data_5ELY # _entry.id 5ELY # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 5ELY WWPDB D_1000211143 # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 5ELY _pdbx_database_status.recvd_initial_deposition_date 2015-11-05 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBE _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 'Barinka, C.' 1 'Novakova, Z.' 2 'Pavlicek, J.' 3 # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country US _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev J.Med.Chem. _citation.journal_id_ASTM JMCMAR _citation.journal_id_CSD 0151 _citation.journal_id_ISSN 0022-2623 _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 59 _citation.language ? _citation.page_first 4539 _citation.page_last 4550 _citation.title ;Unprecedented Binding Mode of Hydroxamate-Based Inhibitors of Glutamate Carboxypeptidase II: Structural Characterization and Biological Activity. ; _citation.year 2016 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1021/acs.jmedchem.5b01806 _citation.pdbx_database_id_PubMed 27074627 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Novakova, Z.' 1 primary 'Wozniak, K.' 2 primary 'Jancarik, A.' 3 primary 'Rais, R.' 4 primary 'Wu, Y.' 5 primary 'Pavlicek, J.' 6 primary 'Ferraris, D.' 7 primary 'Havlinova, B.' 8 primary 'Ptacek, J.' 9 primary 'Vavra, J.' 10 primary 'Hin, N.' 11 primary 'Rojas, C.' 12 primary 'Majer, P.' 13 primary 'Slusher, B.S.' 14 primary 'Tsukamoto, T.' 15 primary 'Barinka, C.' 16 # _cell.angle_alpha 90.000 _cell.angle_alpha_esd ? _cell.angle_beta 90.000 _cell.angle_beta_esd ? _cell.angle_gamma 90.000 _cell.angle_gamma_esd ? _cell.entry_id 5ELY _cell.details ? _cell.formula_units_Z ? _cell.length_a 101.060 _cell.length_a_esd ? _cell.length_b 130.827 _cell.length_b_esd ? _cell.length_c 158.386 _cell.length_c_esd ? _cell.volume ? _cell.volume_esd ? _cell.Z_PDB 8 _cell.reciprocal_angle_alpha ? _cell.reciprocal_angle_beta ? _cell.reciprocal_angle_gamma ? _cell.reciprocal_angle_alpha_esd ? _cell.reciprocal_angle_beta_esd ? _cell.reciprocal_angle_gamma_esd ? _cell.reciprocal_length_a ? _cell.reciprocal_length_b ? _cell.reciprocal_length_c ? _cell.reciprocal_length_a_esd ? _cell.reciprocal_length_b_esd ? _cell.reciprocal_length_c_esd ? _cell.pdbx_unique_axis ? # _symmetry.entry_id 5ELY _symmetry.cell_setting ? _symmetry.Int_Tables_number 23 _symmetry.space_group_name_Hall ? _symmetry.space_group_name_H-M 'I 2 2 2' _symmetry.pdbx_full_space_group_name_H-M ? # 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' 78470.539 1 3.4.17.21 ? 'UNP residues 55-750' ? 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 10 ? ? ? ? 6 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 7 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 8 non-polymer syn '4-[(2~{R})-2-carboxy-5-(oxidanylamino)-5-oxidanylidene-pentyl]benzoic acid' 281.261 1 ? ? ? ? 9 non-polymer nat 'ACETATE ION' 59.044 1 ? ? ? ? 10 water nat water 18.015 466 ? ? ? ? # _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,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 ;KHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINED GNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKV KNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPV HPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVIL GGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADS SIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGR ARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSI SMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAP SSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_seq_one_letter_code_can ;KHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINED GNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKV KNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPV HPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVIL GGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADS SIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGR ARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSI SMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAP SSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _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 LYS n 1 2 HIS n 1 3 ASN n 1 4 MET n 1 5 LYS n 1 6 ALA n 1 7 PHE n 1 8 LEU n 1 9 ASP n 1 10 GLU n 1 11 LEU n 1 12 LYS n 1 13 ALA n 1 14 GLU n 1 15 ASN n 1 16 ILE n 1 17 LYS n 1 18 LYS n 1 19 PHE n 1 20 LEU n 1 21 TYR n 1 22 ASN n 1 23 PHE n 1 24 THR n 1 25 GLN n 1 26 ILE n 1 27 PRO n 1 28 HIS n 1 29 LEU n 1 30 ALA n 1 31 GLY n 1 32 THR n 1 33 GLU n 1 34 GLN n 1 35 ASN n 1 36 PHE n 1 37 GLN n 1 38 LEU n 1 39 ALA n 1 40 LYS n 1 41 GLN n 1 42 ILE n 1 43 GLN n 1 44 SER n 1 45 GLN n 1 46 TRP n 1 47 LYS n 1 48 GLU n 1 49 PHE n 1 50 GLY n 1 51 LEU n 1 52 ASP n 1 53 SER n 1 54 VAL n 1 55 GLU n 1 56 LEU n 1 57 ALA n 1 58 HIS n 1 59 TYR n 1 60 ASP n 1 61 VAL n 1 62 LEU n 1 63 LEU n 1 64 SER n 1 65 TYR n 1 66 PRO n 1 67 ASN n 1 68 LYS n 1 69 THR n 1 70 HIS n 1 71 PRO n 1 72 ASN n 1 73 TYR n 1 74 ILE n 1 75 SER n 1 76 ILE n 1 77 ILE n 1 78 ASN n 1 79 GLU n 1 80 ASP n 1 81 GLY n 1 82 ASN n 1 83 GLU n 1 84 ILE n 1 85 PHE n 1 86 ASN n 1 87 THR n 1 88 SER n 1 89 LEU n 1 90 PHE n 1 91 GLU n 1 92 PRO n 1 93 PRO n 1 94 PRO n 1 95 PRO n 1 96 GLY n 1 97 TYR n 1 98 GLU n 1 99 ASN n 1 100 VAL n 1 101 SER n 1 102 ASP n 1 103 ILE n 1 104 VAL n 1 105 PRO n 1 106 PRO n 1 107 PHE n 1 108 SER n 1 109 ALA n 1 110 PHE n 1 111 SER n 1 112 PRO n 1 113 GLN n 1 114 GLY n 1 115 MET n 1 116 PRO n 1 117 GLU n 1 118 GLY n 1 119 ASP n 1 120 LEU n 1 121 VAL n 1 122 TYR n 1 123 VAL n 1 124 ASN n 1 125 TYR n 1 126 ALA n 1 127 ARG n 1 128 THR n 1 129 GLU n 1 130 ASP n 1 131 PHE n 1 132 PHE n 1 133 LYS n 1 134 LEU n 1 135 GLU n 1 136 ARG n 1 137 ASP n 1 138 MET n 1 139 LYS n 1 140 ILE n 1 141 ASN n 1 142 CYS n 1 143 SER n 1 144 GLY n 1 145 LYS n 1 146 ILE n 1 147 VAL n 1 148 ILE n 1 149 ALA n 1 150 ARG n 1 151 TYR n 1 152 GLY n 1 153 LYS n 1 154 VAL n 1 155 PHE n 1 156 ARG n 1 157 GLY n 1 158 ASN n 1 159 LYS n 1 160 VAL n 1 161 LYS n 1 162 ASN n 1 163 ALA n 1 164 GLN n 1 165 LEU n 1 166 ALA n 1 167 GLY n 1 168 ALA n 1 169 LYS n 1 170 GLY n 1 171 VAL n 1 172 ILE n 1 173 LEU n 1 174 TYR n 1 175 SER n 1 176 ASP n 1 177 PRO n 1 178 ALA n 1 179 ASP n 1 180 TYR n 1 181 PHE n 1 182 ALA n 1 183 PRO n 1 184 GLY n 1 185 VAL n 1 186 LYS n 1 187 SER n 1 188 TYR n 1 189 PRO n 1 190 ASP n 1 191 GLY n 1 192 TRP n 1 193 ASN n 1 194 LEU n 1 195 PRO n 1 196 GLY n 1 197 GLY n 1 198 GLY n 1 199 VAL n 1 200 GLN n 1 201 ARG n 1 202 GLY n 1 203 ASN n 1 204 ILE n 1 205 LEU n 1 206 ASN n 1 207 LEU n 1 208 ASN n 1 209 GLY n 1 210 ALA n 1 211 GLY n 1 212 ASP n 1 213 PRO n 1 214 LEU n 1 215 THR n 1 216 PRO n 1 217 GLY n 1 218 TYR n 1 219 PRO n 1 220 ALA n 1 221 ASN n 1 222 GLU n 1 223 TYR n 1 224 ALA n 1 225 TYR n 1 226 ARG n 1 227 ARG n 1 228 GLY n 1 229 ILE n 1 230 ALA n 1 231 GLU n 1 232 ALA n 1 233 VAL n 1 234 GLY n 1 235 LEU n 1 236 PRO n 1 237 SER n 1 238 ILE n 1 239 PRO n 1 240 VAL n 1 241 HIS n 1 242 PRO n 1 243 ILE n 1 244 GLY n 1 245 TYR n 1 246 TYR n 1 247 ASP n 1 248 ALA n 1 249 GLN n 1 250 LYS n 1 251 LEU n 1 252 LEU n 1 253 GLU n 1 254 LYS n 1 255 MET n 1 256 GLY n 1 257 GLY n 1 258 SER n 1 259 ALA n 1 260 PRO n 1 261 PRO n 1 262 ASP n 1 263 SER n 1 264 SER n 1 265 TRP n 1 266 ARG n 1 267 GLY n 1 268 SER n 1 269 LEU n 1 270 LYS n 1 271 VAL n 1 272 PRO n 1 273 TYR n 1 274 ASN n 1 275 VAL n 1 276 GLY n 1 277 PRO n 1 278 GLY n 1 279 PHE n 1 280 THR n 1 281 GLY n 1 282 ASN n 1 283 PHE n 1 284 SER n 1 285 THR n 1 286 GLN n 1 287 LYS n 1 288 VAL n 1 289 LYS n 1 290 MET n 1 291 HIS n 1 292 ILE n 1 293 HIS n 1 294 SER n 1 295 THR n 1 296 ASN n 1 297 GLU n 1 298 VAL n 1 299 THR n 1 300 ARG n 1 301 ILE n 1 302 TYR n 1 303 ASN n 1 304 VAL n 1 305 ILE n 1 306 GLY n 1 307 THR n 1 308 LEU n 1 309 ARG n 1 310 GLY n 1 311 ALA n 1 312 VAL n 1 313 GLU n 1 314 PRO n 1 315 ASP n 1 316 ARG n 1 317 TYR n 1 318 VAL n 1 319 ILE n 1 320 LEU n 1 321 GLY n 1 322 GLY n 1 323 HIS n 1 324 ARG n 1 325 ASP n 1 326 SER n 1 327 TRP n 1 328 VAL n 1 329 PHE n 1 330 GLY n 1 331 GLY n 1 332 ILE n 1 333 ASP n 1 334 PRO n 1 335 GLN n 1 336 SER n 1 337 GLY n 1 338 ALA n 1 339 ALA n 1 340 VAL n 1 341 VAL n 1 342 HIS n 1 343 GLU n 1 344 ILE n 1 345 VAL n 1 346 ARG n 1 347 SER n 1 348 PHE n 1 349 GLY n 1 350 THR n 1 351 LEU n 1 352 LYS n 1 353 LYS n 1 354 GLU n 1 355 GLY n 1 356 TRP n 1 357 ARG n 1 358 PRO n 1 359 ARG n 1 360 ARG n 1 361 THR n 1 362 ILE n 1 363 LEU n 1 364 PHE n 1 365 ALA n 1 366 SER n 1 367 TRP n 1 368 ASP n 1 369 ALA n 1 370 GLU n 1 371 GLU n 1 372 PHE n 1 373 GLY n 1 374 LEU n 1 375 LEU n 1 376 GLY n 1 377 SER n 1 378 THR n 1 379 GLU n 1 380 TRP n 1 381 ALA n 1 382 GLU n 1 383 GLU n 1 384 ASN n 1 385 SER n 1 386 ARG n 1 387 LEU n 1 388 LEU n 1 389 GLN n 1 390 GLU n 1 391 ARG n 1 392 GLY n 1 393 VAL n 1 394 ALA n 1 395 TYR n 1 396 ILE n 1 397 ASN n 1 398 ALA n 1 399 ASP n 1 400 SER n 1 401 SER n 1 402 ILE n 1 403 GLU n 1 404 GLY n 1 405 ASN n 1 406 TYR n 1 407 THR n 1 408 LEU n 1 409 ARG n 1 410 VAL n 1 411 ASP n 1 412 CYS n 1 413 THR n 1 414 PRO n 1 415 LEU n 1 416 MET n 1 417 TYR n 1 418 SER n 1 419 LEU n 1 420 VAL n 1 421 HIS n 1 422 ASN n 1 423 LEU n 1 424 THR n 1 425 LYS n 1 426 GLU n 1 427 LEU n 1 428 LYS n 1 429 SER n 1 430 PRO n 1 431 ASP n 1 432 GLU n 1 433 GLY n 1 434 PHE n 1 435 GLU n 1 436 GLY n 1 437 LYS n 1 438 SER n 1 439 LEU n 1 440 TYR n 1 441 GLU n 1 442 SER n 1 443 TRP n 1 444 THR n 1 445 LYS n 1 446 LYS n 1 447 SER n 1 448 PRO n 1 449 SER n 1 450 PRO n 1 451 GLU n 1 452 PHE n 1 453 SER n 1 454 GLY n 1 455 MET n 1 456 PRO n 1 457 ARG n 1 458 ILE n 1 459 SER n 1 460 LYS n 1 461 LEU n 1 462 GLY n 1 463 SER n 1 464 GLY n 1 465 ASN n 1 466 ASP n 1 467 PHE n 1 468 GLU n 1 469 VAL n 1 470 PHE n 1 471 PHE n 1 472 GLN n 1 473 ARG n 1 474 LEU n 1 475 GLY n 1 476 ILE n 1 477 ALA n 1 478 SER n 1 479 GLY n 1 480 ARG n 1 481 ALA n 1 482 ARG n 1 483 TYR n 1 484 THR n 1 485 LYS n 1 486 ASN n 1 487 TRP n 1 488 GLU n 1 489 THR n 1 490 ASN n 1 491 LYS n 1 492 PHE n 1 493 SER n 1 494 GLY n 1 495 TYR n 1 496 PRO n 1 497 LEU n 1 498 TYR n 1 499 HIS n 1 500 SER n 1 501 VAL n 1 502 TYR n 1 503 GLU n 1 504 THR n 1 505 TYR n 1 506 GLU n 1 507 LEU n 1 508 VAL n 1 509 GLU n 1 510 LYS n 1 511 PHE n 1 512 TYR n 1 513 ASP n 1 514 PRO n 1 515 MET n 1 516 PHE n 1 517 LYS n 1 518 TYR n 1 519 HIS n 1 520 LEU n 1 521 THR n 1 522 VAL n 1 523 ALA n 1 524 GLN n 1 525 VAL n 1 526 ARG n 1 527 GLY n 1 528 GLY n 1 529 MET n 1 530 VAL n 1 531 PHE n 1 532 GLU n 1 533 LEU n 1 534 ALA n 1 535 ASN n 1 536 SER n 1 537 ILE n 1 538 VAL n 1 539 LEU n 1 540 PRO n 1 541 PHE n 1 542 ASP n 1 543 CYS n 1 544 ARG n 1 545 ASP n 1 546 TYR n 1 547 ALA n 1 548 VAL n 1 549 VAL n 1 550 LEU n 1 551 ARG n 1 552 LYS n 1 553 TYR n 1 554 ALA n 1 555 ASP n 1 556 LYS n 1 557 ILE n 1 558 TYR n 1 559 SER n 1 560 ILE n 1 561 SER n 1 562 MET n 1 563 LYS n 1 564 HIS n 1 565 PRO n 1 566 GLN n 1 567 GLU n 1 568 MET n 1 569 LYS n 1 570 THR n 1 571 TYR n 1 572 SER n 1 573 VAL n 1 574 SER n 1 575 PHE n 1 576 ASP n 1 577 SER n 1 578 LEU n 1 579 PHE n 1 580 SER n 1 581 ALA n 1 582 VAL n 1 583 LYS n 1 584 ASN n 1 585 PHE n 1 586 THR n 1 587 GLU n 1 588 ILE n 1 589 ALA n 1 590 SER n 1 591 LYS n 1 592 PHE n 1 593 SER n 1 594 GLU n 1 595 ARG n 1 596 LEU n 1 597 GLN n 1 598 ASP n 1 599 PHE n 1 600 ASP n 1 601 LYS n 1 602 SER n 1 603 ASN n 1 604 PRO n 1 605 ILE n 1 606 VAL n 1 607 LEU n 1 608 ARG n 1 609 MET n 1 610 MET n 1 611 ASN n 1 612 ASP n 1 613 GLN n 1 614 LEU n 1 615 MET n 1 616 PHE n 1 617 LEU n 1 618 GLU n 1 619 ARG n 1 620 ALA n 1 621 PHE n 1 622 ILE n 1 623 ASP n 1 624 PRO n 1 625 LEU n 1 626 GLY n 1 627 LEU n 1 628 PRO n 1 629 ASP n 1 630 ARG n 1 631 PRO n 1 632 PHE n 1 633 TYR n 1 634 ARG n 1 635 HIS n 1 636 VAL n 1 637 ILE n 1 638 TYR n 1 639 ALA n 1 640 PRO n 1 641 SER n 1 642 SER n 1 643 HIS n 1 644 ASN n 1 645 LYS n 1 646 TYR n 1 647 ALA n 1 648 GLY n 1 649 GLU n 1 650 SER n 1 651 PHE n 1 652 PRO n 1 653 GLY n 1 654 ILE n 1 655 TYR n 1 656 ASP n 1 657 ALA n 1 658 LEU n 1 659 PHE n 1 660 ASP n 1 661 ILE n 1 662 GLU n 1 663 SER n 1 664 LYS n 1 665 VAL n 1 666 ASP n 1 667 PRO n 1 668 SER n 1 669 LYS n 1 670 ALA n 1 671 TRP n 1 672 GLY n 1 673 GLU n 1 674 VAL n 1 675 LYS n 1 676 ARG n 1 677 GLN n 1 678 ILE n 1 679 TYR n 1 680 VAL n 1 681 ALA n 1 682 ALA n 1 683 PHE n 1 684 THR n 1 685 VAL n 1 686 GLN n 1 687 ALA n 1 688 ALA n 1 689 ALA n 1 690 GLU n 1 691 THR n 1 692 LEU n 1 693 SER n 1 694 GLU n 1 695 VAL n 1 696 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 'Biological sequence' _entity_src_gen.pdbx_beg_seq_num 1 _entity_src_gen.pdbx_end_seq_num 696 _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 'Fruit fly' _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.pdbx_db_isoform ? _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;KHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINED GNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKV KNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPV HPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVIL GGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADS SIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGR ARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSI SMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAP SSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _struct_ref.pdbx_align_begin 55 # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 5ELY _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 696 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q04609 _struct_ref_seq.db_align_beg 55 _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 55 _struct_ref_seq.pdbx_auth_seq_align_end 750 # 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 5PU non-polymer . '4-[(2~{R})-2-carboxy-5-(oxidanylamino)-5-oxidanylidene-pentyl]benzoic acid' JHU242 'C13 H15 N O6' 281.261 ACT non-polymer . 'ACETATE ION' ? 'C2 H3 O2 -1' 59.044 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.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 5ELY _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 3.29 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 62.59 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH 8 _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 288 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '33% (v/v) pentaerythritol propoxylate PO/OH 5/4, 2 % (w/v) PEG 3350, and 100 mM Tris-HCl, pH 8.0' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector CCD _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'RAYONIX MX-225' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2011-03-12 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator 'Sagitally bended Si111 double crystal monochromator' _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.91841 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source SYNCHROTRON _diffrn_source.target ? _diffrn_source.type 'BESSY BEAMLINE 14.2' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 0.91841 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline 14.2 _diffrn_source.pdbx_synchrotron_site BESSY # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 5ELY _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 1.81 _reflns.d_resolution_low 100.87 _reflns.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.number_all ? _reflns.number_obs 95135 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 99.48 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 6.0 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 25.42 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half ? _reflns.pdbx_R_split ? # _reflns_shell.d_res_high 1.810 _reflns_shell.d_res_low 1.87 _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_possible ? _reflns_shell.number_unique_all ? _reflns_shell.number_unique_obs ? _reflns_shell.percent_possible_all ? _reflns_shell.percent_possible_obs ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_gt ? _reflns_shell.meanI_over_uI_all ? _reflns_shell.meanI_over_uI_gt ? _reflns_shell.number_measured_gt ? _reflns_shell.number_unique_gt ? _reflns_shell.percent_possible_gt ? _reflns_shell.Rmerge_F_gt ? _reflns_shell.Rmerge_I_gt ? _reflns_shell.pdbx_redundancy ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_netI_over_sigmaI_all ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_CC_half ? _reflns_shell.pdbx_R_split ? # _refine.aniso_B[1][1] 1.1800 _refine.aniso_B[1][2] 0.0000 _refine.aniso_B[1][3] 0.0000 _refine.aniso_B[2][2] -2.0200 _refine.aniso_B[2][3] 0.0000 _refine.aniso_B[3][3] 0.8400 _refine.B_iso_max 76.940 _refine.B_iso_mean 32.8900 _refine.B_iso_min 11.760 _refine.correlation_coeff_Fo_to_Fc 0.9630 _refine.correlation_coeff_Fo_to_Fc_free 0.9540 _refine.details 'U VALUES : WITH TLS ADDED' _refine.diff_density_max ? _refine.diff_density_max_esd ? _refine.diff_density_min ? _refine.diff_density_min_esd ? _refine.diff_density_rms ? _refine.diff_density_rms_esd ? _refine.entry_id 5ELY _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_abs_structure_details ? _refine.ls_abs_structure_Flack ? _refine.ls_abs_structure_Flack_esd ? _refine.ls_abs_structure_Rogers ? _refine.ls_abs_structure_Rogers_esd ? _refine.ls_d_res_high 1.8100 _refine.ls_d_res_low 40.0000 _refine.ls_extinction_coef ? _refine.ls_extinction_coef_esd ? _refine.ls_extinction_expression ? _refine.ls_extinction_method ? _refine.ls_goodness_of_fit_all ? _refine.ls_goodness_of_fit_all_esd ? _refine.ls_goodness_of_fit_obs ? _refine.ls_goodness_of_fit_obs_esd ? _refine.ls_hydrogen_treatment ? _refine.ls_matrix_type ? _refine.ls_number_constraints ? _refine.ls_number_parameters ? _refine.ls_number_reflns_all ? _refine.ls_number_reflns_obs 94013 _refine.ls_number_reflns_R_free 952 _refine.ls_number_reflns_R_work ? _refine.ls_number_restraints ? _refine.ls_percent_reflns_obs 99.5000 _refine.ls_percent_reflns_R_free 1.0000 _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.1777 _refine.ls_R_factor_R_free 0.1986 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_R_factor_R_work 0.1775 _refine.ls_R_Fsqd_factor_obs ? _refine.ls_R_I_factor_obs ? _refine.ls_redundancy_reflns_all ? _refine.ls_redundancy_reflns_obs ? _refine.ls_restrained_S_all ? _refine.ls_restrained_S_obs ? _refine.ls_shift_over_esd_max ? _refine.ls_shift_over_esd_mean ? _refine.ls_structure_factor_coef ? _refine.ls_weighting_details ? _refine.ls_weighting_scheme ? _refine.ls_wR_factor_all ? _refine.ls_wR_factor_obs ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.occupancy_max ? _refine.occupancy_min ? _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.ls_R_factor_gt ? _refine.ls_goodness_of_fit_gt ? _refine.ls_goodness_of_fit_ref ? _refine.ls_shift_over_su_max ? _refine.ls_shift_over_su_max_lt ? _refine.ls_shift_over_su_mean ? _refine.ls_shift_over_su_mean_lt ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.000 _refine.pdbx_ls_sigma_Fsqd ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.pdbx_method_to_determine_struct 'FOURIER SYNTHESIS' _refine.pdbx_starting_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_overall_ESU_R 0.0990 _refine.pdbx_overall_ESU_R_Free 0.0940 _refine.pdbx_solvent_vdw_probe_radii 1.4000 _refine.pdbx_solvent_ion_probe_radii 0.8000 _refine.pdbx_solvent_shrinkage_radii 0.8000 _refine.pdbx_real_space_R ? _refine.pdbx_density_correlation ? _refine.pdbx_pd_number_of_powder_patterns ? _refine.pdbx_pd_number_of_points ? _refine.pdbx_pd_meas_number_of_points ? _refine.pdbx_pd_proc_ls_prof_R_factor ? _refine.pdbx_pd_proc_ls_prof_wR_factor ? _refine.pdbx_pd_Marquardt_correlation_coeff ? _refine.pdbx_pd_Fsqrd_R_factor ? _refine.pdbx_pd_ls_matrix_band_width ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_diffrn_id 1 _refine.overall_SU_B 4.3500 _refine.overall_SU_ML 0.0650 _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_average_fsc_overall ? _refine.pdbx_average_fsc_work ? _refine.pdbx_average_fsc_free ? # _refine_hist.cycle_id final _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.d_res_high 1.8100 _refine_hist.d_res_low 40.0000 _refine_hist.pdbx_number_atoms_ligand 190 _refine_hist.number_atoms_solvent 466 _refine_hist.number_atoms_total 6092 _refine_hist.pdbx_number_residues_total 682 _refine_hist.pdbx_B_iso_mean_ligand 45.60 _refine_hist.pdbx_B_iso_mean_solvent 38.58 _refine_hist.pdbx_number_atoms_protein 5436 _refine_hist.pdbx_number_atoms_nucleic_acid 0 # loop_ _refine_ls_restr.pdbx_refine_id _refine_ls_restr.criterion _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.number _refine_ls_restr.rejects _refine_ls_restr.type _refine_ls_restr.weight _refine_ls_restr.pdbx_restraint_function 'X-RAY DIFFRACTION' ? 0.019 0.022 6118 ? r_bond_refined_d ? ? 'X-RAY DIFFRACTION' ? 1.658 1.993 8346 ? r_angle_refined_deg ? ? 'X-RAY DIFFRACTION' ? 6.207 5.000 745 ? r_dihedral_angle_1_deg ? ? 'X-RAY DIFFRACTION' ? 36.169 23.871 279 ? r_dihedral_angle_2_deg ? ? 'X-RAY DIFFRACTION' ? 14.650 15.000 1006 ? r_dihedral_angle_3_deg ? ? 'X-RAY DIFFRACTION' ? 15.023 15.000 34 ? r_dihedral_angle_4_deg ? ? 'X-RAY DIFFRACTION' ? 0.130 0.200 900 ? r_chiral_restr ? ? 'X-RAY DIFFRACTION' ? 0.009 0.021 4738 ? r_gen_planes_refined ? ? 'X-RAY DIFFRACTION' ? 1.014 1.500 3585 ? r_mcbond_it ? ? 'X-RAY DIFFRACTION' ? 1.683 2.000 5846 ? r_mcangle_it ? ? 'X-RAY DIFFRACTION' ? 2.577 3.000 2533 ? r_scbond_it ? ? 'X-RAY DIFFRACTION' ? 4.102 4.500 2487 ? r_scangle_it ? ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.d_res_high 1.8100 _refine_ls_shell.d_res_low 1.8570 _refine_ls_shell.number_reflns_all 6704 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.number_reflns_R_free 64 _refine_ls_shell.number_reflns_R_work 6640 _refine_ls_shell.percent_reflns_obs 96.4000 _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.R_factor_obs ? _refine_ls_shell.R_factor_R_free 0.2630 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.R_factor_R_work 0.2910 _refine_ls_shell.redundancy_reflns_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.wR_factor_all ? _refine_ls_shell.wR_factor_obs ? _refine_ls_shell.wR_factor_R_free ? _refine_ls_shell.wR_factor_R_work ? _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.pdbx_phase_error ? _refine_ls_shell.pdbx_fsc_work ? _refine_ls_shell.pdbx_fsc_free ? # _struct.entry_id 5ELY _struct.title 'X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a hydroxamate inhibitor JHU242' _struct.pdbx_descriptor 'Glutamate carboxypeptidase 2 (E.C.3.4.17.21)' _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag ? # _struct_keywords.entry_id 5ELY _struct_keywords.text 'prostate-specific membrane antigen, NAALADase, phosphoramidate, hydrolase' _struct_keywords.pdbx_keywords HYDROLASE # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 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 6 ? Q N N 7 ? R N N 8 ? S N N 9 ? T N N 10 ? # 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 AA1 ASN A 3 ? LEU A 11 ? ASN A 57 LEU A 65 1 ? 9 HELX_P HELX_P2 AA2 LYS A 12 ? PHE A 23 ? LYS A 66 PHE A 77 1 ? 12 HELX_P HELX_P3 AA3 THR A 32 ? GLY A 50 ? THR A 86 GLY A 104 1 ? 19 HELX_P HELX_P4 AA4 ARG A 127 ? ASP A 137 ? ARG A 181 ASP A 191 1 ? 11 HELX_P HELX_P5 AA5 PHE A 155 ? ALA A 166 ? PHE A 209 ALA A 220 1 ? 12 HELX_P HELX_P6 AA6 ASP A 176 ? PHE A 181 ? ASP A 230 PHE A 235 1 ? 6 HELX_P HELX_P7 AA7 GLY A 228 ? ALA A 232 ? GLY A 282 ALA A 286 5 ? 5 HELX_P HELX_P8 AA8 GLY A 244 ? GLU A 253 ? GLY A 298 GLU A 307 1 ? 10 HELX_P HELX_P9 AA9 ASP A 262 ? ARG A 266 ? ASP A 316 ARG A 320 5 ? 5 HELX_P HELX_P10 AB1 THR A 280 ? SER A 284 ? THR A 334 SER A 338 5 ? 5 HELX_P HELX_P11 AB2 PRO A 334 ? GLU A 354 ? PRO A 388 GLU A 408 1 ? 21 HELX_P HELX_P12 AB3 ALA A 369 ? GLY A 373 ? ALA A 423 GLY A 427 5 ? 5 HELX_P HELX_P13 AB4 LEU A 374 ? ASN A 384 ? LEU A 428 ASN A 438 1 ? 11 HELX_P HELX_P14 AB5 ASN A 384 ? ARG A 391 ? ASN A 438 ARG A 445 1 ? 8 HELX_P HELX_P15 AB6 MET A 416 ? GLU A 426 ? MET A 470 GLU A 480 1 ? 11 HELX_P HELX_P16 AB7 SER A 438 ? SER A 447 ? SER A 492 SER A 501 1 ? 10 HELX_P HELX_P17 AB8 PHE A 467 ? ARG A 473 ? PHE A 521 ARG A 527 1 ? 7 HELX_P HELX_P18 AB9 THR A 504 ? TYR A 512 ? THR A 558 TYR A 566 1 ? 9 HELX_P HELX_P19 AC1 PHE A 516 ? SER A 536 ? PHE A 570 SER A 590 1 ? 21 HELX_P HELX_P20 AC2 ASP A 542 ? MET A 562 ? ASP A 596 MET A 616 1 ? 21 HELX_P HELX_P21 AC3 HIS A 564 ? TYR A 571 ? HIS A 618 TYR A 625 1 ? 8 HELX_P HELX_P22 AC4 PHE A 575 ? ASP A 598 ? PHE A 629 ASP A 652 1 ? 24 HELX_P HELX_P23 AC5 ASN A 603 ? PHE A 621 ? ASN A 657 PHE A 675 1 ? 19 HELX_P HELX_P24 AC6 PHE A 651 ? PHE A 659 ? PHE A 705 PHE A 713 1 ? 9 HELX_P HELX_P25 AC7 ASP A 660 ? LYS A 664 ? ASP A 714 LYS A 718 5 ? 5 HELX_P HELX_P26 AC8 ASP A 666 ? THR A 691 ? 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 one ? A ASN 22 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 76 A NAG 805 1_555 ? ? ? ? ? ? ? 1.430 ? covale2 covale one ? A ASN 67 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 121 A NAG 807 1_555 ? ? ? ? ? ? ? 1.439 ? covale3 covale one ? A ASN 86 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 140 A NAG 808 1_555 ? ? ? ? ? ? ? 1.445 ? metalc1 metalc ? ? A THR 215 O ? ? ? 1_555 D CA . CA ? ? A THR 269 A CA 803 1_555 ? ? ? ? ? ? ? 2.402 ? metalc2 metalc ? ? A THR 215 OG1 ? ? ? 1_555 D CA . CA ? ? A THR 269 A CA 803 1_555 ? ? ? ? ? ? ? 2.456 ? metalc3 metalc ? ? A TYR 218 O ? ? ? 1_555 D CA . CA ? ? A TYR 272 A CA 803 1_555 ? ? ? ? ? ? ? 2.347 ? metalc4 metalc ? ? A HIS 323 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 377 A ZN 802 1_555 ? ? ? ? ? ? ? 2.042 ? metalc5 metalc ? ? A ASP 333 OD1 ? ? ? 1_555 C ZN . ZN ? ? A ASP 387 A ZN 802 1_555 ? ? ? ? ? ? ? 2.072 ? metalc6 metalc ? ? A ASP 333 OD2 ? ? ? 1_555 B ZN . ZN ? ? A ASP 387 A ZN 801 1_555 ? ? ? ? ? ? ? 2.008 ? metalc7 metalc ? ? A GLU 371 OE1 ? ? ? 1_555 B ZN . ZN ? ? A GLU 425 A ZN 801 1_555 ? ? ? ? ? ? ? 2.514 ? metalc8 metalc ? ? A GLU 371 OE2 ? ? ? 1_555 B ZN . ZN ? ? A GLU 425 A ZN 801 1_555 ? ? ? ? ? ? ? 1.999 ? metalc9 metalc ? ? A GLU 379 OE1 ? ? ? 1_555 D CA . CA ? ? A GLU 433 A CA 803 1_555 ? ? ? ? ? ? ? 2.399 ? metalc10 metalc ? ? A GLU 379 OE2 ? ? ? 1_555 D CA . CA ? ? A GLU 433 A CA 803 1_555 ? ? ? ? ? ? ? 2.398 ? metalc11 metalc ? ? A GLU 382 OE2 ? ? ? 1_555 D CA . CA ? ? A GLU 436 A CA 803 1_555 ? ? ? ? ? ? ? 2.297 ? metalc12 metalc ? ? A ASP 399 OD1 ? ? ? 1_555 C ZN . ZN ? ? A ASP 453 A ZN 802 1_555 ? ? ? ? ? ? ? 2.508 ? metalc13 metalc ? ? A ASP 399 OD2 ? ? ? 1_555 C ZN . ZN ? ? A ASP 453 A ZN 802 1_555 ? ? ? ? ? ? ? 2.087 ? covale4 covale one ? A ASN 405 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 459 A NAG 810 1_555 ? ? ? ? ? ? ? 1.445 ? covale5 covale one ? A ASN 422 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 476 A NAG 811 1_555 ? ? ? ? ? ? ? 1.431 ? metalc14 metalc ? ? A HIS 499 NE2 ? ? ? 1_555 B ZN . ZN ? ? A HIS 553 A ZN 801 1_555 ? ? ? ? ? ? ? 2.108 ? covale6 covale one ? A ASN 584 ND2 ? ? ? 1_555 N NAG . C1 ? ? A ASN 638 A NAG 813 1_555 ? ? ? ? ? ? ? 1.453 ? metalc15 metalc ? ? B ZN . ZN ? ? ? 1_555 R 5PU . OAD ? ? A ZN 801 A 5PU 817 1_555 ? ? ? ? ? ? ? 2.299 ? metalc16 metalc ? ? B ZN . ZN ? ? ? 1_555 R 5PU . OAC ? ? A ZN 801 A 5PU 817 1_555 ? ? ? ? ? ? ? 2.104 ? metalc17 metalc ? ? C ZN . ZN ? ? ? 1_555 R 5PU . OAD ? ? A ZN 802 A 5PU 817 1_555 ? ? ? ? ? ? ? 1.978 ? metalc18 metalc ? ? C ZN . ZN ? ? ? 1_555 T HOH . O ? ? A ZN 802 A HOH 1126 1_555 ? ? ? ? ? ? ? 2.156 ? metalc19 metalc ? ? D CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 803 A HOH 966 1_555 ? ? ? ? ? ? ? 2.499 ? covale7 covale both ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 805 A NAG 806 1_555 ? ? ? ? ? ? ? 1.444 ? covale8 covale both ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 808 A NAG 809 1_555 ? ? ? ? ? ? ? 1.452 ? covale9 covale both ? L NAG . O4 ? ? ? 1_555 M NAG . C1 ? ? A NAG 811 A NAG 812 1_555 ? ? ? ? ? ? ? 1.438 ? covale10 covale both ? N NAG . O4 ? ? ? 1_555 O NAG . C1 ? ? A NAG 813 A NAG 814 1_555 ? ? ? ? ? ? ? 1.444 ? covale11 covale both ? O NAG . O4 ? ? ? 1_555 P BMA . C1 ? ? A NAG 814 A BMA 815 1_555 ? ? ? ? ? ? ? 1.431 ? covale12 covale one ? P BMA . O3 ? ? ? 1_555 Q MAN . C1 ? ? A BMA 815 A MAN 816 1_555 ? ? ? ? ? ? ? 1.453 ? # 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 188 A . ? TYR 242 A PRO 189 A ? PRO 243 A 1 9.96 2 GLY 276 A . ? GLY 330 A PRO 277 A ? PRO 331 A 1 -1.15 3 ASP 333 A . ? ASP 387 A PRO 334 A ? PRO 388 A 1 2.85 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 7 ? AA2 ? 4 ? AA3 ? 2 ? AA4 ? 4 ? # 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 AA1 1 2 ? anti-parallel AA1 2 3 ? anti-parallel AA1 3 4 ? parallel AA1 4 5 ? parallel AA1 5 6 ? parallel AA1 6 7 ? anti-parallel AA2 1 2 ? anti-parallel AA2 2 3 ? anti-parallel AA2 3 4 ? anti-parallel AA3 1 2 ? parallel AA4 1 2 ? parallel AA4 2 3 ? parallel AA4 3 4 ? 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 AA1 1 SER A 53 ? TYR A 65 ? SER A 107 TYR A 119 AA1 2 THR A 295 ? LEU A 308 ? THR A 349 LEU A 362 AA1 3 ARG A 360 ? TRP A 367 ? ARG A 414 TRP A 421 AA1 4 GLU A 313 ? HIS A 323 ? GLU A 367 HIS A 377 AA1 5 GLY A 392 ? ASN A 397 ? GLY A 446 ASN A 451 AA1 6 ALA A 477 ? THR A 484 ? ALA A 531 THR A 538 AA1 7 THR A 407 ? CYS A 412 ? THR A 461 CYS A 466 AA2 1 PHE A 85 ? ASN A 86 ? PHE A 139 ASN A 140 AA2 2 TYR A 73 ? ILE A 77 ? TYR A 127 ILE A 131 AA2 3 LYS A 287 ? HIS A 291 ? LYS A 341 HIS A 345 AA2 4 GLU A 117 ? GLY A 118 ? GLU A 171 GLY A 172 AA3 1 SER A 108 ? ALA A 109 ? SER A 162 ALA A 163 AA3 2 GLY A 202 ? ASN A 203 ? GLY A 256 ASN A 257 AA4 1 LEU A 120 ? TYR A 122 ? LEU A 174 TYR A 176 AA4 2 ILE A 146 ? ARG A 150 ? ILE A 200 ARG A 204 AA4 3 GLY A 170 ? TYR A 174 ? GLY A 224 TYR A 228 AA4 4 VAL A 240 ? ILE A 243 ? VAL A 294 ILE A 297 # 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 AA1 1 2 N ALA A 57 ? N ALA A 111 O ASN A 303 ? O ASN A 357 AA1 2 3 N GLY A 306 ? N GLY A 360 O PHE A 364 ? O PHE A 418 AA1 3 4 O LEU A 363 ? O LEU A 417 N LEU A 320 ? N LEU A 374 AA1 4 5 N ILE A 319 ? N ILE A 373 O ILE A 396 ? O ILE A 450 AA1 5 6 N ASN A 397 ? N ASN A 451 O GLY A 479 ? O GLY A 533 AA1 6 7 O THR A 484 ? O THR A 538 N THR A 407 ? N THR A 461 AA2 1 2 O PHE A 85 ? O PHE A 139 N ILE A 76 ? N ILE A 130 AA2 2 3 N SER A 75 ? N SER A 129 O LYS A 289 ? O LYS A 343 AA2 3 4 O VAL A 288 ? O VAL A 342 N GLY A 118 ? N GLY A 172 AA3 1 2 O ALA A 109 ? O ALA A 163 N GLY A 202 ? N GLY A 256 AA4 1 2 N VAL A 121 ? N VAL A 175 O ILE A 148 ? O ILE A 202 AA4 2 3 N ALA A 149 ? N ALA A 203 O ILE A 172 ? O ILE A 226 AA4 3 4 N LEU A 173 ? N LEU A 227 O HIS A 241 ? O HIS A 295 # 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 A ZN 801 ? 5 'binding site for residue ZN A 801' AC2 Software A ZN 802 ? 6 'binding site for residue ZN A 802' AC3 Software A CA 803 ? 5 'binding site for residue CA A 803' AC4 Software A CL 804 ? 3 'binding site for residue CL A 804' AC5 Software A 5PU 817 ? 19 'binding site for residue 5PU A 817' AC6 Software A ACT 818 ? 9 'binding site for residue ACT A 818' AC7 Software A ASN 76 ? 8 'binding site for Poly-Saccharide residues NAG A 805 through NAG A 806 bound to ASN A 76' AC8 Software A NAG 807 ? 4 'binding site for Mono-Saccharide NAG A 807 bound to ASN A 121' AC9 Software A ASN 140 ? 4 'binding site for Poly-Saccharide residues NAG A 808 through NAG A 809 bound to ASN A 140' AD1 Software A NAG 810 ? 8 'binding site for Mono-Saccharide NAG A 810 bound to ASN A 459' AD2 Software A ASN 476 ? 5 'binding site for Poly-Saccharide residues NAG A 811 through NAG A 812 bound to ASN A 476' AD3 Software A ASN 638 ? 17 'binding site for Poly-Saccharide residues NAG A 813 through MAN A 816 bound to ASN A 638' # 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 5 ASP A 333 ? ASP A 387 . ? 1_555 ? 2 AC1 5 GLU A 371 ? GLU A 425 . ? 1_555 ? 3 AC1 5 HIS A 499 ? HIS A 553 . ? 1_555 ? 4 AC1 5 ZN C . ? ZN A 802 . ? 1_555 ? 5 AC1 5 5PU R . ? 5PU A 817 . ? 1_555 ? 6 AC2 6 HIS A 323 ? HIS A 377 . ? 1_555 ? 7 AC2 6 ASP A 333 ? ASP A 387 . ? 1_555 ? 8 AC2 6 ASP A 399 ? ASP A 453 . ? 1_555 ? 9 AC2 6 ZN B . ? ZN A 801 . ? 1_555 ? 10 AC2 6 5PU R . ? 5PU A 817 . ? 1_555 ? 11 AC2 6 HOH T . ? HOH A 1126 . ? 1_555 ? 12 AC3 5 THR A 215 ? THR A 269 . ? 1_555 ? 13 AC3 5 TYR A 218 ? TYR A 272 . ? 1_555 ? 14 AC3 5 GLU A 379 ? GLU A 433 . ? 1_555 ? 15 AC3 5 GLU A 382 ? GLU A 436 . ? 1_555 ? 16 AC3 5 HOH T . ? HOH A 966 . ? 1_555 ? 17 AC4 3 ASN A 397 ? ASN A 451 . ? 1_555 ? 18 AC4 3 ASP A 399 ? ASP A 453 . ? 1_555 ? 19 AC4 3 ARG A 480 ? ARG A 534 . ? 1_555 ? 20 AC5 19 TYR A 180 ? TYR A 234 . ? 1_555 ? 21 AC5 19 HIS A 323 ? HIS A 377 . ? 1_555 ? 22 AC5 19 ASP A 333 ? ASP A 387 . ? 1_555 ? 23 AC5 19 GLU A 370 ? GLU A 424 . ? 1_555 ? 24 AC5 19 GLU A 371 ? GLU A 425 . ? 1_555 ? 25 AC5 19 ASP A 399 ? ASP A 453 . ? 1_555 ? 26 AC5 19 GLY A 464 ? GLY A 518 . ? 1_555 ? 27 AC5 19 ASN A 465 ? ASN A 519 . ? 1_555 ? 28 AC5 19 ARG A 480 ? ARG A 534 . ? 1_555 ? 29 AC5 19 ARG A 482 ? ARG A 536 . ? 1_555 ? 30 AC5 19 GLY A 494 ? GLY A 548 . ? 1_555 ? 31 AC5 19 TYR A 495 ? TYR A 549 . ? 1_555 ? 32 AC5 19 TYR A 498 ? TYR A 552 . ? 1_555 ? 33 AC5 19 HIS A 499 ? HIS A 553 . ? 1_555 ? 34 AC5 19 ZN B . ? ZN A 801 . ? 1_555 ? 35 AC5 19 ZN C . ? ZN A 802 . ? 1_555 ? 36 AC5 19 ACT S . ? ACT A 818 . ? 1_555 ? 37 AC5 19 HOH T . ? HOH A 1126 . ? 1_555 ? 38 AC5 19 HOH T . ? HOH A 1159 . ? 1_555 ? 39 AC6 9 ARG A 156 ? ARG A 210 . ? 1_555 ? 40 AC6 9 GLU A 371 ? GLU A 425 . ? 1_555 ? 41 AC6 9 TYR A 498 ? TYR A 552 . ? 1_555 ? 42 AC6 9 HIS A 499 ? HIS A 553 . ? 1_555 ? 43 AC6 9 5PU R . ? 5PU A 817 . ? 1_555 ? 44 AC6 9 HOH T . ? HOH A 1076 . ? 1_555 ? 45 AC6 9 HOH T . ? HOH A 1238 . ? 1_555 ? 46 AC6 9 HOH T . ? HOH A 1262 . ? 1_555 ? 47 AC6 9 HOH T . ? HOH A 1350 . ? 1_555 ? 48 AC7 8 ASN A 22 ? ASN A 76 . ? 1_555 ? 49 AC7 8 GLN A 41 ? GLN A 95 . ? 1_555 ? 50 AC7 8 GLN A 45 ? GLN A 99 . ? 1_555 ? 51 AC7 8 HOH T . ? HOH A 911 . ? 1_555 ? 52 AC7 8 HOH T . ? HOH A 1087 . ? 1_555 ? 53 AC7 8 HOH T . ? HOH A 1246 . ? 1_555 ? 54 AC7 8 HOH T . ? HOH A 1265 . ? 1_555 ? 55 AC7 8 HOH T . ? HOH A 1307 . ? 1_555 ? 56 AC8 4 ASN A 67 ? ASN A 121 . ? 1_555 ? 57 AC8 4 THR A 69 ? THR A 123 . ? 1_555 ? 58 AC8 4 HIS A 70 ? HIS A 124 . ? 1_555 ? 59 AC8 4 THR A 295 ? THR A 349 . ? 1_555 ? 60 AC9 4 TYR A 73 ? TYR A 127 . ? 1_555 ? 61 AC9 4 GLU A 83 ? GLU A 137 . ? 1_555 ? 62 AC9 4 ILE A 84 ? ILE A 138 . ? 1_555 ? 63 AC9 4 ASN A 86 ? ASN A 140 . ? 1_555 ? 64 AD1 8 TRP A 192 ? TRP A 246 . ? 1_555 ? 65 AD1 8 ASN A 405 ? ASN A 459 . ? 1_555 ? 66 AD1 8 PHE A 511 ? PHE A 565 . ? 1_555 ? 67 AD1 8 TYR A 512 ? TYR A 566 . ? 1_555 ? 68 AD1 8 HOH T . ? HOH A 924 . ? 1_555 ? 69 AD1 8 HOH T . ? HOH A 1154 . ? 1_555 ? 70 AD1 8 HOH T . ? HOH A 1217 . ? 1_555 ? 71 AD1 8 HOH T . ? HOH A 1245 . ? 1_555 ? 72 AD2 5 SER A 418 ? SER A 472 . ? 1_555 ? 73 AD2 5 ASN A 422 ? ASN A 476 . ? 1_555 ? 74 AD2 5 GLN A 597 ? GLN A 651 . ? 1_555 ? 75 AD2 5 HOH T . ? HOH A 1150 . ? 1_555 ? 76 AD2 5 HOH T . ? HOH A 1267 . ? 1_555 ? 77 AD3 17 HIS A 58 ? HIS A 112 . ? 2_565 ? 78 AD3 17 PHE A 181 ? PHE A 235 . ? 7_555 ? 79 AD3 17 LYS A 186 ? LYS A 240 . ? 7_555 ? 80 AD3 17 SER A 187 ? SER A 241 . ? 7_555 ? 81 AD3 17 GLU A 222 ? GLU A 276 . ? 2_565 ? 82 AD3 17 TYR A 223 ? TYR A 277 . ? 2_565 ? 83 AD3 17 ARG A 300 ? ARG A 354 . ? 2_565 ? 84 AD3 17 SER A 577 ? SER A 631 . ? 1_555 ? 85 AD3 17 SER A 580 ? SER A 634 . ? 1_555 ? 86 AD3 17 ASN A 584 ? ASN A 638 . ? 1_555 ? 87 AD3 17 GLN A 686 ? GLN A 740 . ? 1_555 ? 88 AD3 17 HOH T . ? HOH A 903 . ? 2_565 ? 89 AD3 17 HOH T . ? HOH A 916 . ? 2_565 ? 90 AD3 17 HOH T . ? HOH A 952 . ? 1_555 ? 91 AD3 17 HOH T . ? HOH A 1143 . ? 7_555 ? 92 AD3 17 HOH T . ? HOH A 1176 . ? 1_555 ? 93 AD3 17 HOH T . ? HOH A 1210 . ? 1_555 ? # _atom_sites.entry_id 5ELY _atom_sites.fract_transf_matrix[1][1] 0.009895 _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] 0.007644 _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] 0.006314 _atom_sites.fract_transf_vector[1] 0.000000 _atom_sites.fract_transf_vector[2] 0.000000 _atom_sites.fract_transf_vector[3] 0.000000 # loop_ _atom_type.symbol C CA CL N O S ZN # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . LYS A 1 1 ? 16.257 45.515 82.590 1.00 56.85 ? 55 LYS A N 1 ATOM 2 C CA . LYS A 1 1 ? 15.987 46.753 81.766 1.00 56.42 ? 55 LYS A CA 1 ATOM 3 C C . LYS A 1 1 ? 15.627 46.438 80.296 1.00 54.42 ? 55 LYS A C 1 ATOM 4 O O . LYS A 1 1 ? 16.178 45.511 79.692 1.00 53.62 ? 55 LYS A O 1 ATOM 5 C CB . LYS A 1 1 ? 17.197 47.706 81.834 1.00 57.38 ? 55 LYS A CB 1 ATOM 6 C CG . LYS A 1 1 ? 16.872 49.143 82.257 1.00 60.03 ? 55 LYS A CG 1 ATOM 7 C CD . LYS A 1 1 ? 16.282 49.954 81.084 1.00 63.80 ? 55 LYS A CD 1 ATOM 8 C CE . LYS A 1 1 ? 15.919 51.385 81.490 1.00 65.08 ? 55 LYS A CE 1 ATOM 9 N NZ . LYS A 1 1 ? 15.238 52.095 80.365 1.00 66.33 ? 55 LYS A NZ 1 ATOM 10 N N . HIS A 1 2 ? 14.677 47.194 79.746 1.00 52.17 ? 56 HIS A N 1 ATOM 11 C CA . HIS A 1 2 ? 14.328 47.097 78.322 1.00 49.67 ? 56 HIS A CA 1 ATOM 12 C C . HIS A 1 2 ? 14.788 48.382 77.640 1.00 47.26 ? 56 HIS A C 1 ATOM 13 O O . HIS A 1 2 ? 14.106 49.400 77.719 1.00 47.60 ? 56 HIS A O 1 ATOM 14 C CB . HIS A 1 2 ? 12.818 46.927 78.140 1.00 50.36 ? 56 HIS A CB 1 ATOM 15 C CG . HIS A 1 2 ? 12.286 45.606 78.609 1.00 52.33 ? 56 HIS A CG 1 ATOM 16 N ND1 . HIS A 1 2 ? 11.142 45.496 79.378 1.00 53.57 ? 56 HIS A ND1 1 ATOM 17 C CD2 . HIS A 1 2 ? 12.737 44.343 78.416 1.00 51.43 ? 56 HIS A CD2 1 ATOM 18 C CE1 . HIS A 1 2 ? 10.911 44.219 79.631 1.00 53.92 ? 56 HIS A CE1 1 ATOM 19 N NE2 . HIS A 1 2 ? 11.860 43.501 79.055 1.00 53.23 ? 56 HIS A NE2 1 ATOM 20 N N . ASN A 1 3 ? 15.971 48.338 77.032 1.00 43.24 ? 57 ASN A N 1 ATOM 21 C CA . ASN A 1 3 ? 16.568 49.477 76.341 1.00 39.89 ? 57 ASN A CA 1 ATOM 22 C C . ASN A 1 3 ? 17.179 48.933 75.069 1.00 37.15 ? 57 ASN A C 1 ATOM 23 O O . ASN A 1 3 ? 16.984 47.749 74.748 1.00 36.17 ? 57 ASN A O 1 ATOM 24 C CB . ASN A 1 3 ? 17.651 50.159 77.184 1.00 39.86 ? 57 ASN A CB 1 ATOM 25 C CG . ASN A 1 3 ? 18.608 49.162 77.836 1.00 39.63 ? 57 ASN A CG 1 ATOM 26 O OD1 . ASN A 1 3 ? 18.827 48.044 77.345 1.00 36.62 ? 57 ASN A OD1 1 ATOM 27 N ND2 . ASN A 1 3 ? 19.155 49.560 78.990 1.00 37.20 ? 57 ASN A ND2 1 ATOM 28 N N . MET A 1 4 ? 17.943 49.763 74.355 1.00 35.65 ? 58 MET A N 1 ATOM 29 C CA A MET A 1 4 ? 18.501 49.337 73.064 0.60 35.02 ? 58 MET A CA 1 ATOM 30 C CA B MET A 1 4 ? 18.443 49.279 73.075 0.40 34.10 ? 58 MET A CA 1 ATOM 31 C C . MET A 1 4 ? 19.472 48.178 73.252 1.00 33.84 ? 58 MET A C 1 ATOM 32 O O . MET A 1 4 ? 19.480 47.229 72.483 1.00 32.75 ? 58 MET A O 1 ATOM 33 C CB A MET A 1 4 ? 19.181 50.491 72.317 0.60 34.90 ? 58 MET A CB 1 ATOM 34 C CB B MET A 1 4 ? 18.962 50.368 72.150 0.40 33.60 ? 58 MET A CB 1 ATOM 35 C CG A MET A 1 4 ? 19.471 50.137 70.836 0.60 37.83 ? 58 MET A CG 1 ATOM 36 C CG B MET A 1 4 ? 18.949 49.853 70.701 0.40 31.78 ? 58 MET A CG 1 ATOM 37 S SD A MET A 1 4 ? 19.873 51.565 69.816 0.60 43.24 ? 58 MET A SD 1 ATOM 38 S SD B MET A 1 4 ? 20.192 50.586 69.659 0.40 30.05 ? 58 MET A SD 1 ATOM 39 C CE A MET A 1 4 ? 21.472 52.015 70.457 0.60 42.30 ? 58 MET A CE 1 ATOM 40 C CE B MET A 1 4 ? 19.470 52.217 69.404 0.40 30.46 ? 58 MET A CE 1 ATOM 41 N N . LYS A 1 5 ? 20.299 48.269 74.288 1.00 33.46 ? 59 LYS A N 1 ATOM 42 C CA . LYS A 1 5 ? 21.265 47.191 74.546 1.00 33.68 ? 59 LYS A CA 1 ATOM 43 C C . LYS A 1 5 ? 20.563 45.839 74.714 1.00 32.35 ? 59 LYS A C 1 ATOM 44 O O . LYS A 1 5 ? 21.009 44.828 74.172 1.00 33.98 ? 59 LYS A O 1 ATOM 45 C CB . LYS A 1 5 ? 22.116 47.515 75.799 1.00 33.71 ? 59 LYS A CB 1 ATOM 46 C CG . LYS A 1 5 ? 23.276 46.546 75.964 1.00 37.68 ? 59 LYS A CG 1 ATOM 47 C CD . LYS A 1 5 ? 24.390 47.206 76.824 1.00 47.58 ? 59 LYS A CD 1 ATOM 48 C CE . LYS A 1 5 ? 25.647 46.312 76.902 1.00 51.87 ? 59 LYS A CE 1 ATOM 49 N NZ . LYS A 1 5 ? 25.352 45.083 77.710 1.00 54.70 ? 59 LYS A NZ 1 ATOM 50 N N . ALA A 1 6 ? 19.477 45.810 75.476 1.00 33.23 ? 60 ALA A N 1 ATOM 51 C CA . ALA A 1 6 ? 18.680 44.583 75.612 1.00 33.03 ? 60 ALA A CA 1 ATOM 52 C C . ALA A 1 6 ? 18.228 44.060 74.257 1.00 31.96 ? 60 ALA A C 1 ATOM 53 O O . ALA A 1 6 ? 18.374 42.879 73.967 1.00 30.88 ? 60 ALA A O 1 ATOM 54 C CB . ALA A 1 6 ? 17.485 44.802 76.494 1.00 34.41 ? 60 ALA A CB 1 ATOM 55 N N . PHE A 1 7 ? 17.677 44.958 73.439 1.00 30.55 ? 61 PHE A N 1 ATOM 56 C CA . PHE A 1 7 ? 17.317 44.590 72.087 1.00 29.44 ? 61 PHE A CA 1 ATOM 57 C C . PHE A 1 7 ? 18.510 44.020 71.293 1.00 28.14 ? 61 PHE A C 1 ATOM 58 O O . PHE A 1 7 ? 18.440 42.933 70.685 1.00 28.68 ? 61 PHE A O 1 ATOM 59 C CB . PHE A 1 7 ? 16.672 45.777 71.337 1.00 28.29 ? 61 PHE A CB 1 ATOM 60 C CG . PHE A 1 7 ? 16.581 45.512 69.860 1.00 27.07 ? 61 PHE A CG 1 ATOM 61 C CD1 . PHE A 1 7 ? 15.639 44.607 69.361 1.00 27.82 ? 61 PHE A CD1 1 ATOM 62 C CD2 . PHE A 1 7 ? 17.482 46.094 69.003 1.00 26.92 ? 61 PHE A CD2 1 ATOM 63 C CE1 . PHE A 1 7 ? 15.595 44.308 67.920 1.00 26.57 ? 61 PHE A CE1 1 ATOM 64 C CE2 . PHE A 1 7 ? 17.442 45.836 67.607 1.00 26.44 ? 61 PHE A CE2 1 ATOM 65 C CZ . PHE A 1 7 ? 16.505 44.934 67.087 1.00 26.78 ? 61 PHE A CZ 1 ATOM 66 N N . LEU A 1 8 ? 19.604 44.757 71.274 1.00 28.47 ? 62 LEU A N 1 ATOM 67 C CA . LEU A 1 8 ? 20.769 44.358 70.488 1.00 28.46 ? 62 LEU A CA 1 ATOM 68 C C . LEU A 1 8 ? 21.389 43.018 70.957 1.00 30.63 ? 62 LEU A C 1 ATOM 69 O O . LEU A 1 8 ? 21.784 42.175 70.133 1.00 29.42 ? 62 LEU A O 1 ATOM 70 C CB . LEU A 1 8 ? 21.817 45.465 70.547 1.00 29.19 ? 62 LEU A CB 1 ATOM 71 C CG . LEU A 1 8 ? 21.454 46.761 69.810 1.00 29.11 ? 62 LEU A CG 1 ATOM 72 C CD1 . LEU A 1 8 ? 22.477 47.854 70.146 1.00 30.72 ? 62 LEU A CD1 1 ATOM 73 C CD2 . LEU A 1 8 ? 21.370 46.498 68.282 1.00 28.05 ? 62 LEU A CD2 1 ATOM 74 N N . ASP A 1 9 ? 21.442 42.808 72.271 1.00 33.31 ? 63 ASP A N 1 ATOM 75 C CA . ASP A 1 9 ? 22.087 41.578 72.802 1.00 35.56 ? 63 ASP A CA 1 ATOM 76 C C . ASP A 1 9 ? 21.263 40.322 72.499 1.00 35.13 ? 63 ASP A C 1 ATOM 77 O O . ASP A 1 9 ? 21.791 39.227 72.507 1.00 35.65 ? 63 ASP A O 1 ATOM 78 C CB . ASP A 1 9 ? 22.330 41.669 74.331 1.00 36.58 ? 63 ASP A CB 1 ATOM 79 C CG . ASP A 1 9 ? 23.390 42.685 74.716 1.00 38.79 ? 63 ASP A CG 1 ATOM 80 O OD1 . ASP A 1 9 ? 24.213 43.101 73.881 1.00 42.27 ? 63 ASP A OD1 1 ATOM 81 O OD2 . ASP A 1 9 ? 23.392 43.107 75.895 1.00 42.36 ? 63 ASP A OD2 1 ATOM 82 N N . GLU A 1 10 ? 19.965 40.480 72.254 1.00 34.03 ? 64 GLU A N 1 ATOM 83 C CA . GLU A 1 10 ? 19.097 39.345 72.018 1.00 33.59 ? 64 GLU A CA 1 ATOM 84 C C . GLU A 1 10 ? 19.306 38.767 70.601 1.00 31.91 ? 64 GLU A C 1 ATOM 85 O O . GLU A 1 10 ? 19.167 37.554 70.392 1.00 31.88 ? 64 GLU A O 1 ATOM 86 C CB . GLU A 1 10 ? 17.625 39.694 72.305 1.00 33.93 ? 64 GLU A CB 1 ATOM 87 C CG . GLU A 1 10 ? 16.628 38.556 71.995 1.00 37.13 ? 64 GLU A CG 1 ATOM 88 C CD . GLU A 1 10 ? 16.846 37.299 72.857 1.00 42.79 ? 64 GLU A CD 1 ATOM 89 O OE1 . GLU A 1 10 ? 17.191 37.466 74.038 1.00 44.20 ? 64 GLU A OE1 1 ATOM 90 O OE2 . GLU A 1 10 ? 16.671 36.162 72.360 1.00 40.04 ? 64 GLU A OE2 1 ATOM 91 N N . LEU A 1 11 ? 19.697 39.631 69.656 1.00 30.32 ? 65 LEU A N 1 ATOM 92 C CA . LEU A 1 11 ? 20.099 39.210 68.302 1.00 29.35 ? 65 LEU A CA 1 ATOM 93 C C . LEU A 1 11 ? 21.256 38.194 68.339 1.00 30.71 ? 65 LEU A C 1 ATOM 94 O O . LEU A 1 11 ? 22.273 38.486 68.970 1.00 29.86 ? 65 LEU A O 1 ATOM 95 C CB . LEU A 1 11 ? 20.525 40.418 67.465 1.00 28.98 ? 65 LEU A CB 1 ATOM 96 C CG . LEU A 1 11 ? 19.521 41.583 67.302 1.00 26.53 ? 65 LEU A CG 1 ATOM 97 C CD1 . LEU A 1 11 ? 20.288 42.774 66.755 1.00 25.40 ? 65 LEU A CD1 1 ATOM 98 C CD2 . LEU A 1 11 ? 18.393 41.180 66.336 1.00 25.54 ? 65 LEU A CD2 1 ATOM 99 N N . LYS A 1 12 ? 21.109 37.063 67.637 1.00 30.34 ? 66 LYS A N 1 ATOM 100 C CA . LYS A 1 12 ? 22.141 36.021 67.581 1.00 32.09 ? 66 LYS A CA 1 ATOM 101 C C . LYS A 1 12 ? 22.517 35.661 66.141 1.00 30.15 ? 66 LYS A C 1 ATOM 102 O O . LYS A 1 12 ? 21.640 35.339 65.326 1.00 28.86 ? 66 LYS A O 1 ATOM 103 C CB . LYS A 1 12 ? 21.640 34.718 68.272 1.00 33.18 ? 66 LYS A CB 1 ATOM 104 C CG . LYS A 1 12 ? 21.143 34.892 69.740 1.00 36.31 ? 66 LYS A CG 1 ATOM 105 C CD . LYS A 1 12 ? 22.310 35.241 70.663 1.00 41.81 ? 66 LYS A CD 1 ATOM 106 C CE . LYS A 1 12 ? 21.950 35.129 72.163 1.00 43.04 ? 66 LYS A CE 1 ATOM 107 N NZ . LYS A 1 12 ? 21.306 36.379 72.642 1.00 40.95 ? 66 LYS A NZ 1 ATOM 108 N N . ALA A 1 13 ? 23.814 35.677 65.841 1.00 30.32 ? 67 ALA A N 1 ATOM 109 C CA . ALA A 1 13 ? 24.336 35.169 64.581 1.00 29.68 ? 67 ALA A CA 1 ATOM 110 C C . ALA A 1 13 ? 23.797 33.782 64.215 1.00 30.54 ? 67 ALA A C 1 ATOM 111 O O . ALA A 1 13 ? 23.509 33.536 63.041 1.00 29.75 ? 67 ALA A O 1 ATOM 112 C CB . ALA A 1 13 ? 25.879 35.103 64.635 1.00 30.34 ? 67 ALA A CB 1 ATOM 113 N N . GLU A 1 14 ? 23.704 32.877 65.197 1.00 31.29 ? 68 GLU A N 1 ATOM 114 C CA A GLU A 1 14 ? 23.314 31.483 64.898 0.60 32.07 ? 68 GLU A CA 1 ATOM 115 C CA B GLU A 1 14 ? 23.294 31.477 64.960 0.40 31.42 ? 68 GLU A CA 1 ATOM 116 C C . GLU A 1 14 ? 21.855 31.416 64.443 1.00 31.21 ? 68 GLU A C 1 ATOM 117 O O . GLU A 1 14 ? 21.504 30.557 63.617 1.00 31.39 ? 68 GLU A O 1 ATOM 118 C CB A GLU A 1 14 ? 23.546 30.572 66.110 0.60 33.51 ? 68 GLU A CB 1 ATOM 119 C CB B GLU A 1 14 ? 23.480 30.606 66.233 0.40 32.36 ? 68 GLU A CB 1 ATOM 120 C CG A GLU A 1 14 ? 23.165 29.100 65.916 0.60 36.58 ? 68 GLU A CG 1 ATOM 121 C CG B GLU A 1 14 ? 22.679 31.021 67.493 0.40 32.78 ? 68 GLU A CG 1 ATOM 122 C CD A GLU A 1 14 ? 24.124 28.322 65.033 0.60 41.18 ? 68 GLU A CD 1 ATOM 123 C CD B GLU A 1 14 ? 23.418 30.738 68.843 0.40 35.53 ? 68 GLU A CD 1 ATOM 124 O OE1 A GLU A 1 14 ? 23.707 27.258 64.540 0.60 44.63 ? 68 GLU A OE1 1 ATOM 125 O OE1 B GLU A 1 14 ? 23.837 29.586 69.084 0.40 38.52 ? 68 GLU A OE1 1 ATOM 126 O OE2 A GLU A 1 14 ? 25.284 28.751 64.826 0.60 42.21 ? 68 GLU A OE2 1 ATOM 127 O OE2 B GLU A 1 14 ? 23.572 31.668 69.664 0.40 32.76 ? 68 GLU A OE2 1 ATOM 128 N N . ASN A 1 15 ? 21.026 32.338 64.932 1.00 29.10 ? 69 ASN A N 1 ATOM 129 C CA . ASN A 1 15 ? 19.634 32.362 64.461 1.00 29.62 ? 69 ASN A CA 1 ATOM 130 C C . ASN A 1 15 ? 19.531 32.838 63.022 1.00 27.72 ? 69 ASN A C 1 ATOM 131 O O . ASN A 1 15 ? 18.774 32.260 62.251 1.00 27.18 ? 69 ASN A O 1 ATOM 132 C CB . ASN A 1 15 ? 18.752 33.246 65.324 1.00 29.25 ? 69 ASN A CB 1 ATOM 133 C CG . ASN A 1 15 ? 18.473 32.649 66.692 1.00 33.33 ? 69 ASN A CG 1 ATOM 134 O OD1 . ASN A 1 15 ? 18.404 31.419 66.857 1.00 33.98 ? 69 ASN A OD1 1 ATOM 135 N ND2 . ASN A 1 15 ? 18.339 33.524 67.688 1.00 31.60 ? 69 ASN A ND2 1 ATOM 136 N N . ILE A 1 16 ? 20.284 33.883 62.674 1.00 27.08 ? 70 ILE A N 1 ATOM 137 C CA . ILE A 1 16 ? 20.278 34.420 61.291 1.00 26.00 ? 70 ILE A CA 1 ATOM 138 C C . ILE A 1 16 ? 20.720 33.304 60.322 1.00 26.54 ? 70 ILE A C 1 ATOM 139 O O . ILE A 1 16 ? 20.142 33.097 59.251 1.00 26.70 ? 70 ILE A O 1 ATOM 140 C CB . ILE A 1 16 ? 21.175 35.678 61.182 1.00 25.93 ? 70 ILE A CB 1 ATOM 141 C CG1 . ILE A 1 16 ? 20.616 36.828 62.072 1.00 24.93 ? 70 ILE A CG1 1 ATOM 142 C CG2 . ILE A 1 16 ? 21.264 36.157 59.710 1.00 26.49 ? 70 ILE A CG2 1 ATOM 143 C CD1 . ILE A 1 16 ? 21.651 37.961 62.337 1.00 26.13 ? 70 ILE A CD1 1 ATOM 144 N N . LYS A 1 17 ? 21.726 32.525 60.742 1.00 26.44 ? 71 LYS A N 1 ATOM 145 C CA . LYS A 1 17 ? 22.193 31.385 59.963 1.00 26.08 ? 71 LYS A CA 1 ATOM 146 C C . LYS A 1 17 ? 21.080 30.360 59.729 1.00 26.04 ? 71 LYS A C 1 ATOM 147 O O . LYS A 1 17 ? 20.862 29.917 58.588 1.00 26.25 ? 71 LYS A O 1 ATOM 148 C CB . LYS A 1 17 ? 23.406 30.716 60.708 1.00 26.51 ? 71 LYS A CB 1 ATOM 149 C CG . LYS A 1 17 ? 23.981 29.516 59.956 1.00 29.08 ? 71 LYS A CG 1 ATOM 150 C CD . LYS A 1 17 ? 25.186 28.929 60.748 1.00 32.56 ? 71 LYS A CD 1 ATOM 151 C CE . LYS A 1 17 ? 25.747 27.710 60.051 1.00 33.13 ? 71 LYS A CE 1 ATOM 152 N NZ . LYS A 1 17 ? 26.975 27.211 60.802 1.00 33.45 ? 71 LYS A NZ 1 ATOM 153 N N A LYS A 1 18 ? 20.412 29.948 60.800 0.50 26.42 ? 72 LYS A N 1 ATOM 154 N N B LYS A 1 18 ? 20.409 29.977 60.819 0.50 26.69 ? 72 LYS A N 1 ATOM 155 C CA A LYS A 1 18 ? 19.302 29.000 60.658 0.50 26.40 ? 72 LYS A CA 1 ATOM 156 C CA B LYS A 1 18 ? 19.243 29.061 60.815 0.50 26.93 ? 72 LYS A CA 1 ATOM 157 C C A LYS A 1 18 ? 18.214 29.524 59.704 0.50 25.54 ? 72 LYS A C 1 ATOM 158 C C B LYS A 1 18 ? 18.108 29.488 59.859 0.50 25.96 ? 72 LYS A C 1 ATOM 159 O O A LYS A 1 18 ? 17.789 28.804 58.802 0.50 24.65 ? 72 LYS A O 1 ATOM 160 O O B LYS A 1 18 ? 17.528 28.673 59.135 0.50 25.02 ? 72 LYS A O 1 ATOM 161 C CB A LYS A 1 18 ? 18.717 28.635 62.014 0.50 26.60 ? 72 LYS A CB 1 ATOM 162 C CB B LYS A 1 18 ? 18.689 28.982 62.230 0.50 27.34 ? 72 LYS A CB 1 ATOM 163 C CG A LYS A 1 18 ? 19.671 27.787 62.838 0.50 28.10 ? 72 LYS A CG 1 ATOM 164 C CG B LYS A 1 18 ? 17.468 28.112 62.417 0.50 30.20 ? 72 LYS A CG 1 ATOM 165 C CD A LYS A 1 18 ? 19.229 27.652 64.290 0.50 30.47 ? 72 LYS A CD 1 ATOM 166 C CD B LYS A 1 18 ? 17.117 28.052 63.904 0.50 33.59 ? 72 LYS A CD 1 ATOM 167 C CE A LYS A 1 18 ? 20.157 26.668 65.028 0.50 33.77 ? 72 LYS A CE 1 ATOM 168 C CE B LYS A 1 18 ? 15.625 28.208 64.130 0.50 35.26 ? 72 LYS A CE 1 ATOM 169 N NZ A LYS A 1 18 ? 20.153 26.933 66.498 0.50 35.48 ? 72 LYS A NZ 1 ATOM 170 N NZ B LYS A 1 18 ? 15.392 28.934 65.414 0.50 37.04 ? 72 LYS A NZ 1 ATOM 171 N N . PHE A 1 19 ? 17.782 30.774 59.905 1.00 25.21 ? 73 PHE A N 1 ATOM 172 C CA . PHE A 1 19 ? 16.761 31.355 59.022 1.00 24.74 ? 73 PHE A CA 1 ATOM 173 C C . PHE A 1 19 ? 17.259 31.425 57.578 1.00 24.49 ? 73 PHE A C 1 ATOM 174 O O . PHE A 1 19 ? 16.495 31.110 56.654 1.00 24.06 ? 73 PHE A O 1 ATOM 175 C CB . PHE A 1 19 ? 16.382 32.774 59.551 1.00 24.24 ? 73 PHE A CB 1 ATOM 176 C CG . PHE A 1 19 ? 15.859 32.783 60.954 1.00 25.32 ? 73 PHE A CG 1 ATOM 177 C CD1 . PHE A 1 19 ? 15.102 31.706 61.442 1.00 29.13 ? 73 PHE A CD1 1 ATOM 178 C CD2 . PHE A 1 19 ? 16.010 33.929 61.761 1.00 23.42 ? 73 PHE A CD2 1 ATOM 179 C CE1 . PHE A 1 19 ? 14.590 31.733 62.763 1.00 29.03 ? 73 PHE A CE1 1 ATOM 180 C CE2 . PHE A 1 19 ? 15.497 33.978 63.072 1.00 26.68 ? 73 PHE A CE2 1 ATOM 181 C CZ . PHE A 1 19 ? 14.782 32.879 63.570 1.00 29.68 ? 73 PHE A CZ 1 ATOM 182 N N . LEU A 1 20 ? 18.542 31.764 57.357 1.00 24.24 ? 74 LEU A N 1 ATOM 183 C CA . LEU A 1 20 ? 19.011 31.851 55.977 1.00 23.59 ? 74 LEU A CA 1 ATOM 184 C C . LEU A 1 20 ? 18.916 30.482 55.335 1.00 24.79 ? 74 LEU A C 1 ATOM 185 O O . LEU A 1 20 ? 18.463 30.361 54.198 1.00 23.89 ? 74 LEU A O 1 ATOM 186 C CB . LEU A 1 20 ? 20.458 32.378 55.855 1.00 23.68 ? 74 LEU A CB 1 ATOM 187 C CG . LEU A 1 20 ? 20.982 32.535 54.415 1.00 25.04 ? 74 LEU A CG 1 ATOM 188 C CD1 . LEU A 1 20 ? 20.144 33.633 53.717 1.00 22.57 ? 74 LEU A CD1 1 ATOM 189 C CD2 . LEU A 1 20 ? 22.475 32.907 54.421 1.00 24.42 ? 74 LEU A CD2 1 ATOM 190 N N . TYR A 1 21 ? 19.355 29.452 56.067 1.00 24.80 ? 75 TYR A N 1 ATOM 191 C CA . TYR A 1 21 ? 19.273 28.091 55.540 1.00 25.20 ? 75 TYR A CA 1 ATOM 192 C C . TYR A 1 21 ? 17.808 27.751 55.219 1.00 24.20 ? 75 TYR A C 1 ATOM 193 O O . TYR A 1 21 ? 17.487 27.247 54.145 1.00 25.61 ? 75 TYR A O 1 ATOM 194 C CB . TYR A 1 21 ? 19.854 27.117 56.602 1.00 25.93 ? 75 TYR A CB 1 ATOM 195 C CG . TYR A 1 21 ? 19.779 25.708 56.108 1.00 27.70 ? 75 TYR A CG 1 ATOM 196 C CD1 . TYR A 1 21 ? 20.754 25.216 55.243 1.00 29.99 ? 75 TYR A CD1 1 ATOM 197 C CD2 . TYR A 1 21 ? 18.723 24.893 56.467 1.00 30.80 ? 75 TYR A CD2 1 ATOM 198 C CE1 . TYR A 1 21 ? 20.678 23.896 54.751 1.00 31.43 ? 75 TYR A CE1 1 ATOM 199 C CE2 . TYR A 1 21 ? 18.622 23.598 55.981 1.00 35.11 ? 75 TYR A CE2 1 ATOM 200 C CZ . TYR A 1 21 ? 19.615 23.109 55.141 1.00 35.13 ? 75 TYR A CZ 1 ATOM 201 O OH . TYR A 1 21 ? 19.516 21.815 54.672 1.00 39.35 ? 75 TYR A OH 1 ATOM 202 N N . ASN A 1 22 ? 16.920 28.068 56.140 1.00 25.74 ? 76 ASN A N 1 ATOM 203 C CA . ASN A 1 22 ? 15.497 27.783 55.997 1.00 25.63 ? 76 ASN A CA 1 ATOM 204 C C . ASN A 1 22 ? 14.847 28.450 54.751 1.00 25.70 ? 76 ASN A C 1 ATOM 205 O O . ASN A 1 22 ? 13.974 27.860 54.080 1.00 25.67 ? 76 ASN A O 1 ATOM 206 C CB . ASN A 1 22 ? 14.788 28.237 57.244 1.00 27.46 ? 76 ASN A CB 1 ATOM 207 C CG . ASN A 1 22 ? 13.323 27.880 57.232 1.00 30.15 ? 76 ASN A CG 1 ATOM 208 O OD1 . ASN A 1 22 ? 12.471 28.686 56.847 1.00 26.35 ? 76 ASN A OD1 1 ATOM 209 N ND2 . ASN A 1 22 ? 13.018 26.660 57.633 1.00 31.34 ? 76 ASN A ND2 1 ATOM 210 N N . PHE A 1 23 ? 15.326 29.660 54.438 1.00 24.60 ? 77 PHE A N 1 ATOM 211 C CA . PHE A 1 23 ? 14.762 30.482 53.377 1.00 23.53 ? 77 PHE A CA 1 ATOM 212 C C . PHE A 1 23 ? 15.344 30.213 51.988 1.00 23.76 ? 77 PHE A C 1 ATOM 213 O O . PHE A 1 23 ? 14.947 30.854 51.022 1.00 23.54 ? 77 PHE A O 1 ATOM 214 C CB . PHE A 1 23 ? 14.977 31.994 53.701 1.00 23.04 ? 77 PHE A CB 1 ATOM 215 C CG . PHE A 1 23 ? 14.204 32.532 54.890 1.00 25.27 ? 77 PHE A CG 1 ATOM 216 C CD1 . PHE A 1 23 ? 13.215 31.815 55.568 1.00 25.11 ? 77 PHE A CD1 1 ATOM 217 C CD2 . PHE A 1 23 ? 14.505 33.821 55.330 1.00 25.44 ? 77 PHE A CD2 1 ATOM 218 C CE1 . PHE A 1 23 ? 12.561 32.383 56.719 1.00 24.20 ? 77 PHE A CE1 1 ATOM 219 C CE2 . PHE A 1 23 ? 13.870 34.407 56.409 1.00 20.65 ? 77 PHE A CE2 1 ATOM 220 C CZ . PHE A 1 23 ? 12.876 33.691 57.122 1.00 23.56 ? 77 PHE A CZ 1 ATOM 221 N N . THR A 1 24 ? 16.316 29.286 51.836 1.00 22.75 ? 78 THR A N 1 ATOM 222 C CA . THR A 1 24 ? 17.067 29.247 50.601 1.00 23.12 ? 78 THR A CA 1 ATOM 223 C C . THR A 1 24 ? 17.199 27.815 50.044 1.00 23.84 ? 78 THR A C 1 ATOM 224 O O . THR A 1 24 ? 18.051 27.567 49.174 1.00 21.87 ? 78 THR A O 1 ATOM 225 C CB . THR A 1 24 ? 18.527 29.774 50.810 1.00 22.70 ? 78 THR A CB 1 ATOM 226 O OG1 . THR A 1 24 ? 19.126 29.060 51.899 1.00 23.39 ? 78 THR A OG1 1 ATOM 227 C CG2 . THR A 1 24 ? 18.482 31.295 51.208 1.00 22.64 ? 78 THR A CG2 1 ATOM 228 N N . GLN A 1 25 ? 16.370 26.916 50.545 1.00 24.71 ? 79 GLN A N 1 ATOM 229 C CA . GLN A 1 25 ? 16.444 25.502 50.065 1.00 27.37 ? 79 GLN A CA 1 ATOM 230 C C . GLN A 1 25 ? 15.698 25.273 48.750 1.00 27.67 ? 79 GLN A C 1 ATOM 231 O O . GLN A 1 25 ? 15.985 24.294 48.033 1.00 26.94 ? 79 GLN A O 1 ATOM 232 C CB . GLN A 1 25 ? 15.920 24.542 51.175 1.00 28.08 ? 79 GLN A CB 1 ATOM 233 C CG . GLN A 1 25 ? 16.741 24.624 52.437 1.00 31.05 ? 79 GLN A CG 1 ATOM 234 C CD . GLN A 1 25 ? 18.222 24.508 52.114 1.00 35.94 ? 79 GLN A CD 1 ATOM 235 O OE1 . GLN A 1 25 ? 18.634 23.442 51.659 1.00 39.17 ? 79 GLN A OE1 1 ATOM 236 N NE2 . GLN A 1 25 ? 19.025 25.614 52.278 1.00 32.46 ? 79 GLN A NE2 1 ATOM 237 N N . ILE A 1 26 ? 14.686 26.097 48.443 1.00 26.12 ? 80 ILE A N 1 ATOM 238 C CA . ILE A 1 26 ? 13.967 25.984 47.180 1.00 27.75 ? 80 ILE A CA 1 ATOM 239 C C . ILE A 1 26 ? 13.798 27.394 46.595 1.00 26.56 ? 80 ILE A C 1 ATOM 240 O O . ILE A 1 26 ? 13.950 28.375 47.348 1.00 26.64 ? 80 ILE A O 1 ATOM 241 C CB . ILE A 1 26 ? 12.538 25.360 47.360 1.00 28.70 ? 80 ILE A CB 1 ATOM 242 C CG1 . ILE A 1 26 ? 11.659 26.301 48.177 1.00 29.90 ? 80 ILE A CG1 1 ATOM 243 C CG2 . ILE A 1 26 ? 12.645 23.921 47.935 1.00 31.30 ? 80 ILE A CG2 1 ATOM 244 C CD1 . ILE A 1 26 ? 10.217 25.870 48.397 1.00 34.26 ? 80 ILE A CD1 1 ATOM 245 N N . PRO A 1 27 ? 13.473 27.495 45.289 1.00 26.41 ? 81 PRO A N 1 ATOM 246 C CA . PRO A 1 27 ? 13.362 28.853 44.730 1.00 25.04 ? 81 PRO A CA 1 ATOM 247 C C . PRO A 1 27 ? 12.092 29.519 45.250 1.00 23.95 ? 81 PRO A C 1 ATOM 248 O O . PRO A 1 27 ? 11.095 28.820 45.543 1.00 23.34 ? 81 PRO A O 1 ATOM 249 C CB . PRO A 1 27 ? 13.249 28.617 43.226 1.00 25.76 ? 81 PRO A CB 1 ATOM 250 C CG . PRO A 1 27 ? 13.877 27.240 42.992 1.00 27.31 ? 81 PRO A CG 1 ATOM 251 C CD . PRO A 1 27 ? 13.469 26.459 44.228 1.00 26.61 ? 81 PRO A CD 1 ATOM 252 N N . HIS A 1 28 ? 12.132 30.843 45.378 1.00 22.11 ? 82 HIS A N 1 ATOM 253 C CA . HIS A 1 28 ? 10.944 31.608 45.779 1.00 22.36 ? 82 HIS A CA 1 ATOM 254 C C . HIS A 1 28 ? 10.633 32.738 44.770 1.00 20.93 ? 82 HIS A C 1 ATOM 255 O O . HIS A 1 28 ? 10.560 33.911 45.143 1.00 19.94 ? 82 HIS A O 1 ATOM 256 C CB . HIS A 1 28 ? 11.128 32.160 47.218 1.00 22.16 ? 82 HIS A CB 1 ATOM 257 C CG . HIS A 1 28 ? 11.249 31.069 48.250 1.00 22.90 ? 82 HIS A CG 1 ATOM 258 N ND1 . HIS A 1 28 ? 12.465 30.700 48.789 1.00 22.29 ? 82 HIS A ND1 1 ATOM 259 C CD2 . HIS A 1 28 ? 10.330 30.218 48.773 1.00 24.69 ? 82 HIS A CD2 1 ATOM 260 C CE1 . HIS A 1 28 ? 12.281 29.692 49.630 1.00 23.17 ? 82 HIS A CE1 1 ATOM 261 N NE2 . HIS A 1 28 ? 10.991 29.396 49.658 1.00 22.47 ? 82 HIS A NE2 1 ATOM 262 N N . LEU A 1 29 ? 10.468 32.370 43.499 1.00 21.07 ? 83 LEU A N 1 ATOM 263 C CA . LEU A 1 29 ? 10.140 33.351 42.464 1.00 21.47 ? 83 LEU A CA 1 ATOM 264 C C . LEU A 1 29 ? 8.789 34.004 42.720 1.00 21.62 ? 83 LEU A C 1 ATOM 265 O O . LEU A 1 29 ? 7.815 33.351 43.103 1.00 21.37 ? 83 LEU A O 1 ATOM 266 C CB . LEU A 1 29 ? 10.172 32.664 41.047 1.00 20.89 ? 83 LEU A CB 1 ATOM 267 C CG . LEU A 1 29 ? 9.999 33.541 39.801 1.00 20.93 ? 83 LEU A CG 1 ATOM 268 C CD1 . LEU A 1 29 ? 11.155 34.490 39.679 1.00 22.23 ? 83 LEU A CD1 1 ATOM 269 C CD2 . LEU A 1 29 ? 9.906 32.529 38.507 1.00 19.67 ? 83 LEU A CD2 1 ATOM 270 N N . ALA A 1 30 ? 8.711 35.317 42.504 1.00 20.54 ? 84 ALA A N 1 ATOM 271 C CA . ALA A 1 30 ? 7.439 36.010 42.706 1.00 20.13 ? 84 ALA A CA 1 ATOM 272 C C . ALA A 1 30 ? 6.327 35.364 41.903 1.00 20.84 ? 84 ALA A C 1 ATOM 273 O O . ALA A 1 30 ? 6.514 34.987 40.747 1.00 20.48 ? 84 ALA A O 1 ATOM 274 C CB . ALA A 1 30 ? 7.552 37.486 42.244 1.00 18.40 ? 84 ALA A CB 1 ATOM 275 N N . GLY A 1 31 ? 5.147 35.278 42.510 1.00 21.06 ? 85 GLY A N 1 ATOM 276 C CA . GLY A 1 31 ? 3.988 34.760 41.827 1.00 22.27 ? 85 GLY A CA 1 ATOM 277 C C . GLY A 1 31 ? 3.913 33.242 41.837 1.00 24.61 ? 85 GLY A C 1 ATOM 278 O O . GLY A 1 31 ? 2.943 32.674 41.337 1.00 25.79 ? 85 GLY A O 1 ATOM 279 N N . THR A 1 32 ? 4.893 32.568 42.413 1.00 22.69 ? 86 THR A N 1 ATOM 280 C CA . THR A 1 32 ? 4.834 31.090 42.422 1.00 24.14 ? 86 THR A CA 1 ATOM 281 C C . THR A 1 32 ? 4.284 30.537 43.731 1.00 24.13 ? 86 THR A C 1 ATOM 282 O O . THR A 1 32 ? 4.344 31.179 44.774 1.00 22.51 ? 86 THR A O 1 ATOM 283 C CB . THR A 1 32 ? 6.225 30.416 42.141 1.00 22.92 ? 86 THR A CB 1 ATOM 284 O OG1 . THR A 1 32 ? 7.142 30.698 43.218 1.00 24.58 ? 86 THR A OG1 1 ATOM 285 C CG2 . THR A 1 32 ? 6.817 30.887 40.766 1.00 23.72 ? 86 THR A CG2 1 ATOM 286 N N . GLU A 1 33 ? 3.776 29.300 43.678 1.00 25.32 ? 87 GLU A N 1 ATOM 287 C CA . GLU A 1 33 ? 3.268 28.649 44.875 1.00 27.60 ? 87 GLU A CA 1 ATOM 288 C C . GLU A 1 33 ? 4.286 28.608 46.027 1.00 26.44 ? 87 GLU A C 1 ATOM 289 O O . GLU A 1 33 ? 3.895 28.809 47.196 1.00 26.01 ? 87 GLU A O 1 ATOM 290 C CB . GLU A 1 33 ? 2.808 27.203 44.558 1.00 29.85 ? 87 GLU A CB 1 ATOM 291 C CG . GLU A 1 33 ? 2.285 26.475 45.819 1.00 37.15 ? 87 GLU A CG 1 ATOM 292 C CD . GLU A 1 33 ? 0.927 27.041 46.324 1.00 45.13 ? 87 GLU A CD 1 ATOM 293 O OE1 . GLU A 1 33 ? 0.509 26.693 47.475 1.00 47.61 ? 87 GLU A OE1 1 ATOM 294 O OE2 . GLU A 1 33 ? 0.273 27.834 45.578 1.00 47.51 ? 87 GLU A OE2 1 ATOM 295 N N . GLN A 1 34 ? 5.560 28.323 45.730 1.00 25.88 ? 88 GLN A N 1 ATOM 296 C CA . GLN A 1 34 ? 6.579 28.245 46.799 1.00 26.74 ? 88 GLN A CA 1 ATOM 297 C C . GLN A 1 34 ? 6.757 29.554 47.549 1.00 24.53 ? 88 GLN A C 1 ATOM 298 O O . GLN A 1 34 ? 7.044 29.578 48.740 1.00 23.42 ? 88 GLN A O 1 ATOM 299 C CB . GLN A 1 34 ? 7.942 27.818 46.241 1.00 26.27 ? 88 GLN A CB 1 ATOM 300 C CG . GLN A 1 34 ? 7.867 26.483 45.538 1.00 32.53 ? 88 GLN A CG 1 ATOM 301 C CD . GLN A 1 34 ? 7.866 26.723 44.039 1.00 41.38 ? 88 GLN A CD 1 ATOM 302 O OE1 . GLN A 1 34 ? 6.831 27.168 43.424 1.00 36.82 ? 88 GLN A OE1 1 ATOM 303 N NE2 . GLN A 1 34 ? 9.064 26.531 43.439 1.00 43.40 ? 88 GLN A NE2 1 ATOM 304 N N . ASN A 1 35 ? 6.635 30.656 46.827 1.00 23.44 ? 89 ASN A N 1 ATOM 305 C CA . ASN A 1 35 ? 6.780 31.964 47.505 1.00 23.68 ? 89 ASN A CA 1 ATOM 306 C C . ASN A 1 35 ? 5.540 32.338 48.353 1.00 24.88 ? 89 ASN A C 1 ATOM 307 O O . ASN A 1 35 ? 5.671 33.009 49.409 1.00 24.75 ? 89 ASN A O 1 ATOM 308 C CB . ASN A 1 35 ? 7.098 33.064 46.489 1.00 24.25 ? 89 ASN A CB 1 ATOM 309 C CG . ASN A 1 35 ? 7.702 34.312 47.172 1.00 26.19 ? 89 ASN A CG 1 ATOM 310 O OD1 . ASN A 1 35 ? 8.469 34.198 48.157 1.00 23.32 ? 89 ASN A OD1 1 ATOM 311 N ND2 . ASN A 1 35 ? 7.392 35.484 46.641 1.00 25.72 ? 89 ASN A ND2 1 ATOM 312 N N . PHE A 1 36 ? 4.354 31.883 47.926 1.00 22.74 ? 90 PHE A N 1 ATOM 313 C CA . PHE A 1 36 ? 3.130 32.007 48.750 1.00 24.85 ? 90 PHE A CA 1 ATOM 314 C C . PHE A 1 36 ? 3.295 31.158 50.011 1.00 24.93 ? 90 PHE A C 1 ATOM 315 O O . PHE A 1 36 ? 3.020 31.624 51.111 1.00 23.76 ? 90 PHE A O 1 ATOM 316 C CB . PHE A 1 36 ? 1.927 31.570 47.920 1.00 24.99 ? 90 PHE A CB 1 ATOM 317 C CG . PHE A 1 36 ? 0.613 31.503 48.668 1.00 26.33 ? 90 PHE A CG 1 ATOM 318 C CD1 . PHE A 1 36 ? 0.152 32.567 49.449 1.00 28.16 ? 90 PHE A CD1 1 ATOM 319 C CD2 . PHE A 1 36 ? -0.202 30.384 48.524 1.00 33.53 ? 90 PHE A CD2 1 ATOM 320 C CE1 . PHE A 1 36 ? -1.078 32.513 50.100 1.00 28.73 ? 90 PHE A CE1 1 ATOM 321 C CE2 . PHE A 1 36 ? -1.462 30.304 49.205 1.00 37.00 ? 90 PHE A CE2 1 ATOM 322 C CZ . PHE A 1 36 ? -1.885 31.381 49.988 1.00 33.55 ? 90 PHE A CZ 1 ATOM 323 N N A GLN A 1 37 ? 3.786 29.925 49.856 0.60 25.37 ? 91 GLN A N 1 ATOM 324 N N B GLN A 1 37 ? 3.786 29.924 49.830 0.40 25.04 ? 91 GLN A N 1 ATOM 325 C CA A GLN A 1 37 ? 4.022 29.101 51.050 0.60 26.63 ? 91 GLN A CA 1 ATOM 326 C CA B GLN A 1 37 ? 4.092 29.043 50.967 0.40 25.96 ? 91 GLN A CA 1 ATOM 327 C C A GLN A 1 37 ? 5.029 29.743 52.018 0.60 25.70 ? 91 GLN A C 1 ATOM 328 C C B GLN A 1 37 ? 5.032 29.712 51.981 0.40 25.33 ? 91 GLN A C 1 ATOM 329 O O A GLN A 1 37 ? 4.797 29.749 53.240 0.60 24.93 ? 91 GLN A O 1 ATOM 330 O O B GLN A 1 37 ? 4.756 29.704 53.190 0.40 25.00 ? 91 GLN A O 1 ATOM 331 C CB A GLN A 1 37 ? 4.412 27.651 50.681 0.60 26.70 ? 91 GLN A CB 1 ATOM 332 C CB B GLN A 1 37 ? 4.646 27.679 50.488 0.40 25.64 ? 91 GLN A CB 1 ATOM 333 C CG A GLN A 1 37 ? 3.274 26.920 49.914 0.60 31.59 ? 91 GLN A CG 1 ATOM 334 C CG B GLN A 1 37 ? 3.545 26.771 49.905 0.40 28.83 ? 91 GLN A CG 1 ATOM 335 C CD A GLN A 1 37 ? 1.999 26.765 50.725 0.60 34.32 ? 91 GLN A CD 1 ATOM 336 C CD B GLN A 1 37 ? 4.073 25.535 49.193 0.40 28.04 ? 91 GLN A CD 1 ATOM 337 O OE1 A GLN A 1 37 ? 2.032 26.628 51.954 0.60 39.62 ? 91 GLN A OE1 1 ATOM 338 O OE1 B GLN A 1 37 ? 5.244 25.459 48.826 0.40 29.29 ? 91 GLN A OE1 1 ATOM 339 N NE2 A GLN A 1 37 ? 0.863 26.778 50.041 0.60 38.05 ? 91 GLN A NE2 1 ATOM 340 N NE2 B GLN A 1 37 ? 3.189 24.557 48.977 0.40 31.54 ? 91 GLN A NE2 1 ATOM 341 N N . LEU A 1 38 ? 6.120 30.307 51.487 1.00 24.81 ? 92 LEU A N 1 ATOM 342 C CA . LEU A 1 38 ? 7.065 31.030 52.353 1.00 24.14 ? 92 LEU A CA 1 ATOM 343 C C . LEU A 1 38 ? 6.364 32.230 53.037 1.00 23.92 ? 92 LEU A C 1 ATOM 344 O O . LEU A 1 38 ? 6.581 32.474 54.245 1.00 23.56 ? 92 LEU A O 1 ATOM 345 C CB . LEU A 1 38 ? 8.344 31.504 51.592 1.00 23.36 ? 92 LEU A CB 1 ATOM 346 C CG . LEU A 1 38 ? 9.462 32.102 52.464 1.00 23.32 ? 92 LEU A CG 1 ATOM 347 C CD1 . LEU A 1 38 ? 9.945 31.171 53.660 1.00 23.93 ? 92 LEU A CD1 1 ATOM 348 C CD2 . LEU A 1 38 ? 10.627 32.544 51.581 1.00 21.64 ? 92 LEU A CD2 1 ATOM 349 N N . ALA A 1 39 ? 5.538 32.978 52.291 1.00 23.19 ? 93 ALA A N 1 ATOM 350 C CA . ALA A 1 39 ? 4.792 34.106 52.940 1.00 23.44 ? 93 ALA A CA 1 ATOM 351 C C . ALA A 1 39 ? 3.970 33.605 54.121 1.00 23.02 ? 93 ALA A C 1 ATOM 352 O O . ALA A 1 39 ? 3.944 34.229 55.192 1.00 23.15 ? 93 ALA A O 1 ATOM 353 C CB . ALA A 1 39 ? 3.875 34.824 51.943 1.00 22.82 ? 93 ALA A CB 1 ATOM 354 N N . LYS A 1 40 ? 3.291 32.476 53.926 1.00 23.54 ? 94 LYS A N 1 ATOM 355 C CA . LYS A 1 40 ? 2.437 31.949 55.006 1.00 24.83 ? 94 LYS A CA 1 ATOM 356 C C . LYS A 1 40 ? 3.282 31.518 56.217 1.00 24.72 ? 94 LYS A C 1 ATOM 357 O O . LYS A 1 40 ? 2.858 31.705 57.365 1.00 25.61 ? 94 LYS A O 1 ATOM 358 C CB . LYS A 1 40 ? 1.587 30.797 54.451 1.00 24.43 ? 94 LYS A CB 1 ATOM 359 C CG . LYS A 1 40 ? 0.393 31.344 53.623 1.00 27.80 ? 94 LYS A CG 1 ATOM 360 C CD . LYS A 1 40 ? -0.591 30.247 53.263 1.00 37.08 ? 94 LYS A CD 1 ATOM 361 C CE . LYS A 1 40 ? -0.049 29.382 52.160 1.00 40.52 ? 94 LYS A CE 1 ATOM 362 N NZ . LYS A 1 40 ? -1.076 28.362 51.813 1.00 45.50 ? 94 LYS A NZ 1 ATOM 363 N N . GLN A 1 41 ? 4.475 30.945 55.948 1.00 25.13 ? 95 GLN A N 1 ATOM 364 C CA . GLN A 1 41 ? 5.393 30.564 57.033 1.00 25.83 ? 95 GLN A CA 1 ATOM 365 C C . GLN A 1 41 ? 5.833 31.790 57.824 1.00 26.10 ? 95 GLN A C 1 ATOM 366 O O . GLN A 1 41 ? 5.823 31.818 59.055 1.00 25.78 ? 95 GLN A O 1 ATOM 367 C CB . GLN A 1 41 ? 6.610 29.813 56.486 1.00 25.52 ? 95 GLN A CB 1 ATOM 368 C CG . GLN A 1 41 ? 7.688 29.570 57.574 1.00 26.52 ? 95 GLN A CG 1 ATOM 369 C CD . GLN A 1 41 ? 9.005 29.157 56.988 1.00 25.56 ? 95 GLN A CD 1 ATOM 370 O OE1 . GLN A 1 41 ? 9.060 28.430 55.987 1.00 27.46 ? 95 GLN A OE1 1 ATOM 371 N NE2 . GLN A 1 41 ? 10.082 29.582 57.614 1.00 28.46 ? 95 GLN A NE2 1 ATOM 372 N N . ILE A 1 42 ? 6.224 32.827 57.100 1.00 24.19 ? 96 ILE A N 1 ATOM 373 C CA . ILE A 1 42 ? 6.675 34.034 57.753 1.00 25.12 ? 96 ILE A CA 1 ATOM 374 C C . ILE A 1 42 ? 5.574 34.678 58.567 1.00 24.57 ? 96 ILE A C 1 ATOM 375 O O . ILE A 1 42 ? 5.797 35.157 59.692 1.00 24.80 ? 96 ILE A O 1 ATOM 376 C CB . ILE A 1 42 ? 7.247 35.056 56.706 1.00 24.75 ? 96 ILE A CB 1 ATOM 377 C CG1 A ILE A 1 42 ? 8.440 34.501 55.918 0.65 26.71 ? 96 ILE A CG1 1 ATOM 378 C CG1 B ILE A 1 42 ? 8.559 34.467 56.173 0.35 24.28 ? 96 ILE A CG1 1 ATOM 379 C CG2 . ILE A 1 42 ? 7.557 36.430 57.410 1.00 23.30 ? 96 ILE A CG2 1 ATOM 380 C CD1 A ILE A 1 42 ? 9.633 34.314 56.730 0.65 26.28 ? 96 ILE A CD1 1 ATOM 381 C CD1 B ILE A 1 42 ? 9.216 35.220 55.070 0.35 18.30 ? 96 ILE A CD1 1 ATOM 382 N N . GLN A 1 43 ? 4.372 34.704 58.015 1.00 23.76 ? 97 GLN A N 1 ATOM 383 C CA . GLN A 1 43 ? 3.247 35.248 58.767 1.00 24.39 ? 97 GLN A CA 1 ATOM 384 C C . GLN A 1 43 ? 3.051 34.467 60.086 1.00 25.20 ? 97 GLN A C 1 ATOM 385 O O . GLN A 1 43 ? 2.866 35.067 61.164 1.00 26.21 ? 97 GLN A O 1 ATOM 386 C CB . GLN A 1 43 ? 1.995 35.140 57.909 1.00 23.93 ? 97 GLN A CB 1 ATOM 387 C CG . GLN A 1 43 ? 0.711 35.578 58.617 1.00 25.52 ? 97 GLN A CG 1 ATOM 388 C CD . GLN A 1 43 ? -0.578 35.320 57.820 1.00 26.99 ? 97 GLN A CD 1 ATOM 389 O OE1 . GLN A 1 43 ? -0.671 34.408 56.968 1.00 28.25 ? 97 GLN A OE1 1 ATOM 390 N NE2 . GLN A 1 43 ? -1.595 36.101 58.136 1.00 27.34 ? 97 GLN A NE2 1 ATOM 391 N N . SER A 1 44 ? 3.019 33.154 59.977 1.00 25.70 ? 98 SER A N 1 ATOM 392 C CA . SER A 1 44 ? 2.867 32.287 61.176 1.00 26.83 ? 98 SER A CA 1 ATOM 393 C C . SER A 1 44 ? 3.952 32.561 62.229 1.00 26.40 ? 98 SER A C 1 ATOM 394 O O . SER A 1 44 ? 3.655 32.724 63.427 1.00 28.03 ? 98 SER A O 1 ATOM 395 C CB . SER A 1 44 ? 2.944 30.813 60.770 1.00 26.75 ? 98 SER A CB 1 ATOM 396 O OG A SER A 1 44 ? 1.707 30.409 60.241 0.50 29.69 ? 98 SER A OG 1 ATOM 397 O OG B SER A 1 44 ? 2.624 30.023 61.907 0.50 27.76 ? 98 SER A OG 1 ATOM 398 N N . GLN A 1 45 ? 5.208 32.624 61.776 1.00 26.35 ? 99 GLN A N 1 ATOM 399 C CA . GLN A 1 45 ? 6.333 32.808 62.683 1.00 26.20 ? 99 GLN A CA 1 ATOM 400 C C . GLN A 1 45 ? 6.362 34.197 63.290 1.00 26.45 ? 99 GLN A C 1 ATOM 401 O O . GLN A 1 45 ? 6.640 34.344 64.484 1.00 26.76 ? 99 GLN A O 1 ATOM 402 C CB . GLN A 1 45 ? 7.667 32.515 62.000 1.00 25.88 ? 99 GLN A CB 1 ATOM 403 C CG . GLN A 1 45 ? 7.794 31.052 61.594 1.00 29.65 ? 99 GLN A CG 1 ATOM 404 C CD . GLN A 1 45 ? 9.172 30.731 61.004 1.00 32.90 ? 99 GLN A CD 1 ATOM 405 O OE1 . GLN A 1 45 ? 9.539 31.213 59.941 1.00 32.25 ? 99 GLN A OE1 1 ATOM 406 N NE2 . GLN A 1 45 ? 9.918 29.879 61.698 1.00 37.25 ? 99 GLN A NE2 1 ATOM 407 N N . TRP A 1 46 ? 6.081 35.243 62.495 1.00 24.99 ? 100 TRP A N 1 ATOM 408 C CA . TRP A 1 46 ? 5.985 36.544 63.135 1.00 24.82 ? 100 TRP A CA 1 ATOM 409 C C . TRP A 1 46 ? 4.900 36.620 64.222 1.00 25.12 ? 100 TRP A C 1 ATOM 410 O O . TRP A 1 46 ? 5.075 37.334 65.227 1.00 25.78 ? 100 TRP A O 1 ATOM 411 C CB . TRP A 1 46 ? 5.753 37.643 62.091 1.00 23.57 ? 100 TRP A CB 1 ATOM 412 C CG . TRP A 1 46 ? 6.988 37.927 61.268 1.00 22.58 ? 100 TRP A CG 1 ATOM 413 C CD1 . TRP A 1 46 ? 8.214 37.294 61.305 1.00 22.84 ? 100 TRP A CD1 1 ATOM 414 C CD2 . TRP A 1 46 ? 7.075 38.912 60.224 1.00 20.07 ? 100 TRP A CD2 1 ATOM 415 N NE1 . TRP A 1 46 ? 9.060 37.841 60.347 1.00 24.91 ? 100 TRP A NE1 1 ATOM 416 C CE2 . TRP A 1 46 ? 8.386 38.842 59.685 1.00 22.58 ? 100 TRP A CE2 1 ATOM 417 C CE3 . TRP A 1 46 ? 6.167 39.859 59.713 1.00 22.97 ? 100 TRP A CE3 1 ATOM 418 C CZ2 . TRP A 1 46 ? 8.830 39.678 58.634 1.00 24.47 ? 100 TRP A CZ2 1 ATOM 419 C CZ3 . TRP A 1 46 ? 6.598 40.688 58.640 1.00 21.52 ? 100 TRP A CZ3 1 ATOM 420 C CH2 . TRP A 1 46 ? 7.925 40.580 58.122 1.00 22.70 ? 100 TRP A CH2 1 ATOM 421 N N . LYS A 1 47 ? 3.771 35.933 64.028 1.00 26.74 ? 101 LYS A N 1 ATOM 422 C CA . LYS A 1 47 ? 2.751 35.863 65.116 1.00 30.09 ? 101 LYS A CA 1 ATOM 423 C C . LYS A 1 47 ? 3.321 35.133 66.351 1.00 30.70 ? 101 LYS A C 1 ATOM 424 O O . LYS A 1 47 ? 3.205 35.643 67.472 1.00 31.37 ? 101 LYS A O 1 ATOM 425 C CB . LYS A 1 47 ? 1.489 35.142 64.650 1.00 31.63 ? 101 LYS A CB 1 ATOM 426 C CG . LYS A 1 47 ? 0.741 35.860 63.545 1.00 36.01 ? 101 LYS A CG 1 ATOM 427 C CD . LYS A 1 47 ? -0.487 35.058 63.101 1.00 44.69 ? 101 LYS A CD 1 ATOM 428 C CE . LYS A 1 47 ? -1.543 36.007 62.492 1.00 46.74 ? 101 LYS A CE 1 ATOM 429 N NZ . LYS A 1 47 ? -2.533 35.252 61.679 1.00 50.72 ? 101 LYS A NZ 1 ATOM 430 N N . GLU A 1 48 ? 3.965 34.000 66.117 1.00 30.91 ? 102 GLU A N 1 ATOM 431 C CA A GLU A 1 48 ? 4.649 33.154 67.142 0.50 31.76 ? 102 GLU A CA 1 ATOM 432 C CA B GLU A 1 48 ? 4.537 33.238 67.232 0.50 31.93 ? 102 GLU A CA 1 ATOM 433 C C . GLU A 1 48 ? 5.641 34.036 67.920 1.00 31.65 ? 102 GLU A C 1 ATOM 434 O O . GLU A 1 48 ? 5.749 34.001 69.154 1.00 31.56 ? 102 GLU A O 1 ATOM 435 C CB A GLU A 1 48 ? 5.405 31.984 66.459 0.50 32.45 ? 102 GLU A CB 1 ATOM 436 C CB B GLU A 1 48 ? 4.992 31.861 66.779 0.50 32.44 ? 102 GLU A CB 1 ATOM 437 C CG A GLU A 1 48 ? 4.571 30.801 65.854 0.50 34.92 ? 102 GLU A CG 1 ATOM 438 C CG B GLU A 1 48 ? 5.867 31.122 67.788 0.50 36.52 ? 102 GLU A CG 1 ATOM 439 C CD A GLU A 1 48 ? 5.386 29.843 64.906 0.50 37.85 ? 102 GLU A CD 1 ATOM 440 C CD B GLU A 1 48 ? 6.663 30.011 67.138 0.50 42.60 ? 102 GLU A CD 1 ATOM 441 O OE1 A GLU A 1 48 ? 6.625 29.688 65.076 0.50 36.35 ? 102 GLU A OE1 1 ATOM 442 O OE1 B GLU A 1 48 ? 6.139 29.410 66.170 0.50 46.10 ? 102 GLU A OE1 1 ATOM 443 O OE2 A GLU A 1 48 ? 4.790 29.239 63.972 0.50 37.38 ? 102 GLU A OE2 1 ATOM 444 O OE2 B GLU A 1 48 ? 7.811 29.737 67.578 0.50 45.09 ? 102 GLU A OE2 1 ATOM 445 N N . PHE A 1 49 ? 6.383 34.850 67.160 1.00 30.60 ? 103 PHE A N 1 ATOM 446 C CA . PHE A 1 49 ? 7.421 35.749 67.713 1.00 30.31 ? 103 PHE A CA 1 ATOM 447 C C . PHE A 1 49 ? 6.867 36.835 68.616 1.00 30.05 ? 103 PHE A C 1 ATOM 448 O O . PHE A 1 49 ? 7.613 37.434 69.374 1.00 30.93 ? 103 PHE A O 1 ATOM 449 C CB . PHE A 1 49 ? 8.243 36.432 66.575 1.00 29.87 ? 103 PHE A CB 1 ATOM 450 C CG . PHE A 1 49 ? 9.164 35.506 65.811 1.00 31.09 ? 103 PHE A CG 1 ATOM 451 C CD1 . PHE A 1 49 ? 9.481 34.218 66.288 1.00 32.24 ? 103 PHE A CD1 1 ATOM 452 C CD2 . PHE A 1 49 ? 9.755 35.946 64.614 1.00 26.58 ? 103 PHE A CD2 1 ATOM 453 C CE1 . PHE A 1 49 ? 10.341 33.364 65.560 1.00 34.48 ? 103 PHE A CE1 1 ATOM 454 C CE2 . PHE A 1 49 ? 10.614 35.106 63.882 1.00 29.52 ? 103 PHE A CE2 1 ATOM 455 C CZ . PHE A 1 49 ? 10.910 33.810 64.351 1.00 33.35 ? 103 PHE A CZ 1 ATOM 456 N N . GLY A 1 50 ? 5.576 37.129 68.484 1.00 27.91 ? 104 GLY A N 1 ATOM 457 C CA . GLY A 1 50 ? 4.887 38.025 69.380 1.00 29.38 ? 104 GLY A CA 1 ATOM 458 C C . GLY A 1 50 ? 4.303 39.305 68.807 1.00 28.51 ? 104 GLY A C 1 ATOM 459 O O . GLY A 1 50 ? 3.858 40.147 69.577 1.00 29.52 ? 104 GLY A O 1 ATOM 460 N N . LEU A 1 51 ? 4.332 39.499 67.472 1.00 27.15 ? 105 LEU A N 1 ATOM 461 C CA . LEU A 1 51 ? 3.683 40.712 66.890 1.00 25.90 ? 105 LEU A CA 1 ATOM 462 C C . LEU A 1 51 ? 2.170 40.761 67.160 1.00 28.42 ? 105 LEU A C 1 ATOM 463 O O . LEU A 1 51 ? 1.493 39.698 67.253 1.00 29.15 ? 105 LEU A O 1 ATOM 464 C CB . LEU A 1 51 ? 3.955 40.805 65.362 1.00 24.64 ? 105 LEU A CB 1 ATOM 465 C CG . LEU A 1 51 ? 5.433 40.924 64.998 1.00 23.20 ? 105 LEU A CG 1 ATOM 466 C CD1 . LEU A 1 51 ? 5.511 41.298 63.499 1.00 25.18 ? 105 LEU A CD1 1 ATOM 467 C CD2 . LEU A 1 51 ? 6.148 42.013 65.865 1.00 25.87 ? 105 LEU A CD2 1 ATOM 468 N N . ASP A 1 52 ? 1.633 41.975 67.309 1.00 28.07 ? 106 ASP A N 1 ATOM 469 C CA . ASP A 1 52 ? 0.204 42.151 67.593 1.00 30.73 ? 106 ASP A CA 1 ATOM 470 C C . ASP A 1 52 ? -0.726 41.667 66.484 1.00 31.85 ? 106 ASP A C 1 ATOM 471 O O . ASP A 1 52 ? -1.782 41.067 66.748 1.00 32.36 ? 106 ASP A O 1 ATOM 472 C CB . ASP A 1 52 ? -0.104 43.619 67.928 1.00 29.74 ? 106 ASP A CB 1 ATOM 473 C CG . ASP A 1 52 ? 0.610 44.072 69.146 1.00 32.43 ? 106 ASP A CG 1 ATOM 474 O OD1 . ASP A 1 52 ? 0.345 43.484 70.215 1.00 32.79 ? 106 ASP A OD1 1 ATOM 475 O OD2 . ASP A 1 52 ? 1.433 45.000 69.072 1.00 29.92 ? 106 ASP A OD2 1 ATOM 476 N N . SER A 1 53 ? -0.356 41.936 65.233 1.00 30.73 ? 107 SER A N 1 ATOM 477 C CA . SER A 1 53 ? -1.160 41.445 64.101 1.00 29.87 ? 107 SER A CA 1 ATOM 478 C C . SER A 1 53 ? -0.183 41.157 62.985 1.00 28.52 ? 107 SER A C 1 ATOM 479 O O . SER A 1 53 ? 0.865 41.824 62.880 1.00 25.48 ? 107 SER A O 1 ATOM 480 C CB . SER A 1 53 ? -2.193 42.516 63.656 1.00 31.14 ? 107 SER A CB 1 ATOM 481 O OG A SER A 1 53 ? -1.560 43.774 63.553 0.50 32.44 ? 107 SER A OG 1 ATOM 482 O OG B SER A 1 53 ? -1.610 43.468 62.793 0.50 31.96 ? 107 SER A OG 1 ATOM 483 N N . VAL A 1 54 ? -0.499 40.151 62.172 1.00 27.12 ? 108 VAL A N 1 ATOM 484 C CA . VAL A 1 54 ? 0.321 39.846 61.020 1.00 27.07 ? 108 VAL A CA 1 ATOM 485 C C . VAL A 1 54 ? -0.613 39.410 59.889 1.00 27.47 ? 108 VAL A C 1 ATOM 486 O O . VAL A 1 54 ? -1.284 38.353 59.987 1.00 27.55 ? 108 VAL A O 1 ATOM 487 C CB . VAL A 1 54 ? 1.413 38.723 61.246 1.00 26.25 ? 108 VAL A CB 1 ATOM 488 C CG1 . VAL A 1 54 ? 2.315 38.651 60.021 1.00 27.41 ? 108 VAL A CG1 1 ATOM 489 C CG2 . VAL A 1 54 ? 2.269 38.974 62.527 1.00 27.73 ? 108 VAL A CG2 1 ATOM 490 N N . GLU A 1 55 ? -0.639 40.206 58.809 1.00 25.81 ? 109 GLU A N 1 ATOM 491 C CA . GLU A 1 55 ? -1.601 39.969 57.736 1.00 28.06 ? 109 GLU A CA 1 ATOM 492 C C . GLU A 1 55 ? -0.888 39.794 56.412 1.00 26.06 ? 109 GLU A C 1 ATOM 493 O O . GLU A 1 55 ? 0.248 40.297 56.236 1.00 25.94 ? 109 GLU A O 1 ATOM 494 C CB . GLU A 1 55 ? -2.572 41.164 57.634 1.00 29.70 ? 109 GLU A CB 1 ATOM 495 C CG . GLU A 1 55 ? -3.552 41.305 58.831 1.00 38.47 ? 109 GLU A CG 1 ATOM 496 C CD . GLU A 1 55 ? -4.327 40.018 59.216 1.00 47.27 ? 109 GLU A CD 1 ATOM 497 O OE1 . GLU A 1 55 ? -4.744 39.211 58.338 1.00 48.55 ? 109 GLU A OE1 1 ATOM 498 O OE2 . GLU A 1 55 ? -4.530 39.827 60.444 1.00 53.71 ? 109 GLU A OE2 1 ATOM 499 N N . LEU A 1 56 ? -1.518 39.095 55.473 1.00 24.98 ? 110 LEU A N 1 ATOM 500 C CA . LEU A 1 56 ? -1.048 39.152 54.096 1.00 24.91 ? 110 LEU A CA 1 ATOM 501 C C . LEU A 1 56 ? -1.825 40.226 53.310 1.00 25.59 ? 110 LEU A C 1 ATOM 502 O O . LEU A 1 56 ? -3.067 40.304 53.417 1.00 25.37 ? 110 LEU A O 1 ATOM 503 C CB . LEU A 1 56 ? -1.219 37.807 53.384 1.00 26.16 ? 110 LEU A CB 1 ATOM 504 C CG . LEU A 1 56 ? -0.490 36.587 53.957 1.00 28.22 ? 110 LEU A CG 1 ATOM 505 C CD1 . LEU A 1 56 ? -0.755 35.435 53.002 1.00 29.95 ? 110 LEU A CD1 1 ATOM 506 C CD2 . LEU A 1 56 ? 0.985 36.760 54.151 1.00 26.82 ? 110 LEU A CD2 1 ATOM 507 N N . ALA A 1 57 ? -1.118 41.068 52.569 1.00 22.37 ? 111 ALA A N 1 ATOM 508 C CA . ALA A 1 57 ? -1.771 42.027 51.705 1.00 22.87 ? 111 ALA A CA 1 ATOM 509 C C . ALA A 1 57 ? -1.416 41.548 50.304 1.00 23.11 ? 111 ALA A C 1 ATOM 510 O O . ALA A 1 57 ? -0.219 41.558 49.927 1.00 23.23 ? 111 ALA A O 1 ATOM 511 C CB . ALA A 1 57 ? -1.221 43.467 51.945 1.00 23.04 ? 111 ALA A CB 1 ATOM 512 N N . HIS A 1 58 ? -2.428 41.144 49.551 1.00 21.88 ? 112 HIS A N 1 ATOM 513 C CA . HIS A 1 58 ? -2.190 40.613 48.194 1.00 21.32 ? 112 HIS A CA 1 ATOM 514 C C . HIS A 1 58 ? -2.673 41.568 47.120 1.00 20.79 ? 112 HIS A C 1 ATOM 515 O O . HIS A 1 58 ? -3.580 42.414 47.377 1.00 21.16 ? 112 HIS A O 1 ATOM 516 C CB . HIS A 1 58 ? -2.849 39.242 48.043 1.00 22.35 ? 112 HIS A CB 1 ATOM 517 C CG . HIS A 1 58 ? -4.352 39.279 48.044 1.00 24.42 ? 112 HIS A CG 1 ATOM 518 N ND1 . HIS A 1 58 ? -5.107 39.066 49.190 1.00 29.03 ? 112 HIS A ND1 1 ATOM 519 C CD2 . HIS A 1 58 ? -5.239 39.519 47.049 1.00 27.90 ? 112 HIS A CD2 1 ATOM 520 C CE1 . HIS A 1 58 ? -6.393 39.147 48.884 1.00 29.97 ? 112 HIS A CE1 1 ATOM 521 N NE2 . HIS A 1 58 ? -6.502 39.429 47.596 1.00 29.52 ? 112 HIS A NE2 1 ATOM 522 N N . TYR A 1 59 ? -2.056 41.470 45.937 1.00 20.54 ? 113 TYR A N 1 ATOM 523 C CA . TYR A 1 59 ? -2.376 42.306 44.768 1.00 20.11 ? 113 TYR A CA 1 ATOM 524 C C . TYR A 1 59 ? -2.237 41.403 43.560 1.00 20.06 ? 113 TYR A C 1 ATOM 525 O O . TYR A 1 59 ? -1.522 40.393 43.613 1.00 20.65 ? 113 TYR A O 1 ATOM 526 C CB . TYR A 1 59 ? -1.388 43.500 44.610 1.00 19.54 ? 113 TYR A CB 1 ATOM 527 C CG . TYR A 1 59 ? -1.383 44.310 45.887 1.00 18.89 ? 113 TYR A CG 1 ATOM 528 C CD1 . TYR A 1 59 ? -2.390 45.259 46.126 1.00 18.85 ? 113 TYR A CD1 1 ATOM 529 C CD2 . TYR A 1 59 ? -0.444 44.042 46.881 1.00 18.71 ? 113 TYR A CD2 1 ATOM 530 C CE1 . TYR A 1 59 ? -2.440 45.986 47.391 1.00 19.79 ? 113 TYR A CE1 1 ATOM 531 C CE2 . TYR A 1 59 ? -0.476 44.721 48.096 1.00 20.42 ? 113 TYR A CE2 1 ATOM 532 C CZ . TYR A 1 59 ? -1.486 45.669 48.347 1.00 21.61 ? 113 TYR A CZ 1 ATOM 533 O OH . TYR A 1 59 ? -1.513 46.327 49.565 1.00 21.67 ? 113 TYR A OH 1 ATOM 534 N N . ASP A 1 60 ? -2.828 41.820 42.461 1.00 19.58 ? 114 ASP A N 1 ATOM 535 C CA . ASP A 1 60 ? -2.723 41.059 41.205 1.00 21.24 ? 114 ASP A CA 1 ATOM 536 C C . ASP A 1 60 ? -2.061 41.965 40.210 1.00 20.38 ? 114 ASP A C 1 ATOM 537 O O . ASP A 1 60 ? -2.703 42.913 39.739 1.00 20.70 ? 114 ASP A O 1 ATOM 538 C CB . ASP A 1 60 ? -4.139 40.679 40.707 1.00 22.31 ? 114 ASP A CB 1 ATOM 539 C CG . ASP A 1 60 ? -4.814 39.701 41.657 1.00 27.14 ? 114 ASP A CG 1 ATOM 540 O OD1 . ASP A 1 60 ? -4.154 38.698 41.989 1.00 25.42 ? 114 ASP A OD1 1 ATOM 541 O OD2 . ASP A 1 60 ? -5.946 39.977 42.127 1.00 28.73 ? 114 ASP A OD2 1 ATOM 542 N N . VAL A 1 61 ? -0.790 41.652 39.921 1.00 19.46 ? 115 VAL A N 1 ATOM 543 C CA . VAL A 1 61 ? 0.105 42.548 39.168 1.00 20.23 ? 115 VAL A CA 1 ATOM 544 C C . VAL A 1 61 ? 0.639 41.849 37.909 1.00 20.14 ? 115 VAL A C 1 ATOM 545 O O . VAL A 1 61 ? 0.682 40.616 37.849 1.00 23.28 ? 115 VAL A O 1 ATOM 546 C CB . VAL A 1 61 ? 1.276 43.082 40.049 1.00 20.14 ? 115 VAL A CB 1 ATOM 547 C CG1 . VAL A 1 61 ? 0.745 43.826 41.264 1.00 19.76 ? 115 VAL A CG1 1 ATOM 548 C CG2 . VAL A 1 61 ? 2.231 41.936 40.513 1.00 17.91 ? 115 VAL A CG2 1 ATOM 549 N N . LEU A 1 62 ? 1.130 42.637 36.957 1.00 19.90 ? 116 LEU A N 1 ATOM 550 C CA . LEU A 1 62 ? 1.729 42.056 35.761 1.00 20.22 ? 116 LEU A CA 1 ATOM 551 C C . LEU A 1 62 ? 3.107 41.474 36.083 1.00 20.14 ? 116 LEU A C 1 ATOM 552 O O . LEU A 1 62 ? 3.964 42.221 36.500 1.00 23.09 ? 116 LEU A O 1 ATOM 553 C CB . LEU A 1 62 ? 1.871 43.114 34.655 1.00 17.79 ? 116 LEU A CB 1 ATOM 554 C CG . LEU A 1 62 ? 2.219 42.413 33.301 1.00 20.03 ? 116 LEU A CG 1 ATOM 555 C CD1 . LEU A 1 62 ? 0.928 41.734 32.801 1.00 22.29 ? 116 LEU A CD1 1 ATOM 556 C CD2 . LEU A 1 62 ? 2.570 43.592 32.388 1.00 21.32 ? 116 LEU A CD2 1 ATOM 557 N N . LEU A 1 63 ? 3.307 40.173 35.856 1.00 20.07 ? 117 LEU A N 1 ATOM 558 C CA . LEU A 1 63 ? 4.637 39.508 36.014 1.00 20.72 ? 117 LEU A CA 1 ATOM 559 C C . LEU A 1 63 ? 4.973 38.909 34.646 1.00 22.19 ? 117 LEU A C 1 ATOM 560 O O . LEU A 1 63 ? 4.210 39.104 33.720 1.00 23.04 ? 117 LEU A O 1 ATOM 561 C CB . LEU A 1 63 ? 4.593 38.403 37.092 1.00 20.03 ? 117 LEU A CB 1 ATOM 562 C CG . LEU A 1 63 ? 4.272 38.916 38.528 1.00 19.40 ? 117 LEU A CG 1 ATOM 563 C CD1 . LEU A 1 63 ? 4.388 37.770 39.588 1.00 19.57 ? 117 LEU A CD1 1 ATOM 564 C CD2 . LEU A 1 63 ? 5.154 40.164 39.002 1.00 18.01 ? 117 LEU A CD2 1 ATOM 565 N N . SER A 1 64 ? 6.127 38.234 34.538 1.00 22.45 ? 118 SER A N 1 ATOM 566 C CA . SER A 1 64 ? 6.671 37.805 33.263 1.00 23.77 ? 118 SER A CA 1 ATOM 567 C C . SER A 1 64 ? 7.465 36.533 33.508 1.00 23.71 ? 118 SER A C 1 ATOM 568 O O . SER A 1 64 ? 8.304 36.478 34.442 1.00 24.44 ? 118 SER A O 1 ATOM 569 C CB . SER A 1 64 ? 7.630 38.895 32.715 1.00 24.65 ? 118 SER A CB 1 ATOM 570 O OG . SER A 1 64 ? 8.504 38.400 31.710 1.00 26.24 ? 118 SER A OG 1 ATOM 571 N N . TYR A 1 65 ? 7.251 35.520 32.656 1.00 23.91 ? 119 TYR A N 1 ATOM 572 C CA . TYR A 1 65 ? 7.933 34.263 32.853 1.00 23.82 ? 119 TYR A CA 1 ATOM 573 C C . TYR A 1 65 ? 8.258 33.648 31.480 1.00 26.06 ? 119 TYR A C 1 ATOM 574 O O . TYR A 1 65 ? 7.508 33.840 30.525 1.00 26.29 ? 119 TYR A O 1 ATOM 575 C CB . TYR A 1 65 ? 6.987 33.274 33.521 1.00 24.91 ? 119 TYR A CB 1 ATOM 576 C CG . TYR A 1 65 ? 6.444 33.677 34.878 1.00 24.77 ? 119 TYR A CG 1 ATOM 577 C CD1 . TYR A 1 65 ? 7.236 33.554 36.031 1.00 25.42 ? 119 TYR A CD1 1 ATOM 578 C CD2 . TYR A 1 65 ? 5.115 34.102 35.013 1.00 26.54 ? 119 TYR A CD2 1 ATOM 579 C CE1 . TYR A 1 65 ? 6.719 33.895 37.313 1.00 23.01 ? 119 TYR A CE1 1 ATOM 580 C CE2 . TYR A 1 65 ? 4.584 34.428 36.274 1.00 26.94 ? 119 TYR A CE2 1 ATOM 581 C CZ . TYR A 1 65 ? 5.392 34.306 37.405 1.00 27.36 ? 119 TYR A CZ 1 ATOM 582 O OH . TYR A 1 65 ? 4.887 34.584 38.634 1.00 26.88 ? 119 TYR A OH 1 ATOM 583 N N . PRO A 1 66 ? 9.340 32.884 31.429 1.00 27.11 ? 120 PRO A N 1 ATOM 584 C CA . PRO A 1 66 ? 9.618 32.103 30.203 1.00 28.92 ? 120 PRO A CA 1 ATOM 585 C C . PRO A 1 66 ? 8.535 31.051 29.955 1.00 32.26 ? 120 PRO A C 1 ATOM 586 O O . PRO A 1 66 ? 7.841 30.614 30.887 1.00 30.64 ? 120 PRO A O 1 ATOM 587 C CB . PRO A 1 66 ? 10.938 31.399 30.529 1.00 28.69 ? 120 PRO A CB 1 ATOM 588 C CG . PRO A 1 66 ? 11.593 32.203 31.634 1.00 28.13 ? 120 PRO A CG 1 ATOM 589 C CD . PRO A 1 66 ? 10.437 32.799 32.423 1.00 25.43 ? 120 PRO A CD 1 ATOM 590 N N . ASN A 1 67 ? 8.407 30.631 28.694 1.00 34.44 ? 121 ASN A N 1 ATOM 591 C CA . ASN A 1 67 ? 7.469 29.577 28.373 1.00 38.76 ? 121 ASN A CA 1 ATOM 592 C C . ASN A 1 67 ? 8.221 28.254 28.613 1.00 40.45 ? 121 ASN A C 1 ATOM 593 O O . ASN A 1 67 ? 9.283 28.012 28.021 1.00 40.69 ? 121 ASN A O 1 ATOM 594 C CB . ASN A 1 67 ? 7.021 29.753 26.930 1.00 39.21 ? 121 ASN A CB 1 ATOM 595 C CG . ASN A 1 67 ? 6.007 28.705 26.489 1.00 43.11 ? 121 ASN A CG 1 ATOM 596 O OD1 . ASN A 1 67 ? 6.027 27.556 26.939 1.00 46.14 ? 121 ASN A OD1 1 ATOM 597 N ND2 . ASN A 1 67 ? 5.126 29.097 25.609 1.00 49.46 ? 121 ASN A ND2 1 ATOM 598 N N . LYS A 1 68 ? 7.706 27.442 29.533 1.00 43.15 ? 122 LYS A N 1 ATOM 599 C CA . LYS A 1 68 ? 8.356 26.183 29.935 1.00 46.18 ? 122 LYS A CA 1 ATOM 600 C C . LYS A 1 68 ? 8.561 25.164 28.794 1.00 47.31 ? 122 LYS A C 1 ATOM 601 O O . LYS A 1 68 ? 9.516 24.391 28.828 1.00 47.28 ? 122 LYS A O 1 ATOM 602 C CB . LYS A 1 68 ? 7.580 25.503 31.070 1.00 46.95 ? 122 LYS A CB 1 ATOM 603 C CG . LYS A 1 68 ? 7.785 26.107 32.454 1.00 50.70 ? 122 LYS A CG 1 ATOM 604 C CD . LYS A 1 68 ? 6.541 25.859 33.347 1.00 57.22 ? 122 LYS A CD 1 ATOM 605 C CE . LYS A 1 68 ? 6.409 26.927 34.467 1.00 59.27 ? 122 LYS A CE 1 ATOM 606 N NZ . LYS A 1 68 ? 5.014 26.997 35.010 1.00 61.86 ? 122 LYS A NZ 1 ATOM 607 N N . THR A 1 69 ? 7.677 25.178 27.800 1.00 48.22 ? 123 THR A N 1 ATOM 608 C CA . THR A 1 69 ? 7.744 24.211 26.688 1.00 49.85 ? 123 THR A CA 1 ATOM 609 C C . THR A 1 69 ? 8.270 24.843 25.387 1.00 50.41 ? 123 THR A C 1 ATOM 610 O O . THR A 1 69 ? 8.242 24.223 24.317 1.00 52.01 ? 123 THR A O 1 ATOM 611 C CB . THR A 1 69 ? 6.363 23.517 26.438 1.00 50.24 ? 123 THR A CB 1 ATOM 612 O OG1 . THR A 1 69 ? 5.411 24.488 25.998 1.00 50.67 ? 123 THR A OG1 1 ATOM 613 C CG2 . THR A 1 69 ? 5.833 22.843 27.712 1.00 49.89 ? 123 THR A CG2 1 ATOM 614 N N . HIS A 1 70 ? 8.767 26.068 25.483 1.00 49.60 ? 124 HIS A N 1 ATOM 615 C CA . HIS A 1 70 ? 9.229 26.811 24.318 1.00 49.38 ? 124 HIS A CA 1 ATOM 616 C C . HIS A 1 70 ? 10.386 27.744 24.750 1.00 47.55 ? 124 HIS A C 1 ATOM 617 O O . HIS A 1 70 ? 10.211 28.965 24.861 1.00 46.66 ? 124 HIS A O 1 ATOM 618 C CB . HIS A 1 70 ? 8.044 27.571 23.711 1.00 50.61 ? 124 HIS A CB 1 ATOM 619 C CG . HIS A 1 70 ? 8.260 28.054 22.307 1.00 55.14 ? 124 HIS A CG 1 ATOM 620 N ND1 . HIS A 1 70 ? 7.365 28.890 21.667 1.00 58.91 ? 124 HIS A ND1 1 ATOM 621 C CD2 . HIS A 1 70 ? 9.258 27.824 21.419 1.00 60.03 ? 124 HIS A CD2 1 ATOM 622 C CE1 . HIS A 1 70 ? 7.802 29.152 20.447 1.00 60.74 ? 124 HIS A CE1 1 ATOM 623 N NE2 . HIS A 1 70 ? 8.948 28.517 20.270 1.00 62.07 ? 124 HIS A NE2 1 ATOM 624 N N . PRO A 1 71 ? 11.575 27.160 25.015 1.00 46.20 ? 125 PRO A N 1 ATOM 625 C CA . PRO A 1 71 ? 12.677 27.921 25.650 1.00 44.07 ? 125 PRO A CA 1 ATOM 626 C C . PRO A 1 71 ? 13.259 29.087 24.843 1.00 42.50 ? 125 PRO A C 1 ATOM 627 O O . PRO A 1 71 ? 13.296 29.054 23.614 1.00 42.20 ? 125 PRO A O 1 ATOM 628 C CB . PRO A 1 71 ? 13.752 26.853 25.917 1.00 44.70 ? 125 PRO A CB 1 ATOM 629 C CG . PRO A 1 71 ? 13.029 25.523 25.822 1.00 46.35 ? 125 PRO A CG 1 ATOM 630 C CD . PRO A 1 71 ? 11.928 25.737 24.828 1.00 46.79 ? 125 PRO A CD 1 ATOM 631 N N . ASN A 1 72 ? 13.681 30.132 25.558 1.00 38.54 ? 126 ASN A N 1 ATOM 632 C CA . ASN A 1 72 ? 14.378 31.267 24.974 1.00 37.48 ? 126 ASN A CA 1 ATOM 633 C C . ASN A 1 72 ? 15.824 30.883 24.697 1.00 36.89 ? 126 ASN A C 1 ATOM 634 O O . ASN A 1 72 ? 16.436 30.151 25.492 1.00 35.31 ? 126 ASN A O 1 ATOM 635 C CB . ASN A 1 72 ? 14.375 32.499 25.923 1.00 36.05 ? 126 ASN A CB 1 ATOM 636 C CG . ASN A 1 72 ? 12.976 32.931 26.306 1.00 36.83 ? 126 ASN A CG 1 ATOM 637 O OD1 . ASN A 1 72 ? 12.066 32.903 25.469 1.00 34.21 ? 126 ASN A OD1 1 ATOM 638 N ND2 . ASN A 1 72 ? 12.788 33.337 27.595 1.00 33.20 ? 126 ASN A ND2 1 ATOM 639 N N . TYR A 1 73 ? 16.331 31.347 23.553 1.00 37.37 ? 127 TYR A N 1 ATOM 640 C CA . TYR A 1 73 ? 17.777 31.228 23.220 1.00 38.59 ? 127 TYR A CA 1 ATOM 641 C C . TYR A 1 73 ? 18.176 32.169 22.088 1.00 39.12 ? 127 TYR A C 1 ATOM 642 O O . TYR A 1 73 ? 17.309 32.812 21.477 1.00 39.39 ? 127 TYR A O 1 ATOM 643 C CB . TYR A 1 73 ? 18.167 29.785 22.918 1.00 39.41 ? 127 TYR A CB 1 ATOM 644 C CG . TYR A 1 73 ? 17.603 29.218 21.630 1.00 41.54 ? 127 TYR A CG 1 ATOM 645 C CD1 . TYR A 1 73 ? 18.437 28.988 20.531 1.00 45.88 ? 127 TYR A CD1 1 ATOM 646 C CD2 . TYR A 1 73 ? 16.251 28.873 21.518 1.00 42.37 ? 127 TYR A CD2 1 ATOM 647 C CE1 . TYR A 1 73 ? 17.935 28.435 19.333 1.00 45.43 ? 127 TYR A CE1 1 ATOM 648 C CE2 . TYR A 1 73 ? 15.738 28.318 20.334 1.00 46.81 ? 127 TYR A CE2 1 ATOM 649 C CZ . TYR A 1 73 ? 16.596 28.099 19.251 1.00 46.60 ? 127 TYR A CZ 1 ATOM 650 O OH . TYR A 1 73 ? 16.087 27.560 18.085 1.00 48.15 ? 127 TYR A OH 1 ATOM 651 N N . ILE A 1 74 ? 19.488 32.283 21.852 1.00 38.90 ? 128 ILE A N 1 ATOM 652 C CA . ILE A 1 74 ? 20.032 33.116 20.791 1.00 39.07 ? 128 ILE A CA 1 ATOM 653 C C . ILE A 1 74 ? 20.873 32.182 19.880 1.00 40.51 ? 128 ILE A C 1 ATOM 654 O O . ILE A 1 74 ? 21.520 31.243 20.369 1.00 38.41 ? 128 ILE A O 1 ATOM 655 C CB . ILE A 1 74 ? 20.913 34.265 21.334 1.00 39.29 ? 128 ILE A CB 1 ATOM 656 C CG1 . ILE A 1 74 ? 20.090 35.269 22.183 1.00 36.89 ? 128 ILE A CG1 1 ATOM 657 C CG2 . ILE A 1 74 ? 21.579 35.058 20.214 1.00 39.52 ? 128 ILE A CG2 1 ATOM 658 C CD1 . ILE A 1 74 ? 20.942 36.058 23.175 1.00 37.95 ? 128 ILE A CD1 1 ATOM 659 N N . SER A 1 75 ? 20.817 32.458 18.579 1.00 42.33 ? 129 SER A N 1 ATOM 660 C CA . SER A 1 75 ? 21.559 31.681 17.551 1.00 44.63 ? 129 SER A CA 1 ATOM 661 C C . SER A 1 75 ? 22.471 32.545 16.712 1.00 45.96 ? 129 SER A C 1 ATOM 662 O O . SER A 1 75 ? 22.185 33.726 16.497 1.00 45.20 ? 129 SER A O 1 ATOM 663 C CB . SER A 1 75 ? 20.573 31.010 16.607 1.00 44.48 ? 129 SER A CB 1 ATOM 664 O OG . SER A 1 75 ? 19.922 29.946 17.270 1.00 46.45 ? 129 SER A OG 1 ATOM 665 N N . ILE A 1 76 ? 23.577 31.957 16.235 1.00 48.03 ? 130 ILE A N 1 ATOM 666 C CA . ILE A 1 76 ? 24.174 32.448 14.987 1.00 50.27 ? 130 ILE A CA 1 ATOM 667 C C . ILE A 1 76 ? 23.601 31.558 13.883 1.00 51.33 ? 130 ILE A C 1 ATOM 668 O O . ILE A 1 76 ? 23.612 30.333 13.995 1.00 51.17 ? 130 ILE A O 1 ATOM 669 C CB . ILE A 1 76 ? 25.728 32.397 14.951 1.00 50.81 ? 130 ILE A CB 1 ATOM 670 C CG1 . ILE A 1 76 ? 26.333 33.311 16.019 1.00 49.17 ? 130 ILE A CG1 1 ATOM 671 C CG2 . ILE A 1 76 ? 26.238 32.798 13.552 1.00 51.69 ? 130 ILE A CG2 1 ATOM 672 C CD1 . ILE A 1 76 ? 27.742 32.927 16.426 1.00 48.30 ? 130 ILE A CD1 1 ATOM 673 N N . ILE A 1 77 ? 23.066 32.198 12.847 1.00 53.27 ? 131 ILE A N 1 ATOM 674 C CA . ILE A 1 77 ? 22.502 31.503 11.679 1.00 55.15 ? 131 ILE A CA 1 ATOM 675 C C . ILE A 1 77 ? 23.429 31.714 10.464 1.00 55.86 ? 131 ILE A C 1 ATOM 676 O O . ILE A 1 77 ? 23.919 32.840 10.244 1.00 56.34 ? 131 ILE A O 1 ATOM 677 C CB . ILE A 1 77 ? 21.057 32.018 11.330 1.00 55.39 ? 131 ILE A CB 1 ATOM 678 C CG1 . ILE A 1 77 ? 20.955 33.540 11.511 1.00 56.36 ? 131 ILE A CG1 1 ATOM 679 C CG2 . ILE A 1 77 ? 19.994 31.319 12.154 1.00 54.48 ? 131 ILE A CG2 1 ATOM 680 C CD1 . ILE A 1 77 ? 19.929 34.190 10.591 1.00 58.59 ? 131 ILE A CD1 1 ATOM 681 N N . ASN A 1 82 ? 20.411 27.939 8.732 1.00 61.20 ? 136 ASN A N 1 ATOM 682 C CA . ASN A 1 82 ? 21.078 26.958 9.597 1.00 61.08 ? 136 ASN A CA 1 ATOM 683 C C . ASN A 1 82 ? 21.615 27.611 10.870 1.00 59.32 ? 136 ASN A C 1 ATOM 684 O O . ASN A 1 82 ? 22.402 28.578 10.795 1.00 59.56 ? 136 ASN A O 1 ATOM 685 C CB . ASN A 1 82 ? 22.241 26.277 8.868 1.00 62.06 ? 136 ASN A CB 1 ATOM 686 C CG . ASN A 1 82 ? 21.783 25.361 7.749 1.00 65.35 ? 136 ASN A CG 1 ATOM 687 O OD1 . ASN A 1 82 ? 20.823 24.591 7.894 1.00 67.44 ? 136 ASN A OD1 1 ATOM 688 N ND2 . ASN A 1 82 ? 22.484 25.425 6.622 1.00 67.48 ? 136 ASN A ND2 1 ATOM 689 N N . GLU A 1 83 ? 21.197 27.070 12.020 1.00 57.01 ? 137 GLU A N 1 ATOM 690 C CA . GLU A 1 83 ? 21.623 27.585 13.333 1.00 54.89 ? 137 GLU A CA 1 ATOM 691 C C . GLU A 1 83 ? 22.856 26.843 13.821 1.00 53.59 ? 137 GLU A C 1 ATOM 692 O O . GLU A 1 83 ? 22.766 25.716 14.297 1.00 52.21 ? 137 GLU A O 1 ATOM 693 C CB . GLU A 1 83 ? 20.477 27.525 14.372 1.00 54.31 ? 137 GLU A CB 1 ATOM 694 C CG . GLU A 1 83 ? 19.260 28.364 13.977 1.00 54.52 ? 137 GLU A CG 1 ATOM 695 C CD . GLU A 1 83 ? 18.189 28.521 15.075 1.00 54.29 ? 137 GLU A CD 1 ATOM 696 O OE1 . GLU A 1 83 ? 18.083 27.669 15.989 1.00 53.70 ? 137 GLU A OE1 1 ATOM 697 O OE2 . GLU A 1 83 ? 17.427 29.502 14.973 1.00 53.83 ? 137 GLU A OE2 1 ATOM 698 N N . ILE A 1 84 ? 24.000 27.517 13.722 1.00 53.21 ? 138 ILE A N 1 ATOM 699 C CA . ILE A 1 84 ? 25.323 26.896 13.903 1.00 53.06 ? 138 ILE A CA 1 ATOM 700 C C . ILE A 1 84 ? 25.888 27.039 15.316 1.00 51.83 ? 138 ILE A C 1 ATOM 701 O O . ILE A 1 84 ? 26.823 26.329 15.713 1.00 51.63 ? 138 ILE A O 1 ATOM 702 C CB . ILE A 1 84 ? 26.339 27.394 12.826 1.00 53.84 ? 138 ILE A CB 1 ATOM 703 C CG1 . ILE A 1 84 ? 26.630 28.891 12.989 1.00 54.17 ? 138 ILE A CG1 1 ATOM 704 C CG2 . ILE A 1 84 ? 25.800 27.066 11.427 1.00 55.39 ? 138 ILE A CG2 1 ATOM 705 C CD1 . ILE A 1 84 ? 27.836 29.407 12.174 1.00 54.70 ? 138 ILE A CD1 1 ATOM 706 N N . PHE A 1 85 ? 25.302 27.948 16.094 1.00 49.41 ? 139 PHE A N 1 ATOM 707 C CA . PHE A 1 85 ? 25.620 28.029 17.507 1.00 48.07 ? 139 PHE A CA 1 ATOM 708 C C . PHE A 1 85 ? 24.345 28.462 18.223 1.00 46.10 ? 139 PHE A C 1 ATOM 709 O O . PHE A 1 85 ? 23.645 29.331 17.722 1.00 45.14 ? 139 PHE A O 1 ATOM 710 C CB . PHE A 1 85 ? 26.729 29.046 17.789 1.00 48.19 ? 139 PHE A CB 1 ATOM 711 C CG . PHE A 1 85 ? 26.832 29.418 19.245 1.00 48.96 ? 139 PHE A CG 1 ATOM 712 C CD1 . PHE A 1 85 ? 27.403 28.531 20.165 1.00 49.37 ? 139 PHE A CD1 1 ATOM 713 C CD2 . PHE A 1 85 ? 26.341 30.638 19.702 1.00 49.04 ? 139 PHE A CD2 1 ATOM 714 C CE1 . PHE A 1 85 ? 27.486 28.861 21.514 1.00 49.71 ? 139 PHE A CE1 1 ATOM 715 C CE2 . PHE A 1 85 ? 26.416 30.981 21.057 1.00 46.50 ? 139 PHE A CE2 1 ATOM 716 C CZ . PHE A 1 85 ? 26.981 30.097 21.961 1.00 47.29 ? 139 PHE A CZ 1 ATOM 717 N N . ASN A 1 86 ? 24.045 27.796 19.334 1.00 45.08 ? 140 ASN A N 1 ATOM 718 C CA . ASN A 1 86 ? 22.950 28.186 20.244 1.00 43.93 ? 140 ASN A CA 1 ATOM 719 C C . ASN A 1 86 ? 23.465 28.524 21.633 1.00 41.60 ? 140 ASN A C 1 ATOM 720 O O . ASN A 1 86 ? 24.280 27.781 22.189 1.00 40.84 ? 140 ASN A O 1 ATOM 721 C CB . ASN A 1 86 ? 21.979 27.024 20.404 1.00 44.93 ? 140 ASN A CB 1 ATOM 722 C CG . ASN A 1 86 ? 21.193 26.732 19.134 1.00 49.28 ? 140 ASN A CG 1 ATOM 723 O OD1 . ASN A 1 86 ? 20.934 27.631 18.328 1.00 52.70 ? 140 ASN A OD1 1 ATOM 724 N ND2 . ASN A 1 86 ? 20.801 25.475 18.959 1.00 54.44 ? 140 ASN A ND2 1 ATOM 725 N N . THR A 1 87 ? 22.945 29.604 22.235 1.00 39.74 ? 141 THR A N 1 ATOM 726 C CA . THR A 1 87 ? 23.280 29.889 23.645 1.00 37.24 ? 141 THR A CA 1 ATOM 727 C C . THR A 1 87 ? 22.634 28.807 24.524 1.00 35.86 ? 141 THR A C 1 ATOM 728 O O . THR A 1 87 ? 21.768 28.076 24.064 1.00 36.49 ? 141 THR A O 1 ATOM 729 C CB . THR A 1 87 ? 22.817 31.294 24.055 1.00 36.25 ? 141 THR A CB 1 ATOM 730 O OG1 . THR A 1 87 ? 21.417 31.408 23.804 1.00 34.86 ? 141 THR A OG1 1 ATOM 731 C CG2 . THR A 1 87 ? 23.536 32.369 23.235 1.00 37.91 ? 141 THR A CG2 1 ATOM 732 N N . SER A 1 88 ? 22.987 28.756 25.802 1.00 35.66 ? 142 SER A N 1 ATOM 733 C CA . SER A 1 88 ? 22.486 27.728 26.731 1.00 34.34 ? 142 SER A CA 1 ATOM 734 C C . SER A 1 88 ? 21.003 27.879 27.041 1.00 34.83 ? 142 SER A C 1 ATOM 735 O O . SER A 1 88 ? 20.459 28.997 27.003 1.00 35.26 ? 142 SER A O 1 ATOM 736 C CB . SER A 1 88 ? 23.260 27.826 28.056 1.00 35.19 ? 142 SER A CB 1 ATOM 737 O OG A SER A 1 88 ? 23.312 26.573 28.704 0.50 36.22 ? 142 SER A OG 1 ATOM 738 O OG B SER A 1 88 ? 22.748 28.901 28.857 0.50 32.23 ? 142 SER A OG 1 ATOM 739 N N . LEU A 1 89 ? 20.360 26.775 27.398 1.00 34.59 ? 143 LEU A N 1 ATOM 740 C CA . LEU A 1 89 ? 18.948 26.820 27.769 1.00 35.68 ? 143 LEU A CA 1 ATOM 741 C C . LEU A 1 89 ? 18.793 27.011 29.290 1.00 35.12 ? 143 LEU A C 1 ATOM 742 O O . LEU A 1 89 ? 17.680 27.270 29.762 1.00 35.14 ? 143 LEU A O 1 ATOM 743 C CB . LEU A 1 89 ? 18.213 25.552 27.307 1.00 36.93 ? 143 LEU A CB 1 ATOM 744 C CG . LEU A 1 89 ? 18.162 25.322 25.773 1.00 39.17 ? 143 LEU A CG 1 ATOM 745 C CD1 . LEU A 1 89 ? 17.223 24.201 25.424 1.00 42.46 ? 143 LEU A CD1 1 ATOM 746 C CD2 . LEU A 1 89 ? 17.789 26.583 25.018 1.00 39.24 ? 143 LEU A CD2 1 ATOM 747 N N . PHE A 1 90 ? 19.904 26.872 30.042 1.00 33.54 ? 144 PHE A N 1 ATOM 748 C CA . PHE A 1 90 ? 19.880 26.975 31.511 1.00 32.45 ? 144 PHE A CA 1 ATOM 749 C C . PHE A 1 90 ? 21.293 27.052 32.009 1.00 31.98 ? 144 PHE A C 1 ATOM 750 O O . PHE A 1 90 ? 22.228 26.630 31.287 1.00 31.88 ? 144 PHE A O 1 ATOM 751 C CB . PHE A 1 90 ? 19.170 25.779 32.149 1.00 33.01 ? 144 PHE A CB 1 ATOM 752 C CG . PHE A 1 90 ? 19.757 24.443 31.742 1.00 34.90 ? 144 PHE A CG 1 ATOM 753 C CD1 . PHE A 1 90 ? 20.783 23.872 32.482 1.00 36.64 ? 144 PHE A CD1 1 ATOM 754 C CD2 . PHE A 1 90 ? 19.292 23.785 30.594 1.00 40.86 ? 144 PHE A CD2 1 ATOM 755 C CE1 . PHE A 1 90 ? 21.348 22.650 32.097 1.00 41.69 ? 144 PHE A CE1 1 ATOM 756 C CE2 . PHE A 1 90 ? 19.834 22.562 30.195 1.00 41.67 ? 144 PHE A CE2 1 ATOM 757 C CZ . PHE A 1 90 ? 20.864 21.993 30.951 1.00 43.04 ? 144 PHE A CZ 1 ATOM 758 N N . GLU A 1 91 ? 21.485 27.582 33.217 1.00 28.79 ? 145 GLU A N 1 ATOM 759 C CA . GLU A 1 91 ? 22.796 27.528 33.873 1.00 28.57 ? 145 GLU A CA 1 ATOM 760 C C . GLU A 1 91 ? 23.014 26.141 34.465 1.00 28.45 ? 145 GLU A C 1 ATOM 761 O O . GLU A 1 91 ? 22.101 25.573 35.076 1.00 28.54 ? 145 GLU A O 1 ATOM 762 C CB . GLU A 1 91 ? 22.858 28.521 35.045 1.00 27.50 ? 145 GLU A CB 1 ATOM 763 C CG . GLU A 1 91 ? 22.695 29.978 34.685 1.00 27.02 ? 145 GLU A CG 1 ATOM 764 C CD . GLU A 1 91 ? 22.532 30.826 35.970 1.00 27.94 ? 145 GLU A CD 1 ATOM 765 O OE1 . GLU A 1 91 ? 21.438 30.793 36.545 1.00 29.27 ? 145 GLU A OE1 1 ATOM 766 O OE2 . GLU A 1 91 ? 23.509 31.456 36.405 1.00 29.27 ? 145 GLU A OE2 1 ATOM 767 N N . PRO A 1 92 ? 24.244 25.593 34.343 1.00 29.92 ? 146 PRO A N 1 ATOM 768 C CA . PRO A 1 92 ? 24.493 24.314 35.021 1.00 30.43 ? 146 PRO A CA 1 ATOM 769 C C . PRO A 1 92 ? 24.155 24.406 36.513 1.00 29.79 ? 146 PRO A C 1 ATOM 770 O O . PRO A 1 92 ? 24.730 25.255 37.232 1.00 29.09 ? 146 PRO A O 1 ATOM 771 C CB . PRO A 1 92 ? 26.018 24.086 34.810 1.00 31.50 ? 146 PRO A CB 1 ATOM 772 C CG . PRO A 1 92 ? 26.343 24.843 33.545 1.00 31.59 ? 146 PRO A CG 1 ATOM 773 C CD . PRO A 1 92 ? 25.419 26.084 33.605 1.00 30.20 ? 146 PRO A CD 1 ATOM 774 N N . PRO A 1 93 ? 23.221 23.564 36.994 1.00 30.12 ? 147 PRO A N 1 ATOM 775 C CA . PRO A 1 93 ? 22.843 23.796 38.381 1.00 30.37 ? 147 PRO A CA 1 ATOM 776 C C . PRO A 1 93 ? 23.990 23.481 39.346 1.00 31.22 ? 147 PRO A C 1 ATOM 777 O O . PRO A 1 93 ? 24.830 22.604 39.025 1.00 31.35 ? 147 PRO A O 1 ATOM 778 C CB . PRO A 1 93 ? 21.687 22.815 38.597 1.00 30.72 ? 147 PRO A CB 1 ATOM 779 C CG . PRO A 1 93 ? 21.745 21.876 37.437 1.00 32.37 ? 147 PRO A CG 1 ATOM 780 C CD . PRO A 1 93 ? 22.270 22.659 36.318 1.00 30.59 ? 147 PRO A CD 1 ATOM 781 N N . PRO A 1 94 ? 24.009 24.167 40.506 1.00 30.44 ? 148 PRO A N 1 ATOM 782 C CA . PRO A 1 94 ? 25.046 23.973 41.500 1.00 30.57 ? 148 PRO A CA 1 ATOM 783 C C . PRO A 1 94 ? 24.987 22.550 42.138 1.00 30.34 ? 148 PRO A C 1 ATOM 784 O O . PRO A 1 94 ? 23.906 21.921 42.187 1.00 28.24 ? 148 PRO A O 1 ATOM 785 C CB . PRO A 1 94 ? 24.785 25.090 42.534 1.00 31.38 ? 148 PRO A CB 1 ATOM 786 C CG . PRO A 1 94 ? 23.380 25.515 42.369 1.00 30.19 ? 148 PRO A CG 1 ATOM 787 C CD . PRO A 1 94 ? 22.976 25.137 40.931 1.00 31.07 ? 148 PRO A CD 1 ATOM 788 N N . PRO A 1 95 ? 26.138 22.056 42.653 1.00 29.74 ? 149 PRO A N 1 ATOM 789 C CA . PRO A 1 95 ? 26.216 20.694 43.236 1.00 30.19 ? 149 PRO A CA 1 ATOM 790 C C . PRO A 1 95 ? 25.143 20.399 44.290 1.00 30.03 ? 149 PRO A C 1 ATOM 791 O O . PRO A 1 95 ? 24.974 21.181 45.249 1.00 30.26 ? 149 PRO A O 1 ATOM 792 C CB . PRO A 1 95 ? 27.597 20.673 43.920 1.00 29.73 ? 149 PRO A CB 1 ATOM 793 C CG . PRO A 1 95 ? 28.396 21.707 43.207 1.00 30.96 ? 149 PRO A CG 1 ATOM 794 C CD . PRO A 1 95 ? 27.423 22.772 42.739 1.00 29.32 ? 149 PRO A CD 1 ATOM 795 N N . GLY A 1 96 ? 24.466 19.268 44.146 1.00 30.67 ? 150 GLY A N 1 ATOM 796 C CA . GLY A 1 96 ? 23.516 18.830 45.151 1.00 33.46 ? 150 GLY A CA 1 ATOM 797 C C . GLY A 1 96 ? 22.108 19.407 44.935 1.00 36.30 ? 150 GLY A C 1 ATOM 798 O O . GLY A 1 96 ? 21.171 19.055 45.666 1.00 35.54 ? 150 GLY A O 1 ATOM 799 N N . TYR A 1 97 ? 21.952 20.295 43.960 1.00 37.93 ? 151 TYR A N 1 ATOM 800 C CA . TYR A 1 97 ? 20.634 20.898 43.787 1.00 42.33 ? 151 TYR A CA 1 ATOM 801 C C . TYR A 1 97 ? 19.748 20.053 42.874 1.00 46.55 ? 151 TYR A C 1 ATOM 802 O O . TYR A 1 97 ? 20.163 19.696 41.766 1.00 48.57 ? 151 TYR A O 1 ATOM 803 C CB . TYR A 1 97 ? 20.747 22.386 43.431 1.00 40.35 ? 151 TYR A CB 1 ATOM 804 C CG . TYR A 1 97 ? 21.017 23.190 44.690 1.00 36.27 ? 151 TYR A CG 1 ATOM 805 C CD1 . TYR A 1 97 ? 19.963 23.789 45.404 1.00 32.64 ? 151 TYR A CD1 1 ATOM 806 C CD2 . TYR A 1 97 ? 22.308 23.316 45.189 1.00 31.10 ? 151 TYR A CD2 1 ATOM 807 C CE1 . TYR A 1 97 ? 20.190 24.473 46.558 1.00 31.77 ? 151 TYR A CE1 1 ATOM 808 C CE2 . TYR A 1 97 ? 22.554 24.003 46.323 1.00 29.02 ? 151 TYR A CE2 1 ATOM 809 C CZ . TYR A 1 97 ? 21.491 24.611 47.009 1.00 29.43 ? 151 TYR A CZ 1 ATOM 810 O OH . TYR A 1 97 ? 21.736 25.284 48.158 1.00 28.75 ? 151 TYR A OH 1 ATOM 811 N N . GLU A 1 98 ? 18.559 19.707 43.401 1.00 50.53 ? 152 GLU A N 1 ATOM 812 C CA . GLU A 1 98 ? 17.616 18.752 42.767 1.00 53.97 ? 152 GLU A CA 1 ATOM 813 C C . GLU A 1 98 ? 16.308 19.216 42.081 1.00 54.41 ? 152 GLU A C 1 ATOM 814 O O . GLU A 1 98 ? 15.727 18.422 41.342 1.00 54.40 ? 152 GLU A O 1 ATOM 815 C CB . GLU A 1 98 ? 17.301 17.549 43.713 1.00 55.12 ? 152 GLU A CB 1 ATOM 816 C CG . GLU A 1 98 ? 16.779 17.906 45.106 1.00 56.66 ? 152 GLU A CG 1 ATOM 817 C CD . GLU A 1 98 ? 16.896 16.751 46.112 1.00 60.30 ? 152 GLU A CD 1 ATOM 818 O OE1 . GLU A 1 98 ? 16.994 15.569 45.690 1.00 62.99 ? 152 GLU A OE1 1 ATOM 819 O OE2 . GLU A 1 98 ? 16.877 17.030 47.338 1.00 60.98 ? 152 GLU A OE2 1 ATOM 820 N N . ASN A 1 99 ? 15.780 20.418 42.282 1.00 55.37 ? 153 ASN A N 1 ATOM 821 C CA . ASN A 1 99 ? 14.477 20.598 41.557 1.00 57.32 ? 153 ASN A CA 1 ATOM 822 C C . ASN A 1 99 ? 14.529 21.388 40.273 1.00 57.21 ? 153 ASN A C 1 ATOM 823 O O . ASN A 1 99 ? 13.597 22.115 39.926 1.00 58.04 ? 153 ASN A O 1 ATOM 824 C CB . ASN A 1 99 ? 13.253 20.883 42.441 1.00 57.33 ? 153 ASN A CB 1 ATOM 825 C CG . ASN A 1 99 ? 12.421 19.607 42.752 1.00 59.67 ? 153 ASN A CG 1 ATOM 826 O OD1 . ASN A 1 99 ? 12.656 18.515 42.200 1.00 60.16 ? 153 ASN A OD1 1 ATOM 827 N ND2 . ASN A 1 99 ? 11.436 19.756 43.641 1.00 61.88 ? 153 ASN A ND2 1 ATOM 828 N N . VAL A 1 100 ? 15.583 21.090 39.519 1.00 57.98 ? 154 VAL A N 1 ATOM 829 C CA . VAL A 1 100 ? 16.160 21.977 38.502 1.00 58.11 ? 154 VAL A CA 1 ATOM 830 C C . VAL A 1 100 ? 15.221 22.551 37.431 1.00 58.01 ? 154 VAL A C 1 ATOM 831 O O . VAL A 1 100 ? 15.542 23.579 36.831 1.00 58.33 ? 154 VAL A O 1 ATOM 832 C CB . VAL A 1 100 ? 17.470 21.380 37.873 1.00 58.48 ? 154 VAL A CB 1 ATOM 833 C CG1 . VAL A 1 100 ? 18.441 21.012 38.976 1.00 57.20 ? 154 VAL A CG1 1 ATOM 834 C CG2 . VAL A 1 100 ? 17.174 20.162 36.935 1.00 58.64 ? 154 VAL A CG2 1 ATOM 835 N N . SER A 1 101 ? 14.088 21.880 37.185 1.00 57.68 ? 155 SER A N 1 ATOM 836 C CA . SER A 1 101 ? 13.095 22.399 36.242 1.00 56.17 ? 155 SER A CA 1 ATOM 837 C C . SER A 1 101 ? 12.314 23.562 36.850 1.00 53.59 ? 155 SER A C 1 ATOM 838 O O . SER A 1 101 ? 11.961 24.495 36.106 1.00 54.44 ? 155 SER A O 1 ATOM 839 C CB . SER A 1 101 ? 12.179 21.293 35.685 1.00 57.39 ? 155 SER A CB 1 ATOM 840 O OG . SER A 1 101 ? 11.689 20.457 36.722 1.00 59.78 ? 155 SER A OG 1 ATOM 841 N N . ASP A 1 102 ? 12.090 23.559 38.182 1.00 49.97 ? 156 ASP A N 1 ATOM 842 C CA . ASP A 1 102 ? 11.458 24.724 38.845 1.00 45.62 ? 156 ASP A CA 1 ATOM 843 C C . ASP A 1 102 ? 12.436 25.870 39.087 1.00 41.19 ? 156 ASP A C 1 ATOM 844 O O . ASP A 1 102 ? 12.070 26.928 39.616 1.00 39.30 ? 156 ASP A O 1 ATOM 845 C CB . ASP A 1 102 ? 10.719 24.351 40.129 1.00 47.84 ? 156 ASP A CB 1 ATOM 846 C CG . ASP A 1 102 ? 9.204 24.119 39.904 1.00 52.14 ? 156 ASP A CG 1 ATOM 847 O OD1 . ASP A 1 102 ? 8.496 23.825 40.900 1.00 55.50 ? 156 ASP A OD1 1 ATOM 848 O OD2 . ASP A 1 102 ? 8.713 24.218 38.740 1.00 55.23 ? 156 ASP A OD2 1 ATOM 849 N N . ILE A 1 103 ? 13.689 25.655 38.694 1.00 35.50 ? 157 ILE A N 1 ATOM 850 C CA . ILE A 1 103 ? 14.616 26.762 38.613 1.00 32.53 ? 157 ILE A CA 1 ATOM 851 C C . ILE A 1 103 ? 14.270 27.521 37.327 1.00 31.65 ? 157 ILE A C 1 ATOM 852 O O . ILE A 1 103 ? 14.354 26.951 36.226 1.00 31.26 ? 157 ILE A O 1 ATOM 853 C CB . ILE A 1 103 ? 16.092 26.262 38.564 1.00 30.36 ? 157 ILE A CB 1 ATOM 854 C CG1 . ILE A 1 103 ? 16.480 25.665 39.901 1.00 29.08 ? 157 ILE A CG1 1 ATOM 855 C CG2 . ILE A 1 103 ? 17.027 27.412 38.202 1.00 27.91 ? 157 ILE A CG2 1 ATOM 856 C CD1 . ILE A 1 103 ? 17.825 24.882 39.856 1.00 26.56 ? 157 ILE A CD1 1 ATOM 857 N N . VAL A 1 104 ? 13.857 28.782 37.455 1.00 29.49 ? 158 VAL A N 1 ATOM 858 C CA . VAL A 1 104 ? 13.539 29.556 36.239 1.00 28.63 ? 158 VAL A CA 1 ATOM 859 C C . VAL A 1 104 ? 14.840 29.797 35.469 1.00 28.41 ? 158 VAL A C 1 ATOM 860 O O . VAL A 1 104 ? 15.784 30.291 36.041 1.00 26.61 ? 158 VAL A O 1 ATOM 861 C CB . VAL A 1 104 ? 12.830 30.940 36.560 1.00 26.64 ? 158 VAL A CB 1 ATOM 862 C CG1 . VAL A 1 104 ? 13.889 32.051 37.185 1.00 27.63 ? 158 VAL A CG1 1 ATOM 863 C CG2 . VAL A 1 104 ? 12.095 31.419 35.299 1.00 27.88 ? 158 VAL A CG2 1 ATOM 864 N N . PRO A 1 105 ? 14.883 29.440 34.161 1.00 28.83 ? 159 PRO A N 1 ATOM 865 C CA . PRO A 1 105 ? 16.108 29.702 33.387 1.00 29.09 ? 159 PRO A CA 1 ATOM 866 C C . PRO A 1 105 ? 16.345 31.213 33.209 1.00 27.83 ? 159 PRO A C 1 ATOM 867 O O . PRO A 1 105 ? 15.394 32.021 33.356 1.00 26.96 ? 159 PRO A O 1 ATOM 868 C CB . PRO A 1 105 ? 15.835 28.998 32.017 1.00 29.48 ? 159 PRO A CB 1 ATOM 869 C CG . PRO A 1 105 ? 14.339 28.954 31.902 1.00 31.85 ? 159 PRO A CG 1 ATOM 870 C CD . PRO A 1 105 ? 13.769 28.922 33.330 1.00 30.44 ? 159 PRO A CD 1 ATOM 871 N N . PRO A 1 106 ? 17.591 31.610 32.894 1.00 26.45 ? 160 PRO A N 1 ATOM 872 C CA . PRO A 1 106 ? 17.848 33.023 32.727 1.00 26.49 ? 160 PRO A CA 1 ATOM 873 C C . PRO A 1 106 ? 16.959 33.646 31.652 1.00 26.44 ? 160 PRO A C 1 ATOM 874 O O . PRO A 1 106 ? 16.744 33.060 30.572 1.00 27.16 ? 160 PRO A O 1 ATOM 875 C CB . PRO A 1 106 ? 19.326 33.061 32.315 1.00 25.99 ? 160 PRO A CB 1 ATOM 876 C CG . PRO A 1 106 ? 19.903 31.791 32.911 1.00 25.57 ? 160 PRO A CG 1 ATOM 877 C CD . PRO A 1 106 ? 18.829 30.796 32.694 1.00 27.17 ? 160 PRO A CD 1 ATOM 878 N N . PHE A 1 107 ? 16.421 34.816 31.958 1.00 25.27 ? 161 PHE A N 1 ATOM 879 C CA . PHE A 1 107 ? 15.617 35.568 31.007 1.00 25.20 ? 161 PHE A CA 1 ATOM 880 C C . PHE A 1 107 ? 15.567 37.010 31.487 1.00 24.35 ? 161 PHE A C 1 ATOM 881 O O . PHE A 1 107 ? 15.950 37.275 32.628 1.00 23.91 ? 161 PHE A O 1 ATOM 882 C CB . PHE A 1 107 ? 14.199 34.996 30.931 1.00 25.92 ? 161 PHE A CB 1 ATOM 883 C CG . PHE A 1 107 ? 13.306 35.324 32.139 1.00 26.02 ? 161 PHE A CG 1 ATOM 884 C CD1 . PHE A 1 107 ? 12.159 36.131 31.979 1.00 25.16 ? 161 PHE A CD1 1 ATOM 885 C CD2 . PHE A 1 107 ? 13.537 34.740 33.392 1.00 25.48 ? 161 PHE A CD2 1 ATOM 886 C CE1 . PHE A 1 107 ? 11.302 36.422 33.062 1.00 24.25 ? 161 PHE A CE1 1 ATOM 887 C CE2 . PHE A 1 107 ? 12.685 35.036 34.498 1.00 24.97 ? 161 PHE A CE2 1 ATOM 888 C CZ . PHE A 1 107 ? 11.561 35.861 34.334 1.00 24.07 ? 161 PHE A CZ 1 ATOM 889 N N . SER A 1 108 ? 15.117 37.924 30.618 1.00 23.72 ? 162 SER A N 1 ATOM 890 C CA . SER A 1 108 ? 14.991 39.332 30.981 1.00 23.16 ? 162 SER A CA 1 ATOM 891 C C . SER A 1 108 ? 13.512 39.552 31.177 1.00 23.41 ? 162 SER A C 1 ATOM 892 O O . SER A 1 108 ? 12.747 39.520 30.192 1.00 23.56 ? 162 SER A O 1 ATOM 893 C CB . SER A 1 108 ? 15.489 40.218 29.821 1.00 24.89 ? 162 SER A CB 1 ATOM 894 O OG . SER A 1 108 ? 16.904 40.083 29.640 1.00 25.04 ? 162 SER A OG 1 ATOM 895 N N . ALA A 1 109 ? 13.099 39.760 32.434 1.00 22.23 ? 163 ALA A N 1 ATOM 896 C CA . ALA A 1 109 ? 11.691 39.885 32.745 1.00 22.85 ? 163 ALA A CA 1 ATOM 897 C C . ALA A 1 109 ? 11.079 41.063 32.006 1.00 22.86 ? 163 ALA A C 1 ATOM 898 O O . ALA A 1 109 ? 11.629 42.151 32.024 1.00 22.55 ? 163 ALA A O 1 ATOM 899 C CB . ALA A 1 109 ? 11.466 40.013 34.304 1.00 22.51 ? 163 ALA A CB 1 ATOM 900 N N . PHE A 1 110 ? 9.923 40.789 31.401 1.00 23.59 ? 164 PHE A N 1 ATOM 901 C CA . PHE A 1 110 ? 9.066 41.732 30.632 1.00 25.60 ? 164 PHE A CA 1 ATOM 902 C C . PHE A 1 110 ? 9.474 41.923 29.154 1.00 26.97 ? 164 PHE A C 1 ATOM 903 O O . PHE A 1 110 ? 8.869 42.739 28.437 1.00 28.35 ? 164 PHE A O 1 ATOM 904 C CB . PHE A 1 110 ? 8.833 43.073 31.340 1.00 24.79 ? 164 PHE A CB 1 ATOM 905 C CG . PHE A 1 110 ? 8.168 42.923 32.668 1.00 22.38 ? 164 PHE A CG 1 ATOM 906 C CD1 . PHE A 1 110 ? 6.765 42.734 32.765 1.00 22.37 ? 164 PHE A CD1 1 ATOM 907 C CD2 . PHE A 1 110 ? 8.949 42.951 33.828 1.00 23.75 ? 164 PHE A CD2 1 ATOM 908 C CE1 . PHE A 1 110 ? 6.156 42.603 34.005 1.00 23.99 ? 164 PHE A CE1 1 ATOM 909 C CE2 . PHE A 1 110 ? 8.372 42.827 35.078 1.00 22.14 ? 164 PHE A CE2 1 ATOM 910 C CZ . PHE A 1 110 ? 6.949 42.662 35.170 1.00 19.48 ? 164 PHE A CZ 1 ATOM 911 N N . SER A 1 111 ? 10.460 41.165 28.695 1.00 27.68 ? 165 SER A N 1 ATOM 912 C CA . SER A 1 111 ? 10.791 41.196 27.261 1.00 29.29 ? 165 SER A CA 1 ATOM 913 C C . SER A 1 111 ? 9.530 40.899 26.437 1.00 29.45 ? 165 SER A C 1 ATOM 914 O O . SER A 1 111 ? 8.750 39.985 26.762 1.00 29.74 ? 165 SER A O 1 ATOM 915 C CB . SER A 1 111 ? 11.942 40.221 26.897 1.00 29.69 ? 165 SER A CB 1 ATOM 916 O OG . SER A 1 111 ? 12.119 40.202 25.480 1.00 29.53 ? 165 SER A OG 1 ATOM 917 N N . PRO A 1 112 ? 9.299 41.676 25.364 1.00 30.97 ? 166 PRO A N 1 ATOM 918 C CA . PRO A 1 112 ? 8.273 41.166 24.441 1.00 32.06 ? 166 PRO A CA 1 ATOM 919 C C . PRO A 1 112 ? 8.749 39.892 23.713 1.00 34.02 ? 166 PRO A C 1 ATOM 920 O O . PRO A 1 112 ? 9.944 39.568 23.742 1.00 33.09 ? 166 PRO A O 1 ATOM 921 C CB . PRO A 1 112 ? 8.103 42.320 23.438 1.00 32.60 ? 166 PRO A CB 1 ATOM 922 C CG . PRO A 1 112 ? 9.386 43.000 23.413 1.00 30.58 ? 166 PRO A CG 1 ATOM 923 C CD . PRO A 1 112 ? 9.918 42.918 24.865 1.00 31.78 ? 166 PRO A CD 1 ATOM 924 N N . GLN A 1 113 ? 7.814 39.177 23.095 1.00 35.46 ? 167 GLN A N 1 ATOM 925 C CA . GLN A 1 113 ? 8.130 38.051 22.211 1.00 38.09 ? 167 GLN A CA 1 ATOM 926 C C . GLN A 1 113 ? 8.667 38.493 20.862 1.00 39.48 ? 167 GLN A C 1 ATOM 927 O O . GLN A 1 113 ? 8.438 39.609 20.423 1.00 39.73 ? 167 GLN A O 1 ATOM 928 C CB . GLN A 1 113 ? 6.895 37.198 21.965 1.00 38.36 ? 167 GLN A CB 1 ATOM 929 C CG . GLN A 1 113 ? 6.436 36.486 23.207 1.00 40.70 ? 167 GLN A CG 1 ATOM 930 C CD . GLN A 1 113 ? 5.150 35.780 22.987 1.00 44.86 ? 167 GLN A CD 1 ATOM 931 O OE1 . GLN A 1 113 ? 4.607 35.828 21.898 1.00 50.13 ? 167 GLN A OE1 1 ATOM 932 N NE2 . GLN A 1 113 ? 4.655 35.096 24.010 1.00 46.83 ? 167 GLN A NE2 1 ATOM 933 N N . GLY A 1 114 ? 9.381 37.605 20.188 1.00 41.54 ? 168 GLY A N 1 ATOM 934 C CA . GLY A 1 114 ? 9.967 37.991 18.918 1.00 43.73 ? 168 GLY A CA 1 ATOM 935 C C . GLY A 1 114 ? 11.034 37.009 18.502 1.00 45.71 ? 168 GLY A C 1 ATOM 936 O O . GLY A 1 114 ? 11.513 36.203 19.316 1.00 44.54 ? 168 GLY A O 1 ATOM 937 N N . MET A 1 115 ? 11.371 37.061 17.209 1.00 48.09 ? 169 MET A N 1 ATOM 938 C CA . MET A 1 115 ? 12.517 36.354 16.682 1.00 49.54 ? 169 MET A CA 1 ATOM 939 C C . MET A 1 115 ? 13.278 37.248 15.702 1.00 50.11 ? 169 MET A C 1 ATOM 940 O O . MET A 1 115 ? 13.468 36.859 14.543 1.00 51.20 ? 169 MET A O 1 ATOM 941 C CB . MET A 1 115 ? 12.098 35.057 16.002 1.00 51.05 ? 169 MET A CB 1 ATOM 942 C CG . MET A 1 115 ? 11.326 34.071 16.865 1.00 55.06 ? 169 MET A CG 1 ATOM 943 S SD . MET A 1 115 ? 11.127 32.508 15.991 1.00 66.69 ? 169 MET A SD 1 ATOM 944 C CE . MET A 1 115 ? 9.488 31.982 16.534 1.00 64.25 ? 169 MET A CE 1 ATOM 945 N N . PRO A 1 116 ? 13.729 38.436 16.149 1.00 49.57 ? 170 PRO A N 1 ATOM 946 C CA . PRO A 1 116 ? 14.487 39.305 15.238 1.00 50.47 ? 170 PRO A CA 1 ATOM 947 C C . PRO A 1 116 ? 15.837 38.704 14.780 1.00 51.88 ? 170 PRO A C 1 ATOM 948 O O . PRO A 1 116 ? 16.578 38.144 15.592 1.00 51.10 ? 170 PRO A O 1 ATOM 949 C CB . PRO A 1 116 ? 14.703 40.589 16.041 1.00 50.07 ? 170 PRO A CB 1 ATOM 950 C CG . PRO A 1 116 ? 14.530 40.196 17.489 1.00 48.81 ? 170 PRO A CG 1 ATOM 951 C CD . PRO A 1 116 ? 13.762 38.910 17.547 1.00 48.61 ? 170 PRO A CD 1 ATOM 952 N N . GLU A 1 117 ? 16.113 38.824 13.474 1.00 53.18 ? 171 GLU A N 1 ATOM 953 C CA . GLU A 1 117 ? 17.376 38.378 12.838 1.00 54.15 ? 171 GLU A CA 1 ATOM 954 C C . GLU A 1 117 ? 18.107 39.603 12.348 1.00 54.87 ? 171 GLU A C 1 ATOM 955 O O . GLU A 1 117 ? 17.485 40.496 11.769 1.00 55.80 ? 171 GLU A O 1 ATOM 956 C CB . GLU A 1 117 ? 17.099 37.525 11.611 1.00 54.75 ? 171 GLU A CB 1 ATOM 957 C CG . GLU A 1 117 ? 16.368 36.223 11.849 0.50 54.65 ? 171 GLU A CG 1 ATOM 958 C CD . GLU A 1 117 ? 16.111 35.469 10.554 0.50 55.55 ? 171 GLU A CD 1 ATOM 959 O OE1 . GLU A 1 117 ? 15.008 34.903 10.406 0.50 54.86 ? 171 GLU A OE1 1 ATOM 960 O OE2 . GLU A 1 117 ? 17.008 35.451 9.684 0.50 56.03 ? 171 GLU A OE2 1 ATOM 961 N N . GLY A 1 118 ? 19.416 39.662 12.542 1.00 55.07 ? 172 GLY A N 1 ATOM 962 C CA . GLY A 1 118 ? 20.146 40.866 12.171 1.00 55.75 ? 172 GLY A CA 1 ATOM 963 C C . GLY A 1 118 ? 21.628 40.788 12.458 1.00 56.19 ? 172 GLY A C 1 ATOM 964 O O . GLY A 1 118 ? 22.156 39.723 12.776 1.00 55.73 ? 172 GLY A O 1 ATOM 965 N N . ASP A 1 119 ? 22.277 41.943 12.359 1.00 56.64 ? 173 ASP A N 1 ATOM 966 C CA . ASP A 1 119 ? 23.711 42.062 12.569 1.00 57.26 ? 173 ASP A CA 1 ATOM 967 C C . ASP A 1 119 ? 24.008 42.774 13.876 1.00 56.30 ? 173 ASP A C 1 ATOM 968 O O . ASP A 1 119 ? 23.298 43.714 14.275 1.00 55.73 ? 173 ASP A O 1 ATOM 969 C CB . ASP A 1 119 ? 24.358 42.819 11.403 1.00 58.74 ? 173 ASP A CB 1 ATOM 970 C CG . ASP A 1 119 ? 24.075 42.168 10.050 1.00 60.65 ? 173 ASP A CG 1 ATOM 971 O OD1 . ASP A 1 119 ? 24.411 40.972 9.867 1.00 64.08 ? 173 ASP A OD1 1 ATOM 972 O OD2 . ASP A 1 119 ? 23.515 42.858 9.167 1.00 61.80 ? 173 ASP A OD2 1 ATOM 973 N N . LEU A 1 120 ? 25.070 42.326 14.531 1.00 55.12 ? 174 LEU A N 1 ATOM 974 C CA . LEU A 1 120 ? 25.408 42.790 15.853 1.00 54.15 ? 174 LEU A CA 1 ATOM 975 C C . LEU A 1 120 ? 26.148 44.123 15.834 1.00 54.31 ? 174 LEU A C 1 ATOM 976 O O . LEU A 1 120 ? 26.975 44.369 14.953 1.00 55.82 ? 174 LEU A O 1 ATOM 977 C CB . LEU A 1 120 ? 26.271 41.709 16.517 1.00 53.94 ? 174 LEU A CB 1 ATOM 978 C CG A LEU A 1 120 ? 26.227 41.416 18.014 0.50 52.24 ? 174 LEU A CG 1 ATOM 979 C CG B LEU A 1 120 ? 25.601 40.541 17.255 0.50 52.89 ? 174 LEU A CG 1 ATOM 980 C CD1 A LEU A 1 120 ? 24.833 40.997 18.474 0.50 50.39 ? 174 LEU A CD1 1 ATOM 981 C CD1 B LEU A 1 120 ? 26.631 39.547 17.772 0.50 50.97 ? 174 LEU A CD1 1 ATOM 982 C CD2 A LEU A 1 120 ? 27.240 40.328 18.334 0.50 50.31 ? 174 LEU A CD2 1 ATOM 983 C CD2 B LEU A 1 120 ? 24.731 41.025 18.409 0.50 50.86 ? 174 LEU A CD2 1 ATOM 984 N N . VAL A 1 121 ? 25.835 44.984 16.796 1.00 53.65 ? 175 VAL A N 1 ATOM 985 C CA . VAL A 1 121 ? 26.682 46.126 17.150 1.00 53.11 ? 175 VAL A CA 1 ATOM 986 C C . VAL A 1 121 ? 26.988 46.007 18.637 1.00 52.49 ? 175 VAL A C 1 ATOM 987 O O . VAL A 1 121 ? 26.138 45.535 19.416 1.00 52.22 ? 175 VAL A O 1 ATOM 988 C CB . VAL A 1 121 ? 25.999 47.482 16.860 1.00 53.43 ? 175 VAL A CB 1 ATOM 989 C CG1 . VAL A 1 121 ? 26.791 48.668 17.453 1.00 52.73 ? 175 VAL A CG1 1 ATOM 990 C CG2 . VAL A 1 121 ? 25.797 47.668 15.375 1.00 54.65 ? 175 VAL A CG2 1 ATOM 991 N N . TYR A 1 122 ? 28.186 46.443 19.027 1.00 50.95 ? 176 TYR A N 1 ATOM 992 C CA . TYR A 1 122 ? 28.654 46.284 20.379 1.00 49.54 ? 176 TYR A CA 1 ATOM 993 C C . TYR A 1 122 ? 28.695 47.669 20.995 1.00 49.69 ? 176 TYR A C 1 ATOM 994 O O . TYR A 1 122 ? 29.436 48.565 20.533 1.00 49.47 ? 176 TYR A O 1 ATOM 995 C CB . TYR A 1 122 ? 30.015 45.532 20.451 1.00 49.73 ? 176 TYR A CB 1 ATOM 996 C CG . TYR A 1 122 ? 30.706 45.695 21.790 1.00 48.76 ? 176 TYR A CG 1 ATOM 997 C CD1 . TYR A 1 122 ? 30.219 45.041 22.931 1.00 46.11 ? 176 TYR A CD1 1 ATOM 998 C CD2 . TYR A 1 122 ? 31.811 46.546 21.934 1.00 47.15 ? 176 TYR A CD2 1 ATOM 999 C CE1 . TYR A 1 122 ? 30.831 45.223 24.181 1.00 46.19 ? 176 TYR A CE1 1 ATOM 1000 C CE2 . TYR A 1 122 ? 32.415 46.741 23.170 1.00 46.03 ? 176 TYR A CE2 1 ATOM 1001 C CZ . TYR A 1 122 ? 31.923 46.066 24.292 1.00 45.32 ? 176 TYR A CZ 1 ATOM 1002 O OH . TYR A 1 122 ? 32.514 46.240 25.523 1.00 44.23 ? 176 TYR A OH 1 ATOM 1003 N N . VAL A 1 123 ? 27.879 47.842 22.035 1.00 47.36 ? 177 VAL A N 1 ATOM 1004 C CA . VAL A 1 123 ? 27.568 49.168 22.547 1.00 47.31 ? 177 VAL A CA 1 ATOM 1005 C C . VAL A 1 123 ? 28.178 49.403 23.908 1.00 46.68 ? 177 VAL A C 1 ATOM 1006 O O . VAL A 1 123 ? 27.757 50.294 24.640 1.00 46.09 ? 177 VAL A O 1 ATOM 1007 C CB . VAL A 1 123 ? 26.031 49.492 22.464 1.00 46.84 ? 177 VAL A CB 1 ATOM 1008 C CG1 . VAL A 1 123 ? 25.571 49.376 21.031 1.00 46.94 ? 177 VAL A CG1 1 ATOM 1009 C CG2 . VAL A 1 123 ? 25.183 48.533 23.336 1.00 45.53 ? 177 VAL A CG2 1 ATOM 1010 N N . ASN A 1 124 ? 29.222 48.630 24.223 1.00 46.93 ? 178 ASN A N 1 ATOM 1011 C CA . ASN A 1 124 ? 29.879 48.764 25.516 1.00 47.06 ? 178 ASN A CA 1 ATOM 1012 C C . ASN A 1 124 ? 28.818 48.540 26.647 1.00 46.26 ? 178 ASN A C 1 ATOM 1013 O O . ASN A 1 124 ? 28.138 47.514 26.625 1.00 45.64 ? 178 ASN A O 1 ATOM 1014 C CB . ASN A 1 124 ? 30.623 50.118 25.632 1.00 47.17 ? 178 ASN A CB 1 ATOM 1015 C CG . ASN A 1 124 ? 31.667 50.125 26.737 1.00 47.41 ? 178 ASN A CG 1 ATOM 1016 O OD1 . ASN A 1 124 ? 32.149 49.074 27.150 1.00 45.81 ? 178 ASN A OD1 1 ATOM 1017 N ND2 . ASN A 1 124 ? 32.024 51.312 27.220 1.00 48.25 ? 178 ASN A ND2 1 ATOM 1018 N N . TYR A 1 125 ? 28.688 49.468 27.602 1.00 46.87 ? 179 TYR A N 1 ATOM 1019 C CA . TYR A 1 125 ? 27.654 49.378 28.674 1.00 46.65 ? 179 TYR A CA 1 ATOM 1020 C C . TYR A 1 125 ? 26.255 49.904 28.322 1.00 47.14 ? 179 TYR A C 1 ATOM 1021 O O . TYR A 1 125 ? 25.350 49.907 29.189 1.00 46.25 ? 179 TYR A O 1 ATOM 1022 C CB . TYR A 1 125 ? 28.105 50.113 29.932 1.00 46.39 ? 179 TYR A CB 1 ATOM 1023 C CG . TYR A 1 125 ? 29.361 49.563 30.533 1.00 47.40 ? 179 TYR A CG 1 ATOM 1024 C CD1 . TYR A 1 125 ? 29.339 48.377 31.250 1.00 45.28 ? 179 TYR A CD1 1 ATOM 1025 C CD2 . TYR A 1 125 ? 30.589 50.241 30.383 1.00 46.53 ? 179 TYR A CD2 1 ATOM 1026 C CE1 . TYR A 1 125 ? 30.483 47.870 31.818 1.00 46.28 ? 179 TYR A CE1 1 ATOM 1027 C CE2 . TYR A 1 125 ? 31.750 49.747 30.954 1.00 46.58 ? 179 TYR A CE2 1 ATOM 1028 C CZ . TYR A 1 125 ? 31.696 48.567 31.665 1.00 47.72 ? 179 TYR A CZ 1 ATOM 1029 O OH . TYR A 1 125 ? 32.821 48.057 32.226 1.00 47.48 ? 179 TYR A OH 1 ATOM 1030 N N . ALA A 1 126 ? 26.075 50.339 27.076 1.00 47.63 ? 180 ALA A N 1 ATOM 1031 C CA . ALA A 1 126 ? 24.849 51.008 26.633 1.00 47.50 ? 180 ALA A CA 1 ATOM 1032 C C . ALA A 1 126 ? 24.418 52.196 27.520 1.00 47.54 ? 180 ALA A C 1 ATOM 1033 O O . ALA A 1 126 ? 23.207 52.450 27.708 1.00 46.60 ? 180 ALA A O 1 ATOM 1034 C CB . ALA A 1 126 ? 23.718 49.985 26.467 1.00 47.38 ? 180 ALA A CB 1 ATOM 1035 N N . ARG A 1 127 ? 25.398 52.905 28.086 1.00 47.06 ? 181 ARG A N 1 ATOM 1036 C CA . ARG A 1 127 ? 25.116 54.145 28.796 1.00 47.22 ? 181 ARG A CA 1 ATOM 1037 C C . ARG A 1 127 ? 24.719 55.259 27.804 1.00 47.67 ? 181 ARG A C 1 ATOM 1038 O O . ARG A 1 127 ? 24.911 55.123 26.587 1.00 47.45 ? 181 ARG A O 1 ATOM 1039 C CB . ARG A 1 127 ? 26.305 54.570 29.635 1.00 47.21 ? 181 ARG A CB 1 ATOM 1040 C CG . ARG A 1 127 ? 26.599 53.660 30.805 1.00 46.74 ? 181 ARG A CG 1 ATOM 1041 C CD . ARG A 1 127 ? 27.978 53.922 31.337 1.00 48.38 ? 181 ARG A CD 1 ATOM 1042 N NE . ARG A 1 127 ? 28.996 53.804 30.288 1.00 47.64 ? 181 ARG A NE 1 ATOM 1043 C CZ . ARG A 1 127 ? 30.299 54.007 30.474 1.00 46.90 ? 181 ARG A CZ 1 ATOM 1044 N NH1 . ARG A 1 127 ? 30.762 54.334 31.674 1.00 45.45 ? 181 ARG A NH1 1 ATOM 1045 N NH2 . ARG A 1 127 ? 31.131 53.886 29.446 1.00 48.27 ? 181 ARG A NH2 1 ATOM 1046 N N . THR A 1 128 ? 24.119 56.332 28.337 1.00 47.82 ? 182 THR A N 1 ATOM 1047 C CA . THR A 1 128 ? 23.837 57.531 27.545 1.00 48.14 ? 182 THR A CA 1 ATOM 1048 C C . THR A 1 128 ? 25.157 57.982 26.890 1.00 48.74 ? 182 THR A C 1 ATOM 1049 O O . THR A 1 128 ? 25.226 58.085 25.657 1.00 48.56 ? 182 THR A O 1 ATOM 1050 C CB . THR A 1 128 ? 23.176 58.661 28.393 1.00 48.65 ? 182 THR A CB 1 ATOM 1051 O OG1 . THR A 1 128 ? 21.840 58.266 28.785 1.00 48.47 ? 182 THR A OG1 1 ATOM 1052 C CG2 . THR A 1 128 ? 23.083 59.948 27.597 1.00 47.28 ? 182 THR A CG2 1 ATOM 1053 N N . GLU A 1 129 ? 26.205 58.150 27.703 1.00 48.77 ? 183 GLU A N 1 ATOM 1054 C CA . GLU A 1 129 ? 27.524 58.562 27.179 1.00 51.30 ? 183 GLU A CA 1 ATOM 1055 C C . GLU A 1 129 ? 28.067 57.626 26.090 1.00 51.19 ? 183 GLU A C 1 ATOM 1056 O O . GLU A 1 129 ? 28.648 58.099 25.128 1.00 51.32 ? 183 GLU A O 1 ATOM 1057 C CB . GLU A 1 129 ? 28.555 58.752 28.295 1.00 51.34 ? 183 GLU A CB 1 ATOM 1058 C CG . GLU A 1 129 ? 29.097 57.466 28.918 1.00 54.03 ? 183 GLU A CG 1 ATOM 1059 C CD . GLU A 1 129 ? 29.643 57.688 30.328 1.00 58.00 ? 183 GLU A CD 1 ATOM 1060 O OE1 . GLU A 1 129 ? 28.821 57.786 31.267 1.00 56.71 ? 183 GLU A OE1 1 ATOM 1061 O OE2 . GLU A 1 129 ? 30.892 57.758 30.497 1.00 60.66 ? 183 GLU A OE2 1 ATOM 1062 N N . ASP A 1 130 ? 27.871 56.309 26.244 1.00 51.67 ? 184 ASP A N 1 ATOM 1063 C CA . ASP A 1 130 ? 28.347 55.321 25.231 1.00 51.95 ? 184 ASP A CA 1 ATOM 1064 C C . ASP A 1 130 ? 27.625 55.481 23.889 1.00 52.17 ? 184 ASP A C 1 ATOM 1065 O O . ASP A 1 130 ? 28.230 55.337 22.836 1.00 53.00 ? 184 ASP A O 1 ATOM 1066 C CB . ASP A 1 130 ? 28.209 53.854 25.704 1.00 51.51 ? 184 ASP A CB 1 ATOM 1067 C CG . ASP A 1 130 ? 28.950 53.566 27.008 1.00 50.96 ? 184 ASP A CG 1 ATOM 1068 O OD1 . ASP A 1 130 ? 30.157 53.904 27.138 1.00 48.82 ? 184 ASP A OD1 1 ATOM 1069 O OD2 . ASP A 1 130 ? 28.323 52.949 27.900 1.00 45.15 ? 184 ASP A OD2 1 ATOM 1070 N N . PHE A 1 131 ? 26.327 55.766 23.933 1.00 52.42 ? 185 PHE A N 1 ATOM 1071 C CA . PHE A 1 131 ? 25.542 55.952 22.708 1.00 52.77 ? 185 PHE A CA 1 ATOM 1072 C C . PHE A 1 131 ? 25.842 57.264 21.995 1.00 54.01 ? 185 PHE A C 1 ATOM 1073 O O . PHE A 1 131 ? 25.809 57.307 20.749 1.00 53.40 ? 185 PHE A O 1 ATOM 1074 C CB . PHE A 1 131 ? 24.042 55.829 22.977 1.00 51.65 ? 185 PHE A CB 1 ATOM 1075 C CG . PHE A 1 131 ? 23.548 54.411 22.964 1.00 49.36 ? 185 PHE A CG 1 ATOM 1076 C CD1 . PHE A 1 131 ? 23.295 53.739 24.159 1.00 47.29 ? 185 PHE A CD1 1 ATOM 1077 C CD2 . PHE A 1 131 ? 23.343 53.741 21.752 1.00 46.51 ? 185 PHE A CD2 1 ATOM 1078 C CE1 . PHE A 1 131 ? 22.837 52.410 24.147 1.00 45.14 ? 185 PHE A CE1 1 ATOM 1079 C CE2 . PHE A 1 131 ? 22.905 52.418 21.729 1.00 45.06 ? 185 PHE A CE2 1 ATOM 1080 C CZ . PHE A 1 131 ? 22.638 51.746 22.941 1.00 42.23 ? 185 PHE A CZ 1 ATOM 1081 N N . PHE A 1 132 ? 26.095 58.314 22.800 1.00 54.85 ? 186 PHE A N 1 ATOM 1082 C CA . PHE A 1 132 ? 26.587 59.627 22.324 1.00 56.29 ? 186 PHE A CA 1 ATOM 1083 C C . PHE A 1 132 ? 27.886 59.435 21.531 1.00 58.00 ? 186 PHE A C 1 ATOM 1084 O O . PHE A 1 132 ? 28.029 59.991 20.440 1.00 58.25 ? 186 PHE A O 1 ATOM 1085 C CB . PHE A 1 132 ? 26.899 60.600 23.491 1.00 55.62 ? 186 PHE A CB 1 ATOM 1086 C CG . PHE A 1 132 ? 25.696 61.338 24.073 1.00 54.34 ? 186 PHE A CG 1 ATOM 1087 C CD1 . PHE A 1 132 ? 24.469 61.420 23.400 1.00 53.39 ? 186 PHE A CD1 1 ATOM 1088 C CD2 . PHE A 1 132 ? 25.833 62.019 25.294 1.00 53.35 ? 186 PHE A CD2 1 ATOM 1089 C CE1 . PHE A 1 132 ? 23.384 62.134 23.959 1.00 53.04 ? 186 PHE A CE1 1 ATOM 1090 C CE2 . PHE A 1 132 ? 24.760 62.747 25.861 1.00 50.70 ? 186 PHE A CE2 1 ATOM 1091 C CZ . PHE A 1 132 ? 23.535 62.802 25.196 1.00 50.53 ? 186 PHE A CZ 1 ATOM 1092 N N . LYS A 1 133 ? 28.822 58.662 22.107 1.00 59.24 ? 187 LYS A N 1 ATOM 1093 C CA . LYS A 1 133 ? 30.121 58.328 21.486 1.00 60.96 ? 187 LYS A CA 1 ATOM 1094 C C . LYS A 1 133 ? 30.005 57.483 20.206 1.00 61.63 ? 187 LYS A C 1 ATOM 1095 O O . LYS A 1 133 ? 30.777 57.669 19.268 1.00 62.57 ? 187 LYS A O 1 ATOM 1096 C CB . LYS A 1 133 ? 31.049 57.653 22.509 1.00 61.21 ? 187 LYS A CB 1 ATOM 1097 C CG . LYS A 1 133 ? 32.387 57.125 21.945 1.00 64.35 ? 187 LYS A CG 1 ATOM 1098 C CD . LYS A 1 133 ? 33.544 57.370 22.904 1.00 67.54 ? 187 LYS A CD 1 ATOM 1099 C CE . LYS A 1 133 ? 34.145 58.765 22.696 1.00 69.77 ? 187 LYS A CE 1 ATOM 1100 N NZ . LYS A 1 133 ? 35.109 59.146 23.773 1.00 70.95 ? 187 LYS A NZ 1 ATOM 1101 N N . LEU A 1 134 ? 29.051 56.560 20.171 1.00 61.52 ? 188 LEU A N 1 ATOM 1102 C CA . LEU A 1 134 ? 28.770 55.778 18.969 1.00 62.22 ? 188 LEU A CA 1 ATOM 1103 C C . LEU A 1 134 ? 28.305 56.656 17.827 1.00 63.14 ? 188 LEU A C 1 ATOM 1104 O O . LEU A 1 134 ? 28.855 56.573 16.725 1.00 63.29 ? 188 LEU A O 1 ATOM 1105 C CB . LEU A 1 134 ? 27.676 54.751 19.239 1.00 61.81 ? 188 LEU A CB 1 ATOM 1106 C CG . LEU A 1 134 ? 28.106 53.384 19.740 1.00 62.52 ? 188 LEU A CG 1 ATOM 1107 C CD1 . LEU A 1 134 ? 26.912 52.711 20.377 1.00 63.14 ? 188 LEU A CD1 1 ATOM 1108 C CD2 . LEU A 1 134 ? 28.663 52.545 18.594 1.00 62.57 ? 188 LEU A CD2 1 ATOM 1109 N N . GLU A 1 135 ? 27.298 57.497 18.092 1.00 62.86 ? 189 GLU A N 1 ATOM 1110 C CA . GLU A 1 135 ? 26.619 58.227 17.022 1.00 64.44 ? 189 GLU A CA 1 ATOM 1111 C C . GLU A 1 135 ? 27.323 59.536 16.649 1.00 64.99 ? 189 GLU A C 1 ATOM 1112 O O . GLU A 1 135 ? 27.522 59.823 15.455 1.00 65.73 ? 189 GLU A O 1 ATOM 1113 C CB . GLU A 1 135 ? 25.140 58.481 17.359 1.00 64.23 ? 189 GLU A CB 1 ATOM 1114 C CG . GLU A 1 135 ? 24.313 58.969 16.149 1.00 67.14 ? 189 GLU A CG 1 ATOM 1115 C CD . GLU A 1 135 ? 23.222 59.974 16.521 1.00 69.65 ? 189 GLU A CD 1 ATOM 1116 O OE1 . GLU A 1 135 ? 22.178 59.556 17.072 1.00 69.55 ? 189 GLU A OE1 1 ATOM 1117 O OE2 . GLU A 1 135 ? 23.403 61.186 16.246 1.00 71.45 ? 189 GLU A OE2 1 ATOM 1118 N N . ARG A 1 136 ? 27.704 60.304 17.674 1.00 64.83 ? 190 ARG A N 1 ATOM 1119 C CA . ARG A 1 136 ? 28.275 61.652 17.509 1.00 65.36 ? 190 ARG A CA 1 ATOM 1120 C C . ARG A 1 136 ? 29.777 61.684 17.162 1.00 66.80 ? 190 ARG A C 1 ATOM 1121 O O . ARG A 1 136 ? 30.211 62.570 16.419 1.00 67.53 ? 190 ARG A O 1 ATOM 1122 C CB . ARG A 1 136 ? 28.007 62.520 18.755 1.00 64.33 ? 190 ARG A CB 1 ATOM 1123 C CG . ARG A 1 136 ? 26.537 62.696 19.113 1.00 61.11 ? 190 ARG A CG 1 ATOM 1124 C CD . ARG A 1 136 ? 26.367 63.430 20.427 1.00 56.59 ? 190 ARG A CD 1 ATOM 1125 N NE . ARG A 1 136 ? 24.958 63.767 20.653 1.00 54.83 ? 190 ARG A NE 1 ATOM 1126 C CZ . ARG A 1 136 ? 24.494 64.549 21.635 1.00 51.19 ? 190 ARG A CZ 1 ATOM 1127 N NH1 . ARG A 1 136 ? 25.319 65.093 22.522 1.00 47.45 ? 190 ARG A NH1 1 ATOM 1128 N NH2 . ARG A 1 136 ? 23.189 64.782 21.729 1.00 45.23 ? 190 ARG A NH2 1 ATOM 1129 N N . ASP A 1 137 ? 30.556 60.747 17.717 1.00 67.57 ? 191 ASP A N 1 ATOM 1130 C CA . ASP A 1 137 ? 32.015 60.673 17.484 1.00 68.94 ? 191 ASP A CA 1 ATOM 1131 C C . ASP A 1 137 ? 32.402 59.661 16.395 1.00 69.56 ? 191 ASP A C 1 ATOM 1132 O O . ASP A 1 137 ? 33.307 59.919 15.604 1.00 70.26 ? 191 ASP A O 1 ATOM 1133 C CB . ASP A 1 137 ? 32.784 60.303 18.769 1.00 69.02 ? 191 ASP A CB 1 ATOM 1134 C CG . ASP A 1 137 ? 32.695 61.371 19.862 1.00 70.48 ? 191 ASP A CG 1 ATOM 1135 O OD1 . ASP A 1 137 ? 33.044 62.547 19.599 1.00 72.57 ? 191 ASP A OD1 1 ATOM 1136 O OD2 . ASP A 1 137 ? 32.313 61.015 21.004 1.00 70.52 ? 191 ASP A OD2 1 ATOM 1137 N N . MET A 1 138 ? 31.728 58.511 16.378 1.00 69.18 ? 192 MET A N 1 ATOM 1138 C CA . MET A 1 138 ? 32.102 57.385 15.513 1.00 69.85 ? 192 MET A CA 1 ATOM 1139 C C . MET A 1 138 ? 31.172 57.229 14.313 1.00 69.84 ? 192 MET A C 1 ATOM 1140 O O . MET A 1 138 ? 31.400 56.355 13.458 1.00 69.94 ? 192 MET A O 1 ATOM 1141 C CB . MET A 1 138 ? 32.087 56.059 16.298 1.00 69.64 ? 192 MET A CB 1 ATOM 1142 C CG . MET A 1 138 ? 33.059 55.934 17.465 1.00 70.31 ? 192 MET A CG 1 ATOM 1143 S SD . MET A 1 138 ? 32.842 54.326 18.282 1.00 72.63 ? 192 MET A SD 1 ATOM 1144 C CE . MET A 1 138 ? 33.521 53.196 17.058 1.00 70.73 ? 192 MET A CE 1 ATOM 1145 N N . LYS A 1 139 ? 30.116 58.047 14.267 1.00 69.48 ? 193 LYS A N 1 ATOM 1146 C CA . LYS A 1 139 ? 29.129 57.996 13.176 1.00 69.74 ? 193 LYS A CA 1 ATOM 1147 C C . LYS A 1 139 ? 28.634 56.561 12.883 1.00 69.25 ? 193 LYS A C 1 ATOM 1148 O O . LYS A 1 139 ? 28.539 56.147 11.718 1.00 69.28 ? 193 LYS A O 1 ATOM 1149 C CB . LYS A 1 139 ? 29.704 58.649 11.898 1.00 70.97 ? 193 LYS A CB 1 ATOM 1150 C CG . LYS A 1 139 ? 29.331 60.118 11.684 1.00 72.16 ? 193 LYS A CG 1 ATOM 1151 C CD . LYS A 1 139 ? 29.887 61.046 12.765 1.00 72.47 ? 193 LYS A CD 1 ATOM 1152 C CE . LYS A 1 139 ? 29.900 62.486 12.268 1.00 73.36 ? 193 LYS A CE 1 ATOM 1153 N NZ . LYS A 1 139 ? 30.103 63.467 13.362 1.00 72.93 ? 193 LYS A NZ 1 ATOM 1154 N N . ILE A 1 140 ? 28.346 55.802 13.946 1.00 68.18 ? 194 ILE A N 1 ATOM 1155 C CA . ILE A 1 140 ? 27.810 54.444 13.808 1.00 67.60 ? 194 ILE A CA 1 ATOM 1156 C C . ILE A 1 140 ? 26.314 54.458 14.125 1.00 66.68 ? 194 ILE A C 1 ATOM 1157 O O . ILE A 1 140 ? 25.877 55.154 15.046 1.00 66.25 ? 194 ILE A O 1 ATOM 1158 C CB . ILE A 1 140 ? 28.628 53.389 14.632 1.00 67.73 ? 194 ILE A CB 1 ATOM 1159 C CG1 . ILE A 1 140 ? 29.962 53.087 13.914 1.00 68.10 ? 194 ILE A CG1 1 ATOM 1160 C CG2 . ILE A 1 140 ? 27.837 52.090 14.823 1.00 67.68 ? 194 ILE A CG2 1 ATOM 1161 C CD1 . ILE A 1 140 ? 30.943 52.212 14.680 1.00 66.84 ? 194 ILE A CD1 1 ATOM 1162 N N . ASN A 1 141 ? 25.541 53.724 13.326 1.00 66.20 ? 195 ASN A N 1 ATOM 1163 C CA . ASN A 1 141 ? 24.079 53.780 13.371 1.00 65.68 ? 195 ASN A CA 1 ATOM 1164 C C . ASN A 1 141 ? 23.456 52.459 13.850 1.00 64.61 ? 195 ASN A C 1 ATOM 1165 O O . ASN A 1 141 ? 23.586 51.417 13.186 1.00 64.75 ? 195 ASN A O 1 ATOM 1166 C CB . ASN A 1 141 ? 23.504 54.203 12.001 1.00 66.17 ? 195 ASN A CB 1 ATOM 1167 C CG . ASN A 1 141 ? 22.067 54.733 12.094 1.00 67.09 ? 195 ASN A CG 1 ATOM 1168 O OD1 . ASN A 1 141 ? 21.309 54.382 13.010 1.00 66.27 ? 195 ASN A OD1 1 ATOM 1169 N ND2 . ASN A 1 141 ? 21.686 55.580 11.137 1.00 67.58 ? 195 ASN A ND2 1 ATOM 1170 N N . CYS A 1 142 ? 22.769 52.517 14.994 1.00 62.98 ? 196 CYS A N 1 ATOM 1171 C CA . CYS A 1 142 ? 22.227 51.301 15.622 1.00 61.73 ? 196 CYS A CA 1 ATOM 1172 C C . CYS A 1 142 ? 20.887 50.835 15.046 1.00 61.01 ? 196 CYS A C 1 ATOM 1173 O O . CYS A 1 142 ? 20.456 49.706 15.296 1.00 60.71 ? 196 CYS A O 1 ATOM 1174 C CB . CYS A 1 142 ? 22.137 51.470 17.140 1.00 61.24 ? 196 CYS A CB 1 ATOM 1175 S SG . CYS A 1 142 ? 23.742 51.448 17.962 1.00 61.19 ? 196 CYS A SG 1 ATOM 1176 N N . SER A 1 143 ? 20.243 51.694 14.257 1.00 60.20 ? 197 SER A N 1 ATOM 1177 C CA . SER A 1 143 ? 18.937 51.386 13.671 1.00 59.15 ? 197 SER A CA 1 ATOM 1178 C C . SER A 1 143 ? 18.857 50.033 12.925 1.00 58.63 ? 197 SER A C 1 ATOM 1179 O O . SER A 1 143 ? 19.610 49.792 11.985 1.00 60.09 ? 197 SER A O 1 ATOM 1180 C CB . SER A 1 143 ? 18.482 52.545 12.776 1.00 59.43 ? 197 SER A CB 1 ATOM 1181 O OG . SER A 1 143 ? 17.210 52.284 12.227 1.00 58.64 ? 197 SER A OG 1 ATOM 1182 N N . GLY A 1 144 ? 17.944 49.158 13.356 1.00 57.08 ? 198 GLY A N 1 ATOM 1183 C CA . GLY A 1 144 ? 17.752 47.831 12.748 1.00 55.35 ? 198 GLY A CA 1 ATOM 1184 C C . GLY A 1 144 ? 18.807 46.792 13.145 1.00 54.92 ? 198 GLY A C 1 ATOM 1185 O O . GLY A 1 144 ? 18.742 45.635 12.713 1.00 54.43 ? 198 GLY A O 1 ATOM 1186 N N . LYS A 1 145 ? 19.778 47.194 13.973 1.00 54.06 ? 199 LYS A N 1 ATOM 1187 C CA . LYS A 1 145 ? 20.826 46.272 14.458 1.00 53.46 ? 199 LYS A CA 1 ATOM 1188 C C . LYS A 1 145 ? 20.363 45.550 15.738 1.00 52.48 ? 199 LYS A C 1 ATOM 1189 O O . LYS A 1 145 ? 19.450 46.023 16.425 1.00 51.60 ? 199 LYS A O 1 ATOM 1190 C CB . LYS A 1 145 ? 22.115 47.046 14.757 1.00 53.42 ? 199 LYS A CB 1 ATOM 1191 C CG . LYS A 1 145 ? 22.597 47.946 13.601 1.00 56.41 ? 199 LYS A CG 1 ATOM 1192 C CD . LYS A 1 145 ? 23.239 47.134 12.488 1.00 58.32 ? 199 LYS A CD 1 ATOM 1193 C CE . LYS A 1 145 ? 23.489 47.984 11.246 1.00 61.26 ? 199 LYS A CE 1 ATOM 1194 N NZ . LYS A 1 145 ? 22.582 47.596 10.123 1.00 60.96 ? 199 LYS A NZ 1 ATOM 1195 N N . ILE A 1 146 ? 20.977 44.406 16.040 1.00 51.65 ? 200 ILE A N 1 ATOM 1196 C CA . ILE A 1 146 ? 20.869 43.802 17.380 1.00 50.43 ? 200 ILE A CA 1 ATOM 1197 C C . ILE A 1 146 ? 22.052 44.322 18.194 1.00 49.92 ? 200 ILE A C 1 ATOM 1198 O O . ILE A 1 146 ? 23.202 44.158 17.769 1.00 50.72 ? 200 ILE A O 1 ATOM 1199 C CB . ILE A 1 146 ? 20.867 42.265 17.305 1.00 50.32 ? 200 ILE A CB 1 ATOM 1200 C CG1 . ILE A 1 146 ? 19.568 41.783 16.658 1.00 49.79 ? 200 ILE A CG1 1 ATOM 1201 C CG2 . ILE A 1 146 ? 21.027 41.654 18.697 1.00 50.13 ? 200 ILE A CG2 1 ATOM 1202 C CD1 . ILE A 1 146 ? 19.498 40.272 16.416 1.00 48.25 ? 200 ILE A CD1 1 ATOM 1203 N N . VAL A 1 147 ? 21.801 44.982 19.324 1.00 48.10 ? 201 VAL A N 1 ATOM 1204 C CA . VAL A 1 147 ? 22.937 45.450 20.115 1.00 47.63 ? 201 VAL A CA 1 ATOM 1205 C C . VAL A 1 147 ? 23.314 44.411 21.168 1.00 46.58 ? 201 VAL A C 1 ATOM 1206 O O . VAL A 1 147 ? 22.449 43.722 21.733 1.00 45.81 ? 201 VAL A O 1 ATOM 1207 C CB . VAL A 1 147 ? 22.758 46.865 20.743 1.00 48.55 ? 201 VAL A CB 1 ATOM 1208 C CG1 . VAL A 1 147 ? 22.506 47.942 19.667 1.00 49.57 ? 201 VAL A CG1 1 ATOM 1209 C CG2 . VAL A 1 147 ? 21.669 46.884 21.794 1.00 47.39 ? 201 VAL A CG2 1 ATOM 1210 N N . ILE A 1 148 ? 24.613 44.262 21.393 1.00 45.18 ? 202 ILE A N 1 ATOM 1211 C CA . ILE A 1 148 ? 25.087 43.421 22.470 1.00 43.12 ? 202 ILE A CA 1 ATOM 1212 C C . ILE A 1 148 ? 25.799 44.343 23.434 1.00 42.66 ? 202 ILE A C 1 ATOM 1213 O O . ILE A 1 148 ? 26.654 45.160 23.042 1.00 43.06 ? 202 ILE A O 1 ATOM 1214 C CB . ILE A 1 148 ? 25.953 42.225 21.988 1.00 44.42 ? 202 ILE A CB 1 ATOM 1215 C CG1 . ILE A 1 148 ? 26.455 41.398 23.177 1.00 43.61 ? 202 ILE A CG1 1 ATOM 1216 C CG2 . ILE A 1 148 ? 27.153 42.693 21.068 1.00 43.63 ? 202 ILE A CG2 1 ATOM 1217 C CD1 . ILE A 1 148 ? 26.759 39.940 22.822 1.00 40.55 ? 202 ILE A CD1 1 ATOM 1218 N N . ALA A 1 149 ? 25.394 44.270 24.696 1.00 39.56 ? 203 ALA A N 1 ATOM 1219 C CA . ALA A 1 149 ? 25.925 45.145 25.682 1.00 38.28 ? 203 ALA A CA 1 ATOM 1220 C C . ALA A 1 149 ? 26.329 44.336 26.881 1.00 37.45 ? 203 ALA A C 1 ATOM 1221 O O . ALA A 1 149 ? 25.738 43.290 27.177 1.00 36.47 ? 203 ALA A O 1 ATOM 1222 C CB . ALA A 1 149 ? 24.879 46.226 26.078 1.00 38.02 ? 203 ALA A CB 1 ATOM 1223 N N . ARG A 1 150 ? 27.359 44.813 27.557 1.00 37.47 ? 204 ARG A N 1 ATOM 1224 C CA . ARG A 1 150 ? 27.730 44.211 28.800 1.00 36.95 ? 204 ARG A CA 1 ATOM 1225 C C . ARG A 1 150 ? 26.985 44.876 29.948 1.00 35.95 ? 204 ARG A C 1 ATOM 1226 O O . ARG A 1 150 ? 26.739 46.112 29.957 1.00 34.91 ? 204 ARG A O 1 ATOM 1227 C CB . ARG A 1 150 ? 29.252 44.215 29.002 1.00 37.86 ? 204 ARG A CB 1 ATOM 1228 C CG . ARG A 1 150 ? 29.909 45.569 28.873 1.00 39.23 ? 204 ARG A CG 1 ATOM 1229 C CD . ARG A 1 150 ? 31.353 45.437 29.303 1.00 43.81 ? 204 ARG A CD 1 ATOM 1230 N NE . ARG A 1 150 ? 32.168 46.581 28.872 1.00 46.75 ? 204 ARG A NE 1 ATOM 1231 C CZ . ARG A 1 150 ? 33.402 46.814 29.303 1.00 48.06 ? 204 ARG A CZ 1 ATOM 1232 N NH1 . ARG A 1 150 ? 33.953 45.993 30.185 1.00 46.92 ? 204 ARG A NH1 1 ATOM 1233 N NH2 . ARG A 1 150 ? 34.074 47.884 28.874 1.00 47.41 ? 204 ARG A NH2 1 ATOM 1234 N N . TYR A 1 151 ? 26.627 44.035 30.919 1.00 33.84 ? 205 TYR A N 1 ATOM 1235 C CA . TYR A 1 151 ? 26.061 44.472 32.157 1.00 33.16 ? 205 TYR A CA 1 ATOM 1236 C C . TYR A 1 151 ? 27.060 45.352 32.885 1.00 34.87 ? 205 TYR A C 1 ATOM 1237 O O . TYR A 1 151 ? 28.300 45.202 32.701 1.00 33.98 ? 205 TYR A O 1 ATOM 1238 C CB . TYR A 1 151 ? 25.787 43.253 33.010 1.00 31.61 ? 205 TYR A CB 1 ATOM 1239 C CG . TYR A 1 151 ? 24.446 42.559 32.825 1.00 29.00 ? 205 TYR A CG 1 ATOM 1240 C CD1 . TYR A 1 151 ? 24.376 41.178 32.601 1.00 25.75 ? 205 TYR A CD1 1 ATOM 1241 C CD2 . TYR A 1 151 ? 23.240 43.272 32.975 1.00 25.23 ? 205 TYR A CD2 1 ATOM 1242 C CE1 . TYR A 1 151 ? 23.130 40.513 32.523 1.00 23.85 ? 205 TYR A CE1 1 ATOM 1243 C CE2 . TYR A 1 151 ? 22.012 42.634 32.918 1.00 29.13 ? 205 TYR A CE2 1 ATOM 1244 C CZ . TYR A 1 151 ? 21.951 41.262 32.708 1.00 28.24 ? 205 TYR A CZ 1 ATOM 1245 O OH . TYR A 1 151 ? 20.709 40.662 32.668 1.00 24.02 ? 205 TYR A OH 1 ATOM 1246 N N . GLY A 1 152 ? 26.522 46.260 33.705 1.00 34.30 ? 206 GLY A N 1 ATOM 1247 C CA . GLY A 1 152 ? 27.305 47.038 34.680 1.00 36.42 ? 206 GLY A CA 1 ATOM 1248 C C . GLY A 1 152 ? 27.111 48.541 34.474 1.00 37.12 ? 206 GLY A C 1 ATOM 1249 O O . GLY A 1 152 ? 26.571 48.972 33.449 1.00 36.20 ? 206 GLY A O 1 ATOM 1250 N N . LYS A 1 153 ? 27.551 49.311 35.461 1.00 38.27 ? 207 LYS A N 1 ATOM 1251 C CA . LYS A 1 153 ? 27.611 50.804 35.385 1.00 40.17 ? 207 LYS A CA 1 ATOM 1252 C C . LYS A 1 153 ? 26.270 51.422 35.689 1.00 39.74 ? 207 LYS A C 1 ATOM 1253 O O . LYS A 1 153 ? 26.185 52.333 36.543 1.00 41.77 ? 207 LYS A O 1 ATOM 1254 C CB . LYS A 1 153 ? 28.132 51.335 34.034 1.00 40.36 ? 207 LYS A CB 1 ATOM 1255 C CG . LYS A 1 153 ? 29.614 50.948 33.707 1.00 43.28 ? 207 LYS A CG 1 ATOM 1256 C CD . LYS A 1 153 ? 30.602 51.604 34.617 1.00 47.55 ? 207 LYS A CD 1 ATOM 1257 C CE . LYS A 1 153 ? 32.035 51.130 34.303 1.00 50.06 ? 207 LYS A CE 1 ATOM 1258 N NZ . LYS A 1 153 ? 32.874 51.318 35.528 1.00 52.12 ? 207 LYS A NZ 1 ATOM 1259 N N . VAL A 1 154 ? 25.229 50.931 35.004 1.00 38.41 ? 208 VAL A N 1 ATOM 1260 C CA . VAL A 1 154 ? 23.879 51.453 35.181 1.00 36.44 ? 208 VAL A CA 1 ATOM 1261 C C . VAL A 1 154 ? 22.843 50.340 35.153 1.00 35.25 ? 208 VAL A C 1 ATOM 1262 O O . VAL A 1 154 ? 23.099 49.220 34.685 1.00 32.63 ? 208 VAL A O 1 ATOM 1263 C CB . VAL A 1 154 ? 23.505 52.501 34.078 1.00 36.57 ? 208 VAL A CB 1 ATOM 1264 C CG1 . VAL A 1 154 ? 24.547 53.666 34.039 1.00 40.55 ? 208 VAL A CG1 1 ATOM 1265 C CG2 . VAL A 1 154 ? 23.384 51.850 32.719 1.00 35.08 ? 208 VAL A CG2 1 ATOM 1266 N N . PHE A 1 155 ? 21.642 50.698 35.590 1.00 32.64 ? 209 PHE A N 1 ATOM 1267 C CA . PHE A 1 155 ? 20.534 49.747 35.595 1.00 30.64 ? 209 PHE A CA 1 ATOM 1268 C C . PHE A 1 155 ? 20.245 49.177 34.224 1.00 29.42 ? 209 PHE A C 1 ATOM 1269 O O . PHE A 1 155 ? 20.190 49.904 33.222 1.00 29.81 ? 209 PHE A O 1 ATOM 1270 C CB . PHE A 1 155 ? 19.270 50.436 36.175 1.00 29.95 ? 209 PHE A CB 1 ATOM 1271 C CG . PHE A 1 155 ? 18.064 49.560 36.153 1.00 27.83 ? 209 PHE A CG 1 ATOM 1272 C CD1 . PHE A 1 155 ? 18.034 48.400 36.913 1.00 25.70 ? 209 PHE A CD1 1 ATOM 1273 C CD2 . PHE A 1 155 ? 16.908 49.935 35.424 1.00 30.74 ? 209 PHE A CD2 1 ATOM 1274 C CE1 . PHE A 1 155 ? 16.927 47.557 36.896 1.00 28.20 ? 209 PHE A CE1 1 ATOM 1275 C CE2 . PHE A 1 155 ? 15.796 49.085 35.404 1.00 31.74 ? 209 PHE A CE2 1 ATOM 1276 C CZ . PHE A 1 155 ? 15.807 47.893 36.175 1.00 28.02 ? 209 PHE A CZ 1 ATOM 1277 N N . ARG A 1 156 ? 20.059 47.854 34.152 1.00 27.89 ? 210 ARG A N 1 ATOM 1278 C CA . ARG A 1 156 ? 19.893 47.218 32.850 1.00 27.30 ? 210 ARG A CA 1 ATOM 1279 C C . ARG A 1 156 ? 18.713 47.716 32.013 1.00 28.44 ? 210 ARG A C 1 ATOM 1280 O O . ARG A 1 156 ? 18.756 47.658 30.788 1.00 28.07 ? 210 ARG A O 1 ATOM 1281 C CB . ARG A 1 156 ? 19.866 45.684 32.977 1.00 26.66 ? 210 ARG A CB 1 ATOM 1282 C CG . ARG A 1 156 ? 18.588 45.173 33.647 1.00 23.88 ? 210 ARG A CG 1 ATOM 1283 C CD . ARG A 1 156 ? 18.628 43.616 33.972 1.00 22.49 ? 210 ARG A CD 1 ATOM 1284 N NE . ARG A 1 156 ? 19.366 43.277 35.212 1.00 22.83 ? 210 ARG A NE 1 ATOM 1285 C CZ . ARG A 1 156 ? 18.943 43.520 36.456 1.00 27.35 ? 210 ARG A CZ 1 ATOM 1286 N NH1 . ARG A 1 156 ? 17.766 44.114 36.678 1.00 23.76 ? 210 ARG A NH1 1 ATOM 1287 N NH2 . ARG A 1 156 ? 19.673 43.140 37.499 1.00 24.50 ? 210 ARG A NH2 1 ATOM 1288 N N . GLY A 1 157 ? 17.647 48.184 32.671 1.00 28.47 ? 211 GLY A N 1 ATOM 1289 C CA . GLY A 1 157 ? 16.513 48.747 31.957 1.00 30.93 ? 211 GLY A CA 1 ATOM 1290 C C . GLY A 1 157 ? 16.878 50.030 31.200 1.00 32.61 ? 211 GLY A C 1 ATOM 1291 O O . GLY A 1 157 ? 16.380 50.252 30.086 1.00 32.07 ? 211 GLY A O 1 ATOM 1292 N N . ASN A 1 158 ? 17.756 50.831 31.805 1.00 33.39 ? 212 ASN A N 1 ATOM 1293 C CA . ASN A 1 158 ? 18.288 52.047 31.173 1.00 36.74 ? 212 ASN A CA 1 ATOM 1294 C C . ASN A 1 158 ? 19.042 51.686 29.884 1.00 36.96 ? 212 ASN A C 1 ATOM 1295 O O . ASN A 1 158 ? 18.901 52.397 28.893 1.00 38.35 ? 212 ASN A O 1 ATOM 1296 C CB . ASN A 1 158 ? 19.127 52.924 32.145 1.00 37.09 ? 212 ASN A CB 1 ATOM 1297 C CG . ASN A 1 158 ? 18.284 53.631 33.250 1.00 41.18 ? 212 ASN A CG 1 ATOM 1298 O OD1 . ASN A 1 158 ? 18.291 53.213 34.421 1.00 44.13 ? 212 ASN A OD1 1 ATOM 1299 N ND2 . ASN A 1 158 ? 17.640 54.746 32.905 1.00 43.70 ? 212 ASN A ND2 1 ATOM 1300 N N . LYS A 1 159 ? 19.770 50.553 29.870 1.00 36.93 ? 213 LYS A N 1 ATOM 1301 C CA . LYS A 1 159 ? 20.406 50.012 28.641 1.00 35.82 ? 213 LYS A CA 1 ATOM 1302 C C . LYS A 1 159 ? 19.392 49.726 27.529 1.00 36.33 ? 213 LYS A C 1 ATOM 1303 O O . LYS A 1 159 ? 19.612 50.098 26.371 1.00 36.44 ? 213 LYS A O 1 ATOM 1304 C CB . LYS A 1 159 ? 21.244 48.726 28.897 1.00 35.06 ? 213 LYS A CB 1 ATOM 1305 C CG . LYS A 1 159 ? 22.316 48.867 29.967 1.00 34.36 ? 213 LYS A CG 1 ATOM 1306 C CD . LYS A 1 159 ? 22.941 47.498 30.293 1.00 34.34 ? 213 LYS A CD 1 ATOM 1307 C CE . LYS A 1 159 ? 23.788 47.571 31.536 1.00 35.27 ? 213 LYS A CE 1 ATOM 1308 N NZ . LYS A 1 159 ? 25.174 48.093 31.227 1.00 36.97 ? 213 LYS A NZ 1 ATOM 1309 N N . VAL A 1 160 ? 18.290 49.049 27.866 1.00 34.89 ? 214 VAL A N 1 ATOM 1310 C CA . VAL A 1 160 ? 17.284 48.688 26.887 1.00 34.18 ? 214 VAL A CA 1 ATOM 1311 C C . VAL A 1 160 ? 16.548 49.977 26.388 1.00 35.74 ? 214 VAL A C 1 ATOM 1312 O O . VAL A 1 160 ? 16.217 50.065 25.202 1.00 36.81 ? 214 VAL A O 1 ATOM 1313 C CB . VAL A 1 160 ? 16.289 47.621 27.469 1.00 34.02 ? 214 VAL A CB 1 ATOM 1314 C CG1 . VAL A 1 160 ? 15.103 47.360 26.540 1.00 32.59 ? 214 VAL A CG1 1 ATOM 1315 C CG2 . VAL A 1 160 ? 17.032 46.272 27.801 1.00 30.61 ? 214 VAL A CG2 1 ATOM 1316 N N . LYS A 1 161 ? 16.304 50.932 27.292 1.00 37.12 ? 215 LYS A N 1 ATOM 1317 C CA . LYS A 1 161 ? 15.671 52.224 26.935 1.00 38.71 ? 215 LYS A CA 1 ATOM 1318 C C . LYS A 1 161 ? 16.606 52.963 25.987 1.00 40.26 ? 215 LYS A C 1 ATOM 1319 O O . LYS A 1 161 ? 16.172 53.399 24.908 1.00 40.04 ? 215 LYS A O 1 ATOM 1320 C CB . LYS A 1 161 ? 15.481 53.103 28.155 1.00 38.14 ? 215 LYS A CB 1 ATOM 1321 C CG . LYS A 1 161 ? 14.974 54.518 27.841 1.00 40.25 ? 215 LYS A CG 1 ATOM 1322 C CD . LYS A 1 161 ? 14.887 55.354 29.105 1.00 45.22 ? 215 LYS A CD 1 ATOM 1323 C CE . LYS A 1 161 ? 15.129 56.835 28.820 1.00 50.35 ? 215 LYS A CE 1 ATOM 1324 N NZ . LYS A 1 161 ? 13.925 57.611 29.233 1.00 53.18 ? 215 LYS A NZ 1 ATOM 1325 N N . ASN A 1 162 ? 17.879 53.084 26.411 1.00 40.46 ? 216 ASN A N 1 ATOM 1326 C CA . ASN A 1 162 ? 18.937 53.751 25.599 1.00 41.94 ? 216 ASN A CA 1 ATOM 1327 C C . ASN A 1 162 ? 19.028 53.077 24.231 1.00 42.57 ? 216 ASN A C 1 ATOM 1328 O O . ASN A 1 162 ? 19.058 53.767 23.214 1.00 43.80 ? 216 ASN A O 1 ATOM 1329 C CB . ASN A 1 162 ? 20.304 53.787 26.317 1.00 39.43 ? 216 ASN A CB 1 ATOM 1330 C CG . ASN A 1 162 ? 20.299 54.711 27.516 1.00 43.02 ? 216 ASN A CG 1 ATOM 1331 O OD1 . ASN A 1 162 ? 19.320 55.450 27.727 1.00 44.07 ? 216 ASN A OD1 1 ATOM 1332 N ND2 . ASN A 1 162 ? 21.379 54.690 28.318 1.00 42.14 ? 216 ASN A ND2 1 ATOM 1333 N N . ALA A 1 163 ? 19.046 51.742 24.199 1.00 43.81 ? 217 ALA A N 1 ATOM 1334 C CA . ALA A 1 163 ? 19.045 50.980 22.927 1.00 43.62 ? 217 ALA A CA 1 ATOM 1335 C C . ALA A 1 163 ? 17.834 51.235 22.053 1.00 44.57 ? 217 ALA A C 1 ATOM 1336 O O . ALA A 1 163 ? 17.953 51.360 20.811 1.00 45.31 ? 217 ALA A O 1 ATOM 1337 C CB . ALA A 1 163 ? 19.207 49.480 23.156 1.00 43.55 ? 217 ALA A CB 1 ATOM 1338 N N . GLN A 1 164 ? 16.658 51.257 22.676 1.00 44.93 ? 218 GLN A N 1 ATOM 1339 C CA . GLN A 1 164 ? 15.422 51.484 21.944 1.00 45.90 ? 218 GLN A CA 1 ATOM 1340 C C . GLN A 1 164 ? 15.485 52.822 21.226 1.00 46.18 ? 218 GLN A C 1 ATOM 1341 O O . GLN A 1 164 ? 15.150 52.907 20.055 1.00 45.66 ? 218 GLN A O 1 ATOM 1342 C CB . GLN A 1 164 ? 14.216 51.463 22.895 1.00 45.57 ? 218 GLN A CB 1 ATOM 1343 C CG . GLN A 1 164 ? 13.662 50.071 23.076 1.00 47.28 ? 218 GLN A CG 1 ATOM 1344 C CD . GLN A 1 164 ? 12.457 50.001 24.031 1.00 47.24 ? 218 GLN A CD 1 ATOM 1345 O OE1 . GLN A 1 164 ? 12.182 48.948 24.602 1.00 46.07 ? 218 GLN A OE1 1 ATOM 1346 N NE2 . GLN A 1 164 ? 11.730 51.111 24.173 1.00 48.26 ? 218 GLN A NE2 1 ATOM 1347 N N . LEU A 1 165 ? 15.916 53.857 21.956 1.00 47.33 ? 219 LEU A N 1 ATOM 1348 C CA . LEU A 1 165 ? 15.902 55.234 21.449 1.00 48.27 ? 219 LEU A CA 1 ATOM 1349 C C . LEU A 1 165 ? 16.915 55.432 20.337 1.00 49.27 ? 219 LEU A C 1 ATOM 1350 O O . LEU A 1 165 ? 16.714 56.291 19.474 1.00 49.60 ? 219 LEU A O 1 ATOM 1351 C CB . LEU A 1 165 ? 16.083 56.271 22.567 1.00 48.66 ? 219 LEU A CB 1 ATOM 1352 C CG . LEU A 1 165 ? 14.967 56.375 23.630 1.00 50.41 ? 219 LEU A CG 1 ATOM 1353 C CD1 . LEU A 1 165 ? 15.271 57.509 24.609 1.00 52.80 ? 219 LEU A CD1 1 ATOM 1354 C CD2 . LEU A 1 165 ? 13.530 56.502 23.064 1.00 50.92 ? 219 LEU A CD2 1 ATOM 1355 N N . ALA A 1 166 ? 17.979 54.622 20.341 1.00 49.06 ? 220 ALA A N 1 ATOM 1356 C CA . ALA A 1 166 ? 18.920 54.548 19.208 1.00 49.80 ? 220 ALA A CA 1 ATOM 1357 C C . ALA A 1 166 ? 18.432 53.636 18.059 1.00 49.57 ? 220 ALA A C 1 ATOM 1358 O O . ALA A 1 166 ? 19.161 53.399 17.095 1.00 50.28 ? 220 ALA A O 1 ATOM 1359 C CB . ALA A 1 166 ? 20.296 54.117 19.698 1.00 49.66 ? 220 ALA A CB 1 ATOM 1360 N N . GLY A 1 167 ? 17.213 53.111 18.165 1.00 49.17 ? 221 GLY A N 1 ATOM 1361 C CA . GLY A 1 167 ? 16.596 52.377 17.043 1.00 48.67 ? 221 GLY A CA 1 ATOM 1362 C C . GLY A 1 167 ? 16.870 50.893 16.872 1.00 49.03 ? 221 GLY A C 1 ATOM 1363 O O . GLY A 1 167 ? 16.446 50.287 15.878 1.00 48.69 ? 221 GLY A O 1 ATOM 1364 N N . ALA A 1 168 ? 17.549 50.282 17.851 1.00 49.01 ? 222 ALA A N 1 ATOM 1365 C CA . ALA A 1 168 ? 17.887 48.842 17.806 1.00 48.49 ? 222 ALA A CA 1 ATOM 1366 C C . ALA A 1 168 ? 16.639 47.951 17.743 1.00 48.14 ? 222 ALA A C 1 ATOM 1367 O O . ALA A 1 168 ? 15.530 48.370 18.174 1.00 47.83 ? 222 ALA A O 1 ATOM 1368 C CB . ALA A 1 168 ? 18.777 48.462 19.037 1.00 48.38 ? 222 ALA A CB 1 ATOM 1369 N N . LYS A 1 169 ? 16.796 46.735 17.221 1.00 47.00 ? 223 LYS A N 1 ATOM 1370 C CA . LYS A 1 169 ? 15.669 45.808 17.161 1.00 47.01 ? 223 LYS A CA 1 ATOM 1371 C C . LYS A 1 169 ? 15.767 44.613 18.127 1.00 45.63 ? 223 LYS A C 1 ATOM 1372 O O . LYS A 1 169 ? 14.913 43.720 18.124 1.00 45.00 ? 223 LYS A O 1 ATOM 1373 C CB . LYS A 1 169 ? 15.396 45.333 15.735 1.00 47.83 ? 223 LYS A CB 1 ATOM 1374 C CG . LYS A 1 169 ? 16.415 44.378 15.148 1.00 51.15 ? 223 LYS A CG 1 ATOM 1375 C CD . LYS A 1 169 ? 15.837 43.782 13.867 1.00 53.81 ? 223 LYS A CD 1 ATOM 1376 C CE . LYS A 1 169 ? 16.910 43.302 12.914 1.00 57.34 ? 223 LYS A CE 1 ATOM 1377 N NZ . LYS A 1 169 ? 16.266 42.582 11.774 1.00 56.48 ? 223 LYS A NZ 1 ATOM 1378 N N . GLY A 1 170 ? 16.807 44.620 18.947 1.00 44.38 ? 224 GLY A N 1 ATOM 1379 C CA . GLY A 1 170 ? 17.020 43.559 19.947 1.00 43.07 ? 224 GLY A CA 1 ATOM 1380 C C . GLY A 1 170 ? 18.200 43.920 20.819 1.00 42.01 ? 224 GLY A C 1 ATOM 1381 O O . GLY A 1 170 ? 19.096 44.681 20.392 1.00 42.05 ? 224 GLY A O 1 ATOM 1382 N N . VAL A 1 171 ? 18.201 43.408 22.056 1.00 39.98 ? 225 VAL A N 1 ATOM 1383 C CA . VAL A 1 171 ? 19.321 43.604 22.954 1.00 38.32 ? 225 VAL A CA 1 ATOM 1384 C C . VAL A 1 171 ? 19.740 42.242 23.523 1.00 38.10 ? 225 VAL A C 1 ATOM 1385 O O . VAL A 1 171 ? 18.901 41.425 23.920 1.00 37.17 ? 225 VAL A O 1 ATOM 1386 C CB . VAL A 1 171 ? 19.010 44.577 24.106 1.00 37.70 ? 225 VAL A CB 1 ATOM 1387 C CG1 . VAL A 1 171 ? 20.251 44.880 24.922 1.00 36.44 ? 225 VAL A CG1 1 ATOM 1388 C CG2 . VAL A 1 171 ? 18.387 45.896 23.576 1.00 38.04 ? 225 VAL A CG2 1 ATOM 1389 N N . ILE A 1 172 ? 21.050 42.012 23.532 1.00 37.21 ? 226 ILE A N 1 ATOM 1390 C CA . ILE A 1 172 ? 21.639 40.856 24.198 1.00 35.54 ? 226 ILE A CA 1 ATOM 1391 C C . ILE A 1 172 ? 22.494 41.424 25.310 1.00 34.85 ? 226 ILE A C 1 ATOM 1392 O O . ILE A 1 172 ? 23.341 42.291 25.070 1.00 34.96 ? 226 ILE A O 1 ATOM 1393 C CB . ILE A 1 172 ? 22.502 39.996 23.224 1.00 36.92 ? 226 ILE A CB 1 ATOM 1394 C CG1 . ILE A 1 172 ? 21.606 39.411 22.123 1.00 38.28 ? 226 ILE A CG1 1 ATOM 1395 C CG2 . ILE A 1 172 ? 23.238 38.902 24.013 1.00 33.34 ? 226 ILE A CG2 1 ATOM 1396 C CD1 . ILE A 1 172 ? 22.334 38.928 20.865 1.00 39.70 ? 226 ILE A CD1 1 ATOM 1397 N N . LEU A 1 173 ? 22.236 40.985 26.546 1.00 32.33 ? 227 LEU A N 1 ATOM 1398 C CA . LEU A 1 173 ? 23.001 41.442 27.685 1.00 31.19 ? 227 LEU A CA 1 ATOM 1399 C C . LEU A 1 173 ? 23.932 40.318 28.097 1.00 30.05 ? 227 LEU A C 1 ATOM 1400 O O . LEU A 1 173 ? 23.535 39.162 28.089 1.00 31.75 ? 227 LEU A O 1 ATOM 1401 C CB . LEU A 1 173 ? 22.069 41.759 28.874 1.00 29.84 ? 227 LEU A CB 1 ATOM 1402 C CG . LEU A 1 173 ? 21.052 42.875 28.561 1.00 31.13 ? 227 LEU A CG 1 ATOM 1403 C CD1 . LEU A 1 173 ? 19.894 42.963 29.628 1.00 29.88 ? 227 LEU A CD1 1 ATOM 1404 C CD2 . LEU A 1 173 ? 21.825 44.190 28.471 1.00 32.26 ? 227 LEU A CD2 1 ATOM 1405 N N . TYR A 1 174 ? 25.144 40.641 28.489 1.00 30.05 ? 228 TYR A N 1 ATOM 1406 C CA . TYR A 1 174 ? 26.023 39.559 28.971 1.00 29.37 ? 228 TYR A CA 1 ATOM 1407 C C . TYR A 1 174 ? 26.878 40.089 30.079 1.00 28.30 ? 228 TYR A C 1 ATOM 1408 O O . TYR A 1 174 ? 27.083 41.304 30.181 1.00 29.19 ? 228 TYR A O 1 ATOM 1409 C CB . TYR A 1 174 ? 26.859 38.925 27.832 1.00 29.87 ? 228 TYR A CB 1 ATOM 1410 C CG . TYR A 1 174 ? 28.062 39.751 27.501 1.00 31.67 ? 228 TYR A CG 1 ATOM 1411 C CD1 . TYR A 1 174 ? 29.316 39.459 28.064 1.00 33.36 ? 228 TYR A CD1 1 ATOM 1412 C CD2 . TYR A 1 174 ? 27.948 40.850 26.666 1.00 35.06 ? 228 TYR A CD2 1 ATOM 1413 C CE1 . TYR A 1 174 ? 30.448 40.253 27.749 1.00 36.06 ? 228 TYR A CE1 1 ATOM 1414 C CE2 . TYR A 1 174 ? 29.053 41.652 26.369 1.00 36.38 ? 228 TYR A CE2 1 ATOM 1415 C CZ . TYR A 1 174 ? 30.290 41.347 26.908 1.00 38.25 ? 228 TYR A CZ 1 ATOM 1416 O OH . TYR A 1 174 ? 31.364 42.170 26.617 1.00 40.08 ? 228 TYR A OH 1 ATOM 1417 N N . SER A 1 175 ? 27.406 39.191 30.911 1.00 28.52 ? 229 SER A N 1 ATOM 1418 C CA . SER A 1 175 ? 28.316 39.578 31.981 1.00 27.73 ? 229 SER A CA 1 ATOM 1419 C C . SER A 1 175 ? 29.784 39.395 31.526 1.00 29.46 ? 229 SER A C 1 ATOM 1420 O O . SER A 1 175 ? 30.235 38.260 31.299 1.00 28.26 ? 229 SER A O 1 ATOM 1421 C CB . SER A 1 175 ? 28.048 38.728 33.250 1.00 28.45 ? 229 SER A CB 1 ATOM 1422 O OG . SER A 1 175 ? 26.698 38.868 33.721 1.00 29.11 ? 229 SER A OG 1 ATOM 1423 N N . ASP A 1 176 ? 30.510 40.500 31.407 1.00 29.86 ? 230 ASP A N 1 ATOM 1424 C CA . ASP A 1 176 ? 31.938 40.437 31.033 1.00 32.19 ? 230 ASP A CA 1 ATOM 1425 C C . ASP A 1 176 ? 32.778 40.185 32.289 1.00 32.59 ? 230 ASP A C 1 ATOM 1426 O O . ASP A 1 176 ? 32.524 40.783 33.331 1.00 32.77 ? 230 ASP A O 1 ATOM 1427 C CB . ASP A 1 176 ? 32.358 41.736 30.319 1.00 32.38 ? 230 ASP A CB 1 ATOM 1428 C CG . ASP A 1 176 ? 33.664 41.574 29.543 1.00 34.46 ? 230 ASP A CG 1 ATOM 1429 O OD1 . ASP A 1 176 ? 33.605 41.573 28.312 1.00 34.55 ? 230 ASP A OD1 1 ATOM 1430 O OD2 . ASP A 1 176 ? 34.694 41.380 30.186 1.00 35.77 ? 230 ASP A OD2 1 ATOM 1431 N N . PRO A 1 177 ? 33.800 39.272 32.202 1.00 33.64 ? 231 PRO A N 1 ATOM 1432 C CA . PRO A 1 177 ? 34.668 39.019 33.338 1.00 34.38 ? 231 PRO A CA 1 ATOM 1433 C C . PRO A 1 177 ? 35.364 40.288 33.827 1.00 34.23 ? 231 PRO A C 1 ATOM 1434 O O . PRO A 1 177 ? 35.746 40.346 34.978 1.00 34.48 ? 231 PRO A O 1 ATOM 1435 C CB . PRO A 1 177 ? 35.709 38.022 32.792 1.00 35.79 ? 231 PRO A CB 1 ATOM 1436 C CG . PRO A 1 177 ? 35.001 37.335 31.680 1.00 35.28 ? 231 PRO A CG 1 ATOM 1437 C CD . PRO A 1 177 ? 34.052 38.343 31.085 1.00 34.15 ? 231 PRO A CD 1 ATOM 1438 N N . ALA A 1 178 ? 35.535 41.303 32.978 1.00 35.83 ? 232 ALA A N 1 ATOM 1439 C CA . ALA A 1 178 ? 36.171 42.555 33.450 1.00 36.70 ? 232 ALA A CA 1 ATOM 1440 C C . ALA A 1 178 ? 35.391 43.173 34.604 1.00 37.72 ? 232 ALA A C 1 ATOM 1441 O O . ALA A 1 178 ? 35.961 43.707 35.582 1.00 37.37 ? 232 ALA A O 1 ATOM 1442 C CB . ALA A 1 178 ? 36.306 43.550 32.301 1.00 38.31 ? 232 ALA A CB 1 ATOM 1443 N N . ASP A 1 179 ? 34.070 43.017 34.536 1.00 36.87 ? 233 ASP A N 1 ATOM 1444 C CA . ASP A 1 179 ? 33.177 43.586 35.526 1.00 37.51 ? 233 ASP A CA 1 ATOM 1445 C C . ASP A 1 179 ? 32.732 42.596 36.596 1.00 37.18 ? 233 ASP A C 1 ATOM 1446 O O . ASP A 1 179 ? 32.465 43.007 37.728 1.00 38.12 ? 233 ASP A O 1 ATOM 1447 C CB . ASP A 1 179 ? 31.961 44.156 34.804 1.00 37.08 ? 233 ASP A CB 1 ATOM 1448 C CG . ASP A 1 179 ? 32.342 45.063 33.648 1.00 36.70 ? 233 ASP A CG 1 ATOM 1449 O OD1 . ASP A 1 179 ? 32.730 46.226 33.912 1.00 39.33 ? 233 ASP A OD1 1 ATOM 1450 O OD2 . ASP A 1 179 ? 32.231 44.626 32.481 1.00 37.07 ? 233 ASP A OD2 1 ATOM 1451 N N . TYR A 1 180 ? 32.663 41.301 36.270 1.00 34.56 ? 234 TYR A N 1 ATOM 1452 C CA . TYR A 1 180 ? 32.047 40.332 37.173 1.00 33.29 ? 234 TYR A CA 1 ATOM 1453 C C . TYR A 1 180 ? 32.933 39.162 37.614 1.00 34.39 ? 234 TYR A C 1 ATOM 1454 O O . TYR A 1 180 ? 32.415 38.118 38.069 1.00 34.38 ? 234 TYR A O 1 ATOM 1455 C CB . TYR A 1 180 ? 30.761 39.783 36.537 1.00 32.43 ? 234 TYR A CB 1 ATOM 1456 C CG . TYR A 1 180 ? 29.635 40.822 36.526 1.00 30.94 ? 234 TYR A CG 1 ATOM 1457 C CD1 . TYR A 1 180 ? 29.373 41.586 35.393 1.00 30.38 ? 234 TYR A CD1 1 ATOM 1458 C CD2 . TYR A 1 180 ? 28.903 41.089 37.698 1.00 29.58 ? 234 TYR A CD2 1 ATOM 1459 C CE1 . TYR A 1 180 ? 28.358 42.598 35.398 1.00 29.62 ? 234 TYR A CE1 1 ATOM 1460 C CE2 . TYR A 1 180 ? 27.849 42.090 37.727 1.00 28.12 ? 234 TYR A CE2 1 ATOM 1461 C CZ . TYR A 1 180 ? 27.597 42.820 36.574 1.00 30.89 ? 234 TYR A CZ 1 ATOM 1462 O OH . TYR A 1 180 ? 26.608 43.779 36.594 1.00 27.57 ? 234 TYR A OH 1 ATOM 1463 N N . PHE A 1 181 ? 34.247 39.265 37.402 1.00 34.39 ? 235 PHE A N 1 ATOM 1464 C CA . PHE A 1 181 ? 35.114 38.152 37.763 1.00 35.11 ? 235 PHE A CA 1 ATOM 1465 C C . PHE A 1 181 ? 36.244 38.794 38.509 1.00 36.00 ? 235 PHE A C 1 ATOM 1466 O O . PHE A 1 181 ? 37.016 39.543 37.908 1.00 36.85 ? 235 PHE A O 1 ATOM 1467 C CB . PHE A 1 181 ? 35.608 37.429 36.511 1.00 35.08 ? 235 PHE A CB 1 ATOM 1468 C CG . PHE A 1 181 ? 36.332 36.126 36.790 1.00 34.39 ? 235 PHE A CG 1 ATOM 1469 C CD1 . PHE A 1 181 ? 35.633 34.920 36.833 1.00 31.67 ? 235 PHE A CD1 1 ATOM 1470 C CD2 . PHE A 1 181 ? 37.732 36.121 37.012 1.00 36.27 ? 235 PHE A CD2 1 ATOM 1471 C CE1 . PHE A 1 181 ? 36.321 33.714 37.111 1.00 33.50 ? 235 PHE A CE1 1 ATOM 1472 C CE2 . PHE A 1 181 ? 38.413 34.925 37.276 1.00 33.91 ? 235 PHE A CE2 1 ATOM 1473 C CZ . PHE A 1 181 ? 37.716 33.729 37.316 1.00 34.65 ? 235 PHE A CZ 1 ATOM 1474 N N . ALA A 1 182 ? 36.334 38.541 39.806 1.00 36.24 ? 236 ALA A N 1 ATOM 1475 C CA . ALA A 1 182 ? 37.372 39.164 40.606 1.00 38.18 ? 236 ALA A CA 1 ATOM 1476 C C . ALA A 1 182 ? 38.699 38.439 40.367 1.00 39.84 ? 236 ALA A C 1 ATOM 1477 O O . ALA A 1 182 ? 38.713 37.215 40.336 1.00 39.07 ? 236 ALA A O 1 ATOM 1478 C CB . ALA A 1 182 ? 36.986 39.133 42.091 1.00 38.12 ? 236 ALA A CB 1 ATOM 1479 N N . PRO A 1 183 ? 39.812 39.187 40.163 1.00 42.12 ? 237 PRO A N 1 ATOM 1480 C CA . PRO A 1 183 ? 41.114 38.538 39.944 1.00 42.62 ? 237 PRO A CA 1 ATOM 1481 C C . PRO A 1 183 ? 41.479 37.576 41.064 1.00 42.82 ? 237 PRO A C 1 ATOM 1482 O O . PRO A 1 183 ? 41.344 37.899 42.259 1.00 42.73 ? 237 PRO A O 1 ATOM 1483 C CB . PRO A 1 183 ? 42.087 39.729 39.916 1.00 44.10 ? 237 PRO A CB 1 ATOM 1484 C CG . PRO A 1 183 ? 41.233 40.847 39.359 1.00 44.76 ? 237 PRO A CG 1 ATOM 1485 C CD . PRO A 1 183 ? 39.902 40.655 40.015 1.00 42.71 ? 237 PRO A CD 1 ATOM 1486 N N . GLY A 1 184 ? 41.898 36.375 40.680 1.00 42.74 ? 238 GLY A N 1 ATOM 1487 C CA . GLY A 1 184 ? 42.493 35.438 41.637 1.00 42.79 ? 238 GLY A CA 1 ATOM 1488 C C . GLY A 1 184 ? 41.554 34.728 42.598 1.00 42.18 ? 238 GLY A C 1 ATOM 1489 O O . GLY A 1 184 ? 42.008 34.128 43.574 1.00 43.34 ? 238 GLY A O 1 ATOM 1490 N N . VAL A 1 185 ? 40.248 34.787 42.334 1.00 39.77 ? 239 VAL A N 1 ATOM 1491 C CA . VAL A 1 185 ? 39.268 34.053 43.149 1.00 36.63 ? 239 VAL A CA 1 ATOM 1492 C C . VAL A 1 185 ? 38.686 32.957 42.283 1.00 35.26 ? 239 VAL A C 1 ATOM 1493 O O . VAL A 1 185 ? 38.473 33.155 41.107 1.00 35.16 ? 239 VAL A O 1 ATOM 1494 C CB . VAL A 1 185 ? 38.147 34.998 43.726 1.00 36.96 ? 239 VAL A CB 1 ATOM 1495 C CG1 A VAL A 1 185 ? 37.987 36.196 42.878 0.50 37.24 ? 239 VAL A CG1 1 ATOM 1496 C CG1 B VAL A 1 185 ? 37.003 34.203 44.381 0.50 33.64 ? 239 VAL A CG1 1 ATOM 1497 C CG2 A VAL A 1 185 ? 36.827 34.261 43.944 0.50 33.76 ? 239 VAL A CG2 1 ATOM 1498 C CG2 B VAL A 1 185 ? 38.743 36.063 44.684 0.50 34.29 ? 239 VAL A CG2 1 ATOM 1499 N N A LYS A 1 186 ? 38.464 31.778 42.849 0.50 35.66 ? 240 LYS A N 1 ATOM 1500 N N B LYS A 1 186 ? 38.410 31.825 42.917 0.50 35.58 ? 240 LYS A N 1 ATOM 1501 C CA A LYS A 1 186 ? 37.978 30.672 42.036 0.50 35.65 ? 240 LYS A CA 1 ATOM 1502 C CA B LYS A 1 186 ? 37.877 30.641 42.270 0.50 35.71 ? 240 LYS A CA 1 ATOM 1503 C C A LYS A 1 186 ? 36.459 30.766 41.926 0.50 35.63 ? 240 LYS A C 1 ATOM 1504 C C B LYS A 1 186 ? 36.412 30.878 41.906 0.50 35.63 ? 240 LYS A C 1 ATOM 1505 O O A LYS A 1 186 ? 35.787 31.258 42.850 0.50 34.61 ? 240 LYS A O 1 ATOM 1506 O O B LYS A 1 186 ? 35.727 31.601 42.637 0.50 34.79 ? 240 LYS A O 1 ATOM 1507 C CB A LYS A 1 186 ? 38.397 29.299 42.593 0.50 36.97 ? 240 LYS A CB 1 ATOM 1508 C CB B LYS A 1 186 ? 38.001 29.457 43.241 0.50 36.40 ? 240 LYS A CB 1 ATOM 1509 C CG A LYS A 1 186 ? 39.904 28.981 42.560 0.50 35.73 ? 240 LYS A CG 1 ATOM 1510 C CG B LYS A 1 186 ? 39.469 29.184 43.688 0.50 36.78 ? 240 LYS A CG 1 ATOM 1511 C CD A LYS A 1 186 ? 40.532 29.022 41.151 0.50 38.41 ? 240 LYS A CD 1 ATOM 1512 C CD B LYS A 1 186 ? 39.628 27.851 44.378 0.50 39.28 ? 240 LYS A CD 1 ATOM 1513 C CE A LYS A 1 186 ? 41.679 27.989 41.030 0.50 39.93 ? 240 LYS A CE 1 ATOM 1514 C CE B LYS A 1 186 ? 41.035 27.696 44.968 0.50 41.82 ? 240 LYS A CE 1 ATOM 1515 N NZ A LYS A 1 186 ? 42.543 28.193 39.822 0.50 41.83 ? 240 LYS A NZ 1 ATOM 1516 N NZ B LYS A 1 186 ? 41.622 26.426 44.496 0.50 42.24 ? 240 LYS A NZ 1 ATOM 1517 N N . SER A 1 187 ? 35.960 30.316 40.780 1.00 34.79 ? 241 SER A N 1 ATOM 1518 C CA . SER A 1 187 ? 34.533 30.324 40.424 1.00 35.56 ? 241 SER A CA 1 ATOM 1519 C C . SER A 1 187 ? 33.750 29.321 41.234 1.00 34.59 ? 241 SER A C 1 ATOM 1520 O O . SER A 1 187 ? 34.283 28.272 41.651 1.00 34.75 ? 241 SER A O 1 ATOM 1521 C CB . SER A 1 187 ? 34.360 29.970 38.958 1.00 37.16 ? 241 SER A CB 1 ATOM 1522 O OG . SER A 1 187 ? 35.153 30.821 38.176 1.00 42.36 ? 241 SER A OG 1 ATOM 1523 N N . TYR A 1 188 ? 32.464 29.632 41.433 1.00 32.24 ? 242 TYR A N 1 ATOM 1524 C CA . TYR A 1 188 ? 31.564 28.751 42.144 1.00 31.91 ? 242 TYR A CA 1 ATOM 1525 C C . TYR A 1 188 ? 31.608 27.351 41.502 1.00 31.46 ? 242 TYR A C 1 ATOM 1526 O O . TYR A 1 188 ? 31.574 27.244 40.280 1.00 31.36 ? 242 TYR A O 1 ATOM 1527 C CB . TYR A 1 188 ? 30.116 29.329 42.138 1.00 30.19 ? 242 TYR A CB 1 ATOM 1528 C CG . TYR A 1 188 ? 29.273 28.724 43.225 1.00 28.47 ? 242 TYR A CG 1 ATOM 1529 C CD1 . TYR A 1 188 ? 29.373 29.173 44.557 1.00 28.62 ? 242 TYR A CD1 1 ATOM 1530 C CD2 . TYR A 1 188 ? 28.426 27.646 42.939 1.00 29.51 ? 242 TYR A CD2 1 ATOM 1531 C CE1 . TYR A 1 188 ? 28.649 28.560 45.572 1.00 29.50 ? 242 TYR A CE1 1 ATOM 1532 C CE2 . TYR A 1 188 ? 27.670 27.036 43.946 1.00 31.99 ? 242 TYR A CE2 1 ATOM 1533 C CZ . TYR A 1 188 ? 27.795 27.514 45.264 1.00 31.55 ? 242 TYR A CZ 1 ATOM 1534 O OH . TYR A 1 188 ? 27.044 26.891 46.222 1.00 37.15 ? 242 TYR A OH 1 ATOM 1535 N N . PRO A 1 189 ? 31.603 26.280 42.318 1.00 32.61 ? 243 PRO A N 1 ATOM 1536 C CA . PRO A 1 189 ? 31.376 26.145 43.750 1.00 32.74 ? 243 PRO A CA 1 ATOM 1537 C C . PRO A 1 189 ? 32.609 26.231 44.667 1.00 33.42 ? 243 PRO A C 1 ATOM 1538 O O . PRO A 1 189 ? 32.486 25.987 45.869 1.00 34.24 ? 243 PRO A O 1 ATOM 1539 C CB . PRO A 1 189 ? 30.774 24.748 43.843 1.00 32.52 ? 243 PRO A CB 1 ATOM 1540 C CG . PRO A 1 189 ? 31.559 23.976 42.830 1.00 33.30 ? 243 PRO A CG 1 ATOM 1541 C CD . PRO A 1 189 ? 31.697 24.944 41.662 1.00 34.21 ? 243 PRO A CD 1 ATOM 1542 N N . ASP A 1 190 ? 33.760 26.566 44.118 1.00 33.23 ? 244 ASP A N 1 ATOM 1543 C CA . ASP A 1 190 ? 35.003 26.543 44.902 1.00 34.70 ? 244 ASP A CA 1 ATOM 1544 C C . ASP A 1 190 ? 35.441 27.922 45.349 1.00 34.29 ? 244 ASP A C 1 ATOM 1545 O O . ASP A 1 190 ? 36.434 28.071 46.077 1.00 33.55 ? 244 ASP A O 1 ATOM 1546 C CB . ASP A 1 190 ? 36.131 25.839 44.130 1.00 36.31 ? 244 ASP A CB 1 ATOM 1547 C CG . ASP A 1 190 ? 35.726 24.439 43.665 1.00 39.37 ? 244 ASP A CG 1 ATOM 1548 O OD1 . ASP A 1 190 ? 35.329 23.623 44.548 1.00 41.45 ? 244 ASP A OD1 1 ATOM 1549 O OD2 . ASP A 1 190 ? 35.736 24.199 42.417 1.00 43.29 ? 244 ASP A OD2 1 ATOM 1550 N N . GLY A 1 191 ? 34.654 28.933 44.960 1.00 32.66 ? 245 GLY A N 1 ATOM 1551 C CA . GLY A 1 191 ? 34.925 30.295 45.349 1.00 31.89 ? 245 GLY A CA 1 ATOM 1552 C C . GLY A 1 191 ? 33.714 31.130 44.961 1.00 31.21 ? 245 GLY A C 1 ATOM 1553 O O . GLY A 1 191 ? 32.710 30.564 44.501 1.00 30.73 ? 245 GLY A O 1 ATOM 1554 N N . TRP A 1 192 ? 33.818 32.451 45.111 1.00 29.92 ? 246 TRP A N 1 ATOM 1555 C CA . TRP A 1 192 ? 32.641 33.319 44.858 1.00 29.85 ? 246 TRP A CA 1 ATOM 1556 C C . TRP A 1 192 ? 32.567 34.013 43.486 1.00 30.47 ? 246 TRP A C 1 ATOM 1557 O O . TRP A 1 192 ? 31.746 34.938 43.270 1.00 28.89 ? 246 TRP A O 1 ATOM 1558 C CB . TRP A 1 192 ? 32.475 34.308 46.017 1.00 30.05 ? 246 TRP A CB 1 ATOM 1559 C CG . TRP A 1 192 ? 33.719 35.106 46.384 1.00 32.78 ? 246 TRP A CG 1 ATOM 1560 C CD1 . TRP A 1 192 ? 34.652 34.780 47.338 1.00 35.61 ? 246 TRP A CD1 1 ATOM 1561 C CD2 . TRP A 1 192 ? 34.127 36.361 45.833 1.00 34.13 ? 246 TRP A CD2 1 ATOM 1562 N NE1 . TRP A 1 192 ? 35.607 35.779 47.419 1.00 36.67 ? 246 TRP A NE1 1 ATOM 1563 C CE2 . TRP A 1 192 ? 35.321 36.746 46.496 1.00 33.19 ? 246 TRP A CE2 1 ATOM 1564 C CE3 . TRP A 1 192 ? 33.608 37.204 44.833 1.00 34.24 ? 246 TRP A CE3 1 ATOM 1565 C CZ2 . TRP A 1 192 ? 35.990 37.940 46.210 1.00 34.15 ? 246 TRP A CZ2 1 ATOM 1566 C CZ3 . TRP A 1 192 ? 34.276 38.403 44.555 1.00 36.04 ? 246 TRP A CZ3 1 ATOM 1567 C CH2 . TRP A 1 192 ? 35.476 38.744 45.223 1.00 34.69 ? 246 TRP A CH2 1 ATOM 1568 N N . ASN A 1 193 ? 33.372 33.536 42.524 1.00 29.12 ? 247 ASN A N 1 ATOM 1569 C CA . ASN A 1 193 ? 33.392 34.120 41.206 1.00 30.59 ? 247 ASN A CA 1 ATOM 1570 C C . ASN A 1 193 ? 32.367 33.512 40.303 1.00 29.51 ? 247 ASN A C 1 ATOM 1571 O O . ASN A 1 193 ? 31.869 32.429 40.606 1.00 29.27 ? 247 ASN A O 1 ATOM 1572 C CB . ASN A 1 193 ? 34.779 33.989 40.549 1.00 30.93 ? 247 ASN A CB 1 ATOM 1573 C CG . ASN A 1 193 ? 35.475 35.313 40.412 1.00 34.02 ? 247 ASN A CG 1 ATOM 1574 O OD1 . ASN A 1 193 ? 34.838 36.367 40.509 1.00 34.24 ? 247 ASN A OD1 1 ATOM 1575 N ND2 . ASN A 1 193 ? 36.802 35.287 40.174 1.00 30.92 ? 247 ASN A ND2 1 ATOM 1576 N N . LEU A 1 194 ? 32.076 34.228 39.207 1.00 29.52 ? 248 LEU A N 1 ATOM 1577 C CA . LEU A 1 194 ? 31.073 33.859 38.233 1.00 28.51 ? 248 LEU A CA 1 ATOM 1578 C C . LEU A 1 194 ? 31.702 32.892 37.235 1.00 29.74 ? 248 LEU A C 1 ATOM 1579 O O . LEU A 1 194 ? 32.705 33.230 36.609 1.00 30.29 ? 248 LEU A O 1 ATOM 1580 C CB . LEU A 1 194 ? 30.591 35.088 37.473 1.00 28.13 ? 248 LEU A CB 1 ATOM 1581 C CG . LEU A 1 194 ? 29.517 34.926 36.404 1.00 28.06 ? 248 LEU A CG 1 ATOM 1582 C CD1 . LEU A 1 194 ? 28.158 34.430 36.921 1.00 27.72 ? 248 LEU A CD1 1 ATOM 1583 C CD2 . LEU A 1 194 ? 29.334 36.262 35.651 1.00 26.75 ? 248 LEU A CD2 1 ATOM 1584 N N . PRO A 1 195 ? 31.128 31.692 37.110 1.00 29.50 ? 249 PRO A N 1 ATOM 1585 C CA . PRO A 1 195 ? 31.623 30.807 36.051 1.00 30.42 ? 249 PRO A CA 1 ATOM 1586 C C . PRO A 1 195 ? 31.071 31.260 34.711 1.00 30.89 ? 249 PRO A C 1 ATOM 1587 O O . PRO A 1 195 ? 30.052 31.974 34.663 1.00 29.88 ? 249 PRO A O 1 ATOM 1588 C CB . PRO A 1 195 ? 31.062 29.425 36.437 1.00 31.25 ? 249 PRO A CB 1 ATOM 1589 C CG . PRO A 1 195 ? 29.991 29.645 37.384 1.00 31.06 ? 249 PRO A CG 1 ATOM 1590 C CD . PRO A 1 195 ? 30.139 31.040 37.988 1.00 29.48 ? 249 PRO A CD 1 ATOM 1591 N N . GLY A 1 196 ? 31.685 30.788 33.617 1.00 29.79 ? 250 GLY A N 1 ATOM 1592 C CA . GLY A 1 196 ? 31.253 31.150 32.260 1.00 28.61 ? 250 GLY A CA 1 ATOM 1593 C C . GLY A 1 196 ? 29.841 30.809 31.833 1.00 27.85 ? 250 GLY A C 1 ATOM 1594 O O . GLY A 1 196 ? 29.346 31.393 30.857 1.00 29.16 ? 250 GLY A O 1 ATOM 1595 N N . GLY A 1 197 ? 29.219 29.859 32.530 1.00 26.23 ? 251 GLY A N 1 ATOM 1596 C CA . GLY A 1 197 ? 27.845 29.457 32.277 1.00 26.67 ? 251 GLY A CA 1 ATOM 1597 C C . GLY A 1 197 ? 26.842 30.229 33.154 1.00 25.89 ? 251 GLY A C 1 ATOM 1598 O O . GLY A 1 197 ? 25.633 30.073 32.972 1.00 26.44 ? 251 GLY A O 1 ATOM 1599 N N . GLY A 1 198 ? 27.339 31.032 34.086 1.00 26.72 ? 252 GLY A N 1 ATOM 1600 C CA . GLY A 1 198 ? 26.445 31.795 35.023 1.00 25.35 ? 252 GLY A CA 1 ATOM 1601 C C . GLY A 1 198 ? 25.809 32.953 34.278 1.00 26.14 ? 252 GLY A C 1 ATOM 1602 O O . GLY A 1 198 ? 26.434 33.521 33.366 1.00 25.72 ? 252 GLY A O 1 ATOM 1603 N N . VAL A 1 199 ? 24.591 33.369 34.684 1.00 25.00 ? 253 VAL A N 1 ATOM 1604 C CA . VAL A 1 199 ? 23.874 34.409 33.923 1.00 23.93 ? 253 VAL A CA 1 ATOM 1605 C C . VAL A 1 199 ? 23.110 35.268 34.935 1.00 24.11 ? 253 VAL A C 1 ATOM 1606 O O . VAL A 1 199 ? 22.524 34.751 35.872 1.00 24.83 ? 253 VAL A O 1 ATOM 1607 C CB . VAL A 1 199 ? 22.820 33.838 32.922 1.00 24.44 ? 253 VAL A CB 1 ATOM 1608 C CG1 . VAL A 1 199 ? 22.164 34.977 32.145 1.00 24.04 ? 253 VAL A CG1 1 ATOM 1609 C CG2 . VAL A 1 199 ? 23.447 32.812 31.902 1.00 25.20 ? 253 VAL A CG2 1 ATOM 1610 N N . GLN A 1 200 ? 23.161 36.574 34.722 1.00 23.48 ? 254 GLN A N 1 ATOM 1611 C CA . GLN A 1 200 ? 22.447 37.516 35.584 1.00 23.21 ? 254 GLN A CA 1 ATOM 1612 C C . GLN A 1 200 ? 21.029 37.669 35.061 1.00 22.73 ? 254 GLN A C 1 ATOM 1613 O O . GLN A 1 200 ? 20.826 38.222 33.978 1.00 22.73 ? 254 GLN A O 1 ATOM 1614 C CB . GLN A 1 200 ? 23.156 38.868 35.525 1.00 23.44 ? 254 GLN A CB 1 ATOM 1615 C CG . GLN A 1 200 ? 22.438 39.945 36.435 1.00 24.38 ? 254 GLN A CG 1 ATOM 1616 C CD . GLN A 1 200 ? 23.013 41.344 36.226 1.00 24.68 ? 254 GLN A CD 1 ATOM 1617 O OE1 . GLN A 1 200 ? 22.248 42.347 36.203 1.00 22.82 ? 254 GLN A OE1 1 ATOM 1618 N NE2 . GLN A 1 200 ? 24.363 41.434 36.109 1.00 22.92 ? 254 GLN A NE2 1 ATOM 1619 N N . ARG A 1 201 ? 20.057 37.179 35.824 1.00 21.68 ? 255 ARG A N 1 ATOM 1620 C CA . ARG A 1 201 ? 18.651 37.560 35.563 1.00 22.32 ? 255 ARG A CA 1 ATOM 1621 C C . ARG A 1 201 ? 18.361 39.031 35.883 1.00 21.75 ? 255 ARG A C 1 ATOM 1622 O O . ARG A 1 201 ? 19.140 39.713 36.529 1.00 21.12 ? 255 ARG A O 1 ATOM 1623 C CB . ARG A 1 201 ? 17.688 36.661 36.372 1.00 22.25 ? 255 ARG A CB 1 ATOM 1624 C CG . ARG A 1 201 ? 17.734 35.184 35.914 1.00 21.97 ? 255 ARG A CG 1 ATOM 1625 C CD . ARG A 1 201 ? 17.295 34.243 37.049 1.00 22.30 ? 255 ARG A CD 1 ATOM 1626 N NE . ARG A 1 201 ? 17.437 32.818 36.684 1.00 24.31 ? 255 ARG A NE 1 ATOM 1627 C CZ . ARG A 1 201 ? 18.604 32.197 36.645 1.00 26.52 ? 255 ARG A CZ 1 ATOM 1628 N NH1 . ARG A 1 201 ? 19.704 32.883 36.910 1.00 23.88 ? 255 ARG A NH1 1 ATOM 1629 N NH2 . ARG A 1 201 ? 18.682 30.921 36.301 1.00 25.70 ? 255 ARG A NH2 1 ATOM 1630 N N . GLY A 1 202 ? 17.163 39.481 35.517 1.00 22.90 ? 256 GLY A N 1 ATOM 1631 C CA . GLY A 1 202 ? 16.751 40.814 35.977 1.00 21.49 ? 256 GLY A CA 1 ATOM 1632 C C . GLY A 1 202 ? 15.718 41.474 35.116 1.00 21.87 ? 256 GLY A C 1 ATOM 1633 O O . GLY A 1 202 ? 15.696 41.282 33.869 1.00 21.02 ? 256 GLY A O 1 ATOM 1634 N N . ASN A 1 203 ? 14.830 42.265 35.746 1.00 22.19 ? 257 ASN A N 1 ATOM 1635 C CA . ASN A 1 203 ? 13.832 42.931 34.896 1.00 22.04 ? 257 ASN A CA 1 ATOM 1636 C C . ASN A 1 203 ? 14.483 44.082 34.132 1.00 21.84 ? 257 ASN A C 1 ATOM 1637 O O . ASN A 1 203 ? 15.508 44.631 34.545 1.00 20.96 ? 257 ASN A O 1 ATOM 1638 C CB . ASN A 1 203 ? 12.615 43.462 35.710 1.00 21.99 ? 257 ASN A CB 1 ATOM 1639 C CG . ASN A 1 203 ? 12.894 44.790 36.417 1.00 24.16 ? 257 ASN A CG 1 ATOM 1640 O OD1 . ASN A 1 203 ? 12.927 45.835 35.790 1.00 27.25 ? 257 ASN A OD1 1 ATOM 1641 N ND2 . ASN A 1 203 ? 13.053 44.750 37.758 1.00 24.74 ? 257 ASN A ND2 1 ATOM 1642 N N . ILE A 1 204 ? 13.826 44.473 33.045 1.00 21.94 ? 258 ILE A N 1 ATOM 1643 C CA . ILE A 1 204 ? 14.327 45.515 32.123 1.00 23.20 ? 258 ILE A CA 1 ATOM 1644 C C . ILE A 1 204 ? 13.260 46.597 31.918 1.00 24.83 ? 258 ILE A C 1 ATOM 1645 O O . ILE A 1 204 ? 13.118 47.180 30.848 1.00 24.76 ? 258 ILE A O 1 ATOM 1646 C CB . ILE A 1 204 ? 14.729 44.896 30.757 1.00 25.04 ? 258 ILE A CB 1 ATOM 1647 C CG1 . ILE A 1 204 ? 13.648 43.933 30.272 1.00 24.86 ? 258 ILE A CG1 1 ATOM 1648 C CG2 . ILE A 1 204 ? 16.108 44.182 30.897 1.00 23.62 ? 258 ILE A CG2 1 ATOM 1649 C CD1 . ILE A 1 204 ? 13.660 43.597 28.685 1.00 29.35 ? 258 ILE A CD1 1 ATOM 1650 N N . LEU A 1 205 ? 12.521 46.866 32.973 1.00 24.57 ? 259 LEU A N 1 ATOM 1651 C CA . LEU A 1 205 ? 11.461 47.861 32.914 1.00 25.13 ? 259 LEU A CA 1 ATOM 1652 C C . LEU A 1 205 ? 11.990 49.280 33.025 1.00 25.65 ? 259 LEU A C 1 ATOM 1653 O O . LEU A 1 205 ? 13.073 49.503 33.527 1.00 26.90 ? 259 LEU A O 1 ATOM 1654 C CB . LEU A 1 205 ? 10.522 47.656 34.105 1.00 23.76 ? 259 LEU A CB 1 ATOM 1655 C CG . LEU A 1 205 ? 9.745 46.359 34.103 1.00 26.75 ? 259 LEU A CG 1 ATOM 1656 C CD1 . LEU A 1 205 ? 9.044 46.187 35.429 1.00 29.15 ? 259 LEU A CD1 1 ATOM 1657 C CD2 . LEU A 1 205 ? 8.699 46.384 32.982 1.00 26.83 ? 259 LEU A CD2 1 ATOM 1658 N N A ASN A 1 206 ? 11.206 50.243 32.539 0.70 25.96 ? 260 ASN A N 1 ATOM 1659 N N B ASN A 1 206 ? 11.181 50.245 32.587 0.30 25.78 ? 260 ASN A N 1 ATOM 1660 C CA A ASN A 1 206 ? 11.467 51.664 32.805 0.70 25.85 ? 260 ASN A CA 1 ATOM 1661 C CA B ASN A 1 206 ? 11.468 51.668 32.786 0.30 25.64 ? 260 ASN A CA 1 ATOM 1662 C C A ASN A 1 206 ? 10.187 52.280 33.378 0.70 25.59 ? 260 ASN A C 1 ATOM 1663 C C B ASN A 1 206 ? 10.250 52.354 33.414 0.30 25.15 ? 260 ASN A C 1 ATOM 1664 O O A ASN A 1 206 ? 9.471 52.992 32.680 0.70 25.26 ? 260 ASN A O 1 ATOM 1665 O O B ASN A 1 206 ? 9.655 53.228 32.794 0.30 24.94 ? 260 ASN A O 1 ATOM 1666 C CB A ASN A 1 206 ? 11.874 52.369 31.506 0.70 28.00 ? 260 ASN A CB 1 ATOM 1667 C CB B ASN A 1 206 ? 11.771 52.322 31.435 0.30 26.81 ? 260 ASN A CB 1 ATOM 1668 C CG A ASN A 1 206 ? 13.289 52.031 31.110 0.70 28.07 ? 260 ASN A CG 1 ATOM 1669 C CG B ASN A 1 206 ? 12.195 53.768 31.566 0.30 27.51 ? 260 ASN A CG 1 ATOM 1670 O OD1 A ASN A 1 206 ? 14.218 52.726 31.505 0.70 33.56 ? 260 ASN A OD1 1 ATOM 1671 O OD1 B ASN A 1 206 ? 12.892 54.156 32.518 0.30 29.08 ? 260 ASN A OD1 1 ATOM 1672 N ND2 A ASN A 1 206 ? 13.469 50.917 30.401 0.70 28.05 ? 260 ASN A ND2 1 ATOM 1673 N ND2 B ASN A 1 206 ? 11.800 54.577 30.591 0.30 28.61 ? 260 ASN A ND2 1 ATOM 1674 N N . LEU A 1 207 ? 9.885 51.951 34.632 1.00 24.09 ? 261 LEU A N 1 ATOM 1675 C CA . LEU A 1 207 ? 8.604 52.345 35.232 1.00 23.92 ? 261 LEU A CA 1 ATOM 1676 C C . LEU A 1 207 ? 8.615 53.751 35.793 1.00 23.94 ? 261 LEU A C 1 ATOM 1677 O O . LEU A 1 207 ? 7.545 54.285 36.078 1.00 21.83 ? 261 LEU A O 1 ATOM 1678 C CB . LEU A 1 207 ? 8.224 51.387 36.386 1.00 25.87 ? 261 LEU A CB 1 ATOM 1679 C CG . LEU A 1 207 ? 7.948 49.916 36.060 1.00 26.80 ? 261 LEU A CG 1 ATOM 1680 C CD1 . LEU A 1 207 ? 7.793 49.084 37.414 1.00 28.31 ? 261 LEU A CD1 1 ATOM 1681 C CD2 . LEU A 1 207 ? 6.663 49.866 35.258 1.00 25.94 ? 261 LEU A CD2 1 ATOM 1682 N N . ASN A 1 208 ? 9.806 54.324 36.013 1.00 22.33 ? 262 ASN A N 1 ATOM 1683 C CA . ASN A 1 208 ? 9.876 55.653 36.719 1.00 23.66 ? 262 ASN A CA 1 ATOM 1684 C C . ASN A 1 208 ? 9.042 55.724 37.977 1.00 22.67 ? 262 ASN A C 1 ATOM 1685 O O . ASN A 1 208 ? 8.317 56.710 38.222 1.00 22.82 ? 262 ASN A O 1 ATOM 1686 C CB . ASN A 1 208 ? 9.473 56.732 35.728 1.00 22.64 ? 262 ASN A CB 1 ATOM 1687 C CG . ASN A 1 208 ? 10.568 56.917 34.682 1.00 30.29 ? 262 ASN A CG 1 ATOM 1688 O OD1 . ASN A 1 208 ? 11.749 56.714 35.008 1.00 32.63 ? 262 ASN A OD1 1 ATOM 1689 N ND2 . ASN A 1 208 ? 10.200 57.174 33.463 1.00 30.31 ? 262 ASN A ND2 1 ATOM 1690 N N . GLY A 1 209 ? 9.101 54.651 38.760 1.00 21.63 ? 263 GLY A N 1 ATOM 1691 C CA . GLY A 1 209 ? 8.452 54.661 40.021 1.00 20.89 ? 263 GLY A CA 1 ATOM 1692 C C . GLY A 1 209 ? 6.960 54.315 40.055 1.00 20.93 ? 263 GLY A C 1 ATOM 1693 O O . GLY A 1 209 ? 6.357 54.396 41.119 1.00 20.80 ? 263 GLY A O 1 ATOM 1694 N N . ALA A 1 210 ? 6.395 53.883 38.935 1.00 18.97 ? 264 ALA A N 1 ATOM 1695 C CA . ALA A 1 210 ? 4.939 53.652 38.847 1.00 18.77 ? 264 ALA A CA 1 ATOM 1696 C C . ALA A 1 210 ? 4.457 52.394 39.565 1.00 18.48 ? 264 ALA A C 1 ATOM 1697 O O . ALA A 1 210 ? 3.304 52.327 39.936 1.00 20.64 ? 264 ALA A O 1 ATOM 1698 C CB . ALA A 1 210 ? 4.486 53.600 37.331 1.00 17.95 ? 264 ALA A CB 1 ATOM 1699 N N . GLY A 1 211 ? 5.337 51.411 39.781 1.00 20.27 ? 265 GLY A N 1 ATOM 1700 C CA . GLY A 1 211 ? 4.863 50.117 40.311 1.00 20.64 ? 265 GLY A CA 1 ATOM 1701 C C . GLY A 1 211 ? 4.252 49.244 39.183 1.00 20.14 ? 265 GLY A C 1 ATOM 1702 O O . GLY A 1 211 ? 4.630 49.353 38.036 1.00 22.89 ? 265 GLY A O 1 ATOM 1703 N N . ASP A 1 212 ? 3.227 48.472 39.501 1.00 19.71 ? 266 ASP A N 1 ATOM 1704 C CA . ASP A 1 212 ? 2.563 47.618 38.478 1.00 19.92 ? 266 ASP A CA 1 ATOM 1705 C C . ASP A 1 212 ? 2.212 48.442 37.236 1.00 19.87 ? 266 ASP A C 1 ATOM 1706 O O . ASP A 1 212 ? 1.478 49.441 37.332 1.00 18.69 ? 266 ASP A O 1 ATOM 1707 C CB . ASP A 1 212 ? 1.303 47.019 39.123 1.00 19.43 ? 266 ASP A CB 1 ATOM 1708 C CG . ASP A 1 212 ? 0.392 46.350 38.123 1.00 21.56 ? 266 ASP A CG 1 ATOM 1709 O OD1 . ASP A 1 212 ? 0.909 45.557 37.319 1.00 21.04 ? 266 ASP A OD1 1 ATOM 1710 O OD2 . ASP A 1 212 ? -0.854 46.610 38.153 1.00 21.18 ? 266 ASP A OD2 1 ATOM 1711 N N . PRO A 1 213 ? 2.698 48.014 36.069 1.00 21.82 ? 267 PRO A N 1 ATOM 1712 C CA . PRO A 1 213 ? 2.524 48.733 34.846 1.00 23.73 ? 267 PRO A CA 1 ATOM 1713 C C . PRO A 1 213 ? 1.036 48.989 34.516 1.00 22.50 ? 267 PRO A C 1 ATOM 1714 O O . PRO A 1 213 ? 0.696 49.917 33.766 1.00 23.76 ? 267 PRO A O 1 ATOM 1715 C CB . PRO A 1 213 ? 3.045 47.720 33.812 1.00 24.64 ? 267 PRO A CB 1 ATOM 1716 C CG . PRO A 1 213 ? 4.081 46.971 34.468 1.00 26.58 ? 267 PRO A CG 1 ATOM 1717 C CD . PRO A 1 213 ? 3.589 46.830 35.897 1.00 22.73 ? 267 PRO A CD 1 ATOM 1718 N N . LEU A 1 214 ? 0.165 48.108 34.995 1.00 21.36 ? 268 LEU A N 1 ATOM 1719 C CA . LEU A 1 214 ? -1.264 48.220 34.634 1.00 21.17 ? 268 LEU A CA 1 ATOM 1720 C C . LEU A 1 214 ? -2.132 49.104 35.538 1.00 20.65 ? 268 LEU A C 1 ATOM 1721 O O . LEU A 1 214 ? -3.280 49.457 35.141 1.00 20.68 ? 268 LEU A O 1 ATOM 1722 C CB . LEU A 1 214 ? -1.878 46.822 34.536 1.00 21.60 ? 268 LEU A CB 1 ATOM 1723 C CG . LEU A 1 214 ? -1.138 45.856 33.620 1.00 23.23 ? 268 LEU A CG 1 ATOM 1724 C CD1 . LEU A 1 214 ? -1.988 44.552 33.550 1.00 25.84 ? 268 LEU A CD1 1 ATOM 1725 C CD2 . LEU A 1 214 ? -0.932 46.411 32.219 1.00 26.69 ? 268 LEU A CD2 1 ATOM 1726 N N . THR A 1 215 ? -1.599 49.526 36.701 1.00 19.42 ? 269 THR A N 1 ATOM 1727 C CA . THR A 1 215 ? -2.412 50.284 37.670 1.00 19.14 ? 269 THR A CA 1 ATOM 1728 C C . THR A 1 215 ? -1.697 51.472 38.296 1.00 18.99 ? 269 THR A C 1 ATOM 1729 O O . THR A 1 215 ? -1.688 51.641 39.523 1.00 19.49 ? 269 THR A O 1 ATOM 1730 C CB . THR A 1 215 ? -2.859 49.333 38.843 1.00 18.22 ? 269 THR A CB 1 ATOM 1731 O OG1 . THR A 1 215 ? -1.690 48.736 39.447 1.00 17.55 ? 269 THR A OG1 1 ATOM 1732 C CG2 . THR A 1 215 ? -3.805 48.198 38.270 1.00 20.21 ? 269 THR A CG2 1 ATOM 1733 N N . PRO A 1 216 ? -1.046 52.295 37.481 1.00 20.16 ? 270 PRO A N 1 ATOM 1734 C CA . PRO A 1 216 ? -0.263 53.411 38.068 1.00 19.99 ? 270 PRO A CA 1 ATOM 1735 C C . PRO A 1 216 ? -1.107 54.369 38.890 1.00 20.56 ? 270 PRO A C 1 ATOM 1736 O O . PRO A 1 216 ? -2.156 54.843 38.433 1.00 20.41 ? 270 PRO A O 1 ATOM 1737 C CB . PRO A 1 216 ? 0.312 54.123 36.835 1.00 20.23 ? 270 PRO A CB 1 ATOM 1738 C CG . PRO A 1 216 ? -0.695 53.797 35.721 1.00 20.99 ? 270 PRO A CG 1 ATOM 1739 C CD . PRO A 1 216 ? -1.071 52.331 36.002 1.00 20.27 ? 270 PRO A CD 1 ATOM 1740 N N . GLY A 1 217 ? -0.710 54.562 40.159 1.00 20.15 ? 271 GLY A N 1 ATOM 1741 C CA . GLY A 1 217 ? -1.410 55.487 41.078 1.00 19.48 ? 271 GLY A CA 1 ATOM 1742 C C . GLY A 1 217 ? -2.342 54.804 42.078 1.00 20.17 ? 271 GLY A C 1 ATOM 1743 O O . GLY A 1 217 ? -2.720 55.395 43.064 1.00 20.99 ? 271 GLY A O 1 ATOM 1744 N N . TYR A 1 218 ? -2.772 53.564 41.781 1.00 18.78 ? 272 TYR A N 1 ATOM 1745 C CA . TYR A 1 218 ? -3.833 52.937 42.567 1.00 19.68 ? 272 TYR A CA 1 ATOM 1746 C C . TYR A 1 218 ? -3.459 51.454 42.834 1.00 18.11 ? 272 TYR A C 1 ATOM 1747 O O . TYR A 1 218 ? -2.819 50.826 41.982 1.00 18.84 ? 272 TYR A O 1 ATOM 1748 C CB . TYR A 1 218 ? -5.184 53.039 41.850 1.00 19.05 ? 272 TYR A CB 1 ATOM 1749 C CG . TYR A 1 218 ? -5.461 54.484 41.466 1.00 20.03 ? 272 TYR A CG 1 ATOM 1750 C CD1 . TYR A 1 218 ? -6.038 55.356 42.379 1.00 18.38 ? 272 TYR A CD1 1 ATOM 1751 C CD2 . TYR A 1 218 ? -5.067 54.972 40.205 1.00 20.08 ? 272 TYR A CD2 1 ATOM 1752 C CE1 . TYR A 1 218 ? -6.280 56.675 42.027 1.00 18.05 ? 272 TYR A CE1 1 ATOM 1753 C CE2 . TYR A 1 218 ? -5.275 56.296 39.850 1.00 18.84 ? 272 TYR A CE2 1 ATOM 1754 C CZ . TYR A 1 218 ? -5.887 57.142 40.782 1.00 18.14 ? 272 TYR A CZ 1 ATOM 1755 O OH . TYR A 1 218 ? -6.086 58.469 40.418 1.00 18.15 ? 272 TYR A OH 1 ATOM 1756 N N . PRO A 1 219 ? -3.862 50.905 43.990 1.00 20.06 ? 273 PRO A N 1 ATOM 1757 C CA . PRO A 1 219 ? -3.513 49.522 44.258 1.00 20.58 ? 273 PRO A CA 1 ATOM 1758 C C . PRO A 1 219 ? -4.206 48.522 43.314 1.00 21.14 ? 273 PRO A C 1 ATOM 1759 O O . PRO A 1 219 ? -5.411 48.675 42.980 1.00 20.05 ? 273 PRO A O 1 ATOM 1760 C CB . PRO A 1 219 ? -3.998 49.288 45.707 1.00 20.42 ? 273 PRO A CB 1 ATOM 1761 C CG . PRO A 1 219 ? -5.177 50.257 45.879 1.00 20.94 ? 273 PRO A CG 1 ATOM 1762 C CD . PRO A 1 219 ? -4.647 51.500 45.077 1.00 20.91 ? 273 PRO A CD 1 ATOM 1763 N N . ALA A 1 220 ? -3.429 47.517 42.887 1.00 19.37 ? 274 ALA A N 1 ATOM 1764 C CA . ALA A 1 220 ? -3.955 46.428 42.025 1.00 20.55 ? 274 ALA A CA 1 ATOM 1765 C C . ALA A 1 220 ? -4.814 45.451 42.850 1.00 20.71 ? 274 ALA A C 1 ATOM 1766 O O . ALA A 1 220 ? -4.497 44.254 42.976 1.00 21.09 ? 274 ALA A O 1 ATOM 1767 C CB . ALA A 1 220 ? -2.794 45.712 41.421 1.00 21.16 ? 274 ALA A CB 1 ATOM 1768 N N . ASN A 1 221 ? -5.935 45.956 43.355 1.00 22.08 ? 275 ASN A N 1 ATOM 1769 C CA . ASN A 1 221 ? -6.808 45.211 44.272 1.00 23.46 ? 275 ASN A CA 1 ATOM 1770 C C . ASN A 1 221 ? -7.828 44.427 43.414 1.00 25.35 ? 275 ASN A C 1 ATOM 1771 O O . ASN A 1 221 ? -7.698 44.399 42.186 1.00 23.32 ? 275 ASN A O 1 ATOM 1772 C CB . ASN A 1 221 ? -7.490 46.155 45.264 1.00 24.86 ? 275 ASN A CB 1 ATOM 1773 C CG . ASN A 1 221 ? -8.361 47.199 44.572 1.00 24.72 ? 275 ASN A CG 1 ATOM 1774 O OD1 . ASN A 1 221 ? -8.846 46.978 43.472 1.00 27.16 ? 275 ASN A OD1 1 ATOM 1775 N ND2 . ASN A 1 221 ? -8.522 48.364 45.204 1.00 28.96 ? 275 ASN A ND2 1 ATOM 1776 N N A GLU A 1 222 ? -8.866 43.890 44.081 0.50 25.97 ? 276 GLU A N 1 ATOM 1777 N N B GLU A 1 222 ? -8.821 43.771 44.016 0.50 26.45 ? 276 GLU A N 1 ATOM 1778 C CA A GLU A 1 222 ? -9.848 42.971 43.482 0.50 27.72 ? 276 GLU A CA 1 ATOM 1779 C CA B GLU A 1 222 ? -9.648 42.903 43.174 0.50 28.07 ? 276 GLU A CA 1 ATOM 1780 C C A GLU A 1 222 ? -10.740 43.605 42.417 0.50 28.01 ? 276 GLU A C 1 ATOM 1781 C C B GLU A 1 222 ? -10.511 43.680 42.180 0.50 28.31 ? 276 GLU A C 1 ATOM 1782 O O A GLU A 1 222 ? -11.341 42.896 41.578 0.50 28.68 ? 276 GLU A O 1 ATOM 1783 O O B GLU A 1 222 ? -10.820 43.152 41.109 0.50 29.64 ? 276 GLU A O 1 ATOM 1784 C CB A GLU A 1 222 ? -10.786 42.421 44.582 0.50 28.07 ? 276 GLU A CB 1 ATOM 1785 C CB B GLU A 1 222 ? -10.486 41.913 44.002 0.50 29.47 ? 276 GLU A CB 1 ATOM 1786 C CG A GLU A 1 222 ? -11.058 40.948 44.483 0.50 32.05 ? 276 GLU A CG 1 ATOM 1787 C CG B GLU A 1 222 ? -9.690 40.658 44.381 0.50 33.60 ? 276 GLU A CG 1 ATOM 1788 C CD A GLU A 1 222 ? -9.886 40.135 45.035 0.50 36.10 ? 276 GLU A CD 1 ATOM 1789 C CD B GLU A 1 222 ? -9.984 39.436 43.499 0.50 37.47 ? 276 GLU A CD 1 ATOM 1790 O OE1 A GLU A 1 222 ? -9.432 40.427 46.164 0.50 38.21 ? 276 GLU A OE1 1 ATOM 1791 O OE1 B GLU A 1 222 ? -10.559 39.564 42.396 0.50 36.36 ? 276 GLU A OE1 1 ATOM 1792 O OE2 A GLU A 1 222 ? -9.398 39.220 44.347 0.50 36.49 ? 276 GLU A OE2 1 ATOM 1793 O OE2 B GLU A 1 222 ? -9.622 38.322 43.927 0.50 41.17 ? 276 GLU A OE2 1 ATOM 1794 N N . TYR A 1 223 ? -10.899 44.917 42.497 1.00 26.86 ? 277 TYR A N 1 ATOM 1795 C CA . TYR A 1 223 ? -11.794 45.636 41.571 1.00 28.04 ? 277 TYR A CA 1 ATOM 1796 C C . TYR A 1 223 ? -11.098 46.619 40.669 1.00 27.58 ? 277 TYR A C 1 ATOM 1797 O O . TYR A 1 223 ? -11.759 47.461 40.033 1.00 28.52 ? 277 TYR A O 1 ATOM 1798 C CB . TYR A 1 223 ? -12.974 46.292 42.309 1.00 28.97 ? 277 TYR A CB 1 ATOM 1799 C CG . TYR A 1 223 ? -12.523 47.220 43.385 1.00 26.53 ? 277 TYR A CG 1 ATOM 1800 C CD1 . TYR A 1 223 ? -12.235 48.560 43.081 1.00 29.22 ? 277 TYR A CD1 1 ATOM 1801 C CD2 . TYR A 1 223 ? -12.338 46.767 44.704 1.00 26.68 ? 277 TYR A CD2 1 ATOM 1802 C CE1 . TYR A 1 223 ? -11.763 49.448 44.059 1.00 30.34 ? 277 TYR A CE1 1 ATOM 1803 C CE2 . TYR A 1 223 ? -11.887 47.647 45.679 1.00 29.60 ? 277 TYR A CE2 1 ATOM 1804 C CZ . TYR A 1 223 ? -11.609 48.997 45.335 1.00 31.61 ? 277 TYR A CZ 1 ATOM 1805 O OH . TYR A 1 223 ? -11.150 49.893 46.287 1.00 33.13 ? 277 TYR A OH 1 ATOM 1806 N N . ALA A 1 224 ? -9.761 46.521 40.598 1.00 26.65 ? 278 ALA A N 1 ATOM 1807 C CA . ALA A 1 224 ? -8.966 47.496 39.862 1.00 27.93 ? 278 ALA A CA 1 ATOM 1808 C C . ALA A 1 224 ? -9.339 47.480 38.406 1.00 28.74 ? 278 ALA A C 1 ATOM 1809 O O . ALA A 1 224 ? -9.693 46.390 37.881 1.00 29.56 ? 278 ALA A O 1 ATOM 1810 C CB . ALA A 1 224 ? -7.451 47.175 39.985 1.00 28.22 ? 278 ALA A CB 1 ATOM 1811 N N . TYR A 1 225 ? -9.291 48.655 37.766 1.00 28.19 ? 279 TYR A N 1 ATOM 1812 C CA . TYR A 1 225 ? -9.452 48.739 36.293 1.00 29.18 ? 279 TYR A CA 1 ATOM 1813 C C . TYR A 1 225 ? -8.027 48.765 35.781 1.00 29.43 ? 279 TYR A C 1 ATOM 1814 O O . TYR A 1 225 ? -7.151 49.481 36.306 1.00 30.47 ? 279 TYR A O 1 ATOM 1815 C CB . TYR A 1 225 ? -10.297 49.980 35.761 1.00 29.93 ? 279 TYR A CB 1 ATOM 1816 C CG A TYR A 1 225 ? -10.623 49.883 34.286 0.50 27.20 ? 279 TYR A CG 1 ATOM 1817 C CG B TYR A 1 225 ? -9.581 50.666 34.536 0.50 31.42 ? 279 TYR A CG 1 ATOM 1818 C CD1 A TYR A 1 225 ? -11.612 49.027 33.819 0.50 27.66 ? 279 TYR A CD1 1 ATOM 1819 C CD1 B TYR A 1 225 ? -10.145 50.682 33.269 0.50 32.29 ? 279 TYR A CD1 1 ATOM 1820 C CD2 A TYR A 1 225 ? -9.891 50.610 33.356 0.50 27.78 ? 279 TYR A CD2 1 ATOM 1821 C CD2 B TYR A 1 225 ? -8.308 51.220 34.670 0.50 32.59 ? 279 TYR A CD2 1 ATOM 1822 C CE1 A TYR A 1 225 ? -11.876 48.912 32.465 0.50 29.63 ? 279 TYR A CE1 1 ATOM 1823 C CE1 B TYR A 1 225 ? -9.472 51.275 32.161 0.50 32.30 ? 279 TYR A CE1 1 ATOM 1824 C CE2 A TYR A 1 225 ? -10.161 50.505 31.986 0.50 30.16 ? 279 TYR A CE2 1 ATOM 1825 C CE2 B TYR A 1 225 ? -7.605 51.797 33.576 0.50 33.23 ? 279 TYR A CE2 1 ATOM 1826 C CZ A TYR A 1 225 ? -11.156 49.660 31.559 0.50 30.78 ? 279 TYR A CZ 1 ATOM 1827 C CZ B TYR A 1 225 ? -8.209 51.830 32.321 0.50 34.59 ? 279 TYR A CZ 1 ATOM 1828 O OH A TYR A 1 225 ? -11.394 49.541 30.208 0.50 35.79 ? 279 TYR A OH 1 ATOM 1829 O OH B TYR A 1 225 ? -7.534 52.423 31.247 0.50 33.57 ? 279 TYR A OH 1 ATOM 1830 N N . ARG A 1 226 ? -7.722 47.919 34.831 1.00 27.45 ? 280 ARG A N 1 ATOM 1831 C CA . ARG A 1 226 ? -6.338 47.870 34.348 1.00 28.28 ? 280 ARG A CA 1 ATOM 1832 C C . ARG A 1 226 ? -6.201 48.479 32.973 1.00 30.52 ? 280 ARG A C 1 ATOM 1833 O O . ARG A 1 226 ? -7.104 48.352 32.144 1.00 30.49 ? 280 ARG A O 1 ATOM 1834 C CB . ARG A 1 226 ? -5.885 46.410 34.278 1.00 27.72 ? 280 ARG A CB 1 ATOM 1835 C CG . ARG A 1 226 ? -5.836 45.799 35.656 1.00 27.16 ? 280 ARG A CG 1 ATOM 1836 C CD . ARG A 1 226 ? -5.311 44.362 35.599 1.00 29.79 ? 280 ARG A CD 1 ATOM 1837 N NE . ARG A 1 226 ? -5.018 44.015 36.976 1.00 31.30 ? 280 ARG A NE 1 ATOM 1838 C CZ . ARG A 1 226 ? -5.916 43.689 37.891 1.00 34.95 ? 280 ARG A CZ 1 ATOM 1839 N NH1 . ARG A 1 226 ? -7.216 43.570 37.551 1.00 37.00 ? 280 ARG A NH1 1 ATOM 1840 N NH2 . ARG A 1 226 ? -5.521 43.446 39.143 1.00 30.28 ? 280 ARG A NH2 1 ATOM 1841 N N . ARG A 1 227 ? -5.081 49.157 32.737 1.00 29.41 ? 281 ARG A N 1 ATOM 1842 C CA . ARG A 1 227 ? -4.693 49.517 31.364 1.00 31.92 ? 281 ARG A CA 1 ATOM 1843 C C . ARG A 1 227 ? -4.512 48.263 30.520 1.00 32.71 ? 281 ARG A C 1 ATOM 1844 O O . ARG A 1 227 ? -4.106 47.203 31.054 1.00 32.26 ? 281 ARG A O 1 ATOM 1845 C CB . ARG A 1 227 ? -3.362 50.241 31.397 1.00 30.04 ? 281 ARG A CB 1 ATOM 1846 C CG . ARG A 1 227 ? -3.464 51.506 32.206 1.00 30.06 ? 281 ARG A CG 1 ATOM 1847 C CD . ARG A 1 227 ? -2.209 52.340 32.043 1.00 34.45 ? 281 ARG A CD 1 ATOM 1848 N NE . ARG A 1 227 ? -2.500 53.717 32.431 1.00 33.58 ? 281 ARG A NE 1 ATOM 1849 C CZ . ARG A 1 227 ? -1.657 54.737 32.304 1.00 37.85 ? 281 ARG A CZ 1 ATOM 1850 N NH1 . ARG A 1 227 ? -0.462 54.550 31.754 1.00 37.12 ? 281 ARG A NH1 1 ATOM 1851 N NH2 . ARG A 1 227 ? -2.027 55.948 32.709 1.00 39.13 ? 281 ARG A NH2 1 ATOM 1852 N N . GLY A 1 228 ? -4.829 48.384 29.224 1.00 34.60 ? 282 GLY A N 1 ATOM 1853 C CA . GLY A 1 228 ? -4.437 47.356 28.256 1.00 37.16 ? 282 GLY A CA 1 ATOM 1854 C C . GLY A 1 228 ? -2.914 47.320 28.167 1.00 38.48 ? 282 GLY A C 1 ATOM 1855 O O . GLY A 1 228 ? -2.243 48.319 28.447 1.00 38.10 ? 282 GLY A O 1 ATOM 1856 N N . ILE A 1 229 ? -2.363 46.172 27.801 1.00 40.54 ? 283 ILE A N 1 ATOM 1857 C CA . ILE A 1 229 ? -0.913 46.048 27.597 1.00 42.38 ? 283 ILE A CA 1 ATOM 1858 C C . ILE A 1 229 ? -0.369 47.143 26.713 1.00 42.70 ? 283 ILE A C 1 ATOM 1859 O O . ILE A 1 229 ? 0.700 47.673 26.985 1.00 43.07 ? 283 ILE A O 1 ATOM 1860 C CB . ILE A 1 229 ? -0.491 44.679 27.035 1.00 43.09 ? 283 ILE A CB 1 ATOM 1861 C CG1 . ILE A 1 229 ? -0.539 43.629 28.133 1.00 44.05 ? 283 ILE A CG1 1 ATOM 1862 C CG2 . ILE A 1 229 ? 0.956 44.733 26.492 1.00 44.65 ? 283 ILE A CG2 1 ATOM 1863 C CD1 . ILE A 1 229 ? 0.596 43.763 29.124 1.00 41.10 ? 283 ILE A CD1 1 ATOM 1864 N N . ALA A 1 230 ? -1.112 47.505 25.670 1.00 43.83 ? 284 ALA A N 1 ATOM 1865 C CA . ALA A 1 230 ? -0.671 48.569 24.782 1.00 44.48 ? 284 ALA A CA 1 ATOM 1866 C C . ALA A 1 230 ? -0.426 49.890 25.501 1.00 44.27 ? 284 ALA A C 1 ATOM 1867 O O . ALA A 1 230 ? 0.500 50.597 25.140 1.00 44.75 ? 284 ALA A O 1 ATOM 1868 C CB . ALA A 1 230 ? -1.652 48.758 23.601 1.00 45.43 ? 284 ALA A CB 1 ATOM 1869 N N . GLU A 1 231 ? -1.247 50.211 26.503 1.00 43.68 ? 285 GLU A N 1 ATOM 1870 C CA . GLU A 1 231 ? -1.120 51.458 27.271 1.00 43.67 ? 285 GLU A CA 1 ATOM 1871 C C . GLU A 1 231 ? -0.267 51.324 28.560 1.00 42.83 ? 285 GLU A C 1 ATOM 1872 O O . GLU A 1 231 ? -0.133 52.295 29.312 1.00 43.17 ? 285 GLU A O 1 ATOM 1873 C CB . GLU A 1 231 ? -2.512 51.985 27.663 1.00 44.36 ? 285 GLU A CB 1 ATOM 1874 C CG . GLU A 1 231 ? -3.261 52.781 26.593 1.00 49.25 ? 285 GLU A CG 1 ATOM 1875 C CD . GLU A 1 231 ? -3.874 51.906 25.488 1.00 55.42 ? 285 GLU A CD 1 ATOM 1876 O OE1 . GLU A 1 231 ? -4.196 52.473 24.417 1.00 59.41 ? 285 GLU A OE1 1 ATOM 1877 O OE2 . GLU A 1 231 ? -4.056 50.673 25.674 1.00 56.93 ? 285 GLU A OE2 1 ATOM 1878 N N . ALA A 1 232 ? 0.312 50.149 28.810 1.00 41.79 ? 286 ALA A N 1 ATOM 1879 C CA . ALA A 1 232 ? 1.013 49.882 30.075 1.00 40.93 ? 286 ALA A CA 1 ATOM 1880 C C . ALA A 1 232 ? 2.220 50.819 30.297 1.00 40.63 ? 286 ALA A C 1 ATOM 1881 O O . ALA A 1 232 ? 2.738 51.384 29.357 1.00 39.18 ? 286 ALA A O 1 ATOM 1882 C CB . ALA A 1 232 ? 1.422 48.438 30.160 1.00 39.73 ? 286 ALA A CB 1 ATOM 1883 N N . VAL A 1 233 ? 2.617 51.008 31.562 1.00 39.94 ? 287 VAL A N 1 ATOM 1884 C CA . VAL A 1 233 ? 3.762 51.895 31.878 1.00 39.89 ? 287 VAL A CA 1 ATOM 1885 C C . VAL A 1 233 ? 5.056 51.113 31.771 1.00 38.21 ? 287 VAL A C 1 ATOM 1886 O O . VAL A 1 233 ? 5.182 50.064 32.402 1.00 39.52 ? 287 VAL A O 1 ATOM 1887 C CB . VAL A 1 233 ? 3.687 52.551 33.339 1.00 38.86 ? 287 VAL A CB 1 ATOM 1888 C CG1 . VAL A 1 233 ? 5.016 53.282 33.696 1.00 39.49 ? 287 VAL A CG1 1 ATOM 1889 C CG2 . VAL A 1 233 ? 2.518 53.545 33.452 1.00 41.73 ? 287 VAL A CG2 1 ATOM 1890 N N . GLY A 1 234 ? 5.998 51.574 30.963 1.00 37.54 ? 288 GLY A N 1 ATOM 1891 C CA . GLY A 1 234 ? 7.373 51.062 31.085 1.00 35.37 ? 288 GLY A CA 1 ATOM 1892 C C . GLY A 1 234 ? 7.844 49.765 30.447 1.00 34.87 ? 288 GLY A C 1 ATOM 1893 O O . GLY A 1 234 ? 9.009 49.368 30.680 1.00 33.02 ? 288 GLY A O 1 ATOM 1894 N N . LEU A 1 235 ? 6.995 49.122 29.638 1.00 32.93 ? 289 LEU A N 1 ATOM 1895 C CA . LEU A 1 235 ? 7.369 47.822 29.017 1.00 33.57 ? 289 LEU A CA 1 ATOM 1896 C C . LEU A 1 235 ? 8.333 48.040 27.872 1.00 34.12 ? 289 LEU A C 1 ATOM 1897 O O . LEU A 1 235 ? 8.202 49.028 27.143 1.00 33.52 ? 289 LEU A O 1 ATOM 1898 C CB . LEU A 1 235 ? 6.157 47.037 28.520 1.00 33.19 ? 289 LEU A CB 1 ATOM 1899 C CG . LEU A 1 235 ? 5.049 46.783 29.553 1.00 33.48 ? 289 LEU A CG 1 ATOM 1900 C CD1 . LEU A 1 235 ? 3.900 45.966 28.928 1.00 33.23 ? 289 LEU A CD1 1 ATOM 1901 C CD2 . LEU A 1 235 ? 5.568 46.082 30.793 1.00 34.15 ? 289 LEU A CD2 1 ATOM 1902 N N . PRO A 1 236 ? 9.318 47.137 27.726 1.00 35.00 ? 290 PRO A N 1 ATOM 1903 C CA . PRO A 1 236 ? 10.250 47.281 26.617 1.00 35.24 ? 290 PRO A CA 1 ATOM 1904 C C . PRO A 1 236 ? 9.571 46.905 25.306 1.00 34.85 ? 290 PRO A C 1 ATOM 1905 O O . PRO A 1 236 ? 8.639 46.106 25.293 1.00 33.33 ? 290 PRO A O 1 ATOM 1906 C CB . PRO A 1 236 ? 11.395 46.319 26.984 1.00 35.87 ? 290 PRO A CB 1 ATOM 1907 C CG . PRO A 1 236 ? 10.762 45.316 27.856 1.00 37.57 ? 290 PRO A CG 1 ATOM 1908 C CD . PRO A 1 236 ? 9.700 46.038 28.634 1.00 34.41 ? 290 PRO A CD 1 ATOM 1909 N N . SER A 1 237 ? 10.037 47.491 24.210 1.00 36.35 ? 291 SER A N 1 ATOM 1910 C CA A SER A 1 237 ? 9.405 47.336 22.895 0.50 36.88 ? 291 SER A CA 1 ATOM 1911 C CA B SER A 1 237 ? 9.380 47.282 22.915 0.50 37.10 ? 291 SER A CA 1 ATOM 1912 C C . SER A 1 237 ? 10.148 46.371 21.969 1.00 37.82 ? 291 SER A C 1 ATOM 1913 O O . SER A 1 237 ? 9.643 46.030 20.884 1.00 37.51 ? 291 SER A O 1 ATOM 1914 C CB A SER A 1 237 ? 9.273 48.705 22.223 0.50 37.27 ? 291 SER A CB 1 ATOM 1915 C CB B SER A 1 237 ? 9.058 48.613 22.242 0.50 37.47 ? 291 SER A CB 1 ATOM 1916 O OG A SER A 1 237 ? 10.532 49.359 22.147 0.50 37.18 ? 291 SER A OG 1 ATOM 1917 O OG B SER A 1 237 ? 7.850 49.133 22.756 0.50 38.64 ? 291 SER A OG 1 ATOM 1918 N N . ILE A 1 238 ? 11.347 45.961 22.387 1.00 37.40 ? 292 ILE A N 1 ATOM 1919 C CA . ILE A 1 238 ? 12.199 45.025 21.609 1.00 38.85 ? 292 ILE A CA 1 ATOM 1920 C C . ILE A 1 238 ? 12.621 43.865 22.507 1.00 37.99 ? 292 ILE A C 1 ATOM 1921 O O . ILE A 1 238 ? 12.791 44.057 23.722 1.00 38.09 ? 292 ILE A O 1 ATOM 1922 C CB . ILE A 1 238 ? 13.480 45.731 21.048 1.00 38.48 ? 292 ILE A CB 1 ATOM 1923 C CG1 . ILE A 1 238 ? 14.290 46.378 22.185 1.00 38.44 ? 292 ILE A CG1 1 ATOM 1924 C CG2 . ILE A 1 238 ? 13.084 46.769 19.965 1.00 40.26 ? 292 ILE A CG2 1 ATOM 1925 C CD1 . ILE A 1 238 ? 15.456 47.226 21.726 1.00 41.56 ? 292 ILE A CD1 1 ATOM 1926 N N . PRO A 1 239 ? 12.777 42.669 21.930 1.00 37.57 ? 293 PRO A N 1 ATOM 1927 C CA . PRO A 1 239 ? 13.225 41.486 22.674 1.00 36.34 ? 293 PRO A CA 1 ATOM 1928 C C . PRO A 1 239 ? 14.622 41.646 23.287 1.00 35.47 ? 293 PRO A C 1 ATOM 1929 O O . PRO A 1 239 ? 15.468 42.370 22.719 1.00 35.17 ? 293 PRO A O 1 ATOM 1930 C CB . PRO A 1 239 ? 13.253 40.408 21.597 1.00 37.71 ? 293 PRO A CB 1 ATOM 1931 C CG . PRO A 1 239 ? 12.268 40.934 20.516 1.00 37.11 ? 293 PRO A CG 1 ATOM 1932 C CD . PRO A 1 239 ? 12.577 42.357 20.495 1.00 38.13 ? 293 PRO A CD 1 ATOM 1933 N N . VAL A 1 240 ? 14.812 41.025 24.469 1.00 32.98 ? 294 VAL A N 1 ATOM 1934 C CA . VAL A 1 240 ? 16.024 41.160 25.289 1.00 31.01 ? 294 VAL A CA 1 ATOM 1935 C C . VAL A 1 240 ? 16.283 39.815 25.966 1.00 29.61 ? 294 VAL A C 1 ATOM 1936 O O . VAL A 1 240 ? 15.355 39.124 26.352 1.00 30.01 ? 294 VAL A O 1 ATOM 1937 C CB . VAL A 1 240 ? 15.876 42.269 26.393 1.00 29.86 ? 294 VAL A CB 1 ATOM 1938 C CG1 . VAL A 1 240 ? 17.213 42.485 27.137 1.00 26.85 ? 294 VAL A CG1 1 ATOM 1939 C CG2 . VAL A 1 240 ? 15.442 43.609 25.765 1.00 29.79 ? 294 VAL A CG2 1 ATOM 1940 N N . HIS A 1 241 ? 17.550 39.434 26.074 1.00 30.71 ? 295 HIS A N 1 ATOM 1941 C CA . HIS A 1 241 ? 17.918 38.168 26.691 1.00 29.46 ? 295 HIS A CA 1 ATOM 1942 C C . HIS A 1 241 ? 19.328 38.267 27.244 1.00 29.42 ? 295 HIS A C 1 ATOM 1943 O O . HIS A 1 241 ? 20.174 38.953 26.669 1.00 29.17 ? 295 HIS A O 1 ATOM 1944 C CB . HIS A 1 241 ? 17.771 37.023 25.670 1.00 31.52 ? 295 HIS A CB 1 ATOM 1945 C CG . HIS A 1 241 ? 17.835 35.650 26.262 1.00 30.71 ? 295 HIS A CG 1 ATOM 1946 N ND1 . HIS A 1 241 ? 16.838 35.131 27.065 1.00 29.66 ? 295 HIS A ND1 1 ATOM 1947 C CD2 . HIS A 1 241 ? 18.779 34.679 26.158 1.00 31.50 ? 295 HIS A CD2 1 ATOM 1948 C CE1 . HIS A 1 241 ? 17.161 33.903 27.427 1.00 30.08 ? 295 HIS A CE1 1 ATOM 1949 N NE2 . HIS A 1 241 ? 18.330 33.600 26.883 1.00 31.03 ? 295 HIS A NE2 1 ATOM 1950 N N . PRO A 1 242 ? 19.564 37.689 28.441 1.00 28.22 ? 296 PRO A N 1 ATOM 1951 C CA . PRO A 1 242 ? 20.896 37.767 29.037 1.00 27.15 ? 296 PRO A CA 1 ATOM 1952 C C . PRO A 1 242 ? 21.633 36.436 28.850 1.00 28.37 ? 296 PRO A C 1 ATOM 1953 O O . PRO A 1 242 ? 20.993 35.371 28.764 1.00 27.70 ? 296 PRO A O 1 ATOM 1954 C CB . PRO A 1 242 ? 20.586 37.964 30.538 1.00 27.73 ? 296 PRO A CB 1 ATOM 1955 C CG . PRO A 1 242 ? 19.331 37.145 30.723 1.00 27.19 ? 296 PRO A CG 1 ATOM 1956 C CD . PRO A 1 242 ? 18.582 37.103 29.375 1.00 26.68 ? 296 PRO A CD 1 ATOM 1957 N N . ILE A 1 243 ? 22.964 36.507 28.768 1.00 28.84 ? 297 ILE A N 1 ATOM 1958 C CA . ILE A 1 243 ? 23.789 35.294 28.585 1.00 29.38 ? 297 ILE A CA 1 ATOM 1959 C C . ILE A 1 243 ? 25.076 35.412 29.419 1.00 29.27 ? 297 ILE A C 1 ATOM 1960 O O . ILE A 1 243 ? 25.412 36.486 29.927 1.00 29.27 ? 297 ILE A O 1 ATOM 1961 C CB . ILE A 1 243 ? 24.138 35.054 27.083 1.00 29.11 ? 297 ILE A CB 1 ATOM 1962 C CG1 . ILE A 1 243 ? 25.055 36.182 26.551 1.00 29.03 ? 297 ILE A CG1 1 ATOM 1963 C CG2 . ILE A 1 243 ? 22.868 34.874 26.218 1.00 30.01 ? 297 ILE A CG2 1 ATOM 1964 C CD1 . ILE A 1 243 ? 25.391 36.066 25.038 1.00 28.23 ? 297 ILE A CD1 1 ATOM 1965 N N . GLY A 1 244 ? 25.790 34.295 29.573 1.00 29.79 ? 298 GLY A N 1 ATOM 1966 C CA . GLY A 1 244 ? 27.050 34.309 30.264 1.00 29.86 ? 298 GLY A CA 1 ATOM 1967 C C . GLY A 1 244 ? 28.236 34.574 29.339 1.00 31.93 ? 298 GLY A C 1 ATOM 1968 O O . GLY A 1 244 ? 28.068 34.742 28.130 1.00 31.13 ? 298 GLY A O 1 ATOM 1969 N N . TYR A 1 245 ? 29.436 34.648 29.914 1.00 32.20 ? 299 TYR A N 1 ATOM 1970 C CA . TYR A 1 245 ? 30.578 35.006 29.098 1.00 33.64 ? 299 TYR A CA 1 ATOM 1971 C C . TYR A 1 245 ? 31.126 33.892 28.163 1.00 34.79 ? 299 TYR A C 1 ATOM 1972 O O . TYR A 1 245 ? 31.813 34.227 27.192 1.00 34.75 ? 299 TYR A O 1 ATOM 1973 C CB . TYR A 1 245 ? 31.681 35.698 29.893 1.00 33.15 ? 299 TYR A CB 1 ATOM 1974 C CG . TYR A 1 245 ? 32.298 34.926 31.039 1.00 33.80 ? 299 TYR A CG 1 ATOM 1975 C CD1 . TYR A 1 245 ? 31.916 35.198 32.369 1.00 32.58 ? 299 TYR A CD1 1 ATOM 1976 C CD2 . TYR A 1 245 ? 33.324 33.973 30.824 1.00 34.56 ? 299 TYR A CD2 1 ATOM 1977 C CE1 . TYR A 1 245 ? 32.493 34.513 33.439 1.00 31.32 ? 299 TYR A CE1 1 ATOM 1978 C CE2 . TYR A 1 245 ? 33.907 33.283 31.911 1.00 34.06 ? 299 TYR A CE2 1 ATOM 1979 C CZ . TYR A 1 245 ? 33.503 33.577 33.216 1.00 33.41 ? 299 TYR A CZ 1 ATOM 1980 O OH . TYR A 1 245 ? 34.053 32.926 34.316 1.00 28.42 ? 299 TYR A OH 1 ATOM 1981 N N . TYR A 1 246 ? 30.833 32.615 28.432 1.00 34.35 ? 300 TYR A N 1 ATOM 1982 C CA . TYR A 1 246 ? 31.129 31.552 27.419 1.00 35.93 ? 300 TYR A CA 1 ATOM 1983 C C . TYR A 1 246 ? 30.320 31.789 26.154 1.00 36.97 ? 300 TYR A C 1 ATOM 1984 O O . TYR A 1 246 ? 30.863 31.758 25.039 1.00 37.07 ? 300 TYR A O 1 ATOM 1985 C CB . TYR A 1 246 ? 30.830 30.138 27.920 1.00 34.58 ? 300 TYR A CB 1 ATOM 1986 C CG . TYR A 1 246 ? 31.758 29.589 28.973 1.00 37.13 ? 300 TYR A CG 1 ATOM 1987 C CD1 . TYR A 1 246 ? 33.067 30.111 29.158 1.00 34.79 ? 300 TYR A CD1 1 ATOM 1988 C CD2 . TYR A 1 246 ? 31.346 28.517 29.789 1.00 36.82 ? 300 TYR A CD2 1 ATOM 1989 C CE1 . TYR A 1 246 ? 33.917 29.583 30.108 1.00 36.56 ? 300 TYR A CE1 1 ATOM 1990 C CE2 . TYR A 1 246 ? 32.202 27.988 30.768 1.00 35.64 ? 300 TYR A CE2 1 ATOM 1991 C CZ . TYR A 1 246 ? 33.472 28.518 30.913 1.00 37.95 ? 300 TYR A CZ 1 ATOM 1992 O OH . TYR A 1 246 ? 34.284 27.976 31.884 1.00 39.93 ? 300 TYR A OH 1 ATOM 1993 N N . ASP A 1 247 ? 29.016 32.040 26.324 1.00 36.11 ? 301 ASP A N 1 ATOM 1994 C CA . ASP A 1 247 ? 28.140 32.313 25.191 1.00 36.83 ? 301 ASP A CA 1 ATOM 1995 C C . ASP A 1 247 ? 28.449 33.650 24.536 1.00 37.37 ? 301 ASP A C 1 ATOM 1996 O O . ASP A 1 247 ? 28.426 33.748 23.295 1.00 37.97 ? 301 ASP A O 1 ATOM 1997 C CB . ASP A 1 247 ? 26.661 32.223 25.592 1.00 35.82 ? 301 ASP A CB 1 ATOM 1998 C CG . ASP A 1 247 ? 26.211 30.806 25.784 1.00 37.99 ? 301 ASP A CG 1 ATOM 1999 O OD1 . ASP A 1 247 ? 26.931 29.917 25.282 1.00 39.02 ? 301 ASP A OD1 1 ATOM 2000 O OD2 . ASP A 1 247 ? 25.152 30.544 26.432 1.00 33.96 ? 301 ASP A OD2 1 ATOM 2001 N N . ALA A 1 248 ? 28.730 34.674 25.352 1.00 36.47 ? 302 ALA A N 1 ATOM 2002 C CA . ALA A 1 248 ? 29.145 36.000 24.829 1.00 37.46 ? 302 ALA A CA 1 ATOM 2003 C C . ALA A 1 248 ? 30.416 35.909 23.962 1.00 38.77 ? 302 ALA A C 1 ATOM 2004 O O . ALA A 1 248 ? 30.528 36.608 22.957 1.00 37.97 ? 302 ALA A O 1 ATOM 2005 C CB . ALA A 1 248 ? 29.368 36.984 25.935 1.00 36.69 ? 302 ALA A CB 1 ATOM 2006 N N . GLN A 1 249 ? 31.365 35.085 24.378 1.00 39.43 ? 303 GLN A N 1 ATOM 2007 C CA . GLN A 1 249 ? 32.612 34.931 23.580 1.00 41.61 ? 303 GLN A CA 1 ATOM 2008 C C . GLN A 1 249 ? 32.290 34.433 22.167 1.00 42.37 ? 303 GLN A C 1 ATOM 2009 O O . GLN A 1 249 ? 32.815 34.969 21.166 1.00 43.53 ? 303 GLN A O 1 ATOM 2010 C CB . GLN A 1 249 ? 33.607 34.021 24.283 1.00 41.78 ? 303 GLN A CB 1 ATOM 2011 C CG . GLN A 1 249 ? 34.861 33.721 23.418 1.00 45.97 ? 303 GLN A CG 1 ATOM 2012 C CD . GLN A 1 249 ? 36.150 33.664 24.231 1.00 50.02 ? 303 GLN A CD 1 ATOM 2013 O OE1 . GLN A 1 249 ? 36.233 34.173 25.350 1.00 50.88 ? 303 GLN A OE1 1 ATOM 2014 N NE2 . GLN A 1 249 ? 37.172 33.037 23.659 1.00 51.42 ? 303 GLN A NE2 1 ATOM 2015 N N . LYS A 1 250 ? 31.390 33.455 22.073 1.00 42.56 ? 304 LYS A N 1 ATOM 2016 C CA . LYS A 1 250 ? 30.980 32.924 20.785 1.00 43.80 ? 304 LYS A CA 1 ATOM 2017 C C . LYS A 1 250 ? 30.338 33.975 19.882 1.00 45.13 ? 304 LYS A C 1 ATOM 2018 O O . LYS A 1 250 ? 30.545 33.963 18.662 1.00 45.42 ? 304 LYS A O 1 ATOM 2019 C CB . LYS A 1 250 ? 30.070 31.725 20.957 1.00 43.17 ? 304 LYS A CB 1 ATOM 2020 C CG . LYS A 1 250 ? 30.731 30.559 21.653 1.00 45.15 ? 304 LYS A CG 1 ATOM 2021 C CD . LYS A 1 250 ? 31.773 29.880 20.725 1.00 49.00 ? 304 LYS A CD 1 ATOM 2022 C CE . LYS A 1 250 ? 32.283 28.564 21.324 1.00 51.45 ? 304 LYS A CE 1 ATOM 2023 N NZ . LYS A 1 250 ? 33.269 27.873 20.416 1.00 55.48 ? 304 LYS A NZ 1 ATOM 2024 N N . LEU A 1 251 ? 29.559 34.888 20.472 1.00 44.18 ? 305 LEU A N 1 ATOM 2025 C CA . LEU A 1 251 ? 28.910 35.941 19.692 1.00 44.76 ? 305 LEU A CA 1 ATOM 2026 C C . LEU A 1 251 ? 29.847 37.094 19.333 1.00 45.18 ? 305 LEU A C 1 ATOM 2027 O O . LEU A 1 251 ? 29.611 37.776 18.339 1.00 46.52 ? 305 LEU A O 1 ATOM 2028 C CB . LEU A 1 251 ? 27.639 36.494 20.415 1.00 43.26 ? 305 LEU A CB 1 ATOM 2029 C CG . LEU A 1 251 ? 26.550 35.484 20.804 1.00 42.68 ? 305 LEU A CG 1 ATOM 2030 C CD1 . LEU A 1 251 ? 25.369 36.156 21.587 1.00 41.72 ? 305 LEU A CD1 1 ATOM 2031 C CD2 . LEU A 1 251 ? 25.989 34.717 19.612 1.00 40.37 ? 305 LEU A CD2 1 ATOM 2032 N N . LEU A 1 252 ? 30.880 37.342 20.138 1.00 45.00 ? 306 LEU A N 1 ATOM 2033 C CA . LEU A 1 252 ? 31.683 38.547 19.961 1.00 45.74 ? 306 LEU A CA 1 ATOM 2034 C C . LEU A 1 252 ? 32.928 38.334 19.076 1.00 47.73 ? 306 LEU A C 1 ATOM 2035 O O . LEU A 1 252 ? 33.562 39.306 18.600 1.00 47.92 ? 306 LEU A O 1 ATOM 2036 C CB . LEU A 1 252 ? 32.146 39.078 21.303 1.00 44.85 ? 306 LEU A CB 1 ATOM 2037 C CG . LEU A 1 252 ? 31.106 39.629 22.310 1.00 44.28 ? 306 LEU A CG 1 ATOM 2038 C CD1 . LEU A 1 252 ? 31.818 39.985 23.616 1.00 41.56 ? 306 LEU A CD1 1 ATOM 2039 C CD2 . LEU A 1 252 ? 30.361 40.846 21.775 1.00 45.33 ? 306 LEU A CD2 1 ATOM 2040 N N . GLU A 1 253 ? 33.299 37.074 18.913 1.00 48.64 ? 307 GLU A N 1 ATOM 2041 C CA . GLU A 1 253 ? 34.632 36.776 18.380 1.00 51.33 ? 307 GLU A CA 1 ATOM 2042 C C . GLU A 1 253 ? 34.732 37.106 16.884 1.00 52.82 ? 307 GLU A C 1 ATOM 2043 O O . GLU A 1 253 ? 35.806 37.452 16.394 1.00 54.21 ? 307 GLU A O 1 ATOM 2044 C CB . GLU A 1 253 ? 35.060 35.345 18.720 1.00 50.32 ? 307 GLU A CB 1 ATOM 2045 C CG . GLU A 1 253 ? 34.152 34.290 18.172 1.00 51.30 ? 307 GLU A CG 1 ATOM 2046 C CD . GLU A 1 253 ? 34.506 32.910 18.669 1.00 52.98 ? 307 GLU A CD 1 ATOM 2047 O OE1 . GLU A 1 253 ? 35.432 32.778 19.505 1.00 53.87 ? 307 GLU A OE1 1 ATOM 2048 O OE2 . GLU A 1 253 ? 33.845 31.947 18.227 1.00 53.53 ? 307 GLU A OE2 1 ATOM 2049 N N . LYS A 1 254 ? 33.599 37.055 16.184 1.00 54.00 ? 308 LYS A N 1 ATOM 2050 C CA . LYS A 1 254 ? 33.558 37.372 14.759 1.00 55.14 ? 308 LYS A CA 1 ATOM 2051 C C . LYS A 1 254 ? 33.268 38.855 14.432 1.00 56.12 ? 308 LYS A C 1 ATOM 2052 O O . LYS A 1 254 ? 33.219 39.243 13.263 1.00 56.46 ? 308 LYS A O 1 ATOM 2053 C CB . LYS A 1 254 ? 32.576 36.438 14.056 1.00 55.01 ? 308 LYS A CB 1 ATOM 2054 C CG . LYS A 1 254 ? 32.780 34.984 14.436 1.00 53.48 ? 308 LYS A CG 1 ATOM 2055 C CD . LYS A 1 254 ? 31.818 34.078 13.707 1.00 53.02 ? 308 LYS A CD 1 ATOM 2056 C CE . LYS A 1 254 ? 32.221 32.616 13.841 1.00 53.73 ? 308 LYS A CE 1 ATOM 2057 N NZ . LYS A 1 254 ? 31.169 31.681 13.330 1.00 51.83 ? 308 LYS A NZ 1 ATOM 2058 N N . MET A 1 255 ? 33.112 39.688 15.454 1.00 56.47 ? 309 MET A N 1 ATOM 2059 C CA . MET A 1 255 ? 32.754 41.109 15.240 1.00 57.14 ? 309 MET A CA 1 ATOM 2060 C C . MET A 1 255 ? 33.763 41.955 14.403 1.00 58.67 ? 309 MET A C 1 ATOM 2061 O O . MET A 1 255 ? 34.961 41.998 14.708 1.00 59.13 ? 309 MET A O 1 ATOM 2062 C CB . MET A 1 255 ? 32.428 41.786 16.574 1.00 56.18 ? 309 MET A CB 1 ATOM 2063 C CG A MET A 1 255 ? 31.194 41.160 17.225 0.50 55.43 ? 309 MET A CG 1 ATOM 2064 C CG B MET A 1 255 ? 31.265 41.170 17.332 0.50 55.21 ? 309 MET A CG 1 ATOM 2065 S SD A MET A 1 255 ? 30.113 42.285 18.119 0.50 52.45 ? 309 MET A SD 1 ATOM 2066 S SD B MET A 1 255 ? 29.700 41.380 16.480 0.50 52.41 ? 309 MET A SD 1 ATOM 2067 C CE A MET A 1 255 ? 29.783 43.539 16.875 0.50 53.74 ? 309 MET A CE 1 ATOM 2068 C CE B MET A 1 255 ? 29.605 43.166 16.403 0.50 52.97 ? 309 MET A CE 1 ATOM 2069 N N . GLY A 1 256 ? 33.241 42.630 13.369 1.00 59.58 ? 310 GLY A N 1 ATOM 2070 C CA . GLY A 1 256 ? 34.032 43.467 12.460 1.00 60.64 ? 310 GLY A CA 1 ATOM 2071 C C . GLY A 1 256 ? 33.813 44.966 12.600 1.00 60.99 ? 310 GLY A C 1 ATOM 2072 O O . GLY A 1 256 ? 33.650 45.481 13.725 1.00 59.69 ? 310 GLY A O 1 ATOM 2073 N N . GLY A 1 257 ? 33.835 45.673 11.461 1.00 61.39 ? 311 GLY A N 1 ATOM 2074 C CA . GLY A 1 257 ? 33.691 47.137 11.444 1.00 61.99 ? 311 GLY A CA 1 ATOM 2075 C C . GLY A 1 257 ? 34.711 47.858 12.317 1.00 62.66 ? 311 GLY A C 1 ATOM 2076 O O . GLY A 1 257 ? 35.813 47.363 12.545 1.00 62.72 ? 311 GLY A O 1 ATOM 2077 N N . SER A 1 258 ? 34.327 49.015 12.845 1.00 63.49 ? 312 SER A N 1 ATOM 2078 C CA . SER A 1 258 ? 35.236 49.859 13.626 1.00 64.54 ? 312 SER A CA 1 ATOM 2079 C C . SER A 1 258 ? 35.828 49.202 14.889 1.00 64.80 ? 312 SER A C 1 ATOM 2080 O O . SER A 1 258 ? 35.150 48.463 15.595 1.00 64.50 ? 312 SER A O 1 ATOM 2081 C CB . SER A 1 258 ? 34.533 51.179 13.979 1.00 64.68 ? 312 SER A CB 1 ATOM 2082 O OG A SER A 1 258 ? 35.374 52.005 14.766 0.50 64.82 ? 312 SER A OG 1 ATOM 2083 O OG B SER A 1 258 ? 33.994 51.798 12.817 0.50 64.14 ? 312 SER A OG 1 ATOM 2084 N N . ALA A 1 259 ? 37.104 49.465 15.157 1.00 66.00 ? 313 ALA A N 1 ATOM 2085 C CA . ALA A 1 259 ? 37.747 49.034 16.403 1.00 66.24 ? 313 ALA A CA 1 ATOM 2086 C C . ALA A 1 259 ? 37.127 49.773 17.591 1.00 66.04 ? 313 ALA A C 1 ATOM 2087 O O . ALA A 1 259 ? 36.439 50.778 17.399 1.00 66.14 ? 313 ALA A O 1 ATOM 2088 C CB . ALA A 1 259 ? 39.251 49.304 16.340 1.00 66.76 ? 313 ALA A CB 1 ATOM 2089 N N . PRO A 1 260 ? 37.345 49.277 18.825 1.00 66.08 ? 314 PRO A N 1 ATOM 2090 C CA . PRO A 1 260 ? 36.876 50.067 19.978 1.00 65.96 ? 314 PRO A CA 1 ATOM 2091 C C . PRO A 1 260 ? 37.576 51.437 20.042 1.00 66.62 ? 314 PRO A C 1 ATOM 2092 O O . PRO A 1 260 ? 38.773 51.516 19.798 1.00 67.42 ? 314 PRO A O 1 ATOM 2093 C CB . PRO A 1 260 ? 37.254 49.196 21.187 1.00 65.53 ? 314 PRO A CB 1 ATOM 2094 C CG . PRO A 1 260 ? 38.242 48.171 20.639 1.00 65.54 ? 314 PRO A CG 1 ATOM 2095 C CD . PRO A 1 260 ? 37.832 47.946 19.228 1.00 65.78 ? 314 PRO A CD 1 ATOM 2096 N N . PRO A 1 261 ? 36.832 52.510 20.361 1.00 66.64 ? 315 PRO A N 1 ATOM 2097 C CA . PRO A 1 261 ? 37.399 53.872 20.354 1.00 67.01 ? 315 PRO A CA 1 ATOM 2098 C C . PRO A 1 261 ? 38.564 54.059 21.324 1.00 66.87 ? 315 PRO A C 1 ATOM 2099 O O . PRO A 1 261 ? 39.443 54.876 21.080 1.00 67.13 ? 315 PRO A O 1 ATOM 2100 C CB . PRO A 1 261 ? 36.215 54.750 20.788 1.00 66.72 ? 315 PRO A CB 1 ATOM 2101 C CG . PRO A 1 261 ? 35.275 53.794 21.512 1.00 66.10 ? 315 PRO A CG 1 ATOM 2102 C CD . PRO A 1 261 ? 35.410 52.511 20.756 1.00 65.92 ? 315 PRO A CD 1 ATOM 2103 N N . ASP A 1 262 ? 38.548 53.306 22.416 1.00 66.08 ? 316 ASP A N 1 ATOM 2104 C CA . ASP A 1 262 ? 39.605 53.340 23.417 1.00 65.68 ? 316 ASP A CA 1 ATOM 2105 C C . ASP A 1 262 ? 39.522 52.076 24.298 1.00 64.50 ? 316 ASP A C 1 ATOM 2106 O O . ASP A 1 262 ? 38.646 51.222 24.084 1.00 64.46 ? 316 ASP A O 1 ATOM 2107 C CB . ASP A 1 262 ? 39.560 54.659 24.233 1.00 65.97 ? 316 ASP A CB 1 ATOM 2108 C CG . ASP A 1 262 ? 38.209 54.889 24.942 1.00 65.82 ? 316 ASP A CG 1 ATOM 2109 O OD1 . ASP A 1 262 ? 37.748 53.989 25.670 1.00 67.12 ? 316 ASP A OD1 1 ATOM 2110 O OD2 . ASP A 1 262 ? 37.618 55.984 24.800 1.00 65.71 ? 316 ASP A OD2 1 ATOM 2111 N N A SER A 1 263 ? 40.432 51.961 25.266 0.70 63.85 ? 317 SER A N 1 ATOM 2112 N N B SER A 1 263 ? 40.415 51.978 25.284 0.30 64.04 ? 317 SER A N 1 ATOM 2113 C CA A SER A 1 263 ? 40.512 50.786 26.143 0.70 62.62 ? 317 SER A CA 1 ATOM 2114 C CA B SER A 1 263 ? 40.518 50.800 26.156 0.30 63.02 ? 317 SER A CA 1 ATOM 2115 C C A SER A 1 263 ? 39.275 50.594 27.042 0.70 61.58 ? 317 SER A C 1 ATOM 2116 C C B SER A 1 263 ? 39.368 50.635 27.163 0.30 61.76 ? 317 SER A C 1 ATOM 2117 O O A SER A 1 263 ? 38.973 49.467 27.450 0.70 61.31 ? 317 SER A O 1 ATOM 2118 O O B SER A 1 263 ? 39.220 49.569 27.768 0.30 61.40 ? 317 SER A O 1 ATOM 2119 C CB A SER A 1 263 ? 41.777 50.848 27.003 0.70 62.79 ? 317 SER A CB 1 ATOM 2120 C CB B SER A 1 263 ? 41.861 50.802 26.891 0.30 63.40 ? 317 SER A CB 1 ATOM 2121 O OG A SER A 1 263 ? 41.766 51.986 27.846 0.70 60.60 ? 317 SER A OG 1 ATOM 2122 O OG B SER A 1 263 ? 42.939 50.700 25.977 0.30 64.01 ? 317 SER A OG 1 ATOM 2123 N N . SER A 1 264 ? 38.570 51.687 27.348 1.00 60.82 ? 318 SER A N 1 ATOM 2124 C CA . SER A 1 264 ? 37.384 51.626 28.235 1.00 59.18 ? 318 SER A CA 1 ATOM 2125 C C . SER A 1 264 ? 36.187 50.910 27.591 1.00 57.85 ? 318 SER A C 1 ATOM 2126 O O . SER A 1 264 ? 35.132 50.728 28.240 1.00 57.80 ? 318 SER A O 1 ATOM 2127 C CB . SER A 1 264 ? 36.968 53.028 28.700 1.00 59.28 ? 318 SER A CB 1 ATOM 2128 O OG . SER A 1 264 ? 36.247 53.694 27.675 1.00 58.52 ? 318 SER A OG 1 ATOM 2129 N N . TRP A 1 265 ? 36.353 50.524 26.325 1.00 56.12 ? 319 TRP A N 1 ATOM 2130 C CA . TRP A 1 265 ? 35.364 49.776 25.552 1.00 54.46 ? 319 TRP A CA 1 ATOM 2131 C C . TRP A 1 265 ? 35.693 48.278 25.420 1.00 53.98 ? 319 TRP A C 1 ATOM 2132 O O . TRP A 1 265 ? 34.905 47.510 24.853 1.00 53.21 ? 319 TRP A O 1 ATOM 2133 C CB . TRP A 1 265 ? 35.189 50.407 24.162 1.00 54.44 ? 319 TRP A CB 1 ATOM 2134 C CG . TRP A 1 265 ? 34.158 51.554 24.106 1.00 53.18 ? 319 TRP A CG 1 ATOM 2135 C CD1 . TRP A 1 265 ? 34.207 52.754 24.786 1.00 53.47 ? 319 TRP A CD1 1 ATOM 2136 C CD2 . TRP A 1 265 ? 32.959 51.590 23.319 1.00 51.29 ? 319 TRP A CD2 1 ATOM 2137 N NE1 . TRP A 1 265 ? 33.097 53.526 24.475 1.00 53.27 ? 319 TRP A NE1 1 ATOM 2138 C CE2 . TRP A 1 265 ? 32.316 52.834 23.579 1.00 53.14 ? 319 TRP A CE2 1 ATOM 2139 C CE3 . TRP A 1 265 ? 32.352 50.687 22.437 1.00 50.32 ? 319 TRP A CE3 1 ATOM 2140 C CZ2 . TRP A 1 265 ? 31.095 53.188 22.984 1.00 51.16 ? 319 TRP A CZ2 1 ATOM 2141 C CZ3 . TRP A 1 265 ? 31.141 51.047 21.832 1.00 50.12 ? 319 TRP A CZ3 1 ATOM 2142 C CH2 . TRP A 1 265 ? 30.528 52.288 22.113 1.00 50.36 ? 319 TRP A CH2 1 ATOM 2143 N N . ARG A 1 266 ? 36.860 47.878 25.938 1.00 53.64 ? 320 ARG A N 1 ATOM 2144 C CA . ARG A 1 266 ? 37.326 46.482 25.917 1.00 52.97 ? 320 ARG A CA 1 ATOM 2145 C C . ARG A 1 266 ? 37.194 45.829 27.288 1.00 51.34 ? 320 ARG A C 1 ATOM 2146 O O . ARG A 1 266 ? 37.749 46.318 28.270 1.00 50.95 ? 320 ARG A O 1 ATOM 2147 C CB . ARG A 1 266 ? 38.805 46.394 25.455 1.00 54.15 ? 320 ARG A CB 1 ATOM 2148 C CG . ARG A 1 266 ? 39.010 46.211 23.939 1.00 57.99 ? 320 ARG A CG 1 ATOM 2149 C CD . ARG A 1 266 ? 40.476 45.798 23.551 1.00 64.03 ? 320 ARG A CD 1 ATOM 2150 N NE . ARG A 1 266 ? 41.214 46.901 22.927 1.00 68.72 ? 320 ARG A NE 1 ATOM 2151 C CZ . ARG A 1 266 ? 41.930 47.816 23.586 1.00 71.13 ? 320 ARG A CZ 1 ATOM 2152 N NH1 . ARG A 1 266 ? 42.034 47.780 24.913 1.00 71.16 ? 320 ARG A NH1 1 ATOM 2153 N NH2 . ARG A 1 266 ? 42.545 48.781 22.913 1.00 71.48 ? 320 ARG A NH2 1 ATOM 2154 N N . GLY A 1 267 ? 36.456 44.724 27.355 1.00 50.33 ? 321 GLY A N 1 ATOM 2155 C CA . GLY A 1 267 ? 36.441 43.889 28.556 1.00 48.78 ? 321 GLY A CA 1 ATOM 2156 C C . GLY A 1 267 ? 37.597 42.892 28.543 1.00 49.40 ? 321 GLY A C 1 ATOM 2157 O O . GLY A 1 267 ? 38.621 43.122 27.866 1.00 49.26 ? 321 GLY A O 1 ATOM 2158 N N . SER A 1 268 ? 37.418 41.778 29.254 1.00 47.98 ? 322 SER A N 1 ATOM 2159 C CA . SER A 1 268 ? 38.476 40.794 29.498 1.00 47.77 ? 322 SER A CA 1 ATOM 2160 C C . SER A 1 268 ? 38.491 39.567 28.596 1.00 46.98 ? 322 SER A C 1 ATOM 2161 O O . SER A 1 268 ? 39.387 38.740 28.708 1.00 46.80 ? 322 SER A O 1 ATOM 2162 C CB . SER A 1 268 ? 38.423 40.323 30.956 1.00 47.48 ? 322 SER A CB 1 ATOM 2163 O OG . SER A 1 268 ? 38.939 41.327 31.813 1.00 50.77 ? 322 SER A OG 1 ATOM 2164 N N . LEU A 1 269 ? 37.515 39.420 27.713 1.00 45.79 ? 323 LEU A N 1 ATOM 2165 C CA . LEU A 1 269 ? 37.481 38.243 26.864 1.00 45.79 ? 323 LEU A CA 1 ATOM 2166 C C . LEU A 1 269 ? 38.544 38.306 25.738 1.00 47.26 ? 323 LEU A C 1 ATOM 2167 O O . LEU A 1 269 ? 38.969 39.397 25.315 1.00 46.75 ? 323 LEU A O 1 ATOM 2168 C CB . LEU A 1 269 ? 36.098 38.048 26.247 1.00 45.10 ? 323 LEU A CB 1 ATOM 2169 C CG . LEU A 1 269 ? 34.916 37.764 27.201 1.00 43.85 ? 323 LEU A CG 1 ATOM 2170 C CD1 . LEU A 1 269 ? 33.580 37.794 26.422 1.00 39.07 ? 323 LEU A CD1 1 ATOM 2171 C CD2 . LEU A 1 269 ? 35.124 36.425 27.945 1.00 41.54 ? 323 LEU A CD2 1 ATOM 2172 N N . LYS A 1 270 ? 38.919 37.139 25.236 1.00 47.78 ? 324 LYS A N 1 ATOM 2173 C CA . LYS A 1 270 ? 39.922 37.065 24.169 1.00 50.43 ? 324 LYS A CA 1 ATOM 2174 C C . LYS A 1 270 ? 39.251 37.314 22.826 1.00 50.51 ? 324 LYS A C 1 ATOM 2175 O O . LYS A 1 270 ? 39.081 36.405 22.012 1.00 50.83 ? 324 LYS A O 1 ATOM 2176 C CB . LYS A 1 270 ? 40.653 35.720 24.212 1.00 51.11 ? 324 LYS A CB 1 ATOM 2177 C CG . LYS A 1 270 ? 41.429 35.488 25.505 1.00 53.70 ? 324 LYS A CG 1 ATOM 2178 C CD . LYS A 1 270 ? 42.172 36.763 25.953 1.00 56.81 ? 324 LYS A CD 1 ATOM 2179 C CE . LYS A 1 270 ? 43.097 36.486 27.149 1.00 58.56 ? 324 LYS A CE 1 ATOM 2180 N NZ . LYS A 1 270 ? 43.851 37.719 27.504 1.00 59.31 ? 324 LYS A NZ 1 ATOM 2181 N N . VAL A 1 271 ? 38.834 38.563 22.636 1.00 50.61 ? 325 VAL A N 1 ATOM 2182 C CA . VAL A 1 271 ? 38.129 38.983 21.445 1.00 50.90 ? 325 VAL A CA 1 ATOM 2183 C C . VAL A 1 271 ? 38.548 40.425 21.184 1.00 51.63 ? 325 VAL A C 1 ATOM 2184 O O . VAL A 1 271 ? 39.052 41.102 22.089 1.00 51.16 ? 325 VAL A O 1 ATOM 2185 C CB . VAL A 1 271 ? 36.548 38.864 21.596 1.00 50.35 ? 325 VAL A CB 1 ATOM 2186 C CG1 . VAL A 1 271 ? 36.098 37.407 21.679 1.00 50.05 ? 325 VAL A CG1 1 ATOM 2187 C CG2 . VAL A 1 271 ? 36.035 39.659 22.785 1.00 49.76 ? 325 VAL A CG2 1 ATOM 2188 N N . PRO A 1 272 ? 38.350 40.903 19.947 1.00 53.01 ? 326 PRO A N 1 ATOM 2189 C CA . PRO A 1 272 ? 38.761 42.284 19.637 1.00 54.01 ? 326 PRO A CA 1 ATOM 2190 C C . PRO A 1 272 ? 37.874 43.366 20.256 1.00 53.69 ? 326 PRO A C 1 ATOM 2191 O O . PRO A 1 272 ? 38.360 44.472 20.512 1.00 54.12 ? 326 PRO A O 1 ATOM 2192 C CB . PRO A 1 272 ? 38.705 42.348 18.096 1.00 54.83 ? 326 PRO A CB 1 ATOM 2193 C CG . PRO A 1 272 ? 37.835 41.191 17.674 1.00 54.35 ? 326 PRO A CG 1 ATOM 2194 C CD . PRO A 1 272 ? 37.976 40.134 18.740 1.00 53.47 ? 326 PRO A CD 1 ATOM 2195 N N . TYR A 1 273 ? 36.601 43.045 20.518 1.00 53.31 ? 327 TYR A N 1 ATOM 2196 C CA . TYR A 1 273 ? 35.628 44.053 21.003 1.00 52.57 ? 327 TYR A CA 1 ATOM 2197 C C . TYR A 1 273 ? 35.384 45.116 19.927 1.00 53.36 ? 327 TYR A C 1 ATOM 2198 O O . TYR A 1 273 ? 35.233 46.317 20.214 1.00 53.33 ? 327 TYR A O 1 ATOM 2199 C CB . TYR A 1 273 ? 36.072 44.690 22.324 1.00 51.75 ? 327 TYR A CB 1 ATOM 2200 C CG . TYR A 1 273 ? 35.945 43.741 23.496 1.00 50.50 ? 327 TYR A CG 1 ATOM 2201 C CD1 . TYR A 1 273 ? 34.739 43.629 24.187 1.00 47.48 ? 327 TYR A CD1 1 ATOM 2202 C CD2 . TYR A 1 273 ? 37.020 42.940 23.901 1.00 46.82 ? 327 TYR A CD2 1 ATOM 2203 C CE1 . TYR A 1 273 ? 34.616 42.763 25.265 1.00 46.81 ? 327 TYR A CE1 1 ATOM 2204 C CE2 . TYR A 1 273 ? 36.913 42.069 24.986 1.00 44.76 ? 327 TYR A CE2 1 ATOM 2205 C CZ . TYR A 1 273 ? 35.688 41.976 25.653 1.00 45.19 ? 327 TYR A CZ 1 ATOM 2206 O OH . TYR A 1 273 ? 35.541 41.124 26.723 1.00 40.46 ? 327 TYR A OH 1 ATOM 2207 N N . ASN A 1 274 ? 35.362 44.653 18.683 1.00 53.90 ? 328 ASN A N 1 ATOM 2208 C CA . ASN A 1 274 ? 35.032 45.511 17.574 1.00 54.96 ? 328 ASN A CA 1 ATOM 2209 C C . ASN A 1 274 ? 33.576 45.903 17.697 1.00 54.92 ? 328 ASN A C 1 ATOM 2210 O O . ASN A 1 274 ? 32.719 45.070 17.993 1.00 54.69 ? 328 ASN A O 1 ATOM 2211 C CB . ASN A 1 274 ? 35.271 44.803 16.254 1.00 54.45 ? 328 ASN A CB 1 ATOM 2212 C CG . ASN A 1 274 ? 36.757 44.663 15.918 1.00 55.02 ? 328 ASN A CG 1 ATOM 2213 O OD1 . ASN A 1 274 ? 37.606 45.455 16.364 1.00 55.12 ? 328 ASN A OD1 1 ATOM 2214 N ND2 . ASN A 1 274 ? 37.069 43.644 15.142 1.00 46.06 ? 328 ASN A ND2 1 ATOM 2215 N N . VAL A 1 275 ? 33.313 47.177 17.457 1.00 55.86 ? 329 VAL A N 1 ATOM 2216 C CA . VAL A 1 275 ? 31.986 47.734 17.633 1.00 55.89 ? 329 VAL A CA 1 ATOM 2217 C C . VAL A 1 275 ? 31.032 47.250 16.539 1.00 56.45 ? 329 VAL A C 1 ATOM 2218 O O . VAL A 1 275 ? 29.822 47.299 16.708 1.00 56.02 ? 329 VAL A O 1 ATOM 2219 C CB . VAL A 1 275 ? 32.069 49.262 17.698 1.00 56.42 ? 329 VAL A CB 1 ATOM 2220 C CG1 . VAL A 1 275 ? 30.680 49.896 17.814 1.00 56.83 ? 329 VAL A CG1 1 ATOM 2221 C CG2 . VAL A 1 275 ? 32.968 49.674 18.880 1.00 57.11 ? 329 VAL A CG2 1 ATOM 2222 N N . GLY A 1 276 ? 31.570 46.733 15.436 1.00 57.28 ? 330 GLY A N 1 ATOM 2223 C CA . GLY A 1 276 ? 30.730 46.391 14.283 1.00 58.10 ? 330 GLY A CA 1 ATOM 2224 C C . GLY A 1 276 ? 30.415 47.630 13.450 1.00 59.09 ? 330 GLY A C 1 ATOM 2225 O O . GLY A 1 276 ? 31.221 48.569 13.395 1.00 59.11 ? 330 GLY A O 1 ATOM 2226 N N . PRO A 1 277 ? 29.242 47.656 12.789 1.00 59.87 ? 331 PRO A N 1 ATOM 2227 C CA . PRO A 1 277 ? 28.186 46.631 12.723 1.00 59.83 ? 331 PRO A CA 1 ATOM 2228 C C . PRO A 1 277 ? 28.651 45.369 12.010 1.00 60.03 ? 331 PRO A C 1 ATOM 2229 O O . PRO A 1 277 ? 29.554 45.451 11.180 1.00 60.30 ? 331 PRO A O 1 ATOM 2230 C CB . PRO A 1 277 ? 27.104 47.313 11.880 1.00 60.38 ? 331 PRO A CB 1 ATOM 2231 C CG . PRO A 1 277 ? 27.895 48.269 10.985 1.00 61.03 ? 331 PRO A CG 1 ATOM 2232 C CD . PRO A 1 277 ? 28.923 48.818 11.934 1.00 60.47 ? 331 PRO A CD 1 ATOM 2233 N N . GLY A 1 278 ? 28.047 44.226 12.349 1.00 59.56 ? 332 GLY A N 1 ATOM 2234 C CA . GLY A 1 278 ? 28.256 42.952 11.633 1.00 60.11 ? 332 GLY A CA 1 ATOM 2235 C C . GLY A 1 278 ? 29.574 42.231 11.909 1.00 60.52 ? 332 GLY A C 1 ATOM 2236 O O . GLY A 1 278 ? 30.438 42.761 12.627 1.00 60.20 ? 332 GLY A O 1 ATOM 2237 N N . PHE A 1 279 ? 29.714 41.028 11.334 1.00 60.41 ? 333 PHE A N 1 ATOM 2238 C CA . PHE A 1 279 ? 30.920 40.178 11.458 1.00 61.50 ? 333 PHE A CA 1 ATOM 2239 C C . PHE A 1 279 ? 32.057 40.498 10.426 1.00 62.61 ? 333 PHE A C 1 ATOM 2240 O O . PHE A 1 279 ? 31.862 41.318 9.515 1.00 62.86 ? 333 PHE A O 1 ATOM 2241 C CB . PHE A 1 279 ? 30.531 38.696 11.315 1.00 61.23 ? 333 PHE A CB 1 ATOM 2242 C CG . PHE A 1 279 ? 29.709 38.138 12.463 1.00 60.29 ? 333 PHE A CG 1 ATOM 2243 C CD1 . PHE A 1 279 ? 28.819 37.091 12.237 1.00 59.49 ? 333 PHE A CD1 1 ATOM 2244 C CD2 . PHE A 1 279 ? 29.839 38.633 13.762 1.00 58.69 ? 333 PHE A CD2 1 ATOM 2245 C CE1 . PHE A 1 279 ? 28.064 36.546 13.282 1.00 58.89 ? 333 PHE A CE1 1 ATOM 2246 C CE2 . PHE A 1 279 ? 29.078 38.092 14.818 1.00 57.78 ? 333 PHE A CE2 1 ATOM 2247 C CZ . PHE A 1 279 ? 28.196 37.050 14.570 1.00 56.93 ? 333 PHE A CZ 1 ATOM 2248 N N . THR A 1 280 ? 33.226 39.855 10.568 1.00 63.36 ? 334 THR A N 1 ATOM 2249 C CA . THR A 1 280 ? 34.350 40.014 9.597 1.00 64.44 ? 334 THR A CA 1 ATOM 2250 C C . THR A 1 280 ? 34.252 39.100 8.372 1.00 65.94 ? 334 THR A C 1 ATOM 2251 O O . THR A 1 280 ? 33.746 37.963 8.458 1.00 65.72 ? 334 THR A O 1 ATOM 2252 C CB . THR A 1 280 ? 35.767 39.758 10.219 1.00 64.48 ? 334 THR A CB 1 ATOM 2253 O OG1 . THR A 1 280 ? 35.762 38.547 10.985 1.00 62.76 ? 334 THR A OG1 1 ATOM 2254 C CG2 . THR A 1 280 ? 36.233 40.921 11.072 1.00 63.43 ? 334 THR A CG2 1 ATOM 2255 N N . GLY A 1 281 ? 34.805 39.604 7.256 1.00 67.27 ? 335 GLY A N 1 ATOM 2256 C CA . GLY A 1 281 ? 34.845 38.949 5.947 1.00 68.26 ? 335 GLY A CA 1 ATOM 2257 C C . GLY A 1 281 ? 34.206 37.592 5.699 1.00 68.77 ? 335 GLY A C 1 ATOM 2258 O O . GLY A 1 281 ? 33.167 37.495 5.033 1.00 68.49 ? 335 GLY A O 1 ATOM 2259 N N . ASN A 1 282 ? 34.845 36.538 6.201 1.00 69.34 ? 336 ASN A N 1 ATOM 2260 C CA . ASN A 1 282 ? 34.402 35.169 5.919 1.00 70.41 ? 336 ASN A CA 1 ATOM 2261 C C . ASN A 1 282 ? 33.013 34.878 6.458 1.00 69.88 ? 336 ASN A C 1 ATOM 2262 O O . ASN A 1 282 ? 32.229 34.151 5.836 1.00 70.40 ? 336 ASN A O 1 ATOM 2263 C CB . ASN A 1 282 ? 35.421 34.148 6.441 1.00 70.73 ? 336 ASN A CB 1 ATOM 2264 C CG . ASN A 1 282 ? 36.687 34.098 5.583 1.00 73.25 ? 336 ASN A CG 1 ATOM 2265 O OD1 . ASN A 1 282 ? 36.887 33.159 4.801 1.00 75.69 ? 336 ASN A OD1 1 ATOM 2266 N ND2 . ASN A 1 282 ? 37.536 35.118 5.711 1.00 74.26 ? 336 ASN A ND2 1 ATOM 2267 N N . PHE A 1 283 ? 32.717 35.479 7.612 1.00 69.36 ? 337 PHE A N 1 ATOM 2268 C CA . PHE A 1 283 ? 31.439 35.310 8.291 1.00 68.03 ? 337 PHE A CA 1 ATOM 2269 C C . PHE A 1 283 ? 30.537 36.531 8.088 1.00 68.02 ? 337 PHE A C 1 ATOM 2270 O O . PHE A 1 283 ? 29.526 36.675 8.785 1.00 67.06 ? 337 PHE A O 1 ATOM 2271 C CB . PHE A 1 283 ? 31.660 35.113 9.795 1.00 67.14 ? 337 PHE A CB 1 ATOM 2272 C CG . PHE A 1 283 ? 32.813 34.212 10.148 1.00 66.34 ? 337 PHE A CG 1 ATOM 2273 C CD1 . PHE A 1 283 ? 34.030 34.756 10.570 1.00 64.94 ? 337 PHE A CD1 1 ATOM 2274 C CD2 . PHE A 1 283 ? 32.675 32.820 10.094 1.00 64.70 ? 337 PHE A CD2 1 ATOM 2275 C CE1 . PHE A 1 283 ? 35.090 33.930 10.920 1.00 63.82 ? 337 PHE A CE1 1 ATOM 2276 C CE2 . PHE A 1 283 ? 33.730 31.989 10.443 1.00 64.47 ? 337 PHE A CE2 1 ATOM 2277 C CZ . PHE A 1 283 ? 34.941 32.545 10.854 1.00 63.94 ? 337 PHE A CZ 1 ATOM 2278 N N . SER A 1 284 ? 30.897 37.410 7.147 1.00 68.16 ? 338 SER A N 1 ATOM 2279 C CA . SER A 1 284 ? 30.180 38.681 6.971 1.00 67.73 ? 338 SER A CA 1 ATOM 2280 C C . SER A 1 284 ? 28.726 38.458 6.580 1.00 67.10 ? 338 SER A C 1 ATOM 2281 O O . SER A 1 284 ? 27.918 39.391 6.629 1.00 67.01 ? 338 SER A O 1 ATOM 2282 C CB . SER A 1 284 ? 30.862 39.577 5.932 1.00 68.54 ? 338 SER A CB 1 ATOM 2283 O OG . SER A 1 284 ? 30.546 39.147 4.615 1.00 69.58 ? 338 SER A OG 1 ATOM 2284 N N . THR A 1 285 ? 28.408 37.217 6.217 1.00 66.47 ? 339 THR A N 1 ATOM 2285 C CA . THR A 1 285 ? 27.088 36.847 5.713 1.00 66.10 ? 339 THR A CA 1 ATOM 2286 C C . THR A 1 285 ? 26.224 36.168 6.778 1.00 65.14 ? 339 THR A C 1 ATOM 2287 O O . THR A 1 285 ? 25.002 36.074 6.628 1.00 65.20 ? 339 THR A O 1 ATOM 2288 C CB . THR A 1 285 ? 27.202 35.887 4.511 1.00 66.76 ? 339 THR A CB 1 ATOM 2289 O OG1 . THR A 1 285 ? 27.344 34.543 4.987 1.00 65.99 ? 339 THR A OG1 1 ATOM 2290 C CG2 . THR A 1 285 ? 28.404 36.257 3.624 1.00 67.45 ? 339 THR A CG2 1 ATOM 2291 N N . GLN A 1 286 ? 26.861 35.663 7.831 1.00 64.39 ? 340 GLN A N 1 ATOM 2292 C CA . GLN A 1 286 ? 26.131 35.065 8.963 1.00 63.35 ? 340 GLN A CA 1 ATOM 2293 C C . GLN A 1 286 ? 25.408 36.142 9.764 1.00 62.01 ? 340 GLN A C 1 ATOM 2294 O O . GLN A 1 286 ? 25.822 37.313 9.784 1.00 61.33 ? 340 GLN A O 1 ATOM 2295 C CB . GLN A 1 286 ? 27.071 34.291 9.890 1.00 63.33 ? 340 GLN A CB 1 ATOM 2296 C CG . GLN A 1 286 ? 27.612 32.996 9.309 1.00 64.86 ? 340 GLN A CG 1 ATOM 2297 C CD . GLN A 1 286 ? 28.758 32.413 10.125 1.00 65.71 ? 340 GLN A CD 1 ATOM 2298 O OE1 . GLN A 1 286 ? 29.155 32.955 11.167 1.00 64.92 ? 340 GLN A OE1 1 ATOM 2299 N NE2 . GLN A 1 286 ? 29.290 31.298 9.656 1.00 65.69 ? 340 GLN A NE2 1 ATOM 2300 N N . LYS A 1 287 ? 24.328 35.737 10.431 1.00 61.31 ? 341 LYS A N 1 ATOM 2301 C CA . LYS A 1 287 ? 23.557 36.664 11.267 1.00 59.60 ? 341 LYS A CA 1 ATOM 2302 C C . LYS A 1 287 ? 23.316 36.138 12.701 1.00 57.93 ? 341 LYS A C 1 ATOM 2303 O O . LYS A 1 287 ? 23.645 34.994 13.020 1.00 57.29 ? 341 LYS A O 1 ATOM 2304 C CB . LYS A 1 287 ? 22.227 37.057 10.586 1.00 60.12 ? 341 LYS A CB 1 ATOM 2305 C CG . LYS A 1 287 ? 22.349 37.710 9.199 1.00 62.14 ? 341 LYS A CG 1 ATOM 2306 C CD . LYS A 1 287 ? 21.585 39.045 9.106 1.00 63.97 ? 341 LYS A CD 1 ATOM 2307 C CE . LYS A 1 287 ? 20.709 39.167 7.844 1.00 65.75 ? 341 LYS A CE 1 ATOM 2308 N NZ . LYS A 1 287 ? 21.448 38.883 6.564 1.00 66.88 ? 341 LYS A NZ 1 ATOM 2309 N N . VAL A 1 288 ? 22.738 36.994 13.547 1.00 56.40 ? 342 VAL A N 1 ATOM 2310 C CA . VAL A 1 288 ? 22.335 36.616 14.912 1.00 54.26 ? 342 VAL A CA 1 ATOM 2311 C C . VAL A 1 288 ? 20.806 36.608 15.010 1.00 53.11 ? 342 VAL A C 1 ATOM 2312 O O . VAL A 1 288 ? 20.154 37.532 14.522 1.00 52.69 ? 342 VAL A O 1 ATOM 2313 C CB . VAL A 1 288 ? 22.946 37.571 15.954 1.00 54.64 ? 342 VAL A CB 1 ATOM 2314 C CG1 . VAL A 1 288 ? 22.407 37.263 17.375 1.00 52.47 ? 342 VAL A CG1 1 ATOM 2315 C CG2 . VAL A 1 288 ? 24.474 37.481 15.908 1.00 54.04 ? 342 VAL A CG2 1 ATOM 2316 N N . LYS A 1 289 ? 20.247 35.554 15.606 1.00 51.36 ? 343 LYS A N 1 ATOM 2317 C CA . LYS A 1 289 ? 18.797 35.416 15.732 1.00 50.15 ? 343 LYS A CA 1 ATOM 2318 C C . LYS A 1 289 ? 18.368 35.115 17.187 1.00 48.27 ? 343 LYS A C 1 ATOM 2319 O O . LYS A 1 289 ? 18.794 34.116 17.773 1.00 47.59 ? 343 LYS A O 1 ATOM 2320 C CB . LYS A 1 289 ? 18.294 34.309 14.807 1.00 50.49 ? 343 LYS A CB 1 ATOM 2321 C CG . LYS A 1 289 ? 16.771 34.145 14.708 1.00 51.44 ? 343 LYS A CG 1 ATOM 2322 C CD . LYS A 1 289 ? 16.449 32.932 13.837 1.00 55.77 ? 343 LYS A CD 1 ATOM 2323 C CE . LYS A 1 289 ? 14.993 32.471 13.946 1.00 58.70 ? 343 LYS A CE 1 ATOM 2324 N NZ . LYS A 1 289 ? 14.044 33.254 13.104 1.00 61.00 ? 343 LYS A NZ 1 ATOM 2325 N N . MET A 1 290 ? 17.492 35.960 17.732 1.00 46.65 ? 344 MET A N 1 ATOM 2326 C CA . MET A 1 290 ? 16.945 35.764 19.086 1.00 44.66 ? 344 MET A CA 1 ATOM 2327 C C . MET A 1 290 ? 15.655 34.933 18.978 1.00 44.54 ? 344 MET A C 1 ATOM 2328 O O . MET A 1 290 ? 14.903 35.081 18.010 1.00 45.42 ? 344 MET A O 1 ATOM 2329 C CB . MET A 1 290 ? 16.663 37.133 19.745 1.00 44.26 ? 344 MET A CB 1 ATOM 2330 C CG . MET A 1 290 ? 17.883 38.067 19.853 1.00 42.67 ? 344 MET A CG 1 ATOM 2331 S SD . MET A 1 290 ? 17.572 39.678 20.617 1.00 43.27 ? 344 MET A SD 1 ATOM 2332 C CE . MET A 1 290 ? 17.463 39.107 22.340 1.00 44.03 ? 344 MET A CE 1 ATOM 2333 N N . HIS A 1 291 ? 15.393 34.059 19.939 1.00 42.91 ? 345 HIS A N 1 ATOM 2334 C CA . HIS A 1 291 ? 14.086 33.417 20.041 1.00 42.29 ? 345 HIS A CA 1 ATOM 2335 C C . HIS A 1 291 ? 13.502 33.679 21.439 1.00 39.98 ? 345 HIS A C 1 ATOM 2336 O O . HIS A 1 291 ? 13.902 33.034 22.415 1.00 38.55 ? 345 HIS A O 1 ATOM 2337 C CB . HIS A 1 291 ? 14.183 31.919 19.819 1.00 43.29 ? 345 HIS A CB 1 ATOM 2338 C CG . HIS A 1 291 ? 15.032 31.535 18.644 1.00 46.76 ? 345 HIS A CG 1 ATOM 2339 N ND1 . HIS A 1 291 ? 16.406 31.672 18.645 1.00 48.05 ? 345 HIS A ND1 1 ATOM 2340 C CD2 . HIS A 1 291 ? 14.702 31.017 17.437 1.00 49.89 ? 345 HIS A CD2 1 ATOM 2341 C CE1 . HIS A 1 291 ? 16.887 31.252 17.486 1.00 49.53 ? 345 HIS A CE1 1 ATOM 2342 N NE2 . HIS A 1 291 ? 15.876 30.841 16.740 1.00 51.80 ? 345 HIS A NE2 1 ATOM 2343 N N . ILE A 1 292 ? 12.575 34.627 21.525 1.00 38.45 ? 346 ILE A N 1 ATOM 2344 C CA . ILE A 1 292 ? 12.009 35.009 22.845 1.00 36.68 ? 346 ILE A CA 1 ATOM 2345 C C . ILE A 1 292 ? 10.520 34.762 22.837 1.00 35.81 ? 346 ILE A C 1 ATOM 2346 O O . ILE A 1 292 ? 9.784 35.368 22.035 1.00 36.82 ? 346 ILE A O 1 ATOM 2347 C CB . ILE A 1 292 ? 12.325 36.467 23.243 1.00 36.72 ? 346 ILE A CB 1 ATOM 2348 C CG1 . ILE A 1 292 ? 13.834 36.820 23.066 1.00 34.61 ? 346 ILE A CG1 1 ATOM 2349 C CG2 . ILE A 1 292 ? 11.749 36.773 24.673 1.00 35.83 ? 346 ILE A CG2 1 ATOM 2350 C CD1 . ILE A 1 292 ? 14.871 35.946 23.843 1.00 36.45 ? 346 ILE A CD1 1 ATOM 2351 N N . HIS A 1 293 ? 10.100 33.863 23.729 1.00 34.47 ? 347 HIS A N 1 ATOM 2352 C CA . HIS A 1 293 ? 8.725 33.395 23.870 1.00 35.37 ? 347 HIS A CA 1 ATOM 2353 C C . HIS A 1 293 ? 8.073 33.597 25.279 1.00 33.21 ? 347 HIS A C 1 ATOM 2354 O O . HIS A 1 293 ? 7.034 32.998 25.599 1.00 31.82 ? 347 HIS A O 1 ATOM 2355 C CB . HIS A 1 293 ? 8.686 31.930 23.482 1.00 36.37 ? 347 HIS A CB 1 ATOM 2356 C CG . HIS A 1 293 ? 9.374 31.664 22.179 1.00 41.62 ? 347 HIS A CG 1 ATOM 2357 N ND1 . HIS A 1 293 ? 8.968 32.253 20.997 1.00 45.96 ? 347 HIS A ND1 1 ATOM 2358 C CD2 . HIS A 1 293 ? 10.499 30.968 21.890 1.00 45.13 ? 347 HIS A CD2 1 ATOM 2359 C CE1 . HIS A 1 293 ? 9.784 31.883 20.023 1.00 47.75 ? 347 HIS A CE1 1 ATOM 2360 N NE2 . HIS A 1 293 ? 10.719 31.103 20.537 1.00 47.23 ? 347 HIS A NE2 1 ATOM 2361 N N . SER A 1 294 ? 8.711 34.429 26.103 1.00 31.88 ? 348 SER A N 1 ATOM 2362 C CA . SER A 1 294 ? 8.199 34.770 27.443 1.00 30.60 ? 348 SER A CA 1 ATOM 2363 C C . SER A 1 294 ? 6.837 35.435 27.345 1.00 29.93 ? 348 SER A C 1 ATOM 2364 O O . SER A 1 294 ? 6.553 36.120 26.352 1.00 31.05 ? 348 SER A O 1 ATOM 2365 C CB . SER A 1 294 ? 9.164 35.743 28.153 1.00 28.82 ? 348 SER A CB 1 ATOM 2366 O OG . SER A 1 294 ? 10.463 35.151 28.248 1.00 31.12 ? 348 SER A OG 1 ATOM 2367 N N . THR A 1 295 ? 6.030 35.292 28.407 1.00 28.70 ? 349 THR A N 1 ATOM 2368 C CA A THR A 1 295 ? 4.702 35.918 28.418 0.60 28.33 ? 349 THR A CA 1 ATOM 2369 C CA B THR A 1 295 ? 4.676 35.847 28.441 0.40 28.43 ? 349 THR A CA 1 ATOM 2370 C C . THR A 1 295 ? 4.498 36.743 29.677 1.00 27.90 ? 349 THR A C 1 ATOM 2371 O O . THR A 1 295 ? 4.997 36.388 30.741 1.00 27.13 ? 349 THR A O 1 ATOM 2372 C CB A THR A 1 295 ? 3.587 34.887 28.380 0.60 28.95 ? 349 THR A CB 1 ATOM 2373 C CB B THR A 1 295 ? 3.648 34.704 28.511 0.40 28.96 ? 349 THR A CB 1 ATOM 2374 O OG1 A THR A 1 295 ? 3.767 33.956 29.458 0.60 28.70 ? 349 THR A OG1 1 ATOM 2375 O OG1 B THR A 1 295 ? 3.892 33.755 27.449 0.40 30.20 ? 349 THR A OG1 1 ATOM 2376 C CG2 A THR A 1 295 ? 3.576 34.140 27.023 0.60 29.87 ? 349 THR A CG2 1 ATOM 2377 C CG2 B THR A 1 295 ? 2.224 35.247 28.425 0.40 28.77 ? 349 THR A CG2 1 ATOM 2378 N N . ASN A 1 296 ? 3.781 37.857 29.524 1.00 26.44 ? 350 ASN A N 1 ATOM 2379 C CA . ASN A 1 296 ? 3.432 38.708 30.661 1.00 27.45 ? 350 ASN A CA 1 ATOM 2380 C C . ASN A 1 296 ? 2.050 38.243 31.139 1.00 28.04 ? 350 ASN A C 1 ATOM 2381 O O . ASN A 1 296 ? 1.158 38.014 30.319 1.00 29.58 ? 350 ASN A O 1 ATOM 2382 C CB . ASN A 1 296 ? 3.380 40.184 30.225 1.00 26.99 ? 350 ASN A CB 1 ATOM 2383 C CG . ASN A 1 296 ? 4.727 40.715 29.807 1.00 28.61 ? 350 ASN A CG 1 ATOM 2384 O OD1 . ASN A 1 296 ? 5.761 40.255 30.267 1.00 31.77 ? 350 ASN A OD1 1 ATOM 2385 N ND2 . ASN A 1 296 ? 4.724 41.687 28.886 1.00 32.43 ? 350 ASN A ND2 1 ATOM 2386 N N . GLU A 1 297 ? 1.871 38.060 32.443 1.00 26.26 ? 351 GLU A N 1 ATOM 2387 C CA . GLU A 1 297 ? 0.645 37.506 32.984 1.00 27.46 ? 351 GLU A CA 1 ATOM 2388 C C . GLU A 1 297 ? 0.314 38.182 34.286 1.00 24.83 ? 351 GLU A C 1 ATOM 2389 O O . GLU A 1 297 ? 1.175 38.274 35.169 1.00 22.82 ? 351 GLU A O 1 ATOM 2390 C CB . GLU A 1 297 ? 0.825 36.025 33.373 1.00 29.91 ? 351 GLU A CB 1 ATOM 2391 C CG . GLU A 1 297 ? 1.652 35.192 32.412 1.00 38.80 ? 351 GLU A CG 1 ATOM 2392 C CD . GLU A 1 297 ? 1.389 33.715 32.608 1.00 48.10 ? 351 GLU A CD 1 ATOM 2393 O OE1 . GLU A 1 297 ? 0.913 33.086 31.625 1.00 54.31 ? 351 GLU A OE1 1 ATOM 2394 O OE2 . GLU A 1 297 ? 1.640 33.197 33.734 1.00 46.66 ? 351 GLU A OE2 1 ATOM 2395 N N . VAL A 1 298 ? -0.937 38.577 34.445 1.00 24.89 ? 352 VAL A N 1 ATOM 2396 C CA . VAL A 1 298 ? -1.344 39.200 35.724 1.00 24.24 ? 352 VAL A CA 1 ATOM 2397 C C . VAL A 1 298 ? -1.354 38.033 36.737 1.00 25.03 ? 352 VAL A C 1 ATOM 2398 O O . VAL A 1 298 ? -2.000 36.986 36.478 1.00 24.58 ? 352 VAL A O 1 ATOM 2399 C CB . VAL A 1 298 ? -2.734 39.834 35.576 1.00 24.92 ? 352 VAL A CB 1 ATOM 2400 C CG1 . VAL A 1 298 ? -3.291 40.281 36.946 1.00 24.23 ? 352 VAL A CG1 1 ATOM 2401 C CG2 . VAL A 1 298 ? -2.627 41.051 34.649 1.00 25.25 ? 352 VAL A CG2 1 ATOM 2402 N N . THR A 1 299 ? -0.675 38.218 37.877 1.00 21.71 ? 353 THR A N 1 ATOM 2403 C CA . THR A 1 299 ? -0.398 37.126 38.818 1.00 21.45 ? 353 THR A CA 1 ATOM 2404 C C . THR A 1 299 ? -0.547 37.655 40.249 1.00 21.55 ? 353 THR A C 1 ATOM 2405 O O . THR A 1 299 ? -0.153 38.814 40.499 1.00 20.49 ? 353 THR A O 1 ATOM 2406 C CB . THR A 1 299 ? 1.026 36.607 38.582 1.00 22.41 ? 353 THR A CB 1 ATOM 2407 O OG1 . THR A 1 299 ? 1.176 36.244 37.180 1.00 24.24 ? 353 THR A OG1 1 ATOM 2408 C CG2 . THR A 1 299 ? 1.304 35.367 39.429 1.00 20.84 ? 353 THR A CG2 1 ATOM 2409 N N . ARG A 1 300 ? -1.055 36.821 41.179 1.00 20.76 ? 354 ARG A N 1 ATOM 2410 C CA . ARG A 1 300 ? -1.186 37.307 42.570 1.00 21.52 ? 354 ARG A CA 1 ATOM 2411 C C . ARG A 1 300 ? 0.150 37.288 43.326 1.00 20.38 ? 354 ARG A C 1 ATOM 2412 O O . ARG A 1 300 ? 0.966 36.349 43.191 1.00 20.55 ? 354 ARG A O 1 ATOM 2413 C CB . ARG A 1 300 ? -2.253 36.514 43.354 1.00 22.92 ? 354 ARG A CB 1 ATOM 2414 C CG . ARG A 1 300 ? -2.546 37.016 44.779 1.00 22.57 ? 354 ARG A CG 1 ATOM 2415 C CD . ARG A 1 300 ? -3.958 36.519 45.150 1.00 24.35 ? 354 ARG A CD 1 ATOM 2416 N NE . ARG A 1 300 ? -4.942 37.304 44.388 1.00 26.79 ? 354 ARG A NE 1 ATOM 2417 C CZ . ARG A 1 300 ? -6.271 37.217 44.561 1.00 33.80 ? 354 ARG A CZ 1 ATOM 2418 N NH1 . ARG A 1 300 ? -6.781 36.367 45.455 1.00 31.07 ? 354 ARG A NH1 1 ATOM 2419 N NH2 . ARG A 1 300 ? -7.089 37.993 43.859 1.00 30.46 ? 354 ARG A NH2 1 ATOM 2420 N N . ILE A 1 301 ? 0.359 38.334 44.112 1.00 19.32 ? 355 ILE A N 1 ATOM 2421 C CA . ILE A 1 301 ? 1.582 38.468 44.910 1.00 19.08 ? 355 ILE A CA 1 ATOM 2422 C C . ILE A 1 301 ? 1.115 38.758 46.348 1.00 20.12 ? 355 ILE A C 1 ATOM 2423 O O . ILE A 1 301 ? -0.008 39.216 46.537 1.00 20.29 ? 355 ILE A O 1 ATOM 2424 C CB . ILE A 1 301 ? 2.508 39.622 44.412 1.00 17.37 ? 355 ILE A CB 1 ATOM 2425 C CG1 . ILE A 1 301 ? 1.786 40.986 44.493 1.00 17.11 ? 355 ILE A CG1 1 ATOM 2426 C CG2 . ILE A 1 301 ? 3.024 39.266 43.015 1.00 17.66 ? 355 ILE A CG2 1 ATOM 2427 C CD1 . ILE A 1 301 ? 2.749 42.155 44.331 1.00 20.23 ? 355 ILE A CD1 1 ATOM 2428 N N . TYR A 1 302 ? 1.984 38.513 47.318 1.00 19.66 ? 356 TYR A N 1 ATOM 2429 C CA . TYR A 1 302 ? 1.620 38.593 48.726 1.00 21.03 ? 356 TYR A CA 1 ATOM 2430 C C . TYR A 1 302 ? 2.682 39.296 49.539 1.00 19.86 ? 356 TYR A C 1 ATOM 2431 O O . TYR A 1 302 ? 3.798 38.776 49.744 1.00 19.84 ? 356 TYR A O 1 ATOM 2432 C CB . TYR A 1 302 ? 1.481 37.166 49.312 1.00 21.12 ? 356 TYR A CB 1 ATOM 2433 C CG . TYR A 1 302 ? 0.443 36.324 48.614 1.00 20.87 ? 356 TYR A CG 1 ATOM 2434 C CD1 . TYR A 1 302 ? -0.865 36.340 49.041 1.00 23.95 ? 356 TYR A CD1 1 ATOM 2435 C CD2 . TYR A 1 302 ? 0.789 35.524 47.513 1.00 24.03 ? 356 TYR A CD2 1 ATOM 2436 C CE1 . TYR A 1 302 ? -1.836 35.585 48.384 1.00 23.91 ? 356 TYR A CE1 1 ATOM 2437 C CE2 . TYR A 1 302 ? -0.154 34.755 46.873 1.00 25.11 ? 356 TYR A CE2 1 ATOM 2438 C CZ . TYR A 1 302 ? -1.466 34.804 47.317 1.00 25.60 ? 356 TYR A CZ 1 ATOM 2439 O OH . TYR A 1 302 ? -2.390 34.033 46.647 1.00 28.23 ? 356 TYR A OH 1 ATOM 2440 N N . ASN A 1 303 ? 2.320 40.425 50.121 1.00 20.84 ? 357 ASN A N 1 ATOM 2441 C CA . ASN A 1 303 ? 3.198 40.997 51.148 1.00 20.45 ? 357 ASN A CA 1 ATOM 2442 C C . ASN A 1 303 ? 2.807 40.511 52.551 1.00 21.03 ? 357 ASN A C 1 ATOM 2443 O O . ASN A 1 303 ? 1.591 40.405 52.851 1.00 23.20 ? 357 ASN A O 1 ATOM 2444 C CB . ASN A 1 303 ? 3.047 42.532 51.185 1.00 18.82 ? 357 ASN A CB 1 ATOM 2445 C CG . ASN A 1 303 ? 3.393 43.204 49.849 1.00 20.22 ? 357 ASN A CG 1 ATOM 2446 O OD1 . ASN A 1 303 ? 4.326 42.804 49.119 1.00 19.86 ? 357 ASN A OD1 1 ATOM 2447 N ND2 . ASN A 1 303 ? 2.724 44.330 49.600 1.00 22.04 ? 357 ASN A ND2 1 ATOM 2448 N N . VAL A 1 304 ? 3.794 40.305 53.423 1.00 19.75 ? 358 VAL A N 1 ATOM 2449 C CA . VAL A 1 304 ? 3.464 40.032 54.852 1.00 19.49 ? 358 VAL A CA 1 ATOM 2450 C C . VAL A 1 304 ? 3.732 41.354 55.577 1.00 20.13 ? 358 VAL A C 1 ATOM 2451 O O . VAL A 1 304 ? 4.806 41.943 55.446 1.00 20.56 ? 358 VAL A O 1 ATOM 2452 C CB . VAL A 1 304 ? 4.368 38.955 55.501 1.00 20.53 ? 358 VAL A CB 1 ATOM 2453 C CG1 . VAL A 1 304 ? 3.796 38.569 56.872 1.00 22.41 ? 358 VAL A CG1 1 ATOM 2454 C CG2 . VAL A 1 304 ? 4.457 37.706 54.615 1.00 21.86 ? 358 VAL A CG2 1 ATOM 2455 N N . ILE A 1 305 ? 2.734 41.805 56.303 1.00 19.88 ? 359 ILE A N 1 ATOM 2456 C CA . ILE A 1 305 ? 2.764 43.073 57.093 1.00 21.04 ? 359 ILE A CA 1 ATOM 2457 C C . ILE A 1 305 ? 2.494 42.718 58.578 1.00 20.91 ? 359 ILE A C 1 ATOM 2458 O O . ILE A 1 305 ? 1.371 42.281 58.936 1.00 22.67 ? 359 ILE A O 1 ATOM 2459 C CB . ILE A 1 305 ? 1.663 44.066 56.629 1.00 20.79 ? 359 ILE A CB 1 ATOM 2460 C CG1 . ILE A 1 305 ? 1.691 44.242 55.079 1.00 22.44 ? 359 ILE A CG1 1 ATOM 2461 C CG2 . ILE A 1 305 ? 1.782 45.406 57.415 1.00 21.54 ? 359 ILE A CG2 1 ATOM 2462 C CD1 . ILE A 1 305 ? 3.012 44.847 54.528 1.00 22.42 ? 359 ILE A CD1 1 ATOM 2463 N N . GLY A 1 306 ? 3.507 42.937 59.401 1.00 21.57 ? 360 GLY A N 1 ATOM 2464 C CA . GLY A 1 306 ? 3.459 42.668 60.864 1.00 22.29 ? 360 GLY A CA 1 ATOM 2465 C C . GLY A 1 306 ? 3.383 43.996 61.581 1.00 21.97 ? 360 GLY A C 1 ATOM 2466 O O . GLY A 1 306 ? 4.020 44.966 61.163 1.00 23.25 ? 360 GLY A O 1 ATOM 2467 N N . THR A 1 307 ? 2.586 44.064 62.638 1.00 21.91 ? 361 THR A N 1 ATOM 2468 C CA . THR A 1 307 ? 2.436 45.305 63.424 1.00 22.97 ? 361 THR A CA 1 ATOM 2469 C C . THR A 1 307 ? 2.848 45.060 64.871 1.00 24.29 ? 361 THR A C 1 ATOM 2470 O O . THR A 1 307 ? 2.374 44.107 65.514 1.00 24.34 ? 361 THR A O 1 ATOM 2471 C CB . THR A 1 307 ? 0.964 45.787 63.389 1.00 23.27 ? 361 THR A CB 1 ATOM 2472 O OG1 . THR A 1 307 ? 0.599 46.034 62.019 1.00 24.62 ? 361 THR A OG1 1 ATOM 2473 C CG2 . THR A 1 307 ? 0.728 47.098 64.189 1.00 25.53 ? 361 THR A CG2 1 ATOM 2474 N N . LEU A 1 308 ? 3.687 45.962 65.389 1.00 25.15 ? 362 LEU A N 1 ATOM 2475 C CA . LEU A 1 308 ? 3.966 46.041 66.845 1.00 25.40 ? 362 LEU A CA 1 ATOM 2476 C C . LEU A 1 308 ? 3.504 47.414 67.295 1.00 25.25 ? 362 LEU A C 1 ATOM 2477 O O . LEU A 1 308 ? 4.220 48.414 67.122 1.00 25.15 ? 362 LEU A O 1 ATOM 2478 C CB . LEU A 1 308 ? 5.486 45.858 67.089 1.00 27.12 ? 362 LEU A CB 1 ATOM 2479 C CG . LEU A 1 308 ? 6.016 45.847 68.546 1.00 30.91 ? 362 LEU A CG 1 ATOM 2480 C CD1 . LEU A 1 308 ? 5.282 44.819 69.369 1.00 33.12 ? 362 LEU A CD1 1 ATOM 2481 C CD2 . LEU A 1 308 ? 7.504 45.580 68.573 1.00 30.55 ? 362 LEU A CD2 1 ATOM 2482 N N . ARG A 1 309 ? 2.326 47.448 67.913 1.00 24.66 ? 363 ARG A N 1 ATOM 2483 C CA . ARG A 1 309 ? 1.654 48.714 68.259 1.00 25.68 ? 363 ARG A CA 1 ATOM 2484 C C . ARG A 1 309 ? 2.436 49.516 69.312 1.00 26.11 ? 363 ARG A C 1 ATOM 2485 O O . ARG A 1 309 ? 2.909 48.967 70.321 1.00 26.37 ? 363 ARG A O 1 ATOM 2486 C CB . ARG A 1 309 ? 0.223 48.409 68.704 1.00 27.21 ? 363 ARG A CB 1 ATOM 2487 C CG . ARG A 1 309 ? -0.525 49.666 69.242 1.00 30.99 ? 363 ARG A CG 1 ATOM 2488 C CD . ARG A 1 309 ? -2.021 49.407 69.469 1.00 38.56 ? 363 ARG A CD 1 ATOM 2489 N NE . ARG A 1 309 ? -2.210 48.011 69.880 1.00 46.90 ? 363 ARG A NE 1 ATOM 2490 C CZ . ARG A 1 309 ? -1.955 47.497 71.087 1.00 48.95 ? 363 ARG A CZ 1 ATOM 2491 N NH1 . ARG A 1 309 ? -1.510 48.261 72.098 1.00 49.94 ? 363 ARG A NH1 1 ATOM 2492 N NH2 . ARG A 1 309 ? -2.157 46.193 71.275 1.00 48.07 ? 363 ARG A NH2 1 ATOM 2493 N N . GLY A 1 310 ? 2.624 50.813 69.048 1.00 23.93 ? 364 GLY A N 1 ATOM 2494 C CA . GLY A 1 310 ? 3.323 51.699 69.947 1.00 23.26 ? 364 GLY A CA 1 ATOM 2495 C C . GLY A 1 310 ? 2.505 51.974 71.229 1.00 24.57 ? 364 GLY A C 1 ATOM 2496 O O . GLY A 1 310 ? 1.267 52.086 71.194 1.00 24.94 ? 364 GLY A O 1 ATOM 2497 N N . ALA A 1 311 ? 3.213 52.102 72.336 1.00 26.69 ? 365 ALA A N 1 ATOM 2498 C CA . ALA A 1 311 ? 2.592 52.386 73.665 1.00 29.03 ? 365 ALA A CA 1 ATOM 2499 C C . ALA A 1 311 ? 2.094 53.805 73.794 1.00 30.19 ? 365 ALA A C 1 ATOM 2500 O O . ALA A 1 311 ? 1.117 54.039 74.498 1.00 29.89 ? 365 ALA A O 1 ATOM 2501 C CB . ALA A 1 311 ? 3.609 52.123 74.801 1.00 30.22 ? 365 ALA A CB 1 ATOM 2502 N N . VAL A 1 312 ? 2.782 54.758 73.157 1.00 28.68 ? 366 VAL A N 1 ATOM 2503 C CA . VAL A 1 312 ? 2.487 56.175 73.409 1.00 29.46 ? 366 VAL A CA 1 ATOM 2504 C C . VAL A 1 312 ? 2.008 56.893 72.133 1.00 27.88 ? 366 VAL A C 1 ATOM 2505 O O . VAL A 1 312 ? 1.003 57.629 72.145 1.00 27.42 ? 366 VAL A O 1 ATOM 2506 C CB . VAL A 1 312 ? 3.703 56.885 74.003 1.00 29.87 ? 366 VAL A CB 1 ATOM 2507 C CG1 . VAL A 1 312 ? 3.435 58.375 74.186 1.00 31.04 ? 366 VAL A CG1 1 ATOM 2508 C CG2 . VAL A 1 312 ? 4.031 56.277 75.375 1.00 32.47 ? 366 VAL A CG2 1 ATOM 2509 N N . GLU A 1 313 ? 2.689 56.610 71.016 1.00 25.53 ? 367 GLU A N 1 ATOM 2510 C CA . GLU A 1 313 ? 2.295 57.189 69.726 1.00 24.73 ? 367 GLU A CA 1 ATOM 2511 C C . GLU A 1 313 ? 2.026 56.083 68.715 1.00 23.88 ? 367 GLU A C 1 ATOM 2512 O O . GLU A 1 313 ? 2.809 55.924 67.758 1.00 22.95 ? 367 GLU A O 1 ATOM 2513 C CB . GLU A 1 313 ? 3.393 58.104 69.216 1.00 25.06 ? 367 GLU A CB 1 ATOM 2514 C CG . GLU A 1 313 ? 3.715 59.310 70.142 1.00 25.17 ? 367 GLU A CG 1 ATOM 2515 C CD . GLU A 1 313 ? 4.697 60.234 69.460 1.00 27.47 ? 367 GLU A CD 1 ATOM 2516 O OE1 . GLU A 1 313 ? 4.245 61.124 68.703 1.00 28.22 ? 367 GLU A OE1 1 ATOM 2517 O OE2 . GLU A 1 313 ? 5.926 60.095 69.702 1.00 30.01 ? 367 GLU A OE2 1 ATOM 2518 N N . PRO A 1 314 ? 0.910 55.349 68.881 1.00 23.96 ? 368 PRO A N 1 ATOM 2519 C CA . PRO A 1 314 ? 0.623 54.232 67.989 1.00 23.27 ? 368 PRO A CA 1 ATOM 2520 C C . PRO A 1 314 ? 0.285 54.705 66.579 1.00 22.63 ? 368 PRO A C 1 ATOM 2521 O O . PRO A 1 314 ? 0.355 53.914 65.648 1.00 20.85 ? 368 PRO A O 1 ATOM 2522 C CB . PRO A 1 314 ? -0.614 53.582 68.609 1.00 24.00 ? 368 PRO A CB 1 ATOM 2523 C CG . PRO A 1 314 ? -1.202 54.630 69.458 1.00 25.67 ? 368 PRO A CG 1 ATOM 2524 C CD . PRO A 1 314 ? -0.095 55.434 69.961 1.00 24.80 ? 368 PRO A CD 1 ATOM 2525 N N . ASP A 1 315 ? -0.077 55.985 66.459 1.00 23.35 ? 369 ASP A N 1 ATOM 2526 C CA . ASP A 1 315 ? -0.341 56.576 65.139 1.00 22.89 ? 369 ASP A CA 1 ATOM 2527 C C . ASP A 1 315 ? 0.926 57.151 64.447 1.00 22.17 ? 369 ASP A C 1 ATOM 2528 O O . ASP A 1 315 ? 0.835 57.981 63.552 1.00 20.50 ? 369 ASP A O 1 ATOM 2529 C CB . ASP A 1 315 ? -1.444 57.639 65.306 1.00 22.91 ? 369 ASP A CB 1 ATOM 2530 C CG . ASP A 1 315 ? -0.939 58.881 65.973 1.00 25.72 ? 369 ASP A CG 1 ATOM 2531 O OD1 . ASP A 1 315 ? 0.037 58.786 66.726 1.00 28.25 ? 369 ASP A OD1 1 ATOM 2532 O OD2 . ASP A 1 315 ? -1.470 59.986 65.708 1.00 31.79 ? 369 ASP A OD2 1 ATOM 2533 N N . ARG A 1 316 ? 2.111 56.693 64.842 1.00 21.07 ? 370 ARG A N 1 ATOM 2534 C CA . ARG A 1 316 ? 3.347 57.084 64.176 1.00 20.79 ? 370 ARG A CA 1 ATOM 2535 C C . ARG A 1 316 ? 4.030 55.799 63.826 1.00 20.86 ? 370 ARG A C 1 ATOM 2536 O O . ARG A 1 316 ? 4.164 54.907 64.704 1.00 20.11 ? 370 ARG A O 1 ATOM 2537 C CB . ARG A 1 316 ? 4.239 57.913 65.121 1.00 21.11 ? 370 ARG A CB 1 ATOM 2538 C CG . ARG A 1 316 ? 3.540 59.255 65.425 1.00 21.00 ? 370 ARG A CG 1 ATOM 2539 C CD . ARG A 1 316 ? 3.804 60.165 64.245 1.00 22.78 ? 370 ARG A CD 1 ATOM 2540 N NE . ARG A 1 316 ? 3.145 61.493 64.291 1.00 21.43 ? 370 ARG A NE 1 ATOM 2541 C CZ . ARG A 1 316 ? 1.924 61.795 63.839 1.00 22.14 ? 370 ARG A CZ 1 ATOM 2542 N NH1 . ARG A 1 316 ? 1.072 60.873 63.381 1.00 20.54 ? 370 ARG A NH1 1 ATOM 2543 N NH2 . ARG A 1 316 ? 1.533 63.086 63.829 1.00 21.65 ? 370 ARG A NH2 1 ATOM 2544 N N . TYR A 1 317 ? 4.394 55.653 62.548 1.00 20.02 ? 371 TYR A N 1 ATOM 2545 C CA . TYR A 1 317 ? 4.908 54.370 62.038 1.00 20.51 ? 371 TYR A CA 1 ATOM 2546 C C . TYR A 1 317 ? 6.359 54.439 61.675 1.00 19.83 ? 371 TYR A C 1 ATOM 2547 O O . TYR A 1 317 ? 6.815 55.275 60.830 1.00 20.86 ? 371 TYR A O 1 ATOM 2548 C CB . TYR A 1 317 ? 4.190 53.941 60.752 1.00 19.90 ? 371 TYR A CB 1 ATOM 2549 C CG . TYR A 1 317 ? 2.684 53.893 60.868 1.00 19.52 ? 371 TYR A CG 1 ATOM 2550 C CD1 . TYR A 1 317 ? 2.055 53.489 62.068 1.00 22.81 ? 371 TYR A CD1 1 ATOM 2551 C CD2 . TYR A 1 317 ? 1.881 54.223 59.781 1.00 21.13 ? 371 TYR A CD2 1 ATOM 2552 C CE1 . TYR A 1 317 ? 0.667 53.451 62.177 1.00 22.73 ? 371 TYR A CE1 1 ATOM 2553 C CE2 . TYR A 1 317 ? 0.504 54.160 59.867 1.00 19.47 ? 371 TYR A CE2 1 ATOM 2554 C CZ . TYR A 1 317 ? -0.104 53.787 61.066 1.00 24.64 ? 371 TYR A CZ 1 ATOM 2555 O OH . TYR A 1 317 ? -1.473 53.730 61.148 1.00 22.45 ? 371 TYR A OH 1 ATOM 2556 N N . VAL A 1 318 ? 7.076 53.458 62.196 1.00 19.78 ? 372 VAL A N 1 ATOM 2557 C CA . VAL A 1 318 ? 8.456 53.231 61.762 1.00 19.28 ? 372 VAL A CA 1 ATOM 2558 C C . VAL A 1 318 ? 8.444 51.886 61.041 1.00 18.81 ? 372 VAL A C 1 ATOM 2559 O O . VAL A 1 318 ? 8.032 50.869 61.586 1.00 20.24 ? 372 VAL A O 1 ATOM 2560 C CB . VAL A 1 318 ? 9.432 53.207 62.981 1.00 19.24 ? 372 VAL A CB 1 ATOM 2561 C CG1 . VAL A 1 318 ? 10.896 52.821 62.521 1.00 21.38 ? 372 VAL A CG1 1 ATOM 2562 C CG2 . VAL A 1 318 ? 9.426 54.579 63.709 1.00 20.43 ? 372 VAL A CG2 1 ATOM 2563 N N . ILE A 1 319 ? 8.909 51.894 59.806 1.00 17.75 ? 373 ILE A N 1 ATOM 2564 C CA . ILE A 1 319 ? 8.770 50.714 58.943 1.00 18.29 ? 373 ILE A CA 1 ATOM 2565 C C . ILE A 1 319 ? 10.114 50.074 58.670 1.00 18.98 ? 373 ILE A C 1 ATOM 2566 O O . ILE A 1 319 ? 11.058 50.733 58.256 1.00 19.70 ? 373 ILE A O 1 ATOM 2567 C CB . ILE A 1 319 ? 8.049 51.080 57.595 1.00 17.23 ? 373 ILE A CB 1 ATOM 2568 C CG1 . ILE A 1 319 ? 6.709 51.818 57.904 1.00 19.29 ? 373 ILE A CG1 1 ATOM 2569 C CG2 . ILE A 1 319 ? 7.883 49.757 56.690 1.00 16.52 ? 373 ILE A CG2 1 ATOM 2570 C CD1 . ILE A 1 319 ? 6.108 52.442 56.602 1.00 25.04 ? 373 ILE A CD1 1 ATOM 2571 N N . LEU A 1 320 ? 10.195 48.755 58.887 1.00 17.93 ? 374 LEU A N 1 ATOM 2572 C CA . LEU A 1 320 ? 11.368 48.008 58.458 1.00 17.72 ? 374 LEU A CA 1 ATOM 2573 C C . LEU A 1 320 ? 10.908 47.034 57.390 1.00 17.66 ? 374 LEU A C 1 ATOM 2574 O O . LEU A 1 320 ? 10.108 46.119 57.687 1.00 19.88 ? 374 LEU A O 1 ATOM 2575 C CB . LEU A 1 320 ? 11.965 47.205 59.633 1.00 17.96 ? 374 LEU A CB 1 ATOM 2576 C CG . LEU A 1 320 ? 13.127 46.248 59.281 1.00 19.14 ? 374 LEU A CG 1 ATOM 2577 C CD1 . LEU A 1 320 ? 14.377 47.002 58.773 1.00 19.80 ? 374 LEU A CD1 1 ATOM 2578 C CD2 . LEU A 1 320 ? 13.413 45.415 60.548 1.00 19.85 ? 374 LEU A CD2 1 ATOM 2579 N N . GLY A 1 321 ? 11.398 47.196 56.157 1.00 18.08 ? 375 GLY A N 1 ATOM 2580 C CA . GLY A 1 321 ? 10.836 46.403 55.044 1.00 17.55 ? 375 GLY A CA 1 ATOM 2581 C C . GLY A 1 321 ? 11.909 45.899 54.099 1.00 19.21 ? 375 GLY A C 1 ATOM 2582 O O . GLY A 1 321 ? 12.870 46.618 53.822 1.00 19.40 ? 375 GLY A O 1 ATOM 2583 N N . GLY A 1 322 ? 11.732 44.675 53.565 1.00 18.82 ? 376 GLY A N 1 ATOM 2584 C CA . GLY A 1 322 ? 12.646 44.190 52.532 1.00 19.27 ? 376 GLY A CA 1 ATOM 2585 C C . GLY A 1 322 ? 11.919 43.064 51.820 1.00 18.98 ? 376 GLY A C 1 ATOM 2586 O O . GLY A 1 322 ? 10.926 42.541 52.346 1.00 20.27 ? 376 GLY A O 1 ATOM 2587 N N . HIS A 1 323 ? 12.404 42.685 50.657 1.00 18.42 ? 377 HIS A N 1 ATOM 2588 C CA . HIS A 1 323 ? 11.651 41.731 49.833 1.00 17.77 ? 377 HIS A CA 1 ATOM 2589 C C . HIS A 1 323 ? 11.990 40.272 50.172 1.00 20.28 ? 377 HIS A C 1 ATOM 2590 O O . HIS A 1 323 ? 12.996 40.002 50.829 1.00 20.82 ? 377 HIS A O 1 ATOM 2591 C CB . HIS A 1 323 ? 11.829 42.034 48.314 1.00 17.37 ? 377 HIS A CB 1 ATOM 2592 C CG . HIS A 1 323 ? 13.171 41.703 47.702 1.00 14.47 ? 377 HIS A CG 1 ATOM 2593 N ND1 . HIS A 1 323 ? 13.324 40.615 46.851 1.00 17.29 ? 377 HIS A ND1 1 ATOM 2594 C CD2 . HIS A 1 323 ? 14.331 42.408 47.598 1.00 15.99 ? 377 HIS A CD2 1 ATOM 2595 C CE1 . HIS A 1 323 ? 14.543 40.585 46.360 1.00 18.05 ? 377 HIS A CE1 1 ATOM 2596 N NE2 . HIS A 1 323 ? 15.170 41.680 46.751 1.00 18.25 ? 377 HIS A NE2 1 ATOM 2597 N N . ARG A 1 324 ? 11.158 39.370 49.675 1.00 19.72 ? 378 ARG A N 1 ATOM 2598 C CA . ARG A 1 324 ? 11.216 37.954 50.014 1.00 20.22 ? 378 ARG A CA 1 ATOM 2599 C C . ARG A 1 324 ? 11.370 37.189 48.728 1.00 20.53 ? 378 ARG A C 1 ATOM 2600 O O . ARG A 1 324 ? 11.909 36.061 48.744 1.00 20.66 ? 378 ARG A O 1 ATOM 2601 C CB . ARG A 1 324 ? 9.870 37.568 50.643 1.00 21.08 ? 378 ARG A CB 1 ATOM 2602 C CG . ARG A 1 324 ? 9.736 36.079 51.038 1.00 20.09 ? 378 ARG A CG 1 ATOM 2603 C CD . ARG A 1 324 ? 8.338 35.744 51.530 1.00 22.69 ? 378 ARG A CD 1 ATOM 2604 N NE . ARG A 1 324 ? 7.348 35.799 50.426 1.00 22.37 ? 378 ARG A NE 1 ATOM 2605 C CZ . ARG A 1 324 ? 6.461 36.768 50.235 1.00 20.46 ? 378 ARG A CZ 1 ATOM 2606 N NH1 . ARG A 1 324 ? 6.360 37.810 51.079 1.00 20.85 ? 378 ARG A NH1 1 ATOM 2607 N NH2 . ARG A 1 324 ? 5.614 36.695 49.190 1.00 22.01 ? 378 ARG A NH2 1 ATOM 2608 N N . ASP A 1 325 ? 10.833 37.732 47.618 1.00 19.67 ? 379 ASP A N 1 ATOM 2609 C CA . ASP A 1 325 ? 10.880 37.014 46.330 1.00 19.43 ? 379 ASP A CA 1 ATOM 2610 C C . ASP A 1 325 ? 12.329 37.011 45.837 1.00 20.01 ? 379 ASP A C 1 ATOM 2611 O O . ASP A 1 325 ? 13.062 37.978 46.041 1.00 19.77 ? 379 ASP A O 1 ATOM 2612 C CB . ASP A 1 325 ? 9.970 37.670 45.288 1.00 18.60 ? 379 ASP A CB 1 ATOM 2613 C CG . ASP A 1 325 ? 10.435 39.088 44.931 1.00 18.24 ? 379 ASP A CG 1 ATOM 2614 O OD1 . ASP A 1 325 ? 10.475 39.954 45.833 1.00 19.05 ? 379 ASP A OD1 1 ATOM 2615 O OD2 . ASP A 1 325 ? 10.684 39.324 43.746 1.00 18.82 ? 379 ASP A OD2 1 ATOM 2616 N N . SER A 1 326 ? 12.743 35.924 45.199 1.00 19.96 ? 380 SER A N 1 ATOM 2617 C CA . SER A 1 326 ? 14.108 35.813 44.680 1.00 20.51 ? 380 SER A CA 1 ATOM 2618 C C . SER A 1 326 ? 14.064 35.281 43.236 1.00 21.26 ? 380 SER A C 1 ATOM 2619 O O . SER A 1 326 ? 13.043 34.697 42.798 1.00 21.70 ? 380 SER A O 1 ATOM 2620 C CB . SER A 1 326 ? 14.920 34.846 45.562 1.00 20.89 ? 380 SER A CB 1 ATOM 2621 O OG . SER A 1 326 ? 14.285 33.556 45.525 1.00 22.00 ? 380 SER A OG 1 ATOM 2622 N N . TRP A 1 327 ? 15.128 35.507 42.473 1.00 21.24 ? 381 TRP A N 1 ATOM 2623 C CA . TRP A 1 327 ? 15.189 34.925 41.117 1.00 22.44 ? 381 TRP A CA 1 ATOM 2624 C C . TRP A 1 327 ? 15.271 33.406 41.195 1.00 23.17 ? 381 TRP A C 1 ATOM 2625 O O . TRP A 1 327 ? 14.523 32.735 40.549 1.00 22.58 ? 381 TRP A O 1 ATOM 2626 C CB . TRP A 1 327 ? 16.346 35.493 40.250 1.00 21.88 ? 381 TRP A CB 1 ATOM 2627 C CG . TRP A 1 327 ? 15.910 36.846 39.740 1.00 20.81 ? 381 TRP A CG 1 ATOM 2628 C CD1 . TRP A 1 327 ? 16.480 38.083 40.035 1.00 21.57 ? 381 TRP A CD1 1 ATOM 2629 C CD2 . TRP A 1 327 ? 14.787 37.102 38.899 1.00 21.83 ? 381 TRP A CD2 1 ATOM 2630 N NE1 . TRP A 1 327 ? 15.729 39.097 39.407 1.00 23.27 ? 381 TRP A NE1 1 ATOM 2631 C CE2 . TRP A 1 327 ? 14.720 38.511 38.682 1.00 22.75 ? 381 TRP A CE2 1 ATOM 2632 C CE3 . TRP A 1 327 ? 13.844 36.270 38.239 1.00 21.56 ? 381 TRP A CE3 1 ATOM 2633 C CZ2 . TRP A 1 327 ? 13.712 39.089 37.892 1.00 21.30 ? 381 TRP A CZ2 1 ATOM 2634 C CZ3 . TRP A 1 327 ? 12.834 36.863 37.455 1.00 21.07 ? 381 TRP A CZ3 1 ATOM 2635 C CH2 . TRP A 1 327 ? 12.764 38.258 37.324 1.00 21.83 ? 381 TRP A CH2 1 ATOM 2636 N N . VAL A 1 328 ? 16.148 32.884 42.057 1.00 23.77 ? 382 VAL A N 1 ATOM 2637 C CA . VAL A 1 328 ? 16.181 31.442 42.272 1.00 24.21 ? 382 VAL A CA 1 ATOM 2638 C C . VAL A 1 328 ? 16.248 31.194 43.782 1.00 23.94 ? 382 VAL A C 1 ATOM 2639 O O . VAL A 1 328 ? 15.244 31.369 44.459 1.00 23.68 ? 382 VAL A O 1 ATOM 2640 C CB . VAL A 1 328 ? 17.352 30.737 41.474 1.00 24.06 ? 382 VAL A CB 1 ATOM 2641 C CG1 . VAL A 1 328 ? 17.184 29.182 41.565 1.00 26.17 ? 382 VAL A CG1 1 ATOM 2642 C CG2 . VAL A 1 328 ? 17.309 31.114 39.991 1.00 24.84 ? 382 VAL A CG2 1 ATOM 2643 N N . PHE A 1 329 ? 17.398 30.780 44.313 1.00 23.27 ? 383 PHE A N 1 ATOM 2644 C CA . PHE A 1 329 ? 17.446 30.460 45.750 1.00 22.02 ? 383 PHE A CA 1 ATOM 2645 C C . PHE A 1 329 ? 17.592 31.672 46.650 1.00 21.83 ? 383 PHE A C 1 ATOM 2646 O O . PHE A 1 329 ? 17.281 31.574 47.825 1.00 22.12 ? 383 PHE A O 1 ATOM 2647 C CB . PHE A 1 329 ? 18.578 29.451 46.057 1.00 22.18 ? 383 PHE A CB 1 ATOM 2648 C CG . PHE A 1 329 ? 18.412 28.192 45.272 1.00 22.50 ? 383 PHE A CG 1 ATOM 2649 C CD1 . PHE A 1 329 ? 17.394 27.290 45.625 1.00 22.76 ? 383 PHE A CD1 1 ATOM 2650 C CD2 . PHE A 1 329 ? 19.220 27.931 44.154 1.00 25.39 ? 383 PHE A CD2 1 ATOM 2651 C CE1 . PHE A 1 329 ? 17.203 26.088 44.880 1.00 25.67 ? 383 PHE A CE1 1 ATOM 2652 C CE2 . PHE A 1 329 ? 19.026 26.746 43.404 1.00 26.21 ? 383 PHE A CE2 1 ATOM 2653 C CZ . PHE A 1 329 ? 17.982 25.862 43.757 1.00 24.70 ? 383 PHE A CZ 1 ATOM 2654 N N . GLY A 1 330 ? 18.052 32.801 46.094 1.00 22.41 ? 384 GLY A N 1 ATOM 2655 C CA . GLY A 1 330 ? 18.104 34.058 46.893 1.00 21.24 ? 384 GLY A CA 1 ATOM 2656 C C . GLY A 1 330 ? 19.073 33.997 48.070 1.00 22.22 ? 384 GLY A C 1 ATOM 2657 O O . GLY A 1 330 ? 18.898 34.671 49.069 1.00 22.42 ? 384 GLY A O 1 ATOM 2658 N N . GLY A 1 331 ? 20.181 33.263 47.895 1.00 22.14 ? 385 GLY A N 1 ATOM 2659 C CA . GLY A 1 331 ? 21.104 33.064 49.015 1.00 21.93 ? 385 GLY A CA 1 ATOM 2660 C C . GLY A 1 331 ? 21.622 34.383 49.547 1.00 21.84 ? 385 GLY A C 1 ATOM 2661 O O . GLY A 1 331 ? 21.783 34.554 50.753 1.00 22.20 ? 385 GLY A O 1 ATOM 2662 N N . ILE A 1 332 ? 21.929 35.313 48.640 1.00 22.06 ? 386 ILE A N 1 ATOM 2663 C CA . ILE A 1 332 ? 22.248 36.664 49.114 1.00 21.92 ? 386 ILE A CA 1 ATOM 2664 C C . ILE A 1 332 ? 20.966 37.523 48.928 1.00 21.55 ? 386 ILE A C 1 ATOM 2665 O O . ILE A 1 332 ? 20.463 38.138 49.890 1.00 23.49 ? 386 ILE A O 1 ATOM 2666 C CB . ILE A 1 332 ? 23.451 37.293 48.351 1.00 21.63 ? 386 ILE A CB 1 ATOM 2667 C CG1 . ILE A 1 332 ? 24.784 36.615 48.798 1.00 23.88 ? 386 ILE A CG1 1 ATOM 2668 C CG2 . ILE A 1 332 ? 23.592 38.834 48.610 1.00 22.64 ? 386 ILE A CG2 1 ATOM 2669 C CD1 . ILE A 1 332 ? 25.962 37.013 47.957 1.00 27.78 ? 386 ILE A CD1 1 ATOM 2670 N N . ASP A 1 333 ? 20.488 37.544 47.693 1.00 21.70 ? 387 ASP A N 1 ATOM 2671 C CA . ASP A 1 333 ? 19.395 38.480 47.269 1.00 21.21 ? 387 ASP A CA 1 ATOM 2672 C C . ASP A 1 333 ? 18.042 37.739 47.208 1.00 20.16 ? 387 ASP A C 1 ATOM 2673 O O . ASP A 1 333 ? 17.769 37.010 46.247 1.00 22.22 ? 387 ASP A O 1 ATOM 2674 C CB . ASP A 1 333 ? 19.766 39.026 45.908 1.00 22.44 ? 387 ASP A CB 1 ATOM 2675 C CG . ASP A 1 333 ? 18.823 40.088 45.423 1.00 22.46 ? 387 ASP A CG 1 ATOM 2676 O OD1 . ASP A 1 333 ? 17.855 40.312 46.152 1.00 20.86 ? 387 ASP A OD1 1 ATOM 2677 O OD2 . ASP A 1 333 ? 19.022 40.610 44.274 1.00 22.22 ? 387 ASP A OD2 1 ATOM 2678 N N . PRO A 1 334 ? 17.161 37.970 48.189 1.00 19.90 ? 388 PRO A N 1 ATOM 2679 C CA . PRO A 1 334 ? 17.197 38.870 49.347 1.00 19.25 ? 388 PRO A CA 1 ATOM 2680 C C . PRO A 1 334 ? 17.341 38.134 50.674 1.00 20.02 ? 388 PRO A C 1 ATOM 2681 O O . PRO A 1 334 ? 17.241 38.763 51.740 1.00 20.56 ? 388 PRO A O 1 ATOM 2682 C CB . PRO A 1 334 ? 15.779 39.485 49.302 1.00 19.46 ? 388 PRO A CB 1 ATOM 2683 C CG . PRO A 1 334 ? 14.915 38.245 48.922 1.00 18.48 ? 388 PRO A CG 1 ATOM 2684 C CD . PRO A 1 334 ? 15.804 37.358 48.050 1.00 19.42 ? 388 PRO A CD 1 ATOM 2685 N N . GLN A 1 335 ? 17.551 36.811 50.657 1.00 20.34 ? 389 GLN A N 1 ATOM 2686 C CA . GLN A 1 335 ? 17.355 36.108 51.943 1.00 21.90 ? 389 GLN A CA 1 ATOM 2687 C C . GLN A 1 335 ? 18.417 36.442 53.004 1.00 21.15 ? 389 GLN A C 1 ATOM 2688 O O . GLN A 1 335 ? 18.124 36.343 54.185 1.00 22.43 ? 389 GLN A O 1 ATOM 2689 C CB . GLN A 1 335 ? 17.174 34.560 51.785 1.00 20.79 ? 389 GLN A CB 1 ATOM 2690 C CG . GLN A 1 335 ? 16.187 34.099 50.707 1.00 21.02 ? 389 GLN A CG 1 ATOM 2691 C CD . GLN A 1 335 ? 14.750 34.687 50.913 1.00 19.79 ? 389 GLN A CD 1 ATOM 2692 O OE1 . GLN A 1 335 ? 14.443 35.265 51.963 1.00 22.47 ? 389 GLN A OE1 1 ATOM 2693 N NE2 . GLN A 1 335 ? 13.891 34.500 49.915 1.00 20.08 ? 389 GLN A NE2 1 ATOM 2694 N N . SER A 1 336 ? 19.620 36.895 52.612 1.00 21.82 ? 390 SER A N 1 ATOM 2695 C CA . SER A 1 336 ? 20.533 37.419 53.635 1.00 23.16 ? 390 SER A CA 1 ATOM 2696 C C . SER A 1 336 ? 19.928 38.609 54.376 1.00 22.80 ? 390 SER A C 1 ATOM 2697 O O . SER A 1 336 ? 20.249 38.817 55.556 1.00 22.92 ? 390 SER A O 1 ATOM 2698 C CB . SER A 1 336 ? 21.943 37.773 53.124 1.00 23.74 ? 390 SER A CB 1 ATOM 2699 O OG . SER A 1 336 ? 21.873 38.767 52.143 1.00 27.73 ? 390 SER A OG 1 ATOM 2700 N N . GLY A 1 337 ? 19.132 39.406 53.681 1.00 21.54 ? 391 GLY A N 1 ATOM 2701 C CA . GLY A 1 337 ? 18.364 40.494 54.317 1.00 20.52 ? 391 GLY A CA 1 ATOM 2702 C C . GLY A 1 337 ? 17.145 40.005 55.082 1.00 20.72 ? 391 GLY A C 1 ATOM 2703 O O . GLY A 1 337 ? 16.916 40.424 56.235 1.00 22.00 ? 391 GLY A O 1 ATOM 2704 N N . ALA A 1 338 ? 16.372 39.107 54.470 1.00 20.36 ? 392 ALA A N 1 ATOM 2705 C CA . ALA A 1 338 ? 15.123 38.664 55.112 1.00 20.97 ? 392 ALA A CA 1 ATOM 2706 C C . ALA A 1 338 ? 15.367 37.867 56.416 1.00 20.72 ? 392 ALA A C 1 ATOM 2707 O O . ALA A 1 338 ? 14.588 37.971 57.366 1.00 20.39 ? 392 ALA A O 1 ATOM 2708 C CB . ALA A 1 338 ? 14.291 37.845 54.143 1.00 19.50 ? 392 ALA A CB 1 ATOM 2709 N N . ALA A 1 339 ? 16.499 37.137 56.467 1.00 21.99 ? 393 ALA A N 1 ATOM 2710 C CA . ALA A 1 339 ? 16.871 36.376 57.682 1.00 21.86 ? 393 ALA A CA 1 ATOM 2711 C C . ALA A 1 339 ? 17.199 37.337 58.799 1.00 21.85 ? 393 ALA A C 1 ATOM 2712 O O . ALA A 1 339 ? 16.923 37.094 59.988 1.00 21.46 ? 393 ALA A O 1 ATOM 2713 C CB . ALA A 1 339 ? 18.133 35.496 57.379 1.00 21.80 ? 393 ALA A CB 1 ATOM 2714 N N . VAL A 1 340 ? 17.814 38.453 58.422 1.00 22.14 ? 394 VAL A N 1 ATOM 2715 C CA . VAL A 1 340 ? 18.103 39.538 59.365 1.00 22.12 ? 394 VAL A CA 1 ATOM 2716 C C . VAL A 1 340 ? 16.820 40.159 59.903 1.00 22.21 ? 394 VAL A C 1 ATOM 2717 O O . VAL A 1 340 ? 16.685 40.359 61.116 1.00 20.85 ? 394 VAL A O 1 ATOM 2718 C CB . VAL A 1 340 ? 19.054 40.602 58.723 1.00 22.09 ? 394 VAL A CB 1 ATOM 2719 C CG1 . VAL A 1 340 ? 18.946 41.952 59.466 1.00 20.80 ? 394 VAL A CG1 1 ATOM 2720 C CG2 . VAL A 1 340 ? 20.533 40.078 58.772 1.00 23.54 ? 394 VAL A CG2 1 ATOM 2721 N N . VAL A 1 341 ? 15.887 40.469 59.001 1.00 21.77 ? 395 VAL A N 1 ATOM 2722 C CA . VAL A 1 341 ? 14.613 41.009 59.444 1.00 21.74 ? 395 VAL A CA 1 ATOM 2723 C C . VAL A 1 341 ? 13.918 40.007 60.407 1.00 21.87 ? 395 VAL A C 1 ATOM 2724 O O . VAL A 1 341 ? 13.387 40.395 61.397 1.00 22.23 ? 395 VAL A O 1 ATOM 2725 C CB . VAL A 1 341 ? 13.673 41.320 58.281 1.00 22.21 ? 395 VAL A CB 1 ATOM 2726 C CG1 . VAL A 1 341 ? 12.257 41.730 58.830 1.00 20.77 ? 395 VAL A CG1 1 ATOM 2727 C CG2 . VAL A 1 341 ? 14.284 42.411 57.399 1.00 22.86 ? 395 VAL A CG2 1 ATOM 2728 N N . HIS A 1 342 ? 13.947 38.719 60.092 1.00 22.32 ? 396 HIS A N 1 ATOM 2729 C CA . HIS A 1 342 ? 13.251 37.693 60.899 1.00 21.96 ? 396 HIS A CA 1 ATOM 2730 C C . HIS A 1 342 ? 13.821 37.701 62.318 1.00 23.71 ? 396 HIS A C 1 ATOM 2731 O O . HIS A 1 342 ? 13.054 37.617 63.301 1.00 24.21 ? 396 HIS A O 1 ATOM 2732 C CB . HIS A 1 342 ? 13.476 36.334 60.203 1.00 22.88 ? 396 HIS A CB 1 ATOM 2733 C CG . HIS A 1 342 ? 12.333 35.384 60.297 1.00 25.22 ? 396 HIS A CG 1 ATOM 2734 N ND1 . HIS A 1 342 ? 11.040 35.726 59.964 1.00 24.74 ? 396 HIS A ND1 1 ATOM 2735 C CD2 . HIS A 1 342 ? 12.302 34.065 60.630 1.00 26.71 ? 396 HIS A CD2 1 ATOM 2736 C CE1 . HIS A 1 342 ? 10.253 34.669 60.118 1.00 26.85 ? 396 HIS A CE1 1 ATOM 2737 N NE2 . HIS A 1 342 ? 10.991 33.658 60.551 1.00 25.98 ? 396 HIS A NE2 1 ATOM 2738 N N . GLU A 1 343 ? 15.158 37.802 62.444 1.00 24.19 ? 397 GLU A N 1 ATOM 2739 C CA . GLU A 1 343 ? 15.798 37.822 63.775 1.00 25.79 ? 397 GLU A CA 1 ATOM 2740 C C . GLU A 1 343 ? 15.509 39.134 64.503 1.00 26.38 ? 397 GLU A C 1 ATOM 2741 O O . GLU A 1 343 ? 15.362 39.176 65.730 1.00 25.79 ? 397 GLU A O 1 ATOM 2742 C CB . GLU A 1 343 ? 17.313 37.607 63.643 1.00 26.64 ? 397 GLU A CB 1 ATOM 2743 C CG . GLU A 1 343 ? 18.110 37.660 65.007 1.00 27.74 ? 397 GLU A CG 1 ATOM 2744 C CD . GLU A 1 343 ? 17.767 36.527 65.972 1.00 32.03 ? 397 GLU A CD 1 ATOM 2745 O OE1 . GLU A 1 343 ? 16.764 35.806 65.734 1.00 29.57 ? 397 GLU A OE1 1 ATOM 2746 O OE2 . GLU A 1 343 ? 18.523 36.354 66.979 1.00 30.89 ? 397 GLU A OE2 1 ATOM 2747 N N . ILE A 1 344 ? 15.407 40.232 63.746 1.00 25.65 ? 398 ILE A N 1 ATOM 2748 C CA . ILE A 1 344 ? 15.003 41.507 64.359 1.00 23.69 ? 398 ILE A CA 1 ATOM 2749 C C . ILE A 1 344 ? 13.600 41.434 64.950 1.00 23.73 ? 398 ILE A C 1 ATOM 2750 O O . ILE A 1 344 ? 13.369 41.889 66.071 1.00 24.79 ? 398 ILE A O 1 ATOM 2751 C CB . ILE A 1 344 ? 15.139 42.700 63.326 1.00 22.37 ? 398 ILE A CB 1 ATOM 2752 C CG1 . ILE A 1 344 ? 16.629 43.043 63.165 1.00 23.11 ? 398 ILE A CG1 1 ATOM 2753 C CG2 . ILE A 1 344 ? 14.384 43.990 63.815 1.00 20.52 ? 398 ILE A CG2 1 ATOM 2754 C CD1 . ILE A 1 344 ? 16.944 43.899 61.907 1.00 20.83 ? 398 ILE A CD1 1 ATOM 2755 N N . VAL A 1 345 ? 12.662 40.861 64.210 1.00 24.36 ? 399 VAL A N 1 ATOM 2756 C CA . VAL A 1 345 ? 11.290 40.682 64.706 1.00 25.27 ? 399 VAL A CA 1 ATOM 2757 C C . VAL A 1 345 ? 11.292 39.780 65.959 1.00 26.03 ? 399 VAL A C 1 ATOM 2758 O O . VAL A 1 345 ? 10.622 40.094 66.961 1.00 26.55 ? 399 VAL A O 1 ATOM 2759 C CB . VAL A 1 345 ? 10.380 40.006 63.643 1.00 24.48 ? 399 VAL A CB 1 ATOM 2760 C CG1 . VAL A 1 345 ? 9.011 39.652 64.242 1.00 25.57 ? 399 VAL A CG1 1 ATOM 2761 C CG2 . VAL A 1 345 ? 10.181 40.972 62.377 1.00 22.98 ? 399 VAL A CG2 1 ATOM 2762 N N . ARG A 1 346 ? 12.065 38.696 65.872 1.00 27.59 ? 400 ARG A N 1 ATOM 2763 C CA . ARG A 1 346 ? 12.176 37.764 67.018 1.00 27.58 ? 400 ARG A CA 1 ATOM 2764 C C . ARG A 1 346 ? 12.655 38.501 68.263 1.00 28.76 ? 400 ARG A C 1 ATOM 2765 O O . ARG A 1 346 ? 12.059 38.332 69.329 1.00 29.68 ? 400 ARG A O 1 ATOM 2766 C CB . ARG A 1 346 ? 13.057 36.553 66.683 1.00 27.25 ? 400 ARG A CB 1 ATOM 2767 C CG . ARG A 1 346 ? 12.932 35.424 67.789 1.00 28.63 ? 400 ARG A CG 1 ATOM 2768 C CD . ARG A 1 346 ? 14.096 34.373 67.646 1.00 29.18 ? 400 ARG A CD 1 ATOM 2769 N NE . ARG A 1 346 ? 15.361 35.024 67.953 1.00 28.66 ? 400 ARG A NE 1 ATOM 2770 C CZ . ARG A 1 346 ? 15.738 35.387 69.192 1.00 31.99 ? 400 ARG A CZ 1 ATOM 2771 N NH1 . ARG A 1 346 ? 16.907 35.983 69.392 1.00 31.60 ? 400 ARG A NH1 1 ATOM 2772 N NH2 . ARG A 1 346 ? 14.962 35.106 70.253 1.00 31.74 ? 400 ARG A NH2 1 ATOM 2773 N N . SER A 1 347 ? 13.713 39.318 68.124 1.00 28.97 ? 401 SER A N 1 ATOM 2774 C CA A SER A 1 347 ? 14.258 40.121 69.243 0.50 28.82 ? 401 SER A CA 1 ATOM 2775 C CA B SER A 1 347 ? 14.240 40.079 69.233 0.50 29.96 ? 401 SER A CA 1 ATOM 2776 C C . SER A 1 347 ? 13.248 41.118 69.780 1.00 30.33 ? 401 SER A C 1 ATOM 2777 O O . SER A 1 347 ? 13.049 41.222 71.017 1.00 30.06 ? 401 SER A O 1 ATOM 2778 C CB A SER A 1 347 ? 15.579 40.839 68.898 0.50 28.52 ? 401 SER A CB 1 ATOM 2779 C CB B SER A 1 347 ? 15.597 40.649 68.839 0.50 29.69 ? 401 SER A CB 1 ATOM 2780 O OG A SER A 1 347 ? 16.102 41.575 70.029 0.50 24.60 ? 401 SER A OG 1 ATOM 2781 O OG B SER A 1 347 ? 16.466 39.560 68.522 0.50 32.70 ? 401 SER A OG 1 ATOM 2782 N N . PHE A 1 348 ? 12.589 41.877 68.888 1.00 28.61 ? 402 PHE A N 1 ATOM 2783 C CA . PHE A 1 348 ? 11.550 42.801 69.373 1.00 28.03 ? 402 PHE A CA 1 ATOM 2784 C C . PHE A 1 348 ? 10.412 42.045 70.082 1.00 28.74 ? 402 PHE A C 1 ATOM 2785 O O . PHE A 1 348 ? 9.882 42.529 71.103 1.00 30.17 ? 402 PHE A O 1 ATOM 2786 C CB . PHE A 1 348 ? 10.956 43.661 68.227 1.00 27.15 ? 402 PHE A CB 1 ATOM 2787 C CG . PHE A 1 348 ? 11.764 44.885 67.888 1.00 26.93 ? 402 PHE A CG 1 ATOM 2788 C CD1 . PHE A 1 348 ? 11.978 45.892 68.845 1.00 28.97 ? 402 PHE A CD1 1 ATOM 2789 C CD2 . PHE A 1 348 ? 12.277 45.067 66.589 1.00 26.99 ? 402 PHE A CD2 1 ATOM 2790 C CE1 . PHE A 1 348 ? 12.704 47.044 68.535 1.00 27.75 ? 402 PHE A CE1 1 ATOM 2791 C CE2 . PHE A 1 348 ? 13.003 46.221 66.254 1.00 25.83 ? 402 PHE A CE2 1 ATOM 2792 C CZ . PHE A 1 348 ? 13.215 47.221 67.213 1.00 26.10 ? 402 PHE A CZ 1 ATOM 2793 N N . GLY A 1 349 ? 10.036 40.874 69.564 1.00 27.61 ? 403 GLY A N 1 ATOM 2794 C CA . GLY A 1 349 ? 8.953 40.089 70.149 1.00 29.94 ? 403 GLY A CA 1 ATOM 2795 C C . GLY A 1 349 ? 9.341 39.562 71.540 1.00 31.17 ? 403 GLY A C 1 ATOM 2796 O O . GLY A 1 349 ? 8.501 39.474 72.426 1.00 32.38 ? 403 GLY A O 1 ATOM 2797 N N . THR A 1 350 ? 10.615 39.231 71.720 1.00 32.70 ? 404 THR A N 1 ATOM 2798 C CA . THR A 1 350 ? 11.123 38.826 73.046 1.00 33.77 ? 404 THR A CA 1 ATOM 2799 C C . THR A 1 350 ? 10.905 39.922 74.102 1.00 34.74 ? 404 THR A C 1 ATOM 2800 O O . THR A 1 350 ? 10.443 39.619 75.206 1.00 35.66 ? 404 THR A O 1 ATOM 2801 C CB . THR A 1 350 ? 12.617 38.360 73.022 1.00 33.54 ? 404 THR A CB 1 ATOM 2802 O OG1 A THR A 1 350 ? 12.740 37.241 72.130 0.50 31.98 ? 404 THR A OG1 1 ATOM 2803 O OG1 B THR A 1 350 ? 13.505 39.494 73.036 0.50 34.37 ? 404 THR A OG1 1 ATOM 2804 C CG2 A THR A 1 350 ? 13.126 37.982 74.398 0.50 31.88 ? 404 THR A CG2 1 ATOM 2805 C CG2 B THR A 1 350 ? 12.929 37.408 71.879 0.50 32.59 ? 404 THR A CG2 1 ATOM 2806 N N A LEU A 1 351 ? 11.195 41.182 73.764 0.70 34.54 ? 405 LEU A N 1 ATOM 2807 N N B LEU A 1 351 ? 11.225 41.176 73.774 0.30 34.11 ? 405 LEU A N 1 ATOM 2808 C CA A LEU A 1 351 ? 10.996 42.262 74.732 0.70 34.84 ? 405 LEU A CA 1 ATOM 2809 C CA B LEU A 1 351 ? 10.992 42.277 74.713 0.30 33.99 ? 405 LEU A CA 1 ATOM 2810 C C A LEU A 1 351 ? 9.501 42.474 74.925 0.70 34.93 ? 405 LEU A C 1 ATOM 2811 C C B LEU A 1 351 ? 9.504 42.489 74.919 0.30 34.23 ? 405 LEU A C 1 ATOM 2812 O O A LEU A 1 351 ? 9.039 42.710 76.052 0.70 34.63 ? 405 LEU A O 1 ATOM 2813 O O B LEU A 1 351 ? 9.056 42.748 76.042 0.30 34.30 ? 405 LEU A O 1 ATOM 2814 C CB A LEU A 1 351 ? 11.672 43.585 74.309 0.70 35.63 ? 405 LEU A CB 1 ATOM 2815 C CB B LEU A 1 351 ? 11.635 43.588 74.244 0.30 33.97 ? 405 LEU A CB 1 ATOM 2816 C CG A LEU A 1 351 ? 13.089 43.591 73.724 0.70 36.71 ? 405 LEU A CG 1 ATOM 2817 C CG B LEU A 1 351 ? 13.105 43.772 74.599 0.30 33.19 ? 405 LEU A CG 1 ATOM 2818 C CD1 A LEU A 1 351 ? 13.434 45.002 73.271 0.70 37.35 ? 405 LEU A CD1 1 ATOM 2819 C CD1 B LEU A 1 351 ? 13.930 42.744 73.843 0.30 32.18 ? 405 LEU A CD1 1 ATOM 2820 C CD2 A LEU A 1 351 ? 14.122 43.075 74.691 0.70 39.31 ? 405 LEU A CD2 1 ATOM 2821 C CD2 B LEU A 1 351 ? 13.549 45.178 74.262 0.30 33.82 ? 405 LEU A CD2 1 ATOM 2822 N N . LYS A 1 352 ? 8.742 42.371 73.834 1.00 33.17 ? 406 LYS A N 1 ATOM 2823 C CA . LYS A 1 352 ? 7.289 42.516 73.901 1.00 34.43 ? 406 LYS A CA 1 ATOM 2824 C C . LYS A 1 352 ? 6.667 41.494 74.888 1.00 35.46 ? 406 LYS A C 1 ATOM 2825 O O . LYS A 1 352 ? 5.819 41.865 75.691 1.00 35.39 ? 406 LYS A O 1 ATOM 2826 C CB . LYS A 1 352 ? 6.610 42.417 72.530 1.00 34.27 ? 406 LYS A CB 1 ATOM 2827 C CG . LYS A 1 352 ? 5.131 42.828 72.589 1.00 37.74 ? 406 LYS A CG 1 ATOM 2828 C CD . LYS A 1 352 ? 4.247 41.624 72.421 1.00 44.56 ? 406 LYS A CD 1 ATOM 2829 C CE . LYS A 1 352 ? 2.827 42.032 72.063 1.00 46.29 ? 406 LYS A CE 1 ATOM 2830 N NZ . LYS A 1 352 ? 2.099 40.814 71.663 1.00 50.75 ? 406 LYS A NZ 1 ATOM 2831 N N . LYS A 1 353 ? 7.094 40.237 74.807 1.00 35.95 ? 407 LYS A N 1 ATOM 2832 C CA . LYS A 1 353 ? 6.609 39.191 75.728 1.00 38.18 ? 407 LYS A CA 1 ATOM 2833 C C . LYS A 1 353 ? 6.897 39.447 77.196 1.00 39.60 ? 407 LYS A C 1 ATOM 2834 O O . LYS A 1 353 ? 6.181 38.929 78.069 1.00 41.14 ? 407 LYS A O 1 ATOM 2835 C CB . LYS A 1 353 ? 7.137 37.831 75.321 1.00 38.19 ? 407 LYS A CB 1 ATOM 2836 C CG . LYS A 1 353 ? 6.359 37.262 74.161 1.00 40.69 ? 407 LYS A CG 1 ATOM 2837 C CD . LYS A 1 353 ? 7.103 36.094 73.503 1.00 42.20 ? 407 LYS A CD 1 ATOM 2838 C CE . LYS A 1 353 ? 6.344 35.615 72.273 1.00 40.64 ? 407 LYS A CE 1 ATOM 2839 N NZ . LYS A 1 353 ? 6.793 34.279 71.928 1.00 44.38 ? 407 LYS A NZ 1 ATOM 2840 N N . GLU A 1 354 ? 7.934 40.230 77.462 1.00 40.61 ? 408 GLU A N 1 ATOM 2841 C CA . GLU A 1 354 ? 8.301 40.686 78.820 1.00 42.75 ? 408 GLU A CA 1 ATOM 2842 C C . GLU A 1 354 ? 7.614 41.968 79.255 1.00 42.45 ? 408 GLU A C 1 ATOM 2843 O O . GLU A 1 354 ? 7.887 42.517 80.350 1.00 42.91 ? 408 GLU A O 1 ATOM 2844 C CB . GLU A 1 354 ? 9.825 40.856 78.905 1.00 43.83 ? 408 GLU A CB 1 ATOM 2845 C CG . GLU A 1 354 ? 10.616 39.574 78.613 1.00 48.51 ? 408 GLU A CG 1 ATOM 2846 C CD . GLU A 1 354 ? 12.123 39.810 78.514 1.00 56.56 ? 408 GLU A CD 1 ATOM 2847 O OE1 . GLU A 1 354 ? 12.819 39.002 77.839 1.00 59.74 ? 408 GLU A OE1 1 ATOM 2848 O OE2 . GLU A 1 354 ? 12.618 40.805 79.106 1.00 59.97 ? 408 GLU A OE2 1 ATOM 2849 N N . GLY A 1 355 ? 6.706 42.461 78.413 1.00 40.62 ? 409 GLY A N 1 ATOM 2850 C CA . GLY A 1 355 ? 5.861 43.587 78.772 1.00 39.03 ? 409 GLY A CA 1 ATOM 2851 C C . GLY A 1 355 ? 6.263 44.905 78.140 1.00 38.61 ? 409 GLY A C 1 ATOM 2852 O O . GLY A 1 355 ? 5.643 45.917 78.391 1.00 38.84 ? 409 GLY A O 1 ATOM 2853 N N . TRP A 1 356 ? 7.309 44.901 77.316 1.00 36.85 ? 410 TRP A N 1 ATOM 2854 C CA . TRP A 1 356 ? 7.792 46.158 76.740 1.00 35.75 ? 410 TRP A CA 1 ATOM 2855 C C . TRP A 1 356 ? 7.036 46.409 75.435 1.00 33.60 ? 410 TRP A C 1 ATOM 2856 O O . TRP A 1 356 ? 6.632 45.467 74.743 1.00 33.73 ? 410 TRP A O 1 ATOM 2857 C CB . TRP A 1 356 ? 9.283 46.046 76.445 1.00 36.37 ? 410 TRP A CB 1 ATOM 2858 C CG . TRP A 1 356 ? 9.911 47.187 75.614 1.00 36.91 ? 410 TRP A CG 1 ATOM 2859 C CD1 . TRP A 1 356 ? 10.482 48.334 76.095 1.00 37.10 ? 410 TRP A CD1 1 ATOM 2860 C CD2 . TRP A 1 356 ? 10.061 47.229 74.186 1.00 35.23 ? 410 TRP A CD2 1 ATOM 2861 N NE1 . TRP A 1 356 ? 10.970 49.093 75.056 1.00 36.79 ? 410 TRP A NE1 1 ATOM 2862 C CE2 . TRP A 1 356 ? 10.724 48.443 73.872 1.00 35.74 ? 410 TRP A CE2 1 ATOM 2863 C CE3 . TRP A 1 356 ? 9.651 46.384 73.133 1.00 34.95 ? 410 TRP A CE3 1 ATOM 2864 C CZ2 . TRP A 1 356 ? 11.033 48.823 72.540 1.00 32.22 ? 410 TRP A CZ2 1 ATOM 2865 C CZ3 . TRP A 1 356 ? 9.955 46.758 71.801 1.00 34.86 ? 410 TRP A CZ3 1 ATOM 2866 C CH2 . TRP A 1 356 ? 10.640 47.981 71.527 1.00 31.60 ? 410 TRP A CH2 1 ATOM 2867 N N . ARG A 1 357 ? 6.861 47.676 75.115 1.00 31.53 ? 411 ARG A N 1 ATOM 2868 C CA . ARG A 1 357 ? 6.346 48.096 73.802 1.00 30.36 ? 411 ARG A CA 1 ATOM 2869 C C . ARG A 1 357 ? 7.152 49.290 73.366 1.00 28.89 ? 411 ARG A C 1 ATOM 2870 O O . ARG A 1 357 ? 7.546 50.096 74.202 1.00 27.77 ? 411 ARG A O 1 ATOM 2871 C CB . ARG A 1 357 ? 4.903 48.580 73.904 1.00 31.56 ? 411 ARG A CB 1 ATOM 2872 C CG . ARG A 1 357 ? 3.876 47.473 73.836 1.00 32.85 ? 411 ARG A CG 1 ATOM 2873 C CD . ARG A 1 357 ? 2.439 47.977 73.720 1.00 32.98 ? 411 ARG A CD 1 ATOM 2874 N NE . ARG A 1 357 ? 1.628 46.770 73.639 1.00 30.52 ? 411 ARG A NE 1 ATOM 2875 C CZ . ARG A 1 357 ? 1.470 46.041 72.530 1.00 34.86 ? 411 ARG A CZ 1 ATOM 2876 N NH1 . ARG A 1 357 ? 1.998 46.453 71.357 1.00 28.63 ? 411 ARG A NH1 1 ATOM 2877 N NH2 . ARG A 1 357 ? 0.779 44.909 72.593 1.00 32.09 ? 411 ARG A NH2 1 ATOM 2878 N N . PRO A 1 358 ? 7.392 49.431 72.025 1.00 26.77 ? 412 PRO A N 1 ATOM 2879 C CA . PRO A 1 358 ? 8.053 50.635 71.569 1.00 26.19 ? 412 PRO A CA 1 ATOM 2880 C C . PRO A 1 358 ? 7.175 51.846 71.784 1.00 24.72 ? 412 PRO A C 1 ATOM 2881 O O . PRO A 1 358 ? 5.963 51.718 71.897 1.00 26.70 ? 412 PRO A O 1 ATOM 2882 C CB . PRO A 1 358 ? 8.278 50.376 70.030 1.00 24.91 ? 412 PRO A CB 1 ATOM 2883 C CG . PRO A 1 358 ? 7.185 49.402 69.656 1.00 25.95 ? 412 PRO A CG 1 ATOM 2884 C CD . PRO A 1 358 ? 7.024 48.518 70.931 1.00 25.56 ? 412 PRO A CD 1 ATOM 2885 N N . ARG A 1 359 ? 7.760 53.033 71.815 1.00 25.52 ? 413 ARG A N 1 ATOM 2886 C CA . ARG A 1 359 ? 6.962 54.275 71.951 1.00 24.85 ? 413 ARG A CA 1 ATOM 2887 C C . ARG A 1 359 ? 5.980 54.425 70.741 1.00 24.55 ? 413 ARG A C 1 ATOM 2888 O O . ARG A 1 359 ? 4.770 54.665 70.918 1.00 23.26 ? 413 ARG A O 1 ATOM 2889 C CB . ARG A 1 359 ? 7.858 55.503 72.069 1.00 24.25 ? 413 ARG A CB 1 ATOM 2890 C CG . ARG A 1 359 ? 7.108 56.894 72.087 1.00 26.07 ? 413 ARG A CG 1 ATOM 2891 C CD . ARG A 1 359 ? 8.103 58.082 71.980 1.00 25.07 ? 413 ARG A CD 1 ATOM 2892 N NE . ARG A 1 359 ? 7.346 59.327 71.913 1.00 27.52 ? 413 ARG A NE 1 ATOM 2893 C CZ . ARG A 1 359 ? 6.827 59.954 72.982 1.00 32.56 ? 413 ARG A CZ 1 ATOM 2894 N NH1 . ARG A 1 359 ? 7.048 59.495 74.219 1.00 32.48 ? 413 ARG A NH1 1 ATOM 2895 N NH2 . ARG A 1 359 ? 6.120 61.057 72.831 1.00 30.74 ? 413 ARG A NH2 1 ATOM 2896 N N . ARG A 1 360 ? 6.535 54.248 69.550 1.00 23.28 ? 414 ARG A N 1 ATOM 2897 C CA . ARG A 1 360 ? 5.805 54.380 68.255 1.00 23.07 ? 414 ARG A CA 1 ATOM 2898 C C . ARG A 1 360 ? 5.572 52.989 67.671 1.00 22.43 ? 414 ARG A C 1 ATOM 2899 O O . ARG A 1 360 ? 6.273 52.017 68.013 1.00 23.40 ? 414 ARG A O 1 ATOM 2900 C CB . ARG A 1 360 ? 6.679 55.184 67.241 1.00 20.82 ? 414 ARG A CB 1 ATOM 2901 C CG . ARG A 1 360 ? 7.084 56.583 67.739 1.00 21.47 ? 414 ARG A CG 1 ATOM 2902 C CD . ARG A 1 360 ? 7.813 57.504 66.711 1.00 22.80 ? 414 ARG A CD 1 ATOM 2903 N NE . ARG A 1 360 ? 8.080 58.766 67.403 1.00 21.43 ? 414 ARG A NE 1 ATOM 2904 C CZ . ARG A 1 360 ? 9.096 58.993 68.241 1.00 23.21 ? 414 ARG A CZ 1 ATOM 2905 N NH1 . ARG A 1 360 ? 10.055 58.093 68.408 1.00 20.95 ? 414 ARG A NH1 1 ATOM 2906 N NH2 . ARG A 1 360 ? 9.141 60.163 68.914 1.00 24.36 ? 414 ARG A NH2 1 ATOM 2907 N N . THR A 1 361 ? 4.583 52.878 66.792 1.00 21.27 ? 415 THR A N 1 ATOM 2908 C CA . THR A 1 361 ? 4.305 51.628 66.117 1.00 21.32 ? 415 THR A CA 1 ATOM 2909 C C . THR A 1 361 ? 5.448 51.264 65.183 1.00 21.55 ? 415 THR A C 1 ATOM 2910 O O . THR A 1 361 ? 5.974 52.153 64.453 1.00 21.39 ? 415 THR A O 1 ATOM 2911 C CB . THR A 1 361 ? 2.972 51.718 65.361 1.00 20.66 ? 415 THR A CB 1 ATOM 2912 O OG1 . THR A 1 361 ? 1.904 51.771 66.332 1.00 22.09 ? 415 THR A OG1 1 ATOM 2913 C CG2 . THR A 1 361 ? 2.770 50.557 64.395 1.00 18.15 ? 415 THR A CG2 1 ATOM 2914 N N . ILE A 1 362 ? 5.813 49.978 65.194 1.00 20.50 ? 416 ILE A N 1 ATOM 2915 C CA . ILE A 1 362 ? 6.750 49.434 64.210 1.00 21.28 ? 416 ILE A CA 1 ATOM 2916 C C . ILE A 1 362 ? 5.989 48.529 63.280 1.00 20.93 ? 416 ILE A C 1 ATOM 2917 O O . ILE A 1 362 ? 5.253 47.662 63.717 1.00 22.02 ? 416 ILE A O 1 ATOM 2918 C CB . ILE A 1 362 ? 7.923 48.643 64.864 1.00 21.52 ? 416 ILE A CB 1 ATOM 2919 C CG1 . ILE A 1 362 ? 8.664 49.563 65.846 1.00 22.21 ? 416 ILE A CG1 1 ATOM 2920 C CG2 . ILE A 1 362 ? 8.892 48.127 63.766 1.00 21.54 ? 416 ILE A CG2 1 ATOM 2921 C CD1 . ILE A 1 362 ? 9.797 48.782 66.664 1.00 22.55 ? 416 ILE A CD1 1 ATOM 2922 N N . LEU A 1 363 ? 6.133 48.794 61.984 1.00 19.87 ? 417 LEU A N 1 ATOM 2923 C CA . LEU A 1 363 ? 5.594 47.928 60.920 1.00 19.29 ? 417 LEU A CA 1 ATOM 2924 C C . LEU A 1 363 ? 6.747 47.153 60.308 1.00 20.03 ? 417 LEU A C 1 ATOM 2925 O O . LEU A 1 363 ? 7.820 47.711 59.934 1.00 20.41 ? 417 LEU A O 1 ATOM 2926 C CB . LEU A 1 363 ? 4.925 48.765 59.817 1.00 18.18 ? 417 LEU A CB 1 ATOM 2927 C CG . LEU A 1 363 ? 3.768 49.668 60.320 1.00 20.03 ? 417 LEU A CG 1 ATOM 2928 C CD1 . LEU A 1 363 ? 3.095 50.382 59.126 1.00 22.88 ? 417 LEU A CD1 1 ATOM 2929 C CD2 . LEU A 1 363 ? 2.719 48.796 61.078 1.00 20.73 ? 417 LEU A CD2 1 ATOM 2930 N N . PHE A 1 364 ? 6.546 45.847 60.202 1.00 19.28 ? 418 PHE A N 1 ATOM 2931 C CA . PHE A 1 364 ? 7.540 44.976 59.556 1.00 20.16 ? 418 PHE A CA 1 ATOM 2932 C C . PHE A 1 364 ? 6.946 44.463 58.258 1.00 20.04 ? 418 PHE A C 1 ATOM 2933 O O . PHE A 1 364 ? 5.798 44.000 58.235 1.00 22.78 ? 418 PHE A O 1 ATOM 2934 C CB . PHE A 1 364 ? 7.897 43.761 60.447 1.00 18.88 ? 418 PHE A CB 1 ATOM 2935 C CG . PHE A 1 364 ? 8.458 44.169 61.777 1.00 21.24 ? 418 PHE A CG 1 ATOM 2936 C CD1 . PHE A 1 364 ? 9.818 44.422 61.902 1.00 20.96 ? 418 PHE A CD1 1 ATOM 2937 C CD2 . PHE A 1 364 ? 7.628 44.340 62.880 1.00 22.66 ? 418 PHE A CD2 1 ATOM 2938 C CE1 . PHE A 1 364 ? 10.367 44.812 63.155 1.00 23.54 ? 418 PHE A CE1 1 ATOM 2939 C CE2 . PHE A 1 364 ? 8.163 44.716 64.110 1.00 25.08 ? 418 PHE A CE2 1 ATOM 2940 C CZ . PHE A 1 364 ? 9.565 44.923 64.233 1.00 22.79 ? 418 PHE A CZ 1 ATOM 2941 N N . ALA A 1 365 ? 7.747 44.502 57.194 1.00 20.08 ? 419 ALA A N 1 ATOM 2942 C CA . ALA A 1 365 ? 7.272 44.068 55.857 1.00 19.30 ? 419 ALA A CA 1 ATOM 2943 C C . ALA A 1 365 ? 8.184 43.088 55.141 1.00 18.64 ? 419 ALA A C 1 ATOM 2944 O O . ALA A 1 365 ? 9.398 43.276 55.057 1.00 19.65 ? 419 ALA A O 1 ATOM 2945 C CB . ALA A 1 365 ? 7.029 45.288 54.930 1.00 18.94 ? 419 ALA A CB 1 ATOM 2946 N N . SER A 1 366 ? 7.557 42.056 54.603 1.00 18.02 ? 420 SER A N 1 ATOM 2947 C CA . SER A 1 366 ? 8.200 41.108 53.699 1.00 18.12 ? 420 SER A CA 1 ATOM 2948 C C . SER A 1 366 ? 7.554 41.328 52.317 1.00 18.24 ? 420 SER A C 1 ATOM 2949 O O . SER A 1 366 ? 6.414 40.897 52.075 1.00 19.31 ? 420 SER A O 1 ATOM 2950 C CB . SER A 1 366 ? 7.871 39.695 54.219 1.00 18.79 ? 420 SER A CB 1 ATOM 2951 O OG . SER A 1 366 ? 8.342 38.663 53.314 1.00 19.27 ? 420 SER A OG 1 ATOM 2952 N N . TRP A 1 367 ? 8.222 42.101 51.464 1.00 19.12 ? 421 TRP A N 1 ATOM 2953 C CA . TRP A 1 367 ? 7.652 42.524 50.182 1.00 16.51 ? 421 TRP A CA 1 ATOM 2954 C C . TRP A 1 367 ? 7.760 41.442 49.112 1.00 18.38 ? 421 TRP A C 1 ATOM 2955 O O . TRP A 1 367 ? 8.723 40.665 49.101 1.00 18.67 ? 421 TRP A O 1 ATOM 2956 C CB . TRP A 1 367 ? 8.407 43.734 49.637 1.00 16.13 ? 421 TRP A CB 1 ATOM 2957 C CG . TRP A 1 367 ? 8.435 44.943 50.543 1.00 15.28 ? 421 TRP A CG 1 ATOM 2958 C CD1 . TRP A 1 367 ? 9.561 45.623 50.916 1.00 15.13 ? 421 TRP A CD1 1 ATOM 2959 C CD2 . TRP A 1 367 ? 7.310 45.653 51.135 1.00 16.75 ? 421 TRP A CD2 1 ATOM 2960 N NE1 . TRP A 1 367 ? 9.220 46.720 51.692 1.00 16.69 ? 421 TRP A NE1 1 ATOM 2961 C CE2 . TRP A 1 367 ? 7.840 46.739 51.842 1.00 16.37 ? 421 TRP A CE2 1 ATOM 2962 C CE3 . TRP A 1 367 ? 5.911 45.476 51.105 1.00 20.02 ? 421 TRP A CE3 1 ATOM 2963 C CZ2 . TRP A 1 367 ? 7.031 47.672 52.534 1.00 17.70 ? 421 TRP A CZ2 1 ATOM 2964 C CZ3 . TRP A 1 367 ? 5.086 46.391 51.803 1.00 17.86 ? 421 TRP A CZ3 1 ATOM 2965 C CH2 . TRP A 1 367 ? 5.652 47.465 52.524 1.00 18.08 ? 421 TRP A CH2 1 ATOM 2966 N N . ASP A 1 368 ? 6.733 41.371 48.257 1.00 17.34 ? 422 ASP A N 1 ATOM 2967 C CA . ASP A 1 368 ? 6.772 40.418 47.150 1.00 18.02 ? 422 ASP A CA 1 ATOM 2968 C C . ASP A 1 368 ? 7.096 41.198 45.865 1.00 17.74 ? 422 ASP A C 1 ATOM 2969 O O . ASP A 1 368 ? 6.971 42.455 45.823 1.00 19.67 ? 422 ASP A O 1 ATOM 2970 C CB . ASP A 1 368 ? 5.404 39.707 47.033 1.00 16.70 ? 422 ASP A CB 1 ATOM 2971 C CG . ASP A 1 368 ? 5.491 38.356 46.314 1.00 20.09 ? 422 ASP A CG 1 ATOM 2972 O OD1 . ASP A 1 368 ? 6.537 38.046 45.687 1.00 19.72 ? 422 ASP A OD1 1 ATOM 2973 O OD2 . ASP A 1 368 ? 4.474 37.635 46.370 1.00 20.51 ? 422 ASP A OD2 1 ATOM 2974 N N . ALA A 1 369 ? 7.492 40.442 44.830 1.00 17.64 ? 423 ALA A N 1 ATOM 2975 C CA . ALA A 1 369 ? 7.708 40.951 43.443 1.00 18.40 ? 423 ALA A CA 1 ATOM 2976 C C . ALA A 1 369 ? 8.623 42.163 43.355 1.00 17.36 ? 423 ALA A C 1 ATOM 2977 O O . ALA A 1 369 ? 8.483 42.989 42.457 1.00 18.44 ? 423 ALA A O 1 ATOM 2978 C CB . ALA A 1 369 ? 6.348 41.232 42.744 1.00 17.66 ? 423 ALA A CB 1 ATOM 2979 N N . GLU A 1 370 ? 9.568 42.265 44.286 1.00 18.10 ? 424 GLU A N 1 ATOM 2980 C CA . GLU A 1 370 ? 10.556 43.337 44.212 1.00 18.55 ? 424 GLU A CA 1 ATOM 2981 C C . GLU A 1 370 ? 11.362 43.177 42.922 1.00 19.13 ? 424 GLU A C 1 ATOM 2982 O O . GLU A 1 370 ? 11.730 44.175 42.237 1.00 18.39 ? 424 GLU A O 1 ATOM 2983 C CB . GLU A 1 370 ? 11.436 43.341 45.454 1.00 19.81 ? 424 GLU A CB 1 ATOM 2984 C CG . GLU A 1 370 ? 12.428 44.565 45.454 1.00 17.47 ? 424 GLU A CG 1 ATOM 2985 C CD . GLU A 1 370 ? 13.784 44.281 44.809 1.00 21.94 ? 424 GLU A CD 1 ATOM 2986 O OE1 . GLU A 1 370 ? 14.045 43.150 44.231 1.00 19.46 ? 424 GLU A OE1 1 ATOM 2987 O OE2 . GLU A 1 370 ? 14.607 45.227 44.828 1.00 21.25 ? 424 GLU A OE2 1 ATOM 2988 N N . GLU A 1 371 ? 11.653 41.927 42.560 1.00 18.93 ? 425 GLU A N 1 ATOM 2989 C CA . GLU A 1 371 ? 12.540 41.701 41.387 1.00 18.35 ? 425 GLU A CA 1 ATOM 2990 C C . GLU A 1 371 ? 11.841 42.038 40.079 1.00 19.13 ? 425 GLU A C 1 ATOM 2991 O O . GLU A 1 371 ? 12.481 42.147 39.052 1.00 19.95 ? 425 GLU A O 1 ATOM 2992 C CB . GLU A 1 371 ? 13.016 40.233 41.330 1.00 17.85 ? 425 GLU A CB 1 ATOM 2993 C CG . GLU A 1 371 ? 13.944 39.761 42.495 1.00 17.04 ? 425 GLU A CG 1 ATOM 2994 C CD . GLU A 1 371 ? 15.311 40.528 42.533 1.00 17.12 ? 425 GLU A CD 1 ATOM 2995 O OE1 . GLU A 1 371 ? 15.522 41.484 41.762 1.00 20.11 ? 425 GLU A OE1 1 ATOM 2996 O OE2 . GLU A 1 371 ? 16.189 40.177 43.358 1.00 19.62 ? 425 GLU A OE2 1 ATOM 2997 N N . PHE A 1 372 ? 10.506 42.223 40.105 1.00 18.68 ? 426 PHE A N 1 ATOM 2998 C CA . PHE A 1 372 ? 9.789 42.588 38.896 1.00 18.95 ? 426 PHE A CA 1 ATOM 2999 C C . PHE A 1 372 ? 9.379 44.063 38.826 1.00 19.67 ? 426 PHE A C 1 ATOM 3000 O O . PHE A 1 372 ? 8.418 44.408 38.136 1.00 19.41 ? 426 PHE A O 1 ATOM 3001 C CB . PHE A 1 372 ? 8.523 41.714 38.851 1.00 19.19 ? 426 PHE A CB 1 ATOM 3002 C CG . PHE A 1 372 ? 8.840 40.261 38.534 1.00 19.10 ? 426 PHE A CG 1 ATOM 3003 C CD1 . PHE A 1 372 ? 8.680 39.774 37.234 1.00 18.92 ? 426 PHE A CD1 1 ATOM 3004 C CD2 . PHE A 1 372 ? 9.250 39.380 39.557 1.00 19.64 ? 426 PHE A CD2 1 ATOM 3005 C CE1 . PHE A 1 372 ? 8.926 38.404 36.895 1.00 20.00 ? 426 PHE A CE1 1 ATOM 3006 C CE2 . PHE A 1 372 ? 9.528 38.015 39.256 1.00 19.82 ? 426 PHE A CE2 1 ATOM 3007 C CZ . PHE A 1 372 ? 9.361 37.513 37.886 1.00 19.84 ? 426 PHE A CZ 1 ATOM 3008 N N . GLY A 1 373 ? 10.081 44.923 39.572 1.00 19.99 ? 427 GLY A N 1 ATOM 3009 C CA . GLY A 1 373 ? 9.846 46.352 39.480 1.00 18.94 ? 427 GLY A CA 1 ATOM 3010 C C . GLY A 1 373 ? 9.346 46.992 40.780 1.00 18.92 ? 427 GLY A C 1 ATOM 3011 O O . GLY A 1 373 ? 8.616 48.007 40.721 1.00 19.09 ? 427 GLY A O 1 ATOM 3012 N N . LEU A 1 374 ? 9.703 46.422 41.936 1.00 16.62 ? 428 LEU A N 1 ATOM 3013 C CA . LEU A 1 374 ? 9.324 47.001 43.267 1.00 17.01 ? 428 LEU A CA 1 ATOM 3014 C C . LEU A 1 374 ? 7.802 46.924 43.396 1.00 17.07 ? 428 LEU A C 1 ATOM 3015 O O . LEU A 1 374 ? 7.180 47.778 43.968 1.00 17.18 ? 428 LEU A O 1 ATOM 3016 C CB . LEU A 1 374 ? 9.794 48.484 43.398 1.00 17.50 ? 428 LEU A CB 1 ATOM 3017 C CG . LEU A 1 374 ? 11.244 48.717 42.888 1.00 17.32 ? 428 LEU A CG 1 ATOM 3018 C CD1 . LEU A 1 374 ? 11.647 50.189 43.061 1.00 20.61 ? 428 LEU A CD1 1 ATOM 3019 C CD2 . LEU A 1 374 ? 12.273 47.807 43.621 1.00 17.61 ? 428 LEU A CD2 1 ATOM 3020 N N . LEU A 1 375 ? 7.206 45.842 42.882 1.00 16.97 ? 429 LEU A N 1 ATOM 3021 C CA . LEU A 1 375 ? 5.718 45.888 42.767 1.00 17.04 ? 429 LEU A CA 1 ATOM 3022 C C . LEU A 1 375 ? 4.992 45.783 44.085 1.00 18.07 ? 429 LEU A C 1 ATOM 3023 O O . LEU A 1 375 ? 4.002 46.449 44.266 1.00 18.07 ? 429 LEU A O 1 ATOM 3024 C CB . LEU A 1 375 ? 5.184 44.799 41.798 1.00 16.05 ? 429 LEU A CB 1 ATOM 3025 C CG . LEU A 1 375 ? 5.920 44.831 40.431 1.00 17.29 ? 429 LEU A CG 1 ATOM 3026 C CD1 . LEU A 1 375 ? 5.272 43.677 39.522 1.00 18.31 ? 429 LEU A CD1 1 ATOM 3027 C CD2 . LEU A 1 375 ? 5.817 46.165 39.627 1.00 17.09 ? 429 LEU A CD2 1 ATOM 3028 N N . GLY A 1 376 ? 5.419 44.871 44.957 1.00 16.19 ? 430 GLY A N 1 ATOM 3029 C CA . GLY A 1 376 ? 4.723 44.650 46.243 1.00 17.19 ? 430 GLY A CA 1 ATOM 3030 C C . GLY A 1 376 ? 4.781 45.869 47.133 1.00 17.26 ? 430 GLY A C 1 ATOM 3031 O O . GLY A 1 376 ? 3.770 46.268 47.695 1.00 17.06 ? 430 GLY A O 1 ATOM 3032 N N . SER A 1 377 ? 5.964 46.477 47.275 1.00 16.35 ? 431 SER A N 1 ATOM 3033 C CA . SER A 1 377 ? 6.028 47.648 48.184 1.00 17.13 ? 431 SER A CA 1 ATOM 3034 C C . SER A 1 377 ? 5.240 48.793 47.556 1.00 16.21 ? 431 SER A C 1 ATOM 3035 O O . SER A 1 377 ? 4.545 49.553 48.254 1.00 15.30 ? 431 SER A O 1 ATOM 3036 C CB . SER A 1 377 ? 7.498 48.097 48.396 1.00 16.49 ? 431 SER A CB 1 ATOM 3037 O OG . SER A 1 377 ? 8.173 48.403 47.127 1.00 17.99 ? 431 SER A OG 1 ATOM 3038 N N . THR A 1 378 ? 5.335 48.933 46.231 1.00 15.48 ? 432 THR A N 1 ATOM 3039 C CA . THR A 1 378 ? 4.660 50.094 45.626 1.00 16.46 ? 432 THR A CA 1 ATOM 3040 C C . THR A 1 378 ? 3.118 49.966 45.721 1.00 16.01 ? 432 THR A C 1 ATOM 3041 O O . THR A 1 378 ? 2.428 50.971 45.943 1.00 16.93 ? 432 THR A O 1 ATOM 3042 C CB . THR A 1 378 ? 5.126 50.265 44.130 1.00 16.30 ? 432 THR A CB 1 ATOM 3043 O OG1 . THR A 1 378 ? 6.577 50.452 44.141 1.00 17.54 ? 432 THR A OG1 1 ATOM 3044 C CG2 . THR A 1 378 ? 4.489 51.598 43.531 1.00 17.71 ? 432 THR A CG2 1 ATOM 3045 N N . GLU A 1 379 ? 2.594 48.777 45.449 1.00 16.42 ? 433 GLU A N 1 ATOM 3046 C CA . GLU A 1 379 ? 1.107 48.627 45.510 1.00 17.49 ? 433 GLU A CA 1 ATOM 3047 C C . GLU A 1 379 ? 0.625 48.883 46.932 1.00 16.64 ? 433 GLU A C 1 ATOM 3048 O O . GLU A 1 379 ? -0.437 49.479 47.130 1.00 16.88 ? 433 GLU A O 1 ATOM 3049 C CB . GLU A 1 379 ? 0.662 47.220 45.053 1.00 16.73 ? 433 GLU A CB 1 ATOM 3050 C CG . GLU A 1 379 ? 0.894 46.944 43.511 1.00 19.01 ? 433 GLU A CG 1 ATOM 3051 C CD . GLU A 1 379 ? 0.319 48.068 42.613 1.00 19.34 ? 433 GLU A CD 1 ATOM 3052 O OE1 . GLU A 1 379 ? -0.910 48.366 42.716 1.00 19.00 ? 433 GLU A OE1 1 ATOM 3053 O OE2 . GLU A 1 379 ? 1.045 48.694 41.822 1.00 19.05 ? 433 GLU A OE2 1 ATOM 3054 N N . TRP A 1 380 ? 1.359 48.362 47.931 1.00 15.77 ? 434 TRP A N 1 ATOM 3055 C CA . TRP A 1 380 ? 0.975 48.540 49.343 1.00 16.48 ? 434 TRP A CA 1 ATOM 3056 C C . TRP A 1 380 ? 1.054 50.033 49.704 1.00 16.71 ? 434 TRP A C 1 ATOM 3057 O O . TRP A 1 380 ? 0.156 50.555 50.369 1.00 16.95 ? 434 TRP A O 1 ATOM 3058 C CB . TRP A 1 380 ? 1.866 47.684 50.266 1.00 17.13 ? 434 TRP A CB 1 ATOM 3059 C CG . TRP A 1 380 ? 1.462 47.719 51.726 1.00 17.54 ? 434 TRP A CG 1 ATOM 3060 C CD1 . TRP A 1 380 ? 0.472 46.953 52.337 1.00 18.39 ? 434 TRP A CD1 1 ATOM 3061 C CD2 . TRP A 1 380 ? 1.972 48.589 52.716 1.00 18.33 ? 434 TRP A CD2 1 ATOM 3062 N NE1 . TRP A 1 380 ? 0.401 47.276 53.688 1.00 18.82 ? 434 TRP A NE1 1 ATOM 3063 C CE2 . TRP A 1 380 ? 1.306 48.278 53.943 1.00 19.49 ? 434 TRP A CE2 1 ATOM 3064 C CE3 . TRP A 1 380 ? 2.942 49.605 52.696 1.00 17.89 ? 434 TRP A CE3 1 ATOM 3065 C CZ2 . TRP A 1 380 ? 1.587 48.946 55.162 1.00 20.02 ? 434 TRP A CZ2 1 ATOM 3066 C CZ3 . TRP A 1 380 ? 3.249 50.262 53.942 1.00 19.37 ? 434 TRP A CZ3 1 ATOM 3067 C CH2 . TRP A 1 380 ? 2.563 49.918 55.142 1.00 19.94 ? 434 TRP A CH2 1 ATOM 3068 N N . ALA A 1 381 ? 2.102 50.727 49.241 1.00 16.18 ? 435 ALA A N 1 ATOM 3069 C CA . ALA A 1 381 ? 2.200 52.153 49.526 1.00 17.40 ? 435 ALA A CA 1 ATOM 3070 C C . ALA A 1 381 ? 1.071 52.922 48.800 1.00 17.87 ? 435 ALA A C 1 ATOM 3071 O O . ALA A 1 381 ? 0.549 53.894 49.363 1.00 16.59 ? 435 ALA A O 1 ATOM 3072 C CB . ALA A 1 381 ? 3.575 52.731 49.112 1.00 18.44 ? 435 ALA A CB 1 ATOM 3073 N N . GLU A 1 382 ? 0.723 52.526 47.555 1.00 17.45 ? 436 GLU A N 1 ATOM 3074 C CA . GLU A 1 382 ? -0.446 53.185 46.872 1.00 17.65 ? 436 GLU A CA 1 ATOM 3075 C C . GLU A 1 382 ? -1.758 52.949 47.626 1.00 18.39 ? 436 GLU A C 1 ATOM 3076 O O . GLU A 1 382 ? -2.604 53.869 47.762 1.00 18.77 ? 436 GLU A O 1 ATOM 3077 C CB . GLU A 1 382 ? -0.603 52.693 45.425 1.00 18.80 ? 436 GLU A CB 1 ATOM 3078 C CG . GLU A 1 382 ? 0.590 53.192 44.527 1.00 17.62 ? 436 GLU A CG 1 ATOM 3079 C CD . GLU A 1 382 ? 0.480 52.766 43.072 1.00 19.18 ? 436 GLU A CD 1 ATOM 3080 O OE1 . GLU A 1 382 ? 0.893 53.565 42.198 1.00 19.51 ? 436 GLU A OE1 1 ATOM 3081 O OE2 . GLU A 1 382 ? -0.046 51.653 42.809 1.00 19.10 ? 436 GLU A OE2 1 ATOM 3082 N N . GLU A 1 383 ? -1.924 51.736 48.152 1.00 17.73 ? 437 GLU A N 1 ATOM 3083 C CA . GLU A 1 383 ? -3.113 51.433 48.929 1.00 18.10 ? 437 GLU A CA 1 ATOM 3084 C C . GLU A 1 383 ? -3.181 52.277 50.224 1.00 17.74 ? 437 GLU A C 1 ATOM 3085 O O . GLU A 1 383 ? -4.251 52.821 50.582 1.00 16.77 ? 437 GLU A O 1 ATOM 3086 C CB . GLU A 1 383 ? -3.063 49.974 49.314 1.00 18.09 ? 437 GLU A CB 1 ATOM 3087 C CG . GLU A 1 383 ? -4.400 49.488 50.032 1.00 22.79 ? 437 GLU A CG 1 ATOM 3088 C CD . GLU A 1 383 ? -4.498 47.960 49.808 1.00 32.04 ? 437 GLU A CD 1 ATOM 3089 O OE1 . GLU A 1 383 ? -5.268 47.501 48.967 1.00 42.58 ? 437 GLU A OE1 1 ATOM 3090 O OE2 . GLU A 1 383 ? -3.706 47.258 50.378 1.00 34.09 ? 437 GLU A OE2 1 ATOM 3091 N N . ASN A 1 384 ? -2.028 52.425 50.875 1.00 16.78 ? 438 ASN A N 1 ATOM 3092 C CA . ASN A 1 384 ? -1.989 53.035 52.244 1.00 17.07 ? 438 ASN A CA 1 ATOM 3093 C C . ASN A 1 384 ? -1.401 54.435 52.259 1.00 16.89 ? 438 ASN A C 1 ATOM 3094 O O . ASN A 1 384 ? -1.060 54.960 53.321 1.00 16.32 ? 438 ASN A O 1 ATOM 3095 C CB . ASN A 1 384 ? -1.215 52.073 53.169 1.00 17.47 ? 438 ASN A CB 1 ATOM 3096 C CG . ASN A 1 384 ? -1.988 50.788 53.368 1.00 20.02 ? 438 ASN A CG 1 ATOM 3097 O OD1 . ASN A 1 384 ? -3.059 50.800 54.000 1.00 21.29 ? 438 ASN A OD1 1 ATOM 3098 N ND2 . ASN A 1 384 ? -1.533 49.708 52.757 1.00 20.02 ? 438 ASN A ND2 1 ATOM 3099 N N . SER A 1 385 ? -1.407 55.108 51.093 1.00 16.10 ? 439 SER A N 1 ATOM 3100 C CA . SER A 1 385 ? -0.641 56.349 50.956 1.00 16.93 ? 439 SER A CA 1 ATOM 3101 C C . SER A 1 385 ? -1.111 57.425 51.927 1.00 17.03 ? 439 SER A C 1 ATOM 3102 O O . SER A 1 385 ? -0.284 58.201 52.423 1.00 17.05 ? 439 SER A O 1 ATOM 3103 C CB . SER A 1 385 ? -0.764 56.933 49.510 1.00 17.84 ? 439 SER A CB 1 ATOM 3104 O OG . SER A 1 385 ? -2.124 57.172 49.207 1.00 19.60 ? 439 SER A OG 1 ATOM 3105 N N . ARG A 1 386 ? -2.428 57.521 52.192 1.00 16.04 ? 440 ARG A N 1 ATOM 3106 C CA . ARG A 1 386 ? -2.859 58.557 53.149 1.00 17.38 ? 440 ARG A CA 1 ATOM 3107 C C . ARG A 1 386 ? -2.362 58.291 54.585 1.00 18.37 ? 440 ARG A C 1 ATOM 3108 O O . ARG A 1 386 ? -2.011 59.243 55.301 1.00 16.59 ? 440 ARG A O 1 ATOM 3109 C CB . ARG A 1 386 ? -4.396 58.615 53.156 1.00 17.97 ? 440 ARG A CB 1 ATOM 3110 C CG . ARG A 1 386 ? -4.909 59.122 51.770 1.00 20.40 ? 440 ARG A CG 1 ATOM 3111 C CD . ARG A 1 386 ? -6.329 58.540 51.416 1.00 22.60 ? 440 ARG A CD 1 ATOM 3112 N NE . ARG A 1 386 ? -6.691 59.053 50.073 1.00 20.86 ? 440 ARG A NE 1 ATOM 3113 C CZ . ARG A 1 386 ? -6.257 58.609 48.894 1.00 23.02 ? 440 ARG A CZ 1 ATOM 3114 N NH1 . ARG A 1 386 ? -5.460 57.530 48.767 1.00 23.91 ? 440 ARG A NH1 1 ATOM 3115 N NH2 . ARG A 1 386 ? -6.648 59.266 47.791 1.00 18.66 ? 440 ARG A NH2 1 ATOM 3116 N N . LEU A 1 387 ? -2.424 57.038 55.032 1.00 18.04 ? 441 LEU A N 1 ATOM 3117 C CA . LEU A 1 387 ? -1.886 56.698 56.345 1.00 18.24 ? 441 LEU A CA 1 ATOM 3118 C C . LEU A 1 387 ? -0.368 57.023 56.396 1.00 19.36 ? 441 LEU A C 1 ATOM 3119 O O . LEU A 1 387 ? 0.120 57.585 57.356 1.00 18.62 ? 441 LEU A O 1 ATOM 3120 C CB . LEU A 1 387 ? -2.081 55.217 56.632 1.00 18.36 ? 441 LEU A CB 1 ATOM 3121 C CG . LEU A 1 387 ? -3.507 54.672 56.471 1.00 19.62 ? 441 LEU A CG 1 ATOM 3122 C CD1 . LEU A 1 387 ? -3.554 53.200 56.930 1.00 22.00 ? 441 LEU A CD1 1 ATOM 3123 C CD2 . LEU A 1 387 ? -4.560 55.535 57.148 1.00 23.90 ? 441 LEU A CD2 1 ATOM 3124 N N . LEU A 1 388 ? 0.340 56.661 55.336 1.00 18.22 ? 442 LEU A N 1 ATOM 3125 C CA . LEU A 1 388 ? 1.813 56.787 55.308 1.00 17.34 ? 442 LEU A CA 1 ATOM 3126 C C . LEU A 1 388 ? 2.209 58.220 55.261 1.00 19.01 ? 442 LEU A C 1 ATOM 3127 O O . LEU A 1 388 ? 3.182 58.631 55.930 1.00 21.80 ? 442 LEU A O 1 ATOM 3128 C CB . LEU A 1 388 ? 2.374 56.021 54.064 1.00 17.27 ? 442 LEU A CB 1 ATOM 3129 C CG . LEU A 1 388 ? 2.218 54.514 54.122 1.00 19.37 ? 442 LEU A CG 1 ATOM 3130 C CD1 . LEU A 1 388 ? 2.589 53.879 52.705 1.00 17.56 ? 442 LEU A CD1 1 ATOM 3131 C CD2 . LEU A 1 388 ? 3.127 53.830 55.243 1.00 21.20 ? 442 LEU A CD2 1 ATOM 3132 N N A GLN A 1 389 ? 1.528 59.049 54.490 0.50 17.58 ? 443 GLN A N 1 ATOM 3133 N N B GLN A 1 389 ? 1.494 58.997 54.423 0.50 18.06 ? 443 GLN A N 1 ATOM 3134 C CA A GLN A 1 389 ? 2.045 60.407 54.466 0.50 18.28 ? 443 GLN A CA 1 ATOM 3135 C CA B GLN A 1 389 ? 1.659 60.464 54.310 0.50 19.19 ? 443 GLN A CA 1 ATOM 3136 C C A GLN A 1 389 ? 1.658 61.276 55.694 0.50 18.01 ? 443 GLN A C 1 ATOM 3137 C C B GLN A 1 389 ? 1.669 61.157 55.691 0.50 18.47 ? 443 GLN A C 1 ATOM 3138 O O A GLN A 1 389 ? 2.314 62.293 55.931 0.50 17.45 ? 443 GLN A O 1 ATOM 3139 O O B GLN A 1 389 ? 2.592 61.893 56.043 0.50 17.05 ? 443 GLN A O 1 ATOM 3140 C CB A GLN A 1 389 ? 1.687 61.088 53.165 0.50 16.35 ? 443 GLN A CB 1 ATOM 3141 C CB B GLN A 1 389 ? 0.501 61.053 53.464 0.50 18.90 ? 443 GLN A CB 1 ATOM 3142 C CG A GLN A 1 389 ? 0.192 61.408 53.037 0.50 16.75 ? 443 GLN A CG 1 ATOM 3143 C CG B GLN A 1 389 ? 0.265 62.500 53.659 0.50 18.68 ? 443 GLN A CG 1 ATOM 3144 C CD A GLN A 1 389 ? -0.178 61.672 51.589 0.50 20.88 ? 443 GLN A CD 1 ATOM 3145 C CD B GLN A 1 389 ? 1.187 63.333 52.831 0.50 24.21 ? 443 GLN A CD 1 ATOM 3146 O OE1 A GLN A 1 389 ? 0.654 61.521 50.689 0.50 19.15 ? 443 GLN A OE1 1 ATOM 3147 O OE1 B GLN A 1 389 ? 1.627 62.865 51.762 0.50 25.50 ? 443 GLN A OE1 1 ATOM 3148 N NE2 A GLN A 1 389 ? -1.444 62.021 51.351 0.50 17.54 ? 443 GLN A NE2 1 ATOM 3149 N NE2 B GLN A 1 389 ? 1.486 64.583 53.291 0.50 16.16 ? 443 GLN A NE2 1 ATOM 3150 N N . GLU A 1 390 ? 0.619 60.906 56.467 1.00 18.25 ? 444 GLU A N 1 ATOM 3151 C CA . GLU A 1 390 ? 0.355 61.661 57.671 1.00 18.24 ? 444 GLU A CA 1 ATOM 3152 C C . GLU A 1 390 ? 0.982 61.008 58.922 1.00 18.72 ? 444 GLU A C 1 ATOM 3153 O O . GLU A 1 390 ? 1.140 61.681 59.920 1.00 19.03 ? 444 GLU A O 1 ATOM 3154 C CB . GLU A 1 390 ? -1.172 61.848 57.900 1.00 20.64 ? 444 GLU A CB 1 ATOM 3155 C CG . GLU A 1 390 ? -1.888 62.347 56.565 1.00 20.18 ? 444 GLU A CG 1 ATOM 3156 C CD . GLU A 1 390 ? -1.314 63.690 56.029 1.00 25.58 ? 444 GLU A CD 1 ATOM 3157 O OE1 . GLU A 1 390 ? -0.320 64.242 56.588 1.00 20.74 ? 444 GLU A OE1 1 ATOM 3158 O OE2 . GLU A 1 390 ? -1.901 64.191 55.038 1.00 26.06 ? 444 GLU A OE2 1 ATOM 3159 N N . ARG A 1 391 ? 1.389 59.742 58.818 1.00 17.80 ? 445 ARG A N 1 ATOM 3160 C CA . ARG A 1 391 ? 1.851 59.019 60.007 1.00 17.94 ? 445 ARG A CA 1 ATOM 3161 C C . ARG A 1 391 ? 3.285 58.432 59.881 1.00 19.42 ? 445 ARG A C 1 ATOM 3162 O O . ARG A 1 391 ? 3.822 57.967 60.904 1.00 20.30 ? 445 ARG A O 1 ATOM 3163 C CB . ARG A 1 391 ? 0.874 57.871 60.332 1.00 17.25 ? 445 ARG A CB 1 ATOM 3164 C CG . ARG A 1 391 ? -0.603 58.412 60.643 1.00 18.16 ? 445 ARG A CG 1 ATOM 3165 C CD . ARG A 1 391 ? -1.569 57.244 60.895 1.00 18.71 ? 445 ARG A CD 1 ATOM 3166 N NE . ARG A 1 391 ? -2.958 57.709 60.838 1.00 19.61 ? 445 ARG A NE 1 ATOM 3167 C CZ . ARG A 1 391 ? -3.999 56.896 60.782 1.00 16.35 ? 445 ARG A CZ 1 ATOM 3168 N NH1 . ARG A 1 391 ? -3.804 55.580 60.830 1.00 17.94 ? 445 ARG A NH1 1 ATOM 3169 N NH2 . ARG A 1 391 ? -5.245 57.410 60.697 1.00 20.28 ? 445 ARG A NH2 1 ATOM 3170 N N . GLY A 1 392 ? 3.846 58.439 58.670 1.00 18.24 ? 446 GLY A N 1 ATOM 3171 C CA . GLY A 1 392 ? 5.085 57.662 58.370 1.00 19.79 ? 446 GLY A CA 1 ATOM 3172 C C . GLY A 1 392 ? 6.260 58.467 58.893 1.00 19.07 ? 446 GLY A C 1 ATOM 3173 O O . GLY A 1 392 ? 6.594 59.557 58.401 1.00 21.21 ? 446 GLY A O 1 ATOM 3174 N N . VAL A 1 393 ? 6.928 57.932 59.920 1.00 18.97 ? 447 VAL A N 1 ATOM 3175 C CA . VAL A 1 393 ? 8.099 58.588 60.447 1.00 18.66 ? 447 VAL A CA 1 ATOM 3176 C C . VAL A 1 393 ? 9.347 58.282 59.617 1.00 19.06 ? 447 VAL A C 1 ATOM 3177 O O . VAL A 1 393 ? 10.131 59.187 59.230 1.00 18.92 ? 447 VAL A O 1 ATOM 3178 C CB . VAL A 1 393 ? 8.343 58.120 61.954 1.00 19.70 ? 447 VAL A CB 1 ATOM 3179 C CG1 . VAL A 1 393 ? 9.785 58.526 62.406 1.00 18.64 ? 447 VAL A CG1 1 ATOM 3180 C CG2 . VAL A 1 393 ? 7.242 58.756 62.857 1.00 21.18 ? 447 VAL A CG2 1 ATOM 3181 N N . ALA A 1 394 ? 9.519 57.004 59.291 1.00 17.79 ? 448 ALA A N 1 ATOM 3182 C CA . ALA A 1 394 ? 10.745 56.557 58.645 1.00 18.11 ? 448 ALA A CA 1 ATOM 3183 C C . ALA A 1 394 ? 10.589 55.185 58.062 1.00 17.01 ? 448 ALA A C 1 ATOM 3184 O O . ALA A 1 394 ? 9.762 54.369 58.544 1.00 18.34 ? 448 ALA A O 1 ATOM 3185 C CB . ALA A 1 394 ? 11.909 56.544 59.656 1.00 18.49 ? 448 ALA A CB 1 ATOM 3186 N N . TYR A 1 395 ? 11.431 54.905 57.063 1.00 17.01 ? 449 TYR A N 1 ATOM 3187 C CA . TYR A 1 395 ? 11.447 53.612 56.410 1.00 17.22 ? 449 TYR A CA 1 ATOM 3188 C C . TYR A 1 395 ? 12.908 53.163 56.360 1.00 18.24 ? 449 TYR A C 1 ATOM 3189 O O . TYR A 1 395 ? 13.753 53.875 55.864 1.00 18.42 ? 449 TYR A O 1 ATOM 3190 C CB . TYR A 1 395 ? 10.861 53.724 54.975 1.00 15.83 ? 449 TYR A CB 1 ATOM 3191 C CG . TYR A 1 395 ? 10.986 52.407 54.247 1.00 17.26 ? 449 TYR A CG 1 ATOM 3192 C CD1 . TYR A 1 395 ? 9.956 51.462 54.313 1.00 17.26 ? 449 TYR A CD1 1 ATOM 3193 C CD2 . TYR A 1 395 ? 12.123 52.106 53.511 1.00 16.61 ? 449 TYR A CD2 1 ATOM 3194 C CE1 . TYR A 1 395 ? 10.045 50.228 53.659 1.00 18.37 ? 449 TYR A CE1 1 ATOM 3195 C CE2 . TYR A 1 395 ? 12.257 50.808 52.852 1.00 17.07 ? 449 TYR A CE2 1 ATOM 3196 C CZ . TYR A 1 395 ? 11.168 49.924 52.911 1.00 18.86 ? 449 TYR A CZ 1 ATOM 3197 O OH . TYR A 1 395 ? 11.253 48.693 52.272 1.00 18.78 ? 449 TYR A OH 1 ATOM 3198 N N . ILE A 1 396 ? 13.177 51.974 56.893 1.00 18.55 ? 450 ILE A N 1 ATOM 3199 C CA . ILE A 1 396 ? 14.486 51.355 56.802 1.00 17.39 ? 450 ILE A CA 1 ATOM 3200 C C . ILE A 1 396 ? 14.334 50.121 55.913 1.00 19.04 ? 450 ILE A C 1 ATOM 3201 O O . ILE A 1 396 ? 13.511 49.225 56.179 1.00 17.93 ? 450 ILE A O 1 ATOM 3202 C CB . ILE A 1 396 ? 14.997 50.922 58.210 1.00 19.94 ? 450 ILE A CB 1 ATOM 3203 C CG1 . ILE A 1 396 ? 15.014 52.121 59.195 1.00 17.96 ? 450 ILE A CG1 1 ATOM 3204 C CG2 . ILE A 1 396 ? 16.440 50.244 58.120 1.00 17.57 ? 450 ILE A CG2 1 ATOM 3205 C CD1 . ILE A 1 396 ? 15.961 53.293 58.763 1.00 17.98 ? 450 ILE A CD1 1 ATOM 3206 N N . ASN A 1 397 ? 15.124 50.090 54.845 1.00 17.59 ? 451 ASN A N 1 ATOM 3207 C CA . ASN A 1 397 ? 15.106 48.948 53.918 1.00 18.26 ? 451 ASN A CA 1 ATOM 3208 C C . ASN A 1 397 ? 15.903 47.751 54.489 1.00 19.97 ? 451 ASN A C 1 ATOM 3209 O O . ASN A 1 397 ? 16.705 47.873 55.445 1.00 21.42 ? 451 ASN A O 1 ATOM 3210 C CB . ASN A 1 397 ? 15.639 49.383 52.543 1.00 18.26 ? 451 ASN A CB 1 ATOM 3211 C CG . ASN A 1 397 ? 15.085 48.561 51.377 1.00 19.18 ? 451 ASN A CG 1 ATOM 3212 O OD1 . ASN A 1 397 ? 13.876 48.470 51.188 1.00 21.19 ? 451 ASN A OD1 1 ATOM 3213 N ND2 . ASN A 1 397 ? 15.987 47.993 50.552 1.00 20.02 ? 451 ASN A ND2 1 ATOM 3214 N N . ALA A 1 398 ? 15.681 46.584 53.889 1.00 20.89 ? 452 ALA A N 1 ATOM 3215 C CA . ALA A 1 398 ? 16.322 45.356 54.377 1.00 21.67 ? 452 ALA A CA 1 ATOM 3216 C C . ALA A 1 398 ? 16.415 44.309 53.289 1.00 20.84 ? 452 ALA A C 1 ATOM 3217 O O . ALA A 1 398 ? 15.940 43.165 53.462 1.00 22.33 ? 452 ALA A O 1 ATOM 3218 C CB . ALA A 1 398 ? 15.534 44.803 55.597 1.00 22.61 ? 452 ALA A CB 1 ATOM 3219 N N . ASP A 1 399 ? 17.068 44.669 52.191 1.00 19.62 ? 453 ASP A N 1 ATOM 3220 C CA . ASP A 1 399 ? 17.371 43.674 51.159 1.00 19.70 ? 453 ASP A CA 1 ATOM 3221 C C . ASP A 1 399 ? 18.738 43.085 51.603 1.00 21.23 ? 453 ASP A C 1 ATOM 3222 O O . ASP A 1 399 ? 19.084 43.219 52.763 1.00 21.82 ? 453 ASP A O 1 ATOM 3223 C CB . ASP A 1 399 ? 17.467 44.378 49.820 1.00 18.80 ? 453 ASP A CB 1 ATOM 3224 C CG . ASP A 1 399 ? 17.307 43.446 48.623 1.00 21.08 ? 453 ASP A CG 1 ATOM 3225 O OD1 . ASP A 1 399 ? 17.464 42.245 48.785 1.00 22.62 ? 453 ASP A OD1 1 ATOM 3226 O OD2 . ASP A 1 399 ? 17.029 43.941 47.499 1.00 18.87 ? 453 ASP A OD2 1 ATOM 3227 N N . SER A 1 400 ? 19.448 42.445 50.684 1.00 21.38 ? 454 SER A N 1 ATOM 3228 C CA . SER A 1 400 ? 20.735 41.740 50.917 1.00 23.13 ? 454 SER A CA 1 ATOM 3229 C C . SER A 1 400 ? 21.579 42.411 52.026 1.00 23.66 ? 454 SER A C 1 ATOM 3230 O O . SER A 1 400 ? 21.926 43.602 51.937 1.00 23.47 ? 454 SER A O 1 ATOM 3231 C CB . SER A 1 400 ? 21.534 41.732 49.631 1.00 22.43 ? 454 SER A CB 1 ATOM 3232 O OG . SER A 1 400 ? 20.790 41.076 48.644 1.00 21.79 ? 454 SER A OG 1 ATOM 3233 N N A SER A 1 401 ? 21.882 41.643 53.077 0.50 23.40 ? 455 SER A N 1 ATOM 3234 N N B SER A 1 401 ? 21.888 41.656 53.077 0.50 23.97 ? 455 SER A N 1 ATOM 3235 C CA A SER A 1 401 ? 22.660 42.182 54.206 0.50 24.28 ? 455 SER A CA 1 ATOM 3236 C CA B SER A 1 401 ? 22.653 42.245 54.180 0.50 25.44 ? 455 SER A CA 1 ATOM 3237 C C A SER A 1 401 ? 24.133 42.245 53.841 0.50 25.52 ? 455 SER A C 1 ATOM 3238 C C B SER A 1 401 ? 24.140 42.243 53.850 0.50 26.11 ? 455 SER A C 1 ATOM 3239 O O A SER A 1 401 ? 24.862 43.058 54.377 0.50 25.81 ? 455 SER A O 1 ATOM 3240 O O B SER A 1 401 ? 24.888 43.016 54.414 0.50 26.38 ? 455 SER A O 1 ATOM 3241 C CB A SER A 1 401 ? 22.487 41.341 55.464 0.50 23.65 ? 455 SER A CB 1 ATOM 3242 C CB B SER A 1 401 ? 22.387 41.525 55.489 0.50 25.01 ? 455 SER A CB 1 ATOM 3243 O OG A SER A 1 401 ? 21.147 41.365 55.922 0.50 21.24 ? 455 SER A OG 1 ATOM 3244 O OG B SER A 1 401 ? 22.832 40.192 55.415 0.50 27.25 ? 455 SER A OG 1 ATOM 3245 N N . ILE A 1 402 ? 24.546 41.392 52.915 1.00 26.93 ? 456 ILE A N 1 ATOM 3246 C CA . ILE A 1 402 ? 25.947 41.340 52.487 1.00 29.16 ? 456 ILE A CA 1 ATOM 3247 C C . ILE A 1 402 ? 26.033 41.296 50.979 1.00 30.13 ? 456 ILE A C 1 ATOM 3248 O O . ILE A 1 402 ? 25.317 40.552 50.338 1.00 34.23 ? 456 ILE A O 1 ATOM 3249 C CB . ILE A 1 402 ? 26.688 40.115 53.109 1.00 29.01 ? 456 ILE A CB 1 ATOM 3250 C CG1 . ILE A 1 402 ? 25.855 38.822 52.980 1.00 30.75 ? 456 ILE A CG1 1 ATOM 3251 C CG2 . ILE A 1 402 ? 26.938 40.341 54.587 1.00 31.48 ? 456 ILE A CG2 1 ATOM 3252 C CD1 . ILE A 1 402 ? 26.583 37.697 52.275 1.00 37.64 ? 456 ILE A CD1 1 ATOM 3253 N N A GLU A 1 403 ? 26.904 42.094 50.393 0.50 29.97 ? 457 GLU A N 1 ATOM 3254 N N B GLU A 1 403 ? 26.909 42.113 50.425 0.50 29.87 ? 457 GLU A N 1 ATOM 3255 C CA A GLU A 1 403 ? 27.263 41.912 48.985 0.50 29.50 ? 457 GLU A CA 1 ATOM 3256 C CA B GLU A 1 403 ? 27.255 42.051 49.011 0.50 29.32 ? 457 GLU A CA 1 ATOM 3257 C C A GLU A 1 403 ? 28.781 41.795 48.913 0.50 29.50 ? 457 GLU A C 1 ATOM 3258 C C B GLU A 1 403 ? 28.792 42.009 48.932 0.50 29.48 ? 457 GLU A C 1 ATOM 3259 O O A GLU A 1 403 ? 29.360 41.722 47.832 0.50 29.46 ? 457 GLU A O 1 ATOM 3260 O O B GLU A 1 403 ? 29.395 42.166 47.868 0.50 29.68 ? 457 GLU A O 1 ATOM 3261 C CB A GLU A 1 403 ? 26.748 43.082 48.126 0.50 29.02 ? 457 GLU A CB 1 ATOM 3262 C CB B GLU A 1 403 ? 26.616 43.248 48.261 0.50 28.52 ? 457 GLU A CB 1 ATOM 3263 C CG A GLU A 1 403 ? 26.870 44.409 48.814 0.50 29.22 ? 457 GLU A CG 1 ATOM 3264 C CG B GLU A 1 403 ? 25.081 43.130 48.178 0.50 27.31 ? 457 GLU A CG 1 ATOM 3265 C CD A GLU A 1 403 ? 26.554 45.609 47.927 0.50 28.36 ? 457 GLU A CD 1 ATOM 3266 C CD B GLU A 1 403 ? 24.372 44.330 47.533 0.50 30.00 ? 457 GLU A CD 1 ATOM 3267 O OE1 A GLU A 1 403 ? 25.836 45.468 46.923 0.50 32.00 ? 457 GLU A OE1 1 ATOM 3268 O OE1 B GLU A 1 403 ? 24.877 45.480 47.614 0.50 23.81 ? 457 GLU A OE1 1 ATOM 3269 O OE2 A GLU A 1 403 ? 27.022 46.708 48.255 0.50 27.90 ? 457 GLU A OE2 1 ATOM 3270 O OE2 B GLU A 1 403 ? 23.275 44.107 46.963 0.50 28.99 ? 457 GLU A OE2 1 ATOM 3271 N N . GLY A 1 404 ? 29.411 41.765 50.087 1.00 30.47 ? 458 GLY A N 1 ATOM 3272 C CA . GLY A 1 404 ? 30.878 41.647 50.226 1.00 30.58 ? 458 GLY A CA 1 ATOM 3273 C C . GLY A 1 404 ? 31.155 41.545 51.722 1.00 32.05 ? 458 GLY A C 1 ATOM 3274 O O . GLY A 1 404 ? 30.210 41.486 52.506 1.00 31.71 ? 458 GLY A O 1 ATOM 3275 N N . ASN A 1 405 ? 32.415 41.534 52.139 1.00 31.49 ? 459 ASN A N 1 ATOM 3276 C CA . ASN A 1 405 ? 32.689 41.468 53.598 1.00 32.83 ? 459 ASN A CA 1 ATOM 3277 C C . ASN A 1 405 ? 33.767 42.422 54.052 1.00 31.96 ? 459 ASN A C 1 ATOM 3278 O O . ASN A 1 405 ? 34.466 42.181 55.028 1.00 34.23 ? 459 ASN A O 1 ATOM 3279 C CB . ASN A 1 405 ? 32.973 40.020 54.072 1.00 33.76 ? 459 ASN A CB 1 ATOM 3280 C CG . ASN A 1 405 ? 34.201 39.398 53.401 1.00 35.24 ? 459 ASN A CG 1 ATOM 3281 O OD1 . ASN A 1 405 ? 35.012 40.091 52.785 1.00 33.68 ? 459 ASN A OD1 1 ATOM 3282 N ND2 . ASN A 1 405 ? 34.333 38.064 53.522 1.00 44.39 ? 459 ASN A ND2 1 ATOM 3283 N N . TYR A 1 406 ? 33.874 43.532 53.343 1.00 30.83 ? 460 TYR A N 1 ATOM 3284 C CA . TYR A 1 406 ? 34.899 44.522 53.595 1.00 30.03 ? 460 TYR A CA 1 ATOM 3285 C C . TYR A 1 406 ? 34.466 45.576 54.601 1.00 29.62 ? 460 TYR A C 1 ATOM 3286 O O . TYR A 1 406 ? 35.135 45.788 55.641 1.00 29.92 ? 460 TYR A O 1 ATOM 3287 C CB . TYR A 1 406 ? 35.264 45.183 52.273 1.00 30.38 ? 460 TYR A CB 1 ATOM 3288 C CG . TYR A 1 406 ? 36.392 46.174 52.401 1.00 34.50 ? 460 TYR A CG 1 ATOM 3289 C CD1 . TYR A 1 406 ? 37.679 45.766 52.890 1.00 35.00 ? 460 TYR A CD1 1 ATOM 3290 C CD2 . TYR A 1 406 ? 36.209 47.502 52.025 1.00 33.99 ? 460 TYR A CD2 1 ATOM 3291 C CE1 . TYR A 1 406 ? 38.747 46.686 52.998 1.00 38.79 ? 460 TYR A CE1 1 ATOM 3292 C CE2 . TYR A 1 406 ? 37.261 48.424 52.136 1.00 36.79 ? 460 TYR A CE2 1 ATOM 3293 C CZ . TYR A 1 406 ? 38.517 48.005 52.600 1.00 41.23 ? 460 TYR A CZ 1 ATOM 3294 O OH . TYR A 1 406 ? 39.514 48.955 52.694 1.00 45.69 ? 460 TYR A OH 1 ATOM 3295 N N . THR A 1 407 ? 33.351 46.270 54.333 1.00 27.69 ? 461 THR A N 1 ATOM 3296 C CA . THR A 1 407 ? 32.961 47.283 55.305 1.00 26.05 ? 461 THR A CA 1 ATOM 3297 C C . THR A 1 407 ? 31.482 47.641 55.112 1.00 25.87 ? 461 THR A C 1 ATOM 3298 O O . THR A 1 407 ? 30.847 47.144 54.187 1.00 25.60 ? 461 THR A O 1 ATOM 3299 C CB . THR A 1 407 ? 33.830 48.560 55.219 1.00 27.76 ? 461 THR A CB 1 ATOM 3300 O OG1 . THR A 1 407 ? 33.615 49.387 56.385 1.00 28.25 ? 461 THR A OG1 1 ATOM 3301 C CG2 . THR A 1 407 ? 33.507 49.376 53.968 1.00 27.71 ? 461 THR A CG2 1 ATOM 3302 N N . LEU A 1 408 ? 31.002 48.515 55.977 1.00 24.60 ? 462 LEU A N 1 ATOM 3303 C CA . LEU A 1 408 ? 29.599 48.960 55.924 1.00 24.75 ? 462 LEU A CA 1 ATOM 3304 C C . LEU A 1 408 ? 29.367 49.912 54.767 1.00 24.01 ? 462 LEU A C 1 ATOM 3305 O O . LEU A 1 408 ? 30.292 50.633 54.354 1.00 24.09 ? 462 LEU A O 1 ATOM 3306 C CB . LEU A 1 408 ? 29.246 49.655 57.258 1.00 24.63 ? 462 LEU A CB 1 ATOM 3307 C CG . LEU A 1 408 ? 27.748 49.904 57.518 1.00 23.80 ? 462 LEU A CG 1 ATOM 3308 C CD1 . LEU A 1 408 ? 27.032 48.581 57.804 1.00 25.43 ? 462 LEU A CD1 1 ATOM 3309 C CD2 . LEU A 1 408 ? 27.643 50.889 58.699 1.00 23.88 ? 462 LEU A CD2 1 ATOM 3310 N N . ARG A 1 409 ? 28.112 49.968 54.295 1.00 23.14 ? 463 ARG A N 1 ATOM 3311 C CA . ARG A 1 409 ? 27.723 50.890 53.241 1.00 23.03 ? 463 ARG A CA 1 ATOM 3312 C C . ARG A 1 409 ? 26.327 51.365 53.629 1.00 21.87 ? 463 ARG A C 1 ATOM 3313 O O . ARG A 1 409 ? 25.432 50.556 53.851 1.00 20.53 ? 463 ARG A O 1 ATOM 3314 C CB . ARG A 1 409 ? 27.653 50.128 51.912 1.00 23.67 ? 463 ARG A CB 1 ATOM 3315 C CG . ARG A 1 409 ? 27.215 50.981 50.686 1.00 24.84 ? 463 ARG A CG 1 ATOM 3316 C CD . ARG A 1 409 ? 27.136 50.047 49.477 1.00 30.40 ? 463 ARG A CD 1 ATOM 3317 N NE . ARG A 1 409 ? 26.805 50.774 48.260 1.00 36.74 ? 463 ARG A NE 1 ATOM 3318 C CZ . ARG A 1 409 ? 26.498 50.241 47.074 1.00 39.01 ? 463 ARG A CZ 1 ATOM 3319 N NH1 . ARG A 1 409 ? 26.496 48.918 46.868 1.00 39.49 ? 463 ARG A NH1 1 ATOM 3320 N NH2 . ARG A 1 409 ? 26.198 51.056 46.067 1.00 37.97 ? 463 ARG A NH2 1 ATOM 3321 N N . VAL A 1 410 ? 26.181 52.669 53.785 1.00 21.87 ? 464 VAL A N 1 ATOM 3322 C CA . VAL A 1 410 ? 24.911 53.242 54.222 1.00 21.94 ? 464 VAL A CA 1 ATOM 3323 C C . VAL A 1 410 ? 24.524 54.268 53.156 1.00 22.05 ? 464 VAL A C 1 ATOM 3324 O O . VAL A 1 410 ? 25.331 55.103 52.800 1.00 23.06 ? 464 VAL A O 1 ATOM 3325 C CB . VAL A 1 410 ? 25.090 53.969 55.570 1.00 23.53 ? 464 VAL A CB 1 ATOM 3326 C CG1 . VAL A 1 410 ? 23.802 54.792 56.010 1.00 23.27 ? 464 VAL A CG1 1 ATOM 3327 C CG2 . VAL A 1 410 ? 25.582 52.952 56.683 1.00 22.47 ? 464 VAL A CG2 1 ATOM 3328 N N . ASP A 1 411 ? 23.256 54.251 52.765 1.00 21.57 ? 465 ASP A N 1 ATOM 3329 C CA . ASP A 1 411 ? 22.663 55.303 51.943 1.00 22.49 ? 465 ASP A CA 1 ATOM 3330 C C . ASP A 1 411 ? 21.417 55.766 52.699 1.00 20.80 ? 465 ASP A C 1 ATOM 3331 O O . ASP A 1 411 ? 20.595 54.962 53.123 1.00 20.56 ? 465 ASP A O 1 ATOM 3332 C CB . ASP A 1 411 ? 22.186 54.826 50.552 1.00 21.17 ? 465 ASP A CB 1 ATOM 3333 C CG . ASP A 1 411 ? 23.205 54.005 49.735 1.00 28.58 ? 465 ASP A CG 1 ATOM 3334 O OD1 . ASP A 1 411 ? 24.318 53.747 50.143 1.00 29.46 ? 465 ASP A OD1 1 ATOM 3335 O OD2 . ASP A 1 411 ? 22.808 53.544 48.621 1.00 32.51 ? 465 ASP A OD2 1 ATOM 3336 N N . CYS A 1 412 ? 21.274 57.065 52.901 1.00 20.65 ? 466 CYS A N 1 ATOM 3337 C CA . CYS A 1 412 ? 20.127 57.527 53.669 1.00 20.38 ? 466 CYS A CA 1 ATOM 3338 C C . CYS A 1 412 ? 19.934 59.009 53.451 1.00 19.98 ? 466 CYS A C 1 ATOM 3339 O O . CYS A 1 412 ? 20.762 59.706 52.851 1.00 22.09 ? 466 CYS A O 1 ATOM 3340 C CB . CYS A 1 412 ? 20.263 57.216 55.226 1.00 19.79 ? 466 CYS A CB 1 ATOM 3341 S SG . CYS A 1 412 ? 21.645 58.085 56.014 1.00 23.61 ? 466 CYS A SG 1 ATOM 3342 N N . THR A 1 413 ? 18.794 59.480 53.926 1.00 20.00 ? 467 THR A N 1 ATOM 3343 C CA A THR A 1 413 ? 18.523 60.908 54.006 0.40 19.33 ? 467 THR A CA 1 ATOM 3344 C CA B THR A 1 413 ? 18.518 60.907 54.006 0.20 19.74 ? 467 THR A CA 1 ATOM 3345 C CA C THR A 1 413 ? 18.523 60.908 54.006 0.40 19.33 ? 467 THR A CA 1 ATOM 3346 C C . THR A 1 413 ? 19.494 61.591 54.964 1.00 20.64 ? 467 THR A C 1 ATOM 3347 O O . THR A 1 413 ? 19.881 60.996 55.994 1.00 20.72 ? 467 THR A O 1 ATOM 3348 C CB A THR A 1 413 ? 17.066 61.171 54.485 0.40 18.48 ? 467 THR A CB 1 ATOM 3349 C CB B THR A 1 413 ? 17.058 61.171 54.470 0.20 19.24 ? 467 THR A CB 1 ATOM 3350 C CB C THR A 1 413 ? 17.066 61.171 54.485 0.40 18.48 ? 467 THR A CB 1 ATOM 3351 O OG1 A THR A 1 413 ? 16.883 62.573 54.706 0.40 18.89 ? 467 THR A OG1 1 ATOM 3352 O OG1 B THR A 1 413 ? 16.873 62.571 54.705 0.20 19.49 ? 467 THR A OG1 1 ATOM 3353 O OG1 C THR A 1 413 ? 16.883 62.572 54.705 0.40 18.89 ? 467 THR A OG1 1 ATOM 3354 C CG2 A THR A 1 413 ? 16.744 60.425 55.792 0.40 18.36 ? 467 THR A CG2 1 ATOM 3355 C CG2 B THR A 1 413 ? 16.719 60.404 55.756 0.20 19.24 ? 467 THR A CG2 1 ATOM 3356 C CG2 C THR A 1 413 ? 16.744 60.425 55.792 0.40 18.36 ? 467 THR A CG2 1 ATOM 3357 N N . PRO A 1 414 ? 19.893 62.835 54.655 1.00 20.35 ? 468 PRO A N 1 ATOM 3358 C CA . PRO A 1 414 ? 20.747 63.537 55.628 1.00 21.77 ? 468 PRO A CA 1 ATOM 3359 C C . PRO A 1 414 ? 20.096 63.580 57.032 1.00 22.05 ? 468 PRO A C 1 ATOM 3360 O O . PRO A 1 414 ? 20.821 63.740 58.003 1.00 22.90 ? 468 PRO A O 1 ATOM 3361 C CB . PRO A 1 414 ? 20.802 64.996 55.089 1.00 22.66 ? 468 PRO A CB 1 ATOM 3362 C CG . PRO A 1 414 ? 20.515 64.887 53.695 1.00 23.31 ? 468 PRO A CG 1 ATOM 3363 C CD . PRO A 1 414 ? 19.662 63.636 53.431 1.00 19.26 ? 468 PRO A CD 1 ATOM 3364 N N . LEU A 1 415 ? 18.749 63.488 57.135 1.00 20.32 ? 469 LEU A N 1 ATOM 3365 C CA . LEU A 1 415 ? 18.104 63.530 58.461 1.00 20.79 ? 469 LEU A CA 1 ATOM 3366 C C . LEU A 1 415 ? 18.577 62.388 59.362 1.00 20.82 ? 469 LEU A C 1 ATOM 3367 O O . LEU A 1 415 ? 18.442 62.487 60.562 1.00 22.30 ? 469 LEU A O 1 ATOM 3368 C CB . LEU A 1 415 ? 16.565 63.462 58.368 1.00 20.31 ? 469 LEU A CB 1 ATOM 3369 C CG . LEU A 1 415 ? 15.969 64.711 57.729 1.00 17.80 ? 469 LEU A CG 1 ATOM 3370 C CD1 . LEU A 1 415 ? 14.466 64.541 57.675 1.00 21.07 ? 469 LEU A CD1 1 ATOM 3371 C CD2 . LEU A 1 415 ? 16.313 66.005 58.573 1.00 20.18 ? 469 LEU A CD2 1 ATOM 3372 N N . MET A 1 416 ? 19.131 61.332 58.787 1.00 20.69 ? 470 MET A N 1 ATOM 3373 C CA A MET A 1 416 ? 19.565 60.168 59.565 0.60 21.07 ? 470 MET A CA 1 ATOM 3374 C CA B MET A 1 416 ? 19.565 60.221 59.623 0.40 21.37 ? 470 MET A CA 1 ATOM 3375 C C . MET A 1 416 ? 21.086 60.160 59.797 1.00 22.00 ? 470 MET A C 1 ATOM 3376 O O . MET A 1 416 ? 21.596 59.279 60.489 1.00 22.13 ? 470 MET A O 1 ATOM 3377 C CB A MET A 1 416 ? 19.151 58.858 58.858 0.60 20.52 ? 470 MET A CB 1 ATOM 3378 C CB B MET A 1 416 ? 19.006 58.899 59.092 0.40 21.55 ? 470 MET A CB 1 ATOM 3379 C CG A MET A 1 416 ? 17.645 58.592 58.900 0.60 21.11 ? 470 MET A CG 1 ATOM 3380 C CG B MET A 1 416 ? 17.496 58.800 59.293 0.40 21.77 ? 470 MET A CG 1 ATOM 3381 S SD A MET A 1 416 ? 17.282 57.008 58.106 0.60 20.65 ? 470 MET A SD 1 ATOM 3382 S SD B MET A 1 416 ? 16.878 57.147 58.938 0.40 26.94 ? 470 MET A SD 1 ATOM 3383 C CE A MET A 1 416 ? 15.498 57.025 58.081 0.60 21.20 ? 470 MET A CE 1 ATOM 3384 C CE B MET A 1 416 ? 15.282 57.538 58.259 0.40 25.64 ? 470 MET A CE 1 ATOM 3385 N N . TYR A 1 417 ? 21.816 61.119 59.242 1.00 21.99 ? 471 TYR A N 1 ATOM 3386 C CA . TYR A 1 417 ? 23.306 61.032 59.354 1.00 23.62 ? 471 TYR A CA 1 ATOM 3387 C C . TYR A 1 417 ? 23.796 60.912 60.820 1.00 24.99 ? 471 TYR A C 1 ATOM 3388 O O . TYR A 1 417 ? 24.666 60.084 61.133 1.00 25.95 ? 471 TYR A O 1 ATOM 3389 C CB . TYR A 1 417 ? 24.022 62.232 58.754 1.00 23.94 ? 471 TYR A CB 1 ATOM 3390 C CG . TYR A 1 417 ? 24.032 62.378 57.246 1.00 22.44 ? 471 TYR A CG 1 ATOM 3391 C CD1 . TYR A 1 417 ? 23.550 61.362 56.393 1.00 20.51 ? 471 TYR A CD1 1 ATOM 3392 C CD2 . TYR A 1 417 ? 24.473 63.575 56.692 1.00 21.61 ? 471 TYR A CD2 1 ATOM 3393 C CE1 . TYR A 1 417 ? 23.546 61.559 54.991 1.00 22.99 ? 471 TYR A CE1 1 ATOM 3394 C CE2 . TYR A 1 417 ? 24.491 63.771 55.326 1.00 24.13 ? 471 TYR A CE2 1 ATOM 3395 C CZ . TYR A 1 417 ? 24.027 62.768 54.484 1.00 24.92 ? 471 TYR A CZ 1 ATOM 3396 O OH . TYR A 1 417 ? 24.022 63.030 53.139 1.00 23.82 ? 471 TYR A OH 1 ATOM 3397 N N . SER A 1 418 ? 23.234 61.745 61.692 1.00 25.57 ? 472 SER A N 1 ATOM 3398 C CA . SER A 1 418 ? 23.677 61.812 63.097 1.00 25.06 ? 472 SER A CA 1 ATOM 3399 C C . SER A 1 418 ? 23.322 60.565 63.833 1.00 25.27 ? 472 SER A C 1 ATOM 3400 O O . SER A 1 418 ? 24.180 60.010 64.550 1.00 25.19 ? 472 SER A O 1 ATOM 3401 C CB . SER A 1 418 ? 23.039 62.999 63.802 1.00 26.08 ? 472 SER A CB 1 ATOM 3402 O OG A SER A 1 418 ? 23.440 64.199 63.153 0.50 29.93 ? 472 SER A OG 1 ATOM 3403 O OG B SER A 1 418 ? 23.579 63.195 65.100 0.50 19.55 ? 472 SER A OG 1 ATOM 3404 N N . LEU A 1 419 ? 22.080 60.096 63.634 1.00 25.12 ? 473 LEU A N 1 ATOM 3405 C CA . LEU A 1 419 ? 21.633 58.770 64.106 1.00 24.95 ? 473 LEU A CA 1 ATOM 3406 C C . LEU A 1 419 ? 22.639 57.662 63.726 1.00 25.98 ? 473 LEU A C 1 ATOM 3407 O O . LEU A 1 419 ? 23.064 56.855 64.587 1.00 25.80 ? 473 LEU A O 1 ATOM 3408 C CB . LEU A 1 419 ? 20.238 58.440 63.565 1.00 25.15 ? 473 LEU A CB 1 ATOM 3409 C CG . LEU A 1 419 ? 19.769 56.986 63.639 1.00 26.92 ? 473 LEU A CG 1 ATOM 3410 C CD1 . LEU A 1 419 ? 19.652 56.579 65.093 1.00 31.10 ? 473 LEU A CD1 1 ATOM 3411 C CD2 . LEU A 1 419 ? 18.461 56.844 62.953 1.00 30.92 ? 473 LEU A CD2 1 ATOM 3412 N N . VAL A 1 420 ? 23.034 57.624 62.458 1.00 24.85 ? 474 VAL A N 1 ATOM 3413 C CA . VAL A 1 420 ? 23.910 56.540 61.958 1.00 24.52 ? 474 VAL A CA 1 ATOM 3414 C C . VAL A 1 420 ? 25.308 56.668 62.579 1.00 25.08 ? 474 VAL A C 1 ATOM 3415 O O . VAL A 1 420 ? 25.863 55.673 63.062 1.00 25.21 ? 474 VAL A O 1 ATOM 3416 C CB . VAL A 1 420 ? 24.040 56.564 60.389 1.00 23.27 ? 474 VAL A CB 1 ATOM 3417 C CG1 . VAL A 1 420 ? 25.130 55.563 59.918 1.00 25.37 ? 474 VAL A CG1 1 ATOM 3418 C CG2 . VAL A 1 420 ? 22.663 56.167 59.763 1.00 25.35 ? 474 VAL A CG2 1 ATOM 3419 N N . HIS A 1 421 ? 25.859 57.878 62.575 1.00 25.68 ? 475 HIS A N 1 ATOM 3420 C CA . HIS A 1 421 ? 27.145 58.120 63.284 1.00 28.17 ? 475 HIS A CA 1 ATOM 3421 C C . HIS A 1 421 ? 27.097 57.661 64.756 1.00 28.65 ? 475 HIS A C 1 ATOM 3422 O O . HIS A 1 421 ? 27.991 56.919 65.202 1.00 28.39 ? 475 HIS A O 1 ATOM 3423 C CB . HIS A 1 421 ? 27.557 59.590 63.221 1.00 28.21 ? 475 HIS A CB 1 ATOM 3424 C CG . HIS A 1 421 ? 27.848 60.055 61.832 1.00 31.63 ? 475 HIS A CG 1 ATOM 3425 N ND1 . HIS A 1 421 ? 27.777 61.378 61.460 1.00 38.15 ? 475 HIS A ND1 1 ATOM 3426 C CD2 . HIS A 1 421 ? 28.147 59.362 60.708 1.00 33.29 ? 475 HIS A CD2 1 ATOM 3427 C CE1 . HIS A 1 421 ? 28.043 61.482 60.168 1.00 38.66 ? 475 HIS A CE1 1 ATOM 3428 N NE2 . HIS A 1 421 ? 28.287 60.277 59.694 1.00 32.94 ? 475 HIS A NE2 1 ATOM 3429 N N . ASN A 1 422 ? 26.080 58.113 65.492 1.00 28.40 ? 476 ASN A N 1 ATOM 3430 C CA . ASN A 1 422 ? 25.977 57.789 66.916 1.00 28.66 ? 476 ASN A CA 1 ATOM 3431 C C . ASN A 1 422 ? 25.786 56.300 67.162 1.00 28.95 ? 476 ASN A C 1 ATOM 3432 O O . ASN A 1 422 ? 26.385 55.734 68.105 1.00 29.93 ? 476 ASN A O 1 ATOM 3433 C CB . ASN A 1 422 ? 24.827 58.550 67.582 1.00 27.54 ? 476 ASN A CB 1 ATOM 3434 C CG . ASN A 1 422 ? 25.103 60.040 67.751 1.00 30.29 ? 476 ASN A CG 1 ATOM 3435 O OD1 . ASN A 1 422 ? 26.137 60.551 67.339 1.00 27.09 ? 476 ASN A OD1 1 ATOM 3436 N ND2 . ASN A 1 422 ? 24.154 60.744 68.363 1.00 31.52 ? 476 ASN A ND2 1 ATOM 3437 N N . LEU A 1 423 ? 24.950 55.648 66.353 1.00 27.37 ? 477 LEU A N 1 ATOM 3438 C CA . LEU A 1 423 ? 24.766 54.219 66.522 1.00 27.20 ? 477 LEU A CA 1 ATOM 3439 C C . LEU A 1 423 ? 26.016 53.401 66.250 1.00 27.38 ? 477 LEU A C 1 ATOM 3440 O O . LEU A 1 423 ? 26.376 52.548 67.064 1.00 28.93 ? 477 LEU A O 1 ATOM 3441 C CB . LEU A 1 423 ? 23.575 53.694 65.700 1.00 26.77 ? 477 LEU A CB 1 ATOM 3442 C CG . LEU A 1 423 ? 23.312 52.184 65.718 1.00 28.01 ? 477 LEU A CG 1 ATOM 3443 C CD1 . LEU A 1 423 ? 22.960 51.689 67.137 1.00 27.63 ? 477 LEU A CD1 1 ATOM 3444 C CD2 . LEU A 1 423 ? 22.182 51.834 64.697 1.00 25.32 ? 477 LEU A CD2 1 ATOM 3445 N N . THR A 1 424 ? 26.671 53.651 65.122 1.00 26.41 ? 478 THR A N 1 ATOM 3446 C CA . THR A 1 424 ? 27.840 52.866 64.739 1.00 27.34 ? 478 THR A CA 1 ATOM 3447 C C . THR A 1 424 ? 28.992 53.097 65.740 1.00 28.10 ? 478 THR A C 1 ATOM 3448 O O . THR A 1 424 ? 29.841 52.213 65.876 1.00 27.82 ? 478 THR A O 1 ATOM 3449 C CB . THR A 1 424 ? 28.329 53.122 63.309 1.00 26.91 ? 478 THR A CB 1 ATOM 3450 O OG1 . THR A 1 424 ? 28.622 54.513 63.131 1.00 25.69 ? 478 THR A OG1 1 ATOM 3451 C CG2 . THR A 1 424 ? 27.248 52.655 62.275 1.00 26.25 ? 478 THR A CG2 1 ATOM 3452 N N . LYS A 1 425 ? 29.006 54.226 66.453 1.00 29.49 ? 479 LYS A N 1 ATOM 3453 C CA . LYS A 1 425 ? 30.058 54.425 67.507 1.00 31.74 ? 479 LYS A CA 1 ATOM 3454 C C . LYS A 1 425 ? 29.845 53.491 68.712 1.00 32.98 ? 479 LYS A C 1 ATOM 3455 O O . LYS A 1 425 ? 30.779 53.249 69.492 1.00 32.79 ? 479 LYS A O 1 ATOM 3456 C CB . LYS A 1 425 ? 30.124 55.883 68.001 1.00 32.22 ? 479 LYS A CB 1 ATOM 3457 C CG . LYS A 1 425 ? 30.739 56.827 66.960 1.00 33.05 ? 479 LYS A CG 1 ATOM 3458 C CD . LYS A 1 425 ? 30.708 58.288 67.382 1.00 35.08 ? 479 LYS A CD 1 ATOM 3459 C CE . LYS A 1 425 ? 31.140 59.128 66.185 1.00 33.97 ? 479 LYS A CE 1 ATOM 3460 N NZ . LYS A 1 425 ? 31.018 60.571 66.477 1.00 37.34 ? 479 LYS A NZ 1 ATOM 3461 N N . GLU A 1 426 ? 28.633 52.963 68.852 1.00 32.33 ? 480 GLU A N 1 ATOM 3462 C CA . GLU A 1 426 ? 28.263 52.148 70.018 1.00 34.15 ? 480 GLU A CA 1 ATOM 3463 C C . GLU A 1 426 ? 28.232 50.669 69.689 1.00 33.58 ? 480 GLU A C 1 ATOM 3464 O O . GLU A 1 426 ? 28.003 49.839 70.584 1.00 34.86 ? 480 GLU A O 1 ATOM 3465 C CB . GLU A 1 426 ? 26.888 52.557 70.588 1.00 34.34 ? 480 GLU A CB 1 ATOM 3466 C CG . GLU A 1 426 ? 26.756 53.989 71.027 1.00 40.86 ? 480 GLU A CG 1 ATOM 3467 C CD . GLU A 1 426 ? 27.692 54.401 72.163 1.00 48.90 ? 480 GLU A CD 1 ATOM 3468 O OE1 . GLU A 1 426 ? 28.120 53.532 72.966 1.00 49.51 ? 480 GLU A OE1 1 ATOM 3469 O OE2 . GLU A 1 426 ? 27.984 55.618 72.249 1.00 52.75 ? 480 GLU A OE2 1 ATOM 3470 N N . LEU A 1 427 ? 28.455 50.326 68.422 1.00 31.51 ? 481 LEU A N 1 ATOM 3471 C CA . LEU A 1 427 ? 28.499 48.944 67.985 1.00 30.86 ? 481 LEU A CA 1 ATOM 3472 C C . LEU A 1 427 ? 29.928 48.437 67.794 1.00 31.36 ? 481 LEU A C 1 ATOM 3473 O O . LEU A 1 427 ? 30.811 49.198 67.398 1.00 32.05 ? 481 LEU A O 1 ATOM 3474 C CB . LEU A 1 427 ? 27.753 48.749 66.635 1.00 30.07 ? 481 LEU A CB 1 ATOM 3475 C CG . LEU A 1 427 ? 26.248 49.128 66.670 1.00 29.58 ? 481 LEU A CG 1 ATOM 3476 C CD1 . LEU A 1 427 ? 25.616 49.005 65.260 1.00 27.28 ? 481 LEU A CD1 1 ATOM 3477 C CD2 . LEU A 1 427 ? 25.494 48.240 67.686 1.00 27.08 ? 481 LEU A CD2 1 ATOM 3478 N N . LYS A 1 428 ? 30.122 47.149 68.028 1.00 31.84 ? 482 LYS A N 1 ATOM 3479 C CA . LYS A 1 428 ? 31.464 46.548 67.891 1.00 33.71 ? 482 LYS A CA 1 ATOM 3480 C C . LYS A 1 428 ? 31.759 46.266 66.422 1.00 33.17 ? 482 LYS A C 1 ATOM 3481 O O . LYS A 1 428 ? 30.878 45.766 65.700 1.00 34.25 ? 482 LYS A O 1 ATOM 3482 C CB . LYS A 1 428 ? 31.572 45.246 68.715 1.00 33.66 ? 482 LYS A CB 1 ATOM 3483 C CG . LYS A 1 428 ? 31.248 45.459 70.201 1.00 37.47 ? 482 LYS A CG 1 ATOM 3484 C CD . LYS A 1 428 ? 31.444 44.197 71.036 1.00 48.38 ? 482 LYS A CD 1 ATOM 3485 C CE . LYS A 1 428 ? 30.500 43.084 70.594 1.00 53.62 ? 482 LYS A CE 1 ATOM 3486 N NZ . LYS A 1 428 ? 30.211 42.174 71.749 1.00 59.30 ? 482 LYS A NZ 1 ATOM 3487 N N . SER A 1 429 ? 32.956 46.614 65.967 1.00 31.71 ? 483 SER A N 1 ATOM 3488 C CA . SER A 1 429 ? 33.366 46.180 64.640 1.00 31.76 ? 483 SER A CA 1 ATOM 3489 C C . SER A 1 429 ? 33.543 44.671 64.539 1.00 33.10 ? 483 SER A C 1 ATOM 3490 O O . SER A 1 429 ? 34.236 44.042 65.371 1.00 34.29 ? 483 SER A O 1 ATOM 3491 C CB . SER A 1 429 ? 34.630 46.877 64.149 1.00 31.45 ? 483 SER A CB 1 ATOM 3492 O OG . SER A 1 429 ? 34.991 46.360 62.867 1.00 30.55 ? 483 SER A OG 1 ATOM 3493 N N . PRO A 1 430 ? 32.988 44.068 63.482 1.00 32.31 ? 484 PRO A N 1 ATOM 3494 C CA . PRO A 1 430 ? 33.279 42.645 63.305 1.00 32.77 ? 484 PRO A CA 1 ATOM 3495 C C . PRO A 1 430 ? 34.546 42.417 62.467 1.00 33.04 ? 484 PRO A C 1 ATOM 3496 O O . PRO A 1 430 ? 34.859 41.255 62.168 1.00 32.51 ? 484 PRO A O 1 ATOM 3497 C CB . PRO A 1 430 ? 32.077 42.155 62.489 1.00 31.31 ? 484 PRO A CB 1 ATOM 3498 C CG . PRO A 1 430 ? 31.763 43.387 61.598 1.00 32.04 ? 484 PRO A CG 1 ATOM 3499 C CD . PRO A 1 430 ? 32.007 44.578 62.491 1.00 32.47 ? 484 PRO A CD 1 ATOM 3500 N N . ASP A 1 431 ? 35.234 43.495 62.063 1.00 33.11 ? 485 ASP A N 1 ATOM 3501 C CA . ASP A 1 431 ? 36.267 43.404 61.033 1.00 34.40 ? 485 ASP A CA 1 ATOM 3502 C C . ASP A 1 431 ? 37.583 42.879 61.638 1.00 35.95 ? 485 ASP A C 1 ATOM 3503 O O . ASP A 1 431 ? 37.954 43.251 62.772 1.00 36.39 ? 485 ASP A O 1 ATOM 3504 C CB . ASP A 1 431 ? 36.594 44.773 60.432 1.00 33.78 ? 485 ASP A CB 1 ATOM 3505 C CG . ASP A 1 431 ? 35.450 45.354 59.599 1.00 34.88 ? 485 ASP A CG 1 ATOM 3506 O OD1 . ASP A 1 431 ? 34.360 44.767 59.597 1.00 31.86 ? 485 ASP A OD1 1 ATOM 3507 O OD2 . ASP A 1 431 ? 35.655 46.402 58.962 1.00 34.40 ? 485 ASP A OD2 1 ATOM 3508 N N . GLU A 1 432 ? 38.284 42.076 60.860 1.00 37.56 ? 486 GLU A N 1 ATOM 3509 C CA . GLU A 1 432 ? 39.626 41.592 61.256 1.00 39.66 ? 486 GLU A CA 1 ATOM 3510 C C . GLU A 1 432 ? 40.581 42.768 61.423 1.00 39.47 ? 486 GLU A C 1 ATOM 3511 O O . GLU A 1 432 ? 40.645 43.669 60.571 1.00 39.04 ? 486 GLU A O 1 ATOM 3512 C CB . GLU A 1 432 ? 40.143 40.583 60.225 1.00 39.69 ? 486 GLU A CB 1 ATOM 3513 C CG . GLU A 1 432 ? 39.422 39.238 60.273 1.00 44.39 ? 486 GLU A CG 1 ATOM 3514 C CD . GLU A 1 432 ? 38.166 39.154 59.398 1.00 50.19 ? 486 GLU A CD 1 ATOM 3515 O OE1 . GLU A 1 432 ? 37.557 38.056 59.405 1.00 51.57 ? 486 GLU A OE1 1 ATOM 3516 O OE2 . GLU A 1 432 ? 37.778 40.165 58.720 1.00 51.64 ? 486 GLU A OE2 1 ATOM 3517 N N . GLY A 1 433 ? 41.306 42.783 62.538 1.00 40.70 ? 487 GLY A N 1 ATOM 3518 C CA . GLY A 1 433 ? 42.180 43.914 62.861 1.00 40.75 ? 487 GLY A CA 1 ATOM 3519 C C . GLY A 1 433 ? 41.499 45.052 63.606 1.00 41.20 ? 487 GLY A C 1 ATOM 3520 O O . GLY A 1 433 ? 42.165 46.023 64.016 1.00 42.18 ? 487 GLY A O 1 ATOM 3521 N N . PHE A 1 434 ? 40.178 44.972 63.789 1.00 39.39 ? 488 PHE A N 1 ATOM 3522 C CA . PHE A 1 434 ? 39.480 46.017 64.528 1.00 38.57 ? 488 PHE A CA 1 ATOM 3523 C C . PHE A 1 434 ? 38.783 45.448 65.744 1.00 38.90 ? 488 PHE A C 1 ATOM 3524 O O . PHE A 1 434 ? 37.782 46.004 66.207 1.00 37.72 ? 488 PHE A O 1 ATOM 3525 C CB . PHE A 1 434 ? 38.469 46.757 63.629 1.00 37.58 ? 488 PHE A CB 1 ATOM 3526 C CG . PHE A 1 434 ? 39.109 47.564 62.554 1.00 35.86 ? 488 PHE A CG 1 ATOM 3527 C CD1 . PHE A 1 434 ? 39.421 48.892 62.762 1.00 37.05 ? 488 PHE A CD1 1 ATOM 3528 C CD2 . PHE A 1 434 ? 39.427 46.978 61.334 1.00 35.23 ? 488 PHE A CD2 1 ATOM 3529 C CE1 . PHE A 1 434 ? 40.031 49.655 61.762 1.00 38.91 ? 488 PHE A CE1 1 ATOM 3530 C CE2 . PHE A 1 434 ? 40.038 47.726 60.329 1.00 37.39 ? 488 PHE A CE2 1 ATOM 3531 C CZ . PHE A 1 434 ? 40.339 49.056 60.546 1.00 36.31 ? 488 PHE A CZ 1 ATOM 3532 N N . GLU A 1 435 ? 39.308 44.335 66.254 1.00 38.86 ? 489 GLU A N 1 ATOM 3533 C CA . GLU A 1 435 ? 38.809 43.735 67.494 1.00 40.01 ? 489 GLU A CA 1 ATOM 3534 C C . GLU A 1 435 ? 38.825 44.752 68.634 1.00 40.06 ? 489 GLU A C 1 ATOM 3535 O O . GLU A 1 435 ? 39.797 45.475 68.822 1.00 41.57 ? 489 GLU A O 1 ATOM 3536 C CB . GLU A 1 435 ? 39.628 42.489 67.881 1.00 40.50 ? 489 GLU A CB 1 ATOM 3537 C CG . GLU A 1 435 ? 39.509 41.326 66.911 1.00 42.07 ? 489 GLU A CG 1 ATOM 3538 C CD . GLU A 1 435 ? 40.442 41.443 65.693 1.00 43.00 ? 489 GLU A CD 1 ATOM 3539 O OE1 . GLU A 1 435 ? 40.316 40.604 64.802 1.00 42.25 ? 489 GLU A OE1 1 ATOM 3540 O OE2 . GLU A 1 435 ? 41.271 42.379 65.619 1.00 45.87 ? 489 GLU A OE2 1 ATOM 3541 N N . GLY A 1 436 ? 37.716 44.857 69.358 1.00 39.41 ? 490 GLY A N 1 ATOM 3542 C CA . GLY A 1 436 ? 37.617 45.856 70.424 1.00 39.45 ? 490 GLY A CA 1 ATOM 3543 C C . GLY A 1 436 ? 37.435 47.307 69.982 1.00 39.80 ? 490 GLY A C 1 ATOM 3544 O O . GLY A 1 436 ? 37.383 48.216 70.832 1.00 40.08 ? 490 GLY A O 1 ATOM 3545 N N . LYS A 1 437 ? 37.345 47.536 68.666 1.00 38.19 ? 491 LYS A N 1 ATOM 3546 C CA . LYS A 1 437 ? 37.088 48.884 68.138 1.00 37.63 ? 491 LYS A CA 1 ATOM 3547 C C . LYS A 1 437 ? 35.623 48.985 67.675 1.00 35.16 ? 491 LYS A C 1 ATOM 3548 O O . LYS A 1 437 ? 34.963 47.970 67.471 1.00 33.94 ? 491 LYS A O 1 ATOM 3549 C CB . LYS A 1 437 ? 38.000 49.242 66.950 1.00 37.69 ? 491 LYS A CB 1 ATOM 3550 C CG . LYS A 1 437 ? 39.500 49.058 67.194 1.00 42.79 ? 491 LYS A CG 1 ATOM 3551 C CD . LYS A 1 437 ? 39.930 49.779 68.469 1.00 46.16 ? 491 LYS A CD 1 ATOM 3552 C CE . LYS A 1 437 ? 41.425 49.550 68.753 1.00 53.62 ? 491 LYS A CE 1 ATOM 3553 N NZ . LYS A 1 437 ? 42.161 50.830 68.550 1.00 56.13 ? 491 LYS A NZ 1 ATOM 3554 N N . SER A 1 438 ? 35.152 50.213 67.539 1.00 33.94 ? 492 SER A N 1 ATOM 3555 C CA . SER A 1 438 ? 33.760 50.464 67.118 1.00 32.98 ? 492 SER A CA 1 ATOM 3556 C C . SER A 1 438 ? 33.585 50.216 65.609 1.00 31.43 ? 492 SER A C 1 ATOM 3557 O O . SER A 1 438 ? 34.541 50.290 64.831 1.00 31.06 ? 492 SER A O 1 ATOM 3558 C CB . SER A 1 438 ? 33.331 51.874 67.510 1.00 32.29 ? 492 SER A CB 1 ATOM 3559 O OG . SER A 1 438 ? 33.882 52.841 66.628 1.00 33.23 ? 492 SER A OG 1 ATOM 3560 N N . LEU A 1 439 ? 32.348 49.903 65.200 1.00 30.63 ? 493 LEU A N 1 ATOM 3561 C CA . LEU A 1 439 ? 32.016 49.854 63.781 1.00 28.70 ? 493 LEU A CA 1 ATOM 3562 C C . LEU A 1 439 ? 32.306 51.208 63.130 1.00 28.38 ? 493 LEU A C 1 ATOM 3563 O O . LEU A 1 439 ? 32.791 51.243 62.013 1.00 28.54 ? 493 LEU A O 1 ATOM 3564 C CB . LEU A 1 439 ? 30.538 49.466 63.620 1.00 28.63 ? 493 LEU A CB 1 ATOM 3565 C CG . LEU A 1 439 ? 29.996 49.364 62.210 1.00 27.88 ? 493 LEU A CG 1 ATOM 3566 C CD1 . LEU A 1 439 ? 30.848 48.296 61.429 1.00 25.75 ? 493 LEU A CD1 1 ATOM 3567 C CD2 . LEU A 1 439 ? 28.536 48.952 62.326 1.00 25.81 ? 493 LEU A CD2 1 ATOM 3568 N N . TYR A 1 440 ? 32.018 52.313 63.819 1.00 28.66 ? 494 TYR A N 1 ATOM 3569 C CA . TYR A 1 440 ? 32.295 53.631 63.273 1.00 30.42 ? 494 TYR A CA 1 ATOM 3570 C C . TYR A 1 440 ? 33.762 53.795 62.870 1.00 31.61 ? 494 TYR A C 1 ATOM 3571 O O . TYR A 1 440 ? 34.075 54.329 61.790 1.00 31.10 ? 494 TYR A O 1 ATOM 3572 C CB . TYR A 1 440 ? 31.937 54.720 64.270 1.00 30.71 ? 494 TYR A CB 1 ATOM 3573 C CG . TYR A 1 440 ? 32.161 56.126 63.741 1.00 32.62 ? 494 TYR A CG 1 ATOM 3574 C CD1 . TYR A 1 440 ? 31.134 56.810 63.105 1.00 28.89 ? 494 TYR A CD1 1 ATOM 3575 C CD2 . TYR A 1 440 ? 33.403 56.779 63.897 1.00 31.98 ? 494 TYR A CD2 1 ATOM 3576 C CE1 . TYR A 1 440 ? 31.309 58.101 62.629 1.00 31.44 ? 494 TYR A CE1 1 ATOM 3577 C CE2 . TYR A 1 440 ? 33.594 58.077 63.405 1.00 33.01 ? 494 TYR A CE2 1 ATOM 3578 C CZ . TYR A 1 440 ? 32.539 58.733 62.780 1.00 31.19 ? 494 TYR A CZ 1 ATOM 3579 O OH . TYR A 1 440 ? 32.685 60.016 62.304 1.00 30.63 ? 494 TYR A OH 1 ATOM 3580 N N . GLU A 1 441 ? 34.650 53.342 63.754 1.00 31.71 ? 495 GLU A N 1 ATOM 3581 C CA . GLU A 1 441 ? 36.101 53.413 63.481 1.00 34.02 ? 495 GLU A CA 1 ATOM 3582 C C . GLU A 1 441 ? 36.515 52.597 62.247 1.00 32.42 ? 495 GLU A C 1 ATOM 3583 O O . GLU A 1 441 ? 37.208 53.128 61.383 1.00 32.22 ? 495 GLU A O 1 ATOM 3584 C CB . GLU A 1 441 ? 36.909 52.936 64.701 1.00 35.50 ? 495 GLU A CB 1 ATOM 3585 C CG . GLU A 1 441 ? 38.428 53.043 64.459 1.00 39.78 ? 495 GLU A CG 1 ATOM 3586 C CD . GLU A 1 441 ? 39.256 52.957 65.740 1.00 44.11 ? 495 GLU A CD 1 ATOM 3587 O OE1 . GLU A 1 441 ? 38.857 53.562 66.767 1.00 46.56 ? 495 GLU A OE1 1 ATOM 3588 O OE2 . GLU A 1 441 ? 40.308 52.300 65.689 1.00 44.57 ? 495 GLU A OE2 1 ATOM 3589 N N . SER A 1 442 ? 36.075 51.335 62.162 1.00 31.87 ? 496 SER A N 1 ATOM 3590 C CA . SER A 1 442 ? 36.433 50.476 61.028 1.00 31.93 ? 496 SER A CA 1 ATOM 3591 C C . SER A 1 442 ? 35.861 50.994 59.708 1.00 31.97 ? 496 SER A C 1 ATOM 3592 O O . SER A 1 442 ? 36.536 51.020 58.697 1.00 32.08 ? 496 SER A O 1 ATOM 3593 C CB . SER A 1 442 ? 36.108 48.985 61.261 1.00 32.13 ? 496 SER A CB 1 ATOM 3594 O OG . SER A 1 442 ? 34.730 48.702 61.332 1.00 30.43 ? 496 SER A OG 1 ATOM 3595 N N . TRP A 1 443 ? 34.612 51.436 59.753 1.00 30.28 ? 497 TRP A N 1 ATOM 3596 C CA . TRP A 1 443 ? 33.917 51.924 58.582 1.00 29.87 ? 497 TRP A CA 1 ATOM 3597 C C . TRP A 1 443 ? 34.543 53.238 58.096 1.00 30.62 ? 497 TRP A C 1 ATOM 3598 O O . TRP A 1 443 ? 34.784 53.420 56.897 1.00 30.67 ? 497 TRP A O 1 ATOM 3599 C CB . TRP A 1 443 ? 32.443 52.098 58.992 1.00 29.50 ? 497 TRP A CB 1 ATOM 3600 C CG . TRP A 1 443 ? 31.555 52.770 57.984 1.00 28.62 ? 497 TRP A CG 1 ATOM 3601 C CD1 . TRP A 1 443 ? 31.636 52.680 56.625 1.00 27.03 ? 497 TRP A CD1 1 ATOM 3602 C CD2 . TRP A 1 443 ? 30.424 53.600 58.277 1.00 27.89 ? 497 TRP A CD2 1 ATOM 3603 N NE1 . TRP A 1 443 ? 30.625 53.454 56.042 1.00 26.13 ? 497 TRP A NE1 1 ATOM 3604 C CE2 . TRP A 1 443 ? 29.870 54.017 57.030 1.00 28.37 ? 497 TRP A CE2 1 ATOM 3605 C CE3 . TRP A 1 443 ? 29.839 54.062 59.470 1.00 27.14 ? 497 TRP A CE3 1 ATOM 3606 C CZ2 . TRP A 1 443 ? 28.752 54.865 56.939 1.00 25.10 ? 497 TRP A CZ2 1 ATOM 3607 C CZ3 . TRP A 1 443 ? 28.713 54.887 59.385 1.00 27.35 ? 497 TRP A CZ3 1 ATOM 3608 C CH2 . TRP A 1 443 ? 28.194 55.296 58.112 1.00 26.15 ? 497 TRP A CH2 1 ATOM 3609 N N . THR A 1 444 ? 34.847 54.132 59.038 1.00 30.34 ? 498 THR A N 1 ATOM 3610 C CA . THR A 1 444 ? 35.439 55.403 58.701 1.00 32.74 ? 498 THR A CA 1 ATOM 3611 C C . THR A 1 444 ? 36.848 55.180 58.116 1.00 34.05 ? 498 THR A C 1 ATOM 3612 O O . THR A 1 444 ? 37.241 55.862 57.176 1.00 34.20 ? 498 THR A O 1 ATOM 3613 C CB . THR A 1 444 ? 35.501 56.331 59.932 1.00 33.78 ? 498 THR A CB 1 ATOM 3614 O OG1 . THR A 1 444 ? 34.161 56.728 60.293 1.00 31.61 ? 498 THR A OG1 1 ATOM 3615 C CG2 . THR A 1 444 ? 36.344 57.595 59.638 1.00 36.10 ? 498 THR A CG2 1 ATOM 3616 N N . LYS A 1 445 ? 37.578 54.223 58.673 1.00 34.31 ? 499 LYS A N 1 ATOM 3617 C CA . LYS A 1 445 ? 38.911 53.907 58.163 1.00 37.28 ? 499 LYS A CA 1 ATOM 3618 C C . LYS A 1 445 ? 38.842 53.341 56.742 1.00 37.23 ? 499 LYS A C 1 ATOM 3619 O O . LYS A 1 445 ? 39.561 53.803 55.870 1.00 38.47 ? 499 LYS A O 1 ATOM 3620 C CB . LYS A 1 445 ? 39.660 52.965 59.127 1.00 37.39 ? 499 LYS A CB 1 ATOM 3621 C CG . LYS A 1 445 ? 41.024 52.495 58.611 1.00 42.01 ? 499 LYS A CG 1 ATOM 3622 C CD . LYS A 1 445 ? 42.048 53.621 58.610 1.00 48.12 ? 499 LYS A CD 1 ATOM 3623 C CE . LYS A 1 445 ? 43.468 53.059 58.397 1.00 49.83 ? 499 LYS A CE 1 ATOM 3624 N NZ . LYS A 1 445 ? 44.417 54.207 58.336 1.00 54.11 ? 499 LYS A NZ 1 ATOM 3625 N N . LYS A 1 446 ? 37.929 52.401 56.492 1.00 36.71 ? 500 LYS A N 1 ATOM 3626 C CA . LYS A 1 446 ? 37.876 51.727 55.188 1.00 36.49 ? 500 LYS A CA 1 ATOM 3627 C C . LYS A 1 446 ? 37.134 52.481 54.092 1.00 36.69 ? 500 LYS A C 1 ATOM 3628 O O . LYS A 1 446 ? 37.357 52.218 52.915 1.00 35.59 ? 500 LYS A O 1 ATOM 3629 C CB . LYS A 1 446 ? 37.270 50.353 55.346 1.00 36.30 ? 500 LYS A CB 1 ATOM 3630 C CG . LYS A 1 446 ? 38.194 49.353 56.065 1.00 37.29 ? 500 LYS A CG 1 ATOM 3631 C CD . LYS A 1 446 ? 37.450 48.031 56.236 1.00 38.40 ? 500 LYS A CD 1 ATOM 3632 C CE . LYS A 1 446 ? 38.315 46.937 56.835 1.00 38.44 ? 500 LYS A CE 1 ATOM 3633 N NZ . LYS A 1 446 ? 37.512 45.683 57.027 1.00 38.23 ? 500 LYS A NZ 1 ATOM 3634 N N . SER A 1 447 ? 36.223 53.375 54.488 1.00 36.01 ? 501 SER A N 1 ATOM 3635 C CA . SER A 1 447 ? 35.375 54.109 53.556 1.00 36.13 ? 501 SER A CA 1 ATOM 3636 C C . SER A 1 447 ? 35.328 55.576 54.003 1.00 36.83 ? 501 SER A C 1 ATOM 3637 O O . SER A 1 447 ? 34.303 56.077 54.495 1.00 35.31 ? 501 SER A O 1 ATOM 3638 C CB . SER A 1 447 ? 33.961 53.476 53.544 1.00 35.22 ? 501 SER A CB 1 ATOM 3639 O OG . SER A 1 447 ? 33.202 53.974 52.475 1.00 37.07 ? 501 SER A OG 1 ATOM 3640 N N . PRO A 1 448 ? 36.457 56.297 53.840 1.00 37.03 ? 502 PRO A N 1 ATOM 3641 C CA . PRO A 1 448 ? 36.421 57.663 54.324 1.00 37.28 ? 502 PRO A CA 1 ATOM 3642 C C . PRO A 1 448 ? 35.496 58.567 53.511 1.00 37.22 ? 502 PRO A C 1 ATOM 3643 O O . PRO A 1 448 ? 35.295 58.385 52.306 1.00 36.47 ? 502 PRO A O 1 ATOM 3644 C CB . PRO A 1 448 ? 37.890 58.139 54.187 1.00 37.49 ? 502 PRO A CB 1 ATOM 3645 C CG . PRO A 1 448 ? 38.511 57.212 53.209 1.00 37.82 ? 502 PRO A CG 1 ATOM 3646 C CD . PRO A 1 448 ? 37.758 55.925 53.260 1.00 37.09 ? 502 PRO A CD 1 ATOM 3647 N N . SER A 1 449 ? 34.941 59.541 54.201 1.00 38.39 ? 503 SER A N 1 ATOM 3648 C CA . SER A 1 449 ? 34.242 60.624 53.559 1.00 40.76 ? 503 SER A CA 1 ATOM 3649 C C . SER A 1 449 ? 35.167 61.309 52.559 1.00 43.23 ? 503 SER A C 1 ATOM 3650 O O . SER A 1 449 ? 36.342 61.565 52.876 1.00 43.84 ? 503 SER A O 1 ATOM 3651 C CB . SER A 1 449 ? 33.791 61.619 54.615 1.00 40.60 ? 503 SER A CB 1 ATOM 3652 O OG . SER A 1 449 ? 33.301 62.778 53.999 1.00 40.52 ? 503 SER A OG 1 ATOM 3653 N N . PRO A 1 450 ? 34.665 61.583 51.339 1.00 44.77 ? 504 PRO A N 1 ATOM 3654 C CA . PRO A 1 450 ? 35.529 62.287 50.369 1.00 46.87 ? 504 PRO A CA 1 ATOM 3655 C C . PRO A 1 450 ? 35.727 63.767 50.758 1.00 48.41 ? 504 PRO A C 1 ATOM 3656 O O . PRO A 1 450 ? 36.607 64.449 50.225 1.00 50.12 ? 504 PRO A O 1 ATOM 3657 C CB . PRO A 1 450 ? 34.763 62.154 49.049 1.00 47.09 ? 504 PRO A CB 1 ATOM 3658 C CG . PRO A 1 450 ? 33.324 61.909 49.443 1.00 45.20 ? 504 PRO A CG 1 ATOM 3659 C CD . PRO A 1 450 ? 33.310 61.314 50.819 1.00 43.92 ? 504 PRO A CD 1 ATOM 3660 N N . GLU A 1 451 ? 34.933 64.228 51.721 1.00 48.29 ? 505 GLU A N 1 ATOM 3661 C CA . GLU A 1 451 ? 34.893 65.626 52.123 1.00 49.23 ? 505 GLU A CA 1 ATOM 3662 C C . GLU A 1 451 ? 35.407 65.904 53.540 1.00 48.80 ? 505 GLU A C 1 ATOM 3663 O O . GLU A 1 451 ? 36.075 66.910 53.735 1.00 49.63 ? 505 GLU A O 1 ATOM 3664 C CB . GLU A 1 451 ? 33.462 66.167 51.992 1.00 49.05 ? 505 GLU A CB 1 ATOM 3665 C CG . GLU A 1 451 ? 33.359 67.681 52.046 1.00 51.36 ? 505 GLU A CG 1 ATOM 3666 C CD . GLU A 1 451 ? 31.943 68.182 51.794 1.00 55.08 ? 505 GLU A CD 1 ATOM 3667 O OE1 . GLU A 1 451 ? 31.730 69.429 51.823 1.00 55.24 ? 505 GLU A OE1 1 ATOM 3668 O OE2 . GLU A 1 451 ? 31.043 67.329 51.574 1.00 54.64 ? 505 GLU A OE2 1 ATOM 3669 N N . PHE A 1 452 ? 35.083 65.049 54.519 1.00 47.51 ? 506 PHE A N 1 ATOM 3670 C CA . PHE A 1 452 ? 35.407 65.351 55.929 1.00 47.43 ? 506 PHE A CA 1 ATOM 3671 C C . PHE A 1 452 ? 36.298 64.309 56.610 1.00 46.87 ? 506 PHE A C 1 ATOM 3672 O O . PHE A 1 452 ? 35.958 63.123 56.668 1.00 45.76 ? 506 PHE A O 1 ATOM 3673 C CB . PHE A 1 452 ? 34.135 65.494 56.766 1.00 47.81 ? 506 PHE A CB 1 ATOM 3674 C CG . PHE A 1 452 ? 33.156 66.542 56.265 1.00 48.74 ? 506 PHE A CG 1 ATOM 3675 C CD1 . PHE A 1 452 ? 31.958 66.150 55.644 1.00 48.30 ? 506 PHE A CD1 1 ATOM 3676 C CD2 . PHE A 1 452 ? 33.402 67.914 56.465 1.00 49.68 ? 506 PHE A CD2 1 ATOM 3677 C CE1 . PHE A 1 452 ? 31.015 67.115 55.203 1.00 47.28 ? 506 PHE A CE1 1 ATOM 3678 C CE2 . PHE A 1 452 ? 32.479 68.888 56.015 1.00 51.30 ? 506 PHE A CE2 1 ATOM 3679 C CZ . PHE A 1 452 ? 31.280 68.478 55.381 1.00 49.74 ? 506 PHE A CZ 1 ATOM 3680 N N A SER A 1 453 ? 37.416 64.765 57.162 0.50 47.17 ? 507 SER A N 1 ATOM 3681 N N B SER A 1 453 ? 37.442 64.753 57.131 0.50 47.17 ? 507 SER A N 1 ATOM 3682 C CA A SER A 1 453 ? 38.357 63.870 57.829 0.50 46.61 ? 507 SER A CA 1 ATOM 3683 C CA B SER A 1 453 ? 38.354 63.836 57.823 0.50 46.57 ? 507 SER A CA 1 ATOM 3684 C C A SER A 1 453 ? 37.730 63.331 59.125 0.50 45.59 ? 507 SER A C 1 ATOM 3685 C C B SER A 1 453 ? 37.671 63.309 59.084 0.50 45.52 ? 507 SER A C 1 ATOM 3686 O O A SER A 1 453 ? 37.063 64.078 59.854 0.50 45.87 ? 507 SER A O 1 ATOM 3687 O O B SER A 1 453 ? 36.920 64.041 59.751 0.50 45.66 ? 507 SER A O 1 ATOM 3688 C CB A SER A 1 453 ? 39.660 64.624 58.111 0.50 47.54 ? 507 SER A CB 1 ATOM 3689 C CB B SER A 1 453 ? 39.682 64.518 58.193 0.50 47.52 ? 507 SER A CB 1 ATOM 3690 O OG A SER A 1 453 ? 40.012 65.396 56.974 0.50 47.55 ? 507 SER A OG 1 ATOM 3691 O OG B SER A 1 453 ? 40.561 63.589 58.814 0.50 47.78 ? 507 SER A OG 1 ATOM 3692 N N . GLY A 1 454 ? 37.916 62.037 59.378 1.00 44.27 ? 508 GLY A N 1 ATOM 3693 C CA . GLY A 1 454 ? 37.369 61.386 60.574 1.00 41.92 ? 508 GLY A CA 1 ATOM 3694 C C . GLY A 1 454 ? 35.883 61.011 60.497 1.00 38.88 ? 508 GLY A C 1 ATOM 3695 O O . GLY A 1 454 ? 35.295 60.580 61.516 1.00 38.01 ? 508 GLY A O 1 ATOM 3696 N N A MET A 1 455 ? 35.291 61.169 59.313 0.60 37.46 ? 509 MET A N 1 ATOM 3697 N N B MET A 1 455 ? 35.296 61.196 59.310 0.40 37.10 ? 509 MET A N 1 ATOM 3698 C CA A MET A 1 455 ? 33.902 60.744 59.073 0.60 35.81 ? 509 MET A CA 1 ATOM 3699 C CA B MET A 1 455 ? 33.906 60.808 59.010 0.40 35.08 ? 509 MET A CA 1 ATOM 3700 C C A MET A 1 455 ? 33.793 59.776 57.901 0.60 34.84 ? 509 MET A C 1 ATOM 3701 C C B MET A 1 455 ? 33.883 59.680 57.963 0.40 34.41 ? 509 MET A C 1 ATOM 3702 O O A MET A 1 455 ? 34.583 59.857 56.956 0.60 34.48 ? 509 MET A O 1 ATOM 3703 O O B MET A 1 455 ? 34.825 59.552 57.170 0.40 34.01 ? 509 MET A O 1 ATOM 3704 C CB A MET A 1 455 ? 33.017 61.941 58.809 0.60 35.47 ? 509 MET A CB 1 ATOM 3705 C CB B MET A 1 455 ? 33.125 62.005 58.463 0.40 34.34 ? 509 MET A CB 1 ATOM 3706 C CG A MET A 1 455 ? 32.694 62.703 60.073 0.60 38.68 ? 509 MET A CG 1 ATOM 3707 C CG B MET A 1 455 ? 33.263 63.297 59.274 0.40 35.00 ? 509 MET A CG 1 ATOM 3708 S SD A MET A 1 455 ? 31.697 64.116 59.680 0.60 41.20 ? 509 MET A SD 1 ATOM 3709 S SD B MET A 1 455 ? 32.527 63.192 60.913 0.40 34.03 ? 509 MET A SD 1 ATOM 3710 C CE A MET A 1 455 ? 31.758 65.055 61.211 0.60 42.16 ? 509 MET A CE 1 ATOM 3711 C CE B MET A 1 455 ? 30.887 62.642 60.470 0.40 33.53 ? 509 MET A CE 1 ATOM 3712 N N . PRO A 1 456 ? 32.824 58.838 57.971 1.00 33.34 ? 510 PRO A N 1 ATOM 3713 C CA . PRO A 1 456 ? 32.628 57.851 56.895 1.00 32.40 ? 510 PRO A CA 1 ATOM 3714 C C . PRO A 1 456 ? 31.819 58.395 55.710 1.00 31.29 ? 510 PRO A C 1 ATOM 3715 O O . PRO A 1 456 ? 31.056 59.363 55.850 1.00 30.75 ? 510 PRO A O 1 ATOM 3716 C CB . PRO A 1 456 ? 31.798 56.757 57.570 1.00 30.73 ? 510 PRO A CB 1 ATOM 3717 C CG . PRO A 1 456 ? 30.954 57.521 58.618 1.00 31.41 ? 510 PRO A CG 1 ATOM 3718 C CD . PRO A 1 456 ? 31.886 58.631 59.098 1.00 32.52 ? 510 PRO A CD 1 ATOM 3719 N N . ARG A 1 457 ? 31.918 57.713 54.570 1.00 30.45 ? 511 ARG A N 1 ATOM 3720 C CA . ARG A 1 457 ? 31.096 58.029 53.414 1.00 30.08 ? 511 ARG A CA 1 ATOM 3721 C C . ARG A 1 457 ? 29.680 57.527 53.705 1.00 29.10 ? 511 ARG A C 1 ATOM 3722 O O . ARG A 1 457 ? 29.504 56.373 54.116 1.00 27.21 ? 511 ARG A O 1 ATOM 3723 C CB . ARG A 1 457 ? 31.656 57.284 52.166 1.00 31.01 ? 511 ARG A CB 1 ATOM 3724 C CG . ARG A 1 457 ? 30.849 57.460 50.861 1.00 31.44 ? 511 ARG A CG 1 ATOM 3725 C CD . ARG A 1 457 ? 31.498 56.603 49.741 1.00 36.17 ? 511 ARG A CD 1 ATOM 3726 N NE . ARG A 1 457 ? 32.802 57.170 49.375 1.00 40.19 ? 511 ARG A NE 1 ATOM 3727 C CZ . ARG A 1 457 ? 32.967 58.134 48.465 1.00 43.60 ? 511 ARG A CZ 1 ATOM 3728 N NH1 . ARG A 1 457 ? 31.907 58.632 47.826 1.00 43.38 ? 511 ARG A NH1 1 ATOM 3729 N NH2 . ARG A 1 457 ? 34.180 58.602 48.192 1.00 43.93 ? 511 ARG A NH2 1 ATOM 3730 N N . ILE A 1 458 ? 28.693 58.401 53.499 1.00 27.97 ? 512 ILE A N 1 ATOM 3731 C CA . ILE A 1 458 ? 27.293 57.970 53.379 1.00 27.59 ? 512 ILE A CA 1 ATOM 3732 C C . ILE A 1 458 ? 26.727 58.457 52.041 1.00 28.53 ? 512 ILE A C 1 ATOM 3733 O O . ILE A 1 458 ? 26.835 59.649 51.720 1.00 29.31 ? 512 ILE A O 1 ATOM 3734 C CB . ILE A 1 458 ? 26.433 58.571 54.551 1.00 27.40 ? 512 ILE A CB 1 ATOM 3735 C CG1 . ILE A 1 458 ? 26.950 58.079 55.910 1.00 26.69 ? 512 ILE A CG1 1 ATOM 3736 C CG2 . ILE A 1 458 ? 24.896 58.270 54.355 1.00 25.18 ? 512 ILE A CG2 1 ATOM 3737 C CD1 . ILE A 1 458 ? 26.240 58.743 57.131 1.00 29.74 ? 512 ILE A CD1 1 ATOM 3738 N N . SER A 1 459 ? 26.101 57.558 51.281 1.00 28.72 ? 513 SER A N 1 ATOM 3739 C CA . SER A 1 459 ? 25.682 57.906 49.951 1.00 28.45 ? 513 SER A CA 1 ATOM 3740 C C . SER A 1 459 ? 24.222 58.350 49.941 1.00 27.89 ? 513 SER A C 1 ATOM 3741 O O . SER A 1 459 ? 23.485 58.180 50.907 1.00 25.82 ? 513 SER A O 1 ATOM 3742 C CB . SER A 1 459 ? 25.911 56.740 48.978 1.00 29.25 ? 513 SER A CB 1 ATOM 3743 O OG . SER A 1 459 ? 27.306 56.504 48.910 1.00 34.12 ? 513 SER A OG 1 ATOM 3744 N N . LYS A 1 460 ? 23.807 58.850 48.788 1.00 28.15 ? 514 LYS A N 1 ATOM 3745 C CA . LYS A 1 460 ? 22.418 59.286 48.575 1.00 28.24 ? 514 LYS A CA 1 ATOM 3746 C C . LYS A 1 460 ? 21.563 58.056 48.281 1.00 27.96 ? 514 LYS A C 1 ATOM 3747 O O . LYS A 1 460 ? 22.044 57.066 47.703 1.00 28.21 ? 514 LYS A O 1 ATOM 3748 C CB . LYS A 1 460 ? 22.367 60.211 47.359 1.00 26.95 ? 514 LYS A CB 1 ATOM 3749 C CG . LYS A 1 460 ? 23.210 61.500 47.562 1.00 29.78 ? 514 LYS A CG 1 ATOM 3750 C CD . LYS A 1 460 ? 23.153 62.348 46.298 1.00 30.13 ? 514 LYS A CD 1 ATOM 3751 C CE . LYS A 1 460 ? 24.282 63.330 46.328 1.00 31.83 ? 514 LYS A CE 1 ATOM 3752 N NZ . LYS A 1 460 ? 24.215 64.207 45.093 1.00 34.81 ? 514 LYS A NZ 1 ATOM 3753 N N . LEU A 1 461 ? 20.284 58.127 48.617 1.00 27.26 ? 515 LEU A N 1 ATOM 3754 C CA . LEU A 1 461 ? 19.335 57.155 48.087 1.00 27.77 ? 515 LEU A CA 1 ATOM 3755 C C . LEU A 1 461 ? 18.914 57.554 46.699 1.00 29.73 ? 515 LEU A C 1 ATOM 3756 O O . LEU A 1 461 ? 18.526 58.709 46.441 1.00 31.78 ? 515 LEU A O 1 ATOM 3757 C CB . LEU A 1 461 ? 18.052 57.122 48.925 1.00 27.02 ? 515 LEU A CB 1 ATOM 3758 C CG . LEU A 1 461 ? 18.205 56.490 50.291 1.00 25.39 ? 515 LEU A CG 1 ATOM 3759 C CD1 . LEU A 1 461 ? 16.960 56.862 51.131 1.00 28.15 ? 515 LEU A CD1 1 ATOM 3760 C CD2 . LEU A 1 461 ? 18.377 54.997 50.134 1.00 21.08 ? 515 LEU A CD2 1 ATOM 3761 N N . GLY A 1 462 ? 18.902 56.575 45.816 1.00 30.45 ? 516 GLY A N 1 ATOM 3762 C CA . GLY A 1 462 ? 18.390 56.803 44.472 1.00 29.93 ? 516 GLY A CA 1 ATOM 3763 C C . GLY A 1 462 ? 17.179 55.933 44.229 1.00 30.21 ? 516 GLY A C 1 ATOM 3764 O O . GLY A 1 462 ? 16.056 56.219 44.707 1.00 29.93 ? 516 GLY A O 1 ATOM 3765 N N . SER A 1 463 ? 17.389 54.870 43.452 1.00 29.55 ? 517 SER A N 1 ATOM 3766 C CA . SER A 1 463 ? 16.298 54.109 42.879 1.00 28.37 ? 517 SER A CA 1 ATOM 3767 C C . SER A 1 463 ? 16.665 52.620 43.002 1.00 27.46 ? 517 SER A C 1 ATOM 3768 O O . SER A 1 463 ? 17.819 52.286 43.285 1.00 26.12 ? 517 SER A O 1 ATOM 3769 C CB . SER A 1 463 ? 16.240 54.475 41.350 1.00 29.72 ? 517 SER A CB 1 ATOM 3770 O OG . SER A 1 463 ? 17.517 54.246 40.701 1.00 34.88 ? 517 SER A OG 1 ATOM 3771 N N . GLY A 1 464 ? 15.730 51.712 42.705 1.00 24.41 ? 518 GLY A N 1 ATOM 3772 C CA . GLY A 1 464 ? 16.138 50.337 42.435 1.00 23.56 ? 518 GLY A CA 1 ATOM 3773 C C . GLY A 1 464 ? 15.929 49.391 43.626 1.00 22.07 ? 518 GLY A C 1 ATOM 3774 O O . GLY A 1 464 ? 16.376 48.260 43.595 1.00 21.99 ? 518 GLY A O 1 ATOM 3775 N N . ASN A 1 465 ? 15.283 49.881 44.682 1.00 20.01 ? 519 ASN A N 1 ATOM 3776 C CA . ASN A 1 465 ? 14.905 48.972 45.771 1.00 19.51 ? 519 ASN A CA 1 ATOM 3777 C C . ASN A 1 465 ? 13.650 49.468 46.494 1.00 18.74 ? 519 ASN A C 1 ATOM 3778 O O . ASN A 1 465 ? 13.130 50.537 46.157 1.00 17.68 ? 519 ASN A O 1 ATOM 3779 C CB . ASN A 1 465 ? 16.114 48.739 46.693 1.00 20.28 ? 519 ASN A CB 1 ATOM 3780 C CG . ASN A 1 465 ? 16.157 47.311 47.225 1.00 20.65 ? 519 ASN A CG 1 ATOM 3781 O OD1 . ASN A 1 465 ? 15.250 46.886 47.956 1.00 20.67 ? 519 ASN A OD1 1 ATOM 3782 N ND2 . ASN A 1 465 ? 17.199 46.557 46.820 1.00 18.32 ? 519 ASN A ND2 1 ATOM 3783 N N . ASP A 1 466 ? 13.190 48.742 47.513 1.00 17.06 ? 520 ASP A N 1 ATOM 3784 C CA . ASP A 1 466 ? 11.821 48.953 47.962 1.00 17.07 ? 520 ASP A CA 1 ATOM 3785 C C . ASP A 1 466 ? 11.605 50.228 48.766 1.00 17.75 ? 520 ASP A C 1 ATOM 3786 O O . ASP A 1 466 ? 10.494 50.566 49.053 1.00 17.65 ? 520 ASP A O 1 ATOM 3787 C CB . ASP A 1 466 ? 11.350 47.759 48.816 1.00 18.27 ? 520 ASP A CB 1 ATOM 3788 C CG . ASP A 1 466 ? 10.989 46.529 47.947 1.00 18.10 ? 520 ASP A CG 1 ATOM 3789 O OD1 . ASP A 1 466 ? 10.242 46.689 46.918 1.00 18.66 ? 520 ASP A OD1 1 ATOM 3790 O OD2 . ASP A 1 466 ? 11.427 45.397 48.328 1.00 18.04 ? 520 ASP A OD2 1 ATOM 3791 N N . PHE A 1 467 ? 12.669 50.942 49.118 1.00 18.46 ? 521 PHE A N 1 ATOM 3792 C CA . PHE A 1 467 ? 12.531 52.246 49.774 1.00 18.95 ? 521 PHE A CA 1 ATOM 3793 C C . PHE A 1 467 ? 11.966 53.264 48.765 1.00 18.47 ? 521 PHE A C 1 ATOM 3794 O O . PHE A 1 467 ? 11.585 54.383 49.150 1.00 18.16 ? 521 PHE A O 1 ATOM 3795 C CB . PHE A 1 467 ? 13.920 52.774 50.263 1.00 19.75 ? 521 PHE A CB 1 ATOM 3796 C CG . PHE A 1 467 ? 14.921 52.957 49.162 1.00 19.13 ? 521 PHE A CG 1 ATOM 3797 C CD1 . PHE A 1 467 ? 14.964 54.135 48.403 1.00 21.46 ? 521 PHE A CD1 1 ATOM 3798 C CD2 . PHE A 1 467 ? 15.815 51.945 48.850 1.00 19.87 ? 521 PHE A CD2 1 ATOM 3799 C CE1 . PHE A 1 467 ? 15.857 54.244 47.352 1.00 21.94 ? 521 PHE A CE1 1 ATOM 3800 C CE2 . PHE A 1 467 ? 16.733 52.067 47.803 1.00 22.22 ? 521 PHE A CE2 1 ATOM 3801 C CZ . PHE A 1 467 ? 16.742 53.217 47.056 1.00 22.63 ? 521 PHE A CZ 1 ATOM 3802 N N . GLU A 1 468 ? 12.011 52.911 47.480 1.00 16.55 ? 522 GLU A N 1 ATOM 3803 C CA . GLU A 1 468 ? 11.820 53.943 46.429 1.00 17.98 ? 522 GLU A CA 1 ATOM 3804 C C . GLU A 1 468 ? 10.468 54.667 46.566 1.00 17.09 ? 522 GLU A C 1 ATOM 3805 O O . GLU A 1 468 ? 10.399 55.908 46.592 1.00 16.79 ? 522 GLU A O 1 ATOM 3806 C CB . GLU A 1 468 ? 11.912 53.302 45.030 1.00 17.69 ? 522 GLU A CB 1 ATOM 3807 C CG . GLU A 1 468 ? 12.121 54.395 43.951 1.00 23.28 ? 522 GLU A CG 1 ATOM 3808 C CD . GLU A 1 468 ? 12.289 53.784 42.528 1.00 28.57 ? 522 GLU A CD 1 ATOM 3809 O OE1 . GLU A 1 468 ? 11.355 54.017 41.793 1.00 27.86 ? 522 GLU A OE1 1 ATOM 3810 O OE2 . GLU A 1 468 ? 13.323 53.099 42.205 1.00 29.08 ? 522 GLU A OE2 1 ATOM 3811 N N . VAL A 1 469 ? 9.376 53.919 46.673 1.00 16.20 ? 523 VAL A N 1 ATOM 3812 C CA . VAL A 1 469 ? 8.071 54.626 46.757 1.00 17.71 ? 523 VAL A CA 1 ATOM 3813 C C . VAL A 1 469 ? 7.968 55.490 48.033 1.00 18.24 ? 523 VAL A C 1 ATOM 3814 O O . VAL A 1 469 ? 7.408 56.576 48.037 1.00 17.41 ? 523 VAL A O 1 ATOM 3815 C CB . VAL A 1 469 ? 6.886 53.632 46.644 1.00 18.09 ? 523 VAL A CB 1 ATOM 3816 C CG1 . VAL A 1 469 ? 6.878 52.581 47.891 1.00 16.84 ? 523 VAL A CG1 1 ATOM 3817 C CG2 . VAL A 1 469 ? 5.559 54.366 46.453 1.00 17.41 ? 523 VAL A CG2 1 ATOM 3818 N N . PHE A 1 470 ? 8.495 54.972 49.150 1.00 17.58 ? 524 PHE A N 1 ATOM 3819 C CA . PHE A 1 470 ? 8.369 55.706 50.395 1.00 16.66 ? 524 PHE A CA 1 ATOM 3820 C C . PHE A 1 470 ? 9.128 57.029 50.353 1.00 16.18 ? 524 PHE A C 1 ATOM 3821 O O . PHE A 1 470 ? 8.644 58.046 50.898 1.00 17.12 ? 524 PHE A O 1 ATOM 3822 C CB . PHE A 1 470 ? 8.911 54.798 51.510 1.00 18.43 ? 524 PHE A CB 1 ATOM 3823 C CG . PHE A 1 470 ? 8.108 53.535 51.623 1.00 18.37 ? 524 PHE A CG 1 ATOM 3824 C CD1 . PHE A 1 470 ? 6.823 53.590 52.195 1.00 22.45 ? 524 PHE A CD1 1 ATOM 3825 C CD2 . PHE A 1 470 ? 8.570 52.349 51.093 1.00 18.38 ? 524 PHE A CD2 1 ATOM 3826 C CE1 . PHE A 1 470 ? 6.033 52.415 52.293 1.00 21.67 ? 524 PHE A CE1 1 ATOM 3827 C CE2 . PHE A 1 470 ? 7.795 51.148 51.193 1.00 17.10 ? 524 PHE A CE2 1 ATOM 3828 C CZ . PHE A 1 470 ? 6.538 51.196 51.786 1.00 22.31 ? 524 PHE A CZ 1 ATOM 3829 N N . PHE A 1 471 ? 10.315 56.988 49.783 1.00 17.43 ? 525 PHE A N 1 ATOM 3830 C CA . PHE A 1 471 ? 11.220 58.164 49.805 1.00 17.40 ? 525 PHE A CA 1 ATOM 3831 C C . PHE A 1 471 ? 10.942 59.089 48.623 1.00 17.64 ? 525 PHE A C 1 ATOM 3832 O O . PHE A 1 471 ? 10.654 60.285 48.820 1.00 18.62 ? 525 PHE A O 1 ATOM 3833 C CB . PHE A 1 471 ? 12.692 57.695 49.732 1.00 16.24 ? 525 PHE A CB 1 ATOM 3834 C CG . PHE A 1 471 ? 13.673 58.802 49.971 1.00 17.78 ? 525 PHE A CG 1 ATOM 3835 C CD1 . PHE A 1 471 ? 13.600 59.549 51.158 1.00 17.34 ? 525 PHE A CD1 1 ATOM 3836 C CD2 . PHE A 1 471 ? 14.660 59.094 49.015 1.00 21.75 ? 525 PHE A CD2 1 ATOM 3837 C CE1 . PHE A 1 471 ? 14.528 60.580 51.426 1.00 20.88 ? 525 PHE A CE1 1 ATOM 3838 C CE2 . PHE A 1 471 ? 15.608 60.141 49.276 1.00 21.63 ? 525 PHE A CE2 1 ATOM 3839 C CZ . PHE A 1 471 ? 15.525 60.863 50.500 1.00 20.27 ? 525 PHE A CZ 1 ATOM 3840 N N . GLN A 1 472 ? 10.968 58.529 47.402 1.00 15.87 ? 526 GLN A N 1 ATOM 3841 C CA . GLN A 1 472 ? 10.880 59.357 46.189 1.00 16.61 ? 526 GLN A CA 1 ATOM 3842 C C . GLN A 1 472 ? 9.424 59.809 45.833 1.00 16.86 ? 526 GLN A C 1 ATOM 3843 O O . GLN A 1 472 ? 9.230 60.904 45.257 1.00 18.49 ? 526 GLN A O 1 ATOM 3844 C CB . GLN A 1 472 ? 11.458 58.548 44.996 1.00 16.62 ? 526 GLN A CB 1 ATOM 3845 C CG . GLN A 1 472 ? 12.937 58.056 45.230 1.00 19.05 ? 526 GLN A CG 1 ATOM 3846 C CD . GLN A 1 472 ? 13.946 59.177 45.233 1.00 21.26 ? 526 GLN A CD 1 ATOM 3847 O OE1 . GLN A 1 472 ? 13.600 60.353 45.185 1.00 23.49 ? 526 GLN A OE1 1 ATOM 3848 N NE2 . GLN A 1 472 ? 15.230 58.803 45.263 1.00 19.99 ? 526 GLN A NE2 1 ATOM 3849 N N . ARG A 1 473 ? 8.418 58.983 46.148 1.00 15.15 ? 527 ARG A N 1 ATOM 3850 C CA . ARG A 1 473 ? 7.045 59.411 45.900 1.00 16.27 ? 527 ARG A CA 1 ATOM 3851 C C . ARG A 1 473 ? 6.410 60.067 47.131 1.00 16.21 ? 527 ARG A C 1 ATOM 3852 O O . ARG A 1 473 ? 5.780 61.151 47.036 1.00 16.16 ? 527 ARG A O 1 ATOM 3853 C CB . ARG A 1 473 ? 6.154 58.205 45.428 1.00 15.90 ? 527 ARG A CB 1 ATOM 3854 C CG . ARG A 1 473 ? 4.811 58.731 44.846 1.00 15.64 ? 527 ARG A CG 1 ATOM 3855 C CD . ARG A 1 473 ? 3.771 57.586 44.679 1.00 17.02 ? 527 ARG A CD 1 ATOM 3856 N NE . ARG A 1 473 ? 4.229 56.565 43.696 1.00 16.81 ? 527 ARG A NE 1 ATOM 3857 C CZ . ARG A 1 473 ? 3.350 55.715 43.109 1.00 17.69 ? 527 ARG A CZ 1 ATOM 3858 N NH1 . ARG A 1 473 ? 2.057 55.841 43.398 1.00 17.25 ? 527 ARG A NH1 1 ATOM 3859 N NH2 . ARG A 1 473 ? 3.745 54.807 42.209 1.00 17.60 ? 527 ARG A NH2 1 ATOM 3860 N N . LEU A 1 474 ? 6.537 59.417 48.307 1.00 16.03 ? 528 LEU A N 1 ATOM 3861 C CA . LEU A 1 474 ? 5.816 59.917 49.468 1.00 16.09 ? 528 LEU A CA 1 ATOM 3862 C C . LEU A 1 474 ? 6.632 60.861 50.388 1.00 16.52 ? 528 LEU A C 1 ATOM 3863 O O . LEU A 1 474 ? 6.028 61.552 51.177 1.00 18.34 ? 528 LEU A O 1 ATOM 3864 C CB . LEU A 1 474 ? 5.236 58.763 50.321 1.00 16.92 ? 528 LEU A CB 1 ATOM 3865 C CG . LEU A 1 474 ? 4.362 57.752 49.526 1.00 17.82 ? 528 LEU A CG 1 ATOM 3866 C CD1 . LEU A 1 474 ? 3.877 56.619 50.436 1.00 17.46 ? 528 LEU A CD1 1 ATOM 3867 C CD2 . LEU A 1 474 ? 3.099 58.553 49.006 1.00 20.55 ? 528 LEU A CD2 1 ATOM 3868 N N . GLY A 1 475 ? 7.953 60.877 50.301 1.00 15.31 ? 529 GLY A N 1 ATOM 3869 C CA . GLY A 1 475 ? 8.741 61.843 51.116 1.00 16.36 ? 529 GLY A CA 1 ATOM 3870 C C . GLY A 1 475 ? 8.793 61.428 52.575 1.00 15.28 ? 529 GLY A C 1 ATOM 3871 O O . GLY A 1 475 ? 8.798 62.281 53.454 1.00 16.17 ? 529 GLY A O 1 ATOM 3872 N N . ILE A 1 476 ? 8.938 60.131 52.796 1.00 16.16 ? 530 ILE A N 1 ATOM 3873 C CA . ILE A 1 476 ? 9.202 59.593 54.152 1.00 15.24 ? 530 ILE A CA 1 ATOM 3874 C C . ILE A 1 476 ? 10.711 59.347 54.301 1.00 16.18 ? 530 ILE A C 1 ATOM 3875 O O . ILE A 1 476 ? 11.335 58.741 53.434 1.00 16.22 ? 530 ILE A O 1 ATOM 3876 C CB . ILE A 1 476 ? 8.427 58.263 54.364 1.00 15.78 ? 530 ILE A CB 1 ATOM 3877 C CG1 . ILE A 1 476 ? 6.903 58.552 54.318 1.00 18.49 ? 530 ILE A CG1 1 ATOM 3878 C CG2 . ILE A 1 476 ? 8.813 57.571 55.730 1.00 17.99 ? 530 ILE A CG2 1 ATOM 3879 C CD1 . ILE A 1 476 ? 6.123 57.248 54.077 1.00 19.36 ? 530 ILE A CD1 1 ATOM 3880 N N . ALA A 1 477 ? 11.296 59.929 55.342 1.00 15.95 ? 531 ALA A N 1 ATOM 3881 C CA . ALA A 1 477 ? 12.745 59.779 55.634 1.00 16.95 ? 531 ALA A CA 1 ATOM 3882 C C . ALA A 1 477 ? 13.155 58.315 55.537 1.00 17.74 ? 531 ALA A C 1 ATOM 3883 O O . ALA A 1 477 ? 12.530 57.465 56.206 1.00 19.16 ? 531 ALA A O 1 ATOM 3884 C CB . ALA A 1 477 ? 12.992 60.289 57.099 1.00 17.75 ? 531 ALA A CB 1 ATOM 3885 N N . SER A 1 478 ? 14.178 57.978 54.731 1.00 16.73 ? 532 SER A N 1 ATOM 3886 C CA . SER A 1 478 ? 14.473 56.582 54.454 1.00 16.89 ? 532 SER A CA 1 ATOM 3887 C C . SER A 1 478 ? 15.981 56.344 54.592 1.00 18.73 ? 532 SER A C 1 ATOM 3888 O O . SER A 1 478 ? 16.786 57.281 54.409 1.00 19.00 ? 532 SER A O 1 ATOM 3889 C CB . SER A 1 478 ? 13.970 56.159 53.035 1.00 17.65 ? 532 SER A CB 1 ATOM 3890 O OG . SER A 1 478 ? 12.527 56.170 53.018 1.00 18.76 ? 532 SER A OG 1 ATOM 3891 N N . GLY A 1 479 ? 16.358 55.083 54.837 1.00 18.71 ? 533 GLY A N 1 ATOM 3892 C CA . GLY A 1 479 ? 17.799 54.718 54.935 1.00 18.61 ? 533 GLY A CA 1 ATOM 3893 C C . GLY A 1 479 ? 17.981 53.222 54.650 1.00 19.76 ? 533 GLY A C 1 ATOM 3894 O O . GLY A 1 479 ? 17.014 52.419 54.688 1.00 18.54 ? 533 GLY A O 1 ATOM 3895 N N . ARG A 1 480 ? 19.235 52.840 54.411 1.00 19.06 ? 534 ARG A N 1 ATOM 3896 C CA . ARG A 1 480 ? 19.542 51.437 54.212 1.00 20.52 ? 534 ARG A CA 1 ATOM 3897 C C . ARG A 1 480 ? 20.998 51.267 54.598 1.00 20.34 ? 534 ARG A C 1 ATOM 3898 O O . ARG A 1 480 ? 21.758 52.239 54.562 1.00 21.01 ? 534 ARG A O 1 ATOM 3899 C CB . ARG A 1 480 ? 19.354 51.029 52.742 1.00 20.37 ? 534 ARG A CB 1 ATOM 3900 C CG . ARG A 1 480 ? 20.277 51.734 51.740 1.00 23.21 ? 534 ARG A CG 1 ATOM 3901 C CD . ARG A 1 480 ? 19.765 51.485 50.257 1.00 23.24 ? 534 ARG A CD 1 ATOM 3902 N NE . ARG A 1 480 ? 19.732 50.036 49.917 1.00 23.29 ? 534 ARG A NE 1 ATOM 3903 C CZ . ARG A 1 480 ? 19.847 49.524 48.678 1.00 24.52 ? 534 ARG A CZ 1 ATOM 3904 N NH1 . ARG A 1 480 ? 20.005 50.302 47.616 1.00 24.51 ? 534 ARG A NH1 1 ATOM 3905 N NH2 . ARG A 1 480 ? 19.775 48.212 48.502 1.00 21.62 ? 534 ARG A NH2 1 ATOM 3906 N N . ALA A 1 481 ? 21.339 50.051 54.999 1.00 20.83 ? 535 ALA A N 1 ATOM 3907 C CA . ALA A 1 481 ? 22.728 49.721 55.410 1.00 20.47 ? 535 ALA A CA 1 ATOM 3908 C C . ALA A 1 481 ? 22.983 48.276 55.084 1.00 21.90 ? 535 ALA A C 1 ATOM 3909 O O . ALA A 1 481 ? 22.094 47.421 55.272 1.00 21.53 ? 535 ALA A O 1 ATOM 3910 C CB . ALA A 1 481 ? 22.916 49.936 56.920 1.00 20.50 ? 535 ALA A CB 1 ATOM 3911 N N A ARG A 1 482 ? 24.209 47.972 54.652 0.70 21.12 ? 536 ARG A N 1 ATOM 3912 N N B ARG A 1 482 ? 24.198 48.018 54.567 0.30 21.63 ? 536 ARG A N 1 ATOM 3913 C CA A ARG A 1 482 ? 24.554 46.597 54.396 0.70 22.72 ? 536 ARG A CA 1 ATOM 3914 C CA B ARG A 1 482 ? 24.591 46.721 54.004 0.30 22.41 ? 536 ARG A CA 1 ATOM 3915 C C A ARG A 1 482 ? 26.068 46.535 54.423 0.70 21.83 ? 536 ARG A C 1 ATOM 3916 C C B ARG A 1 482 ? 26.116 46.530 54.039 0.30 22.39 ? 536 ARG A C 1 ATOM 3917 O O A ARG A 1 482 ? 26.728 47.577 54.464 0.70 21.59 ? 536 ARG A O 1 ATOM 3918 O O B ARG A 1 482 ? 26.869 47.476 53.770 0.30 21.75 ? 536 ARG A O 1 ATOM 3919 C CB A ARG A 1 482 ? 23.978 46.048 53.049 0.70 22.77 ? 536 ARG A CB 1 ATOM 3920 C CB B ARG A 1 482 ? 24.046 46.534 52.561 0.30 22.22 ? 536 ARG A CB 1 ATOM 3921 C CG A ARG A 1 482 ? 24.254 46.816 51.744 0.70 25.79 ? 536 ARG A CG 1 ATOM 3922 C CG B ARG A 1 482 ? 24.514 47.535 51.453 0.30 24.27 ? 536 ARG A CG 1 ATOM 3923 C CD A ARG A 1 482 ? 23.476 48.161 51.684 0.70 26.55 ? 536 ARG A CD 1 ATOM 3924 C CD B ARG A 1 482 ? 23.266 48.066 50.658 0.30 23.38 ? 536 ARG A CD 1 ATOM 3925 N NE A ARG A 1 482 ? 23.478 48.809 50.356 0.70 25.21 ? 536 ARG A NE 1 ATOM 3926 N NE B ARG A 1 482 ? 23.489 48.637 49.308 0.30 20.67 ? 536 ARG A NE 1 ATOM 3927 C CZ A ARG A 1 482 ? 23.586 50.112 50.129 0.70 23.33 ? 536 ARG A CZ 1 ATOM 3928 C CZ B ARG A 1 482 ? 23.377 47.921 48.183 0.30 18.25 ? 536 ARG A CZ 1 ATOM 3929 N NH1 A ARG A 1 482 ? 23.757 51.016 51.153 0.70 21.66 ? 536 ARG A NH1 1 ATOM 3930 N NH1 B ARG A 1 482 ? 23.070 46.658 48.268 0.30 15.26 ? 536 ARG A NH1 1 ATOM 3931 N NH2 A ARG A 1 482 ? 23.509 50.511 48.867 0.70 22.08 ? 536 ARG A NH2 1 ATOM 3932 N NH2 B ARG A 1 482 ? 23.554 48.462 46.974 0.30 19.03 ? 536 ARG A NH2 1 ATOM 3933 N N . TYR A 1 483 ? 26.589 45.326 54.353 1.00 22.77 ? 537 TYR A N 1 ATOM 3934 C CA . TYR A 1 483 ? 28.050 45.121 54.201 1.00 24.64 ? 537 TYR A CA 1 ATOM 3935 C C . TYR A 1 483 ? 28.375 44.979 52.718 1.00 25.45 ? 537 TYR A C 1 ATOM 3936 O O . TYR A 1 483 ? 27.623 44.376 51.950 1.00 26.48 ? 537 TYR A O 1 ATOM 3937 C CB . TYR A 1 483 ? 28.620 43.928 55.037 1.00 24.08 ? 537 TYR A CB 1 ATOM 3938 C CG . TYR A 1 483 ? 29.539 44.423 56.145 1.00 24.27 ? 537 TYR A CG 1 ATOM 3939 C CD1 . TYR A 1 483 ? 29.027 45.153 57.221 1.00 25.95 ? 537 TYR A CD1 1 ATOM 3940 C CD2 . TYR A 1 483 ? 30.941 44.164 56.109 1.00 26.46 ? 537 TYR A CD2 1 ATOM 3941 C CE1 . TYR A 1 483 ? 29.852 45.639 58.242 1.00 25.62 ? 537 TYR A CE1 1 ATOM 3942 C CE2 . TYR A 1 483 ? 31.760 44.639 57.112 1.00 25.76 ? 537 TYR A CE2 1 ATOM 3943 C CZ . TYR A 1 483 ? 31.209 45.348 58.183 1.00 27.13 ? 537 TYR A CZ 1 ATOM 3944 O OH . TYR A 1 483 ? 32.013 45.832 59.180 1.00 29.53 ? 537 TYR A OH 1 ATOM 3945 N N . THR A 1 484 ? 29.514 45.531 52.315 1.00 26.93 ? 538 THR A N 1 ATOM 3946 C CA . THR A 1 484 ? 29.819 45.590 50.891 1.00 27.87 ? 538 THR A CA 1 ATOM 3947 C C . THR A 1 484 ? 31.304 45.231 50.668 1.00 29.61 ? 538 THR A C 1 ATOM 3948 O O . THR A 1 484 ? 32.050 45.060 51.621 1.00 27.95 ? 538 THR A O 1 ATOM 3949 C CB . THR A 1 484 ? 29.561 46.998 50.331 1.00 27.62 ? 538 THR A CB 1 ATOM 3950 O OG1 . THR A 1 484 ? 29.636 46.935 48.910 1.00 29.73 ? 538 THR A OG1 1 ATOM 3951 C CG2 . THR A 1 484 ? 30.565 48.011 50.855 1.00 28.37 ? 538 THR A CG2 1 ATOM 3952 N N . LYS A 1 485 ? 31.693 45.152 49.398 1.00 32.37 ? 539 LYS A N 1 ATOM 3953 C CA . LYS A 1 485 ? 33.079 44.845 48.996 1.00 37.17 ? 539 LYS A CA 1 ATOM 3954 C C . LYS A 1 485 ? 33.987 46.079 49.009 1.00 39.81 ? 539 LYS A C 1 ATOM 3955 O O . LYS A 1 485 ? 33.533 47.183 49.269 1.00 39.29 ? 539 LYS A O 1 ATOM 3956 C CB . LYS A 1 485 ? 33.057 44.197 47.595 1.00 36.65 ? 539 LYS A CB 1 ATOM 3957 C CG . LYS A 1 485 ? 32.859 45.202 46.461 1.00 39.96 ? 539 LYS A CG 1 ATOM 3958 C CD . LYS A 1 485 ? 32.424 44.513 45.175 1.00 46.25 ? 539 LYS A CD 1 ATOM 3959 C CE . LYS A 1 485 ? 32.369 45.536 44.038 1.00 49.16 ? 539 LYS A CE 1 ATOM 3960 N NZ . LYS A 1 485 ? 31.919 44.927 42.754 1.00 50.81 ? 539 LYS A NZ 1 ATOM 3961 N N . ASN A 1 486 ? 35.283 45.880 48.761 1.00 44.50 ? 540 ASN A N 1 ATOM 3962 C CA . ASN A 1 486 ? 36.198 46.989 48.496 1.00 49.47 ? 540 ASN A CA 1 ATOM 3963 C C . ASN A 1 486 ? 35.946 47.457 47.061 1.00 52.25 ? 540 ASN A C 1 ATOM 3964 O O . ASN A 1 486 ? 36.207 46.698 46.107 1.00 53.33 ? 540 ASN A O 1 ATOM 3965 C CB . ASN A 1 486 ? 37.654 46.510 48.646 1.00 49.97 ? 540 ASN A CB 1 ATOM 3966 C CG . ASN A 1 486 ? 38.664 47.656 48.713 1.00 52.55 ? 540 ASN A CG 1 ATOM 3967 O OD1 . ASN A 1 486 ? 38.355 48.835 48.449 1.00 55.48 ? 540 ASN A OD1 1 ATOM 3968 N ND2 . ASN A 1 486 ? 39.891 47.307 49.098 1.00 55.25 ? 540 ASN A ND2 1 ATOM 3969 N N . TRP A 1 487 ? 35.418 48.673 46.924 1.00 54.99 ? 541 TRP A N 1 ATOM 3970 C CA . TRP A 1 487 ? 35.054 49.285 45.636 1.00 58.71 ? 541 TRP A CA 1 ATOM 3971 C C . TRP A 1 487 ? 36.235 49.801 44.788 1.00 61.79 ? 541 TRP A C 1 ATOM 3972 O O . TRP A 1 487 ? 36.099 50.776 44.020 1.00 62.52 ? 541 TRP A O 1 ATOM 3973 C CB . TRP A 1 487 ? 34.024 50.399 45.865 1.00 58.41 ? 541 TRP A CB 1 ATOM 3974 C CG . TRP A 1 487 ? 32.667 49.820 46.061 1.00 60.05 ? 541 TRP A CG 1 ATOM 3975 C CD1 . TRP A 1 487 ? 32.023 49.600 47.251 1.00 60.86 ? 541 TRP A CD1 1 ATOM 3976 C CD2 . TRP A 1 487 ? 31.800 49.309 45.033 1.00 61.24 ? 541 TRP A CD2 1 ATOM 3977 N NE1 . TRP A 1 487 ? 30.802 48.999 47.026 1.00 59.75 ? 541 TRP A NE1 1 ATOM 3978 C CE2 . TRP A 1 487 ? 30.633 48.817 45.677 1.00 60.51 ? 541 TRP A CE2 1 ATOM 3979 C CE3 . TRP A 1 487 ? 31.892 49.225 43.631 1.00 61.58 ? 541 TRP A CE3 1 ATOM 3980 C CZ2 . TRP A 1 487 ? 29.561 48.253 44.967 1.00 60.71 ? 541 TRP A CZ2 1 ATOM 3981 C CZ3 . TRP A 1 487 ? 30.817 48.653 42.919 1.00 62.62 ? 541 TRP A CZ3 1 ATOM 3982 C CH2 . TRP A 1 487 ? 29.673 48.173 43.595 1.00 62.59 ? 541 TRP A CH2 1 ATOM 3983 N N . GLU A 1 488 ? 37.388 49.153 44.939 1.00 64.48 ? 542 GLU A N 1 ATOM 3984 C CA . GLU A 1 488 ? 38.566 49.462 44.130 1.00 67.42 ? 542 GLU A CA 1 ATOM 3985 C C . GLU A 1 488 ? 39.394 48.197 43.918 1.00 68.51 ? 542 GLU A C 1 ATOM 3986 O O . GLU A 1 488 ? 40.608 48.195 44.124 1.00 69.55 ? 542 GLU A O 1 ATOM 3987 C CB . GLU A 1 488 ? 39.388 50.594 44.762 1.00 68.05 ? 542 GLU A CB 1 ATOM 3988 C CG . GLU A 1 488 ? 39.878 50.334 46.173 1.00 69.85 ? 542 GLU A CG 1 ATOM 3989 C CD . GLU A 1 488 ? 40.745 51.463 46.687 1.00 73.82 ? 542 GLU A CD 1 ATOM 3990 O OE1 . GLU A 1 488 ? 41.986 51.304 46.679 1.00 75.64 ? 542 GLU A OE1 1 ATOM 3991 O OE2 . GLU A 1 488 ? 40.189 52.517 47.085 1.00 75.26 ? 542 GLU A OE2 1 ATOM 3992 N N . THR A 1 489 ? 38.703 47.131 43.508 1.00 69.32 ? 543 THR A N 1 ATOM 3993 C CA . THR A 1 489 ? 39.289 45.818 43.244 1.00 70.28 ? 543 THR A CA 1 ATOM 3994 C C . THR A 1 489 ? 38.540 45.163 42.077 1.00 70.08 ? 543 THR A C 1 ATOM 3995 O O . THR A 1 489 ? 39.147 44.533 41.202 1.00 70.10 ? 543 THR A O 1 ATOM 3996 C CB . THR A 1 489 ? 39.219 44.901 44.504 1.00 70.55 ? 543 THR A CB 1 ATOM 3997 O OG1 . THR A 1 489 ? 39.879 45.543 45.609 1.00 71.79 ? 543 THR A OG1 1 ATOM 3998 C CG2 . THR A 1 489 ? 39.870 43.525 44.241 1.00 71.08 ? 543 THR A CG2 1 ATOM 3999 N N . GLY A 1 494 ? 28.206 45.503 41.244 1.00 38.68 ? 548 GLY A N 1 ATOM 4000 C CA . GLY A 1 494 ? 27.651 44.577 42.224 1.00 35.83 ? 548 GLY A CA 1 ATOM 4001 C C . GLY A 1 494 ? 28.638 43.489 42.596 1.00 34.92 ? 548 GLY A C 1 ATOM 4002 O O . GLY A 1 494 ? 29.803 43.782 42.888 1.00 36.99 ? 548 GLY A O 1 ATOM 4003 N N . TYR A 1 495 ? 28.200 42.224 42.543 1.00 31.26 ? 549 TYR A N 1 ATOM 4004 C CA . TYR A 1 495 ? 29.058 41.090 42.957 1.00 28.80 ? 549 TYR A CA 1 ATOM 4005 C C . TYR A 1 495 ? 28.943 40.002 41.919 1.00 26.78 ? 549 TYR A C 1 ATOM 4006 O O . TYR A 1 495 ? 27.954 39.976 41.169 1.00 27.67 ? 549 TYR A O 1 ATOM 4007 C CB . TYR A 1 495 ? 28.687 40.604 44.367 1.00 27.56 ? 549 TYR A CB 1 ATOM 4008 C CG . TYR A 1 495 ? 27.190 40.287 44.561 1.00 28.00 ? 549 TYR A CG 1 ATOM 4009 C CD1 . TYR A 1 495 ? 26.718 38.971 44.455 1.00 23.29 ? 549 TYR A CD1 1 ATOM 4010 C CD2 . TYR A 1 495 ? 26.262 41.321 44.866 1.00 26.82 ? 549 TYR A CD2 1 ATOM 4011 C CE1 . TYR A 1 495 ? 25.306 38.671 44.637 1.00 25.53 ? 549 TYR A CE1 1 ATOM 4012 C CE2 . TYR A 1 495 ? 24.885 41.039 45.048 1.00 25.35 ? 549 TYR A CE2 1 ATOM 4013 C CZ . TYR A 1 495 ? 24.431 39.714 44.942 1.00 21.42 ? 549 TYR A CZ 1 ATOM 4014 O OH . TYR A 1 495 ? 23.081 39.464 45.078 1.00 22.16 ? 549 TYR A OH 1 ATOM 4015 N N . PRO A 1 496 ? 29.942 39.101 41.843 1.00 25.95 ? 550 PRO A N 1 ATOM 4016 C CA . PRO A 1 496 ? 29.962 38.222 40.672 1.00 26.00 ? 550 PRO A CA 1 ATOM 4017 C C . PRO A 1 496 ? 28.705 37.386 40.441 1.00 23.88 ? 550 PRO A C 1 ATOM 4018 O O . PRO A 1 496 ? 28.294 37.215 39.300 1.00 24.56 ? 550 PRO A O 1 ATOM 4019 C CB . PRO A 1 496 ? 31.186 37.325 40.938 1.00 26.71 ? 550 PRO A CB 1 ATOM 4020 C CG . PRO A 1 496 ? 32.172 38.284 41.595 1.00 25.64 ? 550 PRO A CG 1 ATOM 4021 C CD . PRO A 1 496 ? 31.224 39.050 42.587 1.00 26.76 ? 550 PRO A CD 1 ATOM 4022 N N . LEU A 1 497 ? 28.104 36.854 41.493 1.00 22.65 ? 551 LEU A N 1 ATOM 4023 C CA . LEU A 1 497 ? 27.042 35.847 41.253 1.00 22.20 ? 551 LEU A CA 1 ATOM 4024 C C . LEU A 1 497 ? 25.628 36.448 41.331 1.00 23.02 ? 551 LEU A C 1 ATOM 4025 O O . LEU A 1 497 ? 24.652 35.711 41.426 1.00 23.81 ? 551 LEU A O 1 ATOM 4026 C CB . LEU A 1 497 ? 27.142 34.737 42.259 1.00 21.42 ? 551 LEU A CB 1 ATOM 4027 C CG . LEU A 1 497 ? 28.439 33.950 41.973 1.00 23.38 ? 551 LEU A CG 1 ATOM 4028 C CD1 . LEU A 1 497 ? 28.651 32.924 43.120 1.00 25.07 ? 551 LEU A CD1 1 ATOM 4029 C CD2 . LEU A 1 497 ? 28.372 33.243 40.578 1.00 22.46 ? 551 LEU A CD2 1 ATOM 4030 N N . TYR A 1 498 ? 25.577 37.771 41.295 1.00 22.35 ? 552 TYR A N 1 ATOM 4031 C CA . TYR A 1 498 ? 24.298 38.521 41.379 1.00 22.43 ? 552 TYR A CA 1 ATOM 4032 C C . TYR A 1 498 ? 23.235 37.973 40.433 1.00 21.33 ? 552 TYR A C 1 ATOM 4033 O O . TYR A 1 498 ? 23.463 37.943 39.207 1.00 23.48 ? 552 TYR A O 1 ATOM 4034 C CB . TYR A 1 498 ? 24.638 39.978 41.079 1.00 22.20 ? 552 TYR A CB 1 ATOM 4035 C CG . TYR A 1 498 ? 23.478 40.942 40.961 1.00 22.58 ? 552 TYR A CG 1 ATOM 4036 C CD1 . TYR A 1 498 ? 22.581 41.103 42.019 1.00 20.94 ? 552 TYR A CD1 1 ATOM 4037 C CD2 . TYR A 1 498 ? 23.287 41.678 39.788 1.00 23.24 ? 552 TYR A CD2 1 ATOM 4038 C CE1 . TYR A 1 498 ? 21.493 42.016 41.927 1.00 21.23 ? 552 TYR A CE1 1 ATOM 4039 C CE2 . TYR A 1 498 ? 22.183 42.611 39.680 1.00 21.20 ? 552 TYR A CE2 1 ATOM 4040 C CZ . TYR A 1 498 ? 21.329 42.757 40.743 1.00 21.95 ? 552 TYR A CZ 1 ATOM 4041 O OH . TYR A 1 498 ? 20.286 43.650 40.608 1.00 21.54 ? 552 TYR A OH 1 ATOM 4042 N N . HIS A 1 499 ? 22.069 37.558 40.979 1.00 21.17 ? 553 HIS A N 1 ATOM 4043 C CA . HIS A 1 499 ? 20.905 37.098 40.189 1.00 21.18 ? 553 HIS A CA 1 ATOM 4044 C C . HIS A 1 499 ? 21.151 35.836 39.335 1.00 22.48 ? 553 HIS A C 1 ATOM 4045 O O . HIS A 1 499 ? 20.415 35.548 38.371 1.00 21.49 ? 553 HIS A O 1 ATOM 4046 C CB . HIS A 1 499 ? 20.381 38.190 39.244 1.00 22.14 ? 553 HIS A CB 1 ATOM 4047 C CG . HIS A 1 499 ? 19.622 39.285 39.948 1.00 21.61 ? 553 HIS A CG 1 ATOM 4048 N ND1 . HIS A 1 499 ? 19.068 40.348 39.266 1.00 21.11 ? 553 HIS A ND1 1 ATOM 4049 C CD2 . HIS A 1 499 ? 19.354 39.492 41.258 1.00 22.94 ? 553 HIS A CD2 1 ATOM 4050 C CE1 . HIS A 1 499 ? 18.422 41.125 40.115 1.00 19.32 ? 553 HIS A CE1 1 ATOM 4051 N NE2 . HIS A 1 499 ? 18.580 40.622 41.327 1.00 20.81 ? 553 HIS A NE2 1 ATOM 4052 N N . SER A 1 500 ? 22.159 35.089 39.737 1.00 24.27 ? 554 SER A N 1 ATOM 4053 C CA . SER A 1 500 ? 22.466 33.798 39.118 1.00 21.88 ? 554 SER A CA 1 ATOM 4054 C C . SER A 1 500 ? 21.970 32.636 40.041 1.00 25.92 ? 554 SER A C 1 ATOM 4055 O O . SER A 1 500 ? 21.754 32.834 41.222 1.00 24.07 ? 554 SER A O 1 ATOM 4056 C CB . SER A 1 500 ? 23.992 33.653 38.899 1.00 22.93 ? 554 SER A CB 1 ATOM 4057 O OG A SER A 1 500 ? 24.668 33.440 40.117 0.50 21.36 ? 554 SER A OG 1 ATOM 4058 O OG B SER A 1 500 ? 24.352 32.252 38.857 0.50 22.42 ? 554 SER A OG 1 ATOM 4059 N N . VAL A 1 501 ? 21.851 31.431 39.457 1.00 23.13 ? 555 VAL A N 1 ATOM 4060 C CA . VAL A 1 501 ? 21.455 30.239 40.218 1.00 24.62 ? 555 VAL A CA 1 ATOM 4061 C C . VAL A 1 501 ? 22.485 29.915 41.332 1.00 24.74 ? 555 VAL A C 1 ATOM 4062 O O . VAL A 1 501 ? 22.153 29.214 42.281 1.00 25.62 ? 555 VAL A O 1 ATOM 4063 C CB . VAL A 1 501 ? 21.341 29.004 39.238 1.00 24.38 ? 555 VAL A CB 1 ATOM 4064 C CG1 . VAL A 1 501 ? 22.771 28.563 38.783 1.00 26.13 ? 555 VAL A CG1 1 ATOM 4065 C CG2 . VAL A 1 501 ? 20.593 27.793 39.900 1.00 23.76 ? 555 VAL A CG2 1 ATOM 4066 N N . TYR A 1 502 ? 23.721 30.429 41.241 1.00 24.77 ? 556 TYR A N 1 ATOM 4067 C CA . TYR A 1 502 ? 24.784 30.107 42.190 1.00 24.73 ? 556 TYR A CA 1 ATOM 4068 C C . TYR A 1 502 ? 24.691 30.929 43.476 1.00 25.84 ? 556 TYR A C 1 ATOM 4069 O O . TYR A 1 502 ? 25.489 30.735 44.384 1.00 25.13 ? 556 TYR A O 1 ATOM 4070 C CB . TYR A 1 502 ? 26.201 30.258 41.549 1.00 24.49 ? 556 TYR A CB 1 ATOM 4071 C CG . TYR A 1 502 ? 26.283 29.459 40.279 1.00 24.66 ? 556 TYR A CG 1 ATOM 4072 C CD1 . TYR A 1 502 ? 26.126 28.058 40.319 1.00 25.19 ? 556 TYR A CD1 1 ATOM 4073 C CD2 . TYR A 1 502 ? 26.444 30.073 39.048 1.00 24.42 ? 556 TYR A CD2 1 ATOM 4074 C CE1 . TYR A 1 502 ? 26.141 27.279 39.140 1.00 23.56 ? 556 TYR A CE1 1 ATOM 4075 C CE2 . TYR A 1 502 ? 26.473 29.299 37.861 1.00 27.24 ? 556 TYR A CE2 1 ATOM 4076 C CZ . TYR A 1 502 ? 26.328 27.917 37.928 1.00 24.97 ? 556 TYR A CZ 1 ATOM 4077 O OH . TYR A 1 502 ? 26.332 27.193 36.741 1.00 27.64 ? 556 TYR A OH 1 ATOM 4078 N N . GLU A 1 503 ? 23.714 31.844 43.549 1.00 24.85 ? 557 GLU A N 1 ATOM 4079 C CA . GLU A 1 503 ? 23.441 32.539 44.825 1.00 25.74 ? 557 GLU A CA 1 ATOM 4080 C C . GLU A 1 503 ? 22.736 31.637 45.802 1.00 24.50 ? 557 GLU A C 1 ATOM 4081 O O . GLU A 1 503 ? 21.499 31.549 45.791 1.00 25.63 ? 557 GLU A O 1 ATOM 4082 C CB . GLU A 1 503 ? 22.507 33.750 44.592 1.00 25.58 ? 557 GLU A CB 1 ATOM 4083 C CG . GLU A 1 503 ? 23.232 35.003 44.497 1.00 31.28 ? 557 GLU A CG 1 ATOM 4084 C CD . GLU A 1 503 ? 22.283 36.178 44.804 1.00 28.05 ? 557 GLU A CD 1 ATOM 4085 O OE1 . GLU A 1 503 ? 22.333 37.131 44.047 1.00 30.01 ? 557 GLU A OE1 1 ATOM 4086 O OE2 . GLU A 1 503 ? 21.445 36.045 45.715 1.00 29.56 ? 557 GLU A OE2 1 ATOM 4087 N N . THR A 1 504 ? 23.513 30.936 46.641 1.00 24.37 ? 558 THR A N 1 ATOM 4088 C CA . THR A 1 504 ? 22.978 29.855 47.460 1.00 23.12 ? 558 THR A CA 1 ATOM 4089 C C . THR A 1 504 ? 23.365 30.051 48.910 1.00 22.62 ? 558 THR A C 1 ATOM 4090 O O . THR A 1 504 ? 24.250 30.871 49.237 1.00 23.59 ? 558 THR A O 1 ATOM 4091 C CB . THR A 1 504 ? 23.577 28.479 47.017 1.00 24.13 ? 558 THR A CB 1 ATOM 4092 O OG1 . THR A 1 504 ? 25.006 28.556 47.126 1.00 26.12 ? 558 THR A OG1 1 ATOM 4093 C CG2 . THR A 1 504 ? 23.176 28.097 45.602 1.00 26.02 ? 558 THR A CG2 1 ATOM 4094 N N . TYR A 1 505 ? 22.723 29.286 49.799 1.00 22.35 ? 559 TYR A N 1 ATOM 4095 C CA . TYR A 1 505 ? 23.183 29.240 51.178 1.00 23.18 ? 559 TYR A CA 1 ATOM 4096 C C . TYR A 1 505 ? 24.707 28.941 51.228 1.00 24.02 ? 559 TYR A C 1 ATOM 4097 O O . TYR A 1 505 ? 25.447 29.553 52.013 1.00 23.58 ? 559 TYR A O 1 ATOM 4098 C CB . TYR A 1 505 ? 22.420 28.173 51.940 1.00 22.84 ? 559 TYR A CB 1 ATOM 4099 C CG . TYR A 1 505 ? 22.933 27.943 53.323 1.00 24.96 ? 559 TYR A CG 1 ATOM 4100 C CD1 . TYR A 1 505 ? 22.608 28.821 54.349 1.00 26.30 ? 559 TYR A CD1 1 ATOM 4101 C CD2 . TYR A 1 505 ? 23.803 26.847 53.606 1.00 27.92 ? 559 TYR A CD2 1 ATOM 4102 C CE1 . TYR A 1 505 ? 23.066 28.613 55.629 1.00 28.71 ? 559 TYR A CE1 1 ATOM 4103 C CE2 . TYR A 1 505 ? 24.279 26.643 54.897 1.00 29.87 ? 559 TYR A CE2 1 ATOM 4104 C CZ . TYR A 1 505 ? 23.919 27.523 55.897 1.00 30.98 ? 559 TYR A CZ 1 ATOM 4105 O OH . TYR A 1 505 ? 24.370 27.339 57.204 1.00 30.15 ? 559 TYR A OH 1 ATOM 4106 N N . GLU A 1 506 ? 25.168 28.018 50.386 1.00 23.82 ? 560 GLU A N 1 ATOM 4107 C CA . GLU A 1 506 ? 26.596 27.588 50.487 1.00 25.81 ? 560 GLU A CA 1 ATOM 4108 C C . GLU A 1 506 ? 27.555 28.710 50.122 1.00 25.52 ? 560 GLU A C 1 ATOM 4109 O O . GLU A 1 506 ? 28.653 28.866 50.724 1.00 27.09 ? 560 GLU A O 1 ATOM 4110 C CB . GLU A 1 506 ? 26.855 26.355 49.590 1.00 27.34 ? 560 GLU A CB 1 ATOM 4111 C CG . GLU A 1 506 ? 26.176 25.050 50.068 1.00 29.14 ? 560 GLU A CG 1 ATOM 4112 C CD . GLU A 1 506 ? 24.658 25.044 49.925 1.00 31.34 ? 560 GLU A CD 1 ATOM 4113 O OE1 . GLU A 1 506 ? 24.127 25.570 48.931 1.00 29.56 ? 560 GLU A OE1 1 ATOM 4114 O OE2 . GLU A 1 506 ? 23.989 24.439 50.789 1.00 30.38 ? 560 GLU A OE2 1 ATOM 4115 N N . LEU A 1 507 ? 27.173 29.483 49.113 1.00 24.23 ? 561 LEU A N 1 ATOM 4116 C CA . LEU A 1 507 ? 27.919 30.672 48.733 1.00 25.69 ? 561 LEU A CA 1 ATOM 4117 C C . LEU A 1 507 ? 28.145 31.548 49.959 1.00 25.57 ? 561 LEU A C 1 ATOM 4118 O O . LEU A 1 507 ? 29.277 32.007 50.227 1.00 26.03 ? 561 LEU A O 1 ATOM 4119 C CB . LEU A 1 507 ? 27.154 31.453 47.641 1.00 25.34 ? 561 LEU A CB 1 ATOM 4120 C CG . LEU A 1 507 ? 27.813 32.809 47.308 1.00 25.95 ? 561 LEU A CG 1 ATOM 4121 C CD1 . LEU A 1 507 ? 29.255 32.600 46.693 1.00 25.02 ? 561 LEU A CD1 1 ATOM 4122 C CD2 . LEU A 1 507 ? 26.933 33.597 46.371 1.00 24.44 ? 561 LEU A CD2 1 ATOM 4123 N N . VAL A 1 508 ? 27.071 31.818 50.709 1.00 25.75 ? 562 VAL A N 1 ATOM 4124 C CA . VAL A 1 508 ? 27.192 32.721 51.867 1.00 25.54 ? 562 VAL A CA 1 ATOM 4125 C C . VAL A 1 508 ? 27.994 32.067 53.011 1.00 26.53 ? 562 VAL A C 1 ATOM 4126 O O . VAL A 1 508 ? 28.949 32.648 53.522 1.00 26.62 ? 562 VAL A O 1 ATOM 4127 C CB . VAL A 1 508 ? 25.806 33.167 52.384 1.00 23.79 ? 562 VAL A CB 1 ATOM 4128 C CG1 . VAL A 1 508 ? 25.957 34.038 53.683 1.00 23.69 ? 562 VAL A CG1 1 ATOM 4129 C CG2 . VAL A 1 508 ? 25.042 33.907 51.280 1.00 26.28 ? 562 VAL A CG2 1 ATOM 4130 N N . GLU A 1 509 ? 27.619 30.838 53.359 1.00 26.89 ? 563 GLU A N 1 ATOM 4131 C CA . GLU A 1 509 ? 28.202 30.157 54.531 1.00 29.55 ? 563 GLU A CA 1 ATOM 4132 C C . GLU A 1 509 ? 29.684 29.834 54.305 1.00 29.80 ? 563 GLU A C 1 ATOM 4133 O O . GLU A 1 509 ? 30.494 29.930 55.243 1.00 30.39 ? 563 GLU A O 1 ATOM 4134 C CB . GLU A 1 509 ? 27.417 28.889 54.855 1.00 29.00 ? 563 GLU A CB 1 ATOM 4135 C CG . GLU A 1 509 ? 27.794 28.284 56.197 1.00 33.48 ? 563 GLU A CG 1 ATOM 4136 C CD . GLU A 1 509 ? 28.959 27.281 56.096 1.00 39.89 ? 563 GLU A CD 1 ATOM 4137 O OE1 . GLU A 1 509 ? 29.212 26.715 54.993 1.00 38.59 ? 563 GLU A OE1 1 ATOM 4138 O OE2 . GLU A 1 509 ? 29.625 27.080 57.135 1.00 40.82 ? 563 GLU A OE2 1 ATOM 4139 N N . LYS A 1 510 ? 30.045 29.482 53.074 1.00 28.67 ? 564 LYS A N 1 ATOM 4140 C CA . LYS A 1 510 ? 31.451 29.086 52.801 1.00 28.93 ? 564 LYS A CA 1 ATOM 4141 C C . LYS A 1 510 ? 32.329 30.302 52.526 1.00 30.34 ? 564 LYS A C 1 ATOM 4142 O O . LYS A 1 510 ? 33.486 30.360 53.011 1.00 30.23 ? 564 LYS A O 1 ATOM 4143 C CB . LYS A 1 510 ? 31.546 28.130 51.602 1.00 27.41 ? 564 LYS A CB 1 ATOM 4144 C CG . LYS A 1 510 ? 30.954 26.748 51.873 1.00 29.88 ? 564 LYS A CG 1 ATOM 4145 C CD . LYS A 1 510 ? 31.179 25.877 50.588 1.00 29.58 ? 564 LYS A CD 1 ATOM 4146 C CE . LYS A 1 510 ? 30.386 24.569 50.556 1.00 37.09 ? 564 LYS A CE 1 ATOM 4147 N NZ . LYS A 1 510 ? 30.542 23.855 51.835 1.00 40.79 ? 564 LYS A NZ 1 ATOM 4148 N N . PHE A 1 511 ? 31.808 31.271 51.754 1.00 28.26 ? 565 PHE A N 1 ATOM 4149 C CA . PHE A 1 511 ? 32.693 32.272 51.154 1.00 29.15 ? 565 PHE A CA 1 ATOM 4150 C C . PHE A 1 511 ? 32.477 33.692 51.614 1.00 29.86 ? 565 PHE A C 1 ATOM 4151 O O . PHE A 1 511 ? 33.385 34.496 51.498 1.00 31.73 ? 565 PHE A O 1 ATOM 4152 C CB . PHE A 1 511 ? 32.641 32.219 49.624 1.00 28.56 ? 565 PHE A CB 1 ATOM 4153 C CG . PHE A 1 511 ? 32.985 30.857 49.078 1.00 31.11 ? 565 PHE A CG 1 ATOM 4154 C CD1 . PHE A 1 511 ? 34.212 30.248 49.455 1.00 33.71 ? 565 PHE A CD1 1 ATOM 4155 C CD2 . PHE A 1 511 ? 32.100 30.171 48.260 1.00 29.27 ? 565 PHE A CD2 1 ATOM 4156 C CE1 . PHE A 1 511 ? 34.524 28.980 48.994 1.00 33.57 ? 565 PHE A CE1 1 ATOM 4157 C CE2 . PHE A 1 511 ? 32.405 28.904 47.763 1.00 34.38 ? 565 PHE A CE2 1 ATOM 4158 C CZ . PHE A 1 511 ? 33.611 28.286 48.142 1.00 33.38 ? 565 PHE A CZ 1 ATOM 4159 N N . TYR A 1 512 ? 31.282 34.021 52.097 1.00 29.17 ? 566 TYR A N 1 ATOM 4160 C CA . TYR A 1 512 ? 31.015 35.416 52.501 1.00 27.48 ? 566 TYR A CA 1 ATOM 4161 C C . TYR A 1 512 ? 31.101 35.644 54.001 1.00 26.91 ? 566 TYR A C 1 ATOM 4162 O O . TYR A 1 512 ? 31.730 36.614 54.467 1.00 27.52 ? 566 TYR A O 1 ATOM 4163 C CB . TYR A 1 512 ? 29.616 35.902 51.955 1.00 27.08 ? 566 TYR A CB 1 ATOM 4164 C CG . TYR A 1 512 ? 29.679 36.383 50.517 1.00 26.92 ? 566 TYR A CG 1 ATOM 4165 C CD1 . TYR A 1 512 ? 29.714 35.471 49.438 1.00 26.70 ? 566 TYR A CD1 1 ATOM 4166 C CD2 . TYR A 1 512 ? 29.760 37.747 50.229 1.00 30.11 ? 566 TYR A CD2 1 ATOM 4167 C CE1 . TYR A 1 512 ? 29.778 35.922 48.095 1.00 26.05 ? 566 TYR A CE1 1 ATOM 4168 C CE2 . TYR A 1 512 ? 29.835 38.209 48.907 1.00 30.51 ? 566 TYR A CE2 1 ATOM 4169 C CZ . TYR A 1 512 ? 29.834 37.292 47.855 1.00 27.64 ? 566 TYR A CZ 1 ATOM 4170 O OH . TYR A 1 512 ? 29.974 37.748 46.582 1.00 31.27 ? 566 TYR A OH 1 ATOM 4171 N N . ASP A 1 513 ? 30.432 34.806 54.784 1.00 26.43 ? 567 ASP A N 1 ATOM 4172 C CA . ASP A 1 513 ? 30.263 35.127 56.198 1.00 27.00 ? 567 ASP A CA 1 ATOM 4173 C C . ASP A 1 513 ? 30.048 33.859 57.013 1.00 27.81 ? 567 ASP A C 1 ATOM 4174 O O . ASP A 1 513 ? 29.002 33.663 57.593 1.00 26.27 ? 567 ASP A O 1 ATOM 4175 C CB . ASP A 1 513 ? 29.032 36.084 56.340 1.00 26.31 ? 567 ASP A CB 1 ATOM 4176 C CG . ASP A 1 513 ? 28.948 36.744 57.702 1.00 29.18 ? 567 ASP A CG 1 ATOM 4177 O OD1 . ASP A 1 513 ? 29.953 36.740 58.486 1.00 28.82 ? 567 ASP A OD1 1 ATOM 4178 O OD2 . ASP A 1 513 ? 27.849 37.280 58.006 1.00 26.92 ? 567 ASP A OD2 1 ATOM 4179 N N . PRO A 1 514 ? 31.067 32.962 57.061 1.00 29.30 ? 568 PRO A N 1 ATOM 4180 C CA . PRO A 1 514 ? 30.903 31.697 57.772 1.00 29.68 ? 568 PRO A CA 1 ATOM 4181 C C . PRO A 1 514 ? 30.477 31.807 59.241 1.00 29.94 ? 568 PRO A C 1 ATOM 4182 O O . PRO A 1 514 ? 29.732 30.946 59.712 1.00 31.54 ? 568 PRO A O 1 ATOM 4183 C CB . PRO A 1 514 ? 32.293 30.996 57.626 1.00 30.35 ? 568 PRO A CB 1 ATOM 4184 C CG . PRO A 1 514 ? 33.204 32.036 57.187 1.00 32.04 ? 568 PRO A CG 1 ATOM 4185 C CD . PRO A 1 514 ? 32.409 33.124 56.484 1.00 30.81 ? 568 PRO A CD 1 ATOM 4186 N N A MET A 1 515 ? 30.923 32.836 59.962 0.60 30.32 ? 569 MET A N 1 ATOM 4187 N N B MET A 1 515 ? 30.917 32.869 59.914 0.40 30.35 ? 569 MET A N 1 ATOM 4188 C CA A MET A 1 515 ? 30.518 33.028 61.379 0.60 30.37 ? 569 MET A CA 1 ATOM 4189 C CA B MET A 1 515 ? 30.602 33.140 61.325 0.40 30.57 ? 569 MET A CA 1 ATOM 4190 C C A MET A 1 515 ? 29.233 33.877 61.530 0.60 29.40 ? 569 MET A C 1 ATOM 4191 C C B MET A 1 515 ? 29.278 33.901 61.516 0.40 29.51 ? 569 MET A C 1 ATOM 4192 O O A MET A 1 515 ? 28.751 34.087 62.652 0.60 27.77 ? 569 MET A O 1 ATOM 4193 O O B MET A 1 515 ? 28.806 34.071 62.647 0.40 28.55 ? 569 MET A O 1 ATOM 4194 C CB A MET A 1 515 ? 31.625 33.688 62.218 0.60 32.04 ? 569 MET A CB 1 ATOM 4195 C CB B MET A 1 515 ? 31.718 33.976 61.950 0.40 31.81 ? 569 MET A CB 1 ATOM 4196 C CG A MET A 1 515 ? 32.966 32.849 62.388 0.60 34.67 ? 569 MET A CG 1 ATOM 4197 C CG B MET A 1 515 ? 33.136 33.373 61.784 0.40 35.09 ? 569 MET A CG 1 ATOM 4198 S SD A MET A 1 515 ? 32.682 31.122 62.768 0.60 43.00 ? 569 MET A SD 1 ATOM 4199 S SD B MET A 1 515 ? 34.239 34.017 63.060 0.40 43.08 ? 569 MET A SD 1 ATOM 4200 C CE A MET A 1 515 ? 32.060 31.162 64.450 0.60 42.43 ? 569 MET A CE 1 ATOM 4201 C CE B MET A 1 515 ? 35.292 35.155 62.155 0.40 40.34 ? 569 MET A CE 1 ATOM 4202 N N . PHE A 1 516 ? 28.701 34.360 60.411 1.00 28.29 ? 570 PHE A N 1 ATOM 4203 C CA . PHE A 1 516 ? 27.471 35.203 60.438 1.00 26.71 ? 570 PHE A CA 1 ATOM 4204 C C . PHE A 1 516 ? 27.636 36.473 61.228 1.00 26.44 ? 570 PHE A C 1 ATOM 4205 O O . PHE A 1 516 ? 26.662 37.116 61.652 1.00 27.36 ? 570 PHE A O 1 ATOM 4206 C CB . PHE A 1 516 ? 26.218 34.370 60.757 1.00 26.79 ? 570 PHE A CB 1 ATOM 4207 C CG . PHE A 1 516 ? 25.795 33.544 59.586 1.00 28.12 ? 570 PHE A CG 1 ATOM 4208 C CD1 . PHE A 1 516 ? 24.803 34.023 58.718 1.00 29.55 ? 570 PHE A CD1 1 ATOM 4209 C CD2 . PHE A 1 516 ? 26.448 32.327 59.285 1.00 30.09 ? 570 PHE A CD2 1 ATOM 4210 C CE1 . PHE A 1 516 ? 24.443 33.280 57.566 1.00 28.76 ? 570 PHE A CE1 1 ATOM 4211 C CE2 . PHE A 1 516 ? 26.120 31.591 58.136 1.00 29.86 ? 570 PHE A CE2 1 ATOM 4212 C CZ . PHE A 1 516 ? 25.115 32.069 57.279 1.00 29.94 ? 570 PHE A CZ 1 ATOM 4213 N N . LYS A 1 517 ? 28.886 36.900 61.371 1.00 26.48 ? 571 LYS A N 1 ATOM 4214 C CA . LYS A 1 517 ? 29.156 38.117 62.147 1.00 27.78 ? 571 LYS A CA 1 ATOM 4215 C C . LYS A 1 517 ? 28.854 39.401 61.356 1.00 26.38 ? 571 LYS A C 1 ATOM 4216 O O . LYS A 1 517 ? 28.484 40.414 61.949 1.00 26.47 ? 571 LYS A O 1 ATOM 4217 C CB . LYS A 1 517 ? 30.607 38.162 62.638 1.00 28.26 ? 571 LYS A CB 1 ATOM 4218 C CG . LYS A 1 517 ? 31.614 38.139 61.529 1.00 29.37 ? 571 LYS A CG 1 ATOM 4219 C CD . LYS A 1 517 ? 33.035 38.277 62.129 1.00 35.70 ? 571 LYS A CD 1 ATOM 4220 C CE . LYS A 1 517 ? 34.084 38.299 61.030 1.00 37.17 ? 571 LYS A CE 1 ATOM 4221 N NZ . LYS A 1 517 ? 35.469 38.653 61.594 1.00 40.83 ? 571 LYS A NZ 1 ATOM 4222 N N . TYR A 1 518 ? 29.052 39.365 60.047 1.00 27.16 ? 572 TYR A N 1 ATOM 4223 C CA . TYR A 1 518 ? 28.662 40.532 59.204 1.00 27.12 ? 572 TYR A CA 1 ATOM 4224 C C . TYR A 1 518 ? 27.127 40.664 59.162 1.00 26.66 ? 572 TYR A C 1 ATOM 4225 O O . TYR A 1 518 ? 26.616 41.776 59.277 1.00 26.73 ? 572 TYR A O 1 ATOM 4226 C CB . TYR A 1 518 ? 29.284 40.449 57.781 1.00 25.93 ? 572 TYR A CB 1 ATOM 4227 C CG . TYR A 1 518 ? 30.797 40.410 57.871 1.00 29.81 ? 572 TYR A CG 1 ATOM 4228 C CD1 . TYR A 1 518 ? 31.501 41.488 58.437 1.00 30.42 ? 572 TYR A CD1 1 ATOM 4229 C CD2 . TYR A 1 518 ? 31.512 39.284 57.460 1.00 31.46 ? 572 TYR A CD2 1 ATOM 4230 C CE1 . TYR A 1 518 ? 32.878 41.455 58.565 1.00 34.85 ? 572 TYR A CE1 1 ATOM 4231 C CE2 . TYR A 1 518 ? 32.897 39.236 57.606 1.00 33.58 ? 572 TYR A CE2 1 ATOM 4232 C CZ . TYR A 1 518 ? 33.570 40.329 58.128 1.00 36.29 ? 572 TYR A CZ 1 ATOM 4233 O OH . TYR A 1 518 ? 34.945 40.261 58.245 1.00 38.28 ? 572 TYR A OH 1 ATOM 4234 N N . HIS A 1 519 ? 26.422 39.546 58.986 1.00 25.76 ? 573 HIS A N 1 ATOM 4235 C CA . HIS A 1 519 ? 24.963 39.519 59.159 1.00 26.07 ? 573 HIS A CA 1 ATOM 4236 C C . HIS A 1 519 ? 24.528 40.104 60.504 1.00 26.05 ? 573 HIS A C 1 ATOM 4237 O O . HIS A 1 519 ? 23.612 40.929 60.580 1.00 24.30 ? 573 HIS A O 1 ATOM 4238 C CB . HIS A 1 519 ? 24.403 38.111 59.057 1.00 25.60 ? 573 HIS A CB 1 ATOM 4239 C CG . HIS A 1 519 ? 24.325 37.587 57.663 1.00 26.65 ? 573 HIS A CG 1 ATOM 4240 N ND1 . HIS A 1 519 ? 25.429 37.126 56.975 1.00 27.16 ? 573 HIS A ND1 1 ATOM 4241 C CD2 . HIS A 1 519 ? 23.259 37.396 56.845 1.00 29.53 ? 573 HIS A CD2 1 ATOM 4242 C CE1 . HIS A 1 519 ? 25.055 36.710 55.778 1.00 29.91 ? 573 HIS A CE1 1 ATOM 4243 N NE2 . HIS A 1 519 ? 23.741 36.834 55.684 1.00 29.37 ? 573 HIS A NE2 1 ATOM 4244 N N . LEU A 1 520 ? 25.159 39.650 61.587 1.00 25.40 ? 574 LEU A N 1 ATOM 4245 C CA . LEU A 1 520 ? 24.826 40.174 62.894 1.00 24.47 ? 574 LEU A CA 1 ATOM 4246 C C . LEU A 1 520 ? 25.082 41.668 63.011 1.00 25.19 ? 574 LEU A C 1 ATOM 4247 O O . LEU A 1 520 ? 24.231 42.388 63.494 1.00 23.72 ? 574 LEU A O 1 ATOM 4248 C CB . LEU A 1 520 ? 25.583 39.402 64.030 1.00 25.53 ? 574 LEU A CB 1 ATOM 4249 C CG . LEU A 1 520 ? 25.237 39.925 65.451 1.00 26.70 ? 574 LEU A CG 1 ATOM 4250 C CD1 . LEU A 1 520 ? 23.768 39.717 65.730 1.00 25.01 ? 574 LEU A CD1 1 ATOM 4251 C CD2 . LEU A 1 520 ? 26.057 39.147 66.513 1.00 27.25 ? 574 LEU A CD2 1 ATOM 4252 N N . THR A 1 521 ? 26.215 42.147 62.512 1.00 25.33 ? 575 THR A N 1 ATOM 4253 C CA . THR A 1 521 ? 26.493 43.581 62.530 1.00 24.99 ? 575 THR A CA 1 ATOM 4254 C C . THR A 1 521 ? 25.407 44.337 61.757 1.00 23.72 ? 575 THR A C 1 ATOM 4255 O O . THR A 1 521 ? 24.939 45.350 62.214 1.00 23.98 ? 575 THR A O 1 ATOM 4256 C CB . THR A 1 521 ? 27.876 43.851 61.961 1.00 26.52 ? 575 THR A CB 1 ATOM 4257 O OG1 . THR A 1 521 ? 28.851 43.357 62.918 1.00 27.88 ? 575 THR A OG1 1 ATOM 4258 C CG2 . THR A 1 521 ? 28.108 45.367 61.755 1.00 25.59 ? 575 THR A CG2 1 ATOM 4259 N N . VAL A 1 522 ? 24.997 43.817 60.603 1.00 23.93 ? 576 VAL A N 1 ATOM 4260 C CA . VAL A 1 522 ? 23.947 44.497 59.814 1.00 23.51 ? 576 VAL A CA 1 ATOM 4261 C C . VAL A 1 522 ? 22.591 44.455 60.558 1.00 23.92 ? 576 VAL A C 1 ATOM 4262 O O . VAL A 1 522 ? 21.813 45.425 60.518 1.00 23.14 ? 576 VAL A O 1 ATOM 4263 C CB . VAL A 1 522 ? 23.900 43.947 58.357 1.00 24.45 ? 576 VAL A CB 1 ATOM 4264 C CG1 . VAL A 1 522 ? 22.626 44.514 57.542 1.00 22.65 ? 576 VAL A CG1 1 ATOM 4265 C CG2 . VAL A 1 522 ? 25.223 44.343 57.628 1.00 24.34 ? 576 VAL A CG2 1 ATOM 4266 N N . ALA A 1 523 ? 22.285 43.349 61.221 1.00 22.84 ? 577 ALA A N 1 ATOM 4267 C CA . ALA A 1 523 ? 21.097 43.305 62.066 1.00 23.22 ? 577 ALA A CA 1 ATOM 4268 C C . ALA A 1 523 ? 21.117 44.379 63.172 1.00 23.70 ? 577 ALA A C 1 ATOM 4269 O O . ALA A 1 523 ? 20.097 45.026 63.481 1.00 23.09 ? 577 ALA A O 1 ATOM 4270 C CB . ALA A 1 523 ? 20.919 41.881 62.649 1.00 23.10 ? 577 ALA A CB 1 ATOM 4271 N N . GLN A 1 524 ? 22.281 44.559 63.789 1.00 23.02 ? 578 GLN A N 1 ATOM 4272 C CA . GLN A 1 524 ? 22.450 45.598 64.804 1.00 24.05 ? 578 GLN A CA 1 ATOM 4273 C C . GLN A 1 524 ? 22.258 47.026 64.254 1.00 22.83 ? 578 GLN A C 1 ATOM 4274 O O . GLN A 1 524 ? 21.695 47.873 64.930 1.00 23.59 ? 578 GLN A O 1 ATOM 4275 C CB . GLN A 1 524 ? 23.833 45.460 65.453 1.00 24.09 ? 578 GLN A CB 1 ATOM 4276 C CG . GLN A 1 524 ? 23.908 44.170 66.296 1.00 26.87 ? 578 GLN A CG 1 ATOM 4277 C CD . GLN A 1 524 ? 25.294 43.960 66.913 1.00 30.88 ? 578 GLN A CD 1 ATOM 4278 O OE1 . GLN A 1 524 ? 26.201 44.776 66.720 1.00 28.13 ? 578 GLN A OE1 1 ATOM 4279 N NE2 . GLN A 1 524 ? 25.440 42.870 67.698 1.00 29.60 ? 578 GLN A NE2 1 ATOM 4280 N N . VAL A 1 525 ? 22.758 47.285 63.058 1.00 23.18 ? 579 VAL A N 1 ATOM 4281 C CA . VAL A 1 525 ? 22.636 48.625 62.462 1.00 22.86 ? 579 VAL A CA 1 ATOM 4282 C C . VAL A 1 525 ? 21.166 48.833 62.083 1.00 21.98 ? 579 VAL A C 1 ATOM 4283 O O . VAL A 1 525 ? 20.549 49.811 62.504 1.00 23.15 ? 579 VAL A O 1 ATOM 4284 C CB . VAL A 1 525 ? 23.534 48.783 61.223 1.00 23.02 ? 579 VAL A CB 1 ATOM 4285 C CG1 . VAL A 1 525 ? 23.262 50.151 60.540 1.00 21.52 ? 579 VAL A CG1 1 ATOM 4286 C CG2 . VAL A 1 525 ? 25.047 48.725 61.660 1.00 23.59 ? 579 VAL A CG2 1 ATOM 4287 N N . ARG A 1 526 ? 20.591 47.887 61.337 1.00 22.43 ? 580 ARG A N 1 ATOM 4288 C CA . ARG A 1 526 ? 19.172 48.095 60.875 1.00 21.62 ? 580 ARG A CA 1 ATOM 4289 C C . ARG A 1 526 ? 18.261 48.085 62.069 1.00 22.54 ? 580 ARG A C 1 ATOM 4290 O O . ARG A 1 526 ? 17.380 48.958 62.236 1.00 23.44 ? 580 ARG A O 1 ATOM 4291 C CB . ARG A 1 526 ? 18.756 46.989 59.911 1.00 19.49 ? 580 ARG A CB 1 ATOM 4292 C CG . ARG A 1 526 ? 19.472 47.036 58.603 1.00 20.14 ? 580 ARG A CG 1 ATOM 4293 C CD . ARG A 1 526 ? 19.083 45.820 57.719 1.00 21.15 ? 580 ARG A CD 1 ATOM 4294 N NE . ARG A 1 526 ? 19.846 45.868 56.475 1.00 20.31 ? 580 ARG A NE 1 ATOM 4295 C CZ . ARG A 1 526 ? 19.816 44.938 55.518 1.00 22.98 ? 580 ARG A CZ 1 ATOM 4296 N NH1 . ARG A 1 526 ? 19.093 43.828 55.642 1.00 23.48 ? 580 ARG A NH1 1 ATOM 4297 N NH2 . ARG A 1 526 ? 20.513 45.144 54.421 1.00 20.94 ? 580 ARG A NH2 1 ATOM 4298 N N . GLY A 1 527 ? 18.427 47.065 62.918 1.00 21.57 ? 581 GLY A N 1 ATOM 4299 C CA . GLY A 1 527 ? 17.573 46.960 64.090 1.00 22.32 ? 581 GLY A CA 1 ATOM 4300 C C . GLY A 1 527 ? 17.732 48.128 65.064 1.00 22.84 ? 581 GLY A C 1 ATOM 4301 O O . GLY A 1 527 ? 16.735 48.664 65.597 1.00 22.87 ? 581 GLY A O 1 ATOM 4302 N N . GLY A 1 528 ? 18.970 48.548 65.286 1.00 23.65 ? 582 GLY A N 1 ATOM 4303 C CA . GLY A 1 528 ? 19.237 49.683 66.150 1.00 23.20 ? 582 GLY A CA 1 ATOM 4304 C C . GLY A 1 528 ? 18.623 50.992 65.617 1.00 22.84 ? 582 GLY A C 1 ATOM 4305 O O . GLY A 1 528 ? 18.131 51.850 66.381 1.00 22.94 ? 582 GLY A O 1 ATOM 4306 N N . MET A 1 529 ? 18.686 51.176 64.307 1.00 23.70 ? 583 MET A N 1 ATOM 4307 C CA . MET A 1 529 ? 18.097 52.392 63.713 1.00 23.20 ? 583 MET A CA 1 ATOM 4308 C C . MET A 1 529 ? 16.604 52.383 63.978 1.00 22.50 ? 583 MET A C 1 ATOM 4309 O O . MET A 1 529 ? 16.024 53.390 64.398 1.00 21.57 ? 583 MET A O 1 ATOM 4310 C CB . MET A 1 529 ? 18.394 52.433 62.208 1.00 23.40 ? 583 MET A CB 1 ATOM 4311 C CG . MET A 1 529 ? 19.852 52.884 61.923 1.00 27.18 ? 583 MET A CG 1 ATOM 4312 S SD . MET A 1 529 ? 20.240 52.905 60.172 1.00 27.97 ? 583 MET A SD 1 ATOM 4313 C CE . MET A 1 529 ? 19.471 54.489 59.747 1.00 26.24 ? 583 MET A CE 1 ATOM 4314 N N . VAL A 1 530 ? 15.981 51.243 63.728 1.00 21.91 ? 584 VAL A N 1 ATOM 4315 C CA . VAL A 1 530 ? 14.533 51.112 63.929 1.00 22.86 ? 584 VAL A CA 1 ATOM 4316 C C . VAL A 1 530 ? 14.191 51.352 65.407 1.00 23.37 ? 584 VAL A C 1 ATOM 4317 O O . VAL A 1 530 ? 13.237 52.053 65.727 1.00 21.15 ? 584 VAL A O 1 ATOM 4318 C CB . VAL A 1 530 ? 14.037 49.702 63.503 1.00 23.25 ? 584 VAL A CB 1 ATOM 4319 C CG1 . VAL A 1 530 ? 12.583 49.392 64.059 1.00 22.67 ? 584 VAL A CG1 1 ATOM 4320 C CG2 . VAL A 1 530 ? 14.141 49.527 61.969 1.00 23.62 ? 584 VAL A CG2 1 ATOM 4321 N N . PHE A 1 531 ? 14.979 50.751 66.308 1.00 23.51 ? 585 PHE A N 1 ATOM 4322 C CA . PHE A 1 531 ? 14.776 50.952 67.749 1.00 23.12 ? 585 PHE A CA 1 ATOM 4323 C C . PHE A 1 531 ? 14.789 52.432 68.131 1.00 23.16 ? 585 PHE A C 1 ATOM 4324 O O . PHE A 1 531 ? 13.839 52.918 68.785 1.00 24.27 ? 585 PHE A O 1 ATOM 4325 C CB . PHE A 1 531 ? 15.837 50.142 68.573 1.00 23.79 ? 585 PHE A CB 1 ATOM 4326 C CG . PHE A 1 531 ? 15.533 50.106 70.059 1.00 25.94 ? 585 PHE A CG 1 ATOM 4327 C CD1 . PHE A 1 531 ? 14.970 48.955 70.629 1.00 27.70 ? 585 PHE A CD1 1 ATOM 4328 C CD2 . PHE A 1 531 ? 15.737 51.241 70.849 1.00 26.65 ? 585 PHE A CD2 1 ATOM 4329 C CE1 . PHE A 1 531 ? 14.640 48.938 71.994 1.00 30.97 ? 585 PHE A CE1 1 ATOM 4330 C CE2 . PHE A 1 531 ? 15.412 51.233 72.209 1.00 31.19 ? 585 PHE A CE2 1 ATOM 4331 C CZ . PHE A 1 531 ? 14.871 50.056 72.782 1.00 30.58 ? 585 PHE A CZ 1 ATOM 4332 N N A GLU A 1 532 ? 15.827 53.166 67.730 0.60 23.09 ? 586 GLU A N 1 ATOM 4333 N N B GLU A 1 532 ? 15.811 53.167 67.706 0.40 22.85 ? 586 GLU A N 1 ATOM 4334 C CA A GLU A 1 532 ? 15.897 54.602 68.049 0.60 23.97 ? 586 GLU A CA 1 ATOM 4335 C CA B GLU A 1 532 ? 15.897 54.583 68.068 0.40 23.05 ? 586 GLU A CA 1 ATOM 4336 C C A GLU A 1 532 ? 14.711 55.366 67.444 0.60 22.99 ? 586 GLU A C 1 ATOM 4337 C C B GLU A 1 532 ? 14.847 55.467 67.382 0.40 22.76 ? 586 GLU A C 1 ATOM 4338 O O A GLU A 1 532 ? 14.085 56.169 68.105 0.60 22.07 ? 586 GLU A O 1 ATOM 4339 O O B GLU A 1 532 ? 14.475 56.495 67.926 0.40 22.19 ? 586 GLU A O 1 ATOM 4340 C CB A GLU A 1 532 ? 17.186 55.216 67.511 0.60 25.03 ? 586 GLU A CB 1 ATOM 4341 C CB B GLU A 1 532 ? 17.268 55.140 67.750 0.40 23.79 ? 586 GLU A CB 1 ATOM 4342 C CG A GLU A 1 532 ? 18.458 54.795 68.268 0.60 28.41 ? 586 GLU A CG 1 ATOM 4343 C CG B GLU A 1 532 ? 17.550 56.409 68.487 0.40 22.84 ? 586 GLU A CG 1 ATOM 4344 C CD A GLU A 1 532 ? 18.576 55.483 69.644 0.60 36.05 ? 586 GLU A CD 1 ATOM 4345 C CD B GLU A 1 532 ? 17.862 56.178 69.969 0.40 26.74 ? 586 GLU A CD 1 ATOM 4346 O OE1 A GLU A 1 532 ? 17.707 56.318 69.992 0.60 40.18 ? 586 GLU A OE1 1 ATOM 4347 O OE1 B GLU A 1 532 ? 17.760 55.013 70.470 0.40 22.99 ? 586 GLU A OE1 1 ATOM 4348 O OE2 A GLU A 1 532 ? 19.534 55.178 70.375 0.60 40.54 ? 586 GLU A OE2 1 ATOM 4349 O OE2 B GLU A 1 532 ? 18.210 57.192 70.621 0.40 28.47 ? 586 GLU A OE2 1 ATOM 4350 N N . LEU A 1 533 ? 14.415 55.083 66.178 1.00 22.56 ? 587 LEU A N 1 ATOM 4351 C CA . LEU A 1 533 ? 13.379 55.861 65.466 1.00 22.63 ? 587 LEU A CA 1 ATOM 4352 C C . LEU A 1 533 ? 12.053 55.620 66.164 1.00 22.92 ? 587 LEU A C 1 ATOM 4353 O O . LEU A 1 533 ? 11.209 56.510 66.279 1.00 23.17 ? 587 LEU A O 1 ATOM 4354 C CB . LEU A 1 533 ? 13.329 55.424 63.978 1.00 23.29 ? 587 LEU A CB 1 ATOM 4355 C CG . LEU A 1 533 ? 14.552 55.857 63.143 1.00 21.88 ? 587 LEU A CG 1 ATOM 4356 C CD1 . LEU A 1 533 ? 14.605 54.966 61.885 1.00 18.62 ? 587 LEU A CD1 1 ATOM 4357 C CD2 . LEU A 1 533 ? 14.371 57.345 62.707 1.00 24.07 ? 587 LEU A CD2 1 ATOM 4358 N N . ALA A 1 534 ? 11.868 54.403 66.677 1.00 22.56 ? 588 ALA A N 1 ATOM 4359 C CA . ALA A 1 534 ? 10.570 54.056 67.259 1.00 22.87 ? 588 ALA A CA 1 ATOM 4360 C C . ALA A 1 534 ? 10.464 54.378 68.756 1.00 24.06 ? 588 ALA A C 1 ATOM 4361 O O . ALA A 1 534 ? 9.355 54.393 69.284 1.00 24.73 ? 588 ALA A O 1 ATOM 4362 C CB . ALA A 1 534 ? 10.255 52.581 67.028 1.00 21.63 ? 588 ALA A CB 1 ATOM 4363 N N A ASN A 1 535 ? 11.592 54.624 69.425 0.60 25.15 ? 589 ASN A N 1 ATOM 4364 N N B ASN A 1 535 ? 11.613 54.644 69.393 0.40 25.04 ? 589 ASN A N 1 ATOM 4365 C CA A ASN A 1 535 ? 11.565 54.778 70.896 0.60 24.96 ? 589 ASN A CA 1 ATOM 4366 C CA B ASN A 1 535 ? 11.699 54.792 70.859 0.40 25.29 ? 589 ASN A CA 1 ATOM 4367 C C A ASN A 1 535 ? 12.023 56.117 71.444 0.60 25.10 ? 589 ASN A C 1 ATOM 4368 C C B ASN A 1 535 ? 12.307 56.068 71.404 0.40 25.94 ? 589 ASN A C 1 ATOM 4369 O O A ASN A 1 535 ? 11.519 56.578 72.506 0.60 25.28 ? 589 ASN A O 1 ATOM 4370 O O B ASN A 1 535 ? 12.201 56.318 72.602 0.40 26.68 ? 589 ASN A O 1 ATOM 4371 C CB A ASN A 1 535 ? 12.367 53.625 71.554 0.60 24.67 ? 589 ASN A CB 1 ATOM 4372 C CB B ASN A 1 535 ? 12.456 53.588 71.465 0.40 24.78 ? 589 ASN A CB 1 ATOM 4373 C CG A ASN A 1 535 ? 11.713 53.130 72.794 0.60 26.38 ? 589 ASN A CG 1 ATOM 4374 C CG B ASN A 1 535 ? 11.654 52.330 71.401 0.40 24.30 ? 589 ASN A CG 1 ATOM 4375 O OD1 A ASN A 1 535 ? 10.505 52.860 72.807 0.60 26.36 ? 589 ASN A OD1 1 ATOM 4376 O OD1 B ASN A 1 535 ? 10.700 52.166 72.146 0.40 24.43 ? 589 ASN A OD1 1 ATOM 4377 N ND2 A ASN A 1 535 ? 12.507 52.977 73.864 0.60 27.80 ? 589 ASN A ND2 1 ATOM 4378 N ND2 B ASN A 1 535 ? 12.012 51.437 70.491 0.40 24.71 ? 589 ASN A ND2 1 ATOM 4379 N N A SER A 1 536 ? 12.958 56.762 70.736 0.60 24.79 ? 590 SER A N 1 ATOM 4380 N N B SER A 1 536 ? 12.963 56.872 70.569 0.40 25.89 ? 590 SER A N 1 ATOM 4381 C CA A SER A 1 536 ? 13.518 58.038 71.201 0.60 24.05 ? 590 SER A CA 1 ATOM 4382 C CA B SER A 1 536 ? 13.537 58.125 71.075 0.40 26.30 ? 590 SER A CA 1 ATOM 4383 C C A SER A 1 536 ? 12.381 59.031 71.402 0.60 24.35 ? 590 SER A C 1 ATOM 4384 C C B SER A 1 536 ? 12.443 59.148 71.314 0.40 25.56 ? 590 SER A C 1 ATOM 4385 O O A SER A 1 536 ? 11.421 59.120 70.580 0.60 24.02 ? 590 SER A O 1 ATOM 4386 O O B SER A 1 536 ? 11.594 59.385 70.422 0.40 24.98 ? 590 SER A O 1 ATOM 4387 C CB A SER A 1 536 ? 14.574 58.581 70.212 0.60 24.23 ? 590 SER A CB 1 ATOM 4388 C CB B SER A 1 536 ? 14.548 58.706 70.089 0.40 26.53 ? 590 SER A CB 1 ATOM 4389 O OG A SER A 1 536 ? 15.144 59.818 70.624 0.60 18.99 ? 590 SER A OG 1 ATOM 4390 O OG B SER A 1 536 ? 15.699 57.901 70.030 0.40 29.45 ? 590 SER A OG 1 ATOM 4391 N N . ILE A 1 537 ? 12.454 59.782 72.482 1.00 24.85 ? 591 ILE A N 1 ATOM 4392 C CA . ILE A 1 537 ? 11.406 60.747 72.794 1.00 25.01 ? 591 ILE A CA 1 ATOM 4393 C C . ILE A 1 537 ? 11.307 61.808 71.713 1.00 23.85 ? 591 ILE A C 1 ATOM 4394 O O . ILE A 1 537 ? 10.206 62.077 71.173 1.00 25.09 ? 591 ILE A O 1 ATOM 4395 C CB . ILE A 1 537 ? 11.708 61.458 74.165 1.00 23.36 ? 591 ILE A CB 1 ATOM 4396 C CG1 . ILE A 1 537 ? 11.690 60.419 75.295 1.00 29.22 ? 591 ILE A CG1 1 ATOM 4397 C CG2 . ILE A 1 537 ? 10.659 62.465 74.427 1.00 29.40 ? 591 ILE A CG2 1 ATOM 4398 C CD1 . ILE A 1 537 ? 10.429 59.550 75.311 1.00 31.73 ? 591 ILE A CD1 1 ATOM 4399 N N . VAL A 1 538 ? 12.445 62.429 71.422 1.00 24.86 ? 592 VAL A N 1 ATOM 4400 C CA . VAL A 1 538 ? 12.550 63.366 70.283 1.00 25.68 ? 592 VAL A CA 1 ATOM 4401 C C . VAL A 1 538 ? 13.039 62.533 69.073 1.00 25.64 ? 592 VAL A C 1 ATOM 4402 O O . VAL A 1 538 ? 14.036 61.776 69.184 1.00 25.06 ? 592 VAL A O 1 ATOM 4403 C CB . VAL A 1 538 ? 13.523 64.532 70.583 1.00 26.26 ? 592 VAL A CB 1 ATOM 4404 C CG1 . VAL A 1 538 ? 13.599 65.462 69.350 1.00 27.60 ? 592 VAL A CG1 1 ATOM 4405 C CG2 . VAL A 1 538 ? 13.033 65.347 71.831 1.00 27.61 ? 592 VAL A CG2 1 ATOM 4406 N N . LEU A 1 539 ? 12.359 62.652 67.920 1.00 24.94 ? 593 LEU A N 1 ATOM 4407 C CA . LEU A 1 539 ? 12.804 61.872 66.727 1.00 24.37 ? 593 LEU A CA 1 ATOM 4408 C C . LEU A 1 539 ? 14.281 62.129 66.489 1.00 23.63 ? 593 LEU A C 1 ATOM 4409 O O . LEU A 1 539 ? 14.732 63.295 66.616 1.00 25.08 ? 593 LEU A O 1 ATOM 4410 C CB . LEU A 1 539 ? 11.973 62.256 65.464 1.00 23.02 ? 593 LEU A CB 1 ATOM 4411 C CG . LEU A 1 539 ? 10.569 61.668 65.499 1.00 25.73 ? 593 LEU A CG 1 ATOM 4412 C CD1 . LEU A 1 539 ? 9.697 62.236 64.317 1.00 24.44 ? 593 LEU A CD1 1 ATOM 4413 C CD2 . LEU A 1 539 ? 10.660 60.145 65.461 1.00 26.57 ? 593 LEU A CD2 1 ATOM 4414 N N . PRO A 1 540 ? 15.045 61.074 66.123 1.00 23.70 ? 594 PRO A N 1 ATOM 4415 C CA . PRO A 1 540 ? 16.508 61.266 66.021 1.00 24.74 ? 594 PRO A CA 1 ATOM 4416 C C . PRO A 1 540 ? 16.951 61.759 64.626 1.00 25.03 ? 594 PRO A C 1 ATOM 4417 O O . PRO A 1 540 ? 17.747 61.085 63.947 1.00 24.15 ? 594 PRO A O 1 ATOM 4418 C CB . PRO A 1 540 ? 17.071 59.872 66.267 1.00 25.24 ? 594 PRO A CB 1 ATOM 4419 C CG . PRO A 1 540 ? 16.004 58.921 65.739 1.00 24.05 ? 594 PRO A CG 1 ATOM 4420 C CD . PRO A 1 540 ? 14.653 59.655 66.020 1.00 23.04 ? 594 PRO A CD 1 ATOM 4421 N N . PHE A 1 541 ? 16.408 62.907 64.242 1.00 23.98 ? 595 PHE A N 1 ATOM 4422 C CA . PHE A 1 541 ? 16.712 63.594 62.971 1.00 24.86 ? 595 PHE A CA 1 ATOM 4423 C C . PHE A 1 541 ? 17.397 64.907 63.264 1.00 25.09 ? 595 PHE A C 1 ATOM 4424 O O . PHE A 1 541 ? 16.935 65.641 64.164 1.00 25.83 ? 595 PHE A O 1 ATOM 4425 C CB . PHE A 1 541 ? 15.385 63.947 62.261 1.00 22.50 ? 595 PHE A CB 1 ATOM 4426 C CG . PHE A 1 541 ? 14.620 62.741 61.744 1.00 23.24 ? 595 PHE A CG 1 ATOM 4427 C CD1 . PHE A 1 541 ? 15.243 61.542 61.510 1.00 23.08 ? 595 PHE A CD1 1 ATOM 4428 C CD2 . PHE A 1 541 ? 13.271 62.857 61.451 1.00 22.82 ? 595 PHE A CD2 1 ATOM 4429 C CE1 . PHE A 1 541 ? 14.526 60.445 60.959 1.00 23.91 ? 595 PHE A CE1 1 ATOM 4430 C CE2 . PHE A 1 541 ? 12.530 61.760 60.956 1.00 23.96 ? 595 PHE A CE2 1 ATOM 4431 C CZ . PHE A 1 541 ? 13.153 60.574 60.732 1.00 21.19 ? 595 PHE A CZ 1 ATOM 4432 N N . ASP A 1 542 ? 18.434 65.243 62.495 1.00 24.12 ? 596 ASP A N 1 ATOM 4433 C CA . ASP A 1 542 ? 19.074 66.552 62.678 1.00 24.12 ? 596 ASP A CA 1 ATOM 4434 C C . ASP A 1 542 ? 18.888 67.356 61.416 1.00 23.50 ? 596 ASP A C 1 ATOM 4435 O O . ASP A 1 542 ? 19.561 67.096 60.394 1.00 23.30 ? 596 ASP A O 1 ATOM 4436 C CB . ASP A 1 542 ? 20.573 66.394 62.986 1.00 23.66 ? 596 ASP A CB 1 ATOM 4437 C CG . ASP A 1 542 ? 21.222 67.725 63.422 1.00 28.94 ? 596 ASP A CG 1 ATOM 4438 O OD1 . ASP A 1 542 ? 20.631 68.799 63.188 1.00 28.07 ? 596 ASP A OD1 1 ATOM 4439 O OD2 . ASP A 1 542 ? 22.300 67.702 64.073 1.00 31.18 ? 596 ASP A OD2 1 ATOM 4440 N N . CYS A 1 543 ? 17.939 68.287 61.444 1.00 23.05 ? 597 CYS A N 1 ATOM 4441 C CA . CYS A 1 543 ? 17.697 69.098 60.245 1.00 24.04 ? 597 CYS A CA 1 ATOM 4442 C C . CYS A 1 543 ? 18.894 69.896 59.765 1.00 23.82 ? 597 CYS A C 1 ATOM 4443 O O . CYS A 1 543 ? 18.930 70.275 58.602 1.00 22.17 ? 597 CYS A O 1 ATOM 4444 C CB . CYS A 1 543 ? 16.516 70.056 60.469 1.00 23.33 ? 597 CYS A CB 1 ATOM 4445 S SG . CYS A 1 543 ? 16.830 71.246 61.931 1.00 28.51 ? 597 CYS A SG 1 ATOM 4446 N N . ARG A 1 544 ? 19.848 70.211 60.653 1.00 24.34 ? 598 ARG A N 1 ATOM 4447 C CA . ARG A 1 544 ? 21.077 70.926 60.241 1.00 24.94 ? 598 ARG A CA 1 ATOM 4448 C C . ARG A 1 544 ? 21.915 70.159 59.215 1.00 24.84 ? 598 ARG A C 1 ATOM 4449 O O . ARG A 1 544 ? 22.572 70.766 58.338 1.00 24.17 ? 598 ARG A O 1 ATOM 4450 C CB . ARG A 1 544 ? 21.943 71.281 61.460 1.00 25.18 ? 598 ARG A CB 1 ATOM 4451 C CG . ARG A 1 544 ? 21.200 72.270 62.398 1.00 26.85 ? 598 ARG A CG 1 ATOM 4452 C CD . ARG A 1 544 ? 21.950 72.405 63.741 1.00 28.14 ? 598 ARG A CD 1 ATOM 4453 N NE . ARG A 1 544 ? 22.046 71.109 64.418 1.00 29.55 ? 598 ARG A NE 1 ATOM 4454 C CZ . ARG A 1 544 ? 22.727 70.929 65.562 1.00 35.57 ? 598 ARG A CZ 1 ATOM 4455 N NH1 . ARG A 1 544 ? 23.330 71.976 66.116 1.00 32.26 ? 598 ARG A NH1 1 ATOM 4456 N NH2 . ARG A 1 544 ? 22.809 69.731 66.130 1.00 30.29 ? 598 ARG A NH2 1 ATOM 4457 N N . ASP A 1 545 ? 21.848 68.831 59.278 1.00 24.20 ? 599 ASP A N 1 ATOM 4458 C CA . ASP A 1 545 ? 22.519 68.033 58.275 1.00 23.95 ? 599 ASP A CA 1 ATOM 4459 C C . ASP A 1 545 ? 21.925 68.207 56.866 1.00 23.12 ? 599 ASP A C 1 ATOM 4460 O O . ASP A 1 545 ? 22.655 68.144 55.886 1.00 22.58 ? 599 ASP A O 1 ATOM 4461 C CB . ASP A 1 545 ? 22.526 66.572 58.662 1.00 23.90 ? 599 ASP A CB 1 ATOM 4462 C CG . ASP A 1 545 ? 23.641 66.264 59.658 1.00 30.15 ? 599 ASP A CG 1 ATOM 4463 O OD1 . ASP A 1 545 ? 24.800 66.680 59.390 1.00 36.21 ? 599 ASP A OD1 1 ATOM 4464 O OD2 . ASP A 1 545 ? 23.360 65.613 60.671 1.00 31.36 ? 599 ASP A OD2 1 ATOM 4465 N N . TYR A 1 546 ? 20.622 68.462 56.769 1.00 22.03 ? 600 TYR A N 1 ATOM 4466 C CA . TYR A 1 546 ? 20.055 68.762 55.453 1.00 21.16 ? 600 TYR A CA 1 ATOM 4467 C C . TYR A 1 546 ? 20.597 70.094 54.961 1.00 21.55 ? 600 TYR A C 1 ATOM 4468 O O . TYR A 1 546 ? 20.882 70.239 53.776 1.00 21.23 ? 600 TYR A O 1 ATOM 4469 C CB . TYR A 1 546 ? 18.520 68.822 55.503 1.00 20.81 ? 600 TYR A CB 1 ATOM 4470 C CG . TYR A 1 546 ? 17.873 67.853 54.485 1.00 19.85 ? 600 TYR A CG 1 ATOM 4471 C CD1 . TYR A 1 546 ? 18.196 67.934 53.143 1.00 19.74 ? 600 TYR A CD1 1 ATOM 4472 C CD2 . TYR A 1 546 ? 16.948 66.904 54.899 1.00 21.77 ? 600 TYR A CD2 1 ATOM 4473 C CE1 . TYR A 1 546 ? 17.638 67.049 52.202 1.00 20.28 ? 600 TYR A CE1 1 ATOM 4474 C CE2 . TYR A 1 546 ? 16.349 66.011 53.987 1.00 24.59 ? 600 TYR A CE2 1 ATOM 4475 C CZ . TYR A 1 546 ? 16.682 66.110 52.632 1.00 20.08 ? 600 TYR A CZ 1 ATOM 4476 O OH . TYR A 1 546 ? 16.066 65.227 51.769 1.00 20.67 ? 600 TYR A OH 1 ATOM 4477 N N . ALA A 1 547 ? 20.715 71.094 55.853 1.00 22.41 ? 601 ALA A N 1 ATOM 4478 C CA . ALA A 1 547 ? 21.206 72.424 55.412 1.00 22.39 ? 601 ALA A CA 1 ATOM 4479 C C . ALA A 1 547 ? 22.597 72.326 54.774 1.00 22.83 ? 601 ALA A C 1 ATOM 4480 O O . ALA A 1 547 ? 22.872 72.945 53.738 1.00 23.05 ? 601 ALA A O 1 ATOM 4481 C CB . ALA A 1 547 ? 21.211 73.449 56.599 1.00 22.14 ? 601 ALA A CB 1 ATOM 4482 N N . VAL A 1 548 ? 23.458 71.538 55.388 1.00 23.54 ? 602 VAL A N 1 ATOM 4483 C CA . VAL A 1 548 ? 24.822 71.361 54.906 1.00 24.21 ? 602 VAL A CA 1 ATOM 4484 C C . VAL A 1 548 ? 24.837 70.755 53.471 1.00 24.06 ? 602 VAL A C 1 ATOM 4485 O O . VAL A 1 548 ? 25.473 71.292 52.569 1.00 24.15 ? 602 VAL A O 1 ATOM 4486 C CB . VAL A 1 548 ? 25.678 70.493 55.898 1.00 24.80 ? 602 VAL A CB 1 ATOM 4487 C CG1 . VAL A 1 548 ? 27.063 70.131 55.292 1.00 28.10 ? 602 VAL A CG1 1 ATOM 4488 C CG2 . VAL A 1 548 ? 25.881 71.272 57.181 1.00 27.02 ? 602 VAL A CG2 1 ATOM 4489 N N . VAL A 1 549 ? 24.063 69.689 53.254 1.00 22.88 ? 603 VAL A N 1 ATOM 4490 C CA A VAL A 1 549 ? 24.137 69.045 51.934 0.60 21.85 ? 603 VAL A CA 1 ATOM 4491 C CA B VAL A 1 549 ? 24.053 68.991 51.999 0.40 22.91 ? 603 VAL A CA 1 ATOM 4492 C C . VAL A 1 549 ? 23.425 69.888 50.897 1.00 22.15 ? 603 VAL A C 1 ATOM 4493 O O . VAL A 1 549 ? 23.846 69.872 49.740 1.00 22.53 ? 603 VAL A O 1 ATOM 4494 C CB A VAL A 1 549 ? 23.636 67.587 51.856 0.60 21.15 ? 603 VAL A CB 1 ATOM 4495 C CB B VAL A 1 549 ? 23.306 67.676 52.249 0.40 23.10 ? 603 VAL A CB 1 ATOM 4496 C CG1 A VAL A 1 549 ? 24.461 66.684 52.773 0.60 20.50 ? 603 VAL A CG1 1 ATOM 4497 C CG1 B VAL A 1 549 ? 22.851 67.091 51.042 0.40 23.00 ? 603 VAL A CG1 1 ATOM 4498 C CG2 A VAL A 1 549 ? 22.134 67.498 52.192 0.60 16.67 ? 603 VAL A CG2 1 ATOM 4499 C CG2 B VAL A 1 549 ? 24.200 66.683 53.015 0.40 22.23 ? 603 VAL A CG2 1 ATOM 4500 N N . LEU A 1 550 ? 22.408 70.664 51.291 1.00 21.89 ? 604 LEU A N 1 ATOM 4501 C CA . LEU A 1 550 ? 21.686 71.500 50.293 1.00 22.69 ? 604 LEU A CA 1 ATOM 4502 C C . LEU A 1 550 ? 22.658 72.529 49.694 1.00 23.27 ? 604 LEU A C 1 ATOM 4503 O O . LEU A 1 550 ? 22.583 72.859 48.498 1.00 23.02 ? 604 LEU A O 1 ATOM 4504 C CB . LEU A 1 550 ? 20.459 72.190 50.874 1.00 21.33 ? 604 LEU A CB 1 ATOM 4505 C CG . LEU A 1 550 ? 19.227 71.271 51.143 1.00 19.20 ? 604 LEU A CG 1 ATOM 4506 C CD1 . LEU A 1 550 ? 18.229 72.017 52.033 1.00 22.11 ? 604 LEU A CD1 1 ATOM 4507 C CD2 . LEU A 1 550 ? 18.558 70.749 49.779 1.00 18.28 ? 604 LEU A CD2 1 ATOM 4508 N N . ARG A 1 551 ? 23.566 73.039 50.533 1.00 24.15 ? 605 ARG A N 1 ATOM 4509 C CA . ARG A 1 551 ? 24.548 74.006 50.026 1.00 25.65 ? 605 ARG A CA 1 ATOM 4510 C C . ARG A 1 551 ? 25.492 73.332 49.078 1.00 24.67 ? 605 ARG A C 1 ATOM 4511 O O . ARG A 1 551 ? 25.814 73.871 48.025 1.00 25.90 ? 605 ARG A O 1 ATOM 4512 C CB . ARG A 1 551 ? 25.302 74.689 51.186 1.00 26.19 ? 605 ARG A CB 1 ATOM 4513 C CG . ARG A 1 551 ? 26.450 75.619 50.717 1.00 29.21 ? 605 ARG A CG 1 ATOM 4514 C CD . ARG A 1 551 ? 25.930 76.714 49.751 1.00 32.34 ? 605 ARG A CD 1 ATOM 4515 N NE . ARG A 1 551 ? 27.077 77.522 49.322 1.00 38.81 ? 605 ARG A NE 1 ATOM 4516 C CZ . ARG A 1 551 ? 27.539 78.576 49.995 1.00 43.28 ? 605 ARG A CZ 1 ATOM 4517 N NH1 . ARG A 1 551 ? 26.926 79.004 51.114 1.00 39.82 ? 605 ARG A NH1 1 ATOM 4518 N NH2 . ARG A 1 551 ? 28.624 79.207 49.545 1.00 44.38 ? 605 ARG A NH2 1 ATOM 4519 N N . LYS A 1 552 ? 25.967 72.145 49.451 1.00 25.07 ? 606 LYS A N 1 ATOM 4520 C CA . LYS A 1 552 ? 26.811 71.351 48.580 1.00 24.88 ? 606 LYS A CA 1 ATOM 4521 C C . LYS A 1 552 ? 26.131 71.104 47.232 1.00 23.89 ? 606 LYS A C 1 ATOM 4522 O O . LYS A 1 552 ? 26.759 71.213 46.162 1.00 22.78 ? 606 LYS A O 1 ATOM 4523 C CB . LYS A 1 552 ? 27.132 70.031 49.291 1.00 26.42 ? 606 LYS A CB 1 ATOM 4524 C CG . LYS A 1 552 ? 27.984 69.050 48.512 1.00 31.04 ? 606 LYS A CG 1 ATOM 4525 C CD . LYS A 1 552 ? 28.418 67.853 49.399 1.00 37.47 ? 606 LYS A CD 1 ATOM 4526 C CE . LYS A 1 552 ? 27.398 66.724 49.332 1.00 42.44 ? 606 LYS A CE 1 ATOM 4527 N NZ . LYS A 1 552 ? 27.649 65.575 50.314 1.00 44.68 ? 606 LYS A NZ 1 ATOM 4528 N N . TYR A 1 553 ? 24.843 70.725 47.249 1.00 21.84 ? 607 TYR A N 1 ATOM 4529 C CA . TYR A 1 553 ? 24.200 70.346 45.972 1.00 21.50 ? 607 TYR A CA 1 ATOM 4530 C C . TYR A 1 553 ? 23.925 71.604 45.140 1.00 20.57 ? 607 TYR A C 1 ATOM 4531 O O . TYR A 1 553 ? 23.957 71.542 43.923 1.00 21.47 ? 607 TYR A O 1 ATOM 4532 C CB . TYR A 1 553 ? 22.834 69.701 46.219 1.00 20.95 ? 607 TYR A CB 1 ATOM 4533 C CG . TYR A 1 553 ? 22.894 68.418 47.046 1.00 21.59 ? 607 TYR A CG 1 ATOM 4534 C CD1 . TYR A 1 553 ? 24.041 67.627 47.064 1.00 21.94 ? 607 TYR A CD1 1 ATOM 4535 C CD2 . TYR A 1 553 ? 21.785 67.992 47.759 1.00 20.39 ? 607 TYR A CD2 1 ATOM 4536 C CE1 . TYR A 1 553 ? 24.125 66.460 47.836 1.00 24.34 ? 607 TYR A CE1 1 ATOM 4537 C CE2 . TYR A 1 553 ? 21.838 66.803 48.542 1.00 22.53 ? 607 TYR A CE2 1 ATOM 4538 C CZ . TYR A 1 553 ? 23.025 66.066 48.570 1.00 23.55 ? 607 TYR A CZ 1 ATOM 4539 O OH . TYR A 1 553 ? 23.049 64.911 49.315 1.00 22.53 ? 607 TYR A OH 1 ATOM 4540 N N . ALA A 1 554 ? 23.674 72.720 45.811 1.00 21.07 ? 608 ALA A N 1 ATOM 4541 C CA . ALA A 1 554 ? 23.462 73.981 45.104 1.00 22.21 ? 608 ALA A CA 1 ATOM 4542 C C . ALA A 1 554 ? 24.774 74.445 44.442 1.00 23.84 ? 608 ALA A C 1 ATOM 4543 O O . ALA A 1 554 ? 24.790 74.886 43.269 1.00 25.30 ? 608 ALA A O 1 ATOM 4544 C CB . ALA A 1 554 ? 22.966 75.038 46.048 1.00 23.75 ? 608 ALA A CB 1 ATOM 4545 N N . ASP A 1 555 ? 25.863 74.370 45.194 1.00 25.10 ? 609 ASP A N 1 ATOM 4546 C CA . ASP A 1 555 ? 27.198 74.628 44.620 1.00 26.81 ? 609 ASP A CA 1 ATOM 4547 C C . ASP A 1 555 ? 27.435 73.753 43.352 1.00 26.32 ? 609 ASP A C 1 ATOM 4548 O O . ASP A 1 555 ? 27.930 74.223 42.316 1.00 26.19 ? 609 ASP A O 1 ATOM 4549 C CB . ASP A 1 555 ? 28.250 74.268 45.656 1.00 27.62 ? 609 ASP A CB 1 ATOM 4550 C CG . ASP A 1 555 ? 28.490 75.344 46.686 1.00 30.86 ? 609 ASP A CG 1 ATOM 4551 O OD1 . ASP A 1 555 ? 28.000 76.478 46.570 1.00 31.98 ? 609 ASP A OD1 1 ATOM 4552 O OD2 . ASP A 1 555 ? 29.229 75.018 47.646 1.00 38.63 ? 609 ASP A OD2 1 ATOM 4553 N N . LYS A 1 556 ? 27.097 72.476 43.446 1.00 24.69 ? 610 LYS A N 1 ATOM 4554 C CA . LYS A 1 556 ? 27.323 71.546 42.369 1.00 25.07 ? 610 LYS A CA 1 ATOM 4555 C C . LYS A 1 556 ? 26.501 71.857 41.116 1.00 24.62 ? 610 LYS A C 1 ATOM 4556 O O . LYS A 1 556 ? 27.027 71.870 39.981 1.00 24.69 ? 610 LYS A O 1 ATOM 4557 C CB . LYS A 1 556 ? 27.069 70.090 42.878 1.00 25.35 ? 610 LYS A CB 1 ATOM 4558 C CG . LYS A 1 556 ? 27.253 69.003 41.836 1.00 30.93 ? 610 LYS A CG 1 ATOM 4559 C CD . LYS A 1 556 ? 28.690 68.906 41.340 1.00 40.57 ? 610 LYS A CD 1 ATOM 4560 C CE . LYS A 1 556 ? 28.729 68.087 40.016 1.00 44.86 ? 610 LYS A CE 1 ATOM 4561 N NZ . LYS A 1 556 ? 30.092 67.878 39.492 1.00 52.18 ? 610 LYS A NZ 1 ATOM 4562 N N . ILE A 1 557 ? 25.199 72.089 41.302 1.00 24.21 ? 611 ILE A N 1 ATOM 4563 C CA . ILE A 1 557 ? 24.359 72.375 40.169 1.00 23.92 ? 611 ILE A CA 1 ATOM 4564 C C . ILE A 1 557 ? 24.748 73.737 39.491 1.00 24.76 ? 611 ILE A C 1 ATOM 4565 O O . ILE A 1 557 ? 24.821 73.841 38.236 1.00 24.18 ? 611 ILE A O 1 ATOM 4566 C CB . ILE A 1 557 ? 22.852 72.226 40.557 1.00 23.84 ? 611 ILE A CB 1 ATOM 4567 C CG1 . ILE A 1 557 ? 21.987 72.147 39.296 1.00 25.95 ? 611 ILE A CG1 1 ATOM 4568 C CG2 . ILE A 1 557 ? 22.350 73.356 41.517 1.00 25.38 ? 611 ILE A CG2 1 ATOM 4569 C CD1 . ILE A 1 557 ? 22.161 70.865 38.537 1.00 24.96 ? 611 ILE A CD1 1 ATOM 4570 N N . TYR A 1 558 ? 25.042 74.742 40.327 1.00 23.41 ? 612 TYR A N 1 ATOM 4571 C CA . TYR A 1 558 ? 25.586 76.002 39.820 1.00 27.18 ? 612 TYR A CA 1 ATOM 4572 C C . TYR A 1 558 ? 26.851 75.730 38.967 1.00 26.95 ? 612 TYR A C 1 ATOM 4573 O O . TYR A 1 558 ? 27.020 76.291 37.863 1.00 28.82 ? 612 TYR A O 1 ATOM 4574 C CB . TYR A 1 558 ? 25.889 76.945 41.012 1.00 26.83 ? 612 TYR A CB 1 ATOM 4575 C CG . TYR A 1 558 ? 26.642 78.175 40.590 1.00 30.88 ? 612 TYR A CG 1 ATOM 4576 C CD1 . TYR A 1 558 ? 25.975 79.240 39.999 1.00 34.12 ? 612 TYR A CD1 1 ATOM 4577 C CD2 . TYR A 1 558 ? 28.027 78.257 40.747 1.00 37.02 ? 612 TYR A CD2 1 ATOM 4578 C CE1 . TYR A 1 558 ? 26.661 80.411 39.617 1.00 40.44 ? 612 TYR A CE1 1 ATOM 4579 C CE2 . TYR A 1 558 ? 28.731 79.432 40.349 1.00 41.68 ? 612 TYR A CE2 1 ATOM 4580 C CZ . TYR A 1 558 ? 28.017 80.486 39.781 1.00 42.25 ? 612 TYR A CZ 1 ATOM 4581 O OH . TYR A 1 558 ? 28.653 81.658 39.381 1.00 50.39 ? 612 TYR A OH 1 ATOM 4582 N N . SER A 1 559 ? 27.759 74.885 39.457 1.00 28.61 ? 613 SER A N 1 ATOM 4583 C CA . SER A 1 559 ? 29.014 74.603 38.715 1.00 29.23 ? 613 SER A CA 1 ATOM 4584 C C . SER A 1 559 ? 28.762 73.971 37.336 1.00 28.93 ? 613 SER A C 1 ATOM 4585 O O . SER A 1 559 ? 29.457 74.290 36.380 1.00 28.78 ? 613 SER A O 1 ATOM 4586 C CB . SER A 1 559 ? 29.969 73.713 39.514 1.00 29.40 ? 613 SER A CB 1 ATOM 4587 O OG A SER A 1 559 ? 30.503 74.442 40.597 0.50 32.80 ? 613 SER A OG 1 ATOM 4588 O OG B SER A 1 559 ? 29.450 72.401 39.645 0.50 29.60 ? 613 SER A OG 1 ATOM 4589 N N . ILE A 1 560 ? 27.747 73.111 37.236 1.00 27.79 ? 614 ILE A N 1 ATOM 4590 C CA . ILE A 1 560 ? 27.350 72.514 35.968 1.00 28.16 ? 614 ILE A CA 1 ATOM 4591 C C . ILE A 1 560 ? 26.844 73.577 35.003 1.00 29.19 ? 614 ILE A C 1 ATOM 4592 O O . ILE A 1 560 ? 27.260 73.618 33.832 1.00 29.17 ? 614 ILE A O 1 ATOM 4593 C CB . ILE A 1 560 ? 26.281 71.412 36.172 1.00 28.26 ? 614 ILE A CB 1 ATOM 4594 C CG1 . ILE A 1 560 ? 26.888 70.236 36.950 1.00 29.58 ? 614 ILE A CG1 1 ATOM 4595 C CG2 . ILE A 1 560 ? 25.637 70.944 34.808 1.00 28.20 ? 614 ILE A CG2 1 ATOM 4596 C CD1 . ILE A 1 560 ? 25.798 69.145 37.273 1.00 29.39 ? 614 ILE A CD1 1 ATOM 4597 N N . SER A 1 561 ? 25.974 74.461 35.493 1.00 27.48 ? 615 SER A N 1 ATOM 4598 C CA . SER A 1 561 ? 25.413 75.504 34.648 1.00 27.53 ? 615 SER A CA 1 ATOM 4599 C C . SER A 1 561 ? 26.499 76.421 34.146 1.00 29.01 ? 615 SER A C 1 ATOM 4600 O O . SER A 1 561 ? 26.471 76.864 32.982 1.00 28.41 ? 615 SER A O 1 ATOM 4601 C CB . SER A 1 561 ? 24.400 76.324 35.441 1.00 27.45 ? 615 SER A CB 1 ATOM 4602 O OG . SER A 1 561 ? 23.694 77.211 34.580 1.00 27.87 ? 615 SER A OG 1 ATOM 4603 N N . MET A 1 562 ? 27.456 76.694 35.031 1.00 29.91 ? 616 MET A N 1 ATOM 4604 C CA . MET A 1 562 ? 28.569 77.631 34.735 1.00 32.78 ? 616 MET A CA 1 ATOM 4605 C C . MET A 1 562 ? 29.579 77.121 33.712 1.00 34.16 ? 616 MET A C 1 ATOM 4606 O O . MET A 1 562 ? 30.531 77.813 33.348 1.00 35.66 ? 616 MET A O 1 ATOM 4607 C CB . MET A 1 562 ? 29.239 78.067 36.032 1.00 32.55 ? 616 MET A CB 1 ATOM 4608 C CG . MET A 1 562 ? 28.385 79.171 36.693 1.00 35.83 ? 616 MET A CG 1 ATOM 4609 S SD . MET A 1 562 ? 28.356 80.788 35.761 1.00 45.06 ? 616 MET A SD 1 ATOM 4610 C CE . MET A 1 562 ? 30.072 81.259 35.832 1.00 39.82 ? 616 MET A CE 1 ATOM 4611 N N . LYS A 1 563 ? 29.362 75.912 33.224 1.00 34.55 ? 617 LYS A N 1 ATOM 4612 C CA . LYS A 1 563 ? 29.997 75.473 31.980 1.00 35.34 ? 617 LYS A CA 1 ATOM 4613 C C . LYS A 1 563 ? 29.482 76.225 30.734 1.00 34.80 ? 617 LYS A C 1 ATOM 4614 O O . LYS A 1 563 ? 30.089 76.113 29.645 1.00 34.24 ? 617 LYS A O 1 ATOM 4615 C CB . LYS A 1 563 ? 29.832 73.974 31.804 1.00 36.52 ? 617 LYS A CB 1 ATOM 4616 C CG . LYS A 1 563 ? 30.874 73.181 32.605 1.00 40.36 ? 617 LYS A CG 1 ATOM 4617 C CD . LYS A 1 563 ? 30.266 71.998 33.392 1.00 46.56 ? 617 LYS A CD 1 ATOM 4618 C CE . LYS A 1 563 ? 29.407 71.008 32.561 1.00 49.30 ? 617 LYS A CE 1 ATOM 4619 N NZ . LYS A 1 563 ? 27.960 71.430 32.424 1.00 50.47 ? 617 LYS A NZ 1 ATOM 4620 N N . HIS A 1 564 ? 28.416 77.016 30.903 1.00 31.50 ? 618 HIS A N 1 ATOM 4621 C CA . HIS A 1 564 ? 27.792 77.735 29.785 1.00 31.20 ? 618 HIS A CA 1 ATOM 4622 C C . HIS A 1 564 ? 27.639 79.244 30.125 1.00 30.37 ? 618 HIS A C 1 ATOM 4623 O O . HIS A 1 564 ? 26.524 79.784 30.119 1.00 29.13 ? 618 HIS A O 1 ATOM 4624 C CB . HIS A 1 564 ? 26.418 77.136 29.450 1.00 30.11 ? 618 HIS A CB 1 ATOM 4625 C CG . HIS A 1 564 ? 26.387 75.634 29.393 1.00 31.75 ? 618 HIS A CG 1 ATOM 4626 N ND1 . HIS A 1 564 ? 26.664 74.924 28.249 1.00 33.60 ? 618 HIS A ND1 1 ATOM 4627 C CD2 . HIS A 1 564 ? 26.042 74.713 30.332 1.00 32.75 ? 618 HIS A CD2 1 ATOM 4628 C CE1 . HIS A 1 564 ? 26.546 73.626 28.493 1.00 36.11 ? 618 HIS A CE1 1 ATOM 4629 N NE2 . HIS A 1 564 ? 26.162 73.470 29.749 1.00 35.16 ? 618 HIS A NE2 1 ATOM 4630 N N . PRO A 1 565 ? 28.769 79.920 30.419 1.00 31.46 ? 619 PRO A N 1 ATOM 4631 C CA . PRO A 1 565 ? 28.702 81.292 30.888 1.00 31.61 ? 619 PRO A CA 1 ATOM 4632 C C . PRO A 1 565 ? 27.988 82.210 29.916 1.00 31.91 ? 619 PRO A C 1 ATOM 4633 O O . PRO A 1 565 ? 27.228 83.074 30.361 1.00 29.83 ? 619 PRO A O 1 ATOM 4634 C CB . PRO A 1 565 ? 30.179 81.711 31.032 1.00 33.61 ? 619 PRO A CB 1 ATOM 4635 C CG . PRO A 1 565 ? 30.993 80.699 30.239 1.00 33.91 ? 619 PRO A CG 1 ATOM 4636 C CD . PRO A 1 565 ? 30.153 79.421 30.337 1.00 31.90 ? 619 PRO A CD 1 ATOM 4637 N N . GLN A 1 566 ? 28.237 82.066 28.606 1.00 32.61 ? 620 GLN A N 1 ATOM 4638 C CA A GLN A 1 566 ? 27.629 82.958 27.611 0.50 32.98 ? 620 GLN A CA 1 ATOM 4639 C CA B GLN A 1 566 ? 27.615 83.012 27.665 0.50 32.72 ? 620 GLN A CA 1 ATOM 4640 C C . GLN A 1 566 ? 26.110 82.857 27.672 1.00 32.10 ? 620 GLN A C 1 ATOM 4641 O O . GLN A 1 566 ? 25.391 83.868 27.645 1.00 31.43 ? 620 GLN A O 1 ATOM 4642 C CB A GLN A 1 566 ? 28.173 82.650 26.194 0.50 34.71 ? 620 GLN A CB 1 ATOM 4643 C CB B GLN A 1 566 ? 28.175 82.915 26.234 0.50 34.46 ? 620 GLN A CB 1 ATOM 4644 C CG A GLN A 1 566 ? 29.715 82.805 26.116 0.50 36.49 ? 620 GLN A CG 1 ATOM 4645 C CG B GLN A 1 566 ? 27.705 84.045 25.270 0.50 34.62 ? 620 GLN A CG 1 ATOM 4646 C CD A GLN A 1 566 ? 30.309 82.978 24.710 0.50 42.68 ? 620 GLN A CD 1 ATOM 4647 C CD B GLN A 1 566 ? 27.745 85.459 25.887 0.50 35.43 ? 620 GLN A CD 1 ATOM 4648 O OE1 A GLN A 1 566 ? 29.791 82.465 23.705 0.50 45.74 ? 620 GLN A OE1 1 ATOM 4649 O OE1 B GLN A 1 566 ? 28.817 86.054 26.070 0.50 40.53 ? 620 GLN A OE1 1 ATOM 4650 N NE2 A GLN A 1 566 ? 31.425 83.689 24.649 0.50 42.56 ? 620 GLN A NE2 1 ATOM 4651 N NE2 B GLN A 1 566 ? 26.573 85.998 26.190 0.50 32.95 ? 620 GLN A NE2 1 ATOM 4652 N N . GLU A 1 567 ? 25.610 81.614 27.739 1.00 30.00 ? 621 GLU A N 1 ATOM 4653 C CA . GLU A 1 567 ? 24.151 81.451 27.759 1.00 29.37 ? 621 GLU A CA 1 ATOM 4654 C C . GLU A 1 567 ? 23.553 81.957 29.054 1.00 28.05 ? 621 GLU A C 1 ATOM 4655 O O . GLU A 1 567 ? 22.439 82.519 29.060 1.00 27.67 ? 621 GLU A O 1 ATOM 4656 C CB . GLU A 1 567 ? 23.748 79.988 27.526 1.00 30.02 ? 621 GLU A CB 1 ATOM 4657 C CG . GLU A 1 567 ? 24.048 79.465 26.101 1.00 35.35 ? 621 GLU A CG 1 ATOM 4658 C CD . GLU A 1 567 ? 25.511 79.213 25.793 1.00 40.37 ? 621 GLU A CD 1 ATOM 4659 O OE1 . GLU A 1 567 ? 26.366 78.995 26.682 1.00 41.05 ? 621 GLU A OE1 1 ATOM 4660 O OE2 . GLU A 1 567 ? 25.827 79.246 24.591 1.00 48.49 ? 621 GLU A OE2 1 ATOM 4661 N N . MET A 1 568 ? 24.277 81.802 30.164 1.00 27.57 ? 622 MET A N 1 ATOM 4662 C CA . MET A 1 568 ? 23.734 82.314 31.427 1.00 27.70 ? 622 MET A CA 1 ATOM 4663 C C . MET A 1 568 ? 23.654 83.838 31.390 1.00 29.25 ? 622 MET A C 1 ATOM 4664 O O . MET A 1 568 ? 22.749 84.441 31.972 1.00 28.18 ? 622 MET A O 1 ATOM 4665 C CB . MET A 1 568 ? 24.572 81.857 32.639 1.00 27.90 ? 622 MET A CB 1 ATOM 4666 C CG . MET A 1 568 ? 24.488 80.320 32.910 1.00 26.86 ? 622 MET A CG 1 ATOM 4667 S SD . MET A 1 568 ? 25.466 79.872 34.379 1.00 30.14 ? 622 MET A SD 1 ATOM 4668 C CE . MET A 1 568 ? 24.582 80.701 35.717 1.00 28.24 ? 622 MET A CE 1 ATOM 4669 N N . LYS A 1 569 ? 24.606 84.469 30.696 1.00 28.34 ? 623 LYS A N 1 ATOM 4670 C CA . LYS A 1 569 ? 24.504 85.941 30.531 1.00 30.04 ? 623 LYS A CA 1 ATOM 4671 C C . LYS A 1 569 ? 23.318 86.348 29.629 1.00 29.51 ? 623 LYS A C 1 ATOM 4672 O O . LYS A 1 569 ? 22.501 87.215 29.986 1.00 29.35 ? 623 LYS A O 1 ATOM 4673 C CB . LYS A 1 569 ? 25.814 86.479 29.940 1.00 30.12 ? 623 LYS A CB 1 ATOM 4674 C CG . LYS A 1 569 ? 26.985 86.412 30.879 1.00 30.40 ? 623 LYS A CG 1 ATOM 4675 C CD . LYS A 1 569 ? 28.279 86.813 30.149 1.00 37.34 ? 623 LYS A CD 1 ATOM 4676 C CE . LYS A 1 569 ? 29.435 86.792 31.136 1.00 40.20 ? 623 LYS A CE 1 ATOM 4677 N NZ . LYS A 1 569 ? 30.623 85.985 30.771 1.00 44.01 ? 623 LYS A NZ 1 ATOM 4678 N N . THR A 1 570 ? 23.199 85.666 28.494 1.00 30.32 ? 624 THR A N 1 ATOM 4679 C CA . THR A 1 570 ? 22.187 85.978 27.492 1.00 31.96 ? 624 THR A CA 1 ATOM 4680 C C . THR A 1 570 ? 20.776 85.809 27.972 1.00 30.31 ? 624 THR A C 1 ATOM 4681 O O . THR A 1 570 ? 19.918 86.645 27.678 1.00 29.20 ? 624 THR A O 1 ATOM 4682 C CB . THR A 1 570 ? 22.392 85.122 26.190 1.00 33.43 ? 624 THR A CB 1 ATOM 4683 O OG1 . THR A 1 570 ? 23.668 85.439 25.650 1.00 38.08 ? 624 THR A OG1 1 ATOM 4684 C CG2 . THR A 1 570 ? 21.337 85.484 25.110 1.00 36.26 ? 624 THR A CG2 1 ATOM 4685 N N . TYR A 1 571 ? 20.529 84.706 28.705 1.00 28.99 ? 625 TYR A N 1 ATOM 4686 C CA . TYR A 1 571 ? 19.209 84.391 29.180 1.00 29.24 ? 625 TYR A CA 1 ATOM 4687 C C . TYR A 1 571 ? 19.025 84.756 30.650 1.00 28.89 ? 625 TYR A C 1 ATOM 4688 O O . TYR A 1 571 ? 18.024 84.387 31.228 1.00 28.83 ? 625 TYR A O 1 ATOM 4689 C CB . TYR A 1 571 ? 18.904 82.895 28.937 1.00 28.66 ? 625 TYR A CB 1 ATOM 4690 C CG . TYR A 1 571 ? 19.023 82.568 27.470 1.00 30.24 ? 625 TYR A CG 1 ATOM 4691 C CD1 . TYR A 1 571 ? 18.120 83.122 26.545 1.00 33.93 ? 625 TYR A CD1 1 ATOM 4692 C CD2 . TYR A 1 571 ? 20.069 81.779 26.992 1.00 33.02 ? 625 TYR A CD2 1 ATOM 4693 C CE1 . TYR A 1 571 ? 18.251 82.874 25.166 1.00 35.70 ? 625 TYR A CE1 1 ATOM 4694 C CE2 . TYR A 1 571 ? 20.197 81.514 25.644 1.00 36.35 ? 625 TYR A CE2 1 ATOM 4695 C CZ . TYR A 1 571 ? 19.280 82.064 24.737 1.00 38.29 ? 625 TYR A CZ 1 ATOM 4696 O OH . TYR A 1 571 ? 19.440 81.814 23.391 1.00 42.68 ? 625 TYR A OH 1 ATOM 4697 N N . SER A 1 572 ? 19.984 85.487 31.230 1.00 28.55 ? 626 SER A N 1 ATOM 4698 C CA . SER A 1 572 ? 19.839 85.992 32.601 1.00 27.53 ? 626 SER A CA 1 ATOM 4699 C C . SER A 1 572 ? 19.529 84.840 33.595 1.00 26.48 ? 626 SER A C 1 ATOM 4700 O O . SER A 1 572 ? 18.567 84.883 34.372 1.00 25.80 ? 626 SER A O 1 ATOM 4701 C CB A SER A 1 572 ? 18.781 87.093 32.686 0.65 27.72 ? 626 SER A CB 1 ATOM 4702 C CB B SER A 1 572 ? 18.742 87.051 32.653 0.35 28.04 ? 626 SER A CB 1 ATOM 4703 O OG A SER A 1 572 ? 19.200 88.202 31.913 0.65 25.18 ? 626 SER A OG 1 ATOM 4704 O OG B SER A 1 572 ? 18.654 87.583 33.946 0.35 30.31 ? 626 SER A OG 1 ATOM 4705 N N . VAL A 1 573 ? 20.366 83.813 33.543 1.00 25.54 ? 627 VAL A N 1 ATOM 4706 C CA . VAL A 1 573 ? 20.150 82.616 34.389 1.00 24.76 ? 627 VAL A CA 1 ATOM 4707 C C . VAL A 1 573 ? 20.815 82.850 35.738 1.00 25.85 ? 627 VAL A C 1 ATOM 4708 O O . VAL A 1 573 ? 22.043 82.822 35.818 1.00 28.02 ? 627 VAL A O 1 ATOM 4709 C CB . VAL A 1 573 ? 20.765 81.366 33.703 1.00 25.73 ? 627 VAL A CB 1 ATOM 4710 C CG1 . VAL A 1 573 ? 20.464 80.031 34.535 1.00 21.69 ? 627 VAL A CG1 1 ATOM 4711 C CG2 . VAL A 1 573 ? 20.210 81.268 32.280 1.00 23.35 ? 627 VAL A CG2 1 ATOM 4712 N N . SER A 1 574 ? 20.025 83.129 36.777 1.00 26.29 ? 628 SER A N 1 ATOM 4713 C CA . SER A 1 574 ? 20.610 83.373 38.092 1.00 27.32 ? 628 SER A CA 1 ATOM 4714 C C . SER A 1 574 ? 20.285 82.237 39.052 1.00 26.38 ? 628 SER A C 1 ATOM 4715 O O . SER A 1 574 ? 19.138 81.788 39.105 1.00 26.71 ? 628 SER A O 1 ATOM 4716 C CB . SER A 1 574 ? 20.061 84.667 38.689 1.00 28.90 ? 628 SER A CB 1 ATOM 4717 O OG . SER A 1 574 ? 20.693 84.900 39.942 1.00 31.28 ? 628 SER A OG 1 ATOM 4718 N N . PHE A 1 575 ? 21.273 81.802 39.821 1.00 26.39 ? 629 PHE A N 1 ATOM 4719 C CA . PHE A 1 575 ? 21.000 80.861 40.917 1.00 25.84 ? 629 PHE A CA 1 ATOM 4720 C C . PHE A 1 575 ? 20.791 81.582 42.243 1.00 25.80 ? 629 PHE A C 1 ATOM 4721 O O . PHE A 1 575 ? 20.744 80.942 43.294 1.00 24.40 ? 629 PHE A O 1 ATOM 4722 C CB . PHE A 1 575 ? 22.130 79.822 41.011 1.00 24.83 ? 629 PHE A CB 1 ATOM 4723 C CG . PHE A 1 575 ? 22.046 78.775 39.947 1.00 24.61 ? 629 PHE A CG 1 ATOM 4724 C CD1 . PHE A 1 575 ? 21.547 77.508 40.244 1.00 25.09 ? 629 PHE A CD1 1 ATOM 4725 C CD2 . PHE A 1 575 ? 22.493 79.042 38.645 1.00 27.11 ? 629 PHE A CD2 1 ATOM 4726 C CE1 . PHE A 1 575 ? 21.511 76.502 39.250 1.00 22.40 ? 629 PHE A CE1 1 ATOM 4727 C CE2 . PHE A 1 575 ? 22.452 78.058 37.633 1.00 26.48 ? 629 PHE A CE2 1 ATOM 4728 C CZ . PHE A 1 575 ? 21.941 76.756 37.959 1.00 27.56 ? 629 PHE A CZ 1 ATOM 4729 N N . ASP A 1 576 ? 20.642 82.923 42.195 1.00 26.33 ? 630 ASP A N 1 ATOM 4730 C CA . ASP A 1 576 ? 20.571 83.681 43.442 1.00 26.27 ? 630 ASP A CA 1 ATOM 4731 C C . ASP A 1 576 ? 19.436 83.208 44.349 1.00 25.36 ? 630 ASP A C 1 ATOM 4732 O O . ASP A 1 576 ? 19.604 83.146 45.576 1.00 24.55 ? 630 ASP A O 1 ATOM 4733 C CB . ASP A 1 576 ? 20.436 85.192 43.202 1.00 27.51 ? 630 ASP A CB 1 ATOM 4734 C CG . ASP A 1 576 ? 21.757 85.842 42.746 1.00 31.65 ? 630 ASP A CG 1 ATOM 4735 O OD1 . ASP A 1 576 ? 22.834 85.163 42.731 1.00 32.57 ? 630 ASP A OD1 1 ATOM 4736 O OD2 . ASP A 1 576 ? 21.683 87.065 42.388 1.00 36.38 ? 630 ASP A OD2 1 ATOM 4737 N N . SER A 1 577 ? 18.277 82.903 43.757 1.00 23.28 ? 631 SER A N 1 ATOM 4738 C CA . SER A 1 577 ? 17.138 82.507 44.561 1.00 23.39 ? 631 SER A CA 1 ATOM 4739 C C . SER A 1 577 ? 17.410 81.188 45.274 1.00 21.98 ? 631 SER A C 1 ATOM 4740 O O . SER A 1 577 ? 17.027 81.016 46.450 1.00 20.90 ? 631 SER A O 1 ATOM 4741 C CB . SER A 1 577 ? 15.849 82.387 43.733 1.00 23.73 ? 631 SER A CB 1 ATOM 4742 O OG . SER A 1 577 ? 15.993 81.416 42.695 1.00 25.05 ? 631 SER A OG 1 ATOM 4743 N N . LEU A 1 578 ? 18.067 80.271 44.587 1.00 21.38 ? 632 LEU A N 1 ATOM 4744 C CA . LEU A 1 578 ? 18.349 78.970 45.201 1.00 21.71 ? 632 LEU A CA 1 ATOM 4745 C C . LEU A 1 578 ? 19.352 79.095 46.374 1.00 22.62 ? 632 LEU A C 1 ATOM 4746 O O . LEU A 1 578 ? 19.119 78.548 47.469 1.00 20.96 ? 632 LEU A O 1 ATOM 4747 C CB . LEU A 1 578 ? 18.817 77.983 44.139 1.00 21.14 ? 632 LEU A CB 1 ATOM 4748 C CG . LEU A 1 578 ? 19.191 76.586 44.687 1.00 21.83 ? 632 LEU A CG 1 ATOM 4749 C CD1 . LEU A 1 578 ? 17.946 75.935 45.309 1.00 20.83 ? 632 LEU A CD1 1 ATOM 4750 C CD2 . LEU A 1 578 ? 19.745 75.692 43.560 1.00 20.53 ? 632 LEU A CD2 1 ATOM 4751 N N . PHE A 1 579 ? 20.432 79.871 46.175 1.00 22.43 ? 633 PHE A N 1 ATOM 4752 C CA . PHE A 1 579 ? 21.337 80.106 47.296 1.00 23.68 ? 633 PHE A CA 1 ATOM 4753 C C . PHE A 1 579 ? 20.675 80.835 48.460 1.00 24.07 ? 633 PHE A C 1 ATOM 4754 O O . PHE A 1 579 ? 20.961 80.518 49.627 1.00 24.13 ? 633 PHE A O 1 ATOM 4755 C CB . PHE A 1 579 ? 22.632 80.820 46.849 1.00 23.83 ? 633 PHE A CB 1 ATOM 4756 C CG . PHE A 1 579 ? 23.540 79.937 46.033 1.00 25.04 ? 633 PHE A CG 1 ATOM 4757 C CD1 . PHE A 1 579 ? 24.302 78.945 46.658 1.00 26.54 ? 633 PHE A CD1 1 ATOM 4758 C CD2 . PHE A 1 579 ? 23.602 80.072 44.647 1.00 26.77 ? 633 PHE A CD2 1 ATOM 4759 C CE1 . PHE A 1 579 ? 25.102 78.079 45.916 1.00 29.60 ? 633 PHE A CE1 1 ATOM 4760 C CE2 . PHE A 1 579 ? 24.433 79.237 43.883 1.00 29.60 ? 633 PHE A CE2 1 ATOM 4761 C CZ . PHE A 1 579 ? 25.176 78.240 44.523 1.00 29.14 ? 633 PHE A CZ 1 ATOM 4762 N N . SER A 1 580 ? 19.798 81.798 48.149 1.00 23.79 ? 634 SER A N 1 ATOM 4763 C CA . SER A 1 580 ? 19.031 82.516 49.182 1.00 24.91 ? 634 SER A CA 1 ATOM 4764 C C . SER A 1 580 ? 18.186 81.531 49.993 1.00 23.86 ? 634 SER A C 1 ATOM 4765 O O . SER A 1 580 ? 18.144 81.588 51.226 1.00 23.81 ? 634 SER A O 1 ATOM 4766 C CB . SER A 1 580 ? 18.127 83.608 48.559 1.00 25.03 ? 634 SER A CB 1 ATOM 4767 O OG . SER A 1 580 ? 17.355 84.237 49.569 1.00 25.97 ? 634 SER A OG 1 ATOM 4768 N N . ALA A 1 581 ? 17.493 80.618 49.301 1.00 22.44 ? 635 ALA A N 1 ATOM 4769 C CA . ALA A 1 581 ? 16.627 79.665 50.001 1.00 22.32 ? 635 ALA A CA 1 ATOM 4770 C C . ALA A 1 581 ? 17.492 78.757 50.897 1.00 21.87 ? 635 ALA A C 1 ATOM 4771 O O . ALA A 1 581 ? 17.093 78.416 52.042 1.00 23.64 ? 635 ALA A O 1 ATOM 4772 C CB . ALA A 1 581 ? 15.835 78.786 48.956 1.00 20.79 ? 635 ALA A CB 1 ATOM 4773 N N . VAL A 1 582 ? 18.658 78.362 50.382 1.00 23.03 ? 636 VAL A N 1 ATOM 4774 C CA . VAL A 1 582 ? 19.571 77.428 51.123 1.00 22.31 ? 636 VAL A CA 1 ATOM 4775 C C . VAL A 1 582 ? 20.079 78.151 52.364 1.00 23.32 ? 636 VAL A C 1 ATOM 4776 O O . VAL A 1 582 ? 20.142 77.588 53.442 1.00 23.20 ? 636 VAL A O 1 ATOM 4777 C CB . VAL A 1 582 ? 20.685 76.901 50.254 1.00 22.99 ? 636 VAL A CB 1 ATOM 4778 C CG1 . VAL A 1 582 ? 21.793 76.217 51.075 1.00 22.55 ? 636 VAL A CG1 1 ATOM 4779 C CG2 . VAL A 1 582 ? 20.092 75.918 49.192 1.00 22.25 ? 636 VAL A CG2 1 ATOM 4780 N N . LYS A 1 583 ? 20.412 79.420 52.199 1.00 23.53 ? 637 LYS A N 1 ATOM 4781 C CA . LYS A 1 583 ? 20.861 80.262 53.342 1.00 25.16 ? 637 LYS A CA 1 ATOM 4782 C C . LYS A 1 583 ? 19.774 80.388 54.397 1.00 24.51 ? 637 LYS A C 1 ATOM 4783 O O . LYS A 1 583 ? 20.021 80.242 55.615 1.00 24.86 ? 637 LYS A O 1 ATOM 4784 C CB . LYS A 1 583 ? 21.275 81.662 52.810 1.00 25.87 ? 637 LYS A CB 1 ATOM 4785 C CG . LYS A 1 583 ? 21.649 82.703 53.948 1.00 30.33 ? 637 LYS A CG 1 ATOM 4786 C CD . LYS A 1 583 ? 22.044 84.054 53.298 1.00 37.44 ? 637 LYS A CD 1 ATOM 4787 C CE . LYS A 1 583 ? 22.500 85.092 54.354 1.00 42.06 ? 637 LYS A CE 1 ATOM 4788 N NZ . LYS A 1 583 ? 21.305 85.431 55.214 1.00 45.20 ? 637 LYS A NZ 1 ATOM 4789 N N . ASN A 1 584 ? 18.541 80.663 53.963 1.00 22.95 ? 638 ASN A N 1 ATOM 4790 C CA . ASN A 1 584 ? 17.430 80.725 54.881 1.00 24.06 ? 638 ASN A CA 1 ATOM 4791 C C . ASN A 1 584 ? 17.166 79.399 55.588 1.00 23.39 ? 638 ASN A C 1 ATOM 4792 O O . ASN A 1 584 ? 16.941 79.375 56.814 1.00 23.06 ? 638 ASN A O 1 ATOM 4793 C CB . ASN A 1 584 ? 16.155 81.158 54.150 1.00 22.76 ? 638 ASN A CB 1 ATOM 4794 C CG . ASN A 1 584 ? 16.227 82.589 53.680 1.00 27.45 ? 638 ASN A CG 1 ATOM 4795 O OD1 . ASN A 1 584 ? 17.156 83.352 54.052 1.00 25.05 ? 638 ASN A OD1 1 ATOM 4796 N ND2 . ASN A 1 584 ? 15.275 82.973 52.868 1.00 26.01 ? 638 ASN A ND2 1 ATOM 4797 N N . PHE A 1 585 ? 17.262 78.293 54.842 1.00 22.86 ? 639 PHE A N 1 ATOM 4798 C CA . PHE A 1 585 ? 17.069 76.971 55.420 1.00 21.87 ? 639 PHE A CA 1 ATOM 4799 C C . PHE A 1 585 ? 18.120 76.782 56.530 1.00 23.09 ? 639 PHE A C 1 ATOM 4800 O O . PHE A 1 585 ? 17.793 76.278 57.620 1.00 23.17 ? 639 PHE A O 1 ATOM 4801 C CB . PHE A 1 585 ? 17.220 75.857 54.347 1.00 20.95 ? 639 PHE A CB 1 ATOM 4802 C CG . PHE A 1 585 ? 16.828 74.489 54.828 1.00 22.07 ? 639 PHE A CG 1 ATOM 4803 C CD1 . PHE A 1 585 ? 15.579 73.950 54.461 1.00 22.25 ? 639 PHE A CD1 1 ATOM 4804 C CD2 . PHE A 1 585 ? 17.681 73.728 55.662 1.00 22.09 ? 639 PHE A CD2 1 ATOM 4805 C CE1 . PHE A 1 585 ? 15.175 72.683 54.902 1.00 22.56 ? 639 PHE A CE1 1 ATOM 4806 C CE2 . PHE A 1 585 ? 17.304 72.443 56.096 1.00 20.40 ? 639 PHE A CE2 1 ATOM 4807 C CZ . PHE A 1 585 ? 16.023 71.923 55.735 1.00 22.08 ? 639 PHE A CZ 1 ATOM 4808 N N . THR A 1 586 ? 19.369 77.178 56.244 1.00 23.75 ? 640 THR A N 1 ATOM 4809 C CA . THR A 1 586 ? 20.477 77.027 57.207 1.00 24.83 ? 640 THR A CA 1 ATOM 4810 C C . THR A 1 586 ? 20.149 77.805 58.512 1.00 26.02 ? 640 THR A C 1 ATOM 4811 O O . THR A 1 586 ? 20.262 77.270 59.618 1.00 24.99 ? 640 THR A O 1 ATOM 4812 C CB . THR A 1 586 ? 21.811 77.438 56.572 1.00 25.83 ? 640 THR A CB 1 ATOM 4813 O OG1 . THR A 1 586 ? 22.023 76.672 55.366 1.00 26.64 ? 640 THR A OG1 1 ATOM 4814 C CG2 . THR A 1 586 ? 23.045 77.170 57.557 1.00 24.81 ? 640 THR A CG2 1 ATOM 4815 N N . GLU A 1 587 ? 19.703 79.048 58.358 1.00 26.35 ? 641 GLU A N 1 ATOM 4816 C CA . GLU A 1 587 ? 19.412 79.924 59.524 1.00 28.64 ? 641 GLU A CA 1 ATOM 4817 C C . GLU A 1 587 ? 18.221 79.396 60.309 1.00 27.13 ? 641 GLU A C 1 ATOM 4818 O O . GLU A 1 587 ? 18.281 79.270 61.538 1.00 25.92 ? 641 GLU A O 1 ATOM 4819 C CB . GLU A 1 587 ? 19.157 81.359 59.039 1.00 29.03 ? 641 GLU A CB 1 ATOM 4820 C CG . GLU A 1 587 ? 20.404 81.905 58.379 1.00 36.86 ? 641 GLU A CG 1 ATOM 4821 C CD . GLU A 1 587 ? 20.299 83.356 57.971 1.00 43.40 ? 641 GLU A CD 1 ATOM 4822 O OE1 . GLU A 1 587 ? 21.329 83.910 57.523 1.00 48.30 ? 641 GLU A OE1 1 ATOM 4823 O OE2 . GLU A 1 587 ? 19.196 83.920 58.096 1.00 46.34 ? 641 GLU A OE2 1 ATOM 4824 N N . ILE A 1 588 ? 17.143 79.031 59.590 1.00 25.37 ? 642 ILE A N 1 ATOM 4825 C CA . ILE A 1 588 ? 15.940 78.546 60.237 1.00 24.79 ? 642 ILE A CA 1 ATOM 4826 C C . ILE A 1 588 ? 16.210 77.214 60.934 1.00 24.34 ? 642 ILE A C 1 ATOM 4827 O O . ILE A 1 588 ? 15.736 77.009 62.045 1.00 24.40 ? 642 ILE A O 1 ATOM 4828 C CB . ILE A 1 588 ? 14.706 78.450 59.234 1.00 23.20 ? 642 ILE A CB 1 ATOM 4829 C CG1 . ILE A 1 588 ? 14.336 79.874 58.776 1.00 24.14 ? 642 ILE A CG1 1 ATOM 4830 C CG2 . ILE A 1 588 ? 13.481 77.780 59.884 1.00 24.93 ? 642 ILE A CG2 1 ATOM 4831 C CD1 . ILE A 1 588 ? 13.267 79.887 57.662 1.00 23.31 ? 642 ILE A CD1 1 ATOM 4832 N N . ALA A 1 589 ? 16.921 76.305 60.273 1.00 24.17 ? 643 ALA A N 1 ATOM 4833 C CA . ALA A 1 589 ? 17.214 74.994 60.899 1.00 24.43 ? 643 ALA A CA 1 ATOM 4834 C C . ALA A 1 589 ? 18.063 75.196 62.163 1.00 26.13 ? 643 ALA A C 1 ATOM 4835 O O . ALA A 1 589 ? 17.876 74.492 63.188 1.00 25.62 ? 643 ALA A O 1 ATOM 4836 C CB . ALA A 1 589 ? 17.941 74.078 59.924 1.00 24.40 ? 643 ALA A CB 1 ATOM 4837 N N . SER A 1 590 ? 19.006 76.138 62.079 1.00 26.79 ? 644 SER A N 1 ATOM 4838 C CA . SER A 1 590 ? 19.858 76.444 63.256 1.00 30.29 ? 644 SER A CA 1 ATOM 4839 C C . SER A 1 590 ? 18.967 76.896 64.433 1.00 29.11 ? 644 SER A C 1 ATOM 4840 O O . SER A 1 590 ? 19.110 76.383 65.553 1.00 30.73 ? 644 SER A O 1 ATOM 4841 C CB . SER A 1 590 ? 20.915 77.514 62.930 1.00 31.55 ? 644 SER A CB 1 ATOM 4842 O OG . SER A 1 590 ? 21.722 77.768 64.082 1.00 39.85 ? 644 SER A OG 1 ATOM 4843 N N . LYS A 1 591 ? 18.026 77.800 64.187 1.00 28.48 ? 645 LYS A N 1 ATOM 4844 C CA A LYS A 1 591 ? 17.121 78.265 65.247 0.50 28.44 ? 645 LYS A CA 1 ATOM 4845 C CA B LYS A 1 591 ? 17.115 78.266 65.244 0.50 28.26 ? 645 LYS A CA 1 ATOM 4846 C C . LYS A 1 591 ? 16.200 77.156 65.757 1.00 27.81 ? 645 LYS A C 1 ATOM 4847 O O . LYS A 1 591 ? 15.923 77.054 66.956 1.00 25.94 ? 645 LYS A O 1 ATOM 4848 C CB A LYS A 1 591 ? 16.339 79.502 64.787 0.50 29.36 ? 645 LYS A CB 1 ATOM 4849 C CB B LYS A 1 591 ? 16.309 79.487 64.782 0.50 28.94 ? 645 LYS A CB 1 ATOM 4850 C CG A LYS A 1 591 ? 17.273 80.699 64.570 0.50 31.96 ? 645 LYS A CG 1 ATOM 4851 C CG B LYS A 1 591 ? 17.156 80.761 64.742 0.50 30.99 ? 645 LYS A CG 1 ATOM 4852 C CD A LYS A 1 591 ? 16.641 81.832 63.798 0.50 36.19 ? 645 LYS A CD 1 ATOM 4853 C CD B LYS A 1 591 ? 17.555 81.170 66.160 0.50 32.00 ? 645 LYS A CD 1 ATOM 4854 C CE A LYS A 1 591 ? 17.643 83.000 63.664 0.50 38.18 ? 645 LYS A CE 1 ATOM 4855 C CE B LYS A 1 591 ? 18.830 82.014 66.177 0.50 36.63 ? 645 LYS A CE 1 ATOM 4856 N NZ A LYS A 1 591 ? 17.257 84.015 62.639 0.50 38.46 ? 645 LYS A NZ 1 ATOM 4857 N NZ B LYS A 1 591 ? 18.899 82.933 65.011 0.50 35.86 ? 645 LYS A NZ 1 ATOM 4858 N N . PHE A 1 592 ? 15.715 76.302 64.847 1.00 24.90 ? 646 PHE A N 1 ATOM 4859 C CA . PHE A 1 592 ? 14.869 75.209 65.266 1.00 24.62 ? 646 PHE A CA 1 ATOM 4860 C C . PHE A 1 592 ? 15.623 74.236 66.169 1.00 25.07 ? 646 PHE A C 1 ATOM 4861 O O . PHE A 1 592 ? 15.078 73.735 67.182 1.00 27.23 ? 646 PHE A O 1 ATOM 4862 C CB . PHE A 1 592 ? 14.350 74.439 64.010 1.00 23.76 ? 646 PHE A CB 1 ATOM 4863 C CG . PHE A 1 592 ? 13.521 73.206 64.338 1.00 23.08 ? 646 PHE A CG 1 ATOM 4864 C CD1 . PHE A 1 592 ? 12.131 73.299 64.554 1.00 22.70 ? 646 PHE A CD1 1 ATOM 4865 C CD2 . PHE A 1 592 ? 14.131 71.969 64.455 1.00 25.58 ? 646 PHE A CD2 1 ATOM 4866 C CE1 . PHE A 1 592 ? 11.378 72.154 64.856 1.00 24.91 ? 646 PHE A CE1 1 ATOM 4867 C CE2 . PHE A 1 592 ? 13.368 70.787 64.751 1.00 26.43 ? 646 PHE A CE2 1 ATOM 4868 C CZ . PHE A 1 592 ? 11.996 70.889 64.944 1.00 25.85 ? 646 PHE A CZ 1 ATOM 4869 N N . SER A 1 593 ? 16.863 73.945 65.823 1.00 25.57 ? 647 SER A N 1 ATOM 4870 C CA . SER A 1 593 ? 17.657 73.045 66.660 1.00 28.15 ? 647 SER A CA 1 ATOM 4871 C C . SER A 1 593 ? 17.835 73.608 68.093 1.00 29.56 ? 647 SER A C 1 ATOM 4872 O O . SER A 1 593 ? 17.844 72.823 69.073 1.00 29.10 ? 647 SER A O 1 ATOM 4873 C CB . SER A 1 593 ? 19.033 72.807 66.068 1.00 28.98 ? 647 SER A CB 1 ATOM 4874 O OG A SER A 1 593 ? 18.958 72.423 64.713 0.50 29.34 ? 647 SER A OG 1 ATOM 4875 O OG B SER A 1 593 ? 19.697 71.735 66.731 0.50 29.10 ? 647 SER A OG 1 ATOM 4876 N N . GLU A 1 594 ? 18.023 74.921 68.183 1.00 29.88 ? 648 GLU A N 1 ATOM 4877 C CA . GLU A 1 594 ? 18.086 75.620 69.493 1.00 33.17 ? 648 GLU A CA 1 ATOM 4878 C C . GLU A 1 594 ? 16.787 75.381 70.293 1.00 33.21 ? 648 GLU A C 1 ATOM 4879 O O . GLU A 1 594 ? 16.844 74.971 71.487 1.00 33.30 ? 648 GLU A O 1 ATOM 4880 C CB . GLU A 1 594 ? 18.308 77.121 69.344 1.00 34.29 ? 648 GLU A CB 1 ATOM 4881 C CG . GLU A 1 594 ? 19.614 77.534 68.663 1.00 41.46 ? 648 GLU A CG 1 ATOM 4882 C CD . GLU A 1 594 ? 19.949 79.055 68.785 1.00 48.48 ? 648 GLU A CD 1 ATOM 4883 O OE1 . GLU A 1 594 ? 19.051 79.929 68.929 1.00 48.67 ? 648 GLU A OE1 1 ATOM 4884 O OE2 . GLU A 1 594 ? 21.155 79.378 68.711 1.00 55.63 ? 648 GLU A OE2 1 ATOM 4885 N N . ARG A 1 595 ? 15.626 75.579 69.643 1.00 30.27 ? 649 ARG A N 1 ATOM 4886 C CA . ARG A 1 595 ? 14.352 75.348 70.326 1.00 30.39 ? 649 ARG A CA 1 ATOM 4887 C C . ARG A 1 595 ? 14.163 73.905 70.747 1.00 30.95 ? 649 ARG A C 1 ATOM 4888 O O . ARG A 1 595 ? 13.617 73.609 71.821 1.00 30.59 ? 649 ARG A O 1 ATOM 4889 C CB . ARG A 1 595 ? 13.169 75.837 69.488 1.00 30.04 ? 649 ARG A CB 1 ATOM 4890 C CG . ARG A 1 595 ? 13.176 77.329 69.221 1.00 30.93 ? 649 ARG A CG 1 ATOM 4891 C CD . ARG A 1 595 ? 11.793 77.852 68.776 1.00 28.94 ? 649 ARG A CD 1 ATOM 4892 N NE . ARG A 1 595 ? 11.260 77.095 67.644 1.00 25.94 ? 649 ARG A NE 1 ATOM 4893 C CZ . ARG A 1 595 ? 11.621 77.304 66.380 1.00 29.29 ? 649 ARG A CZ 1 ATOM 4894 N NH1 . ARG A 1 595 ? 12.548 78.242 66.107 1.00 27.05 ? 649 ARG A NH1 1 ATOM 4895 N NH2 . ARG A 1 595 ? 11.077 76.564 65.390 1.00 25.10 ? 649 ARG A NH2 1 ATOM 4896 N N . LEU A 1 596 ? 14.652 72.983 69.918 1.00 31.26 ? 650 LEU A N 1 ATOM 4897 C CA . LEU A 1 596 ? 14.493 71.571 70.174 1.00 33.39 ? 650 LEU A CA 1 ATOM 4898 C C . LEU A 1 596 ? 15.312 71.161 71.410 1.00 36.63 ? 650 LEU A C 1 ATOM 4899 O O . LEU A 1 596 ? 14.921 70.246 72.134 1.00 36.17 ? 650 LEU A O 1 ATOM 4900 C CB . LEU A 1 596 ? 14.947 70.760 68.936 1.00 32.33 ? 650 LEU A CB 1 ATOM 4901 C CG . LEU A 1 596 ? 14.543 69.306 68.798 1.00 32.31 ? 650 LEU A CG 1 ATOM 4902 C CD1 . LEU A 1 596 ? 13.058 69.151 68.551 1.00 31.47 ? 650 LEU A CD1 1 ATOM 4903 C CD2 . LEU A 1 596 ? 15.396 68.621 67.628 1.00 32.88 ? 650 LEU A CD2 1 ATOM 4904 N N . GLN A 1 597 ? 16.434 71.843 71.625 1.00 39.83 ? 651 GLN A N 1 ATOM 4905 C CA . GLN A 1 597 ? 17.291 71.565 72.775 1.00 45.24 ? 651 GLN A CA 1 ATOM 4906 C C . GLN A 1 597 ? 16.719 72.240 74.014 1.00 45.98 ? 651 GLN A C 1 ATOM 4907 O O . GLN A 1 597 ? 16.772 71.655 75.089 1.00 48.45 ? 651 GLN A O 1 ATOM 4908 C CB . GLN A 1 597 ? 18.746 71.949 72.487 1.00 45.90 ? 651 GLN A CB 1 ATOM 4909 C CG . GLN A 1 597 ? 19.329 70.925 71.505 1.00 50.97 ? 651 GLN A CG 1 ATOM 4910 C CD . GLN A 1 597 ? 20.840 70.956 71.331 1.00 57.23 ? 651 GLN A CD 1 ATOM 4911 O OE1 . GLN A 1 597 ? 21.602 71.069 72.309 1.00 59.57 ? 651 GLN A OE1 1 ATOM 4912 N NE2 . GLN A 1 597 ? 21.291 70.812 70.069 1.00 56.71 ? 651 GLN A NE2 1 ATOM 4913 N N . ASP A 1 598 ? 16.112 73.419 73.821 1.00 46.78 ? 652 ASP A N 1 ATOM 4914 C CA . ASP A 1 598 ? 15.641 74.333 74.888 1.00 48.00 ? 652 ASP A CA 1 ATOM 4915 C C . ASP A 1 598 ? 14.196 74.196 75.408 1.00 47.53 ? 652 ASP A C 1 ATOM 4916 O O . ASP A 1 598 ? 13.765 75.066 76.140 1.00 47.15 ? 652 ASP A O 1 ATOM 4917 C CB . ASP A 1 598 ? 15.809 75.809 74.460 1.00 48.19 ? 652 ASP A CB 1 ATOM 4918 C CG . ASP A 1 598 ? 17.281 76.276 74.435 1.00 52.11 ? 652 ASP A CG 1 ATOM 4919 O OD1 . ASP A 1 598 ? 17.515 77.451 74.040 1.00 56.58 ? 652 ASP A OD1 1 ATOM 4920 O OD2 . ASP A 1 598 ? 18.192 75.492 74.782 1.00 52.24 ? 652 ASP A OD2 1 ATOM 4921 N N . PHE A 1 599 ? 13.443 73.153 75.028 1.00 47.65 ? 653 PHE A N 1 ATOM 4922 C CA . PHE A 1 599 ? 12.081 72.895 75.608 1.00 46.37 ? 653 PHE A CA 1 ATOM 4923 C C . PHE A 1 599 ? 12.129 71.618 76.501 1.00 48.51 ? 653 PHE A C 1 ATOM 4924 O O . PHE A 1 599 ? 11.188 71.266 77.304 1.00 51.46 ? 653 PHE A O 1 ATOM 4925 C CB . PHE A 1 599 ? 11.044 72.769 74.450 1.00 45.50 ? 653 PHE A CB 1 ATOM 4926 C CG . PHE A 1 599 ? 10.885 71.363 73.941 1.00 37.88 ? 653 PHE A CG 1 ATOM 4927 C CD1 . PHE A 1 599 ? 9.787 70.601 74.315 1.00 33.97 ? 653 PHE A CD1 1 ATOM 4928 C CD2 . PHE A 1 599 ? 11.866 70.786 73.143 1.00 38.01 ? 653 PHE A CD2 1 ATOM 4929 C CE1 . PHE A 1 599 ? 9.636 69.307 73.893 1.00 36.65 ? 653 PHE A CE1 1 ATOM 4930 C CE2 . PHE A 1 599 ? 11.753 69.465 72.712 1.00 38.67 ? 653 PHE A CE2 1 ATOM 4931 C CZ . PHE A 1 599 ? 10.623 68.721 73.068 1.00 39.54 ? 653 PHE A CZ 1 ATOM 4932 N N A SER A 1 602 ? 8.984 68.889 79.935 0.50 27.15 ? 656 SER A N 1 ATOM 4933 N N B SER A 1 602 ? 8.061 66.592 78.840 0.50 26.86 ? 656 SER A N 1 ATOM 4934 C CA A SER A 1 602 ? 7.627 68.561 80.341 0.50 27.00 ? 656 SER A CA 1 ATOM 4935 C CA B SER A 1 602 ? 6.927 65.952 79.560 0.50 26.47 ? 656 SER A CA 1 ATOM 4936 C C A SER A 1 602 ? 6.403 68.709 79.348 0.50 25.95 ? 656 SER A C 1 ATOM 4937 C C B SER A 1 602 ? 5.606 66.683 79.293 0.50 26.81 ? 656 SER A C 1 ATOM 4938 O O A SER A 1 602 ? 5.343 68.132 79.612 0.50 25.78 ? 656 SER A O 1 ATOM 4939 O O B SER A 1 602 ? 4.564 66.369 79.875 0.50 27.56 ? 656 SER A O 1 ATOM 4940 C CB A SER A 1 602 ? 7.351 69.321 81.647 0.50 24.46 ? 656 SER A CB 1 ATOM 4941 C CB B SER A 1 602 ? 7.211 65.825 81.096 0.50 24.95 ? 656 SER A CB 1 ATOM 4942 O OG A SER A 1 602 ? 6.801 70.563 81.345 0.50 27.06 ? 656 SER A OG 1 ATOM 4943 O OG B SER A 1 602 ? 6.660 67.002 81.675 0.50 28.89 ? 656 SER A OG 1 ATOM 4944 N N A ASN A 1 603 ? 6.512 69.420 78.216 0.50 25.61 ? 657 ASN A N 1 ATOM 4945 N N B ASN A 1 603 ? 5.631 67.643 78.373 0.50 27.04 ? 657 ASN A N 1 ATOM 4946 C CA A ASN A 1 603 ? 5.308 69.733 77.416 0.50 24.27 ? 657 ASN A CA 1 ATOM 4947 C CA B ASN A 1 603 ? 4.405 68.273 77.899 0.50 28.03 ? 657 ASN A CA 1 ATOM 4948 C C A ASN A 1 603 ? 5.137 68.840 76.173 0.50 23.98 ? 657 ASN A C 1 ATOM 4949 C C B ASN A 1 603 ? 4.006 67.496 76.625 0.50 27.35 ? 657 ASN A C 1 ATOM 4950 O O A ASN A 1 603 ? 5.891 68.973 75.202 0.50 21.93 ? 657 ASN A O 1 ATOM 4951 O O B ASN A 1 603 ? 4.619 67.656 75.569 0.50 26.82 ? 657 ASN A O 1 ATOM 4952 C CB A ASN A 1 603 ? 5.286 71.208 77.012 0.50 24.70 ? 657 ASN A CB 1 ATOM 4953 C CB B ASN A 1 603 ? 4.680 69.763 77.634 0.50 27.41 ? 657 ASN A CB 1 ATOM 4954 C CG A ASN A 1 603 ? 3.935 71.647 76.494 0.50 26.28 ? 657 ASN A CG 1 ATOM 4955 C CG B ASN A 1 603 ? 3.447 70.534 77.173 0.50 30.83 ? 657 ASN A CG 1 ATOM 4956 O OD1 A ASN A 1 603 ? 3.303 70.950 75.696 0.50 27.68 ? 657 ASN A OD1 1 ATOM 4957 O OD1 B ASN A 1 603 ? 2.676 70.053 76.343 0.50 33.61 ? 657 ASN A OD1 1 ATOM 4958 N ND2 A ASN A 1 603 ? 3.483 72.791 76.944 0.50 25.79 ? 657 ASN A ND2 1 ATOM 4959 N ND2 B ASN A 1 603 ? 3.288 71.761 77.676 0.50 28.90 ? 657 ASN A ND2 1 ATOM 4960 N N A PRO A 1 604 ? 4.154 67.917 76.205 0.50 23.29 ? 658 PRO A N 1 ATOM 4961 N N B PRO A 1 604 ? 3.008 66.600 76.725 0.50 27.57 ? 658 PRO A N 1 ATOM 4962 C CA A PRO A 1 604 ? 4.197 66.892 75.175 0.50 22.40 ? 658 PRO A CA 1 ATOM 4963 C CA B PRO A 1 604 ? 2.745 65.754 75.537 0.50 26.92 ? 658 PRO A CA 1 ATOM 4964 C C A PRO A 1 604 ? 3.595 67.421 73.878 0.50 22.23 ? 658 PRO A C 1 ATOM 4965 C C B PRO A 1 604 ? 2.377 66.489 74.218 0.50 26.34 ? 658 PRO A C 1 ATOM 4966 O O A PRO A 1 604 ? 3.784 66.784 72.844 0.50 21.19 ? 658 PRO A O 1 ATOM 4967 O O B PRO A 1 604 ? 2.920 66.118 73.162 0.50 25.73 ? 658 PRO A O 1 ATOM 4968 C CB A PRO A 1 604 ? 3.293 65.792 75.748 0.50 22.29 ? 658 PRO A CB 1 ATOM 4969 C CB B PRO A 1 604 ? 1.629 64.813 76.000 0.50 27.94 ? 658 PRO A CB 1 ATOM 4970 C CG A PRO A 1 604 ? 2.212 66.614 76.493 0.50 23.08 ? 658 PRO A CG 1 ATOM 4971 C CG B PRO A 1 604 ? 1.718 64.833 77.517 0.50 28.12 ? 658 PRO A CG 1 ATOM 4972 C CD A PRO A 1 604 ? 3.035 67.705 77.153 0.50 23.87 ? 658 PRO A CD 1 ATOM 4973 C CD B PRO A 1 604 ? 2.266 66.159 77.915 0.50 27.31 ? 658 PRO A CD 1 ATOM 4974 N N A ILE A 1 605 ? 2.852 68.530 73.955 0.50 22.71 ? 659 ILE A N 1 ATOM 4975 N N B ILE A 1 605 ? 1.497 67.489 74.241 0.50 25.57 ? 659 ILE A N 1 ATOM 4976 C CA A ILE A 1 605 ? 2.327 69.193 72.772 0.50 23.05 ? 659 ILE A CA 1 ATOM 4977 C CA B ILE A 1 605 ? 1.168 68.211 72.982 0.50 25.52 ? 659 ILE A CA 1 ATOM 4978 C C A ILE A 1 605 ? 3.432 69.879 72.002 0.50 22.59 ? 659 ILE A C 1 ATOM 4979 C C B ILE A 1 605 ? 2.313 69.050 72.427 0.50 25.03 ? 659 ILE A C 1 ATOM 4980 O O A ILE A 1 605 ? 3.478 69.769 70.796 0.50 19.96 ? 659 ILE A O 1 ATOM 4981 O O B ILE A 1 605 ? 2.531 69.091 71.209 0.50 23.71 ? 659 ILE A O 1 ATOM 4982 C CB A ILE A 1 605 ? 1.242 70.239 73.027 0.50 24.30 ? 659 ILE A CB 1 ATOM 4983 C CB B ILE A 1 605 ? -0.126 69.026 73.035 0.50 25.38 ? 659 ILE A CB 1 ATOM 4984 C CG1 A ILE A 1 605 ? 0.192 69.691 73.985 0.50 26.46 ? 659 ILE A CG1 1 ATOM 4985 C CG1 B ILE A 1 605 ? -1.294 68.075 73.061 0.50 27.70 ? 659 ILE A CG1 1 ATOM 4986 C CG2 A ILE A 1 605 ? 0.585 70.629 71.711 0.50 22.89 ? 659 ILE A CG2 1 ATOM 4987 C CG2 B ILE A 1 605 ? -0.247 69.933 71.813 0.50 25.31 ? 659 ILE A CG2 1 ATOM 4988 C CD1 A ILE A 1 605 ? 0.207 68.196 73.980 0.50 27.40 ? 659 ILE A CD1 1 ATOM 4989 C CD1 B ILE A 1 605 ? -0.973 66.778 72.406 0.50 28.80 ? 659 ILE A CD1 1 ATOM 4990 N N A VAL A 1 606 ? 4.306 70.587 72.701 0.50 21.41 ? 660 VAL A N 1 ATOM 4991 N N B VAL A 1 606 ? 3.050 69.735 73.291 0.50 24.02 ? 660 VAL A N 1 ATOM 4992 C CA A VAL A 1 606 ? 5.466 71.191 72.060 0.50 22.08 ? 660 VAL A CA 1 ATOM 4993 C CA B VAL A 1 606 ? 4.254 70.436 72.812 0.50 23.08 ? 660 VAL A CA 1 ATOM 4994 C C A VAL A 1 606 ? 6.380 70.128 71.452 0.50 21.68 ? 660 VAL A C 1 ATOM 4995 C C B VAL A 1 606 ? 5.276 69.452 72.190 0.50 23.38 ? 660 VAL A C 1 ATOM 4996 O O A VAL A 1 606 ? 6.873 70.285 70.331 0.50 20.26 ? 660 VAL A O 1 ATOM 4997 O O B VAL A 1 606 ? 5.844 69.725 71.114 0.50 22.19 ? 660 VAL A O 1 ATOM 4998 C CB A VAL A 1 606 ? 6.247 72.073 73.057 0.50 22.81 ? 660 VAL A CB 1 ATOM 4999 C CB B VAL A 1 606 ? 4.889 71.348 73.913 0.50 24.13 ? 660 VAL A CB 1 ATOM 5000 C CG1 A VAL A 1 606 ? 7.558 72.547 72.457 0.50 23.47 ? 660 VAL A CG1 1 ATOM 5001 C CG1 B VAL A 1 606 ? 6.341 71.781 73.551 0.50 22.86 ? 660 VAL A CG1 1 ATOM 5002 C CG2 A VAL A 1 606 ? 5.413 73.241 73.402 0.50 23.68 ? 660 VAL A CG2 1 ATOM 5003 C CG2 B VAL A 1 606 ? 3.993 72.527 74.198 0.50 24.50 ? 660 VAL A CG2 1 ATOM 5004 N N A LEU A 1 607 ? 6.620 69.059 72.214 0.50 21.67 ? 661 LEU A N 1 ATOM 5005 N N B LEU A 1 607 ? 5.485 68.297 72.827 0.50 22.56 ? 661 LEU A N 1 ATOM 5006 C CA A LEU A 1 607 ? 7.390 67.921 71.732 0.50 22.00 ? 661 LEU A CA 1 ATOM 5007 C CA B LEU A 1 607 ? 6.399 67.307 72.264 0.50 23.60 ? 661 LEU A CA 1 ATOM 5008 C C A LEU A 1 607 ? 6.808 67.336 70.456 0.50 22.14 ? 661 LEU A C 1 ATOM 5009 C C B LEU A 1 607 ? 5.886 66.831 70.886 0.50 22.70 ? 661 LEU A C 1 ATOM 5010 O O A LEU A 1 607 ? 7.531 67.149 69.505 0.50 20.86 ? 661 LEU A O 1 ATOM 5011 O O B LEU A 1 607 ? 6.659 66.575 69.969 0.50 21.07 ? 661 LEU A O 1 ATOM 5012 C CB A LEU A 1 607 ? 7.425 66.808 72.781 0.50 22.09 ? 661 LEU A CB 1 ATOM 5013 C CB B LEU A 1 607 ? 6.603 66.125 73.219 0.50 24.12 ? 661 LEU A CB 1 ATOM 5014 C CG A LEU A 1 607 ? 7.955 65.416 72.391 0.50 22.31 ? 661 LEU A CG 1 ATOM 5015 C CG B LEU A 1 607 ? 7.439 64.939 72.694 0.50 24.66 ? 661 LEU A CG 1 ATOM 5016 C CD1 A LEU A 1 607 ? 9.417 65.462 72.062 0.50 23.14 ? 661 LEU A CD1 1 ATOM 5017 C CD1 B LEU A 1 607 ? 8.800 65.393 72.175 0.50 23.83 ? 661 LEU A CD1 1 ATOM 5018 C CD2 A LEU A 1 607 ? 7.712 64.397 73.519 0.50 24.02 ? 661 LEU A CD2 1 ATOM 5019 C CD2 B LEU A 1 607 ? 7.586 63.902 73.798 0.50 24.81 ? 661 LEU A CD2 1 ATOM 5020 N N A ARG A 1 608 ? 5.524 66.989 70.494 0.50 22.71 ? 662 ARG A N 1 ATOM 5021 N N B ARG A 1 608 ? 4.574 66.712 70.742 0.50 22.78 ? 662 ARG A N 1 ATOM 5022 C CA A ARG A 1 608 ? 4.841 66.316 69.385 0.50 23.57 ? 662 ARG A CA 1 ATOM 5023 C CA B ARG A 1 608 ? 4.016 66.281 69.453 0.50 23.07 ? 662 ARG A CA 1 ATOM 5024 C C A ARG A 1 608 ? 4.687 67.309 68.245 0.50 23.52 ? 662 ARG A C 1 ATOM 5025 C C B ARG A 1 608 ? 4.329 67.257 68.283 0.50 23.03 ? 662 ARG A C 1 ATOM 5026 O O A ARG A 1 608 ? 4.888 66.935 67.104 0.50 22.18 ? 662 ARG A O 1 ATOM 5027 O O B ARG A 1 608 ? 4.622 66.820 67.187 0.50 21.73 ? 662 ARG A O 1 ATOM 5028 C CB A ARG A 1 608 ? 3.456 65.800 69.810 0.50 24.10 ? 662 ARG A CB 1 ATOM 5029 C CB B ARG A 1 608 ? 2.526 65.996 69.615 0.50 22.96 ? 662 ARG A CB 1 ATOM 5030 C CG A ARG A 1 608 ? 2.514 65.425 68.635 0.50 24.99 ? 662 ARG A CG 1 ATOM 5031 C CG B ARG A 1 608 ? 1.825 65.508 68.355 0.50 21.65 ? 662 ARG A CG 1 ATOM 5032 C CD A ARG A 1 608 ? 2.535 63.914 68.220 0.50 25.82 ? 662 ARG A CD 1 ATOM 5033 C CD B ARG A 1 608 ? 2.514 64.318 67.640 0.50 27.17 ? 662 ARG A CD 1 ATOM 5034 N NE A ARG A 1 608 ? 1.327 63.636 67.427 0.50 29.96 ? 662 ARG A NE 1 ATOM 5035 N NE B ARG A 1 608 ? 1.427 63.610 66.974 0.50 30.24 ? 662 ARG A NE 1 ATOM 5036 C CZ A ARG A 1 608 ? 0.787 62.440 67.206 0.50 24.58 ? 662 ARG A CZ 1 ATOM 5037 C CZ B ARG A 1 608 ? 1.115 62.339 67.168 0.50 28.60 ? 662 ARG A CZ 1 ATOM 5038 N NH1 A ARG A 1 608 ? 1.330 61.326 67.710 0.50 25.17 ? 662 ARG A NH1 1 ATOM 5039 N NH1 B ARG A 1 608 ? 1.866 61.565 67.949 0.50 29.47 ? 662 ARG A NH1 1 ATOM 5040 N NH2 A ARG A 1 608 ? -0.318 62.374 66.482 0.50 24.16 ? 662 ARG A NH2 1 ATOM 5041 N NH2 B ARG A 1 608 ? 0.062 61.846 66.545 0.50 30.39 ? 662 ARG A NH2 1 ATOM 5042 N N . MET A 1 609 ? 4.345 68.565 68.563 1.00 24.65 ? 663 MET A N 1 ATOM 5043 C CA . MET A 1 609 ? 4.543 69.651 67.550 1.00 24.82 ? 663 MET A CA 1 ATOM 5044 C C . MET A 1 609 ? 5.948 69.611 66.960 1.00 25.38 ? 663 MET A C 1 ATOM 5045 O O . MET A 1 609 ? 6.112 69.663 65.705 1.00 23.99 ? 663 MET A O 1 ATOM 5046 C CB A MET A 1 609 ? 4.360 71.058 68.169 0.50 24.76 ? 663 MET A CB 1 ATOM 5047 C CB B MET A 1 609 ? 4.083 71.015 68.130 0.50 25.47 ? 663 MET A CB 1 ATOM 5048 C CG A MET A 1 609 ? 4.854 72.229 67.276 0.50 22.43 ? 663 MET A CG 1 ATOM 5049 C CG B MET A 1 609 ? 2.578 70.965 68.604 0.50 23.86 ? 663 MET A CG 1 ATOM 5050 S SD A MET A 1 609 ? 4.583 73.884 68.012 0.50 22.68 ? 663 MET A SD 1 ATOM 5051 S SD B MET A 1 609 ? 1.666 72.517 69.046 0.50 28.42 ? 663 MET A SD 1 ATOM 5052 C CE A MET A 1 609 ? 6.014 73.936 69.097 0.50 27.48 ? 663 MET A CE 1 ATOM 5053 C CE B MET A 1 609 ? 2.433 72.928 70.680 0.50 21.63 ? 663 MET A CE 1 ATOM 5054 N N . MET A 1 610 ? 6.987 69.515 67.811 1.00 24.26 ? 664 MET A N 1 ATOM 5055 C CA . MET A 1 610 ? 8.329 69.511 67.279 1.00 24.62 ? 664 MET A CA 1 ATOM 5056 C C . MET A 1 610 ? 8.644 68.205 66.526 1.00 23.87 ? 664 MET A C 1 ATOM 5057 O O . MET A 1 610 ? 9.362 68.203 65.493 1.00 24.02 ? 664 MET A O 1 ATOM 5058 C CB A MET A 1 610 ? 9.331 69.561 68.465 0.50 26.21 ? 664 MET A CB 1 ATOM 5059 C CB B MET A 1 610 ? 9.416 69.948 68.276 0.50 25.24 ? 664 MET A CB 1 ATOM 5060 C CG A MET A 1 610 ? 9.090 70.657 69.484 0.50 28.66 ? 664 MET A CG 1 ATOM 5061 C CG B MET A 1 610 ? 9.300 71.418 68.611 0.50 24.54 ? 664 MET A CG 1 ATOM 5062 S SD A MET A 1 610 ? 9.216 72.222 68.654 0.50 34.73 ? 664 MET A SD 1 ATOM 5063 S SD B MET A 1 610 ? 10.670 72.142 69.514 0.50 25.37 ? 664 MET A SD 1 ATOM 5064 C CE A MET A 1 610 ? 10.975 72.562 68.803 0.50 33.47 ? 664 MET A CE 1 ATOM 5065 C CE B MET A 1 610 ? 11.732 72.656 68.158 0.50 22.80 ? 664 MET A CE 1 ATOM 5066 N N . ASN A 1 611 ? 8.150 67.102 67.069 1.00 22.61 ? 665 ASN A N 1 ATOM 5067 C CA . ASN A 1 611 ? 8.337 65.816 66.368 1.00 22.52 ? 665 ASN A CA 1 ATOM 5068 C C . ASN A 1 611 ? 7.575 65.827 65.031 1.00 22.37 ? 665 ASN A C 1 ATOM 5069 O O . ASN A 1 611 ? 8.032 65.258 64.076 1.00 22.93 ? 665 ASN A O 1 ATOM 5070 C CB . ASN A 1 611 ? 7.844 64.665 67.213 1.00 22.18 ? 665 ASN A CB 1 ATOM 5071 C CG . ASN A 1 611 ? 8.923 64.170 68.194 1.00 22.05 ? 665 ASN A CG 1 ATOM 5072 O OD1 . ASN A 1 611 ? 10.119 64.366 67.956 1.00 23.85 ? 665 ASN A OD1 1 ATOM 5073 N ND2 . ASN A 1 611 ? 8.505 63.497 69.250 1.00 21.07 ? 665 ASN A ND2 1 ATOM 5074 N N . ASP A 1 612 ? 6.397 66.420 65.002 1.00 22.66 ? 666 ASP A N 1 ATOM 5075 C CA . ASP A 1 612 ? 5.731 66.573 63.716 1.00 22.24 ? 666 ASP A CA 1 ATOM 5076 C C . ASP A 1 612 ? 6.564 67.400 62.740 1.00 22.46 ? 666 ASP A C 1 ATOM 5077 O O . ASP A 1 612 ? 6.599 67.089 61.537 1.00 21.53 ? 666 ASP A O 1 ATOM 5078 C CB . ASP A 1 612 ? 4.314 67.170 63.882 1.00 21.89 ? 666 ASP A CB 1 ATOM 5079 C CG . ASP A 1 612 ? 3.298 66.155 64.370 1.00 23.45 ? 666 ASP A CG 1 ATOM 5080 O OD1 . ASP A 1 612 ? 3.656 64.966 64.530 1.00 26.15 ? 666 ASP A OD1 1 ATOM 5081 O OD2 . ASP A 1 612 ? 2.130 66.530 64.552 1.00 24.19 ? 666 ASP A OD2 1 ATOM 5082 N N . GLN A 1 613 ? 7.146 68.519 63.200 1.00 20.84 ? 667 GLN A N 1 ATOM 5083 C CA . GLN A 1 613 ? 8.016 69.316 62.307 1.00 20.14 ? 667 GLN A CA 1 ATOM 5084 C C . GLN A 1 613 ? 9.165 68.492 61.810 1.00 21.68 ? 667 GLN A C 1 ATOM 5085 O O . GLN A 1 613 ? 9.502 68.544 60.647 1.00 21.09 ? 667 GLN A O 1 ATOM 5086 C CB . GLN A 1 613 ? 8.529 70.616 62.972 1.00 21.54 ? 667 GLN A CB 1 ATOM 5087 C CG . GLN A 1 613 ? 7.369 71.645 63.149 1.00 20.60 ? 667 GLN A CG 1 ATOM 5088 C CD . GLN A 1 613 ? 7.830 72.869 63.928 1.00 23.61 ? 667 GLN A CD 1 ATOM 5089 O OE1 . GLN A 1 613 ? 7.927 72.830 65.136 1.00 25.89 ? 667 GLN A OE1 1 ATOM 5090 N NE2 . GLN A 1 613 ? 8.079 73.967 63.225 1.00 21.45 ? 667 GLN A NE2 1 ATOM 5091 N N . LEU A 1 614 ? 9.757 67.657 62.668 1.00 21.62 ? 668 LEU A N 1 ATOM 5092 C CA . LEU A 1 614 ? 10.834 66.795 62.177 1.00 21.51 ? 668 LEU A CA 1 ATOM 5093 C C . LEU A 1 614 ? 10.369 65.725 61.173 1.00 20.22 ? 668 LEU A C 1 ATOM 5094 O O . LEU A 1 614 ? 11.031 65.483 60.149 1.00 20.82 ? 668 LEU A O 1 ATOM 5095 C CB . LEU A 1 614 ? 11.526 66.085 63.362 1.00 22.21 ? 668 LEU A CB 1 ATOM 5096 C CG . LEU A 1 614 ? 12.467 67.073 64.116 1.00 25.16 ? 668 LEU A CG 1 ATOM 5097 C CD1 . LEU A 1 614 ? 12.944 66.351 65.349 1.00 30.73 ? 668 LEU A CD1 1 ATOM 5098 C CD2 . LEU A 1 614 ? 13.618 67.548 63.248 1.00 26.36 ? 668 LEU A CD2 1 ATOM 5099 N N . MET A 1 615 ? 9.229 65.119 61.466 1.00 20.94 ? 669 MET A N 1 ATOM 5100 C CA . MET A 1 615 ? 8.666 64.040 60.588 1.00 21.75 ? 669 MET A CA 1 ATOM 5101 C C . MET A 1 615 ? 8.265 64.631 59.214 1.00 20.18 ? 669 MET A C 1 ATOM 5102 O O . MET A 1 615 ? 8.478 64.022 58.185 1.00 20.68 ? 669 MET A O 1 ATOM 5103 C CB . MET A 1 615 ? 7.383 63.498 61.243 1.00 20.78 ? 669 MET A CB 1 ATOM 5104 C CG . MET A 1 615 ? 6.747 62.369 60.453 1.00 26.44 ? 669 MET A CG 1 ATOM 5105 S SD . MET A 1 615 ? 5.306 61.619 61.217 1.00 27.33 ? 669 MET A SD 1 ATOM 5106 C CE . MET A 1 615 ? 4.053 62.864 61.030 1.00 28.05 ? 669 MET A CE 1 ATOM 5107 N N . PHE A 1 616 ? 7.643 65.793 59.236 1.00 19.71 ? 670 PHE A N 1 ATOM 5108 C CA . PHE A 1 616 ? 7.188 66.404 57.938 1.00 19.92 ? 670 PHE A CA 1 ATOM 5109 C C . PHE A 1 616 ? 8.242 67.168 57.173 1.00 20.39 ? 670 PHE A C 1 ATOM 5110 O O . PHE A 1 616 ? 7.942 67.692 56.068 1.00 20.61 ? 670 PHE A O 1 ATOM 5111 C CB . PHE A 1 616 ? 5.958 67.286 58.197 1.00 18.04 ? 670 PHE A CB 1 ATOM 5112 C CG . PHE A 1 616 ? 4.711 66.510 58.488 1.00 21.40 ? 670 PHE A CG 1 ATOM 5113 C CD1 . PHE A 1 616 ? 4.216 65.541 57.551 1.00 21.17 ? 670 PHE A CD1 1 ATOM 5114 C CD2 . PHE A 1 616 ? 3.978 66.768 59.658 1.00 22.09 ? 670 PHE A CD2 1 ATOM 5115 C CE1 . PHE A 1 616 ? 3.061 64.851 57.814 1.00 20.99 ? 670 PHE A CE1 1 ATOM 5116 C CE2 . PHE A 1 616 ? 2.796 66.088 59.929 1.00 22.59 ? 670 PHE A CE2 1 ATOM 5117 C CZ . PHE A 1 616 ? 2.340 65.092 59.009 1.00 23.14 ? 670 PHE A CZ 1 ATOM 5118 N N . LEU A 1 617 ? 9.485 67.221 57.695 1.00 20.08 ? 671 LEU A N 1 ATOM 5119 C CA . LEU A 1 617 ? 10.544 67.938 56.989 1.00 20.08 ? 671 LEU A CA 1 ATOM 5120 C C . LEU A 1 617 ? 10.924 67.201 55.681 1.00 19.18 ? 671 LEU A C 1 ATOM 5121 O O . LEU A 1 617 ? 10.959 67.809 54.617 1.00 18.42 ? 671 LEU A O 1 ATOM 5122 C CB . LEU A 1 617 ? 11.767 68.187 57.887 1.00 20.06 ? 671 LEU A CB 1 ATOM 5123 C CG . LEU A 1 617 ? 12.933 68.891 57.204 1.00 21.02 ? 671 LEU A CG 1 ATOM 5124 C CD1 . LEU A 1 617 ? 12.552 70.241 56.619 1.00 20.35 ? 671 LEU A CD1 1 ATOM 5125 C CD2 . LEU A 1 617 ? 14.049 69.086 58.247 1.00 24.38 ? 671 LEU A CD2 1 ATOM 5126 N N . GLU A 1 618 ? 11.126 65.890 55.743 1.00 17.31 ? 672 GLU A N 1 ATOM 5127 C CA . GLU A 1 618 ? 11.292 65.153 54.500 1.00 18.24 ? 672 GLU A CA 1 ATOM 5128 C C . GLU A 1 618 ? 10.090 65.351 53.563 1.00 18.35 ? 672 GLU A C 1 ATOM 5129 O O . GLU A 1 618 ? 10.264 65.452 52.323 1.00 18.34 ? 672 GLU A O 1 ATOM 5130 C CB . GLU A 1 618 ? 11.539 63.648 54.781 1.00 18.89 ? 672 GLU A CB 1 ATOM 5131 C CG . GLU A 1 618 ? 12.151 62.952 53.567 1.00 17.27 ? 672 GLU A CG 1 ATOM 5132 C CD . GLU A 1 618 ? 13.657 63.225 53.447 1.00 21.28 ? 672 GLU A CD 1 ATOM 5133 O OE1 . GLU A 1 618 ? 14.392 62.863 54.369 1.00 19.53 ? 672 GLU A OE1 1 ATOM 5134 O OE2 . GLU A 1 618 ? 14.089 63.888 52.463 1.00 19.18 ? 672 GLU A OE2 1 ATOM 5135 N N . ARG A 1 619 ? 8.906 65.379 54.151 1.00 17.77 ? 673 ARG A N 1 ATOM 5136 C CA . ARG A 1 619 ? 7.678 65.453 53.390 1.00 18.01 ? 673 ARG A CA 1 ATOM 5137 C C . ARG A 1 619 ? 7.663 66.774 52.614 1.00 17.87 ? 673 ARG A C 1 ATOM 5138 O O . ARG A 1 619 ? 7.161 66.825 51.511 1.00 17.44 ? 673 ARG A O 1 ATOM 5139 C CB . ARG A 1 619 ? 6.468 65.394 54.293 1.00 18.24 ? 673 ARG A CB 1 ATOM 5140 C CG . ARG A 1 619 ? 5.293 64.694 53.625 1.00 19.06 ? 673 ARG A CG 1 ATOM 5141 C CD . ARG A 1 619 ? 5.391 63.141 53.716 1.00 20.64 ? 673 ARG A CD 1 ATOM 5142 N NE . ARG A 1 619 ? 4.961 62.645 55.044 1.00 16.86 ? 673 ARG A NE 1 ATOM 5143 C CZ . ARG A 1 619 ? 5.759 62.107 55.973 1.00 19.29 ? 673 ARG A CZ 1 ATOM 5144 N NH1 . ARG A 1 619 ? 7.111 61.998 55.796 1.00 16.37 ? 673 ARG A NH1 1 ATOM 5145 N NH2 . ARG A 1 619 ? 5.206 61.688 57.109 1.00 20.08 ? 673 ARG A NH2 1 ATOM 5146 N N . ALA A 1 620 ? 8.256 67.811 53.183 1.00 16.78 ? 674 ALA A N 1 ATOM 5147 C CA . ALA A 1 620 ? 8.209 69.139 52.533 1.00 17.89 ? 674 ALA A CA 1 ATOM 5148 C C . ALA A 1 620 ? 8.999 69.209 51.235 1.00 18.49 ? 674 ALA A C 1 ATOM 5149 O O . ALA A 1 620 ? 8.766 70.139 50.411 1.00 18.88 ? 674 ALA A O 1 ATOM 5150 C CB . ALA A 1 620 ? 8.714 70.222 53.542 1.00 16.50 ? 674 ALA A CB 1 ATOM 5151 N N . PHE A 1 621 ? 9.907 68.255 51.003 1.00 17.07 ? 675 PHE A N 1 ATOM 5152 C CA . PHE A 1 621 ? 10.625 68.273 49.740 1.00 17.74 ? 675 PHE A CA 1 ATOM 5153 C C . PHE A 1 621 ? 9.846 67.648 48.562 1.00 17.22 ? 675 PHE A C 1 ATOM 5154 O O . PHE A 1 621 ? 10.332 67.653 47.428 1.00 17.61 ? 675 PHE A O 1 ATOM 5155 C CB . PHE A 1 621 ? 11.994 67.575 49.882 1.00 18.00 ? 675 PHE A CB 1 ATOM 5156 C CG . PHE A 1 621 ? 12.951 68.370 50.725 1.00 18.77 ? 675 PHE A CG 1 ATOM 5157 C CD1 . PHE A 1 621 ? 13.360 69.643 50.320 1.00 18.37 ? 675 PHE A CD1 1 ATOM 5158 C CD2 . PHE A 1 621 ? 13.360 67.866 51.960 1.00 18.73 ? 675 PHE A CD2 1 ATOM 5159 C CE1 . PHE A 1 621 ? 14.247 70.407 51.151 1.00 20.76 ? 675 PHE A CE1 1 ATOM 5160 C CE2 . PHE A 1 621 ? 14.232 68.644 52.802 1.00 20.71 ? 675 PHE A CE2 1 ATOM 5161 C CZ . PHE A 1 621 ? 14.660 69.887 52.379 1.00 21.54 ? 675 PHE A CZ 1 ATOM 5162 N N . ILE A 1 622 ? 8.658 67.103 48.831 1.00 17.76 ? 676 ILE A N 1 ATOM 5163 C CA . ILE A 1 622 ? 7.794 66.554 47.775 1.00 18.26 ? 676 ILE A CA 1 ATOM 5164 C C . ILE A 1 622 ? 7.077 67.720 47.001 1.00 18.15 ? 676 ILE A C 1 ATOM 5165 O O . ILE A 1 622 ? 6.501 68.627 47.616 1.00 18.87 ? 676 ILE A O 1 ATOM 5166 C CB . ILE A 1 622 ? 6.726 65.642 48.468 1.00 18.73 ? 676 ILE A CB 1 ATOM 5167 C CG1 . ILE A 1 622 ? 7.464 64.438 49.134 1.00 14.36 ? 676 ILE A CG1 1 ATOM 5168 C CG2 . ILE A 1 622 ? 5.610 65.203 47.504 1.00 18.75 ? 676 ILE A CG2 1 ATOM 5169 C CD1 . ILE A 1 622 ? 8.269 63.567 48.039 1.00 16.89 ? 676 ILE A CD1 1 ATOM 5170 N N . ASP A 1 623 ? 7.157 67.672 45.676 1.00 16.73 ? 677 ASP A N 1 ATOM 5171 C CA . ASP A 1 623 ? 6.344 68.540 44.814 1.00 17.10 ? 677 ASP A CA 1 ATOM 5172 C C . ASP A 1 623 ? 5.134 67.709 44.333 1.00 17.39 ? 677 ASP A C 1 ATOM 5173 O O . ASP A 1 623 ? 5.324 66.662 43.671 1.00 17.98 ? 677 ASP A O 1 ATOM 5174 C CB . ASP A 1 623 ? 7.186 68.963 43.603 1.00 16.95 ? 677 ASP A CB 1 ATOM 5175 C CG . ASP A 1 623 ? 6.503 70.044 42.780 1.00 17.55 ? 677 ASP A CG 1 ATOM 5176 O OD1 . ASP A 1 623 ? 5.233 70.081 42.801 1.00 18.81 ? 677 ASP A OD1 1 ATOM 5177 O OD2 . ASP A 1 623 ? 7.235 70.891 42.218 1.00 17.89 ? 677 ASP A OD2 1 ATOM 5178 N N . PRO A 1 624 ? 3.904 68.130 44.655 1.00 19.24 ? 678 PRO A N 1 ATOM 5179 C CA . PRO A 1 624 ? 2.772 67.286 44.252 1.00 20.58 ? 678 PRO A CA 1 ATOM 5180 C C . PRO A 1 624 ? 2.571 67.250 42.714 1.00 22.32 ? 678 PRO A C 1 ATOM 5181 O O . PRO A 1 624 ? 1.787 66.445 42.221 1.00 24.60 ? 678 PRO A O 1 ATOM 5182 C CB . PRO A 1 624 ? 1.554 67.983 44.949 1.00 20.56 ? 678 PRO A CB 1 ATOM 5183 C CG . PRO A 1 624 ? 1.965 69.411 45.065 1.00 20.74 ? 678 PRO A CG 1 ATOM 5184 C CD . PRO A 1 624 ? 3.482 69.366 45.365 1.00 19.43 ? 678 PRO A CD 1 ATOM 5185 N N . LEU A 1 625 ? 3.286 68.098 41.960 1.00 20.05 ? 679 LEU A N 1 ATOM 5186 C CA . LEU A 1 625 ? 3.246 68.053 40.496 1.00 19.29 ? 679 LEU A CA 1 ATOM 5187 C C . LEU A 1 625 ? 4.318 67.107 39.934 1.00 21.07 ? 679 LEU A C 1 ATOM 5188 O O . LEU A 1 625 ? 4.400 66.881 38.708 1.00 20.12 ? 679 LEU A O 1 ATOM 5189 C CB . LEU A 1 625 ? 3.419 69.479 39.940 1.00 19.12 ? 679 LEU A CB 1 ATOM 5190 C CG . LEU A 1 625 ? 2.325 70.503 40.383 1.00 16.54 ? 679 LEU A CG 1 ATOM 5191 C CD1 . LEU A 1 625 ? 2.452 71.833 39.659 1.00 19.35 ? 679 LEU A CD1 1 ATOM 5192 C CD2 . LEU A 1 625 ? 0.930 69.905 39.983 1.00 22.41 ? 679 LEU A CD2 1 ATOM 5193 N N . GLY A 1 626 ? 5.125 66.522 40.829 1.00 20.40 ? 680 GLY A N 1 ATOM 5194 C CA . GLY A 1 626 ? 6.186 65.597 40.385 1.00 21.66 ? 680 GLY A CA 1 ATOM 5195 C C . GLY A 1 626 ? 7.286 66.263 39.558 1.00 23.06 ? 680 GLY A C 1 ATOM 5196 O O . GLY A 1 626 ? 7.385 67.483 39.511 1.00 23.74 ? 680 GLY A O 1 ATOM 5197 N N A LEU A 1 627 ? 8.140 65.459 38.927 0.60 23.00 ? 681 LEU A N 1 ATOM 5198 N N B LEU A 1 627 ? 8.140 65.456 38.927 0.40 23.27 ? 681 LEU A N 1 ATOM 5199 C CA A LEU A 1 627 ? 9.081 65.994 37.949 0.60 24.11 ? 681 LEU A CA 1 ATOM 5200 C CA B LEU A 1 627 ? 9.128 65.957 37.967 0.40 24.37 ? 681 LEU A CA 1 ATOM 5201 C C A LEU A 1 627 ? 8.525 65.909 36.514 0.60 24.30 ? 681 LEU A C 1 ATOM 5202 C C B LEU A 1 627 ? 8.570 65.871 36.525 0.40 24.72 ? 681 LEU A C 1 ATOM 5203 O O A LEU A 1 627 ? 7.579 65.133 36.231 0.60 24.34 ? 681 LEU A O 1 ATOM 5204 O O B LEU A 1 627 ? 7.657 65.064 36.260 0.40 24.93 ? 681 LEU A O 1 ATOM 5205 C CB A LEU A 1 627 ? 10.424 65.257 38.078 0.60 23.52 ? 681 LEU A CB 1 ATOM 5206 C CB B LEU A 1 627 ? 10.425 65.139 38.113 0.40 23.67 ? 681 LEU A CB 1 ATOM 5207 C CG A LEU A 1 627 ? 11.156 65.454 39.414 0.60 24.54 ? 681 LEU A CG 1 ATOM 5208 C CG B LEU A 1 627 ? 11.512 65.607 39.101 0.40 24.91 ? 681 LEU A CG 1 ATOM 5209 C CD1 A LEU A 1 627 ? 12.316 64.520 39.452 0.60 25.35 ? 681 LEU A CD1 1 ATOM 5210 C CD1 B LEU A 1 627 ? 11.999 66.988 38.698 0.40 23.44 ? 681 LEU A CD1 1 ATOM 5211 C CD2 A LEU A 1 627 ? 11.658 66.900 39.602 0.60 25.58 ? 681 LEU A CD2 1 ATOM 5212 C CD2 B LEU A 1 627 ? 11.138 65.607 40.578 0.40 21.23 ? 681 LEU A CD2 1 ATOM 5213 N N . PRO A 1 628 ? 9.102 66.681 35.570 1.00 26.18 ? 682 PRO A N 1 ATOM 5214 C CA . PRO A 1 628 ? 8.552 66.641 34.204 1.00 26.73 ? 682 PRO A CA 1 ATOM 5215 C C . PRO A 1 628 ? 8.357 65.236 33.577 1.00 26.92 ? 682 PRO A C 1 ATOM 5216 O O . PRO A 1 628 ? 9.301 64.448 33.452 1.00 27.28 ? 682 PRO A O 1 ATOM 5217 C CB . PRO A 1 628 ? 9.566 67.503 33.391 1.00 28.66 ? 682 PRO A CB 1 ATOM 5218 C CG . PRO A 1 628 ? 9.985 68.503 34.381 1.00 27.79 ? 682 PRO A CG 1 ATOM 5219 C CD . PRO A 1 628 ? 10.236 67.638 35.626 1.00 26.86 ? 682 PRO A CD 1 ATOM 5220 N N . ASP A 1 629 ? 7.107 64.942 33.212 1.00 28.12 ? 683 ASP A N 1 ATOM 5221 C CA . ASP A 1 629 ? 6.712 63.644 32.639 1.00 29.39 ? 683 ASP A CA 1 ATOM 5222 C C . ASP A 1 629 ? 6.972 62.443 33.565 1.00 27.90 ? 683 ASP A C 1 ATOM 5223 O O . ASP A 1 629 ? 6.973 61.295 33.099 1.00 27.36 ? 683 ASP A O 1 ATOM 5224 C CB . ASP A 1 629 ? 7.462 63.377 31.327 1.00 31.54 ? 683 ASP A CB 1 ATOM 5225 C CG . ASP A 1 629 ? 7.221 64.481 30.304 1.00 37.76 ? 683 ASP A CG 1 ATOM 5226 O OD1 . ASP A 1 629 ? 6.033 64.816 30.084 1.00 40.11 ? 683 ASP A OD1 1 ATOM 5227 O OD2 . ASP A 1 629 ? 8.226 65.013 29.779 1.00 42.49 ? 683 ASP A OD2 1 ATOM 5228 N N . ARG A 1 630 ? 7.258 62.707 34.837 1.00 25.92 ? 684 ARG A N 1 ATOM 5229 C CA . ARG A 1 630 ? 7.538 61.596 35.818 1.00 24.66 ? 684 ARG A CA 1 ATOM 5230 C C . ARG A 1 630 ? 6.757 61.913 37.099 1.00 22.63 ? 684 ARG A C 1 ATOM 5231 O O . ARG A 1 630 ? 7.338 62.269 38.139 1.00 22.42 ? 684 ARG A O 1 ATOM 5232 C CB . ARG A 1 630 ? 9.048 61.427 36.039 1.00 24.23 ? 684 ARG A CB 1 ATOM 5233 C CG . ARG A 1 630 ? 9.863 60.911 34.769 1.00 26.49 ? 684 ARG A CG 1 ATOM 5234 C CD . ARG A 1 630 ? 11.275 60.545 35.044 1.00 29.57 ? 684 ARG A CD 1 ATOM 5235 N NE . ARG A 1 630 ? 12.007 61.681 35.631 1.00 30.81 ? 684 ARG A NE 1 ATOM 5236 C CZ . ARG A 1 630 ? 13.121 61.582 36.340 1.00 30.33 ? 684 ARG A CZ 1 ATOM 5237 N NH1 . ARG A 1 630 ? 13.698 60.395 36.560 1.00 31.23 ? 684 ARG A NH1 1 ATOM 5238 N NH2 . ARG A 1 630 ? 13.716 62.692 36.798 1.00 33.85 ? 684 ARG A NH2 1 ATOM 5239 N N . PRO A 1 631 ? 5.426 61.732 37.049 1.00 23.38 ? 685 PRO A N 1 ATOM 5240 C CA . PRO A 1 631 ? 4.552 62.165 38.155 1.00 22.10 ? 685 PRO A CA 1 ATOM 5241 C C . PRO A 1 631 ? 4.815 61.405 39.443 1.00 19.89 ? 685 PRO A C 1 ATOM 5242 O O . PRO A 1 631 ? 4.419 61.914 40.496 1.00 21.22 ? 685 PRO A O 1 ATOM 5243 C CB . PRO A 1 631 ? 3.119 61.837 37.684 1.00 23.67 ? 685 PRO A CB 1 ATOM 5244 C CG . PRO A 1 631 ? 3.315 60.835 36.558 1.00 25.28 ? 685 PRO A CG 1 ATOM 5245 C CD . PRO A 1 631 ? 4.675 61.106 35.937 1.00 23.45 ? 685 PRO A CD 1 ATOM 5246 N N . PHE A 1 632 ? 5.414 60.221 39.373 1.00 18.75 ? 686 PHE A N 1 ATOM 5247 C CA . PHE A 1 632 ? 5.678 59.429 40.598 1.00 18.47 ? 686 PHE A CA 1 ATOM 5248 C C . PHE A 1 632 ? 7.053 59.640 41.229 1.00 19.46 ? 686 PHE A C 1 ATOM 5249 O O . PHE A 1 632 ? 7.342 59.088 42.295 1.00 19.70 ? 686 PHE A O 1 ATOM 5250 C CB . PHE A 1 632 ? 5.387 57.923 40.358 1.00 18.30 ? 686 PHE A CB 1 ATOM 5251 C CG . PHE A 1 632 ? 3.986 57.686 39.870 1.00 19.87 ? 686 PHE A CG 1 ATOM 5252 C CD1 . PHE A 1 632 ? 2.881 58.042 40.681 1.00 21.37 ? 686 PHE A CD1 1 ATOM 5253 C CD2 . PHE A 1 632 ? 3.774 57.160 38.591 1.00 20.78 ? 686 PHE A CD2 1 ATOM 5254 C CE1 . PHE A 1 632 ? 1.595 57.846 40.229 1.00 19.58 ? 686 PHE A CE1 1 ATOM 5255 C CE2 . PHE A 1 632 ? 2.494 56.979 38.101 1.00 21.23 ? 686 PHE A CE2 1 ATOM 5256 C CZ . PHE A 1 632 ? 1.392 57.322 38.923 1.00 20.32 ? 686 PHE A CZ 1 ATOM 5257 N N . TYR A 1 633 ? 7.862 60.499 40.604 1.00 18.36 ? 687 TYR A N 1 ATOM 5258 C CA . TYR A 1 633 ? 9.087 60.948 41.254 1.00 18.79 ? 687 TYR A CA 1 ATOM 5259 C C . TYR A 1 633 ? 8.845 62.374 41.677 1.00 18.31 ? 687 TYR A C 1 ATOM 5260 O O . TYR A 1 633 ? 8.737 63.294 40.830 1.00 19.18 ? 687 TYR A O 1 ATOM 5261 C CB . TYR A 1 633 ? 10.304 60.835 40.307 1.00 19.94 ? 687 TYR A CB 1 ATOM 5262 C CG . TYR A 1 633 ? 10.799 59.397 40.082 1.00 18.55 ? 687 TYR A CG 1 ATOM 5263 C CD1 . TYR A 1 633 ? 10.620 58.390 41.076 1.00 21.54 ? 687 TYR A CD1 1 ATOM 5264 C CD2 . TYR A 1 633 ? 11.481 59.052 38.937 1.00 24.15 ? 687 TYR A CD2 1 ATOM 5265 C CE1 . TYR A 1 633 ? 11.058 57.093 40.883 1.00 20.39 ? 687 TYR A CE1 1 ATOM 5266 C CE2 . TYR A 1 633 ? 11.941 57.720 38.724 1.00 23.43 ? 687 TYR A CE2 1 ATOM 5267 C CZ . TYR A 1 633 ? 11.722 56.772 39.715 1.00 23.17 ? 687 TYR A CZ 1 ATOM 5268 O OH . TYR A 1 633 ? 12.207 55.500 39.547 1.00 25.84 ? 687 TYR A OH 1 ATOM 5269 N N . ARG A 1 634 ? 8.723 62.597 42.987 1.00 15.86 ? 688 ARG A N 1 ATOM 5270 C CA . ARG A 1 634 ? 8.222 63.896 43.423 1.00 16.49 ? 688 ARG A CA 1 ATOM 5271 C C . ARG A 1 634 ? 9.233 64.577 44.385 1.00 17.58 ? 688 ARG A C 1 ATOM 5272 O O . ARG A 1 634 ? 8.982 65.696 44.834 1.00 18.11 ? 688 ARG A O 1 ATOM 5273 C CB . ARG A 1 634 ? 6.897 63.698 44.178 1.00 16.31 ? 688 ARG A CB 1 ATOM 5274 C CG . ARG A 1 634 ? 5.913 62.861 43.362 1.00 17.93 ? 688 ARG A CG 1 ATOM 5275 C CD . ARG A 1 634 ? 4.446 63.066 43.759 1.00 19.34 ? 688 ARG A CD 1 ATOM 5276 N NE . ARG A 1 634 ? 4.235 62.679 45.183 1.00 18.66 ? 688 ARG A NE 1 ATOM 5277 C CZ . ARG A 1 634 ? 3.159 62.973 45.917 1.00 22.19 ? 688 ARG A CZ 1 ATOM 5278 N NH1 . ARG A 1 634 ? 3.133 62.606 47.228 1.00 19.63 ? 688 ARG A NH1 1 ATOM 5279 N NH2 . ARG A 1 634 ? 2.099 63.619 45.379 1.00 19.65 ? 688 ARG A NH2 1 ATOM 5280 N N . HIS A 1 635 ? 10.293 63.878 44.757 1.00 17.22 ? 689 HIS A N 1 ATOM 5281 C CA . HIS A 1 635 ? 11.238 64.460 45.767 1.00 18.66 ? 689 HIS A CA 1 ATOM 5282 C C . HIS A 1 635 ? 12.136 65.463 44.980 1.00 18.91 ? 689 HIS A C 1 ATOM 5283 O O . HIS A 1 635 ? 12.905 65.041 44.115 1.00 19.71 ? 689 HIS A O 1 ATOM 5284 C CB . HIS A 1 635 ? 12.201 63.395 46.372 1.00 19.37 ? 689 HIS A CB 1 ATOM 5285 C CG . HIS A 1 635 ? 12.850 63.839 47.659 1.00 19.50 ? 689 HIS A CG 1 ATOM 5286 N ND1 . HIS A 1 635 ? 13.758 64.892 47.727 1.00 15.23 ? 689 HIS A ND1 1 ATOM 5287 C CD2 . HIS A 1 635 ? 12.687 63.399 48.924 1.00 18.23 ? 689 HIS A CD2 1 ATOM 5288 C CE1 . HIS A 1 635 ? 14.112 65.074 48.991 1.00 19.11 ? 689 HIS A CE1 1 ATOM 5289 N NE2 . HIS A 1 635 ? 13.504 64.158 49.729 1.00 18.73 ? 689 HIS A NE2 1 ATOM 5290 N N . VAL A 1 636 ? 12.146 66.739 45.372 1.00 18.09 ? 690 VAL A N 1 ATOM 5291 C CA . VAL A 1 636 ? 12.796 67.763 44.510 1.00 18.19 ? 690 VAL A CA 1 ATOM 5292 C C . VAL A 1 636 ? 14.309 67.681 44.707 1.00 18.97 ? 690 VAL A C 1 ATOM 5293 O O . VAL A 1 636 ? 15.070 68.164 43.839 1.00 17.98 ? 690 VAL A O 1 ATOM 5294 C CB . VAL A 1 636 ? 12.238 69.141 44.845 1.00 18.83 ? 690 VAL A CB 1 ATOM 5295 C CG1 . VAL A 1 636 ? 13.026 70.340 44.228 1.00 18.18 ? 690 VAL A CG1 1 ATOM 5296 C CG2 . VAL A 1 636 ? 10.768 69.270 44.410 1.00 16.33 ? 690 VAL A CG2 1 ATOM 5297 N N . ILE A 1 637 ? 14.761 67.160 45.857 1.00 19.04 ? 691 ILE A N 1 ATOM 5298 C CA . ILE A 1 637 ? 16.231 67.096 46.090 1.00 19.31 ? 691 ILE A CA 1 ATOM 5299 C C . ILE A 1 637 ? 16.847 65.864 45.474 1.00 21.17 ? 691 ILE A C 1 ATOM 5300 O O . ILE A 1 637 ? 17.936 65.939 44.897 1.00 21.59 ? 691 ILE A O 1 ATOM 5301 C CB . ILE A 1 637 ? 16.567 67.134 47.612 1.00 18.76 ? 691 ILE A CB 1 ATOM 5302 C CG1 . ILE A 1 637 ? 15.807 68.261 48.306 1.00 17.14 ? 691 ILE A CG1 1 ATOM 5303 C CG2 . ILE A 1 637 ? 18.164 67.270 47.849 1.00 23.10 ? 691 ILE A CG2 1 ATOM 5304 C CD1 . ILE A 1 637 ? 15.985 69.704 47.664 1.00 20.60 ? 691 ILE A CD1 1 ATOM 5305 N N . TYR A 1 638 ? 16.176 64.707 45.611 1.00 20.67 ? 692 TYR A N 1 ATOM 5306 C CA . TYR A 1 638 ? 16.815 63.419 45.352 1.00 21.30 ? 692 TYR A CA 1 ATOM 5307 C C . TYR A 1 638 ? 16.212 62.503 44.288 1.00 24.05 ? 692 TYR A C 1 ATOM 5308 O O . TYR A 1 638 ? 16.707 61.387 44.081 1.00 25.66 ? 692 TYR A O 1 ATOM 5309 C CB . TYR A 1 638 ? 16.836 62.596 46.633 1.00 20.70 ? 692 TYR A CB 1 ATOM 5310 C CG . TYR A 1 638 ? 17.863 63.101 47.653 1.00 19.90 ? 692 TYR A CG 1 ATOM 5311 C CD1 . TYR A 1 638 ? 17.465 63.530 48.919 1.00 21.36 ? 692 TYR A CD1 1 ATOM 5312 C CD2 . TYR A 1 638 ? 19.242 63.136 47.326 1.00 22.55 ? 692 TYR A CD2 1 ATOM 5313 C CE1 . TYR A 1 638 ? 18.409 63.961 49.843 1.00 21.43 ? 692 TYR A CE1 1 ATOM 5314 C CE2 . TYR A 1 638 ? 20.189 63.559 48.253 1.00 25.11 ? 692 TYR A CE2 1 ATOM 5315 C CZ . TYR A 1 638 ? 19.769 63.949 49.507 1.00 22.59 ? 692 TYR A CZ 1 ATOM 5316 O OH . TYR A 1 638 ? 20.733 64.333 50.419 1.00 24.16 ? 692 TYR A OH 1 ATOM 5317 N N . ALA A 1 639 ? 15.105 62.866 43.705 1.00 25.30 ? 693 ALA A N 1 ATOM 5318 C CA . ALA A 1 639 ? 14.558 61.946 42.626 1.00 26.35 ? 693 ALA A CA 1 ATOM 5319 C C . ALA A 1 639 ? 15.600 61.539 41.619 1.00 28.54 ? 693 ALA A C 1 ATOM 5320 O O . ALA A 1 639 ? 16.527 62.328 41.350 1.00 28.67 ? 693 ALA A O 1 ATOM 5321 C CB . ALA A 1 639 ? 13.404 62.665 41.898 1.00 27.58 ? 693 ALA A CB 1 ATOM 5322 N N . PRO A 1 640 ? 15.505 60.300 41.058 1.00 29.39 ? 694 PRO A N 1 ATOM 5323 C CA . PRO A 1 640 ? 16.421 59.946 39.912 1.00 31.40 ? 694 PRO A CA 1 ATOM 5324 C C . PRO A 1 640 ? 16.330 60.930 38.727 1.00 31.97 ? 694 PRO A C 1 ATOM 5325 O O . PRO A 1 640 ? 15.239 61.414 38.356 1.00 32.18 ? 694 PRO A O 1 ATOM 5326 C CB . PRO A 1 640 ? 15.962 58.542 39.496 1.00 31.69 ? 694 PRO A CB 1 ATOM 5327 C CG . PRO A 1 640 ? 15.099 57.992 40.724 1.00 30.08 ? 694 PRO A CG 1 ATOM 5328 C CD . PRO A 1 640 ? 14.470 59.262 41.309 1.00 28.69 ? 694 PRO A CD 1 ATOM 5329 N N . SER A 1 641 ? 17.485 61.294 38.191 1.00 33.17 ? 695 SER A N 1 ATOM 5330 C CA . SER A 1 641 ? 17.569 62.016 36.930 1.00 34.70 ? 695 SER A CA 1 ATOM 5331 C C . SER A 1 641 ? 17.020 61.113 35.813 1.00 36.18 ? 695 SER A C 1 ATOM 5332 O O . SER A 1 641 ? 17.253 59.892 35.797 1.00 35.30 ? 695 SER A O 1 ATOM 5333 C CB . SER A 1 641 ? 19.043 62.381 36.643 1.00 32.67 ? 695 SER A CB 1 ATOM 5334 O OG . SER A 1 641 ? 19.250 62.497 35.270 1.00 37.11 ? 695 SER A OG 1 ATOM 5335 N N . SER A 1 642 ? 16.322 61.746 34.879 1.00 38.08 ? 696 SER A N 1 ATOM 5336 C CA . SER A 1 642 ? 15.825 61.121 33.686 1.00 43.79 ? 696 SER A CA 1 ATOM 5337 C C . SER A 1 642 ? 17.019 60.686 32.832 1.00 46.60 ? 696 SER A C 1 ATOM 5338 O O . SER A 1 642 ? 16.953 59.681 32.122 1.00 48.22 ? 696 SER A O 1 ATOM 5339 C CB . SER A 1 642 ? 14.979 62.148 32.903 1.00 43.52 ? 696 SER A CB 1 ATOM 5340 O OG . SER A 1 642 ? 13.774 61.563 32.466 1.00 48.61 ? 696 SER A OG 1 ATOM 5341 N N . HIS A 1 643 ? 18.111 61.442 32.915 1.00 50.71 ? 697 HIS A N 1 ATOM 5342 C CA . HIS A 1 643 ? 19.265 61.315 31.987 1.00 54.20 ? 697 HIS A CA 1 ATOM 5343 C C . HIS A 1 643 ? 20.493 60.543 32.537 1.00 56.00 ? 697 HIS A C 1 ATOM 5344 O O . HIS A 1 643 ? 21.396 60.186 31.766 1.00 56.36 ? 697 HIS A O 1 ATOM 5345 C CB . HIS A 1 643 ? 19.687 62.708 31.488 1.00 54.68 ? 697 HIS A CB 1 ATOM 5346 C CG . HIS A 1 643 ? 18.657 63.390 30.640 1.00 55.25 ? 697 HIS A CG 1 ATOM 5347 N ND1 . HIS A 1 643 ? 18.258 62.903 29.410 1.00 56.99 ? 697 HIS A ND1 1 ATOM 5348 C CD2 . HIS A 1 643 ? 17.961 64.538 30.834 1.00 55.81 ? 697 HIS A CD2 1 ATOM 5349 C CE1 . HIS A 1 643 ? 17.347 63.715 28.895 1.00 57.01 ? 697 HIS A CE1 1 ATOM 5350 N NE2 . HIS A 1 643 ? 17.157 64.720 29.736 1.00 55.83 ? 697 HIS A NE2 1 ATOM 5351 N N . ASN A 1 644 ? 20.540 60.346 33.865 1.00 57.45 ? 698 ASN A N 1 ATOM 5352 C CA . ASN A 1 644 ? 21.085 59.109 34.478 1.00 58.82 ? 698 ASN A CA 1 ATOM 5353 C C . ASN A 1 644 ? 20.379 57.921 33.822 1.00 58.43 ? 698 ASN A C 1 ATOM 5354 O O . ASN A 1 644 ? 19.262 58.077 33.306 1.00 58.51 ? 698 ASN A O 1 ATOM 5355 C CB . ASN A 1 644 ? 20.898 59.100 36.032 1.00 57.96 ? 698 ASN A CB 1 ATOM 5356 C CG . ASN A 1 644 ? 20.211 57.801 36.579 1.00 61.48 ? 698 ASN A CG 1 ATOM 5357 O OD1 . ASN A 1 644 ? 20.874 56.946 37.189 1.00 65.22 ? 698 ASN A OD1 1 ATOM 5358 N ND2 . ASN A 1 644 ? 18.870 57.690 36.411 1.00 58.12 ? 698 ASN A ND2 1 ATOM 5359 N N . GLU A 1 649 ? 22.895 63.918 39.293 1.00 34.62 ? 703 GLU A N 1 ATOM 5360 C CA . GLU A 1 649 ? 23.097 64.742 40.495 1.00 33.47 ? 703 GLU A CA 1 ATOM 5361 C C . GLU A 1 649 ? 21.750 65.012 41.174 1.00 34.01 ? 703 GLU A C 1 ATOM 5362 O O . GLU A 1 649 ? 20.689 64.893 40.510 1.00 34.64 ? 703 GLU A O 1 ATOM 5363 C CB . GLU A 1 649 ? 23.694 66.136 40.148 1.00 37.39 ? 703 GLU A CB 1 ATOM 5364 C CG . GLU A 1 649 ? 25.096 66.244 39.548 1.00 39.52 ? 703 GLU A CG 1 ATOM 5365 C CD . GLU A 1 649 ? 26.208 65.630 40.326 1.00 47.81 ? 703 GLU A CD 1 ATOM 5366 O OE1 . GLU A 1 649 ? 27.202 65.243 39.645 1.00 52.02 ? 703 GLU A OE1 1 ATOM 5367 O OE2 . GLU A 1 649 ? 26.145 65.550 41.576 1.00 48.10 ? 703 GLU A OE2 1 ATOM 5368 N N . SER A 1 650 ? 21.808 65.405 42.462 1.00 30.87 ? 704 SER A N 1 ATOM 5369 C CA . SER A 1 650 ? 20.683 66.002 43.234 1.00 26.94 ? 704 SER A CA 1 ATOM 5370 C C . SER A 1 650 ? 20.139 67.241 42.542 1.00 24.96 ? 704 SER A C 1 ATOM 5371 O O . SER A 1 650 ? 20.754 67.736 41.628 1.00 27.75 ? 704 SER A O 1 ATOM 5372 C CB . SER A 1 650 ? 21.208 66.366 44.622 1.00 27.77 ? 704 SER A CB 1 ATOM 5373 O OG . SER A 1 650 ? 21.667 65.163 45.287 1.00 31.26 ? 704 SER A OG 1 ATOM 5374 N N . PHE A 1 651 ? 19.026 67.822 43.011 1.00 21.63 ? 705 PHE A N 1 ATOM 5375 C CA . PHE A 1 651 ? 18.289 68.810 42.195 1.00 19.41 ? 705 PHE A CA 1 ATOM 5376 C C . PHE A 1 651 ? 18.066 68.261 40.789 1.00 19.56 ? 705 PHE A C 1 ATOM 5377 O O . PHE A 1 651 ? 18.467 68.851 39.794 1.00 19.19 ? 705 PHE A O 1 ATOM 5378 C CB . PHE A 1 651 ? 18.939 70.198 42.186 1.00 20.32 ? 705 PHE A CB 1 ATOM 5379 C CG . PHE A 1 651 ? 18.904 70.892 43.525 1.00 20.80 ? 705 PHE A CG 1 ATOM 5380 C CD1 . PHE A 1 651 ? 17.658 71.205 44.138 1.00 19.19 ? 705 PHE A CD1 1 ATOM 5381 C CD2 . PHE A 1 651 ? 20.069 71.246 44.160 1.00 20.92 ? 705 PHE A CD2 1 ATOM 5382 C CE1 . PHE A 1 651 ? 17.610 71.858 45.374 1.00 22.17 ? 705 PHE A CE1 1 ATOM 5383 C CE2 . PHE A 1 651 ? 20.032 71.917 45.398 1.00 19.46 ? 705 PHE A CE2 1 ATOM 5384 C CZ . PHE A 1 651 ? 18.802 72.222 46.008 1.00 21.22 ? 705 PHE A CZ 1 ATOM 5385 N N . PRO A 1 652 ? 17.382 67.104 40.698 1.00 19.15 ? 706 PRO A N 1 ATOM 5386 C CA . PRO A 1 652 ? 17.276 66.447 39.392 1.00 19.28 ? 706 PRO A CA 1 ATOM 5387 C C . PRO A 1 652 ? 16.520 67.272 38.357 1.00 20.15 ? 706 PRO A C 1 ATOM 5388 O O . PRO A 1 652 ? 16.788 67.096 37.166 1.00 20.35 ? 706 PRO A O 1 ATOM 5389 C CB . PRO A 1 652 ? 16.461 65.143 39.702 1.00 19.76 ? 706 PRO A CB 1 ATOM 5390 C CG . PRO A 1 652 ? 15.761 65.445 41.014 1.00 19.20 ? 706 PRO A CG 1 ATOM 5391 C CD . PRO A 1 652 ? 16.839 66.276 41.778 1.00 18.90 ? 706 PRO A CD 1 ATOM 5392 N N . GLY A 1 653 ? 15.566 68.112 38.790 1.00 19.51 ? 707 GLY A N 1 ATOM 5393 C CA . GLY A 1 653 ? 14.800 68.936 37.811 1.00 19.38 ? 707 GLY A CA 1 ATOM 5394 C C . GLY A 1 653 ? 15.770 69.861 37.045 1.00 20.80 ? 707 GLY A C 1 ATOM 5395 O O . GLY A 1 653 ? 15.731 69.972 35.777 1.00 20.13 ? 707 GLY A O 1 ATOM 5396 N N . ILE A 1 654 ? 16.642 70.525 37.807 1.00 19.03 ? 708 ILE A N 1 ATOM 5397 C CA . ILE A 1 654 ? 17.600 71.463 37.187 1.00 19.60 ? 708 ILE A CA 1 ATOM 5398 C C . ILE A 1 654 ? 18.675 70.653 36.415 1.00 21.00 ? 708 ILE A C 1 ATOM 5399 O O . ILE A 1 654 ? 19.039 70.996 35.289 1.00 21.73 ? 708 ILE A O 1 ATOM 5400 C CB . ILE A 1 654 ? 18.315 72.296 38.265 1.00 19.94 ? 708 ILE A CB 1 ATOM 5401 C CG1 . ILE A 1 654 ? 17.289 73.097 39.096 1.00 20.96 ? 708 ILE A CG1 1 ATOM 5402 C CG2 . ILE A 1 654 ? 19.385 73.266 37.571 1.00 21.76 ? 708 ILE A CG2 1 ATOM 5403 C CD1 . ILE A 1 654 ? 17.917 73.814 40.347 1.00 21.55 ? 708 ILE A CD1 1 ATOM 5404 N N . TYR A 1 655 ? 19.128 69.555 36.998 1.00 19.88 ? 709 TYR A N 1 ATOM 5405 C CA . TYR A 1 655 ? 20.164 68.727 36.340 1.00 21.96 ? 709 TYR A CA 1 ATOM 5406 C C . TYR A 1 655 ? 19.698 68.235 34.942 1.00 22.37 ? 709 TYR A C 1 ATOM 5407 O O . TYR A 1 655 ? 20.430 68.348 33.947 1.00 22.49 ? 709 TYR A O 1 ATOM 5408 C CB . TYR A 1 655 ? 20.512 67.522 37.242 1.00 21.15 ? 709 TYR A CB 1 ATOM 5409 C CG . TYR A 1 655 ? 21.560 66.639 36.575 1.00 22.77 ? 709 TYR A CG 1 ATOM 5410 C CD1 . TYR A 1 655 ? 22.913 66.911 36.730 1.00 25.76 ? 709 TYR A CD1 1 ATOM 5411 C CD2 . TYR A 1 655 ? 21.180 65.576 35.724 1.00 24.94 ? 709 TYR A CD2 1 ATOM 5412 C CE1 . TYR A 1 655 ? 23.911 66.117 36.101 1.00 29.50 ? 709 TYR A CE1 1 ATOM 5413 C CE2 . TYR A 1 655 ? 22.174 64.782 35.079 1.00 27.29 ? 709 TYR A CE2 1 ATOM 5414 C CZ . TYR A 1 655 ? 23.527 65.073 35.269 1.00 30.62 ? 709 TYR A CZ 1 ATOM 5415 O OH . TYR A 1 655 ? 24.535 64.323 34.675 1.00 30.70 ? 709 TYR A OH 1 ATOM 5416 N N . ASP A 1 656 ? 18.474 67.675 34.875 1.00 22.67 ? 710 ASP A N 1 ATOM 5417 C CA . ASP A 1 656 ? 17.897 67.210 33.618 1.00 22.37 ? 710 ASP A CA 1 ATOM 5418 C C . ASP A 1 656 ? 17.672 68.359 32.626 1.00 23.27 ? 710 ASP A C 1 ATOM 5419 O O . ASP A 1 656 ? 17.923 68.208 31.429 1.00 22.78 ? 710 ASP A O 1 ATOM 5420 C CB . ASP A 1 656 ? 16.585 66.431 33.889 1.00 21.49 ? 710 ASP A CB 1 ATOM 5421 C CG . ASP A 1 656 ? 16.841 65.053 34.471 1.00 25.63 ? 710 ASP A CG 1 ATOM 5422 O OD1 . ASP A 1 656 ? 18.007 64.580 34.456 1.00 27.03 ? 710 ASP A OD1 1 ATOM 5423 O OD2 . ASP A 1 656 ? 15.875 64.420 34.951 1.00 28.04 ? 710 ASP A OD2 1 ATOM 5424 N N . ALA A 1 657 ? 17.265 69.526 33.117 1.00 21.81 ? 711 ALA A N 1 ATOM 5425 C CA . ALA A 1 657 ? 17.107 70.689 32.226 1.00 24.06 ? 711 ALA A CA 1 ATOM 5426 C C . ALA A 1 657 ? 18.458 71.109 31.599 1.00 24.06 ? 711 ALA A C 1 ATOM 5427 O O . ALA A 1 657 ? 18.531 71.523 30.426 1.00 25.00 ? 711 ALA A O 1 ATOM 5428 C CB . ALA A 1 657 ? 16.412 71.855 32.969 1.00 22.74 ? 711 ALA A CB 1 ATOM 5429 N N . LEU A 1 658 ? 19.528 70.939 32.353 1.00 22.22 ? 712 LEU A N 1 ATOM 5430 C CA . LEU A 1 658 ? 20.894 71.302 31.854 1.00 23.87 ? 712 LEU A CA 1 ATOM 5431 C C . LEU A 1 658 ? 21.582 70.234 30.982 1.00 26.24 ? 712 LEU A C 1 ATOM 5432 O O . LEU A 1 658 ? 22.566 70.513 30.263 1.00 26.77 ? 712 LEU A O 1 ATOM 5433 C CB . LEU A 1 658 ? 21.792 71.612 33.048 1.00 23.01 ? 712 LEU A CB 1 ATOM 5434 C CG . LEU A 1 658 ? 21.559 72.948 33.803 1.00 24.48 ? 712 LEU A CG 1 ATOM 5435 C CD1 . LEU A 1 658 ? 22.302 72.956 35.158 1.00 22.72 ? 712 LEU A CD1 1 ATOM 5436 C CD2 . LEU A 1 658 ? 21.973 74.188 32.946 1.00 24.88 ? 712 LEU A CD2 1 ATOM 5437 N N . PHE A 1 659 ? 21.073 69.008 31.059 1.00 26.49 ? 713 PHE A N 1 ATOM 5438 C CA . PHE A 1 659 ? 21.759 67.846 30.466 1.00 28.88 ? 713 PHE A CA 1 ATOM 5439 C C . PHE A 1 659 ? 21.760 67.963 28.974 1.00 29.30 ? 713 PHE A C 1 ATOM 5440 O O . PHE A 1 659 ? 20.707 68.146 28.360 1.00 29.35 ? 713 PHE A O 1 ATOM 5441 C CB . PHE A 1 659 ? 21.111 66.497 30.882 1.00 28.22 ? 713 PHE A CB 1 ATOM 5442 C CG . PHE A 1 659 ? 21.936 65.302 30.486 1.00 29.86 ? 713 PHE A CG 1 ATOM 5443 C CD1 . PHE A 1 659 ? 23.029 64.908 31.276 1.00 34.92 ? 713 PHE A CD1 1 ATOM 5444 C CD2 . PHE A 1 659 ? 21.654 64.617 29.308 1.00 32.57 ? 713 PHE A CD2 1 ATOM 5445 C CE1 . PHE A 1 659 ? 23.831 63.807 30.905 1.00 39.17 ? 713 PHE A CE1 1 ATOM 5446 C CE2 . PHE A 1 659 ? 22.448 63.514 28.907 1.00 33.06 ? 713 PHE A CE2 1 ATOM 5447 C CZ . PHE A 1 659 ? 23.533 63.114 29.699 1.00 37.90 ? 713 PHE A CZ 1 ATOM 5448 N N . ASP A 1 660 ? 22.962 67.953 28.409 1.00 31.55 ? 714 ASP A N 1 ATOM 5449 C CA . ASP A 1 660 ? 23.130 68.019 26.947 1.00 33.42 ? 714 ASP A CA 1 ATOM 5450 C C . ASP A 1 660 ? 22.413 69.253 26.395 1.00 33.18 ? 714 ASP A C 1 ATOM 5451 O O . ASP A 1 660 ? 21.901 69.249 25.262 1.00 33.60 ? 714 ASP A O 1 ATOM 5452 C CB . ASP A 1 660 ? 22.563 66.720 26.309 1.00 34.06 ? 714 ASP A CB 1 ATOM 5453 C CG . ASP A 1 660 ? 23.047 66.497 24.876 1.00 38.03 ? 714 ASP A CG 1 ATOM 5454 O OD1 . ASP A 1 660 ? 24.185 66.892 24.561 1.00 39.65 ? 714 ASP A OD1 1 ATOM 5455 O OD2 . ASP A 1 660 ? 22.263 65.926 24.079 1.00 43.57 ? 714 ASP A OD2 1 ATOM 5456 N N . ILE A 1 661 ? 22.393 70.342 27.177 1.00 32.06 ? 715 ILE A N 1 ATOM 5457 C CA . ILE A 1 661 ? 21.640 71.505 26.763 1.00 30.95 ? 715 ILE A CA 1 ATOM 5458 C C . ILE A 1 661 ? 22.221 72.129 25.467 1.00 34.31 ? 715 ILE A C 1 ATOM 5459 O O . ILE A 1 661 ? 21.467 72.701 24.670 1.00 33.33 ? 715 ILE A O 1 ATOM 5460 C CB . ILE A 1 661 ? 21.562 72.558 27.879 1.00 30.23 ? 715 ILE A CB 1 ATOM 5461 C CG1 . ILE A 1 661 ? 20.520 73.613 27.511 1.00 29.74 ? 715 ILE A CG1 1 ATOM 5462 C CG2 . ILE A 1 661 ? 22.955 73.149 28.208 1.00 29.33 ? 715 ILE A CG2 1 ATOM 5463 C CD1 . ILE A 1 661 ? 19.924 74.381 28.680 1.00 28.14 ? 715 ILE A CD1 1 ATOM 5464 N N . GLU A 1 662 ? 23.538 71.993 25.292 1.00 36.15 ? 716 GLU A N 1 ATOM 5465 C CA . GLU A 1 662 ? 24.220 72.549 24.111 1.00 40.99 ? 716 GLU A CA 1 ATOM 5466 C C . GLU A 1 662 ? 23.746 71.957 22.781 1.00 42.59 ? 716 GLU A C 1 ATOM 5467 O O . GLU A 1 662 ? 24.033 72.541 21.741 1.00 44.22 ? 716 GLU A O 1 ATOM 5468 C CB . GLU A 1 662 ? 25.756 72.499 24.254 1.00 40.94 ? 716 GLU A CB 1 ATOM 5469 C CG . GLU A 1 662 ? 26.385 71.095 24.205 1.00 44.78 ? 716 GLU A CG 1 ATOM 5470 C CD . GLU A 1 662 ? 26.361 70.340 25.556 1.00 48.89 ? 716 GLU A CD 1 ATOM 5471 O OE1 . GLU A 1 662 ? 25.578 70.676 26.480 1.00 45.26 ? 716 GLU A OE1 1 ATOM 5472 O OE2 . GLU A 1 662 ? 27.155 69.385 25.680 1.00 52.00 ? 716 GLU A OE2 1 ATOM 5473 N N . SER A 1 663 ? 23.016 70.826 22.819 1.00 43.44 ? 717 SER A N 1 ATOM 5474 C CA A SER A 1 663 ? 22.471 70.176 21.618 0.60 43.77 ? 717 SER A CA 1 ATOM 5475 C CA B SER A 1 663 ? 22.485 70.203 21.602 0.40 44.10 ? 717 SER A CA 1 ATOM 5476 C C . SER A 1 663 ? 21.023 70.575 21.315 1.00 44.56 ? 717 SER A C 1 ATOM 5477 O O . SER A 1 663 ? 20.492 70.249 20.247 1.00 45.11 ? 717 SER A O 1 ATOM 5478 C CB A SER A 1 663 ? 22.547 68.645 21.741 0.60 43.95 ? 717 SER A CB 1 ATOM 5479 C CB B SER A 1 663 ? 22.636 68.677 21.656 0.40 44.22 ? 717 SER A CB 1 ATOM 5480 O OG A SER A 1 663 ? 23.879 68.188 21.867 0.60 41.57 ? 717 SER A OG 1 ATOM 5481 O OG B SER A 1 663 ? 21.518 68.082 22.293 0.40 43.03 ? 717 SER A OG 1 ATOM 5482 N N . LYS A 1 664 ? 20.367 71.268 22.246 1.00 44.10 ? 718 LYS A N 1 ATOM 5483 C CA . LYS A 1 664 ? 18.966 71.657 22.048 1.00 44.91 ? 718 LYS A CA 1 ATOM 5484 C C . LYS A 1 664 ? 18.864 72.670 20.916 1.00 45.83 ? 718 LYS A C 1 ATOM 5485 O O . LYS A 1 664 ? 19.718 73.556 20.782 1.00 45.68 ? 718 LYS A O 1 ATOM 5486 C CB . LYS A 1 664 ? 18.356 72.222 23.340 1.00 44.26 ? 718 LYS A CB 1 ATOM 5487 C CG . LYS A 1 664 ? 18.345 71.231 24.498 1.00 45.77 ? 718 LYS A CG 1 ATOM 5488 C CD . LYS A 1 664 ? 17.268 70.172 24.292 1.00 48.75 ? 718 LYS A CD 1 ATOM 5489 C CE . LYS A 1 664 ? 17.521 68.968 25.187 1.00 51.11 ? 718 LYS A CE 1 ATOM 5490 N NZ . LYS A 1 664 ? 17.035 69.268 26.561 1.00 48.46 ? 718 LYS A NZ 1 ATOM 5491 N N . VAL A 1 665 ? 17.819 72.552 20.102 1.00 46.35 ? 719 VAL A N 1 ATOM 5492 C CA . VAL A 1 665 ? 17.739 73.384 18.888 1.00 46.70 ? 719 VAL A CA 1 ATOM 5493 C C . VAL A 1 665 ? 17.204 74.775 19.206 1.00 46.24 ? 719 VAL A C 1 ATOM 5494 O O . VAL A 1 665 ? 17.477 75.720 18.486 1.00 47.11 ? 719 VAL A O 1 ATOM 5495 C CB . VAL A 1 665 ? 16.882 72.733 17.771 1.00 47.42 ? 719 VAL A CB 1 ATOM 5496 C CG1 . VAL A 1 665 ? 17.646 71.545 17.102 1.00 49.07 ? 719 VAL A CG1 1 ATOM 5497 C CG2 . VAL A 1 665 ? 15.514 72.304 18.310 1.00 47.13 ? 719 VAL A CG2 1 ATOM 5498 N N . ASP A 1 666 ? 16.449 74.899 20.294 1.00 43.96 ? 720 ASP A N 1 ATOM 5499 C CA . ASP A 1 666 ? 15.880 76.183 20.688 1.00 42.26 ? 720 ASP A CA 1 ATOM 5500 C C . ASP A 1 666 ? 16.479 76.544 22.057 1.00 41.04 ? 720 ASP A C 1 ATOM 5501 O O . ASP A 1 666 ? 15.866 76.253 23.095 1.00 38.73 ? 720 ASP A O 1 ATOM 5502 C CB . ASP A 1 666 ? 14.360 76.038 20.755 1.00 42.54 ? 720 ASP A CB 1 ATOM 5503 C CG . ASP A 1 666 ? 13.647 77.335 21.017 1.00 42.71 ? 720 ASP A CG 1 ATOM 5504 O OD1 . ASP A 1 666 ? 14.281 78.335 21.421 1.00 43.60 ? 720 ASP A OD1 1 ATOM 5505 O OD2 . ASP A 1 666 ? 12.414 77.345 20.832 1.00 46.53 ? 720 ASP A OD2 1 ATOM 5506 N N . PRO A 1 667 ? 17.701 77.130 22.064 1.00 39.97 ? 721 PRO A N 1 ATOM 5507 C CA . PRO A 1 667 ? 18.358 77.435 23.349 1.00 38.79 ? 721 PRO A CA 1 ATOM 5508 C C . PRO A 1 667 ? 17.529 78.358 24.277 1.00 37.70 ? 721 PRO A C 1 ATOM 5509 O O . PRO A 1 667 ? 17.576 78.203 25.514 1.00 35.86 ? 721 PRO A O 1 ATOM 5510 C CB . PRO A 1 667 ? 19.701 78.079 22.937 1.00 39.96 ? 721 PRO A CB 1 ATOM 5511 C CG . PRO A 1 667 ? 19.585 78.432 21.492 1.00 40.88 ? 721 PRO A CG 1 ATOM 5512 C CD . PRO A 1 667 ? 18.467 77.627 20.894 1.00 41.35 ? 721 PRO A CD 1 ATOM 5513 N N . SER A 1 668 ? 16.784 79.306 23.701 1.00 36.19 ? 722 SER A N 1 ATOM 5514 C CA . SER A 1 668 ? 15.936 80.205 24.502 1.00 37.09 ? 722 SER A CA 1 ATOM 5515 C C . SER A 1 668 ? 14.927 79.398 25.339 1.00 35.70 ? 722 SER A C 1 ATOM 5516 O O . SER A 1 668 ? 14.724 79.652 26.532 1.00 33.96 ? 722 SER A O 1 ATOM 5517 C CB . SER A 1 668 ? 15.144 81.133 23.602 1.00 37.70 ? 722 SER A CB 1 ATOM 5518 O OG . SER A 1 668 ? 14.503 82.107 24.389 1.00 40.74 ? 722 SER A OG 1 ATOM 5519 N N . LYS A 1 669 ? 14.266 78.456 24.675 1.00 34.72 ? 723 LYS A N 1 ATOM 5520 C CA . LYS A 1 669 ? 13.331 77.596 25.350 1.00 34.71 ? 723 LYS A CA 1 ATOM 5521 C C . LYS A 1 669 ? 14.037 76.693 26.404 1.00 32.35 ? 723 LYS A C 1 ATOM 5522 O O . LYS A 1 669 ? 13.511 76.493 27.523 1.00 31.80 ? 723 LYS A O 1 ATOM 5523 C CB . LYS A 1 669 ? 12.576 76.751 24.307 1.00 36.18 ? 723 LYS A CB 1 ATOM 5524 C CG . LYS A 1 669 ? 11.577 75.771 24.924 1.00 40.14 ? 723 LYS A CG 1 ATOM 5525 C CD . LYS A 1 669 ? 10.607 75.179 23.886 1.00 47.15 ? 723 LYS A CD 1 ATOM 5526 C CE . LYS A 1 669 ? 9.804 74.057 24.544 1.00 48.49 ? 723 LYS A CE 1 ATOM 5527 N NZ . LYS A 1 669 ? 9.053 73.229 23.567 1.00 54.04 ? 723 LYS A NZ 1 ATOM 5528 N N . ALA A 1 670 ? 15.192 76.143 26.042 1.00 30.55 ? 724 ALA A N 1 ATOM 5529 C CA . ALA A 1 670 ? 15.919 75.216 26.910 1.00 28.57 ? 724 ALA A CA 1 ATOM 5530 C C . ALA A 1 670 ? 16.379 75.946 28.188 1.00 28.59 ? 724 ALA A C 1 ATOM 5531 O O . ALA A 1 670 ? 16.177 75.438 29.295 1.00 25.06 ? 724 ALA A O 1 ATOM 5532 C CB . ALA A 1 670 ? 17.139 74.661 26.194 1.00 29.44 ? 724 ALA A CB 1 ATOM 5533 N N . TRP A 1 671 ? 16.984 77.136 28.024 1.00 25.94 ? 725 TRP A N 1 ATOM 5534 C CA . TRP A 1 671 ? 17.415 77.909 29.187 1.00 26.34 ? 725 TRP A CA 1 ATOM 5535 C C . TRP A 1 671 ? 16.234 78.485 30.005 1.00 25.47 ? 725 TRP A C 1 ATOM 5536 O O . TRP A 1 671 ? 16.332 78.653 31.213 1.00 25.04 ? 725 TRP A O 1 ATOM 5537 C CB . TRP A 1 671 ? 18.412 78.990 28.768 1.00 26.16 ? 725 TRP A CB 1 ATOM 5538 C CG . TRP A 1 671 ? 19.773 78.348 28.507 1.00 26.84 ? 725 TRP A CG 1 ATOM 5539 C CD1 . TRP A 1 671 ? 20.326 78.015 27.290 1.00 27.02 ? 725 TRP A CD1 1 ATOM 5540 C CD2 . TRP A 1 671 ? 20.683 77.930 29.497 1.00 28.59 ? 725 TRP A CD2 1 ATOM 5541 N NE1 . TRP A 1 671 ? 21.557 77.400 27.479 1.00 29.09 ? 725 TRP A NE1 1 ATOM 5542 C CE2 . TRP A 1 671 ? 21.797 77.346 28.831 1.00 28.02 ? 725 TRP A CE2 1 ATOM 5543 C CE3 . TRP A 1 671 ? 20.655 77.955 30.915 1.00 25.65 ? 725 TRP A CE3 1 ATOM 5544 C CZ2 . TRP A 1 671 ? 22.884 76.821 29.518 1.00 30.17 ? 725 TRP A CZ2 1 ATOM 5545 C CZ3 . TRP A 1 671 ? 21.758 77.460 31.595 1.00 27.49 ? 725 TRP A CZ3 1 ATOM 5546 C CH2 . TRP A 1 671 ? 22.864 76.898 30.888 1.00 27.18 ? 725 TRP A CH2 1 ATOM 5547 N N . GLY A 1 672 ? 15.127 78.788 29.350 1.00 27.02 ? 726 GLY A N 1 ATOM 5548 C CA . GLY A 1 672 ? 13.884 79.133 30.075 1.00 24.61 ? 726 GLY A CA 1 ATOM 5549 C C . GLY A 1 672 ? 13.468 78.002 31.003 1.00 24.19 ? 726 GLY A C 1 ATOM 5550 O O . GLY A 1 672 ? 12.995 78.231 32.139 1.00 22.95 ? 726 GLY A O 1 ATOM 5551 N N . GLU A 1 673 ? 13.620 76.773 30.531 1.00 22.98 ? 727 GLU A N 1 ATOM 5552 C CA . GLU A 1 673 ? 13.236 75.640 31.364 1.00 23.86 ? 727 GLU A CA 1 ATOM 5553 C C . GLU A 1 673 ? 14.242 75.438 32.509 1.00 23.24 ? 727 GLU A C 1 ATOM 5554 O O . GLU A 1 673 ? 13.855 75.039 33.599 1.00 22.58 ? 727 GLU A O 1 ATOM 5555 C CB . GLU A 1 673 ? 13.052 74.377 30.507 1.00 23.79 ? 727 GLU A CB 1 ATOM 5556 C CG . GLU A 1 673 ? 12.666 73.095 31.313 1.00 25.84 ? 727 GLU A CG 1 ATOM 5557 C CD . GLU A 1 673 ? 11.338 73.134 32.061 1.00 29.42 ? 727 GLU A CD 1 ATOM 5558 O OE1 . GLU A 1 673 ? 10.503 74.053 31.836 1.00 27.54 ? 727 GLU A OE1 1 ATOM 5559 O OE2 . GLU A 1 673 ? 11.126 72.200 32.894 1.00 29.00 ? 727 GLU A OE2 1 ATOM 5560 N N . VAL A 1 674 ? 15.526 75.738 32.267 1.00 22.69 ? 728 VAL A N 1 ATOM 5561 C CA . VAL A 1 674 ? 16.473 75.716 33.369 1.00 22.73 ? 728 VAL A CA 1 ATOM 5562 C C . VAL A 1 674 ? 16.021 76.730 34.450 1.00 22.25 ? 728 VAL A C 1 ATOM 5563 O O . VAL A 1 674 ? 16.023 76.426 35.638 1.00 20.29 ? 728 VAL A O 1 ATOM 5564 C CB . VAL A 1 674 ? 17.918 76.053 32.894 1.00 24.24 ? 728 VAL A CB 1 ATOM 5565 C CG1 . VAL A 1 674 ? 18.810 76.306 34.109 1.00 23.03 ? 728 VAL A CG1 1 ATOM 5566 C CG2 . VAL A 1 674 ? 18.480 74.899 31.998 1.00 23.09 ? 728 VAL A CG2 1 ATOM 5567 N N . LYS A 1 675 ? 15.671 77.937 34.021 1.00 20.99 ? 729 LYS A N 1 ATOM 5568 C CA . LYS A 1 675 ? 15.227 78.965 34.977 1.00 20.84 ? 729 LYS A CA 1 ATOM 5569 C C . LYS A 1 675 ? 13.958 78.519 35.710 1.00 20.97 ? 729 LYS A C 1 ATOM 5570 O O . LYS A 1 675 ? 13.777 78.814 36.914 1.00 20.04 ? 729 LYS A O 1 ATOM 5571 C CB B LYS A 1 675 ? 14.993 80.297 34.278 0.65 21.72 ? 729 LYS A CB 1 ATOM 5572 C CB C LYS A 1 675 ? 15.016 80.307 34.273 0.35 21.53 ? 729 LYS A CB 1 ATOM 5573 C CG B LYS A 1 675 ? 16.324 80.923 33.828 0.65 21.78 ? 729 LYS A CG 1 ATOM 5574 C CG C LYS A 1 675 ? 16.328 80.874 33.713 0.35 21.69 ? 729 LYS A CG 1 ATOM 5575 C CD B LYS A 1 675 ? 16.112 82.168 32.964 0.65 25.20 ? 729 LYS A CD 1 ATOM 5576 C CD C LYS A 1 675 ? 16.172 82.291 33.162 0.35 23.48 ? 729 LYS A CD 1 ATOM 5577 C CE B LYS A 1 675 ? 15.515 83.312 33.769 0.65 22.49 ? 729 LYS A CE 1 ATOM 5578 C CE C LYS A 1 675 ? 15.501 82.302 31.797 0.35 22.82 ? 729 LYS A CE 1 ATOM 5579 N NZ B LYS A 1 675 ? 15.679 84.579 32.984 0.65 28.78 ? 729 LYS A NZ 1 ATOM 5580 N NZ C LYS A 1 675 ? 15.484 83.702 31.265 0.35 23.91 ? 729 LYS A NZ 1 ATOM 5581 N N . ARG A 1 676 ? 13.056 77.873 34.969 1.00 19.87 ? 730 ARG A N 1 ATOM 5582 C CA . ARG A 1 676 ? 11.849 77.376 35.660 1.00 19.30 ? 730 ARG A CA 1 ATOM 5583 C C . ARG A 1 676 ? 12.228 76.376 36.766 1.00 18.80 ? 730 ARG A C 1 ATOM 5584 O O . ARG A 1 676 ? 11.677 76.427 37.860 1.00 17.60 ? 730 ARG A O 1 ATOM 5585 C CB . ARG A 1 676 ? 10.845 76.750 34.682 1.00 19.75 ? 730 ARG A CB 1 ATOM 5586 C CG . ARG A 1 676 ? 9.474 76.510 35.373 1.00 21.15 ? 730 ARG A CG 1 ATOM 5587 C CD . ARG A 1 676 ? 8.440 75.910 34.351 1.00 22.58 ? 730 ARG A CD 1 ATOM 5588 N NE . ARG A 1 676 ? 8.724 74.512 34.087 1.00 22.94 ? 730 ARG A NE 1 ATOM 5589 C CZ . ARG A 1 676 ? 8.284 73.524 34.871 1.00 25.29 ? 730 ARG A CZ 1 ATOM 5590 N NH1 . ARG A 1 676 ? 7.600 73.802 35.998 1.00 26.77 ? 730 ARG A NH1 1 ATOM 5591 N NH2 . ARG A 1 676 ? 8.567 72.269 34.572 1.00 27.01 ? 730 ARG A NH2 1 ATOM 5592 N N . GLN A 1 677 ? 13.177 75.482 36.499 1.00 19.08 ? 731 GLN A N 1 ATOM 5593 C CA . GLN A 1 677 ? 13.543 74.483 37.494 1.00 19.03 ? 731 GLN A CA 1 ATOM 5594 C C . GLN A 1 677 ? 14.250 75.131 38.686 1.00 19.04 ? 731 GLN A C 1 ATOM 5595 O O . GLN A 1 677 ? 14.149 74.646 39.810 1.00 19.36 ? 731 GLN A O 1 ATOM 5596 C CB . GLN A 1 677 ? 14.415 73.432 36.841 1.00 18.60 ? 731 GLN A CB 1 ATOM 5597 C CG . GLN A 1 677 ? 13.565 72.578 35.778 1.00 18.98 ? 731 GLN A CG 1 ATOM 5598 C CD . GLN A 1 677 ? 12.421 71.773 36.445 1.00 22.92 ? 731 GLN A CD 1 ATOM 5599 O OE1 . GLN A 1 677 ? 12.531 71.324 37.586 1.00 21.59 ? 731 GLN A OE1 1 ATOM 5600 N NE2 . GLN A 1 677 ? 11.319 71.602 35.724 1.00 26.06 ? 731 GLN A NE2 1 ATOM 5601 N N . ILE A 1 678 ? 15.046 76.183 38.422 1.00 19.15 ? 732 ILE A N 1 ATOM 5602 C CA . ILE A 1 678 ? 15.686 76.884 39.546 1.00 19.65 ? 732 ILE A CA 1 ATOM 5603 C C . ILE A 1 678 ? 14.610 77.486 40.455 1.00 20.01 ? 732 ILE A C 1 ATOM 5604 O O . ILE A 1 678 ? 14.721 77.363 41.660 1.00 20.39 ? 732 ILE A O 1 ATOM 5605 C CB . ILE A 1 678 ? 16.607 78.037 39.011 1.00 18.12 ? 732 ILE A CB 1 ATOM 5606 C CG1 . ILE A 1 678 ? 17.812 77.405 38.302 1.00 21.01 ? 732 ILE A CG1 1 ATOM 5607 C CG2 . ILE A 1 678 ? 17.081 78.963 40.188 1.00 19.87 ? 732 ILE A CG2 1 ATOM 5608 C CD1 . ILE A 1 678 ? 18.662 78.477 37.453 1.00 21.30 ? 732 ILE A CD1 1 ATOM 5609 N N . TYR A 1 679 ? 13.610 78.161 39.872 1.00 18.82 ? 733 TYR A N 1 ATOM 5610 C CA . TYR A 1 679 ? 12.490 78.708 40.640 1.00 19.69 ? 733 TYR A CA 1 ATOM 5611 C C . TYR A 1 679 ? 11.779 77.601 41.454 1.00 18.83 ? 733 TYR A C 1 ATOM 5612 O O . TYR A 1 679 ? 11.538 77.786 42.656 1.00 17.75 ? 733 TYR A O 1 ATOM 5613 C CB . TYR A 1 679 ? 11.515 79.351 39.678 1.00 19.70 ? 733 TYR A CB 1 ATOM 5614 C CG . TYR A 1 679 ? 10.062 79.585 40.063 1.00 22.80 ? 733 TYR A CG 1 ATOM 5615 C CD1 . TYR A 1 679 ? 9.719 80.299 41.230 1.00 25.39 ? 733 TYR A CD1 1 ATOM 5616 C CD2 . TYR A 1 679 ? 9.025 79.164 39.186 1.00 22.68 ? 733 TYR A CD2 1 ATOM 5617 C CE1 . TYR A 1 679 ? 8.347 80.604 41.508 1.00 23.10 ? 733 TYR A CE1 1 ATOM 5618 C CE2 . TYR A 1 679 ? 7.674 79.464 39.437 1.00 23.70 ? 733 TYR A CE2 1 ATOM 5619 C CZ . TYR A 1 679 ? 7.356 80.196 40.615 1.00 24.33 ? 733 TYR A CZ 1 ATOM 5620 O OH . TYR A 1 679 ? 6.023 80.522 40.883 1.00 24.86 ? 733 TYR A OH 1 ATOM 5621 N N . VAL A 1 680 ? 11.497 76.472 40.823 1.00 18.93 ? 734 VAL A N 1 ATOM 5622 C CA . VAL A 1 680 ? 10.805 75.368 41.579 1.00 18.53 ? 734 VAL A CA 1 ATOM 5623 C C . VAL A 1 680 ? 11.654 74.861 42.764 1.00 18.77 ? 734 VAL A C 1 ATOM 5624 O O . VAL A 1 680 ? 11.147 74.650 43.895 1.00 18.36 ? 734 VAL A O 1 ATOM 5625 C CB . VAL A 1 680 ? 10.417 74.216 40.610 1.00 18.34 ? 734 VAL A CB 1 ATOM 5626 C CG1 . VAL A 1 680 ? 9.953 72.992 41.381 1.00 19.62 ? 734 VAL A CG1 1 ATOM 5627 C CG2 . VAL A 1 680 ? 9.236 74.689 39.690 1.00 19.25 ? 734 VAL A CG2 1 ATOM 5628 N N . ALA A 1 681 ? 12.965 74.728 42.523 1.00 18.71 ? 735 ALA A N 1 ATOM 5629 C CA . ALA A 1 681 ? 13.845 74.250 43.566 1.00 19.28 ? 735 ALA A CA 1 ATOM 5630 C C . ALA A 1 681 ? 14.006 75.250 44.694 1.00 18.95 ? 735 ALA A C 1 ATOM 5631 O O . ALA A 1 681 ? 13.942 74.855 45.865 1.00 19.59 ? 735 ALA A O 1 ATOM 5632 C CB . ALA A 1 681 ? 15.212 73.866 42.989 1.00 19.52 ? 735 ALA A CB 1 ATOM 5633 N N . ALA A 1 682 ? 14.236 76.528 44.361 1.00 17.63 ? 736 ALA A N 1 ATOM 5634 C CA . ALA A 1 682 ? 14.362 77.566 45.390 1.00 18.44 ? 736 ALA A CA 1 ATOM 5635 C C . ALA A 1 682 ? 13.094 77.625 46.203 1.00 18.99 ? 736 ALA A C 1 ATOM 5636 O O . ALA A 1 682 ? 13.136 77.698 47.431 1.00 18.77 ? 736 ALA A O 1 ATOM 5637 C CB . ALA A 1 682 ? 14.613 78.942 44.727 1.00 19.79 ? 736 ALA A CB 1 ATOM 5638 N N . PHE A 1 683 ? 11.951 77.677 45.518 1.00 17.48 ? 737 PHE A N 1 ATOM 5639 C CA . PHE A 1 683 ? 10.671 77.694 46.237 1.00 18.93 ? 737 PHE A CA 1 ATOM 5640 C C . PHE A 1 683 ? 10.547 76.503 47.209 1.00 16.30 ? 737 PHE A C 1 ATOM 5641 O O . PHE A 1 683 ? 10.165 76.678 48.390 1.00 18.23 ? 737 PHE A O 1 ATOM 5642 C CB . PHE A 1 683 ? 9.492 77.652 45.244 1.00 17.27 ? 737 PHE A CB 1 ATOM 5643 C CG . PHE A 1 683 ? 8.186 77.294 45.917 1.00 20.45 ? 737 PHE A CG 1 ATOM 5644 C CD1 . PHE A 1 683 ? 7.651 78.169 46.897 1.00 21.37 ? 737 PHE A CD1 1 ATOM 5645 C CD2 . PHE A 1 683 ? 7.580 76.078 45.671 1.00 23.93 ? 737 PHE A CD2 1 ATOM 5646 C CE1 . PHE A 1 683 ? 6.518 77.843 47.603 1.00 20.37 ? 737 PHE A CE1 1 ATOM 5647 C CE2 . PHE A 1 683 ? 6.367 75.728 46.373 1.00 22.37 ? 737 PHE A CE2 1 ATOM 5648 C CZ . PHE A 1 683 ? 5.854 76.626 47.317 1.00 20.02 ? 737 PHE A CZ 1 ATOM 5649 N N . THR A 1 684 ? 10.875 75.318 46.721 1.00 17.49 ? 738 THR A N 1 ATOM 5650 C CA . THR A 1 684 ? 10.705 74.111 47.546 1.00 17.72 ? 738 THR A CA 1 ATOM 5651 C C . THR A 1 684 ? 11.618 74.146 48.768 1.00 19.00 ? 738 THR A C 1 ATOM 5652 O O . THR A 1 684 ? 11.182 73.826 49.883 1.00 18.62 ? 738 THR A O 1 ATOM 5653 C CB . THR A 1 684 ? 10.946 72.842 46.730 1.00 19.97 ? 738 THR A CB 1 ATOM 5654 O OG1 . THR A 1 684 ? 10.070 72.828 45.620 1.00 19.13 ? 738 THR A OG1 1 ATOM 5655 C CG2 . THR A 1 684 ? 10.660 71.574 47.579 1.00 18.25 ? 738 THR A CG2 1 ATOM 5656 N N . VAL A 1 685 ? 12.873 74.534 48.555 1.00 18.17 ? 739 VAL A N 1 ATOM 5657 C CA . VAL A 1 685 ? 13.795 74.679 49.682 1.00 19.20 ? 739 VAL A CA 1 ATOM 5658 C C . VAL A 1 685 ? 13.265 75.671 50.722 1.00 18.21 ? 739 VAL A C 1 ATOM 5659 O O . VAL A 1 685 ? 13.279 75.371 51.941 1.00 18.30 ? 739 VAL A O 1 ATOM 5660 C CB . VAL A 1 685 ? 15.248 74.983 49.218 1.00 19.11 ? 739 VAL A CB 1 ATOM 5661 C CG1 . VAL A 1 685 ? 16.220 75.319 50.432 1.00 19.97 ? 739 VAL A CG1 1 ATOM 5662 C CG2 . VAL A 1 685 ? 15.785 73.756 48.449 1.00 19.90 ? 739 VAL A CG2 1 ATOM 5663 N N . GLN A 1 686 ? 12.855 76.858 50.266 1.00 18.20 ? 740 GLN A N 1 ATOM 5664 C CA . GLN A 1 686 ? 12.303 77.859 51.187 1.00 19.21 ? 740 GLN A CA 1 ATOM 5665 C C . GLN A 1 686 ? 11.041 77.356 51.894 1.00 18.86 ? 740 GLN A C 1 ATOM 5666 O O . GLN A 1 686 ? 10.833 77.588 53.125 1.00 19.49 ? 740 GLN A O 1 ATOM 5667 C CB . GLN A 1 686 ? 11.957 79.146 50.394 1.00 19.86 ? 740 GLN A CB 1 ATOM 5668 C CG . GLN A 1 686 ? 11.405 80.293 51.283 1.00 22.06 ? 740 GLN A CG 1 ATOM 5669 C CD . GLN A 1 686 ? 12.442 80.870 52.231 1.00 23.27 ? 740 GLN A CD 1 ATOM 5670 O OE1 . GLN A 1 686 ? 13.663 80.819 51.984 1.00 23.73 ? 740 GLN A OE1 1 ATOM 5671 N NE2 . GLN A 1 686 ? 11.959 81.457 53.321 1.00 23.82 ? 740 GLN A NE2 1 ATOM 5672 N N . ALA A 1 687 ? 10.203 76.650 51.137 1.00 18.38 ? 741 ALA A N 1 ATOM 5673 C CA . ALA A 1 687 ? 8.978 76.117 51.724 1.00 18.18 ? 741 ALA A CA 1 ATOM 5674 C C . ALA A 1 687 ? 9.279 75.084 52.820 1.00 18.43 ? 741 ALA A C 1 ATOM 5675 O O . ALA A 1 687 ? 8.641 75.102 53.891 1.00 18.47 ? 741 ALA A O 1 ATOM 5676 C CB . ALA A 1 687 ? 8.089 75.492 50.623 1.00 18.04 ? 741 ALA A CB 1 ATOM 5677 N N . ALA A 1 688 ? 10.256 74.203 52.568 1.00 17.87 ? 742 ALA A N 1 ATOM 5678 C CA . ALA A 1 688 ? 10.684 73.195 53.568 1.00 18.55 ? 742 ALA A CA 1 ATOM 5679 C C . ALA A 1 688 ? 11.244 73.944 54.786 1.00 18.99 ? 742 ALA A C 1 ATOM 5680 O O . ALA A 1 688 ? 10.937 73.586 55.917 1.00 19.12 ? 742 ALA A O 1 ATOM 5681 C CB . ALA A 1 688 ? 11.770 72.265 52.987 1.00 17.26 ? 742 ALA A CB 1 ATOM 5682 N N . ALA A 1 689 ? 12.105 74.946 54.530 1.00 19.75 ? 743 ALA A N 1 ATOM 5683 C CA . ALA A 1 689 ? 12.651 75.753 55.642 1.00 21.04 ? 743 ALA A CA 1 ATOM 5684 C C . ALA A 1 689 ? 11.548 76.305 56.513 1.00 20.70 ? 743 ALA A C 1 ATOM 5685 O O . ALA A 1 689 ? 11.613 76.214 57.782 1.00 19.97 ? 743 ALA A O 1 ATOM 5686 C CB . ALA A 1 689 ? 13.514 76.922 55.105 1.00 20.09 ? 743 ALA A CB 1 ATOM 5687 N N . GLU A 1 690 ? 10.495 76.859 55.866 1.00 20.09 ? 744 GLU A N 1 ATOM 5688 C CA . GLU A 1 690 ? 9.414 77.475 56.612 1.00 20.34 ? 744 GLU A CA 1 ATOM 5689 C C . GLU A 1 690 ? 8.597 76.513 57.480 1.00 19.99 ? 744 GLU A C 1 ATOM 5690 O O . GLU A 1 690 ? 7.948 76.952 58.418 1.00 20.77 ? 744 GLU A O 1 ATOM 5691 C CB . GLU A 1 690 ? 8.522 78.369 55.715 1.00 20.83 ? 744 GLU A CB 1 ATOM 5692 C CG . GLU A 1 690 ? 9.304 79.605 55.270 1.00 21.86 ? 744 GLU A CG 1 ATOM 5693 C CD . GLU A 1 690 ? 8.545 80.478 54.275 1.00 27.51 ? 744 GLU A CD 1 ATOM 5694 O OE1 . GLU A 1 690 ? 7.411 80.124 53.875 1.00 29.83 ? 744 GLU A OE1 1 ATOM 5695 O OE2 . GLU A 1 690 ? 9.138 81.498 53.878 1.00 27.08 ? 744 GLU A OE2 1 ATOM 5696 N N . THR A 1 691 ? 8.661 75.215 57.184 1.00 19.88 ? 745 THR A N 1 ATOM 5697 C CA . THR A 1 691 ? 8.047 74.219 58.070 1.00 18.74 ? 745 THR A CA 1 ATOM 5698 C C . THR A 1 691 ? 8.721 74.107 59.422 1.00 20.54 ? 745 THR A C 1 ATOM 5699 O O . THR A 1 691 ? 8.138 73.590 60.338 1.00 20.51 ? 745 THR A O 1 ATOM 5700 C CB . THR A 1 691 ? 7.909 72.812 57.471 1.00 20.45 ? 745 THR A CB 1 ATOM 5701 O OG1 . THR A 1 691 ? 9.183 72.133 57.432 1.00 19.94 ? 745 THR A OG1 1 ATOM 5702 C CG2 . THR A 1 691 ? 7.248 72.887 56.015 1.00 16.56 ? 745 THR A CG2 1 ATOM 5703 N N . LEU A 1 692 ? 9.955 74.596 59.497 1.00 20.53 ? 746 LEU A N 1 ATOM 5704 C CA . LEU A 1 692 ? 10.737 74.563 60.731 1.00 21.63 ? 746 LEU A CA 1 ATOM 5705 C C . LEU A 1 692 ? 10.661 75.897 61.446 1.00 22.95 ? 746 LEU A C 1 ATOM 5706 O O . LEU A 1 692 ? 11.152 76.012 62.568 1.00 23.31 ? 746 LEU A O 1 ATOM 5707 C CB . LEU A 1 692 ? 12.199 74.224 60.430 1.00 21.34 ? 746 LEU A CB 1 ATOM 5708 C CG . LEU A 1 692 ? 12.419 72.872 59.734 1.00 21.71 ? 746 LEU A CG 1 ATOM 5709 C CD1 . LEU A 1 692 ? 13.935 72.744 59.551 1.00 21.92 ? 746 LEU A CD1 1 ATOM 5710 C CD2 . LEU A 1 692 ? 11.829 71.712 60.594 1.00 22.44 ? 746 LEU A CD2 1 ATOM 5711 N N . SER A 1 693 ? 10.071 76.931 60.812 1.00 23.17 ? 747 SER A N 1 ATOM 5712 C CA . SER A 1 693 ? 9.799 78.182 61.551 1.00 23.62 ? 747 SER A CA 1 ATOM 5713 C C . SER A 1 693 ? 8.859 77.976 62.747 1.00 23.66 ? 747 SER A C 1 ATOM 5714 O O . SER A 1 693 ? 8.161 76.972 62.833 1.00 22.61 ? 747 SER A O 1 ATOM 5715 C CB . SER A 1 693 ? 9.215 79.240 60.610 1.00 23.13 ? 747 SER A CB 1 ATOM 5716 O OG . SER A 1 693 ? 10.182 79.491 59.603 1.00 24.47 ? 747 SER A OG 1 ATOM 5717 N N . GLU A 1 694 ? 8.856 78.920 63.708 1.00 24.58 ? 748 GLU A N 1 ATOM 5718 C CA . GLU A 1 694 ? 7.808 78.873 64.743 1.00 25.86 ? 748 GLU A CA 1 ATOM 5719 C C . GLU A 1 694 ? 6.433 78.795 64.048 1.00 24.56 ? 748 GLU A C 1 ATOM 5720 O O . GLU A 1 694 ? 6.198 79.441 63.009 1.00 24.97 ? 748 GLU A O 1 ATOM 5721 C CB . GLU A 1 694 ? 7.876 80.113 65.686 1.00 26.44 ? 748 GLU A CB 1 ATOM 5722 C CG . GLU A 1 694 ? 9.206 80.059 66.445 1.00 31.34 ? 748 GLU A CG 1 ATOM 5723 C CD . GLU A 1 694 ? 9.302 81.017 67.636 1.00 40.79 ? 748 GLU A CD 1 ATOM 5724 O OE1 . GLU A 1 694 ? 9.434 82.238 67.429 1.00 41.44 ? 748 GLU A OE1 1 ATOM 5725 O OE2 . GLU A 1 694 ? 9.275 80.499 68.768 1.00 44.91 ? 748 GLU A OE2 1 ATOM 5726 N N . VAL A 1 695 ? 5.535 78.006 64.606 1.00 24.30 ? 749 VAL A N 1 ATOM 5727 C CA . VAL A 1 695 ? 4.338 77.614 63.827 1.00 24.10 ? 749 VAL A CA 1 ATOM 5728 C C . VAL A 1 695 ? 3.273 78.727 63.832 1.00 25.71 ? 749 VAL A C 1 ATOM 5729 O O . VAL A 1 695 ? 2.323 78.681 63.068 1.00 24.97 ? 749 VAL A O 1 ATOM 5730 C CB . VAL A 1 695 ? 3.699 76.302 64.365 1.00 24.76 ? 749 VAL A CB 1 ATOM 5731 C CG1 . VAL A 1 695 ? 4.718 75.096 64.263 1.00 24.95 ? 749 VAL A CG1 1 ATOM 5732 C CG2 . VAL A 1 695 ? 3.215 76.486 65.845 1.00 25.14 ? 749 VAL A CG2 1 ATOM 5733 N N . ALA A 1 696 ? 3.423 79.700 64.744 1.00 25.40 ? 750 ALA A N 1 ATOM 5734 C CA . ALA A 1 696 ? 2.453 80.800 64.840 1.00 28.25 ? 750 ALA A CA 1 ATOM 5735 C C . ALA A 1 696 ? 3.073 81.870 65.732 1.00 30.86 ? 750 ALA A C 1 ATOM 5736 O O . ALA A 1 696 ? 2.580 82.996 65.739 1.00 35.15 ? 750 ALA A O 1 ATOM 5737 C CB . ALA A 1 696 ? 1.122 80.309 65.419 1.00 27.14 ? 750 ALA A CB 1 ATOM 5738 O OXT . ALA A 1 696 ? 4.066 81.619 66.429 1.00 30.53 ? 750 ALA A OXT 1 HETATM 5739 ZN ZN . ZN B 2 . ? 17.686 41.463 43.041 1.00 21.24 ? 801 ZN A ZN 1 HETATM 5740 ZN ZN . ZN C 2 . ? 17.086 42.230 46.306 1.00 20.40 ? 802 ZN A ZN 1 HETATM 5741 CA CA . CA D 3 . ? -0.712 50.189 41.169 1.00 18.86 ? 803 CA A CA 1 HETATM 5742 CL CL . CL E 4 . ? 18.979 47.370 51.698 1.00 24.13 ? 804 CL A CL 1 HETATM 5743 C C1 . NAG F 5 . ? 11.644 26.266 57.675 1.00 32.90 ? 805 NAG A C1 1 HETATM 5744 C C2 . NAG F 5 . ? 11.451 24.815 57.253 1.00 38.86 ? 805 NAG A C2 1 HETATM 5745 C C3 . NAG F 5 . ? 9.979 24.435 57.440 1.00 42.13 ? 805 NAG A C3 1 HETATM 5746 C C4 . NAG F 5 . ? 9.430 24.824 58.806 1.00 40.92 ? 805 NAG A C4 1 HETATM 5747 C C5 . NAG F 5 . ? 9.772 26.276 59.115 1.00 38.19 ? 805 NAG A C5 1 HETATM 5748 C C6 . NAG F 5 . ? 9.276 26.697 60.506 1.00 39.27 ? 805 NAG A C6 1 HETATM 5749 C C7 . NAG F 5 . ? 12.981 24.031 55.490 1.00 45.94 ? 805 NAG A C7 1 HETATM 5750 C C8 . NAG F 5 . ? 13.243 23.941 54.018 1.00 45.58 ? 805 NAG A C8 1 HETATM 5751 N N2 . NAG F 5 . ? 11.843 24.643 55.867 1.00 41.16 ? 805 NAG A N2 1 HETATM 5752 O O3 . NAG F 5 . ? 9.830 23.037 57.293 1.00 44.62 ? 805 NAG A O3 1 HETATM 5753 O O4 . NAG F 5 . ? 8.023 24.724 58.730 1.00 42.88 ? 805 NAG A O4 1 HETATM 5754 O O5 . NAG F 5 . ? 11.177 26.433 59.001 1.00 35.47 ? 805 NAG A O5 1 HETATM 5755 O O6 . NAG F 5 . ? 9.965 25.951 61.487 1.00 41.32 ? 805 NAG A O6 1 HETATM 5756 O O7 . NAG F 5 . ? 13.834 23.580 56.266 1.00 48.96 ? 805 NAG A O7 1 HETATM 5757 C C1 . NAG G 5 . ? 7.473 23.822 59.714 1.00 48.45 ? 806 NAG A C1 1 HETATM 5758 C C2 . NAG G 5 . ? 5.989 24.152 59.898 1.00 49.38 ? 806 NAG A C2 1 HETATM 5759 C C3 . NAG G 5 . ? 5.309 23.137 60.828 1.00 52.54 ? 806 NAG A C3 1 HETATM 5760 C C4 . NAG G 5 . ? 5.592 21.689 60.404 1.00 53.22 ? 806 NAG A C4 1 HETATM 5761 C C5 . NAG G 5 . ? 7.109 21.499 60.191 1.00 53.84 ? 806 NAG A C5 1 HETATM 5762 C C6 . NAG G 5 . ? 7.464 20.137 59.582 1.00 53.59 ? 806 NAG A C6 1 HETATM 5763 C C7 . NAG G 5 . ? 5.435 26.599 59.865 1.00 45.25 ? 806 NAG A C7 1 HETATM 5764 C C8 . NAG G 5 . ? 5.278 26.526 58.394 1.00 37.49 ? 806 NAG A C8 1 HETATM 5765 N N2 . NAG G 5 . ? 5.771 25.468 60.484 1.00 47.45 ? 806 NAG A N2 1 HETATM 5766 O O3 . NAG G 5 . ? 3.930 23.435 60.773 1.00 53.07 ? 806 NAG A O3 1 HETATM 5767 O O4 . NAG G 5 . ? 5.072 20.785 61.370 1.00 55.22 ? 806 NAG A O4 1 HETATM 5768 O O5 . NAG G 5 . ? 7.598 22.483 59.279 1.00 50.63 ? 806 NAG A O5 1 HETATM 5769 O O6 . NAG G 5 . ? 6.818 20.067 58.325 1.00 52.16 ? 806 NAG A O6 1 HETATM 5770 O O7 . NAG G 5 . ? 5.278 27.680 60.491 1.00 47.04 ? 806 NAG A O7 1 HETATM 5771 C C1 . NAG H 5 . ? 4.181 28.114 25.150 1.00 53.47 ? 807 NAG A C1 1 HETATM 5772 C C2 . NAG H 5 . ? 2.773 28.666 24.956 1.00 58.08 ? 807 NAG A C2 1 HETATM 5773 C C3 . NAG H 5 . ? 1.815 27.683 24.254 1.00 59.62 ? 807 NAG A C3 1 HETATM 5774 C C4 . NAG H 5 . ? 2.507 26.777 23.207 1.00 61.01 ? 807 NAG A C4 1 HETATM 5775 C C5 . NAG H 5 . ? 3.877 26.286 23.709 1.00 61.18 ? 807 NAG A C5 1 HETATM 5776 C C6 . NAG H 5 . ? 4.606 25.275 22.786 1.00 61.65 ? 807 NAG A C6 1 HETATM 5777 C C7 . NAG H 5 . ? 2.033 30.392 26.531 1.00 59.57 ? 807 NAG A C7 1 HETATM 5778 C C8 . NAG H 5 . ? 1.583 30.689 27.934 1.00 58.91 ? 807 NAG A C8 1 HETATM 5779 N N2 . NAG H 5 . ? 2.319 29.108 26.271 1.00 57.89 ? 807 NAG A N2 1 HETATM 5780 O O3 . NAG H 5 . ? 0.826 28.464 23.614 1.00 60.28 ? 807 NAG A O3 1 HETATM 5781 O O4 . NAG H 5 . ? 1.686 25.666 22.858 1.00 62.67 ? 807 NAG A O4 1 HETATM 5782 O O5 . NAG H 5 . ? 4.674 27.430 24.011 1.00 57.36 ? 807 NAG A O5 1 HETATM 5783 O O6 . NAG H 5 . ? 5.136 25.824 21.583 1.00 63.92 ? 807 NAG A O6 1 HETATM 5784 O O7 . NAG H 5 . ? 2.099 31.304 25.686 1.00 59.39 ? 807 NAG A O7 1 HETATM 5785 C C1 . NAG I 5 . ? 20.029 25.073 17.806 1.00 52.21 ? 808 NAG A C1 1 HETATM 5786 C C2 . NAG I 5 . ? 20.714 23.978 16.964 1.00 56.25 ? 808 NAG A C2 1 HETATM 5787 C C3 . NAG I 5 . ? 19.885 23.708 15.712 1.00 58.87 ? 808 NAG A C3 1 HETATM 5788 C C4 . NAG I 5 . ? 18.440 23.354 16.094 1.00 60.14 ? 808 NAG A C4 1 HETATM 5789 C C5 . NAG I 5 . ? 17.843 24.394 17.105 1.00 56.86 ? 808 NAG A C5 1 HETATM 5790 C C6 . NAG I 5 . ? 16.455 24.049 17.668 1.00 51.91 ? 808 NAG A C6 1 HETATM 5791 C C7 . NAG I 5 . ? 23.123 23.705 17.115 1.00 56.18 ? 808 NAG A C7 1 HETATM 5792 C C8 . NAG I 5 . ? 24.481 24.165 16.685 1.00 56.84 ? 808 NAG A C8 1 HETATM 5793 N N2 . NAG I 5 . ? 22.078 24.340 16.600 1.00 55.51 ? 808 NAG A N2 1 HETATM 5794 O O3 . NAG I 5 . ? 20.481 22.657 14.973 1.00 59.94 ? 808 NAG A O3 1 HETATM 5795 O O4 . NAG I 5 . ? 17.744 23.263 14.858 1.00 66.33 ? 808 NAG A O4 1 HETATM 5796 O O5 . NAG I 5 . ? 18.742 24.600 18.189 1.00 54.02 ? 808 NAG A O5 1 HETATM 5797 O O6 . NAG I 5 . ? 16.550 22.973 18.574 1.00 51.84 ? 808 NAG A O6 1 HETATM 5798 O O7 . NAG I 5 . ? 23.015 22.783 17.912 1.00 57.29 ? 808 NAG A O7 1 HETATM 5799 C C1 . NAG J 5 . ? 16.816 22.146 14.834 1.00 70.86 ? 809 NAG A C1 1 HETATM 5800 C C2 . NAG J 5 . ? 15.755 22.420 13.759 1.00 72.29 ? 809 NAG A C2 1 HETATM 5801 C C3 . NAG J 5 . ? 14.767 21.242 13.590 1.00 74.62 ? 809 NAG A C3 1 HETATM 5802 C C4 . NAG J 5 . ? 15.385 19.843 13.797 1.00 75.32 ? 809 NAG A C4 1 HETATM 5803 C C5 . NAG J 5 . ? 16.399 19.848 14.953 1.00 75.35 ? 809 NAG A C5 1 HETATM 5804 C C6 . NAG J 5 . ? 16.985 18.453 15.210 1.00 76.18 ? 809 NAG A C6 1 HETATM 5805 C C7 . NAG J 5 . ? 15.467 24.897 13.722 1.00 70.37 ? 809 NAG A C7 1 HETATM 5806 C C8 . NAG J 5 . ? 14.597 26.051 14.134 1.00 69.86 ? 809 NAG A C8 1 HETATM 5807 N N2 . NAG J 5 . ? 15.048 23.664 14.069 1.00 71.06 ? 809 NAG A N2 1 HETATM 5808 O O3 . NAG J 5 . ? 14.184 21.293 12.303 1.00 75.25 ? 809 NAG A O3 1 HETATM 5809 O O4 . NAG J 5 . ? 14.371 18.873 14.032 1.00 75.99 ? 809 NAG A O4 1 HETATM 5810 O O5 . NAG J 5 . ? 17.390 20.845 14.706 1.00 72.75 ? 809 NAG A O5 1 HETATM 5811 O O6 . NAG J 5 . ? 18.277 18.320 14.656 1.00 76.94 ? 809 NAG A O6 1 HETATM 5812 O O7 . NAG J 5 . ? 16.505 25.134 13.103 1.00 68.81 ? 809 NAG A O7 1 HETATM 5813 C C1 . NAG K 5 . ? 35.490 37.431 52.932 1.00 42.79 ? 810 NAG A C1 1 HETATM 5814 C C2 . NAG K 5 . ? 35.786 37.476 51.435 1.00 44.03 ? 810 NAG A C2 1 HETATM 5815 C C3 . NAG K 5 . ? 36.956 36.528 51.068 1.00 48.64 ? 810 NAG A C3 1 HETATM 5816 C C4 . NAG K 5 . ? 38.127 36.569 52.067 1.00 51.29 ? 810 NAG A C4 1 HETATM 5817 C C5 . NAG K 5 . ? 37.871 37.322 53.393 1.00 52.48 ? 810 NAG A C5 1 HETATM 5818 C C6 . NAG K 5 . ? 38.975 38.371 53.615 1.00 56.61 ? 810 NAG A C6 1 HETATM 5819 C C7 . NAG K 5 . ? 34.112 37.914 49.757 1.00 35.12 ? 810 NAG A C7 1 HETATM 5820 C C8 . NAG K 5 . ? 32.925 37.370 49.035 1.00 34.16 ? 810 NAG A C8 1 HETATM 5821 N N2 . NAG K 5 . ? 34.609 37.118 50.690 1.00 39.35 ? 810 NAG A N2 1 HETATM 5822 O O3 . NAG K 5 . ? 37.472 36.913 49.808 1.00 50.42 ? 810 NAG A O3 1 HETATM 5823 O O4 . NAG K 5 . ? 38.679 35.265 52.307 1.00 54.11 ? 810 NAG A O4 1 HETATM 5824 O O5 . NAG K 5 . ? 36.639 38.037 53.486 1.00 48.27 ? 810 NAG A O5 1 HETATM 5825 O O6 . NAG K 5 . ? 38.991 39.328 52.564 1.00 58.39 ? 810 NAG A O6 1 HETATM 5826 O O7 . NAG K 5 . ? 34.558 39.016 49.466 1.00 34.53 ? 810 NAG A O7 1 HETATM 5827 C C1 . NAG L 5 . ? 24.374 62.142 68.578 1.00 29.74 ? 811 NAG A C1 1 HETATM 5828 C C2 . NAG L 5 . ? 23.001 62.800 68.764 1.00 30.39 ? 811 NAG A C2 1 HETATM 5829 C C3 . NAG L 5 . ? 23.247 64.248 69.121 1.00 29.25 ? 811 NAG A C3 1 HETATM 5830 C C4 . NAG L 5 . ? 24.155 64.359 70.351 1.00 30.67 ? 811 NAG A C4 1 HETATM 5831 C C5 . NAG L 5 . ? 25.500 63.652 70.077 1.00 30.67 ? 811 NAG A C5 1 HETATM 5832 C C6 . NAG L 5 . ? 26.460 63.605 71.291 1.00 31.31 ? 811 NAG A C6 1 HETATM 5833 C C7 . NAG L 5 . ? 20.949 62.186 67.535 1.00 33.50 ? 811 NAG A C7 1 HETATM 5834 C C8 . NAG L 5 . ? 20.330 61.728 68.790 1.00 31.22 ? 811 NAG A C8 1 HETATM 5835 N N2 . NAG L 5 . ? 22.186 62.685 67.554 1.00 29.63 ? 811 NAG A N2 1 HETATM 5836 O O3 . NAG L 5 . ? 21.984 64.816 69.392 1.00 27.08 ? 811 NAG A O3 1 HETATM 5837 O O4 . NAG L 5 . ? 24.387 65.744 70.529 1.00 32.45 ? 811 NAG A O4 1 HETATM 5838 O O5 . NAG L 5 . ? 25.135 62.292 69.784 1.00 30.66 ? 811 NAG A O5 1 HETATM 5839 O O6 . NAG L 5 . ? 25.727 63.036 72.377 1.00 34.96 ? 811 NAG A O6 1 HETATM 5840 O O7 . NAG L 5 . ? 20.271 62.112 66.466 1.00 41.15 ? 811 NAG A O7 1 HETATM 5841 C C1 . NAG M 5 . ? 24.093 66.119 71.886 1.00 35.41 ? 812 NAG A C1 1 HETATM 5842 C C2 . NAG M 5 . ? 24.692 67.517 71.995 1.00 38.72 ? 812 NAG A C2 1 HETATM 5843 C C3 . NAG M 5 . ? 24.425 68.197 73.349 1.00 41.98 ? 812 NAG A C3 1 HETATM 5844 C C4 . NAG M 5 . ? 22.925 68.097 73.696 1.00 41.98 ? 812 NAG A C4 1 HETATM 5845 C C5 . NAG M 5 . ? 22.417 66.650 73.469 1.00 42.01 ? 812 NAG A C5 1 HETATM 5846 C C6 . NAG M 5 . ? 20.907 66.571 73.706 1.00 44.08 ? 812 NAG A C6 1 HETATM 5847 C C7 . NAG M 5 . ? 26.614 67.995 70.519 1.00 40.12 ? 812 NAG A C7 1 HETATM 5848 C C8 . NAG M 5 . ? 25.705 68.558 69.478 1.00 38.68 ? 812 NAG A C8 1 HETATM 5849 N N2 . NAG M 5 . ? 26.124 67.504 71.665 1.00 39.24 ? 812 NAG A N2 1 HETATM 5850 O O3 . NAG M 5 . ? 24.876 69.533 73.218 1.00 40.84 ? 812 NAG A O3 1 HETATM 5851 O O4 . NAG M 5 . ? 22.641 68.525 75.036 1.00 46.77 ? 812 NAG A O4 1 HETATM 5852 O O5 . NAG M 5 . ? 22.708 66.178 72.139 1.00 38.32 ? 812 NAG A O5 1 HETATM 5853 O O6 . NAG M 5 . ? 20.358 67.486 72.759 1.00 46.85 ? 812 NAG A O6 1 HETATM 5854 O O7 . NAG M 5 . ? 27.831 67.997 70.283 1.00 48.68 ? 812 NAG A O7 1 HETATM 5855 C C1 . NAG N 5 . ? 15.175 84.347 52.407 1.00 27.69 ? 813 NAG A C1 1 HETATM 5856 C C2 . NAG N 5 . ? 14.162 84.460 51.250 1.00 24.52 ? 813 NAG A C2 1 HETATM 5857 C C3 . NAG N 5 . ? 14.029 85.965 50.958 1.00 29.30 ? 813 NAG A C3 1 HETATM 5858 C C4 . NAG N 5 . ? 13.620 86.763 52.220 1.00 33.83 ? 813 NAG A C4 1 HETATM 5859 C C5 . NAG N 5 . ? 14.529 86.449 53.413 1.00 35.44 ? 813 NAG A C5 1 HETATM 5860 C C6 . NAG N 5 . ? 13.854 87.068 54.655 1.00 36.41 ? 813 NAG A C6 1 HETATM 5861 C C7 . NAG N 5 . ? 13.740 82.978 49.357 1.00 25.66 ? 813 NAG A C7 1 HETATM 5862 C C8 . NAG N 5 . ? 14.310 82.203 48.213 1.00 22.35 ? 813 NAG A C8 1 HETATM 5863 N N2 . NAG N 5 . ? 14.605 83.718 50.068 1.00 22.67 ? 813 NAG A N2 1 HETATM 5864 O O3 . NAG N 5 . ? 13.091 86.162 49.940 1.00 30.79 ? 813 NAG A O3 1 HETATM 5865 O O4 . NAG N 5 . ? 13.730 88.172 52.005 1.00 39.93 ? 813 NAG A O4 1 HETATM 5866 O O5 . NAG N 5 . ? 14.637 85.030 53.545 1.00 28.95 ? 813 NAG A O5 1 HETATM 5867 O O6 . NAG N 5 . ? 14.745 87.205 55.739 1.00 47.84 ? 813 NAG A O6 1 HETATM 5868 O O7 . NAG N 5 . ? 12.543 82.907 49.661 1.00 25.03 ? 813 NAG A O7 1 HETATM 5869 C C1 . NAG O 5 . ? 12.601 88.670 51.255 1.00 41.99 ? 814 NAG A C1 1 HETATM 5870 C C2 . NAG O 5 . ? 12.066 89.941 51.907 1.00 45.89 ? 814 NAG A C2 1 HETATM 5871 C C3 . NAG O 5 . ? 11.127 90.712 50.988 1.00 46.41 ? 814 NAG A C3 1 HETATM 5872 C C4 . NAG O 5 . ? 11.730 90.907 49.588 1.00 46.42 ? 814 NAG A C4 1 HETATM 5873 C C5 . NAG O 5 . ? 12.221 89.554 49.045 1.00 47.04 ? 814 NAG A C5 1 HETATM 5874 C C6 . NAG O 5 . ? 13.001 89.716 47.743 1.00 48.82 ? 814 NAG A C6 1 HETATM 5875 C C7 . NAG O 5 . ? 11.789 89.984 54.343 1.00 49.60 ? 814 NAG A C7 1 HETATM 5876 C C8 . NAG O 5 . ? 13.139 90.639 54.487 1.00 48.39 ? 814 NAG A C8 1 HETATM 5877 N N2 . NAG O 5 . ? 11.330 89.668 53.125 1.00 46.31 ? 814 NAG A N2 1 HETATM 5878 O O3 . NAG O 5 . ? 10.880 91.934 51.658 1.00 45.95 ? 814 NAG A O3 1 HETATM 5879 O O4 . NAG O 5 . ? 10.744 91.340 48.668 1.00 48.81 ? 814 NAG A O4 1 HETATM 5880 O O5 . NAG O 5 . ? 13.098 88.915 49.961 1.00 43.54 ? 814 NAG A O5 1 HETATM 5881 O O6 . NAG O 5 . ? 12.905 88.511 46.996 1.00 53.76 ? 814 NAG A O6 1 HETATM 5882 O O7 . NAG O 5 . ? 11.127 89.725 55.353 1.00 54.47 ? 814 NAG A O7 1 HETATM 5883 C C1 . BMA P 6 . ? 10.593 92.763 48.644 1.00 49.17 ? 815 BMA A C1 1 HETATM 5884 C C2 . BMA P 6 . ? 10.328 93.212 47.207 1.00 48.84 ? 815 BMA A C2 1 HETATM 5885 C C3 . BMA P 6 . ? 10.065 94.702 47.130 1.00 51.07 ? 815 BMA A C3 1 HETATM 5886 C C4 . BMA P 6 . ? 9.012 95.128 48.160 1.00 51.38 ? 815 BMA A C4 1 HETATM 5887 C C5 . BMA P 6 . ? 9.323 94.568 49.557 1.00 52.06 ? 815 BMA A C5 1 HETATM 5888 C C6 . BMA P 6 . ? 8.219 94.821 50.573 1.00 50.83 ? 815 BMA A C6 1 HETATM 5889 O O2 . BMA P 6 . ? 9.184 92.508 46.690 1.00 46.83 ? 815 BMA A O2 1 HETATM 5890 O O3 . BMA P 6 . ? 9.622 94.964 45.791 1.00 50.47 ? 815 BMA A O3 1 HETATM 5891 O O4 . BMA P 6 . ? 8.934 96.550 48.168 1.00 53.84 ? 815 BMA A O4 1 HETATM 5892 O O5 . BMA P 6 . ? 9.514 93.145 49.490 1.00 50.63 ? 815 BMA A O5 1 HETATM 5893 O O6 . BMA P 6 . ? 8.606 94.228 51.827 1.00 50.44 ? 815 BMA A O6 1 HETATM 5894 C C1 . MAN Q 7 . ? 10.316 96.106 45.220 1.00 53.76 ? 816 MAN A C1 1 HETATM 5895 C C2 . MAN Q 7 . ? 9.516 96.563 43.990 1.00 54.32 ? 816 MAN A C2 1 HETATM 5896 C C3 . MAN Q 7 . ? 9.674 95.541 42.859 1.00 55.50 ? 816 MAN A C3 1 HETATM 5897 C C4 . MAN Q 7 . ? 11.143 95.197 42.600 1.00 56.11 ? 816 MAN A C4 1 HETATM 5898 C C5 . MAN Q 7 . ? 11.824 94.793 43.921 1.00 56.20 ? 816 MAN A C5 1 HETATM 5899 C C6 . MAN Q 7 . ? 13.284 94.304 43.796 1.00 57.36 ? 816 MAN A C6 1 HETATM 5900 O O2 . MAN Q 7 . ? 9.960 97.840 43.581 1.00 53.95 ? 816 MAN A O2 1 HETATM 5901 O O3 . MAN Q 7 . ? 9.102 95.977 41.655 1.00 57.01 ? 816 MAN A O3 1 HETATM 5902 O O4 . MAN Q 7 . ? 11.176 94.134 41.672 1.00 58.11 ? 816 MAN A O4 1 HETATM 5903 O O5 . MAN Q 7 . ? 11.676 95.835 44.885 1.00 53.38 ? 816 MAN A O5 1 HETATM 5904 O O6 . MAN Q 7 . ? 14.102 95.257 43.138 1.00 58.53 ? 816 MAN A O6 1 HETATM 5905 C CAG . 5PU R 8 . ? 23.141 46.949 41.486 1.00 30.01 ? 817 5PU A CAG 1 HETATM 5906 C CAI . 5PU R 8 . ? 23.843 46.312 40.421 1.00 33.31 ? 817 5PU A CAI 1 HETATM 5907 C CAS . 5PU R 8 . ? 24.399 45.065 40.678 1.00 28.81 ? 817 5PU A CAS 1 HETATM 5908 C CAO . 5PU R 8 . ? 25.244 44.283 39.615 1.00 34.83 ? 817 5PU A CAO 1 HETATM 5909 O OAE . 5PU R 8 . ? 25.336 44.817 38.543 1.00 33.08 ? 817 5PU A OAE 1 HETATM 5910 O OAA . 5PU R 8 . ? 25.849 43.230 39.973 1.00 39.78 ? 817 5PU A OAA 1 HETATM 5911 C CAJ . 5PU R 8 . ? 24.316 44.476 41.912 1.00 30.06 ? 817 5PU A CAJ 1 HETATM 5912 C CAH . 5PU R 8 . ? 23.630 45.070 42.969 1.00 30.41 ? 817 5PU A CAH 1 HETATM 5913 C CAR . 5PU R 8 . ? 23.052 46.317 42.734 1.00 28.49 ? 817 5PU A CAR 1 HETATM 5914 C CAM . 5PU R 8 . ? 22.300 46.960 43.944 1.00 25.21 ? 817 5PU A CAM 1 HETATM 5915 C CAT . 5PU R 8 . ? 20.767 47.124 43.695 1.00 25.14 ? 817 5PU A CAT 1 HETATM 5916 C CAP . 5PU R 8 . ? 20.198 47.877 44.933 1.00 26.02 ? 817 5PU A CAP 1 HETATM 5917 O OAF . 5PU R 8 . ? 19.818 47.202 45.892 1.00 28.01 ? 817 5PU A OAF 1 HETATM 5918 O OAB . 5PU R 8 . ? 20.332 49.106 44.908 1.00 25.76 ? 817 5PU A OAB 1 HETATM 5919 C CAL . 5PU R 8 . ? 20.122 45.730 43.592 1.00 22.19 ? 817 5PU A CAL 1 HETATM 5920 C CAK . 5PU R 8 . ? 18.642 45.743 43.074 1.00 20.32 ? 817 5PU A CAK 1 HETATM 5921 C CAQ . 5PU R 8 . ? 18.095 44.307 43.238 1.00 22.02 ? 817 5PU A CAQ 1 HETATM 5922 O OAC . 5PU R 8 . ? 18.562 43.328 42.615 1.00 24.92 ? 817 5PU A OAC 1 HETATM 5923 N NAN . 5PU R 8 . ? 17.091 44.183 44.081 1.00 22.40 ? 817 5PU A NAN 1 HETATM 5924 O OAD . 5PU R 8 . ? 16.695 42.937 44.500 1.00 19.82 ? 817 5PU A OAD 1 HETATM 5925 C C . ACT S 9 . ? 16.969 44.859 40.025 1.00 35.95 ? 818 ACT A C 1 HETATM 5926 O O . ACT S 9 . ? 17.398 44.406 39.060 1.00 37.56 ? 818 ACT A O 1 HETATM 5927 O OXT . ACT S 9 . ? 16.024 44.212 40.526 1.00 39.16 ? 818 ACT A OXT 1 HETATM 5928 C CH3 . ACT S 9 . ? 17.584 46.133 40.487 1.00 38.84 ? 818 ACT A CH3 1 HETATM 5929 O O . HOH T 10 . ? 22.923 43.896 46.468 0.50 24.05 ? 901 HOH A O 1 HETATM 5930 O O . HOH T 10 . ? 11.848 56.591 30.859 1.00 52.47 ? 902 HOH A O 1 HETATM 5931 O O . HOH T 10 . ? -8.775 41.735 47.898 1.00 41.40 ? 903 HOH A O 1 HETATM 5932 O O . HOH T 10 . ? 25.241 65.485 62.579 1.00 43.04 ? 904 HOH A O 1 HETATM 5933 O O . HOH T 10 . ? 39.345 51.041 51.770 1.00 46.22 ? 905 HOH A O 1 HETATM 5934 O O . HOH T 10 . ? 13.627 58.051 34.924 1.00 43.70 ? 906 HOH A O 1 HETATM 5935 O O . HOH T 10 . ? 0.250 65.701 65.641 0.50 25.49 ? 907 HOH A O 1 HETATM 5936 O O . HOH T 10 . ? -6.636 45.570 49.000 1.00 43.09 ? 908 HOH A O 1 HETATM 5937 O O . HOH T 10 . ? 15.276 51.778 33.399 1.00 47.81 ? 909 HOH A O 1 HETATM 5938 O O . HOH T 10 . ? 30.948 63.074 53.823 1.00 37.79 ? 910 HOH A O 1 HETATM 5939 O O . HOH T 10 . ? 10.166 24.819 54.182 1.00 50.81 ? 911 HOH A O 1 HETATM 5940 O O . HOH T 10 . ? 38.156 34.618 26.688 1.00 47.08 ? 912 HOH A O 1 HETATM 5941 O O . HOH T 10 . ? -7.216 48.422 47.901 1.00 39.32 ? 913 HOH A O 1 HETATM 5942 O O . HOH T 10 . ? 3.508 48.109 41.868 1.00 43.63 ? 914 HOH A O 1 HETATM 5943 O O . HOH T 10 . ? 29.612 70.220 52.697 1.00 48.42 ? 915 HOH A O 1 HETATM 5944 O O . HOH T 10 . ? -10.437 48.892 48.402 1.00 31.13 ? 916 HOH A O 1 HETATM 5945 O O . HOH T 10 . ? -3.993 37.864 56.368 1.00 33.36 ? 917 HOH A O 1 HETATM 5946 O O . HOH T 10 . ? -2.786 46.149 68.285 1.00 47.59 ? 918 HOH A O 1 HETATM 5947 O O . HOH T 10 . ? 23.958 75.523 54.230 1.00 33.73 ? 919 HOH A O 1 HETATM 5948 O O . HOH T 10 . ? 10.920 82.779 65.465 1.00 42.92 ? 920 HOH A O 1 HETATM 5949 O O . HOH T 10 . ? 33.798 28.964 34.153 1.00 42.04 ? 921 HOH A O 1 HETATM 5950 O O . HOH T 10 . ? 14.846 37.115 27.809 1.00 24.85 ? 922 HOH A O 1 HETATM 5951 O O . HOH T 10 . ? 27.897 54.545 50.411 1.00 43.59 ? 923 HOH A O 1 HETATM 5952 O O . HOH T 10 . ? 33.599 40.426 47.582 1.00 38.54 ? 924 HOH A O 1 HETATM 5953 O O . HOH T 10 . ? 26.901 65.251 34.680 1.00 42.52 ? 925 HOH A O 1 HETATM 5954 O O . HOH T 10 . ? 0.544 33.885 36.476 1.00 43.00 ? 926 HOH A O 1 HETATM 5955 O O . HOH T 10 . ? 21.089 79.751 65.541 1.00 53.13 ? 927 HOH A O 1 HETATM 5956 O O . HOH T 10 . ? 29.545 35.054 64.880 1.00 48.31 ? 928 HOH A O 1 HETATM 5957 O O . HOH T 10 . ? 29.241 28.381 59.296 1.00 44.27 ? 929 HOH A O 1 HETATM 5958 O O . HOH T 10 . ? 33.790 48.124 58.650 1.00 32.83 ? 930 HOH A O 1 HETATM 5959 O O . HOH T 10 . ? 12.587 43.990 17.088 1.00 44.10 ? 931 HOH A O 1 HETATM 5960 O O . HOH T 10 . ? 3.622 62.657 50.166 1.00 21.61 ? 932 HOH A O 1 HETATM 5961 O O . HOH T 10 . ? 5.070 65.111 36.757 1.00 22.10 ? 933 HOH A O 1 HETATM 5962 O O . HOH T 10 . ? 16.076 67.976 72.461 1.00 46.37 ? 934 HOH A O 1 HETATM 5963 O O . HOH T 10 . ? 42.173 35.300 38.360 1.00 56.08 ? 935 HOH A O 1 HETATM 5964 O O . HOH T 10 . ? 7.679 26.931 54.413 1.00 46.80 ? 936 HOH A O 1 HETATM 5965 O O . HOH T 10 . ? 18.708 66.707 27.597 1.00 53.72 ? 937 HOH A O 1 HETATM 5966 O O . HOH T 10 . ? 11.934 29.334 19.103 1.00 49.24 ? 938 HOH A O 1 HETATM 5967 O O . HOH T 10 . ? 9.150 52.458 74.967 1.00 41.70 ? 939 HOH A O 1 HETATM 5968 O O . HOH T 10 . ? 23.010 44.807 36.395 1.00 31.38 ? 940 HOH A O 1 HETATM 5969 O O . HOH T 10 . ? 21.112 89.120 43.847 1.00 39.25 ? 941 HOH A O 1 HETATM 5970 O O . HOH T 10 . ? 28.535 44.744 65.292 1.00 36.37 ? 942 HOH A O 1 HETATM 5971 O O . HOH T 10 . ? 30.417 26.077 38.275 1.00 47.99 ? 943 HOH A O 1 HETATM 5972 O O . HOH T 10 . ? -0.964 57.501 73.830 1.00 46.80 ? 944 HOH A O 1 HETATM 5973 O O . HOH T 10 . ? 29.311 73.462 49.719 1.00 44.72 ? 945 HOH A O 1 HETATM 5974 O O . HOH T 10 . ? 31.904 75.146 36.210 1.00 48.02 ? 946 HOH A O 1 HETATM 5975 O O . HOH T 10 . ? -2.514 44.479 37.495 1.00 24.35 ? 947 HOH A O 1 HETATM 5976 O O . HOH T 10 . ? 15.782 55.279 72.136 1.00 47.84 ? 948 HOH A O 1 HETATM 5977 O O . HOH T 10 . ? 26.545 39.359 36.270 1.00 27.84 ? 949 HOH A O 1 HETATM 5978 O O . HOH T 10 . ? 16.965 37.493 43.821 1.00 21.77 ? 950 HOH A O 1 HETATM 5979 O O . HOH T 10 . ? 36.319 43.517 49.102 1.00 54.22 ? 951 HOH A O 1 HETATM 5980 O O . HOH T 10 . ? 12.635 93.863 39.532 1.00 42.29 ? 952 HOH A O 1 HETATM 5981 O O . HOH T 10 . ? 3.179 48.339 26.520 1.00 57.72 ? 953 HOH A O 1 HETATM 5982 O O . HOH T 10 . ? 7.671 38.811 29.220 1.00 34.99 ? 954 HOH A O 1 HETATM 5983 O O . HOH T 10 . ? 5.055 31.852 30.324 1.00 44.53 ? 955 HOH A O 1 HETATM 5984 O O . HOH T 10 . ? 22.003 61.520 51.432 1.00 34.84 ? 956 HOH A O 1 HETATM 5985 O O . HOH T 10 . ? 8.843 74.971 66.329 1.00 25.41 ? 957 HOH A O 1 HETATM 5986 O O . HOH T 10 . ? 19.208 48.221 54.762 1.00 25.38 ? 958 HOH A O 1 HETATM 5987 O O . HOH T 10 . ? 29.069 28.426 25.024 1.00 46.43 ? 959 HOH A O 1 HETATM 5988 O O . HOH T 10 . ? -1.566 32.671 44.565 1.00 38.60 ? 960 HOH A O 1 HETATM 5989 O O . HOH T 10 . ? 18.940 70.174 28.117 1.00 37.33 ? 961 HOH A O 1 HETATM 5990 O O . HOH T 10 . ? 31.085 40.201 46.574 1.00 31.21 ? 962 HOH A O 1 HETATM 5991 O O . HOH T 10 . ? 22.073 88.489 32.237 1.00 30.27 ? 963 HOH A O 1 HETATM 5992 O O . HOH T 10 . ? 8.307 29.594 33.260 1.00 38.47 ? 964 HOH A O 1 HETATM 5993 O O . HOH T 10 . ? 1.300 37.370 68.452 1.00 38.04 ? 965 HOH A O 1 HETATM 5994 O O . HOH T 10 . ? 1.175 50.811 39.653 1.00 19.25 ? 966 HOH A O 1 HETATM 5995 O O . HOH T 10 . ? 24.748 29.806 30.304 1.00 33.88 ? 967 HOH A O 1 HETATM 5996 O O . HOH T 10 . ? 24.062 24.801 30.497 1.00 40.66 ? 968 HOH A O 1 HETATM 5997 O O . HOH T 10 . ? 34.159 55.281 67.571 1.00 45.17 ? 969 HOH A O 1 HETATM 5998 O O . HOH T 10 . ? 20.370 31.589 26.213 1.00 38.27 ? 970 HOH A O 1 HETATM 5999 O O . HOH T 10 . ? 6.642 43.220 27.115 1.00 39.01 ? 971 HOH A O 1 HETATM 6000 O O . HOH T 10 . ? 4.250 43.980 75.788 1.00 44.54 ? 972 HOH A O 1 HETATM 6001 O O . HOH T 10 . ? 31.211 61.684 63.716 1.00 46.03 ? 973 HOH A O 1 HETATM 6002 O O . HOH T 10 . ? -5.193 44.818 30.772 1.00 41.84 ? 974 HOH A O 1 HETATM 6003 O O . HOH T 10 . ? 4.642 35.272 45.213 1.00 23.14 ? 975 HOH A O 1 HETATM 6004 O O . HOH T 10 . ? 4.124 63.887 72.435 1.00 29.17 ? 976 HOH A O 1 HETATM 6005 O O . HOH T 10 . ? 20.654 27.735 48.774 1.00 23.38 ? 977 HOH A O 1 HETATM 6006 O O . HOH T 10 . ? 14.446 68.580 41.307 1.00 25.25 ? 978 HOH A O 1 HETATM 6007 O O . HOH T 10 . ? 20.030 25.919 36.680 1.00 28.97 ? 979 HOH A O 1 HETATM 6008 O O . HOH T 10 . ? -3.326 47.439 52.988 1.00 34.92 ? 980 HOH A O 1 HETATM 6009 O O . HOH T 10 . ? 13.609 27.323 51.516 1.00 23.31 ? 981 HOH A O 1 HETATM 6010 O O . HOH T 10 . ? 30.163 64.849 51.861 1.00 43.43 ? 982 HOH A O 1 HETATM 6011 O O . HOH T 10 . ? -4.968 36.715 40.426 1.00 45.09 ? 983 HOH A O 1 HETATM 6012 O O . HOH T 10 . ? 32.086 35.313 59.159 1.00 32.92 ? 984 HOH A O 1 HETATM 6013 O O . HOH T 10 . ? 9.662 47.564 80.139 1.00 56.53 ? 985 HOH A O 1 HETATM 6014 O O . HOH T 10 . ? 26.379 69.685 28.810 1.00 44.22 ? 986 HOH A O 1 HETATM 6015 O O . HOH T 10 . ? 12.454 27.642 21.526 1.00 48.29 ? 987 HOH A O 1 HETATM 6016 O O . HOH T 10 . ? 35.982 38.135 57.033 1.00 52.66 ? 988 HOH A O 1 HETATM 6017 O O . HOH T 10 . ? 26.160 26.660 63.434 1.00 54.73 ? 989 HOH A O 1 HETATM 6018 O O . HOH T 10 . ? 5.093 66.661 33.495 1.00 43.90 ? 990 HOH A O 1 HETATM 6019 O O . HOH T 10 . ? 6.056 75.739 53.830 1.00 23.31 ? 991 HOH A O 1 HETATM 6020 O O . HOH T 10 . ? 17.152 26.052 59.453 1.00 33.73 ? 992 HOH A O 1 HETATM 6021 O O . HOH T 10 . ? 30.818 52.803 52.719 1.00 31.62 ? 993 HOH A O 1 HETATM 6022 O O . HOH T 10 . ? 0.257 31.651 57.955 1.00 32.25 ? 994 HOH A O 1 HETATM 6023 O O . HOH T 10 . ? 5.045 31.612 24.482 1.00 42.80 ? 995 HOH A O 1 HETATM 6024 O O . HOH T 10 . ? 20.109 46.186 78.771 1.00 44.27 ? 996 HOH A O 1 HETATM 6025 O O . HOH T 10 . ? 10.554 37.599 54.373 1.00 31.69 ? 997 HOH A O 1 HETATM 6026 O O . HOH T 10 . ? 15.559 25.657 29.996 1.00 44.80 ? 998 HOH A O 1 HETATM 6027 O O . HOH T 10 . ? 24.008 40.989 69.237 1.00 32.07 ? 999 HOH A O 1 HETATM 6028 O O . HOH T 10 . ? 27.647 31.434 28.789 1.00 33.63 ? 1000 HOH A O 1 HETATM 6029 O O . HOH T 10 . ? 29.280 60.880 57.159 1.00 31.92 ? 1001 HOH A O 1 HETATM 6030 O O . HOH T 10 . ? 24.701 37.610 32.453 1.00 27.94 ? 1002 HOH A O 1 HETATM 6031 O O . HOH T 10 . ? 8.188 52.070 42.739 1.00 28.17 ? 1003 HOH A O 1 HETATM 6032 O O . HOH T 10 . ? 36.672 42.676 65.055 1.00 36.70 ? 1004 HOH A O 1 HETATM 6033 O O . HOH T 10 . ? 21.320 63.879 60.860 1.00 24.88 ? 1005 HOH A O 1 HETATM 6034 O O . HOH T 10 . ? -0.323 43.836 60.466 1.00 25.58 ? 1006 HOH A O 1 HETATM 6035 O O . HOH T 10 . ? 25.469 63.995 50.035 1.00 25.49 ? 1007 HOH A O 1 HETATM 6036 O O . HOH T 10 . ? 7.092 56.072 43.085 1.00 22.61 ? 1008 HOH A O 1 HETATM 6037 O O . HOH T 10 . ? 20.132 31.370 43.484 1.00 26.34 ? 1009 HOH A O 1 HETATM 6038 O O . HOH T 10 . ? 10.389 27.523 51.490 1.00 34.26 ? 1010 HOH A O 1 HETATM 6039 O O . HOH T 10 . ? 23.095 68.109 33.686 1.00 30.06 ? 1011 HOH A O 1 HETATM 6040 O O . HOH T 10 . ? 23.005 65.794 65.831 1.00 35.43 ? 1012 HOH A O 1 HETATM 6041 O O . HOH T 10 . ? 35.158 20.953 44.278 1.00 46.47 ? 1013 HOH A O 1 HETATM 6042 O O . HOH T 10 . ? 29.406 70.820 45.879 1.00 29.64 ? 1014 HOH A O 1 HETATM 6043 O O . HOH T 10 . ? 25.703 25.021 57.506 1.00 37.22 ? 1015 HOH A O 1 HETATM 6044 O O . HOH T 10 . ? 20.381 53.318 47.478 1.00 28.55 ? 1016 HOH A O 1 HETATM 6045 O O . HOH T 10 . ? -4.256 37.446 51.165 1.00 47.09 ? 1017 HOH A O 1 HETATM 6046 O O . HOH T 10 . ? 8.248 45.053 46.143 1.00 17.06 ? 1018 HOH A O 1 HETATM 6047 O O . HOH T 10 . ? 5.562 82.072 53.671 1.00 34.19 ? 1019 HOH A O 1 HETATM 6048 O O . HOH T 10 . ? 25.128 86.516 42.308 1.00 36.20 ? 1020 HOH A O 1 HETATM 6049 O O . HOH T 10 . ? -2.583 59.660 48.272 1.00 23.93 ? 1021 HOH A O 1 HETATM 6050 O O . HOH T 10 . ? 8.518 50.745 25.087 1.00 52.38 ? 1022 HOH A O 1 HETATM 6051 O O . HOH T 10 . ? 37.696 61.428 55.205 1.00 55.40 ? 1023 HOH A O 1 HETATM 6052 O O . HOH T 10 . ? 24.786 23.221 53.061 1.00 44.59 ? 1024 HOH A O 1 HETATM 6053 O O . HOH T 10 . ? 30.672 84.625 28.441 1.00 40.48 ? 1025 HOH A O 1 HETATM 6054 O O . HOH T 10 . ? 19.109 54.531 72.960 1.00 42.09 ? 1026 HOH A O 1 HETATM 6055 O O . HOH T 10 . ? 34.800 56.031 50.792 1.00 47.25 ? 1027 HOH A O 1 HETATM 6056 O O . HOH T 10 . ? -6.024 41.893 44.031 1.00 41.01 ? 1028 HOH A O 1 HETATM 6057 O O . HOH T 10 . ? 12.266 37.147 28.516 1.00 27.74 ? 1029 HOH A O 1 HETATM 6058 O O . HOH T 10 . ? 13.823 45.071 49.541 1.00 20.32 ? 1030 HOH A O 1 HETATM 6059 O O . HOH T 10 . ? 22.161 80.956 57.109 1.00 44.28 ? 1031 HOH A O 1 HETATM 6060 O O . HOH T 10 . ? 28.575 54.145 52.886 1.00 27.37 ? 1032 HOH A O 1 HETATM 6061 O O . HOH T 10 . ? 29.893 43.076 32.168 1.00 33.41 ? 1033 HOH A O 1 HETATM 6062 O O . HOH T 10 . ? 4.220 71.095 80.705 1.00 49.88 ? 1034 HOH A O 1 HETATM 6063 O O . HOH T 10 . ? 0.332 30.376 44.634 1.00 53.59 ? 1035 HOH A O 1 HETATM 6064 O O . HOH T 10 . ? 23.865 82.716 42.176 1.00 40.36 ? 1036 HOH A O 1 HETATM 6065 O O . HOH T 10 . ? 30.141 76.786 49.491 1.00 49.99 ? 1037 HOH A O 1 HETATM 6066 O O . HOH T 10 . ? 25.158 71.054 30.856 1.00 36.62 ? 1038 HOH A O 1 HETATM 6067 O O . HOH T 10 . ? 28.888 58.586 48.183 1.00 41.72 ? 1039 HOH A O 1 HETATM 6068 O O . HOH T 10 . ? 19.012 40.919 75.734 1.00 40.56 ? 1040 HOH A O 1 HETATM 6069 O O . HOH T 10 . ? 21.831 25.379 23.756 1.00 39.76 ? 1041 HOH A O 1 HETATM 6070 O O . HOH T 10 . ? 11.233 63.863 57.979 1.00 28.09 ? 1042 HOH A O 1 HETATM 6071 O O . HOH T 10 . ? 6.331 38.827 26.308 1.00 39.84 ? 1043 HOH A O 1 HETATM 6072 O O . HOH T 10 . ? 21.949 81.267 22.505 1.00 45.80 ? 1044 HOH A O 1 HETATM 6073 O O . HOH T 10 . ? 17.606 83.034 40.973 1.00 34.83 ? 1045 HOH A O 1 HETATM 6074 O O . HOH T 10 . ? -1.221 51.861 72.270 1.00 40.16 ? 1046 HOH A O 1 HETATM 6075 O O . HOH T 10 . ? -10.469 43.831 38.380 1.00 49.29 ? 1047 HOH A O 1 HETATM 6076 O O . HOH T 10 . ? 16.159 72.718 29.336 1.00 29.11 ? 1048 HOH A O 1 HETATM 6077 O O . HOH T 10 . ? 25.876 27.359 24.352 1.00 40.79 ? 1049 HOH A O 1 HETATM 6078 O O . HOH T 10 . ? 11.697 61.917 43.495 1.00 38.87 ? 1050 HOH A O 1 HETATM 6079 O O . HOH T 10 . ? -9.667 46.187 34.039 1.00 37.70 ? 1051 HOH A O 1 HETATM 6080 O O . HOH T 10 . ? 27.947 72.423 52.455 1.00 38.03 ? 1052 HOH A O 1 HETATM 6081 O O . HOH T 10 . ? -5.578 50.785 28.180 1.00 50.23 ? 1053 HOH A O 1 HETATM 6082 O O . HOH T 10 . ? 21.614 84.526 46.789 1.00 33.09 ? 1054 HOH A O 1 HETATM 6083 O O . HOH T 10 . ? 20.085 61.805 62.747 1.00 22.19 ? 1055 HOH A O 1 HETATM 6084 O O . HOH T 10 . ? 5.385 78.332 54.210 1.00 25.98 ? 1056 HOH A O 1 HETATM 6085 O O . HOH T 10 . ? 35.262 32.269 53.805 1.00 53.47 ? 1057 HOH A O 1 HETATM 6086 O O . HOH T 10 . ? 9.587 29.532 42.896 1.00 24.39 ? 1058 HOH A O 1 HETATM 6087 O O . HOH T 10 . ? 10.858 29.238 40.414 1.00 28.64 ? 1059 HOH A O 1 HETATM 6088 O O . HOH T 10 . ? 3.549 27.610 54.463 1.00 31.87 ? 1060 HOH A O 1 HETATM 6089 O O . HOH T 10 . ? 12.473 54.042 35.216 1.00 30.95 ? 1061 HOH A O 1 HETATM 6090 O O . HOH T 10 . ? 8.220 70.353 36.492 1.00 43.16 ? 1062 HOH A O 1 HETATM 6091 O O . HOH T 10 . ? 18.335 55.639 30.271 1.00 59.23 ? 1063 HOH A O 1 HETATM 6092 O O . HOH T 10 . ? 13.751 68.610 34.470 1.00 24.36 ? 1064 HOH A O 1 HETATM 6093 O O . HOH T 10 . ? 29.037 34.141 32.795 1.00 27.23 ? 1065 HOH A O 1 HETATM 6094 O O . HOH T 10 . ? 11.580 81.425 60.945 1.00 37.34 ? 1066 HOH A O 1 HETATM 6095 O O . HOH T 10 . ? 14.380 54.946 37.976 1.00 49.34 ? 1067 HOH A O 1 HETATM 6096 O O . HOH T 10 . ? 13.566 71.991 40.140 1.00 21.92 ? 1068 HOH A O 1 HETATM 6097 O O . HOH T 10 . ? -0.023 60.778 48.139 1.00 28.16 ? 1069 HOH A O 1 HETATM 6098 O O . HOH T 10 . ? 0.544 33.640 43.208 1.00 25.95 ? 1070 HOH A O 1 HETATM 6099 O O . HOH T 10 . ? 24.445 31.885 28.720 1.00 33.75 ? 1071 HOH A O 1 HETATM 6100 O O . HOH T 10 . ? 11.755 64.304 34.674 1.00 34.82 ? 1072 HOH A O 1 HETATM 6101 O O . HOH T 10 . ? 21.181 45.482 50.079 1.00 26.04 ? 1073 HOH A O 1 HETATM 6102 O O . HOH T 10 . ? 10.256 31.020 26.699 1.00 30.08 ? 1074 HOH A O 1 HETATM 6103 O O . HOH T 10 . ? 18.092 31.162 29.111 1.00 33.38 ? 1075 HOH A O 1 HETATM 6104 O O . HOH T 10 . ? 15.188 42.214 38.570 1.00 20.56 ? 1076 HOH A O 1 HETATM 6105 O O . HOH T 10 . ? 10.125 36.419 69.848 1.00 35.88 ? 1077 HOH A O 1 HETATM 6106 O O . HOH T 10 . ? 22.220 59.161 69.514 1.00 49.19 ? 1078 HOH A O 1 HETATM 6107 O O . HOH T 10 . ? -3.112 48.768 55.856 1.00 50.58 ? 1079 HOH A O 1 HETATM 6108 O O . HOH T 10 . ? 11.120 37.089 42.194 1.00 20.81 ? 1080 HOH A O 1 HETATM 6109 O O . HOH T 10 . ? -6.312 59.053 37.734 1.00 27.06 ? 1081 HOH A O 1 HETATM 6110 O O . HOH T 10 . ? 1.508 31.391 64.529 1.00 37.66 ? 1082 HOH A O 1 HETATM 6111 O O . HOH T 10 . ? 20.699 75.063 23.473 1.00 51.22 ? 1083 HOH A O 1 HETATM 6112 O O . HOH T 10 . ? 9.910 76.474 30.656 1.00 39.21 ? 1084 HOH A O 1 HETATM 6113 O O . HOH T 10 . ? -4.219 44.163 27.446 1.00 52.14 ? 1085 HOH A O 1 HETATM 6114 O O . HOH T 10 . ? 5.678 54.114 29.936 1.00 49.32 ? 1086 HOH A O 1 HETATM 6115 O O . HOH T 10 . ? 15.078 24.924 58.332 1.00 37.17 ? 1087 HOH A O 1 HETATM 6116 O O . HOH T 10 . ? -3.637 62.555 53.648 1.00 20.11 ? 1088 HOH A O 1 HETATM 6117 O O . HOH T 10 . ? -2.702 33.188 55.548 1.00 39.08 ? 1089 HOH A O 1 HETATM 6118 O O . HOH T 10 . ? 19.808 54.067 45.087 1.00 43.43 ? 1090 HOH A O 1 HETATM 6119 O O . HOH T 10 . ? 24.655 68.751 63.074 1.00 50.13 ? 1091 HOH A O 1 HETATM 6120 O O . HOH T 10 . ? 1.056 63.720 42.820 1.00 34.49 ? 1092 HOH A O 1 HETATM 6121 O O . HOH T 10 . ? 16.289 79.916 69.068 1.00 43.83 ? 1093 HOH A O 1 HETATM 6122 O O . HOH T 10 . ? 10.517 55.905 74.995 1.00 33.84 ? 1094 HOH A O 1 HETATM 6123 O O . HOH T 10 . ? 9.100 54.361 43.360 1.00 27.09 ? 1095 HOH A O 1 HETATM 6124 O O . HOH T 10 . ? 2.676 64.051 40.258 1.00 33.03 ? 1096 HOH A O 1 HETATM 6125 O O . HOH T 10 . ? 14.270 81.853 40.571 1.00 36.66 ? 1097 HOH A O 1 HETATM 6126 O O . HOH T 10 . ? 14.635 32.358 48.060 1.00 23.12 ? 1098 HOH A O 1 HETATM 6127 O O . HOH T 10 . ? 23.431 79.494 50.350 1.00 29.32 ? 1099 HOH A O 1 HETATM 6128 O O . HOH T 10 . ? 14.549 38.333 34.771 1.00 23.46 ? 1100 HOH A O 1 HETATM 6129 O O . HOH T 10 . ? 7.975 69.942 58.806 1.00 20.80 ? 1101 HOH A O 1 HETATM 6130 O O . HOH T 10 . ? 21.518 32.653 28.643 1.00 29.78 ? 1102 HOH A O 1 HETATM 6131 O O . HOH T 10 . ? 7.455 72.170 44.982 1.00 22.01 ? 1103 HOH A O 1 HETATM 6132 O O . HOH T 10 . ? 4.122 68.987 48.991 1.00 23.49 ? 1104 HOH A O 1 HETATM 6133 O O . HOH T 10 . ? 27.234 57.357 70.187 1.00 35.65 ? 1105 HOH A O 1 HETATM 6134 O O . HOH T 10 . ? 16.527 26.444 34.577 1.00 32.79 ? 1106 HOH A O 1 HETATM 6135 O O . HOH T 10 . ? 5.610 63.013 64.796 1.00 28.69 ? 1107 HOH A O 1 HETATM 6136 O O . HOH T 10 . ? 29.551 36.398 44.146 1.00 24.40 ? 1108 HOH A O 1 HETATM 6137 O O . HOH T 10 . ? 27.373 63.588 63.096 1.00 52.25 ? 1109 HOH A O 1 HETATM 6138 O O . HOH T 10 . ? 7.082 82.023 62.478 1.00 45.56 ? 1110 HOH A O 1 HETATM 6139 O O . HOH T 10 . ? 13.158 51.835 39.733 1.00 37.85 ? 1111 HOH A O 1 HETATM 6140 O O . HOH T 10 . ? 20.290 87.652 39.915 1.00 52.56 ? 1112 HOH A O 1 HETATM 6141 O O . HOH T 10 . ? 21.790 41.749 46.137 1.00 24.24 ? 1113 HOH A O 1 HETATM 6142 O O . HOH T 10 . ? 33.041 30.075 24.625 1.00 47.62 ? 1114 HOH A O 1 HETATM 6143 O O . HOH T 10 . ? 23.761 46.531 34.401 1.00 32.49 ? 1115 HOH A O 1 HETATM 6144 O O . HOH T 10 . ? 14.678 81.248 37.923 1.00 24.32 ? 1116 HOH A O 1 HETATM 6145 O O . HOH T 10 . ? 21.210 24.354 50.956 1.00 42.01 ? 1117 HOH A O 1 HETATM 6146 O O . HOH T 10 . ? 32.642 42.939 19.785 1.00 49.82 ? 1118 HOH A O 1 HETATM 6147 O O . HOH T 10 . ? -1.649 46.371 55.343 1.00 34.25 ? 1119 HOH A O 1 HETATM 6148 O O . HOH T 10 . ? 20.641 30.408 29.886 1.00 32.16 ? 1120 HOH A O 1 HETATM 6149 O O . HOH T 10 . ? 13.997 41.165 53.376 1.00 22.44 ? 1121 HOH A O 1 HETATM 6150 O O . HOH T 10 . ? 32.759 87.779 30.682 1.00 45.57 ? 1122 HOH A O 1 HETATM 6151 O O . HOH T 10 . ? 35.091 44.048 68.030 1.00 45.38 ? 1123 HOH A O 1 HETATM 6152 O O . HOH T 10 . ? 22.956 76.266 25.344 1.00 40.12 ? 1124 HOH A O 1 HETATM 6153 O O . HOH T 10 . ? 6.412 76.322 60.667 1.00 20.84 ? 1125 HOH A O 1 HETATM 6154 O O . HOH T 10 . ? 19.116 42.877 45.973 1.00 21.16 ? 1126 HOH A O 1 HETATM 6155 O O . HOH T 10 . ? -4.517 56.574 33.817 1.00 48.01 ? 1127 HOH A O 1 HETATM 6156 O O . HOH T 10 . ? 27.998 45.482 68.756 1.00 30.83 ? 1128 HOH A O 1 HETATM 6157 O O . HOH T 10 . ? 13.258 45.775 40.352 1.00 44.22 ? 1129 HOH A O 1 HETATM 6158 O O . HOH T 10 . ? 29.047 40.590 64.685 1.00 32.19 ? 1130 HOH A O 1 HETATM 6159 O O . HOH T 10 . ? -7.532 42.007 40.741 1.00 45.47 ? 1131 HOH A O 1 HETATM 6160 O O . HOH T 10 . ? 28.474 29.884 61.977 1.00 47.69 ? 1132 HOH A O 1 HETATM 6161 O O . HOH T 10 . ? 19.426 60.465 49.899 1.00 31.25 ? 1133 HOH A O 1 HETATM 6162 O O . HOH T 10 . ? 6.769 58.761 37.105 1.00 18.30 ? 1134 HOH A O 1 HETATM 6163 O O . HOH T 10 . ? 14.355 32.016 29.543 1.00 27.53 ? 1135 HOH A O 1 HETATM 6164 O O . HOH T 10 . ? 23.515 69.006 42.812 1.00 24.29 ? 1136 HOH A O 1 HETATM 6165 O O . HOH T 10 . ? 33.162 60.819 68.267 1.00 53.20 ? 1137 HOH A O 1 HETATM 6166 O O . HOH T 10 . ? 16.345 29.199 28.128 1.00 35.65 ? 1138 HOH A O 1 HETATM 6167 O O . HOH T 10 . ? 39.374 57.656 57.498 1.00 41.18 ? 1139 HOH A O 1 HETATM 6168 O O . HOH T 10 . ? 39.471 43.932 58.036 1.00 37.21 ? 1140 HOH A O 1 HETATM 6169 O O . HOH T 10 . ? 17.926 40.839 32.142 1.00 23.86 ? 1141 HOH A O 1 HETATM 6170 O O . HOH T 10 . ? 18.844 69.348 65.523 1.00 31.74 ? 1142 HOH A O 1 HETATM 6171 O O . HOH T 10 . ? 40.580 32.641 39.323 1.00 44.46 ? 1143 HOH A O 1 HETATM 6172 O O . HOH T 10 . ? -2.083 45.480 65.725 1.00 45.26 ? 1144 HOH A O 1 HETATM 6173 O O . HOH T 10 . ? 26.235 23.659 45.668 1.00 31.72 ? 1145 HOH A O 1 HETATM 6174 O O . HOH T 10 . ? 25.885 37.378 37.852 1.00 24.70 ? 1146 HOH A O 1 HETATM 6175 O O . HOH T 10 . ? 10.954 77.348 28.338 1.00 34.13 ? 1147 HOH A O 1 HETATM 6176 O O . HOH T 10 . ? 12.820 70.003 32.389 1.00 30.73 ? 1148 HOH A O 1 HETATM 6177 O O . HOH T 10 . ? 29.108 79.512 27.101 1.00 42.31 ? 1149 HOH A O 1 HETATM 6178 O O . HOH T 10 . ? 20.572 65.646 67.093 1.00 52.66 ? 1150 HOH A O 1 HETATM 6179 O O . HOH T 10 . ? -4.583 54.030 34.311 1.00 35.50 ? 1151 HOH A O 1 HETATM 6180 O O . HOH T 10 . ? 12.379 48.159 37.298 1.00 31.04 ? 1152 HOH A O 1 HETATM 6181 O O . HOH T 10 . ? 18.471 33.805 43.373 1.00 25.67 ? 1153 HOH A O 1 HETATM 6182 O O . HOH T 10 . ? 34.405 41.916 50.170 1.00 37.35 ? 1154 HOH A O 1 HETATM 6183 O O . HOH T 10 . ? 18.622 85.701 53.482 1.00 49.24 ? 1155 HOH A O 1 HETATM 6184 O O . HOH T 10 . ? 36.865 52.466 68.448 1.00 41.54 ? 1156 HOH A O 1 HETATM 6185 O O . HOH T 10 . ? 11.114 27.768 54.160 1.00 26.09 ? 1157 HOH A O 1 HETATM 6186 O O . HOH T 10 . ? 9.893 70.490 38.171 1.00 34.39 ? 1158 HOH A O 1 HETATM 6187 O O . HOH T 10 . ? 20.563 44.913 47.377 1.00 26.64 ? 1159 HOH A O 1 HETATM 6188 O O . HOH T 10 . ? 13.619 30.105 39.973 1.00 28.02 ? 1160 HOH A O 1 HETATM 6189 O O . HOH T 10 . ? 9.553 61.269 57.386 1.00 18.60 ? 1161 HOH A O 1 HETATM 6190 O O . HOH T 10 . ? 14.571 73.748 23.438 1.00 49.05 ? 1162 HOH A O 1 HETATM 6191 O O . HOH T 10 . ? 5.786 69.250 55.069 1.00 20.56 ? 1163 HOH A O 1 HETATM 6192 O O . HOH T 10 . ? -2.166 55.987 45.914 1.00 24.95 ? 1164 HOH A O 1 HETATM 6193 O O . HOH T 10 . ? 32.348 27.642 56.523 1.00 41.41 ? 1165 HOH A O 1 HETATM 6194 O O . HOH T 10 . ? 26.362 62.721 65.487 1.00 39.75 ? 1166 HOH A O 1 HETATM 6195 O O . HOH T 10 . ? 3.596 28.043 41.125 1.00 28.36 ? 1167 HOH A O 1 HETATM 6196 O O . HOH T 10 . ? 21.591 75.494 66.644 1.00 40.49 ? 1168 HOH A O 1 HETATM 6197 O O . HOH T 10 . ? 25.063 33.129 67.694 1.00 35.50 ? 1169 HOH A O 1 HETATM 6198 O O . HOH T 10 . ? 9.124 69.478 40.583 1.00 19.87 ? 1170 HOH A O 1 HETATM 6199 O O . HOH T 10 . ? 11.821 27.926 29.334 1.00 42.14 ? 1171 HOH A O 1 HETATM 6200 O O . HOH T 10 . ? 8.418 50.820 40.242 1.00 26.30 ? 1172 HOH A O 1 HETATM 6201 O O . HOH T 10 . ? -4.261 53.563 36.968 1.00 33.63 ? 1173 HOH A O 1 HETATM 6202 O O . HOH T 10 . ? 2.650 33.464 45.132 1.00 24.23 ? 1174 HOH A O 1 HETATM 6203 O O . HOH T 10 . ? 3.605 72.392 43.279 1.00 19.56 ? 1175 HOH A O 1 HETATM 6204 O O . HOH T 10 . ? 13.376 83.287 55.442 1.00 34.81 ? 1176 HOH A O 1 HETATM 6205 O O . HOH T 10 . ? 20.757 46.199 36.390 1.00 27.68 ? 1177 HOH A O 1 HETATM 6206 O O . HOH T 10 . ? 21.386 24.094 27.387 1.00 52.76 ? 1178 HOH A O 1 HETATM 6207 O O . HOH T 10 . ? 28.980 26.224 36.195 1.00 34.56 ? 1179 HOH A O 1 HETATM 6208 O O . HOH T 10 . ? 12.056 35.351 53.558 1.00 24.70 ? 1180 HOH A O 1 HETATM 6209 O O . HOH T 10 . ? 0.441 63.478 47.729 1.00 26.73 ? 1181 HOH A O 1 HETATM 6210 O O . HOH T 10 . ? 25.445 67.400 29.748 1.00 39.24 ? 1182 HOH A O 1 HETATM 6211 O O . HOH T 10 . ? 4.608 62.456 74.837 1.00 28.62 ? 1183 HOH A O 1 HETATM 6212 O O . HOH T 10 . ? 11.685 50.554 36.389 1.00 26.57 ? 1184 HOH A O 1 HETATM 6213 O O . HOH T 10 . ? 30.708 72.547 47.598 1.00 44.74 ? 1185 HOH A O 1 HETATM 6214 O O . HOH T 10 . ? 4.948 50.052 27.837 1.00 42.83 ? 1186 HOH A O 1 HETATM 6215 O O . HOH T 10 . ? 13.847 80.302 67.648 1.00 36.59 ? 1187 HOH A O 1 HETATM 6216 O O . HOH T 10 . ? -2.830 38.184 32.306 1.00 34.53 ? 1188 HOH A O 1 HETATM 6217 O O . HOH T 10 . ? 38.773 55.472 61.995 1.00 41.32 ? 1189 HOH A O 1 HETATM 6218 O O . HOH T 10 . ? 18.258 24.008 35.954 1.00 43.87 ? 1190 HOH A O 1 HETATM 6219 O O . HOH T 10 . ? 5.138 40.257 23.035 1.00 39.80 ? 1191 HOH A O 1 HETATM 6220 O O . HOH T 10 . ? 21.779 74.923 60.354 1.00 30.91 ? 1192 HOH A O 1 HETATM 6221 O O . HOH T 10 . ? 20.173 81.114 62.712 1.00 50.91 ? 1193 HOH A O 1 HETATM 6222 O O . HOH T 10 . ? 25.250 66.974 56.433 1.00 31.38 ? 1194 HOH A O 1 HETATM 6223 O O . HOH T 10 . ? -2.175 34.244 40.451 1.00 28.34 ? 1195 HOH A O 1 HETATM 6224 O O . HOH T 10 . ? 29.982 27.320 33.713 1.00 33.43 ? 1196 HOH A O 1 HETATM 6225 O O . HOH T 10 . ? 0.318 57.219 45.272 1.00 21.41 ? 1197 HOH A O 1 HETATM 6226 O O . HOH T 10 . ? 3.973 70.804 64.105 1.00 22.21 ? 1198 HOH A O 1 HETATM 6227 O O . HOH T 10 . ? 13.353 78.232 63.316 1.00 31.02 ? 1199 HOH A O 1 HETATM 6228 O O . HOH T 10 . ? -3.083 38.975 62.819 1.00 35.97 ? 1200 HOH A O 1 HETATM 6229 O O . HOH T 10 . ? 24.017 82.976 24.140 1.00 54.60 ? 1201 HOH A O 1 HETATM 6230 O O . HOH T 10 . ? 18.048 60.051 70.099 1.00 51.89 ? 1202 HOH A O 1 HETATM 6231 O O . HOH T 10 . ? 4.321 67.354 51.144 1.00 22.25 ? 1203 HOH A O 1 HETATM 6232 O O . HOH T 10 . ? 5.094 27.646 30.806 1.00 51.37 ? 1204 HOH A O 1 HETATM 6233 O O . HOH T 10 . ? 14.703 59.362 74.285 1.00 29.18 ? 1205 HOH A O 1 HETATM 6234 O O . HOH T 10 . ? 16.587 80.267 20.956 1.00 47.52 ? 1206 HOH A O 1 HETATM 6235 O O . HOH T 10 . ? 25.683 35.841 68.072 1.00 33.35 ? 1207 HOH A O 1 HETATM 6236 O O . HOH T 10 . ? -4.514 55.615 51.465 1.00 26.65 ? 1208 HOH A O 1 HETATM 6237 O O . HOH T 10 . ? 6.549 61.183 66.819 1.00 25.71 ? 1209 HOH A O 1 HETATM 6238 O O . HOH T 10 . ? 10.458 84.480 50.967 1.00 32.28 ? 1210 HOH A O 1 HETATM 6239 O O . HOH T 10 . ? 34.521 46.113 69.683 1.00 50.83 ? 1211 HOH A O 1 HETATM 6240 O O . HOH T 10 . ? 5.702 63.180 70.185 1.00 25.87 ? 1212 HOH A O 1 HETATM 6241 O O . HOH T 10 . ? 41.015 45.504 19.848 1.00 50.40 ? 1213 HOH A O 1 HETATM 6242 O O . HOH T 10 . ? 9.378 75.519 69.235 1.00 50.67 ? 1214 HOH A O 1 HETATM 6243 O O . HOH T 10 . ? 10.232 81.471 63.310 1.00 33.66 ? 1215 HOH A O 1 HETATM 6244 O O . HOH T 10 . ? 3.400 38.924 26.826 1.00 45.36 ? 1216 HOH A O 1 HETATM 6245 O O . HOH T 10 . ? 36.767 40.323 55.311 1.00 45.90 ? 1217 HOH A O 1 HETATM 6246 O O . HOH T 10 . ? 6.849 76.276 37.377 1.00 30.04 ? 1218 HOH A O 1 HETATM 6247 O O . HOH T 10 . ? 20.031 56.527 23.036 1.00 47.37 ? 1219 HOH A O 1 HETATM 6248 O O . HOH T 10 . ? 16.752 68.605 64.106 1.00 26.37 ? 1220 HOH A O 1 HETATM 6249 O O . HOH T 10 . ? -12.867 47.671 37.324 1.00 35.54 ? 1221 HOH A O 1 HETATM 6250 O O . HOH T 10 . ? 35.953 43.091 57.390 1.00 34.47 ? 1222 HOH A O 1 HETATM 6251 O O . HOH T 10 . ? 12.791 33.170 70.660 1.00 41.03 ? 1223 HOH A O 1 HETATM 6252 O O . HOH T 10 . ? -7.000 51.967 51.167 1.00 23.44 ? 1224 HOH A O 1 HETATM 6253 O O . HOH T 10 . ? 5.919 44.994 25.349 1.00 52.60 ? 1225 HOH A O 1 HETATM 6254 O O . HOH T 10 . ? 27.072 64.813 59.427 1.00 46.49 ? 1226 HOH A O 1 HETATM 6255 O O . HOH T 10 . ? 10.502 52.087 39.097 1.00 33.12 ? 1227 HOH A O 1 HETATM 6256 O O . HOH T 10 . ? 37.101 59.410 63.521 1.00 42.83 ? 1228 HOH A O 1 HETATM 6257 O O . HOH T 10 . ? 17.111 82.208 37.014 1.00 29.62 ? 1229 HOH A O 1 HETATM 6258 O O . HOH T 10 . ? 19.655 58.677 68.526 1.00 51.71 ? 1230 HOH A O 1 HETATM 6259 O O . HOH T 10 . ? 6.565 76.918 67.148 1.00 29.72 ? 1231 HOH A O 1 HETATM 6260 O O . HOH T 10 . ? 13.425 66.065 35.003 1.00 31.63 ? 1232 HOH A O 1 HETATM 6261 O O . HOH T 10 . ? 25.391 75.163 21.692 1.00 51.26 ? 1233 HOH A O 1 HETATM 6262 O O . HOH T 10 . ? -1.320 62.032 62.056 1.00 31.40 ? 1234 HOH A O 1 HETATM 6263 O O . HOH T 10 . ? 17.804 32.553 70.449 1.00 36.86 ? 1235 HOH A O 1 HETATM 6264 O O . HOH T 10 . ? 14.964 62.176 72.987 1.00 28.02 ? 1236 HOH A O 1 HETATM 6265 O O . HOH T 10 . ? 17.863 86.919 25.542 1.00 60.89 ? 1237 HOH A O 1 HETATM 6266 O O . HOH T 10 . ? 16.506 47.664 40.681 1.00 35.19 ? 1238 HOH A O 1 HETATM 6267 O O . HOH T 10 . ? 9.244 50.997 46.117 1.00 17.90 ? 1239 HOH A O 1 HETATM 6268 O O . HOH T 10 . ? 16.489 69.914 20.474 1.00 59.48 ? 1240 HOH A O 1 HETATM 6269 O O . HOH T 10 . ? -4.455 59.876 56.884 1.00 20.15 ? 1241 HOH A O 1 HETATM 6270 O O . HOH T 10 . ? -5.534 60.108 59.455 1.00 20.21 ? 1242 HOH A O 1 HETATM 6271 O O . HOH T 10 . ? 29.904 25.496 47.287 1.00 43.12 ? 1243 HOH A O 1 HETATM 6272 O O . HOH T 10 . ? 16.753 63.590 68.803 1.00 48.89 ? 1244 HOH A O 1 HETATM 6273 O O . HOH T 10 . ? 37.516 41.931 52.493 1.00 49.60 ? 1245 HOH A O 1 HETATM 6274 O O . HOH T 10 . ? 12.457 28.771 60.562 1.00 49.30 ? 1246 HOH A O 1 HETATM 6275 O O . HOH T 10 . ? 16.188 57.240 34.903 1.00 42.35 ? 1247 HOH A O 1 HETATM 6276 O O . HOH T 10 . ? 25.806 25.556 20.258 1.00 50.78 ? 1248 HOH A O 1 HETATM 6277 O O . HOH T 10 . ? 15.018 82.155 28.153 1.00 39.93 ? 1249 HOH A O 1 HETATM 6278 O O . HOH T 10 . ? 30.881 70.776 37.566 1.00 52.44 ? 1250 HOH A O 1 HETATM 6279 O O . HOH T 10 . ? 41.302 56.251 55.891 1.00 54.60 ? 1251 HOH A O 1 HETATM 6280 O O . HOH T 10 . ? 39.100 31.504 45.835 1.00 45.30 ? 1252 HOH A O 1 HETATM 6281 O O . HOH T 10 . ? 17.938 52.731 74.928 1.00 34.20 ? 1253 HOH A O 1 HETATM 6282 O O . HOH T 10 . ? -5.080 42.369 50.350 1.00 41.88 ? 1254 HOH A O 1 HETATM 6283 O O . HOH T 10 . ? 28.204 41.977 68.561 1.00 45.00 ? 1255 HOH A O 1 HETATM 6284 O O . HOH T 10 . ? -5.440 34.428 47.363 1.00 41.65 ? 1256 HOH A O 1 HETATM 6285 O O . HOH T 10 . ? -3.505 60.608 61.549 1.00 21.51 ? 1257 HOH A O 1 HETATM 6286 O O . HOH T 10 . ? 15.230 72.190 21.646 1.00 57.91 ? 1258 HOH A O 1 HETATM 6287 O O . HOH T 10 . ? 11.712 41.316 55.212 1.00 23.73 ? 1259 HOH A O 1 HETATM 6288 O O . HOH T 10 . ? 19.160 28.055 35.112 1.00 24.64 ? 1260 HOH A O 1 HETATM 6289 O O . HOH T 10 . ? 29.661 61.172 52.714 1.00 36.49 ? 1261 HOH A O 1 HETATM 6290 O O . HOH T 10 . ? 19.941 46.395 39.294 1.00 29.20 ? 1262 HOH A O 1 HETATM 6291 O O . HOH T 10 . ? 20.809 50.795 75.944 1.00 38.09 ? 1263 HOH A O 1 HETATM 6292 O O . HOH T 10 . ? 13.634 29.598 28.576 1.00 27.59 ? 1264 HOH A O 1 HETATM 6293 O O . HOH T 10 . ? 6.045 24.925 56.387 1.00 59.12 ? 1265 HOH A O 1 HETATM 6294 O O . HOH T 10 . ? 28.332 67.941 52.895 1.00 50.85 ? 1266 HOH A O 1 HETATM 6295 O O . HOH T 10 . ? 20.477 63.444 71.700 1.00 43.15 ? 1267 HOH A O 1 HETATM 6296 O O . HOH T 10 . ? -10.031 44.143 46.921 1.00 33.53 ? 1268 HOH A O 1 HETATM 6297 O O . HOH T 10 . ? 30.025 76.317 43.204 1.00 55.49 ? 1269 HOH A O 1 HETATM 6298 O O . HOH T 10 . ? 15.617 70.587 40.725 1.00 28.90 ? 1270 HOH A O 1 HETATM 6299 O O . HOH T 10 . ? 23.576 74.962 65.308 1.00 40.40 ? 1271 HOH A O 1 HETATM 6300 O O . HOH T 10 . ? 8.148 56.892 75.511 1.00 33.61 ? 1272 HOH A O 1 HETATM 6301 O O . HOH T 10 . ? 25.753 58.915 46.356 1.00 37.74 ? 1273 HOH A O 1 HETATM 6302 O O . HOH T 10 . ? 23.379 56.010 31.348 1.00 46.51 ? 1274 HOH A O 1 HETATM 6303 O O . HOH T 10 . ? 6.152 68.781 36.955 1.00 35.21 ? 1275 HOH A O 1 HETATM 6304 O O . HOH T 10 . ? 26.781 31.256 63.713 1.00 50.23 ? 1276 HOH A O 1 HETATM 6305 O O . HOH T 10 . ? 12.569 50.483 27.315 1.00 53.57 ? 1277 HOH A O 1 HETATM 6306 O O . HOH T 10 . ? 38.742 39.412 35.200 1.00 49.12 ? 1278 HOH A O 1 HETATM 6307 O O . HOH T 10 . ? 11.202 52.954 27.954 1.00 50.26 ? 1279 HOH A O 1 HETATM 6308 O O . HOH T 10 . ? -3.883 57.972 46.059 1.00 22.17 ? 1280 HOH A O 1 HETATM 6309 O O . HOH T 10 . ? 3.141 65.368 50.471 1.00 26.88 ? 1281 HOH A O 1 HETATM 6310 O O . HOH T 10 . ? 25.197 69.661 60.502 1.00 54.44 ? 1282 HOH A O 1 HETATM 6311 O O . HOH T 10 . ? 27.084 20.465 39.835 1.00 36.57 ? 1283 HOH A O 1 HETATM 6312 O O . HOH T 10 . ? 23.793 73.643 59.096 1.00 32.81 ? 1284 HOH A O 1 HETATM 6313 O O . HOH T 10 . ? 27.414 28.536 28.147 1.00 51.44 ? 1285 HOH A O 1 HETATM 6314 O O . HOH T 10 . ? -8.500 43.454 34.593 1.00 46.33 ? 1286 HOH A O 1 HETATM 6315 O O . HOH T 10 . ? 24.213 78.331 52.737 1.00 33.78 ? 1287 HOH A O 1 HETATM 6316 O O . HOH T 10 . ? 21.477 73.786 68.783 1.00 56.74 ? 1288 HOH A O 1 HETATM 6317 O O . HOH T 10 . ? 38.382 43.164 55.167 1.00 45.84 ? 1289 HOH A O 1 HETATM 6318 O O . HOH T 10 . ? -0.786 32.724 60.579 1.00 37.48 ? 1290 HOH A O 1 HETATM 6319 O O . HOH T 10 . ? 19.320 36.372 43.046 1.00 25.29 ? 1291 HOH A O 1 HETATM 6320 O O . HOH T 10 . ? 27.627 24.753 18.466 1.00 51.92 ? 1292 HOH A O 1 HETATM 6321 O O . HOH T 10 . ? 5.639 56.900 35.463 1.00 45.35 ? 1293 HOH A O 1 HETATM 6322 O O . HOH T 10 . ? 10.613 83.188 56.297 1.00 54.23 ? 1294 HOH A O 1 HETATM 6323 O O . HOH T 10 . ? -4.292 47.215 24.813 1.00 59.25 ? 1295 HOH A O 1 HETATM 6324 O O . HOH T 10 . ? 11.516 38.765 56.406 1.00 32.07 ? 1296 HOH A O 1 HETATM 6325 O O . HOH T 10 . ? 23.271 78.944 22.467 1.00 52.07 ? 1297 HOH A O 1 HETATM 6326 O O . HOH T 10 . ? 2.355 41.484 26.533 1.00 48.70 ? 1298 HOH A O 1 HETATM 6327 O O . HOH T 10 . ? 27.095 65.764 45.832 1.00 38.50 ? 1299 HOH A O 1 HETATM 6328 O O . HOH T 10 . ? 14.077 69.162 75.224 1.00 39.76 ? 1300 HOH A O 1 HETATM 6329 O O . HOH T 10 . ? 24.166 83.896 45.616 1.00 44.92 ? 1301 HOH A O 1 HETATM 6330 O O . HOH T 10 . ? 9.462 60.215 30.987 1.00 53.85 ? 1302 HOH A O 1 HETATM 6331 O O . HOH T 10 . ? 31.784 74.358 43.832 1.00 54.60 ? 1303 HOH A O 1 HETATM 6332 O O . HOH T 10 . ? 7.580 73.789 80.240 1.00 39.70 ? 1304 HOH A O 1 HETATM 6333 O O . HOH T 10 . ? -0.831 58.387 42.959 1.00 21.74 ? 1305 HOH A O 1 HETATM 6334 O O . HOH T 10 . ? 0.600 69.136 79.060 0.50 35.95 ? 1306 HOH A O 1 HETATM 6335 O O . HOH T 10 . ? 3.403 27.815 57.217 1.00 52.41 ? 1307 HOH A O 1 HETATM 6336 O O . HOH T 10 . ? 12.114 23.230 43.877 1.00 51.32 ? 1308 HOH A O 1 HETATM 6337 O O . HOH T 10 . ? 30.612 71.988 43.218 1.00 37.22 ? 1309 HOH A O 1 HETATM 6338 O O . HOH T 10 . ? 9.594 28.976 38.078 1.00 45.92 ? 1310 HOH A O 1 HETATM 6339 O O . HOH T 10 . ? 8.775 73.752 78.162 1.00 45.05 ? 1311 HOH A O 1 HETATM 6340 O O . HOH T 10 . ? 22.205 84.028 49.559 1.00 37.20 ? 1312 HOH A O 1 HETATM 6341 O O . HOH T 10 . ? 11.930 69.920 40.847 1.00 33.74 ? 1313 HOH A O 1 HETATM 6342 O O . HOH T 10 . ? 20.442 38.919 75.851 1.00 54.02 ? 1314 HOH A O 1 HETATM 6343 O O . HOH T 10 . ? 25.349 25.451 25.892 1.00 53.29 ? 1315 HOH A O 1 HETATM 6344 O O . HOH T 10 . ? 30.024 60.860 50.077 1.00 50.42 ? 1316 HOH A O 1 HETATM 6345 O O . HOH T 10 . ? -0.211 58.081 35.135 1.00 58.88 ? 1317 HOH A O 1 HETATM 6346 O O . HOH T 10 . ? 1.329 59.572 46.063 1.00 23.79 ? 1318 HOH A O 1 HETATM 6347 O O . HOH T 10 . ? 6.532 52.462 27.390 1.00 55.10 ? 1319 HOH A O 1 HETATM 6348 O O . HOH T 10 . ? -4.556 35.547 55.919 1.00 57.27 ? 1320 HOH A O 1 HETATM 6349 O O . HOH T 10 . ? -12.521 45.795 35.443 1.00 44.18 ? 1321 HOH A O 1 HETATM 6350 O O . HOH T 10 . ? 24.487 81.856 50.078 1.00 48.85 ? 1322 HOH A O 1 HETATM 6351 O O . HOH T 10 . ? 39.519 64.329 52.712 1.00 63.23 ? 1323 HOH A O 1 HETATM 6352 O O . HOH T 10 . ? 6.621 54.259 75.266 1.00 33.33 ? 1324 HOH A O 1 HETATM 6353 O O . HOH T 10 . ? -8.245 49.843 49.658 1.00 38.19 ? 1325 HOH A O 1 HETATM 6354 O O . HOH T 10 . ? 23.288 24.201 25.663 1.00 57.53 ? 1326 HOH A O 1 HETATM 6355 O O . HOH T 10 . ? 22.865 80.021 60.447 1.00 51.19 ? 1327 HOH A O 1 HETATM 6356 O O . HOH T 10 . ? 1.197 60.356 43.457 0.50 11.76 ? 1328 HOH A O 1 HETATM 6357 O O . HOH T 10 . ? 34.670 35.878 57.925 1.00 47.40 ? 1329 HOH A O 1 HETATM 6358 O O . HOH T 10 . ? 13.630 81.960 65.526 1.00 46.65 ? 1330 HOH A O 1 HETATM 6359 O O . HOH T 10 . ? 21.292 48.736 38.963 1.00 47.90 ? 1331 HOH A O 1 HETATM 6360 O O . HOH T 10 . ? 25.658 72.155 60.332 0.50 30.54 ? 1332 HOH A O 1 HETATM 6361 O O . HOH T 10 . ? 28.916 26.072 31.461 1.00 44.48 ? 1333 HOH A O 1 HETATM 6362 O O . HOH T 10 . ? -0.194 66.726 61.306 1.00 34.03 ? 1334 HOH A O 1 HETATM 6363 O O . HOH T 10 . ? 32.211 80.684 40.924 1.00 52.48 ? 1335 HOH A O 1 HETATM 6364 O O . HOH T 10 . ? 24.392 79.918 55.134 1.00 46.63 ? 1336 HOH A O 1 HETATM 6365 O O . HOH T 10 . ? 40.026 57.161 60.172 1.00 45.37 ? 1337 HOH A O 1 HETATM 6366 O O . HOH T 10 . ? 31.890 77.251 37.920 1.00 53.44 ? 1338 HOH A O 1 HETATM 6367 O O . HOH T 10 . ? 16.543 85.211 40.755 1.00 43.52 ? 1339 HOH A O 1 HETATM 6368 O O . HOH T 10 . ? 14.474 70.497 29.940 1.00 37.24 ? 1340 HOH A O 1 HETATM 6369 O O . HOH T 10 . ? 18.671 22.188 34.364 1.00 40.38 ? 1341 HOH A O 1 HETATM 6370 O O . HOH T 10 . ? 36.068 42.216 46.798 1.00 42.17 ? 1342 HOH A O 1 HETATM 6371 O O . HOH T 10 . ? 24.627 22.262 31.692 1.00 52.75 ? 1343 HOH A O 1 HETATM 6372 O O . HOH T 10 . ? 15.268 24.952 32.432 1.00 41.45 ? 1344 HOH A O 1 HETATM 6373 O O . HOH T 10 . ? 26.135 86.122 45.307 1.00 53.66 ? 1345 HOH A O 1 HETATM 6374 O O . HOH T 10 . ? 11.662 25.054 51.586 1.00 49.71 ? 1346 HOH A O 1 HETATM 6375 O O . HOH T 10 . ? 26.000 61.032 31.034 1.00 57.36 ? 1347 HOH A O 1 HETATM 6376 O O . HOH T 10 . ? 28.905 64.030 68.555 1.00 46.39 ? 1348 HOH A O 1 HETATM 6377 O O . HOH T 10 . ? -8.518 47.950 51.797 1.00 34.44 ? 1349 HOH A O 1 HETATM 6378 O O . HOH T 10 . ? 19.205 48.767 40.331 1.00 43.27 ? 1350 HOH A O 1 HETATM 6379 O O . HOH T 10 . ? 13.926 48.462 39.859 1.00 31.30 ? 1351 HOH A O 1 HETATM 6380 O O . HOH T 10 . ? 37.327 56.872 63.707 1.00 43.51 ? 1352 HOH A O 1 HETATM 6381 O O . HOH T 10 . ? 26.435 65.196 28.317 1.00 49.95 ? 1353 HOH A O 1 HETATM 6382 O O . HOH T 10 . ? 30.159 68.333 45.722 1.00 49.91 ? 1354 HOH A O 1 HETATM 6383 O O . HOH T 10 . ? 11.923 56.762 77.113 1.00 41.45 ? 1355 HOH A O 1 HETATM 6384 O O . HOH T 10 . ? 26.195 82.615 47.729 1.00 61.73 ? 1356 HOH A O 1 HETATM 6385 O O . HOH T 10 . ? -4.182 58.218 36.050 1.00 39.51 ? 1357 HOH A O 1 HETATM 6386 O O . HOH T 10 . ? 28.167 36.357 67.439 1.00 48.16 ? 1358 HOH A O 1 HETATM 6387 O O . HOH T 10 . ? 25.757 74.798 57.852 1.00 53.69 ? 1359 HOH A O 1 HETATM 6388 O O . HOH T 10 . ? 27.507 66.366 54.961 1.00 35.46 ? 1360 HOH A O 1 HETATM 6389 O O . HOH T 10 . ? 26.807 17.263 40.531 1.00 42.71 ? 1361 HOH A O 1 HETATM 6390 O O . HOH T 10 . ? 29.671 38.242 66.106 0.50 29.32 ? 1362 HOH A O 1 HETATM 6391 O O . HOH T 10 . ? 14.798 60.518 76.757 1.00 44.82 ? 1363 HOH A O 1 HETATM 6392 O O . HOH T 10 . ? 8.466 75.225 75.219 1.00 37.40 ? 1364 HOH A O 1 HETATM 6393 O O . HOH T 10 . ? 12.864 58.748 78.649 1.00 41.04 ? 1365 HOH A O 1 HETATM 6394 O O . HOH T 10 . ? 16.933 59.145 79.563 1.00 51.79 ? 1366 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . LYS A 1 ? 0.8802 0.6719 0.6079 0.2018 -0.0367 -0.0325 55 LYS A N 2 C CA . LYS A 1 ? 0.8680 0.6685 0.6072 0.1947 -0.0386 -0.0342 55 LYS A CA 3 C C . LYS A 1 ? 0.8320 0.6456 0.5899 0.1824 -0.0330 -0.0321 55 LYS A C 4 O O . LYS A 1 ? 0.8175 0.6356 0.5841 0.1778 -0.0325 -0.0327 55 LYS A O 5 C CB . LYS A 1 ? 0.8788 0.6796 0.6215 0.1958 -0.0506 -0.0419 55 LYS A CB 6 C CG . LYS A 1 ? 0.9151 0.7132 0.6524 0.1992 -0.0547 -0.0437 55 LYS A CG 7 C CD . LYS A 1 ? 0.9541 0.7635 0.7063 0.1891 -0.0519 -0.0427 55 LYS A CD 8 C CE . LYS A 1 ? 0.9729 0.7796 0.7200 0.1923 -0.0558 -0.0443 55 LYS A CE 9 N NZ . LYS A 1 ? 0.9807 0.7980 0.7413 0.1827 -0.0520 -0.0426 55 LYS A NZ 10 N N . HIS A 2 ? 0.7999 0.6190 0.5632 0.1775 -0.0289 -0.0296 56 HIS A N 11 C CA . HIS A 2 ? 0.7584 0.5897 0.5390 0.1661 -0.0247 -0.0282 56 HIS A CA 12 C C . HIS A 2 ? 0.7221 0.5603 0.5130 0.1610 -0.0313 -0.0328 56 HIS A C 13 O O . HIS A 2 ? 0.7272 0.5654 0.5159 0.1613 -0.0308 -0.0320 56 HIS A O 14 C CB . HIS A 2 ? 0.7669 0.5996 0.5469 0.1641 -0.0145 -0.0216 56 HIS A CB 15 C CG . HIS A 2 ? 0.7958 0.6233 0.5692 0.1674 -0.0069 -0.0164 56 HIS A CG 16 N ND1 . HIS A 2 ? 0.8173 0.6382 0.5797 0.1729 0.0003 -0.0108 56 HIS A ND1 17 C CD2 . HIS A 2 ? 0.7833 0.6111 0.5598 0.1661 -0.0052 -0.0158 56 HIS A CD2 18 C CE1 . HIS A 2 ? 0.8239 0.6414 0.5834 0.1747 0.0063 -0.0068 56 HIS A CE1 19 N NE2 . HIS A 2 ? 0.8109 0.6325 0.5788 0.1706 0.0029 -0.0099 56 HIS A NE2 20 N N . ASN A 3 ? 0.6659 0.5093 0.4674 0.1569 -0.0375 -0.0376 57 ASN A N 21 C CA . ASN A 3 ? 0.6176 0.4677 0.4303 0.1518 -0.0439 -0.0421 57 ASN A CA 22 C C . ASN A 3 ? 0.5740 0.4342 0.4031 0.1428 -0.0435 -0.0434 57 ASN A C 23 O O . ASN A 3 ? 0.5605 0.4222 0.3913 0.1406 -0.0380 -0.0406 57 ASN A O 24 C CB . ASN A 3 ? 0.6210 0.4649 0.4284 0.1584 -0.0543 -0.0480 57 ASN A CB 25 C CG . ASN A 3 ? 0.6220 0.4599 0.4238 0.1639 -0.0580 -0.0503 57 ASN A CG 26 O OD1 . ASN A 3 ? 0.5810 0.4222 0.3881 0.1604 -0.0544 -0.0489 57 ASN A OD1 27 N ND2 . ASN A 3 ? 0.5982 0.4266 0.3884 0.1731 -0.0652 -0.0538 57 ASN A ND2 28 N N . MET A 4 ? 0.5489 0.4156 0.3899 0.1378 -0.0492 -0.0475 58 MET A N 29 C CA A MET A 4 ? 0.5323 0.4091 0.3891 0.1292 -0.0483 -0.0486 58 MET A CA 30 C CA B MET A 4 ? 0.5208 0.3974 0.3771 0.1292 -0.0479 -0.0483 58 MET A CA 31 C C . MET A 4 ? 0.5178 0.3927 0.3749 0.1311 -0.0504 -0.0505 58 MET A C 32 O O . MET A 4 ? 0.5001 0.3801 0.3640 0.1262 -0.0460 -0.0489 58 MET A O 33 C CB A MET A 4 ? 0.5243 0.4079 0.3937 0.1241 -0.0539 -0.0525 58 MET A CB 34 C CB B MET A 4 ? 0.5072 0.3919 0.3772 0.1229 -0.0520 -0.0514 58 MET A CB 35 C CG A MET A 4 ? 0.5525 0.4470 0.4377 0.1146 -0.0510 -0.0523 58 MET A CG 36 C CG B MET A 4 ? 0.4761 0.3711 0.3600 0.1136 -0.0473 -0.0500 58 MET A CG 37 S SD A MET A 4 ? 0.6134 0.5164 0.5130 0.1078 -0.0547 -0.0550 58 MET A SD 38 S SD B MET A 4 ? 0.4457 0.3494 0.3465 0.1072 -0.0531 -0.0547 58 MET A SD 39 C CE A MET A 4 ? 0.6016 0.5013 0.5042 0.1121 -0.0655 -0.0615 58 MET A CE 40 C CE B MET A 4 ? 0.4494 0.3555 0.3522 0.1049 -0.0536 -0.0542 58 MET A CE 41 N N . LYS A 5 ? 0.5182 0.3854 0.3675 0.1386 -0.0574 -0.0542 59 LYS A N 42 C CA . LYS A 5 ? 0.5219 0.3867 0.3709 0.1411 -0.0600 -0.0563 59 LYS A CA 43 C C . LYS A 5 ? 0.5084 0.3703 0.3504 0.1423 -0.0522 -0.0514 59 LYS A C 44 O O . LYS A 5 ? 0.5257 0.3912 0.3741 0.1390 -0.0505 -0.0514 59 LYS A O 45 C CB . LYS A 5 ? 0.5287 0.3840 0.3679 0.1504 -0.0689 -0.0608 59 LYS A CB 46 C CG . LYS A 5 ? 0.5789 0.4326 0.4201 0.1523 -0.0729 -0.0640 59 LYS A CG 47 C CD . LYS A 5 ? 0.7072 0.5548 0.5455 0.1590 -0.0841 -0.0703 59 LYS A CD 48 C CE . LYS A 5 ? 0.7605 0.6075 0.6029 0.1604 -0.0889 -0.0740 59 LYS A CE 49 N NZ . LYS A 5 ? 0.8038 0.6424 0.6318 0.1668 -0.0853 -0.0712 59 LYS A NZ 50 N N . ALA A 6 ? 0.5260 0.3812 0.3550 0.1473 -0.0473 -0.0472 60 ALA A N 51 C CA . ALA A 6 ? 0.5263 0.3788 0.3496 0.1481 -0.0390 -0.0419 60 ALA A CA 52 C C . ALA A 6 ? 0.5048 0.3676 0.3418 0.1384 -0.0328 -0.0393 60 ALA A C 53 O O . ALA A 6 ? 0.4899 0.3538 0.3296 0.1367 -0.0296 -0.0380 60 ALA A O 54 C CB . ALA A 6 ? 0.5509 0.3960 0.3605 0.1539 -0.0340 -0.0373 60 ALA A CB 55 N N . PHE A 7 ? 0.4819 0.3517 0.3270 0.1323 -0.0312 -0.0387 61 PHE A N 56 C CA . PHE A 7 ? 0.4602 0.3398 0.3185 0.1232 -0.0263 -0.0369 61 PHE A CA 57 C C . PHE A 7 ? 0.4380 0.3236 0.3075 0.1188 -0.0298 -0.0406 61 PHE A C 58 O O . PHE A 7 ? 0.4420 0.3309 0.3166 0.1152 -0.0256 -0.0389 61 PHE A O 59 C CB . PHE A 7 ? 0.4412 0.3272 0.3063 0.1178 -0.0253 -0.0364 61 PHE A CB 60 C CG . PHE A 7 ? 0.4176 0.3139 0.2969 0.1086 -0.0222 -0.0359 61 PHE A CG 61 C CD1 . PHE A 7 ? 0.4256 0.3242 0.3071 0.1053 -0.0147 -0.0316 61 PHE A CD1 62 C CD2 . PHE A 7 ? 0.4096 0.3130 0.3002 0.1036 -0.0268 -0.0398 61 PHE A CD2 63 C CE1 . PHE A 7 ? 0.4021 0.3102 0.2968 0.0969 -0.0122 -0.0315 61 PHE A CE1 64 C CE2 . PHE A 7 ? 0.3963 0.3088 0.2992 0.0955 -0.0238 -0.0394 61 PHE A CE2 65 C CZ . PHE A 7 ? 0.3994 0.3141 0.3038 0.0924 -0.0168 -0.0354 61 PHE A CZ 66 N N . LEU A 8 ? 0.4401 0.3272 0.3141 0.1190 -0.0373 -0.0456 62 LEU A N 67 C CA . LEU A 8 ? 0.4341 0.3273 0.3198 0.1147 -0.0406 -0.0492 62 LEU A CA 68 C C . LEU A 8 ? 0.4644 0.3532 0.3460 0.1184 -0.0411 -0.0497 62 LEU A C 69 O O . LEU A 8 ? 0.4443 0.3386 0.3346 0.1138 -0.0393 -0.0500 62 LEU A O 70 C CB . LEU A 8 ? 0.4412 0.3357 0.3322 0.1152 -0.0489 -0.0543 62 LEU A CB 71 C CG . LEU A 8 ? 0.4355 0.3362 0.3342 0.1100 -0.0490 -0.0544 62 LEU A CG 72 C CD1 . LEU A 8 ? 0.4549 0.3548 0.3572 0.1121 -0.0578 -0.0595 62 LEU A CD1 73 C CD2 . LEU A 8 ? 0.4141 0.3253 0.3263 0.1008 -0.0445 -0.0532 62 LEU A CD2 74 N N . ASP A 9 ? 0.5063 0.3850 0.3743 0.1270 -0.0433 -0.0498 63 ASP A N 75 C CA . ASP A 9 ? 0.5380 0.4117 0.4013 0.1312 -0.0443 -0.0505 63 ASP A CA 76 C C . ASP A 9 ? 0.5328 0.4069 0.3951 0.1292 -0.0359 -0.0455 63 ASP A C 77 O O . ASP A 9 ? 0.5395 0.4126 0.4024 0.1299 -0.0358 -0.0460 63 ASP A O 78 C CB . ASP A 9 ? 0.5601 0.4219 0.4077 0.1417 -0.0488 -0.0517 63 ASP A CB 79 C CG . ASP A 9 ? 0.5881 0.4485 0.4372 0.1446 -0.0586 -0.0577 63 ASP A CG 80 O OD1 . ASP A 9 ? 0.6249 0.4931 0.4878 0.1391 -0.0625 -0.0613 63 ASP A OD1 81 O OD2 . ASP A 9 ? 0.6407 0.4917 0.4768 0.1529 -0.0625 -0.0587 63 ASP A OD2 82 N N . GLU A 10 ? 0.5188 0.3942 0.3798 0.1267 -0.0291 -0.0408 64 GLU A N 83 C CA . GLU A 10 ? 0.5134 0.3887 0.3740 0.1250 -0.0212 -0.0360 64 GLU A CA 84 C C . GLU A 10 ? 0.4839 0.3692 0.3592 0.1164 -0.0192 -0.0365 64 GLU A C 85 O O . GLU A 10 ? 0.4831 0.3683 0.3598 0.1154 -0.0153 -0.0345 64 GLU A O 86 C CB . GLU A 10 ? 0.5205 0.3934 0.3751 0.1259 -0.0147 -0.0307 64 GLU A CB 87 C CG . GLU A 10 ? 0.5604 0.4337 0.4165 0.1235 -0.0062 -0.0254 64 GLU A CG 88 C CD . GLU A 10 ? 0.6376 0.5029 0.4851 0.1295 -0.0046 -0.0237 64 GLU A CD 89 O OE1 . GLU A 10 ? 0.6626 0.5191 0.4976 0.1376 -0.0077 -0.0245 64 GLU A OE1 90 O OE2 . GLU A 10 ? 0.6003 0.4677 0.4532 0.1264 -0.0004 -0.0217 64 GLU A OE2 91 N N . LEU A 11 ? 0.4575 0.3509 0.3435 0.1106 -0.0220 -0.0394 65 LEU A N 92 C CA . LEU A 11 ? 0.4376 0.3404 0.3372 0.1030 -0.0212 -0.0407 65 LEU A CA 93 C C . LEU A 11 ? 0.4542 0.3564 0.3560 0.1043 -0.0243 -0.0436 65 LEU A C 94 O O . LEU A 11 ? 0.4454 0.3443 0.3446 0.1085 -0.0306 -0.0473 65 LEU A O 95 C CB . LEU A 11 ? 0.4271 0.3374 0.3363 0.0981 -0.0247 -0.0437 65 LEU A CB 96 C CG . LEU A 11 ? 0.3958 0.3077 0.3044 0.0962 -0.0226 -0.0416 65 LEU A CG 97 C CD1 . LEU A 11 ? 0.3769 0.2942 0.2937 0.0931 -0.0278 -0.0454 65 LEU A CD1 98 C CD2 . LEU A 11 ? 0.3799 0.2969 0.2936 0.0904 -0.0155 -0.0377 65 LEU A CD2 99 N N . LYS A 12 ? 0.4468 0.3522 0.3538 0.1007 -0.0202 -0.0421 66 LYS A N 100 C CA . LYS A 12 ? 0.4681 0.3734 0.3778 0.1015 -0.0226 -0.0445 66 LYS A CA 101 C C . LYS A 12 ? 0.4358 0.3507 0.3588 0.0941 -0.0215 -0.0460 66 LYS A C 102 O O . LYS A 12 ? 0.4167 0.3356 0.3440 0.0895 -0.0162 -0.0431 66 LYS A O 103 C CB . LYS A 12 ? 0.4870 0.3853 0.3884 0.1056 -0.0184 -0.0411 66 LYS A CB 104 C CG . LYS A 12 ? 0.5352 0.4228 0.4216 0.1137 -0.0181 -0.0387 66 LYS A CG 105 C CD . LYS A 12 ? 0.6087 0.4908 0.4889 0.1199 -0.0258 -0.0431 66 LYS A CD 106 C CE . LYS A 12 ? 0.6337 0.5040 0.4975 0.1291 -0.0256 -0.0409 66 LYS A CE 107 N NZ . LYS A 12 ? 0.6100 0.4779 0.4678 0.1313 -0.0259 -0.0400 66 LYS A NZ 108 N N . ALA A 13 ? 0.4347 0.3529 0.3642 0.0935 -0.0266 -0.0504 67 ALA A N 109 C CA . ALA A 13 ? 0.4201 0.3463 0.3611 0.0877 -0.0257 -0.0519 67 ALA A CA 110 C C . ALA A 13 ? 0.4311 0.3571 0.3722 0.0862 -0.0206 -0.0493 67 ALA A C 111 O O . ALA A 13 ? 0.4162 0.3489 0.3653 0.0805 -0.0175 -0.0486 67 ALA A O 112 C CB . ALA A 13 ? 0.4264 0.3539 0.3724 0.0890 -0.0319 -0.0568 67 ALA A CB 113 N N . GLU A 14 ? 0.4461 0.3643 0.3784 0.0915 -0.0201 -0.0478 68 GLU A N 114 C CA A GLU A 14 ? 0.4558 0.3735 0.3889 0.0904 -0.0157 -0.0456 68 GLU A CA 115 C CA B GLU A 14 ? 0.4479 0.3652 0.3805 0.0907 -0.0157 -0.0455 68 GLU A CA 116 C C . GLU A 14 ? 0.4442 0.3633 0.3781 0.0870 -0.0093 -0.0410 68 GLU A C 117 O O . GLU A 14 ? 0.4435 0.3660 0.3832 0.0832 -0.0059 -0.0399 68 GLU A O 118 C CB A GLU A 14 ? 0.4804 0.3889 0.4037 0.0972 -0.0165 -0.0448 68 GLU A CB 119 C CB B GLU A 14 ? 0.4666 0.3742 0.3886 0.0977 -0.0164 -0.0445 68 GLU A CB 120 C CG A GLU A 14 ? 0.5197 0.4266 0.4435 0.0966 -0.0122 -0.0423 68 GLU A CG 121 C CG B GLU A 14 ? 0.4790 0.3779 0.3885 0.1036 -0.0149 -0.0413 68 GLU A CG 122 C CD A GLU A 14 ? 0.5731 0.4855 0.5060 0.0933 -0.0141 -0.0456 68 GLU A CD 123 C CD B GLU A 14 ? 0.5206 0.4102 0.4191 0.1118 -0.0192 -0.0428 68 GLU A CD 124 O OE1 A GLU A 14 ? 0.6154 0.5288 0.5514 0.0911 -0.0103 -0.0438 68 GLU A OE1 125 O OE1 B GLU A 14 ? 0.5601 0.4464 0.4568 0.1141 -0.0191 -0.0429 68 GLU A OE1 126 O OE2 A GLU A 14 ? 0.5835 0.4993 0.5207 0.0931 -0.0192 -0.0500 68 GLU A OE2 127 O OE2 B GLU A 14 ? 0.4894 0.3746 0.3807 0.1163 -0.0228 -0.0439 68 GLU A OE2 128 N N . ASN A 15 ? 0.4201 0.3367 0.3487 0.0884 -0.0079 -0.0387 69 ASN A N 129 C CA . ASN A 15 ? 0.4255 0.3440 0.3559 0.0850 -0.0020 -0.0346 69 ASN A CA 130 C C . ASN A 15 ? 0.3947 0.3226 0.3359 0.0779 -0.0015 -0.0359 69 ASN A C 131 O O . ASN A 15 ? 0.3851 0.3160 0.3314 0.0740 0.0024 -0.0339 69 ASN A O 132 C CB . ASN A 15 ? 0.4251 0.3387 0.3473 0.0883 -0.0005 -0.0318 69 ASN A CB 133 C CG . ASN A 15 ? 0.4841 0.3877 0.3946 0.0954 0.0011 -0.0290 69 ASN A CG 134 O OD1 . ASN A 15 ? 0.4936 0.3941 0.4032 0.0966 0.0036 -0.0273 69 ASN A OD1 135 N ND2 . ASN A 15 ? 0.4670 0.3651 0.3682 0.1003 -0.0004 -0.0285 69 ASN A ND2 136 N N . ILE A 16 ? 0.3840 0.3162 0.3288 0.0763 -0.0057 -0.0392 70 ILE A N 137 C CA . ILE A 16 ? 0.3640 0.3050 0.3187 0.0699 -0.0053 -0.0405 70 ILE A CA 138 C C . ILE A 16 ? 0.3671 0.3123 0.3290 0.0667 -0.0044 -0.0418 70 ILE A C 139 O O . ILE A 16 ? 0.3654 0.3156 0.3332 0.0621 -0.0014 -0.0409 70 ILE A O 140 C CB . ILE A 16 ? 0.3611 0.3053 0.3187 0.0694 -0.0101 -0.0439 70 ILE A CB 141 C CG1 . ILE A 16 ? 0.3522 0.2922 0.3027 0.0724 -0.0109 -0.0425 70 ILE A CG1 142 C CG2 . ILE A 16 ? 0.3618 0.3149 0.3295 0.0631 -0.0093 -0.0450 70 ILE A CG2 143 C CD1 . ILE A 16 ? 0.3666 0.3075 0.3186 0.0737 -0.0168 -0.0462 70 ILE A CD1 144 N N . LYS A 17 ? 0.3669 0.3097 0.3277 0.0696 -0.0071 -0.0440 71 LYS A N 145 C CA . LYS A 17 ? 0.3593 0.3053 0.3260 0.0674 -0.0064 -0.0453 71 LYS A CA 146 C C . LYS A 17 ? 0.3594 0.3038 0.3259 0.0662 -0.0015 -0.0419 71 LYS A C 147 O O . LYS A 17 ? 0.3581 0.3077 0.3315 0.0618 0.0003 -0.0421 71 LYS A O 148 C CB . LYS A 17 ? 0.3669 0.3091 0.3310 0.0718 -0.0103 -0.0480 71 LYS A CB 149 C CG . LYS A 17 ? 0.3966 0.3417 0.3666 0.0699 -0.0100 -0.0496 71 LYS A CG 150 C CD . LYS A 17 ? 0.4428 0.3839 0.4101 0.0745 -0.0142 -0.0523 71 LYS A CD 151 C CE . LYS A 17 ? 0.4474 0.3912 0.4201 0.0729 -0.0139 -0.0539 71 LYS A CE 152 N NZ . LYS A 17 ? 0.4533 0.3935 0.4239 0.0773 -0.0184 -0.0569 71 LYS A NZ 153 N N A LYS A 18 ? 0.3693 0.3064 0.3281 0.0702 0.0005 -0.0387 72 LYS A N 154 N N B LYS A 18 ? 0.3727 0.3098 0.3314 0.0702 0.0004 -0.0387 72 LYS A N 155 C CA A LYS A 18 ? 0.3694 0.3047 0.3289 0.0691 0.0054 -0.0351 72 LYS A CA 156 C CA B LYS A 18 ? 0.3767 0.3111 0.3351 0.0697 0.0055 -0.0348 72 LYS A CA 157 C C A LYS A 18 ? 0.3550 0.2953 0.3200 0.0642 0.0085 -0.0334 72 LYS A C 158 C C B LYS A 18 ? 0.3610 0.3004 0.3250 0.0647 0.0089 -0.0329 72 LYS A C 159 O O A LYS A 18 ? 0.3405 0.2841 0.3118 0.0607 0.0106 -0.0331 72 LYS A O 160 O O B LYS A 18 ? 0.3466 0.2880 0.3160 0.0618 0.0115 -0.0319 72 LYS A O 161 C CB A LYS A 18 ? 0.3780 0.3044 0.3282 0.0745 0.0077 -0.0315 72 LYS A CB 162 C CB B LYS A 18 ? 0.3881 0.3139 0.3365 0.0753 0.0073 -0.0314 72 LYS A CB 163 C CG A LYS A 18 ? 0.4005 0.3214 0.3456 0.0794 0.0052 -0.0329 72 LYS A CG 164 C CG B LYS A 18 ? 0.4257 0.3479 0.3736 0.0755 0.0129 -0.0268 72 LYS A CG 165 C CD A LYS A 18 ? 0.4375 0.3489 0.3714 0.0858 0.0069 -0.0295 72 LYS A CD 166 C CD B LYS A 18 ? 0.4754 0.3883 0.4123 0.0819 0.0146 -0.0235 72 LYS A CD 167 C CE A LYS A 18 ? 0.4827 0.3885 0.4116 0.0906 0.0046 -0.0308 72 LYS A CE 168 C CE B LYS A 18 ? 0.4976 0.4084 0.4336 0.0817 0.0203 -0.0185 72 LYS A CE 169 N NZ A LYS A 18 ? 0.5117 0.4083 0.4280 0.0978 0.0040 -0.0292 72 LYS A NZ 170 N NZ B LYS A 18 ? 0.5262 0.4301 0.4510 0.0875 0.0207 -0.0164 72 LYS A NZ 171 N N . PHE A 19 ? 0.3514 0.2923 0.3141 0.0640 0.0084 -0.0326 73 PHE A N 172 C CA . PHE A 19 ? 0.3422 0.2877 0.3097 0.0595 0.0110 -0.0312 73 PHE A CA 173 C C . PHE A 19 ? 0.3336 0.2870 0.3096 0.0546 0.0095 -0.0343 73 PHE A C 174 O O . PHE A 19 ? 0.3253 0.2820 0.3067 0.0509 0.0120 -0.0334 73 PHE A O 175 C CB . PHE A 19 ? 0.3377 0.2823 0.3007 0.0607 0.0105 -0.0302 73 PHE A CB 176 C CG . PHE A 19 ? 0.3572 0.2939 0.3110 0.0660 0.0121 -0.0271 73 PHE A CG 177 C CD1 . PHE A 19 ? 0.4077 0.3395 0.3594 0.0679 0.0163 -0.0236 73 PHE A CD1 178 C CD2 . PHE A 19 ? 0.3362 0.2702 0.2835 0.0692 0.0099 -0.0274 73 PHE A CD2 179 C CE1 . PHE A 19 ? 0.4121 0.3361 0.3546 0.0734 0.0184 -0.0203 73 PHE A CE1 180 C CE2 . PHE A 19 ? 0.3833 0.3095 0.3209 0.0747 0.0116 -0.0244 73 PHE A CE2 181 C CZ . PHE A 19 ? 0.4238 0.3449 0.3588 0.0769 0.0161 -0.0207 73 PHE A CZ 182 N N . LEU A 20 ? 0.3289 0.2852 0.3065 0.0546 0.0057 -0.0379 74 LEU A N 183 C CA . LEU A 20 ? 0.3158 0.2793 0.3010 0.0502 0.0049 -0.0405 74 LEU A CA 184 C C . LEU A 20 ? 0.3295 0.2938 0.3186 0.0488 0.0064 -0.0407 74 LEU A C 185 O O . LEU A 20 ? 0.3149 0.2836 0.3092 0.0451 0.0079 -0.0409 74 LEU A O 186 C CB . LEU A 20 ? 0.3153 0.2818 0.3027 0.0506 0.0009 -0.0442 74 LEU A CB 187 C CG . LEU A 20 ? 0.3274 0.3014 0.3225 0.0464 0.0006 -0.0465 74 LEU A CG 188 C CD1 . LEU A 20 ? 0.2943 0.2719 0.2912 0.0430 0.0023 -0.0452 74 LEU A CD1 189 C CD2 . LEU A 20 ? 0.3177 0.2941 0.3158 0.0472 -0.0030 -0.0499 74 LEU A CD2 190 N N . TYR A 21 ? 0.3321 0.2918 0.3184 0.0521 0.0059 -0.0407 75 TYR A N 191 C CA . TYR A 21 ? 0.3358 0.2957 0.3258 0.0511 0.0072 -0.0409 75 TYR A CA 192 C C . TYR A 21 ? 0.3228 0.2820 0.3147 0.0491 0.0110 -0.0377 75 TYR A C 193 O O . TYR A 21 ? 0.3374 0.3002 0.3351 0.0459 0.0118 -0.0384 75 TYR A O 194 C CB . TYR A 21 ? 0.3486 0.3025 0.3341 0.0556 0.0062 -0.0408 75 TYR A CB 195 C CG . TYR A 21 ? 0.3698 0.3234 0.3590 0.0547 0.0074 -0.0410 75 TYR A CG 196 C CD1 . TYR A 21 ? 0.3958 0.3538 0.3899 0.0532 0.0053 -0.0445 75 TYR A CD1 197 C CD2 . TYR A 21 ? 0.4107 0.3600 0.3993 0.0553 0.0108 -0.0376 75 TYR A CD2 198 C CE1 . TYR A 21 ? 0.4129 0.3706 0.4106 0.0525 0.0061 -0.0449 75 TYR A CE1 199 C CE2 . TYR A 21 ? 0.4640 0.4130 0.4569 0.0544 0.0116 -0.0378 75 TYR A CE2 200 C CZ . TYR A 21 ? 0.4615 0.4146 0.4585 0.0531 0.0091 -0.0416 75 TYR A CZ 201 O OH . TYR A 21 ? 0.5137 0.4664 0.5148 0.0524 0.0097 -0.0420 75 TYR A OH 202 N N . ASN A 22 ? 0.3453 0.2999 0.3326 0.0511 0.0132 -0.0343 76 ASN A N 203 C CA . ASN A 22 ? 0.3435 0.2969 0.3331 0.0495 0.0170 -0.0309 76 ASN A CA 204 C C . ASN A 22 ? 0.3405 0.2999 0.3359 0.0449 0.0175 -0.0315 76 ASN A C 205 O O . ASN A 22 ? 0.3380 0.2985 0.3387 0.0425 0.0194 -0.0305 76 ASN A O 206 C CB . ASN A 22 ? 0.3709 0.3185 0.3539 0.0528 0.0193 -0.0272 76 ASN A CB 207 C CG . ASN A 22 ? 0.4044 0.3504 0.3904 0.0517 0.0236 -0.0233 76 ASN A CG 208 O OD1 . ASN A 22 ? 0.3548 0.3032 0.3429 0.0494 0.0249 -0.0222 76 ASN A OD1 209 N ND2 . ASN A 22 ? 0.4207 0.3624 0.4075 0.0533 0.0259 -0.0213 76 ASN A ND2 210 N N . PHE A 23 ? 0.3255 0.2888 0.3201 0.0437 0.0155 -0.0333 77 PHE A N 211 C CA . PHE A 23 ? 0.3089 0.2773 0.3075 0.0399 0.0158 -0.0337 77 PHE A CA 212 C C . PHE A 23 ? 0.3082 0.2823 0.3122 0.0369 0.0142 -0.0370 77 PHE A C 213 O O . PHE A 23 ? 0.3030 0.2813 0.3099 0.0339 0.0144 -0.0375 77 PHE A O 214 C CB . PHE A 23 ? 0.3036 0.2732 0.2986 0.0402 0.0145 -0.0339 77 PHE A CB 215 C CG . PHE A 23 ? 0.3353 0.2999 0.3247 0.0429 0.0162 -0.0306 77 PHE A CG 216 C CD1 . PHE A 23 ? 0.3354 0.2951 0.3234 0.0446 0.0194 -0.0272 77 PHE A CD1 217 C CD2 . PHE A 23 ? 0.3386 0.3034 0.3242 0.0439 0.0145 -0.0310 77 PHE A CD2 218 C CE1 . PHE A 23 ? 0.3275 0.2824 0.3094 0.0476 0.0213 -0.0240 77 PHE A CE1 219 C CE2 . PHE A 23 ? 0.2815 0.2417 0.2612 0.0467 0.0157 -0.0283 77 PHE A CE2 220 C CZ . PHE A 23 ? 0.3208 0.2760 0.2983 0.0488 0.0193 -0.0247 77 PHE A CZ 221 N N . THR A 24 ? 0.2950 0.2692 0.3002 0.0378 0.0127 -0.0392 78 THR A N 222 C CA . THR A 24 ? 0.2964 0.2761 0.3057 0.0355 0.0112 -0.0425 78 THR A CA 223 C C . THR A 24 ? 0.3045 0.2840 0.3172 0.0353 0.0111 -0.0438 78 THR A C 224 O O . THR A 24 ? 0.2775 0.2608 0.2928 0.0345 0.0097 -0.0467 78 THR A O 225 C CB . THR A 24 ? 0.2908 0.2724 0.2990 0.0368 0.0086 -0.0450 78 THR A CB 226 O OG1 . THR A 24 ? 0.3022 0.2792 0.3072 0.0403 0.0076 -0.0450 78 THR A OG1 227 C CG2 . THR A 24 ? 0.2908 0.2731 0.2964 0.0368 0.0081 -0.0442 78 THR A CG2 228 N N . GLN A 25 ? 0.3169 0.2921 0.3299 0.0362 0.0128 -0.0416 79 GLN A N 229 C CA . GLN A 25 ? 0.3495 0.3241 0.3662 0.0361 0.0126 -0.0428 79 GLN A CA 230 C C . GLN A 25 ? 0.3504 0.3283 0.3723 0.0331 0.0128 -0.0438 79 GLN A C 231 O O . GLN A 25 ? 0.3399 0.3186 0.3650 0.0328 0.0117 -0.0459 79 GLN A O 232 C CB . GLN A 25 ? 0.3611 0.3293 0.3765 0.0386 0.0143 -0.0400 79 GLN A CB 233 C CG . GLN A 25 ? 0.4020 0.3664 0.4114 0.0422 0.0136 -0.0394 79 GLN A CG 234 C CD . GLN A 25 ? 0.4630 0.4302 0.4723 0.0429 0.0106 -0.0432 79 GLN A CD 235 O OE1 . GLN A 25 ? 0.5029 0.4704 0.5150 0.0428 0.0099 -0.0450 79 GLN A OE1 236 N NE2 . GLN A 25 ? 0.4190 0.3885 0.4258 0.0433 0.0089 -0.0446 79 GLN A NE2 237 N N . ILE A 26 ? 0.3302 0.3092 0.3529 0.0312 0.0139 -0.0423 80 ILE A N 238 C CA . ILE A 26 ? 0.3483 0.3302 0.3756 0.0286 0.0136 -0.0434 80 ILE A CA 239 C C . ILE A 26 ? 0.3324 0.3182 0.3583 0.0268 0.0135 -0.0437 80 ILE A C 240 O O . ILE A 26 ? 0.3348 0.3202 0.3571 0.0275 0.0141 -0.0422 80 ILE A O 241 C CB . ILE A 26 ? 0.3600 0.3387 0.3915 0.0280 0.0153 -0.0409 80 ILE A CB 242 C CG1 . ILE A 26 ? 0.3765 0.3534 0.4060 0.0280 0.0175 -0.0374 80 ILE A CG1 243 C CG2 . ILE A 26 ? 0.3937 0.3682 0.4272 0.0298 0.0156 -0.0403 80 ILE A CG2 244 C CD1 . ILE A 26 ? 0.4311 0.4052 0.4655 0.0274 0.0196 -0.0345 80 ILE A CD1 245 N N . PRO A 27 ? 0.3285 0.3176 0.3571 0.0249 0.0126 -0.0455 81 PRO A N 246 C CA . PRO A 27 ? 0.3107 0.3032 0.3375 0.0233 0.0127 -0.0456 81 PRO A CA 247 C C . PRO A 27 ? 0.2973 0.2881 0.3243 0.0225 0.0142 -0.0426 81 PRO A C 248 O O . PRO A 27 ? 0.2896 0.2774 0.3198 0.0225 0.0151 -0.0409 81 PRO A O 249 C CB . PRO A 27 ? 0.3180 0.3135 0.3471 0.0220 0.0114 -0.0482 81 PRO A CB 250 C CG . PRO A 27 ? 0.3374 0.3319 0.3683 0.0232 0.0103 -0.0504 81 PRO A CG 251 C CD . PRO A 27 ? 0.3296 0.3196 0.3618 0.0244 0.0112 -0.0481 81 PRO A CD 252 N N . HIS A 28 ? 0.2745 0.2670 0.2986 0.0219 0.0145 -0.0417 82 HIS A N 253 C CA . HIS A 28 ? 0.2781 0.2694 0.3021 0.0212 0.0159 -0.0390 82 HIS A CA 254 C C . HIS A 28 ? 0.2588 0.2538 0.2826 0.0191 0.0154 -0.0398 82 HIS A C 255 O O . HIS A 28 ? 0.2470 0.2425 0.2680 0.0189 0.0159 -0.0385 82 HIS A O 256 C CB . HIS A 28 ? 0.2778 0.2662 0.2977 0.0231 0.0171 -0.0366 82 HIS A CB 257 C CG . HIS A 28 ? 0.2889 0.2728 0.3084 0.0254 0.0180 -0.0353 82 HIS A CG 258 N ND1 . HIS A 28 ? 0.2824 0.2653 0.2991 0.0275 0.0169 -0.0365 82 HIS A ND1 259 C CD2 . HIS A 28 ? 0.3119 0.2921 0.3339 0.0261 0.0198 -0.0330 82 HIS A CD2 260 C CE1 . HIS A 28 ? 0.2950 0.2735 0.3116 0.0295 0.0181 -0.0349 82 HIS A CE1 261 N NE2 . HIS A 28 ? 0.2857 0.2625 0.3056 0.0287 0.0200 -0.0326 82 HIS A NE2 262 N N . LEU A 29 ? 0.2590 0.2561 0.2852 0.0179 0.0142 -0.0420 83 LEU A N 263 C CA . LEU A 29 ? 0.2633 0.2634 0.2888 0.0163 0.0137 -0.0428 83 LEU A CA 264 C C . LEU A 29 ? 0.2653 0.2643 0.2919 0.0153 0.0145 -0.0405 83 LEU A C 265 O O . LEU A 29 ? 0.2617 0.2581 0.2920 0.0153 0.0151 -0.0391 83 LEU A O 266 C CB . LEU A 29 ? 0.2549 0.2566 0.2822 0.0160 0.0120 -0.0458 83 LEU A CB 267 C CG . LEU A 29 ? 0.2550 0.2596 0.2805 0.0149 0.0113 -0.0470 83 LEU A CG 268 C CD1 . LEU A 29 ? 0.2718 0.2792 0.2936 0.0151 0.0120 -0.0473 83 LEU A CD1 269 C CD2 . LEU A 29 ? 0.2385 0.2432 0.2656 0.0154 0.0093 -0.0502 83 LEU A CD2 270 N N . ALA A 30 ? 0.2518 0.2528 0.2758 0.0144 0.0147 -0.0399 84 ALA A N 271 C CA . ALA A 30 ? 0.2465 0.2466 0.2716 0.0134 0.0154 -0.0378 84 ALA A CA 272 C C . ALA A 30 ? 0.2541 0.2537 0.2838 0.0125 0.0145 -0.0386 84 ALA A C 273 O O . ALA A 30 ? 0.2488 0.2499 0.2791 0.0122 0.0127 -0.0413 84 ALA A O 274 C CB . ALA A 30 ? 0.2249 0.2276 0.2466 0.0124 0.0152 -0.0378 84 ALA A CB 275 N N . GLY A 31 ? 0.2565 0.2539 0.2897 0.0122 0.0156 -0.0364 85 GLY A N 276 C CA . GLY A 31 ? 0.2701 0.2670 0.3091 0.0113 0.0145 -0.0370 85 GLY A CA 277 C C . GLY A 31 ? 0.2986 0.2934 0.3427 0.0119 0.0140 -0.0379 85 GLY A C 278 O O . GLY A 31 ? 0.3119 0.3059 0.3621 0.0112 0.0128 -0.0385 85 GLY A O 279 N N . THR A 32 ? 0.2753 0.2691 0.3176 0.0132 0.0146 -0.0379 86 THR A N 280 C CA . THR A 32 ? 0.2927 0.2844 0.3400 0.0138 0.0141 -0.0387 86 THR A CA 281 C C . THR A 32 ? 0.2927 0.2807 0.3432 0.0146 0.0168 -0.0352 86 THR A C 282 O O . THR A 32 ? 0.2738 0.2607 0.3207 0.0154 0.0192 -0.0325 86 THR A O 283 C CB . THR A 32 ? 0.2780 0.2705 0.3222 0.0149 0.0129 -0.0413 86 THR A CB 284 O OG1 . THR A 32 ? 0.3009 0.2927 0.3403 0.0162 0.0146 -0.0397 86 THR A OG1 285 C CG2 . THR A 32 ? 0.2881 0.2840 0.3289 0.0145 0.0106 -0.0446 86 THR A CG2 286 N N . GLU A 33 ? 0.3062 0.2921 0.3635 0.0147 0.0165 -0.0354 87 GLU A N 287 C CA . GLU A 33 ? 0.3352 0.3173 0.3961 0.0156 0.0195 -0.0318 87 GLU A CA 288 C C . GLU A 33 ? 0.3233 0.3035 0.3776 0.0178 0.0216 -0.0302 87 GLU A C 289 O O . GLU A 33 ? 0.3192 0.2966 0.3724 0.0190 0.0248 -0.0264 87 GLU A O 290 C CB . GLU A 33 ? 0.3615 0.3416 0.4310 0.0155 0.0186 -0.0326 87 GLU A CB 291 C CG . GLU A 33 ? 0.4540 0.4298 0.5276 0.0166 0.0223 -0.0285 87 GLU A CG 292 C CD . GLU A 33 ? 0.5538 0.5286 0.6321 0.0159 0.0251 -0.0248 87 GLU A CD 293 O OE1 . GLU A 33 ? 0.5858 0.5570 0.6659 0.0173 0.0291 -0.0207 87 GLU A OE1 294 O OE2 . GLU A 33 ? 0.5825 0.5599 0.6626 0.0143 0.0235 -0.0260 87 GLU A OE2 295 N N . GLN A 34 ? 0.3173 0.2987 0.3673 0.0185 0.0198 -0.0328 88 GLN A N 296 C CA . GLN A 34 ? 0.3308 0.3102 0.3748 0.0208 0.0211 -0.0317 88 GLN A CA 297 C C . GLN A 34 ? 0.3049 0.2846 0.3425 0.0215 0.0224 -0.0299 88 GLN A C 298 O O . GLN A 34 ? 0.2932 0.2698 0.3268 0.0238 0.0242 -0.0276 88 GLN A O 299 C CB . GLN A 34 ? 0.3251 0.3065 0.3664 0.0213 0.0186 -0.0352 88 GLN A CB 300 C CG . GLN A 34 ? 0.4027 0.3835 0.4496 0.0210 0.0170 -0.0373 88 GLN A CG 301 C CD . GLN A 34 ? 0.5131 0.4977 0.5613 0.0194 0.0142 -0.0409 88 GLN A CD 302 O OE1 . GLN A 34 ? 0.4540 0.4396 0.5054 0.0178 0.0137 -0.0408 88 GLN A OE1 303 N NE2 . GLN A 34 ? 0.5391 0.5259 0.5840 0.0200 0.0124 -0.0439 88 GLN A NE2 304 N N . ASN A 35 ? 0.2903 0.2735 0.3266 0.0199 0.0212 -0.0310 89 ASN A N 305 C CA . ASN A 35 ? 0.2952 0.2786 0.3258 0.0205 0.0222 -0.0294 89 ASN A CA 306 C C . ASN A 35 ? 0.3109 0.2916 0.3426 0.0210 0.0250 -0.0256 89 ASN A C 307 O O . ASN A 35 ? 0.3118 0.2904 0.3382 0.0228 0.0265 -0.0234 89 ASN A O 308 C CB . ASN A 35 ? 0.3016 0.2895 0.3303 0.0188 0.0202 -0.0317 89 ASN A CB 309 C CG . ASN A 35 ? 0.3281 0.3164 0.3506 0.0197 0.0204 -0.0309 89 ASN A CG 310 O OD1 . ASN A 35 ? 0.2937 0.2798 0.3124 0.0219 0.0208 -0.0303 89 ASN A OD1 311 N ND2 . ASN A 35 ? 0.3216 0.3125 0.3431 0.0181 0.0199 -0.0310 89 ASN A ND2 312 N N . PHE A 36 ? 0.2816 0.2620 0.3203 0.0195 0.0257 -0.0248 90 PHE A N 313 C CA . PHE A 36 ? 0.3084 0.2859 0.3498 0.0201 0.0290 -0.0208 90 PHE A CA 314 C C . PHE A 36 ? 0.3114 0.2842 0.3515 0.0229 0.0318 -0.0180 90 PHE A C 315 O O . PHE A 36 ? 0.2989 0.2687 0.3350 0.0250 0.0346 -0.0147 90 PHE A O 316 C CB . PHE A 36 ? 0.3066 0.2851 0.3574 0.0179 0.0286 -0.0210 90 PHE A CB 317 C CG . PHE A 36 ? 0.3228 0.2987 0.3789 0.0182 0.0322 -0.0170 90 PHE A CG 318 C CD1 . PHE A 36 ? 0.3475 0.3225 0.3996 0.0191 0.0347 -0.0141 90 PHE A CD1 319 C CD2 . PHE A 36 ? 0.4113 0.3855 0.4770 0.0176 0.0331 -0.0161 90 PHE A CD2 320 C CE1 . PHE A 36 ? 0.3539 0.3265 0.4111 0.0196 0.0384 -0.0102 90 PHE A CE1 321 C CE2 . PHE A 36 ? 0.4540 0.4257 0.5258 0.0179 0.0369 -0.0120 90 PHE A CE2 322 C CZ . PHE A 36 ? 0.4120 0.3831 0.4794 0.0190 0.0397 -0.0090 90 PHE A CZ 323 N N A GLN A 37 ? 0.3165 0.2881 0.3592 0.0233 0.0311 -0.0192 91 GLN A N 324 N N B GLN A 37 ? 0.3123 0.2840 0.3551 0.0232 0.0310 -0.0193 91 GLN A N 325 C CA A GLN A 37 ? 0.3347 0.3014 0.3754 0.0262 0.0337 -0.0165 91 GLN A CA 326 C CA B GLN A 37 ? 0.3261 0.2930 0.3670 0.0261 0.0334 -0.0169 91 GLN A CA 327 C C A GLN A 37 ? 0.3270 0.2919 0.3574 0.0291 0.0338 -0.0161 91 GLN A C 328 C C B GLN A 37 ? 0.3221 0.2872 0.3528 0.0290 0.0338 -0.0162 91 GLN A C 329 O O A GLN A 37 ? 0.3201 0.2805 0.3466 0.0320 0.0369 -0.0126 91 GLN A O 330 O O B GLN A 37 ? 0.3207 0.2813 0.3478 0.0319 0.0369 -0.0126 91 GLN A O 331 C CB A GLN A 37 ? 0.3344 0.3001 0.3798 0.0261 0.0326 -0.0181 91 GLN A CB 332 C CB B GLN A 37 ? 0.3209 0.2874 0.3657 0.0259 0.0317 -0.0191 91 GLN A CB 333 C CG A GLN A 37 ? 0.3924 0.3587 0.4489 0.0238 0.0326 -0.0181 91 GLN A CG 334 C CG B GLN A 37 ? 0.3578 0.3240 0.4134 0.0240 0.0322 -0.0186 91 GLN A CG 335 C CD A GLN A 37 ? 0.4264 0.3893 0.4881 0.0244 0.0369 -0.0134 91 GLN A CD 336 C CD B GLN A 37 ? 0.3464 0.3128 0.4062 0.0235 0.0296 -0.0217 91 GLN A CD 337 O OE1 A GLN A 37 ? 0.4963 0.4550 0.5540 0.0272 0.0405 -0.0097 91 GLN A OE1 338 O OE1 B GLN A 37 ? 0.3632 0.3314 0.4183 0.0239 0.0270 -0.0248 91 GLN A OE1 339 N NE2 A GLN A 37 ? 0.4701 0.4346 0.5408 0.0220 0.0367 -0.0133 91 GLN A NE2 340 N NE2 B GLN A 37 ? 0.3880 0.3529 0.4575 0.0226 0.0302 -0.0208 91 GLN A NE2 341 N N . LEU A 38 ? 0.3160 0.2843 0.3422 0.0285 0.0305 -0.0196 92 LEU A N 342 C CA . LEU A 38 ? 0.3108 0.2778 0.3283 0.0311 0.0300 -0.0196 92 LEU A CA 343 C C . LEU A 38 ? 0.3097 0.2756 0.3234 0.0320 0.0318 -0.0169 92 LEU A C 344 O O . LEU A 38 ? 0.3087 0.2704 0.3158 0.0355 0.0332 -0.0148 92 LEU A O 345 C CB . LEU A 38 ? 0.3004 0.2716 0.3155 0.0300 0.0262 -0.0237 92 LEU A CB 346 C CG . LEU A 38 ? 0.3029 0.2727 0.3104 0.0328 0.0249 -0.0243 92 LEU A CG 347 C CD1 . LEU A 38 ? 0.3138 0.2780 0.3174 0.0367 0.0259 -0.0229 92 LEU A CD1 348 C CD2 . LEU A 38 ? 0.2801 0.2546 0.2876 0.0313 0.0216 -0.0282 92 LEU A CD2 349 N N . ALA A 39 ? 0.2982 0.2673 0.3155 0.0293 0.0317 -0.0170 93 ALA A N 350 C CA . ALA A 39 ? 0.3028 0.2707 0.3168 0.0301 0.0336 -0.0143 93 ALA A CA 351 C C . ALA A 39 ? 0.2994 0.2620 0.3130 0.0330 0.0379 -0.0099 93 ALA A C 352 O O . ALA A 39 ? 0.3044 0.2637 0.3112 0.0361 0.0395 -0.0076 93 ALA A O 353 C CB . ALA A 39 ? 0.2919 0.2639 0.3110 0.0268 0.0332 -0.0148 93 ALA A CB 354 N N . LYS A 40 ? 0.3040 0.2654 0.3249 0.0322 0.0399 -0.0085 94 LYS A N 355 C CA . LYS A 40 ? 0.3218 0.2780 0.3435 0.0348 0.0447 -0.0038 94 LYS A CA 356 C C . LYS A 40 ? 0.3250 0.2759 0.3382 0.0393 0.0457 -0.0025 94 LYS A C 357 O O . LYS A 40 ? 0.3394 0.2856 0.3478 0.0428 0.0493 0.0012 94 LYS A O 358 C CB . LYS A 40 ? 0.3130 0.2694 0.3458 0.0327 0.0462 -0.0029 94 LYS A CB 359 C CG . LYS A 40 ? 0.3519 0.3118 0.3926 0.0294 0.0462 -0.0029 94 LYS A CG 360 C CD . LYS A 40 ? 0.4656 0.4249 0.5182 0.0278 0.0480 -0.0015 94 LYS A CD 361 C CE . LYS A 40 ? 0.5067 0.4686 0.5642 0.0255 0.0440 -0.0056 94 LYS A CE 362 N NZ . LYS A 40 ? 0.5660 0.5270 0.6358 0.0240 0.0453 -0.0044 94 LYS A NZ 363 N N . GLN A 41 ? 0.3306 0.2821 0.3420 0.0394 0.0426 -0.0057 95 GLN A N 364 C CA . GLN A 41 ? 0.3439 0.2905 0.3470 0.0438 0.0428 -0.0051 95 GLN A CA 365 C C . GLN A 41 ? 0.3510 0.2962 0.3443 0.0467 0.0418 -0.0050 95 GLN A C 366 O O . GLN A 41 ? 0.3513 0.2908 0.3373 0.0512 0.0440 -0.0023 95 GLN A O 367 C CB . GLN A 41 ? 0.3392 0.2875 0.3429 0.0431 0.0391 -0.0089 95 GLN A CB 368 C CG . GLN A 41 ? 0.3564 0.3000 0.3511 0.0477 0.0383 -0.0090 95 GLN A CG 369 C CD . GLN A 41 ? 0.3433 0.2896 0.3381 0.0469 0.0341 -0.0134 95 GLN A CD 370 O OE1 . GLN A 41 ? 0.3639 0.3135 0.3658 0.0438 0.0330 -0.0154 95 GLN A OE1 371 N NE2 . GLN A 41 ? 0.3831 0.3279 0.3704 0.0498 0.0316 -0.0150 95 GLN A NE2 372 N N . ILE A 42 ? 0.3253 0.2754 0.3184 0.0442 0.0384 -0.0081 96 ILE A N 373 C CA . ILE A 42 ? 0.3401 0.2892 0.3249 0.0466 0.0368 -0.0085 96 ILE A CA 374 C C . ILE A 42 ? 0.3353 0.2811 0.3170 0.0487 0.0405 -0.0046 96 ILE A C 375 O O . ILE A 42 ? 0.3427 0.2838 0.3155 0.0531 0.0409 -0.0032 96 ILE A O 376 C CB . ILE A 42 ? 0.3328 0.2882 0.3193 0.0431 0.0327 -0.0124 96 ILE A CB 377 C CG1 A ILE A 42 ? 0.3556 0.3143 0.3447 0.0414 0.0293 -0.0164 96 ILE A CG1 378 C CG1 B ILE A 42 ? 0.3257 0.2833 0.3133 0.0423 0.0293 -0.0162 96 ILE A CG1 379 C CG2 . ILE A 42 ? 0.3174 0.2716 0.2963 0.0454 0.0311 -0.0126 96 ILE A CG2 380 C CD1 A ILE A 42 ? 0.3533 0.3089 0.3361 0.0450 0.0272 -0.0177 96 ILE A CD1 381 C CD1 B ILE A 42 ? 0.2471 0.2109 0.2373 0.0390 0.0258 -0.0198 96 ILE A CD1 382 N N . GLN A 43 ? 0.3218 0.2699 0.3107 0.0458 0.0430 -0.0027 97 GLN A N 383 C CA . GLN A 43 ? 0.3315 0.2765 0.3185 0.0478 0.0471 0.0012 97 GLN A CA 384 C C . GLN A 43 ? 0.3459 0.2836 0.3279 0.0529 0.0513 0.0053 97 GLN A C 385 O O . GLN A 43 ? 0.3629 0.2961 0.3366 0.0572 0.0532 0.0077 97 GLN A O 386 C CB . GLN A 43 ? 0.3211 0.2696 0.3185 0.0438 0.0491 0.0025 97 GLN A CB 387 C CG . GLN A 43 ? 0.3421 0.2879 0.3396 0.0455 0.0539 0.0070 97 GLN A CG 388 C CD . GLN A 43 ? 0.3557 0.3046 0.3650 0.0417 0.0561 0.0083 97 GLN A CD 389 O OE1 . GLN A 43 ? 0.3679 0.3192 0.3860 0.0387 0.0551 0.0070 97 GLN A OE1 390 N NE2 . GLN A 43 ? 0.3601 0.3086 0.3699 0.0422 0.0588 0.0110 97 GLN A NE2 391 N N . SER A 44 ? 0.3509 0.2873 0.3380 0.0525 0.0530 0.0062 98 SER A N 392 C CA . SER A 44 ? 0.3691 0.2983 0.3519 0.0574 0.0573 0.0102 98 SER A CA 393 C C . SER A 44 ? 0.3697 0.2939 0.3394 0.0627 0.0553 0.0094 98 SER A C 394 O O . SER A 44 ? 0.3951 0.3131 0.3567 0.0679 0.0586 0.0130 98 SER A O 395 C CB . SER A 44 ? 0.3657 0.2946 0.3559 0.0558 0.0581 0.0103 98 SER A CB 396 O OG A SER A 44 ? 0.3985 0.3293 0.4000 0.0527 0.0614 0.0127 98 SER A OG 397 O OG B SER A 44 ? 0.3820 0.3038 0.3688 0.0604 0.0630 0.0149 98 SER A OG 398 N N . GLN A 45 ? 0.3687 0.2956 0.3366 0.0617 0.0499 0.0047 99 GLN A N 399 C CA . GLN A 45 ? 0.3719 0.2944 0.3289 0.0665 0.0471 0.0033 99 GLN A CA 400 C C . GLN A 45 ? 0.3783 0.2995 0.3270 0.0692 0.0457 0.0031 99 GLN A C 401 O O . GLN A 45 ? 0.3878 0.3026 0.3261 0.0750 0.0461 0.0044 99 GLN A O 402 C CB . GLN A 45 ? 0.3661 0.2923 0.3248 0.0645 0.0417 -0.0017 99 GLN A CB 403 C CG . GLN A 45 ? 0.4118 0.3379 0.3767 0.0631 0.0428 -0.0016 99 GLN A CG 404 C CD . GLN A 45 ? 0.4516 0.3808 0.4174 0.0617 0.0376 -0.0065 99 GLN A CD 405 O OE1 . GLN A 45 ? 0.4396 0.3752 0.4103 0.0576 0.0344 -0.0100 99 GLN A OE1 406 N NE2 . GLN A 45 ? 0.5099 0.4344 0.4710 0.0655 0.0371 -0.0066 99 GLN A NE2 407 N N . TRP A 46 ? 0.3565 0.2835 0.3093 0.0652 0.0439 0.0013 100 TRP A N 408 C CA . TRP A 46 ? 0.3575 0.2827 0.3026 0.0680 0.0429 0.0016 100 TRP A CA 409 C C . TRP A 46 ? 0.3652 0.2842 0.3048 0.0724 0.0485 0.0068 100 TRP A C 410 O O . TRP A 46 ? 0.3786 0.2928 0.3079 0.0775 0.0479 0.0073 100 TRP A O 411 C CB . TRP A 46 ? 0.3375 0.2697 0.2883 0.0629 0.0406 -0.0006 100 TRP A CB 412 C CG . TRP A 46 ? 0.3225 0.2597 0.2756 0.0600 0.0348 -0.0057 100 TRP A CG 413 C CD1 . TRP A 46 ? 0.3264 0.2630 0.2782 0.0610 0.0317 -0.0085 100 TRP A CD1 414 C CD2 . TRP A 46 ? 0.2870 0.2307 0.2449 0.0555 0.0320 -0.0084 100 TRP A CD2 415 N NE1 . TRP A 46 ? 0.3493 0.2919 0.3051 0.0574 0.0273 -0.0126 100 TRP A NE1 416 C CE2 . TRP A 46 ? 0.3172 0.2639 0.2765 0.0540 0.0275 -0.0125 100 TRP A CE2 417 C CE3 . TRP A 46 ? 0.3216 0.2686 0.2826 0.0527 0.0330 -0.0075 100 TRP A CE3 418 C CZ2 . TRP A 46 ? 0.3375 0.2906 0.3014 0.0499 0.0243 -0.0156 100 TRP A CZ2 419 C CZ3 . TRP A 46 ? 0.2998 0.2529 0.2649 0.0485 0.0294 -0.0108 100 TRP A CZ3 420 C CH2 . TRP A 46 ? 0.3134 0.2694 0.2798 0.0473 0.0253 -0.0146 100 TRP A CH2 421 N N . LYS A 47 ? 0.3833 0.3024 0.3300 0.0708 0.0538 0.0105 101 LYS A N 422 C CA . LYS A 47 ? 0.4294 0.3423 0.3714 0.0754 0.0600 0.0161 101 LYS A CA 423 C C . LYS A 47 ? 0.4433 0.3479 0.3750 0.0821 0.0614 0.0179 101 LYS A C 424 O O . LYS A 47 ? 0.4575 0.3560 0.3783 0.0881 0.0630 0.0200 101 LYS A O 425 C CB . LYS A 47 ? 0.4446 0.3593 0.3979 0.0722 0.0655 0.0197 101 LYS A CB 426 C CG . LYS A 47 ? 0.4944 0.4162 0.4573 0.0664 0.0647 0.0185 101 LYS A CG 427 C CD . LYS A 47 ? 0.5999 0.5231 0.5750 0.0635 0.0696 0.0219 101 LYS A CD 428 C CE . LYS A 47 ? 0.6222 0.5500 0.6036 0.0601 0.0703 0.0223 101 LYS A CE 429 N NZ . LYS A 47 ? 0.6668 0.5979 0.6625 0.0557 0.0728 0.0237 101 LYS A NZ 430 N N . GLU A 48 ? 0.4451 0.3494 0.3798 0.0813 0.0605 0.0167 102 GLU A N 431 C CA A GLU A 48 ? 0.4613 0.3582 0.3870 0.0872 0.0611 0.0178 102 GLU A CA 432 C CA B GLU A 48 ? 0.4639 0.3603 0.3890 0.0876 0.0616 0.0183 102 GLU A CA 433 C C . GLU A 48 ? 0.4654 0.3587 0.3782 0.0922 0.0562 0.0150 102 GLU A C 434 O O . GLU A 48 ? 0.4709 0.3561 0.3720 0.0992 0.0578 0.0172 102 GLU A O 435 C CB A GLU A 48 ? 0.4670 0.3664 0.3994 0.0842 0.0588 0.0153 102 GLU A CB 436 C CB B GLU A 48 ? 0.4680 0.3651 0.3995 0.0856 0.0614 0.0176 102 GLU A CB 437 C CG A GLU A 48 ? 0.4937 0.3948 0.4382 0.0804 0.0633 0.0181 102 GLU A CG 438 C CG B GLU A 48 ? 0.5254 0.4151 0.4469 0.0917 0.0609 0.0179 102 GLU A CG 439 C CD A GLU A 48 ? 0.5270 0.4321 0.4790 0.0764 0.0596 0.0143 102 GLU A CD 440 C CD B GLU A 48 ? 0.5996 0.4916 0.5272 0.0888 0.0583 0.0151 102 GLU A CD 441 O OE1 A GLU A 48 ? 0.5102 0.4143 0.4565 0.0783 0.0552 0.0109 102 GLU A OE1 442 O OE1 B GLU A 48 ? 0.6383 0.5352 0.5781 0.0834 0.0598 0.0154 102 GLU A OE1 443 O OE2 A GLU A 48 ? 0.5156 0.4250 0.4796 0.0715 0.0610 0.0145 102 GLU A OE2 444 O OE2 B GLU A 48 ? 0.6346 0.5234 0.5550 0.0922 0.0544 0.0125 102 GLU A OE2 445 N N . PHE A 49 ? 0.4493 0.3486 0.3646 0.0886 0.0500 0.0099 103 PHE A N 446 C CA . PHE A 49 ? 0.4496 0.3467 0.3552 0.0923 0.0442 0.0062 103 PHE A CA 447 C C . PHE A 49 ? 0.4509 0.3436 0.3472 0.0969 0.0454 0.0082 103 PHE A C 448 O O . PHE A 49 ? 0.4668 0.3553 0.3531 0.1018 0.0413 0.0060 103 PHE A O 449 C CB . PHE A 49 ? 0.4390 0.3443 0.3515 0.0866 0.0379 0.0007 103 PHE A CB 450 C CG . PHE A 49 ? 0.4511 0.3600 0.3702 0.0833 0.0352 -0.0024 103 PHE A CG 451 C CD1 . PHE A 49 ? 0.4678 0.3721 0.3847 0.0862 0.0368 -0.0011 103 PHE A CD1 452 C CD2 . PHE A 49 ? 0.3885 0.3055 0.3157 0.0776 0.0310 -0.0066 103 PHE A CD2 453 C CE1 . PHE A 49 ? 0.4930 0.4008 0.4161 0.0832 0.0341 -0.0042 103 PHE A CE1 454 C CE2 . PHE A 49 ? 0.4227 0.3431 0.3558 0.0748 0.0286 -0.0095 103 PHE A CE2 455 C CZ . PHE A 49 ? 0.4733 0.3893 0.4046 0.0775 0.0300 -0.0084 103 PHE A CZ 456 N N . GLY A 50 ? 0.4221 0.3160 0.3221 0.0953 0.0506 0.0120 104 GLY A N 457 C CA . GLY A 50 ? 0.4453 0.3345 0.3365 0.1001 0.0530 0.0147 104 GLY A CA 458 C C . GLY A 50 ? 0.4311 0.3257 0.3263 0.0964 0.0519 0.0138 104 GLY A C 459 O O . GLY A 50 ? 0.4479 0.3386 0.3350 0.1008 0.0530 0.0154 104 GLY A O 460 N N . LEU A 51 ? 0.4071 0.3105 0.3140 0.0889 0.0495 0.0111 105 LEU A N 461 C CA . LEU A 51 ? 0.3882 0.2966 0.2991 0.0854 0.0489 0.0105 105 LEU A CA 462 C C . LEU A 51 ? 0.4200 0.3269 0.3328 0.0860 0.0558 0.0158 105 LEU A C 463 O O . LEU A 51 ? 0.4283 0.3336 0.3455 0.0861 0.0614 0.0196 105 LEU A O 464 C CB . LEU A 51 ? 0.3652 0.2827 0.2881 0.0775 0.0456 0.0069 105 LEU A CB 465 C CG . LEU A 51 ? 0.3464 0.2662 0.2686 0.0764 0.0389 0.0017 105 LEU A CG 466 C CD1 . LEU A 51 ? 0.3649 0.2936 0.2979 0.0690 0.0364 -0.0012 105 LEU A CD1 467 C CD2 . LEU A 51 ? 0.3850 0.3009 0.2968 0.0812 0.0344 -0.0004 105 LEU A CD2 468 N N . ASP A 52 ? 0.4164 0.3238 0.3263 0.0867 0.0556 0.0161 106 ASP A N 469 C CA . ASP A 52 ? 0.4499 0.3561 0.3615 0.0875 0.0620 0.0210 106 ASP A CA 470 C C . ASP A 52 ? 0.4571 0.3697 0.3834 0.0809 0.0651 0.0223 106 ASP A C 471 O O . ASP A 52 ? 0.4628 0.3735 0.3932 0.0816 0.0716 0.0270 106 ASP A O 472 C CB . ASP A 52 ? 0.4395 0.3453 0.3451 0.0894 0.0604 0.0204 106 ASP A CB 473 C CG . ASP A 52 ? 0.4810 0.3794 0.3717 0.0969 0.0579 0.0197 106 ASP A CG 474 O OD1 . ASP A 52 ? 0.4907 0.3817 0.3735 0.1031 0.0624 0.0234 106 ASP A OD1 475 O OD2 . ASP A 52 ? 0.4501 0.3496 0.3370 0.0970 0.0515 0.0154 106 ASP A OD2 476 N N . SER A 53 ? 0.4377 0.3576 0.3721 0.0745 0.0606 0.0183 107 SER A N 477 C CA . SER A 53 ? 0.4202 0.3460 0.3685 0.0684 0.0626 0.0189 107 SER A CA 478 C C . SER A 53 ? 0.3995 0.3307 0.3532 0.0635 0.0572 0.0141 107 SER A C 479 O O . SER A 53 ? 0.3623 0.2947 0.3110 0.0636 0.0519 0.0102 107 SER A O 480 C CB . SER A 53 ? 0.4336 0.3631 0.3861 0.0658 0.0635 0.0196 107 SER A CB 481 O OG A SER A 53 ? 0.4515 0.3827 0.3982 0.0657 0.0583 0.0161 107 SER A OG 482 O OG B SER A 53 ? 0.4420 0.3768 0.3955 0.0621 0.0576 0.0151 107 SER A OG 483 N N . VAL A 54 ? 0.3772 0.3116 0.3413 0.0595 0.0586 0.0143 108 VAL A N 484 C CA . VAL A 54 ? 0.3730 0.3127 0.3426 0.0549 0.0540 0.0099 108 VAL A CA 485 C C . VAL A 54 ? 0.3721 0.3168 0.3545 0.0496 0.0554 0.0102 108 VAL A C 486 O O . VAL A 54 ? 0.3717 0.3147 0.3602 0.0496 0.0594 0.0131 108 VAL A O 487 C CB . VAL A 54 ? 0.3642 0.3015 0.3316 0.0565 0.0526 0.0085 108 VAL A CB 488 C CG1 . VAL A 54 ? 0.3752 0.3185 0.3476 0.0519 0.0475 0.0037 108 VAL A CG1 489 C CG2 . VAL A 54 ? 0.3893 0.3203 0.3438 0.0627 0.0514 0.0086 108 VAL A CG2 490 N N . GLU A 55 ? 0.3479 0.2983 0.3344 0.0453 0.0520 0.0073 109 GLU A N 491 C CA . GLU A 55 ? 0.3712 0.3260 0.3689 0.0407 0.0527 0.0073 109 GLU A CA 492 C C . GLU A 55 ? 0.3425 0.3026 0.3449 0.0364 0.0481 0.0028 109 GLU A C 493 O O . GLU A 55 ? 0.3423 0.3038 0.3392 0.0364 0.0442 -0.0003 109 GLU A O 494 C CB . GLU A 55 ? 0.3911 0.3476 0.3896 0.0399 0.0536 0.0084 109 GLU A CB 495 C CG . GLU A 55 ? 0.5046 0.4563 0.5005 0.0439 0.0591 0.0134 109 GLU A CG 496 C CD . GLU A 55 ? 0.6148 0.5636 0.6174 0.0449 0.0644 0.0173 109 GLU A CD 497 O OE1 . GLU A 55 ? 0.6265 0.5782 0.6399 0.0412 0.0644 0.0167 109 GLU A OE1 498 O OE2 . GLU A 55 ? 0.7003 0.6434 0.6969 0.0498 0.0687 0.0211 109 GLU A OE2 499 N N . LEU A 56 ? 0.3246 0.2875 0.3369 0.0330 0.0484 0.0024 110 LEU A N 500 C CA . LEU A 56 ? 0.3206 0.2887 0.3370 0.0290 0.0441 -0.0017 110 LEU A CA 501 C C . LEU A 56 ? 0.3269 0.2988 0.3464 0.0262 0.0429 -0.0025 110 LEU A C 502 O O . LEU A 56 ? 0.3225 0.2940 0.3472 0.0259 0.0456 0.0000 110 LEU A O 503 C CB . LEU A 56 ? 0.3332 0.3023 0.3582 0.0269 0.0440 -0.0026 110 LEU A CB 504 C CG . LEU A 56 ? 0.3610 0.3267 0.3846 0.0291 0.0449 -0.0021 110 LEU A CG 505 C CD1 . LEU A 56 ? 0.3790 0.3465 0.4122 0.0264 0.0440 -0.0036 110 LEU A CD1 506 C CD2 . LEU A 56 ? 0.3459 0.3115 0.3613 0.0306 0.0420 -0.0047 110 LEU A CD2 507 N N . ALA A 57 ? 0.2860 0.2614 0.3024 0.0244 0.0390 -0.0057 111 ALA A N 508 C CA . ALA A 57 ? 0.2902 0.2692 0.3094 0.0217 0.0376 -0.0067 111 ALA A CA 509 C C . ALA A 57 ? 0.2904 0.2731 0.3144 0.0186 0.0344 -0.0102 111 ALA A C 510 O O . ALA A 57 ? 0.2926 0.2768 0.3130 0.0183 0.0318 -0.0129 111 ALA A O 511 C CB . ALA A 57 ? 0.2947 0.2744 0.3062 0.0225 0.0357 -0.0075 111 ALA A CB 512 N N . HIS A 58 ? 0.2716 0.2558 0.3037 0.0164 0.0345 -0.0103 112 HIS A N 513 C CA . HIS A 58 ? 0.2620 0.2492 0.2985 0.0139 0.0314 -0.0137 112 HIS A CA 514 C C . HIS A 58 ? 0.2539 0.2443 0.2915 0.0116 0.0290 -0.0155 112 HIS A C 515 O O . HIS A 58 ? 0.2583 0.2487 0.2966 0.0115 0.0301 -0.0137 112 HIS A O 516 C CB . HIS A 58 ? 0.2726 0.2585 0.3178 0.0135 0.0324 -0.0132 112 HIS A CB 517 C CG . HIS A 58 ? 0.2963 0.2819 0.3494 0.0127 0.0342 -0.0111 112 HIS A CG 518 N ND1 . HIS A 58 ? 0.3550 0.3374 0.4104 0.0145 0.0386 -0.0070 112 HIS A ND1 519 C CD2 . HIS A 58 ? 0.3375 0.3254 0.3969 0.0105 0.0322 -0.0126 112 HIS A CD2 520 C CE1 . HIS A 58 ? 0.3639 0.3470 0.4276 0.0132 0.0393 -0.0059 112 HIS A CE1 521 N NE2 . HIS A 58 ? 0.3563 0.3427 0.4226 0.0108 0.0352 -0.0094 112 HIS A NE2 522 N N . TYR A 59 ? 0.2500 0.2431 0.2873 0.0101 0.0258 -0.0189 113 TYR A N 523 C CA . TYR A 59 ? 0.2435 0.2395 0.2810 0.0082 0.0232 -0.0209 113 TYR A CA 524 C C . TYR A 59 ? 0.2411 0.2384 0.2824 0.0071 0.0206 -0.0241 113 TYR A C 525 O O . TYR A 59 ? 0.2487 0.2453 0.2904 0.0077 0.0205 -0.0250 113 TYR A O 526 C CB . TYR A 59 ? 0.2383 0.2360 0.2680 0.0081 0.0220 -0.0219 113 TYR A CB 527 C CG . TYR A 59 ? 0.2321 0.2280 0.2574 0.0097 0.0241 -0.0192 113 TYR A CG 528 C CD1 . TYR A 59 ? 0.2315 0.2273 0.2573 0.0095 0.0250 -0.0174 113 TYR A CD1 529 C CD2 . TYR A 59 ? 0.2318 0.2258 0.2529 0.0117 0.0252 -0.0184 113 TYR A CD2 530 C CE1 . TYR A 59 ? 0.2456 0.2392 0.2669 0.0115 0.0270 -0.0148 113 TYR A CE1 531 C CE2 . TYR A 59 ? 0.2558 0.2475 0.2724 0.0138 0.0269 -0.0161 113 TYR A CE2 532 C CZ . TYR A 59 ? 0.2710 0.2624 0.2877 0.0137 0.0279 -0.0142 113 TYR A CZ 533 O OH . TYR A 59 ? 0.2743 0.2631 0.2860 0.0162 0.0295 -0.0120 113 TYR A OH 534 N N . ASP A 60 ? 0.2339 0.2329 0.2771 0.0057 0.0183 -0.0258 114 ASP A N 535 C CA . ASP A 60 ? 0.2537 0.2536 0.2996 0.0051 0.0153 -0.0292 114 ASP A CA 536 C C . ASP A 60 ? 0.2443 0.2464 0.2837 0.0046 0.0132 -0.0313 114 ASP A C 537 O O . ASP A 60 ? 0.2483 0.2513 0.2870 0.0039 0.0123 -0.0314 114 ASP A O 538 C CB . ASP A 60 ? 0.2646 0.2639 0.3189 0.0043 0.0139 -0.0296 114 ASP A CB 539 C CG . ASP A 60 ? 0.3240 0.3211 0.3861 0.0046 0.0163 -0.0272 114 ASP A CG 540 O OD1 . ASP A 60 ? 0.3024 0.2983 0.3649 0.0054 0.0170 -0.0274 114 ASP A OD1 541 O OD2 . ASP A 60 ? 0.3426 0.3390 0.4100 0.0043 0.0179 -0.0250 114 ASP A OD2 542 N N . VAL A 61 ? 0.2338 0.2367 0.2689 0.0052 0.0128 -0.0329 115 VAL A N 543 C CA . VAL A 61 ? 0.2449 0.2500 0.2734 0.0051 0.0118 -0.0343 115 VAL A CA 544 C C . VAL A 61 ? 0.2438 0.2497 0.2715 0.0055 0.0096 -0.0375 115 VAL A C 545 O O . VAL A 61 ? 0.2827 0.2875 0.3140 0.0060 0.0090 -0.0387 115 VAL A O 546 C CB . VAL A 61 ? 0.2454 0.2509 0.2690 0.0056 0.0137 -0.0329 115 VAL A CB 547 C CG1 . VAL A 61 ? 0.2410 0.2453 0.2643 0.0057 0.0156 -0.0299 115 VAL A CG1 548 C CG2 . VAL A 61 ? 0.2172 0.2220 0.2412 0.0067 0.0143 -0.0335 115 VAL A CG2 549 N N . LEU A 62 ? 0.2420 0.2495 0.2645 0.0054 0.0088 -0.0388 116 LEU A N 550 C CA . LEU A 62 ? 0.2466 0.2546 0.2670 0.0064 0.0071 -0.0417 116 LEU A CA 551 C C . LEU A 62 ? 0.2459 0.2546 0.2645 0.0071 0.0084 -0.0421 116 LEU A C 552 O O . LEU A 62 ? 0.2839 0.2940 0.2992 0.0069 0.0100 -0.0408 116 LEU A O 553 C CB . LEU A 62 ? 0.2172 0.2264 0.2321 0.0065 0.0063 -0.0425 116 LEU A CB 554 C CG . LEU A 62 ? 0.2464 0.2554 0.2589 0.0080 0.0043 -0.0457 116 LEU A CG 555 C CD1 . LEU A 62 ? 0.2742 0.2812 0.2913 0.0083 0.0011 -0.0476 116 LEU A CD1 556 C CD2 . LEU A 62 ? 0.2646 0.2747 0.2705 0.0084 0.0046 -0.0457 116 LEU A CD2 557 N N . LEU A 63 ? 0.2445 0.2524 0.2656 0.0079 0.0073 -0.0439 117 LEU A N 558 C CA . LEU A 63 ? 0.2530 0.2616 0.2725 0.0089 0.0082 -0.0447 117 LEU A CA 559 C C . LEU A 63 ? 0.2722 0.2810 0.2897 0.0101 0.0064 -0.0479 117 LEU A C 560 O O . LEU A 63 ? 0.2834 0.2916 0.3002 0.0104 0.0044 -0.0492 117 LEU A O 561 C CB . LEU A 63 ? 0.2433 0.2501 0.2674 0.0091 0.0089 -0.0439 117 LEU A CB 562 C CG . LEU A 63 ? 0.2353 0.2412 0.2605 0.0085 0.0110 -0.0406 117 LEU A CG 563 C CD1 . LEU A 63 ? 0.2370 0.2407 0.2657 0.0092 0.0120 -0.0397 117 LEU A CD1 564 C CD2 . LEU A 63 ? 0.2187 0.2263 0.2391 0.0083 0.0125 -0.0392 117 LEU A CD2 565 N N . SER A 64 ? 0.2758 0.2853 0.2919 0.0112 0.0069 -0.0491 118 SER A N 566 C CA . SER A 64 ? 0.2933 0.3033 0.3062 0.0128 0.0057 -0.0519 118 SER A CA 567 C C . SER A 64 ? 0.2921 0.3017 0.3068 0.0139 0.0056 -0.0532 118 SER A C 568 O O . SER A 64 ? 0.3009 0.3114 0.3163 0.0136 0.0075 -0.0519 118 SER A O 569 C CB . SER A 64 ? 0.3056 0.3180 0.3127 0.0132 0.0076 -0.0513 118 SER A CB 570 O OG . SER A 64 ? 0.3267 0.3397 0.3305 0.0151 0.0076 -0.0535 118 SER A OG 571 N N . TYR A 65 ? 0.2949 0.3032 0.3102 0.0153 0.0032 -0.0561 119 TYR A N 572 C CA . TYR A 65 ? 0.2933 0.3010 0.3106 0.0164 0.0029 -0.0575 119 TYR A CA 573 C C . TYR A 65 ? 0.3229 0.3302 0.3369 0.0187 0.0009 -0.0610 119 TYR A C 574 O O . TYR A 65 ? 0.3268 0.3330 0.3390 0.0195 -0.0012 -0.0625 119 TYR A O 575 C CB . TYR A 65 ? 0.3056 0.3108 0.3298 0.0157 0.0014 -0.0575 119 TYR A CB 576 C CG . TYR A 65 ? 0.3029 0.3075 0.3307 0.0139 0.0032 -0.0541 119 TYR A CG 577 C CD1 . TYR A 65 ? 0.3109 0.3159 0.3389 0.0138 0.0055 -0.0522 119 TYR A CD1 578 C CD2 . TYR A 65 ? 0.3245 0.3281 0.3556 0.0128 0.0025 -0.0529 119 TYR A CD2 579 C CE1 . TYR A 65 ? 0.2800 0.2838 0.3104 0.0127 0.0072 -0.0491 119 TYR A CE1 580 C CE2 . TYR A 65 ? 0.3288 0.3316 0.3630 0.0115 0.0045 -0.0497 119 TYR A CE2 581 C CZ . TYR A 65 ? 0.3344 0.3371 0.3678 0.0116 0.0069 -0.0478 119 TYR A CZ 582 O OH . TYR A 65 ? 0.3280 0.3295 0.3635 0.0110 0.0089 -0.0447 119 TYR A OH 583 N N . PRO A 66 ? 0.3363 0.3442 0.3494 0.0200 0.0015 -0.0622 120 PRO A N 584 C CA . PRO A 66 ? 0.3605 0.3675 0.3707 0.0227 -0.0004 -0.0657 120 PRO A CA 585 C C . PRO A 66 ? 0.4024 0.4062 0.4171 0.0232 -0.0044 -0.0680 120 PRO A C 586 O O . PRO A 66 ? 0.3801 0.3826 0.4013 0.0215 -0.0049 -0.0668 120 PRO A O 587 C CB . PRO A 66 ? 0.3572 0.3655 0.3674 0.0236 0.0011 -0.0662 120 PRO A CB 588 C CG . PRO A 66 ? 0.3490 0.3595 0.3600 0.0217 0.0044 -0.0630 120 PRO A CG 589 C CD . PRO A 66 ? 0.3142 0.3237 0.3283 0.0195 0.0041 -0.0607 120 PRO A CD 590 N N . ASN A 67 ? 0.4315 0.4339 0.4428 0.0257 -0.0072 -0.0713 121 ASN A N 591 C CA . ASN A 67 ? 0.4857 0.4850 0.5017 0.0265 -0.0115 -0.0740 121 ASN A CA 592 C C . ASN A 67 ? 0.5065 0.5051 0.5250 0.0276 -0.0119 -0.0756 121 ASN A C 593 O O . ASN A 67 ? 0.5111 0.5106 0.5242 0.0298 -0.0111 -0.0772 121 ASN A O 594 C CB . ASN A 67 ? 0.4939 0.4914 0.5045 0.0292 -0.0147 -0.0771 121 ASN A CB 595 C CG . ASN A 67 ? 0.5427 0.5366 0.5585 0.0303 -0.0201 -0.0805 121 ASN A CG 596 O OD1 . ASN A 67 ? 0.5794 0.5722 0.6013 0.0301 -0.0214 -0.0815 121 ASN A OD1 597 N ND2 . ASN A 67 ? 0.6244 0.6165 0.6382 0.0316 -0.0234 -0.0823 121 ASN A ND2 598 N N . LYS A 68 ? 0.5385 0.5357 0.5651 0.0260 -0.0128 -0.0749 122 LYS A N 599 C CA . LYS A 68 ? 0.5762 0.5726 0.6059 0.0267 -0.0130 -0.0760 122 LYS A CA 600 C C . LYS A 68 ? 0.5917 0.5861 0.6195 0.0299 -0.0167 -0.0805 122 LYS A C 601 O O . LYS A 68 ? 0.5916 0.5862 0.6184 0.0312 -0.0163 -0.0816 122 LYS A O 602 C CB . LYS A 68 ? 0.5835 0.5780 0.6225 0.0247 -0.0133 -0.0742 122 LYS A CB 603 C CG . LYS A 68 ? 0.6300 0.6260 0.6704 0.0224 -0.0092 -0.0699 122 LYS A CG 604 C CD . LYS A 68 ? 0.7105 0.7043 0.7594 0.0204 -0.0093 -0.0676 122 LYS A CD 605 C CE . LYS A 68 ? 0.7362 0.7313 0.7845 0.0184 -0.0055 -0.0633 122 LYS A CE 606 N NZ . LYS A 68 ? 0.7671 0.7604 0.8226 0.0168 -0.0056 -0.0612 122 LYS A NZ 607 N N . THR A 69 ? 0.6042 0.5965 0.6313 0.0313 -0.0206 -0.0831 123 THR A N 608 C CA . THR A 69 ? 0.6263 0.6161 0.6514 0.0347 -0.0249 -0.0877 123 THR A CA 609 C C . THR A 69 ? 0.6369 0.6271 0.6511 0.0380 -0.0249 -0.0897 123 THR A C 610 O O . THR A 69 ? 0.6592 0.6469 0.6699 0.0415 -0.0287 -0.0937 123 THR A O 611 C CB . THR A 69 ? 0.6298 0.6160 0.6629 0.0347 -0.0303 -0.0901 123 THR A CB 612 O OG1 . THR A 69 ? 0.6357 0.6216 0.6676 0.0343 -0.0316 -0.0899 123 THR A OG1 613 C CG2 . THR A 69 ? 0.6218 0.6073 0.6662 0.0317 -0.0297 -0.0878 123 THR A CG2 614 N N . HIS A 70 ? 0.6276 0.6207 0.6363 0.0371 -0.0207 -0.0868 124 HIS A N 615 C CA . HIS A 70 ? 0.6280 0.6216 0.6265 0.0400 -0.0198 -0.0878 124 HIS A CA 616 C C . HIS A 70 ? 0.6047 0.6023 0.5993 0.0389 -0.0139 -0.0843 124 HIS A C 617 O O . HIS A 70 ? 0.5936 0.5929 0.5860 0.0373 -0.0115 -0.0817 124 HIS A O 618 C CB . HIS A 70 ? 0.6447 0.6365 0.6416 0.0403 -0.0225 -0.0883 124 HIS A CB 619 C CG . HIS A 70 ? 0.7061 0.6965 0.6922 0.0443 -0.0232 -0.0904 124 HIS A CG 620 N ND1 . HIS A 70 ? 0.7556 0.7444 0.7381 0.0451 -0.0252 -0.0907 124 HIS A ND1 621 C CD2 . HIS A 70 ? 0.7709 0.7611 0.7487 0.0482 -0.0221 -0.0921 124 HIS A CD2 622 C CE1 . HIS A 70 ? 0.7828 0.7702 0.7548 0.0493 -0.0252 -0.0925 124 HIS A CE1 623 N NE2 . HIS A 70 ? 0.8004 0.7886 0.7693 0.0514 -0.0231 -0.0933 124 HIS A NE2 624 N N . PRO A 71 ? 0.5873 0.5865 0.5817 0.0396 -0.0116 -0.0844 125 PRO A N 625 C CA . PRO A 71 ? 0.5592 0.5624 0.5526 0.0380 -0.0063 -0.0811 125 PRO A CA 626 C C . PRO A 71 ? 0.5414 0.5464 0.5269 0.0395 -0.0030 -0.0798 125 PRO A C 627 O O . PRO A 71 ? 0.5404 0.5438 0.5190 0.0430 -0.0039 -0.0820 125 PRO A O 628 C CB . PRO A 71 ? 0.5664 0.5703 0.5615 0.0392 -0.0056 -0.0823 125 PRO A CB 629 C CG . PRO A 71 ? 0.5871 0.5874 0.5863 0.0401 -0.0105 -0.0855 125 PRO A CG 630 C CD . PRO A 71 ? 0.5947 0.5921 0.5908 0.0417 -0.0141 -0.0875 125 PRO A CD 631 N N . ASN A 72 ? 0.4898 0.4980 0.4765 0.0369 0.0008 -0.0762 126 ASN A N 632 C CA . ASN A 72 ? 0.4775 0.4879 0.4585 0.0377 0.0047 -0.0744 126 ASN A CA 633 C C . ASN A 72 ? 0.4700 0.4824 0.4491 0.0398 0.0077 -0.0748 126 ASN A C 634 O O . ASN A 72 ? 0.4480 0.4616 0.4321 0.0389 0.0080 -0.0750 126 ASN A O 635 C CB . ASN A 72 ? 0.4576 0.4705 0.4416 0.0341 0.0075 -0.0705 126 ASN A CB 636 C CG . ASN A 72 ? 0.4672 0.4784 0.4535 0.0319 0.0050 -0.0697 126 ASN A CG 637 O OD1 . ASN A 72 ? 0.4359 0.4445 0.4191 0.0334 0.0022 -0.0715 126 ASN A OD1 638 N ND2 . ASN A 72 ? 0.4190 0.4314 0.4109 0.0285 0.0059 -0.0671 126 ASN A ND2 639 N N . TYR A 73 ? 0.4784 0.4912 0.4503 0.0429 0.0101 -0.0750 127 TYR A N 640 C CA . TYR A 73 ? 0.4936 0.5089 0.4638 0.0449 0.0141 -0.0747 127 TYR A CA 641 C C . TYR A 73 ? 0.5027 0.5184 0.4652 0.0476 0.0178 -0.0734 127 TYR A C 642 O O . TYR A 73 ? 0.5084 0.5220 0.4660 0.0483 0.0167 -0.0732 127 TYR A O 643 C CB . TYR A 73 ? 0.5045 0.5183 0.4745 0.0477 0.0120 -0.0782 127 TYR A CB 644 C CG . TYR A 73 ? 0.5353 0.5451 0.4978 0.0520 0.0088 -0.0816 127 TYR A CG 645 C CD1 . TYR A 73 ? 0.5927 0.6022 0.5481 0.0566 0.0111 -0.0828 127 TYR A CD1 646 C CD2 . TYR A 73 ? 0.5470 0.5530 0.5097 0.0518 0.0035 -0.0836 127 TYR A CD2 647 C CE1 . TYR A 73 ? 0.5911 0.5963 0.5386 0.0613 0.0078 -0.0863 127 TYR A CE1 648 C CE2 . TYR A 73 ? 0.6067 0.6088 0.5627 0.0562 0.0000 -0.0872 127 TYR A CE2 649 C CZ . TYR A 73 ? 0.6070 0.6084 0.5549 0.0610 0.0020 -0.0886 127 TYR A CZ 650 O OH . TYR A 73 ? 0.6307 0.6276 0.5712 0.0658 -0.0018 -0.0924 127 TYR A OH 651 N N . ILE A 74 ? 0.4991 0.5177 0.4612 0.0490 0.0224 -0.0723 128 ILE A N 652 C CA . ILE A 74 ? 0.5033 0.5224 0.4587 0.0518 0.0269 -0.0706 128 ILE A CA 653 C C . ILE A 74 ? 0.5233 0.5418 0.4740 0.0567 0.0281 -0.0729 128 ILE A C 654 O O . ILE A 74 ? 0.4947 0.5144 0.4501 0.0565 0.0276 -0.0744 128 ILE A O 655 C CB . ILE A 74 ? 0.5030 0.5265 0.4633 0.0491 0.0321 -0.0665 128 ILE A CB 656 C CG1 . ILE A 74 ? 0.4711 0.4951 0.4353 0.0448 0.0309 -0.0642 128 ILE A CG1 657 C CG2 . ILE A 74 ? 0.5077 0.5319 0.4619 0.0523 0.0375 -0.0645 128 ILE A CG2 658 C CD1 . ILE A 74 ? 0.4805 0.5087 0.4526 0.0414 0.0343 -0.0611 128 ILE A CD1 659 N N . SER A 75 ? 0.5504 0.5665 0.4913 0.0611 0.0297 -0.0732 129 SER A N 660 C CA . SER A 75 ? 0.5821 0.5969 0.5165 0.0665 0.0313 -0.0753 129 SER A CA 661 C C . SER A 75 ? 0.6002 0.6165 0.5295 0.0694 0.0382 -0.0723 129 SER A C 662 O O . SER A 75 ? 0.5912 0.6076 0.5182 0.0685 0.0406 -0.0693 129 SER A O 663 C CB . SER A 75 ? 0.5851 0.5942 0.5107 0.0707 0.0261 -0.0792 129 SER A CB 664 O OG . SER A 75 ? 0.6087 0.6164 0.5397 0.0689 0.0200 -0.0824 129 SER A OG 665 N N . ILE A 76 ? 0.6265 0.6440 0.5544 0.0729 0.0416 -0.0728 130 ILE A N 666 C CA . ILE A 76 ? 0.6581 0.6747 0.5769 0.0780 0.0473 -0.0711 130 ILE A CA 667 C C . ILE A 76 ? 0.6774 0.6882 0.5846 0.0840 0.0434 -0.0753 130 ILE A C 668 O O . ILE A 76 ? 0.6753 0.6850 0.5836 0.0852 0.0394 -0.0790 130 ILE A O 669 C CB . ILE A 76 ? 0.6622 0.6831 0.5853 0.0791 0.0540 -0.0690 130 ILE A CB 670 C CG1 . ILE A 76 ? 0.6356 0.6620 0.5706 0.0735 0.0575 -0.0652 130 ILE A CG1 671 C CG2 . ILE A 76 ? 0.6774 0.6965 0.5899 0.0853 0.0599 -0.0674 130 ILE A CG2 672 C CD1 . ILE A 76 ? 0.6202 0.6512 0.5637 0.0732 0.0615 -0.0644 130 ILE A CD1 673 N N . ILE A 77 ? 0.7068 0.7138 0.6032 0.0877 0.0441 -0.0747 131 ILE A N 674 C CA . ILE A 77 ? 0.7369 0.7377 0.6208 0.0942 0.0403 -0.0786 131 ILE A CA 675 C C . ILE A 77 ? 0.7497 0.7494 0.6233 0.1008 0.0471 -0.0770 131 ILE A C 676 O O . ILE A 77 ? 0.7554 0.7571 0.6282 0.1006 0.0538 -0.0723 131 ILE A O 677 C CB . ILE A 77 ? 0.7435 0.7397 0.6212 0.0944 0.0352 -0.0797 131 ILE A CB 678 C CG1 . ILE A 77 ? 0.7547 0.7529 0.6336 0.0913 0.0396 -0.0748 131 ILE A CG1 679 C CG2 . ILE A 77 ? 0.7299 0.7251 0.6147 0.0905 0.0271 -0.0832 131 ILE A CG2 680 C CD1 . ILE A 77 ? 0.7885 0.7814 0.6562 0.0946 0.0374 -0.0752 131 ILE A CD1 681 N N . ASN A 82 ? 0.8311 0.8107 0.6835 0.1140 0.0187 -0.0973 136 ASN A N 682 C CA . ASN A 82 ? 0.8248 0.8082 0.6878 0.1110 0.0183 -0.0984 136 ASN A CA 683 C C . ASN A 82 ? 0.7957 0.7862 0.6718 0.1035 0.0229 -0.0938 136 ASN A C 684 O O . ASN A 82 ? 0.7977 0.7916 0.6734 0.1030 0.0304 -0.0892 136 ASN A O 685 C CB . ASN A 82 ? 0.8393 0.8225 0.6960 0.1170 0.0222 -0.0994 136 ASN A CB 686 C CG . ASN A 82 ? 0.8874 0.8634 0.7322 0.1246 0.0165 -0.1048 136 ASN A CG 687 O OD1 . ASN A 82 ? 0.9142 0.8868 0.7611 0.1241 0.0081 -0.1093 136 ASN A OD1 688 N ND2 . ASN A 82 ? 0.9193 0.8929 0.7517 0.1319 0.0212 -0.1045 136 ASN A ND2 689 N N . GLU A 83 ? 0.7620 0.7544 0.6497 0.0979 0.0185 -0.0950 137 GLU A N 690 C CA . GLU A 83 ? 0.7290 0.7274 0.6291 0.0909 0.0217 -0.0913 137 GLU A CA 691 C C . GLU A 83 ? 0.7092 0.7114 0.6156 0.0905 0.0246 -0.0913 137 GLU A C 692 O O . GLU A 83 ? 0.6902 0.6918 0.6015 0.0897 0.0202 -0.0944 137 GLU A O 693 C CB . GLU A 83 ? 0.7187 0.7170 0.6275 0.0852 0.0159 -0.0920 137 GLU A CB 694 C CG . GLU A 83 ? 0.7242 0.7192 0.6281 0.0851 0.0132 -0.0917 137 GLU A CG 695 C CD . GLU A 83 ? 0.7179 0.7135 0.6312 0.0790 0.0089 -0.0914 137 GLU A CD 696 O OE1 . GLU A 83 ? 0.7070 0.7037 0.6293 0.0759 0.0058 -0.0928 137 GLU A OE1 697 O OE2 . GLU A 83 ? 0.7131 0.7079 0.6244 0.0777 0.0086 -0.0897 137 GLU A OE2 698 N N . ILE A 84 ? 0.7028 0.7089 0.6097 0.0908 0.0322 -0.0876 138 ILE A N 699 C CA . ILE A 84 ? 0.6984 0.7080 0.6096 0.0918 0.0360 -0.0875 138 ILE A CA 700 C C . ILE A 84 ? 0.6764 0.6915 0.6013 0.0854 0.0375 -0.0852 138 ILE A C 701 O O . ILE A 84 ? 0.6711 0.6889 0.6016 0.0854 0.0387 -0.0859 138 ILE A O 702 C CB . ILE A 84 ? 0.7106 0.7209 0.6141 0.0970 0.0437 -0.0851 138 ILE A CB 703 C CG1 . ILE A 84 ? 0.7127 0.7264 0.6189 0.0942 0.0499 -0.0796 138 ILE A CG1 704 C CG2 . ILE A 84 ? 0.7373 0.7412 0.6259 0.1043 0.0416 -0.0880 138 ILE A CG2 705 C CD1 . ILE A 84 ? 0.7199 0.7357 0.6224 0.0982 0.0587 -0.0763 138 ILE A CD1 706 N N . PHE A 85 ? 0.6434 0.6601 0.5737 0.0803 0.0369 -0.0826 139 PHE A N 707 C CA . PHE A 85 ? 0.6209 0.6418 0.5635 0.0744 0.0368 -0.0811 139 PHE A CA 708 C C . PHE A 85 ? 0.5955 0.6149 0.5408 0.0700 0.0323 -0.0807 139 PHE A C 709 O O . PHE A 85 ? 0.5858 0.6035 0.5258 0.0704 0.0326 -0.0794 139 PHE A O 710 C CB . PHE A 85 ? 0.6189 0.6449 0.5669 0.0726 0.0438 -0.0768 139 PHE A CB 711 C CG . PHE A 85 ? 0.6237 0.6532 0.5832 0.0665 0.0431 -0.0750 139 PHE A CG 712 C CD1 . PHE A 85 ? 0.6256 0.6571 0.5930 0.0648 0.0413 -0.0765 139 PHE A CD1 713 C CD2 . PHE A 85 ? 0.6235 0.6541 0.5855 0.0628 0.0439 -0.0719 139 PHE A CD2 714 C CE1 . PHE A 85 ? 0.6259 0.6599 0.6029 0.0598 0.0403 -0.0750 139 PHE A CE1 715 C CE2 . PHE A 85 ? 0.5871 0.6205 0.5590 0.0577 0.0429 -0.0704 139 PHE A CE2 716 C CZ . PHE A 85 ? 0.5942 0.6292 0.5733 0.0563 0.0411 -0.0719 139 PHE A CZ 717 N N . ASN A 86 ? 0.5799 0.5996 0.5330 0.0665 0.0283 -0.0820 140 ASN A N 718 C CA . ASN A 86 ? 0.5641 0.5831 0.5218 0.0618 0.0247 -0.0812 140 ASN A CA 719 C C . ASN A 86 ? 0.5298 0.5529 0.4977 0.0570 0.0262 -0.0787 140 ASN A C 720 O O . ASN A 86 ? 0.5179 0.5427 0.4909 0.0567 0.0264 -0.0796 140 ASN A O 721 C CB . ASN A 86 ? 0.5779 0.5930 0.5361 0.0620 0.0181 -0.0850 140 ASN A CB 722 C CG . ASN A 86 ? 0.6377 0.6480 0.5864 0.0665 0.0150 -0.0879 140 ASN A CG 723 O OD1 . ASN A 86 ? 0.6837 0.6931 0.6255 0.0683 0.0169 -0.0866 140 ASN A OD1 724 N ND2 . ASN A 86 ? 0.7043 0.7114 0.6527 0.0685 0.0100 -0.0918 140 ASN A ND2 725 N N . THR A 87 ? 0.5051 0.5291 0.4756 0.0533 0.0267 -0.0759 141 THR A N 726 C CA . THR A 87 ? 0.4694 0.4964 0.4491 0.0489 0.0271 -0.0740 141 THR A CA 727 C C . THR A 87 ? 0.4513 0.4760 0.4351 0.0473 0.0220 -0.0761 141 THR A C 728 O O . THR A 87 ? 0.4616 0.4827 0.4420 0.0489 0.0182 -0.0787 141 THR A O 729 C CB . THR A 87 ? 0.4559 0.4841 0.4370 0.0457 0.0285 -0.0706 141 THR A CB 730 O OG1 . THR A 87 ? 0.4408 0.4655 0.4179 0.0454 0.0249 -0.0714 141 THR A OG1 731 C CG2 . THR A 87 ? 0.4773 0.5077 0.4553 0.0472 0.0339 -0.0681 141 THR A CG2 732 N N . SER A 88 ? 0.4457 0.4722 0.4368 0.0443 0.0218 -0.0750 142 SER A N 733 C CA . SER A 88 ? 0.4283 0.4527 0.4237 0.0429 0.0177 -0.0766 142 SER A CA 734 C C . SER A 88 ? 0.4356 0.4570 0.4308 0.0409 0.0144 -0.0763 142 SER A C 735 O O . SER A 88 ? 0.4414 0.4631 0.4352 0.0393 0.0154 -0.0742 142 SER A O 736 C CB . SER A 88 ? 0.4358 0.4626 0.4383 0.0404 0.0187 -0.0750 142 SER A CB 737 O OG A SER A 88 ? 0.4484 0.4735 0.4540 0.0406 0.0159 -0.0769 142 SER A OG 738 O OG B SER A 88 ? 0.3974 0.4248 0.4022 0.0372 0.0191 -0.0722 142 SER A OG 739 N N . LEU A 89 ? 0.4328 0.4512 0.4301 0.0408 0.0105 -0.0783 143 LEU A N 740 C CA . LEU A 89 ? 0.4470 0.4626 0.4458 0.0389 0.0074 -0.0780 143 LEU A CA 741 C C . LEU A 89 ? 0.4378 0.4538 0.4427 0.0354 0.0075 -0.0755 143 LEU A C 742 O O . LEU A 89 ? 0.4380 0.4523 0.4447 0.0335 0.0060 -0.0744 143 LEU A O 743 C CB . LEU A 89 ? 0.4642 0.4760 0.4628 0.0406 0.0031 -0.0813 143 LEU A CB 744 C CG . LEU A 89 ? 0.4955 0.5057 0.4871 0.0446 0.0020 -0.0842 143 LEU A CG 745 C CD1 . LEU A 89 ? 0.5382 0.5443 0.5307 0.0459 -0.0031 -0.0875 143 LEU A CD1 746 C CD2 . LEU A 89 ? 0.4980 0.5088 0.4841 0.0449 0.0036 -0.0828 143 LEU A CD2 747 N N . PHE A 90 ? 0.4161 0.4343 0.4240 0.0351 0.0094 -0.0748 144 PHE A N 748 C CA . PHE A 90 ? 0.4006 0.4188 0.4135 0.0326 0.0093 -0.0728 144 PHE A CA 749 C C . PHE A 90 ? 0.3930 0.4140 0.4081 0.0330 0.0115 -0.0723 144 PHE A C 750 O O . PHE A 90 ? 0.3916 0.4142 0.4055 0.0352 0.0126 -0.0741 144 PHE A O 751 C CB . PHE A 90 ? 0.4078 0.4223 0.4239 0.0324 0.0063 -0.0737 144 PHE A CB 752 C CG . PHE A 90 ? 0.4320 0.4456 0.4484 0.0347 0.0049 -0.0767 144 PHE A CG 753 C CD1 . PHE A 90 ? 0.4529 0.4673 0.4720 0.0352 0.0055 -0.0769 144 PHE A CD1 754 C CD2 . PHE A 90 ? 0.5090 0.5208 0.5227 0.0368 0.0027 -0.0795 144 PHE A CD2 755 C CE1 . PHE A 90 ? 0.5170 0.5306 0.5363 0.0375 0.0042 -0.0797 144 PHE A CE1 756 C CE2 . PHE A 90 ? 0.5195 0.5303 0.5333 0.0393 0.0012 -0.0824 144 PHE A CE2 757 C CZ . PHE A 90 ? 0.5355 0.5473 0.5522 0.0395 0.0021 -0.0825 144 PHE A CZ 758 N N . GLU A 91 ? 0.3513 0.3728 0.3695 0.0311 0.0121 -0.0702 145 GLU A N 759 C CA . GLU A 91 ? 0.3468 0.3706 0.3682 0.0314 0.0133 -0.0701 145 GLU A CA 760 C C . GLU A 91 ? 0.3453 0.3667 0.3687 0.0325 0.0112 -0.0718 145 GLU A C 761 O O . GLU A 91 ? 0.3473 0.3654 0.3715 0.0318 0.0092 -0.0715 145 GLU A O 762 C CB . GLU A 91 ? 0.3322 0.3566 0.3559 0.0294 0.0138 -0.0676 145 GLU A CB 763 C CG . GLU A 91 ? 0.3259 0.3524 0.3483 0.0281 0.0158 -0.0656 145 GLU A CG 764 C CD . GLU A 91 ? 0.3370 0.3630 0.3615 0.0263 0.0155 -0.0633 145 GLU A CD 765 O OE1 . GLU A 91 ? 0.3551 0.3782 0.3787 0.0253 0.0141 -0.0623 145 GLU A OE1 766 O OE2 . GLU A 91 ? 0.3521 0.3805 0.3794 0.0261 0.0165 -0.0627 145 GLU A OE2 767 N N . PRO A 92 ? 0.3628 0.3861 0.3878 0.0342 0.0118 -0.0734 146 PRO A N 768 C CA . PRO A 92 ? 0.3693 0.3902 0.3965 0.0352 0.0098 -0.0749 146 PRO A CA 769 C C . PRO A 92 ? 0.3613 0.3799 0.3906 0.0338 0.0087 -0.0729 146 PRO A C 770 O O . PRO A 92 ? 0.3515 0.3716 0.3822 0.0331 0.0096 -0.0715 146 PRO A O 771 C CB . PRO A 92 ? 0.3812 0.4052 0.4103 0.0370 0.0111 -0.0763 146 PRO A CB 772 C CG . PRO A 92 ? 0.3819 0.4093 0.4088 0.0376 0.0138 -0.0764 146 PRO A CG 773 C CD . PRO A 92 ? 0.3649 0.3922 0.3901 0.0354 0.0145 -0.0738 146 PRO A CD 774 N N . PRO A 93 ? 0.3668 0.3813 0.3962 0.0336 0.0067 -0.0728 147 PRO A N 775 C CA . PRO A 93 ? 0.3705 0.3825 0.4009 0.0325 0.0063 -0.0705 147 PRO A CA 776 C C . PRO A 93 ? 0.3806 0.3926 0.4128 0.0338 0.0060 -0.0708 147 PRO A C 777 O O . PRO A 93 ? 0.3817 0.3944 0.4150 0.0354 0.0054 -0.0731 147 PRO A O 778 C CB . PRO A 93 ? 0.3761 0.3838 0.4072 0.0324 0.0047 -0.0703 147 PRO A CB 779 C CG . PRO A 93 ? 0.3970 0.4048 0.4279 0.0337 0.0036 -0.0732 147 PRO A CG 780 C CD . PRO A 93 ? 0.3739 0.3857 0.4026 0.0340 0.0050 -0.0742 147 PRO A CD 781 N N . PRO A 94 ? 0.3711 0.3820 0.4033 0.0332 0.0060 -0.0688 148 PRO A N 782 C CA . PRO A 94 ? 0.3725 0.3829 0.4060 0.0346 0.0052 -0.0691 148 PRO A CA 783 C C . PRO A 94 ? 0.3709 0.3771 0.4046 0.0362 0.0036 -0.0698 148 PRO A C 784 O O . PRO A 94 ? 0.3457 0.3485 0.3787 0.0358 0.0033 -0.0689 148 PRO A O 785 C CB . PRO A 94 ? 0.3834 0.3928 0.4159 0.0339 0.0053 -0.0667 148 PRO A CB 786 C CG . PRO A 94 ? 0.3694 0.3774 0.4000 0.0322 0.0061 -0.0646 148 PRO A CG 787 C CD . PRO A 94 ? 0.3800 0.3898 0.4107 0.0315 0.0067 -0.0661 148 PRO A CD 788 N N . PRO A 95 ? 0.3629 0.3691 0.3979 0.0381 0.0026 -0.0713 149 PRO A N 789 C CA . PRO A 95 ? 0.3699 0.3721 0.4049 0.0398 0.0011 -0.0720 149 PRO A CA 790 C C . PRO A 95 ? 0.3704 0.3670 0.4034 0.0399 0.0009 -0.0694 149 PRO A C 791 O O . PRO A 95 ? 0.3745 0.3695 0.4056 0.0399 0.0011 -0.0673 149 PRO A O 792 C CB . PRO A 95 ? 0.3634 0.3663 0.3997 0.0417 0.0000 -0.0734 149 PRO A CB 793 C CG . PRO A 95 ? 0.3764 0.3849 0.4150 0.0409 0.0010 -0.0743 149 PRO A CG 794 C CD . PRO A 95 ? 0.3556 0.3655 0.3927 0.0386 0.0026 -0.0723 149 PRO A CD 795 N N . GLY A 96 ? 0.3793 0.3729 0.4130 0.0401 0.0005 -0.0694 150 GLY A N 796 C CA . GLY A 96 ? 0.4168 0.4049 0.4494 0.0404 0.0008 -0.0667 150 GLY A CA 797 C C . GLY A 96 ? 0.4530 0.4404 0.4855 0.0382 0.0022 -0.0644 150 GLY A C 798 O O . GLY A 96 ? 0.4448 0.4280 0.4773 0.0383 0.0029 -0.0618 150 GLY A O 799 N N . TYR A 97 ? 0.4722 0.4639 0.5050 0.0365 0.0027 -0.0650 151 TYR A N 800 C CA . TYR A 97 ? 0.5280 0.5192 0.5608 0.0346 0.0038 -0.0629 151 TYR A CA 801 C C . TYR A 97 ? 0.5809 0.5712 0.6166 0.0338 0.0032 -0.0639 151 TYR A C 802 O O . TYR A 97 ? 0.6053 0.5981 0.6417 0.0340 0.0021 -0.0668 151 TYR A O 803 C CB . TYR A 97 ? 0.5022 0.4974 0.5334 0.0332 0.0047 -0.0625 151 TYR A CB 804 C CG . TYR A 97 ? 0.4518 0.4456 0.4807 0.0339 0.0052 -0.0603 151 TYR A CG 805 C CD1 . TYR A 97 ? 0.4071 0.3984 0.4345 0.0332 0.0063 -0.0573 151 TYR A CD1 806 C CD2 . TYR A 97 ? 0.3862 0.3810 0.4144 0.0355 0.0043 -0.0616 151 TYR A CD2 807 C CE1 . TYR A 97 ? 0.3977 0.3871 0.4222 0.0343 0.0065 -0.0555 151 TYR A CE1 808 C CE2 . TYR A 97 ? 0.3612 0.3542 0.3871 0.0365 0.0041 -0.0601 151 TYR A CE2 809 C CZ . TYR A 97 ? 0.3680 0.3582 0.3916 0.0360 0.0052 -0.0570 151 TYR A CZ 810 O OH . TYR A 97 ? 0.3612 0.3492 0.3818 0.0375 0.0048 -0.0557 151 TYR A OH 811 N N . GLU A 98 ? 0.6319 0.6185 0.6694 0.0332 0.0037 -0.0615 152 GLU A N 812 C CA . GLU A 98 ? 0.6747 0.6594 0.7164 0.0326 0.0027 -0.0622 152 GLU A CA 813 C C . GLU A 98 ? 0.6794 0.6646 0.7234 0.0305 0.0028 -0.0615 152 GLU A C 814 O O . GLU A 98 ? 0.6783 0.6624 0.7260 0.0303 0.0011 -0.0631 152 GLU A O 815 C CB . GLU A 98 ? 0.6901 0.6695 0.7344 0.0337 0.0029 -0.0606 152 GLU A CB 816 C CG . GLU A 98 ? 0.7114 0.6871 0.7543 0.0340 0.0052 -0.0564 152 GLU A CG 817 C CD . GLU A 98 ? 0.7588 0.7294 0.8026 0.0359 0.0057 -0.0549 152 GLU A CD 818 O OE1 . GLU A 98 ? 0.7922 0.7615 0.8395 0.0364 0.0042 -0.0567 152 GLU A OE1 819 O OE2 . GLU A 98 ? 0.7695 0.7370 0.8101 0.0373 0.0075 -0.0519 152 GLU A OE2 820 N N . ASN A 99 ? 0.6917 0.6780 0.7339 0.0292 0.0042 -0.0594 153 ASN A N 821 C CA . ASN A 99 ? 0.7152 0.7016 0.7608 0.0275 0.0037 -0.0592 153 ASN A CA 822 C C . ASN A 99 ? 0.7133 0.7036 0.7567 0.0268 0.0027 -0.0615 153 ASN A C 823 O O . ASN A 99 ? 0.7233 0.7143 0.7674 0.0254 0.0029 -0.0606 153 ASN A O 824 C CB . ASN A 99 ? 0.7156 0.6991 0.7636 0.0265 0.0055 -0.0554 153 ASN A CB 825 C CG . ASN A 99 ? 0.7445 0.7238 0.7989 0.0266 0.0053 -0.0545 153 ASN A CG 826 O OD1 . ASN A 99 ? 0.7501 0.7285 0.8073 0.0273 0.0032 -0.0570 153 ASN A OD1 827 N ND2 . ASN A 99 ? 0.7725 0.7490 0.8295 0.0261 0.0075 -0.0507 153 ASN A ND2 828 N N . VAL A 100 ? 0.7229 0.7155 0.7643 0.0280 0.0016 -0.0645 154 VAL A N 829 C CA . VAL A 100 ? 0.7244 0.7212 0.7620 0.0280 0.0017 -0.0663 154 VAL A CA 830 C C . VAL A 100 ? 0.7230 0.7207 0.7602 0.0270 0.0008 -0.0670 154 VAL A C 831 O O . VAL A 100 ? 0.7272 0.7280 0.7608 0.0268 0.0017 -0.0672 154 VAL A O 832 C CB . VAL A 100 ? 0.7291 0.7277 0.7649 0.0299 0.0010 -0.0694 154 VAL A CB 833 C CG1 . VAL A 100 ? 0.7131 0.7110 0.7490 0.0309 0.0017 -0.0686 154 VAL A CG1 834 C CG2 . VAL A 100 ? 0.7310 0.7280 0.7689 0.0311 -0.0015 -0.0725 154 VAL A CG2 835 N N . SER A 101 ? 0.7184 0.7134 0.7597 0.0266 -0.0009 -0.0674 155 SER A N 836 C CA . SER A 101 ? 0.6991 0.6945 0.7405 0.0259 -0.0022 -0.0681 155 SER A CA 837 C C . SER A 101 ? 0.6662 0.6620 0.7076 0.0239 -0.0004 -0.0648 155 SER A C 838 O O . SER A 101 ? 0.6773 0.6749 0.7161 0.0234 -0.0005 -0.0652 155 SER A O 839 C CB . SER A 101 ? 0.7138 0.7062 0.7603 0.0262 -0.0054 -0.0702 155 SER A CB 840 O OG . SER A 101 ? 0.7432 0.7324 0.7957 0.0257 -0.0050 -0.0683 155 SER A OG 841 N N . ASP A 102 ? 0.6203 0.6143 0.6639 0.0232 0.0014 -0.0617 156 ASP A N 842 C CA . ASP A 102 ? 0.5654 0.5597 0.6082 0.0217 0.0034 -0.0584 156 ASP A CA 843 C C . ASP A 102 ? 0.5101 0.5074 0.5474 0.0217 0.0052 -0.0576 156 ASP A C 844 O O . ASP A 102 ? 0.4865 0.4843 0.5224 0.0207 0.0067 -0.0552 156 ASP A O 845 C CB . ASP A 102 ? 0.5933 0.5842 0.6400 0.0213 0.0049 -0.0551 156 ASP A CB 846 C CG . ASP A 102 ? 0.6463 0.6353 0.6993 0.0200 0.0041 -0.0544 156 ASP A CG 847 O OD1 . ASP A 102 ? 0.6885 0.6746 0.7454 0.0197 0.0058 -0.0514 156 ASP A OD1 848 O OD2 . ASP A 102 ? 0.6847 0.6748 0.7387 0.0196 0.0018 -0.0568 156 ASP A OD2 849 N N . ILE A 103 ? 0.4382 0.4375 0.4728 0.0230 0.0049 -0.0597 157 ILE A N 850 C CA . ILE A 103 ? 0.4009 0.4034 0.4314 0.0229 0.0063 -0.0595 157 ILE A CA 851 C C . ILE A 103 ? 0.3897 0.3946 0.4181 0.0224 0.0059 -0.0607 157 ILE A C 852 O O . ILE A 103 ? 0.3849 0.3901 0.4127 0.0234 0.0044 -0.0634 157 ILE A O 853 C CB . ILE A 103 ? 0.3734 0.3775 0.4028 0.0245 0.0063 -0.0614 157 ILE A CB 854 C CG1 . ILE A 103 ? 0.3575 0.3591 0.3882 0.0253 0.0066 -0.0601 157 ILE A CG1 855 C CG2 . ILE A 103 ? 0.3419 0.3499 0.3684 0.0244 0.0077 -0.0614 157 ILE A CG2 856 C CD1 . ILE A 103 ? 0.3253 0.3278 0.3559 0.0271 0.0061 -0.0623 157 ILE A CD1 857 N N . VAL A 104 ? 0.3626 0.3686 0.3893 0.0211 0.0070 -0.0587 158 VAL A N 858 C CA . VAL A 104 ? 0.3519 0.3599 0.3760 0.0208 0.0068 -0.0596 158 VAL A CA 859 C C . VAL A 104 ? 0.3491 0.3601 0.3699 0.0220 0.0077 -0.0612 158 VAL A C 860 O O . VAL A 104 ? 0.3259 0.3387 0.3463 0.0219 0.0093 -0.0602 158 VAL A O 861 C CB . VAL A 104 ? 0.3268 0.3355 0.3499 0.0190 0.0079 -0.0570 158 VAL A CB 862 C CG1 . VAL A 104 ? 0.3392 0.3504 0.3600 0.0187 0.0100 -0.0554 158 VAL A CG1 863 C CG2 . VAL A 104 ? 0.3429 0.3521 0.3640 0.0189 0.0069 -0.0582 158 VAL A CG2 864 N N . PRO A 105 ? 0.3550 0.3665 0.3737 0.0234 0.0067 -0.0638 159 PRO A N 865 C CA . PRO A 105 ? 0.3584 0.3728 0.3739 0.0248 0.0082 -0.0649 159 PRO A CA 866 C C . PRO A 105 ? 0.3424 0.3594 0.3555 0.0238 0.0105 -0.0630 159 PRO A C 867 O O . PRO A 105 ? 0.3317 0.3481 0.3444 0.0223 0.0104 -0.0613 159 PRO A O 868 C CB . PRO A 105 ? 0.3646 0.3779 0.3775 0.0269 0.0064 -0.0680 159 PRO A CB 869 C CG . PRO A 105 ? 0.3951 0.4057 0.4092 0.0260 0.0040 -0.0680 159 PRO A CG 870 C CD . PRO A 105 ? 0.3761 0.3854 0.3951 0.0238 0.0041 -0.0655 159 PRO A CD 871 N N . PRO A 106 ? 0.3243 0.3443 0.3362 0.0247 0.0127 -0.0630 160 PRO A N 872 C CA . PRO A 106 ? 0.3245 0.3468 0.3349 0.0237 0.0150 -0.0610 160 PRO A CA 873 C C . PRO A 106 ? 0.3255 0.3473 0.3318 0.0239 0.0148 -0.0610 160 PRO A C 874 O O . PRO A 106 ? 0.3361 0.3567 0.3391 0.0258 0.0139 -0.0631 160 PRO A O 875 C CB . PRO A 106 ? 0.3171 0.3425 0.3277 0.0251 0.0174 -0.0616 160 PRO A CB 876 C CG . PRO A 106 ? 0.3110 0.3357 0.3246 0.0260 0.0161 -0.0633 160 PRO A CG 877 C CD . PRO A 106 ? 0.3328 0.3541 0.3454 0.0265 0.0134 -0.0648 160 PRO A CD 878 N N . PHE A 107 ? 0.3107 0.3328 0.3166 0.0220 0.0155 -0.0587 161 PHE A N 879 C CA . PHE A 107 ? 0.3112 0.3328 0.3131 0.0222 0.0155 -0.0584 161 PHE A CA 880 C C . PHE A 107 ? 0.2999 0.3230 0.3022 0.0202 0.0172 -0.0556 161 PHE A C 881 O O . PHE A 107 ? 0.2929 0.3168 0.2987 0.0188 0.0176 -0.0542 161 PHE A O 882 C CB . PHE A 107 ? 0.3214 0.3398 0.3234 0.0220 0.0123 -0.0595 161 PHE A CB 883 C CG . PHE A 107 ? 0.3218 0.3390 0.3275 0.0196 0.0114 -0.0575 161 PHE A CG 884 C CD1 . PHE A 107 ? 0.3116 0.3278 0.3163 0.0184 0.0107 -0.0564 161 PHE A CD1 885 C CD2 . PHE A 107 ? 0.3139 0.3305 0.3237 0.0188 0.0113 -0.0569 161 PHE A CD2 886 C CE1 . PHE A 107 ? 0.2993 0.3144 0.3073 0.0165 0.0102 -0.0545 161 PHE A CE1 887 C CE2 . PHE A 107 ? 0.3070 0.3221 0.3195 0.0171 0.0109 -0.0548 161 PHE A CE2 888 C CZ . PHE A 107 ? 0.2960 0.3105 0.3078 0.0159 0.0105 -0.0536 161 PHE A CZ 889 N N . SER A 108 ? 0.2932 0.3163 0.2915 0.0203 0.0179 -0.0549 162 SER A N 890 C CA . SER A 108 ? 0.2857 0.3101 0.2842 0.0184 0.0193 -0.0522 162 SER A CA 891 C C . SER A 108 ? 0.2898 0.3118 0.2878 0.0173 0.0170 -0.0519 162 SER A C 892 O O . SER A 108 ? 0.2934 0.3138 0.2877 0.0184 0.0158 -0.0529 162 SER A O 893 C CB . SER A 108 ? 0.3084 0.3342 0.3028 0.0195 0.0220 -0.0514 162 SER A CB 894 O OG . SER A 108 ? 0.3090 0.3374 0.3049 0.0206 0.0247 -0.0515 162 SER A OG 895 N N . ALA A 109 ? 0.2737 0.2952 0.2753 0.0154 0.0164 -0.0504 163 ALA A N 896 C CA . ALA A 109 ? 0.2821 0.3014 0.2843 0.0143 0.0144 -0.0499 163 ALA A CA 897 C C . ALA A 109 ? 0.2834 0.3029 0.2821 0.0139 0.0148 -0.0489 163 ALA A C 898 O O . ALA A 109 ? 0.2793 0.3005 0.2769 0.0133 0.0167 -0.0472 163 ALA A O 899 C CB . ALA A 109 ? 0.2769 0.2955 0.2829 0.0128 0.0144 -0.0480 163 ALA A CB 900 N N . PHE A 110 ? 0.2938 0.3111 0.2912 0.0144 0.0125 -0.0501 164 PHE A N 901 C CA . PHE A 110 ? 0.3207 0.3373 0.3146 0.0143 0.0119 -0.0497 164 PHE A CA 902 C C . PHE A 110 ? 0.3400 0.3567 0.3278 0.0166 0.0126 -0.0509 164 PHE A C 903 O O . PHE A 110 ? 0.3592 0.3749 0.3431 0.0170 0.0122 -0.0505 164 PHE A O 904 C CB . PHE A 110 ? 0.3099 0.3275 0.3045 0.0123 0.0132 -0.0468 164 PHE A CB 905 C CG . PHE A 110 ? 0.2781 0.2948 0.2773 0.0107 0.0124 -0.0457 164 PHE A CG 906 C CD1 . PHE A 110 ? 0.2780 0.2926 0.2792 0.0101 0.0103 -0.0459 164 PHE A CD1 907 C CD2 . PHE A 110 ? 0.2943 0.3119 0.2961 0.0099 0.0138 -0.0443 164 PHE A CD2 908 C CE1 . PHE A 110 ? 0.2974 0.3111 0.3029 0.0089 0.0102 -0.0444 164 PHE A CE1 909 C CE2 . PHE A 110 ? 0.2732 0.2896 0.2784 0.0090 0.0134 -0.0431 164 PHE A CE2 910 C CZ . PHE A 110 ? 0.2395 0.2540 0.2464 0.0085 0.0119 -0.0429 164 PHE A CZ 911 N N . SER A 111 ? 0.3492 0.3665 0.3358 0.0184 0.0135 -0.0523 165 SER A N 912 C CA . SER A 111 ? 0.3720 0.3887 0.3520 0.0213 0.0141 -0.0536 165 SER A CA 913 C C . SER A 111 ? 0.3761 0.3896 0.3531 0.0227 0.0105 -0.0558 165 SER A C 914 O O . SER A 111 ? 0.3791 0.3908 0.3598 0.0224 0.0072 -0.0576 165 SER A O 915 C CB . SER A 111 ? 0.3770 0.3945 0.3564 0.0234 0.0153 -0.0552 165 SER A CB 916 O OG . SER A 111 ? 0.3778 0.3941 0.3501 0.0266 0.0158 -0.0566 165 SER A OG 917 N N . PRO A 112 ? 0.3979 0.4103 0.3684 0.0244 0.0108 -0.0557 166 PRO A N 918 C CA . PRO A 112 ? 0.4140 0.4229 0.3809 0.0268 0.0068 -0.0586 166 PRO A CA 919 C C . PRO A 112 ? 0.4401 0.4476 0.4046 0.0300 0.0054 -0.0618 166 PRO A C 920 O O . PRO A 112 ? 0.4279 0.4373 0.3921 0.0307 0.0084 -0.0614 166 PRO A O 921 C CB . PRO A 112 ? 0.4237 0.4316 0.3831 0.0284 0.0079 -0.0576 166 PRO A CB 922 C CG . PRO A 112 ? 0.3979 0.4084 0.3553 0.0283 0.0130 -0.0549 166 PRO A CG 923 C CD . PRO A 112 ? 0.4093 0.4230 0.3751 0.0248 0.0145 -0.0532 166 PRO A CD 924 N N . GLN A 113 ? 0.4599 0.4641 0.4233 0.0319 0.0009 -0.0650 167 GLN A N 925 C CA . GLN A 113 ? 0.4951 0.4972 0.4549 0.0357 -0.0010 -0.0685 167 GLN A CA 926 C C . GLN A 113 ? 0.5167 0.5174 0.4658 0.0398 0.0006 -0.0689 167 GLN A C 927 O O . GLN A 113 ? 0.5217 0.5219 0.4659 0.0402 0.0020 -0.0672 167 GLN A O 928 C CB . GLN A 113 ? 0.4988 0.4973 0.4612 0.0366 -0.0070 -0.0720 167 GLN A CB 929 C CG . GLN A 113 ? 0.5246 0.5241 0.4977 0.0332 -0.0085 -0.0718 167 GLN A CG 930 C CD . GLN A 113 ? 0.5769 0.5732 0.5542 0.0338 -0.0142 -0.0748 167 GLN A CD 931 O OE1 . GLN A 113 ? 0.6464 0.6396 0.6184 0.0368 -0.0175 -0.0774 167 GLN A OE1 932 N NE2 . GLN A 113 ? 0.5986 0.5951 0.5855 0.0311 -0.0154 -0.0745 167 GLN A NE2 933 N N . GLY A 114 ? 0.5445 0.5442 0.4897 0.0433 0.0006 -0.0712 168 GLY A N 934 C CA . GLY A 114 ? 0.5763 0.5745 0.5108 0.0477 0.0029 -0.0713 168 GLY A CA 935 C C . GLY A 114 ? 0.6020 0.6004 0.5342 0.0508 0.0043 -0.0730 168 GLY A C 936 O O . GLY A 114 ? 0.5842 0.5847 0.5234 0.0488 0.0045 -0.0734 168 GLY A O 937 N N . MET A 115 ? 0.6365 0.6323 0.5582 0.0559 0.0053 -0.0741 169 MET A N 938 C CA . MET A 115 ? 0.6562 0.6522 0.5739 0.0594 0.0079 -0.0751 169 MET A CA 939 C C . MET A 115 ? 0.6666 0.6624 0.5747 0.0629 0.0134 -0.0726 169 MET A C 940 O O . MET A 115 ? 0.6848 0.6772 0.5832 0.0685 0.0131 -0.0747 169 MET A O 941 C CB . MET A 115 ? 0.6777 0.6696 0.5921 0.0635 0.0024 -0.0802 169 MET A CB 942 C CG . MET A 115 ? 0.7254 0.7170 0.6496 0.0605 -0.0030 -0.0827 169 MET A CG 943 S SD . MET A 115 ? 0.8754 0.8623 0.7959 0.0657 -0.0089 -0.0887 169 MET A SD 944 C CE . MET A 115 ? 0.8424 0.8268 0.7719 0.0630 -0.0167 -0.0914 169 MET A CE 945 N N . PRO A 116 ? 0.6579 0.6571 0.5685 0.0599 0.0185 -0.0681 170 PRO A N 946 C CA . PRO A 116 ? 0.6720 0.6711 0.5744 0.0631 0.0244 -0.0653 170 PRO A CA 947 C C . PRO A 116 ? 0.6902 0.6906 0.5902 0.0664 0.0289 -0.0652 170 PRO A C 948 O O . PRO A 116 ? 0.6763 0.6804 0.5846 0.0638 0.0301 -0.0651 170 PRO A O 949 C CB . PRO A 116 ? 0.6635 0.6665 0.5721 0.0582 0.0284 -0.0607 170 PRO A CB 950 C CG . PRO A 116 ? 0.6425 0.6488 0.5631 0.0528 0.0259 -0.0610 170 PRO A CG 951 C CD . PRO A 116 ? 0.6405 0.6441 0.5621 0.0537 0.0196 -0.0655 170 PRO A CD 952 N N . GLU A 117 ? 0.7116 0.7088 0.6000 0.0723 0.0313 -0.0654 171 GLU A N 953 C CA . GLU A 117 ? 0.7251 0.7229 0.6094 0.0764 0.0363 -0.0649 171 GLU A CA 954 C C . GLU A 117 ? 0.7350 0.7341 0.6156 0.0775 0.0440 -0.0600 171 GLU A C 955 O O . GLU A 117 ? 0.7501 0.7463 0.6237 0.0789 0.0442 -0.0586 171 GLU A O 956 C CB . GLU A 117 ? 0.7385 0.7307 0.6109 0.0834 0.0332 -0.0689 171 GLU A CB 957 C CG . GLU A 117 ? 0.7372 0.7271 0.6120 0.0836 0.0254 -0.0743 171 GLU A CG 958 C CD . GLU A 117 ? 0.7549 0.7387 0.6171 0.0911 0.0221 -0.0784 171 GLU A CD 959 O OE1 . GLU A 117 ? 0.7479 0.7277 0.6088 0.0921 0.0145 -0.0826 171 GLU A OE1 960 O OE2 . GLU A 117 ? 0.7641 0.7469 0.6179 0.0963 0.0270 -0.0775 171 GLU A OE2 961 N N . GLY A 118 ? 0.7344 0.7378 0.6199 0.0770 0.0503 -0.0573 172 GLY A N 962 C CA . GLY A 118 ? 0.7430 0.7480 0.6272 0.0775 0.0579 -0.0522 172 GLY A CA 963 C C . GLY A 118 ? 0.7444 0.7544 0.6361 0.0767 0.0645 -0.0496 172 GLY A C 964 O O . GLY A 118 ? 0.7366 0.7483 0.6325 0.0769 0.0633 -0.0521 172 GLY A O 965 N N . ASP A 119 ? 0.7485 0.7609 0.6426 0.0758 0.0712 -0.0447 173 ASP A N 966 C CA . ASP A 119 ? 0.7521 0.7693 0.6542 0.0751 0.0781 -0.0417 173 ASP A CA 967 C C . ASP A 119 ? 0.7333 0.7558 0.6500 0.0681 0.0786 -0.0393 173 ASP A C 968 O O . ASP A 119 ? 0.7255 0.7478 0.6439 0.0648 0.0769 -0.0377 173 ASP A O 969 C CB . ASP A 119 ? 0.7738 0.7896 0.6684 0.0799 0.0862 -0.0376 173 ASP A CB 970 C CG . ASP A 119 ? 0.8053 0.8151 0.6838 0.0877 0.0859 -0.0399 173 ASP A CG 971 O OD1 . ASP A 119 ? 0.8496 0.8590 0.7262 0.0906 0.0842 -0.0433 173 ASP A OD1 972 O OD2 . ASP A 119 ? 0.8251 0.8304 0.6925 0.0912 0.0871 -0.0384 173 ASP A OD2 973 N N . LEU A 120 ? 0.7133 0.7404 0.6404 0.0662 0.0806 -0.0391 174 LEU A N 974 C CA . LEU A 120 ? 0.6947 0.7266 0.6359 0.0600 0.0800 -0.0377 174 LEU A CA 975 C C . LEU A 120 ? 0.6937 0.7286 0.6411 0.0584 0.0866 -0.0325 174 LEU A C 976 O O . LEU A 120 ? 0.7136 0.7488 0.6585 0.0620 0.0934 -0.0298 174 LEU A O 977 C CB . LEU A 120 ? 0.6882 0.7235 0.6377 0.0592 0.0792 -0.0400 174 LEU A CB 978 C CG A LEU A 120 ? 0.6619 0.7001 0.6227 0.0538 0.0744 -0.0416 174 LEU A CG 979 C CG B LEU A 120 ? 0.6750 0.7091 0.6253 0.0577 0.0716 -0.0447 174 LEU A CG 980 C CD1 A LEU A 120 ? 0.6408 0.6758 0.5978 0.0522 0.0669 -0.0448 174 LEU A CD1 981 C CD1 B LEU A 120 ? 0.6470 0.6844 0.6050 0.0575 0.0719 -0.0464 174 LEU A CD1 982 C CD2 A LEU A 120 ? 0.6346 0.6755 0.6013 0.0546 0.0748 -0.0436 174 LEU A CD2 983 C CD2 B LEU A 120 ? 0.6473 0.6818 0.6033 0.0523 0.0667 -0.0448 174 LEU A CD2 984 N N . VAL A 121 ? 0.6821 0.7189 0.6375 0.0532 0.0847 -0.0311 175 VAL A N 985 C CA . VAL A 121 ? 0.6704 0.7111 0.6361 0.0505 0.0899 -0.0267 175 VAL A CA 986 C C . VAL A 121 ? 0.6569 0.7015 0.6359 0.0452 0.0862 -0.0279 175 VAL A C 987 O O . VAL A 121 ? 0.6539 0.6974 0.6326 0.0430 0.0796 -0.0310 175 VAL A O 988 C CB . VAL A 121 ? 0.6764 0.7151 0.6385 0.0495 0.0912 -0.0235 175 VAL A CB 989 C CG1 . VAL A 121 ? 0.6620 0.7047 0.6368 0.0457 0.0952 -0.0194 175 VAL A CG1 990 C CG2 . VAL A 121 ? 0.6977 0.7322 0.6463 0.0551 0.0953 -0.0219 175 VAL A CG2 991 N N . TYR A 122 ? 0.6320 0.6810 0.6228 0.0436 0.0904 -0.0255 176 TYR A N 992 C CA . TYR A 122 ? 0.6088 0.6614 0.6122 0.0394 0.0872 -0.0268 176 TYR A CA 993 C C . TYR A 122 ? 0.6072 0.6615 0.6189 0.0355 0.0879 -0.0237 176 TYR A C 994 O O . TYR A 122 ? 0.6023 0.6584 0.6189 0.0358 0.0939 -0.0198 176 TYR A O 995 C CB . TYR A 122 ? 0.6072 0.6635 0.6186 0.0407 0.0902 -0.0274 176 TYR A CB 996 C CG . TYR A 122 ? 0.5887 0.6489 0.6148 0.0365 0.0880 -0.0278 176 TYR A CG 997 C CD1 . TYR A 122 ? 0.5547 0.6145 0.5826 0.0341 0.0810 -0.0313 176 TYR A CD1 998 C CD2 . TYR A 122 ? 0.5630 0.6272 0.6013 0.0351 0.0926 -0.0246 176 TYR A CD2 999 C CE1 . TYR A 122 ? 0.5506 0.6134 0.5910 0.0308 0.0786 -0.0317 176 TYR A CE1 1000 C CE2 . TYR A 122 ? 0.5433 0.6106 0.5949 0.0316 0.0899 -0.0253 176 TYR A CE2 1001 C CZ . TYR A 122 ? 0.5345 0.6010 0.5865 0.0296 0.0827 -0.0290 176 TYR A CZ 1002 O OH . TYR A 122 ? 0.5158 0.5848 0.5799 0.0267 0.0797 -0.0298 176 TYR A OH 1003 N N . VAL A 123 ? 0.5775 0.6311 0.5909 0.0320 0.0819 -0.0253 177 VAL A N 1004 C CA . VAL A 123 ? 0.5751 0.6290 0.5932 0.0287 0.0814 -0.0228 177 VAL A CA 1005 C C . VAL A 123 ? 0.5616 0.6188 0.5931 0.0250 0.0788 -0.0233 177 VAL A C 1006 O O . VAL A 123 ? 0.5530 0.6100 0.5882 0.0219 0.0763 -0.0224 177 VAL A O 1007 C CB . VAL A 123 ? 0.5740 0.6238 0.5820 0.0282 0.0774 -0.0234 177 VAL A CB 1008 C CG1 . VAL A 123 ? 0.5806 0.6270 0.5758 0.0324 0.0803 -0.0227 177 VAL A CG1 1009 C CG2 . VAL A 123 ? 0.5587 0.6069 0.5644 0.0270 0.0704 -0.0275 177 VAL A CG2 1010 N N . ASN A 124 ? 0.5613 0.6214 0.6001 0.0255 0.0795 -0.0247 178 ASN A N 1011 C CA . ASN A 124 ? 0.5579 0.6208 0.6093 0.0225 0.0765 -0.0256 178 ASN A CA 1012 C C . ASN A 124 ? 0.5495 0.6100 0.5979 0.0202 0.0692 -0.0283 178 ASN A C 1013 O O . ASN A 124 ? 0.5451 0.6033 0.5857 0.0214 0.0662 -0.0309 178 ASN A O 1014 C CB . ASN A 124 ? 0.5548 0.6203 0.6172 0.0205 0.0800 -0.0220 178 ASN A CB 1015 C CG . ASN A 124 ? 0.5518 0.6208 0.6287 0.0184 0.0780 -0.0231 178 ASN A CG 1016 O OD1 . ASN A 124 ? 0.5304 0.6004 0.6097 0.0192 0.0760 -0.0259 178 ASN A OD1 1017 N ND2 . ASN A 124 ? 0.5586 0.6291 0.6455 0.0159 0.0783 -0.0210 178 ASN A ND2 1018 N N . TYR A 125 ? 0.5550 0.6159 0.6098 0.0172 0.0666 -0.0275 179 TYR A N 1019 C CA . TYR A 125 ? 0.5540 0.6124 0.6058 0.0153 0.0603 -0.0295 179 TYR A CA 1020 C C . TYR A 125 ? 0.5646 0.6197 0.6067 0.0149 0.0591 -0.0287 179 TYR A C 1021 O O . TYR A 125 ? 0.5548 0.6078 0.5946 0.0134 0.0543 -0.0300 179 TYR A O 1022 C CB . TYR A 125 ? 0.5468 0.6066 0.6091 0.0126 0.0574 -0.0294 179 TYR A CB 1023 C CG . TYR A 125 ? 0.5552 0.6179 0.6276 0.0128 0.0569 -0.0310 179 TYR A CG 1024 C CD1 . TYR A 125 ? 0.5292 0.5910 0.6002 0.0135 0.0530 -0.0342 179 TYR A CD1 1025 C CD2 . TYR A 125 ? 0.5393 0.6054 0.6232 0.0124 0.0604 -0.0291 179 TYR A CD2 1026 C CE1 . TYR A 125 ? 0.5380 0.6022 0.6181 0.0138 0.0523 -0.0358 179 TYR A CE1 1027 C CE2 . TYR A 125 ? 0.5357 0.6045 0.6297 0.0126 0.0597 -0.0307 179 TYR A CE2 1028 C CZ . TYR A 125 ? 0.5512 0.6190 0.6429 0.0134 0.0555 -0.0341 179 TYR A CZ 1029 O OH . TYR A 125 ? 0.5442 0.6144 0.6454 0.0138 0.0544 -0.0359 179 TYR A OH 1030 N N . ALA A 126 ? 0.5729 0.6273 0.6092 0.0165 0.0634 -0.0264 180 ALA A N 1031 C CA . ALA A 126 ? 0.5752 0.6265 0.6028 0.0163 0.0627 -0.0253 180 ALA A CA 1032 C C . ALA A 126 ? 0.5743 0.6254 0.6063 0.0131 0.0602 -0.0240 180 ALA A C 1033 O O . ALA A 126 ? 0.5654 0.6138 0.5912 0.0124 0.0571 -0.0244 180 ALA A O 1034 C CB . ALA A 126 ? 0.5782 0.6263 0.5956 0.0177 0.0591 -0.0281 180 ALA A CB 1035 N N . ARG A 127 ? 0.5636 0.6175 0.6068 0.0115 0.0613 -0.0226 181 ARG A N 1036 C CA . ARG A 127 ? 0.5642 0.6178 0.6119 0.0088 0.0594 -0.0211 181 ARG A CA 1037 C C . ARG A 127 ? 0.5716 0.6241 0.6153 0.0090 0.0632 -0.0177 181 ARG A C 1038 O O . ARG A 127 ? 0.5705 0.6229 0.6094 0.0113 0.0679 -0.0162 181 ARG A O 1039 C CB . ARG A 127 ? 0.5586 0.6152 0.6198 0.0073 0.0591 -0.0209 181 ARG A CB 1040 C CG . ARG A 127 ? 0.5512 0.6083 0.6163 0.0070 0.0545 -0.0242 181 ARG A CG 1041 C CD . ARG A 127 ? 0.5664 0.6267 0.6450 0.0063 0.0550 -0.0242 181 ARG A CD 1042 N NE . ARG A 127 ? 0.5547 0.6178 0.6375 0.0077 0.0611 -0.0224 181 ARG A NE 1043 C CZ . ARG A 127 ? 0.5399 0.6064 0.6355 0.0073 0.0628 -0.0219 181 ARG A CZ 1044 N NH1 . ARG A 127 ? 0.5181 0.5854 0.6233 0.0057 0.0585 -0.0233 181 ARG A NH1 1045 N NH2 . ARG A 127 ? 0.5555 0.6243 0.6541 0.0088 0.0690 -0.0199 181 ARG A NH2 1046 N N . THR A 128 ? 0.5735 0.6249 0.6184 0.0069 0.0609 -0.0166 182 THR A N 1047 C CA . THR A 128 ? 0.5786 0.6291 0.6213 0.0067 0.0643 -0.0132 182 THR A CA 1048 C C . THR A 128 ? 0.5825 0.6358 0.6335 0.0073 0.0704 -0.0102 182 THR A C 1049 O O . THR A 128 ? 0.5822 0.6348 0.6278 0.0094 0.0756 -0.0079 182 THR A O 1050 C CB . THR A 128 ? 0.5847 0.6339 0.6296 0.0041 0.0606 -0.0126 182 THR A CB 1051 O OG1 . THR A 128 ? 0.5864 0.6327 0.6225 0.0040 0.0560 -0.0148 182 THR A OG1 1052 C CG2 . THR A 128 ? 0.5678 0.6163 0.6123 0.0038 0.0645 -0.0088 182 THR A CG2 1053 N N . GLU A 129 ? 0.5775 0.6338 0.6415 0.0057 0.0698 -0.0105 183 GLU A N 1054 C CA . GLU A 129 ? 0.6052 0.6645 0.6794 0.0060 0.0755 -0.0077 183 GLU A CA 1055 C C . GLU A 129 ? 0.6049 0.6651 0.6749 0.0092 0.0807 -0.0073 183 GLU A C 1056 O O . GLU A 129 ? 0.6056 0.6666 0.6774 0.0104 0.0871 -0.0039 183 GLU A O 1057 C CB . GLU A 129 ? 0.5995 0.6619 0.6890 0.0039 0.0731 -0.0088 183 GLU A CB 1058 C CG . GLU A 129 ? 0.6323 0.6962 0.7243 0.0047 0.0703 -0.0124 183 GLU A CG 1059 C CD . GLU A 129 ? 0.6783 0.7435 0.7819 0.0027 0.0651 -0.0145 183 GLU A CD 1060 O OE1 . GLU A 129 ? 0.6640 0.7269 0.7637 0.0016 0.0593 -0.0165 183 GLU A OE1 1061 O OE2 . GLU A 129 ? 0.7066 0.7750 0.8231 0.0024 0.0666 -0.0142 183 GLU A OE2 1062 N N . ASP A 130 ? 0.6131 0.6728 0.6774 0.0106 0.0781 -0.0108 184 ASP A N 1063 C CA . ASP A 130 ? 0.6180 0.6782 0.6774 0.0139 0.0825 -0.0109 184 ASP A CA 1064 C C . ASP A 130 ? 0.6262 0.6833 0.6725 0.0167 0.0863 -0.0089 184 ASP A C 1065 O O . ASP A 130 ? 0.6372 0.6948 0.6817 0.0195 0.0923 -0.0068 184 ASP A O 1066 C CB . ASP A 130 ? 0.6137 0.6737 0.6694 0.0149 0.0783 -0.0152 184 ASP A CB 1067 C CG . ASP A 130 ? 0.6020 0.6647 0.6695 0.0129 0.0745 -0.0174 184 ASP A CG 1068 O OD1 . ASP A 130 ? 0.5698 0.6357 0.6495 0.0123 0.0772 -0.0161 184 ASP A OD1 1069 O OD2 . ASP A 130 ? 0.5299 0.5910 0.5943 0.0121 0.0687 -0.0206 184 ASP A OD2 1070 N N . PHE A 131 ? 0.6337 0.6874 0.6707 0.0162 0.0826 -0.0095 185 PHE A N 1071 C CA . PHE A 131 ? 0.6435 0.6937 0.6676 0.0189 0.0853 -0.0080 185 PHE A CA 1072 C C . PHE A 131 ? 0.6587 0.7087 0.6846 0.0191 0.0910 -0.0032 185 PHE A C 1073 O O . PHE A 131 ? 0.6545 0.7025 0.6719 0.0225 0.0959 -0.0011 185 PHE A O 1074 C CB . PHE A 131 ? 0.6337 0.6804 0.6480 0.0184 0.0794 -0.0104 185 PHE A CB 1075 C CG . PHE A 131 ? 0.6077 0.6529 0.6147 0.0202 0.0758 -0.0144 185 PHE A CG 1076 C CD1 . PHE A 131 ? 0.5800 0.6260 0.5909 0.0180 0.0701 -0.0177 185 PHE A CD1 1077 C CD2 . PHE A 131 ? 0.5760 0.6189 0.5723 0.0243 0.0781 -0.0149 185 PHE A CD2 1078 C CE1 . PHE A 131 ? 0.5551 0.5997 0.5600 0.0197 0.0670 -0.0212 185 PHE A CE1 1079 C CE2 . PHE A 131 ? 0.5600 0.6015 0.5503 0.0260 0.0745 -0.0187 185 PHE A CE2 1080 C CZ . PHE A 131 ? 0.5223 0.5647 0.5173 0.0235 0.0690 -0.0218 185 PHE A CZ 1081 N N . PHE A 132 ? 0.6651 0.7169 0.7018 0.0156 0.0900 -0.0016 186 PHE A N 1082 C CA . PHE A 132 ? 0.6813 0.7336 0.7237 0.0150 0.0954 0.0030 186 PHE A CA 1083 C C . PHE A 132 ? 0.7003 0.7551 0.7484 0.0173 0.1029 0.0057 186 PHE A C 1084 O O . PHE A 132 ? 0.7052 0.7586 0.7492 0.0196 0.1093 0.0096 186 PHE A O 1085 C CB . PHE A 132 ? 0.6675 0.7220 0.7237 0.0108 0.0925 0.0035 186 PHE A CB 1086 C CG . PHE A 132 ? 0.6536 0.7054 0.7054 0.0086 0.0871 0.0029 186 PHE A CG 1087 C CD1 . PHE A 132 ? 0.6477 0.6955 0.6853 0.0102 0.0864 0.0029 186 PHE A CD1 1088 C CD2 . PHE A 132 ? 0.6371 0.6903 0.6996 0.0051 0.0829 0.0022 186 PHE A CD2 1089 C CE1 . PHE A 132 ? 0.6450 0.6906 0.6795 0.0081 0.0817 0.0024 186 PHE A CE1 1090 C CE2 . PHE A 132 ? 0.6055 0.6563 0.6643 0.0033 0.0782 0.0017 186 PHE A CE2 1091 C CZ . PHE A 132 ? 0.6091 0.6563 0.6542 0.0046 0.0777 0.0018 186 PHE A CZ 1092 N N . LYS A 133 ? 0.7117 0.7700 0.7692 0.0168 0.1023 0.0037 187 LYS A N 1093 C CA . LYS A 133 ? 0.7302 0.7914 0.7944 0.0189 0.1091 0.0057 187 LYS A CA 1094 C C . LYS A 133 ? 0.7440 0.8029 0.7947 0.0238 0.1134 0.0059 187 LYS A C 1095 O O . LYS A 133 ? 0.7552 0.8148 0.8072 0.0264 0.1211 0.0095 187 LYS A O 1096 C CB . LYS A 133 ? 0.7277 0.7929 0.8048 0.0171 0.1061 0.0028 187 LYS A CB 1097 C CG . LYS A 133 ? 0.7639 0.8325 0.8485 0.0194 0.1125 0.0042 187 LYS A CG 1098 C CD . LYS A 133 ? 0.7963 0.8694 0.9003 0.0165 0.1116 0.0039 187 LYS A CD 1099 C CE . LYS A 133 ? 0.8200 0.8947 0.9360 0.0149 0.1166 0.0088 187 LYS A CE 1100 N NZ . LYS A 133 ? 0.8273 0.9058 0.9627 0.0116 0.1140 0.0080 187 LYS A NZ 1101 N N . LEU A 134 ? 0.7478 0.8039 0.7859 0.0253 0.1086 0.0021 188 LEU A N 1102 C CA . LEU A 134 ? 0.7624 0.8155 0.7862 0.0302 0.1115 0.0018 188 LEU A CA 1103 C C . LEU A 134 ? 0.7784 0.8278 0.7925 0.0328 0.1163 0.0057 188 LEU A C 1104 O O . LEU A 134 ? 0.7821 0.8307 0.7917 0.0369 0.1232 0.0084 188 LEU A O 1105 C CB . LEU A 134 ? 0.7616 0.8120 0.7747 0.0308 0.1044 -0.0031 188 LEU A CB 1106 C CG . LEU A 134 ? 0.7690 0.8214 0.7848 0.0312 0.1014 -0.0071 188 LEU A CG 1107 C CD1 . LEU A 134 ? 0.7800 0.8300 0.7889 0.0300 0.0934 -0.0114 188 LEU A CD1 1108 C CD2 . LEU A 134 ? 0.7722 0.8239 0.7811 0.0362 0.1065 -0.0069 188 LEU A CD2 1109 N N . GLU A 135 ? 0.7769 0.8239 0.7874 0.0307 0.1127 0.0060 189 GLU A N 1110 C CA . GLU A 135 ? 0.8023 0.8449 0.8010 0.0334 0.1159 0.0090 189 GLU A CA 1111 C C . GLU A 135 ? 0.8064 0.8500 0.8128 0.0328 0.1230 0.0148 189 GLU A C 1112 O O . GLU A 135 ? 0.8191 0.8602 0.8181 0.0369 0.1298 0.0184 189 GLU A O 1113 C CB . GLU A 135 ? 0.8036 0.8428 0.7937 0.0319 0.1090 0.0067 189 GLU A CB 1114 C CG . GLU A 135 ? 0.8474 0.8812 0.8224 0.0357 0.1112 0.0086 189 GLU A CG 1115 C CD . GLU A 135 ? 0.8806 0.9121 0.8534 0.0330 0.1071 0.0091 189 GLU A CD 1116 O OE1 . GLU A 135 ? 0.8813 0.9115 0.8498 0.0317 0.0999 0.0051 189 GLU A OE1 1117 O OE2 . GLU A 135 ? 0.9026 0.9337 0.8783 0.0324 0.1112 0.0134 189 GLU A OE2 1118 N N . ARG A 136 ? 0.7984 0.8453 0.8196 0.0280 0.1213 0.0157 190 ARG A N 1119 C CA . ARG A 136 ? 0.8015 0.8494 0.8322 0.0265 0.1268 0.0209 190 ARG A CA 1120 C C . ARG A 136 ? 0.8144 0.8661 0.8573 0.0275 0.1347 0.0244 190 ARG A C 1121 O O . ARG A 136 ? 0.8232 0.8742 0.8683 0.0287 0.1420 0.0297 190 ARG A O 1122 C CB . ARG A 136 ? 0.7843 0.8339 0.8259 0.0211 0.1212 0.0202 190 ARG A CB 1123 C CG . ARG A 136 ? 0.7483 0.7943 0.7794 0.0200 0.1141 0.0176 190 ARG A CG 1124 C CD . ARG A 136 ? 0.6867 0.7345 0.7288 0.0150 0.1085 0.0165 190 ARG A CD 1125 N NE . ARG A 136 ? 0.6690 0.7132 0.7011 0.0142 0.1029 0.0149 190 ARG A NE 1126 C CZ . ARG A 136 ? 0.6209 0.6652 0.6586 0.0105 0.0979 0.0142 190 ARG A CZ 1127 N NH1 . ARG A 136 ? 0.5673 0.6150 0.6206 0.0074 0.0973 0.0148 190 ARG A NH1 1128 N NH2 . ARG A 136 ? 0.5499 0.5909 0.5777 0.0102 0.0934 0.0128 190 ARG A NH2 1129 N N . ASP A 137 ? 0.8202 0.8757 0.8714 0.0269 0.1334 0.0216 191 ASP A N 1130 C CA . ASP A 137 ? 0.8318 0.8914 0.8961 0.0276 0.1404 0.0244 191 ASP A CA 1131 C C . ASP A 137 ? 0.8431 0.9018 0.8977 0.0331 0.1459 0.0246 191 ASP A C 1132 O O . ASP A 137 ? 0.8504 0.9100 0.9092 0.0356 0.1546 0.0290 191 ASP A O 1133 C CB . ASP A 137 ? 0.8255 0.8901 0.9065 0.0238 0.1358 0.0213 191 ASP A CB 1134 C CG . ASP A 137 ? 0.8395 0.9054 0.9329 0.0188 0.1312 0.0214 191 ASP A CG 1135 O OD1 . ASP A 137 ? 0.8632 0.9295 0.9646 0.0177 0.1358 0.0260 191 ASP A OD1 1136 O OD2 . ASP A 137 ? 0.8390 0.9056 0.9346 0.0161 0.1230 0.0169 191 ASP A OD2 1137 N N . MET A 138 ? 0.8433 0.8999 0.8854 0.0351 0.1409 0.0199 192 MET A N 1138 C CA . MET A 138 ? 0.8549 0.9108 0.8883 0.0401 0.1446 0.0190 192 MET A CA 1139 C C . MET A 138 ? 0.8637 0.9135 0.8764 0.0453 0.1461 0.0194 192 MET A C 1140 O O . MET A 138 ? 0.8685 0.9168 0.8718 0.0503 0.1493 0.0188 192 MET A O 1141 C CB . MET A 138 ? 0.8512 0.9090 0.8855 0.0393 0.1378 0.0131 192 MET A CB 1142 C CG . MET A 138 ? 0.8516 0.9149 0.9047 0.0352 0.1357 0.0117 192 MET A CG 1143 S SD . MET A 138 ? 0.8816 0.9457 0.9321 0.0349 0.1276 0.0048 192 MET A SD 1144 C CE . MET A 138 ? 0.8603 0.9241 0.9029 0.0411 0.1340 0.0050 192 MET A CE 1145 N N . LYS A 139 ? 0.8627 0.9089 0.8681 0.0442 0.1433 0.0202 193 LYS A N 1146 C CA . LYS A 139 ? 0.8746 0.9147 0.8604 0.0489 0.1436 0.0203 193 LYS A CA 1147 C C . LYS A 139 ? 0.8734 0.9111 0.8464 0.0525 0.1392 0.0151 193 LYS A C 1148 O O . LYS A 139 ? 0.8797 0.9135 0.8389 0.0585 0.1429 0.0156 193 LYS A O 1149 C CB . LYS A 139 ? 0.8925 0.9303 0.8737 0.0536 0.1540 0.0263 193 LYS A CB 1150 C CG . LYS A 139 ? 0.9082 0.9439 0.8897 0.0522 0.1567 0.0310 193 LYS A CG 1151 C CD . LYS A 139 ? 0.9037 0.9444 0.9054 0.0458 0.1562 0.0329 193 LYS A CD 1152 C CE . LYS A 139 ? 0.9151 0.9537 0.9184 0.0457 0.1620 0.0389 193 LYS A CE 1153 N NZ . LYS A 139 ? 0.9026 0.9449 0.9232 0.0393 0.1594 0.0400 193 LYS A NZ 1154 N N . ILE A 140 ? 0.8576 0.8975 0.8354 0.0491 0.1315 0.0101 194 ILE A N 1155 C CA . ILE A 140 ? 0.8544 0.8923 0.8219 0.0518 0.1264 0.0049 194 ILE A CA 1156 C C . ILE A 140 ? 0.8468 0.8811 0.8055 0.0503 0.1182 0.0016 194 ILE A C 1157 O O . ILE A 140 ? 0.8385 0.8741 0.8043 0.0455 0.1143 0.0016 194 ILE A O 1158 C CB . ILE A 140 ? 0.8508 0.8934 0.8290 0.0500 0.1243 0.0017 194 ILE A CB 1159 C CG1 . ILE A 140 ? 0.8536 0.8983 0.8354 0.0535 0.1327 0.0044 194 ILE A CG1 1160 C CG2 . ILE A 140 ? 0.8538 0.8942 0.8232 0.0511 0.1169 -0.0040 194 ILE A CG2 1161 C CD1 . ILE A 140 ? 0.8318 0.8816 0.8260 0.0518 0.1318 0.0021 194 ILE A CD1 1162 N N . ASN A 141 ? 0.8474 0.8769 0.7907 0.0549 0.1158 -0.0010 195 ASN A N 1163 C CA . ASN A 141 ? 0.8454 0.8708 0.7791 0.0545 0.1089 -0.0038 195 ASN A CA 1164 C C . ASN A 141 ? 0.8329 0.8578 0.7639 0.0543 0.1012 -0.0097 195 ASN A C 1165 O O . ASN A 141 ? 0.8380 0.8610 0.7612 0.0587 0.1013 -0.0121 195 ASN A O 1166 C CB . ASN A 141 ? 0.8590 0.8783 0.7766 0.0601 0.1117 -0.0020 195 ASN A CB 1167 C CG . ASN A 141 ? 0.8743 0.8899 0.7848 0.0588 0.1056 -0.0034 195 ASN A CG 1168 O OD1 . ASN A 141 ? 0.8624 0.8789 0.7765 0.0551 0.0983 -0.0071 195 ASN A OD1 1169 N ND2 . ASN A 141 ? 0.8854 0.8965 0.7857 0.0621 0.1088 -0.0004 195 ASN A ND2 1170 N N . CYS A 142 ? 0.8097 0.8360 0.7470 0.0493 0.0947 -0.0120 196 CYS A N 1171 C CA . CYS A 142 ? 0.7940 0.8202 0.7311 0.0484 0.0877 -0.0172 196 CYS A CA 1172 C C . CYS A 142 ? 0.7910 0.8119 0.7150 0.0512 0.0822 -0.0205 196 CYS A C 1173 O O . CYS A 142 ? 0.7880 0.8082 0.7104 0.0516 0.0770 -0.0248 196 CYS A O 1174 C CB . CYS A 142 ? 0.7823 0.8123 0.7321 0.0422 0.0834 -0.0181 196 CYS A CB 1175 S SG . CYS A 142 ? 0.7742 0.8104 0.7400 0.0394 0.0873 -0.0165 196 CYS A SG 1176 N N . SER A 143 ? 0.7850 0.8021 0.7000 0.0533 0.0834 -0.0186 197 SER A N 1177 C CA . SER A 143 ? 0.7775 0.7892 0.6804 0.0561 0.0780 -0.0217 197 SER A CA 1178 C C . SER A 143 ? 0.7750 0.7837 0.6688 0.0612 0.0758 -0.0257 197 SER A C 1179 O O . SER A 143 ? 0.7959 0.8034 0.6836 0.0660 0.0809 -0.0245 197 SER A O 1180 C CB . SER A 143 ? 0.7854 0.7932 0.6792 0.0585 0.0807 -0.0185 197 SER A CB 1181 O OG . SER A 143 ? 0.7809 0.7835 0.6635 0.0613 0.0751 -0.0217 197 SER A OG 1182 N N . GLY A 144 ? 0.7559 0.7634 0.6493 0.0603 0.0684 -0.0303 198 GLY A N 1183 C CA . GLY A 144 ? 0.7375 0.7421 0.6234 0.0647 0.0651 -0.0347 198 GLY A CA 1184 C C . GLY A 144 ? 0.7286 0.7367 0.6213 0.0645 0.0666 -0.0360 198 GLY A C 1185 O O . GLY A 144 ? 0.7248 0.7308 0.6123 0.0680 0.0640 -0.0397 198 GLY A O 1186 N N . LYS A 145 ? 0.7119 0.7254 0.6164 0.0604 0.0707 -0.0331 199 LYS A N 1187 C CA . LYS A 145 ? 0.7005 0.7179 0.6128 0.0598 0.0721 -0.0342 199 LYS A CA 1188 C C . LYS A 145 ? 0.6845 0.7039 0.6055 0.0552 0.0656 -0.0375 199 LYS A C 1189 O O . LYS A 145 ? 0.6726 0.6917 0.5963 0.0516 0.0615 -0.0377 199 LYS A O 1190 C CB . LYS A 145 ? 0.6953 0.7174 0.6170 0.0577 0.0792 -0.0297 199 LYS A CB 1191 C CG . LYS A 145 ? 0.7359 0.7563 0.6509 0.0616 0.0866 -0.0254 199 LYS A CG 1192 C CD . LYS A 145 ? 0.7636 0.7821 0.6700 0.0680 0.0903 -0.0261 199 LYS A CD 1193 C CE . LYS A 145 ? 0.8050 0.8204 0.7018 0.0728 0.0972 -0.0219 199 LYS A CE 1194 N NZ . LYS A 145 ? 0.8093 0.8178 0.6891 0.0788 0.0944 -0.0245 199 LYS A NZ 1195 N N . ILE A 146 ? 0.6721 0.6933 0.5970 0.0557 0.0648 -0.0399 200 ILE A N 1196 C CA . ILE A 146 ? 0.6524 0.6763 0.5874 0.0511 0.0603 -0.0420 200 ILE A CA 1197 C C . ILE A 146 ? 0.6403 0.6695 0.5870 0.0477 0.0645 -0.0391 200 ILE A C 1198 O O . ILE A 146 ? 0.6492 0.6804 0.5974 0.0499 0.0696 -0.0378 200 ILE A O 1199 C CB . ILE A 146 ? 0.6520 0.6747 0.5851 0.0534 0.0567 -0.0464 200 ILE A CB 1200 C CG1 . ILE A 146 ? 0.6503 0.6678 0.5737 0.0561 0.0512 -0.0497 200 ILE A CG1 1201 C CG2 . ILE A 146 ? 0.6448 0.6707 0.5890 0.0490 0.0535 -0.0478 200 ILE A CG2 1202 C CD1 . ILE A 146 ? 0.6323 0.6477 0.5530 0.0590 0.0474 -0.0542 200 ILE A CD1 1203 N N . VAL A 147 ? 0.6137 0.6450 0.5687 0.0428 0.0626 -0.0379 201 VAL A N 1204 C CA . VAL A 147 ? 0.6024 0.6384 0.5689 0.0399 0.0660 -0.0356 201 VAL A CA 1205 C C . VAL A 147 ? 0.5857 0.6240 0.5599 0.0380 0.0627 -0.0383 201 VAL A C 1206 O O . VAL A 147 ? 0.5769 0.6134 0.5500 0.0368 0.0571 -0.0411 201 VAL A O 1207 C CB . VAL A 147 ? 0.6116 0.6491 0.5839 0.0360 0.0667 -0.0324 201 VAL A CB 1208 C CG1 . VAL A 147 ? 0.6276 0.6629 0.5927 0.0380 0.0706 -0.0292 201 VAL A CG1 1209 C CG2 . VAL A 147 ? 0.5966 0.6331 0.5707 0.0325 0.0605 -0.0341 201 VAL A CG2 1210 N N . ILE A 148 ? 0.5642 0.6061 0.5460 0.0379 0.0662 -0.0374 202 ILE A N 1211 C CA . ILE A 148 ? 0.5347 0.5788 0.5246 0.0360 0.0633 -0.0396 202 ILE A CA 1212 C C . ILE A 148 ? 0.5239 0.5717 0.5251 0.0323 0.0647 -0.0373 202 ILE A C 1213 O O . ILE A 148 ? 0.5268 0.5769 0.5323 0.0326 0.0699 -0.0342 202 ILE A O 1214 C CB . ILE A 148 ? 0.5511 0.5960 0.5403 0.0393 0.0650 -0.0416 202 ILE A CB 1215 C CG1 . ILE A 148 ? 0.5373 0.5844 0.5351 0.0372 0.0618 -0.0438 202 ILE A CG1 1216 C CG2 . ILE A 148 ? 0.5400 0.5872 0.5305 0.0419 0.0724 -0.0387 202 ILE A CG2 1217 C CD1 . ILE A 148 ? 0.4998 0.5461 0.4945 0.0402 0.0607 -0.0471 202 ILE A CD1 1218 N N . ALA A 149 ? 0.4829 0.5308 0.4891 0.0291 0.0599 -0.0385 203 ALA A N 1219 C CA . ALA A 149 ? 0.4625 0.5131 0.4787 0.0259 0.0600 -0.0368 203 ALA A CA 1220 C C . ALA A 149 ? 0.4494 0.5012 0.4723 0.0245 0.0564 -0.0392 203 ALA A C 1221 O O . ALA A 149 ? 0.4390 0.4887 0.4580 0.0250 0.0526 -0.0419 203 ALA A O 1222 C CB . ALA A 149 ? 0.4603 0.5092 0.4748 0.0233 0.0579 -0.0353 203 ALA A CB 1223 N N . ARG A 150 ? 0.4451 0.5001 0.4783 0.0229 0.0575 -0.0382 204 ARG A N 1224 C CA . ARG A 150 ? 0.4361 0.4919 0.4757 0.0216 0.0537 -0.0403 204 ARG A CA 1225 C C . ARG A 150 ? 0.4235 0.4778 0.4646 0.0188 0.0495 -0.0401 204 ARG A C 1226 O O . ARG A 150 ? 0.4098 0.4643 0.4523 0.0172 0.0504 -0.0377 204 ARG A O 1227 C CB . ARG A 150 ? 0.4428 0.5024 0.4930 0.0218 0.0562 -0.0400 204 ARG A CB 1228 C CG . ARG A 150 ? 0.4567 0.5190 0.5146 0.0205 0.0597 -0.0369 204 ARG A CG 1229 C CD . ARG A 150 ? 0.5095 0.5755 0.5795 0.0204 0.0609 -0.0372 204 ARG A CD 1230 N NE . ARG A 150 ? 0.5429 0.6118 0.6212 0.0198 0.0657 -0.0340 204 ARG A NE 1231 C CZ . ARG A 150 ? 0.5541 0.6265 0.6453 0.0191 0.0667 -0.0337 204 ARG A CZ 1232 N NH1 . ARG A 150 ? 0.5377 0.6109 0.6341 0.0192 0.0631 -0.0367 204 ARG A NH1 1233 N NH2 . ARG A 150 ? 0.5422 0.6172 0.6417 0.0184 0.0713 -0.0305 204 ARG A NH2 1234 N N . TYR A 151 ? 0.3974 0.4501 0.4382 0.0184 0.0450 -0.0425 205 TYR A N 1235 C CA . TYR A 151 ? 0.3887 0.4399 0.4312 0.0163 0.0410 -0.0426 205 TYR A CA 1236 C C . TYR A 151 ? 0.4063 0.4599 0.4587 0.0149 0.0412 -0.0416 205 TYR A C 1237 O O . TYR A 151 ? 0.3916 0.4482 0.4510 0.0157 0.0434 -0.0417 205 TYR A O 1238 C CB . TYR A 151 ? 0.3702 0.4194 0.4113 0.0168 0.0371 -0.0452 205 TYR A CB 1239 C CG . TYR A 151 ? 0.3411 0.3868 0.3737 0.0172 0.0350 -0.0462 205 TYR A CG 1240 C CD1 . TYR A 151 ? 0.3014 0.3459 0.3310 0.0189 0.0341 -0.0485 205 TYR A CD1 1241 C CD2 . TYR A 151 ? 0.2955 0.3390 0.3240 0.0158 0.0337 -0.0450 205 TYR A CD2 1242 C CE1 . TYR A 151 ? 0.2804 0.3217 0.3038 0.0192 0.0317 -0.0495 205 TYR A CE1 1243 C CE2 . TYR A 151 ? 0.3479 0.3884 0.3703 0.0161 0.0315 -0.0460 205 TYR A CE2 1244 C CZ . TYR A 151 ? 0.3378 0.3771 0.3580 0.0177 0.0305 -0.0482 205 TYR A CZ 1245 O OH . TYR A 151 ? 0.2869 0.3231 0.3023 0.0178 0.0281 -0.0491 205 TYR A OH 1246 N N . GLY A 152 ? 0.3991 0.4515 0.4525 0.0131 0.0387 -0.0407 206 GLY A N 1247 C CA . GLY A 152 ? 0.4225 0.4763 0.4851 0.0119 0.0371 -0.0404 206 GLY A CA 1248 C C . GLY A 152 ? 0.4303 0.4847 0.4951 0.0102 0.0385 -0.0378 206 GLY A C 1249 O O . GLY A 152 ? 0.4205 0.4746 0.4802 0.0102 0.0416 -0.0359 206 GLY A O 1250 N N . LYS A 153 ? 0.4424 0.4971 0.5144 0.0091 0.0360 -0.0378 207 LYS A N 1251 C CA . LYS A 153 ? 0.4646 0.5202 0.5413 0.0074 0.0370 -0.0354 207 LYS A CA 1252 C C . LYS A 153 ? 0.4626 0.5151 0.5321 0.0064 0.0349 -0.0346 207 LYS A C 1253 O O . LYS A 153 ? 0.4875 0.5391 0.5605 0.0053 0.0321 -0.0343 207 LYS A O 1254 C CB . LYS A 153 ? 0.4653 0.5236 0.5445 0.0074 0.0429 -0.0327 207 LYS A CB 1255 C CG . LYS A 153 ? 0.4978 0.5598 0.5866 0.0083 0.0459 -0.0330 207 LYS A CG 1256 C CD . LYS A 153 ? 0.5470 0.6108 0.6486 0.0072 0.0437 -0.0334 207 LYS A CD 1257 C CE . LYS A 153 ? 0.5742 0.6418 0.6858 0.0082 0.0464 -0.0338 207 LYS A CE 1258 N NZ . LYS A 153 ? 0.5964 0.6647 0.7189 0.0077 0.0419 -0.0358 207 LYS A NZ 1259 N N . VAL A 154 ? 0.4496 0.5003 0.5092 0.0069 0.0359 -0.0343 208 VAL A N 1260 C CA . VAL A 154 ? 0.4280 0.4759 0.4807 0.0060 0.0342 -0.0336 208 VAL A CA 1261 C C . VAL A 154 ? 0.4166 0.4619 0.4606 0.0070 0.0327 -0.0351 208 VAL A C 1262 O O . VAL A 154 ? 0.3839 0.4297 0.4260 0.0084 0.0337 -0.0364 208 VAL A O 1263 C CB . VAL A 154 ? 0.4303 0.4786 0.4806 0.0053 0.0377 -0.0308 208 VAL A CB 1264 C CG1 . VAL A 154 ? 0.4765 0.5274 0.5365 0.0042 0.0397 -0.0289 208 VAL A CG1 1265 C CG2 . VAL A 154 ? 0.4133 0.4619 0.4577 0.0068 0.0414 -0.0305 208 VAL A CG2 1266 N N . PHE A 155 ? 0.3861 0.4288 0.4251 0.0063 0.0304 -0.0347 209 PHE A N 1267 C CA . PHE A 155 ? 0.3641 0.4042 0.3958 0.0069 0.0289 -0.0359 209 PHE A CA 1268 C C . PHE A 155 ? 0.3503 0.3906 0.3768 0.0080 0.0315 -0.0360 209 PHE A C 1269 O O . PHE A 155 ? 0.3555 0.3966 0.3803 0.0079 0.0343 -0.0343 209 PHE A O 1270 C CB . PHE A 155 ? 0.3574 0.3949 0.3854 0.0059 0.0267 -0.0350 209 PHE A CB 1271 C CG . PHE A 155 ? 0.3335 0.3684 0.3552 0.0064 0.0254 -0.0359 209 PHE A CG 1272 C CD1 . PHE A 155 ? 0.3070 0.3406 0.3287 0.0073 0.0235 -0.0376 209 PHE A CD1 1273 C CD2 . PHE A 155 ? 0.3726 0.4063 0.3890 0.0060 0.0258 -0.0350 209 PHE A CD2 1274 C CE1 . PHE A 155 ? 0.3409 0.3721 0.3581 0.0078 0.0224 -0.0383 209 PHE A CE1 1275 C CE2 . PHE A 155 ? 0.3875 0.4189 0.3996 0.0065 0.0244 -0.0360 209 PHE A CE2 1276 C CZ . PHE A 155 ? 0.3405 0.3707 0.3534 0.0073 0.0227 -0.0376 209 PHE A CZ 1277 N N . ARG A 156 ? 0.3321 0.3714 0.3559 0.0093 0.0307 -0.0379 210 ARG A N 1278 C CA . ARG A 156 ? 0.3263 0.3656 0.3451 0.0108 0.0327 -0.0385 210 ARG A CA 1279 C C . ARG A 156 ? 0.3436 0.3811 0.3559 0.0107 0.0330 -0.0375 210 ARG A C 1280 O O . ARG A 156 ? 0.3401 0.3777 0.3484 0.0122 0.0353 -0.0374 210 ARG A O 1281 C CB . ARG A 156 ? 0.3190 0.3573 0.3365 0.0122 0.0312 -0.0410 210 ARG A CB 1282 C CG . ARG A 156 ? 0.2859 0.3211 0.3003 0.0117 0.0279 -0.0418 210 ARG A CG 1283 C CD . ARG A 156 ? 0.2687 0.3027 0.2830 0.0130 0.0261 -0.0441 210 ARG A CD 1284 N NE . ARG A 156 ? 0.2713 0.3056 0.2904 0.0129 0.0248 -0.0447 210 ARG A NE 1285 C CZ . ARG A 156 ? 0.3288 0.3613 0.3490 0.0120 0.0226 -0.0441 210 ARG A CZ 1286 N NH1 . ARG A 156 ? 0.2848 0.3155 0.3022 0.0110 0.0217 -0.0429 210 ARG A NH1 1287 N NH2 . ARG A 156 ? 0.2916 0.3239 0.3153 0.0125 0.0213 -0.0449 210 ARG A NH2 1288 N N . GLY A 157 ? 0.3451 0.3806 0.3559 0.0094 0.0306 -0.0370 211 GLY A N 1289 C CA . GLY A 157 ? 0.3786 0.4125 0.3839 0.0093 0.0305 -0.0362 211 GLY A CA 1290 C C . GLY A 157 ? 0.3996 0.4347 0.4046 0.0089 0.0335 -0.0339 211 GLY A C 1291 O O . GLY A 157 ? 0.3949 0.4290 0.3943 0.0100 0.0347 -0.0334 211 GLY A O 1292 N N . ASN A 158 ? 0.4068 0.4438 0.4179 0.0077 0.0344 -0.0325 212 ASN A N 1293 C CA . ASN A 158 ? 0.4482 0.4867 0.4610 0.0073 0.0376 -0.0300 212 ASN A CA 1294 C C . ASN A 158 ? 0.4512 0.4909 0.4622 0.0093 0.0416 -0.0297 212 ASN A C 1295 O O . ASN A 158 ? 0.4701 0.5095 0.4775 0.0099 0.0443 -0.0279 212 ASN A O 1296 C CB . ASN A 158 ? 0.4491 0.4895 0.4703 0.0056 0.0373 -0.0289 212 ASN A CB 1297 C CG . ASN A 158 ? 0.5015 0.5401 0.5230 0.0039 0.0338 -0.0287 212 ASN A CG 1298 O OD1 . ASN A 158 ? 0.5382 0.5762 0.5621 0.0037 0.0308 -0.0300 212 ASN A OD1 1299 N ND2 . ASN A 158 ? 0.5344 0.5722 0.5536 0.0031 0.0343 -0.0268 212 ASN A ND2 1300 N N . LYS A 159 ? 0.4498 0.4907 0.4625 0.0106 0.0419 -0.0315 213 LYS A N 1301 C CA . LYS A 159 ? 0.4364 0.4780 0.4463 0.0131 0.0456 -0.0315 213 LYS A CA 1302 C C . LYS A 159 ? 0.4471 0.4859 0.4470 0.0151 0.0455 -0.0321 213 LYS A C 1303 O O . LYS A 159 ? 0.4500 0.4886 0.4458 0.0170 0.0491 -0.0306 213 LYS A O 1304 C CB . LYS A 159 ? 0.4253 0.4683 0.4383 0.0143 0.0453 -0.0338 213 LYS A CB 1305 C CG . LYS A 159 ? 0.4123 0.4579 0.4352 0.0128 0.0449 -0.0338 213 LYS A CG 1306 C CD . LYS A 159 ? 0.4110 0.4574 0.4360 0.0141 0.0439 -0.0363 213 LYS A CD 1307 C CE . LYS A 159 ? 0.4193 0.4674 0.4533 0.0127 0.0421 -0.0368 213 LYS A CE 1308 N NZ . LYS A 159 ? 0.4369 0.4886 0.4790 0.0128 0.0458 -0.0354 213 LYS A NZ 1309 N N . VAL A 160 ? 0.4310 0.4674 0.4271 0.0150 0.0415 -0.0342 214 VAL A N 1310 C CA . VAL A 160 ? 0.4259 0.4594 0.4134 0.0170 0.0405 -0.0353 214 VAL A CA 1311 C C . VAL A 160 ? 0.4474 0.4794 0.4308 0.0165 0.0412 -0.0331 214 VAL A C 1312 O O . VAL A 160 ? 0.4641 0.4942 0.4402 0.0189 0.0425 -0.0330 214 VAL A O 1313 C CB . VAL A 160 ? 0.4249 0.4563 0.4113 0.0167 0.0358 -0.0381 214 VAL A CB 1314 C CG1 . VAL A 160 ? 0.4104 0.4386 0.3890 0.0185 0.0339 -0.0394 214 VAL A CG1 1315 C CG2 . VAL A 160 ? 0.3803 0.4127 0.3697 0.0176 0.0353 -0.0403 214 VAL A CG2 1316 N N . LYS A 161 ? 0.4633 0.4959 0.4510 0.0137 0.0402 -0.0316 215 LYS A N 1317 C CA . LYS A 161 ? 0.4848 0.5163 0.4696 0.0130 0.0408 -0.0293 215 LYS A CA 1318 C C . LYS A 161 ? 0.5042 0.5369 0.4886 0.0142 0.0459 -0.0268 215 LYS A C 1319 O O . LYS A 161 ? 0.5044 0.5350 0.4816 0.0161 0.0474 -0.0258 215 LYS A O 1320 C CB . LYS A 161 ? 0.4754 0.5077 0.4660 0.0100 0.0391 -0.0281 215 LYS A CB 1321 C CG . LYS A 161 ? 0.5030 0.5344 0.4916 0.0091 0.0400 -0.0257 215 LYS A CG 1322 C CD . LYS A 161 ? 0.5637 0.5959 0.5584 0.0063 0.0381 -0.0247 215 LYS A CD 1323 C CE . LYS A 161 ? 0.6281 0.6607 0.6242 0.0054 0.0404 -0.0217 215 LYS A CE 1324 N NZ . LYS A 161 ? 0.6654 0.6960 0.6592 0.0040 0.0376 -0.0213 215 LYS A NZ 1325 N N . ASN A 162 ? 0.5031 0.5389 0.4953 0.0134 0.0484 -0.0257 216 ASN A N 1326 C CA . ASN A 162 ? 0.5207 0.5581 0.5146 0.0144 0.0539 -0.0229 216 ASN A CA 1327 C C . ASN A 162 ? 0.5319 0.5678 0.5176 0.0183 0.0566 -0.0234 216 ASN A C 1328 O O . ASN A 162 ? 0.5495 0.5842 0.5304 0.0200 0.0602 -0.0210 216 ASN A O 1329 C CB . ASN A 162 ? 0.4840 0.5250 0.4889 0.0131 0.0556 -0.0223 216 ASN A CB 1330 C CG . ASN A 162 ? 0.5266 0.5687 0.5391 0.0098 0.0533 -0.0214 216 ASN A CG 1331 O OD1 . ASN A 162 ? 0.5415 0.5818 0.5510 0.0086 0.0512 -0.0208 216 ASN A OD1 1332 N ND2 . ASN A 162 ? 0.5112 0.5561 0.5336 0.0086 0.0534 -0.0216 216 ASN A ND2 1333 N N . ALA A 163 ? 0.5484 0.5840 0.5321 0.0198 0.0549 -0.0264 217 ALA A N 1334 C CA . ALA A 163 ? 0.5495 0.5831 0.5245 0.0239 0.0566 -0.0274 217 ALA A CA 1335 C C . ALA A 163 ? 0.5665 0.5960 0.5309 0.0258 0.0551 -0.0278 217 ALA A C 1336 O O . ALA A 163 ? 0.5791 0.6066 0.5358 0.0294 0.0583 -0.0268 217 ALA A O 1337 C CB . ALA A 163 ? 0.5486 0.5824 0.5238 0.0251 0.0542 -0.0309 217 ALA A CB 1338 N N . GLN A 164 ? 0.5717 0.5996 0.5355 0.0239 0.0501 -0.0293 218 GLN A N 1339 C CA . GLN A 164 ? 0.5883 0.6123 0.5432 0.0255 0.0478 -0.0299 218 GLN A CA 1340 C C . GLN A 164 ? 0.5933 0.6165 0.5446 0.0262 0.0515 -0.0265 218 GLN A C 1341 O O . GLN A 164 ? 0.5909 0.6109 0.5329 0.0297 0.0526 -0.0263 218 GLN A O 1342 C CB . GLN A 164 ? 0.5836 0.6068 0.5408 0.0228 0.0424 -0.0315 218 GLN A CB 1343 C CG . GLN A 164 ? 0.6060 0.6279 0.5623 0.0236 0.0382 -0.0353 218 GLN A CG 1344 C CD . GLN A 164 ? 0.6048 0.6258 0.5640 0.0210 0.0334 -0.0365 218 GLN A CD 1345 O OE1 . GLN A 164 ? 0.5891 0.6100 0.5511 0.0206 0.0305 -0.0389 218 GLN A OE1 1346 N NE2 . GLN A 164 ? 0.6182 0.6385 0.5767 0.0195 0.0328 -0.0348 218 GLN A NE2 1347 N N . LEU A 165 ? 0.6046 0.6303 0.5634 0.0230 0.0532 -0.0237 219 LEU A N 1348 C CA . LEU A 165 ? 0.6174 0.6423 0.5743 0.0229 0.0564 -0.0202 219 LEU A CA 1349 C C . LEU A 165 ? 0.6310 0.6559 0.5849 0.0261 0.0627 -0.0177 219 LEU A C 1350 O O . LEU A 165 ? 0.6379 0.6606 0.5858 0.0278 0.0655 -0.0152 219 LEU A O 1351 C CB . LEU A 165 ? 0.6184 0.6457 0.5847 0.0187 0.0561 -0.0181 219 LEU A CB 1352 C CG . LEU A 165 ? 0.6401 0.6667 0.6082 0.0159 0.0505 -0.0198 219 LEU A CG 1353 C CD1 . LEU A 165 ? 0.6669 0.6956 0.6435 0.0124 0.0507 -0.0176 219 LEU A CD1 1354 C CD2 . LEU A 165 ? 0.6509 0.6737 0.6101 0.0172 0.0474 -0.0209 219 LEU A CD2 1355 N N . ALA A 166 ? 0.6262 0.6535 0.5841 0.0270 0.0651 -0.0182 220 ALA A N 1356 C CA . ALA A 166 ? 0.6369 0.6641 0.5911 0.0308 0.0713 -0.0163 220 ALA A CA 1357 C C . ALA A 166 ? 0.6396 0.6628 0.5810 0.0358 0.0705 -0.0186 220 ALA A C 1358 O O . ALA A 166 ? 0.6502 0.6728 0.5871 0.0396 0.0753 -0.0174 220 ALA A O 1359 C CB . ALA A 166 ? 0.6303 0.6618 0.5946 0.0298 0.0743 -0.0158 220 ALA A CB 1360 N N . GLY A 167 ? 0.6372 0.6576 0.5732 0.0359 0.0644 -0.0220 221 GLY A N 1361 C CA . GLY A 167 ? 0.6365 0.6525 0.5602 0.0408 0.0628 -0.0245 221 GLY A CA 1362 C C . GLY A 167 ? 0.6417 0.6575 0.5637 0.0433 0.0611 -0.0281 221 GLY A C 1363 O O . GLY A 167 ? 0.6422 0.6540 0.5537 0.0479 0.0598 -0.0303 221 GLY A O 1364 N N . ALA A 168 ? 0.6368 0.6566 0.5687 0.0405 0.0607 -0.0291 222 ALA A N 1365 C CA . ALA A 168 ? 0.6302 0.6502 0.5618 0.0424 0.0590 -0.0325 222 ALA A CA 1366 C C . ALA A 168 ? 0.6288 0.6453 0.5550 0.0435 0.0522 -0.0368 222 ALA A C 1367 O O . ALA A 168 ? 0.6252 0.6404 0.5517 0.0412 0.0481 -0.0373 222 ALA A O 1368 C CB . ALA A 168 ? 0.6230 0.6479 0.5671 0.0387 0.0593 -0.0325 222 ALA A CB 1369 N N . LYS A 169 ? 0.6162 0.6312 0.5381 0.0469 0.0509 -0.0399 223 LYS A N 1370 C CA . LYS A 169 ? 0.6187 0.6304 0.5369 0.0480 0.0443 -0.0442 223 LYS A CA 1371 C C . LYS A 169 ? 0.5980 0.6117 0.5240 0.0458 0.0408 -0.0470 223 LYS A C 1372 O O . LYS A 169 ? 0.5913 0.6026 0.5158 0.0465 0.0355 -0.0506 223 LYS A O 1373 C CB . LYS A 169 ? 0.6349 0.6418 0.5405 0.0542 0.0437 -0.0463 223 LYS A CB 1374 C CG . LYS A 169 ? 0.6778 0.6849 0.5806 0.0581 0.0464 -0.0475 223 LYS A CG 1375 C CD . LYS A 169 ? 0.7177 0.7191 0.6077 0.0642 0.0436 -0.0506 223 LYS A CD 1376 C CE . LYS A 169 ? 0.7648 0.7654 0.6482 0.0696 0.0484 -0.0504 223 LYS A CE 1377 N NZ . LYS A 169 ? 0.7601 0.7546 0.6310 0.0758 0.0444 -0.0543 223 LYS A NZ 1378 N N . GLY A 170 ? 0.5778 0.5958 0.5126 0.0431 0.0439 -0.0454 224 GLY A N 1379 C CA . GLY A 170 ? 0.5580 0.5780 0.5005 0.0409 0.0411 -0.0476 224 GLY A CA 1380 C C . GLY A 170 ? 0.5398 0.5645 0.4916 0.0380 0.0449 -0.0452 224 GLY A C 1381 O O . GLY A 170 ? 0.5397 0.5662 0.4917 0.0388 0.0502 -0.0422 224 GLY A O 1382 N N . VAL A 171 ? 0.5109 0.5374 0.4708 0.0348 0.0421 -0.0463 225 VAL A N 1383 C CA . VAL A 171 ? 0.4854 0.5161 0.4545 0.0324 0.0446 -0.0446 225 VAL A CA 1384 C C . VAL A 171 ? 0.4810 0.5125 0.4541 0.0326 0.0425 -0.0474 225 VAL A C 1385 O O . VAL A 171 ? 0.4701 0.4995 0.4427 0.0321 0.0379 -0.0499 225 VAL A O 1386 C CB . VAL A 171 ? 0.4748 0.5069 0.4504 0.0281 0.0436 -0.0426 225 VAL A CB 1387 C CG1 . VAL A 171 ? 0.4545 0.4906 0.4393 0.0262 0.0462 -0.0410 225 VAL A CG1 1388 C CG2 . VAL A 171 ? 0.4810 0.5118 0.4522 0.0278 0.0449 -0.0401 225 VAL A CG2 1389 N N . ILE A 172 ? 0.4673 0.5016 0.4445 0.0333 0.0459 -0.0469 226 ILE A N 1390 C CA . ILE A 172 ? 0.4441 0.4797 0.4264 0.0332 0.0443 -0.0491 226 ILE A CA 1391 C C . ILE A 172 ? 0.4309 0.4702 0.4230 0.0301 0.0457 -0.0472 226 ILE A C 1392 O O . ILE A 172 ? 0.4304 0.4721 0.4256 0.0299 0.0500 -0.0447 226 ILE A O 1393 C CB . ILE A 172 ? 0.4627 0.4985 0.4416 0.0372 0.0470 -0.0505 226 ILE A CB 1394 C CG1 . ILE A 172 ? 0.4847 0.5163 0.4533 0.0407 0.0448 -0.0527 226 ILE A CG1 1395 C CG2 . ILE A 172 ? 0.4146 0.4522 0.3999 0.0367 0.0456 -0.0525 226 ILE A CG2 1396 C CD1 . ILE A 172 ? 0.5050 0.5361 0.4673 0.0456 0.0483 -0.0534 226 ILE A CD1 1397 N N . LEU A 173 ? 0.3973 0.4365 0.3944 0.0277 0.0420 -0.0484 227 LEU A N 1398 C CA . LEU A 173 ? 0.3791 0.4210 0.3849 0.0252 0.0423 -0.0472 227 LEU A CA 1399 C C . LEU A 173 ? 0.3627 0.4060 0.3729 0.0261 0.0418 -0.0493 227 LEU A C 1400 O O . LEU A 173 ? 0.3858 0.4271 0.3932 0.0273 0.0392 -0.0518 227 LEU A O 1401 C CB . LEU A 173 ? 0.3618 0.4023 0.3696 0.0223 0.0384 -0.0471 227 LEU A CB 1402 C CG . LEU A 173 ? 0.3801 0.4190 0.3837 0.0212 0.0384 -0.0452 227 LEU A CG 1403 C CD1 . LEU A 173 ? 0.3648 0.4016 0.3688 0.0189 0.0343 -0.0454 227 LEU A CD1 1404 C CD2 . LEU A 173 ? 0.3921 0.4337 0.3998 0.0202 0.0420 -0.0423 227 LEU A CD2 1405 N N . TYR A 174 ? 0.3591 0.4057 0.3768 0.0255 0.0441 -0.0483 228 TYR A N 1406 C CA . TYR A 174 ? 0.3486 0.3964 0.3708 0.0264 0.0432 -0.0504 228 TYR A CA 1407 C C . TYR A 174 ? 0.3311 0.3814 0.3626 0.0244 0.0429 -0.0496 228 TYR A C 1408 O O . TYR A 174 ? 0.3406 0.3925 0.3758 0.0229 0.0446 -0.0472 228 TYR A O 1409 C CB . TYR A 174 ? 0.3551 0.4042 0.3754 0.0296 0.0468 -0.0511 228 TYR A CB 1410 C CG . TYR A 174 ? 0.3746 0.4275 0.4011 0.0298 0.0517 -0.0488 228 TYR A CG 1411 C CD1 . TYR A 174 ? 0.3920 0.4480 0.4274 0.0297 0.0524 -0.0493 228 TYR A CD1 1412 C CD2 . TYR A 174 ? 0.4183 0.4715 0.4423 0.0300 0.0555 -0.0460 228 TYR A CD2 1413 C CE1 . TYR A 174 ? 0.4226 0.4822 0.4653 0.0297 0.0572 -0.0470 228 TYR A CE1 1414 C CE2 . TYR A 174 ? 0.4315 0.4882 0.4622 0.0300 0.0604 -0.0434 228 TYR A CE2 1415 C CZ . TYR A 174 ? 0.4509 0.5109 0.4914 0.0298 0.0612 -0.0440 228 TYR A CZ 1416 O OH . TYR A 174 ? 0.4702 0.5337 0.5187 0.0297 0.0661 -0.0414 228 TYR A OH 1417 N N . SER A 175 ? 0.3324 0.3829 0.3681 0.0246 0.0406 -0.0516 229 SER A N 1418 C CA . SER A 175 ? 0.3187 0.3713 0.3634 0.0232 0.0397 -0.0514 229 SER A CA 1419 C C . SER A 175 ? 0.3372 0.3935 0.3885 0.0247 0.0431 -0.0515 229 SER A C 1420 O O . SER A 175 ? 0.3221 0.3786 0.3728 0.0266 0.0430 -0.0536 229 SER A O 1421 C CB . SER A 175 ? 0.3284 0.3787 0.3738 0.0229 0.0349 -0.0534 229 SER A CB 1422 O OG . SER A 175 ? 0.3396 0.3865 0.3796 0.0216 0.0322 -0.0530 229 SER A OG 1423 N N . ASP A 176 ? 0.3390 0.3983 0.3970 0.0237 0.0460 -0.0493 230 ASP A N 1424 C CA . ASP A 176 ? 0.3646 0.4278 0.4306 0.0249 0.0495 -0.0491 230 ASP A CA 1425 C C . ASP A 176 ? 0.3662 0.4306 0.4414 0.0242 0.0462 -0.0509 230 ASP A C 1426 O O . ASP A 176 ? 0.3679 0.4312 0.4459 0.0223 0.0428 -0.0507 230 ASP A O 1427 C CB . ASP A 176 ? 0.3647 0.4305 0.4349 0.0243 0.0544 -0.0458 230 ASP A CB 1428 C CG . ASP A 176 ? 0.3877 0.4572 0.4642 0.0262 0.0596 -0.0451 230 ASP A CG 1429 O OD1 . ASP A 176 ? 0.3907 0.4603 0.4617 0.0282 0.0642 -0.0437 230 ASP A OD1 1430 O OD2 . ASP A 176 ? 0.4003 0.4722 0.4866 0.0260 0.0588 -0.0462 230 ASP A OD2 1431 N N . PRO A 177 ? 0.3773 0.4436 0.4570 0.0260 0.0470 -0.0526 231 PRO A N 1432 C CA . PRO A 177 ? 0.3834 0.4508 0.4719 0.0257 0.0437 -0.0544 231 PRO A CA 1433 C C . PRO A 177 ? 0.3770 0.4469 0.4763 0.0239 0.0440 -0.0529 231 PRO A C 1434 O O . PRO A 177 ? 0.3784 0.4479 0.4835 0.0233 0.0398 -0.0543 231 PRO A O 1435 C CB . PRO A 177 ? 0.3994 0.4692 0.4912 0.0281 0.0460 -0.0560 231 PRO A CB 1436 C CG . PRO A 177 ? 0.3970 0.4651 0.4781 0.0298 0.0483 -0.0560 231 PRO A CG 1437 C CD . PRO A 177 ? 0.3851 0.4520 0.4603 0.0287 0.0502 -0.0534 231 PRO A CD 1438 N N . ALA A 178 ? 0.3958 0.4679 0.4977 0.0232 0.0487 -0.0500 232 ALA A N 1439 C CA . ALA A 178 ? 0.4022 0.4767 0.5154 0.0214 0.0488 -0.0484 232 ALA A CA 1440 C C . ALA A 178 ? 0.4167 0.4881 0.5282 0.0195 0.0435 -0.0488 232 ALA A C 1441 O O . ALA A 178 ? 0.4090 0.4811 0.5295 0.0186 0.0402 -0.0495 232 ALA A O 1442 C CB . ALA A 178 ? 0.4213 0.4981 0.5362 0.0210 0.0551 -0.0448 232 ALA A CB 1443 N N . ASP A 179 ? 0.4110 0.4789 0.5108 0.0192 0.0421 -0.0486 233 ASP A N 1444 C CA . ASP A 179 ? 0.4212 0.4859 0.5178 0.0177 0.0377 -0.0486 233 ASP A CA 1445 C C . ASP A 179 ? 0.4198 0.4811 0.5117 0.0185 0.0325 -0.0513 233 ASP A C 1446 O O . ASP A 179 ? 0.4322 0.4913 0.5249 0.0178 0.0283 -0.0519 233 ASP A O 1447 C CB . ASP A 179 ? 0.4194 0.4824 0.5070 0.0168 0.0397 -0.0464 233 ASP A CB 1448 C CG . ASP A 179 ? 0.4126 0.4785 0.5033 0.0165 0.0453 -0.0434 233 ASP A CG 1449 O OD1 . ASP A 179 ? 0.4428 0.5102 0.5413 0.0149 0.0457 -0.0418 233 ASP A OD1 1450 O OD2 . ASP A 179 ? 0.4189 0.4852 0.5041 0.0179 0.0493 -0.0427 233 ASP A OD2 1451 N N . TYR A 180 ? 0.3885 0.4490 0.4754 0.0201 0.0328 -0.0529 234 TYR A N 1452 C CA . TYR A 180 ? 0.3756 0.4323 0.4567 0.0209 0.0284 -0.0550 234 TYR A CA 1453 C C . TYR A 180 ? 0.3884 0.4453 0.4728 0.0227 0.0267 -0.0577 234 TYR A C 1454 O O . TYR A 180 ? 0.3913 0.4450 0.4699 0.0237 0.0241 -0.0592 234 TYR A O 1455 C CB . TYR A 180 ? 0.3692 0.4232 0.4394 0.0211 0.0292 -0.0546 234 TYR A CB 1456 C CG . TYR A 180 ? 0.3525 0.4048 0.4181 0.0193 0.0291 -0.0524 234 TYR A CG 1457 C CD1 . TYR A 180 ? 0.3455 0.3994 0.4093 0.0187 0.0330 -0.0503 234 TYR A CD1 1458 C CD2 . TYR A 180 ? 0.3371 0.3861 0.4004 0.0185 0.0253 -0.0525 234 TYR A CD2 1459 C CE1 . TYR A 180 ? 0.3377 0.3901 0.3977 0.0170 0.0328 -0.0484 234 TYR A CE1 1460 C CE2 . TYR A 180 ? 0.3205 0.3680 0.3799 0.0170 0.0251 -0.0505 234 TYR A CE2 1461 C CZ . TYR A 180 ? 0.3554 0.4047 0.4133 0.0161 0.0288 -0.0486 234 TYR A CZ 1462 O OH . TYR A 180 ? 0.3151 0.3630 0.3695 0.0147 0.0285 -0.0468 234 TYR A OH 1463 N N . PHE A 181 ? 0.3840 0.4447 0.4779 0.0233 0.0283 -0.0581 235 PHE A N 1464 C CA . PHE A 181 ? 0.3917 0.4528 0.4891 0.0251 0.0267 -0.0608 235 PHE A CA 1465 C C . PHE A 181 ? 0.3985 0.4617 0.5075 0.0249 0.0248 -0.0615 235 PHE A C 1466 O O . PHE A 181 ? 0.4051 0.4723 0.5225 0.0243 0.0281 -0.0601 235 PHE A O 1467 C CB . PHE A 181 ? 0.3905 0.4544 0.4877 0.0265 0.0311 -0.0609 235 PHE A CB 1468 C CG . PHE A 181 ? 0.3812 0.4451 0.4802 0.0286 0.0295 -0.0637 235 PHE A CG 1469 C CD1 . PHE A 181 ? 0.3507 0.4112 0.4410 0.0298 0.0278 -0.0652 235 PHE A CD1 1470 C CD2 . PHE A 181 ? 0.4001 0.4674 0.5103 0.0293 0.0296 -0.0649 235 PHE A CD2 1471 C CE1 . PHE A 181 ? 0.3734 0.4337 0.4655 0.0317 0.0261 -0.0678 235 PHE A CE1 1472 C CE2 . PHE A 181 ? 0.3697 0.4369 0.4816 0.0313 0.0280 -0.0676 235 PHE A CE2 1473 C CZ . PHE A 181 ? 0.3834 0.4471 0.4860 0.0325 0.0263 -0.0690 235 PHE A CZ 1474 N N . ALA A 182 ? 0.4023 0.4626 0.5120 0.0256 0.0195 -0.0634 236 ALA A N 1475 C CA . ALA A 182 ? 0.4227 0.4845 0.5434 0.0257 0.0166 -0.0646 236 ALA A CA 1476 C C . ALA A 182 ? 0.4397 0.5048 0.5691 0.0272 0.0174 -0.0665 236 ALA A C 1477 O O . ALA A 182 ? 0.4319 0.4958 0.5567 0.0289 0.0170 -0.0681 236 ALA A O 1478 C CB . ALA A 182 ? 0.4247 0.4816 0.5420 0.0266 0.0104 -0.0661 236 ALA A CB 1479 N N . PRO A 183 ? 0.4628 0.5322 0.6052 0.0267 0.0189 -0.0662 237 PRO A N 1480 C CA . PRO A 183 ? 0.4648 0.5377 0.6167 0.0282 0.0198 -0.0679 237 PRO A CA 1481 C C . PRO A 183 ? 0.4685 0.5385 0.6200 0.0303 0.0140 -0.0715 237 PRO A C 1482 O O . PRO A 183 ? 0.4685 0.5350 0.6198 0.0306 0.0084 -0.0728 237 PRO A O 1483 C CB . PRO A 183 ? 0.4772 0.5541 0.6441 0.0270 0.0207 -0.0671 237 PRO A CB 1484 C CG . PRO A 183 ? 0.4868 0.5637 0.6499 0.0248 0.0239 -0.0637 237 PRO A CG 1485 C CD . PRO A 183 ? 0.4673 0.5387 0.6167 0.0247 0.0202 -0.0639 237 PRO A CD 1486 N N . GLY A 184 ? 0.4676 0.5383 0.6178 0.0320 0.0153 -0.0730 238 GLY A N 1487 C CA . GLY A 184 ? 0.4684 0.5371 0.6203 0.0342 0.0103 -0.0764 238 GLY A CA 1488 C C . GLY A 184 ? 0.4667 0.5291 0.6066 0.0354 0.0057 -0.0776 238 GLY A C 1489 O O . GLY A 184 ? 0.4820 0.5417 0.6228 0.0374 0.0009 -0.0802 238 GLY A O 1490 N N . VAL A 185 ? 0.4409 0.5006 0.5696 0.0343 0.0072 -0.0755 239 VAL A N 1491 C CA . VAL A 185 ? 0.4069 0.4606 0.5242 0.0353 0.0038 -0.0761 239 VAL A CA 1492 C C . VAL A 185 ? 0.3922 0.4456 0.5017 0.0356 0.0069 -0.0758 239 VAL A C 1493 O O . VAL A 185 ? 0.3902 0.4466 0.4990 0.0345 0.0116 -0.0742 239 VAL A O 1494 C CB . VAL A 185 ? 0.4142 0.4645 0.5253 0.0340 0.0022 -0.0742 239 VAL A CB 1495 C CG1 A VAL A 185 ? 0.4155 0.4694 0.5301 0.0315 0.0060 -0.0717 239 VAL A CG1 1496 C CG1 B VAL A 185 ? 0.3783 0.4226 0.4773 0.0350 0.0001 -0.0742 239 VAL A CG1 1497 C CG2 A VAL A 185 ? 0.3795 0.4249 0.4779 0.0343 0.0018 -0.0735 239 VAL A CG2 1498 C CG2 B VAL A 185 ? 0.3780 0.4281 0.4967 0.0341 -0.0017 -0.0750 239 VAL A CG2 1499 N N A LYS A 186 ? 0.4006 0.4501 0.5043 0.0374 0.0043 -0.0775 240 LYS A N 1500 N N B LYS A 186 ? 0.3997 0.4489 0.5031 0.0374 0.0041 -0.0774 240 LYS A N 1501 C CA A LYS A 186 ? 0.4027 0.4517 0.5000 0.0379 0.0068 -0.0775 240 LYS A CA 1502 C CA B LYS A 186 ? 0.4041 0.4521 0.5004 0.0380 0.0060 -0.0776 240 LYS A CA 1503 C C A LYS A 186 ? 0.4069 0.4526 0.4941 0.0366 0.0075 -0.0754 240 LYS A C 1504 C C B LYS A 186 ? 0.4069 0.4526 0.4941 0.0364 0.0076 -0.0752 240 LYS A C 1505 O O A LYS A 186 ? 0.3964 0.4384 0.4800 0.0362 0.0049 -0.0746 240 LYS A O 1506 O O B LYS A 186 ? 0.3981 0.4411 0.4824 0.0356 0.0058 -0.0740 240 LYS A O 1507 C CB A LYS A 186 ? 0.4207 0.4672 0.5167 0.0404 0.0039 -0.0801 240 LYS A CB 1508 C CB B LYS A 186 ? 0.4154 0.4591 0.5086 0.0404 0.0019 -0.0798 240 LYS A CB 1509 C CG A LYS A 186 ? 0.4006 0.4506 0.5064 0.0419 0.0034 -0.0825 240 LYS A CG 1510 C CG B LYS A 186 ? 0.4165 0.4621 0.5189 0.0423 -0.0003 -0.0825 240 LYS A CG 1511 C CD A LYS A 186 ? 0.4308 0.4866 0.5420 0.0415 0.0087 -0.0821 240 LYS A CD 1512 C CD B LYS A 186 ? 0.4506 0.4923 0.5494 0.0448 -0.0035 -0.0847 240 LYS A CD 1513 C CE A LYS A 186 ? 0.4476 0.5053 0.5642 0.0438 0.0083 -0.0847 240 LYS A CE 1514 C CE B LYS A 186 ? 0.4793 0.5223 0.5871 0.0468 -0.0067 -0.0875 240 LYS A CE 1515 N NZ A LYS A 186 ? 0.4672 0.5309 0.5912 0.0438 0.0133 -0.0843 240 LYS A NZ 1516 N NZ B LYS A 186 ? 0.4839 0.5281 0.5927 0.0485 -0.0059 -0.0894 240 LYS A NZ 1517 N N . SER A 187 ? 0.3973 0.4440 0.4803 0.0362 0.0109 -0.0748 241 SER A N 1518 C CA . SER A 187 ? 0.4108 0.4549 0.4851 0.0350 0.0119 -0.0731 241 SER A CA 1519 C C . SER A 187 ? 0.4025 0.4413 0.4704 0.0360 0.0090 -0.0737 241 SER A C 1520 O O . SER A 187 ? 0.4048 0.4420 0.4733 0.0378 0.0071 -0.0757 241 SER A O 1521 C CB . SER A 187 ? 0.4311 0.4776 0.5030 0.0350 0.0159 -0.0728 241 SER A CB 1522 O OG . SER A 187 ? 0.4934 0.5447 0.5713 0.0345 0.0193 -0.0720 241 SER A OG 1523 N N . TYR A 188 ? 0.3758 0.4115 0.4375 0.0347 0.0087 -0.0718 242 TYR A N 1524 C CA . TYR A 188 ? 0.3754 0.4058 0.4312 0.0354 0.0066 -0.0718 242 TYR A CA 1525 C C . TYR A 188 ? 0.3704 0.4003 0.4245 0.0367 0.0071 -0.0735 242 TYR A C 1526 O O . TYR A 188 ? 0.3683 0.4010 0.4222 0.0364 0.0096 -0.0737 242 TYR A O 1527 C CB . TYR A 188 ? 0.3562 0.3843 0.4065 0.0337 0.0073 -0.0694 242 TYR A CB 1528 C CG . TYR A 188 ? 0.3378 0.3603 0.3833 0.0345 0.0051 -0.0687 242 TYR A CG 1529 C CD1 . TYR A 188 ? 0.3409 0.3605 0.3860 0.0354 0.0027 -0.0681 242 TYR A CD1 1530 C CD2 . TYR A 188 ? 0.3531 0.3730 0.3949 0.0347 0.0053 -0.0687 242 TYR A CD2 1531 C CE1 . TYR A 188 ? 0.3555 0.3696 0.3958 0.0366 0.0011 -0.0673 242 TYR A CE1 1532 C CE2 . TYR A 188 ? 0.3876 0.4021 0.4257 0.0355 0.0038 -0.0678 242 TYR A CE2 1533 C CZ . TYR A 188 ? 0.3832 0.3949 0.4204 0.0366 0.0019 -0.0669 242 TYR A CZ 1534 O OH . TYR A 188 ? 0.4573 0.4635 0.4904 0.0377 0.0010 -0.0657 242 TYR A OH 1535 N N . PRO A 189 ? 0.3868 0.4128 0.4392 0.0384 0.0046 -0.0745 243 PRO A N 1536 C CA . PRO A 189 ? 0.3907 0.4120 0.4410 0.0394 0.0017 -0.0740 243 PRO A CA 1537 C C . PRO A 189 ? 0.3979 0.4192 0.4524 0.0412 -0.0008 -0.0756 243 PRO A C 1538 O O . PRO A 189 ? 0.4107 0.4275 0.4625 0.0428 -0.0034 -0.0755 243 PRO A O 1539 C CB . PRO A 189 ? 0.3906 0.4079 0.4370 0.0404 0.0011 -0.0744 243 PRO A CB 1540 C CG . PRO A 189 ? 0.3984 0.4189 0.4477 0.0412 0.0020 -0.0768 243 PRO A CG 1541 C CD . PRO A 189 ? 0.4075 0.4332 0.4589 0.0396 0.0049 -0.0763 243 PRO A CD 1542 N N . ASP A 190 ? 0.3917 0.4179 0.4527 0.0413 0.0000 -0.0771 244 ASP A N 1543 C CA . ASP A 190 ? 0.4085 0.4350 0.4748 0.0432 -0.0028 -0.0790 244 ASP A CA 1544 C C . ASP A 190 ? 0.4012 0.4295 0.4721 0.0425 -0.0038 -0.0785 244 ASP A C 1545 O O . ASP A 190 ? 0.3901 0.4185 0.4659 0.0440 -0.0067 -0.0803 244 ASP A O 1546 C CB . ASP A 190 ? 0.4256 0.4561 0.4976 0.0441 -0.0018 -0.0813 244 ASP A CB 1547 C CG . ASP A 190 ? 0.4666 0.4951 0.5341 0.0450 -0.0011 -0.0821 244 ASP A CG 1548 O OD1 . ASP A 190 ? 0.4961 0.5194 0.5592 0.0465 -0.0036 -0.0824 244 ASP A OD1 1549 O OD2 . ASP A 190 ? 0.5149 0.5467 0.5830 0.0444 0.0018 -0.0824 244 ASP A OD2 1550 N N . GLY A 191 ? 0.3807 0.4102 0.4499 0.0402 -0.0017 -0.0762 245 GLY A N 1551 C CA . GLY A 191 ? 0.3691 0.4000 0.4424 0.0393 -0.0026 -0.0755 245 GLY A CA 1552 C C . GLY A 191 ? 0.3622 0.3928 0.4308 0.0370 -0.0004 -0.0728 245 GLY A C 1553 O O . GLY A 191 ? 0.3586 0.3876 0.4211 0.0363 0.0012 -0.0717 245 GLY A O 1554 N N . TRP A 192 ? 0.3442 0.3764 0.4162 0.0358 -0.0006 -0.0718 246 TRP A N 1555 C CA . TRP A 192 ? 0.3451 0.3767 0.4125 0.0337 0.0010 -0.0692 246 TRP A CA 1556 C C . TRP A 192 ? 0.3503 0.3868 0.4203 0.0313 0.0052 -0.0678 246 TRP A C 1557 O O . TRP A 192 ? 0.3312 0.3677 0.3987 0.0296 0.0065 -0.0657 246 TRP A O 1558 C CB . TRP A 192 ? 0.3486 0.3774 0.4155 0.0341 -0.0020 -0.0686 246 TRP A CB 1559 C CG . TRP A 192 ? 0.3794 0.4107 0.4553 0.0345 -0.0042 -0.0701 246 TRP A CG 1560 C CD1 . TRP A 192 ? 0.4147 0.4442 0.4940 0.0371 -0.0083 -0.0725 246 TRP A CD1 1561 C CD2 . TRP A 192 ? 0.3926 0.4282 0.4756 0.0326 -0.0027 -0.0693 246 TRP A CD2 1562 N NE1 . TRP A 192 ? 0.4239 0.4565 0.5125 0.0367 -0.0097 -0.0734 246 TRP A NE1 1563 C CE2 . TRP A 192 ? 0.3777 0.4142 0.4691 0.0339 -0.0061 -0.0713 246 TRP A CE2 1564 C CE3 . TRP A 192 ? 0.3930 0.4317 0.4762 0.0299 0.0010 -0.0670 246 TRP A CE3 1565 C CZ2 . TRP A 192 ? 0.3855 0.4259 0.4862 0.0324 -0.0057 -0.0710 246 TRP A CZ2 1566 C CZ3 . TRP A 192 ? 0.4117 0.4541 0.5035 0.0286 0.0017 -0.0665 246 TRP A CZ3 1567 C CH2 . TRP A 192 ? 0.3912 0.4346 0.4922 0.0297 -0.0015 -0.0685 246 TRP A CH2 1568 N N . ASN A 193 ? 0.3305 0.3709 0.4049 0.0316 0.0077 -0.0688 247 ASN A N 1569 C CA . ASN A 193 ? 0.3471 0.3917 0.4233 0.0300 0.0120 -0.0675 247 ASN A CA 1570 C C . ASN A 193 ? 0.3362 0.3798 0.4050 0.0297 0.0143 -0.0667 247 ASN A C 1571 O O . ASN A 193 ? 0.3360 0.3762 0.3998 0.0307 0.0127 -0.0677 247 ASN A O 1572 C CB . ASN A 193 ? 0.3469 0.3964 0.4317 0.0307 0.0140 -0.0687 247 ASN A CB 1573 C CG . ASN A 193 ? 0.3820 0.4351 0.4752 0.0295 0.0153 -0.0676 247 ASN A CG 1574 O OD1 . ASN A 193 ? 0.3855 0.4380 0.4773 0.0278 0.0155 -0.0656 247 ASN A OD1 1575 N ND2 . ASN A 193 ? 0.3383 0.3954 0.4411 0.0302 0.0163 -0.0687 247 ASN A ND2 1576 N N . LEU A 194 ? 0.3357 0.3819 0.4038 0.0283 0.0178 -0.0650 248 LEU A N 1577 C CA . LEU A 194 ? 0.3256 0.3709 0.3867 0.0281 0.0198 -0.0643 248 LEU A CA 1578 C C . LEU A 194 ? 0.3403 0.3877 0.4018 0.0297 0.0220 -0.0659 248 LEU A C 1579 O O . LEU A 194 ? 0.3442 0.3955 0.4112 0.0302 0.0248 -0.0658 248 LEU A O 1580 C CB . LEU A 194 ? 0.3205 0.3676 0.3806 0.0264 0.0226 -0.0620 248 LEU A CB 1581 C CG . LEU A 194 ? 0.3224 0.3684 0.3751 0.0262 0.0245 -0.0612 248 LEU A CG 1582 C CD1 . LEU A 194 ? 0.3218 0.3633 0.3680 0.0258 0.0219 -0.0612 248 LEU A CD1 1583 C CD2 . LEU A 194 ? 0.3051 0.3533 0.3580 0.0248 0.0276 -0.0588 248 LEU A CD2 1584 N N . PRO A 195 ? 0.3400 0.3846 0.3962 0.0308 0.0208 -0.0672 249 PRO A N 1585 C CA . PRO A 195 ? 0.3513 0.3975 0.4069 0.0327 0.0229 -0.0687 249 PRO A CA 1586 C C . PRO A 195 ? 0.3583 0.4056 0.4095 0.0325 0.0262 -0.0675 249 PRO A C 1587 O O . PRO A 195 ? 0.3473 0.3931 0.3946 0.0310 0.0261 -0.0658 249 PRO A O 1588 C CB . PRO A 195 ? 0.3645 0.4067 0.4159 0.0338 0.0200 -0.0705 249 PRO A CB 1589 C CG . PRO A 195 ? 0.3643 0.4028 0.4127 0.0324 0.0174 -0.0694 249 PRO A CG 1590 C CD . PRO A 195 ? 0.3429 0.3827 0.3944 0.0307 0.0176 -0.0675 249 PRO A CD 1591 N N . GLY A 196 ? 0.3438 0.3932 0.3947 0.0345 0.0289 -0.0685 250 GLY A N 1592 C CA . GLY A 196 ? 0.3304 0.3805 0.3761 0.0352 0.0322 -0.0675 250 GLY A CA 1593 C C . GLY A 196 ? 0.3248 0.3711 0.3622 0.0352 0.0306 -0.0677 250 GLY A C 1594 O O . GLY A 196 ? 0.3428 0.3892 0.3757 0.0355 0.0328 -0.0666 250 GLY A O 1595 N N . GLY A 197 ? 0.3059 0.3488 0.3416 0.0351 0.0268 -0.0693 251 GLY A N 1596 C CA . GLY A 197 ? 0.3148 0.3539 0.3443 0.0349 0.0247 -0.0697 251 GLY A CA 1597 C C . GLY A 197 ? 0.3057 0.3430 0.3349 0.0322 0.0229 -0.0677 251 GLY A C 1598 O O . GLY A 197 ? 0.3151 0.3495 0.3401 0.0317 0.0214 -0.0676 251 GLY A O 1599 N N . GLY A 198 ? 0.3142 0.3529 0.3481 0.0307 0.0231 -0.0662 252 GLY A N 1600 C CA . GLY A 198 ? 0.2976 0.3343 0.3310 0.0285 0.0214 -0.0644 252 GLY A CA 1601 C C . GLY A 198 ? 0.3083 0.3460 0.3389 0.0274 0.0234 -0.0625 252 GLY A C 1602 O O . GLY A 198 ? 0.3018 0.3424 0.3330 0.0279 0.0264 -0.0619 252 GLY A O 1603 N N . VAL A 199 ? 0.2955 0.3306 0.3234 0.0258 0.0219 -0.0612 253 VAL A N 1604 C CA . VAL A 199 ? 0.2830 0.3185 0.3076 0.0249 0.0234 -0.0595 253 VAL A CA 1605 C C . VAL A 199 ? 0.2856 0.3196 0.3107 0.0227 0.0220 -0.0576 253 VAL A C 1606 O O . VAL A 199 ? 0.2956 0.3269 0.3206 0.0224 0.0196 -0.0578 253 VAL A O 1607 C CB . VAL A 199 ? 0.2921 0.3253 0.3109 0.0258 0.0227 -0.0606 253 VAL A CB 1608 C CG1 . VAL A 199 ? 0.2881 0.3217 0.3035 0.0250 0.0243 -0.0589 253 VAL A CG1 1609 C CG2 . VAL A 199 ? 0.3021 0.3360 0.3193 0.0285 0.0236 -0.0629 253 VAL A CG2 1610 N N . GLN A 200 ? 0.2769 0.3127 0.3025 0.0215 0.0237 -0.0557 254 GLN A N 1611 C CA . GLN A 200 ? 0.2738 0.3084 0.2995 0.0197 0.0226 -0.0539 254 GLN A CA 1612 C C . GLN A 200 ? 0.2701 0.3025 0.2908 0.0191 0.0221 -0.0533 254 GLN A C 1613 O O . GLN A 200 ? 0.2707 0.3042 0.2887 0.0192 0.0238 -0.0527 254 GLN A O 1614 C CB . GLN A 200 ? 0.2747 0.3122 0.3037 0.0187 0.0245 -0.0522 254 GLN A CB 1615 C CG . GLN A 200 ? 0.2871 0.3231 0.3161 0.0169 0.0231 -0.0503 254 GLN A CG 1616 C CD . GLN A 200 ? 0.2888 0.3276 0.3211 0.0159 0.0250 -0.0486 254 GLN A CD 1617 O OE1 . GLN A 200 ? 0.2661 0.3042 0.2965 0.0145 0.0251 -0.0469 254 GLN A OE1 1618 N NE2 . GLN A 200 ? 0.2637 0.3054 0.3017 0.0164 0.0264 -0.0490 254 GLN A NE2 1619 N N . ARG A 201 ? 0.2582 0.2875 0.2778 0.0186 0.0198 -0.0533 255 ARG A N 1620 C CA . ARG A 201 ? 0.2681 0.2955 0.2844 0.0176 0.0191 -0.0523 255 ARG A CA 1621 C C . ARG A 201 ? 0.2607 0.2887 0.2769 0.0160 0.0198 -0.0500 255 ARG A C 1622 O O . ARG A 201 ? 0.2512 0.2807 0.2704 0.0155 0.0202 -0.0492 255 ARG A O 1623 C CB . ARG A 201 ? 0.2683 0.2922 0.2846 0.0176 0.0169 -0.0526 255 ARG A CB 1624 C CG . ARG A 201 ? 0.2652 0.2879 0.2815 0.0191 0.0159 -0.0549 255 ARG A CG 1625 C CD . ARG A 201 ? 0.2698 0.2894 0.2879 0.0192 0.0142 -0.0549 255 ARG A CD 1626 N NE . ARG A 201 ? 0.2954 0.3138 0.3141 0.0206 0.0131 -0.0571 255 ARG A NE 1627 C CZ . ARG A 201 ? 0.3226 0.3423 0.3425 0.0220 0.0134 -0.0586 255 ARG A CZ 1628 N NH1 . ARG A 201 ? 0.2879 0.3102 0.3090 0.0220 0.0147 -0.0581 255 ARG A NH1 1629 N NH2 . ARG A 201 ? 0.3125 0.3310 0.3328 0.0233 0.0123 -0.0607 255 ARG A NH2 1630 N N . GLY A 202 ? 0.2766 0.3033 0.2900 0.0152 0.0194 -0.0492 256 GLY A N 1631 C CA . GLY A 202 ? 0.2587 0.2856 0.2720 0.0136 0.0196 -0.0470 256 GLY A CA 1632 C C . GLY A 202 ? 0.2649 0.2912 0.2748 0.0130 0.0199 -0.0463 256 GLY A C 1633 O O . GLY A 202 ? 0.2549 0.2817 0.2620 0.0140 0.0207 -0.0473 256 GLY A O 1634 N N . ASN A 203 ? 0.2695 0.2946 0.2790 0.0117 0.0191 -0.0447 257 ASN A N 1635 C CA . ASN A 203 ? 0.2688 0.2934 0.2751 0.0112 0.0192 -0.0441 257 ASN A CA 1636 C C . ASN A 203 ? 0.2659 0.2928 0.2710 0.0109 0.0213 -0.0430 257 ASN A C 1637 O O . ASN A 203 ? 0.2531 0.2819 0.2611 0.0106 0.0225 -0.0422 257 ASN A O 1638 C CB . ASN A 203 ? 0.2689 0.2914 0.2752 0.0099 0.0179 -0.0426 257 ASN A CB 1639 C CG . ASN A 203 ? 0.2957 0.3192 0.3029 0.0088 0.0185 -0.0406 257 ASN A CG 1640 O OD1 . ASN A 203 ? 0.3350 0.3596 0.3407 0.0082 0.0196 -0.0396 257 ASN A OD1 1641 N ND2 . ASN A 203 ? 0.3028 0.3252 0.3120 0.0087 0.0178 -0.0400 257 ASN A ND2 1642 N N . ILE A 204 ? 0.2687 0.2951 0.2699 0.0112 0.0217 -0.0429 258 ILE A N 1643 C CA . ILE A 204 ? 0.2846 0.3127 0.2838 0.0114 0.0241 -0.0417 258 ILE A CA 1644 C C . ILE A 204 ? 0.3066 0.3336 0.3032 0.0103 0.0236 -0.0402 258 ILE A C 1645 O O . ILE A 204 ? 0.3071 0.3340 0.2997 0.0110 0.0248 -0.0397 258 ILE A O 1646 C CB . ILE A 204 ? 0.3091 0.3374 0.3046 0.0136 0.0254 -0.0431 258 ILE A CB 1647 C CG1 . ILE A 204 ? 0.3089 0.3346 0.3011 0.0148 0.0228 -0.0452 258 ILE A CG1 1648 C CG2 . ILE A 204 ? 0.2894 0.3198 0.2882 0.0146 0.0270 -0.0439 258 ILE A CG2 1649 C CD1 . ILE A 204 ? 0.3680 0.3927 0.3541 0.0176 0.0235 -0.0467 258 ILE A CD1 1650 N N . LEU A 205 ? 0.3031 0.3289 0.3015 0.0089 0.0219 -0.0394 259 LEU A N 1651 C CA . LEU A 205 ? 0.3112 0.3359 0.3076 0.0079 0.0212 -0.0381 259 LEU A CA 1652 C C . LEU A 205 ? 0.3170 0.3432 0.3141 0.0068 0.0228 -0.0360 259 LEU A C 1653 O O . LEU A 205 ? 0.3311 0.3591 0.3318 0.0065 0.0239 -0.0354 259 LEU A O 1654 C CB . LEU A 205 ? 0.2937 0.3167 0.2922 0.0069 0.0191 -0.0379 259 LEU A CB 1655 C CG . LEU A 205 ? 0.3321 0.3533 0.3310 0.0076 0.0173 -0.0396 259 LEU A CG 1656 C CD1 . LEU A 205 ? 0.3620 0.3816 0.3636 0.0068 0.0162 -0.0387 259 LEU A CD1 1657 C CD2 . LEU A 205 ? 0.3347 0.3545 0.3302 0.0081 0.0162 -0.0404 259 LEU A CD2 1658 N N A ASN A 206 ? 0.3222 0.3477 0.3165 0.0063 0.0228 -0.0348 260 ASN A N 1659 N N B ASN A 206 ? 0.3199 0.3453 0.3142 0.0062 0.0227 -0.0348 260 ASN A N 1660 C CA A ASN A 206 ? 0.3201 0.3465 0.3155 0.0050 0.0238 -0.0326 260 ASN A CA 1661 C CA B ASN A 206 ? 0.3174 0.3438 0.3127 0.0050 0.0239 -0.0326 260 ASN A CA 1662 C C A ASN A 206 ? 0.3177 0.3423 0.3122 0.0039 0.0219 -0.0318 260 ASN A C 1663 C C B ASN A 206 ? 0.3120 0.3367 0.3067 0.0038 0.0220 -0.0317 260 ASN A C 1664 O O A ASN A 206 ? 0.3148 0.3386 0.3061 0.0038 0.0218 -0.0311 260 ASN A O 1665 O O B ASN A 206 ? 0.3105 0.3346 0.3023 0.0036 0.0221 -0.0307 260 ASN A O 1666 C CB A ASN A 206 ? 0.3481 0.3753 0.3405 0.0057 0.0264 -0.0316 260 ASN A CB 1667 C CB B ASN A 206 ? 0.3333 0.3602 0.3251 0.0058 0.0263 -0.0317 260 ASN A CB 1668 C CG A ASN A 206 ? 0.3475 0.3768 0.3420 0.0066 0.0290 -0.0316 260 ASN A CG 1669 C CG B ASN A 206 ? 0.3411 0.3692 0.3349 0.0045 0.0278 -0.0293 260 ASN A CG 1670 O OD1 A ASN A 206 ? 0.4149 0.4461 0.4139 0.0057 0.0305 -0.0303 260 ASN A OD1 1671 O OD1 B ASN A 206 ? 0.3589 0.3882 0.3578 0.0034 0.0278 -0.0286 260 ASN A OD1 1672 N ND2 A ASN A 206 ? 0.3482 0.3773 0.3403 0.0084 0.0294 -0.0334 260 ASN A ND2 1673 N ND2 B ASN A 206 ? 0.3566 0.3839 0.3462 0.0049 0.0290 -0.0280 260 ASN A ND2 1674 N N . LEU A 207 ? 0.2981 0.3219 0.2953 0.0034 0.0203 -0.0320 261 LEU A N 1675 C CA . LEU A 207 ? 0.2967 0.3187 0.2932 0.0027 0.0186 -0.0313 261 LEU A CA 1676 C C . LEU A 207 ? 0.2967 0.3188 0.2938 0.0016 0.0187 -0.0294 261 LEU A C 1677 O O . LEU A 207 ? 0.2709 0.2917 0.2669 0.0011 0.0176 -0.0287 261 LEU A O 1678 C CB . LEU A 207 ? 0.3211 0.3417 0.3199 0.0030 0.0173 -0.0319 261 LEU A CB 1679 C CG . LEU A 207 ? 0.3331 0.3529 0.3321 0.0039 0.0168 -0.0337 261 LEU A CG 1680 C CD1 . LEU A 207 ? 0.3518 0.3701 0.3535 0.0042 0.0161 -0.0337 261 LEU A CD1 1681 C CD2 . LEU A 207 ? 0.3233 0.3419 0.3204 0.0039 0.0157 -0.0342 261 LEU A CD2 1682 N N . ASN A 208 ? 0.2750 0.2988 0.2746 0.0013 0.0197 -0.0288 262 ASN A N 1683 C CA . ASN A 208 ? 0.2914 0.3151 0.2925 0.0004 0.0192 -0.0272 262 ASN A CA 1684 C C . ASN A 208 ? 0.2795 0.3011 0.2805 0.0004 0.0173 -0.0270 262 ASN A C 1685 O O . ASN A 208 ? 0.2822 0.3028 0.2820 -0.0001 0.0166 -0.0258 262 ASN A O 1686 C CB . ASN A 208 ? 0.2792 0.3030 0.2778 -0.0002 0.0201 -0.0259 262 ASN A CB 1687 C CG . ASN A 208 ? 0.3752 0.4010 0.3745 0.0000 0.0227 -0.0255 262 ASN A CG 1688 O OD1 . ASN A 208 ? 0.4029 0.4303 0.4063 0.0000 0.0234 -0.0257 262 ASN A OD1 1689 N ND2 . ASN A 208 ? 0.3768 0.4023 0.3722 0.0002 0.0239 -0.0250 262 ASN A ND2 1690 N N . GLY A 209 ? 0.2664 0.2871 0.2683 0.0013 0.0166 -0.0280 263 GLY A N 1691 C CA . GLY A 209 ? 0.2578 0.2764 0.2595 0.0019 0.0153 -0.0275 263 GLY A CA 1692 C C . GLY A 209 ? 0.2595 0.2762 0.2593 0.0019 0.0150 -0.0271 263 GLY A C 1693 O O . GLY A 209 ? 0.2587 0.2735 0.2581 0.0026 0.0144 -0.0264 263 GLY A O 1694 N N . ALA A 210 ? 0.2348 0.2521 0.2336 0.0015 0.0154 -0.0278 264 ALA A N 1695 C CA . ALA A 210 ? 0.2331 0.2488 0.2312 0.0014 0.0148 -0.0275 264 ALA A CA 1696 C C . ALA A 210 ? 0.2292 0.2434 0.2292 0.0023 0.0147 -0.0279 264 ALA A C 1697 O O . ALA A 210 ? 0.2569 0.2696 0.2576 0.0023 0.0144 -0.0272 264 ALA A O 1698 C CB . ALA A 210 ? 0.2230 0.2395 0.2195 0.0010 0.0147 -0.0285 264 ALA A CB 1699 N N . GLY A 211 ? 0.2515 0.2660 0.2527 0.0030 0.0150 -0.0289 265 GLY A N 1700 C CA . GLY A 211 ? 0.2560 0.2688 0.2591 0.0038 0.0151 -0.0293 265 GLY A CA 1701 C C . GLY A 211 ? 0.2493 0.2623 0.2534 0.0036 0.0145 -0.0308 265 GLY A C 1702 O O . GLY A 211 ? 0.2841 0.2986 0.2868 0.0033 0.0143 -0.0320 265 GLY A O 1703 N N . ASP A 212 ? 0.2435 0.2549 0.2503 0.0038 0.0143 -0.0306 266 ASP A N 1704 C CA . ASP A 212 ? 0.2456 0.2568 0.2542 0.0037 0.0132 -0.0323 266 ASP A CA 1705 C C . ASP A 212 ? 0.2456 0.2577 0.2517 0.0031 0.0121 -0.0331 266 ASP A C 1706 O O . ASP A 212 ? 0.2308 0.2428 0.2363 0.0025 0.0120 -0.0319 266 ASP A O 1707 C CB . ASP A 212 ? 0.2386 0.2479 0.2516 0.0037 0.0132 -0.0314 266 ASP A CB 1708 C CG . ASP A 212 ? 0.2648 0.2736 0.2808 0.0035 0.0114 -0.0332 266 ASP A CG 1709 O OD1 . ASP A 212 ? 0.2580 0.2673 0.2738 0.0040 0.0104 -0.0353 266 ASP A OD1 1710 O OD2 . ASP A 212 ? 0.2592 0.2673 0.2781 0.0030 0.0109 -0.0325 266 ASP A OD2 1711 N N . PRO A 213 ? 0.2705 0.2834 0.2749 0.0037 0.0114 -0.0351 267 PRO A N 1712 C CA . PRO A 213 ? 0.2957 0.3091 0.2965 0.0037 0.0106 -0.0358 267 PRO A CA 1713 C C . PRO A 213 ? 0.2802 0.2922 0.2823 0.0034 0.0088 -0.0360 267 PRO A C 1714 O O . PRO A 213 ? 0.2972 0.3093 0.2962 0.0033 0.0082 -0.0359 267 PRO A O 1715 C CB . PRO A 213 ? 0.3077 0.3211 0.3073 0.0050 0.0099 -0.0383 267 PRO A CB 1716 C CG . PRO A 213 ? 0.3314 0.3456 0.3326 0.0053 0.0111 -0.0384 267 PRO A CG 1717 C CD . PRO A 213 ? 0.2817 0.2950 0.2868 0.0046 0.0116 -0.0367 267 PRO A CD 1718 N N . LEU A 214 ? 0.2645 0.2753 0.2717 0.0033 0.0079 -0.0363 268 LEU A N 1719 C CA . LEU A 214 ? 0.2616 0.2712 0.2715 0.0031 0.0060 -0.0368 268 LEU A CA 1720 C C . LEU A 214 ? 0.2544 0.2637 0.2663 0.0021 0.0068 -0.0344 268 LEU A C 1721 O O . LEU A 214 ? 0.2544 0.2630 0.2681 0.0019 0.0051 -0.0347 268 LEU A O 1722 C CB . LEU A 214 ? 0.2655 0.2738 0.2811 0.0036 0.0043 -0.0385 268 LEU A CB 1723 C CG . LEU A 214 ? 0.2868 0.2950 0.3006 0.0049 0.0031 -0.0412 268 LEU A CG 1724 C CD1 . LEU A 214 ? 0.3181 0.3247 0.3388 0.0052 0.0009 -0.0429 268 LEU A CD1 1725 C CD2 . LEU A 214 ? 0.3327 0.3409 0.3403 0.0059 0.0016 -0.0429 268 LEU A CD2 1726 N N . THR A 215 ? 0.2390 0.2487 0.2502 0.0018 0.0091 -0.0321 269 THR A N 1727 C CA . THR A 215 ? 0.2350 0.2442 0.2479 0.0013 0.0100 -0.0298 269 THR A CA 1728 C C . THR A 215 ? 0.2344 0.2442 0.2429 0.0011 0.0114 -0.0281 269 THR A C 1729 O O . THR A 215 ? 0.2407 0.2497 0.2499 0.0014 0.0129 -0.0262 269 THR A O 1730 C CB . THR A 215 ? 0.2221 0.2298 0.2401 0.0017 0.0115 -0.0285 269 THR A CB 1731 O OG1 . THR A 215 ? 0.2141 0.2219 0.2307 0.0023 0.0128 -0.0284 269 THR A OG1 1732 C CG2 . THR A 215 ? 0.2455 0.2524 0.2698 0.0017 0.0099 -0.0301 269 THR A CG2 1733 N N . PRO A 216 ? 0.2502 0.2612 0.2545 0.0008 0.0109 -0.0286 270 PRO A N 1734 C CA . PRO A 216 ? 0.2488 0.2604 0.2500 0.0006 0.0120 -0.0271 270 PRO A CA 1735 C C . PRO A 216 ? 0.2562 0.2670 0.2577 0.0003 0.0122 -0.0252 270 PRO A C 1736 O O . PRO A 216 ? 0.2544 0.2648 0.2563 0.0000 0.0113 -0.0251 270 PRO A O 1737 C CB . PRO A 216 ? 0.2527 0.2656 0.2501 0.0003 0.0115 -0.0279 270 PRO A CB 1738 C CG . PRO A 216 ? 0.2626 0.2748 0.2601 0.0004 0.0098 -0.0294 270 PRO A CG 1739 C CD . PRO A 216 ? 0.2522 0.2636 0.2541 0.0009 0.0094 -0.0305 270 PRO A CD 1740 N N . GLY A 217 ? 0.2514 0.2614 0.2526 0.0009 0.0133 -0.0238 271 GLY A N 1741 C CA . GLY A 217 ? 0.2435 0.2524 0.2442 0.0012 0.0136 -0.0219 271 GLY A CA 1742 C C . GLY A 217 ? 0.2518 0.2588 0.2555 0.0022 0.0148 -0.0207 271 GLY A C 1743 O O . GLY A 217 ? 0.2629 0.2687 0.2658 0.0031 0.0156 -0.0190 271 GLY A O 1744 N N . TYR A 218 ? 0.2330 0.2398 0.2406 0.0022 0.0150 -0.0215 272 TYR A N 1745 C CA . TYR A 218 ? 0.2436 0.2488 0.2553 0.0029 0.0164 -0.0200 272 TYR A CA 1746 C C . TYR A 218 ? 0.2230 0.2274 0.2376 0.0036 0.0173 -0.0205 272 TYR A C 1747 O O . TYR A 218 ? 0.2318 0.2373 0.2465 0.0030 0.0161 -0.0225 272 TYR A O 1748 C CB . TYR A 218 ? 0.2341 0.2396 0.2499 0.0020 0.0155 -0.0203 272 TYR A CB 1749 C CG . TYR A 218 ? 0.2473 0.2536 0.2600 0.0013 0.0144 -0.0201 272 TYR A CG 1750 C CD1 . TYR A 218 ? 0.2271 0.2323 0.2389 0.0020 0.0155 -0.0180 272 TYR A CD1 1751 C CD2 . TYR A 218 ? 0.2484 0.2560 0.2583 0.0004 0.0123 -0.0219 272 TYR A CD2 1752 C CE1 . TYR A 218 ? 0.2236 0.2294 0.2326 0.0014 0.0143 -0.0179 272 TYR A CE1 1753 C CE2 . TYR A 218 ? 0.2337 0.2417 0.2404 -0.0001 0.0114 -0.0215 272 TYR A CE2 1754 C CZ . TYR A 218 ? 0.2252 0.2323 0.2317 0.0002 0.0123 -0.0196 272 TYR A CZ 1755 O OH . TYR A 218 ? 0.2261 0.2336 0.2297 -0.0002 0.0113 -0.0193 272 TYR A OH 1756 N N . PRO A 219 ? 0.2477 0.2501 0.2643 0.0049 0.0195 -0.0185 273 PRO A N 1757 C CA . PRO A 219 ? 0.2538 0.2552 0.2729 0.0056 0.0204 -0.0188 273 PRO A CA 1758 C C . PRO A 219 ? 0.2585 0.2605 0.2840 0.0045 0.0194 -0.0202 273 PRO A C 1759 O O . PRO A 219 ? 0.2432 0.2453 0.2733 0.0038 0.0191 -0.0199 273 PRO A O 1760 C CB . PRO A 219 ? 0.2524 0.2510 0.2722 0.0076 0.0234 -0.0158 273 PRO A CB 1761 C CG . PRO A 219 ? 0.2588 0.2572 0.2796 0.0074 0.0240 -0.0142 273 PRO A CG 1762 C CD . PRO A 219 ? 0.2592 0.2598 0.2754 0.0062 0.0214 -0.0159 273 PRO A CD 1763 N N . ALA A 220 ? 0.2358 0.2381 0.2619 0.0045 0.0186 -0.0220 274 ALA A N 1764 C CA . ALA A 220 ? 0.2486 0.2512 0.2807 0.0038 0.0172 -0.0238 274 ALA A CA 1765 C C . ALA A 220 ? 0.2491 0.2496 0.2880 0.0044 0.0194 -0.0219 274 ALA A C 1766 O O . ALA A 220 ? 0.2533 0.2528 0.2951 0.0049 0.0197 -0.0223 274 ALA A O 1767 C CB . ALA A 220 ? 0.2569 0.2602 0.2868 0.0039 0.0160 -0.0261 274 ALA A CB 1768 N N . ASN A 221 ? 0.2656 0.2654 0.3077 0.0045 0.0208 -0.0197 275 ASN A N 1769 C CA . ASN A 221 ? 0.2816 0.2793 0.3302 0.0053 0.0237 -0.0170 275 ASN A CA 1770 C C . ASN A 221 ? 0.3022 0.3003 0.3606 0.0040 0.0220 -0.0185 275 ASN A C 1771 O O . ASN A 221 ? 0.2760 0.2756 0.3344 0.0030 0.0184 -0.0217 275 ASN A O 1772 C CB . ASN A 221 ? 0.3002 0.2968 0.3474 0.0062 0.0265 -0.0139 275 ASN A CB 1773 C CG . ASN A 221 ? 0.2973 0.2957 0.3459 0.0049 0.0247 -0.0145 275 ASN A CG 1774 O OD1 . ASN A 221 ? 0.3264 0.3260 0.3796 0.0035 0.0219 -0.0168 275 ASN A OD1 1775 N ND2 . ASN A 221 ? 0.3527 0.3508 0.3967 0.0057 0.0260 -0.0127 275 ASN A ND2 1776 N N A GLU A 222 ? 0.3079 0.3045 0.3743 0.0044 0.0246 -0.0160 276 GLU A N 1777 N N B GLU A 222 ? 0.3138 0.3104 0.3806 0.0043 0.0244 -0.0162 276 GLU A N 1778 C CA A GLU A 222 ? 0.3263 0.3229 0.4040 0.0034 0.0233 -0.0170 276 GLU A CA 1779 C CA B GLU A 222 ? 0.3308 0.3277 0.4077 0.0032 0.0221 -0.0181 276 GLU A CA 1780 C C A GLU A 222 ? 0.3282 0.3264 0.4095 0.0020 0.0198 -0.0192 276 GLU A C 1781 C C B GLU A 222 ? 0.3324 0.3310 0.4119 0.0019 0.0189 -0.0200 276 GLU A C 1782 O O A GLU A 222 ? 0.3338 0.3323 0.4233 0.0012 0.0169 -0.0215 276 GLU A O 1783 O O B GLU A 222 ? 0.3475 0.3466 0.4320 0.0011 0.0152 -0.0231 276 GLU A O 1784 C CB A GLU A 222 ? 0.3287 0.3232 0.4146 0.0042 0.0277 -0.0131 276 GLU A CB 1785 C CB B GLU A 222 ? 0.3458 0.3407 0.4328 0.0037 0.0255 -0.0152 276 GLU A CB 1786 C CG A GLU A 222 ? 0.3762 0.3695 0.4719 0.0040 0.0278 -0.0134 276 GLU A CG 1787 C CG B GLU A 222 ? 0.3987 0.3919 0.4859 0.0045 0.0267 -0.0150 276 GLU A CG 1788 C CD A GLU A 222 ? 0.4298 0.4215 0.5203 0.0052 0.0293 -0.0129 276 GLU A CD 1789 C CD B GLU A 222 ? 0.4445 0.4378 0.5411 0.0035 0.0237 -0.0177 276 GLU A CD 1790 O OE1 A GLU A 222 ? 0.4592 0.4492 0.5432 0.0069 0.0329 -0.0100 276 GLU A OE1 1791 O OE1 B GLU A 222 ? 0.4286 0.4232 0.5295 0.0023 0.0197 -0.0207 276 GLU A OE1 1792 O OE2 A GLU A 222 ? 0.4340 0.4259 0.5265 0.0047 0.0266 -0.0157 276 GLU A OE2 1793 O OE2 B GLU A 222 ? 0.4912 0.4827 0.5904 0.0041 0.0252 -0.0170 276 GLU A OE2 1794 N N . TYR A 223 ? 0.3150 0.3142 0.3910 0.0020 0.0200 -0.0185 277 TYR A N 1795 C CA . TYR A 223 ? 0.3286 0.3291 0.4075 0.0009 0.0168 -0.0202 277 TYR A CA 1796 C C . TYR A 223 ? 0.3255 0.3275 0.3949 0.0006 0.0138 -0.0227 277 TYR A C 1797 O O . TYR A 223 ? 0.3371 0.3398 0.4066 0.0000 0.0116 -0.0237 277 TYR A O 1798 C CB . TYR A 223 ? 0.3389 0.3392 0.4226 0.0011 0.0195 -0.0172 277 TYR A CB 1799 C CG . TYR A 223 ? 0.3109 0.3106 0.3862 0.0022 0.0229 -0.0142 277 TYR A CG 1800 C CD1 . TYR A 223 ? 0.3473 0.3482 0.4145 0.0020 0.0214 -0.0149 277 TYR A CD1 1801 C CD2 . TYR A 223 ? 0.3136 0.3113 0.3886 0.0038 0.0276 -0.0108 277 TYR A CD2 1802 C CE1 . TYR A 223 ? 0.3644 0.3646 0.4237 0.0032 0.0240 -0.0126 277 TYR A CE1 1803 C CE2 . TYR A 223 ? 0.3538 0.3506 0.4202 0.0054 0.0301 -0.0084 277 TYR A CE2 1804 C CZ . TYR A 223 ? 0.3813 0.3794 0.4401 0.0050 0.0281 -0.0095 277 TYR A CZ 1805 O OH . TYR A 223 ? 0.4036 0.4007 0.4543 0.0066 0.0301 -0.0075 277 TYR A OH 1806 N N . ALA A 224 ? 0.3163 0.3185 0.3777 0.0010 0.0137 -0.0236 278 ALA A N 1807 C CA . ALA A 224 ? 0.3351 0.3385 0.3873 0.0008 0.0117 -0.0253 278 ALA A CA 1808 C C . ALA A 224 ? 0.3449 0.3489 0.3983 0.0003 0.0074 -0.0287 278 ALA A C 1809 O O . ALA A 224 ? 0.3533 0.3567 0.4131 0.0003 0.0054 -0.0307 278 ALA A O 1810 C CB . ALA A 224 ? 0.3410 0.3446 0.3864 0.0013 0.0123 -0.0259 278 ALA A CB 1811 N N . TYR A 225 ? 0.3395 0.3443 0.3869 0.0001 0.0058 -0.0295 279 TYR A N 1812 C CA . TYR A 225 ? 0.3526 0.3575 0.3984 0.0002 0.0016 -0.0329 279 TYR A CA 1813 C C . TYR A 225 ? 0.3584 0.3639 0.3957 0.0007 0.0015 -0.0341 279 TYR A C 1814 O O . TYR A 225 ? 0.3733 0.3796 0.4046 0.0006 0.0038 -0.0324 279 TYR A O 1815 C CB . TYR A 225 ? 0.3625 0.3677 0.4069 0.0000 -0.0001 -0.0331 279 TYR A CB 1816 C CG A TYR A 225 ? 0.3284 0.3330 0.3720 0.0006 -0.0047 -0.0367 279 TYR A CG 1817 C CG B TYR A 225 ? 0.3843 0.3897 0.4194 0.0005 -0.0024 -0.0352 279 TYR A CG 1818 C CD1 A TYR A 225 ? 0.3318 0.3353 0.3839 0.0008 -0.0077 -0.0388 279 TYR A CD1 1819 C CD1 B TYR A 225 ? 0.3957 0.4002 0.4306 0.0012 -0.0065 -0.0382 279 TYR A CD1 1820 C CD2 A TYR A 225 ? 0.3388 0.3435 0.3729 0.0012 -0.0060 -0.0380 279 TYR A CD2 1821 C CD2 B TYR A 225 ? 0.4017 0.4079 0.4286 0.0005 -0.0004 -0.0342 279 TYR A CD2 1822 C CE1 A TYR A 225 ? 0.3575 0.3599 0.4081 0.0019 -0.0124 -0.0425 279 TYR A CE1 1823 C CE1 B TYR A 225 ? 0.3991 0.4033 0.4248 0.0022 -0.0081 -0.0398 279 TYR A CE1 1824 C CE2 A TYR A 225 ? 0.3701 0.3735 0.4020 0.0024 -0.0101 -0.0413 279 TYR A CE2 1825 C CE2 B TYR A 225 ? 0.4124 0.4188 0.4314 0.0012 -0.0018 -0.0357 279 TYR A CE2 1826 C CZ A TYR A 225 ? 0.3757 0.3780 0.4156 0.0029 -0.0135 -0.0437 279 TYR A CZ 1827 C CZ B TYR A 225 ? 0.4303 0.4355 0.4483 0.0021 -0.0054 -0.0383 279 TYR A CZ 1828 O OH A TYR A 225 ? 0.4407 0.4413 0.4778 0.0046 -0.0181 -0.0473 279 TYR A OH 1829 O OH B TYR A 225 ? 0.4204 0.4253 0.4298 0.0031 -0.0063 -0.0394 279 TYR A OH 1830 N N . ARG A 226 ? 0.3336 0.3387 0.3708 0.0014 -0.0008 -0.0370 280 ARG A N 1831 C CA . ARG A 226 ? 0.3464 0.3521 0.3759 0.0021 -0.0005 -0.0380 280 ARG A CA 1832 C C . ARG A 226 ? 0.3769 0.3824 0.4000 0.0030 -0.0031 -0.0402 280 ARG A C 1833 O O . ARG A 226 ? 0.3762 0.3805 0.4016 0.0036 -0.0064 -0.0424 280 ARG A O 1834 C CB . ARG A 226 ? 0.3385 0.3436 0.3712 0.0027 -0.0010 -0.0396 280 ARG A CB 1835 C CG . ARG A 226 ? 0.3297 0.3347 0.3675 0.0021 0.0020 -0.0371 280 ARG A CG 1836 C CD . ARG A 226 ? 0.3622 0.3665 0.4028 0.0028 0.0016 -0.0387 280 ARG A CD 1837 N NE . ARG A 226 ? 0.3808 0.3848 0.4235 0.0025 0.0051 -0.0358 280 ARG A NE 1838 C CZ . ARG A 226 ? 0.4250 0.4280 0.4748 0.0022 0.0067 -0.0337 280 ARG A CZ 1839 N NH1 . ARG A 226 ? 0.4487 0.4512 0.5059 0.0017 0.0050 -0.0342 280 ARG A NH1 1840 N NH2 . ARG A 226 ? 0.3661 0.3684 0.4159 0.0025 0.0101 -0.0310 280 ARG A NH2 1841 N N . ARG A 227 ? 0.3652 0.3717 0.3805 0.0032 -0.0016 -0.0396 281 ARG A N 1842 C CA . ARG A 227 ? 0.3994 0.4055 0.4077 0.0046 -0.0034 -0.0416 281 ARG A CA 1843 C C . ARG A 227 ? 0.4097 0.4146 0.4185 0.0062 -0.0057 -0.0448 281 ARG A C 1844 O O . ARG A 227 ? 0.4026 0.4077 0.4152 0.0060 -0.0049 -0.0450 281 ARG A O 1845 C CB . ARG A 227 ? 0.3775 0.3849 0.3790 0.0045 -0.0005 -0.0401 281 ARG A CB 1846 C CG . ARG A 227 ? 0.3776 0.3860 0.3784 0.0031 0.0013 -0.0372 281 ARG A CG 1847 C CD . ARG A 227 ? 0.4348 0.4444 0.4294 0.0031 0.0036 -0.0360 281 ARG A CD 1848 N NE . ARG A 227 ? 0.4242 0.4342 0.4174 0.0021 0.0044 -0.0338 281 ARG A NE 1849 C CZ . ARG A 227 ? 0.4794 0.4903 0.4682 0.0018 0.0061 -0.0324 281 ARG A CZ 1850 N NH1 . ARG A 227 ? 0.4711 0.4827 0.4566 0.0026 0.0074 -0.0328 281 ARG A NH1 1851 N NH2 . ARG A 227 ? 0.4960 0.5068 0.4840 0.0009 0.0064 -0.0306 281 ARG A NH2 1852 N N . GLY A 228 ? 0.4355 0.4387 0.4401 0.0080 -0.0088 -0.0473 282 GLY A N 1853 C CA . GLY A 228 ? 0.4691 0.4710 0.4716 0.0101 -0.0111 -0.0505 282 GLY A CA 1854 C C . GLY A 228 ? 0.4874 0.4906 0.4838 0.0107 -0.0080 -0.0498 282 GLY A C 1855 O O . GLY A 228 ? 0.4835 0.4883 0.4757 0.0099 -0.0049 -0.0473 282 GLY A O 1856 N N . ILE A 229 ? 0.5137 0.5164 0.5101 0.0121 -0.0088 -0.0519 283 ILE A N 1857 C CA . ILE A 229 ? 0.5384 0.5423 0.5293 0.0130 -0.0059 -0.0515 283 ILE A CA 1858 C C . ILE A 229 ? 0.5455 0.5494 0.5274 0.0143 -0.0046 -0.0508 283 ILE A C 1859 O O . ILE A 229 ? 0.5504 0.5563 0.5296 0.0137 -0.0009 -0.0487 283 ILE A O 1860 C CB . ILE A 229 ? 0.5478 0.5506 0.5388 0.0150 -0.0077 -0.0545 283 ILE A CB 1861 C CG1 . ILE A 229 ? 0.5569 0.5603 0.5563 0.0135 -0.0073 -0.0543 283 ILE A CG1 1862 C CG2 . ILE A 229 ? 0.5696 0.5734 0.5534 0.0166 -0.0049 -0.0544 283 ILE A CG2 1863 C CD1 . ILE A 229 ? 0.5187 0.5246 0.5182 0.0120 -0.0031 -0.0516 283 ILE A CD1 1864 N N . ALA A 230 ? 0.5620 0.5635 0.5397 0.0162 -0.0075 -0.0525 284 ALA A N 1865 C CA . ALA A 230 ? 0.5734 0.5744 0.5422 0.0177 -0.0060 -0.0516 284 ALA A CA 1866 C C . ALA A 230 ? 0.5700 0.5731 0.5387 0.0153 -0.0026 -0.0478 284 ALA A C 1867 O O . ALA A 230 ? 0.5777 0.5816 0.5409 0.0158 0.0004 -0.0462 284 ALA A O 1868 C CB . ALA A 230 ? 0.5881 0.5856 0.5523 0.0204 -0.0102 -0.0541 284 ALA A CB 1869 N N . GLU A 231 ? 0.5602 0.5641 0.5353 0.0128 -0.0031 -0.0466 285 GLU A N 1870 C CA . GLU A 231 ? 0.5594 0.5650 0.5348 0.0106 -0.0005 -0.0433 285 GLU A CA 1871 C C . GLU A 231 ? 0.5464 0.5546 0.5262 0.0085 0.0026 -0.0411 285 GLU A C 1872 O O . GLU A 231 ? 0.5500 0.5594 0.5306 0.0068 0.0045 -0.0386 285 GLU A O 1873 C CB . GLU A 231 ? 0.5670 0.5719 0.5463 0.0093 -0.0027 -0.0429 285 GLU A CB 1874 C CG . GLU A 231 ? 0.6314 0.6341 0.6055 0.0109 -0.0050 -0.0438 285 GLU A CG 1875 C CD . GLU A 231 ? 0.7111 0.7109 0.6836 0.0136 -0.0093 -0.0476 285 GLU A CD 1876 O OE1 . GLU A 231 ? 0.7646 0.7621 0.7305 0.0157 -0.0111 -0.0486 285 GLU A OE1 1877 O OE2 . GLU A 231 ? 0.7285 0.7281 0.7062 0.0138 -0.0110 -0.0496 285 GLU A OE2 1878 N N . ALA A 232 ? 0.5322 0.5409 0.5146 0.0088 0.0029 -0.0423 286 ALA A N 1879 C CA . ALA A 232 ? 0.5192 0.5298 0.5060 0.0072 0.0052 -0.0407 286 ALA A CA 1880 C C . ALA A 232 ? 0.5158 0.5283 0.4997 0.0066 0.0085 -0.0384 286 ALA A C 1881 O O . ALA A 232 ? 0.4991 0.5116 0.4778 0.0077 0.0095 -0.0383 286 ALA A O 1882 C CB . ALA A 232 ? 0.5031 0.5136 0.4926 0.0080 0.0048 -0.0425 286 ALA A CB 1883 N N . VAL A 233 ? 0.5053 0.5192 0.4929 0.0051 0.0101 -0.0367 287 VAL A N 1884 C CA . VAL A 233 ? 0.5045 0.5201 0.4908 0.0044 0.0126 -0.0347 287 VAL A CA 1885 C C . VAL A 233 ? 0.4827 0.4997 0.4693 0.0052 0.0142 -0.0355 287 VAL A C 1886 O O . VAL A 233 ? 0.4982 0.5151 0.4880 0.0053 0.0137 -0.0364 287 VAL A O 1887 C CB . VAL A 233 ? 0.4901 0.5063 0.4799 0.0028 0.0132 -0.0326 287 VAL A CB 1888 C CG1 . VAL A 233 ? 0.4975 0.5155 0.4873 0.0023 0.0154 -0.0312 287 VAL A CG1 1889 C CG2 . VAL A 233 ? 0.5271 0.5422 0.5163 0.0020 0.0122 -0.0315 287 VAL A CG2 1890 N N . GLY A 234 ? 0.4749 0.4929 0.4582 0.0060 0.0161 -0.0351 288 GLY A N 1891 C CA . GLY A 234 ? 0.4464 0.4662 0.4312 0.0064 0.0181 -0.0353 288 GLY A CA 1892 C C . GLY A 234 ? 0.4404 0.4600 0.4242 0.0082 0.0180 -0.0375 288 GLY A C 1893 O O . GLY A 234 ? 0.4158 0.4372 0.4016 0.0085 0.0197 -0.0375 288 GLY A O 1894 N N . LEU A 235 ? 0.4174 0.4351 0.3986 0.0096 0.0159 -0.0395 289 LEU A N 1895 C CA . LEU A 235 ? 0.4260 0.4431 0.4061 0.0116 0.0153 -0.0419 289 LEU A CA 1896 C C . LEU A 235 ? 0.4345 0.4522 0.4096 0.0136 0.0177 -0.0419 289 LEU A C 1897 O O . LEU A 235 ? 0.4285 0.4457 0.3992 0.0142 0.0188 -0.0407 289 LEU A O 1898 C CB . LEU A 235 ? 0.4223 0.4368 0.4018 0.0127 0.0118 -0.0444 289 LEU A CB 1899 C CG . LEU A 235 ? 0.4245 0.4382 0.4095 0.0109 0.0096 -0.0442 289 LEU A CG 1900 C CD1 . LEU A 235 ? 0.4219 0.4331 0.4074 0.0121 0.0060 -0.0468 289 LEU A CD1 1901 C CD2 . LEU A 235 ? 0.4307 0.4455 0.4211 0.0098 0.0105 -0.0437 289 LEU A CD2 1902 N N . PRO A 236 ? 0.4451 0.4638 0.4208 0.0149 0.0189 -0.0431 290 PRO A N 1903 C CA . PRO A 236 ? 0.4495 0.4688 0.4204 0.0171 0.0217 -0.0429 290 PRO A CA 1904 C C . PRO A 236 ? 0.4479 0.4642 0.4119 0.0202 0.0198 -0.0450 290 PRO A C 1905 O O . PRO A 236 ? 0.4292 0.4433 0.3936 0.0206 0.0161 -0.0474 290 PRO A O 1906 C CB . PRO A 236 ? 0.4558 0.4769 0.4302 0.0176 0.0230 -0.0438 290 PRO A CB 1907 C CG . PRO A 236 ? 0.4762 0.4964 0.4548 0.0166 0.0198 -0.0455 290 PRO A CG 1908 C CD . PRO A 236 ? 0.4356 0.4551 0.4165 0.0143 0.0182 -0.0441 290 PRO A CD 1909 N N . SER A 237 ? 0.4692 0.4850 0.4269 0.0224 0.0224 -0.0441 291 SER A N 1910 C CA A SER A 237 ? 0.4797 0.4920 0.4292 0.0258 0.0207 -0.0459 291 SER A CA 1911 C CA B SER A 237 ? 0.4825 0.4948 0.4322 0.0258 0.0205 -0.0461 291 SER A CA 1912 C C . SER A 237 ? 0.4936 0.5050 0.4385 0.0296 0.0216 -0.0479 291 SER A C 1913 O O . SER A 237 ? 0.4931 0.5012 0.4308 0.0331 0.0196 -0.0501 291 SER A O 1914 C CB A SER A 237 ? 0.4869 0.4983 0.4309 0.0265 0.0228 -0.0435 291 SER A CB 1915 C CB B SER A 237 ? 0.4895 0.5005 0.4336 0.0264 0.0220 -0.0439 291 SER A CB 1916 O OG A SER A 237 ? 0.4848 0.4986 0.4292 0.0263 0.0281 -0.0406 291 SER A OG 1917 O OG B SER A 237 ? 0.5039 0.5140 0.4502 0.0243 0.0189 -0.0438 291 SER A OG 1918 N N . ILE A 238 ? 0.4859 0.5002 0.4347 0.0291 0.0246 -0.0473 292 ILE A N 1919 C CA . ILE A 238 ? 0.5056 0.5196 0.4509 0.0325 0.0260 -0.0490 292 ILE A CA 1920 C C . ILE A 238 ? 0.4918 0.5075 0.4440 0.0312 0.0247 -0.0506 292 ILE A C 1921 O O . ILE A 238 ? 0.4897 0.5079 0.4494 0.0277 0.0249 -0.0493 292 ILE A O 1922 C CB . ILE A 238 ? 0.5011 0.5170 0.4440 0.0339 0.0320 -0.0461 292 ILE A CB 1923 C CG1 . ILE A 238 ? 0.4962 0.5163 0.4480 0.0300 0.0349 -0.0432 292 ILE A CG1 1924 C CG2 . ILE A 238 ? 0.5274 0.5407 0.4617 0.0362 0.0336 -0.0445 292 ILE A CG2 1925 C CD1 . ILE A 238 ? 0.5351 0.5572 0.4867 0.0308 0.0408 -0.0400 292 ILE A CD1 1926 N N . PRO A 239 ? 0.4879 0.5021 0.4374 0.0341 0.0232 -0.0536 293 PRO A N 1927 C CA . PRO A 239 ? 0.4699 0.4854 0.4253 0.0333 0.0220 -0.0554 293 PRO A CA 1928 C C . PRO A 239 ? 0.4559 0.4753 0.4164 0.0319 0.0263 -0.0533 293 PRO A C 1929 O O . PRO A 239 ? 0.4524 0.4733 0.4104 0.0331 0.0307 -0.0512 293 PRO A O 1930 C CB . PRO A 239 ? 0.4901 0.5029 0.4395 0.0376 0.0202 -0.0587 293 PRO A CB 1931 C CG . PRO A 239 ? 0.4866 0.4956 0.4278 0.0402 0.0183 -0.0595 293 PRO A CG 1932 C CD . PRO A 239 ? 0.4994 0.5101 0.4393 0.0389 0.0224 -0.0557 293 PRO A CD 1933 N N . VAL A 240 ? 0.4213 0.4423 0.3892 0.0295 0.0250 -0.0537 294 VAL A N 1934 C CA . VAL A 240 ? 0.3932 0.4178 0.3673 0.0278 0.0280 -0.0521 294 VAL A CA 1935 C C . VAL A 240 ? 0.3739 0.3985 0.3523 0.0277 0.0258 -0.0543 294 VAL A C 1936 O O . VAL A 240 ? 0.3794 0.4019 0.3590 0.0271 0.0221 -0.0560 294 VAL A O 1937 C CB . VAL A 240 ? 0.3762 0.4025 0.3555 0.0241 0.0285 -0.0493 294 VAL A CB 1938 C CG1 . VAL A 240 ? 0.3349 0.3647 0.3206 0.0228 0.0313 -0.0478 294 VAL A CG1 1939 C CG2 . VAL A 240 ? 0.3770 0.4027 0.3521 0.0240 0.0300 -0.0471 294 VAL A CG2 1940 N N . HIS A 241 ? 0.3862 0.4133 0.3674 0.0284 0.0283 -0.0544 295 HIS A N 1941 C CA . HIS A 241 ? 0.3689 0.3961 0.3540 0.0286 0.0265 -0.0564 295 HIS A CA 1942 C C . HIS A 241 ? 0.3655 0.3962 0.3560 0.0280 0.0295 -0.0553 295 HIS A C 1943 O O . HIS A 241 ? 0.3618 0.3946 0.3517 0.0288 0.0334 -0.0537 295 HIS A O 1944 C CB . HIS A 241 ? 0.3975 0.4223 0.3775 0.0320 0.0249 -0.0596 295 HIS A CB 1945 C CG . HIS A 241 ? 0.3863 0.4103 0.3700 0.0321 0.0222 -0.0620 295 HIS A CG 1946 N ND1 . HIS A 241 ? 0.3726 0.3946 0.3596 0.0303 0.0184 -0.0628 295 HIS A ND1 1947 C CD2 . HIS A 241 ? 0.3957 0.4206 0.3806 0.0340 0.0228 -0.0637 295 HIS A CD2 1948 C CE1 . HIS A 241 ? 0.3772 0.3987 0.3670 0.0310 0.0169 -0.0648 295 HIS A CE1 1949 N NE2 . HIS A 241 ? 0.3891 0.4123 0.3775 0.0332 0.0193 -0.0655 295 HIS A NE2 1950 N N . PRO A 242 ? 0.3482 0.3793 0.3445 0.0264 0.0278 -0.0558 296 PRO A N 1951 C CA . PRO A 242 ? 0.3317 0.3660 0.3337 0.0259 0.0300 -0.0551 296 PRO A CA 1952 C C . PRO A 242 ? 0.3469 0.3814 0.3496 0.0281 0.0297 -0.0576 296 PRO A C 1953 O O . PRO A 242 ? 0.3400 0.3718 0.3406 0.0290 0.0268 -0.0598 296 PRO A O 1954 C CB . PRO A 242 ? 0.3375 0.3714 0.3445 0.0231 0.0277 -0.0543 296 PRO A CB 1955 C CG . PRO A 242 ? 0.3326 0.3631 0.3372 0.0231 0.0242 -0.0557 296 PRO A CG 1956 C CD . PRO A 242 ? 0.3289 0.3577 0.3272 0.0248 0.0240 -0.0567 296 PRO A CD 1957 N N . ILE A 243 ? 0.3506 0.3881 0.3568 0.0288 0.0327 -0.0572 297 ILE A N 1958 C CA . ILE A 243 ? 0.3570 0.3950 0.3643 0.0310 0.0327 -0.0595 297 ILE A CA 1959 C C . ILE A 243 ? 0.3519 0.3931 0.3670 0.0302 0.0341 -0.0589 297 ILE A C 1960 O O . ILE A 243 ? 0.3498 0.3931 0.3692 0.0282 0.0354 -0.0567 297 ILE A O 1961 C CB . ILE A 243 ? 0.3554 0.3936 0.3570 0.0345 0.0355 -0.0602 297 ILE A CB 1962 C CG1 . ILE A 243 ? 0.3528 0.3941 0.3559 0.0348 0.0406 -0.0575 297 ILE A CG1 1963 C CG2 . ILE A 243 ? 0.3708 0.4052 0.3642 0.0359 0.0333 -0.0614 297 ILE A CG2 1964 C CD1 . ILE A 243 ? 0.3450 0.3861 0.3414 0.0387 0.0441 -0.0577 297 ILE A CD1 1965 N N . GLY A 244 ? 0.3576 0.3992 0.3749 0.0316 0.0335 -0.0610 298 GLY A N 1966 C CA . GLY A 244 ? 0.3551 0.3997 0.3798 0.0313 0.0345 -0.0608 298 GLY A CA 1967 C C . GLY A 244 ? 0.3794 0.4275 0.4061 0.0331 0.0392 -0.0602 298 GLY A C 1968 O O . GLY A 244 ? 0.3712 0.4190 0.3923 0.0350 0.0418 -0.0597 298 GLY A O 1969 N N . TYR A 245 ? 0.3792 0.4303 0.4138 0.0328 0.0402 -0.0601 299 TYR A N 1970 C CA . TYR A 245 ? 0.3951 0.4498 0.4331 0.0344 0.0451 -0.0590 299 TYR A CA 1971 C C . TYR A 245 ? 0.4107 0.4656 0.4456 0.0379 0.0469 -0.0610 299 TYR A C 1972 O O . TYR A 245 ? 0.4093 0.4665 0.4443 0.0398 0.0517 -0.0597 299 TYR A O 1973 C CB . TYR A 245 ? 0.3841 0.4423 0.4328 0.0327 0.0461 -0.0579 299 TYR A CB 1974 C CG . TYR A 245 ? 0.3903 0.4488 0.4451 0.0325 0.0427 -0.0600 299 TYR A CG 1975 C CD1 . TYR A 245 ? 0.3745 0.4313 0.4318 0.0302 0.0385 -0.0601 299 TYR A CD1 1976 C CD2 . TYR A 245 ? 0.3982 0.4584 0.4563 0.0347 0.0437 -0.0619 299 TYR A CD2 1977 C CE1 . TYR A 245 ? 0.3570 0.4136 0.4192 0.0304 0.0353 -0.0621 299 TYR A CE1 1978 C CE2 . TYR A 245 ? 0.3900 0.4502 0.4536 0.0345 0.0402 -0.0639 299 TYR A CE2 1979 C CZ . TYR A 245 ? 0.3819 0.4401 0.4473 0.0324 0.0361 -0.0640 299 TYR A CZ 1980 O OH . TYR A 245 ? 0.3173 0.3749 0.3873 0.0327 0.0325 -0.0660 299 TYR A OH 1981 N N . TYR A 246 ? 0.4067 0.4592 0.4390 0.0389 0.0433 -0.0639 300 TYR A N 1982 C CA . TYR A 246 ? 0.4286 0.4805 0.4561 0.0426 0.0445 -0.0660 300 TYR A CA 1983 C C . TYR A 246 ? 0.4456 0.4954 0.4636 0.0446 0.0461 -0.0655 300 TYR A C 1984 O O . TYR A 246 ? 0.4477 0.4984 0.4624 0.0477 0.0501 -0.0652 300 TYR A O 1985 C CB . TYR A 246 ? 0.4128 0.4620 0.4390 0.0433 0.0399 -0.0692 300 TYR A CB 1986 C CG . TYR A 246 ? 0.4418 0.4927 0.4760 0.0426 0.0384 -0.0703 300 TYR A CG 1987 C CD1 . TYR A 246 ? 0.4080 0.4632 0.4504 0.0425 0.0415 -0.0692 300 TYR A CD1 1988 C CD2 . TYR A 246 ? 0.4389 0.4869 0.4729 0.0423 0.0338 -0.0726 300 TYR A CD2 1989 C CE1 . TYR A 246 ? 0.4277 0.4841 0.4773 0.0422 0.0396 -0.0706 300 TYR A CE1 1990 C CE2 . TYR A 246 ? 0.4215 0.4705 0.4620 0.0421 0.0322 -0.0737 300 TYR A CE2 1991 C CZ . TYR A 246 ? 0.4468 0.5000 0.4949 0.0421 0.0349 -0.0729 300 TYR A CZ 1992 O OH . TYR A 246 ? 0.4696 0.5235 0.5240 0.0421 0.0328 -0.0743 300 TYR A OH 1993 N N . ASP A 247 ? 0.4373 0.4839 0.4507 0.0430 0.0430 -0.0654 301 ASP A N 1994 C CA . ASP A 247 ? 0.4503 0.4943 0.4545 0.0448 0.0436 -0.0651 301 ASP A CA 1995 C C . ASP A 247 ? 0.4568 0.5028 0.4603 0.0449 0.0487 -0.0618 301 ASP A C 1996 O O . ASP A 247 ? 0.4671 0.5121 0.4635 0.0482 0.0515 -0.0615 301 ASP A O 1997 C CB . ASP A 247 ? 0.4401 0.4803 0.4407 0.0430 0.0388 -0.0659 301 ASP A CB 1998 C CG . ASP A 247 ? 0.4689 0.5062 0.4680 0.0441 0.0344 -0.0693 301 ASP A CG 1999 O OD1 . ASP A 247 ? 0.4821 0.5198 0.4803 0.0470 0.0352 -0.0712 301 ASP A OD1 2000 O OD2 . ASP A 247 ? 0.4187 0.4534 0.4179 0.0421 0.0303 -0.0699 301 ASP A OD2 2001 N N . ALA A 248 ? 0.4421 0.4906 0.4528 0.0416 0.0496 -0.0593 302 ALA A N 2002 C CA . ALA A 248 ? 0.4535 0.5043 0.4655 0.0413 0.0547 -0.0558 302 ALA A CA 2003 C C . ALA A 248 ? 0.4686 0.5222 0.4823 0.0444 0.0604 -0.0550 302 ALA A C 2004 O O . ALA A 248 ? 0.4596 0.5134 0.4693 0.0463 0.0650 -0.0527 302 ALA A O 2005 C CB . ALA A 248 ? 0.4400 0.4931 0.4607 0.0374 0.0543 -0.0538 302 ALA A CB 2006 N N . GLN A 249 ? 0.4741 0.5298 0.4939 0.0450 0.0602 -0.0567 303 GLN A N 2007 C CA . GLN A 249 ? 0.5001 0.5587 0.5222 0.0481 0.0658 -0.0559 303 GLN A CA 2008 C C . GLN A 249 ? 0.5145 0.5703 0.5250 0.0528 0.0679 -0.0567 303 GLN A C 2009 O O . GLN A 249 ? 0.5296 0.5864 0.5378 0.0554 0.0739 -0.0543 303 GLN A O 2010 C CB . GLN A 249 ? 0.4987 0.5597 0.5289 0.0481 0.0646 -0.0581 303 GLN A CB 2011 C CG . GLN A 249 ? 0.5500 0.6139 0.5825 0.0516 0.0703 -0.0576 303 GLN A CG 2012 C CD . GLN A 249 ? 0.5954 0.6637 0.6413 0.0503 0.0712 -0.0576 303 GLN A CD 2013 O OE1 . GLN A 249 ? 0.6032 0.6728 0.6572 0.0467 0.0685 -0.0572 303 GLN A OE1 2014 N NE2 . GLN A 249 ? 0.6117 0.6821 0.6597 0.0534 0.0748 -0.0582 303 GLN A NE2 2015 N N . LYS A 250 ? 0.5207 0.5726 0.5236 0.0540 0.0630 -0.0599 304 LYS A N 2016 C CA . LYS A 250 ? 0.5415 0.5900 0.5328 0.0587 0.0638 -0.0613 304 LYS A CA 2017 C C . LYS A 250 ? 0.5615 0.6080 0.5450 0.0598 0.0665 -0.0588 304 LYS A C 2018 O O . LYS A 250 ? 0.5684 0.6135 0.5439 0.0644 0.0703 -0.0583 304 LYS A O 2019 C CB . LYS A 250 ? 0.5365 0.5811 0.5227 0.0593 0.0573 -0.0654 304 LYS A CB 2020 C CG . LYS A 250 ? 0.5591 0.6049 0.5513 0.0591 0.0549 -0.0681 304 LYS A CG 2021 C CD . LYS A 250 ? 0.6083 0.6552 0.5982 0.0639 0.0588 -0.0690 304 LYS A CD 2022 C CE . LYS A 250 ? 0.6377 0.6850 0.6321 0.0643 0.0557 -0.0723 304 LYS A CE 2023 N NZ . LYS A 250 ? 0.6892 0.7374 0.6812 0.0691 0.0594 -0.0734 304 LYS A NZ 2024 N N . LEU A 251 ? 0.5491 0.5952 0.5342 0.0560 0.0645 -0.0571 305 LEU A N 2025 C CA . LEU A 251 ? 0.5594 0.6035 0.5375 0.0568 0.0668 -0.0546 305 LEU A CA 2026 C C . LEU A 251 ? 0.5622 0.6097 0.5447 0.0568 0.0740 -0.0503 305 LEU A C 2027 O O . LEU A 251 ? 0.5823 0.6279 0.5572 0.0593 0.0776 -0.0481 305 LEU A O 2028 C CB . LEU A 251 ? 0.5412 0.5834 0.5191 0.0529 0.0619 -0.0546 305 LEU A CB 2029 C CG . LEU A 251 ? 0.5360 0.5747 0.5106 0.0524 0.0548 -0.0584 305 LEU A CG 2030 C CD1 . LEU A 251 ? 0.5239 0.5613 0.4997 0.0483 0.0509 -0.0577 305 LEU A CD1 2031 C CD2 . LEU A 251 ? 0.5121 0.5465 0.4753 0.0573 0.0533 -0.0610 305 LEU A CD2 2032 N N . LEU A 252 ? 0.5543 0.6063 0.5489 0.0542 0.0760 -0.0489 306 LEU A N 2033 C CA . LEU A 252 ? 0.5604 0.6158 0.5615 0.0533 0.0823 -0.0446 306 LEU A CA 2034 C C . LEU A 252 ? 0.5844 0.6421 0.5868 0.0573 0.0892 -0.0432 306 LEU A C 2035 O O . LEU A 252 ? 0.5850 0.6448 0.5909 0.0578 0.0957 -0.0392 306 LEU A O 2036 C CB . LEU A 252 ? 0.5433 0.6024 0.5580 0.0484 0.0807 -0.0437 306 LEU A CB 2037 C CG . LEU A 252 ? 0.5362 0.5939 0.5520 0.0440 0.0752 -0.0440 306 LEU A CG 2038 C CD1 . LEU A 252 ? 0.4960 0.5573 0.5255 0.0401 0.0738 -0.0436 306 LEU A CD1 2039 C CD2 . LEU A 252 ? 0.5519 0.6078 0.5625 0.0435 0.0771 -0.0410 306 LEU A CD2 2040 N N . GLU A 253 ? 0.5968 0.6541 0.5972 0.0601 0.0880 -0.0463 307 GLU A N 2041 C CA . GLU A 253 ? 0.6283 0.6888 0.6331 0.0632 0.0941 -0.0453 307 GLU A CA 2042 C C . GLU A 253 ? 0.6513 0.7097 0.6459 0.0685 0.1007 -0.0428 307 GLU A C 2043 O O . GLU A 253 ? 0.6662 0.7276 0.6657 0.0704 0.1079 -0.0398 307 GLU A O 2044 C CB . GLU A 253 ? 0.6148 0.6757 0.6212 0.0645 0.0908 -0.0494 307 GLU A CB 2045 C CG . GLU A 253 ? 0.6332 0.6891 0.6267 0.0677 0.0864 -0.0531 307 GLU A CG 2046 C CD . GLU A 253 ? 0.6534 0.7097 0.6496 0.0683 0.0824 -0.0572 307 GLU A CD 2047 O OE1 . GLU A 253 ? 0.6594 0.7198 0.6674 0.0660 0.0828 -0.0572 307 GLU A OE1 2048 O OE2 . GLU A 253 ? 0.6650 0.7173 0.6517 0.0711 0.0786 -0.0605 307 GLU A OE2 2049 N N . LYS A 254 ? 0.6726 0.7258 0.6533 0.0708 0.0984 -0.0438 308 LYS A N 2050 C CA . LYS A 254 ? 0.6920 0.7421 0.6608 0.0764 0.1039 -0.0417 308 LYS A CA 2051 C C . LYS A 254 ? 0.7049 0.7546 0.6727 0.0752 0.1081 -0.0370 308 LYS A C 2052 O O . LYS A 254 ? 0.7134 0.7603 0.6712 0.0799 0.1131 -0.0347 308 LYS A O 2053 C CB . LYS A 254 ? 0.6973 0.7416 0.6510 0.0806 0.0991 -0.0457 308 LYS A CB 2054 C CG . LYS A 254 ? 0.6774 0.7218 0.6326 0.0814 0.0944 -0.0504 308 LYS A CG 2055 C CD . LYS A 254 ? 0.6783 0.7168 0.6194 0.0857 0.0894 -0.0545 308 LYS A CD 2056 C CE . LYS A 254 ? 0.6871 0.7256 0.6289 0.0877 0.0863 -0.0588 308 LYS A CE 2057 N NZ . LYS A 254 ? 0.6688 0.7014 0.5988 0.0910 0.0797 -0.0634 308 LYS A NZ 2058 N N . MET A 255 ? 0.7050 0.7574 0.6831 0.0694 0.1061 -0.0355 309 MET A N 2059 C CA . MET A 255 ? 0.7138 0.7656 0.6915 0.0678 0.1092 -0.0313 309 MET A CA 2060 C C . MET A 255 ? 0.7317 0.7855 0.7120 0.0704 0.1192 -0.0260 309 MET A C 2061 O O . MET A 255 ? 0.7317 0.7902 0.7244 0.0694 0.1235 -0.0244 309 MET A O 2062 C CB . MET A 255 ? 0.6972 0.7514 0.6858 0.0611 0.1048 -0.0310 309 MET A CB 2063 C CG A MET A 255 ? 0.6905 0.7417 0.6740 0.0591 0.0958 -0.0353 309 MET A CG 2064 C CG B MET A 255 ? 0.6870 0.7387 0.6719 0.0587 0.0958 -0.0353 309 MET A CG 2065 S SD A MET A 255 ? 0.6520 0.7025 0.6382 0.0536 0.0913 -0.0342 309 MET A SD 2066 S SD B MET A 255 ? 0.6593 0.7045 0.6275 0.0611 0.0927 -0.0361 309 MET A SD 2067 C CE A MET A 255 ? 0.6723 0.7201 0.6495 0.0563 0.0972 -0.0297 309 MET A CE 2068 C CE B MET A 255 ? 0.6651 0.7110 0.6362 0.0586 0.0971 -0.0307 309 MET A CE 2069 N N . GLY A 256 ? 0.7484 0.7982 0.7172 0.0737 0.1227 -0.0234 310 GLY A N 2070 C CA . GLY A 256 ? 0.7615 0.8120 0.7305 0.0768 0.1325 -0.0180 310 GLY A CA 2071 C C . GLY A 256 ? 0.7641 0.8152 0.7378 0.0735 0.1352 -0.0134 310 GLY A C 2072 O O . GLY A 256 ? 0.7430 0.7969 0.7278 0.0674 0.1311 -0.0136 310 GLY A O 2073 N N . GLY A 257 ? 0.7731 0.8212 0.7381 0.0777 0.1421 -0.0093 311 GLY A N 2074 C CA . GLY A 257 ? 0.7794 0.8277 0.7483 0.0752 0.1457 -0.0044 311 GLY A CA 2075 C C . GLY A 257 ? 0.7789 0.8336 0.7683 0.0700 0.1489 -0.0013 311 GLY A C 2076 O O . GLY A 257 ? 0.7746 0.8336 0.7746 0.0700 0.1518 -0.0014 311 GLY A O 2077 N N . SER A 258 ? 0.7871 0.8424 0.7826 0.0655 0.1478 0.0009 312 SER A N 2078 C CA . SER A 258 ? 0.7922 0.8529 0.8072 0.0607 0.1506 0.0040 312 SER A CA 2079 C C . SER A 258 ? 0.7888 0.8545 0.8184 0.0565 0.1454 0.0003 312 SER A C 2080 O O . SER A 258 ? 0.7865 0.8512 0.8127 0.0548 0.1372 -0.0044 312 SER A O 2081 C CB . SER A 258 ? 0.7935 0.8531 0.8105 0.0568 0.1489 0.0064 312 SER A CB 2082 O OG A SER A 258 ? 0.7873 0.8519 0.8235 0.0522 0.1508 0.0090 312 SER A OG 2083 O OG B SER A 258 ? 0.7929 0.8477 0.7963 0.0608 0.1536 0.0098 312 SER A OG 2084 N N . ALA A 259 ? 0.7969 0.8677 0.8429 0.0552 0.1504 0.0028 313 ALA A N 2085 C CA . ALA A 259 ? 0.7932 0.8688 0.8547 0.0511 0.1456 -0.0002 313 ALA A CA 2086 C C . ALA A 259 ? 0.7883 0.8643 0.8565 0.0453 0.1386 -0.0013 313 ALA A C 2087 O O . ALA A 259 ? 0.7917 0.8653 0.8558 0.0442 0.1390 0.0012 313 ALA A O 2088 C CB . ALA A 259 ? 0.7924 0.8733 0.8708 0.0511 0.1529 0.0030 313 ALA A CB 2089 N N . PRO A 260 ? 0.7847 0.8634 0.8626 0.0418 0.1319 -0.0051 314 PRO A N 2090 C CA . PRO A 260 ? 0.7807 0.8597 0.8658 0.0366 0.1258 -0.0058 314 PRO A CA 2091 C C . PRO A 260 ? 0.7833 0.8651 0.8827 0.0342 0.1307 -0.0011 314 PRO A C 2092 O O . PRO A 260 ? 0.7882 0.8738 0.8996 0.0350 0.1365 0.0011 314 PRO A O 2093 C CB . PRO A 260 ? 0.7716 0.8531 0.8651 0.0344 0.1192 -0.0104 314 PRO A CB 2094 C CG . PRO A 260 ? 0.7704 0.8541 0.8657 0.0380 0.1235 -0.0111 314 PRO A CG 2095 C CD . PRO A 260 ? 0.7797 0.8600 0.8595 0.0428 0.1289 -0.0093 314 PRO A CD 2096 N N . PRO A 261 ? 0.7843 0.8644 0.8832 0.0314 0.1283 0.0003 315 PRO A N 2097 C CA . PRO A 261 ? 0.7840 0.8662 0.8959 0.0292 0.1328 0.0049 315 PRO A CA 2098 C C . PRO A 261 ? 0.7735 0.8608 0.9065 0.0261 0.1316 0.0044 315 PRO A C 2099 O O . PRO A 261 ? 0.7714 0.8614 0.9177 0.0255 0.1375 0.0084 315 PRO A O 2100 C CB . PRO A 261 ? 0.7832 0.8622 0.8894 0.0264 0.1278 0.0049 315 PRO A CB 2101 C CG . PRO A 261 ? 0.7795 0.8562 0.8758 0.0258 0.1190 -0.0005 315 PRO A CG 2102 C CD . PRO A 261 ? 0.7806 0.8566 0.8672 0.0300 0.1212 -0.0022 315 PRO A CD 2103 N N . ASP A 262 ? 0.7621 0.8502 0.8981 0.0244 0.1240 -0.0005 316 ASP A N 2104 C CA . ASP A 262 ? 0.7494 0.8419 0.9043 0.0219 0.1215 -0.0019 316 ASP A CA 2105 C C . ASP A 262 ? 0.7353 0.8277 0.8875 0.0218 0.1141 -0.0077 316 ASP A C 2106 O O . ASP A 262 ? 0.7411 0.8304 0.8777 0.0236 0.1115 -0.0101 316 ASP A O 2107 C CB . ASP A 262 ? 0.7490 0.8420 0.9155 0.0178 0.1184 -0.0007 316 ASP A CB 2108 C CG . ASP A 262 ? 0.7521 0.8411 0.9077 0.0157 0.1106 -0.0031 316 ASP A CG 2109 O OD1 . ASP A 262 ? 0.7710 0.8587 0.9204 0.0156 0.1040 -0.0076 316 ASP A OD1 2110 O OD2 . ASP A 262 ? 0.7518 0.8390 0.9056 0.0143 0.1112 -0.0004 316 ASP A OD2 2111 N N A SER A 263 ? 0.7208 0.8166 0.8886 0.0200 0.1108 -0.0097 317 SER A N 2112 N N B SER A 263 ? 0.7232 0.8189 0.8909 0.0199 0.1107 -0.0098 317 SER A N 2113 C CA A SER A 263 ? 0.7054 0.8013 0.8724 0.0201 0.1042 -0.0149 317 SER A CA 2114 C CA B SER A 263 ? 0.7105 0.8064 0.8776 0.0201 0.1041 -0.0149 317 SER A CA 2115 C C A SER A 263 ? 0.6972 0.7891 0.8534 0.0185 0.0957 -0.0183 317 SER A C 2116 C C B SER A 263 ? 0.6987 0.7909 0.8567 0.0183 0.0953 -0.0185 317 SER A C 2117 O O A SER A 263 ? 0.6965 0.7870 0.8456 0.0195 0.0912 -0.0221 317 SER A O 2118 O O B SER A 263 ? 0.6959 0.7872 0.8496 0.0189 0.0902 -0.0225 317 SER A O 2119 C CB A SER A 263 ? 0.6996 0.7997 0.8863 0.0186 0.1023 -0.0163 317 SER A CB 2120 C CB B SER A 263 ? 0.7071 0.8075 0.8941 0.0189 0.1031 -0.0161 317 SER A CB 2121 O OG A SER A 263 ? 0.6683 0.7686 0.8654 0.0153 0.0985 -0.0158 317 SER A OG 2122 O OG B SER A 263 ? 0.7109 0.8149 0.9060 0.0210 0.1113 -0.0132 317 SER A OG 2123 N N . SER A 264 ? 0.6885 0.7785 0.8438 0.0162 0.0936 -0.0168 318 SER A N 2124 C CA . SER A 264 ? 0.6720 0.7583 0.8180 0.0146 0.0859 -0.0196 318 SER A CA 2125 C C . SER A 264 ? 0.6629 0.7453 0.7898 0.0166 0.0858 -0.0204 318 SER A C 2126 O O . SER A 264 ? 0.6660 0.7453 0.7845 0.0156 0.0799 -0.0227 318 SER A O 2127 C CB . SER A 264 ? 0.6721 0.7575 0.8225 0.0117 0.0840 -0.0177 318 SER A CB 2128 O OG . SER A 264 ? 0.6662 0.7497 0.8075 0.0122 0.0887 -0.0141 318 SER A OG 2129 N N . TRP A 265 ? 0.6429 0.7256 0.7636 0.0195 0.0922 -0.0185 319 TRP A N 2130 C CA . TRP A 265 ? 0.6288 0.7079 0.7323 0.0220 0.0925 -0.0194 319 TRP A CA 2131 C C . TRP A 265 ? 0.6239 0.7034 0.7236 0.0247 0.0918 -0.0226 319 TRP A C 2132 O O . TRP A 265 ? 0.6198 0.6962 0.7057 0.0269 0.0911 -0.0241 319 TRP A O 2133 C CB . TRP A 265 ? 0.6311 0.7092 0.7279 0.0242 0.0998 -0.0152 319 TRP A CB 2134 C CG . TRP A 265 ? 0.6180 0.6933 0.7093 0.0224 0.0988 -0.0130 319 TRP A CG 2135 C CD1 . TRP A 265 ? 0.6181 0.6943 0.7189 0.0190 0.0974 -0.0114 319 TRP A CD1 2136 C CD2 . TRP A 265 ? 0.6008 0.6718 0.6761 0.0241 0.0990 -0.0125 319 TRP A CD2 2137 N NE1 . TRP A 265 ? 0.6198 0.6926 0.7113 0.0185 0.0968 -0.0097 319 TRP A NE1 2138 C CE2 . TRP A 265 ? 0.6244 0.6941 0.7003 0.0215 0.0978 -0.0104 319 TRP A CE2 2139 C CE3 . TRP A 265 ? 0.5944 0.6624 0.6551 0.0277 0.0997 -0.0138 319 TRP A CE3 2140 C CZ2 . TRP A 265 ? 0.6052 0.6708 0.6677 0.0224 0.0974 -0.0096 319 TRP A CZ2 2141 C CZ3 . TRP A 265 ? 0.5976 0.6615 0.6451 0.0286 0.0991 -0.0131 319 TRP A CZ3 2142 C CH2 . TRP A 265 ? 0.6007 0.6634 0.6492 0.0259 0.0979 -0.0110 319 TRP A CH2 2143 N N . ARG A 266 ? 0.6143 0.6973 0.7263 0.0244 0.0917 -0.0239 320 ARG A N 2144 C CA . ARG A 266 ? 0.6061 0.6899 0.7166 0.0268 0.0909 -0.0270 320 ARG A CA 2145 C C . ARG A 266 ? 0.5847 0.6679 0.6979 0.0250 0.0829 -0.0312 320 ARG A C 2146 O O . ARG A 266 ? 0.5752 0.6603 0.7004 0.0227 0.0801 -0.0317 320 ARG A O 2147 C CB . ARG A 266 ? 0.6155 0.7038 0.7381 0.0283 0.0970 -0.0254 320 ARG A CB 2148 C CG . ARG A 266 ? 0.6665 0.7547 0.7819 0.0322 0.1051 -0.0227 320 ARG A CG 2149 C CD . ARG A 266 ? 0.7378 0.8304 0.8644 0.0343 0.1108 -0.0219 320 ARG A CD 2150 N NE . ARG A 266 ? 0.7930 0.8883 0.9294 0.0342 0.1184 -0.0169 320 ARG A NE 2151 C CZ . ARG A 266 ? 0.8168 0.9155 0.9702 0.0312 0.1185 -0.0154 320 ARG A CZ 2152 N NH1 . ARG A 266 ? 0.8141 0.9135 0.9761 0.0281 0.1110 -0.0186 320 ARG A NH1 2153 N NH2 . ARG A 266 ? 0.8177 0.9185 0.9795 0.0313 0.1260 -0.0105 320 ARG A NH2 2154 N N . GLY A 267 ? 0.5767 0.6569 0.6786 0.0264 0.0793 -0.0342 321 GLY A N 2155 C CA . GLY A 267 ? 0.5566 0.6361 0.6605 0.0255 0.0726 -0.0381 321 GLY A CA 2156 C C . GLY A 267 ? 0.5613 0.6436 0.6717 0.0274 0.0737 -0.0400 321 GLY A C 2157 O O . GLY A 267 ? 0.5559 0.6417 0.6740 0.0286 0.0795 -0.0380 321 GLY A O 2158 N N . SER A 268 ? 0.5450 0.6256 0.6523 0.0279 0.0685 -0.0437 322 SER A N 2159 C CA . SER A 268 ? 0.5393 0.6222 0.6533 0.0294 0.0682 -0.0461 322 SER A CA 2160 C C . SER A 268 ? 0.5324 0.6146 0.6380 0.0328 0.0705 -0.0474 322 SER A C 2161 O O . SER A 268 ? 0.5276 0.6118 0.6386 0.0343 0.0706 -0.0493 322 SER A O 2162 C CB . SER A 268 ? 0.5351 0.6165 0.6521 0.0281 0.0608 -0.0493 322 SER A CB 2163 O OG . SER A 268 ? 0.5724 0.6556 0.7011 0.0258 0.0589 -0.0486 322 SER A OG 2164 N N . LEU A 269 ? 0.5225 0.6018 0.6152 0.0342 0.0719 -0.0467 323 LEU A N 2165 C CA . LEU A 269 ? 0.5257 0.6039 0.6100 0.0376 0.0735 -0.0484 323 LEU A CA 2166 C C . LEU A 269 ? 0.5421 0.6235 0.6300 0.0405 0.0810 -0.0464 323 LEU A C 2167 O O . LEU A 269 ? 0.5329 0.6166 0.6265 0.0399 0.0861 -0.0428 323 LEU A O 2168 C CB . LEU A 269 ? 0.5235 0.5972 0.5929 0.0386 0.0722 -0.0486 323 LEU A CB 2169 C CG . LEU A 269 ? 0.5106 0.5805 0.5747 0.0364 0.0652 -0.0507 323 LEU A CG 2170 C CD1 . LEU A 269 ? 0.4558 0.5218 0.5067 0.0373 0.0649 -0.0504 323 LEU A CD1 2171 C CD2 . LEU A 269 ? 0.4813 0.5504 0.5464 0.0370 0.0607 -0.0545 323 LEU A CD2 2172 N N . LYS A 270 ? 0.5499 0.6313 0.6341 0.0437 0.0820 -0.0485 324 LYS A N 2173 C CA . LYS A 270 ? 0.5816 0.6658 0.6684 0.0470 0.0893 -0.0467 324 LYS A CA 2174 C C . LYS A 270 ? 0.5879 0.6693 0.6617 0.0500 0.0938 -0.0446 324 LYS A C 2175 O O . LYS A 270 ? 0.5960 0.6753 0.6599 0.0538 0.0947 -0.0461 324 LYS A O 2176 C CB . LYS A 270 ? 0.5894 0.6746 0.6778 0.0496 0.0884 -0.0499 324 LYS A CB 2177 C CG . LYS A 270 ? 0.6169 0.7048 0.7185 0.0471 0.0842 -0.0520 324 LYS A CG 2178 C CD . LYS A 270 ? 0.6501 0.7419 0.7663 0.0444 0.0865 -0.0491 324 LYS A CD 2179 C CE . LYS A 270 ? 0.6668 0.7612 0.7966 0.0427 0.0824 -0.0515 324 LYS A CE 2180 N NZ . LYS A 270 ? 0.6702 0.7683 0.8149 0.0403 0.0845 -0.0489 324 LYS A NZ 2181 N N . VAL A 271 ? 0.5893 0.6704 0.6630 0.0482 0.0960 -0.0412 325 VAL A N 2182 C CA . VAL A 271 ? 0.5981 0.6762 0.6594 0.0508 0.0999 -0.0389 325 VAL A CA 2183 C C . VAL A 271 ? 0.6041 0.6846 0.6729 0.0493 0.1056 -0.0340 325 VAL A C 2184 O O . VAL A 271 ? 0.5927 0.6763 0.6749 0.0457 0.1046 -0.0331 325 VAL A O 2185 C CB . VAL A 271 ? 0.5970 0.6700 0.6457 0.0498 0.0937 -0.0408 325 VAL A CB 2186 C CG1 . VAL A 271 ? 0.5968 0.6670 0.6377 0.0517 0.0887 -0.0453 325 VAL A CG1 2187 C CG2 . VAL A 271 ? 0.5875 0.6607 0.6423 0.0448 0.0890 -0.0405 325 VAL A CG2 2188 N N . PRO A 272 ? 0.6250 0.7038 0.6853 0.0525 0.1117 -0.0309 326 PRO A N 2189 C CA . PRO A 272 ? 0.6346 0.7154 0.7020 0.0513 0.1178 -0.0259 326 PRO A CA 2190 C C . PRO A 272 ? 0.6308 0.7102 0.6988 0.0471 0.1141 -0.0247 326 PRO A C 2191 O O . PRO A 272 ? 0.6317 0.7137 0.7107 0.0446 0.1169 -0.0215 326 PRO A O 2192 C CB . PRO A 272 ? 0.6498 0.7282 0.7054 0.0566 0.1251 -0.0231 326 PRO A CB 2193 C CG . PRO A 272 ? 0.6505 0.7244 0.6901 0.0598 0.1207 -0.0271 326 PRO A CG 2194 C CD . PRO A 272 ? 0.6370 0.7122 0.6821 0.0578 0.1139 -0.0318 326 PRO A CD 2195 N N . TYR A 273 ? 0.6311 0.7064 0.6879 0.0464 0.1077 -0.0274 327 TYR A N 2196 C CA . TYR A 273 ? 0.6228 0.6962 0.6781 0.0429 0.1043 -0.0263 327 TYR A CA 2197 C C . TYR A 273 ? 0.6352 0.7071 0.6848 0.0445 0.1105 -0.0218 327 TYR A C 2198 O O . TYR A 273 ? 0.6329 0.7053 0.6878 0.0416 0.1112 -0.0190 327 TYR A O 2199 C CB . TYR A 273 ? 0.6063 0.6829 0.6768 0.0381 0.1012 -0.0262 327 TYR A CB 2200 C CG . TYR A 273 ? 0.5897 0.6663 0.6626 0.0364 0.0937 -0.0307 327 TYR A CG 2201 C CD1 . TYR A 273 ? 0.5549 0.6281 0.6210 0.0344 0.0870 -0.0329 327 TYR A CD1 2202 C CD2 . TYR A 273 ? 0.5391 0.6188 0.6210 0.0370 0.0936 -0.0327 327 TYR A CD2 2203 C CE1 . TYR A 273 ? 0.5459 0.6187 0.6139 0.0330 0.0806 -0.0367 327 TYR A CE1 2204 C CE2 . TYR A 273 ? 0.5125 0.5918 0.5962 0.0356 0.0868 -0.0366 327 TYR A CE2 2205 C CZ . TYR A 273 ? 0.5216 0.5972 0.5979 0.0337 0.0805 -0.0385 327 TYR A CZ 2206 O OH . TYR A 273 ? 0.4616 0.5364 0.5392 0.0327 0.0743 -0.0421 327 TYR A OH 2207 N N . ASN A 274 ? 0.6466 0.7162 0.6851 0.0495 0.1149 -0.0212 328 ASN A N 2208 C CA . ASN A 274 ? 0.6636 0.7307 0.6937 0.0520 0.1205 -0.0173 328 ASN A CA 2209 C C . ASN A 274 ? 0.6680 0.7307 0.6878 0.0505 0.1151 -0.0183 328 ASN A C 2210 O O . ASN A 274 ? 0.6685 0.7286 0.6808 0.0505 0.1086 -0.0224 328 ASN A O 2211 C CB . ASN A 274 ? 0.6617 0.7265 0.6804 0.0583 0.1256 -0.0171 328 ASN A CB 2212 C CG . ASN A 274 ? 0.6642 0.7333 0.6930 0.0604 0.1331 -0.0148 328 ASN A CG 2213 O OD1 . ASN A 274 ? 0.6590 0.7324 0.7029 0.0574 0.1366 -0.0118 328 ASN A OD1 2214 N ND2 . ASN A 274 ? 0.5537 0.6216 0.5746 0.0654 0.1354 -0.0163 328 ASN A ND2 2215 N N . VAL A 275 ? 0.6800 0.7420 0.7002 0.0493 0.1180 -0.0144 329 VAL A N 2216 C CA . VAL A 275 ? 0.6842 0.7426 0.6965 0.0475 0.1132 -0.0149 329 VAL A CA 2217 C C . VAL A 275 ? 0.6991 0.7521 0.6933 0.0522 0.1126 -0.0162 329 VAL A C 2218 O O . VAL A 275 ? 0.6974 0.7470 0.6839 0.0512 0.1071 -0.0181 329 VAL A O 2219 C CB . VAL A 275 ? 0.6884 0.7479 0.7074 0.0448 0.1167 -0.0102 329 VAL A CB 2220 C CG1 . VAL A 275 ? 0.6977 0.7533 0.7081 0.0432 0.1121 -0.0105 329 VAL A CG1 2221 C CG2 . VAL A 275 ? 0.6892 0.7538 0.7268 0.0402 0.1159 -0.0098 329 VAL A CG2 2222 N N . GLY A 276 ? 0.7123 0.7642 0.6997 0.0575 0.1180 -0.0154 330 GLY A N 2223 C CA . GLY A 276 ? 0.7306 0.7767 0.7001 0.0627 0.1179 -0.0164 330 GLY A CA 2224 C C . GLY A 276 ? 0.7462 0.7896 0.7093 0.0644 0.1229 -0.0118 330 GLY A C 2225 O O . GLY A 276 ? 0.7425 0.7888 0.7145 0.0632 0.1294 -0.0072 330 GLY A O 2226 N N . PRO A 277 ? 0.7629 0.8007 0.7110 0.0671 0.1199 -0.0131 331 PRO A N 2227 C CA . PRO A 277 ? 0.7674 0.8012 0.7046 0.0688 0.1122 -0.0184 331 PRO A CA 2228 C C . PRO A 277 ? 0.7727 0.8051 0.7029 0.0742 0.1133 -0.0210 331 PRO A C 2229 O O . PRO A 277 ? 0.7766 0.8094 0.7049 0.0784 0.1209 -0.0181 331 PRO A O 2230 C CB . PRO A 277 ? 0.7808 0.8089 0.7042 0.0715 0.1116 -0.0174 331 PRO A CB 2231 C CG . PRO A 277 ? 0.7895 0.8175 0.7117 0.0745 0.1213 -0.0116 331 PRO A CG 2232 C CD . PRO A 277 ? 0.7741 0.8086 0.7147 0.0692 0.1246 -0.0087 331 PRO A CD 2233 N N . GLY A 278 ? 0.7684 0.7994 0.6953 0.0743 0.1060 -0.0263 332 GLY A N 2234 C CA . GLY A 278 ? 0.7790 0.8076 0.6973 0.0798 0.1055 -0.0297 332 GLY A CA 2235 C C . GLY A 278 ? 0.7795 0.8128 0.7072 0.0800 0.1090 -0.0298 332 GLY A C 2236 O O . GLY A 278 ? 0.7689 0.8075 0.7107 0.0760 0.1124 -0.0271 332 GLY A O 2237 N N . PHE A 279 ? 0.7813 0.8124 0.7014 0.0849 0.1079 -0.0333 333 PHE A N 2238 C CA . PHE A 279 ? 0.7915 0.8263 0.7186 0.0861 0.1109 -0.0340 333 PHE A CA 2239 C C . PHE A 279 ? 0.8061 0.8417 0.7310 0.0912 0.1212 -0.0298 333 PHE A C 2240 O O . PHE A 279 ? 0.8132 0.8457 0.7293 0.0945 0.1260 -0.0264 333 PHE A O 2241 C CB . PHE A 279 ? 0.7915 0.8233 0.7113 0.0891 0.1047 -0.0398 333 PHE A CB 2242 C CG . PHE A 279 ? 0.7777 0.8099 0.7029 0.0840 0.0956 -0.0438 333 PHE A CG 2243 C CD1 . PHE A 279 ? 0.7721 0.7998 0.6884 0.0864 0.0886 -0.0488 333 PHE A CD1 2244 C CD2 . PHE A 279 ? 0.7512 0.7879 0.6905 0.0771 0.0939 -0.0427 333 PHE A CD2 2245 C CE1 . PHE A 279 ? 0.7626 0.7905 0.6843 0.0818 0.0807 -0.0522 333 PHE A CE1 2246 C CE2 . PHE A 279 ? 0.7384 0.7750 0.6818 0.0729 0.0859 -0.0462 333 PHE A CE2 2247 C CZ . PHE A 279 ? 0.7319 0.7642 0.6668 0.0752 0.0796 -0.0508 333 PHE A CZ 2248 N N . THR A 280 ? 0.8116 0.8511 0.7445 0.0920 0.1247 -0.0300 334 THR A N 2249 C CA . THR A 280 ? 0.8254 0.8659 0.7569 0.0973 0.1347 -0.0262 334 THR A CA 2250 C C . THR A 280 ? 0.8518 0.8870 0.7666 0.1056 0.1357 -0.0284 334 THR A C 2251 O O . THR A 280 ? 0.8517 0.8845 0.7607 0.1069 0.1286 -0.0339 334 THR A O 2252 C CB . THR A 280 ? 0.8180 0.8654 0.7664 0.0950 0.1389 -0.0250 334 THR A CB 2253 O OG1 . THR A 280 ? 0.7944 0.8431 0.7468 0.0932 0.1319 -0.0303 334 THR A OG1 2254 C CG2 . THR A 280 ? 0.7975 0.8501 0.7624 0.0887 0.1415 -0.0210 334 THR A CG2 2255 N N . GLY A 281 ? 0.8715 0.9051 0.7794 0.1112 0.1447 -0.0241 335 GLY A N 2256 C CA . GLY A 281 ? 0.8914 0.9196 0.7824 0.1202 0.1476 -0.0251 335 GLY A CA 2257 C C . GLY A 281 ? 0.9032 0.9269 0.7827 0.1239 0.1396 -0.0318 335 GLY A C 2258 O O . GLY A 281 ? 0.9070 0.9241 0.7710 0.1278 0.1353 -0.0341 335 GLY A O 2259 N N . ASN A 282 ? 0.9067 0.9339 0.7939 0.1231 0.1377 -0.0349 336 ASN A N 2260 C CA . ASN A 282 ? 0.9250 0.9481 0.8022 0.1271 0.1308 -0.0411 336 ASN A CA 2261 C C . ASN A 282 ? 0.9204 0.9402 0.7944 0.1237 0.1198 -0.0458 336 ASN A C 2262 O O . ASN A 282 ? 0.9334 0.9472 0.7939 0.1284 0.1143 -0.0501 336 ASN A O 2263 C CB . ASN A 282 ? 0.9239 0.9517 0.8116 0.1264 0.1312 -0.0433 336 ASN A CB 2264 C CG . ASN A 282 ? 0.9558 0.9850 0.8422 0.1324 0.1415 -0.0399 336 ASN A CG 2265 O OD1 . ASN A 282 ? 0.9914 1.0173 0.8672 0.1392 0.1418 -0.0426 336 ASN A OD1 2266 N ND2 . ASN A 282 ? 0.9633 0.9973 0.8606 0.1301 0.1501 -0.0340 336 ASN A ND2 2267 N N . PHE A 283 ? 0.9082 0.9319 0.7949 0.1157 0.1168 -0.0448 337 PHE A N 2268 C CA . PHE A 283 ? 0.8922 0.9138 0.7786 0.1114 0.1070 -0.0485 337 PHE A CA 2269 C C . PHE A 283 ? 0.8947 0.9136 0.7760 0.1101 0.1069 -0.0457 337 PHE A C 2270 O O . PHE A 283 ? 0.8820 0.9003 0.7657 0.1054 0.1000 -0.0476 337 PHE A O 2271 C CB . PHE A 283 ? 0.8733 0.9007 0.7768 0.1036 0.1032 -0.0495 337 PHE A CB 2272 C CG . PHE A 283 ? 0.8589 0.8905 0.7710 0.1038 0.1051 -0.0507 337 PHE A CG 2273 C CD1 . PHE A 283 ? 0.8348 0.8725 0.7601 0.1013 0.1119 -0.0467 337 PHE A CD1 2274 C CD2 . PHE A 283 ? 0.8403 0.8697 0.7482 0.1064 0.0997 -0.0560 337 PHE A CD2 2275 C CE1 . PHE A 283 ? 0.8164 0.8581 0.7503 0.1015 0.1134 -0.0480 337 PHE A CE1 2276 C CE2 . PHE A 283 ? 0.8334 0.8667 0.7495 0.1066 0.1012 -0.0572 337 PHE A CE2 2277 C CZ . PHE A 283 ? 0.8203 0.8597 0.7492 0.1042 0.1081 -0.0532 337 PHE A CZ 2278 N N . SER A 284 ? 0.8992 0.9166 0.7736 0.1141 0.1149 -0.0411 338 SER A N 2279 C CA . SER A 284 ? 0.8957 0.9111 0.7665 0.1127 0.1158 -0.0378 338 SER A CA 2280 C C . SER A 284 ? 0.8944 0.9031 0.7520 0.1148 0.1077 -0.0418 338 SER A C 2281 O O . SER A 284 ? 0.8946 0.9015 0.7500 0.1126 0.1062 -0.0402 338 SER A O 2282 C CB . SER A 284 ? 0.9084 0.9226 0.7731 0.1176 0.1263 -0.0321 338 SER A CB 2283 O OG . SER A 284 ? 0.9302 0.9374 0.7760 0.1263 0.1269 -0.0336 338 SER A OG 2284 N N . THR A 285 ? 0.8902 0.8952 0.7398 0.1189 0.1022 -0.0471 339 THR A N 2285 C CA . THR A 285 ? 0.8922 0.8903 0.7289 0.1220 0.0942 -0.0515 339 THR A CA 2286 C C . THR A 285 ? 0.8770 0.8762 0.7218 0.1163 0.0843 -0.0562 339 THR A C 2287 O O . THR A 285 ? 0.8815 0.8760 0.7196 0.1167 0.0772 -0.0594 339 THR A O 2288 C CB . THR A 285 ? 0.9075 0.8999 0.7290 0.1312 0.0939 -0.0548 339 THR A CB 2289 O OG1 . THR A 285 ? 0.8957 0.8893 0.7221 0.1305 0.0885 -0.0598 339 THR A OG1 2290 C CG2 . THR A 285 ? 0.9178 0.9106 0.7342 0.1369 0.1050 -0.0502 339 THR A CG2 2291 N N . GLN A 286 ? 0.8609 0.8658 0.7198 0.1112 0.0839 -0.0568 340 GLN A N 2292 C CA . GLN A 286 ? 0.8443 0.8505 0.7121 0.1054 0.0754 -0.0605 340 GLN A CA 2293 C C . GLN A 286 ? 0.8245 0.8325 0.6991 0.0990 0.0737 -0.0581 340 GLN A C 2294 O O . GLN A 286 ? 0.8141 0.8245 0.6917 0.0972 0.0799 -0.0532 340 GLN A O 2295 C CB . GLN A 286 ? 0.8379 0.8497 0.7186 0.1020 0.0759 -0.0613 340 GLN A CB 2296 C CG . GLN A 286 ? 0.8596 0.8697 0.7350 0.1076 0.0754 -0.0649 340 GLN A CG 2297 C CD . GLN A 286 ? 0.8641 0.8800 0.7523 0.1047 0.0777 -0.0647 340 GLN A CD 2298 O OE1 . GLN A 286 ? 0.8481 0.8693 0.7493 0.0985 0.0793 -0.0621 340 GLN A OE1 2299 N NE2 . GLN A 286 ? 0.8656 0.8803 0.7498 0.1094 0.0775 -0.0677 340 GLN A NE2 2300 N N . LYS A 287 ? 0.8152 0.8218 0.6925 0.0955 0.0655 -0.0615 341 LYS A N 2301 C CA . LYS A 287 ? 0.7909 0.7990 0.6747 0.0894 0.0632 -0.0597 341 LYS A CA 2302 C C . LYS A 287 ? 0.7641 0.7757 0.6610 0.0829 0.0581 -0.0616 341 LYS A C 2303 O O . LYS A 287 ? 0.7547 0.7670 0.6550 0.0832 0.0555 -0.0647 341 LYS A O 2304 C CB . LYS A 287 ? 0.8030 0.8053 0.6759 0.0917 0.0588 -0.0611 341 LYS A CB 2305 C CG . LYS A 287 ? 0.8346 0.8327 0.6935 0.0982 0.0637 -0.0589 341 LYS A CG 2306 C CD . LYS A 287 ? 0.8592 0.8558 0.7154 0.0965 0.0642 -0.0559 341 LYS A CD 2307 C CE . LYS A 287 ? 0.8898 0.8789 0.7294 0.1030 0.0617 -0.0577 341 LYS A CE 2308 N NZ . LYS A 287 ? 0.9094 0.8951 0.7365 0.1112 0.0668 -0.0573 341 LYS A NZ 2309 N N . VAL A 288 ? 0.7421 0.7554 0.6455 0.0774 0.0566 -0.0597 342 VAL A N 2310 C CA . VAL A 288 ? 0.7104 0.7261 0.6248 0.0715 0.0516 -0.0611 342 VAL A CA 2311 C C . VAL A 288 ? 0.6982 0.7100 0.6094 0.0703 0.0447 -0.0635 342 VAL A C 2312 O O . VAL A 288 ? 0.6956 0.7052 0.6011 0.0709 0.0451 -0.0619 342 VAL A O 2313 C CB . VAL A 288 ? 0.7097 0.7308 0.6355 0.0660 0.0554 -0.0571 342 VAL A CB 2314 C CG1 . VAL A 288 ? 0.6783 0.7011 0.6140 0.0603 0.0501 -0.0585 342 VAL A CG1 2315 C CG2 . VAL A 288 ? 0.6991 0.7242 0.6299 0.0670 0.0617 -0.0552 342 VAL A CG2 2316 N N . LYS A 289 ? 0.6751 0.6860 0.5903 0.0688 0.0386 -0.0671 343 LYS A N 2317 C CA . LYS A 289 ? 0.6614 0.6687 0.5752 0.0677 0.0319 -0.0696 343 LYS A CA 2318 C C . LYS A 289 ? 0.6329 0.6427 0.5584 0.0618 0.0283 -0.0700 343 LYS A C 2319 O O . LYS A 289 ? 0.6219 0.6330 0.5530 0.0609 0.0269 -0.0717 343 LYS A O 2320 C CB . LYS A 289 ? 0.6701 0.6725 0.5758 0.0729 0.0271 -0.0743 343 LYS A CB 2321 C CG . LYS A 289 ? 0.6842 0.6822 0.5879 0.0727 0.0199 -0.0773 343 LYS A CG 2322 C CD . LYS A 289 ? 0.7429 0.7361 0.6398 0.0781 0.0149 -0.0823 343 LYS A CD 2323 C CE . LYS A 289 ? 0.7808 0.7702 0.6794 0.0773 0.0068 -0.0859 343 LYS A CE 2324 N NZ . LYS A 289 ? 0.8141 0.7994 0.7041 0.0798 0.0047 -0.0863 343 LYS A NZ 2325 N N . MET A 290 ? 0.6113 0.6212 0.5396 0.0581 0.0267 -0.0683 344 MET A N 2326 C CA . MET A 290 ? 0.5823 0.5938 0.5205 0.0530 0.0234 -0.0684 344 MET A CA 2327 C C . MET A 290 ? 0.5825 0.5898 0.5198 0.0536 0.0166 -0.0722 344 MET A C 2328 O O . MET A 290 ? 0.5974 0.6010 0.5270 0.0567 0.0142 -0.0738 344 MET A O 2329 C CB . MET A 290 ? 0.5754 0.5889 0.5172 0.0489 0.0254 -0.0646 344 MET A CB 2330 C CG . MET A 290 ? 0.5533 0.5708 0.4972 0.0480 0.0320 -0.0608 344 MET A CG 2331 S SD . MET A 290 ? 0.5586 0.5784 0.5071 0.0434 0.0339 -0.0566 344 MET A SD 2332 C CE . MET A 290 ? 0.5637 0.5857 0.5235 0.0386 0.0307 -0.0572 344 MET A CE 2333 N N . HIS A 291 ? 0.5590 0.5669 0.5042 0.0510 0.0133 -0.0737 345 HIS A N 2334 C CA . HIS A 291 ? 0.5517 0.5562 0.4988 0.0506 0.0071 -0.0765 345 HIS A CA 2335 C C . HIS A 291 ? 0.5187 0.5250 0.4753 0.0452 0.0062 -0.0746 345 HIS A C 2336 O O . HIS A 291 ? 0.4977 0.5057 0.4613 0.0430 0.0063 -0.0744 345 HIS A O 2337 C CB . HIS A 291 ? 0.5648 0.5672 0.5126 0.0530 0.0036 -0.0805 345 HIS A CB 2338 C CG . HIS A 291 ? 0.6121 0.6133 0.5513 0.0584 0.0053 -0.0822 345 HIS A CG 2339 N ND1 . HIS A 291 ? 0.6275 0.6320 0.5661 0.0591 0.0109 -0.0803 345 HIS A ND1 2340 C CD2 . HIS A 291 ? 0.6559 0.6528 0.5867 0.0635 0.0023 -0.0857 345 HIS A CD2 2341 C CE1 . HIS A 291 ? 0.6497 0.6521 0.5798 0.0644 0.0116 -0.0823 345 HIS A CE1 2342 N NE2 . HIS A 291 ? 0.6819 0.6795 0.6067 0.0673 0.0063 -0.0856 345 HIS A NE2 2343 N N . ILE A 292 ? 0.4997 0.5053 0.4560 0.0434 0.0053 -0.0731 346 ILE A N 2344 C CA . ILE A 292 ? 0.4739 0.4812 0.4384 0.0386 0.0049 -0.0709 346 ILE A CA 2345 C C . ILE A 292 ? 0.4632 0.4673 0.4298 0.0380 -0.0001 -0.0727 346 ILE A C 2346 O O . ILE A 292 ? 0.4785 0.4805 0.4400 0.0395 -0.0017 -0.0732 346 ILE A O 2347 C CB . ILE A 292 ? 0.4735 0.4836 0.4379 0.0362 0.0091 -0.0669 346 ILE A CB 2348 C CG1 . ILE A 292 ? 0.4463 0.4595 0.4089 0.0371 0.0144 -0.0650 346 ILE A CG1 2349 C CG2 . ILE A 292 ? 0.4591 0.4705 0.4317 0.0317 0.0085 -0.0648 346 ILE A CG2 2350 C CD1 . ILE A 292 ? 0.4670 0.4825 0.4353 0.0364 0.0156 -0.0654 346 ILE A CD1 2351 N N . HIS A 293 ? 0.4438 0.4476 0.4183 0.0360 -0.0025 -0.0735 347 HIS A N 2352 C CA . HIS A 293 ? 0.4545 0.4555 0.4338 0.0352 -0.0074 -0.0753 347 HIS A CA 2353 C C . HIS A 293 ? 0.4238 0.4260 0.4119 0.0309 -0.0071 -0.0727 347 HIS A C 2354 O O . HIS A 293 ? 0.4048 0.4050 0.3990 0.0299 -0.0105 -0.0738 347 HIS A O 2355 C CB . HIS A 293 ? 0.4675 0.4660 0.4483 0.0376 -0.0111 -0.0792 347 HIS A CB 2356 C CG . HIS A 293 ? 0.5374 0.5345 0.5092 0.0422 -0.0113 -0.0817 347 HIS A CG 2357 N ND1 . HIS A 293 ? 0.5959 0.5907 0.5594 0.0453 -0.0126 -0.0830 347 HIS A ND1 2358 C CD2 . HIS A 293 ? 0.5825 0.5803 0.5516 0.0446 -0.0096 -0.0829 347 HIS A CD2 2359 C CE1 . HIS A 293 ? 0.6216 0.6153 0.5774 0.0496 -0.0119 -0.0848 347 HIS A CE1 2360 N NE2 . HIS A 293 ? 0.6132 0.6089 0.5724 0.0491 -0.0100 -0.0848 347 HIS A NE2 2361 N N . SER A 294 ? 0.4057 0.4109 0.3945 0.0285 -0.0029 -0.0692 348 SER A N 2362 C CA . SER A 294 ? 0.3868 0.3931 0.3825 0.0249 -0.0021 -0.0665 348 SER A CA 2363 C C . SER A 294 ? 0.3785 0.3833 0.3753 0.0238 -0.0042 -0.0660 348 SER A C 2364 O O . SER A 294 ? 0.3949 0.3989 0.3859 0.0254 -0.0049 -0.0667 348 SER A O 2365 C CB . SER A 294 ? 0.3636 0.3731 0.3583 0.0232 0.0023 -0.0631 348 SER A CB 2366 O OG . SER A 294 ? 0.3923 0.4033 0.3866 0.0242 0.0043 -0.0636 348 SER A OG 2367 N N . THR A 295 ? 0.3606 0.3650 0.3646 0.0213 -0.0048 -0.0646 349 THR A N 2368 C CA A THR A 295 ? 0.3556 0.3588 0.3620 0.0201 -0.0066 -0.0639 349 THR A CA 2369 C CA B THR A 295 ? 0.3568 0.3599 0.3635 0.0201 -0.0067 -0.0640 349 THR A CA 2370 C C . THR A 295 ? 0.3484 0.3533 0.3582 0.0172 -0.0038 -0.0602 349 THR A C 2371 O O . THR A 295 ? 0.3373 0.3431 0.3504 0.0160 -0.0017 -0.0585 349 THR A O 2372 C CB A THR A 295 ? 0.3620 0.3626 0.3753 0.0202 -0.0107 -0.0661 349 THR A CB 2373 C CB B THR A 295 ? 0.3619 0.3624 0.3761 0.0201 -0.0106 -0.0661 349 THR A CB 2374 O OG1 A THR A 295 ? 0.3565 0.3571 0.3766 0.0189 -0.0097 -0.0652 349 THR A OG1 2375 O OG1 B THR A 295 ? 0.3790 0.3776 0.3907 0.0231 -0.0137 -0.0700 349 THR A OG1 2376 C CG2 A THR A 295 ? 0.3756 0.3738 0.3853 0.0236 -0.0146 -0.0705 349 THR A CG2 2377 C CG2 B THR A 295 ? 0.3587 0.3580 0.3764 0.0191 -0.0129 -0.0659 349 THR A CG2 2378 N N . ASN A 296 ? 0.3305 0.3355 0.3386 0.0163 -0.0038 -0.0589 350 ASN A N 2379 C CA . ASN A 296 ? 0.3419 0.3481 0.3530 0.0138 -0.0016 -0.0555 350 ASN A CA 2380 C C . ASN A 296 ? 0.3474 0.3517 0.3661 0.0127 -0.0037 -0.0555 350 ASN A C 2381 O O . ASN A 296 ? 0.3670 0.3696 0.3871 0.0136 -0.0071 -0.0577 350 ASN A O 2382 C CB . ASN A 296 ? 0.3375 0.3447 0.3430 0.0135 -0.0005 -0.0541 350 ASN A CB 2383 C CG . ASN A 296 ? 0.3595 0.3687 0.3586 0.0144 0.0021 -0.0536 350 ASN A CG 2384 O OD1 . ASN A 296 ? 0.3990 0.4094 0.3987 0.0145 0.0039 -0.0533 350 ASN A OD1 2385 N ND2 . ASN A 296 ? 0.4099 0.4191 0.4030 0.0153 0.0023 -0.0535 350 ASN A ND2 2386 N N . GLU A 297 ? 0.3230 0.3275 0.3471 0.0111 -0.0018 -0.0530 351 GLU A N 2387 C CA . GLU A 297 ? 0.3360 0.3388 0.3684 0.0102 -0.0030 -0.0525 351 GLU A CA 2388 C C . GLU A 297 ? 0.3018 0.3051 0.3365 0.0084 0.0000 -0.0487 351 GLU A C 2389 O O . GLU A 297 ? 0.2767 0.2808 0.3094 0.0082 0.0027 -0.0468 351 GLU A O 2390 C CB . GLU A 297 ? 0.3657 0.3670 0.4036 0.0106 -0.0035 -0.0535 351 GLU A CB 2391 C CG . GLU A 297 ? 0.4795 0.4806 0.5141 0.0126 -0.0055 -0.0568 351 GLU A CG 2392 C CD . GLU A 297 ? 0.5955 0.5946 0.6373 0.0130 -0.0072 -0.0583 351 GLU A CD 2393 O OE1 . GLU A 297 ? 0.6741 0.6716 0.7177 0.0143 -0.0112 -0.0616 351 GLU A OE1 2394 O OE2 . GLU A 297 ? 0.5762 0.5750 0.6216 0.0122 -0.0049 -0.0561 351 GLU A OE2 2395 N N . VAL A 298 ? 0.3014 0.3039 0.3405 0.0075 -0.0007 -0.0478 352 VAL A N 2396 C CA . VAL A 298 ? 0.2922 0.2949 0.3336 0.0062 0.0022 -0.0440 352 VAL A CA 2397 C C . VAL A 298 ? 0.3008 0.3019 0.3482 0.0062 0.0038 -0.0428 352 VAL A C 2398 O O . VAL A 298 ? 0.2933 0.2929 0.3477 0.0064 0.0019 -0.0442 352 VAL A O 2399 C CB . VAL A 298 ? 0.2997 0.3020 0.3451 0.0054 0.0011 -0.0435 352 VAL A CB 2400 C CG1 . VAL A 298 ? 0.2899 0.2919 0.3385 0.0044 0.0043 -0.0396 352 VAL A CG1 2401 C CG2 . VAL A 298 ? 0.3059 0.3093 0.3442 0.0055 -0.0001 -0.0444 352 VAL A CG2 2402 N N . THR A 299 ? 0.2595 0.2609 0.3045 0.0063 0.0070 -0.0401 353 THR A N 2403 C CA . THR A 299 ? 0.2556 0.2553 0.3041 0.0068 0.0087 -0.0389 353 THR A CA 2404 C C . THR A 299 ? 0.2573 0.2561 0.3054 0.0068 0.0123 -0.0350 353 THR A C 2405 O O . THR A 299 ? 0.2454 0.2455 0.2876 0.0067 0.0132 -0.0340 353 THR A O 2406 C CB . THR A 299 ? 0.2691 0.2695 0.3129 0.0078 0.0085 -0.0407 353 THR A CB 2407 O OG1 . THR A 299 ? 0.2923 0.2934 0.3353 0.0082 0.0053 -0.0444 353 THR A OG1 2408 C CG2 . THR A 299 ? 0.2485 0.2469 0.2961 0.0085 0.0097 -0.0399 353 THR A CG2 2409 N N . ARG A 300 ? 0.2461 0.2426 0.2999 0.0071 0.0142 -0.0329 354 ARG A N 2410 C CA . ARG A 300 ? 0.2567 0.2518 0.3088 0.0078 0.0178 -0.0291 354 ARG A CA 2411 C C . ARG A 300 ? 0.2447 0.2393 0.2901 0.0092 0.0191 -0.0286 354 ARG A C 2412 O O . ARG A 300 ? 0.2471 0.2414 0.2923 0.0098 0.0184 -0.0301 354 ARG A O 2413 C CB . ARG A 300 ? 0.2727 0.2651 0.3330 0.0080 0.0200 -0.0264 354 ARG A CB 2414 C CG . ARG A 300 ? 0.2696 0.2600 0.3279 0.0092 0.0241 -0.0222 354 ARG A CG 2415 C CD . ARG A 300 ? 0.2894 0.2781 0.3575 0.0089 0.0261 -0.0197 354 ARG A CD 2416 N NE . ARG A 300 ? 0.3185 0.3091 0.3901 0.0073 0.0244 -0.0206 354 ARG A NE 2417 C CZ . ARG A 300 ? 0.4047 0.3945 0.4849 0.0068 0.0257 -0.0187 354 ARG A CZ 2418 N NH1 . ARG A 300 ? 0.3688 0.3560 0.4555 0.0076 0.0291 -0.0156 354 ARG A NH1 2419 N NH2 . ARG A 300 ? 0.3609 0.3525 0.4437 0.0055 0.0237 -0.0197 354 ARG A NH2 2420 N N . ILE A 301 ? 0.2330 0.2276 0.2732 0.0097 0.0207 -0.0266 355 ILE A N 2421 C CA . ILE A 301 ? 0.2324 0.2263 0.2663 0.0113 0.0216 -0.0261 355 ILE A CA 2422 C C . ILE A 301 ? 0.2469 0.2379 0.2795 0.0129 0.0247 -0.0224 355 ILE A C 2423 O O . ILE A 301 ? 0.2483 0.2388 0.2836 0.0125 0.0260 -0.0205 355 ILE A O 2424 C CB . ILE A 301 ? 0.2118 0.2085 0.2396 0.0108 0.0201 -0.0277 355 ILE A CB 2425 C CG1 . ILE A 301 ? 0.2088 0.2063 0.2350 0.0101 0.0205 -0.0263 355 ILE A CG1 2426 C CG2 . ILE A 301 ? 0.2143 0.2136 0.2428 0.0098 0.0176 -0.0311 355 ILE A CG2 2427 C CD1 . ILE A 301 ? 0.2495 0.2490 0.2699 0.0099 0.0195 -0.0271 355 ILE A CD1 2428 N N . TYR A 302 ? 0.2433 0.2322 0.2714 0.0150 0.0257 -0.0216 356 TYR A N 2429 C CA . TYR A 302 ? 0.2626 0.2478 0.2886 0.0173 0.0287 -0.0181 356 TYR A CA 2430 C C . TYR A 302 ? 0.2507 0.2349 0.2687 0.0194 0.0283 -0.0181 356 TYR A C 2431 O O . TYR A 302 ? 0.2516 0.2352 0.2669 0.0206 0.0273 -0.0194 356 TYR A O 2432 C CB . TYR A 302 ? 0.2636 0.2455 0.2931 0.0188 0.0307 -0.0166 356 TYR A CB 2433 C CG . TYR A 302 ? 0.2573 0.2396 0.2960 0.0170 0.0309 -0.0167 356 TYR A CG 2434 C CD1 . TYR A 302 ? 0.2952 0.2759 0.3389 0.0170 0.0337 -0.0136 356 TYR A CD1 2435 C CD2 . TYR A 302 ? 0.2953 0.2796 0.3379 0.0154 0.0282 -0.0199 356 TYR A CD2 2436 C CE1 . TYR A 302 ? 0.2912 0.2723 0.3447 0.0153 0.0335 -0.0138 356 TYR A CE1 2437 C CE2 . TYR A 302 ? 0.3060 0.2904 0.3574 0.0140 0.0278 -0.0203 356 TYR A CE2 2438 C CZ . TYR A 302 ? 0.3109 0.2937 0.3680 0.0138 0.0303 -0.0173 356 TYR A CZ 2439 O OH . TYR A 302 ? 0.3408 0.3239 0.4079 0.0123 0.0295 -0.0179 356 TYR A OH 2440 N N . ASN A 303 ? 0.2646 0.2481 0.2788 0.0202 0.0291 -0.0164 357 ASN A N 2441 C CA . ASN A 303 ? 0.2629 0.2443 0.2698 0.0229 0.0288 -0.0160 357 ASN A CA 2442 C C . ASN A 303 ? 0.2729 0.2490 0.2770 0.0265 0.0319 -0.0127 357 ASN A C 2443 O O . ASN A 303 ? 0.2999 0.2744 0.3071 0.0267 0.0349 -0.0099 357 ASN A O 2444 C CB . ASN A 303 ? 0.2430 0.2257 0.2463 0.0226 0.0279 -0.0159 357 ASN A CB 2445 C CG . ASN A 303 ? 0.2585 0.2460 0.2636 0.0194 0.0252 -0.0186 357 ASN A CG 2446 O OD1 . ASN A 303 ? 0.2528 0.2426 0.2589 0.0183 0.0234 -0.0211 357 ASN A OD1 2447 N ND2 . ASN A 303 ? 0.2812 0.2700 0.2860 0.0183 0.0251 -0.0180 357 ASN A ND2 2448 N N . VAL A 304 ? 0.2596 0.2328 0.2580 0.0295 0.0313 -0.0129 358 VAL A N 2449 C CA . VAL A 304 ? 0.2597 0.2272 0.2534 0.0336 0.0343 -0.0096 358 VAL A CA 2450 C C . VAL A 304 ? 0.2708 0.2368 0.2570 0.0359 0.0331 -0.0095 358 VAL A C 2451 O O . VAL A 304 ? 0.2768 0.2443 0.2599 0.0359 0.0297 -0.0122 358 VAL A O 2452 C CB . VAL A 304 ? 0.2750 0.2391 0.2658 0.0364 0.0342 -0.0099 358 VAL A CB 2453 C CG1 . VAL A 304 ? 0.3024 0.2601 0.2888 0.0408 0.0381 -0.0059 358 VAL A CG1 2454 C CG2 . VAL A 304 ? 0.2888 0.2549 0.2867 0.0339 0.0341 -0.0113 358 VAL A CG2 2455 N N . ILE A 305 ? 0.2693 0.2325 0.2534 0.0378 0.0360 -0.0063 359 ILE A N 2456 C CA . ILE A 305 ? 0.2871 0.2483 0.2639 0.0404 0.0353 -0.0057 359 ILE A CA 2457 C C . ILE A 305 ? 0.2900 0.2443 0.2599 0.0459 0.0385 -0.0024 359 ILE A C 2458 O O . ILE A 305 ? 0.3123 0.2644 0.2845 0.0468 0.0430 0.0011 359 ILE A O 2459 C CB . ILE A 305 ? 0.2820 0.2458 0.2617 0.0381 0.0362 -0.0047 359 ILE A CB 2460 C CG1 . ILE A 305 ? 0.2985 0.2686 0.2854 0.0329 0.0338 -0.0074 359 ILE A CG1 2461 C CG2 . ILE A 305 ? 0.2949 0.2565 0.2669 0.0409 0.0349 -0.0045 359 ILE A CG2 2462 C CD1 . ILE A 305 ? 0.2978 0.2709 0.2828 0.0316 0.0294 -0.0111 359 ILE A CD1 2463 N N . GLY A 306 ? 0.3021 0.2531 0.2641 0.0497 0.0361 -0.0036 360 GLY A N 2464 C CA . GLY A 306 ? 0.3166 0.2602 0.2699 0.0558 0.0384 -0.0010 360 GLY A CA 2465 C C . GLY A 306 ? 0.3158 0.2571 0.2616 0.0588 0.0370 -0.0008 360 GLY A C 2466 O O . GLY A 306 ? 0.3312 0.2756 0.2766 0.0572 0.0326 -0.0040 360 GLY A O 2467 N N . THR A 307 ? 0.3189 0.2547 0.2587 0.0633 0.0409 0.0028 361 THR A N 2468 C CA . THR A 307 ? 0.3361 0.2688 0.2677 0.0670 0.0398 0.0031 361 THR A CA 2469 C C . THR A 307 ? 0.3594 0.2840 0.2795 0.0744 0.0403 0.0044 361 THR A C 2470 O O . THR A 307 ? 0.3622 0.2823 0.2802 0.0775 0.0451 0.0079 361 THR A O 2471 C CB . THR A 307 ? 0.3387 0.2721 0.2730 0.0662 0.0443 0.0066 361 THR A CB 2472 O OG1 . THR A 307 ? 0.3499 0.2906 0.2946 0.0596 0.0433 0.0051 361 THR A OG1 2473 C CG2 . THR A 307 ? 0.3713 0.3015 0.2971 0.0701 0.0434 0.0070 361 THR A CG2 2474 N N . LEU A 308 ? 0.3735 0.2959 0.2861 0.0775 0.0353 0.0016 362 LEU A N 2475 C CA . LEU A 308 ? 0.3838 0.2976 0.2835 0.0854 0.0351 0.0025 362 LEU A CA 2476 C C . LEU A 308 ? 0.3843 0.2966 0.2784 0.0878 0.0341 0.0027 362 LEU A C 2477 O O . LEU A 308 ? 0.3827 0.2967 0.2759 0.0871 0.0283 -0.0010 362 LEU A O 2478 C CB . LEU A 308 ? 0.4074 0.3195 0.3033 0.0874 0.0291 -0.0016 362 LEU A CB 2479 C CG . LEU A 308 ? 0.4629 0.3660 0.3453 0.0960 0.0275 -0.0016 362 LEU A CG 2480 C CD1 . LEU A 308 ? 0.4948 0.3916 0.3717 0.1005 0.0340 0.0032 362 LEU A CD1 2481 C CD2 . LEU A 308 ? 0.4589 0.3615 0.3403 0.0968 0.0213 -0.0060 362 LEU A CD2 2482 N N . ARG A 309 ? 0.3792 0.2879 0.2696 0.0909 0.0397 0.0071 363 ARG A N 2483 C CA . ARG A 309 ? 0.3940 0.3015 0.2800 0.0927 0.0398 0.0079 363 ARG A CA 2484 C C . ARG A 309 ? 0.4057 0.3070 0.2793 0.0994 0.0348 0.0055 363 ARG A C 2485 O O . ARG A 309 ? 0.4145 0.3088 0.2786 0.1057 0.0347 0.0060 363 ARG A O 2486 C CB . ARG A 309 ? 0.4143 0.3193 0.2999 0.0948 0.0476 0.0135 363 ARG A CB 2487 C CG . ARG A 309 ? 0.4650 0.3678 0.3445 0.0979 0.0483 0.0148 363 ARG A CG 2488 C CD . ARG A 309 ? 0.5604 0.4622 0.4423 0.0988 0.0564 0.0204 363 ARG A CD 2489 N NE . ARG A 309 ? 0.6671 0.5653 0.5493 0.1009 0.0619 0.0240 363 ARG A NE 2490 C CZ . ARG A 309 ? 0.6997 0.5895 0.5705 0.1084 0.0641 0.0261 363 ARG A CZ 2491 N NH1 . ARG A 309 ? 0.7190 0.6024 0.5760 0.1153 0.0611 0.0249 363 ARG A NH1 2492 N NH2 . ARG A 309 ? 0.6884 0.5761 0.5617 0.1091 0.0692 0.0294 363 ARG A NH2 2493 N N . GLY A 310 ? 0.3772 0.2810 0.2510 0.0980 0.0301 0.0026 364 GLY A N 2494 C CA . GLY A 310 ? 0.3739 0.2723 0.2373 0.1038 0.0246 0.0000 364 GLY A CA 2495 C C . GLY A 310 ? 0.3974 0.2877 0.2484 0.1117 0.0283 0.0034 364 GLY A C 2496 O O . GLY A 310 ? 0.4013 0.2922 0.2538 0.1111 0.0342 0.0073 364 GLY A O 2497 N N . ALA A 311 ? 0.4309 0.3134 0.2697 0.1192 0.0247 0.0018 365 ALA A N 2498 C CA . ALA A 311 ? 0.4682 0.3416 0.2929 0.1281 0.0276 0.0047 365 ALA A CA 2499 C C . ALA A 311 ? 0.4839 0.3574 0.3058 0.1291 0.0256 0.0039 365 ALA A C 2500 O O . ALA A 311 ? 0.4841 0.3530 0.2986 0.1339 0.0305 0.0077 365 ALA A O 2501 C CB . ALA A 311 ? 0.4906 0.3552 0.3023 0.1363 0.0232 0.0025 365 ALA A CB 2502 N N . VAL A 312 ? 0.4613 0.3395 0.2887 0.1250 0.0185 -0.0007 366 VAL A N 2503 C CA . VAL A 312 ? 0.4730 0.3501 0.2963 0.1270 0.0153 -0.0021 366 VAL A CA 2504 C C . VAL A 312 ? 0.4455 0.3320 0.2817 0.1183 0.0153 -0.0026 366 VAL A C 2505 O O . VAL A 312 ? 0.4396 0.3266 0.2752 0.1183 0.0181 -0.0005 366 VAL A O 2506 C CB . VAL A 312 ? 0.4818 0.3545 0.2983 0.1315 0.0062 -0.0074 366 VAL A CB 2507 C CG1 . VAL A 312 ? 0.4980 0.3699 0.3114 0.1330 0.0023 -0.0091 366 VAL A CG1 2508 C CG2 . VAL A 312 ? 0.5232 0.3854 0.3248 0.1413 0.0062 -0.0067 366 VAL A CG2 2509 N N . GLU A 313 ? 0.4094 0.3031 0.2572 0.1110 0.0128 -0.0050 367 GLU A N 2510 C CA . GLU A 313 ? 0.3923 0.2948 0.2523 0.1027 0.0129 -0.0055 367 GLU A CA 2511 C C . GLU A 313 ? 0.3760 0.2846 0.2465 0.0963 0.0175 -0.0036 367 GLU A C 2512 O O . GLU A 313 ? 0.3594 0.2737 0.2387 0.0908 0.0143 -0.0064 367 GLU A O 2513 C CB . GLU A 313 ? 0.3939 0.2997 0.2584 0.0998 0.0049 -0.0106 367 GLU A CB 2514 C CG . GLU A 313 ? 0.4003 0.3003 0.2555 0.1058 -0.0007 -0.0131 367 GLU A CG 2515 C CD . GLU A 313 ? 0.4255 0.3299 0.2881 0.1016 -0.0079 -0.0177 367 GLU A CD 2516 O OE1 . GLU A 313 ? 0.4313 0.3407 0.3002 0.0969 -0.0081 -0.0178 367 GLU A OE1 2517 O OE2 . GLU A 313 ? 0.4583 0.3611 0.3206 0.1032 -0.0135 -0.0213 367 GLU A OE2 2518 N N . PRO A 314 ? 0.3774 0.2850 0.2479 0.0971 0.0249 0.0010 368 PRO A N 2519 C CA . PRO A 314 ? 0.3636 0.2762 0.2441 0.0915 0.0290 0.0027 368 PRO A CA 2520 C C . PRO A 314 ? 0.3486 0.2699 0.2411 0.0834 0.0284 0.0017 368 PRO A C 2521 O O . PRO A 314 ? 0.3215 0.2478 0.2230 0.0782 0.0297 0.0016 368 PRO A O 2522 C CB . PRO A 314 ? 0.3750 0.2840 0.2527 0.0948 0.0369 0.0081 368 PRO A CB 2523 C CG . PRO A 314 ? 0.4007 0.3051 0.2695 0.1000 0.0373 0.0093 368 PRO A CG 2524 C CD . PRO A 314 ? 0.3933 0.2944 0.2544 0.1035 0.0299 0.0050 368 PRO A CD 2525 N N . ASP A 315 ? 0.3575 0.2800 0.2495 0.0828 0.0263 0.0008 369 ASP A N 2526 C CA . ASP A 315 ? 0.3456 0.2759 0.2479 0.0756 0.0252 -0.0003 369 ASP A CA 2527 C C . ASP A 315 ? 0.3340 0.2680 0.2401 0.0721 0.0184 -0.0049 369 ASP A C 2528 O O . ASP A 315 ? 0.3093 0.2483 0.2213 0.0675 0.0164 -0.0063 369 ASP A O 2529 C CB . ASP A 315 ? 0.3467 0.2766 0.2472 0.0764 0.0268 0.0014 369 ASP A CB 2530 C CG . ASP A 315 ? 0.3860 0.3123 0.2788 0.0803 0.0216 -0.0009 369 ASP A CG 2531 O OD1 . ASP A 315 ? 0.4218 0.3436 0.3078 0.0847 0.0180 -0.0030 369 ASP A OD1 2532 O OD2 . ASP A 315 ? 0.4620 0.3901 0.3558 0.0790 0.0206 -0.0012 369 ASP A OD2 2533 N N . ARG A 316 ? 0.3219 0.2535 0.2250 0.0743 0.0150 -0.0073 370 ARG A N 2534 C CA . ARG A 316 ? 0.3154 0.2508 0.2236 0.0710 0.0092 -0.0114 370 ARG A CA 2535 C C . ARG A 316 ? 0.3144 0.2513 0.2265 0.0693 0.0099 -0.0120 370 ARG A C 2536 O O . ARG A 316 ? 0.3088 0.2405 0.2147 0.0739 0.0115 -0.0109 370 ARG A O 2537 C CB . ARG A 316 ? 0.3236 0.2539 0.2243 0.0761 0.0032 -0.0144 370 ARG A CB 2538 C CG . ARG A 316 ? 0.3240 0.2528 0.2211 0.0777 0.0022 -0.0140 370 ARG A CG 2539 C CD . ARG A 316 ? 0.3412 0.2768 0.2475 0.0714 -0.0006 -0.0160 370 ARG A CD 2540 N NE . ARG A 316 ? 0.3246 0.2601 0.2294 0.0716 -0.0018 -0.0158 370 ARG A NE 2541 C CZ . ARG A 316 ? 0.3321 0.2700 0.2391 0.0692 0.0022 -0.0132 370 ARG A CZ 2542 N NH1 . ARG A 316 ? 0.3098 0.2501 0.2204 0.0667 0.0080 -0.0102 370 ARG A NH1 2543 N NH2 . ARG A 316 ? 0.3261 0.2641 0.2322 0.0691 0.0001 -0.0136 370 ARG A NH2 2544 N N . TYR A 317 ? 0.2984 0.2421 0.2201 0.0630 0.0092 -0.0135 371 TYR A N 2545 C CA . TYR A 317 ? 0.3023 0.2482 0.2287 0.0607 0.0104 -0.0138 371 TYR A CA 2546 C C . TYR A 317 ? 0.2918 0.2400 0.2216 0.0593 0.0054 -0.0176 371 TYR A C 2547 O O . TYR A 317 ? 0.3013 0.2542 0.2370 0.0553 0.0024 -0.0198 371 TYR A O 2548 C CB . TYR A 317 ? 0.2895 0.2416 0.2248 0.0546 0.0139 -0.0125 371 TYR A CB 2549 C CG . TYR A 317 ? 0.2852 0.2364 0.2201 0.0549 0.0190 -0.0088 371 TYR A CG 2550 C CD1 . TYR A 317 ? 0.3313 0.2764 0.2590 0.0603 0.0224 -0.0058 371 TYR A CD1 2551 C CD2 . TYR A 317 ? 0.3014 0.2579 0.2434 0.0499 0.0206 -0.0081 371 TYR A CD2 2552 C CE1 . TYR A 317 ? 0.3301 0.2747 0.2585 0.0605 0.0274 -0.0022 371 TYR A CE1 2553 C CE2 . TYR A 317 ? 0.2803 0.2363 0.2231 0.0500 0.0250 -0.0048 371 TYR A CE2 2554 C CZ . TYR A 317 ? 0.3498 0.3000 0.2862 0.0552 0.0286 -0.0019 371 TYR A CZ 2555 O OH . TYR A 317 ? 0.3215 0.2715 0.2598 0.0553 0.0333 0.0015 371 TYR A OH 2556 N N . VAL A 318 ? 0.2930 0.2382 0.2202 0.0620 0.0048 -0.0183 372 VAL A N 2557 C CA . VAL A 318 ? 0.2842 0.2320 0.2161 0.0603 0.0008 -0.0218 372 VAL A CA 2558 C C . VAL A 318 ? 0.2755 0.2264 0.2127 0.0572 0.0041 -0.0209 372 VAL A C 2559 O O . VAL A 318 ? 0.2960 0.2434 0.2295 0.0598 0.0074 -0.0188 372 VAL A O 2560 C CB . VAL A 318 ? 0.2881 0.2298 0.2129 0.0664 -0.0035 -0.0240 372 VAL A CB 2561 C CG1 . VAL A 318 ? 0.3123 0.2569 0.2431 0.0646 -0.0074 -0.0275 372 VAL A CG1 2562 C CG2 . VAL A 318 ? 0.3061 0.2443 0.2255 0.0698 -0.0074 -0.0251 372 VAL A CG2 2563 N N . ILE A 319 ? 0.2571 0.2144 0.2027 0.0519 0.0033 -0.0226 373 ILE A N 2564 C CA . ILE A 319 ? 0.2610 0.2217 0.2122 0.0484 0.0065 -0.0219 373 ILE A CA 2565 C C . ILE A 319 ? 0.2681 0.2304 0.2226 0.0479 0.0038 -0.0247 373 ILE A C 2566 O O . ILE A 319 ? 0.2749 0.2402 0.2333 0.0463 0.0002 -0.0273 373 ILE A O 2567 C CB . ILE A 319 ? 0.2432 0.2100 0.2013 0.0428 0.0085 -0.0211 373 ILE A CB 2568 C CG1 . ILE A 319 ? 0.2708 0.2360 0.2259 0.0435 0.0108 -0.0185 373 ILE A CG1 2569 C CG2 . ILE A 319 ? 0.2313 0.2013 0.1950 0.0396 0.0115 -0.0207 373 ILE A CG2 2570 C CD1 . ILE A 319 ? 0.3397 0.3106 0.3010 0.0382 0.0117 -0.0183 373 ILE A CD1 2571 N N . LEU A 320 ? 0.2556 0.2162 0.2094 0.0492 0.0058 -0.0240 374 LEU A N 2572 C CA . LEU A 320 ? 0.2508 0.2137 0.2087 0.0480 0.0039 -0.0265 374 LEU A CA 2573 C C . LEU A 320 ? 0.2468 0.2136 0.2105 0.0440 0.0074 -0.0255 374 LEU A C 2574 O O . LEU A 320 ? 0.2764 0.2406 0.2383 0.0451 0.0109 -0.0231 374 LEU A O 2575 C CB . LEU A 320 ? 0.2578 0.2147 0.2096 0.0533 0.0027 -0.0269 374 LEU A CB 2576 C CG . LEU A 320 ? 0.2709 0.2295 0.2267 0.0526 0.0010 -0.0294 374 LEU A CG 2577 C CD1 . LEU A 320 ? 0.2761 0.2388 0.2374 0.0507 -0.0034 -0.0329 374 LEU A CD1 2578 C CD2 . LEU A 320 ? 0.2847 0.2364 0.2330 0.0584 0.0006 -0.0290 374 LEU A CD2 2579 N N . GLY A 321 ? 0.2478 0.2206 0.2185 0.0396 0.0066 -0.0273 375 GLY A N 2580 C CA . GLY A 321 ? 0.2381 0.2145 0.2139 0.0359 0.0096 -0.0265 375 GLY A CA 2581 C C . GLY A 321 ? 0.2559 0.2366 0.2372 0.0334 0.0083 -0.0291 375 GLY A C 2582 O O . GLY A 321 ? 0.2567 0.2399 0.2404 0.0326 0.0055 -0.0312 375 GLY A O 2583 N N . GLY A 322 ? 0.2498 0.2315 0.2337 0.0322 0.0103 -0.0289 376 GLY A N 2584 C CA . GLY A 322 ? 0.2523 0.2383 0.2415 0.0298 0.0095 -0.0312 376 GLY A CA 2585 C C . GLY A 322 ? 0.2473 0.2344 0.2392 0.0281 0.0122 -0.0304 376 GLY A C 2586 O O . GLY A 322 ? 0.2655 0.2493 0.2554 0.0293 0.0144 -0.0281 376 GLY A O 2587 N N . HIS A 323 ? 0.2374 0.2286 0.2338 0.0255 0.0120 -0.0321 377 HIS A N 2588 C CA . HIS A 323 ? 0.2278 0.2202 0.2271 0.0237 0.0141 -0.0317 377 HIS A CA 2589 C C . HIS A 323 ? 0.2603 0.2504 0.2599 0.0253 0.0144 -0.0321 377 HIS A C 2590 O O . HIS A 323 ? 0.2682 0.2568 0.2662 0.0275 0.0129 -0.0332 377 HIS A O 2591 C CB . HIS A 323 ? 0.2197 0.2173 0.2229 0.0204 0.0139 -0.0332 377 HIS A CB 2592 C CG . HIS A 323 ? 0.1812 0.1816 0.1868 0.0200 0.0127 -0.0358 377 HIS A CG 2593 N ND1 . HIS A 323 ? 0.2156 0.2175 0.2237 0.0192 0.0132 -0.0371 377 HIS A ND1 2594 C CD2 . HIS A 323 ? 0.1994 0.2021 0.2061 0.0200 0.0111 -0.0372 377 HIS A CD2 2595 C CE1 . HIS A 323 ? 0.2237 0.2284 0.2337 0.0190 0.0123 -0.0391 377 HIS A CE1 2596 N NE2 . HIS A 323 ? 0.2261 0.2315 0.2358 0.0193 0.0111 -0.0392 377 HIS A NE2 2597 N N . ARG A 324 ? 0.2523 0.2423 0.2545 0.0242 0.0162 -0.0314 378 ARG A N 2598 C CA . ARG A 324 ? 0.2593 0.2467 0.2622 0.0256 0.0169 -0.0313 378 ARG A CA 2599 C C . ARG A 324 ? 0.2606 0.2513 0.2681 0.0234 0.0166 -0.0333 378 ARG A C 2600 O O . ARG A 324 ? 0.2621 0.2520 0.2708 0.0243 0.0163 -0.0344 378 ARG A O 2601 C CB . ARG A 324 ? 0.2715 0.2552 0.2742 0.0265 0.0195 -0.0282 378 ARG A CB 2602 C CG . ARG A 324 ? 0.2595 0.2400 0.2637 0.0279 0.0209 -0.0274 378 ARG A CG 2603 C CD . ARG A 324 ? 0.2931 0.2703 0.2986 0.0284 0.0239 -0.0240 378 ARG A CD 2604 N NE . ARG A 324 ? 0.2861 0.2664 0.2974 0.0251 0.0243 -0.0242 378 ARG A NE 2605 C CZ . ARG A 324 ? 0.2614 0.2429 0.2731 0.0238 0.0250 -0.0230 378 ARG A CZ 2606 N NH1 . ARG A 324 ? 0.2685 0.2484 0.2753 0.0254 0.0256 -0.0213 378 ARG A NH1 2607 N NH2 . ARG A 324 ? 0.2783 0.2623 0.2955 0.0211 0.0249 -0.0235 378 ARG A NH2 2608 N N . ASP A 325 ? 0.2478 0.2419 0.2576 0.0208 0.0167 -0.0338 379 ASP A N 2609 C CA . ASP A 325 ? 0.2427 0.2395 0.2561 0.0191 0.0163 -0.0358 379 ASP A CA 2610 C C . ASP A 325 ? 0.2491 0.2487 0.2624 0.0192 0.0149 -0.0383 379 ASP A C 2611 O O . ASP A 325 ? 0.2461 0.2472 0.2578 0.0193 0.0142 -0.0386 379 ASP A O 2612 C CB . ASP A 325 ? 0.2308 0.2301 0.2458 0.0167 0.0164 -0.0357 379 ASP A CB 2613 C CG . ASP A 325 ? 0.2259 0.2280 0.2388 0.0158 0.0158 -0.0361 379 ASP A CG 2614 O OD1 . ASP A 325 ? 0.2375 0.2383 0.2479 0.0166 0.0159 -0.0346 379 ASP A OD1 2615 O OD2 . ASP A 325 ? 0.2320 0.2372 0.2457 0.0144 0.0153 -0.0377 379 ASP A OD2 2616 N N . SER A 326 ? 0.2474 0.2479 0.2629 0.0192 0.0145 -0.0402 380 SER A N 2617 C CA . SER A 326 ? 0.2533 0.2565 0.2692 0.0195 0.0135 -0.0426 380 SER A CA 2618 C C . SER A 326 ? 0.2613 0.2671 0.2793 0.0183 0.0134 -0.0446 380 SER A C 2619 O O . SER A 326 ? 0.2667 0.2714 0.2861 0.0177 0.0135 -0.0444 380 SER A O 2620 C CB . SER A 326 ? 0.2590 0.2598 0.2747 0.0217 0.0129 -0.0432 380 SER A CB 2621 O OG . SER A 326 ? 0.2734 0.2718 0.2907 0.0220 0.0133 -0.0431 380 SER A OG 2622 N N . TRP A 327 ? 0.2598 0.2689 0.2781 0.0181 0.0131 -0.0464 381 TRP A N 2623 C CA . TRP A 327 ? 0.2741 0.2852 0.2933 0.0178 0.0130 -0.0484 381 TRP A CA 2624 C C . TRP A 327 ? 0.2834 0.2926 0.3042 0.0189 0.0123 -0.0497 381 TRP A C 2625 O O . TRP A 327 ? 0.2759 0.2843 0.2977 0.0187 0.0119 -0.0505 381 TRP A O 2626 C CB . TRP A 327 ? 0.2656 0.2807 0.2848 0.0177 0.0135 -0.0498 381 TRP A CB 2627 C CG . TRP A 327 ? 0.2519 0.2688 0.2697 0.0162 0.0143 -0.0486 381 TRP A CG 2628 C CD1 . TRP A 327 ? 0.2611 0.2796 0.2789 0.0157 0.0149 -0.0475 381 TRP A CD1 2629 C CD2 . TRP A 327 ? 0.2654 0.2821 0.2818 0.0152 0.0144 -0.0483 381 TRP A CD2 2630 N NE1 . TRP A 327 ? 0.2828 0.3023 0.2990 0.0143 0.0155 -0.0464 381 TRP A NE1 2631 C CE2 . TRP A 327 ? 0.2769 0.2952 0.2920 0.0141 0.0152 -0.0469 381 TRP A CE2 2632 C CE3 . TRP A 327 ? 0.2624 0.2776 0.2789 0.0153 0.0136 -0.0492 381 TRP A CE3 2633 C CZ2 . TRP A 327 ? 0.2592 0.2776 0.2725 0.0132 0.0153 -0.0464 381 TRP A CZ2 2634 C CZ3 . TRP A 327 ? 0.2567 0.2719 0.2718 0.0144 0.0134 -0.0489 381 TRP A CZ3 2635 C CH2 . TRP A 327 ? 0.2664 0.2832 0.2797 0.0134 0.0143 -0.0474 381 TRP A CH2 2636 N N . VAL A 328 ? 0.2913 0.2994 0.3125 0.0204 0.0120 -0.0501 382 VAL A N 2637 C CA . VAL A 328 ? 0.2972 0.3029 0.3197 0.0216 0.0113 -0.0510 382 VAL A CA 2638 C C . VAL A 328 ? 0.2952 0.2973 0.3170 0.0230 0.0113 -0.0493 382 VAL A C 2639 O O . VAL A 328 ? 0.2930 0.2924 0.3142 0.0228 0.0121 -0.0470 382 VAL A O 2640 C CB . VAL A 328 ? 0.2942 0.3022 0.3177 0.0225 0.0108 -0.0539 382 VAL A CB 2641 C CG1 . VAL A 328 ? 0.3212 0.3265 0.3464 0.0236 0.0099 -0.0550 382 VAL A CG1 2642 C CG2 . VAL A 328 ? 0.3031 0.3144 0.3262 0.0217 0.0111 -0.0553 382 VAL A CG2 2643 N N . PHE A 329 ? 0.2869 0.2887 0.3085 0.0247 0.0106 -0.0504 383 PHE A N 2644 C CA . PHE A 329 ? 0.2730 0.2707 0.2929 0.0266 0.0104 -0.0490 383 PHE A CA 2645 C C . PHE A 329 ? 0.2717 0.2687 0.2889 0.0271 0.0103 -0.0475 383 PHE A C 2646 O O . PHE A 329 ? 0.2775 0.2704 0.2922 0.0288 0.0105 -0.0457 383 PHE A O 2647 C CB . PHE A 329 ? 0.2751 0.2720 0.2956 0.0286 0.0093 -0.0508 383 PHE A CB 2648 C CG . PHE A 329 ? 0.2783 0.2751 0.3012 0.0284 0.0092 -0.0523 383 PHE A CG 2649 C CD1 . PHE A 329 ? 0.2827 0.2756 0.3064 0.0286 0.0097 -0.0509 383 PHE A CD1 2650 C CD2 . PHE A 329 ? 0.3131 0.3136 0.3378 0.0280 0.0086 -0.0551 383 PHE A CD2 2651 C CE1 . PHE A 329 ? 0.3186 0.3112 0.3452 0.0285 0.0092 -0.0524 383 PHE A CE1 2652 C CE2 . PHE A 329 ? 0.3230 0.3232 0.3496 0.0281 0.0081 -0.0567 383 PHE A CE2 2653 C CZ . PHE A 329 ? 0.3048 0.3011 0.3326 0.0282 0.0082 -0.0554 383 PHE A CZ 2654 N N . GLY A 330 ? 0.2776 0.2785 0.2953 0.0259 0.0101 -0.0482 384 GLY A N 2655 C CA . GLY A 330 ? 0.2636 0.2639 0.2792 0.0262 0.0097 -0.0468 384 GLY A CA 2656 C C . GLY A 330 ? 0.2774 0.2753 0.2915 0.0289 0.0080 -0.0474 384 GLY A C 2657 O O . GLY A 330 ? 0.2817 0.2770 0.2929 0.0302 0.0074 -0.0461 384 GLY A O 2658 N N . GLY A 331 ? 0.2752 0.2743 0.2915 0.0298 0.0069 -0.0496 385 GLY A N 2659 C CA . GLY A 331 ? 0.2739 0.2703 0.2889 0.0327 0.0048 -0.0505 385 GLY A CA 2660 C C . GLY A 331 ? 0.2726 0.2697 0.2874 0.0332 0.0032 -0.0506 385 GLY A C 2661 O O . GLY A 331 ? 0.2796 0.2727 0.2910 0.0358 0.0015 -0.0502 385 GLY A O 2662 N N . ILE A 332 ? 0.2726 0.2746 0.2909 0.0308 0.0036 -0.0512 386 ILE A N 2663 C CA . ILE A 332 ? 0.2706 0.2730 0.2892 0.0310 0.0021 -0.0510 386 ILE A CA 2664 C C . ILE A 332 ? 0.2668 0.2690 0.2828 0.0292 0.0038 -0.0486 386 ILE A C 2665 O O . ILE A 332 ? 0.2938 0.2926 0.3061 0.0305 0.0030 -0.0472 386 ILE A O 2666 C CB . ILE A 332 ? 0.2630 0.2707 0.2878 0.0297 0.0015 -0.0529 386 ILE A CB 2667 C CG1 . ILE A 332 ? 0.2906 0.2981 0.3184 0.0319 -0.0007 -0.0554 386 ILE A CG1 2668 C CG2 . ILE A 332 ? 0.2750 0.2838 0.3012 0.0290 0.0004 -0.0524 386 ILE A CG2 2669 C CD1 . ILE A 332 ? 0.3358 0.3487 0.3708 0.0306 -0.0006 -0.0571 386 ILE A CD1 2670 N N . ASP A 333 ? 0.2670 0.2726 0.2849 0.0265 0.0059 -0.0483 387 ASP A N 2671 C CA . ASP A 333 ? 0.2610 0.2673 0.2774 0.0245 0.0074 -0.0464 387 ASP A CA 2672 C C . ASP A 333 ? 0.2494 0.2532 0.2633 0.0241 0.0090 -0.0447 387 ASP A C 2673 O O . ASP A 333 ? 0.2744 0.2798 0.2898 0.0229 0.0102 -0.0453 387 ASP A O 2674 C CB . ASP A 333 ? 0.2736 0.2851 0.2937 0.0221 0.0085 -0.0471 387 ASP A CB 2675 C CG . ASP A 333 ? 0.2740 0.2865 0.2928 0.0201 0.0097 -0.0454 387 ASP A CG 2676 O OD1 . ASP A 333 ? 0.2558 0.2651 0.2714 0.0205 0.0096 -0.0437 387 ASP A OD1 2677 O OD2 . ASP A 333 ? 0.2689 0.2852 0.2899 0.0183 0.0109 -0.0457 387 ASP A OD2 2678 N N . PRO A 334 ? 0.2486 0.2485 0.2589 0.0252 0.0092 -0.0427 388 PRO A N 2679 C CA . PRO A 334 ? 0.2423 0.2395 0.2495 0.0270 0.0079 -0.0417 388 PRO A CA 2680 C C . PRO A 334 ? 0.2550 0.2469 0.2585 0.0305 0.0071 -0.0413 388 PRO A C 2681 O O . PRO A 334 ? 0.2643 0.2528 0.2638 0.0327 0.0060 -0.0404 388 PRO A O 2682 C CB . PRO A 334 ? 0.2460 0.2422 0.2512 0.0258 0.0096 -0.0392 388 PRO A CB 2683 C CG . PRO A 334 ? 0.2337 0.2288 0.2396 0.0253 0.0116 -0.0385 388 PRO A CG 2684 C CD . PRO A 334 ? 0.2435 0.2414 0.2528 0.0246 0.0111 -0.0409 388 PRO A CD 2685 N N . GLN A 335 ? 0.2593 0.2499 0.2634 0.0314 0.0075 -0.0419 389 GLN A N 2686 C CA . GLN A 335 ? 0.2826 0.2673 0.2822 0.0349 0.0074 -0.0407 389 GLN A CA 2687 C C . GLN A 335 ? 0.2748 0.2570 0.2717 0.0382 0.0044 -0.0420 389 GLN A C 2688 O O . GLN A 335 ? 0.2946 0.2714 0.2860 0.0415 0.0043 -0.0406 389 GLN A O 2689 C CB . GLN A 335 ? 0.2686 0.2518 0.2693 0.0353 0.0087 -0.0406 389 GLN A CB 2690 C CG . GLN A 335 ? 0.2696 0.2550 0.2739 0.0323 0.0110 -0.0398 389 GLN A CG 2691 C CD . GLN A 335 ? 0.2550 0.2389 0.2578 0.0315 0.0131 -0.0369 389 GLN A CD 2692 O OE1 . GLN A 335 ? 0.2916 0.2720 0.2901 0.0335 0.0133 -0.0350 389 GLN A OE1 2693 N NE2 . GLN A 335 ? 0.2567 0.2429 0.2631 0.0288 0.0144 -0.0365 389 GLN A NE2 2694 N N . SER A 336 ? 0.2808 0.2666 0.2814 0.0376 0.0021 -0.0447 390 SER A N 2695 C CA . SER A 336 ? 0.2993 0.2826 0.2978 0.0407 -0.0013 -0.0460 390 SER A CA 2696 C C . SER A 336 ? 0.2971 0.2778 0.2914 0.0418 -0.0019 -0.0445 390 SER A C 2697 O O . SER A 336 ? 0.3016 0.2777 0.2913 0.0456 -0.0043 -0.0448 390 SER A O 2698 C CB . SER A 336 ? 0.3032 0.2909 0.3079 0.0398 -0.0038 -0.0491 390 SER A CB 2699 O OG . SER A 336 ? 0.3505 0.3434 0.3596 0.0364 -0.0029 -0.0491 390 SER A OG 2700 N N . GLY A 337 ? 0.2796 0.2632 0.2753 0.0388 0.0000 -0.0431 391 GLY A N 2701 C CA . GLY A 337 ? 0.2689 0.2502 0.2605 0.0397 -0.0001 -0.0413 391 GLY A CA 2702 C C . GLY A 337 ? 0.2752 0.2513 0.2607 0.0417 0.0023 -0.0383 391 GLY A C 2703 O O . GLY A 337 ? 0.2951 0.2661 0.2744 0.0452 0.0014 -0.0373 391 GLY A O 2704 N N . ALA A 338 ? 0.2698 0.2468 0.2570 0.0398 0.0055 -0.0369 392 ALA A N 2705 C CA . ALA A 338 ? 0.2804 0.2528 0.2633 0.0414 0.0085 -0.0336 392 ALA A CA 2706 C C . ALA A 338 ? 0.2814 0.2473 0.2584 0.0462 0.0082 -0.0329 392 ALA A C 2707 O O . ALA A 338 ? 0.2808 0.2417 0.2522 0.0491 0.0098 -0.0303 392 ALA A O 2708 C CB . ALA A 338 ? 0.2595 0.2343 0.2468 0.0382 0.0115 -0.0326 392 ALA A CB 2709 N N . ALA A 339 ? 0.2971 0.2630 0.2753 0.0474 0.0060 -0.0353 393 ALA A N 2710 C CA . ALA A 339 ? 0.2996 0.2591 0.2718 0.0523 0.0053 -0.0350 393 ALA A CA 2711 C C . ALA A 339 ? 0.3030 0.2584 0.2688 0.0563 0.0025 -0.0353 393 ALA A C 2712 O O . ALA A 339 ? 0.3029 0.2515 0.2610 0.0610 0.0029 -0.0336 393 ALA A O 2713 C CB . ALA A 339 ? 0.2971 0.2581 0.2727 0.0525 0.0029 -0.0380 393 ALA A CB 2714 N N . VAL A 340 ? 0.3044 0.2636 0.2733 0.0547 -0.0005 -0.0376 394 VAL A N 2715 C CA . VAL A 340 ? 0.3069 0.2628 0.2707 0.0581 -0.0037 -0.0383 394 VAL A CA 2716 C C . VAL A 340 ? 0.3110 0.2636 0.2692 0.0593 -0.0011 -0.0350 394 VAL A C 2717 O O . VAL A 340 ? 0.2986 0.2448 0.2486 0.0643 -0.0020 -0.0342 394 VAL A O 2718 C CB . VAL A 340 ? 0.3026 0.2639 0.2728 0.0555 -0.0074 -0.0415 394 VAL A CB 2719 C CG1 . VAL A 340 ? 0.2884 0.2471 0.2546 0.0578 -0.0100 -0.0416 394 VAL A CG1 2720 C CG2 . VAL A 340 ? 0.3195 0.2815 0.2932 0.0568 -0.0111 -0.0450 394 VAL A CG2 2721 N N . VAL A 341 ? 0.3027 0.2595 0.2649 0.0550 0.0019 -0.0333 395 VAL A N 2722 C CA . VAL A 341 ? 0.3047 0.2588 0.2625 0.0559 0.0048 -0.0301 395 VAL A CA 2723 C C . VAL A 341 ? 0.3106 0.2582 0.2621 0.0598 0.0081 -0.0269 395 VAL A C 2724 O O . VAL A 341 ? 0.3192 0.2616 0.2635 0.0637 0.0089 -0.0250 395 VAL A O 2725 C CB . VAL A 341 ? 0.3069 0.2664 0.2706 0.0506 0.0077 -0.0287 395 VAL A CB 2726 C CG1 . VAL A 341 ? 0.2912 0.2474 0.2504 0.0519 0.0111 -0.0250 395 VAL A CG1 2727 C CG2 . VAL A 341 ? 0.3114 0.2767 0.2804 0.0472 0.0049 -0.0312 395 VAL A CG2 2728 N N . HIS A 342 ? 0.3152 0.2630 0.2695 0.0590 0.0101 -0.0265 396 HIS A N 2729 C CA . HIS A 342 ? 0.3143 0.2561 0.2640 0.0623 0.0138 -0.0232 396 HIS A CA 2730 C C . HIS A 342 ? 0.3422 0.2765 0.2820 0.0689 0.0117 -0.0233 396 HIS A C 2731 O O . HIS A 342 ? 0.3530 0.2812 0.2856 0.0730 0.0146 -0.0199 396 HIS A O 2732 C CB . HIS A 342 ? 0.3233 0.2671 0.2788 0.0600 0.0151 -0.0236 396 HIS A CB 2733 C CG . HIS A 342 ? 0.3534 0.2948 0.3099 0.0599 0.0201 -0.0198 396 HIS A CG 2734 N ND1 . HIS A 342 ? 0.3459 0.2887 0.3052 0.0576 0.0237 -0.0170 396 HIS A ND1 2735 C CD2 . HIS A 342 ? 0.3736 0.3115 0.3298 0.0617 0.0222 -0.0184 396 HIS A CD2 2736 C CE1 . HIS A 342 ? 0.3729 0.3131 0.3340 0.0580 0.0278 -0.0140 396 HIS A CE1 2737 N NE2 . HIS A 342 ? 0.3637 0.3006 0.3227 0.0605 0.0271 -0.0146 396 HIS A NE2 2738 N N . GLU A 343 ? 0.3483 0.2829 0.2878 0.0703 0.0067 -0.0271 397 GLU A N 2739 C CA . GLU A 343 ? 0.3741 0.3015 0.3042 0.0770 0.0037 -0.0279 397 GLU A CA 2740 C C . GLU A 343 ? 0.3848 0.3091 0.3084 0.0799 0.0020 -0.0276 397 GLU A C 2741 O O . GLU A 343 ? 0.3832 0.2999 0.2967 0.0861 0.0019 -0.0263 397 GLU A O 2742 C CB . GLU A 343 ? 0.3834 0.3123 0.3163 0.0773 -0.0015 -0.0324 397 GLU A CB 2743 C CG . GLU A 343 ? 0.4031 0.3243 0.3264 0.0846 -0.0058 -0.0340 397 GLU A CG 2744 C CD . GLU A 343 ? 0.4629 0.3762 0.3778 0.0897 -0.0029 -0.0312 397 GLU A CD 2745 O OE1 . GLU A 343 ? 0.4313 0.3446 0.3473 0.0881 0.0027 -0.0274 397 GLU A OE1 2746 O OE2 . GLU A 343 ? 0.4530 0.3600 0.3603 0.0957 -0.0065 -0.0328 397 GLU A OE2 2747 N N . ILE A 344 ? 0.3718 0.3019 0.3009 0.0758 0.0008 -0.0288 398 ILE A N 2748 C CA . ILE A 344 ? 0.3495 0.2771 0.2731 0.0782 -0.0004 -0.0284 398 ILE A CA 2749 C C . ILE A 344 ? 0.3537 0.2769 0.2711 0.0805 0.0049 -0.0236 398 ILE A C 2750 O O . ILE A 344 ? 0.3725 0.2891 0.2802 0.0861 0.0044 -0.0226 398 ILE A O 2751 C CB . ILE A 344 ? 0.3277 0.2627 0.2593 0.0728 -0.0025 -0.0304 398 ILE A CB 2752 C CG1 . ILE A 344 ? 0.3350 0.2723 0.2707 0.0727 -0.0086 -0.0350 398 ILE A CG1 2753 C CG2 . ILE A 344 ? 0.3066 0.2395 0.2333 0.0745 -0.0026 -0.0291 398 ILE A CG2 2754 C CD1 . ILE A 344 ? 0.3000 0.2455 0.2459 0.0666 -0.0099 -0.0369 398 ILE A CD1 2755 N N . VAL A 345 ? 0.3587 0.2852 0.2817 0.0764 0.0100 -0.0208 399 VAL A N 2756 C CA . VAL A 345 ? 0.3728 0.2955 0.2917 0.0782 0.0157 -0.0161 399 VAL A CA 2757 C C . VAL A 345 ? 0.3885 0.3026 0.2980 0.0848 0.0177 -0.0138 399 VAL A C 2758 O O . VAL A 345 ? 0.4000 0.3080 0.3008 0.0897 0.0200 -0.0109 399 VAL A O 2759 C CB . VAL A 345 ? 0.3579 0.2858 0.2861 0.0725 0.0204 -0.0138 399 VAL A CB 2760 C CG1 . VAL A 345 ? 0.3742 0.2977 0.2993 0.0747 0.0267 -0.0087 399 VAL A CG1 2761 C CG2 . VAL A 345 ? 0.3335 0.2695 0.2701 0.0662 0.0191 -0.0156 399 VAL A CG2 2762 N N . ARG A 346 ? 0.4078 0.3215 0.3190 0.0850 0.0167 -0.0151 400 ARG A N 2763 C CA . ARG A 346 ? 0.4133 0.3186 0.3156 0.0914 0.0183 -0.0131 400 ARG A CA 2764 C C . ARG A 346 ? 0.4347 0.3330 0.3250 0.0985 0.0146 -0.0143 400 ARG A C 2765 O O . ARG A 346 ? 0.4521 0.3428 0.3327 0.1043 0.0179 -0.0108 400 ARG A O 2766 C CB . ARG A 346 ? 0.4076 0.3138 0.3138 0.0904 0.0169 -0.0150 400 ARG A CB 2767 C CG . ARG A 346 ? 0.4309 0.3283 0.3286 0.0965 0.0200 -0.0119 400 ARG A CG 2768 C CD . ARG A 346 ? 0.4372 0.3346 0.3369 0.0968 0.0169 -0.0148 400 ARG A CD 2769 N NE . ARG A 346 ? 0.4319 0.3287 0.3281 0.0992 0.0098 -0.0196 400 ARG A NE 2770 C CZ . ARG A 346 ? 0.4805 0.3696 0.3651 0.1065 0.0071 -0.0201 400 ARG A CZ 2771 N NH1 . ARG A 346 ? 0.4761 0.3652 0.3593 0.1083 0.0001 -0.0249 400 ARG A NH1 2772 N NH2 . ARG A 346 ? 0.4835 0.3644 0.3578 0.1123 0.0113 -0.0158 400 ARG A NH2 2773 N N . SER A 347 ? 0.4363 0.3368 0.3275 0.0982 0.0079 -0.0190 401 SER A N 2774 C CA A SER A 347 ? 0.4400 0.3341 0.3207 0.1048 0.0031 -0.0210 401 SER A CA 2775 C CA B SER A 347 ? 0.4544 0.3485 0.3352 0.1048 0.0033 -0.0209 401 SER A CA 2776 C C . SER A 347 ? 0.4622 0.3534 0.3366 0.1073 0.0053 -0.0184 401 SER A C 2777 O O . SER A 347 ? 0.4658 0.3483 0.3277 0.1147 0.0056 -0.0168 401 SER A O 2778 C CB A SER A 347 ? 0.4334 0.3313 0.3187 0.1034 -0.0046 -0.0268 401 SER A CB 2779 C CB B SER A 347 ? 0.4480 0.3461 0.3339 0.1031 -0.0042 -0.0266 401 SER A CB 2780 O OG A SER A 347 ? 0.3894 0.2804 0.2646 0.1103 -0.0098 -0.0289 401 SER A OG 2781 O OG B SER A 347 ? 0.4843 0.3837 0.3744 0.1020 -0.0054 -0.0285 401 SER A OG 2782 N N . PHE A 348 ? 0.4356 0.3335 0.3176 0.1015 0.0069 -0.0178 402 PHE A N 2783 C CA . PHE A 348 ? 0.4311 0.3264 0.3075 0.1037 0.0093 -0.0151 402 PHE A CA 2784 C C . PHE A 348 ? 0.4441 0.3336 0.3141 0.1074 0.0167 -0.0094 402 PHE A C 2785 O O . PHE A 348 ? 0.4680 0.3508 0.3274 0.1135 0.0182 -0.0072 402 PHE A O 2786 C CB . PHE A 348 ? 0.4138 0.3175 0.3001 0.0966 0.0102 -0.0152 402 PHE A CB 2787 C CG . PHE A 348 ? 0.4088 0.3161 0.2981 0.0948 0.0036 -0.0197 402 PHE A CG 2788 C CD1 . PHE A 348 ? 0.4394 0.3414 0.3198 0.1003 -0.0003 -0.0211 402 PHE A CD1 2789 C CD2 . PHE A 348 ? 0.4027 0.3187 0.3039 0.0877 0.0016 -0.0223 402 PHE A CD2 2790 C CE1 . PHE A 348 ? 0.4216 0.3268 0.3057 0.0986 -0.0064 -0.0251 402 PHE A CE1 2791 C CE2 . PHE A 348 ? 0.3857 0.3051 0.2905 0.0860 -0.0039 -0.0260 402 PHE A CE2 2792 C CZ . PHE A 348 ? 0.3935 0.3077 0.2904 0.0912 -0.0081 -0.0275 402 PHE A CZ 2793 N N . GLY A 349 ? 0.4270 0.3186 0.3032 0.1042 0.0214 -0.0070 403 GLY A N 2794 C CA . GLY A 349 ? 0.4595 0.3461 0.3318 0.1072 0.0289 -0.0013 403 GLY A CA 2795 C C . GLY A 349 ? 0.4831 0.3594 0.3418 0.1160 0.0289 -0.0001 403 GLY A C 2796 O O . GLY A 349 ? 0.5033 0.3730 0.3537 0.1212 0.0341 0.0042 403 GLY A O 2797 N N . THR A 350 ? 0.5038 0.3784 0.3601 0.1179 0.0233 -0.0041 404 THR A N 2798 C CA . THR A 350 ? 0.5253 0.3898 0.3678 0.1269 0.0220 -0.0038 404 THR A CA 2799 C C . THR A 350 ? 0.5440 0.4018 0.3738 0.1338 0.0204 -0.0036 404 THR A C 2800 O O . THR A 350 ? 0.5627 0.4116 0.3805 0.1411 0.0241 0.0000 404 THR A O 2801 C CB . THR A 350 ? 0.5225 0.3867 0.3652 0.1277 0.0152 -0.0088 404 THR A CB 2802 O OG1 A THR A 350 ? 0.4974 0.3669 0.3507 0.1221 0.0175 -0.0085 404 THR A OG1 2803 O OG1 B THR A 350 ? 0.5327 0.3984 0.3747 0.1282 0.0073 -0.0141 404 THR A OG1 2804 C CG2 A THR A 350 ? 0.5100 0.3633 0.3379 0.1373 0.0135 -0.0087 404 THR A CG2 2805 C CG2 B THR A 350 ? 0.5036 0.3752 0.3594 0.1206 0.0160 -0.0098 404 THR A CG2 2806 N N A LEU A 351 ? 0.5394 0.4013 0.3717 0.1316 0.0151 -0.0073 405 LEU A N 2807 N N B LEU A 351 ? 0.5340 0.3958 0.3662 0.1317 0.0149 -0.0074 405 LEU A N 2808 C CA A LEU A 351 ? 0.5492 0.4048 0.3697 0.1381 0.0130 -0.0075 405 LEU A CA 2809 C CA B LEU A 351 ? 0.5382 0.3940 0.3590 0.1380 0.0130 -0.0075 405 LEU A CA 2810 C C A LEU A 351 ? 0.5515 0.4058 0.3698 0.1387 0.0209 -0.0018 405 LEU A C 2811 C C B LEU A 351 ? 0.5426 0.3970 0.3610 0.1386 0.0208 -0.0018 405 LEU A C 2812 O O A LEU A 351 ? 0.5549 0.4008 0.3601 0.1465 0.0230 0.0008 405 LEU A O 2813 O O B LEU A 351 ? 0.5506 0.3966 0.3559 0.1464 0.0228 0.0006 405 LEU A O 2814 C CB A LEU A 351 ? 0.5562 0.4165 0.3809 0.1355 0.0052 -0.0128 405 LEU A CB 2815 C CB B LEU A 351 ? 0.5348 0.3956 0.3603 0.1351 0.0055 -0.0127 405 LEU A CB 2816 C CG A LEU A 351 ? 0.5657 0.4307 0.3982 0.1322 -0.0023 -0.0187 405 LEU A CG 2817 C CG B LEU A 351 ? 0.5266 0.3850 0.3493 0.1383 -0.0034 -0.0186 405 LEU A CG 2818 C CD1 A LEU A 351 ? 0.5705 0.4404 0.4082 0.1292 -0.0081 -0.0227 405 LEU A CD1 2819 C CD1 B LEU A 351 ? 0.5090 0.3723 0.3413 0.1336 -0.0045 -0.0205 405 LEU A CD1 2820 C CD2 A LEU A 351 ? 0.6045 0.4616 0.4275 0.1395 -0.0071 -0.0213 405 LEU A CD2 2821 C CD2 B LEU A 351 ? 0.5319 0.3943 0.3588 0.1360 -0.0100 -0.0229 405 LEU A CD2 2822 N N . LYS A 352 ? 0.5222 0.3848 0.3533 0.1307 0.0252 0.0001 406 LYS A N 2823 C CA . LYS A 352 ? 0.5381 0.4006 0.3695 0.1304 0.0328 0.0055 406 LYS A CA 2824 C C . LYS A 352 ? 0.5569 0.4108 0.3795 0.1368 0.0400 0.0111 406 LYS A C 2825 O O . LYS A 352 ? 0.5607 0.4091 0.3747 0.1420 0.0444 0.0149 406 LYS A O 2826 C CB . LYS A 352 ? 0.5275 0.3999 0.3746 0.1209 0.0360 0.0065 406 LYS A CB 2827 C CG . LYS A 352 ? 0.5710 0.4437 0.4191 0.1205 0.0427 0.0113 406 LYS A CG 2828 C CD . LYS A 352 ? 0.6554 0.5282 0.5095 0.1188 0.0507 0.0165 406 LYS A CD 2829 C CE . LYS A 352 ? 0.6740 0.5502 0.5344 0.1158 0.0565 0.0204 406 LYS A CE 2830 N NZ . LYS A 352 ? 0.7269 0.6047 0.5966 0.1126 0.0631 0.0244 406 LYS A NZ 2831 N N . LYS A 353 ? 0.5625 0.4156 0.3875 0.1364 0.0413 0.0117 407 LYS A N 2832 C CA . LYS A 353 ? 0.5962 0.4410 0.4133 0.1424 0.0480 0.0171 407 LYS A CA 2833 C C . LYS A 353 ? 0.6242 0.4575 0.4227 0.1533 0.0469 0.0176 407 LYS A C 2834 O O . LYS A 353 ? 0.6491 0.4748 0.4392 0.1592 0.0538 0.0232 407 LYS A O 2835 C CB . LYS A 353 ? 0.5939 0.4399 0.4173 0.1397 0.0486 0.0169 407 LYS A CB 2836 C CG . LYS A 353 ? 0.6174 0.4717 0.4569 0.1312 0.0534 0.0191 407 LYS A CG 2837 C CD . LYS A 353 ? 0.6328 0.4903 0.4804 0.1272 0.0517 0.0171 407 LYS A CD 2838 C CE . LYS A 353 ? 0.6048 0.4707 0.4686 0.1186 0.0555 0.0186 407 LYS A CE 2839 N NZ . LYS A 353 ? 0.6500 0.5165 0.5195 0.1167 0.0560 0.0185 407 LYS A NZ 2840 N N . GLU A 354 ? 0.6396 0.4714 0.4319 0.1560 0.0382 0.0120 408 GLU A N 2841 C CA . GLU A 354 ? 0.6763 0.4973 0.4505 0.1665 0.0352 0.0113 408 GLU A CA 2842 C C . GLU A 354 ? 0.6754 0.4944 0.4429 0.1697 0.0355 0.0121 408 GLU A C 2843 O O . GLU A 354 ? 0.6893 0.4994 0.4415 0.1786 0.0323 0.0110 408 GLU A O 2844 C CB . GLU A 354 ? 0.6911 0.5113 0.4628 0.1681 0.0250 0.0044 408 GLU A CB 2845 C CG . GLU A 354 ? 0.7485 0.5695 0.5250 0.1663 0.0241 0.0033 408 GLU A CG 2846 C CD . GLU A 354 ? 0.8500 0.6719 0.6271 0.1664 0.0138 -0.0038 408 GLU A CD 2847 O OE1 . GLU A 354 ? 0.8856 0.7122 0.6719 0.1618 0.0121 -0.0058 408 GLU A OE1 2848 O OE2 . GLU A 354 ? 0.8972 0.7152 0.6662 0.1713 0.0072 -0.0074 408 GLU A OE2 2849 N N . GLY A 355 ? 0.6458 0.4728 0.4245 0.1628 0.0391 0.0138 409 GLY A N 2850 C CA . GLY A 355 ? 0.6279 0.4534 0.4014 0.1653 0.0408 0.0154 409 GLY A CA 2851 C C . GLY A 355 ? 0.6186 0.4505 0.3977 0.1608 0.0334 0.0101 409 GLY A C 2852 O O . GLY A 355 ? 0.6231 0.4541 0.3982 0.1627 0.0338 0.0108 409 GLY A O 2853 N N . TRP A 356 ? 0.5911 0.4293 0.3795 0.1551 0.0266 0.0048 410 TRP A N 2854 C CA . TRP A 356 ? 0.5735 0.4175 0.3674 0.1512 0.0193 -0.0002 410 TRP A CA 2855 C C . TRP A 356 ? 0.5375 0.3922 0.3468 0.1413 0.0227 0.0010 410 TRP A C 2856 O O . TRP A 356 ? 0.5346 0.3938 0.3531 0.1362 0.0279 0.0036 410 TRP A O 2857 C CB . TRP A 356 ? 0.5794 0.4254 0.3769 0.1497 0.0108 -0.0063 410 TRP A CB 2858 C CG . TRP A 356 ? 0.5806 0.4341 0.3876 0.1439 0.0035 -0.0116 410 TRP A CG 2859 C CD1 . TRP A 356 ? 0.5858 0.4364 0.3872 0.1477 -0.0038 -0.0157 410 TRP A CD1 2860 C CD2 . TRP A 356 ? 0.5502 0.4148 0.3736 0.1339 0.0030 -0.0131 410 TRP A CD2 2861 N NE1 . TRP A 356 ? 0.5748 0.4342 0.3889 0.1404 -0.0085 -0.0195 410 TRP A NE1 2862 C CE2 . TRP A 356 ? 0.5543 0.4223 0.3814 0.1319 -0.0042 -0.0180 410 TRP A CE2 2863 C CE3 . TRP A 356 ? 0.5403 0.4121 0.3754 0.1265 0.0082 -0.0109 410 TRP A CE3 2864 C CZ2 . TRP A 356 ? 0.5013 0.3795 0.3431 0.1230 -0.0062 -0.0203 410 TRP A CZ2 2865 C CZ3 . TRP A 356 ? 0.5312 0.4130 0.3803 0.1178 0.0059 -0.0135 410 TRP A CZ3 2866 C CH2 . TRP A 356 ? 0.4879 0.3727 0.3400 0.1162 -0.0010 -0.0180 410 TRP A CH2 2867 N N . ARG A 357 ? 0.5093 0.3675 0.3210 0.1391 0.0196 -0.0010 411 ARG A N 2868 C CA . ARG A 357 ? 0.4862 0.3547 0.3123 0.1297 0.0209 -0.0010 411 ARG A CA 2869 C C . ARG A 357 ? 0.4651 0.3376 0.2948 0.1271 0.0127 -0.0065 411 ARG A C 2870 O O . ARG A 357 ? 0.4560 0.3228 0.2761 0.1331 0.0078 -0.0088 411 ARG A O 2871 C CB . ARG A 357 ? 0.5018 0.3703 0.3271 0.1299 0.0274 0.0035 411 ARG A CB 2872 C CG . ARG A 357 ? 0.5171 0.3854 0.3457 0.1289 0.0365 0.0093 411 ARG A CG 2873 C CD . ARG A 357 ? 0.5173 0.3874 0.3484 0.1276 0.0427 0.0136 411 ARG A CD 2874 N NE . ARG A 357 ? 0.4845 0.3545 0.3205 0.1265 0.0509 0.0187 411 ARG A NE 2875 C CZ . ARG A 357 ? 0.5325 0.4098 0.3823 0.1188 0.0527 0.0190 411 ARG A CZ 2876 N NH1 . ARG A 357 ? 0.4473 0.3329 0.3073 0.1115 0.0474 0.0146 411 ARG A NH1 2877 N NH2 . ARG A 357 ? 0.4964 0.3725 0.3500 0.1187 0.0598 0.0236 411 ARG A NH2 2878 N N . PRO A 358 ? 0.4302 0.3125 0.2742 0.1182 0.0111 -0.0086 412 PRO A N 2879 C CA . PRO A 358 ? 0.4201 0.3063 0.2684 0.1155 0.0042 -0.0131 412 PRO A CA 2880 C C . PRO A 358 ? 0.4029 0.2885 0.2478 0.1166 0.0049 -0.0119 412 PRO A C 2881 O O . PRO A 358 ? 0.4288 0.3135 0.2720 0.1170 0.0115 -0.0074 412 PRO A O 2882 C CB . PRO A 358 ? 0.3952 0.2920 0.2592 0.1058 0.0044 -0.0144 412 PRO A CB 2883 C CG . PRO A 358 ? 0.4066 0.3051 0.2742 0.1031 0.0125 -0.0095 412 PRO A CG 2884 C CD . PRO A 358 ? 0.4087 0.2979 0.2645 0.1110 0.0158 -0.0066 412 PRO A CD 2885 N N . ARG A 359 ? 0.4130 0.2989 0.2576 0.1170 -0.0017 -0.0159 413 ARG A N 2886 C CA . ARG A 359 ? 0.4055 0.2911 0.2475 0.1178 -0.0016 -0.0151 413 ARG A CA 2887 C C . ARG A 359 ? 0.3950 0.2892 0.2484 0.1097 0.0033 -0.0125 413 ARG A C 2888 O O . ARG A 359 ? 0.3798 0.2730 0.2306 0.1105 0.0086 -0.0088 413 ARG A O 2889 C CB . ARG A 359 ? 0.3981 0.2834 0.2399 0.1188 -0.0103 -0.0202 413 ARG A CB 2890 C CG . ARG A 359 ? 0.4214 0.3071 0.2618 0.1188 -0.0110 -0.0199 413 ARG A CG 2891 C CD . ARG A 359 ? 0.4073 0.2941 0.2509 0.1183 -0.0200 -0.0253 413 ARG A CD 2892 N NE . ARG A 359 ? 0.4383 0.3259 0.2814 0.1178 -0.0202 -0.0248 413 ARG A NE 2893 C CZ . ARG A 359 ? 0.5086 0.3888 0.3396 0.1251 -0.0208 -0.0241 413 ARG A CZ 2894 N NH1 . ARG A 359 ? 0.5151 0.3861 0.3329 0.1338 -0.0216 -0.0241 413 ARG A NH1 2895 N NH2 . ARG A 359 ? 0.4850 0.3665 0.3163 0.1240 -0.0208 -0.0236 413 ARG A NH2 2896 N N . ARG A 360 ? 0.3723 0.2743 0.2378 0.1023 0.0017 -0.0146 414 ARG A N 2897 C CA . ARG A 360 ? 0.3631 0.2735 0.2400 0.0942 0.0052 -0.0131 414 ARG A CA 2898 C C . ARG A 360 ? 0.3519 0.2654 0.2348 0.0907 0.0103 -0.0108 414 ARG A C 2899 O O . ARG A 360 ? 0.3658 0.2766 0.2466 0.0929 0.0098 -0.0114 414 ARG A O 2900 C CB . ARG A 360 ? 0.3291 0.2462 0.2155 0.0884 -0.0004 -0.0172 414 ARG A CB 2901 C CG . ARG A 360 ? 0.3396 0.2541 0.2219 0.0914 -0.0065 -0.0201 414 ARG A CG 2902 C CD . ARG A 360 ? 0.3507 0.2719 0.2433 0.0855 -0.0115 -0.0236 414 ARG A CD 2903 N NE . ARG A 360 ? 0.3364 0.2537 0.2239 0.0894 -0.0170 -0.0260 414 ARG A NE 2904 C CZ . ARG A 360 ? 0.3623 0.2745 0.2449 0.0945 -0.0232 -0.0294 414 ARG A CZ 2905 N NH1 . ARG A 360 ? 0.3339 0.2450 0.2171 0.0957 -0.0251 -0.0312 414 ARG A NH1 2906 N NH2 . ARG A 360 ? 0.3800 0.2881 0.2574 0.0985 -0.0280 -0.0313 414 ARG A NH2 2907 N N . THR A 361 ? 0.3329 0.2517 0.2235 0.0855 0.0150 -0.0082 415 THR A N 2908 C CA . THR A 361 ? 0.3301 0.2522 0.2277 0.0816 0.0194 -0.0063 415 THR A CA 2909 C C . THR A 361 ? 0.3286 0.2560 0.2341 0.0769 0.0155 -0.0099 415 THR A C 2910 O O . THR A 361 ? 0.3233 0.2554 0.2339 0.0732 0.0113 -0.0129 415 THR A O 2911 C CB . THR A 361 ? 0.3179 0.2444 0.2224 0.0772 0.0244 -0.0033 415 THR A CB 2912 O OG1 . THR A 361 ? 0.3402 0.2613 0.2376 0.0821 0.0292 0.0006 415 THR A OG1 2913 C CG2 . THR A 361 ? 0.2813 0.2127 0.1954 0.0720 0.0276 -0.0023 415 THR A CG2 2914 N N . ILE A 362 ? 0.3152 0.2418 0.2218 0.0771 0.0172 -0.0095 416 ILE A N 2915 C CA . ILE A 362 ? 0.3206 0.2525 0.2354 0.0724 0.0147 -0.0123 416 ILE A CA 2916 C C . ILE A 362 ? 0.3120 0.2483 0.2349 0.0675 0.0196 -0.0101 416 ILE A C 2917 O O . ILE A 362 ? 0.3274 0.2606 0.2485 0.0695 0.0243 -0.0067 416 ILE A O 2918 C CB . ILE A 362 ? 0.3264 0.2543 0.2369 0.0762 0.0119 -0.0143 416 ILE A CB 2919 C CG1 . ILE A 362 ? 0.3395 0.2624 0.2418 0.0816 0.0064 -0.0169 416 ILE A CG1 2920 C CG2 . ILE A 362 ? 0.3215 0.2556 0.2413 0.0710 0.0095 -0.0173 416 ILE A CG2 2921 C CD1 . ILE A 362 ? 0.3474 0.2651 0.2442 0.0866 0.0032 -0.0189 416 ILE A CD1 2922 N N . LEU A 363 ? 0.2931 0.2366 0.2251 0.0614 0.0183 -0.0119 417 LEU A N 2923 C CA . LEU A 363 ? 0.2813 0.2295 0.2218 0.0564 0.0216 -0.0108 417 LEU A CA 2924 C C . LEU A 363 ? 0.2884 0.2394 0.2333 0.0543 0.0191 -0.0136 417 LEU A C 2925 O O . LEU A 363 ? 0.2917 0.2454 0.2383 0.0530 0.0147 -0.0170 417 LEU A O 2926 C CB . LEU A 363 ? 0.2632 0.2172 0.2102 0.0513 0.0218 -0.0109 417 LEU A CB 2927 C CG . LEU A 363 ? 0.2886 0.2405 0.2320 0.0530 0.0240 -0.0083 417 LEU A CG 2928 C CD1 . LEU A 363 ? 0.3202 0.2781 0.2707 0.0477 0.0241 -0.0085 417 LEU A CD1 2929 C CD2 . LEU A 363 ? 0.2997 0.2472 0.2407 0.0561 0.0296 -0.0041 417 LEU A CD2 2930 N N . PHE A 364 ? 0.2783 0.2287 0.2255 0.0540 0.0221 -0.0122 418 PHE A N 2931 C CA . PHE A 364 ? 0.2869 0.2402 0.2388 0.0518 0.0203 -0.0147 418 PHE A CA 2932 C C . PHE A 364 ? 0.2806 0.2392 0.2413 0.0464 0.0225 -0.0144 418 PHE A C 2933 O O . PHE A 364 ? 0.3149 0.2729 0.2777 0.0459 0.0265 -0.0115 418 PHE A O 2934 C CB . PHE A 364 ? 0.2739 0.2218 0.2214 0.0560 0.0215 -0.0138 418 PHE A CB 2935 C CG . PHE A 364 ? 0.3091 0.2508 0.2469 0.0620 0.0192 -0.0142 418 PHE A CG 2936 C CD1 . PHE A 364 ? 0.3060 0.2477 0.2425 0.0631 0.0140 -0.0179 418 PHE A CD1 2937 C CD2 . PHE A 364 ? 0.3317 0.2673 0.2618 0.0667 0.0221 -0.0109 418 PHE A CD2 2938 C CE1 . PHE A 364 ? 0.3439 0.2793 0.2712 0.0692 0.0111 -0.0187 418 PHE A CE1 2939 C CE2 . PHE A 364 ? 0.3679 0.2971 0.2880 0.0729 0.0196 -0.0115 418 PHE A CE2 2940 C CZ . PHE A 364 ? 0.3393 0.2684 0.2581 0.0741 0.0137 -0.0157 418 PHE A CZ 2941 N N . ALA A 365 ? 0.2777 0.2415 0.2438 0.0428 0.0198 -0.0174 419 ALA A N 2942 C CA . ALA A 365 ? 0.2634 0.2324 0.2374 0.0379 0.0212 -0.0177 419 ALA A CA 2943 C C . ALA A 365 ? 0.2528 0.2244 0.2309 0.0362 0.0200 -0.0200 419 ALA A C 2944 O O . ALA A 365 ? 0.2653 0.2381 0.2430 0.0364 0.0169 -0.0227 419 ALA A O 2945 C CB . ALA A 365 ? 0.2563 0.2300 0.2332 0.0344 0.0199 -0.0187 419 ALA A CB 2946 N N . SER A 366 ? 0.2432 0.2156 0.2258 0.0345 0.0224 -0.0191 420 SER A N 2947 C CA . SER A 366 ? 0.2419 0.2172 0.2293 0.0323 0.0215 -0.0213 420 SER A CA 2948 C C . SER A 366 ? 0.2397 0.2200 0.2331 0.0280 0.0218 -0.0219 420 SER A C 2949 O O . SER A 366 ? 0.2523 0.2323 0.2490 0.0269 0.0242 -0.0201 420 SER A O 2950 C CB . SER A 366 ? 0.2513 0.2230 0.2393 0.0341 0.0240 -0.0196 420 SER A CB 2951 O OG . SER A 366 ? 0.2549 0.2292 0.2479 0.0321 0.0233 -0.0216 420 SER A OG 2952 N N . TRP A 367 ? 0.2491 0.2335 0.2437 0.0258 0.0195 -0.0242 421 TRP A N 2953 C CA . TRP A 367 ? 0.2134 0.2020 0.2120 0.0223 0.0196 -0.0248 421 TRP A CA 2954 C C . TRP A 367 ? 0.2346 0.2256 0.2380 0.0204 0.0196 -0.0264 421 TRP A C 2955 O O . TRP A 367 ? 0.2382 0.2292 0.2418 0.0211 0.0187 -0.0280 421 TRP A O 2956 C CB . TRP A 367 ? 0.2076 0.1995 0.2056 0.0209 0.0174 -0.0265 421 TRP A CB 2957 C CG . TRP A 367 ? 0.1988 0.1889 0.1926 0.0226 0.0166 -0.0256 421 TRP A CG 2958 C CD1 . TRP A 367 ? 0.1974 0.1877 0.1894 0.0237 0.0142 -0.0271 421 TRP A CD1 2959 C CD2 . TRP A 367 ? 0.2190 0.2069 0.2104 0.0233 0.0179 -0.0232 421 TRP A CD2 2960 N NE1 . TRP A 367 ? 0.2192 0.2074 0.2075 0.0251 0.0136 -0.0259 421 TRP A NE1 2961 C CE2 . TRP A 367 ? 0.2159 0.2026 0.2035 0.0250 0.0160 -0.0235 421 TRP A CE2 2962 C CE3 . TRP A 367 ? 0.2603 0.2472 0.2531 0.0228 0.0204 -0.0209 421 TRP A CE3 2963 C CZ2 . TRP A 367 ? 0.2346 0.2191 0.2188 0.0264 0.0166 -0.0216 421 TRP A CZ2 2964 C CZ3 . TRP A 367 ? 0.2345 0.2194 0.2243 0.0240 0.0213 -0.0188 421 TRP A CZ3 2965 C CH2 . TRP A 367 ? 0.2395 0.2230 0.2245 0.0259 0.0194 -0.0192 421 TRP A CH2 2966 N N . ASP A 368 ? 0.2198 0.2123 0.2267 0.0182 0.0204 -0.0261 422 ASP A N 2967 C CA . ASP A 368 ? 0.2262 0.2208 0.2374 0.0166 0.0199 -0.0279 422 ASP A CA 2968 C C . ASP A 368 ? 0.2212 0.2200 0.2328 0.0144 0.0184 -0.0299 422 ASP A C 2969 O O . ASP A 368 ? 0.2460 0.2459 0.2556 0.0137 0.0181 -0.0294 422 ASP A O 2970 C CB . ASP A 368 ? 0.2086 0.2017 0.2242 0.0160 0.0214 -0.0265 422 ASP A CB 2971 C CG . ASP A 368 ? 0.2499 0.2434 0.2698 0.0154 0.0208 -0.0282 422 ASP A CG 2972 O OD1 . ASP A 368 ? 0.2448 0.2403 0.2641 0.0152 0.0193 -0.0307 422 ASP A OD1 2973 O OD2 . ASP A 368 ? 0.2544 0.2462 0.2787 0.0152 0.0219 -0.0270 422 ASP A OD2 2974 N N . ALA A 369 ? 0.2185 0.2192 0.2323 0.0135 0.0175 -0.0321 423 ALA A N 2975 C CA . ALA A 369 ? 0.2269 0.2312 0.2410 0.0118 0.0164 -0.0340 423 ALA A CA 2976 C C . ALA A 369 ? 0.2139 0.2204 0.2253 0.0115 0.0160 -0.0343 423 ALA A C 2977 O O . ALA A 369 ? 0.2270 0.2357 0.2378 0.0101 0.0157 -0.0347 423 ALA A O 2978 C CB . ALA A 369 ? 0.2168 0.2213 0.2328 0.0103 0.0164 -0.0335 423 ALA A CB 2979 N N . GLU A 370 ? 0.2240 0.2297 0.2339 0.0129 0.0158 -0.0342 424 GLU A N 2980 C CA . GLU A 370 ? 0.2294 0.2372 0.2382 0.0126 0.0151 -0.0347 424 GLU A CA 2981 C C . GLU A 370 ? 0.2351 0.2464 0.2453 0.0117 0.0150 -0.0367 424 GLU A C 2982 O O . GLU A 370 ? 0.2250 0.2388 0.2350 0.0106 0.0151 -0.0368 424 GLU A O 2983 C CB . GLU A 370 ? 0.2463 0.2523 0.2538 0.0146 0.0144 -0.0346 424 GLU A CB 2984 C CG . GLU A 370 ? 0.2161 0.2241 0.2236 0.0144 0.0133 -0.0352 424 GLU A CG 2985 C CD . GLU A 370 ? 0.2707 0.2817 0.2809 0.0142 0.0129 -0.0372 424 GLU A CD 2986 O OE1 . GLU A 370 ? 0.2387 0.2504 0.2502 0.0142 0.0133 -0.0385 424 GLU A OE1 2987 O OE2 . GLU A 370 ? 0.2611 0.2738 0.2725 0.0139 0.0121 -0.0376 424 GLU A OE2 2988 N N . GLU A 371 ? 0.2321 0.2434 0.2437 0.0122 0.0150 -0.0381 425 GLU A N 2989 C CA . GLU A 371 ? 0.2235 0.2377 0.2359 0.0118 0.0151 -0.0401 425 GLU A CA 2990 C C . GLU A 371 ? 0.2331 0.2488 0.2447 0.0106 0.0154 -0.0404 425 GLU A C 2991 O O . GLU A 371 ? 0.2428 0.2608 0.2541 0.0105 0.0159 -0.0415 425 GLU A O 2992 C CB . GLU A 371 ? 0.2168 0.2304 0.2307 0.0130 0.0148 -0.0417 425 GLU A CB 2993 C CG . GLU A 371 ? 0.2069 0.2191 0.2213 0.0146 0.0143 -0.0419 425 GLU A CG 2994 C CD . GLU A 371 ? 0.2068 0.2216 0.2221 0.0148 0.0140 -0.0426 425 GLU A CD 2995 O OE1 . GLU A 371 ? 0.2436 0.2611 0.2592 0.0136 0.0146 -0.0425 425 GLU A OE1 2996 O OE2 . GLU A 371 ? 0.2385 0.2524 0.2546 0.0162 0.0132 -0.0433 425 GLU A OE2 2997 N N . PHE A 372 ? 0.2281 0.2422 0.2393 0.0099 0.0152 -0.0393 426 PHE A N 2998 C CA . PHE A 372 ? 0.2315 0.2465 0.2417 0.0090 0.0151 -0.0397 426 PHE A CA 2999 C C . PHE A 372 ? 0.2409 0.2567 0.2495 0.0079 0.0154 -0.0382 426 PHE A C 3000 O O . PHE A 372 ? 0.2380 0.2537 0.2458 0.0073 0.0150 -0.0380 426 PHE A O 3001 C CB . PHE A 372 ? 0.2347 0.2475 0.2467 0.0090 0.0143 -0.0399 426 PHE A CB 3002 C CG . PHE A 372 ? 0.2331 0.2453 0.2469 0.0100 0.0136 -0.0419 426 PHE A CG 3003 C CD1 . PHE A 372 ? 0.2308 0.2436 0.2442 0.0103 0.0126 -0.0440 426 PHE A CD1 3004 C CD2 . PHE A 372 ? 0.2399 0.2506 0.2555 0.0109 0.0139 -0.0416 426 PHE A CD2 3005 C CE1 . PHE A 372 ? 0.2442 0.2562 0.2593 0.0114 0.0117 -0.0461 426 PHE A CE1 3006 C CE2 . PHE A 372 ? 0.2418 0.2518 0.2592 0.0118 0.0132 -0.0434 426 PHE A CE2 3007 C CZ . PHE A 372 ? 0.2419 0.2526 0.2592 0.0120 0.0120 -0.0458 426 PHE A CZ 3008 N N . GLY A 373 ? 0.2448 0.2613 0.2531 0.0079 0.0158 -0.0371 427 GLY A N 3009 C CA . GLY A 373 ? 0.2318 0.2490 0.2387 0.0069 0.0160 -0.0357 427 GLY A CA 3010 C C . GLY A 373 ? 0.2323 0.2475 0.2389 0.0070 0.0157 -0.0339 427 GLY A C 3011 O O . GLY A 373 ? 0.2349 0.2500 0.2404 0.0061 0.0156 -0.0327 427 GLY A O 3012 N N . LEU A 374 ? 0.2035 0.2171 0.2108 0.0083 0.0154 -0.0338 428 LEU A N 3013 C CA . LEU A 374 ? 0.2096 0.2207 0.2156 0.0091 0.0151 -0.0321 428 LEU A CA 3014 C C . LEU A 374 ? 0.2111 0.2203 0.2168 0.0088 0.0156 -0.0307 428 LEU A C 3015 O O . LEU A 374 ? 0.2134 0.2215 0.2177 0.0089 0.0157 -0.0292 428 LEU A O 3016 C CB . LEU A 374 ? 0.2158 0.2280 0.2210 0.0086 0.0145 -0.0316 428 LEU A CB 3017 C CG . LEU A 374 ? 0.2120 0.2270 0.2191 0.0083 0.0143 -0.0329 428 LEU A CG 3018 C CD1 . LEU A 374 ? 0.2532 0.2691 0.2607 0.0077 0.0136 -0.0322 428 LEU A CD1 3019 C CD2 . LEU A 374 ? 0.2154 0.2296 0.2238 0.0100 0.0136 -0.0341 428 LEU A CD2 3020 N N . LEU A 375 ? 0.2095 0.2183 0.2169 0.0086 0.0160 -0.0313 429 LEU A N 3021 C CA . LEU A 375 ? 0.2104 0.2181 0.2189 0.0079 0.0163 -0.0302 429 LEU A CA 3022 C C . LEU A 375 ? 0.2244 0.2290 0.2329 0.0092 0.0173 -0.0281 429 LEU A C 3023 O O . LEU A 375 ? 0.2247 0.2287 0.2332 0.0088 0.0178 -0.0266 429 LEU A O 3024 C CB . LEU A 375 ? 0.1968 0.2048 0.2082 0.0074 0.0159 -0.0316 429 LEU A CB 3025 C CG . LEU A 375 ? 0.2119 0.2225 0.2223 0.0068 0.0151 -0.0338 429 LEU A CG 3026 C CD1 . LEU A 375 ? 0.2242 0.2343 0.2371 0.0067 0.0142 -0.0355 429 LEU A CD1 3027 C CD2 . LEU A 375 ? 0.2096 0.2220 0.2176 0.0057 0.0149 -0.0336 429 LEU A CD2 3028 N N . GLY A 376 ? 0.2014 0.2039 0.2099 0.0108 0.0179 -0.0278 430 GLY A N 3029 C CA . GLY A 376 ? 0.2153 0.2143 0.2234 0.0125 0.0194 -0.0254 430 GLY A CA 3030 C C . GLY A 376 ? 0.2179 0.2158 0.2220 0.0136 0.0194 -0.0240 430 GLY A C 3031 O O . GLY A 376 ? 0.2162 0.2122 0.2198 0.0142 0.0206 -0.0220 430 GLY A O 3032 N N . SER A 377 ? 0.2069 0.2057 0.2085 0.0141 0.0179 -0.0252 431 SER A N 3033 C CA . SER A 377 ? 0.2186 0.2158 0.2165 0.0154 0.0174 -0.0241 431 SER A CA 3034 C C . SER A 377 ? 0.2062 0.2052 0.2045 0.0135 0.0173 -0.0235 431 SER A C 3035 O O . SER A 377 ? 0.1960 0.1931 0.1921 0.0145 0.0177 -0.0218 431 SER A O 3036 C CB . SER A 377 ? 0.2106 0.2087 0.2072 0.0162 0.0153 -0.0258 431 SER A CB 3037 O OG . SER A 377 ? 0.2273 0.2295 0.2265 0.0137 0.0145 -0.0275 431 SER A OG 3038 N N . THR A 378 ? 0.1951 0.1974 0.1956 0.0111 0.0167 -0.0248 432 THR A N 3039 C CA . THR A 378 ? 0.2071 0.2109 0.2073 0.0095 0.0164 -0.0243 432 THR A CA 3040 C C . THR A 378 ? 0.2014 0.2039 0.2030 0.0093 0.0177 -0.0227 432 THR A C 3041 O O . THR A 378 ? 0.2137 0.2157 0.2139 0.0092 0.0177 -0.0215 432 THR A O 3042 C CB . THR A 378 ? 0.2035 0.2108 0.2051 0.0074 0.0157 -0.0260 432 THR A CB 3043 O OG1 . THR A 378 ? 0.2188 0.2274 0.2202 0.0077 0.0150 -0.0272 432 THR A OG1 3044 C CG2 . THR A 378 ? 0.2212 0.2297 0.2219 0.0060 0.0153 -0.0253 432 THR A CG2 3045 N N . GLU A 379 ? 0.2057 0.2078 0.2104 0.0092 0.0185 -0.0229 433 GLU A N 3046 C CA . GLU A 379 ? 0.2187 0.2196 0.2262 0.0089 0.0197 -0.0213 433 GLU A CA 3047 C C . GLU A 379 ? 0.2096 0.2073 0.2151 0.0110 0.0214 -0.0188 433 GLU A C 3048 O O . GLU A 379 ? 0.2126 0.2098 0.2188 0.0109 0.0223 -0.0172 433 GLU A O 3049 C CB . GLU A 379 ? 0.2075 0.2081 0.2198 0.0085 0.0202 -0.0220 433 GLU A CB 3050 C CG . GLU A 379 ? 0.2349 0.2383 0.2489 0.0067 0.0183 -0.0246 433 GLU A CG 3051 C CD . GLU A 379 ? 0.2388 0.2440 0.2521 0.0052 0.0171 -0.0250 433 GLU A CD 3052 O OE1 . GLU A 379 ? 0.2339 0.2383 0.2494 0.0049 0.0175 -0.0238 433 GLU A OE1 3053 O OE2 . GLU A 379 ? 0.2353 0.2424 0.2458 0.0045 0.0160 -0.0263 433 GLU A OE2 3054 N N . TRP A 380 ? 0.2001 0.1956 0.2032 0.0132 0.0221 -0.0184 434 TRP A N 3055 C CA . TRP A 380 ? 0.2114 0.2031 0.2114 0.0161 0.0238 -0.0159 434 TRP A CA 3056 C C . TRP A 380 ? 0.2158 0.2074 0.2115 0.0166 0.0227 -0.0156 434 TRP A C 3057 O O . TRP A 380 ? 0.2199 0.2096 0.2142 0.0179 0.0241 -0.0135 434 TRP A O 3058 C CB . TRP A 380 ? 0.2215 0.2104 0.2188 0.0187 0.0242 -0.0159 434 TRP A CB 3059 C CG . TRP A 380 ? 0.2296 0.2140 0.2228 0.0223 0.0263 -0.0132 434 TRP A CG 3060 C CD1 . TRP A 380 ? 0.2407 0.2222 0.2357 0.0237 0.0296 -0.0105 434 TRP A CD1 3061 C CD2 . TRP A 380 ? 0.2425 0.2244 0.2293 0.0250 0.0253 -0.0129 434 TRP A CD2 3062 N NE1 . TRP A 380 ? 0.2496 0.2268 0.2386 0.0276 0.0311 -0.0084 434 TRP A NE1 3063 C CE2 . TRP A 380 ? 0.2598 0.2370 0.2435 0.0286 0.0282 -0.0100 434 TRP A CE2 3064 C CE3 . TRP A 380 ? 0.2377 0.2206 0.2213 0.0251 0.0222 -0.0148 434 TRP A CE3 3065 C CZ2 . TRP A 380 ? 0.2704 0.2436 0.2467 0.0325 0.0278 -0.0092 434 TRP A CZ2 3066 C CZ3 . TRP A 380 ? 0.2599 0.2389 0.2371 0.0288 0.0214 -0.0142 434 TRP A CZ3 3067 C CH2 . TRP A 380 ? 0.2700 0.2442 0.2432 0.0326 0.0241 -0.0115 434 TRP A CH2 3068 N N . ALA A 381 ? 0.2089 0.2026 0.2030 0.0156 0.0202 -0.0175 435 ALA A N 3069 C CA . ALA A 381 ? 0.2255 0.2191 0.2163 0.0160 0.0188 -0.0174 435 ALA A CA 3070 C C . ALA A 381 ? 0.2302 0.2256 0.2230 0.0139 0.0192 -0.0166 435 ALA A C 3071 O O . ALA A 381 ? 0.2154 0.2094 0.2056 0.0149 0.0192 -0.0154 435 ALA A O 3072 C CB . ALA A 381 ? 0.2382 0.2340 0.2285 0.0151 0.0163 -0.0195 435 ALA A CB 3073 N N . GLU A 382 ? 0.2226 0.2207 0.2194 0.0113 0.0191 -0.0176 436 GLU A N 3074 C CA . GLU A 382 ? 0.2242 0.2235 0.2228 0.0096 0.0192 -0.0170 436 GLU A CA 3075 C C . GLU A 382 ? 0.2338 0.2308 0.2339 0.0109 0.0214 -0.0147 436 GLU A C 3076 O O . GLU A 382 ? 0.2389 0.2357 0.2385 0.0109 0.0217 -0.0135 436 GLU A O 3077 C CB . GLU A 382 ? 0.2366 0.2386 0.2388 0.0072 0.0184 -0.0187 436 GLU A CB 3078 C CG . GLU A 382 ? 0.2214 0.2259 0.2219 0.0060 0.0167 -0.0206 436 GLU A CG 3079 C CD . GLU A 382 ? 0.2398 0.2465 0.2424 0.0042 0.0160 -0.0223 436 GLU A CD 3080 O OE1 . GLU A 382 ? 0.2439 0.2524 0.2450 0.0031 0.0150 -0.0230 436 GLU A OE1 3081 O OE2 . GLU A 382 ? 0.2377 0.2441 0.2436 0.0042 0.0163 -0.0227 436 GLU A OE2 3082 N N . GLU A 383 ? 0.2253 0.2206 0.2275 0.0121 0.0233 -0.0138 437 GLU A N 3083 C CA . GLU A 383 ? 0.2302 0.2231 0.2344 0.0136 0.0261 -0.0112 437 GLU A CA 3084 C C . GLU A 383 ? 0.2285 0.2184 0.2271 0.0165 0.0271 -0.0093 437 GLU A C 3085 O O . GLU A 383 ? 0.2163 0.2054 0.2155 0.0171 0.0287 -0.0074 437 GLU A O 3086 C CB . GLU A 383 ? 0.2297 0.2209 0.2367 0.0146 0.0280 -0.0106 437 GLU A CB 3087 C CG . GLU A 383 ? 0.2887 0.2776 0.2997 0.0160 0.0316 -0.0075 437 GLU A CG 3088 C CD . GLU A 383 ? 0.4039 0.3925 0.4208 0.0155 0.0327 -0.0075 437 GLU A CD 3089 O OE1 . GLU A 383 ? 0.5345 0.5248 0.5585 0.0134 0.0324 -0.0081 437 GLU A OE1 3090 O OE2 . GLU A 383 ? 0.4313 0.4180 0.4457 0.0172 0.0333 -0.0074 437 GLU A OE2 3091 N N . ASN A 384 ? 0.2186 0.2070 0.2118 0.0184 0.0260 -0.0100 438 ASN A N 3092 C CA . ASN A 384 ? 0.2257 0.2103 0.2127 0.0221 0.0267 -0.0083 438 ASN A CA 3093 C C . ASN A 384 ? 0.2246 0.2097 0.2074 0.0221 0.0238 -0.0096 438 ASN A C 3094 O O . ASN A 384 ? 0.2202 0.2022 0.1974 0.0253 0.0232 -0.0091 438 ASN A O 3095 C CB . ASN A 384 ? 0.2328 0.2142 0.2167 0.0250 0.0275 -0.0080 438 ASN A CB 3096 C CG . ASN A 384 ? 0.2642 0.2441 0.2521 0.0256 0.0311 -0.0060 438 ASN A CG 3097 O OD1 . ASN A 384 ? 0.2809 0.2586 0.2692 0.0272 0.0342 -0.0032 438 ASN A OD1 3098 N ND2 . ASN A 384 ? 0.2624 0.2439 0.2543 0.0240 0.0308 -0.0073 438 ASN A ND2 3099 N N . SER A 385 ? 0.2124 0.2013 0.1980 0.0187 0.0219 -0.0111 439 SER A N 3100 C CA . SER A 385 ? 0.2235 0.2133 0.2062 0.0183 0.0189 -0.0125 439 SER A CA 3101 C C . SER A 385 ? 0.2272 0.2142 0.2054 0.0208 0.0188 -0.0112 439 SER A C 3102 O O . SER A 385 ? 0.2291 0.2149 0.2037 0.0223 0.0163 -0.0122 439 SER A O 3103 C CB . SER A 385 ? 0.2325 0.2264 0.2188 0.0145 0.0176 -0.0137 439 SER A CB 3104 O OG . SER A 385 ? 0.2540 0.2483 0.2424 0.0136 0.0189 -0.0124 439 SER A OG 3105 N N . ARG A 386 ? 0.2148 0.2008 0.1936 0.0215 0.0212 -0.0090 440 ARG A N 3106 C CA . ARG A 386 ? 0.2345 0.2175 0.2084 0.0243 0.0211 -0.0078 440 ARG A CA 3107 C C . ARG A 386 ? 0.2507 0.2289 0.2183 0.0290 0.0215 -0.0071 440 ARG A C 3108 O O . ARG A 386 ? 0.2307 0.2066 0.1931 0.0315 0.0194 -0.0075 440 ARG A O 3109 C CB . ARG A 386 ? 0.2411 0.2240 0.2175 0.0242 0.0241 -0.0055 440 ARG A CB 3110 C CG . ARG A 386 ? 0.2687 0.2559 0.2502 0.0200 0.0228 -0.0064 440 ARG A CG 3111 C CD . ARG A 386 ? 0.2944 0.2824 0.2818 0.0190 0.0257 -0.0048 440 ARG A CD 3112 N NE . ARG A 386 ? 0.2698 0.2614 0.2611 0.0153 0.0238 -0.0062 440 ARG A NE 3113 C CZ . ARG A 386 ? 0.2952 0.2896 0.2896 0.0125 0.0222 -0.0082 440 ARG A CZ 3114 N NH1 . ARG A 386 ? 0.3060 0.3007 0.3014 0.0123 0.0223 -0.0091 440 ARG A NH1 3115 N NH2 . ARG A 386 ? 0.2385 0.2354 0.2349 0.0100 0.0204 -0.0092 440 ARG A NH2 3116 N N . LEU A 387 ? 0.2469 0.2234 0.2149 0.0306 0.0242 -0.0059 441 LEU A N 3117 C CA . LEU A 387 ? 0.2533 0.2248 0.2147 0.0354 0.0245 -0.0053 441 LEU A CA 3118 C C . LEU A 387 ? 0.2683 0.2399 0.2272 0.0357 0.0201 -0.0083 441 LEU A C 3119 O O . LEU A 387 ? 0.2623 0.2302 0.2150 0.0394 0.0181 -0.0088 441 LEU A O 3120 C CB . LEU A 387 ? 0.2547 0.2247 0.2179 0.0364 0.0279 -0.0037 441 LEU A CB 3121 C CG . LEU A 387 ? 0.2688 0.2393 0.2370 0.0356 0.0324 -0.0008 441 LEU A CG 3122 C CD1 . LEU A 387 ? 0.2994 0.2676 0.2689 0.0373 0.0357 0.0008 441 LEU A CD1 3123 C CD2 . LEU A 387 ? 0.3248 0.2930 0.2900 0.0380 0.0344 0.0014 441 LEU A CD2 3124 N N . LEU A 388 ? 0.2509 0.2265 0.2149 0.0320 0.0186 -0.0103 442 LEU A N 3125 C CA . LEU A 388 ? 0.2398 0.2159 0.2031 0.0320 0.0149 -0.0130 442 LEU A CA 3126 C C . LEU A 388 ? 0.2612 0.2378 0.2232 0.0317 0.0114 -0.0144 442 LEU A C 3127 O O . LEU A 388 ? 0.2982 0.2726 0.2571 0.0342 0.0082 -0.0160 442 LEU A O 3128 C CB . LEU A 388 ? 0.2353 0.2159 0.2049 0.0280 0.0148 -0.0145 442 LEU A CB 3129 C CG . LEU A 388 ? 0.2616 0.2415 0.2328 0.0284 0.0175 -0.0137 442 LEU A CG 3130 C CD1 . LEU A 388 ? 0.2349 0.2196 0.2125 0.0242 0.0173 -0.0152 442 LEU A CD1 3131 C CD2 . LEU A 388 ? 0.2877 0.2635 0.2543 0.0324 0.0167 -0.0141 442 LEU A CD2 3132 N N A GLN A 389 ? 0.2413 0.2207 0.2060 0.0289 0.0116 -0.0140 443 GLN A N 3133 N N B GLN A 389 ? 0.2471 0.2267 0.2121 0.0287 0.0117 -0.0139 443 GLN A N 3134 C CA A GLN A 389 ? 0.2503 0.2300 0.2141 0.0286 0.0080 -0.0154 443 GLN A CA 3135 C CA B GLN A 389 ? 0.2615 0.2417 0.2258 0.0281 0.0088 -0.0148 443 GLN A CA 3136 C C A GLN A 389 ? 0.2506 0.2256 0.2080 0.0329 0.0070 -0.0147 443 GLN A C 3137 C C B GLN A 389 ? 0.2563 0.2314 0.2138 0.0329 0.0072 -0.0146 443 GLN A C 3138 O O A GLN A 389 ? 0.2441 0.2184 0.2003 0.0336 0.0033 -0.0162 443 GLN A O 3139 O O B GLN A 389 ? 0.2392 0.2131 0.1952 0.0341 0.0033 -0.0165 443 GLN A O 3140 C CB A GLN A 389 ? 0.2228 0.2069 0.1913 0.0242 0.0080 -0.0155 443 GLN A CB 3141 C CB B GLN A 389 ? 0.2561 0.2388 0.2231 0.0252 0.0103 -0.0136 443 GLN A CB 3142 C CG A GLN A 389 ? 0.2279 0.2120 0.1962 0.0238 0.0104 -0.0134 443 GLN A CG 3143 C CG B GLN A 389 ? 0.2542 0.2362 0.2191 0.0256 0.0083 -0.0136 443 GLN A CG 3144 C CD A GLN A 389 ? 0.2772 0.2657 0.2505 0.0193 0.0107 -0.0136 443 GLN A CD 3145 C CD B GLN A 389 ? 0.3223 0.3072 0.2904 0.0228 0.0052 -0.0155 443 GLN A CD 3146 O OE1 A GLN A 389 ? 0.2531 0.2446 0.2296 0.0168 0.0096 -0.0151 443 GLN A OE1 3147 O OE1 B GLN A 389 ? 0.3359 0.3244 0.3085 0.0196 0.0056 -0.0162 443 GLN A OE1 3148 N NE2 A GLN A 389 ? 0.2345 0.2233 0.2084 0.0186 0.0122 -0.0122 443 GLN A NE2 3149 N NE2 B GLN A 389 ? 0.2215 0.2048 0.1876 0.0241 0.0022 -0.0162 443 GLN A NE2 3150 N N . GLU A 390 ? 0.2560 0.2278 0.2095 0.0358 0.0101 -0.0123 444 GLU A N 3151 C CA . GLU A 390 ? 0.2598 0.2267 0.2062 0.0405 0.0091 -0.0117 444 GLU A CA 3152 C C . GLU A 390 ? 0.2698 0.2315 0.2098 0.0457 0.0086 -0.0120 444 GLU A C 3153 O O . GLU A 390 ? 0.2773 0.2346 0.2109 0.0501 0.0064 -0.0125 444 GLU A O 3154 C CB . GLU A 390 ? 0.2910 0.2570 0.2360 0.0414 0.0129 -0.0088 444 GLU A CB 3155 C CG . GLU A 390 ? 0.2813 0.2525 0.2330 0.0361 0.0135 -0.0086 444 GLU A CG 3156 C CD . GLU A 390 ? 0.3486 0.3217 0.3014 0.0340 0.0093 -0.0107 444 GLU A CD 3157 O OE1 . GLU A 390 ? 0.2890 0.2600 0.2388 0.0361 0.0056 -0.0125 444 GLU A OE1 3158 O OE2 . GLU A 390 ? 0.3522 0.3288 0.3092 0.0304 0.0096 -0.0104 444 GLU A OE2 3159 N N . ARG A 391 ? 0.2575 0.2196 0.1993 0.0454 0.0102 -0.0119 445 ARG A N 3160 C CA . ARG A 391 ? 0.2632 0.2199 0.1985 0.0506 0.0103 -0.0118 445 ARG A CA 3161 C C . ARG A 391 ? 0.2810 0.2384 0.2181 0.0502 0.0072 -0.0145 445 ARG A C 3162 O O . ARG A 391 ? 0.2958 0.2483 0.2270 0.0549 0.0062 -0.0149 445 ARG A O 3163 C CB . ARG A 391 ? 0.2553 0.2102 0.1897 0.0520 0.0160 -0.0084 445 ARG A CB 3164 C CG . ARG A 391 ? 0.2679 0.2215 0.2004 0.0533 0.0196 -0.0054 445 ARG A CG 3165 C CD . ARG A 391 ? 0.2750 0.2272 0.2086 0.0543 0.0256 -0.0019 445 ARG A CD 3166 N NE . ARG A 391 ? 0.2856 0.2384 0.2208 0.0539 0.0290 0.0007 445 ARG A NE 3167 C CZ . ARG A 391 ? 0.2429 0.1960 0.1821 0.0535 0.0343 0.0038 445 ARG A CZ 3168 N NH1 . ARG A 391 ? 0.2625 0.2150 0.2039 0.0536 0.0366 0.0047 445 ARG A NH1 3169 N NH2 . ARG A 391 ? 0.2916 0.2456 0.2332 0.0530 0.0370 0.0060 445 ARG A NH2 3170 N N . GLY A 392 ? 0.2617 0.2247 0.2064 0.0450 0.0059 -0.0162 446 GLY A N 3171 C CA . GLY A 392 ? 0.2797 0.2442 0.2277 0.0440 0.0041 -0.0183 446 GLY A CA 3172 C C . GLY A 392 ? 0.2718 0.2346 0.2182 0.0462 -0.0013 -0.0212 446 GLY A C 3173 O O . GLY A 392 ? 0.2969 0.2622 0.2467 0.0439 -0.0041 -0.0227 446 GLY A O 3174 N N . VAL A 393 ? 0.2737 0.2318 0.2150 0.0508 -0.0030 -0.0222 447 VAL A N 3175 C CA . VAL A 393 ? 0.2708 0.2268 0.2111 0.0531 -0.0087 -0.0253 447 VAL A CA 3176 C C . VAL A 393 ? 0.2716 0.2322 0.2201 0.0496 -0.0109 -0.0278 447 VAL A C 3177 O O . VAL A 393 ? 0.2673 0.2303 0.2209 0.0477 -0.0147 -0.0301 447 VAL A O 3178 C CB . VAL A 393 ? 0.2898 0.2382 0.2205 0.0603 -0.0101 -0.0256 447 VAL A CB 3179 C CG1 . VAL A 393 ? 0.2767 0.2233 0.2080 0.0626 -0.0167 -0.0296 447 VAL A CG1 3180 C CG2 . VAL A 393 ? 0.3130 0.2564 0.2351 0.0646 -0.0087 -0.0235 447 VAL A CG2 3181 N N . ALA A 394 ? 0.2545 0.2164 0.2048 0.0485 -0.0083 -0.0274 448 ALA A N 3182 C CA . ALA A 394 ? 0.2550 0.2206 0.2121 0.0460 -0.0102 -0.0297 448 ALA A CA 3183 C C . ALA A 394 ? 0.2396 0.2074 0.1990 0.0440 -0.0063 -0.0286 448 ALA A C 3184 O O . ALA A 394 ? 0.2591 0.2239 0.2136 0.0461 -0.0029 -0.0263 448 ALA A O 3185 C CB . ALA A 394 ? 0.2621 0.2235 0.2166 0.0505 -0.0152 -0.0325 448 ALA A CB 3186 N N . TYR A 395 ? 0.2355 0.2083 0.2024 0.0403 -0.0068 -0.0302 449 TYR A N 3187 C CA . TYR A 395 ? 0.2364 0.2117 0.2062 0.0383 -0.0038 -0.0297 449 TYR A CA 3188 C C . TYR A 395 ? 0.2476 0.2240 0.2213 0.0386 -0.0066 -0.0325 449 TYR A C 3189 O O . TYR A 395 ? 0.2470 0.2265 0.2262 0.0366 -0.0092 -0.0343 449 TYR A O 3190 C CB . TYR A 395 ? 0.2150 0.1959 0.1904 0.0330 -0.0008 -0.0286 449 TYR A CB 3191 C CG . TYR A 395 ? 0.2312 0.2146 0.2098 0.0311 0.0016 -0.0286 449 TYR A CG 3192 C CD1 . TYR A 395 ? 0.2325 0.2144 0.2089 0.0314 0.0051 -0.0265 449 TYR A CD1 3193 C CD2 . TYR A 395 ? 0.2199 0.2069 0.2041 0.0291 0.0004 -0.0307 449 TYR A CD2 3194 C CE1 . TYR A 395 ? 0.2447 0.2286 0.2244 0.0298 0.0071 -0.0266 449 TYR A CE1 3195 C CE2 . TYR A 395 ? 0.2242 0.2133 0.2110 0.0277 0.0026 -0.0308 449 TYR A CE2 3196 C CZ . TYR A 395 ? 0.2482 0.2356 0.2326 0.0279 0.0057 -0.0288 449 TYR A CZ 3197 O OH . TYR A 395 ? 0.2457 0.2348 0.2329 0.0266 0.0075 -0.0291 449 TYR A OH 3198 N N . ILE A 396 ? 0.2534 0.2270 0.2243 0.0411 -0.0061 -0.0326 450 ILE A N 3199 C CA . ILE A 396 ? 0.2370 0.2119 0.2118 0.0413 -0.0084 -0.0352 450 ILE A CA 3200 C C . ILE A 396 ? 0.2558 0.2338 0.2338 0.0385 -0.0048 -0.0344 450 ILE A C 3201 O O . ILE A 396 ? 0.2438 0.2194 0.2180 0.0396 -0.0017 -0.0324 450 ILE A O 3202 C CB . ILE A 396 ? 0.2736 0.2420 0.2419 0.0471 -0.0112 -0.0363 450 ILE A CB 3203 C CG1 . ILE A 396 ? 0.2514 0.2156 0.2150 0.0507 -0.0150 -0.0370 450 ILE A CG1 3204 C CG2 . ILE A 396 ? 0.2415 0.2113 0.2145 0.0474 -0.0140 -0.0392 450 ILE A CG2 3205 C CD1 . ILE A 396 ? 0.2481 0.2158 0.2190 0.0486 -0.0193 -0.0397 450 ILE A CD1 3206 N N . ASN A 397 ? 0.2331 0.2164 0.2185 0.0351 -0.0050 -0.0359 451 ASN A N 3207 C CA . ASN A 397 ? 0.2395 0.2260 0.2282 0.0326 -0.0021 -0.0357 451 ASN A CA 3208 C C . ASN A 397 ? 0.2623 0.2464 0.2501 0.0353 -0.0031 -0.0371 451 ASN A C 3209 O O . ASN A 397 ? 0.2823 0.2632 0.2681 0.0387 -0.0066 -0.0387 451 ASN A O 3210 C CB . ASN A 397 ? 0.2349 0.2276 0.2311 0.0284 -0.0017 -0.0367 451 ASN A CB 3211 C CG . ASN A 397 ? 0.2448 0.2407 0.2431 0.0254 0.0018 -0.0358 451 ASN A CG 3212 O OD1 . ASN A 397 ? 0.2712 0.2665 0.2671 0.0245 0.0041 -0.0338 451 ASN A OD1 3213 N ND2 . ASN A 397 ? 0.2527 0.2522 0.2559 0.0238 0.0020 -0.0373 451 ASN A ND2 3214 N N . ALA A 398 ? 0.2730 0.2585 0.2622 0.0339 -0.0004 -0.0366 452 ALA A N 3215 C CA . ALA A 398 ? 0.2839 0.2672 0.2721 0.0363 -0.0010 -0.0376 452 ALA A CA 3216 C C . ALA A 398 ? 0.2707 0.2577 0.2634 0.0335 0.0012 -0.0380 452 ALA A C 3217 O O . ALA A 398 ? 0.2910 0.2758 0.2816 0.0344 0.0032 -0.0369 452 ALA A O 3218 C CB . ALA A 398 ? 0.3006 0.2773 0.2810 0.0403 0.0000 -0.0356 452 ALA A CB 3219 N N . ASP A 399 ? 0.2514 0.2437 0.2501 0.0305 0.0010 -0.0394 453 ASP A N 3220 C CA . ASP A 399 ? 0.2499 0.2456 0.2526 0.0284 0.0027 -0.0402 453 ASP A CA 3221 C C . ASP A 399 ? 0.2688 0.2640 0.2734 0.0305 0.0002 -0.0427 453 ASP A C 3222 O O . ASP A 399 ? 0.2787 0.2699 0.2801 0.0338 -0.0022 -0.0432 453 ASP A O 3223 C CB . ASP A 399 ? 0.2352 0.2363 0.2427 0.0248 0.0037 -0.0405 453 ASP A CB 3224 C CG . ASP A 399 ? 0.2623 0.2664 0.2722 0.0227 0.0061 -0.0408 453 ASP A CG 3225 O OD1 . ASP A 399 ? 0.2823 0.2851 0.2918 0.0238 0.0064 -0.0414 453 ASP A OD1 3226 O OD2 . ASP A 399 ? 0.2324 0.2401 0.2445 0.0200 0.0076 -0.0404 453 ASP A OD2 3227 N N . SER A 400 ? 0.2680 0.2669 0.2774 0.0289 0.0008 -0.0441 454 SER A N 3228 C CA . SER A 400 ? 0.2891 0.2882 0.3012 0.0306 -0.0010 -0.0465 454 SER A CA 3229 C C . SER A 400 ? 0.2968 0.2934 0.3087 0.0334 -0.0050 -0.0480 454 SER A C 3230 O O . SER A 400 ? 0.2927 0.2912 0.3077 0.0325 -0.0065 -0.0484 454 SER A O 3231 C CB . SER A 400 ? 0.2761 0.2811 0.2950 0.0279 0.0000 -0.0479 454 SER A CB 3232 O OG . SER A 400 ? 0.2675 0.2742 0.2860 0.0259 0.0029 -0.0470 454 SER A OG 3233 N N A SER A 401 ? 0.2963 0.2883 0.3045 0.0370 -0.0068 -0.0487 455 SER A N 3234 N N B SER A 401 ? 0.3035 0.2956 0.3117 0.0370 -0.0069 -0.0487 455 SER A N 3235 C CA A SER A 401 ? 0.3089 0.2976 0.3159 0.0404 -0.0112 -0.0504 455 SER A CA 3236 C CA B SER A 401 ? 0.3234 0.3123 0.3306 0.0403 -0.0112 -0.0504 455 SER A CA 3237 C C A SER A 401 ? 0.3206 0.3131 0.3357 0.0400 -0.0137 -0.0534 455 SER A C 3238 C C B SER A 401 ? 0.3282 0.3206 0.3433 0.0400 -0.0137 -0.0534 455 SER A C 3239 O O A SER A 401 ? 0.3236 0.3155 0.3412 0.0414 -0.0174 -0.0551 455 SER A O 3240 O O B SER A 401 ? 0.3309 0.3227 0.3484 0.0415 -0.0175 -0.0551 455 SER A O 3241 C CB A SER A 401 ? 0.3056 0.2876 0.3051 0.0450 -0.0124 -0.0502 455 SER A CB 3242 C CB B SER A 401 ? 0.3230 0.3049 0.3222 0.0449 -0.0124 -0.0500 455 SER A CB 3243 O OG A SER A 401 ? 0.2788 0.2570 0.2712 0.0458 -0.0099 -0.0472 455 SER A OG 3244 O OG B SER A 401 ? 0.3514 0.3329 0.3511 0.0457 -0.0119 -0.0508 455 SER A OG 3245 N N . ILE A 402 ? 0.3358 0.3321 0.3553 0.0380 -0.0116 -0.0540 456 ILE A N 3246 C CA . ILE A 402 ? 0.3599 0.3601 0.3877 0.0376 -0.0133 -0.0566 456 ILE A CA 3247 C C . ILE A 402 ? 0.3682 0.3747 0.4018 0.0336 -0.0096 -0.0562 456 ILE A C 3248 O O . ILE A 402 ? 0.4208 0.4279 0.4516 0.0323 -0.0065 -0.0549 456 ILE A O 3249 C CB . ILE A 402 ? 0.3593 0.3567 0.3861 0.0407 -0.0153 -0.0586 456 ILE A CB 3250 C CG1 . ILE A 402 ? 0.3839 0.3792 0.4051 0.0409 -0.0123 -0.0571 456 ILE A CG1 3251 C CG2 . ILE A 402 ? 0.3941 0.3855 0.4162 0.0451 -0.0198 -0.0597 456 ILE A CG2 3252 C CD1 . ILE A 402 ? 0.4688 0.4670 0.4942 0.0402 -0.0113 -0.0586 456 ILE A CD1 3253 N N A GLU A 403 ? 0.3620 0.3730 0.4036 0.0319 -0.0100 -0.0572 457 GLU A N 3254 N N B GLU A 403 ? 0.3608 0.3717 0.4024 0.0320 -0.0102 -0.0572 457 GLU A N 3255 C CA A GLU A 403 ? 0.3522 0.3690 0.3995 0.0290 -0.0066 -0.0570 457 GLU A CA 3256 C CA B GLU A 403 ? 0.3499 0.3667 0.3974 0.0290 -0.0067 -0.0570 457 GLU A CA 3257 C C A GLU A 403 ? 0.3484 0.3680 0.4044 0.0297 -0.0083 -0.0595 457 GLU A C 3258 C C B GLU A 403 ? 0.3478 0.3676 0.4044 0.0296 -0.0085 -0.0595 457 GLU A C 3259 O O A GLU A 403 ? 0.3442 0.3688 0.4062 0.0279 -0.0057 -0.0597 457 GLU A O 3260 O O B GLU A 403 ? 0.3465 0.3714 0.4098 0.0275 -0.0060 -0.0595 457 GLU A O 3261 C CB A GLU A 403 ? 0.3445 0.3645 0.3935 0.0260 -0.0041 -0.0551 457 GLU A CB 3262 C CB B GLU A 403 ? 0.3387 0.3580 0.3869 0.0261 -0.0044 -0.0549 457 GLU A CB 3263 C CG A GLU A 403 ? 0.3467 0.3656 0.3977 0.0263 -0.0069 -0.0551 457 GLU A CG 3264 C CG B GLU A 403 ? 0.3268 0.3437 0.3669 0.0253 -0.0023 -0.0526 457 GLU A CG 3265 C CD A GLU A 403 ? 0.3337 0.3560 0.3877 0.0233 -0.0046 -0.0533 457 GLU A CD 3266 C CD B GLU A 403 ? 0.3602 0.3791 0.4003 0.0228 -0.0004 -0.0506 457 GLU A CD 3267 O OE1 A GLU A 403 ? 0.3800 0.4042 0.4315 0.0212 -0.0008 -0.0516 457 GLU A OE1 3268 O OE1 B GLU A 403 ? 0.2798 0.3002 0.3246 0.0221 -0.0018 -0.0507 457 GLU A OE1 3269 O OE2 A GLU A 403 ? 0.3260 0.3488 0.3849 0.0231 -0.0068 -0.0536 457 GLU A OE2 3270 O OE2 B GLU A 403 ? 0.3490 0.3677 0.3846 0.0215 0.0021 -0.0489 457 GLU A OE2 3271 N N . GLY A 404 ? 0.3616 0.3779 0.4181 0.0327 -0.0128 -0.0615 458 GLY A N 3272 C CA . GLY A 404 ? 0.3594 0.3778 0.4247 0.0338 -0.0154 -0.0643 458 GLY A CA 3273 C C . GLY A 404 ? 0.3810 0.3937 0.4430 0.0378 -0.0209 -0.0662 458 GLY A C 3274 O O . GLY A 404 ? 0.3815 0.3890 0.4341 0.0396 -0.0217 -0.0650 458 GLY A O 3275 N N . ASN A 405 ? 0.3713 0.3845 0.4405 0.0396 -0.0246 -0.0691 459 ASN A N 3276 C CA . ASN A 405 ? 0.3916 0.3987 0.4569 0.0440 -0.0304 -0.0712 459 ASN A CA 3277 C C . ASN A 405 ? 0.3773 0.3851 0.4519 0.0450 -0.0354 -0.0738 459 ASN A C 3278 O O . ASN A 405 ? 0.4071 0.4113 0.4820 0.0487 -0.0406 -0.0766 459 ASN A O 3279 C CB . ASN A 405 ? 0.4060 0.4098 0.4668 0.0470 -0.0314 -0.0726 459 ASN A CB 3280 C CG . ASN A 405 ? 0.4198 0.4286 0.4905 0.0462 -0.0311 -0.0747 459 ASN A CG 3281 O OD1 . ASN A 405 ? 0.3946 0.4086 0.4763 0.0441 -0.0309 -0.0755 459 ASN A OD1 3282 N ND2 . ASN A 405 ? 0.5376 0.5445 0.6045 0.0479 -0.0307 -0.0755 459 ASN A ND2 3283 N N . TYR A 406 ? 0.3588 0.3713 0.4412 0.0418 -0.0339 -0.0728 460 TYR A N 3284 C CA . TYR A 406 ? 0.3444 0.3586 0.4380 0.0420 -0.0380 -0.0750 460 TYR A CA 3285 C C . TYR A 406 ? 0.3422 0.3515 0.4317 0.0441 -0.0426 -0.0754 460 TYR A C 3286 O O . TYR A 406 ? 0.3466 0.3521 0.4379 0.0476 -0.0490 -0.0785 460 TYR A O 3287 C CB . TYR A 406 ? 0.3426 0.3642 0.4472 0.0376 -0.0336 -0.0735 460 TYR A CB 3288 C CG . TYR A 406 ? 0.3893 0.4134 0.5079 0.0374 -0.0373 -0.0755 460 TYR A CG 3289 C CD1 . TYR A 406 ? 0.3928 0.4170 0.5201 0.0397 -0.0417 -0.0791 460 TYR A CD1 3290 C CD2 . TYR A 406 ? 0.3803 0.4066 0.5043 0.0348 -0.0364 -0.0739 460 TYR A CD2 3291 C CE1 . TYR A 406 ? 0.4350 0.4617 0.5769 0.0394 -0.0453 -0.0811 460 TYR A CE1 3292 C CE2 . TYR A 406 ? 0.4103 0.4390 0.5485 0.0345 -0.0398 -0.0757 460 TYR A CE2 3293 C CZ . TYR A 406 ? 0.4633 0.4924 0.6108 0.0367 -0.0441 -0.0793 460 TYR A CZ 3294 O OH . TYR A 406 ? 0.5139 0.5453 0.6766 0.0362 -0.0476 -0.0810 460 TYR A OH 3295 N N . THR A 407 ? 0.3197 0.3287 0.4034 0.0421 -0.0398 -0.0725 461 THR A N 3296 C CA . THR A 407 ? 0.3019 0.3062 0.3817 0.0443 -0.0442 -0.0730 461 THR A CA 3297 C C . THR A 407 ? 0.3035 0.3063 0.3732 0.0428 -0.0404 -0.0695 461 THR A C 3298 O O . THR A 407 ? 0.2998 0.3056 0.3670 0.0399 -0.0347 -0.0670 461 THR A O 3299 C CB . THR A 407 ? 0.3181 0.3253 0.4110 0.0431 -0.0476 -0.0746 461 THR A CB 3300 O OG1 . THR A 407 ? 0.3277 0.3291 0.4163 0.0464 -0.0535 -0.0761 461 THR A OG1 3301 C CG2 . THR A 407 ? 0.3136 0.3267 0.4125 0.0380 -0.0422 -0.0716 461 THR A CG2 3302 N N . LEU A 408 ? 0.2905 0.2888 0.3553 0.0449 -0.0439 -0.0697 462 LEU A N 3303 C CA . LEU A 408 ? 0.2961 0.2925 0.3516 0.0439 -0.0409 -0.0665 462 LEU A CA 3304 C C . LEU A 408 ? 0.2825 0.2847 0.3449 0.0390 -0.0371 -0.0644 462 LEU A C 3305 O O . LEU A 408 ? 0.2782 0.2844 0.3525 0.0372 -0.0385 -0.0656 462 LEU A O 3306 C CB . LEU A 408 ? 0.2993 0.2888 0.3475 0.0482 -0.0461 -0.0676 462 LEU A CB 3307 C CG . LEU A 408 ? 0.2939 0.2800 0.3303 0.0485 -0.0434 -0.0645 462 LEU A CG 3308 C CD1 . LEU A 408 ? 0.3192 0.3019 0.3450 0.0504 -0.0403 -0.0630 462 LEU A CD1 3309 C CD2 . LEU A 408 ? 0.2984 0.2786 0.3304 0.0526 -0.0491 -0.0660 462 LEU A CD2 3310 N N . ARG A 409 ? 0.2739 0.2763 0.3291 0.0370 -0.0326 -0.0612 463 ARG A N 3311 C CA . ARG A 409 ? 0.2694 0.2764 0.3291 0.0327 -0.0291 -0.0590 463 ARG A CA 3312 C C . ARG A 409 ? 0.2593 0.2626 0.3088 0.0332 -0.0282 -0.0568 463 ARG A C 3313 O O . ARG A 409 ? 0.2464 0.2469 0.2865 0.0343 -0.0260 -0.0554 463 ARG A O 3314 C CB . ARG A 409 ? 0.2751 0.2872 0.3369 0.0294 -0.0232 -0.0573 463 ARG A CB 3315 C CG . ARG A 409 ? 0.2872 0.3039 0.3526 0.0252 -0.0189 -0.0547 463 ARG A CG 3316 C CD . ARG A 409 ? 0.3562 0.3769 0.4218 0.0229 -0.0135 -0.0535 463 ARG A CD 3317 N NE . ARG A 409 ? 0.4342 0.4590 0.5028 0.0195 -0.0094 -0.0511 463 ARG A NE 3318 C CZ . ARG A 409 ? 0.4622 0.4901 0.5297 0.0174 -0.0045 -0.0496 463 ARG A CZ 3319 N NH1 . ARG A 409 ? 0.4694 0.4972 0.5336 0.0182 -0.0030 -0.0502 463 ARG A NH1 3320 N NH2 . ARG A 409 ? 0.4474 0.4783 0.5169 0.0148 -0.0013 -0.0475 463 ARG A NH2 3321 N N . VAL A 410 ? 0.2587 0.2617 0.3104 0.0327 -0.0302 -0.0565 464 VAL A N 3322 C CA . VAL A 410 ? 0.2639 0.2632 0.3064 0.0334 -0.0298 -0.0547 464 VAL A CA 3323 C C . VAL A 410 ? 0.2622 0.2659 0.3094 0.0292 -0.0268 -0.0525 464 VAL A C 3324 O O . VAL A 410 ? 0.2708 0.2776 0.3278 0.0275 -0.0282 -0.0533 464 VAL A O 3325 C CB . VAL A 410 ? 0.2869 0.2806 0.3266 0.0376 -0.0361 -0.0567 464 VAL A CB 3326 C CG1 . VAL A 410 ? 0.2876 0.2778 0.3186 0.0384 -0.0358 -0.0548 464 VAL A CG1 3327 C CG2 . VAL A 410 ? 0.2767 0.2654 0.3113 0.0426 -0.0396 -0.0591 464 VAL A CG2 3328 N N . ASP A 411 ? 0.2586 0.2621 0.2987 0.0277 -0.0229 -0.0498 465 ASP A N 3329 C CA . ASP A 411 ? 0.2686 0.2749 0.3107 0.0244 -0.0205 -0.0477 465 ASP A CA 3330 C C . ASP A 411 ? 0.2520 0.2537 0.2845 0.0262 -0.0212 -0.0464 465 ASP A C 3331 O O . ASP A 411 ? 0.2527 0.2514 0.2768 0.0279 -0.0198 -0.0455 465 ASP A O 3332 C CB . ASP A 411 ? 0.2504 0.2611 0.2928 0.0208 -0.0147 -0.0454 465 ASP A CB 3333 C CG . ASP A 411 ? 0.3405 0.3555 0.3897 0.0195 -0.0127 -0.0463 465 ASP A CG 3334 O OD1 . ASP A 411 ? 0.3498 0.3650 0.4046 0.0209 -0.0154 -0.0485 465 ASP A OD1 3335 O OD2 . ASP A 411 ? 0.3895 0.4075 0.4380 0.0171 -0.0081 -0.0447 465 ASP A OD2 3336 N N . CYS A 412 ? 0.2498 0.2508 0.2839 0.0259 -0.0235 -0.0463 466 CYS A N 3337 C CA . CYS A 412 ? 0.2509 0.2474 0.2759 0.0280 -0.0243 -0.0452 466 CYS A CA 3338 C C . CYS A 412 ? 0.2444 0.2417 0.2728 0.0264 -0.0255 -0.0446 466 CYS A C 3339 O O . CYS A 412 ? 0.2667 0.2676 0.3047 0.0240 -0.0263 -0.0452 466 CYS A O 3340 C CB . CYS A 412 ? 0.2478 0.2377 0.2661 0.0336 -0.0288 -0.0471 466 CYS A CB 3341 S SG . CYS A 412 ? 0.2944 0.2825 0.3200 0.0361 -0.0362 -0.0509 466 CYS A SG 3342 N N . THR A 413 ? 0.2485 0.2425 0.2690 0.0276 -0.0254 -0.0432 467 THR A N 3343 C CA A THR A 413 ? 0.2396 0.2330 0.2616 0.0270 -0.0274 -0.0429 467 THR A CA 3344 C CA B THR A 413 ? 0.2448 0.2382 0.2667 0.0270 -0.0274 -0.0429 467 THR A CA 3345 C CA C THR A 413 ? 0.2396 0.2330 0.2616 0.0270 -0.0274 -0.0429 467 THR A CA 3346 C C . THR A 413 ? 0.2559 0.2464 0.2817 0.0300 -0.0339 -0.0459 467 THR A C 3347 O O . THR A 413 ? 0.2596 0.2460 0.2815 0.0342 -0.0371 -0.0479 467 THR A O 3348 C CB A THR A 413 ? 0.2335 0.2233 0.2453 0.0286 -0.0262 -0.0410 467 THR A CB 3349 C CB B THR A 413 ? 0.2431 0.2330 0.2549 0.0285 -0.0261 -0.0409 467 THR A CB 3350 C CB C THR A 413 ? 0.2335 0.2233 0.2453 0.0286 -0.0262 -0.0410 467 THR A CB 3351 O OG1 A THR A 413 ? 0.2386 0.2273 0.2516 0.0286 -0.0290 -0.0411 467 THR A OG1 3352 O OG1 B THR A 413 ? 0.2463 0.2349 0.2591 0.0286 -0.0289 -0.0411 467 THR A OG1 3353 O OG1 C THR A 413 ? 0.2386 0.2273 0.2516 0.0286 -0.0290 -0.0411 467 THR A OG1 3354 C CG2 A THR A 413 ? 0.2370 0.2210 0.2394 0.0337 -0.0278 -0.0417 467 THR A CG2 3355 C CG2 B THR A 413 ? 0.2482 0.2322 0.2505 0.0335 -0.0276 -0.0416 467 THR A CG2 3356 C CG2 C THR A 413 ? 0.2370 0.2209 0.2393 0.0337 -0.0278 -0.0417 467 THR A CG2 3357 N N . PRO A 414 ? 0.2491 0.2414 0.2826 0.0282 -0.0360 -0.0463 468 PRO A N 3358 C CA . PRO A 414 ? 0.2669 0.2559 0.3042 0.0313 -0.0428 -0.0494 468 PRO A CA 3359 C C . PRO A 414 ? 0.2768 0.2586 0.3025 0.0368 -0.0464 -0.0505 468 PRO A C 3360 O O . PRO A 414 ? 0.2887 0.2665 0.3149 0.0406 -0.0523 -0.0535 468 PRO A O 3361 C CB . PRO A 414 ? 0.2749 0.2661 0.3199 0.0284 -0.0437 -0.0488 468 PRO A CB 3362 C CG . PRO A 414 ? 0.2801 0.2769 0.3286 0.0235 -0.0375 -0.0458 468 PRO A CG 3363 C CD . PRO A 414 ? 0.2317 0.2287 0.2711 0.0234 -0.0326 -0.0440 468 PRO A CD 3364 N N . LEU A 415 ? 0.2589 0.2387 0.2742 0.0373 -0.0431 -0.0480 469 LEU A N 3365 C CA . LEU A 415 ? 0.2711 0.2439 0.2750 0.0428 -0.0458 -0.0486 469 LEU A CA 3366 C C . LEU A 415 ? 0.2745 0.2433 0.2731 0.0473 -0.0476 -0.0503 469 LEU A C 3367 O O . LEU A 415 ? 0.2980 0.2605 0.2886 0.0528 -0.0513 -0.0517 469 LEU A O 3368 C CB . LEU A 415 ? 0.2684 0.2403 0.2630 0.0425 -0.0410 -0.0452 469 LEU A CB 3369 C CG . LEU A 415 ? 0.2348 0.2090 0.2323 0.0393 -0.0401 -0.0437 469 LEU A CG 3370 C CD1 . LEU A 415 ? 0.2795 0.2527 0.2682 0.0393 -0.0355 -0.0406 469 LEU A CD1 3371 C CD2 . LEU A 415 ? 0.2661 0.2363 0.2643 0.0423 -0.0467 -0.0461 469 LEU A CD2 3372 N N . MET A 416 ? 0.2703 0.2426 0.2732 0.0453 -0.0450 -0.0503 470 MET A N 3373 C CA A MET A 416 ? 0.2779 0.2466 0.2759 0.0493 -0.0463 -0.0517 470 MET A CA 3374 C CA B MET A 416 ? 0.2819 0.2503 0.2796 0.0496 -0.0466 -0.0518 470 MET A CA 3375 C C . MET A 416 ? 0.2867 0.2558 0.2934 0.0504 -0.0517 -0.0555 470 MET A C 3376 O O . MET A 416 ? 0.2906 0.2564 0.2938 0.0541 -0.0537 -0.0572 470 MET A O 3377 C CB A MET A 416 ? 0.2704 0.2422 0.2667 0.0469 -0.0400 -0.0494 470 MET A CB 3378 C CB B MET A 416 ? 0.2847 0.2551 0.2788 0.0479 -0.0404 -0.0493 470 MET A CB 3379 C CG A MET A 416 ? 0.2817 0.2518 0.2685 0.0471 -0.0351 -0.0460 470 MET A CG 3380 C CG B MET A 416 ? 0.2917 0.2597 0.2757 0.0487 -0.0362 -0.0461 470 MET A CG 3381 S SD A MET A 416 ? 0.2750 0.2483 0.2613 0.0444 -0.0288 -0.0438 470 MET A SD 3382 S SD B MET A 416 ? 0.3583 0.3272 0.3380 0.0478 -0.0300 -0.0437 470 MET A SD 3383 C CE A MET A 416 ? 0.2852 0.2570 0.2631 0.0441 -0.0237 -0.0400 470 MET A CE 3384 C CE B MET A 416 ? 0.3421 0.3130 0.3189 0.0446 -0.0245 -0.0398 470 MET A CE 3385 N N . TYR A 417 ? 0.2814 0.2542 0.2996 0.0475 -0.0541 -0.0567 471 TYR A N 3386 C CA . TYR A 417 ? 0.2982 0.2722 0.3268 0.0480 -0.0588 -0.0602 471 TYR A CA 3387 C C . TYR A 417 ? 0.3199 0.2866 0.3427 0.0548 -0.0659 -0.0638 471 TYR A C 3388 O O . TYR A 417 ? 0.3317 0.2975 0.3565 0.0568 -0.0681 -0.0660 471 TYR A O 3389 C CB . TYR A 417 ? 0.2964 0.2744 0.3385 0.0447 -0.0611 -0.0611 471 TYR A CB 3390 C CG . TYR A 417 ? 0.2719 0.2576 0.3231 0.0382 -0.0551 -0.0584 471 TYR A CG 3391 C CD1 . TYR A 417 ? 0.2473 0.2364 0.2953 0.0355 -0.0484 -0.0557 471 TYR A CD1 3392 C CD2 . TYR A 417 ? 0.2566 0.2454 0.3190 0.0352 -0.0564 -0.0584 471 TYR A CD2 3393 C CE1 . TYR A 417 ? 0.2741 0.2697 0.3295 0.0301 -0.0431 -0.0533 471 TYR A CE1 3394 C CE2 . TYR A 417 ? 0.2838 0.2790 0.3538 0.0297 -0.0508 -0.0557 471 TYR A CE2 3395 C CZ . TYR A 417 ? 0.2942 0.2926 0.3601 0.0274 -0.0443 -0.0532 471 TYR A CZ 3396 O OH . TYR A 417 ? 0.2761 0.2802 0.3486 0.0226 -0.0391 -0.0506 471 TYR A OH 3397 N N . SER A 418 ? 0.3316 0.2927 0.3470 0.0585 -0.0695 -0.0644 472 SER A N 3398 C CA . SER A 418 ? 0.3297 0.2831 0.3390 0.0656 -0.0768 -0.0680 472 SER A CA 3399 C C . SER A 418 ? 0.3383 0.2868 0.3349 0.0701 -0.0752 -0.0675 472 SER A C 3400 O O . SER A 418 ? 0.3387 0.2836 0.3347 0.0743 -0.0799 -0.0706 472 SER A O 3401 C CB . SER A 418 ? 0.3463 0.2948 0.3495 0.0686 -0.0805 -0.0685 472 SER A CB 3402 O OG A SER A 418 ? 0.3896 0.3423 0.4053 0.0646 -0.0825 -0.0691 472 SER A OG 3403 O OG B SER A 418 ? 0.2678 0.2088 0.2661 0.0756 -0.0885 -0.0725 472 SER A OG 3404 N N . LEU A 419 ? 0.3395 0.2879 0.3268 0.0692 -0.0686 -0.0635 473 LEU A N 3405 C CA . LEU A 419 ? 0.3422 0.2871 0.3187 0.0723 -0.0651 -0.0620 473 LEU A CA 3406 C C . LEU A 419 ? 0.3520 0.3000 0.3351 0.0709 -0.0648 -0.0634 473 LEU A C 3407 O O . LEU A 419 ? 0.3534 0.2963 0.3304 0.0760 -0.0674 -0.0651 473 LEU A O 3408 C CB . LEU A 419 ? 0.3460 0.2928 0.3165 0.0695 -0.0572 -0.0573 473 LEU A CB 3409 C CG . LEU A 419 ? 0.3711 0.3168 0.3346 0.0705 -0.0521 -0.0550 473 LEU A CG 3410 C CD1 . LEU A 419 ? 0.4314 0.3680 0.3820 0.0783 -0.0548 -0.0558 473 LEU A CD1 3411 C CD2 . LEU A 419 ? 0.4218 0.3703 0.3826 0.0668 -0.0449 -0.0507 473 LEU A CD2 3412 N N . VAL A 420 ? 0.3310 0.2870 0.3261 0.0646 -0.0617 -0.0626 474 VAL A N 3413 C CA . VAL A 420 ? 0.3234 0.2830 0.3250 0.0628 -0.0605 -0.0635 474 VAL A CA 3414 C C . VAL A 420 ? 0.3291 0.2867 0.3371 0.0660 -0.0680 -0.0682 474 VAL A C 3415 O O . VAL A 420 ? 0.3325 0.2875 0.3379 0.0691 -0.0695 -0.0698 474 VAL A O 3416 C CB . VAL A 420 ? 0.3008 0.2694 0.3138 0.0554 -0.0553 -0.0617 474 VAL A CB 3417 C CG1 . VAL A 420 ? 0.3236 0.2958 0.3445 0.0541 -0.0549 -0.0632 474 VAL A CG1 3418 C CG2 . VAL A 420 ? 0.3289 0.2991 0.3351 0.0527 -0.0479 -0.0573 474 VAL A CG2 3419 N N . HIS A 421 ? 0.3335 0.2920 0.3501 0.0653 -0.0728 -0.0703 475 HIS A N 3420 C CA . HIS A 421 ? 0.3637 0.3196 0.3868 0.0689 -0.0810 -0.0751 475 HIS A CA 3421 C C . HIS A 421 ? 0.3774 0.3239 0.3871 0.0770 -0.0860 -0.0774 475 HIS A C 3422 O O . HIS A 421 ? 0.3743 0.3188 0.3853 0.0800 -0.0896 -0.0802 475 HIS A O 3423 C CB . HIS A 421 ? 0.3606 0.3176 0.3937 0.0677 -0.0859 -0.0770 475 HIS A CB 3424 C CG . HIS A 421 ? 0.3960 0.3619 0.4436 0.0604 -0.0818 -0.0752 475 HIS A CG 3425 N ND1 . HIS A 421 ? 0.4755 0.4435 0.5305 0.0577 -0.0830 -0.0749 475 HIS A ND1 3426 C CD2 . HIS A 421 ? 0.4124 0.3851 0.4673 0.0555 -0.0760 -0.0734 475 HIS A CD2 3427 C CE1 . HIS A 421 ? 0.4755 0.4513 0.5420 0.0515 -0.0779 -0.0728 475 HIS A CE1 3428 N NE2 . HIS A 421 ? 0.4021 0.3808 0.4686 0.0502 -0.0738 -0.0719 475 HIS A NE2 3429 N N . ASN A 422 ? 0.3804 0.3211 0.3775 0.0806 -0.0862 -0.0761 476 ASN A N 3430 C CA . ASN A 422 ? 0.3915 0.3225 0.3746 0.0889 -0.0907 -0.0779 476 ASN A CA 3431 C C . ASN A 422 ? 0.3990 0.3277 0.3731 0.0911 -0.0867 -0.0764 476 ASN A C 3432 O O . ASN A 422 ? 0.4153 0.3379 0.3838 0.0971 -0.0915 -0.0792 476 ASN A O 3433 C CB . ASN A 422 ? 0.3834 0.3089 0.3541 0.0923 -0.0905 -0.0763 476 ASN A CB 3434 C CG . ASN A 422 ? 0.4163 0.3412 0.3932 0.0926 -0.0968 -0.0789 476 ASN A CG 3435 O OD1 . ASN A 422 ? 0.3697 0.2985 0.3609 0.0899 -0.1011 -0.0818 476 ASN A OD1 3436 N ND2 . ASN A 422 ? 0.4372 0.3570 0.4034 0.0959 -0.0971 -0.0778 476 ASN A ND2 3437 N N . LEU A 423 ? 0.3780 0.3111 0.3506 0.0866 -0.0783 -0.0720 477 LEU A N 3438 C CA . LEU A 423 ? 0.3790 0.3102 0.3443 0.0883 -0.0744 -0.0704 477 LEU A CA 3439 C C . LEU A 423 ? 0.3774 0.3114 0.3515 0.0875 -0.0765 -0.0731 477 LEU A C 3440 O O . LEU A 423 ? 0.4012 0.3296 0.3682 0.0926 -0.0788 -0.0746 477 LEU A O 3441 C CB . LEU A 423 ? 0.3732 0.3083 0.3357 0.0837 -0.0652 -0.0653 477 LEU A CB 3442 C CG . LEU A 423 ? 0.3911 0.3252 0.3478 0.0844 -0.0604 -0.0632 477 LEU A CG 3443 C CD1 . LEU A 423 ? 0.3948 0.3188 0.3360 0.0926 -0.0620 -0.0631 477 LEU A CD1 3444 C CD2 . LEU A 423 ? 0.3551 0.2944 0.3124 0.0788 -0.0519 -0.0586 477 LEU A CD2 3445 N N . THR A 424 ? 0.3573 0.2996 0.3463 0.0812 -0.0757 -0.0737 478 THR A N 3446 C CA . THR A 424 ? 0.3648 0.3105 0.3632 0.0799 -0.0769 -0.0760 478 THR A CA 3447 C C . THR A 424 ? 0.3754 0.3162 0.3759 0.0855 -0.0862 -0.0811 478 THR A C 3448 O O . THR A 424 ? 0.3711 0.3115 0.3742 0.0870 -0.0881 -0.0833 478 THR A O 3449 C CB . THR A 424 ? 0.3508 0.3064 0.3650 0.0724 -0.0737 -0.0754 478 THR A CB 3450 O OG1 . THR A 424 ? 0.3317 0.2894 0.3548 0.0707 -0.0773 -0.0767 478 THR A OG1 3451 C CG2 . THR A 424 ? 0.3418 0.3020 0.3534 0.0674 -0.0647 -0.0706 478 THR A CG2 3452 N N . LYS A 425 ? 0.3950 0.3314 0.3939 0.0888 -0.0921 -0.0833 479 LYS A N 3453 C CA . LYS A 425 ? 0.4253 0.3558 0.4250 0.0950 -0.1018 -0.0886 479 LYS A CA 3454 C C . LYS A 425 ? 0.4495 0.3707 0.4327 0.1027 -0.1035 -0.0892 479 LYS A C 3455 O O . LYS A 425 ? 0.4487 0.3652 0.4318 0.1079 -0.1106 -0.0934 479 LYS A O 3456 C CB . LYS A 425 ? 0.4315 0.3591 0.4334 0.0970 -0.1083 -0.0911 479 LYS A CB 3457 C CG . LYS A 425 ? 0.4329 0.3690 0.4539 0.0904 -0.1088 -0.0918 479 LYS A CG 3458 C CD . LYS A 425 ? 0.4586 0.3921 0.4822 0.0919 -0.1148 -0.0938 479 LYS A CD 3459 C CE . LYS A 425 ? 0.4353 0.3778 0.4774 0.0844 -0.1130 -0.0931 479 LYS A CE 3460 N NZ . LYS A 425 ? 0.4776 0.4181 0.5229 0.0851 -0.1180 -0.0946 479 LYS A NZ 3461 N N . GLU A 426 ? 0.4466 0.3651 0.4163 0.1036 -0.0970 -0.0849 480 GLU A N 3462 C CA . GLU A 426 ? 0.4785 0.3876 0.4312 0.1112 -0.0976 -0.0845 480 GLU A CA 3463 C C . GLU A 426 ? 0.4716 0.3822 0.4222 0.1099 -0.0920 -0.0823 480 GLU A C 3464 O O . GLU A 426 ? 0.4946 0.3978 0.4321 0.1159 -0.0919 -0.0817 480 GLU A O 3465 C CB . GLU A 426 ? 0.4877 0.3913 0.4257 0.1142 -0.0942 -0.0810 480 GLU A CB 3466 C CG . GLU A 426 ? 0.5713 0.4722 0.5088 0.1164 -0.0995 -0.0829 480 GLU A CG 3467 C CD . GLU A 426 ? 0.6766 0.5699 0.6113 0.1240 -0.1101 -0.0885 480 GLU A CD 3468 O OE1 . GLU A 426 ? 0.6892 0.5762 0.6157 0.1300 -0.1128 -0.0902 480 GLU A OE1 3469 O OE2 . GLU A 426 ? 0.7233 0.6167 0.6640 0.1240 -0.1158 -0.0913 480 GLU A OE2 3470 N N . LEU A 427 ? 0.4380 0.3579 0.4011 0.1024 -0.0873 -0.0810 481 LEU A N 3471 C CA . LEU A 427 ? 0.4292 0.3513 0.3920 0.1007 -0.0823 -0.0792 481 LEU A CA 3472 C C . LEU A 427 ? 0.4309 0.3558 0.4045 0.1004 -0.0867 -0.0832 481 LEU A C 3473 O O . LEU A 427 ? 0.4338 0.3631 0.4206 0.0979 -0.0910 -0.0862 481 LEU A O 3474 C CB . LEU A 427 ? 0.4144 0.3449 0.3831 0.0927 -0.0737 -0.0750 481 LEU A CB 3475 C CG . LEU A 427 ? 0.4118 0.3407 0.3711 0.0922 -0.0682 -0.0706 481 LEU A CG 3476 C CD1 . LEU A 427 ? 0.3774 0.3149 0.3441 0.0843 -0.0607 -0.0671 481 LEU A CD1 3477 C CD2 . LEU A 427 ? 0.3884 0.3089 0.3316 0.0982 -0.0660 -0.0683 481 LEU A CD2 3478 N N . LYS A 428 ? 0.4395 0.3619 0.4081 0.1026 -0.0852 -0.0830 482 LYS A N 3479 C CA . LYS A 428 ? 0.4593 0.3839 0.4374 0.1027 -0.0893 -0.0868 482 LYS A CA 3480 C C . LYS A 428 ? 0.4441 0.3793 0.4365 0.0947 -0.0841 -0.0855 482 LYS A C 3481 O O . LYS A 428 ? 0.4576 0.3962 0.4475 0.0907 -0.0765 -0.0814 482 LYS A O 3482 C CB . LYS A 428 ? 0.4648 0.3824 0.4317 0.1085 -0.0898 -0.0870 482 LYS A CB 3483 C CG . LYS A 428 ? 0.5221 0.4283 0.4730 0.1173 -0.0944 -0.0879 482 LYS A CG 3484 C CD . LYS A 428 ? 0.6664 0.5653 0.6064 0.1234 -0.0952 -0.0882 482 LYS A CD 3485 C CE . LYS A 428 ? 0.7343 0.6343 0.6684 0.1208 -0.0859 -0.0830 482 LYS A CE 3486 N NZ . LYS A 428 ? 0.8152 0.7050 0.7330 0.1285 -0.0860 -0.0819 482 LYS A NZ 3487 N N . SER A 429 ? 0.4191 0.3594 0.4263 0.0924 -0.0881 -0.0890 483 SER A N 3488 C CA . SER A 429 ? 0.4124 0.3620 0.4323 0.0858 -0.0832 -0.0880 483 SER A CA 3489 C C . SER A 429 ? 0.4305 0.3798 0.4470 0.0865 -0.0803 -0.0875 483 SER A C 3490 O O . SER A 429 ? 0.4485 0.3927 0.4617 0.0917 -0.0853 -0.0904 483 SER A O 3491 C CB . SER A 429 ? 0.4006 0.3561 0.4381 0.0832 -0.0875 -0.0915 483 SER A CB 3492 O OG . SER A 429 ? 0.3828 0.3468 0.4311 0.0774 -0.0820 -0.0901 483 SER A OG 3493 N N . PRO A 430 ? 0.4183 0.3731 0.4362 0.0814 -0.0727 -0.0840 484 PRO A N 3494 C CA . PRO A 430 ? 0.4244 0.3794 0.4410 0.0818 -0.0704 -0.0839 484 PRO A CA 3495 C C . PRO A 430 ? 0.4203 0.3826 0.4524 0.0785 -0.0713 -0.0865 484 PRO A C 3496 O O . PRO A 430 ? 0.4131 0.3766 0.4456 0.0783 -0.0692 -0.0866 484 PRO A O 3497 C CB . PRO A 430 ? 0.4066 0.3645 0.4186 0.0776 -0.0620 -0.0792 484 PRO A CB 3498 C CG . PRO A 430 ? 0.4111 0.3753 0.4310 0.0724 -0.0598 -0.0778 484 PRO A CG 3499 C CD . PRO A 430 ? 0.4180 0.3781 0.4374 0.0757 -0.0662 -0.0801 484 PRO A CD 3500 N N . ASP A 431 ? 0.4154 0.3824 0.4601 0.0761 -0.0740 -0.0884 485 ASP A N 3501 C CA . ASP A 431 ? 0.4237 0.3989 0.4843 0.0719 -0.0729 -0.0898 485 ASP A CA 3502 C C . ASP A 431 ? 0.4421 0.4154 0.5082 0.0758 -0.0793 -0.0943 485 ASP A C 3503 O O . ASP A 431 ? 0.4507 0.4178 0.5139 0.0809 -0.0865 -0.0974 485 ASP A O 3504 C CB . ASP A 431 ? 0.4099 0.3906 0.4830 0.0681 -0.0736 -0.0900 485 ASP A CB 3505 C CG . ASP A 431 ? 0.4235 0.4076 0.4939 0.0635 -0.0671 -0.0857 485 ASP A CG 3506 O OD1 . ASP A 431 ? 0.3900 0.3717 0.4486 0.0636 -0.0627 -0.0827 485 ASP A OD1 3507 O OD2 . ASP A 431 ? 0.4124 0.4014 0.4930 0.0600 -0.0665 -0.0853 485 ASP A OD2 3508 N N . GLU A 432 ? 0.4579 0.4366 0.5324 0.0733 -0.0767 -0.0948 486 GLU A N 3509 C CA . GLU A 432 ? 0.4820 0.4603 0.5645 0.0763 -0.0823 -0.0992 486 GLU A CA 3510 C C . GLU A 432 ? 0.4743 0.4547 0.5707 0.0763 -0.0884 -0.1025 486 GLU A C 3511 O O . GLU A 432 ? 0.4632 0.4499 0.5703 0.0716 -0.0857 -0.1012 486 GLU A O 3512 C CB . GLU A 432 ? 0.4778 0.4625 0.5676 0.0730 -0.0775 -0.0987 486 GLU A CB 3513 C CG . GLU A 432 ? 0.5427 0.5242 0.6196 0.0742 -0.0734 -0.0966 486 GLU A CG 3514 C CD . GLU A 432 ? 0.6173 0.6015 0.6881 0.0699 -0.0654 -0.0918 486 GLU A CD 3515 O OE1 . GLU A 432 ? 0.6388 0.6205 0.7001 0.0706 -0.0620 -0.0900 486 GLU A OE1 3516 O OE2 . GLU A 432 ? 0.6326 0.6212 0.7082 0.0659 -0.0626 -0.0898 486 GLU A OE2 3517 N N . GLY A 433 ? 0.4918 0.4664 0.5879 0.0819 -0.0967 -0.1069 487 GLY A N 3518 C CA . GLY A 433 ? 0.4880 0.4633 0.5969 0.0827 -0.1037 -0.1105 487 GLY A CA 3519 C C . GLY A 433 ? 0.4979 0.4678 0.5997 0.0850 -0.1074 -0.1104 487 GLY A C 3520 O O . GLY A 433 ? 0.5073 0.4765 0.6186 0.0864 -0.1142 -0.1138 487 GLY A O 3521 N N . PHE A 434 ? 0.4816 0.4476 0.5674 0.0854 -0.1032 -0.1068 488 PHE A N 3522 C CA . PHE A 434 ? 0.4756 0.4361 0.5535 0.0879 -0.1065 -0.1066 488 PHE A CA 3523 C C . PHE A 434 ? 0.4898 0.4401 0.5479 0.0946 -0.1088 -0.1065 488 PHE A C 3524 O O . PHE A 434 ? 0.4802 0.4259 0.5270 0.0962 -0.1081 -0.1045 488 PHE A O 3525 C CB . PHE A 434 ? 0.4614 0.4268 0.5394 0.0822 -0.0995 -0.1020 488 PHE A CB 3526 C CG . PHE A 434 ? 0.4305 0.4048 0.5271 0.0764 -0.0978 -0.1020 488 PHE A CG 3527 C CD1 . PHE A 434 ? 0.4425 0.4170 0.5478 0.0763 -0.1028 -0.1038 488 PHE A CD1 3528 C CD2 . PHE A 434 ? 0.4169 0.3992 0.5225 0.0713 -0.0913 -0.1001 488 PHE A CD2 3529 C CE1 . PHE A 434 ? 0.4575 0.4401 0.5808 0.0709 -0.1008 -0.1034 488 PHE A CE1 3530 C CE2 . PHE A 434 ? 0.4358 0.4261 0.5585 0.0662 -0.0893 -0.0997 488 PHE A CE2 3531 C CZ . PHE A 434 ? 0.4191 0.4096 0.5508 0.0659 -0.0938 -0.1013 488 PHE A CZ 3532 N N . GLU A 435 ? 0.4920 0.4385 0.5458 0.0986 -0.1111 -0.1085 489 GLU A N 3533 C CA . GLU A 435 ? 0.5163 0.4523 0.5516 0.1058 -0.1138 -0.1088 489 GLU A CA 3534 C C . GLU A 435 ? 0.5213 0.4497 0.5511 0.1116 -0.1219 -0.1117 489 GLU A C 3535 O O . GLU A 435 ? 0.5362 0.4655 0.5777 0.1126 -0.1292 -0.1161 489 GLU A O 3536 C CB . GLU A 435 ? 0.5237 0.4570 0.5578 0.1095 -0.1165 -0.1114 489 GLU A CB 3537 C CG . GLU A 435 ? 0.5410 0.4800 0.5772 0.1050 -0.1086 -0.1084 489 GLU A CG 3538 C CD . GLU A 435 ? 0.5425 0.4922 0.5988 0.0987 -0.1069 -0.1095 489 GLU A CD 3539 O OE1 . GLU A 435 ? 0.5306 0.4855 0.5890 0.0947 -0.1003 -0.1071 489 GLU A OE1 3540 O OE2 . GLU A 435 ? 0.5733 0.5261 0.6431 0.0979 -0.1119 -0.1126 489 GLU A OE2 3541 N N . GLY A 436 ? 0.5212 0.4423 0.5337 0.1154 -0.1205 -0.1092 490 GLY A N 3542 C CA . GLY A 436 ? 0.5265 0.4401 0.5323 0.1212 -0.1278 -0.1118 490 GLY A CA 3543 C C . GLY A 436 ? 0.5264 0.4443 0.5415 0.1172 -0.1286 -0.1117 490 GLY A C 3544 O O . GLY A 436 ? 0.5334 0.4453 0.5440 0.1219 -0.1351 -0.1141 490 GLY A O 3545 N N . LYS A 437 ? 0.4983 0.4265 0.5262 0.1090 -0.1221 -0.1090 491 LYS A N 3546 C CA . LYS A 437 ? 0.4868 0.4195 0.5233 0.1046 -0.1217 -0.1082 491 LYS A CA 3547 C C . LYS A 437 ? 0.4584 0.3923 0.4849 0.1013 -0.1131 -0.1024 491 LYS A C 3548 O O . LYS A 437 ? 0.4461 0.3798 0.4636 0.1007 -0.1066 -0.0990 491 LYS A O 3549 C CB . LYS A 437 ? 0.4768 0.4200 0.5352 0.0977 -0.1205 -0.1090 491 LYS A CB 3550 C CG . LYS A 437 ? 0.5367 0.4806 0.6082 0.0998 -0.1279 -0.1143 491 LYS A CG 3551 C CD . LYS A 437 ? 0.5831 0.5187 0.6519 0.1069 -0.1388 -0.1193 491 LYS A CD 3552 C CE . LYS A 437 ? 0.6730 0.6088 0.7552 0.1093 -0.1468 -0.1249 491 LYS A CE 3553 N NZ . LYS A 437 ? 0.6975 0.6370 0.7979 0.1071 -0.1523 -0.1279 491 LYS A NZ 3554 N N . SER A 438 ? 0.4418 0.3769 0.4706 0.0994 -0.1134 -0.1016 492 SER A N 3555 C CA . SER A 438 ? 0.4322 0.3684 0.4525 0.0964 -0.1059 -0.0964 492 SER A CA 3556 C C . SER A 438 ? 0.4058 0.3522 0.4362 0.0880 -0.0975 -0.0929 492 SER A C 3557 O O . SER A 438 ? 0.3936 0.3467 0.4396 0.0841 -0.0979 -0.0944 492 SER A O 3558 C CB . SER A 438 ? 0.4248 0.3583 0.4437 0.0975 -0.1095 -0.0969 492 SER A CB 3559 O OG . SER A 438 ? 0.4283 0.3695 0.4646 0.0919 -0.1101 -0.0977 492 SER A OG 3560 N N . LEU A 439 ? 0.3984 0.3455 0.4196 0.0856 -0.0899 -0.0881 493 LEU A N 3561 C CA . LEU A 439 ? 0.3684 0.3243 0.3976 0.0781 -0.0823 -0.0848 493 LEU A CA 3562 C C . LEU A 439 ? 0.3582 0.3196 0.4004 0.0739 -0.0834 -0.0852 493 LEU A C 3563 O O . LEU A 439 ? 0.3535 0.3226 0.4082 0.0685 -0.0801 -0.0845 493 LEU A O 3564 C CB . LEU A 439 ? 0.3722 0.3268 0.3888 0.0771 -0.0751 -0.0800 493 LEU A CB 3565 C CG . LEU A 439 ? 0.3581 0.3206 0.3803 0.0701 -0.0673 -0.0763 493 LEU A CG 3566 C CD1 . LEU A 439 ? 0.3265 0.2944 0.3572 0.0675 -0.0650 -0.0771 493 LEU A CD1 3567 C CD2 . LEU A 439 ? 0.3374 0.2970 0.3462 0.0704 -0.0617 -0.0722 493 LEU A CD2 3568 N N . TYR A 440 ? 0.3643 0.3214 0.4032 0.0765 -0.0879 -0.0862 494 TYR A N 3569 C CA . TYR A 440 ? 0.3809 0.3425 0.4322 0.0728 -0.0894 -0.0867 494 TYR A CA 3570 C C . TYR A 440 ? 0.3884 0.3549 0.4577 0.0709 -0.0932 -0.0901 494 TYR A C 3571 O O . TYR A 440 ? 0.3750 0.3490 0.4577 0.0653 -0.0900 -0.0888 494 TYR A O 3572 C CB . TYR A 440 ? 0.3889 0.3440 0.4340 0.0771 -0.0954 -0.0883 494 TYR A CB 3573 C CG . TYR A 440 ? 0.4074 0.3668 0.4651 0.0733 -0.0970 -0.0886 494 TYR A CG 3574 C CD1 . TYR A 440 ? 0.3599 0.3221 0.4154 0.0694 -0.0917 -0.0848 494 TYR A CD1 3575 C CD2 . TYR A 440 ? 0.3941 0.3546 0.4664 0.0738 -0.1041 -0.0929 494 TYR A CD2 3576 C CE1 . TYR A 440 ? 0.3875 0.3531 0.4540 0.0660 -0.0931 -0.0849 494 TYR A CE1 3577 C CE2 . TYR A 440 ? 0.4017 0.3660 0.4863 0.0702 -0.1054 -0.0929 494 TYR A CE2 3578 C CZ . TYR A 440 ? 0.3790 0.3457 0.4602 0.0664 -0.0998 -0.0889 494 TYR A CZ 3579 O OH . TYR A 440 ? 0.3670 0.3370 0.4596 0.0630 -0.1009 -0.0887 494 TYR A OH 3580 N N . GLU A 441 ? 0.3910 0.3531 0.4606 0.0760 -0.1000 -0.0942 495 GLU A N 3581 C CA . GLU A 441 ? 0.4130 0.3793 0.5002 0.0749 -0.1042 -0.0978 495 GLU A CA 3582 C C . GLU A 441 ? 0.3869 0.3615 0.4834 0.0695 -0.0972 -0.0958 495 GLU A C 3583 O O . GLU A 441 ? 0.3766 0.3581 0.4894 0.0650 -0.0960 -0.0958 495 GLU A O 3584 C CB . GLU A 441 ? 0.4350 0.3944 0.5192 0.0819 -0.1128 -0.1028 495 GLU A CB 3585 C CG . GLU A 441 ? 0.4813 0.4450 0.5849 0.0808 -0.1176 -0.1068 495 GLU A CG 3586 C CD . GLU A 441 ? 0.5390 0.4952 0.6414 0.0881 -0.1282 -0.1125 495 GLU A CD 3587 O OE1 . GLU A 441 ? 0.5760 0.5245 0.6685 0.0933 -0.1340 -0.1143 495 GLU A OE1 3588 O OE2 . GLU A 441 ? 0.5412 0.4994 0.6528 0.0887 -0.1306 -0.1152 495 GLU A OE2 3589 N N . SER A 442 ? 0.3837 0.3574 0.4699 0.0701 -0.0926 -0.0939 496 SER A N 3590 C CA . SER A 442 ? 0.3796 0.3605 0.4731 0.0656 -0.0862 -0.0922 496 SER A CA 3591 C C . SER A 442 ? 0.3759 0.3640 0.4746 0.0590 -0.0786 -0.0880 496 SER A C 3592 O O . SER A 442 ? 0.3705 0.3657 0.4824 0.0549 -0.0755 -0.0875 496 SER A O 3593 C CB . SER A 442 ? 0.3870 0.3650 0.4687 0.0679 -0.0835 -0.0914 496 SER A CB 3594 O OG . SER A 442 ? 0.3714 0.3464 0.4381 0.0680 -0.0786 -0.0876 496 SER A OG 3595 N N . TRP A 443 ? 0.3589 0.3447 0.4468 0.0585 -0.0758 -0.0850 497 TRP A N 3596 C CA . TRP A 443 ? 0.3510 0.3425 0.4414 0.0529 -0.0688 -0.0811 497 TRP A CA 3597 C C . TRP A 443 ? 0.3540 0.3499 0.4595 0.0498 -0.0705 -0.0817 497 TRP A C 3598 O O . TRP A 443 ? 0.3490 0.3519 0.4644 0.0449 -0.0653 -0.0796 497 TRP A O 3599 C CB . TRP A 443 ? 0.3531 0.3398 0.4278 0.0541 -0.0667 -0.0783 497 TRP A CB 3600 C CG . TRP A 443 ? 0.3404 0.3315 0.4156 0.0491 -0.0607 -0.0744 497 TRP A CG 3601 C CD1 . TRP A 443 ? 0.3152 0.3135 0.3981 0.0439 -0.0546 -0.0721 497 TRP A CD1 3602 C CD2 . TRP A 443 ? 0.3348 0.3229 0.4016 0.0494 -0.0603 -0.0725 497 TRP A CD2 3603 N NE1 . TRP A 443 ? 0.3043 0.3042 0.3842 0.0408 -0.0507 -0.0689 497 TRP A NE1 3604 C CE2 . TRP A 443 ? 0.3379 0.3317 0.4083 0.0440 -0.0540 -0.0691 497 TRP A CE2 3605 C CE3 . TRP A 443 ? 0.3313 0.3120 0.3877 0.0540 -0.0647 -0.0733 497 TRP A CE3 3606 C CZ2 . TRP A 443 ? 0.2988 0.2916 0.3633 0.0427 -0.0521 -0.0666 497 TRP A CZ2 3607 C CZ3 . TRP A 443 ? 0.3363 0.3161 0.3867 0.0528 -0.0625 -0.0707 497 TRP A CZ3 3608 C CH2 . TRP A 443 ? 0.3175 0.3035 0.3725 0.0470 -0.0564 -0.0674 497 TRP A CH2 3609 N N . THR A 444 ? 0.3513 0.3428 0.4587 0.0530 -0.0779 -0.0846 498 THR A N 3610 C CA . THR A 444 ? 0.3756 0.3706 0.4977 0.0505 -0.0802 -0.0854 498 THR A CA 3611 C C . THR A 444 ? 0.3843 0.3851 0.5242 0.0485 -0.0806 -0.0872 498 THR A C 3612 O O . THR A 444 ? 0.3797 0.3867 0.5330 0.0441 -0.0775 -0.0857 498 THR A O 3613 C CB . THR A 444 ? 0.3917 0.3800 0.5118 0.0551 -0.0890 -0.0887 498 THR A CB 3614 O OG1 . THR A 444 ? 0.3706 0.3545 0.4759 0.0562 -0.0876 -0.0864 498 THR A OG1 3615 C CG2 . THR A 444 ? 0.4138 0.4056 0.5521 0.0527 -0.0926 -0.0902 498 THR A CG2 3616 N N . LYS A 445 ? 0.3883 0.3871 0.5282 0.0519 -0.0841 -0.0903 499 LYS A N 3617 C CA . LYS A 445 ? 0.4186 0.4228 0.5751 0.0503 -0.0845 -0.0921 499 LYS A CA 3618 C C . LYS A 445 ? 0.4142 0.4259 0.5745 0.0452 -0.0750 -0.0883 499 LYS A C 3619 O O . LYS A 445 ? 0.4225 0.4406 0.5983 0.0416 -0.0724 -0.0875 499 LYS A O 3620 C CB . LYS A 445 ? 0.4221 0.4219 0.5765 0.0555 -0.0906 -0.0964 499 LYS A CB 3621 C CG . LYS A 445 ? 0.4731 0.4785 0.6443 0.0541 -0.0907 -0.0984 499 LYS A CG 3622 C CD . LYS A 445 ? 0.5431 0.5512 0.7339 0.0531 -0.0957 -0.1009 499 LYS A CD 3623 C CE . LYS A 445 ? 0.5580 0.5703 0.7650 0.0532 -0.0975 -0.1037 499 LYS A CE 3624 N NZ . LYS A 445 ? 0.6044 0.6196 0.8319 0.0518 -0.1018 -0.1058 499 LYS A NZ 3625 N N . LYS A 446 ? 0.4127 0.4234 0.5587 0.0450 -0.0697 -0.0857 500 LYS A N 3626 C CA . LYS A 446 ? 0.4070 0.4241 0.5554 0.0409 -0.0613 -0.0826 500 LYS A CA 3627 C C . LYS A 446 ? 0.4078 0.4292 0.5569 0.0362 -0.0547 -0.0783 500 LYS A C 3628 O O . LYS A 446 ? 0.3899 0.4173 0.5449 0.0328 -0.0484 -0.0761 500 LYS A O 3629 C CB . LYS A 446 ? 0.4102 0.4245 0.5443 0.0428 -0.0588 -0.0820 500 LYS A CB 3630 C CG . LYS A 446 ? 0.4232 0.4351 0.5586 0.0467 -0.0635 -0.0857 500 LYS A CG 3631 C CD . LYS A 446 ? 0.4433 0.4520 0.5637 0.0484 -0.0606 -0.0846 500 LYS A CD 3632 C CE . LYS A 446 ? 0.4443 0.4508 0.5653 0.0520 -0.0644 -0.0879 500 LYS A CE 3633 N NZ . LYS A 446 ? 0.4479 0.4507 0.5539 0.0537 -0.0615 -0.0864 500 LYS A NZ 3634 N N . SER A 447 ? 0.4028 0.4207 0.5447 0.0365 -0.0561 -0.0772 501 SER A N 3635 C CA . SER A 447 ? 0.4037 0.4246 0.5442 0.0324 -0.0503 -0.0732 501 SER A CA 3636 C C . SER A 447 ? 0.4115 0.4307 0.5571 0.0324 -0.0547 -0.0738 501 SER A C 3637 O O . SER A 447 ? 0.3972 0.4121 0.5320 0.0335 -0.0558 -0.0729 501 SER A O 3638 C CB . SER A 447 ? 0.3991 0.4170 0.5220 0.0328 -0.0465 -0.0707 501 SER A CB 3639 O OG . SER A 447 ? 0.4217 0.4432 0.5435 0.0288 -0.0403 -0.0669 501 SER A OG 3640 N N . PRO A 448 ? 0.4072 0.4297 0.5698 0.0313 -0.0572 -0.0754 502 PRO A N 3641 C CA . PRO A 448 ? 0.4095 0.4299 0.5771 0.0315 -0.0620 -0.0762 502 PRO A CA 3642 C C . PRO A 448 ? 0.4087 0.4312 0.5740 0.0278 -0.0567 -0.0721 502 PRO A C 3643 O O . PRO A 448 ? 0.3972 0.4247 0.5638 0.0241 -0.0491 -0.0686 502 PRO A O 3644 C CB . PRO A 448 ? 0.4039 0.4281 0.5923 0.0307 -0.0651 -0.0785 502 PRO A CB 3645 C CG . PRO A 448 ? 0.4041 0.4341 0.5987 0.0285 -0.0590 -0.0772 502 PRO A CG 3646 C CD . PRO A 448 ? 0.4010 0.4289 0.5791 0.0299 -0.0560 -0.0764 502 PRO A CD 3647 N N . SER A 449 ? 0.4263 0.4445 0.5876 0.0291 -0.0610 -0.0726 503 SER A N 3648 C CA . SER A 449 ? 0.4557 0.4755 0.6175 0.0259 -0.0576 -0.0694 503 SER A CA 3649 C C . SER A 449 ? 0.4786 0.5048 0.6589 0.0219 -0.0547 -0.0680 503 SER A C 3650 O O . SER A 449 ? 0.4812 0.5084 0.6760 0.0226 -0.0592 -0.0708 503 SER A O 3651 C CB . SER A 449 ? 0.4570 0.4710 0.6145 0.0286 -0.0644 -0.0712 503 SER A CB 3652 O OG . SER A 449 ? 0.4542 0.4701 0.6150 0.0253 -0.0618 -0.0684 503 SER A OG 3653 N N . PRO A 450 ? 0.4967 0.5272 0.6769 0.0178 -0.0469 -0.0636 504 PRO A N 3654 C CA . PRO A 450 ? 0.5155 0.5518 0.7132 0.0143 -0.0435 -0.0618 504 PRO A CA 3655 C C . PRO A 450 ? 0.5321 0.5671 0.7398 0.0138 -0.0482 -0.0625 504 PRO A C 3656 O O . PRO A 450 ? 0.5469 0.5857 0.7716 0.0114 -0.0471 -0.0617 504 PRO A O 3657 C CB . PRO A 450 ? 0.5194 0.5592 0.7106 0.0109 -0.0342 -0.0570 504 PRO A CB 3658 C CG . PRO A 450 ? 0.5033 0.5386 0.6754 0.0122 -0.0344 -0.0563 504 PRO A CG 3659 C CD . PRO A 450 ? 0.4913 0.5212 0.6560 0.0166 -0.0414 -0.0603 504 PRO A CD 3660 N N . GLU A 451 ? 0.5361 0.5652 0.7335 0.0163 -0.0536 -0.0640 505 GLU A N 3661 C CA . GLU A 451 ? 0.5466 0.5736 0.7504 0.0161 -0.0583 -0.0646 505 GLU A CA 3662 C C . GLU A 451 ? 0.5419 0.5636 0.7486 0.0205 -0.0688 -0.0699 505 GLU A C 3663 O O . GLU A 451 ? 0.5476 0.5694 0.7686 0.0200 -0.0733 -0.0714 505 GLU A O 3664 C CB . GLU A 451 ? 0.5498 0.5744 0.7395 0.0153 -0.0559 -0.0618 505 GLU A CB 3665 C CG . GLU A 451 ? 0.5768 0.6005 0.7740 0.0140 -0.0586 -0.0613 505 GLU A CG 3666 C CD . GLU A 451 ? 0.6291 0.6509 0.8127 0.0130 -0.0554 -0.0582 505 GLU A CD 3667 O OE1 . GLU A 451 ? 0.6300 0.6508 0.8181 0.0119 -0.0574 -0.0576 505 GLU A OE1 3668 O OE2 . GLU A 451 ? 0.6287 0.6500 0.7974 0.0132 -0.0511 -0.0566 505 GLU A OE2 3669 N N . PHE A 452 ? 0.5317 0.5483 0.7249 0.0248 -0.0728 -0.0726 506 PHE A N 3670 C CA . PHE A 452 ? 0.5330 0.5432 0.7256 0.0298 -0.0831 -0.0776 506 PHE A CA 3671 C C . PHE A 452 ? 0.5260 0.5347 0.7202 0.0335 -0.0876 -0.0816 506 PHE A C 3672 O O . PHE A 452 ? 0.5161 0.5239 0.6985 0.0349 -0.0847 -0.0812 506 PHE A O 3673 C CB . PHE A 452 ? 0.5465 0.5500 0.7198 0.0332 -0.0855 -0.0778 506 PHE A CB 3674 C CG . PHE A 452 ? 0.5592 0.5633 0.7292 0.0303 -0.0821 -0.0743 506 PHE A CG 3675 C CD1 . PHE A 452 ? 0.5578 0.5629 0.7142 0.0284 -0.0747 -0.0702 506 PHE A CD1 3676 C CD2 . PHE A 452 ? 0.5680 0.5711 0.7482 0.0298 -0.0869 -0.0753 506 PHE A CD2 3677 C CE1 . PHE A 452 ? 0.5461 0.5514 0.6989 0.0260 -0.0718 -0.0671 506 PHE A CE1 3678 C CE2 . PHE A 452 ? 0.5897 0.5930 0.7664 0.0273 -0.0838 -0.0722 506 PHE A CE2 3679 C CZ . PHE A 452 ? 0.5742 0.5787 0.7370 0.0254 -0.0763 -0.0680 506 PHE A CZ 3680 N N A SER A 453 ? 0.5251 0.5330 0.7341 0.0352 -0.0950 -0.0857 507 SER A N 3681 N N B SER A 453 ? 0.5249 0.5330 0.7342 0.0351 -0.0949 -0.0856 507 SER A N 3682 C CA A SER A 453 ? 0.5175 0.5238 0.7296 0.0388 -0.1002 -0.0899 507 SER A CA 3683 C CA B SER A 453 ? 0.5170 0.5233 0.7289 0.0388 -0.1000 -0.0899 507 SER A CA 3684 C C A SER A 453 ? 0.5138 0.5117 0.7067 0.0450 -0.1058 -0.0928 507 SER A C 3685 C C B SER A 453 ? 0.5130 0.5110 0.7052 0.0449 -0.1054 -0.0925 507 SER A C 3686 O O A SER A 453 ? 0.5220 0.5143 0.7065 0.0477 -0.1103 -0.0937 507 SER A O 3687 O O B SER A 453 ? 0.5197 0.5123 0.7027 0.0473 -0.1091 -0.0930 507 SER A O 3688 C CB A SER A 453 ? 0.5218 0.5291 0.7554 0.0392 -0.1073 -0.0937 507 SER A CB 3689 C CB B SER A 453 ? 0.5219 0.5288 0.7546 0.0396 -0.1077 -0.0940 507 SER A CB 3690 O OG A SER A 453 ? 0.5141 0.5283 0.7642 0.0335 -0.1018 -0.0903 507 SER A OG 3691 O OG B SER A 453 ? 0.5249 0.5302 0.7600 0.0433 -0.1126 -0.0981 507 SER A OG 3692 N N . GLY A 454 ? 0.4998 0.4966 0.6854 0.0474 -0.1052 -0.0939 508 GLY A N 3693 C CA . GLY A 454 ? 0.4789 0.4676 0.6460 0.0536 -0.1097 -0.0961 508 GLY A CA 3694 C C . GLY A 454 ? 0.4479 0.4343 0.5948 0.0535 -0.1036 -0.0922 508 GLY A C 3695 O O . GLY A 454 ? 0.4447 0.4239 0.5753 0.0588 -0.1068 -0.0935 508 GLY A O 3696 N N A MET A 455 ? 0.4276 0.4198 0.5756 0.0479 -0.0950 -0.0874 509 MET A N 3697 N N B MET A 455 ? 0.4230 0.4153 0.5713 0.0479 -0.0951 -0.0874 509 MET A N 3698 C CA A MET A 455 ? 0.4128 0.4039 0.5437 0.0472 -0.0885 -0.0835 509 MET A CA 3699 C CA B MET A 455 ? 0.4031 0.3946 0.5348 0.0469 -0.0883 -0.0834 509 MET A CA 3700 C C A MET A 455 ? 0.3983 0.3956 0.5296 0.0430 -0.0796 -0.0801 509 MET A C 3701 C C B MET A 455 ? 0.3929 0.3900 0.5243 0.0434 -0.0800 -0.0804 509 MET A C 3702 O O A MET A 455 ? 0.3868 0.3906 0.5326 0.0391 -0.0766 -0.0793 509 MET A O 3703 O O B MET A 455 ? 0.3811 0.3842 0.5268 0.0403 -0.0779 -0.0804 509 MET A O 3704 C CB A MET A 455 ? 0.4092 0.4002 0.5380 0.0450 -0.0870 -0.0810 509 MET A CB 3705 C CB B MET A 455 ? 0.3930 0.3862 0.5254 0.0435 -0.0855 -0.0803 509 MET A CB 3706 C CG A MET A 455 ? 0.4548 0.4382 0.5764 0.0501 -0.0949 -0.0838 509 MET A CG 3707 C CG B MET A 455 ? 0.4015 0.3903 0.5378 0.0459 -0.0934 -0.0831 509 MET A CG 3708 S SD A MET A 455 ? 0.4870 0.4709 0.6074 0.0472 -0.0928 -0.0808 509 MET A SD 3709 S SD B MET A 455 ? 0.3992 0.3775 0.5163 0.0537 -0.1003 -0.0859 509 MET A SD 3710 C CE A MET A 455 ? 0.5034 0.4785 0.6198 0.0537 -0.1040 -0.0855 509 MET A CE 3711 C CE B MET A 455 ? 0.3989 0.3771 0.4977 0.0520 -0.0912 -0.0806 509 MET A CE 3712 N N . PRO A 456 ? 0.3853 0.3804 0.5008 0.0441 -0.0755 -0.0780 510 PRO A N 3713 C CA . PRO A 456 ? 0.3721 0.3724 0.4865 0.0406 -0.0674 -0.0750 510 PRO A CA 3714 C C . PRO A 456 ? 0.3565 0.3614 0.4710 0.0355 -0.0602 -0.0705 510 PRO A C 3715 O O . PRO A 456 ? 0.3515 0.3546 0.4622 0.0351 -0.0608 -0.0693 510 PRO A O 3716 C CB . PRO A 456 ? 0.3584 0.3535 0.4556 0.0441 -0.0666 -0.0746 510 PRO A CB 3717 C CG . PRO A 456 ? 0.3728 0.3611 0.4592 0.0478 -0.0708 -0.0751 510 PRO A CG 3718 C CD . PRO A 456 ? 0.3833 0.3706 0.4814 0.0490 -0.0782 -0.0785 510 PRO A CD 3719 N N . ARG A 457 ? 0.3429 0.3534 0.4606 0.0320 -0.0535 -0.0682 511 ARG A N 3720 C CA . ARG A 457 ? 0.3375 0.3519 0.4533 0.0277 -0.0464 -0.0641 511 ARG A CA 3721 C C . ARG A 457 ? 0.3322 0.3426 0.4309 0.0290 -0.0442 -0.0622 511 ARG A C 3722 O O . ARG A 457 ? 0.3117 0.3198 0.4023 0.0313 -0.0440 -0.0629 511 ARG A O 3723 C CB . ARG A 457 ? 0.3448 0.3656 0.4676 0.0245 -0.0402 -0.0625 511 ARG A CB 3724 C CG . ARG A 457 ? 0.3499 0.3746 0.4700 0.0204 -0.0327 -0.0583 511 ARG A CG 3725 C CD . ARG A 457 ? 0.4061 0.4362 0.5320 0.0183 -0.0272 -0.0573 511 ARG A CD 3726 N NE . ARG A 457 ? 0.4499 0.4842 0.5926 0.0169 -0.0277 -0.0580 511 ARG A NE 3727 C CZ . ARG A 457 ? 0.4889 0.5271 0.6403 0.0137 -0.0242 -0.0556 511 ARG A CZ 3728 N NH1 . ARG A 457 ? 0.4886 0.5269 0.6327 0.0117 -0.0202 -0.0524 511 ARG A NH1 3729 N NH2 . ARG A 457 ? 0.4866 0.5283 0.6540 0.0127 -0.0246 -0.0562 511 ARG A NH2 3730 N N . ILE A 458 ? 0.3196 0.3295 0.4137 0.0275 -0.0425 -0.0599 512 ILE A N 3731 C CA . ILE A 458 ? 0.3199 0.3279 0.4003 0.0273 -0.0385 -0.0573 512 ILE A CA 3732 C C . ILE A 458 ? 0.3296 0.3424 0.4121 0.0227 -0.0324 -0.0538 512 ILE A C 3733 O O . ILE A 458 ? 0.3366 0.3510 0.4257 0.0207 -0.0329 -0.0530 512 ILE A O 3734 C CB . ILE A 458 ? 0.3230 0.3245 0.3933 0.0308 -0.0426 -0.0578 512 ILE A CB 3735 C CG1 . ILE A 458 ? 0.3172 0.3131 0.3838 0.0361 -0.0488 -0.0612 512 ILE A CG1 3736 C CG2 . ILE A 458 ? 0.2997 0.2997 0.3573 0.0302 -0.0380 -0.0546 512 ILE A CG2 3737 C CD1 . ILE A 458 ? 0.3613 0.3503 0.4181 0.0403 -0.0534 -0.0620 512 ILE A CD1 3738 N N . SER A 459 ? 0.3332 0.3479 0.4098 0.0211 -0.0269 -0.0517 513 SER A N 3739 C CA . SER A 459 ? 0.3277 0.3468 0.4063 0.0172 -0.0213 -0.0487 513 SER A CA 3740 C C . SER A 459 ? 0.3248 0.3415 0.3934 0.0167 -0.0197 -0.0464 513 SER A C 3741 O O . SER A 459 ? 0.3031 0.3151 0.3627 0.0194 -0.0220 -0.0469 513 SER A O 3742 C CB . SER A 459 ? 0.3365 0.3593 0.4155 0.0157 -0.0164 -0.0479 513 SER A CB 3743 O OG . SER A 459 ? 0.3938 0.4191 0.4835 0.0159 -0.0177 -0.0498 513 SER A OG 3744 N N . LYS A 460 ? 0.3263 0.3465 0.3965 0.0134 -0.0153 -0.0439 514 LYS A N 3745 C CA . LYS A 460 ? 0.3309 0.3496 0.3926 0.0125 -0.0133 -0.0416 514 LYS A CA 3746 C C . LYS A 460 ? 0.3304 0.3486 0.3833 0.0127 -0.0100 -0.0407 514 LYS A C 3747 O O . LYS A 460 ? 0.3321 0.3528 0.3869 0.0122 -0.0076 -0.0410 514 LYS A O 3748 C CB . LYS A 460 ? 0.3115 0.3340 0.3783 0.0090 -0.0099 -0.0393 514 LYS A CB 3749 C CG . LYS A 460 ? 0.3437 0.3669 0.4207 0.0084 -0.0129 -0.0398 514 LYS A CG 3750 C CD . LYS A 460 ? 0.3454 0.3721 0.4271 0.0051 -0.0087 -0.0371 514 LYS A CD 3751 C CE . LYS A 460 ? 0.3620 0.3905 0.4567 0.0042 -0.0107 -0.0376 514 LYS A CE 3752 N NZ . LYS A 460 ? 0.3972 0.4288 0.4964 0.0011 -0.0062 -0.0345 514 LYS A NZ 3753 N N . LEU A 461 ? 0.3254 0.3407 0.3695 0.0134 -0.0096 -0.0395 515 LEU A N 3754 C CA . LEU A 461 ? 0.3341 0.3496 0.3714 0.0128 -0.0059 -0.0381 515 LEU A CA 3755 C C . LEU A 461 ? 0.3574 0.3764 0.3959 0.0096 -0.0019 -0.0360 515 LEU A C 3756 O O . LEU A 461 ? 0.3830 0.4023 0.4222 0.0082 -0.0018 -0.0348 515 LEU A O 3757 C CB . LEU A 461 ? 0.3291 0.3402 0.3571 0.0146 -0.0067 -0.0373 515 LEU A CB 3758 C CG . LEU A 461 ? 0.3114 0.3180 0.3352 0.0185 -0.0098 -0.0389 515 LEU A CG 3759 C CD1 . LEU A 461 ? 0.3505 0.3528 0.3661 0.0204 -0.0104 -0.0377 515 LEU A CD1 3760 C CD2 . LEU A 461 ? 0.2570 0.2641 0.2795 0.0191 -0.0079 -0.0394 515 LEU A CD2 3761 N N . GLY A 462 ? 0.3659 0.3872 0.4037 0.0086 0.0013 -0.0357 516 GLY A N 3762 C CA . GLY A 462 ? 0.3587 0.3827 0.3959 0.0062 0.0052 -0.0338 516 GLY A CA 3763 C C . GLY A 462 ? 0.3651 0.3877 0.3947 0.0064 0.0069 -0.0332 516 GLY A C 3764 O O . GLY A 462 ? 0.3642 0.3842 0.3886 0.0068 0.0062 -0.0323 516 GLY A O 3765 N N . SER A 463 ? 0.3562 0.3807 0.3859 0.0061 0.0093 -0.0336 517 SER A N 3766 C CA . SER A 463 ? 0.3433 0.3672 0.3674 0.0058 0.0112 -0.0330 517 SER A CA 3767 C C . SER A 463 ? 0.3319 0.3556 0.3556 0.0071 0.0114 -0.0345 517 SER A C 3768 O O . SER A 463 ? 0.3132 0.3379 0.3411 0.0079 0.0106 -0.0358 517 SER A O 3769 C CB . SER A 463 ? 0.3592 0.3860 0.3838 0.0039 0.0143 -0.0319 517 SER A CB 3770 O OG . SER A 463 ? 0.4218 0.4516 0.4517 0.0037 0.0159 -0.0324 517 SER A OG 3771 N N . GLY A 464 ? 0.2951 0.3177 0.3144 0.0072 0.0126 -0.0343 518 GLY A N 3772 C CA . GLY A 464 ? 0.2841 0.3072 0.3037 0.0080 0.0133 -0.0357 518 GLY A CA 3773 C C . GLY A 464 ? 0.2670 0.2869 0.2846 0.0100 0.0117 -0.0364 518 GLY A C 3774 O O . GLY A 464 ? 0.2657 0.2857 0.2839 0.0108 0.0119 -0.0376 518 GLY A O 3775 N N . ASN A 465 ? 0.2428 0.2597 0.2577 0.0109 0.0102 -0.0355 519 ASN A N 3776 C CA . ASN A 465 ? 0.2387 0.2519 0.2505 0.0130 0.0093 -0.0356 519 ASN A CA 3777 C C . ASN A 465 ? 0.2314 0.2415 0.2390 0.0136 0.0091 -0.0339 519 ASN A C 3778 O O . ASN A 465 ? 0.2179 0.2287 0.2251 0.0123 0.0093 -0.0329 519 ASN A O 3779 C CB . ASN A 465 ? 0.2482 0.2603 0.2618 0.0151 0.0071 -0.0372 519 ASN A CB 3780 C CG . ASN A 465 ? 0.2542 0.2641 0.2661 0.0170 0.0071 -0.0379 519 ASN A CG 3781 O OD1 . ASN A 465 ? 0.2570 0.2633 0.2647 0.0184 0.0073 -0.0368 519 ASN A OD1 3782 N ND2 . ASN A 465 ? 0.2230 0.2348 0.2382 0.0171 0.0071 -0.0396 519 ASN A ND2 3783 N N . ASP A 466 ? 0.2124 0.2188 0.2169 0.0158 0.0089 -0.0335 520 ASP A N 3784 C CA . ASP A 466 ? 0.2146 0.2183 0.2154 0.0162 0.0098 -0.0315 520 ASP A CA 3785 C C . ASP A 466 ? 0.2246 0.2265 0.2231 0.0172 0.0083 -0.0307 520 ASP A C 3786 O O . ASP A 466 ? 0.2248 0.2249 0.2206 0.0174 0.0092 -0.0290 520 ASP A O 3787 C CB . ASP A 466 ? 0.2319 0.2319 0.2302 0.0184 0.0106 -0.0308 520 ASP A CB 3788 C CG . ASP A 466 ? 0.2286 0.2300 0.2291 0.0171 0.0124 -0.0311 520 ASP A CG 3789 O OD1 . ASP A 466 ? 0.2345 0.2380 0.2364 0.0148 0.0135 -0.0307 520 ASP A OD1 3790 O OD2 . ASP A 466 ? 0.2282 0.2281 0.2288 0.0186 0.0124 -0.0318 520 ASP A OD2 3791 N N . PHE A 467 ? 0.2330 0.2353 0.2330 0.0178 0.0060 -0.0319 521 PHE A N 3792 C CA . PHE A 467 ? 0.2403 0.2409 0.2386 0.0187 0.0041 -0.0314 521 PHE A CA 3793 C C . PHE A 467 ? 0.2328 0.2363 0.2327 0.0157 0.0052 -0.0304 521 PHE A C 3794 O O . PHE A 467 ? 0.2296 0.2320 0.2281 0.0160 0.0040 -0.0297 521 PHE A O 3795 C CB . PHE A 467 ? 0.2495 0.2502 0.2506 0.0199 0.0008 -0.0334 521 PHE A CB 3796 C CG . PHE A 467 ? 0.2379 0.2433 0.2455 0.0173 0.0011 -0.0345 521 PHE A CG 3797 C CD1 . PHE A 467 ? 0.2654 0.2736 0.2763 0.0149 0.0012 -0.0340 521 PHE A CD1 3798 C CD2 . PHE A 467 ? 0.2458 0.2528 0.2564 0.0174 0.0014 -0.0359 521 PHE A CD2 3799 C CE1 . PHE A 467 ? 0.2681 0.2805 0.2849 0.0128 0.0022 -0.0346 521 PHE A CE1 3800 C CE2 . PHE A 467 ? 0.2721 0.2835 0.2888 0.0152 0.0022 -0.0367 521 PHE A CE2 3801 C CZ . PHE A 467 ? 0.2754 0.2894 0.2950 0.0130 0.0028 -0.0360 521 PHE A CZ 3802 N N . GLU A 468 ? 0.2063 0.2134 0.2091 0.0132 0.0070 -0.0306 522 GLU A N 3803 C CA . GLU A 468 ? 0.2228 0.2328 0.2275 0.0106 0.0078 -0.0300 522 GLU A CA 3804 C C . GLU A 468 ? 0.2131 0.2216 0.2146 0.0102 0.0082 -0.0282 522 GLU A C 3805 O O . GLU A 468 ? 0.2091 0.2178 0.2107 0.0097 0.0072 -0.0277 522 GLU A O 3806 C CB . GLU A 468 ? 0.2172 0.2306 0.2240 0.0086 0.0099 -0.0303 522 GLU A CB 3807 C CG . GLU A 468 ? 0.2864 0.3026 0.2954 0.0064 0.0106 -0.0298 522 GLU A CG 3808 C CD . GLU A 468 ? 0.3521 0.3711 0.3621 0.0050 0.0129 -0.0302 522 GLU A CD 3809 O OE1 . GLU A 468 ? 0.3437 0.3630 0.3516 0.0040 0.0139 -0.0294 522 GLU A OE1 3810 O OE2 . GLU A 468 ? 0.3571 0.3779 0.3699 0.0053 0.0134 -0.0314 522 GLU A OE2 3811 N N . VAL A 469 ? 0.2031 0.2101 0.2020 0.0106 0.0096 -0.0273 523 VAL A N 3812 C CA . VAL A 469 ? 0.2236 0.2293 0.2201 0.0103 0.0102 -0.0257 523 VAL A CA 3813 C C . VAL A 469 ? 0.2322 0.2348 0.2258 0.0125 0.0085 -0.0251 523 VAL A C 3814 O O . VAL A 469 ? 0.2221 0.2245 0.2147 0.0120 0.0080 -0.0242 523 VAL A O 3815 C CB . VAL A 469 ? 0.2289 0.2336 0.2246 0.0103 0.0121 -0.0248 523 VAL A CB 3816 C CG1 . VAL A 469 ? 0.2149 0.2161 0.2087 0.0132 0.0125 -0.0245 523 VAL A CG1 3817 C CG2 . VAL A 469 ? 0.2208 0.2251 0.2154 0.0095 0.0128 -0.0233 523 VAL A CG2 3818 N N . PHE A 470 ? 0.2253 0.2251 0.2172 0.0153 0.0075 -0.0256 524 PHE A N 3819 C CA . PHE A 470 ? 0.2162 0.2123 0.2043 0.0180 0.0057 -0.0252 524 PHE A CA 3820 C C . PHE A 470 ? 0.2092 0.2063 0.1991 0.0175 0.0030 -0.0262 524 PHE A C 3821 O O . PHE A 470 ? 0.2226 0.2178 0.2100 0.0185 0.0018 -0.0255 524 PHE A O 3822 C CB . PHE A 470 ? 0.2407 0.2333 0.2261 0.0215 0.0050 -0.0258 524 PHE A CB 3823 C CG . PHE A 470 ? 0.2409 0.2321 0.2248 0.0221 0.0079 -0.0245 524 PHE A CG 3824 C CD1 . PHE A 470 ? 0.2946 0.2832 0.2752 0.0235 0.0098 -0.0223 524 PHE A CD1 3825 C CD2 . PHE A 470 ? 0.2395 0.2324 0.2263 0.0212 0.0089 -0.0253 524 PHE A CD2 3826 C CE1 . PHE A 470 ? 0.2852 0.2725 0.2657 0.0240 0.0127 -0.0208 524 PHE A CE1 3827 C CE2 . PHE A 470 ? 0.2240 0.2155 0.2102 0.0217 0.0115 -0.0241 524 PHE A CE2 3828 C CZ . PHE A 470 ? 0.2918 0.2805 0.2753 0.0230 0.0134 -0.0218 524 PHE A CZ 3829 N N . PHE A 471 ? 0.2226 0.2225 0.2171 0.0162 0.0020 -0.0277 525 PHE A N 3830 C CA . PHE A 471 ? 0.2208 0.2216 0.2187 0.0157 -0.0006 -0.0287 525 PHE A CA 3831 C C . PHE A 471 ? 0.2216 0.2258 0.2224 0.0124 0.0005 -0.0278 525 PHE A C 3832 O O . PHE A 471 ? 0.2345 0.2379 0.2349 0.0123 -0.0008 -0.0273 525 PHE A O 3833 C CB . PHE A 471 ? 0.2039 0.2063 0.2066 0.0159 -0.0020 -0.0307 525 PHE A CB 3834 C CG . PHE A 471 ? 0.2218 0.2246 0.2289 0.0160 -0.0052 -0.0320 525 PHE A CG 3835 C CD1 . PHE A 471 ? 0.2186 0.2174 0.2228 0.0188 -0.0086 -0.0325 525 PHE A CD1 3836 C CD2 . PHE A 471 ? 0.2683 0.2752 0.2828 0.0135 -0.0048 -0.0325 525 PHE A CD2 3837 C CE1 . PHE A 471 ? 0.2618 0.2607 0.2708 0.0191 -0.0122 -0.0340 525 PHE A CE1 3838 C CE2 . PHE A 471 ? 0.2648 0.2720 0.2849 0.0135 -0.0079 -0.0336 525 PHE A CE2 3839 C CZ . PHE A 471 ? 0.2498 0.2529 0.2673 0.0163 -0.0119 -0.0345 525 PHE A CZ 3840 N N . GLN A 472 ? 0.1974 0.2049 0.2005 0.0100 0.0030 -0.0276 526 GLN A N 3841 C CA . GLN A 472 ? 0.2048 0.2154 0.2105 0.0072 0.0043 -0.0267 526 GLN A CA 3842 C C . GLN A 472 ? 0.2096 0.2195 0.2115 0.0062 0.0056 -0.0251 526 GLN A C 3843 O O . GLN A 472 ? 0.2296 0.2406 0.2324 0.0047 0.0055 -0.0243 526 GLN A O 3844 C CB . GLN A 472 ? 0.2030 0.2169 0.2116 0.0055 0.0066 -0.0272 526 GLN A CB 3845 C CG . GLN A 472 ? 0.2318 0.2468 0.2449 0.0062 0.0057 -0.0288 526 GLN A CG 3846 C CD . GLN A 472 ? 0.2576 0.2739 0.2762 0.0056 0.0041 -0.0291 526 GLN A CD 3847 O OE1 . GLN A 472 ? 0.2858 0.3018 0.3046 0.0048 0.0034 -0.0281 526 GLN A OE1 3848 N NE2 . GLN A 472 ? 0.2393 0.2571 0.2631 0.0059 0.0035 -0.0305 526 GLN A NE2 3849 N N . ARG A 473 ? 0.1897 0.1979 0.1881 0.0072 0.0067 -0.0246 527 ARG A N 3850 C CA . ARG A 473 ? 0.2049 0.2125 0.2007 0.0065 0.0076 -0.0231 527 ARG A CA 3851 C C . ARG A 473 ? 0.2064 0.2106 0.1989 0.0086 0.0063 -0.0224 527 ARG A C 3852 O O . ARG A 473 ? 0.2061 0.2100 0.1976 0.0080 0.0058 -0.0215 527 ARG A O 3853 C CB . ARG A 473 ? 0.2005 0.2082 0.1954 0.0062 0.0097 -0.0229 527 ARG A CB 3854 C CG . ARG A 473 ? 0.1974 0.2053 0.1912 0.0050 0.0105 -0.0217 527 ARG A CG 3855 C CD . ARG A 473 ? 0.2151 0.2225 0.2088 0.0051 0.0121 -0.0214 527 ARG A CD 3856 N NE . ARG A 473 ? 0.2112 0.2205 0.2068 0.0041 0.0128 -0.0226 527 ARG A NE 3857 C CZ . ARG A 473 ? 0.2220 0.2314 0.2184 0.0036 0.0137 -0.0227 527 ARG A CZ 3858 N NH1 . ARG A 473 ? 0.2170 0.2251 0.2132 0.0038 0.0141 -0.0216 527 ARG A NH1 3859 N NH2 . ARG A 473 ? 0.2199 0.2309 0.2177 0.0030 0.0141 -0.0240 527 ARG A NH2 3860 N N . LEU A 474 ? 0.2059 0.2072 0.1961 0.0114 0.0057 -0.0227 528 LEU A N 3861 C CA . LEU A 474 ? 0.2092 0.2068 0.1952 0.0140 0.0050 -0.0217 528 LEU A CA 3862 C C . LEU A 474 ? 0.2156 0.2111 0.2007 0.0161 0.0016 -0.0227 528 LEU A C 3863 O O . LEU A 474 ? 0.2408 0.2335 0.2222 0.0180 0.0007 -0.0220 528 LEU A O 3864 C CB . LEU A 474 ? 0.2217 0.2164 0.2046 0.0165 0.0066 -0.0209 528 LEU A CB 3865 C CG . LEU A 474 ? 0.2319 0.2283 0.2166 0.0148 0.0096 -0.0200 528 LEU A CG 3866 C CD1 . LEU A 474 ? 0.2292 0.2225 0.2117 0.0174 0.0114 -0.0190 528 LEU A CD1 3867 C CD2 . LEU A 474 ? 0.2663 0.2635 0.2510 0.0132 0.0105 -0.0187 528 LEU A CD2 3868 N N . GLY A 475 ? 0.1988 0.1955 0.1873 0.0158 -0.0002 -0.0244 529 GLY A N 3869 C CA . GLY A 475 ? 0.2127 0.2074 0.2014 0.0177 -0.0039 -0.0257 529 GLY A CA 3870 C C . GLY A 475 ? 0.2023 0.1922 0.1859 0.0222 -0.0056 -0.0262 529 GLY A C 3871 O O . GLY A 475 ? 0.2156 0.2023 0.1964 0.0247 -0.0084 -0.0267 529 GLY A O 3872 N N . ILE A 476 ? 0.2141 0.2033 0.1964 0.0233 -0.0041 -0.0264 530 ILE A N 3873 C CA . ILE A 476 ? 0.2058 0.1901 0.1831 0.0279 -0.0057 -0.0270 530 ILE A CA 3874 C C . ILE A 476 ? 0.2163 0.2011 0.1973 0.0286 -0.0088 -0.0296 530 ILE A C 3875 O O . ILE A 476 ? 0.2137 0.2023 0.2000 0.0260 -0.0076 -0.0302 530 ILE A O 3876 C CB . ILE A 476 ? 0.2142 0.1971 0.1880 0.0291 -0.0020 -0.0254 530 ILE A CB 3877 C CG1 . ILE A 476 ? 0.2498 0.2319 0.2207 0.0287 0.0007 -0.0229 530 ILE A CG1 3878 C CG2 . ILE A 476 ? 0.2458 0.2234 0.2140 0.0341 -0.0033 -0.0260 530 ILE A CG2 3879 C CD1 . ILE A 476 ? 0.2607 0.2431 0.2316 0.0282 0.0048 -0.0212 530 ILE A CD1 3880 N N . ALA A 477 ? 0.2153 0.1964 0.1942 0.0321 -0.0129 -0.0312 531 ALA A N 3881 C CA . ALA A 477 ? 0.2266 0.2076 0.2095 0.0332 -0.0166 -0.0340 531 ALA A CA 3882 C C . ALA A 477 ? 0.2364 0.2180 0.2196 0.0335 -0.0147 -0.0342 531 ALA A C 3883 O O . ALA A 477 ? 0.2578 0.2358 0.2344 0.0363 -0.0129 -0.0331 531 ALA A O 3884 C CB . ALA A 477 ? 0.2407 0.2156 0.2179 0.0387 -0.0212 -0.0355 531 ALA A CB 3885 N N . SER A 478 ? 0.2197 0.2054 0.2103 0.0309 -0.0149 -0.0356 532 SER A N 3886 C CA . SER A 478 ? 0.2212 0.2081 0.2124 0.0306 -0.0127 -0.0357 532 SER A CA 3887 C C . SER A 478 ? 0.2423 0.2300 0.2390 0.0313 -0.0159 -0.0385 532 SER A C 3888 O O . SER A 478 ? 0.2432 0.2327 0.2461 0.0303 -0.0188 -0.0400 532 SER A O 3889 C CB . SER A 478 ? 0.2280 0.2199 0.2227 0.0261 -0.0082 -0.0341 532 SER A CB 3890 O OG . SER A 478 ? 0.2441 0.2348 0.2338 0.0259 -0.0054 -0.0317 532 SER A OG 3891 N N . GLY A 479 ? 0.2429 0.2296 0.2383 0.0329 -0.0153 -0.0392 533 GLY A N 3892 C CA . GLY A 479 ? 0.2394 0.2271 0.2404 0.0336 -0.0183 -0.0419 533 GLY A CA 3893 C C . GLY A 479 ? 0.2538 0.2424 0.2545 0.0335 -0.0157 -0.0419 533 GLY A C 3894 O O . GLY A 479 ? 0.2407 0.2277 0.2359 0.0339 -0.0124 -0.0399 533 GLY A O 3895 N N . ARG A 480 ? 0.2421 0.2329 0.2492 0.0332 -0.0174 -0.0440 534 ARG A N 3896 C CA . ARG A 480 ? 0.2604 0.2518 0.2674 0.0334 -0.0156 -0.0444 534 ARG A CA 3897 C C . ARG A 480 ? 0.2563 0.2477 0.2686 0.0352 -0.0195 -0.0475 534 ARG A C 3898 O O . ARG A 480 ? 0.2622 0.2552 0.2808 0.0346 -0.0225 -0.0490 534 ARG A O 3899 C CB . ARG A 480 ? 0.2551 0.2521 0.2666 0.0290 -0.0112 -0.0432 534 ARG A CB 3900 C CG . ARG A 480 ? 0.2861 0.2886 0.3070 0.0259 -0.0113 -0.0441 534 ARG A CG 3901 C CD . ARG A 480 ? 0.2843 0.2915 0.3071 0.0219 -0.0065 -0.0424 534 ARG A CD 3902 N NE . ARG A 480 ? 0.2853 0.2929 0.3066 0.0221 -0.0043 -0.0425 534 ARG A NE 3903 C CZ . ARG A 480 ? 0.2985 0.3102 0.3229 0.0196 -0.0012 -0.0423 534 ARG A CZ 3904 N NH1 . ARG A 480 ? 0.2956 0.3113 0.3244 0.0168 0.0004 -0.0416 534 ARG A NH1 3905 N NH2 . ARG A 480 ? 0.2624 0.2737 0.2850 0.0201 0.0002 -0.0426 534 ARG A NH2 3906 N N . ALA A 481 ? 0.2640 0.2535 0.2739 0.0374 -0.0196 -0.0483 535 ALA A N 3907 C CA . ALA A 481 ? 0.2579 0.2471 0.2726 0.0394 -0.0235 -0.0514 535 ALA A CA 3908 C C . ALA A 481 ? 0.2758 0.2659 0.2904 0.0393 -0.0213 -0.0516 535 ALA A C 3909 O O . ALA A 481 ? 0.2742 0.2618 0.2818 0.0402 -0.0185 -0.0498 535 ALA A O 3910 C CB . ALA A 481 ? 0.2626 0.2450 0.2712 0.0448 -0.0285 -0.0530 535 ALA A CB 3911 N N A ARG A 482 ? 0.2620 0.2556 0.2848 0.0385 -0.0225 -0.0538 536 ARG A N 3912 N N B ARG A 482 ? 0.2682 0.2621 0.2913 0.0382 -0.0223 -0.0537 536 ARG A N 3913 C CA A ARG A 482 ? 0.2820 0.2763 0.3048 0.0387 -0.0208 -0.0543 536 ARG A CA 3914 C CA B ARG A 482 ? 0.2767 0.2729 0.3018 0.0374 -0.0200 -0.0541 536 ARG A CA 3915 C C A ARG A 482 ? 0.2672 0.2636 0.2986 0.0394 -0.0242 -0.0575 536 ARG A C 3916 C C B ARG A 482 ? 0.2731 0.2712 0.3064 0.0382 -0.0231 -0.0572 536 ARG A C 3917 O O A ARG A 482 ? 0.2614 0.2593 0.2994 0.0390 -0.0271 -0.0588 536 ARG A O 3918 O O B ARG A 482 ? 0.2611 0.2623 0.3027 0.0369 -0.0250 -0.0584 536 ARG A O 3919 C CB A ARG A 482 ? 0.2805 0.2795 0.3049 0.0347 -0.0154 -0.0524 536 ARG A CB 3920 C CB B ARG A 482 ? 0.2716 0.2731 0.2992 0.0330 -0.0147 -0.0521 536 ARG A CB 3921 C CG A ARG A 482 ? 0.3140 0.3193 0.3463 0.0305 -0.0132 -0.0519 536 ARG A CG 3922 C CG B ARG A 482 ? 0.2927 0.3001 0.3291 0.0293 -0.0135 -0.0520 536 ARG A CG 3923 C CD A ARG A 482 ? 0.3241 0.3293 0.3551 0.0291 -0.0129 -0.0502 536 ARG A CD 3924 C CD B ARG A 482 ? 0.2820 0.2909 0.3152 0.0264 -0.0097 -0.0492 536 ARG A CD 3925 N NE A ARG A 482 ? 0.3033 0.3141 0.3401 0.0251 -0.0099 -0.0491 536 ARG A NE 3926 N NE B ARG A 482 ? 0.2437 0.2581 0.2832 0.0227 -0.0068 -0.0483 536 ARG A NE 3927 C CZ A ARG A 482 ? 0.2777 0.2901 0.3186 0.0236 -0.0106 -0.0486 536 ARG A CZ 3928 C CZ B ARG A 482 ? 0.2117 0.2294 0.2520 0.0208 -0.0031 -0.0477 536 ARG A CZ 3929 N NH1 A ARG A 482 ? 0.2576 0.2669 0.2985 0.0256 -0.0148 -0.0496 536 ARG A NH1 3930 N NH1 B ARG A 482 ? 0.1758 0.1919 0.2119 0.0218 -0.0021 -0.0479 536 ARG A NH1 3931 N NH2 A ARG A 482 ? 0.2590 0.2760 0.3039 0.0202 -0.0071 -0.0472 536 ARG A NH2 3932 N NH2 B ARG A 482 ? 0.2186 0.2407 0.2635 0.0180 -0.0003 -0.0468 536 ARG A NH2 3933 N N . TYR A 483 ? 0.2788 0.2753 0.3107 0.0403 -0.0237 -0.0585 537 TYR A N 3934 C CA . TYR A 483 ? 0.2985 0.2979 0.3397 0.0406 -0.0263 -0.0615 537 TYR A CA 3935 C C . TYR A 483 ? 0.3038 0.3102 0.3529 0.0363 -0.0220 -0.0608 537 TYR A C 3936 O O . TYR A 483 ? 0.3175 0.3255 0.3631 0.0343 -0.0176 -0.0588 537 TYR A O 3937 C CB . TYR A 483 ? 0.2939 0.2892 0.3318 0.0445 -0.0289 -0.0635 537 TYR A CB 3938 C CG . TYR A 483 ? 0.2967 0.2886 0.3366 0.0483 -0.0354 -0.0666 537 TYR A CG 3939 C CD1 . TYR A 483 ? 0.3222 0.3084 0.3551 0.0515 -0.0387 -0.0665 537 TYR A CD1 3940 C CD2 . TYR A 483 ? 0.3206 0.3147 0.3698 0.0490 -0.0385 -0.0697 537 TYR A CD2 3941 C CE1 . TYR A 483 ? 0.3188 0.3013 0.3532 0.0554 -0.0453 -0.0697 537 TYR A CE1 3942 C CE2 . TYR A 483 ? 0.3121 0.3029 0.3637 0.0526 -0.0450 -0.0728 537 TYR A CE2 3943 C CZ . TYR A 483 ? 0.3340 0.3188 0.3778 0.0560 -0.0485 -0.0729 537 TYR A CZ 3944 O OH . TYR A 483 ? 0.3651 0.3460 0.4108 0.0599 -0.0555 -0.0763 537 TYR A OH 3945 N N . THR A 484 ? 0.3175 0.3281 0.3774 0.0351 -0.0233 -0.0624 538 THR A N 3946 C CA . THR A 484 ? 0.3249 0.3420 0.3921 0.0313 -0.0189 -0.0614 538 THR A CA 3947 C C . THR A 484 ? 0.3422 0.3628 0.4200 0.0317 -0.0202 -0.0639 538 THR A C 3948 O O . THR A 484 ? 0.3214 0.3393 0.4011 0.0346 -0.0249 -0.0665 538 THR A O 3949 C CB . THR A 484 ? 0.3193 0.3392 0.3907 0.0285 -0.0176 -0.0597 538 THR A CB 3950 O OG1 . THR A 484 ? 0.3428 0.3682 0.4185 0.0252 -0.0125 -0.0582 538 THR A OG1 3951 C CG2 . THR A 484 ? 0.3256 0.3460 0.4062 0.0292 -0.0220 -0.0617 538 THR A CG2 3952 N N . LYS A 485 ? 0.3731 0.3994 0.4574 0.0288 -0.0159 -0.0630 539 LYS A N 3953 C CA . LYS A 485 ? 0.4289 0.4593 0.5241 0.0288 -0.0159 -0.0649 539 LYS A CA 3954 C C . LYS A 485 ? 0.4573 0.4905 0.5646 0.0278 -0.0180 -0.0656 539 LYS A C 3955 O O . LYS A 485 ? 0.4512 0.4832 0.5581 0.0271 -0.0192 -0.0647 539 LYS A O 3956 C CB . LYS A 485 ? 0.4204 0.4554 0.5165 0.0265 -0.0100 -0.0634 539 LYS A CB 3957 C CG . LYS A 485 ? 0.4595 0.4988 0.5598 0.0233 -0.0056 -0.0609 539 LYS A CG 3958 C CD . LYS A 485 ? 0.5396 0.5816 0.6361 0.0218 0.0000 -0.0592 539 LYS A CD 3959 C CE . LYS A 485 ? 0.5737 0.6197 0.6745 0.0190 0.0043 -0.0567 539 LYS A CE 3960 N NZ . LYS A 485 ? 0.5954 0.6436 0.6916 0.0181 0.0095 -0.0551 539 LYS A NZ 3961 N N . ASN A 486 ? 0.5117 0.5485 0.6303 0.0280 -0.0184 -0.0674 540 ASN A N 3962 C CA . ASN A 486 ? 0.5688 0.6094 0.7013 0.0265 -0.0190 -0.0677 540 ASN A CA 3963 C C . ASN A 486 ? 0.6014 0.6471 0.7367 0.0229 -0.0122 -0.0643 540 ASN A C 3964 O O . ASN A 486 ? 0.6136 0.6627 0.7498 0.0222 -0.0075 -0.0636 540 ASN A O 3965 C CB . ASN A 486 ? 0.5704 0.6134 0.7146 0.0279 -0.0213 -0.0706 540 ASN A CB 3966 C CG . ASN A 486 ? 0.5970 0.6429 0.7567 0.0270 -0.0236 -0.0715 540 ASN A CG 3967 O OD1 . ASN A 486 ? 0.6327 0.6796 0.7955 0.0249 -0.0226 -0.0696 540 ASN A OD1 3968 N ND2 . ASN A 486 ? 0.6274 0.6744 0.7975 0.0287 -0.0270 -0.0745 540 ASN A ND2 3969 N N . TRP A 487 ? 0.6359 0.6816 0.7716 0.0211 -0.0116 -0.0624 541 TRP A N 3970 C CA . TRP A 487 ? 0.6813 0.7309 0.8184 0.0180 -0.0054 -0.0589 541 TRP A CA 3971 C C . TRP A 487 ? 0.7134 0.7687 0.8655 0.0164 -0.0022 -0.0582 541 TRP A C 3972 O O . TRP A 487 ? 0.7205 0.7783 0.8766 0.0141 0.0013 -0.0555 541 TRP A O 3973 C CB . TRP A 487 ? 0.6801 0.7272 0.8118 0.0169 -0.0063 -0.0571 541 TRP A CB 3974 C CG . TRP A 487 ? 0.7073 0.7505 0.8238 0.0175 -0.0058 -0.0563 541 TRP A CG 3975 C CD1 . TRP A 487 ? 0.7223 0.7600 0.8301 0.0198 -0.0103 -0.0576 541 TRP A CD1 3976 C CD2 . TRP A 487 ? 0.7247 0.7689 0.8332 0.0162 -0.0005 -0.0540 541 TRP A CD2 3977 N NE1 . TRP A 487 ? 0.7128 0.7484 0.8087 0.0197 -0.0078 -0.0560 541 TRP A NE1 3978 C CE2 . TRP A 487 ? 0.7210 0.7606 0.8172 0.0174 -0.0021 -0.0540 541 TRP A CE2 3979 C CE3 . TRP A 487 ? 0.7269 0.7753 0.8373 0.0143 0.0054 -0.0519 541 TRP A CE3 3980 C CZ2 . TRP A 487 ? 0.7269 0.7660 0.8138 0.0165 0.0015 -0.0522 541 TRP A CZ2 3981 C CZ3 . TRP A 487 ? 0.7438 0.7915 0.8437 0.0138 0.0088 -0.0504 541 TRP A CZ3 3982 C CH2 . TRP A 487 ? 0.7486 0.7918 0.8376 0.0148 0.0067 -0.0506 541 TRP A CH2 3983 N N . GLU A 488 ? 0.7439 0.8012 0.9046 0.0177 -0.0035 -0.0605 542 GLU A N 3984 C CA . GLU A 488 ? 0.7744 0.8373 0.9500 0.0164 0.0000 -0.0598 542 GLU A CA 3985 C C . GLU A 488 ? 0.7865 0.8515 0.9650 0.0180 0.0011 -0.0616 542 GLU A C 3986 O O . GLU A 488 ? 0.7945 0.8620 0.9861 0.0186 -0.0006 -0.0634 542 GLU A O 3987 C CB . GLU A 488 ? 0.7774 0.8410 0.9673 0.0161 -0.0043 -0.0610 542 GLU A CB 3988 C CG . GLU A 488 ? 0.8006 0.8605 0.9926 0.0190 -0.0125 -0.0652 542 GLU A CG 3989 C CD . GLU A 488 ? 0.8455 0.9062 1.0530 0.0187 -0.0169 -0.0666 542 GLU A CD 3990 O OE1 . GLU A 488 ? 0.8627 0.9266 1.0844 0.0192 -0.0179 -0.0684 542 GLU A OE1 3991 O OE2 . GLU A 488 ? 0.8650 0.9234 1.0711 0.0180 -0.0194 -0.0660 542 GLU A OE2 3992 N N . THR A 489 ? 0.8013 0.8651 0.9675 0.0186 0.0037 -0.0611 543 THR A N 3993 C CA . THR A 489 ? 0.8129 0.8782 0.9791 0.0202 0.0050 -0.0627 543 THR A CA 3994 C C . THR A 489 ? 0.8135 0.8796 0.9695 0.0195 0.0112 -0.0604 543 THR A C 3995 O O . THR A 489 ? 0.8114 0.8811 0.9709 0.0199 0.0154 -0.0601 543 THR A O 3996 C CB . THR A 489 ? 0.8199 0.8804 0.9800 0.0229 -0.0012 -0.0661 543 THR A CB 3997 O OG1 . THR A 489 ? 0.8334 0.8923 1.0018 0.0240 -0.0075 -0.0686 543 THR A OG1 3998 C CG2 . THR A 489 ? 0.8260 0.8879 0.9865 0.0246 -0.0001 -0.0679 543 THR A CG2 3999 N N . GLY A 494 ? 0.4512 0.4955 0.5230 0.0148 0.0154 -0.0494 548 GLY A N 4000 C CA . GLY A 494 ? 0.4184 0.4585 0.4841 0.0163 0.0123 -0.0507 548 GLY A CA 4001 C C . GLY A 494 ? 0.4057 0.4461 0.4748 0.0182 0.0109 -0.0531 548 GLY A C 4002 O O . GLY A 494 ? 0.4285 0.4708 0.5058 0.0186 0.0096 -0.0543 548 GLY A O 4003 N N . TYR A 495 ? 0.3619 0.4005 0.4253 0.0193 0.0111 -0.0539 549 TYR A N 4004 C CA . TYR A 495 ? 0.3300 0.3683 0.3957 0.0212 0.0095 -0.0562 549 TYR A CA 4005 C C . TYR A 495 ? 0.3049 0.3445 0.3680 0.0214 0.0124 -0.0566 549 TYR A C 4006 O O . TYR A 495 ? 0.3181 0.3573 0.3757 0.0204 0.0146 -0.0552 549 TYR A O 4007 C CB . TYR A 495 ? 0.3175 0.3507 0.3787 0.0231 0.0055 -0.0572 549 TYR A CB 4008 C CG . TYR A 495 ? 0.3274 0.3568 0.3794 0.0229 0.0058 -0.0557 549 TYR A CG 4009 C CD1 . TYR A 495 ? 0.2699 0.2973 0.3174 0.0238 0.0064 -0.0562 549 TYR A CD1 4010 C CD2 . TYR A 495 ? 0.3141 0.3418 0.3629 0.0219 0.0055 -0.0539 549 TYR A CD2 4011 C CE1 . TYR A 495 ? 0.3018 0.3258 0.3422 0.0236 0.0068 -0.0547 549 TYR A CE1 4012 C CE2 . TYR A 495 ? 0.2991 0.3236 0.3405 0.0218 0.0060 -0.0524 549 TYR A CE2 4013 C CZ . TYR A 495 ? 0.2512 0.2738 0.2888 0.0226 0.0067 -0.0528 549 TYR A CZ 4014 O OH . TYR A 495 ? 0.2635 0.2831 0.2953 0.0223 0.0073 -0.0513 549 TYR A OH 4015 N N . PRO A 496 ? 0.2926 0.3336 0.3595 0.0228 0.0123 -0.0585 550 PRO A N 4016 C CA . PRO A 496 ? 0.2932 0.3361 0.3584 0.0230 0.0154 -0.0588 550 PRO A CA 4017 C C . PRO A 496 ? 0.2703 0.3100 0.3268 0.0231 0.0156 -0.0586 550 PRO A C 4018 O O . PRO A 496 ? 0.2795 0.3205 0.3331 0.0227 0.0183 -0.0580 550 PRO A O 4019 C CB . PRO A 496 ? 0.3001 0.3441 0.3705 0.0248 0.0143 -0.0612 550 PRO A CB 4020 C CG . PRO A 496 ? 0.2832 0.3289 0.3621 0.0247 0.0126 -0.0615 550 PRO A CG 4021 C CD . PRO A 496 ? 0.3001 0.3420 0.3745 0.0241 0.0097 -0.0604 550 PRO A CD 4022 N N . LEU A 497 ? 0.2575 0.2930 0.3101 0.0239 0.0127 -0.0589 551 LEU A N 4023 C CA . LEU A 497 ? 0.2549 0.2876 0.3010 0.0242 0.0129 -0.0589 551 LEU A CA 4024 C C . LEU A 497 ? 0.2677 0.2981 0.3087 0.0228 0.0131 -0.0569 551 LEU A C 4025 O O . LEU A 497 ? 0.2802 0.3076 0.3168 0.0230 0.0126 -0.0566 551 LEU A O 4026 C CB . LEU A 497 ? 0.2466 0.2757 0.2914 0.0261 0.0103 -0.0602 551 LEU A CB 4027 C CG . LEU A 497 ? 0.2690 0.3005 0.3185 0.0275 0.0104 -0.0625 551 LEU A CG 4028 C CD1 . LEU A 497 ? 0.2921 0.3198 0.3404 0.0296 0.0074 -0.0638 551 LEU A CD1 4029 C CD2 . LEU A 497 ? 0.2571 0.2907 0.3054 0.0274 0.0130 -0.0631 551 LEU A CD2 4030 N N . TYR A 498 ? 0.2583 0.2901 0.3007 0.0215 0.0136 -0.0554 552 TYR A N 4031 C CA . TYR A 498 ? 0.2613 0.2912 0.2994 0.0201 0.0138 -0.0534 552 TYR A CA 4032 C C . TYR A 498 ? 0.2491 0.2784 0.2827 0.0196 0.0153 -0.0530 552 TYR A C 4033 O O . TYR A 498 ? 0.2754 0.3074 0.3092 0.0193 0.0175 -0.0534 552 TYR A O 4034 C CB . TYR A 498 ? 0.2564 0.2892 0.2978 0.0187 0.0148 -0.0522 552 TYR A CB 4035 C CG . TYR A 498 ? 0.2628 0.2945 0.3005 0.0172 0.0153 -0.0501 552 TYR A CG 4036 C CD1 . TYR A 498 ? 0.2444 0.2723 0.2786 0.0173 0.0133 -0.0493 552 TYR A CD1 4037 C CD2 . TYR A 498 ? 0.2704 0.3047 0.3080 0.0158 0.0180 -0.0489 552 TYR A CD2 4038 C CE1 . TYR A 498 ? 0.2494 0.2765 0.2806 0.0160 0.0138 -0.0474 552 TYR A CE1 4039 C CE2 . TYR A 498 ? 0.2460 0.2792 0.2802 0.0144 0.0182 -0.0471 552 TYR A CE2 4040 C CZ . TYR A 498 ? 0.2575 0.2873 0.2889 0.0144 0.0161 -0.0464 552 TYR A CZ 4041 O OH . TYR A 498 ? 0.2536 0.2826 0.2820 0.0132 0.0164 -0.0447 552 TYR A OH 4042 N N . HIS A 499 ? 0.2496 0.2753 0.2792 0.0196 0.0142 -0.0523 553 HIS A N 4043 C CA . HIS A 499 ? 0.2513 0.2759 0.2773 0.0190 0.0150 -0.0521 553 HIS A CA 4044 C C . HIS A 499 ? 0.2677 0.2927 0.2936 0.0200 0.0154 -0.0540 553 HIS A C 4045 O O . HIS A 499 ? 0.2559 0.2809 0.2795 0.0197 0.0160 -0.0543 553 HIS A O 4046 C CB . HIS A 499 ? 0.2633 0.2898 0.2880 0.0174 0.0166 -0.0508 553 HIS A CB 4047 C CG . HIS A 499 ? 0.2575 0.2826 0.2810 0.0163 0.0160 -0.0488 553 HIS A CG 4048 N ND1 . HIS A 499 ? 0.2512 0.2775 0.2733 0.0149 0.0172 -0.0475 553 HIS A ND1 4049 C CD2 . HIS A 499 ? 0.2753 0.2977 0.2984 0.0166 0.0145 -0.0479 553 HIS A CD2 4050 C CE1 . HIS A 499 ? 0.2294 0.2540 0.2506 0.0142 0.0163 -0.0459 553 HIS A CE1 4051 N NE2 . HIS A 499 ? 0.2489 0.2711 0.2705 0.0154 0.0147 -0.0462 553 HIS A NE2 4052 N N . SER A 500 ? 0.2894 0.3148 0.3178 0.0214 0.0147 -0.0555 554 SER A N 4053 C CA . SER A 500 ? 0.2592 0.2846 0.2876 0.0227 0.0147 -0.0575 554 SER A CA 4054 C C . SER A 500 ? 0.3120 0.3333 0.3395 0.0236 0.0128 -0.0579 554 SER A C 4055 O O . SER A 500 ? 0.2895 0.3083 0.3167 0.0237 0.0117 -0.0567 554 SER A O 4056 C CB . SER A 500 ? 0.2701 0.2987 0.3024 0.0238 0.0154 -0.0590 554 SER A CB 4057 O OG A SER A 500 ? 0.2498 0.2771 0.2845 0.0246 0.0136 -0.0594 554 SER A OG 4058 O OG B SER A 500 ? 0.2639 0.2914 0.2964 0.0254 0.0146 -0.0610 554 SER A OG 4059 N N . VAL A 501 ? 0.2771 0.2975 0.3041 0.0245 0.0125 -0.0595 555 VAL A N 4060 C CA . VAL A 501 ? 0.2973 0.3139 0.3242 0.0255 0.0110 -0.0598 555 VAL A CA 4061 C C . VAL A 501 ? 0.2985 0.3143 0.3271 0.0269 0.0099 -0.0603 555 VAL A C 4062 O O . VAL A 501 ? 0.3111 0.3231 0.3390 0.0278 0.0088 -0.0598 555 VAL A O 4063 C CB . VAL A 501 ? 0.2943 0.3107 0.3211 0.0263 0.0106 -0.0620 555 VAL A CB 4064 C CG1 . VAL A 501 ? 0.3150 0.3341 0.3435 0.0279 0.0110 -0.0642 555 VAL A CG1 4065 C CG2 . VAL A 501 ? 0.2879 0.2999 0.3150 0.0269 0.0091 -0.0619 555 VAL A CG2 4066 N N . TYR A 502 ? 0.2969 0.3159 0.3280 0.0273 0.0102 -0.0612 556 TYR A N 4067 C CA . TYR A 502 ? 0.2960 0.3143 0.3291 0.0289 0.0088 -0.0621 556 TYR A CA 4068 C C . TYR A 502 ? 0.3110 0.3272 0.3434 0.0291 0.0076 -0.0606 556 TYR A C 4069 O O . TYR A 502 ? 0.3020 0.3169 0.3356 0.0307 0.0058 -0.0614 556 TYR A O 4070 C CB . TYR A 502 ? 0.2900 0.3129 0.3274 0.0295 0.0095 -0.0639 556 TYR A CB 4071 C CG . TYR A 502 ? 0.2917 0.3163 0.3288 0.0298 0.0109 -0.0655 556 TYR A CG 4072 C CD1 . TYR A 502 ? 0.2996 0.3216 0.3356 0.0311 0.0097 -0.0669 556 TYR A CD1 4073 C CD2 . TYR A 502 ? 0.2873 0.3156 0.3247 0.0291 0.0132 -0.0654 556 TYR A CD2 4074 C CE1 . TYR A 502 ? 0.2788 0.3020 0.3141 0.0318 0.0105 -0.0686 556 TYR A CE1 4075 C CE2 . TYR A 502 ? 0.3232 0.3525 0.3593 0.0300 0.0143 -0.0670 556 TYR A CE2 4076 C CZ . TYR A 502 ? 0.2956 0.3224 0.3307 0.0314 0.0127 -0.0687 556 TYR A CZ 4077 O OH . TYR A 502 ? 0.3297 0.3572 0.3631 0.0325 0.0134 -0.0704 556 TYR A OH 4078 N N . GLU A 503 ? 0.2994 0.3149 0.3296 0.0276 0.0082 -0.0585 557 GLU A N 4079 C CA . GLU A 503 ? 0.3123 0.3249 0.3407 0.0281 0.0070 -0.0569 557 GLU A CA 4080 C C . GLU A 503 ? 0.2994 0.3067 0.3245 0.0296 0.0062 -0.0560 557 GLU A C 4081 O O . GLU A 503 ? 0.3152 0.3204 0.3380 0.0288 0.0073 -0.0542 557 GLU A O 4082 C CB . GLU A 503 ? 0.3105 0.3238 0.3374 0.0262 0.0081 -0.0549 557 GLU A CB 4083 C CG . GLU A 503 ? 0.3808 0.3972 0.4103 0.0255 0.0080 -0.0549 557 GLU A CG 4084 C CD . GLU A 503 ? 0.3410 0.3564 0.3681 0.0243 0.0083 -0.0527 557 GLU A CD 4085 O OE1 . GLU A 503 ? 0.3643 0.3829 0.3929 0.0226 0.0094 -0.0523 557 GLU A OE1 4086 O OE2 . GLU A 503 ? 0.3628 0.3741 0.3862 0.0251 0.0077 -0.0513 557 GLU A OE2 4087 N N . THR A 504 ? 0.2985 0.3035 0.3236 0.0320 0.0046 -0.0571 558 THR A N 4088 C CA . THR A 504 ? 0.2854 0.2852 0.3076 0.0337 0.0042 -0.0563 558 THR A CA 4089 C C . THR A 504 ? 0.2814 0.2772 0.3008 0.0364 0.0023 -0.0558 558 THR A C 4090 O O . THR A 504 ? 0.2928 0.2901 0.3134 0.0371 0.0006 -0.0569 558 THR A O 4091 C CB . THR A 504 ? 0.2975 0.2976 0.3217 0.0346 0.0038 -0.0584 558 THR A CB 4092 O OG1 . THR A 504 ? 0.3210 0.3233 0.3479 0.0359 0.0022 -0.0606 558 THR A OG1 4093 C CG2 . THR A 504 ? 0.3197 0.3229 0.3458 0.0327 0.0053 -0.0592 558 THR A CG2 4094 N N . TYR A 505 ? 0.2810 0.2715 0.2967 0.0383 0.0025 -0.0542 559 TYR A N 4095 C CA . TYR A 505 ? 0.2943 0.2801 0.3063 0.0417 0.0006 -0.0540 559 TYR A CA 4096 C C . TYR A 505 ? 0.3035 0.2909 0.3183 0.0433 -0.0019 -0.0572 559 TYR A C 4097 O O . TYR A 505 ? 0.2985 0.2848 0.3125 0.0453 -0.0044 -0.0581 559 TYR A O 4098 C CB . TYR A 505 ? 0.2933 0.2731 0.3014 0.0437 0.0017 -0.0520 559 TYR A CB 4099 C CG . TYR A 505 ? 0.3235 0.2978 0.3268 0.0478 -0.0001 -0.0519 559 TYR A CG 4100 C CD1 . TYR A 505 ? 0.3434 0.3141 0.3416 0.0498 -0.0006 -0.0502 559 TYR A CD1 4101 C CD2 . TYR A 505 ? 0.3616 0.3340 0.3652 0.0501 -0.0017 -0.0537 559 TYR A CD2 4102 C CE1 . TYR A 505 ? 0.3776 0.3427 0.3705 0.0542 -0.0025 -0.0502 559 TYR A CE1 4103 C CE2 . TYR A 505 ? 0.3898 0.3566 0.3883 0.0544 -0.0037 -0.0537 559 TYR A CE2 4104 C CZ . TYR A 505 ? 0.4069 0.3700 0.3999 0.0565 -0.0042 -0.0520 559 TYR A CZ 4105 O OH . TYR A 505 ? 0.4006 0.3573 0.3874 0.0614 -0.0064 -0.0521 559 TYR A OH 4106 N N . GLU A 506 ? 0.2988 0.2887 0.3172 0.0425 -0.0015 -0.0590 560 GLU A N 4107 C CA . GLU A 506 ? 0.3226 0.3138 0.3440 0.0443 -0.0039 -0.0619 560 GLU A CA 4108 C C . GLU A 506 ? 0.3158 0.3119 0.3419 0.0433 -0.0051 -0.0636 560 GLU A C 4109 O O . GLU A 506 ? 0.3350 0.3310 0.3630 0.0454 -0.0079 -0.0655 560 GLU A O 4110 C CB . GLU A 506 ? 0.3405 0.3335 0.3648 0.0437 -0.0031 -0.0635 560 GLU A CB 4111 C CG . GLU A 506 ? 0.3661 0.3538 0.3870 0.0451 -0.0026 -0.0623 560 GLU A CG 4112 C CD . GLU A 506 ? 0.3954 0.3812 0.4141 0.0435 -0.0001 -0.0594 560 GLU A CD 4113 O OE1 . GLU A 506 ? 0.3709 0.3605 0.3917 0.0407 0.0013 -0.0591 560 GLU A OE1 4114 O OE2 . GLU A 506 ? 0.3862 0.3664 0.4014 0.0452 0.0004 -0.0574 560 GLU A OE2 4115 N N . LEU A 507 ? 0.2971 0.2977 0.3256 0.0403 -0.0030 -0.0629 561 LEU A N 4116 C CA . LEU A 507 ? 0.3126 0.3177 0.3457 0.0390 -0.0035 -0.0638 561 LEU A CA 4117 C C . LEU A 507 ? 0.3126 0.3148 0.3441 0.0409 -0.0062 -0.0636 561 LEU A C 4118 O O . LEU A 507 ? 0.3163 0.3201 0.3523 0.0419 -0.0087 -0.0656 561 LEU A O 4119 C CB . LEU A 507 ? 0.3066 0.3155 0.3405 0.0358 -0.0006 -0.0623 561 LEU A CB 4120 C CG . LEU A 507 ? 0.3114 0.3245 0.3500 0.0345 -0.0007 -0.0626 561 LEU A CG 4121 C CD1 . LEU A 507 ? 0.2956 0.3133 0.3414 0.0347 -0.0009 -0.0651 561 LEU A CD1 4122 C CD2 . LEU A 507 ? 0.2916 0.3072 0.3295 0.0316 0.0019 -0.0608 561 LEU A CD2 4123 N N . VAL A 508 ? 0.3184 0.3161 0.3437 0.0415 -0.0060 -0.0613 562 VAL A N 4124 C CA . VAL A 508 ? 0.3177 0.3122 0.3404 0.0437 -0.0087 -0.0611 562 VAL A CA 4125 C C . VAL A 508 ? 0.3325 0.3224 0.3531 0.0478 -0.0122 -0.0628 562 VAL A C 4126 O O . VAL A 508 ? 0.3327 0.3227 0.3560 0.0494 -0.0156 -0.0648 562 VAL A O 4127 C CB . VAL A 508 ? 0.2989 0.2896 0.3152 0.0436 -0.0073 -0.0580 562 VAL A CB 4128 C CG1 . VAL A 508 ? 0.3004 0.2868 0.3128 0.0467 -0.0104 -0.0579 562 VAL A CG1 4129 C CG2 . VAL A 508 ? 0.3283 0.3233 0.3467 0.0397 -0.0044 -0.0565 562 VAL A CG2 4130 N N . GLU A 509 ? 0.3397 0.3256 0.3561 0.0495 -0.0114 -0.0621 563 GLU A N 4131 C CA . GLU A 509 ? 0.3766 0.3569 0.3892 0.0539 -0.0144 -0.0633 563 GLU A CA 4132 C C . GLU A 509 ? 0.3766 0.3600 0.3956 0.0546 -0.0172 -0.0668 563 GLU A C 4133 O O . GLU A 509 ? 0.3853 0.3657 0.4035 0.0580 -0.0211 -0.0687 563 GLU A O 4134 C CB . GLU A 509 ? 0.3730 0.3485 0.3802 0.0552 -0.0124 -0.0613 563 GLU A CB 4135 C CG . GLU A 509 ? 0.4340 0.4025 0.4353 0.0602 -0.0150 -0.0617 563 GLU A CG 4136 C CD . GLU A 509 ? 0.5140 0.4831 0.5186 0.0617 -0.0172 -0.0647 563 GLU A CD 4137 O OE1 . GLU A 509 ? 0.4939 0.4679 0.5043 0.0589 -0.0156 -0.0658 563 GLU A OE1 4138 O OE2 . GLU A 509 ? 0.5284 0.4928 0.5296 0.0659 -0.0206 -0.0661 563 GLU A OE2 4139 N N . LYS A 510 ? 0.3582 0.3474 0.3835 0.0517 -0.0152 -0.0679 564 LYS A N 4140 C CA . LYS A 510 ? 0.3582 0.3506 0.3902 0.0525 -0.0173 -0.0712 564 LYS A CA 4141 C C . LYS A 510 ? 0.3721 0.3692 0.4115 0.0513 -0.0189 -0.0727 564 LYS A C 4142 O O . LYS A 510 ? 0.3692 0.3665 0.4129 0.0535 -0.0226 -0.0754 564 LYS A O 4143 C CB . LYS A 510 ? 0.3365 0.3328 0.3720 0.0504 -0.0145 -0.0717 564 LYS A CB 4144 C CG . LYS A 510 ? 0.3711 0.3627 0.4012 0.0519 -0.0137 -0.0709 564 LYS A CG 4145 C CD . LYS A 510 ? 0.3644 0.3605 0.3989 0.0499 -0.0114 -0.0720 564 LYS A CD 4146 C CE . LYS A 510 ? 0.4621 0.4545 0.4925 0.0504 -0.0100 -0.0709 564 LYS A CE 4147 N NZ . LYS A 510 ? 0.5127 0.4986 0.5385 0.0541 -0.0123 -0.0709 564 LYS A NZ 4148 N N . PHE A 511 ? 0.3437 0.3448 0.3852 0.0480 -0.0164 -0.0712 565 PHE A N 4149 C CA . PHE A 511 ? 0.3501 0.3570 0.4005 0.0462 -0.0167 -0.0724 565 PHE A CA 4150 C C . PHE A 511 ? 0.3591 0.3656 0.4098 0.0458 -0.0182 -0.0716 565 PHE A C 4151 O O . PHE A 511 ? 0.3791 0.3889 0.4376 0.0454 -0.0198 -0.0731 565 PHE A O 4152 C CB . PHE A 511 ? 0.3391 0.3521 0.3940 0.0428 -0.0123 -0.0718 565 PHE A CB 4153 C CG . PHE A 511 ? 0.3708 0.3848 0.4263 0.0433 -0.0111 -0.0731 565 PHE A CG 4154 C CD1 . PHE A 511 ? 0.4022 0.4163 0.4622 0.0456 -0.0138 -0.0759 565 PHE A CD1 4155 C CD2 . PHE A 511 ? 0.3487 0.3630 0.4005 0.0418 -0.0078 -0.0717 565 PHE A CD2 4156 C CE1 . PHE A 511 ? 0.4002 0.4148 0.4604 0.0463 -0.0129 -0.0771 565 PHE A CE1 4157 C CE2 . PHE A 511 ? 0.4130 0.4278 0.4652 0.0425 -0.0070 -0.0730 565 PHE A CE2 4158 C CZ . PHE A 511 ? 0.3990 0.4138 0.4552 0.0447 -0.0094 -0.0757 565 PHE A CZ 4159 N N . TYR A 512 ? 0.3542 0.3567 0.3971 0.0459 -0.0175 -0.0692 566 TYR A N 4160 C CA . TYR A 512 ? 0.3330 0.3351 0.3758 0.0455 -0.0189 -0.0684 566 TYR A CA 4161 C C . TYR A 512 ? 0.3297 0.3253 0.3673 0.0497 -0.0235 -0.0692 566 TYR A C 4162 O O . TYR A 512 ? 0.3361 0.3318 0.3775 0.0506 -0.0270 -0.0707 566 TYR A O 4163 C CB . TYR A 512 ? 0.3293 0.3318 0.3676 0.0428 -0.0150 -0.0651 566 TYR A CB 4164 C CG . TYR A 512 ? 0.3230 0.3322 0.3675 0.0388 -0.0116 -0.0646 566 TYR A CG 4165 C CD1 . TYR A 512 ? 0.3185 0.3309 0.3647 0.0373 -0.0085 -0.0647 566 TYR A CD1 4166 C CD2 . TYR A 512 ? 0.3610 0.3731 0.4097 0.0369 -0.0116 -0.0640 566 TYR A CD2 4167 C CE1 . TYR A 512 ? 0.3069 0.3250 0.3578 0.0342 -0.0052 -0.0641 566 TYR A CE1 4168 C CE2 . TYR A 512 ? 0.3623 0.3803 0.4163 0.0336 -0.0081 -0.0632 566 TYR A CE2 4169 C CZ . TYR A 512 ? 0.3249 0.3456 0.3795 0.0324 -0.0049 -0.0632 566 TYR A CZ 4170 O OH . TYR A 512 ? 0.3677 0.3936 0.4268 0.0298 -0.0015 -0.0625 566 TYR A OH 4171 N N . ASP A 513 ? 0.3286 0.3182 0.3573 0.0524 -0.0234 -0.0681 567 ASP A N 4172 C CA . ASP A 513 ? 0.3406 0.3233 0.3620 0.0566 -0.0271 -0.0682 567 ASP A CA 4173 C C . ASP A 513 ? 0.3555 0.3319 0.3691 0.0603 -0.0274 -0.0678 567 ASP A C 4174 O O . ASP A 513 ? 0.3405 0.3119 0.3455 0.0618 -0.0257 -0.0652 567 ASP A O 4175 C CB . ASP A 513 ? 0.3340 0.3152 0.3502 0.0555 -0.0252 -0.0652 567 ASP A CB 4176 C CG . ASP A 513 ? 0.3747 0.3495 0.3844 0.0598 -0.0291 -0.0655 567 ASP A CG 4177 O OD1 . ASP A 513 ? 0.3708 0.3429 0.3813 0.0634 -0.0341 -0.0684 567 ASP A OD1 4178 O OD2 . ASP A 513 ? 0.3490 0.3212 0.3524 0.0598 -0.0274 -0.0629 567 ASP A OD2 4179 N N . PRO A 514 ? 0.3733 0.3498 0.3901 0.0620 -0.0294 -0.0704 568 PRO A N 4180 C CA . PRO A 514 ? 0.3825 0.3530 0.3921 0.0654 -0.0295 -0.0699 568 PRO A CA 4181 C C . PRO A 514 ? 0.3922 0.3540 0.3912 0.0706 -0.0319 -0.0690 568 PRO A C 4182 O O . PRO A 514 ? 0.4167 0.3734 0.4080 0.0725 -0.0297 -0.0667 568 PRO A O 4183 C CB . PRO A 514 ? 0.3881 0.3607 0.4042 0.0666 -0.0324 -0.0736 568 PRO A CB 4184 C CG . PRO A 514 ? 0.4045 0.3826 0.4302 0.0648 -0.0347 -0.0759 568 PRO A CG 4185 C CD . PRO A 514 ? 0.3870 0.3691 0.4144 0.0608 -0.0316 -0.0736 568 PRO A CD 4186 N N A MET A 515 ? 0.3978 0.3577 0.3963 0.0730 -0.0363 -0.0706 569 MET A N 4187 N N B MET A 515 ? 0.3980 0.3582 0.3969 0.0728 -0.0362 -0.0706 569 MET A N 4188 C CA A MET A 515 ? 0.4051 0.3562 0.3925 0.0785 -0.0387 -0.0698 569 MET A CA 4189 C CA B MET A 515 ? 0.4071 0.3588 0.3955 0.0783 -0.0390 -0.0701 569 MET A CA 4190 C C A MET A 515 ? 0.3952 0.3448 0.3769 0.0776 -0.0358 -0.0664 569 MET A C 4191 C C B MET A 515 ? 0.3964 0.3462 0.3784 0.0776 -0.0360 -0.0665 569 MET A C 4192 O O A MET A 515 ? 0.3804 0.3226 0.3521 0.0822 -0.0370 -0.0652 569 MET A O 4193 O O B MET A 515 ? 0.3901 0.3324 0.3621 0.0822 -0.0372 -0.0654 569 MET A O 4194 C CB A MET A 515 ? 0.4267 0.3753 0.4154 0.0825 -0.0458 -0.0737 569 MET A CB 4195 C CB B MET A 515 ? 0.4220 0.3728 0.4137 0.0812 -0.0458 -0.0740 569 MET A CB 4196 C CG A MET A 515 ? 0.4586 0.4069 0.4517 0.0849 -0.0499 -0.0775 569 MET A CG 4197 C CG B MET A 515 ? 0.4601 0.4133 0.4598 0.0819 -0.0495 -0.0780 569 MET A CG 4198 S SD A MET A 515 ? 0.5686 0.5115 0.5536 0.0878 -0.0474 -0.0760 569 MET A SD 4199 S SD B MET A 515 ? 0.5633 0.5111 0.5622 0.0880 -0.0584 -0.0824 569 MET A SD 4200 C CE A MET A 515 ? 0.5708 0.5017 0.5396 0.0953 -0.0495 -0.0744 569 MET A CE 4201 C CE B MET A 515 ? 0.5200 0.4769 0.5358 0.0836 -0.0609 -0.0855 569 MET A CE 4202 N N . PHE A 516 ? 0.3770 0.3331 0.3646 0.0721 -0.0321 -0.0649 570 PHE A N 4203 C CA . PHE A 516 ? 0.3587 0.3141 0.3419 0.0708 -0.0292 -0.0617 570 PHE A CA 4204 C C . PHE A 516 ? 0.3570 0.3097 0.3377 0.0734 -0.0334 -0.0628 570 PHE A C 4205 O O . PHE A 516 ? 0.3718 0.3215 0.3462 0.0742 -0.0319 -0.0604 570 PHE A O 4206 C CB . PHE A 516 ? 0.3641 0.3148 0.3389 0.0718 -0.0246 -0.0578 570 PHE A CB 4207 C CG . PHE A 516 ? 0.3776 0.3333 0.3576 0.0672 -0.0200 -0.0564 570 PHE A CG 4208 C CD1 . PHE A 516 ? 0.3934 0.3532 0.3759 0.0628 -0.0161 -0.0541 570 PHE A CD1 4209 C CD2 . PHE A 516 ? 0.4012 0.3577 0.3842 0.0673 -0.0201 -0.0579 570 PHE A CD2 4210 C CE1 . PHE A 516 ? 0.3802 0.3446 0.3677 0.0588 -0.0124 -0.0533 570 PHE A CE1 4211 C CE2 . PHE A 516 ? 0.3951 0.3563 0.3831 0.0632 -0.0164 -0.0571 570 PHE A CE2 4212 C CZ . PHE A 516 ? 0.3941 0.3591 0.3843 0.0590 -0.0127 -0.0549 570 PHE A CZ 4213 N N . LYS A 517 ? 0.3550 0.3091 0.3417 0.0745 -0.0386 -0.0667 571 LYS A N 4214 C CA . LYS A 517 ? 0.3730 0.3242 0.3581 0.0773 -0.0436 -0.0684 571 LYS A CA 4215 C C . LYS A 517 ? 0.3511 0.3082 0.3429 0.0727 -0.0424 -0.0677 571 LYS A C 4216 O O . LYS A 517 ? 0.3545 0.3088 0.3425 0.0745 -0.0444 -0.0674 571 LYS A O 4217 C CB . LYS A 517 ? 0.3777 0.3281 0.3678 0.0805 -0.0503 -0.0730 571 LYS A CB 4218 C CG . LYS A 517 ? 0.3843 0.3430 0.3884 0.0760 -0.0504 -0.0752 571 LYS A CG 4219 C CD . LYS A 517 ? 0.4631 0.4204 0.4727 0.0795 -0.0576 -0.0799 571 LYS A CD 4220 C CE . LYS A 517 ? 0.4738 0.4398 0.4985 0.0752 -0.0574 -0.0820 571 LYS A CE 4221 N NZ . LYS A 517 ? 0.5179 0.4832 0.5502 0.0782 -0.0648 -0.0868 571 LYS A NZ 4222 N N . TYR A 518 ? 0.3550 0.3201 0.3566 0.0672 -0.0393 -0.0675 572 TYR A N 4223 C CA . TYR A 518 ? 0.3508 0.3214 0.3581 0.0626 -0.0373 -0.0663 572 TYR A CA 4224 C C . TYR A 518 ? 0.3483 0.3170 0.3476 0.0615 -0.0327 -0.0623 572 TYR A C 4225 O O . TYR A 518 ? 0.3496 0.3182 0.3478 0.0610 -0.0331 -0.0614 572 TYR A O 4226 C CB . TYR A 518 ? 0.3290 0.3082 0.3481 0.0574 -0.0348 -0.0670 572 TYR A CB 4227 C CG . TYR A 518 ? 0.3745 0.3556 0.4025 0.0586 -0.0393 -0.0708 572 TYR A CG 4228 C CD1 . TYR A 518 ? 0.3810 0.3613 0.4135 0.0603 -0.0447 -0.0733 572 TYR A CD1 4229 C CD2 . TYR A 518 ? 0.3934 0.3766 0.4253 0.0584 -0.0386 -0.0722 572 TYR A CD2 4230 C CE1 . TYR A 518 ? 0.4335 0.4154 0.4750 0.0615 -0.0492 -0.0770 572 TYR A CE1 4231 C CE2 . TYR A 518 ? 0.4170 0.4017 0.4572 0.0597 -0.0429 -0.0758 572 TYR A CE2 4232 C CZ . TYR A 518 ? 0.4496 0.4339 0.4951 0.0611 -0.0481 -0.0781 572 TYR A CZ 4233 O OH . TYR A 518 ? 0.4710 0.4571 0.5261 0.0624 -0.0524 -0.0818 572 TYR A OH 4234 N N . HIS A 519 ? 0.3388 0.3063 0.3335 0.0612 -0.0285 -0.0600 573 HIS A N 4235 C CA . HIS A 519 ? 0.3463 0.3109 0.3332 0.0611 -0.0244 -0.0563 573 HIS A CA 4236 C C . HIS A 519 ? 0.3517 0.3089 0.3291 0.0661 -0.0268 -0.0556 573 HIS A C 4237 O O . HIS A 519 ? 0.3307 0.2873 0.3049 0.0654 -0.0253 -0.0535 573 HIS A O 4238 C CB . HIS A 519 ? 0.3421 0.3049 0.3254 0.0613 -0.0206 -0.0543 573 HIS A CB 4239 C CG . HIS A 519 ? 0.3508 0.3202 0.3414 0.0562 -0.0170 -0.0540 573 HIS A CG 4240 N ND1 . HIS A 519 ? 0.3533 0.3271 0.3513 0.0547 -0.0182 -0.0566 573 HIS A ND1 4241 C CD2 . HIS A 519 ? 0.3863 0.3583 0.3774 0.0527 -0.0124 -0.0514 573 HIS A CD2 4242 C CE1 . HIS A 519 ? 0.3851 0.3638 0.3874 0.0506 -0.0144 -0.0556 573 HIS A CE1 4243 N NE2 . HIS A 519 ? 0.3801 0.3576 0.3782 0.0494 -0.0111 -0.0526 573 HIS A NE2 4244 N N . LEU A 520 ? 0.3472 0.2985 0.3194 0.0715 -0.0306 -0.0573 574 LEU A N 4245 C CA . LEU A 520 ? 0.3413 0.2849 0.3034 0.0770 -0.0332 -0.0570 574 LEU A CA 4246 C C . LEU A 520 ? 0.3491 0.2939 0.3141 0.0768 -0.0371 -0.0587 574 LEU A C 4247 O O . LEU A 520 ? 0.3337 0.2753 0.2922 0.0783 -0.0364 -0.0568 574 LEU A O 4248 C CB . LEU A 520 ? 0.3592 0.2957 0.3149 0.0834 -0.0372 -0.0590 574 LEU A CB 4249 C CG . LEU A 520 ? 0.3811 0.3086 0.3247 0.0901 -0.0400 -0.0586 574 LEU A CG 4250 C CD1 . LEU A 520 ? 0.3639 0.2878 0.2986 0.0908 -0.0341 -0.0538 574 LEU A CD1 4251 C CD2 . LEU A 520 ? 0.3926 0.3129 0.3297 0.0967 -0.0443 -0.0609 574 LEU A CD2 4252 N N . THR A 521 ? 0.3458 0.2955 0.3210 0.0747 -0.0409 -0.0621 575 THR A N 4253 C CA . THR A 521 ? 0.3394 0.2908 0.3191 0.0741 -0.0446 -0.0637 575 THR A CA 4254 C C . THR A 521 ? 0.3217 0.2770 0.3025 0.0695 -0.0400 -0.0606 575 THR A C 4255 O O . THR A 521 ? 0.3270 0.2799 0.3041 0.0708 -0.0415 -0.0601 575 THR A O 4256 C CB . THR A 521 ? 0.3528 0.3096 0.3452 0.0719 -0.0483 -0.0674 575 THR A CB 4257 O OG1 . THR A 521 ? 0.3724 0.3241 0.3628 0.0772 -0.0539 -0.0707 575 THR A OG1 4258 C CG2 . THR A 521 ? 0.3377 0.2974 0.3370 0.0700 -0.0513 -0.0686 575 THR A CG2 4259 N N . VAL A 522 ? 0.3209 0.2819 0.3063 0.0645 -0.0346 -0.0586 576 VAL A N 4260 C CA . VAL A 522 ? 0.3140 0.2788 0.3004 0.0602 -0.0304 -0.0557 576 VAL A CA 4261 C C . VAL A 522 ? 0.3248 0.2838 0.3000 0.0628 -0.0277 -0.0524 576 VAL A C 4262 O O . VAL A 522 ? 0.3155 0.2747 0.2890 0.0618 -0.0268 -0.0508 576 VAL A O 4263 C CB . VAL A 522 ? 0.3210 0.2930 0.3150 0.0545 -0.0258 -0.0547 576 VAL A CB 4264 C CG1 . VAL A 522 ? 0.2972 0.2723 0.2909 0.0505 -0.0212 -0.0515 576 VAL A CG1 4265 C CG2 . VAL A 522 ? 0.3137 0.2916 0.3194 0.0520 -0.0283 -0.0577 576 VAL A CG2 4266 N N . ALA A 523 ? 0.3153 0.2692 0.2831 0.0662 -0.0262 -0.0512 577 ALA A N 4267 C CA . ALA A 523 ? 0.3257 0.2735 0.2829 0.0695 -0.0237 -0.0480 577 ALA A CA 4268 C C . ALA A 523 ? 0.3358 0.2781 0.2864 0.0742 -0.0279 -0.0490 577 ALA A C 4269 O O . ALA A 523 ? 0.3306 0.2707 0.2757 0.0750 -0.0260 -0.0466 577 ALA A O 4270 C CB . ALA A 523 ? 0.3280 0.2708 0.2788 0.0728 -0.0215 -0.0466 577 ALA A CB 4271 N N . GLN A 524 ? 0.3279 0.2677 0.2789 0.0777 -0.0340 -0.0527 578 GLN A N 4272 C CA . GLN A 524 ? 0.3445 0.2791 0.2900 0.0825 -0.0391 -0.0544 578 GLN A CA 4273 C C . GLN A 524 ? 0.3257 0.2647 0.2771 0.0788 -0.0401 -0.0547 578 GLN A C 4274 O O . GLN A 524 ? 0.3388 0.2736 0.2837 0.0817 -0.0414 -0.0541 578 GLN A O 4275 C CB . GLN A 524 ? 0.3456 0.2772 0.2923 0.0865 -0.0460 -0.0588 578 GLN A CB 4276 C CG . GLN A 524 ? 0.3860 0.3110 0.3237 0.0917 -0.0455 -0.0583 578 GLN A CG 4277 C CD . GLN A 524 ? 0.4374 0.3594 0.3764 0.0959 -0.0526 -0.0629 578 GLN A CD 4278 O OE1 . GLN A 524 ? 0.3987 0.3237 0.3461 0.0948 -0.0578 -0.0665 578 GLN A OE1 4279 N NE2 . GLN A 524 ? 0.4261 0.3417 0.3567 0.1010 -0.0527 -0.0628 578 GLN A NE2 4280 N N . VAL A 525 ? 0.3233 0.2703 0.2868 0.0729 -0.0396 -0.0557 579 VAL A N 4281 C CA . VAL A 525 ? 0.3157 0.2671 0.2855 0.0693 -0.0404 -0.0559 579 VAL A CA 4282 C C . VAL A 525 ? 0.3058 0.2580 0.2713 0.0669 -0.0346 -0.0517 579 VAL A C 4283 O O . VAL A 525 ? 0.3228 0.2726 0.2840 0.0682 -0.0355 -0.0509 579 VAL A O 4284 C CB . VAL A 525 ? 0.3104 0.2701 0.2941 0.0637 -0.0405 -0.0575 579 VAL A CB 4285 C CG1 . VAL A 525 ? 0.2879 0.2519 0.2776 0.0597 -0.0402 -0.0569 579 VAL A CG1 4286 C CG2 . VAL A 525 ? 0.3160 0.2749 0.3054 0.0662 -0.0468 -0.0619 579 VAL A CG2 4287 N N . ARG A 526 ? 0.3101 0.2654 0.2765 0.0637 -0.0290 -0.0493 580 ARG A N 4288 C CA . ARG A 526 ? 0.3003 0.2569 0.2641 0.0610 -0.0237 -0.0455 580 ARG A CA 4289 C C . ARG A 526 ? 0.3183 0.2675 0.2704 0.0661 -0.0229 -0.0434 580 ARG A C 4290 O O . ARG A 526 ? 0.3312 0.2793 0.2799 0.0663 -0.0218 -0.0417 580 ARG A O 4291 C CB . ARG A 526 ? 0.2709 0.2315 0.2380 0.0571 -0.0185 -0.0436 580 ARG A CB 4292 C CG . ARG A 526 ? 0.2730 0.2412 0.2509 0.0519 -0.0183 -0.0451 580 ARG A CG 4293 C CD . ARG A 526 ? 0.2841 0.2553 0.2642 0.0489 -0.0136 -0.0436 580 ARG A CD 4294 N NE . ARG A 526 ? 0.2680 0.2460 0.2576 0.0446 -0.0134 -0.0452 580 ARG A NE 4295 C CZ . ARG A 526 ? 0.2993 0.2811 0.2926 0.0417 -0.0103 -0.0448 580 ARG A CZ 4296 N NH1 . ARG A 526 ? 0.3078 0.2872 0.2970 0.0425 -0.0074 -0.0430 580 ARG A NH1 4297 N NH2 . ARG A 526 ? 0.2688 0.2564 0.2701 0.0382 -0.0101 -0.0461 580 ARG A NH2 4298 N N . GLY A 527 ? 0.3102 0.2538 0.2556 0.0707 -0.0229 -0.0433 581 GLY A N 4299 C CA . GLY A 527 ? 0.3261 0.2620 0.2597 0.0762 -0.0215 -0.0409 581 GLY A CA 4300 C C . GLY A 527 ? 0.3363 0.2673 0.2640 0.0809 -0.0264 -0.0425 581 GLY A C 4301 O O . GLY A 527 ? 0.3404 0.2677 0.2608 0.0832 -0.0245 -0.0401 581 GLY A O 4302 N N . GLY A 528 ? 0.3456 0.2764 0.2766 0.0823 -0.0328 -0.0466 582 GLY A N 4303 C CA . GLY A 528 ? 0.3428 0.2690 0.2694 0.0867 -0.0384 -0.0489 582 GLY A CA 4304 C C . GLY A 528 ? 0.3358 0.2658 0.2662 0.0831 -0.0379 -0.0480 582 GLY A C 4305 O O . GLY A 528 ? 0.3411 0.2664 0.2642 0.0869 -0.0396 -0.0478 582 GLY A O 4306 N N . MET A 529 ? 0.3402 0.2785 0.2816 0.0761 -0.0357 -0.0477 583 MET A N 4307 C CA . MET A 529 ? 0.3314 0.2734 0.2766 0.0724 -0.0349 -0.0468 583 MET A CA 4308 C C . MET A 529 ? 0.3261 0.2655 0.2631 0.0734 -0.0298 -0.0428 583 MET A C 4309 O O . MET A 529 ? 0.3165 0.2535 0.2492 0.0751 -0.0308 -0.0422 583 MET A O 4310 C CB . MET A 529 ? 0.3268 0.2778 0.2844 0.0650 -0.0327 -0.0468 583 MET A CB 4311 C CG . MET A 529 ? 0.3702 0.3244 0.3378 0.0638 -0.0381 -0.0507 583 MET A CG 4312 S SD . MET A 529 ? 0.3724 0.3367 0.3537 0.0558 -0.0349 -0.0504 583 MET A SD 4313 C CE . MET A 529 ? 0.3491 0.3155 0.3322 0.0530 -0.0345 -0.0490 583 MET A CE 4314 N N . VAL A 530 ? 0.3191 0.2589 0.2543 0.0723 -0.0243 -0.0400 584 VAL A N 4315 C CA . VAL A 530 ? 0.3340 0.2717 0.2629 0.0730 -0.0188 -0.0358 584 VAL A CA 4316 C C . VAL A 530 ? 0.3476 0.2764 0.2639 0.0806 -0.0202 -0.0352 584 VAL A C 4317 O O . VAL A 530 ? 0.3218 0.2485 0.2332 0.0819 -0.0185 -0.0332 584 VAL A O 4318 C CB . VAL A 530 ? 0.3381 0.2771 0.2679 0.0711 -0.0132 -0.0332 584 VAL A CB 4319 C CG1 . VAL A 530 ? 0.3348 0.2696 0.2569 0.0735 -0.0076 -0.0288 584 VAL A CG1 4320 C CG2 . VAL A 530 ? 0.3362 0.2838 0.2773 0.0637 -0.0112 -0.0334 584 VAL A CG2 4321 N N . PHE A 531 ? 0.3531 0.2763 0.2638 0.0859 -0.0234 -0.0370 585 PHE A N 4322 C CA . PHE A 531 ? 0.3556 0.2695 0.2533 0.0940 -0.0252 -0.0368 585 PHE A CA 4323 C C . PHE A 531 ? 0.3573 0.2696 0.2529 0.0959 -0.0299 -0.0387 585 PHE A C 4324 O O . PHE A 531 ? 0.3758 0.2836 0.2628 0.0994 -0.0280 -0.0364 585 PHE A O 4325 C CB . PHE A 531 ? 0.3674 0.2759 0.2603 0.0994 -0.0292 -0.0393 585 PHE A CB 4326 C CG . PHE A 531 ? 0.4032 0.3012 0.2810 0.1083 -0.0300 -0.0384 585 PHE A CG 4327 C CD1 . PHE A 531 ? 0.4298 0.3228 0.2995 0.1120 -0.0248 -0.0349 585 PHE A CD1 4328 C CD2 . PHE A 531 ? 0.4158 0.3091 0.2876 0.1132 -0.0356 -0.0408 585 PHE A CD2 4329 C CE1 . PHE A 531 ? 0.4796 0.3626 0.3345 0.1207 -0.0249 -0.0337 585 PHE A CE1 4330 C CE2 . PHE A 531 ? 0.4816 0.3648 0.3384 0.1220 -0.0363 -0.0400 585 PHE A CE2 4331 C CZ . PHE A 531 ? 0.4786 0.3567 0.3266 0.1258 -0.0306 -0.0362 585 PHE A CZ 4332 N N A GLU A 532 ? 0.3526 0.2684 0.2564 0.0936 -0.0359 -0.0427 586 GLU A N 4333 N N B GLU A 532 ? 0.3494 0.2653 0.2533 0.0935 -0.0358 -0.0426 586 GLU A N 4334 C CA A GLU A 532 ? 0.3644 0.2788 0.2675 0.0951 -0.0408 -0.0447 586 GLU A CA 4335 C CA B GLU A 532 ? 0.3528 0.2671 0.2557 0.0952 -0.0408 -0.0447 586 GLU A CA 4336 C C A GLU A 532 ? 0.3501 0.2682 0.2549 0.0911 -0.0365 -0.0417 586 GLU A C 4337 C C B GLU A 532 ? 0.3467 0.2653 0.2527 0.0908 -0.0372 -0.0422 586 GLU A C 4338 O O A GLU A 532 ? 0.3423 0.2561 0.2398 0.0948 -0.0372 -0.0410 586 GLU A O 4339 O O B GLU A 532 ? 0.3422 0.2574 0.2432 0.0937 -0.0396 -0.0425 586 GLU A O 4340 C CB A GLU A 532 ? 0.3724 0.2913 0.2870 0.0920 -0.0471 -0.0491 586 GLU A CB 4341 C CB B GLU A 532 ? 0.3578 0.2752 0.2705 0.0935 -0.0478 -0.0495 586 GLU A CB 4342 C CG A GLU A 532 ? 0.4172 0.3317 0.3304 0.0969 -0.0535 -0.0532 586 GLU A CG 4343 C CG B GLU A 532 ? 0.3483 0.2614 0.2581 0.0976 -0.0545 -0.0524 586 GLU A CG 4344 C CD A GLU A 532 ? 0.5207 0.4260 0.4230 0.1052 -0.0595 -0.0555 586 GLU A CD 4345 C CD B GLU A 532 ? 0.4053 0.3082 0.3022 0.1069 -0.0590 -0.0543 586 GLU A CD 4346 O OE1 A GLU A 532 ? 0.5758 0.4786 0.4720 0.1070 -0.0588 -0.0540 586 GLU A OE1 4347 O OE1 B GLU A 532 ? 0.3617 0.2606 0.2510 0.1104 -0.0562 -0.0528 586 GLU A OE1 4348 O OE2 A GLU A 532 ? 0.5800 0.4806 0.4797 0.1101 -0.0652 -0.0589 586 GLU A OE2 4349 O OE2 B GLU A 532 ? 0.4294 0.3282 0.3239 0.1109 -0.0656 -0.0573 586 GLU A OE2 4350 N N . LEU A 533 ? 0.3390 0.2649 0.2532 0.0839 -0.0320 -0.0400 587 LEU A N 4351 C CA . LEU A 533 ? 0.3375 0.2675 0.2547 0.0796 -0.0285 -0.0375 587 LEU A CA 4352 C C . LEU A 533 ? 0.3463 0.2714 0.2531 0.0833 -0.0235 -0.0336 587 LEU A C 4353 O O . LEU A 533 ? 0.3506 0.2750 0.2547 0.0836 -0.0226 -0.0322 587 LEU A O 4354 C CB . LEU A 533 ? 0.3393 0.2780 0.2676 0.0717 -0.0246 -0.0365 587 LEU A CB 4355 C CG . LEU A 533 ? 0.3158 0.2601 0.2553 0.0676 -0.0287 -0.0398 587 LEU A CG 4356 C CD1 . LEU A 533 ? 0.2696 0.2206 0.2172 0.0617 -0.0244 -0.0387 587 LEU A CD1 4357 C CD2 . LEU A 533 ? 0.3412 0.2883 0.2851 0.0649 -0.0308 -0.0403 587 LEU A CD2 4358 N N . ALA A 534 ? 0.3449 0.2663 0.2460 0.0864 -0.0202 -0.0318 588 ALA A N 4359 C CA . ALA A 534 ? 0.3530 0.2701 0.2457 0.0895 -0.0144 -0.0275 588 ALA A CA 4360 C C . ALA A 534 ? 0.3757 0.2834 0.2549 0.0983 -0.0165 -0.0275 588 ALA A C 4361 O O . ALA A 534 ? 0.3878 0.2918 0.2597 0.1012 -0.0119 -0.0239 588 ALA A O 4362 C CB . ALA A 534 ? 0.3366 0.2545 0.2304 0.0882 -0.0088 -0.0248 588 ALA A CB 4363 N N A ASN A 535 ? 0.3920 0.2956 0.2678 0.1026 -0.0233 -0.0315 589 ASN A N 4364 N N B ASN A 535 ? 0.3905 0.2943 0.2666 0.1024 -0.0234 -0.0316 589 ASN A N 4365 C CA A ASN A 535 ? 0.3978 0.2913 0.2592 0.1119 -0.0256 -0.0317 589 ASN A CA 4366 C CA B ASN A 535 ? 0.4016 0.2954 0.2638 0.1117 -0.0263 -0.0322 589 ASN A CA 4367 C C A ASN A 535 ? 0.4017 0.2920 0.2599 0.1154 -0.0329 -0.0354 589 ASN A C 4368 C C B ASN A 535 ? 0.4117 0.3024 0.2713 0.1152 -0.0342 -0.0363 589 ASN A C 4369 O O A ASN A 535 ? 0.4105 0.2932 0.2566 0.1224 -0.0335 -0.0346 589 ASN A O 4370 O O B ASN A 535 ? 0.4282 0.3102 0.2752 0.1232 -0.0364 -0.0366 589 ASN A O 4371 C CB A ASN A 535 ? 0.3974 0.2859 0.2537 0.1165 -0.0270 -0.0328 589 ASN A CB 4372 C CB B ASN A 535 ? 0.3983 0.2874 0.2556 0.1159 -0.0272 -0.0330 589 ASN A CB 4373 C CG A ASN A 535 ? 0.4273 0.3064 0.2686 0.1246 -0.0236 -0.0297 589 ASN A CG 4374 C CG B ASN A 535 ? 0.3930 0.2818 0.2483 0.1154 -0.0191 -0.0283 589 ASN A CG 4375 O OD1 A ASN A 535 ? 0.4281 0.3068 0.2665 0.1244 -0.0163 -0.0250 589 ASN A OD1 4376 O OD1 B ASN A 535 ? 0.3997 0.2829 0.2453 0.1201 -0.0145 -0.0247 589 ASN A OD1 4377 N ND2 A ASN A 535 ? 0.4510 0.3222 0.2827 0.1323 -0.0288 -0.0324 589 ASN A ND2 4378 N ND2 B ASN A 535 ? 0.3931 0.2878 0.2580 0.1097 -0.0172 -0.0283 589 ASN A ND2 4379 N N A SER A 536 ? 0.3923 0.2880 0.2614 0.1109 -0.0385 -0.0393 590 SER A N 4380 N N B SER A 536 ? 0.4052 0.3021 0.2761 0.1098 -0.0386 -0.0394 590 SER A N 4381 C CA A SER A 536 ? 0.3842 0.2772 0.2523 0.1138 -0.0463 -0.0432 590 SER A CA 4382 C CA B SER A 536 ? 0.4119 0.3058 0.2814 0.1130 -0.0464 -0.0434 590 SER A CA 4383 C C A SER A 536 ? 0.3901 0.2816 0.2531 0.1149 -0.0442 -0.0410 590 SER A C 4384 C C B SER A 536 ? 0.4049 0.2971 0.2691 0.1143 -0.0447 -0.0414 590 SER A C 4385 O O A SER A 536 ? 0.3826 0.2797 0.2503 0.1094 -0.0382 -0.0376 590 SER A O 4386 O O B SER A 536 ? 0.3934 0.2917 0.2637 0.1083 -0.0396 -0.0385 590 SER A O 4387 C CB A SER A 536 ? 0.3789 0.2794 0.2621 0.1074 -0.0512 -0.0469 590 SER A CB 4388 C CB B SER A 536 ? 0.4074 0.3087 0.2918 0.1066 -0.0512 -0.0469 590 SER A CB 4389 O OG A SER A 536 ? 0.3131 0.2111 0.1970 0.1099 -0.0589 -0.0508 590 SER A OG 4390 O OG B SER A 536 ? 0.4427 0.3447 0.3316 0.1065 -0.0541 -0.0495 590 SER A OG 4391 N N . ILE A 537 ? 0.4024 0.2863 0.2555 0.1221 -0.0492 -0.0430 591 ILE A N 4392 C CA . ILE A 537 ? 0.4072 0.2889 0.2542 0.1241 -0.0476 -0.0411 591 ILE A CA 4393 C C . ILE A 537 ? 0.3858 0.2753 0.2450 0.1166 -0.0487 -0.0419 591 ILE A C 4394 O O . ILE A 537 ? 0.3997 0.2929 0.2605 0.1130 -0.0430 -0.0384 591 ILE A O 4395 C CB . ILE A 537 ? 0.3938 0.2654 0.2280 0.1338 -0.0545 -0.0442 591 ILE A CB 4396 C CG1 . ILE A 537 ? 0.4758 0.3385 0.2958 0.1421 -0.0527 -0.0430 591 ILE A CG1 4397 C CG2 . ILE A 537 ? 0.4729 0.3425 0.3014 0.1357 -0.0529 -0.0424 591 ILE A CG2 4398 C CD1 . ILE A 537 ? 0.5095 0.3719 0.3240 0.1421 -0.0423 -0.0367 591 ILE A CD1 4399 N N . VAL A 538 ? 0.3949 0.2868 0.2627 0.1147 -0.0560 -0.0464 592 VAL A N 4400 C CA . VAL A 538 ? 0.3982 0.2980 0.2793 0.1070 -0.0571 -0.0472 592 VAL A CA 4401 C C . VAL A 538 ? 0.3908 0.2990 0.2843 0.0994 -0.0539 -0.0465 592 VAL A C 4402 O O . VAL A 538 ? 0.3829 0.2906 0.2787 0.1003 -0.0564 -0.0487 592 VAL A O 4403 C CB . VAL A 538 ? 0.4048 0.3028 0.2899 0.1088 -0.0666 -0.0522 592 VAL A CB 4404 C CG1 . VAL A 538 ? 0.4143 0.3207 0.3137 0.1006 -0.0668 -0.0524 592 VAL A CG1 4405 C CG2 . VAL A 538 ? 0.4294 0.3183 0.3011 0.1171 -0.0702 -0.0531 592 VAL A CG2 4406 N N . LEU A 539 ? 0.3770 0.2924 0.2780 0.0923 -0.0485 -0.0437 593 LEU A N 4407 C CA . LEU A 539 ? 0.3634 0.2866 0.2757 0.0853 -0.0454 -0.0431 593 LEU A CA 4408 C C . LEU A 539 ? 0.3503 0.2756 0.2720 0.0839 -0.0519 -0.0474 593 LEU A C 4409 O O . LEU A 539 ? 0.3676 0.2923 0.2929 0.0844 -0.0576 -0.0501 593 LEU A O 4410 C CB . LEU A 539 ? 0.3414 0.2720 0.2611 0.0780 -0.0403 -0.0403 593 LEU A CB 4411 C CG . LEU A 539 ? 0.3782 0.3080 0.2913 0.0783 -0.0330 -0.0359 593 LEU A CG 4412 C CD1 . LEU A 539 ? 0.3573 0.2937 0.2773 0.0717 -0.0291 -0.0335 593 LEU A CD1 4413 C CD2 . LEU A 539 ? 0.3891 0.3190 0.3012 0.0784 -0.0291 -0.0344 593 LEU A CD2 4414 N N . PRO A 540 ? 0.3486 0.2765 0.2753 0.0821 -0.0511 -0.0481 594 PRO A N 4415 C CA . PRO A 540 ? 0.3583 0.2877 0.2940 0.0815 -0.0575 -0.0524 594 PRO A CA 4416 C C . PRO A 540 ? 0.3540 0.2923 0.3046 0.0736 -0.0566 -0.0525 594 PRO A C 4417 O O . PRO A 540 ? 0.3385 0.2814 0.2975 0.0702 -0.0559 -0.0532 594 PRO A O 4418 C CB . PRO A 540 ? 0.3657 0.2938 0.2994 0.0834 -0.0565 -0.0528 594 PRO A CB 4419 C CG . PRO A 540 ? 0.3508 0.2814 0.2814 0.0806 -0.0480 -0.0483 594 PRO A CG 4420 C CD . PRO A 540 ? 0.3413 0.2696 0.2644 0.0819 -0.0452 -0.0454 594 PRO A CD 4421 N N . PHE A 541 ? 0.3392 0.2794 0.2923 0.0711 -0.0566 -0.0516 595 PHE A N 4422 C CA . PHE A 541 ? 0.3436 0.2914 0.3096 0.0642 -0.0557 -0.0514 595 PHE A CA 4423 C C . PHE A 541 ? 0.3450 0.2914 0.3166 0.0652 -0.0627 -0.0546 595 PHE A C 4424 O O . PHE A 541 ? 0.3589 0.2997 0.3228 0.0698 -0.0660 -0.0553 595 PHE A O 4425 C CB . PHE A 541 ? 0.3133 0.2641 0.2774 0.0605 -0.0498 -0.0476 595 PHE A CB 4426 C CG . PHE A 541 ? 0.3229 0.2760 0.2838 0.0584 -0.0427 -0.0443 595 PHE A CG 4427 C CD1 . PHE A 541 ? 0.3195 0.2743 0.2829 0.0577 -0.0412 -0.0447 595 PHE A CD1 4428 C CD2 . PHE A 541 ? 0.3189 0.2727 0.2752 0.0569 -0.0377 -0.0409 595 PHE A CD2 4429 C CE1 . PHE A 541 ? 0.3299 0.2871 0.2914 0.0554 -0.0348 -0.0418 595 PHE A CE1 4430 C CE2 . PHE A 541 ? 0.3333 0.2893 0.2878 0.0549 -0.0314 -0.0380 595 PHE A CE2 4431 C CZ . PHE A 541 ? 0.2969 0.2544 0.2538 0.0542 -0.0301 -0.0385 595 PHE A CZ 4432 N N . ASP A 542 ? 0.3265 0.2781 0.3117 0.0610 -0.0647 -0.0562 596 ASP A N 4433 C CA . ASP A 542 ? 0.3242 0.2751 0.3168 0.0613 -0.0712 -0.0590 596 ASP A CA 4434 C C . ASP A 542 ? 0.3108 0.2684 0.3134 0.0546 -0.0680 -0.0569 596 ASP A C 4435 O O . ASP A 542 ? 0.3026 0.2664 0.3161 0.0497 -0.0656 -0.0565 596 ASP A O 4436 C CB . ASP A 542 ? 0.3156 0.2661 0.3170 0.0628 -0.0773 -0.0631 596 ASP A CB 4437 C CG . ASP A 542 ? 0.3809 0.3292 0.3893 0.0644 -0.0852 -0.0666 596 ASP A CG 4438 O OD1 . ASP A 542 ? 0.3695 0.3182 0.3786 0.0628 -0.0851 -0.0654 596 ASP A OD1 4439 O OD2 . ASP A 542 ? 0.4088 0.3542 0.4215 0.0678 -0.0920 -0.0706 596 ASP A OD2 4440 N N . CYS A 543 ? 0.3070 0.2633 0.3053 0.0545 -0.0674 -0.0554 597 CYS A N 4441 C CA . CYS A 543 ? 0.3148 0.2770 0.3216 0.0484 -0.0643 -0.0532 597 CYS A CA 4442 C C . CYS A 543 ? 0.3059 0.2713 0.3276 0.0455 -0.0682 -0.0553 597 CYS A C 4443 O O . CYS A 543 ? 0.2802 0.2513 0.3105 0.0400 -0.0645 -0.0532 597 CYS A O 4444 C CB . CYS A 543 ? 0.3090 0.2686 0.3087 0.0493 -0.0639 -0.0516 597 CYS A CB 4445 S SG . CYS A 543 ? 0.3785 0.3301 0.3747 0.0559 -0.0736 -0.0558 597 CYS A SG 4446 N N . ARG A 544 ? 0.3126 0.2742 0.3378 0.0494 -0.0756 -0.0593 598 ARG A N 4447 C CA . ARG A 544 ? 0.3138 0.2785 0.3551 0.0468 -0.0797 -0.0614 598 ARG A CA 4448 C C . ARG A 544 ? 0.3068 0.2781 0.3588 0.0422 -0.0756 -0.0605 598 ARG A C 4449 O O . ARG A 544 ? 0.2920 0.2683 0.3577 0.0378 -0.0749 -0.0600 598 ARG A O 4450 C CB . ARG A 544 ? 0.3184 0.2772 0.3612 0.0524 -0.0890 -0.0663 598 ARG A CB 4451 C CG . ARG A 544 ? 0.3446 0.2970 0.3783 0.0568 -0.0936 -0.0674 598 ARG A CG 4452 C CD . ARG A 544 ? 0.3640 0.3093 0.3956 0.0638 -0.1031 -0.0725 598 ARG A CD 4453 N NE . ARG A 544 ? 0.3863 0.3282 0.4081 0.0681 -0.1027 -0.0734 598 ARG A NE 4454 C CZ . ARG A 544 ? 0.4658 0.4013 0.4842 0.0746 -0.1102 -0.0777 598 ARG A CZ 4455 N NH1 . ARG A 544 ? 0.4231 0.3551 0.4475 0.0772 -0.1187 -0.0817 598 ARG A NH1 4456 N NH2 . ARG A 544 ? 0.4029 0.3353 0.4123 0.0784 -0.1094 -0.0782 598 ARG A NH2 4457 N N . ASP A 545 ? 0.3008 0.2722 0.3464 0.0433 -0.0723 -0.0600 599 ASP A N 4458 C CA . ASP A 545 ? 0.2927 0.2703 0.3470 0.0391 -0.0679 -0.0589 599 ASP A CA 4459 C C . ASP A 545 ? 0.2792 0.2628 0.3364 0.0332 -0.0605 -0.0548 599 ASP A C 4460 O O . ASP A 545 ? 0.2668 0.2559 0.3352 0.0292 -0.0578 -0.0540 599 ASP A O 4461 C CB . ASP A 545 ? 0.2952 0.2713 0.3416 0.0417 -0.0662 -0.0592 599 ASP A CB 4462 C CG . ASP A 545 ? 0.3747 0.3470 0.4238 0.0462 -0.0732 -0.0636 599 ASP A CG 4463 O OD1 . ASP A 545 ? 0.4459 0.4209 0.5090 0.0446 -0.0764 -0.0656 599 ASP A OD1 4464 O OD2 . ASP A 545 ? 0.3957 0.3624 0.4333 0.0514 -0.0752 -0.0648 599 ASP A OD2 4465 N N . TYR A 546 ? 0.2689 0.2514 0.3165 0.0328 -0.0573 -0.0522 600 TYR A N 4466 C CA . TYR A 546 ? 0.2553 0.2429 0.3057 0.0276 -0.0511 -0.0486 600 TYR A CA 4467 C C . TYR A 546 ? 0.2555 0.2454 0.3177 0.0248 -0.0531 -0.0487 600 TYR A C 4468 O O . TYR A 546 ? 0.2470 0.2422 0.3174 0.0203 -0.0488 -0.0466 600 TYR A O 4469 C CB . TYR A 546 ? 0.2556 0.2412 0.2937 0.0280 -0.0478 -0.0461 600 TYR A CB 4470 C CG . TYR A 546 ? 0.2432 0.2328 0.2780 0.0249 -0.0406 -0.0431 600 TYR A CG 4471 C CD1 . TYR A 546 ? 0.2373 0.2326 0.2802 0.0201 -0.0364 -0.0413 600 TYR A CD1 4472 C CD2 . TYR A 546 ? 0.2720 0.2592 0.2957 0.0270 -0.0381 -0.0421 600 TYR A CD2 4473 C CE1 . TYR A 546 ? 0.2440 0.2426 0.2838 0.0176 -0.0304 -0.0389 600 TYR A CE1 4474 C CE2 . TYR A 546 ? 0.3074 0.2980 0.3286 0.0243 -0.0320 -0.0397 600 TYR A CE2 4475 C CZ . TYR A 546 ? 0.2459 0.2420 0.2749 0.0197 -0.0284 -0.0382 600 TYR A CZ 4476 O OH . TYR A 546 ? 0.2536 0.2524 0.2795 0.0175 -0.0231 -0.0362 600 TYR A OH 4477 N N . ALA A 547 ? 0.2676 0.2532 0.3305 0.0276 -0.0595 -0.0509 601 ALA A N 4478 C CA . ALA A 547 ? 0.2627 0.2501 0.3376 0.0249 -0.0616 -0.0509 601 ALA A CA 4479 C C . ALA A 547 ? 0.2616 0.2536 0.3522 0.0222 -0.0615 -0.0516 601 ALA A C 4480 O O . ALA A 547 ? 0.2596 0.2561 0.3602 0.0178 -0.0583 -0.0494 601 ALA A O 4481 C CB . ALA A 547 ? 0.2620 0.2435 0.3356 0.0291 -0.0696 -0.0540 601 ALA A CB 4482 N N . VAL A 548 ? 0.2702 0.2612 0.3630 0.0248 -0.0647 -0.0545 602 VAL A N 4483 C CA . VAL A 548 ? 0.2722 0.2673 0.3802 0.0227 -0.0650 -0.0555 602 VAL A CA 4484 C C . VAL A 548 ? 0.2671 0.2687 0.3784 0.0179 -0.0564 -0.0518 602 VAL A C 4485 O O . VAL A 548 ? 0.2625 0.2685 0.3864 0.0143 -0.0540 -0.0503 602 VAL A O 4486 C CB . VAL A 548 ? 0.2806 0.2728 0.3887 0.0270 -0.0702 -0.0596 602 VAL A CB 4487 C CG1 . VAL A 548 ? 0.3155 0.3128 0.4394 0.0246 -0.0695 -0.0603 602 VAL A CG1 4488 C CG2 . VAL A 548 ? 0.3110 0.2970 0.4186 0.0316 -0.0793 -0.0635 602 VAL A CG2 4489 N N . VAL A 549 ? 0.2559 0.2578 0.3555 0.0181 -0.0517 -0.0502 603 VAL A N 4490 C CA A VAL A 549 ? 0.2400 0.2476 0.3424 0.0142 -0.0442 -0.0472 603 VAL A CA 4491 C CA B VAL A 549 ? 0.2540 0.2612 0.3551 0.0145 -0.0443 -0.0473 603 VAL A CA 4492 C C . VAL A 549 ? 0.2430 0.2530 0.3456 0.0105 -0.0395 -0.0436 603 VAL A C 4493 O O . VAL A 549 ? 0.2437 0.2585 0.3536 0.0071 -0.0346 -0.0413 603 VAL A O 4494 C CB A VAL A 549 ? 0.2347 0.2424 0.3264 0.0152 -0.0404 -0.0467 603 VAL A CB 4495 C CB B VAL A 549 ? 0.2615 0.2671 0.3491 0.0164 -0.0418 -0.0470 603 VAL A CB 4496 C CG1 A VAL A 549 ? 0.2270 0.2326 0.3193 0.0187 -0.0446 -0.0501 603 VAL A CG1 4497 C CG1 B VAL A 549 ? 0.2596 0.2693 0.3449 0.0132 -0.0346 -0.0439 603 VAL A CG1 4498 C CG2 A VAL A 549 ? 0.1840 0.1883 0.2608 0.0165 -0.0391 -0.0453 603 VAL A CG2 4499 C CG2 B VAL A 549 ? 0.2505 0.2546 0.3394 0.0195 -0.0452 -0.0502 603 VAL A CG2 4500 N N . LEU A 550 ? 0.2433 0.2500 0.3383 0.0114 -0.0412 -0.0430 604 LEU A N 4501 C CA . LEU A 550 ? 0.2528 0.2616 0.3477 0.0080 -0.0369 -0.0396 604 LEU A CA 4502 C C . LEU A 550 ? 0.2540 0.2657 0.3642 0.0052 -0.0371 -0.0389 604 LEU A C 4503 O O . LEU A 550 ? 0.2485 0.2637 0.3624 0.0018 -0.0317 -0.0357 604 LEU A O 4504 C CB . LEU A 550 ? 0.2403 0.2449 0.3250 0.0096 -0.0389 -0.0393 604 LEU A CB 4505 C CG . LEU A 550 ? 0.2191 0.2216 0.2886 0.0114 -0.0365 -0.0385 604 LEU A CG 4506 C CD1 . LEU A 550 ? 0.2604 0.2581 0.3214 0.0140 -0.0399 -0.0390 604 LEU A CD1 4507 C CD2 . LEU A 550 ? 0.2072 0.2138 0.2734 0.0079 -0.0289 -0.0350 604 LEU A CD2 4508 N N . ARG A 551 ? 0.2628 0.2727 0.3821 0.0070 -0.0435 -0.0419 605 ARG A N 4509 C CA . ARG A 551 ? 0.2754 0.2880 0.4111 0.0044 -0.0440 -0.0414 605 ARG A CA 4510 C C . ARG A 551 ? 0.2581 0.2759 0.4031 0.0020 -0.0389 -0.0400 605 ARG A C 4511 O O . ARG A 551 ? 0.2696 0.2911 0.4233 -0.0012 -0.0344 -0.0370 605 ARG A O 4512 C CB . ARG A 551 ? 0.2807 0.2897 0.4246 0.0071 -0.0527 -0.0454 605 ARG A CB 4513 C CG . ARG A 551 ? 0.3114 0.3234 0.4748 0.0045 -0.0536 -0.0451 605 ARG A CG 4514 C CD . ARG A 551 ? 0.3497 0.3634 0.5157 0.0009 -0.0493 -0.0410 605 ARG A CD 4515 N NE . ARG A 551 ? 0.4242 0.4407 0.6097 -0.0014 -0.0497 -0.0405 605 ARG A NE 4516 C CZ . ARG A 551 ? 0.4781 0.4921 0.6738 -0.0006 -0.0564 -0.0428 605 ARG A CZ 4517 N NH1 . ARG A 551 ? 0.4391 0.4475 0.6264 0.0027 -0.0634 -0.0458 605 ARG A NH1 4518 N NH2 . ARG A 551 ? 0.4847 0.5017 0.6995 -0.0030 -0.0562 -0.0420 605 ARG A NH2 4519 N N . LYS A 552 ? 0.2637 0.2817 0.4069 0.0039 -0.0396 -0.0421 606 LYS A N 4520 C CA . LYS A 552 ? 0.2573 0.2802 0.4079 0.0020 -0.0346 -0.0409 606 LYS A CA 4521 C C . LYS A 552 ? 0.2455 0.2717 0.3903 -0.0008 -0.0262 -0.0366 606 LYS A C 4522 O O . LYS A 552 ? 0.2270 0.2575 0.3810 -0.0035 -0.0211 -0.0342 606 LYS A O 4523 C CB . LYS A 552 ? 0.2787 0.3005 0.4244 0.0049 -0.0368 -0.0439 606 LYS A CB 4524 C CG . LYS A 552 ? 0.3336 0.3601 0.4856 0.0036 -0.0322 -0.0432 606 LYS A CG 4525 C CD . LYS A 552 ? 0.4169 0.4415 0.5653 0.0069 -0.0358 -0.0468 606 LYS A CD 4526 C CE . LYS A 552 ? 0.4855 0.5089 0.6178 0.0079 -0.0324 -0.0459 606 LYS A CE 4527 N NZ . LYS A 552 ? 0.5167 0.5373 0.6435 0.0116 -0.0361 -0.0491 606 LYS A NZ 4528 N N . TYR A 553 ? 0.2253 0.2494 0.3548 -0.0001 -0.0246 -0.0357 607 TYR A N 4529 C CA . TYR A 553 ? 0.2221 0.2490 0.3455 -0.0024 -0.0171 -0.0321 607 TYR A CA 4530 C C . TYR A 553 ? 0.2087 0.2367 0.3361 -0.0051 -0.0143 -0.0289 607 TYR A C 4531 O O . TYR A 553 ? 0.2186 0.2497 0.3472 -0.0073 -0.0081 -0.0259 607 TYR A O 4532 C CB . TYR A 553 ? 0.2216 0.2458 0.3286 -0.0010 -0.0165 -0.0320 607 TYR A CB 4533 C CG . TYR A 553 ? 0.2322 0.2547 0.3332 0.0017 -0.0187 -0.0347 607 TYR A CG 4534 C CD1 . TYR A 553 ? 0.2335 0.2582 0.3418 0.0022 -0.0188 -0.0363 607 TYR A CD1 4535 C CD2 . TYR A 553 ? 0.2226 0.2414 0.3107 0.0039 -0.0202 -0.0354 607 TYR A CD2 4536 C CE1 . TYR A 553 ? 0.2663 0.2892 0.3691 0.0049 -0.0209 -0.0388 607 TYR A CE1 4537 C CE2 . TYR A 553 ? 0.2522 0.2691 0.3346 0.0067 -0.0220 -0.0376 607 TYR A CE2 4538 C CZ . TYR A 553 ? 0.2620 0.2808 0.3517 0.0072 -0.0225 -0.0393 607 TYR A CZ 4539 O OH . TYR A 553 ? 0.2518 0.2685 0.3355 0.0100 -0.0241 -0.0413 607 TYR A OH 4540 N N . ALA A 554 ? 0.2154 0.2405 0.3445 -0.0047 -0.0190 -0.0297 608 ALA A N 4541 C CA . ALA A 554 ? 0.2281 0.2539 0.3619 -0.0071 -0.0169 -0.0268 608 ALA A CA 4542 C C . ALA A 554 ? 0.2419 0.2713 0.3925 -0.0093 -0.0147 -0.0254 608 ALA A C 4543 O O . ALA A 554 ? 0.2585 0.2904 0.4124 -0.0117 -0.0088 -0.0217 608 ALA A O 4544 C CB . ALA A 554 ? 0.2494 0.2710 0.3818 -0.0059 -0.0230 -0.0283 608 ALA A CB 4545 N N . ASP A 555 ? 0.2541 0.2836 0.4156 -0.0081 -0.0193 -0.0284 609 ASP A N 4546 C CA . ASP A 555 ? 0.2687 0.3021 0.4476 -0.0100 -0.0170 -0.0273 609 ASP A CA 4547 C C . ASP A 555 ? 0.2615 0.2991 0.4393 -0.0115 -0.0086 -0.0243 609 ASP A C 4548 O O . ASP A 555 ? 0.2559 0.2966 0.4425 -0.0138 -0.0031 -0.0208 609 ASP A O 4549 C CB . ASP A 555 ? 0.2761 0.3089 0.4643 -0.0080 -0.0233 -0.0316 609 ASP A CB 4550 C CG . ASP A 555 ? 0.3158 0.3452 0.5115 -0.0068 -0.0313 -0.0343 609 ASP A CG 4551 O OD1 . ASP A 555 ? 0.3301 0.3581 0.5266 -0.0080 -0.0319 -0.0327 609 ASP A OD1 4552 O OD2 . ASP A 555 ? 0.4128 0.4408 0.6140 -0.0045 -0.0374 -0.0383 609 ASP A OD2 4553 N N . LYS A 556 ? 0.2444 0.2820 0.4114 -0.0100 -0.0077 -0.0256 610 LYS A N 4554 C CA . LYS A 556 ? 0.2487 0.2898 0.4139 -0.0108 -0.0007 -0.0234 610 LYS A CA 4555 C C . LYS A 556 ? 0.2452 0.2871 0.4029 -0.0125 0.0059 -0.0192 610 LYS A C 4556 O O . LYS A 556 ? 0.2433 0.2884 0.4064 -0.0139 0.0123 -0.0161 610 LYS A O 4557 C CB . LYS A 556 ? 0.2559 0.2962 0.4107 -0.0085 -0.0021 -0.0262 610 LYS A CB 4558 C CG . LYS A 556 ? 0.3266 0.3701 0.4783 -0.0089 0.0044 -0.0245 610 LYS A CG 4559 C CD . LYS A 556 ? 0.4423 0.4899 0.6092 -0.0097 0.0072 -0.0239 610 LYS A CD 4560 C CE . LYS A 556 ? 0.4970 0.5477 0.6597 -0.0103 0.0151 -0.0212 610 LYS A CE 4561 N NZ . LYS A 556 ? 0.5836 0.6384 0.7602 -0.0108 0.0186 -0.0204 610 LYS A NZ 4562 N N . ILE A 557 ? 0.2453 0.2841 0.3901 -0.0120 0.0046 -0.0190 611 ILE A N 4563 C CA . ILE A 557 ? 0.2442 0.2833 0.3812 -0.0133 0.0101 -0.0154 611 ILE A CA 4564 C C . ILE A 557 ? 0.2511 0.2911 0.3983 -0.0154 0.0128 -0.0120 611 ILE A C 4565 O O . ILE A 557 ? 0.2431 0.2851 0.3903 -0.0166 0.0195 -0.0084 611 ILE A O 4566 C CB . ILE A 557 ? 0.2496 0.2852 0.3709 -0.0123 0.0079 -0.0162 611 ILE A CB 4567 C CG1 . ILE A 557 ? 0.2793 0.3154 0.3911 -0.0131 0.0138 -0.0130 611 ILE A CG1 4568 C CG2 . ILE A 557 ? 0.2702 0.3024 0.3917 -0.0120 0.0021 -0.0173 611 ILE A CG2 4569 C CD1 . ILE A 557 ? 0.2675 0.3059 0.3749 -0.0125 0.0183 -0.0127 611 ILE A CD1 4570 N N . TYR A 558 ? 0.2316 0.2700 0.3875 -0.0157 0.0075 -0.0133 612 TYR A N 4571 C CA . TYR A 558 ? 0.2750 0.3144 0.4433 -0.0177 0.0094 -0.0104 612 TYR A CA 4572 C C . TYR A 558 ? 0.2664 0.3100 0.4473 -0.0188 0.0151 -0.0082 612 TYR A C 4573 O O . TYR A 558 ? 0.2883 0.3334 0.4730 -0.0203 0.0213 -0.0040 612 TYR A O 4574 C CB . TYR A 558 ? 0.2683 0.3053 0.4456 -0.0175 0.0016 -0.0132 612 TYR A CB 4575 C CG . TYR A 558 ? 0.3140 0.3522 0.5071 -0.0196 0.0030 -0.0106 612 TYR A CG 4576 C CD1 . TYR A 558 ? 0.3562 0.3930 0.5469 -0.0210 0.0054 -0.0073 612 TYR A CD1 4577 C CD2 . TYR A 558 ? 0.3850 0.4257 0.5959 -0.0201 0.0022 -0.0113 612 TYR A CD2 4578 C CE1 . TYR A 558 ? 0.4310 0.4686 0.6368 -0.0230 0.0068 -0.0046 612 TYR A CE1 4579 C CE2 . TYR A 558 ? 0.4382 0.4800 0.6653 -0.0222 0.0037 -0.0086 612 TYR A CE2 4580 C CZ . TYR A 558 ? 0.4470 0.4872 0.6710 -0.0236 0.0061 -0.0052 612 TYR A CZ 4581 O OH . TYR A 558 ? 0.5447 0.5856 0.7842 -0.0257 0.0079 -0.0023 612 TYR A OH 4582 N N . SER A 559 ? 0.2847 0.3301 0.4721 -0.0178 0.0132 -0.0109 613 SER A N 4583 C CA . SER A 559 ? 0.2869 0.3365 0.4872 -0.0187 0.0185 -0.0090 613 SER A CA 4584 C C . SER A 559 ? 0.2852 0.3367 0.4771 -0.0188 0.0272 -0.0054 613 SER A C 4585 O O . SER A 559 ? 0.2795 0.3336 0.4802 -0.0198 0.0335 -0.0018 613 SER A O 4586 C CB . SER A 559 ? 0.2861 0.3371 0.4938 -0.0173 0.0146 -0.0130 613 SER A CB 4587 O OG A SER A 559 ? 0.3256 0.3752 0.5451 -0.0172 0.0073 -0.0158 613 SER A OG 4588 O OG B SER A 559 ? 0.2934 0.3440 0.4873 -0.0156 0.0146 -0.0149 613 SER A OG 4589 N N . ILE A 560 ? 0.2769 0.3269 0.4518 -0.0175 0.0275 -0.0064 614 ILE A N 4590 C CA . ILE A 560 ? 0.2846 0.3356 0.4495 -0.0171 0.0348 -0.0035 614 ILE A CA 4591 C C . ILE A 560 ? 0.2987 0.3488 0.4614 -0.0183 0.0393 0.0008 614 ILE A C 4592 O O . ILE A 560 ? 0.2971 0.3490 0.4619 -0.0184 0.0466 0.0046 614 ILE A O 4593 C CB . ILE A 560 ? 0.2921 0.3414 0.4400 -0.0155 0.0330 -0.0058 614 ILE A CB 4594 C CG1 . ILE A 560 ? 0.3077 0.3581 0.4578 -0.0141 0.0298 -0.0096 614 ILE A CG1 4595 C CG2 . ILE A 560 ? 0.2954 0.3448 0.4313 -0.0149 0.0398 -0.0029 614 ILE A CG2 4596 C CD1 . ILE A 560 ? 0.3115 0.3597 0.4454 -0.0125 0.0277 -0.0120 614 ILE A CD1 4597 N N . SER A 561 ? 0.2795 0.3265 0.4380 -0.0188 0.0353 0.0005 615 SER A N 4598 C CA . SER A 561 ? 0.2816 0.3272 0.4372 -0.0198 0.0390 0.0045 615 SER A CA 4599 C C . SER A 561 ? 0.2942 0.3418 0.4661 -0.0213 0.0429 0.0079 615 SER A C 4600 O O . SER A 561 ? 0.2869 0.3346 0.4576 -0.0217 0.0497 0.0124 615 SER A O 4601 C CB . SER A 561 ? 0.2834 0.3255 0.4338 -0.0202 0.0330 0.0031 615 SER A CB 4602 O OG . SER A 561 ? 0.2912 0.3316 0.4362 -0.0209 0.0366 0.0067 615 SER A OG 4603 N N . MET A 562 ? 0.3001 0.3489 0.4872 -0.0221 0.0387 0.0058 616 MET A N 4604 C CA . MET A 562 ? 0.3296 0.3804 0.5354 -0.0237 0.0414 0.0087 616 MET A CA 4605 C C . MET A 562 ? 0.3434 0.3979 0.5565 -0.0236 0.0495 0.0119 616 MET A C 4606 O O . MET A 562 ? 0.3565 0.4129 0.5855 -0.0248 0.0530 0.0148 616 MET A O 4607 C CB . MET A 562 ? 0.3220 0.3726 0.5419 -0.0242 0.0335 0.0050 616 MET A CB 4608 C CG . MET A 562 ? 0.3659 0.4127 0.5827 -0.0248 0.0277 0.0041 616 MET A CG 4609 S SD . MET A 562 ? 0.4804 0.5264 0.7051 -0.0270 0.0327 0.0099 616 MET A SD 4610 C CE . MET A 562 ? 0.4040 0.4535 0.6553 -0.0285 0.0337 0.0109 616 MET A CE 4611 N N . LYS A 563 ? 0.3518 0.4072 0.5534 -0.0219 0.0527 0.0114 617 LYS A N 4612 C CA . LYS A 563 ? 0.3604 0.4184 0.5637 -0.0212 0.0617 0.0152 617 LYS A CA 4613 C C . LYS A 563 ? 0.3564 0.4127 0.5531 -0.0212 0.0688 0.0206 617 LYS A C 4614 O O . LYS A 563 ? 0.3477 0.4057 0.5473 -0.0205 0.0770 0.0246 617 LYS A O 4615 C CB . LYS A 563 ? 0.3790 0.4379 0.5707 -0.0192 0.0626 0.0129 617 LYS A CB 4616 C CG . LYS A 563 ? 0.4230 0.4848 0.6257 -0.0189 0.0593 0.0093 617 LYS A CG 4617 C CD . LYS A 563 ? 0.5059 0.5665 0.6964 -0.0175 0.0536 0.0043 617 LYS A CD 4618 C CE . LYS A 563 ? 0.5470 0.6066 0.7192 -0.0157 0.0574 0.0048 617 LYS A CE 4619 N NZ . LYS A 563 ? 0.5681 0.6240 0.7254 -0.0156 0.0559 0.0053 617 LYS A NZ 4620 N N . HIS A 564 ? 0.3185 0.3713 0.5070 -0.0218 0.0657 0.0208 618 HIS A N 4621 C CA . HIS A 564 ? 0.3181 0.3687 0.4986 -0.0216 0.0715 0.0255 618 HIS A CA 4622 C C . HIS A 564 ? 0.3054 0.3541 0.4942 -0.0236 0.0690 0.0272 618 HIS A C 4623 O O . HIS A 564 ? 0.2944 0.3398 0.4723 -0.0237 0.0667 0.0273 618 HIS A O 4624 C CB . HIS A 564 ? 0.3124 0.3601 0.4713 -0.0199 0.0707 0.0243 618 HIS A CB 4625 C CG . HIS A 564 ? 0.3357 0.3847 0.4858 -0.0180 0.0708 0.0214 618 HIS A CG 4626 N ND1 . HIS A 564 ? 0.3606 0.4106 0.5052 -0.0160 0.0779 0.0238 618 HIS A ND1 4627 C CD2 . HIS A 564 ? 0.3499 0.3991 0.4951 -0.0175 0.0646 0.0165 618 HIS A CD2 4628 C CE1 . HIS A 564 ? 0.3944 0.4453 0.5320 -0.0146 0.0759 0.0202 618 HIS A CE1 4629 N NE2 . HIS A 564 ? 0.3825 0.4330 0.5203 -0.0156 0.0680 0.0159 618 HIS A NE2 4630 N N . PRO A 565 ? 0.3119 0.3627 0.5208 -0.0253 0.0692 0.0284 619 PRO A N 4631 C CA . PRO A 565 ? 0.3112 0.3602 0.5296 -0.0273 0.0657 0.0292 619 PRO A CA 4632 C C . PRO A 565 ? 0.3184 0.3645 0.5292 -0.0274 0.0707 0.0341 619 PRO A C 4633 O O . PRO A 565 ? 0.2941 0.3373 0.5019 -0.0283 0.0660 0.0334 619 PRO A O 4634 C CB . PRO A 565 ? 0.3275 0.3797 0.5696 -0.0288 0.0673 0.0306 619 PRO A CB 4635 C CG . PRO A 565 ? 0.3296 0.3852 0.5733 -0.0275 0.0747 0.0324 619 PRO A CG 4636 C CD . PRO A 565 ? 0.3110 0.3659 0.5350 -0.0254 0.0725 0.0288 619 PRO A CD 4637 N N . GLN A 566 ? 0.3282 0.3749 0.5358 -0.0262 0.0801 0.0390 620 GLN A N 4638 C CA A GLN A 566 ? 0.3363 0.3798 0.5367 -0.0259 0.0854 0.0440 620 GLN A CA 4639 C CA B GLN A 566 ? 0.3330 0.3764 0.5338 -0.0260 0.0850 0.0439 620 GLN A CA 4640 C C . GLN A 566 ? 0.3332 0.3730 0.5132 -0.0249 0.0813 0.0419 620 GLN A C 4641 O O . GLN A 566 ? 0.3269 0.3636 0.5036 -0.0256 0.0797 0.0433 620 GLN A O 4642 C CB A GLN A 566 ? 0.3585 0.4029 0.5571 -0.0240 0.0963 0.0494 620 GLN A CB 4643 C CB B GLN A 566 ? 0.3548 0.3989 0.5554 -0.0244 0.0961 0.0499 620 GLN A CB 4644 C CG A GLN A 566 ? 0.3725 0.4208 0.5931 -0.0251 0.1010 0.0520 620 GLN A CG 4645 C CG B GLN A 566 ? 0.3595 0.4000 0.5556 -0.0242 0.1016 0.0556 620 GLN A CG 4646 C CD A GLN A 566 ? 0.4502 0.4986 0.6725 -0.0235 0.1127 0.0589 620 GLN A CD 4647 C CD B GLN A 566 ? 0.3659 0.4051 0.5751 -0.0270 0.0977 0.0565 620 GLN A CD 4648 O OE1 A GLN A 566 ? 0.4952 0.5419 0.7008 -0.0206 0.1181 0.0609 620 GLN A OE1 4649 O OE1 B GLN A 566 ? 0.4230 0.4644 0.6525 -0.0288 0.0993 0.0585 620 GLN A OE1 4650 N NE2 A GLN A 566 ? 0.4410 0.4916 0.6843 -0.0251 0.1167 0.0624 620 GLN A NE2 4651 N NE2 B GLN A 566 ? 0.3393 0.3749 0.5375 -0.0273 0.0924 0.0549 620 GLN A NE2 4652 N N . GLU A 567 ? 0.3109 0.3511 0.4776 -0.0231 0.0796 0.0384 621 GLU A N 4653 C CA . GLU A 567 ? 0.3104 0.3472 0.4583 -0.0220 0.0760 0.0364 621 GLU A CA 4654 C C . GLU A 567 ? 0.2936 0.3291 0.4430 -0.0236 0.0668 0.0324 621 GLU A C 4655 O O . GLU A 567 ? 0.2932 0.3255 0.4325 -0.0236 0.0643 0.0324 621 GLU A O 4656 C CB . GLU A 567 ? 0.3229 0.3604 0.4570 -0.0198 0.0762 0.0337 621 GLU A CB 4657 C CG . GLU A 567 ? 0.3925 0.4302 0.5201 -0.0174 0.0851 0.0374 621 GLU A CG 4658 C CD . GLU A 567 ? 0.4502 0.4915 0.5920 -0.0174 0.0908 0.0397 621 GLU A CD 4659 O OE1 . GLU A 567 ? 0.4531 0.4975 0.6088 -0.0189 0.0876 0.0373 621 GLU A OE1 4660 O OE2 . GLU A 567 ? 0.5542 0.5950 0.6932 -0.0156 0.0990 0.0442 621 GLU A OE2 4661 N N . MET A 568 ? 0.2826 0.3203 0.4445 -0.0248 0.0617 0.0291 622 MET A N 4662 C CA . MET A 568 ? 0.2844 0.3204 0.4474 -0.0258 0.0529 0.0253 622 MET A CA 4663 C C . MET A 568 ? 0.3024 0.3362 0.4727 -0.0274 0.0525 0.0281 622 MET A C 4664 O O . MET A 568 ? 0.2916 0.3226 0.4563 -0.0277 0.0471 0.0264 622 MET A O 4665 C CB . MET A 568 ? 0.2824 0.3206 0.4569 -0.0262 0.0471 0.0210 622 MET A CB 4666 C CG . MET A 568 ? 0.2717 0.3114 0.4375 -0.0245 0.0460 0.0174 622 MET A CG 4667 S SD . MET A 568 ? 0.3081 0.3497 0.4873 -0.0247 0.0387 0.0123 622 MET A SD 4668 C CE . MET A 568 ? 0.2862 0.3240 0.4625 -0.0248 0.0291 0.0087 622 MET A CE 4669 N N . LYS A 569 ? 0.2860 0.3212 0.4694 -0.0284 0.0584 0.0325 623 LYS A N 4670 C CA . LYS A 569 ? 0.3061 0.3389 0.4964 -0.0300 0.0587 0.0358 623 LYS A CA 4671 C C . LYS A 569 ? 0.3060 0.3354 0.4799 -0.0290 0.0620 0.0387 623 LYS A C 4672 O O . LYS A 569 ? 0.3061 0.3325 0.4763 -0.0296 0.0578 0.0382 623 LYS A O 4673 C CB . LYS A 569 ? 0.3003 0.3353 0.5089 -0.0312 0.0651 0.0403 623 LYS A CB 4674 C CG . LYS A 569 ? 0.2962 0.3343 0.5242 -0.0325 0.0609 0.0376 623 LYS A CG 4675 C CD . LYS A 569 ? 0.3772 0.4179 0.6234 -0.0335 0.0685 0.0425 623 LYS A CD 4676 C CE . LYS A 569 ? 0.4056 0.4492 0.6723 -0.0348 0.0635 0.0394 623 LYS A CE 4677 N NZ . LYS A 569 ? 0.4490 0.4968 0.7263 -0.0345 0.0688 0.0404 623 LYS A NZ 4678 N N . THR A 570 ? 0.3196 0.3491 0.4830 -0.0272 0.0690 0.0414 624 THR A N 4679 C CA . THR A 570 ? 0.3467 0.3728 0.4946 -0.0257 0.0728 0.0444 624 THR A CA 4680 C C . THR A 570 ? 0.3318 0.3553 0.4643 -0.0251 0.0665 0.0407 624 THR A C 4681 O O . THR A 570 ? 0.3212 0.3414 0.4467 -0.0250 0.0660 0.0423 624 THR A O 4682 C CB . THR A 570 ? 0.3681 0.3947 0.5071 -0.0232 0.0812 0.0474 624 THR A CB 4683 O OG1 . THR A 570 ? 0.4214 0.4501 0.5751 -0.0237 0.0880 0.0518 624 THR A OG1 4684 C CG2 . THR A 570 ? 0.4109 0.4333 0.5332 -0.0213 0.0848 0.0504 624 THR A CG2 4685 N N . TYR A 571 ? 0.3164 0.3414 0.4436 -0.0244 0.0619 0.0358 625 TYR A N 4686 C CA . TYR A 571 ? 0.3249 0.3478 0.4379 -0.0236 0.0564 0.0322 625 TYR A CA 4687 C C . TYR A 571 ? 0.3186 0.3413 0.4374 -0.0249 0.0479 0.0281 625 TYR A C 4688 O O . TYR A 571 ? 0.3218 0.3431 0.4302 -0.0242 0.0430 0.0248 625 TYR A O 4689 C CB . TYR A 571 ? 0.3211 0.3452 0.4226 -0.0216 0.0572 0.0298 625 TYR A CB 4690 C CG . TYR A 571 ? 0.3436 0.3673 0.4380 -0.0198 0.0652 0.0337 625 TYR A CG 4691 C CD1 . TYR A 571 ? 0.3953 0.4155 0.4782 -0.0186 0.0678 0.0364 625 TYR A CD1 4692 C CD2 . TYR A 571 ? 0.3762 0.4027 0.4756 -0.0190 0.0703 0.0347 625 TYR A CD2 4693 C CE1 . TYR A 571 ? 0.4205 0.4397 0.4962 -0.0163 0.0752 0.0401 625 TYR A CE1 4694 C CE2 . TYR A 571 ? 0.4210 0.4467 0.5134 -0.0168 0.0778 0.0384 625 TYR A CE2 4695 C CZ . TYR A 571 ? 0.4509 0.4727 0.5310 -0.0153 0.0802 0.0410 625 TYR A CZ 4696 O OH . TYR A 571 ? 0.5095 0.5300 0.5820 -0.0126 0.0876 0.0446 625 TYR A OH 4697 N N . SER A 572 ? 0.3085 0.3323 0.4438 -0.0266 0.0461 0.0284 626 SER A N 4698 C CA . SER A 572 ? 0.2941 0.3169 0.4350 -0.0275 0.0378 0.0246 626 SER A CA 4699 C C . SER A 572 ? 0.2826 0.3062 0.4171 -0.0263 0.0325 0.0194 626 SER A C 4700 O O . SER A 572 ? 0.2774 0.2989 0.4038 -0.0256 0.0269 0.0164 626 SER A O 4701 C CB A SER A 572 ? 0.2996 0.3188 0.4345 -0.0278 0.0350 0.0253 626 SER A CB 4702 C CB B SER A 572 ? 0.3040 0.3232 0.4382 -0.0278 0.0352 0.0253 626 SER A CB 4703 O OG A SER A 572 ? 0.2651 0.2834 0.4080 -0.0291 0.0394 0.0301 626 SER A OG 4704 O OG B SER A 572 ? 0.3312 0.3493 0.4710 -0.0283 0.0274 0.0218 626 SER A OG 4705 N N . VAL A 573 ? 0.2684 0.2951 0.4070 -0.0258 0.0346 0.0185 627 VAL A N 4706 C CA . VAL A 573 ? 0.2603 0.2877 0.3928 -0.0245 0.0303 0.0139 627 VAL A CA 4707 C C . VAL A 573 ? 0.2701 0.2978 0.4142 -0.0248 0.0235 0.0103 627 VAL A C 4708 O O . VAL A 573 ? 0.2921 0.3221 0.4502 -0.0255 0.0244 0.0105 627 VAL A O 4709 C CB . VAL A 573 ? 0.2719 0.3024 0.4032 -0.0236 0.0356 0.0144 627 VAL A CB 4710 C CG1 . VAL A 573 ? 0.2230 0.2540 0.3468 -0.0221 0.0315 0.0097 627 VAL A CG1 4711 C CG2 . VAL A 573 ? 0.2457 0.2754 0.3662 -0.0229 0.0424 0.0181 627 VAL A CG2 4712 N N . SER A 574 ? 0.2783 0.3034 0.4171 -0.0241 0.0168 0.0072 628 SER A N 4713 C CA . SER A 574 ? 0.2884 0.3128 0.4369 -0.0238 0.0097 0.0035 628 SER A CA 4714 C C . SER A 574 ? 0.2792 0.3033 0.4195 -0.0217 0.0054 -0.0008 628 SER A C 4715 O O . SER A 574 ? 0.2887 0.3113 0.4148 -0.0206 0.0051 -0.0015 628 SER A O 4716 C CB . SER A 574 ? 0.3090 0.3301 0.4587 -0.0241 0.0047 0.0030 628 SER A CB 4717 O OG . SER A 574 ? 0.3363 0.3566 0.4956 -0.0234 -0.0023 -0.0006 628 SER A OG 4718 N N . PHE A 575 ? 0.2759 0.3012 0.4256 -0.0211 0.0021 -0.0036 629 PHE A N 4719 C CA . PHE A 575 ? 0.2716 0.2958 0.4141 -0.0188 -0.0028 -0.0079 629 PHE A CA 4720 C C . PHE A 575 ? 0.2718 0.2925 0.4158 -0.0174 -0.0109 -0.0112 629 PHE A C 4721 O O . PHE A 575 ? 0.2559 0.2751 0.3959 -0.0151 -0.0157 -0.0149 629 PHE A O 4722 C CB . PHE A 575 ? 0.2555 0.2826 0.4052 -0.0184 -0.0019 -0.0094 629 PHE A CB 4723 C CG . PHE A 575 ? 0.2541 0.2838 0.3971 -0.0186 0.0049 -0.0073 629 PHE A CG 4724 C CD1 . PHE A 575 ? 0.2639 0.2935 0.3958 -0.0169 0.0044 -0.0095 629 PHE A CD1 4725 C CD2 . PHE A 575 ? 0.2832 0.3154 0.4313 -0.0204 0.0119 -0.0031 629 PHE A CD2 4726 C CE1 . PHE A 575 ? 0.2309 0.2629 0.3571 -0.0170 0.0104 -0.0078 629 PHE A CE1 4727 C CE2 . PHE A 575 ? 0.2766 0.3110 0.4182 -0.0201 0.0182 -0.0013 629 PHE A CE2 4728 C CZ . PHE A 575 ? 0.2942 0.3284 0.4245 -0.0184 0.0171 -0.0040 629 PHE A CZ 4729 N N . ASP A 576 ? 0.2775 0.2964 0.4265 -0.0185 -0.0125 -0.0098 630 ASP A N 4730 C CA . ASP A 576 ? 0.2770 0.2924 0.4288 -0.0170 -0.0205 -0.0131 630 ASP A CA 4731 C C . ASP A 576 ? 0.2716 0.2838 0.4079 -0.0142 -0.0244 -0.0159 630 ASP A C 4732 O O . ASP A 576 ? 0.2622 0.2718 0.3988 -0.0117 -0.0310 -0.0198 630 ASP A O 4733 C CB . ASP A 576 ? 0.2910 0.3048 0.4493 -0.0186 -0.0215 -0.0111 630 ASP A CB 4734 C CG . ASP A 576 ? 0.3363 0.3524 0.5138 -0.0208 -0.0200 -0.0093 630 ASP A CG 4735 O OD1 . ASP A 576 ? 0.3440 0.3628 0.5307 -0.0210 -0.0190 -0.0101 630 ASP A OD1 4736 O OD2 . ASP A 576 ? 0.3945 0.4095 0.5781 -0.0224 -0.0197 -0.0069 630 ASP A OD2 4737 N N . SER A 577 ? 0.2497 0.2618 0.3729 -0.0144 -0.0204 -0.0139 631 SER A N 4738 C CA . SER A 577 ? 0.2567 0.2659 0.3660 -0.0119 -0.0234 -0.0161 631 SER A CA 4739 C C . SER A 577 ? 0.2400 0.2494 0.3455 -0.0097 -0.0249 -0.0190 631 SER A C 4740 O O . SER A 577 ? 0.2295 0.2356 0.3289 -0.0067 -0.0300 -0.0220 631 SER A O 4741 C CB . SER A 577 ? 0.2652 0.2744 0.3621 -0.0127 -0.0187 -0.0134 631 SER A CB 4742 O OG . SER A 577 ? 0.2814 0.2939 0.3762 -0.0139 -0.0125 -0.0115 631 SER A OG 4743 N N . LEU A 578 ? 0.2303 0.2432 0.3388 -0.0108 -0.0205 -0.0180 632 LEU A N 4744 C CA . LEU A 578 ? 0.2355 0.2487 0.3405 -0.0087 -0.0216 -0.0206 632 LEU A CA 4745 C C . LEU A 578 ? 0.2447 0.2563 0.3585 -0.0067 -0.0282 -0.0243 632 LEU A C 4746 O O . LEU A 578 ? 0.2268 0.2356 0.3340 -0.0036 -0.0325 -0.0273 632 LEU A O 4747 C CB . LEU A 578 ? 0.2265 0.2437 0.3328 -0.0103 -0.0153 -0.0188 632 LEU A CB 4748 C CG . LEU A 578 ? 0.2359 0.2537 0.3394 -0.0084 -0.0161 -0.0213 632 LEU A CG 4749 C CD1 . LEU A 578 ? 0.2292 0.2442 0.3180 -0.0061 -0.0174 -0.0225 632 LEU A CD1 4750 C CD2 . LEU A 578 ? 0.2173 0.2393 0.3232 -0.0099 -0.0099 -0.0194 632 LEU A CD2 4751 N N . PHE A 579 ? 0.2368 0.2498 0.3655 -0.0083 -0.0293 -0.0240 633 PHE A N 4752 C CA . PHE A 579 ? 0.2503 0.2613 0.3879 -0.0063 -0.0364 -0.0278 633 PHE A CA 4753 C C . PHE A 579 ? 0.2589 0.2647 0.3906 -0.0034 -0.0433 -0.0304 633 PHE A C 4754 O O . PHE A 579 ? 0.2611 0.2640 0.3915 -0.0001 -0.0493 -0.0342 633 PHE A O 4755 C CB . PHE A 579 ? 0.2451 0.2587 0.4016 -0.0086 -0.0363 -0.0269 633 PHE A CB 4756 C CG . PHE A 579 ? 0.2566 0.2748 0.4200 -0.0103 -0.0308 -0.0255 633 PHE A CG 4757 C CD1 . PHE A 579 ? 0.2745 0.2933 0.4404 -0.0083 -0.0334 -0.0286 633 PHE A CD1 4758 C CD2 . PHE A 579 ? 0.2762 0.2980 0.4426 -0.0134 -0.0230 -0.0210 633 PHE A CD2 4759 C CE1 . PHE A 579 ? 0.3100 0.3331 0.4816 -0.0097 -0.0283 -0.0274 633 PHE A CE1 4760 C CE2 . PHE A 579 ? 0.3088 0.3348 0.4811 -0.0145 -0.0177 -0.0196 633 PHE A CE2 4761 C CZ . PHE A 579 ? 0.3018 0.3285 0.4768 -0.0127 -0.0204 -0.0229 633 PHE A CZ 4762 N N . SER A 580 ? 0.2571 0.2616 0.3849 -0.0045 -0.0425 -0.0283 634 SER A N 4763 C CA . SER A 580 ? 0.2753 0.2748 0.3961 -0.0017 -0.0485 -0.0305 634 SER A CA 4764 C C . SER A 580 ? 0.2681 0.2650 0.3735 0.0017 -0.0495 -0.0324 634 SER A C 4765 O O . SER A 580 ? 0.2701 0.2628 0.3718 0.0056 -0.0558 -0.0358 634 SER A O 4766 C CB . SER A 580 ? 0.2779 0.2769 0.3960 -0.0037 -0.0464 -0.0275 634 SER A CB 4767 O OG . SER A 580 ? 0.2940 0.2881 0.4046 -0.0007 -0.0520 -0.0297 634 SER A OG 4768 N N . ALA A 581 ? 0.2523 0.2514 0.3487 0.0006 -0.0434 -0.0301 635 ALA A N 4769 C CA . ALA A 581 ? 0.2562 0.2531 0.3387 0.0037 -0.0436 -0.0313 635 ALA A CA 4770 C C . ALA A 581 ? 0.2503 0.2461 0.3344 0.0065 -0.0471 -0.0346 635 ALA A C 4771 O O . ALA A 581 ? 0.2771 0.2687 0.3525 0.0106 -0.0510 -0.0371 635 ALA A O 4772 C CB . ALA A 581 ? 0.2383 0.2383 0.3130 0.0016 -0.0362 -0.0283 635 ALA A CB 4773 N N . VAL A 582 ? 0.2601 0.2595 0.3551 0.0047 -0.0456 -0.0346 636 VAL A N 4774 C CA . VAL A 582 ? 0.2504 0.2492 0.3479 0.0072 -0.0487 -0.0378 636 VAL A CA 4775 C C . VAL A 582 ? 0.2634 0.2577 0.3650 0.0106 -0.0572 -0.0416 636 VAL A C 4776 O O . VAL A 582 ? 0.2650 0.2557 0.3606 0.0147 -0.0615 -0.0446 636 VAL A O 4777 C CB . VAL A 582 ? 0.2536 0.2574 0.3623 0.0044 -0.0451 -0.0368 636 VAL A CB 4778 C CG1 . VAL A 582 ? 0.2465 0.2495 0.3608 0.0069 -0.0495 -0.0405 636 VAL A CG1 4779 C CG2 . VAL A 582 ? 0.2455 0.2528 0.3470 0.0023 -0.0373 -0.0337 636 VAL A CG2 4780 N N . LYS A 583 ? 0.2628 0.2570 0.3742 0.0090 -0.0597 -0.0414 637 LYS A N 4781 C CA . LYS A 583 ? 0.2834 0.2730 0.3995 0.0123 -0.0685 -0.0452 637 LYS A CA 4782 C C . LYS A 583 ? 0.2821 0.2660 0.3830 0.0167 -0.0721 -0.0468 637 LYS A C 4783 O O . LYS A 583 ? 0.2893 0.2685 0.3868 0.0215 -0.0786 -0.0506 637 LYS A O 4784 C CB . LYS A 583 ? 0.2874 0.2782 0.4170 0.0093 -0.0696 -0.0440 637 LYS A CB 4785 C CG . LYS A 583 ? 0.3439 0.3296 0.4788 0.0126 -0.0792 -0.0481 637 LYS A CG 4786 C CD . LYS A 583 ? 0.4286 0.4159 0.5780 0.0090 -0.0796 -0.0464 637 LYS A CD 4787 C CE . LYS A 583 ? 0.4864 0.4687 0.6428 0.0121 -0.0894 -0.0505 637 LYS A CE 4788 N NZ . LYS A 583 ? 0.5333 0.5101 0.6737 0.0160 -0.0929 -0.0519 637 LYS A NZ 4789 N N . ASN A 584 ? 0.2654 0.2493 0.3570 0.0155 -0.0680 -0.0439 638 ASN A N 4790 C CA . ASN A 584 ? 0.2860 0.2649 0.3631 0.0195 -0.0703 -0.0449 638 ASN A CA 4791 C C . ASN A 584 ? 0.2820 0.2590 0.3477 0.0232 -0.0697 -0.0461 638 ASN A C 4792 O O . ASN A 584 ? 0.2823 0.2537 0.3399 0.0284 -0.0747 -0.0488 638 ASN A O 4793 C CB . ASN A 584 ? 0.2715 0.2515 0.3415 0.0171 -0.0652 -0.0412 638 ASN A CB 4794 C CG . ASN A 584 ? 0.3279 0.3084 0.4065 0.0146 -0.0667 -0.0402 638 ASN A CG 4795 O OD1 . ASN A 584 ? 0.2943 0.2735 0.3839 0.0151 -0.0723 -0.0425 638 ASN A OD1 4796 N ND2 . ASN A 584 ? 0.3105 0.2926 0.3849 0.0119 -0.0620 -0.0369 638 ASN A ND2 4797 N N . PHE A 585 ? 0.2739 0.2550 0.3393 0.0208 -0.0638 -0.0442 639 PHE A N 4798 C CA . PHE A 585 ? 0.2651 0.2448 0.3210 0.0238 -0.0627 -0.0450 639 PHE A CA 4799 C C . PHE A 585 ? 0.2806 0.2566 0.3398 0.0280 -0.0697 -0.0493 639 PHE A C 4800 O O . PHE A 585 ? 0.2868 0.2579 0.3354 0.0330 -0.0725 -0.0512 639 PHE A O 4801 C CB . PHE A 585 ? 0.2510 0.2361 0.3087 0.0202 -0.0558 -0.0426 639 PHE A CB 4802 C CG . PHE A 585 ? 0.2691 0.2528 0.3164 0.0229 -0.0538 -0.0429 639 PHE A CG 4803 C CD1 . PHE A 585 ? 0.2747 0.2590 0.3118 0.0222 -0.0484 -0.0402 639 PHE A CD1 4804 C CD2 . PHE A 585 ? 0.2700 0.2515 0.3177 0.0262 -0.0575 -0.0459 639 PHE A CD2 4805 C CE1 . PHE A 585 ? 0.2820 0.2648 0.3100 0.0246 -0.0464 -0.0402 639 PHE A CE1 4806 C CE2 . PHE A 585 ? 0.2523 0.2323 0.2903 0.0287 -0.0553 -0.0459 639 PHE A CE2 4807 C CZ . PHE A 585 ? 0.2767 0.2573 0.3049 0.0279 -0.0497 -0.0430 639 PHE A CZ 4808 N N . THR A 586 ? 0.2833 0.2616 0.3572 0.0261 -0.0724 -0.0508 640 THR A N 4809 C CA . THR A 586 ? 0.2963 0.2716 0.3755 0.0298 -0.0796 -0.0551 640 THR A CA 4810 C C . THR A 586 ? 0.3160 0.2841 0.3884 0.0353 -0.0872 -0.0583 640 THR A C 4811 O O . THR A 586 ? 0.3072 0.2703 0.3719 0.0407 -0.0916 -0.0612 640 THR A O 4812 C CB . THR A 586 ? 0.3012 0.2807 0.3992 0.0263 -0.0808 -0.0557 640 THR A CB 4813 O OG1 . THR A 586 ? 0.3080 0.2938 0.4103 0.0218 -0.0731 -0.0526 640 THR A OG1 4814 C CG2 . THR A 586 ? 0.2871 0.2637 0.3918 0.0302 -0.0885 -0.0606 640 THR A CG2 4815 N N . GLU A 587 ? 0.3198 0.2871 0.3943 0.0341 -0.0886 -0.0575 641 GLU A N 4816 C CA . GLU A 587 ? 0.3528 0.3133 0.4218 0.0393 -0.0962 -0.0606 641 GLU A CA 4817 C C . GLU A 587 ? 0.3416 0.2975 0.3917 0.0439 -0.0948 -0.0601 641 GLU A C 4818 O O . GLU A 587 ? 0.3310 0.2806 0.3731 0.0501 -0.1006 -0.0634 641 GLU A O 4819 C CB . GLU A 587 ? 0.3552 0.3165 0.4312 0.0364 -0.0971 -0.0594 641 GLU A CB 4820 C CG . GLU A 587 ? 0.4465 0.4118 0.5421 0.0324 -0.0987 -0.0599 641 GLU A CG 4821 C CD . GLU A 587 ? 0.5264 0.4920 0.6305 0.0298 -0.1004 -0.0589 641 GLU A CD 4822 O OE1 . GLU A 587 ? 0.5819 0.5502 0.7030 0.0268 -0.1022 -0.0594 641 GLU A OE1 4823 O OE2 . GLU A 587 ? 0.5677 0.5308 0.6619 0.0306 -0.0997 -0.0576 641 GLU A OE2 4824 N N . ILE A 588 ? 0.3208 0.2796 0.3635 0.0410 -0.0871 -0.0560 642 ILE A N 4825 C CA . ILE A 588 ? 0.3203 0.2753 0.3463 0.0449 -0.0849 -0.0550 642 ILE A CA 4826 C C . ILE A 588 ? 0.3177 0.2705 0.3366 0.0488 -0.0848 -0.0563 642 ILE A C 4827 O O . ILE A 588 ? 0.3245 0.2712 0.3312 0.0547 -0.0873 -0.0577 642 ILE A O 4828 C CB . ILE A 588 ? 0.3003 0.2594 0.3216 0.0406 -0.0766 -0.0503 642 ILE A CB 4829 C CG1 . ILE A 588 ? 0.3104 0.2701 0.3365 0.0381 -0.0777 -0.0493 642 ILE A CG1 4830 C CG2 . ILE A 588 ? 0.3287 0.2843 0.3340 0.0445 -0.0736 -0.0490 642 ILE A CG2 4831 C CD1 . ILE A 588 ? 0.2994 0.2634 0.3229 0.0335 -0.0702 -0.0449 642 ILE A CD1 4832 N N . ALA A 589 ? 0.3117 0.2690 0.3374 0.0456 -0.0816 -0.0557 643 ALA A N 4833 C CA . ALA A 589 ? 0.3178 0.2732 0.3371 0.0491 -0.0815 -0.0570 643 ALA A CA 4834 C C . ALA A 589 ? 0.3416 0.2907 0.3605 0.0552 -0.0903 -0.0618 643 ALA A C 4835 O O . ALA A 589 ? 0.3408 0.2844 0.3481 0.0610 -0.0920 -0.0631 643 ALA A O 4836 C CB . ALA A 589 ? 0.3125 0.2740 0.3406 0.0446 -0.0770 -0.0558 643 ALA A CB 4837 N N . SER A 590 ? 0.3454 0.2951 0.3772 0.0540 -0.0960 -0.0643 644 SER A N 4838 C CA . SER A 590 ? 0.3915 0.3351 0.4243 0.0599 -0.1055 -0.0694 644 SER A CA 4839 C C . SER A 590 ? 0.3842 0.3198 0.4018 0.0666 -0.1092 -0.0706 644 SER A C 4840 O O . SER A 590 ? 0.4100 0.3394 0.4180 0.0732 -0.1133 -0.0733 644 SER A O 4841 C CB . SER A 590 ? 0.4008 0.3464 0.4513 0.0572 -0.1111 -0.0717 644 SER A CB 4842 O OG . SER A 590 ? 0.5076 0.4472 0.5593 0.0631 -0.1208 -0.0770 644 SER A OG 4843 N N . LYS A 591 ? 0.3772 0.3129 0.3918 0.0652 -0.1075 -0.0685 645 LYS A N 4844 C CA A LYS A 591 ? 0.3841 0.3125 0.3841 0.0714 -0.1104 -0.0694 645 LYS A CA 4845 C CA B LYS A 591 ? 0.3817 0.3101 0.3817 0.0714 -0.1103 -0.0694 645 LYS A CA 4846 C C . LYS A 591 ? 0.3825 0.3081 0.3660 0.0752 -0.1051 -0.0672 645 LYS A C 4847 O O . LYS A 591 ? 0.3655 0.2836 0.3363 0.0825 -0.1087 -0.0691 645 LYS A O 4848 C CB A LYS A 591 ? 0.3948 0.3244 0.3964 0.0687 -0.1095 -0.0676 645 LYS A CB 4849 C CB B LYS A 591 ? 0.3895 0.3191 0.3908 0.0687 -0.1093 -0.0674 645 LYS A CB 4850 C CG A LYS A 591 ? 0.4222 0.3526 0.4392 0.0666 -0.1161 -0.0703 645 LYS A CG 4851 C CG B LYS A 591 ? 0.4110 0.3403 0.4259 0.0676 -0.1167 -0.0705 645 LYS A CG 4852 C CD A LYS A 591 ? 0.4733 0.4067 0.4950 0.0621 -0.1139 -0.0678 645 LYS A CD 4853 C CD B LYS A 591 ? 0.4287 0.3493 0.4379 0.0757 -0.1266 -0.0757 645 LYS A CD 4854 C CE A LYS A 591 ? 0.4929 0.4266 0.5308 0.0604 -0.1209 -0.0706 645 LYS A CE 4855 C CE B LYS A 591 ? 0.4817 0.4023 0.5075 0.0749 -0.1349 -0.0797 645 LYS A CE 4856 N NZ A LYS A 591 ? 0.4924 0.4304 0.5384 0.0545 -0.1178 -0.0676 645 LYS A NZ 4857 N NZ B LYS A 591 ? 0.4651 0.3920 0.5054 0.0676 -0.1324 -0.0774 645 LYS A NZ 4858 N N . PHE A 592 ? 0.3437 0.2751 0.3272 0.0703 -0.0966 -0.0632 646 PHE A N 4859 C CA . PHE A 592 ? 0.3455 0.2746 0.3151 0.0733 -0.0913 -0.0609 646 PHE A CA 4860 C C . PHE A 592 ? 0.3543 0.2789 0.3192 0.0787 -0.0946 -0.0636 646 PHE A C 4861 O O . PHE A 592 ? 0.3886 0.3069 0.3391 0.0851 -0.0945 -0.0636 646 PHE A O 4862 C CB . PHE A 592 ? 0.3310 0.2676 0.3040 0.0666 -0.0821 -0.0565 646 PHE A CB 4863 C CG . PHE A 592 ? 0.3270 0.2619 0.2878 0.0690 -0.0762 -0.0539 646 PHE A CG 4864 C CD1 . PHE A 592 ? 0.3263 0.2594 0.2766 0.0706 -0.0719 -0.0510 646 PHE A CD1 4865 C CD2 . PHE A 592 ? 0.3586 0.2939 0.3192 0.0698 -0.0751 -0.0545 646 PHE A CD2 4866 C CE1 . PHE A 592 ? 0.3582 0.2897 0.2986 0.0727 -0.0663 -0.0484 646 PHE A CE1 4867 C CE2 . PHE A 592 ? 0.3734 0.3071 0.3235 0.0720 -0.0694 -0.0519 646 PHE A CE2 4868 C CZ . PHE A 592 ? 0.3699 0.3018 0.3103 0.0733 -0.0650 -0.0488 646 PHE A CZ 4869 N N . SER A 593 ? 0.3557 0.2834 0.3322 0.0763 -0.0973 -0.0658 647 SER A N 4870 C CA . SER A 593 ? 0.3910 0.3145 0.3639 0.0814 -0.1010 -0.0687 647 SER A CA 4871 C C . SER A 593 ? 0.4149 0.3290 0.3789 0.0900 -0.1097 -0.0729 647 SER A C 4872 O O . SER A 593 ? 0.4151 0.3230 0.3674 0.0965 -0.1110 -0.0741 647 SER A O 4873 C CB . SER A 593 ? 0.3948 0.3231 0.3833 0.0776 -0.1035 -0.0709 647 SER A CB 4874 O OG A SER A 593 ? 0.3936 0.3304 0.3908 0.0699 -0.0961 -0.0674 647 SER A OG 4875 O OG B SER A 593 ? 0.3987 0.3238 0.3832 0.0818 -0.1056 -0.0731 647 SER A OG 4876 N N . GLU A 594 ? 0.4175 0.3303 0.3873 0.0901 -0.1156 -0.0751 648 GLU A N 4877 C CA . GLU A 594 ? 0.4651 0.3687 0.4263 0.0984 -0.1241 -0.0792 648 GLU A CA 4878 C C . GLU A 594 ? 0.4742 0.3717 0.4156 0.1042 -0.1205 -0.0769 648 GLU A C 4879 O O . GLU A 594 ? 0.4824 0.3718 0.4110 0.1125 -0.1242 -0.0791 648 GLU A O 4880 C CB . GLU A 594 ? 0.4760 0.3797 0.4468 0.0969 -0.1301 -0.0814 648 GLU A CB 4881 C CG . GLU A 594 ? 0.5583 0.4672 0.5496 0.0918 -0.1344 -0.0838 648 GLU A CG 4882 C CD . GLU A 594 ? 0.6447 0.5518 0.6452 0.0920 -0.1422 -0.0869 648 GLU A CD 4883 O OE1 . GLU A 594 ? 0.6500 0.5548 0.6442 0.0930 -0.1421 -0.0858 648 GLU A OE1 4884 O OE2 . GLU A 594 ? 0.7301 0.6383 0.7453 0.0909 -0.1485 -0.0904 648 GLU A OE2 4885 N N . ARG A 595 ? 0.4365 0.3379 0.3754 0.1002 -0.1131 -0.0723 649 ARG A N 4886 C CA . ARG A 595 ? 0.4455 0.3419 0.3672 0.1052 -0.1088 -0.0697 649 ARG A CA 4887 C C . ARG A 595 ? 0.4566 0.3508 0.3682 0.1083 -0.1039 -0.0679 649 ARG A C 4888 O O . ARG A 595 ? 0.4598 0.3464 0.3558 0.1159 -0.1039 -0.0677 649 ARG A O 4889 C CB . ARG A 595 ? 0.4392 0.3405 0.3617 0.0999 -0.1019 -0.0653 649 ARG A CB 4890 C CG . ARG A 595 ? 0.4477 0.3498 0.3775 0.0979 -0.1065 -0.0668 649 ARG A CG 4891 C CD . ARG A 595 ? 0.4233 0.3274 0.3486 0.0954 -0.1005 -0.0628 649 ARG A CD 4892 N NE . ARG A 595 ? 0.3814 0.2931 0.3109 0.0885 -0.0914 -0.0582 649 ARG A NE 4893 C CZ . ARG A 595 ? 0.4167 0.3361 0.3600 0.0805 -0.0893 -0.0571 649 ARG A CZ 4894 N NH1 . ARG A 595 ? 0.3839 0.3046 0.3391 0.0784 -0.0954 -0.0600 649 ARG A NH1 4895 N NH2 . ARG A 595 ? 0.3607 0.2864 0.3063 0.0750 -0.0812 -0.0532 649 ARG A NH2 4896 N N . LEU A 596 ? 0.4556 0.3561 0.3758 0.1028 -0.0999 -0.0665 650 LEU A N 4897 C CA . LEU A 596 ? 0.4856 0.3850 0.3980 0.1048 -0.0949 -0.0646 650 LEU A CA 4898 C C . LEU A 596 ? 0.5319 0.4231 0.4366 0.1131 -0.1017 -0.0686 650 LEU A C 4899 O O . LEU A 596 ? 0.5321 0.4183 0.4240 0.1183 -0.0988 -0.0672 650 LEU A O 4900 C CB . LEU A 596 ? 0.4650 0.3733 0.3898 0.0968 -0.0899 -0.0628 650 LEU A CB 4901 C CG . LEU A 596 ? 0.4662 0.3758 0.3855 0.0963 -0.0825 -0.0595 650 LEU A CG 4902 C CD1 . LEU A 596 ? 0.4577 0.3683 0.3696 0.0950 -0.0745 -0.0546 650 LEU A CD1 4903 C CD2 . LEU A 596 ? 0.4659 0.3837 0.3994 0.0890 -0.0802 -0.0594 650 LEU A CD2 4904 N N . GLN A 597 ? 0.5701 0.4600 0.4831 0.1142 -0.1107 -0.0735 651 GLN A N 4905 C CA . GLN A 597 ? 0.6433 0.5252 0.5501 0.1222 -0.1185 -0.0781 651 GLN A CA 4906 C C . GLN A 597 ? 0.6611 0.5332 0.5525 0.1312 -0.1229 -0.0796 651 GLN A C 4907 O O . GLN A 597 ? 0.6997 0.5637 0.5775 0.1393 -0.1250 -0.0809 651 GLN A O 4908 C CB . GLN A 597 ? 0.6454 0.5299 0.5684 0.1197 -0.1264 -0.0828 651 GLN A CB 4909 C CG . GLN A 597 ? 0.7033 0.5958 0.6373 0.1130 -0.1214 -0.0812 651 GLN A CG 4910 C CD . GLN A 597 ? 0.7769 0.6716 0.7258 0.1115 -0.1284 -0.0857 651 GLN A CD 4911 O OE1 . GLN A 597 ? 0.8097 0.6975 0.7560 0.1181 -0.1371 -0.0905 651 GLN A OE1 4912 N NE2 . GLN A 597 ? 0.7619 0.6660 0.7267 0.1029 -0.1244 -0.0840 651 GLN A NE2 4913 N N . ASP A 598 ? 0.6705 0.5433 0.5633 0.1297 -0.1236 -0.0792 652 ASP A N 4914 C CA . ASP A 598 ? 0.6930 0.5570 0.5736 0.1377 -0.1289 -0.0812 652 ASP A CA 4915 C C . ASP A 598 ? 0.6942 0.5539 0.5575 0.1421 -0.1222 -0.0770 652 ASP A C 4916 O O . ASP A 598 ? 0.6944 0.5479 0.5490 0.1478 -0.1261 -0.0785 652 ASP A O 4917 C CB . ASP A 598 ? 0.6908 0.5573 0.5827 0.1342 -0.1343 -0.0834 652 ASP A CB 4918 C CG . ASP A 598 ? 0.7356 0.6025 0.6419 0.1335 -0.1443 -0.0891 652 ASP A CG 4919 O OD1 . ASP A 598 ? 0.7876 0.6568 0.7051 0.1302 -0.1488 -0.0909 652 ASP A OD1 4920 O OD2 . ASP A 598 ? 0.7375 0.6024 0.6448 0.1360 -0.1476 -0.0917 652 ASP A OD2 4921 N N . PHE A 599 ? 0.6960 0.5591 0.5552 0.1394 -0.1122 -0.0719 653 PHE A N 4922 C CA . PHE A 599 ? 0.6867 0.5453 0.5296 0.1442 -0.1053 -0.0676 653 PHE A CA 4923 C C . PHE A 599 ? 0.7204 0.5725 0.5499 0.1512 -0.1029 -0.0667 653 PHE A C 4924 O O . PHE A 599 ? 0.7652 0.6111 0.5788 0.1577 -0.0982 -0.0637 653 PHE A O 4925 C CB . PHE A 599 ? 0.6707 0.5381 0.5199 0.1357 -0.0954 -0.0621 653 PHE A CB 4926 C CG . PHE A 599 ? 0.5722 0.4441 0.4229 0.1319 -0.0873 -0.0584 653 PHE A CG 4927 C CD1 . PHE A 599 ? 0.5274 0.3967 0.3664 0.1349 -0.0793 -0.0538 653 PHE A CD1 4928 C CD2 . PHE A 599 ? 0.5675 0.4455 0.4310 0.1260 -0.0881 -0.0596 653 PHE A CD2 4929 C CE1 . PHE A 599 ? 0.5597 0.4325 0.4002 0.1318 -0.0723 -0.0505 653 PHE A CE1 4930 C CE2 . PHE A 599 ? 0.5743 0.4559 0.4387 0.1230 -0.0811 -0.0565 653 PHE A CE2 4931 C CZ . PHE A 599 ? 0.5900 0.4691 0.4431 0.1257 -0.0733 -0.0519 653 PHE A CZ 4932 N N A SER A 602 ? 0.4805 0.3057 0.2453 0.1794 -0.0807 -0.0533 656 SER A N 4933 N N B SER A 602 ? 0.4713 0.3063 0.2429 0.1701 -0.0624 -0.0437 656 SER A N 4934 C CA A SER A 602 ? 0.4835 0.3057 0.2366 0.1830 -0.0712 -0.0475 656 SER A CA 4935 C CA B SER A 602 ? 0.4728 0.3022 0.2305 0.1760 -0.0537 -0.0383 656 SER A CA 4936 C C A SER A 602 ? 0.4645 0.2954 0.2260 0.1748 -0.0621 -0.0423 656 SER A C 4937 C C B SER A 602 ? 0.4763 0.3083 0.2339 0.1740 -0.0480 -0.0346 656 SER A C 4938 O O A SER A 602 ? 0.4654 0.2947 0.2194 0.1770 -0.0532 -0.0370 656 SER A O 4939 O O B SER A 602 ? 0.4907 0.3185 0.2379 0.1788 -0.0408 -0.0300 656 SER A O 4940 C CB A SER A 602 ? 0.4608 0.2717 0.1966 0.1944 -0.0755 -0.0492 656 SER A CB 4941 C CB B SER A 602 ? 0.4645 0.2807 0.2028 0.1889 -0.0575 -0.0400 656 SER A CB 4942 O OG A SER A 602 ? 0.4918 0.3052 0.2312 0.1921 -0.0770 -0.0497 656 SER A OG 4943 O OG B SER A 602 ? 0.5187 0.3301 0.2487 0.1942 -0.0601 -0.0408 656 SER A OG 4944 N N A ASN A 603 ? 0.4520 0.2919 0.2290 0.1656 -0.0638 -0.0435 657 ASN A N 4945 N N B ASN A 603 ? 0.4726 0.3120 0.2428 0.1666 -0.0509 -0.0364 657 ASN A N 4946 C CA A ASN A 603 ? 0.4308 0.2775 0.2136 0.1594 -0.0564 -0.0391 657 ASN A CA 4947 C CA B ASN A 603 ? 0.4828 0.3264 0.2557 0.1630 -0.0454 -0.0329 657 ASN A CA 4948 C C A ASN A 603 ? 0.4194 0.2760 0.2155 0.1495 -0.0495 -0.0358 657 ASN A C 4949 C C B ASN A 603 ? 0.4662 0.3201 0.2529 0.1529 -0.0380 -0.0292 657 ASN A C 4950 O O A ASN A 603 ? 0.3865 0.2502 0.1964 0.1420 -0.0528 -0.0382 657 ASN A O 4951 O O B ASN A 603 ? 0.4523 0.3139 0.2529 0.1447 -0.0408 -0.0313 657 ASN A O 4952 C CB A ASN A 603 ? 0.4332 0.2826 0.2225 0.1564 -0.0619 -0.0418 657 ASN A CB 4953 C CB B ASN A 603 ? 0.4727 0.3179 0.2509 0.1612 -0.0531 -0.0370 657 ASN A CB 4954 C CG A ASN A 603 ? 0.4512 0.3049 0.2423 0.1527 -0.0548 -0.0375 657 ASN A CG 4955 C CG B ASN A 603 ? 0.5139 0.3629 0.2944 0.1579 -0.0482 -0.0338 657 ASN A CG 4956 O OD1 A ASN A 603 ? 0.4645 0.3248 0.2623 0.1465 -0.0470 -0.0334 657 ASN A OD1 4957 O OD1 B ASN A 603 ? 0.5443 0.4002 0.3322 0.1514 -0.0405 -0.0297 657 ASN A OD1 4958 N ND2 A ASN A 603 ? 0.4482 0.2981 0.2336 0.1566 -0.0578 -0.0386 657 ASN A ND2 4959 N ND2 B ASN A 603 ? 0.4927 0.3375 0.2677 0.1622 -0.0534 -0.0362 657 ASN A ND2 4960 N N A PRO A 604 ? 0.4119 0.2688 0.2041 0.1497 -0.0400 -0.0305 658 PRO A N 4961 N N B PRO A 604 ? 0.4704 0.3240 0.2532 0.1535 -0.0285 -0.0238 658 PRO A N 4962 C CA A PRO A 604 ? 0.3941 0.2590 0.1977 0.1417 -0.0348 -0.0282 658 PRO A CA 4963 C CA B PRO A 604 ? 0.4546 0.3174 0.2505 0.1443 -0.0224 -0.0209 658 PRO A CA 4964 C C A PRO A 604 ? 0.3845 0.2589 0.2013 0.1323 -0.0319 -0.0267 658 PRO A C 4965 C C B PRO A 604 ? 0.4392 0.3118 0.2495 0.1347 -0.0220 -0.0209 658 PRO A C 4966 O O A PRO A 604 ? 0.3651 0.2469 0.1931 0.1248 -0.0293 -0.0259 658 PRO A O 4967 O O B PRO A 604 ? 0.4249 0.3049 0.2476 0.1270 -0.0226 -0.0219 658 PRO A O 4968 C CB A PRO A 604 ? 0.3971 0.2581 0.1916 0.1458 -0.0259 -0.0230 658 PRO A CB 4969 C CB B PRO A 604 ? 0.4709 0.3309 0.2598 0.1476 -0.0125 -0.0150 658 PRO A CB 4970 C CG A PRO A 604 ? 0.4123 0.2681 0.1963 0.1518 -0.0236 -0.0209 658 PRO A CG 4971 C CG B PRO A 604 ? 0.4830 0.3313 0.2540 0.1593 -0.0141 -0.0153 658 PRO A CG 4972 C CD A PRO A 604 ? 0.4263 0.2764 0.2043 0.1571 -0.0337 -0.0263 658 PRO A CD 4973 C CD B PRO A 604 ? 0.4753 0.3201 0.2422 0.1628 -0.0233 -0.0202 658 PRO A CD 4974 N N A ILE A 605 ? 0.3914 0.2652 0.2060 0.1331 -0.0323 -0.0263 659 ILE A N 4975 N N B ILE A 605 ? 0.4301 0.3027 0.2386 0.1351 -0.0211 -0.0198 659 ILE A N 4976 C CA A ILE A 605 ? 0.3890 0.2712 0.2154 0.1248 -0.0307 -0.0254 659 ILE A CA 4977 C CA B ILE A 605 ? 0.4222 0.3036 0.2438 0.1262 -0.0210 -0.0199 659 ILE A CA 4978 C C A ILE A 605 ? 0.3778 0.2648 0.2154 0.1193 -0.0381 -0.0298 659 ILE A C 4979 C C B ILE A 605 ? 0.4121 0.2967 0.2420 0.1223 -0.0297 -0.0250 659 ILE A C 4980 O O A ILE A 605 ? 0.3378 0.2329 0.1876 0.1111 -0.0362 -0.0292 659 ILE A O 4981 O O B ILE A 605 ? 0.3883 0.2811 0.2312 0.1139 -0.0295 -0.0253 659 ILE A O 4982 C CB A ILE A 605 ? 0.4070 0.2875 0.2287 0.1270 -0.0293 -0.0239 659 ILE A CB 4983 C CB B ILE A 605 ? 0.4213 0.3027 0.2403 0.1270 -0.0173 -0.0172 659 ILE A CB 4984 C CG1 A ILE A 605 ? 0.4405 0.3150 0.2498 0.1339 -0.0224 -0.0197 659 ILE A CG1 4985 C CG1 B ILE A 605 ? 0.4508 0.3329 0.2684 0.1271 -0.0075 -0.0117 659 ILE A CG1 4986 C CG2 A ILE A 605 ? 0.3820 0.2715 0.2160 0.1179 -0.0260 -0.0221 659 ILE A CG2 4987 C CG2 B ILE A 605 ? 0.4135 0.3030 0.2450 0.1186 -0.0192 -0.0184 659 ILE A CG2 4988 C CD1 A ILE A 605 ? 0.4522 0.3271 0.2616 0.1335 -0.0166 -0.0168 659 ILE A CD1 4989 C CD1 B ILE A 605 ? 0.4607 0.3474 0.2860 0.1221 -0.0040 -0.0104 659 ILE A CD1 4990 N N A VAL A 606 ? 0.3660 0.2477 0.1995 0.1242 -0.0464 -0.0342 660 VAL A N 4991 N N B VAL A 606 ? 0.4038 0.2820 0.2268 0.1285 -0.0373 -0.0289 660 VAL A N 4992 C CA A VAL A 606 ? 0.3694 0.2551 0.2143 0.1195 -0.0536 -0.0385 660 VAL A CA 4993 C CA B VAL A 606 ? 0.3879 0.2689 0.2200 0.1250 -0.0457 -0.0339 660 VAL A CA 4994 C C A VAL A 606 ? 0.3600 0.2501 0.2133 0.1151 -0.0530 -0.0391 660 VAL A C 4995 C C B VAL A 606 ? 0.3873 0.2727 0.2283 0.1203 -0.0462 -0.0350 660 VAL A C 4996 O O A VAL A 606 ? 0.3352 0.2327 0.2017 0.1074 -0.0538 -0.0399 660 VAL A O 4997 O O B VAL A 606 ? 0.3654 0.2579 0.2195 0.1129 -0.0482 -0.0365 660 VAL A O 4998 C CB A VAL A 606 ? 0.3832 0.2614 0.2220 0.1265 -0.0631 -0.0434 660 VAL A CB 4999 C CB B VAL A 606 ? 0.4068 0.2795 0.2302 0.1329 -0.0545 -0.0383 660 VAL A CB 5000 C CG1 A VAL A 606 ? 0.3860 0.2680 0.2376 0.1219 -0.0705 -0.0478 660 VAL A CG1 5001 C CG1 B VAL A 606 ? 0.3867 0.2615 0.2202 0.1300 -0.0634 -0.0436 660 VAL A CG1 5002 C CG2 A VAL A 606 ? 0.3969 0.2723 0.2302 0.1293 -0.0640 -0.0431 660 VAL A CG2 5003 C CG2 B VAL A 606 ? 0.4140 0.2844 0.2324 0.1353 -0.0549 -0.0378 660 VAL A CG2 5004 N N A LEU A 607 ? 0.3643 0.2494 0.2094 0.1202 -0.0517 -0.0387 661 LEU A N 5005 N N B LEU A 607 ? 0.3806 0.2618 0.2146 0.1246 -0.0440 -0.0341 661 LEU A N 5006 C CA A LEU A 607 ? 0.3651 0.2539 0.2167 0.1168 -0.0505 -0.0389 661 LEU A CA 5007 C CA B LEU A 607 ? 0.3898 0.2751 0.2317 0.1205 -0.0441 -0.0350 661 LEU A CA 5008 C C A LEU A 607 ? 0.3607 0.2582 0.2222 0.1082 -0.0432 -0.0353 661 LEU A C 5009 C C B LEU A 607 ? 0.3712 0.2660 0.2250 0.1112 -0.0376 -0.0319 661 LEU A C 5010 O O A LEU A 607 ? 0.3385 0.2424 0.2116 0.1020 -0.0443 -0.0366 661 LEU A O 5011 O O B LEU A 607 ? 0.3448 0.2458 0.2098 0.1050 -0.0390 -0.0334 661 LEU A O 5012 C CB A LEU A 607 ? 0.3727 0.2543 0.2122 0.1240 -0.0485 -0.0379 661 LEU A CB 5013 C CB B LEU A 607 ? 0.4020 0.2807 0.2335 0.1271 -0.0423 -0.0342 661 LEU A CB 5014 C CG A LEU A 607 ? 0.3730 0.2575 0.2170 0.1212 -0.0455 -0.0370 661 LEU A CG 5015 C CG B LEU A 607 ? 0.4053 0.2877 0.2439 0.1233 -0.0415 -0.0347 661 LEU A CG 5016 C CD1 A LEU A 607 ? 0.3798 0.2667 0.2327 0.1189 -0.0526 -0.0417 661 LEU A CD1 5017 C CD1 B LEU A 607 ? 0.3901 0.2761 0.2393 0.1197 -0.0494 -0.0396 661 LEU A CD1 5018 C CD2 A LEU A 607 ? 0.4019 0.2784 0.2321 0.1291 -0.0423 -0.0351 661 LEU A CD2 5019 C CD2 B LEU A 607 ? 0.4138 0.2883 0.2402 0.1311 -0.0402 -0.0339 661 LEU A CD2 5020 N N A ARG A 608 ? 0.3695 0.2670 0.2262 0.1086 -0.0358 -0.0308 662 ARG A N 5021 N N B ARG A 608 ? 0.3727 0.2687 0.2241 0.1103 -0.0305 -0.0276 662 ARG A N 5022 C CA A ARG A 608 ? 0.3752 0.2801 0.2402 0.1014 -0.0286 -0.0273 662 ARG A CA 5023 C CA B ARG A 608 ? 0.3699 0.2744 0.2321 0.1019 -0.0247 -0.0248 662 ARG A CA 5024 C C A ARG A 608 ? 0.3687 0.2806 0.2444 0.0943 -0.0297 -0.0278 662 ARG A C 5025 C C B ARG A 608 ? 0.3630 0.2746 0.2372 0.0946 -0.0280 -0.0268 662 ARG A C 5026 O O A ARG A 608 ? 0.3459 0.2648 0.2319 0.0874 -0.0278 -0.0274 662 ARG A O 5027 O O B ARG A 608 ? 0.3408 0.2592 0.2253 0.0879 -0.0264 -0.0266 662 ARG A O 5028 C CB A ARG A 608 ? 0.3852 0.2876 0.2428 0.1042 -0.0208 -0.0225 662 ARG A CB 5029 C CB B ARG A 608 ? 0.3702 0.2740 0.2279 0.1031 -0.0169 -0.0200 662 ARG A CB 5030 C CG A ARG A 608 ? 0.3909 0.3010 0.2576 0.0968 -0.0140 -0.0190 662 ARG A CG 5031 C CG B ARG A 608 ? 0.3475 0.2594 0.2157 0.0951 -0.0110 -0.0171 662 ARG A CG 5032 C CD A ARG A 608 ? 0.3992 0.3119 0.2698 0.0941 -0.0089 -0.0168 662 ARG A CD 5033 C CD B ARG A 608 ? 0.4134 0.3296 0.2891 0.0906 -0.0097 -0.0174 662 ARG A CD 5034 N NE A ARG A 608 ? 0.4481 0.3658 0.3244 0.0893 -0.0022 -0.0131 662 ARG A NE 5035 N NE B ARG A 608 ? 0.4493 0.3698 0.3297 0.0867 -0.0023 -0.0134 662 ARG A NE 5036 C CZ A ARG A 608 ? 0.3787 0.2978 0.2572 0.0879 0.0039 -0.0099 662 ARG A CZ 5037 C CZ B ARG A 608 ? 0.4293 0.3487 0.3084 0.0877 0.0028 -0.0107 662 ARG A CZ 5038 N NH1 A ARG A 608 ? 0.3884 0.3044 0.2635 0.0908 0.0048 -0.0097 662 ARG A NH1 5039 N NH1 B ARG A 608 ? 0.4439 0.3584 0.3171 0.0923 0.0016 -0.0115 662 ARG A NH1 5040 N NH2 A ARG A 608 ? 0.3699 0.2936 0.2543 0.0837 0.0089 -0.0071 662 ARG A NH2 5041 N NH2 B ARG A 608 ? 0.4490 0.3722 0.3334 0.0840 0.0089 -0.0074 662 ARG A NH2 5042 N N . MET A 609 ? 0.3848 0.2944 0.2574 0.0964 -0.0329 -0.0288 663 MET A N 5043 C CA . MET A 609 ? 0.3815 0.2969 0.2645 0.0901 -0.0359 -0.0303 663 MET A CA 5044 C C . MET A 609 ? 0.3841 0.3031 0.2769 0.0863 -0.0408 -0.0337 663 MET A C 5045 O O . MET A 609 ? 0.3603 0.2867 0.2643 0.0790 -0.0394 -0.0333 663 MET A O 5046 C CB A MET A 609 ? 0.3837 0.2949 0.2620 0.0940 -0.0409 -0.0322 663 MET A CB 5047 C CB B MET A 609 ? 0.3929 0.3043 0.2705 0.0938 -0.0394 -0.0313 663 MET A CB 5048 C CG A MET A 609 ? 0.3490 0.2650 0.2380 0.0885 -0.0455 -0.0344 663 MET A CG 5049 C CG B MET A 609 ? 0.3762 0.2850 0.2450 0.0971 -0.0332 -0.0273 663 MET A CG 5050 S SD A MET A 609 ? 0.3558 0.2665 0.2393 0.0931 -0.0515 -0.0366 663 MET A SD 5051 S SD B MET A 609 ? 0.4369 0.3425 0.3001 0.1003 -0.0351 -0.0273 663 MET A SD 5052 C CE A MET A 609 ? 0.4201 0.3240 0.2999 0.0996 -0.0604 -0.0417 663 MET A CE 5053 C CE B MET A 609 ? 0.3589 0.2537 0.2090 0.1109 -0.0426 -0.0311 663 MET A CE 5054 N N . MET A 610 ? 0.3728 0.2868 0.2621 0.0913 -0.0466 -0.0371 664 MET A N 5055 C CA . MET A 610 ? 0.3728 0.2902 0.2723 0.0879 -0.0514 -0.0403 664 MET A CA 5056 C C . MET A 610 ? 0.3596 0.2821 0.2650 0.0834 -0.0469 -0.0389 664 MET A C 5057 O O . MET A 610 ? 0.3556 0.2843 0.2726 0.0774 -0.0476 -0.0398 664 MET A O 5058 C CB A MET A 610 ? 0.3972 0.3074 0.2909 0.0950 -0.0587 -0.0443 664 MET A CB 5059 C CB B MET A 610 ? 0.3838 0.2950 0.2802 0.0938 -0.0600 -0.0449 664 MET A CB 5060 C CG A MET A 610 ? 0.4335 0.3366 0.3185 0.1015 -0.0639 -0.0462 664 MET A CG 5061 C CG B MET A 610 ? 0.3760 0.2845 0.2716 0.0958 -0.0654 -0.0469 664 MET A CG 5062 S SD A MET A 610 ? 0.5051 0.4129 0.4014 0.0960 -0.0679 -0.0478 664 MET A SD 5063 S SD B MET A 610 ? 0.3884 0.2909 0.2845 0.1012 -0.0767 -0.0530 664 MET A SD 5064 C CE A MET A 610 ? 0.4863 0.3933 0.3918 0.0965 -0.0776 -0.0535 664 MET A CE 5065 C CE B MET A 610 ? 0.3463 0.2576 0.2624 0.0922 -0.0794 -0.0548 664 MET A CE 5066 N N . ASN A 611 ? 0.3474 0.2667 0.2447 0.0868 -0.0423 -0.0366 665 ASN A N 5067 C CA . ASN A 611 ? 0.3431 0.2669 0.2455 0.0828 -0.0378 -0.0351 665 ASN A CA 5068 C C . ASN A 611 ? 0.3359 0.2673 0.2464 0.0752 -0.0323 -0.0322 665 ASN A C 5069 O O . ASN A 611 ? 0.3383 0.2753 0.2573 0.0701 -0.0308 -0.0322 665 ASN A O 5070 C CB . ASN A 611 ? 0.3438 0.2626 0.2361 0.0879 -0.0336 -0.0328 665 ASN A CB 5071 C CG . ASN A 611 ? 0.3460 0.2588 0.2328 0.0938 -0.0385 -0.0357 665 ASN A CG 5072 O OD1 . ASN A 611 ? 0.3659 0.2805 0.2597 0.0923 -0.0440 -0.0393 665 ASN A OD1 5073 N ND2 . ASN A 611 ? 0.3398 0.2459 0.2148 0.1004 -0.0362 -0.0341 665 ASN A ND2 5074 N N . ASP A 612 ? 0.3406 0.2720 0.2481 0.0751 -0.0294 -0.0298 666 ASP A N 5075 C CA . ASP A 612 ? 0.3303 0.2686 0.2458 0.0682 -0.0253 -0.0277 666 ASP A CA 5076 C C . ASP A 612 ? 0.3279 0.2714 0.2538 0.0629 -0.0291 -0.0300 666 ASP A C 5077 O O . ASP A 612 ? 0.3114 0.2611 0.2455 0.0569 -0.0263 -0.0291 666 ASP A O 5078 C CB . ASP A 612 ? 0.3280 0.2651 0.2386 0.0692 -0.0219 -0.0250 666 ASP A CB 5079 C CG . ASP A 612 ? 0.3506 0.2853 0.2548 0.0720 -0.0157 -0.0215 666 ASP A CG 5080 O OD1 . ASP A 612 ? 0.3854 0.3194 0.2888 0.0728 -0.0137 -0.0211 666 ASP A OD1 5081 O OD2 . ASP A 612 ? 0.3615 0.2951 0.2621 0.0731 -0.0124 -0.0190 666 ASP A OD2 5082 N N . GLN A 613 ? 0.3084 0.2492 0.2342 0.0651 -0.0352 -0.0328 667 GLN A N 5083 C CA . GLN A 613 ? 0.2943 0.2398 0.2310 0.0602 -0.0388 -0.0348 667 GLN A CA 5084 C C . GLN A 613 ? 0.3102 0.2591 0.2543 0.0577 -0.0394 -0.0362 667 GLN A C 5085 O O . GLN A 613 ? 0.2977 0.2525 0.2510 0.0519 -0.0380 -0.0359 667 GLN A O 5086 C CB . GLN A 613 ? 0.3134 0.2551 0.2497 0.0633 -0.0459 -0.0378 667 GLN A CB 5087 C CG . GLN A 613 ? 0.3037 0.2436 0.2351 0.0644 -0.0451 -0.0363 667 GLN A CG 5088 C CD . GLN A 613 ? 0.3440 0.2792 0.2738 0.0683 -0.0524 -0.0394 667 GLN A CD 5089 O OE1 . GLN A 613 ? 0.3780 0.3065 0.2989 0.0750 -0.0556 -0.0410 667 GLN A OE1 5090 N NE2 . GLN A 613 ? 0.3126 0.2511 0.2509 0.0643 -0.0550 -0.0402 667 GLN A NE2 5091 N N . LEU A 614 ? 0.3124 0.2572 0.2518 0.0621 -0.0411 -0.0377 668 LEU A N 5092 C CA . LEU A 614 ? 0.3075 0.2556 0.2540 0.0596 -0.0413 -0.0390 668 LEU A CA 5093 C C . LEU A 614 ? 0.2885 0.2418 0.2379 0.0550 -0.0346 -0.0362 668 LEU A C 5094 O O . LEU A 614 ? 0.2912 0.2500 0.2498 0.0501 -0.0339 -0.0366 668 LEU A O 5095 C CB . LEU A 614 ? 0.3205 0.2627 0.2606 0.0658 -0.0447 -0.0412 668 LEU A CB 5096 C CG . LEU A 614 ? 0.3589 0.2970 0.2999 0.0695 -0.0529 -0.0452 668 LEU A CG 5097 C CD1 . LEU A 614 ? 0.4346 0.3659 0.3671 0.0764 -0.0560 -0.0471 668 LEU A CD1 5098 C CD2 . LEU A 614 ? 0.3676 0.3111 0.3226 0.0646 -0.0562 -0.0474 668 LEU A CD2 5099 N N . MET A 615 ? 0.3006 0.2521 0.2426 0.0566 -0.0299 -0.0333 669 MET A N 5100 C CA . MET A 615 ? 0.3087 0.2644 0.2532 0.0527 -0.0237 -0.0307 669 MET A CA 5101 C C . MET A 615 ? 0.2841 0.2462 0.2364 0.0463 -0.0215 -0.0295 669 MET A C 5102 O O . MET A 615 ? 0.2868 0.2538 0.2451 0.0420 -0.0189 -0.0290 669 MET A O 5103 C CB . MET A 615 ? 0.3006 0.2526 0.2362 0.0560 -0.0192 -0.0277 669 MET A CB 5104 C CG . MET A 615 ? 0.3701 0.3259 0.3085 0.0524 -0.0132 -0.0252 669 MET A CG 5105 S SD . MET A 615 ? 0.3855 0.3371 0.3156 0.0561 -0.0075 -0.0214 669 MET A SD 5106 C CE . MET A 615 ? 0.3947 0.3470 0.3239 0.0551 -0.0063 -0.0196 669 MET A CE 5107 N N . PHE A 616 ? 0.2787 0.2403 0.2298 0.0462 -0.0224 -0.0290 670 PHE A N 5108 C CA . PHE A 616 ? 0.2773 0.2444 0.2348 0.0405 -0.0203 -0.0277 670 PHE A CA 5109 C C . PHE A 616 ? 0.2792 0.2499 0.2455 0.0370 -0.0235 -0.0296 670 PHE A C 5110 O O . PHE A 616 ? 0.2789 0.2539 0.2502 0.0325 -0.0218 -0.0285 670 PHE A O 5111 C CB . PHE A 616 ? 0.2557 0.2209 0.2085 0.0416 -0.0194 -0.0260 670 PHE A CB 5112 C CG . PHE A 616 ? 0.3007 0.2645 0.2478 0.0432 -0.0145 -0.0233 670 PHE A CG 5113 C CD1 . PHE A 616 ? 0.2952 0.2631 0.2459 0.0394 -0.0097 -0.0215 670 PHE A CD1 5114 C CD2 . PHE A 616 ? 0.3142 0.2724 0.2526 0.0484 -0.0144 -0.0224 670 PHE A CD2 5115 C CE1 . PHE A 616 ? 0.2947 0.2612 0.2415 0.0407 -0.0053 -0.0189 670 PHE A CE1 5116 C CE2 . PHE A 616 ? 0.3224 0.2794 0.2565 0.0498 -0.0094 -0.0195 670 PHE A CE2 5117 C CZ . PHE A 616 ? 0.3264 0.2876 0.2652 0.0458 -0.0048 -0.0177 670 PHE A CZ 5118 N N . LEU A 617 ? 0.2750 0.2441 0.2437 0.0390 -0.0281 -0.0323 671 LEU A N 5119 C CA . LEU A 617 ? 0.2706 0.2431 0.2490 0.0357 -0.0309 -0.0340 671 LEU A CA 5120 C C . LEU A 617 ? 0.2548 0.2334 0.2404 0.0307 -0.0270 -0.0330 671 LEU A C 5121 O O . LEU A 617 ? 0.2418 0.2244 0.2334 0.0265 -0.0258 -0.0322 671 LEU A O 5122 C CB . LEU A 617 ? 0.2708 0.2401 0.2512 0.0392 -0.0370 -0.0373 671 LEU A CB 5123 C CG . LEU A 617 ? 0.2779 0.2508 0.2699 0.0358 -0.0399 -0.0389 671 LEU A CG 5124 C CD1 . LEU A 617 ? 0.2674 0.2421 0.2633 0.0330 -0.0403 -0.0380 671 LEU A CD1 5125 C CD2 . LEU A 617 ? 0.3212 0.2902 0.3148 0.0400 -0.0465 -0.0426 671 LEU A CD2 5126 N N . GLU A 618 ? 0.2315 0.2104 0.2156 0.0314 -0.0249 -0.0330 672 GLU A N 5127 C CA . GLU A 618 ? 0.2397 0.2238 0.2291 0.0271 -0.0210 -0.0320 672 GLU A CA 5128 C C . GLU A 618 ? 0.2407 0.2274 0.2290 0.0239 -0.0167 -0.0293 672 GLU A C 5129 O O . GLU A 618 ? 0.2372 0.2285 0.2311 0.0198 -0.0146 -0.0286 672 GLU A O 5130 C CB . GLU A 618 ? 0.2490 0.2325 0.2360 0.0286 -0.0192 -0.0323 672 GLU A CB 5131 C CG . GLU A 618 ? 0.2244 0.2132 0.2183 0.0247 -0.0166 -0.0322 672 GLU A CG 5132 C CD . GLU A 618 ? 0.2720 0.2625 0.2739 0.0241 -0.0198 -0.0345 672 GLU A CD 5133 O OE1 . GLU A 618 ? 0.2511 0.2387 0.2522 0.0274 -0.0231 -0.0365 672 GLU A OE1 5134 O OE2 . GLU A 618 ? 0.2416 0.2361 0.2508 0.0205 -0.0193 -0.0342 672 GLU A OE2 5135 N N . ARG A 619 ? 0.2368 0.2205 0.2179 0.0260 -0.0155 -0.0279 673 ARG A N 5136 C CA . ARG A 619 ? 0.2395 0.2252 0.2194 0.0235 -0.0118 -0.0256 673 ARG A CA 5137 C C . ARG A 619 ? 0.2355 0.2236 0.2197 0.0206 -0.0128 -0.0253 673 ARG A C 5138 O O . ARG A 619 ? 0.2283 0.2197 0.2146 0.0172 -0.0100 -0.0240 673 ARG A O 5139 C CB . ARG A 619 ? 0.2464 0.2281 0.2186 0.0268 -0.0106 -0.0242 673 ARG A CB 5140 C CG . ARG A 619 ? 0.2563 0.2400 0.2278 0.0248 -0.0059 -0.0219 673 ARG A CG 5141 C CD . ARG A 619 ? 0.2766 0.2602 0.2475 0.0255 -0.0034 -0.0217 673 ARG A CD 5142 N NE . ARG A 619 ? 0.2325 0.2111 0.1967 0.0302 -0.0029 -0.0210 673 ARG A NE 5143 C CZ . ARG A 619 ? 0.2654 0.2407 0.2267 0.0337 -0.0047 -0.0223 673 ARG A CZ 5144 N NH1 . ARG A 619 ? 0.2266 0.2033 0.1920 0.0331 -0.0075 -0.0246 673 ARG A NH1 5145 N NH2 . ARG A 619 ? 0.2793 0.2498 0.2338 0.0382 -0.0036 -0.0211 673 ARG A NH2 5146 N N . ALA A 620 ? 0.2220 0.2081 0.2074 0.0220 -0.0169 -0.0268 674 ALA A N 5147 C CA . ALA A 620 ? 0.2341 0.2219 0.2235 0.0194 -0.0180 -0.0263 674 ALA A CA 5148 C C . ALA A 620 ? 0.2374 0.2301 0.2349 0.0152 -0.0167 -0.0262 674 ALA A C 5149 O O . ALA A 620 ? 0.2407 0.2354 0.2411 0.0125 -0.0160 -0.0250 674 ALA A O 5150 C CB . ALA A 620 ? 0.2177 0.2019 0.2071 0.0223 -0.0234 -0.0282 674 ALA A CB 5151 N N . PHE A 621 ? 0.2177 0.2122 0.2186 0.0147 -0.0159 -0.0270 675 PHE A N 5152 C CA . PHE A 621 ? 0.2223 0.2213 0.2304 0.0110 -0.0140 -0.0266 675 PHE A CA 5153 C C . PHE A 621 ? 0.2152 0.2172 0.2216 0.0083 -0.0092 -0.0247 675 PHE A C 5154 O O . PHE A 621 ? 0.2174 0.2229 0.2286 0.0056 -0.0071 -0.0241 675 PHE A O 5155 C CB . PHE A 621 ? 0.2233 0.2235 0.2368 0.0114 -0.0151 -0.0284 675 PHE A CB 5156 C CG . PHE A 621 ? 0.2323 0.2304 0.2502 0.0132 -0.0201 -0.0305 675 PHE A CG 5157 C CD1 . PHE A 621 ? 0.2247 0.2240 0.2491 0.0113 -0.0217 -0.0302 675 PHE A CD1 5158 C CD2 . PHE A 621 ? 0.2340 0.2285 0.2491 0.0171 -0.0235 -0.0326 675 PHE A CD2 5159 C CE1 . PHE A 621 ? 0.2540 0.2511 0.2835 0.0132 -0.0270 -0.0325 675 PHE A CE1 5160 C CE2 . PHE A 621 ? 0.2585 0.2506 0.2776 0.0193 -0.0290 -0.0350 675 PHE A CE2 5161 C CZ . PHE A 621 ? 0.2660 0.2595 0.2926 0.0172 -0.0308 -0.0349 675 PHE A CZ 5162 N N . ILE A 622 ? 0.2248 0.2252 0.2248 0.0095 -0.0076 -0.0238 676 ILE A N 5163 C CA . ILE A 622 ? 0.2308 0.2335 0.2293 0.0073 -0.0038 -0.0223 676 ILE A CA 5164 C C . ILE A 622 ? 0.2292 0.2328 0.2276 0.0052 -0.0032 -0.0209 676 ILE A C 5165 O O . ILE A 622 ? 0.2398 0.2411 0.2358 0.0063 -0.0050 -0.0206 676 ILE A O 5166 C CB . ILE A 622 ? 0.2396 0.2399 0.2321 0.0094 -0.0025 -0.0219 676 ILE A CB 5167 C CG1 . ILE A 622 ? 0.1846 0.1839 0.1769 0.0115 -0.0028 -0.0231 676 ILE A CG1 5168 C CG2 . ILE A 622 ? 0.2396 0.2417 0.2308 0.0075 0.0006 -0.0205 676 ILE A CG2 5169 C CD1 . ILE A 622 ? 0.2139 0.2170 0.2108 0.0091 -0.0008 -0.0236 676 ILE A CD1 5170 N N . ASP A 623 ? 0.2094 0.2160 0.2102 0.0025 -0.0008 -0.0201 677 ASP A N 5171 C CA . ASP A 623 ? 0.2142 0.2215 0.2139 0.0007 0.0001 -0.0186 677 ASP A CA 5172 C C . ASP A 623 ? 0.2191 0.2267 0.2148 0.0005 0.0024 -0.0179 677 ASP A C 5173 O O . ASP A 623 ? 0.2258 0.2352 0.2220 0.0000 0.0044 -0.0182 677 ASP A O 5174 C CB . ASP A 623 ? 0.2098 0.2200 0.2141 -0.0016 0.0015 -0.0180 677 ASP A CB 5175 C CG . ASP A 623 ? 0.2177 0.2281 0.2210 -0.0031 0.0022 -0.0164 677 ASP A CG 5176 O OD1 . ASP A 623 ? 0.2356 0.2448 0.2343 -0.0028 0.0024 -0.0159 677 ASP A OD1 5177 O OD2 . ASP A 623 ? 0.2203 0.2317 0.2277 -0.0045 0.0024 -0.0156 677 ASP A OD2 5178 N N . PRO A 624 ? 0.2443 0.2502 0.2364 0.0011 0.0021 -0.0172 678 PRO A N 5179 C CA . PRO A 624 ? 0.2620 0.2681 0.2516 0.0010 0.0040 -0.0168 678 PRO A CA 5180 C C . PRO A 624 ? 0.2831 0.2915 0.2732 -0.0011 0.0057 -0.0163 678 PRO A C 5181 O O . PRO A 624 ? 0.3122 0.3210 0.3011 -0.0013 0.0070 -0.0164 678 PRO A O 5182 C CB . PRO A 624 ? 0.2636 0.2673 0.2501 0.0022 0.0032 -0.0159 678 PRO A CB 5183 C CG . PRO A 624 ? 0.2658 0.2690 0.2531 0.0018 0.0011 -0.0157 678 PRO A CG 5184 C CD . PRO A 624 ? 0.2479 0.2516 0.2386 0.0021 0.0000 -0.0168 678 PRO A CD 5185 N N . LEU A 625 ? 0.2533 0.2629 0.2453 -0.0026 0.0057 -0.0159 679 LEU A N 5186 C CA . LEU A 625 ? 0.2432 0.2546 0.2350 -0.0041 0.0075 -0.0154 679 LEU A CA 5187 C C . LEU A 625 ? 0.2645 0.2777 0.2583 -0.0044 0.0091 -0.0161 679 LEU A C 5188 O O . LEU A 625 ? 0.2522 0.2668 0.2453 -0.0051 0.0109 -0.0159 679 LEU A O 5189 C CB . LEU A 625 ? 0.2409 0.2522 0.2332 -0.0053 0.0072 -0.0142 679 LEU A CB 5190 C CG . LEU A 625 ? 0.2096 0.2190 0.1996 -0.0050 0.0056 -0.0135 679 LEU A CG 5191 C CD1 . LEU A 625 ? 0.2451 0.2545 0.2356 -0.0063 0.0055 -0.0122 679 LEU A CD1 5192 C CD2 . LEU A 625 ? 0.2852 0.2942 0.2718 -0.0047 0.0061 -0.0136 679 LEU A CD2 5193 N N . GLY A 626 ? 0.2551 0.2684 0.2513 -0.0035 0.0085 -0.0171 680 GLY A N 5194 C CA . GLY A 626 ? 0.2697 0.2849 0.2683 -0.0036 0.0099 -0.0179 680 GLY A CA 5195 C C . GLY A 626 ? 0.2856 0.3026 0.2877 -0.0048 0.0111 -0.0171 680 GLY A C 5196 O O . GLY A 626 ? 0.2940 0.3107 0.2974 -0.0055 0.0105 -0.0161 680 GLY A O 5197 N N A LEU A 627 ? 0.2837 0.3025 0.2875 -0.0049 0.0130 -0.0176 681 LEU A N 5198 N N B LEU A 627 ? 0.2871 0.3059 0.2909 -0.0049 0.0130 -0.0176 681 LEU A N 5199 C CA A LEU A 627 ? 0.2961 0.3168 0.3030 -0.0059 0.0151 -0.0165 681 LEU A CA 5200 C CA B LEU A 627 ? 0.2993 0.3201 0.3064 -0.0059 0.0151 -0.0166 681 LEU A CA 5201 C C A LEU A 627 ? 0.2999 0.3209 0.3024 -0.0062 0.0175 -0.0156 681 LEU A C 5202 C C B LEU A 627 ? 0.3052 0.3262 0.3078 -0.0062 0.0175 -0.0156 681 LEU A C 5203 O O A LEU A 627 ? 0.3022 0.3224 0.3002 -0.0056 0.0174 -0.0164 681 LEU A O 5204 O O B LEU A 627 ? 0.3095 0.3297 0.3077 -0.0055 0.0174 -0.0165 681 LEU A O 5205 C CB A LEU A 627 ? 0.2864 0.3089 0.2981 -0.0056 0.0160 -0.0174 681 LEU A CB 5206 C CB B LEU A 627 ? 0.2883 0.3109 0.3000 -0.0055 0.0159 -0.0176 681 LEU A CB 5207 C CG A LEU A 627 ? 0.2979 0.3200 0.3144 -0.0051 0.0132 -0.0184 681 LEU A CG 5208 C CG B LEU A 627 ? 0.3018 0.3247 0.3200 -0.0055 0.0140 -0.0181 681 LEU A CG 5209 C CD1 A LEU A 627 ? 0.3062 0.3300 0.3268 -0.0046 0.0140 -0.0196 681 LEU A CD1 5210 C CD1 B LEU A 627 ? 0.2814 0.3049 0.3040 -0.0067 0.0146 -0.0164 681 LEU A CD1 5211 C CD2 A LEU A 627 ? 0.3095 0.3315 0.3309 -0.0060 0.0122 -0.0174 681 LEU A CD2 5212 C CD2 B LEU A 627 ? 0.2562 0.2768 0.2735 -0.0042 0.0105 -0.0193 681 LEU A CD2 5213 N N . PRO A 628 ? 0.3230 0.3448 0.3268 -0.0069 0.0197 -0.0139 682 PRO A N 5214 C CA . PRO A 628 ? 0.3318 0.3532 0.3303 -0.0065 0.0219 -0.0131 682 PRO A CA 5215 C C . PRO A 628 ? 0.3354 0.3572 0.3302 -0.0053 0.0228 -0.0146 682 PRO A C 5216 O O . PRO A 628 ? 0.3387 0.3620 0.3359 -0.0049 0.0243 -0.0152 682 PRO A O 5217 C CB . PRO A 628 ? 0.3550 0.3774 0.3565 -0.0071 0.0249 -0.0109 682 PRO A CB 5218 C CG . PRO A 628 ? 0.3419 0.3645 0.3495 -0.0082 0.0231 -0.0103 682 PRO A CG 5219 C CD . PRO A 628 ? 0.3291 0.3520 0.3393 -0.0078 0.0206 -0.0126 682 PRO A CD 5220 N N . ASP A 629 ? 0.3529 0.3730 0.3423 -0.0047 0.0217 -0.0153 683 ASP A N 5221 C CA . ASP A 629 ? 0.3703 0.3901 0.3561 -0.0035 0.0218 -0.0170 683 ASP A CA 5222 C C . ASP A 629 ? 0.3502 0.3708 0.3390 -0.0032 0.0207 -0.0188 683 ASP A C 5223 O O . ASP A 629 ? 0.3438 0.3646 0.3310 -0.0022 0.0211 -0.0203 683 ASP A O 5224 C CB . ASP A 629 ? 0.3981 0.4186 0.3817 -0.0024 0.0248 -0.0166 683 ASP A CB 5225 C CG . ASP A 629 ? 0.4785 0.4978 0.4583 -0.0022 0.0263 -0.0146 683 ASP A CG 5226 O OD1 . ASP A 629 ? 0.5103 0.5277 0.4860 -0.0020 0.0244 -0.0148 683 ASP A OD1 5227 O OD2 . ASP A 629 ? 0.5376 0.5578 0.5190 -0.0022 0.0293 -0.0128 683 ASP A OD2 5228 N N . ARG A 630 ? 0.3237 0.3446 0.3166 -0.0039 0.0194 -0.0188 684 ARG A N 5229 C CA . ARG A 630 ? 0.3068 0.3280 0.3021 -0.0034 0.0184 -0.0203 684 ARG A CA 5230 C C . ARG A 630 ? 0.2815 0.3010 0.2771 -0.0034 0.0161 -0.0203 684 ARG A C 5231 O O . ARG A 630 ? 0.2780 0.2974 0.2765 -0.0034 0.0150 -0.0202 684 ARG A O 5232 C CB . ARG A 630 ? 0.2992 0.3222 0.2991 -0.0034 0.0195 -0.0204 684 ARG A CB 5233 C CG . ARG A 630 ? 0.3274 0.3521 0.3270 -0.0029 0.0224 -0.0205 684 ARG A CG 5234 C CD . ARG A 630 ? 0.3639 0.3906 0.3687 -0.0028 0.0234 -0.0208 684 ARG A CD 5235 N NE . ARG A 630 ? 0.3777 0.4050 0.3878 -0.0037 0.0231 -0.0197 684 ARG A NE 5236 C CZ . ARG A 630 ? 0.3692 0.3977 0.3853 -0.0038 0.0226 -0.0202 684 ARG A CZ 5237 N NH1 . ARG A 630 ? 0.3798 0.4093 0.3973 -0.0029 0.0227 -0.0219 684 ARG A NH1 5238 N NH2 . ARG A 630 ? 0.4119 0.4408 0.4333 -0.0046 0.0219 -0.0193 684 ARG A NH2 5239 N N . PRO A 631 ? 0.2925 0.3106 0.2851 -0.0032 0.0152 -0.0205 685 PRO A N 5240 C CA . PRO A 631 ? 0.2769 0.2933 0.2693 -0.0031 0.0135 -0.0200 685 PRO A CA 5241 C C . PRO A 631 ? 0.2485 0.2642 0.2427 -0.0021 0.0127 -0.0207 685 PRO A C 5242 O O . PRO A 631 ? 0.2659 0.2801 0.2599 -0.0015 0.0115 -0.0202 685 PRO A O 5243 C CB . PRO A 631 ? 0.2980 0.3133 0.2878 -0.0030 0.0130 -0.0203 685 PRO A CB 5244 C CG . PRO A 631 ? 0.3184 0.3346 0.3073 -0.0027 0.0140 -0.0215 685 PRO A CG 5245 C CD . PRO A 631 ? 0.2946 0.3124 0.2840 -0.0029 0.0156 -0.0212 685 PRO A CD 5246 N N . PHE A 632 ? 0.2335 0.2500 0.2288 -0.0015 0.0134 -0.0219 686 PHE A N 5247 C CA . PHE A 632 ? 0.2300 0.2454 0.2265 -0.0003 0.0128 -0.0225 686 PHE A CA 5248 C C . PHE A 632 ? 0.2413 0.2573 0.2405 0.0000 0.0123 -0.0229 686 PHE A C 5249 O O . PHE A 632 ? 0.2446 0.2594 0.2442 0.0014 0.0114 -0.0234 686 PHE A O 5250 C CB . PHE A 632 ? 0.2278 0.2432 0.2243 0.0001 0.0135 -0.0235 686 PHE A CB 5251 C CG . PHE A 632 ? 0.2483 0.2629 0.2434 0.0000 0.0135 -0.0234 686 PHE A CG 5252 C CD1 . PHE A 632 ? 0.2682 0.2810 0.2627 0.0003 0.0130 -0.0224 686 PHE A CD1 5253 C CD2 . PHE A 632 ? 0.2598 0.2753 0.2542 -0.0004 0.0139 -0.0243 686 PHE A CD2 5254 C CE1 . PHE A 632 ? 0.2457 0.2579 0.2401 0.0000 0.0128 -0.0223 686 PHE A CE1 5255 C CE2 . PHE A 632 ? 0.2661 0.2807 0.2598 -0.0006 0.0134 -0.0245 686 PHE A CE2 5256 C CZ . PHE A 632 ? 0.2549 0.2680 0.2491 -0.0005 0.0128 -0.0235 686 PHE A CZ 5257 N N . TYR A 633 ? 0.2263 0.2439 0.2273 -0.0009 0.0127 -0.0225 687 TYR A N 5258 C CA . TYR A 633 ? 0.2302 0.2483 0.2350 -0.0006 0.0117 -0.0228 687 TYR A CA 5259 C C . TYR A 633 ? 0.2245 0.2415 0.2295 -0.0010 0.0102 -0.0218 687 TYR A C 5260 O O . TYR A 633 ? 0.2352 0.2531 0.2404 -0.0023 0.0110 -0.0206 687 TYR A O 5261 C CB . TYR A 633 ? 0.2428 0.2636 0.2512 -0.0014 0.0134 -0.0230 687 TYR A CB 5262 C CG . TYR A 633 ? 0.2247 0.2465 0.2335 -0.0007 0.0145 -0.0243 687 TYR A CG 5263 C CD1 . TYR A 633 ? 0.2634 0.2836 0.2713 0.0006 0.0132 -0.0254 687 TYR A CD1 5264 C CD2 . TYR A 633 ? 0.2944 0.3185 0.3045 -0.0012 0.0167 -0.0244 687 TYR A CD2 5265 C CE1 . TYR A 633 ? 0.2484 0.2693 0.2568 0.0013 0.0141 -0.0266 687 TYR A CE1 5266 C CE2 . TYR A 633 ? 0.2850 0.3099 0.2954 -0.0004 0.0176 -0.0258 687 TYR A CE2 5267 C CZ . TYR A 633 ? 0.2824 0.3057 0.2921 0.0007 0.0161 -0.0269 687 TYR A CZ 5268 O OH . TYR A 633 ? 0.3158 0.3398 0.3262 0.0015 0.0167 -0.0283 687 TYR A OH 5269 N N . ARG A 634 ? 0.1945 0.2092 0.1989 0.0004 0.0079 -0.0221 688 ARG A N 5270 C CA . ARG A 634 ? 0.2033 0.2165 0.2068 0.0004 0.0063 -0.0213 688 ARG A CA 5271 C C . ARG A 634 ? 0.2162 0.2285 0.2231 0.0014 0.0036 -0.0220 688 ARG A C 5272 O O . ARG A 634 ? 0.2234 0.2343 0.2301 0.0016 0.0018 -0.0216 688 ARG A O 5273 C CB . ARG A 634 ? 0.2034 0.2140 0.2022 0.0017 0.0058 -0.0209 688 ARG A CB 5274 C CG . ARG A 634 ? 0.2245 0.2358 0.2210 0.0010 0.0080 -0.0205 688 ARG A CG 5275 C CD . ARG A 634 ? 0.2440 0.2534 0.2373 0.0016 0.0079 -0.0196 688 ARG A CD 5276 N NE . ARG A 634 ? 0.2369 0.2435 0.2283 0.0040 0.0071 -0.0196 688 ARG A NE 5277 C CZ . ARG A 634 ? 0.2833 0.2877 0.2720 0.0053 0.0069 -0.0187 688 ARG A CZ 5278 N NH1 . ARG A 634 ? 0.2525 0.2540 0.2391 0.0080 0.0065 -0.0187 688 ARG A NH1 5279 N NH2 . ARG A 634 ? 0.2514 0.2560 0.2393 0.0042 0.0073 -0.0177 688 ARG A NH2 5280 N N . HIS A 635 ? 0.2105 0.2233 0.2203 0.0022 0.0030 -0.0234 689 HIS A N 5281 C CA . HIS A 635 ? 0.2280 0.2395 0.2414 0.0036 -0.0002 -0.0246 689 HIS A CA 5282 C C . HIS A 635 ? 0.2281 0.2421 0.2482 0.0015 0.0000 -0.0241 689 HIS A C 5283 O O . HIS A 635 ? 0.2359 0.2528 0.2600 0.0002 0.0021 -0.0240 689 HIS A O 5284 C CB . HIS A 635 ? 0.2365 0.2478 0.2517 0.0053 -0.0011 -0.0264 689 HIS A CB 5285 C CG . HIS A 635 ? 0.2386 0.2472 0.2552 0.0077 -0.0053 -0.0279 689 HIS A CG 5286 N ND1 . HIS A 635 ? 0.1822 0.1913 0.2052 0.0072 -0.0077 -0.0286 689 HIS A ND1 5287 C CD2 . HIS A 635 ? 0.2252 0.2301 0.2374 0.0109 -0.0075 -0.0290 689 HIS A CD2 5288 C CE1 . HIS A 635 ? 0.2326 0.2385 0.2550 0.0101 -0.0118 -0.0303 689 HIS A CE1 5289 N NE2 . HIS A 635 ? 0.2309 0.2341 0.2463 0.0125 -0.0116 -0.0306 689 HIS A NE2 5290 N N . VAL A 636 ? 0.2175 0.2302 0.2394 0.0015 -0.0024 -0.0238 690 VAL A N 5291 C CA . VAL A 636 ? 0.2159 0.2309 0.2442 -0.0007 -0.0015 -0.0227 690 VAL A CA 5292 C C . VAL A 636 ? 0.2224 0.2389 0.2592 -0.0006 -0.0028 -0.0240 690 VAL A C 5293 O O . VAL A 636 ? 0.2068 0.2259 0.2503 -0.0025 -0.0009 -0.0230 690 VAL A O 5294 C CB . VAL A 636 ? 0.2248 0.2379 0.2525 -0.0008 -0.0037 -0.0220 690 VAL A CB 5295 C CG1 . VAL A 636 ? 0.2135 0.2281 0.2491 -0.0028 -0.0037 -0.0210 690 VAL A CG1 5296 C CG2 . VAL A 636 ? 0.1959 0.2081 0.2163 -0.0013 -0.0020 -0.0205 690 VAL A CG2 5297 N N . ILE A 637 ? 0.2240 0.2385 0.2609 0.0017 -0.0060 -0.0262 691 ILE A N 5298 C CA . ILE A 637 ? 0.2240 0.2399 0.2698 0.0019 -0.0077 -0.0278 691 ILE A CA 5299 C C . ILE A 637 ? 0.2461 0.2647 0.2935 0.0015 -0.0047 -0.0280 691 ILE A C 5300 O O . ILE A 637 ? 0.2476 0.2692 0.3034 0.0002 -0.0035 -0.0280 691 ILE A O 5301 C CB . ILE A 637 ? 0.2183 0.2305 0.2637 0.0051 -0.0131 -0.0304 691 ILE A CB 5302 C CG1 . ILE A 637 ? 0.2001 0.2089 0.2420 0.0062 -0.0162 -0.0303 691 ILE A CG1 5303 C CG2 . ILE A 637 ? 0.2692 0.2828 0.3257 0.0053 -0.0158 -0.0323 691 ILE A CG2 5304 C CD1 . ILE A 637 ? 0.2413 0.2516 0.2898 0.0038 -0.0163 -0.0289 691 ILE A CD1 5305 N N . TYR A 638 ? 0.2424 0.2601 0.2825 0.0026 -0.0035 -0.0283 692 TYR A N 5306 C CA . TYR A 638 ? 0.2494 0.2689 0.2908 0.0029 -0.0018 -0.0293 692 TYR A CA 5307 C C . TYR A 638 ? 0.2852 0.3065 0.3221 0.0018 0.0024 -0.0281 692 TYR A C 5308 O O . TYR A 638 ? 0.3049 0.3275 0.3424 0.0022 0.0037 -0.0290 692 TYR A O 5309 C CB . TYR A 638 ? 0.2441 0.2604 0.2817 0.0060 -0.0048 -0.0313 692 TYR A CB 5310 C CG . TYR A 638 ? 0.2326 0.2474 0.2759 0.0077 -0.0095 -0.0334 692 TYR A CG 5311 C CD1 . TYR A 638 ? 0.2540 0.2644 0.2930 0.0105 -0.0136 -0.0345 692 TYR A CD1 5312 C CD2 . TYR A 638 ? 0.2620 0.2797 0.3152 0.0069 -0.0099 -0.0344 692 TYR A CD2 5313 C CE1 . TYR A 638 ? 0.2539 0.2624 0.2977 0.0125 -0.0185 -0.0368 692 TYR A CE1 5314 C CE2 . TYR A 638 ? 0.2928 0.3090 0.3520 0.0086 -0.0147 -0.0366 692 TYR A CE2 5315 C CZ . TYR A 638 ? 0.2642 0.2757 0.3184 0.0115 -0.0192 -0.0380 692 TYR A CZ 5316 O OH . TYR A 638 ? 0.2828 0.2924 0.3427 0.0136 -0.0245 -0.0406 692 TYR A OH 5317 N N . ALA A 639 ? 0.3027 0.3237 0.3346 0.0007 0.0042 -0.0264 693 ALA A N 5318 C CA . ALA A 639 ? 0.3169 0.3394 0.3448 0.0000 0.0079 -0.0257 693 ALA A CA 5319 C C . ALA A 639 ? 0.3418 0.3677 0.3746 -0.0009 0.0107 -0.0256 693 ALA A C 5320 O O . ALA A 639 ? 0.3407 0.3683 0.3803 -0.0018 0.0110 -0.0250 693 ALA A O 5321 C CB . ALA A 639 ? 0.3340 0.3562 0.3577 -0.0012 0.0094 -0.0238 693 ALA A CB 5322 N N . PRO A 640 ? 0.3533 0.3801 0.3833 -0.0006 0.0128 -0.0261 694 PRO A N 5323 C CA . PRO A 640 ? 0.3764 0.4064 0.4102 -0.0013 0.0160 -0.0257 694 PRO A CA 5324 C C . PRO A 640 ? 0.3830 0.4144 0.4173 -0.0028 0.0189 -0.0235 694 PRO A C 5325 O O . PRO A 640 ? 0.3879 0.4179 0.4169 -0.0033 0.0192 -0.0224 694 PRO A O 5326 C CB . PRO A 640 ? 0.3818 0.4117 0.4105 -0.0005 0.0174 -0.0266 694 PRO A CB 5327 C CG . PRO A 640 ? 0.3639 0.3906 0.3883 0.0007 0.0145 -0.0277 694 PRO A CG 5328 C CD . PRO A 640 ? 0.3472 0.3721 0.3706 0.0003 0.0126 -0.0267 694 PRO A CD 5329 N N . SER A 641 ? 0.3950 0.4289 0.4361 -0.0034 0.0209 -0.0228 695 SER A N 5330 C CA . SER A 641 ? 0.4138 0.4491 0.4554 -0.0044 0.0247 -0.0204 695 SER A CA 5331 C C . SER A 641 ? 0.4350 0.4703 0.4694 -0.0036 0.0276 -0.0202 695 SER A C 5332 O O . SER A 641 ? 0.4241 0.4599 0.4572 -0.0026 0.0278 -0.0219 695 SER A O 5333 C CB . SER A 641 ? 0.3840 0.4220 0.4353 -0.0049 0.0267 -0.0196 695 SER A CB 5334 O OG . SER A 641 ? 0.4400 0.4795 0.4904 -0.0050 0.0315 -0.0175 695 SER A OG 5335 N N . SER A 642 ? 0.4608 0.4954 0.4905 -0.0040 0.0295 -0.0184 696 SER A N 5336 C CA . SER A 642 ? 0.5355 0.5698 0.5584 -0.0031 0.0321 -0.0182 696 SER A CA 5337 C C . SER A 642 ? 0.5691 0.6059 0.5953 -0.0023 0.0360 -0.0176 696 SER A C 5338 O O . SER A 642 ? 0.5911 0.6279 0.6128 -0.0009 0.0375 -0.0185 696 SER A O 5339 C CB . SER A 642 ? 0.5342 0.5671 0.5523 -0.0035 0.0332 -0.0161 696 SER A CB 5340 O OG . SER A 642 ? 0.6021 0.6330 0.6119 -0.0026 0.0323 -0.0170 696 SER A OG 5341 N N . HIS A 643 ? 0.6177 0.6564 0.6523 -0.0031 0.0376 -0.0162 697 HIS A N 5342 C CA . HIS A 643 ? 0.6598 0.7009 0.6985 -0.0025 0.0422 -0.0148 697 HIS A CA 5343 C C . HIS A 643 ? 0.6791 0.7227 0.7258 -0.0022 0.0421 -0.0164 697 HIS A C 5344 O O . HIS A 643 ? 0.6821 0.7277 0.7316 -0.0013 0.0460 -0.0156 697 HIS A O 5345 C CB . HIS A 643 ? 0.6641 0.7058 0.7077 -0.0035 0.0451 -0.0116 697 HIS A CB 5346 C CG . HIS A 643 ? 0.6748 0.7141 0.7101 -0.0033 0.0465 -0.0097 697 HIS A CG 5347 N ND1 . HIS A 643 ? 0.7000 0.7384 0.7267 -0.0014 0.0495 -0.0091 697 HIS A ND1 5348 C CD2 . HIS A 643 ? 0.6828 0.7205 0.7172 -0.0045 0.0450 -0.0083 697 HIS A CD2 5349 C CE1 . HIS A 643 ? 0.7031 0.7391 0.7237 -0.0015 0.0497 -0.0075 697 HIS A CE1 5350 N NE2 . HIS A 643 ? 0.6867 0.7224 0.7120 -0.0035 0.0472 -0.0069 697 HIS A NE2 5351 N N . ASN A 644 ? 0.6964 0.7396 0.7466 -0.0027 0.0375 -0.0186 698 ASN A N 5352 C CA . ASN A 644 ? 0.7129 0.7569 0.7650 -0.0017 0.0359 -0.0212 698 ASN A CA 5353 C C . ASN A 644 ? 0.7113 0.7543 0.7543 -0.0003 0.0368 -0.0223 698 ASN A C 5354 O O . ASN A 644 ? 0.7156 0.7566 0.7507 -0.0002 0.0369 -0.0216 698 ASN A O 5355 C CB . ASN A 644 ? 0.7019 0.7443 0.7560 -0.0020 0.0305 -0.0233 698 ASN A CB 5356 C CG . ASN A 644 ? 0.7493 0.7898 0.7967 -0.0007 0.0280 -0.0256 698 ASN A CG 5357 O OD1 . ASN A 644 ? 0.7954 0.8365 0.8459 0.0001 0.0266 -0.0276 698 ASN A OD1 5358 N ND2 . ASN A 644 ? 0.7103 0.7485 0.7492 -0.0007 0.0274 -0.0255 698 ASN A ND2 5359 N N . GLU A 649 ? 0.3953 0.4368 0.4833 -0.0056 0.0188 -0.0227 703 GLU A N 5360 C CA . GLU A 649 ? 0.3794 0.4191 0.4729 -0.0054 0.0134 -0.0241 703 GLU A CA 5361 C C . GLU A 649 ? 0.3910 0.4269 0.4744 -0.0048 0.0103 -0.0246 703 GLU A C 5362 O O . GLU A 649 ? 0.4021 0.4373 0.4765 -0.0052 0.0128 -0.0231 703 GLU A O 5363 C CB . GLU A 649 ? 0.4252 0.4662 0.5289 -0.0072 0.0143 -0.0221 703 GLU A CB 5364 C CG . GLU A 649 ? 0.4467 0.4914 0.5634 -0.0080 0.0174 -0.0211 703 GLU A CG 5365 C CD . GLU A 649 ? 0.5485 0.5943 0.6737 -0.0069 0.0143 -0.0240 703 GLU A CD 5366 O OE1 . GLU A 649 ? 0.5980 0.6472 0.7309 -0.0073 0.0181 -0.0232 703 GLU A OE1 5367 O OE2 . GLU A 649 ? 0.5532 0.5964 0.6777 -0.0055 0.0083 -0.0269 703 GLU A OE2 5368 N N . SER A 650 ? 0.3514 0.3847 0.4365 -0.0036 0.0047 -0.0267 704 SER A N 5369 C CA . SER A 650 ? 0.3053 0.3350 0.3831 -0.0029 0.0014 -0.0270 704 SER A CA 5370 C C . SER A 650 ? 0.2801 0.3099 0.3580 -0.0048 0.0032 -0.0243 704 SER A C 5371 O O . SER A 650 ? 0.3124 0.3448 0.3972 -0.0065 0.0065 -0.0224 704 SER A O 5372 C CB . SER A 650 ? 0.3152 0.3424 0.3974 -0.0010 -0.0046 -0.0296 704 SER A CB 5373 O OG . SER A 650 ? 0.3600 0.3866 0.4410 0.0010 -0.0064 -0.0321 704 SER A OG 5374 N N . PHE A 651 ? 0.2414 0.2681 0.3123 -0.0044 0.0011 -0.0241 705 PHE A N 5375 C CA . PHE A 651 ? 0.2140 0.2408 0.2827 -0.0061 0.0034 -0.0214 705 PHE A CA 5376 C C . PHE A 651 ? 0.2162 0.2454 0.2814 -0.0073 0.0092 -0.0193 705 PHE A C 5377 O O . PHE A 651 ? 0.2094 0.2405 0.2790 -0.0088 0.0126 -0.0171 705 PHE A O 5378 C CB . PHE A 651 ? 0.2221 0.2493 0.3005 -0.0074 0.0022 -0.0205 705 PHE A CB 5379 C CG . PHE A 651 ? 0.2288 0.2528 0.3088 -0.0059 -0.0039 -0.0226 705 PHE A CG 5380 C CD1 . PHE A 651 ? 0.2126 0.2332 0.2832 -0.0048 -0.0063 -0.0229 705 PHE A CD1 5381 C CD2 . PHE A 651 ? 0.2266 0.2508 0.3173 -0.0055 -0.0074 -0.0244 705 PHE A CD2 5382 C CE1 . PHE A 651 ? 0.2512 0.2685 0.3223 -0.0030 -0.0119 -0.0249 705 PHE A CE1 5383 C CE2 . PHE A 651 ? 0.2090 0.2298 0.3007 -0.0037 -0.0136 -0.0266 705 PHE A CE2 5384 C CZ . PHE A 651 ? 0.2359 0.2531 0.3173 -0.0023 -0.0158 -0.0269 705 PHE A CZ 5385 N N . PRO A 652 ? 0.2140 0.2427 0.2709 -0.0063 0.0102 -0.0201 706 PRO A N 5386 C CA . PRO A 652 ? 0.2160 0.2467 0.2696 -0.0069 0.0151 -0.0187 706 PRO A CA 5387 C C . PRO A 652 ? 0.2284 0.2589 0.2781 -0.0081 0.0178 -0.0160 706 PRO A C 5388 O O . PRO A 652 ? 0.2305 0.2627 0.2800 -0.0085 0.0221 -0.0144 706 PRO A O 5389 C CB . PRO A 652 ? 0.2254 0.2549 0.2705 -0.0055 0.0145 -0.0203 706 PRO A CB 5390 C CG . PRO A 652 ? 0.2204 0.2467 0.2624 -0.0044 0.0100 -0.0215 706 PRO A CG 5391 C CD . PRO A 652 ? 0.2135 0.2398 0.2645 -0.0044 0.0071 -0.0223 706 PRO A CD 5392 N N . GLY A 653 ? 0.2223 0.2504 0.2683 -0.0083 0.0155 -0.0157 707 GLY A N 5393 C CA . GLY A 653 ? 0.2223 0.2498 0.2642 -0.0093 0.0178 -0.0133 707 GLY A CA 5394 C C . GLY A 653 ? 0.2370 0.2663 0.2869 -0.0106 0.0207 -0.0109 707 GLY A C 5395 O O . GLY A 653 ? 0.2290 0.2591 0.2766 -0.0109 0.0250 -0.0087 707 GLY A O 5396 N N . ILE A 654 ? 0.2114 0.2410 0.2705 -0.0110 0.0183 -0.0114 708 ILE A N 5397 C CA . ILE A 654 ? 0.2149 0.2461 0.2834 -0.0124 0.0208 -0.0091 708 ILE A CA 5398 C C . ILE A 654 ? 0.2301 0.2644 0.3033 -0.0123 0.0252 -0.0085 708 ILE A C 5399 O O . ILE A 654 ? 0.2382 0.2739 0.3133 -0.0129 0.0300 -0.0056 708 ILE A O 5400 C CB . ILE A 654 ? 0.2160 0.2468 0.2946 -0.0128 0.0165 -0.0102 708 ILE A CB 5401 C CG1 . ILE A 654 ? 0.2317 0.2592 0.3055 -0.0125 0.0120 -0.0110 708 ILE A CG1 5402 C CG2 . ILE A 654 ? 0.2345 0.2673 0.3249 -0.0144 0.0196 -0.0075 708 ILE A CG2 5403 C CD1 . ILE A 654 ? 0.2367 0.2630 0.3191 -0.0122 0.0065 -0.0130 708 ILE A CD1 5404 N N . TYR A 655 ? 0.2153 0.2506 0.2894 -0.0113 0.0236 -0.0110 709 TYR A N 5405 C CA . TYR A 655 ? 0.2391 0.2773 0.3177 -0.0110 0.0275 -0.0107 709 TYR A CA 5406 C C . TYR A 655 ? 0.2470 0.2856 0.3173 -0.0105 0.0328 -0.0087 709 TYR A C 5407 O O . TYR A 655 ? 0.2466 0.2871 0.3207 -0.0106 0.0377 -0.0064 709 TYR A O 5408 C CB . TYR A 655 ? 0.2288 0.2673 0.3075 -0.0097 0.0245 -0.0140 709 TYR A CB 5409 C CG . TYR A 655 ? 0.2468 0.2883 0.3300 -0.0092 0.0283 -0.0139 709 TYR A CG 5410 C CD1 . TYR A 655 ? 0.2795 0.3235 0.3756 -0.0097 0.0287 -0.0138 709 TYR A CD1 5411 C CD2 . TYR A 655 ? 0.2768 0.3188 0.3517 -0.0082 0.0317 -0.0137 709 TYR A CD2 5412 C CE1 . TYR A 655 ? 0.3244 0.3713 0.4252 -0.0092 0.0326 -0.0135 709 TYR A CE1 5413 C CE2 . TYR A 655 ? 0.3043 0.3491 0.3832 -0.0076 0.0354 -0.0136 709 TYR A CE2 5414 C CZ . TYR A 655 ? 0.3414 0.3887 0.4332 -0.0081 0.0360 -0.0133 709 TYR A CZ 5415 O OH . TYR A 655 ? 0.3399 0.3900 0.4364 -0.0074 0.0398 -0.0131 709 TYR A OH 5416 N N . ASP A 656 ? 0.2552 0.2918 0.3140 -0.0097 0.0318 -0.0097 710 ASP A N 5417 C CA . ASP A 656 ? 0.2545 0.2908 0.3046 -0.0088 0.0357 -0.0084 710 ASP A CA 5418 C C . ASP A 656 ? 0.2665 0.3021 0.3154 -0.0094 0.0390 -0.0050 710 ASP A C 5419 O O . ASP A 656 ? 0.2610 0.2971 0.3074 -0.0086 0.0438 -0.0030 710 ASP A O 5420 C CB . ASP A 656 ? 0.2475 0.2817 0.2871 -0.0079 0.0330 -0.0104 710 ASP A CB 5421 C CG . ASP A 656 ? 0.2998 0.3348 0.3392 -0.0069 0.0314 -0.0132 710 ASP A CG 5422 O OD1 . ASP A 656 ? 0.3146 0.3518 0.3603 -0.0067 0.0329 -0.0136 710 ASP A OD1 5423 O OD2 . ASP A 656 ? 0.3330 0.3662 0.3660 -0.0063 0.0288 -0.0149 710 ASP A OD2 5424 N N . ALA A 657 ? 0.2479 0.2820 0.2988 -0.0106 0.0366 -0.0042 711 ALA A N 5425 C CA . ALA A 657 ? 0.2768 0.3100 0.3273 -0.0112 0.0397 -0.0009 711 ALA A CA 5426 C C . ALA A 657 ? 0.2727 0.3082 0.3331 -0.0117 0.0444 0.0017 711 ALA A C 5427 O O . ALA A 657 ? 0.2854 0.3206 0.3435 -0.0112 0.0493 0.0049 711 ALA A O 5428 C CB . ALA A 657 ? 0.2606 0.2917 0.3117 -0.0124 0.0357 -0.0008 711 ALA A CB 5429 N N . LEU A 658 ? 0.2451 0.2828 0.3163 -0.0123 0.0430 0.0005 712 LEU A N 5430 C CA . LEU A 658 ? 0.2612 0.3015 0.3440 -0.0128 0.0474 0.0029 712 LEU A CA 5431 C C . LEU A 658 ? 0.2908 0.3333 0.3726 -0.0113 0.0524 0.0034 712 LEU A C 5432 O O . LEU A 658 ? 0.2944 0.3387 0.3837 -0.0114 0.0576 0.0063 712 LEU A O 5433 C CB . LEU A 658 ? 0.2455 0.2872 0.3415 -0.0140 0.0433 0.0011 712 LEU A CB 5434 C CG . LEU A 658 ? 0.2629 0.3028 0.3643 -0.0155 0.0392 0.0014 712 LEU A CG 5435 C CD1 . LEU A 658 ? 0.2369 0.2776 0.3488 -0.0159 0.0336 -0.0017 712 LEU A CD1 5436 C CD2 . LEU A 658 ? 0.2655 0.3057 0.3738 -0.0167 0.0437 0.0057 712 LEU A CD2 5437 N N . PHE A 659 ? 0.2971 0.3392 0.3701 -0.0100 0.0510 0.0008 713 PHE A N 5438 C CA . PHE A 659 ? 0.3269 0.3709 0.3993 -0.0084 0.0545 0.0004 713 PHE A CA 5439 C C . PHE A 659 ? 0.3342 0.3778 0.4011 -0.0069 0.0610 0.0037 713 PHE A C 5440 O O . PHE A 659 ? 0.3394 0.3803 0.3953 -0.0061 0.0614 0.0044 713 PHE A O 5441 C CB . PHE A 659 ? 0.3216 0.3650 0.3855 -0.0072 0.0512 -0.0032 713 PHE A CB 5442 C CG . PHE A 659 ? 0.3413 0.3868 0.4063 -0.0057 0.0539 -0.0041 713 PHE A CG 5443 C CD1 . PHE A 659 ? 0.4010 0.4491 0.4767 -0.0062 0.0525 -0.0058 713 PHE A CD1 5444 C CD2 . PHE A 659 ? 0.3789 0.4238 0.4347 -0.0036 0.0578 -0.0034 713 PHE A CD2 5445 C CE1 . PHE A 659 ? 0.4536 0.5039 0.5308 -0.0047 0.0551 -0.0066 713 PHE A CE1 5446 C CE2 . PHE A 659 ? 0.3840 0.4310 0.4408 -0.0020 0.0605 -0.0043 713 PHE A CE2 5447 C CZ . PHE A 659 ? 0.4409 0.4906 0.5085 -0.0027 0.0593 -0.0058 713 PHE A CZ 5448 N N . ASP A 660 ? 0.3592 0.4053 0.4342 -0.0065 0.0661 0.0058 714 ASP A N 5449 C CA . ASP A 660 ? 0.3847 0.4303 0.4546 -0.0046 0.0732 0.0093 714 ASP A CA 5450 C C . ASP A 660 ? 0.3841 0.4269 0.4495 -0.0049 0.0747 0.0125 714 ASP A C 5451 O O . ASP A 660 ? 0.3938 0.4343 0.4484 -0.0028 0.0784 0.0145 714 ASP A O 5452 C CB . ASP A 660 ? 0.3977 0.4421 0.4544 -0.0018 0.0737 0.0074 714 ASP A CB 5453 C CG . ASP A 660 ? 0.4494 0.4937 0.5017 0.0009 0.0811 0.0104 714 ASP A CG 5454 O OD1 . ASP A 660 ? 0.4658 0.5124 0.5281 0.0008 0.0862 0.0133 714 ASP A OD1 5455 O OD2 . ASP A 660 ? 0.5249 0.5666 0.5638 0.0034 0.0818 0.0098 714 ASP A OD2 5456 N N . ILE A 661 ? 0.3672 0.4099 0.4407 -0.0074 0.0716 0.0130 715 ILE A N 5457 C CA . ILE A 661 ? 0.3557 0.3955 0.4247 -0.0079 0.0723 0.0157 715 ILE A CA 5458 C C . ILE A 661 ? 0.3979 0.4374 0.4681 -0.0066 0.0803 0.0208 715 ILE A C 5459 O O . ILE A 661 ? 0.3897 0.4261 0.4506 -0.0056 0.0823 0.0231 715 ILE A O 5460 C CB . ILE A 661 ? 0.3436 0.3833 0.4216 -0.0106 0.0673 0.0151 715 ILE A CB 5461 C CG1 . ILE A 661 ? 0.3410 0.3773 0.4117 -0.0109 0.0669 0.0171 715 ILE A CG1 5462 C CG2 . ILE A 661 ? 0.3253 0.3679 0.4209 -0.0123 0.0691 0.0168 715 ILE A CG2 5463 C CD1 . ILE A 661 ? 0.3201 0.3553 0.3938 -0.0130 0.0604 0.0152 715 ILE A CD1 5464 N N . GLU A 662 ? 0.4165 0.4590 0.4980 -0.0067 0.0847 0.0225 716 GLU A N 5465 C CA . GLU A 662 ? 0.4769 0.5194 0.5611 -0.0053 0.0930 0.0277 716 GLU A CA 5466 C C . GLU A 662 ? 0.5032 0.5432 0.5717 -0.0015 0.0979 0.0291 716 GLU A C 5467 O O . GLU A 662 ? 0.5247 0.5633 0.5918 0.0000 0.1047 0.0337 716 GLU A O 5468 C CB . GLU A 662 ? 0.4693 0.5159 0.5703 -0.0062 0.0968 0.0292 716 GLU A CB 5469 C CG . GLU A 662 ? 0.5171 0.5663 0.6179 -0.0045 0.0979 0.0267 716 GLU A CG 5470 C CD . GLU A 662 ? 0.5672 0.6183 0.6719 -0.0061 0.0900 0.0212 716 GLU A CD 5471 O OE1 . GLU A 662 ? 0.5223 0.5720 0.6252 -0.0078 0.0833 0.0187 716 GLU A OE1 5472 O OE2 . GLU A 662 ? 0.6041 0.6580 0.7134 -0.0053 0.0909 0.0196 716 GLU A OE2 5473 N N . SER A 663 ? 0.5183 0.5573 0.5749 0.0000 0.0944 0.0252 717 SER A N 5474 C CA A SER A 663 ? 0.5286 0.5647 0.5696 0.0039 0.0976 0.0257 717 SER A CA 5475 C CA B SER A 663 ? 0.5328 0.5689 0.5739 0.0039 0.0978 0.0258 717 SER A CA 5476 C C . SER A 663 ? 0.5446 0.5763 0.5719 0.0047 0.0945 0.0251 717 SER A C 5477 O O . SER A 663 ? 0.5572 0.5857 0.5710 0.0082 0.0969 0.0258 717 SER A O 5478 C CB A SER A 663 ? 0.5319 0.5694 0.5684 0.0055 0.0957 0.0216 717 SER A CB 5479 C CB B SER A 663 ? 0.5352 0.5728 0.5721 0.0056 0.0964 0.0220 717 SER A CB 5480 O OG A SER A 663 ? 0.4967 0.5380 0.5445 0.0053 0.0991 0.0221 717 SER A OG 5481 O OG B SER A 663 ? 0.5232 0.5594 0.5522 0.0051 0.0892 0.0176 717 SER A OG 5482 N N . LYS A 664 ? 0.5379 0.5692 0.5682 0.0017 0.0888 0.0238 718 LYS A N 5483 C CA . LYS A 664 ? 0.5536 0.5809 0.5719 0.0023 0.0854 0.0231 718 LYS A CA 5484 C C . LYS A 664 ? 0.5679 0.5921 0.5812 0.0040 0.0908 0.0279 718 LYS A C 5485 O O . LYS A 664 ? 0.5624 0.5876 0.5854 0.0030 0.0953 0.0318 718 LYS A O 5486 C CB . LYS A 664 ? 0.5435 0.5712 0.5670 -0.0010 0.0785 0.0208 718 LYS A CB 5487 C CG . LYS A 664 ? 0.5605 0.5906 0.5875 -0.0024 0.0730 0.0162 718 LYS A CG 5488 C CD . LYS A 664 ? 0.6033 0.6315 0.6174 -0.0004 0.0699 0.0128 718 LYS A CD 5489 C CE . LYS A 664 ? 0.6312 0.6620 0.6487 -0.0010 0.0663 0.0089 718 LYS A CE 5490 N NZ . LYS A 664 ? 0.5960 0.6271 0.6181 -0.0036 0.0602 0.0066 718 LYS A NZ 5491 N N . VAL A 665 ? 0.5809 0.6010 0.5791 0.0068 0.0904 0.0275 719 VAL A N 5492 C CA . VAL A 665 ? 0.5888 0.6052 0.5800 0.0094 0.0960 0.0321 719 VAL A CA 5493 C C . VAL A 665 ? 0.5827 0.5974 0.5766 0.0070 0.0942 0.0341 719 VAL A C 5494 O O . VAL A 665 ? 0.5944 0.6071 0.5884 0.0080 0.0994 0.0387 719 VAL A O 5495 C CB . VAL A 665 ? 0.6054 0.6174 0.5786 0.0140 0.0963 0.0310 719 VAL A CB 5496 C CG1 . VAL A 665 ? 0.6271 0.6401 0.5972 0.0174 0.1005 0.0306 719 VAL A CG1 5497 C CG2 . VAL A 665 ? 0.6047 0.6154 0.5706 0.0134 0.0883 0.0262 719 VAL A CG2 5498 N N . ASP A 666 ? 0.5528 0.5682 0.5491 0.0042 0.0870 0.0307 720 ASP A N 5499 C CA . ASP A 666 ? 0.5310 0.5447 0.5297 0.0019 0.0845 0.0321 720 ASP A CA 5500 C C . ASP A 666 ? 0.5091 0.5266 0.5235 -0.0021 0.0812 0.0309 720 ASP A C 5501 O O . ASP A 666 ? 0.4794 0.4977 0.4944 -0.0038 0.0747 0.0270 720 ASP A O 5502 C CB . ASP A 666 ? 0.5397 0.5503 0.5263 0.0027 0.0787 0.0289 720 ASP A CB 5503 C CG . ASP A 666 ? 0.5425 0.5509 0.5294 0.0010 0.0763 0.0303 720 ASP A CG 5504 O OD1 . ASP A 666 ? 0.5496 0.5592 0.5476 -0.0013 0.0777 0.0330 720 ASP A OD1 5505 O OD2 . ASP A 666 ? 0.5953 0.6008 0.5718 0.0021 0.0726 0.0285 720 ASP A OD2 5506 N N . PRO A 667 ? 0.4906 0.5102 0.5179 -0.0034 0.0857 0.0343 721 PRO A N 5507 C CA . PRO A 667 ? 0.4693 0.4924 0.5121 -0.0069 0.0821 0.0329 721 PRO A CA 5508 C C . PRO A 667 ? 0.4554 0.4771 0.4998 -0.0094 0.0758 0.0315 721 PRO A C 5509 O O . PRO A 667 ? 0.4292 0.4528 0.4805 -0.0115 0.0702 0.0281 721 PRO A O 5510 C CB . PRO A 667 ? 0.4792 0.5040 0.5349 -0.0075 0.0887 0.0375 721 PRO A CB 5511 C CG . PRO A 667 ? 0.4950 0.5165 0.5415 -0.0045 0.0957 0.0421 721 PRO A CG 5512 C CD . PRO A 667 ? 0.5080 0.5266 0.5362 -0.0015 0.0941 0.0397 721 PRO A CD 5513 N N . SER A 668 ? 0.4397 0.4578 0.4775 -0.0089 0.0767 0.0339 722 SER A N 5514 C CA . SER A 668 ? 0.4515 0.4680 0.4898 -0.0109 0.0709 0.0327 722 SER A CA 5515 C C . SER A 668 ? 0.4361 0.4527 0.4675 -0.0109 0.0640 0.0275 722 SER A C 5516 O O . SER A 668 ? 0.4119 0.4294 0.4489 -0.0130 0.0585 0.0250 722 SER A O 5517 C CB . SER A 668 ? 0.4635 0.4758 0.4928 -0.0096 0.0729 0.0358 722 SER A CB 5518 O OG . SER A 668 ? 0.5015 0.5126 0.5336 -0.0117 0.0678 0.0350 722 SER A OG 5519 N N . LYS A 669 ? 0.4283 0.4437 0.4472 -0.0085 0.0645 0.0261 723 LYS A N 5520 C CA . LYS A 669 ? 0.4302 0.4456 0.4429 -0.0083 0.0589 0.0216 723 LYS A CA 5521 C C . LYS A 669 ? 0.3963 0.4153 0.4173 -0.0096 0.0564 0.0185 723 LYS A C 5522 O O . LYS A 669 ? 0.3889 0.4084 0.4109 -0.0107 0.0508 0.0152 723 LYS A O 5523 C CB . LYS A 669 ? 0.4542 0.4675 0.4528 -0.0052 0.0602 0.0208 723 LYS A CB 5524 C CG . LYS A 669 ? 0.5063 0.5196 0.4990 -0.0050 0.0546 0.0162 723 LYS A CG 5525 C CD . LYS A 669 ? 0.6007 0.6110 0.5796 -0.0020 0.0548 0.0153 723 LYS A CD 5526 C CE . LYS A 669 ? 0.6186 0.6295 0.5941 -0.0019 0.0498 0.0108 723 LYS A CE 5527 N NZ . LYS A 669 ? 0.6935 0.7021 0.6575 0.0010 0.0497 0.0093 723 LYS A NZ 5528 N N . ALA A 670 ? 0.3710 0.3924 0.3974 -0.0090 0.0607 0.0195 724 ALA A N 5529 C CA . ALA A 670 ? 0.3423 0.3671 0.3760 -0.0098 0.0588 0.0167 724 ALA A CA 5530 C C . ALA A 670 ? 0.3380 0.3641 0.3841 -0.0124 0.0548 0.0159 724 ALA A C 5531 O O . ALA A 670 ? 0.2925 0.3195 0.3401 -0.0131 0.0497 0.0124 724 ALA A O 5532 C CB . ALA A 670 ? 0.3511 0.3780 0.3893 -0.0086 0.0646 0.0185 724 ALA A CB 5533 N N . TRP A 671 ? 0.3016 0.3276 0.3564 -0.0137 0.0571 0.0192 725 TRP A N 5534 C CA . TRP A 671 ? 0.3024 0.3293 0.3691 -0.0160 0.0530 0.0183 725 TRP A CA 5535 C C . TRP A 671 ? 0.2938 0.3183 0.3556 -0.0167 0.0469 0.0163 725 TRP A C 5536 O O . TRP A 671 ? 0.2861 0.3111 0.3540 -0.0177 0.0417 0.0138 725 TRP A O 5537 C CB . TRP A 671 ? 0.2959 0.3235 0.3744 -0.0172 0.0572 0.0224 725 TRP A CB 5538 C CG . TRP A 671 ? 0.3002 0.3312 0.3882 -0.0169 0.0614 0.0232 725 TRP A CG 5539 C CD1 . TRP A 671 ? 0.3029 0.3345 0.3892 -0.0154 0.0688 0.0264 725 TRP A CD1 5540 C CD2 . TRP A 671 ? 0.3176 0.3514 0.4171 -0.0180 0.0584 0.0206 725 TRP A CD2 5541 N NE1 . TRP A 671 ? 0.3244 0.3595 0.4214 -0.0156 0.0707 0.0260 725 TRP A NE1 5542 C CE2 . TRP A 671 ? 0.3074 0.3440 0.4130 -0.0172 0.0642 0.0224 725 TRP A CE2 5543 C CE3 . TRP A 671 ? 0.2785 0.3126 0.3835 -0.0191 0.0512 0.0167 725 TRP A CE3 5544 C CZ2 . TRP A 671 ? 0.3297 0.3694 0.4472 -0.0178 0.0629 0.0204 725 TRP A CZ2 5545 C CZ3 . TRP A 671 ? 0.2970 0.3340 0.4135 -0.0195 0.0497 0.0147 725 TRP A CZ3 5546 C CH2 . TRP A 671 ? 0.2899 0.3298 0.4129 -0.0190 0.0555 0.0166 725 TRP A CH2 5547 N N . GLY A 672 ? 0.3181 0.3398 0.3687 -0.0158 0.0474 0.0173 726 GLY A N 5548 C CA . GLY A 672 ? 0.2903 0.3098 0.3348 -0.0161 0.0418 0.0151 726 GLY A CA 5549 C C . GLY A 672 ? 0.2857 0.3062 0.3269 -0.0156 0.0375 0.0108 726 GLY A C 5550 O O . GLY A 672 ? 0.2700 0.2898 0.3122 -0.0161 0.0323 0.0085 726 GLY A O 5551 N N . GLU A 673 ? 0.2716 0.2933 0.3083 -0.0142 0.0398 0.0099 727 GLU A N 5552 C CA . GLU A 673 ? 0.2835 0.3059 0.3171 -0.0137 0.0361 0.0061 727 GLU A CA 5553 C C . GLU A 673 ? 0.2713 0.2959 0.3156 -0.0145 0.0336 0.0043 727 GLU A C 5554 O O . GLU A 673 ? 0.2634 0.2876 0.3068 -0.0144 0.0290 0.0014 727 GLU A O 5555 C CB . GLU A 673 ? 0.2851 0.3080 0.3108 -0.0119 0.0388 0.0055 727 GLU A CB 5556 C CG . GLU A 673 ? 0.3118 0.3353 0.3345 -0.0112 0.0354 0.0017 727 GLU A CG 5557 C CD . GLU A 673 ? 0.3597 0.3813 0.3767 -0.0112 0.0308 -0.0002 727 GLU A CD 5558 O OE1 . GLU A 673 ? 0.3379 0.3574 0.3511 -0.0115 0.0300 0.0009 727 GLU A OE1 5559 O OE2 . GLU A 673 ? 0.3545 0.3766 0.3708 -0.0108 0.0280 -0.0029 727 GLU A OE2 5560 N N . VAL A 674 ? 0.2604 0.2869 0.3148 -0.0152 0.0365 0.0061 728 VAL A N 5561 C CA . VAL A 674 ? 0.2566 0.2847 0.3220 -0.0160 0.0334 0.0042 728 VAL A CA 5562 C C . VAL A 674 ? 0.2504 0.2766 0.3185 -0.0169 0.0279 0.0031 728 VAL A C 5563 O O . VAL A 674 ? 0.2250 0.2509 0.2947 -0.0165 0.0231 0.0001 728 VAL A O 5564 C CB . VAL A 674 ? 0.2709 0.3014 0.3486 -0.0168 0.0375 0.0066 728 VAL A CB 5565 C CG1 . VAL A 674 ? 0.2510 0.2827 0.3412 -0.0177 0.0332 0.0046 728 VAL A CG1 5566 C CG2 . VAL A 674 ? 0.2564 0.2891 0.3318 -0.0156 0.0426 0.0072 728 VAL A CG2 5567 N N . LYS A 675 ? 0.2348 0.2593 0.3031 -0.0177 0.0288 0.0056 729 LYS A N 5568 C CA . LYS A 675 ? 0.2329 0.2553 0.3035 -0.0183 0.0236 0.0047 729 LYS A CA 5569 C C . LYS A 675 ? 0.2386 0.2591 0.2988 -0.0172 0.0195 0.0019 729 LYS A C 5570 O O . LYS A 675 ? 0.2267 0.2460 0.2887 -0.0169 0.0143 -0.0003 729 LYS A O 5571 C CB B LYS A 675 ? 0.2442 0.2650 0.3159 -0.0194 0.0256 0.0080 729 LYS A CB 5572 C CB C LYS A 675 ? 0.2416 0.2625 0.3136 -0.0194 0.0257 0.0081 729 LYS A CB 5573 C CG B LYS A 675 ? 0.2400 0.2625 0.3249 -0.0207 0.0291 0.0108 729 LYS A CG 5574 C CG C LYS A 675 ? 0.2390 0.2616 0.3235 -0.0206 0.0296 0.0110 729 LYS A CG 5575 C CD B LYS A 675 ? 0.2837 0.3045 0.3691 -0.0215 0.0322 0.0148 729 LYS A CD 5576 C CD C LYS A 675 ? 0.2613 0.2821 0.3485 -0.0217 0.0313 0.0145 729 LYS A CD 5577 C CE B LYS A 675 ? 0.2497 0.2680 0.3366 -0.0223 0.0269 0.0140 729 LYS A CE 5578 C CE C LYS A 675 ? 0.2570 0.2764 0.3336 -0.0209 0.0366 0.0176 729 LYS A CE 5579 N NZ B LYS A 675 ? 0.3283 0.3452 0.4198 -0.0234 0.0301 0.0181 729 LYS A NZ 5580 N NZ C LYS A 675 ? 0.2702 0.2877 0.3503 -0.0219 0.0385 0.0213 729 LYS A NZ 5581 N N . ARG A 676 ? 0.2285 0.2485 0.2779 -0.0164 0.0217 0.0022 730 ARG A N 5582 C CA . ARG A 676 ? 0.2246 0.2431 0.2653 -0.0153 0.0182 -0.0001 730 ARG A CA 5583 C C . ARG A 676 ? 0.2174 0.2367 0.2601 -0.0144 0.0152 -0.0033 730 ARG A C 5584 O O . ARG A 676 ? 0.2034 0.2211 0.2440 -0.0136 0.0110 -0.0053 730 ARG A O 5585 C CB . ARG A 676 ? 0.2342 0.2520 0.2641 -0.0145 0.0207 0.0003 730 ARG A CB 5586 C CG . ARG A 676 ? 0.2551 0.2710 0.2772 -0.0136 0.0171 -0.0016 730 ARG A CG 5587 C CD . ARG A 676 ? 0.2767 0.2919 0.2891 -0.0128 0.0191 -0.0013 730 ARG A CD 5588 N NE . ARG A 676 ? 0.2813 0.2981 0.2919 -0.0119 0.0208 -0.0026 730 ARG A NE 5589 C CZ . ARG A 676 ? 0.3118 0.3287 0.3202 -0.0112 0.0185 -0.0051 730 ARG A CZ 5590 N NH1 . ARG A 676 ? 0.3312 0.3467 0.3390 -0.0110 0.0148 -0.0064 730 ARG A NH1 5591 N NH2 . ARG A 676 ? 0.3336 0.3519 0.3407 -0.0104 0.0200 -0.0062 730 ARG A NH2 5592 N N . GLN A 677 ? 0.2189 0.2406 0.2653 -0.0143 0.0176 -0.0036 731 GLN A N 5593 C CA . GLN A 677 ? 0.2176 0.2399 0.2653 -0.0132 0.0149 -0.0065 731 GLN A CA 5594 C C . GLN A 677 ? 0.2151 0.2368 0.2714 -0.0133 0.0106 -0.0080 731 GLN A C 5595 O O . GLN A 677 ? 0.2199 0.2406 0.2750 -0.0119 0.0068 -0.0106 731 GLN A O 5596 C CB . GLN A 677 ? 0.2106 0.2356 0.2606 -0.0131 0.0186 -0.0064 731 GLN A CB 5597 C CG . GLN A 677 ? 0.2188 0.2437 0.2585 -0.0124 0.0219 -0.0058 731 GLN A CG 5598 C CD . GLN A 677 ? 0.2719 0.2953 0.3035 -0.0112 0.0190 -0.0081 731 GLN A CD 5599 O OE1 . GLN A 677 ? 0.2548 0.2778 0.2878 -0.0105 0.0158 -0.0103 731 GLN A OE1 5600 N NE2 . GLN A 677 ? 0.3149 0.3371 0.3381 -0.0109 0.0202 -0.0076 731 GLN A NE2 5601 N N . ILE A 678 ? 0.2132 0.2356 0.2787 -0.0146 0.0112 -0.0063 732 ILE A N 5602 C CA . ILE A 678 ? 0.2170 0.2384 0.2911 -0.0145 0.0063 -0.0079 732 ILE A CA 5603 C C . ILE A 678 ? 0.2247 0.2428 0.2927 -0.0135 0.0017 -0.0093 732 ILE A C 5604 O O . ILE A 678 ? 0.2298 0.2463 0.2986 -0.0119 -0.0029 -0.0120 732 ILE A O 5605 C CB . ILE A 678 ? 0.1934 0.2158 0.2791 -0.0163 0.0080 -0.0055 732 ILE A CB 5606 C CG1 . ILE A 678 ? 0.2263 0.2521 0.3196 -0.0169 0.0123 -0.0044 732 ILE A CG1 5607 C CG2 . ILE A 678 ? 0.2131 0.2339 0.3077 -0.0161 0.0020 -0.0074 732 ILE A CG2 5608 C CD1 . ILE A 678 ? 0.2258 0.2529 0.3303 -0.0188 0.0160 -0.0009 732 ILE A CD1 5609 N N . TYR A 679 ? 0.2120 0.2288 0.2740 -0.0141 0.0031 -0.0073 733 TYR A N 5610 C CA . TYR A 679 ? 0.2263 0.2400 0.2818 -0.0131 -0.0007 -0.0084 733 TYR A CA 5611 C C . TYR A 679 ? 0.2184 0.2311 0.2657 -0.0110 -0.0025 -0.0108 733 TYR A C 5612 O O . TYR A 679 ? 0.2060 0.2163 0.2519 -0.0093 -0.0070 -0.0129 733 TYR A O 5613 C CB . TYR A 679 ? 0.2286 0.2415 0.2782 -0.0141 0.0018 -0.0058 733 TYR A CB 5614 C CG . TYR A 679 ? 0.2718 0.2822 0.3120 -0.0131 -0.0002 -0.0064 733 TYR A CG 5615 C CD1 . TYR A 679 ? 0.3055 0.3133 0.3458 -0.0119 -0.0051 -0.0080 733 TYR A CD1 5616 C CD2 . TYR A 679 ? 0.2731 0.2836 0.3047 -0.0132 0.0027 -0.0052 733 TYR A CD2 5617 C CE1 . TYR A 679 ? 0.2801 0.2857 0.3120 -0.0110 -0.0065 -0.0082 733 TYR A CE1 5618 C CE2 . TYR A 679 ? 0.2894 0.2978 0.3134 -0.0124 0.0010 -0.0055 733 TYR A CE2 5619 C CZ . TYR A 679 ? 0.2979 0.3040 0.3224 -0.0114 -0.0034 -0.0069 733 TYR A CZ 5620 O OH . TYR A 679 ? 0.3077 0.3117 0.3251 -0.0105 -0.0048 -0.0070 733 TYR A OH 5621 N N . VAL A 680 ? 0.2210 0.2352 0.2630 -0.0110 0.0008 -0.0105 734 VAL A N 5622 C CA . VAL A 680 ? 0.2186 0.2318 0.2534 -0.0091 -0.0005 -0.0126 734 VAL A CA 5623 C C . VAL A 680 ? 0.2205 0.2333 0.2593 -0.0074 -0.0038 -0.0151 734 VAL A C 5624 O O . VAL A 680 ? 0.2175 0.2278 0.2520 -0.0053 -0.0071 -0.0169 734 VAL A O 5625 C CB . VAL A 680 ? 0.2174 0.2324 0.2469 -0.0094 0.0035 -0.0119 734 VAL A CB 5626 C CG1 . VAL A 680 ? 0.2356 0.2498 0.2599 -0.0076 0.0024 -0.0139 734 VAL A CG1 5627 C CG2 . VAL A 680 ? 0.2313 0.2456 0.2544 -0.0101 0.0054 -0.0101 734 VAL A CG2 5628 N N . ALA A 681 ? 0.2161 0.2310 0.2635 -0.0082 -0.0030 -0.0153 735 ALA A N 5629 C CA . ALA A 681 ? 0.2220 0.2365 0.2738 -0.0066 -0.0063 -0.0178 735 ALA A CA 5630 C C . ALA A 681 ? 0.2178 0.2294 0.2728 -0.0053 -0.0118 -0.0194 735 ALA A C 5631 O O . ALA A 681 ? 0.2276 0.2369 0.2796 -0.0027 -0.0155 -0.0218 735 ALA A O 5632 C CB . ALA A 681 ? 0.2210 0.2387 0.2820 -0.0078 -0.0041 -0.0176 735 ALA A CB 5633 N N . ALA A 682 ? 0.1989 0.2105 0.2601 -0.0068 -0.0124 -0.0181 736 ALA A N 5634 C CA . ALA A 682 ? 0.2092 0.2178 0.2736 -0.0055 -0.0180 -0.0197 736 ALA A CA 5635 C C . ALA A 682 ? 0.2208 0.2259 0.2745 -0.0033 -0.0204 -0.0206 736 ALA A C 5636 O O . ALA A 682 ? 0.2196 0.2217 0.2719 -0.0005 -0.0252 -0.0231 736 ALA A O 5637 C CB . ALA A 682 ? 0.2236 0.2327 0.2956 -0.0079 -0.0175 -0.0176 736 ALA A CB 5638 N N . PHE A 683 ? 0.2041 0.2095 0.2505 -0.0043 -0.0172 -0.0185 737 PHE A N 5639 C CA . PHE A 683 ? 0.2268 0.2291 0.2633 -0.0021 -0.0188 -0.0191 737 PHE A CA 5640 C C . PHE A 683 ? 0.1957 0.1966 0.2267 0.0006 -0.0200 -0.0212 737 PHE A C 5641 O O . PHE A 683 ? 0.2228 0.2202 0.2495 0.0037 -0.0237 -0.0228 737 PHE A O 5642 C CB . PHE A 683 ? 0.2075 0.2109 0.2376 -0.0037 -0.0147 -0.0168 737 PHE A CB 5643 C CG . PHE A 683 ? 0.2519 0.2528 0.2723 -0.0015 -0.0154 -0.0173 737 PHE A CG 5644 C CD1 . PHE A 683 ? 0.2656 0.2631 0.2833 0.0004 -0.0193 -0.0181 737 PHE A CD1 5645 C CD2 . PHE A 683 ? 0.2974 0.2994 0.3123 -0.0013 -0.0124 -0.0170 737 PHE A CD2 5646 C CE1 . PHE A 683 ? 0.2563 0.2516 0.2658 0.0027 -0.0196 -0.0185 737 PHE A CE1 5647 C CE2 . PHE A 683 ? 0.2811 0.2808 0.2881 0.0008 -0.0128 -0.0174 737 PHE A CE2 5648 C CZ . PHE A 683 ? 0.2533 0.2497 0.2576 0.0028 -0.0162 -0.0179 737 PHE A CZ 5649 N N . THR A 684 ? 0.2100 0.2134 0.2410 0.0000 -0.0168 -0.0210 738 THR A N 5650 C CA . THR A 684 ? 0.2152 0.2172 0.2407 0.0026 -0.0173 -0.0226 738 THR A CA 5651 C C . THR A 684 ? 0.2311 0.2308 0.2598 0.0053 -0.0222 -0.0253 738 THR A C 5652 O O . THR A 684 ? 0.2297 0.2259 0.2520 0.0087 -0.0245 -0.0266 738 THR A O 5653 C CB . THR A 684 ? 0.2426 0.2478 0.2682 0.0012 -0.0131 -0.0220 738 THR A CB 5654 O OG1 . THR A 684 ? 0.2326 0.2394 0.2547 -0.0007 -0.0093 -0.0198 738 THR A OG1 5655 C CG2 . THR A 684 ? 0.2233 0.2269 0.2430 0.0039 -0.0134 -0.0234 738 THR A CG2 5656 N N . VAL A 685 ? 0.2167 0.2180 0.2553 0.0041 -0.0236 -0.0260 739 VAL A N 5657 C CA . VAL A 685 ? 0.2293 0.2281 0.2719 0.0068 -0.0290 -0.0288 739 VAL A CA 5658 C C . VAL A 685 ? 0.2195 0.2138 0.2584 0.0095 -0.0338 -0.0301 739 VAL A C 5659 O O . VAL A 685 ? 0.2235 0.2140 0.2577 0.0135 -0.0376 -0.0324 739 VAL A O 5660 C CB . VAL A 685 ? 0.2228 0.2245 0.2786 0.0048 -0.0296 -0.0293 739 VAL A CB 5661 C CG1 . VAL A 685 ? 0.2329 0.2315 0.2942 0.0077 -0.0364 -0.0328 739 VAL A CG1 5662 C CG2 . VAL A 685 ? 0.2309 0.2363 0.2886 0.0033 -0.0252 -0.0287 739 VAL A CG2 5663 N N . GLN A 686 ? 0.2188 0.2131 0.2596 0.0077 -0.0339 -0.0286 740 GLN A N 5664 C CA . GLN A 686 ? 0.2343 0.2243 0.2713 0.0103 -0.0384 -0.0297 740 GLN A CA 5665 C C . GLN A 686 ? 0.2351 0.2221 0.2594 0.0133 -0.0378 -0.0297 740 GLN A C 5666 O O . GLN A 686 ? 0.2463 0.2287 0.2654 0.0175 -0.0421 -0.0316 740 GLN A O 5667 C CB . GLN A 686 ? 0.2408 0.2319 0.2816 0.0074 -0.0376 -0.0277 740 GLN A CB 5668 C CG . GLN A 686 ? 0.2712 0.2579 0.3088 0.0099 -0.0425 -0.0289 740 GLN A CG 5669 C CD . GLN A 686 ? 0.2853 0.2691 0.3296 0.0122 -0.0492 -0.0320 740 GLN A CD 5670 O OE1 . GLN A 686 ? 0.2869 0.2728 0.3418 0.0108 -0.0502 -0.0329 740 GLN A OE1 5671 N NE2 . GLN A 686 ? 0.2959 0.2749 0.3343 0.0161 -0.0540 -0.0339 740 GLN A NE2 5672 N N . ALA A 687 ? 0.2298 0.2192 0.2492 0.0115 -0.0325 -0.0274 741 ALA A N 5673 C CA . ALA A 687 ? 0.2316 0.2186 0.2404 0.0141 -0.0312 -0.0269 741 ALA A CA 5674 C C . ALA A 687 ? 0.2372 0.2215 0.2415 0.0180 -0.0327 -0.0288 741 ALA A C 5675 O O . ALA A 687 ? 0.2417 0.2217 0.2383 0.0220 -0.0346 -0.0295 741 ALA A O 5676 C CB . ALA A 687 ? 0.2297 0.2199 0.2356 0.0112 -0.0254 -0.0244 741 ALA A CB 5677 N N . ALA A 688 ? 0.2277 0.2142 0.2367 0.0171 -0.0319 -0.0296 742 ALA A N 5678 C CA . ALA A 688 ? 0.2385 0.2223 0.2439 0.0208 -0.0336 -0.0315 742 ALA A CA 5679 C C . ALA A 688 ? 0.2455 0.2248 0.2510 0.0248 -0.0401 -0.0343 742 ALA A C 5680 O O . ALA A 688 ? 0.2514 0.2260 0.2489 0.0294 -0.0420 -0.0355 742 ALA A O 5681 C CB . ALA A 688 ? 0.2188 0.2062 0.2308 0.0189 -0.0320 -0.0320 742 ALA A CB 5682 N N . ALA A 689 ? 0.2518 0.2320 0.2666 0.0232 -0.0434 -0.0354 743 ALA A N 5683 C CA . ALA A 689 ? 0.2693 0.2449 0.2851 0.0269 -0.0504 -0.0384 743 ALA A CA 5684 C C . ALA A 689 ? 0.2701 0.2408 0.2756 0.0307 -0.0521 -0.0384 743 ALA A C 5685 O O . ALA A 689 ? 0.2647 0.2301 0.2639 0.0361 -0.0563 -0.0407 743 ALA A O 5686 C CB . ALA A 689 ? 0.2524 0.2301 0.2805 0.0240 -0.0532 -0.0390 743 ALA A CB 5687 N N . GLU A 690 ? 0.2625 0.2348 0.2657 0.0282 -0.0488 -0.0358 744 GLU A N 5688 C CA . GLU A 690 ? 0.2701 0.2382 0.2643 0.0315 -0.0501 -0.0356 744 GLU A CA 5689 C C . GLU A 690 ? 0.2708 0.2354 0.2532 0.0358 -0.0481 -0.0352 744 GLU A C 5690 O O . GLU A 690 ? 0.2849 0.2448 0.2595 0.0401 -0.0502 -0.0357 744 GLU A O 5691 C CB . GLU A 690 ? 0.2752 0.2456 0.2704 0.0280 -0.0474 -0.0331 744 GLU A CB 5692 C CG . GLU A 690 ? 0.2845 0.2560 0.2899 0.0255 -0.0509 -0.0339 744 GLU A CG 5693 C CD . GLU A 690 ? 0.3547 0.3287 0.3618 0.0217 -0.0482 -0.0313 744 GLU A CD 5694 O OE1 . GLU A 690 ? 0.3858 0.3609 0.3865 0.0209 -0.0437 -0.0291 744 GLU A OE1 5695 O OE2 . GLU A 690 ? 0.3462 0.3210 0.3617 0.0196 -0.0506 -0.0316 744 GLU A OE2 5696 N N . THR A 691 ? 0.2689 0.2358 0.2505 0.0349 -0.0441 -0.0342 745 THR A N 5697 C CA . THR A 691 ? 0.2590 0.2224 0.2305 0.0391 -0.0422 -0.0338 745 THR A CA 5698 C C . THR A 691 ? 0.2852 0.2429 0.2523 0.0451 -0.0474 -0.0368 745 THR A C 5699 O O . THR A 691 ? 0.2895 0.2429 0.2469 0.0497 -0.0466 -0.0364 745 THR A O 5700 C CB . THR A 691 ? 0.2795 0.2463 0.2510 0.0369 -0.0368 -0.0321 745 THR A CB 5701 O OG1 . THR A 691 ? 0.2708 0.2388 0.2477 0.0366 -0.0384 -0.0339 745 THR A OG1 5702 C CG2 . THR A 691 ? 0.2270 0.1994 0.2028 0.0311 -0.0318 -0.0294 745 THR A CG2 5703 N N . LEU A 692 ? 0.2825 0.2401 0.2572 0.0449 -0.0527 -0.0395 746 LEU A N 5704 C CA . LEU A 692 ? 0.2993 0.2514 0.2710 0.0506 -0.0587 -0.0429 746 LEU A CA 5705 C C . LEU A 692 ? 0.3181 0.2656 0.2880 0.0538 -0.0646 -0.0449 746 LEU A C 5706 O O . LEU A 692 ? 0.3260 0.2678 0.2917 0.0594 -0.0703 -0.0480 746 LEU A O 5707 C CB . LEU A 692 ? 0.2914 0.2460 0.2734 0.0487 -0.0615 -0.0452 746 LEU A CB 5708 C CG . LEU A 692 ? 0.2939 0.2528 0.2781 0.0457 -0.0562 -0.0437 746 LEU A CG 5709 C CD1 . LEU A 692 ? 0.2923 0.2532 0.2874 0.0445 -0.0598 -0.0463 746 LEU A CD1 5710 C CD2 . LEU A 692 ? 0.3084 0.2633 0.2807 0.0504 -0.0538 -0.0430 746 LEU A CD2 5711 N N . SER A 693 ? 0.3192 0.2689 0.2922 0.0506 -0.0638 -0.0434 747 SER A N 5712 C CA . SER A 693 ? 0.3276 0.2724 0.2972 0.0541 -0.0690 -0.0451 747 SER A CA 5713 C C . SER A 693 ? 0.3351 0.2736 0.2900 0.0608 -0.0690 -0.0450 747 SER A C 5714 O O . SER A 693 ? 0.3242 0.2628 0.2720 0.0617 -0.0636 -0.0427 747 SER A O 5715 C CB . SER A 693 ? 0.3185 0.2669 0.2933 0.0494 -0.0673 -0.0431 747 SER A CB 5716 O OG . SER A 693 ? 0.3294 0.2828 0.3176 0.0440 -0.0676 -0.0433 747 SER A OG 5717 N N . GLU A 694 ? 0.3502 0.2828 0.3006 0.0659 -0.0750 -0.0475 748 GLU A N 5718 C CA . GLU A 694 ? 0.3732 0.2999 0.3092 0.0722 -0.0741 -0.0468 748 GLU A CA 5719 C C . GLU A 694 ? 0.3565 0.2868 0.2897 0.0688 -0.0666 -0.0425 748 GLU A C 5720 O O . GLU A 694 ? 0.3575 0.2927 0.2984 0.0631 -0.0650 -0.0410 748 GLU A O 5721 C CB . GLU A 694 ? 0.3840 0.3043 0.3160 0.0775 -0.0816 -0.0499 748 GLU A CB 5722 C CG . GLU A 694 ? 0.4467 0.3629 0.3810 0.0815 -0.0893 -0.0544 748 GLU A CG 5723 C CD . GLU A 694 ? 0.5714 0.4795 0.4988 0.0887 -0.0973 -0.0581 748 GLU A CD 5724 O OE1 . GLU A 694 ? 0.5774 0.4857 0.5113 0.0873 -0.1017 -0.0595 748 GLU A OE1 5725 O OE2 . GLU A 694 ? 0.6296 0.5311 0.5454 0.0961 -0.0990 -0.0594 748 GLU A OE2 5726 N N . VAL A 695 ? 0.3576 0.2853 0.2802 0.0724 -0.0620 -0.0403 749 VAL A N 5727 C CA . VAL A 695 ? 0.3538 0.2860 0.2759 0.0685 -0.0543 -0.0362 749 VAL A CA 5728 C C . VAL A 695 ? 0.3756 0.3067 0.2945 0.0689 -0.0540 -0.0350 749 VAL A C 5729 O O . VAL A 695 ? 0.3644 0.2995 0.2847 0.0651 -0.0488 -0.0321 749 VAL A O 5730 C CB . VAL A 695 ? 0.3657 0.2959 0.2790 0.0718 -0.0487 -0.0339 749 VAL A CB 5731 C CG1 . VAL A 695 ? 0.3665 0.2981 0.2831 0.0709 -0.0485 -0.0348 749 VAL A CG1 5732 C CG2 . VAL A 695 ? 0.3778 0.2997 0.2777 0.0804 -0.0505 -0.0345 749 VAL A CG2 5733 N N . ALA A 696 ? 0.3751 0.3006 0.2894 0.0740 -0.0600 -0.0376 750 ALA A N 5734 C CA . ALA A 696 ? 0.4128 0.3368 0.3236 0.0750 -0.0603 -0.0368 750 ALA A CA 5735 C C . ALA A 696 ? 0.4487 0.3667 0.3571 0.0800 -0.0687 -0.0407 750 ALA A C 5736 O O . ALA A 696 ? 0.5035 0.4204 0.4115 0.0803 -0.0708 -0.0410 750 ALA A O 5737 C CB . ALA A 696 ? 0.4033 0.3247 0.3032 0.0790 -0.0545 -0.0338 750 ALA A CB 5738 O OXT . ALA A 696 ? 0.4460 0.3603 0.3534 0.0837 -0.0736 -0.0437 750 ALA A OXT 5929 O O . HOH T . ? 0.2865 0.3060 0.3211 0.0206 0.0036 -0.0484 901 HOH A O 5930 O O . HOH T . ? 0.6581 0.6858 0.6498 0.0029 0.0300 -0.0248 902 HOH A O 5931 O O . HOH T . ? 0.5050 0.4930 0.5747 0.0101 0.0377 -0.0057 903 HOH A O 5932 O O . HOH T . ? 0.5453 0.5033 0.5865 0.0608 -0.0898 -0.0733 904 HOH A O 5933 O O . HOH T . ? 0.5147 0.5512 0.6900 0.0311 -0.0443 -0.0775 905 HOH A O 5934 O O . HOH T . ? 0.5395 0.5699 0.5506 -0.0009 0.0259 -0.0238 906 HOH A O 5935 O O . HOH T . ? 0.3836 0.3117 0.2732 0.0793 -0.0032 -0.0132 907 HOH A O 5936 O O . HOH T . ? 0.5369 0.5257 0.5746 0.0131 0.0358 -0.0060 908 HOH A O 5937 O O . HOH T . ? 0.5921 0.6247 0.5997 0.0051 0.0284 -0.0319 909 HOH A O 5938 O O . HOH T . ? 0.4288 0.4412 0.5656 0.0245 -0.0564 -0.0638 910 HOH A O 5939 O O . HOH T . ? 0.6539 0.6055 0.6709 0.0406 0.0296 -0.0210 911 HOH A O 5940 O O . HOH T . ? 0.5452 0.6216 0.6218 0.0440 0.0692 -0.0567 912 HOH A O 5941 O O . HOH T . ? 0.4895 0.4826 0.5218 0.0106 0.0316 -0.0080 913 HOH A O 5942 O O . HOH T . ? 0.5472 0.5557 0.5547 0.0055 0.0159 -0.0282 914 HOH A O 5943 O O . HOH T . ? 0.5542 0.5671 0.7182 0.0145 -0.0603 -0.0569 915 HOH A O 5944 O O . HOH T . ? 0.3813 0.3736 0.4277 0.0107 0.0363 -0.0031 916 HOH A O 5945 O O . HOH T . ? 0.4279 0.3859 0.4535 0.0345 0.0584 0.0107 917 HOH A O 5946 O O . HOH T . ? 0.6656 0.5725 0.5702 0.0907 0.0669 0.0259 918 HOH A O 5947 O O . HOH T . ? 0.3884 0.3826 0.5105 0.0175 -0.0687 -0.0523 919 HOH A O 5948 O O . HOH T . ? 0.5826 0.5024 0.5456 0.0744 -0.1025 -0.0596 920 HOH A O 5949 O O . HOH T . ? 0.4953 0.5469 0.5550 0.0379 0.0276 -0.0727 921 HOH A O 5950 O O . HOH T . ? 0.3119 0.3326 0.2995 0.0257 0.0170 -0.0590 922 HOH A O 5951 O O . HOH T . ? 0.5174 0.5378 0.6008 0.0215 -0.0226 -0.0540 923 HOH A O 5952 O O . HOH T . ? 0.4478 0.4807 0.5358 0.0308 -0.0091 -0.0669 924 HOH A O 5953 O O . HOH T . ? 0.4793 0.5343 0.6018 -0.0088 0.0425 -0.0113 925 HOH A O 5954 O O . HOH T . ? 0.5273 0.5254 0.5809 0.0092 0.0013 -0.0481 926 HOH A O 5955 O O . HOH T . ? 0.6822 0.6106 0.7257 0.0710 -0.1327 -0.0813 927 HOH A O 5956 O O . HOH T . ? 0.6483 0.5786 0.6084 0.0928 -0.0470 -0.0688 928 HOH A O 5957 O O . HOH T . ? 0.5797 0.5339 0.5683 0.0724 -0.0245 -0.0646 929 HOH A O 5958 O O . HOH T . ? 0.3954 0.3840 0.4679 0.0565 -0.0623 -0.0804 930 HOH A O 5959 O O . HOH T . ? 0.5864 0.5899 0.4993 0.0494 0.0275 -0.0539 931 HOH A O 5960 O O . HOH T . ? 0.2823 0.2764 0.2624 0.0150 0.0037 -0.0190 932 HOH A O 5961 O O . HOH T . ? 0.2769 0.2940 0.2686 -0.0051 0.0144 -0.0169 933 HOH A O 5962 O O . HOH T . ? 0.6624 0.5473 0.5522 0.1208 -0.0974 -0.0680 934 HOH A O 5963 O O . HOH T . ? 0.6358 0.7119 0.7830 0.0330 0.0256 -0.0713 935 HOH A O 5964 O O . HOH T . ? 0.6021 0.5550 0.6209 0.0384 0.0346 -0.0153 936 HOH A O 5965 O O . HOH T . ? 0.6573 0.6941 0.6894 -0.0030 0.0590 0.0013 937 HOH A O 5966 O O . HOH T . ? 0.6425 0.6351 0.5931 0.0569 -0.0118 -0.0906 938 HOH A O 5967 O O . HOH T . ? 0.6365 0.4989 0.4488 0.1392 -0.0094 -0.0188 939 HOH A O 5968 O O . HOH T . ? 0.3712 0.4125 0.4084 0.0123 0.0268 -0.0438 940 HOH A O 5969 O O . HOH T . ? 0.4317 0.4398 0.6196 -0.0211 -0.0320 -0.0103 941 HOH A O 5970 O O . HOH T . ? 0.4902 0.4275 0.4639 0.0882 -0.0632 -0.0728 942 HOH A O 5971 O O . HOH T . ? 0.5814 0.6136 0.6283 0.0367 0.0121 -0.0746 943 HOH A O 5972 O O . HOH T . ? 0.6942 0.5703 0.5133 0.1296 0.0296 0.0078 944 HOH A O 5973 O O . HOH T . ? 0.4962 0.5184 0.6845 0.0024 -0.0478 -0.0461 945 HOH A O 5974 O O . HOH T . ? 0.5092 0.5687 0.7465 -0.0219 0.0365 0.0004 946 HOH A O 5975 O O . HOH T . ? 0.2962 0.3020 0.3268 0.0032 0.0081 -0.0350 947 HOH A O 5976 O O . HOH T . ? 0.6892 0.5752 0.5532 0.1209 -0.0508 -0.0474 948 HOH A O 5977 O O . HOH T . ? 0.3227 0.3669 0.3679 0.0196 0.0263 -0.0530 949 HOH A O 5978 O O . HOH T . ? 0.2662 0.2773 0.2837 0.0190 0.0123 -0.0457 950 HOH A O 5979 O O . HOH T . ? 0.6355 0.6714 0.7531 0.0318 -0.0199 -0.0712 951 HOH A O 5981 O O . HOH T . ? 0.7378 0.7465 0.7087 0.0148 0.0055 -0.0463 953 HOH A O 5982 O O . HOH T . ? 0.4409 0.4521 0.4362 0.0181 0.0047 -0.0567 954 HOH A O 5983 O O . HOH T . ? 0.5555 0.5556 0.5807 0.0196 -0.0089 -0.0663 955 HOH A O 5984 O O . HOH T . ? 0.4194 0.4274 0.4767 0.0184 -0.0262 -0.0447 956 HOH A O 5985 O O . HOH T . ? 0.3748 0.2953 0.2951 0.0815 -0.0695 -0.0473 957 HOH A O 5986 O O . HOH T . ? 0.3263 0.3131 0.3247 0.0370 -0.0117 -0.0438 958 HOH A O 5987 O O . HOH T . ? 0.5732 0.6144 0.5762 0.0511 0.0380 -0.0740 959 HOH A O 5988 O O . HOH T . ? 0.4697 0.4555 0.5411 0.0105 0.0226 -0.0252 960 HOH A O 5989 O O . HOH T . ? 0.4450 0.4808 0.4922 -0.0074 0.0593 0.0074 961 HOH A O 5990 O O . HOH T . ? 0.3610 0.3919 0.4328 0.0279 -0.0029 -0.0623 962 HOH A O 5991 O O . HOH T . ? 0.3153 0.3391 0.4958 -0.0316 0.0421 0.0318 963 HOH A O 5992 O O . HOH T . ? 0.4765 0.4785 0.5064 0.0194 -0.0019 -0.0632 964 HOH A O 5993 O O . HOH T . ? 0.5454 0.4404 0.4594 0.0924 0.0698 0.0261 965 HOH A O 5994 O O . HOH T . ? 0.2384 0.2490 0.2438 0.0024 0.0139 -0.0278 966 HOH A O 5995 O O . HOH T . ? 0.4132 0.4464 0.4275 0.0351 0.0231 -0.0694 967 HOH A O 5996 O O . HOH T . ? 0.5022 0.5261 0.5163 0.0400 0.0129 -0.0786 968 HOH A O 5997 O O . HOH T . ? 0.5792 0.5151 0.6218 0.0956 -0.1226 -0.1025 969 HOH A O 5998 O O . HOH T . ? 0.4802 0.5049 0.4687 0.0382 0.0208 -0.0695 970 HOH A O 5999 O O . HOH T . ? 0.4972 0.5086 0.4762 0.0183 0.0073 -0.0524 971 HOH A O 6000 O O . HOH T . ? 0.6767 0.5270 0.4885 0.1422 0.0470 0.0172 972 HOH A O 6001 O O . HOH T . ? 0.5716 0.5307 0.6465 0.0690 -0.1073 -0.0892 973 HOH A O 6002 O O . HOH T . ? 0.5206 0.5231 0.5458 0.0070 -0.0097 -0.0492 974 HOH A O 6003 O O . HOH T . ? 0.2851 0.2768 0.3174 0.0145 0.0202 -0.0303 975 HOH A O 6004 O O . HOH T . ? 0.4638 0.3486 0.2960 0.1215 -0.0200 -0.0218 976 HOH A O 6005 O O . HOH T . ? 0.2943 0.2828 0.3110 0.0358 0.0062 -0.0519 977 HOH A O 6006 O O . HOH T . ? 0.2984 0.3211 0.3397 -0.0061 0.0068 -0.0187 978 HOH A O 6007 O O . HOH T . ? 0.3540 0.3668 0.3797 0.0287 0.0076 -0.0677 979 HOH A O 6008 O O . HOH T . ? 0.4482 0.4273 0.4513 0.0242 0.0374 -0.0031 980 HOH A O 6009 O O . HOH T . ? 0.3011 0.2705 0.3138 0.0358 0.0181 -0.0343 981 HOH A O 6010 O O . HOH T . ? 0.4953 0.5145 0.6401 0.0165 -0.0472 -0.0569 982 HOH A O 6011 O O . HOH T . ? 0.5473 0.5424 0.6235 0.0046 0.0119 -0.0321 983 HOH A O 6012 O O . HOH T . ? 0.4218 0.3917 0.4372 0.0686 -0.0407 -0.0742 984 HOH A O 6013 O O . HOH T . ? 0.8602 0.6766 0.6107 0.1785 0.0021 -0.0084 985 HOH A O 6014 O O . HOH T . ? 0.5029 0.5563 0.6206 -0.0101 0.0725 0.0111 986 HOH A O 6015 O O . HOH T . ? 0.6227 0.6190 0.5931 0.0504 -0.0119 -0.0897 987 HOH A O 6016 O O . HOH T . ? 0.6486 0.6409 0.7113 0.0604 -0.0480 -0.0830 988 HOH A O 6017 O O . HOH T . ? 0.7360 0.6581 0.6853 0.0884 -0.0180 -0.0523 989 HOH A O 6018 O O . HOH T . ? 0.5553 0.5722 0.5403 -0.0056 0.0185 -0.0140 990 HOH A O 6019 O O . HOH T . ? 0.3076 0.2858 0.2922 0.0225 -0.0306 -0.0261 991 HOH A O 6020 O O . HOH T . ? 0.4586 0.3934 0.4294 0.0639 0.0154 -0.0291 992 HOH A O 6021 O O . HOH T . ? 0.3640 0.3795 0.4577 0.0302 -0.0354 -0.0634 993 HOH A O 6022 O O . HOH T . ? 0.4213 0.3644 0.4397 0.0429 0.0582 0.0092 994 HOH A O 6023 O O . HOH T . ? 0.5443 0.5380 0.5436 0.0327 -0.0206 -0.0802 995 HOH A O 6024 O O . HOH T . ? 0.6874 0.5152 0.4793 0.1723 -0.0587 -0.0512 996 HOH A O 6025 O O . HOH T . ? 0.4153 0.3858 0.4028 0.0368 0.0201 -0.0244 997 HOH A O 6026 O O . HOH T . ? 0.5608 0.5684 0.5730 0.0329 -0.0007 -0.0768 998 HOH A O 6027 O O . HOH T . ? 0.4702 0.3716 0.3765 0.1101 -0.0453 -0.0564 999 HOH A O 6028 O O . HOH T . ? 0.4055 0.4482 0.4238 0.0377 0.0338 -0.0667 1000 HOH A O 6029 O O . HOH T . ? 0.3753 0.3690 0.4686 0.0389 -0.0657 -0.0687 1001 HOH A O 6030 O O . HOH T . ? 0.3311 0.3730 0.3573 0.0232 0.0308 -0.0546 1002 HOH A O 6031 O O . HOH T . ? 0.3515 0.3650 0.3537 0.0056 0.0142 -0.0284 1003 HOH A O 6032 O O . HOH T . ? 0.4713 0.4202 0.5027 0.0923 -0.0910 -0.0969 1004 HOH A O 6033 O O . HOH T . ? 0.3228 0.2864 0.3361 0.0534 -0.0650 -0.0595 1005 HOH A O 6034 O O . HOH T . ? 0.3539 0.3003 0.3177 0.0523 0.0482 0.0068 1006 HOH A O 6035 O O . HOH T . ? 0.2835 0.3018 0.3831 0.0124 -0.0293 -0.0462 1007 HOH A O 6036 O O . HOH T . ? 0.2823 0.2951 0.2814 0.0038 0.0125 -0.0251 1008 HOH A O 6037 O O . HOH T . ? 0.3226 0.3315 0.3464 0.0254 0.0097 -0.0544 1009 HOH A O 6038 O O . HOH T . ? 0.4382 0.4051 0.4582 0.0330 0.0238 -0.0279 1010 HOH A O 6039 O O . HOH T . ? 0.3333 0.3795 0.4290 -0.0110 0.0424 -0.0054 1011 HOH A O 6040 O O . HOH T . ? 0.4711 0.4066 0.4685 0.0785 -0.0968 -0.0746 1012 HOH A O 6041 O O . HOH T . ? 0.5627 0.5814 0.6212 0.0492 -0.0046 -0.0848 1013 HOH A O 6042 O O . HOH T . ? 0.3023 0.3390 0.4847 -0.0045 -0.0209 -0.0358 1014 HOH A O 6043 O O . HOH T . ? 0.4913 0.4441 0.4786 0.0652 -0.0087 -0.0549 1015 HOH A O 6044 O O . HOH T . ? 0.3434 0.3614 0.3799 0.0144 -0.0019 -0.0406 1016 HOH A O 6045 O O . HOH T . ? 0.5875 0.5628 0.6388 0.0194 0.0441 -0.0027 1017 HOH A O 6046 O O . HOH T . ? 0.2138 0.2162 0.2182 0.0136 0.0162 -0.0296 1018 HOH A O 6047 O O . HOH T . ? 0.4438 0.4165 0.4387 0.0205 -0.0442 -0.0269 1019 HOH A O 6048 O O . HOH T . ? 0.3763 0.3985 0.6006 -0.0245 -0.0185 -0.0077 1020 HOH A O 6049 O O . HOH T . ? 0.3085 0.3051 0.2953 0.0111 0.0159 -0.0128 1021 HOH A O 6050 O O . HOH T . ? 0.6717 0.6875 0.6307 0.0172 0.0225 -0.0384 1022 HOH A O 6051 O O . HOH T . ? 0.6283 0.6472 0.8295 0.0309 -0.0765 -0.0804 1023 HOH A O 6052 O O . HOH T . ? 0.5722 0.5419 0.5801 0.0522 -0.0022 -0.0569 1024 HOH A O 6053 O O . HOH T . ? 0.4099 0.4595 0.6684 -0.0310 0.0866 0.0476 1025 HOH A O 6054 O O . HOH T . ? 0.6161 0.4970 0.4857 0.1274 -0.0679 -0.0586 1026 HOH A O 6055 O O . HOH T . ? 0.5362 0.5687 0.6902 0.0220 -0.0369 -0.0650 1027 HOH A O 6056 O O . HOH T . ? 0.5014 0.4970 0.5597 0.0057 0.0234 -0.0192 1028 HOH A O 6057 O O . HOH T . ? 0.3489 0.3654 0.3395 0.0230 0.0114 -0.0590 1029 HOH A O 6058 O O . HOH T . ? 0.2577 0.2561 0.2582 0.0223 0.0088 -0.0347 1030 HOH A O 6059 O O . HOH T . ? 0.5304 0.5047 0.6473 0.0263 -0.0938 -0.0587 1031 HOH A O 6060 O O . HOH T . ? 0.3166 0.3279 0.3955 0.0291 -0.0335 -0.0594 1032 HOH A O 6061 O O . HOH T . ? 0.3824 0.4418 0.4452 0.0194 0.0454 -0.0451 1033 HOH A O 6062 O O . HOH T . ? 0.7787 0.5987 0.5177 0.1871 -0.0611 -0.0402 1034 HOH A O 6063 O O . HOH T . ? 0.6609 0.6443 0.7310 0.0126 0.0212 -0.0281 1035 HOH A O 6064 O O . HOH T . ? 0.4410 0.4659 0.6265 -0.0203 -0.0122 -0.0106 1036 HOH A O 6065 O O . HOH T . ? 0.5525 0.5747 0.7721 -0.0016 -0.0533 -0.0446 1037 HOH A O 6066 O O . HOH T . ? 0.4072 0.4571 0.5268 -0.0133 0.0597 0.0075 1038 HOH A O 6067 O O . HOH T . ? 0.4801 0.5112 0.5937 0.0124 -0.0185 -0.0494 1039 HOH A O 6068 O O . HOH T . ? 0.6244 0.4721 0.4444 0.1499 -0.0298 -0.0369 1040 HOH A O 6069 O O . HOH T . ? 0.5044 0.5212 0.4849 0.0530 0.0121 -0.0853 1041 HOH A O 6070 O O . HOH T . ? 0.3759 0.3455 0.3459 0.0410 -0.0259 -0.0343 1042 HOH A O 6071 O O . HOH T . ? 0.5075 0.5138 0.4922 0.0233 -0.0009 -0.0618 1043 HOH A O 6072 O O . HOH T . ? 0.5409 0.5666 0.6324 -0.0117 0.1002 0.0500 1044 HOH A O 6073 O O . HOH T . ? 0.3967 0.4126 0.5139 -0.0186 -0.0063 -0.0056 1045 HOH A O 6074 O O . HOH T . ? 0.5983 0.4828 0.4445 0.1174 0.0486 0.0176 1046 HOH A O 6075 O O . HOH T . ? 0.5980 0.5993 0.6754 0.0004 0.0059 -0.0308 1047 HOH A O 6076 O O . HOH T . ? 0.3460 0.3752 0.3848 -0.0105 0.0491 0.0073 1048 HOH A O 6077 O O . HOH T . ? 0.5100 0.5406 0.4992 0.0520 0.0278 -0.0782 1049 HOH A O 6078 O O . HOH T . ? 0.4817 0.4990 0.4961 0.0013 0.0067 -0.0246 1050 HOH A O 6079 O O . HOH T . ? 0.4585 0.4614 0.5122 0.0018 -0.0063 -0.0407 1051 HOH A O 6080 O O . HOH T . ? 0.4259 0.4357 0.5834 0.0123 -0.0600 -0.0533 1052 HOH A O 6081 O O . HOH T . ? 0.6370 0.6393 0.6321 0.0085 -0.0100 -0.0462 1053 HOH A O 6082 O O . HOH T . ? 0.3616 0.3695 0.5263 -0.0111 -0.0417 -0.0240 1054 HOH A O 6083 O O . HOH T . ? 0.3021 0.2539 0.2869 0.0637 -0.0625 -0.0583 1055 HOH A O 6084 O O . HOH T . ? 0.3427 0.3171 0.3269 0.0235 -0.0362 -0.0264 1056 HOH A O 6085 O O . HOH T . ? 0.6587 0.6586 0.7142 0.0551 -0.0297 -0.0793 1057 HOH A O 6086 O O . HOH T . ? 0.2993 0.2925 0.3347 0.0184 0.0128 -0.0439 1058 HOH A O 6087 O O . HOH T . ? 0.3520 0.3507 0.3855 0.0184 0.0093 -0.0504 1059 HOH A O 6088 O O . HOH T . ? 0.4081 0.3599 0.4429 0.0348 0.0438 -0.0060 1060 HOH A O 6089 O O . HOH T . ? 0.3811 0.4090 0.3856 0.0020 0.0232 -0.0292 1061 HOH A O 6090 O O . HOH T . ? 0.5383 0.5568 0.5448 -0.0089 0.0158 -0.0107 1062 HOH A O 6091 O O . HOH T . ? 0.7319 0.7711 0.7472 0.0047 0.0425 -0.0231 1063 HOH A O 6092 O O . HOH T . ? 0.2897 0.3179 0.3180 -0.0093 0.0274 -0.0090 1064 HOH A O 6093 O O . HOH T . ? 0.3150 0.3630 0.3563 0.0294 0.0319 -0.0615 1065 HOH A O 6094 O O . HOH T . ? 0.4922 0.4381 0.4883 0.0494 -0.0827 -0.0499 1066 HOH A O 6095 O O . HOH T . ? 0.6099 0.6388 0.6258 0.0014 0.0204 -0.0291 1067 HOH A O 6096 O O . HOH T . ? 0.2558 0.2771 0.2996 -0.0095 0.0077 -0.0136 1068 HOH A O 6097 O O . HOH T . ? 0.3627 0.3605 0.3467 0.0106 0.0116 -0.0155 1069 HOH A O 6098 O O . HOH T . ? 0.3127 0.3033 0.3698 0.0104 0.0181 -0.0309 1070 HOH A O 6099 O O . HOH T . ? 0.4129 0.4484 0.4210 0.0352 0.0281 -0.0662 1071 HOH A O 6100 O O . HOH T . ? 0.4286 0.4553 0.4389 -0.0055 0.0249 -0.0156 1072 HOH A O 6101 O O . HOH T . ? 0.3208 0.3269 0.3414 0.0261 -0.0029 -0.0462 1073 HOH A O 6102 O O . HOH T . ? 0.3806 0.3848 0.3771 0.0309 -0.0049 -0.0740 1074 HOH A O 6103 O O . HOH T . ? 0.4160 0.4366 0.4158 0.0310 0.0136 -0.0681 1075 HOH A O 6104 O O . HOH T . ? 0.2481 0.2708 0.2620 0.0115 0.0172 -0.0433 1076 HOH A O 6105 O O . HOH T . ? 0.5332 0.4174 0.4126 0.1063 0.0319 -0.0006 1077 HOH A O 6106 O O . HOH T . ? 0.6745 0.5843 0.6099 0.1036 -0.0877 -0.0717 1078 HOH A O 6107 O O . HOH T . ? 0.6554 0.6253 0.6410 0.0334 0.0403 0.0010 1079 HOH A O 6108 O O . HOH T . ? 0.2555 0.2619 0.2732 0.0146 0.0144 -0.0415 1080 HOH A O 6109 O O . HOH T . ? 0.3396 0.3483 0.3400 -0.0016 0.0076 -0.0223 1081 HOH A O 6110 O O . HOH T . ? 0.5177 0.4275 0.4853 0.0715 0.0718 0.0238 1082 HOH A O 6111 O O . HOH T . ? 0.6196 0.6506 0.6757 -0.0056 0.0873 0.0305 1083 HOH A O 6112 O O . HOH T . ? 0.4876 0.5035 0.4984 -0.0123 0.0323 0.0061 1084 HOH A O 6113 O O . HOH T . ? 0.6575 0.6565 0.6669 0.0132 -0.0163 -0.0571 1085 HOH A O 6114 O O . HOH T . ? 0.6264 0.6440 0.6035 0.0055 0.0177 -0.0319 1086 HOH A O 6115 O O . HOH T . ? 0.4977 0.4344 0.4799 0.0583 0.0221 -0.0247 1087 HOH A O 6116 O O . HOH T . ? 0.2721 0.2536 0.2382 0.0257 0.0161 -0.0078 1088 HOH A O 6117 O O . HOH T . ? 0.4958 0.4509 0.5380 0.0326 0.0575 0.0083 1089 HOH A O 6118 O O . HOH T . ? 0.5291 0.5531 0.5679 0.0094 0.0044 -0.0375 1090 HOH A O 6119 O O . HOH T . ? 0.6348 0.5884 0.6812 0.0615 -0.0991 -0.0750 1091 HOH A O 6120 O O . HOH T . ? 0.4377 0.4459 0.4267 0.0004 0.0090 -0.0175 1092 HOH A O 6121 O O . HOH T . ? 0.5988 0.5011 0.5654 0.0951 -0.1301 -0.0785 1093 HOH A O 6122 O O . HOH T . ? 0.5355 0.3992 0.3511 0.1398 -0.0292 -0.0303 1094 HOH A O 6123 O O . HOH T . ? 0.3375 0.3516 0.3400 0.0052 0.0125 -0.0275 1095 HOH A O 6124 O O . HOH T . ? 0.4172 0.4297 0.4079 -0.0025 0.0102 -0.0181 1096 HOH A O 6125 O O . HOH T . ? 0.4330 0.4459 0.5138 -0.0163 -0.0036 -0.0055 1097 HOH A O 6126 O O . HOH T . ? 0.2915 0.2816 0.3052 0.0269 0.0136 -0.0408 1098 HOH A O 6127 O O . HOH T . ? 0.3194 0.3246 0.4700 0.0016 -0.0546 -0.0393 1099 HOH A O 6128 O O . HOH T . ? 0.2867 0.3084 0.2961 0.0153 0.0162 -0.0505 1100 HOH A O 6129 O O . HOH T . ? 0.2893 0.2517 0.2491 0.0434 -0.0328 -0.0320 1101 HOH A O 6130 O O . HOH T . ? 0.3669 0.3966 0.3680 0.0326 0.0234 -0.0651 1102 HOH A O 6131 O O . HOH T . ? 0.2739 0.2800 0.2823 -0.0008 -0.0052 -0.0178 1103 HOH A O 6132 O O . HOH T . ? 0.3036 0.2995 0.2891 0.0101 -0.0051 -0.0191 1104 HOH A O 6133 O O . HOH T . ? 0.4945 0.4034 0.4563 0.1094 -0.1088 -0.0872 1105 HOH A O 6134 O O . HOH T . ? 0.4044 0.4138 0.4273 0.0268 0.0047 -0.0680 1106 HOH A O 6135 O O . HOH T . ? 0.4174 0.3502 0.3224 0.0743 -0.0160 -0.0239 1107 HOH A O 6136 O O . HOH T . ? 0.2794 0.3105 0.3369 0.0276 0.0054 -0.0619 1108 HOH A O 6137 O O . HOH T . ? 0.6593 0.6170 0.7088 0.0645 -0.0949 -0.0787 1109 HOH A O 6138 O O . HOH T . ? 0.6131 0.5488 0.5690 0.0596 -0.0750 -0.0445 1110 HOH A O 6139 O O . HOH T . ? 0.4675 0.4916 0.4789 0.0042 0.0171 -0.0322 1111 HOH A O 6140 O O . HOH T . ? 0.6039 0.6198 0.7733 -0.0256 -0.0058 0.0023 1112 HOH A O 6141 O O . HOH T . ? 0.2921 0.3088 0.3199 0.0213 0.0059 -0.0481 1113 HOH A O 6142 O O . HOH T . ? 0.5780 0.6325 0.5987 0.0527 0.0534 -0.0683 1114 HOH A O 6143 O O . HOH T . ? 0.3828 0.4287 0.4227 0.0115 0.0335 -0.0405 1115 HOH A O 6144 O O . HOH T . ? 0.2756 0.2928 0.3553 -0.0186 0.0087 0.0003 1116 HOH A O 6145 O O . HOH T . ? 0.5360 0.5113 0.5488 0.0430 0.0051 -0.0514 1117 HOH A O 6146 O O . HOH T . ? 0.6043 0.6658 0.6228 0.0476 0.0964 -0.0309 1118 HOH A O 6147 O O . HOH T . ? 0.4470 0.4173 0.4370 0.0322 0.0393 -0.0014 1119 HOH A O 6148 O O . HOH T . ? 0.3971 0.4221 0.4025 0.0322 0.0169 -0.0685 1120 HOH A O 6149 O O . HOH T . ? 0.2942 0.2755 0.2827 0.0343 0.0093 -0.0330 1121 HOH A O 6150 O O . HOH T . ? 0.4522 0.5031 0.7760 -0.0384 0.0728 0.0463 1122 HOH A O 6151 O O . HOH T . ? 0.6001 0.5265 0.5975 0.1069 -0.1002 -0.0971 1123 HOH A O 6152 O O . HOH T . ? 0.4638 0.5014 0.5591 -0.0117 0.0852 0.0312 1124 HOH A O 6153 O O . HOH T . ? 0.2968 0.2463 0.2485 0.0514 -0.0498 -0.0355 1125 HOH A O 6154 O O . HOH T . ? 0.2565 0.2706 0.2766 0.0190 0.0081 -0.0440 1126 HOH A O 6155 O O . HOH T . ? 0.6066 0.6160 0.6013 -0.0001 0.0043 -0.0293 1127 HOH A O 6156 O O . HOH T . ? 0.4387 0.3519 0.3806 0.1070 -0.0738 -0.0749 1128 HOH A O 6157 O O . HOH T . ? 0.5495 0.5696 0.5607 0.0088 0.0162 -0.0378 1129 HOH A O 6158 O O . HOH T . ? 0.4380 0.3759 0.4091 0.0879 -0.0548 -0.0709 1130 HOH A O 6159 O O . HOH T . ? 0.5534 0.5526 0.6216 0.0025 0.0140 -0.0267 1131 HOH A O 6160 O O . HOH T . ? 0.6342 0.5739 0.6038 0.0818 -0.0287 -0.0622 1132 HOH A O 6161 O O . HOH T . ? 0.3787 0.3887 0.4198 0.0149 -0.0154 -0.0392 1133 HOH A O 6162 O O . HOH T . ? 0.2267 0.2465 0.2221 -0.0016 0.0165 -0.0236 1134 HOH A O 6163 O O . HOH T . ? 0.3434 0.3581 0.3444 0.0270 0.0077 -0.0664 1135 HOH A O 6164 O O . HOH T . ? 0.2582 0.2925 0.3721 -0.0067 0.0000 -0.0251 1136 HOH A O 6165 O O . HOH T . ? 0.6787 0.6096 0.7328 0.0958 -0.1378 -0.1059 1137 HOH A O 6166 O O . HOH T . ? 0.4474 0.4614 0.4455 0.0337 0.0064 -0.0733 1138 HOH A O 6167 O O . HOH T . ? 0.4556 0.4656 0.6435 0.0438 -0.0885 -0.0913 1139 HOH A O 6168 O O . HOH T . ? 0.4341 0.4338 0.5459 0.0602 -0.0695 -0.0932 1140 HOH A O 6169 O O . HOH T . ? 0.2896 0.3207 0.2961 0.0170 0.0249 -0.0489 1141 HOH A O 6170 O O . HOH T . ? 0.4313 0.3644 0.4099 0.0757 -0.0894 -0.0659 1142 HOH A O 6172 O O . HOH T . ? 0.6241 0.5451 0.5503 0.0767 0.0607 0.0198 1144 HOH A O 6173 O O . HOH T . ? 0.3909 0.3917 0.4224 0.0393 0.0011 -0.0671 1145 HOH A O 6174 O O . HOH T . ? 0.2861 0.3246 0.3276 0.0211 0.0208 -0.0558 1146 HOH A O 6175 O O . HOH T . ? 0.4239 0.4389 0.4340 -0.0113 0.0420 0.0125 1147 HOH A O 6176 O O . HOH T . ? 0.3738 0.3999 0.3938 -0.0094 0.0323 -0.0045 1148 HOH A O 6177 O O . HOH T . ? 0.4534 0.5046 0.6494 -0.0217 0.0920 0.0401 1149 HOH A O 6178 O O . HOH T . ? 0.7030 0.6283 0.6693 0.0862 -0.0913 -0.0700 1150 HOH A O 6179 O O . HOH T . ? 0.4456 0.4547 0.4484 0.0004 0.0041 -0.0314 1151 HOH A O 6180 O O . HOH T . ? 0.3828 0.4068 0.3896 0.0060 0.0189 -0.0361 1152 HOH A O 6181 O O . HOH T . ? 0.3147 0.3246 0.3357 0.0223 0.0112 -0.0506 1153 HOH A O 6182 O O . HOH T . ? 0.4336 0.4596 0.5259 0.0351 -0.0208 -0.0704 1154 HOH A O 6183 O O . HOH T . ? 0.5906 0.5709 0.7092 0.0107 -0.0782 -0.0427 1155 HOH A O 6184 O O . HOH T . ? 0.5322 0.4645 0.5815 0.1036 -0.1318 -0.1111 1156 HOH A O 6185 O O . HOH T . ? 0.3423 0.2999 0.3488 0.0403 0.0259 -0.0239 1157 HOH A O 6186 O O . HOH T . ? 0.4233 0.4427 0.4405 -0.0088 0.0129 -0.0121 1158 HOH A O 6187 O O . HOH T . ? 0.3247 0.3385 0.3490 0.0205 0.0036 -0.0449 1159 HOH A O 6188 O O . HOH T . ? 0.3445 0.3489 0.3711 0.0197 0.0098 -0.0529 1160 HOH A O 6189 O O . HOH T . ? 0.2571 0.2284 0.2210 0.0394 -0.0146 -0.0293 1161 HOH A O 6190 O O . HOH T . ? 0.6152 0.6337 0.6145 -0.0014 0.0675 0.0187 1162 HOH A O 6191 O O . HOH T . ? 0.2780 0.2553 0.2477 0.0287 -0.0182 -0.0248 1163 HOH A O 6192 O O . HOH T . ? 0.3163 0.3177 0.3139 0.0071 0.0176 -0.0159 1164 HOH A O 6193 O O . HOH T . ? 0.5279 0.5011 0.5443 0.0657 -0.0271 -0.0735 1165 HOH A O 6194 O O . HOH T . ? 0.5170 0.4585 0.5347 0.0780 -0.1000 -0.0806 1166 HOH A O 6195 O O . HOH T . ? 0.3417 0.3297 0.4059 0.0135 0.0097 -0.0427 1167 HOH A O 6196 O O . HOH T . ? 0.5314 0.4565 0.5504 0.0792 -0.1258 -0.0817 1168 HOH A O 6197 O O . HOH T . ? 0.5102 0.4133 0.4252 0.1056 -0.0300 -0.0518 1169 HOH A O 6198 O O . HOH T . ? 0.2415 0.2580 0.2553 -0.0062 0.0074 -0.0156 1170 HOH A O 6199 O O . HOH T . ? 0.5283 0.5327 0.5402 0.0292 -0.0043 -0.0742 1171 HOH A O 6200 O O . HOH T . ? 0.3263 0.3433 0.3295 0.0042 0.0156 -0.0306 1172 HOH A O 6201 O O . HOH T . ? 0.4200 0.4294 0.4283 0.0000 0.0082 -0.0279 1173 HOH A O 6202 O O . HOH T . ? 0.2955 0.2836 0.3413 0.0138 0.0214 -0.0286 1174 HOH A O 6203 O O . HOH T . ? 0.2476 0.2533 0.2423 -0.0026 -0.0005 -0.0143 1175 HOH A O 6204 O O . HOH T . ? 0.4348 0.4049 0.4827 0.0227 -0.0704 -0.0411 1176 HOH A O 6205 O O . HOH T . ? 0.3283 0.3661 0.3574 0.0102 0.0257 -0.0412 1177 HOH A O 6206 O O . HOH T . ? 0.6626 0.6789 0.6628 0.0447 0.0072 -0.0836 1178 HOH A O 6207 O O . HOH T . ? 0.4135 0.4462 0.4531 0.0360 0.0150 -0.0740 1179 HOH A O 6208 O O . HOH T . ? 0.3244 0.2965 0.3175 0.0363 0.0183 -0.0282 1180 HOH A O 6209 O O . HOH T . ? 0.3447 0.3435 0.3272 0.0091 0.0079 -0.0159 1181 HOH A O 6210 O O . HOH T . ? 0.4455 0.4981 0.5473 -0.0081 0.0649 0.0035 1182 HOH A O 6211 O O . HOH T . ? 0.4711 0.3385 0.2779 0.1384 -0.0196 -0.0210 1183 HOH A O 6212 O O . HOH T . ? 0.3268 0.3518 0.3308 0.0042 0.0200 -0.0334 1184 HOH A O 6213 O O . HOH T . ? 0.4872 0.5200 0.6924 -0.0027 -0.0348 -0.0412 1185 HOH A O 6214 O O . HOH T . ? 0.5470 0.5605 0.5197 0.0114 0.0124 -0.0406 1186 HOH A O 6215 O O . HOH T . ? 0.5068 0.4168 0.4664 0.0869 -0.1144 -0.0690 1187 HOH A O 6216 O O . HOH T . ? 0.4225 0.4224 0.4670 0.0088 -0.0089 -0.0534 1188 HOH A O 6217 O O . HOH T . ? 0.4829 0.4644 0.6225 0.0661 -0.1100 -0.1023 1189 HOH A O 6218 O O . HOH T . ? 0.5439 0.5511 0.5717 0.0294 0.0037 -0.0701 1190 HOH A O 6219 O O . HOH T . ? 0.5153 0.5159 0.4810 0.0301 -0.0051 -0.0653 1191 HOH A O 6220 O O . HOH T . ? 0.3824 0.3450 0.4469 0.0450 -0.0933 -0.0651 1192 HOH A O 6221 O O . HOH T . ? 0.6431 0.5862 0.7049 0.0547 -0.1188 -0.0720 1193 HOH A O 6222 O O . HOH T . ? 0.3722 0.3626 0.4571 0.0317 -0.0642 -0.0598 1194 HOH A O 6223 O O . HOH T . ? 0.3376 0.3311 0.4078 0.0070 0.0112 -0.0355 1195 HOH A O 6224 O O . HOH T . ? 0.3970 0.4369 0.4360 0.0375 0.0218 -0.0738 1196 HOH A O 6225 O O . HOH T . ? 0.2720 0.2759 0.2654 0.0059 0.0144 -0.0184 1197 HOH A O 6226 O O . HOH T . ? 0.3330 0.2676 0.2433 0.0704 -0.0318 -0.0282 1198 HOH A O 6227 O O . HOH T . ? 0.4195 0.3567 0.4024 0.0620 -0.0879 -0.0562 1199 HOH A O 6228 O O . HOH T . ? 0.4869 0.4171 0.4626 0.0609 0.0716 0.0242 1200 HOH A O 6229 O O . HOH T . ? 0.6360 0.6672 0.7712 -0.0184 0.0979 0.0520 1201 HOH A O 6230 O O . HOH T . ? 0.7211 0.6242 0.6262 0.1067 -0.0724 -0.0601 1202 HOH A O 6231 O O . HOH T . ? 0.2918 0.2824 0.2709 0.0164 -0.0057 -0.0203 1203 HOH A O 6232 O O . HOH T . ? 0.6386 0.6330 0.6800 0.0217 -0.0145 -0.0715 1204 HOH A O 6233 O O . HOH T . ? 0.4650 0.3358 0.3076 0.1351 -0.0637 -0.0515 1205 HOH A O 6234 O O . HOH T . ? 0.5909 0.6023 0.6124 -0.0036 0.0892 0.0428 1206 HOH A O 6235 O O . HOH T . ? 0.4817 0.3866 0.3984 0.1068 -0.0391 -0.0567 1207 HOH A O 6236 O O . HOH T . ? 0.3451 0.3325 0.3348 0.0193 0.0268 -0.0064 1208 HOH A O 6237 O O . HOH T . ? 0.3886 0.3097 0.2786 0.0857 -0.0168 -0.0246 1209 HOH A O 6239 O O . HOH T . ? 0.6769 0.5920 0.6622 0.1151 -0.1099 -0.0996 1211 HOH A O 6240 O O . HOH T . ? 0.4083 0.3082 0.2663 0.1064 -0.0231 -0.0254 1212 HOH A O 6241 O O . HOH T . ? 0.5724 0.6633 0.6789 0.0457 0.1320 -0.0142 1213 HOH A O 6242 O O . HOH T . ? 0.7080 0.6102 0.6070 0.0995 -0.0822 -0.0536 1214 HOH A O 6243 O O . HOH T . ? 0.4586 0.3915 0.4285 0.0626 -0.0872 -0.0522 1215 HOH A O 6244 O O . HOH T . ? 0.5753 0.5781 0.5698 0.0207 -0.0072 -0.0625 1216 HOH A O 6245 O O . HOH T . ? 0.5509 0.5563 0.6367 0.0527 -0.0453 -0.0825 1217 HOH A O 6246 O O . HOH T . ? 0.3729 0.3849 0.3835 -0.0117 0.0091 -0.0056 1218 HOH A O 6247 O O . HOH T . ? 0.5909 0.6278 0.5811 0.0173 0.0677 -0.0133 1219 HOH A O 6248 O O . HOH T . ? 0.3633 0.3035 0.3348 0.0684 -0.0737 -0.0573 1220 HOH A O 6249 O O . HOH T . ? 0.4243 0.4278 0.4979 -0.0007 0.0020 -0.0307 1221 HOH A O 6250 O O . HOH T . ? 0.4117 0.4072 0.4904 0.0570 -0.0554 -0.0833 1222 HOH A O 6251 O O . HOH T . ? 0.6037 0.4780 0.4769 0.1134 0.0267 -0.0045 1223 HOH A O 6252 O O . HOH T . ? 0.2980 0.2849 0.3076 0.0181 0.0352 -0.0023 1224 HOH A O 6253 O O . HOH T . ? 0.6739 0.6831 0.6416 0.0206 0.0071 -0.0517 1225 HOH A O 6254 O O . HOH T . ? 0.5705 0.5487 0.6470 0.0458 -0.0790 -0.0700 1226 HOH A O 6255 O O . HOH T . ? 0.4107 0.4321 0.4156 0.0033 0.0169 -0.0308 1227 HOH A O 6256 O O . HOH T . ? 0.5088 0.4783 0.6401 0.0701 -0.1224 -0.1035 1228 HOH A O 6257 O O . HOH T . ? 0.3333 0.3540 0.4380 -0.0214 0.0139 0.0044 1229 HOH A O 6258 O O . HOH T . ? 0.7078 0.6226 0.6341 0.0974 -0.0710 -0.0617 1230 HOH A O 6259 O O . HOH T . ? 0.4367 0.3507 0.3418 0.0871 -0.0689 -0.0449 1231 HOH A O 6260 O O . HOH T . ? 0.3835 0.4121 0.4059 -0.0072 0.0258 -0.0132 1232 HOH A O 6261 O O . HOH T . ? 0.6046 0.6444 0.6985 -0.0038 0.1119 0.0427 1233 HOH A O 6262 O O . HOH T . ? 0.4422 0.3895 0.3611 0.0601 0.0135 -0.0063 1234 HOH A O 6263 O O . HOH T . ? 0.5495 0.4264 0.4245 0.1161 0.0030 -0.0227 1235 HOH A O 6264 O O . HOH T . ? 0.4400 0.3211 0.3033 0.1255 -0.0720 -0.0559 1236 HOH A O 6265 O O . HOH T . ? 0.7359 0.7490 0.8286 -0.0210 0.0727 0.0471 1237 HOH A O 6266 O O . HOH T . ? 0.4308 0.4563 0.4498 0.0086 0.0164 -0.0381 1238 HOH A O 6267 O O . HOH T . ? 0.2243 0.2313 0.2245 0.0110 0.0123 -0.0284 1239 HOH A O 6268 O O . HOH T . ? 0.7524 0.7722 0.7350 0.0093 0.0812 0.0179 1240 HOH A O 6269 O O . HOH T . ? 0.2796 0.2496 0.2364 0.0373 0.0254 -0.0021 1241 HOH A O 6270 O O . HOH T . ? 0.2879 0.2478 0.2319 0.0478 0.0304 0.0025 1242 HOH A O 6271 O O . HOH T . ? 0.5313 0.5370 0.5699 0.0431 -0.0037 -0.0710 1243 HOH A O 6272 O O . HOH T . ? 0.6758 0.5874 0.5941 0.0975 -0.0737 -0.0590 1244 HOH A O 6273 O O . HOH T . ? 0.5837 0.6062 0.6946 0.0426 -0.0361 -0.0796 1245 HOH A O 6274 O O . HOH T . ? 0.6591 0.5892 0.6246 0.0631 0.0285 -0.0154 1246 HOH A O 6275 O O . HOH T . ? 0.5177 0.5523 0.5389 -0.0001 0.0286 -0.0247 1247 HOH A O 6276 O O . HOH T . ? 0.6477 0.6705 0.6110 0.0674 0.0274 -0.0858 1248 HOH A O 6277 O O . HOH T . ? 0.4811 0.4978 0.5379 -0.0177 0.0523 0.0263 1249 HOH A O 6278 O O . HOH T . ? 0.5780 0.6363 0.7779 -0.0156 0.0290 -0.0107 1250 HOH A O 6279 O O . HOH T . ? 0.6132 0.6357 0.8254 0.0392 -0.0807 -0.0908 1251 HOH A O 6280 O O . HOH T . ? 0.5253 0.5663 0.6295 0.0416 -0.0073 -0.0813 1252 HOH A O 6281 O O . HOH T . ? 0.5321 0.3962 0.3711 0.1414 -0.0602 -0.0527 1253 HOH A O 6282 O O . HOH T . ? 0.5234 0.5061 0.5616 0.0169 0.0396 -0.0045 1254 HOH A O 6283 O O . HOH T . ? 0.6207 0.5322 0.5567 0.1079 -0.0656 -0.0719 1255 HOH A O 6284 O O . HOH T . ? 0.5060 0.4871 0.5893 0.0114 0.0348 -0.0116 1256 HOH A O 6285 O O . HOH T . ? 0.3137 0.2637 0.2398 0.0575 0.0244 -0.0002 1257 HOH A O 6286 O O . HOH T . ? 0.7314 0.7493 0.7195 0.0041 0.0749 0.0194 1258 HOH A O 6287 O O . HOH T . ? 0.3169 0.2889 0.2958 0.0387 0.0137 -0.0268 1259 HOH A O 6288 O O . HOH T . ? 0.2996 0.3159 0.3205 0.0270 0.0096 -0.0663 1260 HOH A O 6289 O O . HOH T . ? 0.4176 0.4327 0.5361 0.0226 -0.0449 -0.0593 1261 HOH A O 6290 O O . HOH T . ? 0.3492 0.3818 0.3785 0.0100 0.0194 -0.0413 1262 HOH A O 6291 O O . HOH T . ? 0.5846 0.4404 0.4219 0.1501 -0.0726 -0.0613 1263 HOH A O 6292 O O . HOH T . ? 0.3456 0.3552 0.3475 0.0305 0.0016 -0.0723 1264 HOH A O 6293 O O . HOH T . ? 0.7610 0.7012 0.7840 0.0434 0.0442 -0.0055 1265 HOH A O 6294 O O . HOH T . ? 0.5949 0.6056 0.7316 0.0174 -0.0548 -0.0561 1266 HOH A O 6297 O O . HOH T . ? 0.6141 0.6554 0.8388 -0.0154 -0.0114 -0.0226 1269 HOH A O 6298 O O . HOH T . ? 0.3398 0.3641 0.3941 -0.0085 0.0072 -0.0163 1270 HOH A O 6299 O O . HOH T . ? 0.5171 0.4529 0.5650 0.0709 -0.1253 -0.0828 1271 HOH A O 6300 O O . HOH T . ? 0.5372 0.3975 0.3420 0.1432 -0.0197 -0.0233 1272 HOH A O 6301 O O . HOH T . ? 0.4372 0.4684 0.5280 0.0081 -0.0078 -0.0421 1273 HOH A O 6302 O O . HOH T . ? 0.5555 0.6054 0.6059 0.0035 0.0486 -0.0217 1274 HOH A O 6303 O O . HOH T . ? 0.4413 0.4579 0.4385 -0.0073 0.0138 -0.0131 1275 HOH A O 6304 O O . HOH T . ? 0.6758 0.6046 0.6279 0.0875 -0.0274 -0.0572 1276 HOH A O 6305 O O . HOH T . ? 0.6777 0.7031 0.6545 0.0135 0.0308 -0.0349 1277 HOH A O 6306 O O . HOH T . ? 0.5538 0.6305 0.6817 0.0259 0.0411 -0.0575 1278 HOH A O 6307 O O . HOH T . ? 0.6361 0.6604 0.6130 0.0099 0.0296 -0.0312 1279 HOH A O 6308 O O . HOH T . ? 0.2817 0.2825 0.2781 0.0069 0.0173 -0.0139 1280 HOH A O 6309 O O . HOH T . ? 0.3501 0.3427 0.3282 0.0152 0.0001 -0.0185 1281 HOH A O 6310 O O . HOH T . ? 0.6754 0.6440 0.7488 0.0479 -0.0906 -0.0704 1282 HOH A O 6311 O O . HOH T . ? 0.4468 0.4584 0.4840 0.0397 0.0030 -0.0772 1283 HOH A O 6312 O O . HOH T . ? 0.3958 0.3682 0.4824 0.0391 -0.0895 -0.0653 1284 HOH A O 6313 O O . HOH T . ? 0.6346 0.6726 0.6472 0.0425 0.0290 -0.0730 1285 HOH A O 6314 O O . HOH T . ? 0.5660 0.5677 0.6263 0.0024 -0.0050 -0.0419 1286 HOH A O 6315 O O . HOH T . ? 0.3799 0.3783 0.5253 0.0099 -0.0671 -0.0479 1287 HOH A O 6316 O O . HOH T . ? 0.7509 0.6627 0.7423 0.0934 -0.1299 -0.0851 1288 HOH A O 6317 O O . HOH T . ? 0.5389 0.5512 0.6515 0.0501 -0.0515 -0.0855 1289 HOH A O 6318 O O . HOH T . ? 0.4958 0.4285 0.4995 0.0522 0.0675 0.0183 1290 HOH A O 6319 O O . HOH T . ? 0.3079 0.3230 0.3298 0.0205 0.0118 -0.0498 1291 HOH A O 6320 O O . HOH T . ? 0.6649 0.6885 0.6192 0.0768 0.0337 -0.0878 1292 HOH A O 6321 O O . HOH T . ? 0.5708 0.5899 0.5622 -0.0004 0.0166 -0.0259 1293 HOH A O 6322 O O . HOH T . ? 0.6917 0.6563 0.7125 0.0278 -0.0672 -0.0391 1294 HOH A O 6323 O O . HOH T . ? 0.7565 0.7528 0.7418 0.0175 -0.0180 -0.0575 1295 HOH A O 6324 O O . HOH T . ? 0.4264 0.3903 0.4019 0.0436 0.0172 -0.0243 1296 HOH A O 6325 O O . HOH T . ? 0.6175 0.6492 0.7118 -0.0095 0.1033 0.0465 1297 HOH A O 6326 O O . HOH T . ? 0.6193 0.6226 0.6083 0.0191 -0.0062 -0.0591 1298 HOH A O 6327 O O . HOH T . ? 0.4322 0.4666 0.5640 0.0007 -0.0131 -0.0375 1299 HOH A O 6328 O O . HOH T . ? 0.5992 0.4623 0.4492 0.1411 -0.1001 -0.0673 1300 HOH A O 6329 O O . HOH T . ? 0.4990 0.5151 0.6927 -0.0149 -0.0353 -0.0218 1301 HOH A O 6330 O O . HOH T . ? 0.6784 0.7023 0.6652 0.0000 0.0276 -0.0202 1302 HOH A O 6331 O O . HOH T . ? 0.5980 0.6430 0.8332 -0.0129 -0.0137 -0.0277 1303 HOH A O 6332 O O . HOH T . ? 0.6413 0.4626 0.4042 0.1830 -0.0948 -0.0592 1304 HOH A O 6333 O O . HOH T . ? 0.2747 0.2820 0.2693 0.0023 0.0133 -0.0189 1305 HOH A O 6334 O O . HOH T . ? 0.5932 0.4293 0.3432 0.1732 -0.0268 -0.0208 1306 HOH A O 6335 O O . HOH T . ? 0.6765 0.6173 0.6974 0.0432 0.0511 0.0017 1307 HOH A O 6336 O O . HOH T . ? 0.6408 0.6243 0.6847 0.0249 0.0099 -0.0489 1308 HOH A O 6337 O O . HOH T . ? 0.3874 0.4331 0.5936 -0.0109 -0.0067 -0.0273 1309 HOH A O 6338 O O . HOH T . ? 0.5695 0.5693 0.6057 0.0175 0.0057 -0.0543 1310 HOH A O 6339 O O . HOH T . ? 0.6926 0.5308 0.4879 0.1653 -0.0968 -0.0611 1311 HOH A O 6340 O O . HOH T . ? 0.4164 0.4175 0.5795 -0.0035 -0.0577 -0.0340 1312 HOH A O 6341 O O . HOH T . ? 0.4111 0.4305 0.4403 -0.0069 0.0068 -0.0162 1313 HOH A O 6342 O O . HOH T . ? 0.7954 0.6404 0.6166 0.1520 -0.0323 -0.0394 1314 HOH A O 6343 O O . HOH T . ? 0.6670 0.6943 0.6633 0.0499 0.0204 -0.0816 1315 HOH A O 6344 O O . HOH T . ? 0.5865 0.6129 0.7161 0.0150 -0.0318 -0.0538 1316 HOH A O 6345 O O . HOH T . ? 0.7451 0.7584 0.7334 -0.0011 0.0107 -0.0254 1317 HOH A O 6346 O O . HOH T . ? 0.3038 0.3070 0.2931 0.0067 0.0117 -0.0181 1318 HOH A O 6347 O O . HOH T . ? 0.7032 0.7192 0.6711 0.0108 0.0187 -0.0355 1319 HOH A O 6348 O O . HOH T . ? 0.7258 0.6828 0.7673 0.0326 0.0610 0.0121 1320 HOH A O 6349 O O . HOH T . ? 0.5330 0.5351 0.6106 0.0001 -0.0049 -0.0374 1321 HOH A O 6350 O O . HOH T . ? 0.5579 0.5633 0.7348 -0.0016 -0.0593 -0.0387 1322 HOH A O 6351 O O . HOH T . ? 0.7043 0.7389 0.9592 0.0189 -0.0686 -0.0746 1323 HOH A O 6352 O O . HOH T . ? 0.5331 0.3945 0.3386 0.1408 -0.0013 -0.0125 1324 HOH A O 6353 O O . HOH T . ? 0.4779 0.4678 0.5054 0.0140 0.0360 -0.0031 1325 HOH A O 6354 O O . HOH T . ? 0.7243 0.7444 0.7171 0.0504 0.0125 -0.0852 1326 HOH A O 6355 O O . HOH T . ? 0.6282 0.5876 0.7290 0.0422 -0.1120 -0.0701 1327 HOH A O 6356 O O . HOH T . ? 0.1492 0.1570 0.1405 0.0023 0.0114 -0.0189 1328 HOH A O 6357 O O . HOH T . ? 0.5926 0.5747 0.6335 0.0650 -0.0451 -0.0804 1329 HOH A O 6358 O O . HOH T . ? 0.6231 0.5445 0.6048 0.0736 -0.1106 -0.0653 1330 HOH A O 6359 O O . HOH T . ? 0.5815 0.6184 0.6198 0.0082 0.0210 -0.0393 1331 HOH A O 6360 O O . HOH T . ? 0.3666 0.3356 0.4581 0.0454 -0.0978 -0.0720 1332 HOH A O 6361 O O . HOH T . ? 0.5416 0.5787 0.5697 0.0409 0.0221 -0.0765 1333 HOH A O 6362 O O . HOH T . ? 0.4740 0.4242 0.3948 0.0566 -0.0024 -0.0138 1334 HOH A O 6363 O O . HOH T . ? 0.5542 0.6013 0.8382 -0.0247 -0.0008 -0.0099 1335 HOH A O 6364 O O . HOH T . ? 0.5460 0.5332 0.6924 0.0177 -0.0851 -0.0557 1336 HOH A O 6365 O O . HOH T . ? 0.5169 0.5126 0.6943 0.0560 -0.1064 -0.1007 1337 HOH A O 6366 O O . HOH T . ? 0.5739 0.6291 0.8274 -0.0236 0.0235 -0.0027 1338 HOH A O 6367 O O . HOH T . ? 0.5084 0.5203 0.6247 -0.0199 -0.0083 -0.0029 1339 HOH A O 6368 O O . HOH T . ? 0.4547 0.4826 0.4776 -0.0085 0.0431 0.0009 1340 HOH A O 6369 O O . HOH T . ? 0.5003 0.5064 0.5276 0.0327 0.0007 -0.0756 1341 HOH A O 6370 O O . HOH T . ? 0.4813 0.5241 0.5968 0.0285 -0.0090 -0.0683 1342 HOH A O 6371 O O . HOH T . ? 0.6547 0.6750 0.6746 0.0414 0.0085 -0.0820 1343 HOH A O 6372 O O . HOH T . ? 0.5157 0.5215 0.5377 0.0295 -0.0004 -0.0735 1344 HOH A O 6373 O O . HOH T . ? 0.5959 0.6135 0.8294 -0.0189 -0.0383 -0.0200 1345 HOH A O 6374 O O . HOH T . ? 0.6344 0.5977 0.6566 0.0354 0.0223 -0.0303 1346 HOH A O 6375 O O . HOH T . ? 0.6790 0.7349 0.7652 -0.0019 0.0572 -0.0110 1347 HOH A O 6377 O O . HOH T . ? 0.4320 0.4151 0.4614 0.0192 0.0439 0.0025 1349 HOH A O 6378 O O . HOH T . ? 0.5278 0.5588 0.5575 0.0083 0.0174 -0.0387 1350 HOH A O 6379 O O . HOH T . ? 0.3845 0.4079 0.3967 0.0068 0.0171 -0.0358 1351 HOH A O 6380 O O . HOH T . ? 0.5223 0.4905 0.6403 0.0733 -0.1181 -0.1035 1352 HOH A O 6381 O O . HOH T . ? 0.5820 0.6376 0.6780 -0.0039 0.0729 0.0031 1353 HOH A O 6382 O O . HOH T . ? 0.5595 0.5993 0.7373 -0.0025 -0.0175 -0.0379 1354 HOH A O 6383 O O . HOH T . ? 0.6439 0.4912 0.4394 0.1559 -0.0436 -0.0377 1355 HOH A O 6384 O O . HOH T . ? 0.7073 0.7223 0.9157 -0.0098 -0.0481 -0.0315 1356 HOH A O 6385 O O . HOH T . ? 0.4986 0.5088 0.4936 -0.0014 0.0074 -0.0249 1357 HOH A O 6386 O O . HOH T . ? 0.6609 0.5737 0.5950 0.1046 -0.0500 -0.0658 1358 HOH A O 6387 O O . HOH T . ? 0.6462 0.6267 0.7670 0.0321 -0.0913 -0.0659 1359 HOH A O 6388 O O . HOH T . ? 0.4115 0.4124 0.5232 0.0262 -0.0610 -0.0603 1360 HOH A O 6389 O O . HOH T . ? 0.5271 0.5301 0.5655 0.0428 -0.0010 -0.0798 1361 HOH A O 6390 O O . HOH T . ? 0.4101 0.3364 0.3675 0.0972 -0.0569 -0.0720 1362 HOH A O 6391 O O . HOH T . ? 0.6782 0.5296 0.4949 0.1534 -0.0744 -0.0559 1363 HOH A O 6392 O O . HOH T . ? 0.5763 0.4368 0.4079 0.1422 -0.0934 -0.0589 1364 HOH A O 6393 O O . HOH T . ? 0.6472 0.4824 0.4294 0.1682 -0.0598 -0.0460 1365 HOH A O 6394 O O . HOH T . ? 0.7833 0.6110 0.5733 0.1761 -0.0894 -0.0642 1366 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 LYS 1 55 55 LYS LYS A . n A 1 2 HIS 2 56 56 HIS HIS A . n A 1 3 ASN 3 57 57 ASN ASN A . n A 1 4 MET 4 58 58 MET MET A . n A 1 5 LYS 5 59 59 LYS LYS A . n A 1 6 ALA 6 60 60 ALA ALA A . n A 1 7 PHE 7 61 61 PHE PHE A . n A 1 8 LEU 8 62 62 LEU LEU A . n A 1 9 ASP 9 63 63 ASP ASP A . n A 1 10 GLU 10 64 64 GLU GLU A . n A 1 11 LEU 11 65 65 LEU LEU A . n A 1 12 LYS 12 66 66 LYS LYS A . n A 1 13 ALA 13 67 67 ALA ALA A . n A 1 14 GLU 14 68 68 GLU GLU A . n A 1 15 ASN 15 69 69 ASN ASN A . n A 1 16 ILE 16 70 70 ILE ILE A . n A 1 17 LYS 17 71 71 LYS LYS A . n A 1 18 LYS 18 72 72 LYS LYS A . n A 1 19 PHE 19 73 73 PHE PHE A . n A 1 20 LEU 20 74 74 LEU LEU A . n A 1 21 TYR 21 75 75 TYR TYR A . n A 1 22 ASN 22 76 76 ASN ASN A . n A 1 23 PHE 23 77 77 PHE PHE A . n A 1 24 THR 24 78 78 THR THR A . n A 1 25 GLN 25 79 79 GLN GLN A . n A 1 26 ILE 26 80 80 ILE ILE A . n A 1 27 PRO 27 81 81 PRO PRO A . n A 1 28 HIS 28 82 82 HIS HIS A . n A 1 29 LEU 29 83 83 LEU LEU A . n A 1 30 ALA 30 84 84 ALA ALA A . n A 1 31 GLY 31 85 85 GLY GLY A . n A 1 32 THR 32 86 86 THR THR A . n A 1 33 GLU 33 87 87 GLU GLU A . n A 1 34 GLN 34 88 88 GLN GLN A . n A 1 35 ASN 35 89 89 ASN ASN A . n A 1 36 PHE 36 90 90 PHE PHE A . n A 1 37 GLN 37 91 91 GLN GLN A . n A 1 38 LEU 38 92 92 LEU LEU A . n A 1 39 ALA 39 93 93 ALA ALA A . n A 1 40 LYS 40 94 94 LYS LYS A . n A 1 41 GLN 41 95 95 GLN GLN A . n A 1 42 ILE 42 96 96 ILE ILE A . n A 1 43 GLN 43 97 97 GLN GLN A . n A 1 44 SER 44 98 98 SER SER A . n A 1 45 GLN 45 99 99 GLN GLN A . n A 1 46 TRP 46 100 100 TRP TRP A . n A 1 47 LYS 47 101 101 LYS LYS A . n A 1 48 GLU 48 102 102 GLU GLU A . n A 1 49 PHE 49 103 103 PHE PHE A . n A 1 50 GLY 50 104 104 GLY GLY A . n A 1 51 LEU 51 105 105 LEU LEU A . n A 1 52 ASP 52 106 106 ASP ASP A . n A 1 53 SER 53 107 107 SER SER A . n A 1 54 VAL 54 108 108 VAL VAL A . n A 1 55 GLU 55 109 109 GLU GLU A . n A 1 56 LEU 56 110 110 LEU LEU A . n A 1 57 ALA 57 111 111 ALA ALA A . n A 1 58 HIS 58 112 112 HIS HIS A . n A 1 59 TYR 59 113 113 TYR TYR A . n A 1 60 ASP 60 114 114 ASP ASP A . n A 1 61 VAL 61 115 115 VAL VAL A . n A 1 62 LEU 62 116 116 LEU LEU A . n A 1 63 LEU 63 117 117 LEU LEU A . n A 1 64 SER 64 118 118 SER SER A . n A 1 65 TYR 65 119 119 TYR TYR A . n A 1 66 PRO 66 120 120 PRO PRO A . n A 1 67 ASN 67 121 121 ASN ASN A . n A 1 68 LYS 68 122 122 LYS LYS A . n A 1 69 THR 69 123 123 THR THR A . n A 1 70 HIS 70 124 124 HIS HIS A . n A 1 71 PRO 71 125 125 PRO PRO A . n A 1 72 ASN 72 126 126 ASN ASN A . n A 1 73 TYR 73 127 127 TYR TYR A . n A 1 74 ILE 74 128 128 ILE ILE A . n A 1 75 SER 75 129 129 SER SER A . n A 1 76 ILE 76 130 130 ILE ILE A . n A 1 77 ILE 77 131 131 ILE ILE A . n A 1 78 ASN 78 132 ? ? ? A . n A 1 79 GLU 79 133 ? ? ? A . n A 1 80 ASP 80 134 ? ? ? A . n A 1 81 GLY 81 135 ? ? ? A . n A 1 82 ASN 82 136 136 ASN ASN A . n A 1 83 GLU 83 137 137 GLU GLU A . n A 1 84 ILE 84 138 138 ILE ILE A . n A 1 85 PHE 85 139 139 PHE PHE A . n A 1 86 ASN 86 140 140 ASN ASN A . n A 1 87 THR 87 141 141 THR THR A . n A 1 88 SER 88 142 142 SER SER A . n A 1 89 LEU 89 143 143 LEU LEU A . n A 1 90 PHE 90 144 144 PHE PHE A . n A 1 91 GLU 91 145 145 GLU GLU A . n A 1 92 PRO 92 146 146 PRO PRO A . n A 1 93 PRO 93 147 147 PRO PRO A . n A 1 94 PRO 94 148 148 PRO PRO A . n A 1 95 PRO 95 149 149 PRO PRO A . n A 1 96 GLY 96 150 150 GLY GLY A . n A 1 97 TYR 97 151 151 TYR TYR A . n A 1 98 GLU 98 152 152 GLU GLU A . n A 1 99 ASN 99 153 153 ASN ASN A . n A 1 100 VAL 100 154 154 VAL VAL A . n A 1 101 SER 101 155 155 SER SER A . n A 1 102 ASP 102 156 156 ASP ASP A . n A 1 103 ILE 103 157 157 ILE ILE A . n A 1 104 VAL 104 158 158 VAL VAL A . n A 1 105 PRO 105 159 159 PRO PRO A . n A 1 106 PRO 106 160 160 PRO PRO A . n A 1 107 PHE 107 161 161 PHE PHE A . n A 1 108 SER 108 162 162 SER SER A . n A 1 109 ALA 109 163 163 ALA ALA A . n A 1 110 PHE 110 164 164 PHE PHE A . n A 1 111 SER 111 165 165 SER SER A . n A 1 112 PRO 112 166 166 PRO PRO A . n A 1 113 GLN 113 167 167 GLN GLN A . n A 1 114 GLY 114 168 168 GLY GLY A . n A 1 115 MET 115 169 169 MET MET A . n A 1 116 PRO 116 170 170 PRO PRO A . n A 1 117 GLU 117 171 171 GLU GLU A . n A 1 118 GLY 118 172 172 GLY GLY A . n A 1 119 ASP 119 173 173 ASP ASP A . n A 1 120 LEU 120 174 174 LEU LEU A . n A 1 121 VAL 121 175 175 VAL VAL A . n A 1 122 TYR 122 176 176 TYR TYR A . n A 1 123 VAL 123 177 177 VAL VAL A . n A 1 124 ASN 124 178 178 ASN ASN A . n A 1 125 TYR 125 179 179 TYR TYR A . n A 1 126 ALA 126 180 180 ALA ALA A . n A 1 127 ARG 127 181 181 ARG ARG A . n A 1 128 THR 128 182 182 THR THR A . n A 1 129 GLU 129 183 183 GLU GLU A . n A 1 130 ASP 130 184 184 ASP ASP A . n A 1 131 PHE 131 185 185 PHE PHE A . n A 1 132 PHE 132 186 186 PHE PHE A . n A 1 133 LYS 133 187 187 LYS LYS A . n A 1 134 LEU 134 188 188 LEU LEU A . n A 1 135 GLU 135 189 189 GLU GLU A . n A 1 136 ARG 136 190 190 ARG ARG A . n A 1 137 ASP 137 191 191 ASP ASP A . n A 1 138 MET 138 192 192 MET MET A . n A 1 139 LYS 139 193 193 LYS LYS A . n A 1 140 ILE 140 194 194 ILE ILE A . n A 1 141 ASN 141 195 195 ASN ASN A . n A 1 142 CYS 142 196 196 CYS CYS A . n A 1 143 SER 143 197 197 SER SER A . n A 1 144 GLY 144 198 198 GLY GLY A . n A 1 145 LYS 145 199 199 LYS LYS A . n A 1 146 ILE 146 200 200 ILE ILE A . n A 1 147 VAL 147 201 201 VAL VAL A . n A 1 148 ILE 148 202 202 ILE ILE A . n A 1 149 ALA 149 203 203 ALA ALA A . n A 1 150 ARG 150 204 204 ARG ARG A . n A 1 151 TYR 151 205 205 TYR TYR A . n A 1 152 GLY 152 206 206 GLY GLY A . n A 1 153 LYS 153 207 207 LYS LYS A . n A 1 154 VAL 154 208 208 VAL VAL A . n A 1 155 PHE 155 209 209 PHE PHE A . n A 1 156 ARG 156 210 210 ARG ARG A . n A 1 157 GLY 157 211 211 GLY GLY A . n A 1 158 ASN 158 212 212 ASN ASN A . n A 1 159 LYS 159 213 213 LYS LYS A . n A 1 160 VAL 160 214 214 VAL VAL A . n A 1 161 LYS 161 215 215 LYS LYS A . n A 1 162 ASN 162 216 216 ASN ASN A . n A 1 163 ALA 163 217 217 ALA ALA A . n A 1 164 GLN 164 218 218 GLN GLN A . n A 1 165 LEU 165 219 219 LEU LEU A . n A 1 166 ALA 166 220 220 ALA ALA A . n A 1 167 GLY 167 221 221 GLY GLY A . n A 1 168 ALA 168 222 222 ALA ALA A . n A 1 169 LYS 169 223 223 LYS LYS A . n A 1 170 GLY 170 224 224 GLY GLY A . n A 1 171 VAL 171 225 225 VAL VAL A . n A 1 172 ILE 172 226 226 ILE ILE A . n A 1 173 LEU 173 227 227 LEU LEU A . n A 1 174 TYR 174 228 228 TYR TYR A . n A 1 175 SER 175 229 229 SER SER A . n A 1 176 ASP 176 230 230 ASP ASP A . n A 1 177 PRO 177 231 231 PRO PRO A . n A 1 178 ALA 178 232 232 ALA ALA A . n A 1 179 ASP 179 233 233 ASP ASP A . n A 1 180 TYR 180 234 234 TYR TYR A . n A 1 181 PHE 181 235 235 PHE PHE A . n A 1 182 ALA 182 236 236 ALA ALA A . n A 1 183 PRO 183 237 237 PRO PRO A . n A 1 184 GLY 184 238 238 GLY GLY A . n A 1 185 VAL 185 239 239 VAL VAL A . n A 1 186 LYS 186 240 240 LYS LYS A . n A 1 187 SER 187 241 241 SER SER A . n A 1 188 TYR 188 242 242 TYR TYR A . n A 1 189 PRO 189 243 243 PRO PRO A . n A 1 190 ASP 190 244 244 ASP ASP A . n A 1 191 GLY 191 245 245 GLY GLY A . n A 1 192 TRP 192 246 246 TRP TRP A . n A 1 193 ASN 193 247 247 ASN ASN A . n A 1 194 LEU 194 248 248 LEU LEU A . n A 1 195 PRO 195 249 249 PRO PRO A . n A 1 196 GLY 196 250 250 GLY GLY A . n A 1 197 GLY 197 251 251 GLY GLY A . n A 1 198 GLY 198 252 252 GLY GLY A . n A 1 199 VAL 199 253 253 VAL VAL A . n A 1 200 GLN 200 254 254 GLN GLN A . n A 1 201 ARG 201 255 255 ARG ARG A . n A 1 202 GLY 202 256 256 GLY GLY A . n A 1 203 ASN 203 257 257 ASN ASN A . n A 1 204 ILE 204 258 258 ILE ILE A . n A 1 205 LEU 205 259 259 LEU LEU A . n A 1 206 ASN 206 260 260 ASN ASN A . n A 1 207 LEU 207 261 261 LEU LEU A . n A 1 208 ASN 208 262 262 ASN ASN A . n A 1 209 GLY 209 263 263 GLY GLY A . n A 1 210 ALA 210 264 264 ALA ALA A . n A 1 211 GLY 211 265 265 GLY GLY A . n A 1 212 ASP 212 266 266 ASP ASP A . n A 1 213 PRO 213 267 267 PRO PRO A . n A 1 214 LEU 214 268 268 LEU LEU A . n A 1 215 THR 215 269 269 THR THR A . n A 1 216 PRO 216 270 270 PRO PRO A . n A 1 217 GLY 217 271 271 GLY GLY A . n A 1 218 TYR 218 272 272 TYR TYR A . n A 1 219 PRO 219 273 273 PRO PRO A . n A 1 220 ALA 220 274 274 ALA ALA A . n A 1 221 ASN 221 275 275 ASN ASN A . n A 1 222 GLU 222 276 276 GLU GLU A . n A 1 223 TYR 223 277 277 TYR TYR A . n A 1 224 ALA 224 278 278 ALA ALA A . n A 1 225 TYR 225 279 279 TYR TYR A . n A 1 226 ARG 226 280 280 ARG ARG A . n A 1 227 ARG 227 281 281 ARG ARG A . n A 1 228 GLY 228 282 282 GLY GLY A . n A 1 229 ILE 229 283 283 ILE ILE A . n A 1 230 ALA 230 284 284 ALA ALA A . n A 1 231 GLU 231 285 285 GLU GLU A . n A 1 232 ALA 232 286 286 ALA ALA A . n A 1 233 VAL 233 287 287 VAL VAL A . n A 1 234 GLY 234 288 288 GLY GLY A . n A 1 235 LEU 235 289 289 LEU LEU A . n A 1 236 PRO 236 290 290 PRO PRO A . n A 1 237 SER 237 291 291 SER SER A . n A 1 238 ILE 238 292 292 ILE ILE A . n A 1 239 PRO 239 293 293 PRO PRO A . n A 1 240 VAL 240 294 294 VAL VAL A . n A 1 241 HIS 241 295 295 HIS HIS A . n A 1 242 PRO 242 296 296 PRO PRO A . n A 1 243 ILE 243 297 297 ILE ILE A . n A 1 244 GLY 244 298 298 GLY GLY A . n A 1 245 TYR 245 299 299 TYR TYR A . n A 1 246 TYR 246 300 300 TYR TYR A . n A 1 247 ASP 247 301 301 ASP ASP A . n A 1 248 ALA 248 302 302 ALA ALA A . n A 1 249 GLN 249 303 303 GLN GLN A . n A 1 250 LYS 250 304 304 LYS LYS A . n A 1 251 LEU 251 305 305 LEU LEU A . n A 1 252 LEU 252 306 306 LEU LEU A . n A 1 253 GLU 253 307 307 GLU GLU A . n A 1 254 LYS 254 308 308 LYS LYS A . n A 1 255 MET 255 309 309 MET MET A . n A 1 256 GLY 256 310 310 GLY GLY A . n A 1 257 GLY 257 311 311 GLY GLY A . n A 1 258 SER 258 312 312 SER SER A . n A 1 259 ALA 259 313 313 ALA ALA A . n A 1 260 PRO 260 314 314 PRO PRO A . n A 1 261 PRO 261 315 315 PRO PRO A . n A 1 262 ASP 262 316 316 ASP ASP A . n A 1 263 SER 263 317 317 SER SER A . n A 1 264 SER 264 318 318 SER SER A . n A 1 265 TRP 265 319 319 TRP TRP A . n A 1 266 ARG 266 320 320 ARG ARG A . n A 1 267 GLY 267 321 321 GLY GLY A . n A 1 268 SER 268 322 322 SER SER A . n A 1 269 LEU 269 323 323 LEU LEU A . n A 1 270 LYS 270 324 324 LYS LYS A . n A 1 271 VAL 271 325 325 VAL VAL A . n A 1 272 PRO 272 326 326 PRO PRO A . n A 1 273 TYR 273 327 327 TYR TYR A . n A 1 274 ASN 274 328 328 ASN ASN A . n A 1 275 VAL 275 329 329 VAL VAL A . n A 1 276 GLY 276 330 330 GLY GLY A . n A 1 277 PRO 277 331 331 PRO PRO A . n A 1 278 GLY 278 332 332 GLY GLY A . n A 1 279 PHE 279 333 333 PHE PHE A . n A 1 280 THR 280 334 334 THR THR A . n A 1 281 GLY 281 335 335 GLY GLY A . n A 1 282 ASN 282 336 336 ASN ASN A . n A 1 283 PHE 283 337 337 PHE PHE A . n A 1 284 SER 284 338 338 SER SER A . n A 1 285 THR 285 339 339 THR THR A . n A 1 286 GLN 286 340 340 GLN GLN A . n A 1 287 LYS 287 341 341 LYS LYS A . n A 1 288 VAL 288 342 342 VAL VAL A . n A 1 289 LYS 289 343 343 LYS LYS A . n A 1 290 MET 290 344 344 MET MET A . n A 1 291 HIS 291 345 345 HIS HIS A . n A 1 292 ILE 292 346 346 ILE ILE A . n A 1 293 HIS 293 347 347 HIS HIS A . n A 1 294 SER 294 348 348 SER SER A . n A 1 295 THR 295 349 349 THR THR A . n A 1 296 ASN 296 350 350 ASN ASN A . n A 1 297 GLU 297 351 351 GLU GLU A . n A 1 298 VAL 298 352 352 VAL VAL A . n A 1 299 THR 299 353 353 THR THR A . n A 1 300 ARG 300 354 354 ARG ARG A . n A 1 301 ILE 301 355 355 ILE ILE A . n A 1 302 TYR 302 356 356 TYR TYR A . n A 1 303 ASN 303 357 357 ASN ASN A . n A 1 304 VAL 304 358 358 VAL VAL A . n A 1 305 ILE 305 359 359 ILE ILE A . n A 1 306 GLY 306 360 360 GLY GLY A . n A 1 307 THR 307 361 361 THR THR A . n A 1 308 LEU 308 362 362 LEU LEU A . n A 1 309 ARG 309 363 363 ARG ARG A . n A 1 310 GLY 310 364 364 GLY GLY A . n A 1 311 ALA 311 365 365 ALA ALA A . n A 1 312 VAL 312 366 366 VAL VAL A . n A 1 313 GLU 313 367 367 GLU GLU A . n A 1 314 PRO 314 368 368 PRO PRO A . n A 1 315 ASP 315 369 369 ASP ASP A . n A 1 316 ARG 316 370 370 ARG ARG A . n A 1 317 TYR 317 371 371 TYR TYR A . n A 1 318 VAL 318 372 372 VAL VAL A . n A 1 319 ILE 319 373 373 ILE ILE A . n A 1 320 LEU 320 374 374 LEU LEU A . n A 1 321 GLY 321 375 375 GLY GLY A . n A 1 322 GLY 322 376 376 GLY GLY A . n A 1 323 HIS 323 377 377 HIS HIS A . n A 1 324 ARG 324 378 378 ARG ARG A . n A 1 325 ASP 325 379 379 ASP ASP A . n A 1 326 SER 326 380 380 SER SER A . n A 1 327 TRP 327 381 381 TRP TRP A . n A 1 328 VAL 328 382 382 VAL VAL A . n A 1 329 PHE 329 383 383 PHE PHE A . n A 1 330 GLY 330 384 384 GLY GLY A . n A 1 331 GLY 331 385 385 GLY GLY A . n A 1 332 ILE 332 386 386 ILE ILE A . n A 1 333 ASP 333 387 387 ASP ASP A . n A 1 334 PRO 334 388 388 PRO PRO A . n A 1 335 GLN 335 389 389 GLN GLN A . n A 1 336 SER 336 390 390 SER SER A . n A 1 337 GLY 337 391 391 GLY GLY A . n A 1 338 ALA 338 392 392 ALA ALA A . n A 1 339 ALA 339 393 393 ALA ALA A . n A 1 340 VAL 340 394 394 VAL VAL A . n A 1 341 VAL 341 395 395 VAL VAL A . n A 1 342 HIS 342 396 396 HIS HIS A . n A 1 343 GLU 343 397 397 GLU GLU A . n A 1 344 ILE 344 398 398 ILE ILE A . n A 1 345 VAL 345 399 399 VAL VAL A . n A 1 346 ARG 346 400 400 ARG ARG A . n A 1 347 SER 347 401 401 SER SER A . n A 1 348 PHE 348 402 402 PHE PHE A . n A 1 349 GLY 349 403 403 GLY GLY A . n A 1 350 THR 350 404 404 THR THR A . n A 1 351 LEU 351 405 405 LEU LEU A . n A 1 352 LYS 352 406 406 LYS LYS A . n A 1 353 LYS 353 407 407 LYS LYS A . n A 1 354 GLU 354 408 408 GLU GLU A . n A 1 355 GLY 355 409 409 GLY GLY A . n A 1 356 TRP 356 410 410 TRP TRP A . n A 1 357 ARG 357 411 411 ARG ARG A . n A 1 358 PRO 358 412 412 PRO PRO A . n A 1 359 ARG 359 413 413 ARG ARG A . n A 1 360 ARG 360 414 414 ARG ARG A . n A 1 361 THR 361 415 415 THR THR A . n A 1 362 ILE 362 416 416 ILE ILE A . n A 1 363 LEU 363 417 417 LEU LEU A . n A 1 364 PHE 364 418 418 PHE PHE A . n A 1 365 ALA 365 419 419 ALA ALA A . n A 1 366 SER 366 420 420 SER SER A . n A 1 367 TRP 367 421 421 TRP TRP A . n A 1 368 ASP 368 422 422 ASP ASP A . n A 1 369 ALA 369 423 423 ALA ALA A . n A 1 370 GLU 370 424 424 GLU GLU A . n A 1 371 GLU 371 425 425 GLU GLU A . n A 1 372 PHE 372 426 426 PHE PHE A . n A 1 373 GLY 373 427 427 GLY GLY A . n A 1 374 LEU 374 428 428 LEU LEU A . n A 1 375 LEU 375 429 429 LEU LEU A . n A 1 376 GLY 376 430 430 GLY GLY A . n A 1 377 SER 377 431 431 SER SER A . n A 1 378 THR 378 432 432 THR THR A . n A 1 379 GLU 379 433 433 GLU GLU A . n A 1 380 TRP 380 434 434 TRP TRP A . n A 1 381 ALA 381 435 435 ALA ALA A . n A 1 382 GLU 382 436 436 GLU GLU A . n A 1 383 GLU 383 437 437 GLU GLU A . n A 1 384 ASN 384 438 438 ASN ASN A . n A 1 385 SER 385 439 439 SER SER A . n A 1 386 ARG 386 440 440 ARG ARG A . n A 1 387 LEU 387 441 441 LEU LEU A . n A 1 388 LEU 388 442 442 LEU LEU A . n A 1 389 GLN 389 443 443 GLN GLN A . n A 1 390 GLU 390 444 444 GLU GLU A . n A 1 391 ARG 391 445 445 ARG ARG A . n A 1 392 GLY 392 446 446 GLY GLY A . n A 1 393 VAL 393 447 447 VAL VAL A . n A 1 394 ALA 394 448 448 ALA ALA A . n A 1 395 TYR 395 449 449 TYR TYR A . n A 1 396 ILE 396 450 450 ILE ILE A . n A 1 397 ASN 397 451 451 ASN ASN A . n A 1 398 ALA 398 452 452 ALA ALA A . n A 1 399 ASP 399 453 453 ASP ASP A . n A 1 400 SER 400 454 454 SER SER A . n A 1 401 SER 401 455 455 SER SER A . n A 1 402 ILE 402 456 456 ILE ILE A . n A 1 403 GLU 403 457 457 GLU GLU A . n A 1 404 GLY 404 458 458 GLY GLY A . n A 1 405 ASN 405 459 459 ASN ASN A . n A 1 406 TYR 406 460 460 TYR TYR A . n A 1 407 THR 407 461 461 THR THR A . n A 1 408 LEU 408 462 462 LEU LEU A . n A 1 409 ARG 409 463 463 ARG ARG A . n A 1 410 VAL 410 464 464 VAL VAL A . n A 1 411 ASP 411 465 465 ASP ASP A . n A 1 412 CYS 412 466 466 CYS CYS A . n A 1 413 THR 413 467 467 THR THR A . n A 1 414 PRO 414 468 468 PRO PRO A . n A 1 415 LEU 415 469 469 LEU LEU A . n A 1 416 MET 416 470 470 MET MET A . n A 1 417 TYR 417 471 471 TYR TYR A . n A 1 418 SER 418 472 472 SER SER A . n A 1 419 LEU 419 473 473 LEU LEU A . n A 1 420 VAL 420 474 474 VAL VAL A . n A 1 421 HIS 421 475 475 HIS HIS A . n A 1 422 ASN 422 476 476 ASN ASN A . n A 1 423 LEU 423 477 477 LEU LEU A . n A 1 424 THR 424 478 478 THR THR A . n A 1 425 LYS 425 479 479 LYS LYS A . n A 1 426 GLU 426 480 480 GLU GLU A . n A 1 427 LEU 427 481 481 LEU LEU A . n A 1 428 LYS 428 482 482 LYS LYS A . n A 1 429 SER 429 483 483 SER SER A . n A 1 430 PRO 430 484 484 PRO PRO A . n A 1 431 ASP 431 485 485 ASP ASP A . n A 1 432 GLU 432 486 486 GLU GLU A . n A 1 433 GLY 433 487 487 GLY GLY A . n A 1 434 PHE 434 488 488 PHE PHE A . n A 1 435 GLU 435 489 489 GLU GLU A . n A 1 436 GLY 436 490 490 GLY GLY A . n A 1 437 LYS 437 491 491 LYS LYS A . n A 1 438 SER 438 492 492 SER SER A . n A 1 439 LEU 439 493 493 LEU LEU A . n A 1 440 TYR 440 494 494 TYR TYR A . n A 1 441 GLU 441 495 495 GLU GLU A . n A 1 442 SER 442 496 496 SER SER A . n A 1 443 TRP 443 497 497 TRP TRP A . n A 1 444 THR 444 498 498 THR THR A . n A 1 445 LYS 445 499 499 LYS LYS A . n A 1 446 LYS 446 500 500 LYS LYS A . n A 1 447 SER 447 501 501 SER SER A . n A 1 448 PRO 448 502 502 PRO PRO A . n A 1 449 SER 449 503 503 SER SER A . n A 1 450 PRO 450 504 504 PRO PRO A . n A 1 451 GLU 451 505 505 GLU GLU A . n A 1 452 PHE 452 506 506 PHE PHE A . n A 1 453 SER 453 507 507 SER SER A . n A 1 454 GLY 454 508 508 GLY GLY A . n A 1 455 MET 455 509 509 MET MET A . n A 1 456 PRO 456 510 510 PRO PRO A . n A 1 457 ARG 457 511 511 ARG ARG A . n A 1 458 ILE 458 512 512 ILE ILE A . n A 1 459 SER 459 513 513 SER SER A . n A 1 460 LYS 460 514 514 LYS LYS A . n A 1 461 LEU 461 515 515 LEU LEU A . n A 1 462 GLY 462 516 516 GLY GLY A . n A 1 463 SER 463 517 517 SER SER A . n A 1 464 GLY 464 518 518 GLY GLY A . n A 1 465 ASN 465 519 519 ASN ASN A . n A 1 466 ASP 466 520 520 ASP ASP A . n A 1 467 PHE 467 521 521 PHE PHE A . n A 1 468 GLU 468 522 522 GLU GLU A . n A 1 469 VAL 469 523 523 VAL VAL A . n A 1 470 PHE 470 524 524 PHE PHE A . n A 1 471 PHE 471 525 525 PHE PHE A . n A 1 472 GLN 472 526 526 GLN GLN A . n A 1 473 ARG 473 527 527 ARG ARG A . n A 1 474 LEU 474 528 528 LEU LEU A . n A 1 475 GLY 475 529 529 GLY GLY A . n A 1 476 ILE 476 530 530 ILE ILE A . n A 1 477 ALA 477 531 531 ALA ALA A . n A 1 478 SER 478 532 532 SER SER A . n A 1 479 GLY 479 533 533 GLY GLY A . n A 1 480 ARG 480 534 534 ARG ARG A . n A 1 481 ALA 481 535 535 ALA ALA A . n A 1 482 ARG 482 536 536 ARG ARG A . n A 1 483 TYR 483 537 537 TYR TYR A . n A 1 484 THR 484 538 538 THR THR A . n A 1 485 LYS 485 539 539 LYS LYS A . n A 1 486 ASN 486 540 540 ASN ASN A . n A 1 487 TRP 487 541 541 TRP TRP A . n A 1 488 GLU 488 542 542 GLU GLU A . n A 1 489 THR 489 543 543 THR THR A . n A 1 490 ASN 490 544 ? ? ? A . n A 1 491 LYS 491 545 ? ? ? A . n A 1 492 PHE 492 546 ? ? ? A . n A 1 493 SER 493 547 ? ? ? A . n A 1 494 GLY 494 548 548 GLY GLY A . n A 1 495 TYR 495 549 549 TYR TYR A . n A 1 496 PRO 496 550 550 PRO PRO A . n A 1 497 LEU 497 551 551 LEU LEU A . n A 1 498 TYR 498 552 552 TYR TYR A . n A 1 499 HIS 499 553 553 HIS HIS A . n A 1 500 SER 500 554 554 SER SER A . n A 1 501 VAL 501 555 555 VAL VAL A . n A 1 502 TYR 502 556 556 TYR TYR A . n A 1 503 GLU 503 557 557 GLU GLU A . n A 1 504 THR 504 558 558 THR THR A . n A 1 505 TYR 505 559 559 TYR TYR A . n A 1 506 GLU 506 560 560 GLU GLU A . n A 1 507 LEU 507 561 561 LEU LEU A . n A 1 508 VAL 508 562 562 VAL VAL A . n A 1 509 GLU 509 563 563 GLU GLU A . n A 1 510 LYS 510 564 564 LYS LYS A . n A 1 511 PHE 511 565 565 PHE PHE A . n A 1 512 TYR 512 566 566 TYR TYR A . n A 1 513 ASP 513 567 567 ASP ASP A . n A 1 514 PRO 514 568 568 PRO PRO A . n A 1 515 MET 515 569 569 MET MET A . n A 1 516 PHE 516 570 570 PHE PHE A . n A 1 517 LYS 517 571 571 LYS LYS A . n A 1 518 TYR 518 572 572 TYR TYR A . n A 1 519 HIS 519 573 573 HIS HIS A . n A 1 520 LEU 520 574 574 LEU LEU A . n A 1 521 THR 521 575 575 THR THR A . n A 1 522 VAL 522 576 576 VAL VAL A . n A 1 523 ALA 523 577 577 ALA ALA A . n A 1 524 GLN 524 578 578 GLN GLN A . n A 1 525 VAL 525 579 579 VAL VAL A . n A 1 526 ARG 526 580 580 ARG ARG A . n A 1 527 GLY 527 581 581 GLY GLY A . n A 1 528 GLY 528 582 582 GLY GLY A . n A 1 529 MET 529 583 583 MET MET A . n A 1 530 VAL 530 584 584 VAL VAL A . n A 1 531 PHE 531 585 585 PHE PHE A . n A 1 532 GLU 532 586 586 GLU GLU A . n A 1 533 LEU 533 587 587 LEU LEU A . n A 1 534 ALA 534 588 588 ALA ALA A . n A 1 535 ASN 535 589 589 ASN ASN A . n A 1 536 SER 536 590 590 SER SER A . n A 1 537 ILE 537 591 591 ILE ILE A . n A 1 538 VAL 538 592 592 VAL VAL A . n A 1 539 LEU 539 593 593 LEU LEU A . n A 1 540 PRO 540 594 594 PRO PRO A . n A 1 541 PHE 541 595 595 PHE PHE A . n A 1 542 ASP 542 596 596 ASP ASP A . n A 1 543 CYS 543 597 597 CYS CYS A . n A 1 544 ARG 544 598 598 ARG ARG A . n A 1 545 ASP 545 599 599 ASP ASP A . n A 1 546 TYR 546 600 600 TYR TYR A . n A 1 547 ALA 547 601 601 ALA ALA A . n A 1 548 VAL 548 602 602 VAL VAL A . n A 1 549 VAL 549 603 603 VAL VAL A . n A 1 550 LEU 550 604 604 LEU LEU A . n A 1 551 ARG 551 605 605 ARG ARG A . n A 1 552 LYS 552 606 606 LYS LYS A . n A 1 553 TYR 553 607 607 TYR TYR A . n A 1 554 ALA 554 608 608 ALA ALA A . n A 1 555 ASP 555 609 609 ASP ASP A . n A 1 556 LYS 556 610 610 LYS LYS A . n A 1 557 ILE 557 611 611 ILE ILE A . n A 1 558 TYR 558 612 612 TYR TYR A . n A 1 559 SER 559 613 613 SER SER A . n A 1 560 ILE 560 614 614 ILE ILE A . n A 1 561 SER 561 615 615 SER SER A . n A 1 562 MET 562 616 616 MET MET A . n A 1 563 LYS 563 617 617 LYS LYS A . n A 1 564 HIS 564 618 618 HIS HIS A . n A 1 565 PRO 565 619 619 PRO PRO A . n A 1 566 GLN 566 620 620 GLN GLN A . n A 1 567 GLU 567 621 621 GLU GLU A . n A 1 568 MET 568 622 622 MET MET A . n A 1 569 LYS 569 623 623 LYS LYS A . n A 1 570 THR 570 624 624 THR THR A . n A 1 571 TYR 571 625 625 TYR TYR A . n A 1 572 SER 572 626 626 SER SER A . n A 1 573 VAL 573 627 627 VAL VAL A . n A 1 574 SER 574 628 628 SER SER A . n A 1 575 PHE 575 629 629 PHE PHE A . n A 1 576 ASP 576 630 630 ASP ASP A . n A 1 577 SER 577 631 631 SER SER A . n A 1 578 LEU 578 632 632 LEU LEU A . n A 1 579 PHE 579 633 633 PHE PHE A . n A 1 580 SER 580 634 634 SER SER A . n A 1 581 ALA 581 635 635 ALA ALA A . n A 1 582 VAL 582 636 636 VAL VAL A . n A 1 583 LYS 583 637 637 LYS LYS A . n A 1 584 ASN 584 638 638 ASN ASN A . n A 1 585 PHE 585 639 639 PHE PHE A . n A 1 586 THR 586 640 640 THR THR A . n A 1 587 GLU 587 641 641 GLU GLU A . n A 1 588 ILE 588 642 642 ILE ILE A . n A 1 589 ALA 589 643 643 ALA ALA A . n A 1 590 SER 590 644 644 SER SER A . n A 1 591 LYS 591 645 645 LYS LYS A . n A 1 592 PHE 592 646 646 PHE PHE A . n A 1 593 SER 593 647 647 SER SER A . n A 1 594 GLU 594 648 648 GLU GLU A . n A 1 595 ARG 595 649 649 ARG ARG A . n A 1 596 LEU 596 650 650 LEU LEU A . n A 1 597 GLN 597 651 651 GLN GLN A . n A 1 598 ASP 598 652 652 ASP ASP A . n A 1 599 PHE 599 653 653 PHE PHE A . n A 1 600 ASP 600 654 ? ? ? A . n A 1 601 LYS 601 655 ? ? ? A . n A 1 602 SER 602 656 656 SER SER A . n A 1 603 ASN 603 657 657 ASN ASN A . n A 1 604 PRO 604 658 658 PRO PRO A . n A 1 605 ILE 605 659 659 ILE ILE A . n A 1 606 VAL 606 660 660 VAL VAL A . n A 1 607 LEU 607 661 661 LEU LEU A . n A 1 608 ARG 608 662 662 ARG ARG A . n A 1 609 MET 609 663 663 MET MET A . n A 1 610 MET 610 664 664 MET MET A . n A 1 611 ASN 611 665 665 ASN ASN A . n A 1 612 ASP 612 666 666 ASP ASP A . n A 1 613 GLN 613 667 667 GLN GLN A . n A 1 614 LEU 614 668 668 LEU LEU A . n A 1 615 MET 615 669 669 MET MET A . n A 1 616 PHE 616 670 670 PHE PHE A . n A 1 617 LEU 617 671 671 LEU LEU A . n A 1 618 GLU 618 672 672 GLU GLU A . n A 1 619 ARG 619 673 673 ARG ARG A . n A 1 620 ALA 620 674 674 ALA ALA A . n A 1 621 PHE 621 675 675 PHE PHE A . n A 1 622 ILE 622 676 676 ILE ILE A . n A 1 623 ASP 623 677 677 ASP ASP A . n A 1 624 PRO 624 678 678 PRO PRO A . n A 1 625 LEU 625 679 679 LEU LEU A . n A 1 626 GLY 626 680 680 GLY GLY A . n A 1 627 LEU 627 681 681 LEU LEU A . n A 1 628 PRO 628 682 682 PRO PRO A . n A 1 629 ASP 629 683 683 ASP ASP A . n A 1 630 ARG 630 684 684 ARG ARG A . n A 1 631 PRO 631 685 685 PRO PRO A . n A 1 632 PHE 632 686 686 PHE PHE A . n A 1 633 TYR 633 687 687 TYR TYR A . n A 1 634 ARG 634 688 688 ARG ARG A . n A 1 635 HIS 635 689 689 HIS HIS A . n A 1 636 VAL 636 690 690 VAL VAL A . n A 1 637 ILE 637 691 691 ILE ILE A . n A 1 638 TYR 638 692 692 TYR TYR A . n A 1 639 ALA 639 693 693 ALA ALA A . n A 1 640 PRO 640 694 694 PRO PRO A . n A 1 641 SER 641 695 695 SER SER A . n A 1 642 SER 642 696 696 SER SER A . n A 1 643 HIS 643 697 697 HIS HIS A . n A 1 644 ASN 644 698 698 ASN ASN A . n A 1 645 LYS 645 699 ? ? ? A . n A 1 646 TYR 646 700 ? ? ? A . n A 1 647 ALA 647 701 ? ? ? A . n A 1 648 GLY 648 702 ? ? ? A . n A 1 649 GLU 649 703 703 GLU GLU A . n A 1 650 SER 650 704 704 SER SER A . n A 1 651 PHE 651 705 705 PHE PHE A . n A 1 652 PRO 652 706 706 PRO PRO A . n A 1 653 GLY 653 707 707 GLY GLY A . n A 1 654 ILE 654 708 708 ILE ILE A . n A 1 655 TYR 655 709 709 TYR TYR A . n A 1 656 ASP 656 710 710 ASP ASP A . n A 1 657 ALA 657 711 711 ALA ALA A . n A 1 658 LEU 658 712 712 LEU LEU A . n A 1 659 PHE 659 713 713 PHE PHE A . n A 1 660 ASP 660 714 714 ASP ASP A . n A 1 661 ILE 661 715 715 ILE ILE A . n A 1 662 GLU 662 716 716 GLU GLU A . n A 1 663 SER 663 717 717 SER SER A . n A 1 664 LYS 664 718 718 LYS LYS A . n A 1 665 VAL 665 719 719 VAL VAL A . n A 1 666 ASP 666 720 720 ASP ASP A . n A 1 667 PRO 667 721 721 PRO PRO A . n A 1 668 SER 668 722 722 SER SER A . n A 1 669 LYS 669 723 723 LYS LYS A . n A 1 670 ALA 670 724 724 ALA ALA A . n A 1 671 TRP 671 725 725 TRP TRP A . n A 1 672 GLY 672 726 726 GLY GLY A . n A 1 673 GLU 673 727 727 GLU GLU A . n A 1 674 VAL 674 728 728 VAL VAL A . n A 1 675 LYS 675 729 729 LYS LYS A . n A 1 676 ARG 676 730 730 ARG ARG A . n A 1 677 GLN 677 731 731 GLN GLN A . n A 1 678 ILE 678 732 732 ILE ILE A . n A 1 679 TYR 679 733 733 TYR TYR A . n A 1 680 VAL 680 734 734 VAL VAL A . n A 1 681 ALA 681 735 735 ALA ALA A . n A 1 682 ALA 682 736 736 ALA ALA A . n A 1 683 PHE 683 737 737 PHE PHE A . n A 1 684 THR 684 738 738 THR THR A . n A 1 685 VAL 685 739 739 VAL VAL A . n A 1 686 GLN 686 740 740 GLN GLN A . n A 1 687 ALA 687 741 741 ALA ALA A . n A 1 688 ALA 688 742 742 ALA ALA A . n A 1 689 ALA 689 743 743 ALA ALA A . n A 1 690 GLU 690 744 744 GLU GLU A . n A 1 691 THR 691 745 745 THR THR A . n A 1 692 LEU 692 746 746 LEU LEU A . n A 1 693 SER 693 747 747 SER SER A . n A 1 694 GLU 694 748 748 GLU GLU A . n A 1 695 VAL 695 749 749 VAL VAL A . n A 1 696 ALA 696 750 750 ALA ALA A . n # 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 1751 ZN ZN A . C 2 ZN 1 802 1752 ZN ZN A . D 3 CA 1 803 1753 CA CA A . E 4 CL 1 804 1754 CL CL A . F 5 NAG 1 805 1755 NAG NAG A . G 5 NAG 2 806 1756 NAG NAG A . H 5 NAG 1 807 1757 NAG NAG A . I 5 NAG 1 808 1758 NAG NAG A . J 5 NAG 2 809 1767 NAG NAG A . K 5 NAG 1 810 1760 NAG NAG A . L 5 NAG 1 811 1761 NAG NAG A . M 5 NAG 2 812 1762 NAG NAG A . N 5 NAG 1 813 1763 NAG NAG A . O 5 NAG 2 814 1764 NAG NAG A . P 6 BMA 3 815 1765 BMA BMA A . Q 7 MAN 4 816 1766 MAN MAN A . R 8 5PU 1 817 1 5PU DRG A . S 9 ACT 1 818 1 ACT ACT A . T 10 HOH 1 901 2221 HOH HOH A . T 10 HOH 2 902 2088 HOH HOH A . T 10 HOH 3 903 2136 HOH HOH A . T 10 HOH 4 904 2444 HOH HOH A . T 10 HOH 5 905 2225 HOH HOH A . T 10 HOH 6 906 2454 HOH HOH A . T 10 HOH 7 907 2459 HOH HOH A . T 10 HOH 8 908 2202 HOH HOH A . T 10 HOH 9 909 2114 HOH HOH A . T 10 HOH 10 910 2466 HOH HOH A . T 10 HOH 11 911 2420 HOH HOH A . T 10 HOH 12 912 2162 HOH HOH A . T 10 HOH 13 913 2134 HOH HOH A . T 10 HOH 14 914 2442 HOH HOH A . T 10 HOH 15 915 2446 HOH HOH A . T 10 HOH 16 916 2139 HOH HOH A . T 10 HOH 17 917 2038 HOH HOH A . T 10 HOH 18 918 2455 HOH HOH A . T 10 HOH 19 919 2332 HOH HOH A . T 10 HOH 20 920 2416 HOH HOH A . T 10 HOH 21 921 2157 HOH HOH A . T 10 HOH 22 922 2154 HOH HOH A . T 10 HOH 23 923 2254 HOH HOH A . T 10 HOH 24 924 2422 HOH HOH A . T 10 HOH 25 925 2383 HOH HOH A . T 10 HOH 26 926 2173 HOH HOH A . T 10 HOH 27 927 2336 HOH HOH A . T 10 HOH 28 928 2280 HOH HOH A . T 10 HOH 29 929 2274 HOH HOH A . T 10 HOH 30 930 2238 HOH HOH A . T 10 HOH 31 931 2095 HOH HOH A . T 10 HOH 32 932 2213 HOH HOH A . T 10 HOH 33 933 2362 HOH HOH A . T 10 HOH 34 934 2343 HOH HOH A . T 10 HOH 35 935 2100 HOH HOH A . T 10 HOH 36 936 2024 HOH HOH A . T 10 HOH 37 937 2387 HOH HOH A . T 10 HOH 38 938 2048 HOH HOH A . T 10 HOH 39 939 2192 HOH HOH A . T 10 HOH 40 940 2111 HOH HOH A . T 10 HOH 41 941 2324 HOH HOH A . T 10 HOH 42 942 2235 HOH HOH A . T 10 HOH 43 943 2102 HOH HOH A . T 10 HOH 44 944 2179 HOH HOH A . T 10 HOH 45 945 2303 HOH HOH A . T 10 HOH 46 946 2311 HOH HOH A . T 10 HOH 47 947 2125 HOH HOH A . T 10 HOH 48 948 2286 HOH HOH A . T 10 HOH 49 949 2096 HOH HOH A . T 10 HOH 50 950 2187 HOH HOH A . T 10 HOH 51 951 2265 HOH HOH A . T 10 HOH 52 952 2429 HOH HOH A . T 10 HOH 53 953 2147 HOH HOH A . T 10 HOH 54 954 2043 HOH HOH A . T 10 HOH 55 955 2169 HOH HOH A . T 10 HOH 56 956 2227 HOH HOH A . T 10 HOH 57 957 2355 HOH HOH A . T 10 HOH 58 958 2218 HOH HOH A . T 10 HOH 59 959 2160 HOH HOH A . T 10 HOH 60 960 2176 HOH HOH A . T 10 HOH 61 961 2392 HOH HOH A . T 10 HOH 62 962 2276 HOH HOH A . T 10 HOH 63 963 2316 HOH HOH A . T 10 HOH 64 964 2044 HOH HOH A . T 10 HOH 65 965 2035 HOH HOH A . T 10 HOH 66 966 2122 HOH HOH A . T 10 HOH 67 967 2062 HOH HOH A . T 10 HOH 68 968 2067 HOH HOH A . T 10 HOH 69 969 2240 HOH HOH A . T 10 HOH 70 970 2060 HOH HOH A . T 10 HOH 71 971 2082 HOH HOH A . T 10 HOH 72 972 2191 HOH HOH A . T 10 HOH 73 973 2233 HOH HOH A . T 10 HOH 74 974 2145 HOH HOH A . T 10 HOH 75 975 2197 HOH HOH A . T 10 HOH 76 976 2350 HOH HOH A . T 10 HOH 77 977 2013 HOH HOH A . T 10 HOH 78 978 2374 HOH HOH A . T 10 HOH 79 979 2069 HOH HOH A . T 10 HOH 80 980 2206 HOH HOH A . T 10 HOH 81 981 2011 HOH HOH A . T 10 HOH 82 982 2467 HOH HOH A . T 10 HOH 83 983 2041 HOH HOH A . T 10 HOH 84 984 2277 HOH HOH A . T 10 HOH 85 985 2432 HOH HOH A . T 10 HOH 86 986 2391 HOH HOH A . T 10 HOH 87 987 2050 HOH HOH A . T 10 HOH 88 988 2282 HOH HOH A . T 10 HOH 89 989 2438 HOH HOH A . T 10 HOH 90 990 2365 HOH HOH A . T 10 HOH 91 991 2408 HOH HOH A . T 10 HOH 92 992 2010 HOH HOH A . T 10 HOH 93 993 2247 HOH HOH A . T 10 HOH 94 994 2021 HOH HOH A . T 10 HOH 95 995 2167 HOH HOH A . T 10 HOH 96 996 2001 HOH HOH A . T 10 HOH 97 997 2196 HOH HOH A . T 10 HOH 98 998 2064 HOH HOH A . T 10 HOH 99 999 2005 HOH HOH A . T 10 HOH 100 1000 2106 HOH HOH A . T 10 HOH 101 1001 2250 HOH HOH A . T 10 HOH 102 1002 2097 HOH HOH A . T 10 HOH 103 1003 2260 HOH HOH A . T 10 HOH 104 1004 2237 HOH HOH A . T 10 HOH 105 1005 2295 HOH HOH A . T 10 HOH 106 1006 2036 HOH HOH A . T 10 HOH 107 1007 2302 HOH HOH A . T 10 HOH 108 1008 2121 HOH HOH A . T 10 HOH 109 1009 2268 HOH HOH A . T 10 HOH 110 1010 2015 HOH HOH A . T 10 HOH 111 1011 2382 HOH HOH A . T 10 HOH 112 1012 2229 HOH HOH A . T 10 HOH 113 1013 2104 HOH HOH A . T 10 HOH 114 1014 2300 HOH HOH A . T 10 HOH 115 1015 2270 HOH HOH A . T 10 HOH 116 1016 2226 HOH HOH A . T 10 HOH 117 1017 2039 HOH HOH A . T 10 HOH 118 1018 2258 HOH HOH A . T 10 HOH 119 1019 2411 HOH HOH A . T 10 HOH 120 1020 2325 HOH HOH A . T 10 HOH 121 1021 2208 HOH HOH A . T 10 HOH 122 1022 2152 HOH HOH A . T 10 HOH 123 1023 2457 HOH HOH A . T 10 HOH 124 1024 2272 HOH HOH A . T 10 HOH 125 1025 2314 HOH HOH A . T 10 HOH 126 1026 2437 HOH HOH A . T 10 HOH 127 1027 2248 HOH HOH A . T 10 HOH 128 1028 2042 HOH HOH A . T 10 HOH 129 1029 2168 HOH HOH A . T 10 HOH 130 1030 2259 HOH HOH A . T 10 HOH 131 1031 2331 HOH HOH A . T 10 HOH 132 1032 2251 HOH HOH A . T 10 HOH 133 1033 2098 HOH HOH A . T 10 HOH 134 1034 2348 HOH HOH A . T 10 HOH 135 1035 2019 HOH HOH A . T 10 HOH 136 1036 2326 HOH HOH A . T 10 HOH 137 1037 2305 HOH HOH A . T 10 HOH 138 1038 2386 HOH HOH A . T 10 HOH 139 1039 2255 HOH HOH A . T 10 HOH 140 1040 2004 HOH HOH A . T 10 HOH 141 1041 2059 HOH HOH A . T 10 HOH 142 1042 2356 HOH HOH A . T 10 HOH 143 1043 2083 HOH HOH A . T 10 HOH 144 1044 2319 HOH HOH A . T 10 HOH 145 1045 2321 HOH HOH A . T 10 HOH 146 1046 2178 HOH HOH A . T 10 HOH 147 1047 2137 HOH HOH A . T 10 HOH 148 1048 2385 HOH HOH A . T 10 HOH 149 1049 2057 HOH HOH A . T 10 HOH 150 1050 2375 HOH HOH A . T 10 HOH 151 1051 2142 HOH HOH A . T 10 HOH 152 1052 2298 HOH HOH A . T 10 HOH 153 1053 2146 HOH HOH A . T 10 HOH 154 1054 2323 HOH HOH A . T 10 HOH 155 1055 2228 HOH HOH A . T 10 HOH 156 1056 2409 HOH HOH A . T 10 HOH 157 1057 2275 HOH HOH A . T 10 HOH 158 1058 2016 HOH HOH A . T 10 HOH 159 1059 2076 HOH HOH A . T 10 HOH 160 1060 2020 HOH HOH A . T 10 HOH 161 1061 2119 HOH HOH A . T 10 HOH 162 1062 2404 HOH HOH A . T 10 HOH 163 1063 2091 HOH HOH A . T 10 HOH 164 1064 2381 HOH HOH A . T 10 HOH 165 1065 2110 HOH HOH A . T 10 HOH 166 1066 2413 HOH HOH A . T 10 HOH 167 1067 2368 HOH HOH A . T 10 HOH 168 1068 2405 HOH HOH A . T 10 HOH 169 1069 2211 HOH HOH A . T 10 HOH 170 1070 2174 HOH HOH A . T 10 HOH 171 1071 2161 HOH HOH A . T 10 HOH 172 1072 2364 HOH HOH A . T 10 HOH 173 1073 2433 HOH HOH A . T 10 HOH 174 1074 2047 HOH HOH A . T 10 HOH 175 1075 2078 HOH HOH A . T 10 HOH 176 1076 2430 HOH HOH A . T 10 HOH 177 1077 2034 HOH HOH A . T 10 HOH 178 1078 2231 HOH HOH A . T 10 HOH 179 1079 2207 HOH HOH A . T 10 HOH 180 1080 2183 HOH HOH A . T 10 HOH 181 1081 2129 HOH HOH A . T 10 HOH 182 1082 2027 HOH HOH A . T 10 HOH 183 1083 2389 HOH HOH A . T 10 HOH 184 1084 2401 HOH HOH A . T 10 HOH 185 1085 2148 HOH HOH A . T 10 HOH 186 1086 2151 HOH HOH A . T 10 HOH 187 1087 2418 HOH HOH A . T 10 HOH 188 1088 2214 HOH HOH A . T 10 HOH 189 1089 2025 HOH HOH A . T 10 HOH 190 1090 2452 HOH HOH A . T 10 HOH 191 1091 2291 HOH HOH A . T 10 HOH 192 1092 2369 HOH HOH A . T 10 HOH 193 1093 2340 HOH HOH A . T 10 HOH 194 1094 2287 HOH HOH A . T 10 HOH 195 1095 2440 HOH HOH A . T 10 HOH 196 1096 2367 HOH HOH A . T 10 HOH 197 1097 2328 HOH HOH A . T 10 HOH 198 1098 2184 HOH HOH A . T 10 HOH 199 1099 2329 HOH HOH A . T 10 HOH 200 1100 2080 HOH HOH A . T 10 HOH 201 1101 2354 HOH HOH A . T 10 HOH 202 1102 2155 HOH HOH A . T 10 HOH 203 1103 2407 HOH HOH A . T 10 HOH 204 1104 2359 HOH HOH A . T 10 HOH 205 1105 2232 HOH HOH A . T 10 HOH 206 1106 2077 HOH HOH A . T 10 HOH 207 1107 2352 HOH HOH A . T 10 HOH 208 1108 2105 HOH HOH A . T 10 HOH 209 1109 2445 HOH HOH A . T 10 HOH 210 1110 2415 HOH HOH A . T 10 HOH 211 1111 2441 HOH HOH A . T 10 HOH 212 1112 2322 HOH HOH A . T 10 HOH 213 1113 2220 HOH HOH A . T 10 HOH 214 1114 2156 HOH HOH A . T 10 HOH 215 1115 2087 HOH HOH A . T 10 HOH 216 1116 2402 HOH HOH A . T 10 HOH 217 1117 2271 HOH HOH A . T 10 HOH 218 1118 2166 HOH HOH A . T 10 HOH 219 1119 2199 HOH HOH A . T 10 HOH 220 1120 2063 HOH HOH A . T 10 HOH 221 1121 2219 HOH HOH A . T 10 HOH 222 1122 2315 HOH HOH A . T 10 HOH 223 1123 2236 HOH HOH A . T 10 HOH 224 1124 2399 HOH HOH A . T 10 HOH 225 1125 2412 HOH HOH A . T 10 HOH 226 1126 2449 HOH HOH A . T 10 HOH 227 1127 2462 HOH HOH A . T 10 HOH 228 1128 2234 HOH HOH A . T 10 HOH 229 1129 2464 HOH HOH A . T 10 HOH 230 1130 2281 HOH HOH A . T 10 HOH 231 1131 2133 HOH HOH A . T 10 HOH 232 1132 2278 HOH HOH A . T 10 HOH 233 1133 2257 HOH HOH A . T 10 HOH 234 1134 2118 HOH HOH A . T 10 HOH 235 1135 2079 HOH HOH A . T 10 HOH 236 1136 2380 HOH HOH A . T 10 HOH 237 1137 2456 HOH HOH A . T 10 HOH 238 1138 2052 HOH HOH A . T 10 HOH 239 1139 2243 HOH HOH A . T 10 HOH 240 1140 2245 HOH HOH A . T 10 HOH 241 1141 2081 HOH HOH A . T 10 HOH 242 1142 2338 HOH HOH A . T 10 HOH 243 1143 2428 HOH HOH A . T 10 HOH 244 1144 2443 HOH HOH A . T 10 HOH 245 1145 2072 HOH HOH A . T 10 HOH 246 1146 2266 HOH HOH A . T 10 HOH 247 1147 2398 HOH HOH A . T 10 HOH 248 1148 2400 HOH HOH A . T 10 HOH 249 1149 2312 HOH HOH A . T 10 HOH 250 1150 2423 HOH HOH A . T 10 HOH 251 1151 2143 HOH HOH A . T 10 HOH 252 1152 2431 HOH HOH A . T 10 HOH 253 1153 2186 HOH HOH A . T 10 HOH 254 1154 2421 HOH HOH A . T 10 HOH 255 1155 2330 HOH HOH A . T 10 HOH 256 1156 2241 HOH HOH A . T 10 HOH 257 1157 2023 HOH HOH A . T 10 HOH 258 1158 2406 HOH HOH A . T 10 HOH 259 1159 2434 HOH HOH A . T 10 HOH 260 1160 2185 HOH HOH A . T 10 HOH 261 1161 2217 HOH HOH A . T 10 HOH 262 1162 2396 HOH HOH A . T 10 HOH 263 1163 2357 HOH HOH A . T 10 HOH 264 1164 2200 HOH HOH A . T 10 HOH 265 1165 2273 HOH HOH A . T 10 HOH 266 1166 2230 HOH HOH A . T 10 HOH 267 1167 2018 HOH HOH A . T 10 HOH 268 1168 2335 HOH HOH A . T 10 HOH 269 1169 2008 HOH HOH A . T 10 HOH 270 1170 2360 HOH HOH A . T 10 HOH 271 1171 2045 HOH HOH A . T 10 HOH 272 1172 2198 HOH HOH A . T 10 HOH 273 1173 2127 HOH HOH A . T 10 HOH 274 1174 2017 HOH HOH A . T 10 HOH 275 1175 2361 HOH HOH A . T 10 HOH 276 1176 2425 HOH HOH A . T 10 HOH 277 1177 2379 HOH HOH A . T 10 HOH 278 1178 2065 HOH HOH A . T 10 HOH 279 1179 2267 HOH HOH A . T 10 HOH 280 1180 2188 HOH HOH A . T 10 HOH 281 1181 2371 HOH HOH A . T 10 HOH 282 1182 2388 HOH HOH A . T 10 HOH 283 1183 2193 HOH HOH A . T 10 HOH 284 1184 2378 HOH HOH A . T 10 HOH 285 1185 2304 HOH HOH A . T 10 HOH 286 1186 2150 HOH HOH A . T 10 HOH 287 1187 2341 HOH HOH A . T 10 HOH 288 1188 2172 HOH HOH A . T 10 HOH 289 1189 2242 HOH HOH A . T 10 HOH 290 1190 2031 HOH HOH A . T 10 HOH 291 1191 2084 HOH HOH A . T 10 HOH 292 1192 2333 HOH HOH A . T 10 HOH 293 1193 2337 HOH HOH A . T 10 HOH 294 1194 2296 HOH HOH A . T 10 HOH 295 1195 2175 HOH HOH A . T 10 HOH 296 1196 2108 HOH HOH A . T 10 HOH 297 1197 2263 HOH HOH A . T 10 HOH 298 1198 2351 HOH HOH A . T 10 HOH 299 1199 2334 HOH HOH A . T 10 HOH 300 1200 2037 HOH HOH A . T 10 HOH 301 1201 2318 HOH HOH A . T 10 HOH 302 1202 2285 HOH HOH A . T 10 HOH 303 1203 2358 HOH HOH A . T 10 HOH 304 1204 2046 HOH HOH A . T 10 HOH 305 1205 2288 HOH HOH A . T 10 HOH 306 1206 2394 HOH HOH A . T 10 HOH 307 1207 2007 HOH HOH A . T 10 HOH 308 1208 2203 HOH HOH A . T 10 HOH 309 1209 2195 HOH HOH A . T 10 HOH 310 1210 2426 HOH HOH A . T 10 HOH 311 1211 2239 HOH HOH A . T 10 HOH 312 1212 2180 HOH HOH A . T 10 HOH 313 1213 2165 HOH HOH A . T 10 HOH 314 1214 2342 HOH HOH A . T 10 HOH 315 1215 2414 HOH HOH A . T 10 HOH 316 1216 2170 HOH HOH A . T 10 HOH 317 1217 2224 HOH HOH A . T 10 HOH 318 1218 2403 HOH HOH A . T 10 HOH 319 1219 2090 HOH HOH A . T 10 HOH 320 1220 2292 HOH HOH A . T 10 HOH 321 1221 2140 HOH HOH A . T 10 HOH 322 1222 2223 HOH HOH A . T 10 HOH 323 1223 2190 HOH HOH A . T 10 HOH 324 1224 2201 HOH HOH A . T 10 HOH 325 1225 2153 HOH HOH A . T 10 HOH 326 1226 2297 HOH HOH A . T 10 HOH 327 1227 2261 HOH HOH A . T 10 HOH 328 1228 2249 HOH HOH A . T 10 HOH 329 1229 2320 HOH HOH A . T 10 HOH 330 1230 2284 HOH HOH A . T 10 HOH 331 1231 2417 HOH HOH A . T 10 HOH 332 1232 2384 HOH HOH A . T 10 HOH 333 1233 2390 HOH HOH A . T 10 HOH 334 1234 2181 HOH HOH A . T 10 HOH 335 1235 2009 HOH HOH A . T 10 HOH 336 1236 2289 HOH HOH A . T 10 HOH 337 1237 2317 HOH HOH A . T 10 HOH 338 1238 2450 HOH HOH A . T 10 HOH 339 1239 2262 HOH HOH A . T 10 HOH 340 1240 2393 HOH HOH A . T 10 HOH 341 1241 2210 HOH HOH A . T 10 HOH 342 1242 2216 HOH HOH A . T 10 HOH 343 1243 2103 HOH HOH A . T 10 HOH 344 1244 2290 HOH HOH A . T 10 HOH 345 1245 2222 HOH HOH A . T 10 HOH 346 1246 2029 HOH HOH A . T 10 HOH 347 1247 2376 HOH HOH A . T 10 HOH 348 1248 2058 HOH HOH A . T 10 HOH 349 1249 2397 HOH HOH A . T 10 HOH 350 1250 2310 HOH HOH A . T 10 HOH 351 1251 2244 HOH HOH A . T 10 HOH 352 1252 2101 HOH HOH A . T 10 HOH 353 1253 2002 HOH HOH A . T 10 HOH 354 1254 2040 HOH HOH A . T 10 HOH 355 1255 2283 HOH HOH A . T 10 HOH 356 1256 2177 HOH HOH A . T 10 HOH 357 1257 2215 HOH HOH A . T 10 HOH 358 1258 2395 HOH HOH A . T 10 HOH 359 1259 2182 HOH HOH A . T 10 HOH 360 1260 2070 HOH HOH A . T 10 HOH 361 1261 2253 HOH HOH A . T 10 HOH 362 1262 2435 HOH HOH A . T 10 HOH 363 1263 2003 HOH HOH A . T 10 HOH 364 1264 2051 HOH HOH A . T 10 HOH 365 1265 2419 HOH HOH A . T 10 HOH 366 1266 2301 HOH HOH A . T 10 HOH 367 1267 2424 HOH HOH A . T 10 HOH 368 1268 2427 HOH HOH A . T 10 HOH 369 1269 2308 HOH HOH A . T 10 HOH 370 1270 2461 HOH HOH A . T 10 HOH 371 1271 2294 HOH HOH A . T 10 HOH 372 1272 2194 HOH HOH A . T 10 HOH 373 1273 2256 HOH HOH A . T 10 HOH 374 1274 2377 HOH HOH A . T 10 HOH 375 1275 2363 HOH HOH A . T 10 HOH 376 1276 2279 HOH HOH A . T 10 HOH 377 1277 2092 HOH HOH A . T 10 HOH 378 1278 2099 HOH HOH A . T 10 HOH 379 1279 2049 HOH HOH A . T 10 HOH 380 1280 2209 HOH HOH A . T 10 HOH 381 1281 2212 HOH HOH A . T 10 HOH 382 1282 2458 HOH HOH A . T 10 HOH 383 1283 2073 HOH HOH A . T 10 HOH 384 1284 2293 HOH HOH A . T 10 HOH 385 1285 2159 HOH HOH A . T 10 HOH 386 1286 2068 HOH HOH A . T 10 HOH 387 1287 2299 HOH HOH A . T 10 HOH 388 1288 2339 HOH HOH A . T 10 HOH 389 1289 2246 HOH HOH A . T 10 HOH 390 1290 2032 HOH HOH A . T 10 HOH 391 1291 2269 HOH HOH A . T 10 HOH 392 1292 2056 HOH HOH A . T 10 HOH 393 1293 2115 HOH HOH A . T 10 HOH 394 1294 2410 HOH HOH A . T 10 HOH 395 1295 2149 HOH HOH A . T 10 HOH 396 1296 2189 HOH HOH A . T 10 HOH 397 1297 2313 HOH HOH A . T 10 HOH 398 1298 2171 HOH HOH A . T 10 HOH 399 1299 2158 HOH HOH A . T 10 HOH 400 1300 2344 HOH HOH A . T 10 HOH 401 1301 2327 HOH HOH A . T 10 HOH 402 1302 2366 HOH HOH A . T 10 HOH 403 1303 2309 HOH HOH A . T 10 HOH 404 1304 2347 HOH HOH A . T 10 HOH 405 1305 2370 HOH HOH A . T 10 HOH 406 1306 2349 HOH HOH A . T 10 HOH 407 1307 2022 HOH HOH A . T 10 HOH 408 1308 2075 HOH HOH A . T 10 HOH 409 1309 2306 HOH HOH A . T 10 HOH 410 1310 2033 HOH HOH A . T 10 HOH 411 1311 2346 HOH HOH A . T 10 HOH 412 1312 2448 HOH HOH A . T 10 HOH 413 1313 2460 HOH HOH A . T 10 HOH 414 1314 2006 HOH HOH A . T 10 HOH 415 1315 2028 HOH HOH A . T 10 HOH 416 1316 2252 HOH HOH A . T 10 HOH 417 1317 2144 HOH HOH A . T 10 HOH 418 1318 2373 HOH HOH A . T 10 HOH 419 1319 2071 HOH HOH A . T 10 HOH 420 1320 2026 HOH HOH A . T 10 HOH 421 1321 2066 HOH HOH A . T 10 HOH 422 1322 2135 HOH HOH A . T 10 HOH 423 1323 2447 HOH HOH A . T 10 HOH 424 1324 2086 HOH HOH A . T 10 HOH 425 1325 2205 HOH HOH A . T 10 HOH 426 1326 2061 HOH HOH A . T 10 HOH 427 1327 2138 HOH HOH A . T 10 HOH 428 1328 2372 HOH HOH A . T 10 HOH 429 1329 2107 HOH HOH A . T 10 HOH 430 1330 2141 HOH HOH A . T 10 HOH 431 1331 2451 HOH HOH A . T 10 HOH 432 1332 2116 HOH HOH A . T 10 HOH 433 1333 2053 HOH HOH A . T 10 HOH 434 1334 2353 HOH HOH A . T 10 HOH 435 1335 2307 HOH HOH A . T 10 HOH 436 1336 2123 HOH HOH A . T 10 HOH 437 1337 2094 HOH HOH A . T 10 HOH 438 1338 2126 HOH HOH A . T 10 HOH 439 1339 2130 HOH HOH A . T 10 HOH 440 1340 2163 HOH HOH A . T 10 HOH 441 1341 2453 HOH HOH A . T 10 HOH 442 1342 2264 HOH HOH A . T 10 HOH 443 1343 2030 HOH HOH A . T 10 HOH 444 1344 2439 HOH HOH A . T 10 HOH 445 1345 2131 HOH HOH A . T 10 HOH 446 1346 2014 HOH HOH A . T 10 HOH 447 1347 2085 HOH HOH A . T 10 HOH 448 1348 2089 HOH HOH A . T 10 HOH 449 1349 2204 HOH HOH A . T 10 HOH 450 1350 2436 HOH HOH A . T 10 HOH 451 1351 2463 HOH HOH A . T 10 HOH 452 1352 2093 HOH HOH A . T 10 HOH 453 1353 2164 HOH HOH A . T 10 HOH 454 1354 2124 HOH HOH A . T 10 HOH 455 1355 2112 HOH HOH A . T 10 HOH 456 1356 2132 HOH HOH A . T 10 HOH 457 1357 2128 HOH HOH A . T 10 HOH 458 1358 2012 HOH HOH A . T 10 HOH 459 1359 2117 HOH HOH A . T 10 HOH 460 1360 2120 HOH HOH A . T 10 HOH 461 1361 2074 HOH HOH A . T 10 HOH 462 1362 2109 HOH HOH A . T 10 HOH 463 1363 2113 HOH HOH A . T 10 HOH 464 1364 2345 HOH HOH A . T 10 HOH 465 1365 2054 HOH HOH A . T 10 HOH 466 1366 2055 HOH HOH A . # _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)' 12100 ? 1 MORE -62 ? 1 'SSA (A^2)' 50750 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_565 -x,-y+1,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 130.8270000000 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 ? A THR 215 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OG1 ? A THR 215 ? A THR 269 ? 1_555 73.5 ? 2 O ? A THR 215 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A TYR 218 ? A TYR 272 ? 1_555 73.1 ? 3 OG1 ? A THR 215 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? A TYR 218 ? A TYR 272 ? 1_555 92.6 ? 4 O ? A THR 215 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 379 ? A GLU 433 ? 1_555 150.2 ? 5 OG1 ? A THR 215 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 379 ? A GLU 433 ? 1_555 88.3 ? 6 O ? A TYR 218 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE1 ? A GLU 379 ? A GLU 433 ? 1_555 84.8 ? 7 O ? A THR 215 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 379 ? A GLU 433 ? 1_555 149.5 ? 8 OG1 ? A THR 215 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 379 ? A GLU 433 ? 1_555 96.5 ? 9 O ? A TYR 218 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 379 ? A GLU 433 ? 1_555 137.1 ? 10 OE1 ? A GLU 379 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 379 ? A GLU 433 ? 1_555 53.9 ? 11 O ? A THR 215 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 382 ? A GLU 436 ? 1_555 102.8 ? 12 OG1 ? A THR 215 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 382 ? A GLU 436 ? 1_555 173.2 ? 13 O ? A TYR 218 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 382 ? A GLU 436 ? 1_555 80.8 ? 14 OE1 ? A GLU 379 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 382 ? A GLU 436 ? 1_555 92.7 ? 15 OE2 ? A GLU 379 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 OE2 ? A GLU 382 ? A GLU 436 ? 1_555 89.5 ? 16 O ? A THR 215 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 966 ? 1_555 75.0 ? 17 OG1 ? A THR 215 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 966 ? 1_555 91.3 ? 18 O ? A TYR 218 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 966 ? 1_555 145.1 ? 19 OE1 ? A GLU 379 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 966 ? 1_555 130.0 ? 20 OE2 ? A GLU 379 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 966 ? 1_555 76.5 ? 21 OE2 ? A GLU 382 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 803 ? 1_555 O ? T HOH . ? A HOH 966 ? 1_555 93.2 ? 22 NE2 ? A HIS 323 ? A HIS 377 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD1 ? A ASP 333 ? A ASP 387 ? 1_555 96.6 ? 23 NE2 ? A HIS 323 ? A HIS 377 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD1 ? A ASP 399 ? A ASP 453 ? 1_555 85.8 ? 24 OD1 ? A ASP 333 ? A ASP 387 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD1 ? A ASP 399 ? A ASP 453 ? 1_555 91.3 ? 25 NE2 ? A HIS 323 ? A HIS 377 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP 399 ? A ASP 453 ? 1_555 94.0 ? 26 OD1 ? A ASP 333 ? A ASP 387 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP 399 ? A ASP 453 ? 1_555 144.3 ? 27 OD1 ? A ASP 399 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP 399 ? A ASP 453 ? 1_555 55.5 ? 28 NE2 ? A HIS 323 ? A HIS 377 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OAD ? R 5PU . ? A 5PU 817 ? 1_555 96.3 ? 29 OD1 ? A ASP 333 ? A ASP 387 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OAD ? R 5PU . ? A 5PU 817 ? 1_555 109.6 ? 30 OD1 ? A ASP 399 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OAD ? R 5PU . ? A 5PU 817 ? 1_555 158.4 ? 31 OD2 ? A ASP 399 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 OAD ? R 5PU . ? A 5PU 817 ? 1_555 102.9 ? 32 NE2 ? A HIS 323 ? A HIS 377 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 O ? T HOH . ? A HOH 1126 ? 1_555 176.0 ? 33 OD1 ? A ASP 333 ? A ASP 387 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 O ? T HOH . ? A HOH 1126 ? 1_555 85.2 ? 34 OD1 ? A ASP 399 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 O ? T HOH . ? A HOH 1126 ? 1_555 90.5 ? 35 OD2 ? A ASP 399 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 O ? T HOH . ? A HOH 1126 ? 1_555 82.4 ? 36 OAD ? R 5PU . ? A 5PU 817 ? 1_555 ZN ? C ZN . ? A ZN 802 ? 1_555 O ? T HOH . ? A HOH 1126 ? 1_555 86.4 ? 37 OD2 ? A ASP 333 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE1 ? A GLU 371 ? A GLU 425 ? 1_555 152.7 ? 38 OD2 ? A ASP 333 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE2 ? A GLU 371 ? A GLU 425 ? 1_555 97.3 ? 39 OE1 ? A GLU 371 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OE2 ? A GLU 371 ? A GLU 425 ? 1_555 56.0 ? 40 OD2 ? A ASP 333 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 NE2 ? A HIS 499 ? A HIS 553 ? 1_555 92.7 ? 41 OE1 ? A GLU 371 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 NE2 ? A HIS 499 ? A HIS 553 ? 1_555 87.4 ? 42 OE2 ? A GLU 371 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 NE2 ? A HIS 499 ? A HIS 553 ? 1_555 100.9 ? 43 OD2 ? A ASP 333 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAD ? R 5PU . ? A 5PU 817 ? 1_555 99.8 ? 44 OE1 ? A GLU 371 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAD ? R 5PU . ? A 5PU 817 ? 1_555 86.9 ? 45 OE2 ? A GLU 371 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAD ? R 5PU . ? A 5PU 817 ? 1_555 89.4 ? 46 NE2 ? A HIS 499 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAD ? R 5PU . ? A 5PU 817 ? 1_555 162.7 ? 47 OD2 ? A ASP 333 ? A ASP 387 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAC ? R 5PU . ? A 5PU 817 ? 1_555 102.9 ? 48 OE1 ? A GLU 371 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAC ? R 5PU . ? A 5PU 817 ? 1_555 104.4 ? 49 OE2 ? A GLU 371 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAC ? R 5PU . ? A 5PU 817 ? 1_555 156.1 ? 50 NE2 ? A HIS 499 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAC ? R 5PU . ? A 5PU 817 ? 1_555 90.7 ? 51 OAD ? R 5PU . ? A 5PU 817 ? 1_555 ZN ? B ZN . ? A ZN 801 ? 1_555 OAC ? R 5PU . ? A 5PU 817 ? 1_555 74.9 ? # 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 2016-04-27 2 'Structure model' 1 1 2016-06-08 # _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.id 1 _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 17.5404 _pdbx_refine_tls.origin_y 50.0822 _pdbx_refine_tls.origin_z 45.0093 _pdbx_refine_tls.T[1][1] 0.0430 _pdbx_refine_tls.T[1][1]_esd ? _pdbx_refine_tls.T[1][2] 0.0118 _pdbx_refine_tls.T[1][2]_esd ? _pdbx_refine_tls.T[1][3] 0.0082 _pdbx_refine_tls.T[1][3]_esd ? _pdbx_refine_tls.T[2][2] 0.0623 _pdbx_refine_tls.T[2][2]_esd ? _pdbx_refine_tls.T[2][3] -0.0378 _pdbx_refine_tls.T[2][3]_esd ? _pdbx_refine_tls.T[3][3] 0.0654 _pdbx_refine_tls.T[3][3]_esd ? _pdbx_refine_tls.L[1][1] 0.2546 _pdbx_refine_tls.L[1][1]_esd ? _pdbx_refine_tls.L[1][2] -0.3111 _pdbx_refine_tls.L[1][2]_esd ? _pdbx_refine_tls.L[1][3] 0.0591 _pdbx_refine_tls.L[1][3]_esd ? _pdbx_refine_tls.L[2][2] 0.5553 _pdbx_refine_tls.L[2][2]_esd ? _pdbx_refine_tls.L[2][3] 0.0110 _pdbx_refine_tls.L[2][3]_esd ? _pdbx_refine_tls.L[3][3] 0.0831 _pdbx_refine_tls.L[3][3]_esd ? _pdbx_refine_tls.S[1][1] -0.0377 _pdbx_refine_tls.S[1][1]_esd ? _pdbx_refine_tls.S[1][2] 0.0358 _pdbx_refine_tls.S[1][2]_esd ? _pdbx_refine_tls.S[1][3] 0.0171 _pdbx_refine_tls.S[1][3]_esd ? _pdbx_refine_tls.S[2][1] 0.0360 _pdbx_refine_tls.S[2][1]_esd ? _pdbx_refine_tls.S[2][2] 0.0487 _pdbx_refine_tls.S[2][2]_esd ? _pdbx_refine_tls.S[2][3] -0.1098 _pdbx_refine_tls.S[2][3]_esd ? _pdbx_refine_tls.S[3][1] 0.0142 _pdbx_refine_tls.S[3][1]_esd ? _pdbx_refine_tls.S[3][2] 0.0409 _pdbx_refine_tls.S[3][2]_esd ? _pdbx_refine_tls.S[3][3] -0.0110 _pdbx_refine_tls.S[3][3]_esd ? # _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.beg_auth_asym_id A _pdbx_refine_tls_group.beg_auth_seq_id 55 _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id A _pdbx_refine_tls_group.end_auth_seq_id 750 _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details ? # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.5.0109 1 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? . 2 ? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.15 3 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 4 ? 'data collection' ? ? ? ? ? ? ? ? ? ? ? MxCuBE ? ? ? . 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 CH3 A ACT 818 ? ? O A HOH 1238 ? ? 1.88 2 1 ND2 A ASN 260 ? B O A HOH 902 ? ? 2.03 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 OE1 _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 GLU _pdbx_validate_symm_contact.auth_seq_id_1 276 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 A _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O2 _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 BMA _pdbx_validate_symm_contact.auth_seq_id_2 815 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 2_565 _pdbx_validate_symm_contact.dist 2.19 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CB _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 VAL _pdbx_validate_rmsd_bond.auth_seq_id_1 158 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 CG1 _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 VAL _pdbx_validate_rmsd_bond.auth_seq_id_2 158 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.657 _pdbx_validate_rmsd_bond.bond_target_value 1.524 _pdbx_validate_rmsd_bond.bond_deviation 0.133 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.021 _pdbx_validate_rmsd_bond.linker_flag N # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 NE _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 ARG _pdbx_validate_rmsd_angle.auth_seq_id_1 536 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 A _pdbx_validate_rmsd_angle.auth_atom_id_2 CZ _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 ARG _pdbx_validate_rmsd_angle.auth_seq_id_2 536 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 A _pdbx_validate_rmsd_angle.auth_atom_id_3 NH2 _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 ARG _pdbx_validate_rmsd_angle.auth_seq_id_3 536 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 A _pdbx_validate_rmsd_angle.angle_value 116.97 _pdbx_validate_rmsd_angle.angle_target_value 120.30 _pdbx_validate_rmsd_angle.angle_deviation -3.33 _pdbx_validate_rmsd_angle.angle_standard_deviation 0.50 _pdbx_validate_rmsd_angle.linker_flag N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 153 ? ? -101.32 41.74 2 1 PHE A 164 ? ? 84.12 5.14 3 1 ASN A 178 ? ? 57.35 -126.93 4 1 LYS A 207 ? ? 81.96 -50.74 5 1 VAL A 382 ? ? -134.19 -106.58 6 1 ALA A 452 ? ? -156.51 57.68 7 1 SER A 454 ? ? -32.18 120.82 8 1 SER A 454 ? ? -32.18 120.88 9 1 TRP A 541 ? ? -75.50 29.73 10 1 GLU A 542 ? ? -148.21 48.98 11 1 ASP A 567 ? ? -155.10 64.24 12 1 SER A 704 ? ? -56.25 172.38 # _pdbx_validate_peptide_omega.id 1 _pdbx_validate_peptide_omega.PDB_model_num 1 _pdbx_validate_peptide_omega.auth_comp_id_1 HIS _pdbx_validate_peptide_omega.auth_asym_id_1 A _pdbx_validate_peptide_omega.auth_seq_id_1 697 _pdbx_validate_peptide_omega.PDB_ins_code_1 ? _pdbx_validate_peptide_omega.label_alt_id_1 ? _pdbx_validate_peptide_omega.auth_comp_id_2 ASN _pdbx_validate_peptide_omega.auth_asym_id_2 A _pdbx_validate_peptide_omega.auth_seq_id_2 698 _pdbx_validate_peptide_omega.PDB_ins_code_2 ? _pdbx_validate_peptide_omega.label_alt_id_2 ? _pdbx_validate_peptide_omega.omega 144.08 # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 1365 ? 6.27 . 2 1 O ? A HOH 1366 ? 7.30 . # 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 ASN 132 ? A ASN 78 2 1 Y 1 A GLU 133 ? A GLU 79 3 1 Y 1 A ASP 134 ? A ASP 80 4 1 Y 1 A GLY 135 ? A GLY 81 5 1 Y 1 A ASN 544 ? A ASN 490 6 1 Y 1 A LYS 545 ? A LYS 491 7 1 Y 1 A PHE 546 ? A PHE 492 8 1 Y 1 A SER 547 ? A SER 493 9 1 Y 1 A ASP 654 ? A ASP 600 10 1 Y 1 A LYS 655 ? A LYS 601 11 1 Y 1 A LYS 699 ? A LYS 645 12 1 Y 1 A TYR 700 ? A TYR 646 13 1 Y 1 A ALA 701 ? A ALA 647 14 1 Y 1 A GLY 702 ? A GLY 648 # _pdbx_audit_support.funding_organization 'Helmholtz-Zentrum Berlin and BioStruct-X' _pdbx_audit_support.country Germany _pdbx_audit_support.grant_number N283570 _pdbx_audit_support.ordinal 1 # 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 '4-[(2~{R})-2-carboxy-5-(oxidanylamino)-5-oxidanylidene-pentyl]benzoic acid' 5PU 9 'ACETATE ION' ACT 10 water HOH #