1064 HOH A O 6231 O O . HOH T . ? 0.3286 0.4624 0.4325 -0.0047 0.0779 -0.0141 1065 HOH A O 6232 O O . HOH T . ? 0.3269 0.3870 0.4210 -0.0575 -0.0153 -0.0962 1066 HOH A O 6233 O O . HOH T . ? 0.2230 0.2195 0.2379 0.0149 0.0236 -0.0173 1067 HOH A O 6234 O O . HOH T . ? 0.2498 0.2898 0.2384 0.0410 0.0130 -0.0033 1068 HOH A O 6235 O O . HOH T . ? 0.3794 0.3640 0.3428 0.0524 0.0272 -0.0632 1069 HOH A O 6236 O O . HOH T . ? 0.4218 0.3944 0.5278 -0.0155 0.2096 -0.0288 1070 HOH A O 6237 O O . HOH T . ? 0.3730 0.3716 0.3701 0.0282 0.0561 -0.0747 1071 HOH A O 6238 O O . HOH T . ? 0.2967 0.3402 0.3299 -0.0363 0.0364 0.0000 1072 HOH A O 6239 O O . HOH T . ? 0.6403 0.4411 0.5110 -0.1252 -0.2082 -0.0754 1073 HOH A O 6240 O O . HOH T . ? 0.2090 0.3159 0.5160 -0.0158 -0.0215 0.0862 1074 HOH A O 6241 O O . HOH T . ? 0.6044 0.3591 0.4399 0.0934 0.0531 0.0056 1075 HOH A O 6242 O O . HOH T . ? 0.3738 0.4531 0.5345 -0.0841 0.0614 0.0645 1076 HOH A O 6243 O O . HOH T . ? 0.2804 0.3119 0.2801 0.0662 0.0461 -0.0572 1077 HOH A O 6244 O O . HOH T . ? 0.3218 0.3239 0.4284 -0.0508 0.0913 -0.0921 1078 HOH A O 6245 O O . HOH T . ? 0.5496 0.6106 0.3335 0.0327 0.0511 0.0332 1079 HOH A O 6246 O O . HOH T . ? 0.2645 0.2953 0.3139 0.0324 0.0079 -0.0351 1080 HOH A O 6247 O O . HOH T . ? 0.3594 0.3562 0.3497 0.0955 -0.1277 -0.0200 1081 HOH A O 6248 O O . HOH T . ? 0.6213 0.3582 0.3600 0.1238 -0.0711 -0.0610 1082 HOH A O 6249 O O . HOH T . ? 0.7280 0.2957 0.4407 -0.1051 0.0064 -0.0186 1083 HOH A O 6250 O O . HOH T . ? 0.3311 0.3881 0.4080 0.0736 0.0235 -0.0642 1084 HOH A O 6251 O O . HOH T . ? 0.4467 0.2933 0.3581 -0.0152 0.0819 -0.0911 1085 HOH A O 6252 O O . HOH T . ? 0.3254 0.3520 0.3540 0.0040 -0.0421 0.0513 1086 HOH A O 6253 O O . HOH T . ? 0.3486 0.3460 0.3329 0.0321 0.0358 -0.1204 1087 HOH A O 6254 O O . HOH T . ? 0.2523 0.4152 0.2827 -0.0714 -0.0152 -0.0737 1088 HOH A O 6255 O O . HOH T . ? 0.3042 0.3994 0.6202 -0.1147 -0.0204 0.0154 1089 HOH A O 6256 O O . HOH T . ? 0.4187 0.3513 0.4627 0.0489 0.0993 -0.0061 1090 HOH A O 6257 O O . HOH T . ? 0.3261 0.3311 0.3260 -0.0283 0.0198 0.0259 1091 HOH A O 6258 O O . HOH T . ? 0.3157 0.4124 0.4100 0.0356 -0.0577 -0.1410 1092 HOH A O 6259 O O . HOH T . ? 0.3254 0.4008 0.4510 0.0730 -0.0978 -0.0702 1093 HOH A O 6260 O O . HOH T . ? 0.2922 0.4170 0.4377 -0.0525 -0.0689 -0.0626 1094 HOH A O 6261 O O . HOH T . ? 0.3185 0.3945 0.3128 -0.0709 0.0598 -0.0087 1095 HOH A O 6262 O O . HOH T . ? 0.5632 0.3560 0.3422 0.0968 -0.1775 -0.0645 1096 HOH A O 6263 O O . HOH T . ? 0.4641 0.4122 0.3237 0.1078 -0.1727 -0.1079 1097 HOH A O 6264 O O . HOH T . ? 0.2036 0.3734 0.3196 -0.0039 0.0301 0.0286 1098 HOH A O 6265 O O . HOH T . ? 0.3314 0.5187 0.4607 0.1870 0.0046 -0.0468 1099 HOH A O 6266 O O . HOH T . ? 0.3048 0.4592 0.9293 0.1415 0.1720 0.1196 1100 HOH A O 6267 O O . HOH T . ? 0.2506 0.4764 0.6134 -0.0917 -0.1181 0.1671 1101 HOH A O 6268 O O . HOH T . ? 0.3815 0.4899 0.4080 -0.1382 -0.0488 -0.1147 1102 HOH A O 6269 O O . HOH T . ? 0.3776 0.4131 0.5263 0.0017 0.1552 0.0232 1103 HOH A O 6270 O O . HOH T . ? 0.4627 0.5618 0.3151 -0.0133 0.1860 0.0797 1104 HOH A O 6271 O O . HOH T . ? 0.3649 0.3560 0.3982 -0.0110 0.1197 0.0899 1105 HOH A O 6272 O O . HOH T . ? 0.4665 0.3444 0.4301 -0.0133 -0.0451 -0.1257 1106 HOH A O 6273 O O . HOH T . ? 0.3582 0.2785 0.3536 0.0233 0.0342 -0.0122 1107 HOH A O 6274 O O . HOH T . ? 0.3200 0.4797 0.3161 0.0436 -0.0749 0.0233 1108 HOH A O 6275 O O . HOH T . ? 0.3557 0.3941 0.4355 0.1242 0.0036 -0.0275 1109 HOH A O 6276 O O . HOH T . ? 0.5493 0.5803 0.2845 0.1361 0.1347 -0.0101 1110 HOH A O 6277 O O A HOH T . ? 0.2656 0.5388 0.3225 -0.1524 0.0531 0.1301 1111 HOH A O 6278 O O B HOH T . ? 0.1998 0.3617 0.5818 0.0050 0.1194 -0.0736 1111 HOH A O 6279 O O . HOH T . ? 0.3621 0.7081 0.5211 0.1239 0.0656 0.2901 1112 HOH A O 6280 O O . HOH T . ? 0.2434 0.2886 0.2187 0.0319 -0.0008 -0.0339 1113 HOH A O 6281 O O . HOH T . ? 0.3758 0.5267 0.4938 0.1722 0.0232 0.0351 1114 HOH A O 6282 O O . HOH T . ? 0.2696 0.5503 0.2805 -0.0552 -0.0611 -0.1251 1115 HOH A O 6283 O O . HOH T . ? 0.2775 0.4697 0.4930 -0.0842 -0.1579 0.0226 1116 HOH A O 6284 O O . HOH T . ? 0.4870 0.3194 0.4396 -0.0432 0.0005 0.0162 1117 HOH A O 6285 O O . HOH T . ? 0.1964 0.1856 0.2118 0.0316 0.0022 -0.0033 1118 HOH A O 6286 O O . HOH T . ? 0.2897 0.5037 0.5209 -0.0449 0.1007 -0.0371 1119 HOH A O 6287 O O . HOH T . ? 0.3055 0.4844 0.4320 -0.0278 0.0916 -0.0716 1120 HOH A O 6288 O O . HOH T . ? 0.2762 0.4408 0.4077 -0.0644 0.1004 -0.0945 1121 HOH A O 6289 O O . HOH T . ? 0.4296 0.3791 0.3437 -0.0113 -0.0343 -0.1099 1122 HOH A O 6290 O O . HOH T . ? 0.3402 0.5722 0.3853 -0.0227 -0.0585 -0.1774 1123 HOH A O 6291 O O . HOH T . ? 0.3817 0.3598 0.3688 -0.0214 -0.0813 0.0644 1124 HOH A O 6292 O O . HOH T . ? 0.4334 0.5364 0.4849 0.1747 0.0876 -0.1010 1125 HOH A O 6293 O O . HOH T . ? 0.2145 0.3704 0.2784 0.0226 0.0522 0.0363 1126 HOH A O 6294 O O . HOH T . ? 0.4492 0.2851 0.6094 0.0539 -0.1424 0.0645 1127 HOH A O 6295 O O . HOH T . ? 0.6065 0.4590 0.3383 0.0605 -0.0093 0.0953 1128 HOH A O 6296 O O . HOH T . ? 0.9194 0.4293 0.2987 0.2758 -0.1397 -0.0812 1129 HOH A O 6297 O O . HOH T . ? 0.3573 0.3739 0.5131 -0.0288 -0.0947 -0.0309 1130 HOH A O 6298 O O . HOH T . ? 0.5422 0.3940 0.3227 0.1588 0.0415 0.0353 1131 HOH A O 6299 O O . HOH T . ? 0.3749 0.4010 0.3960 0.0116 0.0315 0.0138 1132 HOH A O 6300 O O . HOH T . ? 0.3040 0.3633 0.3636 -0.0274 -0.0276 -0.0122 1133 HOH A O 6301 O O . HOH T . ? 0.4884 0.3766 0.3893 0.1427 -0.1186 -0.0143 1134 HOH A O 6302 O O . HOH T . ? 0.3483 0.4643 0.5090 0.0338 0.0490 -0.0069 1135 HOH A O 6303 O O . HOH T . ? 0.4427 0.3569 0.3938 -0.0273 0.0994 0.0944 1136 HOH A O 6304 O O . HOH T . ? 0.5814 0.4620 0.3212 0.0251 0.0466 0.0317 1137 HOH A O 6305 O O . HOH T . ? 0.4489 0.5179 0.3130 0.0090 0.0634 -0.0540 1138 HOH A O 6306 O O . HOH T . ? 0.3957 0.6645 0.4604 0.0447 -0.1190 -0.0198 1139 HOH A O 6307 O O . HOH T . ? 0.2809 0.3816 0.4561 -0.0541 0.0579 0.0308 1140 HOH A O 6308 O O . HOH T . ? 0.4169 0.7765 0.5455 0.0579 0.0439 0.0446 1141 HOH A O 6309 O O . HOH T . ? 0.3258 0.2755 0.8192 -0.0568 0.0766 -0.0451 1142 HOH A O 6310 O O . HOH T . ? 0.3157 0.4855 0.4841 -0.0036 -0.0241 0.0033 1143 HOH A O 6311 O O . HOH T . ? 0.2165 0.2205 0.2203 0.0073 -0.0046 -0.0264 1144 HOH A O 6312 O O . HOH T . ? 0.4251 0.3396 0.3336 0.0683 0.0606 -0.1316 1145 HOH A O 6313 O O . HOH T . ? 0.3112 0.3185 0.2655 -0.0613 0.1033 0.0170 1146 HOH A O 6314 O O . HOH T . ? 0.3356 0.5957 0.2786 0.0304 -0.0256 -0.0038 1147 HOH A O 6315 O O . HOH T . ? 0.3500 0.3575 0.4240 0.0081 0.1279 0.0076 1148 HOH A O 6316 O O . HOH T . ? 0.3353 0.5962 0.4576 0.0437 0.0928 -0.0949 1149 HOH A O 6317 O O . HOH T . ? 0.4143 0.5776 0.5595 -0.0008 -0.0090 -0.1899 1150 HOH A O 6318 O O . HOH T . ? 0.4918 0.3074 0.5629 -0.1005 0.1482 0.0303 1151 HOH A O 6319 O O A HOH T . ? 0.2578 0.3798 0.4336 0.0049 -0.0678 0.1259 1152 HOH A O 6320 O O B HOH T . ? 0.2517 0.3467 0.4325 0.1472 -0.0122 0.0290 1152 HOH A O 6321 O O . HOH T . ? 0.5619 0.5354 0.4618 0.0331 0.1800 0.0754 1153 HOH A O 6322 O O . HOH T . ? 0.3837 0.5629 0.6128 0.0187 0.0841 -0.0011 1154 HOH A O 6323 O O . HOH T . ? 0.4059 0.5211 0.4879 0.0051 0.0101 -0.0779 1155 HOH A O 6324 O O . HOH T . ? 0.4824 0.3382 0.3336 -0.0729 0.0326 0.0313 1156 HOH A O 6325 O O . HOH T . ? 0.4261 0.3797 0.4827 -0.0375 0.1155 0.0787 1157 HOH A O 6326 O O . HOH T . ? 0.4616 0.4508 0.5029 0.0207 0.1320 -0.0827 1158 HOH A O 6327 O O . HOH T . ? 0.4182 0.2928 0.4286 -0.0156 0.0996 -0.0588 1159 HOH A O 6328 O O . HOH T . ? 0.4262 0.4093 0.4351 0.1578 -0.0635 0.0582 1160 HOH A O 6329 O O . HOH T . ? 0.5908 0.3925 0.5149 -0.0565 -0.0661 0.0334 1161 HOH A O 6330 O O . HOH T . ? 0.3224 0.4011 0.0823 0.0781 0.0000 0.0452 1162 HOH A O 6331 O O . HOH T . ? 0.2328 0.2224 0.2062 0.0030 0.0033 -0.0133 1163 HOH A O 6332 O O . HOH T . ? 0.3968 0.4751 0.4140 -0.0778 0.1450 -0.1341 1164 HOH A O 6333 O O . HOH T . ? 0.4445 0.4662 0.3208 -0.0774 -0.0945 0.1817 1165 HOH A O 6334 O O . HOH T . ? 0.4525 0.5766 0.5713 -0.0245 -0.1663 -0.0806 1166 HOH A O 6335 O O . HOH T . ? 0.5060 0.6038 0.3946 -0.0238 -0.1238 -0.0107 1167 HOH A O 6336 O O . HOH T . ? 0.3904 0.4065 0.5364 -0.0143 0.0237 -0.1327 1168 HOH A O 6337 O O . HOH T . ? 0.5173 0.3525 0.3890 0.0556 0.0694 0.0973 1169 HOH A O 6338 O O . HOH T . ? 0.4857 0.4060 0.4291 0.0518 0.0111 0.1122 1170 HOH A O 6339 O O . HOH T . ? 0.5506 0.5231 0.2611 0.1100 -0.0374 0.0715 1171 HOH A O 6340 O O . HOH T . ? 0.6271 0.5375 0.2457 0.0376 -0.1017 -0.0107 1172 HOH A O 6341 O O . HOH T . ? 0.2800 0.2922 0.2160 -0.0367 0.0244 -0.0374 1173 HOH A O 6342 O O . HOH T . ? 0.3585 0.3197 0.3645 0.0052 0.0402 -0.0165 1174 HOH A O 6343 O O . HOH T . ? 0.3143 0.5167 0.4734 -0.0053 -0.0241 0.0156 1175 HOH A O 6344 O O . HOH T . ? 0.5650 0.4084 0.3610 0.0299 0.0002 0.0199 1176 HOH A O 6345 O O . HOH T . ? 0.5551 0.5281 0.2829 0.1740 -0.0830 -0.0553 1177 HOH A O 6346 O O . HOH T . ? 0.5704 0.5597 0.4016 0.1312 -0.1685 -0.0310 1178 HOH A O 6347 O O . HOH T . ? 0.2785 0.3921 0.4201 -0.1153 -0.0645 0.0824 1179 HOH A O 6348 O O . HOH T . ? 0.4746 0.6025 0.3014 0.0055 0.0921 -0.0068 1180 HOH A O 6349 O O . HOH T . ? 0.5215 0.4183 0.4904 -0.0947 -0.0006 0.0304 1181 HOH A O 6350 O O . HOH T . ? 0.3762 0.3804 0.3218 0.0013 0.0276 -0.0579 1182 HOH A O 6351 O O . HOH T . ? 0.2390 0.3721 0.4155 -0.1149 0.0395 -0.1555 1183 HOH A O 6352 O O . HOH T . ? 0.7364 0.2818 0.4225 0.0457 -0.0311 0.0388 1184 HOH A O 6353 O O . HOH T . ? 0.4455 0.4117 0.4134 -0.0044 -0.0225 0.0515 1185 HOH A O 6354 O O . HOH T . ? 0.1592 0.4844 0.3245 -0.0727 -0.0091 -0.1473 1186 HOH A O 6355 O O . HOH T . ? 0.4350 0.5610 0.2920 0.0937 -0.0104 -0.0895 1187 HOH A O 6356 O O . HOH T . ? 0.4460 0.6862 0.4680 0.1616 -0.0840 -0.0778 1188 HOH A O 6357 O O . HOH T . ? 0.2383 0.1887 0.4160 -0.0221 -0.2177 -0.0305 1189 HOH A O 6358 O O . HOH T . ? 0.3452 0.5405 0.3982 0.0142 -0.0511 0.0250 1190 HOH A O 6359 O O . HOH T . ? 0.2296 0.1957 0.3164 0.1035 0.0338 0.0375 1191 HOH A O 6360 O O . HOH T . ? 0.3665 0.4508 0.5652 0.0028 0.1564 0.0496 1192 HOH A O 6361 O O . HOH T . ? 0.3801 0.4194 0.6639 -0.0410 -0.0415 -0.0092 1193 HOH A O 6362 O O . HOH T . ? 0.5416 0.3280 0.3025 -0.0421 -0.1054 -0.0040 1194 HOH A O 6363 O O . HOH T . ? 0.6014 0.5614 0.4068 0.3029 0.1225 -0.0347 1195 HOH A O 6364 O O . HOH T . ? 0.5117 0.4800 0.4789 0.0614 0.0898 -0.1198 1196 HOH A O 6365 O O . HOH T . ? 0.3496 0.3507 0.4140 0.0478 0.0145 0.1085 1197 HOH A O 6366 O O . HOH T . ? 0.4203 0.4420 0.3499 0.1343 -0.0069 -0.0927 1198 HOH A O 6367 O O . HOH T . ? 0.5764 0.4602 0.4458 0.0066 -0.0764 -0.0217 1199 HOH A O 6368 O O . HOH T . ? 0.4865 0.3777 0.9181 -0.0499 -0.2476 -0.1850 1200 HOH A O 6369 O O . HOH T . ? 0.3405 0.1304 0.5983 -0.0318 0.0808 -0.1191 1201 HOH A O 6370 O O . HOH T . ? 0.4532 0.4788 0.5424 -0.1238 -0.1310 -0.0111 1202 HOH A O 6371 O O . HOH T . ? 0.3599 0.3468 0.1898 0.0065 0.0400 -0.0070 1203 HOH A O 6372 O O . HOH T . ? 0.5520 0.4866 0.5084 -0.0728 -0.1142 -0.1146 1204 HOH A O 6373 O O . HOH T . ? 0.1548 0.2831 0.4169 -0.0331 -0.0167 -0.0709 1205 HOH A O 6374 O O . HOH T . ? 0.2419 0.3563 0.3497 0.0130 -0.1151 -0.0730 1206 HOH A O 6375 O O . HOH T . ? 0.2844 0.6291 0.5952 -0.0938 -0.0073 -0.1054 1207 HOH A O 6376 O O . HOH T . ? 0.3652 0.3072 0.3299 0.1140 -0.1576 -0.1112 1208 HOH A O 6377 O O . HOH T . ? 0.4435 0.4268 0.3460 0.0726 0.0571 -0.0107 1209 HOH A O 6378 O O . HOH T . ? 0.5617 0.3273 0.4294 -0.0051 -0.0232 -0.0527 1210 HOH A O 6379 O O . HOH T . ? 0.5484 0.4293 0.4535 -0.0644 0.0192 -0.0891 1211 HOH A O 6380 O O . HOH T . ? 0.4185 0.4104 0.3546 0.0260 0.0597 0.0518 1212 HOH A O 6381 O O . HOH T . ? 0.4241 0.3719 0.5449 -0.0176 0.1053 -0.0051 1213 HOH A O 6382 O O . HOH T . ? 0.4028 0.3901 0.5060 0.0344 0.1722 0.0419 1214 HOH A O 6383 O O . HOH T . ? 0.2467 0.4476 0.3571 -0.0051 0.0776 -0.0475 1215 HOH A O 6384 O O . HOH T . ? 0.3856 0.4367 0.6723 0.1106 0.0653 0.0173 1216 HOH A O 6385 O O . HOH T . ? 0.2905 0.6511 0.7742 0.0680 0.1259 -0.1684 1217 HOH A O 6386 O O . HOH T . ? 0.5143 0.3441 0.3182 0.0230 0.1141 0.0099 1218 HOH A O 6387 O O . HOH T . ? 0.3241 0.3392 0.3948 0.0932 -0.0988 0.0871 1219 HOH A O 6388 O O . HOH T . ? 0.3843 0.6048 0.4852 0.2353 -0.1146 0.0777 1220 HOH A O 6389 O O . HOH T . ? 0.5184 0.4579 0.4163 0.1059 -0.1540 -0.1286 1221 HOH A O 6390 O O . HOH T . ? 0.2727 0.3306 0.1575 -0.1637 0.0380 -0.0044 1222 HOH A O 6391 O O . HOH T . ? 0.1240 0.2846 0.4494 -0.0430 0.0613 -0.0338 1223 HOH A O 6392 O O . HOH T . ? 0.6506 0.4805 0.3430 -0.1758 0.0296 -0.0360 1224 HOH A O 6393 O O . HOH T . ? 0.4258 0.3949 0.3879 0.0725 0.0246 -0.0106 1225 HOH A O 6394 O O . HOH T . ? 0.5058 0.5544 0.4120 0.0214 -0.0906 -0.1454 1226 HOH A O 6395 O O . HOH T . ? 0.4512 0.4470 0.6273 -0.0301 0.1610 -0.0190 1227 HOH A O 6396 O O . HOH T . ? 0.5200 0.5768 0.5096 0.2082 -0.1534 -0.1278 1228 HOH A O 6397 O O . HOH T . ? 0.4466 0.4104 0.4748 -0.0807 -0.0122 0.1478 1229 HOH A O 6398 O O . HOH T . ? 0.3542 0.4190 0.3060 -0.0001 0.0157 0.0136 1230 HOH A O 6399 O O . HOH T . ? 0.4968 0.5188 0.3270 -0.1065 0.0610 0.0163 1231 HOH A O 6400 O O . HOH T . ? 0.3601 0.3764 0.2708 0.0729 -0.0048 0.0116 1232 HOH A O 6401 O O . HOH T . ? 0.6678 0.5211 0.5180 -0.0466 -0.0660 -0.0990 1233 HOH A O 6402 O O . HOH T . ? 0.4555 0.4426 0.4707 0.0390 -0.0777 0.0380 1234 HOH A O 6403 O O . HOH T . ? 0.8801 0.5794 0.3259 0.2100 -0.0106 -0.1219 1235 HOH A O 6404 O O . HOH T . ? 0.3678 0.5154 0.6219 0.0604 0.0482 0.0746 1236 HOH A O 6405 O O . HOH T . ? 0.5337 0.4334 0.4667 0.1033 -0.1795 -0.0070 1237 HOH A O 6406 O O . HOH T . ? 0.4207 0.3835 0.5058 -0.0127 0.0858 0.0044 1238 HOH A O 6407 O O . HOH T . ? 0.4463 0.4124 0.6977 0.0783 -0.2029 -0.0514 1239 HOH A O 6408 O O . HOH T . ? 0.5956 0.4482 0.5350 0.0718 0.0945 0.1021 1240 HOH A O 6409 O O . HOH T . ? 0.4901 0.3752 0.6609 -0.0464 0.0572 -0.0607 1241 HOH A O 6410 O O . HOH T . ? 0.6364 0.5936 0.2678 -0.0736 -0.0671 -0.1401 1242 HOH A O 6411 O O . HOH T . ? 0.6036 0.3804 0.6579 -0.1146 0.1520 -0.0735 1243 HOH A O 6412 O O . HOH T . ? 0.5060 0.7802 0.4982 0.1870 -0.1802 -0.2122 1244 HOH A O 6413 O O . HOH T . ? 0.4907 0.5969 0.4201 0.0673 -0.0873 0.1495 1245 HOH A O 6414 O O . HOH T . ? 0.4739 0.5974 0.6823 0.2632 -0.1812 -0.0094 1246 HOH A O 6415 O O . HOH T . ? 0.6244 0.3827 0.3708 0.0368 -0.0014 -0.0306 1247 HOH A O 6416 O O . HOH T . ? 0.4371 0.4959 0.3710 0.0723 -0.0491 0.0102 1248 HOH A O 6417 O O . HOH T . ? 0.2022 0.5009 0.4254 -0.0906 0.2170 0.0297 1249 HOH A O 6418 O O . HOH T . ? 0.5855 0.3436 0.5421 -0.0328 -0.1649 0.0219 1250 HOH A O 6419 O O . HOH T . ? 0.3657 0.5424 0.6512 0.1559 0.0163 0.0296 1251 HOH A O 6420 O O . HOH T . ? 0.4040 0.4187 0.3605 0.2350 -0.0878 -0.0530 1252 HOH A O 6421 O O . HOH T . ? 0.4009 0.3634 0.3416 -0.0519 -0.0472 0.0682 1253 HOH A O 6422 O O . HOH T . ? 0.3748 0.4138 0.3179 -0.0152 0.0268 0.0877 1254 HOH A O 6423 O O . HOH T . ? 0.2910 0.5772 0.5051 -0.0500 0.0393 0.0446 1255 HOH A O 6424 O O . HOH T . ? 0.5304 0.4358 0.1647 0.1201 0.0315 -0.0084 1256 HOH A O 6425 O O . HOH T . ? 0.6378 0.4089 0.1423 -0.0184 -0.0182 -0.0293 1257 HOH A O 6426 O O . HOH T . ? 0.4206 0.4927 0.5587 0.0184 -0.0054 -0.0357 1258 HOH A O 6427 O O . HOH T . ? 0.3298 0.3373 0.7443 -0.0062 -0.0207 0.0446 1259 HOH A O 6428 O O . HOH T . ? 0.1258 0.3264 0.4636 -0.0632 0.0054 -0.0426 1260 HOH A O 6429 O O . HOH T . ? 0.5519 0.4599 0.4111 0.0420 -0.0299 -0.0329 1261 HOH A O 6430 O O . HOH T . ? 0.2220 0.2725 0.3550 0.0097 0.0080 -0.0373 1262 HOH A O 6431 O O . HOH T . ? 0.4153 0.5617 0.6350 0.0721 -0.1063 -0.0803 1263 HOH A O 6432 O O . HOH T . ? 0.7325 0.3506 0.6283 -0.0230 -0.2476 -0.0125 1264 HOH A O 6433 O O . HOH T . ? 0.6266 0.4654 0.6282 0.1333 0.0920 0.0769 1265 HOH A O 6434 O O . HOH T . ? 0.4796 0.6237 0.7166 0.0613 -0.0618 -0.1640 1266 HOH A O 6435 O O . HOH T . ? 0.2741 0.5204 0.5096 0.0362 0.0145 0.0366 1267 HOH A O 6436 O O . HOH T . ? 0.3600 0.4309 0.5410 0.0418 0.0851 -0.0198 1268 HOH A O 6437 O O . HOH T . ? 0.3106 0.6419 0.8601 0.0046 0.1048 -0.1585 1269 HOH A O 6438 O O . HOH T . ? 0.4358 0.4246 0.4211 0.0868 0.0941 0.0373 1270 HOH A O 6439 O O . HOH T . ? 0.3194 0.3366 0.4266 0.0102 -0.0184 -0.0282 1271 HOH A O 6440 O O . HOH T . ? 0.2813 0.2592 0.3712 0.0006 -0.0117 -0.0158 1272 HOH A O 6441 O O . HOH T . ? 0.3870 0.3879 0.4870 0.1358 -0.0882 -0.0703 1273 HOH A O 6442 O O . HOH T . ? 0.4006 0.6106 0.6724 0.1734 0.1092 -0.1521 1274 HOH A O 6443 O O . HOH T . ? 0.5005 0.8750 0.3192 0.1799 -0.0163 0.0939 1275 HOH A O 6444 O O . HOH T . ? 0.2591 0.5418 0.3498 0.0143 -0.0243 -0.0488 1276 HOH A O 6445 O O . HOH T . ? 0.3340 0.3928 0.3335 0.0112 0.0034 -0.0289 1277 HOH A O 6446 O O . HOH T . ? 0.3890 0.4073 0.6114 -0.1018 0.1227 0.0971 1278 HOH A O 6447 O O . HOH T . ? 0.4365 0.4734 0.2951 0.1120 0.0890 -0.1128 1279 HOH A O 6448 O O . HOH T . ? 0.5132 0.3756 0.4636 0.0485 -0.0138 -0.0904 1280 HOH A O 6449 O O . HOH T . ? 0.5677 0.5283 0.4294 0.1914 -0.0610 0.0120 1281 HOH A O 6450 O O . HOH T . ? 0.5721 0.3530 0.7924 -0.0842 -0.4225 0.1994 1282 HOH A O 6451 O O . HOH T . ? 0.4768 0.5884 0.3610 0.1719 0.0789 -0.0183 1283 HOH A O 6452 O O . HOH T . ? 0.3769 0.4080 0.5369 0.0237 0.0397 0.0030 1284 HOH A O 6453 O O . HOH T . ? 0.2551 0.3786 0.2175 0.1047 -0.1318 0.0148 1285 HOH A O 6454 O O . HOH T . ? 0.2632 0.4754 0.1635 -0.0413 0.0294 -0.0988 1286 HOH A O 6455 O O . HOH T . ? 0.3849 0.5304 0.6040 -0.1281 0.1007 -0.0721 1287 HOH A O 6456 O O . HOH T . ? 0.3734 0.3318 0.4302 0.0000 -0.0110 -0.0667 1288 HOH A O 6457 O O . HOH T . ? 0.6040 0.6213 0.3966 -0.0393 0.0232 -0.2406 1289 HOH A O 6458 O O . HOH T . ? 0.5636 0.5679 0.3716 0.0495 -0.0933 0.0093 1290 HOH A O 6459 O O . HOH T . ? 0.5602 0.3815 0.5994 0.0044 -0.1173 0.1154 1291 HOH A O 6460 O O . HOH T . ? 0.2320 0.5784 0.4260 -0.1371 0.0349 0.0664 1292 HOH A O 6461 O O . HOH T . ? 0.5248 0.4252 0.4414 -0.0386 0.1915 -0.0945 1293 HOH A O 6462 O O . HOH T . ? 0.4387 0.9081 0.5838 -0.3019 -0.1133 0.0352 1294 HOH A O 6463 O O . HOH T . ? 0.2430 0.3262 0.2740 0.0660 -0.1824 -0.2194 1295 HOH A O 6464 O O . HOH T . ? 0.3256 0.6318 0.5964 0.0017 -0.0092 0.2947 1296 HOH A O 6465 O O . HOH T . ? 0.4336 0.4956 0.5548 0.1375 -0.1213 -0.0282 1297 HOH A O 6466 O O A HOH T . ? 0.2742 0.2741 0.3904 -0.0714 -0.0712 0.1191 1298 HOH A O 6467 O O B HOH T . ? 0.3452 0.4390 0.1982 0.0458 0.1298 0.0847 1298 HOH A O 6468 O O . HOH T . ? 0.2180 0.4674 0.5828 0.0774 0.0125 0.1154 1299 HOH A O 6469 O O . HOH T . ? 0.3074 0.5577 0.6785 0.0103 0.0910 -0.1717 1300 HOH A O 6470 O O . HOH T . ? 0.6948 0.4384 0.6791 0.0001 0.2927 0.0985 1301 HOH A O 6471 O O . HOH T . ? 0.3901 0.4646 0.6544 0.0025 -0.0346 -0.0438 1302 HOH A O 6472 O O . HOH T . ? 0.3681 0.4988 0.5800 0.0088 -0.0474 0.0342 1303 HOH A O 6473 O O . HOH T . ? 0.5572 0.7395 0.6281 -0.0838 -0.0797 0.0772 1304 HOH A O 6474 O O . HOH T . ? 0.4774 0.6224 0.4152 0.0119 0.0472 -0.1773 1305 HOH A O 6475 O O . HOH T . ? 0.3794 0.5368 0.5969 0.2628 0.0122 -0.0733 1306 HOH A O 6476 O O . HOH T . ? 0.2797 0.2248 0.2442 0.0095 0.0815 -0.0336 1307 HOH A O 6477 O O . HOH T . ? 0.1376 0.1905 0.2356 -0.0433 -0.0800 -0.0428 1308 HOH A O 6478 O O . HOH T . ? 0.6242 0.4553 1.2286 0.1147 0.2650 -0.0534 1309 HOH A O 6479 O O . HOH T . ? 0.5516 0.5700 0.4370 -0.0506 -0.0601 -0.2220 1310 HOH A O 6480 O O . HOH T . ? 0.4803 0.6244 0.4568 -0.2381 -0.1101 0.0137 1311 HOH A O 6481 O O A HOH T . ? 0.3238 0.2601 0.4516 0.0173 -0.0519 0.0526 1312 HOH A O 6482 O O B HOH T . ? 0.4892 0.3589 0.5090 0.0052 -0.2429 -0.1145 1312 HOH A O 6483 O O . HOH T . ? 0.3430 0.5631 0.4087 0.0817 0.0574 0.0806 1313 HOH A O 6484 O O . HOH T . ? 0.3284 0.5067 0.7203 0.0431 -0.0697 -0.0971 1314 HOH A O 6485 O O . HOH T . ? 0.3826 0.5323 0.7384 0.0013 0.1170 0.0405 1315 HOH A O 6486 O O . HOH T . ? 0.3194 0.6135 0.9587 -0.0736 0.1685 -0.3903 1316 HOH A O 6487 O O . HOH T . ? 0.4016 0.6611 0.5605 0.0944 0.0599 -0.0863 1317 HOH A O 6488 O O . HOH T . ? 0.4637 0.4803 0.4482 0.0907 -0.0254 0.0120 1318 HOH A O 6489 O O . HOH T . ? 0.5407 0.6685 0.5897 0.1129 -0.2003 -0.2459 1319 HOH A O 6490 O O . HOH T . ? 0.4392 0.7481 0.4054 0.1074 0.0610 0.0553 1320 HOH A O 6491 O O . HOH T . ? 0.3253 0.4218 0.6744 0.0703 -0.0750 -0.1458 1321 HOH A O 6492 O O . HOH T . ? 0.6389 0.4697 0.3425 0.1291 0.0722 0.1198 1322 HOH A O 6493 O O . HOH T . ? 0.5055 0.6209 0.5907 0.0877 -0.0388 -0.0819 1323 HOH A O 6494 O O . HOH T . ? 0.5345 0.7171 0.6627 0.1784 0.0827 0.1440 1324 HOH A O 6495 O O . HOH T . ? 0.6777 0.8209 0.6925 -0.1743 0.0884 -0.3226 1325 HOH A O 6496 O O . HOH T . ? 0.4322 0.5472 0.6925 0.1522 -0.1394 0.0056 1326 HOH A O 6497 O O . HOH T . ? 0.5485 0.5009 0.8902 0.0513 -0.0590 -0.1950 1327 HOH A O 6498 O O . HOH T . ? 0.5702 0.4345 0.4256 0.0301 0.1501 -0.0905 1328 HOH A O 6499 O O . HOH T . ? 0.5348 0.5437 0.5674 0.0831 -0.0281 -0.1341 1329 HOH A O 6500 O O . HOH T . ? 0.4274 0.7638 0.6639 0.0590 0.1783 -0.0608 1330 HOH A O 6501 O O . HOH T . ? 0.3499 0.7570 0.3866 0.0318 -0.0272 0.2205 1331 HOH A O 6502 O O . HOH T . ? 0.5315 0.5009 0.4348 0.0534 0.2249 0.0397 1332 HOH A O 6503 O O . HOH T . ? 0.5135 0.4846 0.5003 -0.1030 0.0560 0.0533 1333 HOH A O 6504 O O . HOH T . ? 0.4769 0.3779 0.5566 -0.0673 0.0416 0.0453 1334 HOH A O 6505 O O . HOH T . ? 0.3798 0.8290 0.7212 0.1670 -0.0793 -0.0943 1335 HOH A O 6506 O O . HOH T . ? 0.7134 0.4091 0.4273 0.0052 -0.0141 -0.0020 1336 HOH A O 6507 O O . HOH T . ? 0.4050 0.5175 0.7386 0.0429 -0.1668 0.0263 1337 HOH A O 6508 O O . HOH T . ? 0.3094 0.5228 0.5564 0.1102 -0.0445 -0.0305 1338 HOH A O 6509 O O . HOH T . ? 0.2458 0.1940 0.2275 0.0301 -0.0233 -0.0188 1339 HOH A O 6510 O O . HOH T . ? 0.5193 0.6497 0.3232 0.0381 -0.1808 0.1024 1340 HOH A O 6511 O O . HOH T . ? 0.8300 0.5422 0.1456 -0.0232 0.1138 -0.0165 1341 HOH A O 6512 O O . HOH T . ? 0.8494 0.6132 0.4516 0.1483 -0.1383 0.0740 1342 HOH A O 6513 O O . HOH T . ? 0.4536 0.2848 0.2448 0.0605 0.0467 0.0781 1343 HOH A O 6514 O O . HOH T . ? 0.4909 0.3296 0.2599 -0.0411 -0.0190 0.0075 1344 HOH A O 6515 O O . HOH T . ? 0.5830 0.7728 0.7828 0.0367 -0.1834 0.3167 1345 HOH A O 6516 O O . HOH T . ? 0.4946 0.3207 0.2246 0.0057 -0.0215 0.1217 1346 HOH A O 6517 O O . HOH T . ? 0.2296 0.2094 0.4397 0.0113 0.0455 0.0127 1347 HOH A O 6518 O O . HOH T . ? 0.5409 0.7361 0.2781 -0.0599 0.0460 -0.1913 1348 HOH A O 6519 O O . HOH T . ? 0.6630 0.6721 0.6256 -0.0444 0.1269 -0.0243 1349 HOH A O 6520 O O . HOH T . ? 0.4641 0.5544 0.4323 -0.0184 0.1460 0.1805 1350 HOH A O 6521 O O . HOH T . ? 0.4763 0.4843 0.2577 -0.0909 0.0057 -0.1843 1351 HOH A O 6522 O O . HOH T . ? 0.5805 1.1231 0.6466 0.1721 -0.1121 -0.3561 1352 HOH A O 6523 O O . HOH T . ? 0.4564 0.6200 0.4666 0.0109 -0.0501 -0.0877 1353 HOH A O 6524 O O . HOH T . ? 0.4916 0.5633 0.6206 0.0563 0.0766 -0.2462 1354 HOH A O 6525 O O . HOH T . ? 0.3447 0.4951 0.4637 0.1702 0.0687 -0.1037 1355 HOH A O 6526 O O . HOH T . ? 0.5877 0.1840 0.5718 -0.0142 0.2495 -0.0679 1356 HOH A O 6527 O O . HOH T . ? 0.5162 0.4597 0.5237 -0.0593 -0.1833 -0.0143 1357 HOH A O 6528 O O . HOH T . ? 0.2705 0.4944 0.3842 -0.1371 -0.0022 -0.0006 1358 HOH A O 6529 O O . HOH T . ? 0.4129 0.5653 0.9764 -0.1433 0.1575 0.1341 1359 HOH A O 6530 O O . HOH T . ? 0.5890 0.4121 0.8054 0.1305 0.1770 -0.0835 1360 HOH A O 6531 O O . HOH T . ? 0.7851 0.6619 0.4962 -0.0238 0.1226 -0.2109 1361 HOH A O 6532 O O . HOH T . ? 0.3860 0.5757 0.5850 0.0392 -0.0145 -0.1243 1362 HOH A O 6533 O O . HOH T . ? 0.3505 0.6270 0.7818 0.0407 0.0742 -0.0798 1363 HOH A O 6534 O O . HOH T . ? 0.5632 0.4341 0.5401 -0.1134 0.1143 -0.0715 1364 HOH A O 6535 O O . HOH T . ? 0.3850 0.8244 0.6116 0.1069 -0.1451 0.0693 1365 HOH A O 6536 O O . HOH T . ? 0.5826 0.7248 0.7954 -0.0552 -0.2244 -0.2851 1366 HOH A O 6537 O O . HOH T . ? 0.2482 0.5348 0.5099 0.1296 0.0775 0.0090 1367 HOH A O 6538 O O . HOH T . ? 0.2379 0.4930 0.3306 0.0469 -0.1040 -0.0659 1368 HOH A O 6539 O O . HOH T . ? 0.8482 0.9314 0.4475 0.2741 0.1452 -0.0598 1369 HOH A O 6540 O O . HOH T . ? 0.4577 0.5821 0.5908 -0.1461 -0.1657 0.0847 1370 HOH A O 6541 O O . HOH T . ? 0.4386 0.2976 0.3087 -0.0156 0.1137 0.0519 1371 HOH A O 6542 O O . HOH T . ? 0.3546 0.3866 0.4058 0.0703 -0.1292 0.0023 1372 HOH A O 6543 O O . HOH T . ? 0.3242 0.4509 0.3885 -0.0450 0.0374 -0.0366 1373 HOH A O 6544 O O . HOH T . ? 0.2518 0.5295 0.4398 -0.1120 0.0560 0.1114 1374 HOH A O 6545 O O . HOH T . ? 0.4199 0.5438 0.5795 0.0807 0.1347 0.1924 1375 HOH A O 6546 O O . HOH T . ? 0.5245 0.4842 0.5219 0.1797 -0.1779 -0.1346 1376 HOH A O 6547 O O . HOH T . ? 0.4814 0.5436 0.4735 0.0522 -0.0400 0.0048 1377 HOH A O 6548 O O . HOH T . ? 0.3714 0.2241 0.3849 0.0435 -0.0793 -0.0878 1378 HOH A O 6549 O O . HOH T . ? 0.5013 0.4150 0.4445 -0.0659 -0.0062 -0.1286 1379 HOH A O 6550 O O . HOH T . ? 0.2628 0.3826 0.2855 -0.0726 -0.0444 -0.0082 1380 HOH A O 6551 O O . HOH T . ? 0.3813 0.3987 0.1982 -0.0616 0.0329 -0.0119 1381 HOH A O 6552 O O . HOH T . ? 0.3353 0.4978 0.3356 -0.0459 -0.0366 -0.0579 1382 HOH A O 6553 O O . HOH T . ? 0.3825 0.4267 0.4216 0.0045 0.0174 -0.0909 1383 HOH A O 6554 O O . HOH T . ? 0.2570 0.3458 0.3547 0.0218 0.0045 0.0095 1384 HOH A O 6555 O O . HOH T . ? 0.3280 0.2768 0.3971 0.0385 0.0297 -0.0481 1385 HOH A O 6556 O O . HOH T . ? 0.3692 0.3036 0.3307 -0.1004 -0.1113 -0.0548 1386 HOH A O 6557 O O . HOH T . ? 0.2336 0.3647 0.4256 -0.0297 -0.0893 0.0813 1387 HOH A O 6558 O O . HOH T . ? 0.2169 0.3597 0.4750 -0.0327 0.0511 -0.0495 1388 HOH A O 6559 O O . HOH T . ? 0.4757 0.4407 0.4581 -0.0427 0.0158 0.0557 1389 HOH A O 6560 O O . HOH T . ? 0.2302 0.3027 0.3259 0.0577 0.1022 0.0265 1390 HOH A O 6561 O O . HOH T . ? 0.1508 0.1534 0.5025 -0.0982 0.1270 -0.0245 1391 HOH A O 6562 O O . HOH T . ? 0.2323 0.4066 0.5802 -0.0291 0.1809 -0.0221 1392 HOH A O 6563 O O . HOH T . ? 0.6918 0.4855 0.4741 0.1054 0.1182 0.0707 1393 HOH A O 6564 O O . HOH T . ? 0.3403 0.5949 0.2578 0.0020 0.0961 0.0277 1394 HOH A O 6565 O O . HOH T . ? 0.2983 0.3932 0.1674 -0.0582 0.0348 0.0700 1395 HOH A O 6566 O O . HOH T . ? 0.2596 0.4103 0.4243 0.0881 0.1339 0.0598 1396 HOH A O 6567 O O . HOH T . ? 0.3499 0.2547 0.3393 0.1868 0.0959 0.0499 1397 HOH A O 6568 O O . HOH T . ? 0.3067 0.4925 0.5954 0.1809 0.2773 0.1432 1398 HOH A O 6569 O O . HOH T . ? 0.1265 0.2371 0.3010 0.0155 0.0534 0.0986 1399 HOH A O 6570 O O . HOH T . ? 0.6076 0.5744 0.6082 -0.1053 0.0794 -0.2784 1400 HOH A O 6571 O O . HOH T . ? 0.0416 0.4538 0.4075 0.0835 0.0150 0.0663 1401 HOH A O 6572 O O . HOH T . ? 0.3866 0.4607 0.1864 0.1115 0.0604 0.0857 1402 HOH A O 6573 O O . HOH T . ? 0.5059 0.4543 0.4140 0.0341 -0.0019 -0.0477 1403 HOH A O 6574 O O . HOH T . ? 0.4881 0.4613 0.3530 0.0020 0.0946 0.0215 1404 HOH A O 6575 O O . HOH T . ? 1.3410 1.2188 0.4367 -0.0051 0.1373 0.3106 1405 HOH A O 6576 O O . HOH T . ? 0.5615 0.2960 0.1766 -0.0103 0.0753 -0.0417 1406 HOH A O 6577 O O . HOH T . ? 0.4933 0.2474 0.3115 -0.0349 0.0446 -0.0915 1407 HOH A O 6578 O O . HOH T . ? 0.1308 0.4034 0.4016 0.0090 0.0623 -0.1166 1408 HOH A O 6579 O O . HOH T . ? 0.5562 0.3851 0.5915 0.0284 -0.0527 -0.1774 1409 HOH A O 6580 O O . HOH T . ? 0.3812 0.4353 0.6734 -0.1115 -0.0802 -0.0823 1410 HOH A O 6581 O O . HOH T . ? 0.2798 0.4270 0.4301 -0.0171 0.0420 -0.0579 1411 HOH A O 6582 O O . HOH T . ? 0.3000 0.3226 0.5304 -0.0393 -0.0284 0.0047 1412 HOH A O 6583 O O . HOH T . ? 0.2452 0.3856 0.3568 -0.1502 -0.0194 0.0410 1413 HOH A O 6584 O O . HOH T . ? 0.0500 0.2961 0.3831 -0.0558 0.0577 0.0483 1414 HOH A O 6585 O O . HOH T . ? 0.1575 0.2053 0.4048 0.0523 -0.0175 -0.1356 1415 HOH A O 6586 O O . HOH T . ? 0.5808 0.6279 0.4717 -0.0537 0.1198 0.0312 1416 HOH A O 6587 O O . HOH T . ? 0.8570 0.4679 0.5778 0.0116 0.3735 0.0633 1417 HOH A O 6588 O O . HOH T . ? 0.3531 0.4225 0.2405 -0.0133 0.0157 0.0899 1418 HOH A O 6589 O O . HOH T . ? 0.2116 0.4260 0.4181 0.0570 0.1842 0.0199 1419 HOH A O 6590 O O . HOH T . ? 0.3540 0.6405 0.4726 0.0030 0.1239 -0.2868 1420 HOH A O 6591 O O . HOH T . ? 0.2096 0.6418 0.7390 0.1162 0.0054 -0.0537 1421 HOH A O 6592 O O . HOH T . ? 0.3035 0.2612 0.2398 0.0058 0.0162 -0.1051 1422 HOH A O 6593 O O . HOH T . ? 0.3796 0.3916 0.3982 0.1200 -0.1179 -0.0082 1423 HOH A O 6594 O O . HOH T . ? 0.8600 0.6758 0.5218 0.0936 -0.0129 -0.2168 1424 HOH A O 6595 O O . HOH T . ? 0.3992 0.4449 0.3328 0.0795 -0.1511 -0.0250 1425 HOH A O 6596 O O . HOH T . ? 0.3376 0.4557 0.6601 -0.0439 -0.2512 0.0415 1426 HOH A O 6597 O O . HOH T . ? 0.3124 0.5527 0.7734 -0.0160 -0.0954 -0.0781 1427 HOH A O 6598 O O . HOH T . ? 0.2803 0.3362 0.3964 0.0343 -0.1704 -0.0550 1428 HOH A O 6599 O O . HOH T . ? 0.4456 0.4800 0.4967 -0.0433 -0.0320 -0.0749 1429 HOH A O 6600 O O . HOH T . ? 0.3562 0.4852 0.5689 -0.0070 -0.0530 -0.0551 1430 HOH A O 6601 O O . HOH T . ? 0.4309 1.3442 1.0337 0.3106 -0.3692 -0.2767 1431 HOH A O 6602 O O . HOH T . ? 0.3618 0.3335 0.2746 0.0917 -0.0689 -0.0930 1432 HOH A O 6603 O O . HOH T . ? 0.0749 0.1457 0.3963 0.0341 -0.1355 -0.0835 1433 HOH A O 6604 O O . HOH T . ? 0.5978 0.5822 0.3794 0.0702 -0.0315 0.0012 1434 HOH A O 6605 O O . HOH T . ? 0.3201 1.0617 0.4889 -0.3999 0.0775 -0.2306 1435 HOH A O 6606 O O . HOH T . ? 0.2915 0.4198 0.3980 -0.0081 -0.1008 0.0407 1436 HOH A O 6607 O O . HOH T . ? 0.5109 0.1808 0.3291 0.0422 0.0082 -0.0886 1437 HOH A O 6608 O O . HOH T . ? 0.4121 0.4222 0.4626 0.1057 0.0985 0.0244 1438 HOH A O 6609 O O . HOH T . ? 0.6490 0.5999 1.0819 -0.0131 0.2243 -0.2566 1439 HOH A O 6610 O O . HOH T . ? 0.4774 0.3126 0.3981 -0.0167 0.0879 -0.0010 1440 HOH A O 6611 O O . HOH T . ? 0.5935 0.3238 0.4847 -0.1990 0.0136 0.0703 1441 HOH A O 6612 O O . HOH T . ? 0.4675 0.6646 0.7114 0.0017 -0.1628 -0.0787 1442 HOH A O 6613 O O . HOH T . ? 0.5716 0.5745 0.5251 0.3034 0.1098 0.1283 1443 HOH A O 6614 O O . HOH T . ? 0.2676 0.5810 0.3701 -0.1959 -0.0009 -0.1686 1444 HOH A O 6615 O O . HOH T . ? 0.4256 0.5461 0.6397 -0.0611 0.2268 0.0167 1445 HOH A O 6616 O O . HOH T . ? 0.1871 0.3829 0.3891 0.1856 -0.0746 -0.0278 1446 HOH A O 6617 O O . HOH T . ? 0.3206 0.1076 0.1822 -0.0661 0.0685 -0.0609 1447 HOH A O 6618 O O . HOH T . ? 0.2816 0.4129 0.4344 0.0847 -0.0906 -0.1643 1448 HOH A O 6619 O O . HOH T . ? 0.5878 0.4628 0.5272 -0.0811 0.0389 -0.1536 1449 HOH A O 6620 O O A HOH T . ? 0.3439 0.5162 0.2837 0.1456 0.0851 -0.0619 1450 HOH A O 6621 O O B HOH T . ? 0.3729 0.4255 0.3348 0.0630 0.1003 -0.0352 1450 HOH A O 6622 O O . HOH T . ? 0.5430 0.8415 0.3524 -0.1756 0.1290 -0.1671 1451 HOH A O 6623 O O . HOH T . ? 0.7054 0.5842 0.5477 0.2077 0.1025 0.2094 1452 HOH A O 6624 O O . HOH T . ? 0.1758 0.2655 0.2666 0.0313 -0.0146 -0.0136 1453 HOH A O 6625 O O . HOH T . ? 0.2786 0.3520 0.4937 0.1540 -0.1029 -0.1335 1454 HOH A O 6626 O O . HOH T . ? 0.4450 0.4900 0.5120 0.0252 -0.0254 -0.0103 1455 HOH A O 6627 O O . HOH T . ? 0.4920 0.5212 0.5519 0.2445 0.0006 0.0659 1456 HOH A O 6628 O O . HOH T . ? 0.5940 0.2675 0.6606 -0.0037 -0.0809 -0.0253 1457 HOH A O 6629 O O . HOH T . ? 0.1200 0.2025 0.2569 0.0536 -0.0294 -0.0773 1458 HOH A O 6630 O O . HOH T . ? 0.2323 0.2489 0.2339 0.0580 -0.1100 -0.0991 1459 HOH A O 6631 O O . HOH T . ? 0.0991 0.2553 0.3773 0.0685 -0.0693 -0.1135 1460 HOH A O 6632 O O . HOH T . ? 0.5257 0.5461 0.5878 0.0374 -0.0837 -0.0834 1461 HOH A O 6633 O O . HOH T . ? 0.7027 0.3771 0.3534 -0.1108 0.1436 -0.0471 1462 HOH A O 6634 O O . HOH T . ? 0.2009 0.4143 0.4250 -0.0300 -0.0831 -0.0344 1463 HOH A O 6635 O O . HOH T . ? 0.2972 0.5564 0.4584 0.0398 -0.2023 -0.1336 1464 HOH A O 6636 O O . HOH T . ? 0.0878 0.3380 0.1482 0.0560 0.0150 0.0261 1465 HOH A O 6637 O O . HOH T . ? 0.1482 0.5767 0.5502 0.0005 -0.0649 -0.3969 1466 HOH A O 6638 O O . HOH T . ? 0.3878 0.4207 0.3626 0.1853 -0.1012 -0.2294 1467 HOH A O 6639 O O . HOH T . ? 0.2181 0.5009 0.5052 0.0500 -0.0725 0.0517 1468 HOH A O 6640 O O . HOH T . ? 0.4155 0.2214 0.2976 0.0090 -0.0698 0.0348 1469 HOH A O 6641 O O . HOH T . ? 0.5256 0.4086 0.5664 -0.0049 0.0741 -0.0097 1470 HOH A O 6642 O O . HOH T . ? 0.5437 0.5799 0.9081 0.0895 -0.0398 -0.0795 1471 HOH A O 6643 O O . HOH T . ? 0.3247 0.9435 0.5477 -0.0367 0.0102 0.0713 1472 HOH A O 6644 O O . HOH T . ? 0.3295 0.4830 0.5059 -0.0248 0.1133 0.0332 1473 HOH A O 6645 O O . HOH T . ? 0.2375 0.2580 0.3536 0.1121 -0.0890 -0.0950 1474 HOH A O 6646 O O . HOH T . ? 0.5004 0.7862 0.4192 0.0990 -0.1394 -0.1899 1475 HOH A O 6647 O O . HOH T . ? 0.7158 0.5695 0.5380 0.0325 -0.2632 -0.0249 1476 HOH A O 6648 O O . HOH T . ? 0.5513 0.2961 0.4543 0.0943 -0.2035 -0.0392 1477 HOH A O 6649 O O . HOH T . ? 0.2128 0.4258 0.4165 0.0773 -0.1047 0.0277 1478 HOH A O 6650 O O . HOH T . ? 0.2697 0.4792 0.3316 -0.1498 0.0373 -0.1369 1479 HOH A O 6651 O O . HOH T . ? 0.3617 0.4072 0.4227 -0.0898 0.0006 -0.0651 1480 HOH A O 6652 O O . HOH T . ? 0.2238 0.3640 0.4622 -0.0422 -0.0838 -0.1001 1481 HOH A O 6653 O O . HOH T . ? 0.2699 0.2739 0.3187 0.0426 -0.0166 -0.1360 1482 HOH A O 6654 O O . HOH T . ? 0.2308 0.3803 0.4391 -0.0106 0.0394 0.0191 1483 HOH A O 6655 O O . HOH T . ? 0.2397 0.1785 0.1552 -0.0234 0.0047 -0.0470 1484 HOH A O 6656 O O . HOH T . ? 0.3966 0.7794 0.2920 0.1424 -0.0369 0.0542 1485 HOH A O 6657 O O . HOH T . ? 0.4233 0.4289 0.3420 -0.0582 0.0551 0.0012 1486 HOH A O 6658 O O . HOH T . ? 0.8594 0.4066 0.4649 -0.1006 -0.0742 0.0228 1487 HOH A O 6659 O O . HOH T . ? 0.3601 0.5673 0.4600 0.0767 -0.0756 -0.0192 1488 HOH A O 6660 O O . HOH T . ? 0.3303 0.1735 0.2377 0.0712 -0.0268 0.0540 1489 HOH A O 6661 O O . HOH T . ? 0.8823 0.4894 0.6774 0.0134 -0.0488 0.1364 1490 HOH A O 6662 O O . HOH T . ? 0.5079 0.1484 0.5038 -0.0042 0.0720 0.1195 1491 HOH A O 6663 O O . HOH T . ? 0.8690 0.6932 0.5310 -0.0047 -0.0872 -0.1751 1492 HOH A O 6664 O O . HOH T . ? 0.6564 0.7401 0.3908 0.1107 -0.1848 -0.0100 1493 HOH A O 6665 O O . HOH T . ? 0.2623 0.6084 0.5086 0.0570 0.0014 -0.0126 1494 HOH A O 6666 O O . HOH T . ? 0.8942 0.6831 0.5789 -0.0024 -0.0311 0.1605 1495 HOH A O 6667 O O . HOH T . ? 0.7736 0.7608 0.8567 0.2371 -0.0198 -0.1346 1496 HOH A O 6668 O O . HOH T . ? 0.8026 0.4096 0.4241 0.0446 0.0085 0.0212 1497 HOH A O 6669 O O . HOH T . ? 0.3998 1.0600 0.3597 0.0075 -0.0221 0.0091 1498 HOH A O 6670 O O . HOH T . ? 0.7853 0.5628 0.6778 0.1464 -0.1973 -0.0531 1499 HOH A O 6671 O O . HOH T . ? 0.1108 0.2212 0.0810 -0.0041 0.0485 0.0112 1500 HOH A O 6672 O O . HOH T . ? 0.6686 0.7089 0.6272 -0.0806 -0.2137 0.0177 1501 HOH A O 6673 O O . HOH T . ? 0.7285 0.4708 1.0837 -0.0877 0.0246 -0.1952 1502 HOH A O 6674 O O . HOH T . ? 0.8238 0.3743 0.4348 0.0547 0.0371 -0.2263 1503 HOH A O 6675 O O . HOH T . ? 1.0057 0.5170 0.6589 0.1420 -0.1866 0.0797 1504 HOH A O 6676 O O . HOH T . ? 0.1687 0.3816 0.4920 0.0529 -0.0813 -0.0565 1505 HOH A O 6677 O O . HOH T . ? 0.6805 1.0179 0.7376 -0.0075 -0.2075 0.0554 1506 HOH A O 6678 O O . HOH T . ? 0.6370 0.6568 0.6609 -0.0658 0.0787 0.1126 1507 HOH A O 6679 O O . HOH T . ? 0.5983 0.4697 0.6745 0.0119 0.2944 -0.0353 1508 HOH A O 6680 O O . HOH T . ? 0.4354 0.5590 0.7174 0.0704 0.0279 0.0045 1509 HOH A O 6681 O O . HOH T . ? 0.6485 0.3675 1.0682 0.0636 0.0046 -0.1587 1510 HOH A O # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 MET 1 -6 ? ? ? A . n A 1 2 LYS 2 -5 ? ? ? A . n A 1 3 LEU 3 -4 ? ? ? A . n A 1 4 CYS 4 -3 ? ? ? A . n A 1 5 ILE 5 -2 ? ? ? A . n A 1 6 LEU 6 -1 ? ? ? A . n A 1 7 LEU 7 0 ? ? ? A . n A 1 8 ALA 8 1 ? ? ? A . n A 1 9 VAL 9 2 ? ? ? A . n A 1 10 VAL 10 3 ? ? ? A . n A 1 11 ALA 11 4 ? ? ? A . n A 1 12 PHE 12 5 ? ? ? A . n A 1 13 VAL 13 6 ? ? ? A . n A 1 14 GLY 14 7 ? ? ? A . n A 1 15 LEU 15 8 ? ? ? A . n A 1 16 SER 16 9 ? ? ? A . n A 1 17 LEU 17 10 ? ? ? A . n A 1 18 GLY 18 11 ? ? ? A . n A 1 19 ARG 19 12 ? ? ? A . n A 1 20 SER 20 13 ? ? ? A . n A 1 21 GLY 21 14 ? ? ? A . n A 1 22 LEU 22 15 ? ? ? A . n A 1 23 ASN 23 16 ? ? ? A . n A 1 24 ASP 24 17 ? ? ? A . n A 1 25 ILE 25 18 ? ? ? A . n A 1 26 PHE 26 19 ? ? ? A . n A 1 27 GLU 27 20 ? ? ? A . n A 1 28 ALA 28 21 ? ? ? A . n A 1 29 GLN 29 22 ? ? ? A . n A 1 30 LYS 30 23 ? ? ? A . n A 1 31 ILE 31 24 ? ? ? A . n A 1 32 GLU 32 25 ? ? ? A . n A 1 33 TRP 33 26 ? ? ? A . n A 1 34 HIS 34 27 ? ? ? A . n A 1 35 GLU 35 28 ? ? ? A . n A 1 36 GLY 36 29 ? ? ? A . n A 1 37 SER 37 30 ? ? ? A . n A 1 38 GLY 38 31 ? ? ? A . n A 1 39 SER 39 32 ? ? ? A . n A 1 40 GLY 40 33 ? ? ? A . n A 1 41 SER 41 34 ? ? ? A . n A 1 42 GLU 42 35 ? ? ? A . n A 1 43 ASN 43 36 ? ? ? A . n A 1 44 LEU 44 37 ? ? ? A . n A 1 45 TYR 45 38 ? ? ? A . n A 1 46 PHE 46 39 ? ? ? A . n A 1 47 GLN 47 40 ? ? ? A . n A 1 48 GLY 48 41 ? ? ? A . n A 1 49 ARG 49 42 ? ? ? A . n A 1 50 SER 50 43 ? ? ? A . n A 1 51 LYS 51 44 ? ? ? A . n A 1 52 SER 52 45 ? ? ? A . n A 1 53 SER 53 46 ? ? ? A . n A 1 54 ASN 54 47 ? ? ? A . n A 1 55 GLU 55 48 ? ? ? A . n A 1 56 ALA 56 49 ? ? ? A . n A 1 57 THR 57 50 ? ? ? A . n A 1 58 ASN 58 51 ? ? ? A . n A 1 59 ILE 59 52 ? ? ? A . n A 1 60 THR 60 53 ? ? ? A . n A 1 61 PRO 61 54 ? ? ? A . n A 1 62 LYS 62 55 ? ? ? A . n A 1 63 HIS 63 56 56 HIS HIS A . n A 1 64 ASN 64 57 57 ASN ASN A . n A 1 65 MET 65 58 58 MET MET A . n A 1 66 LYS 66 59 59 LYS LYS A . n A 1 67 ALA 67 60 60 ALA ALA A . n A 1 68 PHE 68 61 61 PHE PHE A . n A 1 69 LEU 69 62 62 LEU LEU A . n A 1 70 ASP 70 63 63 ASP ASP A . n A 1 71 GLU 71 64 64 GLU GLU A . n A 1 72 LEU 72 65 65 LEU LEU A . n A 1 73 LYS 73 66 66 LYS LYS A . n A 1 74 ALA 74 67 67 ALA ALA A . n A 1 75 GLU 75 68 68 GLU GLU A . n A 1 76 ASN 76 69 69 ASN ASN A . n A 1 77 ILE 77 70 70 ILE ILE A . n A 1 78 LYS 78 71 71 LYS LYS A . n A 1 79 LYS 79 72 72 LYS LYS A . n A 1 80 PHE 80 73 73 PHE PHE A . n A 1 81 LEU 81 74 74 LEU LEU A . n A 1 82 TYR 82 75 75 TYR TYR A . n A 1 83 ASN 83 76 76 ASN ASN A . n A 1 84 PHE 84 77 77 PHE PHE A . n A 1 85 THR 85 78 78 THR THR A . n A 1 86 GLN 86 79 79 GLN GLN A . n A 1 87 ILE 87 80 80 ILE ILE A . n A 1 88 PRO 88 81 81 PRO PRO A . n A 1 89 HIS 89 82 82 HIS HIS A . n A 1 90 LEU 90 83 83 LEU LEU A . n A 1 91 ALA 91 84 84 ALA ALA A . n A 1 92 GLY 92 85 85 GLY GLY A . n A 1 93 THR 93 86 86 THR THR A . n A 1 94 GLU 94 87 87 GLU GLU A . n A 1 95 GLN 95 88 88 GLN GLN A . n A 1 96 ASN 96 89 89 ASN ASN A . n A 1 97 PHE 97 90 90 PHE PHE A . n A 1 98 GLN 98 91 91 GLN GLN A . n A 1 99 LEU 99 92 92 LEU LEU A . n A 1 100 ALA 100 93 93 ALA ALA A . n A 1 101 LYS 101 94 94 LYS LYS A . n A 1 102 GLN 102 95 95 GLN GLN A . n A 1 103 ILE 103 96 96 ILE ILE A . n A 1 104 GLN 104 97 97 GLN GLN A . n A 1 105 SER 105 98 98 SER SER A . n A 1 106 GLN 106 99 99 GLN GLN A . n A 1 107 TRP 107 100 100 TRP TRP A . n A 1 108 LYS 108 101 101 LYS LYS A . n A 1 109 GLU 109 102 102 GLU GLU A . n A 1 110 PHE 110 103 103 PHE PHE A . n A 1 111 GLY 111 104 104 GLY GLY A . n A 1 112 LEU 112 105 105 LEU LEU A . n A 1 113 ASP 113 106 106 ASP ASP A . n A 1 114 SER 114 107 107 SER SER A . n A 1 115 VAL 115 108 108 VAL VAL A . n A 1 116 GLU 116 109 109 GLU GLU A . n A 1 117 LEU 117 110 110 LEU LEU A . n A 1 118 ALA 118 111 111 ALA ALA A . n A 1 119 HIS 119 112 112 HIS HIS A . n A 1 120 TYR 120 113 113 TYR TYR A . n A 1 121 ASP 121 114 114 ASP ASP A . n A 1 122 VAL 122 115 115 VAL VAL A . n A 1 123 LEU 123 116 116 LEU LEU A . n A 1 124 LEU 124 117 117 LEU LEU A . n A 1 125 SER 125 118 118 SER SER A . n A 1 126 TYR 126 119 119 TYR TYR A . n A 1 127 PRO 127 120 120 PRO PRO A . n A 1 128 ASN 128 121 121 ASN ASN A . n A 1 129 LYS 129 122 122 LYS LYS A . n A 1 130 THR 130 123 123 THR THR A . n A 1 131 HIS 131 124 124 HIS HIS A . n A 1 132 PRO 132 125 125 PRO PRO A . n A 1 133 ASN 133 126 126 ASN ASN A . n A 1 134 TYR 134 127 127 TYR TYR A . n A 1 135 ILE 135 128 128 ILE ILE A . n A 1 136 SER 136 129 129 SER SER A . n A 1 137 ILE 137 130 130 ILE ILE A . n A 1 138 ILE 138 131 131 ILE ILE A . n A 1 139 ASN 139 132 132 ASN ASN A . n A 1 140 GLU 140 133 133 GLU GLU A . n A 1 141 ASP 141 134 134 ASP ASP A . n A 1 142 GLY 142 135 135 GLY GLY A . n A 1 143 ASN 143 136 136 ASN ASN A . n A 1 144 GLU 144 137 137 GLU GLU A . n A 1 145 ILE 145 138 138 ILE ILE A . n A 1 146 PHE 146 139 139 PHE PHE A . n A 1 147 ASN 147 140 140 ASN ASN A . n A 1 148 THR 148 141 141 THR THR A . n A 1 149 SER 149 142 142 SER SER A . n A 1 150 LEU 150 143 143 LEU LEU A . n A 1 151 PHE 151 144 144 PHE PHE A . n A 1 152 GLU 152 145 145 GLU GLU A . n A 1 153 PRO 153 146 146 PRO PRO A . n A 1 154 PRO 154 147 147 PRO PRO A . n A 1 155 PRO 155 148 148 PRO PRO A . n A 1 156 PRO 156 149 149 PRO PRO A . n A 1 157 GLY 157 150 150 GLY GLY A . n A 1 158 TYR 158 151 151 TYR TYR A . n A 1 159 GLU 159 152 152 GLU GLU A . n A 1 160 ASN 160 153 153 ASN ASN A . n A 1 161 VAL 161 154 154 VAL VAL A . n A 1 162 SER 162 155 155 SER SER A . n A 1 163 ASP 163 156 156 ASP ASP A . n A 1 164 ILE 164 157 157 ILE ILE A . n A 1 165 VAL 165 158 158 VAL VAL A . n A 1 166 PRO 166 159 159 PRO PRO A . n A 1 167 PRO 167 160 160 PRO PRO A . n A 1 168 PHE 168 161 161 PHE PHE A . n A 1 169 SER 169 162 162 SER SER A . n A 1 170 ALA 170 163 163 ALA ALA A . n A 1 171 PHE 171 164 164 PHE PHE A . n A 1 172 SER 172 165 165 SER SER A . n A 1 173 PRO 173 166 166 PRO PRO A . n A 1 174 GLN 174 167 167 GLN GLN A . n A 1 175 GLY 175 168 168 GLY GLY A . n A 1 176 MET 176 169 169 MET MET A . n A 1 177 PRO 177 170 170 PRO PRO A . n A 1 178 GLU 178 171 171 GLU GLU A . n A 1 179 GLY 179 172 172 GLY GLY A . n A 1 180 ASP 180 173 173 ASP ASP A . n A 1 181 LEU 181 174 174 LEU LEU A . n A 1 182 VAL 182 175 175 VAL VAL A . n A 1 183 TYR 183 176 176 TYR TYR A . n A 1 184 VAL 184 177 177 VAL VAL A . n A 1 185 ASN 185 178 178 ASN ASN A . n A 1 186 TYR 186 179 179 TYR TYR A . n A 1 187 ALA 187 180 180 ALA ALA A . n A 1 188 ARG 188 181 181 ARG ARG A . n A 1 189 THR 189 182 182 THR THR A . n A 1 190 GLU 190 183 183 GLU GLU A . n A 1 191 ASP 191 184 184 ASP ASP A . n A 1 192 PHE 192 185 185 PHE PHE A . n A 1 193 PHE 193 186 186 PHE PHE A . n A 1 194 LYS 194 187 187 LYS LYS A . n A 1 195 LEU 195 188 188 LEU LEU A . n A 1 196 GLU 196 189 189 GLU GLU A . n A 1 197 ARG 197 190 190 ARG ARG A . n A 1 198 ASP 198 191 191 ASP ASP A . n A 1 199 MET 199 192 192 MET MET A . n A 1 200 LYS 200 193 193 LYS LYS A . n A 1 201 ILE 201 194 194 ILE ILE A . n A 1 202 ASN 202 195 195 ASN ASN A . n A 1 203 CYS 203 196 196 CYS CYS A . n A 1 204 SER 204 197 197 SER SER A . n A 1 205 GLY 205 198 198 GLY GLY A . n A 1 206 LYS 206 199 199 LYS LYS A . n A 1 207 ILE 207 200 200 ILE ILE A . n A 1 208 VAL 208 201 201 VAL VAL A . n A 1 209 ILE 209 202 202 ILE ILE A . n A 1 210 ALA 210 203 203 ALA ALA A . n A 1 211 ARG 211 204 204 ARG ARG A . n A 1 212 TYR 212 205 205 TYR TYR A . n A 1 213 GLY 213 206 206 GLY GLY A . n A 1 214 LYS 214 207 207 LYS LYS A . n A 1 215 VAL 215 208 208 VAL VAL A . n A 1 216 PHE 216 209 209 PHE PHE A . n A 1 217 ARG 217 210 210 ARG ARG A . n A 1 218 GLY 218 211 211 GLY GLY A . n A 1 219 ASN 219 212 212 ASN ASN A . n A 1 220 LYS 220 213 213 LYS LYS A . n A 1 221 VAL 221 214 214 VAL VAL A . n A 1 222 LYS 222 215 215 LYS LYS A . n A 1 223 ASN 223 216 216 ASN ASN A . n A 1 224 ALA 224 217 217 ALA ALA A . n A 1 225 GLN 225 218 218 GLN GLN A . n A 1 226 LEU 226 219 219 LEU LEU A . n A 1 227 ALA 227 220 220 ALA ALA A . n A 1 228 GLY 228 221 221 GLY GLY A . n A 1 229 ALA 229 222 222 ALA ALA A . n A 1 230 LYS 230 223 223 LYS LYS A . n A 1 231 GLY 231 224 224 GLY GLY A . n A 1 232 VAL 232 225 225 VAL VAL A . n A 1 233 ILE 233 226 226 ILE ILE A . n A 1 234 LEU 234 227 227 LEU LEU A . n A 1 235 TYR 235 228 228 TYR TYR A . n A 1 236 SER 236 229 229 SER SER A . n A 1 237 ASP 237 230 230 ASP ASP A . n A 1 238 PRO 238 231 231 PRO PRO A . n A 1 239 ALA 239 232 232 ALA ALA A . n A 1 240 ASP 240 233 233 ASP ASP A . n A 1 241 TYR 241 234 234 TYR TYR A . n A 1 242 PHE 242 235 235 PHE PHE A . n A 1 243 ALA 243 236 236 ALA ALA A . n A 1 244 PRO 244 237 237 PRO PRO A . n A 1 245 GLY 245 238 238 GLY GLY A . n A 1 246 VAL 246 239 239 VAL VAL A . n A 1 247 LYS 247 240 240 LYS LYS A . n A 1 248 SER 248 241 241 SER SER A . n A 1 249 TYR 249 242 242 TYR TYR A . n A 1 250 PRO 250 243 243 PRO PRO A . n A 1 251 ASP 251 244 244 ASP ASP A . n A 1 252 GLY 252 245 245 GLY GLY A . n A 1 253 TRP 253 246 246 TRP TRP A . n A 1 254 ASN 254 247 247 ASN ASN A . n A 1 255 LEU 255 248 248 LEU LEU A . n A 1 256 PRO 256 249 249 PRO PRO A . n A 1 257 GLY 257 250 250 GLY GLY A . n A 1 258 GLY 258 251 251 GLY GLY A . n A 1 259 GLY 259 252 252 GLY GLY A . n A 1 260 VAL 260 253 253 VAL VAL A . n A 1 261 GLN 261 254 254 GLN GLN A . n A 1 262 ARG 262 255 255 ARG ARG A . n A 1 263 GLY 263 256 256 GLY GLY A . n A 1 264 ASN 264 257 257 ASN ASN A . n A 1 265 ILE 265 258 258 ILE ILE A . n A 1 266 LEU 266 259 259 LEU LEU A . n A 1 267 ASN 267 260 260 ASN ASN A . n A 1 268 LEU 268 261 261 LEU LEU A . n A 1 269 ASN 269 262 262 ASN ASN A . n A 1 270 GLY 270 263 263 GLY GLY A . n A 1 271 ALA 271 264 264 ALA ALA A . n A 1 272 GLY 272 265 265 GLY GLY A . n A 1 273 ASP 273 266 266 ASP ASP A . n A 1 274 PRO 274 267 267 PRO PRO A . n A 1 275 LEU 275 268 268 LEU LEU A . n A 1 276 THR 276 269 269 THR THR A . n A 1 277 PRO 277 270 270 PRO PRO A . n A 1 278 GLY 278 271 271 GLY GLY A . n A 1 279 TYR 279 272 272 TYR TYR A . n A 1 280 PRO 280 273 273 PRO PRO A . n A 1 281 ALA 281 274 274 ALA ALA A . n A 1 282 ASN 282 275 275 ASN ASN A . n A 1 283 GLU 283 276 276 GLU GLU A . n A 1 284 TYR 284 277 277 TYR TYR A . n A 1 285 ALA 285 278 278 ALA ALA A . n A 1 286 TYR 286 279 279 TYR TYR A . n A 1 287 ARG 287 280 280 ARG ARG A . n A 1 288 ARG 288 281 281 ARG ARG A . n A 1 289 GLY 289 282 282 GLY GLY A . n A 1 290 ILE 290 283 283 ILE ILE A . n A 1 291 ALA 291 284 284 ALA ALA A . n A 1 292 GLU 292 285 285 GLU GLU A . n A 1 293 ALA 293 286 286 ALA ALA A . n A 1 294 VAL 294 287 287 VAL VAL A . n A 1 295 GLY 295 288 288 GLY GLY A . n A 1 296 LEU 296 289 289 LEU LEU A . n A 1 297 PRO 297 290 290 PRO PRO A . n A 1 298 SER 298 291 291 SER SER A . n A 1 299 ILE 299 292 292 ILE ILE A . n A 1 300 PRO 300 293 293 PRO PRO A . n A 1 301 VAL 301 294 294 VAL VAL A . n A 1 302 HIS 302 295 295 HIS HIS A . n A 1 303 PRO 303 296 296 PRO PRO A . n A 1 304 ILE 304 297 297 ILE ILE A . n A 1 305 GLY 305 298 298 GLY GLY A . n A 1 306 TYR 306 299 299 TYR TYR A . n A 1 307 TYR 307 300 300 TYR TYR A . n A 1 308 ASP 308 301 301 ASP ASP A . n A 1 309 ALA 309 302 302 ALA ALA A . n A 1 310 GLN 310 303 303 GLN GLN A . n A 1 311 LYS 311 304 304 LYS LYS A . n A 1 312 LEU 312 305 305 LEU LEU A . n A 1 313 LEU 313 306 306 LEU LEU A . n A 1 314 GLU 314 307 307 GLU GLU A . n A 1 315 LYS 315 308 308 LYS LYS A . n A 1 316 MET 316 309 309 MET MET A . n A 1 317 GLY 317 310 310 GLY GLY A . n A 1 318 GLY 318 311 311 GLY GLY A . n A 1 319 SER 319 312 312 SER SER A . n A 1 320 ALA 320 313 313 ALA ALA A . n A 1 321 PRO 321 314 314 PRO PRO A . n A 1 322 PRO 322 315 315 PRO PRO A . n A 1 323 ASP 323 316 316 ASP ASP A . n A 1 324 SER 324 317 317 SER SER A . n A 1 325 SER 325 318 318 SER SER A . n A 1 326 TRP 326 319 319 TRP TRP A . n A 1 327 ARG 327 320 320 ARG ARG A . n A 1 328 GLY 328 321 321 GLY GLY A . n A 1 329 SER 329 322 322 SER SER A . n A 1 330 LEU 330 323 323 LEU LEU A . n A 1 331 LYS 331 324 324 LYS LYS A . n A 1 332 VAL 332 325 325 VAL VAL A . n A 1 333 PRO 333 326 326 PRO PRO A . n A 1 334 TYR 334 327 327 TYR TYR A . n A 1 335 ASN 335 328 328 ASN ASN A . n A 1 336 VAL 336 329 329 VAL VAL A . n A 1 337 GLY 337 330 330 GLY GLY A . n A 1 338 PRO 338 331 331 PRO PRO A . n A 1 339 GLY 339 332 332 GLY GLY A . n A 1 340 PHE 340 333 333 PHE PHE A . n A 1 341 THR 341 334 334 THR THR A . n A 1 342 GLY 342 335 335 GLY GLY A . n A 1 343 ASN 343 336 336 ASN ASN A . n A 1 344 PHE 344 337 337 PHE PHE A . n A 1 345 SER 345 338 338 SER SER A . n A 1 346 THR 346 339 339 THR THR A . n A 1 347 GLN 347 340 340 GLN GLN A . n A 1 348 LYS 348 341 341 LYS LYS A . n A 1 349 VAL 349 342 342 VAL VAL A . n A 1 350 LYS 350 343 343 LYS LYS A . n A 1 351 MET 351 344 344 MET MET A . n A 1 352 HIS 352 345 345 HIS HIS A . n A 1 353 ILE 353 346 346 ILE ILE A . n A 1 354 HIS 354 347 347 HIS HIS A . n A 1 355 SER 355 348 348 SER SER A . n A 1 356 THR 356 349 349 THR THR A . n A 1 357 ASN 357 350 350 ASN ASN A . n A 1 358 GLU 358 351 351 GLU GLU A . n A 1 359 VAL 359 352 352 VAL VAL A . n A 1 360 THR 360 353 353 THR THR A . n A 1 361 ARG 361 354 354 ARG ARG A . n A 1 362 ILE 362 355 355 ILE ILE A . n A 1 363 TYR 363 356 356 TYR TYR A . n A 1 364 ASN 364 357 357 ASN ASN A . n A 1 365 VAL 365 358 358 VAL VAL A . n A 1 366 ILE 366 359 359 ILE ILE A . n A 1 367 GLY 367 360 360 GLY GLY A . n A 1 368 THR 368 361 361 THR THR A . n A 1 369 LEU 369 362 362 LEU LEU A . n A 1 370 ARG 370 363 363 ARG ARG A . n A 1 371 GLY 371 364 364 GLY GLY A . n A 1 372 ALA 372 365 365 ALA ALA A . n A 1 373 VAL 373 366 366 VAL VAL A . n A 1 374 GLU 374 367 367 GLU GLU A . n A 1 375 PRO 375 368 368 PRO PRO A . n A 1 376 ASP 376 369 369 ASP ASP A . n A 1 377 ARG 377 370 370 ARG ARG A . n A 1 378 TYR 378 371 371 TYR TYR A . n A 1 379 VAL 379 372 372 VAL VAL A . n A 1 380 ILE 380 373 373 ILE ILE A . n A 1 381 LEU 381 374 374 LEU LEU A . n A 1 382 GLY 382 375 375 GLY GLY A . n A 1 383 GLY 383 376 376 GLY GLY A . n A 1 384 HIS 384 377 377 HIS HIS A . n A 1 385 ARG 385 378 378 ARG ARG A . n A 1 386 ASP 386 379 379 ASP ASP A . n A 1 387 SER 387 380 380 SER SER A . n A 1 388 TRP 388 381 381 TRP TRP A . n A 1 389 VAL 389 382 382 VAL VAL A . n A 1 390 PHE 390 383 383 PHE PHE A . n A 1 391 GLY 391 384 384 GLY GLY A . n A 1 392 GLY 392 385 385 GLY GLY A . n A 1 393 ILE 393 386 386 ILE ILE A . n A 1 394 ASP 394 387 387 ASP ASP A . n A 1 395 PRO 395 388 388 PRO PRO A . n A 1 396 GLN 396 389 389 GLN GLN A . n A 1 397 SER 397 390 390 SER SER A . n A 1 398 GLY 398 391 391 GLY GLY A . n A 1 399 ALA 399 392 392 ALA ALA A . n A 1 400 ALA 400 393 393 ALA ALA A . n A 1 401 VAL 401 394 394 VAL VAL A . n A 1 402 VAL 402 395 395 VAL VAL A . n A 1 403 HIS 403 396 396 HIS HIS A . n A 1 404 GLU 404 397 397 GLU GLU A . n A 1 405 ILE 405 398 398 ILE ILE A . n A 1 406 VAL 406 399 399 VAL VAL A . n A 1 407 ARG 407 400 400 ARG ARG A . n A 1 408 SER 408 401 401 SER SER A . n A 1 409 PHE 409 402 402 PHE PHE A . n A 1 410 GLY 410 403 403 GLY GLY A . n A 1 411 THR 411 404 404 THR THR A . n A 1 412 LEU 412 405 405 LEU LEU A . n A 1 413 LYS 413 406 406 LYS LYS A . n A 1 414 LYS 414 407 407 LYS LYS A . n A 1 415 GLU 415 408 408 GLU GLU A . n A 1 416 GLY 416 409 409 GLY GLY A . n A 1 417 TRP 417 410 410 TRP TRP A . n A 1 418 ARG 418 411 411 ARG ARG A . n A 1 419 PRO 419 412 412 PRO PRO A . n A 1 420 ARG 420 413 413 ARG ARG A . n A 1 421 ARG 421 414 414 ARG ARG A . n A 1 422 THR 422 415 415 THR THR A . n A 1 423 ILE 423 416 416 ILE ILE A . n A 1 424 LEU 424 417 417 LEU LEU A . n A 1 425 PHE 425 418 418 PHE PHE A . n A 1 426 ALA 426 419 419 ALA ALA A . n A 1 427 SER 427 420 420 SER SER A . n A 1 428 TRP 428 421 421 TRP TRP A . n A 1 429 ASP 429 422 422 ASP ASP A . n A 1 430 ALA 430 423 423 ALA ALA A . n A 1 431 ALA 431 424 424 ALA ALA A . n A 1 432 GLU 432 425 425 GLU GLU A . n A 1 433 PHE 433 426 426 PHE PHE A . n A 1 434 GLY 434 427 427 GLY GLY A . n A 1 435 LEU 435 428 428 LEU LEU A . n A 1 436 LEU 436 429 429 LEU LEU A . n A 1 437 GLY 437 430 430 GLY GLY A . n A 1 438 SER 438 431 431 SER SER A . n A 1 439 THR 439 432 432 THR THR A . n A 1 440 GLU 440 433 433 GLU GLU A . n A 1 441 TRP 441 434 434 TRP TRP A . n A 1 442 ALA 442 435 435 ALA ALA A . n A 1 443 GLU 443 436 436 GLU GLU A . n A 1 444 GLU 444 437 437 GLU GLU A . n A 1 445 ASN 445 438 438 ASN ASN A . n A 1 446 SER 446 439 439 SER SER A . n A 1 447 ARG 447 440 440 ARG ARG A . n A 1 448 LEU 448 441 441 LEU LEU A . n A 1 449 LEU 449 442 442 LEU LEU A . n A 1 450 GLN 450 443 443 GLN GLN A . n A 1 451 GLU 451 444 444 GLU GLU A . n A 1 452 ARG 452 445 445 ARG ARG A . n A 1 453 GLY 453 446 446 GLY GLY A . n A 1 454 VAL 454 447 447 VAL VAL A . n A 1 455 ALA 455 448 448 ALA ALA A . n A 1 456 TYR 456 449 449 TYR TYR A . n A 1 457 ILE 457 450 450 ILE ILE A . n A 1 458 ASN 458 451 451 ASN ASN A . n A 1 459 ALA 459 452 452 ALA ALA A . n A 1 460 ASP 460 453 453 ASP ASP A . n A 1 461 SER 461 454 454 SER SER A . n A 1 462 SER 462 455 455 SER SER A . n A 1 463 ILE 463 456 456 ILE ILE A . n A 1 464 GLU 464 457 457 GLU GLU A . n A 1 465 GLY 465 458 458 GLY GLY A . n A 1 466 ASN 466 459 459 ASN ASN A . n A 1 467 TYR 467 460 460 TYR TYR A . n A 1 468 THR 468 461 461 THR THR A . n A 1 469 LEU 469 462 462 LEU LEU A . n A 1 470 ARG 470 463 463 ARG ARG A . n A 1 471 VAL 471 464 464 VAL VAL A . n A 1 472 ASP 472 465 465 ASP ASP A . n A 1 473 CYS 473 466 466 CYS CYS A . n A 1 474 THR 474 467 467 THR THR A . n A 1 475 PRO 475 468 468 PRO PRO A . n A 1 476 LEU 476 469 469 LEU LEU A . n A 1 477 MET 477 470 470 MET MET A . n A 1 478 TYR 478 471 471 TYR TYR A . n A 1 479 SER 479 472 472 SER SER A . n A 1 480 LEU 480 473 473 LEU LEU A . n A 1 481 VAL 481 474 474 VAL VAL A . n A 1 482 HIS 482 475 475 HIS HIS A . n A 1 483 ASN 483 476 476 ASN ASN A . n A 1 484 LEU 484 477 477 LEU LEU A . n A 1 485 THR 485 478 478 THR THR A . n A 1 486 LYS 486 479 479 LYS LYS A . n A 1 487 GLU 487 480 480 GLU GLU A . n A 1 488 LEU 488 481 481 LEU LEU A . n A 1 489 LYS 489 482 482 LYS LYS A . n A 1 490 SER 490 483 483 SER SER A . n A 1 491 PRO 491 484 484 PRO PRO A . n A 1 492 ASP 492 485 485 ASP ASP A . n A 1 493 GLU 493 486 486 GLU GLU A . n A 1 494 GLY 494 487 487 GLY GLY A . n A 1 495 PHE 495 488 488 PHE PHE A . n A 1 496 GLU 496 489 489 GLU GLU A . n A 1 497 GLY 497 490 490 GLY GLY A . n A 1 498 LYS 498 491 491 LYS LYS A . n A 1 499 SER 499 492 492 SER SER A . n A 1 500 LEU 500 493 493 LEU LEU A . n A 1 501 TYR 501 494 494 TYR TYR A . n A 1 502 GLU 502 495 495 GLU GLU A . n A 1 503 SER 503 496 496 SER SER A . n A 1 504 TRP 504 497 497 TRP TRP A . n A 1 505 THR 505 498 498 THR THR A . n A 1 506 LYS 506 499 499 LYS LYS A . n A 1 507 LYS 507 500 500 LYS LYS A . n A 1 508 SER 508 501 501 SER SER A . n A 1 509 PRO 509 502 502 PRO PRO A . n A 1 510 SER 510 503 503 SER SER A . n A 1 511 PRO 511 504 504 PRO PRO A . n A 1 512 GLU 512 505 505 GLU GLU A . n A 1 513 PHE 513 506 506 PHE PHE A . n A 1 514 SER 514 507 507 SER SER A . n A 1 515 GLY 515 508 508 GLY GLY A . n A 1 516 MET 516 509 509 MET MET A . n A 1 517 PRO 517 510 510 PRO PRO A . n A 1 518 ARG 518 511 511 ARG ARG A . n A 1 519 ILE 519 512 512 ILE ILE A . n A 1 520 SER 520 513 513 SER SER A . n A 1 521 LYS 521 514 514 LYS LYS A . n A 1 522 LEU 522 515 515 LEU LEU A . n A 1 523 GLY 523 516 516 GLY GLY A . n A 1 524 SER 524 517 517 SER SER A . n A 1 525 GLY 525 518 518 GLY GLY A . n A 1 526 ASN 526 519 519 ASN ASN A . n A 1 527 ASP 527 520 520 ASP ASP A . n A 1 528 PHE 528 521 521 PHE PHE A . n A 1 529 GLU 529 522 522 GLU GLU A . n A 1 530 VAL 530 523 523 VAL VAL A . n A 1 531 PHE 531 524 524 PHE PHE A . n A 1 532 PHE 532 525 525 PHE PHE A . n A 1 533 GLN 533 526 526 GLN GLN A . n A 1 534 ARG 534 527 527 ARG ARG A . n A 1 535 LEU 535 528 528 LEU LEU A . n A 1 536 GLY 536 529 529 GLY GLY A . n A 1 537 ILE 537 530 530 ILE ILE A . n A 1 538 ALA 538 531 531 ALA ALA A . n A 1 539 SER 539 532 532 SER SER A . n A 1 540 GLY 540 533 533 GLY GLY A . n A 1 541 ARG 541 534 534 ARG ARG A . n A 1 542 ALA 542 535 535 ALA ALA A . n A 1 543 ARG 543 536 536 ARG ARG A . n A 1 544 TYR 544 537 537 TYR TYR A . n A 1 545 THR 545 538 538 THR THR A . n A 1 546 LYS 546 539 539 LYS LYS A . n A 1 547 ASN 547 540 540 ASN ASN A . n A 1 548 TRP 548 541 541 TRP TRP A . n A 1 549 GLU 549 542 542 GLU GLU A . n A 1 550 THR 550 543 543 THR THR A . n A 1 551 ASN 551 544 544 ASN ASN A . n A 1 552 LYS 552 545 545 LYS LYS A . n A 1 553 PHE 553 546 546 PHE PHE A . n A 1 554 SER 554 547 547 SER SER A . n A 1 555 GLY 555 548 548 GLY GLY A . n A 1 556 TYR 556 549 549 TYR TYR A . n A 1 557 PRO 557 550 550 PRO PRO A . n A 1 558 LEU 558 551 551 LEU LEU A . n A 1 559 TYR 559 552 552 TYR TYR A . n A 1 560 HIS 560 553 553 HIS HIS A . n A 1 561 SER 561 554 554 SER SER A . n A 1 562 VAL 562 555 555 VAL VAL A . n A 1 563 TYR 563 556 556 TYR TYR A . n A 1 564 GLU 564 557 557 GLU GLU A . n A 1 565 THR 565 558 558 THR THR A . n A 1 566 TYR 566 559 559 TYR TYR A . n A 1 567 GLU 567 560 560 GLU GLU A . n A 1 568 LEU 568 561 561 LEU LEU A . n A 1 569 VAL 569 562 562 VAL VAL A . n A 1 570 GLU 570 563 563 GLU GLU A . n A 1 571 LYS 571 564 564 LYS LYS A . n A 1 572 PHE 572 565 565 PHE PHE A . n A 1 573 TYR 573 566 566 TYR TYR A . n A 1 574 ASP 574 567 567 ASP ASP A . n A 1 575 PRO 575 568 568 PRO PRO A . n A 1 576 MET 576 569 569 MET MET A . n A 1 577 PHE 577 570 570 PHE PHE A . n A 1 578 LYS 578 571 571 LYS LYS A . n A 1 579 TYR 579 572 572 TYR TYR A . n A 1 580 HIS 580 573 573 HIS HIS A . n A 1 581 LEU 581 574 574 LEU LEU A . n A 1 582 THR 582 575 575 THR THR A . n A 1 583 VAL 583 576 576 VAL VAL A . n A 1 584 ALA 584 577 577 ALA ALA A . n A 1 585 GLN 585 578 578 GLN GLN A . n A 1 586 VAL 586 579 579 VAL VAL A . n A 1 587 ARG 587 580 580 ARG ARG A . n A 1 588 GLY 588 581 581 GLY GLY A . n A 1 589 GLY 589 582 582 GLY GLY A . n A 1 590 MET 590 583 583 MET MET A . n A 1 591 VAL 591 584 584 VAL VAL A . n A 1 592 PHE 592 585 585 PHE PHE A . n A 1 593 GLU 593 586 586 GLU GLU A . n A 1 594 LEU 594 587 587 LEU LEU A . n A 1 595 ALA 595 588 588 ALA ALA A . n A 1 596 ASN 596 589 589 ASN ASN A . n A 1 597 SER 597 590 590 SER SER A . n A 1 598 ILE 598 591 591 ILE ILE A . n A 1 599 VAL 599 592 592 VAL VAL A . n A 1 600 LEU 600 593 593 LEU LEU A . n A 1 601 PRO 601 594 594 PRO PRO A . n A 1 602 PHE 602 595 595 PHE PHE A . n A 1 603 ASP 603 596 596 ASP ASP A . n A 1 604 CYS 604 597 597 CYS CYS A . n A 1 605 ARG 605 598 598 ARG ARG A . n A 1 606 ASP 606 599 599 ASP ASP A . n A 1 607 TYR 607 600 600 TYR TYR A . n A 1 608 ALA 608 601 601 ALA ALA A . n A 1 609 VAL 609 602 602 VAL VAL A . n A 1 610 VAL 610 603 603 VAL VAL A . n A 1 611 LEU 611 604 604 LEU LEU A . n A 1 612 ARG 612 605 605 ARG ARG A . n A 1 613 LYS 613 606 606 LYS LYS A . n A 1 614 TYR 614 607 607 TYR TYR A . n A 1 615 ALA 615 608 608 ALA ALA A . n A 1 616 ASP 616 609 609 ASP ASP A . n A 1 617 LYS 617 610 610 LYS LYS A . n A 1 618 ILE 618 611 611 ILE ILE A . n A 1 619 TYR 619 612 612 TYR TYR A . n A 1 620 SER 620 613 613 SER SER A . n A 1 621 ILE 621 614 614 ILE ILE A . n A 1 622 SER 622 615 615 SER SER A . n A 1 623 MET 623 616 616 MET MET A . n A 1 624 LYS 624 617 617 LYS LYS A . n A 1 625 HIS 625 618 618 HIS HIS A . n A 1 626 PRO 626 619 619 PRO PRO A . n A 1 627 GLN 627 620 620 GLN GLN A . n A 1 628 GLU 628 621 621 GLU GLU A . n A 1 629 MET 629 622 622 MET MET A . n A 1 630 LYS 630 623 623 LYS LYS A . n A 1 631 THR 631 624 624 THR THR A . n A 1 632 TYR 632 625 625 TYR TYR A . n A 1 633 SER 633 626 626 SER SER A . n A 1 634 VAL 634 627 627 VAL VAL A . n A 1 635 SER 635 628 628 SER SER A . n A 1 636 PHE 636 629 629 PHE PHE A . n A 1 637 ASP 637 630 630 ASP ASP A . n A 1 638 SER 638 631 631 SER SER A . n A 1 639 LEU 639 632 632 LEU LEU A . n A 1 640 PHE 640 633 633 PHE PHE A . n A 1 641 SER 641 634 634 SER SER A . n A 1 642 ALA 642 635 635 ALA ALA A . n A 1 643 VAL 643 636 636 VAL VAL A . n A 1 644 LYS 644 637 637 LYS LYS A . n A 1 645 ASN 645 638 638 ASN ASN A . n A 1 646 PHE 646 639 639 PHE PHE A . n A 1 647 THR 647 640 640 THR THR A . n A 1 648 GLU 648 641 641 GLU GLU A . n A 1 649 ILE 649 642 642 ILE ILE A . n A 1 650 ALA 650 643 643 ALA ALA A . n A 1 651 SER 651 644 644 SER SER A . n A 1 652 LYS 652 645 645 LYS LYS A . n A 1 653 PHE 653 646 646 PHE PHE A . n A 1 654 SER 654 647 647 SER SER A . n A 1 655 GLU 655 648 648 GLU GLU A . n A 1 656 ARG 656 649 649 ARG ARG A . n A 1 657 LEU 657 650 650 LEU LEU A . n A 1 658 GLN 658 651 651 GLN GLN A . n A 1 659 ASP 659 652 652 ASP ASP A . n A 1 660 PHE 660 653 653 PHE PHE A . n A 1 661 ASP 661 654 ? ? ? A . n A 1 662 LYS 662 655 ? ? ? A . n A 1 663 SER 663 656 656 SER SER A . n A 1 664 ASN 664 657 657 ASN ASN A . n A 1 665 PRO 665 658 658 PRO PRO A . n A 1 666 ILE 666 659 659 ILE ILE A . n A 1 667 VAL 667 660 660 VAL VAL A . n A 1 668 LEU 668 661 661 LEU LEU A . n A 1 669 ARG 669 662 662 ARG ARG A . n A 1 670 MET 670 663 663 MET MET A . n A 1 671 MET 671 664 664 MET MET A . n A 1 672 ASN 672 665 665 ASN ASN A . n A 1 673 ASP 673 666 666 ASP ASP A . n A 1 674 GLN 674 667 667 GLN GLN A . n A 1 675 LEU 675 668 668 LEU LEU A . n A 1 676 MET 676 669 669 MET MET A . n A 1 677 PHE 677 670 670 PHE PHE A . n A 1 678 LEU 678 671 671 LEU LEU A . n A 1 679 GLU 679 672 672 GLU GLU A . n A 1 680 ARG 680 673 673 ARG ARG A . n A 1 681 ALA 681 674 674 ALA ALA A . n A 1 682 PHE 682 675 675 PHE PHE A . n A 1 683 ILE 683 676 676 ILE ILE A . n A 1 684 ASP 684 677 677 ASP ASP A . n A 1 685 PRO 685 678 678 PRO PRO A . n A 1 686 LEU 686 679 679 LEU LEU A . n A 1 687 GLY 687 680 680 GLY GLY A . n A 1 688 LEU 688 681 681 LEU LEU A . n A 1 689 PRO 689 682 682 PRO PRO A . n A 1 690 ASP 690 683 683 ASP ASP A . n A 1 691 ARG 691 684 684 ARG ARG A . n A 1 692 PRO 692 685 685 PRO PRO A . n A 1 693 PHE 693 686 686 PHE PHE A . n A 1 694 TYR 694 687 687 TYR TYR A . n A 1 695 ARG 695 688 688 ARG ARG A . n A 1 696 HIS 696 689 689 HIS HIS A . n A 1 697 VAL 697 690 690 VAL VAL A . n A 1 698 ILE 698 691 691 ILE ILE A . n A 1 699 TYR 699 692 692 TYR TYR A . n A 1 700 ALA 700 693 693 ALA ALA A . n A 1 701 PRO 701 694 694 PRO PRO A . n A 1 702 SER 702 695 695 SER SER A . n A 1 703 SER 703 696 696 SER SER A . n A 1 704 HIS 704 697 697 HIS HIS A . n A 1 705 ASN 705 698 698 ASN ASN A . n A 1 706 LYS 706 699 699 LYS LYS A . n A 1 707 TYR 707 700 700 TYR TYR A . n A 1 708 ALA 708 701 701 ALA ALA A . n A 1 709 GLY 709 702 702 GLY GLY A . n A 1 710 GLU 710 703 703 GLU GLU A . n A 1 711 SER 711 704 704 SER SER A . n A 1 712 PHE 712 705 705 PHE PHE A . n A 1 713 PRO 713 706 706 PRO PRO A . n A 1 714 GLY 714 707 707 GLY GLY A . n A 1 715 ILE 715 708 708 ILE ILE A . n A 1 716 TYR 716 709 709 TYR TYR A . n A 1 717 ASP 717 710 710 ASP ASP A . n A 1 718 ALA 718 711 711 ALA ALA A . n A 1 719 LEU 719 712 712 LEU LEU A . n A 1 720 PHE 720 713 713 PHE PHE A . n A 1 721 ASP 721 714 714 ASP ASP A . n A 1 722 ILE 722 715 715 ILE ILE A . n A 1 723 GLU 723 716 716 GLU GLU A . n A 1 724 SER 724 717 717 SER SER A . n A 1 725 LYS 725 718 718 LYS LYS A . n A 1 726 VAL 726 719 719 VAL VAL A . n A 1 727 ASP 727 720 720 ASP ASP A . n A 1 728 PRO 728 721 721 PRO PRO A . n A 1 729 SER 729 722 722 SER SER A . n A 1 730 LYS 730 723 723 LYS LYS A . n A 1 731 ALA 731 724 724 ALA ALA A . n A 1 732 TRP 732 725 725 TRP TRP A . n A 1 733 GLY 733 726 726 GLY GLY A . n A 1 734 GLU 734 727 727 GLU GLU A . n A 1 735 VAL 735 728 728 VAL VAL A . n A 1 736 LYS 736 729 729 LYS LYS A . n A 1 737 ARG 737 730 730 ARG ARG A . n A 1 738 GLN 738 731 731 GLN GLN A . n A 1 739 ILE 739 732 732 ILE ILE A . n A 1 740 TYR 740 733 733 TYR TYR A . n A 1 741 VAL 741 734 734 VAL VAL A . n A 1 742 ALA 742 735 735 ALA ALA A . n A 1 743 ALA 743 736 736 ALA ALA A . n A 1 744 PHE 744 737 737 PHE PHE A . n A 1 745 THR 745 738 738 THR THR A . n A 1 746 VAL 746 739 739 VAL VAL A . n A 1 747 GLN 747 740 740 GLN GLN A . n A 1 748 ALA 748 741 741 ALA ALA A . n A 1 749 ALA 749 742 742 ALA ALA A . n A 1 750 ALA 750 743 743 ALA ALA A . n A 1 751 GLU 751 744 744 GLU GLU A . n A 1 752 THR 752 745 745 THR THR A . n A 1 753 LEU 753 746 746 LEU LEU A . n A 1 754 SER 754 747 747 SER SER A . n A 1 755 GLU 755 748 748 GLU GLU A . n A 1 756 VAL 756 749 749 VAL VAL A . n A 1 757 ALA 757 750 750 ALA ALA A . n # _pdbx_molecule_features.prd_id PRD_001163 _pdbx_molecule_features.name ;N-(4-{[(2-AMINO-4-OXO-3,4-DIHYDROPTERIDIN-6-YL)METHYL]AMINO}BENZOYL)-L-GAMMA-GLUTAMYL-L-GAMMA-GLUTAMYL-L-GAMMA-GLUTAMYL-L-GLUTAMIC ACID ; _pdbx_molecule_features.type Peptide-like _pdbx_molecule_features.class Inhibitor _pdbx_molecule_features.details ? # _pdbx_molecule.instance_id 1 _pdbx_molecule.prd_id PRD_001163 _pdbx_molecule.asym_id S # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 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 147 A ASN 140 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 466 A ASN 459 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 128 A ASN 121 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 202 A ASN 195 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 11870 ? 1 MORE -57 ? 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 129.8300000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? T HOH . ? A HOH 1339 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 105.9 ? 2 O ? T HOH . ? A HOH 1339 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 112.5 ? 3 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 119.2 ? 4 O ? T HOH . ? A HOH 1339 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 110.5 ? 5 OD1 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 105.7 ? 6 OD2 ? A ASP 460 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 NE2 ? A HIS 384 ? A HIS 377 ? 1_555 102.7 ? 7 O ? T HOH . ? A HOH 1339 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 96.8 ? 8 O ? T HOH . ? A HOH 1339 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 161.7 ? 9 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 90.7 ? 10 O ? T HOH . ? A HOH 1339 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 95.5 ? 11 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 97.3 ? 12 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 100.1 ? 13 O ? T HOH . ? A HOH 1339 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAG ? S 29D . ? A 29D 818 ? 1_555 76.2 ? 14 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAG ? S 29D . ? A 29D 818 ? 1_555 105.6 ? 15 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAG ? S 29D . ? A 29D 818 ? 1_555 85.7 ? 16 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAG ? S 29D . ? A 29D 818 ? 1_555 156.3 ? 17 O ? T HOH . ? A HOH 1339 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 89.5 ? 18 OD2 ? A ASP 394 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 155.6 ? 19 NE2 ? A HIS 560 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 90.6 ? 20 OE2 ? A GLU 432 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 58.5 ? 21 OAG ? S 29D . ? A 29D 818 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 432 ? A GLU 425 ? 1_555 98.8 ? 22 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A TYR 279 ? A TYR 272 ? 1_555 80.1 ? 23 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 93.5 ? 24 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 86.0 ? 25 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 96.9 ? 26 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 144.3 ? 27 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 906 ? 1_555 129.7 ? 28 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 102.4 ? 29 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 72.6 ? 30 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 150.4 ? 31 O ? T HOH . ? A HOH 906 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A THR 276 ? A THR 269 ? 1_555 73.4 ? 32 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 170.9 ? 33 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 90.9 ? 34 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 87.3 ? 35 O ? T HOH . ? A HOH 906 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 89.5 ? 36 O ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 276 ? A THR 269 ? 1_555 73.1 ? 37 OE2 ? A GLU 443 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 88.3 ? 38 O ? A TYR 279 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 137.9 ? 39 OE1 ? A GLU 440 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 54.3 ? 40 O ? T HOH . ? A HOH 906 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 77.0 ? 41 O ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 149.4 ? 42 OG1 ? A THR 276 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 440 ? A GLU 433 ? 1_555 99.5 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2014-06-18 2 'Structure model' 1 1 2014-08-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 17.7355 _pdbx_refine_tls.origin_y 49.6081 _pdbx_refine_tls.origin_z 44.6032 _pdbx_refine_tls.T[1][1] 0.0076 _pdbx_refine_tls.T[2][2] 0.0099 _pdbx_refine_tls.T[3][3] 0.0136 _pdbx_refine_tls.T[1][2] 0.0025 _pdbx_refine_tls.T[1][3] -0.0014 _pdbx_refine_tls.T[2][3] -0.0066 _pdbx_refine_tls.L[1][1] 0.1704 _pdbx_refine_tls.L[2][2] 0.2724 _pdbx_refine_tls.L[3][3] 0.1320 _pdbx_refine_tls.L[1][2] -0.0764 _pdbx_refine_tls.L[1][3] -0.0027 _pdbx_refine_tls.L[2][3] 0.0182 _pdbx_refine_tls.S[1][1] -0.0163 _pdbx_refine_tls.S[2][2] 0.0189 _pdbx_refine_tls.S[3][3] -0.0026 _pdbx_refine_tls.S[1][2] 0.0062 _pdbx_refine_tls.S[1][3] -0.0077 _pdbx_refine_tls.S[2][3] -0.0471 _pdbx_refine_tls.S[2][1] 0.0052 _pdbx_refine_tls.S[3][1] 0.0080 _pdbx_refine_tls.S[3][2] 0.0151 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 56 A 750 ? . . . . ? 'X-RAY DIFFRACTION' 2 1 A 801 A 818 ? . . . . ? 'X-RAY DIFFRACTION' 3 1 A 901 A 1510 ? . . . . ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal SERGUI 'data collection' . ? 1 REFMAC refinement . ? 2 HKL-2000 'data reduction' . ? 3 HKL-2000 'data scaling' . ? 4 REFMAC phasing . ? 5 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O4 A NAG 815 ? ? O5 A BMA 816 ? ? 2.05 2 1 NH2 A ARG 688 ? B O A HOH 969 ? ? 2.05 3 1 OH A TYR 242 ? ? O A HOH 1273 ? ? 2.18 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 OE1 A GLU 425 ? ? CD A GLU 425 ? ? OE2 A GLU 425 ? ? 113.57 123.30 -9.73 1.20 N 2 1 NE A ARG 440 ? ? CZ A ARG 440 ? ? NH2 A ARG 440 ? ? 117.07 120.30 -3.23 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 PHE A 164 ? ? 86.06 5.43 2 1 ASN A 178 ? ? 56.81 -126.96 3 1 LYS A 207 ? ? 72.12 -47.11 4 1 VAL A 382 ? ? -128.84 -108.23 5 1 ALA A 452 ? ? -154.83 57.14 6 1 ASP A 453 ? ? -81.74 -157.29 7 1 SER A 454 ? ? -37.05 126.85 8 1 SER A 454 ? ? -39.50 128.29 9 1 ASP A 567 ? ? -154.74 65.52 10 1 ASN A 698 ? ? -168.94 96.52 11 1 PHE A 705 ? ? 37.97 57.29 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A MET -6 ? A MET 1 2 1 Y 1 A LYS -5 ? A LYS 2 3 1 Y 1 A LEU -4 ? A LEU 3 4 1 Y 1 A CYS -3 ? A CYS 4 5 1 Y 1 A ILE -2 ? A ILE 5 6 1 Y 1 A LEU -1 ? A LEU 6 7 1 Y 1 A LEU 0 ? A LEU 7 8 1 Y 1 A ALA 1 ? A ALA 8 9 1 Y 1 A VAL 2 ? A VAL 9 10 1 Y 1 A VAL 3 ? A VAL 10 11 1 Y 1 A ALA 4 ? A ALA 11 12 1 Y 1 A PHE 5 ? A PHE 12 13 1 Y 1 A VAL 6 ? A VAL 13 14 1 Y 1 A GLY 7 ? A GLY 14 15 1 Y 1 A LEU 8 ? A LEU 15 16 1 Y 1 A SER 9 ? A SER 16 17 1 Y 1 A LEU 10 ? A LEU 17 18 1 Y 1 A GLY 11 ? A GLY 18 19 1 Y 1 A ARG 12 ? A ARG 19 20 1 Y 1 A SER 13 ? A SER 20 21 1 Y 1 A GLY 14 ? A GLY 21 22 1 Y 1 A LEU 15 ? A LEU 22 23 1 Y 1 A ASN 16 ? A ASN 23 24 1 Y 1 A ASP 17 ? A ASP 24 25 1 Y 1 A ILE 18 ? A ILE 25 26 1 Y 1 A PHE 19 ? A PHE 26 27 1 Y 1 A GLU 20 ? A GLU 27 28 1 Y 1 A ALA 21 ? A ALA 28 29 1 Y 1 A GLN 22 ? A GLN 29 30 1 Y 1 A LYS 23 ? A LYS 30 31 1 Y 1 A ILE 24 ? A ILE 31 32 1 Y 1 A GLU 25 ? A GLU 32 33 1 Y 1 A TRP 26 ? A TRP 33 34 1 Y 1 A HIS 27 ? A HIS 34 35 1 Y 1 A GLU 28 ? A GLU 35 36 1 Y 1 A GLY 29 ? A GLY 36 37 1 Y 1 A SER 30 ? A SER 37 38 1 Y 1 A GLY 31 ? A GLY 38 39 1 Y 1 A SER 32 ? A SER 39 40 1 Y 1 A GLY 33 ? A GLY 40 41 1 Y 1 A SER 34 ? A SER 41 42 1 Y 1 A GLU 35 ? A GLU 42 43 1 Y 1 A ASN 36 ? A ASN 43 44 1 Y 1 A LEU 37 ? A LEU 44 45 1 Y 1 A TYR 38 ? A TYR 45 46 1 Y 1 A PHE 39 ? A PHE 46 47 1 Y 1 A GLN 40 ? A GLN 47 48 1 Y 1 A GLY 41 ? A GLY 48 49 1 Y 1 A ARG 42 ? A ARG 49 50 1 Y 1 A SER 43 ? A SER 50 51 1 Y 1 A LYS 44 ? A LYS 51 52 1 Y 1 A SER 45 ? A SER 52 53 1 Y 1 A SER 46 ? A SER 53 54 1 Y 1 A ASN 47 ? A ASN 54 55 1 Y 1 A GLU 48 ? A GLU 55 56 1 Y 1 A ALA 49 ? A ALA 56 57 1 Y 1 A THR 50 ? A THR 57 58 1 Y 1 A ASN 51 ? A ASN 58 59 1 Y 1 A ILE 52 ? A ILE 59 60 1 Y 1 A THR 53 ? A THR 60 61 1 Y 1 A PRO 54 ? A PRO 61 62 1 Y 1 A LYS 55 ? A LYS 62 63 1 Y 1 A ASP 654 ? A ASP 661 64 1 Y 1 A LYS 655 ? A LYS 662 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'ZINC ION' ZN 3 'CALCIUM ION' CA 4 'CHLORIDE ION' CL 5 N-ACETYL-D-GLUCOSAMINE NAG 6 BETA-D-MANNOSE BMA 7 ALPHA-D-MANNOSE MAN 8 ;N-(4-{[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino}benzoyl)-L-gamma-glutamyl-L-gamma-glutamyl-L-gamma-glutamyl-L-glutamic acid ; 29D 9 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 ZN 1 801 801 ZN ZN A . C 2 ZN 1 802 802 ZN ZN A . D 3 CA 1 803 803 CA CA A . E 4 CL 1 804 804 CL CL A . F 5 NAG 1 805 805 NAG NAG A . G 5 NAG 2 806 806 NAG NAG A . H 5 NAG 1 807 807 NAG NAG A . I 5 NAG 1 808 808 NAG NAG A . J 5 NAG 2 809 809 NAG NAG A . K 5 NAG 1 810 810 NAG NAG A . L 5 NAG 1 811 811 NAG NAG A . M 5 NAG 1 812 812 NAG NAG A . N 5 NAG 2 813 813 NAG NAG A . O 5 NAG 1 814 814 NAG NAG A . P 5 NAG 2 815 815 NAG NAG A . Q 6 BMA 3 816 816 BMA BMA A . R 7 MAN 4 817 817 MAN MAN A . S 8 29D 1 818 818 29D 29D A . T 9 HOH 1 901 901 HOH HOH A . T 9 HOH 2 902 902 HOH HOH A . T 9 HOH 3 903 903 HOH HOH A . T 9 HOH 4 904 904 HOH HOH A . T 9 HOH 5 905 905 HOH HOH A . T 9 HOH 6 906 906 HOH HOH A . T 9 HOH 7 907 907 HOH HOH A . T 9 HOH 8 908 908 HOH HOH A . T 9 HOH 9 909 909 HOH HOH A . T 9 HOH 10 910 910 HOH HOH A . T 9 HOH 11 911 911 HOH HOH A . T 9 HOH 12 912 912 HOH HOH A . T 9 HOH 13 913 913 HOH HOH A . T 9 HOH 14 914 914 HOH HOH A . T 9 HOH 15 915 915 HOH HOH A . T 9 HOH 16 916 916 HOH HOH A . T 9 HOH 17 917 917 HOH HOH A . T 9 HOH 18 918 918 HOH HOH A . T 9 HOH 19 919 919 HOH HOH A . T 9 HOH 20 920 920 HOH HOH A . T 9 HOH 21 921 921 HOH HOH A . T 9 HOH 22 922 922 HOH HOH A . T 9 HOH 23 923 923 HOH HOH A . T 9 HOH 24 924 924 HOH HOH A . T 9 HOH 25 925 925 HOH HOH A . T 9 HOH 26 926 926 HOH HOH A . T 9 HOH 27 927 927 HOH HOH A . T 9 HOH 28 928 928 HOH HOH A . T 9 HOH 29 929 929 HOH HOH A . T 9 HOH 30 930 930 HOH HOH A . T 9 HOH 31 931 931 HOH HOH A . T 9 HOH 32 932 932 HOH HOH A . T 9 HOH 33 933 933 HOH HOH A . T 9 HOH 34 934 934 HOH HOH A . T 9 HOH 35 935 935 HOH HOH A . T 9 HOH 36 936 936 HOH HOH A . T 9 HOH 37 937 937 HOH HOH A . T 9 HOH 38 938 938 HOH HOH A . T 9 HOH 39 939 939 HOH HOH A . T 9 HOH 40 940 940 HOH HOH A . T 9 HOH 41 941 941 HOH HOH A . T 9 HOH 42 942 942 HOH HOH A . T 9 HOH 43 943 943 HOH HOH A . T 9 HOH 44 944 944 HOH HOH A . T 9 HOH 45 945 945 HOH HOH A . T 9 HOH 46 946 946 HOH HOH A . T 9 HOH 47 947 947 HOH HOH A . T 9 HOH 48 948 948 HOH HOH A . T 9 HOH 49 949 949 HOH HOH A . T 9 HOH 50 950 950 HOH HOH A . T 9 HOH 51 951 951 HOH HOH A . T 9 HOH 52 952 952 HOH HOH A . T 9 HOH 53 953 953 HOH HOH A . T 9 HOH 54 954 954 HOH HOH A . T 9 HOH 55 955 955 HOH HOH A . T 9 HOH 56 956 956 HOH HOH A . T 9 HOH 57 957 957 HOH HOH A . T 9 HOH 58 958 958 HOH HOH A . T 9 HOH 59 959 959 HOH HOH A . T 9 HOH 60 960 960 HOH HOH A . T 9 HOH 61 961 961 HOH HOH A . T 9 HOH 62 962 962 HOH HOH A . T 9 HOH 63 963 963 HOH HOH A . T 9 HOH 64 964 964 HOH HOH A . T 9 HOH 65 965 965 HOH HOH A . T 9 HOH 66 966 966 HOH HOH A . T 9 HOH 67 967 967 HOH HOH A . T 9 HOH 68 968 968 HOH HOH A . T 9 HOH 69 969 969 HOH HOH A . T 9 HOH 70 970 970 HOH HOH A . T 9 HOH 71 971 971 HOH HOH A . T 9 HOH 72 972 972 HOH HOH A . T 9 HOH 73 973 973 HOH HOH A . T 9 HOH 74 974 974 HOH HOH A . T 9 HOH 75 975 975 HOH HOH A . T 9 HOH 76 976 976 HOH HOH A . T 9 HOH 77 977 977 HOH HOH A . T 9 HOH 78 978 978 HOH HOH A . T 9 HOH 79 979 979 HOH HOH A . T 9 HOH 80 980 980 HOH HOH A . T 9 HOH 81 981 981 HOH HOH A . T 9 HOH 82 982 982 HOH HOH A . T 9 HOH 83 983 983 HOH HOH A . T 9 HOH 84 984 984 HOH HOH A . T 9 HOH 85 985 985 HOH HOH A . T 9 HOH 86 986 986 HOH HOH A . T 9 HOH 87 987 987 HOH HOH A . T 9 HOH 88 988 988 HOH HOH A . T 9 HOH 89 989 989 HOH HOH A . T 9 HOH 90 990 990 HOH HOH A . T 9 HOH 91 991 991 HOH HOH A . T 9 HOH 92 992 992 HOH HOH A . T 9 HOH 93 993 993 HOH HOH A . T 9 HOH 94 994 994 HOH HOH A . T 9 HOH 95 995 995 HOH HOH A . T 9 HOH 96 996 996 HOH HOH A . T 9 HOH 97 997 997 HOH HOH A . T 9 HOH 98 998 998 HOH HOH A . T 9 HOH 99 999 999 HOH HOH A . T 9 HOH 100 1000 1000 HOH HOH A . T 9 HOH 101 1001 1001 HOH HOH A . T 9 HOH 102 1002 1002 HOH HOH A . T 9 HOH 103 1003 1003 HOH HOH A . T 9 HOH 104 1004 1004 HOH HOH A . T 9 HOH 105 1005 1005 HOH HOH A . T 9 HOH 106 1006 1006 HOH HOH A . T 9 HOH 107 1007 1007 HOH HOH A . T 9 HOH 108 1008 1008 HOH HOH A . T 9 HOH 109 1009 1009 HOH HOH A . T 9 HOH 110 1010 1010 HOH HOH A . T 9 HOH 111 1011 1011 HOH HOH A . T 9 HOH 112 1012 1012 HOH HOH A . T 9 HOH 113 1013 1013 HOH HOH A . T 9 HOH 114 1014 1014 HOH HOH A . T 9 HOH 115 1015 1015 HOH HOH A . T 9 HOH 116 1016 1016 HOH HOH A . T 9 HOH 117 1017 1017 HOH HOH A . T 9 HOH 118 1018 1018 HOH HOH A . T 9 HOH 119 1019 1019 HOH HOH A . T 9 HOH 120 1020 1020 HOH HOH A . T 9 HOH 121 1021 1021 HOH HOH A . T 9 HOH 122 1022 1022 HOH HOH A . T 9 HOH 123 1023 1023 HOH HOH A . T 9 HOH 124 1024 1024 HOH HOH A . T 9 HOH 125 1025 1025 HOH HOH A . T 9 HOH 126 1026 1026 HOH HOH A . T 9 HOH 127 1027 1027 HOH HOH A . T 9 HOH 128 1028 1028 HOH HOH A . T 9 HOH 129 1029 1029 HOH HOH A . T 9 HOH 130 1030 1030 HOH HOH A . T 9 HOH 131 1031 1031 HOH HOH A . T 9 HOH 132 1032 1032 HOH HOH A . T 9 HOH 133 1033 1033 HOH HOH A . T 9 HOH 134 1034 1034 HOH HOH A . T 9 HOH 135 1035 1035 HOH HOH A . T 9 HOH 136 1036 1036 HOH HOH A . T 9 HOH 137 1037 1037 HOH HOH A . T 9 HOH 138 1038 1038 HOH HOH A . T 9 HOH 139 1039 1039 HOH HOH A . T 9 HOH 140 1040 1040 HOH HOH A . T 9 HOH 141 1041 1041 HOH HOH A . T 9 HOH 142 1042 1042 HOH HOH A . T 9 HOH 143 1043 1043 HOH HOH A . T 9 HOH 144 1044 1044 HOH HOH A . T 9 HOH 145 1045 1045 HOH HOH A . T 9 HOH 146 1046 1046 HOH HOH A . T 9 HOH 147 1047 1047 HOH HOH A . T 9 HOH 148 1048 1048 HOH HOH A . T 9 HOH 149 1049 1049 HOH HOH A . T 9 HOH 150 1050 1050 HOH HOH A . T 9 HOH 151 1051 1051 HOH HOH A . T 9 HOH 152 1052 1052 HOH HOH A . T 9 HOH 153 1053 1053 HOH HOH A . T 9 HOH 154 1054 1054 HOH HOH A . T 9 HOH 155 1055 1055 HOH HOH A . T 9 HOH 156 1056 1056 HOH HOH A . T 9 HOH 157 1057 1057 HOH HOH A . T 9 HOH 158 1058 1058 HOH HOH A . T 9 HOH 159 1059 1059 HOH HOH A . T 9 HOH 160 1060 1060 HOH HOH A . T 9 HOH 161 1061 1061 HOH HOH A . T 9 HOH 162 1062 1062 HOH HOH A . T 9 HOH 163 1063 1063 HOH HOH A . T 9 HOH 164 1064 1064 HOH HOH A . T 9 HOH 165 1065 1065 HOH HOH A . T 9 HOH 166 1066 1066 HOH HOH A . T 9 HOH 167 1067 1067 HOH HOH A . T 9 HOH 168 1068 1068 HOH HOH A . T 9 HOH 169 1069 1069 HOH HOH A . T 9 HOH 170 1070 1070 HOH HOH A . T 9 HOH 171 1071 1071 HOH HOH A . T 9 HOH 172 1072 1072 HOH HOH A . T 9 HOH 173 1073 1073 HOH HOH A . T 9 HOH 174 1074 1074 HOH HOH A . T 9 HOH 175 1075 1075 HOH HOH A . T 9 HOH 176 1076 1076 HOH HOH A . T 9 HOH 177 1077 1077 HOH HOH A . T 9 HOH 178 1078 1078 HOH HOH A . T 9 HOH 179 1079 1079 HOH HOH A . T 9 HOH 180 1080 1080 HOH HOH A . T 9 HOH 181 1081 1081 HOH HOH A . T 9 HOH 182 1082 1082 HOH HOH A . T 9 HOH 183 1083 1083 HOH HOH A . T 9 HOH 184 1084 1084 HOH HOH A . T 9 HOH 185 1085 1085 HOH HOH A . T 9 HOH 186 1086 1086 HOH HOH A . T 9 HOH 187 1087 1087 HOH HOH A . T 9 HOH 188 1088 1088 HOH HOH A . T 9 HOH 189 1089 1089 HOH HOH A . T 9 HOH 190 1090 1090 HOH HOH A . T 9 HOH 191 1091 1091 HOH HOH A . T 9 HOH 192 1092 1092 HOH HOH A . T 9 HOH 193 1093 1093 HOH HOH A . T 9 HOH 194 1094 1094 HOH HOH A . T 9 HOH 195 1095 1095 HOH HOH A . T 9 HOH 196 1096 1096 HOH HOH A . T 9 HOH 197 1097 1097 HOH HOH A . T 9 HOH 198 1098 1098 HOH HOH A . T 9 HOH 199 1099 1099 HOH HOH A . T 9 HOH 200 1100 1100 HOH HOH A . T 9 HOH 201 1101 1101 HOH HOH A . T 9 HOH 202 1102 1102 HOH HOH A . T 9 HOH 203 1103 1103 HOH HOH A . T 9 HOH 204 1104 1104 HOH HOH A . T 9 HOH 205 1105 1105 HOH HOH A . T 9 HOH 206 1106 1106 HOH HOH A . T 9 HOH 207 1107 1107 HOH HOH A . T 9 HOH 208 1108 1108 HOH HOH A . T 9 HOH 209 1109 1109 HOH HOH A . T 9 HOH 210 1110 1110 HOH HOH A . T 9 HOH 211 1111 1111 HOH HOH A . T 9 HOH 212 1112 1112 HOH HOH A . T 9 HOH 213 1113 1113 HOH HOH A . T 9 HOH 214 1114 1114 HOH HOH A . T 9 HOH 215 1115 1115 HOH HOH A . T 9 HOH 216 1116 1116 HOH HOH A . T 9 HOH 217 1117 1117 HOH HOH A . T 9 HOH 218 1118 1118 HOH HOH A . T 9 HOH 219 1119 1119 HOH HOH A . T 9 HOH 220 1120 1120 HOH HOH A . T 9 HOH 221 1121 1121 HOH HOH A . T 9 HOH 222 1122 1122 HOH HOH A . T 9 HOH 223 1123 1123 HOH HOH A . T 9 HOH 224 1124 1124 HOH HOH A . T 9 HOH 225 1125 1125 HOH HOH A . T 9 HOH 226 1126 1126 HOH HOH A . T 9 HOH 227 1127 1127 HOH HOH A . T 9 HOH 228 1128 1128 HOH HOH A . T 9 HOH 229 1129 1129 HOH HOH A . T 9 HOH 230 1130 1130 HOH HOH A . T 9 HOH 231 1131 1131 HOH HOH A . T 9 HOH 232 1132 1132 HOH HOH A . T 9 HOH 233 1133 1133 HOH HOH A . T 9 HOH 234 1134 1134 HOH HOH A . T 9 HOH 235 1135 1135 HOH HOH A . T 9 HOH 236 1136 1136 HOH HOH A . T 9 HOH 237 1137 1137 HOH HOH A . T 9 HOH 238 1138 1138 HOH HOH A . T 9 HOH 239 1139 1139 HOH HOH A . T 9 HOH 240 1140 1140 HOH HOH A . T 9 HOH 241 1141 1141 HOH HOH A . T 9 HOH 242 1142 1142 HOH HOH A . T 9 HOH 243 1143 1143 HOH HOH A . T 9 HOH 244 1144 1144 HOH HOH A . T 9 HOH 245 1145 1145 HOH HOH A . T 9 HOH 246 1146 1146 HOH HOH A . T 9 HOH 247 1147 1147 HOH HOH A . T 9 HOH 248 1148 1148 HOH HOH A . T 9 HOH 249 1149 1149 HOH HOH A . T 9 HOH 250 1150 1150 HOH HOH A . T 9 HOH 251 1151 1151 HOH HOH A . T 9 HOH 252 1152 1152 HOH HOH A . T 9 HOH 253 1153 1153 HOH HOH A . T 9 HOH 254 1154 1154 HOH HOH A . T 9 HOH 255 1155 1155 HOH HOH A . T 9 HOH 256 1156 1156 HOH HOH A . T 9 HOH 257 1157 1157 HOH HOH A . T 9 HOH 258 1158 1158 HOH HOH A . T 9 HOH 259 1159 1159 HOH HOH A . T 9 HOH 260 1160 1160 HOH HOH A . T 9 HOH 261 1161 1161 HOH HOH A . T 9 HOH 262 1162 1162 HOH HOH A . T 9 HOH 263 1163 1163 HOH HOH A . T 9 HOH 264 1164 1164 HOH HOH A . T 9 HOH 265 1165 1165 HOH HOH A . T 9 HOH 266 1166 1166 HOH HOH A . T 9 HOH 267 1167 1167 HOH HOH A . T 9 HOH 268 1168 1168 HOH HOH A . T 9 HOH 269 1169 1169 HOH HOH A . T 9 HOH 270 1170 1170 HOH HOH A . T 9 HOH 271 1171 1171 HOH HOH A . T 9 HOH 272 1172 1172 HOH HOH A . T 9 HOH 273 1173 1173 HOH HOH A . T 9 HOH 274 1174 1174 HOH HOH A . T 9 HOH 275 1175 1175 HOH HOH A . T 9 HOH 276 1176 1176 HOH HOH A . T 9 HOH 277 1177 1177 HOH HOH A . T 9 HOH 278 1178 1178 HOH HOH A . T 9 HOH 279 1179 1179 HOH HOH A . T 9 HOH 280 1180 1180 HOH HOH A . T 9 HOH 281 1181 1181 HOH HOH A . T 9 HOH 282 1182 1182 HOH HOH A . T 9 HOH 283 1183 1183 HOH HOH A . T 9 HOH 284 1184 1184 HOH HOH A . T 9 HOH 285 1185 1185 HOH HOH A . T 9 HOH 286 1186 1186 HOH HOH A . T 9 HOH 287 1187 1187 HOH HOH A . T 9 HOH 288 1188 1188 HOH HOH A . T 9 HOH 289 1189 1189 HOH HOH A . T 9 HOH 290 1190 1190 HOH HOH A . T 9 HOH 291 1191 1191 HOH HOH A . T 9 HOH 292 1192 1192 HOH HOH A . T 9 HOH 293 1193 1193 HOH HOH A . T 9 HOH 294 1194 1194 HOH HOH A . T 9 HOH 295 1195 1195 HOH HOH A . T 9 HOH 296 1196 1196 HOH HOH A . T 9 HOH 297 1197 1197 HOH HOH A . T 9 HOH 298 1198 1198 HOH HOH A . T 9 HOH 299 1199 1199 HOH HOH A . T 9 HOH 300 1200 1200 HOH HOH A . T 9 HOH 301 1201 1201 HOH HOH A . T 9 HOH 302 1202 1202 HOH HOH A . T 9 HOH 303 1203 1203 HOH HOH A . T 9 HOH 304 1204 1204 HOH HOH A . T 9 HOH 305 1205 1205 HOH HOH A . T 9 HOH 306 1206 1206 HOH HOH A . T 9 HOH 307 1207 1207 HOH HOH A . T 9 HOH 308 1208 1208 HOH HOH A . T 9 HOH 309 1209 1209 HOH HOH A . T 9 HOH 310 1210 1210 HOH HOH A . T 9 HOH 311 1211 1211 HOH HOH A . T 9 HOH 312 1212 1212 HOH HOH A . T 9 HOH 313 1213 1213 HOH HOH A . T 9 HOH 314 1214 1214 HOH HOH A . T 9 HOH 315 1215 1215 HOH HOH A . T 9 HOH 316 1216 1216 HOH HOH A . T 9 HOH 317 1217 1217 HOH HOH A . T 9 HOH 318 1218 1218 HOH HOH A . T 9 HOH 319 1219 1219 HOH HOH A . T 9 HOH 320 1220 1220 HOH HOH A . T 9 HOH 321 1221 1221 HOH HOH A . T 9 HOH 322 1222 1222 HOH HOH A . T 9 HOH 323 1223 1223 HOH HOH A . T 9 HOH 324 1224 1224 HOH HOH A . T 9 HOH 325 1225 1225 HOH HOH A . T 9 HOH 326 1226 1226 HOH HOH A . T 9 HOH 327 1227 1227 HOH HOH A . T 9 HOH 328 1228 1228 HOH HOH A . T 9 HOH 329 1229 1229 HOH HOH A . T 9 HOH 330 1230 1230 HOH HOH A . T 9 HOH 331 1231 1231 HOH HOH A . T 9 HOH 332 1232 1232 HOH HOH A . T 9 HOH 333 1233 1233 HOH HOH A . T 9 HOH 334 1234 1234 HOH HOH A . T 9 HOH 335 1235 1235 HOH HOH A . T 9 HOH 336 1236 1236 HOH HOH A . T 9 HOH 337 1237 1237 HOH HOH A . T 9 HOH 338 1238 1238 HOH HOH A . T 9 HOH 339 1239 1239 HOH HOH A . T 9 HOH 340 1240 1240 HOH HOH A . T 9 HOH 341 1241 1241 HOH HOH A . T 9 HOH 342 1242 1242 HOH HOH A . T 9 HOH 343 1243 1243 HOH HOH A . T 9 HOH 344 1244 1244 HOH HOH A . T 9 HOH 345 1245 1245 HOH HOH A . T 9 HOH 346 1246 1246 HOH HOH A . T 9 HOH 347 1247 1247 HOH HOH A . T 9 HOH 348 1248 1248 HOH HOH A . T 9 HOH 349 1249 1249 HOH HOH A . T 9 HOH 350 1250 1250 HOH HOH A . T 9 HOH 351 1251 1251 HOH HOH A . T 9 HOH 352 1252 1252 HOH HOH A . T 9 HOH 353 1253 1253 HOH HOH A . T 9 HOH 354 1254 1254 HOH HOH A . T 9 HOH 355 1255 1255 HOH HOH A . T 9 HOH 356 1256 1256 HOH HOH A . T 9 HOH 357 1257 1257 HOH HOH A . T 9 HOH 358 1258 1258 HOH HOH A . T 9 HOH 359 1259 1259 HOH HOH A . T 9 HOH 360 1260 1260 HOH HOH A . T 9 HOH 361 1261 1261 HOH HOH A . T 9 HOH 362 1262 1262 HOH HOH A . T 9 HOH 363 1263 1263 HOH HOH A . T 9 HOH 364 1264 1264 HOH HOH A . T 9 HOH 365 1265 1265 HOH HOH A . T 9 HOH 366 1266 1266 HOH HOH A . T 9 HOH 367 1267 1267 HOH HOH A . T 9 HOH 368 1268 1268 HOH HOH A . T 9 HOH 369 1269 1269 HOH HOH A . T 9 HOH 370 1270 1270 HOH HOH A . T 9 HOH 371 1271 1271 HOH HOH A . T 9 HOH 372 1272 1272 HOH HOH A . T 9 HOH 373 1273 1273 HOH HOH A . T 9 HOH 374 1274 1274 HOH HOH A . T 9 HOH 375 1275 1275 HOH HOH A . T 9 HOH 376 1276 1276 HOH HOH A . T 9 HOH 377 1277 1277 HOH HOH A . T 9 HOH 378 1278 1278 HOH HOH A . T 9 HOH 379 1279 1279 HOH HOH A . T 9 HOH 380 1280 1280 HOH HOH A . T 9 HOH 381 1281 1281 HOH HOH A . T 9 HOH 382 1282 1282 HOH HOH A . T 9 HOH 383 1283 1283 HOH HOH A . T 9 HOH 384 1284 1284 HOH HOH A . T 9 HOH 385 1285 1285 HOH HOH A . T 9 HOH 386 1286 1286 HOH HOH A . T 9 HOH 387 1287 1287 HOH HOH A . T 9 HOH 388 1288 1288 HOH HOH A . T 9 HOH 389 1289 1289 HOH HOH A . T 9 HOH 390 1290 1290 HOH HOH A . T 9 HOH 391 1291 1291 HOH HOH A . T 9 HOH 392 1292 1292 HOH HOH A . T 9 HOH 393 1293 1293 HOH HOH A . T 9 HOH 394 1294 1294 HOH HOH A . T 9 HOH 395 1295 1295 HOH HOH A . T 9 HOH 396 1296 1296 HOH HOH A . T 9 HOH 397 1297 1297 HOH HOH A . T 9 HOH 398 1298 1298 HOH HOH A . T 9 HOH 399 1299 1299 HOH HOH A . T 9 HOH 400 1300 1300 HOH HOH A . T 9 HOH 401 1301 1301 HOH HOH A . T 9 HOH 402 1302 1302 HOH HOH A . T 9 HOH 403 1303 1303 HOH HOH A . T 9 HOH 404 1304 1304 HOH HOH A . T 9 HOH 405 1305 1305 HOH HOH A . T 9 HOH 406 1306 1306 HOH HOH A . T 9 HOH 407 1307 1307 HOH HOH A . T 9 HOH 408 1308 1308 HOH HOH A . T 9 HOH 409 1309 1309 HOH HOH A . T 9 HOH 410 1310 1310 HOH HOH A . T 9 HOH 411 1311 1311 HOH HOH A . T 9 HOH 412 1312 1312 HOH HOH A . T 9 HOH 413 1313 1313 HOH HOH A . T 9 HOH 414 1314 1314 HOH HOH A . T 9 HOH 415 1315 1315 HOH HOH A . T 9 HOH 416 1316 1316 HOH HOH A . T 9 HOH 417 1317 1317 HOH HOH A . T 9 HOH 418 1318 1318 HOH HOH A . T 9 HOH 419 1319 1319 HOH HOH A . T 9 HOH 420 1320 1320 HOH HOH A . T 9 HOH 421 1321 1321 HOH HOH A . T 9 HOH 422 1322 1322 HOH HOH A . T 9 HOH 423 1323 1323 HOH HOH A . T 9 HOH 424 1324 1324 HOH HOH A . T 9 HOH 425 1325 1325 HOH HOH A . T 9 HOH 426 1326 1326 HOH HOH A . T 9 HOH 427 1327 1327 HOH HOH A . T 9 HOH 428 1328 1328 HOH HOH A . T 9 HOH 429 1329 1329 HOH HOH A . T 9 HOH 430 1330 1330 HOH HOH A . T 9 HOH 431 1331 1331 HOH HOH A . T 9 HOH 432 1332 1332 HOH HOH A . T 9 HOH 433 1333 1333 HOH HOH A . T 9 HOH 434 1334 1334 HOH HOH A . T 9 HOH 435 1335 1335 HOH HOH A . T 9 HOH 436 1336 1336 HOH HOH A . T 9 HOH 437 1337 1337 HOH HOH A . T 9 HOH 438 1338 1338 HOH HOH A . T 9 HOH 439 1339 1339 HOH HOH A . T 9 HOH 440 1340 1340 HOH HOH A . T 9 HOH 441 1341 1341 HOH HOH A . T 9 HOH 442 1342 1342 HOH HOH A . T 9 HOH 443 1343 1343 HOH HOH A . T 9 HOH 444 1344 1344 HOH HOH A . T 9 HOH 445 1345 1345 HOH HOH A . T 9 HOH 446 1346 1346 HOH HOH A . T 9 HOH 447 1347 1347 HOH HOH A . T 9 HOH 448 1348 1348 HOH HOH A . T 9 HOH 449 1349 1349 HOH HOH A . T 9 HOH 450 1350 1350 HOH HOH A . T 9 HOH 451 1351 1351 HOH HOH A . T 9 HOH 452 1352 1352 HOH HOH A . T 9 HOH 453 1353 1353 HOH HOH A . T 9 HOH 454 1354 1354 HOH HOH A . T 9 HOH 455 1355 1355 HOH HOH A . T 9 HOH 456 1356 1356 HOH HOH A . T 9 HOH 457 1357 1357 HOH HOH A . T 9 HOH 458 1358 1358 HOH HOH A . T 9 HOH 459 1359 1359 HOH HOH A . T 9 HOH 460 1360 1360 HOH HOH A . T 9 HOH 461 1361 1361 HOH HOH A . T 9 HOH 462 1362 1362 HOH HOH A . T 9 HOH 463 1363 1363 HOH HOH A . T 9 HOH 464 1364 1364 HOH HOH A . T 9 HOH 465 1365 1365 HOH HOH A . T 9 HOH 466 1366 1366 HOH HOH A . T 9 HOH 467 1367 1367 HOH HOH A . T 9 HOH 468 1368 1368 HOH HOH A . T 9 HOH 469 1369 1369 HOH HOH A . T 9 HOH 470 1370 1370 HOH HOH A . T 9 HOH 471 1371 1371 HOH HOH A . T 9 HOH 472 1372 1372 HOH HOH A . T 9 HOH 473 1373 1373 HOH HOH A . T 9 HOH 474 1374 1374 HOH HOH A . T 9 HOH 475 1375 1375 HOH HOH A . T 9 HOH 476 1376 1376 HOH HOH A . T 9 HOH 477 1377 1377 HOH HOH A . T 9 HOH 478 1378 1378 HOH HOH A . T 9 HOH 479 1379 1379 HOH HOH A . T 9 HOH 480 1380 1380 HOH HOH A . T 9 HOH 481 1381 1381 HOH HOH A . T 9 HOH 482 1382 1382 HOH HOH A . T 9 HOH 483 1383 1383 HOH HOH A . T 9 HOH 484 1384 1384 HOH HOH A . T 9 HOH 485 1385 1385 HOH HOH A . T 9 HOH 486 1386 1386 HOH HOH A . T 9 HOH 487 1387 1387 HOH HOH A . T 9 HOH 488 1388 1388 HOH HOH A . T 9 HOH 489 1389 1389 HOH HOH A . T 9 HOH 490 1390 1390 HOH HOH A . T 9 HOH 491 1391 1391 HOH HOH A . T 9 HOH 492 1392 1392 HOH HOH A . T 9 HOH 493 1393 1393 HOH HOH A . T 9 HOH 494 1394 1394 HOH HOH A . T 9 HOH 495 1395 1395 HOH HOH A . T 9 HOH 496 1396 1396 HOH HOH A . T 9 HOH 497 1397 1397 HOH HOH A . T 9 HOH 498 1398 1398 HOH HOH A . T 9 HOH 499 1399 1399 HOH HOH A . T 9 HOH 500 1400 1400 HOH HOH A . T 9 HOH 501 1401 1401 HOH HOH A . T 9 HOH 502 1402 1402 HOH HOH A . T 9 HOH 503 1403 1403 HOH HOH A . T 9 HOH 504 1404 1404 HOH HOH A . T 9 HOH 505 1405 1405 HOH HOH A . T 9 HOH 506 1406 1406 HOH HOH A . T 9 HOH 507 1407 1407 HOH HOH A . T 9 HOH 508 1408 1408 HOH HOH A . T 9 HOH 509 1409 1409 HOH HOH A . T 9 HOH 510 1410 1410 HOH HOH A . T 9 HOH 511 1411 1411 HOH HOH A . T 9 HOH 512 1412 1412 HOH HOH A . T 9 HOH 513 1413 1413 HOH HOH A . T 9 HOH 514 1414 1414 HOH HOH A . T 9 HOH 515 1415 1415 HOH HOH A . T 9 HOH 516 1416 1416 HOH HOH A . T 9 HOH 517 1417 1417 HOH HOH A . T 9 HOH 518 1418 1418 HOH HOH A . T 9 HOH 519 1419 1419 HOH HOH A . T 9 HOH 520 1420 1420 HOH HOH A . T 9 HOH 521 1421 1421 HOH HOH A . T 9 HOH 522 1422 1422 HOH HOH A . T 9 HOH 523 1423 1423 HOH HOH A . T 9 HOH 524 1424 1424 HOH HOH A . T 9 HOH 525 1425 1425 HOH HOH A . T 9 HOH 526 1426 1426 HOH HOH A . T 9 HOH 527 1427 1427 HOH HOH A . T 9 HOH 528 1428 1428 HOH HOH A . T 9 HOH 529 1429 1429 HOH HOH A . T 9 HOH 530 1430 1430 HOH HOH A . T 9 HOH 531 1431 1431 HOH HOH A . T 9 HOH 532 1432 1432 HOH HOH A . T 9 HOH 533 1433 1433 HOH HOH A . T 9 HOH 534 1434 1434 HOH HOH A . T 9 HOH 535 1435 1435 HOH HOH A . T 9 HOH 536 1436 1436 HOH HOH A . T 9 HOH 537 1437 1437 HOH HOH A . T 9 HOH 538 1438 1438 HOH HOH A . T 9 HOH 539 1439 1439 HOH HOH A . T 9 HOH 540 1440 1440 HOH HOH A . T 9 HOH 541 1441 1441 HOH HOH A . T 9 HOH 542 1442 1442 HOH HOH A . T 9 HOH 543 1443 1443 HOH HOH A . T 9 HOH 544 1444 1444 HOH HOH A . T 9 HOH 545 1445 1445 HOH HOH A . T 9 HOH 546 1446 1446 HOH HOH A . T 9 HOH 547 1447 1447 HOH HOH A . T 9 HOH 548 1448 1448 HOH HOH A . T 9 HOH 549 1449 1449 HOH HOH A . T 9 HOH 550 1450 1450 HOH HOH A . T 9 HOH 551 1451 1451 HOH HOH A . T 9 HOH 552 1452 1452 HOH HOH A . T 9 HOH 553 1453 1453 HOH HOH A . T 9 HOH 554 1454 1454 HOH HOH A . T 9 HOH 555 1455 1455 HOH HOH A . T 9 HOH 556 1456 1456 HOH HOH A . T 9 HOH 557 1457 1457 HOH HOH A . T 9 HOH 558 1458 1458 HOH HOH A . T 9 HOH 559 1459 1459 HOH HOH A . T 9 HOH 560 1460 1460 HOH HOH A . T 9 HOH 561 1461 1461 HOH HOH A . T 9 HOH 562 1462 1462 HOH HOH A . T 9 HOH 563 1463 1463 HOH HOH A . T 9 HOH 564 1464 1464 HOH HOH A . T 9 HOH 565 1465 1465 HOH HOH A . T 9 HOH 566 1466 1466 HOH HOH A . T 9 HOH 567 1467 1467 HOH HOH A . T 9 HOH 568 1468 1468 HOH HOH A . T 9 HOH 569 1469 1469 HOH HOH A . T 9 HOH 570 1470 1470 HOH HOH A . T 9 HOH 571 1471 1471 HOH HOH A . T 9 HOH 572 1472 1472 HOH HOH A . T 9 HOH 573 1473 1473 HOH HOH A . T 9 HOH 574 1474 1474 HOH HOH A . T 9 HOH 575 1475 1475 HOH HOH A . T 9 HOH 576 1476 1476 HOH HOH A . T 9 HOH 577 1477 1477 HOH HOH A . T 9 HOH 578 1478 1478 HOH HOH A . T 9 HOH 579 1479 1479 HOH HOH A . T 9 HOH 580 1480 1480 HOH HOH A . T 9 HOH 581 1481 1481 HOH HOH A . T 9 HOH 582 1482 1482 HOH HOH A . T 9 HOH 583 1483 1483 HOH HOH A . T 9 HOH 584 1484 1484 HOH HOH A . T 9 HOH 585 1485 1485 HOH HOH A . T 9 HOH 586 1486 1486 HOH HOH A . T 9 HOH 587 1487 1487 HOH HOH A . T 9 HOH 588 1488 1488 HOH HOH A . T 9 HOH 589 1489 1489 HOH HOH A . T 9 HOH 590 1490 1490 HOH HOH A . T 9 HOH 591 1491 1491 HOH HOH A . T 9 HOH 592 1492 1492 HOH HOH A . T 9 HOH 593 1493 1493 HOH HOH A . T 9 HOH 594 1494 1494 HOH HOH A . T 9 HOH 595 1495 1495 HOH HOH A . T 9 HOH 596 1496 1496 HOH HOH A . T 9 HOH 597 1497 1497 HOH HOH A . T 9 HOH 598 1498 1498 HOH HOH A . T 9 HOH 599 1499 1499 HOH HOH A . T 9 HOH 600 1500 1500 HOH HOH A . T 9 HOH 601 1501 1501 HOH HOH A . T 9 HOH 602 1502 1502 HOH HOH A . T 9 HOH 603 1503 1503 HOH HOH A . T 9 HOH 604 1504 1504 HOH HOH A . T 9 HOH 605 1505 1505 HOH HOH A . T 9 HOH 606 1506 1506 HOH HOH A . T 9 HOH 607 1507 1507 HOH HOH A . T 9 HOH 608 1508 1508 HOH HOH A . T 9 HOH 609 1509 1511 HOH HOH A . T 9 HOH 610 1510 1512 HOH HOH A . #