data_2XEG # _entry.id 2XEG # _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 2XEG PDBE EBI-43916 WWPDB D_1290043916 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 2C6G unspecified 'MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II ( GCPII) WITH BOUND GLUTAMATE' PDB 2C6C unspecified ;MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II ( GCPII) IN COMPLEX WITH GPI-18431 (S)-2-( 4-IODOBENZYLPHOSPHONOMETHYL)-PENTANEDIOIC ACID ; PDB 2C6P unspecified 'MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II ( GCPII) IN COMPLEX WITH PHOSPHATE ANION' PDB 1Z8L unspecified 'CRYSTAL STRUCTURE OF PROSTATE-SPECIFIC MEMBRANE ANTIGEN, ATUMOR MARKER AND PEPTIDASE' PDB 2JBJ unspecified 'MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II ( GCPII) IN COMPLEX WITH 2-PMPA' PDB 2JBK unspecified ;MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II ( GCPII) IN COMPLEX WITH QUISQUALIC ACID ( QUISQUALATE, ALPHA-AMINO-3,5-DIOXO-1,2,4 -OXADIAZOLIDINE-2-PROPANOIC ACID) ; PDB 2CIJ unspecified 'MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II ( GCPII) WITH BOUND METHIONINE' PDB 2XEJ unspecified 'HUMAN GLUTAMATE CARBOXYPEPTIDASE II IN COMPLEX WITH ARM-M4, UREA-BASED INHIBITOR' PDB 2XEF unspecified 'HUMAN GLUTAMATE CARBOXYPEPTIDASE II IN COMPLEX WITH ANTIBODY-RECRUITING MOLECULE ARM-P8' PDB 2XEI unspecified 'HUMAN GLUTAMATE CARBOXYPEPTIDASE II IN COMPLEX WITH ANTIBODY-RECRUITING MOLECULE ARM-P2' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2XEG _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2010-05-14 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Zhang, A.X.' 1 'Murelli, R.P.' 2 'Barinka, C.' 3 'Michel, J.' 4 'Cocleaza, A.' 5 'Jorgensen, W.L.' 6 'Lubkowski, J.' 7 'Spiegel, D.A.' 8 # _citation.id primary _citation.title 'A Remote Arene-Binding Site on Prostate Specific Membrane Antigen Revealed by Antibody-Recruiting Small Molecules.' _citation.journal_abbrev J.Am.Chem.Soc. _citation.journal_volume 132 _citation.page_first 12711 _citation.page_last ? _citation.year 2010 _citation.journal_id_ASTM JACSAT _citation.country US _citation.journal_id_ISSN 0002-7863 _citation.journal_id_CSD 0004 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 20726553 _citation.pdbx_database_id_DOI 10.1021/JA104591M # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Zhang, A.X.' 1 primary 'Murelli, R.P.' 2 primary 'Barinka, C.' 3 primary 'Michel, J.' 4 primary 'Cocleaza, A.' 5 primary 'Jorgensen, W.L.' 6 primary 'Lubkowski, J.' 7 primary 'Spiegel, D.A.' 8 # _cell.entry_id 2XEG _cell.length_a 101.707 _cell.length_b 130.039 _cell.length_c 159.026 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 2XEG _symmetry.space_group_name_H-M 'I 2 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 23 # 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' 79874.000 1 3.4.17.21 ? 'ECTODOMAIN, RESIDUES 44-750' ? 2 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 3 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 4 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 11 ? ? ? ? 6 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 7 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 8 non-polymer syn ;N-({(1S)-5-[4-(13-{[2,4-BIS(DIHYDROXYAMINO)PHENYL]AMINO}-2,5,8,11-TETRAOXATRIDEC-1-YL)-1H-1,2,3-TRIAZOL-1-YL]-1-CARBOXYPENTYL}CARBAMOYL)-L-GLUTAMIC ACID ; 746.720 1 ? ? ? ? 9 water nat water 18.015 612 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ;GLUTAMATE CARBOXYPEPTIDASE II, GCPII, MEMBRANE GLUTAMATE CARBOXYPEPTIDASE, N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE I, MGCP, NAALADASE I, PTEROYLPOLY-GAMMA- GLUTAMATE CARBOXYPEPTIDASE, FOLYLPOLY-GAMMA-GLUTAMATE CARBOXYPEPTIDASE, FGCP, FOLATE HYDROLASE 1, PROSTATE- SPECIFIC MEMBRANE ANTIGEN, PSMA, PSM, CELL GROWTH-INHIBITING GENE 27 PROTEIN ; # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;RSKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPN KTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIV IARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRR GIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGT LRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRL LQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDF EVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVQPFDCRDYA VVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGL PDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_seq_one_letter_code_can ;RSKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPN KTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIV IARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRR GIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGT LRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRL LQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDF EVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVQPFDCRDYA VVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGL PDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ARG n 1 2 SER n 1 3 LYS n 1 4 SER n 1 5 SER n 1 6 ASN n 1 7 GLU n 1 8 ALA n 1 9 THR n 1 10 ASN n 1 11 ILE n 1 12 THR n 1 13 PRO n 1 14 LYS n 1 15 HIS n 1 16 ASN n 1 17 MET n 1 18 LYS n 1 19 ALA n 1 20 PHE n 1 21 LEU n 1 22 ASP n 1 23 GLU n 1 24 LEU n 1 25 LYS n 1 26 ALA n 1 27 GLU n 1 28 ASN n 1 29 ILE n 1 30 LYS n 1 31 LYS n 1 32 PHE n 1 33 LEU n 1 34 TYR n 1 35 ASN n 1 36 PHE n 1 37 THR n 1 38 GLN n 1 39 ILE n 1 40 PRO n 1 41 HIS n 1 42 LEU n 1 43 ALA n 1 44 GLY n 1 45 THR n 1 46 GLU n 1 47 GLN n 1 48 ASN n 1 49 PHE n 1 50 GLN n 1 51 LEU n 1 52 ALA n 1 53 LYS n 1 54 GLN n 1 55 ILE n 1 56 GLN n 1 57 SER n 1 58 GLN n 1 59 TRP n 1 60 LYS n 1 61 GLU n 1 62 PHE n 1 63 GLY n 1 64 LEU n 1 65 ASP n 1 66 SER n 1 67 VAL n 1 68 GLU n 1 69 LEU n 1 70 ALA n 1 71 HIS n 1 72 TYR n 1 73 ASP n 1 74 VAL n 1 75 LEU n 1 76 LEU n 1 77 SER n 1 78 TYR n 1 79 PRO n 1 80 ASN n 1 81 LYS n 1 82 THR n 1 83 HIS n 1 84 PRO n 1 85 ASN n 1 86 TYR n 1 87 ILE n 1 88 SER n 1 89 ILE n 1 90 ILE n 1 91 ASN n 1 92 GLU n 1 93 ASP n 1 94 GLY n 1 95 ASN n 1 96 GLU n 1 97 ILE n 1 98 PHE n 1 99 ASN n 1 100 THR n 1 101 SER n 1 102 LEU n 1 103 PHE n 1 104 GLU n 1 105 PRO n 1 106 PRO n 1 107 PRO n 1 108 PRO n 1 109 GLY n 1 110 TYR n 1 111 GLU n 1 112 ASN n 1 113 VAL n 1 114 SER n 1 115 ASP n 1 116 ILE n 1 117 VAL n 1 118 PRO n 1 119 PRO n 1 120 PHE n 1 121 SER n 1 122 ALA n 1 123 PHE n 1 124 SER n 1 125 PRO n 1 126 GLN n 1 127 GLY n 1 128 MET n 1 129 PRO n 1 130 GLU n 1 131 GLY n 1 132 ASP n 1 133 LEU n 1 134 VAL n 1 135 TYR n 1 136 VAL n 1 137 ASN n 1 138 TYR n 1 139 ALA n 1 140 ARG n 1 141 THR n 1 142 GLU n 1 143 ASP n 1 144 PHE n 1 145 PHE n 1 146 LYS n 1 147 LEU n 1 148 GLU n 1 149 ARG n 1 150 ASP n 1 151 MET n 1 152 LYS n 1 153 ILE n 1 154 ASN n 1 155 CYS n 1 156 SER n 1 157 GLY n 1 158 LYS n 1 159 ILE n 1 160 VAL n 1 161 ILE n 1 162 ALA n 1 163 ARG n 1 164 TYR n 1 165 GLY n 1 166 LYS n 1 167 VAL n 1 168 PHE n 1 169 ARG n 1 170 GLY n 1 171 ASN n 1 172 LYS n 1 173 VAL n 1 174 LYS n 1 175 ASN n 1 176 ALA n 1 177 GLN n 1 178 LEU n 1 179 ALA n 1 180 GLY n 1 181 ALA n 1 182 LYS n 1 183 GLY n 1 184 VAL n 1 185 ILE n 1 186 LEU n 1 187 TYR n 1 188 SER n 1 189 ASP n 1 190 PRO n 1 191 ALA n 1 192 ASP n 1 193 TYR n 1 194 PHE n 1 195 ALA n 1 196 PRO n 1 197 GLY n 1 198 VAL n 1 199 LYS n 1 200 SER n 1 201 TYR n 1 202 PRO n 1 203 ASP n 1 204 GLY n 1 205 TRP n 1 206 ASN n 1 207 LEU n 1 208 PRO n 1 209 GLY n 1 210 GLY n 1 211 GLY n 1 212 VAL n 1 213 GLN n 1 214 ARG n 1 215 GLY n 1 216 ASN n 1 217 ILE n 1 218 LEU n 1 219 ASN n 1 220 LEU n 1 221 ASN n 1 222 GLY n 1 223 ALA n 1 224 GLY n 1 225 ASP n 1 226 PRO n 1 227 LEU n 1 228 THR n 1 229 PRO n 1 230 GLY n 1 231 TYR n 1 232 PRO n 1 233 ALA n 1 234 ASN n 1 235 GLU n 1 236 TYR n 1 237 ALA n 1 238 TYR n 1 239 ARG n 1 240 ARG n 1 241 GLY n 1 242 ILE n 1 243 ALA n 1 244 GLU n 1 245 ALA n 1 246 VAL n 1 247 GLY n 1 248 LEU n 1 249 PRO n 1 250 SER n 1 251 ILE n 1 252 PRO n 1 253 VAL n 1 254 HIS n 1 255 PRO n 1 256 ILE n 1 257 GLY n 1 258 TYR n 1 259 TYR n 1 260 ASP n 1 261 ALA n 1 262 GLN n 1 263 LYS n 1 264 LEU n 1 265 LEU n 1 266 GLU n 1 267 LYS n 1 268 MET n 1 269 GLY n 1 270 GLY n 1 271 SER n 1 272 ALA n 1 273 PRO n 1 274 PRO n 1 275 ASP n 1 276 SER n 1 277 SER n 1 278 TRP n 1 279 ARG n 1 280 GLY n 1 281 SER n 1 282 LEU n 1 283 LYS n 1 284 VAL n 1 285 PRO n 1 286 TYR n 1 287 ASN n 1 288 VAL n 1 289 GLY n 1 290 PRO n 1 291 GLY n 1 292 PHE n 1 293 THR n 1 294 GLY n 1 295 ASN n 1 296 PHE n 1 297 SER n 1 298 THR n 1 299 GLN n 1 300 LYS n 1 301 VAL n 1 302 LYS n 1 303 MET n 1 304 HIS n 1 305 ILE n 1 306 HIS n 1 307 SER n 1 308 THR n 1 309 ASN n 1 310 GLU n 1 311 VAL n 1 312 THR n 1 313 ARG n 1 314 ILE n 1 315 TYR n 1 316 ASN n 1 317 VAL n 1 318 ILE n 1 319 GLY n 1 320 THR n 1 321 LEU n 1 322 ARG n 1 323 GLY n 1 324 ALA n 1 325 VAL n 1 326 GLU n 1 327 PRO n 1 328 ASP n 1 329 ARG n 1 330 TYR n 1 331 VAL n 1 332 ILE n 1 333 LEU n 1 334 GLY n 1 335 GLY n 1 336 HIS n 1 337 ARG n 1 338 ASP n 1 339 SER n 1 340 TRP n 1 341 VAL n 1 342 PHE n 1 343 GLY n 1 344 GLY n 1 345 ILE n 1 346 ASP n 1 347 PRO n 1 348 GLN n 1 349 SER n 1 350 GLY n 1 351 ALA n 1 352 ALA n 1 353 VAL n 1 354 VAL n 1 355 HIS n 1 356 GLU n 1 357 ILE n 1 358 VAL n 1 359 ARG n 1 360 SER n 1 361 PHE n 1 362 GLY n 1 363 THR n 1 364 LEU n 1 365 LYS n 1 366 LYS n 1 367 GLU n 1 368 GLY n 1 369 TRP n 1 370 ARG n 1 371 PRO n 1 372 ARG n 1 373 ARG n 1 374 THR n 1 375 ILE n 1 376 LEU n 1 377 PHE n 1 378 ALA n 1 379 SER n 1 380 TRP n 1 381 ASP n 1 382 ALA n 1 383 GLU n 1 384 GLU n 1 385 PHE n 1 386 GLY n 1 387 LEU n 1 388 LEU n 1 389 GLY n 1 390 SER n 1 391 THR n 1 392 GLU n 1 393 TRP n 1 394 ALA n 1 395 GLU n 1 396 GLU n 1 397 ASN n 1 398 SER n 1 399 ARG n 1 400 LEU n 1 401 LEU n 1 402 GLN n 1 403 GLU n 1 404 ARG n 1 405 GLY n 1 406 VAL n 1 407 ALA n 1 408 TYR n 1 409 ILE n 1 410 ASN n 1 411 ALA n 1 412 ASP n 1 413 SER n 1 414 SER n 1 415 ILE n 1 416 GLU n 1 417 GLY n 1 418 ASN n 1 419 TYR n 1 420 THR n 1 421 LEU n 1 422 ARG n 1 423 VAL n 1 424 ASP n 1 425 CYS n 1 426 THR n 1 427 PRO n 1 428 LEU n 1 429 MET n 1 430 TYR n 1 431 SER n 1 432 LEU n 1 433 VAL n 1 434 HIS n 1 435 ASN n 1 436 LEU n 1 437 THR n 1 438 LYS n 1 439 GLU n 1 440 LEU n 1 441 LYS n 1 442 SER n 1 443 PRO n 1 444 ASP n 1 445 GLU n 1 446 GLY n 1 447 PHE n 1 448 GLU n 1 449 GLY n 1 450 LYS n 1 451 SER n 1 452 LEU n 1 453 TYR n 1 454 GLU n 1 455 SER n 1 456 TRP n 1 457 THR n 1 458 LYS n 1 459 LYS n 1 460 SER n 1 461 PRO n 1 462 SER n 1 463 PRO n 1 464 GLU n 1 465 PHE n 1 466 SER n 1 467 GLY n 1 468 MET n 1 469 PRO n 1 470 ARG n 1 471 ILE n 1 472 SER n 1 473 LYS n 1 474 LEU n 1 475 GLY n 1 476 SER n 1 477 GLY n 1 478 ASN n 1 479 ASP n 1 480 PHE n 1 481 GLU n 1 482 VAL n 1 483 PHE n 1 484 PHE n 1 485 GLN n 1 486 ARG n 1 487 LEU n 1 488 GLY n 1 489 ILE n 1 490 ALA n 1 491 SER n 1 492 GLY n 1 493 ARG n 1 494 ALA n 1 495 ARG n 1 496 TYR n 1 497 THR n 1 498 LYS n 1 499 ASN n 1 500 TRP n 1 501 GLU n 1 502 THR n 1 503 ASN n 1 504 LYS n 1 505 PHE n 1 506 SER n 1 507 GLY n 1 508 TYR n 1 509 PRO n 1 510 LEU n 1 511 TYR n 1 512 HIS n 1 513 SER n 1 514 VAL n 1 515 TYR n 1 516 GLU n 1 517 THR n 1 518 TYR n 1 519 GLU n 1 520 LEU n 1 521 VAL n 1 522 GLU n 1 523 LYS n 1 524 PHE n 1 525 TYR n 1 526 ASP n 1 527 PRO n 1 528 MET n 1 529 PHE n 1 530 LYS n 1 531 TYR n 1 532 HIS n 1 533 LEU n 1 534 THR n 1 535 VAL n 1 536 ALA n 1 537 GLN n 1 538 VAL n 1 539 ARG n 1 540 GLY n 1 541 GLY n 1 542 MET n 1 543 VAL n 1 544 PHE n 1 545 GLU n 1 546 LEU n 1 547 ALA n 1 548 ASN n 1 549 SER n 1 550 ILE n 1 551 VAL n 1 552 GLN n 1 553 PRO n 1 554 PHE n 1 555 ASP n 1 556 CYS n 1 557 ARG n 1 558 ASP n 1 559 TYR n 1 560 ALA n 1 561 VAL n 1 562 VAL n 1 563 LEU n 1 564 ARG n 1 565 LYS n 1 566 TYR n 1 567 ALA n 1 568 ASP n 1 569 LYS n 1 570 ILE n 1 571 TYR n 1 572 SER n 1 573 ILE n 1 574 SER n 1 575 MET n 1 576 LYS n 1 577 HIS n 1 578 PRO n 1 579 GLN n 1 580 GLU n 1 581 MET n 1 582 LYS n 1 583 THR n 1 584 TYR n 1 585 SER n 1 586 VAL n 1 587 SER n 1 588 PHE n 1 589 ASP n 1 590 SER n 1 591 LEU n 1 592 PHE n 1 593 SER n 1 594 ALA n 1 595 VAL n 1 596 LYS n 1 597 ASN n 1 598 PHE n 1 599 THR n 1 600 GLU n 1 601 ILE n 1 602 ALA n 1 603 SER n 1 604 LYS n 1 605 PHE n 1 606 SER n 1 607 GLU n 1 608 ARG n 1 609 LEU n 1 610 GLN n 1 611 ASP n 1 612 PHE n 1 613 ASP n 1 614 LYS n 1 615 SER n 1 616 ASN n 1 617 PRO n 1 618 ILE n 1 619 VAL n 1 620 LEU n 1 621 ARG n 1 622 MET n 1 623 MET n 1 624 ASN n 1 625 ASP n 1 626 GLN n 1 627 LEU n 1 628 MET n 1 629 PHE n 1 630 LEU n 1 631 GLU n 1 632 ARG n 1 633 ALA n 1 634 PHE n 1 635 ILE n 1 636 ASP n 1 637 PRO n 1 638 LEU n 1 639 GLY n 1 640 LEU n 1 641 PRO n 1 642 ASP n 1 643 ARG n 1 644 PRO n 1 645 PHE n 1 646 TYR n 1 647 ARG n 1 648 HIS n 1 649 VAL n 1 650 ILE n 1 651 TYR n 1 652 ALA n 1 653 PRO n 1 654 SER n 1 655 SER n 1 656 HIS n 1 657 ASN n 1 658 LYS n 1 659 TYR n 1 660 ALA n 1 661 GLY n 1 662 GLU n 1 663 SER n 1 664 PHE n 1 665 PRO n 1 666 GLY n 1 667 ILE n 1 668 TYR n 1 669 ASP n 1 670 ALA n 1 671 LEU n 1 672 PHE n 1 673 ASP n 1 674 ILE n 1 675 GLU n 1 676 SER n 1 677 LYS n 1 678 VAL n 1 679 ASP n 1 680 PRO n 1 681 SER n 1 682 LYS n 1 683 ALA n 1 684 TRP n 1 685 GLY n 1 686 GLU n 1 687 VAL n 1 688 LYS n 1 689 ARG n 1 690 GLN n 1 691 ILE n 1 692 TYR n 1 693 VAL n 1 694 ALA n 1 695 ALA n 1 696 PHE n 1 697 THR n 1 698 VAL n 1 699 GLN n 1 700 ALA n 1 701 ALA n 1 702 ALA n 1 703 GLU n 1 704 THR n 1 705 LEU n 1 706 SER n 1 707 GLU n 1 708 VAL n 1 709 ALA n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name HUMAN _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _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 S2 _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code FOLH1_HUMAN _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession Q04609 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 2XEG _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 3 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 709 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q04609 _struct_ref_seq.db_align_beg 44 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 750 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 44 _struct_ref_seq.pdbx_auth_seq_align_end 750 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 2XEG ARG A 1 ? UNP Q04609 ? ? 'expression tag' 42 1 1 2XEG SER A 2 ? UNP Q04609 ? ? 'expression tag' 43 2 1 2XEG GLN A 552 ? UNP Q04609 LEU 593 conflict 593 3 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CI9 non-polymer . ;N-({(1S)-5-[4-(13-{[2,4-BIS(DIHYDROXYAMINO)PHENYL]AMINO}-2,5,8,11-TETRAOXATRIDEC-1-YL)-1H-1,2,3-TRIAZOL-1-YL]-1-CARBOXYPENTYL}CARBAMOYL)-L-GLUTAMIC ACID ; ? 'C29 H46 N8 O15' 746.720 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 2XEG _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.29 _exptl_crystal.density_percent_sol 62.64 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8.0 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '33% (V/V) PENTAERYTHRITOL PROPOXYLATE PO/OH 5/4, 1% (W/V) PEG 3350, 100 MM TRIS-HCL, pH 8.0' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 2009-10-21 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.000 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 22-BM' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 22-BM _diffrn_source.pdbx_wavelength 1.000 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 2XEG _reflns.observed_criterion_sigma_I -3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 30.00 _reflns.d_resolution_high 1.59 _reflns.number_obs 137271 _reflns.number_all ? _reflns.percent_possible_obs 97.6 _reflns.pdbx_Rmerge_I_obs 0.06 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 27.80 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 7.0 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.59 _reflns_shell.d_res_low 1.65 _reflns_shell.percent_possible_all 79.9 _reflns_shell.Rmerge_I_obs 0.50 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.00 _reflns_shell.pdbx_redundancy 5.0 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 2XEG _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 135823 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 30.00 _refine.ls_d_res_high 1.59 _refine.ls_percent_reflns_obs 97.59 _refine.ls_R_factor_obs 0.16879 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.16858 _refine.ls_R_factor_R_free 0.19063 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 1.0 _refine.ls_number_reflns_R_free 1373 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.969 _refine.correlation_coeff_Fo_to_Fc_free 0.962 _refine.B_iso_mean 25.815 _refine.aniso_B[1][1] 0.72 _refine.aniso_B[2][2] -1.77 _refine.aniso_B[3][3] 1.06 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ;HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. ; _refine.pdbx_starting_model 'PDB ENTRY 2OOT' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.067 _refine.pdbx_overall_ESU_R_Free 0.068 _refine.overall_SU_ML 0.047 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 2.464 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 5530 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 232 _refine_hist.number_atoms_solvent 612 _refine_hist.number_atoms_total 6374 _refine_hist.d_res_high 1.59 _refine_hist.d_res_low 30.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.018 0.022 ? 6194 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.711 2.000 ? 8427 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.608 5.000 ? 737 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 35.636 23.754 ? 285 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 13.666 15.000 ? 1014 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 14.051 15.000 ? 36 'X-RAY DIFFRACTION' ? r_chiral_restr 0.126 0.200 ? 902 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.010 0.021 ? 4773 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 0.963 1.500 ? 3588 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.608 2.000 ? 5838 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.582 3.000 ? 2606 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 4.211 4.500 ? 2577 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.591 _refine_ls_shell.d_res_low 1.632 _refine_ls_shell.number_reflns_R_work 7815 _refine_ls_shell.R_factor_R_work 0.253 _refine_ls_shell.percent_reflns_obs 76.88 _refine_ls_shell.R_factor_R_free 0.330 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 72 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 2XEG _struct.title 'Human glutamate carboxypeptidase II in complex with Antibody- Recruiting Molecule ARM-P4' _struct.pdbx_descriptor 'GLUTAMATE CARBOXYPEPTIDASE 2 (E.C.3.4.17.21)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2XEG _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'METALLOPEPTIDASE, 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 5 ? Q N N 6 ? R N N 7 ? S N N 8 ? T N N 9 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASN A 16 ? LEU A 24 ? ASN A 57 LEU A 65 1 ? 9 HELX_P HELX_P2 2 LYS A 25 ? THR A 37 ? LYS A 66 THR A 78 1 ? 13 HELX_P HELX_P3 3 THR A 45 ? GLY A 63 ? THR A 86 GLY A 104 1 ? 19 HELX_P HELX_P4 4 ARG A 140 ? ASP A 150 ? ARG A 181 ASP A 191 1 ? 11 HELX_P HELX_P5 5 PHE A 168 ? ALA A 179 ? PHE A 209 ALA A 220 1 ? 12 HELX_P HELX_P6 6 ASP A 189 ? PHE A 194 ? ASP A 230 PHE A 235 1 ? 6 HELX_P HELX_P7 7 GLY A 241 ? ALA A 245 ? GLY A 282 ALA A 286 5 ? 5 HELX_P HELX_P8 8 GLY A 257 ? GLU A 266 ? GLY A 298 GLU A 307 1 ? 10 HELX_P HELX_P9 9 ASP A 275 ? ARG A 279 ? ASP A 316 ARG A 320 5 ? 5 HELX_P HELX_P10 10 THR A 293 ? SER A 297 ? THR A 334 SER A 338 5 ? 5 HELX_P HELX_P11 11 PRO A 347 ? GLU A 367 ? PRO A 388 GLU A 408 1 ? 21 HELX_P HELX_P12 12 ALA A 382 ? GLY A 386 ? ALA A 423 GLY A 427 5 ? 5 HELX_P HELX_P13 13 LEU A 387 ? ARG A 404 ? LEU A 428 ARG A 445 1 ? 18 HELX_P HELX_P14 14 MET A 429 ? GLU A 439 ? MET A 470 GLU A 480 1 ? 11 HELX_P HELX_P15 15 SER A 451 ? SER A 460 ? SER A 492 SER A 501 1 ? 10 HELX_P HELX_P16 16 ASP A 479 ? GLN A 485 ? ASP A 520 GLN A 526 1 ? 7 HELX_P HELX_P17 17 THR A 517 ? TYR A 525 ? THR A 558 TYR A 566 1 ? 9 HELX_P HELX_P18 18 PHE A 529 ? SER A 549 ? PHE A 570 SER A 590 1 ? 21 HELX_P HELX_P19 19 ASP A 555 ? MET A 575 ? ASP A 596 MET A 616 1 ? 21 HELX_P HELX_P20 20 HIS A 577 ? SER A 585 ? HIS A 618 SER A 626 1 ? 9 HELX_P HELX_P21 21 PHE A 588 ? PHE A 612 ? PHE A 629 PHE A 653 1 ? 25 HELX_P HELX_P22 22 ASN A 616 ? PHE A 634 ? ASN A 657 PHE A 675 1 ? 19 HELX_P HELX_P23 23 PHE A 664 ? PHE A 672 ? PHE A 705 PHE A 713 1 ? 9 HELX_P HELX_P24 24 ASP A 673 ? LYS A 677 ? ASP A 714 LYS A 718 5 ? 5 HELX_P HELX_P25 25 ASP A 679 ? THR A 704 ? ASP A 720 THR A 745 1 ? 26 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order covale1 covale ? ? A ASN 35 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 76 A NAG 1755 1_555 ? ? ? ? ? ? ? 1.440 ? covale2 covale ? ? A ASN 80 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 121 A NAG 1757 1_555 ? ? ? ? ? ? ? 1.441 ? covale3 covale ? ? A ASN 99 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 140 A NAG 1758 1_555 ? ? ? ? ? ? ? 1.434 ? covale4 covale ? ? A ASN 154 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 195 A NAG 1759 1_555 ? ? ? ? ? ? ? 1.444 ? covale5 covale ? ? A ASN 418 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 459 A NAG 1760 1_555 ? ? ? ? ? ? ? 1.453 ? covale6 covale ? ? A ASN 435 ND2 ? ? ? 1_555 M NAG . C1 ? ? A ASN 476 A NAG 1761 1_555 ? ? ? ? ? ? ? 1.441 ? covale7 covale ? ? A ASN 597 ND2 ? ? ? 1_555 O NAG . C1 ? ? A ASN 638 A NAG 1763 1_555 ? ? ? ? ? ? ? 1.445 ? metalc1 metalc ? ? B ZN . ZN ? ? ? 1_555 A GLU 384 OE1 ? ? A ZN 1751 A GLU 425 1_555 ? ? ? ? ? ? ? 2.420 ? metalc2 metalc ? ? B ZN . ZN ? ? ? 1_555 A GLU 384 OE2 ? ? A ZN 1751 A GLU 425 1_555 ? ? ? ? ? ? ? 2.141 ? metalc3 metalc ? ? B ZN . ZN ? ? ? 1_555 A HIS 512 NE2 ? ? A ZN 1751 A HIS 553 1_555 ? ? ? ? ? ? ? 2.058 ? metalc4 metalc ? ? B ZN . ZN ? ? ? 1_555 S CI9 . OAD ? ? A ZN 1751 A CI9 1768 1_555 ? ? ? ? ? ? ? 2.571 ? metalc5 metalc ? ? B ZN . ZN ? ? ? 1_555 A ASP 346 OD2 ? ? A ZN 1751 A ASP 387 1_555 ? ? ? ? ? ? ? 2.087 ? metalc6 metalc ? ? C ZN . ZN ? ? ? 1_555 A ASP 412 OD2 ? ? A ZN 1752 A ASP 453 1_555 ? ? ? ? ? ? ? 1.973 ? metalc7 metalc ? ? C ZN . ZN ? ? ? 1_555 A ASP 346 OD1 ? ? A ZN 1752 A ASP 387 1_555 ? ? ? ? ? ? ? 1.996 ? metalc8 metalc ? ? C ZN . ZN ? ? ? 1_555 A HIS 336 NE2 ? ? A ZN 1752 A HIS 377 1_555 ? ? ? ? ? ? ? 2.033 ? metalc9 metalc ? ? D CA . CA ? ? ? 1_555 A GLU 392 OE1 ? ? A CA 1753 A GLU 433 1_555 ? ? ? ? ? ? ? 2.511 ? metalc10 metalc ? ? D CA . CA ? ? ? 1_555 A TYR 231 O ? ? A CA 1753 A TYR 272 1_555 ? ? ? ? ? ? ? 2.315 ? metalc11 metalc ? ? D CA . CA ? ? ? 1_555 A GLU 392 OE2 ? ? A CA 1753 A GLU 433 1_555 ? ? ? ? ? ? ? 2.504 ? metalc12 metalc ? ? D CA . CA ? ? ? 1_555 A THR 228 OG1 ? ? A CA 1753 A THR 269 1_555 ? ? ? ? ? ? ? 2.489 ? metalc13 metalc ? ? D CA . CA ? ? ? 1_555 A GLU 395 OE2 ? ? A CA 1753 A GLU 436 1_555 ? ? ? ? ? ? ? 2.315 ? metalc14 metalc ? ? D CA . CA ? ? ? 1_555 A THR 228 O ? ? A CA 1753 A THR 269 1_555 ? ? ? ? ? ? ? 2.443 ? metalc15 metalc ? ? D CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 1753 A HOH 2196 1_555 ? ? ? ? ? ? ? 2.420 ? covale8 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 1755 A NAG 1756 1_555 ? ? ? ? ? ? ? 1.443 ? covale9 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 1758 A NAG 1767 1_555 ? ? ? ? ? ? ? 1.442 ? covale10 covale ? ? M NAG . O4 ? ? ? 1_555 N NAG . C1 ? ? A NAG 1761 A NAG 1762 1_555 ? ? ? ? ? ? ? 1.446 ? covale11 covale ? ? O NAG . O4 ? ? ? 1_555 P NAG . C1 ? ? A NAG 1763 A NAG 1764 1_555 ? ? ? ? ? ? ? 1.436 ? covale12 covale ? ? P NAG . O4 ? ? ? 1_555 Q BMA . C1 ? ? A NAG 1764 A BMA 1765 1_555 ? ? ? ? ? ? ? 1.428 ? covale13 covale ? ? Q BMA . O3 ? ? ? 1_555 R MAN . C1 ? ? A BMA 1765 A MAN 1766 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 201 A . ? TYR 242 A PRO 202 A ? PRO 243 A 1 9.72 2 GLY 289 A . ? GLY 330 A PRO 290 A ? PRO 331 A 1 0.76 3 ASP 346 A . ? ASP 387 A PRO 347 A ? PRO 388 A 1 6.91 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 7 ? AB ? 4 ? AC ? 2 ? AD ? 4 ? AE ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA 1 2 ? anti-parallel AA 2 3 ? anti-parallel AA 3 4 ? parallel AA 4 5 ? parallel AA 5 6 ? parallel AA 6 7 ? anti-parallel AB 1 2 ? anti-parallel AB 2 3 ? anti-parallel AB 3 4 ? anti-parallel AC 1 2 ? parallel AD 1 2 ? parallel AD 2 3 ? parallel AD 3 4 ? parallel AE 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA 1 SER A 66 ? TYR A 78 ? SER A 107 TYR A 119 AA 2 THR A 308 ? LEU A 321 ? THR A 349 LEU A 362 AA 3 ARG A 373 ? TRP A 380 ? ARG A 414 TRP A 421 AA 4 GLU A 326 ? HIS A 336 ? GLU A 367 HIS A 377 AA 5 GLY A 405 ? ASN A 410 ? GLY A 446 ASN A 451 AA 6 ALA A 490 ? THR A 497 ? ALA A 531 THR A 538 AA 7 THR A 420 ? CYS A 425 ? THR A 461 CYS A 466 AB 1 GLU A 96 ? ASN A 99 ? GLU A 137 ASN A 140 AB 2 TYR A 86 ? ILE A 90 ? TYR A 127 ILE A 131 AB 3 LYS A 300 ? HIS A 304 ? LYS A 341 HIS A 345 AB 4 GLU A 130 ? GLY A 131 ? GLU A 171 GLY A 172 AC 1 SER A 121 ? ALA A 122 ? SER A 162 ALA A 163 AC 2 GLY A 215 ? ASN A 216 ? GLY A 256 ASN A 257 AD 1 LEU A 133 ? TYR A 135 ? LEU A 174 TYR A 176 AD 2 ILE A 159 ? ARG A 163 ? ILE A 200 ARG A 204 AD 3 GLY A 183 ? TYR A 187 ? GLY A 224 TYR A 228 AD 4 VAL A 253 ? ILE A 256 ? VAL A 294 ILE A 297 AE 1 TYR A 651 ? SER A 654 ? TYR A 692 SER A 695 AE 2 ASN A 657 ? SER A 663 ? ASN A 698 SER A 704 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA 1 2 N TYR A 78 ? N TYR A 119 O THR A 308 ? O THR A 349 AA 2 3 N LEU A 321 ? N LEU A 362 O ILE A 375 ? O ILE A 416 AA 3 4 N THR A 374 ? N THR A 415 O ARG A 329 ? O ARG A 370 AA 4 5 O TYR A 330 ? O TYR A 371 N VAL A 406 ? N VAL A 447 AA 5 6 N TYR A 408 ? N TYR A 449 O ALA A 490 ? O ALA A 531 AA 6 7 N THR A 497 ? N THR A 538 O THR A 420 ? O THR A 461 AB 1 2 N ILE A 97 ? N ILE A 138 O ILE A 89 ? O ILE A 130 AB 2 3 N ILE A 90 ? N ILE A 131 O LYS A 300 ? O LYS A 341 AB 3 4 N VAL A 301 ? N VAL A 342 O GLY A 131 ? O GLY A 172 AC 1 2 N ALA A 122 ? N ALA A 163 O GLY A 215 ? O GLY A 256 AD 1 2 N VAL A 134 ? N VAL A 175 O ILE A 159 ? O ILE A 200 AD 2 3 N VAL A 160 ? N VAL A 201 O GLY A 183 ? O GLY A 224 AD 3 4 N LEU A 186 ? N LEU A 227 O HIS A 254 ? O HIS A 295 AE 1 2 O SER A 654 ? O SER A 695 N ASN A 657 ? N ASN A 698 # 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 ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 1751' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ZN A 1752' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 1753' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CL A 1754' AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 1757' AC6 Software ? ? ? ? 31 'BINDING SITE FOR RESIDUE CI9 A 1768' AC7 Software ? ? ? ? 7 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 76 RESIDUES 1755 TO 1756' AC8 Software ? ? ? ? 34 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 140 RESIDUES 1758 TO 1767' AC9 Software ? ? ? ? 8 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 476 RESIDUES 1761 TO 1762' BC1 Software ? ? ? ? 8 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 638 RESIDUES 1763 TO 1766' # 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 346 ? ASP A 387 . ? 1_555 ? 2 AC1 5 GLU A 384 ? GLU A 425 . ? 1_555 ? 3 AC1 5 HIS A 512 ? HIS A 553 . ? 1_555 ? 4 AC1 5 ZN C . ? ZN A 1752 . ? 1_555 ? 5 AC1 5 CI9 S . ? CI9 A 1768 . ? 1_555 ? 6 AC2 6 HIS A 336 ? HIS A 377 . ? 1_555 ? 7 AC2 6 ASP A 346 ? ASP A 387 . ? 1_555 ? 8 AC2 6 GLU A 383 ? GLU A 424 . ? 1_555 ? 9 AC2 6 GLU A 384 ? GLU A 425 . ? 1_555 ? 10 AC2 6 ASP A 412 ? ASP A 453 . ? 1_555 ? 11 AC2 6 ZN B . ? ZN A 1751 . ? 1_555 ? 12 AC3 5 THR A 228 ? THR A 269 . ? 1_555 ? 13 AC3 5 TYR A 231 ? TYR A 272 . ? 1_555 ? 14 AC3 5 GLU A 392 ? GLU A 433 . ? 1_555 ? 15 AC3 5 GLU A 395 ? GLU A 436 . ? 1_555 ? 16 AC3 5 HOH T . ? HOH A 2196 . ? 1_555 ? 17 AC4 5 ASN A 410 ? ASN A 451 . ? 1_555 ? 18 AC4 5 ASP A 412 ? ASP A 453 . ? 1_555 ? 19 AC4 5 ARG A 493 ? ARG A 534 . ? 1_555 ? 20 AC4 5 ARG A 495 ? ARG A 536 . ? 1_555 ? 21 AC4 5 HOH T . ? HOH A 2392 . ? 1_555 ? 22 AC5 5 ASN A 80 ? ASN A 121 . ? 1_555 ? 23 AC5 5 THR A 82 ? THR A 123 . ? 1_555 ? 24 AC5 5 HIS A 83 ? HIS A 124 . ? 1_555 ? 25 AC5 5 THR A 308 ? THR A 349 . ? 1_555 ? 26 AC5 5 HOH T . ? HOH A 2115 . ? 1_555 ? 27 AC6 31 LYS A 166 ? LYS A 207 . ? 1_555 ? 28 AC6 31 ARG A 169 ? ARG A 210 . ? 1_555 ? 29 AC6 31 ASN A 216 ? ASN A 257 . ? 1_555 ? 30 AC6 31 ASP A 346 ? ASP A 387 . ? 1_555 ? 31 AC6 31 GLU A 383 ? GLU A 424 . ? 1_555 ? 32 AC6 31 GLU A 384 ? GLU A 425 . ? 1_555 ? 33 AC6 31 GLY A 386 ? GLY A 427 . ? 1_555 ? 34 AC6 31 LEU A 387 ? LEU A 428 . ? 1_555 ? 35 AC6 31 ARG A 422 ? ARG A 463 . ? 1_555 ? 36 AC6 31 SER A 460 ? SER A 501 . ? 1_555 ? 37 AC6 31 ARG A 470 ? ARG A 511 . ? 1_555 ? 38 AC6 31 SER A 472 ? SER A 513 . ? 1_555 ? 39 AC6 31 GLY A 477 ? GLY A 518 . ? 1_555 ? 40 AC6 31 ASN A 478 ? ASN A 519 . ? 1_555 ? 41 AC6 31 ARG A 493 ? ARG A 534 . ? 1_555 ? 42 AC6 31 ARG A 495 ? ARG A 536 . ? 1_555 ? 43 AC6 31 TRP A 500 ? TRP A 541 . ? 1_555 ? 44 AC6 31 GLU A 501 ? GLU A 542 . ? 1_555 ? 45 AC6 31 TYR A 511 ? TYR A 552 . ? 1_555 ? 46 AC6 31 HIS A 512 ? HIS A 553 . ? 1_555 ? 47 AC6 31 ASN A 657 ? ASN A 698 . ? 1_555 ? 48 AC6 31 LYS A 658 ? LYS A 699 . ? 1_555 ? 49 AC6 31 TYR A 659 ? TYR A 700 . ? 1_555 ? 50 AC6 31 ALA A 660 ? ALA A 701 . ? 1_555 ? 51 AC6 31 ZN B . ? ZN A 1751 . ? 1_555 ? 52 AC6 31 HOH T . ? HOH A 2385 . ? 1_555 ? 53 AC6 31 HOH T . ? HOH A 2608 . ? 1_555 ? 54 AC6 31 HOH T . ? HOH A 2609 . ? 1_555 ? 55 AC6 31 HOH T . ? HOH A 2610 . ? 1_555 ? 56 AC6 31 HOH T . ? HOH A 2611 . ? 1_555 ? 57 AC6 31 HOH T . ? HOH A 2612 . ? 1_555 ? 58 AC7 7 ASN A 35 ? ASN A 76 . ? 1_555 ? 59 AC7 7 GLN A 58 ? GLN A 99 . ? 1_555 ? 60 AC7 7 HOH T . ? HOH A 2022 . ? 1_555 ? 61 AC7 7 HOH T . ? HOH A 2032 . ? 1_555 ? 62 AC7 7 HOH T . ? HOH A 2594 . ? 1_555 ? 63 AC7 7 HOH T . ? HOH A 2595 . ? 1_555 ? 64 AC7 7 HOH T . ? HOH A 2596 . ? 1_555 ? 65 AC8 34 TYR A 86 ? TYR A 127 . ? 1_555 ? 66 AC8 34 GLU A 96 ? GLU A 137 . ? 1_555 ? 67 AC8 34 ILE A 97 ? ILE A 138 . ? 1_555 ? 68 AC8 34 ASN A 99 ? ASN A 140 . ? 1_555 ? 69 AC8 34 ASN A 154 ? ASN A 195 . ? 1_555 ? 70 AC8 34 SER A 156 ? SER A 197 . ? 1_555 ? 71 AC8 34 TRP A 205 ? TRP A 246 . ? 1_555 ? 72 AC8 34 ASN A 418 ? ASN A 459 . ? 1_555 ? 73 AC8 34 SER A 431 ? SER A 472 . ? 1_555 ? 74 AC8 34 ASN A 435 ? ASN A 476 . ? 1_555 ? 75 AC8 34 PHE A 524 ? PHE A 565 . ? 1_555 ? 76 AC8 34 TYR A 525 ? TYR A 566 . ? 1_555 ? 77 AC8 34 PRO A 553 ? PRO A 594 . ? 1_555 ? 78 AC8 34 SER A 590 ? SER A 631 . ? 1_555 ? 79 AC8 34 SER A 593 ? SER A 634 . ? 1_555 ? 80 AC8 34 ASN A 597 ? ASN A 638 . ? 1_555 ? 81 AC8 34 GLN A 610 ? GLN A 651 . ? 1_555 ? 82 AC8 34 GLN A 699 ? GLN A 740 . ? 1_555 ? 83 AC8 34 HOH T . ? HOH A 2078 . ? 1_555 ? 84 AC8 34 HOH T . ? HOH A 2341 . ? 1_555 ? 85 AC8 34 HOH T . ? HOH A 2342 . ? 1_555 ? 86 AC8 34 HOH T . ? HOH A 2411 . ? 1_555 ? 87 AC8 34 HOH T . ? HOH A 2422 . ? 1_555 ? 88 AC8 34 HOH T . ? HOH A 2597 . ? 1_555 ? 89 AC8 34 HOH T . ? HOH A 2598 . ? 1_555 ? 90 AC8 34 HOH T . ? HOH A 2599 . ? 1_555 ? 91 AC8 34 HOH T . ? HOH A 2600 . ? 1_555 ? 92 AC8 34 HOH T . ? HOH A 2601 . ? 1_555 ? 93 AC8 34 HOH T . ? HOH A 2602 . ? 1_555 ? 94 AC8 34 HOH T . ? HOH A 2603 . ? 1_555 ? 95 AC8 34 HOH T . ? HOH A 2604 . ? 1_555 ? 96 AC8 34 HOH T . ? HOH A 2605 . ? 1_555 ? 97 AC8 34 HOH T . ? HOH A 2606 . ? 1_555 ? 98 AC8 34 HOH T . ? HOH A 2607 . ? 1_555 ? 99 AC9 8 SER A 431 ? SER A 472 . ? 1_555 ? 100 AC9 8 ASN A 435 ? ASN A 476 . ? 1_555 ? 101 AC9 8 PRO A 553 ? PRO A 594 . ? 1_555 ? 102 AC9 8 GLN A 610 ? GLN A 651 . ? 1_555 ? 103 AC9 8 HOH T . ? HOH A 2422 . ? 1_555 ? 104 AC9 8 HOH T . ? HOH A 2600 . ? 1_555 ? 105 AC9 8 HOH T . ? HOH A 2601 . ? 1_555 ? 106 AC9 8 HOH T . ? HOH A 2602 . ? 1_555 ? 107 BC1 8 SER A 590 ? SER A 631 . ? 1_555 ? 108 BC1 8 SER A 593 ? SER A 634 . ? 1_555 ? 109 BC1 8 ASN A 597 ? ASN A 638 . ? 1_555 ? 110 BC1 8 GLN A 699 ? GLN A 740 . ? 1_555 ? 111 BC1 8 HOH T . ? HOH A 2603 . ? 1_555 ? 112 BC1 8 HOH T . ? HOH A 2604 . ? 1_555 ? 113 BC1 8 HOH T . ? HOH A 2605 . ? 1_555 ? 114 BC1 8 HOH T . ? HOH A 2606 . ? 1_555 ? # _database_PDB_matrix.entry_id 2XEG _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 2XEG _atom_sites.fract_transf_matrix[1][1] 0.009832 _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] 0.007690 _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] 0.006288 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CA CL N O S ZN # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . LYS A 1 14 ? 16.326 45.196 82.704 1.00 51.29 ? 55 LYS A N 1 ATOM 2 C CA . LYS A 1 14 ? 16.069 46.421 81.951 1.00 50.02 ? 55 LYS A CA 1 ATOM 3 C C . LYS A 1 14 ? 15.778 46.107 80.483 1.00 48.05 ? 55 LYS A C 1 ATOM 4 O O . LYS A 1 14 ? 16.479 45.323 79.849 1.00 47.47 ? 55 LYS A O 1 ATOM 5 C CB . LYS A 1 14 ? 17.127 47.525 82.050 1.00 51.23 ? 55 LYS A CB 1 ATOM 6 C CG . LYS A 1 14 ? 16.578 48.921 82.319 1.00 53.98 ? 55 LYS A CG 1 ATOM 7 C CD . LYS A 1 14 ? 15.933 49.539 81.070 1.00 57.25 ? 55 LYS A CD 1 ATOM 8 C CE . LYS A 1 14 ? 15.676 51.030 81.247 1.00 58.67 ? 55 LYS A CE 1 ATOM 9 N NZ . LYS A 1 14 ? 15.150 51.607 79.976 1.00 60.66 ? 55 LYS A NZ 1 ATOM 10 N N . HIS A 1 15 ? 14.722 46.724 79.967 1.00 45.87 ? 56 HIS A N 1 ATOM 11 C CA . HIS A 1 15 ? 14.366 46.627 78.557 1.00 43.49 ? 56 HIS A CA 1 ATOM 12 C C . HIS A 1 15 ? 14.850 47.903 77.899 1.00 41.40 ? 56 HIS A C 1 ATOM 13 O O . HIS A 1 15 ? 14.203 48.943 77.994 1.00 43.00 ? 56 HIS A O 1 ATOM 14 C CB . HIS A 1 15 ? 12.860 46.548 78.401 1.00 43.77 ? 56 HIS A CB 1 ATOM 15 C CG . HIS A 1 15 ? 12.264 45.265 78.885 1.00 44.77 ? 56 HIS A CG 1 ATOM 16 N ND1 . HIS A 1 15 ? 12.812 44.032 78.592 1.00 45.57 ? 56 HIS A ND1 1 ATOM 17 C CD2 . HIS A 1 15 ? 11.140 45.022 79.601 1.00 44.14 ? 56 HIS A CD2 1 ATOM 18 C CE1 . HIS A 1 15 ? 12.058 43.086 79.121 1.00 45.79 ? 56 HIS A CE1 1 ATOM 19 N NE2 . HIS A 1 15 ? 11.031 43.659 79.725 1.00 47.01 ? 56 HIS A NE2 1 ATOM 20 N N . ASN A 1 16 ? 16.012 47.833 77.269 1.00 37.35 ? 57 ASN A N 1 ATOM 21 C CA . ASN A 1 16 ? 16.577 48.996 76.615 1.00 34.03 ? 57 ASN A CA 1 ATOM 22 C C . ASN A 1 16 ? 17.206 48.498 75.349 1.00 30.58 ? 57 ASN A C 1 ATOM 23 O O . ASN A 1 16 ? 17.041 47.326 75.001 1.00 29.24 ? 57 ASN A O 1 ATOM 24 C CB . ASN A 1 16 ? 17.606 49.690 77.506 1.00 33.90 ? 57 ASN A CB 1 ATOM 25 C CG . ASN A 1 16 ? 18.575 48.725 78.156 1.00 35.94 ? 57 ASN A CG 1 ATOM 26 O OD1 . ASN A 1 16 ? 19.184 49.070 79.176 1.00 39.84 ? 57 ASN A OD1 1 ATOM 27 N ND2 . ASN A 1 16 ? 18.722 47.521 77.611 1.00 31.43 ? 57 ASN A ND2 1 ATOM 28 N N . MET A 1 17 ? 17.934 49.348 74.648 1.00 29.51 ? 58 MET A N 1 ATOM 29 C CA A MET A 1 17 ? 18.495 48.937 73.351 0.60 29.18 ? 58 MET A CA 1 ATOM 30 C CA B MET A 1 17 ? 18.399 48.846 73.380 0.40 28.72 ? 58 MET A CA 1 ATOM 31 C C . MET A 1 17 ? 19.435 47.743 73.546 1.00 28.85 ? 58 MET A C 1 ATOM 32 O O . MET A 1 17 ? 19.477 46.807 72.732 1.00 28.63 ? 58 MET A O 1 ATOM 33 C CB A MET A 1 17 ? 19.221 50.096 72.635 0.60 29.11 ? 58 MET A CB 1 ATOM 34 C CB B MET A 1 17 ? 18.875 49.917 72.430 0.40 28.31 ? 58 MET A CB 1 ATOM 35 C CG A MET A 1 17 ? 19.696 49.724 71.196 0.60 31.39 ? 58 MET A CG 1 ATOM 36 C CG B MET A 1 17 ? 18.852 49.328 71.035 0.40 27.68 ? 58 MET A CG 1 ATOM 37 S SD A MET A 1 17 ? 20.101 51.131 70.132 0.60 36.42 ? 58 MET A SD 1 ATOM 38 S SD B MET A 1 17 ? 20.009 50.135 70.013 0.40 25.80 ? 58 MET A SD 1 ATOM 39 C CE A MET A 1 17 ? 21.506 51.828 71.008 0.60 37.18 ? 58 MET A CE 1 ATOM 40 C CE B MET A 1 17 ? 19.199 51.728 69.803 0.40 24.46 ? 58 MET A CE 1 ATOM 41 N N . LYS A 1 18 ? 20.234 47.800 74.608 1.00 29.02 ? 59 LYS A N 1 ATOM 42 C CA . LYS A 1 18 ? 21.213 46.753 74.843 1.00 29.57 ? 59 LYS A CA 1 ATOM 43 C C . LYS A 1 18 ? 20.545 45.382 74.973 1.00 28.79 ? 59 LYS A C 1 ATOM 44 O O . LYS A 1 18 ? 21.063 44.383 74.480 1.00 29.39 ? 59 LYS A O 1 ATOM 45 C CB . LYS A 1 18 ? 22.013 47.059 76.123 1.00 30.30 ? 59 LYS A CB 1 ATOM 46 C CG . LYS A 1 18 ? 23.162 46.090 76.386 1.00 32.84 ? 59 LYS A CG 1 ATOM 47 C CD . LYS A 1 18 ? 23.788 46.368 77.779 1.00 38.93 ? 59 LYS A CD 1 ATOM 48 C CE . LYS A 1 18 ? 25.095 45.557 78.075 1.00 44.08 ? 59 LYS A CE 1 ATOM 49 N NZ . LYS A 1 18 ? 25.316 44.289 77.277 1.00 47.16 ? 59 LYS A NZ 1 ATOM 50 N N . ALA A 1 19 ? 19.401 45.339 75.649 1.00 28.72 ? 60 ALA A N 1 ATOM 51 C CA . ALA A 1 19 ? 18.666 44.083 75.827 1.00 29.82 ? 60 ALA A CA 1 ATOM 52 C C . ALA A 1 19 ? 18.218 43.575 74.463 1.00 28.61 ? 60 ALA A C 1 ATOM 53 O O . ALA A 1 19 ? 18.341 42.388 74.161 1.00 29.56 ? 60 ALA A O 1 ATOM 54 C CB . ALA A 1 19 ? 17.462 44.285 76.712 1.00 30.62 ? 60 ALA A CB 1 ATOM 55 N N . PHE A 1 20 ? 17.690 44.490 73.658 1.00 27.05 ? 61 PHE A N 1 ATOM 56 C CA . PHE A 1 20 ? 17.287 44.101 72.312 1.00 26.55 ? 61 PHE A CA 1 ATOM 57 C C . PHE A 1 20 ? 18.469 43.569 71.492 1.00 24.45 ? 61 PHE A C 1 ATOM 58 O O . PHE A 1 20 ? 18.401 42.492 70.889 1.00 24.97 ? 61 PHE A O 1 ATOM 59 C CB . PHE A 1 20 ? 16.612 45.275 71.596 1.00 24.39 ? 61 PHE A CB 1 ATOM 60 C CG . PHE A 1 20 ? 16.541 45.068 70.104 1.00 24.18 ? 61 PHE A CG 1 ATOM 61 C CD1 . PHE A 1 20 ? 15.611 44.188 69.554 1.00 24.74 ? 61 PHE A CD1 1 ATOM 62 C CD2 . PHE A 1 20 ? 17.476 45.666 69.293 1.00 23.26 ? 61 PHE A CD2 1 ATOM 63 C CE1 . PHE A 1 20 ? 15.603 43.945 68.162 1.00 23.16 ? 61 PHE A CE1 1 ATOM 64 C CE2 . PHE A 1 20 ? 17.459 45.446 67.904 1.00 20.56 ? 61 PHE A CE2 1 ATOM 65 C CZ . PHE A 1 20 ? 16.561 44.570 67.359 1.00 22.94 ? 61 PHE A CZ 1 ATOM 66 N N . LEU A 1 21 ? 19.573 44.309 71.488 1.00 25.02 ? 62 LEU A N 1 ATOM 67 C CA . LEU A 1 21 ? 20.733 43.910 70.706 1.00 24.91 ? 62 LEU A CA 1 ATOM 68 C C . LEU A 1 21 ? 21.317 42.585 71.174 1.00 26.11 ? 62 LEU A C 1 ATOM 69 O O . LEU A 1 21 ? 21.744 41.776 70.368 1.00 26.43 ? 62 LEU A O 1 ATOM 70 C CB . LEU A 1 21 ? 21.815 44.981 70.733 1.00 25.66 ? 62 LEU A CB 1 ATOM 71 C CG . LEU A 1 21 ? 21.385 46.298 70.107 1.00 25.19 ? 62 LEU A CG 1 ATOM 72 C CD1 . LEU A 1 21 ? 22.396 47.381 70.426 1.00 28.66 ? 62 LEU A CD1 1 ATOM 73 C CD2 . LEU A 1 21 ? 21.267 46.107 68.579 1.00 25.09 ? 62 LEU A CD2 1 ATOM 74 N N . ASP A 1 22 ? 21.321 42.358 72.485 1.00 26.78 ? 63 ASP A N 1 ATOM 75 C CA . ASP A 1 22 ? 21.988 41.160 73.024 1.00 28.85 ? 63 ASP A CA 1 ATOM 76 C C . ASP A 1 22 ? 21.215 39.890 72.709 1.00 28.00 ? 63 ASP A C 1 ATOM 77 O O . ASP A 1 22 ? 21.782 38.799 72.710 1.00 29.41 ? 63 ASP A O 1 ATOM 78 C CB . ASP A 1 22 ? 22.095 41.286 74.548 1.00 30.07 ? 63 ASP A CB 1 ATOM 79 C CG . ASP A 1 22 ? 23.228 42.189 74.995 1.00 33.52 ? 63 ASP A CG 1 ATOM 80 O OD1 . ASP A 1 22 ? 24.099 42.553 74.172 1.00 34.43 ? 63 ASP A OD1 1 ATOM 81 O OD2 . ASP A 1 22 ? 23.242 42.534 76.208 1.00 35.43 ? 63 ASP A OD2 1 ATOM 82 N N . GLU A 1 23 ? 19.907 40.029 72.496 1.00 27.28 ? 64 GLU A N 1 ATOM 83 C CA . GLU A 1 23 ? 19.072 38.892 72.209 1.00 27.53 ? 64 GLU A CA 1 ATOM 84 C C . GLU A 1 23 ? 19.313 38.348 70.802 1.00 26.65 ? 64 GLU A C 1 ATOM 85 O O . GLU A 1 23 ? 19.116 37.147 70.573 1.00 27.76 ? 64 GLU A O 1 ATOM 86 C CB . GLU A 1 23 ? 17.606 39.230 72.448 1.00 27.92 ? 64 GLU A CB 1 ATOM 87 C CG . GLU A 1 23 ? 16.629 38.097 72.137 1.00 30.07 ? 64 GLU A CG 1 ATOM 88 C CD . GLU A 1 23 ? 16.816 36.871 73.036 1.00 33.78 ? 64 GLU A CD 1 ATOM 89 O OE1 . GLU A 1 23 ? 17.081 37.060 74.247 1.00 36.37 ? 64 GLU A OE1 1 ATOM 90 O OE2 . GLU A 1 23 ? 16.711 35.730 72.537 1.00 32.58 ? 64 GLU A OE2 1 ATOM 91 N N . LEU A 1 24 ? 19.778 39.211 69.883 1.00 25.63 ? 65 LEU A N 1 ATOM 92 C CA . LEU A 1 24 ? 20.119 38.791 68.500 1.00 24.76 ? 65 LEU A CA 1 ATOM 93 C C . LEU A 1 24 ? 21.259 37.773 68.493 1.00 25.81 ? 65 LEU A C 1 ATOM 94 O O . LEU A 1 24 ? 22.283 38.019 69.127 1.00 26.80 ? 65 LEU A O 1 ATOM 95 C CB . LEU A 1 24 ? 20.545 40.009 67.654 1.00 23.76 ? 65 LEU A CB 1 ATOM 96 C CG . LEU A 1 24 ? 19.559 41.192 67.537 1.00 23.91 ? 65 LEU A CG 1 ATOM 97 C CD1 . LEU A 1 24 ? 20.255 42.435 67.016 1.00 23.62 ? 65 LEU A CD1 1 ATOM 98 C CD2 . LEU A 1 24 ? 18.379 40.803 66.610 1.00 22.56 ? 65 LEU A CD2 1 ATOM 99 N N . LYS A 1 25 ? 21.118 36.714 67.685 1.00 24.71 ? 66 LYS A N 1 ATOM 100 C CA . LYS A 1 25 ? 22.136 35.650 67.651 1.00 25.33 ? 66 LYS A CA 1 ATOM 101 C C . LYS A 1 25 ? 22.522 35.307 66.221 1.00 24.03 ? 66 LYS A C 1 ATOM 102 O O . LYS A 1 25 ? 21.663 35.010 65.402 1.00 24.05 ? 66 LYS A O 1 ATOM 103 C CB . LYS A 1 25 ? 21.583 34.375 68.343 1.00 25.80 ? 66 LYS A CB 1 ATOM 104 C CG . LYS A 1 25 ? 21.193 34.560 69.845 1.00 29.56 ? 66 LYS A CG 1 ATOM 105 C CD . LYS A 1 25 ? 22.414 34.980 70.656 1.00 37.13 ? 66 LYS A CD 1 ATOM 106 C CE . LYS A 1 25 ? 22.193 34.891 72.177 1.00 39.17 ? 66 LYS A CE 1 ATOM 107 N NZ . LYS A 1 25 ? 21.394 36.022 72.691 1.00 37.74 ? 66 LYS A NZ 1 ATOM 108 N N . ALA A 1 26 ? 23.824 35.254 65.948 1.00 23.61 ? 67 ALA A N 1 ATOM 109 C CA . ALA A 1 26 ? 24.312 34.812 64.667 1.00 23.89 ? 67 ALA A CA 1 ATOM 110 C C . ALA A 1 26 ? 23.782 33.439 64.309 1.00 23.88 ? 67 ALA A C 1 ATOM 111 O O . ALA A 1 26 ? 23.463 33.194 63.137 1.00 23.12 ? 67 ALA A O 1 ATOM 112 C CB . ALA A 1 26 ? 25.824 34.791 64.658 1.00 22.30 ? 67 ALA A CB 1 ATOM 113 N N . GLU A 1 27 ? 23.730 32.528 65.290 1.00 24.36 ? 68 GLU A N 1 ATOM 114 C CA . GLU A 1 27 ? 23.318 31.148 64.973 1.00 26.21 ? 68 GLU A CA 1 ATOM 115 C C . GLU A 1 27 ? 21.860 31.063 64.517 1.00 25.31 ? 68 GLU A C 1 ATOM 116 O O . GLU A 1 27 ? 21.498 30.206 63.675 1.00 24.56 ? 68 GLU A O 1 ATOM 117 C CB . GLU A 1 27 ? 23.514 30.249 66.194 1.00 27.30 ? 68 GLU A CB 1 ATOM 118 C CG . GLU A 1 27 ? 23.003 28.821 65.970 1.00 34.45 ? 68 GLU A CG 1 ATOM 119 C CD . GLU A 1 27 ? 23.735 28.097 64.826 1.00 44.86 ? 68 GLU A CD 1 ATOM 120 O OE1 . GLU A 1 27 ? 23.021 27.566 63.907 1.00 48.87 ? 68 GLU A OE1 1 ATOM 121 O OE2 . GLU A 1 27 ? 25.008 28.097 64.828 1.00 44.35 ? 68 GLU A OE2 1 ATOM 122 N N . ASN A 1 28 ? 21.027 31.973 65.032 1.00 23.94 ? 69 ASN A N 1 ATOM 123 C CA . ASN A 1 28 ? 19.619 32.032 64.618 1.00 23.24 ? 69 ASN A CA 1 ATOM 124 C C . ASN A 1 28 ? 19.534 32.518 63.178 1.00 22.15 ? 69 ASN A C 1 ATOM 125 O O . ASN A 1 28 ? 18.781 31.969 62.367 1.00 21.89 ? 69 ASN A O 1 ATOM 126 C CB . ASN A 1 28 ? 18.816 32.941 65.536 1.00 24.07 ? 69 ASN A CB 1 ATOM 127 C CG . ASN A 1 28 ? 18.543 32.291 66.874 1.00 25.43 ? 69 ASN A CG 1 ATOM 128 O OD1 . ASN A 1 28 ? 18.500 31.054 66.971 1.00 26.48 ? 69 ASN A OD1 1 ATOM 129 N ND2 . ASN A 1 28 ? 18.362 33.113 67.910 1.00 25.48 ? 69 ASN A ND2 1 ATOM 130 N N . ILE A 1 29 ? 20.330 33.535 62.853 1.00 21.53 ? 70 ILE A N 1 ATOM 131 C CA . ILE A 1 29 ? 20.331 34.086 61.472 1.00 21.61 ? 70 ILE A CA 1 ATOM 132 C C . ILE A 1 29 ? 20.772 32.987 60.488 1.00 21.94 ? 70 ILE A C 1 ATOM 133 O O . ILE A 1 29 ? 20.162 32.810 59.409 1.00 21.60 ? 70 ILE A O 1 ATOM 134 C CB . ILE A 1 29 ? 21.235 35.322 61.374 1.00 20.96 ? 70 ILE A CB 1 ATOM 135 C CG1 . ILE A 1 29 ? 20.718 36.428 62.344 1.00 22.49 ? 70 ILE A CG1 1 ATOM 136 C CG2 . ILE A 1 29 ? 21.269 35.860 59.916 1.00 21.32 ? 70 ILE A CG2 1 ATOM 137 C CD1 . ILE A 1 29 ? 21.678 37.601 62.499 1.00 24.09 ? 70 ILE A CD1 1 ATOM 138 N N . LYS A 1 30 ? 21.809 32.224 60.866 1.00 21.92 ? 71 LYS A N 1 ATOM 139 C CA . LYS A 1 30 ? 22.260 31.082 60.065 1.00 21.97 ? 71 LYS A CA 1 ATOM 140 C C . LYS A 1 30 ? 21.167 30.044 59.836 1.00 22.82 ? 71 LYS A C 1 ATOM 141 O O . LYS A 1 30 ? 20.932 29.632 58.688 1.00 23.41 ? 71 LYS A O 1 ATOM 142 C CB . LYS A 1 30 ? 23.456 30.427 60.790 1.00 23.30 ? 71 LYS A CB 1 ATOM 143 C CG . LYS A 1 30 ? 23.983 29.197 60.069 1.00 24.29 ? 71 LYS A CG 1 ATOM 144 C CD . LYS A 1 30 ? 25.241 28.714 60.835 1.00 27.38 ? 71 LYS A CD 1 ATOM 145 C CE . LYS A 1 30 ? 25.963 27.613 60.081 1.00 30.94 ? 71 LYS A CE 1 ATOM 146 N NZ . LYS A 1 30 ? 27.148 27.098 60.923 1.00 28.84 ? 71 LYS A NZ 1 ATOM 147 N N . LYS A 1 31 ? 20.482 29.633 60.911 1.00 23.55 ? 72 LYS A N 1 ATOM 148 C CA . LYS A 1 31 ? 19.364 28.680 60.808 1.00 23.68 ? 72 LYS A CA 1 ATOM 149 C C . LYS A 1 31 ? 18.240 29.195 59.899 1.00 22.54 ? 72 LYS A C 1 ATOM 150 O O . LYS A 1 31 ? 17.730 28.462 59.054 1.00 21.00 ? 72 LYS A O 1 ATOM 151 C CB . LYS A 1 31 ? 18.803 28.354 62.193 1.00 24.96 ? 72 LYS A CB 1 ATOM 152 C CG . LYS A 1 31 ? 19.747 27.449 62.972 1.00 31.01 ? 72 LYS A CG 1 ATOM 153 C CD . LYS A 1 31 ? 19.347 27.391 64.444 1.00 37.86 ? 72 LYS A CD 1 ATOM 154 C CE . LYS A 1 31 ? 20.383 26.554 65.238 1.00 43.41 ? 72 LYS A CE 1 ATOM 155 N NZ . LYS A 1 31 ? 20.171 26.730 66.714 1.00 47.65 ? 72 LYS A NZ 1 ATOM 156 N N . PHE A 1 32 ? 17.899 30.480 60.035 1.00 21.15 ? 73 PHE A N 1 ATOM 157 C CA . PHE A 1 32 ? 16.826 31.018 59.195 1.00 21.02 ? 73 PHE A CA 1 ATOM 158 C C . PHE A 1 32 ? 17.271 31.077 57.731 1.00 20.15 ? 73 PHE A C 1 ATOM 159 O O . PHE A 1 32 ? 16.517 30.752 56.795 1.00 21.32 ? 73 PHE A O 1 ATOM 160 C CB . PHE A 1 32 ? 16.445 32.415 59.708 1.00 21.95 ? 73 PHE A CB 1 ATOM 161 C CG . PHE A 1 32 ? 15.884 32.421 61.103 1.00 21.38 ? 73 PHE A CG 1 ATOM 162 C CD1 . PHE A 1 32 ? 15.164 31.319 61.585 1.00 21.81 ? 73 PHE A CD1 1 ATOM 163 C CD2 . PHE A 1 32 ? 15.983 33.572 61.932 1.00 18.76 ? 73 PHE A CD2 1 ATOM 164 C CE1 . PHE A 1 32 ? 14.620 31.338 62.899 1.00 22.50 ? 73 PHE A CE1 1 ATOM 165 C CE2 . PHE A 1 32 ? 15.442 33.589 63.226 1.00 21.90 ? 73 PHE A CE2 1 ATOM 166 C CZ . PHE A 1 32 ? 14.742 32.497 63.700 1.00 25.44 ? 73 PHE A CZ 1 ATOM 167 N N . LEU A 1 33 ? 18.524 31.465 57.513 1.00 18.61 ? 74 LEU A N 1 ATOM 168 C CA . LEU A 1 33 ? 19.016 31.539 56.141 1.00 17.92 ? 74 LEU A CA 1 ATOM 169 C C . LEU A 1 33 ? 18.966 30.172 55.473 1.00 18.76 ? 74 LEU A C 1 ATOM 170 O O . LEU A 1 33 ? 18.461 30.056 54.358 1.00 19.71 ? 74 LEU A O 1 ATOM 171 C CB . LEU A 1 33 ? 20.428 32.085 56.099 1.00 18.48 ? 74 LEU A CB 1 ATOM 172 C CG . LEU A 1 33 ? 20.914 32.257 54.646 1.00 18.62 ? 74 LEU A CG 1 ATOM 173 C CD1 . LEU A 1 33 ? 20.084 33.292 53.766 1.00 18.84 ? 74 LEU A CD1 1 ATOM 174 C CD2 . LEU A 1 33 ? 22.384 32.595 54.606 1.00 21.06 ? 74 LEU A CD2 1 ATOM 175 N N . TYR A 1 34 ? 19.486 29.142 56.161 1.00 19.27 ? 75 TYR A N 1 ATOM 176 C CA . TYR A 1 34 ? 19.368 27.807 55.619 1.00 19.89 ? 75 TYR A CA 1 ATOM 177 C C . TYR A 1 34 ? 17.889 27.456 55.306 1.00 20.20 ? 75 TYR A C 1 ATOM 178 O O . TYR A 1 34 ? 17.602 26.941 54.237 1.00 21.65 ? 75 TYR A O 1 ATOM 179 C CB . TYR A 1 34 ? 19.925 26.796 56.630 1.00 20.85 ? 75 TYR A CB 1 ATOM 180 C CG . TYR A 1 34 ? 19.867 25.400 56.100 1.00 20.45 ? 75 TYR A CG 1 ATOM 181 C CD1 . TYR A 1 34 ? 20.904 24.924 55.296 1.00 21.96 ? 75 TYR A CD1 1 ATOM 182 C CD2 . TYR A 1 34 ? 18.791 24.562 56.400 1.00 26.84 ? 75 TYR A CD2 1 ATOM 183 C CE1 . TYR A 1 34 ? 20.883 23.640 54.795 1.00 24.03 ? 75 TYR A CE1 1 ATOM 184 C CE2 . TYR A 1 34 ? 18.762 23.235 55.891 1.00 27.22 ? 75 TYR A CE2 1 ATOM 185 C CZ . TYR A 1 34 ? 19.810 22.824 55.084 1.00 27.02 ? 75 TYR A CZ 1 ATOM 186 O OH . TYR A 1 34 ? 19.827 21.537 54.566 1.00 33.26 ? 75 TYR A OH 1 ATOM 187 N N . ASN A 1 35 ? 16.966 27.762 56.218 1.00 19.35 ? 76 ASN A N 1 ATOM 188 C CA . ASN A 1 35 ? 15.565 27.429 56.083 1.00 20.50 ? 76 ASN A CA 1 ATOM 189 C C . ASN A 1 35 ? 14.924 28.110 54.868 1.00 20.26 ? 76 ASN A C 1 ATOM 190 O O . ASN A 1 35 ? 14.008 27.535 54.236 1.00 20.59 ? 76 ASN A O 1 ATOM 191 C CB . ASN A 1 35 ? 14.835 27.866 57.327 1.00 20.92 ? 76 ASN A CB 1 ATOM 192 C CG . ASN A 1 35 ? 13.363 27.508 57.295 1.00 23.38 ? 76 ASN A CG 1 ATOM 193 O OD1 . ASN A 1 35 ? 12.521 28.325 56.895 1.00 23.37 ? 76 ASN A OD1 1 ATOM 194 N ND2 . ASN A 1 35 ? 13.036 26.261 57.696 1.00 24.03 ? 76 ASN A ND2 1 ATOM 195 N N . PHE A 1 36 ? 15.411 29.314 54.543 1.00 19.01 ? 77 PHE A N 1 ATOM 196 C CA . PHE A 1 36 ? 14.773 30.112 53.484 1.00 18.48 ? 77 PHE A CA 1 ATOM 197 C C . PHE A 1 36 ? 15.333 29.853 52.092 1.00 19.43 ? 77 PHE A C 1 ATOM 198 O O . PHE A 1 36 ? 14.833 30.435 51.104 1.00 17.58 ? 77 PHE A O 1 ATOM 199 C CB . PHE A 1 36 ? 14.934 31.630 53.767 1.00 18.98 ? 77 PHE A CB 1 ATOM 200 C CG . PHE A 1 36 ? 14.251 32.147 55.009 1.00 19.55 ? 77 PHE A CG 1 ATOM 201 C CD1 . PHE A 1 36 ? 13.280 31.425 55.705 1.00 19.68 ? 77 PHE A CD1 1 ATOM 202 C CD2 . PHE A 1 36 ? 14.533 33.464 55.427 1.00 18.50 ? 77 PHE A CD2 1 ATOM 203 C CE1 . PHE A 1 36 ? 12.623 31.964 56.838 1.00 19.98 ? 77 PHE A CE1 1 ATOM 204 C CE2 . PHE A 1 36 ? 13.880 34.021 56.570 1.00 18.66 ? 77 PHE A CE2 1 ATOM 205 C CZ . PHE A 1 36 ? 12.928 33.269 57.264 1.00 21.06 ? 77 PHE A CZ 1 ATOM 206 N N . THR A 1 37 ? 16.370 28.989 51.975 1.00 18.95 ? 78 THR A N 1 ATOM 207 C CA . THR A 1 37 ? 17.076 28.937 50.719 1.00 19.88 ? 78 THR A CA 1 ATOM 208 C C . THR A 1 37 ? 17.213 27.516 50.144 1.00 20.08 ? 78 THR A C 1 ATOM 209 O O . THR A 1 37 ? 18.042 27.302 49.259 1.00 21.39 ? 78 THR A O 1 ATOM 210 C CB . THR A 1 37 ? 18.524 29.466 50.900 1.00 20.01 ? 78 THR A CB 1 ATOM 211 O OG1 . THR A 1 37 ? 19.135 28.758 51.984 1.00 19.82 ? 78 THR A OG1 1 ATOM 212 C CG2 . THR A 1 37 ? 18.508 30.973 51.227 1.00 18.76 ? 78 THR A CG2 1 ATOM 213 N N . GLN A 1 38 ? 16.387 26.586 50.623 1.00 21.20 ? 79 GLN A N 1 ATOM 214 C CA . GLN A 1 38 ? 16.489 25.180 50.147 1.00 22.95 ? 79 GLN A CA 1 ATOM 215 C C . GLN A 1 38 ? 15.765 24.948 48.832 1.00 23.75 ? 79 GLN A C 1 ATOM 216 O O . GLN A 1 38 ? 16.062 23.987 48.121 1.00 24.34 ? 79 GLN A O 1 ATOM 217 C CB . GLN A 1 38 ? 15.953 24.208 51.210 1.00 23.06 ? 79 GLN A CB 1 ATOM 218 C CG . GLN A 1 38 ? 16.746 24.283 52.519 1.00 24.96 ? 79 GLN A CG 1 ATOM 219 C CD . GLN A 1 38 ? 18.229 24.120 52.231 1.00 28.02 ? 79 GLN A CD 1 ATOM 220 O OE1 . GLN A 1 38 ? 18.646 23.059 51.732 1.00 34.09 ? 79 GLN A OE1 1 ATOM 221 N NE2 . GLN A 1 38 ? 19.023 25.182 52.444 1.00 28.24 ? 79 GLN A NE2 1 ATOM 222 N N . ILE A 1 39 ? 14.766 25.789 48.547 1.00 23.23 ? 80 ILE A N 1 ATOM 223 C CA . ILE A 1 39 ? 14.028 25.677 47.301 1.00 22.79 ? 80 ILE A CA 1 ATOM 224 C C . ILE A 1 39 ? 13.861 27.097 46.729 1.00 22.07 ? 80 ILE A C 1 ATOM 225 O O . ILE A 1 39 ? 14.000 28.068 47.478 1.00 19.55 ? 80 ILE A O 1 ATOM 226 C CB . ILE A 1 39 ? 12.632 25.035 47.499 1.00 23.60 ? 80 ILE A CB 1 ATOM 227 C CG1 . ILE A 1 39 ? 11.754 25.869 48.413 1.00 25.10 ? 80 ILE A CG1 1 ATOM 228 C CG2 . ILE A 1 39 ? 12.752 23.589 48.050 1.00 26.08 ? 80 ILE A CG2 1 ATOM 229 C CD1 . ILE A 1 39 ? 10.302 25.424 48.476 1.00 27.38 ? 80 ILE A CD1 1 ATOM 230 N N . PRO A 1 40 ? 13.559 27.212 45.423 1.00 21.08 ? 81 PRO A N 1 ATOM 231 C CA . PRO A 1 40 ? 13.344 28.558 44.881 1.00 19.95 ? 81 PRO A CA 1 ATOM 232 C C . PRO A 1 40 ? 12.053 29.170 45.417 1.00 19.35 ? 81 PRO A C 1 ATOM 233 O O . PRO A 1 40 ? 11.064 28.465 45.748 1.00 20.32 ? 81 PRO A O 1 ATOM 234 C CB . PRO A 1 40 ? 13.197 28.312 43.377 1.00 21.06 ? 81 PRO A CB 1 ATOM 235 C CG . PRO A 1 40 ? 13.897 26.937 43.138 1.00 21.52 ? 81 PRO A CG 1 ATOM 236 C CD . PRO A 1 40 ? 13.509 26.175 44.377 1.00 21.39 ? 81 PRO A CD 1 ATOM 237 N N . HIS A 1 41 ? 12.064 30.504 45.531 1.00 17.46 ? 82 HIS A N 1 ATOM 238 C CA . HIS A 1 41 ? 10.873 31.235 45.975 1.00 16.72 ? 82 HIS A CA 1 ATOM 239 C C . HIS A 1 41 ? 10.500 32.352 44.999 1.00 16.52 ? 82 HIS A C 1 ATOM 240 O O . HIS A 1 41 ? 10.413 33.535 45.389 1.00 17.07 ? 82 HIS A O 1 ATOM 241 C CB . HIS A 1 41 ? 11.056 31.795 47.425 1.00 18.46 ? 82 HIS A CB 1 ATOM 242 C CG . HIS A 1 41 ? 11.216 30.711 48.439 1.00 17.08 ? 82 HIS A CG 1 ATOM 243 N ND1 . HIS A 1 41 ? 12.446 30.360 48.962 1.00 18.69 ? 82 HIS A ND1 1 ATOM 244 C CD2 . HIS A 1 41 ? 10.316 29.830 48.947 1.00 19.26 ? 82 HIS A CD2 1 ATOM 245 C CE1 . HIS A 1 41 ? 12.281 29.344 49.805 1.00 20.47 ? 82 HIS A CE1 1 ATOM 246 N NE2 . HIS A 1 41 ? 11.000 29.000 49.812 1.00 20.71 ? 82 HIS A NE2 1 ATOM 247 N N . LEU A 1 42 ? 10.333 31.978 43.735 1.00 16.50 ? 83 LEU A N 1 ATOM 248 C CA . LEU A 1 42 ? 10.010 32.966 42.686 1.00 16.51 ? 83 LEU A CA 1 ATOM 249 C C . LEU A 1 42 ? 8.651 33.622 42.942 1.00 16.90 ? 83 LEU A C 1 ATOM 250 O O . LEU A 1 42 ? 7.700 32.952 43.321 1.00 17.54 ? 83 LEU A O 1 ATOM 251 C CB . LEU A 1 42 ? 9.997 32.271 41.309 1.00 16.95 ? 83 LEU A CB 1 ATOM 252 C CG . LEU A 1 42 ? 9.870 33.197 40.100 1.00 16.39 ? 83 LEU A CG 1 ATOM 253 C CD1 . LEU A 1 42 ? 11.059 34.100 39.910 1.00 18.79 ? 83 LEU A CD1 1 ATOM 254 C CD2 . LEU A 1 42 ? 9.785 32.228 38.780 1.00 16.63 ? 83 LEU A CD2 1 ATOM 255 N N . ALA A 1 43 ? 8.563 34.952 42.784 1.00 15.58 ? 84 ALA A N 1 ATOM 256 C CA . ALA A 1 43 ? 7.285 35.617 42.973 1.00 15.18 ? 84 ALA A CA 1 ATOM 257 C C . ALA A 1 43 ? 6.186 34.984 42.142 1.00 16.33 ? 84 ALA A C 1 ATOM 258 O O . ALA A 1 43 ? 6.425 34.641 40.955 1.00 15.85 ? 84 ALA A O 1 ATOM 259 C CB . ALA A 1 43 ? 7.423 37.074 42.589 1.00 16.33 ? 84 ALA A CB 1 ATOM 260 N N . GLY A 1 44 ? 5.002 34.839 42.758 1.00 16.59 ? 85 GLY A N 1 ATOM 261 C CA . GLY A 1 44 ? 3.811 34.337 42.089 1.00 18.96 ? 85 GLY A CA 1 ATOM 262 C C . GLY A 1 44 ? 3.751 32.828 42.089 1.00 20.54 ? 85 GLY A C 1 ATOM 263 O O . GLY A 1 44 ? 2.754 32.267 41.596 1.00 22.48 ? 85 GLY A O 1 ATOM 264 N N . THR A 1 45 ? 4.778 32.150 42.603 1.00 18.90 ? 86 THR A N 1 ATOM 265 C CA . THR A 1 45 ? 4.724 30.676 42.641 1.00 18.80 ? 86 THR A CA 1 ATOM 266 C C . THR A 1 45 ? 4.200 30.119 43.970 1.00 19.85 ? 86 THR A C 1 ATOM 267 O O . THR A 1 45 ? 4.232 30.755 45.014 1.00 19.44 ? 86 THR A O 1 ATOM 268 C CB . THR A 1 45 ? 6.125 30.054 42.370 1.00 18.98 ? 86 THR A CB 1 ATOM 269 O OG1 . THR A 1 45 ? 7.008 30.365 43.462 1.00 19.40 ? 86 THR A OG1 1 ATOM 270 C CG2 . THR A 1 45 ? 6.713 30.512 41.025 1.00 18.34 ? 86 THR A CG2 1 ATOM 271 N N . GLU A 1 46 ? 3.741 28.859 43.952 1.00 20.44 ? 87 GLU A N 1 ATOM 272 C CA . GLU A 1 46 ? 3.186 28.264 45.164 1.00 22.21 ? 87 GLU A CA 1 ATOM 273 C C . GLU A 1 46 ? 4.199 28.224 46.311 1.00 21.44 ? 87 GLU A C 1 ATOM 274 O O . GLU A 1 46 ? 3.813 28.419 47.497 1.00 22.82 ? 87 GLU A O 1 ATOM 275 C CB . GLU A 1 46 ? 2.717 26.839 44.836 1.00 24.39 ? 87 GLU A CB 1 ATOM 276 C CG . GLU A 1 46 ? 2.235 26.095 46.088 1.00 30.70 ? 87 GLU A CG 1 ATOM 277 C CD . GLU A 1 46 ? 0.943 26.660 46.700 1.00 38.32 ? 87 GLU A CD 1 ATOM 278 O OE1 . GLU A 1 46 ? 0.649 26.308 47.869 1.00 43.95 ? 87 GLU A OE1 1 ATOM 279 O OE2 . GLU A 1 46 ? 0.221 27.453 46.040 1.00 41.60 ? 87 GLU A OE2 1 ATOM 280 N N . GLN A 1 47 ? 5.468 27.941 45.967 1.00 22.01 ? 88 GLN A N 1 ATOM 281 C CA . GLN A 1 47 ? 6.559 27.855 46.951 1.00 21.67 ? 88 GLN A CA 1 ATOM 282 C C . GLN A 1 47 ? 6.714 29.175 47.700 1.00 20.50 ? 88 GLN A C 1 ATOM 283 O O . GLN A 1 47 ? 6.924 29.173 48.919 1.00 20.48 ? 88 GLN A O 1 ATOM 284 C CB . GLN A 1 47 ? 7.884 27.494 46.291 1.00 23.46 ? 88 GLN A CB 1 ATOM 285 C CG . GLN A 1 47 ? 7.849 26.099 45.640 1.00 25.81 ? 88 GLN A CG 1 ATOM 286 C CD . GLN A 1 47 ? 7.606 26.203 44.125 1.00 34.89 ? 88 GLN A CD 1 ATOM 287 O OE1 . GLN A 1 47 ? 6.635 26.831 43.666 1.00 29.73 ? 88 GLN A OE1 1 ATOM 288 N NE2 . GLN A 1 47 ? 8.507 25.585 43.336 1.00 38.78 ? 88 GLN A NE2 1 ATOM 289 N N . ASN A 1 48 ? 6.519 30.300 46.991 1.00 19.35 ? 89 ASN A N 1 ATOM 290 C CA . ASN A 1 48 ? 6.658 31.585 47.670 1.00 19.42 ? 89 ASN A CA 1 ATOM 291 C C . ASN A 1 48 ? 5.445 31.929 48.542 1.00 21.41 ? 89 ASN A C 1 ATOM 292 O O . ASN A 1 48 ? 5.573 32.650 49.544 1.00 21.79 ? 89 ASN A O 1 ATOM 293 C CB . ASN A 1 48 ? 6.918 32.729 46.684 1.00 20.10 ? 89 ASN A CB 1 ATOM 294 C CG . ASN A 1 48 ? 7.569 33.948 47.378 1.00 22.35 ? 89 ASN A CG 1 ATOM 295 O OD1 . ASN A 1 48 ? 8.339 33.801 48.348 1.00 20.58 ? 89 ASN A OD1 1 ATOM 296 N ND2 . ASN A 1 48 ? 7.263 35.133 46.888 1.00 20.94 ? 89 ASN A ND2 1 ATOM 297 N N . PHE A 1 49 ? 4.264 31.429 48.169 1.00 19.71 ? 90 PHE A N 1 ATOM 298 C CA . PHE A 1 49 ? 3.068 31.594 48.987 1.00 20.25 ? 90 PHE A CA 1 ATOM 299 C C . PHE A 1 49 ? 3.233 30.736 50.253 1.00 20.63 ? 90 PHE A C 1 ATOM 300 O O . PHE A 1 49 ? 2.967 31.188 51.372 1.00 20.62 ? 90 PHE A O 1 ATOM 301 C CB A PHE A 1 49 ? 1.848 31.132 48.178 0.65 21.20 ? 90 PHE A CB 1 ATOM 302 C CB B PHE A 1 49 ? 1.806 31.209 48.222 0.35 20.21 ? 90 PHE A CB 1 ATOM 303 C CG A PHE A 1 49 ? 0.532 31.198 48.916 0.65 21.48 ? 90 PHE A CG 1 ATOM 304 C CG B PHE A 1 49 ? 0.601 31.037 49.096 0.35 18.31 ? 90 PHE A CG 1 ATOM 305 C CD1 A PHE A 1 49 ? 0.262 32.196 49.845 0.65 21.71 ? 90 PHE A CD1 1 ATOM 306 C CD1 B PHE A 1 49 ? -0.094 32.132 49.573 0.35 16.85 ? 90 PHE A CD1 1 ATOM 307 C CD2 A PHE A 1 49 ? -0.468 30.261 48.607 0.65 24.84 ? 90 PHE A CD2 1 ATOM 308 C CD2 B PHE A 1 49 ? 0.158 29.761 49.416 0.35 18.79 ? 90 PHE A CD2 1 ATOM 309 C CE1 A PHE A 1 49 ? -0.992 32.262 50.495 0.65 24.54 ? 90 PHE A CE1 1 ATOM 310 C CE1 B PHE A 1 49 ? -1.220 31.975 50.368 0.35 16.68 ? 90 PHE A CE1 1 ATOM 311 C CE2 A PHE A 1 49 ? -1.703 30.300 49.249 0.65 26.79 ? 90 PHE A CE2 1 ATOM 312 C CE2 B PHE A 1 49 ? -0.942 29.582 50.197 0.35 15.60 ? 90 PHE A CE2 1 ATOM 313 C CZ A PHE A 1 49 ? -1.966 31.305 50.197 0.65 27.66 ? 90 PHE A CZ 1 ATOM 314 C CZ B PHE A 1 49 ? -1.647 30.688 50.689 0.35 15.98 ? 90 PHE A CZ 1 ATOM 315 N N . GLN A 1 50 ? 3.741 29.503 50.086 1.00 21.19 ? 91 GLN A N 1 ATOM 316 C CA . GLN A 1 50 ? 3.969 28.699 51.300 1.00 22.80 ? 91 GLN A CA 1 ATOM 317 C C . GLN A 1 50 ? 4.956 29.352 52.265 1.00 21.45 ? 91 GLN A C 1 ATOM 318 O O . GLN A 1 50 ? 4.748 29.369 53.484 1.00 21.28 ? 91 GLN A O 1 ATOM 319 C CB . GLN A 1 50 ? 4.403 27.260 50.954 1.00 24.45 ? 91 GLN A CB 1 ATOM 320 C CG . GLN A 1 50 ? 3.259 26.499 50.262 1.00 29.00 ? 91 GLN A CG 1 ATOM 321 C CD . GLN A 1 50 ? 2.021 26.315 51.178 1.00 38.78 ? 91 GLN A CD 1 ATOM 322 O OE1 . GLN A 1 50 ? 2.135 26.126 52.416 1.00 41.16 ? 91 GLN A OE1 1 ATOM 323 N NE2 . GLN A 1 50 ? 0.830 26.378 50.571 1.00 41.82 ? 91 GLN A NE2 1 ATOM 324 N N . LEU A 1 51 ? 6.031 29.936 51.719 1.00 20.54 ? 92 LEU A N 1 ATOM 325 C CA . LEU A 1 51 ? 6.990 30.626 52.586 1.00 19.79 ? 92 LEU A CA 1 ATOM 326 C C . LEU A 1 51 ? 6.297 31.833 53.257 1.00 19.74 ? 92 LEU A C 1 ATOM 327 O O . LEU A 1 51 ? 6.519 32.084 54.463 1.00 19.98 ? 92 LEU A O 1 ATOM 328 C CB . LEU A 1 51 ? 8.234 31.080 51.833 1.00 19.84 ? 92 LEU A CB 1 ATOM 329 C CG . LEU A 1 51 ? 9.309 31.699 52.711 1.00 19.83 ? 92 LEU A CG 1 ATOM 330 C CD1 . LEU A 1 51 ? 9.771 30.732 53.850 1.00 20.78 ? 92 LEU A CD1 1 ATOM 331 C CD2 . LEU A 1 51 ? 10.529 32.133 51.866 1.00 20.43 ? 92 LEU A CD2 1 ATOM 332 N N . ALA A 1 52 ? 5.491 32.594 52.505 1.00 18.02 ? 93 ALA A N 1 ATOM 333 C CA . ALA A 1 52 ? 4.703 33.672 53.156 1.00 18.89 ? 93 ALA A CA 1 ATOM 334 C C . ALA A 1 52 ? 3.909 33.203 54.382 1.00 19.67 ? 93 ALA A C 1 ATOM 335 O O . ALA A 1 52 ? 3.936 33.832 55.445 1.00 19.74 ? 93 ALA A O 1 ATOM 336 C CB . ALA A 1 52 ? 3.746 34.322 52.170 1.00 19.03 ? 93 ALA A CB 1 ATOM 337 N N . LYS A 1 53 ? 3.220 32.079 54.223 1.00 20.91 ? 94 LYS A N 1 ATOM 338 C CA . LYS A 1 53 ? 2.420 31.524 55.324 1.00 21.23 ? 94 LYS A CA 1 ATOM 339 C C . LYS A 1 53 ? 3.300 31.082 56.491 1.00 20.60 ? 94 LYS A C 1 ATOM 340 O O . LYS A 1 53 ? 2.907 31.258 57.677 1.00 21.33 ? 94 LYS A O 1 ATOM 341 C CB . LYS A 1 53 ? 1.578 30.373 54.776 1.00 22.35 ? 94 LYS A CB 1 ATOM 342 C CG . LYS A 1 53 ? 0.495 30.893 53.838 1.00 26.99 ? 94 LYS A CG 1 ATOM 343 C CD . LYS A 1 53 ? -0.563 29.847 53.606 1.00 37.80 ? 94 LYS A CD 1 ATOM 344 C CE . LYS A 1 53 ? 0.025 28.719 52.794 1.00 42.78 ? 94 LYS A CE 1 ATOM 345 N NZ . LYS A 1 53 ? -1.028 27.843 52.213 1.00 48.17 ? 94 LYS A NZ 1 ATOM 346 N N . GLN A 1 54 ? 4.467 30.502 56.173 1.00 21.73 ? 95 GLN A N 1 ATOM 347 C CA . GLN A 1 54 ? 5.390 30.136 57.229 1.00 21.51 ? 95 GLN A CA 1 ATOM 348 C C . GLN A 1 54 ? 5.843 31.386 58.017 1.00 21.47 ? 95 GLN A C 1 ATOM 349 O O . GLN A 1 54 ? 5.854 31.391 59.258 1.00 21.24 ? 95 GLN A O 1 ATOM 350 C CB . GLN A 1 54 ? 6.602 29.452 56.609 1.00 21.55 ? 95 GLN A CB 1 ATOM 351 C CG . GLN A 1 54 ? 7.606 29.151 57.712 1.00 22.82 ? 95 GLN A CG 1 ATOM 352 C CD . GLN A 1 54 ? 8.953 28.773 57.175 1.00 23.23 ? 95 GLN A CD 1 ATOM 353 O OE1 . GLN A 1 54 ? 9.068 28.046 56.164 1.00 23.11 ? 95 GLN A OE1 1 ATOM 354 N NE2 . GLN A 1 54 ? 9.990 29.269 57.835 1.00 22.98 ? 95 GLN A NE2 1 ATOM 355 N N . ILE A 1 55 ? 6.232 32.447 57.307 1.00 20.88 ? 96 ILE A N 1 ATOM 356 C CA . ILE A 1 55 ? 6.715 33.657 57.991 1.00 20.40 ? 96 ILE A CA 1 ATOM 357 C C . ILE A 1 55 ? 5.579 34.254 58.831 1.00 19.89 ? 96 ILE A C 1 ATOM 358 O O . ILE A 1 55 ? 5.772 34.644 59.998 1.00 21.22 ? 96 ILE A O 1 ATOM 359 C CB . ILE A 1 55 ? 7.227 34.686 56.939 1.00 20.11 ? 96 ILE A CB 1 ATOM 360 C CG1 A ILE A 1 55 ? 8.389 34.118 56.128 0.65 22.25 ? 96 ILE A CG1 1 ATOM 361 C CG1 B ILE A 1 55 ? 8.546 34.146 56.373 0.35 20.66 ? 96 ILE A CG1 1 ATOM 362 C CG2 . ILE A 1 55 ? 7.558 36.034 57.585 1.00 22.19 ? 96 ILE A CG2 1 ATOM 363 C CD1 A ILE A 1 55 ? 9.591 33.887 56.896 0.65 22.68 ? 96 ILE A CD1 1 ATOM 364 C CD1 B ILE A 1 55 ? 8.980 34.758 55.065 0.35 20.39 ? 96 ILE A CD1 1 ATOM 365 N N . GLN A 1 56 ? 4.371 34.289 58.258 1.00 19.88 ? 97 GLN A N 1 ATOM 366 C CA . GLN A 1 56 ? 3.214 34.798 59.004 1.00 20.70 ? 97 GLN A CA 1 ATOM 367 C C . GLN A 1 56 ? 3.059 34.013 60.325 1.00 21.77 ? 97 GLN A C 1 ATOM 368 O O . GLN A 1 56 ? 2.923 34.597 61.389 1.00 23.17 ? 97 GLN A O 1 ATOM 369 C CB . GLN A 1 56 ? 1.961 34.664 58.145 1.00 20.72 ? 97 GLN A CB 1 ATOM 370 C CG . GLN A 1 56 ? 0.692 35.064 58.902 1.00 22.10 ? 97 GLN A CG 1 ATOM 371 C CD . GLN A 1 56 ? -0.571 34.862 58.094 1.00 23.45 ? 97 GLN A CD 1 ATOM 372 O OE1 . GLN A 1 56 ? -0.662 33.959 57.231 1.00 24.08 ? 97 GLN A OE1 1 ATOM 373 N NE2 . GLN A 1 56 ? -1.580 35.706 58.374 1.00 23.46 ? 97 GLN A NE2 1 ATOM 374 N N . SER A 1 57 ? 3.095 32.691 60.238 1.00 22.73 ? 98 SER A N 1 ATOM 375 C CA . SER A 1 57 ? 2.929 31.862 61.441 1.00 23.55 ? 98 SER A CA 1 ATOM 376 C C . SER A 1 57 ? 4.015 32.095 62.472 1.00 22.93 ? 98 SER A C 1 ATOM 377 O O . SER A 1 57 ? 3.722 32.198 63.687 1.00 23.19 ? 98 SER A O 1 ATOM 378 C CB . SER A 1 57 ? 2.927 30.396 61.055 1.00 23.99 ? 98 SER A CB 1 ATOM 379 O OG A SER A 1 57 ? 1.671 30.029 60.534 0.50 28.27 ? 98 SER A OG 1 ATOM 380 O OG B SER A 1 57 ? 2.748 29.606 62.214 0.50 22.43 ? 98 SER A OG 1 ATOM 381 N N . GLN A 1 58 ? 5.271 32.170 61.999 1.00 21.51 ? 99 GLN A N 1 ATOM 382 C CA . GLN A 1 58 ? 6.390 32.387 62.910 1.00 22.45 ? 99 GLN A CA 1 ATOM 383 C C . GLN A 1 58 ? 6.366 33.765 63.546 1.00 21.71 ? 99 GLN A C 1 ATOM 384 O O . GLN A 1 58 ? 6.644 33.913 64.737 1.00 22.96 ? 99 GLN A O 1 ATOM 385 C CB . GLN A 1 58 ? 7.699 32.107 62.226 1.00 21.85 ? 99 GLN A CB 1 ATOM 386 C CG . GLN A 1 58 ? 7.796 30.631 61.833 1.00 24.51 ? 99 GLN A CG 1 ATOM 387 C CD . GLN A 1 58 ? 9.148 30.294 61.255 1.00 28.80 ? 99 GLN A CD 1 ATOM 388 O OE1 . GLN A 1 58 ? 9.548 30.829 60.226 1.00 26.43 ? 99 GLN A OE1 1 ATOM 389 N NE2 . GLN A 1 58 ? 9.854 29.382 61.913 1.00 34.82 ? 99 GLN A NE2 1 ATOM 390 N N . TRP A 1 59 ? 6.068 34.816 62.773 1.00 21.00 ? 100 TRP A N 1 ATOM 391 C CA . TRP A 1 59 ? 5.969 36.129 63.389 1.00 20.96 ? 100 TRP A CA 1 ATOM 392 C C . TRP A 1 59 ? 4.880 36.203 64.449 1.00 21.78 ? 100 TRP A C 1 ATOM 393 O O . TRP A 1 59 ? 5.047 36.917 65.441 1.00 22.28 ? 100 TRP A O 1 ATOM 394 C CB . TRP A 1 59 ? 5.719 37.157 62.276 1.00 20.20 ? 100 TRP A CB 1 ATOM 395 C CG . TRP A 1 59 ? 6.940 37.454 61.497 1.00 17.94 ? 100 TRP A CG 1 ATOM 396 C CD1 . TRP A 1 59 ? 8.171 36.832 61.559 1.00 19.86 ? 100 TRP A CD1 1 ATOM 397 C CD2 . TRP A 1 59 ? 7.050 38.461 60.452 1.00 18.75 ? 100 TRP A CD2 1 ATOM 398 N NE1 . TRP A 1 59 ? 9.042 37.409 60.638 1.00 19.41 ? 100 TRP A NE1 1 ATOM 399 C CE2 . TRP A 1 59 ? 8.377 38.402 59.954 1.00 19.43 ? 100 TRP A CE2 1 ATOM 400 C CE3 . TRP A 1 59 ? 6.155 39.420 59.925 1.00 19.58 ? 100 TRP A CE3 1 ATOM 401 C CZ2 . TRP A 1 59 ? 8.843 39.253 58.935 1.00 20.01 ? 100 TRP A CZ2 1 ATOM 402 C CZ3 . TRP A 1 59 ? 6.614 40.259 58.893 1.00 17.48 ? 100 TRP A CZ3 1 ATOM 403 C CH2 . TRP A 1 59 ? 7.953 40.170 58.432 1.00 19.18 ? 100 TRP A CH2 1 ATOM 404 N N . LYS A 1 60 ? 3.779 35.464 64.252 1.00 22.56 ? 101 LYS A N 1 ATOM 405 C CA . LYS A 1 60 ? 2.760 35.368 65.312 1.00 25.71 ? 101 LYS A CA 1 ATOM 406 C C . LYS A 1 60 ? 3.361 34.680 66.542 1.00 25.84 ? 101 LYS A C 1 ATOM 407 O O . LYS A 1 60 ? 3.241 35.223 67.653 1.00 26.79 ? 101 LYS A O 1 ATOM 408 C CB . LYS A 1 60 ? 1.499 34.624 64.864 1.00 27.13 ? 101 LYS A CB 1 ATOM 409 C CG . LYS A 1 60 ? 0.784 35.306 63.765 1.00 29.75 ? 101 LYS A CG 1 ATOM 410 C CD . LYS A 1 60 ? -0.436 34.525 63.275 1.00 34.96 ? 101 LYS A CD 1 ATOM 411 C CE . LYS A 1 60 ? -1.321 35.464 62.431 1.00 36.74 ? 101 LYS A CE 1 ATOM 412 N NZ . LYS A 1 60 ? -2.714 35.017 62.383 1.00 43.58 ? 101 LYS A NZ 1 ATOM 413 N N . GLU A 1 61 ? 3.989 33.521 66.345 1.00 26.08 ? 102 GLU A N 1 ATOM 414 C CA A GLU A 1 61 ? 4.680 32.745 67.402 0.50 27.11 ? 102 GLU A CA 1 ATOM 415 C CA B GLU A 1 61 ? 4.570 32.820 67.488 0.50 27.06 ? 102 GLU A CA 1 ATOM 416 C C . GLU A 1 61 ? 5.645 33.670 68.156 1.00 27.34 ? 102 GLU A C 1 ATOM 417 O O . GLU A 1 61 ? 5.753 33.662 69.389 1.00 26.97 ? 102 GLU A O 1 ATOM 418 C CB A GLU A 1 61 ? 5.478 31.579 66.768 0.50 27.76 ? 102 GLU A CB 1 ATOM 419 C CB B GLU A 1 61 ? 5.104 31.448 67.100 0.50 27.33 ? 102 GLU A CB 1 ATOM 420 C CG A GLU A 1 61 ? 4.677 30.395 66.184 0.50 30.99 ? 102 GLU A CG 1 ATOM 421 C CG B GLU A 1 61 ? 6.004 30.814 68.175 0.50 31.77 ? 102 GLU A CG 1 ATOM 422 C CD A GLU A 1 61 ? 5.486 29.495 65.209 0.50 33.92 ? 102 GLU A CD 1 ATOM 423 C CD B GLU A 1 61 ? 6.964 29.780 67.604 0.50 38.24 ? 102 GLU A CD 1 ATOM 424 O OE1 A GLU A 1 61 ? 6.711 29.288 65.411 0.50 32.39 ? 102 GLU A OE1 1 ATOM 425 O OE1 B GLU A 1 61 ? 6.475 28.817 66.959 0.50 41.29 ? 102 GLU A OE1 1 ATOM 426 O OE2 A GLU A 1 61 ? 4.891 28.984 64.225 0.50 33.82 ? 102 GLU A OE2 1 ATOM 427 O OE2 B GLU A 1 61 ? 8.204 29.924 67.797 0.50 41.30 ? 102 GLU A OE2 1 ATOM 428 N N . PHE A 1 62 ? 6.383 34.470 67.382 1.00 24.99 ? 103 PHE A N 1 ATOM 429 C CA . PHE A 1 62 ? 7.417 35.342 67.964 1.00 24.37 ? 103 PHE A CA 1 ATOM 430 C C . PHE A 1 62 ? 6.851 36.438 68.859 1.00 24.61 ? 103 PHE A C 1 ATOM 431 O O . PHE A 1 62 ? 7.599 37.015 69.662 1.00 26.48 ? 103 PHE A O 1 ATOM 432 C CB . PHE A 1 62 ? 8.257 36.033 66.863 1.00 23.93 ? 103 PHE A CB 1 ATOM 433 C CG . PHE A 1 62 ? 9.185 35.086 66.087 1.00 23.01 ? 103 PHE A CG 1 ATOM 434 C CD1 . PHE A 1 62 ? 9.488 33.784 66.527 1.00 23.68 ? 103 PHE A CD1 1 ATOM 435 C CD2 . PHE A 1 62 ? 9.783 35.531 64.902 1.00 24.54 ? 103 PHE A CD2 1 ATOM 436 C CE1 . PHE A 1 62 ? 10.359 32.939 65.757 1.00 27.02 ? 103 PHE A CE1 1 ATOM 437 C CE2 . PHE A 1 62 ? 10.649 34.715 64.145 1.00 25.04 ? 103 PHE A CE2 1 ATOM 438 C CZ . PHE A 1 62 ? 10.938 33.411 64.551 1.00 26.46 ? 103 PHE A CZ 1 ATOM 439 N N . GLY A 1 63 ? 5.556 36.745 68.711 1.00 24.38 ? 104 GLY A N 1 ATOM 440 C CA . GLY A 1 63 ? 4.842 37.614 69.636 1.00 25.34 ? 104 GLY A CA 1 ATOM 441 C C . GLY A 1 63 ? 4.215 38.885 69.063 1.00 25.34 ? 104 GLY A C 1 ATOM 442 O O . GLY A 1 63 ? 3.702 39.708 69.834 1.00 26.90 ? 104 GLY A O 1 ATOM 443 N N . LEU A 1 64 ? 4.234 39.071 67.733 1.00 24.01 ? 105 LEU A N 1 ATOM 444 C CA . LEU A 1 64 ? 3.634 40.305 67.192 1.00 21.74 ? 105 LEU A CA 1 ATOM 445 C C . LEU A 1 64 ? 2.154 40.349 67.461 1.00 23.60 ? 105 LEU A C 1 ATOM 446 O O . LEU A 1 64 ? 1.502 39.286 67.576 1.00 25.61 ? 105 LEU A O 1 ATOM 447 C CB . LEU A 1 64 ? 3.892 40.407 65.666 1.00 21.15 ? 105 LEU A CB 1 ATOM 448 C CG . LEU A 1 64 ? 5.381 40.540 65.321 1.00 20.79 ? 105 LEU A CG 1 ATOM 449 C CD1 . LEU A 1 64 ? 5.517 40.909 63.816 1.00 21.77 ? 105 LEU A CD1 1 ATOM 450 C CD2 . LEU A 1 64 ? 6.186 41.559 66.152 1.00 22.41 ? 105 LEU A CD2 1 ATOM 451 N N . ASP A 1 65 ? 1.603 41.557 67.585 1.00 23.49 ? 106 ASP A N 1 ATOM 452 C CA . ASP A 1 65 ? 0.185 41.721 67.889 1.00 24.84 ? 106 ASP A CA 1 ATOM 453 C C . ASP A 1 65 ? -0.749 41.255 66.793 1.00 25.72 ? 106 ASP A C 1 ATOM 454 O O . ASP A 1 65 ? -1.791 40.676 67.088 1.00 27.05 ? 106 ASP A O 1 ATOM 455 C CB . ASP A 1 65 ? -0.105 43.181 68.205 1.00 24.83 ? 106 ASP A CB 1 ATOM 456 C CG . ASP A 1 65 ? 0.614 43.627 69.435 1.00 27.29 ? 106 ASP A CG 1 ATOM 457 O OD1 . ASP A 1 65 ? 0.385 43.023 70.531 1.00 27.05 ? 106 ASP A OD1 1 ATOM 458 O OD2 . ASP A 1 65 ? 1.437 44.541 69.314 1.00 24.67 ? 106 ASP A OD2 1 ATOM 459 N N . SER A 1 66 ? -0.399 41.533 65.535 1.00 24.26 ? 107 SER A N 1 ATOM 460 C CA . SER A 1 66 ? -1.144 40.991 64.391 1.00 24.46 ? 107 SER A CA 1 ATOM 461 C C . SER A 1 66 ? -0.180 40.723 63.251 1.00 22.71 ? 107 SER A C 1 ATOM 462 O O . SER A 1 66 ? 0.863 41.381 63.114 1.00 21.34 ? 107 SER A O 1 ATOM 463 C CB . SER A 1 66 ? -2.240 41.947 63.913 1.00 25.19 ? 107 SER A CB 1 ATOM 464 O OG A SER A 1 66 ? -1.765 43.268 63.884 0.50 25.38 ? 107 SER A OG 1 ATOM 465 O OG B SER A 1 66 ? -1.755 42.905 62.988 0.50 25.35 ? 107 SER A OG 1 ATOM 466 N N . VAL A 1 67 ? -0.514 39.727 62.445 1.00 21.28 ? 108 VAL A N 1 ATOM 467 C CA . VAL A 1 67 ? 0.315 39.447 61.280 1.00 21.46 ? 108 VAL A CA 1 ATOM 468 C C . VAL A 1 67 ? -0.652 39.001 60.209 1.00 22.57 ? 108 VAL A C 1 ATOM 469 O O . VAL A 1 67 ? -1.285 37.937 60.333 1.00 23.21 ? 108 VAL A O 1 ATOM 470 C CB . VAL A 1 67 ? 1.351 38.318 61.531 1.00 21.24 ? 108 VAL A CB 1 ATOM 471 C CG1 . VAL A 1 67 ? 2.348 38.266 60.332 1.00 20.31 ? 108 VAL A CG1 1 ATOM 472 C CG2 . VAL A 1 67 ? 2.120 38.586 62.853 1.00 20.86 ? 108 VAL A CG2 1 ATOM 473 N N . GLU A 1 68 ? -0.706 39.773 59.115 1.00 20.98 ? 109 GLU A N 1 ATOM 474 C CA . GLU A 1 68 ? -1.675 39.508 58.046 1.00 23.41 ? 109 GLU A CA 1 ATOM 475 C C . GLU A 1 68 ? -0.980 39.367 56.706 1.00 22.56 ? 109 GLU A C 1 ATOM 476 O O . GLU A 1 68 ? 0.135 39.856 56.558 1.00 23.03 ? 109 GLU A O 1 ATOM 477 C CB . GLU A 1 68 ? -2.663 40.672 57.927 1.00 25.03 ? 109 GLU A CB 1 ATOM 478 C CG . GLU A 1 68 ? -3.533 40.887 59.189 1.00 31.26 ? 109 GLU A CG 1 ATOM 479 C CD . GLU A 1 68 ? -4.341 39.643 59.602 1.00 41.06 ? 109 GLU A CD 1 ATOM 480 O OE1 . GLU A 1 68 ? -4.836 38.895 58.714 1.00 42.55 ? 109 GLU A OE1 1 ATOM 481 O OE2 . GLU A 1 68 ? -4.499 39.420 60.835 1.00 45.49 ? 109 GLU A OE2 1 ATOM 482 N N . LEU A 1 69 ? -1.600 38.671 55.756 1.00 20.72 ? 110 LEU A N 1 ATOM 483 C CA . LEU A 1 69 ? -1.133 38.716 54.373 1.00 21.08 ? 110 LEU A CA 1 ATOM 484 C C . LEU A 1 69 ? -1.916 39.782 53.634 1.00 20.63 ? 110 LEU A C 1 ATOM 485 O O . LEU A 1 69 ? -3.149 39.889 53.787 1.00 23.00 ? 110 LEU A O 1 ATOM 486 C CB . LEU A 1 69 ? -1.377 37.377 53.671 1.00 21.77 ? 110 LEU A CB 1 ATOM 487 C CG . LEU A 1 69 ? -0.672 36.161 54.277 1.00 23.95 ? 110 LEU A CG 1 ATOM 488 C CD1 . LEU A 1 69 ? -0.896 34.975 53.339 1.00 27.60 ? 110 LEU A CD1 1 ATOM 489 C CD2 . LEU A 1 69 ? 0.801 36.407 54.414 1.00 23.58 ? 110 LEU A CD2 1 ATOM 490 N N . ALA A 1 70 ? -1.220 40.585 52.838 1.00 18.77 ? 111 ALA A N 1 ATOM 491 C CA . ALA A 1 70 ? -1.850 41.590 51.996 1.00 18.29 ? 111 ALA A CA 1 ATOM 492 C C . ALA A 1 70 ? -1.519 41.114 50.598 1.00 17.61 ? 111 ALA A C 1 ATOM 493 O O . ALA A 1 70 ? -0.326 41.061 50.233 1.00 19.05 ? 111 ALA A O 1 ATOM 494 C CB . ALA A 1 70 ? -1.227 42.981 52.244 1.00 18.09 ? 111 ALA A CB 1 ATOM 495 N N . HIS A 1 71 ? -2.538 40.772 49.803 1.00 16.81 ? 112 HIS A N 1 ATOM 496 C CA . HIS A 1 71 ? -2.264 40.227 48.469 1.00 16.43 ? 112 HIS A CA 1 ATOM 497 C C . HIS A 1 71 ? -2.770 41.210 47.413 1.00 16.07 ? 112 HIS A C 1 ATOM 498 O O . HIS A 1 71 ? -3.655 42.037 47.675 1.00 17.68 ? 112 HIS A O 1 ATOM 499 C CB . HIS A 1 71 ? -2.937 38.837 48.277 1.00 17.00 ? 112 HIS A CB 1 ATOM 500 C CG . HIS A 1 71 ? -4.446 38.894 48.298 1.00 20.42 ? 112 HIS A CG 1 ATOM 501 N ND1 . HIS A 1 71 ? -5.171 38.654 49.448 1.00 25.81 ? 112 HIS A ND1 1 ATOM 502 C CD2 . HIS A 1 71 ? -5.353 39.163 47.326 1.00 24.37 ? 112 HIS A CD2 1 ATOM 503 C CE1 . HIS A 1 71 ? -6.466 38.769 49.176 1.00 25.22 ? 112 HIS A CE1 1 ATOM 504 N NE2 . HIS A 1 71 ? -6.605 39.049 47.893 1.00 24.80 ? 112 HIS A NE2 1 ATOM 505 N N . TYR A 1 72 ? -2.222 41.067 46.198 1.00 16.28 ? 113 TYR A N 1 ATOM 506 C CA . TYR A 1 72 ? -2.487 41.929 45.051 1.00 15.46 ? 113 TYR A CA 1 ATOM 507 C C . TYR A 1 72 ? -2.339 41.047 43.840 1.00 15.88 ? 113 TYR A C 1 ATOM 508 O O . TYR A 1 72 ? -1.598 40.051 43.880 1.00 17.35 ? 113 TYR A O 1 ATOM 509 C CB . TYR A 1 72 ? -1.475 43.124 44.934 1.00 15.86 ? 113 TYR A CB 1 ATOM 510 C CG . TYR A 1 72 ? -1.471 43.934 46.205 1.00 15.26 ? 113 TYR A CG 1 ATOM 511 C CD1 . TYR A 1 72 ? -2.455 44.901 46.410 1.00 15.36 ? 113 TYR A CD1 1 ATOM 512 C CD2 . TYR A 1 72 ? -0.612 43.626 47.242 1.00 17.72 ? 113 TYR A CD2 1 ATOM 513 C CE1 . TYR A 1 72 ? -2.541 45.576 47.657 1.00 17.79 ? 113 TYR A CE1 1 ATOM 514 C CE2 . TYR A 1 72 ? -0.667 44.284 48.462 1.00 18.15 ? 113 TYR A CE2 1 ATOM 515 C CZ . TYR A 1 72 ? -1.626 45.247 48.658 1.00 18.75 ? 113 TYR A CZ 1 ATOM 516 O OH . TYR A 1 72 ? -1.669 45.867 49.895 1.00 18.91 ? 113 TYR A OH 1 ATOM 517 N N . ASP A 1 73 ? -2.962 41.448 42.739 1.00 16.05 ? 114 ASP A N 1 ATOM 518 C CA . ASP A 1 73 ? -2.848 40.693 41.472 1.00 16.92 ? 114 ASP A CA 1 ATOM 519 C C . ASP A 1 73 ? -2.189 41.632 40.487 1.00 17.04 ? 114 ASP A C 1 ATOM 520 O O . ASP A 1 73 ? -2.780 42.598 40.005 1.00 16.60 ? 114 ASP A O 1 ATOM 521 C CB . ASP A 1 73 ? -4.248 40.259 40.979 1.00 18.06 ? 114 ASP A CB 1 ATOM 522 C CG . ASP A 1 73 ? -4.908 39.310 41.934 1.00 21.44 ? 114 ASP A CG 1 ATOM 523 O OD1 . ASP A 1 73 ? -4.261 38.319 42.292 1.00 21.77 ? 114 ASP A OD1 1 ATOM 524 O OD2 . ASP A 1 73 ? -6.078 39.589 42.302 1.00 25.86 ? 114 ASP A OD2 1 ATOM 525 N N . VAL A 1 74 ? -0.912 41.326 40.239 1.00 16.42 ? 115 VAL A N 1 ATOM 526 C CA . VAL A 1 74 ? -0.036 42.228 39.468 1.00 16.07 ? 115 VAL A CA 1 ATOM 527 C C . VAL A 1 74 ? 0.552 41.563 38.233 1.00 16.64 ? 115 VAL A C 1 ATOM 528 O O . VAL A 1 74 ? 0.605 40.316 38.178 1.00 16.43 ? 115 VAL A O 1 ATOM 529 C CB . VAL A 1 74 ? 1.174 42.697 40.335 1.00 15.45 ? 115 VAL A CB 1 ATOM 530 C CG1 . VAL A 1 74 ? 0.664 43.428 41.605 1.00 15.45 ? 115 VAL A CG1 1 ATOM 531 C CG2 . VAL A 1 74 ? 2.136 41.524 40.734 1.00 16.46 ? 115 VAL A CG2 1 ATOM 532 N N . LEU A 1 75 ? 1.003 42.377 37.266 1.00 14.99 ? 116 LEU A N 1 ATOM 533 C CA . LEU A 1 75 ? 1.607 41.801 36.068 1.00 14.39 ? 116 LEU A CA 1 ATOM 534 C C . LEU A 1 75 ? 2.996 41.224 36.337 1.00 14.65 ? 116 LEU A C 1 ATOM 535 O O . LEU A 1 75 ? 3.910 41.950 36.761 1.00 15.93 ? 116 LEU A O 1 ATOM 536 C CB . LEU A 1 75 ? 1.663 42.832 34.946 1.00 14.29 ? 116 LEU A CB 1 ATOM 537 C CG . LEU A 1 75 ? 2.061 42.250 33.595 1.00 15.91 ? 116 LEU A CG 1 ATOM 538 C CD1 . LEU A 1 75 ? 0.830 41.537 32.985 1.00 17.51 ? 116 LEU A CD1 1 ATOM 539 C CD2 . LEU A 1 75 ? 2.467 43.389 32.665 1.00 17.61 ? 116 LEU A CD2 1 ATOM 540 N N . LEU A 1 76 ? 3.139 39.894 36.167 1.00 15.14 ? 117 LEU A N 1 ATOM 541 C CA . LEU A 1 76 ? 4.461 39.243 36.269 1.00 15.54 ? 117 LEU A CA 1 ATOM 542 C C . LEU A 1 76 ? 4.860 38.666 34.893 1.00 16.50 ? 117 LEU A C 1 ATOM 543 O O . LEU A 1 76 ? 4.134 38.873 33.890 1.00 17.79 ? 117 LEU A O 1 ATOM 544 C CB . LEU A 1 76 ? 4.527 38.156 37.356 1.00 16.37 ? 117 LEU A CB 1 ATOM 545 C CG . LEU A 1 76 ? 4.148 38.591 38.788 1.00 15.49 ? 117 LEU A CG 1 ATOM 546 C CD1 . LEU A 1 76 ? 4.348 37.479 39.812 1.00 16.86 ? 117 LEU A CD1 1 ATOM 547 C CD2 . LEU A 1 76 ? 5.022 39.796 39.214 1.00 16.80 ? 117 LEU A CD2 1 ATOM 548 N N . SER A 1 77 ? 6.051 38.040 34.819 1.00 16.60 ? 118 SER A N 1 ATOM 549 C CA . SER A 1 77 ? 6.527 37.574 33.495 1.00 17.91 ? 118 SER A CA 1 ATOM 550 C C . SER A 1 77 ? 7.288 36.280 33.717 1.00 18.38 ? 118 SER A C 1 ATOM 551 O O . SER A 1 77 ? 8.109 36.204 34.660 1.00 17.90 ? 118 SER A O 1 ATOM 552 C CB . SER A 1 77 ? 7.521 38.608 32.924 1.00 19.08 ? 118 SER A CB 1 ATOM 553 O OG . SER A 1 77 ? 8.278 38.082 31.820 1.00 19.61 ? 118 SER A OG 1 ATOM 554 N N . TYR A 1 78 ? 7.055 35.275 32.846 1.00 17.08 ? 119 TYR A N 1 ATOM 555 C CA . TYR A 1 78 ? 7.722 33.977 33.014 1.00 18.59 ? 119 TYR A CA 1 ATOM 556 C C . TYR A 1 78 ? 8.065 33.352 31.678 1.00 19.64 ? 119 TYR A C 1 ATOM 557 O O . TYR A 1 78 ? 7.349 33.545 30.716 1.00 20.43 ? 119 TYR A O 1 ATOM 558 C CB . TYR A 1 78 ? 6.784 33.009 33.678 1.00 18.12 ? 119 TYR A CB 1 ATOM 559 C CG . TYR A 1 78 ? 6.290 33.396 35.043 1.00 19.41 ? 119 TYR A CG 1 ATOM 560 C CD1 . TYR A 1 78 ? 7.138 33.326 36.158 1.00 19.16 ? 119 TYR A CD1 1 ATOM 561 C CD2 . TYR A 1 78 ? 4.933 33.775 35.223 1.00 19.71 ? 119 TYR A CD2 1 ATOM 562 C CE1 . TYR A 1 78 ? 6.643 33.646 37.456 1.00 17.99 ? 119 TYR A CE1 1 ATOM 563 C CE2 . TYR A 1 78 ? 4.443 34.080 36.501 1.00 21.46 ? 119 TYR A CE2 1 ATOM 564 C CZ . TYR A 1 78 ? 5.290 33.975 37.590 1.00 18.51 ? 119 TYR A CZ 1 ATOM 565 O OH . TYR A 1 78 ? 4.774 34.254 38.856 1.00 19.07 ? 119 TYR A OH 1 ATOM 566 N N . PRO A 1 79 ? 9.166 32.608 31.633 1.00 20.94 ? 120 PRO A N 1 ATOM 567 C CA . PRO A 1 79 ? 9.419 31.901 30.373 1.00 21.87 ? 120 PRO A CA 1 ATOM 568 C C . PRO A 1 79 ? 8.340 30.866 30.129 1.00 22.54 ? 120 PRO A C 1 ATOM 569 O O . PRO A 1 79 ? 7.642 30.433 31.057 1.00 23.00 ? 120 PRO A O 1 ATOM 570 C CB . PRO A 1 79 ? 10.778 31.199 30.616 1.00 22.79 ? 120 PRO A CB 1 ATOM 571 C CG . PRO A 1 79 ? 11.413 31.887 31.763 1.00 23.45 ? 120 PRO A CG 1 ATOM 572 C CD . PRO A 1 79 ? 10.253 32.426 32.610 1.00 21.28 ? 120 PRO A CD 1 ATOM 573 N N . ASN A 1 80 ? 8.239 30.428 28.868 1.00 23.27 ? 121 ASN A N 1 ATOM 574 C CA . ASN A 1 80 ? 7.305 29.344 28.529 1.00 26.24 ? 121 ASN A CA 1 ATOM 575 C C . ASN A 1 80 ? 8.055 28.024 28.694 1.00 27.31 ? 121 ASN A C 1 ATOM 576 O O . ASN A 1 80 ? 9.065 27.800 28.024 1.00 26.38 ? 121 ASN A O 1 ATOM 577 C CB . ASN A 1 80 ? 6.842 29.549 27.098 1.00 25.71 ? 121 ASN A CB 1 ATOM 578 C CG . ASN A 1 80 ? 5.862 28.486 26.671 1.00 30.58 ? 121 ASN A CG 1 ATOM 579 O OD1 . ASN A 1 80 ? 5.929 27.355 27.151 1.00 31.12 ? 121 ASN A OD1 1 ATOM 580 N ND2 . ASN A 1 80 ? 4.941 28.841 25.796 1.00 30.59 ? 121 ASN A ND2 1 ATOM 581 N N . LYS A 1 81 ? 7.588 27.197 29.634 1.00 29.75 ? 122 LYS A N 1 ATOM 582 C CA . LYS A 1 81 ? 8.270 25.940 29.987 1.00 32.57 ? 122 LYS A CA 1 ATOM 583 C C . LYS A 1 81 ? 8.441 24.993 28.815 1.00 33.59 ? 122 LYS A C 1 ATOM 584 O O . LYS A 1 81 ? 9.415 24.230 28.772 1.00 34.99 ? 122 LYS A O 1 ATOM 585 C CB . LYS A 1 81 ? 7.521 25.218 31.098 1.00 33.48 ? 122 LYS A CB 1 ATOM 586 C CG . LYS A 1 81 ? 7.821 25.749 32.470 1.00 37.79 ? 122 LYS A CG 1 ATOM 587 C CD . LYS A 1 81 ? 6.752 25.307 33.484 1.00 44.15 ? 122 LYS A CD 1 ATOM 588 C CE . LYS A 1 81 ? 6.651 26.293 34.666 1.00 47.87 ? 122 LYS A CE 1 ATOM 589 N NZ . LYS A 1 81 ? 5.667 25.815 35.715 1.00 51.55 ? 122 LYS A NZ 1 ATOM 590 N N . THR A 1 82 ? 7.527 25.055 27.856 1.00 33.89 ? 123 THR A N 1 ATOM 591 C CA . THR A 1 82 ? 7.608 24.141 26.713 1.00 34.58 ? 123 THR A CA 1 ATOM 592 C C . THR A 1 82 ? 8.053 24.805 25.398 1.00 34.74 ? 123 THR A C 1 ATOM 593 O O . THR A 1 82 ? 7.964 24.224 24.317 1.00 36.12 ? 123 THR A O 1 ATOM 594 C CB . THR A 1 82 ? 6.271 23.403 26.530 1.00 35.52 ? 123 THR A CB 1 ATOM 595 O OG1 . THR A 1 82 ? 5.255 24.358 26.220 1.00 37.21 ? 123 THR A OG1 1 ATOM 596 C CG2 . THR A 1 82 ? 5.880 22.676 27.814 1.00 36.41 ? 123 THR A CG2 1 ATOM 597 N N . HIS A 1 83 ? 8.561 26.025 25.483 1.00 33.20 ? 124 HIS A N 1 ATOM 598 C CA . HIS A 1 83 ? 9.034 26.729 24.330 1.00 32.43 ? 124 HIS A CA 1 ATOM 599 C C . HIS A 1 83 ? 10.181 27.655 24.769 1.00 31.34 ? 124 HIS A C 1 ATOM 600 O O . HIS A 1 83 ? 9.997 28.870 24.907 1.00 30.54 ? 124 HIS A O 1 ATOM 601 C CB . HIS A 1 83 ? 7.880 27.490 23.724 1.00 32.87 ? 124 HIS A CB 1 ATOM 602 C CG . HIS A 1 83 ? 8.144 27.995 22.345 1.00 37.58 ? 124 HIS A CG 1 ATOM 603 N ND1 . HIS A 1 83 ? 7.249 28.801 21.671 1.00 41.62 ? 124 HIS A ND1 1 ATOM 604 C CD2 . HIS A 1 83 ? 9.198 27.815 21.510 1.00 43.32 ? 124 HIS A CD2 1 ATOM 605 C CE1 . HIS A 1 83 ? 7.736 29.086 20.472 1.00 44.17 ? 124 HIS A CE1 1 ATOM 606 N NE2 . HIS A 1 83 ? 8.923 28.509 20.353 1.00 44.67 ? 124 HIS A NE2 1 ATOM 607 N N . PRO A 1 84 ? 11.363 27.077 25.002 1.00 30.64 ? 125 PRO A N 1 ATOM 608 C CA . PRO A 1 84 ? 12.501 27.752 25.664 1.00 29.89 ? 125 PRO A CA 1 ATOM 609 C C . PRO A 1 84 ? 13.066 28.936 24.913 1.00 28.98 ? 125 PRO A C 1 ATOM 610 O O . PRO A 1 84 ? 13.052 28.985 23.679 1.00 29.06 ? 125 PRO A O 1 ATOM 611 C CB . PRO A 1 84 ? 13.560 26.654 25.781 1.00 31.40 ? 125 PRO A CB 1 ATOM 612 C CG . PRO A 1 84 ? 12.812 25.362 25.572 1.00 31.62 ? 125 PRO A CG 1 ATOM 613 C CD . PRO A 1 84 ? 11.673 25.673 24.676 1.00 32.34 ? 125 PRO A CD 1 ATOM 614 N N . ASN A 1 85 ? 13.512 29.938 25.679 1.00 26.01 ? 126 ASN A N 1 ATOM 615 C CA . ASN A 1 85 ? 14.163 31.088 25.093 1.00 25.32 ? 126 ASN A CA 1 ATOM 616 C C . ASN A 1 85 ? 15.605 30.739 24.768 1.00 25.39 ? 126 ASN A C 1 ATOM 617 O O . ASN A 1 85 ? 16.249 30.049 25.560 1.00 25.70 ? 126 ASN A O 1 ATOM 618 C CB . ASN A 1 85 ? 14.165 32.243 26.138 1.00 24.01 ? 126 ASN A CB 1 ATOM 619 C CG . ASN A 1 85 ? 12.772 32.701 26.499 1.00 24.96 ? 126 ASN A CG 1 ATOM 620 O OD1 . ASN A 1 85 ? 11.882 32.664 25.669 1.00 22.44 ? 126 ASN A OD1 1 ATOM 621 N ND2 . ASN A 1 85 ? 12.565 33.113 27.775 1.00 20.74 ? 126 ASN A ND2 1 ATOM 622 N N . TYR A 1 86 ? 16.111 31.201 23.620 1.00 26.19 ? 127 TYR A N 1 ATOM 623 C CA . TYR A 1 86 ? 17.547 31.042 23.318 1.00 26.46 ? 127 TYR A CA 1 ATOM 624 C C . TYR A 1 86 ? 17.941 31.955 22.174 1.00 25.98 ? 127 TYR A C 1 ATOM 625 O O . TYR A 1 86 ? 17.083 32.571 21.526 1.00 26.38 ? 127 TYR A O 1 ATOM 626 C CB . TYR A 1 86 ? 17.914 29.564 22.997 1.00 27.98 ? 127 TYR A CB 1 ATOM 627 C CG . TYR A 1 86 ? 17.379 29.061 21.656 1.00 29.62 ? 127 TYR A CG 1 ATOM 628 C CD1 . TYR A 1 86 ? 18.236 28.816 20.584 1.00 33.71 ? 127 TYR A CD1 1 ATOM 629 C CD2 . TYR A 1 86 ? 16.020 28.807 21.473 1.00 31.01 ? 127 TYR A CD2 1 ATOM 630 C CE1 . TYR A 1 86 ? 17.763 28.351 19.380 1.00 32.28 ? 127 TYR A CE1 1 ATOM 631 C CE2 . TYR A 1 86 ? 15.533 28.332 20.248 1.00 32.89 ? 127 TYR A CE2 1 ATOM 632 C CZ . TYR A 1 86 ? 16.420 28.116 19.211 1.00 32.51 ? 127 TYR A CZ 1 ATOM 633 O OH . TYR A 1 86 ? 15.976 27.663 17.977 1.00 32.40 ? 127 TYR A OH 1 ATOM 634 N N . ILE A 1 87 ? 19.256 32.058 21.955 1.00 25.62 ? 128 ILE A N 1 ATOM 635 C CA . ILE A 1 87 ? 19.805 32.871 20.879 1.00 24.66 ? 128 ILE A CA 1 ATOM 636 C C . ILE A 1 87 ? 20.649 31.951 19.994 1.00 25.83 ? 128 ILE A C 1 ATOM 637 O O . ILE A 1 87 ? 21.330 31.044 20.502 1.00 25.79 ? 128 ILE A O 1 ATOM 638 C CB . ILE A 1 87 ? 20.696 33.979 21.437 1.00 25.04 ? 128 ILE A CB 1 ATOM 639 C CG1 . ILE A 1 87 ? 19.857 34.900 22.372 1.00 23.47 ? 128 ILE A CG1 1 ATOM 640 C CG2 . ILE A 1 87 ? 21.327 34.808 20.314 1.00 25.45 ? 128 ILE A CG2 1 ATOM 641 C CD1 . ILE A 1 87 ? 20.784 35.747 23.264 1.00 24.48 ? 128 ILE A CD1 1 ATOM 642 N N . SER A 1 88 ? 20.597 32.213 18.695 1.00 26.99 ? 129 SER A N 1 ATOM 643 C CA . SER A 1 88 ? 21.408 31.446 17.705 1.00 28.18 ? 129 SER A CA 1 ATOM 644 C C . SER A 1 88 ? 22.284 32.336 16.865 1.00 29.10 ? 129 SER A C 1 ATOM 645 O O . SER A 1 88 ? 21.986 33.526 16.658 1.00 28.29 ? 129 SER A O 1 ATOM 646 C CB . SER A 1 88 ? 20.498 30.680 16.753 1.00 27.75 ? 129 SER A CB 1 ATOM 647 O OG . SER A 1 88 ? 19.684 29.761 17.455 1.00 31.36 ? 129 SER A OG 1 ATOM 648 N N . ILE A 1 89 ? 23.354 31.735 16.317 1.00 30.32 ? 130 ILE A N 1 ATOM 649 C CA . ILE A 1 89 ? 23.966 32.296 15.120 1.00 31.34 ? 130 ILE A CA 1 ATOM 650 C C . ILE A 1 89 ? 23.411 31.406 14.007 1.00 32.67 ? 130 ILE A C 1 ATOM 651 O O . ILE A 1 89 ? 23.363 30.171 14.141 1.00 30.83 ? 130 ILE A O 1 ATOM 652 C CB . ILE A 1 89 ? 25.508 32.224 15.111 1.00 32.12 ? 130 ILE A CB 1 ATOM 653 C CG1 . ILE A 1 89 ? 26.124 33.146 16.174 1.00 30.68 ? 130 ILE A CG1 1 ATOM 654 C CG2 . ILE A 1 89 ? 26.045 32.566 13.700 1.00 30.87 ? 130 ILE A CG2 1 ATOM 655 C CD1 . ILE A 1 89 ? 27.649 32.987 16.334 1.00 32.05 ? 130 ILE A CD1 1 ATOM 656 N N . ILE A 1 90 ? 22.925 32.043 12.956 1.00 35.35 ? 131 ILE A N 1 ATOM 657 C CA . ILE A 1 90 ? 22.350 31.303 11.823 1.00 38.82 ? 131 ILE A CA 1 ATOM 658 C C . ILE A 1 90 ? 23.172 31.586 10.564 1.00 40.68 ? 131 ILE A C 1 ATOM 659 O O . ILE A 1 90 ? 23.711 32.684 10.394 1.00 40.40 ? 131 ILE A O 1 ATOM 660 C CB . ILE A 1 90 ? 20.873 31.692 11.585 1.00 39.01 ? 131 ILE A CB 1 ATOM 661 C CG1 . ILE A 1 90 ? 20.737 33.210 11.520 1.00 39.97 ? 131 ILE A CG1 1 ATOM 662 C CG2 . ILE A 1 90 ? 19.998 31.182 12.711 1.00 39.96 ? 131 ILE A CG2 1 ATOM 663 C CD1 . ILE A 1 90 ? 19.389 33.692 11.059 1.00 45.29 ? 131 ILE A CD1 1 ATOM 664 N N . ASN A 1 91 ? 23.287 30.589 9.687 1.00 42.83 ? 132 ASN A N 1 ATOM 665 C CA . ASN A 1 91 ? 23.937 30.825 8.392 1.00 45.26 ? 132 ASN A CA 1 ATOM 666 C C . ASN A 1 91 ? 22.960 31.255 7.311 1.00 47.44 ? 132 ASN A C 1 ATOM 667 O O . ASN A 1 91 ? 21.755 31.340 7.567 1.00 47.52 ? 132 ASN A O 1 ATOM 668 C CB . ASN A 1 91 ? 24.743 29.595 7.936 1.00 45.58 ? 132 ASN A CB 1 ATOM 669 C CG . ASN A 1 91 ? 23.877 28.363 7.722 1.00 44.09 ? 132 ASN A CG 1 ATOM 670 O OD1 . ASN A 1 91 ? 22.684 28.458 7.404 1.00 44.75 ? 132 ASN A OD1 1 ATOM 671 N ND2 . ASN A 1 91 ? 24.483 27.187 7.901 1.00 45.20 ? 132 ASN A ND2 1 ATOM 672 N N . GLU A 1 92 ? 23.485 31.500 6.103 1.00 49.99 ? 133 GLU A N 1 ATOM 673 C CA . GLU A 1 92 ? 22.695 31.923 4.925 1.00 52.78 ? 133 GLU A CA 1 ATOM 674 C C . GLU A 1 92 ? 21.484 31.047 4.619 1.00 53.38 ? 133 GLU A C 1 ATOM 675 O O . GLU A 1 92 ? 20.492 31.533 4.081 1.00 53.91 ? 133 GLU A O 1 ATOM 676 C CB . GLU A 1 92 ? 23.552 31.928 3.657 1.00 53.78 ? 133 GLU A CB 1 ATOM 677 C CG . GLU A 1 92 ? 25.051 32.056 3.851 1.00 56.76 ? 133 GLU A CG 1 ATOM 678 C CD . GLU A 1 92 ? 25.764 32.394 2.547 1.00 59.99 ? 133 GLU A CD 1 ATOM 679 O OE1 . GLU A 1 92 ? 26.618 31.591 2.103 1.00 62.35 ? 133 GLU A OE1 1 ATOM 680 O OE2 . GLU A 1 92 ? 25.456 33.462 1.969 1.00 61.22 ? 133 GLU A OE2 1 ATOM 681 N N . ASP A 1 93 ? 21.595 29.754 4.921 1.00 53.98 ? 134 ASP A N 1 ATOM 682 C CA . ASP A 1 93 ? 20.510 28.789 4.713 1.00 55.00 ? 134 ASP A CA 1 ATOM 683 C C . ASP A 1 93 ? 19.449 28.876 5.801 1.00 54.32 ? 134 ASP A C 1 ATOM 684 O O . ASP A 1 93 ? 18.333 28.362 5.649 1.00 55.06 ? 134 ASP A O 1 ATOM 685 C CB . ASP A 1 93 ? 21.075 27.369 4.680 1.00 55.63 ? 134 ASP A CB 1 ATOM 686 C CG . ASP A 1 93 ? 22.036 27.161 3.534 1.00 58.60 ? 134 ASP A CG 1 ATOM 687 O OD1 . ASP A 1 93 ? 21.723 27.635 2.417 1.00 60.93 ? 134 ASP A OD1 1 ATOM 688 O OD2 . ASP A 1 93 ? 23.104 26.540 3.745 1.00 61.06 ? 134 ASP A OD2 1 ATOM 689 N N . GLY A 1 94 ? 19.798 29.530 6.900 1.00 52.74 ? 135 GLY A N 1 ATOM 690 C CA . GLY A 1 94 ? 18.933 29.550 8.053 1.00 51.40 ? 135 GLY A CA 1 ATOM 691 C C . GLY A 1 94 ? 19.151 28.325 8.925 1.00 50.04 ? 135 GLY A C 1 ATOM 692 O O . GLY A 1 94 ? 18.237 27.917 9.645 1.00 50.62 ? 135 GLY A O 1 ATOM 693 N N . ASN A 1 95 ? 20.348 27.735 8.862 1.00 48.26 ? 136 ASN A N 1 ATOM 694 C CA . ASN A 1 95 ? 20.726 26.705 9.827 1.00 46.25 ? 136 ASN A CA 1 ATOM 695 C C . ASN A 1 95 ? 21.292 27.353 11.089 1.00 43.67 ? 136 ASN A C 1 ATOM 696 O O . ASN A 1 95 ? 22.158 28.221 11.008 1.00 42.54 ? 136 ASN A O 1 ATOM 697 C CB . ASN A 1 95 ? 21.741 25.736 9.237 1.00 47.23 ? 136 ASN A CB 1 ATOM 698 C CG . ASN A 1 95 ? 21.227 25.059 7.968 1.00 50.63 ? 136 ASN A CG 1 ATOM 699 O OD1 . ASN A 1 95 ? 21.969 24.920 6.986 1.00 54.92 ? 136 ASN A OD1 1 ATOM 700 N ND2 . ASN A 1 95 ? 19.950 24.647 7.979 1.00 52.58 ? 136 ASN A ND2 1 ATOM 701 N N . GLU A 1 96 ? 20.795 26.928 12.244 1.00 41.15 ? 137 GLU A N 1 ATOM 702 C CA . GLU A 1 96 ? 21.278 27.493 13.515 1.00 38.63 ? 137 GLU A CA 1 ATOM 703 C C . GLU A 1 96 ? 22.531 26.768 13.919 1.00 37.11 ? 137 GLU A C 1 ATOM 704 O O . GLU A 1 96 ? 22.474 25.635 14.395 1.00 38.03 ? 137 GLU A O 1 ATOM 705 C CB . GLU A 1 96 ? 20.192 27.430 14.592 1.00 38.24 ? 137 GLU A CB 1 ATOM 706 C CG . GLU A 1 96 ? 19.002 28.287 14.187 1.00 37.06 ? 137 GLU A CG 1 ATOM 707 C CD . GLU A 1 96 ? 17.876 28.347 15.206 1.00 35.85 ? 137 GLU A CD 1 ATOM 708 O OE1 . GLU A 1 96 ? 17.816 27.495 16.109 1.00 34.62 ? 137 GLU A OE1 1 ATOM 709 O OE2 . GLU A 1 96 ? 17.034 29.248 15.055 1.00 36.16 ? 137 GLU A OE2 1 ATOM 710 N N . ILE A 1 97 ? 23.672 27.410 13.691 1.00 36.16 ? 138 ILE A N 1 ATOM 711 C CA . ILE A 1 97 ? 24.975 26.758 13.902 1.00 35.54 ? 138 ILE A CA 1 ATOM 712 C C . ILE A 1 97 ? 25.554 26.873 15.302 1.00 34.85 ? 138 ILE A C 1 ATOM 713 O O . ILE A 1 97 ? 26.552 26.234 15.626 1.00 34.27 ? 138 ILE A O 1 ATOM 714 C CB . ILE A 1 97 ? 26.040 27.191 12.852 1.00 36.49 ? 138 ILE A CB 1 ATOM 715 C CG1 . ILE A 1 97 ? 26.380 28.677 13.001 1.00 34.10 ? 138 ILE A CG1 1 ATOM 716 C CG2 . ILE A 1 97 ? 25.559 26.796 11.436 1.00 37.45 ? 138 ILE A CG2 1 ATOM 717 C CD1 . ILE A 1 97 ? 27.580 29.118 12.140 1.00 36.74 ? 138 ILE A CD1 1 ATOM 718 N N . PHE A 1 98 ? 24.927 27.692 16.141 1.00 33.16 ? 139 PHE A N 1 ATOM 719 C CA . PHE A 1 98 ? 25.348 27.788 17.517 1.00 31.85 ? 139 PHE A CA 1 ATOM 720 C C . PHE A 1 98 ? 24.133 28.244 18.273 1.00 30.61 ? 139 PHE A C 1 ATOM 721 O O . PHE A 1 98 ? 23.443 29.106 17.776 1.00 28.99 ? 139 PHE A O 1 ATOM 722 C CB . PHE A 1 98 ? 26.429 28.855 17.699 1.00 32.24 ? 139 PHE A CB 1 ATOM 723 C CG . PHE A 1 98 ? 26.580 29.292 19.132 1.00 33.34 ? 139 PHE A CG 1 ATOM 724 C CD1 . PHE A 1 98 ? 27.115 28.418 20.090 1.00 33.95 ? 139 PHE A CD1 1 ATOM 725 C CD2 . PHE A 1 98 ? 26.124 30.547 19.541 1.00 32.42 ? 139 PHE A CD2 1 ATOM 726 C CE1 . PHE A 1 98 ? 27.230 28.796 21.433 1.00 34.92 ? 139 PHE A CE1 1 ATOM 727 C CE2 . PHE A 1 98 ? 26.237 30.937 20.893 1.00 32.10 ? 139 PHE A CE2 1 ATOM 728 C CZ . PHE A 1 98 ? 26.783 30.060 21.833 1.00 31.49 ? 139 PHE A CZ 1 ATOM 729 N N . ASN A 1 99 ? 23.866 27.630 19.426 1.00 30.20 ? 140 ASN A N 1 ATOM 730 C CA . ASN A 1 99 ? 22.752 28.011 20.301 1.00 30.14 ? 140 ASN A CA 1 ATOM 731 C C . ASN A 1 99 ? 23.239 28.303 21.683 1.00 29.14 ? 140 ASN A C 1 ATOM 732 O O . ASN A 1 99 ? 24.062 27.558 22.233 1.00 28.96 ? 140 ASN A O 1 ATOM 733 C CB . ASN A 1 99 ? 21.791 26.850 20.415 1.00 31.24 ? 140 ASN A CB 1 ATOM 734 C CG . ASN A 1 99 ? 21.079 26.553 19.119 1.00 32.79 ? 140 ASN A CG 1 ATOM 735 O OD1 . ASN A 1 99 ? 20.863 27.440 18.296 1.00 33.43 ? 140 ASN A OD1 1 ATOM 736 N ND2 . ASN A 1 99 ? 20.707 25.285 18.933 1.00 37.29 ? 140 ASN A ND2 1 ATOM 737 N N . THR A 1 100 ? 22.720 29.384 22.284 1.00 27.59 ? 141 THR A N 1 ATOM 738 C CA . THR A 1 100 ? 23.064 29.618 23.681 1.00 25.83 ? 141 THR A CA 1 ATOM 739 C C . THR A 1 100 ? 22.387 28.603 24.574 1.00 25.66 ? 141 THR A C 1 ATOM 740 O O . THR A 1 100 ? 21.423 27.914 24.168 1.00 26.20 ? 141 THR A O 1 ATOM 741 C CB . THR A 1 100 ? 22.692 31.048 24.121 1.00 24.90 ? 141 THR A CB 1 ATOM 742 O OG1 . THR A 1 100 ? 21.279 31.232 23.966 1.00 25.19 ? 141 THR A OG1 1 ATOM 743 C CG2 . THR A 1 100 ? 23.426 32.066 23.284 1.00 25.65 ? 141 THR A CG2 1 ATOM 744 N N . SER A 1 101 ? 22.837 28.545 25.830 1.00 25.31 ? 142 SER A N 1 ATOM 745 C CA . SER A 1 101 ? 22.344 27.547 26.759 1.00 24.49 ? 142 SER A CA 1 ATOM 746 C C . SER A 1 101 ? 20.851 27.641 27.093 1.00 24.34 ? 142 SER A C 1 ATOM 747 O O . SER A 1 101 ? 20.272 28.747 27.064 1.00 25.74 ? 142 SER A O 1 ATOM 748 C CB . SER A 1 101 ? 23.143 27.610 28.061 1.00 25.94 ? 142 SER A CB 1 ATOM 749 O OG A SER A 1 101 ? 22.832 26.472 28.830 0.50 29.27 ? 142 SER A OG 1 ATOM 750 O OG B SER A 1 101 ? 22.649 28.640 28.946 0.50 20.53 ? 142 SER A OG 1 ATOM 751 N N . LEU A 1 102 ? 20.221 26.527 27.443 1.00 24.98 ? 143 LEU A N 1 ATOM 752 C CA . LEU A 1 102 ? 18.819 26.621 27.888 1.00 25.54 ? 143 LEU A CA 1 ATOM 753 C C . LEU A 1 102 ? 18.653 26.764 29.410 1.00 26.04 ? 143 LEU A C 1 ATOM 754 O O . LEU A 1 102 ? 17.525 26.999 29.874 1.00 25.02 ? 143 LEU A O 1 ATOM 755 C CB . LEU A 1 102 ? 17.979 25.441 27.381 1.00 27.85 ? 143 LEU A CB 1 ATOM 756 C CG . LEU A 1 102 ? 18.037 25.297 25.845 1.00 29.36 ? 143 LEU A CG 1 ATOM 757 C CD1 . LEU A 1 102 ? 17.223 24.108 25.422 1.00 33.78 ? 143 LEU A CD1 1 ATOM 758 C CD2 . LEU A 1 102 ? 17.575 26.582 25.131 1.00 31.65 ? 143 LEU A CD2 1 ATOM 759 N N . PHE A 1 103 ? 19.745 26.640 30.154 1.00 25.39 ? 144 PHE A N 1 ATOM 760 C CA . PHE A 1 103 ? 19.740 26.709 31.617 1.00 25.35 ? 144 PHE A CA 1 ATOM 761 C C . PHE A 1 103 ? 21.173 26.781 32.129 1.00 24.89 ? 144 PHE A C 1 ATOM 762 O O . PHE A 1 103 ? 22.122 26.422 31.437 1.00 25.83 ? 144 PHE A O 1 ATOM 763 C CB . PHE A 1 103 ? 19.009 25.501 32.219 1.00 27.08 ? 144 PHE A CB 1 ATOM 764 C CG . PHE A 1 103 ? 19.628 24.176 31.842 1.00 31.01 ? 144 PHE A CG 1 ATOM 765 C CD1 . PHE A 1 103 ? 20.610 23.604 32.645 1.00 32.81 ? 144 PHE A CD1 1 ATOM 766 C CD2 . PHE A 1 103 ? 19.268 23.535 30.657 1.00 36.06 ? 144 PHE A CD2 1 ATOM 767 C CE1 . PHE A 1 103 ? 21.184 22.402 32.311 1.00 38.20 ? 144 PHE A CE1 1 ATOM 768 C CE2 . PHE A 1 103 ? 19.858 22.337 30.296 1.00 38.01 ? 144 PHE A CE2 1 ATOM 769 C CZ . PHE A 1 103 ? 20.809 21.769 31.119 1.00 37.38 ? 144 PHE A CZ 1 ATOM 770 N N . GLU A 1 104 ? 21.342 27.276 33.361 1.00 22.32 ? 145 GLU A N 1 ATOM 771 C CA . GLU A 1 104 ? 22.678 27.300 33.967 1.00 23.03 ? 145 GLU A CA 1 ATOM 772 C C . GLU A 1 104 ? 22.910 25.904 34.548 1.00 23.00 ? 145 GLU A C 1 ATOM 773 O O . GLU A 1 104 ? 22.030 25.323 35.210 1.00 22.47 ? 145 GLU A O 1 ATOM 774 C CB . GLU A 1 104 ? 22.730 28.258 35.155 1.00 24.02 ? 145 GLU A CB 1 ATOM 775 C CG . GLU A 1 104 ? 22.594 29.706 34.821 1.00 22.09 ? 145 GLU A CG 1 ATOM 776 C CD . GLU A 1 104 ? 22.521 30.533 36.108 1.00 20.18 ? 145 GLU A CD 1 ATOM 777 O OE1 . GLU A 1 104 ? 21.413 30.573 36.696 1.00 21.81 ? 145 GLU A OE1 1 ATOM 778 O OE2 . GLU A 1 104 ? 23.603 31.065 36.509 1.00 20.49 ? 145 GLU A OE2 1 ATOM 779 N N . PRO A 1 105 ? 24.128 25.387 34.397 1.00 23.59 ? 146 PRO A N 1 ATOM 780 C CA . PRO A 1 105 ? 24.381 24.095 35.045 1.00 23.82 ? 146 PRO A CA 1 ATOM 781 C C . PRO A 1 105 ? 24.136 24.187 36.562 1.00 23.19 ? 146 PRO A C 1 ATOM 782 O O . PRO A 1 105 ? 24.694 25.086 37.218 1.00 25.68 ? 146 PRO A O 1 ATOM 783 C CB . PRO A 1 105 ? 25.875 23.876 34.765 1.00 25.18 ? 146 PRO A CB 1 ATOM 784 C CG . PRO A 1 105 ? 26.136 24.653 33.481 1.00 25.83 ? 146 PRO A CG 1 ATOM 785 C CD . PRO A 1 105 ? 25.285 25.893 33.633 1.00 25.62 ? 146 PRO A CD 1 ATOM 786 N N . PRO A 1 106 ? 23.278 23.335 37.136 1.00 22.99 ? 147 PRO A N 1 ATOM 787 C CA . PRO A 1 106 ? 22.983 23.562 38.551 1.00 24.15 ? 147 PRO A CA 1 ATOM 788 C C . PRO A 1 106 ? 24.154 23.222 39.455 1.00 25.15 ? 147 PRO A C 1 ATOM 789 O O . PRO A 1 106 ? 24.978 22.328 39.098 1.00 25.91 ? 147 PRO A O 1 ATOM 790 C CB . PRO A 1 106 ? 21.795 22.624 38.819 1.00 24.75 ? 147 PRO A CB 1 ATOM 791 C CG . PRO A 1 106 ? 21.861 21.636 37.758 1.00 24.14 ? 147 PRO A CG 1 ATOM 792 C CD . PRO A 1 106 ? 22.354 22.358 36.545 1.00 24.22 ? 147 PRO A CD 1 ATOM 793 N N . PRO A 1 107 ? 24.206 23.874 40.635 1.00 25.47 ? 148 PRO A N 1 ATOM 794 C CA . PRO A 1 107 ? 25.365 23.634 41.478 1.00 25.84 ? 148 PRO A CA 1 ATOM 795 C C . PRO A 1 107 ? 25.310 22.260 42.169 1.00 25.61 ? 148 PRO A C 1 ATOM 796 O O . PRO A 1 107 ? 24.244 21.641 42.245 1.00 25.71 ? 148 PRO A O 1 ATOM 797 C CB . PRO A 1 107 ? 25.298 24.770 42.507 1.00 25.12 ? 148 PRO A CB 1 ATOM 798 C CG . PRO A 1 107 ? 23.864 25.169 42.594 1.00 24.87 ? 148 PRO A CG 1 ATOM 799 C CD . PRO A 1 107 ? 23.294 24.888 41.191 1.00 26.08 ? 148 PRO A CD 1 ATOM 800 N N . PRO A 1 108 ? 26.451 21.824 42.733 1.00 26.19 ? 149 PRO A N 1 ATOM 801 C CA . PRO A 1 108 ? 26.503 20.509 43.376 1.00 26.55 ? 149 PRO A CA 1 ATOM 802 C C . PRO A 1 108 ? 25.371 20.240 44.385 1.00 26.73 ? 149 PRO A C 1 ATOM 803 O O . PRO A 1 108 ? 25.130 21.034 45.313 1.00 26.83 ? 149 PRO A O 1 ATOM 804 C CB . PRO A 1 108 ? 27.880 20.510 44.054 1.00 26.80 ? 149 PRO A CB 1 ATOM 805 C CG . PRO A 1 108 ? 28.705 21.454 43.203 1.00 26.79 ? 149 PRO A CG 1 ATOM 806 C CD . PRO A 1 108 ? 27.717 22.559 42.861 1.00 26.41 ? 149 PRO A CD 1 ATOM 807 N N . GLY A 1 109 ? 24.677 19.118 44.194 1.00 27.08 ? 150 GLY A N 1 ATOM 808 C CA . GLY A 1 109 ? 23.652 18.720 45.117 1.00 28.76 ? 150 GLY A CA 1 ATOM 809 C C . GLY A 1 109 ? 22.290 19.336 44.821 1.00 30.81 ? 150 GLY A C 1 ATOM 810 O O . GLY A 1 109 ? 21.307 18.948 45.450 1.00 32.31 ? 150 GLY A O 1 ATOM 811 N N . TYR A 1 110 ? 22.245 20.254 43.853 1.00 32.26 ? 151 TYR A N 1 ATOM 812 C CA . TYR A 1 110 ? 20.986 20.900 43.408 1.00 33.29 ? 151 TYR A CA 1 ATOM 813 C C . TYR A 1 110 ? 20.624 20.515 41.986 1.00 35.65 ? 151 TYR A C 1 ATOM 814 O O . TYR A 1 110 ? 19.730 21.125 41.378 1.00 35.48 ? 151 TYR A O 1 ATOM 815 C CB . TYR A 1 110 ? 21.147 22.405 43.385 1.00 32.52 ? 151 TYR A CB 1 ATOM 816 C CG . TYR A 1 110 ? 21.331 23.056 44.722 1.00 28.44 ? 151 TYR A CG 1 ATOM 817 C CD1 . TYR A 1 110 ? 20.237 23.595 45.414 1.00 27.07 ? 151 TYR A CD1 1 ATOM 818 C CD2 . TYR A 1 110 ? 22.600 23.230 45.266 1.00 24.87 ? 151 TYR A CD2 1 ATOM 819 C CE1 . TYR A 1 110 ? 20.396 24.198 46.624 1.00 25.10 ? 151 TYR A CE1 1 ATOM 820 C CE2 . TYR A 1 110 ? 22.772 23.856 46.484 1.00 22.89 ? 151 TYR A CE2 1 ATOM 821 C CZ . TYR A 1 110 ? 21.650 24.386 47.145 1.00 24.20 ? 151 TYR A CZ 1 ATOM 822 O OH . TYR A 1 110 ? 21.854 25.000 48.350 1.00 23.46 ? 151 TYR A OH 1 ATOM 823 N N . GLU A 1 111 ? 21.331 19.546 41.425 1.00 36.17 ? 152 GLU A N 1 ATOM 824 C CA . GLU A 1 111 ? 21.095 19.162 40.060 1.00 37.96 ? 152 GLU A CA 1 ATOM 825 C C . GLU A 1 111 ? 19.714 18.494 39.875 1.00 38.96 ? 152 GLU A C 1 ATOM 826 O O . GLU A 1 111 ? 19.272 18.307 38.734 1.00 39.19 ? 152 GLU A O 1 ATOM 827 C CB . GLU A 1 111 ? 22.237 18.262 39.532 1.00 38.82 ? 152 GLU A CB 1 ATOM 828 C CG . GLU A 1 111 ? 23.660 18.808 39.806 1.00 38.49 ? 152 GLU A CG 1 ATOM 829 C CD . GLU A 1 111 ? 24.268 18.278 41.110 1.00 40.40 ? 152 GLU A CD 1 ATOM 830 O OE1 . GLU A 1 111 ? 23.515 17.912 42.018 1.00 40.40 ? 152 GLU A OE1 1 ATOM 831 O OE2 . GLU A 1 111 ? 25.517 18.229 41.226 1.00 39.67 ? 152 GLU A OE2 1 ATOM 832 N N . ASN A 1 112 ? 19.038 18.169 40.983 1.00 39.87 ? 153 ASN A N 1 ATOM 833 C CA . ASN A 1 112 ? 17.692 17.562 40.925 1.00 40.60 ? 153 ASN A CA 1 ATOM 834 C C . ASN A 1 112 ? 16.584 18.465 41.449 1.00 40.62 ? 153 ASN A C 1 ATOM 835 O O . ASN A 1 112 ? 15.411 18.078 41.501 1.00 41.31 ? 153 ASN A O 1 ATOM 836 C CB . ASN A 1 112 ? 17.649 16.229 41.676 1.00 40.97 ? 153 ASN A CB 1 ATOM 837 C CG . ASN A 1 112 ? 16.431 15.395 41.315 1.00 41.82 ? 153 ASN A CG 1 ATOM 838 O OD1 . ASN A 1 112 ? 16.193 15.087 40.141 1.00 41.92 ? 153 ASN A OD1 1 ATOM 839 N ND2 . ASN A 1 112 ? 15.654 15.028 42.326 1.00 43.99 ? 153 ASN A ND2 1 ATOM 840 N N . VAL A 1 113 ? 16.948 19.673 41.857 1.00 40.14 ? 154 VAL A N 1 ATOM 841 C CA . VAL A 1 113 ? 15.943 20.615 42.303 1.00 38.60 ? 154 VAL A CA 1 ATOM 842 C C . VAL A 1 113 ? 15.078 21.026 41.096 1.00 38.59 ? 154 VAL A C 1 ATOM 843 O O . VAL A 1 113 ? 15.587 21.283 40.009 1.00 38.59 ? 154 VAL A O 1 ATOM 844 C CB . VAL A 1 113 ? 16.565 21.831 43.020 1.00 39.47 ? 154 VAL A CB 1 ATOM 845 C CG1 . VAL A 1 113 ? 15.461 22.872 43.367 1.00 37.27 ? 154 VAL A CG1 1 ATOM 846 C CG2 . VAL A 1 113 ? 17.260 21.369 44.297 1.00 40.79 ? 154 VAL A CG2 1 ATOM 847 N N . SER A 1 114 ? 13.765 21.022 41.282 1.00 37.41 ? 155 SER A N 1 ATOM 848 C CA . SER A 1 114 ? 12.896 21.418 40.194 1.00 37.45 ? 155 SER A CA 1 ATOM 849 C C . SER A 1 114 ? 12.505 22.891 40.351 1.00 35.20 ? 155 SER A C 1 ATOM 850 O O . SER A 1 114 ? 12.726 23.522 41.417 1.00 34.04 ? 155 SER A O 1 ATOM 851 C CB . SER A 1 114 ? 11.629 20.547 40.162 1.00 39.02 ? 155 SER A CB 1 ATOM 852 O OG . SER A 1 114 ? 11.004 20.591 41.439 1.00 43.26 ? 155 SER A OG 1 ATOM 853 N N . ASP A 1 115 ? 11.931 23.417 39.276 1.00 32.80 ? 156 ASP A N 1 ATOM 854 C CA . ASP A 1 115 ? 11.332 24.722 39.326 1.00 30.53 ? 156 ASP A CA 1 ATOM 855 C C . ASP A 1 115 ? 12.417 25.782 39.453 1.00 26.45 ? 156 ASP A C 1 ATOM 856 O O . ASP A 1 115 ? 12.136 26.877 39.948 1.00 26.53 ? 156 ASP A O 1 ATOM 857 C CB . ASP A 1 115 ? 10.350 24.831 40.496 1.00 31.28 ? 156 ASP A CB 1 ATOM 858 C CG . ASP A 1 115 ? 9.122 23.935 40.330 1.00 37.51 ? 156 ASP A CG 1 ATOM 859 O OD1 . ASP A 1 115 ? 8.638 23.755 39.185 1.00 42.83 ? 156 ASP A OD1 1 ATOM 860 O OD2 . ASP A 1 115 ? 8.654 23.409 41.363 1.00 43.54 ? 156 ASP A OD2 1 ATOM 861 N N . ILE A 1 116 ? 13.633 25.485 38.983 1.00 23.21 ? 157 ILE A N 1 ATOM 862 C CA . ILE A 1 116 ? 14.584 26.570 38.793 1.00 20.47 ? 157 ILE A CA 1 ATOM 863 C C . ILE A 1 116 ? 14.235 27.324 37.505 1.00 20.38 ? 157 ILE A C 1 ATOM 864 O O . ILE A 1 116 ? 14.293 26.765 36.374 1.00 20.86 ? 157 ILE A O 1 ATOM 865 C CB . ILE A 1 116 ? 16.059 26.055 38.749 1.00 19.65 ? 157 ILE A CB 1 ATOM 866 C CG1 . ILE A 1 116 ? 16.435 25.454 40.105 1.00 20.91 ? 157 ILE A CG1 1 ATOM 867 C CG2 . ILE A 1 116 ? 16.988 27.163 38.294 1.00 20.38 ? 157 ILE A CG2 1 ATOM 868 C CD1 . ILE A 1 116 ? 17.787 24.650 40.093 1.00 20.24 ? 157 ILE A CD1 1 ATOM 869 N N . VAL A 1 117 ? 13.845 28.603 37.639 1.00 19.29 ? 158 VAL A N 1 ATOM 870 C CA . VAL A 1 117 ? 13.491 29.340 36.452 1.00 19.12 ? 158 VAL A CA 1 ATOM 871 C C . VAL A 1 117 ? 14.748 29.530 35.583 1.00 19.59 ? 158 VAL A C 1 ATOM 872 O O . VAL A 1 117 ? 15.779 30.000 36.068 1.00 18.93 ? 158 VAL A O 1 ATOM 873 C CB . VAL A 1 117 ? 12.773 30.705 36.773 1.00 19.92 ? 158 VAL A CB 1 ATOM 874 C CG1 . VAL A 1 117 ? 13.811 31.785 37.259 1.00 20.44 ? 158 VAL A CG1 1 ATOM 875 C CG2 . VAL A 1 117 ? 11.987 31.168 35.540 1.00 20.65 ? 158 VAL A CG2 1 ATOM 876 N N . PRO A 1 118 ? 14.680 29.192 34.273 1.00 19.93 ? 159 PRO A N 1 ATOM 877 C CA . PRO A 1 118 ? 15.903 29.429 33.493 1.00 20.90 ? 159 PRO A CA 1 ATOM 878 C C . PRO A 1 118 ? 16.207 30.926 33.335 1.00 20.09 ? 159 PRO A C 1 ATOM 879 O O . PRO A 1 118 ? 15.280 31.750 33.511 1.00 20.08 ? 159 PRO A O 1 ATOM 880 C CB . PRO A 1 118 ? 15.560 28.834 32.097 1.00 21.87 ? 159 PRO A CB 1 ATOM 881 C CG . PRO A 1 118 ? 14.061 28.810 32.038 1.00 21.52 ? 159 PRO A CG 1 ATOM 882 C CD . PRO A 1 118 ? 13.605 28.559 33.474 1.00 21.07 ? 159 PRO A CD 1 ATOM 883 N N . PRO A 1 119 ? 17.464 31.272 32.999 1.00 20.01 ? 160 PRO A N 1 ATOM 884 C CA . PRO A 1 119 ? 17.763 32.700 32.790 1.00 18.95 ? 160 PRO A CA 1 ATOM 885 C C . PRO A 1 119 ? 16.838 33.329 31.748 1.00 18.95 ? 160 PRO A C 1 ATOM 886 O O . PRO A 1 119 ? 16.602 32.741 30.668 1.00 19.13 ? 160 PRO A O 1 ATOM 887 C CB . PRO A 1 119 ? 19.245 32.710 32.371 1.00 18.84 ? 160 PRO A CB 1 ATOM 888 C CG . PRO A 1 119 ? 19.807 31.437 32.932 1.00 20.31 ? 160 PRO A CG 1 ATOM 889 C CD . PRO A 1 119 ? 18.668 30.425 32.810 1.00 19.86 ? 160 PRO A CD 1 ATOM 890 N N . PHE A 1 120 ? 16.270 34.502 32.100 1.00 17.57 ? 161 PHE A N 1 ATOM 891 C CA . PHE A 1 120 ? 15.488 35.281 31.151 1.00 17.50 ? 161 PHE A CA 1 ATOM 892 C C . PHE A 1 120 ? 15.451 36.712 31.627 1.00 17.85 ? 161 PHE A C 1 ATOM 893 O O . PHE A 1 120 ? 15.771 36.962 32.801 1.00 17.83 ? 161 PHE A O 1 ATOM 894 C CB . PHE A 1 120 ? 14.041 34.771 31.032 1.00 18.41 ? 161 PHE A CB 1 ATOM 895 C CG . PHE A 1 120 ? 13.149 35.038 32.269 1.00 18.71 ? 161 PHE A CG 1 ATOM 896 C CD1 . PHE A 1 120 ? 11.971 35.806 32.130 1.00 16.88 ? 161 PHE A CD1 1 ATOM 897 C CD2 . PHE A 1 120 ? 13.433 34.481 33.515 1.00 18.88 ? 161 PHE A CD2 1 ATOM 898 C CE1 . PHE A 1 120 ? 11.082 36.030 33.220 1.00 17.54 ? 161 PHE A CE1 1 ATOM 899 C CE2 . PHE A 1 120 ? 12.573 34.726 34.631 1.00 16.12 ? 161 PHE A CE2 1 ATOM 900 C CZ . PHE A 1 120 ? 11.392 35.515 34.478 1.00 16.69 ? 161 PHE A CZ 1 ATOM 901 N N . SER A 1 121 ? 15.059 37.616 30.719 1.00 17.66 ? 162 SER A N 1 ATOM 902 C CA . SER A 1 121 ? 14.824 39.025 31.125 1.00 16.26 ? 162 SER A CA 1 ATOM 903 C C . SER A 1 121 ? 13.327 39.239 31.348 1.00 17.32 ? 162 SER A C 1 ATOM 904 O O . SER A 1 121 ? 12.549 39.275 30.408 1.00 17.97 ? 162 SER A O 1 ATOM 905 C CB . SER A 1 121 ? 15.322 39.950 30.012 1.00 17.69 ? 162 SER A CB 1 ATOM 906 O OG . SER A 1 121 ? 16.756 39.801 29.813 1.00 18.51 ? 162 SER A OG 1 ATOM 907 N N . ALA A 1 122 ? 12.945 39.428 32.613 1.00 16.22 ? 163 ALA A N 1 ATOM 908 C CA . ALA A 1 122 ? 11.515 39.560 32.890 1.00 15.71 ? 163 ALA A CA 1 ATOM 909 C C . ALA A 1 122 ? 10.942 40.794 32.184 1.00 17.30 ? 163 ALA A C 1 ATOM 910 O O . ALA A 1 122 ? 11.487 41.912 32.274 1.00 15.57 ? 163 ALA A O 1 ATOM 911 C CB . ALA A 1 122 ? 11.261 39.625 34.408 1.00 16.07 ? 163 ALA A CB 1 ATOM 912 N N . PHE A 1 123 ? 9.777 40.555 31.555 1.00 16.86 ? 164 PHE A N 1 ATOM 913 C CA . PHE A 1 123 ? 8.923 41.518 30.835 1.00 16.46 ? 164 PHE A CA 1 ATOM 914 C C . PHE A 1 123 ? 9.344 41.736 29.389 1.00 17.45 ? 164 PHE A C 1 ATOM 915 O O . PHE A 1 123 ? 8.734 42.554 28.690 1.00 18.28 ? 164 PHE A O 1 ATOM 916 C CB . PHE A 1 123 ? 8.667 42.829 31.568 1.00 15.71 ? 164 PHE A CB 1 ATOM 917 C CG . PHE A 1 123 ? 8.033 42.626 32.914 1.00 14.86 ? 164 PHE A CG 1 ATOM 918 C CD1 . PHE A 1 123 ? 6.631 42.460 32.996 1.00 15.35 ? 164 PHE A CD1 1 ATOM 919 C CD2 . PHE A 1 123 ? 8.814 42.593 34.093 1.00 15.74 ? 164 PHE A CD2 1 ATOM 920 C CE1 . PHE A 1 123 ? 6.015 42.322 34.201 1.00 15.45 ? 164 PHE A CE1 1 ATOM 921 C CE2 . PHE A 1 123 ? 8.168 42.419 35.354 1.00 14.30 ? 164 PHE A CE2 1 ATOM 922 C CZ . PHE A 1 123 ? 6.732 42.286 35.396 1.00 15.36 ? 164 PHE A CZ 1 ATOM 923 N N . SER A 1 124 ? 10.352 41.009 28.942 1.00 17.43 ? 165 SER A N 1 ATOM 924 C CA . SER A 1 124 ? 10.637 41.026 27.483 1.00 18.77 ? 165 SER A CA 1 ATOM 925 C C . SER A 1 124 ? 9.385 40.681 26.680 1.00 19.31 ? 165 SER A C 1 ATOM 926 O O . SER A 1 124 ? 8.654 39.758 27.061 1.00 20.43 ? 165 SER A O 1 ATOM 927 C CB . SER A 1 124 ? 11.674 39.973 27.127 1.00 19.37 ? 165 SER A CB 1 ATOM 928 O OG . SER A 1 124 ? 11.898 40.062 25.703 1.00 19.63 ? 165 SER A OG 1 ATOM 929 N N . PRO A 1 125 ? 9.135 41.408 25.577 1.00 19.46 ? 166 PRO A N 1 ATOM 930 C CA . PRO A 1 125 ? 8.074 40.913 24.666 1.00 20.80 ? 166 PRO A CA 1 ATOM 931 C C . PRO A 1 125 ? 8.581 39.685 23.920 1.00 21.70 ? 166 PRO A C 1 ATOM 932 O O . PRO A 1 125 ? 9.784 39.384 23.923 1.00 21.17 ? 166 PRO A O 1 ATOM 933 C CB . PRO A 1 125 ? 7.907 42.074 23.673 1.00 21.84 ? 166 PRO A CB 1 ATOM 934 C CG . PRO A 1 125 ? 9.300 42.706 23.587 1.00 20.14 ? 166 PRO A CG 1 ATOM 935 C CD . PRO A 1 125 ? 9.743 42.658 25.081 1.00 19.89 ? 166 PRO A CD 1 ATOM 936 N N . GLN A 1 126 ? 7.659 38.993 23.260 1.00 22.54 ? 167 GLN A N 1 ATOM 937 C CA . GLN A 1 126 ? 8.003 37.855 22.406 1.00 23.91 ? 167 GLN A CA 1 ATOM 938 C C . GLN A 1 126 ? 8.512 38.333 21.075 1.00 24.92 ? 167 GLN A C 1 ATOM 939 O O . GLN A 1 126 ? 8.161 39.420 20.597 1.00 25.53 ? 167 GLN A O 1 ATOM 940 C CB . GLN A 1 126 ? 6.753 37.006 22.188 1.00 24.04 ? 167 GLN A CB 1 ATOM 941 C CG . GLN A 1 126 ? 6.183 36.430 23.480 1.00 26.95 ? 167 GLN A CG 1 ATOM 942 C CD . GLN A 1 126 ? 4.921 35.620 23.282 1.00 34.55 ? 167 GLN A CD 1 ATOM 943 O OE1 . GLN A 1 126 ? 4.378 35.557 22.183 1.00 37.46 ? 167 GLN A OE1 1 ATOM 944 N NE2 . GLN A 1 126 ? 4.453 34.984 24.340 1.00 31.90 ? 167 GLN A NE2 1 ATOM 945 N N . GLY A 1 127 ? 9.347 37.511 20.450 1.00 25.82 ? 168 GLY A N 1 ATOM 946 C CA . GLY A 1 127 ? 9.783 37.837 19.103 1.00 26.22 ? 168 GLY A CA 1 ATOM 947 C C . GLY A 1 127 ? 10.906 36.925 18.679 1.00 27.34 ? 168 GLY A C 1 ATOM 948 O O . GLY A 1 127 ? 11.541 36.267 19.502 1.00 27.23 ? 168 GLY A O 1 ATOM 949 N N . MET A 1 128 ? 11.141 36.875 17.365 1.00 28.41 ? 169 MET A N 1 ATOM 950 C CA . MET A 1 128 ? 12.295 36.131 16.860 1.00 29.50 ? 169 MET A CA 1 ATOM 951 C C . MET A 1 128 ? 13.105 36.994 15.884 1.00 30.08 ? 169 MET A C 1 ATOM 952 O O . MET A 1 128 ? 13.339 36.568 14.723 1.00 31.97 ? 169 MET A O 1 ATOM 953 C CB . MET A 1 128 ? 11.819 34.833 16.184 1.00 30.55 ? 169 MET A CB 1 ATOM 954 C CG . MET A 1 128 ? 11.228 33.810 17.142 1.00 34.71 ? 169 MET A CG 1 ATOM 955 S SD . MET A 1 128 ? 10.807 32.280 16.278 1.00 16.98 ? 169 MET A SD 1 ATOM 956 C CE . MET A 1 128 ? 9.127 32.050 16.872 1.00 47.56 ? 169 MET A CE 1 ATOM 957 N N . PRO A 1 129 ? 13.562 38.185 16.313 1.00 29.48 ? 170 PRO A N 1 ATOM 958 C CA . PRO A 1 129 ? 14.320 39.087 15.433 1.00 30.22 ? 170 PRO A CA 1 ATOM 959 C C . PRO A 1 129 ? 15.656 38.448 14.976 1.00 31.40 ? 170 PRO A C 1 ATOM 960 O O . PRO A 1 129 ? 16.321 37.776 15.775 1.00 31.46 ? 170 PRO A O 1 ATOM 961 C CB . PRO A 1 129 ? 14.603 40.305 16.330 1.00 30.50 ? 170 PRO A CB 1 ATOM 962 C CG . PRO A 1 129 ? 14.545 39.734 17.737 1.00 28.65 ? 170 PRO A CG 1 ATOM 963 C CD . PRO A 1 129 ? 13.432 38.745 17.682 1.00 28.61 ? 170 PRO A CD 1 ATOM 964 N N . GLU A 1 130 ? 16.018 38.652 13.699 1.00 32.12 ? 171 GLU A N 1 ATOM 965 C CA . GLU A 1 130 ? 17.320 38.185 13.143 1.00 32.89 ? 171 GLU A CA 1 ATOM 966 C C . GLU A 1 130 ? 18.052 39.396 12.612 1.00 32.65 ? 171 GLU A C 1 ATOM 967 O O . GLU A 1 130 ? 17.433 40.247 11.971 1.00 34.24 ? 171 GLU A O 1 ATOM 968 C CB . GLU A 1 130 ? 17.134 37.236 11.937 1.00 33.54 ? 171 GLU A CB 1 ATOM 969 C CG A GLU A 1 130 ? 16.052 36.195 12.058 0.50 34.37 ? 171 GLU A CG 1 ATOM 970 C CD A GLU A 1 130 ? 16.051 35.230 10.875 0.50 34.94 ? 171 GLU A CD 1 ATOM 971 O OE1 A GLU A 1 130 ? 15.189 34.330 10.844 0.50 36.03 ? 171 GLU A OE1 1 ATOM 972 O OE2 A GLU A 1 130 ? 16.921 35.373 9.991 0.50 35.21 ? 171 GLU A OE2 1 ATOM 973 N N . GLY A 1 131 ? 19.359 39.487 12.810 1.00 31.74 ? 172 GLY A N 1 ATOM 974 C CA . GLY A 1 131 ? 20.056 40.669 12.325 1.00 31.65 ? 172 GLY A CA 1 ATOM 975 C C . GLY A 1 131 ? 21.532 40.670 12.612 1.00 31.28 ? 172 GLY A C 1 ATOM 976 O O . GLY A 1 131 ? 22.081 39.682 13.095 1.00 31.82 ? 172 GLY A O 1 ATOM 977 N N . ASP A 1 132 ? 22.167 41.792 12.314 1.00 31.26 ? 173 ASP A N 1 ATOM 978 C CA . ASP A 1 132 ? 23.584 41.967 12.579 1.00 32.14 ? 173 ASP A CA 1 ATOM 979 C C . ASP A 1 132 ? 23.776 42.571 13.964 1.00 31.30 ? 173 ASP A C 1 ATOM 980 O O . ASP A 1 132 ? 23.012 43.455 14.389 1.00 30.93 ? 173 ASP A O 1 ATOM 981 C CB . ASP A 1 132 ? 24.178 42.907 11.553 1.00 33.03 ? 173 ASP A CB 1 ATOM 982 C CG . ASP A 1 132 ? 23.974 42.405 10.112 1.00 37.57 ? 173 ASP A CG 1 ATOM 983 O OD1 . ASP A 1 132 ? 24.052 41.179 9.909 1.00 39.26 ? 173 ASP A OD1 1 ATOM 984 O OD2 . ASP A 1 132 ? 23.710 43.236 9.217 1.00 38.44 ? 173 ASP A OD2 1 ATOM 985 N N . LEU A 1 133 ? 24.799 42.092 14.655 1.00 30.24 ? 174 LEU A N 1 ATOM 986 C CA . LEU A 1 133 ? 25.106 42.579 15.997 1.00 28.78 ? 174 LEU A CA 1 ATOM 987 C C . LEU A 1 133 ? 25.825 43.913 15.969 1.00 29.62 ? 174 LEU A C 1 ATOM 988 O O . LEU A 1 133 ? 26.685 44.151 15.091 1.00 29.01 ? 174 LEU A O 1 ATOM 989 C CB . LEU A 1 133 ? 26.021 41.558 16.665 1.00 28.85 ? 174 LEU A CB 1 ATOM 990 C CG A LEU A 1 133 ? 25.981 41.109 18.122 0.50 29.58 ? 174 LEU A CG 1 ATOM 991 C CG B LEU A 1 133 ? 25.406 40.252 17.175 0.50 25.35 ? 174 LEU A CG 1 ATOM 992 C CD1 A LEU A 1 133 ? 24.538 40.960 18.640 0.50 27.62 ? 174 LEU A CD1 1 ATOM 993 C CD1 B LEU A 1 133 ? 26.477 39.428 17.878 0.50 26.63 ? 174 LEU A CD1 1 ATOM 994 C CD2 A LEU A 1 133 ? 26.745 39.811 18.273 0.50 28.89 ? 174 LEU A CD2 1 ATOM 995 C CD2 B LEU A 1 133 ? 24.179 40.469 18.094 0.50 24.18 ? 174 LEU A CD2 1 ATOM 996 N N . VAL A 1 134 ? 25.520 44.771 16.950 1.00 28.20 ? 175 VAL A N 1 ATOM 997 C CA . VAL A 1 134 ? 26.378 45.916 17.283 1.00 27.63 ? 175 VAL A CA 1 ATOM 998 C C . VAL A 1 134 ? 26.717 45.774 18.772 1.00 27.47 ? 175 VAL A C 1 ATOM 999 O O . VAL A 1 134 ? 25.802 45.538 19.578 1.00 26.88 ? 175 VAL A O 1 ATOM 1000 C CB . VAL A 1 134 ? 25.683 47.289 16.966 1.00 28.63 ? 175 VAL A CB 1 ATOM 1001 C CG1 . VAL A 1 134 ? 26.480 48.454 17.511 1.00 28.11 ? 175 VAL A CG1 1 ATOM 1002 C CG2 . VAL A 1 134 ? 25.520 47.448 15.443 1.00 29.38 ? 175 VAL A CG2 1 ATOM 1003 N N . TYR A 1 135 ? 27.996 45.871 19.121 1.00 26.02 ? 176 TYR A N 1 ATOM 1004 C CA . TYR A 1 135 ? 28.412 45.835 20.537 1.00 25.22 ? 176 TYR A CA 1 ATOM 1005 C C . TYR A 1 135 ? 28.429 47.248 21.102 1.00 25.43 ? 176 TYR A C 1 ATOM 1006 O O . TYR A 1 135 ? 29.082 48.147 20.565 1.00 24.90 ? 176 TYR A O 1 ATOM 1007 C CB . TYR A 1 135 ? 29.824 45.225 20.639 1.00 25.54 ? 176 TYR A CB 1 ATOM 1008 C CG . TYR A 1 135 ? 30.489 45.396 21.994 1.00 25.95 ? 176 TYR A CG 1 ATOM 1009 C CD1 . TYR A 1 135 ? 29.929 44.815 23.133 1.00 24.59 ? 176 TYR A CD1 1 ATOM 1010 C CD2 . TYR A 1 135 ? 31.683 46.105 22.124 1.00 26.76 ? 176 TYR A CD2 1 ATOM 1011 C CE1 . TYR A 1 135 ? 30.528 44.988 24.413 1.00 24.71 ? 176 TYR A CE1 1 ATOM 1012 C CE2 . TYR A 1 135 ? 32.292 46.272 23.363 1.00 28.35 ? 176 TYR A CE2 1 ATOM 1013 C CZ . TYR A 1 135 ? 31.707 45.706 24.513 1.00 24.61 ? 176 TYR A CZ 1 ATOM 1014 O OH . TYR A 1 135 ? 32.326 45.881 25.736 1.00 25.28 ? 176 TYR A OH 1 ATOM 1015 N N . VAL A 1 136 ? 27.720 47.448 22.235 1.00 23.52 ? 177 VAL A N 1 ATOM 1016 C CA . VAL A 1 136 ? 27.455 48.808 22.729 1.00 24.53 ? 177 VAL A CA 1 ATOM 1017 C C . VAL A 1 136 ? 28.043 49.045 24.143 1.00 23.48 ? 177 VAL A C 1 ATOM 1018 O O . VAL A 1 136 ? 27.594 49.933 24.882 1.00 23.34 ? 177 VAL A O 1 ATOM 1019 C CB . VAL A 1 136 ? 25.916 49.134 22.672 1.00 23.74 ? 177 VAL A CB 1 ATOM 1020 C CG1 . VAL A 1 136 ? 25.378 49.056 21.250 1.00 25.22 ? 177 VAL A CG1 1 ATOM 1021 C CG2 . VAL A 1 136 ? 25.126 48.147 23.554 1.00 25.98 ? 177 VAL A CG2 1 ATOM 1022 N N . ASN A 1 137 ? 29.098 48.302 24.490 1.00 23.96 ? 178 ASN A N 1 ATOM 1023 C CA . ASN A 1 137 ? 29.765 48.441 25.782 1.00 22.42 ? 178 ASN A CA 1 ATOM 1024 C C . ASN A 1 137 ? 28.700 48.194 26.864 1.00 23.19 ? 178 ASN A C 1 ATOM 1025 O O . ASN A 1 137 ? 28.030 47.182 26.813 1.00 22.37 ? 178 ASN A O 1 ATOM 1026 C CB . ASN A 1 137 ? 30.477 49.804 25.928 1.00 22.84 ? 178 ASN A CB 1 ATOM 1027 C CG . ASN A 1 137 ? 31.605 49.782 26.947 1.00 22.67 ? 178 ASN A CG 1 ATOM 1028 O OD1 . ASN A 1 137 ? 32.078 48.723 27.336 1.00 24.41 ? 178 ASN A OD1 1 ATOM 1029 N ND2 . ASN A 1 137 ? 32.028 50.964 27.404 1.00 25.01 ? 178 ASN A ND2 1 ATOM 1030 N N . TYR A 1 138 ? 28.545 49.128 27.805 1.00 22.75 ? 179 TYR A N 1 ATOM 1031 C CA . TYR A 1 138 ? 27.591 48.937 28.909 1.00 21.58 ? 179 TYR A CA 1 ATOM 1032 C C . TYR A 1 138 ? 26.209 49.469 28.549 1.00 21.57 ? 179 TYR A C 1 ATOM 1033 O O . TYR A 1 138 ? 25.302 49.465 29.403 1.00 20.81 ? 179 TYR A O 1 ATOM 1034 C CB . TYR A 1 138 ? 28.086 49.661 30.182 1.00 20.97 ? 179 TYR A CB 1 ATOM 1035 C CG . TYR A 1 138 ? 29.370 49.087 30.745 1.00 21.39 ? 179 TYR A CG 1 ATOM 1036 C CD1 . TYR A 1 138 ? 29.357 47.900 31.464 1.00 21.74 ? 179 TYR A CD1 1 ATOM 1037 C CD2 . TYR A 1 138 ? 30.587 49.771 30.602 1.00 24.29 ? 179 TYR A CD2 1 ATOM 1038 C CE1 . TYR A 1 138 ? 30.536 47.370 32.047 1.00 24.35 ? 179 TYR A CE1 1 ATOM 1039 C CE2 . TYR A 1 138 ? 31.770 49.263 31.177 1.00 25.33 ? 179 TYR A CE2 1 ATOM 1040 C CZ . TYR A 1 138 ? 31.733 48.075 31.899 1.00 26.56 ? 179 TYR A CZ 1 ATOM 1041 O OH . TYR A 1 138 ? 32.875 47.586 32.460 1.00 27.18 ? 179 TYR A OH 1 ATOM 1042 N N . ALA A 1 139 ? 26.007 49.901 27.295 1.00 20.45 ? 180 ALA A N 1 ATOM 1043 C CA . ALA A 1 139 ? 24.707 50.430 26.864 1.00 20.59 ? 180 ALA A CA 1 ATOM 1044 C C . ALA A 1 139 ? 24.277 51.672 27.679 1.00 20.81 ? 180 ALA A C 1 ATOM 1045 O O . ALA A 1 139 ? 23.066 51.968 27.810 1.00 21.20 ? 180 ALA A O 1 ATOM 1046 C CB . ALA A 1 139 ? 23.613 49.328 26.881 1.00 21.50 ? 180 ALA A CB 1 ATOM 1047 N N . ARG A 1 140 ? 25.277 52.403 28.189 1.00 20.68 ? 181 ARG A N 1 ATOM 1048 C CA . ARG A 1 140 ? 24.986 53.679 28.898 1.00 20.72 ? 181 ARG A CA 1 ATOM 1049 C C . ARG A 1 140 ? 24.667 54.798 27.915 1.00 21.33 ? 181 ARG A C 1 ATOM 1050 O O . ARG A 1 140 ? 25.021 54.751 26.718 1.00 20.86 ? 181 ARG A O 1 ATOM 1051 C CB . ARG A 1 140 ? 26.174 54.095 29.752 1.00 20.24 ? 181 ARG A CB 1 ATOM 1052 C CG . ARG A 1 140 ? 26.505 53.112 30.858 1.00 21.49 ? 181 ARG A CG 1 ATOM 1053 C CD . ARG A 1 140 ? 27.843 53.385 31.443 1.00 23.77 ? 181 ARG A CD 1 ATOM 1054 N NE . ARG A 1 140 ? 28.891 53.241 30.430 1.00 24.15 ? 181 ARG A NE 1 ATOM 1055 C CZ . ARG A 1 140 ? 30.209 53.401 30.651 1.00 26.20 ? 181 ARG A CZ 1 ATOM 1056 N NH1 . ARG A 1 140 ? 30.686 53.661 31.866 1.00 26.58 ? 181 ARG A NH1 1 ATOM 1057 N NH2 . ARG A 1 140 ? 31.074 53.271 29.639 1.00 27.05 ? 181 ARG A NH2 1 ATOM 1058 N N . THR A 1 141 ? 24.036 55.854 28.437 1.00 20.93 ? 182 THR A N 1 ATOM 1059 C CA . THR A 1 141 ? 23.782 57.035 27.634 1.00 21.67 ? 182 THR A CA 1 ATOM 1060 C C . THR A 1 141 ? 25.057 57.482 26.925 1.00 22.45 ? 182 THR A C 1 ATOM 1061 O O . THR A 1 141 ? 25.026 57.748 25.711 1.00 23.12 ? 182 THR A O 1 ATOM 1062 C CB . THR A 1 141 ? 23.246 58.149 28.533 1.00 22.12 ? 182 THR A CB 1 ATOM 1063 O OG1 . THR A 1 141 ? 21.966 57.724 29.031 1.00 22.17 ? 182 THR A OG1 1 ATOM 1064 C CG2 . THR A 1 141 ? 23.101 59.440 27.709 1.00 22.27 ? 182 THR A CG2 1 ATOM 1065 N N . GLU A 1 142 ? 26.172 57.532 27.641 1.00 23.14 ? 183 GLU A N 1 ATOM 1066 C CA . GLU A 1 142 ? 27.425 58.004 27.007 1.00 24.08 ? 183 GLU A CA 1 ATOM 1067 C C . GLU A 1 142 ? 27.945 56.999 25.996 1.00 25.05 ? 183 GLU A C 1 ATOM 1068 O O . GLU A 1 142 ? 28.614 57.409 25.023 1.00 25.44 ? 183 GLU A O 1 ATOM 1069 C CB . GLU A 1 142 ? 28.476 58.328 28.050 1.00 24.04 ? 183 GLU A CB 1 ATOM 1070 C CG . GLU A 1 142 ? 28.898 57.155 28.916 1.00 27.67 ? 183 GLU A CG 1 ATOM 1071 C CD . GLU A 1 142 ? 28.176 57.127 30.275 1.00 30.62 ? 183 GLU A CD 1 ATOM 1072 O OE1 . GLU A 1 142 ? 26.949 57.497 30.341 1.00 26.27 ? 183 GLU A OE1 1 ATOM 1073 O OE2 . GLU A 1 142 ? 28.852 56.720 31.268 1.00 27.94 ? 183 GLU A OE2 1 ATOM 1074 N N . ASP A 1 143 ? 27.624 55.708 26.178 1.00 24.32 ? 184 ASP A N 1 ATOM 1075 C CA . ASP A 1 143 ? 28.091 54.692 25.177 1.00 25.43 ? 184 ASP A CA 1 ATOM 1076 C C . ASP A 1 143 ? 27.368 54.920 23.847 1.00 26.23 ? 184 ASP A C 1 ATOM 1077 O O . ASP A 1 143 ? 27.979 54.837 22.759 1.00 26.25 ? 184 ASP A O 1 ATOM 1078 C CB . ASP A 1 143 ? 27.852 53.261 25.697 1.00 25.85 ? 184 ASP A CB 1 ATOM 1079 C CG . ASP A 1 143 ? 28.696 52.953 26.918 1.00 24.88 ? 184 ASP A CG 1 ATOM 1080 O OD1 . ASP A 1 143 ? 29.875 53.411 26.964 1.00 25.44 ? 184 ASP A OD1 1 ATOM 1081 O OD2 . ASP A 1 143 ? 28.222 52.235 27.823 1.00 23.95 ? 184 ASP A OD2 1 ATOM 1082 N N . PHE A 1 144 ? 26.055 55.194 23.924 1.00 25.26 ? 185 PHE A N 1 ATOM 1083 C CA . PHE A 1 144 ? 25.317 55.488 22.711 1.00 25.62 ? 185 PHE A CA 1 ATOM 1084 C C . PHE A 1 144 ? 25.718 56.837 22.110 1.00 25.89 ? 185 PHE A C 1 ATOM 1085 O O . PHE A 1 144 ? 25.739 56.974 20.864 1.00 26.95 ? 185 PHE A O 1 ATOM 1086 C CB . PHE A 1 144 ? 23.811 55.363 22.924 1.00 24.57 ? 185 PHE A CB 1 ATOM 1087 C CG . PHE A 1 144 ? 23.350 53.930 22.990 1.00 23.38 ? 185 PHE A CG 1 ATOM 1088 C CD1 . PHE A 1 144 ? 23.079 53.336 24.221 1.00 23.45 ? 185 PHE A CD1 1 ATOM 1089 C CD2 . PHE A 1 144 ? 23.238 53.154 21.833 1.00 21.11 ? 185 PHE A CD2 1 ATOM 1090 C CE1 . PHE A 1 144 ? 22.679 52.005 24.312 1.00 22.19 ? 185 PHE A CE1 1 ATOM 1091 C CE2 . PHE A 1 144 ? 22.847 51.806 21.913 1.00 21.64 ? 185 PHE A CE2 1 ATOM 1092 C CZ . PHE A 1 144 ? 22.561 51.221 23.178 1.00 23.80 ? 185 PHE A CZ 1 ATOM 1093 N N . PHE A 1 145 ? 25.981 57.841 22.954 1.00 25.95 ? 186 PHE A N 1 ATOM 1094 C CA . PHE A 1 145 ? 26.521 59.109 22.428 1.00 27.13 ? 186 PHE A CA 1 ATOM 1095 C C . PHE A 1 145 ? 27.766 58.802 21.581 1.00 29.02 ? 186 PHE A C 1 ATOM 1096 O O . PHE A 1 145 ? 27.925 59.326 20.456 1.00 30.10 ? 186 PHE A O 1 ATOM 1097 C CB . PHE A 1 145 ? 26.943 60.095 23.539 1.00 26.76 ? 186 PHE A CB 1 ATOM 1098 C CG . PHE A 1 145 ? 25.798 60.846 24.202 1.00 28.10 ? 186 PHE A CG 1 ATOM 1099 C CD1 . PHE A 1 145 ? 24.529 60.883 23.647 1.00 26.09 ? 186 PHE A CD1 1 ATOM 1100 C CD2 . PHE A 1 145 ? 26.026 61.530 25.392 1.00 27.54 ? 186 PHE A CD2 1 ATOM 1101 C CE1 . PHE A 1 145 ? 23.476 61.594 24.279 1.00 27.55 ? 186 PHE A CE1 1 ATOM 1102 C CE2 . PHE A 1 145 ? 25.001 62.251 26.023 1.00 24.35 ? 186 PHE A CE2 1 ATOM 1103 C CZ . PHE A 1 145 ? 23.730 62.287 25.452 1.00 25.45 ? 186 PHE A CZ 1 ATOM 1104 N N . LYS A 1 146 ? 28.666 57.985 22.126 1.00 29.52 ? 187 LYS A N 1 ATOM 1105 C CA . LYS A 1 146 ? 29.956 57.725 21.448 1.00 30.94 ? 187 LYS A CA 1 ATOM 1106 C C . LYS A 1 146 ? 29.727 57.029 20.109 1.00 32.02 ? 187 LYS A C 1 ATOM 1107 O O . LYS A 1 146 ? 30.306 57.427 19.089 1.00 32.52 ? 187 LYS A O 1 ATOM 1108 C CB . LYS A 1 146 ? 30.855 56.876 22.332 1.00 30.80 ? 187 LYS A CB 1 ATOM 1109 C CG . LYS A 1 146 ? 32.147 56.429 21.629 1.00 35.68 ? 187 LYS A CG 1 ATOM 1110 C CD . LYS A 1 146 ? 33.307 56.442 22.580 1.00 42.53 ? 187 LYS A CD 1 ATOM 1111 C CE . LYS A 1 146 ? 33.920 57.829 22.620 1.00 47.38 ? 187 LYS A CE 1 ATOM 1112 N NZ . LYS A 1 146 ? 34.491 58.098 23.984 1.00 51.32 ? 187 LYS A NZ 1 ATOM 1113 N N . LEU A 1 147 ? 28.895 55.992 20.105 1.00 31.08 ? 188 LEU A N 1 ATOM 1114 C CA . LEU A 1 147 ? 28.543 55.287 18.869 1.00 32.62 ? 188 LEU A CA 1 ATOM 1115 C C . LEU A 1 147 ? 27.909 56.181 17.815 1.00 34.06 ? 188 LEU A C 1 ATOM 1116 O O . LEU A 1 147 ? 28.374 56.201 16.666 1.00 34.62 ? 188 LEU A O 1 ATOM 1117 C CB . LEU A 1 147 ? 27.563 54.153 19.150 1.00 32.18 ? 188 LEU A CB 1 ATOM 1118 C CG . LEU A 1 147 ? 28.100 52.903 19.799 1.00 32.21 ? 188 LEU A CG 1 ATOM 1119 C CD1 . LEU A 1 147 ? 26.920 52.066 20.330 1.00 34.60 ? 188 LEU A CD1 1 ATOM 1120 C CD2 . LEU A 1 147 ? 28.905 52.126 18.789 1.00 34.04 ? 188 LEU A CD2 1 ATOM 1121 N N . GLU A 1 148 ? 26.845 56.902 18.189 1.00 33.93 ? 189 GLU A N 1 ATOM 1122 C CA . GLU A 1 148 ? 26.102 57.715 17.229 1.00 35.78 ? 189 GLU A CA 1 ATOM 1123 C C . GLU A 1 148 ? 26.834 58.982 16.828 1.00 36.36 ? 189 GLU A C 1 ATOM 1124 O O . GLU A 1 148 ? 26.937 59.296 15.619 1.00 37.38 ? 189 GLU A O 1 ATOM 1125 C CB . GLU A 1 148 ? 24.682 58.097 17.715 1.00 36.17 ? 189 GLU A CB 1 ATOM 1126 C CG . GLU A 1 148 ? 24.054 59.145 16.728 1.00 42.26 ? 189 GLU A CG 1 ATOM 1127 C CD . GLU A 1 148 ? 22.667 59.658 17.117 1.00 48.52 ? 189 GLU A CD 1 ATOM 1128 O OE1 . GLU A 1 148 ? 21.708 58.857 17.067 1.00 50.76 ? 189 GLU A OE1 1 ATOM 1129 O OE2 . GLU A 1 148 ? 22.530 60.874 17.426 1.00 50.91 ? 189 GLU A OE2 1 ATOM 1130 N N . ARG A 1 149 ? 27.339 59.717 17.818 1.00 34.69 ? 190 ARG A N 1 ATOM 1131 C CA . ARG A 1 149 ? 27.881 61.051 17.561 1.00 35.42 ? 190 ARG A CA 1 ATOM 1132 C C . ARG A 1 149 ? 29.331 61.016 17.079 1.00 36.38 ? 190 ARG A C 1 ATOM 1133 O O . ARG A 1 149 ? 29.677 61.749 16.144 1.00 38.10 ? 190 ARG A O 1 ATOM 1134 C CB . ARG A 1 149 ? 27.728 61.967 18.786 1.00 34.33 ? 190 ARG A CB 1 ATOM 1135 C CG . ARG A 1 149 ? 26.268 62.182 19.212 1.00 30.71 ? 190 ARG A CG 1 ATOM 1136 C CD . ARG A 1 149 ? 26.190 62.888 20.578 1.00 30.20 ? 190 ARG A CD 1 ATOM 1137 N NE . ARG A 1 149 ? 24.815 63.261 20.910 1.00 31.49 ? 190 ARG A NE 1 ATOM 1138 C CZ . ARG A 1 149 ? 24.496 64.034 21.950 1.00 31.23 ? 190 ARG A CZ 1 ATOM 1139 N NH1 . ARG A 1 149 ? 25.451 64.485 22.759 1.00 29.06 ? 190 ARG A NH1 1 ATOM 1140 N NH2 . ARG A 1 149 ? 23.218 64.330 22.185 1.00 31.30 ? 190 ARG A NH2 1 ATOM 1141 N N . ASP A 1 150 ? 30.162 60.174 17.705 1.00 36.70 ? 191 ASP A N 1 ATOM 1142 C CA . ASP A 1 150 ? 31.598 60.138 17.411 1.00 38.08 ? 191 ASP A CA 1 ATOM 1143 C C . ASP A 1 150 ? 31.940 59.098 16.361 1.00 38.35 ? 191 ASP A C 1 ATOM 1144 O O . ASP A 1 150 ? 32.680 59.389 15.423 1.00 39.13 ? 191 ASP A O 1 ATOM 1145 C CB . ASP A 1 150 ? 32.420 59.859 18.665 1.00 38.78 ? 191 ASP A CB 1 ATOM 1146 C CG . ASP A 1 150 ? 32.187 60.875 19.745 1.00 42.55 ? 191 ASP A CG 1 ATOM 1147 O OD1 . ASP A 1 150 ? 31.649 61.957 19.423 1.00 45.68 ? 191 ASP A OD1 1 ATOM 1148 O OD2 . ASP A 1 150 ? 32.540 60.586 20.915 1.00 46.34 ? 191 ASP A OD2 1 ATOM 1149 N N . MET A 1 151 ? 31.410 57.892 16.506 1.00 37.18 ? 192 MET A N 1 ATOM 1150 C CA . MET A 1 151 ? 31.791 56.812 15.602 1.00 37.44 ? 192 MET A CA 1 ATOM 1151 C C . MET A 1 151 ? 30.893 56.698 14.385 1.00 37.71 ? 192 MET A C 1 ATOM 1152 O O . MET A 1 151 ? 31.239 55.975 13.430 1.00 38.28 ? 192 MET A O 1 ATOM 1153 C CB . MET A 1 151 ? 31.793 55.471 16.342 1.00 36.53 ? 192 MET A CB 1 ATOM 1154 C CG . MET A 1 151 ? 32.748 55.411 17.488 1.00 36.60 ? 192 MET A CG 1 ATOM 1155 S SD . MET A 1 151 ? 32.726 53.763 18.236 1.00 14.38 ? 192 MET A SD 1 ATOM 1156 C CE . MET A 1 151 ? 33.832 52.881 17.094 1.00 38.37 ? 192 MET A CE 1 ATOM 1157 N N . LYS A 1 152 ? 29.763 57.389 14.411 1.00 37.43 ? 193 LYS A N 1 ATOM 1158 C CA . LYS A 1 152 ? 28.782 57.386 13.336 1.00 38.44 ? 193 LYS A CA 1 ATOM 1159 C C . LYS A 1 152 ? 28.234 56.004 13.047 1.00 38.84 ? 193 LYS A C 1 ATOM 1160 O O . LYS A 1 152 ? 28.005 55.657 11.886 1.00 40.81 ? 193 LYS A O 1 ATOM 1161 C CB . LYS A 1 152 ? 29.365 58.010 12.044 1.00 39.37 ? 193 LYS A CB 1 ATOM 1162 C CG . LYS A 1 152 ? 29.099 59.486 11.907 1.00 43.29 ? 193 LYS A CG 1 ATOM 1163 C CD . LYS A 1 152 ? 29.882 60.350 12.883 1.00 47.02 ? 193 LYS A CD 1 ATOM 1164 C CE . LYS A 1 152 ? 29.360 61.777 12.810 1.00 49.46 ? 193 LYS A CE 1 ATOM 1165 N NZ . LYS A 1 152 ? 30.150 62.693 13.663 1.00 50.00 ? 193 LYS A NZ 1 ATOM 1166 N N . ILE A 1 153 ? 28.030 55.199 14.091 1.00 37.33 ? 194 ILE A N 1 ATOM 1167 C CA . ILE A 1 153 ? 27.468 53.861 13.911 1.00 37.22 ? 194 ILE A CA 1 ATOM 1168 C C . ILE A 1 153 ? 25.977 53.902 14.218 1.00 37.39 ? 194 ILE A C 1 ATOM 1169 O O . ILE A 1 153 ? 25.560 54.463 15.231 1.00 36.83 ? 194 ILE A O 1 ATOM 1170 C CB . ILE A 1 153 ? 28.237 52.824 14.752 1.00 37.19 ? 194 ILE A CB 1 ATOM 1171 C CG1 . ILE A 1 153 ? 29.558 52.497 14.045 1.00 38.41 ? 194 ILE A CG1 1 ATOM 1172 C CG2 . ILE A 1 153 ? 27.431 51.543 14.916 1.00 36.69 ? 194 ILE A CG2 1 ATOM 1173 C CD1 . ILE A 1 153 ? 30.665 52.064 14.950 1.00 40.80 ? 194 ILE A CD1 1 ATOM 1174 N N . ASN A 1 154 ? 25.169 53.344 13.334 1.00 37.44 ? 195 ASN A N 1 ATOM 1175 C CA . ASN A 1 154 ? 23.719 53.429 13.456 1.00 37.74 ? 195 ASN A CA 1 ATOM 1176 C C . ASN A 1 154 ? 23.185 52.079 13.962 1.00 36.55 ? 195 ASN A C 1 ATOM 1177 O O . ASN A 1 154 ? 23.435 51.051 13.340 1.00 35.08 ? 195 ASN A O 1 ATOM 1178 C CB . ASN A 1 154 ? 23.133 53.810 12.088 1.00 39.50 ? 195 ASN A CB 1 ATOM 1179 C CG . ASN A 1 154 ? 21.622 54.050 12.118 1.00 44.02 ? 195 ASN A CG 1 ATOM 1180 O OD1 . ASN A 1 154 ? 20.953 53.863 13.149 1.00 43.86 ? 195 ASN A OD1 1 ATOM 1181 N ND2 . ASN A 1 154 ? 21.077 54.470 10.966 1.00 50.88 ? 195 ASN A ND2 1 ATOM 1182 N N . CYS A 1 155 ? 22.490 52.072 15.113 1.00 34.55 ? 196 CYS A N 1 ATOM 1183 C CA . CYS A 1 155 ? 21.948 50.830 15.672 1.00 33.37 ? 196 CYS A CA 1 ATOM 1184 C C . CYS A 1 155 ? 20.567 50.492 15.156 1.00 33.76 ? 196 CYS A C 1 ATOM 1185 O O . CYS A 1 155 ? 19.970 49.465 15.541 1.00 32.68 ? 196 CYS A O 1 ATOM 1186 C CB . CYS A 1 155 ? 21.900 50.899 17.218 1.00 32.68 ? 196 CYS A CB 1 ATOM 1187 S SG . CYS A 1 155 ? 23.497 51.039 17.959 1.00 11.76 ? 196 CYS A SG 1 ATOM 1188 N N . SER A 1 156 ? 20.023 51.360 14.314 1.00 33.96 ? 197 SER A N 1 ATOM 1189 C CA . SER A 1 156 ? 18.677 51.147 13.799 1.00 34.87 ? 197 SER A CA 1 ATOM 1190 C C . SER A 1 156 ? 18.549 49.778 13.117 1.00 34.90 ? 197 SER A C 1 ATOM 1191 O O . SER A 1 156 ? 19.249 49.482 12.128 1.00 36.55 ? 197 SER A O 1 ATOM 1192 C CB . SER A 1 156 ? 18.292 52.265 12.823 1.00 35.63 ? 197 SER A CB 1 ATOM 1193 O OG . SER A 1 156 ? 16.940 52.133 12.383 1.00 37.47 ? 197 SER A OG 1 ATOM 1194 N N . GLY A 1 157 ? 17.657 48.940 13.633 1.00 33.76 ? 198 GLY A N 1 ATOM 1195 C CA . GLY A 1 157 ? 17.401 47.647 13.017 1.00 32.44 ? 198 GLY A CA 1 ATOM 1196 C C . GLY A 1 157 ? 18.454 46.603 13.325 1.00 32.17 ? 198 GLY A C 1 ATOM 1197 O O . GLY A 1 157 ? 18.425 45.502 12.758 1.00 33.14 ? 198 GLY A O 1 ATOM 1198 N N . LYS A 1 158 ? 19.385 46.924 14.224 1.00 30.96 ? 199 LYS A N 1 ATOM 1199 C CA . LYS A 1 158 ? 20.425 45.985 14.633 1.00 31.08 ? 199 LYS A CA 1 ATOM 1200 C C . LYS A 1 158 ? 20.061 45.315 15.956 1.00 30.89 ? 199 LYS A C 1 ATOM 1201 O O . LYS A 1 158 ? 19.264 45.846 16.740 1.00 29.75 ? 199 LYS A O 1 ATOM 1202 C CB . LYS A 1 158 ? 21.769 46.691 14.816 1.00 31.50 ? 199 LYS A CB 1 ATOM 1203 C CG . LYS A 1 158 ? 22.247 47.463 13.605 1.00 35.18 ? 199 LYS A CG 1 ATOM 1204 C CD . LYS A 1 158 ? 22.557 46.497 12.461 1.00 38.30 ? 199 LYS A CD 1 ATOM 1205 C CE . LYS A 1 158 ? 23.301 47.205 11.335 1.00 42.40 ? 199 LYS A CE 1 ATOM 1206 N NZ . LYS A 1 158 ? 22.309 47.872 10.467 1.00 42.42 ? 199 LYS A NZ 1 ATOM 1207 N N . ILE A 1 159 ? 20.672 44.167 16.210 1.00 29.94 ? 200 ILE A N 1 ATOM 1208 C CA . ILE A 1 159 ? 20.586 43.555 17.541 1.00 29.24 ? 200 ILE A CA 1 ATOM 1209 C C . ILE A 1 159 ? 21.793 44.051 18.314 1.00 29.04 ? 200 ILE A C 1 ATOM 1210 O O . ILE A 1 159 ? 22.930 43.969 17.835 1.00 29.67 ? 200 ILE A O 1 ATOM 1211 C CB . ILE A 1 159 ? 20.523 42.016 17.458 1.00 30.14 ? 200 ILE A CB 1 ATOM 1212 C CG1 . ILE A 1 159 ? 19.182 41.601 16.824 1.00 31.48 ? 200 ILE A CG1 1 ATOM 1213 C CG2 . ILE A 1 159 ? 20.657 41.383 18.858 1.00 29.23 ? 200 ILE A CG2 1 ATOM 1214 C CD1 . ILE A 1 159 ? 19.144 40.124 16.409 1.00 32.63 ? 200 ILE A CD1 1 ATOM 1215 N N . VAL A 1 160 ? 21.572 44.629 19.497 1.00 27.13 ? 201 VAL A N 1 ATOM 1216 C CA . VAL A 1 160 ? 22.731 45.095 20.233 1.00 27.00 ? 201 VAL A CA 1 ATOM 1217 C C . VAL A 1 160 ? 23.112 44.095 21.313 1.00 25.81 ? 201 VAL A C 1 ATOM 1218 O O . VAL A 1 160 ? 22.257 43.444 21.917 1.00 25.41 ? 201 VAL A O 1 ATOM 1219 C CB . VAL A 1 160 ? 22.521 46.512 20.835 1.00 28.45 ? 201 VAL A CB 1 ATOM 1220 C CG1 . VAL A 1 160 ? 22.263 47.551 19.747 1.00 28.08 ? 201 VAL A CG1 1 ATOM 1221 C CG2 . VAL A 1 160 ? 21.416 46.520 21.863 1.00 28.66 ? 201 VAL A CG2 1 ATOM 1222 N N . ILE A 1 161 ? 24.406 43.973 21.536 1.00 24.10 ? 202 ILE A N 1 ATOM 1223 C CA . ILE A 1 161 ? 24.903 43.164 22.620 1.00 24.42 ? 202 ILE A CA 1 ATOM 1224 C C . ILE A 1 161 ? 25.626 44.094 23.590 1.00 24.46 ? 202 ILE A C 1 ATOM 1225 O O . ILE A 1 161 ? 26.473 44.892 23.198 1.00 23.71 ? 202 ILE A O 1 ATOM 1226 C CB . ILE A 1 161 ? 25.780 41.999 22.096 1.00 24.91 ? 202 ILE A CB 1 ATOM 1227 C CG1 . ILE A 1 161 ? 26.289 41.148 23.260 1.00 24.85 ? 202 ILE A CG1 1 ATOM 1228 C CG2 . ILE A 1 161 ? 26.913 42.530 21.154 1.00 24.67 ? 202 ILE A CG2 1 ATOM 1229 C CD1 . ILE A 1 161 ? 26.763 39.705 22.776 1.00 23.55 ? 202 ILE A CD1 1 ATOM 1230 N N . ALA A 1 162 ? 25.212 44.049 24.863 1.00 22.33 ? 203 ALA A N 1 ATOM 1231 C CA . ALA A 1 162 ? 25.747 44.926 25.877 1.00 22.17 ? 203 ALA A CA 1 ATOM 1232 C C . ALA A 1 162 ? 26.235 44.101 27.054 1.00 22.18 ? 203 ALA A C 1 ATOM 1233 O O . ALA A 1 162 ? 25.619 43.081 27.406 1.00 21.49 ? 203 ALA A O 1 ATOM 1234 C CB . ALA A 1 162 ? 24.650 45.902 26.331 1.00 21.18 ? 203 ALA A CB 1 ATOM 1235 N N . ARG A 1 163 ? 27.346 44.521 27.658 1.00 22.59 ? 204 ARG A N 1 ATOM 1236 C CA . ARG A 1 163 ? 27.748 43.896 28.893 1.00 22.75 ? 204 ARG A CA 1 ATOM 1237 C C . ARG A 1 163 ? 26.994 44.494 30.078 1.00 22.20 ? 204 ARG A C 1 ATOM 1238 O O . ARG A 1 163 ? 26.687 45.717 30.112 1.00 20.54 ? 204 ARG A O 1 ATOM 1239 C CB . ARG A 1 163 ? 29.263 43.933 29.097 1.00 23.87 ? 204 ARG A CB 1 ATOM 1240 C CG . ARG A 1 163 ? 29.892 45.263 28.998 1.00 25.40 ? 204 ARG A CG 1 ATOM 1241 C CD . ARG A 1 163 ? 31.379 45.029 29.309 1.00 27.66 ? 204 ARG A CD 1 ATOM 1242 N NE . ARG A 1 163 ? 32.195 46.197 28.964 1.00 25.53 ? 204 ARG A NE 1 ATOM 1243 C CZ . ARG A 1 163 ? 33.410 46.407 29.462 1.00 28.24 ? 204 ARG A CZ 1 ATOM 1244 N NH1 . ARG A 1 163 ? 33.890 45.576 30.388 1.00 25.08 ? 204 ARG A NH1 1 ATOM 1245 N NH2 . ARG A 1 163 ? 34.083 47.499 29.088 1.00 27.34 ? 204 ARG A NH2 1 ATOM 1246 N N . TYR A 1 164 ? 26.649 43.615 31.016 1.00 20.85 ? 205 TYR A N 1 ATOM 1247 C CA . TYR A 1 164 ? 26.018 44.042 32.258 1.00 20.93 ? 205 TYR A CA 1 ATOM 1248 C C . TYR A 1 164 ? 27.035 44.860 33.032 1.00 21.23 ? 205 TYR A C 1 ATOM 1249 O O . TYR A 1 164 ? 28.261 44.696 32.833 1.00 20.84 ? 205 TYR A O 1 ATOM 1250 C CB . TYR A 1 164 ? 25.700 42.804 33.049 1.00 20.10 ? 205 TYR A CB 1 ATOM 1251 C CG . TYR A 1 164 ? 24.331 42.174 32.879 1.00 18.79 ? 205 TYR A CG 1 ATOM 1252 C CD1 . TYR A 1 164 ? 24.217 40.802 32.641 1.00 18.82 ? 205 TYR A CD1 1 ATOM 1253 C CD2 . TYR A 1 164 ? 23.152 42.908 33.139 1.00 18.13 ? 205 TYR A CD2 1 ATOM 1254 C CE1 . TYR A 1 164 ? 22.959 40.160 32.556 1.00 15.98 ? 205 TYR A CE1 1 ATOM 1255 C CE2 . TYR A 1 164 ? 21.881 42.316 33.096 1.00 15.77 ? 205 TYR A CE2 1 ATOM 1256 C CZ . TYR A 1 164 ? 21.757 40.921 32.857 1.00 18.30 ? 205 TYR A CZ 1 ATOM 1257 O OH . TYR A 1 164 ? 20.517 40.340 32.869 1.00 19.13 ? 205 TYR A OH 1 ATOM 1258 N N . GLY A 1 165 ? 26.544 45.705 33.952 1.00 19.87 ? 206 GLY A N 1 ATOM 1259 C CA . GLY A 1 165 ? 27.431 46.475 34.835 1.00 19.64 ? 206 GLY A CA 1 ATOM 1260 C C . GLY A 1 165 ? 27.187 47.967 34.725 1.00 20.14 ? 206 GLY A C 1 ATOM 1261 O O . GLY A 1 165 ? 26.602 48.414 33.744 1.00 19.99 ? 206 GLY A O 1 ATOM 1262 N N . LYS A 1 166 ? 27.675 48.714 35.722 1.00 20.14 ? 207 LYS A N 1 ATOM 1263 C CA . LYS A 1 166 ? 27.682 50.202 35.710 1.00 19.90 ? 207 LYS A CA 1 ATOM 1264 C C . LYS A 1 166 ? 26.311 50.824 35.933 1.00 19.94 ? 207 LYS A C 1 ATOM 1265 O O . LYS A 1 166 ? 26.198 51.740 36.774 1.00 21.96 ? 207 LYS A O 1 ATOM 1266 C CB . LYS A 1 166 ? 28.255 50.801 34.433 1.00 19.83 ? 207 LYS A CB 1 ATOM 1267 C CG . LYS A 1 166 ? 29.705 50.307 34.077 1.00 21.68 ? 207 LYS A CG 1 ATOM 1268 C CD . LYS A 1 166 ? 30.720 50.747 35.109 1.00 26.53 ? 207 LYS A CD 1 ATOM 1269 C CE . LYS A 1 166 ? 32.122 50.368 34.595 1.00 31.17 ? 207 LYS A CE 1 ATOM 1270 N NZ . LYS A 1 166 ? 33.119 50.795 35.647 1.00 36.47 ? 207 LYS A NZ 1 ATOM 1271 N N . VAL A 1 167 ? 25.281 50.331 35.240 1.00 18.86 ? 208 VAL A N 1 ATOM 1272 C CA . VAL A 1 167 ? 23.920 50.924 35.383 1.00 17.95 ? 208 VAL A CA 1 ATOM 1273 C C . VAL A 1 167 ? 22.871 49.853 35.382 1.00 17.67 ? 208 VAL A C 1 ATOM 1274 O O . VAL A 1 167 ? 23.113 48.738 34.857 1.00 17.08 ? 208 VAL A O 1 ATOM 1275 C CB . VAL A 1 167 ? 23.598 51.950 34.229 1.00 19.15 ? 208 VAL A CB 1 ATOM 1276 C CG1 . VAL A 1 167 ? 24.668 53.070 34.210 1.00 18.29 ? 208 VAL A CG1 1 ATOM 1277 C CG2 . VAL A 1 167 ? 23.436 51.278 32.860 1.00 19.29 ? 208 VAL A CG2 1 ATOM 1278 N N . PHE A 1 168 ? 21.688 50.206 35.898 1.00 16.25 ? 209 PHE A N 1 ATOM 1279 C CA . PHE A 1 168 ? 20.534 49.281 35.888 1.00 15.64 ? 209 PHE A CA 1 ATOM 1280 C C . PHE A 1 168 ? 20.223 48.776 34.467 1.00 15.89 ? 209 PHE A C 1 ATOM 1281 O O . PHE A 1 168 ? 20.165 49.562 33.479 1.00 16.50 ? 209 PHE A O 1 ATOM 1282 C CB . PHE A 1 168 ? 19.329 50.033 36.461 1.00 15.52 ? 209 PHE A CB 1 ATOM 1283 C CG . PHE A 1 168 ? 18.035 49.264 36.388 1.00 14.54 ? 209 PHE A CG 1 ATOM 1284 C CD1 . PHE A 1 168 ? 17.930 48.033 37.045 1.00 15.49 ? 209 PHE A CD1 1 ATOM 1285 C CD2 . PHE A 1 168 ? 16.885 49.829 35.739 1.00 15.83 ? 209 PHE A CD2 1 ATOM 1286 C CE1 . PHE A 1 168 ? 16.709 47.323 37.051 1.00 16.84 ? 209 PHE A CE1 1 ATOM 1287 C CE2 . PHE A 1 168 ? 15.665 49.107 35.727 1.00 16.86 ? 209 PHE A CE2 1 ATOM 1288 C CZ . PHE A 1 168 ? 15.589 47.848 36.348 1.00 17.81 ? 209 PHE A CZ 1 ATOM 1289 N N . ARG A 1 169 ? 19.949 47.477 34.363 1.00 16.21 ? 210 ARG A N 1 ATOM 1290 C CA . ARG A 1 169 ? 19.703 46.875 33.022 1.00 15.61 ? 210 ARG A CA 1 ATOM 1291 C C . ARG A 1 169 ? 18.462 47.459 32.297 1.00 16.46 ? 210 ARG A C 1 ATOM 1292 O O . ARG A 1 169 ? 18.401 47.497 31.059 1.00 17.02 ? 210 ARG A O 1 ATOM 1293 C CB . ARG A 1 169 ? 19.612 45.351 33.127 1.00 15.47 ? 210 ARG A CB 1 ATOM 1294 C CG . ARG A 1 169 ? 18.308 44.877 33.861 1.00 15.85 ? 210 ARG A CG 1 ATOM 1295 C CD . ARG A 1 169 ? 18.354 43.333 34.048 1.00 17.04 ? 210 ARG A CD 1 ATOM 1296 N NE . ARG A 1 169 ? 19.162 42.919 35.223 1.00 15.84 ? 210 ARG A NE 1 ATOM 1297 C CZ . ARG A 1 169 ? 18.729 43.128 36.485 1.00 16.60 ? 210 ARG A CZ 1 ATOM 1298 N NH1 . ARG A 1 169 ? 17.557 43.771 36.684 1.00 15.74 ? 210 ARG A NH1 1 ATOM 1299 N NH2 . ARG A 1 169 ? 19.462 42.735 37.532 1.00 16.25 ? 210 ARG A NH2 1 ATOM 1300 N N . GLY A 1 170 ? 17.462 47.917 33.058 1.00 16.32 ? 211 GLY A N 1 ATOM 1301 C CA . GLY A 1 170 ? 16.330 48.592 32.462 1.00 18.00 ? 211 GLY A CA 1 ATOM 1302 C C . GLY A 1 170 ? 16.771 49.861 31.698 1.00 17.52 ? 211 GLY A C 1 ATOM 1303 O O . GLY A 1 170 ? 16.217 50.148 30.631 1.00 17.53 ? 211 GLY A O 1 ATOM 1304 N N . ASN A 1 171 ? 17.735 50.628 32.234 1.00 17.76 ? 212 ASN A N 1 ATOM 1305 C CA . ASN A 1 171 ? 18.219 51.791 31.485 1.00 18.20 ? 212 ASN A CA 1 ATOM 1306 C C . ASN A 1 171 ? 18.936 51.402 30.200 1.00 19.23 ? 212 ASN A C 1 ATOM 1307 O O . ASN A 1 171 ? 18.802 52.070 29.162 1.00 18.62 ? 212 ASN A O 1 ATOM 1308 C CB . ASN A 1 171 ? 19.154 52.620 32.352 1.00 17.91 ? 212 ASN A CB 1 ATOM 1309 C CG . ASN A 1 171 ? 18.406 53.298 33.500 1.00 19.26 ? 212 ASN A CG 1 ATOM 1310 O OD1 . ASN A 1 171 ? 18.339 52.748 34.605 1.00 20.11 ? 212 ASN A OD1 1 ATOM 1311 N ND2 . ASN A 1 171 ? 17.739 54.455 33.218 1.00 17.28 ? 212 ASN A ND2 1 ATOM 1312 N N . LYS A 1 172 ? 19.668 50.296 30.260 1.00 18.12 ? 213 LYS A N 1 ATOM 1313 C CA . LYS A 1 172 ? 20.307 49.786 29.051 1.00 19.02 ? 213 LYS A CA 1 ATOM 1314 C C . LYS A 1 172 ? 19.311 49.523 27.952 1.00 18.55 ? 213 LYS A C 1 ATOM 1315 O O . LYS A 1 172 ? 19.560 49.864 26.758 1.00 19.23 ? 213 LYS A O 1 ATOM 1316 C CB . LYS A 1 172 ? 21.081 48.493 29.338 1.00 17.63 ? 213 LYS A CB 1 ATOM 1317 C CG . LYS A 1 172 ? 22.195 48.614 30.393 1.00 18.42 ? 213 LYS A CG 1 ATOM 1318 C CD . LYS A 1 172 ? 22.809 47.234 30.585 1.00 18.77 ? 213 LYS A CD 1 ATOM 1319 C CE . LYS A 1 172 ? 23.742 47.217 31.779 1.00 18.52 ? 213 LYS A CE 1 ATOM 1320 N NZ . LYS A 1 172 ? 25.210 47.543 31.517 1.00 18.95 ? 213 LYS A NZ 1 ATOM 1321 N N . VAL A 1 173 ? 18.207 48.858 28.295 1.00 17.58 ? 214 VAL A N 1 ATOM 1322 C CA . VAL A 1 173 ? 17.225 48.469 27.309 1.00 19.21 ? 214 VAL A CA 1 ATOM 1323 C C . VAL A 1 173 ? 16.515 49.735 26.764 1.00 19.95 ? 214 VAL A C 1 ATOM 1324 O O . VAL A 1 173 ? 16.274 49.858 25.540 1.00 20.08 ? 214 VAL A O 1 ATOM 1325 C CB . VAL A 1 173 ? 16.244 47.466 27.923 1.00 20.48 ? 214 VAL A CB 1 ATOM 1326 C CG1 . VAL A 1 173 ? 15.037 47.210 26.968 1.00 21.05 ? 214 VAL A CG1 1 ATOM 1327 C CG2 . VAL A 1 173 ? 17.039 46.148 28.281 1.00 18.64 ? 214 VAL A CG2 1 ATOM 1328 N N . LYS A 1 174 ? 16.211 50.688 27.654 1.00 18.20 ? 215 LYS A N 1 ATOM 1329 C CA . LYS A 1 174 ? 15.564 51.926 27.206 1.00 19.25 ? 215 LYS A CA 1 ATOM 1330 C C . LYS A 1 174 ? 16.503 52.609 26.217 1.00 19.43 ? 215 LYS A C 1 ATOM 1331 O O . LYS A 1 174 ? 16.062 53.073 25.135 1.00 20.40 ? 215 LYS A O 1 ATOM 1332 C CB . LYS A 1 174 ? 15.373 52.864 28.383 1.00 18.22 ? 215 LYS A CB 1 ATOM 1333 C CG . LYS A 1 174 ? 14.669 54.169 28.007 1.00 22.18 ? 215 LYS A CG 1 ATOM 1334 C CD . LYS A 1 174 ? 14.493 55.073 29.242 1.00 24.56 ? 215 LYS A CD 1 ATOM 1335 C CE . LYS A 1 174 ? 14.222 56.514 28.785 1.00 31.94 ? 215 LYS A CE 1 ATOM 1336 N NZ . LYS A 1 174 ? 14.076 57.491 29.934 1.00 39.46 ? 215 LYS A NZ 1 ATOM 1337 N N . ASN A 1 175 ? 17.781 52.674 26.575 1.00 20.28 ? 216 ASN A N 1 ATOM 1338 C CA . ASN A 1 175 ? 18.796 53.323 25.703 1.00 19.25 ? 216 ASN A CA 1 ATOM 1339 C C . ASN A 1 175 ? 18.893 52.617 24.337 1.00 20.17 ? 216 ASN A C 1 ATOM 1340 O O . ASN A 1 175 ? 18.920 53.290 23.317 1.00 22.23 ? 216 ASN A O 1 ATOM 1341 C CB . ASN A 1 175 ? 20.185 53.381 26.363 1.00 18.99 ? 216 ASN A CB 1 ATOM 1342 C CG . ASN A 1 175 ? 20.185 54.218 27.642 1.00 19.48 ? 216 ASN A CG 1 ATOM 1343 O OD1 . ASN A 1 175 ? 19.236 54.996 27.890 1.00 21.36 ? 216 ASN A OD1 1 ATOM 1344 N ND2 . ASN A 1 175 ? 21.238 54.099 28.432 1.00 19.00 ? 216 ASN A ND2 1 ATOM 1345 N N . ALA A 1 176 ? 18.913 51.285 24.346 1.00 20.16 ? 217 ALA A N 1 ATOM 1346 C CA . ALA A 1 176 ? 18.973 50.527 23.048 1.00 21.52 ? 217 ALA A CA 1 ATOM 1347 C C . ALA A 1 176 ? 17.712 50.778 22.211 1.00 23.09 ? 217 ALA A C 1 ATOM 1348 O O . ALA A 1 176 ? 17.786 50.909 20.967 1.00 24.39 ? 217 ALA A O 1 ATOM 1349 C CB . ALA A 1 176 ? 19.148 49.022 23.304 1.00 21.37 ? 217 ALA A CB 1 ATOM 1350 N N . GLN A 1 177 ? 16.540 50.780 22.860 1.00 24.12 ? 218 GLN A N 1 ATOM 1351 C CA . GLN A 1 177 ? 15.284 51.021 22.134 1.00 26.05 ? 218 GLN A CA 1 ATOM 1352 C C . GLN A 1 177 ? 15.318 52.366 21.472 1.00 27.14 ? 218 GLN A C 1 ATOM 1353 O O . GLN A 1 177 ? 14.947 52.506 20.308 1.00 27.79 ? 218 GLN A O 1 ATOM 1354 C CB . GLN A 1 177 ? 14.085 51.047 23.074 1.00 27.07 ? 218 GLN A CB 1 ATOM 1355 C CG . GLN A 1 177 ? 13.682 49.745 23.482 1.00 29.66 ? 218 GLN A CG 1 ATOM 1356 C CD . GLN A 1 177 ? 12.344 49.750 24.272 1.00 32.68 ? 218 GLN A CD 1 ATOM 1357 O OE1 . GLN A 1 177 ? 12.085 48.810 24.970 1.00 35.16 ? 218 GLN A OE1 1 ATOM 1358 N NE2 . GLN A 1 177 ? 11.513 50.789 24.110 1.00 36.90 ? 218 GLN A NE2 1 ATOM 1359 N N . LEU A 1 178 ? 15.733 53.380 22.220 1.00 26.47 ? 219 LEU A N 1 ATOM 1360 C CA . LEU A 1 178 ? 15.758 54.719 21.646 1.00 28.20 ? 219 LEU A CA 1 ATOM 1361 C C . LEU A 1 178 ? 16.790 54.871 20.525 1.00 28.89 ? 219 LEU A C 1 ATOM 1362 O O . LEU A 1 178 ? 16.593 55.709 19.628 1.00 29.65 ? 219 LEU A O 1 ATOM 1363 C CB . LEU A 1 178 ? 15.919 55.791 22.704 1.00 28.72 ? 219 LEU A CB 1 ATOM 1364 C CG . LEU A 1 178 ? 14.714 55.810 23.672 1.00 33.64 ? 219 LEU A CG 1 ATOM 1365 C CD1 . LEU A 1 178 ? 14.908 56.866 24.737 1.00 37.34 ? 219 LEU A CD1 1 ATOM 1366 C CD2 . LEU A 1 178 ? 13.335 55.959 23.008 1.00 37.30 ? 219 LEU A CD2 1 ATOM 1367 N N . ALA A 1 179 ? 17.865 54.072 20.558 1.00 27.17 ? 220 ALA A N 1 ATOM 1368 C CA . ALA A 1 179 ? 18.822 54.002 19.434 1.00 27.87 ? 220 ALA A CA 1 ATOM 1369 C C . ALA A 1 179 ? 18.264 53.216 18.247 1.00 28.12 ? 220 ALA A C 1 ATOM 1370 O O . ALA A 1 179 ? 18.939 53.105 17.229 1.00 29.91 ? 220 ALA A O 1 ATOM 1371 C CB . ALA A 1 179 ? 20.104 53.360 19.892 1.00 27.24 ? 220 ALA A CB 1 ATOM 1372 N N . GLY A 1 180 ? 17.076 52.644 18.379 1.00 26.90 ? 221 GLY A N 1 ATOM 1373 C CA . GLY A 1 180 ? 16.457 51.908 17.267 1.00 26.32 ? 221 GLY A CA 1 ATOM 1374 C C . GLY A 1 180 ? 16.802 50.428 17.161 1.00 26.85 ? 221 GLY A C 1 ATOM 1375 O O . GLY A 1 180 ? 16.528 49.786 16.127 1.00 27.94 ? 221 GLY A O 1 ATOM 1376 N N . ALA A 1 181 ? 17.403 49.854 18.208 1.00 26.07 ? 222 ALA A N 1 ATOM 1377 C CA . ALA A 1 181 ? 17.716 48.420 18.198 1.00 26.53 ? 222 ALA A CA 1 ATOM 1378 C C . ALA A 1 181 ? 16.455 47.585 18.038 1.00 26.03 ? 222 ALA A C 1 ATOM 1379 O O . ALA A 1 181 ? 15.366 48.021 18.430 1.00 25.96 ? 222 ALA A O 1 ATOM 1380 C CB . ALA A 1 181 ? 18.449 48.037 19.498 1.00 26.39 ? 222 ALA A CB 1 ATOM 1381 N N . LYS A 1 182 ? 16.592 46.380 17.469 1.00 25.70 ? 223 LYS A N 1 ATOM 1382 C CA . LYS A 1 182 ? 15.444 45.499 17.376 1.00 26.04 ? 223 LYS A CA 1 ATOM 1383 C C . LYS A 1 182 ? 15.528 44.349 18.364 1.00 25.04 ? 223 LYS A C 1 ATOM 1384 O O . LYS A 1 182 ? 14.626 43.540 18.424 1.00 25.40 ? 223 LYS A O 1 ATOM 1385 C CB . LYS A 1 182 ? 15.226 45.024 15.922 1.00 29.12 ? 223 LYS A CB 1 ATOM 1386 C CG . LYS A 1 182 ? 16.154 43.991 15.415 1.00 31.30 ? 223 LYS A CG 1 ATOM 1387 C CD . LYS A 1 182 ? 15.627 43.542 14.028 1.00 35.72 ? 223 LYS A CD 1 ATOM 1388 C CE . LYS A 1 182 ? 16.675 42.845 13.244 1.00 38.97 ? 223 LYS A CE 1 ATOM 1389 N NZ . LYS A 1 182 ? 16.133 42.528 11.865 1.00 40.85 ? 223 LYS A NZ 1 ATOM 1390 N N . GLY A 1 183 ? 16.599 44.308 19.165 1.00 24.60 ? 224 GLY A N 1 ATOM 1391 C CA . GLY A 1 183 ? 16.698 43.320 20.260 1.00 22.82 ? 224 GLY A CA 1 ATOM 1392 C C . GLY A 1 183 ? 17.929 43.639 21.066 1.00 23.36 ? 224 GLY A C 1 ATOM 1393 O O . GLY A 1 183 ? 18.807 44.363 20.603 1.00 23.27 ? 224 GLY A O 1 ATOM 1394 N N . VAL A 1 184 ? 18.010 43.107 22.285 1.00 22.28 ? 225 VAL A N 1 ATOM 1395 C CA . VAL A 1 184 ? 19.172 43.369 23.117 1.00 21.50 ? 225 VAL A CA 1 ATOM 1396 C C . VAL A 1 184 ? 19.620 42.036 23.723 1.00 21.22 ? 225 VAL A C 1 ATOM 1397 O O . VAL A 1 184 ? 18.799 41.271 24.237 1.00 21.35 ? 225 VAL A O 1 ATOM 1398 C CB . VAL A 1 184 ? 18.810 44.297 24.333 1.00 22.56 ? 225 VAL A CB 1 ATOM 1399 C CG1 . VAL A 1 184 ? 20.050 44.585 25.134 1.00 23.66 ? 225 VAL A CG1 1 ATOM 1400 C CG2 . VAL A 1 184 ? 18.156 45.608 23.852 1.00 23.48 ? 225 VAL A CG2 1 ATOM 1401 N N . ILE A 1 185 ? 20.910 41.764 23.663 1.00 22.07 ? 226 ILE A N 1 ATOM 1402 C CA . ILE A 1 185 ? 21.503 40.618 24.358 1.00 21.99 ? 226 ILE A CA 1 ATOM 1403 C C . ILE A 1 185 ? 22.364 41.192 25.478 1.00 21.79 ? 226 ILE A C 1 ATOM 1404 O O . ILE A 1 185 ? 23.234 42.010 25.206 1.00 22.47 ? 226 ILE A O 1 ATOM 1405 C CB . ILE A 1 185 ? 22.343 39.783 23.358 1.00 23.80 ? 226 ILE A CB 1 ATOM 1406 C CG1 . ILE A 1 185 ? 21.417 39.252 22.273 1.00 24.12 ? 226 ILE A CG1 1 ATOM 1407 C CG2 . ILE A 1 185 ? 23.114 38.674 24.085 1.00 23.33 ? 226 ILE A CG2 1 ATOM 1408 C CD1 . ILE A 1 185 ? 22.219 38.679 21.042 1.00 25.94 ? 226 ILE A CD1 1 ATOM 1409 N N . LEU A 1 186 ? 22.102 40.778 26.728 1.00 21.07 ? 227 LEU A N 1 ATOM 1410 C CA . LEU A 1 186 ? 22.898 41.220 27.880 1.00 20.25 ? 227 LEU A CA 1 ATOM 1411 C C . LEU A 1 186 ? 23.794 40.080 28.261 1.00 19.60 ? 227 LEU A C 1 ATOM 1412 O O . LEU A 1 186 ? 23.352 38.917 28.202 1.00 20.90 ? 227 LEU A O 1 ATOM 1413 C CB . LEU A 1 186 ? 21.956 41.527 29.073 1.00 19.77 ? 227 LEU A CB 1 ATOM 1414 C CG . LEU A 1 186 ? 20.925 42.642 28.792 1.00 19.57 ? 227 LEU A CG 1 ATOM 1415 C CD1 . LEU A 1 186 ? 19.823 42.682 29.931 1.00 20.66 ? 227 LEU A CD1 1 ATOM 1416 C CD2 . LEU A 1 186 ? 21.617 43.980 28.754 1.00 20.41 ? 227 LEU A CD2 1 ATOM 1417 N N . TYR A 1 187 ? 25.048 40.367 28.628 1.00 20.20 ? 228 TYR A N 1 ATOM 1418 C CA . TYR A 1 187 ? 25.909 39.270 29.081 1.00 20.73 ? 228 TYR A CA 1 ATOM 1419 C C . TYR A 1 187 ? 26.827 39.729 30.185 1.00 20.83 ? 228 TYR A C 1 ATOM 1420 O O . TYR A 1 187 ? 27.097 40.945 30.298 1.00 21.94 ? 228 TYR A O 1 ATOM 1421 C CB . TYR A 1 187 ? 26.745 38.647 27.910 1.00 20.75 ? 228 TYR A CB 1 ATOM 1422 C CG . TYR A 1 187 ? 27.983 39.442 27.593 1.00 19.62 ? 228 TYR A CG 1 ATOM 1423 C CD1 . TYR A 1 187 ? 29.219 39.078 28.142 1.00 20.69 ? 228 TYR A CD1 1 ATOM 1424 C CD2 . TYR A 1 187 ? 27.908 40.581 26.784 1.00 20.73 ? 228 TYR A CD2 1 ATOM 1425 C CE1 . TYR A 1 187 ? 30.395 39.844 27.866 1.00 20.50 ? 228 TYR A CE1 1 ATOM 1426 C CE2 . TYR A 1 187 ? 29.051 41.353 26.523 1.00 19.88 ? 228 TYR A CE2 1 ATOM 1427 C CZ . TYR A 1 187 ? 30.277 40.975 27.068 1.00 21.76 ? 228 TYR A CZ 1 ATOM 1428 O OH . TYR A 1 187 ? 31.378 41.759 26.839 1.00 23.35 ? 228 TYR A OH 1 ATOM 1429 N N . SER A 1 188 ? 27.328 38.777 30.983 1.00 20.64 ? 229 SER A N 1 ATOM 1430 C CA . SER A 1 188 ? 28.240 39.069 32.074 1.00 21.04 ? 229 SER A CA 1 ATOM 1431 C C . SER A 1 188 ? 29.692 38.927 31.617 1.00 20.87 ? 229 SER A C 1 ATOM 1432 O O . SER A 1 188 ? 30.141 37.809 31.365 1.00 21.97 ? 229 SER A O 1 ATOM 1433 C CB . SER A 1 188 ? 27.942 38.158 33.296 1.00 20.50 ? 229 SER A CB 1 ATOM 1434 O OG . SER A 1 188 ? 26.599 38.386 33.776 1.00 22.01 ? 229 SER A OG 1 ATOM 1435 N N . ASP A 1 189 ? 30.401 40.033 31.528 1.00 21.33 ? 230 ASP A N 1 ATOM 1436 C CA . ASP A 1 189 ? 31.834 39.949 31.139 1.00 23.12 ? 230 ASP A CA 1 ATOM 1437 C C . ASP A 1 189 ? 32.672 39.617 32.379 1.00 23.44 ? 230 ASP A C 1 ATOM 1438 O O . ASP A 1 189 ? 32.451 40.172 33.442 1.00 23.51 ? 230 ASP A O 1 ATOM 1439 C CB . ASP A 1 189 ? 32.293 41.254 30.466 1.00 23.83 ? 230 ASP A CB 1 ATOM 1440 C CG . ASP A 1 189 ? 33.614 41.092 29.681 1.00 25.72 ? 230 ASP A CG 1 ATOM 1441 O OD1 . ASP A 1 189 ? 33.528 41.102 28.445 1.00 24.99 ? 230 ASP A OD1 1 ATOM 1442 O OD2 . ASP A 1 189 ? 34.691 40.928 30.299 1.00 24.37 ? 230 ASP A OD2 1 ATOM 1443 N N . PRO A 1 190 ? 33.681 38.731 32.254 1.00 24.30 ? 231 PRO A N 1 ATOM 1444 C CA . PRO A 1 190 ? 34.558 38.487 33.391 1.00 24.95 ? 231 PRO A CA 1 ATOM 1445 C C . PRO A 1 190 ? 35.231 39.753 33.924 1.00 26.30 ? 231 PRO A C 1 ATOM 1446 O O . PRO A 1 190 ? 35.533 39.824 35.129 1.00 26.36 ? 231 PRO A O 1 ATOM 1447 C CB . PRO A 1 190 ? 35.630 37.536 32.820 1.00 25.59 ? 231 PRO A CB 1 ATOM 1448 C CG . PRO A 1 190 ? 34.994 36.892 31.698 1.00 27.22 ? 231 PRO A CG 1 ATOM 1449 C CD . PRO A 1 190 ? 34.007 37.854 31.102 1.00 24.72 ? 231 PRO A CD 1 ATOM 1450 N N . ALA A 1 191 ? 35.432 40.761 33.073 1.00 26.03 ? 232 ALA A N 1 ATOM 1451 C CA . ALA A 1 191 ? 35.956 42.033 33.577 1.00 27.36 ? 232 ALA A CA 1 ATOM 1452 C C . ALA A 1 191 ? 35.116 42.592 34.753 1.00 26.78 ? 232 ALA A C 1 ATOM 1453 O O . ALA A 1 191 ? 35.650 43.213 35.694 1.00 28.83 ? 232 ALA A O 1 ATOM 1454 C CB . ALA A 1 191 ? 36.046 43.052 32.442 1.00 27.64 ? 232 ALA A CB 1 ATOM 1455 N N . ASP A 1 192 ? 33.808 42.355 34.724 1.00 26.15 ? 233 ASP A N 1 ATOM 1456 C CA . ASP A 1 192 ? 32.871 42.976 35.666 1.00 25.34 ? 233 ASP A CA 1 ATOM 1457 C C . ASP A 1 192 ? 32.326 41.958 36.658 1.00 24.94 ? 233 ASP A C 1 ATOM 1458 O O . ASP A 1 192 ? 31.706 42.343 37.665 1.00 26.35 ? 233 ASP A O 1 ATOM 1459 C CB . ASP A 1 192 ? 31.719 43.551 34.839 1.00 25.24 ? 233 ASP A CB 1 ATOM 1460 C CG . ASP A 1 192 ? 32.218 44.506 33.759 1.00 24.00 ? 233 ASP A CG 1 ATOM 1461 O OD1 . ASP A 1 192 ? 32.680 45.607 34.143 1.00 26.80 ? 233 ASP A OD1 1 ATOM 1462 O OD2 . ASP A 1 192 ? 32.163 44.140 32.547 1.00 24.18 ? 233 ASP A OD2 1 ATOM 1463 N N . TYR A 1 193 ? 32.539 40.665 36.419 1.00 24.50 ? 234 TYR A N 1 ATOM 1464 C CA . TYR A 1 193 ? 31.972 39.633 37.287 1.00 23.72 ? 234 TYR A CA 1 ATOM 1465 C C . TYR A 1 193 ? 32.934 38.495 37.656 1.00 25.13 ? 234 TYR A C 1 ATOM 1466 O O . TYR A 1 193 ? 32.489 37.425 38.095 1.00 24.69 ? 234 TYR A O 1 ATOM 1467 C CB . TYR A 1 193 ? 30.694 39.049 36.650 1.00 24.49 ? 234 TYR A CB 1 ATOM 1468 C CG . TYR A 1 193 ? 29.628 40.129 36.541 1.00 23.09 ? 234 TYR A CG 1 ATOM 1469 C CD1 . TYR A 1 193 ? 29.499 40.892 35.366 1.00 24.02 ? 234 TYR A CD1 1 ATOM 1470 C CD2 . TYR A 1 193 ? 28.819 40.449 37.645 1.00 22.15 ? 234 TYR A CD2 1 ATOM 1471 C CE1 . TYR A 1 193 ? 28.546 41.948 35.299 1.00 22.67 ? 234 TYR A CE1 1 ATOM 1472 C CE2 . TYR A 1 193 ? 27.874 41.470 37.580 1.00 24.03 ? 234 TYR A CE2 1 ATOM 1473 C CZ . TYR A 1 193 ? 27.741 42.197 36.401 1.00 24.69 ? 234 TYR A CZ 1 ATOM 1474 O OH . TYR A 1 193 ? 26.842 43.215 36.327 1.00 22.84 ? 234 TYR A OH 1 ATOM 1475 N N . PHE A 1 194 ? 34.246 38.709 37.467 1.00 25.07 ? 235 PHE A N 1 ATOM 1476 C CA . PHE A 1 194 ? 35.192 37.658 37.847 1.00 27.03 ? 235 PHE A CA 1 ATOM 1477 C C . PHE A 1 194 ? 36.383 38.367 38.499 1.00 28.28 ? 235 PHE A C 1 ATOM 1478 O O . PHE A 1 194 ? 37.166 39.016 37.807 1.00 29.79 ? 235 PHE A O 1 ATOM 1479 C CB . PHE A 1 194 ? 35.656 36.881 36.618 1.00 27.95 ? 235 PHE A CB 1 ATOM 1480 C CG . PHE A 1 194 ? 36.423 35.630 36.956 1.00 26.21 ? 235 PHE A CG 1 ATOM 1481 C CD1 . PHE A 1 194 ? 35.775 34.391 37.001 1.00 27.09 ? 235 PHE A CD1 1 ATOM 1482 C CD2 . PHE A 1 194 ? 37.787 35.691 37.223 1.00 28.90 ? 235 PHE A CD2 1 ATOM 1483 C CE1 . PHE A 1 194 ? 36.482 33.219 37.315 1.00 27.60 ? 235 PHE A CE1 1 ATOM 1484 C CE2 . PHE A 1 194 ? 38.488 34.520 37.553 1.00 25.79 ? 235 PHE A CE2 1 ATOM 1485 C CZ . PHE A 1 194 ? 37.835 33.286 37.601 1.00 28.06 ? 235 PHE A CZ 1 ATOM 1486 N N . ALA A 1 195 ? 36.485 38.273 39.820 1.00 27.87 ? 236 ALA A N 1 ATOM 1487 C CA . ALA A 1 195 ? 37.562 38.928 40.552 1.00 29.37 ? 236 ALA A CA 1 ATOM 1488 C C . ALA A 1 195 ? 38.855 38.133 40.311 1.00 31.36 ? 236 ALA A C 1 ATOM 1489 O O . ALA A 1 195 ? 38.869 36.922 40.483 1.00 30.87 ? 236 ALA A O 1 ATOM 1490 C CB . ALA A 1 195 ? 37.234 38.968 42.029 1.00 29.52 ? 236 ALA A CB 1 ATOM 1491 N N . PRO A 1 196 ? 39.929 38.822 39.904 1.00 33.18 ? 237 PRO A N 1 ATOM 1492 C CA . PRO A 1 196 ? 41.219 38.137 39.696 1.00 34.04 ? 237 PRO A CA 1 ATOM 1493 C C . PRO A 1 196 ? 41.642 37.353 40.944 1.00 33.52 ? 237 PRO A C 1 ATOM 1494 O O . PRO A 1 196 ? 41.504 37.829 42.089 1.00 33.74 ? 237 PRO A O 1 ATOM 1495 C CB . PRO A 1 196 ? 42.173 39.306 39.417 1.00 35.66 ? 237 PRO A CB 1 ATOM 1496 C CG . PRO A 1 196 ? 41.269 40.306 38.693 1.00 36.19 ? 237 PRO A CG 1 ATOM 1497 C CD . PRO A 1 196 ? 40.016 40.254 39.557 1.00 33.98 ? 237 PRO A CD 1 ATOM 1498 N N . GLY A 1 197 ? 42.110 36.121 40.726 1.00 33.88 ? 238 GLY A N 1 ATOM 1499 C CA . GLY A 1 197 ? 42.671 35.340 41.801 1.00 32.87 ? 238 GLY A CA 1 ATOM 1500 C C . GLY A 1 197 ? 41.726 34.570 42.678 1.00 33.68 ? 238 GLY A C 1 ATOM 1501 O O . GLY A 1 197 ? 42.167 33.994 43.683 1.00 34.98 ? 238 GLY A O 1 ATOM 1502 N N . VAL A 1 198 ? 40.428 34.554 42.322 1.00 30.31 ? 239 VAL A N 1 ATOM 1503 C CA . VAL A 1 198 ? 39.401 33.810 43.054 1.00 28.84 ? 239 VAL A CA 1 ATOM 1504 C C . VAL A 1 198 ? 38.771 32.806 42.092 1.00 27.60 ? 239 VAL A C 1 ATOM 1505 O O . VAL A 1 198 ? 38.707 33.045 40.886 1.00 28.08 ? 239 VAL A O 1 ATOM 1506 C CB . VAL A 1 198 ? 38.345 34.795 43.752 1.00 28.99 ? 239 VAL A CB 1 ATOM 1507 C CG1 A VAL A 1 198 ? 38.831 36.250 43.693 0.50 27.94 ? 239 VAL A CG1 1 ATOM 1508 C CG1 B VAL A 1 198 ? 37.135 34.029 44.320 0.50 26.37 ? 239 VAL A CG1 1 ATOM 1509 C CG2 A VAL A 1 198 ? 36.935 34.573 43.298 0.50 28.44 ? 239 VAL A CG2 1 ATOM 1510 C CG2 B VAL A 1 198 ? 38.996 35.677 44.829 0.50 26.72 ? 239 VAL A CG2 1 ATOM 1511 N N . LYS A 1 199 ? 38.321 31.688 42.627 1.00 27.91 ? 240 LYS A N 1 ATOM 1512 C CA . LYS A 1 199 ? 37.816 30.617 41.806 1.00 28.96 ? 240 LYS A CA 1 ATOM 1513 C C . LYS A 1 199 ? 36.310 30.792 41.601 1.00 29.31 ? 240 LYS A C 1 ATOM 1514 O O . LYS A 1 199 ? 35.653 31.412 42.427 1.00 29.77 ? 240 LYS A O 1 ATOM 1515 C CB . LYS A 1 199 ? 38.054 29.276 42.505 1.00 29.72 ? 240 LYS A CB 1 ATOM 1516 C CG . LYS A 1 199 ? 39.560 28.772 42.423 1.00 32.43 ? 240 LYS A CG 1 ATOM 1517 C CD . LYS A 1 199 ? 40.070 28.743 40.971 1.00 38.43 ? 240 LYS A CD 1 ATOM 1518 C CE . LYS A 1 199 ? 41.540 28.205 40.868 1.00 43.32 ? 240 LYS A CE 1 ATOM 1519 N NZ . LYS A 1 199 ? 42.145 28.276 39.467 1.00 45.61 ? 240 LYS A NZ 1 ATOM 1520 N N . SER A 1 200 ? 35.816 30.222 40.507 1.00 29.46 ? 241 SER A N 1 ATOM 1521 C CA . SER A 1 200 ? 34.403 30.171 40.149 1.00 29.01 ? 241 SER A CA 1 ATOM 1522 C C . SER A 1 200 ? 33.658 29.292 41.117 1.00 28.34 ? 241 SER A C 1 ATOM 1523 O O . SER A 1 200 ? 34.217 28.293 41.609 1.00 28.09 ? 241 SER A O 1 ATOM 1524 C CB . SER A 1 200 ? 34.260 29.472 38.788 1.00 31.49 ? 241 SER A CB 1 ATOM 1525 O OG . SER A 1 200 ? 34.730 30.252 37.733 1.00 35.10 ? 241 SER A OG 1 ATOM 1526 N N . TYR A 1 201 ? 32.368 29.584 41.332 1.00 25.74 ? 242 TYR A N 1 ATOM 1527 C CA . TYR A 1 201 ? 31.533 28.711 42.111 1.00 24.93 ? 242 TYR A CA 1 ATOM 1528 C C . TYR A 1 201 ? 31.578 27.295 41.503 1.00 25.30 ? 242 TYR A C 1 ATOM 1529 O O . TYR A 1 201 ? 31.499 27.175 40.292 1.00 25.73 ? 242 TYR A O 1 ATOM 1530 C CB . TYR A 1 201 ? 30.076 29.250 42.101 1.00 24.67 ? 242 TYR A CB 1 ATOM 1531 C CG . TYR A 1 201 ? 29.351 28.693 43.271 1.00 22.56 ? 242 TYR A CG 1 ATOM 1532 C CD1 . TYR A 1 201 ? 29.654 29.125 44.563 1.00 23.63 ? 242 TYR A CD1 1 ATOM 1533 C CD2 . TYR A 1 201 ? 28.472 27.621 43.104 1.00 24.55 ? 242 TYR A CD2 1 ATOM 1534 C CE1 . TYR A 1 201 ? 29.071 28.529 45.655 1.00 24.83 ? 242 TYR A CE1 1 ATOM 1535 C CE2 . TYR A 1 201 ? 27.862 27.032 44.192 1.00 24.29 ? 242 TYR A CE2 1 ATOM 1536 C CZ . TYR A 1 201 ? 28.166 27.517 45.469 1.00 25.92 ? 242 TYR A CZ 1 ATOM 1537 O OH . TYR A 1 201 ? 27.598 26.894 46.517 1.00 30.23 ? 242 TYR A OH 1 ATOM 1538 N N . PRO A 1 202 ? 31.651 26.224 42.328 1.00 26.25 ? 243 PRO A N 1 ATOM 1539 C CA . PRO A 1 202 ? 31.516 26.090 43.795 1.00 26.18 ? 243 PRO A CA 1 ATOM 1540 C C . PRO A 1 202 ? 32.796 26.245 44.612 1.00 27.60 ? 243 PRO A C 1 ATOM 1541 O O . PRO A 1 202 ? 32.749 26.129 45.838 1.00 28.77 ? 243 PRO A O 1 ATOM 1542 C CB . PRO A 1 202 ? 30.949 24.685 43.971 1.00 26.75 ? 243 PRO A CB 1 ATOM 1543 C CG . PRO A 1 202 ? 31.630 23.896 42.817 1.00 26.89 ? 243 PRO A CG 1 ATOM 1544 C CD . PRO A 1 202 ? 31.704 24.895 41.661 1.00 26.88 ? 243 PRO A CD 1 ATOM 1545 N N . ASP A 1 203 ? 33.894 26.543 43.949 1.00 27.44 ? 244 ASP A N 1 ATOM 1546 C CA . ASP A 1 203 ? 35.176 26.580 44.626 1.00 29.59 ? 244 ASP A CA 1 ATOM 1547 C C . ASP A 1 203 ? 35.567 27.969 45.086 1.00 28.99 ? 244 ASP A C 1 ATOM 1548 O O . ASP A 1 203 ? 36.560 28.134 45.789 1.00 28.79 ? 244 ASP A O 1 ATOM 1549 C CB . ASP A 1 203 ? 36.236 25.990 43.718 1.00 30.46 ? 244 ASP A CB 1 ATOM 1550 C CG . ASP A 1 203 ? 35.890 24.559 43.292 1.00 34.86 ? 244 ASP A CG 1 ATOM 1551 O OD1 . ASP A 1 203 ? 35.554 23.715 44.178 1.00 37.91 ? 244 ASP A OD1 1 ATOM 1552 O OD2 . ASP A 1 203 ? 35.863 24.313 42.067 1.00 42.47 ? 244 ASP A OD2 1 ATOM 1553 N N . GLY A 1 204 ? 34.770 28.978 44.716 1.00 27.64 ? 245 GLY A N 1 ATOM 1554 C CA . GLY A 1 204 ? 35.000 30.326 45.192 1.00 26.59 ? 245 GLY A CA 1 ATOM 1555 C C . GLY A 1 204 ? 33.750 31.087 44.853 1.00 26.20 ? 245 GLY A C 1 ATOM 1556 O O . GLY A 1 204 ? 32.706 30.475 44.554 1.00 27.56 ? 245 GLY A O 1 ATOM 1557 N N . TRP A 1 205 ? 33.854 32.408 44.924 1.00 25.05 ? 246 TRP A N 1 ATOM 1558 C CA . TRP A 1 205 ? 32.642 33.243 44.800 1.00 23.53 ? 246 TRP A CA 1 ATOM 1559 C C . TRP A 1 205 ? 32.497 33.940 43.450 1.00 23.99 ? 246 TRP A C 1 ATOM 1560 O O . TRP A 1 205 ? 31.599 34.815 43.273 1.00 22.42 ? 246 TRP A O 1 ATOM 1561 C CB . TRP A 1 205 ? 32.543 34.221 45.989 1.00 23.71 ? 246 TRP A CB 1 ATOM 1562 C CG . TRP A 1 205 ? 33.810 34.971 46.342 1.00 26.79 ? 246 TRP A CG 1 ATOM 1563 C CD1 . TRP A 1 205 ? 34.761 34.591 47.255 1.00 30.17 ? 246 TRP A CD1 1 ATOM 1564 C CD2 . TRP A 1 205 ? 34.236 36.227 45.813 1.00 26.20 ? 246 TRP A CD2 1 ATOM 1565 N NE1 . TRP A 1 205 ? 35.752 35.552 47.332 1.00 29.31 ? 246 TRP A NE1 1 ATOM 1566 C CE2 . TRP A 1 205 ? 35.454 36.562 46.454 1.00 26.21 ? 246 TRP A CE2 1 ATOM 1567 C CE3 . TRP A 1 205 ? 33.706 37.106 44.854 1.00 25.77 ? 246 TRP A CE3 1 ATOM 1568 C CZ2 . TRP A 1 205 ? 36.156 37.723 46.162 1.00 25.44 ? 246 TRP A CZ2 1 ATOM 1569 C CZ3 . TRP A 1 205 ? 34.392 38.279 44.565 1.00 27.48 ? 246 TRP A CZ3 1 ATOM 1570 C CH2 . TRP A 1 205 ? 35.620 38.584 45.223 1.00 26.25 ? 246 TRP A CH2 1 ATOM 1571 N N . ASN A 1 206 ? 33.291 33.534 42.464 1.00 23.02 ? 247 ASN A N 1 ATOM 1572 C CA . ASN A 1 206 ? 33.206 34.078 41.094 1.00 23.43 ? 247 ASN A CA 1 ATOM 1573 C C . ASN A 1 206 ? 32.148 33.455 40.210 1.00 22.57 ? 247 ASN A C 1 ATOM 1574 O O . ASN A 1 206 ? 31.709 32.350 40.479 1.00 22.40 ? 247 ASN A O 1 ATOM 1575 C CB . ASN A 1 206 ? 34.574 33.982 40.380 1.00 24.39 ? 247 ASN A CB 1 ATOM 1576 C CG . ASN A 1 206 ? 35.405 35.218 40.598 1.00 25.89 ? 247 ASN A CG 1 ATOM 1577 O OD1 . ASN A 1 206 ? 34.892 36.276 41.071 1.00 24.55 ? 247 ASN A OD1 1 ATOM 1578 N ND2 . ASN A 1 206 ? 36.720 35.112 40.297 1.00 25.96 ? 247 ASN A ND2 1 ATOM 1579 N N . LEU A 1 207 ? 31.737 34.190 39.165 1.00 23.01 ? 248 LEU A N 1 ATOM 1580 C CA . LEU A 1 207 ? 30.740 33.713 38.220 1.00 22.46 ? 248 LEU A CA 1 ATOM 1581 C C . LEU A 1 207 ? 31.429 32.794 37.213 1.00 22.44 ? 248 LEU A C 1 ATOM 1582 O O . LEU A 1 207 ? 32.413 33.223 36.568 1.00 23.09 ? 248 LEU A O 1 ATOM 1583 C CB . LEU A 1 207 ? 30.157 34.896 37.437 1.00 22.45 ? 248 LEU A CB 1 ATOM 1584 C CG . LEU A 1 207 ? 28.970 34.566 36.527 1.00 21.82 ? 248 LEU A CG 1 ATOM 1585 C CD1 . LEU A 1 207 ? 27.750 34.144 37.316 1.00 20.96 ? 248 LEU A CD1 1 ATOM 1586 C CD2 . LEU A 1 207 ? 28.697 35.805 35.650 1.00 24.18 ? 248 LEU A CD2 1 ATOM 1587 N N . PRO A 1 208 ? 30.928 31.556 37.099 1.00 22.68 ? 249 PRO A N 1 ATOM 1588 C CA . PRO A 1 208 ? 31.398 30.655 36.057 1.00 22.58 ? 249 PRO A CA 1 ATOM 1589 C C . PRO A 1 208 ? 30.893 31.060 34.685 1.00 22.97 ? 249 PRO A C 1 ATOM 1590 O O . PRO A 1 208 ? 29.911 31.809 34.565 1.00 22.89 ? 249 PRO A O 1 ATOM 1591 C CB . PRO A 1 208 ? 30.787 29.304 36.445 1.00 23.22 ? 249 PRO A CB 1 ATOM 1592 C CG . PRO A 1 208 ? 29.755 29.564 37.420 1.00 24.93 ? 249 PRO A CG 1 ATOM 1593 C CD . PRO A 1 208 ? 30.000 30.901 38.031 1.00 22.79 ? 249 PRO A CD 1 ATOM 1594 N N . GLY A 1 209 ? 31.501 30.513 33.624 1.00 21.72 ? 250 GLY A N 1 ATOM 1595 C CA . GLY A 1 209 ? 31.165 30.974 32.273 1.00 22.79 ? 250 GLY A CA 1 ATOM 1596 C C . GLY A 1 209 ? 29.748 30.587 31.865 1.00 21.58 ? 250 GLY A C 1 ATOM 1597 O O . GLY A 1 209 ? 29.224 31.130 30.884 1.00 23.19 ? 250 GLY A O 1 ATOM 1598 N N . GLY A 1 210 ? 29.164 29.603 32.551 1.00 21.31 ? 251 GLY A N 1 ATOM 1599 C CA . GLY A 1 210 ? 27.764 29.173 32.300 1.00 21.00 ? 251 GLY A CA 1 ATOM 1600 C C . GLY A 1 210 ? 26.744 29.931 33.176 1.00 21.26 ? 251 GLY A C 1 ATOM 1601 O O . GLY A 1 210 ? 25.531 29.731 33.039 1.00 21.50 ? 251 GLY A O 1 ATOM 1602 N N . GLY A 1 211 ? 27.244 30.756 34.086 1.00 21.08 ? 252 GLY A N 1 ATOM 1603 C CA . GLY A 1 211 ? 26.360 31.533 35.017 1.00 20.33 ? 252 GLY A CA 1 ATOM 1604 C C . GLY A 1 211 ? 25.704 32.679 34.251 1.00 20.38 ? 252 GLY A C 1 ATOM 1605 O O . GLY A 1 211 ? 26.275 33.265 33.333 1.00 20.32 ? 252 GLY A O 1 ATOM 1606 N N . VAL A 1 212 ? 24.484 33.029 34.642 1.00 19.30 ? 253 VAL A N 1 ATOM 1607 C CA . VAL A 1 212 ? 23.747 34.099 33.969 1.00 18.39 ? 253 VAL A CA 1 ATOM 1608 C C . VAL A 1 212 ? 22.959 34.876 35.034 1.00 18.40 ? 253 VAL A C 1 ATOM 1609 O O . VAL A 1 212 ? 22.371 34.278 35.959 1.00 18.70 ? 253 VAL A O 1 ATOM 1610 C CB . VAL A 1 212 ? 22.682 33.513 32.983 1.00 18.74 ? 253 VAL A CB 1 ATOM 1611 C CG1 . VAL A 1 212 ? 22.091 34.576 32.096 1.00 20.96 ? 253 VAL A CG1 1 ATOM 1612 C CG2 . VAL A 1 212 ? 23.386 32.486 32.047 1.00 19.59 ? 253 VAL A CG2 1 ATOM 1613 N N . GLN A 1 213 ? 22.940 36.191 34.818 1.00 17.79 ? 254 GLN A N 1 ATOM 1614 C CA . GLN A 1 213 ? 22.213 37.109 35.719 1.00 16.55 ? 254 GLN A CA 1 ATOM 1615 C C . GLN A 1 213 ? 20.793 37.338 35.199 1.00 17.00 ? 254 GLN A C 1 ATOM 1616 O O . GLN A 1 213 ? 20.599 37.891 34.066 1.00 18.73 ? 254 GLN A O 1 ATOM 1617 C CB . GLN A 1 213 ? 22.975 38.439 35.740 1.00 16.86 ? 254 GLN A CB 1 ATOM 1618 C CG . GLN A 1 213 ? 22.242 39.506 36.598 1.00 15.89 ? 254 GLN A CG 1 ATOM 1619 C CD . GLN A 1 213 ? 22.814 40.907 36.382 1.00 18.70 ? 254 GLN A CD 1 ATOM 1620 O OE1 . GLN A 1 213 ? 22.084 41.909 36.431 1.00 18.75 ? 254 GLN A OE1 1 ATOM 1621 N NE2 . GLN A 1 213 ? 24.144 41.006 36.243 1.00 18.31 ? 254 GLN A NE2 1 ATOM 1622 N N . ARG A 1 214 ? 19.811 36.853 35.967 1.00 17.42 ? 255 ARG A N 1 ATOM 1623 C CA . ARG A 1 214 ? 18.375 37.158 35.730 1.00 16.79 ? 255 ARG A CA 1 ATOM 1624 C C . ARG A 1 214 ? 18.093 38.610 36.112 1.00 16.17 ? 255 ARG A C 1 ATOM 1625 O O . ARG A 1 214 ? 18.898 39.231 36.791 1.00 17.23 ? 255 ARG A O 1 ATOM 1626 C CB . ARG A 1 214 ? 17.476 36.250 36.576 1.00 15.96 ? 255 ARG A CB 1 ATOM 1627 C CG . ARG A 1 214 ? 17.463 34.787 36.063 1.00 16.37 ? 255 ARG A CG 1 ATOM 1628 C CD . ARG A 1 214 ? 17.131 33.824 37.188 1.00 17.43 ? 255 ARG A CD 1 ATOM 1629 N NE . ARG A 1 214 ? 17.364 32.427 36.785 1.00 19.31 ? 255 ARG A NE 1 ATOM 1630 C CZ . ARG A 1 214 ? 18.568 31.878 36.737 1.00 21.35 ? 255 ARG A CZ 1 ATOM 1631 N NH1 . ARG A 1 214 ? 19.654 32.607 36.988 1.00 19.55 ? 255 ARG A NH1 1 ATOM 1632 N NH2 . ARG A 1 214 ? 18.672 30.577 36.371 1.00 18.11 ? 255 ARG A NH2 1 ATOM 1633 N N . GLY A 1 215 ? 16.915 39.116 35.716 1.00 16.26 ? 256 GLY A N 1 ATOM 1634 C CA . GLY A 1 215 ? 16.502 40.442 36.207 1.00 16.35 ? 256 GLY A CA 1 ATOM 1635 C C . GLY A 1 215 ? 15.495 41.088 35.295 1.00 16.53 ? 256 GLY A C 1 ATOM 1636 O O . GLY A 1 215 ? 15.569 40.923 34.065 1.00 15.04 ? 256 GLY A O 1 ATOM 1637 N N . ASN A 1 216 ? 14.626 41.903 35.879 1.00 15.82 ? 257 ASN A N 1 ATOM 1638 C CA . ASN A 1 216 ? 13.629 42.592 35.055 1.00 15.41 ? 257 ASN A CA 1 ATOM 1639 C C . ASN A 1 216 ? 14.267 43.782 34.339 1.00 15.45 ? 257 ASN A C 1 ATOM 1640 O O . ASN A 1 216 ? 15.333 44.297 34.737 1.00 16.58 ? 257 ASN A O 1 ATOM 1641 C CB . ASN A 1 216 ? 12.397 43.055 35.871 1.00 13.53 ? 257 ASN A CB 1 ATOM 1642 C CG . ASN A 1 216 ? 12.650 44.395 36.599 1.00 11.89 ? 257 ASN A CG 1 ATOM 1643 O OD1 . ASN A 1 216 ? 12.607 45.448 35.962 1.00 15.28 ? 257 ASN A OD1 1 ATOM 1644 N ND2 . ASN A 1 216 ? 12.772 44.363 37.962 1.00 15.59 ? 257 ASN A ND2 1 ATOM 1645 N N . ILE A 1 217 ? 13.641 44.120 33.202 1.00 15.32 ? 258 ILE A N 1 ATOM 1646 C CA . ILE A 1 217 ? 14.092 45.205 32.344 1.00 15.90 ? 258 ILE A CA 1 ATOM 1647 C C . ILE A 1 217 ? 13.049 46.306 32.150 1.00 16.81 ? 258 ILE A C 1 ATOM 1648 O O . ILE A 1 217 ? 12.998 46.944 31.078 1.00 17.24 ? 258 ILE A O 1 ATOM 1649 C CB . ILE A 1 217 ? 14.524 44.647 30.963 1.00 16.08 ? 258 ILE A CB 1 ATOM 1650 C CG1 . ILE A 1 217 ? 13.436 43.705 30.433 1.00 15.59 ? 258 ILE A CG1 1 ATOM 1651 C CG2 . ILE A 1 217 ? 15.850 43.855 31.112 1.00 16.41 ? 258 ILE A CG2 1 ATOM 1652 C CD1 . ILE A 1 217 ? 13.609 43.374 28.846 1.00 20.96 ? 258 ILE A CD1 1 ATOM 1653 N N . LEU A 1 218 ? 12.237 46.538 33.184 1.00 15.82 ? 259 LEU A N 1 ATOM 1654 C CA . LEU A 1 218 ? 11.218 47.583 33.130 1.00 17.03 ? 259 LEU A CA 1 ATOM 1655 C C . LEU A 1 218 ? 11.838 48.951 33.354 1.00 15.90 ? 259 LEU A C 1 ATOM 1656 O O . LEU A 1 218 ? 12.930 49.087 33.925 1.00 16.92 ? 259 LEU A O 1 ATOM 1657 C CB . LEU A 1 218 ? 10.199 47.358 34.270 1.00 15.96 ? 259 LEU A CB 1 ATOM 1658 C CG . LEU A 1 218 ? 9.340 46.086 34.144 1.00 16.46 ? 259 LEU A CG 1 ATOM 1659 C CD1 . LEU A 1 218 ? 8.481 45.908 35.408 1.00 16.62 ? 259 LEU A CD1 1 ATOM 1660 C CD2 . LEU A 1 218 ? 8.468 46.092 32.908 1.00 17.11 ? 259 LEU A CD2 1 ATOM 1661 N N . ASN A 1 219 ? 11.062 49.982 32.965 1.00 15.66 ? 260 ASN A N 1 ATOM 1662 C CA . ASN A 1 219 ? 11.361 51.374 33.286 1.00 15.97 ? 260 ASN A CA 1 ATOM 1663 C C . ASN A 1 219 ? 10.090 51.948 33.917 1.00 14.96 ? 260 ASN A C 1 ATOM 1664 O O . ASN A 1 219 ? 9.336 52.740 33.302 1.00 15.54 ? 260 ASN A O 1 ATOM 1665 C CB . ASN A 1 219 ? 11.779 52.172 32.040 1.00 17.49 ? 260 ASN A CB 1 ATOM 1666 C CG . ASN A 1 219 ? 13.188 51.843 31.642 1.00 18.88 ? 260 ASN A CG 1 ATOM 1667 O OD1 . ASN A 1 219 ? 14.163 52.432 32.163 1.00 20.24 ? 260 ASN A OD1 1 ATOM 1668 N ND2 . ASN A 1 219 ? 13.329 50.823 30.795 1.00 18.01 ? 260 ASN A ND2 1 ATOM 1669 N N . LEU A 1 220 ? 9.850 51.540 35.151 1.00 14.76 ? 261 LEU A N 1 ATOM 1670 C CA . LEU A 1 220 ? 8.586 51.918 35.791 1.00 14.66 ? 261 LEU A CA 1 ATOM 1671 C C . LEU A 1 220 ? 8.603 53.324 36.384 1.00 14.54 ? 261 LEU A C 1 ATOM 1672 O O . LEU A 1 220 ? 7.532 53.883 36.638 1.00 13.80 ? 261 LEU A O 1 ATOM 1673 C CB . LEU A 1 220 ? 8.331 50.995 37.006 1.00 14.06 ? 261 LEU A CB 1 ATOM 1674 C CG . LEU A 1 220 ? 8.049 49.561 36.616 1.00 14.50 ? 261 LEU A CG 1 ATOM 1675 C CD1 . LEU A 1 220 ? 7.936 48.701 37.923 1.00 13.00 ? 261 LEU A CD1 1 ATOM 1676 C CD2 . LEU A 1 220 ? 6.688 49.528 35.871 1.00 15.54 ? 261 LEU A CD2 1 ATOM 1677 N N . ASN A 1 221 ? 9.801 53.868 36.639 1.00 14.21 ? 262 ASN A N 1 ATOM 1678 C CA . ASN A 1 221 ? 9.893 55.196 37.328 1.00 15.70 ? 262 ASN A CA 1 ATOM 1679 C C . ASN A 1 221 ? 8.991 55.340 38.571 1.00 15.23 ? 262 ASN A C 1 ATOM 1680 O O . ASN A 1 221 ? 8.355 56.372 38.788 1.00 15.15 ? 262 ASN A O 1 ATOM 1681 C CB . ASN A 1 221 ? 9.591 56.316 36.343 1.00 15.75 ? 262 ASN A CB 1 ATOM 1682 C CG . ASN A 1 221 ? 10.632 56.386 35.248 1.00 17.76 ? 262 ASN A CG 1 ATOM 1683 O OD1 . ASN A 1 221 ? 11.818 56.114 35.481 1.00 19.26 ? 262 ASN A OD1 1 ATOM 1684 N ND2 . ASN A 1 221 ? 10.178 56.686 34.021 1.00 20.04 ? 262 ASN A ND2 1 ATOM 1685 N N . GLY A 1 222 ? 8.906 54.278 39.341 1.00 13.50 ? 263 GLY A N 1 ATOM 1686 C CA . GLY A 1 222 ? 8.167 54.355 40.587 1.00 13.76 ? 263 GLY A CA 1 ATOM 1687 C C . GLY A 1 222 ? 6.715 53.918 40.518 1.00 14.17 ? 263 GLY A C 1 ATOM 1688 O O . GLY A 1 222 ? 6.035 53.902 41.555 1.00 14.17 ? 263 GLY A O 1 ATOM 1689 N N . ALA A 1 223 ? 6.273 53.444 39.356 1.00 12.46 ? 264 ALA A N 1 ATOM 1690 C CA . ALA A 1 223 ? 4.824 53.225 39.207 1.00 13.52 ? 264 ALA A CA 1 ATOM 1691 C C . ALA A 1 223 ? 4.256 52.013 39.949 1.00 14.17 ? 264 ALA A C 1 ATOM 1692 O O . ALA A 1 223 ? 3.027 51.995 40.211 1.00 15.56 ? 264 ALA A O 1 ATOM 1693 C CB . ALA A 1 223 ? 4.436 53.134 37.690 1.00 13.28 ? 264 ALA A CB 1 ATOM 1694 N N . GLY A 1 224 ? 5.084 51.008 40.195 1.00 13.57 ? 265 GLY A N 1 ATOM 1695 C CA . GLY A 1 224 ? 4.566 49.753 40.753 1.00 14.00 ? 265 GLY A CA 1 ATOM 1696 C C . GLY A 1 224 ? 4.024 48.849 39.650 1.00 14.80 ? 265 GLY A C 1 ATOM 1697 O O . GLY A 1 224 ? 4.512 48.844 38.512 1.00 14.92 ? 265 GLY A O 1 ATOM 1698 N N . ASP A 1 225 ? 2.956 48.102 39.978 1.00 13.03 ? 266 ASP A N 1 ATOM 1699 C CA . ASP A 1 225 ? 2.361 47.216 38.945 1.00 13.98 ? 266 ASP A CA 1 ATOM 1700 C C . ASP A 1 225 ? 2.145 47.972 37.633 1.00 14.01 ? 266 ASP A C 1 ATOM 1701 O O . ASP A 1 225 ? 1.489 49.009 37.647 1.00 15.20 ? 266 ASP A O 1 ATOM 1702 C CB . ASP A 1 225 ? 1.033 46.706 39.469 1.00 14.39 ? 266 ASP A CB 1 ATOM 1703 C CG . ASP A 1 225 ? 0.162 46.039 38.402 1.00 16.01 ? 266 ASP A CG 1 ATOM 1704 O OD1 . ASP A 1 225 ? 0.717 45.216 37.583 1.00 16.46 ? 266 ASP A OD1 1 ATOM 1705 O OD2 . ASP A 1 225 ? -1.090 46.263 38.460 1.00 16.54 ? 266 ASP A OD2 1 ATOM 1706 N N . PRO A 1 226 ? 2.653 47.437 36.502 1.00 14.80 ? 267 PRO A N 1 ATOM 1707 C CA . PRO A 1 226 ? 2.475 48.167 35.243 1.00 15.59 ? 267 PRO A CA 1 ATOM 1708 C C . PRO A 1 226 ? 1.030 48.499 34.891 1.00 15.14 ? 267 PRO A C 1 ATOM 1709 O O . PRO A 1 226 ? 0.816 49.476 34.112 1.00 16.62 ? 267 PRO A O 1 ATOM 1710 C CB . PRO A 1 226 ? 2.981 47.177 34.192 1.00 16.42 ? 267 PRO A CB 1 ATOM 1711 C CG . PRO A 1 226 ? 4.152 46.482 34.894 1.00 16.33 ? 267 PRO A CG 1 ATOM 1712 C CD . PRO A 1 226 ? 3.666 46.363 36.405 1.00 16.10 ? 267 PRO A CD 1 ATOM 1713 N N . LEU A 1 227 ? 0.081 47.697 35.378 1.00 16.14 ? 268 LEU A N 1 ATOM 1714 C CA . LEU A 1 227 ? -1.281 47.901 34.915 1.00 16.20 ? 268 LEU A CA 1 ATOM 1715 C C . LEU A 1 227 ? -2.113 48.848 35.777 1.00 15.75 ? 268 LEU A C 1 ATOM 1716 O O . LEU A 1 227 ? -3.251 49.205 35.386 1.00 15.61 ? 268 LEU A O 1 ATOM 1717 C CB . LEU A 1 227 ? -1.995 46.555 34.844 1.00 15.20 ? 268 LEU A CB 1 ATOM 1718 C CG . LEU A 1 227 ? -1.284 45.485 33.976 1.00 15.64 ? 268 LEU A CG 1 ATOM 1719 C CD1 . LEU A 1 227 ? -2.136 44.215 33.994 1.00 19.37 ? 268 LEU A CD1 1 ATOM 1720 C CD2 . LEU A 1 227 ? -1.095 45.991 32.531 1.00 18.82 ? 268 LEU A CD2 1 ATOM 1721 N N . THR A 1 228 ? -1.630 49.212 36.970 1.00 14.85 ? 269 THR A N 1 ATOM 1722 C CA . THR A 1 228 ? -2.485 49.992 37.905 1.00 15.31 ? 269 THR A CA 1 ATOM 1723 C C . THR A 1 228 ? -1.756 51.182 38.558 1.00 14.94 ? 269 THR A C 1 ATOM 1724 O O . THR A 1 228 ? -1.828 51.376 39.784 1.00 14.33 ? 269 THR A O 1 ATOM 1725 C CB . THR A 1 228 ? -2.966 49.075 39.093 1.00 14.75 ? 269 THR A CB 1 ATOM 1726 O OG1 . THR A 1 228 ? -1.845 48.437 39.748 1.00 14.72 ? 269 THR A OG1 1 ATOM 1727 C CG2 . THR A 1 228 ? -3.907 47.989 38.541 1.00 15.09 ? 269 THR A CG2 1 ATOM 1728 N N . PRO A 1 229 ? -1.065 52.000 37.759 1.00 14.46 ? 270 PRO A N 1 ATOM 1729 C CA . PRO A 1 229 ? -0.305 53.116 38.379 1.00 14.58 ? 270 PRO A CA 1 ATOM 1730 C C . PRO A 1 229 ? -1.217 54.039 39.209 1.00 14.40 ? 270 PRO A C 1 ATOM 1731 O O . PRO A 1 229 ? -2.284 54.484 38.721 1.00 17.02 ? 270 PRO A O 1 ATOM 1732 C CB . PRO A 1 229 ? 0.272 53.869 37.195 1.00 15.55 ? 270 PRO A CB 1 ATOM 1733 C CG . PRO A 1 229 ? -0.668 53.492 36.030 1.00 14.50 ? 270 PRO A CG 1 ATOM 1734 C CD . PRO A 1 229 ? -1.046 52.063 36.278 1.00 14.21 ? 270 PRO A CD 1 ATOM 1735 N N . GLY A 1 230 ? -0.818 54.291 40.463 1.00 13.85 ? 271 GLY A N 1 ATOM 1736 C CA . GLY A 1 230 ? -1.540 55.198 41.379 1.00 14.62 ? 271 GLY A CA 1 ATOM 1737 C C . GLY A 1 230 ? -2.487 54.535 42.376 1.00 15.09 ? 271 GLY A C 1 ATOM 1738 O O . GLY A 1 230 ? -2.841 55.154 43.402 1.00 16.90 ? 271 GLY A O 1 ATOM 1739 N N . TYR A 1 231 ? -2.826 53.250 42.151 1.00 13.84 ? 272 TYR A N 1 ATOM 1740 C CA . TYR A 1 231 ? -3.921 52.608 42.921 1.00 15.17 ? 272 TYR A CA 1 ATOM 1741 C C . TYR A 1 231 ? -3.537 51.132 43.146 1.00 14.64 ? 272 TYR A C 1 ATOM 1742 O O . TYR A 1 231 ? -2.878 50.492 42.293 1.00 14.76 ? 272 TYR A O 1 ATOM 1743 C CB . TYR A 1 231 ? -5.257 52.715 42.156 1.00 14.49 ? 272 TYR A CB 1 ATOM 1744 C CG . TYR A 1 231 ? -5.521 54.136 41.755 1.00 15.24 ? 272 TYR A CG 1 ATOM 1745 C CD1 . TYR A 1 231 ? -6.075 55.029 42.683 1.00 15.97 ? 272 TYR A CD1 1 ATOM 1746 C CD2 . TYR A 1 231 ? -5.161 54.617 40.486 1.00 15.15 ? 272 TYR A CD2 1 ATOM 1747 C CE1 . TYR A 1 231 ? -6.280 56.372 42.353 1.00 15.41 ? 272 TYR A CE1 1 ATOM 1748 C CE2 . TYR A 1 231 ? -5.376 55.976 40.123 1.00 15.02 ? 272 TYR A CE2 1 ATOM 1749 C CZ . TYR A 1 231 ? -5.950 56.826 41.074 1.00 14.75 ? 272 TYR A CZ 1 ATOM 1750 O OH . TYR A 1 231 ? -6.104 58.135 40.745 1.00 16.76 ? 272 TYR A OH 1 ATOM 1751 N N . PRO A 1 232 ? -3.932 50.598 44.304 1.00 15.41 ? 273 PRO A N 1 ATOM 1752 C CA . PRO A 1 232 ? -3.544 49.184 44.514 1.00 15.31 ? 273 PRO A CA 1 ATOM 1753 C C . PRO A 1 232 ? -4.242 48.207 43.608 1.00 15.96 ? 273 PRO A C 1 ATOM 1754 O O . PRO A 1 232 ? -5.446 48.390 43.320 1.00 15.93 ? 273 PRO A O 1 ATOM 1755 C CB . PRO A 1 232 ? -3.946 48.922 45.970 1.00 14.69 ? 273 PRO A CB 1 ATOM 1756 C CG . PRO A 1 232 ? -5.148 49.906 46.237 1.00 15.86 ? 273 PRO A CG 1 ATOM 1757 C CD . PRO A 1 232 ? -4.729 51.167 45.410 1.00 16.85 ? 273 PRO A CD 1 ATOM 1758 N N . ALA A 1 233 ? -3.515 47.149 43.241 1.00 15.36 ? 274 ALA A N 1 ATOM 1759 C CA . ALA A 1 233 ? -4.014 46.125 42.319 1.00 15.49 ? 274 ALA A CA 1 ATOM 1760 C C . ALA A 1 233 ? -4.875 45.112 43.129 1.00 16.71 ? 274 ALA A C 1 ATOM 1761 O O . ALA A 1 233 ? -4.533 43.923 43.286 1.00 17.07 ? 274 ALA A O 1 ATOM 1762 C CB . ALA A 1 233 ? -2.831 45.463 41.643 1.00 16.03 ? 274 ALA A CB 1 ATOM 1763 N N . ASN A 1 234 ? -5.990 45.619 43.654 1.00 17.69 ? 275 ASN A N 1 ATOM 1764 C CA . ASN A 1 234 ? -6.882 44.825 44.509 1.00 20.40 ? 275 ASN A CA 1 ATOM 1765 C C . ASN A 1 234 ? -7.893 44.077 43.633 1.00 22.19 ? 275 ASN A C 1 ATOM 1766 O O . ASN A 1 234 ? -7.721 44.033 42.407 1.00 20.30 ? 275 ASN A O 1 ATOM 1767 C CB . ASN A 1 234 ? -7.542 45.748 45.564 1.00 20.35 ? 275 ASN A CB 1 ATOM 1768 C CG . ASN A 1 234 ? -8.333 46.858 44.936 1.00 22.02 ? 275 ASN A CG 1 ATOM 1769 O OD1 . ASN A 1 234 ? -8.838 46.730 43.806 1.00 22.79 ? 275 ASN A OD1 1 ATOM 1770 N ND2 . ASN A 1 234 ? -8.483 48.001 45.675 1.00 25.71 ? 275 ASN A ND2 1 ATOM 1771 N N A GLU A 1 235 ? -8.960 43.568 44.276 0.50 23.27 ? 276 GLU A N 1 ATOM 1772 N N B GLU A 1 235 ? -8.918 43.448 44.217 0.50 23.58 ? 276 GLU A N 1 ATOM 1773 C CA A GLU A 1 235 ? -9.945 42.657 43.667 0.50 24.83 ? 276 GLU A CA 1 ATOM 1774 C CA B GLU A 1 235 ? -9.792 42.604 43.386 0.50 25.18 ? 276 GLU A CA 1 ATOM 1775 C C A GLU A 1 235 ? -10.832 43.288 42.608 0.50 24.77 ? 276 GLU A C 1 ATOM 1776 C C B GLU A 1 235 ? -10.553 43.403 42.347 0.50 25.15 ? 276 GLU A C 1 ATOM 1777 O O A GLU A 1 235 ? -11.406 42.586 41.741 0.50 25.30 ? 276 GLU A O 1 ATOM 1778 O O B GLU A 1 235 ? -10.727 42.950 41.212 0.50 26.30 ? 276 GLU A O 1 ATOM 1779 C CB A GLU A 1 235 ? -10.878 42.106 44.764 0.50 25.70 ? 276 GLU A CB 1 ATOM 1780 C CB B GLU A 1 235 ? -10.760 41.767 44.239 0.50 26.39 ? 276 GLU A CB 1 ATOM 1781 C CG A GLU A 1 235 ? -11.179 40.640 44.628 0.50 27.86 ? 276 GLU A CG 1 ATOM 1782 C CG B GLU A 1 235 ? -10.097 40.583 44.849 0.50 30.27 ? 276 GLU A CG 1 ATOM 1783 C CD A GLU A 1 235 ? -10.007 39.777 45.100 0.50 30.29 ? 276 GLU A CD 1 ATOM 1784 C CD B GLU A 1 235 ? -10.315 39.309 44.032 0.50 33.46 ? 276 GLU A CD 1 ATOM 1785 O OE1 A GLU A 1 235 ? -9.606 39.873 46.288 0.50 31.73 ? 276 GLU A OE1 1 ATOM 1786 O OE1 B GLU A 1 235 ? -10.911 39.377 42.922 0.50 33.97 ? 276 GLU A OE1 1 ATOM 1787 O OE2 A GLU A 1 235 ? -9.480 39.013 44.277 0.50 27.73 ? 276 GLU A OE2 1 ATOM 1788 O OE2 B GLU A 1 235 ? -9.891 38.234 44.509 0.50 36.03 ? 276 GLU A OE2 1 ATOM 1789 N N . TYR A 1 236 ? -11.001 44.600 42.709 1.00 23.76 ? 277 TYR A N 1 ATOM 1790 C CA . TYR A 1 236 ? -11.873 45.326 41.770 1.00 23.66 ? 277 TYR A CA 1 ATOM 1791 C C . TYR A 1 236 ? -11.117 46.320 40.934 1.00 23.68 ? 277 TYR A C 1 ATOM 1792 O O . TYR A 1 236 ? -11.700 47.161 40.267 1.00 23.49 ? 277 TYR A O 1 ATOM 1793 C CB . TYR A 1 236 ? -13.044 46.006 42.512 1.00 24.48 ? 277 TYR A CB 1 ATOM 1794 C CG . TYR A 1 236 ? -12.587 46.946 43.574 1.00 22.74 ? 277 TYR A CG 1 ATOM 1795 C CD1 . TYR A 1 236 ? -12.344 48.296 43.259 1.00 24.77 ? 277 TYR A CD1 1 ATOM 1796 C CD2 . TYR A 1 236 ? -12.384 46.507 44.882 1.00 21.72 ? 277 TYR A CD2 1 ATOM 1797 C CE1 . TYR A 1 236 ? -11.896 49.192 44.217 1.00 25.37 ? 277 TYR A CE1 1 ATOM 1798 C CE2 . TYR A 1 236 ? -11.938 47.404 45.876 1.00 25.57 ? 277 TYR A CE2 1 ATOM 1799 C CZ . TYR A 1 236 ? -11.670 48.749 45.493 1.00 26.17 ? 277 TYR A CZ 1 ATOM 1800 O OH . TYR A 1 236 ? -11.230 49.645 46.453 1.00 28.76 ? 277 TYR A OH 1 ATOM 1801 N N . ALA A 1 237 ? -9.791 46.239 40.920 1.00 21.70 ? 278 ALA A N 1 ATOM 1802 C CA . ALA A 1 237 ? -9.028 47.279 40.270 1.00 22.81 ? 278 ALA A CA 1 ATOM 1803 C C . ALA A 1 237 ? -9.320 47.273 38.785 1.00 22.64 ? 278 ALA A C 1 ATOM 1804 O O . ALA A 1 237 ? -9.569 46.198 38.219 1.00 24.96 ? 278 ALA A O 1 ATOM 1805 C CB . ALA A 1 237 ? -7.530 46.995 40.462 1.00 22.46 ? 278 ALA A CB 1 ATOM 1806 N N . TYR A 1 238 ? -9.315 48.465 38.185 1.00 23.23 ? 279 TYR A N 1 ATOM 1807 C CA . TYR A 1 238 ? -9.383 48.592 36.738 1.00 23.55 ? 279 TYR A CA 1 ATOM 1808 C C . TYR A 1 238 ? -7.967 48.571 36.214 1.00 24.10 ? 279 TYR A C 1 ATOM 1809 O O . TYR A 1 238 ? -7.093 49.260 36.742 1.00 25.94 ? 279 TYR A O 1 ATOM 1810 C CB . TYR A 1 238 ? -10.095 49.899 36.318 1.00 26.70 ? 279 TYR A CB 1 ATOM 1811 C CG A TYR A 1 238 ? -10.447 49.900 34.842 0.50 24.48 ? 279 TYR A CG 1 ATOM 1812 C CG B TYR A 1 238 ? -9.510 50.510 35.014 0.50 27.97 ? 279 TYR A CG 1 ATOM 1813 C CD1 A TYR A 1 238 ? -11.504 49.142 34.351 0.50 25.46 ? 279 TYR A CD1 1 ATOM 1814 C CD1 B TYR A 1 238 ? -10.203 50.420 33.815 0.50 29.37 ? 279 TYR A CD1 1 ATOM 1815 C CD2 A TYR A 1 238 ? -9.685 50.639 33.950 0.50 26.23 ? 279 TYR A CD2 1 ATOM 1816 C CD2 B TYR A 1 238 ? -8.241 51.102 34.992 0.50 29.97 ? 279 TYR A CD2 1 ATOM 1817 C CE1 A TYR A 1 238 ? -11.789 49.124 32.992 0.50 29.36 ? 279 TYR A CE1 1 ATOM 1818 C CE1 B TYR A 1 238 ? -9.671 50.943 32.641 0.50 31.52 ? 279 TYR A CE1 1 ATOM 1819 C CE2 A TYR A 1 238 ? -9.961 50.632 32.613 0.50 28.65 ? 279 TYR A CE2 1 ATOM 1820 C CE2 B TYR A 1 238 ? -7.692 51.619 33.820 0.50 32.49 ? 279 TYR A CE2 1 ATOM 1821 C CZ A TYR A 1 238 ? -11.007 49.885 32.136 0.50 30.48 ? 279 TYR A CZ 1 ATOM 1822 C CZ B TYR A 1 238 ? -8.423 51.537 32.644 0.50 31.64 ? 279 TYR A CZ 1 ATOM 1823 O OH A TYR A 1 238 ? -11.256 49.883 30.789 0.50 32.44 ? 279 TYR A OH 1 ATOM 1824 O OH B TYR A 1 238 ? -7.908 52.055 31.468 0.50 35.62 ? 279 TYR A OH 1 ATOM 1825 N N . ARG A 1 239 ? -7.709 47.743 35.220 1.00 20.80 ? 280 ARG A N 1 ATOM 1826 C CA . ARG A 1 239 ? -6.347 47.593 34.706 1.00 20.59 ? 280 ARG A CA 1 ATOM 1827 C C . ARG A 1 239 ? -6.227 48.203 33.362 1.00 22.21 ? 280 ARG A C 1 ATOM 1828 O O . ARG A 1 239 ? -7.094 48.030 32.492 1.00 23.01 ? 280 ARG A O 1 ATOM 1829 C CB A ARG A 1 239 ? -5.989 46.135 34.553 0.65 20.28 ? 280 ARG A CB 1 ATOM 1830 C CB B ARG A 1 239 ? -5.993 46.093 34.631 0.35 20.70 ? 280 ARG A CB 1 ATOM 1831 C CG A ARG A 1 239 ? -5.920 45.494 35.869 0.65 19.48 ? 280 ARG A CG 1 ATOM 1832 C CG B ARG A 1 239 ? -5.365 45.445 35.906 0.35 19.83 ? 280 ARG A CG 1 ATOM 1833 C CD A ARG A 1 239 ? -5.532 44.052 35.802 0.65 17.34 ? 280 ARG A CD 1 ATOM 1834 C CD B ARG A 1 239 ? -6.325 45.205 37.102 0.35 18.43 ? 280 ARG A CD 1 ATOM 1835 N NE A ARG A 1 239 ? -5.262 43.646 37.150 0.65 19.42 ? 280 ARG A NE 1 ATOM 1836 N NE B ARG A 1 239 ? -5.661 44.536 38.241 0.35 17.90 ? 280 ARG A NE 1 ATOM 1837 C CZ A ARG A 1 239 ? -6.161 43.311 38.046 0.65 22.18 ? 280 ARG A CZ 1 ATOM 1838 C CZ B ARG A 1 239 ? -6.296 44.005 39.285 0.35 16.93 ? 280 ARG A CZ 1 ATOM 1839 N NH1 A ARG A 1 239 ? -7.470 43.270 37.730 0.65 22.26 ? 280 ARG A NH1 1 ATOM 1840 N NH1 B ARG A 1 239 ? -7.614 44.045 39.339 0.35 16.05 ? 280 ARG A NH1 1 ATOM 1841 N NH2 A ARG A 1 239 ? -5.748 43.008 39.255 0.65 21.35 ? 280 ARG A NH2 1 ATOM 1842 N NH2 B ARG A 1 239 ? -5.638 43.436 40.292 0.35 10.56 ? 280 ARG A NH2 1 ATOM 1843 N N . ARG A 1 240 ? -5.092 48.847 33.137 1.00 20.90 ? 281 ARG A N 1 ATOM 1844 C CA . ARG A 1 240 ? -4.762 49.262 31.780 1.00 22.00 ? 281 ARG A CA 1 ATOM 1845 C C . ARG A 1 240 ? -4.631 48.036 30.889 1.00 22.73 ? 281 ARG A C 1 ATOM 1846 O O . ARG A 1 240 ? -4.288 46.925 31.361 1.00 22.43 ? 281 ARG A O 1 ATOM 1847 C CB . ARG A 1 240 ? -3.429 49.977 31.786 1.00 21.11 ? 281 ARG A CB 1 ATOM 1848 C CG . ARG A 1 240 ? -3.488 51.277 32.515 1.00 20.46 ? 281 ARG A CG 1 ATOM 1849 C CD . ARG A 1 240 ? -2.232 52.070 32.374 1.00 20.85 ? 281 ARG A CD 1 ATOM 1850 N NE . ARG A 1 240 ? -2.431 53.396 32.967 1.00 22.32 ? 281 ARG A NE 1 ATOM 1851 C CZ . ARG A 1 240 ? -1.576 54.391 32.799 1.00 25.55 ? 281 ARG A CZ 1 ATOM 1852 N NH1 . ARG A 1 240 ? -0.520 54.179 32.061 1.00 25.19 ? 281 ARG A NH1 1 ATOM 1853 N NH2 . ARG A 1 240 ? -1.760 55.565 33.383 1.00 27.05 ? 281 ARG A NH2 1 ATOM 1854 N N . GLY A 1 241 ? -4.890 48.233 29.591 1.00 24.71 ? 282 GLY A N 1 ATOM 1855 C CA . GLY A 1 241 ? -4.539 47.210 28.634 1.00 26.78 ? 282 GLY A CA 1 ATOM 1856 C C . GLY A 1 241 ? -3.026 47.189 28.484 1.00 27.12 ? 282 GLY A C 1 ATOM 1857 O O . GLY A 1 241 ? -2.356 48.193 28.793 1.00 26.51 ? 282 GLY A O 1 ATOM 1858 N N . ILE A 1 242 ? -2.483 46.057 28.037 1.00 28.85 ? 283 ILE A N 1 ATOM 1859 C CA . ILE A 1 242 ? -1.027 45.931 27.847 1.00 29.73 ? 283 ILE A CA 1 ATOM 1860 C C . ILE A 1 242 ? -0.429 47.076 27.064 1.00 29.83 ? 283 ILE A C 1 ATOM 1861 O O . ILE A 1 242 ? 0.640 47.594 27.406 1.00 29.31 ? 283 ILE A O 1 ATOM 1862 C CB . ILE A 1 242 ? -0.564 44.557 27.236 1.00 30.88 ? 283 ILE A CB 1 ATOM 1863 C CG1 . ILE A 1 242 ? -0.581 43.478 28.292 1.00 32.63 ? 283 ILE A CG1 1 ATOM 1864 C CG2 . ILE A 1 242 ? 0.909 44.630 26.726 1.00 32.41 ? 283 ILE A CG2 1 ATOM 1865 C CD1 . ILE A 1 242 ? 0.648 43.539 29.237 1.00 30.40 ? 283 ILE A CD1 1 ATOM 1866 N N . ALA A 1 243 ? -1.112 47.521 26.016 1.00 30.29 ? 284 ALA A N 1 ATOM 1867 C CA . ALA A 1 243 ? -0.530 48.571 25.198 1.00 30.84 ? 284 ALA A CA 1 ATOM 1868 C C . ALA A 1 243 ? -0.331 49.871 25.945 1.00 30.58 ? 284 ALA A C 1 ATOM 1869 O O . ALA A 1 243 ? 0.519 50.655 25.554 1.00 31.48 ? 284 ALA A O 1 ATOM 1870 C CB . ALA A 1 243 ? -1.375 48.795 23.916 1.00 32.07 ? 284 ALA A CB 1 ATOM 1871 N N . GLU A 1 244 ? -1.090 50.097 27.028 1.00 29.41 ? 285 GLU A N 1 ATOM 1872 C CA . GLU A 1 244 ? -0.977 51.337 27.819 1.00 29.06 ? 285 GLU A CA 1 ATOM 1873 C C . GLU A 1 244 ? -0.231 51.085 29.148 1.00 27.78 ? 285 GLU A C 1 ATOM 1874 O O . GLU A 1 244 ? -0.127 51.996 29.972 1.00 27.63 ? 285 GLU A O 1 ATOM 1875 C CB . GLU A 1 244 ? -2.369 51.932 28.129 1.00 30.44 ? 285 GLU A CB 1 ATOM 1876 C CG . GLU A 1 244 ? -3.102 52.523 26.910 1.00 34.48 ? 285 GLU A CG 1 ATOM 1877 C CD . GLU A 1 244 ? -3.519 51.461 25.900 1.00 40.86 ? 285 GLU A CD 1 ATOM 1878 O OE1 . GLU A 1 244 ? -3.231 51.654 24.690 1.00 45.98 ? 285 GLU A OE1 1 ATOM 1879 O OE2 . GLU A 1 244 ? -4.113 50.427 26.290 1.00 40.51 ? 285 GLU A OE2 1 ATOM 1880 N N . ALA A 1 245 ? 0.282 49.868 29.337 1.00 25.74 ? 286 ALA A N 1 ATOM 1881 C CA . ALA A 1 245 ? 0.967 49.519 30.602 1.00 23.51 ? 286 ALA A CA 1 ATOM 1882 C C . ALA A 1 245 ? 2.212 50.411 30.782 1.00 24.19 ? 286 ALA A C 1 ATOM 1883 O O . ALA A 1 245 ? 2.790 50.949 29.815 1.00 24.05 ? 286 ALA A O 1 ATOM 1884 C CB . ALA A 1 245 ? 1.328 48.090 30.626 1.00 24.06 ? 286 ALA A CB 1 ATOM 1885 N N . VAL A 1 246 ? 2.601 50.592 32.040 1.00 20.45 ? 287 VAL A N 1 ATOM 1886 C CA . VAL A 1 246 ? 3.786 51.389 32.296 1.00 19.24 ? 287 VAL A CA 1 ATOM 1887 C C . VAL A 1 246 ? 5.049 50.567 32.216 1.00 20.49 ? 287 VAL A C 1 ATOM 1888 O O . VAL A 1 246 ? 5.172 49.516 32.843 1.00 20.50 ? 287 VAL A O 1 ATOM 1889 C CB . VAL A 1 246 ? 3.730 52.089 33.692 1.00 20.26 ? 287 VAL A CB 1 ATOM 1890 C CG1 . VAL A 1 246 ? 4.974 52.971 33.894 1.00 18.75 ? 287 VAL A CG1 1 ATOM 1891 C CG2 . VAL A 1 246 ? 2.475 52.938 33.803 1.00 22.74 ? 287 VAL A CG2 1 ATOM 1892 N N . GLY A 1 247 ? 5.992 51.103 31.454 1.00 19.14 ? 288 GLY A N 1 ATOM 1893 C CA . GLY A 1 247 ? 7.399 50.654 31.567 1.00 18.50 ? 288 GLY A CA 1 ATOM 1894 C C . GLY A 1 247 ? 7.849 49.404 30.827 1.00 18.53 ? 288 GLY A C 1 ATOM 1895 O O . GLY A 1 247 ? 8.995 48.987 30.980 1.00 18.36 ? 288 GLY A O 1 ATOM 1896 N N . LEU A 1 248 ? 6.984 48.842 29.999 1.00 19.77 ? 289 LEU A N 1 ATOM 1897 C CA . LEU A 1 248 ? 7.351 47.592 29.303 1.00 19.44 ? 289 LEU A CA 1 ATOM 1898 C C . LEU A 1 248 ? 8.280 47.901 28.121 1.00 20.17 ? 289 LEU A C 1 ATOM 1899 O O . LEU A 1 248 ? 8.112 48.922 27.425 1.00 20.91 ? 289 LEU A O 1 ATOM 1900 C CB . LEU A 1 248 ? 6.103 46.888 28.771 1.00 20.28 ? 289 LEU A CB 1 ATOM 1901 C CG . LEU A 1 248 ? 5.001 46.558 29.753 1.00 25.23 ? 289 LEU A CG 1 ATOM 1902 C CD1 . LEU A 1 248 ? 3.843 45.858 28.980 1.00 25.93 ? 289 LEU A CD1 1 ATOM 1903 C CD2 . LEU A 1 248 ? 5.596 45.611 30.747 1.00 26.64 ? 289 LEU A CD2 1 ATOM 1904 N N . PRO A 1 249 ? 9.257 47.021 27.888 1.00 20.59 ? 290 PRO A N 1 ATOM 1905 C CA . PRO A 1 249 ? 10.159 47.177 26.752 1.00 21.67 ? 290 PRO A CA 1 ATOM 1906 C C . PRO A 1 249 ? 9.460 46.789 25.463 1.00 22.46 ? 290 PRO A C 1 ATOM 1907 O O . PRO A 1 249 ? 8.539 45.944 25.493 1.00 22.68 ? 290 PRO A O 1 ATOM 1908 C CB . PRO A 1 249 ? 11.296 46.193 27.048 1.00 22.38 ? 290 PRO A CB 1 ATOM 1909 C CG . PRO A 1 249 ? 10.694 45.162 27.929 1.00 21.51 ? 290 PRO A CG 1 ATOM 1910 C CD . PRO A 1 249 ? 9.541 45.818 28.692 1.00 21.51 ? 290 PRO A CD 1 ATOM 1911 N N . SER A 1 250 ? 9.914 47.373 24.353 1.00 23.29 ? 291 SER A N 1 ATOM 1912 C CA A SER A 1 250 ? 9.295 47.173 23.037 0.50 23.34 ? 291 SER A CA 1 ATOM 1913 C CA B SER A 1 250 ? 9.257 47.111 23.075 0.50 24.17 ? 291 SER A CA 1 ATOM 1914 C C . SER A 1 250 ? 10.048 46.190 22.166 1.00 23.72 ? 291 SER A C 1 ATOM 1915 O O . SER A 1 250 ? 9.601 45.875 21.055 1.00 25.06 ? 291 SER A O 1 ATOM 1916 C CB A SER A 1 250 ? 9.198 48.503 22.294 0.50 23.99 ? 291 SER A CB 1 ATOM 1917 C CB B SER A 1 250 ? 8.875 48.416 22.378 0.50 24.94 ? 291 SER A CB 1 ATOM 1918 O OG A SER A 1 250 ? 10.487 49.017 22.041 0.50 22.81 ? 291 SER A OG 1 ATOM 1919 O OG B SER A 1 250 ? 7.729 48.974 23.011 0.50 28.18 ? 291 SER A OG 1 ATOM 1920 N N . ILE A 1 251 ? 11.208 45.756 22.633 1.00 22.16 ? 292 ILE A N 1 ATOM 1921 C CA . ILE A 1 251 ? 12.074 44.841 21.832 1.00 21.80 ? 292 ILE A CA 1 ATOM 1922 C C . ILE A 1 251 ? 12.490 43.666 22.690 1.00 22.05 ? 292 ILE A C 1 ATOM 1923 O O . ILE A 1 251 ? 12.584 43.781 23.921 1.00 21.71 ? 292 ILE A O 1 ATOM 1924 C CB . ILE A 1 251 ? 13.308 45.560 21.260 1.00 22.31 ? 292 ILE A CB 1 ATOM 1925 C CG1 . ILE A 1 251 ? 14.138 46.238 22.369 1.00 21.88 ? 292 ILE A CG1 1 ATOM 1926 C CG2 . ILE A 1 251 ? 12.849 46.609 20.253 1.00 24.65 ? 292 ILE A CG2 1 ATOM 1927 C CD1 . ILE A 1 251 ? 15.385 46.955 21.829 1.00 22.72 ? 292 ILE A CD1 1 ATOM 1928 N N . PRO A 1 252 ? 12.703 42.506 22.079 1.00 21.87 ? 293 PRO A N 1 ATOM 1929 C CA . PRO A 1 252 ? 13.044 41.350 22.899 1.00 21.80 ? 293 PRO A CA 1 ATOM 1930 C C . PRO A 1 252 ? 14.445 41.469 23.541 1.00 21.13 ? 293 PRO A C 1 ATOM 1931 O O . PRO A 1 252 ? 15.346 42.104 22.955 1.00 21.25 ? 293 PRO A O 1 ATOM 1932 C CB . PRO A 1 252 ? 13.039 40.176 21.883 1.00 22.93 ? 293 PRO A CB 1 ATOM 1933 C CG . PRO A 1 252 ? 12.059 40.683 20.773 1.00 23.59 ? 293 PRO A CG 1 ATOM 1934 C CD . PRO A 1 252 ? 12.418 42.143 20.668 1.00 22.10 ? 293 PRO A CD 1 ATOM 1935 N N . VAL A 1 253 ? 14.618 40.848 24.718 1.00 19.98 ? 294 VAL A N 1 ATOM 1936 C CA . VAL A 1 253 ? 15.885 40.965 25.456 1.00 19.43 ? 294 VAL A CA 1 ATOM 1937 C C . VAL A 1 253 ? 16.143 39.629 26.125 1.00 19.40 ? 294 VAL A C 1 ATOM 1938 O O . VAL A 1 253 ? 15.188 38.993 26.609 1.00 18.69 ? 294 VAL A O 1 ATOM 1939 C CB . VAL A 1 253 ? 15.757 42.037 26.588 1.00 18.66 ? 294 VAL A CB 1 ATOM 1940 C CG1 . VAL A 1 253 ? 17.052 42.144 27.377 1.00 20.50 ? 294 VAL A CG1 1 ATOM 1941 C CG2 . VAL A 1 253 ? 15.318 43.379 26.006 1.00 20.06 ? 294 VAL A CG2 1 ATOM 1942 N N . HIS A 1 254 ? 17.407 39.228 26.234 1.00 19.47 ? 295 HIS A N 1 ATOM 1943 C CA . HIS A 1 254 ? 17.737 37.968 26.879 1.00 18.84 ? 295 HIS A CA 1 ATOM 1944 C C . HIS A 1 254 ? 19.156 38.036 27.410 1.00 19.31 ? 295 HIS A C 1 ATOM 1945 O O . HIS A 1 254 ? 20.011 38.646 26.761 1.00 20.34 ? 295 HIS A O 1 ATOM 1946 C CB . HIS A 1 254 ? 17.670 36.817 25.845 1.00 20.80 ? 295 HIS A CB 1 ATOM 1947 C CG . HIS A 1 254 ? 17.727 35.445 26.439 1.00 20.36 ? 295 HIS A CG 1 ATOM 1948 N ND1 . HIS A 1 254 ? 16.726 34.962 27.257 1.00 19.79 ? 295 HIS A ND1 1 ATOM 1949 C CD2 . HIS A 1 254 ? 18.627 34.429 26.289 1.00 22.13 ? 295 HIS A CD2 1 ATOM 1950 C CE1 . HIS A 1 254 ? 17.014 33.714 27.604 1.00 21.58 ? 295 HIS A CE1 1 ATOM 1951 N NE2 . HIS A 1 254 ? 18.173 33.379 27.055 1.00 22.26 ? 295 HIS A NE2 1 ATOM 1952 N N . PRO A 1 255 ? 19.411 37.435 28.593 1.00 19.16 ? 296 PRO A N 1 ATOM 1953 C CA . PRO A 1 255 ? 20.759 37.453 29.170 1.00 18.33 ? 296 PRO A CA 1 ATOM 1954 C C . PRO A 1 255 ? 21.479 36.126 28.992 1.00 19.90 ? 296 PRO A C 1 ATOM 1955 O O . PRO A 1 255 ? 20.828 35.067 29.000 1.00 20.77 ? 296 PRO A O 1 ATOM 1956 C CB . PRO A 1 255 ? 20.464 37.646 30.675 1.00 18.82 ? 296 PRO A CB 1 ATOM 1957 C CG . PRO A 1 255 ? 19.122 36.888 30.873 1.00 19.62 ? 296 PRO A CG 1 ATOM 1958 C CD . PRO A 1 255 ? 18.394 36.907 29.539 1.00 19.24 ? 296 PRO A CD 1 ATOM 1959 N N . ILE A 1 256 ? 22.800 36.217 28.853 1.00 20.53 ? 297 ILE A N 1 ATOM 1960 C CA . ILE A 1 256 ? 23.678 35.050 28.656 1.00 21.53 ? 297 ILE A CA 1 ATOM 1961 C C . ILE A 1 256 ? 24.970 35.169 29.476 1.00 21.64 ? 297 ILE A C 1 ATOM 1962 O O . ILE A 1 256 ? 25.317 36.269 30.016 1.00 20.74 ? 297 ILE A O 1 ATOM 1963 C CB . ILE A 1 256 ? 24.008 34.837 27.143 1.00 22.08 ? 297 ILE A CB 1 ATOM 1964 C CG1 . ILE A 1 256 ? 24.967 35.931 26.651 1.00 22.91 ? 297 ILE A CG1 1 ATOM 1965 C CG2 . ILE A 1 256 ? 22.692 34.669 26.300 1.00 21.93 ? 297 ILE A CG2 1 ATOM 1966 C CD1 . ILE A 1 256 ? 25.445 35.763 25.145 1.00 24.09 ? 297 ILE A CD1 1 ATOM 1967 N N . GLY A 1 257 ? 25.660 34.030 29.625 1.00 21.65 ? 298 GLY A N 1 ATOM 1968 C CA . GLY A 1 257 ? 26.936 34.005 30.330 1.00 21.77 ? 298 GLY A CA 1 ATOM 1969 C C . GLY A 1 257 ? 28.090 34.229 29.355 1.00 22.27 ? 298 GLY A C 1 ATOM 1970 O O . GLY A 1 257 ? 27.880 34.465 28.153 1.00 22.95 ? 298 GLY A O 1 ATOM 1971 N N . TYR A 1 258 ? 29.293 34.268 29.905 1.00 22.49 ? 299 TYR A N 1 ATOM 1972 C CA . TYR A 1 258 ? 30.429 34.657 29.088 1.00 22.18 ? 299 TYR A CA 1 ATOM 1973 C C . TYR A 1 258 ? 30.962 33.555 28.171 1.00 23.10 ? 299 TYR A C 1 ATOM 1974 O O . TYR A 1 258 ? 31.560 33.914 27.169 1.00 24.58 ? 299 TYR A O 1 ATOM 1975 C CB . TYR A 1 258 ? 31.565 35.350 29.865 1.00 23.38 ? 299 TYR A CB 1 ATOM 1976 C CG . TYR A 1 258 ? 32.159 34.631 31.065 1.00 23.52 ? 299 TYR A CG 1 ATOM 1977 C CD1 . TYR A 1 258 ? 31.741 34.937 32.378 1.00 23.85 ? 299 TYR A CD1 1 ATOM 1978 C CD2 . TYR A 1 258 ? 33.202 33.693 30.909 1.00 24.80 ? 299 TYR A CD2 1 ATOM 1979 C CE1 . TYR A 1 258 ? 32.294 34.322 33.477 1.00 21.82 ? 299 TYR A CE1 1 ATOM 1980 C CE2 . TYR A 1 258 ? 33.779 33.086 32.012 1.00 23.62 ? 299 TYR A CE2 1 ATOM 1981 C CZ . TYR A 1 258 ? 33.314 33.391 33.315 1.00 24.68 ? 299 TYR A CZ 1 ATOM 1982 O OH . TYR A 1 258 ? 33.869 32.769 34.418 1.00 24.54 ? 299 TYR A OH 1 ATOM 1983 N N . TYR A 1 259 ? 30.724 32.283 28.479 1.00 23.38 ? 300 TYR A N 1 ATOM 1984 C CA . TYR A 1 259 ? 31.033 31.234 27.456 1.00 24.10 ? 300 TYR A CA 1 ATOM 1985 C C . TYR A 1 259 ? 30.224 31.488 26.217 1.00 25.71 ? 300 TYR A C 1 ATOM 1986 O O . TYR A 1 259 ? 30.777 31.482 25.099 1.00 26.78 ? 300 TYR A O 1 ATOM 1987 C CB . TYR A 1 259 ? 30.745 29.840 27.955 1.00 25.02 ? 300 TYR A CB 1 ATOM 1988 C CG . TYR A 1 259 ? 31.670 29.323 29.022 1.00 25.41 ? 300 TYR A CG 1 ATOM 1989 C CD1 . TYR A 1 259 ? 32.987 29.826 29.182 1.00 26.41 ? 300 TYR A CD1 1 ATOM 1990 C CD2 . TYR A 1 259 ? 31.251 28.263 29.846 1.00 25.90 ? 300 TYR A CD2 1 ATOM 1991 C CE1 . TYR A 1 259 ? 33.823 29.327 30.157 1.00 26.02 ? 300 TYR A CE1 1 ATOM 1992 C CE2 . TYR A 1 259 ? 32.092 27.751 30.825 1.00 26.17 ? 300 TYR A CE2 1 ATOM 1993 C CZ . TYR A 1 259 ? 33.369 28.269 30.960 1.00 26.84 ? 300 TYR A CZ 1 ATOM 1994 O OH . TYR A 1 259 ? 34.191 27.738 31.938 1.00 30.29 ? 300 TYR A OH 1 ATOM 1995 N N . ASP A 1 260 ? 28.913 31.705 26.385 1.00 25.16 ? 301 ASP A N 1 ATOM 1996 C CA . ASP A 1 260 ? 28.074 31.971 25.226 1.00 25.99 ? 301 ASP A CA 1 ATOM 1997 C C . ASP A 1 260 ? 28.396 33.312 24.587 1.00 26.58 ? 301 ASP A C 1 ATOM 1998 O O . ASP A 1 260 ? 28.374 33.446 23.341 1.00 25.92 ? 301 ASP A O 1 ATOM 1999 C CB . ASP A 1 260 ? 26.614 31.946 25.640 1.00 25.57 ? 301 ASP A CB 1 ATOM 2000 C CG . ASP A 1 260 ? 26.081 30.540 25.799 1.00 27.24 ? 301 ASP A CG 1 ATOM 2001 O OD1 . ASP A 1 260 ? 26.717 29.601 25.233 1.00 28.04 ? 301 ASP A OD1 1 ATOM 2002 O OD2 . ASP A 1 260 ? 25.015 30.364 26.464 1.00 25.10 ? 301 ASP A OD2 1 ATOM 2003 N N . ALA A 1 261 ? 28.645 34.340 25.412 1.00 24.74 ? 302 ALA A N 1 ATOM 2004 C CA . ALA A 1 261 ? 29.002 35.661 24.823 1.00 25.27 ? 302 ALA A CA 1 ATOM 2005 C C . ALA A 1 261 ? 30.238 35.580 23.940 1.00 26.17 ? 302 ALA A C 1 ATOM 2006 O O . ALA A 1 261 ? 30.316 36.265 22.912 1.00 27.65 ? 302 ALA A O 1 ATOM 2007 C CB . ALA A 1 261 ? 29.227 36.716 25.904 1.00 24.25 ? 302 ALA A CB 1 ATOM 2008 N N . GLN A 1 262 ? 31.211 34.795 24.367 1.00 25.99 ? 303 GLN A N 1 ATOM 2009 C CA . GLN A 1 262 ? 32.458 34.711 23.595 1.00 28.04 ? 303 GLN A CA 1 ATOM 2010 C C . GLN A 1 262 ? 32.153 34.203 22.163 1.00 28.75 ? 303 GLN A C 1 ATOM 2011 O O . GLN A 1 262 ? 32.705 34.715 21.182 1.00 29.17 ? 303 GLN A O 1 ATOM 2012 C CB . GLN A 1 262 ? 33.458 33.837 24.312 1.00 27.73 ? 303 GLN A CB 1 ATOM 2013 C CG . GLN A 1 262 ? 34.682 33.586 23.397 1.00 31.11 ? 303 GLN A CG 1 ATOM 2014 C CD . GLN A 1 262 ? 35.982 33.544 24.129 1.00 37.83 ? 303 GLN A CD 1 ATOM 2015 O OE1 . GLN A 1 262 ? 37.064 33.473 23.496 1.00 44.62 ? 303 GLN A OE1 1 ATOM 2016 N NE2 . GLN A 1 262 ? 35.927 33.520 25.447 1.00 36.25 ? 303 GLN A NE2 1 ATOM 2017 N N . LYS A 1 263 ? 31.225 33.255 22.054 1.00 29.59 ? 304 LYS A N 1 ATOM 2018 C CA . LYS A 1 263 ? 30.834 32.741 20.747 1.00 29.82 ? 304 LYS A CA 1 ATOM 2019 C C . LYS A 1 263 ? 30.112 33.774 19.887 1.00 30.75 ? 304 LYS A C 1 ATOM 2020 O O . LYS A 1 263 ? 30.182 33.720 18.668 1.00 31.36 ? 304 LYS A O 1 ATOM 2021 C CB . LYS A 1 263 ? 29.965 31.499 20.890 1.00 30.11 ? 304 LYS A CB 1 ATOM 2022 C CG . LYS A 1 263 ? 30.649 30.368 21.600 1.00 32.44 ? 304 LYS A CG 1 ATOM 2023 C CD . LYS A 1 263 ? 31.553 29.631 20.608 1.00 40.58 ? 304 LYS A CD 1 ATOM 2024 C CE . LYS A 1 263 ? 32.696 28.958 21.339 1.00 45.46 ? 304 LYS A CE 1 ATOM 2025 N NZ . LYS A 1 263 ? 33.243 27.838 20.503 1.00 52.13 ? 304 LYS A NZ 1 ATOM 2026 N N . LEU A 1 264 ? 29.367 34.699 20.502 1.00 27.82 ? 305 LEU A N 1 ATOM 2027 C CA . LEU A 1 264 ? 28.709 35.757 19.717 1.00 29.16 ? 305 LEU A CA 1 ATOM 2028 C C . LEU A 1 264 ? 29.647 36.905 19.342 1.00 29.02 ? 305 LEU A C 1 ATOM 2029 O O . LEU A 1 264 ? 29.450 37.539 18.284 1.00 31.15 ? 305 LEU A O 1 ATOM 2030 C CB . LEU A 1 264 ? 27.508 36.329 20.494 1.00 26.57 ? 305 LEU A CB 1 ATOM 2031 C CG . LEU A 1 264 ? 26.372 35.321 20.786 1.00 27.79 ? 305 LEU A CG 1 ATOM 2032 C CD1 . LEU A 1 264 ? 25.192 36.044 21.492 1.00 27.89 ? 305 LEU A CD1 1 ATOM 2033 C CD2 . LEU A 1 264 ? 25.843 34.665 19.523 1.00 29.58 ? 305 LEU A CD2 1 ATOM 2034 N N . LEU A 1 265 ? 30.623 37.207 20.211 1.00 27.90 ? 306 LEU A N 1 ATOM 2035 C CA . LEU A 1 265 ? 31.521 38.330 20.021 1.00 27.93 ? 306 LEU A CA 1 ATOM 2036 C C . LEU A 1 265 ? 32.753 37.988 19.171 1.00 28.93 ? 306 LEU A C 1 ATOM 2037 O O . LEU A 1 265 ? 33.359 38.883 18.597 1.00 30.49 ? 306 LEU A O 1 ATOM 2038 C CB . LEU A 1 265 ? 32.077 38.824 21.334 1.00 27.41 ? 306 LEU A CB 1 ATOM 2039 C CG . LEU A 1 265 ? 31.007 39.375 22.308 1.00 27.16 ? 306 LEU A CG 1 ATOM 2040 C CD1 . LEU A 1 265 ? 31.623 39.620 23.710 1.00 25.20 ? 306 LEU A CD1 1 ATOM 2041 C CD2 . LEU A 1 265 ? 30.331 40.643 21.783 1.00 26.86 ? 306 LEU A CD2 1 ATOM 2042 N N . GLU A 1 266 ? 33.158 36.728 19.190 1.00 29.91 ? 307 GLU A N 1 ATOM 2043 C CA . GLU A 1 266 ? 34.472 36.392 18.596 1.00 31.05 ? 307 GLU A CA 1 ATOM 2044 C C . GLU A 1 266 ? 34.539 36.696 17.096 1.00 31.93 ? 307 GLU A C 1 ATOM 2045 O O . GLU A 1 266 ? 35.623 36.958 16.565 1.00 32.13 ? 307 GLU A O 1 ATOM 2046 C CB . GLU A 1 266 ? 34.847 34.938 18.881 1.00 30.70 ? 307 GLU A CB 1 ATOM 2047 C CG . GLU A 1 266 ? 33.931 33.946 18.267 1.00 33.41 ? 307 GLU A CG 1 ATOM 2048 C CD . GLU A 1 266 ? 34.308 32.537 18.654 1.00 35.35 ? 307 GLU A CD 1 ATOM 2049 O OE1 . GLU A 1 266 ? 35.203 32.373 19.525 1.00 39.86 ? 307 GLU A OE1 1 ATOM 2050 O OE2 . GLU A 1 266 ? 33.709 31.603 18.074 1.00 36.37 ? 307 GLU A OE2 1 ATOM 2051 N N . LYS A 1 267 ? 33.392 36.662 16.435 1.00 32.23 ? 308 LYS A N 1 ATOM 2052 C CA . LYS A 1 267 ? 33.333 36.862 14.996 1.00 33.66 ? 308 LYS A CA 1 ATOM 2053 C C . LYS A 1 267 ? 33.065 38.303 14.606 1.00 33.84 ? 308 LYS A C 1 ATOM 2054 O O . LYS A 1 267 ? 32.979 38.619 13.406 1.00 33.08 ? 308 LYS A O 1 ATOM 2055 C CB . LYS A 1 267 ? 32.260 35.961 14.387 1.00 33.75 ? 308 LYS A CB 1 ATOM 2056 C CG . LYS A 1 267 ? 32.699 34.488 14.262 1.00 35.17 ? 308 LYS A CG 1 ATOM 2057 C CD . LYS A 1 267 ? 31.516 33.622 13.915 1.00 37.76 ? 308 LYS A CD 1 ATOM 2058 C CE . LYS A 1 267 ? 31.936 32.194 13.578 1.00 39.69 ? 308 LYS A CE 1 ATOM 2059 N NZ . LYS A 1 267 ? 30.724 31.457 13.120 1.00 41.26 ? 308 LYS A NZ 1 ATOM 2060 N N . MET A 1 268 ? 32.885 39.182 15.603 1.00 32.15 ? 309 MET A N 1 ATOM 2061 C CA . MET A 1 268 ? 32.547 40.570 15.289 1.00 33.08 ? 309 MET A CA 1 ATOM 2062 C C . MET A 1 268 ? 33.549 41.339 14.418 1.00 33.74 ? 309 MET A C 1 ATOM 2063 O O . MET A 1 268 ? 34.749 41.311 14.661 1.00 33.41 ? 309 MET A O 1 ATOM 2064 C CB . MET A 1 268 ? 32.218 41.349 16.556 1.00 32.22 ? 309 MET A CB 1 ATOM 2065 C CG A MET A 1 268 ? 30.835 40.842 17.017 0.50 31.51 ? 309 MET A CG 1 ATOM 2066 C CG B MET A 1 268 ? 31.052 40.836 17.336 0.50 32.80 ? 309 MET A CG 1 ATOM 2067 S SD A MET A 1 268 ? 29.892 41.784 18.206 0.50 10.60 ? 309 MET A SD 1 ATOM 2068 S SD B MET A 1 268 ? 29.577 41.495 16.611 0.50 11.97 ? 309 MET A SD 1 ATOM 2069 C CE A MET A 1 268 ? 29.607 43.323 17.317 0.50 29.97 ? 309 MET A CE 1 ATOM 2070 C CE B MET A 1 268 ? 29.845 43.263 16.746 0.50 32.79 ? 309 MET A CE 1 ATOM 2071 N N . GLY A 1 269 ? 33.012 42.062 13.439 1.00 34.72 ? 310 GLY A N 1 ATOM 2072 C CA . GLY A 1 269 ? 33.824 42.892 12.552 1.00 35.52 ? 310 GLY A CA 1 ATOM 2073 C C . GLY A 1 269 ? 33.485 44.363 12.658 1.00 36.48 ? 310 GLY A C 1 ATOM 2074 O O . GLY A 1 269 ? 33.143 44.867 13.748 1.00 35.63 ? 310 GLY A O 1 ATOM 2075 N N . GLY A 1 270 ? 33.567 45.066 11.530 1.00 36.60 ? 311 GLY A N 1 ATOM 2076 C CA . GLY A 1 270 ? 33.293 46.498 11.508 1.00 37.13 ? 311 GLY A CA 1 ATOM 2077 C C . GLY A 1 270 ? 34.364 47.252 12.274 1.00 37.85 ? 311 GLY A C 1 ATOM 2078 O O . GLY A 1 270 ? 35.548 46.883 12.245 1.00 38.30 ? 311 GLY A O 1 ATOM 2079 N N . SER A 1 271 ? 33.951 48.295 12.986 1.00 37.19 ? 312 SER A N 1 ATOM 2080 C CA . SER A 1 271 ? 34.893 49.191 13.642 1.00 37.90 ? 312 SER A CA 1 ATOM 2081 C C . SER A 1 271 ? 35.548 48.575 14.871 1.00 37.35 ? 312 SER A C 1 ATOM 2082 O O . SER A 1 271 ? 34.922 47.780 15.589 1.00 37.79 ? 312 SER A O 1 ATOM 2083 C CB . SER A 1 271 ? 34.173 50.481 14.028 1.00 38.14 ? 312 SER A CB 1 ATOM 2084 O OG . SER A 1 271 ? 33.692 51.137 12.855 1.00 40.90 ? 312 SER A OG 1 ATOM 2085 N N . ALA A 1 272 ? 36.803 48.939 15.123 1.00 37.41 ? 313 ALA A N 1 ATOM 2086 C CA . ALA A 1 272 ? 37.483 48.560 16.370 1.00 36.78 ? 313 ALA A CA 1 ATOM 2087 C C . ALA A 1 272 ? 36.803 49.264 17.553 1.00 35.64 ? 313 ALA A C 1 ATOM 2088 O O . ALA A 1 272 ? 36.146 50.292 17.343 1.00 34.94 ? 313 ALA A O 1 ATOM 2089 C CB . ALA A 1 272 ? 38.945 48.980 16.317 1.00 36.99 ? 313 ALA A CB 1 ATOM 2090 N N . PRO A 1 273 ? 36.993 48.743 18.793 1.00 35.52 ? 314 PRO A N 1 ATOM 2091 C CA . PRO A 1 273 ? 36.527 49.482 19.990 1.00 35.51 ? 314 PRO A CA 1 ATOM 2092 C C . PRO A 1 273 ? 37.252 50.831 20.007 1.00 36.09 ? 314 PRO A C 1 ATOM 2093 O O . PRO A 1 273 ? 38.425 50.898 19.597 1.00 36.27 ? 314 PRO A O 1 ATOM 2094 C CB . PRO A 1 273 ? 36.983 48.593 21.165 1.00 35.01 ? 314 PRO A CB 1 ATOM 2095 C CG . PRO A 1 273 ? 38.131 47.743 20.579 1.00 36.17 ? 314 PRO A CG 1 ATOM 2096 C CD . PRO A 1 273 ? 37.700 47.499 19.161 1.00 35.53 ? 314 PRO A CD 1 ATOM 2097 N N . PRO A 1 274 ? 36.569 51.903 20.430 1.00 36.01 ? 315 PRO A N 1 ATOM 2098 C CA . PRO A 1 274 ? 37.165 53.235 20.325 1.00 36.35 ? 315 PRO A CA 1 ATOM 2099 C C . PRO A 1 274 ? 38.310 53.471 21.303 1.00 36.75 ? 315 PRO A C 1 ATOM 2100 O O . PRO A 1 274 ? 39.117 54.386 21.103 1.00 37.48 ? 315 PRO A O 1 ATOM 2101 C CB . PRO A 1 274 ? 35.980 54.171 20.625 1.00 35.31 ? 315 PRO A CB 1 ATOM 2102 C CG . PRO A 1 274 ? 35.019 53.321 21.451 1.00 35.51 ? 315 PRO A CG 1 ATOM 2103 C CD . PRO A 1 274 ? 35.143 51.962 20.820 1.00 34.88 ? 315 PRO A CD 1 ATOM 2104 N N . ASP A 1 275 ? 38.363 52.684 22.370 1.00 36.35 ? 316 ASP A N 1 ATOM 2105 C CA . ASP A 1 275 ? 39.431 52.787 23.367 1.00 36.88 ? 316 ASP A CA 1 ATOM 2106 C C . ASP A 1 275 ? 39.312 51.637 24.361 1.00 36.69 ? 316 ASP A C 1 ATOM 2107 O O . ASP A 1 275 ? 38.367 50.830 24.282 1.00 36.11 ? 316 ASP A O 1 ATOM 2108 C CB . ASP A 1 275 ? 39.412 54.156 24.074 1.00 37.37 ? 316 ASP A CB 1 ATOM 2109 C CG . ASP A 1 275 ? 38.172 54.366 24.941 1.00 38.94 ? 316 ASP A CG 1 ATOM 2110 O OD1 . ASP A 1 275 ? 37.873 53.502 25.798 1.00 39.40 ? 316 ASP A OD1 1 ATOM 2111 O OD2 . ASP A 1 275 ? 37.511 55.417 24.796 1.00 40.72 ? 316 ASP A OD2 1 ATOM 2112 N N . SER A 1 276 ? 40.237 51.563 25.312 1.00 36.61 ? 317 SER A N 1 ATOM 2113 C CA . SER A 1 276 ? 40.305 50.402 26.204 1.00 36.84 ? 317 SER A CA 1 ATOM 2114 C C . SER A 1 276 ? 39.097 50.258 27.169 1.00 35.38 ? 317 SER A C 1 ATOM 2115 O O . SER A 1 276 ? 38.830 49.144 27.618 1.00 35.49 ? 317 SER A O 1 ATOM 2116 C CB . SER A 1 276 ? 41.614 50.392 27.002 1.00 37.49 ? 317 SER A CB 1 ATOM 2117 O OG . SER A 1 276 ? 41.608 51.459 27.948 1.00 39.29 ? 317 SER A OG 1 ATOM 2118 N N . SER A 1 277 ? 38.395 51.356 27.485 1.00 34.71 ? 318 SER A N 1 ATOM 2119 C CA . SER A 1 277 ? 37.213 51.324 28.392 1.00 32.78 ? 318 SER A CA 1 ATOM 2120 C C . SER A 1 277 ? 36.041 50.542 27.792 1.00 31.72 ? 318 SER A C 1 ATOM 2121 O O . SER A 1 277 ? 35.011 50.317 28.470 1.00 31.71 ? 318 SER A O 1 ATOM 2122 C CB . SER A 1 277 ? 36.744 52.742 28.699 1.00 32.60 ? 318 SER A CB 1 ATOM 2123 O OG . SER A 1 277 ? 36.125 53.331 27.558 1.00 33.02 ? 318 SER A OG 1 ATOM 2124 N N . TRP A 1 278 ? 36.185 50.192 26.513 1.00 29.99 ? 319 TRP A N 1 ATOM 2125 C CA . TRP A 1 278 ? 35.211 49.375 25.764 1.00 28.83 ? 319 TRP A CA 1 ATOM 2126 C C . TRP A 1 278 ? 35.609 47.896 25.722 1.00 28.43 ? 319 TRP A C 1 ATOM 2127 O O . TRP A 1 278 ? 34.806 47.049 25.316 1.00 27.63 ? 319 TRP A O 1 ATOM 2128 C CB . TRP A 1 278 ? 35.049 49.908 24.339 1.00 29.29 ? 319 TRP A CB 1 ATOM 2129 C CG . TRP A 1 278 ? 34.100 51.070 24.266 1.00 28.44 ? 319 TRP A CG 1 ATOM 2130 C CD1 . TRP A 1 278 ? 34.217 52.284 24.906 1.00 28.27 ? 319 TRP A CD1 1 ATOM 2131 C CD2 . TRP A 1 278 ? 32.865 51.102 23.555 1.00 26.37 ? 319 TRP A CD2 1 ATOM 2132 N NE1 . TRP A 1 278 ? 33.131 53.073 24.620 1.00 29.21 ? 319 TRP A NE1 1 ATOM 2133 C CE2 . TRP A 1 278 ? 32.270 52.373 23.812 1.00 28.76 ? 319 TRP A CE2 1 ATOM 2134 C CE3 . TRP A 1 278 ? 32.193 50.184 22.743 1.00 24.49 ? 319 TRP A CE3 1 ATOM 2135 C CZ2 . TRP A 1 278 ? 31.054 52.763 23.249 1.00 26.49 ? 319 TRP A CZ2 1 ATOM 2136 C CZ3 . TRP A 1 278 ? 30.973 50.574 22.173 1.00 25.21 ? 319 TRP A CZ3 1 ATOM 2137 C CH2 . TRP A 1 278 ? 30.409 51.857 22.454 1.00 25.68 ? 319 TRP A CH2 1 ATOM 2138 N N . ARG A 1 279 ? 36.831 47.583 26.165 1.00 28.68 ? 320 ARG A N 1 ATOM 2139 C CA . ARG A 1 279 ? 37.317 46.205 26.174 1.00 29.01 ? 320 ARG A CA 1 ATOM 2140 C C . ARG A 1 279 ? 37.138 45.499 27.523 1.00 28.28 ? 320 ARG A C 1 ATOM 2141 O O . ARG A 1 279 ? 37.648 45.961 28.538 1.00 29.24 ? 320 ARG A O 1 ATOM 2142 C CB . ARG A 1 279 ? 38.809 46.156 25.765 1.00 28.84 ? 320 ARG A CB 1 ATOM 2143 C CG . ARG A 1 279 ? 39.001 46.428 24.269 1.00 32.24 ? 320 ARG A CG 1 ATOM 2144 C CD . ARG A 1 279 ? 40.385 45.960 23.734 1.00 43.28 ? 320 ARG A CD 1 ATOM 2145 N NE . ARG A 1 279 ? 41.244 47.110 23.503 1.00 53.11 ? 320 ARG A NE 1 ATOM 2146 C CZ . ARG A 1 279 ? 42.068 47.640 24.408 1.00 57.13 ? 320 ARG A CZ 1 ATOM 2147 N NH1 . ARG A 1 279 ? 42.168 47.115 25.634 1.00 58.67 ? 320 ARG A NH1 1 ATOM 2148 N NH2 . ARG A 1 279 ? 42.796 48.700 24.085 1.00 59.13 ? 320 ARG A NH2 1 ATOM 2149 N N . GLY A 1 280 ? 36.408 44.379 27.518 1.00 29.27 ? 321 GLY A N 1 ATOM 2150 C CA . GLY A 1 280 ? 36.345 43.460 28.651 1.00 28.79 ? 321 GLY A CA 1 ATOM 2151 C C . GLY A 1 280 ? 37.533 42.511 28.667 1.00 30.40 ? 321 GLY A C 1 ATOM 2152 O O . GLY A 1 280 ? 38.595 42.817 28.084 1.00 30.30 ? 321 GLY A O 1 ATOM 2153 N N . SER A 1 281 ? 37.370 41.361 29.319 1.00 29.59 ? 322 SER A N 1 ATOM 2154 C CA . SER A 1 281 ? 38.500 40.454 29.532 1.00 32.47 ? 322 SER A CA 1 ATOM 2155 C C . SER A 1 281 ? 38.463 39.216 28.664 1.00 31.89 ? 322 SER A C 1 ATOM 2156 O O . SER A 1 281 ? 39.346 38.374 28.767 1.00 33.78 ? 322 SER A O 1 ATOM 2157 C CB . SER A 1 281 ? 38.574 40.018 31.002 1.00 32.03 ? 322 SER A CB 1 ATOM 2158 O OG . SER A 1 281 ? 38.881 41.137 31.813 1.00 38.72 ? 322 SER A OG 1 ATOM 2159 N N . LEU A 1 282 ? 37.470 39.068 27.799 1.00 30.42 ? 323 LEU A N 1 ATOM 2160 C CA . LEU A 1 282 ? 37.441 37.868 26.969 1.00 30.85 ? 323 LEU A CA 1 ATOM 2161 C C . LEU A 1 282 ? 38.501 37.994 25.858 1.00 31.67 ? 323 LEU A C 1 ATOM 2162 O O . LEU A 1 282 ? 38.932 39.104 25.500 1.00 31.38 ? 323 LEU A O 1 ATOM 2163 C CB . LEU A 1 282 ? 36.069 37.663 26.349 1.00 30.44 ? 323 LEU A CB 1 ATOM 2164 C CG . LEU A 1 282 ? 34.929 37.392 27.341 1.00 28.66 ? 323 LEU A CG 1 ATOM 2165 C CD1 . LEU A 1 282 ? 33.626 37.581 26.600 1.00 28.52 ? 323 LEU A CD1 1 ATOM 2166 C CD2 . LEU A 1 282 ? 35.052 36.020 27.970 1.00 28.61 ? 323 LEU A CD2 1 ATOM 2167 N N . LYS A 1 283 ? 38.879 36.856 25.296 1.00 32.87 ? 324 LYS A N 1 ATOM 2168 C CA . LYS A 1 283 ? 39.838 36.843 24.195 1.00 35.02 ? 324 LYS A CA 1 ATOM 2169 C C . LYS A 1 283 ? 39.154 37.085 22.864 1.00 34.32 ? 324 LYS A C 1 ATOM 2170 O O . LYS A 1 283 ? 39.111 36.206 21.980 1.00 35.34 ? 324 LYS A O 1 ATOM 2171 C CB . LYS A 1 283 ? 40.617 35.538 24.216 1.00 35.80 ? 324 LYS A CB 1 ATOM 2172 C CG . LYS A 1 283 ? 41.447 35.418 25.483 1.00 40.84 ? 324 LYS A CG 1 ATOM 2173 C CD . LYS A 1 283 ? 42.509 36.542 25.558 1.00 46.69 ? 324 LYS A CD 1 ATOM 2174 C CE . LYS A 1 283 ? 42.629 37.103 26.975 1.00 49.52 ? 324 LYS A CE 1 ATOM 2175 N NZ . LYS A 1 283 ? 43.885 37.913 27.154 1.00 52.49 ? 324 LYS A NZ 1 ATOM 2176 N N . VAL A 1 284 ? 38.620 38.301 22.745 1.00 32.95 ? 325 VAL A N 1 ATOM 2177 C CA . VAL A 1 284 ? 38.003 38.769 21.534 1.00 32.69 ? 325 VAL A CA 1 ATOM 2178 C C . VAL A 1 284 ? 38.427 40.222 21.367 1.00 31.82 ? 325 VAL A C 1 ATOM 2179 O O . VAL A 1 284 ? 38.880 40.852 22.333 1.00 31.92 ? 325 VAL A O 1 ATOM 2180 C CB . VAL A 1 284 ? 36.439 38.661 21.563 1.00 31.67 ? 325 VAL A CB 1 ATOM 2181 C CG1 . VAL A 1 284 ? 35.956 37.191 21.752 1.00 33.26 ? 325 VAL A CG1 1 ATOM 2182 C CG2 . VAL A 1 284 ? 35.814 39.607 22.621 1.00 31.58 ? 325 VAL A CG2 1 ATOM 2183 N N . PRO A 1 285 ? 38.268 40.769 20.154 1.00 32.61 ? 326 PRO A N 1 ATOM 2184 C CA . PRO A 1 285 ? 38.708 42.135 19.839 1.00 32.45 ? 326 PRO A CA 1 ATOM 2185 C C . PRO A 1 285 ? 37.791 43.221 20.384 1.00 31.88 ? 326 PRO A C 1 ATOM 2186 O O . PRO A 1 285 ? 38.187 44.373 20.442 1.00 31.72 ? 326 PRO A O 1 ATOM 2187 C CB . PRO A 1 285 ? 38.651 42.187 18.301 1.00 33.41 ? 326 PRO A CB 1 ATOM 2188 C CG . PRO A 1 285 ? 37.711 41.071 17.899 1.00 34.68 ? 326 PRO A CG 1 ATOM 2189 C CD . PRO A 1 285 ? 37.812 40.022 18.957 1.00 33.40 ? 326 PRO A CD 1 ATOM 2190 N N . TYR A 1 286 ? 36.566 42.854 20.747 1.00 31.33 ? 327 TYR A N 1 ATOM 2191 C CA . TYR A 1 286 ? 35.550 43.838 21.167 1.00 30.68 ? 327 TYR A CA 1 ATOM 2192 C C . TYR A 1 286 ? 35.242 44.842 20.045 1.00 31.20 ? 327 TYR A C 1 ATOM 2193 O O . TYR A 1 286 ? 34.991 46.033 20.295 1.00 31.36 ? 327 TYR A O 1 ATOM 2194 C CB . TYR A 1 286 ? 35.953 44.530 22.480 1.00 30.53 ? 327 TYR A CB 1 ATOM 2195 C CG . TYR A 1 286 ? 35.838 43.578 23.637 1.00 30.48 ? 327 TYR A CG 1 ATOM 2196 C CD1 . TYR A 1 286 ? 34.598 43.374 24.267 1.00 28.23 ? 327 TYR A CD1 1 ATOM 2197 C CD2 . TYR A 1 286 ? 36.936 42.842 24.078 1.00 29.71 ? 327 TYR A CD2 1 ATOM 2198 C CE1 . TYR A 1 286 ? 34.482 42.466 25.315 1.00 26.01 ? 327 TYR A CE1 1 ATOM 2199 C CE2 . TYR A 1 286 ? 36.833 41.941 25.117 1.00 27.83 ? 327 TYR A CE2 1 ATOM 2200 C CZ . TYR A 1 286 ? 35.597 41.752 25.737 1.00 27.58 ? 327 TYR A CZ 1 ATOM 2201 O OH . TYR A 1 286 ? 35.474 40.849 26.771 1.00 26.97 ? 327 TYR A OH 1 ATOM 2202 N N . ASN A 1 287 ? 35.263 44.357 18.798 1.00 31.14 ? 328 ASN A N 1 ATOM 2203 C CA . ASN A 1 287 ? 34.823 45.177 17.684 1.00 31.67 ? 328 ASN A CA 1 ATOM 2204 C C . ASN A 1 287 ? 33.376 45.573 17.866 1.00 31.11 ? 328 ASN A C 1 ATOM 2205 O O . ASN A 1 287 ? 32.564 44.780 18.327 1.00 30.68 ? 328 ASN A O 1 ATOM 2206 C CB . ASN A 1 287 ? 34.973 44.439 16.370 1.00 31.47 ? 328 ASN A CB 1 ATOM 2207 C CG . ASN A 1 287 ? 36.430 44.265 15.975 1.00 32.69 ? 328 ASN A CG 1 ATOM 2208 O OD1 . ASN A 1 287 ? 37.267 45.114 16.290 1.00 33.67 ? 328 ASN A OD1 1 ATOM 2209 N ND2 . ASN A 1 287 ? 36.747 43.144 15.317 1.00 33.39 ? 328 ASN A ND2 1 ATOM 2210 N N . VAL A 1 288 ? 33.061 46.788 17.447 1.00 32.46 ? 329 VAL A N 1 ATOM 2211 C CA . VAL A 1 288 ? 31.712 47.329 17.640 1.00 32.93 ? 329 VAL A CA 1 ATOM 2212 C C . VAL A 1 288 ? 30.728 46.812 16.579 1.00 32.99 ? 329 VAL A C 1 ATOM 2213 O O . VAL A 1 288 ? 29.507 46.838 16.765 1.00 31.73 ? 329 VAL A O 1 ATOM 2214 C CB . VAL A 1 288 ? 31.758 48.880 17.644 1.00 34.35 ? 329 VAL A CB 1 ATOM 2215 C CG1 . VAL A 1 288 ? 30.363 49.446 17.495 1.00 34.45 ? 329 VAL A CG1 1 ATOM 2216 C CG2 . VAL A 1 288 ? 32.371 49.380 18.953 1.00 34.46 ? 329 VAL A CG2 1 ATOM 2217 N N . GLY A 1 289 ? 31.260 46.332 15.452 1.00 33.25 ? 330 GLY A N 1 ATOM 2218 C CA . GLY A 1 289 ? 30.389 45.956 14.335 1.00 33.27 ? 330 GLY A CA 1 ATOM 2219 C C . GLY A 1 289 ? 30.071 47.150 13.459 1.00 33.35 ? 330 GLY A C 1 ATOM 2220 O O . GLY A 1 289 ? 30.855 48.102 13.385 1.00 33.72 ? 330 GLY A O 1 ATOM 2221 N N . PRO A 1 290 ? 28.916 47.126 12.788 1.00 34.19 ? 331 PRO A N 1 ATOM 2222 C CA . PRO A 1 290 ? 27.899 46.082 12.806 1.00 34.33 ? 331 PRO A CA 1 ATOM 2223 C C . PRO A 1 290 ? 28.361 44.810 12.105 1.00 35.37 ? 331 PRO A C 1 ATOM 2224 O O . PRO A 1 290 ? 29.200 44.859 11.178 1.00 36.03 ? 331 PRO A O 1 ATOM 2225 C CB . PRO A 1 290 ? 26.741 46.706 12.020 1.00 34.78 ? 331 PRO A CB 1 ATOM 2226 C CG . PRO A 1 290 ? 27.415 47.635 11.057 1.00 36.84 ? 331 PRO A CG 1 ATOM 2227 C CD . PRO A 1 290 ? 28.597 48.196 11.819 1.00 35.71 ? 331 PRO A CD 1 ATOM 2228 N N . GLY A 1 291 ? 27.824 43.686 12.553 1.00 35.09 ? 332 GLY A N 1 ATOM 2229 C CA . GLY A 1 291 ? 28.033 42.407 11.876 1.00 34.96 ? 332 GLY A CA 1 ATOM 2230 C C . GLY A 1 291 ? 29.370 41.744 12.125 1.00 35.45 ? 332 GLY A C 1 ATOM 2231 O O . GLY A 1 291 ? 30.197 42.246 12.905 1.00 34.79 ? 332 GLY A O 1 ATOM 2232 N N . PHE A 1 292 ? 29.586 40.632 11.409 1.00 35.86 ? 333 PHE A N 1 ATOM 2233 C CA . PHE A 1 292 ? 30.741 39.763 11.586 1.00 36.73 ? 333 PHE A CA 1 ATOM 2234 C C . PHE A 1 292 ? 31.804 40.043 10.506 1.00 38.05 ? 333 PHE A C 1 ATOM 2235 O O . PHE A 1 292 ? 31.498 40.701 9.503 1.00 38.01 ? 333 PHE A O 1 ATOM 2236 C CB . PHE A 1 292 ? 30.317 38.294 11.473 1.00 36.76 ? 333 PHE A CB 1 ATOM 2237 C CG . PHE A 1 292 ? 29.432 37.811 12.596 1.00 37.08 ? 333 PHE A CG 1 ATOM 2238 C CD1 . PHE A 1 292 ? 28.485 36.829 12.368 1.00 36.88 ? 333 PHE A CD1 1 ATOM 2239 C CD2 . PHE A 1 292 ? 29.543 38.349 13.874 1.00 36.45 ? 333 PHE A CD2 1 ATOM 2240 C CE1 . PHE A 1 292 ? 27.668 36.365 13.393 1.00 37.85 ? 333 PHE A CE1 1 ATOM 2241 C CE2 . PHE A 1 292 ? 28.723 37.890 14.920 1.00 34.31 ? 333 PHE A CE2 1 ATOM 2242 C CZ . PHE A 1 292 ? 27.789 36.906 14.678 1.00 32.48 ? 333 PHE A CZ 1 ATOM 2243 N N . THR A 1 293 ? 33.034 39.579 10.735 1.00 38.96 ? 334 THR A N 1 ATOM 2244 C CA . THR A 1 293 ? 34.117 39.762 9.739 1.00 41.74 ? 334 THR A CA 1 ATOM 2245 C C . THR A 1 293 ? 33.859 38.987 8.439 1.00 43.56 ? 334 THR A C 1 ATOM 2246 O O . THR A 1 293 ? 33.082 38.024 8.408 1.00 43.48 ? 334 THR A O 1 ATOM 2247 C CB . THR A 1 293 ? 35.505 39.356 10.269 1.00 41.75 ? 334 THR A CB 1 ATOM 2248 O OG1 . THR A 1 293 ? 35.455 38.040 10.832 1.00 41.81 ? 334 THR A OG1 1 ATOM 2249 C CG2 . THR A 1 293 ? 36.022 40.341 11.289 1.00 42.08 ? 334 THR A CG2 1 ATOM 2250 N N . GLY A 1 294 ? 34.559 39.393 7.375 1.00 45.07 ? 335 GLY A N 1 ATOM 2251 C CA . GLY A 1 294 ? 34.314 38.898 6.015 1.00 47.01 ? 335 GLY A CA 1 ATOM 2252 C C . GLY A 1 294 ? 33.870 37.464 5.790 1.00 47.99 ? 335 GLY A C 1 ATOM 2253 O O . GLY A 1 294 ? 32.880 37.227 5.093 1.00 48.94 ? 335 GLY A O 1 ATOM 2254 N N . ASN A 1 295 ? 34.604 36.504 6.344 1.00 48.26 ? 336 ASN A N 1 ATOM 2255 C CA . ASN A 1 295 ? 34.250 35.089 6.176 1.00 49.26 ? 336 ASN A CA 1 ATOM 2256 C C . ASN A 1 295 ? 32.848 34.758 6.671 1.00 48.26 ? 336 ASN A C 1 ATOM 2257 O O . ASN A 1 295 ? 32.192 33.851 6.166 1.00 48.62 ? 336 ASN A O 1 ATOM 2258 C CB . ASN A 1 295 ? 35.253 34.188 6.912 1.00 49.86 ? 336 ASN A CB 1 ATOM 2259 C CG . ASN A 1 295 ? 36.640 34.166 6.254 1.00 54.57 ? 336 ASN A CG 1 ATOM 2260 O OD1 . ASN A 1 295 ? 36.959 34.988 5.370 1.00 57.77 ? 336 ASN A OD1 1 ATOM 2261 N ND2 . ASN A 1 295 ? 37.477 33.211 6.688 1.00 58.02 ? 336 ASN A ND2 1 ATOM 2262 N N . PHE A 1 296 ? 32.394 35.505 7.674 1.00 46.72 ? 337 PHE A N 1 ATOM 2263 C CA . PHE A 1 296 ? 31.147 35.200 8.346 1.00 45.22 ? 337 PHE A CA 1 ATOM 2264 C C . PHE A 1 296 ? 30.102 36.284 8.136 1.00 44.90 ? 337 PHE A C 1 ATOM 2265 O O . PHE A 1 296 ? 29.048 36.276 8.789 1.00 44.28 ? 337 PHE A O 1 ATOM 2266 C CB . PHE A 1 296 ? 31.424 35.034 9.834 1.00 44.43 ? 337 PHE A CB 1 ATOM 2267 C CG . PHE A 1 296 ? 32.567 34.110 10.132 1.00 43.87 ? 337 PHE A CG 1 ATOM 2268 C CD1 . PHE A 1 296 ? 33.801 34.617 10.519 1.00 43.58 ? 337 PHE A CD1 1 ATOM 2269 C CD2 . PHE A 1 296 ? 32.408 32.728 10.015 1.00 43.53 ? 337 PHE A CD2 1 ATOM 2270 C CE1 . PHE A 1 296 ? 34.865 33.763 10.805 1.00 43.40 ? 337 PHE A CE1 1 ATOM 2271 C CE2 . PHE A 1 296 ? 33.465 31.858 10.295 1.00 43.60 ? 337 PHE A CE2 1 ATOM 2272 C CZ . PHE A 1 296 ? 34.699 32.381 10.692 1.00 44.07 ? 337 PHE A CZ 1 ATOM 2273 N N . SER A 1 297 ? 30.395 37.203 7.222 1.00 44.41 ? 338 SER A N 1 ATOM 2274 C CA . SER A 1 297 ? 29.555 38.359 6.966 1.00 44.22 ? 338 SER A CA 1 ATOM 2275 C C . SER A 1 297 ? 28.106 38.006 6.653 1.00 43.35 ? 338 SER A C 1 ATOM 2276 O O . SER A 1 297 ? 27.205 38.821 6.907 1.00 43.95 ? 338 SER A O 1 ATOM 2277 C CB . SER A 1 297 ? 30.147 39.191 5.836 1.00 45.12 ? 338 SER A CB 1 ATOM 2278 O OG . SER A 1 297 ? 30.039 38.482 4.612 1.00 47.53 ? 338 SER A OG 1 ATOM 2279 N N . THR A 1 298 ? 27.851 36.802 6.140 1.00 42.16 ? 339 THR A N 1 ATOM 2280 C CA . THR A 1 298 ? 26.471 36.439 5.786 1.00 41.01 ? 339 THR A CA 1 ATOM 2281 C C . THR A 1 298 ? 25.718 35.732 6.911 1.00 40.34 ? 339 THR A C 1 ATOM 2282 O O . THR A 1 298 ? 24.525 35.431 6.786 1.00 40.09 ? 339 THR A O 1 ATOM 2283 C CB . THR A 1 298 ? 26.383 35.599 4.503 1.00 41.91 ? 339 THR A CB 1 ATOM 2284 O OG1 . THR A 1 298 ? 27.158 34.412 4.669 1.00 42.59 ? 339 THR A OG1 1 ATOM 2285 C CG2 . THR A 1 298 ? 26.898 36.406 3.333 1.00 42.12 ? 339 THR A CG2 1 ATOM 2286 N N . GLN A 1 299 ? 26.433 35.456 7.995 1.00 38.31 ? 340 GLN A N 1 ATOM 2287 C CA . GLN A 1 299 ? 25.806 34.869 9.164 1.00 37.67 ? 340 GLN A CA 1 ATOM 2288 C C . GLN A 1 299 ? 25.106 35.995 9.913 1.00 36.95 ? 340 GLN A C 1 ATOM 2289 O O . GLN A 1 299 ? 25.455 37.175 9.752 1.00 36.28 ? 340 GLN A O 1 ATOM 2290 C CB . GLN A 1 299 ? 26.840 34.186 10.034 1.00 36.81 ? 340 GLN A CB 1 ATOM 2291 C CG . GLN A 1 299 ? 27.492 33.040 9.281 1.00 37.69 ? 340 GLN A CG 1 ATOM 2292 C CD . GLN A 1 299 ? 28.470 32.226 10.098 1.00 39.66 ? 340 GLN A CD 1 ATOM 2293 O OE1 . GLN A 1 299 ? 28.902 32.618 11.188 1.00 39.89 ? 340 GLN A OE1 1 ATOM 2294 N NE2 . GLN A 1 299 ? 28.848 31.069 9.551 1.00 42.00 ? 340 GLN A NE2 1 ATOM 2295 N N . LYS A 1 300 ? 24.080 35.624 10.673 1.00 35.88 ? 341 LYS A N 1 ATOM 2296 C CA . LYS A 1 300 ? 23.310 36.603 11.440 1.00 34.82 ? 341 LYS A CA 1 ATOM 2297 C C . LYS A 1 300 ? 23.028 36.036 12.823 1.00 33.56 ? 341 LYS A C 1 ATOM 2298 O O . LYS A 1 300 ? 23.234 34.847 13.084 1.00 32.36 ? 341 LYS A O 1 ATOM 2299 C CB . LYS A 1 300 ? 22.000 36.984 10.714 1.00 35.88 ? 341 LYS A CB 1 ATOM 2300 C CG . LYS A 1 300 ? 22.210 37.817 9.425 1.00 39.34 ? 341 LYS A CG 1 ATOM 2301 C CD . LYS A 1 300 ? 20.987 38.645 9.035 1.00 45.66 ? 341 LYS A CD 1 ATOM 2302 C CE . LYS A 1 300 ? 21.082 39.194 7.596 1.00 50.59 ? 341 LYS A CE 1 ATOM 2303 N NZ . LYS A 1 300 ? 22.294 40.063 7.356 1.00 52.09 ? 341 LYS A NZ 1 ATOM 2304 N N . VAL A 1 301 ? 22.559 36.905 13.717 1.00 31.16 ? 342 VAL A N 1 ATOM 2305 C CA . VAL A 1 301 ? 22.146 36.460 15.044 1.00 30.14 ? 342 VAL A CA 1 ATOM 2306 C C . VAL A 1 301 ? 20.626 36.480 15.142 1.00 29.32 ? 342 VAL A C 1 ATOM 2307 O O . VAL A 1 301 ? 19.991 37.425 14.684 1.00 30.57 ? 342 VAL A O 1 ATOM 2308 C CB . VAL A 1 301 ? 22.794 37.325 16.127 1.00 29.92 ? 342 VAL A CB 1 ATOM 2309 C CG1 . VAL A 1 301 ? 22.090 37.091 17.469 1.00 27.37 ? 342 VAL A CG1 1 ATOM 2310 C CG2 . VAL A 1 301 ? 24.290 36.987 16.224 1.00 30.04 ? 342 VAL A CG2 1 ATOM 2311 N N . LYS A 1 302 ? 20.047 35.430 15.719 1.00 28.37 ? 343 LYS A N 1 ATOM 2312 C CA . LYS A 1 302 ? 18.601 35.327 15.834 1.00 29.04 ? 343 LYS A CA 1 ATOM 2313 C C . LYS A 1 302 ? 18.202 35.071 17.282 1.00 28.69 ? 343 LYS A C 1 ATOM 2314 O O . LYS A 1 302 ? 18.664 34.111 17.884 1.00 28.24 ? 343 LYS A O 1 ATOM 2315 C CB . LYS A 1 302 ? 18.092 34.149 14.994 1.00 30.66 ? 343 LYS A CB 1 ATOM 2316 C CG . LYS A 1 302 ? 16.560 34.071 14.954 1.00 31.94 ? 343 LYS A CG 1 ATOM 2317 C CD . LYS A 1 302 ? 16.063 32.946 14.014 1.00 35.56 ? 343 LYS A CD 1 ATOM 2318 C CE . LYS A 1 302 ? 14.530 32.964 13.950 1.00 39.15 ? 343 LYS A CE 1 ATOM 2319 N NZ . LYS A 1 302 ? 14.019 32.362 12.671 1.00 42.40 ? 343 LYS A NZ 1 ATOM 2320 N N . MET A 1 303 ? 17.340 35.919 17.841 1.00 28.19 ? 344 MET A N 1 ATOM 2321 C CA . MET A 1 303 ? 16.779 35.658 19.174 1.00 27.20 ? 344 MET A CA 1 ATOM 2322 C C . MET A 1 303 ? 15.483 34.839 19.082 1.00 28.06 ? 344 MET A C 1 ATOM 2323 O O . MET A 1 303 ? 14.759 34.924 18.094 1.00 29.69 ? 344 MET A O 1 ATOM 2324 C CB . MET A 1 303 ? 16.466 37.006 19.855 1.00 25.45 ? 344 MET A CB 1 ATOM 2325 C CG . MET A 1 303 ? 17.658 37.904 19.856 1.00 24.81 ? 344 MET A CG 1 ATOM 2326 S SD . MET A 1 303 ? 17.373 39.496 20.730 1.00 8.28 ? 344 MET A SD 1 ATOM 2327 C CE . MET A 1 303 ? 17.217 38.837 22.412 1.00 24.90 ? 344 MET A CE 1 ATOM 2328 N N . HIS A 1 304 ? 15.170 34.068 20.115 1.00 27.20 ? 345 HIS A N 1 ATOM 2329 C CA . HIS A 1 304 ? 13.891 33.394 20.158 1.00 26.50 ? 345 HIS A CA 1 ATOM 2330 C C . HIS A 1 304 ? 13.344 33.592 21.568 1.00 25.68 ? 345 HIS A C 1 ATOM 2331 O O . HIS A 1 304 ? 13.775 32.907 22.503 1.00 25.53 ? 345 HIS A O 1 ATOM 2332 C CB . HIS A 1 304 ? 14.026 31.892 19.871 1.00 28.01 ? 345 HIS A CB 1 ATOM 2333 C CG . HIS A 1 304 ? 15.065 31.540 18.839 1.00 30.06 ? 345 HIS A CG 1 ATOM 2334 N ND1 . HIS A 1 304 ? 14.736 31.083 17.578 1.00 35.00 ? 345 HIS A ND1 1 ATOM 2335 C CD2 . HIS A 1 304 ? 16.418 31.527 18.903 1.00 29.97 ? 345 HIS A CD2 1 ATOM 2336 C CE1 . HIS A 1 304 ? 15.845 30.836 16.896 1.00 32.45 ? 345 HIS A CE1 1 ATOM 2337 N NE2 . HIS A 1 304 ? 16.881 31.087 17.678 1.00 35.13 ? 345 HIS A NE2 1 ATOM 2338 N N . ILE A 1 305 ? 12.404 34.512 21.698 1.00 24.86 ? 346 ILE A N 1 ATOM 2339 C CA . ILE A 1 305 ? 11.887 34.855 23.036 1.00 24.29 ? 346 ILE A CA 1 ATOM 2340 C C . ILE A 1 305 ? 10.389 34.581 23.048 1.00 24.68 ? 346 ILE A C 1 ATOM 2341 O O . ILE A 1 305 ? 9.637 35.127 22.209 1.00 24.87 ? 346 ILE A O 1 ATOM 2342 C CB . ILE A 1 305 ? 12.204 36.331 23.383 1.00 24.80 ? 346 ILE A CB 1 ATOM 2343 C CG1 . ILE A 1 305 ? 13.701 36.649 23.204 1.00 22.68 ? 346 ILE A CG1 1 ATOM 2344 C CG2 . ILE A 1 305 ? 11.677 36.680 24.811 1.00 25.23 ? 346 ILE A CG2 1 ATOM 2345 C CD1 . ILE A 1 305 ? 14.681 35.748 24.039 1.00 26.86 ? 346 ILE A CD1 1 ATOM 2346 N N . HIS A 1 306 ? 9.950 33.775 24.016 1.00 24.67 ? 347 HIS A N 1 ATOM 2347 C CA . HIS A 1 306 ? 8.551 33.308 24.092 1.00 24.64 ? 347 HIS A CA 1 ATOM 2348 C C . HIS A 1 306 ? 7.887 33.443 25.472 1.00 24.08 ? 347 HIS A C 1 ATOM 2349 O O . HIS A 1 306 ? 6.787 32.901 25.759 1.00 23.86 ? 347 HIS A O 1 ATOM 2350 C CB . HIS A 1 306 ? 8.447 31.858 23.602 1.00 26.33 ? 347 HIS A CB 1 ATOM 2351 C CG . HIS A 1 306 ? 9.114 31.635 22.281 1.00 31.58 ? 347 HIS A CG 1 ATOM 2352 N ND1 . HIS A 1 306 ? 10.233 30.845 22.139 1.00 35.83 ? 347 HIS A ND1 1 ATOM 2353 C CD2 . HIS A 1 306 ? 8.834 32.129 21.048 1.00 35.72 ? 347 HIS A CD2 1 ATOM 2354 C CE1 . HIS A 1 306 ? 10.614 30.857 20.869 1.00 35.40 ? 347 HIS A CE1 1 ATOM 2355 N NE2 . HIS A 1 306 ? 9.779 31.623 20.188 1.00 37.84 ? 347 HIS A NE2 1 ATOM 2356 N N . SER A 1 307 ? 8.541 34.253 26.300 1.00 22.35 ? 348 SER A N 1 ATOM 2357 C CA . SER A 1 307 ? 8.036 34.536 27.656 1.00 20.31 ? 348 SER A CA 1 ATOM 2358 C C . SER A 1 307 ? 6.674 35.195 27.562 1.00 22.43 ? 348 SER A C 1 ATOM 2359 O O . SER A 1 307 ? 6.382 35.852 26.560 1.00 22.48 ? 348 SER A O 1 ATOM 2360 C CB . SER A 1 307 ? 9.001 35.492 28.362 1.00 20.62 ? 348 SER A CB 1 ATOM 2361 O OG . SER A 1 307 ? 10.313 34.930 28.383 1.00 20.44 ? 348 SER A OG 1 ATOM 2362 N N . THR A 1 308 ? 5.894 35.086 28.640 1.00 21.16 ? 349 THR A N 1 ATOM 2363 C CA . THR A 1 308 ? 4.562 35.707 28.645 1.00 21.49 ? 349 THR A CA 1 ATOM 2364 C C . THR A 1 308 ? 4.376 36.535 29.901 1.00 21.89 ? 349 THR A C 1 ATOM 2365 O O . THR A 1 308 ? 4.844 36.148 30.963 1.00 22.43 ? 349 THR A O 1 ATOM 2366 C CB . THR A 1 308 ? 3.459 34.671 28.616 1.00 23.40 ? 349 THR A CB 1 ATOM 2367 O OG1 . THR A 1 308 ? 3.607 33.818 29.751 1.00 28.99 ? 349 THR A OG1 1 ATOM 2368 C CG2 . THR A 1 308 ? 3.606 33.827 27.359 1.00 22.22 ? 349 THR A CG2 1 ATOM 2369 N N . ASN A 1 309 ? 3.672 37.641 29.760 1.00 20.74 ? 350 ASN A N 1 ATOM 2370 C CA . ASN A 1 309 ? 3.353 38.478 30.921 1.00 20.97 ? 350 ASN A CA 1 ATOM 2371 C C . ASN A 1 309 ? 1.993 37.983 31.404 1.00 21.78 ? 350 ASN A C 1 ATOM 2372 O O . ASN A 1 309 ? 1.078 37.729 30.587 1.00 23.36 ? 350 ASN A O 1 ATOM 2373 C CB . ASN A 1 309 ? 3.221 39.925 30.449 1.00 20.59 ? 350 ASN A CB 1 ATOM 2374 C CG . ASN A 1 309 ? 4.506 40.498 29.971 1.00 23.00 ? 350 ASN A CG 1 ATOM 2375 O OD1 . ASN A 1 309 ? 5.552 40.151 30.458 1.00 21.86 ? 350 ASN A OD1 1 ATOM 2376 N ND2 . ASN A 1 309 ? 4.435 41.414 29.006 1.00 26.34 ? 350 ASN A ND2 1 ATOM 2377 N N . GLU A 1 310 ? 1.801 37.880 32.717 1.00 21.30 ? 351 GLU A N 1 ATOM 2378 C CA . GLU A 1 310 ? 0.558 37.322 33.220 1.00 21.80 ? 351 GLU A CA 1 ATOM 2379 C C . GLU A 1 310 ? 0.244 37.922 34.549 1.00 20.59 ? 351 GLU A C 1 ATOM 2380 O O . GLU A 1 310 ? 1.136 38.015 35.429 1.00 19.68 ? 351 GLU A O 1 ATOM 2381 C CB . GLU A 1 310 ? 0.692 35.840 33.517 1.00 24.43 ? 351 GLU A CB 1 ATOM 2382 C CG . GLU A 1 310 ? 1.642 35.100 32.653 1.00 31.53 ? 351 GLU A CG 1 ATOM 2383 C CD . GLU A 1 310 ? 1.357 33.630 32.696 1.00 42.63 ? 351 GLU A CD 1 ATOM 2384 O OE1 . GLU A 1 310 ? 1.108 33.084 31.589 1.00 49.26 ? 351 GLU A OE1 1 ATOM 2385 O OE2 . GLU A 1 310 ? 1.361 33.038 33.822 1.00 41.82 ? 351 GLU A OE2 1 ATOM 2386 N N . VAL A 1 311 ? -1.016 38.300 34.693 1.00 18.97 ? 352 VAL A N 1 ATOM 2387 C CA . VAL A 1 311 ? -1.455 38.839 35.991 1.00 17.57 ? 352 VAL A CA 1 ATOM 2388 C C . VAL A 1 311 ? -1.464 37.681 36.994 1.00 18.87 ? 352 VAL A C 1 ATOM 2389 O O . VAL A 1 311 ? -2.116 36.635 36.771 1.00 19.47 ? 352 VAL A O 1 ATOM 2390 C CB . VAL A 1 311 ? -2.825 39.502 35.897 1.00 18.03 ? 352 VAL A CB 1 ATOM 2391 C CG1 . VAL A 1 311 ? -3.314 39.910 37.260 1.00 18.07 ? 352 VAL A CG1 1 ATOM 2392 C CG2 . VAL A 1 311 ? -2.742 40.736 34.975 1.00 18.68 ? 352 VAL A CG2 1 ATOM 2393 N N . THR A 1 312 ? -0.818 37.897 38.137 1.00 17.33 ? 353 THR A N 1 ATOM 2394 C CA . THR A 1 312 ? -0.515 36.812 39.078 1.00 17.66 ? 353 THR A CA 1 ATOM 2395 C C . THR A 1 312 ? -0.641 37.343 40.500 1.00 17.81 ? 353 THR A C 1 ATOM 2396 O O . THR A 1 312 ? -0.314 38.525 40.758 1.00 18.15 ? 353 THR A O 1 ATOM 2397 C CB . THR A 1 312 ? 0.902 36.268 38.836 1.00 18.63 ? 353 THR A CB 1 ATOM 2398 O OG1 . THR A 1 312 ? 1.051 35.929 37.427 1.00 19.99 ? 353 THR A OG1 1 ATOM 2399 C CG2 . THR A 1 312 ? 1.174 35.041 39.685 1.00 19.12 ? 353 THR A CG2 1 ATOM 2400 N N . ARG A 1 313 ? -1.132 36.512 41.413 1.00 17.67 ? 354 ARG A N 1 ATOM 2401 C CA . ARG A 1 313 ? -1.288 36.956 42.815 1.00 16.98 ? 354 ARG A CA 1 ATOM 2402 C C . ARG A 1 313 ? 0.047 36.915 43.569 1.00 17.62 ? 354 ARG A C 1 ATOM 2403 O O . ARG A 1 313 ? 0.813 35.920 43.419 1.00 16.75 ? 354 ARG A O 1 ATOM 2404 C CB . ARG A 1 313 ? -2.364 36.101 43.552 1.00 17.69 ? 354 ARG A CB 1 ATOM 2405 C CG . ARG A 1 313 ? -2.672 36.602 44.977 1.00 19.61 ? 354 ARG A CG 1 ATOM 2406 C CD . ARG A 1 313 ? -4.071 36.131 45.399 1.00 20.48 ? 354 ARG A CD 1 ATOM 2407 N NE . ARG A 1 313 ? -5.048 36.891 44.630 1.00 19.33 ? 354 ARG A NE 1 ATOM 2408 C CZ . ARG A 1 313 ? -6.360 36.852 44.858 1.00 24.43 ? 354 ARG A CZ 1 ATOM 2409 N NH1 . ARG A 1 313 ? -6.831 36.064 45.844 1.00 22.75 ? 354 ARG A NH1 1 ATOM 2410 N NH2 . ARG A 1 313 ? -7.180 37.596 44.120 1.00 26.78 ? 354 ARG A NH2 1 ATOM 2411 N N . ILE A 1 314 ? 0.284 37.959 44.371 1.00 16.28 ? 355 ILE A N 1 ATOM 2412 C CA . ILE A 1 314 ? 1.508 38.067 45.208 1.00 16.13 ? 355 ILE A CA 1 ATOM 2413 C C . ILE A 1 314 ? 1.039 38.356 46.631 1.00 16.67 ? 355 ILE A C 1 ATOM 2414 O O . ILE A 1 314 ? -0.094 38.857 46.818 1.00 16.48 ? 355 ILE A O 1 ATOM 2415 C CB . ILE A 1 314 ? 2.432 39.191 44.684 1.00 14.95 ? 355 ILE A CB 1 ATOM 2416 C CG1 . ILE A 1 314 ? 1.730 40.554 44.658 1.00 15.37 ? 355 ILE A CG1 1 ATOM 2417 C CG2 . ILE A 1 314 ? 2.861 38.818 43.267 1.00 15.60 ? 355 ILE A CG2 1 ATOM 2418 C CD1 . ILE A 1 314 ? 2.690 41.749 44.632 1.00 15.47 ? 355 ILE A CD1 1 ATOM 2419 N N . TYR A 1 315 ? 1.912 38.104 47.597 1.00 15.81 ? 356 TYR A N 1 ATOM 2420 C CA . TYR A 1 315 ? 1.542 38.170 49.024 1.00 16.20 ? 356 TYR A CA 1 ATOM 2421 C C . TYR A 1 315 ? 2.627 38.854 49.852 1.00 15.42 ? 356 TYR A C 1 ATOM 2422 O O . TYR A 1 315 ? 3.744 38.332 49.987 1.00 16.27 ? 356 TYR A O 1 ATOM 2423 C CB . TYR A 1 315 ? 1.408 36.750 49.573 1.00 15.68 ? 356 TYR A CB 1 ATOM 2424 C CG . TYR A 1 315 ? 0.334 35.930 48.879 1.00 17.71 ? 356 TYR A CG 1 ATOM 2425 C CD1 . TYR A 1 315 ? -0.978 35.941 49.354 1.00 20.19 ? 356 TYR A CD1 1 ATOM 2426 C CD2 . TYR A 1 315 ? 0.654 35.168 47.753 1.00 19.15 ? 356 TYR A CD2 1 ATOM 2427 C CE1 . TYR A 1 315 ? -1.949 35.185 48.726 1.00 19.54 ? 356 TYR A CE1 1 ATOM 2428 C CE2 . TYR A 1 315 ? -0.319 34.405 47.088 1.00 18.64 ? 356 TYR A CE2 1 ATOM 2429 C CZ . TYR A 1 315 ? -1.622 34.447 47.580 1.00 21.22 ? 356 TYR A CZ 1 ATOM 2430 O OH . TYR A 1 315 ? -2.609 33.690 46.908 1.00 23.87 ? 356 TYR A OH 1 ATOM 2431 N N . ASN A 1 316 ? 2.277 39.984 50.458 1.00 16.34 ? 357 ASN A N 1 ATOM 2432 C CA . ASN A 1 316 ? 3.164 40.602 51.447 1.00 16.40 ? 357 ASN A CA 1 ATOM 2433 C C . ASN A 1 316 ? 2.785 40.098 52.831 1.00 16.46 ? 357 ASN A C 1 ATOM 2434 O O . ASN A 1 316 ? 1.568 39.948 53.126 1.00 18.51 ? 357 ASN A O 1 ATOM 2435 C CB . ASN A 1 316 ? 2.961 42.112 51.495 1.00 15.74 ? 357 ASN A CB 1 ATOM 2436 C CG . ASN A 1 316 ? 3.318 42.804 50.183 1.00 16.37 ? 357 ASN A CG 1 ATOM 2437 O OD1 . ASN A 1 316 ? 4.182 42.382 49.424 1.00 17.17 ? 357 ASN A OD1 1 ATOM 2438 N ND2 . ASN A 1 316 ? 2.625 43.932 49.927 1.00 17.39 ? 357 ASN A ND2 1 ATOM 2439 N N . VAL A 1 317 ? 3.763 39.903 53.707 1.00 16.21 ? 358 VAL A N 1 ATOM 2440 C CA . VAL A 1 317 ? 3.380 39.621 55.126 1.00 16.25 ? 358 VAL A CA 1 ATOM 2441 C C . VAL A 1 317 ? 3.572 40.935 55.893 1.00 16.45 ? 358 VAL A C 1 ATOM 2442 O O . VAL A 1 317 ? 4.662 41.521 55.785 1.00 17.92 ? 358 VAL A O 1 ATOM 2443 C CB . VAL A 1 317 ? 4.248 38.510 55.751 1.00 16.94 ? 358 VAL A CB 1 ATOM 2444 C CG1 . VAL A 1 317 ? 3.656 38.118 57.162 1.00 17.93 ? 358 VAL A CG1 1 ATOM 2445 C CG2 . VAL A 1 317 ? 4.301 37.251 54.873 1.00 18.57 ? 358 VAL A CG2 1 ATOM 2446 N N . ILE A 1 318 ? 2.552 41.369 56.659 1.00 17.04 ? 359 ILE A N 1 ATOM 2447 C CA . ILE A 1 318 ? 2.629 42.635 57.403 1.00 16.41 ? 359 ILE A CA 1 ATOM 2448 C C . ILE A 1 318 ? 2.402 42.328 58.889 1.00 16.69 ? 359 ILE A C 1 ATOM 2449 O O . ILE A 1 318 ? 1.300 41.910 59.257 1.00 18.73 ? 359 ILE A O 1 ATOM 2450 C CB . ILE A 1 318 ? 1.553 43.641 56.909 1.00 17.58 ? 359 ILE A CB 1 ATOM 2451 C CG1 . ILE A 1 318 ? 1.605 43.807 55.371 1.00 17.43 ? 359 ILE A CG1 1 ATOM 2452 C CG2 . ILE A 1 318 ? 1.649 44.983 57.685 1.00 17.60 ? 359 ILE A CG2 1 ATOM 2453 C CD1 . ILE A 1 318 ? 2.891 44.490 54.906 1.00 21.27 ? 359 ILE A CD1 1 ATOM 2454 N N . GLY A 1 319 ? 3.437 42.529 59.675 1.00 18.27 ? 360 GLY A N 1 ATOM 2455 C CA . GLY A 1 319 ? 3.409 42.297 61.158 1.00 18.54 ? 360 GLY A CA 1 ATOM 2456 C C . GLY A 1 319 ? 3.357 43.614 61.878 1.00 19.57 ? 360 GLY A C 1 ATOM 2457 O O . GLY A 1 319 ? 4.012 44.565 61.465 1.00 19.00 ? 360 GLY A O 1 ATOM 2458 N N . THR A 1 320 ? 2.605 43.665 62.985 1.00 19.38 ? 361 THR A N 1 ATOM 2459 C CA . THR A 1 320 ? 2.440 44.920 63.729 1.00 20.24 ? 361 THR A CA 1 ATOM 2460 C C . THR A 1 320 ? 2.841 44.675 65.167 1.00 21.05 ? 361 THR A C 1 ATOM 2461 O O . THR A 1 320 ? 2.418 43.682 65.763 1.00 22.04 ? 361 THR A O 1 ATOM 2462 C CB . THR A 1 320 ? 0.957 45.361 63.696 1.00 21.55 ? 361 THR A CB 1 ATOM 2463 O OG1 . THR A 1 320 ? 0.571 45.606 62.337 1.00 22.28 ? 361 THR A OG1 1 ATOM 2464 C CG2 . THR A 1 320 ? 0.709 46.657 64.501 1.00 22.00 ? 361 THR A CG2 1 ATOM 2465 N N . LEU A 1 321 ? 3.649 45.575 65.712 1.00 20.31 ? 362 LEU A N 1 ATOM 2466 C CA . LEU A 1 321 ? 3.943 45.606 67.188 1.00 19.96 ? 362 LEU A CA 1 ATOM 2467 C C . LEU A 1 321 ? 3.479 46.978 67.622 1.00 21.36 ? 362 LEU A C 1 ATOM 2468 O O . LEU A 1 321 ? 4.151 47.988 67.361 1.00 20.77 ? 362 LEU A O 1 ATOM 2469 C CB . LEU A 1 321 ? 5.456 45.413 67.379 1.00 21.28 ? 362 LEU A CB 1 ATOM 2470 C CG . LEU A 1 321 ? 5.937 45.435 68.846 1.00 26.03 ? 362 LEU A CG 1 ATOM 2471 C CD1 . LEU A 1 321 ? 5.151 44.470 69.678 1.00 28.42 ? 362 LEU A CD1 1 ATOM 2472 C CD2 . LEU A 1 321 ? 7.404 45.087 68.882 1.00 25.61 ? 362 LEU A CD2 1 ATOM 2473 N N . ARG A 1 322 ? 2.286 47.005 68.208 1.00 20.55 ? 363 ARG A N 1 ATOM 2474 C CA . ARG A 1 322 ? 1.631 48.278 68.568 1.00 22.01 ? 363 ARG A CA 1 ATOM 2475 C C . ARG A 1 322 ? 2.438 49.112 69.587 1.00 22.45 ? 363 ARG A C 1 ATOM 2476 O O . ARG A 1 322 ? 2.916 48.572 70.602 1.00 22.69 ? 363 ARG A O 1 ATOM 2477 C CB . ARG A 1 322 ? 0.221 47.979 69.078 1.00 22.79 ? 363 ARG A CB 1 ATOM 2478 C CG . ARG A 1 322 ? -0.483 49.183 69.624 1.00 26.91 ? 363 ARG A CG 1 ATOM 2479 C CD . ARG A 1 322 ? -1.937 48.820 69.908 1.00 34.05 ? 363 ARG A CD 1 ATOM 2480 N NE . ARG A 1 322 ? -2.117 47.391 70.229 1.00 42.69 ? 363 ARG A NE 1 ATOM 2481 C CZ . ARG A 1 322 ? -1.940 46.835 71.426 1.00 46.43 ? 363 ARG A CZ 1 ATOM 2482 N NH1 . ARG A 1 322 ? -1.568 47.571 72.478 1.00 49.95 ? 363 ARG A NH1 1 ATOM 2483 N NH2 . ARG A 1 322 ? -2.140 45.528 71.570 1.00 47.97 ? 363 ARG A NH2 1 ATOM 2484 N N . GLY A 1 323 ? 2.600 50.421 69.336 1.00 21.29 ? 364 GLY A N 1 ATOM 2485 C CA . GLY A 1 323 ? 3.313 51.313 70.269 1.00 21.35 ? 364 GLY A CA 1 ATOM 2486 C C . GLY A 1 323 ? 2.519 51.543 71.556 1.00 21.86 ? 364 GLY A C 1 ATOM 2487 O O . GLY A 1 323 ? 1.276 51.615 71.537 1.00 23.16 ? 364 GLY A O 1 ATOM 2488 N N . ALA A 1 324 ? 3.246 51.672 72.665 1.00 23.08 ? 365 ALA A N 1 ATOM 2489 C CA . ALA A 1 324 ? 2.617 51.963 73.970 1.00 23.77 ? 365 ALA A CA 1 ATOM 2490 C C . ALA A 1 324 ? 2.140 53.391 74.122 1.00 25.21 ? 365 ALA A C 1 ATOM 2491 O O . ALA A 1 324 ? 1.175 53.651 74.903 1.00 26.31 ? 365 ALA A O 1 ATOM 2492 C CB . ALA A 1 324 ? 3.620 51.645 75.064 1.00 23.42 ? 365 ALA A CB 1 ATOM 2493 N N . VAL A 1 325 ? 2.822 54.345 73.473 1.00 22.78 ? 366 VAL A N 1 ATOM 2494 C CA . VAL A 1 325 ? 2.514 55.768 73.716 1.00 24.19 ? 366 VAL A CA 1 ATOM 2495 C C . VAL A 1 325 ? 2.002 56.469 72.451 1.00 24.02 ? 366 VAL A C 1 ATOM 2496 O O . VAL A 1 325 ? 1.019 57.232 72.482 1.00 24.06 ? 366 VAL A O 1 ATOM 2497 C CB . VAL A 1 325 ? 3.740 56.508 74.311 1.00 25.31 ? 366 VAL A CB 1 ATOM 2498 C CG1 . VAL A 1 325 ? 3.431 57.993 74.483 1.00 25.22 ? 366 VAL A CG1 1 ATOM 2499 C CG2 . VAL A 1 325 ? 4.136 55.909 75.672 1.00 27.31 ? 366 VAL A CG2 1 ATOM 2500 N N . GLU A 1 326 ? 2.667 56.175 71.329 1.00 22.07 ? 367 GLU A N 1 ATOM 2501 C CA . GLU A 1 326 ? 2.319 56.768 70.038 1.00 22.60 ? 367 GLU A CA 1 ATOM 2502 C C . GLU A 1 326 ? 2.026 55.667 69.025 1.00 20.89 ? 367 GLU A C 1 ATOM 2503 O O . GLU A 1 326 ? 2.809 55.487 68.071 1.00 20.14 ? 367 GLU A O 1 ATOM 2504 C CB . GLU A 1 326 ? 3.445 57.658 69.546 1.00 22.38 ? 367 GLU A CB 1 ATOM 2505 C CG . GLU A 1 326 ? 3.705 58.875 70.424 1.00 25.83 ? 367 GLU A CG 1 ATOM 2506 C CD . GLU A 1 326 ? 4.701 59.821 69.766 1.00 23.24 ? 367 GLU A CD 1 ATOM 2507 O OE1 . GLU A 1 326 ? 4.239 60.741 69.075 1.00 24.91 ? 367 GLU A OE1 1 ATOM 2508 O OE2 . GLU A 1 326 ? 5.928 59.656 69.983 1.00 27.68 ? 367 GLU A OE2 1 ATOM 2509 N N . PRO A 1 327 ? 0.915 54.936 69.215 1.00 20.84 ? 368 PRO A N 1 ATOM 2510 C CA . PRO A 1 327 ? 0.525 53.850 68.308 1.00 20.29 ? 368 PRO A CA 1 ATOM 2511 C C . PRO A 1 327 ? 0.238 54.333 66.905 1.00 19.05 ? 368 PRO A C 1 ATOM 2512 O O . PRO A 1 327 ? 0.356 53.536 65.982 1.00 19.82 ? 368 PRO A O 1 ATOM 2513 C CB . PRO A 1 327 ? -0.740 53.252 68.955 1.00 21.72 ? 368 PRO A CB 1 ATOM 2514 C CG . PRO A 1 327 ? -1.233 54.340 69.853 1.00 21.61 ? 368 PRO A CG 1 ATOM 2515 C CD . PRO A 1 327 ? -0.021 55.031 70.371 1.00 22.80 ? 368 PRO A CD 1 ATOM 2516 N N . ASP A 1 328 ? -0.076 55.623 66.755 1.00 18.51 ? 369 ASP A N 1 ATOM 2517 C CA . ASP A 1 328 ? -0.337 56.177 65.419 1.00 19.48 ? 369 ASP A CA 1 ATOM 2518 C C . ASP A 1 328 ? 0.921 56.773 64.789 1.00 19.09 ? 369 ASP A C 1 ATOM 2519 O O . ASP A 1 328 ? 0.822 57.619 63.886 1.00 17.37 ? 369 ASP A O 1 ATOM 2520 C CB . ASP A 1 328 ? -1.430 57.232 65.533 1.00 20.68 ? 369 ASP A CB 1 ATOM 2521 C CG . ASP A 1 328 ? -0.952 58.485 66.249 1.00 24.94 ? 369 ASP A CG 1 ATOM 2522 O OD1 . ASP A 1 328 ? 0.032 58.443 66.987 1.00 24.35 ? 369 ASP A OD1 1 ATOM 2523 O OD2 . ASP A 1 328 ? -1.565 59.577 66.081 1.00 25.45 ? 369 ASP A OD2 1 ATOM 2524 N N . ARG A 1 329 ? 2.093 56.268 65.181 1.00 18.22 ? 370 ARG A N 1 ATOM 2525 C CA . ARG A 1 329 ? 3.335 56.659 64.524 1.00 17.17 ? 370 ARG A CA 1 ATOM 2526 C C . ARG A 1 329 ? 4.004 55.375 64.136 1.00 17.84 ? 370 ARG A C 1 ATOM 2527 O O . ARG A 1 329 ? 4.172 54.503 64.988 1.00 17.36 ? 370 ARG A O 1 ATOM 2528 C CB . ARG A 1 329 ? 4.204 57.489 65.499 1.00 17.14 ? 370 ARG A CB 1 ATOM 2529 C CG . ARG A 1 329 ? 3.623 58.868 65.754 1.00 17.14 ? 370 ARG A CG 1 ATOM 2530 C CD . ARG A 1 329 ? 3.816 59.720 64.523 1.00 19.19 ? 370 ARG A CD 1 ATOM 2531 N NE . ARG A 1 329 ? 3.209 61.066 64.599 1.00 17.92 ? 370 ARG A NE 1 ATOM 2532 C CZ . ARG A 1 329 ? 1.959 61.397 64.189 1.00 17.25 ? 370 ARG A CZ 1 ATOM 2533 N NH1 . ARG A 1 329 ? 1.070 60.473 63.754 1.00 17.17 ? 370 ARG A NH1 1 ATOM 2534 N NH2 . ARG A 1 329 ? 1.593 62.698 64.143 1.00 18.36 ? 370 ARG A NH2 1 ATOM 2535 N N . TYR A 1 330 ? 4.401 55.251 62.862 1.00 15.10 ? 371 TYR A N 1 ATOM 2536 C CA . TYR A 1 330 ? 4.891 53.948 62.365 1.00 15.79 ? 371 TYR A CA 1 ATOM 2537 C C . TYR A 1 330 ? 6.336 53.997 61.960 1.00 16.67 ? 371 TYR A C 1 ATOM 2538 O O . TYR A 1 330 ? 6.740 54.845 61.150 1.00 17.76 ? 371 TYR A O 1 ATOM 2539 C CB . TYR A 1 330 ? 4.142 53.561 61.102 1.00 15.80 ? 371 TYR A CB 1 ATOM 2540 C CG . TYR A 1 330 ? 2.646 53.501 61.219 1.00 16.94 ? 371 TYR A CG 1 ATOM 2541 C CD1 . TYR A 1 330 ? 2.003 53.135 62.412 1.00 17.53 ? 371 TYR A CD1 1 ATOM 2542 C CD2 . TYR A 1 330 ? 1.857 53.764 60.119 1.00 16.16 ? 371 TYR A CD2 1 ATOM 2543 C CE1 . TYR A 1 330 ? 0.600 53.081 62.482 1.00 17.81 ? 371 TYR A CE1 1 ATOM 2544 C CE2 . TYR A 1 330 ? 0.471 53.710 60.182 1.00 15.21 ? 371 TYR A CE2 1 ATOM 2545 C CZ . TYR A 1 330 ? -0.161 53.348 61.373 1.00 18.29 ? 371 TYR A CZ 1 ATOM 2546 O OH . TYR A 1 330 ? -1.538 53.306 61.439 1.00 17.63 ? 371 TYR A OH 1 ATOM 2547 N N . VAL A 1 331 ? 7.109 53.052 62.489 1.00 14.93 ? 372 VAL A N 1 ATOM 2548 C CA . VAL A 1 331 ? 8.519 52.841 62.095 1.00 15.65 ? 372 VAL A CA 1 ATOM 2549 C C . VAL A 1 331 ? 8.475 51.501 61.365 1.00 16.11 ? 372 VAL A C 1 ATOM 2550 O O . VAL A 1 331 ? 8.012 50.521 61.928 1.00 17.50 ? 372 VAL A O 1 ATOM 2551 C CB . VAL A 1 331 ? 9.467 52.798 63.307 1.00 17.50 ? 372 VAL A CB 1 ATOM 2552 C CG1 . VAL A 1 331 ? 10.865 52.413 62.851 1.00 17.51 ? 372 VAL A CG1 1 ATOM 2553 C CG2 . VAL A 1 331 ? 9.504 54.201 63.913 1.00 16.80 ? 372 VAL A CG2 1 ATOM 2554 N N . ILE A 1 332 ? 8.938 51.459 60.112 1.00 14.74 ? 373 ILE A N 1 ATOM 2555 C CA . ILE A 1 332 ? 8.732 50.267 59.287 1.00 14.56 ? 373 ILE A CA 1 ATOM 2556 C C . ILE A 1 332 ? 10.065 49.623 58.946 1.00 15.23 ? 373 ILE A C 1 ATOM 2557 O O . ILE A 1 332 ? 10.980 50.283 58.492 1.00 15.61 ? 373 ILE A O 1 ATOM 2558 C CB . ILE A 1 332 ? 8.053 50.671 57.944 1.00 14.64 ? 373 ILE A CB 1 ATOM 2559 C CG1 . ILE A 1 332 ? 6.730 51.358 58.259 1.00 15.95 ? 373 ILE A CG1 1 ATOM 2560 C CG2 . ILE A 1 332 ? 7.774 49.404 57.092 1.00 16.98 ? 373 ILE A CG2 1 ATOM 2561 C CD1 . ILE A 1 332 ? 6.099 52.024 57.031 1.00 19.59 ? 373 ILE A CD1 1 ATOM 2562 N N . LEU A 1 333 ? 10.162 48.325 59.184 1.00 14.79 ? 374 LEU A N 1 ATOM 2563 C CA . LEU A 1 333 ? 11.337 47.546 58.758 1.00 14.83 ? 374 LEU A CA 1 ATOM 2564 C C . LEU A 1 333 ? 10.823 46.605 57.679 1.00 15.65 ? 374 LEU A C 1 ATOM 2565 O O . LEU A 1 333 ? 10.034 45.705 57.974 1.00 16.61 ? 374 LEU A O 1 ATOM 2566 C CB . LEU A 1 333 ? 11.911 46.728 59.926 1.00 16.19 ? 374 LEU A CB 1 ATOM 2567 C CG . LEU A 1 333 ? 13.076 45.809 59.529 1.00 15.83 ? 374 LEU A CG 1 ATOM 2568 C CD1 . LEU A 1 333 ? 14.311 46.599 59.064 1.00 18.40 ? 374 LEU A CD1 1 ATOM 2569 C CD2 . LEU A 1 333 ? 13.430 45.016 60.850 1.00 18.55 ? 374 LEU A CD2 1 ATOM 2570 N N . GLY A 1 334 ? 11.286 46.786 56.445 1.00 14.88 ? 375 GLY A N 1 ATOM 2571 C CA . GLY A 1 334 ? 10.717 46.004 55.330 1.00 14.61 ? 375 GLY A CA 1 ATOM 2572 C C . GLY A 1 334 ? 11.817 45.465 54.433 1.00 17.12 ? 375 GLY A C 1 ATOM 2573 O O . GLY A 1 334 ? 12.797 46.162 54.178 1.00 16.18 ? 375 GLY A O 1 ATOM 2574 N N . GLY A 1 335 ? 11.648 44.232 53.961 1.00 15.52 ? 376 GLY A N 1 ATOM 2575 C CA . GLY A 1 335 ? 12.562 43.742 52.900 1.00 16.15 ? 376 GLY A CA 1 ATOM 2576 C C . GLY A 1 335 ? 11.807 42.644 52.166 1.00 16.07 ? 376 GLY A C 1 ATOM 2577 O O . GLY A 1 335 ? 10.795 42.108 52.699 1.00 16.22 ? 376 GLY A O 1 ATOM 2578 N N . HIS A 1 336 ? 12.286 42.283 50.964 1.00 14.98 ? 377 HIS A N 1 ATOM 2579 C CA . HIS A 1 336 ? 11.510 41.307 50.203 1.00 14.51 ? 377 HIS A CA 1 ATOM 2580 C C . HIS A 1 336 ? 11.897 39.866 50.485 1.00 15.95 ? 377 HIS A C 1 ATOM 2581 O O . HIS A 1 336 ? 12.943 39.575 51.124 1.00 16.63 ? 377 HIS A O 1 ATOM 2582 C CB . HIS A 1 336 ? 11.551 41.634 48.706 1.00 14.44 ? 377 HIS A CB 1 ATOM 2583 C CG . HIS A 1 336 ? 12.848 41.312 48.033 1.00 14.47 ? 377 HIS A CG 1 ATOM 2584 N ND1 . HIS A 1 336 ? 12.964 40.206 47.211 1.00 14.03 ? 377 HIS A ND1 1 ATOM 2585 C CD2 . HIS A 1 336 ? 14.007 42.017 47.883 1.00 14.62 ? 377 HIS A CD2 1 ATOM 2586 C CE1 . HIS A 1 336 ? 14.167 40.213 46.636 1.00 13.66 ? 377 HIS A CE1 1 ATOM 2587 N NE2 . HIS A 1 336 ? 14.812 41.309 47.018 1.00 14.09 ? 377 HIS A NE2 1 ATOM 2588 N N . ARG A 1 337 ? 11.000 38.981 50.025 1.00 14.01 ? 378 ARG A N 1 ATOM 2589 C CA . ARG A 1 337 ? 11.083 37.539 50.279 1.00 15.55 ? 378 ARG A CA 1 ATOM 2590 C C . ARG A 1 337 ? 11.212 36.767 48.975 1.00 15.59 ? 378 ARG A C 1 ATOM 2591 O O . ARG A 1 337 ? 11.791 35.660 48.970 1.00 15.94 ? 378 ARG A O 1 ATOM 2592 C CB . ARG A 1 337 ? 9.759 37.140 50.931 1.00 17.01 ? 378 ARG A CB 1 ATOM 2593 C CG . ARG A 1 337 ? 9.693 35.616 51.288 1.00 17.66 ? 378 ARG A CG 1 ATOM 2594 C CD . ARG A 1 337 ? 8.259 35.332 51.823 1.00 18.36 ? 378 ARG A CD 1 ATOM 2595 N NE . ARG A 1 337 ? 7.271 35.386 50.737 1.00 19.30 ? 378 ARG A NE 1 ATOM 2596 C CZ . ARG A 1 337 ? 6.377 36.355 50.553 1.00 18.25 ? 378 ARG A CZ 1 ATOM 2597 N NH1 . ARG A 1 337 ? 6.267 37.393 51.399 1.00 17.02 ? 378 ARG A NH1 1 ATOM 2598 N NH2 . ARG A 1 337 ? 5.549 36.284 49.502 1.00 17.90 ? 378 ARG A NH2 1 ATOM 2599 N N . ASP A 1 338 ? 10.617 37.286 47.886 1.00 14.72 ? 379 ASP A N 1 ATOM 2600 C CA . ASP A 1 338 ? 10.710 36.595 46.575 1.00 15.13 ? 379 ASP A CA 1 ATOM 2601 C C . ASP A 1 338 ? 12.175 36.613 46.093 1.00 15.74 ? 379 ASP A C 1 ATOM 2602 O O . ASP A 1 338 ? 12.921 37.592 46.302 1.00 15.18 ? 379 ASP A O 1 ATOM 2603 C CB . ASP A 1 338 ? 9.867 37.260 45.514 1.00 15.20 ? 379 ASP A CB 1 ATOM 2604 C CG . ASP A 1 338 ? 10.305 38.674 45.208 1.00 15.50 ? 379 ASP A CG 1 ATOM 2605 O OD1 . ASP A 1 338 ? 10.328 39.530 46.138 1.00 14.66 ? 379 ASP A OD1 1 ATOM 2606 O OD2 . ASP A 1 338 ? 10.520 38.930 44.021 1.00 14.77 ? 379 ASP A OD2 1 ATOM 2607 N N . SER A 1 339 ? 12.584 35.547 45.389 1.00 16.42 ? 380 SER A N 1 ATOM 2608 C CA . SER A 1 339 ? 13.958 35.455 44.922 1.00 15.29 ? 380 SER A CA 1 ATOM 2609 C C . SER A 1 339 ? 13.930 35.026 43.442 1.00 16.82 ? 380 SER A C 1 ATOM 2610 O O . SER A 1 339 ? 12.889 34.514 42.976 1.00 16.85 ? 380 SER A O 1 ATOM 2611 C CB . SER A 1 339 ? 14.714 34.417 45.775 1.00 16.79 ? 380 SER A CB 1 ATOM 2612 O OG . SER A 1 339 ? 14.112 33.133 45.698 1.00 17.42 ? 380 SER A OG 1 ATOM 2613 N N . TRP A 1 340 ? 15.011 35.214 42.715 1.00 15.87 ? 381 TRP A N 1 ATOM 2614 C CA . TRP A 1 340 ? 15.039 34.671 41.333 1.00 14.16 ? 381 TRP A CA 1 ATOM 2615 C C . TRP A 1 340 ? 15.147 33.140 41.366 1.00 16.68 ? 381 TRP A C 1 ATOM 2616 O O . TRP A 1 340 ? 14.410 32.456 40.677 1.00 17.77 ? 381 TRP A O 1 ATOM 2617 C CB . TRP A 1 340 ? 16.200 35.305 40.496 1.00 16.05 ? 381 TRP A CB 1 ATOM 2618 C CG . TRP A 1 340 ? 15.739 36.645 39.976 1.00 15.41 ? 381 TRP A CG 1 ATOM 2619 C CD1 . TRP A 1 340 ? 16.257 37.931 40.260 1.00 16.60 ? 381 TRP A CD1 1 ATOM 2620 C CD2 . TRP A 1 340 ? 14.629 36.851 39.106 1.00 15.61 ? 381 TRP A CD2 1 ATOM 2621 N NE1 . TRP A 1 340 ? 15.490 38.898 39.602 1.00 15.81 ? 381 TRP A NE1 1 ATOM 2622 C CE2 . TRP A 1 340 ? 14.512 38.252 38.877 1.00 15.18 ? 381 TRP A CE2 1 ATOM 2623 C CE3 . TRP A 1 340 ? 13.717 35.977 38.463 1.00 16.21 ? 381 TRP A CE3 1 ATOM 2624 C CZ2 . TRP A 1 340 ? 13.486 38.787 38.104 1.00 16.71 ? 381 TRP A CZ2 1 ATOM 2625 C CZ3 . TRP A 1 340 ? 12.694 36.520 37.685 1.00 17.01 ? 381 TRP A CZ3 1 ATOM 2626 C CH2 . TRP A 1 340 ? 12.601 37.920 37.506 1.00 17.15 ? 381 TRP A CH2 1 ATOM 2627 N N . VAL A 1 341 ? 16.102 32.638 42.163 1.00 17.25 ? 382 VAL A N 1 ATOM 2628 C CA . VAL A 1 341 ? 16.232 31.175 42.398 1.00 17.27 ? 382 VAL A CA 1 ATOM 2629 C C . VAL A 1 341 ? 16.276 30.929 43.929 1.00 17.06 ? 382 VAL A C 1 ATOM 2630 O O . VAL A 1 341 ? 15.242 31.069 44.600 1.00 17.45 ? 382 VAL A O 1 ATOM 2631 C CB . VAL A 1 341 ? 17.400 30.501 41.580 1.00 17.16 ? 382 VAL A CB 1 ATOM 2632 C CG1 . VAL A 1 341 ? 17.154 28.957 41.578 1.00 18.31 ? 382 VAL A CG1 1 ATOM 2633 C CG2 . VAL A 1 341 ? 17.383 30.940 40.106 1.00 19.27 ? 382 VAL A CG2 1 ATOM 2634 N N . PHE A 1 342 ? 17.442 30.553 44.470 1.00 16.31 ? 383 PHE A N 1 ATOM 2635 C CA . PHE A 1 342 ? 17.502 30.207 45.905 1.00 16.35 ? 383 PHE A CA 1 ATOM 2636 C C . PHE A 1 342 ? 17.642 31.431 46.792 1.00 17.02 ? 383 PHE A C 1 ATOM 2637 O O . PHE A 1 342 ? 17.292 31.347 47.964 1.00 18.28 ? 383 PHE A O 1 ATOM 2638 C CB . PHE A 1 342 ? 18.662 29.238 46.183 1.00 17.21 ? 383 PHE A CB 1 ATOM 2639 C CG . PHE A 1 342 ? 18.520 27.948 45.384 1.00 19.69 ? 383 PHE A CG 1 ATOM 2640 C CD1 . PHE A 1 342 ? 17.498 27.046 45.710 1.00 21.29 ? 383 PHE A CD1 1 ATOM 2641 C CD2 . PHE A 1 342 ? 19.301 27.735 44.256 1.00 21.00 ? 383 PHE A CD2 1 ATOM 2642 C CE1 . PHE A 1 342 ? 17.337 25.856 44.933 1.00 21.95 ? 383 PHE A CE1 1 ATOM 2643 C CE2 . PHE A 1 342 ? 19.138 26.551 43.487 1.00 20.80 ? 383 PHE A CE2 1 ATOM 2644 C CZ . PHE A 1 342 ? 18.130 25.655 43.844 1.00 20.34 ? 383 PHE A CZ 1 ATOM 2645 N N . GLY A 1 343 ? 18.094 32.565 46.229 1.00 17.19 ? 384 GLY A N 1 ATOM 2646 C CA . GLY A 1 343 ? 18.182 33.836 47.033 1.00 16.66 ? 384 GLY A CA 1 ATOM 2647 C C . GLY A 1 343 ? 19.118 33.761 48.235 1.00 18.38 ? 384 GLY A C 1 ATOM 2648 O O . GLY A 1 343 ? 18.857 34.399 49.269 1.00 17.55 ? 384 GLY A O 1 ATOM 2649 N N . GLY A 1 344 ? 20.195 32.986 48.099 1.00 18.26 ? 385 GLY A N 1 ATOM 2650 C CA . GLY A 1 344 ? 21.191 32.846 49.162 1.00 18.18 ? 385 GLY A CA 1 ATOM 2651 C C . GLY A 1 344 ? 21.622 34.178 49.706 1.00 17.86 ? 385 GLY A C 1 ATOM 2652 O O . GLY A 1 344 ? 21.745 34.322 50.904 1.00 18.41 ? 385 GLY A O 1 ATOM 2653 N N . ILE A 1 345 ? 21.901 35.145 48.820 1.00 17.24 ? 386 ILE A N 1 ATOM 2654 C CA . ILE A 1 345 ? 22.232 36.498 49.313 1.00 16.10 ? 386 ILE A CA 1 ATOM 2655 C C . ILE A 1 345 ? 20.953 37.344 49.145 1.00 16.63 ? 386 ILE A C 1 ATOM 2656 O O . ILE A 1 345 ? 20.450 37.920 50.144 1.00 16.99 ? 386 ILE A O 1 ATOM 2657 C CB . ILE A 1 345 ? 23.436 37.131 48.585 1.00 17.19 ? 386 ILE A CB 1 ATOM 2658 C CG1 . ILE A 1 345 ? 24.716 36.427 49.089 1.00 18.71 ? 386 ILE A CG1 1 ATOM 2659 C CG2 . ILE A 1 345 ? 23.557 38.656 48.911 1.00 17.50 ? 386 ILE A CG2 1 ATOM 2660 C CD1 . ILE A 1 345 ? 26.000 36.895 48.354 1.00 18.84 ? 386 ILE A CD1 1 ATOM 2661 N N . ASP A 1 346 ? 20.458 37.411 47.915 1.00 16.45 ? 387 ASP A N 1 ATOM 2662 C CA . ASP A 1 346 ? 19.359 38.339 47.572 1.00 15.66 ? 387 ASP A CA 1 ATOM 2663 C C . ASP A 1 346 ? 18.037 37.549 47.414 1.00 16.31 ? 387 ASP A C 1 ATOM 2664 O O . ASP A 1 346 ? 17.888 36.856 46.407 1.00 16.73 ? 387 ASP A O 1 ATOM 2665 C CB . ASP A 1 346 ? 19.784 38.976 46.247 1.00 15.54 ? 387 ASP A CB 1 ATOM 2666 C CG . ASP A 1 346 ? 18.777 39.973 45.721 1.00 18.04 ? 387 ASP A CG 1 ATOM 2667 O OD1 . ASP A 1 346 ? 17.787 40.157 46.446 1.00 15.26 ? 387 ASP A OD1 1 ATOM 2668 O OD2 . ASP A 1 346 ? 18.983 40.474 44.574 1.00 19.41 ? 387 ASP A OD2 1 ATOM 2669 N N . PRO A 1 347 ? 17.090 37.641 48.376 1.00 15.10 ? 388 PRO A N 1 ATOM 2670 C CA . PRO A 1 347 ? 17.076 38.541 49.562 1.00 14.98 ? 388 PRO A CA 1 ATOM 2671 C C . PRO A 1 347 ? 17.266 37.819 50.862 1.00 15.54 ? 388 PRO A C 1 ATOM 2672 O O . PRO A 1 347 ? 17.165 38.458 51.921 1.00 15.40 ? 388 PRO A O 1 ATOM 2673 C CB . PRO A 1 347 ? 15.613 39.058 49.574 1.00 14.87 ? 388 PRO A CB 1 ATOM 2674 C CG . PRO A 1 347 ? 14.813 37.817 49.155 1.00 16.98 ? 388 PRO A CG 1 ATOM 2675 C CD . PRO A 1 347 ? 15.720 37.087 48.145 1.00 15.47 ? 388 PRO A CD 1 ATOM 2676 N N . GLN A 1 348 ? 17.505 36.501 50.834 1.00 15.65 ? 389 GLN A N 1 ATOM 2677 C CA . GLN A 1 348 ? 17.293 35.796 52.106 1.00 17.36 ? 389 GLN A CA 1 ATOM 2678 C C . GLN A 1 348 ? 18.319 36.125 53.215 1.00 16.31 ? 389 GLN A C 1 ATOM 2679 O O . GLN A 1 348 ? 18.011 35.986 54.398 1.00 16.98 ? 389 GLN A O 1 ATOM 2680 C CB . GLN A 1 348 ? 17.192 34.267 51.917 1.00 17.39 ? 389 GLN A CB 1 ATOM 2681 C CG . GLN A 1 348 ? 16.157 33.824 50.887 1.00 18.57 ? 389 GLN A CG 1 ATOM 2682 C CD . GLN A 1 348 ? 14.714 34.343 51.143 1.00 19.13 ? 389 GLN A CD 1 ATOM 2683 O OE1 . GLN A 1 348 ? 14.376 34.922 52.205 1.00 17.29 ? 389 GLN A OE1 1 ATOM 2684 N NE2 . GLN A 1 348 ? 13.857 34.117 50.155 1.00 18.53 ? 389 GLN A NE2 1 ATOM 2685 N N . SER A 1 349 ? 19.487 36.626 52.838 1.00 17.21 ? 390 SER A N 1 ATOM 2686 C CA . SER A 1 349 ? 20.420 37.084 53.858 1.00 18.79 ? 390 SER A CA 1 ATOM 2687 C C . SER A 1 349 ? 19.848 38.284 54.574 1.00 17.88 ? 390 SER A C 1 ATOM 2688 O O . SER A 1 349 ? 20.175 38.494 55.747 1.00 19.30 ? 390 SER A O 1 ATOM 2689 C CB . SER A 1 349 ? 21.808 37.439 53.266 1.00 19.61 ? 390 SER A CB 1 ATOM 2690 O OG . SER A 1 349 ? 21.741 38.585 52.395 1.00 18.33 ? 390 SER A OG 1 ATOM 2691 N N . GLY A 1 350 ? 19.016 39.076 53.887 1.00 16.82 ? 391 GLY A N 1 ATOM 2692 C CA . GLY A 1 350 ? 18.272 40.149 54.568 1.00 16.07 ? 391 GLY A CA 1 ATOM 2693 C C . GLY A 1 350 ? 17.047 39.644 55.299 1.00 15.80 ? 391 GLY A C 1 ATOM 2694 O O . GLY A 1 350 ? 16.825 40.043 56.462 1.00 16.84 ? 391 GLY A O 1 ATOM 2695 N N . ALA A 1 351 ? 16.253 38.763 54.672 1.00 15.78 ? 392 ALA A N 1 ATOM 2696 C CA . ALA A 1 351 ? 15.015 38.238 55.318 1.00 17.66 ? 392 ALA A CA 1 ATOM 2697 C C . ALA A 1 351 ? 15.338 37.491 56.614 1.00 17.75 ? 392 ALA A C 1 ATOM 2698 O O . ALA A 1 351 ? 14.563 37.564 57.558 1.00 18.14 ? 392 ALA A O 1 ATOM 2699 C CB . ALA A 1 351 ? 14.188 37.378 54.385 1.00 17.81 ? 392 ALA A CB 1 ATOM 2700 N N . ALA A 1 352 ? 16.480 36.776 56.661 1.00 17.89 ? 393 ALA A N 1 ATOM 2701 C CA . ALA A 1 352 ? 16.868 36.052 57.897 1.00 18.71 ? 393 ALA A CA 1 ATOM 2702 C C . ALA A 1 352 ? 17.194 37.012 59.013 1.00 18.91 ? 393 ALA A C 1 ATOM 2703 O O . ALA A 1 352 ? 16.915 36.752 60.185 1.00 19.63 ? 393 ALA A O 1 ATOM 2704 C CB . ALA A 1 352 ? 18.082 35.188 57.601 1.00 18.84 ? 393 ALA A CB 1 ATOM 2705 N N . VAL A 1 353 ? 17.774 38.148 58.642 1.00 18.94 ? 394 VAL A N 1 ATOM 2706 C CA . VAL A 1 353 ? 18.101 39.208 59.613 1.00 18.96 ? 394 VAL A CA 1 ATOM 2707 C C . VAL A 1 353 ? 16.781 39.820 60.133 1.00 19.07 ? 394 VAL A C 1 ATOM 2708 O O . VAL A 1 353 ? 16.643 40.030 61.365 1.00 18.44 ? 394 VAL A O 1 ATOM 2709 C CB . VAL A 1 353 ? 19.035 40.247 58.942 1.00 18.54 ? 394 VAL A CB 1 ATOM 2710 C CG1 . VAL A 1 353 ? 18.941 41.646 59.611 1.00 18.26 ? 394 VAL A CG1 1 ATOM 2711 C CG2 . VAL A 1 353 ? 20.503 39.713 58.998 1.00 17.41 ? 394 VAL A CG2 1 ATOM 2712 N N . VAL A 1 354 ? 15.827 40.102 59.237 1.00 18.42 ? 395 VAL A N 1 ATOM 2713 C CA . VAL A 1 354 ? 14.536 40.661 59.691 1.00 18.46 ? 395 VAL A CA 1 ATOM 2714 C C . VAL A 1 354 ? 13.883 39.660 60.638 1.00 18.50 ? 395 VAL A C 1 ATOM 2715 O O . VAL A 1 354 ? 13.388 40.052 61.667 1.00 19.25 ? 395 VAL A O 1 ATOM 2716 C CB . VAL A 1 354 ? 13.561 40.915 58.537 1.00 19.04 ? 395 VAL A CB 1 ATOM 2717 C CG1 . VAL A 1 354 ? 12.171 41.354 59.078 1.00 18.05 ? 395 VAL A CG1 1 ATOM 2718 C CG2 . VAL A 1 354 ? 14.165 42.010 57.596 1.00 20.70 ? 395 VAL A CG2 1 ATOM 2719 N N . HIS A 1 355 ? 13.937 38.369 60.294 1.00 18.65 ? 396 HIS A N 1 ATOM 2720 C CA . HIS A 1 355 ? 13.280 37.318 61.095 1.00 18.55 ? 396 HIS A CA 1 ATOM 2721 C C . HIS A 1 355 ? 13.842 37.327 62.515 1.00 20.44 ? 396 HIS A C 1 ATOM 2722 O O . HIS A 1 355 ? 13.086 37.317 63.508 1.00 21.05 ? 396 HIS A O 1 ATOM 2723 C CB . HIS A 1 355 ? 13.507 35.950 60.402 1.00 20.15 ? 396 HIS A CB 1 ATOM 2724 C CG . HIS A 1 355 ? 12.357 34.998 60.504 1.00 20.05 ? 396 HIS A CG 1 ATOM 2725 N ND1 . HIS A 1 355 ? 11.055 35.353 60.214 1.00 21.94 ? 396 HIS A ND1 1 ATOM 2726 C CD2 . HIS A 1 355 ? 12.326 33.675 60.821 1.00 23.17 ? 396 HIS A CD2 1 ATOM 2727 C CE1 . HIS A 1 355 ? 10.271 34.300 60.364 1.00 22.99 ? 396 HIS A CE1 1 ATOM 2728 N NE2 . HIS A 1 355 ? 11.021 33.264 60.702 1.00 22.76 ? 396 HIS A NE2 1 ATOM 2729 N N . GLU A 1 356 ? 15.160 37.422 62.617 1.00 19.97 ? 397 GLU A N 1 ATOM 2730 C CA . GLU A 1 356 ? 15.798 37.434 63.954 1.00 20.49 ? 397 GLU A CA 1 ATOM 2731 C C . GLU A 1 356 ? 15.491 38.721 64.705 1.00 20.83 ? 397 GLU A C 1 ATOM 2732 O O . GLU A 1 356 ? 15.348 38.731 65.937 1.00 21.83 ? 397 GLU A O 1 ATOM 2733 C CB . GLU A 1 356 ? 17.305 37.194 63.789 1.00 21.96 ? 397 GLU A CB 1 ATOM 2734 C CG . GLU A 1 356 ? 18.106 37.213 65.114 1.00 22.03 ? 397 GLU A CG 1 ATOM 2735 C CD . GLU A 1 356 ? 17.721 36.105 66.083 1.00 25.67 ? 397 GLU A CD 1 ATOM 2736 O OE1 . GLU A 1 356 ? 16.752 35.350 65.825 1.00 23.32 ? 397 GLU A OE1 1 ATOM 2737 O OE2 . GLU A 1 356 ? 18.421 35.996 67.129 1.00 25.89 ? 397 GLU A OE2 1 ATOM 2738 N N . ILE A 1 357 ? 15.370 39.838 63.976 1.00 19.18 ? 398 ILE A N 1 ATOM 2739 C CA . ILE A 1 357 ? 14.950 41.094 64.613 1.00 19.57 ? 398 ILE A CA 1 ATOM 2740 C C . ILE A 1 357 ? 13.539 41.036 65.193 1.00 19.69 ? 398 ILE A C 1 ATOM 2741 O O . ILE A 1 357 ? 13.291 41.453 66.356 1.00 22.32 ? 398 ILE A O 1 ATOM 2742 C CB . ILE A 1 357 ? 15.097 42.266 63.600 1.00 17.85 ? 398 ILE A CB 1 ATOM 2743 C CG1 . ILE A 1 357 ? 16.591 42.604 63.426 1.00 17.06 ? 398 ILE A CG1 1 ATOM 2744 C CG2 . ILE A 1 357 ? 14.378 43.531 64.108 1.00 19.05 ? 398 ILE A CG2 1 ATOM 2745 C CD1 . ILE A 1 357 ? 16.908 43.394 62.068 1.00 18.21 ? 398 ILE A CD1 1 ATOM 2746 N N . VAL A 1 358 ? 12.621 40.475 64.417 1.00 19.87 ? 399 VAL A N 1 ATOM 2747 C CA . VAL A 1 358 ? 11.254 40.254 64.904 1.00 20.34 ? 399 VAL A CA 1 ATOM 2748 C C . VAL A 1 358 ? 11.313 39.376 66.146 1.00 20.91 ? 399 VAL A C 1 ATOM 2749 O O . VAL A 1 358 ? 10.650 39.700 67.148 1.00 21.49 ? 399 VAL A O 1 ATOM 2750 C CB . VAL A 1 358 ? 10.334 39.593 63.868 1.00 19.64 ? 399 VAL A CB 1 ATOM 2751 C CG1 . VAL A 1 358 ? 8.947 39.347 64.461 1.00 20.72 ? 399 VAL A CG1 1 ATOM 2752 C CG2 . VAL A 1 358 ? 10.221 40.526 62.564 1.00 20.06 ? 399 VAL A CG2 1 ATOM 2753 N N . ARG A 1 359 ? 12.083 38.292 66.078 1.00 21.22 ? 400 ARG A N 1 ATOM 2754 C CA . ARG A 1 359 ? 12.188 37.371 67.219 1.00 22.52 ? 400 ARG A CA 1 ATOM 2755 C C . ARG A 1 359 ? 12.673 38.109 68.457 1.00 23.23 ? 400 ARG A C 1 ATOM 2756 O O . ARG A 1 359 ? 12.102 37.916 69.557 1.00 24.51 ? 400 ARG A O 1 ATOM 2757 C CB . ARG A 1 359 ? 13.073 36.166 66.917 1.00 22.56 ? 400 ARG A CB 1 ATOM 2758 C CG . ARG A 1 359 ? 12.912 35.020 67.989 1.00 22.50 ? 400 ARG A CG 1 ATOM 2759 C CD . ARG A 1 359 ? 14.109 33.990 67.849 1.00 24.34 ? 400 ARG A CD 1 ATOM 2760 N NE . ARG A 1 359 ? 15.396 34.649 68.129 1.00 25.23 ? 400 ARG A NE 1 ATOM 2761 C CZ . ARG A 1 359 ? 15.815 35.000 69.354 1.00 26.59 ? 400 ARG A CZ 1 ATOM 2762 N NH1 . ARG A 1 359 ? 16.977 35.617 69.512 1.00 26.09 ? 400 ARG A NH1 1 ATOM 2763 N NH2 . ARG A 1 359 ? 15.084 34.715 70.428 1.00 27.99 ? 400 ARG A NH2 1 ATOM 2764 N N . SER A 1 360 ? 13.714 38.946 68.313 1.00 23.41 ? 401 SER A N 1 ATOM 2765 C CA A SER A 1 360 ? 14.252 39.678 69.472 0.50 23.71 ? 401 SER A CA 1 ATOM 2766 C CA B SER A 1 360 ? 14.246 39.662 69.454 0.50 25.03 ? 401 SER A CA 1 ATOM 2767 C C . SER A 1 360 ? 13.250 40.684 70.002 1.00 24.89 ? 401 SER A C 1 ATOM 2768 O O . SER A 1 360 ? 13.013 40.758 71.224 1.00 25.20 ? 401 SER A O 1 ATOM 2769 C CB A SER A 1 360 ? 15.592 40.378 69.196 0.50 23.67 ? 401 SER A CB 1 ATOM 2770 C CB B SER A 1 360 ? 15.573 40.295 69.080 0.50 25.09 ? 401 SER A CB 1 ATOM 2771 O OG A SER A 1 360 ? 16.024 41.134 70.341 0.50 19.26 ? 401 SER A OG 1 ATOM 2772 O OG B SER A 1 360 ? 16.399 39.295 68.515 0.50 28.97 ? 401 SER A OG 1 ATOM 2773 N N . PHE A 1 361 ? 12.632 41.488 69.109 1.00 23.35 ? 402 PHE A N 1 ATOM 2774 C CA . PHE A 1 361 ? 11.592 42.406 69.617 1.00 24.45 ? 402 PHE A CA 1 ATOM 2775 C C . PHE A 1 361 ? 10.473 41.654 70.323 1.00 26.32 ? 402 PHE A C 1 ATOM 2776 O O . PHE A 1 361 ? 10.003 42.116 71.359 1.00 26.62 ? 402 PHE A O 1 ATOM 2777 C CB . PHE A 1 361 ? 10.987 43.264 68.485 1.00 24.05 ? 402 PHE A CB 1 ATOM 2778 C CG . PHE A 1 361 ? 11.779 44.490 68.144 1.00 21.88 ? 402 PHE A CG 1 ATOM 2779 C CD1 . PHE A 1 361 ? 11.946 45.524 69.052 1.00 19.91 ? 402 PHE A CD1 1 ATOM 2780 C CD2 . PHE A 1 361 ? 12.306 44.635 66.843 1.00 22.53 ? 402 PHE A CD2 1 ATOM 2781 C CE1 . PHE A 1 361 ? 12.659 46.682 68.711 1.00 21.32 ? 402 PHE A CE1 1 ATOM 2782 C CE2 . PHE A 1 361 ? 13.016 45.805 66.481 1.00 22.86 ? 402 PHE A CE2 1 ATOM 2783 C CZ . PHE A 1 361 ? 13.207 46.813 67.416 1.00 21.76 ? 402 PHE A CZ 1 ATOM 2784 N N . GLY A 1 362 ? 10.087 40.476 69.810 1.00 26.15 ? 403 GLY A N 1 ATOM 2785 C CA . GLY A 1 362 ? 8.992 39.705 70.383 1.00 26.61 ? 403 GLY A CA 1 ATOM 2786 C C . GLY A 1 362 ? 9.390 39.121 71.742 1.00 26.95 ? 403 GLY A C 1 ATOM 2787 O O . GLY A 1 362 ? 8.558 39.017 72.653 1.00 28.53 ? 403 GLY A O 1 ATOM 2788 N N . THR A 1 363 ? 10.663 38.828 71.924 1.00 27.99 ? 404 THR A N 1 ATOM 2789 C CA . THR A 1 363 ? 11.129 38.381 73.250 1.00 28.83 ? 404 THR A CA 1 ATOM 2790 C C . THR A 1 363 ? 10.892 39.472 74.301 1.00 30.23 ? 404 THR A C 1 ATOM 2791 O O . THR A 1 363 ? 10.415 39.182 75.419 1.00 32.03 ? 404 THR A O 1 ATOM 2792 C CB . THR A 1 363 ? 12.614 37.924 73.272 1.00 29.08 ? 404 THR A CB 1 ATOM 2793 O OG1 A THR A 1 363 ? 12.791 36.829 72.361 0.50 28.83 ? 404 THR A OG1 1 ATOM 2794 O OG1 B THR A 1 363 ? 13.497 39.056 73.271 0.50 29.72 ? 404 THR A OG1 1 ATOM 2795 C CG2 A THR A 1 363 ? 13.058 37.527 74.675 0.50 28.43 ? 404 THR A CG2 1 ATOM 2796 C CG2 B THR A 1 363 ? 12.935 36.972 72.115 0.50 28.53 ? 404 THR A CG2 1 ATOM 2797 N N . LEU A 1 364 ? 11.228 40.717 73.974 1.00 29.01 ? 405 LEU A N 1 ATOM 2798 C CA . LEU A 1 364 ? 11.020 41.823 74.908 1.00 29.25 ? 405 LEU A CA 1 ATOM 2799 C C . LEU A 1 364 ? 9.534 42.000 75.161 1.00 29.82 ? 405 LEU A C 1 ATOM 2800 O O . LEU A 1 364 ? 9.097 42.215 76.286 1.00 28.62 ? 405 LEU A O 1 ATOM 2801 C CB . LEU A 1 364 ? 11.608 43.141 74.348 1.00 30.12 ? 405 LEU A CB 1 ATOM 2802 C CG A LEU A 1 364 ? 13.101 43.407 74.629 0.50 29.53 ? 405 LEU A CG 1 ATOM 2803 C CG B LEU A 1 364 ? 13.122 43.217 74.166 0.50 29.63 ? 405 LEU A CG 1 ATOM 2804 C CD1 A LEU A 1 364 ? 14.059 42.427 73.917 0.50 29.51 ? 405 LEU A CD1 1 ATOM 2805 C CD1 B LEU A 1 364 ? 13.504 44.517 73.482 0.50 30.02 ? 405 LEU A CD1 1 ATOM 2806 C CD2 A LEU A 1 364 ? 13.477 44.849 74.289 0.50 29.72 ? 405 LEU A CD2 1 ATOM 2807 C CD2 B LEU A 1 364 ? 13.826 43.085 75.502 0.50 32.08 ? 405 LEU A CD2 1 ATOM 2808 N N . LYS A 1 365 ? 8.745 41.955 74.095 1.00 27.86 ? 406 LYS A N 1 ATOM 2809 C CA . LYS A 1 365 ? 7.304 42.099 74.205 1.00 29.80 ? 406 LYS A CA 1 ATOM 2810 C C . LYS A 1 365 ? 6.701 41.043 75.159 1.00 30.95 ? 406 LYS A C 1 ATOM 2811 O O . LYS A 1 365 ? 5.822 41.379 75.961 1.00 30.04 ? 406 LYS A O 1 ATOM 2812 C CB . LYS A 1 365 ? 6.689 41.993 72.805 1.00 29.95 ? 406 LYS A CB 1 ATOM 2813 C CG . LYS A 1 365 ? 5.235 42.428 72.737 1.00 34.50 ? 406 LYS A CG 1 ATOM 2814 C CD . LYS A 1 365 ? 4.314 41.246 72.631 1.00 39.96 ? 406 LYS A CD 1 ATOM 2815 C CE . LYS A 1 365 ? 2.907 41.696 72.261 1.00 42.17 ? 406 LYS A CE 1 ATOM 2816 N NZ . LYS A 1 365 ? 2.132 40.519 71.804 1.00 46.80 ? 406 LYS A NZ 1 ATOM 2817 N N . LYS A 1 366 ? 7.173 39.794 75.061 1.00 30.58 ? 407 LYS A N 1 ATOM 2818 C CA . LYS A 1 366 ? 6.643 38.735 75.934 1.00 32.35 ? 407 LYS A CA 1 ATOM 2819 C C . LYS A 1 366 ? 6.952 38.997 77.398 1.00 34.35 ? 407 LYS A C 1 ATOM 2820 O O . LYS A 1 366 ? 6.213 38.516 78.275 1.00 35.36 ? 407 LYS A O 1 ATOM 2821 C CB . LYS A 1 366 ? 7.119 37.358 75.499 1.00 31.77 ? 407 LYS A CB 1 ATOM 2822 C CG . LYS A 1 366 ? 6.430 36.907 74.222 1.00 33.97 ? 407 LYS A CG 1 ATOM 2823 C CD . LYS A 1 366 ? 6.954 35.574 73.732 1.00 35.75 ? 407 LYS A CD 1 ATOM 2824 C CE . LYS A 1 366 ? 6.181 35.155 72.500 1.00 38.07 ? 407 LYS A CE 1 ATOM 2825 N NZ . LYS A 1 366 ? 6.762 33.892 71.995 1.00 41.89 ? 407 LYS A NZ 1 ATOM 2826 N N . GLU A 1 367 ? 8.015 39.762 77.661 1.00 34.11 ? 408 GLU A N 1 ATOM 2827 C CA . GLU A 1 367 ? 8.368 40.181 79.027 1.00 36.42 ? 408 GLU A CA 1 ATOM 2828 C C . GLU A 1 367 ? 7.654 41.447 79.473 1.00 36.02 ? 408 GLU A C 1 ATOM 2829 O O . GLU A 1 367 ? 7.882 41.936 80.586 1.00 37.73 ? 408 GLU A O 1 ATOM 2830 C CB . GLU A 1 367 ? 9.887 40.334 79.148 1.00 36.87 ? 408 GLU A CB 1 ATOM 2831 C CG . GLU A 1 367 ? 10.605 39.022 78.836 1.00 43.12 ? 408 GLU A CG 1 ATOM 2832 C CD . GLU A 1 367 ? 12.121 39.147 78.757 1.00 50.84 ? 408 GLU A CD 1 ATOM 2833 O OE1 . GLU A 1 367 ? 12.789 38.092 78.578 1.00 56.40 ? 408 GLU A OE1 1 ATOM 2834 O OE2 . GLU A 1 367 ? 12.657 40.279 78.870 1.00 54.04 ? 408 GLU A OE2 1 ATOM 2835 N N . GLY A 1 368 ? 6.785 41.983 78.620 1.00 33.84 ? 409 GLY A N 1 ATOM 2836 C CA . GLY A 1 368 ? 5.926 43.100 79.001 1.00 33.34 ? 409 GLY A CA 1 ATOM 2837 C C . GLY A 1 368 ? 6.314 44.442 78.431 1.00 32.23 ? 409 GLY A C 1 ATOM 2838 O O . GLY A 1 368 ? 5.720 45.461 78.776 1.00 32.80 ? 409 GLY A O 1 ATOM 2839 N N . TRP A 1 369 ? 7.322 44.448 77.556 1.00 31.48 ? 410 TRP A N 1 ATOM 2840 C CA . TRP A 1 369 ? 7.789 45.692 76.969 1.00 29.85 ? 410 TRP A CA 1 ATOM 2841 C C . TRP A 1 369 ? 6.975 45.993 75.700 1.00 28.14 ? 410 TRP A C 1 ATOM 2842 O O . TRP A 1 369 ? 6.466 45.073 75.022 1.00 28.14 ? 410 TRP A O 1 ATOM 2843 C CB . TRP A 1 369 ? 9.268 45.544 76.615 1.00 29.98 ? 410 TRP A CB 1 ATOM 2844 C CG . TRP A 1 369 ? 9.903 46.689 75.850 1.00 30.84 ? 410 TRP A CG 1 ATOM 2845 C CD1 . TRP A 1 369 ? 10.432 47.845 76.371 1.00 30.95 ? 410 TRP A CD1 1 ATOM 2846 C CD2 . TRP A 1 369 ? 10.072 46.768 74.431 1.00 29.71 ? 410 TRP A CD2 1 ATOM 2847 N NE1 . TRP A 1 369 ? 10.923 48.639 75.346 1.00 30.61 ? 410 TRP A NE1 1 ATOM 2848 C CE2 . TRP A 1 369 ? 10.730 47.990 74.150 1.00 29.18 ? 410 TRP A CE2 1 ATOM 2849 C CE3 . TRP A 1 369 ? 9.712 45.927 73.359 1.00 29.33 ? 410 TRP A CE3 1 ATOM 2850 C CZ2 . TRP A 1 369 ? 11.035 48.397 72.825 1.00 26.54 ? 410 TRP A CZ2 1 ATOM 2851 C CZ3 . TRP A 1 369 ? 10.035 46.321 72.042 1.00 26.71 ? 410 TRP A CZ3 1 ATOM 2852 C CH2 . TRP A 1 369 ? 10.687 47.558 71.808 1.00 27.92 ? 410 TRP A CH2 1 ATOM 2853 N N . ARG A 1 370 ? 6.830 47.278 75.412 1.00 26.90 ? 411 ARG A N 1 ATOM 2854 C CA . ARG A 1 370 ? 6.363 47.689 74.076 1.00 25.44 ? 411 ARG A CA 1 ATOM 2855 C C . ARG A 1 370 ? 7.171 48.890 73.688 1.00 23.38 ? 411 ARG A C 1 ATOM 2856 O O . ARG A 1 370 ? 7.553 49.684 74.518 1.00 23.83 ? 411 ARG A O 1 ATOM 2857 C CB . ARG A 1 370 ? 4.899 48.141 74.103 1.00 26.88 ? 411 ARG A CB 1 ATOM 2858 C CG . ARG A 1 370 ? 3.857 47.045 74.135 1.00 27.57 ? 411 ARG A CG 1 ATOM 2859 C CD . ARG A 1 370 ? 2.397 47.586 73.961 1.00 27.00 ? 411 ARG A CD 1 ATOM 2860 N NE . ARG A 1 370 ? 1.579 46.394 73.896 1.00 27.06 ? 411 ARG A NE 1 ATOM 2861 C CZ . ARG A 1 370 ? 1.470 45.623 72.808 1.00 29.65 ? 411 ARG A CZ 1 ATOM 2862 N NH1 . ARG A 1 370 ? 2.007 45.998 71.624 1.00 26.05 ? 411 ARG A NH1 1 ATOM 2863 N NH2 . ARG A 1 370 ? 0.756 44.517 72.878 1.00 29.84 ? 411 ARG A NH2 1 ATOM 2864 N N . PRO A 1 371 ? 7.417 49.051 72.376 1.00 21.48 ? 412 PRO A N 1 ATOM 2865 C CA . PRO A 1 371 ? 8.097 50.259 71.952 1.00 21.24 ? 412 PRO A CA 1 ATOM 2866 C C . PRO A 1 371 ? 7.202 51.476 72.096 1.00 20.53 ? 412 PRO A C 1 ATOM 2867 O O . PRO A 1 371 ? 6.000 51.351 72.182 1.00 21.96 ? 412 PRO A O 1 ATOM 2868 C CB . PRO A 1 371 ? 8.340 50.011 70.444 1.00 20.80 ? 412 PRO A CB 1 ATOM 2869 C CG . PRO A 1 371 ? 7.127 49.130 70.050 1.00 20.27 ? 412 PRO A CG 1 ATOM 2870 C CD . PRO A 1 371 ? 6.937 48.207 71.267 1.00 20.98 ? 412 PRO A CD 1 ATOM 2871 N N . ARG A 1 372 ? 7.784 52.663 72.093 1.00 20.20 ? 413 ARG A N 1 ATOM 2872 C CA . ARG A 1 372 ? 7.004 53.883 72.245 1.00 20.22 ? 413 ARG A CA 1 ATOM 2873 C C . ARG A 1 372 ? 6.030 54.026 71.066 1.00 20.79 ? 413 ARG A C 1 ATOM 2874 O O . ARG A 1 372 ? 4.814 54.263 71.238 1.00 21.40 ? 413 ARG A O 1 ATOM 2875 C CB . ARG A 1 372 ? 7.938 55.076 72.267 1.00 19.77 ? 413 ARG A CB 1 ATOM 2876 C CG . ARG A 1 372 ? 7.177 56.396 72.388 1.00 22.23 ? 413 ARG A CG 1 ATOM 2877 C CD . ARG A 1 372 ? 8.081 57.594 72.302 1.00 23.83 ? 413 ARG A CD 1 ATOM 2878 N NE . ARG A 1 372 ? 7.312 58.839 72.254 1.00 24.34 ? 413 ARG A NE 1 ATOM 2879 C CZ . ARG A 1 372 ? 6.880 59.503 73.338 1.00 27.81 ? 413 ARG A CZ 1 ATOM 2880 N NH1 . ARG A 1 372 ? 7.118 59.036 74.576 1.00 28.00 ? 413 ARG A NH1 1 ATOM 2881 N NH2 . ARG A 1 372 ? 6.198 60.627 73.171 1.00 27.96 ? 413 ARG A NH2 1 ATOM 2882 N N . ARG A 1 373 ? 6.607 53.881 69.874 1.00 19.69 ? 414 ARG A N 1 ATOM 2883 C CA . ARG A 1 373 ? 5.829 53.959 68.608 1.00 19.37 ? 414 ARG A CA 1 ATOM 2884 C C . ARG A 1 373 ? 5.571 52.580 68.035 1.00 19.89 ? 414 ARG A C 1 ATOM 2885 O O . ARG A 1 373 ? 6.238 51.594 68.381 1.00 20.37 ? 414 ARG A O 1 ATOM 2886 C CB . ARG A 1 373 ? 6.621 54.792 67.580 1.00 19.73 ? 414 ARG A CB 1 ATOM 2887 C CG . ARG A 1 373 ? 7.044 56.192 68.082 1.00 19.64 ? 414 ARG A CG 1 ATOM 2888 C CD . ARG A 1 373 ? 7.807 57.078 67.042 1.00 18.85 ? 414 ARG A CD 1 ATOM 2889 N NE . ARG A 1 373 ? 8.025 58.344 67.737 1.00 19.70 ? 414 ARG A NE 1 ATOM 2890 C CZ . ARG A 1 373 ? 9.025 58.582 68.610 1.00 22.15 ? 414 ARG A CZ 1 ATOM 2891 N NH1 . ARG A 1 373 ? 9.998 57.725 68.782 1.00 20.39 ? 414 ARG A NH1 1 ATOM 2892 N NH2 . ARG A 1 373 ? 9.054 59.737 69.275 1.00 21.69 ? 414 ARG A NH2 1 ATOM 2893 N N . THR A 1 374 ? 4.623 52.496 67.115 1.00 18.44 ? 415 THR A N 1 ATOM 2894 C CA . THR A 1 374 ? 4.314 51.235 66.472 1.00 18.21 ? 415 THR A CA 1 ATOM 2895 C C . THR A 1 374 ? 5.447 50.869 65.510 1.00 18.89 ? 415 THR A C 1 ATOM 2896 O O . THR A 1 374 ? 5.937 51.723 64.767 1.00 18.50 ? 415 THR A O 1 ATOM 2897 C CB . THR A 1 374 ? 2.977 51.362 65.707 1.00 18.25 ? 415 THR A CB 1 ATOM 2898 O OG1 . THR A 1 374 ? 1.878 51.389 66.644 1.00 18.43 ? 415 THR A OG1 1 ATOM 2899 C CG2 . THR A 1 374 ? 2.741 50.208 64.737 1.00 18.57 ? 415 THR A CG2 1 ATOM 2900 N N . ILE A 1 375 ? 5.811 49.591 65.515 1.00 17.16 ? 416 ILE A N 1 ATOM 2901 C CA . ILE A 1 375 ? 6.706 49.064 64.490 1.00 16.88 ? 416 ILE A CA 1 ATOM 2902 C C . ILE A 1 375 ? 5.963 48.143 63.568 1.00 17.22 ? 416 ILE A C 1 ATOM 2903 O O . ILE A 1 375 ? 5.209 47.269 64.029 1.00 18.11 ? 416 ILE A O 1 ATOM 2904 C CB . ILE A 1 375 ? 7.936 48.285 65.119 1.00 16.62 ? 416 ILE A CB 1 ATOM 2905 C CG1 . ILE A 1 375 ? 8.665 49.160 66.156 1.00 19.00 ? 416 ILE A CG1 1 ATOM 2906 C CG2 . ILE A 1 375 ? 8.851 47.797 64.012 1.00 18.55 ? 416 ILE A CG2 1 ATOM 2907 C CD1 . ILE A 1 375 ? 9.697 48.403 67.020 1.00 19.77 ? 416 ILE A CD1 1 ATOM 2908 N N . LEU A 1 376 ? 6.122 48.373 62.248 1.00 15.80 ? 417 LEU A N 1 ATOM 2909 C CA . LEU A 1 376 ? 5.535 47.486 61.235 1.00 16.68 ? 417 LEU A CA 1 ATOM 2910 C C . LEU A 1 376 ? 6.719 46.738 60.610 1.00 17.10 ? 417 LEU A C 1 ATOM 2911 O O . LEU A 1 376 ? 7.787 47.335 60.325 1.00 17.14 ? 417 LEU A O 1 ATOM 2912 C CB . LEU A 1 376 ? 4.815 48.275 60.126 1.00 15.92 ? 417 LEU A CB 1 ATOM 2913 C CG . LEU A 1 376 ? 3.691 49.193 60.695 1.00 19.13 ? 417 LEU A CG 1 ATOM 2914 C CD1 . LEU A 1 376 ? 3.022 49.952 59.528 1.00 16.54 ? 417 LEU A CD1 1 ATOM 2915 C CD2 . LEU A 1 376 ? 2.644 48.395 61.440 1.00 20.93 ? 417 LEU A CD2 1 ATOM 2916 N N . PHE A 1 377 ? 6.534 45.429 60.434 1.00 16.57 ? 418 PHE A N 1 ATOM 2917 C CA . PHE A 1 377 ? 7.540 44.563 59.785 1.00 15.95 ? 418 PHE A CA 1 ATOM 2918 C C . PHE A 1 377 ? 6.925 44.035 58.510 1.00 16.73 ? 418 PHE A C 1 ATOM 2919 O O . PHE A 1 377 ? 5.752 43.640 58.504 1.00 15.87 ? 418 PHE A O 1 ATOM 2920 C CB . PHE A 1 377 ? 7.828 43.371 60.728 1.00 16.82 ? 418 PHE A CB 1 ATOM 2921 C CG . PHE A 1 377 ? 8.420 43.790 62.054 1.00 17.80 ? 418 PHE A CG 1 ATOM 2922 C CD1 . PHE A 1 377 ? 9.804 44.019 62.152 1.00 17.59 ? 418 PHE A CD1 1 ATOM 2923 C CD2 . PHE A 1 377 ? 7.613 43.950 63.206 1.00 20.18 ? 418 PHE A CD2 1 ATOM 2924 C CE1 . PHE A 1 377 ? 10.394 44.411 63.417 1.00 19.86 ? 418 PHE A CE1 1 ATOM 2925 C CE2 . PHE A 1 377 ? 8.202 44.343 64.454 1.00 19.35 ? 418 PHE A CE2 1 ATOM 2926 C CZ . PHE A 1 377 ? 9.604 44.546 64.532 1.00 20.14 ? 418 PHE A CZ 1 ATOM 2927 N N . ALA A 1 378 ? 7.672 44.085 57.415 1.00 15.87 ? 419 ALA A N 1 ATOM 2928 C CA . ALA A 1 378 ? 7.122 43.627 56.133 1.00 15.44 ? 419 ALA A CA 1 ATOM 2929 C C . ALA A 1 378 ? 8.063 42.660 55.435 1.00 15.51 ? 419 ALA A C 1 ATOM 2930 O O . ALA A 1 378 ? 9.275 42.873 55.384 1.00 15.30 ? 419 ALA A O 1 ATOM 2931 C CB . ALA A 1 378 ? 6.876 44.846 55.215 1.00 14.26 ? 419 ALA A CB 1 ATOM 2932 N N . SER A 1 379 ? 7.458 41.600 54.906 1.00 15.33 ? 420 SER A N 1 ATOM 2933 C CA . SER A 1 379 ? 8.079 40.639 53.994 1.00 14.45 ? 420 SER A CA 1 ATOM 2934 C C . SER A 1 379 ? 7.434 40.871 52.621 1.00 15.06 ? 420 SER A C 1 ATOM 2935 O O . SER A 1 379 ? 6.299 40.419 52.382 1.00 16.05 ? 420 SER A O 1 ATOM 2936 C CB . SER A 1 379 ? 7.733 39.207 54.498 1.00 15.75 ? 420 SER A CB 1 ATOM 2937 O OG . SER A 1 379 ? 8.241 38.225 53.539 1.00 14.62 ? 420 SER A OG 1 ATOM 2938 N N . TRP A 1 380 ? 8.090 41.665 51.785 1.00 14.39 ? 421 TRP A N 1 ATOM 2939 C CA . TRP A 1 380 ? 7.429 42.078 50.528 1.00 13.10 ? 421 TRP A CA 1 ATOM 2940 C C . TRP A 1 380 ? 7.577 40.979 49.492 1.00 15.10 ? 421 TRP A C 1 ATOM 2941 O O . TRP A 1 380 ? 8.584 40.213 49.461 1.00 15.59 ? 421 TRP A O 1 ATOM 2942 C CB . TRP A 1 380 ? 8.138 43.309 49.946 1.00 14.22 ? 421 TRP A CB 1 ATOM 2943 C CG . TRP A 1 380 ? 8.246 44.500 50.820 1.00 13.25 ? 421 TRP A CG 1 ATOM 2944 C CD1 . TRP A 1 380 ? 9.395 45.173 51.142 1.00 14.11 ? 421 TRP A CD1 1 ATOM 2945 C CD2 . TRP A 1 380 ? 7.161 45.227 51.424 1.00 12.63 ? 421 TRP A CD2 1 ATOM 2946 N NE1 . TRP A 1 380 ? 9.081 46.287 51.914 1.00 14.42 ? 421 TRP A NE1 1 ATOM 2947 C CE2 . TRP A 1 380 ? 7.712 46.331 52.092 1.00 13.61 ? 421 TRP A CE2 1 ATOM 2948 C CE3 . TRP A 1 380 ? 5.752 45.079 51.403 1.00 14.23 ? 421 TRP A CE3 1 ATOM 2949 C CZ2 . TRP A 1 380 ? 6.902 47.273 52.809 1.00 13.89 ? 421 TRP A CZ2 1 ATOM 2950 C CZ3 . TRP A 1 380 ? 4.944 45.992 52.131 1.00 15.29 ? 421 TRP A CZ3 1 ATOM 2951 C CH2 . TRP A 1 380 ? 5.541 47.090 52.841 1.00 14.68 ? 421 TRP A CH2 1 ATOM 2952 N N . ASP A 1 381 ? 6.606 40.978 48.571 1.00 14.25 ? 422 ASP A N 1 ATOM 2953 C CA . ASP A 1 381 ? 6.676 40.040 47.430 1.00 13.04 ? 422 ASP A CA 1 ATOM 2954 C C . ASP A 1 381 ? 6.968 40.807 46.166 1.00 13.63 ? 422 ASP A C 1 ATOM 2955 O O . ASP A 1 381 ? 6.804 42.058 46.083 1.00 15.01 ? 422 ASP A O 1 ATOM 2956 C CB . ASP A 1 381 ? 5.328 39.318 47.295 1.00 13.86 ? 422 ASP A CB 1 ATOM 2957 C CG . ASP A 1 381 ? 5.408 37.954 46.581 1.00 14.85 ? 422 ASP A CG 1 ATOM 2958 O OD1 . ASP A 1 381 ? 6.453 37.594 45.968 1.00 15.74 ? 422 ASP A OD1 1 ATOM 2959 O OD2 . ASP A 1 381 ? 4.352 37.240 46.649 1.00 15.60 ? 422 ASP A OD2 1 ATOM 2960 N N . ALA A 1 382 ? 7.391 40.048 45.160 1.00 13.39 ? 423 ALA A N 1 ATOM 2961 C CA . ALA A 1 382 ? 7.572 40.573 43.799 1.00 13.43 ? 423 ALA A CA 1 ATOM 2962 C C . ALA A 1 382 ? 8.506 41.775 43.722 1.00 13.29 ? 423 ALA A C 1 ATOM 2963 O O . ALA A 1 382 ? 8.362 42.631 42.830 1.00 13.53 ? 423 ALA A O 1 ATOM 2964 C CB . ALA A 1 382 ? 6.221 40.870 43.133 1.00 14.61 ? 423 ALA A CB 1 ATOM 2965 N N . GLU A 1 383 ? 9.471 41.866 44.640 1.00 13.76 ? 424 GLU A N 1 ATOM 2966 C CA . GLU A 1 383 ? 10.465 42.966 44.495 1.00 13.79 ? 424 GLU A CA 1 ATOM 2967 C C . GLU A 1 383 ? 11.201 42.784 43.186 1.00 13.67 ? 424 GLU A C 1 ATOM 2968 O O . GLU A 1 383 ? 11.525 43.785 42.486 1.00 13.91 ? 424 GLU A O 1 ATOM 2969 C CB . GLU A 1 383 ? 11.402 42.998 45.705 1.00 13.99 ? 424 GLU A CB 1 ATOM 2970 C CG . GLU A 1 383 ? 12.369 44.186 45.689 1.00 13.82 ? 424 GLU A CG 1 ATOM 2971 C CD . GLU A 1 383 ? 13.612 43.993 44.849 1.00 15.01 ? 424 GLU A CD 1 ATOM 2972 O OE1 . GLU A 1 383 ? 13.898 42.854 44.358 1.00 15.49 ? 424 GLU A OE1 1 ATOM 2973 O OE2 . GLU A 1 383 ? 14.426 44.965 44.771 1.00 14.82 ? 424 GLU A OE2 1 ATOM 2974 N N . GLU A 1 384 ? 11.500 41.531 42.842 1.00 12.85 ? 425 GLU A N 1 ATOM 2975 C CA . GLU A 1 384 ? 12.352 41.283 41.672 1.00 14.35 ? 425 GLU A CA 1 ATOM 2976 C C . GLU A 1 384 ? 11.726 41.699 40.358 1.00 13.17 ? 425 GLU A C 1 ATOM 2977 O O . GLU A 1 384 ? 12.404 41.856 39.325 1.00 15.59 ? 425 GLU A O 1 ATOM 2978 C CB . GLU A 1 384 ? 12.798 39.809 41.659 1.00 14.77 ? 425 GLU A CB 1 ATOM 2979 C CG . GLU A 1 384 ? 13.680 39.391 42.858 1.00 14.85 ? 425 GLU A CG 1 ATOM 2980 C CD . GLU A 1 384 ? 15.135 40.015 42.826 1.00 15.98 ? 425 GLU A CD 1 ATOM 2981 O OE1 . GLU A 1 384 ? 15.397 40.981 42.050 1.00 14.37 ? 425 GLU A OE1 1 ATOM 2982 O OE2 . GLU A 1 384 ? 15.972 39.635 43.661 1.00 17.55 ? 425 GLU A OE2 1 ATOM 2983 N N . PHE A 1 385 ? 10.383 41.826 40.411 1.00 13.70 ? 426 PHE A N 1 ATOM 2984 C CA . PHE A 1 385 ? 9.622 42.162 39.218 1.00 13.40 ? 426 PHE A CA 1 ATOM 2985 C C . PHE A 1 385 ? 9.273 43.650 39.115 1.00 14.90 ? 426 PHE A C 1 ATOM 2986 O O . PHE A 1 385 ? 8.413 44.034 38.297 1.00 15.48 ? 426 PHE A O 1 ATOM 2987 C CB . PHE A 1 385 ? 8.367 41.304 39.147 1.00 15.66 ? 426 PHE A CB 1 ATOM 2988 C CG . PHE A 1 385 ? 8.658 39.860 38.822 1.00 14.22 ? 426 PHE A CG 1 ATOM 2989 C CD1 . PHE A 1 385 ? 8.571 39.441 37.505 1.00 15.05 ? 426 PHE A CD1 1 ATOM 2990 C CD2 . PHE A 1 385 ? 9.000 38.950 39.820 1.00 16.11 ? 426 PHE A CD2 1 ATOM 2991 C CE1 . PHE A 1 385 ? 8.804 38.052 37.140 1.00 15.84 ? 426 PHE A CE1 1 ATOM 2992 C CE2 . PHE A 1 385 ? 9.288 37.575 39.499 1.00 16.48 ? 426 PHE A CE2 1 ATOM 2993 C CZ . PHE A 1 385 ? 9.141 37.135 38.150 1.00 16.49 ? 426 PHE A CZ 1 ATOM 2994 N N . GLY A 1 386 ? 9.923 44.469 39.977 1.00 14.44 ? 427 GLY A N 1 ATOM 2995 C CA . GLY A 1 386 ? 9.739 45.929 39.900 1.00 13.11 ? 427 GLY A CA 1 ATOM 2996 C C . GLY A 1 386 ? 9.250 46.568 41.178 1.00 13.60 ? 427 GLY A C 1 ATOM 2997 O O . GLY A 1 386 ? 8.514 47.573 41.106 1.00 13.29 ? 427 GLY A O 1 ATOM 2998 N N A LEU A 1 387 ? 9.628 46.044 42.335 0.50 11.83 ? 428 LEU A N 1 ATOM 2999 N N B LEU A 1 387 ? 9.649 46.007 42.313 0.50 11.93 ? 428 LEU A N 1 ATOM 3000 C CA A LEU A 1 387 ? 9.200 46.685 43.583 0.50 12.58 ? 428 LEU A CA 1 ATOM 3001 C CA B LEU A 1 387 ? 9.265 46.572 43.597 0.50 12.83 ? 428 LEU A CA 1 ATOM 3002 C C A LEU A 1 387 ? 7.677 46.565 43.779 0.50 11.99 ? 428 LEU A C 1 ATOM 3003 C C B LEU A 1 387 ? 7.713 46.601 43.676 0.50 12.26 ? 428 LEU A C 1 ATOM 3004 O O A LEU A 1 387 ? 7.054 47.386 44.485 0.50 11.15 ? 428 LEU A O 1 ATOM 3005 O O B LEU A 1 387 ? 7.097 47.560 44.178 0.50 12.74 ? 428 LEU A O 1 ATOM 3006 C CB A LEU A 1 387 ? 9.609 48.172 43.603 0.50 12.58 ? 428 LEU A CB 1 ATOM 3007 C CB B LEU A 1 387 ? 9.894 47.973 43.777 0.50 12.76 ? 428 LEU A CB 1 ATOM 3008 C CG A LEU A 1 387 ? 11.070 48.479 43.237 0.50 12.08 ? 428 LEU A CG 1 ATOM 3009 C CG B LEU A 1 387 ? 11.231 48.232 43.043 0.50 11.60 ? 428 LEU A CG 1 ATOM 3010 C CD1 A LEU A 1 387 ? 11.395 49.919 43.617 0.50 10.57 ? 428 LEU A CD1 1 ATOM 3011 C CD1 B LEU A 1 387 ? 11.674 49.708 43.108 0.50 12.29 ? 428 LEU A CD1 1 ATOM 3012 C CD2 A LEU A 1 387 ? 12.013 47.546 43.965 0.50 12.92 ? 428 LEU A CD2 1 ATOM 3013 C CD2 B LEU A 1 387 ? 12.328 47.328 43.636 0.50 12.45 ? 428 LEU A CD2 1 ATOM 3014 N N . LEU A 1 388 ? 7.091 45.509 43.217 1.00 11.74 ? 429 LEU A N 1 ATOM 3015 C CA . LEU A 1 388 ? 5.607 45.512 43.089 1.00 12.57 ? 429 LEU A CA 1 ATOM 3016 C C . LEU A 1 388 ? 4.891 45.385 44.431 1.00 12.62 ? 429 LEU A C 1 ATOM 3017 O O . LEU A 1 388 ? 3.893 46.108 44.613 1.00 13.51 ? 429 LEU A O 1 ATOM 3018 C CB . LEU A 1 388 ? 5.174 44.448 42.053 1.00 12.00 ? 429 LEU A CB 1 ATOM 3019 C CG . LEU A 1 388 ? 5.869 44.479 40.690 1.00 14.72 ? 429 LEU A CG 1 ATOM 3020 C CD1 . LEU A 1 388 ? 5.237 43.404 39.823 1.00 16.93 ? 429 LEU A CD1 1 ATOM 3021 C CD2 . LEU A 1 388 ? 5.745 45.855 39.986 1.00 15.01 ? 429 LEU A CD2 1 ATOM 3022 N N . GLY A 1 389 ? 5.323 44.502 45.316 1.00 14.33 ? 430 GLY A N 1 ATOM 3023 C CA . GLY A 1 389 ? 4.588 44.247 46.554 1.00 14.62 ? 430 GLY A CA 1 ATOM 3024 C C . GLY A 1 389 ? 4.639 45.468 47.476 1.00 14.26 ? 430 GLY A C 1 ATOM 3025 O O . GLY A 1 389 ? 3.624 45.888 48.058 1.00 14.83 ? 430 GLY A O 1 ATOM 3026 N N . SER A 1 390 ? 5.839 46.037 47.635 1.00 13.69 ? 431 SER A N 1 ATOM 3027 C CA . SER A 1 390 ? 5.957 47.224 48.518 1.00 13.56 ? 431 SER A CA 1 ATOM 3028 C C . SER A 1 390 ? 5.158 48.361 47.905 1.00 12.67 ? 431 SER A C 1 ATOM 3029 O O . SER A 1 390 ? 4.444 49.083 48.620 1.00 13.42 ? 431 SER A O 1 ATOM 3030 C CB . SER A 1 390 ? 7.424 47.663 48.648 1.00 14.10 ? 431 SER A CB 1 ATOM 3031 O OG . SER A 1 390 ? 8.017 47.952 47.392 1.00 15.03 ? 431 SER A OG 1 ATOM 3032 N N . THR A 1 391 ? 5.270 48.559 46.589 1.00 12.17 ? 432 THR A N 1 ATOM 3033 C CA . THR A 1 391 ? 4.579 49.715 45.968 1.00 12.19 ? 432 THR A CA 1 ATOM 3034 C C . THR A 1 391 ? 3.060 49.582 46.041 1.00 10.71 ? 432 THR A C 1 ATOM 3035 O O . THR A 1 391 ? 2.392 50.583 46.343 1.00 12.38 ? 432 THR A O 1 ATOM 3036 C CB . THR A 1 391 ? 5.104 49.947 44.514 1.00 11.47 ? 432 THR A CB 1 ATOM 3037 O OG1 . THR A 1 391 ? 6.544 50.083 44.610 1.00 13.81 ? 432 THR A OG1 1 ATOM 3038 C CG2 . THR A 1 391 ? 4.526 51.265 43.977 1.00 13.33 ? 432 THR A CG2 1 ATOM 3039 N N . GLU A 1 392 ? 2.538 48.388 45.771 1.00 11.24 ? 433 GLU A N 1 ATOM 3040 C CA . GLU A 1 392 ? 1.048 48.244 45.783 1.00 12.92 ? 433 GLU A CA 1 ATOM 3041 C C . GLU A 1 392 ? 0.555 48.452 47.219 1.00 12.25 ? 433 GLU A C 1 ATOM 3042 O O . GLU A 1 392 ? -0.489 49.099 47.399 1.00 13.78 ? 433 GLU A O 1 ATOM 3043 C CB . GLU A 1 392 ? 0.590 46.894 45.264 1.00 12.99 ? 433 GLU A CB 1 ATOM 3044 C CG . GLU A 1 392 ? 0.916 46.688 43.773 1.00 13.55 ? 433 GLU A CG 1 ATOM 3045 C CD . GLU A 1 392 ? 0.310 47.785 42.928 1.00 13.82 ? 433 GLU A CD 1 ATOM 3046 O OE1 . GLU A 1 392 ? -0.955 47.975 43.036 1.00 15.32 ? 433 GLU A OE1 1 ATOM 3047 O OE2 . GLU A 1 392 ? 1.089 48.438 42.171 1.00 16.31 ? 433 GLU A OE2 1 ATOM 3048 N N . TRP A 1 393 ? 1.261 47.928 48.235 1.00 12.94 ? 434 TRP A N 1 ATOM 3049 C CA . TRP A 1 393 ? 0.839 48.125 49.634 1.00 14.08 ? 434 TRP A CA 1 ATOM 3050 C C . TRP A 1 393 ? 0.897 49.588 50.006 1.00 14.30 ? 434 TRP A C 1 ATOM 3051 O O . TRP A 1 393 ? -0.038 50.085 50.632 1.00 13.88 ? 434 TRP A O 1 ATOM 3052 C CB . TRP A 1 393 ? 1.689 47.257 50.530 1.00 14.36 ? 434 TRP A CB 1 ATOM 3053 C CG . TRP A 1 393 ? 1.277 47.305 51.969 1.00 12.92 ? 434 TRP A CG 1 ATOM 3054 C CD1 . TRP A 1 393 ? 0.293 46.541 52.589 1.00 13.70 ? 434 TRP A CD1 1 ATOM 3055 C CD2 . TRP A 1 393 ? 1.805 48.180 52.952 1.00 15.56 ? 434 TRP A CD2 1 ATOM 3056 N NE1 . TRP A 1 393 ? 0.248 46.873 53.934 1.00 15.73 ? 434 TRP A NE1 1 ATOM 3057 C CE2 . TRP A 1 393 ? 1.184 47.841 54.185 1.00 15.80 ? 434 TRP A CE2 1 ATOM 3058 C CE3 . TRP A 1 393 ? 2.834 49.142 52.945 1.00 14.65 ? 434 TRP A CE3 1 ATOM 3059 C CZ2 . TRP A 1 393 ? 1.470 48.516 55.396 1.00 15.97 ? 434 TRP A CZ2 1 ATOM 3060 C CZ3 . TRP A 1 393 ? 3.155 49.819 54.193 1.00 15.52 ? 434 TRP A CZ3 1 ATOM 3061 C CH2 . TRP A 1 393 ? 2.459 49.487 55.389 1.00 16.68 ? 434 TRP A CH2 1 ATOM 3062 N N . ALA A 1 394 ? 1.955 50.290 49.586 1.00 12.94 ? 435 ALA A N 1 ATOM 3063 C CA . ALA A 1 394 ? 2.050 51.696 49.897 1.00 13.75 ? 435 ALA A CA 1 ATOM 3064 C C . ALA A 1 394 ? 0.969 52.470 49.166 1.00 13.67 ? 435 ALA A C 1 ATOM 3065 O O . ALA A 1 394 ? 0.438 53.466 49.693 1.00 14.27 ? 435 ALA A O 1 ATOM 3066 C CB . ALA A 1 394 ? 3.459 52.233 49.547 1.00 14.46 ? 435 ALA A CB 1 ATOM 3067 N N . GLU A 1 395 ? 0.644 52.069 47.916 1.00 12.76 ? 436 GLU A N 1 ATOM 3068 C CA . GLU A 1 395 ? -0.476 52.750 47.249 1.00 14.19 ? 436 GLU A CA 1 ATOM 3069 C C . GLU A 1 395 ? -1.780 52.559 48.010 1.00 14.13 ? 436 GLU A C 1 ATOM 3070 O O . GLU A 1 395 ? -2.600 53.486 48.108 1.00 15.38 ? 436 GLU A O 1 ATOM 3071 C CB . GLU A 1 395 ? -0.625 52.244 45.803 1.00 13.26 ? 436 GLU A CB 1 ATOM 3072 C CG . GLU A 1 395 ? 0.543 52.778 44.913 1.00 13.75 ? 436 GLU A CG 1 ATOM 3073 C CD . GLU A 1 395 ? 0.363 52.460 43.426 1.00 16.70 ? 436 GLU A CD 1 ATOM 3074 O OE1 . GLU A 1 395 ? 0.739 53.336 42.587 1.00 14.48 ? 436 GLU A OE1 1 ATOM 3075 O OE2 . GLU A 1 395 ? -0.164 51.343 43.163 1.00 15.88 ? 436 GLU A OE2 1 ATOM 3076 N N . GLU A 1 396 ? -1.985 51.361 48.521 1.00 14.13 ? 437 GLU A N 1 ATOM 3077 C CA . GLU A 1 396 ? -3.217 51.076 49.222 1.00 13.68 ? 437 GLU A CA 1 ATOM 3078 C C . GLU A 1 396 ? -3.273 51.937 50.516 1.00 13.91 ? 437 GLU A C 1 ATOM 3079 O O . GLU A 1 396 ? -4.335 52.473 50.886 1.00 15.60 ? 437 GLU A O 1 ATOM 3080 C CB . GLU A 1 396 ? -3.259 49.573 49.544 1.00 15.63 ? 437 GLU A CB 1 ATOM 3081 C CG . GLU A 1 396 ? -4.592 49.237 50.326 1.00 18.11 ? 437 GLU A CG 1 ATOM 3082 C CD . GLU A 1 396 ? -4.878 47.768 50.536 1.00 30.70 ? 437 GLU A CD 1 ATOM 3083 O OE1 . GLU A 1 396 ? -5.968 47.438 51.094 1.00 38.82 ? 437 GLU A OE1 1 ATOM 3084 O OE2 . GLU A 1 396 ? -4.030 46.938 50.286 1.00 24.80 ? 437 GLU A OE2 1 ATOM 3085 N N . ASN A 1 397 ? -2.133 52.054 51.197 1.00 13.14 ? 438 ASN A N 1 ATOM 3086 C CA . ASN A 1 397 ? -2.075 52.652 52.536 1.00 13.45 ? 438 ASN A CA 1 ATOM 3087 C C . ASN A 1 397 ? -1.441 54.040 52.542 1.00 12.99 ? 438 ASN A C 1 ATOM 3088 O O . ASN A 1 397 ? -1.074 54.539 53.621 1.00 14.57 ? 438 ASN A O 1 ATOM 3089 C CB . ASN A 1 397 ? -1.305 51.689 53.462 1.00 14.14 ? 438 ASN A CB 1 ATOM 3090 C CG . ASN A 1 397 ? -2.082 50.422 53.671 1.00 16.39 ? 438 ASN A CG 1 ATOM 3091 O OD1 . ASN A 1 397 ? -3.167 50.452 54.307 1.00 18.33 ? 438 ASN A OD1 1 ATOM 3092 N ND2 . ASN A 1 397 ? -1.618 49.313 53.084 1.00 16.11 ? 438 ASN A ND2 1 ATOM 3093 N N . SER A 1 398 ? -1.442 54.702 51.370 1.00 12.78 ? 439 SER A N 1 ATOM 3094 C CA . SER A 1 398 ? -0.689 55.969 51.289 1.00 13.10 ? 439 SER A CA 1 ATOM 3095 C C . SER A 1 398 ? -1.136 57.018 52.291 1.00 12.59 ? 439 SER A C 1 ATOM 3096 O O . SER A 1 398 ? -0.313 57.793 52.772 1.00 15.51 ? 439 SER A O 1 ATOM 3097 C CB . SER A 1 398 ? -0.821 56.588 49.860 1.00 12.89 ? 439 SER A CB 1 ATOM 3098 O OG . SER A 1 398 ? -2.211 56.805 49.545 1.00 15.92 ? 439 SER A OG 1 ATOM 3099 N N . ARG A 1 399 ? -2.437 57.122 52.595 1.00 12.23 ? 440 ARG A N 1 ATOM 3100 C CA . ARG A 1 399 ? -2.916 58.180 53.512 1.00 12.35 ? 440 ARG A CA 1 ATOM 3101 C C . ARG A 1 399 ? -2.405 57.900 54.930 1.00 13.81 ? 440 ARG A C 1 ATOM 3102 O O . ARG A 1 399 ? -2.064 58.836 55.683 1.00 15.19 ? 440 ARG A O 1 ATOM 3103 C CB . ARG A 1 399 ? -4.427 58.227 53.503 1.00 13.45 ? 440 ARG A CB 1 ATOM 3104 C CG . ARG A 1 399 ? -4.935 58.712 52.121 1.00 15.62 ? 440 ARG A CG 1 ATOM 3105 C CD . ARG A 1 399 ? -6.318 58.173 51.706 1.00 18.65 ? 440 ARG A CD 1 ATOM 3106 N NE . ARG A 1 399 ? -6.608 58.686 50.353 1.00 17.00 ? 440 ARG A NE 1 ATOM 3107 C CZ . ARG A 1 399 ? -6.212 58.197 49.194 1.00 18.92 ? 440 ARG A CZ 1 ATOM 3108 N NH1 . ARG A 1 399 ? -5.400 57.084 49.113 1.00 20.69 ? 440 ARG A NH1 1 ATOM 3109 N NH2 . ARG A 1 399 ? -6.602 58.866 48.105 1.00 18.14 ? 440 ARG A NH2 1 ATOM 3110 N N . LEU A 1 400 ? -2.389 56.622 55.319 1.00 12.90 ? 441 LEU A N 1 ATOM 3111 C CA . LEU A 1 400 ? -1.909 56.281 56.642 1.00 14.84 ? 441 LEU A CA 1 ATOM 3112 C C . LEU A 1 400 ? -0.397 56.590 56.697 1.00 15.53 ? 441 LEU A C 1 ATOM 3113 O O . LEU A 1 400 ? 0.128 57.119 57.685 1.00 15.82 ? 441 LEU A O 1 ATOM 3114 C CB . LEU A 1 400 ? -2.102 54.788 56.929 1.00 15.39 ? 441 LEU A CB 1 ATOM 3115 C CG . LEU A 1 400 ? -3.553 54.326 56.771 1.00 16.06 ? 441 LEU A CG 1 ATOM 3116 C CD1 . LEU A 1 400 ? -3.673 52.862 57.233 1.00 16.21 ? 441 LEU A CD1 1 ATOM 3117 C CD2 . LEU A 1 400 ? -4.528 55.201 57.568 1.00 18.97 ? 441 LEU A CD2 1 ATOM 3118 N N . LEU A 1 401 ? 0.313 56.236 55.623 1.00 14.27 ? 442 LEU A N 1 ATOM 3119 C CA . LEU A 1 401 ? 1.782 56.368 55.637 1.00 15.56 ? 442 LEU A CA 1 ATOM 3120 C C . LEU A 1 401 ? 2.159 57.829 55.593 1.00 16.51 ? 442 LEU A C 1 ATOM 3121 O O . LEU A 1 401 ? 3.095 58.229 56.274 1.00 18.80 ? 442 LEU A O 1 ATOM 3122 C CB . LEU A 1 401 ? 2.394 55.592 54.453 1.00 14.98 ? 442 LEU A CB 1 ATOM 3123 C CG . LEU A 1 401 ? 2.192 54.111 54.534 1.00 14.55 ? 442 LEU A CG 1 ATOM 3124 C CD1 . LEU A 1 401 ? 2.541 53.486 53.133 1.00 15.05 ? 442 LEU A CD1 1 ATOM 3125 C CD2 . LEU A 1 401 ? 3.195 53.517 55.569 1.00 17.16 ? 442 LEU A CD2 1 ATOM 3126 N N A GLN A 1 402 ? 1.501 58.659 54.807 0.50 15.00 ? 443 GLN A N 1 ATOM 3127 N N B GLN A 1 402 ? 1.441 58.605 54.762 0.50 15.58 ? 443 GLN A N 1 ATOM 3128 C CA A GLN A 1 402 ? 2.011 60.018 54.770 0.50 15.42 ? 443 GLN A CA 1 ATOM 3129 C CA B GLN A 1 402 ? 1.622 60.060 54.611 0.50 16.30 ? 443 GLN A CA 1 ATOM 3130 C C A GLN A 1 402 ? 1.624 60.868 56.000 0.50 15.38 ? 443 GLN A C 1 ATOM 3131 C C B GLN A 1 402 ? 1.634 60.750 55.975 0.50 16.16 ? 443 GLN A C 1 ATOM 3132 O O A GLN A 1 402 ? 2.256 61.905 56.263 0.50 14.53 ? 443 GLN A O 1 ATOM 3133 O O B GLN A 1 402 ? 2.555 61.500 56.317 0.50 15.37 ? 443 GLN A O 1 ATOM 3134 C CB A GLN A 1 402 ? 1.620 60.685 53.479 0.50 14.18 ? 443 GLN A CB 1 ATOM 3135 C CB B GLN A 1 402 ? 0.506 60.656 53.735 0.50 16.41 ? 443 GLN A CB 1 ATOM 3136 C CG A GLN A 1 402 ? 0.163 60.905 53.362 0.50 12.75 ? 443 GLN A CG 1 ATOM 3137 C CG B GLN A 1 402 ? 0.293 62.119 53.953 0.50 17.51 ? 443 GLN A CG 1 ATOM 3138 C CD A GLN A 1 402 ? -0.166 61.251 51.952 0.50 15.06 ? 443 GLN A CD 1 ATOM 3139 C CD B GLN A 1 402 ? 1.185 62.958 53.098 0.50 20.17 ? 443 GLN A CD 1 ATOM 3140 O OE1 A GLN A 1 402 ? 0.683 61.144 51.047 0.50 14.56 ? 443 GLN A OE1 1 ATOM 3141 O OE1 B GLN A 1 402 ? 1.632 62.483 52.029 0.50 20.20 ? 443 GLN A OE1 1 ATOM 3142 N NE2 A GLN A 1 402 ? -1.391 61.640 51.736 0.50 15.89 ? 443 GLN A NE2 1 ATOM 3143 N NE2 B GLN A 1 402 ? 1.485 64.204 53.566 0.50 11.64 ? 443 GLN A NE2 1 ATOM 3144 N N . GLU A 1 403 ? 0.616 60.437 56.751 1.00 15.33 ? 444 GLU A N 1 ATOM 3145 C CA . GLU A 1 403 ? 0.340 61.216 57.960 1.00 14.40 ? 444 GLU A CA 1 ATOM 3146 C C . GLU A 1 403 ? 0.945 60.571 59.212 1.00 15.85 ? 444 GLU A C 1 ATOM 3147 O O . GLU A 1 403 ? 1.046 61.265 60.250 1.00 15.06 ? 444 GLU A O 1 ATOM 3148 C CB . GLU A 1 403 ? -1.170 61.423 58.174 1.00 15.33 ? 444 GLU A CB 1 ATOM 3149 C CG . GLU A 1 403 ? -1.874 61.953 56.922 1.00 17.11 ? 444 GLU A CG 1 ATOM 3150 C CD . GLU A 1 403 ? -1.301 63.286 56.421 1.00 21.98 ? 444 GLU A CD 1 ATOM 3151 O OE1 . GLU A 1 403 ? -0.319 63.834 56.982 1.00 17.10 ? 444 GLU A OE1 1 ATOM 3152 O OE2 . GLU A 1 403 ? -1.826 63.786 55.410 1.00 21.23 ? 444 GLU A OE2 1 ATOM 3153 N N . ARG A 1 404 ? 1.349 59.310 59.122 1.00 15.06 ? 445 ARG A N 1 ATOM 3154 C CA . ARG A 1 404 ? 1.831 58.604 60.315 1.00 14.28 ? 445 ARG A CA 1 ATOM 3155 C C . ARG A 1 404 ? 3.233 58.027 60.183 1.00 16.13 ? 445 ARG A C 1 ATOM 3156 O O . ARG A 1 404 ? 3.756 57.536 61.164 1.00 15.76 ? 445 ARG A O 1 ATOM 3157 C CB . ARG A 1 404 ? 0.900 57.465 60.640 1.00 14.45 ? 445 ARG A CB 1 ATOM 3158 C CG . ARG A 1 404 ? -0.551 57.969 60.931 1.00 15.39 ? 445 ARG A CG 1 ATOM 3159 C CD . ARG A 1 404 ? -1.466 56.797 61.214 1.00 16.46 ? 445 ARG A CD 1 ATOM 3160 N NE . ARG A 1 404 ? -2.870 57.227 61.152 1.00 14.99 ? 445 ARG A NE 1 ATOM 3161 C CZ . ARG A 1 404 ? -3.935 56.426 61.094 1.00 17.09 ? 445 ARG A CZ 1 ATOM 3162 N NH1 . ARG A 1 404 ? -3.803 55.107 61.119 1.00 16.23 ? 445 ARG A NH1 1 ATOM 3163 N NH2 . ARG A 1 404 ? -5.150 56.976 61.021 1.00 17.79 ? 445 ARG A NH2 1 ATOM 3164 N N . GLY A 1 405 ? 3.817 58.041 58.978 1.00 14.86 ? 446 GLY A N 1 ATOM 3165 C CA . GLY A 1 405 ? 5.073 57.319 58.755 1.00 14.22 ? 446 GLY A CA 1 ATOM 3166 C C . GLY A 1 405 ? 6.281 58.088 59.265 1.00 15.04 ? 446 GLY A C 1 ATOM 3167 O O . GLY A 1 405 ? 6.634 59.166 58.764 1.00 17.43 ? 446 GLY A O 1 ATOM 3168 N N . VAL A 1 406 ? 6.939 57.516 60.257 1.00 15.48 ? 447 VAL A N 1 ATOM 3169 C CA . VAL A 1 406 ? 8.140 58.122 60.773 1.00 16.06 ? 447 VAL A CA 1 ATOM 3170 C C . VAL A 1 406 ? 9.367 57.807 59.936 1.00 15.95 ? 447 VAL A C 1 ATOM 3171 O O . VAL A 1 406 ? 10.107 58.725 59.544 1.00 16.22 ? 447 VAL A O 1 ATOM 3172 C CB . VAL A 1 406 ? 8.398 57.676 62.248 1.00 17.35 ? 447 VAL A CB 1 ATOM 3173 C CG1 . VAL A 1 406 ? 9.797 58.107 62.756 1.00 19.18 ? 447 VAL A CG1 1 ATOM 3174 C CG2 . VAL A 1 406 ? 7.310 58.273 63.148 1.00 18.93 ? 447 VAL A CG2 1 ATOM 3175 N N . ALA A 1 407 ? 9.575 56.521 59.627 1.00 15.44 ? 448 ALA A N 1 ATOM 3176 C CA . ALA A 1 407 ? 10.808 56.121 58.916 1.00 15.50 ? 448 ALA A CA 1 ATOM 3177 C C . ALA A 1 407 ? 10.609 54.761 58.370 1.00 15.77 ? 448 ALA A C 1 ATOM 3178 O O . ALA A 1 407 ? 9.758 54.009 58.848 1.00 16.08 ? 448 ALA A O 1 ATOM 3179 C CB . ALA A 1 407 ? 12.004 56.053 59.880 1.00 17.64 ? 448 ALA A CB 1 ATOM 3180 N N . TYR A 1 408 ? 11.419 54.456 57.359 1.00 15.13 ? 449 TYR A N 1 ATOM 3181 C CA . TYR A 1 408 ? 11.353 53.149 56.674 1.00 13.55 ? 449 TYR A CA 1 ATOM 3182 C C . TYR A 1 408 ? 12.823 52.715 56.634 1.00 14.82 ? 449 TYR A C 1 ATOM 3183 O O . TYR A 1 408 ? 13.687 53.413 56.080 1.00 15.19 ? 449 TYR A O 1 ATOM 3184 C CB . TYR A 1 408 ? 10.786 53.283 55.230 1.00 13.58 ? 449 TYR A CB 1 ATOM 3185 C CG . TYR A 1 408 ? 10.902 51.954 54.539 1.00 12.61 ? 449 TYR A CG 1 ATOM 3186 C CD1 . TYR A 1 408 ? 9.882 51.012 54.671 1.00 13.92 ? 449 TYR A CD1 1 ATOM 3187 C CD2 . TYR A 1 408 ? 11.990 51.670 53.704 1.00 14.21 ? 449 TYR A CD2 1 ATOM 3188 C CE1 . TYR A 1 408 ? 9.937 49.765 54.071 1.00 14.42 ? 449 TYR A CE1 1 ATOM 3189 C CE2 . TYR A 1 408 ? 12.097 50.402 53.068 1.00 15.08 ? 449 TYR A CE2 1 ATOM 3190 C CZ . TYR A 1 408 ? 11.067 49.484 53.245 1.00 14.16 ? 449 TYR A CZ 1 ATOM 3191 O OH . TYR A 1 408 ? 11.219 48.244 52.579 1.00 15.57 ? 449 TYR A OH 1 ATOM 3192 N N . ILE A 1 409 ? 13.085 51.511 57.138 1.00 14.06 ? 450 ILE A N 1 ATOM 3193 C CA . ILE A 1 409 ? 14.437 50.904 57.065 1.00 14.63 ? 450 ILE A CA 1 ATOM 3194 C C . ILE A 1 409 ? 14.327 49.671 56.166 1.00 15.64 ? 450 ILE A C 1 ATOM 3195 O O . ILE A 1 409 ? 13.523 48.752 56.446 1.00 14.56 ? 450 ILE A O 1 ATOM 3196 C CB . ILE A 1 409 ? 14.917 50.466 58.471 1.00 14.75 ? 450 ILE A CB 1 ATOM 3197 C CG1 . ILE A 1 409 ? 15.026 51.683 59.430 1.00 16.32 ? 450 ILE A CG1 1 ATOM 3198 C CG2 . ILE A 1 409 ? 16.276 49.740 58.358 1.00 16.14 ? 450 ILE A CG2 1 ATOM 3199 C CD1 . ILE A 1 409 ? 15.949 52.805 58.906 1.00 18.94 ? 450 ILE A CD1 1 ATOM 3200 N N . ASN A 1 410 ? 15.100 49.678 55.077 1.00 14.93 ? 451 ASN A N 1 ATOM 3201 C CA . ASN A 1 410 ? 15.040 48.536 54.151 1.00 13.56 ? 451 ASN A CA 1 ATOM 3202 C C . ASN A 1 410 ? 15.831 47.360 54.699 1.00 15.91 ? 451 ASN A C 1 ATOM 3203 O O . ASN A 1 410 ? 16.705 47.527 55.550 1.00 16.88 ? 451 ASN A O 1 ATOM 3204 C CB . ASN A 1 410 ? 15.591 48.965 52.782 1.00 13.27 ? 451 ASN A CB 1 ATOM 3205 C CG . ASN A 1 410 ? 14.984 48.169 51.647 1.00 14.80 ? 451 ASN A CG 1 ATOM 3206 O OD1 . ASN A 1 410 ? 13.744 48.044 51.520 1.00 15.87 ? 451 ASN A OD1 1 ATOM 3207 N ND2 . ASN A 1 410 ? 15.853 47.616 50.801 1.00 16.33 ? 451 ASN A ND2 1 ATOM 3208 N N . ALA A 1 411 ? 15.544 46.166 54.182 1.00 16.01 ? 452 ALA A N 1 ATOM 3209 C CA . ALA A 1 411 ? 16.265 44.978 54.646 1.00 16.63 ? 452 ALA A CA 1 ATOM 3210 C C . ALA A 1 411 ? 16.393 43.929 53.530 1.00 16.38 ? 452 ALA A C 1 ATOM 3211 O O . ALA A 1 411 ? 15.930 42.765 53.680 1.00 16.67 ? 452 ALA A O 1 ATOM 3212 C CB . ALA A 1 411 ? 15.575 44.442 55.933 1.00 18.09 ? 452 ALA A CB 1 ATOM 3213 N N . ASP A 1 412 ? 16.983 44.317 52.398 1.00 15.74 ? 453 ASP A N 1 ATOM 3214 C CA . ASP A 1 412 ? 17.358 43.301 51.399 1.00 15.67 ? 453 ASP A CA 1 ATOM 3215 C C . ASP A 1 412 ? 18.730 42.745 51.800 1.00 16.69 ? 453 ASP A C 1 ATOM 3216 O O . ASP A 1 412 ? 19.043 42.768 53.018 1.00 15.59 ? 453 ASP A O 1 ATOM 3217 C CB . ASP A 1 412 ? 17.348 43.902 49.993 1.00 15.18 ? 453 ASP A CB 1 ATOM 3218 C CG . ASP A 1 412 ? 17.207 42.858 48.877 1.00 17.19 ? 453 ASP A CG 1 ATOM 3219 O OD1 . ASP A 1 412 ? 17.248 41.663 49.161 1.00 19.06 ? 453 ASP A OD1 1 ATOM 3220 O OD2 . ASP A 1 412 ? 17.106 43.283 47.708 1.00 16.14 ? 453 ASP A OD2 1 ATOM 3221 N N . SER A 1 413 ? 19.494 42.252 50.820 1.00 15.66 ? 454 SER A N 1 ATOM 3222 C CA . SER A 1 413 ? 20.791 41.563 51.076 1.00 16.93 ? 454 SER A CA 1 ATOM 3223 C C . SER A 1 413 ? 21.602 42.167 52.223 1.00 17.69 ? 454 SER A C 1 ATOM 3224 O O . SER A 1 413 ? 21.861 43.372 52.251 1.00 17.00 ? 454 SER A O 1 ATOM 3225 C CB . SER A 1 413 ? 21.609 41.598 49.817 1.00 18.44 ? 454 SER A CB 1 ATOM 3226 O OG . SER A 1 413 ? 20.830 41.015 48.828 1.00 16.77 ? 454 SER A OG 1 ATOM 3227 N N . SER A 1 414 ? 21.941 41.327 53.204 1.00 18.54 ? 455 SER A N 1 ATOM 3228 C CA . SER A 1 414 ? 22.719 41.823 54.352 1.00 19.55 ? 455 SER A CA 1 ATOM 3229 C C . SER A 1 414 ? 24.204 41.965 54.031 1.00 19.38 ? 455 SER A C 1 ATOM 3230 O O . SER A 1 414 ? 24.938 42.673 54.734 1.00 18.65 ? 455 SER A O 1 ATOM 3231 C CB . SER A 1 414 ? 22.572 40.904 55.562 1.00 20.08 ? 455 SER A CB 1 ATOM 3232 O OG . SER A 1 414 ? 21.237 40.989 56.067 1.00 20.35 ? 455 SER A OG 1 ATOM 3233 N N . ILE A 1 415 ? 24.650 41.277 52.980 1.00 19.91 ? 456 ILE A N 1 ATOM 3234 C CA . ILE A 1 415 ? 26.066 41.254 52.638 1.00 20.13 ? 456 ILE A CA 1 ATOM 3235 C C . ILE A 1 415 ? 26.228 41.317 51.134 1.00 21.21 ? 456 ILE A C 1 ATOM 3236 O O . ILE A 1 415 ? 25.459 40.711 50.399 1.00 22.28 ? 456 ILE A O 1 ATOM 3237 C CB . ILE A 1 415 ? 26.765 39.948 53.189 1.00 19.68 ? 456 ILE A CB 1 ATOM 3238 C CG1 . ILE A 1 415 ? 25.946 38.699 52.770 1.00 22.42 ? 456 ILE A CG1 1 ATOM 3239 C CG2 . ILE A 1 415 ? 26.840 39.980 54.726 1.00 20.94 ? 456 ILE A CG2 1 ATOM 3240 C CD1 . ILE A 1 415 ? 26.732 37.479 52.531 1.00 28.47 ? 456 ILE A CD1 1 ATOM 3241 N N . GLU A 1 416 ? 27.259 42.013 50.654 1.00 20.75 ? 457 GLU A N 1 ATOM 3242 C CA . GLU A 1 416 ? 27.663 41.872 49.247 1.00 20.72 ? 457 GLU A CA 1 ATOM 3243 C C . GLU A 1 416 ? 29.203 41.785 49.241 1.00 21.39 ? 457 GLU A C 1 ATOM 3244 O O . GLU A 1 416 ? 29.833 41.911 48.214 1.00 21.46 ? 457 GLU A O 1 ATOM 3245 C CB . GLU A 1 416 ? 27.184 43.044 48.404 1.00 21.60 ? 457 GLU A CB 1 ATOM 3246 C CG . GLU A 1 416 ? 27.690 44.414 48.928 1.00 22.65 ? 457 GLU A CG 1 ATOM 3247 C CD . GLU A 1 416 ? 27.032 45.611 48.224 1.00 23.49 ? 457 GLU A CD 1 ATOM 3248 O OE1 . GLU A 1 416 ? 25.997 45.450 47.549 1.00 23.87 ? 457 GLU A OE1 1 ATOM 3249 O OE2 . GLU A 1 416 ? 27.564 46.737 48.397 1.00 24.29 ? 457 GLU A OE2 1 ATOM 3250 N N . GLY A 1 417 ? 29.753 41.571 50.427 1.00 21.64 ? 458 GLY A N 1 ATOM 3251 C CA . GLY A 1 417 ? 31.207 41.480 50.661 1.00 21.57 ? 458 GLY A CA 1 ATOM 3252 C C . GLY A 1 417 ? 31.464 41.353 52.159 1.00 22.59 ? 458 GLY A C 1 ATOM 3253 O O . GLY A 1 417 ? 30.512 41.197 52.968 1.00 22.65 ? 458 GLY A O 1 ATOM 3254 N N . ASN A 1 418 ? 32.735 41.329 52.564 1.00 23.26 ? 459 ASN A N 1 ATOM 3255 C CA . ASN A 1 418 ? 33.016 41.088 53.977 1.00 23.94 ? 459 ASN A CA 1 ATOM 3256 C C . ASN A 1 418 ? 34.047 42.100 54.493 1.00 25.02 ? 459 ASN A C 1 ATOM 3257 O O . ASN A 1 418 ? 34.819 41.818 55.430 1.00 26.94 ? 459 ASN A O 1 ATOM 3258 C CB . ASN A 1 418 ? 33.505 39.610 54.200 1.00 25.47 ? 459 ASN A CB 1 ATOM 3259 C CG . ASN A 1 418 ? 34.812 39.304 53.484 1.00 28.87 ? 459 ASN A CG 1 ATOM 3260 O OD1 . ASN A 1 418 ? 35.404 40.184 52.881 1.00 30.52 ? 459 ASN A OD1 1 ATOM 3261 N ND2 . ASN A 1 418 ? 35.271 38.038 53.553 1.00 37.75 ? 459 ASN A ND2 1 ATOM 3262 N N . TYR A 1 419 ? 34.051 43.287 53.900 1.00 22.81 ? 460 TYR A N 1 ATOM 3263 C CA . TYR A 1 419 ? 35.123 44.248 54.189 1.00 23.44 ? 460 TYR A CA 1 ATOM 3264 C C . TYR A 1 419 ? 34.685 45.297 55.191 1.00 22.56 ? 460 TYR A C 1 ATOM 3265 O O . TYR A 1 419 ? 35.348 45.510 56.218 1.00 22.70 ? 460 TYR A O 1 ATOM 3266 C CB . TYR A 1 419 ? 35.581 44.920 52.901 1.00 23.37 ? 460 TYR A CB 1 ATOM 3267 C CG . TYR A 1 419 ? 36.701 45.917 53.098 1.00 25.79 ? 460 TYR A CG 1 ATOM 3268 C CD1 . TYR A 1 419 ? 37.964 45.499 53.528 1.00 28.55 ? 460 TYR A CD1 1 ATOM 3269 C CD2 . TYR A 1 419 ? 36.496 47.262 52.813 1.00 28.38 ? 460 TYR A CD2 1 ATOM 3270 C CE1 . TYR A 1 419 ? 38.997 46.414 53.688 1.00 30.03 ? 460 TYR A CE1 1 ATOM 3271 C CE2 . TYR A 1 419 ? 37.524 48.186 52.965 1.00 28.70 ? 460 TYR A CE2 1 ATOM 3272 C CZ . TYR A 1 419 ? 38.769 47.733 53.405 1.00 32.23 ? 460 TYR A CZ 1 ATOM 3273 O OH . TYR A 1 419 ? 39.792 48.623 53.566 1.00 37.57 ? 460 TYR A OH 1 ATOM 3274 N N . THR A 1 420 ? 33.577 46.009 54.913 1.00 21.24 ? 461 THR A N 1 ATOM 3275 C CA . THR A 1 420 ? 33.163 47.036 55.875 1.00 19.78 ? 461 THR A CA 1 ATOM 3276 C C . THR A 1 420 ? 31.662 47.351 55.688 1.00 20.18 ? 461 THR A C 1 ATOM 3277 O O . THR A 1 420 ? 30.987 46.729 54.836 1.00 20.12 ? 461 THR A O 1 ATOM 3278 C CB . THR A 1 420 ? 33.981 48.341 55.750 1.00 21.31 ? 461 THR A CB 1 ATOM 3279 O OG1 . THR A 1 420 ? 33.752 49.191 56.867 1.00 22.03 ? 461 THR A OG1 1 ATOM 3280 C CG2 . THR A 1 420 ? 33.682 49.118 54.440 1.00 21.46 ? 461 THR A CG2 1 ATOM 3281 N N . LEU A 1 421 ? 31.186 48.293 56.489 1.00 19.73 ? 462 LEU A N 1 ATOM 3282 C CA . LEU A 1 421 ? 29.748 48.670 56.416 1.00 19.18 ? 462 LEU A CA 1 ATOM 3283 C C . LEU A 1 421 ? 29.489 49.577 55.211 1.00 20.00 ? 462 LEU A C 1 ATOM 3284 O O . LEU A 1 421 ? 30.365 50.353 54.792 1.00 20.63 ? 462 LEU A O 1 ATOM 3285 C CB . LEU A 1 421 ? 29.342 49.389 57.701 1.00 20.49 ? 462 LEU A CB 1 ATOM 3286 C CG . LEU A 1 421 ? 27.824 49.567 57.912 1.00 20.77 ? 462 LEU A CG 1 ATOM 3287 C CD1 . LEU A 1 421 ? 27.164 48.209 58.200 1.00 22.13 ? 462 LEU A CD1 1 ATOM 3288 C CD2 . LEU A 1 421 ? 27.688 50.489 59.123 1.00 19.19 ? 462 LEU A CD2 1 ATOM 3289 N N . ARG A 1 422 ? 28.256 49.507 54.697 1.00 18.64 ? 463 ARG A N 1 ATOM 3290 C CA A ARG A 1 422 ? 27.760 50.397 53.643 0.50 18.39 ? 463 ARG A CA 1 ATOM 3291 C CA B ARG A 1 422 ? 27.770 50.425 53.681 0.50 18.27 ? 463 ARG A CA 1 ATOM 3292 C C . ARG A 1 422 ? 26.425 50.919 54.178 1.00 18.29 ? 463 ARG A C 1 ATOM 3293 O O . ARG A 1 422 ? 25.563 50.116 54.553 1.00 19.74 ? 463 ARG A O 1 ATOM 3294 C CB A ARG A 1 422 ? 27.568 49.632 52.297 0.50 18.19 ? 463 ARG A CB 1 ATOM 3295 C CB B ARG A 1 422 ? 27.578 49.738 52.323 0.50 18.09 ? 463 ARG A CB 1 ATOM 3296 C CG A ARG A 1 422 ? 27.262 50.528 51.052 0.50 19.91 ? 463 ARG A CG 1 ATOM 3297 C CG B ARG A 1 422 ? 26.596 50.521 51.442 0.50 18.82 ? 463 ARG A CG 1 ATOM 3298 C CD A ARG A 1 422 ? 27.035 49.686 49.798 0.50 21.86 ? 463 ARG A CD 1 ATOM 3299 C CD B ARG A 1 422 ? 26.340 49.780 50.189 0.50 17.00 ? 463 ARG A CD 1 ATOM 3300 N NE A ARG A 1 422 ? 26.714 50.506 48.630 0.50 24.37 ? 463 ARG A NE 1 ATOM 3301 N NE B ARG A 1 422 ? 25.284 50.424 49.431 0.50 17.74 ? 463 ARG A NE 1 ATOM 3302 C CZ A ARG A 1 422 ? 26.269 50.025 47.473 0.50 25.35 ? 463 ARG A CZ 1 ATOM 3303 C CZ B ARG A 1 422 ? 24.714 49.851 48.386 0.50 18.81 ? 463 ARG A CZ 1 ATOM 3304 N NH1 A ARG A 1 422 ? 26.095 48.720 47.326 0.50 25.59 ? 463 ARG A NH1 1 ATOM 3305 N NH1 B ARG A 1 422 ? 25.110 48.630 48.019 0.50 17.51 ? 463 ARG A NH1 1 ATOM 3306 N NH2 A ARG A 1 422 ? 25.996 50.855 46.465 0.50 26.44 ? 463 ARG A NH2 1 ATOM 3307 N NH2 B ARG A 1 422 ? 23.746 50.476 47.733 0.50 17.36 ? 463 ARG A NH2 1 ATOM 3308 N N . VAL A 1 423 ? 26.272 52.240 54.259 1.00 17.90 ? 464 VAL A N 1 ATOM 3309 C CA . VAL A 1 423 ? 24.958 52.817 54.625 1.00 16.87 ? 464 VAL A CA 1 ATOM 3310 C C . VAL A 1 423 ? 24.587 53.841 53.563 1.00 17.88 ? 464 VAL A C 1 ATOM 3311 O O . VAL A 1 423 ? 25.411 54.680 53.212 1.00 17.44 ? 464 VAL A O 1 ATOM 3312 C CB . VAL A 1 423 ? 25.034 53.511 56.024 1.00 17.28 ? 464 VAL A CB 1 ATOM 3313 C CG1 . VAL A 1 423 ? 23.749 54.188 56.382 1.00 17.41 ? 464 VAL A CG1 1 ATOM 3314 C CG2 . VAL A 1 423 ? 25.441 52.512 57.102 1.00 21.47 ? 464 VAL A CG2 1 ATOM 3315 N N . ASP A 1 424 ? 23.328 53.804 53.093 1.00 16.54 ? 465 ASP A N 1 ATOM 3316 C CA . ASP A 1 424 ? 22.764 54.850 52.210 1.00 16.40 ? 465 ASP A CA 1 ATOM 3317 C C . ASP A 1 424 ? 21.504 55.296 52.947 1.00 16.52 ? 465 ASP A C 1 ATOM 3318 O O . ASP A 1 424 ? 20.660 54.465 53.319 1.00 16.13 ? 465 ASP A O 1 ATOM 3319 C CB . ASP A 1 424 ? 22.292 54.329 50.822 1.00 16.90 ? 465 ASP A CB 1 ATOM 3320 C CG . ASP A 1 424 ? 23.328 53.519 50.060 1.00 21.69 ? 465 ASP A CG 1 ATOM 3321 O OD1 . ASP A 1 424 ? 24.518 53.430 50.450 1.00 24.71 ? 465 ASP A OD1 1 ATOM 3322 O OD2 . ASP A 1 424 ? 22.942 52.923 49.004 1.00 20.28 ? 465 ASP A OD2 1 ATOM 3323 N N . CYS A 1 425 ? 21.333 56.592 53.149 1.00 16.49 ? 466 CYS A N 1 ATOM 3324 C CA . CYS A 1 425 ? 20.145 57.044 53.836 1.00 16.57 ? 466 CYS A CA 1 ATOM 3325 C C . CYS A 1 425 ? 19.929 58.526 53.680 1.00 16.32 ? 466 CYS A C 1 ATOM 3326 O O . CYS A 1 425 ? 20.797 59.243 53.231 1.00 18.10 ? 466 CYS A O 1 ATOM 3327 C CB . CYS A 1 425 ? 20.167 56.740 55.365 1.00 16.71 ? 466 CYS A CB 1 ATOM 3328 S SG . CYS A 1 425 ? 21.537 57.573 56.301 1.00 4.41 ? 466 CYS A SG 1 ATOM 3329 N N . THR A 1 426 ? 18.764 58.963 54.113 1.00 15.03 ? 467 THR A N 1 ATOM 3330 C CA . THR A 1 426 ? 18.516 60.388 54.222 1.00 15.22 ? 467 THR A CA 1 ATOM 3331 C C . THR A 1 426 ? 19.492 61.072 55.191 1.00 17.42 ? 467 THR A C 1 ATOM 3332 O O . THR A 1 426 ? 19.875 60.492 56.213 1.00 16.63 ? 467 THR A O 1 ATOM 3333 C CB . THR A 1 426 ? 17.046 60.645 54.712 1.00 14.18 ? 467 THR A CB 1 ATOM 3334 O OG1 . THR A 1 426 ? 16.923 62.043 54.918 1.00 15.84 ? 467 THR A OG1 1 ATOM 3335 C CG2 . THR A 1 426 ? 16.730 59.895 56.033 1.00 16.32 ? 467 THR A CG2 1 ATOM 3336 N N . PRO A 1 427 ? 19.862 62.330 54.907 1.00 16.23 ? 468 PRO A N 1 ATOM 3337 C CA . PRO A 1 427 ? 20.660 63.101 55.880 1.00 17.39 ? 468 PRO A CA 1 ATOM 3338 C C . PRO A 1 427 ? 20.035 63.101 57.269 1.00 16.74 ? 468 PRO A C 1 ATOM 3339 O O . PRO A 1 427 ? 20.733 63.253 58.279 1.00 18.06 ? 468 PRO A O 1 ATOM 3340 C CB . PRO A 1 427 ? 20.670 64.513 55.269 1.00 17.98 ? 468 PRO A CB 1 ATOM 3341 C CG . PRO A 1 427 ? 20.593 64.283 53.790 1.00 17.26 ? 468 PRO A CG 1 ATOM 3342 C CD . PRO A 1 427 ? 19.588 63.115 53.675 1.00 17.03 ? 468 PRO A CD 1 ATOM 3343 N N . LEU A 1 428 ? 18.690 63.021 57.349 1.00 15.85 ? 469 LEU A N 1 ATOM 3344 C CA . LEU A 1 428 ? 18.089 63.063 58.696 1.00 17.08 ? 469 LEU A CA 1 ATOM 3345 C C . LEU A 1 428 ? 18.543 61.915 59.614 1.00 16.65 ? 469 LEU A C 1 ATOM 3346 O O . LEU A 1 428 ? 18.416 62.053 60.853 1.00 18.72 ? 469 LEU A O 1 ATOM 3347 C CB . LEU A 1 428 ? 16.557 63.000 58.613 1.00 15.86 ? 469 LEU A CB 1 ATOM 3348 C CG . LEU A 1 428 ? 15.952 64.245 57.988 1.00 17.56 ? 469 LEU A CG 1 ATOM 3349 C CD1 . LEU A 1 428 ? 14.436 64.082 57.937 1.00 16.36 ? 469 LEU A CD1 1 ATOM 3350 C CD2 . LEU A 1 428 ? 16.340 65.513 58.792 1.00 16.65 ? 469 LEU A CD2 1 ATOM 3351 N N . MET A 1 429 ? 19.048 60.813 59.050 1.00 16.96 ? 470 MET A N 1 ATOM 3352 C CA . MET A 1 429 ? 19.548 59.679 59.849 1.00 16.71 ? 470 MET A CA 1 ATOM 3353 C C . MET A 1 429 ? 21.063 59.639 60.053 1.00 18.94 ? 470 MET A C 1 ATOM 3354 O O . MET A 1 429 ? 21.540 58.701 60.712 1.00 17.82 ? 470 MET A O 1 ATOM 3355 C CB . MET A 1 429 ? 19.051 58.347 59.239 1.00 17.25 ? 470 MET A CB 1 ATOM 3356 C CG . MET A 1 429 ? 17.548 58.124 59.388 1.00 20.18 ? 470 MET A CG 1 ATOM 3357 S SD . MET A 1 429 ? 17.195 56.560 58.502 1.00 5.66 ? 470 MET A SD 1 ATOM 3358 C CE . MET A 1 429 ? 15.412 56.643 58.391 1.00 20.97 ? 470 MET A CE 1 ATOM 3359 N N . TYR A 1 430 ? 21.831 60.615 59.522 1.00 17.84 ? 471 TYR A N 1 ATOM 3360 C CA . TYR A 1 430 ? 23.298 60.499 59.621 1.00 19.00 ? 471 TYR A CA 1 ATOM 3361 C C . TYR A 1 430 ? 23.741 60.403 61.085 1.00 19.96 ? 471 TYR A C 1 ATOM 3362 O O . TYR A 1 430 ? 24.613 59.574 61.459 1.00 21.01 ? 471 TYR A O 1 ATOM 3363 C CB . TYR A 1 430 ? 23.969 61.718 59.027 1.00 18.78 ? 471 TYR A CB 1 ATOM 3364 C CG . TYR A 1 430 ? 23.963 61.822 57.520 1.00 16.85 ? 471 TYR A CG 1 ATOM 3365 C CD1 . TYR A 1 430 ? 23.457 60.819 56.707 1.00 17.12 ? 471 TYR A CD1 1 ATOM 3366 C CD2 . TYR A 1 430 ? 24.434 62.995 56.924 1.00 19.39 ? 471 TYR A CD2 1 ATOM 3367 C CE1 . TYR A 1 430 ? 23.471 60.980 55.282 1.00 17.97 ? 471 TYR A CE1 1 ATOM 3368 C CE2 . TYR A 1 430 ? 24.459 63.158 55.570 1.00 19.99 ? 471 TYR A CE2 1 ATOM 3369 C CZ . TYR A 1 430 ? 23.978 62.165 54.747 1.00 20.14 ? 471 TYR A CZ 1 ATOM 3370 O OH . TYR A 1 430 ? 24.018 62.401 53.365 1.00 20.73 ? 471 TYR A OH 1 ATOM 3371 N N . SER A 1 431 ? 23.182 61.292 61.916 1.00 20.31 ? 472 SER A N 1 ATOM 3372 C CA . SER A 1 431 ? 23.655 61.377 63.333 1.00 20.18 ? 472 SER A CA 1 ATOM 3373 C C . SER A 1 431 ? 23.241 60.129 64.077 1.00 20.91 ? 472 SER A C 1 ATOM 3374 O O . SER A 1 431 ? 24.031 59.578 64.891 1.00 21.65 ? 472 SER A O 1 ATOM 3375 C CB . SER A 1 431 ? 23.094 62.649 63.971 1.00 22.11 ? 472 SER A CB 1 ATOM 3376 O OG A SER A 1 431 ? 23.849 63.763 63.464 0.50 23.91 ? 472 SER A OG 1 ATOM 3377 O OG B SER A 1 431 ? 23.394 62.763 65.378 0.50 18.33 ? 472 SER A OG 1 ATOM 3378 N N . LEU A 1 432 ? 22.018 59.658 63.820 1.00 20.23 ? 473 LEU A N 1 ATOM 3379 C CA . LEU A 1 432 ? 21.567 58.403 64.410 1.00 20.72 ? 473 LEU A CA 1 ATOM 3380 C C . LEU A 1 432 ? 22.566 57.253 64.070 1.00 20.66 ? 473 LEU A C 1 ATOM 3381 O O . LEU A 1 432 ? 22.938 56.417 64.913 1.00 21.96 ? 473 LEU A O 1 ATOM 3382 C CB . LEU A 1 432 ? 20.167 58.048 63.871 1.00 20.84 ? 473 LEU A CB 1 ATOM 3383 C CG . LEU A 1 432 ? 19.730 56.585 64.064 1.00 21.70 ? 473 LEU A CG 1 ATOM 3384 C CD1 . LEU A 1 432 ? 19.572 56.188 65.514 1.00 24.40 ? 473 LEU A CD1 1 ATOM 3385 C CD2 . LEU A 1 432 ? 18.462 56.391 63.303 1.00 23.80 ? 473 LEU A CD2 1 ATOM 3386 N N . VAL A 1 433 ? 22.973 57.200 62.809 1.00 19.08 ? 474 VAL A N 1 ATOM 3387 C CA . VAL A 1 433 ? 23.872 56.123 62.354 1.00 18.86 ? 474 VAL A CA 1 ATOM 3388 C C . VAL A 1 433 ? 25.237 56.269 63.015 1.00 20.75 ? 474 VAL A C 1 ATOM 3389 O O . VAL A 1 433 ? 25.828 55.247 63.477 1.00 21.74 ? 474 VAL A O 1 ATOM 3390 C CB . VAL A 1 433 ? 23.958 56.113 60.788 1.00 19.27 ? 474 VAL A CB 1 ATOM 3391 C CG1 . VAL A 1 433 ? 25.088 55.197 60.326 1.00 21.09 ? 474 VAL A CG1 1 ATOM 3392 C CG2 . VAL A 1 433 ? 22.600 55.627 60.220 1.00 20.24 ? 474 VAL A CG2 1 ATOM 3393 N N . HIS A 1 434 ? 25.762 57.489 63.053 1.00 20.55 ? 475 HIS A N 1 ATOM 3394 C CA . HIS A 1 434 ? 27.096 57.675 63.694 1.00 23.34 ? 475 HIS A CA 1 ATOM 3395 C C . HIS A 1 434 ? 27.006 57.208 65.133 1.00 23.20 ? 475 HIS A C 1 ATOM 3396 O O . HIS A 1 434 ? 27.869 56.440 65.615 1.00 24.23 ? 475 HIS A O 1 ATOM 3397 C CB . HIS A 1 434 ? 27.548 59.127 63.661 1.00 23.60 ? 475 HIS A CB 1 ATOM 3398 C CG . HIS A 1 434 ? 27.850 59.621 62.291 1.00 26.77 ? 475 HIS A CG 1 ATOM 3399 N ND1 . HIS A 1 434 ? 27.949 60.962 61.996 1.00 37.01 ? 475 HIS A ND1 1 ATOM 3400 C CD2 . HIS A 1 434 ? 28.002 58.966 61.120 1.00 28.24 ? 475 HIS A CD2 1 ATOM 3401 C CE1 . HIS A 1 434 ? 28.195 61.106 60.704 1.00 35.52 ? 475 HIS A CE1 1 ATOM 3402 N NE2 . HIS A 1 434 ? 28.242 59.911 60.154 1.00 29.05 ? 475 HIS A NE2 1 ATOM 3403 N N . ASN A 1 435 ? 25.986 57.682 65.823 1.00 22.69 ? 476 ASN A N 1 ATOM 3404 C CA . ASN A 1 435 ? 25.846 57.364 67.245 1.00 23.97 ? 476 ASN A CA 1 ATOM 3405 C C . ASN A 1 435 ? 25.678 55.876 67.490 1.00 24.02 ? 476 ASN A C 1 ATOM 3406 O O . ASN A 1 435 ? 26.284 55.308 68.429 1.00 25.72 ? 476 ASN A O 1 ATOM 3407 C CB . ASN A 1 435 ? 24.694 58.137 67.899 1.00 23.82 ? 476 ASN A CB 1 ATOM 3408 C CG . ASN A 1 435 ? 24.985 59.615 68.058 1.00 25.36 ? 476 ASN A CG 1 ATOM 3409 O OD1 . ASN A 1 435 ? 26.029 60.115 67.645 1.00 24.36 ? 476 ASN A OD1 1 ATOM 3410 N ND2 . ASN A 1 435 ? 24.021 60.347 68.661 1.00 24.77 ? 476 ASN A ND2 1 ATOM 3411 N N . LEU A 1 436 ? 24.847 55.232 66.690 1.00 22.29 ? 477 LEU A N 1 ATOM 3412 C CA . LEU A 1 436 ? 24.596 53.811 66.894 1.00 22.37 ? 477 LEU A CA 1 ATOM 3413 C C . LEU A 1 436 ? 25.845 53.001 66.671 1.00 22.24 ? 477 LEU A C 1 ATOM 3414 O O . LEU A 1 436 ? 26.181 52.086 67.454 1.00 23.18 ? 477 LEU A O 1 ATOM 3415 C CB . LEU A 1 436 ? 23.474 53.326 65.947 1.00 21.94 ? 477 LEU A CB 1 ATOM 3416 C CG . LEU A 1 436 ? 23.271 51.809 66.026 1.00 22.97 ? 477 LEU A CG 1 ATOM 3417 C CD1 . LEU A 1 436 ? 22.866 51.364 67.470 1.00 23.29 ? 477 LEU A CD1 1 ATOM 3418 C CD2 . LEU A 1 436 ? 22.211 51.416 64.982 1.00 25.83 ? 477 LEU A CD2 1 ATOM 3419 N N . THR A 1 437 ? 26.551 53.299 65.583 1.00 21.66 ? 478 THR A N 1 ATOM 3420 C CA . THR A 1 437 ? 27.748 52.504 65.244 1.00 21.96 ? 478 THR A CA 1 ATOM 3421 C C . THR A 1 437 ? 28.909 52.697 66.224 1.00 23.39 ? 478 THR A C 1 ATOM 3422 O O . THR A 1 437 ? 29.778 51.821 66.314 1.00 23.66 ? 478 THR A O 1 ATOM 3423 C CB . THR A 1 437 ? 28.231 52.746 63.796 1.00 22.95 ? 478 THR A CB 1 ATOM 3424 O OG1 . THR A 1 437 ? 28.591 54.113 63.603 1.00 22.70 ? 478 THR A OG1 1 ATOM 3425 C CG2 . THR A 1 437 ? 27.138 52.314 62.725 1.00 23.88 ? 478 THR A CG2 1 ATOM 3426 N N . LYS A 1 438 ? 28.898 53.806 66.959 1.00 23.78 ? 479 LYS A N 1 ATOM 3427 C CA . LYS A 1 438 ? 29.919 54.008 68.014 1.00 25.70 ? 479 LYS A CA 1 ATOM 3428 C C . LYS A 1 438 ? 29.648 53.087 69.191 1.00 26.41 ? 479 LYS A C 1 ATOM 3429 O O . LYS A 1 438 ? 30.566 52.861 70.020 1.00 27.47 ? 479 LYS A O 1 ATOM 3430 C CB . LYS A 1 438 ? 29.924 55.469 68.503 1.00 26.18 ? 479 LYS A CB 1 ATOM 3431 C CG . LYS A 1 438 ? 30.495 56.428 67.474 1.00 27.05 ? 479 LYS A CG 1 ATOM 3432 C CD . LYS A 1 438 ? 30.382 57.892 67.880 1.00 28.02 ? 479 LYS A CD 1 ATOM 3433 C CE . LYS A 1 438 ? 30.919 58.742 66.761 1.00 29.54 ? 479 LYS A CE 1 ATOM 3434 N NZ . LYS A 1 438 ? 30.810 60.203 67.091 1.00 34.18 ? 479 LYS A NZ 1 ATOM 3435 N N . GLU A 1 439 ? 28.428 52.578 69.299 1.00 25.91 ? 480 GLU A N 1 ATOM 3436 C CA . GLU A 1 439 ? 28.045 51.699 70.414 1.00 29.07 ? 480 GLU A CA 1 ATOM 3437 C C . GLU A 1 439 ? 28.074 50.232 70.060 1.00 28.80 ? 480 GLU A C 1 ATOM 3438 O O . GLU A 1 439 ? 27.821 49.383 70.913 1.00 30.47 ? 480 GLU A O 1 ATOM 3439 C CB . GLU A 1 439 ? 26.628 52.016 70.876 1.00 29.13 ? 480 GLU A CB 1 ATOM 3440 C CG . GLU A 1 439 ? 26.434 53.437 71.400 1.00 36.01 ? 480 GLU A CG 1 ATOM 3441 C CD . GLU A 1 439 ? 27.291 53.735 72.618 1.00 45.28 ? 480 GLU A CD 1 ATOM 3442 O OE1 . GLU A 1 439 ? 27.426 52.828 73.484 1.00 48.72 ? 480 GLU A OE1 1 ATOM 3443 O OE2 . GLU A 1 439 ? 27.828 54.873 72.709 1.00 51.14 ? 480 GLU A OE2 1 ATOM 3444 N N . LEU A 1 440 ? 28.310 49.924 68.789 1.00 26.50 ? 481 LEU A N 1 ATOM 3445 C CA . LEU A 1 440 ? 28.369 48.538 68.364 1.00 25.64 ? 481 LEU A CA 1 ATOM 3446 C C . LEU A 1 440 ? 29.813 48.061 68.232 1.00 26.12 ? 481 LEU A C 1 ATOM 3447 O O . LEU A 1 440 ? 30.694 48.859 67.922 1.00 27.05 ? 481 LEU A O 1 ATOM 3448 C CB . LEU A 1 440 ? 27.673 48.366 66.997 1.00 23.85 ? 481 LEU A CB 1 ATOM 3449 C CG . LEU A 1 440 ? 26.200 48.791 66.953 1.00 24.32 ? 481 LEU A CG 1 ATOM 3450 C CD1 . LEU A 1 440 ? 25.684 48.642 65.506 1.00 22.96 ? 481 LEU A CD1 1 ATOM 3451 C CD2 . LEU A 1 440 ? 25.379 47.933 67.924 1.00 23.84 ? 481 LEU A CD2 1 ATOM 3452 N N . LYS A 1 441 ? 30.016 46.763 68.409 1.00 26.27 ? 482 LYS A N 1 ATOM 3453 C CA . LYS A 1 441 ? 31.350 46.152 68.293 1.00 27.61 ? 482 LYS A CA 1 ATOM 3454 C C . LYS A 1 441 ? 31.721 45.901 66.833 1.00 27.47 ? 482 LYS A C 1 ATOM 3455 O O . LYS A 1 441 ? 30.867 45.421 66.048 1.00 28.41 ? 482 LYS A O 1 ATOM 3456 C CB . LYS A 1 441 ? 31.365 44.817 69.022 1.00 28.15 ? 482 LYS A CB 1 ATOM 3457 C CG . LYS A 1 441 ? 31.156 45.003 70.527 1.00 31.90 ? 482 LYS A CG 1 ATOM 3458 C CD . LYS A 1 441 ? 31.597 43.797 71.305 1.00 41.16 ? 482 LYS A CD 1 ATOM 3459 C CE . LYS A 1 441 ? 30.681 42.626 71.067 1.00 43.94 ? 482 LYS A CE 1 ATOM 3460 N NZ . LYS A 1 441 ? 30.904 41.589 72.131 1.00 51.11 ? 482 LYS A NZ 1 ATOM 3461 N N . SER A 1 442 ? 32.952 46.195 66.441 1.00 26.07 ? 483 SER A N 1 ATOM 3462 C CA . SER A 1 442 ? 33.357 45.841 65.084 1.00 25.97 ? 483 SER A CA 1 ATOM 3463 C C . SER A 1 442 ? 33.536 44.333 64.962 1.00 26.46 ? 483 SER A C 1 ATOM 3464 O O . SER A 1 442 ? 34.186 43.703 65.842 1.00 26.96 ? 483 SER A O 1 ATOM 3465 C CB . SER A 1 442 ? 34.674 46.509 64.664 1.00 26.18 ? 483 SER A CB 1 ATOM 3466 O OG . SER A 1 442 ? 35.046 46.059 63.374 1.00 25.48 ? 483 SER A OG 1 ATOM 3467 N N . PRO A 1 443 ? 33.045 43.745 63.858 1.00 25.58 ? 484 PRO A N 1 ATOM 3468 C CA . PRO A 1 443 ? 33.258 42.309 63.681 1.00 25.62 ? 484 PRO A CA 1 ATOM 3469 C C . PRO A 1 443 ? 34.553 42.043 62.904 1.00 26.39 ? 484 PRO A C 1 ATOM 3470 O O . PRO A 1 443 ? 34.843 40.876 62.592 1.00 25.96 ? 484 PRO A O 1 ATOM 3471 C CB . PRO A 1 443 ? 32.064 41.897 62.820 1.00 25.16 ? 484 PRO A CB 1 ATOM 3472 C CG . PRO A 1 443 ? 31.831 43.115 61.932 1.00 24.50 ? 484 PRO A CG 1 ATOM 3473 C CD . PRO A 1 443 ? 32.148 44.316 62.814 1.00 25.69 ? 484 PRO A CD 1 ATOM 3474 N N . ASP A 1 444 ? 35.300 43.099 62.561 1.00 26.65 ? 485 ASP A N 1 ATOM 3475 C CA . ASP A 1 444 ? 36.382 42.961 61.569 1.00 27.48 ? 485 ASP A CA 1 ATOM 3476 C C . ASP A 1 444 ? 37.645 42.416 62.263 1.00 28.68 ? 485 ASP A C 1 ATOM 3477 O O . ASP A 1 444 ? 37.953 42.819 63.393 1.00 28.53 ? 485 ASP A O 1 ATOM 3478 C CB . ASP A 1 444 ? 36.760 44.314 60.962 1.00 26.78 ? 485 ASP A CB 1 ATOM 3479 C CG . ASP A 1 444 ? 35.621 44.961 60.165 1.00 26.65 ? 485 ASP A CG 1 ATOM 3480 O OD1 . ASP A 1 444 ? 34.526 44.361 60.098 1.00 28.84 ? 485 ASP A OD1 1 ATOM 3481 O OD2 . ASP A 1 444 ? 35.833 46.057 59.602 1.00 26.95 ? 485 ASP A OD2 1 ATOM 3482 N N . GLU A 1 445 ? 38.350 41.532 61.574 1.00 29.78 ? 486 GLU A N 1 ATOM 3483 C CA . GLU A 1 445 ? 39.705 41.133 62.006 1.00 31.95 ? 486 GLU A CA 1 ATOM 3484 C C . GLU A 1 445 ? 40.598 42.359 62.150 1.00 31.60 ? 486 GLU A C 1 ATOM 3485 O O . GLU A 1 445 ? 40.648 43.224 61.263 1.00 32.48 ? 486 GLU A O 1 ATOM 3486 C CB . GLU A 1 445 ? 40.298 40.214 60.965 1.00 32.53 ? 486 GLU A CB 1 ATOM 3487 C CG . GLU A 1 445 ? 40.276 38.771 61.374 1.00 41.58 ? 486 GLU A CG 1 ATOM 3488 C CD . GLU A 1 445 ? 41.546 38.015 60.884 1.00 50.32 ? 486 GLU A CD 1 ATOM 3489 O OE1 . GLU A 1 445 ? 42.259 37.374 61.721 1.00 52.77 ? 486 GLU A OE1 1 ATOM 3490 O OE2 . GLU A 1 445 ? 41.830 38.086 59.657 1.00 53.88 ? 486 GLU A OE2 1 ATOM 3491 N N . GLY A 1 446 ? 41.341 42.446 63.256 1.00 32.37 ? 487 GLY A N 1 ATOM 3492 C CA . GLY A 1 446 ? 42.211 43.588 63.437 1.00 31.40 ? 487 GLY A CA 1 ATOM 3493 C C . GLY A 1 446 ? 41.552 44.677 64.241 1.00 32.37 ? 487 GLY A C 1 ATOM 3494 O O . GLY A 1 446 ? 42.220 45.565 64.756 1.00 33.54 ? 487 GLY A O 1 ATOM 3495 N N . PHE A 1 447 ? 40.226 44.628 64.347 1.00 31.05 ? 488 PHE A N 1 ATOM 3496 C CA . PHE A 1 447 ? 39.511 45.652 65.094 1.00 30.54 ? 488 PHE A CA 1 ATOM 3497 C C . PHE A 1 447 ? 38.806 45.080 66.319 1.00 31.71 ? 488 PHE A C 1 ATOM 3498 O O . PHE A 1 447 ? 37.812 45.625 66.790 1.00 31.28 ? 488 PHE A O 1 ATOM 3499 C CB . PHE A 1 447 ? 38.519 46.370 64.173 1.00 30.15 ? 488 PHE A CB 1 ATOM 3500 C CG . PHE A 1 447 ? 39.183 47.171 63.122 1.00 26.87 ? 488 PHE A CG 1 ATOM 3501 C CD1 . PHE A 1 447 ? 39.424 48.519 63.329 1.00 29.11 ? 488 PHE A CD1 1 ATOM 3502 C CD2 . PHE A 1 447 ? 39.594 46.573 61.935 1.00 28.28 ? 488 PHE A CD2 1 ATOM 3503 C CE1 . PHE A 1 447 ? 40.060 49.298 62.356 1.00 29.71 ? 488 PHE A CE1 1 ATOM 3504 C CE2 . PHE A 1 447 ? 40.226 47.341 60.943 1.00 27.12 ? 488 PHE A CE2 1 ATOM 3505 C CZ . PHE A 1 447 ? 40.452 48.697 61.161 1.00 27.97 ? 488 PHE A CZ 1 ATOM 3506 N N . GLU A 1 448 ? 39.323 43.971 66.833 1.00 31.83 ? 489 GLU A N 1 ATOM 3507 C CA . GLU A 1 448 ? 38.773 43.349 68.024 1.00 33.51 ? 489 GLU A CA 1 ATOM 3508 C C . GLU A 1 448 ? 38.790 44.364 69.155 1.00 33.90 ? 489 GLU A C 1 ATOM 3509 O O . GLU A 1 448 ? 39.820 45.014 69.418 1.00 35.61 ? 489 GLU A O 1 ATOM 3510 C CB . GLU A 1 448 ? 39.600 42.115 68.427 1.00 33.80 ? 489 GLU A CB 1 ATOM 3511 C CG . GLU A 1 448 ? 39.531 40.978 67.407 1.00 34.22 ? 489 GLU A CG 1 ATOM 3512 C CD . GLU A 1 448 ? 40.521 41.136 66.252 1.00 34.02 ? 489 GLU A CD 1 ATOM 3513 O OE1 . GLU A 1 448 ? 40.480 40.274 65.345 1.00 36.07 ? 489 GLU A OE1 1 ATOM 3514 O OE2 . GLU A 1 448 ? 41.321 42.100 66.257 1.00 35.20 ? 489 GLU A OE2 1 ATOM 3515 N N . GLY A 1 449 ? 37.647 44.526 69.807 1.00 33.31 ? 490 GLY A N 1 ATOM 3516 C CA . GLY A 1 449 ? 37.536 45.471 70.903 1.00 33.26 ? 490 GLY A CA 1 ATOM 3517 C C . GLY A 1 449 ? 37.289 46.925 70.500 1.00 32.66 ? 490 GLY A C 1 ATOM 3518 O O . GLY A 1 449 ? 37.145 47.806 71.371 1.00 33.68 ? 490 GLY A O 1 ATOM 3519 N N . LYS A 1 450 ? 37.231 47.204 69.199 1.00 30.89 ? 491 LYS A N 1 ATOM 3520 C CA . LYS A 1 450 ? 36.996 48.551 68.742 1.00 29.98 ? 491 LYS A CA 1 ATOM 3521 C C . LYS A 1 450 ? 35.536 48.642 68.266 1.00 28.04 ? 491 LYS A C 1 ATOM 3522 O O . LYS A 1 450 ? 34.908 47.617 68.024 1.00 28.50 ? 491 LYS A O 1 ATOM 3523 C CB . LYS A 1 450 ? 37.908 48.873 67.561 1.00 30.09 ? 491 LYS A CB 1 ATOM 3524 C CG . LYS A 1 450 ? 39.420 48.683 67.852 1.00 33.05 ? 491 LYS A CG 1 ATOM 3525 C CD . LYS A 1 450 ? 39.815 49.530 69.072 1.00 38.42 ? 491 LYS A CD 1 ATOM 3526 C CE . LYS A 1 450 ? 41.336 49.494 69.320 1.00 43.08 ? 491 LYS A CE 1 ATOM 3527 N NZ . LYS A 1 450 ? 42.002 49.889 68.037 1.00 46.97 ? 491 LYS A NZ 1 ATOM 3528 N N . SER A 1 451 ? 35.036 49.862 68.131 1.00 27.32 ? 492 SER A N 1 ATOM 3529 C CA . SER A 1 451 ? 33.649 50.095 67.653 1.00 25.82 ? 492 SER A CA 1 ATOM 3530 C C . SER A 1 451 ? 33.562 49.855 66.156 1.00 25.82 ? 492 SER A C 1 ATOM 3531 O O . SER A 1 451 ? 34.530 49.982 65.411 1.00 24.63 ? 492 SER A O 1 ATOM 3532 C CB . SER A 1 451 ? 33.194 51.522 67.978 1.00 26.60 ? 492 SER A CB 1 ATOM 3533 O OG . SER A 1 451 ? 33.814 52.446 67.108 1.00 27.99 ? 492 SER A OG 1 ATOM 3534 N N . LEU A 1 452 ? 32.343 49.578 65.720 1.00 25.63 ? 493 LEU A N 1 ATOM 3535 C CA . LEU A 1 452 ? 32.036 49.473 64.289 1.00 24.07 ? 493 LEU A CA 1 ATOM 3536 C C . LEU A 1 452 ? 32.295 50.848 63.657 1.00 24.18 ? 493 LEU A C 1 ATOM 3537 O O . LEU A 1 452 ? 32.754 50.947 62.504 1.00 24.26 ? 493 LEU A O 1 ATOM 3538 C CB . LEU A 1 452 ? 30.554 49.072 64.139 1.00 23.01 ? 493 LEU A CB 1 ATOM 3539 C CG . LEU A 1 452 ? 30.031 48.987 62.703 1.00 25.76 ? 493 LEU A CG 1 ATOM 3540 C CD1 . LEU A 1 452 ? 30.823 48.012 61.820 1.00 24.60 ? 493 LEU A CD1 1 ATOM 3541 C CD2 . LEU A 1 452 ? 28.590 48.593 62.746 1.00 22.05 ? 493 LEU A CD2 1 ATOM 3542 N N . TYR A 1 453 ? 31.958 51.926 64.383 1.00 22.79 ? 494 TYR A N 1 ATOM 3543 C CA . TYR A 1 453 ? 32.252 53.254 63.855 1.00 23.54 ? 494 TYR A CA 1 ATOM 3544 C C . TYR A 1 453 ? 33.736 53.401 63.511 1.00 23.23 ? 494 TYR A C 1 ATOM 3545 O O . TYR A 1 453 ? 34.096 53.973 62.469 1.00 24.73 ? 494 TYR A O 1 ATOM 3546 C CB . TYR A 1 453 ? 31.884 54.366 64.843 1.00 23.39 ? 494 TYR A CB 1 ATOM 3547 C CG . TYR A 1 453 ? 32.092 55.772 64.313 1.00 23.66 ? 494 TYR A CG 1 ATOM 3548 C CD1 . TYR A 1 453 ? 31.055 56.468 63.682 1.00 22.63 ? 494 TYR A CD1 1 ATOM 3549 C CD2 . TYR A 1 453 ? 33.291 56.438 64.481 1.00 25.80 ? 494 TYR A CD2 1 ATOM 3550 C CE1 . TYR A 1 453 ? 31.231 57.760 63.205 1.00 23.64 ? 494 TYR A CE1 1 ATOM 3551 C CE2 . TYR A 1 453 ? 33.460 57.754 64.016 1.00 23.72 ? 494 TYR A CE2 1 ATOM 3552 C CZ . TYR A 1 453 ? 32.423 58.411 63.395 1.00 24.31 ? 494 TYR A CZ 1 ATOM 3553 O OH . TYR A 1 453 ? 32.601 59.685 62.919 1.00 27.14 ? 494 TYR A OH 1 ATOM 3554 N N . GLU A 1 454 ? 34.588 52.942 64.414 1.00 25.06 ? 495 GLU A N 1 ATOM 3555 C CA . GLU A 1 454 ? 36.020 53.064 64.189 1.00 25.55 ? 495 GLU A CA 1 ATOM 3556 C C . GLU A 1 454 ? 36.488 52.247 62.952 1.00 25.22 ? 495 GLU A C 1 ATOM 3557 O O . GLU A 1 454 ? 37.228 52.775 62.128 1.00 26.00 ? 495 GLU A O 1 ATOM 3558 C CB . GLU A 1 454 ? 36.819 52.627 65.434 1.00 28.01 ? 495 GLU A CB 1 ATOM 3559 C CG . GLU A 1 454 ? 38.310 52.699 65.175 1.00 31.35 ? 495 GLU A CG 1 ATOM 3560 C CD . GLU A 1 454 ? 39.141 52.483 66.432 1.00 38.46 ? 495 GLU A CD 1 ATOM 3561 O OE1 . GLU A 1 454 ? 38.686 52.919 67.524 1.00 39.71 ? 495 GLU A OE1 1 ATOM 3562 O OE2 . GLU A 1 454 ? 40.240 51.882 66.303 1.00 40.55 ? 495 GLU A OE2 1 ATOM 3563 N N . SER A 1 455 ? 36.023 50.999 62.814 1.00 24.09 ? 496 SER A N 1 ATOM 3564 C CA . SER A 1 455 ? 36.481 50.161 61.677 1.00 24.41 ? 496 SER A CA 1 ATOM 3565 C C . SER A 1 455 ? 35.934 50.706 60.370 1.00 24.70 ? 496 SER A C 1 ATOM 3566 O O . SER A 1 455 ? 36.642 50.840 59.359 1.00 24.27 ? 496 SER A O 1 ATOM 3567 C CB . SER A 1 455 ? 36.153 48.665 61.837 1.00 25.23 ? 496 SER A CB 1 ATOM 3568 O OG . SER A 1 455 ? 34.776 48.411 61.988 1.00 26.97 ? 496 SER A OG 1 ATOM 3569 N N . TRP A 1 456 ? 34.659 51.077 60.404 1.00 23.10 ? 497 TRP A N 1 ATOM 3570 C CA . TRP A 1 456 ? 34.004 51.614 59.236 1.00 23.47 ? 497 TRP A CA 1 ATOM 3571 C C . TRP A 1 456 ? 34.641 52.925 58.757 1.00 23.25 ? 497 TRP A C 1 ATOM 3572 O O . TRP A 1 456 ? 34.888 53.117 57.563 1.00 24.14 ? 497 TRP A O 1 ATOM 3573 C CB . TRP A 1 456 ? 32.539 51.803 59.626 1.00 22.47 ? 497 TRP A CB 1 ATOM 3574 C CG . TRP A 1 456 ? 31.656 52.390 58.542 1.00 22.51 ? 497 TRP A CG 1 ATOM 3575 C CD1 . TRP A 1 456 ? 31.821 52.292 57.171 1.00 23.03 ? 497 TRP A CD1 1 ATOM 3576 C CD2 . TRP A 1 456 ? 30.481 53.171 58.748 1.00 24.21 ? 497 TRP A CD2 1 ATOM 3577 N NE1 . TRP A 1 456 ? 30.773 52.970 56.516 1.00 24.95 ? 497 TRP A NE1 1 ATOM 3578 C CE2 . TRP A 1 456 ? 29.958 53.522 57.467 1.00 23.23 ? 497 TRP A CE2 1 ATOM 3579 C CE3 . TRP A 1 456 ? 29.810 53.625 59.906 1.00 23.47 ? 497 TRP A CE3 1 ATOM 3580 C CZ2 . TRP A 1 456 ? 28.785 54.297 57.320 1.00 23.08 ? 497 TRP A CZ2 1 ATOM 3581 C CZ3 . TRP A 1 456 ? 28.643 54.407 59.754 1.00 24.13 ? 497 TRP A CZ3 1 ATOM 3582 C CH2 . TRP A 1 456 ? 28.152 54.720 58.456 1.00 23.17 ? 497 TRP A CH2 1 ATOM 3583 N N . THR A 1 457 ? 34.904 53.841 59.687 1.00 24.47 ? 498 THR A N 1 ATOM 3584 C CA . THR A 1 457 ? 35.478 55.112 59.337 1.00 25.44 ? 498 THR A CA 1 ATOM 3585 C C . THR A 1 457 ? 36.916 54.925 58.781 1.00 26.80 ? 498 THR A C 1 ATOM 3586 O O . THR A 1 457 ? 37.326 55.591 57.828 1.00 26.20 ? 498 THR A O 1 ATOM 3587 C CB . THR A 1 457 ? 35.486 56.007 60.586 1.00 26.51 ? 498 THR A CB 1 ATOM 3588 O OG1 . THR A 1 457 ? 34.128 56.277 60.998 1.00 25.27 ? 498 THR A OG1 1 ATOM 3589 C CG2 . THR A 1 457 ? 36.217 57.337 60.298 1.00 28.28 ? 498 THR A CG2 1 ATOM 3590 N N . LYS A 1 458 ? 37.658 53.984 59.347 1.00 27.75 ? 499 LYS A N 1 ATOM 3591 C CA . LYS A 1 458 ? 39.013 53.748 58.874 1.00 29.51 ? 499 LYS A CA 1 ATOM 3592 C C . LYS A 1 458 ? 38.981 53.176 57.443 1.00 29.26 ? 499 LYS A C 1 ATOM 3593 O O . LYS A 1 458 ? 39.699 53.647 56.579 1.00 30.69 ? 499 LYS A O 1 ATOM 3594 C CB . LYS A 1 458 ? 39.753 52.805 59.828 1.00 30.40 ? 499 LYS A CB 1 ATOM 3595 C CG . LYS A 1 458 ? 41.092 52.315 59.310 1.00 35.02 ? 499 LYS A CG 1 ATOM 3596 C CD . LYS A 1 458 ? 42.026 53.468 59.093 1.00 42.52 ? 499 LYS A CD 1 ATOM 3597 C CE . LYS A 1 458 ? 43.478 52.971 58.931 1.00 47.19 ? 499 LYS A CE 1 ATOM 3598 N NZ . LYS A 1 458 ? 44.393 54.146 59.097 1.00 51.27 ? 499 LYS A NZ 1 ATOM 3599 N N . LYS A 1 459 ? 38.109 52.200 57.201 1.00 27.52 ? 500 LYS A N 1 ATOM 3600 C CA . LYS A 1 459 ? 38.006 51.519 55.888 1.00 27.66 ? 500 LYS A CA 1 ATOM 3601 C C . LYS A 1 459 ? 37.273 52.307 54.805 1.00 28.38 ? 500 LYS A C 1 ATOM 3602 O O . LYS A 1 459 ? 37.529 52.102 53.604 1.00 29.09 ? 500 LYS A O 1 ATOM 3603 C CB . LYS A 1 459 ? 37.327 50.169 56.085 1.00 27.11 ? 500 LYS A CB 1 ATOM 3604 C CG . LYS A 1 459 ? 38.221 49.169 56.851 1.00 25.89 ? 500 LYS A CG 1 ATOM 3605 C CD . LYS A 1 459 ? 37.470 47.828 56.998 1.00 24.02 ? 500 LYS A CD 1 ATOM 3606 C CE . LYS A 1 459 ? 38.408 46.736 57.560 1.00 27.17 ? 500 LYS A CE 1 ATOM 3607 N NZ . LYS A 1 459 ? 37.759 45.387 57.578 1.00 27.71 ? 500 LYS A NZ 1 ATOM 3608 N N . SER A 1 460 ? 36.341 53.162 55.220 1.00 27.77 ? 501 SER A N 1 ATOM 3609 C CA . SER A 1 460 ? 35.496 53.886 54.279 1.00 27.97 ? 501 SER A CA 1 ATOM 3610 C C . SER A 1 460 ? 35.330 55.347 54.699 1.00 28.51 ? 501 SER A C 1 ATOM 3611 O O . SER A 1 460 ? 34.245 55.769 55.086 1.00 26.97 ? 501 SER A O 1 ATOM 3612 C CB . SER A 1 460 ? 34.117 53.214 54.186 1.00 27.78 ? 501 SER A CB 1 ATOM 3613 O OG . SER A 1 460 ? 33.461 53.694 53.036 1.00 29.97 ? 501 SER A OG 1 ATOM 3614 N N . PRO A 1 461 ? 36.426 56.129 54.624 1.00 28.82 ? 502 PRO A N 1 ATOM 3615 C CA . PRO A 1 461 ? 36.353 57.505 55.113 1.00 29.93 ? 502 PRO A CA 1 ATOM 3616 C C . PRO A 1 461 ? 35.439 58.350 54.257 1.00 30.53 ? 502 PRO A C 1 ATOM 3617 O O . PRO A 1 461 ? 35.357 58.172 53.042 1.00 29.80 ? 502 PRO A O 1 ATOM 3618 C CB . PRO A 1 461 ? 37.810 58.008 55.008 1.00 30.48 ? 502 PRO A CB 1 ATOM 3619 C CG . PRO A 1 461 ? 38.479 57.064 54.033 1.00 30.85 ? 502 PRO A CG 1 ATOM 3620 C CD . PRO A 1 461 ? 37.792 55.733 54.214 1.00 29.79 ? 502 PRO A CD 1 ATOM 3621 N N . SER A 1 462 ? 34.768 59.274 54.914 1.00 31.72 ? 503 SER A N 1 ATOM 3622 C CA . SER A 1 462 ? 33.984 60.281 54.231 1.00 35.69 ? 503 SER A CA 1 ATOM 3623 C C . SER A 1 462 ? 34.867 61.079 53.282 1.00 38.09 ? 503 SER A C 1 ATOM 3624 O O . SER A 1 462 ? 35.980 61.460 53.654 1.00 39.35 ? 503 SER A O 1 ATOM 3625 C CB . SER A 1 462 ? 33.403 61.237 55.266 1.00 34.88 ? 503 SER A CB 1 ATOM 3626 O OG . SER A 1 462 ? 33.002 62.418 54.623 1.00 39.22 ? 503 SER A OG 1 ATOM 3627 N N . PRO A 1 463 ? 34.382 61.341 52.065 1.00 40.11 ? 504 PRO A N 1 ATOM 3628 C CA . PRO A 1 463 ? 35.134 62.209 51.161 1.00 42.45 ? 504 PRO A CA 1 ATOM 3629 C C . PRO A 1 463 ? 35.159 63.664 51.652 1.00 44.97 ? 504 PRO A C 1 ATOM 3630 O O . PRO A 1 463 ? 36.099 64.405 51.336 1.00 45.99 ? 504 PRO A O 1 ATOM 3631 C CB . PRO A 1 463 ? 34.371 62.089 49.838 1.00 41.81 ? 504 PRO A CB 1 ATOM 3632 C CG . PRO A 1 463 ? 32.985 61.644 50.230 1.00 40.82 ? 504 PRO A CG 1 ATOM 3633 C CD . PRO A 1 463 ? 33.158 60.803 51.439 1.00 39.97 ? 504 PRO A CD 1 ATOM 3634 N N . GLU A 1 464 ? 34.170 64.071 52.446 1.00 46.56 ? 505 GLU A N 1 ATOM 3635 C CA . GLU A 1 464 ? 34.125 65.472 52.879 1.00 48.18 ? 505 GLU A CA 1 ATOM 3636 C C . GLU A 1 464 ? 34.754 65.727 54.249 1.00 48.66 ? 505 GLU A C 1 ATOM 3637 O O . GLU A 1 464 ? 35.276 66.819 54.484 1.00 49.70 ? 505 GLU A O 1 ATOM 3638 C CB . GLU A 1 464 ? 32.705 66.053 52.820 1.00 48.34 ? 505 GLU A CB 1 ATOM 3639 C CG . GLU A 1 464 ? 32.027 66.009 51.428 1.00 51.65 ? 505 GLU A CG 1 ATOM 3640 C CD . GLU A 1 464 ? 31.005 64.889 51.305 1.00 54.92 ? 505 GLU A CD 1 ATOM 3641 O OE1 . GLU A 1 464 ? 30.596 64.544 50.165 1.00 56.81 ? 505 GLU A OE1 1 ATOM 3642 O OE2 . GLU A 1 464 ? 30.598 64.358 52.364 1.00 56.98 ? 505 GLU A OE2 1 ATOM 3643 N N . PHE A 1 465 ? 34.715 64.749 55.153 1.00 47.67 ? 506 PHE A N 1 ATOM 3644 C CA . PHE A 1 465 ? 35.041 65.054 56.545 1.00 48.29 ? 506 PHE A CA 1 ATOM 3645 C C . PHE A 1 465 ? 35.982 64.066 57.179 1.00 47.61 ? 506 PHE A C 1 ATOM 3646 O O . PHE A 1 465 ? 35.781 62.846 57.128 1.00 46.68 ? 506 PHE A O 1 ATOM 3647 C CB . PHE A 1 465 ? 33.773 65.199 57.394 1.00 49.00 ? 506 PHE A CB 1 ATOM 3648 C CG . PHE A 1 465 ? 32.824 66.288 56.918 1.00 50.89 ? 506 PHE A CG 1 ATOM 3649 C CD1 . PHE A 1 465 ? 31.691 65.966 56.163 1.00 52.06 ? 506 PHE A CD1 1 ATOM 3650 C CD2 . PHE A 1 465 ? 33.056 67.629 57.246 1.00 53.02 ? 506 PHE A CD2 1 ATOM 3651 C CE1 . PHE A 1 465 ? 30.800 66.967 55.734 1.00 52.28 ? 506 PHE A CE1 1 ATOM 3652 C CE2 . PHE A 1 465 ? 32.184 68.632 56.816 1.00 53.80 ? 506 PHE A CE2 1 ATOM 3653 C CZ . PHE A 1 465 ? 31.047 68.300 56.058 1.00 53.40 ? 506 PHE A CZ 1 ATOM 3654 N N . SER A 1 466 ? 37.028 64.606 57.785 1.00 47.27 ? 507 SER A N 1 ATOM 3655 C CA . SER A 1 466 ? 38.011 63.780 58.455 1.00 46.39 ? 507 SER A CA 1 ATOM 3656 C C . SER A 1 466 ? 37.371 63.156 59.688 1.00 43.70 ? 507 SER A C 1 ATOM 3657 O O . SER A 1 466 ? 36.683 63.848 60.457 1.00 44.31 ? 507 SER A O 1 ATOM 3658 C CB . SER A 1 466 ? 39.236 64.624 58.848 1.00 47.74 ? 507 SER A CB 1 ATOM 3659 O OG . SER A 1 466 ? 40.094 64.793 57.721 1.00 50.70 ? 507 SER A OG 1 ATOM 3660 N N . GLY A 1 467 ? 37.575 61.850 59.859 1.00 40.06 ? 508 GLY A N 1 ATOM 3661 C CA . GLY A 1 467 ? 37.208 61.199 61.111 1.00 36.10 ? 508 GLY A CA 1 ATOM 3662 C C . GLY A 1 467 ? 35.765 60.763 61.109 1.00 33.45 ? 508 GLY A C 1 ATOM 3663 O O . GLY A 1 467 ? 35.243 60.350 62.159 1.00 32.61 ? 508 GLY A O 1 ATOM 3664 N N A MET A 1 468 ? 35.130 60.868 59.945 0.60 31.99 ? 509 MET A N 1 ATOM 3665 N N B MET A 1 468 ? 35.129 60.886 59.937 0.40 31.91 ? 509 MET A N 1 ATOM 3666 C CA A MET A 1 468 ? 33.770 60.350 59.744 0.60 30.80 ? 509 MET A CA 1 ATOM 3667 C CA B MET A 1 468 ? 33.735 60.469 59.677 0.40 30.48 ? 509 MET A CA 1 ATOM 3668 C C A MET A 1 468 ? 33.716 59.377 58.583 0.60 29.66 ? 509 MET A C 1 ATOM 3669 C C B MET A 1 468 ? 33.721 59.392 58.583 0.40 29.45 ? 509 MET A C 1 ATOM 3670 O O A MET A 1 468 ? 34.542 59.442 57.671 0.60 28.89 ? 509 MET A O 1 ATOM 3671 O O B MET A 1 468 ? 34.600 59.387 57.721 0.40 28.99 ? 509 MET A O 1 ATOM 3672 C CB A MET A 1 468 ? 32.783 61.475 59.478 0.60 30.73 ? 509 MET A CB 1 ATOM 3673 C CB B MET A 1 468 ? 32.899 61.664 59.193 0.40 30.24 ? 509 MET A CB 1 ATOM 3674 C CG A MET A 1 468 ? 32.572 62.336 60.687 0.60 34.58 ? 509 MET A CG 1 ATOM 3675 C CG B MET A 1 468 ? 33.066 62.933 60.036 0.40 32.61 ? 509 MET A CG 1 ATOM 3676 S SD A MET A 1 468 ? 31.643 63.750 60.187 0.60 39.56 ? 509 MET A SD 1 ATOM 3677 S SD B MET A 1 468 ? 32.252 62.811 61.637 0.40 36.33 ? 509 MET A SD 1 ATOM 3678 C CE A MET A 1 468 ? 31.494 64.603 61.763 0.60 38.45 ? 509 MET A CE 1 ATOM 3679 C CE B MET A 1 468 ? 30.555 63.078 61.153 0.40 36.55 ? 509 MET A CE 1 ATOM 3680 N N . PRO A 1 469 ? 32.727 58.476 58.610 1.00 27.96 ? 510 PRO A N 1 ATOM 3681 C CA . PRO A 1 469 ? 32.599 57.465 57.559 1.00 27.12 ? 510 PRO A CA 1 ATOM 3682 C C . PRO A 1 469 ? 31.743 57.945 56.398 1.00 26.90 ? 510 PRO A C 1 ATOM 3683 O O . PRO A 1 469 ? 30.957 58.890 56.548 1.00 26.52 ? 510 PRO A O 1 ATOM 3684 C CB . PRO A 1 469 ? 31.864 56.346 58.281 1.00 26.45 ? 510 PRO A CB 1 ATOM 3685 C CG . PRO A 1 469 ? 30.864 57.101 59.153 1.00 26.47 ? 510 PRO A CG 1 ATOM 3686 C CD . PRO A 1 469 ? 31.826 58.177 59.740 1.00 27.95 ? 510 PRO A CD 1 ATOM 3687 N N . ARG A 1 470 ? 31.869 57.278 55.256 1.00 25.28 ? 511 ARG A N 1 ATOM 3688 C CA . ARG A 1 470 ? 31.057 57.622 54.085 1.00 24.29 ? 511 ARG A CA 1 ATOM 3689 C C . ARG A 1 470 ? 29.640 57.145 54.300 1.00 22.92 ? 511 ARG A C 1 ATOM 3690 O O . ARG A 1 470 ? 29.416 55.974 54.653 1.00 23.11 ? 511 ARG A O 1 ATOM 3691 C CB . ARG A 1 470 ? 31.630 56.881 52.867 1.00 25.69 ? 511 ARG A CB 1 ATOM 3692 C CG . ARG A 1 470 ? 30.884 57.128 51.571 1.00 27.46 ? 511 ARG A CG 1 ATOM 3693 C CD . ARG A 1 470 ? 31.435 56.254 50.475 1.00 30.85 ? 511 ARG A CD 1 ATOM 3694 N NE . ARG A 1 470 ? 32.779 56.686 50.081 1.00 30.70 ? 511 ARG A NE 1 ATOM 3695 C CZ . ARG A 1 470 ? 33.023 57.600 49.143 1.00 36.30 ? 511 ARG A CZ 1 ATOM 3696 N NH1 . ARG A 1 470 ? 32.015 58.203 48.502 1.00 36.17 ? 511 ARG A NH1 1 ATOM 3697 N NH2 . ARG A 1 470 ? 34.283 57.922 48.848 1.00 38.61 ? 511 ARG A NH2 1 ATOM 3698 N N . ILE A 1 471 ? 28.675 58.035 54.081 1.00 21.48 ? 512 ILE A N 1 ATOM 3699 C CA . ILE A 1 471 ? 27.272 57.578 53.989 1.00 22.18 ? 512 ILE A CA 1 ATOM 3700 C C . ILE A 1 471 ? 26.741 58.181 52.701 1.00 21.97 ? 512 ILE A C 1 ATOM 3701 O O . ILE A 1 471 ? 26.909 59.402 52.488 1.00 23.36 ? 512 ILE A O 1 ATOM 3702 C CB . ILE A 1 471 ? 26.424 58.123 55.156 1.00 21.52 ? 512 ILE A CB 1 ATOM 3703 C CG1 . ILE A 1 471 ? 26.928 57.609 56.518 1.00 22.87 ? 512 ILE A CG1 1 ATOM 3704 C CG2 . ILE A 1 471 ? 24.904 57.756 54.968 1.00 22.40 ? 512 ILE A CG2 1 ATOM 3705 C CD1 . ILE A 1 471 ? 26.114 58.135 57.723 1.00 26.33 ? 512 ILE A CD1 1 ATOM 3706 N N . SER A 1 472 ? 26.160 57.338 51.846 1.00 21.81 ? 513 SER A N 1 ATOM 3707 C CA . SER A 1 472 ? 25.744 57.742 50.513 1.00 21.34 ? 513 SER A CA 1 ATOM 3708 C C . SER A 1 472 ? 24.255 58.123 50.521 1.00 20.45 ? 513 SER A C 1 ATOM 3709 O O . SER A 1 472 ? 23.493 57.732 51.402 1.00 19.94 ? 513 SER A O 1 ATOM 3710 C CB . SER A 1 472 ? 25.939 56.588 49.521 1.00 22.35 ? 513 SER A CB 1 ATOM 3711 O OG . SER A 1 472 ? 27.343 56.255 49.451 1.00 26.28 ? 513 SER A OG 1 ATOM 3712 N N . LYS A 1 473 ? 23.878 58.841 49.476 1.00 19.74 ? 514 LYS A N 1 ATOM 3713 C CA A LYS A 1 473 ? 22.474 59.144 49.172 0.50 19.47 ? 514 LYS A CA 1 ATOM 3714 C CA B LYS A 1 473 ? 22.465 59.138 49.284 0.50 17.64 ? 514 LYS A CA 1 ATOM 3715 C C . LYS A 1 473 ? 21.792 57.825 48.843 1.00 17.85 ? 514 LYS A C 1 ATOM 3716 O O . LYS A 1 473 ? 22.428 56.878 48.382 1.00 18.29 ? 514 LYS A O 1 ATOM 3717 C CB A LYS A 1 473 ? 22.374 60.062 47.935 0.50 20.65 ? 514 LYS A CB 1 ATOM 3718 C CB B LYS A 1 473 ? 22.293 60.247 48.243 0.50 17.68 ? 514 LYS A CB 1 ATOM 3719 C CG A LYS A 1 473 ? 23.288 61.273 47.950 0.50 23.28 ? 514 LYS A CG 1 ATOM 3720 C CG B LYS A 1 473 ? 22.724 59.809 46.839 0.50 11.48 ? 514 LYS A CG 1 ATOM 3721 C CD A LYS A 1 473 ? 23.022 62.220 46.750 0.50 25.08 ? 514 LYS A CD 1 ATOM 3722 C CD B LYS A 1 473 ? 22.444 60.925 45.830 0.50 15.15 ? 514 LYS A CD 1 ATOM 3723 C CE A LYS A 1 473 ? 23.516 61.661 45.431 0.50 24.64 ? 514 LYS A CE 1 ATOM 3724 C CE B LYS A 1 473 ? 23.277 62.187 46.008 0.50 17.00 ? 514 LYS A CE 1 ATOM 3725 N NZ A LYS A 1 473 ? 24.969 61.950 45.284 0.50 23.51 ? 514 LYS A NZ 1 ATOM 3726 N NZ B LYS A 1 473 ? 24.713 61.869 46.156 0.50 17.96 ? 514 LYS A NZ 1 ATOM 3727 N N . LEU A 1 474 ? 20.477 57.768 48.991 1.00 16.88 ? 515 LEU A N 1 ATOM 3728 C CA . LEU A 1 474 ? 19.742 56.625 48.501 1.00 17.34 ? 515 LEU A CA 1 ATOM 3729 C C . LEU A 1 474 ? 19.601 56.758 47.000 1.00 17.39 ? 515 LEU A C 1 ATOM 3730 O O . LEU A 1 474 ? 19.357 57.868 46.474 1.00 18.90 ? 515 LEU A O 1 ATOM 3731 C CB . LEU A 1 474 ? 18.327 56.605 49.077 1.00 15.35 ? 515 LEU A CB 1 ATOM 3732 C CG . LEU A 1 474 ? 18.237 56.149 50.546 1.00 15.05 ? 515 LEU A CG 1 ATOM 3733 C CD1 . LEU A 1 474 ? 16.893 56.536 51.186 1.00 17.96 ? 515 LEU A CD1 1 ATOM 3734 C CD2 . LEU A 1 474 ? 18.465 54.653 50.654 1.00 16.79 ? 515 LEU A CD2 1 ATOM 3735 N N . GLY A 1 475 ? 19.757 55.620 46.302 1.00 18.07 ? 516 GLY A N 1 ATOM 3736 C CA . GLY A 1 475 ? 19.444 55.535 44.897 1.00 17.24 ? 516 GLY A CA 1 ATOM 3737 C C . GLY A 1 475 ? 18.082 54.888 44.747 1.00 17.90 ? 516 GLY A C 1 ATOM 3738 O O . GLY A 1 475 ? 17.151 55.269 45.410 1.00 17.37 ? 516 GLY A O 1 ATOM 3739 N N . SER A 1 476 ? 17.981 53.860 43.898 1.00 16.10 ? 517 SER A N 1 ATOM 3740 C CA . SER A 1 476 ? 16.764 53.080 43.839 1.00 16.23 ? 517 SER A CA 1 ATOM 3741 C C . SER A 1 476 ? 17.068 51.640 43.435 1.00 15.72 ? 517 SER A C 1 ATOM 3742 O O . SER A 1 476 ? 18.223 51.159 43.641 1.00 15.68 ? 517 SER A O 1 ATOM 3743 C CB . SER A 1 476 ? 15.715 53.734 42.933 1.00 15.86 ? 517 SER A CB 1 ATOM 3744 O OG . SER A 1 476 ? 14.462 53.090 43.115 1.00 17.38 ? 517 SER A OG 1 ATOM 3745 N N . GLY A 1 477 ? 16.054 50.953 42.901 1.00 14.37 ? 518 GLY A N 1 ATOM 3746 C CA . GLY A 1 477 ? 16.177 49.528 42.639 1.00 14.82 ? 518 GLY A CA 1 ATOM 3747 C C . GLY A 1 477 ? 15.996 48.695 43.914 1.00 14.25 ? 518 GLY A C 1 ATOM 3748 O O . GLY A 1 477 ? 16.490 47.564 44.002 1.00 14.90 ? 518 GLY A O 1 ATOM 3749 N N . ASN A 1 478 ? 15.260 49.231 44.899 1.00 13.25 ? 519 ASN A N 1 ATOM 3750 C CA . ASN A 1 478 ? 14.860 48.412 46.057 1.00 14.31 ? 519 ASN A CA 1 ATOM 3751 C C . ASN A 1 478 ? 13.619 48.988 46.690 1.00 14.47 ? 519 ASN A C 1 ATOM 3752 O O . ASN A 1 478 ? 13.152 50.080 46.291 1.00 13.50 ? 519 ASN A O 1 ATOM 3753 C CB . ASN A 1 478 ? 16.019 48.197 47.056 1.00 14.09 ? 519 ASN A CB 1 ATOM 3754 C CG . ASN A 1 478 ? 16.031 46.772 47.550 1.00 15.81 ? 519 ASN A CG 1 ATOM 3755 O OD1 . ASN A 1 478 ? 15.080 46.325 48.188 1.00 15.46 ? 519 ASN A OD1 1 ATOM 3756 N ND2 . ASN A 1 478 ? 17.066 46.003 47.143 1.00 14.63 ? 519 ASN A ND2 1 ATOM 3757 N N . ASP A 1 479 ? 13.104 48.318 47.723 1.00 12.88 ? 520 ASP A N 1 ATOM 3758 C CA . ASP A 1 479 ? 11.700 48.527 48.158 1.00 14.07 ? 520 ASP A CA 1 ATOM 3759 C C . ASP A 1 479 ? 11.472 49.823 48.928 1.00 13.76 ? 520 ASP A C 1 ATOM 3760 O O . ASP A 1 479 ? 10.312 50.214 49.169 1.00 14.20 ? 520 ASP A O 1 ATOM 3761 C CB . ASP A 1 479 ? 11.231 47.358 49.026 1.00 14.81 ? 520 ASP A CB 1 ATOM 3762 C CG . ASP A 1 479 ? 10.852 46.135 48.199 1.00 16.87 ? 520 ASP A CG 1 ATOM 3763 O OD1 . ASP A 1 479 ? 10.168 46.337 47.181 1.00 14.66 ? 520 ASP A OD1 1 ATOM 3764 O OD2 . ASP A 1 479 ? 11.284 45.009 48.563 1.00 16.44 ? 520 ASP A OD2 1 ATOM 3765 N N . PHE A 1 480 ? 12.536 50.549 49.240 1.00 13.38 ? 521 PHE A N 1 ATOM 3766 C CA . PHE A 1 480 ? 12.324 51.872 49.856 1.00 12.70 ? 521 PHE A CA 1 ATOM 3767 C C . PHE A 1 480 ? 11.834 52.936 48.893 1.00 13.38 ? 521 PHE A C 1 ATOM 3768 O O . PHE A 1 480 ? 11.452 54.022 49.324 1.00 14.04 ? 521 PHE A O 1 ATOM 3769 C CB . PHE A 1 480 ? 13.636 52.388 50.510 1.00 14.62 ? 521 PHE A CB 1 ATOM 3770 C CG . PHE A 1 480 ? 14.786 52.469 49.528 1.00 12.64 ? 521 PHE A CG 1 ATOM 3771 C CD1 . PHE A 1 480 ? 14.915 53.588 48.656 1.00 15.06 ? 521 PHE A CD1 1 ATOM 3772 C CD2 . PHE A 1 480 ? 15.736 51.424 49.448 1.00 13.79 ? 521 PHE A CD2 1 ATOM 3773 C CE1 . PHE A 1 480 ? 16.001 53.596 47.720 1.00 15.22 ? 521 PHE A CE1 1 ATOM 3774 C CE2 . PHE A 1 480 ? 16.808 51.482 48.545 1.00 14.95 ? 521 PHE A CE2 1 ATOM 3775 C CZ . PHE A 1 480 ? 16.919 52.550 47.661 1.00 15.66 ? 521 PHE A CZ 1 ATOM 3776 N N . GLU A 1 481 ? 11.862 52.654 47.579 1.00 12.50 ? 522 GLU A N 1 ATOM 3777 C CA . GLU A 1 481 ? 11.582 53.704 46.560 1.00 13.72 ? 522 GLU A CA 1 ATOM 3778 C C . GLU A 1 481 ? 10.222 54.350 46.796 1.00 12.65 ? 522 GLU A C 1 ATOM 3779 O O . GLU A 1 481 ? 10.116 55.589 46.747 1.00 14.00 ? 522 GLU A O 1 ATOM 3780 C CB . GLU A 1 481 ? 11.633 53.112 45.146 1.00 13.76 ? 522 GLU A CB 1 ATOM 3781 C CG . GLU A 1 481 ? 11.603 54.224 44.051 1.00 12.78 ? 522 GLU A CG 1 ATOM 3782 C CD . GLU A 1 481 ? 11.473 53.610 42.645 1.00 14.75 ? 522 GLU A CD 1 ATOM 3783 O OE1 . GLU A 1 481 ? 10.417 52.954 42.420 1.00 16.16 ? 522 GLU A OE1 1 ATOM 3784 O OE2 . GLU A 1 481 ? 12.408 53.835 41.799 1.00 16.73 ? 522 GLU A OE2 1 ATOM 3785 N N . VAL A 1 482 ? 9.160 53.551 47.011 1.00 11.40 ? 523 VAL A N 1 ATOM 3786 C CA . VAL A 1 482 ? 7.832 54.185 47.177 1.00 12.43 ? 523 VAL A CA 1 ATOM 3787 C C . VAL A 1 482 ? 7.829 55.057 48.448 1.00 13.12 ? 523 VAL A C 1 ATOM 3788 O O . VAL A 1 482 ? 7.235 56.147 48.451 1.00 14.27 ? 523 VAL A O 1 ATOM 3789 C CB . VAL A 1 482 ? 6.730 53.156 47.142 1.00 12.80 ? 523 VAL A CB 1 ATOM 3790 C CG1 . VAL A 1 482 ? 6.741 52.212 48.400 1.00 12.89 ? 523 VAL A CG1 1 ATOM 3791 C CG2 . VAL A 1 482 ? 5.395 53.841 46.998 1.00 13.96 ? 523 VAL A CG2 1 ATOM 3792 N N . PHE A 1 483 ? 8.460 54.557 49.515 1.00 13.40 ? 524 PHE A N 1 ATOM 3793 C CA . PHE A 1 483 ? 8.413 55.275 50.794 1.00 13.03 ? 524 PHE A CA 1 ATOM 3794 C C . PHE A 1 483 ? 9.178 56.573 50.716 1.00 13.72 ? 524 PHE A C 1 ATOM 3795 O O . PHE A 1 483 ? 8.708 57.584 51.266 1.00 15.26 ? 524 PHE A O 1 ATOM 3796 C CB . PHE A 1 483 ? 8.966 54.372 51.879 1.00 14.43 ? 524 PHE A CB 1 ATOM 3797 C CG . PHE A 1 483 ? 8.125 53.131 52.040 1.00 13.22 ? 524 PHE A CG 1 ATOM 3798 C CD1 . PHE A 1 483 ? 6.899 53.184 52.747 1.00 15.87 ? 524 PHE A CD1 1 ATOM 3799 C CD2 . PHE A 1 483 ? 8.519 51.936 51.447 1.00 14.22 ? 524 PHE A CD2 1 ATOM 3800 C CE1 . PHE A 1 483 ? 6.123 52.013 52.909 1.00 17.25 ? 524 PHE A CE1 1 ATOM 3801 C CE2 . PHE A 1 483 ? 7.763 50.777 51.591 1.00 15.47 ? 524 PHE A CE2 1 ATOM 3802 C CZ . PHE A 1 483 ? 6.540 50.808 52.296 1.00 16.03 ? 524 PHE A CZ 1 ATOM 3803 N N . PHE A 1 484 ? 10.327 56.557 50.061 1.00 13.40 ? 525 PHE A N 1 ATOM 3804 C CA . PHE A 1 484 ? 11.215 57.736 50.108 1.00 12.62 ? 525 PHE A CA 1 ATOM 3805 C C . PHE A 1 484 ? 10.862 58.693 48.949 1.00 13.88 ? 525 PHE A C 1 ATOM 3806 O O . PHE A 1 484 ? 10.389 59.826 49.183 1.00 14.81 ? 525 PHE A O 1 ATOM 3807 C CB . PHE A 1 484 ? 12.664 57.280 49.987 1.00 13.35 ? 525 PHE A CB 1 ATOM 3808 C CG . PHE A 1 484 ? 13.638 58.382 50.215 1.00 13.89 ? 525 PHE A CG 1 ATOM 3809 C CD1 . PHE A 1 484 ? 13.618 59.080 51.479 1.00 13.82 ? 525 PHE A CD1 1 ATOM 3810 C CD2 . PHE A 1 484 ? 14.574 58.715 49.239 1.00 17.75 ? 525 PHE A CD2 1 ATOM 3811 C CE1 . PHE A 1 484 ? 14.535 60.124 51.729 1.00 14.20 ? 525 PHE A CE1 1 ATOM 3812 C CE2 . PHE A 1 484 ? 15.530 59.753 49.483 1.00 16.22 ? 525 PHE A CE2 1 ATOM 3813 C CZ . PHE A 1 484 ? 15.491 60.439 50.722 1.00 13.81 ? 525 PHE A CZ 1 ATOM 3814 N N . GLN A 1 485 ? 11.066 58.252 47.703 1.00 12.95 ? 526 GLN A N 1 ATOM 3815 C CA . GLN A 1 485 ? 10.883 59.211 46.592 1.00 12.39 ? 526 GLN A CA 1 ATOM 3816 C C . GLN A 1 485 ? 9.411 59.481 46.232 1.00 11.98 ? 526 GLN A C 1 ATOM 3817 O O . GLN A 1 485 ? 9.151 60.531 45.586 1.00 14.19 ? 526 GLN A O 1 ATOM 3818 C CB . GLN A 1 485 ? 11.662 58.766 45.349 1.00 13.24 ? 526 GLN A CB 1 ATOM 3819 C CG . GLN A 1 485 ? 13.247 58.876 45.495 1.00 14.91 ? 526 GLN A CG 1 ATOM 3820 C CD . GLN A 1 485 ? 13.853 57.549 45.845 1.00 18.02 ? 526 GLN A CD 1 ATOM 3821 O OE1 . GLN A 1 485 ? 13.190 56.667 46.429 1.00 17.22 ? 526 GLN A OE1 1 ATOM 3822 N NE2 . GLN A 1 485 ? 15.201 57.431 45.623 1.00 16.80 ? 526 GLN A NE2 1 ATOM 3823 N N . ARG A 1 486 ? 8.491 58.550 46.535 1.00 11.92 ? 527 ARG A N 1 ATOM 3824 C CA . ARG A 1 486 ? 7.077 58.930 46.267 1.00 12.05 ? 527 ARG A CA 1 ATOM 3825 C C . ARG A 1 486 ? 6.471 59.607 47.482 1.00 12.76 ? 527 ARG A C 1 ATOM 3826 O O . ARG A 1 486 ? 5.877 60.691 47.344 1.00 13.93 ? 527 ARG A O 1 ATOM 3827 C CB . ARG A 1 486 ? 6.198 57.742 45.776 1.00 13.15 ? 527 ARG A CB 1 ATOM 3828 C CG . ARG A 1 486 ? 4.862 58.260 45.255 1.00 12.41 ? 527 ARG A CG 1 ATOM 3829 C CD . ARG A 1 486 ? 3.786 57.167 45.148 1.00 14.59 ? 527 ARG A CD 1 ATOM 3830 N NE . ARG A 1 486 ? 4.081 56.109 44.144 1.00 13.57 ? 527 ARG A NE 1 ATOM 3831 C CZ . ARG A 1 486 ? 3.122 55.379 43.548 1.00 13.95 ? 527 ARG A CZ 1 ATOM 3832 N NH1 . ARG A 1 486 ? 1.814 55.600 43.805 1.00 14.46 ? 527 ARG A NH1 1 ATOM 3833 N NH2 . ARG A 1 486 ? 3.500 54.406 42.727 1.00 12.67 ? 527 ARG A NH2 1 ATOM 3834 N N . LEU A 1 487 ? 6.543 58.968 48.646 1.00 12.74 ? 528 LEU A N 1 ATOM 3835 C CA . LEU A 1 487 ? 5.835 59.476 49.798 1.00 14.54 ? 528 LEU A CA 1 ATOM 3836 C C . LEU A 1 487 ? 6.620 60.415 50.733 1.00 14.80 ? 528 LEU A C 1 ATOM 3837 O O . LEU A 1 487 ? 5.980 61.084 51.542 1.00 15.58 ? 528 LEU A O 1 ATOM 3838 C CB . LEU A 1 487 ? 5.275 58.300 50.629 1.00 13.23 ? 528 LEU A CB 1 ATOM 3839 C CG . LEU A 1 487 ? 4.282 57.371 49.868 1.00 15.43 ? 528 LEU A CG 1 ATOM 3840 C CD1 . LEU A 1 487 ? 3.869 56.171 50.754 1.00 17.62 ? 528 LEU A CD1 1 ATOM 3841 C CD2 . LEU A 1 487 ? 2.965 58.129 49.387 1.00 15.99 ? 528 LEU A CD2 1 ATOM 3842 N N . GLY A 1 488 ? 7.954 60.475 50.624 1.00 13.21 ? 529 GLY A N 1 ATOM 3843 C CA . GLY A 1 488 ? 8.688 61.411 51.483 1.00 13.36 ? 529 GLY A CA 1 ATOM 3844 C C . GLY A 1 488 ? 8.760 60.972 52.925 1.00 12.18 ? 529 GLY A C 1 ATOM 3845 O O . GLY A 1 488 ? 8.767 61.860 53.799 1.00 13.23 ? 529 GLY A O 1 ATOM 3846 N N . ILE A 1 489 ? 8.982 59.669 53.149 1.00 12.97 ? 530 ILE A N 1 ATOM 3847 C CA . ILE A 1 489 ? 9.199 59.149 54.516 1.00 12.51 ? 530 ILE A CA 1 ATOM 3848 C C . ILE A 1 489 ? 10.717 58.893 54.625 1.00 13.94 ? 530 ILE A C 1 ATOM 3849 O O . ILE A 1 489 ? 11.306 58.248 53.762 1.00 13.91 ? 530 ILE A O 1 ATOM 3850 C CB . ILE A 1 489 ? 8.421 57.849 54.674 1.00 13.41 ? 530 ILE A CB 1 ATOM 3851 C CG1 . ILE A 1 489 ? 6.919 58.193 54.674 1.00 13.11 ? 530 ILE A CG1 1 ATOM 3852 C CG2 . ILE A 1 489 ? 8.805 57.185 56.000 1.00 14.01 ? 530 ILE A CG2 1 ATOM 3853 C CD1 . ILE A 1 489 ? 6.067 56.913 54.461 1.00 15.21 ? 530 ILE A CD1 1 ATOM 3854 N N . ALA A 1 490 ? 11.307 59.437 55.692 1.00 13.92 ? 531 ALA A N 1 ATOM 3855 C CA . ALA A 1 490 ? 12.752 59.296 55.942 1.00 13.47 ? 531 ALA A CA 1 ATOM 3856 C C . ALA A 1 490 ? 13.118 57.834 55.807 1.00 14.50 ? 531 ALA A C 1 ATOM 3857 O O . ALA A 1 490 ? 12.509 56.990 56.487 1.00 14.77 ? 531 ALA A O 1 ATOM 3858 C CB . ALA A 1 490 ? 13.076 59.750 57.407 1.00 15.49 ? 531 ALA A CB 1 ATOM 3859 N N . SER A 1 491 ? 14.125 57.496 54.977 1.00 13.75 ? 532 SER A N 1 ATOM 3860 C CA . SER A 1 491 ? 14.430 56.080 54.734 1.00 12.90 ? 532 SER A CA 1 ATOM 3861 C C . SER A 1 491 ? 15.950 55.825 54.817 1.00 14.70 ? 532 SER A C 1 ATOM 3862 O O . SER A 1 491 ? 16.787 56.745 54.605 1.00 14.78 ? 532 SER A O 1 ATOM 3863 C CB . SER A 1 491 ? 13.918 55.686 53.321 1.00 13.86 ? 532 SER A CB 1 ATOM 3864 O OG . SER A 1 491 ? 12.505 55.760 53.223 1.00 14.75 ? 532 SER A OG 1 ATOM 3865 N N . GLY A 1 492 ? 16.298 54.567 55.082 1.00 14.39 ? 533 GLY A N 1 ATOM 3866 C CA . GLY A 1 492 ? 17.730 54.174 55.116 1.00 14.29 ? 533 GLY A CA 1 ATOM 3867 C C . GLY A 1 492 ? 17.919 52.685 54.833 1.00 14.95 ? 533 GLY A C 1 ATOM 3868 O O . GLY A 1 492 ? 16.963 51.908 54.854 1.00 16.52 ? 533 GLY A O 1 ATOM 3869 N N . ARG A 1 493 ? 19.176 52.317 54.577 1.00 15.32 ? 534 ARG A N 1 ATOM 3870 C CA . ARG A 1 493 ? 19.514 50.899 54.336 1.00 14.27 ? 534 ARG A CA 1 ATOM 3871 C C . ARG A 1 493 ? 20.975 50.730 54.730 1.00 15.94 ? 534 ARG A C 1 ATOM 3872 O O . ARG A 1 493 ? 21.739 51.714 54.768 1.00 16.11 ? 534 ARG A O 1 ATOM 3873 C CB . ARG A 1 493 ? 19.357 50.543 52.840 1.00 15.01 ? 534 ARG A CB 1 ATOM 3874 C CG . ARG A 1 493 ? 20.357 51.274 51.943 1.00 15.16 ? 534 ARG A CG 1 ATOM 3875 C CD . ARG A 1 493 ? 20.020 51.128 50.433 1.00 15.98 ? 534 ARG A CD 1 ATOM 3876 N NE . ARG A 1 493 ? 19.842 49.707 50.016 1.00 16.12 ? 534 ARG A NE 1 ATOM 3877 C CZ . ARG A 1 493 ? 19.837 49.324 48.734 1.00 18.33 ? 534 ARG A CZ 1 ATOM 3878 N NH1 . ARG A 1 493 ? 19.981 50.216 47.750 1.00 18.22 ? 534 ARG A NH1 1 ATOM 3879 N NH2 . ARG A 1 493 ? 19.631 48.032 48.419 1.00 17.21 ? 534 ARG A NH2 1 ATOM 3880 N N . ALA A 1 494 ? 21.335 49.492 55.090 1.00 15.47 ? 535 ALA A N 1 ATOM 3881 C CA . ALA A 1 494 ? 22.729 49.206 55.530 1.00 15.33 ? 535 ALA A CA 1 ATOM 3882 C C . ALA A 1 494 ? 23.040 47.744 55.280 1.00 16.42 ? 535 ALA A C 1 ATOM 3883 O O . ALA A 1 494 ? 22.167 46.867 55.466 1.00 16.73 ? 535 ALA A O 1 ATOM 3884 C CB . ALA A 1 494 ? 22.845 49.508 57.030 1.00 15.79 ? 535 ALA A CB 1 ATOM 3885 N N . ARG A 1 495 ? 24.296 47.490 54.916 1.00 16.83 ? 536 ARG A N 1 ATOM 3886 C CA . ARG A 1 495 ? 24.724 46.112 54.682 1.00 17.19 ? 536 ARG A CA 1 ATOM 3887 C C . ARG A 1 495 ? 26.227 46.076 54.757 1.00 18.34 ? 536 ARG A C 1 ATOM 3888 O O . ARG A 1 495 ? 26.867 47.119 54.755 1.00 18.80 ? 536 ARG A O 1 ATOM 3889 C CB . ARG A 1 495 ? 24.268 45.626 53.282 1.00 17.50 ? 536 ARG A CB 1 ATOM 3890 C CG . ARG A 1 495 ? 24.897 46.416 52.052 1.00 17.04 ? 536 ARG A CG 1 ATOM 3891 C CD . ARG A 1 495 ? 24.575 45.744 50.712 1.00 20.38 ? 536 ARG A CD 1 ATOM 3892 N NE . ARG A 1 495 ? 23.123 45.554 50.560 1.00 20.00 ? 536 ARG A NE 1 ATOM 3893 C CZ . ARG A 1 495 ? 22.505 45.459 49.388 1.00 19.70 ? 536 ARG A CZ 1 ATOM 3894 N NH1 . ARG A 1 495 ? 23.190 45.552 48.258 1.00 22.45 ? 536 ARG A NH1 1 ATOM 3895 N NH2 . ARG A 1 495 ? 21.172 45.255 49.341 1.00 18.89 ? 536 ARG A NH2 1 ATOM 3896 N N . TYR A 1 496 ? 26.776 44.877 54.820 1.00 18.73 ? 537 TYR A N 1 ATOM 3897 C CA . TYR A 1 496 ? 28.226 44.727 54.672 1.00 19.93 ? 537 TYR A CA 1 ATOM 3898 C C . TYR A 1 496 ? 28.613 44.670 53.200 1.00 21.12 ? 537 TYR A C 1 ATOM 3899 O O . TYR A 1 496 ? 27.863 44.136 52.366 1.00 20.39 ? 537 TYR A O 1 ATOM 3900 C CB . TYR A 1 496 ? 28.761 43.521 55.483 1.00 19.78 ? 537 TYR A CB 1 ATOM 3901 C CG . TYR A 1 496 ? 29.696 43.996 56.582 1.00 20.16 ? 537 TYR A CG 1 ATOM 3902 C CD1 . TYR A 1 496 ? 29.189 44.693 57.685 1.00 19.36 ? 537 TYR A CD1 1 ATOM 3903 C CD2 . TYR A 1 496 ? 31.079 43.778 56.501 1.00 21.76 ? 537 TYR A CD2 1 ATOM 3904 C CE1 . TYR A 1 496 ? 30.009 45.176 58.694 1.00 20.63 ? 537 TYR A CE1 1 ATOM 3905 C CE2 . TYR A 1 496 ? 31.934 44.271 57.515 1.00 21.63 ? 537 TYR A CE2 1 ATOM 3906 C CZ . TYR A 1 496 ? 31.380 44.954 58.597 1.00 20.53 ? 537 TYR A CZ 1 ATOM 3907 O OH . TYR A 1 496 ? 32.200 45.455 59.578 1.00 23.81 ? 537 TYR A OH 1 ATOM 3908 N N . THR A 1 497 ? 29.759 45.264 52.874 1.00 20.52 ? 538 THR A N 1 ATOM 3909 C CA . THR A 1 497 ? 30.151 45.411 51.475 1.00 21.23 ? 538 THR A CA 1 ATOM 3910 C C . THR A 1 497 ? 31.635 45.057 51.265 1.00 22.85 ? 538 THR A C 1 ATOM 3911 O O . THR A 1 497 ? 32.327 44.761 52.229 1.00 22.20 ? 538 THR A O 1 ATOM 3912 C CB . THR A 1 497 ? 29.833 46.878 50.981 1.00 21.68 ? 538 THR A CB 1 ATOM 3913 O OG1 . THR A 1 497 ? 29.936 46.919 49.544 1.00 22.23 ? 538 THR A OG1 1 ATOM 3914 C CG2 . THR A 1 497 ? 30.774 47.895 51.607 1.00 21.46 ? 538 THR A CG2 1 ATOM 3915 N N . LYS A 1 498 ? 32.069 45.086 50.002 1.00 23.76 ? 539 LYS A N 1 ATOM 3916 C CA . LYS A 1 498 ? 33.455 44.780 49.610 1.00 25.96 ? 539 LYS A CA 1 ATOM 3917 C C . LYS A 1 498 ? 34.297 46.038 49.707 1.00 27.15 ? 539 LYS A C 1 ATOM 3918 O O . LYS A 1 498 ? 33.804 47.126 50.013 1.00 26.03 ? 539 LYS A O 1 ATOM 3919 C CB . LYS A 1 498 ? 33.467 44.279 48.155 1.00 26.76 ? 539 LYS A CB 1 ATOM 3920 C CG . LYS A 1 498 ? 32.922 45.339 47.228 1.00 31.12 ? 539 LYS A CG 1 ATOM 3921 C CD . LYS A 1 498 ? 32.840 44.906 45.794 1.00 40.36 ? 539 LYS A CD 1 ATOM 3922 C CE . LYS A 1 498 ? 31.875 45.824 45.043 1.00 43.61 ? 539 LYS A CE 1 ATOM 3923 N NZ . LYS A 1 498 ? 31.943 45.597 43.575 1.00 49.36 ? 539 LYS A NZ 1 ATOM 3924 N N . ASN A 1 499 ? 35.595 45.869 49.468 1.00 29.10 ? 540 ASN A N 1 ATOM 3925 C CA . ASN A 1 499 ? 36.506 46.990 49.389 1.00 32.61 ? 540 ASN A CA 1 ATOM 3926 C C . ASN A 1 499 ? 36.405 47.549 47.992 1.00 35.08 ? 540 ASN A C 1 ATOM 3927 O O . ASN A 1 499 ? 36.839 46.917 47.030 1.00 35.79 ? 540 ASN A O 1 ATOM 3928 C CB . ASN A 1 499 ? 37.944 46.508 49.635 1.00 33.03 ? 540 ASN A CB 1 ATOM 3929 C CG . ASN A 1 499 ? 38.950 47.651 49.607 1.00 33.50 ? 540 ASN A CG 1 ATOM 3930 O OD1 . ASN A 1 499 ? 38.664 48.760 49.107 1.00 34.88 ? 540 ASN A OD1 1 ATOM 3931 N ND2 . ASN A 1 499 ? 40.138 47.396 50.173 1.00 35.88 ? 540 ASN A ND2 1 ATOM 3932 N N . TRP A 1 500 ? 35.837 48.732 47.879 1.00 38.22 ? 541 TRP A N 1 ATOM 3933 C CA . TRP A 1 500 ? 35.587 49.336 46.583 1.00 42.42 ? 541 TRP A CA 1 ATOM 3934 C C . TRP A 1 500 ? 36.897 49.706 45.863 1.00 45.79 ? 541 TRP A C 1 ATOM 3935 O O . TRP A 1 500 ? 36.929 49.757 44.629 1.00 46.74 ? 541 TRP A O 1 ATOM 3936 C CB . TRP A 1 500 ? 34.672 50.550 46.758 1.00 42.38 ? 541 TRP A CB 1 ATOM 3937 C CG . TRP A 1 500 ? 33.237 50.133 47.039 1.00 43.14 ? 541 TRP A CG 1 ATOM 3938 C CD1 . TRP A 1 500 ? 32.796 49.174 47.945 1.00 43.14 ? 541 TRP A CD1 1 ATOM 3939 C CD2 . TRP A 1 500 ? 32.068 50.651 46.418 1.00 44.31 ? 541 TRP A CD2 1 ATOM 3940 N NE1 . TRP A 1 500 ? 31.425 49.066 47.896 1.00 39.63 ? 541 TRP A NE1 1 ATOM 3941 C CE2 . TRP A 1 500 ? 30.952 49.960 46.969 1.00 43.34 ? 541 TRP A CE2 1 ATOM 3942 C CE3 . TRP A 1 500 ? 31.846 51.640 45.437 1.00 46.23 ? 541 TRP A CE3 1 ATOM 3943 C CZ2 . TRP A 1 500 ? 29.637 50.239 46.582 1.00 44.91 ? 541 TRP A CZ2 1 ATOM 3944 C CZ3 . TRP A 1 500 ? 30.545 51.906 45.044 1.00 45.83 ? 541 TRP A CZ3 1 ATOM 3945 C CH2 . TRP A 1 500 ? 29.455 51.202 45.612 1.00 46.32 ? 541 TRP A CH2 1 ATOM 3946 N N . GLU A 1 501 ? 37.965 49.913 46.635 1.00 48.82 ? 542 GLU A N 1 ATOM 3947 C CA . GLU A 1 501 ? 39.271 50.311 46.099 1.00 52.30 ? 542 GLU A CA 1 ATOM 3948 C C . GLU A 1 501 ? 39.908 49.190 45.303 1.00 53.37 ? 542 GLU A C 1 ATOM 3949 O O . GLU A 1 501 ? 40.418 49.401 44.205 1.00 54.41 ? 542 GLU A O 1 ATOM 3950 C CB . GLU A 1 501 ? 40.239 50.691 47.227 1.00 53.37 ? 542 GLU A CB 1 ATOM 3951 C CG . GLU A 1 501 ? 39.694 51.694 48.228 1.00 57.50 ? 542 GLU A CG 1 ATOM 3952 C CD . GLU A 1 501 ? 39.689 53.103 47.682 1.00 63.33 ? 542 GLU A CD 1 ATOM 3953 O OE1 . GLU A 1 501 ? 40.796 53.666 47.498 1.00 66.42 ? 542 GLU A OE1 1 ATOM 3954 O OE2 . GLU A 1 501 ? 38.582 53.647 47.440 1.00 65.72 ? 542 GLU A OE2 1 ATOM 3955 N N . THR A 1 502 ? 39.893 47.996 45.872 1.00 54.14 ? 543 THR A N 1 ATOM 3956 C CA . THR A 1 502 ? 40.624 46.887 45.297 1.00 55.11 ? 543 THR A CA 1 ATOM 3957 C C . THR A 1 502 ? 39.744 46.024 44.414 1.00 55.27 ? 543 THR A C 1 ATOM 3958 O O . THR A 1 502 ? 40.243 45.141 43.717 1.00 54.93 ? 543 THR A O 1 ATOM 3959 C CB . THR A 1 502 ? 41.274 46.038 46.402 1.00 55.60 ? 543 THR A CB 1 ATOM 3960 O OG1 . THR A 1 502 ? 40.253 45.484 47.242 1.00 55.78 ? 543 THR A OG1 1 ATOM 3961 C CG2 . THR A 1 502 ? 42.223 46.900 47.250 1.00 55.76 ? 543 THR A CG2 1 ATOM 3962 N N . ASN A 1 503 ? 38.433 46.284 44.439 1.00 55.83 ? 544 ASN A N 1 ATOM 3963 C CA . ASN A 1 503 ? 37.462 45.478 43.688 1.00 56.23 ? 544 ASN A CA 1 ATOM 3964 C C . ASN A 1 503 ? 36.736 46.271 42.606 1.00 56.38 ? 544 ASN A C 1 ATOM 3965 O O . ASN A 1 503 ? 35.912 47.135 42.910 1.00 56.58 ? 544 ASN A O 1 ATOM 3966 C CB . ASN A 1 503 ? 36.453 44.824 44.637 1.00 55.95 ? 544 ASN A CB 1 ATOM 3967 C CG . ASN A 1 503 ? 37.107 43.839 45.593 1.00 58.09 ? 544 ASN A CG 1 ATOM 3968 O OD1 . ASN A 1 503 ? 37.612 42.788 45.170 1.00 61.60 ? 544 ASN A OD1 1 ATOM 3969 N ND2 . ASN A 1 503 ? 37.103 44.167 46.891 1.00 57.81 ? 544 ASN A ND2 1 ATOM 3970 N N . LYS A 1 504 ? 37.047 45.947 41.354 1.00 56.45 ? 545 LYS A N 1 ATOM 3971 C CA . LYS A 1 504 ? 36.532 46.637 40.166 1.00 56.53 ? 545 LYS A CA 1 ATOM 3972 C C . LYS A 1 504 ? 35.221 46.016 39.591 1.00 55.22 ? 545 LYS A C 1 ATOM 3973 O O . LYS A 1 504 ? 34.562 46.598 38.709 1.00 55.87 ? 545 LYS A O 1 ATOM 3974 C CB . LYS A 1 504 ? 37.660 46.724 39.112 1.00 57.41 ? 545 LYS A CB 1 ATOM 3975 C CG . LYS A 1 504 ? 37.233 46.567 37.642 1.00 59.74 ? 545 LYS A CG 1 ATOM 3976 C CD . LYS A 1 504 ? 38.377 46.009 36.797 1.00 62.83 ? 545 LYS A CD 1 ATOM 3977 C CE . LYS A 1 504 ? 37.857 45.200 35.600 1.00 63.17 ? 545 LYS A CE 1 ATOM 3978 N NZ . LYS A 1 504 ? 38.795 44.082 35.219 1.00 63.17 ? 545 LYS A NZ 1 ATOM 3979 N N . PHE A 1 505 ? 34.837 44.849 40.098 1.00 53.25 ? 546 PHE A N 1 ATOM 3980 C CA . PHE A 1 505 ? 33.585 44.217 39.676 1.00 50.34 ? 546 PHE A CA 1 ATOM 3981 C C . PHE A 1 505 ? 32.328 44.936 40.208 1.00 48.75 ? 546 PHE A C 1 ATOM 3982 O O . PHE A 1 505 ? 32.397 45.741 41.144 1.00 48.29 ? 546 PHE A O 1 ATOM 3983 C CB . PHE A 1 505 ? 33.592 42.725 40.034 1.00 50.48 ? 546 PHE A CB 1 ATOM 3984 C CG . PHE A 1 505 ? 33.704 42.439 41.507 1.00 49.67 ? 546 PHE A CG 1 ATOM 3985 C CD1 . PHE A 1 505 ? 32.564 42.390 42.315 1.00 49.85 ? 546 PHE A CD1 1 ATOM 3986 C CD2 . PHE A 1 505 ? 34.948 42.191 42.084 1.00 51.49 ? 546 PHE A CD2 1 ATOM 3987 C CE1 . PHE A 1 505 ? 32.659 42.112 43.695 1.00 49.18 ? 546 PHE A CE1 1 ATOM 3988 C CE2 . PHE A 1 505 ? 35.065 41.917 43.460 1.00 51.38 ? 546 PHE A CE2 1 ATOM 3989 C CZ . PHE A 1 505 ? 33.920 41.875 44.266 1.00 50.93 ? 546 PHE A CZ 1 ATOM 3990 N N . SER A 1 506 ? 31.177 44.640 39.598 1.00 46.51 ? 547 SER A N 1 ATOM 3991 C CA . SER A 1 506 ? 29.885 45.269 39.978 1.00 44.02 ? 547 SER A CA 1 ATOM 3992 C C . SER A 1 506 ? 29.109 44.399 40.965 1.00 41.43 ? 547 SER A C 1 ATOM 3993 O O . SER A 1 506 ? 28.999 43.178 40.758 1.00 41.89 ? 547 SER A O 1 ATOM 3994 C CB . SER A 1 506 ? 29.003 45.411 38.738 1.00 44.85 ? 547 SER A CB 1 ATOM 3995 O OG . SER A 1 506 ? 29.762 45.135 37.582 1.00 46.86 ? 547 SER A OG 1 ATOM 3996 N N . GLY A 1 507 ? 28.543 45.020 42.001 1.00 37.48 ? 548 GLY A N 1 ATOM 3997 C CA . GLY A 1 507 ? 27.816 44.298 43.069 1.00 34.06 ? 548 GLY A CA 1 ATOM 3998 C C . GLY A 1 507 ? 28.631 43.095 43.542 1.00 32.46 ? 548 GLY A C 1 ATOM 3999 O O . GLY A 1 507 ? 29.835 43.220 43.788 1.00 34.20 ? 548 GLY A O 1 ATOM 4000 N N . TYR A 1 508 ? 28.004 41.921 43.630 1.00 27.06 ? 549 TYR A N 1 ATOM 4001 C CA . TYR A 1 508 ? 28.760 40.684 43.853 1.00 23.64 ? 549 TYR A CA 1 ATOM 4002 C C . TYR A 1 508 ? 28.596 39.773 42.613 1.00 21.97 ? 549 TYR A C 1 ATOM 4003 O O . TYR A 1 508 ? 27.547 39.804 41.911 1.00 21.28 ? 549 TYR A O 1 ATOM 4004 C CB . TYR A 1 508 ? 28.320 39.971 45.134 1.00 22.79 ? 549 TYR A CB 1 ATOM 4005 C CG . TYR A 1 508 ? 26.848 39.676 45.200 1.00 20.64 ? 549 TYR A CG 1 ATOM 4006 C CD1 . TYR A 1 508 ? 26.341 38.412 44.895 1.00 19.54 ? 549 TYR A CD1 1 ATOM 4007 C CD2 . TYR A 1 508 ? 25.961 40.674 45.558 1.00 19.41 ? 549 TYR A CD2 1 ATOM 4008 C CE1 . TYR A 1 508 ? 24.956 38.121 44.913 1.00 17.44 ? 549 TYR A CE1 1 ATOM 4009 C CE2 . TYR A 1 508 ? 24.587 40.394 45.593 1.00 19.16 ? 549 TYR A CE2 1 ATOM 4010 C CZ . TYR A 1 508 ? 24.093 39.145 45.262 1.00 18.55 ? 549 TYR A CZ 1 ATOM 4011 O OH . TYR A 1 508 ? 22.737 38.892 45.303 1.00 18.00 ? 549 TYR A OH 1 ATOM 4012 N N . PRO A 1 509 ? 29.622 38.952 42.327 1.00 21.06 ? 550 PRO A N 1 ATOM 4013 C CA . PRO A 1 509 ? 29.596 38.242 41.038 1.00 20.10 ? 550 PRO A CA 1 ATOM 4014 C C . PRO A 1 509 ? 28.423 37.315 40.768 1.00 18.98 ? 550 PRO A C 1 ATOM 4015 O O . PRO A 1 509 ? 28.032 37.215 39.625 1.00 20.45 ? 550 PRO A O 1 ATOM 4016 C CB . PRO A 1 509 ? 30.922 37.419 41.053 1.00 19.76 ? 550 PRO A CB 1 ATOM 4017 C CG . PRO A 1 509 ? 31.871 38.395 41.842 1.00 21.81 ? 550 PRO A CG 1 ATOM 4018 C CD . PRO A 1 509 ? 30.959 38.870 42.983 1.00 22.09 ? 550 PRO A CD 1 ATOM 4019 N N . LEU A 1 510 ? 27.905 36.652 41.806 1.00 18.23 ? 551 LEU A N 1 ATOM 4020 C CA . LEU A 1 510 ? 26.882 35.598 41.592 1.00 18.41 ? 551 LEU A CA 1 ATOM 4021 C C . LEU A 1 510 ? 25.479 36.173 41.654 1.00 18.06 ? 551 LEU A C 1 ATOM 4022 O O . LEU A 1 510 ? 24.483 35.425 41.674 1.00 19.69 ? 551 LEU A O 1 ATOM 4023 C CB . LEU A 1 510 ? 27.028 34.476 42.611 1.00 17.84 ? 551 LEU A CB 1 ATOM 4024 C CG . LEU A 1 510 ? 28.368 33.749 42.285 1.00 18.29 ? 551 LEU A CG 1 ATOM 4025 C CD1 . LEU A 1 510 ? 28.668 32.715 43.334 1.00 20.87 ? 551 LEU A CD1 1 ATOM 4026 C CD2 . LEU A 1 510 ? 28.337 33.121 40.874 1.00 17.27 ? 551 LEU A CD2 1 ATOM 4027 N N . TYR A 1 511 ? 25.415 37.490 41.698 1.00 17.17 ? 552 TYR A N 1 ATOM 4028 C CA . TYR A 1 511 ? 24.089 38.181 41.697 1.00 16.59 ? 552 TYR A CA 1 ATOM 4029 C C . TYR A 1 511 ? 23.075 37.654 40.687 1.00 15.92 ? 552 TYR A C 1 ATOM 4030 O O . TYR A 1 511 ? 23.323 37.645 39.459 1.00 17.09 ? 552 TYR A O 1 ATOM 4031 C CB . TYR A 1 511 ? 24.409 39.659 41.477 1.00 16.46 ? 552 TYR A CB 1 ATOM 4032 C CG . TYR A 1 511 ? 23.214 40.611 41.262 1.00 16.23 ? 552 TYR A CG 1 ATOM 4033 C CD1 . TYR A 1 511 ? 22.315 40.878 42.297 1.00 17.13 ? 552 TYR A CD1 1 ATOM 4034 C CD2 . TYR A 1 511 ? 23.018 41.235 40.018 1.00 19.32 ? 552 TYR A CD2 1 ATOM 4035 C CE1 . TYR A 1 511 ? 21.231 41.782 42.069 1.00 14.81 ? 552 TYR A CE1 1 ATOM 4036 C CE2 . TYR A 1 511 ? 22.007 42.155 39.816 1.00 17.76 ? 552 TYR A CE2 1 ATOM 4037 C CZ . TYR A 1 511 ? 21.094 42.381 40.800 1.00 16.70 ? 552 TYR A CZ 1 ATOM 4038 O OH . TYR A 1 511 ? 20.057 43.250 40.502 1.00 16.34 ? 552 TYR A OH 1 ATOM 4039 N N . HIS A 1 512 ? 21.922 37.190 41.196 1.00 17.33 ? 553 HIS A N 1 ATOM 4040 C CA . HIS A 1 512 ? 20.733 36.756 40.408 1.00 16.20 ? 553 HIS A CA 1 ATOM 4041 C C . HIS A 1 512 ? 20.990 35.503 39.554 1.00 17.76 ? 553 HIS A C 1 ATOM 4042 O O . HIS A 1 512 ? 20.247 35.219 38.584 1.00 17.72 ? 553 HIS A O 1 ATOM 4043 C CB . HIS A 1 512 ? 20.220 37.890 39.511 1.00 16.90 ? 553 HIS A CB 1 ATOM 4044 C CG . HIS A 1 512 ? 19.454 38.992 40.254 1.00 15.52 ? 553 HIS A CG 1 ATOM 4045 N ND1 . HIS A 1 512 ? 18.811 40.010 39.577 1.00 15.14 ? 553 HIS A ND1 1 ATOM 4046 C CD2 . HIS A 1 512 ? 19.239 39.232 41.575 1.00 16.26 ? 553 HIS A CD2 1 ATOM 4047 C CE1 . HIS A 1 512 ? 18.229 40.830 40.441 1.00 17.05 ? 553 HIS A CE1 1 ATOM 4048 N NE2 . HIS A 1 512 ? 18.383 40.322 41.647 1.00 13.27 ? 553 HIS A NE2 1 ATOM 4049 N N . SER A 1 513 ? 22.030 34.767 39.963 1.00 17.29 ? 554 SER A N 1 ATOM 4050 C CA . SER A 1 513 ? 22.332 33.454 39.305 1.00 17.59 ? 554 SER A CA 1 ATOM 4051 C C . SER A 1 513 ? 21.854 32.293 40.168 1.00 18.42 ? 554 SER A C 1 ATOM 4052 O O . SER A 1 513 ? 21.685 32.450 41.388 1.00 18.64 ? 554 SER A O 1 ATOM 4053 C CB . SER A 1 513 ? 23.863 33.406 39.098 1.00 17.38 ? 554 SER A CB 1 ATOM 4054 O OG A SER A 1 513 ? 24.535 33.000 40.266 0.50 19.69 ? 554 SER A OG 1 ATOM 4055 O OG B SER A 1 513 ? 24.373 32.074 39.046 0.50 17.90 ? 554 SER A OG 1 ATOM 4056 N N . VAL A 1 514 ? 21.795 31.096 39.588 1.00 18.49 ? 555 VAL A N 1 ATOM 4057 C CA . VAL A 1 514 ? 21.400 29.891 40.352 1.00 19.63 ? 555 VAL A CA 1 ATOM 4058 C C . VAL A 1 514 ? 22.476 29.594 41.443 1.00 19.57 ? 555 VAL A C 1 ATOM 4059 O O . VAL A 1 514 ? 22.179 28.857 42.422 1.00 20.72 ? 555 VAL A O 1 ATOM 4060 C CB . VAL A 1 514 ? 21.282 28.692 39.410 1.00 19.83 ? 555 VAL A CB 1 ATOM 4061 C CG1 . VAL A 1 514 ? 22.714 28.260 39.007 1.00 19.18 ? 555 VAL A CG1 1 ATOM 4062 C CG2 . VAL A 1 514 ? 20.598 27.508 40.099 1.00 20.71 ? 555 VAL A CG2 1 ATOM 4063 N N . TYR A 1 515 ? 23.680 30.192 41.305 1.00 17.75 ? 556 TYR A N 1 ATOM 4064 C CA . TYR A 1 515 ? 24.811 29.864 42.217 1.00 20.14 ? 556 TYR A CA 1 ATOM 4065 C C . TYR A 1 515 ? 24.711 30.602 43.542 1.00 21.01 ? 556 TYR A C 1 ATOM 4066 O O . TYR A 1 515 ? 25.498 30.333 44.456 1.00 22.28 ? 556 TYR A O 1 ATOM 4067 C CB . TYR A 1 515 ? 26.203 30.080 41.548 1.00 19.61 ? 556 TYR A CB 1 ATOM 4068 C CG . TYR A 1 515 ? 26.274 29.281 40.291 1.00 20.06 ? 556 TYR A CG 1 ATOM 4069 C CD1 . TYR A 1 515 ? 26.222 27.868 40.342 1.00 20.57 ? 556 TYR A CD1 1 ATOM 4070 C CD2 . TYR A 1 515 ? 26.368 29.899 39.061 1.00 20.95 ? 556 TYR A CD2 1 ATOM 4071 C CE1 . TYR A 1 515 ? 26.219 27.109 39.149 1.00 18.60 ? 556 TYR A CE1 1 ATOM 4072 C CE2 . TYR A 1 515 ? 26.427 29.134 37.862 1.00 21.87 ? 556 TYR A CE2 1 ATOM 4073 C CZ . TYR A 1 515 ? 26.334 27.755 37.936 1.00 21.80 ? 556 TYR A CZ 1 ATOM 4074 O OH . TYR A 1 515 ? 26.308 27.002 36.768 1.00 22.76 ? 556 TYR A OH 1 ATOM 4075 N N . GLU A 1 516 ? 23.764 31.553 43.651 1.00 20.07 ? 557 GLU A N 1 ATOM 4076 C CA . GLU A 1 516 ? 23.576 32.300 44.897 1.00 20.94 ? 557 GLU A CA 1 ATOM 4077 C C . GLU A 1 516 ? 22.825 31.437 45.899 1.00 19.62 ? 557 GLU A C 1 ATOM 4078 O O . GLU A 1 516 ? 21.584 31.399 45.902 1.00 19.34 ? 557 GLU A O 1 ATOM 4079 C CB . GLU A 1 516 ? 22.728 33.547 44.536 1.00 23.18 ? 557 GLU A CB 1 ATOM 4080 C CG . GLU A 1 516 ? 23.264 34.765 44.961 1.00 27.33 ? 557 GLU A CG 1 ATOM 4081 C CD . GLU A 1 516 ? 22.114 35.792 45.073 1.00 22.31 ? 557 GLU A CD 1 ATOM 4082 O OE1 . GLU A 1 516 ? 21.861 36.568 44.115 1.00 24.39 ? 557 GLU A OE1 1 ATOM 4083 O OE2 . GLU A 1 516 ? 21.431 35.694 46.068 1.00 20.56 ? 557 GLU A OE2 1 ATOM 4084 N N . THR A 1 517 ? 23.562 30.654 46.709 1.00 18.78 ? 558 THR A N 1 ATOM 4085 C CA . THR A 1 517 ? 22.988 29.639 47.554 1.00 19.36 ? 558 THR A CA 1 ATOM 4086 C C . THR A 1 517 ? 23.387 29.865 49.013 1.00 18.69 ? 558 THR A C 1 ATOM 4087 O O . THR A 1 517 ? 24.265 30.667 49.305 1.00 19.65 ? 558 THR A O 1 ATOM 4088 C CB . THR A 1 517 ? 23.567 28.255 47.165 1.00 19.25 ? 558 THR A CB 1 ATOM 4089 O OG1 . THR A 1 517 ? 24.994 28.346 47.233 1.00 22.26 ? 558 THR A OG1 1 ATOM 4090 C CG2 . THR A 1 517 ? 23.153 27.874 45.738 1.00 20.60 ? 558 THR A CG2 1 ATOM 4091 N N . TYR A 1 518 ? 22.785 29.080 49.906 1.00 18.65 ? 559 TYR A N 1 ATOM 4092 C CA . TYR A 1 518 ? 23.215 29.056 51.291 1.00 19.24 ? 559 TYR A CA 1 ATOM 4093 C C . TYR A 1 518 ? 24.734 28.746 51.371 1.00 19.98 ? 559 TYR A C 1 ATOM 4094 O O . TYR A 1 518 ? 25.476 29.387 52.112 1.00 20.93 ? 559 TYR A O 1 ATOM 4095 C CB . TYR A 1 518 ? 22.439 27.995 52.050 1.00 19.57 ? 559 TYR A CB 1 ATOM 4096 C CG . TYR A 1 518 ? 23.011 27.747 53.424 1.00 20.31 ? 559 TYR A CG 1 ATOM 4097 C CD1 . TYR A 1 518 ? 22.703 28.573 54.461 1.00 22.49 ? 559 TYR A CD1 1 ATOM 4098 C CD2 . TYR A 1 518 ? 23.915 26.673 53.672 1.00 22.43 ? 559 TYR A CD2 1 ATOM 4099 C CE1 . TYR A 1 518 ? 23.228 28.373 55.738 1.00 24.77 ? 559 TYR A CE1 1 ATOM 4100 C CE2 . TYR A 1 518 ? 24.447 26.464 54.951 1.00 25.30 ? 559 TYR A CE2 1 ATOM 4101 C CZ . TYR A 1 518 ? 24.100 27.311 55.983 1.00 26.64 ? 559 TYR A CZ 1 ATOM 4102 O OH . TYR A 1 518 ? 24.587 27.136 57.286 1.00 26.93 ? 559 TYR A OH 1 ATOM 4103 N N . GLU A 1 519 ? 25.176 27.798 50.563 1.00 19.55 ? 560 GLU A N 1 ATOM 4104 C CA . GLU A 1 519 ? 26.613 27.439 50.637 1.00 20.63 ? 560 GLU A CA 1 ATOM 4105 C C . GLU A 1 519 ? 27.527 28.576 50.250 1.00 20.99 ? 560 GLU A C 1 ATOM 4106 O O . GLU A 1 519 ? 28.657 28.707 50.771 1.00 22.37 ? 560 GLU A O 1 ATOM 4107 C CB . GLU A 1 519 ? 26.912 26.198 49.762 1.00 22.44 ? 560 GLU A CB 1 ATOM 4108 C CG . GLU A 1 519 ? 26.274 24.916 50.289 1.00 22.78 ? 560 GLU A CG 1 ATOM 4109 C CD . GLU A 1 519 ? 24.777 24.857 50.086 1.00 24.09 ? 560 GLU A CD 1 ATOM 4110 O OE1 . GLU A 1 519 ? 24.289 25.371 49.057 1.00 24.19 ? 560 GLU A OE1 1 ATOM 4111 O OE2 . GLU A 1 519 ? 24.080 24.264 50.934 1.00 26.12 ? 560 GLU A OE2 1 ATOM 4112 N N . LEU A 1 520 ? 27.090 29.399 49.293 1.00 20.09 ? 561 LEU A N 1 ATOM 4113 C CA . LEU A 1 520 ? 27.927 30.530 48.918 1.00 20.57 ? 561 LEU A CA 1 ATOM 4114 C C . LEU A 1 520 ? 28.202 31.392 50.137 1.00 20.43 ? 561 LEU A C 1 ATOM 4115 O O . LEU A 1 520 ? 29.349 31.846 50.377 1.00 20.69 ? 561 LEU A O 1 ATOM 4116 C CB . LEU A 1 520 ? 27.215 31.376 47.848 1.00 19.46 ? 561 LEU A CB 1 ATOM 4117 C CG . LEU A 1 520 ? 27.875 32.694 47.473 1.00 20.35 ? 561 LEU A CG 1 ATOM 4118 C CD1 . LEU A 1 520 ? 29.278 32.469 46.968 1.00 21.72 ? 561 LEU A CD1 1 ATOM 4119 C CD2 . LEU A 1 520 ? 26.993 33.506 46.466 1.00 21.47 ? 561 LEU A CD2 1 ATOM 4120 N N . VAL A 1 521 ? 27.126 31.678 50.894 1.00 20.48 ? 562 VAL A N 1 ATOM 4121 C CA . VAL A 1 521 ? 27.235 32.548 52.050 1.00 20.04 ? 562 VAL A CA 1 ATOM 4122 C C . VAL A 1 521 ? 28.062 31.890 53.175 1.00 22.29 ? 562 VAL A C 1 ATOM 4123 O O . VAL A 1 521 ? 29.042 32.463 53.663 1.00 23.54 ? 562 VAL A O 1 ATOM 4124 C CB . VAL A 1 521 ? 25.844 32.921 52.571 1.00 21.32 ? 562 VAL A CB 1 ATOM 4125 C CG1 . VAL A 1 521 ? 25.986 33.773 53.840 1.00 20.23 ? 562 VAL A CG1 1 ATOM 4126 C CG2 . VAL A 1 521 ? 25.102 33.696 51.452 1.00 21.26 ? 562 VAL A CG2 1 ATOM 4127 N N . GLU A 1 522 ? 27.701 30.660 53.519 1.00 22.98 ? 563 GLU A N 1 ATOM 4128 C CA . GLU A 1 522 ? 28.324 29.939 54.636 1.00 24.35 ? 563 GLU A CA 1 ATOM 4129 C C . GLU A 1 522 ? 29.799 29.637 54.367 1.00 24.60 ? 563 GLU A C 1 ATOM 4130 O O . GLU A 1 522 ? 30.634 29.677 55.289 1.00 25.34 ? 563 GLU A O 1 ATOM 4131 C CB . GLU A 1 522 ? 27.578 28.630 54.862 1.00 25.57 ? 563 GLU A CB 1 ATOM 4132 C CG . GLU A 1 522 ? 27.885 27.970 56.206 1.00 30.45 ? 563 GLU A CG 1 ATOM 4133 C CD . GLU A 1 522 ? 29.077 27.026 56.119 1.00 38.21 ? 563 GLU A CD 1 ATOM 4134 O OE1 . GLU A 1 522 ? 29.325 26.467 55.014 1.00 38.28 ? 563 GLU A OE1 1 ATOM 4135 O OE2 . GLU A 1 522 ? 29.769 26.872 57.160 1.00 39.37 ? 563 GLU A OE2 1 ATOM 4136 N N . LYS A 1 523 ? 30.137 29.344 53.113 1.00 22.85 ? 564 LYS A N 1 ATOM 4137 C CA . LYS A 1 523 ? 31.524 28.959 52.824 1.00 23.65 ? 564 LYS A CA 1 ATOM 4138 C C . LYS A 1 523 ? 32.417 30.166 52.536 1.00 24.70 ? 564 LYS A C 1 ATOM 4139 O O . LYS A 1 523 ? 33.601 30.188 52.938 1.00 26.74 ? 564 LYS A O 1 ATOM 4140 C CB . LYS A 1 523 ? 31.553 28.002 51.629 1.00 23.05 ? 564 LYS A CB 1 ATOM 4141 C CG . LYS A 1 523 ? 30.999 26.620 51.912 1.00 25.71 ? 564 LYS A CG 1 ATOM 4142 C CD . LYS A 1 523 ? 31.134 25.755 50.627 1.00 28.07 ? 564 LYS A CD 1 ATOM 4143 C CE . LYS A 1 523 ? 30.388 24.398 50.687 1.00 33.30 ? 564 LYS A CE 1 ATOM 4144 N NZ . LYS A 1 523 ? 30.549 23.668 51.960 1.00 37.62 ? 564 LYS A NZ 1 ATOM 4145 N N . PHE A 1 524 ? 31.885 31.174 51.841 1.00 23.73 ? 565 PHE A N 1 ATOM 4146 C CA . PHE A 1 524 ? 32.749 32.188 51.258 1.00 23.41 ? 565 PHE A CA 1 ATOM 4147 C C . PHE A 1 524 ? 32.506 33.574 51.798 1.00 23.92 ? 565 PHE A C 1 ATOM 4148 O O . PHE A 1 524 ? 33.438 34.382 51.805 1.00 27.68 ? 565 PHE A O 1 ATOM 4149 C CB . PHE A 1 524 ? 32.673 32.200 49.721 1.00 24.10 ? 565 PHE A CB 1 ATOM 4150 C CG . PHE A 1 524 ? 33.081 30.891 49.099 1.00 25.11 ? 565 PHE A CG 1 ATOM 4151 C CD1 . PHE A 1 524 ? 34.404 30.467 49.212 1.00 27.93 ? 565 PHE A CD1 1 ATOM 4152 C CD2 . PHE A 1 524 ? 32.153 30.082 48.448 1.00 24.55 ? 565 PHE A CD2 1 ATOM 4153 C CE1 . PHE A 1 524 ? 34.789 29.255 48.673 1.00 29.18 ? 565 PHE A CE1 1 ATOM 4154 C CE2 . PHE A 1 524 ? 32.525 28.838 47.880 1.00 26.35 ? 565 PHE A CE2 1 ATOM 4155 C CZ . PHE A 1 524 ? 33.859 28.431 48.008 1.00 28.23 ? 565 PHE A CZ 1 ATOM 4156 N N . TYR A 1 525 ? 31.277 33.905 52.215 1.00 22.67 ? 566 TYR A N 1 ATOM 4157 C CA . TYR A 1 525 ? 31.088 35.276 52.681 1.00 21.14 ? 566 TYR A CA 1 ATOM 4158 C C . TYR A 1 525 ? 31.162 35.460 54.179 1.00 19.92 ? 566 TYR A C 1 ATOM 4159 O O . TYR A 1 525 ? 31.761 36.456 54.646 1.00 22.23 ? 566 TYR A O 1 ATOM 4160 C CB . TYR A 1 525 ? 29.725 35.840 52.159 1.00 19.48 ? 566 TYR A CB 1 ATOM 4161 C CG . TYR A 1 525 ? 29.831 36.338 50.726 1.00 20.54 ? 566 TYR A CG 1 ATOM 4162 C CD1 . TYR A 1 525 ? 29.840 35.432 49.668 1.00 21.19 ? 566 TYR A CD1 1 ATOM 4163 C CD2 . TYR A 1 525 ? 29.950 37.719 50.425 1.00 21.49 ? 566 TYR A CD2 1 ATOM 4164 C CE1 . TYR A 1 525 ? 29.943 35.852 48.337 1.00 20.33 ? 566 TYR A CE1 1 ATOM 4165 C CE2 . TYR A 1 525 ? 30.046 38.170 49.085 1.00 21.42 ? 566 TYR A CE2 1 ATOM 4166 C CZ . TYR A 1 525 ? 30.067 37.219 48.048 1.00 20.67 ? 566 TYR A CZ 1 ATOM 4167 O OH . TYR A 1 525 ? 30.211 37.625 46.759 1.00 23.52 ? 566 TYR A OH 1 ATOM 4168 N N . ASP A 1 526 ? 30.500 34.598 54.963 1.00 20.45 ? 567 ASP A N 1 ATOM 4169 C CA . ASP A 1 526 ? 30.335 34.896 56.393 1.00 21.11 ? 567 ASP A CA 1 ATOM 4170 C C . ASP A 1 526 ? 30.131 33.615 57.208 1.00 22.28 ? 567 ASP A C 1 ATOM 4171 O O . ASP A 1 526 ? 29.089 33.364 57.770 1.00 22.85 ? 567 ASP A O 1 ATOM 4172 C CB . ASP A 1 526 ? 29.109 35.844 56.581 1.00 19.36 ? 567 ASP A CB 1 ATOM 4173 C CG . ASP A 1 526 ? 29.024 36.455 57.991 1.00 21.18 ? 567 ASP A CG 1 ATOM 4174 O OD1 . ASP A 1 526 ? 29.999 36.410 58.796 1.00 25.16 ? 567 ASP A OD1 1 ATOM 4175 O OD2 . ASP A 1 526 ? 27.944 37.016 58.266 1.00 21.98 ? 567 ASP A OD2 1 ATOM 4176 N N . PRO A 1 527 ? 31.175 32.755 57.265 1.00 23.31 ? 568 PRO A N 1 ATOM 4177 C CA . PRO A 1 527 ? 30.984 31.460 57.884 1.00 23.75 ? 568 PRO A CA 1 ATOM 4178 C C . PRO A 1 527 ? 30.511 31.542 59.320 1.00 23.74 ? 568 PRO A C 1 ATOM 4179 O O . PRO A 1 527 ? 29.789 30.640 59.765 1.00 25.45 ? 568 PRO A O 1 ATOM 4180 C CB . PRO A 1 527 ? 32.393 30.832 57.865 1.00 24.67 ? 568 PRO A CB 1 ATOM 4181 C CG . PRO A 1 527 ? 33.185 31.613 56.886 1.00 25.71 ? 568 PRO A CG 1 ATOM 4182 C CD . PRO A 1 527 ? 32.478 32.939 56.623 1.00 25.43 ? 568 PRO A CD 1 ATOM 4183 N N A MET A 1 528 ? 30.906 32.575 60.055 0.60 23.77 ? 569 MET A N 1 ATOM 4184 N N B MET A 1 528 ? 30.927 32.601 60.013 0.40 23.74 ? 569 MET A N 1 ATOM 4185 C CA A MET A 1 528 ? 30.503 32.689 61.471 0.60 23.92 ? 569 MET A CA 1 ATOM 4186 C CA B MET A 1 528 ? 30.625 32.819 61.429 0.40 23.73 ? 569 MET A CA 1 ATOM 4187 C C A MET A 1 528 ? 29.185 33.458 61.621 0.60 23.40 ? 569 MET A C 1 ATOM 4188 C C B MET A 1 528 ? 29.367 33.662 61.621 0.40 23.08 ? 569 MET A C 1 ATOM 4189 O O A MET A 1 528 ? 28.573 33.497 62.703 0.60 22.02 ? 569 MET A O 1 ATOM 4190 O O B MET A 1 528 ? 28.983 33.966 62.739 0.40 22.03 ? 569 MET A O 1 ATOM 4191 C CB A MET A 1 528 ? 31.592 33.367 62.324 0.60 25.65 ? 569 MET A CB 1 ATOM 4192 C CB B MET A 1 528 ? 31.778 33.558 62.111 0.40 25.17 ? 569 MET A CB 1 ATOM 4193 C CG A MET A 1 528 ? 32.933 32.603 62.366 0.60 28.55 ? 569 MET A CG 1 ATOM 4194 C CG B MET A 1 528 ? 33.150 32.935 61.890 0.40 27.02 ? 569 MET A CG 1 ATOM 4195 S SD A MET A 1 528 ? 32.762 30.862 62.742 0.60 33.89 ? 569 MET A SD 1 ATOM 4196 S SD B MET A 1 528 ? 34.293 33.612 63.119 0.40 34.96 ? 569 MET A SD 1 ATOM 4197 C CE A MET A 1 528 ? 31.852 30.817 64.284 0.60 31.76 ? 569 MET A CE 1 ATOM 4198 C CE B MET A 1 528 ? 35.308 34.711 62.126 0.40 31.87 ? 569 MET A CE 1 ATOM 4199 N N . PHE A 1 529 ? 28.739 34.052 60.519 1.00 22.14 ? 570 PHE A N 1 ATOM 4200 C CA . PHE A 1 529 ? 27.525 34.888 60.581 1.00 21.82 ? 570 PHE A CA 1 ATOM 4201 C C . PHE A 1 529 ? 27.686 36.130 61.429 1.00 22.76 ? 570 PHE A C 1 ATOM 4202 O O . PHE A 1 529 ? 26.706 36.759 61.849 1.00 22.64 ? 570 PHE A O 1 ATOM 4203 C CB . PHE A 1 529 ? 26.269 34.047 60.879 1.00 22.65 ? 570 PHE A CB 1 ATOM 4204 C CG . PHE A 1 529 ? 25.848 33.252 59.678 1.00 22.45 ? 570 PHE A CG 1 ATOM 4205 C CD1 . PHE A 1 529 ? 24.863 33.729 58.799 1.00 22.35 ? 570 PHE A CD1 1 ATOM 4206 C CD2 . PHE A 1 529 ? 26.491 32.053 59.376 1.00 21.62 ? 570 PHE A CD2 1 ATOM 4207 C CE1 . PHE A 1 529 ? 24.521 33.010 57.634 1.00 22.67 ? 570 PHE A CE1 1 ATOM 4208 C CE2 . PHE A 1 529 ? 26.167 31.328 58.208 1.00 24.28 ? 570 PHE A CE2 1 ATOM 4209 C CZ . PHE A 1 529 ? 25.172 31.817 57.332 1.00 23.50 ? 570 PHE A CZ 1 ATOM 4210 N N . LYS A 1 530 ? 28.945 36.516 61.641 1.00 21.75 ? 571 LYS A N 1 ATOM 4211 C CA . LYS A 1 530 ? 29.227 37.732 62.390 1.00 22.93 ? 571 LYS A CA 1 ATOM 4212 C C . LYS A 1 530 ? 28.898 39.017 61.618 1.00 22.13 ? 571 LYS A C 1 ATOM 4213 O O . LYS A 1 530 ? 28.478 40.012 62.237 1.00 22.31 ? 571 LYS A O 1 ATOM 4214 C CB . LYS A 1 530 ? 30.699 37.755 62.841 1.00 23.45 ? 571 LYS A CB 1 ATOM 4215 C CG . LYS A 1 530 ? 31.701 37.810 61.716 1.00 24.74 ? 571 LYS A CG 1 ATOM 4216 C CD . LYS A 1 530 ? 33.093 37.855 62.347 1.00 26.30 ? 571 LYS A CD 1 ATOM 4217 C CE . LYS A 1 530 ? 34.164 38.000 61.290 1.00 28.82 ? 571 LYS A CE 1 ATOM 4218 N NZ . LYS A 1 530 ? 35.536 38.225 61.922 1.00 31.78 ? 571 LYS A NZ 1 ATOM 4219 N N . TYR A 1 531 ? 29.075 39.028 60.294 1.00 22.04 ? 572 TYR A N 1 ATOM 4220 C CA . TYR A 1 531 ? 28.725 40.236 59.531 1.00 21.04 ? 572 TYR A CA 1 ATOM 4221 C C . TYR A 1 531 ? 27.208 40.342 59.470 1.00 20.87 ? 572 TYR A C 1 ATOM 4222 O O . TYR A 1 531 ? 26.672 41.450 59.598 1.00 20.83 ? 572 TYR A O 1 ATOM 4223 C CB . TYR A 1 531 ? 29.342 40.240 58.114 1.00 21.63 ? 572 TYR A CB 1 ATOM 4224 C CG . TYR A 1 531 ? 30.858 40.107 58.178 1.00 22.15 ? 572 TYR A CG 1 ATOM 4225 C CD1 . TYR A 1 531 ? 31.628 41.078 58.821 1.00 24.92 ? 572 TYR A CD1 1 ATOM 4226 C CD2 . TYR A 1 531 ? 31.506 38.990 57.637 1.00 24.78 ? 572 TYR A CD2 1 ATOM 4227 C CE1 . TYR A 1 531 ? 33.005 40.961 58.886 1.00 26.95 ? 572 TYR A CE1 1 ATOM 4228 C CE2 . TYR A 1 531 ? 32.877 38.878 57.712 1.00 25.99 ? 572 TYR A CE2 1 ATOM 4229 C CZ . TYR A 1 531 ? 33.615 39.866 58.340 1.00 26.71 ? 572 TYR A CZ 1 ATOM 4230 O OH . TYR A 1 531 ? 35.006 39.708 58.408 1.00 32.06 ? 572 TYR A OH 1 ATOM 4231 N N . HIS A 1 532 ? 26.518 39.223 59.274 1.00 20.38 ? 573 HIS A N 1 ATOM 4232 C CA . HIS A 1 532 ? 25.039 39.243 59.398 1.00 20.36 ? 573 HIS A CA 1 ATOM 4233 C C . HIS A 1 532 ? 24.583 39.783 60.746 1.00 20.15 ? 573 HIS A C 1 ATOM 4234 O O . HIS A 1 532 ? 23.651 40.579 60.832 1.00 19.10 ? 573 HIS A O 1 ATOM 4235 C CB . HIS A 1 532 ? 24.457 37.853 59.271 1.00 19.84 ? 573 HIS A CB 1 ATOM 4236 C CG . HIS A 1 532 ? 24.364 37.373 57.875 1.00 20.87 ? 573 HIS A CG 1 ATOM 4237 N ND1 . HIS A 1 532 ? 25.456 36.930 57.162 1.00 20.18 ? 573 HIS A ND1 1 ATOM 4238 C CD2 . HIS A 1 532 ? 23.292 37.223 57.065 1.00 21.59 ? 573 HIS A CD2 1 ATOM 4239 C CE1 . HIS A 1 532 ? 25.060 36.522 55.963 1.00 22.68 ? 573 HIS A CE1 1 ATOM 4240 N NE2 . HIS A 1 532 ? 23.746 36.687 55.878 1.00 22.21 ? 573 HIS A NE2 1 ATOM 4241 N N . LEU A 1 533 ? 25.204 39.316 61.824 1.00 20.45 ? 574 LEU A N 1 ATOM 4242 C CA . LEU A 1 533 ? 24.807 39.788 63.127 1.00 19.76 ? 574 LEU A CA 1 ATOM 4243 C C . LEU A 1 533 ? 25.040 41.295 63.283 1.00 20.05 ? 574 LEU A C 1 ATOM 4244 O O . LEU A 1 533 ? 24.157 42.006 63.797 1.00 20.29 ? 574 LEU A O 1 ATOM 4245 C CB . LEU A 1 533 ? 25.560 39.023 64.225 1.00 21.23 ? 574 LEU A CB 1 ATOM 4246 C CG . LEU A 1 533 ? 25.183 39.535 65.630 1.00 22.05 ? 574 LEU A CG 1 ATOM 4247 C CD1 . LEU A 1 533 ? 23.691 39.346 65.969 1.00 22.95 ? 574 LEU A CD1 1 ATOM 4248 C CD2 . LEU A 1 533 ? 26.057 38.748 66.624 1.00 25.18 ? 574 LEU A CD2 1 ATOM 4249 N N . THR A 1 534 ? 26.174 41.794 62.780 1.00 19.68 ? 575 THR A N 1 ATOM 4250 C CA . THR A 1 534 ? 26.477 43.234 62.793 1.00 19.47 ? 575 THR A CA 1 ATOM 4251 C C . THR A 1 534 ? 25.398 44.005 62.022 1.00 19.32 ? 575 THR A C 1 ATOM 4252 O O . THR A 1 534 ? 24.873 45.020 62.503 1.00 20.11 ? 575 THR A O 1 ATOM 4253 C CB . THR A 1 534 ? 27.878 43.520 62.271 1.00 22.06 ? 575 THR A CB 1 ATOM 4254 O OG1 . THR A 1 534 ? 28.810 42.981 63.240 1.00 21.83 ? 575 THR A OG1 1 ATOM 4255 C CG2 . THR A 1 534 ? 28.148 45.032 62.103 1.00 22.13 ? 575 THR A CG2 1 ATOM 4256 N N . VAL A 1 535 ? 25.048 43.496 60.851 1.00 19.10 ? 576 VAL A N 1 ATOM 4257 C CA . VAL A 1 535 ? 23.981 44.159 60.068 1.00 18.99 ? 576 VAL A CA 1 ATOM 4258 C C . VAL A 1 535 ? 22.634 44.103 60.808 1.00 19.51 ? 576 VAL A C 1 ATOM 4259 O O . VAL A 1 535 ? 21.857 45.060 60.774 1.00 19.94 ? 576 VAL A O 1 ATOM 4260 C CB . VAL A 1 535 ? 23.925 43.563 58.628 1.00 19.44 ? 576 VAL A CB 1 ATOM 4261 C CG1 . VAL A 1 535 ? 22.711 44.129 57.843 1.00 18.61 ? 576 VAL A CG1 1 ATOM 4262 C CG2 . VAL A 1 535 ? 25.227 43.908 57.930 1.00 19.95 ? 576 VAL A CG2 1 ATOM 4263 N N . ALA A 1 536 ? 22.350 43.001 61.499 1.00 18.84 ? 577 ALA A N 1 ATOM 4264 C CA . ALA A 1 536 ? 21.118 42.933 62.296 1.00 19.52 ? 577 ALA A CA 1 ATOM 4265 C C . ALA A 1 536 ? 21.125 43.975 63.397 1.00 20.04 ? 577 ALA A C 1 ATOM 4266 O O . ALA A 1 536 ? 20.097 44.622 63.678 1.00 18.60 ? 577 ALA A O 1 ATOM 4267 C CB . ALA A 1 536 ? 20.925 41.545 62.882 1.00 19.66 ? 577 ALA A CB 1 ATOM 4268 N N . GLN A 1 537 ? 22.278 44.143 64.034 1.00 20.06 ? 578 GLN A N 1 ATOM 4269 C CA . GLN A 1 537 ? 22.418 45.205 65.044 1.00 19.85 ? 578 GLN A CA 1 ATOM 4270 C C . GLN A 1 537 ? 22.219 46.629 64.492 1.00 20.59 ? 578 GLN A C 1 ATOM 4271 O O . GLN A 1 537 ? 21.625 47.497 65.169 1.00 20.85 ? 578 GLN A O 1 ATOM 4272 C CB . GLN A 1 537 ? 23.783 45.082 65.763 1.00 21.58 ? 578 GLN A CB 1 ATOM 4273 C CG . GLN A 1 537 ? 23.887 43.774 66.559 1.00 21.19 ? 578 GLN A CG 1 ATOM 4274 C CD . GLN A 1 537 ? 25.279 43.587 67.137 1.00 26.95 ? 578 GLN A CD 1 ATOM 4275 O OE1 . GLN A 1 537 ? 26.172 44.411 66.915 1.00 25.11 ? 578 GLN A OE1 1 ATOM 4276 N NE2 . GLN A 1 537 ? 25.465 42.497 67.909 1.00 27.24 ? 578 GLN A NE2 1 ATOM 4277 N N . VAL A 1 538 ? 22.728 46.880 63.293 1.00 19.49 ? 579 VAL A N 1 ATOM 4278 C CA . VAL A 1 538 ? 22.613 48.225 62.715 1.00 19.77 ? 579 VAL A CA 1 ATOM 4279 C C . VAL A 1 538 ? 21.143 48.408 62.335 1.00 18.73 ? 579 VAL A C 1 ATOM 4280 O O . VAL A 1 538 ? 20.489 49.400 62.753 1.00 18.95 ? 579 VAL A O 1 ATOM 4281 C CB . VAL A 1 538 ? 23.541 48.403 61.494 1.00 19.11 ? 579 VAL A CB 1 ATOM 4282 C CG1 . VAL A 1 538 ? 23.230 49.751 60.822 1.00 19.22 ? 579 VAL A CG1 1 ATOM 4283 C CG2 . VAL A 1 538 ? 25.032 48.351 61.909 1.00 19.98 ? 579 VAL A CG2 1 ATOM 4284 N N . ARG A 1 539 ? 20.588 47.485 61.544 1.00 18.03 ? 580 ARG A N 1 ATOM 4285 C CA . ARG A 1 539 ? 19.172 47.705 61.095 1.00 17.67 ? 580 ARG A CA 1 ATOM 4286 C C . ARG A 1 539 ? 18.208 47.728 62.287 1.00 19.37 ? 580 ARG A C 1 ATOM 4287 O O . ARG A 1 539 ? 17.327 48.593 62.386 1.00 18.43 ? 580 ARG A O 1 ATOM 4288 C CB . ARG A 1 539 ? 18.757 46.632 60.105 1.00 18.43 ? 580 ARG A CB 1 ATOM 4289 C CG . ARG A 1 539 ? 19.494 46.694 58.815 1.00 17.58 ? 580 ARG A CG 1 ATOM 4290 C CD . ARG A 1 539 ? 19.170 45.475 57.963 1.00 20.12 ? 580 ARG A CD 1 ATOM 4291 N NE . ARG A 1 539 ? 19.890 45.538 56.690 1.00 16.71 ? 580 ARG A NE 1 ATOM 4292 C CZ . ARG A 1 539 ? 19.827 44.599 55.738 1.00 19.15 ? 580 ARG A CZ 1 ATOM 4293 N NH1 . ARG A 1 539 ? 19.080 43.505 55.925 1.00 20.20 ? 580 ARG A NH1 1 ATOM 4294 N NH2 . ARG A 1 539 ? 20.505 44.753 54.595 1.00 16.63 ? 580 ARG A NH2 1 ATOM 4295 N N . GLY A 1 540 ? 18.366 46.748 63.184 1.00 18.19 ? 581 GLY A N 1 ATOM 4296 C CA . GLY A 1 540 ? 17.500 46.630 64.352 1.00 19.00 ? 581 GLY A CA 1 ATOM 4297 C C . GLY A 1 540 ? 17.672 47.790 65.339 1.00 19.07 ? 581 GLY A C 1 ATOM 4298 O O . GLY A 1 540 ? 16.682 48.305 65.894 1.00 18.62 ? 581 GLY A O 1 ATOM 4299 N N . GLY A 1 541 ? 18.914 48.220 65.529 1.00 19.33 ? 582 GLY A N 1 ATOM 4300 C CA . GLY A 1 541 ? 19.226 49.321 66.415 1.00 18.84 ? 582 GLY A CA 1 ATOM 4301 C C . GLY A 1 541 ? 18.594 50.591 65.867 1.00 19.29 ? 582 GLY A C 1 ATOM 4302 O O . GLY A 1 541 ? 18.054 51.396 66.611 1.00 20.22 ? 582 GLY A O 1 ATOM 4303 N N . MET A 1 542 ? 18.669 50.787 64.539 1.00 17.95 ? 583 MET A N 1 ATOM 4304 C CA . MET A 1 542 ? 18.046 51.990 63.959 1.00 17.54 ? 583 MET A CA 1 ATOM 4305 C C . MET A 1 542 ? 16.554 51.939 64.219 1.00 18.44 ? 583 MET A C 1 ATOM 4306 O O . MET A 1 542 ? 15.991 52.935 64.678 1.00 18.33 ? 583 MET A O 1 ATOM 4307 C CB . MET A 1 542 ? 18.352 52.068 62.444 1.00 16.92 ? 583 MET A CB 1 ATOM 4308 C CG . MET A 1 542 ? 19.784 52.460 62.178 1.00 18.69 ? 583 MET A CG 1 ATOM 4309 S SD . MET A 1 542 ? 20.229 52.452 60.434 1.00 5.82 ? 583 MET A SD 1 ATOM 4310 C CE . MET A 1 542 ? 19.485 54.008 59.889 1.00 21.47 ? 583 MET A CE 1 ATOM 4311 N N . VAL A 1 543 ? 15.916 50.783 63.965 1.00 17.56 ? 584 VAL A N 1 ATOM 4312 C CA . VAL A 1 543 ? 14.475 50.648 64.220 1.00 18.39 ? 584 VAL A CA 1 ATOM 4313 C C . VAL A 1 543 ? 14.176 50.932 65.699 1.00 18.56 ? 584 VAL A C 1 ATOM 4314 O O . VAL A 1 543 ? 13.227 51.669 65.996 1.00 18.94 ? 584 VAL A O 1 ATOM 4315 C CB . VAL A 1 543 ? 13.977 49.248 63.814 1.00 17.76 ? 584 VAL A CB 1 ATOM 4316 C CG1 . VAL A 1 543 ? 12.539 48.986 64.315 1.00 19.28 ? 584 VAL A CG1 1 ATOM 4317 C CG2 . VAL A 1 543 ? 14.069 49.128 62.266 1.00 16.81 ? 584 VAL A CG2 1 ATOM 4318 N N . PHE A 1 544 ? 14.967 50.325 66.588 1.00 19.96 ? 585 PHE A N 1 ATOM 4319 C CA . PHE A 1 544 ? 14.772 50.531 68.012 1.00 19.49 ? 585 PHE A CA 1 ATOM 4320 C C . PHE A 1 544 ? 14.765 51.992 68.393 1.00 20.38 ? 585 PHE A C 1 ATOM 4321 O O . PHE A 1 544 ? 13.836 52.460 69.078 1.00 20.53 ? 585 PHE A O 1 ATOM 4322 C CB . PHE A 1 544 ? 15.873 49.793 68.833 1.00 20.46 ? 585 PHE A CB 1 ATOM 4323 C CG . PHE A 1 544 ? 15.548 49.732 70.307 1.00 22.58 ? 585 PHE A CG 1 ATOM 4324 C CD1 . PHE A 1 544 ? 15.012 48.564 70.861 1.00 23.63 ? 585 PHE A CD1 1 ATOM 4325 C CD2 . PHE A 1 544 ? 15.716 50.861 71.115 1.00 23.80 ? 585 PHE A CD2 1 ATOM 4326 C CE1 . PHE A 1 544 ? 14.651 48.526 72.222 1.00 25.69 ? 585 PHE A CE1 1 ATOM 4327 C CE2 . PHE A 1 544 ? 15.369 50.811 72.502 1.00 23.46 ? 585 PHE A CE2 1 ATOM 4328 C CZ . PHE A 1 544 ? 14.838 49.630 73.013 1.00 23.07 ? 585 PHE A CZ 1 ATOM 4329 N N A GLU A 1 545 ? 15.795 52.719 67.985 0.60 20.25 ? 586 GLU A N 1 ATOM 4330 N N B GLU A 1 545 ? 15.780 52.728 67.961 0.40 20.35 ? 586 GLU A N 1 ATOM 4331 C CA A GLU A 1 545 ? 15.891 54.150 68.334 0.60 20.61 ? 586 GLU A CA 1 ATOM 4332 C CA B GLU A 1 545 ? 15.911 54.143 68.343 0.40 20.75 ? 586 GLU A CA 1 ATOM 4333 C C A GLU A 1 545 ? 14.712 54.913 67.740 0.60 19.74 ? 586 GLU A C 1 ATOM 4334 C C B GLU A 1 545 ? 14.857 55.036 67.677 0.40 19.90 ? 586 GLU A C 1 ATOM 4335 O O A GLU A 1 545 ? 14.025 55.658 68.432 0.60 20.29 ? 586 GLU A O 1 ATOM 4336 O O B GLU A 1 545 ? 14.416 56.021 68.265 0.40 20.30 ? 586 GLU A O 1 ATOM 4337 C CB A GLU A 1 545 ? 17.185 54.770 67.827 0.60 20.96 ? 586 GLU A CB 1 ATOM 4338 C CB B GLU A 1 545 ? 17.291 54.670 68.009 0.40 21.39 ? 586 GLU A CB 1 ATOM 4339 C CG A GLU A 1 545 ? 18.425 54.264 68.573 0.60 24.22 ? 586 GLU A CG 1 ATOM 4340 C CG B GLU A 1 545 ? 17.652 55.931 68.745 0.40 23.91 ? 586 GLU A CG 1 ATOM 4341 C CD A GLU A 1 545 ? 18.553 54.845 69.983 0.60 31.62 ? 586 GLU A CD 1 ATOM 4342 C CD B GLU A 1 545 ? 17.850 55.728 70.235 0.40 26.66 ? 586 GLU A CD 1 ATOM 4343 O OE1 A GLU A 1 545 ? 17.555 55.368 70.547 0.60 34.17 ? 586 GLU A OE1 1 ATOM 4344 O OE1 B GLU A 1 545 ? 17.947 54.554 70.709 0.40 25.38 ? 586 GLU A OE1 1 ATOM 4345 O OE2 A GLU A 1 545 ? 19.667 54.785 70.522 0.60 34.30 ? 586 GLU A OE2 1 ATOM 4346 O OE2 B GLU A 1 545 ? 17.913 56.764 70.930 0.40 29.38 ? 586 GLU A OE2 1 ATOM 4347 N N . LEU A 1 546 ? 14.465 54.692 66.450 1.00 19.33 ? 587 LEU A N 1 ATOM 4348 C CA . LEU A 1 546 ? 13.372 55.418 65.773 1.00 18.14 ? 587 LEU A CA 1 ATOM 4349 C C . LEU A 1 546 ? 12.034 55.188 66.478 1.00 19.22 ? 587 LEU A C 1 ATOM 4350 O O . LEU A 1 546 ? 11.190 56.106 66.601 1.00 20.42 ? 587 LEU A O 1 ATOM 4351 C CB . LEU A 1 546 ? 13.263 55.024 64.262 1.00 17.74 ? 587 LEU A CB 1 ATOM 4352 C CG . LEU A 1 546 ? 14.489 55.476 63.466 1.00 17.02 ? 587 LEU A CG 1 ATOM 4353 C CD1 . LEU A 1 546 ? 14.688 54.579 62.219 1.00 15.94 ? 587 LEU A CD1 1 ATOM 4354 C CD2 . LEU A 1 546 ? 14.282 56.967 63.082 1.00 20.02 ? 587 LEU A CD2 1 ATOM 4355 N N . ALA A 1 547 ? 11.814 53.964 66.943 1.00 18.17 ? 588 ALA A N 1 ATOM 4356 C CA . ALA A 1 547 ? 10.532 53.599 67.564 1.00 19.17 ? 588 ALA A CA 1 ATOM 4357 C C . ALA A 1 547 ? 10.464 53.951 69.074 1.00 19.40 ? 588 ALA A C 1 ATOM 4358 O O . ALA A 1 547 ? 9.357 54.012 69.596 1.00 21.08 ? 588 ALA A O 1 ATOM 4359 C CB . ALA A 1 547 ? 10.222 52.112 67.362 1.00 19.38 ? 588 ALA A CB 1 ATOM 4360 N N A ASN A 1 548 ? 11.597 54.099 69.743 0.60 20.25 ? 589 ASN A N 1 ATOM 4361 N N B ASN A 1 548 ? 11.617 54.206 69.698 0.40 20.13 ? 589 ASN A N 1 ATOM 4362 C CA A ASN A 1 548 ? 11.553 54.264 71.213 0.60 20.52 ? 589 ASN A CA 1 ATOM 4363 C CA B ASN A 1 548 ? 11.700 54.391 71.170 0.40 20.32 ? 589 ASN A CA 1 ATOM 4364 C C A ASN A 1 548 ? 11.976 55.618 71.737 0.60 21.57 ? 589 ASN A C 1 ATOM 4365 C C B ASN A 1 548 ? 12.361 55.648 71.728 0.40 21.25 ? 589 ASN A C 1 ATOM 4366 O O A ASN A 1 548 ? 11.508 56.031 72.828 0.60 21.01 ? 589 ASN A O 1 ATOM 4367 O O B ASN A 1 548 ? 12.258 55.891 72.934 0.40 20.74 ? 589 ASN A O 1 ATOM 4368 C CB A ASN A 1 548 ? 12.403 53.192 71.897 0.60 20.71 ? 589 ASN A CB 1 ATOM 4369 C CB B ASN A 1 548 ? 12.390 53.185 71.813 0.40 20.50 ? 589 ASN A CB 1 ATOM 4370 C CG A ASN A 1 548 ? 11.733 52.648 73.123 0.60 23.83 ? 589 ASN A CG 1 ATOM 4371 C CG B ASN A 1 548 ? 11.573 51.933 71.694 0.40 20.83 ? 589 ASN A CG 1 ATOM 4372 O OD1 A ASN A 1 548 ? 10.522 52.368 73.111 0.60 24.01 ? 589 ASN A OD1 1 ATOM 4373 O OD1 B ASN A 1 548 ? 10.600 51.743 72.424 0.40 23.44 ? 589 ASN A OD1 1 ATOM 4374 N ND2 A ASN A 1 548 ? 12.517 52.467 74.202 0.60 28.30 ? 589 ASN A ND2 1 ATOM 4375 N ND2 B ASN A 1 548 ? 11.981 51.045 70.786 0.40 22.98 ? 589 ASN A ND2 1 ATOM 4376 N N A SER A 1 549 ? 12.867 56.296 70.997 0.60 20.36 ? 590 SER A N 1 ATOM 4377 N N B SER A 1 549 ? 13.046 56.440 70.907 0.40 20.60 ? 590 SER A N 1 ATOM 4378 C CA A SER A 1 549 ? 13.403 57.597 71.446 0.60 21.06 ? 590 SER A CA 1 ATOM 4379 C CA B SER A 1 549 ? 13.612 57.692 71.443 0.40 21.64 ? 590 SER A CA 1 ATOM 4380 C C A SER A 1 549 ? 12.256 58.547 71.734 0.60 20.76 ? 590 SER A C 1 ATOM 4381 C C B SER A 1 549 ? 12.520 58.739 71.609 0.40 20.97 ? 590 SER A C 1 ATOM 4382 O O A SER A 1 549 ? 11.218 58.576 71.027 0.60 19.46 ? 590 SER A O 1 ATOM 4383 O O B SER A 1 549 ? 11.786 59.032 70.662 0.40 19.79 ? 590 SER A O 1 ATOM 4384 C CB A SER A 1 549 ? 14.363 58.212 70.407 0.60 20.55 ? 590 SER A CB 1 ATOM 4385 C CB B SER A 1 549 ? 14.715 58.239 70.543 0.40 21.47 ? 590 SER A CB 1 ATOM 4386 O OG A SER A 1 549 ? 15.029 59.389 70.863 0.60 19.25 ? 590 SER A OG 1 ATOM 4387 O OG B SER A 1 549 ? 15.767 57.305 70.435 0.40 24.36 ? 590 SER A OG 1 ATOM 4388 N N . ILE A 1 550 ? 12.417 59.322 72.807 1.00 20.97 ? 591 ILE A N 1 ATOM 4389 C CA A ILE A 1 550 ? 11.388 60.306 73.125 0.70 20.94 ? 591 ILE A CA 1 ATOM 4390 C CA B ILE A 1 550 ? 11.347 60.276 73.091 0.30 20.65 ? 591 ILE A CA 1 ATOM 4391 C C . ILE A 1 550 ? 11.261 61.376 72.031 1.00 20.03 ? 591 ILE A C 1 ATOM 4392 O O . ILE A 1 550 ? 10.147 61.649 71.498 1.00 20.68 ? 591 ILE A O 1 ATOM 4393 C CB A ILE A 1 550 ? 11.667 60.973 74.487 0.70 21.32 ? 591 ILE A CB 1 ATOM 4394 C CB B ILE A 1 550 ? 11.500 60.906 74.489 0.30 20.70 ? 591 ILE A CB 1 ATOM 4395 C CG1 A ILE A 1 550 ? 11.502 59.944 75.598 0.70 25.33 ? 591 ILE A CG1 1 ATOM 4396 C CG1 B ILE A 1 550 ? 11.835 59.831 75.514 0.30 21.16 ? 591 ILE A CG1 1 ATOM 4397 C CG2 A ILE A 1 550 ? 10.756 62.158 74.653 0.70 20.16 ? 591 ILE A CG2 1 ATOM 4398 C CG2 B ILE A 1 550 ? 10.229 61.651 74.868 0.30 20.98 ? 591 ILE A CG2 1 ATOM 4399 C CD1 A ILE A 1 550 ? 10.306 59.033 75.476 0.70 26.02 ? 591 ILE A CD1 1 ATOM 4400 C CD1 B ILE A 1 550 ? 12.065 60.393 76.889 0.30 14.70 ? 591 ILE A CD1 1 ATOM 4401 N N . VAL A 1 551 ? 12.414 61.972 71.711 1.00 21.34 ? 592 VAL A N 1 ATOM 4402 C CA . VAL A 1 551 ? 12.499 62.896 70.563 1.00 21.10 ? 592 VAL A CA 1 ATOM 4403 C C . VAL A 1 551 ? 12.989 62.064 69.372 1.00 20.30 ? 592 VAL A C 1 ATOM 4404 O O . VAL A 1 551 ? 13.979 61.339 69.485 1.00 20.87 ? 592 VAL A O 1 ATOM 4405 C CB . VAL A 1 551 ? 13.474 64.014 70.844 1.00 22.00 ? 592 VAL A CB 1 ATOM 4406 C CG1 . VAL A 1 551 ? 13.634 64.929 69.673 1.00 23.91 ? 592 VAL A CG1 1 ATOM 4407 C CG2 . VAL A 1 551 ? 12.981 64.870 72.042 1.00 25.68 ? 592 VAL A CG2 1 ATOM 4408 N N . GLN A 1 552 ? 12.315 62.179 68.233 1.00 20.55 ? 593 GLN A N 1 ATOM 4409 C CA . GLN A 1 552 ? 12.777 61.426 67.047 1.00 19.17 ? 593 GLN A CA 1 ATOM 4410 C C . GLN A 1 552 ? 14.253 61.708 66.776 1.00 19.51 ? 593 GLN A C 1 ATOM 4411 O O . GLN A 1 552 ? 14.706 62.872 66.838 1.00 19.89 ? 593 GLN A O 1 ATOM 4412 C CB . GLN A 1 552 ? 11.918 61.811 65.827 1.00 18.80 ? 593 GLN A CB 1 ATOM 4413 C CG . GLN A 1 552 ? 10.581 61.183 65.905 1.00 22.53 ? 593 GLN A CG 1 ATOM 4414 C CD . GLN A 1 552 ? 9.738 61.661 64.811 1.00 28.42 ? 593 GLN A CD 1 ATOM 4415 O OE1 . GLN A 1 552 ? 9.997 62.694 64.229 1.00 42.01 ? 593 GLN A OE1 1 ATOM 4416 N NE2 . GLN A 1 552 ? 8.727 60.909 64.493 1.00 40.70 ? 593 GLN A NE2 1 ATOM 4417 N N . PRO A 1 553 ? 15.013 60.663 66.414 1.00 19.61 ? 594 PRO A N 1 ATOM 4418 C CA . PRO A 1 553 ? 16.476 60.810 66.304 1.00 20.01 ? 594 PRO A CA 1 ATOM 4419 C C . PRO A 1 553 ? 16.887 61.305 64.894 1.00 21.49 ? 594 PRO A C 1 ATOM 4420 O O . PRO A 1 553 ? 17.672 60.636 64.213 1.00 21.01 ? 594 PRO A O 1 ATOM 4421 C CB . PRO A 1 553 ? 16.985 59.381 66.544 1.00 21.13 ? 594 PRO A CB 1 ATOM 4422 C CG . PRO A 1 553 ? 15.897 58.521 65.992 1.00 21.40 ? 594 PRO A CG 1 ATOM 4423 C CD . PRO A 1 553 ? 14.598 59.260 66.382 1.00 20.08 ? 594 PRO A CD 1 ATOM 4424 N N . PHE A 1 554 ? 16.350 62.463 64.497 1.00 19.09 ? 595 PHE A N 1 ATOM 4425 C CA . PHE A 1 554 ? 16.686 63.101 63.229 1.00 20.41 ? 595 PHE A CA 1 ATOM 4426 C C . PHE A 1 554 ? 17.369 64.431 63.530 1.00 20.66 ? 595 PHE A C 1 ATOM 4427 O O . PHE A 1 554 ? 16.919 65.185 64.420 1.00 22.54 ? 595 PHE A O 1 ATOM 4428 C CB . PHE A 1 554 ? 15.391 63.467 62.460 1.00 18.94 ? 595 PHE A CB 1 ATOM 4429 C CG . PHE A 1 554 ? 14.581 62.276 61.957 1.00 18.72 ? 595 PHE A CG 1 ATOM 4430 C CD1 . PHE A 1 554 ? 15.164 61.045 61.677 1.00 19.18 ? 595 PHE A CD1 1 ATOM 4431 C CD2 . PHE A 1 554 ? 13.219 62.441 61.723 1.00 20.72 ? 595 PHE A CD2 1 ATOM 4432 C CE1 . PHE A 1 554 ? 14.369 60.002 61.164 1.00 19.73 ? 595 PHE A CE1 1 ATOM 4433 C CE2 . PHE A 1 554 ? 12.418 61.383 61.227 1.00 19.22 ? 595 PHE A CE2 1 ATOM 4434 C CZ . PHE A 1 554 ? 13.006 60.164 60.944 1.00 17.68 ? 595 PHE A CZ 1 ATOM 4435 N N . ASP A 1 555 ? 18.408 64.757 62.779 1.00 20.15 ? 596 ASP A N 1 ATOM 4436 C CA . ASP A 1 555 ? 19.057 66.056 62.926 1.00 19.65 ? 596 ASP A CA 1 ATOM 4437 C C . ASP A 1 555 ? 18.876 66.885 61.649 1.00 20.26 ? 596 ASP A C 1 ATOM 4438 O O . ASP A 1 555 ? 19.531 66.627 60.628 1.00 20.12 ? 596 ASP A O 1 ATOM 4439 C CB . ASP A 1 555 ? 20.553 65.902 63.250 1.00 18.53 ? 596 ASP A CB 1 ATOM 4440 C CG . ASP A 1 555 ? 21.169 67.215 63.752 1.00 24.50 ? 596 ASP A CG 1 ATOM 4441 O OD1 . ASP A 1 555 ? 20.607 68.299 63.493 1.00 23.29 ? 596 ASP A OD1 1 ATOM 4442 O OD2 . ASP A 1 555 ? 22.251 67.155 64.374 1.00 27.13 ? 596 ASP A OD2 1 ATOM 4443 N N . CYS A 1 556 ? 17.943 67.843 61.698 1.00 19.04 ? 597 CYS A N 1 ATOM 4444 C CA . CYS A 1 556 ? 17.688 68.665 60.497 1.00 19.82 ? 597 CYS A CA 1 ATOM 4445 C C . CYS A 1 556 ? 18.918 69.427 60.016 1.00 19.80 ? 597 CYS A C 1 ATOM 4446 O O . CYS A 1 556 ? 19.052 69.742 58.829 1.00 20.09 ? 597 CYS A O 1 ATOM 4447 C CB . CYS A 1 556 ? 16.547 69.649 60.750 1.00 19.51 ? 597 CYS A CB 1 ATOM 4448 S SG . CYS A 1 556 ? 16.849 70.727 62.227 1.00 7.08 ? 597 CYS A SG 1 ATOM 4449 N N . ARG A 1 557 ? 19.859 69.706 60.910 1.00 21.13 ? 598 ARG A N 1 ATOM 4450 C CA . ARG A 1 557 ? 21.060 70.435 60.497 1.00 21.18 ? 598 ARG A CA 1 ATOM 4451 C C . ARG A 1 557 ? 21.889 69.653 59.460 1.00 21.46 ? 598 ARG A C 1 ATOM 4452 O O . ARG A 1 557 ? 22.608 70.246 58.633 1.00 22.49 ? 598 ARG A O 1 ATOM 4453 C CB . ARG A 1 557 ? 21.917 70.758 61.729 1.00 22.09 ? 598 ARG A CB 1 ATOM 4454 C CG . ARG A 1 557 ? 21.186 71.703 62.674 1.00 21.54 ? 598 ARG A CG 1 ATOM 4455 C CD . ARG A 1 557 ? 21.983 71.874 63.987 1.00 23.35 ? 598 ARG A CD 1 ATOM 4456 N NE . ARG A 1 557 ? 22.096 70.598 64.644 1.00 23.53 ? 598 ARG A NE 1 ATOM 4457 C CZ . ARG A 1 557 ? 22.717 70.428 65.816 1.00 29.22 ? 598 ARG A CZ 1 ATOM 4458 N NH1 . ARG A 1 557 ? 23.259 71.489 66.406 1.00 28.05 ? 598 ARG A NH1 1 ATOM 4459 N NH2 . ARG A 1 557 ? 22.781 69.218 66.382 1.00 27.24 ? 598 ARG A NH2 1 ATOM 4460 N N . ASP A 1 558 ? 21.802 68.328 59.512 1.00 20.07 ? 599 ASP A N 1 ATOM 4461 C CA . ASP A 1 558 ? 22.585 67.533 58.564 1.00 19.69 ? 599 ASP A CA 1 ATOM 4462 C C . ASP A 1 558 ? 21.968 67.704 57.175 1.00 19.01 ? 599 ASP A C 1 ATOM 4463 O O . ASP A 1 558 ? 22.685 67.608 56.191 1.00 20.07 ? 599 ASP A O 1 ATOM 4464 C CB . ASP A 1 558 ? 22.575 66.070 58.966 1.00 19.46 ? 599 ASP A CB 1 ATOM 4465 C CG . ASP A 1 558 ? 23.533 65.793 60.147 1.00 23.71 ? 599 ASP A CG 1 ATOM 4466 O OD1 . ASP A 1 558 ? 24.580 66.462 60.216 1.00 34.24 ? 599 ASP A OD1 1 ATOM 4467 O OD2 . ASP A 1 558 ? 23.248 64.969 61.028 1.00 23.10 ? 599 ASP A OD2 1 ATOM 4468 N N . TYR A 1 559 ? 20.660 67.946 57.098 1.00 19.02 ? 600 TYR A N 1 ATOM 4469 C CA . TYR A 1 559 ? 20.098 68.214 55.766 1.00 16.96 ? 600 TYR A CA 1 ATOM 4470 C C . TYR A 1 559 ? 20.625 69.535 55.254 1.00 17.69 ? 600 TYR A C 1 ATOM 4471 O O . TYR A 1 559 ? 20.910 69.691 54.060 1.00 18.33 ? 600 TYR A O 1 ATOM 4472 C CB . TYR A 1 559 ? 18.550 68.280 55.789 1.00 17.22 ? 600 TYR A CB 1 ATOM 4473 C CG . TYR A 1 559 ? 17.910 67.291 54.775 1.00 16.94 ? 600 TYR A CG 1 ATOM 4474 C CD1 . TYR A 1 559 ? 18.270 67.335 53.418 1.00 15.71 ? 600 TYR A CD1 1 ATOM 4475 C CD2 . TYR A 1 559 ? 16.950 66.370 55.171 1.00 16.62 ? 600 TYR A CD2 1 ATOM 4476 C CE1 . TYR A 1 559 ? 17.686 66.450 52.472 1.00 16.74 ? 600 TYR A CE1 1 ATOM 4477 C CE2 . TYR A 1 559 ? 16.375 65.449 54.245 1.00 16.96 ? 600 TYR A CE2 1 ATOM 4478 C CZ . TYR A 1 559 ? 16.752 65.521 52.897 1.00 17.70 ? 600 TYR A CZ 1 ATOM 4479 O OH . TYR A 1 559 ? 16.165 64.635 51.999 1.00 17.05 ? 600 TYR A OH 1 ATOM 4480 N N . ALA A 1 560 ? 20.795 70.522 56.148 1.00 17.42 ? 601 ALA A N 1 ATOM 4481 C CA . ALA A 1 560 ? 21.266 71.832 55.674 1.00 18.57 ? 601 ALA A CA 1 ATOM 4482 C C . ALA A 1 560 ? 22.677 71.720 55.054 1.00 19.56 ? 601 ALA A C 1 ATOM 4483 O O . ALA A 1 560 ? 22.944 72.319 53.993 1.00 19.07 ? 601 ALA A O 1 ATOM 4484 C CB . ALA A 1 560 ? 21.263 72.841 56.846 1.00 18.47 ? 601 ALA A CB 1 ATOM 4485 N N . VAL A 1 561 ? 23.546 70.942 55.691 1.00 19.77 ? 602 VAL A N 1 ATOM 4486 C CA . VAL A 1 561 ? 24.893 70.751 55.187 1.00 20.40 ? 602 VAL A CA 1 ATOM 4487 C C . VAL A 1 561 ? 24.869 70.114 53.778 1.00 20.46 ? 602 VAL A C 1 ATOM 4488 O O . VAL A 1 561 ? 25.506 70.638 52.853 1.00 21.51 ? 602 VAL A O 1 ATOM 4489 C CB . VAL A 1 561 ? 25.699 69.873 56.126 1.00 22.27 ? 602 VAL A CB 1 ATOM 4490 C CG1 . VAL A 1 561 ? 27.033 69.509 55.467 1.00 23.21 ? 602 VAL A CG1 1 ATOM 4491 C CG2 . VAL A 1 561 ? 25.926 70.700 57.392 1.00 23.87 ? 602 VAL A CG2 1 ATOM 4492 N N . VAL A 1 562 ? 24.074 69.054 53.591 1.00 19.34 ? 603 VAL A N 1 ATOM 4493 C CA . VAL A 1 562 ? 24.086 68.411 52.270 1.00 18.76 ? 603 VAL A CA 1 ATOM 4494 C C . VAL A 1 562 ? 23.429 69.276 51.219 1.00 18.86 ? 603 VAL A C 1 ATOM 4495 O O . VAL A 1 562 ? 23.849 69.257 50.054 1.00 19.00 ? 603 VAL A O 1 ATOM 4496 C CB . VAL A 1 562 ? 23.611 66.946 52.248 1.00 21.78 ? 603 VAL A CB 1 ATOM 4497 C CG1 . VAL A 1 562 ? 24.259 66.101 53.378 1.00 20.17 ? 603 VAL A CG1 1 ATOM 4498 C CG2 . VAL A 1 562 ? 22.167 66.865 52.291 1.00 24.74 ? 603 VAL A CG2 1 ATOM 4499 N N . LEU A 1 563 ? 22.380 70.018 51.586 1.00 17.43 ? 604 LEU A N 1 ATOM 4500 C CA . LEU A 1 563 ? 21.706 70.867 50.595 1.00 18.29 ? 604 LEU A CA 1 ATOM 4501 C C . LEU A 1 563 ? 22.705 71.863 50.005 1.00 18.55 ? 604 LEU A C 1 ATOM 4502 O O . LEU A 1 563 ? 22.661 72.142 48.797 1.00 19.28 ? 604 LEU A O 1 ATOM 4503 C CB . LEU A 1 563 ? 20.517 71.604 51.199 1.00 17.53 ? 604 LEU A CB 1 ATOM 4504 C CG . LEU A 1 563 ? 19.326 70.699 51.495 1.00 16.94 ? 604 LEU A CG 1 ATOM 4505 C CD1 . LEU A 1 563 ? 18.302 71.460 52.328 1.00 17.33 ? 604 LEU A CD1 1 ATOM 4506 C CD2 . LEU A 1 563 ? 18.733 70.224 50.110 1.00 18.91 ? 604 LEU A CD2 1 ATOM 4507 N N . ARG A 1 564 ? 23.612 72.389 50.835 1.00 19.25 ? 605 ARG A N 1 ATOM 4508 C CA . ARG A 1 564 ? 24.612 73.323 50.320 1.00 19.79 ? 605 ARG A CA 1 ATOM 4509 C C . ARG A 1 564 ? 25.596 72.627 49.377 1.00 19.99 ? 605 ARG A C 1 ATOM 4510 O O . ARG A 1 564 ? 25.884 73.144 48.283 1.00 20.46 ? 605 ARG A O 1 ATOM 4511 C CB . ARG A 1 564 ? 25.375 73.993 51.472 1.00 20.00 ? 605 ARG A CB 1 ATOM 4512 C CG . ARG A 1 564 ? 26.527 74.862 50.988 1.00 23.71 ? 605 ARG A CG 1 ATOM 4513 C CD . ARG A 1 564 ? 26.037 76.025 50.075 1.00 28.36 ? 605 ARG A CD 1 ATOM 4514 N NE . ARG A 1 564 ? 27.172 76.819 49.599 1.00 31.56 ? 605 ARG A NE 1 ATOM 4515 C CZ . ARG A 1 564 ? 27.641 77.885 50.252 1.00 38.12 ? 605 ARG A CZ 1 ATOM 4516 N NH1 . ARG A 1 564 ? 27.061 78.290 51.394 1.00 35.59 ? 605 ARG A NH1 1 ATOM 4517 N NH2 . ARG A 1 564 ? 28.694 78.543 49.766 1.00 38.90 ? 605 ARG A NH2 1 ATOM 4518 N N . LYS A 1 565 ? 26.050 71.425 49.754 1.00 19.72 ? 606 LYS A N 1 ATOM 4519 C CA . LYS A 1 565 ? 26.867 70.606 48.881 1.00 19.99 ? 606 LYS A CA 1 ATOM 4520 C C . LYS A 1 565 ? 26.161 70.392 47.530 1.00 20.16 ? 606 LYS A C 1 ATOM 4521 O O . LYS A 1 565 ? 26.753 70.554 46.470 1.00 19.32 ? 606 LYS A O 1 ATOM 4522 C CB . LYS A 1 565 ? 27.152 69.249 49.566 1.00 21.14 ? 606 LYS A CB 1 ATOM 4523 C CG . LYS A 1 565 ? 28.034 68.322 48.753 1.00 23.68 ? 606 LYS A CG 1 ATOM 4524 C CD . LYS A 1 565 ? 28.310 66.987 49.459 1.00 26.91 ? 606 LYS A CD 1 ATOM 4525 C CE . LYS A 1 565 ? 27.050 66.178 49.658 1.00 26.72 ? 606 LYS A CE 1 ATOM 4526 N NZ . LYS A 1 565 ? 27.307 64.993 50.512 1.00 28.83 ? 606 LYS A NZ 1 ATOM 4527 N N . TYR A 1 566 ? 24.874 70.005 47.563 1.00 17.96 ? 607 TYR A N 1 ATOM 4528 C CA . TYR A 1 566 ? 24.183 69.728 46.282 1.00 17.38 ? 607 TYR A CA 1 ATOM 4529 C C . TYR A 1 566 ? 23.974 71.009 45.488 1.00 17.17 ? 607 TYR A C 1 ATOM 4530 O O . TYR A 1 566 ? 24.049 70.948 44.262 1.00 17.57 ? 607 TYR A O 1 ATOM 4531 C CB . TYR A 1 566 ? 22.818 69.101 46.558 1.00 17.45 ? 607 TYR A CB 1 ATOM 4532 C CG . TYR A 1 566 ? 22.882 67.761 47.289 1.00 16.75 ? 607 TYR A CG 1 ATOM 4533 C CD1 . TYR A 1 566 ? 24.040 66.953 47.239 1.00 16.79 ? 607 TYR A CD1 1 ATOM 4534 C CD2 . TYR A 1 566 ? 21.775 67.318 48.039 1.00 18.64 ? 607 TYR A CD2 1 ATOM 4535 C CE1 . TYR A 1 566 ? 24.068 65.676 47.912 1.00 19.25 ? 607 TYR A CE1 1 ATOM 4536 C CE2 . TYR A 1 566 ? 21.776 66.080 48.711 1.00 18.37 ? 607 TYR A CE2 1 ATOM 4537 C CZ . TYR A 1 566 ? 22.929 65.269 48.655 1.00 19.53 ? 607 TYR A CZ 1 ATOM 4538 O OH . TYR A 1 566 ? 22.900 64.053 49.348 1.00 20.51 ? 607 TYR A OH 1 ATOM 4539 N N . ALA A 1 567 ? 23.712 72.129 46.161 1.00 17.84 ? 608 ALA A N 1 ATOM 4540 C CA . ALA A 1 567 ? 23.553 73.404 45.433 1.00 17.54 ? 608 ALA A CA 1 ATOM 4541 C C . ALA A 1 567 ? 24.873 73.774 44.751 1.00 18.73 ? 608 ALA A C 1 ATOM 4542 O O . ALA A 1 567 ? 24.881 74.184 43.563 1.00 19.56 ? 608 ALA A O 1 ATOM 4543 C CB . ALA A 1 567 ? 23.130 74.520 46.430 1.00 18.34 ? 608 ALA A CB 1 ATOM 4544 N N . ASP A 1 568 ? 25.980 73.657 45.496 1.00 20.42 ? 609 ASP A N 1 ATOM 4545 C CA . ASP A 1 568 ? 27.318 73.913 44.884 1.00 21.25 ? 609 ASP A CA 1 ATOM 4546 C C . ASP A 1 568 ? 27.532 73.011 43.634 1.00 20.79 ? 609 ASP A C 1 ATOM 4547 O O . ASP A 1 568 ? 28.029 73.461 42.571 1.00 20.22 ? 609 ASP A O 1 ATOM 4548 C CB . ASP A 1 568 ? 28.449 73.623 45.869 1.00 22.54 ? 609 ASP A CB 1 ATOM 4549 C CG . ASP A 1 568 ? 28.546 74.618 46.998 1.00 27.30 ? 609 ASP A CG 1 ATOM 4550 O OD1 . ASP A 1 568 ? 27.979 75.706 46.910 1.00 27.69 ? 609 ASP A OD1 1 ATOM 4551 O OD2 . ASP A 1 568 ? 29.246 74.278 47.993 1.00 31.84 ? 609 ASP A OD2 1 ATOM 4552 N N . LYS A 1 569 ? 27.114 71.746 43.747 1.00 19.21 ? 610 LYS A N 1 ATOM 4553 C CA A LYS A 1 569 ? 27.335 70.802 42.669 0.70 19.83 ? 610 LYS A CA 1 ATOM 4554 C CA B LYS A 1 569 ? 27.332 70.799 42.682 0.30 19.74 ? 610 LYS A CA 1 ATOM 4555 C C . LYS A 1 569 ? 26.528 71.191 41.440 1.00 19.82 ? 610 LYS A C 1 ATOM 4556 O O . LYS A 1 569 ? 27.054 71.204 40.316 1.00 21.23 ? 610 LYS A O 1 ATOM 4557 C CB A LYS A 1 569 ? 27.012 69.352 43.102 0.70 20.22 ? 610 LYS A CB 1 ATOM 4558 C CB B LYS A 1 569 ? 26.964 69.396 43.171 0.30 19.54 ? 610 LYS A CB 1 ATOM 4559 C CG A LYS A 1 569 ? 27.023 68.314 41.919 0.70 21.39 ? 610 LYS A CG 1 ATOM 4560 C CG B LYS A 1 569 ? 27.619 68.260 42.401 0.30 20.01 ? 610 LYS A CG 1 ATOM 4561 C CD A LYS A 1 569 ? 26.287 66.996 42.296 0.70 24.28 ? 610 LYS A CD 1 ATOM 4562 C CD B LYS A 1 569 ? 26.992 66.945 42.838 0.30 18.87 ? 610 LYS A CD 1 ATOM 4563 C CE A LYS A 1 569 ? 26.362 65.908 41.183 0.70 25.91 ? 610 LYS A CE 1 ATOM 4564 C CE B LYS A 1 569 ? 27.404 65.756 41.996 0.30 20.67 ? 610 LYS A CE 1 ATOM 4565 N NZ A LYS A 1 569 ? 25.210 65.782 40.217 0.70 27.76 ? 610 LYS A NZ 1 ATOM 4566 N NZ B LYS A 1 569 ? 26.320 64.733 42.005 0.30 21.02 ? 610 LYS A NZ 1 ATOM 4567 N N . ILE A 1 570 ? 25.241 71.500 41.625 1.00 18.33 ? 611 ILE A N 1 ATOM 4568 C CA . ILE A 1 570 ? 24.431 71.772 40.434 1.00 17.92 ? 611 ILE A CA 1 ATOM 4569 C C . ILE A 1 570 ? 24.829 73.143 39.808 1.00 18.62 ? 611 ILE A C 1 ATOM 4570 O O . ILE A 1 570 ? 24.816 73.282 38.575 1.00 19.14 ? 611 ILE A O 1 ATOM 4571 C CB . ILE A 1 570 ? 22.906 71.664 40.772 1.00 18.99 ? 611 ILE A CB 1 ATOM 4572 C CG1 . ILE A 1 570 ? 22.052 71.628 39.508 1.00 20.86 ? 611 ILE A CG1 1 ATOM 4573 C CG2 . ILE A 1 570 ? 22.460 72.791 41.727 1.00 18.29 ? 611 ILE A CG2 1 ATOM 4574 C CD1 . ILE A 1 570 ? 22.276 70.377 38.715 1.00 20.45 ? 611 ILE A CD1 1 ATOM 4575 N N . TYR A 1 571 ? 25.193 74.107 40.658 1.00 18.69 ? 612 TYR A N 1 ATOM 4576 C CA . TYR A 1 571 ? 25.688 75.374 40.157 1.00 20.91 ? 612 TYR A CA 1 ATOM 4577 C C . TYR A 1 571 ? 26.957 75.136 39.299 1.00 20.94 ? 612 TYR A C 1 ATOM 4578 O O . TYR A 1 571 ? 27.088 75.685 38.182 1.00 20.83 ? 612 TYR A O 1 ATOM 4579 C CB . TYR A 1 571 ? 25.998 76.321 41.336 1.00 20.01 ? 612 TYR A CB 1 ATOM 4580 C CG . TYR A 1 571 ? 26.902 77.463 40.939 1.00 26.26 ? 612 TYR A CG 1 ATOM 4581 C CD1 . TYR A 1 571 ? 26.395 78.583 40.293 1.00 28.70 ? 612 TYR A CD1 1 ATOM 4582 C CD2 . TYR A 1 571 ? 28.273 77.357 41.159 1.00 31.19 ? 612 TYR A CD2 1 ATOM 4583 C CE1 . TYR A 1 571 ? 27.297 79.646 39.912 1.00 31.57 ? 612 TYR A CE1 1 ATOM 4584 C CE2 . TYR A 1 571 ? 29.149 78.370 40.795 1.00 33.85 ? 612 TYR A CE2 1 ATOM 4585 C CZ . TYR A 1 571 ? 28.651 79.486 40.165 1.00 36.32 ? 612 TYR A CZ 1 ATOM 4586 O OH . TYR A 1 571 ? 29.564 80.468 39.806 1.00 44.03 ? 612 TYR A OH 1 ATOM 4587 N N . SER A 1 572 ? 27.838 74.262 39.778 1.00 22.00 ? 613 SER A N 1 ATOM 4588 C CA . SER A 1 572 ? 29.076 73.977 39.041 1.00 22.95 ? 613 SER A CA 1 ATOM 4589 C C . SER A 1 572 ? 28.785 73.357 37.689 1.00 23.67 ? 613 SER A C 1 ATOM 4590 O O . SER A 1 572 ? 29.491 73.630 36.723 1.00 24.64 ? 613 SER A O 1 ATOM 4591 C CB . SER A 1 572 ? 30.029 73.092 39.843 1.00 24.45 ? 613 SER A CB 1 ATOM 4592 O OG A SER A 1 572 ? 30.483 73.789 41.004 0.50 23.40 ? 613 SER A OG 1 ATOM 4593 O OG B SER A 1 572 ? 29.568 71.752 39.854 0.50 26.22 ? 613 SER A OG 1 ATOM 4594 N N . ILE A 1 573 ? 27.742 72.516 37.603 1.00 21.32 ? 614 ILE A N 1 ATOM 4595 C CA . ILE A 1 573 ? 27.396 71.946 36.331 1.00 21.00 ? 614 ILE A CA 1 ATOM 4596 C C . ILE A 1 573 ? 26.964 73.062 35.374 1.00 21.42 ? 614 ILE A C 1 ATOM 4597 O O . ILE A 1 573 ? 27.356 73.104 34.199 1.00 22.47 ? 614 ILE A O 1 ATOM 4598 C CB . ILE A 1 573 ? 26.274 70.870 36.502 1.00 21.42 ? 614 ILE A CB 1 ATOM 4599 C CG1 . ILE A 1 573 ? 26.896 69.626 37.191 1.00 22.69 ? 614 ILE A CG1 1 ATOM 4600 C CG2 . ILE A 1 573 ? 25.639 70.539 35.111 1.00 22.01 ? 614 ILE A CG2 1 ATOM 4601 C CD1 . ILE A 1 573 ? 25.845 68.587 37.650 1.00 22.50 ? 614 ILE A CD1 1 ATOM 4602 N N . SER A 1 574 ? 26.130 73.964 35.879 1.00 21.70 ? 615 SER A N 1 ATOM 4603 C CA . SER A 1 574 ? 25.572 75.007 35.035 1.00 21.96 ? 615 SER A CA 1 ATOM 4604 C C . SER A 1 574 ? 26.668 75.931 34.528 1.00 23.67 ? 615 SER A C 1 ATOM 4605 O O . SER A 1 574 ? 26.629 76.387 33.379 1.00 23.46 ? 615 SER A O 1 ATOM 4606 C CB . SER A 1 574 ? 24.567 75.816 35.840 1.00 21.85 ? 615 SER A CB 1 ATOM 4607 O OG . SER A 1 574 ? 23.880 76.719 34.980 1.00 22.37 ? 615 SER A OG 1 ATOM 4608 N N . MET A 1 575 ? 27.638 76.167 35.400 1.00 23.78 ? 616 MET A N 1 ATOM 4609 C CA . MET A 1 575 ? 28.725 77.148 35.127 1.00 26.59 ? 616 MET A CA 1 ATOM 4610 C C . MET A 1 575 ? 29.722 76.670 34.068 1.00 27.41 ? 616 MET A C 1 ATOM 4611 O O . MET A 1 575 ? 30.642 77.426 33.697 1.00 28.98 ? 616 MET A O 1 ATOM 4612 C CB . MET A 1 575 ? 29.407 77.507 36.420 1.00 27.65 ? 616 MET A CB 1 ATOM 4613 C CG . MET A 1 575 ? 28.657 78.596 37.161 1.00 32.27 ? 616 MET A CG 1 ATOM 4614 S SD . MET A 1 575 ? 28.517 80.205 36.271 1.00 14.98 ? 616 MET A SD 1 ATOM 4615 C CE . MET A 1 575 ? 30.230 80.706 36.139 1.00 40.24 ? 616 MET A CE 1 ATOM 4616 N N . LYS A 1 576 ? 29.545 75.452 33.568 1.00 27.95 ? 617 LYS A N 1 ATOM 4617 C CA . LYS A 1 576 ? 30.241 74.987 32.359 1.00 29.27 ? 617 LYS A CA 1 ATOM 4618 C C . LYS A 1 576 ? 29.717 75.715 31.107 1.00 28.36 ? 617 LYS A C 1 ATOM 4619 O O . LYS A 1 576 ? 30.367 75.646 30.043 1.00 28.31 ? 617 LYS A O 1 ATOM 4620 C CB . LYS A 1 576 ? 30.100 73.469 32.191 1.00 30.82 ? 617 LYS A CB 1 ATOM 4621 C CG . LYS A 1 576 ? 30.590 72.643 33.386 1.00 34.50 ? 617 LYS A CG 1 ATOM 4622 C CD . LYS A 1 576 ? 32.095 72.421 33.411 1.00 43.43 ? 617 LYS A CD 1 ATOM 4623 C CE . LYS A 1 576 ? 32.508 71.490 34.605 1.00 46.52 ? 617 LYS A CE 1 ATOM 4624 N NZ . LYS A 1 576 ? 32.469 72.155 35.977 1.00 48.02 ? 617 LYS A NZ 1 ATOM 4625 N N . HIS A 1 577 ? 28.598 76.442 31.246 1.00 26.09 ? 618 HIS A N 1 ATOM 4626 C CA . HIS A 1 577 ? 27.923 77.163 30.134 1.00 25.52 ? 618 HIS A CA 1 ATOM 4627 C C . HIS A 1 577 ? 27.761 78.662 30.456 1.00 25.29 ? 618 HIS A C 1 ATOM 4628 O O . HIS A 1 577 ? 26.626 79.182 30.443 1.00 24.13 ? 618 HIS A O 1 ATOM 4629 C CB . HIS A 1 577 ? 26.536 76.560 29.895 1.00 25.01 ? 618 HIS A CB 1 ATOM 4630 C CG . HIS A 1 577 ? 26.555 75.068 29.695 1.00 26.17 ? 618 HIS A CG 1 ATOM 4631 N ND1 . HIS A 1 577 ? 26.299 74.167 30.719 1.00 30.85 ? 618 HIS A ND1 1 ATOM 4632 C CD2 . HIS A 1 577 ? 26.806 74.322 28.596 1.00 25.90 ? 618 HIS A CD2 1 ATOM 4633 C CE1 . HIS A 1 577 ? 26.395 72.929 30.257 1.00 28.41 ? 618 HIS A CE1 1 ATOM 4634 N NE2 . HIS A 1 577 ? 26.692 72.996 28.969 1.00 31.54 ? 618 HIS A NE2 1 ATOM 4635 N N . PRO A 1 578 ? 28.899 79.378 30.707 1.00 25.42 ? 619 PRO A N 1 ATOM 4636 C CA . PRO A 1 578 ? 28.794 80.763 31.185 1.00 25.16 ? 619 PRO A CA 1 ATOM 4637 C C . PRO A 1 578 ? 28.127 81.689 30.199 1.00 25.73 ? 619 PRO A C 1 ATOM 4638 O O . PRO A 1 578 ? 27.350 82.545 30.643 1.00 25.47 ? 619 PRO A O 1 ATOM 4639 C CB . PRO A 1 578 ? 30.264 81.193 31.431 1.00 26.47 ? 619 PRO A CB 1 ATOM 4640 C CG . PRO A 1 578 ? 31.055 80.236 30.548 1.00 27.13 ? 619 PRO A CG 1 ATOM 4641 C CD . PRO A 1 578 ? 30.284 78.920 30.666 1.00 26.37 ? 619 PRO A CD 1 ATOM 4642 N N . GLN A 1 579 ? 28.354 81.510 28.888 1.00 26.57 ? 620 GLN A N 1 ATOM 4643 C CA A GLN A 1 579 ? 27.698 82.357 27.889 0.50 26.73 ? 620 GLN A CA 1 ATOM 4644 C CA B GLN A 1 579 ? 27.690 82.380 27.912 0.50 26.32 ? 620 GLN A CA 1 ATOM 4645 C C . GLN A 1 579 ? 26.178 82.236 27.966 1.00 26.30 ? 620 GLN A C 1 ATOM 4646 O O . GLN A 1 579 ? 25.463 83.232 27.954 1.00 25.96 ? 620 GLN A O 1 ATOM 4647 C CB A GLN A 1 579 ? 28.192 82.034 26.467 0.50 28.06 ? 620 GLN A CB 1 ATOM 4648 C CB B GLN A 1 579 ? 28.155 82.144 26.474 0.50 27.33 ? 620 GLN A CB 1 ATOM 4649 C CG A GLN A 1 579 ? 29.653 82.409 26.251 0.50 30.32 ? 620 GLN A CG 1 ATOM 4650 C CG B GLN A 1 579 ? 27.389 83.009 25.471 0.50 27.61 ? 620 GLN A CG 1 ATOM 4651 C CD A GLN A 1 579 ? 30.196 82.080 24.851 0.50 35.81 ? 620 GLN A CD 1 ATOM 4652 C CD B GLN A 1 579 ? 27.703 84.491 25.626 0.50 29.44 ? 620 GLN A CD 1 ATOM 4653 O OE1 A GLN A 1 579 ? 29.526 81.452 24.027 0.50 37.89 ? 620 GLN A OE1 1 ATOM 4654 O OE1 B GLN A 1 579 ? 28.766 84.932 25.203 0.50 34.17 ? 620 GLN A OE1 1 ATOM 4655 N NE2 A GLN A 1 579 ? 31.426 82.508 24.590 0.50 37.06 ? 620 GLN A NE2 1 ATOM 4656 N NE2 B GLN A 1 579 ? 26.799 85.260 26.258 0.50 23.95 ? 620 GLN A NE2 1 ATOM 4657 N N . GLU A 1 580 ? 25.687 80.997 28.054 1.00 23.89 ? 621 GLU A N 1 ATOM 4658 C CA . GLU A 1 580 ? 24.253 80.828 28.107 1.00 22.48 ? 621 GLU A CA 1 ATOM 4659 C C . GLU A 1 580 ? 23.642 81.367 29.395 1.00 21.62 ? 621 GLU A C 1 ATOM 4660 O O . GLU A 1 580 ? 22.502 81.861 29.408 1.00 23.21 ? 621 GLU A O 1 ATOM 4661 C CB . GLU A 1 580 ? 23.911 79.350 27.961 1.00 23.32 ? 621 GLU A CB 1 ATOM 4662 C CG . GLU A 1 580 ? 24.141 78.807 26.526 1.00 27.84 ? 621 GLU A CG 1 ATOM 4663 C CD . GLU A 1 580 ? 25.588 78.697 26.111 1.00 34.42 ? 621 GLU A CD 1 ATOM 4664 O OE1 . GLU A 1 580 ? 26.514 78.494 26.952 1.00 33.83 ? 621 GLU A OE1 1 ATOM 4665 O OE2 . GLU A 1 580 ? 25.805 78.834 24.887 1.00 41.78 ? 621 GLU A OE2 1 ATOM 4666 N N . MET A 1 581 ? 24.371 81.239 30.509 1.00 21.07 ? 622 MET A N 1 ATOM 4667 C CA . MET A 1 581 ? 23.843 81.768 31.766 1.00 21.36 ? 622 MET A CA 1 ATOM 4668 C C . MET A 1 581 ? 23.715 83.304 31.665 1.00 22.48 ? 622 MET A C 1 ATOM 4669 O O . MET A 1 581 ? 22.760 83.885 32.201 1.00 22.11 ? 622 MET A O 1 ATOM 4670 C CB . MET A 1 581 ? 24.689 81.363 32.977 1.00 21.63 ? 622 MET A CB 1 ATOM 4671 C CG . MET A 1 581 ? 24.661 79.840 33.221 1.00 20.68 ? 622 MET A CG 1 ATOM 4672 S SD . MET A 1 581 ? 25.616 79.378 34.707 1.00 8.08 ? 622 MET A SD 1 ATOM 4673 C CE . MET A 1 581 ? 24.768 80.261 36.013 1.00 22.56 ? 622 MET A CE 1 ATOM 4674 N N . LYS A 1 582 ? 24.656 83.923 30.930 1.00 22.81 ? 623 LYS A N 1 ATOM 4675 C CA . LYS A 1 582 ? 24.593 85.383 30.696 1.00 23.95 ? 623 LYS A CA 1 ATOM 4676 C C . LYS A 1 582 ? 23.408 85.720 29.789 1.00 23.57 ? 623 LYS A C 1 ATOM 4677 O O . LYS A 1 582 ? 22.572 86.562 30.124 1.00 24.05 ? 623 LYS A O 1 ATOM 4678 C CB . LYS A 1 582 ? 25.916 85.919 30.102 1.00 25.23 ? 623 LYS A CB 1 ATOM 4679 C CG . LYS A 1 582 ? 27.081 85.758 31.013 1.00 24.38 ? 623 LYS A CG 1 ATOM 4680 C CD . LYS A 1 582 ? 28.359 86.356 30.400 1.00 29.64 ? 623 LYS A CD 1 ATOM 4681 C CE . LYS A 1 582 ? 29.482 86.103 31.377 1.00 36.60 ? 623 LYS A CE 1 ATOM 4682 N NZ . LYS A 1 582 ? 30.702 85.541 30.764 1.00 44.07 ? 623 LYS A NZ 1 ATOM 4683 N N . THR A 1 583 ? 23.326 85.031 28.653 1.00 24.91 ? 624 THR A N 1 ATOM 4684 C CA . THR A 1 583 ? 22.262 85.283 27.672 1.00 26.41 ? 624 THR A CA 1 ATOM 4685 C C . THR A 1 583 ? 20.883 85.148 28.235 1.00 26.09 ? 624 THR A C 1 ATOM 4686 O O . THR A 1 583 ? 20.010 85.989 28.014 1.00 25.76 ? 624 THR A O 1 ATOM 4687 C CB . THR A 1 583 ? 22.426 84.344 26.439 1.00 27.93 ? 624 THR A CB 1 ATOM 4688 O OG1 . THR A 1 583 ? 23.695 84.613 25.849 1.00 32.28 ? 624 THR A OG1 1 ATOM 4689 C CG2 . THR A 1 583 ? 21.328 84.573 25.395 1.00 30.66 ? 624 THR A CG2 1 ATOM 4690 N N . TYR A 1 584 ? 20.670 84.076 28.999 1.00 24.68 ? 625 TYR A N 1 ATOM 4691 C CA . TYR A 1 584 ? 19.327 83.787 29.487 1.00 24.53 ? 625 TYR A CA 1 ATOM 4692 C C . TYR A 1 584 ? 19.111 84.168 30.942 1.00 24.23 ? 625 TYR A C 1 ATOM 4693 O O . TYR A 1 584 ? 18.057 83.855 31.497 1.00 23.89 ? 625 TYR A O 1 ATOM 4694 C CB . TYR A 1 584 ? 19.007 82.290 29.279 1.00 24.11 ? 625 TYR A CB 1 ATOM 4695 C CG . TYR A 1 584 ? 19.104 81.954 27.821 1.00 23.90 ? 625 TYR A CG 1 ATOM 4696 C CD1 . TYR A 1 584 ? 18.200 82.508 26.902 1.00 27.30 ? 625 TYR A CD1 1 ATOM 4697 C CD2 . TYR A 1 584 ? 20.143 81.161 27.340 1.00 25.70 ? 625 TYR A CD2 1 ATOM 4698 C CE1 . TYR A 1 584 ? 18.314 82.237 25.532 1.00 28.44 ? 625 TYR A CE1 1 ATOM 4699 C CE2 . TYR A 1 584 ? 20.271 80.878 25.973 1.00 30.10 ? 625 TYR A CE2 1 ATOM 4700 C CZ . TYR A 1 584 ? 19.349 81.422 25.079 1.00 30.44 ? 625 TYR A CZ 1 ATOM 4701 O OH . TYR A 1 584 ? 19.478 81.163 23.731 1.00 33.42 ? 625 TYR A OH 1 ATOM 4702 N N . SER A 1 585 ? 20.085 84.872 31.544 1.00 22.35 ? 626 SER A N 1 ATOM 4703 C CA . SER A 1 585 ? 19.932 85.394 32.898 1.00 22.44 ? 626 SER A CA 1 ATOM 4704 C C . SER A 1 585 ? 19.622 84.273 33.882 1.00 21.60 ? 626 SER A C 1 ATOM 4705 O O . SER A 1 585 ? 18.675 84.362 34.673 1.00 20.88 ? 626 SER A O 1 ATOM 4706 C CB A SER A 1 585 ? 18.878 86.500 32.952 0.65 23.31 ? 626 SER A CB 1 ATOM 4707 C CB B SER A 1 585 ? 18.782 86.394 32.930 0.35 22.67 ? 626 SER A CB 1 ATOM 4708 O OG A SER A 1 585 ? 19.299 87.578 32.108 0.65 24.04 ? 626 SER A OG 1 ATOM 4709 O OG B SER A 1 585 ? 18.786 87.087 34.146 0.35 24.09 ? 626 SER A OG 1 ATOM 4710 N N . VAL A 1 586 ? 20.449 83.243 33.827 1.00 20.59 ? 627 VAL A N 1 ATOM 4711 C CA . VAL A 1 586 ? 20.228 82.030 34.643 1.00 20.00 ? 627 VAL A CA 1 ATOM 4712 C C . VAL A 1 586 ? 20.943 82.256 35.985 1.00 20.97 ? 627 VAL A C 1 ATOM 4713 O O . VAL A 1 586 ? 22.202 82.336 36.042 1.00 23.35 ? 627 VAL A O 1 ATOM 4714 C CB . VAL A 1 586 ? 20.815 80.810 33.917 1.00 19.32 ? 627 VAL A CB 1 ATOM 4715 C CG1 . VAL A 1 586 ? 20.528 79.536 34.772 1.00 19.70 ? 627 VAL A CG1 1 ATOM 4716 C CG2 . VAL A 1 586 ? 20.234 80.645 32.515 1.00 20.23 ? 627 VAL A CG2 1 ATOM 4717 N N . SER A 1 587 ? 20.164 82.471 37.042 1.00 21.84 ? 628 SER A N 1 ATOM 4718 C CA . SER A 1 587 ? 20.765 82.674 38.382 1.00 23.30 ? 628 SER A CA 1 ATOM 4719 C C . SER A 1 587 ? 20.395 81.591 39.359 1.00 22.21 ? 628 SER A C 1 ATOM 4720 O O . SER A 1 587 ? 19.229 81.183 39.410 1.00 21.97 ? 628 SER A O 1 ATOM 4721 C CB . SER A 1 587 ? 20.261 83.960 39.032 1.00 25.16 ? 628 SER A CB 1 ATOM 4722 O OG . SER A 1 587 ? 21.060 84.161 40.202 1.00 28.45 ? 628 SER A OG 1 ATOM 4723 N N . PHE A 1 588 ? 21.367 81.167 40.150 1.00 22.18 ? 629 PHE A N 1 ATOM 4724 C CA . PHE A 1 588 ? 21.131 80.257 41.279 1.00 20.05 ? 629 PHE A CA 1 ATOM 4725 C C . PHE A 1 588 ? 20.907 80.992 42.587 1.00 20.60 ? 629 PHE A C 1 ATOM 4726 O O . PHE A 1 588 ? 20.839 80.359 43.636 1.00 19.17 ? 629 PHE A O 1 ATOM 4727 C CB . PHE A 1 588 ? 22.254 79.202 41.404 1.00 20.44 ? 629 PHE A CB 1 ATOM 4728 C CG . PHE A 1 588 ? 22.182 78.154 40.337 1.00 20.26 ? 629 PHE A CG 1 ATOM 4729 C CD1 . PHE A 1 588 ? 21.635 76.894 40.606 1.00 18.85 ? 629 PHE A CD1 1 ATOM 4730 C CD2 . PHE A 1 588 ? 22.577 78.446 39.031 1.00 22.72 ? 629 PHE A CD2 1 ATOM 4731 C CE1 . PHE A 1 588 ? 21.499 75.934 39.614 1.00 19.79 ? 629 PHE A CE1 1 ATOM 4732 C CE2 . PHE A 1 588 ? 22.483 77.477 38.032 1.00 22.59 ? 629 PHE A CE2 1 ATOM 4733 C CZ . PHE A 1 588 ? 21.911 76.193 38.342 1.00 18.13 ? 629 PHE A CZ 1 ATOM 4734 N N . ASP A 1 589 ? 20.816 82.339 42.545 1.00 20.92 ? 630 ASP A N 1 ATOM 4735 C CA . ASP A 1 589 ? 20.738 83.089 43.801 1.00 21.37 ? 630 ASP A CA 1 ATOM 4736 C C . ASP A 1 589 ? 19.584 82.641 44.684 1.00 20.92 ? 630 ASP A C 1 ATOM 4737 O O . ASP A 1 589 ? 19.727 82.560 45.928 1.00 21.88 ? 630 ASP A O 1 ATOM 4738 C CB . ASP A 1 589 ? 20.629 84.599 43.534 1.00 21.51 ? 630 ASP A CB 1 ATOM 4739 C CG . ASP A 1 589 ? 21.957 85.223 43.001 1.00 27.53 ? 630 ASP A CG 1 ATOM 4740 O OD1 . ASP A 1 589 ? 23.027 84.557 42.974 1.00 29.15 ? 630 ASP A OD1 1 ATOM 4741 O OD2 . ASP A 1 589 ? 21.881 86.430 42.626 1.00 29.05 ? 630 ASP A OD2 1 ATOM 4742 N N . SER A 1 590 ? 18.438 82.357 44.062 1.00 19.79 ? 631 SER A N 1 ATOM 4743 C CA . SER A 1 590 ? 17.287 81.947 44.870 1.00 19.69 ? 631 SER A CA 1 ATOM 4744 C C . SER A 1 590 ? 17.538 80.621 45.547 1.00 19.03 ? 631 SER A C 1 ATOM 4745 O O . SER A 1 590 ? 17.111 80.442 46.692 1.00 18.55 ? 631 SER A O 1 ATOM 4746 C CB . SER A 1 590 ? 15.986 81.856 44.067 1.00 18.90 ? 631 SER A CB 1 ATOM 4747 O OG . SER A 1 590 ? 16.099 80.913 42.982 1.00 20.55 ? 631 SER A OG 1 ATOM 4748 N N . LEU A 1 591 ? 18.209 79.695 44.869 1.00 17.64 ? 632 LEU A N 1 ATOM 4749 C CA . LEU A 1 591 ? 18.473 78.392 45.507 1.00 18.53 ? 632 LEU A CA 1 ATOM 4750 C C . LEU A 1 591 ? 19.467 78.520 46.675 1.00 18.51 ? 632 LEU A C 1 ATOM 4751 O O . LEU A 1 591 ? 19.233 77.986 47.783 1.00 18.57 ? 632 LEU A O 1 ATOM 4752 C CB . LEU A 1 591 ? 18.957 77.380 44.491 1.00 18.12 ? 632 LEU A CB 1 ATOM 4753 C CG . LEU A 1 591 ? 19.256 75.993 45.063 1.00 16.79 ? 632 LEU A CG 1 ATOM 4754 C CD1 . LEU A 1 591 ? 18.014 75.323 45.631 1.00 16.57 ? 632 LEU A CD1 1 ATOM 4755 C CD2 . LEU A 1 591 ? 19.753 75.154 43.904 1.00 18.69 ? 632 LEU A CD2 1 ATOM 4756 N N . PHE A 1 592 ? 20.554 79.286 46.487 1.00 17.92 ? 633 PHE A N 1 ATOM 4757 C CA . PHE A 1 592 ? 21.455 79.502 47.619 1.00 18.79 ? 633 PHE A CA 1 ATOM 4758 C C . PHE A 1 592 ? 20.791 80.232 48.790 1.00 18.22 ? 633 PHE A C 1 ATOM 4759 O O . PHE A 1 592 ? 21.079 79.936 49.967 1.00 20.76 ? 633 PHE A O 1 ATOM 4760 C CB . PHE A 1 592 ? 22.700 80.215 47.119 1.00 20.46 ? 633 PHE A CB 1 ATOM 4761 C CG . PHE A 1 592 ? 23.614 79.303 46.372 1.00 20.96 ? 633 PHE A CG 1 ATOM 4762 C CD1 . PHE A 1 592 ? 24.388 78.360 47.058 1.00 22.19 ? 633 PHE A CD1 1 ATOM 4763 C CD2 . PHE A 1 592 ? 23.700 79.372 44.984 1.00 23.48 ? 633 PHE A CD2 1 ATOM 4764 C CE1 . PHE A 1 592 ? 25.249 77.496 46.361 1.00 22.44 ? 633 PHE A CE1 1 ATOM 4765 C CE2 . PHE A 1 592 ? 24.574 78.500 44.270 1.00 23.36 ? 633 PHE A CE2 1 ATOM 4766 C CZ . PHE A 1 592 ? 25.310 77.541 44.966 1.00 22.50 ? 633 PHE A CZ 1 ATOM 4767 N N . SER A 1 593 ? 19.922 81.187 48.470 1.00 19.17 ? 634 SER A N 1 ATOM 4768 C CA . SER A 1 593 ? 19.160 81.907 49.502 1.00 19.55 ? 634 SER A CA 1 ATOM 4769 C C . SER A 1 593 ? 18.294 80.966 50.313 1.00 18.63 ? 634 SER A C 1 ATOM 4770 O O . SER A 1 593 ? 18.257 81.002 51.542 1.00 19.86 ? 634 SER A O 1 ATOM 4771 C CB . SER A 1 593 ? 18.338 83.016 48.875 1.00 18.96 ? 634 SER A CB 1 ATOM 4772 O OG . SER A 1 593 ? 17.518 83.669 49.847 1.00 21.52 ? 634 SER A OG 1 ATOM 4773 N N . ALA A 1 594 ? 17.627 80.068 49.603 1.00 18.16 ? 635 ALA A N 1 ATOM 4774 C CA . ALA A 1 594 ? 16.763 79.093 50.278 1.00 18.26 ? 635 ALA A CA 1 ATOM 4775 C C . ALA A 1 594 ? 17.580 78.185 51.202 1.00 17.57 ? 635 ALA A C 1 ATOM 4776 O O . ALA A 1 594 ? 17.170 77.864 52.358 1.00 18.71 ? 635 ALA A O 1 ATOM 4777 C CB . ALA A 1 594 ? 15.947 78.264 49.226 1.00 18.59 ? 635 ALA A CB 1 ATOM 4778 N N . VAL A 1 595 ? 18.745 77.783 50.701 1.00 17.87 ? 636 VAL A N 1 ATOM 4779 C CA . VAL A 1 595 ? 19.621 76.868 51.469 1.00 17.34 ? 636 VAL A CA 1 ATOM 4780 C C . VAL A 1 595 ? 20.154 77.597 52.712 1.00 18.49 ? 636 VAL A C 1 ATOM 4781 O O . VAL A 1 595 ? 20.208 77.029 53.800 1.00 19.86 ? 636 VAL A O 1 ATOM 4782 C CB . VAL A 1 595 ? 20.737 76.328 50.597 1.00 17.92 ? 636 VAL A CB 1 ATOM 4783 C CG1 . VAL A 1 595 ? 21.754 75.586 51.435 1.00 20.13 ? 636 VAL A CG1 1 ATOM 4784 C CG2 . VAL A 1 595 ? 20.103 75.364 49.583 1.00 17.46 ? 636 VAL A CG2 1 ATOM 4785 N N . LYS A 1 596 ? 20.539 78.867 52.526 1.00 19.78 ? 637 LYS A N 1 ATOM 4786 C CA . LYS A 1 596 ? 20.973 79.682 53.672 1.00 20.32 ? 637 LYS A CA 1 ATOM 4787 C C . LYS A 1 596 ? 19.866 79.818 54.704 1.00 19.65 ? 637 LYS A C 1 ATOM 4788 O O . LYS A 1 596 ? 20.081 79.631 55.922 1.00 19.87 ? 637 LYS A O 1 ATOM 4789 C CB . LYS A 1 596 ? 21.395 81.069 53.158 1.00 21.64 ? 637 LYS A CB 1 ATOM 4790 C CG . LYS A 1 596 ? 21.711 82.082 54.273 1.00 25.29 ? 637 LYS A CG 1 ATOM 4791 C CD . LYS A 1 596 ? 22.116 83.397 53.612 1.00 30.80 ? 637 LYS A CD 1 ATOM 4792 C CE . LYS A 1 596 ? 22.587 84.386 54.662 1.00 33.51 ? 637 LYS A CE 1 ATOM 4793 N NZ . LYS A 1 596 ? 21.380 85.006 55.325 1.00 37.52 ? 637 LYS A NZ 1 ATOM 4794 N N . ASN A 1 597 ? 18.638 80.091 54.250 1.00 19.20 ? 638 ASN A N 1 ATOM 4795 C CA . ASN A 1 597 ? 17.505 80.173 55.141 1.00 19.47 ? 638 ASN A CA 1 ATOM 4796 C C . ASN A 1 597 ? 17.227 78.861 55.856 1.00 19.28 ? 638 ASN A C 1 ATOM 4797 O O . ASN A 1 597 ? 16.979 78.844 57.082 1.00 20.77 ? 638 ASN A O 1 ATOM 4798 C CB . ASN A 1 597 ? 16.254 80.609 54.380 1.00 17.98 ? 638 ASN A CB 1 ATOM 4799 C CG . ASN A 1 597 ? 16.319 82.051 53.945 1.00 21.45 ? 638 ASN A CG 1 ATOM 4800 O OD1 . ASN A 1 597 ? 17.225 82.805 54.364 1.00 22.55 ? 638 ASN A OD1 1 ATOM 4801 N ND2 . ASN A 1 597 ? 15.368 82.459 53.113 1.00 21.72 ? 638 ASN A ND2 1 ATOM 4802 N N . PHE A 1 598 ? 17.329 77.745 55.132 1.00 17.92 ? 639 PHE A N 1 ATOM 4803 C CA . PHE A 1 598 ? 17.121 76.458 55.736 1.00 18.10 ? 639 PHE A CA 1 ATOM 4804 C C . PHE A 1 598 ? 18.143 76.226 56.854 1.00 19.59 ? 639 PHE A C 1 ATOM 4805 O O . PHE A 1 598 ? 17.819 75.732 57.980 1.00 19.17 ? 639 PHE A O 1 ATOM 4806 C CB . PHE A 1 598 ? 17.274 75.354 54.676 1.00 17.18 ? 639 PHE A CB 1 ATOM 4807 C CG . PHE A 1 598 ? 16.866 73.975 55.166 1.00 17.16 ? 639 PHE A CG 1 ATOM 4808 C CD1 . PHE A 1 598 ? 15.654 73.389 54.735 1.00 17.67 ? 639 PHE A CD1 1 ATOM 4809 C CD2 . PHE A 1 598 ? 17.712 73.214 55.971 1.00 17.69 ? 639 PHE A CD2 1 ATOM 4810 C CE1 . PHE A 1 598 ? 15.280 72.110 55.147 1.00 18.79 ? 639 PHE A CE1 1 ATOM 4811 C CE2 . PHE A 1 598 ? 17.355 71.937 56.402 1.00 19.17 ? 639 PHE A CE2 1 ATOM 4812 C CZ . PHE A 1 598 ? 16.120 71.383 56.004 1.00 18.02 ? 639 PHE A CZ 1 ATOM 4813 N N . THR A 1 599 ? 19.387 76.618 56.558 1.00 19.58 ? 640 THR A N 1 ATOM 4814 C CA . THR A 1 599 ? 20.495 76.424 57.527 1.00 20.77 ? 640 THR A CA 1 ATOM 4815 C C . THR A 1 599 ? 20.213 77.217 58.802 1.00 21.77 ? 640 THR A C 1 ATOM 4816 O O . THR A 1 599 ? 20.345 76.691 59.911 1.00 22.38 ? 640 THR A O 1 ATOM 4817 C CB . THR A 1 599 ? 21.787 76.881 56.921 1.00 22.16 ? 640 THR A CB 1 ATOM 4818 O OG1 . THR A 1 599 ? 22.032 76.141 55.709 1.00 21.95 ? 640 THR A OG1 1 ATOM 4819 C CG2 . THR A 1 599 ? 22.959 76.618 57.933 1.00 20.94 ? 640 THR A CG2 1 ATOM 4820 N N . GLU A 1 600 ? 19.765 78.469 58.621 1.00 21.51 ? 641 GLU A N 1 ATOM 4821 C CA . GLU A 1 600 ? 19.466 79.329 59.786 1.00 22.94 ? 641 GLU A CA 1 ATOM 4822 C C . GLU A 1 600 ? 18.264 78.837 60.600 1.00 21.69 ? 641 GLU A C 1 ATOM 4823 O O . GLU A 1 600 ? 18.320 78.723 61.852 1.00 22.20 ? 641 GLU A O 1 ATOM 4824 C CB . GLU A 1 600 ? 19.269 80.779 59.339 1.00 23.65 ? 641 GLU A CB 1 ATOM 4825 C CG . GLU A 1 600 ? 20.595 81.374 58.847 1.00 30.05 ? 641 GLU A CG 1 ATOM 4826 C CD . GLU A 1 600 ? 20.454 82.755 58.198 1.00 38.06 ? 641 GLU A CD 1 ATOM 4827 O OE1 . GLU A 1 600 ? 21.484 83.307 57.726 1.00 41.62 ? 641 GLU A OE1 1 ATOM 4828 O OE2 . GLU A 1 600 ? 19.314 83.272 58.145 1.00 40.89 ? 641 GLU A OE2 1 ATOM 4829 N N . ILE A 1 601 ? 17.192 78.465 59.893 1.00 20.41 ? 642 ILE A N 1 ATOM 4830 C CA . ILE A 1 601 ? 16.002 78.022 60.561 1.00 20.53 ? 642 ILE A CA 1 ATOM 4831 C C . ILE A 1 601 ? 16.224 76.677 61.241 1.00 20.21 ? 642 ILE A C 1 ATOM 4832 O O . ILE A 1 601 ? 15.730 76.446 62.361 1.00 20.87 ? 642 ILE A O 1 ATOM 4833 C CB . ILE A 1 601 ? 14.798 77.973 59.577 1.00 19.82 ? 642 ILE A CB 1 ATOM 4834 C CG1 . ILE A 1 601 ? 14.491 79.405 59.089 1.00 18.47 ? 642 ILE A CG1 1 ATOM 4835 C CG2 . ILE A 1 601 ? 13.599 77.328 60.219 1.00 22.39 ? 642 ILE A CG2 1 ATOM 4836 C CD1 . ILE A 1 601 ? 13.437 79.474 57.881 1.00 21.28 ? 642 ILE A CD1 1 ATOM 4837 N N . ALA A 1 602 ? 16.978 75.785 60.599 1.00 18.60 ? 643 ALA A N 1 ATOM 4838 C CA . ALA A 1 602 ? 17.254 74.472 61.204 1.00 20.47 ? 643 ALA A CA 1 ATOM 4839 C C . ALA A 1 602 ? 18.085 74.688 62.483 1.00 22.08 ? 643 ALA A C 1 ATOM 4840 O O . ALA A 1 602 ? 17.855 74.013 63.493 1.00 22.87 ? 643 ALA A O 1 ATOM 4841 C CB . ALA A 1 602 ? 18.026 73.565 60.204 1.00 21.16 ? 643 ALA A CB 1 ATOM 4842 N N . SER A 1 603 ? 19.032 75.623 62.430 1.00 23.43 ? 644 SER A N 1 ATOM 4843 C CA . SER A 1 603 ? 19.847 75.880 63.641 1.00 25.67 ? 644 SER A CA 1 ATOM 4844 C C . SER A 1 603 ? 18.974 76.352 64.814 1.00 25.23 ? 644 SER A C 1 ATOM 4845 O O . SER A 1 603 ? 19.139 75.884 65.959 1.00 25.53 ? 644 SER A O 1 ATOM 4846 C CB . SER A 1 603 ? 20.953 76.865 63.353 1.00 26.39 ? 644 SER A CB 1 ATOM 4847 O OG . SER A 1 603 ? 21.659 77.117 64.578 1.00 32.30 ? 644 SER A OG 1 ATOM 4848 N N . LYS A 1 604 ? 18.040 77.245 64.534 1.00 24.20 ? 645 LYS A N 1 ATOM 4849 C CA A LYS A 1 604 ? 17.145 77.743 65.582 0.50 24.83 ? 645 LYS A CA 1 ATOM 4850 C CA B LYS A 1 604 ? 17.137 77.748 65.574 0.50 24.63 ? 645 LYS A CA 1 ATOM 4851 C C . LYS A 1 604 ? 16.202 76.647 66.079 1.00 24.51 ? 645 LYS A C 1 ATOM 4852 O O . LYS A 1 604 ? 15.951 76.529 67.266 1.00 24.30 ? 645 LYS A O 1 ATOM 4853 C CB A LYS A 1 604 ? 16.388 78.987 65.128 0.50 25.05 ? 645 LYS A CB 1 ATOM 4854 C CB B LYS A 1 604 ? 16.367 78.981 65.099 0.50 24.69 ? 645 LYS A CB 1 ATOM 4855 C CG A LYS A 1 604 ? 17.314 80.170 64.856 0.50 27.63 ? 645 LYS A CG 1 ATOM 4856 C CG B LYS A 1 604 ? 17.255 80.219 64.961 0.50 26.47 ? 645 LYS A CG 1 ATOM 4857 C CD A LYS A 1 604 ? 16.567 81.328 64.248 0.50 32.71 ? 645 LYS A CD 1 ATOM 4858 C CD B LYS A 1 604 ? 17.826 80.591 66.320 0.50 29.45 ? 645 LYS A CD 1 ATOM 4859 C CE A LYS A 1 604 ? 17.484 82.536 64.085 0.50 36.05 ? 645 LYS A CE 1 ATOM 4860 C CE B LYS A 1 604 ? 19.079 81.451 66.208 0.50 33.66 ? 645 LYS A CE 1 ATOM 4861 N NZ A LYS A 1 604 ? 16.811 83.624 63.311 0.50 39.47 ? 645 LYS A NZ 1 ATOM 4862 N NZ B LYS A 1 604 ? 18.990 82.368 65.040 0.50 35.05 ? 645 LYS A NZ 1 ATOM 4863 N N . PHE A 1 605 ? 15.684 75.810 65.154 1.00 21.88 ? 646 PHE A N 1 ATOM 4864 C CA . PHE A 1 605 ? 14.858 74.706 65.567 1.00 21.93 ? 646 PHE A CA 1 ATOM 4865 C C . PHE A 1 605 ? 15.602 73.761 66.485 1.00 22.51 ? 646 PHE A C 1 ATOM 4866 O O . PHE A 1 605 ? 15.061 73.276 67.506 1.00 23.99 ? 646 PHE A O 1 ATOM 4867 C CB . PHE A 1 605 ? 14.413 73.913 64.295 1.00 20.83 ? 646 PHE A CB 1 ATOM 4868 C CG . PHE A 1 605 ? 13.580 72.729 64.608 1.00 19.94 ? 646 PHE A CG 1 ATOM 4869 C CD1 . PHE A 1 605 ? 12.210 72.883 64.842 1.00 19.64 ? 646 PHE A CD1 1 ATOM 4870 C CD2 . PHE A 1 605 ? 14.162 71.453 64.720 1.00 23.04 ? 646 PHE A CD2 1 ATOM 4871 C CE1 . PHE A 1 605 ? 11.423 71.762 65.160 1.00 21.57 ? 646 PHE A CE1 1 ATOM 4872 C CE2 . PHE A 1 605 ? 13.384 70.327 65.049 1.00 23.48 ? 646 PHE A CE2 1 ATOM 4873 C CZ . PHE A 1 605 ? 12.019 70.468 65.250 1.00 20.09 ? 646 PHE A CZ 1 ATOM 4874 N N . SER A 1 606 ? 16.857 73.499 66.151 1.00 22.29 ? 647 SER A N 1 ATOM 4875 C CA . SER A 1 606 ? 17.679 72.606 66.965 1.00 23.83 ? 647 SER A CA 1 ATOM 4876 C C . SER A 1 606 ? 17.839 73.143 68.406 1.00 25.67 ? 647 SER A C 1 ATOM 4877 O O . SER A 1 606 ? 17.783 72.353 69.339 1.00 26.44 ? 647 SER A O 1 ATOM 4878 C CB . SER A 1 606 ? 19.043 72.470 66.328 1.00 24.95 ? 647 SER A CB 1 ATOM 4879 O OG A SER A 1 606 ? 18.958 71.800 65.083 0.50 25.12 ? 647 SER A OG 1 ATOM 4880 O OG B SER A 1 606 ? 19.705 71.324 66.828 0.50 25.65 ? 647 SER A OG 1 ATOM 4881 N N . GLU A 1 607 ? 18.014 74.458 68.530 1.00 25.03 ? 648 GLU A N 1 ATOM 4882 C CA . GLU A 1 607 ? 18.107 75.107 69.862 1.00 27.91 ? 648 GLU A CA 1 ATOM 4883 C C . GLU A 1 607 ? 16.823 74.856 70.654 1.00 27.84 ? 648 GLU A C 1 ATOM 4884 O O . GLU A 1 607 ? 16.874 74.401 71.838 1.00 29.50 ? 648 GLU A O 1 ATOM 4885 C CB . GLU A 1 607 ? 18.309 76.600 69.689 1.00 30.22 ? 648 GLU A CB 1 ATOM 4886 C CG . GLU A 1 607 ? 19.664 76.981 69.122 1.00 36.18 ? 648 GLU A CG 1 ATOM 4887 C CD . GLU A 1 607 ? 19.855 78.513 68.970 1.00 44.47 ? 648 GLU A CD 1 ATOM 4888 O OE1 . GLU A 1 607 ? 18.976 79.332 69.370 1.00 46.43 ? 648 GLU A OE1 1 ATOM 4889 O OE2 . GLU A 1 607 ? 20.906 78.892 68.414 1.00 49.99 ? 648 GLU A OE2 1 ATOM 4890 N N . ARG A 1 608 ? 15.671 75.101 70.007 1.00 26.54 ? 649 ARG A N 1 ATOM 4891 C CA . ARG A 1 608 ? 14.396 74.893 70.688 1.00 25.62 ? 649 ARG A CA 1 ATOM 4892 C C . ARG A 1 608 ? 14.218 73.447 71.070 1.00 26.96 ? 649 ARG A C 1 ATOM 4893 O O . ARG A 1 608 ? 13.709 73.126 72.127 1.00 27.95 ? 649 ARG A O 1 ATOM 4894 C CB . ARG A 1 608 ? 13.225 75.371 69.822 1.00 24.45 ? 649 ARG A CB 1 ATOM 4895 C CG . ARG A 1 608 ? 13.269 76.872 69.527 1.00 24.80 ? 649 ARG A CG 1 ATOM 4896 C CD . ARG A 1 608 ? 11.905 77.418 69.091 1.00 24.59 ? 649 ARG A CD 1 ATOM 4897 N NE . ARG A 1 608 ? 11.303 76.649 67.977 1.00 25.02 ? 649 ARG A NE 1 ATOM 4898 C CZ . ARG A 1 608 ? 11.644 76.838 66.709 1.00 26.43 ? 649 ARG A CZ 1 ATOM 4899 N NH1 . ARG A 1 608 ? 12.586 77.740 66.409 1.00 25.64 ? 649 ARG A NH1 1 ATOM 4900 N NH2 . ARG A 1 608 ? 11.069 76.118 65.730 1.00 25.98 ? 649 ARG A NH2 1 ATOM 4901 N N . LEU A 1 609 ? 14.684 72.542 70.213 1.00 26.76 ? 650 LEU A N 1 ATOM 4902 C CA . LEU A 1 609 ? 14.495 71.128 70.449 1.00 29.21 ? 650 LEU A CA 1 ATOM 4903 C C . LEU A 1 609 ? 15.295 70.715 71.683 1.00 32.45 ? 650 LEU A C 1 ATOM 4904 O O . LEU A 1 609 ? 14.900 69.825 72.433 1.00 32.79 ? 650 LEU A O 1 ATOM 4905 C CB . LEU A 1 609 ? 14.976 70.335 69.218 1.00 28.91 ? 650 LEU A CB 1 ATOM 4906 C CG . LEU A 1 609 ? 14.532 68.876 69.125 1.00 30.56 ? 650 LEU A CG 1 ATOM 4907 C CD1 . LEU A 1 609 ? 13.032 68.743 68.921 1.00 28.69 ? 650 LEU A CD1 1 ATOM 4908 C CD2 . LEU A 1 609 ? 15.331 68.160 67.990 1.00 31.66 ? 650 LEU A CD2 1 ATOM 4909 N N . GLN A 1 610 ? 16.429 71.363 71.868 1.00 35.83 ? 651 GLN A N 1 ATOM 4910 C CA . GLN A 1 610 ? 17.293 70.956 72.950 1.00 40.49 ? 651 GLN A CA 1 ATOM 4911 C C . GLN A 1 610 ? 16.865 71.614 74.232 1.00 41.30 ? 651 GLN A C 1 ATOM 4912 O O . GLN A 1 610 ? 17.045 71.014 75.287 1.00 43.15 ? 651 GLN A O 1 ATOM 4913 C CB . GLN A 1 610 ? 18.755 71.193 72.615 1.00 41.12 ? 651 GLN A CB 1 ATOM 4914 C CG . GLN A 1 610 ? 19.256 70.054 71.764 1.00 46.06 ? 651 GLN A CG 1 ATOM 4915 C CD . GLN A 1 610 ? 20.736 70.120 71.473 1.00 51.91 ? 651 GLN A CD 1 ATOM 4916 O OE1 . GLN A 1 610 ? 21.546 70.418 72.357 1.00 56.40 ? 651 GLN A OE1 1 ATOM 4917 N NE2 . GLN A 1 610 ? 21.104 69.825 70.218 1.00 54.48 ? 651 GLN A NE2 1 ATOM 4918 N N . ASP A 1 611 ? 16.274 72.809 74.097 1.00 41.98 ? 652 ASP A N 1 ATOM 4919 C CA . ASP A 1 611 ? 15.849 73.744 75.163 1.00 43.49 ? 652 ASP A CA 1 ATOM 4920 C C . ASP A 1 611 ? 14.401 73.626 75.606 1.00 42.67 ? 652 ASP A C 1 ATOM 4921 O O . ASP A 1 611 ? 13.992 74.323 76.518 1.00 42.21 ? 652 ASP A O 1 ATOM 4922 C CB . ASP A 1 611 ? 15.839 75.176 74.609 1.00 44.72 ? 652 ASP A CB 1 ATOM 4923 C CG . ASP A 1 611 ? 17.165 75.878 74.709 1.00 50.20 ? 652 ASP A CG 1 ATOM 4924 O OD1 . ASP A 1 611 ? 17.140 77.122 74.514 1.00 55.39 ? 652 ASP A OD1 1 ATOM 4925 O OD2 . ASP A 1 611 ? 18.205 75.216 74.969 1.00 55.76 ? 652 ASP A OD2 1 ATOM 4926 N N . PHE A 1 612 ? 13.575 72.877 74.895 1.00 41.01 ? 653 PHE A N 1 ATOM 4927 C CA . PHE A 1 612 ? 12.157 72.994 75.184 1.00 39.64 ? 653 PHE A CA 1 ATOM 4928 C C . PHE A 1 612 ? 11.731 72.311 76.447 1.00 40.07 ? 653 PHE A C 1 ATOM 4929 O O . PHE A 1 612 ? 10.677 72.759 76.933 1.00 41.69 ? 653 PHE A O 1 ATOM 4930 C CB . PHE A 1 612 ? 11.253 72.542 74.038 1.00 37.82 ? 653 PHE A CB 1 ATOM 4931 C CG . PHE A 1 612 ? 11.071 71.047 73.930 1.00 35.05 ? 653 PHE A CG 1 ATOM 4932 C CD1 . PHE A 1 612 ? 9.961 70.421 74.496 1.00 31.51 ? 653 PHE A CD1 1 ATOM 4933 C CD2 . PHE A 1 612 ? 11.954 70.300 73.180 1.00 33.72 ? 653 PHE A CD2 1 ATOM 4934 C CE1 . PHE A 1 612 ? 9.735 69.075 74.332 1.00 36.11 ? 653 PHE A CE1 1 ATOM 4935 C CE2 . PHE A 1 612 ? 11.765 68.939 73.006 1.00 36.85 ? 653 PHE A CE2 1 ATOM 4936 C CZ . PHE A 1 612 ? 10.649 68.316 73.575 1.00 37.13 ? 653 PHE A CZ 1 ATOM 4937 N N A SER A 1 615 ? 8.868 68.777 80.072 0.50 22.99 ? 656 SER A N 1 ATOM 4938 N N B SER A 1 615 ? 7.907 66.175 79.131 0.50 21.39 ? 656 SER A N 1 ATOM 4939 C CA A SER A 1 615 ? 7.674 68.133 80.574 0.50 22.68 ? 656 SER A CA 1 ATOM 4940 C CA B SER A 1 615 ? 6.811 65.535 79.888 0.50 21.29 ? 656 SER A CA 1 ATOM 4941 C C A SER A 1 615 ? 6.414 68.300 79.686 0.50 21.65 ? 656 SER A C 1 ATOM 4942 C C B SER A 1 615 ? 5.506 66.260 79.599 0.50 21.65 ? 656 SER A C 1 ATOM 4943 O O A SER A 1 615 ? 5.353 67.767 80.029 0.50 22.56 ? 656 SER A O 1 ATOM 4944 O O B SER A 1 615 ? 4.468 65.956 80.176 0.50 22.55 ? 656 SER A O 1 ATOM 4945 C CB A SER A 1 615 ? 7.388 68.729 81.953 0.50 20.28 ? 656 SER A CB 1 ATOM 4946 C CB B SER A 1 615 ? 7.126 65.482 81.425 0.50 20.17 ? 656 SER A CB 1 ATOM 4947 O OG A SER A 1 615 ? 7.192 70.079 81.789 0.50 21.43 ? 656 SER A OG 1 ATOM 4948 O OG B SER A 1 615 ? 6.786 66.755 81.960 0.50 23.39 ? 656 SER A OG 1 ATOM 4949 N N A ASN A 1 616 ? 6.504 69.041 78.577 0.50 20.55 ? 657 ASN A N 1 ATOM 4950 N N B ASN A 1 616 ? 5.541 67.226 78.683 0.50 21.53 ? 657 ASN A N 1 ATOM 4951 C CA A ASN A 1 616 ? 5.318 69.353 77.754 0.50 21.47 ? 657 ASN A CA 1 ATOM 4952 C CA B ASN A 1 616 ? 4.332 67.877 78.215 0.50 22.96 ? 657 ASN A CA 1 ATOM 4953 C C A ASN A 1 616 ? 5.218 68.413 76.554 0.50 22.10 ? 657 ASN A C 1 ATOM 4954 C C B ASN A 1 616 ? 3.892 67.178 76.918 0.50 23.00 ? 657 ASN A C 1 ATOM 4955 O O A ASN A 1 616 ? 6.015 68.510 75.594 0.50 21.67 ? 657 ASN A O 1 ATOM 4956 O O B ASN A 1 616 ? 4.387 67.484 75.840 0.50 23.23 ? 657 ASN A O 1 ATOM 4957 C CB A ASN A 1 616 ? 5.332 70.798 77.277 0.50 21.62 ? 657 ASN A CB 1 ATOM 4958 C CB B ASN A 1 616 ? 4.624 69.386 78.010 0.50 21.98 ? 657 ASN A CB 1 ATOM 4959 C CG A ASN A 1 616 ? 4.005 71.219 76.726 0.50 22.86 ? 657 ASN A CG 1 ATOM 4960 C CG B ASN A 1 616 ? 3.439 70.167 77.492 0.50 25.86 ? 657 ASN A CG 1 ATOM 4961 O OD1 A ASN A 1 616 ? 3.368 70.467 76.010 0.50 22.03 ? 657 ASN A OD1 1 ATOM 4962 O OD1 B ASN A 1 616 ? 2.665 69.675 76.658 0.50 27.76 ? 657 ASN A OD1 1 ATOM 4963 N ND2 A ASN A 1 616 ? 3.563 72.417 77.071 0.50 26.23 ? 657 ASN A ND2 1 ATOM 4964 N ND2 B ASN A 1 616 ? 3.337 71.426 77.914 0.50 27.81 ? 657 ASN A ND2 1 ATOM 4965 N N A PRO A 1 617 ? 4.280 67.451 76.612 0.50 21.24 ? 658 PRO A N 1 ATOM 4966 N N B PRO A 1 617 ? 2.955 66.216 77.018 0.50 23.93 ? 658 PRO A N 1 ATOM 4967 C CA A PRO A 1 617 ? 4.250 66.418 75.572 0.50 20.75 ? 658 PRO A CA 1 ATOM 4968 C CA B PRO A 1 617 ? 2.544 65.408 75.838 0.50 23.31 ? 658 PRO A CA 1 ATOM 4969 C C A PRO A 1 617 ? 3.688 66.992 74.271 0.50 20.54 ? 658 PRO A C 1 ATOM 4970 C C B PRO A 1 617 ? 2.288 66.134 74.507 0.50 23.46 ? 658 PRO A C 1 ATOM 4971 O O A PRO A 1 617 ? 3.888 66.401 73.207 0.50 19.82 ? 658 PRO A O 1 ATOM 4972 O O B PRO A 1 617 ? 2.738 65.649 73.461 0.50 21.78 ? 658 PRO A O 1 ATOM 4973 C CB A PRO A 1 617 ? 3.272 65.379 76.141 0.50 20.74 ? 658 PRO A CB 1 ATOM 4974 C CB B PRO A 1 617 ? 1.245 64.767 76.318 0.50 24.15 ? 658 PRO A CB 1 ATOM 4975 C CG A PRO A 1 617 ? 2.253 66.298 76.968 0.50 19.72 ? 658 PRO A CG 1 ATOM 4976 C CG B PRO A 1 617 ? 1.420 64.642 77.799 0.50 25.30 ? 658 PRO A CG 1 ATOM 4977 C CD A PRO A 1 617 ? 3.148 67.360 77.562 0.50 22.95 ? 658 PRO A CD 1 ATOM 4978 C CD B PRO A 1 617 ? 2.261 65.798 78.248 0.50 24.35 ? 658 PRO A CD 1 ATOM 4979 N N A ILE A 1 618 ? 2.946 68.097 74.355 0.50 20.71 ? 659 ILE A N 1 ATOM 4980 N N B ILE A 1 618 ? 1.541 67.233 74.510 0.50 22.76 ? 659 ILE A N 1 ATOM 4981 C CA A ILE A 1 618 ? 2.392 68.717 73.156 0.50 21.39 ? 659 ILE A CA 1 ATOM 4982 C CA B ILE A 1 618 ? 1.244 67.904 73.232 0.50 22.61 ? 659 ILE A CA 1 ATOM 4983 C C A ILE A 1 618 ? 3.487 69.464 72.403 0.50 21.25 ? 659 ILE A C 1 ATOM 4984 C C B ILE A 1 618 ? 2.418 68.695 72.712 0.50 21.84 ? 659 ILE A C 1 ATOM 4985 O O A ILE A 1 618 ? 3.562 69.397 71.180 0.50 19.63 ? 659 ILE A O 1 ATOM 4986 O O B ILE A 1 618 ? 2.638 68.774 71.502 0.50 22.28 ? 659 ILE A O 1 ATOM 4987 C CB A ILE A 1 618 ? 1.248 69.715 73.433 0.50 22.38 ? 659 ILE A CB 1 ATOM 4988 C CB B ILE A 1 618 ? -0.021 68.785 73.216 0.50 22.08 ? 659 ILE A CB 1 ATOM 4989 C CG1 A ILE A 1 618 ? 0.104 69.052 74.223 0.50 25.92 ? 659 ILE A CG1 1 ATOM 4990 C CG1 B ILE A 1 618 ? -1.249 67.911 73.051 0.50 26.40 ? 659 ILE A CG1 1 ATOM 4991 C CG2 A ILE A 1 618 ? 0.780 70.350 72.101 0.50 22.04 ? 659 ILE A CG2 1 ATOM 4992 C CG2 B ILE A 1 618 ? -0.008 69.650 71.998 0.50 24.11 ? 659 ILE A CG2 1 ATOM 4993 C CD1 A ILE A 1 618 ? -0.256 67.686 73.705 0.50 24.83 ? 659 ILE A CD1 1 ATOM 4994 C CD1 B ILE A 1 618 ? -1.536 67.604 71.603 0.50 29.55 ? 659 ILE A CD1 1 ATOM 4995 N N A VAL A 1 619 ? 4.324 70.200 73.121 0.50 20.09 ? 660 VAL A N 1 ATOM 4996 N N B VAL A 1 619 ? 3.184 69.306 73.604 0.50 21.81 ? 660 VAL A N 1 ATOM 4997 C CA A VAL A 1 619 ? 5.456 70.826 72.455 0.50 20.82 ? 660 VAL A CA 1 ATOM 4998 C CA B VAL A 1 619 ? 4.352 70.042 73.129 0.50 20.04 ? 660 VAL A CA 1 ATOM 4999 C C A VAL A 1 619 ? 6.398 69.756 71.869 0.50 19.55 ? 660 VAL A C 1 ATOM 5000 C C B VAL A 1 619 ? 5.333 69.055 72.474 0.50 19.91 ? 660 VAL A C 1 ATOM 5001 O O A VAL A 1 619 ? 6.938 69.916 70.760 0.50 19.60 ? 660 VAL A O 1 ATOM 5002 O O B VAL A 1 619 ? 5.879 69.292 71.380 0.50 19.93 ? 660 VAL A O 1 ATOM 5003 C CB A VAL A 1 619 ? 6.234 71.719 73.424 0.50 20.41 ? 660 VAL A CB 1 ATOM 5004 C CB B VAL A 1 619 ? 5.014 70.866 74.232 0.50 21.66 ? 660 VAL A CB 1 ATOM 5005 C CG1 A VAL A 1 619 ? 7.380 72.389 72.720 0.50 23.41 ? 660 VAL A CG1 1 ATOM 5006 C CG1 B VAL A 1 619 ? 6.330 71.470 73.720 0.50 20.01 ? 660 VAL A CG1 1 ATOM 5007 C CG2 A VAL A 1 619 ? 5.302 72.762 74.012 0.50 21.18 ? 660 VAL A CG2 1 ATOM 5008 C CG2 B VAL A 1 619 ? 4.063 71.944 74.697 0.50 19.58 ? 660 VAL A CG2 1 ATOM 5009 N N A LEU A 1 620 ? 6.600 68.671 72.628 0.50 18.61 ? 661 LEU A N 1 ATOM 5010 N N B LEU A 1 620 ? 5.509 67.904 73.099 0.50 18.03 ? 661 LEU A N 1 ATOM 5011 C CA A LEU A 1 620 ? 7.393 67.512 72.192 0.50 17.11 ? 661 LEU A CA 1 ATOM 5012 C CA B LEU A 1 620 ? 6.389 66.878 72.542 0.50 18.55 ? 661 LEU A CA 1 ATOM 5013 C C A LEU A 1 620 ? 6.819 66.963 70.873 0.50 18.40 ? 661 LEU A C 1 ATOM 5014 C C B LEU A 1 620 ? 5.839 66.424 71.199 0.50 18.27 ? 661 LEU A C 1 ATOM 5015 O O A LEU A 1 620 ? 7.549 66.830 69.896 0.50 18.44 ? 661 LEU A O 1 ATOM 5016 O O B LEU A 1 620 ? 6.571 66.202 70.249 0.50 19.25 ? 661 LEU A O 1 ATOM 5017 C CB A LEU A 1 620 ? 7.436 66.457 73.327 0.50 18.65 ? 661 LEU A CB 1 ATOM 5018 C CB B LEU A 1 620 ? 6.464 65.690 73.475 0.50 18.47 ? 661 LEU A CB 1 ATOM 5019 C CG A LEU A 1 620 ? 7.944 65.065 72.961 0.50 18.76 ? 661 LEU A CG 1 ATOM 5020 C CG B LEU A 1 620 ? 7.355 64.541 72.951 0.50 20.49 ? 661 LEU A CG 1 ATOM 5021 C CD1 A LEU A 1 620 ? 9.307 65.133 72.319 0.50 19.19 ? 661 LEU A CD1 1 ATOM 5022 C CD1 B LEU A 1 620 ? 8.801 64.941 72.569 0.50 20.48 ? 661 LEU A CD1 1 ATOM 5023 C CD2 A LEU A 1 620 ? 7.993 64.129 74.185 0.50 18.53 ? 661 LEU A CD2 1 ATOM 5024 C CD2 B LEU A 1 620 ? 7.375 63.406 73.953 0.50 18.52 ? 661 LEU A CD2 1 ATOM 5025 N N A ARG A 1 621 ? 5.518 66.675 70.864 0.50 18.39 ? 662 ARG A N 1 ATOM 5026 N N B ARG A 1 621 ? 4.532 66.277 71.126 0.50 17.86 ? 662 ARG A N 1 ATOM 5027 C CA A ARG A 1 621 ? 4.876 65.988 69.731 0.50 19.72 ? 662 ARG A CA 1 ATOM 5028 C CA B ARG A 1 621 ? 3.930 65.897 69.850 0.50 18.30 ? 662 ARG A CA 1 ATOM 5029 C C A ARG A 1 621 ? 4.778 66.969 68.624 0.50 19.06 ? 662 ARG A C 1 ATOM 5030 C C B ARG A 1 621 ? 4.219 66.862 68.659 0.50 18.56 ? 662 ARG A C 1 ATOM 5031 O O A ARG A 1 621 ? 5.123 66.634 67.496 0.50 17.71 ? 662 ARG A O 1 ATOM 5032 O O B ARG A 1 621 ? 4.428 66.400 67.532 0.50 17.99 ? 662 ARG A O 1 ATOM 5033 C CB A ARG A 1 621 ? 3.473 65.481 70.085 0.50 19.73 ? 662 ARG A CB 1 ATOM 5034 C CB B ARG A 1 621 ? 2.447 65.593 70.063 0.50 18.05 ? 662 ARG A CB 1 ATOM 5035 C CG A ARG A 1 621 ? 2.578 65.124 68.869 0.50 20.22 ? 662 ARG A CG 1 ATOM 5036 C CG B ARG A 1 621 ? 1.764 65.054 68.851 0.50 18.71 ? 662 ARG A CG 1 ATOM 5037 C CD A ARG A 1 621 ? 2.620 63.616 68.442 0.50 22.82 ? 662 ARG A CD 1 ATOM 5038 C CD B ARG A 1 621 ? 2.462 63.845 68.203 0.50 26.73 ? 662 ARG A CD 1 ATOM 5039 N NE A ARG A 1 621 ? 1.358 63.310 67.732 0.50 24.14 ? 662 ARG A NE 1 ATOM 5040 N NE B ARG A 1 621 ? 1.415 63.121 67.486 0.50 29.75 ? 662 ARG A NE 1 ATOM 5041 C CZ A ARG A 1 621 ? 0.825 62.094 67.580 0.50 19.18 ? 662 ARG A CZ 1 ATOM 5042 C CZ B ARG A 1 621 ? 1.141 61.831 67.631 0.50 29.32 ? 662 ARG A CZ 1 ATOM 5043 N NH1 A ARG A 1 621 ? 1.452 61.009 68.060 0.50 21.59 ? 662 ARG A NH1 1 ATOM 5044 N NH1 B ARG A 1 621 ? 1.882 61.060 68.417 0.50 27.84 ? 662 ARG A NH1 1 ATOM 5045 N NH2 A ARG A 1 621 ? -0.332 61.963 66.930 0.50 17.37 ? 662 ARG A NH2 1 ATOM 5046 N NH2 B ARG A 1 621 ? 0.131 61.307 66.955 0.50 31.43 ? 662 ARG A NH2 1 ATOM 5047 N N . MET A 1 622 ? 4.288 68.186 68.919 1.00 19.48 ? 663 MET A N 1 ATOM 5048 C CA . MET A 1 622 ? 4.501 69.252 67.913 1.00 19.50 ? 663 MET A CA 1 ATOM 5049 C C . MET A 1 622 ? 5.897 69.205 67.295 1.00 20.63 ? 663 MET A C 1 ATOM 5050 O O . MET A 1 622 ? 6.052 69.228 66.060 1.00 19.50 ? 663 MET A O 1 ATOM 5051 C CB A MET A 1 622 ? 4.374 70.652 68.544 0.50 19.07 ? 663 MET A CB 1 ATOM 5052 C CB B MET A 1 622 ? 4.074 70.620 68.481 0.50 19.98 ? 663 MET A CB 1 ATOM 5053 C CG A MET A 1 622 ? 4.837 71.791 67.615 0.50 18.93 ? 663 MET A CG 1 ATOM 5054 C CG B MET A 1 622 ? 2.584 70.563 68.903 0.50 20.12 ? 663 MET A CG 1 ATOM 5055 S SD A MET A 1 622 ? 4.558 73.435 68.333 0.50 5.32 ? 663 MET A SD 1 ATOM 5056 S SD B MET A 1 622 ? 1.700 72.093 69.382 0.50 7.46 ? 663 MET A SD 1 ATOM 5057 C CE A MET A 1 622 ? 5.840 73.403 69.572 0.50 25.34 ? 663 MET A CE 1 ATOM 5058 C CE B MET A 1 622 ? 2.448 72.506 71.012 0.50 18.33 ? 663 MET A CE 1 ATOM 5059 N N . MET A 1 623 ? 6.944 69.119 68.140 1.00 19.60 ? 664 MET A N 1 ATOM 5060 C CA . MET A 1 623 ? 8.293 69.101 67.603 1.00 20.12 ? 664 MET A CA 1 ATOM 5061 C C . MET A 1 623 ? 8.597 67.784 66.876 1.00 20.00 ? 664 MET A C 1 ATOM 5062 O O . MET A 1 623 ? 9.293 67.804 65.848 1.00 20.24 ? 664 MET A O 1 ATOM 5063 C CB A MET A 1 623 ? 9.229 69.090 68.839 0.50 21.47 ? 664 MET A CB 1 ATOM 5064 C CB B MET A 1 623 ? 9.393 69.512 68.608 0.50 20.88 ? 664 MET A CB 1 ATOM 5065 C CG A MET A 1 623 ? 8.881 70.131 69.900 0.50 24.96 ? 664 MET A CG 1 ATOM 5066 C CG B MET A 1 623 ? 9.311 70.981 68.979 0.50 17.97 ? 664 MET A CG 1 ATOM 5067 S SD A MET A 1 623 ? 9.013 71.717 69.100 0.50 9.04 ? 664 MET A SD 1 ATOM 5068 S SD B MET A 1 623 ? 10.739 71.667 69.863 0.50 6.55 ? 664 MET A SD 1 ATOM 5069 C CE A MET A 1 623 ? 10.752 72.110 69.328 0.50 26.72 ? 664 MET A CE 1 ATOM 5070 C CE B MET A 1 623 ? 11.657 72.296 68.456 0.50 18.77 ? 664 MET A CE 1 ATOM 5071 N N . ASN A 1 624 ? 8.094 66.672 67.409 1.00 19.98 ? 665 ASN A N 1 ATOM 5072 C CA . ASN A 1 624 ? 8.283 65.353 66.718 1.00 19.81 ? 665 ASN A CA 1 ATOM 5073 C C . ASN A 1 624 ? 7.566 65.403 65.369 1.00 19.35 ? 665 ASN A C 1 ATOM 5074 O O . ASN A 1 624 ? 8.082 64.879 64.385 1.00 19.49 ? 665 ASN A O 1 ATOM 5075 C CB . ASN A 1 624 ? 7.781 64.176 67.544 1.00 20.71 ? 665 ASN A CB 1 ATOM 5076 C CG . ASN A 1 624 ? 8.838 63.699 68.540 1.00 20.29 ? 665 ASN A CG 1 ATOM 5077 O OD1 . ASN A 1 624 ? 10.045 63.889 68.283 1.00 19.15 ? 665 ASN A OD1 1 ATOM 5078 N ND2 . ASN A 1 624 ? 8.414 63.077 69.648 1.00 20.09 ? 665 ASN A ND2 1 ATOM 5079 N N . ASP A 1 625 ? 6.396 66.041 65.315 1.00 17.95 ? 666 ASP A N 1 ATOM 5080 C CA . ASP A 1 625 ? 5.736 66.131 63.989 1.00 18.12 ? 666 ASP A CA 1 ATOM 5081 C C . ASP A 1 625 ? 6.545 66.999 63.029 1.00 18.31 ? 666 ASP A C 1 ATOM 5082 O O . ASP A 1 625 ? 6.597 66.689 61.831 1.00 19.49 ? 666 ASP A O 1 ATOM 5083 C CB . ASP A 1 625 ? 4.356 66.708 64.172 1.00 18.97 ? 666 ASP A CB 1 ATOM 5084 C CG . ASP A 1 625 ? 3.352 65.707 64.721 1.00 18.84 ? 666 ASP A CG 1 ATOM 5085 O OD1 . ASP A 1 625 ? 3.670 64.489 64.890 1.00 20.72 ? 666 ASP A OD1 1 ATOM 5086 O OD2 . ASP A 1 625 ? 2.182 66.185 64.909 1.00 20.96 ? 666 ASP A OD2 1 ATOM 5087 N N . GLN A 1 626 ? 7.156 68.092 63.519 1.00 16.67 ? 667 GLN A N 1 ATOM 5088 C CA . GLN A 1 626 ? 7.991 68.916 62.645 1.00 17.97 ? 667 GLN A CA 1 ATOM 5089 C C . GLN A 1 626 ? 9.162 68.051 62.132 1.00 17.32 ? 667 GLN A C 1 ATOM 5090 O O . GLN A 1 626 ? 9.530 68.121 60.947 1.00 18.88 ? 667 GLN A O 1 ATOM 5091 C CB . GLN A 1 626 ? 8.490 70.169 63.365 1.00 17.57 ? 667 GLN A CB 1 ATOM 5092 C CG . GLN A 1 626 ? 7.360 71.201 63.548 1.00 16.78 ? 667 GLN A CG 1 ATOM 5093 C CD . GLN A 1 626 ? 7.851 72.431 64.281 1.00 19.33 ? 667 GLN A CD 1 ATOM 5094 O OE1 . GLN A 1 626 ? 7.995 72.383 65.509 1.00 21.66 ? 667 GLN A OE1 1 ATOM 5095 N NE2 . GLN A 1 626 ? 8.121 73.532 63.532 1.00 21.10 ? 667 GLN A NE2 1 ATOM 5096 N N . LEU A 1 627 ? 9.744 67.231 63.019 1.00 19.00 ? 668 LEU A N 1 ATOM 5097 C CA . LEU A 1 627 ? 10.825 66.312 62.579 1.00 18.97 ? 668 LEU A CA 1 ATOM 5098 C C . LEU A 1 627 ? 10.338 65.272 61.547 1.00 18.45 ? 668 LEU A C 1 ATOM 5099 O O . LEU A 1 627 ? 10.984 65.050 60.511 1.00 19.98 ? 668 LEU A O 1 ATOM 5100 C CB . LEU A 1 627 ? 11.420 65.566 63.778 1.00 20.19 ? 668 LEU A CB 1 ATOM 5101 C CG . LEU A 1 627 ? 12.355 66.540 64.542 1.00 21.34 ? 668 LEU A CG 1 ATOM 5102 C CD1 . LEU A 1 627 ? 12.834 65.858 65.810 1.00 24.49 ? 668 LEU A CD1 1 ATOM 5103 C CD2 . LEU A 1 627 ? 13.536 67.018 63.706 1.00 27.26 ? 668 LEU A CD2 1 ATOM 5104 N N . MET A 1 628 ? 9.138 64.731 61.796 1.00 18.79 ? 669 MET A N 1 ATOM 5105 C CA . MET A 1 628 ? 8.605 63.647 60.929 1.00 17.10 ? 669 MET A CA 1 ATOM 5106 C C . MET A 1 628 ? 8.213 64.211 59.561 1.00 16.43 ? 669 MET A C 1 ATOM 5107 O O . MET A 1 628 ? 8.429 63.562 58.533 1.00 16.93 ? 669 MET A O 1 ATOM 5108 C CB . MET A 1 628 ? 7.367 63.042 61.560 1.00 18.73 ? 669 MET A CB 1 ATOM 5109 C CG . MET A 1 628 ? 6.638 61.988 60.648 1.00 21.25 ? 669 MET A CG 1 ATOM 5110 S SD . MET A 1 628 ? 5.245 61.233 61.517 1.00 5.38 ? 669 MET A SD 1 ATOM 5111 C CE . MET A 1 628 ? 3.994 62.523 61.364 1.00 20.18 ? 669 MET A CE 1 ATOM 5112 N N . PHE A 1 629 ? 7.622 65.401 59.594 1.00 15.54 ? 670 PHE A N 1 ATOM 5113 C CA . PHE A 1 629 ? 7.140 65.997 58.319 1.00 15.99 ? 670 PHE A CA 1 ATOM 5114 C C . PHE A 1 629 ? 8.222 66.723 57.537 1.00 15.27 ? 670 PHE A C 1 ATOM 5115 O O . PHE A 1 629 ? 7.940 67.277 56.447 1.00 15.62 ? 670 PHE A O 1 ATOM 5116 C CB . PHE A 1 629 ? 5.903 66.884 58.506 1.00 16.26 ? 670 PHE A CB 1 ATOM 5117 C CG . PHE A 1 629 ? 4.663 66.106 58.811 1.00 18.04 ? 670 PHE A CG 1 ATOM 5118 C CD1 . PHE A 1 629 ? 4.138 65.202 57.868 1.00 17.30 ? 670 PHE A CD1 1 ATOM 5119 C CD2 . PHE A 1 629 ? 3.941 66.332 60.000 1.00 16.82 ? 670 PHE A CD2 1 ATOM 5120 C CE1 . PHE A 1 629 ? 2.956 64.496 58.127 1.00 19.46 ? 670 PHE A CE1 1 ATOM 5121 C CE2 . PHE A 1 629 ? 2.727 65.644 60.264 1.00 19.69 ? 670 PHE A CE2 1 ATOM 5122 C CZ . PHE A 1 629 ? 2.255 64.689 59.323 1.00 19.46 ? 670 PHE A CZ 1 ATOM 5123 N N . LEU A 1 630 ? 9.456 66.775 58.059 1.00 16.02 ? 671 LEU A N 1 ATOM 5124 C CA . LEU A 1 630 ? 10.508 67.484 57.344 1.00 16.33 ? 671 LEU A CA 1 ATOM 5125 C C . LEU A 1 630 ? 10.865 66.741 56.042 1.00 14.52 ? 671 LEU A C 1 ATOM 5126 O O . LEU A 1 630 ? 10.871 67.362 54.979 1.00 15.33 ? 671 LEU A O 1 ATOM 5127 C CB . LEU A 1 630 ? 11.744 67.718 58.226 1.00 17.22 ? 671 LEU A CB 1 ATOM 5128 C CG . LEU A 1 630 ? 12.924 68.388 57.540 1.00 18.58 ? 671 LEU A CG 1 ATOM 5129 C CD1 . LEU A 1 630 ? 12.558 69.796 57.019 1.00 19.82 ? 671 LEU A CD1 1 ATOM 5130 C CD2 . LEU A 1 630 ? 14.077 68.488 58.614 1.00 19.81 ? 671 LEU A CD2 1 ATOM 5131 N N . GLU A 1 631 ? 11.115 65.426 56.099 1.00 13.87 ? 672 GLU A N 1 ATOM 5132 C CA . GLU A 1 631 ? 11.322 64.696 54.828 1.00 14.85 ? 672 GLU A CA 1 ATOM 5133 C C . GLU A 1 631 ? 10.078 64.890 53.912 1.00 13.22 ? 672 GLU A C 1 ATOM 5134 O O . GLU A 1 631 ? 10.235 65.065 52.645 1.00 14.32 ? 672 GLU A O 1 ATOM 5135 C CB . GLU A 1 631 ? 11.519 63.202 55.060 1.00 14.60 ? 672 GLU A CB 1 ATOM 5136 C CG . GLU A 1 631 ? 12.100 62.528 53.850 1.00 13.77 ? 672 GLU A CG 1 ATOM 5137 C CD . GLU A 1 631 ? 13.612 62.804 53.738 1.00 18.37 ? 672 GLU A CD 1 ATOM 5138 O OE1 . GLU A 1 631 ? 14.303 62.361 54.633 1.00 18.00 ? 672 GLU A OE1 1 ATOM 5139 O OE2 . GLU A 1 631 ? 14.082 63.443 52.730 1.00 16.79 ? 672 GLU A OE2 1 ATOM 5140 N N . ARG A 1 632 ? 8.893 64.928 54.516 1.00 14.82 ? 673 ARG A N 1 ATOM 5141 C CA . ARG A 1 632 ? 7.670 65.043 53.753 1.00 12.75 ? 673 ARG A CA 1 ATOM 5142 C C . ARG A 1 632 ? 7.615 66.345 52.945 1.00 13.67 ? 673 ARG A C 1 ATOM 5143 O O . ARG A 1 632 ? 7.007 66.422 51.868 1.00 14.65 ? 673 ARG A O 1 ATOM 5144 C CB . ARG A 1 632 ? 6.413 64.922 54.650 1.00 14.14 ? 673 ARG A CB 1 ATOM 5145 C CG . ARG A 1 632 ? 5.230 64.276 53.905 1.00 14.04 ? 673 ARG A CG 1 ATOM 5146 C CD . ARG A 1 632 ? 5.341 62.716 54.003 1.00 15.39 ? 673 ARG A CD 1 ATOM 5147 N NE . ARG A 1 632 ? 4.956 62.234 55.381 1.00 13.13 ? 673 ARG A NE 1 ATOM 5148 C CZ . ARG A 1 632 ? 5.752 61.690 56.278 1.00 14.88 ? 673 ARG A CZ 1 ATOM 5149 N NH1 . ARG A 1 632 ? 7.106 61.593 56.101 1.00 15.58 ? 673 ARG A NH1 1 ATOM 5150 N NH2 . ARG A 1 632 ? 5.168 61.303 57.439 1.00 15.42 ? 673 ARG A NH2 1 ATOM 5151 N N . ALA A 1 633 ? 8.253 67.378 53.517 1.00 12.94 ? 674 ALA A N 1 ATOM 5152 C CA . ALA A 1 633 ? 8.149 68.691 52.923 1.00 13.67 ? 674 ALA A CA 1 ATOM 5153 C C . ALA A 1 633 ? 8.899 68.768 51.602 1.00 13.70 ? 674 ALA A C 1 ATOM 5154 O O . ALA A 1 633 ? 8.669 69.698 50.811 1.00 16.39 ? 674 ALA A O 1 ATOM 5155 C CB . ALA A 1 633 ? 8.693 69.695 53.895 1.00 14.97 ? 674 ALA A CB 1 ATOM 5156 N N . PHE A 1 634 ? 9.822 67.813 51.334 1.00 13.95 ? 675 PHE A N 1 ATOM 5157 C CA . PHE A 1 634 ? 10.539 67.873 50.053 1.00 13.27 ? 675 PHE A CA 1 ATOM 5158 C C . PHE A 1 634 ? 9.754 67.278 48.915 1.00 13.93 ? 675 PHE A C 1 ATOM 5159 O O . PHE A 1 634 ? 10.207 67.290 47.766 1.00 14.55 ? 675 PHE A O 1 ATOM 5160 C CB . PHE A 1 634 ? 11.890 67.154 50.163 1.00 13.99 ? 675 PHE A CB 1 ATOM 5161 C CG . PHE A 1 634 ? 12.840 67.888 51.065 1.00 14.21 ? 675 PHE A CG 1 ATOM 5162 C CD1 . PHE A 1 634 ? 13.289 69.155 50.691 1.00 14.72 ? 675 PHE A CD1 1 ATOM 5163 C CD2 . PHE A 1 634 ? 13.244 67.339 52.289 1.00 17.54 ? 675 PHE A CD2 1 ATOM 5164 C CE1 . PHE A 1 634 ? 14.204 69.903 51.540 1.00 15.65 ? 675 PHE A CE1 1 ATOM 5165 C CE2 . PHE A 1 634 ? 14.110 68.061 53.144 1.00 16.31 ? 675 PHE A CE2 1 ATOM 5166 C CZ . PHE A 1 634 ? 14.598 69.366 52.769 1.00 15.10 ? 675 PHE A CZ 1 ATOM 5167 N N . ILE A 1 635 ? 8.560 66.773 49.186 1.00 13.13 ? 676 ILE A N 1 ATOM 5168 C CA . ILE A 1 635 ? 7.720 66.207 48.126 1.00 13.65 ? 676 ILE A CA 1 ATOM 5169 C C . ILE A 1 635 ? 7.002 67.335 47.361 1.00 13.90 ? 676 ILE A C 1 ATOM 5170 O O . ILE A 1 635 ? 6.437 68.256 47.990 1.00 16.75 ? 676 ILE A O 1 ATOM 5171 C CB . ILE A 1 635 ? 6.663 65.264 48.807 1.00 13.76 ? 676 ILE A CB 1 ATOM 5172 C CG1 . ILE A 1 635 ? 7.403 64.056 49.384 1.00 14.03 ? 676 ILE A CG1 1 ATOM 5173 C CG2 . ILE A 1 635 ? 5.495 64.836 47.824 1.00 15.47 ? 676 ILE A CG2 1 ATOM 5174 C CD1 . ILE A 1 635 ? 8.140 63.206 48.330 1.00 14.59 ? 676 ILE A CD1 1 ATOM 5175 N N . ASP A 1 636 ? 6.984 67.226 46.028 1.00 14.38 ? 677 ASP A N 1 ATOM 5176 C CA . ASP A 1 636 ? 6.182 68.104 45.179 1.00 15.31 ? 677 ASP A CA 1 ATOM 5177 C C . ASP A 1 636 ? 5.021 67.282 44.629 1.00 14.81 ? 677 ASP A C 1 ATOM 5178 O O . ASP A 1 636 ? 5.231 66.272 44.010 1.00 14.13 ? 677 ASP A O 1 ATOM 5179 C CB . ASP A 1 636 ? 7.062 68.584 44.027 1.00 15.18 ? 677 ASP A CB 1 ATOM 5180 C CG . ASP A 1 636 ? 6.380 69.629 43.178 1.00 14.14 ? 677 ASP A CG 1 ATOM 5181 O OD1 . ASP A 1 636 ? 5.107 69.598 43.111 1.00 15.64 ? 677 ASP A OD1 1 ATOM 5182 O OD2 . ASP A 1 636 ? 7.153 70.399 42.557 1.00 15.87 ? 677 ASP A OD2 1 ATOM 5183 N N . PRO A 1 637 ? 3.790 67.680 44.921 1.00 17.55 ? 678 PRO A N 1 ATOM 5184 C CA . PRO A 1 637 ? 2.707 66.822 44.550 1.00 18.23 ? 678 PRO A CA 1 ATOM 5185 C C . PRO A 1 637 ? 2.616 66.719 42.999 1.00 20.02 ? 678 PRO A C 1 ATOM 5186 O O . PRO A 1 637 ? 2.006 65.776 42.450 1.00 23.94 ? 678 PRO A O 1 ATOM 5187 C CB . PRO A 1 637 ? 1.450 67.560 45.116 1.00 18.46 ? 678 PRO A CB 1 ATOM 5188 C CG . PRO A 1 637 ? 1.861 68.902 45.422 1.00 20.70 ? 678 PRO A CG 1 ATOM 5189 C CD . PRO A 1 637 ? 3.379 68.896 45.632 1.00 18.51 ? 678 PRO A CD 1 ATOM 5190 N N . LEU A 1 638 ? 3.261 67.623 42.279 1.00 16.54 ? 679 LEU A N 1 ATOM 5191 C CA . LEU A 1 638 ? 3.166 67.508 40.804 1.00 16.29 ? 679 LEU A CA 1 ATOM 5192 C C . LEU A 1 638 ? 4.217 66.556 40.193 1.00 16.98 ? 679 LEU A C 1 ATOM 5193 O O . LEU A 1 638 ? 4.205 66.280 38.961 1.00 17.35 ? 679 LEU A O 1 ATOM 5194 C CB . LEU A 1 638 ? 3.348 68.898 40.192 1.00 16.98 ? 679 LEU A CB 1 ATOM 5195 C CG . LEU A 1 638 ? 2.227 69.892 40.591 1.00 19.01 ? 679 LEU A CG 1 ATOM 5196 C CD1 . LEU A 1 638 ? 2.420 71.303 39.965 1.00 19.78 ? 679 LEU A CD1 1 ATOM 5197 C CD2 . LEU A 1 638 ? 0.816 69.355 40.274 1.00 20.27 ? 679 LEU A CD2 1 ATOM 5198 N N . GLY A 1 639 ? 5.157 66.084 41.021 1.00 16.32 ? 680 GLY A N 1 ATOM 5199 C CA . GLY A 1 639 ? 6.158 65.142 40.568 1.00 16.70 ? 680 GLY A CA 1 ATOM 5200 C C . GLY A 1 639 ? 7.244 65.818 39.729 1.00 17.85 ? 680 GLY A C 1 ATOM 5201 O O . GLY A 1 639 ? 7.182 67.020 39.454 1.00 19.03 ? 680 GLY A O 1 ATOM 5202 N N . LEU A 1 640 ? 8.237 65.048 39.281 1.00 16.55 ? 681 LEU A N 1 ATOM 5203 C CA . LEU A 1 640 ? 9.248 65.591 38.379 1.00 16.59 ? 681 LEU A CA 1 ATOM 5204 C C . LEU A 1 640 ? 8.777 65.377 36.967 1.00 17.25 ? 681 LEU A C 1 ATOM 5205 O O . LEU A 1 640 ? 7.882 64.554 36.699 1.00 17.30 ? 681 LEU A O 1 ATOM 5206 C CB . LEU A 1 640 ? 10.538 64.788 38.610 1.00 16.13 ? 681 LEU A CB 1 ATOM 5207 C CG . LEU A 1 640 ? 11.182 65.112 39.963 1.00 16.08 ? 681 LEU A CG 1 ATOM 5208 C CD1 . LEU A 1 640 ? 12.284 64.114 40.229 1.00 20.20 ? 681 LEU A CD1 1 ATOM 5209 C CD2 . LEU A 1 640 ? 11.811 66.571 40.023 1.00 20.34 ? 681 LEU A CD2 1 ATOM 5210 N N . PRO A 1 641 ? 9.362 66.096 36.004 1.00 19.66 ? 682 PRO A N 1 ATOM 5211 C CA . PRO A 1 641 ? 8.900 66.012 34.615 1.00 19.16 ? 682 PRO A CA 1 ATOM 5212 C C . PRO A 1 641 ? 8.804 64.608 34.029 1.00 19.04 ? 682 PRO A C 1 ATOM 5213 O O . PRO A 1 641 ? 9.787 63.873 33.982 1.00 19.62 ? 682 PRO A O 1 ATOM 5214 C CB . PRO A 1 641 ? 9.947 66.883 33.849 1.00 20.67 ? 682 PRO A CB 1 ATOM 5215 C CG . PRO A 1 641 ? 10.393 67.837 34.863 1.00 21.06 ? 682 PRO A CG 1 ATOM 5216 C CD . PRO A 1 641 ? 10.475 67.044 36.166 1.00 20.54 ? 682 PRO A CD 1 ATOM 5217 N N . ASP A 1 642 ? 7.588 64.222 33.625 1.00 20.06 ? 683 ASP A N 1 ATOM 5218 C CA . ASP A 1 642 ? 7.301 62.924 33.033 1.00 20.17 ? 683 ASP A CA 1 ATOM 5219 C C . ASP A 1 642 ? 7.547 61.741 33.950 1.00 18.01 ? 683 ASP A C 1 ATOM 5220 O O . ASP A 1 642 ? 7.483 60.580 33.513 1.00 19.24 ? 683 ASP A O 1 ATOM 5221 C CB . ASP A 1 642 ? 8.033 62.708 31.701 1.00 22.25 ? 683 ASP A CB 1 ATOM 5222 C CG . ASP A 1 642 ? 7.699 63.785 30.683 1.00 30.12 ? 683 ASP A CG 1 ATOM 5223 O OD1 . ASP A 1 642 ? 6.493 64.071 30.486 1.00 30.80 ? 683 ASP A OD1 1 ATOM 5224 O OD2 . ASP A 1 642 ? 8.662 64.334 30.114 1.00 37.30 ? 683 ASP A OD2 1 ATOM 5225 N N . ARG A 1 643 ? 7.763 62.039 35.248 1.00 16.63 ? 684 ARG A N 1 ATOM 5226 C CA . ARG A 1 643 ? 7.971 60.954 36.250 1.00 15.70 ? 684 ARG A CA 1 ATOM 5227 C C . ARG A 1 643 ? 7.144 61.309 37.495 1.00 15.20 ? 684 ARG A C 1 ATOM 5228 O O . ARG A 1 643 ? 7.652 61.707 38.554 1.00 14.50 ? 684 ARG A O 1 ATOM 5229 C CB . ARG A 1 643 ? 9.465 60.818 36.585 1.00 15.16 ? 684 ARG A CB 1 ATOM 5230 C CG . ARG A 1 643 ? 10.272 60.380 35.328 1.00 15.05 ? 684 ARG A CG 1 ATOM 5231 C CD . ARG A 1 643 ? 11.700 59.929 35.696 1.00 15.21 ? 684 ARG A CD 1 ATOM 5232 N NE . ARG A 1 643 ? 12.484 61.037 36.288 1.00 17.73 ? 684 ARG A NE 1 ATOM 5233 C CZ . ARG A 1 643 ? 13.650 60.918 36.937 1.00 18.27 ? 684 ARG A CZ 1 ATOM 5234 N NH1 . ARG A 1 643 ? 14.264 59.727 37.123 1.00 15.46 ? 684 ARG A NH1 1 ATOM 5235 N NH2 . ARG A 1 643 ? 14.227 62.048 37.437 1.00 16.22 ? 684 ARG A NH2 1 ATOM 5236 N N . PRO A 1 644 ? 5.820 61.157 37.388 1.00 14.90 ? 685 PRO A N 1 ATOM 5237 C CA . PRO A 1 644 ? 4.908 61.659 38.418 1.00 14.37 ? 685 PRO A CA 1 ATOM 5238 C C . PRO A 1 644 ? 5.081 60.962 39.748 1.00 13.63 ? 685 PRO A C 1 ATOM 5239 O O . PRO A 1 644 ? 4.607 61.514 40.758 1.00 15.81 ? 685 PRO A O 1 ATOM 5240 C CB . PRO A 1 644 ? 3.489 61.302 37.896 1.00 15.07 ? 685 PRO A CB 1 ATOM 5241 C CG . PRO A 1 644 ? 3.683 60.288 36.764 1.00 15.95 ? 685 PRO A CG 1 ATOM 5242 C CD . PRO A 1 644 ? 5.147 60.548 36.240 1.00 15.94 ? 685 PRO A CD 1 ATOM 5243 N N . PHE A 1 645 ? 5.680 59.763 39.761 1.00 13.27 ? 686 PHE A N 1 ATOM 5244 C CA . PHE A 1 645 ? 5.875 59.035 41.058 1.00 11.99 ? 686 PHE A CA 1 ATOM 5245 C C . PHE A 1 645 ? 7.235 59.281 41.700 1.00 13.38 ? 686 PHE A C 1 ATOM 5246 O O . PHE A 1 645 ? 7.458 58.786 42.818 1.00 14.39 ? 686 PHE A O 1 ATOM 5247 C CB . PHE A 1 645 ? 5.599 57.530 40.866 1.00 13.17 ? 686 PHE A CB 1 ATOM 5248 C CG . PHE A 1 645 ? 4.177 57.288 40.380 1.00 14.09 ? 686 PHE A CG 1 ATOM 5249 C CD1 . PHE A 1 645 ? 3.104 57.664 41.158 1.00 15.71 ? 686 PHE A CD1 1 ATOM 5250 C CD2 . PHE A 1 645 ? 3.953 56.739 39.122 1.00 15.02 ? 686 PHE A CD2 1 ATOM 5251 C CE1 . PHE A 1 645 ? 1.789 57.472 40.719 1.00 13.49 ? 686 PHE A CE1 1 ATOM 5252 C CE2 . PHE A 1 645 ? 2.634 56.536 38.664 1.00 14.04 ? 686 PHE A CE2 1 ATOM 5253 C CZ . PHE A 1 645 ? 1.561 56.883 39.450 1.00 13.40 ? 686 PHE A CZ 1 ATOM 5254 N N . TYR A 1 646 ? 8.066 60.113 41.062 1.00 11.79 ? 687 TYR A N 1 ATOM 5255 C CA . TYR A 1 646 ? 9.261 60.614 41.710 1.00 12.70 ? 687 TYR A CA 1 ATOM 5256 C C . TYR A 1 646 ? 8.949 62.048 42.079 1.00 13.73 ? 687 TYR A C 1 ATOM 5257 O O . TYR A 1 646 ? 8.973 62.970 41.249 1.00 14.65 ? 687 TYR A O 1 ATOM 5258 C CB . TYR A 1 646 ? 10.508 60.525 40.776 1.00 12.67 ? 687 TYR A CB 1 ATOM 5259 C CG . TYR A 1 646 ? 10.953 59.099 40.473 1.00 13.27 ? 687 TYR A CG 1 ATOM 5260 C CD1 . TYR A 1 646 ? 10.686 58.050 41.366 1.00 14.82 ? 687 TYR A CD1 1 ATOM 5261 C CD2 . TYR A 1 646 ? 11.660 58.824 39.295 1.00 13.22 ? 687 TYR A CD2 1 ATOM 5262 C CE1 . TYR A 1 646 ? 11.081 56.748 41.093 1.00 14.16 ? 687 TYR A CE1 1 ATOM 5263 C CE2 . TYR A 1 646 ? 12.086 57.517 39.013 1.00 13.85 ? 687 TYR A CE2 1 ATOM 5264 C CZ . TYR A 1 646 ? 11.798 56.494 39.926 1.00 14.70 ? 687 TYR A CZ 1 ATOM 5265 O OH . TYR A 1 646 ? 12.252 55.230 39.631 1.00 15.37 ? 687 TYR A OH 1 ATOM 5266 N N . ARG A 1 647 ? 8.608 62.215 43.348 1.00 12.06 ? 688 ARG A N 1 ATOM 5267 C CA A ARG A 1 647 ? 8.067 63.481 43.831 0.50 12.43 ? 688 ARG A CA 1 ATOM 5268 C CA B ARG A 1 647 ? 8.044 63.470 43.851 0.50 13.26 ? 688 ARG A CA 1 ATOM 5269 C C . ARG A 1 647 ? 9.021 64.245 44.753 1.00 13.28 ? 688 ARG A C 1 ATOM 5270 O O . ARG A 1 647 ? 8.806 65.429 45.037 1.00 14.76 ? 688 ARG A O 1 ATOM 5271 C CB A ARG A 1 647 ? 6.752 63.224 44.576 0.50 12.95 ? 688 ARG A CB 1 ATOM 5272 C CB B ARG A 1 647 ? 6.722 63.215 44.624 0.50 13.98 ? 688 ARG A CB 1 ATOM 5273 C CG A ARG A 1 647 ? 5.819 62.377 43.699 0.50 8.58 ? 688 ARG A CG 1 ATOM 5274 C CG B ARG A 1 647 ? 5.537 62.831 43.667 0.50 14.18 ? 688 ARG A CG 1 ATOM 5275 C CD A ARG A 1 647 ? 4.327 62.574 44.082 0.50 9.70 ? 688 ARG A CD 1 ATOM 5276 C CD B ARG A 1 647 ? 4.295 62.241 44.389 0.50 19.40 ? 688 ARG A CD 1 ATOM 5277 N NE A ARG A 1 647 ? 4.154 62.199 45.506 0.50 8.50 ? 688 ARG A NE 1 ATOM 5278 N NE B ARG A 1 647 ? 3.302 61.510 43.564 0.50 18.49 ? 688 ARG A NE 1 ATOM 5279 C CZ A ARG A 1 647 ? 3.135 62.475 46.324 0.50 11.78 ? 688 ARG A CZ 1 ATOM 5280 C CZ B ARG A 1 647 ? 2.261 60.833 44.117 0.50 19.29 ? 688 ARG A CZ 1 ATOM 5281 N NH1 A ARG A 1 647 ? 3.244 62.069 47.629 0.50 7.72 ? 688 ARG A NH1 1 ATOM 5282 N NH1 B ARG A 1 647 ? 1.349 60.144 43.420 0.50 14.69 ? 688 ARG A NH1 1 ATOM 5283 N NH2 A ARG A 1 647 ? 2.065 63.177 45.895 0.50 11.23 ? 688 ARG A NH2 1 ATOM 5284 N NH2 B ARG A 1 647 ? 2.165 60.768 45.426 0.50 22.22 ? 688 ARG A NH2 1 ATOM 5285 N N . HIS A 1 648 ? 10.105 63.590 45.196 1.00 13.02 ? 689 HIS A N 1 ATOM 5286 C CA . HIS A 1 648 ? 11.022 64.236 46.124 1.00 13.26 ? 689 HIS A CA 1 ATOM 5287 C C . HIS A 1 648 ? 11.879 65.177 45.249 1.00 14.36 ? 689 HIS A C 1 ATOM 5288 O O . HIS A 1 648 ? 12.418 64.773 44.234 1.00 14.88 ? 689 HIS A O 1 ATOM 5289 C CB . HIS A 1 648 ? 11.929 63.153 46.710 1.00 12.90 ? 689 HIS A CB 1 ATOM 5290 C CG . HIS A 1 648 ? 12.593 63.550 47.974 1.00 13.61 ? 689 HIS A CG 1 ATOM 5291 N ND1 . HIS A 1 648 ? 13.569 64.534 48.047 1.00 13.06 ? 689 HIS A ND1 1 ATOM 5292 C CD2 . HIS A 1 648 ? 12.393 63.109 49.240 1.00 13.82 ? 689 HIS A CD2 1 ATOM 5293 C CE1 . HIS A 1 648 ? 13.974 64.647 49.311 1.00 15.48 ? 689 HIS A CE1 1 ATOM 5294 N NE2 . HIS A 1 648 ? 13.279 63.801 50.057 1.00 13.81 ? 689 HIS A NE2 1 ATOM 5295 N N . VAL A 1 649 ? 12.026 66.425 45.684 1.00 13.15 ? 690 VAL A N 1 ATOM 5296 C CA . VAL A 1 649 ? 12.686 67.427 44.834 1.00 13.13 ? 690 VAL A CA 1 ATOM 5297 C C . VAL A 1 649 ? 14.203 67.373 45.042 1.00 14.23 ? 690 VAL A C 1 ATOM 5298 O O . VAL A 1 649 ? 14.964 67.826 44.203 1.00 15.52 ? 690 VAL A O 1 ATOM 5299 C CB . VAL A 1 649 ? 12.110 68.809 45.140 1.00 13.49 ? 690 VAL A CB 1 ATOM 5300 C CG1 . VAL A 1 649 ? 12.903 69.937 44.406 1.00 13.83 ? 690 VAL A CG1 1 ATOM 5301 C CG2 . VAL A 1 649 ? 10.645 68.884 44.679 1.00 14.85 ? 690 VAL A CG2 1 ATOM 5302 N N . ILE A 1 650 ? 14.625 66.825 46.163 1.00 13.07 ? 691 ILE A N 1 ATOM 5303 C CA . ILE A 1 650 ? 16.085 66.772 46.394 1.00 13.40 ? 691 ILE A CA 1 ATOM 5304 C C . ILE A 1 650 ? 16.707 65.525 45.784 1.00 15.01 ? 691 ILE A C 1 ATOM 5305 O O . ILE A 1 650 ? 17.835 65.581 45.327 1.00 15.03 ? 691 ILE A O 1 ATOM 5306 C CB . ILE A 1 650 ? 16.422 66.796 47.927 1.00 13.55 ? 691 ILE A CB 1 ATOM 5307 C CG1 . ILE A 1 650 ? 15.695 67.927 48.660 1.00 14.00 ? 691 ILE A CG1 1 ATOM 5308 C CG2 . ILE A 1 650 ? 17.989 66.996 48.084 1.00 16.55 ? 691 ILE A CG2 1 ATOM 5309 C CD1 . ILE A 1 650 ? 15.863 69.321 48.050 1.00 15.43 ? 691 ILE A CD1 1 ATOM 5310 N N . TYR A 1 651 ? 15.983 64.384 45.877 1.00 14.25 ? 692 TYR A N 1 ATOM 5311 C CA . TYR A 1 651 ? 16.553 63.090 45.467 1.00 14.26 ? 692 TYR A CA 1 ATOM 5312 C C . TYR A 1 651 ? 15.631 62.334 44.525 1.00 15.64 ? 692 TYR A C 1 ATOM 5313 O O . TYR A 1 651 ? 14.440 62.106 44.850 1.00 15.74 ? 692 TYR A O 1 ATOM 5314 C CB . TYR A 1 651 ? 16.673 62.200 46.729 1.00 14.31 ? 692 TYR A CB 1 ATOM 5315 C CG . TYR A 1 651 ? 17.750 62.641 47.694 1.00 14.03 ? 692 TYR A CG 1 ATOM 5316 C CD1 . TYR A 1 651 ? 19.115 62.673 47.309 1.00 16.15 ? 692 TYR A CD1 1 ATOM 5317 C CD2 . TYR A 1 651 ? 17.419 62.923 49.055 1.00 14.41 ? 692 TYR A CD2 1 ATOM 5318 C CE1 . TYR A 1 651 ? 20.088 63.047 48.217 1.00 17.13 ? 692 TYR A CE1 1 ATOM 5319 C CE2 . TYR A 1 651 ? 18.387 63.304 49.945 1.00 16.22 ? 692 TYR A CE2 1 ATOM 5320 C CZ . TYR A 1 651 ? 19.723 63.305 49.527 1.00 18.07 ? 692 TYR A CZ 1 ATOM 5321 O OH . TYR A 1 651 ? 20.742 63.626 50.421 1.00 18.63 ? 692 TYR A OH 1 ATOM 5322 N N . ALA A 1 652 ? 16.158 61.919 43.364 1.00 13.86 ? 693 ALA A N 1 ATOM 5323 C CA . ALA A 1 652 ? 15.441 60.935 42.575 1.00 15.01 ? 693 ALA A CA 1 ATOM 5324 C C . ALA A 1 652 ? 16.439 59.929 42.034 1.00 15.29 ? 693 ALA A C 1 ATOM 5325 O O . ALA A 1 652 ? 17.653 60.169 42.028 1.00 15.86 ? 693 ALA A O 1 ATOM 5326 C CB . ALA A 1 652 ? 14.746 61.601 41.386 1.00 15.31 ? 693 ALA A CB 1 ATOM 5327 N N . PRO A 1 653 ? 15.960 58.765 41.600 1.00 14.26 ? 694 PRO A N 1 ATOM 5328 C CA . PRO A 1 653 ? 16.875 57.838 40.909 1.00 14.94 ? 694 PRO A CA 1 ATOM 5329 C C . PRO A 1 653 ? 17.374 58.513 39.633 1.00 15.58 ? 694 PRO A C 1 ATOM 5330 O O . PRO A 1 653 ? 16.622 59.199 38.936 1.00 15.72 ? 694 PRO A O 1 ATOM 5331 C CB . PRO A 1 653 ? 15.948 56.638 40.569 1.00 15.60 ? 694 PRO A CB 1 ATOM 5332 C CG . PRO A 1 653 ? 14.800 56.785 41.553 1.00 16.26 ? 694 PRO A CG 1 ATOM 5333 C CD . PRO A 1 653 ? 14.569 58.269 41.604 1.00 14.68 ? 694 PRO A CD 1 ATOM 5334 N N . SER A 1 654 ? 18.648 58.311 39.325 1.00 14.01 ? 695 SER A N 1 ATOM 5335 C CA . SER A 1 654 ? 19.183 58.891 38.099 1.00 15.04 ? 695 SER A CA 1 ATOM 5336 C C . SER A 1 654 ? 18.401 58.464 36.876 1.00 15.81 ? 695 SER A C 1 ATOM 5337 O O . SER A 1 654 ? 18.091 57.280 36.684 1.00 15.36 ? 695 SER A O 1 ATOM 5338 C CB . SER A 1 654 ? 20.680 58.486 37.944 1.00 15.94 ? 695 SER A CB 1 ATOM 5339 O OG . SER A 1 654 ? 21.100 58.871 36.623 1.00 18.12 ? 695 SER A OG 1 ATOM 5340 N N . SER A 1 655 ? 18.082 59.406 35.996 1.00 15.59 ? 696 SER A N 1 ATOM 5341 C CA . SER A 1 655 ? 17.380 59.082 34.731 1.00 17.38 ? 696 SER A CA 1 ATOM 5342 C C . SER A 1 655 ? 18.230 58.173 33.802 1.00 17.36 ? 696 SER A C 1 ATOM 5343 O O . SER A 1 655 ? 17.670 57.627 32.798 1.00 18.44 ? 696 SER A O 1 ATOM 5344 C CB . SER A 1 655 ? 16.949 60.386 34.007 1.00 18.09 ? 696 SER A CB 1 ATOM 5345 O OG A SER A 1 655 ? 15.948 61.084 34.741 0.50 10.99 ? 696 SER A OG 1 ATOM 5346 O OG B SER A 1 655 ? 18.037 61.176 33.620 0.50 24.82 ? 696 SER A OG 1 ATOM 5347 N N . HIS A 1 656 ? 19.524 58.060 34.131 1.00 17.32 ? 697 HIS A N 1 ATOM 5348 C CA . HIS A 1 656 ? 20.457 57.212 33.360 1.00 17.99 ? 697 HIS A CA 1 ATOM 5349 C C . HIS A 1 656 ? 20.800 55.917 34.036 1.00 18.95 ? 697 HIS A C 1 ATOM 5350 O O . HIS A 1 656 ? 21.458 55.045 33.436 1.00 20.21 ? 697 HIS A O 1 ATOM 5351 C CB . HIS A 1 656 ? 21.729 58.036 33.080 1.00 19.16 ? 697 HIS A CB 1 ATOM 5352 C CG . HIS A 1 656 ? 21.404 59.318 32.394 1.00 19.35 ? 697 HIS A CG 1 ATOM 5353 N ND1 . HIS A 1 656 ? 21.189 59.405 31.030 1.00 21.63 ? 697 HIS A ND1 1 ATOM 5354 C CD2 . HIS A 1 656 ? 21.169 60.555 32.897 1.00 19.43 ? 697 HIS A CD2 1 ATOM 5355 C CE1 . HIS A 1 656 ? 20.848 60.650 30.724 1.00 22.02 ? 697 HIS A CE1 1 ATOM 5356 N NE2 . HIS A 1 656 ? 20.796 61.358 31.845 1.00 21.31 ? 697 HIS A NE2 1 ATOM 5357 N N . ASN A 1 657 ? 20.378 55.765 35.293 1.00 16.64 ? 698 ASN A N 1 ATOM 5358 C CA . ASN A 1 657 ? 20.775 54.566 36.026 1.00 16.45 ? 698 ASN A CA 1 ATOM 5359 C C . ASN A 1 657 ? 19.953 54.539 37.310 1.00 15.16 ? 698 ASN A C 1 ATOM 5360 O O . ASN A 1 657 ? 20.272 55.204 38.288 1.00 16.45 ? 698 ASN A O 1 ATOM 5361 C CB . ASN A 1 657 ? 22.237 54.688 36.449 1.00 16.92 ? 698 ASN A CB 1 ATOM 5362 C CG . ASN A 1 657 ? 22.679 53.542 37.397 1.00 16.57 ? 698 ASN A CG 1 ATOM 5363 O OD1 . ASN A 1 657 ? 21.947 52.564 37.553 1.00 17.43 ? 698 ASN A OD1 1 ATOM 5364 N ND2 . ASN A 1 657 ? 23.911 53.650 38.006 1.00 18.75 ? 698 ASN A ND2 1 ATOM 5365 N N . LYS A 1 658 ? 18.867 53.761 37.288 1.00 16.07 ? 699 LYS A N 1 ATOM 5366 C CA . LYS A 1 658 ? 17.965 53.667 38.433 1.00 16.21 ? 699 LYS A CA 1 ATOM 5367 C C . LYS A 1 658 ? 18.657 53.333 39.726 1.00 16.09 ? 699 LYS A C 1 ATOM 5368 O O . LYS A 1 658 ? 18.166 53.710 40.817 1.00 15.90 ? 699 LYS A O 1 ATOM 5369 C CB . LYS A 1 658 ? 16.954 52.579 38.103 1.00 17.21 ? 699 LYS A CB 1 ATOM 5370 C CG . LYS A 1 658 ? 15.812 52.555 39.130 1.00 16.45 ? 699 LYS A CG 1 ATOM 5371 C CD . LYS A 1 658 ? 14.814 51.465 38.678 1.00 16.07 ? 699 LYS A CD 1 ATOM 5372 C CE . LYS A 1 658 ? 13.461 51.617 39.445 1.00 17.39 ? 699 LYS A CE 1 ATOM 5373 N NZ . LYS A 1 658 ? 12.506 50.481 39.157 1.00 16.36 ? 699 LYS A NZ 1 ATOM 5374 N N . TYR A 1 659 ? 19.827 52.642 39.663 1.00 15.16 ? 700 TYR A N 1 ATOM 5375 C CA . TYR A 1 659 ? 20.460 52.341 40.978 1.00 15.25 ? 700 TYR A CA 1 ATOM 5376 C C . TYR A 1 659 ? 21.067 53.534 41.682 1.00 16.65 ? 700 TYR A C 1 ATOM 5377 O O . TYR A 1 659 ? 21.244 53.519 42.910 1.00 17.66 ? 700 TYR A O 1 ATOM 5378 C CB . TYR A 1 659 ? 21.553 51.307 40.851 1.00 16.27 ? 700 TYR A CB 1 ATOM 5379 C CG . TYR A 1 659 ? 21.100 49.934 40.391 1.00 15.41 ? 700 TYR A CG 1 ATOM 5380 C CD1 . TYR A 1 659 ? 19.968 49.313 40.936 1.00 14.85 ? 700 TYR A CD1 1 ATOM 5381 C CD2 . TYR A 1 659 ? 21.855 49.226 39.421 1.00 17.65 ? 700 TYR A CD2 1 ATOM 5382 C CE1 . TYR A 1 659 ? 19.555 48.008 40.495 1.00 15.55 ? 700 TYR A CE1 1 ATOM 5383 C CE2 . TYR A 1 659 ? 21.459 47.931 38.977 1.00 17.53 ? 700 TYR A CE2 1 ATOM 5384 C CZ . TYR A 1 659 ? 20.321 47.332 39.524 1.00 21.05 ? 700 TYR A CZ 1 ATOM 5385 O OH . TYR A 1 659 ? 19.957 46.070 39.095 1.00 18.03 ? 700 TYR A OH 1 ATOM 5386 N N . ALA A 1 660 ? 21.476 54.535 40.910 1.00 16.41 ? 701 ALA A N 1 ATOM 5387 C CA . ALA A 1 660 ? 22.179 55.693 41.445 1.00 17.01 ? 701 ALA A CA 1 ATOM 5388 C C . ALA A 1 660 ? 21.188 56.788 41.862 1.00 17.38 ? 701 ALA A C 1 ATOM 5389 O O . ALA A 1 660 ? 20.156 57.011 41.195 1.00 18.49 ? 701 ALA A O 1 ATOM 5390 C CB . ALA A 1 660 ? 23.094 56.245 40.365 1.00 17.13 ? 701 ALA A CB 1 ATOM 5391 N N . GLY A 1 661 ? 21.539 57.488 42.922 1.00 15.94 ? 702 GLY A N 1 ATOM 5392 C CA . GLY A 1 661 ? 20.693 58.649 43.256 1.00 16.85 ? 702 GLY A CA 1 ATOM 5393 C C . GLY A 1 661 ? 21.254 59.886 42.571 1.00 16.99 ? 702 GLY A C 1 ATOM 5394 O O . GLY A 1 661 ? 22.488 60.016 42.368 1.00 19.09 ? 702 GLY A O 1 ATOM 5395 N N . GLU A 1 662 ? 20.354 60.814 42.233 1.00 16.53 ? 703 GLU A N 1 ATOM 5396 C CA . GLU A 1 662 ? 20.760 62.134 41.732 1.00 16.15 ? 703 GLU A CA 1 ATOM 5397 C C . GLU A 1 662 ? 20.205 63.198 42.659 1.00 15.78 ? 703 GLU A C 1 ATOM 5398 O O . GLU A 1 662 ? 19.072 63.078 43.087 1.00 16.39 ? 703 GLU A O 1 ATOM 5399 C CB . GLU A 1 662 ? 20.210 62.356 40.317 1.00 16.84 ? 703 GLU A CB 1 ATOM 5400 C CG . GLU A 1 662 ? 20.808 63.593 39.616 1.00 17.99 ? 703 GLU A CG 1 ATOM 5401 C CD . GLU A 1 662 ? 22.333 63.547 39.668 1.00 20.35 ? 703 GLU A CD 1 ATOM 5402 O OE1 . GLU A 1 662 ? 22.906 62.762 38.889 1.00 18.95 ? 703 GLU A OE1 1 ATOM 5403 O OE2 . GLU A 1 662 ? 22.950 64.228 40.555 1.00 21.02 ? 703 GLU A OE2 1 ATOM 5404 N N . SER A 1 663 ? 21.003 64.238 42.930 1.00 15.32 ? 704 SER A N 1 ATOM 5405 C CA . SER A 1 663 ? 20.543 65.362 43.767 1.00 15.72 ? 704 SER A CA 1 ATOM 5406 C C . SER A 1 663 ? 20.049 66.480 42.863 1.00 16.88 ? 704 SER A C 1 ATOM 5407 O O . SER A 1 663 ? 20.484 66.607 41.712 1.00 16.53 ? 704 SER A O 1 ATOM 5408 C CB . SER A 1 663 ? 21.663 65.830 44.699 1.00 18.37 ? 704 SER A CB 1 ATOM 5409 O OG . SER A 1 663 ? 22.844 66.133 43.960 1.00 19.00 ? 704 SER A OG 1 ATOM 5410 N N . PHE A 1 664 ? 19.064 67.259 43.346 1.00 15.36 ? 705 PHE A N 1 ATOM 5411 C CA . PHE A 1 664 ? 18.378 68.278 42.515 1.00 15.36 ? 705 PHE A CA 1 ATOM 5412 C C . PHE A 1 664 ? 18.121 67.720 41.111 1.00 15.50 ? 705 PHE A C 1 ATOM 5413 O O . PHE A 1 664 ? 18.464 68.319 40.092 1.00 15.87 ? 705 PHE A O 1 ATOM 5414 C CB . PHE A 1 664 ? 19.147 69.623 42.478 1.00 15.17 ? 705 PHE A CB 1 ATOM 5415 C CG . PHE A 1 664 ? 19.090 70.334 43.796 1.00 14.39 ? 705 PHE A CG 1 ATOM 5416 C CD1 . PHE A 1 664 ? 17.872 70.647 44.354 1.00 15.51 ? 705 PHE A CD1 1 ATOM 5417 C CD2 . PHE A 1 664 ? 20.236 70.704 44.465 1.00 15.90 ? 705 PHE A CD2 1 ATOM 5418 C CE1 . PHE A 1 664 ? 17.754 71.291 45.591 1.00 14.07 ? 705 PHE A CE1 1 ATOM 5419 C CE2 . PHE A 1 664 ? 20.172 71.359 45.718 1.00 16.29 ? 705 PHE A CE2 1 ATOM 5420 C CZ . PHE A 1 664 ? 18.929 71.681 46.291 1.00 16.27 ? 705 PHE A CZ 1 ATOM 5421 N N . PRO A 1 665 ? 17.432 66.568 41.062 1.00 14.30 ? 706 PRO A N 1 ATOM 5422 C CA . PRO A 1 665 ? 17.260 65.890 39.784 1.00 14.73 ? 706 PRO A CA 1 ATOM 5423 C C . PRO A 1 665 ? 16.557 66.702 38.743 1.00 14.45 ? 706 PRO A C 1 ATOM 5424 O O . PRO A 1 665 ? 16.835 66.525 37.551 1.00 15.53 ? 706 PRO A O 1 ATOM 5425 C CB . PRO A 1 665 ? 16.372 64.646 40.160 1.00 15.33 ? 706 PRO A CB 1 ATOM 5426 C CG . PRO A 1 665 ? 15.704 65.007 41.477 1.00 15.31 ? 706 PRO A CG 1 ATOM 5427 C CD . PRO A 1 665 ? 16.784 65.830 42.180 1.00 16.39 ? 706 PRO A CD 1 ATOM 5428 N N . GLY A 1 666 ? 15.607 67.552 39.138 1.00 14.24 ? 707 GLY A N 1 ATOM 5429 C CA . GLY A 1 666 ? 14.864 68.317 38.089 1.00 14.65 ? 707 GLY A CA 1 ATOM 5430 C C . GLY A 1 666 ? 15.838 69.256 37.418 1.00 14.97 ? 707 GLY A C 1 ATOM 5431 O O . GLY A 1 666 ? 15.809 69.400 36.170 1.00 16.06 ? 707 GLY A O 1 ATOM 5432 N N . ILE A 1 667 ? 16.693 69.915 38.216 1.00 14.62 ? 708 ILE A N 1 ATOM 5433 C CA . ILE A 1 667 ? 17.672 70.836 37.562 1.00 15.78 ? 708 ILE A CA 1 ATOM 5434 C C . ILE A 1 667 ? 18.739 70.018 36.799 1.00 16.82 ? 708 ILE A C 1 ATOM 5435 O O . ILE A 1 667 ? 19.116 70.350 35.643 1.00 17.62 ? 708 ILE A O 1 ATOM 5436 C CB . ILE A 1 667 ? 18.409 71.732 38.597 1.00 15.27 ? 708 ILE A CB 1 ATOM 5437 C CG1 . ILE A 1 667 ? 17.400 72.454 39.511 1.00 17.38 ? 708 ILE A CG1 1 ATOM 5438 C CG2 . ILE A 1 667 ? 19.263 72.792 37.843 1.00 17.42 ? 708 ILE A CG2 1 ATOM 5439 C CD1 . ILE A 1 667 ? 18.137 73.195 40.708 1.00 17.35 ? 708 ILE A CD1 1 ATOM 5440 N N . TYR A 1 668 ? 19.180 68.905 37.386 1.00 16.74 ? 709 TYR A N 1 ATOM 5441 C CA . TYR A 1 668 ? 20.178 68.064 36.741 1.00 16.98 ? 709 TYR A CA 1 ATOM 5442 C C . TYR A 1 668 ? 19.712 67.632 35.328 1.00 16.41 ? 709 TYR A C 1 ATOM 5443 O O . TYR A 1 668 ? 20.410 67.816 34.312 1.00 17.46 ? 709 TYR A O 1 ATOM 5444 C CB . TYR A 1 668 ? 20.536 66.836 37.580 1.00 16.47 ? 709 TYR A CB 1 ATOM 5445 C CG . TYR A 1 668 ? 21.622 66.033 36.915 1.00 17.08 ? 709 TYR A CG 1 ATOM 5446 C CD1 . TYR A 1 668 ? 22.948 66.207 37.267 1.00 18.22 ? 709 TYR A CD1 1 ATOM 5447 C CD2 . TYR A 1 668 ? 21.307 65.094 35.879 1.00 18.20 ? 709 TYR A CD2 1 ATOM 5448 C CE1 . TYR A 1 668 ? 23.993 65.448 36.620 1.00 18.58 ? 709 TYR A CE1 1 ATOM 5449 C CE2 . TYR A 1 668 ? 22.330 64.336 35.227 1.00 16.89 ? 709 TYR A CE2 1 ATOM 5450 C CZ . TYR A 1 668 ? 23.676 64.547 35.599 1.00 19.18 ? 709 TYR A CZ 1 ATOM 5451 O OH . TYR A 1 668 ? 24.701 63.801 34.991 1.00 20.56 ? 709 TYR A OH 1 ATOM 5452 N N . ASP A 1 669 ? 18.499 67.073 35.242 1.00 16.15 ? 710 ASP A N 1 ATOM 5453 C CA . ASP A 1 669 ? 18.041 66.593 33.940 1.00 16.25 ? 710 ASP A CA 1 ATOM 5454 C C . ASP A 1 669 ? 17.818 67.773 32.972 1.00 17.36 ? 710 ASP A C 1 ATOM 5455 O O . ASP A 1 669 ? 17.961 67.612 31.778 1.00 19.45 ? 710 ASP A O 1 ATOM 5456 C CB . ASP A 1 669 ? 16.762 65.759 34.123 1.00 16.92 ? 710 ASP A CB 1 ATOM 5457 C CG . ASP A 1 669 ? 17.053 64.368 34.675 1.00 19.32 ? 710 ASP A CG 1 ATOM 5458 O OD1 . ASP A 1 669 ? 18.213 63.908 34.612 1.00 18.87 ? 710 ASP A OD1 1 ATOM 5459 O OD2 . ASP A 1 669 ? 16.067 63.730 35.131 1.00 20.38 ? 710 ASP A OD2 1 ATOM 5460 N N . ALA A 1 670 ? 17.388 68.940 33.479 1.00 17.45 ? 711 ALA A N 1 ATOM 5461 C CA . ALA A 1 670 ? 17.227 70.105 32.583 1.00 17.27 ? 711 ALA A CA 1 ATOM 5462 C C . ALA A 1 670 ? 18.600 70.535 31.989 1.00 17.88 ? 711 ALA A C 1 ATOM 5463 O O . ALA A 1 670 ? 18.690 71.004 30.829 1.00 19.14 ? 711 ALA A O 1 ATOM 5464 C CB . ALA A 1 670 ? 16.627 71.278 33.364 1.00 17.30 ? 711 ALA A CB 1 ATOM 5465 N N . LEU A 1 671 ? 19.676 70.352 32.757 1.00 18.30 ? 712 LEU A N 1 ATOM 5466 C CA . LEU A 1 671 ? 21.032 70.719 32.271 1.00 18.92 ? 712 LEU A CA 1 ATOM 5467 C C . LEU A 1 671 ? 21.712 69.641 31.446 1.00 19.74 ? 712 LEU A C 1 ATOM 5468 O O . LEU A 1 671 ? 22.715 69.902 30.767 1.00 21.71 ? 712 LEU A O 1 ATOM 5469 C CB . LEU A 1 671 ? 21.934 71.020 33.465 1.00 18.99 ? 712 LEU A CB 1 ATOM 5470 C CG . LEU A 1 671 ? 21.666 72.394 34.111 1.00 18.88 ? 712 LEU A CG 1 ATOM 5471 C CD1 . LEU A 1 671 ? 22.300 72.477 35.491 1.00 18.81 ? 712 LEU A CD1 1 ATOM 5472 C CD2 . LEU A 1 671 ? 22.173 73.496 33.188 1.00 21.16 ? 712 LEU A CD2 1 ATOM 5473 N N . PHE A 1 672 ? 21.240 68.401 31.596 1.00 19.18 ? 713 PHE A N 1 ATOM 5474 C CA . PHE A 1 672 ? 21.977 67.301 31.012 1.00 19.83 ? 713 PHE A CA 1 ATOM 5475 C C . PHE A 1 672 ? 22.020 67.406 29.480 1.00 19.95 ? 713 PHE A C 1 ATOM 5476 O O . PHE A 1 672 ? 20.977 67.525 28.824 1.00 20.46 ? 713 PHE A O 1 ATOM 5477 C CB . PHE A 1 672 ? 21.377 65.944 31.415 1.00 20.51 ? 713 PHE A CB 1 ATOM 5478 C CG . PHE A 1 672 ? 22.183 64.771 30.887 1.00 19.87 ? 713 PHE A CG 1 ATOM 5479 C CD1 . PHE A 1 672 ? 23.337 64.360 31.570 1.00 20.49 ? 713 PHE A CD1 1 ATOM 5480 C CD2 . PHE A 1 672 ? 21.866 64.175 29.666 1.00 20.73 ? 713 PHE A CD2 1 ATOM 5481 C CE1 . PHE A 1 672 ? 24.139 63.316 31.079 1.00 23.32 ? 713 PHE A CE1 1 ATOM 5482 C CE2 . PHE A 1 672 ? 22.638 63.103 29.167 1.00 21.74 ? 713 PHE A CE2 1 ATOM 5483 C CZ . PHE A 1 672 ? 23.798 62.697 29.854 1.00 23.51 ? 713 PHE A CZ 1 ATOM 5484 N N . ASP A 1 673 ? 23.224 67.364 28.922 1.00 20.93 ? 714 ASP A N 1 ATOM 5485 C CA . ASP A 1 673 ? 23.384 67.397 27.442 1.00 22.61 ? 714 ASP A CA 1 ATOM 5486 C C . ASP A 1 673 ? 22.726 68.627 26.807 1.00 23.32 ? 714 ASP A C 1 ATOM 5487 O O . ASP A 1 673 ? 22.326 68.590 25.632 1.00 24.26 ? 714 ASP A O 1 ATOM 5488 C CB . ASP A 1 673 ? 22.838 66.110 26.802 1.00 22.55 ? 714 ASP A CB 1 ATOM 5489 C CG . ASP A 1 673 ? 23.276 65.941 25.323 1.00 24.72 ? 714 ASP A CG 1 ATOM 5490 O OD1 . ASP A 1 673 ? 24.461 66.217 24.993 1.00 25.28 ? 714 ASP A OD1 1 ATOM 5491 O OD2 . ASP A 1 673 ? 22.440 65.495 24.513 1.00 26.61 ? 714 ASP A OD2 1 ATOM 5492 N N . ILE A 1 674 ? 22.640 69.734 27.562 1.00 22.93 ? 715 ILE A N 1 ATOM 5493 C CA . ILE A 1 674 ? 21.860 70.884 27.109 1.00 22.09 ? 715 ILE A CA 1 ATOM 5494 C C . ILE A 1 674 ? 22.473 71.536 25.855 1.00 24.69 ? 715 ILE A C 1 ATOM 5495 O O . ILE A 1 674 ? 21.732 72.138 25.063 1.00 24.62 ? 715 ILE A O 1 ATOM 5496 C CB . ILE A 1 674 ? 21.712 71.946 28.216 1.00 22.22 ? 715 ILE A CB 1 ATOM 5497 C CG1 . ILE A 1 674 ? 20.706 73.019 27.827 1.00 22.05 ? 715 ILE A CG1 1 ATOM 5498 C CG2 . ILE A 1 674 ? 23.048 72.527 28.593 1.00 20.92 ? 715 ILE A CG2 1 ATOM 5499 C CD1 . ILE A 1 674 ? 20.228 73.778 29.041 1.00 24.44 ? 715 ILE A CD1 1 ATOM 5500 N N . GLU A 1 675 ? 23.797 71.406 25.700 1.00 25.43 ? 716 GLU A N 1 ATOM 5501 C CA . GLU A 1 675 ? 24.483 72.006 24.544 1.00 28.26 ? 716 GLU A CA 1 ATOM 5502 C C . GLU A 1 675 ? 24.039 71.349 23.237 1.00 29.71 ? 716 GLU A C 1 ATOM 5503 O O . GLU A 1 675 ? 24.343 71.879 22.147 1.00 31.31 ? 716 GLU A O 1 ATOM 5504 C CB . GLU A 1 675 ? 25.999 71.908 24.708 1.00 28.42 ? 716 GLU A CB 1 ATOM 5505 C CG . GLU A 1 675 ? 26.547 70.478 24.548 1.00 29.96 ? 716 GLU A CG 1 ATOM 5506 C CD . GLU A 1 675 ? 26.580 69.687 25.867 1.00 33.10 ? 716 GLU A CD 1 ATOM 5507 O OE1 . GLU A 1 675 ? 25.843 70.034 26.816 1.00 28.63 ? 716 GLU A OE1 1 ATOM 5508 O OE2 . GLU A 1 675 ? 27.356 68.706 25.931 1.00 35.43 ? 716 GLU A OE2 1 ATOM 5509 N N . SER A 1 676 ? 23.322 70.222 23.327 1.00 30.14 ? 717 SER A N 1 ATOM 5510 C CA A SER A 1 676 ? 22.835 69.501 22.151 0.60 30.87 ? 717 SER A CA 1 ATOM 5511 C CA B SER A 1 676 ? 22.830 69.513 22.145 0.40 31.82 ? 717 SER A CA 1 ATOM 5512 C C . SER A 1 676 ? 21.382 69.856 21.806 1.00 32.09 ? 717 SER A C 1 ATOM 5513 O O . SER A 1 676 ? 20.876 69.437 20.759 1.00 33.55 ? 717 SER A O 1 ATOM 5514 C CB A SER A 1 676 ? 23.003 67.971 22.323 0.60 30.21 ? 717 SER A CB 1 ATOM 5515 C CB B SER A 1 676 ? 22.964 67.996 22.319 0.40 31.44 ? 717 SER A CB 1 ATOM 5516 O OG A SER A 1 676 ? 24.368 67.578 22.477 0.60 26.37 ? 717 SER A OG 1 ATOM 5517 O OG B SER A 1 676 ? 21.782 67.457 22.883 0.40 32.80 ? 717 SER A OG 1 ATOM 5518 N N . LYS A 1 677 ? 20.706 70.635 22.660 1.00 32.00 ? 718 LYS A N 1 ATOM 5519 C CA . LYS A 1 677 ? 19.307 70.968 22.410 1.00 32.52 ? 718 LYS A CA 1 ATOM 5520 C C . LYS A 1 677 ? 19.152 71.990 21.291 1.00 33.61 ? 718 LYS A C 1 ATOM 5521 O O . LYS A 1 677 ? 19.923 72.941 21.172 1.00 33.51 ? 718 LYS A O 1 ATOM 5522 C CB . LYS A 1 677 ? 18.600 71.514 23.661 1.00 32.44 ? 718 LYS A CB 1 ATOM 5523 C CG . LYS A 1 677 ? 18.528 70.544 24.815 1.00 33.10 ? 718 LYS A CG 1 ATOM 5524 C CD . LYS A 1 677 ? 17.798 69.278 24.450 1.00 38.17 ? 718 LYS A CD 1 ATOM 5525 C CE . LYS A 1 677 ? 18.061 68.180 25.516 1.00 40.62 ? 718 LYS A CE 1 ATOM 5526 N NZ . LYS A 1 677 ? 17.364 68.539 26.798 1.00 39.19 ? 718 LYS A NZ 1 ATOM 5527 N N . VAL A 1 678 ? 18.095 71.821 20.518 1.00 34.65 ? 719 VAL A N 1 ATOM 5528 C CA . VAL A 1 678 ? 17.955 72.574 19.274 1.00 36.28 ? 719 VAL A CA 1 ATOM 5529 C C . VAL A 1 678 ? 17.483 74.001 19.554 1.00 35.81 ? 719 VAL A C 1 ATOM 5530 O O . VAL A 1 678 ? 17.856 74.954 18.846 1.00 36.29 ? 719 VAL A O 1 ATOM 5531 C CB . VAL A 1 678 ? 17.018 71.767 18.348 1.00 37.11 ? 719 VAL A CB 1 ATOM 5532 C CG1 . VAL A 1 678 ? 15.869 72.602 17.794 1.00 39.07 ? 719 VAL A CG1 1 ATOM 5533 C CG2 . VAL A 1 678 ? 17.852 71.011 17.267 1.00 38.79 ? 719 VAL A CG2 1 ATOM 5534 N N . ASP A 1 679 ? 16.729 74.157 20.641 1.00 34.32 ? 720 ASP A N 1 ATOM 5535 C CA . ASP A 1 679 ? 16.178 75.454 21.053 1.00 33.08 ? 720 ASP A CA 1 ATOM 5536 C C . ASP A 1 679 ? 16.711 75.847 22.438 1.00 31.95 ? 720 ASP A C 1 ATOM 5537 O O . ASP A 1 679 ? 16.064 75.545 23.472 1.00 30.74 ? 720 ASP A O 1 ATOM 5538 C CB . ASP A 1 679 ? 14.655 75.355 21.070 1.00 33.19 ? 720 ASP A CB 1 ATOM 5539 C CG . ASP A 1 679 ? 13.976 76.651 21.447 1.00 34.23 ? 720 ASP A CG 1 ATOM 5540 O OD1 . ASP A 1 679 ? 14.646 77.617 21.881 1.00 34.73 ? 720 ASP A OD1 1 ATOM 5541 O OD2 . ASP A 1 679 ? 12.733 76.697 21.313 1.00 38.88 ? 720 ASP A OD2 1 ATOM 5542 N N . PRO A 1 680 ? 17.895 76.487 22.481 1.00 30.89 ? 721 PRO A N 1 ATOM 5543 C CA . PRO A 1 680 ? 18.506 76.823 23.770 1.00 30.39 ? 721 PRO A CA 1 ATOM 5544 C C . PRO A 1 680 ? 17.666 77.740 24.647 1.00 29.35 ? 721 PRO A C 1 ATOM 5545 O O . PRO A 1 680 ? 17.702 77.625 25.875 1.00 27.91 ? 721 PRO A O 1 ATOM 5546 C CB . PRO A 1 680 ? 19.827 77.510 23.396 1.00 31.64 ? 721 PRO A CB 1 ATOM 5547 C CG . PRO A 1 680 ? 19.742 77.830 21.944 1.00 33.34 ? 721 PRO A CG 1 ATOM 5548 C CD . PRO A 1 680 ? 18.720 76.914 21.329 1.00 32.36 ? 721 PRO A CD 1 ATOM 5549 N N . SER A 1 681 ? 16.897 78.646 24.039 1.00 28.62 ? 722 SER A N 1 ATOM 5550 C CA . SER A 1 681 ? 16.038 79.508 24.842 1.00 28.56 ? 722 SER A CA 1 ATOM 5551 C C . SER A 1 681 ? 15.034 78.687 25.660 1.00 27.66 ? 722 SER A C 1 ATOM 5552 O O . SER A 1 681 ? 14.827 78.932 26.853 1.00 26.52 ? 722 SER A O 1 ATOM 5553 C CB . SER A 1 681 ? 15.290 80.497 23.951 1.00 29.79 ? 722 SER A CB 1 ATOM 5554 O OG . SER A 1 681 ? 14.629 81.431 24.764 1.00 34.28 ? 722 SER A OG 1 ATOM 5555 N N . LYS A 1 682 ? 14.409 77.720 24.999 1.00 26.78 ? 723 LYS A N 1 ATOM 5556 C CA . LYS A 1 682 ? 13.500 76.801 25.674 1.00 27.42 ? 723 LYS A CA 1 ATOM 5557 C C . LYS A 1 682 ? 14.208 75.984 26.770 1.00 25.42 ? 723 LYS A C 1 ATOM 5558 O O . LYS A 1 682 ? 13.672 75.823 27.893 1.00 24.61 ? 723 LYS A O 1 ATOM 5559 C CB . LYS A 1 682 ? 12.869 75.851 24.652 1.00 28.98 ? 723 LYS A CB 1 ATOM 5560 C CG . LYS A 1 682 ? 11.750 75.020 25.194 1.00 33.56 ? 723 LYS A CG 1 ATOM 5561 C CD . LYS A 1 682 ? 11.165 74.097 24.112 1.00 40.30 ? 723 LYS A CD 1 ATOM 5562 C CE . LYS A 1 682 ? 10.010 73.281 24.696 1.00 44.22 ? 723 LYS A CE 1 ATOM 5563 N NZ . LYS A 1 682 ? 9.481 72.324 23.674 1.00 49.95 ? 723 LYS A NZ 1 ATOM 5564 N N . ALA A 1 683 ? 15.368 75.440 26.413 1.00 24.13 ? 724 ALA A N 1 ATOM 5565 C CA . ALA A 1 683 ? 16.081 74.550 27.324 1.00 22.78 ? 724 ALA A CA 1 ATOM 5566 C C . ALA A 1 683 ? 16.530 75.315 28.569 1.00 22.56 ? 724 ALA A C 1 ATOM 5567 O O . ALA A 1 683 ? 16.411 74.811 29.691 1.00 20.81 ? 724 ALA A O 1 ATOM 5568 C CB . ALA A 1 683 ? 17.297 73.956 26.627 1.00 23.76 ? 724 ALA A CB 1 ATOM 5569 N N . TRP A 1 684 ? 17.099 76.515 28.374 1.00 20.54 ? 725 TRP A N 1 ATOM 5570 C CA . TRP A 1 684 ? 17.550 77.270 29.557 1.00 20.14 ? 725 TRP A CA 1 ATOM 5571 C C . TRP A 1 684 ? 16.376 77.827 30.363 1.00 19.17 ? 725 TRP A C 1 ATOM 5572 O O . TRP A 1 684 ? 16.444 77.971 31.624 1.00 18.90 ? 725 TRP A O 1 ATOM 5573 C CB . TRP A 1 684 ? 18.524 78.365 29.129 1.00 19.38 ? 725 TRP A CB 1 ATOM 5574 C CG . TRP A 1 684 ? 19.863 77.742 28.843 1.00 21.05 ? 725 TRP A CG 1 ATOM 5575 C CD1 . TRP A 1 684 ? 20.378 77.393 27.612 1.00 20.10 ? 725 TRP A CD1 1 ATOM 5576 C CD2 . TRP A 1 684 ? 20.813 77.318 29.813 1.00 20.50 ? 725 TRP A CD2 1 ATOM 5577 N NE1 . TRP A 1 684 ? 21.638 76.817 27.771 1.00 22.50 ? 725 TRP A NE1 1 ATOM 5578 C CE2 . TRP A 1 684 ? 21.918 76.757 29.114 1.00 21.31 ? 725 TRP A CE2 1 ATOM 5579 C CE3 . TRP A 1 684 ? 20.861 77.384 31.218 1.00 19.55 ? 725 TRP A CE3 1 ATOM 5580 C CZ2 . TRP A 1 684 ? 23.060 76.257 29.783 1.00 21.41 ? 725 TRP A CZ2 1 ATOM 5581 C CZ3 . TRP A 1 684 ? 21.995 76.884 31.877 1.00 20.50 ? 725 TRP A CZ3 1 ATOM 5582 C CH2 . TRP A 1 684 ? 23.070 76.333 31.165 1.00 22.07 ? 725 TRP A CH2 1 ATOM 5583 N N . GLY A 1 685 ? 15.263 78.096 29.691 1.00 19.88 ? 726 GLY A N 1 ATOM 5584 C CA . GLY A 1 685 ? 14.003 78.458 30.370 1.00 19.60 ? 726 GLY A CA 1 ATOM 5585 C C . GLY A 1 685 ? 13.609 77.342 31.325 1.00 19.14 ? 726 GLY A C 1 ATOM 5586 O O . GLY A 1 685 ? 13.204 77.626 32.460 1.00 19.82 ? 726 GLY A O 1 ATOM 5587 N N . GLU A 1 686 ? 13.735 76.097 30.879 1.00 18.66 ? 727 GLU A N 1 ATOM 5588 C CA . GLU A 1 686 ? 13.359 74.973 31.751 1.00 19.08 ? 727 GLU A CA 1 ATOM 5589 C C . GLU A 1 686 ? 14.379 74.797 32.865 1.00 18.58 ? 727 GLU A C 1 ATOM 5590 O O . GLU A 1 686 ? 14.008 74.480 34.007 1.00 17.05 ? 727 GLU A O 1 ATOM 5591 C CB . GLU A 1 686 ? 13.177 73.725 30.902 1.00 20.35 ? 727 GLU A CB 1 ATOM 5592 C CG A GLU A 1 686 ? 12.840 72.464 31.718 1.00 21.47 ? 727 GLU A CG 1 ATOM 5593 C CD A GLU A 1 686 ? 11.460 72.507 32.417 1.00 23.98 ? 727 GLU A CD 1 ATOM 5594 O OE1 A GLU A 1 686 ? 10.649 73.431 32.150 1.00 22.02 ? 727 GLU A OE1 1 ATOM 5595 O OE2 A GLU A 1 686 ? 11.228 71.604 33.272 1.00 22.81 ? 727 GLU A OE2 1 ATOM 5596 N N . VAL A 1 687 ? 15.667 75.073 32.618 1.00 17.50 ? 728 VAL A N 1 ATOM 5597 C CA . VAL A 1 687 ? 16.594 75.103 33.757 1.00 18.02 ? 728 VAL A CA 1 ATOM 5598 C C . VAL A 1 687 ? 16.134 76.123 34.809 1.00 17.84 ? 728 VAL A C 1 ATOM 5599 O O . VAL A 1 687 ? 16.131 75.846 36.013 1.00 18.00 ? 728 VAL A O 1 ATOM 5600 C CB . VAL A 1 687 ? 18.054 75.435 33.316 1.00 17.67 ? 728 VAL A CB 1 ATOM 5601 C CG1 . VAL A 1 687 ? 18.958 75.676 34.533 1.00 18.55 ? 728 VAL A CG1 1 ATOM 5602 C CG2 . VAL A 1 687 ? 18.596 74.338 32.326 1.00 18.59 ? 728 VAL A CG2 1 ATOM 5603 N N . LYS A 1 688 ? 15.774 77.339 34.356 1.00 17.30 ? 729 LYS A N 1 ATOM 5604 C CA . LYS A 1 688 ? 15.320 78.373 35.296 1.00 17.20 ? 729 LYS A CA 1 ATOM 5605 C C . LYS A 1 688 ? 14.047 77.943 36.070 1.00 17.07 ? 729 LYS A C 1 ATOM 5606 O O . LYS A 1 688 ? 13.924 78.157 37.273 1.00 16.74 ? 729 LYS A O 1 ATOM 5607 C CB B LYS A 1 688 ? 15.159 79.686 34.556 0.65 17.50 ? 729 LYS A CB 1 ATOM 5608 C CB C LYS A 1 688 ? 15.009 79.677 34.546 0.35 17.51 ? 729 LYS A CB 1 ATOM 5609 C CG B LYS A 1 688 ? 16.559 80.158 34.073 0.65 14.20 ? 729 LYS A CG 1 ATOM 5610 C CG C LYS A 1 688 ? 16.235 80.540 34.243 0.35 18.18 ? 729 LYS A CG 1 ATOM 5611 C CD B LYS A 1 688 ? 16.439 81.490 33.265 0.65 19.82 ? 729 LYS A CD 1 ATOM 5612 C CD C LYS A 1 688 ? 15.845 81.791 33.434 0.35 19.68 ? 729 LYS A CD 1 ATOM 5613 C CE B LYS A 1 688 ? 15.860 82.650 34.123 0.65 21.38 ? 729 LYS A CE 1 ATOM 5614 C CE C LYS A 1 688 ? 15.697 81.468 31.950 0.35 20.14 ? 729 LYS A CE 1 ATOM 5615 N NZ B LYS A 1 688 ? 15.846 83.965 33.342 0.65 24.17 ? 729 LYS A NZ 1 ATOM 5616 N NZ C LYS A 1 688 ? 15.588 82.687 31.084 0.35 20.80 ? 729 LYS A NZ 1 ATOM 5617 N N . ARG A 1 689 ? 13.132 77.296 35.368 1.00 16.53 ? 730 ARG A N 1 ATOM 5618 C CA . ARG A 1 689 ? 11.934 76.780 36.014 1.00 16.50 ? 730 ARG A CA 1 ATOM 5619 C C . ARG A 1 689 ? 12.284 75.784 37.108 1.00 16.25 ? 730 ARG A C 1 ATOM 5620 O O . ARG A 1 689 ? 11.746 75.880 38.222 1.00 16.28 ? 730 ARG A O 1 ATOM 5621 C CB . ARG A 1 689 ? 11.034 76.113 35.024 1.00 17.83 ? 730 ARG A CB 1 ATOM 5622 C CG . ARG A 1 689 ? 9.680 75.896 35.630 1.00 18.09 ? 730 ARG A CG 1 ATOM 5623 C CD . ARG A 1 689 ? 8.699 75.284 34.624 1.00 21.83 ? 730 ARG A CD 1 ATOM 5624 N NE . ARG A 1 689 ? 8.916 73.881 34.387 1.00 19.94 ? 730 ARG A NE 1 ATOM 5625 C CZ . ARG A 1 689 ? 8.379 72.913 35.157 1.00 22.75 ? 730 ARG A CZ 1 ATOM 5626 N NH1 . ARG A 1 689 ? 7.666 73.222 36.267 1.00 24.14 ? 730 ARG A NH1 1 ATOM 5627 N NH2 . ARG A 1 689 ? 8.598 71.646 34.861 1.00 25.25 ? 730 ARG A NH2 1 ATOM 5628 N N . GLN A 1 690 ? 13.248 74.907 36.826 1.00 15.27 ? 731 GLN A N 1 ATOM 5629 C CA . GLN A 1 690 ? 13.625 73.910 37.832 1.00 15.55 ? 731 GLN A CA 1 ATOM 5630 C C . GLN A 1 690 ? 14.385 74.537 39.004 1.00 16.82 ? 731 GLN A C 1 ATOM 5631 O O . GLN A 1 690 ? 14.262 74.080 40.143 1.00 15.57 ? 731 GLN A O 1 ATOM 5632 C CB . GLN A 1 690 ? 14.411 72.757 37.195 1.00 17.16 ? 731 GLN A CB 1 ATOM 5633 C CG . GLN A 1 690 ? 13.599 71.994 36.140 1.00 15.24 ? 731 GLN A CG 1 ATOM 5634 C CD . GLN A 1 690 ? 12.448 71.259 36.803 1.00 18.20 ? 731 GLN A CD 1 ATOM 5635 O OE1 . GLN A 1 690 ? 12.552 70.862 37.989 1.00 16.17 ? 731 GLN A OE1 1 ATOM 5636 N NE2 . GLN A 1 690 ? 11.321 71.077 36.086 1.00 21.05 ? 731 GLN A NE2 1 ATOM 5637 N N . ILE A 1 691 ? 15.162 75.595 38.722 1.00 16.50 ? 732 ILE A N 1 ATOM 5638 C CA . ILE A 1 691 ? 15.780 76.315 39.850 1.00 16.24 ? 732 ILE A CA 1 ATOM 5639 C C . ILE A 1 691 ? 14.729 76.927 40.767 1.00 17.00 ? 732 ILE A C 1 ATOM 5640 O O . ILE A 1 691 ? 14.817 76.807 41.984 1.00 17.71 ? 732 ILE A O 1 ATOM 5641 C CB . ILE A 1 691 ? 16.730 77.430 39.317 1.00 16.00 ? 732 ILE A CB 1 ATOM 5642 C CG1 . ILE A 1 691 ? 17.943 76.795 38.622 1.00 16.26 ? 732 ILE A CG1 1 ATOM 5643 C CG2 . ILE A 1 691 ? 17.193 78.351 40.508 1.00 18.38 ? 732 ILE A CG2 1 ATOM 5644 C CD1 . ILE A 1 691 ? 18.811 77.868 37.855 1.00 18.07 ? 732 ILE A CD1 1 ATOM 5645 N N . TYR A 1 692 ? 13.704 77.541 40.184 1.00 16.38 ? 733 TYR A N 1 ATOM 5646 C CA . TYR A 1 692 ? 12.570 78.093 40.944 1.00 16.73 ? 733 TYR A CA 1 ATOM 5647 C C . TYR A 1 692 ? 11.870 77.008 41.749 1.00 16.10 ? 733 TYR A C 1 ATOM 5648 O O . TYR A 1 692 ? 11.632 77.187 42.953 1.00 17.33 ? 733 TYR A O 1 ATOM 5649 C CB . TYR A 1 692 ? 11.575 78.678 39.967 1.00 18.50 ? 733 TYR A CB 1 ATOM 5650 C CG . TYR A 1 692 ? 10.125 78.978 40.410 1.00 21.62 ? 733 TYR A CG 1 ATOM 5651 C CD1 . TYR A 1 692 ? 9.832 79.707 41.586 1.00 23.23 ? 733 TYR A CD1 1 ATOM 5652 C CD2 . TYR A 1 692 ? 9.053 78.630 39.550 1.00 20.92 ? 733 TYR A CD2 1 ATOM 5653 C CE1 . TYR A 1 692 ? 8.450 80.063 41.888 1.00 22.35 ? 733 TYR A CE1 1 ATOM 5654 C CE2 . TYR A 1 692 ? 7.743 78.960 39.815 1.00 21.47 ? 733 TYR A CE2 1 ATOM 5655 C CZ . TYR A 1 692 ? 7.437 79.694 40.972 1.00 24.04 ? 733 TYR A CZ 1 ATOM 5656 O OH . TYR A 1 692 ? 6.074 80.032 41.178 1.00 26.12 ? 733 TYR A OH 1 ATOM 5657 N N . VAL A 1 693 ? 11.572 75.874 41.116 1.00 16.66 ? 734 VAL A N 1 ATOM 5658 C CA . VAL A 1 693 ? 10.922 74.815 41.897 1.00 15.32 ? 734 VAL A CA 1 ATOM 5659 C C . VAL A 1 693 ? 11.755 74.321 43.068 1.00 15.61 ? 734 VAL A C 1 ATOM 5660 O O . VAL A 1 693 ? 11.262 74.164 44.194 1.00 16.12 ? 734 VAL A O 1 ATOM 5661 C CB . VAL A 1 693 ? 10.568 73.634 40.977 1.00 16.32 ? 734 VAL A CB 1 ATOM 5662 C CG1 . VAL A 1 693 ? 10.091 72.417 41.793 1.00 15.83 ? 734 VAL A CG1 1 ATOM 5663 C CG2 . VAL A 1 693 ? 9.463 74.084 39.999 1.00 17.87 ? 734 VAL A CG2 1 ATOM 5664 N N . ALA A 1 694 ? 13.070 74.177 42.842 1.00 14.19 ? 735 ALA A N 1 ATOM 5665 C CA . ALA A 1 694 ? 13.943 73.686 43.903 1.00 13.81 ? 735 ALA A CA 1 ATOM 5666 C C . ALA A 1 694 ? 14.114 74.700 45.041 1.00 13.21 ? 735 ALA A C 1 ATOM 5667 O O . ALA A 1 694 ? 14.023 74.341 46.234 1.00 15.32 ? 735 ALA A O 1 ATOM 5668 C CB . ALA A 1 694 ? 15.320 73.316 43.313 1.00 15.14 ? 735 ALA A CB 1 ATOM 5669 N N . ALA A 1 695 ? 14.321 75.995 44.679 1.00 14.64 ? 736 ALA A N 1 ATOM 5670 C CA . ALA A 1 695 ? 14.471 77.034 45.712 1.00 15.27 ? 736 ALA A CA 1 ATOM 5671 C C . ALA A 1 695 ? 13.181 77.152 46.541 1.00 15.02 ? 736 ALA A C 1 ATOM 5672 O O . ALA A 1 695 ? 13.207 77.222 47.804 1.00 15.92 ? 736 ALA A O 1 ATOM 5673 C CB . ALA A 1 695 ? 14.782 78.389 45.023 1.00 16.50 ? 736 ALA A CB 1 ATOM 5674 N N . PHE A 1 696 ? 12.050 77.099 45.838 1.00 14.96 ? 737 PHE A N 1 ATOM 5675 C CA . PHE A 1 696 ? 10.765 77.208 46.516 1.00 14.52 ? 737 PHE A CA 1 ATOM 5676 C C . PHE A 1 696 ? 10.603 76.032 47.485 1.00 14.14 ? 737 PHE A C 1 ATOM 5677 O O . PHE A 1 696 ? 10.249 76.194 48.675 1.00 14.79 ? 737 PHE A O 1 ATOM 5678 C CB . PHE A 1 696 ? 9.602 77.237 45.533 1.00 14.19 ? 737 PHE A CB 1 ATOM 5679 C CG . PHE A 1 696 ? 8.299 76.910 46.213 1.00 15.17 ? 737 PHE A CG 1 ATOM 5680 C CD1 . PHE A 1 696 ? 7.753 77.780 47.198 1.00 17.51 ? 737 PHE A CD1 1 ATOM 5681 C CD2 . PHE A 1 696 ? 7.724 75.653 46.015 1.00 16.79 ? 737 PHE A CD2 1 ATOM 5682 C CE1 . PHE A 1 696 ? 6.566 77.422 47.892 1.00 19.94 ? 737 PHE A CE1 1 ATOM 5683 C CE2 . PHE A 1 696 ? 6.450 75.300 46.704 1.00 15.98 ? 737 PHE A CE2 1 ATOM 5684 C CZ . PHE A 1 696 ? 5.933 76.195 47.648 1.00 17.32 ? 737 PHE A CZ 1 ATOM 5685 N N . THR A 1 697 ? 10.931 74.830 47.012 1.00 14.00 ? 738 THR A N 1 ATOM 5686 C CA . THR A 1 697 ? 10.697 73.639 47.873 1.00 13.66 ? 738 THR A CA 1 ATOM 5687 C C . THR A 1 697 ? 11.633 73.668 49.070 1.00 15.60 ? 738 THR A C 1 ATOM 5688 O O . THR A 1 697 ? 11.204 73.359 50.188 1.00 15.52 ? 738 THR A O 1 ATOM 5689 C CB . THR A 1 697 ? 10.893 72.361 47.083 1.00 14.26 ? 738 THR A CB 1 ATOM 5690 O OG1 . THR A 1 697 ? 10.052 72.352 45.905 1.00 14.03 ? 738 THR A OG1 1 ATOM 5691 C CG2 . THR A 1 697 ? 10.569 71.158 48.013 1.00 14.60 ? 738 THR A CG2 1 ATOM 5692 N N . VAL A 1 698 ? 12.918 74.066 48.871 1.00 15.09 ? 739 VAL A N 1 ATOM 5693 C CA . VAL A 1 698 ? 13.833 74.141 50.029 1.00 15.89 ? 739 VAL A CA 1 ATOM 5694 C C . VAL A 1 698 ? 13.337 75.164 51.057 1.00 15.90 ? 739 VAL A C 1 ATOM 5695 O O . VAL A 1 698 ? 13.363 74.885 52.261 1.00 16.61 ? 739 VAL A O 1 ATOM 5696 C CB . VAL A 1 698 ? 15.252 74.439 49.554 1.00 16.63 ? 739 VAL A CB 1 ATOM 5697 C CG1 . VAL A 1 698 ? 16.177 74.736 50.749 1.00 17.89 ? 739 VAL A CG1 1 ATOM 5698 C CG2 . VAL A 1 698 ? 15.768 73.239 48.759 1.00 15.10 ? 739 VAL A CG2 1 ATOM 5699 N N . GLN A 1 699 ? 12.897 76.347 50.579 1.00 16.49 ? 740 GLN A N 1 ATOM 5700 C CA . GLN A 1 699 ? 12.377 77.376 51.494 1.00 16.74 ? 740 GLN A CA 1 ATOM 5701 C C . GLN A 1 699 ? 11.097 76.875 52.205 1.00 15.55 ? 740 GLN A C 1 ATOM 5702 O O . GLN A 1 699 ? 10.960 77.019 53.420 1.00 16.50 ? 740 GLN A O 1 ATOM 5703 C CB . GLN A 1 699 ? 12.072 78.655 50.752 1.00 17.61 ? 740 GLN A CB 1 ATOM 5704 C CG . GLN A 1 699 ? 11.508 79.748 51.670 1.00 17.65 ? 740 GLN A CG 1 ATOM 5705 C CD . GLN A 1 699 ? 12.559 80.367 52.557 1.00 18.58 ? 740 GLN A CD 1 ATOM 5706 O OE1 . GLN A 1 699 ? 13.765 80.311 52.272 1.00 19.42 ? 740 GLN A OE1 1 ATOM 5707 N NE2 . GLN A 1 699 ? 12.117 80.921 53.700 1.00 19.01 ? 740 GLN A NE2 1 ATOM 5708 N N . ALA A 1 700 ? 10.235 76.176 51.469 1.00 14.99 ? 741 ALA A N 1 ATOM 5709 C CA . ALA A 1 700 ? 8.990 75.702 52.069 1.00 15.77 ? 741 ALA A CA 1 ATOM 5710 C C . ALA A 1 700 ? 9.319 74.648 53.128 1.00 15.51 ? 741 ALA A C 1 ATOM 5711 O O . ALA A 1 700 ? 8.726 74.634 54.220 1.00 16.47 ? 741 ALA A O 1 ATOM 5712 C CB . ALA A 1 700 ? 8.101 75.094 50.985 1.00 15.62 ? 741 ALA A CB 1 ATOM 5713 N N . ALA A 1 701 ? 10.303 73.774 52.849 1.00 15.17 ? 742 ALA A N 1 ATOM 5714 C CA . ALA A 1 701 ? 10.695 72.772 53.849 1.00 15.07 ? 742 ALA A CA 1 ATOM 5715 C C . ALA A 1 701 ? 11.298 73.503 55.062 1.00 15.28 ? 742 ALA A C 1 ATOM 5716 O O . ALA A 1 701 ? 10.996 73.133 56.190 1.00 16.03 ? 742 ALA A O 1 ATOM 5717 C CB . ALA A 1 701 ? 11.723 71.807 53.245 1.00 15.37 ? 742 ALA A CB 1 ATOM 5718 N N . ALA A 1 702 ? 12.168 74.499 54.833 1.00 14.12 ? 743 ALA A N 1 ATOM 5719 C CA . ALA A 1 702 ? 12.703 75.251 55.987 1.00 17.14 ? 743 ALA A CA 1 ATOM 5720 C C . ALA A 1 702 ? 11.573 75.822 56.844 1.00 16.37 ? 743 ALA A C 1 ATOM 5721 O O . ALA A 1 702 ? 11.607 75.741 58.108 1.00 17.20 ? 743 ALA A O 1 ATOM 5722 C CB . ALA A 1 702 ? 13.611 76.405 55.500 1.00 17.54 ? 743 ALA A CB 1 ATOM 5723 N N . GLU A 1 703 ? 10.544 76.393 56.207 1.00 16.14 ? 744 GLU A N 1 ATOM 5724 C CA . GLU A 1 703 ? 9.470 77.048 56.956 1.00 17.21 ? 744 GLU A CA 1 ATOM 5725 C C . GLU A 1 703 ? 8.660 76.087 57.778 1.00 17.29 ? 744 GLU A C 1 ATOM 5726 O O . GLU A 1 703 ? 8.025 76.497 58.750 1.00 17.98 ? 744 GLU A O 1 ATOM 5727 C CB . GLU A 1 703 ? 8.593 77.895 56.006 1.00 18.54 ? 744 GLU A CB 1 ATOM 5728 C CG . GLU A 1 703 ? 9.429 79.070 55.488 1.00 18.62 ? 744 GLU A CG 1 ATOM 5729 C CD . GLU A 1 703 ? 8.649 80.003 54.608 1.00 25.38 ? 744 GLU A CD 1 ATOM 5730 O OE1 . GLU A 1 703 ? 7.507 79.661 54.202 1.00 24.74 ? 744 GLU A OE1 1 ATOM 5731 O OE2 . GLU A 1 703 ? 9.229 81.062 54.256 1.00 25.44 ? 744 GLU A OE2 1 ATOM 5732 N N . THR A 1 704 ? 8.720 74.775 57.463 1.00 16.58 ? 745 THR A N 1 ATOM 5733 C CA . THR A 1 704 ? 8.043 73.823 58.356 1.00 16.30 ? 745 THR A CA 1 ATOM 5734 C C . THR A 1 704 ? 8.724 73.704 59.729 1.00 17.25 ? 745 THR A C 1 ATOM 5735 O O . THR A 1 704 ? 8.152 73.182 60.663 1.00 17.84 ? 745 THR A O 1 ATOM 5736 C CB . THR A 1 704 ? 7.891 72.386 57.770 1.00 16.01 ? 745 THR A CB 1 ATOM 5737 O OG1 . THR A 1 704 ? 9.163 71.713 57.759 1.00 15.22 ? 745 THR A OG1 1 ATOM 5738 C CG2 . THR A 1 704 ? 7.287 72.440 56.334 1.00 15.29 ? 745 THR A CG2 1 ATOM 5739 N N . LEU A 1 705 ? 9.978 74.161 59.809 1.00 17.07 ? 746 LEU A N 1 ATOM 5740 C CA . LEU A 1 705 ? 10.739 74.115 61.077 1.00 17.91 ? 746 LEU A CA 1 ATOM 5741 C C . LEU A 1 705 ? 10.652 75.445 61.852 1.00 18.32 ? 746 LEU A C 1 ATOM 5742 O O . LEU A 1 705 ? 11.168 75.518 62.997 1.00 19.45 ? 746 LEU A O 1 ATOM 5743 C CB . LEU A 1 705 ? 12.187 73.825 60.760 1.00 17.88 ? 746 LEU A CB 1 ATOM 5744 C CG . LEU A 1 705 ? 12.379 72.478 60.041 1.00 18.08 ? 746 LEU A CG 1 ATOM 5745 C CD1 . LEU A 1 705 ? 13.891 72.343 59.744 1.00 17.59 ? 746 LEU A CD1 1 ATOM 5746 C CD2 . LEU A 1 705 ? 11.897 71.310 60.921 1.00 19.15 ? 746 LEU A CD2 1 ATOM 5747 N N . SER A 1 706 ? 10.098 76.501 61.218 1.00 19.54 ? 747 SER A N 1 ATOM 5748 C CA . SER A 1 706 ? 9.873 77.778 61.954 1.00 19.63 ? 747 SER A CA 1 ATOM 5749 C C . SER A 1 706 ? 8.880 77.550 63.106 1.00 21.13 ? 747 SER A C 1 ATOM 5750 O O . SER A 1 706 ? 8.115 76.567 63.118 1.00 20.34 ? 747 SER A O 1 ATOM 5751 C CB . SER A 1 706 ? 9.277 78.774 60.979 1.00 20.93 ? 747 SER A CB 1 ATOM 5752 O OG . SER A 1 706 ? 10.232 79.088 60.016 1.00 22.79 ? 747 SER A OG 1 ATOM 5753 N N . GLU A 1 707 ? 8.841 78.471 64.093 1.00 20.56 ? 748 GLU A N 1 ATOM 5754 C CA . GLU A 1 707 ? 7.768 78.409 65.069 1.00 22.98 ? 748 GLU A CA 1 ATOM 5755 C C . GLU A 1 707 ? 6.424 78.395 64.355 1.00 20.51 ? 748 GLU A C 1 ATOM 5756 O O . GLU A 1 707 ? 6.236 79.047 63.317 1.00 21.79 ? 748 GLU A O 1 ATOM 5757 C CB . GLU A 1 707 ? 7.851 79.601 66.043 1.00 23.58 ? 748 GLU A CB 1 ATOM 5758 C CG . GLU A 1 707 ? 9.204 79.533 66.761 1.00 28.94 ? 748 GLU A CG 1 ATOM 5759 C CD . GLU A 1 707 ? 9.297 80.389 67.988 1.00 39.75 ? 748 GLU A CD 1 ATOM 5760 O OE1 . GLU A 1 707 ? 9.639 81.575 67.836 1.00 43.41 ? 748 GLU A OE1 1 ATOM 5761 O OE2 . GLU A 1 707 ? 9.082 79.851 69.085 1.00 44.21 ? 748 GLU A OE2 1 ATOM 5762 N N . VAL A 1 708 ? 5.502 77.599 64.882 1.00 21.04 ? 749 VAL A N 1 ATOM 5763 C CA . VAL A 1 708 ? 4.298 77.245 64.117 1.00 20.89 ? 749 VAL A CA 1 ATOM 5764 C C . VAL A 1 708 ? 3.261 78.356 64.150 1.00 22.13 ? 749 VAL A C 1 ATOM 5765 O O . VAL A 1 708 ? 2.320 78.360 63.387 1.00 21.80 ? 749 VAL A O 1 ATOM 5766 C CB . VAL A 1 708 ? 3.685 75.920 64.650 1.00 19.93 ? 749 VAL A CB 1 ATOM 5767 C CG1 . VAL A 1 708 ? 4.692 74.778 64.546 1.00 21.87 ? 749 VAL A CG1 1 ATOM 5768 C CG2 . VAL A 1 708 ? 3.223 76.086 66.177 1.00 20.57 ? 749 VAL A CG2 1 ATOM 5769 N N . ALA A 1 709 ? 3.436 79.297 65.089 1.00 22.47 ? 750 ALA A N 1 ATOM 5770 C CA . ALA A 1 709 ? 2.477 80.422 65.227 1.00 24.82 ? 750 ALA A CA 1 ATOM 5771 C C . ALA A 1 709 ? 3.085 81.371 66.237 1.00 26.32 ? 750 ALA A C 1 ATOM 5772 O O . ALA A 1 709 ? 2.453 82.417 66.541 1.00 29.58 ? 750 ALA A O 1 ATOM 5773 C CB . ALA A 1 709 ? 1.146 79.945 65.764 1.00 24.76 ? 750 ALA A CB 1 ATOM 5774 O OXT . ALA A 1 709 ? 4.137 81.123 66.816 1.00 27.44 ? 750 ALA A OXT 1 HETATM 5775 ZN ZN . ZN B 2 . ? 17.463 41.129 43.302 1.00 5.81 ? 1751 ZN A ZN 1 HETATM 5776 ZN ZN . ZN C 2 . ? 16.693 41.826 46.444 1.00 5.68 ? 1752 ZN A ZN 1 HETATM 5777 CA CA . CA D 3 . ? -0.799 49.918 41.453 1.00 4.64 ? 1753 CA A CA 1 HETATM 5778 CL CL . CL E 4 . ? 18.962 46.884 51.526 1.00 5.91 ? 1754 CL A CL 1 HETATM 5779 C C1 . NAG F 5 . ? 11.649 25.874 57.727 1.00 28.12 ? 1755 NAG A C1 1 HETATM 5780 C C2 . NAG F 5 . ? 11.437 24.428 57.313 1.00 33.24 ? 1755 NAG A C2 1 HETATM 5781 C C3 . NAG F 5 . ? 9.980 24.017 57.516 1.00 34.74 ? 1755 NAG A C3 1 HETATM 5782 C C4 . NAG F 5 . ? 9.447 24.369 58.904 1.00 33.14 ? 1755 NAG A C4 1 HETATM 5783 C C5 . NAG F 5 . ? 9.834 25.795 59.247 1.00 31.49 ? 1755 NAG A C5 1 HETATM 5784 C C6 . NAG F 5 . ? 9.462 26.147 60.683 1.00 33.96 ? 1755 NAG A C6 1 HETATM 5785 C C7 . NAG F 5 . ? 12.952 23.774 55.568 1.00 40.07 ? 1755 NAG A C7 1 HETATM 5786 C C8 . NAG F 5 . ? 13.244 23.694 54.114 1.00 39.72 ? 1755 NAG A C8 1 HETATM 5787 N N2 . NAG F 5 . ? 11.776 24.305 55.916 1.00 35.85 ? 1755 NAG A N2 1 HETATM 5788 O O3 . NAG F 5 . ? 9.929 22.617 57.392 1.00 38.11 ? 1755 NAG A O3 1 HETATM 5789 O O4 . NAG F 5 . ? 8.030 24.296 58.881 1.00 35.82 ? 1755 NAG A O4 1 HETATM 5790 O O5 . NAG F 5 . ? 11.232 25.988 59.081 1.00 29.27 ? 1755 NAG A O5 1 HETATM 5791 O O6 . NAG F 5 . ? 10.162 25.266 61.531 1.00 38.13 ? 1755 NAG A O6 1 HETATM 5792 O O7 . NAG F 5 . ? 13.797 23.382 56.373 1.00 43.28 ? 1755 NAG A O7 1 HETATM 5793 C C1 . NAG G 5 . ? 7.568 23.374 59.891 1.00 41.63 ? 1756 NAG A C1 1 HETATM 5794 C C2 . NAG G 5 . ? 6.089 23.661 60.128 1.00 42.59 ? 1756 NAG A C2 1 HETATM 5795 C C3 . NAG G 5 . ? 5.462 22.625 61.071 1.00 46.62 ? 1756 NAG A C3 1 HETATM 5796 C C4 . NAG G 5 . ? 5.784 21.184 60.641 1.00 48.60 ? 1756 NAG A C4 1 HETATM 5797 C C5 . NAG G 5 . ? 7.302 21.038 60.390 1.00 48.62 ? 1756 NAG A C5 1 HETATM 5798 C C6 . NAG G 5 . ? 7.671 19.670 59.811 1.00 47.92 ? 1756 NAG A C6 1 HETATM 5799 C C7 . NAG G 5 . ? 5.526 26.126 60.013 1.00 40.87 ? 1756 NAG A C7 1 HETATM 5800 C C8 . NAG G 5 . ? 5.388 26.041 58.543 1.00 38.06 ? 1756 NAG A C8 1 HETATM 5801 N N2 . NAG G 5 . ? 5.868 25.002 60.671 1.00 42.05 ? 1756 NAG A N2 1 HETATM 5802 O O3 . NAG G 5 . ? 4.060 22.834 61.075 1.00 47.52 ? 1756 NAG A O3 1 HETATM 5803 O O4 . NAG G 5 . ? 5.280 20.230 61.594 1.00 52.10 ? 1756 NAG A O4 1 HETATM 5804 O O5 . NAG G 5 . ? 7.744 22.030 59.459 1.00 44.66 ? 1756 NAG A O5 1 HETATM 5805 O O6 . NAG G 5 . ? 7.037 19.567 58.551 1.00 49.84 ? 1756 NAG A O6 1 HETATM 5806 O O7 . NAG G 5 . ? 5.350 27.231 60.584 1.00 42.10 ? 1756 NAG A O7 1 HETATM 5807 C C1 . NAG H 5 . ? 4.033 27.795 25.398 1.00 40.79 ? 1757 NAG A C1 1 HETATM 5808 C C2 . NAG H 5 . ? 2.672 28.407 25.170 1.00 43.58 ? 1757 NAG A C2 1 HETATM 5809 C C3 . NAG H 5 . ? 1.682 27.401 24.581 1.00 46.20 ? 1757 NAG A C3 1 HETATM 5810 C C4 . NAG H 5 . ? 2.304 26.544 23.467 1.00 48.21 ? 1757 NAG A C4 1 HETATM 5811 C C5 . NAG H 5 . ? 3.655 26.005 23.959 1.00 47.61 ? 1757 NAG A C5 1 HETATM 5812 C C6 . NAG H 5 . ? 4.345 24.979 23.030 1.00 48.82 ? 1757 NAG A C6 1 HETATM 5813 C C7 . NAG H 5 . ? 1.964 30.156 26.677 1.00 48.06 ? 1757 NAG A C7 1 HETATM 5814 C C8 . NAG H 5 . ? 1.510 30.503 28.058 1.00 48.79 ? 1757 NAG A C8 1 HETATM 5815 N N2 . NAG H 5 . ? 2.220 28.869 26.464 1.00 45.44 ? 1757 NAG A N2 1 HETATM 5816 O O3 . NAG H 5 . ? 0.623 28.172 24.087 1.00 46.98 ? 1757 NAG A O3 1 HETATM 5817 O O4 . NAG H 5 . ? 1.429 25.478 23.092 1.00 51.88 ? 1757 NAG A O4 1 HETATM 5818 O O5 . NAG H 5 . ? 4.499 27.120 24.255 1.00 43.51 ? 1757 NAG A O5 1 HETATM 5819 O O6 . NAG H 5 . ? 4.768 25.479 21.765 1.00 52.26 ? 1757 NAG A O6 1 HETATM 5820 O O7 . NAG H 5 . ? 2.077 31.025 25.802 1.00 51.14 ? 1757 NAG A O7 1 HETATM 5821 C C1 . NAG I 5 . ? 19.979 24.869 17.770 1.00 37.36 ? 1758 NAG A C1 1 HETATM 5822 C C2 . NAG I 5 . ? 20.555 23.672 17.016 1.00 39.30 ? 1758 NAG A C2 1 HETATM 5823 C C3 . NAG I 5 . ? 19.710 23.391 15.786 1.00 42.31 ? 1758 NAG A C3 1 HETATM 5824 C C4 . NAG I 5 . ? 18.215 23.301 16.106 1.00 43.31 ? 1758 NAG A C4 1 HETATM 5825 C C5 . NAG I 5 . ? 17.763 24.469 17.026 1.00 39.87 ? 1758 NAG A C5 1 HETATM 5826 C C6 . NAG I 5 . ? 16.325 24.301 17.516 1.00 36.60 ? 1758 NAG A C6 1 HETATM 5827 C C7 . NAG I 5 . ? 22.953 23.468 17.217 1.00 41.01 ? 1758 NAG A C7 1 HETATM 5828 C C8 . NAG I 5 . ? 24.322 23.831 16.726 1.00 41.86 ? 1758 NAG A C8 1 HETATM 5829 N N2 . NAG I 5 . ? 21.900 23.974 16.591 1.00 39.70 ? 1758 NAG A N2 1 HETATM 5830 O O3 . NAG I 5 . ? 20.154 22.147 15.274 1.00 43.57 ? 1758 NAG A O3 1 HETATM 5831 O O4 . NAG I 5 . ? 17.507 23.334 14.877 1.00 49.92 ? 1758 NAG A O4 1 HETATM 5832 O O5 . NAG I 5 . ? 18.644 24.563 18.139 1.00 37.07 ? 1758 NAG A O5 1 HETATM 5833 O O6 . NAG I 5 . ? 16.206 23.121 18.282 1.00 36.24 ? 1758 NAG A O6 1 HETATM 5834 O O7 . NAG I 5 . ? 22.836 22.727 18.180 1.00 43.99 ? 1758 NAG A O7 1 HETATM 5835 C C1 . NAG J 5 . ? 16.546 22.264 14.771 1.00 54.05 ? 1767 NAG A C1 1 HETATM 5836 C C2 . NAG J 5 . ? 15.557 22.680 13.691 1.00 55.41 ? 1767 NAG A C2 1 HETATM 5837 C C3 . NAG J 5 . ? 14.527 21.576 13.442 1.00 58.06 ? 1767 NAG A C3 1 HETATM 5838 C C4 . NAG J 5 . ? 15.232 20.251 13.163 1.00 59.97 ? 1767 NAG A C4 1 HETATM 5839 C C5 . NAG J 5 . ? 16.155 19.938 14.355 1.00 59.53 ? 1767 NAG A C5 1 HETATM 5840 C C6 . NAG J 5 . ? 16.868 18.591 14.227 1.00 60.21 ? 1767 NAG A C6 1 HETATM 5841 C C7 . NAG J 5 . ? 15.382 25.117 13.705 1.00 54.58 ? 1767 NAG A C7 1 HETATM 5842 C C8 . NAG J 5 . ? 14.603 26.303 14.180 1.00 53.17 ? 1767 NAG A C8 1 HETATM 5843 N N2 . NAG J 5 . ? 14.911 23.924 14.076 1.00 54.40 ? 1767 NAG A N2 1 HETATM 5844 O O3 . NAG J 5 . ? 13.742 21.905 12.328 1.00 59.11 ? 1767 NAG A O3 1 HETATM 5845 O O4 . NAG J 5 . ? 14.279 19.231 12.890 1.00 62.80 ? 1767 NAG A O4 1 HETATM 5846 O O5 . NAG J 5 . ? 17.117 20.987 14.496 1.00 57.35 ? 1767 NAG A O5 1 HETATM 5847 O O6 . NAG J 5 . ? 17.916 18.698 13.287 1.00 61.59 ? 1767 NAG A O6 1 HETATM 5848 O O7 . NAG J 5 . ? 16.400 25.287 13.024 1.00 54.25 ? 1767 NAG A O7 1 HETATM 5849 C C1 . NAG K 5 . ? 19.676 54.731 10.731 1.00 56.35 ? 1759 NAG A C1 1 HETATM 5850 C C2 . NAG K 5 . ? 19.359 56.121 10.207 1.00 62.04 ? 1759 NAG A C2 1 HETATM 5851 C C3 . NAG K 5 . ? 17.845 56.223 10.163 1.00 62.62 ? 1759 NAG A C3 1 HETATM 5852 C C4 . NAG K 5 . ? 17.332 55.277 9.084 1.00 62.32 ? 1759 NAG A C4 1 HETATM 5853 C C5 . NAG K 5 . ? 17.824 53.841 9.277 1.00 61.52 ? 1759 NAG A C5 1 HETATM 5854 C C6 . NAG K 5 . ? 17.817 53.198 7.886 1.00 61.71 ? 1759 NAG A C6 1 HETATM 5855 C C7 . NAG K 5 . ? 21.125 57.758 10.826 1.00 66.70 ? 1759 NAG A C7 1 HETATM 5856 C C8 . NAG K 5 . ? 22.021 57.327 9.688 1.00 65.99 ? 1759 NAG A C8 1 HETATM 5857 N N2 . NAG K 5 . ? 19.931 57.175 11.021 1.00 64.05 ? 1759 NAG A N2 1 HETATM 5858 O O3 . NAG K 5 . ? 17.473 57.544 9.867 1.00 64.17 ? 1759 NAG A O3 1 HETATM 5859 O O4 . NAG K 5 . ? 15.925 55.301 9.036 1.00 64.53 ? 1759 NAG A O4 1 HETATM 5860 O O5 . NAG K 5 . ? 19.144 53.742 9.841 1.00 59.44 ? 1759 NAG A O5 1 HETATM 5861 O O6 . NAG K 5 . ? 17.627 51.804 7.940 1.00 63.35 ? 1759 NAG A O6 1 HETATM 5862 O O7 . NAG K 5 . ? 21.515 58.653 11.577 1.00 68.04 ? 1759 NAG A O7 1 HETATM 5863 C C1 . NAG L 5 . ? 36.519 37.646 52.920 1.00 40.07 ? 1760 NAG A C1 1 HETATM 5864 C C2 . NAG L 5 . ? 36.468 37.751 51.388 1.00 38.45 ? 1760 NAG A C2 1 HETATM 5865 C C3 . NAG L 5 . ? 37.799 37.295 50.755 1.00 44.00 ? 1760 NAG A C3 1 HETATM 5866 C C4 . NAG L 5 . ? 39.000 38.057 51.343 1.00 45.53 ? 1760 NAG A C4 1 HETATM 5867 C C5 . NAG L 5 . ? 38.944 37.983 52.876 1.00 44.96 ? 1760 NAG A C5 1 HETATM 5868 C C6 . NAG L 5 . ? 40.074 38.806 53.506 1.00 44.62 ? 1760 NAG A C6 1 HETATM 5869 C C7 . NAG L 5 . ? 34.474 37.646 50.031 1.00 29.32 ? 1760 NAG A C7 1 HETATM 5870 C C8 . NAG L 5 . ? 33.338 36.871 49.443 1.00 28.72 ? 1760 NAG A C8 1 HETATM 5871 N N2 . NAG L 5 . ? 35.331 37.021 50.842 1.00 32.80 ? 1760 NAG A N2 1 HETATM 5872 O O3 . NAG L 5 . ? 37.801 37.569 49.376 1.00 45.65 ? 1760 NAG A O3 1 HETATM 5873 O O4 . NAG L 5 . ? 40.266 37.610 50.814 1.00 48.64 ? 1760 NAG A O4 1 HETATM 5874 O O5 . NAG L 5 . ? 37.659 38.405 53.371 1.00 43.32 ? 1760 NAG A O5 1 HETATM 5875 O O6 . NAG L 5 . ? 40.117 40.109 52.949 1.00 46.22 ? 1760 NAG A O6 1 HETATM 5876 O O7 . NAG L 5 . ? 34.592 38.820 49.712 1.00 26.01 ? 1760 NAG A O7 1 HETATM 5877 C C1 . NAG M 5 . ? 24.240 61.754 68.884 1.00 24.09 ? 1761 NAG A C1 1 HETATM 5878 C C2 . NAG M 5 . ? 22.855 62.362 69.084 1.00 23.81 ? 1761 NAG A C2 1 HETATM 5879 C C3 . NAG M 5 . ? 23.121 63.805 69.462 1.00 23.95 ? 1761 NAG A C3 1 HETATM 5880 C C4 . NAG M 5 . ? 24.058 63.947 70.679 1.00 26.36 ? 1761 NAG A C4 1 HETATM 5881 C C5 . NAG M 5 . ? 25.357 63.220 70.380 1.00 25.53 ? 1761 NAG A C5 1 HETATM 5882 C C6 . NAG M 5 . ? 26.316 63.187 71.594 1.00 28.42 ? 1761 NAG A C6 1 HETATM 5883 C C7 . NAG M 5 . ? 20.918 61.737 67.699 1.00 29.92 ? 1761 NAG A C7 1 HETATM 5884 C C8 . NAG M 5 . ? 20.362 61.090 68.908 1.00 31.22 ? 1761 NAG A C8 1 HETATM 5885 N N2 . NAG M 5 . ? 22.077 62.346 67.836 1.00 26.33 ? 1761 NAG A N2 1 HETATM 5886 O O3 . NAG M 5 . ? 21.863 64.429 69.695 1.00 26.88 ? 1761 NAG A O3 1 HETATM 5887 O O4 . NAG M 5 . ? 24.376 65.308 70.823 1.00 27.72 ? 1761 NAG A O4 1 HETATM 5888 O O5 . NAG M 5 . ? 24.942 61.885 70.128 1.00 26.97 ? 1761 NAG A O5 1 HETATM 5889 O O6 . NAG M 5 . ? 25.610 62.617 72.685 1.00 29.88 ? 1761 NAG A O6 1 HETATM 5890 O O7 . NAG M 5 . ? 20.234 61.730 66.612 1.00 37.18 ? 1761 NAG A O7 1 HETATM 5891 C C1 . NAG N 5 . ? 24.125 65.755 72.175 1.00 30.79 ? 1762 NAG A C1 1 HETATM 5892 C C2 . NAG N 5 . ? 24.699 67.162 72.206 1.00 32.66 ? 1762 NAG A C2 1 HETATM 5893 C C3 . NAG N 5 . ? 24.483 67.751 73.604 1.00 36.06 ? 1762 NAG A C3 1 HETATM 5894 C C4 . NAG N 5 . ? 22.990 67.667 73.955 1.00 35.42 ? 1762 NAG A C4 1 HETATM 5895 C C5 . NAG N 5 . ? 22.533 66.201 73.848 1.00 35.61 ? 1762 NAG A C5 1 HETATM 5896 C C6 . NAG N 5 . ? 21.077 66.005 74.235 1.00 36.72 ? 1762 NAG A C6 1 HETATM 5897 C C7 . NAG N 5 . ? 26.656 67.492 70.740 1.00 36.17 ? 1762 NAG A C7 1 HETATM 5898 C C8 . NAG N 5 . ? 25.813 67.976 69.607 1.00 33.76 ? 1762 NAG A C8 1 HETATM 5899 N N2 . NAG N 5 . ? 26.118 67.115 71.893 1.00 34.79 ? 1762 NAG A N2 1 HETATM 5900 O O3 . NAG N 5 . ? 24.949 69.079 73.610 1.00 37.75 ? 1762 NAG A O3 1 HETATM 5901 O O4 . NAG N 5 . ? 22.732 68.184 75.248 1.00 40.66 ? 1762 NAG A O4 1 HETATM 5902 O O5 . NAG N 5 . ? 22.745 65.808 72.489 1.00 31.30 ? 1762 NAG A O5 1 HETATM 5903 O O6 . NAG N 5 . ? 20.365 66.973 73.486 1.00 40.68 ? 1762 NAG A O6 1 HETATM 5904 O O7 . NAG N 5 . ? 27.882 67.411 70.576 1.00 43.65 ? 1762 NAG A O7 1 HETATM 5905 C C1 . NAG O 5 . ? 15.290 83.834 52.674 1.00 22.34 ? 1763 NAG A C1 1 HETATM 5906 C C2 . NAG O 5 . ? 14.241 83.899 51.556 1.00 20.83 ? 1763 NAG A C2 1 HETATM 5907 C C3 . NAG O 5 . ? 14.069 85.386 51.230 1.00 26.45 ? 1763 NAG A C3 1 HETATM 5908 C C4 . NAG O 5 . ? 13.677 86.186 52.489 1.00 29.33 ? 1763 NAG A C4 1 HETATM 5909 C C5 . NAG O 5 . ? 14.626 85.894 53.652 1.00 29.92 ? 1763 NAG A C5 1 HETATM 5910 C C6 . NAG O 5 . ? 14.025 86.477 54.943 1.00 32.93 ? 1763 NAG A C6 1 HETATM 5911 C C7 . NAG O 5 . ? 13.825 82.417 49.654 1.00 21.73 ? 1763 NAG A C7 1 HETATM 5912 C C8 . NAG O 5 . ? 14.389 81.703 48.459 1.00 21.81 ? 1763 NAG A C8 1 HETATM 5913 N N2 . NAG O 5 . ? 14.680 83.161 50.397 1.00 19.67 ? 1763 NAG A N2 1 HETATM 5914 O O3 . NAG O 5 . ? 13.085 85.511 50.216 1.00 28.35 ? 1763 NAG A O3 1 HETATM 5915 O O4 . NAG O 5 . ? 13.817 87.575 52.260 1.00 32.98 ? 1763 NAG A O4 1 HETATM 5916 O O5 . NAG O 5 . ? 14.733 84.479 53.810 1.00 24.87 ? 1763 NAG A O5 1 HETATM 5917 O O6 . NAG O 5 . ? 15.045 86.741 55.899 1.00 42.58 ? 1763 NAG A O6 1 HETATM 5918 O O7 . NAG O 5 . ? 12.618 82.352 49.947 1.00 20.11 ? 1763 NAG A O7 1 HETATM 5919 C C1 . NAG P 5 . ? 12.666 88.104 51.583 1.00 34.32 ? 1764 NAG A C1 1 HETATM 5920 C C2 . NAG P 5 . ? 12.156 89.379 52.238 1.00 35.53 ? 1764 NAG A C2 1 HETATM 5921 C C3 . NAG P 5 . ? 11.180 90.103 51.326 1.00 35.75 ? 1764 NAG A C3 1 HETATM 5922 C C4 . NAG P 5 . ? 11.789 90.290 49.941 1.00 34.46 ? 1764 NAG A C4 1 HETATM 5923 C C5 . NAG P 5 . ? 12.205 88.916 49.407 1.00 37.04 ? 1764 NAG A C5 1 HETATM 5924 C C6 . NAG P 5 . ? 12.852 89.027 48.024 1.00 41.55 ? 1764 NAG A C6 1 HETATM 5925 C C7 . NAG P 5 . ? 12.062 89.437 54.673 1.00 42.08 ? 1764 NAG A C7 1 HETATM 5926 C C8 . NAG P 5 . ? 13.390 90.153 54.647 1.00 39.94 ? 1764 NAG A C8 1 HETATM 5927 N N2 . NAG P 5 . ? 11.500 89.087 53.493 1.00 38.09 ? 1764 NAG A N2 1 HETATM 5928 O O3 . NAG P 5 . ? 10.931 91.380 51.902 1.00 37.75 ? 1764 NAG A O3 1 HETATM 5929 O O4 . NAG P 5 . ? 10.810 90.766 49.040 1.00 34.16 ? 1764 NAG A O4 1 HETATM 5930 O O5 . NAG P 5 . ? 13.147 88.379 50.306 1.00 34.47 ? 1764 NAG A O5 1 HETATM 5931 O O6 . NAG P 5 . ? 12.788 87.758 47.372 1.00 49.42 ? 1764 NAG A O6 1 HETATM 5932 O O7 . NAG P 5 . ? 11.530 89.176 55.768 1.00 46.07 ? 1764 NAG A O7 1 HETATM 5933 C C1 . BMA Q 6 . ? 10.739 92.192 49.011 1.00 34.08 ? 1765 BMA A C1 1 HETATM 5934 C C2 . BMA Q 6 . ? 10.485 92.638 47.572 1.00 35.32 ? 1765 BMA A C2 1 HETATM 5935 C C3 . BMA Q 6 . ? 10.260 94.132 47.472 1.00 36.51 ? 1765 BMA A C3 1 HETATM 5936 C C4 . BMA Q 6 . ? 9.134 94.495 48.439 1.00 36.42 ? 1765 BMA A C4 1 HETATM 5937 C C5 . BMA Q 6 . ? 9.453 93.985 49.847 1.00 36.62 ? 1765 BMA A C5 1 HETATM 5938 C C6 . BMA Q 6 . ? 8.335 94.263 50.839 1.00 34.23 ? 1765 BMA A C6 1 HETATM 5939 O O2 . BMA Q 6 . ? 9.310 91.962 47.054 1.00 35.48 ? 1765 BMA A O2 1 HETATM 5940 O O3 . BMA Q 6 . ? 9.845 94.344 46.116 1.00 33.45 ? 1765 BMA A O3 1 HETATM 5941 O O4 . BMA Q 6 . ? 8.946 95.907 48.452 1.00 37.79 ? 1765 BMA A O4 1 HETATM 5942 O O5 . BMA Q 6 . ? 9.633 92.558 49.805 1.00 32.95 ? 1765 BMA A O5 1 HETATM 5943 O O6 . BMA Q 6 . ? 8.704 93.694 52.106 1.00 38.89 ? 1765 BMA A O6 1 HETATM 5944 C C1 . MAN R 7 . ? 10.533 95.448 45.469 1.00 40.60 ? 1766 MAN A C1 1 HETATM 5945 C C2 . MAN R 7 . ? 9.692 95.855 44.256 1.00 40.69 ? 1766 MAN A C2 1 HETATM 5946 C C3 . MAN R 7 . ? 9.804 94.869 43.100 1.00 43.31 ? 1766 MAN A C3 1 HETATM 5947 C C4 . MAN R 7 . ? 11.251 94.514 42.781 1.00 42.79 ? 1766 MAN A C4 1 HETATM 5948 C C5 . MAN R 7 . ? 11.999 94.145 44.066 1.00 41.98 ? 1766 MAN A C5 1 HETATM 5949 C C6 . MAN R 7 . ? 13.478 93.785 43.857 1.00 44.36 ? 1766 MAN A C6 1 HETATM 5950 O O2 . MAN R 7 . ? 10.193 97.083 43.798 1.00 42.37 ? 1766 MAN A O2 1 HETATM 5951 O O3 . MAN R 7 . ? 9.261 95.421 41.929 1.00 45.66 ? 1766 MAN A O3 1 HETATM 5952 O O4 . MAN R 7 . ? 11.264 93.409 41.887 1.00 42.17 ? 1766 MAN A O4 1 HETATM 5953 O O5 . MAN R 7 . ? 11.871 95.170 45.040 1.00 38.80 ? 1766 MAN A O5 1 HETATM 5954 O O6 . MAN R 7 . ? 14.217 94.913 43.442 1.00 44.47 ? 1766 MAN A O6 1 HETATM 5955 O OAA . CI9 S 8 . ? 13.702 48.558 40.576 1.00 16.73 ? 1768 CI9 A OAA 1 HETATM 5956 C CBN . CI9 S 8 . ? 13.712 47.316 40.369 1.00 17.93 ? 1768 CI9 A CBN 1 HETATM 5957 O OAG . CI9 S 8 . ? 12.915 46.745 39.587 1.00 17.80 ? 1768 CI9 A OAG 1 HETATM 5958 C CAZ . CI9 S 8 . ? 14.908 46.536 41.003 1.00 13.33 ? 1768 CI9 A CAZ 1 HETATM 5959 C CBB . CI9 S 8 . ? 14.652 45.017 41.080 1.00 14.19 ? 1768 CI9 A CBB 1 HETATM 5960 C CBW . CI9 S 8 . ? 15.946 44.276 41.502 1.00 17.13 ? 1768 CI9 A CBW 1 HETATM 5961 C CBP . CI9 S 8 . ? 16.930 44.446 40.311 1.00 17.89 ? 1768 CI9 A CBP 1 HETATM 5962 O OAI . CI9 S 8 . ? 16.818 43.646 39.335 1.00 17.61 ? 1768 CI9 A OAI 1 HETATM 5963 O OAC . CI9 S 8 . ? 17.807 45.358 40.327 1.00 15.68 ? 1768 CI9 A OAC 1 HETATM 5964 N NBI . CI9 S 8 . ? 16.594 44.895 42.682 1.00 15.82 ? 1768 CI9 A NBI 1 HETATM 5965 C CBQ . CI9 S 8 . ? 17.844 44.501 43.028 1.00 17.44 ? 1768 CI9 A CBQ 1 HETATM 5966 O OAD . CI9 S 8 . ? 18.266 43.448 42.536 1.00 14.54 ? 1768 CI9 A OAD 1 HETATM 5967 N N . CI9 S 8 . ? 18.526 45.276 43.890 1.00 16.03 ? 1768 CI9 A N 1 HETATM 5968 C CA . CI9 S 8 . ? 19.849 44.891 44.368 1.00 17.76 ? 1768 CI9 A CA 1 HETATM 5969 C C . CI9 S 8 . ? 20.103 45.592 45.695 1.00 18.73 ? 1768 CI9 A C 1 HETATM 5970 O OXT . CI9 S 8 . ? 19.542 46.703 45.865 1.00 17.91 ? 1768 CI9 A OXT 1 HETATM 5971 O O . CI9 S 8 . ? 20.718 44.910 46.553 1.00 19.98 ? 1768 CI9 A O 1 HETATM 5972 C CB . CI9 S 8 . ? 20.678 45.580 43.305 1.00 19.64 ? 1768 CI9 A CB 1 HETATM 5973 C CAP . CI9 S 8 . ? 22.183 45.315 43.358 1.00 23.89 ? 1768 CI9 A CAP 1 HETATM 5974 C CAQ . CI9 S 8 . ? 22.726 46.041 42.095 1.00 29.20 ? 1768 CI9 A CAQ 1 HETATM 5975 C CBC . CI9 S 8 . ? 24.174 45.714 41.846 1.00 37.54 ? 1768 CI9 A CBC 1 HETATM 5976 N NBX . CI9 S 8 . ? 24.655 46.548 40.716 1.00 43.27 ? 1768 CI9 A NBX 1 HETATM 5977 C CAO . CI9 S 8 . ? 24.867 47.862 40.747 1.00 44.93 ? 1768 CI9 A CAO 1 HETATM 5978 N NBF . CI9 S 8 . ? 24.906 46.078 39.587 1.00 47.61 ? 1768 CI9 A NBF 1 HETATM 5979 N NBE . CI9 S 8 . ? 25.290 46.964 38.810 1.00 48.69 ? 1768 CI9 A NBE 1 HETATM 5980 C CBR . CI9 S 8 . ? 25.282 48.101 39.502 1.00 49.35 ? 1768 CI9 A CBR 1 HETATM 5981 C CBD . CI9 S 8 . ? 25.637 49.339 38.991 1.00 51.88 ? 1768 CI9 A CBD 1 HETATM 5982 O OBM . CI9 S 8 . ? 25.874 50.414 39.914 1.00 56.30 ? 1768 CI9 A OBM 1 HETATM 5983 C CAY . CI9 S 8 . ? 24.972 51.477 39.648 1.00 57.90 ? 1768 CI9 A CAY 1 HETATM 5984 C CAX . CI9 S 8 . ? 25.419 52.682 40.443 1.00 61.97 ? 1768 CI9 A CAX 1 HETATM 5985 O OBL . CI9 S 8 . ? 25.323 52.351 41.840 1.00 65.83 ? 1768 CI9 A OBL 1 HETATM 5986 C CAW . CI9 S 8 . ? 24.825 53.482 42.548 1.00 68.23 ? 1768 CI9 A CAW 1 HETATM 5987 C CAV . CI9 S 8 . ? 25.845 53.802 43.598 1.00 70.68 ? 1768 CI9 A CAV 1 HETATM 5988 O OBK . CI9 S 8 . ? 26.695 54.888 43.150 1.00 74.09 ? 1768 CI9 A OBK 1 HETATM 5989 C CAU . CI9 S 8 . ? 27.812 55.036 44.071 1.00 75.71 ? 1768 CI9 A CAU 1 HETATM 5990 C CAT . CI9 S 8 . ? 27.341 55.132 45.546 1.00 77.79 ? 1768 CI9 A CAT 1 HETATM 5991 O OBJ . CI9 S 8 . ? 28.209 54.410 46.438 1.00 78.99 ? 1768 CI9 A OBJ 1 HETATM 5992 C CAS . CI9 S 8 . ? 27.466 53.623 47.375 1.00 78.35 ? 1768 CI9 A CAS 1 HETATM 5993 C CAR . CI9 S 8 . ? 28.561 52.801 48.057 1.00 78.62 ? 1768 CI9 A CAR 1 HETATM 5994 N NBG . CI9 S 8 . ? 29.605 53.683 48.611 1.00 78.44 ? 1768 CI9 A NBG 1 HETATM 5995 C CBT . CI9 S 8 . ? 30.917 53.703 48.308 1.00 76.66 ? 1768 CI9 A CBT 1 HETATM 5996 C CAM . CI9 S 8 . ? 31.351 54.597 47.318 1.00 76.58 ? 1768 CI9 A CAM 1 HETATM 5997 C CAL . CI9 S 8 . ? 32.706 54.692 46.996 1.00 77.46 ? 1768 CI9 A CAL 1 HETATM 5998 C CBS . CI9 S 8 . ? 33.640 53.899 47.670 1.00 78.28 ? 1768 CI9 A CBS 1 HETATM 5999 N NBY . CI9 S 8 . ? 34.955 53.956 47.379 1.00 80.49 ? 1768 CI9 A NBY 1 HETATM 6000 O OAJ . CI9 S 8 . ? 35.439 53.784 46.028 1.00 81.62 ? 1768 CI9 A OAJ 1 HETATM 6001 O OAE . CI9 S 8 . ? 35.921 54.139 48.428 1.00 81.29 ? 1768 CI9 A OAE 1 HETATM 6002 C CAN . CI9 S 8 . ? 33.205 53.024 48.667 1.00 76.30 ? 1768 CI9 A CAN 1 HETATM 6003 C CBU . CI9 S 8 . ? 31.856 52.909 49.006 1.00 74.65 ? 1768 CI9 A CBU 1 HETATM 6004 N NBZ . CI9 S 8 . ? 31.527 52.024 49.974 1.00 71.74 ? 1768 CI9 A NBZ 1 HETATM 6005 O OAK . CI9 S 8 . ? 30.206 51.644 50.231 1.00 68.32 ? 1768 CI9 A OAK 1 HETATM 6006 O OAF . CI9 S 8 . ? 32.528 51.392 50.744 1.00 71.19 ? 1768 CI9 A OAF 1 HETATM 6007 O O . HOH T 9 . ? 19.956 45.591 79.214 1.00 40.49 ? 2001 HOH A O 1 HETATM 6008 O O . HOH T 9 . ? 17.855 52.284 75.125 1.00 33.33 ? 2002 HOH A O 1 HETATM 6009 O O . HOH T 9 . ? 20.660 50.268 76.215 1.00 34.18 ? 2003 HOH A O 1 HETATM 6010 O O . HOH T 9 . ? 18.780 40.527 76.105 1.00 37.29 ? 2004 HOH A O 1 HETATM 6011 O O . HOH T 9 . ? 23.848 40.441 69.543 1.00 30.82 ? 2005 HOH A O 1 HETATM 6012 O O . HOH T 9 . ? 20.500 38.429 75.979 1.00 52.74 ? 2006 HOH A O 1 HETATM 6013 O O . HOH T 9 . ? 24.975 42.949 71.622 1.00 46.44 ? 2007 HOH A O 1 HETATM 6014 O O . HOH T 9 . ? 21.323 43.167 78.027 1.00 55.66 ? 2008 HOH A O 1 HETATM 6015 O O . HOH T 9 . ? 19.128 34.379 72.390 1.00 53.31 ? 2009 HOH A O 1 HETATM 6016 O O . HOH T 9 . ? 15.350 34.296 74.348 1.00 54.90 ? 2010 HOH A O 1 HETATM 6017 O O . HOH T 9 . ? 24.767 37.141 70.225 1.00 53.64 ? 2011 HOH A O 1 HETATM 6018 O O . HOH T 9 . ? 25.641 35.476 68.235 1.00 26.99 ? 2012 HOH A O 1 HETATM 6019 O O . HOH T 9 . ? 25.032 32.686 67.906 1.00 31.02 ? 2013 HOH A O 1 HETATM 6020 O O . HOH T 9 . ? 26.842 30.752 63.776 1.00 41.57 ? 2014 HOH A O 1 HETATM 6021 O O . HOH T 9 . ? 17.825 32.127 70.664 1.00 34.54 ? 2015 HOH A O 1 HETATM 6022 O O . HOH T 9 . ? 26.359 26.313 63.287 1.00 50.34 ? 2016 HOH A O 1 HETATM 6023 O O . HOH T 9 . ? 17.363 25.716 59.465 1.00 31.34 ? 2017 HOH A O 1 HETATM 6024 O O . HOH T 9 . ? 19.501 41.450 78.496 1.00 48.35 ? 2018 HOH A O 1 HETATM 6025 O O . HOH T 9 . ? 13.608 26.941 51.643 1.00 20.94 ? 2019 HOH A O 1 HETATM 6026 O O . HOH T 9 . ? 20.703 27.504 48.855 1.00 22.15 ? 2020 HOH A O 1 HETATM 6027 O O . HOH T 9 . ? 28.193 35.781 67.463 1.00 42.03 ? 2021 HOH A O 1 HETATM 6028 O O . HOH T 9 . ? 11.589 24.768 51.743 1.00 41.85 ? 2022 HOH A O 1 HETATM 6029 O O . HOH T 9 . ? 10.457 27.077 51.610 1.00 28.72 ? 2023 HOH A O 1 HETATM 6030 O O . HOH T 9 . ? 0.218 31.710 41.058 1.00 50.76 ? 2024 HOH A O 1 HETATM 6031 O O . HOH T 9 . ? 2.583 33.055 45.394 1.00 20.62 ? 2025 HOH A O 1 HETATM 6032 O O . HOH T 9 . ? 9.495 29.145 43.053 1.00 19.55 ? 2026 HOH A O 1 HETATM 6033 O O . HOH T 9 . ? -0.156 29.691 44.837 1.00 42.75 ? 2027 HOH A O 1 HETATM 6034 O O . HOH T 9 . ? 3.470 27.618 41.377 1.00 28.90 ? 2028 HOH A O 1 HETATM 6035 O O . HOH T 9 . ? 10.006 23.935 44.455 1.00 44.07 ? 2029 HOH A O 1 HETATM 6036 O O . HOH T 9 . ? 3.628 27.243 54.662 1.00 32.60 ? 2030 HOH A O 1 HETATM 6037 O O . HOH T 9 . ? 0.291 31.322 58.255 1.00 27.50 ? 2031 HOH A O 1 HETATM 6038 O O . HOH T 9 . ? 3.283 27.348 57.311 1.00 47.36 ? 2032 HOH A O 1 HETATM 6039 O O . HOH T 9 . ? 7.679 26.303 54.740 1.00 51.59 ? 2033 HOH A O 1 HETATM 6040 O O . HOH T 9 . ? 11.083 27.370 54.361 1.00 21.58 ? 2034 HOH A O 1 HETATM 6041 O O . HOH T 9 . ? 5.394 30.024 37.101 1.00 48.55 ? 2035 HOH A O 1 HETATM 6042 O O . HOH T 9 . ? 10.251 28.291 33.952 1.00 44.67 ? 2036 HOH A O 1 HETATM 6043 O O . HOH T 9 . ? 8.144 30.097 36.255 1.00 40.23 ? 2037 HOH A O 1 HETATM 6044 O O . HOH T 9 . ? 10.983 27.210 31.982 1.00 37.72 ? 2038 HOH A O 1 HETATM 6045 O O . HOH T 9 . ? -2.699 32.808 56.051 1.00 35.45 ? 2039 HOH A O 1 HETATM 6046 O O . HOH T 9 . ? -4.305 35.111 56.681 1.00 49.78 ? 2040 HOH A O 1 HETATM 6047 O O . HOH T 9 . ? 1.638 31.091 64.848 1.00 35.09 ? 2041 HOH A O 1 HETATM 6048 O O . HOH T 9 . ? -0.788 32.224 60.731 1.00 36.05 ? 2042 HOH A O 1 HETATM 6049 O O . HOH T 9 . ? 12.609 28.456 60.710 1.00 45.20 ? 2043 HOH A O 1 HETATM 6050 O O . HOH T 9 . ? 27.338 25.624 22.642 0.50 29.64 ? 2044 HOH A O 1 HETATM 6051 O O . HOH T 9 . ? 25.197 25.067 26.165 1.00 45.95 ? 2045 HOH A O 1 HETATM 6052 O O . HOH T 9 . ? 19.754 21.855 26.918 0.50 33.00 ? 2046 HOH A O 1 HETATM 6053 O O . HOH T 9 . ? 24.308 21.882 31.324 1.00 52.75 ? 2047 HOH A O 1 HETATM 6054 O O . HOH T 9 . ? 18.874 23.025 36.598 1.00 41.55 ? 2048 HOH A O 1 HETATM 6055 O O . HOH T 9 . ? 10.058 35.994 70.066 1.00 28.65 ? 2049 HOH A O 1 HETATM 6056 O O . HOH T 9 . ? 1.469 36.987 68.692 1.00 35.25 ? 2050 HOH A O 1 HETATM 6057 O O . HOH T 9 . ? -0.879 40.918 71.396 1.00 54.95 ? 2051 HOH A O 1 HETATM 6058 O O . HOH T 9 . ? -0.436 43.441 60.831 0.50 13.81 ? 2052 HOH A O 1 HETATM 6059 O O . HOH T 9 . ? -2.238 45.090 65.649 1.00 54.30 ? 2053 HOH A O 1 HETATM 6060 O O . HOH T 9 . ? 9.386 28.627 38.015 1.00 35.48 ? 2054 HOH A O 1 HETATM 6061 O O . HOH T 9 . ? 10.265 26.686 36.320 1.00 48.71 ? 2055 HOH A O 1 HETATM 6062 O O . HOH T 9 . ? -4.025 37.401 56.624 1.00 35.32 ? 2056 HOH A O 1 HETATM 6063 O O . HOH T 9 . ? -3.034 38.591 63.046 1.00 34.87 ? 2057 HOH A O 1 HETATM 6064 O O . HOH T 9 . ? -4.287 37.415 51.548 1.00 44.68 ? 2058 HOH A O 1 HETATM 6065 O O . HOH T 9 . ? -5.168 42.049 50.613 1.00 35.76 ? 2059 HOH A O 1 HETATM 6066 O O . HOH T 9 . ? -5.455 36.177 40.829 1.00 44.35 ? 2060 HOH A O 1 HETATM 6067 O O . HOH T 9 . ? -6.061 41.654 44.301 1.00 39.09 ? 2061 HOH A O 1 HETATM 6068 O O . HOH T 9 . ? 20.352 59.944 24.898 1.00 49.55 ? 2062 HOH A O 1 HETATM 6069 O O . HOH T 9 . ? 24.653 59.829 32.518 1.00 36.75 ? 2063 HOH A O 1 HETATM 6070 O O . HOH T 9 . ? 20.549 56.898 20.594 1.00 42.77 ? 2064 HOH A O 1 HETATM 6071 O O . HOH T 9 . ? 7.494 38.543 29.362 1.00 28.26 ? 2065 HOH A O 1 HETATM 6072 O O . HOH T 9 . ? 3.381 31.317 38.444 1.00 54.30 ? 2066 HOH A O 1 HETATM 6073 O O . HOH T 9 . ? 8.142 29.363 33.540 1.00 34.05 ? 2067 HOH A O 1 HETATM 6074 O O . HOH T 9 . ? 11.487 27.688 29.336 1.00 30.19 ? 2068 HOH A O 1 HETATM 6075 O O . HOH T 9 . ? 4.910 27.364 30.733 1.00 42.47 ? 2069 HOH A O 1 HETATM 6076 O O . HOH T 9 . ? 4.091 25.227 29.211 1.00 48.45 ? 2070 HOH A O 1 HETATM 6077 O O . HOH T 9 . ? 11.662 29.018 19.235 1.00 42.58 ? 2071 HOH A O 1 HETATM 6078 O O . HOH T 9 . ? 10.048 30.878 26.782 1.00 23.33 ? 2072 HOH A O 1 HETATM 6079 O O . HOH T 9 . ? 12.089 27.583 21.560 1.00 43.24 ? 2073 HOH A O 1 HETATM 6080 O O . HOH T 9 . ? 13.566 29.419 28.547 1.00 23.96 ? 2074 HOH A O 1 HETATM 6081 O O . HOH T 9 . ? 16.114 29.009 28.097 1.00 26.61 ? 2075 HOH A O 1 HETATM 6082 O O . HOH T 9 . ? 13.288 27.746 17.119 1.00 51.83 ? 2076 HOH A O 1 HETATM 6083 O O . HOH T 9 . ? 11.277 52.436 28.079 1.00 40.02 ? 2077 HOH A O 1 HETATM 6084 O O . HOH T 9 . ? 19.118 24.753 12.585 1.00 46.05 ? 2078 HOH A O 1 HETATM 6085 O O . HOH T 9 . ? 15.498 29.672 13.054 1.00 44.90 ? 2079 HOH A O 1 HETATM 6086 O O . HOH T 9 . ? 27.712 25.175 17.847 1.00 54.58 ? 2080 HOH A O 1 HETATM 6087 O O . HOH T 9 . ? 29.017 25.791 31.513 1.00 39.59 ? 2081 HOH A O 1 HETATM 6088 O O . HOH T 9 . ? 25.672 27.122 24.347 1.00 31.03 ? 2082 HOH A O 1 HETATM 6089 O O . HOH T 9 . ? 21.103 23.262 20.895 1.00 49.13 ? 2083 HOH A O 1 HETATM 6090 O O . HOH T 9 . ? 25.647 25.370 20.232 1.00 35.32 ? 2084 HOH A O 1 HETATM 6091 O O . HOH T 9 . ? 20.212 31.371 26.352 1.00 26.56 ? 2085 HOH A O 1 HETATM 6092 O O . HOH T 9 . ? 21.560 25.063 23.917 1.00 33.68 ? 2086 HOH A O 1 HETATM 6093 O O . HOH T 9 . ? 20.445 30.146 29.933 1.00 27.08 ? 2087 HOH A O 1 HETATM 6094 O O . HOH T 9 . ? 23.498 24.026 27.472 1.00 50.66 ? 2088 HOH A O 1 HETATM 6095 O O . HOH T 9 . ? 24.605 29.453 30.398 1.00 28.21 ? 2089 HOH A O 1 HETATM 6096 O O . HOH T 9 . ? 15.383 25.421 30.090 1.00 38.26 ? 2090 HOH A O 1 HETATM 6097 O O . HOH T 9 . ? 21.197 24.032 27.059 1.00 37.63 ? 2091 HOH A O 1 HETATM 6098 O O . HOH T 9 . ? 23.501 24.377 30.453 1.00 41.52 ? 2092 HOH A O 1 HETATM 6099 O O . HOH T 9 . ? 18.899 27.644 35.144 1.00 19.75 ? 2093 HOH A O 1 HETATM 6100 O O . HOH T 9 . ? 19.929 25.574 36.883 1.00 25.77 ? 2094 HOH A O 1 HETATM 6101 O O . HOH T 9 . ? -12.458 45.935 35.496 1.00 44.94 ? 2095 HOH A O 1 HETATM 6102 O O . HOH T 9 . ? 26.339 23.557 45.731 1.00 31.40 ? 2096 HOH A O 1 HETATM 6103 O O . HOH T 9 . ? 19.336 18.308 43.928 1.00 45.39 ? 2097 HOH A O 1 HETATM 6104 O O . HOH T 9 . ? 3.996 46.564 25.354 1.00 50.44 ? 2098 HOH A O 1 HETATM 6105 O O . HOH T 9 . ? 27.194 20.159 39.958 1.00 32.23 ? 2099 HOH A O 1 HETATM 6106 O O . HOH T 9 . ? 26.744 16.597 39.895 1.00 38.43 ? 2100 HOH A O 1 HETATM 6107 O O . HOH T 9 . ? 6.455 52.519 27.856 1.00 48.89 ? 2101 HOH A O 1 HETATM 6108 O O . HOH T 9 . ? 14.610 22.945 37.742 1.00 30.63 ? 2102 HOH A O 1 HETATM 6109 O O . HOH T 9 . ? 17.997 21.205 38.922 1.00 39.50 ? 2103 HOH A O 1 HETATM 6110 O O . HOH T 9 . ? 12.387 22.830 43.983 1.00 43.84 ? 2104 HOH A O 1 HETATM 6111 O O . HOH T 9 . ? 10.865 29.002 40.510 1.00 26.10 ? 2105 HOH A O 1 HETATM 6112 O O . HOH T 9 . ? 12.081 22.436 36.839 1.00 58.98 ? 2106 HOH A O 1 HETATM 6113 O O . HOH T 9 . ? 32.201 27.372 25.478 1.00 57.09 ? 2107 HOH A O 1 HETATM 6114 O O . HOH T 9 . ? 16.413 26.111 34.818 1.00 23.52 ? 2108 HOH A O 1 HETATM 6115 O O . HOH T 9 . ? 12.456 24.955 35.808 1.00 45.01 ? 2109 HOH A O 1 HETATM 6116 O O . HOH T 9 . ? 14.270 31.781 29.573 1.00 22.72 ? 2110 HOH A O 1 HETATM 6117 O O . HOH T 9 . ? 17.966 30.872 29.216 1.00 24.04 ? 2111 HOH A O 1 HETATM 6118 O O . HOH T 9 . ? 14.404 38.051 34.916 1.00 19.16 ? 2112 HOH A O 1 HETATM 6119 O O . HOH T 9 . ? 17.751 40.533 32.278 1.00 17.78 ? 2113 HOH A O 1 HETATM 6120 O O . HOH T 9 . ? 6.417 42.722 27.210 1.00 31.79 ? 2114 HOH A O 1 HETATM 6121 O O . HOH T 9 . ? 2.169 33.537 24.348 1.00 51.90 ? 2115 HOH A O 1 HETATM 6122 O O . HOH T 9 . ? 4.997 40.009 23.205 1.00 32.02 ? 2116 HOH A O 1 HETATM 6123 O O . HOH T 9 . ? 5.959 33.326 20.886 1.00 61.47 ? 2117 HOH A O 1 HETATM 6124 O O . HOH T 9 . ? 8.784 41.737 19.741 1.00 49.89 ? 2118 HOH A O 1 HETATM 6125 O O . HOH T 9 . ? 41.054 42.991 15.402 1.00 57.10 ? 2119 HOH A O 1 HETATM 6126 O O . HOH T 9 . ? 10.019 38.926 15.573 1.00 51.87 ? 2120 HOH A O 1 HETATM 6127 O O . HOH T 9 . ? 26.202 39.994 13.415 1.00 33.68 ? 2121 HOH A O 1 HETATM 6128 O O . HOH T 9 . ? 35.002 49.173 33.120 1.00 40.21 ? 2122 HOH A O 1 HETATM 6129 O O . HOH T 9 . ? 29.349 54.349 34.576 1.00 29.97 ? 2123 HOH A O 1 HETATM 6130 O O . HOH T 9 . ? 33.576 53.491 31.655 1.00 34.49 ? 2124 HOH A O 1 HETATM 6131 O O . HOH T 9 . ? 19.950 57.815 27.419 1.00 32.69 ? 2125 HOH A O 1 HETATM 6132 O O . HOH T 9 . ? 22.540 58.439 24.288 1.00 28.35 ? 2126 HOH A O 1 HETATM 6133 O O . HOH T 9 . ? 31.390 57.133 31.255 1.00 44.04 ? 2127 HOH A O 1 HETATM 6134 O O . HOH T 9 . ? 25.032 56.877 32.199 1.00 31.51 ? 2128 HOH A O 1 HETATM 6135 O O . HOH T 9 . ? 26.414 60.193 30.616 1.00 35.07 ? 2129 HOH A O 1 HETATM 6136 O O . HOH T 9 . ? 31.779 57.973 26.301 1.00 46.39 ? 2130 HOH A O 1 HETATM 6137 O O . HOH T 9 . ? 30.227 59.705 25.086 0.50 27.84 ? 2131 HOH A O 1 HETATM 6138 O O . HOH T 9 . ? 28.493 56.668 33.989 1.00 43.76 ? 2132 HOH A O 1 HETATM 6139 O O . HOH T 9 . ? 31.717 55.260 26.202 1.00 34.65 ? 2133 HOH A O 1 HETATM 6140 O O . HOH T 9 . ? 22.855 58.764 21.434 1.00 39.77 ? 2134 HOH A O 1 HETATM 6141 O O . HOH T 9 . ? 23.005 61.018 20.074 1.00 40.64 ? 2135 HOH A O 1 HETATM 6142 O O . HOH T 9 . ? 28.146 63.706 22.949 1.00 38.81 ? 2136 HOH A O 1 HETATM 6143 O O . HOH T 9 . ? 30.234 61.395 22.702 1.00 48.73 ? 2137 HOH A O 1 HETATM 6144 O O . HOH T 9 . ? 21.202 54.253 16.167 1.00 38.86 ? 2138 HOH A O 1 HETATM 6145 O O . HOH T 9 . ? 6.703 53.755 75.580 1.00 30.92 ? 2139 HOH A O 1 HETATM 6146 O O . HOH T 9 . ? 21.426 50.797 11.139 1.00 44.79 ? 2140 HOH A O 1 HETATM 6147 O O . HOH T 9 . ? 16.103 50.068 10.817 1.00 50.21 ? 2141 HOH A O 1 HETATM 6148 O O . HOH T 9 . ? 20.147 43.847 11.394 1.00 39.20 ? 2142 HOH A O 1 HETATM 6149 O O . HOH T 9 . ? 19.793 47.058 10.398 1.00 56.45 ? 2143 HOH A O 1 HETATM 6150 O O . HOH T 9 . ? 36.519 46.364 31.709 1.00 38.51 ? 2144 HOH A O 1 HETATM 6151 O O . HOH T 9 . ? 23.864 46.019 34.720 1.00 19.06 ? 2145 HOH A O 1 HETATM 6152 O O . HOH T 9 . ? 29.371 47.797 37.452 1.00 57.04 ? 2146 HOH A O 1 HETATM 6153 O O . HOH T 9 . ? 28.306 53.339 37.098 1.00 36.92 ? 2147 HOH A O 1 HETATM 6154 O O . HOH T 9 . ? 32.095 49.093 37.775 1.00 50.17 ? 2148 HOH A O 1 HETATM 6155 O O . HOH T 9 . ? 15.028 57.343 32.261 1.00 38.92 ? 2149 HOH A O 1 HETATM 6156 O O . HOH T 9 . ? 11.967 56.228 31.463 1.00 35.39 ? 2150 HOH A O 1 HETATM 6157 O O . HOH T 9 . ? 18.292 55.397 30.522 1.00 25.88 ? 2151 HOH A O 1 HETATM 6158 O O . HOH T 9 . ? 19.696 55.903 23.061 1.00 30.88 ? 2152 HOH A O 1 HETATM 6159 O O . HOH T 9 . ? 21.053 56.487 25.239 1.00 27.70 ? 2153 HOH A O 1 HETATM 6160 O O . HOH T 9 . ? 12.466 50.234 27.461 1.00 29.04 ? 2154 HOH A O 1 HETATM 6161 O O . HOH T 9 . ? 28.756 63.746 69.032 1.00 44.69 ? 2155 HOH A O 1 HETATM 6162 O O . HOH T 9 . ? 13.792 50.265 18.969 1.00 28.90 ? 2156 HOH A O 1 HETATM 6163 O O . HOH T 9 . ? 12.122 43.443 17.239 1.00 35.12 ? 2157 HOH A O 1 HETATM 6164 O O . HOH T 9 . ? 14.034 40.480 12.286 1.00 44.54 ? 2158 HOH A O 1 HETATM 6165 O O . HOH T 9 . ? 37.253 56.609 64.292 1.00 41.70 ? 2159 HOH A O 1 HETATM 6166 O O . HOH T 9 . ? 40.035 56.769 60.824 1.00 42.24 ? 2160 HOH A O 1 HETATM 6167 O O . HOH T 9 . ? 24.403 37.168 32.558 1.00 20.67 ? 2161 HOH A O 1 HETATM 6168 O O . HOH T 9 . ? 26.354 38.959 36.232 1.00 20.57 ? 2162 HOH A O 1 HETATM 6169 O O . HOH T 9 . ? 37.016 41.871 37.561 1.00 51.04 ? 2163 HOH A O 1 HETATM 6170 O O . HOH T 9 . ? 29.950 42.655 32.201 1.00 22.34 ? 2164 HOH A O 1 HETATM 6171 O O . HOH T 9 . ? 38.695 38.868 35.327 1.00 49.65 ? 2165 HOH A O 1 HETATM 6172 O O . HOH T 9 . ? 40.598 40.040 43.152 1.00 48.60 ? 2166 HOH A O 1 HETATM 6173 O O . HOH T 9 . ? 42.209 34.735 38.028 1.00 44.58 ? 2167 HOH A O 1 HETATM 6174 O O . HOH T 9 . ? 40.871 32.341 39.381 1.00 33.27 ? 2168 HOH A O 1 HETATM 6175 O O . HOH T 9 . ? 38.677 30.973 45.248 1.00 56.16 ? 2169 HOH A O 1 HETATM 6176 O O . HOH T 9 . ? 42.658 31.174 41.069 1.00 51.94 ? 2170 HOH A O 1 HETATM 6177 O O . HOH T 9 . ? 44.727 27.488 41.065 1.00 48.76 ? 2171 HOH A O 1 HETATM 6178 O O . HOH T 9 . ? 30.062 25.376 47.434 1.00 34.71 ? 2172 HOH A O 1 HETATM 6179 O O . HOH T 9 . ? 30.514 25.860 38.474 1.00 41.05 ? 2173 HOH A O 1 HETATM 6180 O O . HOH T 9 . ? 35.089 21.021 44.123 1.00 45.66 ? 2174 HOH A O 1 HETATM 6181 O O . HOH T 9 . ? 37.325 26.119 48.082 1.00 56.12 ? 2175 HOH A O 1 HETATM 6182 O O . HOH T 9 . ? 38.743 42.996 51.047 1.00 55.35 ? 2176 HOH A O 1 HETATM 6183 O O . HOH T 9 . ? 29.456 36.159 44.424 1.00 20.79 ? 2177 HOH A O 1 HETATM 6184 O O . HOH T 9 . ? 27.507 31.106 28.753 1.00 25.89 ? 2178 HOH A O 1 HETATM 6185 O O . HOH T 9 . ? 29.961 27.080 33.720 1.00 26.15 ? 2179 HOH A O 1 HETATM 6186 O O . HOH T 9 . ? 28.903 33.863 32.826 1.00 22.21 ? 2180 HOH A O 1 HETATM 6187 O O . HOH T 9 . ? 23.055 44.349 36.724 1.00 20.43 ? 2181 HOH A O 1 HETATM 6188 O O . HOH T 9 . ? 34.738 35.551 58.408 1.00 44.97 ? 2182 HOH A O 1 HETATM 6189 O O . HOH T 9 . ? 29.594 37.841 66.391 0.50 22.32 ? 2183 HOH A O 1 HETATM 6190 O O . HOH T 9 . ? 11.452 48.782 29.653 1.00 19.76 ? 2184 HOH A O 1 HETATM 6191 O O . HOH T 9 . ? 8.730 54.432 31.330 1.00 30.38 ? 2185 HOH A O 1 HETATM 6192 O O . HOH T 9 . ? 14.955 52.550 34.846 1.00 24.63 ? 2186 HOH A O 1 HETATM 6193 O O . HOH T 9 . ? 13.658 55.074 32.891 1.00 27.83 ? 2187 HOH A O 1 HETATM 6194 O O . HOH T 9 . ? 5.829 56.179 35.928 1.00 20.57 ? 2188 HOH A O 1 HETATM 6195 O O . HOH T 9 . ? 6.864 58.267 37.568 1.00 15.46 ? 2189 HOH A O 1 HETATM 6196 O O . HOH T 9 . ? 14.035 57.467 35.211 1.00 18.05 ? 2190 HOH A O 1 HETATM 6197 O O . HOH T 9 . ? 7.509 57.379 33.740 1.00 40.26 ? 2191 HOH A O 1 HETATM 6198 O O . HOH T 9 . ? 12.589 53.362 35.990 1.00 21.37 ? 2192 HOH A O 1 HETATM 6199 O O . HOH T 9 . ? 11.964 56.374 77.300 1.00 42.85 ? 2193 HOH A O 1 HETATM 6200 O O . HOH T 9 . ? 6.732 54.859 43.931 1.00 15.69 ? 2194 HOH A O 1 HETATM 6201 O O . HOH T 9 . ? 14.976 60.076 76.994 1.00 42.49 ? 2195 HOH A O 1 HETATM 6202 O O . HOH T 9 . ? 0.962 50.473 39.888 1.00 14.31 ? 2196 HOH A O 1 HETATM 6203 O O . HOH T 9 . ? -2.641 44.170 37.723 1.00 18.56 ? 2197 HOH A O 1 HETATM 6204 O O . HOH T 9 . ? 25.532 71.590 60.945 0.50 29.17 ? 2198 HOH A O 1 HETATM 6205 O O . HOH T 9 . ? 25.951 74.502 58.452 1.00 40.43 ? 2199 HOH A O 1 HETATM 6206 O O . HOH T 9 . ? 27.470 65.808 55.356 1.00 34.63 ? 2200 HOH A O 1 HETATM 6207 O O . HOH T 9 . ? 24.459 79.272 55.433 1.00 40.86 ? 2201 HOH A O 1 HETATM 6208 O O . HOH T 9 . ? 29.614 67.328 45.534 1.00 34.50 ? 2202 HOH A O 1 HETATM 6209 O O . HOH T 9 . ? -4.330 53.291 37.222 1.00 29.38 ? 2203 HOH A O 1 HETATM 6210 O O . HOH T 9 . ? -3.635 55.981 36.757 1.00 55.68 ? 2204 HOH A O 1 HETATM 6211 O O . HOH T 9 . ? 28.557 80.068 44.635 1.00 54.87 ? 2205 HOH A O 1 HETATM 6212 O O . HOH T 9 . ? -6.199 58.664 38.098 1.00 24.94 ? 2206 HOH A O 1 HETATM 6213 O O . HOH T 9 . ? 32.031 76.913 38.225 1.00 57.39 ? 2207 HOH A O 1 HETATM 6214 O O . HOH T 9 . ? -7.223 48.112 48.117 1.00 39.01 ? 2208 HOH A O 1 HETATM 6215 O O . HOH T 9 . ? -10.654 43.591 38.689 1.00 48.35 ? 2209 HOH A O 1 HETATM 6216 O O . HOH T 9 . ? -8.944 41.354 48.163 1.00 38.75 ? 2210 HOH A O 1 HETATM 6217 O O . HOH T 9 . ? -10.086 43.745 47.078 1.00 31.09 ? 2211 HOH A O 1 HETATM 6218 O O . HOH T 9 . ? -12.872 47.547 37.577 1.00 31.56 ? 2212 HOH A O 1 HETATM 6219 O O . HOH T 9 . ? -10.501 48.690 48.705 1.00 24.88 ? 2213 HOH A O 1 HETATM 6220 O O . HOH T 9 . ? 26.144 85.761 45.605 1.00 43.34 ? 2214 HOH A O 1 HETATM 6221 O O . HOH T 9 . ? 26.196 82.229 48.253 1.00 55.31 ? 2215 HOH A O 1 HETATM 6222 O O . HOH T 9 . ? 24.438 81.353 50.475 1.00 44.74 ? 2216 HOH A O 1 HETATM 6223 O O . HOH T 9 . ? -10.577 51.162 28.849 1.00 59.28 ? 2217 HOH A O 1 HETATM 6224 O O . HOH T 9 . ? 23.053 79.341 60.215 1.00 46.65 ? 2218 HOH A O 1 HETATM 6225 O O . HOH T 9 . ? -8.832 43.488 34.893 1.00 52.24 ? 2219 HOH A O 1 HETATM 6226 O O . HOH T 9 . ? -9.763 45.936 34.381 1.00 34.21 ? 2220 HOH A O 1 HETATM 6227 O O . HOH T 9 . ? -9.112 46.262 32.054 1.00 51.46 ? 2221 HOH A O 1 HETATM 6228 O O . HOH T 9 . ? -7.585 41.670 41.002 1.00 35.45 ? 2222 HOH A O 1 HETATM 6229 O O . HOH T 9 . ? 1.531 55.784 30.504 1.00 54.16 ? 2223 HOH A O 1 HETATM 6230 O O . HOH T 9 . ? -5.096 44.484 30.901 1.00 37.84 ? 2224 HOH A O 1 HETATM 6231 O O . HOH T 9 . ? -4.574 53.844 34.614 1.00 30.56 ? 2225 HOH A O 1 HETATM 6232 O O . HOH T 9 . ? 13.651 81.286 65.930 1.00 43.73 ? 2226 HOH A O 1 HETATM 6233 O O . HOH T 9 . ? 12.913 71.743 80.232 1.00 35.24 ? 2227 HOH A O 1 HETATM 6234 O O . HOH T 9 . ? 16.699 70.964 79.295 1.00 36.00 ? 2228 HOH A O 1 HETATM 6235 O O . HOH T 9 . ? 3.298 48.747 26.647 1.00 36.87 ? 2229 HOH A O 1 HETATM 6236 O O . HOH T 9 . ? -4.171 44.100 27.041 1.00 48.21 ? 2230 HOH A O 1 HETATM 6237 O O . HOH T 9 . ? -3.689 46.637 25.038 1.00 39.30 ? 2231 HOH A O 1 HETATM 6238 O O . HOH T 9 . ? -5.629 50.708 28.512 1.00 37.59 ? 2232 HOH A O 1 HETATM 6239 O O . HOH T 9 . ? 4.753 50.139 28.326 1.00 32.24 ? 2233 HOH A O 1 HETATM 6240 O O . HOH T 9 . ? 5.947 53.620 30.115 1.00 29.72 ? 2234 HOH A O 1 HETATM 6241 O O . HOH T 9 . ? 8.935 51.930 28.795 1.00 49.42 ? 2235 HOH A O 1 HETATM 6242 O O . HOH T 9 . ? 8.268 50.475 25.396 1.00 43.46 ? 2236 HOH A O 1 HETATM 6243 O O . HOH T 9 . ? 6.043 44.891 25.591 1.00 33.69 ? 2237 HOH A O 1 HETATM 6244 O O . HOH T 9 . ? 14.682 36.702 27.972 1.00 17.98 ? 2238 HOH A O 1 HETATM 6245 O O . HOH T 9 . ? 21.364 32.353 28.765 1.00 25.74 ? 2239 HOH A O 1 HETATM 6246 O O . HOH T 9 . ? 32.957 29.973 24.544 1.00 39.20 ? 2240 HOH A O 1 HETATM 6247 O O . HOH T 9 . ? 32.602 26.859 34.338 1.00 56.14 ? 2241 HOH A O 1 HETATM 6248 O O . HOH T 9 . ? 33.769 29.048 34.233 1.00 36.84 ? 2242 HOH A O 1 HETATM 6249 O O . HOH T 9 . ? 18.057 61.803 28.202 1.00 46.11 ? 2243 HOH A O 1 HETATM 6250 O O . HOH T 9 . ? 26.945 28.308 28.370 1.00 40.29 ? 2244 HOH A O 1 HETATM 6251 O O . HOH T 9 . ? 29.113 28.242 24.998 1.00 45.48 ? 2245 HOH A O 1 HETATM 6252 O O . HOH T 9 . ? 24.275 31.655 28.770 1.00 26.09 ? 2246 HOH A O 1 HETATM 6253 O O . HOH T 9 . ? 38.095 34.448 26.451 1.00 34.88 ? 2247 HOH A O 1 HETATM 6254 O O . HOH T 9 . ? 34.205 32.689 27.319 1.00 40.71 ? 2248 HOH A O 1 HETATM 6255 O O . HOH T 9 . ? 27.282 65.560 45.983 1.00 30.09 ? 2249 HOH A O 1 HETATM 6256 O O . HOH T 9 . ? 30.715 35.439 16.787 1.00 39.86 ? 2250 HOH A O 1 HETATM 6257 O O . HOH T 9 . ? 31.023 31.669 17.138 1.00 36.26 ? 2251 HOH A O 1 HETATM 6258 O O . HOH T 9 . ? 25.770 59.992 36.153 1.00 52.24 ? 2252 HOH A O 1 HETATM 6259 O O . HOH T 9 . ? 34.621 41.131 19.409 1.00 38.83 ? 2253 HOH A O 1 HETATM 6260 O O . HOH T 9 . ? 20.191 61.668 27.173 1.00 37.20 ? 2254 HOH A O 1 HETATM 6261 O O . HOH T 9 . ? 26.774 64.749 28.767 1.00 32.18 ? 2255 HOH A O 1 HETATM 6262 O O . HOH T 9 . ? 36.276 38.898 14.956 1.00 39.62 ? 2256 HOH A O 1 HETATM 6263 O O . HOH T 9 . ? 14.595 69.895 30.320 1.00 31.26 ? 2257 HOH A O 1 HETATM 6264 O O . HOH T 9 . ? 29.452 30.413 15.083 1.00 43.64 ? 2258 HOH A O 1 HETATM 6265 O O . HOH T 9 . ? 31.040 29.264 11.138 1.00 50.86 ? 2259 HOH A O 1 HETATM 6266 O O . HOH T 9 . ? 34.052 44.100 8.965 1.00 55.00 ? 2260 HOH A O 1 HETATM 6267 O O . HOH T 9 . ? 37.321 52.451 16.316 1.00 52.61 ? 2261 HOH A O 1 HETATM 6268 O O . HOH T 9 . ? 37.739 51.069 13.307 1.00 59.86 ? 2262 HOH A O 1 HETATM 6269 O O . HOH T 9 . ? 40.339 47.488 28.958 1.00 58.59 ? 2263 HOH A O 1 HETATM 6270 O O . HOH T 9 . ? 42.567 53.120 24.924 1.00 50.19 ? 2264 HOH A O 1 HETATM 6271 O O . HOH T 9 . ? 33.505 54.303 28.040 1.00 40.27 ? 2265 HOH A O 1 HETATM 6272 O O . HOH T 9 . ? 34.847 51.081 31.031 1.00 36.48 ? 2266 HOH A O 1 HETATM 6273 O O . HOH T 9 . ? 36.826 48.391 30.169 1.00 40.12 ? 2267 HOH A O 1 HETATM 6274 O O . HOH T 9 . ? 38.944 45.012 31.252 1.00 50.60 ? 2268 HOH A O 1 HETATM 6275 O O . HOH T 9 . ? 40.306 41.444 26.426 1.00 41.56 ? 2269 HOH A O 1 HETATM 6276 O O . HOH T 9 . ? 39.728 41.478 34.165 1.00 52.92 ? 2270 HOH A O 1 HETATM 6277 O O . HOH T 9 . ? 38.609 35.189 19.422 1.00 48.33 ? 2271 HOH A O 1 HETATM 6278 O O . HOH T 9 . ? 41.527 38.955 20.563 1.00 54.33 ? 2272 HOH A O 1 HETATM 6279 O O . HOH T 9 . ? 40.500 42.638 23.592 1.00 51.15 ? 2273 HOH A O 1 HETATM 6280 O O . HOH T 9 . ? 40.588 45.040 19.725 1.00 40.62 ? 2274 HOH A O 1 HETATM 6281 O O . HOH T 9 . ? 32.540 42.748 20.035 1.00 36.63 ? 2275 HOH A O 1 HETATM 6282 O O . HOH T 9 . ? 39.800 45.271 16.302 1.00 45.16 ? 2276 HOH A O 1 HETATM 6283 O O . HOH T 9 . ? 31.373 50.137 11.495 1.00 43.88 ? 2277 HOH A O 1 HETATM 6284 O O . HOH T 9 . ? 27.652 40.159 9.503 1.00 54.62 ? 2278 HOH A O 1 HETATM 6285 O O . HOH T 9 . ? 25.673 39.370 10.923 1.00 48.37 ? 2279 HOH A O 1 HETATM 6286 O O . HOH T 9 . ? 4.954 31.376 24.670 1.00 32.99 ? 2280 HOH A O 1 HETATM 6287 O O . HOH T 9 . ? 12.041 36.924 28.700 1.00 20.80 ? 2281 HOH A O 1 HETATM 6288 O O . HOH T 9 . ? 6.172 38.620 26.503 1.00 26.15 ? 2282 HOH A O 1 HETATM 6289 O O . HOH T 9 . ? 4.902 31.440 30.521 1.00 33.94 ? 2283 HOH A O 1 HETATM 6290 O O . HOH T 9 . ? 2.992 38.337 27.195 1.00 34.63 ? 2284 HOH A O 1 HETATM 6291 O O . HOH T 9 . ? 1.889 40.973 27.170 1.00 41.87 ? 2285 HOH A O 1 HETATM 6292 O O . HOH T 9 . ? -3.679 35.601 34.803 1.00 48.65 ? 2286 HOH A O 1 HETATM 6293 O O . HOH T 9 . ? -2.974 37.928 32.646 1.00 27.99 ? 2287 HOH A O 1 HETATM 6294 O O . HOH T 9 . ? 0.635 33.445 36.650 1.00 38.25 ? 2288 HOH A O 1 HETATM 6295 O O . HOH T 9 . ? 0.448 33.311 43.424 1.00 21.86 ? 2289 HOH A O 1 HETATM 6296 O O . HOH T 9 . ? -5.502 34.123 47.681 1.00 37.31 ? 2290 HOH A O 1 HETATM 6297 O O . HOH T 9 . ? -2.191 33.903 40.614 1.00 24.89 ? 2291 HOH A O 1 HETATM 6298 O O . HOH T 9 . ? -1.682 32.275 44.782 1.00 30.90 ? 2292 HOH A O 1 HETATM 6299 O O . HOH T 9 . ? -1.117 51.424 72.666 1.00 32.31 ? 2293 HOH A O 1 HETATM 6300 O O . HOH T 9 . ? -1.040 57.022 74.114 1.00 46.61 ? 2294 HOH A O 1 HETATM 6301 O O . HOH T 9 . ? 5.661 62.792 70.544 1.00 23.69 ? 2295 HOH A O 1 HETATM 6302 O O . HOH T 9 . ? -1.306 61.587 62.374 1.00 27.08 ? 2296 HOH A O 1 HETATM 6303 O O . HOH T 9 . ? 11.745 40.835 55.448 1.00 20.79 ? 2297 HOH A O 1 HETATM 6304 O O . HOH T 9 . ? 10.838 36.673 42.409 1.00 17.28 ? 2298 HOH A O 1 HETATM 6305 O O . HOH T 9 . ? 14.590 32.049 48.198 1.00 17.92 ? 2299 HOH A O 1 HETATM 6306 O O . HOH T 9 . ? 13.554 29.863 40.195 1.00 18.76 ? 2300 HOH A O 1 HETATM 6307 O O . HOH T 9 . ? 18.429 33.510 43.548 1.00 19.33 ? 2301 HOH A O 1 HETATM 6308 O O . HOH T 9 . ? 16.758 37.055 44.027 1.00 16.07 ? 2302 HOH A O 1 HETATM 6309 O O . HOH T 9 . ? 12.084 34.915 53.750 1.00 19.79 ? 2303 HOH A O 1 HETATM 6310 O O . HOH T 9 . ? 11.610 38.364 56.679 1.00 23.98 ? 2304 HOH A O 1 HETATM 6311 O O . HOH T 9 . ? 12.689 32.774 70.923 1.00 34.60 ? 2305 HOH A O 1 HETATM 6312 O O . HOH T 9 . ? 13.338 30.560 66.466 1.00 41.71 ? 2306 HOH A O 1 HETATM 6313 O O . HOH T 9 . ? 10.555 36.487 76.467 1.00 35.22 ? 2307 HOH A O 1 HETATM 6314 O O . HOH T 9 . ? 4.248 43.660 75.987 1.00 40.89 ? 2308 HOH A O 1 HETATM 6315 O O . HOH T 9 . ? 8.618 51.851 75.340 1.00 36.37 ? 2309 HOH A O 1 HETATM 6316 O O . HOH T 9 . ? 7.771 49.268 77.929 1.00 56.58 ? 2310 HOH A O 1 HETATM 6317 O O . HOH T 9 . ? 8.020 56.505 75.739 1.00 29.58 ? 2311 HOH A O 1 HETATM 6318 O O . HOH T 9 . ? 4.799 62.094 75.168 1.00 25.48 ? 2312 HOH A O 1 HETATM 6319 O O . HOH T 9 . ? 6.469 60.702 67.172 1.00 22.15 ? 2313 HOH A O 1 HETATM 6320 O O . HOH T 9 . ? 10.526 37.186 54.515 1.00 24.98 ? 2314 HOH A O 1 HETATM 6321 O O . HOH T 9 . ? 4.582 34.919 45.466 1.00 17.99 ? 2315 HOH A O 1 HETATM 6322 O O . HOH T 9 . ? 7.906 50.308 40.868 1.00 15.04 ? 2316 HOH A O 1 HETATM 6323 O O . HOH T 9 . ? -1.789 46.066 55.837 1.00 33.33 ? 2317 HOH A O 1 HETATM 6324 O O . HOH T 9 . ? -2.217 55.500 46.149 1.00 19.82 ? 2318 HOH A O 1 HETATM 6325 O O . HOH T 9 . ? -8.371 49.530 50.086 1.00 29.95 ? 2319 HOH A O 1 HETATM 6326 O O . HOH T 9 . ? -8.432 47.604 52.077 1.00 29.95 ? 2320 HOH A O 1 HETATM 6327 O O . HOH T 9 . ? -4.612 55.208 51.810 1.00 18.77 ? 2321 HOH A O 1 HETATM 6328 O O . HOH T 9 . ? -6.669 45.204 49.391 1.00 42.68 ? 2322 HOH A O 1 HETATM 6329 O O . HOH T 9 . ? -3.435 47.082 53.210 1.00 35.33 ? 2323 HOH A O 1 HETATM 6330 O O . HOH T 9 . ? -3.462 48.118 55.874 1.00 48.65 ? 2324 HOH A O 1 HETATM 6331 O O . HOH T 9 . ? -2.494 59.287 48.569 1.00 21.13 ? 2325 HOH A O 1 HETATM 6332 O O . HOH T 9 . ? -4.440 59.514 57.260 1.00 17.84 ? 2326 HOH A O 1 HETATM 6333 O O . HOH T 9 . ? -3.909 57.652 46.371 1.00 21.21 ? 2327 HOH A O 1 HETATM 6334 O O . HOH T 9 . ? 3.598 62.263 50.500 1.00 17.80 ? 2328 HOH A O 1 HETATM 6335 O O . HOH T 9 . ? -0.136 60.371 48.483 1.00 31.90 ? 2329 HOH A O 1 HETATM 6336 O O . HOH T 9 . ? 2.943 64.824 51.028 1.00 23.44 ? 2330 HOH A O 1 HETATM 6337 O O . HOH T 9 . ? -3.638 62.231 53.979 1.00 16.61 ? 2331 HOH A O 1 HETATM 6338 O O . HOH T 9 . ? -5.449 59.688 59.780 1.00 16.29 ? 2332 HOH A O 1 HETATM 6339 O O . HOH T 9 . ? -3.506 60.049 61.858 1.00 16.72 ? 2333 HOH A O 1 HETATM 6340 O O . HOH T 9 . ? -6.388 54.121 61.017 1.00 18.75 ? 2334 HOH A O 1 HETATM 6341 O O . HOH T 9 . ? 9.635 60.800 57.731 1.00 15.69 ? 2335 HOH A O 1 HETATM 6342 O O . HOH T 9 . ? 19.276 47.674 54.610 1.00 16.38 ? 2336 HOH A O 1 HETATM 6343 O O . HOH T 9 . ? 13.875 40.791 53.556 1.00 18.35 ? 2337 HOH A O 1 HETATM 6344 O O . HOH T 9 . ? 24.751 44.038 45.412 1.00 43.24 ? 2338 HOH A O 1 HETATM 6345 O O . HOH T 9 . ? 28.920 47.129 45.700 1.00 44.21 ? 2339 HOH A O 1 HETATM 6346 O O . HOH T 9 . ? 36.075 42.825 57.789 1.00 31.90 ? 2340 HOH A O 1 HETATM 6347 O O . HOH T 9 . ? 34.512 41.606 50.398 1.00 26.34 ? 2341 HOH A O 1 HETATM 6348 O O . HOH T 9 . ? 37.033 40.003 55.903 1.00 40.41 ? 2342 HOH A O 1 HETATM 6349 O O . HOH T 9 . ? 39.587 50.701 52.347 1.00 50.31 ? 2343 HOH A O 1 HETATM 6350 O O . HOH T 9 . ? 31.007 52.563 53.457 1.00 26.10 ? 2344 HOH A O 1 HETATM 6351 O O . HOH T 9 . ? 23.345 49.747 52.205 1.00 36.33 ? 2345 HOH A O 1 HETATM 6352 O O . HOH T 9 . ? 24.998 48.764 43.882 1.00 36.32 ? 2346 HOH A O 1 HETATM 6353 O O . HOH T 9 . ? 22.407 49.823 44.913 1.00 28.25 ? 2347 HOH A O 1 HETATM 6354 O O . HOH T 9 . ? 20.754 53.107 47.504 1.00 17.66 ? 2348 HOH A O 1 HETATM 6355 O O . HOH T 9 . ? 21.926 61.332 51.798 1.00 21.75 ? 2349 HOH A O 1 HETATM 6356 O O . HOH T 9 . ? 20.039 61.412 62.966 1.00 19.03 ? 2350 HOH A O 1 HETATM 6357 O O . HOH T 9 . ? 26.118 62.230 65.715 1.00 43.66 ? 2351 HOH A O 1 HETATM 6358 O O . HOH T 9 . ? 21.739 56.221 67.804 1.00 54.88 ? 2352 HOH A O 1 HETATM 6359 O O . HOH T 9 . ? 27.340 63.139 63.617 1.00 49.71 ? 2353 HOH A O 1 HETATM 6360 O O . HOH T 9 . ? 22.059 58.549 70.065 1.00 56.68 ? 2354 HOH A O 1 HETATM 6361 O O . HOH T 9 . ? 26.979 56.840 70.653 1.00 31.68 ? 2355 HOH A O 1 HETATM 6362 O O . HOH T 9 . ? 28.334 60.795 68.941 1.00 43.08 ? 2356 HOH A O 1 HETATM 6363 O O . HOH T 9 . ? 32.668 54.238 70.848 1.00 44.34 ? 2357 HOH A O 1 HETATM 6364 O O . HOH T 9 . ? 28.536 44.515 65.471 1.00 33.04 ? 2358 HOH A O 1 HETATM 6365 O O . HOH T 9 . ? 27.981 42.751 71.012 1.00 46.21 ? 2359 HOH A O 1 HETATM 6366 O O . HOH T 9 . ? 34.880 43.641 68.554 1.00 38.30 ? 2360 HOH A O 1 HETATM 6367 O O . HOH T 9 . ? 36.521 42.248 65.562 1.00 29.50 ? 2361 HOH A O 1 HETATM 6368 O O . HOH T 9 . ? 33.974 47.766 59.353 1.00 25.78 ? 2362 HOH A O 1 HETATM 6369 O O . HOH T 9 . ? 39.643 43.655 58.713 1.00 32.28 ? 2363 HOH A O 1 HETATM 6370 O O . HOH T 9 . ? 42.136 45.704 68.086 1.00 53.98 ? 2364 HOH A O 1 HETATM 6371 O O . HOH T 9 . ? 34.315 45.661 70.236 1.00 37.69 ? 2365 HOH A O 1 HETATM 6372 O O . HOH T 9 . ? 33.985 54.854 68.144 1.00 42.97 ? 2366 HOH A O 1 HETATM 6373 O O . HOH T 9 . ? 30.991 61.286 64.505 1.00 43.64 ? 2367 HOH A O 1 HETATM 6374 O O . HOH T 9 . ? 38.696 55.047 62.645 1.00 34.36 ? 2368 HOH A O 1 HETATM 6375 O O . HOH T 9 . ? 36.723 51.957 68.961 1.00 31.84 ? 2369 HOH A O 1 HETATM 6376 O O . HOH T 9 . ? 39.404 57.409 58.246 1.00 36.56 ? 2370 HOH A O 1 HETATM 6377 O O . HOH T 9 . ? 41.260 56.298 56.479 1.00 47.03 ? 2371 HOH A O 1 HETATM 6378 O O . HOH T 9 . ? 38.507 42.858 55.739 1.00 41.38 ? 2372 HOH A O 1 HETATM 6379 O O . HOH T 9 . ? 35.009 55.814 51.623 1.00 35.89 ? 2373 HOH A O 1 HETATM 6380 O O . HOH T 9 . ? 37.087 59.291 64.119 1.00 37.67 ? 2374 HOH A O 1 HETATM 6381 O O . HOH T 9 . ? 38.252 59.938 58.243 1.00 56.79 ? 2375 HOH A O 1 HETATM 6382 O O . HOH T 9 . ? 29.123 60.518 57.594 1.00 30.05 ? 2376 HOH A O 1 HETATM 6383 O O . HOH T 9 . ? 28.645 53.752 53.299 1.00 22.91 ? 2377 HOH A O 1 HETATM 6384 O O . HOH T 9 . ? 29.915 60.809 53.304 1.00 33.93 ? 2378 HOH A O 1 HETATM 6385 O O . HOH T 9 . ? 29.352 60.973 50.795 1.00 46.94 ? 2379 HOH A O 1 HETATM 6386 O O . HOH T 9 . ? 27.330 54.079 50.855 1.00 26.47 ? 2380 HOH A O 1 HETATM 6387 O O . HOH T 9 . ? 29.112 58.018 48.688 1.00 46.88 ? 2381 HOH A O 1 HETATM 6388 O O . HOH T 9 . ? 26.039 59.993 47.788 1.00 33.69 ? 2382 HOH A O 1 HETATM 6389 O O . HOH T 9 . ? 17.382 59.086 44.923 1.00 18.92 ? 2383 HOH A O 1 HETATM 6390 O O . HOH T 9 . ? 19.178 60.001 50.299 1.00 23.64 ? 2384 HOH A O 1 HETATM 6391 O O . HOH T 9 . ? 19.687 49.317 45.021 1.00 18.29 ? 2385 HOH A O 1 HETATM 6392 O O . HOH T 9 . ? 13.543 44.626 49.909 1.00 14.21 ? 2386 HOH A O 1 HETATM 6393 O O . HOH T 9 . ? 8.107 44.661 46.437 1.00 13.52 ? 2387 HOH A O 1 HETATM 6394 O O . HOH T 9 . ? 8.100 51.786 43.189 1.00 19.85 ? 2388 HOH A O 1 HETATM 6395 O O . HOH T 9 . ? 10.170 51.745 40.044 1.00 14.88 ? 2389 HOH A O 1 HETATM 6396 O O . HOH T 9 . ? 9.088 50.683 46.486 1.00 14.88 ? 2390 HOH A O 1 HETATM 6397 O O . HOH T 9 . ? 0.242 56.919 45.781 1.00 17.95 ? 2391 HOH A O 1 HETATM 6398 O O . HOH T 9 . ? 21.824 47.553 52.279 1.00 38.06 ? 2392 HOH A O 1 HETATM 6399 O O . HOH T 9 . ? 40.912 45.055 51.106 1.00 44.79 ? 2393 HOH A O 1 HETATM 6400 O O . HOH T 9 . ? 36.682 43.267 49.487 1.00 37.79 ? 2394 HOH A O 1 HETATM 6401 O O . HOH T 9 . ? 38.670 42.050 42.460 1.00 53.81 ? 2395 HOH A O 1 HETATM 6402 O O . HOH T 9 . ? 26.448 42.241 40.662 1.00 25.96 ? 2396 HOH A O 1 HETATM 6403 O O . HOH T 9 . ? 31.925 46.435 36.627 1.00 37.00 ? 2397 HOH A O 1 HETATM 6404 O O . HOH T 9 . ? 25.017 42.709 43.142 1.00 28.31 ? 2398 HOH A O 1 HETATM 6405 O O . HOH T 9 . ? 25.679 37.170 38.160 1.00 20.24 ? 2399 HOH A O 1 HETATM 6406 O O . HOH T 9 . ? 28.913 25.981 36.179 1.00 27.22 ? 2400 HOH A O 1 HETATM 6407 O O . HOH T 9 . ? 20.181 31.313 43.561 1.00 21.91 ? 2401 HOH A O 1 HETATM 6408 O O . HOH T 9 . ? 19.262 36.121 43.220 1.00 18.29 ? 2402 HOH A O 1 HETATM 6409 O O . HOH T 9 . ? 26.029 24.917 57.565 1.00 35.27 ? 2403 HOH A O 1 HETATM 6410 O O . HOH T 9 . ? 21.416 24.069 51.247 1.00 35.76 ? 2404 HOH A O 1 HETATM 6411 O O . HOH T 9 . ? 24.763 23.100 53.061 1.00 39.82 ? 2405 HOH A O 1 HETATM 6412 O O . HOH T 9 . ? 32.512 27.516 56.454 1.00 39.56 ? 2406 HOH A O 1 HETATM 6413 O O . HOH T 9 . ? 29.385 27.904 59.428 1.00 42.03 ? 2407 HOH A O 1 HETATM 6414 O O . HOH T 9 . ? 31.060 24.510 54.819 1.00 51.81 ? 2408 HOH A O 1 HETATM 6415 O O . HOH T 9 . ? 35.670 31.853 53.705 1.00 51.60 ? 2409 HOH A O 1 HETATM 6416 O O . HOH T 9 . ? 28.131 24.379 53.280 1.00 55.43 ? 2410 HOH A O 1 HETATM 6417 O O . HOH T 9 . ? 35.935 34.335 51.052 1.00 42.48 ? 2411 HOH A O 1 HETATM 6418 O O . HOH T 9 . ? 31.264 40.099 46.543 1.00 21.26 ? 2412 HOH A O 1 HETATM 6419 O O . HOH T 9 . ? 32.208 35.024 59.316 1.00 25.18 ? 2413 HOH A O 1 HETATM 6420 O O . HOH T 9 . ? 28.589 29.526 61.983 1.00 38.66 ? 2414 HOH A O 1 HETATM 6421 O O . HOH T 9 . ? 29.502 34.383 65.198 1.00 49.80 ? 2415 HOH A O 1 HETATM 6422 O O . HOH T 9 . ? 29.040 40.180 64.959 1.00 27.60 ? 2416 HOH A O 1 HETATM 6423 O O . HOH T 9 . ? 37.550 37.809 60.046 1.00 52.18 ? 2417 HOH A O 1 HETATM 6424 O O . HOH T 9 . ? 37.542 40.925 58.821 1.00 43.35 ? 2418 HOH A O 1 HETATM 6425 O O . HOH T 9 . ? 36.277 37.813 57.143 1.00 54.62 ? 2419 HOH A O 1 HETATM 6426 O O . HOH T 9 . ? 27.842 45.026 69.150 1.00 30.46 ? 2420 HOH A O 1 HETATM 6427 O O . HOH T 9 . ? 28.032 41.644 68.777 1.00 41.84 ? 2421 HOH A O 1 HETATM 6428 O O . HOH T 9 . ? 19.775 58.206 68.554 1.00 45.49 ? 2422 HOH A O 1 HETATM 6429 O O . HOH T 9 . ? 22.461 55.179 70.036 1.00 56.48 ? 2423 HOH A O 1 HETATM 6430 O O . HOH T 9 . ? 17.987 59.488 70.175 1.00 47.77 ? 2424 HOH A O 1 HETATM 6431 O O . HOH T 9 . ? 15.764 54.823 72.409 1.00 48.34 ? 2425 HOH A O 1 HETATM 6432 O O . HOH T 9 . ? 16.924 57.500 73.063 1.00 58.62 ? 2426 HOH A O 1 HETATM 6433 O O . HOH T 9 . ? 10.499 55.425 75.236 1.00 31.91 ? 2427 HOH A O 1 HETATM 6434 O O . HOH T 9 . ? 14.721 58.993 74.587 1.00 28.78 ? 2428 HOH A O 1 HETATM 6435 O O . HOH T 9 . ? 14.905 61.674 73.281 1.00 26.12 ? 2429 HOH A O 1 HETATM 6436 O O . HOH T 9 . ? 16.795 63.212 69.031 1.00 38.98 ? 2430 HOH A O 1 HETATM 6437 O O . HOH T 9 . ? 24.626 67.901 63.264 1.00 40.79 ? 2431 HOH A O 1 HETATM 6438 O O . HOH T 9 . ? 22.824 65.278 66.180 1.00 32.11 ? 2432 HOH A O 1 HETATM 6439 O O . HOH T 9 . ? 16.720 68.130 64.331 1.00 23.82 ? 2433 HOH A O 1 HETATM 6440 O O . HOH T 9 . ? 23.488 74.343 65.612 1.00 36.33 ? 2434 HOH A O 1 HETATM 6441 O O . HOH T 9 . ? 23.829 73.095 59.324 1.00 27.55 ? 2435 HOH A O 1 HETATM 6442 O O . HOH T 9 . ? 25.342 69.180 60.833 1.00 57.92 ? 2436 HOH A O 1 HETATM 6443 O O . HOH T 9 . ? 25.326 66.482 56.818 1.00 30.35 ? 2437 HOH A O 1 HETATM 6444 O O . HOH T 9 . ? 27.059 64.395 60.297 1.00 52.60 ? 2438 HOH A O 1 HETATM 6445 O O . HOH T 9 . ? 21.148 63.435 61.043 1.00 22.66 ? 2439 HOH A O 1 HETATM 6446 O O . HOH T 9 . ? 27.988 71.672 52.637 1.00 32.12 ? 2440 HOH A O 1 HETATM 6447 O O . HOH T 9 . ? 24.446 77.571 53.038 1.00 33.75 ? 2441 HOH A O 1 HETATM 6448 O O . HOH T 9 . ? 29.467 70.071 45.934 1.00 24.30 ? 2442 HOH A O 1 HETATM 6449 O O . HOH T 9 . ? 27.764 66.947 52.968 1.00 36.18 ? 2443 HOH A O 1 HETATM 6450 O O . HOH T 9 . ? 25.221 63.325 50.273 1.00 29.91 ? 2444 HOH A O 1 HETATM 6451 O O . HOH T 9 . ? 30.714 71.584 47.938 1.00 45.41 ? 2445 HOH A O 1 HETATM 6452 O O . HOH T 9 . ? 29.278 72.577 50.114 1.00 37.59 ? 2446 HOH A O 1 HETATM 6453 O O . HOH T 9 . ? 30.303 76.316 49.258 1.00 51.85 ? 2447 HOH A O 1 HETATM 6454 O O . HOH T 9 . ? 29.135 77.436 44.653 1.00 58.71 ? 2448 HOH A O 1 HETATM 6455 O O . HOH T 9 . ? 30.605 71.215 43.764 1.00 32.82 ? 2449 HOH A O 1 HETATM 6456 O O . HOH T 9 . ? 23.058 67.315 40.523 1.00 23.17 ? 2450 HOH A O 1 HETATM 6457 O O . HOH T 9 . ? 32.099 80.444 40.818 1.00 54.38 ? 2451 HOH A O 1 HETATM 6458 O O . HOH T 9 . ? 31.102 69.692 41.608 1.00 33.92 ? 2452 HOH A O 1 HETATM 6459 O O . HOH T 9 . ? 30.254 75.502 43.257 1.00 51.28 ? 2453 HOH A O 1 HETATM 6460 O O . HOH T 9 . ? 31.869 73.549 44.237 1.00 46.61 ? 2454 HOH A O 1 HETATM 6461 O O . HOH T 9 . ? 28.168 70.891 32.684 1.00 43.84 ? 2455 HOH A O 1 HETATM 6462 O O . HOH T 9 . ? 30.784 70.149 37.307 1.00 43.15 ? 2456 HOH A O 1 HETATM 6463 O O . HOH T 9 . ? 32.043 74.559 36.382 1.00 51.59 ? 2457 HOH A O 1 HETATM 6464 O O . HOH T 9 . ? 29.681 86.156 27.164 1.00 49.60 ? 2458 HOH A O 1 HETATM 6465 O O . HOH T 9 . ? 29.184 79.005 27.478 1.00 38.06 ? 2459 HOH A O 1 HETATM 6466 O O . HOH T 9 . ? 23.346 78.395 22.973 1.00 43.78 ? 2460 HOH A O 1 HETATM 6467 O O . HOH T 9 . ? 25.790 75.578 26.020 1.00 59.02 ? 2461 HOH A O 1 HETATM 6468 O O . HOH T 9 . ? 22.202 87.989 32.507 1.00 26.15 ? 2462 HOH A O 1 HETATM 6469 O O . HOH T 9 . ? 30.700 84.092 28.460 1.00 39.45 ? 2463 HOH A O 1 HETATM 6470 O O . HOH T 9 . ? 32.358 84.571 32.422 1.00 53.02 ? 2464 HOH A O 1 HETATM 6471 O O . HOH T 9 . ? 32.555 87.432 30.582 1.00 44.05 ? 2465 HOH A O 1 HETATM 6472 O O . HOH T 9 . ? 24.313 82.174 24.432 1.00 44.67 ? 2466 HOH A O 1 HETATM 6473 O O . HOH T 9 . ? 17.906 86.436 25.695 1.00 59.67 ? 2467 HOH A O 1 HETATM 6474 O O . HOH T 9 . ? 22.048 80.711 22.843 1.00 41.35 ? 2468 HOH A O 1 HETATM 6475 O O . HOH T 9 . ? 18.220 82.687 21.799 1.00 55.42 ? 2469 HOH A O 1 HETATM 6476 O O . HOH T 9 . ? 17.725 87.503 29.793 1.00 52.71 ? 2470 HOH A O 1 HETATM 6477 O O . HOH T 9 . ? 17.728 82.433 41.262 1.00 29.61 ? 2471 HOH A O 1 HETATM 6478 O O . HOH T 9 . ? 20.686 87.078 40.003 1.00 52.12 ? 2472 HOH A O 1 HETATM 6479 O O . HOH T 9 . ? 17.292 81.532 37.428 1.00 25.56 ? 2473 HOH A O 1 HETATM 6480 O O . HOH T 9 . ? 21.881 83.892 47.155 1.00 31.77 ? 2474 HOH A O 1 HETATM 6481 O O . HOH T 9 . ? 21.397 88.452 44.164 1.00 34.84 ? 2475 HOH A O 1 HETATM 6482 O O . HOH T 9 . ? 25.328 85.746 42.688 1.00 30.11 ? 2476 HOH A O 1 HETATM 6483 O O . HOH T 9 . ? 24.207 82.142 42.423 1.00 35.33 ? 2477 HOH A O 1 HETATM 6484 O O . HOH T 9 . ? 24.317 83.357 45.889 1.00 45.77 ? 2478 HOH A O 1 HETATM 6485 O O . HOH T 9 . ? 14.352 81.193 40.889 1.00 34.49 ? 2479 HOH A O 1 HETATM 6486 O O . HOH T 9 . ? 23.544 78.872 50.576 1.00 29.29 ? 2480 HOH A O 1 HETATM 6487 O O . HOH T 9 . ? 18.749 84.648 52.058 1.00 50.76 ? 2481 HOH A O 1 HETATM 6488 O O . HOH T 9 . ? 22.675 80.320 57.216 1.00 50.45 ? 2482 HOH A O 1 HETATM 6489 O O . HOH T 9 . ? 18.177 85.306 54.483 1.00 50.54 ? 2483 HOH A O 1 HETATM 6490 O O . HOH T 9 . ? 24.122 74.942 54.554 1.00 23.68 ? 2484 HOH A O 1 HETATM 6491 O O . HOH T 9 . ? 21.927 74.369 60.630 1.00 27.69 ? 2485 HOH A O 1 HETATM 6492 O O . HOH T 9 . ? 15.854 82.546 57.730 1.00 50.66 ? 2486 HOH A O 1 HETATM 6493 O O . HOH T 9 . ? 13.436 77.738 63.613 1.00 27.18 ? 2487 HOH A O 1 HETATM 6494 O O . HOH T 9 . ? 21.598 75.095 67.005 1.00 36.76 ? 2488 HOH A O 1 HETATM 6495 O O . HOH T 9 . ? 20.980 79.427 65.643 1.00 49.55 ? 2489 HOH A O 1 HETATM 6496 O O . HOH T 9 . ? 18.875 68.963 65.841 1.00 30.68 ? 2490 HOH A O 1 HETATM 6497 O O . HOH T 9 . ? 21.441 73.305 68.953 1.00 52.95 ? 2491 HOH A O 1 HETATM 6498 O O . HOH T 9 . ? 16.184 79.335 69.280 1.00 41.21 ? 2492 HOH A O 1 HETATM 6499 O O . HOH T 9 . ? 13.857 79.755 68.027 1.00 32.38 ? 2493 HOH A O 1 HETATM 6500 O O . HOH T 9 . ? 9.427 74.915 69.570 1.00 48.24 ? 2494 HOH A O 1 HETATM 6501 O O . HOH T 9 . ? 16.041 67.390 72.721 1.00 40.29 ? 2495 HOH A O 1 HETATM 6502 O O . HOH T 9 . ? 14.082 68.748 75.411 1.00 37.57 ? 2496 HOH A O 1 HETATM 6503 O O . HOH T 9 . ? 14.714 73.006 78.859 1.00 52.47 ? 2497 HOH A O 1 HETATM 6504 O O . HOH T 9 . ? 15.693 78.554 71.922 1.00 51.45 ? 2498 HOH A O 1 HETATM 6505 O O . HOH T 9 . ? 8.619 74.818 75.569 1.00 38.62 ? 2499 HOH A O 1 HETATM 6506 O O . HOH T 9 . ? 8.970 73.253 78.611 1.00 38.32 ? 2500 HOH A O 1 HETATM 6507 O O . HOH T 9 . ? 7.649 73.334 80.619 1.00 32.05 ? 2501 HOH A O 1 HETATM 6508 O O . HOH T 9 . ? 4.098 70.721 80.964 1.00 39.04 ? 2502 HOH A O 1 HETATM 6509 O O . HOH T 9 . ? 4.254 63.478 72.751 1.00 26.41 ? 2503 HOH A O 1 HETATM 6510 O O . HOH T 9 . ? 4.014 70.400 64.431 1.00 18.46 ? 2504 HOH A O 1 HETATM 6511 O O . HOH T 9 . ? 0.597 66.161 62.886 1.00 41.42 ? 2505 HOH A O 1 HETATM 6512 O O . HOH T 9 . ? 5.628 62.685 65.084 1.00 23.48 ? 2506 HOH A O 1 HETATM 6513 O O . HOH T 9 . ? 0.290 65.467 66.066 1.00 29.62 ? 2507 HOH A O 1 HETATM 6514 O O . HOH T 9 . ? 7.961 69.488 59.171 1.00 15.46 ? 2508 HOH A O 1 HETATM 6515 O O . HOH T 9 . ? 8.782 74.582 66.733 1.00 23.18 ? 2509 HOH A O 1 HETATM 6516 O O . HOH T 9 . ? 11.144 63.355 58.271 1.00 22.36 ? 2510 HOH A O 1 HETATM 6517 O O . HOH T 9 . ? 5.797 68.903 55.439 1.00 17.32 ? 2511 HOH A O 1 HETATM 6518 O O . HOH T 9 . ? 4.405 67.004 51.535 1.00 17.25 ? 2512 HOH A O 1 HETATM 6519 O O . HOH T 9 . ? 3.980 68.546 49.313 1.00 17.85 ? 2513 HOH A O 1 HETATM 6520 O O . HOH T 9 . ? 8.963 68.995 40.965 1.00 20.67 ? 2514 HOH A O 1 HETATM 6521 O O . HOH T 9 . ? 3.535 71.890 43.577 1.00 17.96 ? 2515 HOH A O 1 HETATM 6522 O O . HOH T 9 . ? 1.112 63.265 43.024 1.00 28.36 ? 2516 HOH A O 1 HETATM 6523 O O . HOH T 9 . ? 1.885 66.506 37.217 1.00 44.61 ? 2517 HOH A O 1 HETATM 6524 O O . HOH T 9 . ? 5.130 64.615 37.021 1.00 18.02 ? 2518 HOH A O 1 HETATM 6525 O O . HOH T 9 . ? 6.052 68.330 37.158 1.00 29.79 ? 2519 HOH A O 1 HETATM 6526 O O . HOH T 9 . ? 12.022 63.643 35.517 1.00 27.01 ? 2520 HOH A O 1 HETATM 6527 O O . HOH T 9 . ? 5.350 66.020 33.747 1.00 36.12 ? 2521 HOH A O 1 HETATM 6528 O O . HOH T 9 . ? 9.384 59.400 31.520 1.00 50.60 ? 2522 HOH A O 1 HETATM 6529 O O . HOH T 9 . ? 16.885 61.952 38.318 1.00 16.62 ? 2523 HOH A O 1 HETATM 6530 O O . HOH T 9 . ? 2.506 63.178 40.688 1.00 32.18 ? 2524 HOH A O 1 HETATM 6531 O O . HOH T 9 . ? 9.005 56.555 43.872 1.00 15.01 ? 2525 HOH A O 1 HETATM 6532 O O . HOH T 9 . ? 14.153 54.704 37.472 1.00 31.57 ? 2526 HOH A O 1 HETATM 6533 O O . HOH T 9 . ? -0.657 58.215 43.448 1.00 20.68 ? 2527 HOH A O 1 HETATM 6534 O O . HOH T 9 . ? 0.277 65.244 47.212 0.50 36.95 ? 2528 HOH A O 1 HETATM 6535 O O . HOH T 9 . ? 0.394 63.073 48.171 1.00 33.27 ? 2529 HOH A O 1 HETATM 6536 O O . HOH T 9 . ? 12.019 61.944 43.519 1.00 15.04 ? 2530 HOH A O 1 HETATM 6537 O O . HOH T 9 . ? 16.135 55.578 35.551 1.00 17.97 ? 2531 HOH A O 1 HETATM 6538 O O . HOH T 9 . ? 17.865 58.210 29.911 1.00 33.44 ? 2532 HOH A O 1 HETATM 6539 O O . HOH T 9 . ? 17.653 61.073 30.610 1.00 47.22 ? 2533 HOH A O 1 HETATM 6540 O O . HOH T 9 . ? 13.863 61.634 33.022 1.00 37.06 ? 2534 HOH A O 1 HETATM 6541 O O . HOH T 9 . ? 23.140 55.201 31.171 1.00 23.24 ? 2535 HOH A O 1 HETATM 6542 O O . HOH T 9 . ? 25.396 56.053 37.228 1.00 24.61 ? 2536 HOH A O 1 HETATM 6543 O O . HOH T 9 . ? 12.004 50.033 36.428 1.00 16.17 ? 2537 HOH A O 1 HETATM 6544 O O . HOH T 9 . ? 20.563 45.697 36.486 1.00 17.14 ? 2538 HOH A O 1 HETATM 6545 O O . HOH T 9 . ? 22.092 52.444 45.146 1.00 32.73 ? 2539 HOH A O 1 HETATM 6546 O O . HOH T 9 . ? 21.770 61.555 36.753 1.00 21.19 ? 2540 HOH A O 1 HETATM 6547 O O . HOH T 9 . ? 25.654 63.155 38.862 1.00 32.22 ? 2541 HOH A O 1 HETATM 6548 O O . HOH T 9 . ? 24.987 64.663 44.474 1.00 30.54 ? 2542 HOH A O 1 HETATM 6549 O O . HOH T 9 . ? 23.091 68.628 42.995 1.00 22.32 ? 2543 HOH A O 1 HETATM 6550 O O . HOH T 9 . ? 15.197 68.962 41.585 1.00 23.38 ? 2544 HOH A O 1 HETATM 6551 O O . HOH T 9 . ? 13.925 67.865 34.769 1.00 20.20 ? 2545 HOH A O 1 HETATM 6552 O O . HOH T 9 . ? 23.291 67.689 34.313 1.00 20.39 ? 2546 HOH A O 1 HETATM 6553 O O . HOH T 9 . ? 23.926 61.321 34.685 1.00 27.63 ? 2547 HOH A O 1 HETATM 6554 O O . HOH T 9 . ? 26.942 64.913 34.784 1.00 42.18 ? 2548 HOH A O 1 HETATM 6555 O O . HOH T 9 . ? 19.229 63.575 32.127 1.00 25.64 ? 2549 HOH A O 1 HETATM 6556 O O . HOH T 9 . ? 19.041 62.112 36.471 1.00 17.22 ? 2550 HOH A O 1 HETATM 6557 O O . HOH T 9 . ? 17.696 65.237 30.422 1.00 29.63 ? 2551 HOH A O 1 HETATM 6558 O O . HOH T 9 . ? 13.956 65.170 36.088 1.00 29.36 ? 2552 HOH A O 1 HETATM 6559 O O . HOH T 9 . ? 25.292 70.448 31.233 1.00 23.36 ? 2553 HOH A O 1 HETATM 6560 O O . HOH T 9 . ? 18.812 65.947 27.882 1.00 32.28 ? 2554 HOH A O 1 HETATM 6561 O O . HOH T 9 . ? 25.685 66.942 30.162 1.00 25.64 ? 2555 HOH A O 1 HETATM 6562 O O . HOH T 9 . ? 26.572 66.158 26.338 1.00 33.51 ? 2556 HOH A O 1 HETATM 6563 O O . HOH T 9 . ? 20.163 64.246 25.609 1.00 38.96 ? 2557 HOH A O 1 HETATM 6564 O O . HOH T 9 . ? 20.901 74.351 23.765 1.00 32.32 ? 2558 HOH A O 1 HETATM 6565 O O . HOH T 9 . ? 25.523 74.631 22.150 1.00 46.30 ? 2559 HOH A O 1 HETATM 6566 O O . HOH T 9 . ? 26.627 69.172 29.087 1.00 31.34 ? 2560 HOH A O 1 HETATM 6567 O O . HOH T 9 . ? 19.089 69.575 28.442 1.00 27.86 ? 2561 HOH A O 1 HETATM 6568 O O . HOH T 9 . ? 16.050 67.898 29.382 1.00 37.66 ? 2562 HOH A O 1 HETATM 6569 O O . HOH T 9 . ? 16.844 69.091 20.867 1.00 43.77 ? 2563 HOH A O 1 HETATM 6570 O O . HOH T 9 . ? 16.670 79.482 21.242 1.00 39.79 ? 2564 HOH A O 1 HETATM 6571 O O . HOH T 9 . ? 15.308 71.859 21.853 1.00 43.55 ? 2565 HOH A O 1 HETATM 6572 O O . HOH T 9 . ? 14.992 73.065 24.057 1.00 44.56 ? 2566 HOH A O 1 HETATM 6573 O O . HOH T 9 . ? 11.650 74.395 20.047 1.00 53.11 ? 2567 HOH A O 1 HETATM 6574 O O . HOH T 9 . ? 11.220 76.571 28.591 1.00 29.19 ? 2568 HOH A O 1 HETATM 6575 O O . HOH T 9 . ? 16.306 72.045 29.739 1.00 21.18 ? 2569 HOH A O 1 HETATM 6576 O O . HOH T 9 . ? 23.066 75.651 25.709 1.00 35.79 ? 2570 HOH A O 1 HETATM 6577 O O . HOH T 9 . ? 12.874 69.340 32.676 1.00 28.83 ? 2571 HOH A O 1 HETATM 6578 O O . HOH T 9 . ? 9.937 75.805 30.941 1.00 36.83 ? 2572 HOH A O 1 HETATM 6579 O O . HOH T 9 . ? 14.808 80.707 38.226 1.00 22.51 ? 2573 HOH A O 1 HETATM 6580 O O . HOH T 9 . ? 15.083 81.524 28.503 1.00 41.49 ? 2574 HOH A O 1 HETATM 6581 O O . HOH T 9 . ? 7.008 75.734 37.715 1.00 25.63 ? 2575 HOH A O 1 HETATM 6582 O O . HOH T 9 . ? 8.285 69.777 36.836 1.00 40.03 ? 2576 HOH A O 1 HETATM 6583 O O . HOH T 9 . ? 13.753 71.312 40.499 1.00 18.80 ? 2577 HOH A O 1 HETATM 6584 O O . HOH T 9 . ? 9.909 69.821 38.587 1.00 22.70 ? 2578 HOH A O 1 HETATM 6585 O O . HOH T 9 . ? 5.533 78.968 38.650 1.00 36.46 ? 2579 HOH A O 1 HETATM 6586 O O . HOH T 9 . ? 9.045 78.647 49.677 1.00 38.35 ? 2580 HOH A O 1 HETATM 6587 O O . HOH T 9 . ? 7.437 71.759 45.262 1.00 17.54 ? 2581 HOH A O 1 HETATM 6588 O O . HOH T 9 . ? 5.998 75.339 54.222 1.00 20.15 ? 2582 HOH A O 1 HETATM 6589 O O . HOH T 9 . ? 5.513 77.994 54.591 1.00 21.20 ? 2583 HOH A O 1 HETATM 6590 O O . HOH T 9 . ? 7.076 78.462 51.535 1.00 17.83 ? 2584 HOH A O 1 HETATM 6591 O O . HOH T 9 . ? 10.409 82.582 56.351 1.00 47.49 ? 2585 HOH A O 1 HETATM 6592 O O . HOH T 9 . ? 5.618 81.658 54.069 1.00 34.49 ? 2586 HOH A O 1 HETATM 6593 O O . HOH T 9 . ? 11.680 81.057 61.217 1.00 35.35 ? 2587 HOH A O 1 HETATM 6594 O O . HOH T 9 . ? 9.546 81.247 58.581 1.00 47.84 ? 2588 HOH A O 1 HETATM 6595 O O . HOH T 9 . ? 10.203 80.937 63.665 1.00 29.39 ? 2589 HOH A O 1 HETATM 6596 O O . HOH T 9 . ? 7.194 81.539 62.898 1.00 54.74 ? 2590 HOH A O 1 HETATM 6597 O O . HOH T 9 . ? 12.311 80.963 69.935 1.00 48.45 ? 2591 HOH A O 1 HETATM 6598 O O . HOH T 9 . ? 11.168 82.030 65.859 1.00 43.95 ? 2592 HOH A O 1 HETATM 6599 O O . HOH T 9 . ? 6.575 76.291 67.376 1.00 28.30 ? 2593 HOH A O 1 HETATM 6600 O O . HOH T 9 . ? 15.154 24.523 58.486 1.00 33.35 ? 2594 HOH A O 1 HETATM 6601 O O . HOH T 9 . ? 6.372 24.327 56.547 1.00 47.53 ? 2595 HOH A O 1 HETATM 6602 O O . HOH T 9 . ? 10.057 24.227 54.101 1.00 45.66 ? 2596 HOH A O 1 HETATM 6603 O O . HOH T 9 . ? 19.692 22.194 12.652 1.00 48.68 ? 2597 HOH A O 1 HETATM 6604 O O . HOH T 9 . ? 38.093 39.845 48.675 1.00 53.64 ? 2598 HOH A O 1 HETATM 6605 O O . HOH T 9 . ? 37.829 41.564 53.105 1.00 46.37 ? 2599 HOH A O 1 HETATM 6606 O O . HOH T 9 . ? 20.600 65.340 67.491 1.00 53.95 ? 2600 HOH A O 1 HETATM 6607 O O . HOH T 9 . ? 20.456 63.193 71.976 1.00 54.58 ? 2601 HOH A O 1 HETATM 6608 O O . HOH T 9 . ? 27.714 65.976 73.904 1.00 48.52 ? 2602 HOH A O 1 HETATM 6609 O O . HOH T 9 . ? 13.548 82.662 55.769 1.00 29.39 ? 2603 HOH A O 1 HETATM 6610 O O . HOH T 9 . ? 10.566 84.034 51.274 1.00 40.70 ? 2604 HOH A O 1 HETATM 6611 O O . HOH T 9 . ? 13.342 93.711 40.514 1.00 42.74 ? 2605 HOH A O 1 HETATM 6612 O O . HOH T 9 . ? 14.663 96.456 45.523 1.00 47.24 ? 2606 HOH A O 1 HETATM 6613 O O . HOH T 9 . ? 12.870 23.520 15.754 1.00 59.22 ? 2607 HOH A O 1 HETATM 6614 O O . HOH T 9 . ? 15.105 41.766 38.716 1.00 16.55 ? 2608 HOH A O 1 HETATM 6615 O O . HOH T 9 . ? 11.683 47.599 37.445 1.00 17.37 ? 2609 HOH A O 1 HETATM 6616 O O . HOH T 9 . ? 25.368 43.711 38.504 1.00 28.28 ? 2610 HOH A O 1 HETATM 6617 O O . HOH T 9 . ? 21.351 42.185 46.277 1.00 27.89 ? 2611 HOH A O 1 HETATM 6618 O O . HOH T 9 . ? 34.784 49.975 50.459 1.00 53.40 ? 2612 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . LYS A 14 ? 0.7757 0.6376 0.5354 0.1978 -0.0411 0.0018 55 LYS A N 2 C CA . LYS A 14 ? 0.7551 0.6228 0.5227 0.1916 -0.0430 -0.0011 55 LYS A CA 3 C C . LYS A 14 ? 0.7217 0.5982 0.5059 0.1810 -0.0382 -0.0002 55 LYS A C 4 O O . LYS A 14 ? 0.7099 0.5902 0.5036 0.1771 -0.0386 -0.0011 55 LYS A O 5 C CB . LYS A 14 ? 0.7695 0.6384 0.5387 0.1924 -0.0534 -0.0081 55 LYS A CB 6 C CG . LYS A 14 ? 0.8063 0.6741 0.5704 0.1936 -0.0556 -0.0098 55 LYS A CG 7 C CD . LYS A 14 ? 0.8410 0.7167 0.6177 0.1839 -0.0521 -0.0096 55 LYS A CD 8 C CE . LYS A 14 ? 0.8600 0.7354 0.6338 0.1845 -0.0561 -0.0126 55 LYS A CE 9 N NZ . LYS A 14 ? 0.8782 0.7615 0.6650 0.1750 -0.0531 -0.0126 55 LYS A NZ 10 N N . HIS A 15 ? 0.6921 0.5715 0.4792 0.1766 -0.0337 0.0017 56 HIS A N 11 C CA . HIS A 15 ? 0.6542 0.5419 0.4563 0.1667 -0.0297 0.0021 56 HIS A CA 12 C C . HIS A 15 ? 0.6234 0.5164 0.4331 0.1619 -0.0358 -0.0031 56 HIS A C 13 O O . HIS A 15 ? 0.6448 0.5375 0.4513 0.1619 -0.0360 -0.0034 56 HIS A O 14 C CB . HIS A 15 ? 0.6583 0.5458 0.4591 0.1650 -0.0211 0.0074 56 HIS A CB 15 C CG . HIS A 15 ? 0.6741 0.5572 0.4698 0.1685 -0.0138 0.0132 56 HIS A CG 16 N ND1 . HIS A 15 ? 0.6820 0.5661 0.4832 0.1671 -0.0124 0.0140 56 HIS A ND1 17 C CD2 . HIS A 15 ? 0.6709 0.5488 0.4575 0.1730 -0.0071 0.0185 56 HIS A CD2 18 C CE1 . HIS A 15 ? 0.6883 0.5678 0.4839 0.1707 -0.0053 0.0196 56 HIS A CE1 19 N NE2 . HIS A 15 ? 0.7078 0.5836 0.4948 0.1742 -0.0018 0.0225 56 HIS A NE2 20 N N . ASN A 16 ? 0.5674 0.4648 0.3870 0.1581 -0.0409 -0.0073 57 ASN A N 21 C CA . ASN A 16 ? 0.5208 0.4233 0.3487 0.1535 -0.0467 -0.0123 57 ASN A CA 22 C C . ASN A 16 ? 0.4698 0.3796 0.3127 0.1456 -0.0462 -0.0138 57 ASN A C 23 O O . ASN A 16 ? 0.4514 0.3622 0.2975 0.1438 -0.0411 -0.0108 57 ASN A O 24 C CB . ASN A 16 ? 0.5225 0.4212 0.3445 0.1595 -0.0558 -0.0172 57 ASN A CB 25 C CG . ASN A 16 ? 0.5506 0.4457 0.3692 0.1647 -0.0590 -0.0180 57 ASN A CG 26 O OD1 . ASN A 16 ? 0.6047 0.4946 0.4146 0.1718 -0.0655 -0.0208 57 ASN A OD1 27 N ND2 . ASN A 16 ? 0.4906 0.3881 0.3155 0.1616 -0.0548 -0.0158 57 ASN A ND2 28 N N . MET A 17 ? 0.4514 0.3662 0.3038 0.1410 -0.0512 -0.0183 58 MET A N 29 C CA A MET A 17 ? 0.4400 0.3620 0.3069 0.1332 -0.0502 -0.0196 58 MET A CA 30 C CA B MET A 17 ? 0.4344 0.3561 0.3006 0.1334 -0.0495 -0.0191 58 MET A CA 31 C C . MET A 17 ? 0.4355 0.3566 0.3041 0.1353 -0.0514 -0.0201 58 MET A C 32 O O . MET A 17 ? 0.4290 0.3537 0.3053 0.1307 -0.0473 -0.0186 58 MET A O 33 C CB A MET A 17 ? 0.4342 0.3613 0.3108 0.1285 -0.0556 -0.0245 58 MET A CB 34 C CB B MET A 17 ? 0.4237 0.3514 0.3007 0.1272 -0.0531 -0.0231 58 MET A CB 35 C CG A MET A 17 ? 0.4555 0.3902 0.3469 0.1201 -0.0536 -0.0254 58 MET A CG 36 C CG B MET A 17 ? 0.4094 0.3438 0.2987 0.1191 -0.0485 -0.0221 58 MET A CG 37 S SD A MET A 17 ? 0.5133 0.4543 0.4162 0.1133 -0.0570 -0.0294 58 MET A SD 38 S SD B MET A 17 ? 0.3788 0.3198 0.2818 0.1131 -0.0536 -0.0273 58 MET A SD 39 C CE A MET A 17 ? 0.5239 0.4624 0.4264 0.1184 -0.0670 -0.0350 58 MET A CE 40 C CE B MET A 17 ? 0.3618 0.3038 0.2637 0.1109 -0.0541 -0.0277 58 MET A CE 41 N N . LYS A 18 ? 0.4417 0.3579 0.3032 0.1422 -0.0576 -0.0226 59 LYS A N 42 C CA . LYS A 18 ? 0.4484 0.3636 0.3116 0.1446 -0.0597 -0.0235 59 LYS A CA 43 C C . LYS A 18 ? 0.4408 0.3535 0.2998 0.1459 -0.0524 -0.0182 59 LYS A C 44 O O . LYS A 18 ? 0.4453 0.3603 0.3112 0.1435 -0.0509 -0.0180 59 LYS A O 45 C CB . LYS A 18 ? 0.4627 0.3718 0.3166 0.1531 -0.0675 -0.0266 59 LYS A CB 46 C CG . LYS A 18 ? 0.4945 0.4027 0.3507 0.1559 -0.0709 -0.0283 59 LYS A CG 47 C CD . LYS A 18 ? 0.5778 0.4788 0.4225 0.1654 -0.0785 -0.0309 59 LYS A CD 48 C CE . LYS A 18 ? 0.6423 0.5425 0.4900 0.1684 -0.0837 -0.0337 59 LYS A CE 49 N NZ . LYS A 18 ? 0.6771 0.5811 0.5337 0.1639 -0.0787 -0.0315 59 LYS A NZ 50 N N . ALA A 19 ? 0.4452 0.3529 0.2932 0.1498 -0.0478 -0.0139 60 ALA A N 51 C CA . ALA A 19 ? 0.4614 0.3663 0.3054 0.1513 -0.0404 -0.0085 60 ALA A CA 52 C C . ALA A 19 ? 0.4396 0.3513 0.2962 0.1425 -0.0345 -0.0068 60 ALA A C 53 O O . ALA A 19 ? 0.4501 0.3624 0.3106 0.1412 -0.0310 -0.0049 60 ALA A O 54 C CB . ALA A 19 ? 0.4777 0.3767 0.3089 0.1565 -0.0362 -0.0043 60 ALA A CB 55 N N . PHE A 20 ? 0.4163 0.3327 0.2786 0.1368 -0.0335 -0.0077 61 PHE A N 56 C CA . PHE A 20 ? 0.4040 0.3268 0.2780 0.1286 -0.0286 -0.0066 61 PHE A CA 57 C C . PHE A 20 ? 0.3721 0.2997 0.2573 0.1244 -0.0312 -0.0098 61 PHE A C 58 O O . PHE A 20 ? 0.3761 0.3057 0.2671 0.1213 -0.0269 -0.0080 61 PHE A O 59 C CB . PHE A 20 ? 0.3741 0.3009 0.2519 0.1235 -0.0279 -0.0073 61 PHE A CB 60 C CG . PHE A 20 ? 0.3646 0.2987 0.2554 0.1148 -0.0250 -0.0078 61 PHE A CG 61 C CD1 . PHE A 20 ? 0.3703 0.3056 0.2641 0.1117 -0.0180 -0.0039 61 PHE A CD1 62 C CD2 . PHE A 20 ? 0.3482 0.2874 0.2482 0.1103 -0.0294 -0.0121 61 PHE A CD2 63 C CE1 . PHE A 20 ? 0.3443 0.2859 0.2497 0.1041 -0.0157 -0.0047 61 PHE A CE1 64 C CE2 . PHE A 20 ? 0.3082 0.2537 0.2194 0.1027 -0.0267 -0.0126 61 PHE A CE2 65 C CZ . PHE A 20 ? 0.3371 0.2837 0.2506 0.0998 -0.0201 -0.0090 61 PHE A CZ 66 N N . LEU A 21 ? 0.3777 0.3070 0.2661 0.1245 -0.0382 -0.0146 62 LEU A N 67 C CA . LEU A 21 ? 0.3709 0.3049 0.2705 0.1206 -0.0408 -0.0178 62 LEU A CA 68 C C . LEU A 21 ? 0.3877 0.3188 0.2857 0.1243 -0.0405 -0.0169 62 LEU A C 69 O O . LEU A 21 ? 0.3874 0.3224 0.2944 0.1202 -0.0386 -0.0172 62 LEU A O 70 C CB . LEU A 21 ? 0.3785 0.3144 0.2821 0.1206 -0.0485 -0.0231 62 LEU A CB 71 C CG . LEU A 21 ? 0.3701 0.3096 0.2774 0.1161 -0.0490 -0.0245 62 LEU A CG 72 C CD1 . LEU A 21 ? 0.4132 0.3530 0.3226 0.1177 -0.0570 -0.0294 62 LEU A CD1 73 C CD2 . LEU A 21 ? 0.3625 0.3091 0.2819 0.1075 -0.0448 -0.0242 62 LEU A CD2 74 N N . ASP A 22 ? 0.4024 0.3266 0.2887 0.1323 -0.0423 -0.0157 63 ASP A N 75 C CA . ASP A 22 ? 0.4304 0.3513 0.3145 0.1365 -0.0429 -0.0150 63 ASP A CA 76 C C . ASP A 22 ? 0.4195 0.3399 0.3043 0.1349 -0.0350 -0.0102 63 ASP A C 77 O O . ASP A 22 ? 0.4368 0.3566 0.3242 0.1358 -0.0345 -0.0098 63 ASP A O 78 C CB . ASP A 22 ? 0.4533 0.3662 0.3230 0.1461 -0.0467 -0.0147 63 ASP A CB 79 C CG . ASP A 22 ? 0.4971 0.4097 0.3669 0.1490 -0.0560 -0.0202 63 ASP A CG 80 O OD1 . ASP A 22 ? 0.5027 0.4212 0.3844 0.1440 -0.0596 -0.0243 63 ASP A OD1 81 O OD2 . ASP A 22 ? 0.5276 0.4336 0.3851 0.1568 -0.0597 -0.0204 63 ASP A OD2 82 N N . GLU A 23 ? 0.4112 0.3315 0.2938 0.1328 -0.0290 -0.0065 64 GLU A N 83 C CA . GLU A 23 ? 0.4140 0.3339 0.2979 0.1312 -0.0214 -0.0019 64 GLU A CA 84 C C . GLU A 23 ? 0.3960 0.3227 0.2938 0.1232 -0.0191 -0.0031 64 GLU A C 85 O O . GLU A 23 ? 0.4093 0.3356 0.3099 0.1223 -0.0146 -0.0005 64 GLU A O 86 C CB . GLU A 23 ? 0.4218 0.3394 0.2997 0.1317 -0.0159 0.0023 64 GLU A CB 87 C CG . GLU A 23 ? 0.4485 0.3656 0.3287 0.1297 -0.0078 0.0072 64 GLU A CG 88 C CD . GLU A 23 ? 0.4995 0.4105 0.3734 0.1358 -0.0058 0.0103 64 GLU A CD 89 O OE1 . GLU A 23 ? 0.5382 0.4430 0.4005 0.1434 -0.0087 0.0107 64 GLU A OE1 90 O OE2 . GLU A 23 ? 0.4819 0.3941 0.3621 0.1332 -0.0015 0.0122 64 GLU A OE2 91 N N . LEU A 24 ? 0.3783 0.3111 0.2845 0.1177 -0.0223 -0.0070 65 LEU A N 92 C CA . LEU A 24 ? 0.3608 0.3001 0.2798 0.1103 -0.0206 -0.0086 65 LEU A CA 93 C C . LEU A 24 ? 0.3726 0.3121 0.2960 0.1114 -0.0226 -0.0102 65 LEU A C 94 O O . LEU A 24 ? 0.3864 0.3242 0.3077 0.1154 -0.0285 -0.0130 65 LEU A O 95 C CB . LEU A 24 ? 0.3439 0.2889 0.2700 0.1053 -0.0242 -0.0126 65 LEU A CB 96 C CG . LEU A 24 ? 0.3465 0.2922 0.2697 0.1036 -0.0232 -0.0118 65 LEU A CG 97 C CD1 . LEU A 24 ? 0.3396 0.2895 0.2683 0.1005 -0.0283 -0.0161 65 LEU A CD1 98 C CD2 . LEU A 24 ? 0.3272 0.2756 0.2545 0.0983 -0.0164 -0.0087 65 LEU A CD2 99 N N . LYS A 25 ? 0.3555 0.2975 0.2860 0.1075 -0.0181 -0.0089 66 LYS A N 100 C CA . LYS A 25 ? 0.3619 0.3039 0.2967 0.1085 -0.0193 -0.0101 66 LYS A CA 101 C C . LYS A 25 ? 0.3390 0.2876 0.2864 0.1012 -0.0178 -0.0122 66 LYS A C 102 O O . LYS A 25 ? 0.3372 0.2881 0.2884 0.0966 -0.0126 -0.0103 66 LYS A O 103 C CB . LYS A 25 ? 0.3716 0.3081 0.3006 0.1126 -0.0148 -0.0056 66 LYS A CB 104 C CG . LYS A 25 ? 0.4264 0.3553 0.3415 0.1207 -0.0156 -0.0029 66 LYS A CG 105 C CD . LYS A 25 ? 0.5243 0.4511 0.4354 0.1260 -0.0232 -0.0064 66 LYS A CD 106 C CE . LYS A 25 ? 0.5577 0.4761 0.4545 0.1349 -0.0243 -0.0039 66 LYS A CE 107 N NZ . LYS A 25 ? 0.5431 0.4593 0.4316 0.1369 -0.0245 -0.0030 66 LYS A NZ 108 N N . ALA A 26 ? 0.3306 0.2820 0.2844 0.1006 -0.0221 -0.0160 67 ALA A N 109 C CA . ALA A 26 ? 0.3286 0.2856 0.2937 0.0946 -0.0205 -0.0180 67 ALA A CA 110 C C . ALA A 26 ? 0.3280 0.2842 0.2951 0.0933 -0.0149 -0.0151 67 ALA A C 111 O O . ALA A 26 ? 0.3146 0.2751 0.2890 0.0875 -0.0114 -0.0153 67 ALA A O 112 C CB . ALA A 26 ? 0.3059 0.2648 0.2768 0.0955 -0.0258 -0.0221 67 ALA A CB 113 N N . GLU A 27 ? 0.3379 0.2887 0.2989 0.0988 -0.0141 -0.0125 68 GLU A N 114 C CA . GLU A 27 ? 0.3608 0.3106 0.3246 0.0977 -0.0088 -0.0099 68 GLU A CA 115 C C . GLU A 27 ? 0.3494 0.2994 0.3129 0.0944 -0.0028 -0.0065 68 GLU A C 116 O O . GLU A 27 ? 0.3371 0.2892 0.3071 0.0905 0.0014 -0.0057 68 GLU A O 117 C CB . GLU A 27 ? 0.3792 0.3225 0.3357 0.1047 -0.0090 -0.0074 68 GLU A CB 118 C CG . GLU A 27 ? 0.4694 0.4110 0.4285 0.1040 -0.0033 -0.0042 68 GLU A CG 119 C CD . GLU A 27 ? 0.5958 0.5423 0.5663 0.0991 -0.0029 -0.0069 68 GLU A CD 120 O OE1 . GLU A 27 ? 0.6439 0.5928 0.6201 0.0942 0.0019 -0.0058 68 GLU A OE1 121 O OE2 . GLU A 27 ? 0.5877 0.5358 0.5615 0.1000 -0.0075 -0.0104 68 GLU A OE2 122 N N . ASN A 28 ? 0.3350 0.2831 0.2915 0.0960 -0.0026 -0.0048 69 ASN A N 123 C CA . ASN A 28 ? 0.3260 0.2746 0.2825 0.0929 0.0028 -0.0017 69 ASN A CA 124 C C . ASN A 28 ? 0.3069 0.2622 0.2724 0.0856 0.0032 -0.0044 69 ASN A C 125 O O . ASN A 28 ? 0.3013 0.2584 0.2718 0.0815 0.0076 -0.0031 69 ASN A O 126 C CB . ASN A 28 ? 0.3410 0.2859 0.2878 0.0966 0.0027 0.0005 69 ASN A CB 127 C CG . ASN A 28 ? 0.3637 0.3014 0.3012 0.1037 0.0043 0.0043 69 ASN A CG 128 O OD1 . ASN A 28 ? 0.3772 0.3127 0.3163 0.1048 0.0075 0.0065 69 ASN A OD1 129 N ND2 . ASN A 28 ? 0.3689 0.3027 0.2965 0.1088 0.0021 0.0051 69 ASN A ND2 130 N N . ILE A 29 ? 0.2973 0.2560 0.2649 0.0840 -0.0014 -0.0081 70 ILE A N 131 C CA . ILE A 29 ? 0.2936 0.2584 0.2691 0.0773 -0.0010 -0.0106 70 ILE A CA 132 C C . ILE A 29 ? 0.2939 0.2616 0.2780 0.0737 0.0011 -0.0118 70 ILE A C 133 O O . ILE A 29 ? 0.2869 0.2578 0.2762 0.0687 0.0044 -0.0118 70 ILE A O 134 C CB . ILE A 29 ? 0.2841 0.2516 0.2608 0.0767 -0.0063 -0.0144 70 ILE A CB 135 C CG1 . ILE A 29 ? 0.3074 0.2718 0.2753 0.0803 -0.0085 -0.0133 70 ILE A CG1 136 C CG2 . ILE A 29 ? 0.2839 0.2576 0.2686 0.0699 -0.0056 -0.0167 70 ILE A CG2 137 C CD1 . ILE A 29 ? 0.3270 0.2930 0.2955 0.0809 -0.0144 -0.0169 70 ILE A CD1 138 N N . LYS A 30 ? 0.2936 0.2601 0.2792 0.0764 -0.0009 -0.0130 71 LYS A N 139 C CA . LYS A 30 ? 0.2910 0.2596 0.2841 0.0738 0.0012 -0.0140 71 LYS A CA 140 C C . LYS A 30 ? 0.3021 0.2690 0.2959 0.0726 0.0067 -0.0107 71 LYS A C 141 O O . LYS A 30 ? 0.3062 0.2765 0.3068 0.0678 0.0093 -0.0116 71 LYS A O 142 C CB . LYS A 30 ? 0.3087 0.2750 0.3016 0.0782 -0.0020 -0.0151 71 LYS A CB 143 C CG . LYS A 30 ? 0.3181 0.2862 0.3186 0.0760 0.0000 -0.0161 71 LYS A CG 144 C CD . LYS A 30 ? 0.3581 0.3240 0.3583 0.0807 -0.0039 -0.0176 71 LYS A CD 145 C CE . LYS A 30 ? 0.3996 0.3678 0.4081 0.0785 -0.0026 -0.0193 71 LYS A CE 146 N NZ . LYS A 30 ? 0.3740 0.3398 0.3819 0.0835 -0.0065 -0.0204 71 LYS A NZ 147 N N . LYS A 31 ? 0.3154 0.2769 0.3024 0.0771 0.0086 -0.0069 72 LYS A N 148 C CA . LYS A 31 ? 0.3174 0.2768 0.3054 0.0764 0.0140 -0.0034 72 LYS A CA 149 C C . LYS A 31 ? 0.3010 0.2636 0.2919 0.0713 0.0168 -0.0030 72 LYS A C 150 O O . LYS A 31 ? 0.2789 0.2431 0.2759 0.0677 0.0201 -0.0028 72 LYS A O 151 C CB . LYS A 31 ? 0.3387 0.2916 0.3181 0.0824 0.0157 0.0009 72 LYS A CB 152 C CG . LYS A 31 ? 0.4173 0.3665 0.3946 0.0873 0.0142 0.0011 72 LYS A CG 153 C CD . LYS A 31 ? 0.5097 0.4521 0.4766 0.0942 0.0148 0.0050 72 LYS A CD 154 C CE . LYS A 31 ? 0.5822 0.5208 0.5464 0.0994 0.0126 0.0050 72 LYS A CE 155 N NZ . LYS A 31 ? 0.6421 0.5739 0.5945 0.1068 0.0121 0.0082 72 LYS A NZ 156 N N . PHE A 32 ? 0.2844 0.2479 0.2712 0.0711 0.0151 -0.0033 73 PHE A N 157 C CA . PHE A 32 ? 0.2811 0.2474 0.2704 0.0666 0.0174 -0.0029 73 PHE A CA 158 C C . PHE A 32 ? 0.2655 0.2375 0.2628 0.0608 0.0168 -0.0066 73 PHE A C 159 O O . PHE A 32 ? 0.2779 0.2520 0.2801 0.0567 0.0197 -0.0064 73 PHE A O 160 C CB . PHE A 32 ? 0.2951 0.2610 0.2780 0.0679 0.0154 -0.0025 73 PHE A CB 161 C CG . PHE A 32 ? 0.2927 0.2528 0.2668 0.0737 0.0165 0.0012 73 PHE A CG 162 C CD1 . PHE A 32 ? 0.2997 0.2560 0.2731 0.0758 0.0209 0.0050 73 PHE A CD1 163 C CD2 . PHE A 32 ? 0.2626 0.2210 0.2292 0.0771 0.0133 0.0011 73 PHE A CD2 164 C CE1 . PHE A 32 ? 0.3132 0.2638 0.2780 0.0816 0.0224 0.0088 73 PHE A CE1 165 C CE2 . PHE A 32 ? 0.3072 0.2599 0.2648 0.0828 0.0144 0.0046 73 PHE A CE2 166 C CZ . PHE A 32 ? 0.3537 0.3025 0.3102 0.0851 0.0192 0.0085 73 PHE A CZ 167 N N . LEU A 33 ? 0.2445 0.2189 0.2436 0.0605 0.0130 -0.0099 74 LEU A N 168 C CA . LEU A 33 ? 0.2317 0.2112 0.2380 0.0554 0.0127 -0.0133 74 LEU A CA 169 C C . LEU A 33 ? 0.2402 0.2201 0.2524 0.0535 0.0157 -0.0133 74 LEU A C 170 O O . LEU A 33 ? 0.2498 0.2325 0.2665 0.0491 0.0177 -0.0143 74 LEU A O 171 C CB . LEU A 33 ? 0.2375 0.2192 0.2456 0.0558 0.0085 -0.0166 74 LEU A CB 172 C CG . LEU A 33 ? 0.2351 0.2220 0.2503 0.0505 0.0086 -0.0198 74 LEU A CG 173 C CD1 . LEU A 33 ? 0.2369 0.2268 0.2521 0.0464 0.0096 -0.0200 74 LEU A CD1 174 C CD2 . LEU A 33 ? 0.2642 0.2532 0.2826 0.0510 0.0050 -0.0230 74 LEU A CD2 175 N N . TYR A 34 ? 0.2477 0.2246 0.2598 0.0569 0.0159 -0.0125 75 TYR A N 176 C CA . TYR A 34 ? 0.2539 0.2306 0.2714 0.0554 0.0188 -0.0123 75 TYR A CA 177 C C . TYR A 34 ? 0.2577 0.2335 0.2762 0.0534 0.0229 -0.0098 75 TYR A C 178 O O . TYR A 34 ? 0.2733 0.2515 0.2977 0.0496 0.0248 -0.0111 75 TYR A O 179 C CB . TYR A 34 ? 0.2679 0.2404 0.2838 0.0602 0.0188 -0.0108 75 TYR A CB 180 C CG . TYR A 34 ? 0.2610 0.2331 0.2828 0.0588 0.0217 -0.0107 75 TYR A CG 181 C CD1 . TYR A 34 ? 0.2771 0.2522 0.3050 0.0568 0.0206 -0.0141 75 TYR A CD1 182 C CD2 . TYR A 34 ? 0.3431 0.3119 0.3650 0.0596 0.0257 -0.0073 75 TYR A CD2 183 C CE1 . TYR A 34 ? 0.3017 0.2764 0.3351 0.0556 0.0231 -0.0143 75 TYR A CE1 184 C CE2 . TYR A 34 ? 0.3459 0.3143 0.3741 0.0582 0.0282 -0.0074 75 TYR A CE2 185 C CZ . TYR A 34 ? 0.3406 0.3120 0.3742 0.0563 0.0267 -0.0111 75 TYR A CZ 186 O OH . TYR A 34 ? 0.4177 0.3886 0.4574 0.0550 0.0290 -0.0115 75 TYR A OH 187 N N . ASN A 35 ? 0.2500 0.2224 0.2629 0.0561 0.0243 -0.0063 76 ASN A N 188 C CA . ASN A 35 ? 0.2645 0.2358 0.2788 0.0547 0.0282 -0.0035 76 ASN A CA 189 C C . ASN A 35 ? 0.2588 0.2344 0.2766 0.0495 0.0284 -0.0054 76 ASN A C 190 O O . ASN A 35 ? 0.2612 0.2373 0.2837 0.0468 0.0312 -0.0048 76 ASN A O 191 C CB . ASN A 35 ? 0.2736 0.2408 0.2806 0.0588 0.0292 0.0003 76 ASN A CB 192 C CG . ASN A 35 ? 0.3046 0.2703 0.3135 0.0578 0.0336 0.0036 76 ASN A CG 193 O OD1 . ASN A 35 ? 0.3039 0.2715 0.3127 0.0554 0.0340 0.0037 76 ASN A OD1 194 N ND2 . ASN A 35 ? 0.3132 0.2754 0.3244 0.0596 0.0370 0.0062 76 ASN A ND2 195 N N . PHE A 36 ? 0.2427 0.2212 0.2583 0.0482 0.0253 -0.0077 77 PHE A N 196 C CA . PHE A 36 ? 0.2341 0.2163 0.2517 0.0437 0.0253 -0.0091 77 PHE A CA 197 C C . PHE A 36 ? 0.2428 0.2291 0.2664 0.0395 0.0248 -0.0128 77 PHE A C 198 O O . PHE A 36 ? 0.2179 0.2071 0.2431 0.0359 0.0249 -0.0142 77 PHE A O 199 C CB . PHE A 36 ? 0.2419 0.2252 0.2543 0.0442 0.0224 -0.0097 77 PHE A CB 200 C CG . PHE A 36 ? 0.2525 0.2322 0.2582 0.0480 0.0228 -0.0063 77 PHE A CG 201 C CD1 . PHE A 36 ? 0.2558 0.2318 0.2603 0.0503 0.0262 -0.0026 77 PHE A CD1 202 C CD2 . PHE A 36 ? 0.2408 0.2209 0.2414 0.0493 0.0198 -0.0069 77 PHE A CD2 203 C CE1 . PHE A 36 ? 0.2630 0.2355 0.2608 0.0540 0.0268 0.0005 77 PHE A CE1 204 C CE2 . PHE A 36 ? 0.2463 0.2229 0.2400 0.0530 0.0200 -0.0040 77 PHE A CE2 205 C CZ . PHE A 36 ? 0.2785 0.2513 0.2706 0.0554 0.0236 -0.0003 77 PHE A CZ 206 N N . THR A 37 ? 0.2356 0.2220 0.2624 0.0402 0.0244 -0.0145 78 THR A N 207 C CA . THR A 37 ? 0.2446 0.2348 0.2760 0.0367 0.0236 -0.0181 78 THR A CA 208 C C . THR A 37 ? 0.2453 0.2352 0.2824 0.0356 0.0256 -0.0191 78 THR A C 209 O O . THR A 37 ? 0.2598 0.2523 0.3005 0.0337 0.0250 -0.0222 78 THR A O 210 C CB . THR A 37 ? 0.2459 0.2376 0.2767 0.0379 0.0205 -0.0203 78 THR A CB 211 O OG1 . THR A 37 ? 0.2449 0.2335 0.2745 0.0420 0.0199 -0.0192 78 THR A OG1 212 C CG2 . THR A 37 ? 0.2313 0.2240 0.2575 0.0382 0.0181 -0.0202 78 THR A CG2 213 N N . GLN A 38 ? 0.2602 0.2469 0.2983 0.0369 0.0281 -0.0166 79 GLN A N 214 C CA . GLN A 38 ? 0.2807 0.2668 0.3247 0.0362 0.0299 -0.0174 79 GLN A CA 215 C C . GLN A 38 ? 0.2885 0.2768 0.3370 0.0319 0.0311 -0.0194 79 GLN A C 216 O O . GLN A 38 ? 0.2941 0.2830 0.3476 0.0306 0.0319 -0.0214 79 GLN A O 217 C CB . GLN A 38 ? 0.2836 0.2650 0.3275 0.0394 0.0323 -0.0138 79 GLN A CB 218 C CG . GLN A 38 ? 0.3103 0.2890 0.3492 0.0442 0.0309 -0.0120 79 GLN A CG 219 C CD . GLN A 38 ? 0.3479 0.3284 0.3885 0.0444 0.0285 -0.0152 79 GLN A CD 220 O OE1 . GLN A 38 ? 0.4230 0.4037 0.4687 0.0436 0.0294 -0.0167 79 GLN A OE1 221 N NE2 . GLN A 38 ? 0.3512 0.3334 0.3883 0.0452 0.0253 -0.0166 79 GLN A NE2 222 N N . ILE A 39 ? 0.2821 0.2715 0.3290 0.0301 0.0313 -0.0187 80 ILE A N 223 C CA . ILE A 39 ? 0.2747 0.2661 0.3253 0.0263 0.0319 -0.0206 80 ILE A CA 224 C C . ILE A 39 ? 0.2657 0.2601 0.3127 0.0243 0.0302 -0.0217 80 ILE A C 225 O O . ILE A 39 ? 0.2355 0.2297 0.2776 0.0259 0.0290 -0.0202 80 ILE A O 226 C CB . ILE A 39 ? 0.2846 0.2738 0.3384 0.0261 0.0343 -0.0182 80 ILE A CB 227 C CG1 . ILE A 39 ? 0.3055 0.2932 0.3551 0.0277 0.0349 -0.0147 80 ILE A CG1 228 C CG2 . ILE A 39 ? 0.3157 0.3017 0.3736 0.0281 0.0364 -0.0169 80 ILE A CG2 229 C CD1 . ILE A 39 ? 0.3336 0.3197 0.3871 0.0270 0.0373 -0.0125 80 ILE A CD1 230 N N . PRO A 40 ? 0.2517 0.2486 0.3008 0.0209 0.0299 -0.0244 81 PRO A N 231 C CA . PRO A 40 ? 0.2377 0.2370 0.2832 0.0190 0.0285 -0.0252 81 PRO A CA 232 C C . PRO A 40 ? 0.2312 0.2294 0.2747 0.0193 0.0290 -0.0223 81 PRO A C 233 O O . PRO A 40 ? 0.2432 0.2394 0.2896 0.0197 0.0307 -0.0205 81 PRO A O 234 C CB . PRO A 40 ? 0.2501 0.2516 0.2983 0.0158 0.0284 -0.0285 81 PRO A CB 235 C CG . PRO A 40 ? 0.2547 0.2554 0.3074 0.0162 0.0293 -0.0302 81 PRO A CG 236 C CD . PRO A 40 ? 0.2536 0.2510 0.3079 0.0189 0.0307 -0.0270 81 PRO A CD 237 N N . HIS A 41 ? 0.2083 0.2079 0.2472 0.0191 0.0275 -0.0219 82 HIS A N 238 C CA . HIS A 41 ? 0.2000 0.1988 0.2366 0.0193 0.0278 -0.0194 82 HIS A CA 239 C C . HIS A 41 ? 0.1971 0.1986 0.2318 0.0166 0.0264 -0.0210 82 HIS A C 240 O O . HIS A 41 ? 0.2054 0.2073 0.2358 0.0171 0.0253 -0.0199 82 HIS A O 241 C CB . HIS A 41 ? 0.2244 0.2210 0.2562 0.0228 0.0275 -0.0165 82 HIS A CB 242 C CG . HIS A 41 ? 0.2076 0.2010 0.2405 0.0259 0.0291 -0.0144 82 HIS A CG 243 N ND1 . HIS A 41 ? 0.2285 0.2211 0.2605 0.0282 0.0283 -0.0150 82 HIS A ND1 244 C CD2 . HIS A 41 ? 0.2352 0.2259 0.2708 0.0271 0.0317 -0.0119 82 HIS A CD2 245 C CE1 . HIS A 41 ? 0.2518 0.2411 0.2849 0.0308 0.0301 -0.0127 82 HIS A CE1 246 N NE2 . HIS A 41 ? 0.2545 0.2426 0.2899 0.0302 0.0325 -0.0107 82 HIS A NE2 247 N N . LEU A 42 ? 0.1955 0.1986 0.2331 0.0139 0.0263 -0.0236 83 LEU A N 248 C CA . LEU A 42 ? 0.1955 0.2009 0.2310 0.0114 0.0250 -0.0253 83 LEU A CA 249 C C . LEU A 42 ? 0.2010 0.2059 0.2354 0.0111 0.0250 -0.0232 83 LEU A C 250 O O . LEU A 42 ? 0.2085 0.2118 0.2463 0.0115 0.0264 -0.0216 83 LEU A O 251 C CB . LEU A 42 ? 0.1997 0.2062 0.2382 0.0090 0.0250 -0.0285 83 LEU A CB 252 C CG . LEU A 42 ? 0.1929 0.2015 0.2285 0.0067 0.0237 -0.0305 83 LEU A CG 253 C CD1 . LEU A 42 ? 0.2239 0.2342 0.2558 0.0067 0.0230 -0.0313 83 LEU A CD1 254 C CD2 . LEU A 42 ? 0.1947 0.2037 0.2334 0.0050 0.0238 -0.0339 83 LEU A CD2 255 N N . ALA A 43 ? 0.1851 0.1914 0.2153 0.0104 0.0237 -0.0230 84 ALA A N 256 C CA . ALA A 43 ? 0.1805 0.1865 0.2098 0.0101 0.0236 -0.0211 84 ALA A CA 257 C C . ALA A 43 ? 0.1936 0.1997 0.2273 0.0082 0.0239 -0.0222 84 ALA A C 258 O O . ALA A 43 ? 0.1866 0.1940 0.2216 0.0063 0.0232 -0.0252 84 ALA A O 259 C CB . ALA A 43 ? 0.1961 0.2038 0.2207 0.0091 0.0219 -0.0216 84 ALA A CB 260 N N . GLY A 44 ? 0.1965 0.2013 0.2326 0.0089 0.0250 -0.0198 85 GLY A N 261 C CA . GLY A 44 ? 0.2247 0.2297 0.2660 0.0072 0.0251 -0.0205 85 GLY A CA 262 C C . GLY A 44 ? 0.2430 0.2467 0.2907 0.0074 0.0266 -0.0211 85 GLY A C 263 O O . GLY A 44 ? 0.2658 0.2693 0.3189 0.0061 0.0266 -0.0218 85 GLY A O 264 N N . THR A 45 ? 0.2227 0.2253 0.2702 0.0089 0.0276 -0.0209 86 THR A N 265 C CA . THR A 45 ? 0.2198 0.2208 0.2736 0.0091 0.0291 -0.0213 86 THR A CA 266 C C . THR A 45 ? 0.2331 0.2314 0.2896 0.0115 0.0318 -0.0173 86 THR A C 267 O O . THR A 45 ? 0.2297 0.2269 0.2820 0.0137 0.0326 -0.0144 86 THR A O 268 C CB . THR A 45 ? 0.2223 0.2235 0.2753 0.0095 0.0289 -0.0235 86 THR A CB 269 O OG1 . THR A 45 ? 0.2293 0.2295 0.2781 0.0120 0.0294 -0.0213 86 THR A OG1 270 C CG2 . THR A 45 ? 0.2142 0.2179 0.2646 0.0073 0.0268 -0.0272 86 THR A CG2 271 N N . GLU A 46 ? 0.2387 0.2355 0.3023 0.0114 0.0334 -0.0173 87 GLU A N 272 C CA . GLU A 46 ? 0.2611 0.2550 0.3278 0.0137 0.0365 -0.0133 87 GLU A CA 273 C C . GLU A 46 ? 0.2537 0.2456 0.3153 0.0169 0.0376 -0.0110 87 GLU A C 274 O O . GLU A 46 ? 0.2726 0.2622 0.3321 0.0196 0.0397 -0.0071 87 GLU A O 275 C CB . GLU A 46 ? 0.2861 0.2787 0.3619 0.0128 0.0379 -0.0140 87 GLU A CB 276 C CG . GLU A 46 ? 0.3659 0.3552 0.4454 0.0154 0.0416 -0.0097 87 GLU A CG 277 C CD . GLU A 46 ? 0.4621 0.4507 0.5430 0.0160 0.0434 -0.0063 87 GLU A CD 278 O OE1 . GLU A 46 ? 0.5342 0.5199 0.6158 0.0187 0.0468 -0.0021 87 GLU A OE1 279 O OE2 . GLU A 46 ? 0.5028 0.4937 0.5840 0.0139 0.0416 -0.0076 87 GLU A OE2 280 N N . GLN A 47 ? 0.2614 0.2540 0.3210 0.0169 0.0363 -0.0134 88 GLN A N 281 C CA . GLN A 47 ? 0.2591 0.2500 0.3142 0.0200 0.0367 -0.0120 88 GLN A CA 282 C C . GLN A 47 ? 0.2468 0.2378 0.2944 0.0217 0.0358 -0.0101 88 GLN A C 283 O O . GLN A 47 ? 0.2486 0.2370 0.2927 0.0251 0.0370 -0.0072 88 GLN A O 284 C CB . GLN A 47 ? 0.2814 0.2738 0.3361 0.0193 0.0351 -0.0154 88 GLN A CB 285 C CG . GLN A 47 ? 0.3090 0.3008 0.3709 0.0180 0.0360 -0.0173 88 GLN A CG 286 C CD . GLN A 47 ? 0.4223 0.4169 0.4866 0.0145 0.0342 -0.0213 88 GLN A CD 287 O OE1 . GLN A 47 ? 0.3564 0.3521 0.4209 0.0129 0.0335 -0.0214 88 GLN A OE1 288 N NE2 . GLN A 47 ? 0.4708 0.4662 0.5364 0.0136 0.0334 -0.0246 88 GLN A NE2 289 N N . ASN A 48 ? 0.2322 0.2259 0.2771 0.0196 0.0337 -0.0118 89 ASN A N 290 C CA . ASN A 48 ? 0.2354 0.2292 0.2735 0.0212 0.0327 -0.0103 89 ASN A CA 291 C C . ASN A 48 ? 0.2613 0.2532 0.2988 0.0228 0.0346 -0.0066 89 ASN A C 292 O O . ASN A 48 ? 0.2686 0.2590 0.3003 0.0255 0.0345 -0.0044 89 ASN A O 293 C CB . ASN A 48 ? 0.2438 0.2409 0.2791 0.0186 0.0300 -0.0130 89 ASN A CB 294 C CG . ASN A 48 ? 0.2745 0.2717 0.3030 0.0204 0.0284 -0.0122 89 ASN A CG 295 O OD1 . ASN A 48 ? 0.2536 0.2489 0.2794 0.0234 0.0284 -0.0110 89 ASN A OD1 296 N ND2 . ASN A 48 ? 0.2569 0.2560 0.2827 0.0188 0.0268 -0.0129 89 ASN A ND2 297 N N . PHE A 49 ? 0.2379 0.2297 0.2813 0.0212 0.0362 -0.0060 90 PHE A N 298 C CA . PHE A 49 ? 0.2451 0.2350 0.2893 0.0227 0.0386 -0.0023 90 PHE A CA 299 C C . PHE A 49 ? 0.2513 0.2373 0.2952 0.0265 0.0416 0.0011 90 PHE A C 300 O O . PHE A 49 ? 0.2535 0.2371 0.2928 0.0296 0.0431 0.0045 90 PHE A O 301 C CB A PHE A 49 ? 0.2541 0.2451 0.3064 0.0199 0.0394 -0.0029 90 PHE A CB 302 C CB B PHE A 49 ? 0.2416 0.2326 0.2936 0.0200 0.0394 -0.0028 90 PHE A CB 303 C CG A PHE A 49 ? 0.2572 0.2465 0.3123 0.0212 0.0423 0.0008 90 PHE A CG 304 C CG B PHE A 49 ? 0.2173 0.2061 0.2724 0.0217 0.0428 0.0013 90 PHE A CG 305 C CD1 A PHE A 49 ? 0.2625 0.2508 0.3115 0.0235 0.0430 0.0036 90 PHE A CD1 306 C CD1 B PHE A 49 ? 0.2001 0.1888 0.2514 0.0226 0.0430 0.0033 90 PHE A CD1 307 C CD2 A PHE A 49 ? 0.2968 0.2856 0.3612 0.0198 0.0442 0.0012 90 PHE A CD2 308 C CD2 B PHE A 49 ? 0.2218 0.2083 0.2840 0.0223 0.0459 0.0030 90 PHE A CD2 309 C CE1 A PHE A 49 ? 0.2980 0.2847 0.3498 0.0247 0.0460 0.0072 90 PHE A CE1 310 C CE1 B PHE A 49 ? 0.1975 0.1842 0.2520 0.0242 0.0465 0.0072 90 PHE A CE1 311 C CE2 A PHE A 49 ? 0.3208 0.3083 0.3890 0.0208 0.0472 0.0047 90 PHE A CE2 312 C CE2 B PHE A 49 ? 0.1809 0.1653 0.2466 0.0239 0.0494 0.0069 90 PHE A CE2 313 C CZ A PHE A 49 ? 0.3343 0.3207 0.3959 0.0233 0.0482 0.0078 90 PHE A CZ 314 C CZ B PHE A 49 ? 0.1869 0.1714 0.2487 0.0249 0.0499 0.0091 90 PHE A CZ 315 N N . GLN A 50 ? 0.2572 0.2423 0.3055 0.0264 0.0425 0.0003 91 GLN A N 316 C CA . GLN A 50 ? 0.2793 0.2604 0.3267 0.0302 0.0453 0.0037 91 GLN A CA 317 C C . GLN A 50 ? 0.2657 0.2453 0.3039 0.0338 0.0440 0.0047 91 GLN A C 318 O O . GLN A 50 ? 0.2660 0.2421 0.3003 0.0376 0.0461 0.0083 91 GLN A O 319 C CB . GLN A 50 ? 0.2984 0.2786 0.3521 0.0297 0.0463 0.0025 91 GLN A CB 320 C CG . GLN A 50 ? 0.3526 0.3333 0.4161 0.0269 0.0480 0.0022 91 GLN A CG 321 C CD . GLN A 50 ? 0.4765 0.4543 0.5428 0.0288 0.0520 0.0069 91 GLN A CD 322 O OE1 . GLN A 50 ? 0.5090 0.4833 0.5715 0.0327 0.0547 0.0108 91 GLN A OE1 323 N NE2 . GLN A 50 ? 0.5122 0.4916 0.5852 0.0262 0.0525 0.0066 91 GLN A NE2 324 N N . LEU A 51 ? 0.2545 0.2366 0.2893 0.0326 0.0405 0.0013 92 LEU A N 325 C CA . LEU A 51 ? 0.2481 0.2290 0.2750 0.0358 0.0387 0.0018 92 LEU A CA 326 C C . LEU A 51 ? 0.2495 0.2297 0.2708 0.0374 0.0386 0.0040 92 LEU A C 327 O O . LEU A 51 ? 0.2557 0.2327 0.2707 0.0416 0.0390 0.0065 92 LEU A O 328 C CB . LEU A 51 ? 0.2480 0.2321 0.2736 0.0341 0.0350 -0.0022 92 LEU A CB 329 C CG . LEU A 51 ? 0.2507 0.2335 0.2694 0.0374 0.0328 -0.0022 92 LEU A CG 330 C CD1 . LEU A 51 ? 0.2645 0.2432 0.2816 0.0417 0.0342 0.0001 92 LEU A CD1 331 C CD2 . LEU A 51 ? 0.2570 0.2432 0.2759 0.0352 0.0295 -0.0062 92 LEU A CD2 332 N N . ALA A 52 ? 0.2263 0.2091 0.2491 0.0344 0.0380 0.0031 93 ALA A N 333 C CA . ALA A 52 ? 0.2391 0.2212 0.2573 0.0359 0.0384 0.0054 93 ALA A CA 334 C C . ALA A 52 ? 0.2508 0.2286 0.2679 0.0397 0.0423 0.0100 93 ALA A C 335 O O . ALA A 52 ? 0.2549 0.2302 0.2650 0.0434 0.0425 0.0123 93 ALA A O 336 C CB . ALA A 52 ? 0.2388 0.2240 0.2604 0.0322 0.0378 0.0042 93 ALA A CB 337 N N . LYS A 53 ? 0.2644 0.2413 0.2887 0.0389 0.0455 0.0114 94 LYS A N 338 C CA . LYS A 53 ? 0.2698 0.2425 0.2943 0.0423 0.0500 0.0161 94 LYS A CA 339 C C . LYS A 53 ? 0.2653 0.2339 0.2835 0.0472 0.0506 0.0181 94 LYS A C 340 O O . LYS A 53 ? 0.2776 0.2424 0.2905 0.0515 0.0531 0.0219 94 LYS A O 341 C CB . LYS A 53 ? 0.2805 0.2533 0.3154 0.0400 0.0530 0.0167 94 LYS A CB 342 C CG . LYS A 53 ? 0.3362 0.3124 0.3768 0.0361 0.0525 0.0154 94 LYS A CG 343 C CD . LYS A 53 ? 0.4700 0.4455 0.5209 0.0347 0.0559 0.0169 94 LYS A CD 344 C CE . LYS A 53 ? 0.5306 0.5071 0.5877 0.0324 0.0550 0.0140 94 LYS A CE 345 N NZ . LYS A 53 ? 0.5950 0.5719 0.6635 0.0299 0.0571 0.0141 94 LYS A NZ 346 N N . GLN A 54 ? 0.2792 0.2484 0.2979 0.0468 0.0485 0.0155 95 GLN A N 347 C CA . GLN A 54 ? 0.2797 0.2452 0.2923 0.0515 0.0485 0.0169 95 GLN A CA 348 C C . GLN A 54 ? 0.2829 0.2474 0.2854 0.0547 0.0458 0.0171 95 GLN A C 349 O O . GLN A 54 ? 0.2837 0.2438 0.2795 0.0597 0.0472 0.0202 95 GLN A O 350 C CB . GLN A 54 ? 0.2788 0.2459 0.2942 0.0500 0.0460 0.0135 95 GLN A CB 351 C CG . GLN A 54 ? 0.2983 0.2616 0.3071 0.0550 0.0454 0.0147 95 GLN A CG 352 C CD . GLN A 54 ? 0.3024 0.2676 0.3127 0.0539 0.0422 0.0110 95 GLN A CD 353 O OE1 . GLN A 54 ? 0.2976 0.2653 0.3154 0.0503 0.0424 0.0088 95 GLN A OE1 354 N NE2 . GLN A 54 ? 0.3018 0.2660 0.3053 0.0571 0.0391 0.0102 95 GLN A NE2 355 N N . ILE A 55 ? 0.2746 0.2429 0.2759 0.0519 0.0419 0.0137 96 ILE A N 356 C CA . ILE A 55 ? 0.2717 0.2393 0.2643 0.0547 0.0389 0.0133 96 ILE A CA 357 C C . ILE A 55 ? 0.2675 0.2324 0.2557 0.0573 0.0414 0.0170 96 ILE A C 358 O O . ILE A 55 ? 0.2883 0.2496 0.2683 0.0623 0.0412 0.0189 96 ILE A O 359 C CB . ILE A 55 ? 0.2661 0.2385 0.2596 0.0506 0.0347 0.0091 96 ILE A CB 360 C CG1 A ILE A 55 ? 0.2910 0.2659 0.2887 0.0483 0.0325 0.0056 96 ILE A CG1 361 C CG1 B ILE A 55 ? 0.2714 0.2457 0.2677 0.0493 0.0323 0.0058 96 ILE A CG1 362 C CG2 . ILE A 55 ? 0.2952 0.2671 0.2808 0.0531 0.0317 0.0088 96 ILE A CG2 363 C CD1 A ILE A 55 ? 0.2985 0.2713 0.2921 0.0519 0.0305 0.0051 96 ILE A CD1 364 C CD1 B ILE A 55 ? 0.2653 0.2445 0.2651 0.0446 0.0295 0.0019 96 ILE A CD1 365 N N . GLN A 56 ? 0.2650 0.2317 0.2588 0.0543 0.0439 0.0180 97 GLN A N 366 C CA . GLN A 56 ? 0.2772 0.2415 0.2679 0.0567 0.0469 0.0216 97 GLN A CA 367 C C . GLN A 56 ? 0.2940 0.2526 0.2807 0.0622 0.0508 0.0260 97 GLN A C 368 O O . GLN A 56 ? 0.3155 0.2708 0.2940 0.0667 0.0514 0.0283 97 GLN A O 369 C CB . GLN A 56 ? 0.2736 0.2407 0.2729 0.0525 0.0493 0.0220 97 GLN A CB 370 C CG . GLN A 56 ? 0.2924 0.2571 0.2901 0.0549 0.0530 0.0260 97 GLN A CG 371 C CD . GLN A 56 ? 0.3055 0.2727 0.3127 0.0509 0.0553 0.0265 97 GLN A CD 372 O OE1 . GLN A 56 ? 0.3099 0.2791 0.3258 0.0475 0.0558 0.0250 97 GLN A OE1 373 N NE2 . GLN A 56 ? 0.3061 0.2733 0.3121 0.0515 0.0567 0.0284 97 GLN A NE2 374 N N . SER A 57 ? 0.3047 0.2621 0.2970 0.0620 0.0535 0.0271 98 SER A N 375 C CA . SER A 57 ? 0.3180 0.2697 0.3070 0.0672 0.0577 0.0315 98 SER A CA 376 C C . SER A 57 ? 0.3149 0.2630 0.2932 0.0725 0.0552 0.0316 98 SER A C 377 O O . SER A 57 ? 0.3225 0.2656 0.2931 0.0780 0.0576 0.0353 98 SER A O 378 C CB . SER A 57 ? 0.3208 0.2722 0.3184 0.0656 0.0604 0.0321 98 SER A CB 379 O OG A SER A 57 ? 0.3716 0.3243 0.3784 0.0625 0.0641 0.0336 98 SER A OG 380 O OG B SER A 57 ? 0.3041 0.2497 0.2984 0.0707 0.0647 0.0367 98 SER A OG 381 N N . GLN A 58 ? 0.2963 0.2468 0.2742 0.0711 0.0504 0.0275 99 GLN A N 382 C CA . GLN A 58 ? 0.3123 0.2597 0.2810 0.0760 0.0472 0.0270 99 GLN A CA 383 C C . GLN A 58 ? 0.3062 0.2527 0.2659 0.0787 0.0446 0.0268 99 GLN A C 384 O O . GLN A 58 ? 0.3267 0.2684 0.2772 0.0846 0.0444 0.0287 99 GLN A O 385 C CB . GLN A 58 ? 0.3028 0.2531 0.2745 0.0737 0.0430 0.0227 99 GLN A CB 386 C CG . GLN A 58 ? 0.3340 0.2840 0.3133 0.0723 0.0457 0.0233 99 GLN A CG 387 C CD . GLN A 58 ? 0.3867 0.3391 0.3685 0.0707 0.0418 0.0192 99 GLN A CD 388 O OE1 . GLN A 58 ? 0.3538 0.3111 0.3394 0.0663 0.0387 0.0153 99 GLN A OE1 389 N NE2 . GLN A 58 ? 0.4648 0.4137 0.4446 0.0744 0.0421 0.0203 99 GLN A NE2 390 N N . TRP A 59 ? 0.2951 0.2460 0.2570 0.0747 0.0424 0.0244 100 TRP A N 391 C CA . TRP A 59 ? 0.2976 0.2474 0.2512 0.0774 0.0402 0.0243 100 TRP A CA 392 C C . TRP A 59 ? 0.3115 0.2566 0.2595 0.0818 0.0447 0.0291 100 TRP A C 393 O O . TRP A 59 ? 0.3222 0.2639 0.2605 0.0867 0.0432 0.0299 100 TRP A O 394 C CB . TRP A 59 ? 0.2847 0.2399 0.2427 0.0719 0.0377 0.0212 100 TRP A CB 395 C CG . TRP A 59 ? 0.2541 0.2131 0.2144 0.0689 0.0326 0.0166 100 TRP A CG 396 C CD1 . TRP A 59 ? 0.2785 0.2372 0.2390 0.0700 0.0303 0.0147 100 TRP A CD1 397 C CD2 . TRP A 59 ? 0.2617 0.2257 0.2252 0.0642 0.0295 0.0132 100 TRP A CD2 398 N NE1 . TRP A 59 ? 0.2703 0.2334 0.2340 0.0662 0.0261 0.0104 100 TRP A NE1 399 C CE2 . TRP A 59 ? 0.2689 0.2352 0.2343 0.0627 0.0256 0.0095 100 TRP A CE2 400 C CE3 . TRP A 59 ? 0.2710 0.2374 0.2356 0.0614 0.0297 0.0131 100 TRP A CE3 401 C CZ2 . TRP A 59 ? 0.2737 0.2445 0.2422 0.0584 0.0223 0.0059 100 TRP A CZ2 402 C CZ3 . TRP A 59 ? 0.2419 0.2129 0.2094 0.0571 0.0261 0.0094 100 TRP A CZ3 403 C CH2 . TRP A 59 ? 0.2621 0.2351 0.2314 0.0558 0.0227 0.0060 100 TRP A CH2 404 N N . LYS A 60 ? 0.3193 0.2641 0.2737 0.0803 0.0501 0.0322 101 LYS A N 405 C CA . LYS A 60 ? 0.3624 0.3024 0.3121 0.0849 0.0553 0.0373 101 LYS A CA 406 C C . LYS A 60 ? 0.3689 0.3026 0.3104 0.0916 0.0565 0.0399 101 LYS A C 407 O O . LYS A 60 ? 0.3859 0.3151 0.3170 0.0972 0.0569 0.0421 101 LYS A O 408 C CB . LYS A 60 ? 0.3768 0.3176 0.3362 0.0820 0.0611 0.0403 101 LYS A CB 409 C CG . LYS A 60 ? 0.4058 0.3521 0.3725 0.0763 0.0601 0.0382 101 LYS A CG 410 C CD . LYS A 60 ? 0.4679 0.4152 0.4454 0.0733 0.0653 0.0406 101 LYS A CD 411 C CE . LYS A 60 ? 0.4872 0.4391 0.4696 0.0689 0.0644 0.0391 101 LYS A CE 412 N NZ . LYS A 60 ? 0.5713 0.5229 0.5616 0.0679 0.0698 0.0425 101 LYS A NZ 413 N N . GLU A 61 ? 0.3706 0.3039 0.3163 0.0911 0.0569 0.0396 102 GLU A N 414 C CA A GLU A 61 ? 0.3879 0.3155 0.3265 0.0971 0.0576 0.0417 102 GLU A CA 415 C CA B GLU A 61 ? 0.3876 0.3148 0.3255 0.0975 0.0579 0.0421 102 GLU A CA 416 C C . GLU A 61 ? 0.3954 0.3209 0.3225 0.1016 0.0521 0.0395 102 GLU A C 417 O O . GLU A 61 ? 0.3962 0.3156 0.3128 0.1084 0.0529 0.0422 102 GLU A O 418 C CB A GLU A 61 ? 0.3933 0.3224 0.3392 0.0945 0.0568 0.0399 102 GLU A CB 419 C CB B GLU A 61 ? 0.3888 0.3161 0.3336 0.0960 0.0590 0.0419 102 GLU A CB 420 C CG A GLU A 61 ? 0.4301 0.3601 0.3872 0.0911 0.0622 0.0422 102 GLU A CG 421 C CG B GLU A 61 ? 0.4497 0.3713 0.3861 0.1024 0.0584 0.0434 102 GLU A CG 422 C CD A GLU A 61 ? 0.4632 0.3965 0.4290 0.0869 0.0602 0.0389 102 GLU A CD 423 C CD B GLU A 61 ? 0.5291 0.4522 0.4717 0.1002 0.0567 0.0411 102 GLU A CD 424 O OE1 A GLU A 61 ? 0.4454 0.3779 0.4074 0.0888 0.0564 0.0367 102 GLU A OE1 425 O OE1 B GLU A 61 ? 0.5639 0.4885 0.5165 0.0967 0.0604 0.0422 102 GLU A OE1 426 O OE2 A GLU A 61 ? 0.4573 0.3940 0.4338 0.0817 0.0622 0.0383 102 GLU A OE2 427 O OE2 B GLU A 61 ? 0.5694 0.4924 0.5075 0.1022 0.0515 0.0381 102 GLU A OE2 428 N N . PHE A 62 ? 0.3634 0.2938 0.2926 0.0978 0.0462 0.0345 103 PHE A N 429 C CA . PHE A 62 ? 0.3588 0.2879 0.2791 0.1014 0.0402 0.0316 103 PHE A CA 430 C C . PHE A 62 ? 0.3662 0.2921 0.2766 0.1057 0.0401 0.0332 103 PHE A C 431 O O . PHE A 62 ? 0.3941 0.3170 0.2952 0.1105 0.0358 0.0317 103 PHE A O 432 C CB . PHE A 62 ? 0.3493 0.2847 0.2753 0.0959 0.0344 0.0260 103 PHE A CB 433 C CG . PHE A 62 ? 0.3342 0.2724 0.2679 0.0927 0.0330 0.0235 103 PHE A CG 434 C CD1 . PHE A 62 ? 0.3437 0.2784 0.2775 0.0955 0.0354 0.0256 103 PHE A CD1 435 C CD2 . PHE A 62 ? 0.3492 0.2934 0.2899 0.0870 0.0293 0.0190 103 PHE A CD2 436 C CE1 . PHE A 62 ? 0.3825 0.3201 0.3239 0.0923 0.0339 0.0230 103 PHE A CE1 437 C CE2 . PHE A 62 ? 0.3523 0.2993 0.3001 0.0840 0.0280 0.0165 103 PHE A CE2 438 C CZ . PHE A 62 ? 0.3710 0.3149 0.3194 0.0865 0.0303 0.0184 103 PHE A CZ 439 N N . GLY A 63 ? 0.3624 0.2889 0.2750 0.1041 0.0445 0.0358 104 GLY A N 440 C CA . GLY A 63 ? 0.3789 0.3017 0.2822 0.1087 0.0458 0.0382 104 GLY A CA 441 C C . GLY A 63 ? 0.3768 0.3037 0.2822 0.1050 0.0444 0.0365 104 GLY A C 442 O O . GLY A 63 ? 0.4003 0.3242 0.2976 0.1089 0.0449 0.0380 104 GLY A O 443 N N . LEU A 64 ? 0.3545 0.2878 0.2700 0.0978 0.0426 0.0334 105 LEU A N 444 C CA . LEU A 64 ? 0.3241 0.2610 0.2411 0.0945 0.0412 0.0319 105 LEU A CA 445 C C . LEU A 64 ? 0.3479 0.2834 0.2656 0.0952 0.0471 0.0361 105 LEU A C 446 O O . LEU A 64 ? 0.3725 0.3063 0.2944 0.0956 0.0526 0.0397 105 LEU A O 447 C CB . LEU A 64 ? 0.3106 0.2545 0.2384 0.0868 0.0386 0.0280 105 LEU A CB 448 C CG . LEU A 64 ? 0.3054 0.2513 0.2332 0.0858 0.0327 0.0236 105 LEU A CG 449 C CD1 . LEU A 64 ? 0.3125 0.2651 0.2496 0.0784 0.0304 0.0200 105 LEU A CD1 450 C CD2 . LEU A 64 ? 0.3300 0.2734 0.2482 0.0902 0.0275 0.0215 105 LEU A CD2 451 N N . ASP A 65 ? 0.3475 0.2835 0.2616 0.0956 0.0461 0.0358 106 ASP A N 452 C CA . ASP A 65 ? 0.3649 0.2995 0.2794 0.0965 0.0515 0.0398 106 ASP A CA 453 C C . ASP A 65 ? 0.3703 0.3094 0.2974 0.0904 0.0550 0.0405 106 ASP A C 454 O O . ASP A 65 ? 0.3867 0.3241 0.3169 0.0914 0.0610 0.0446 106 ASP A O 455 C CB . ASP A 65 ? 0.3671 0.3015 0.2750 0.0980 0.0490 0.0387 106 ASP A CB 456 C CG . ASP A 65 ? 0.4043 0.3333 0.2992 0.1050 0.0463 0.0385 106 ASP A CG 457 O OD1 . ASP A 65 ? 0.4056 0.3287 0.2935 0.1111 0.0502 0.0424 106 ASP A OD1 458 O OD2 . ASP A 65 ? 0.3718 0.3022 0.2634 0.1046 0.0401 0.0345 106 ASP A OD2 459 N N . SER A 66 ? 0.3474 0.2923 0.2819 0.0842 0.0512 0.0364 107 SER A N 460 C CA . SER A 66 ? 0.3444 0.2938 0.2911 0.0782 0.0535 0.0364 107 SER A CA 461 C C . SER A 66 ? 0.3189 0.2727 0.2714 0.0733 0.0493 0.0321 107 SER A C 462 O O . SER A 66 ? 0.3025 0.2574 0.2509 0.0731 0.0441 0.0286 107 SER A O 463 C CB . SER A 66 ? 0.3516 0.3038 0.3015 0.0755 0.0541 0.0365 107 SER A CB 464 O OG A SER A 66 ? 0.3557 0.3090 0.2996 0.0756 0.0492 0.0336 107 SER A OG 465 O OG B SER A 66 ? 0.3519 0.3085 0.3029 0.0714 0.0487 0.0322 107 SER A OG 466 N N . VAL A 67 ? 0.2967 0.2528 0.2590 0.0694 0.0516 0.0322 108 VAL A N 467 C CA . VAL A 67 ? 0.2956 0.2559 0.2637 0.0646 0.0480 0.0281 108 VAL A CA 468 C C . VAL A 67 ? 0.3049 0.2687 0.2839 0.0595 0.0502 0.0280 108 VAL A C 469 O O . VAL A 67 ? 0.3117 0.2741 0.2963 0.0598 0.0547 0.0307 108 VAL A O 470 C CB . VAL A 67 ? 0.2936 0.2520 0.2615 0.0662 0.0478 0.0278 108 VAL A CB 471 C CG1 . VAL A 67 ? 0.2787 0.2416 0.2514 0.0615 0.0434 0.0230 108 VAL A CG1 472 C CG2 . VAL A 67 ? 0.2941 0.2476 0.2507 0.0726 0.0464 0.0288 108 VAL A CG2 473 N N . GLU A 68 ? 0.2822 0.2506 0.2645 0.0550 0.0470 0.0248 109 GLU A N 474 C CA . GLU A 68 ? 0.3085 0.2803 0.3005 0.0503 0.0484 0.0243 109 GLU A CA 475 C C . GLU A 68 ? 0.2947 0.2708 0.2916 0.0454 0.0447 0.0200 109 GLU A C 476 O O . GLU A 68 ? 0.3019 0.2789 0.2943 0.0453 0.0409 0.0173 109 GLU A O 477 C CB . GLU A 68 ? 0.3288 0.3021 0.3203 0.0494 0.0482 0.0248 109 GLU A CB 478 C CG . GLU A 68 ? 0.4104 0.3797 0.3976 0.0541 0.0523 0.0293 109 GLU A CG 479 C CD . GLU A 68 ? 0.5333 0.5002 0.5266 0.0554 0.0581 0.0331 109 GLU A CD 480 O OE1 . GLU A 68 ? 0.5479 0.5174 0.5514 0.0515 0.0592 0.0324 109 GLU A OE1 481 O OE2 . GLU A 68 ? 0.5927 0.5550 0.5806 0.0605 0.0616 0.0368 109 GLU A OE2 482 N N . LEU A 69 ? 0.2675 0.2460 0.2736 0.0416 0.0459 0.0193 110 LEU A N 483 C CA . LEU A 69 ? 0.2694 0.2520 0.2795 0.0369 0.0425 0.0151 110 LEU A CA 484 C C . LEU A 69 ? 0.2623 0.2479 0.2737 0.0342 0.0408 0.0139 110 LEU A C 485 O O . LEU A 69 ? 0.2913 0.2766 0.3061 0.0342 0.0433 0.0161 110 LEU A O 486 C CB . LEU A 69 ? 0.2748 0.2583 0.2941 0.0345 0.0442 0.0144 110 LEU A CB 487 C CG . LEU A 69 ? 0.3033 0.2839 0.3229 0.0368 0.0461 0.0156 110 LEU A CG 488 C CD1 . LEU A 69 ? 0.3458 0.3278 0.3750 0.0336 0.0470 0.0140 110 LEU A CD1 489 C CD2 . LEU A 69 ? 0.3008 0.2813 0.3139 0.0380 0.0429 0.0134 110 LEU A CD2 490 N N . ALA A 70 ? 0.2387 0.2269 0.2475 0.0318 0.0369 0.0106 111 ALA A N 491 C CA . ALA A 70 ? 0.2313 0.2224 0.2411 0.0290 0.0349 0.0092 111 ALA A CA 492 C C . ALA A 70 ? 0.2200 0.2141 0.2349 0.0249 0.0330 0.0057 111 ALA A C 493 O O . ALA A 70 ? 0.2387 0.2337 0.2513 0.0242 0.0308 0.0033 111 ALA A O 494 C CB . ALA A 70 ? 0.2314 0.2227 0.2333 0.0299 0.0319 0.0082 111 ALA A CB 495 N N . HIS A 71 ? 0.2070 0.2028 0.2288 0.0222 0.0336 0.0052 112 HIS A N 496 C CA . HIS A 71 ? 0.1999 0.1981 0.2263 0.0187 0.0318 0.0018 112 HIS A CA 497 C C . HIS A 71 ? 0.1944 0.1954 0.2207 0.0159 0.0291 -0.0002 112 HIS A C 498 O O . HIS A 71 ? 0.2151 0.2161 0.2406 0.0163 0.0293 0.0013 112 HIS A O 499 C CB . HIS A 71 ? 0.2043 0.2021 0.2395 0.0179 0.0342 0.0023 112 HIS A CB 500 C CG . HIS A 71 ? 0.2456 0.2436 0.2867 0.0174 0.0358 0.0040 112 HIS A CG 501 N ND1 . HIS A 71 ? 0.3142 0.3096 0.3568 0.0202 0.0396 0.0080 112 HIS A ND1 502 C CD2 . HIS A 71 ? 0.2933 0.2935 0.3391 0.0147 0.0343 0.0024 112 HIS A CD2 503 C CE1 . HIS A 71 ? 0.3043 0.3007 0.3531 0.0190 0.0404 0.0087 112 HIS A CE1 504 N NE2 . HIS A 71 ? 0.2973 0.2967 0.3484 0.0156 0.0370 0.0053 112 HIS A NE2 505 N N . TYR A 72 ? 0.1961 0.1992 0.2233 0.0132 0.0267 -0.0036 113 TYR A N 506 C CA . TYR A 72 ? 0.1853 0.1907 0.2115 0.0106 0.0239 -0.0059 113 TYR A CA 507 C C . TYR A 72 ? 0.1886 0.1954 0.2192 0.0081 0.0228 -0.0090 113 TYR A C 508 O O . TYR A 72 ? 0.2069 0.2130 0.2392 0.0083 0.0237 -0.0098 113 TYR A O 509 C CB . TYR A 72 ? 0.1926 0.1988 0.2112 0.0106 0.0217 -0.0069 113 TYR A CB 510 C CG . TYR A 72 ? 0.1872 0.1917 0.2010 0.0134 0.0224 -0.0042 113 TYR A CG 511 C CD1 . TYR A 72 ? 0.1887 0.1933 0.2014 0.0137 0.0222 -0.0027 113 TYR A CD1 512 C CD2 . TYR A 72 ? 0.2200 0.2225 0.2309 0.0161 0.0235 -0.0030 113 TYR A CD2 513 C CE1 . TYR A 72 ? 0.2217 0.2244 0.2300 0.0167 0.0232 -0.0001 113 TYR A CE1 514 C CE2 . TYR A 72 ? 0.2276 0.2281 0.2339 0.0192 0.0241 -0.0005 113 TYR A CE2 515 C CZ . TYR A 72 ? 0.2357 0.2363 0.2406 0.0195 0.0240 0.0009 113 TYR A CZ 516 O OH . TYR A 72 ? 0.2401 0.2384 0.2399 0.0229 0.0247 0.0032 113 TYR A OH 517 N N . ASP A 73 ? 0.1898 0.1984 0.2218 0.0058 0.0207 -0.0110 114 ASP A N 518 C CA . ASP A 73 ? 0.1994 0.2090 0.2346 0.0036 0.0193 -0.0144 114 ASP A CA 519 C C . ASP A 73 ? 0.2025 0.2135 0.2316 0.0023 0.0167 -0.0167 114 ASP A C 520 O O . ASP A 73 ? 0.1972 0.2091 0.2242 0.0015 0.0150 -0.0169 114 ASP A O 521 C CB . ASP A 73 ? 0.2112 0.2212 0.2537 0.0024 0.0188 -0.0149 114 ASP A CB 522 C CG . ASP A 73 ? 0.2522 0.2608 0.3017 0.0037 0.0219 -0.0124 114 ASP A CG 523 O OD1 . ASP A 73 ? 0.2562 0.2635 0.3073 0.0045 0.0235 -0.0123 114 ASP A OD1 524 O OD2 . ASP A 73 ? 0.3069 0.3155 0.3602 0.0040 0.0226 -0.0105 114 ASP A OD2 525 N N . VAL A 74 ? 0.1954 0.2065 0.2218 0.0022 0.0166 -0.0182 115 VAL A N 526 C CA . VAL A 74 ? 0.1927 0.2049 0.2130 0.0013 0.0149 -0.0198 115 VAL A CA 527 C C . VAL A 74 ? 0.1996 0.2125 0.2203 -0.0002 0.0141 -0.0232 115 VAL A C 528 O O . VAL A 74 ? 0.1956 0.2079 0.2208 -0.0002 0.0149 -0.0242 115 VAL A O 529 C CB . VAL A 74 ? 0.1865 0.1982 0.2025 0.0028 0.0157 -0.0186 115 VAL A CB 530 C CG1 . VAL A 74 ? 0.1872 0.1979 0.2017 0.0047 0.0164 -0.0154 115 VAL A CG1 531 C CG2 . VAL A 74 ? 0.1987 0.2097 0.2169 0.0037 0.0172 -0.0190 115 VAL A CG2 532 N N . LEU A 75 ? 0.1800 0.1938 0.1957 -0.0013 0.0126 -0.0248 116 LEU A N 533 C CA . LEU A 75 ? 0.1724 0.1866 0.1875 -0.0024 0.0120 -0.0279 116 LEU A CA 534 C C . LEU A 75 ? 0.1759 0.1900 0.1906 -0.0018 0.0135 -0.0284 116 LEU A C 535 O O . LEU A 75 ? 0.1932 0.2076 0.2045 -0.0012 0.0140 -0.0274 116 LEU A O 536 C CB . LEU A 75 ? 0.1728 0.1877 0.1823 -0.0034 0.0103 -0.0292 116 LEU A CB 537 C CG . LEU A 75 ? 0.1938 0.2087 0.2020 -0.0042 0.0097 -0.0325 116 LEU A CG 538 C CD1 . LEU A 75 ? 0.2129 0.2274 0.2250 -0.0047 0.0079 -0.0343 116 LEU A CD1 539 C CD2 . LEU A 75 ? 0.2175 0.2327 0.2189 -0.0048 0.0089 -0.0331 116 LEU A CD2 540 N N . LEU A 76 ? 0.1809 0.1945 0.1999 -0.0018 0.0142 -0.0300 117 LEU A N 541 C CA . LEU A 76 ? 0.1859 0.1994 0.2050 -0.0013 0.0155 -0.0309 117 LEU A CA 542 C C . LEU A 76 ? 0.1982 0.2120 0.2167 -0.0023 0.0150 -0.0343 117 LEU A C 543 O O . LEU A 76 ? 0.2150 0.2289 0.2321 -0.0033 0.0134 -0.0360 117 LEU A O 544 C CB . LEU A 76 ? 0.1952 0.2076 0.2192 0.0001 0.0171 -0.0295 117 LEU A CB 545 C CG . LEU A 76 ? 0.1842 0.1958 0.2084 0.0017 0.0180 -0.0260 117 LEU A CG 546 C CD1 . LEU A 76 ? 0.2008 0.2108 0.2290 0.0033 0.0198 -0.0247 117 LEU A CD1 547 C CD2 . LEU A 76 ? 0.2025 0.2146 0.2213 0.0023 0.0176 -0.0250 117 LEU A CD2 548 N N . SER A 77 ? 0.1993 0.2132 0.2181 -0.0019 0.0162 -0.0355 118 SER A N 549 C CA . SER A 77 ? 0.2163 0.2304 0.2336 -0.0027 0.0160 -0.0388 118 SER A CA 550 C C . SER A 77 ? 0.2212 0.2348 0.2425 -0.0021 0.0173 -0.0399 118 SER A C 551 O O . SER A 77 ? 0.2147 0.2284 0.2371 -0.0011 0.0186 -0.0384 118 SER A O 552 C CB . SER A 77 ? 0.2327 0.2478 0.2443 -0.0030 0.0164 -0.0390 118 SER A CB 553 O OG . SER A 77 ? 0.2399 0.2550 0.2500 -0.0032 0.0170 -0.0419 118 SER A OG 554 N N . TYR A 78 ? 0.2042 0.2171 0.2275 -0.0024 0.0168 -0.0428 119 TYR A N 555 C CA . TYR A 78 ? 0.2222 0.2345 0.2497 -0.0018 0.0181 -0.0441 119 TYR A CA 556 C C . TYR A 78 ? 0.2360 0.2480 0.2623 -0.0022 0.0177 -0.0478 119 TYR A C 557 O O . TYR A 78 ? 0.2468 0.2585 0.2708 -0.0028 0.0160 -0.0497 119 TYR A O 558 C CB . TYR A 78 ? 0.2145 0.2256 0.2486 -0.0016 0.0180 -0.0433 119 TYR A CB 559 C CG . TYR A 78 ? 0.2303 0.2411 0.2662 -0.0008 0.0187 -0.0396 119 TYR A CG 560 C CD1 . TYR A 78 ? 0.2270 0.2376 0.2632 0.0005 0.0203 -0.0374 119 TYR A CD1 561 C CD2 . TYR A 78 ? 0.2336 0.2442 0.2711 -0.0013 0.0176 -0.0383 119 TYR A CD2 562 C CE1 . TYR A 78 ? 0.2122 0.2220 0.2493 0.0017 0.0209 -0.0339 119 TYR A CE1 563 C CE2 . TYR A 78 ? 0.2554 0.2655 0.2944 -0.0003 0.0186 -0.0347 119 TYR A CE2 564 C CZ . TYR A 78 ? 0.2184 0.2279 0.2569 0.0012 0.0203 -0.0326 119 TYR A CZ 565 O OH . TYR A 78 ? 0.2255 0.2341 0.2648 0.0026 0.0213 -0.0291 119 TYR A OH 566 N N . PRO A 79 ? 0.2520 0.2640 0.2795 -0.0016 0.0192 -0.0491 120 PRO A N 567 C CA . PRO A 79 ? 0.2644 0.2758 0.2909 -0.0018 0.0189 -0.0528 120 PRO A CA 568 C C . PRO A 79 ? 0.2718 0.2817 0.3031 -0.0020 0.0173 -0.0547 120 PRO A C 569 O O . PRO A 79 ? 0.2759 0.2853 0.3128 -0.0020 0.0172 -0.0529 120 PRO A O 570 C CB . PRO A 79 ? 0.2753 0.2869 0.3036 -0.0010 0.0210 -0.0534 120 PRO A CB 571 C CG . PRO A 79 ? 0.2833 0.2960 0.3117 -0.0005 0.0222 -0.0502 120 PRO A CG 572 C CD . PRO A 79 ? 0.2555 0.2679 0.2849 -0.0007 0.0210 -0.0474 120 PRO A CD 573 N N . ASN A 80 ? 0.2819 0.2910 0.3112 -0.0020 0.0161 -0.0583 121 ASN A N 574 C CA . ASN A 80 ? 0.3183 0.3259 0.3528 -0.0022 0.0142 -0.0608 121 ASN A CA 575 C C . ASN A 80 ? 0.3306 0.3374 0.3698 -0.0016 0.0156 -0.0623 121 ASN A C 576 O O . ASN A 80 ? 0.3199 0.3267 0.3558 -0.0010 0.0166 -0.0643 121 ASN A O 577 C CB . ASN A 80 ? 0.3135 0.3203 0.3430 -0.0022 0.0118 -0.0643 121 ASN A CB 578 C CG . ASN A 80 ? 0.3738 0.3791 0.4089 -0.0023 0.0092 -0.0673 121 ASN A CG 579 O OD1 . ASN A 80 ? 0.3786 0.3832 0.4207 -0.0022 0.0099 -0.0677 121 ASN A OD1 580 N ND2 . ASN A 80 ? 0.3750 0.3796 0.4075 -0.0024 0.0062 -0.0693 121 ASN A ND2 581 N N . LYS A 81 ? 0.3591 0.3652 0.4060 -0.0016 0.0159 -0.0609 122 LYS A N 582 C CA . LYS A 81 ? 0.3934 0.3986 0.4454 -0.0009 0.0175 -0.0617 122 LYS A CA 583 C C . LYS A 81 ? 0.4066 0.4106 0.4590 -0.0006 0.0164 -0.0663 122 LYS A C 584 O O . LYS A 81 ? 0.4241 0.4277 0.4775 0.0001 0.0179 -0.0676 122 LYS A O 585 C CB . LYS A 81 ? 0.4026 0.4068 0.4628 -0.0009 0.0179 -0.0594 122 LYS A CB 586 C CG . LYS A 81 ? 0.4569 0.4617 0.5171 -0.0003 0.0199 -0.0548 122 LYS A CG 587 C CD . LYS A 81 ? 0.5355 0.5392 0.6027 -0.0002 0.0204 -0.0521 122 LYS A CD 588 C CE . LYS A 81 ? 0.5831 0.5875 0.6480 0.0004 0.0216 -0.0476 122 LYS A CE 589 N NZ . LYS A 81 ? 0.6281 0.6310 0.6996 0.0008 0.0227 -0.0446 122 LYS A NZ 590 N N . THR A 82 ? 0.4111 0.4143 0.4622 -0.0011 0.0136 -0.0691 123 THR A N 591 C CA . THR A 82 ? 0.4203 0.4220 0.4715 -0.0006 0.0121 -0.0739 123 THR A CA 592 C C . THR A 82 ? 0.4256 0.4273 0.4671 0.0000 0.0113 -0.0765 123 THR A C 593 O O . THR A 82 ? 0.4441 0.4442 0.4839 0.0007 0.0096 -0.0808 123 THR A O 594 C CB . THR A 82 ? 0.4304 0.4306 0.4887 -0.0011 0.0091 -0.0759 123 THR A CB 595 O OG1 . THR A 82 ? 0.4525 0.4532 0.5080 -0.0017 0.0068 -0.0755 123 THR A OG1 596 C CG2 . THR A 82 ? 0.4385 0.4383 0.5065 -0.0015 0.0105 -0.0730 123 THR A CG2 597 N N . HIS A 83 ? 0.4078 0.4110 0.4427 -0.0001 0.0128 -0.0741 124 HIS A N 598 C CA . HIS A 83 ? 0.4012 0.4043 0.4269 0.0006 0.0128 -0.0759 124 HIS A CA 599 C C . HIS A 83 ? 0.3881 0.3931 0.4097 0.0006 0.0160 -0.0728 124 HIS A C 600 O O . HIS A 83 ? 0.3789 0.3850 0.3964 0.0001 0.0161 -0.0703 124 HIS A O 601 C CB . HIS A 83 ? 0.4081 0.4108 0.4300 0.0003 0.0097 -0.0765 124 HIS A CB 602 C CG . HIS A 83 ? 0.4714 0.4730 0.4836 0.0014 0.0091 -0.0791 124 HIS A CG 603 N ND1 . HIS A 83 ? 0.5244 0.5254 0.5314 0.0015 0.0063 -0.0798 124 HIS A ND1 604 C CD2 . HIS A 83 ? 0.5462 0.5471 0.5528 0.0027 0.0109 -0.0812 124 HIS A CD2 605 C CE1 . HIS A 83 ? 0.5601 0.5598 0.5582 0.0029 0.0065 -0.0821 124 HIS A CE1 606 N NE2 . HIS A 83 ? 0.5667 0.5663 0.5643 0.0036 0.0095 -0.0829 124 HIS A NE2 607 N N . PRO A 84 ? 0.3785 0.3838 0.4018 0.0012 0.0187 -0.0729 125 PRO A N 608 C CA . PRO A 84 ? 0.3687 0.3760 0.3910 0.0012 0.0216 -0.0699 125 PRO A CA 609 C C . PRO A 84 ? 0.3596 0.3677 0.3738 0.0014 0.0229 -0.0695 125 PRO A C 610 O O . PRO A 84 ? 0.3630 0.3699 0.3714 0.0021 0.0226 -0.0722 125 PRO A O 611 C CB . PRO A 84 ? 0.3866 0.3937 0.4127 0.0021 0.0236 -0.0713 125 PRO A CB 612 C CG . PRO A 84 ? 0.3885 0.3936 0.4195 0.0022 0.0216 -0.0742 125 PRO A CG 613 C CD . PRO A 84 ? 0.3991 0.4031 0.4264 0.0020 0.0187 -0.0761 125 PRO A CD 614 N N . ASN A 85 ? 0.3215 0.3314 0.3353 0.0009 0.0243 -0.0660 126 ASN A N 615 C CA . ASN A 85 ? 0.3147 0.3254 0.3221 0.0010 0.0260 -0.0651 126 ASN A CA 616 C C . ASN A 85 ? 0.3154 0.3267 0.3228 0.0018 0.0291 -0.0662 126 ASN A C 617 O O . ASN A 85 ? 0.3170 0.3291 0.3303 0.0020 0.0301 -0.0657 126 ASN A O 618 C CB . ASN A 85 ? 0.2972 0.3097 0.3054 0.0001 0.0262 -0.0611 126 ASN A CB 619 C CG . ASN A 85 ? 0.3094 0.3215 0.3175 -0.0006 0.0235 -0.0598 126 ASN A CG 620 O OD1 . ASN A 85 ? 0.2789 0.2897 0.2839 -0.0006 0.0215 -0.0617 126 ASN A OD1 621 N ND2 . ASN A 85 ? 0.2544 0.2675 0.2661 -0.0011 0.0232 -0.0567 126 ASN A ND2 622 N N . TYR A 86 ? 0.3277 0.3386 0.3287 0.0025 0.0308 -0.0674 127 TYR A N 623 C CA . TYR A 86 ? 0.3309 0.3426 0.3320 0.0032 0.0344 -0.0679 127 TYR A CA 624 C C . TYR A 86 ? 0.3276 0.3389 0.3208 0.0038 0.0365 -0.0680 127 TYR A C 625 O O . TYR A 86 ? 0.3351 0.3451 0.3222 0.0038 0.0349 -0.0681 127 TYR A O 626 C CB . TYR A 86 ? 0.3495 0.3601 0.3537 0.0043 0.0348 -0.0712 127 TYR A CB 627 C CG . TYR A 86 ? 0.3731 0.3811 0.3713 0.0054 0.0337 -0.0749 127 TYR A CG 628 C CD1 . TYR A 86 ? 0.4267 0.4338 0.4205 0.0069 0.0364 -0.0771 127 TYR A CD1 629 C CD2 . TYR A 86 ? 0.3915 0.3978 0.3889 0.0052 0.0299 -0.0762 127 TYR A CD2 630 C CE1 . TYR A 86 ? 0.4114 0.4158 0.3992 0.0083 0.0352 -0.0806 127 TYR A CE1 631 C CE2 . TYR A 86 ? 0.4180 0.4218 0.4100 0.0064 0.0284 -0.0800 127 TYR A CE2 632 C CZ . TYR A 86 ? 0.4152 0.4179 0.4020 0.0081 0.0310 -0.0822 127 TYR A CZ 633 O OH . TYR A 86 ? 0.4169 0.4168 0.3975 0.0098 0.0294 -0.0861 127 TYR A OH 634 N N . ILE A 87 ? 0.3225 0.3348 0.3163 0.0044 0.0402 -0.0677 128 ILE A N 635 C CA . ILE A 87 ? 0.3127 0.3246 0.2996 0.0051 0.0432 -0.0675 128 ILE A CA 636 C C . ILE A 87 ? 0.3282 0.3391 0.3139 0.0068 0.0459 -0.0704 128 ILE A C 637 O O . ILE A 87 ? 0.3252 0.3370 0.3174 0.0070 0.0467 -0.0713 128 ILE A O 638 C CB . ILE A 87 ? 0.3159 0.3302 0.3054 0.0043 0.0457 -0.0641 128 ILE A CB 639 C CG1 . ILE A 87 ? 0.2953 0.3105 0.2860 0.0027 0.0429 -0.0613 128 ILE A CG1 640 C CG2 . ILE A 87 ? 0.3234 0.3371 0.3065 0.0051 0.0495 -0.0636 128 ILE A CG2 641 C CD1 . ILE A 87 ? 0.3055 0.3232 0.3014 0.0019 0.0446 -0.0584 128 ILE A CD1 642 N N . SER A 88 ? 0.3465 0.3553 0.3236 0.0082 0.0473 -0.0718 129 SER A N 643 C CA . SER A 88 ? 0.3631 0.3705 0.3373 0.0102 0.0504 -0.0745 129 SER A CA 644 C C . SER A 88 ? 0.3766 0.3838 0.3453 0.0112 0.0551 -0.0731 129 SER A C 645 O O . SER A 88 ? 0.3679 0.3749 0.3319 0.0108 0.0555 -0.0707 129 SER A O 646 C CB . SER A 88 ? 0.3608 0.3648 0.3287 0.0118 0.0476 -0.0784 129 SER A CB 647 O OG . SER A 88 ? 0.4047 0.4086 0.3783 0.0109 0.0435 -0.0799 129 SER A OG 648 N N . ILE A 89 ? 0.3920 0.3990 0.3611 0.0127 0.0590 -0.0746 130 ILE A N 649 C CA . ILE A 89 ? 0.4079 0.4134 0.3692 0.0145 0.0635 -0.0743 130 ILE A CA 650 C C . ILE A 89 ? 0.4288 0.4305 0.3819 0.0170 0.0621 -0.0785 130 ILE A C 651 O O . ILE A 89 ? 0.4044 0.4057 0.3611 0.0175 0.0604 -0.0816 130 ILE A O 652 C CB . ILE A 89 ? 0.4155 0.4229 0.3820 0.0150 0.0691 -0.0735 130 ILE A CB 653 C CG1 . ILE A 89 ? 0.3932 0.4042 0.3681 0.0128 0.0703 -0.0696 130 ILE A CG1 654 C CG2 . ILE A 89 ? 0.4036 0.4085 0.3608 0.0175 0.0741 -0.0737 130 ILE A CG2 655 C CD1 . ILE A 89 ? 0.4073 0.4207 0.3897 0.0130 0.0752 -0.0690 130 ILE A CD1 656 N N . ILE A 90 ? 0.4673 0.4662 0.4095 0.0186 0.0624 -0.0786 131 ILE A N 657 C CA . ILE A 90 ? 0.5157 0.5105 0.4488 0.0213 0.0607 -0.0827 131 ILE A CA 658 C C . ILE A 90 ? 0.5430 0.5355 0.4670 0.0242 0.0662 -0.0828 131 ILE A C 659 O O . ILE A 90 ? 0.5401 0.5332 0.4618 0.0241 0.0703 -0.0793 131 ILE A O 660 C CB . ILE A 90 ? 0.5209 0.5136 0.4476 0.0212 0.0553 -0.0834 131 ILE A CB 661 C CG1 . ILE A 90 ? 0.5344 0.5275 0.4567 0.0205 0.0567 -0.0793 131 ILE A CG1 662 C CG2 . ILE A 90 ? 0.5294 0.5239 0.4650 0.0188 0.0500 -0.0839 131 ILE A CG2 663 C CD1 . ILE A 90 ? 0.6054 0.5959 0.5197 0.0211 0.0521 -0.0800 131 ILE A CD1 664 N N . ASN A 91 ? 0.5730 0.5625 0.4918 0.0270 0.0665 -0.0868 132 ASN A N 665 C CA . ASN A 91 ? 0.6083 0.5948 0.5167 0.0304 0.0716 -0.0871 132 ASN A CA 666 C C . ASN A 91 ? 0.6420 0.6240 0.5365 0.0329 0.0692 -0.0884 132 ASN A C 667 O O . ASN A 91 ? 0.6435 0.6249 0.5371 0.0319 0.0632 -0.0893 132 ASN A O 668 C CB . ASN A 91 ? 0.6125 0.5979 0.5216 0.0326 0.0741 -0.0906 132 ASN A CB 669 C CG . ASN A 91 ? 0.5949 0.5779 0.5026 0.0338 0.0684 -0.0958 132 ASN A CG 670 O OD1 . ASN A 91 ? 0.6061 0.5867 0.5077 0.0342 0.0633 -0.0975 132 ASN A OD1 671 N ND2 . ASN A 91 ? 0.6066 0.5902 0.5205 0.0342 0.0692 -0.0984 132 ASN A ND2 672 N N . GLU A 92 ? 0.6791 0.6578 0.5626 0.0364 0.0738 -0.0886 133 GLU A N 673 C CA . GLU A 92 ? 0.7211 0.6948 0.5895 0.0396 0.0721 -0.0899 133 GLU A CA 674 C C . GLU A 92 ? 0.7309 0.7018 0.5954 0.0409 0.0647 -0.0950 133 GLU A C 675 O O . GLU A 92 ? 0.7417 0.7097 0.5972 0.0421 0.0609 -0.0956 133 GLU A O 676 C CB . GLU A 92 ? 0.7386 0.7087 0.5961 0.0439 0.0784 -0.0903 133 GLU A CB 677 C CG . GLU A 92 ? 0.7733 0.7461 0.6374 0.0434 0.0863 -0.0874 133 GLU A CG 678 C CD . GLU A 92 ? 0.8196 0.7884 0.6714 0.0477 0.0931 -0.0866 133 GLU A CD 679 O OE1 . GLU A 92 ? 0.8499 0.8178 0.7014 0.0500 0.0971 -0.0886 133 GLU A OE1 680 O OE2 . GLU A 92 ? 0.8391 0.8055 0.6815 0.0490 0.0946 -0.0839 133 GLU A OE2 681 N N . ASP A 93 ? 0.7361 0.7076 0.6073 0.0406 0.0627 -0.0987 134 ASP A N 682 C CA . ASP A 93 ? 0.7503 0.7193 0.6201 0.0416 0.0556 -0.1039 134 ASP A CA 683 C C . ASP A 93 ? 0.7377 0.7095 0.6167 0.0378 0.0496 -0.1032 134 ASP A C 684 O O . ASP A 93 ? 0.7481 0.7180 0.6260 0.0382 0.0432 -0.1067 134 ASP A O 685 C CB . ASP A 93 ? 0.7567 0.7255 0.6314 0.0426 0.0561 -0.1079 134 ASP A CB 686 C CG . ASP A 93 ? 0.7987 0.7643 0.6636 0.0468 0.0617 -0.1092 134 ASP A CG 687 O OD1 . ASP A 93 ? 0.8344 0.7955 0.6852 0.0503 0.0619 -0.1100 134 ASP A OD1 688 O OD2 . ASP A 93 ? 0.8273 0.7945 0.6983 0.0468 0.0660 -0.1093 134 ASP A OD2 689 N N . GLY A 94 ? 0.7131 0.6893 0.6015 0.0343 0.0516 -0.0986 135 GLY A N 690 C CA . GLY A 94 ? 0.6919 0.6711 0.5901 0.0308 0.0467 -0.0977 135 GLY A CA 691 C C . GLY A 94 ? 0.6699 0.6513 0.5801 0.0291 0.0454 -0.0995 135 GLY A C 692 O O . GLY A 94 ? 0.6746 0.6569 0.5917 0.0271 0.0403 -0.1005 135 GLY A O 693 N N . ASN A 95 ? 0.6462 0.6282 0.5591 0.0299 0.0500 -0.1000 136 ASN A N 694 C CA . ASN A 95 ? 0.6158 0.6004 0.5411 0.0281 0.0495 -0.1009 136 ASN A CA 695 C C . ASN A 95 ? 0.5783 0.5675 0.5133 0.0249 0.0519 -0.0961 136 ASN A C 696 O O . ASN A 95 ? 0.5641 0.5546 0.4976 0.0249 0.0568 -0.0928 136 ASN A O 697 C CB . ASN A 95 ? 0.6288 0.6122 0.5534 0.0305 0.0531 -0.1037 136 ASN A CB 698 C CG . ASN A 95 ? 0.6770 0.6554 0.5913 0.0341 0.0506 -0.1089 136 ASN A CG 699 O OD1 . ASN A 95 ? 0.7347 0.7107 0.6412 0.0373 0.0546 -0.1103 136 ASN A OD1 700 N ND2 . ASN A 95 ? 0.7022 0.6789 0.6166 0.0338 0.0441 -0.1117 136 ASN A ND2 701 N N . GLU A 96 ? 0.5423 0.5337 0.4874 0.0224 0.0484 -0.0956 137 GLU A N 702 C CA . GLU A 96 ? 0.5060 0.5015 0.4603 0.0196 0.0500 -0.0913 137 GLU A CA 703 C C . GLU A 96 ? 0.4837 0.4811 0.4453 0.0197 0.0536 -0.0915 137 GLU A C 704 O O . GLU A 96 ? 0.4930 0.4906 0.4613 0.0194 0.0517 -0.0936 137 GLU A O 705 C CB . GLU A 96 ? 0.4984 0.4952 0.4594 0.0171 0.0450 -0.0904 137 GLU A CB 706 C CG . GLU A 96 ? 0.4864 0.4816 0.4403 0.0170 0.0417 -0.0899 137 GLU A CG 707 C CD . GLU A 96 ? 0.4685 0.4651 0.4287 0.0147 0.0372 -0.0887 137 GLU A CD 708 O OE1 . GLU A 96 ? 0.4494 0.4472 0.4188 0.0135 0.0358 -0.0891 137 GLU A OE1 709 O OE2 . GLU A 96 ? 0.4741 0.4701 0.4297 0.0142 0.0351 -0.0874 137 GLU A OE2 710 N N . ILE A 97 ? 0.4715 0.4702 0.4322 0.0201 0.0590 -0.0893 138 ILE A N 711 C CA . ILE A 97 ? 0.4609 0.4613 0.4280 0.0206 0.0629 -0.0896 138 ILE A CA 712 C C . ILE A 97 ? 0.4470 0.4514 0.4258 0.0182 0.0633 -0.0867 138 ILE A C 713 O O . ILE A 97 ? 0.4369 0.4428 0.4223 0.0185 0.0657 -0.0872 138 ILE A O 714 C CB . ILE A 97 ? 0.4753 0.4749 0.4363 0.0228 0.0690 -0.0892 138 ILE A CB 715 C CG1 . ILE A 97 ? 0.4447 0.4462 0.4048 0.0216 0.0720 -0.0847 138 ILE A CG1 716 C CG2 . ILE A 97 ? 0.4929 0.4879 0.4419 0.0260 0.0686 -0.0929 138 ILE A CG2 717 C CD1 . ILE A 97 ? 0.4795 0.4807 0.4360 0.0235 0.0789 -0.0836 138 ILE A CD1 718 N N . PHE A 98 ? 0.4242 0.4302 0.4053 0.0161 0.0607 -0.0838 139 PHE A N 719 C CA . PHE A 98 ? 0.4032 0.4125 0.3946 0.0141 0.0603 -0.0813 139 PHE A CA 720 C C . PHE A 98 ? 0.3872 0.3966 0.3791 0.0123 0.0557 -0.0797 139 PHE A C 721 O O . PHE A 98 ? 0.3694 0.3777 0.3543 0.0122 0.0549 -0.0788 139 PHE A O 722 C CB . PHE A 98 ? 0.4064 0.4183 0.4001 0.0135 0.0645 -0.0780 139 PHE A CB 723 C CG . PHE A 98 ? 0.4164 0.4313 0.4189 0.0114 0.0629 -0.0750 139 PHE A CG 724 C CD1 . PHE A 98 ? 0.4206 0.4371 0.4323 0.0112 0.0622 -0.0755 139 PHE A CD1 725 C CD2 . PHE A 98 ? 0.4049 0.4208 0.4061 0.0099 0.0618 -0.0719 139 PHE A CD2 726 C CE1 . PHE A 98 ? 0.4296 0.4485 0.4485 0.0096 0.0604 -0.0729 139 PHE A CE1 727 C CE2 . PHE A 98 ? 0.3975 0.4159 0.4063 0.0083 0.0601 -0.0694 139 PHE A CE2 728 C CZ . PHE A 98 ? 0.3864 0.4062 0.4038 0.0083 0.0593 -0.0700 139 PHE A CZ 729 N N . ASN A 99 ? 0.3790 0.3896 0.3788 0.0111 0.0530 -0.0793 140 ASN A N 730 C CA . ASN A 99 ? 0.3776 0.3885 0.3791 0.0095 0.0490 -0.0775 140 ASN A CA 731 C C . ASN A 99 ? 0.3614 0.3750 0.3709 0.0081 0.0490 -0.0745 140 ASN A C 732 O O . ASN A 99 ? 0.3564 0.3712 0.3726 0.0085 0.0500 -0.0750 140 ASN A O 733 C CB . ASN A 99 ? 0.3915 0.4005 0.3948 0.0096 0.0453 -0.0801 140 ASN A CB 734 C CG . ASN A 99 ? 0.4149 0.4208 0.4102 0.0109 0.0440 -0.0835 140 ASN A CG 735 O OD1 . ASN A 99 ? 0.4259 0.4310 0.4133 0.0114 0.0447 -0.0831 140 ASN A OD1 736 N ND2 . ASN A 99 ? 0.4717 0.4758 0.4692 0.0117 0.0420 -0.0868 140 ASN A ND2 737 N N . THR A 100 ? 0.3415 0.3562 0.3505 0.0068 0.0475 -0.0716 141 THR A N 738 C CA . THR A 100 ? 0.3161 0.3330 0.3323 0.0058 0.0468 -0.0689 141 THR A CA 739 C C . THR A 100 ? 0.3125 0.3287 0.3337 0.0057 0.0438 -0.0695 141 THR A C 740 O O . THR A 100 ? 0.3208 0.3349 0.3400 0.0059 0.0417 -0.0715 141 THR A O 741 C CB . THR A 100 ? 0.3046 0.3226 0.3189 0.0046 0.0460 -0.0657 141 THR A CB 742 O OG1 . THR A 100 ? 0.3102 0.3266 0.3201 0.0041 0.0429 -0.0658 141 THR A OG1 743 C CG2 . THR A 100 ? 0.3152 0.3339 0.3255 0.0047 0.0494 -0.0648 141 THR A CG2 744 N N . SER A 101 ? 0.3053 0.3231 0.3331 0.0054 0.0433 -0.0675 142 SER A N 745 C CA . SER A 101 ? 0.2935 0.3105 0.3264 0.0056 0.0411 -0.0676 142 SER A CA 746 C C . SER A 101 ? 0.2927 0.3082 0.3239 0.0048 0.0380 -0.0668 142 SER A C 747 O O . SER A 101 ? 0.3117 0.3276 0.3389 0.0039 0.0371 -0.0650 142 SER A O 748 C CB . SER A 101 ? 0.3093 0.3280 0.3485 0.0058 0.0412 -0.0654 142 SER A CB 749 O OG A SER A 101 ? 0.3503 0.3678 0.3941 0.0064 0.0397 -0.0657 142 SER A OG 750 O OG B SER A 101 ? 0.2407 0.2601 0.2793 0.0050 0.0395 -0.0624 142 SER A OG 751 N N . LEU A 102 ? 0.3002 0.3142 0.3349 0.0050 0.0363 -0.0678 143 LEU A N 752 C CA . LEU A 102 ? 0.3076 0.3205 0.3422 0.0042 0.0336 -0.0666 143 LEU A CA 753 C C . LEU A 102 ? 0.3123 0.3257 0.3514 0.0041 0.0327 -0.0633 143 LEU A C 754 O O . LEU A 102 ? 0.2997 0.3124 0.3387 0.0035 0.0309 -0.0618 143 LEU A O 755 C CB . LEU A 102 ? 0.3371 0.3477 0.3732 0.0044 0.0321 -0.0695 143 LEU A CB 756 C CG . LEU A 102 ? 0.3584 0.3680 0.3890 0.0049 0.0325 -0.0731 143 LEU A CG 757 C CD1 . LEU A 102 ? 0.4145 0.4217 0.4473 0.0051 0.0305 -0.0761 143 LEU A CD1 758 C CD2 . LEU A 102 ? 0.3899 0.3997 0.4130 0.0043 0.0320 -0.0724 143 LEU A CD2 759 N N . PHE A 103 ? 0.3025 0.3171 0.3452 0.0049 0.0340 -0.0623 144 PHE A N 760 C CA . PHE A 103 ? 0.3007 0.3155 0.3471 0.0054 0.0332 -0.0593 144 PHE A CA 761 C C . PHE A 103 ? 0.2934 0.3097 0.3426 0.0064 0.0345 -0.0588 144 PHE A C 762 O O . PHE A 103 ? 0.3048 0.3218 0.3549 0.0068 0.0363 -0.0609 144 PHE A O 763 C CB . PHE A 103 ? 0.3219 0.3345 0.3726 0.0059 0.0322 -0.0593 144 PHE A CB 764 C CG . PHE A 103 ? 0.3707 0.3824 0.4251 0.0068 0.0332 -0.0619 144 PHE A CG 765 C CD1 . PHE A 103 ? 0.3920 0.4040 0.4508 0.0081 0.0340 -0.0613 144 PHE A CD1 766 C CD2 . PHE A 103 ? 0.4354 0.4461 0.4887 0.0064 0.0332 -0.0652 144 PHE A CD2 767 C CE1 . PHE A 103 ? 0.4593 0.4705 0.5216 0.0089 0.0350 -0.0636 144 PHE A CE1 768 C CE2 . PHE A 103 ? 0.4593 0.4690 0.5159 0.0072 0.0341 -0.0678 144 PHE A CE2 769 C CZ . PHE A 103 ? 0.4496 0.4597 0.5108 0.0084 0.0351 -0.0669 144 PHE A CZ 770 N N . GLU A 104 ? 0.2601 0.2769 0.3109 0.0070 0.0336 -0.0561 145 GLU A N 771 C CA . GLU A 104 ? 0.2675 0.2856 0.3218 0.0082 0.0343 -0.0557 145 GLU A CA 772 C C . GLU A 104 ? 0.2660 0.2826 0.3251 0.0096 0.0343 -0.0563 145 GLU A C 773 O O . GLU A 104 ? 0.2596 0.2743 0.3197 0.0101 0.0332 -0.0550 145 GLU A O 774 C CB . GLU A 104 ? 0.2799 0.2986 0.3340 0.0087 0.0328 -0.0528 145 GLU A CB 775 C CG . GLU A 104 ? 0.2563 0.2764 0.3065 0.0075 0.0326 -0.0518 145 GLU A CG 776 C CD . GLU A 104 ? 0.2322 0.2524 0.2823 0.0083 0.0308 -0.0491 145 GLU A CD 777 O OE1 . GLU A 104 ? 0.2539 0.2726 0.3021 0.0084 0.0295 -0.0474 145 GLU A OE1 778 O OE2 . GLU A 104 ? 0.2348 0.2566 0.2872 0.0089 0.0306 -0.0489 145 GLU A OE2 779 N N . PRO A 105 ? 0.2720 0.2896 0.3347 0.0105 0.0355 -0.0578 146 PRO A N 780 C CA . PRO A 105 ? 0.2739 0.2899 0.3412 0.0121 0.0354 -0.0581 146 PRO A CA 781 C C . PRO A 105 ? 0.2659 0.2808 0.3342 0.0135 0.0336 -0.0550 146 PRO A C 782 O O . PRO A 105 ? 0.2972 0.3134 0.3651 0.0141 0.0328 -0.0535 146 PRO A O 783 C CB . PRO A 105 ? 0.2894 0.3072 0.3602 0.0129 0.0368 -0.0598 146 PRO A CB 784 C CG . PRO A 105 ? 0.2980 0.3177 0.3657 0.0114 0.0386 -0.0614 146 PRO A CG 785 C CD . PRO A 105 ? 0.2968 0.3167 0.3598 0.0102 0.0373 -0.0593 146 PRO A CD 786 N N . PRO A 106 ? 0.2640 0.2763 0.3334 0.0141 0.0331 -0.0539 147 PRO A N 787 C CA . PRO A 106 ? 0.2792 0.2902 0.3483 0.0157 0.0317 -0.0507 147 PRO A CA 788 C C . PRO A 106 ? 0.2907 0.3017 0.3630 0.0181 0.0313 -0.0502 147 PRO A C 789 O O . PRO A 106 ? 0.2991 0.3103 0.3752 0.0187 0.0322 -0.0523 147 PRO A O 790 C CB . PRO A 106 ? 0.2874 0.2954 0.3575 0.0159 0.0319 -0.0497 147 PRO A CB 791 C CG . PRO A 106 ? 0.2789 0.2867 0.3516 0.0150 0.0330 -0.0528 147 PRO A CG 792 C CD . PRO A 106 ? 0.2798 0.2902 0.3501 0.0134 0.0336 -0.0552 147 PRO A CD 793 N N . PRO A 107 ? 0.2955 0.3060 0.3662 0.0197 0.0297 -0.0477 148 PRO A N 794 C CA . PRO A 107 ? 0.2993 0.3098 0.3728 0.0221 0.0287 -0.0475 148 PRO A CA 795 C C . PRO A 107 ? 0.2965 0.3040 0.3726 0.0243 0.0290 -0.0467 148 PRO A C 796 O O . PRO A 107 ? 0.2987 0.3038 0.3743 0.0241 0.0298 -0.0456 148 PRO A O 797 C CB . PRO A 107 ? 0.2912 0.3017 0.3614 0.0233 0.0266 -0.0452 148 PRO A CB 798 C CG . PRO A 107 ? 0.2900 0.2990 0.3559 0.0223 0.0268 -0.0431 148 PRO A CG 799 C CD . PRO A 107 ? 0.3049 0.3149 0.3711 0.0194 0.0286 -0.0452 148 PRO A CD 800 N N . PRO A 108 ? 0.3028 0.3102 0.3820 0.0265 0.0283 -0.0472 149 PRO A N 801 C CA . PRO A 108 ? 0.3075 0.3120 0.3894 0.0288 0.0286 -0.0465 149 PRO A CA 802 C C . PRO A 108 ? 0.3120 0.3128 0.3909 0.0303 0.0285 -0.0430 149 PRO A C 803 O O . PRO A 108 ? 0.3149 0.3148 0.3899 0.0318 0.0271 -0.0406 149 PRO A O 804 C CB . PRO A 108 ? 0.3096 0.3148 0.3940 0.0314 0.0269 -0.0470 149 PRO A CB 805 C CG . PRO A 108 ? 0.3077 0.3170 0.3934 0.0295 0.0269 -0.0494 149 PRO A CG 806 C CD . PRO A 108 ? 0.3042 0.3143 0.3851 0.0272 0.0269 -0.0483 149 PRO A CD 807 N N . GLY A 109 ? 0.3165 0.3149 0.3975 0.0301 0.0302 -0.0428 150 GLY A N 808 C CA . GLY A 109 ? 0.3395 0.3343 0.4190 0.0316 0.0307 -0.0394 150 GLY A CA 809 C C . GLY A 109 ? 0.3664 0.3612 0.4431 0.0294 0.0313 -0.0381 150 GLY A C 810 O O . GLY A 109 ? 0.3866 0.3784 0.4628 0.0303 0.0323 -0.0354 150 GLY A O 811 N N . TYR A 110 ? 0.3842 0.3822 0.4594 0.0267 0.0309 -0.0401 151 TYR A N 812 C CA . TYR A 110 ? 0.3979 0.3963 0.4706 0.0244 0.0313 -0.0394 151 TYR A CA 813 C C . TYR A 110 ? 0.4266 0.4263 0.5016 0.0215 0.0322 -0.0425 151 TYR A C 814 O O . TYR A 110 ? 0.4248 0.4254 0.4978 0.0194 0.0321 -0.0428 151 TYR A O 815 C CB . TYR A 110 ? 0.3888 0.3896 0.4571 0.0237 0.0298 -0.0392 151 TYR A CB 816 C CG . TYR A 110 ? 0.3386 0.3382 0.4035 0.0264 0.0284 -0.0364 151 TYR A CG 817 C CD1 . TYR A 110 ? 0.3231 0.3210 0.3844 0.0269 0.0284 -0.0334 151 TYR A CD1 818 C CD2 . TYR A 110 ? 0.2931 0.2934 0.3583 0.0285 0.0270 -0.0369 151 TYR A CD2 819 C CE1 . TYR A 110 ? 0.2999 0.2964 0.3573 0.0297 0.0271 -0.0310 151 TYR A CE1 820 C CE2 . TYR A 110 ? 0.2697 0.2686 0.3314 0.0312 0.0252 -0.0346 151 TYR A CE2 821 C CZ . TYR A 110 ? 0.2884 0.2854 0.3457 0.0318 0.0253 -0.0317 151 TYR A CZ 822 O OH . TYR A 110 ? 0.2809 0.2764 0.3342 0.0349 0.0235 -0.0296 151 TYR A OH 823 N N . GLU A 111 ? 0.4319 0.4317 0.5108 0.0215 0.0329 -0.0450 152 GLU A N 824 C CA . GLU A 111 ? 0.4537 0.4545 0.5342 0.0192 0.0335 -0.0483 152 GLU A CA 825 C C . GLU A 111 ? 0.4664 0.4649 0.5490 0.0182 0.0341 -0.0479 152 GLU A C 826 O O . GLU A 111 ? 0.4689 0.4680 0.5522 0.0162 0.0341 -0.0506 152 GLU A O 827 C CB . GLU A 111 ? 0.4632 0.4645 0.5474 0.0197 0.0342 -0.0512 152 GLU A CB 828 C CG . GLU A 111 ? 0.4584 0.4619 0.5422 0.0210 0.0337 -0.0517 152 GLU A CG 829 C CD . GLU A 111 ? 0.4826 0.4842 0.5683 0.0240 0.0332 -0.0496 152 GLU A CD 830 O OE1 . GLU A 111 ? 0.4836 0.4823 0.5691 0.0253 0.0332 -0.0467 152 GLU A OE1 831 O OE2 . GLU A 111 ? 0.4722 0.4751 0.5598 0.0253 0.0328 -0.0507 152 GLU A OE2 832 N N . ASN A 112 ? 0.4785 0.4743 0.5621 0.0196 0.0345 -0.0444 153 ASN A N 833 C CA . ASN A 112 ? 0.4874 0.4811 0.5741 0.0187 0.0352 -0.0436 153 ASN A CA 834 C C . ASN A 112 ? 0.4888 0.4821 0.5724 0.0183 0.0350 -0.0406 153 ASN A C 835 O O . ASN A 112 ? 0.4971 0.4888 0.5837 0.0176 0.0357 -0.0394 153 ASN A O 836 C CB . ASN A 112 ? 0.4916 0.4819 0.5833 0.0206 0.0366 -0.0420 153 ASN A CB 837 C CG . ASN A 112 ? 0.5013 0.4896 0.5982 0.0193 0.0374 -0.0422 153 ASN A CG 838 O OD1 . ASN A 112 ? 0.5015 0.4907 0.6006 0.0172 0.0368 -0.0458 153 ASN A OD1 839 N ND2 . ASN A 112 ? 0.5291 0.5144 0.6281 0.0206 0.0388 -0.0384 153 ASN A ND2 840 N N . VAL A 113 ? 0.4839 0.4789 0.5623 0.0188 0.0341 -0.0393 154 VAL A N 841 C CA . VAL A 113 ? 0.4656 0.4605 0.5408 0.0185 0.0338 -0.0367 154 VAL A CA 842 C C . VAL A 113 ? 0.4649 0.4614 0.5400 0.0155 0.0332 -0.0389 154 VAL A C 843 O O . VAL A 113 ? 0.4646 0.4634 0.5385 0.0140 0.0324 -0.0422 154 VAL A O 844 C CB . VAL A 113 ? 0.4781 0.4742 0.5476 0.0198 0.0327 -0.0350 154 VAL A CB 845 C CG1 . VAL A 113 ? 0.4513 0.4475 0.5174 0.0193 0.0324 -0.0326 154 VAL A CG1 846 C CG2 . VAL A 113 ? 0.4956 0.4894 0.5650 0.0232 0.0330 -0.0327 154 VAL A CG2 847 N N . SER A 114 ? 0.4498 0.4451 0.5264 0.0148 0.0336 -0.0372 155 SER A N 848 C CA . SER A 114 ? 0.4498 0.4466 0.5265 0.0122 0.0326 -0.0393 155 SER A CA 849 C C . SER A 114 ? 0.4227 0.4211 0.4938 0.0117 0.0317 -0.0377 155 SER A C 850 O O . SER A 114 ? 0.4091 0.4071 0.4770 0.0135 0.0319 -0.0347 155 SER A O 851 C CB . SER A 114 ? 0.4683 0.4630 0.5512 0.0115 0.0333 -0.0388 155 SER A CB 852 O OG . SER A 114 ? 0.5225 0.5152 0.6061 0.0132 0.0348 -0.0344 155 SER A OG 853 N N . ASP A 115 ? 0.3922 0.3922 0.4620 0.0095 0.0304 -0.0399 156 ASP A N 854 C CA . ASP A 115 ? 0.3644 0.3657 0.4298 0.0088 0.0295 -0.0385 156 ASP A CA 855 C C . ASP A 115 ? 0.3140 0.3172 0.3737 0.0093 0.0290 -0.0383 156 ASP A C 856 O O . ASP A 115 ? 0.3161 0.3198 0.3720 0.0095 0.0284 -0.0362 156 ASP A O 857 C CB . ASP A 115 ? 0.3742 0.3736 0.4408 0.0099 0.0305 -0.0345 156 ASP A CB 858 C CG . ASP A 115 ? 0.4514 0.4493 0.5246 0.0091 0.0311 -0.0344 156 ASP A CG 859 O OD1 . ASP A 115 ? 0.5178 0.5165 0.5930 0.0071 0.0299 -0.0375 156 ASP A OD1 860 O OD2 . ASP A 115 ? 0.5274 0.5230 0.6039 0.0106 0.0329 -0.0312 156 ASP A OD2 861 N N . ILE A 116 ? 0.2727 0.2768 0.3322 0.0095 0.0290 -0.0407 157 ILE A N 862 C CA . ILE A 116 ? 0.2388 0.2451 0.2937 0.0094 0.0284 -0.0411 157 ILE A CA 863 C C . ILE A 116 ? 0.2382 0.2463 0.2900 0.0072 0.0276 -0.0433 157 ILE A C 864 O O . ILE A 116 ? 0.2439 0.2522 0.2966 0.0061 0.0277 -0.0464 157 ILE A O 865 C CB . ILE A 116 ? 0.2278 0.2347 0.2841 0.0104 0.0290 -0.0427 157 ILE A CB 866 C CG1 . ILE A 116 ? 0.2436 0.2487 0.3021 0.0129 0.0295 -0.0403 157 ILE A CG1 867 C CG2 . ILE A 116 ? 0.2374 0.2469 0.2902 0.0098 0.0286 -0.0437 157 ILE A CG2 868 C CD1 . ILE A 116 ? 0.2341 0.2394 0.2954 0.0141 0.0300 -0.0420 157 ILE A CD1 869 N N . VAL A 117 ? 0.2255 0.2345 0.2732 0.0067 0.0268 -0.0418 158 VAL A N 870 C CA . VAL A 117 ? 0.2240 0.2344 0.2683 0.0048 0.0260 -0.0436 158 VAL A CA 871 C C . VAL A 117 ? 0.2300 0.2420 0.2724 0.0045 0.0266 -0.0460 158 VAL A C 872 O O . VAL A 117 ? 0.2215 0.2345 0.2633 0.0053 0.0270 -0.0452 158 VAL A O 873 C CB . VAL A 117 ? 0.2351 0.2461 0.2755 0.0044 0.0250 -0.0413 158 VAL A CB 874 C CG1 . VAL A 117 ? 0.2423 0.2547 0.2795 0.0050 0.0250 -0.0401 158 VAL A CG1 875 C CG2 . VAL A 117 ? 0.2451 0.2567 0.2828 0.0026 0.0241 -0.0431 158 VAL A CG2 876 N N . PRO A 118 ? 0.2345 0.2467 0.2760 0.0034 0.0267 -0.0490 159 PRO A N 877 C CA . PRO A 118 ? 0.2469 0.2606 0.2865 0.0033 0.0278 -0.0509 159 PRO A CA 878 C C . PRO A 118 ? 0.2376 0.2529 0.2726 0.0027 0.0278 -0.0497 159 PRO A C 879 O O . PRO A 118 ? 0.2385 0.2537 0.2709 0.0021 0.0266 -0.0481 159 PRO A O 880 C CB . PRO A 118 ? 0.2598 0.2728 0.2982 0.0026 0.0278 -0.0543 159 PRO A CB 881 C CG . PRO A 118 ? 0.2558 0.2676 0.2942 0.0018 0.0260 -0.0540 159 PRO A CG 882 C CD . PRO A 118 ? 0.2491 0.2601 0.2916 0.0025 0.0258 -0.0509 159 PRO A CD 883 N N . PRO A 119 ? 0.2364 0.2531 0.2708 0.0029 0.0291 -0.0505 160 PRO A N 884 C CA . PRO A 119 ? 0.2238 0.2420 0.2545 0.0022 0.0292 -0.0494 160 PRO A CA 885 C C . PRO A 119 ? 0.2256 0.2435 0.2511 0.0010 0.0287 -0.0500 160 PRO A C 886 O O . PRO A 119 ? 0.2286 0.2457 0.2526 0.0008 0.0290 -0.0524 160 PRO A O 887 C CB . PRO A 119 ? 0.2214 0.2411 0.2535 0.0026 0.0312 -0.0506 160 PRO A CB 888 C CG . PRO A 119 ? 0.2384 0.2576 0.2756 0.0038 0.0316 -0.0514 160 PRO A CG 889 C CD . PRO A 119 ? 0.2332 0.2504 0.2709 0.0037 0.0307 -0.0523 160 PRO A CD 890 N N . PHE A 120 ? 0.2088 0.2270 0.2316 0.0005 0.0276 -0.0478 161 PHE A N 891 C CA . PHE A 120 ? 0.2097 0.2277 0.2273 -0.0005 0.0270 -0.0481 161 PHE A CA 892 C C . PHE A 120 ? 0.2147 0.2336 0.2300 -0.0009 0.0265 -0.0456 161 PHE A C 893 O O . PHE A 120 ? 0.2134 0.2327 0.2313 -0.0003 0.0261 -0.0437 161 PHE A O 894 C CB . PHE A 120 ? 0.2219 0.2384 0.2393 -0.0008 0.0252 -0.0486 161 PHE A CB 895 C CG . PHE A 120 ? 0.2250 0.2412 0.2445 -0.0007 0.0237 -0.0459 161 PHE A CG 896 C CD1 . PHE A 120 ? 0.2030 0.2188 0.2196 -0.0014 0.0222 -0.0449 161 PHE A CD1 897 C CD2 . PHE A 120 ? 0.2259 0.2417 0.2497 0.0004 0.0240 -0.0444 161 PHE A CD2 898 C CE1 . PHE A 120 ? 0.2109 0.2263 0.2294 -0.0011 0.0211 -0.0424 161 PHE A CE1 899 C CE2 . PHE A 120 ? 0.1907 0.2059 0.2157 0.0008 0.0230 -0.0418 161 PHE A CE2 900 C CZ . PHE A 120 ? 0.1989 0.2139 0.2213 0.0000 0.0217 -0.0408 161 PHE A CZ 901 N N . SER A 121 ? 0.2139 0.2328 0.2241 -0.0017 0.0264 -0.0457 162 SER A N 902 C CA . SER A 121 ? 0.1968 0.2162 0.2047 -0.0022 0.0257 -0.0432 162 SER A CA 903 C C . SER A 121 ? 0.2111 0.2296 0.2174 -0.0025 0.0235 -0.0423 162 SER A C 904 O O . SER A 121 ? 0.2208 0.2385 0.2236 -0.0030 0.0228 -0.0434 162 SER A O 905 C CB . SER A 121 ? 0.2162 0.2361 0.2196 -0.0028 0.0272 -0.0435 162 SER A CB 906 O OG . SER A 121 ? 0.2255 0.2465 0.2312 -0.0025 0.0296 -0.0442 162 SER A OG 907 N N . ALA A 122 ? 0.1963 0.2148 0.2050 -0.0021 0.0224 -0.0402 163 ALA A N 908 C CA . ALA A 122 ? 0.1904 0.2080 0.1985 -0.0023 0.0206 -0.0392 163 ALA A CA 909 C C . ALA A 122 ? 0.2123 0.2299 0.2152 -0.0032 0.0198 -0.0386 163 ALA A C 910 O O . ALA A 122 ? 0.1907 0.2092 0.1915 -0.0034 0.0202 -0.0373 163 ALA A O 911 C CB . ALA A 122 ? 0.1941 0.2115 0.2050 -0.0013 0.0200 -0.0367 163 ALA A CB 912 N N . PHE A 123 ? 0.2074 0.2242 0.2090 -0.0036 0.0184 -0.0396 164 PHE A N 913 C CA . PHE A 123 ? 0.2040 0.2205 0.2009 -0.0042 0.0171 -0.0393 164 PHE A CA 914 C C . PHE A 123 ? 0.2183 0.2345 0.2102 -0.0045 0.0178 -0.0413 164 PHE A C 915 O O . PHE A 123 ? 0.2305 0.2462 0.2177 -0.0048 0.0167 -0.0411 164 PHE A O 916 C CB . PHE A 123 ? 0.1948 0.2118 0.1903 -0.0043 0.0165 -0.0366 164 PHE A CB 917 C CG . PHE A 123 ? 0.1828 0.1996 0.1822 -0.0038 0.0158 -0.0347 164 PHE A CG 918 C CD1 . PHE A 123 ? 0.1888 0.2051 0.1894 -0.0039 0.0142 -0.0344 164 PHE A CD1 919 C CD2 . PHE A 123 ? 0.1929 0.2101 0.1949 -0.0029 0.0166 -0.0332 164 PHE A CD2 920 C CE1 . PHE A 123 ? 0.1890 0.2049 0.1929 -0.0032 0.0140 -0.0324 164 PHE A CE1 921 C CE2 . PHE A 123 ? 0.1740 0.1906 0.1788 -0.0019 0.0161 -0.0313 164 PHE A CE2 922 C CZ . PHE A 123 ? 0.1873 0.2032 0.1930 -0.0021 0.0151 -0.0307 164 PHE A CZ 923 N N . SER A 124 ? 0.2179 0.2342 0.2104 -0.0042 0.0196 -0.0430 165 SER A N 924 C CA . SER A 124 ? 0.2367 0.2522 0.2240 -0.0040 0.0203 -0.0451 165 SER A CA 925 C C . SER A 124 ? 0.2450 0.2590 0.2297 -0.0039 0.0179 -0.0470 165 SER A C 926 O O . SER A 124 ? 0.2578 0.2715 0.2469 -0.0039 0.0163 -0.0479 165 SER A O 927 C CB . SER A 124 ? 0.2438 0.2593 0.2329 -0.0035 0.0223 -0.0472 165 SER A CB 928 O OG . SER A 124 ? 0.2494 0.2639 0.2325 -0.0030 0.0233 -0.0491 165 SER A OG 929 N N . PRO A 125 ? 0.2495 0.2626 0.2275 -0.0038 0.0175 -0.0475 166 PRO A N 930 C CA . PRO A 125 ? 0.2678 0.2793 0.2433 -0.0033 0.0149 -0.0501 166 PRO A CA 931 C C . PRO A 125 ? 0.2796 0.2900 0.2551 -0.0025 0.0156 -0.0534 166 PRO A C 932 O O . PRO A 125 ? 0.2724 0.2834 0.2486 -0.0022 0.0184 -0.0535 166 PRO A O 933 C CB . PRO A 125 ? 0.2840 0.2944 0.2513 -0.0030 0.0147 -0.0496 166 PRO A CB 934 C CG . PRO A 125 ? 0.2631 0.2742 0.2281 -0.0030 0.0184 -0.0481 166 PRO A CG 935 C CD . PRO A 125 ? 0.2567 0.2698 0.2292 -0.0038 0.0192 -0.0459 166 PRO A CD 936 N N . GLN A 126 ? 0.2908 0.2998 0.2657 -0.0020 0.0129 -0.0562 167 GLN A N 937 C CA . GLN A 126 ? 0.3089 0.3165 0.2830 -0.0010 0.0130 -0.0598 167 GLN A CA 938 C C . GLN A 126 ? 0.3253 0.3314 0.2901 0.0003 0.0142 -0.0610 167 GLN A C 939 O O . GLN A 126 ? 0.3354 0.3408 0.2940 0.0005 0.0136 -0.0598 167 GLN A O 940 C CB . GLN A 126 ? 0.3099 0.3163 0.2871 -0.0008 0.0092 -0.0625 167 GLN A CB 941 C CG . GLN A 126 ? 0.3431 0.3508 0.3299 -0.0019 0.0084 -0.0612 167 GLN A CG 942 C CD . GLN A 126 ? 0.4383 0.4450 0.4295 -0.0019 0.0048 -0.0636 167 GLN A CD 943 O OE1 . GLN A 126 ? 0.4771 0.4821 0.4640 -0.0011 0.0022 -0.0666 167 GLN A OE1 944 N NE2 . GLN A 126 ? 0.4016 0.4090 0.4015 -0.0027 0.0046 -0.0626 167 GLN A NE2 945 N N . GLY A 127 ? 0.3374 0.3426 0.3009 0.0013 0.0160 -0.0634 168 GLY A N 946 C CA . GLY A 127 ? 0.3464 0.3496 0.3004 0.0030 0.0173 -0.0649 168 GLY A CA 947 C C . GLY A 127 ? 0.3606 0.3634 0.3147 0.0040 0.0201 -0.0669 168 GLY A C 948 O O . GLY A 127 ? 0.3564 0.3608 0.3177 0.0032 0.0217 -0.0665 168 GLY A O 949 N N . MET A 128 ? 0.3779 0.3782 0.3235 0.0060 0.0208 -0.0691 169 MET A N 950 C CA . MET A 128 ? 0.3922 0.3920 0.3368 0.0072 0.0242 -0.0709 169 MET A CA 951 C C . MET A 128 ? 0.4030 0.4015 0.3385 0.0087 0.0280 -0.0698 169 MET A C 952 O O . MET A 128 ? 0.4302 0.4260 0.3585 0.0110 0.0288 -0.0725 169 MET A O 953 C CB . MET A 128 ? 0.4064 0.4039 0.3505 0.0087 0.0214 -0.0756 169 MET A CB 954 C CG . MET A 128 ? 0.4554 0.4540 0.4096 0.0073 0.0186 -0.0767 169 MET A CG 955 S SD . MET A 128 ? 0.2317 0.2275 0.1858 0.0091 0.0157 -0.0825 169 MET A SD 956 C CE . MET A 128 ? 0.6168 0.6128 0.5775 0.0077 0.0100 -0.0831 169 MET A CE 957 N N . PRO A 129 ? 0.3948 0.3949 0.3303 0.0076 0.0306 -0.0658 170 PRO A N 958 C CA . PRO A 129 ? 0.4073 0.4061 0.3349 0.0088 0.0346 -0.0642 170 PRO A CA 959 C C . PRO A 129 ? 0.4222 0.4209 0.3499 0.0101 0.0392 -0.0653 170 PRO A C 960 O O . PRO A 129 ? 0.4194 0.4204 0.3556 0.0090 0.0404 -0.0654 170 PRO A O 961 C CB . PRO A 129 ? 0.4087 0.4100 0.3403 0.0068 0.0361 -0.0598 170 PRO A CB 962 C CG . PRO A 129 ? 0.3806 0.3848 0.3231 0.0048 0.0344 -0.0595 170 PRO A CG 963 C CD . PRO A 129 ? 0.3802 0.3832 0.3235 0.0052 0.0300 -0.0626 170 PRO A CD 964 N N . GLU A 130 ? 0.4355 0.4314 0.3534 0.0125 0.0418 -0.0661 171 GLU A N 965 C CA . GLU A 130 ? 0.4457 0.4412 0.3627 0.0139 0.0470 -0.0668 171 GLU A CA 966 C C . GLU A 130 ? 0.4446 0.4396 0.3563 0.0146 0.0519 -0.0635 171 GLU A C 967 O O . GLU A 130 ? 0.4683 0.4610 0.3715 0.0155 0.0511 -0.0624 171 GLU A O 968 C CB . GLU A 130 ? 0.4578 0.4497 0.3667 0.0170 0.0462 -0.0711 171 GLU A CB 969 C CG A GLU A 130 ? 0.4681 0.4591 0.3789 0.0170 0.0404 -0.0750 171 GLU A CG 970 C CD A GLU A 130 ? 0.4789 0.4662 0.3823 0.0202 0.0399 -0.0795 171 GLU A CD 971 O OE1 A GLU A 130 ? 0.4926 0.4789 0.3975 0.0205 0.0351 -0.0831 171 GLU A OE1 972 O OE2 A GLU A 130 ? 0.4853 0.4709 0.3818 0.0224 0.0445 -0.0794 171 GLU A OE2 973 N N . GLY A 131 ? 0.4309 0.4278 0.3474 0.0142 0.0571 -0.0618 172 GLY A N 974 C CA . GLY A 131 ? 0.4312 0.4276 0.3438 0.0146 0.0621 -0.0583 172 GLY A CA 975 C C . GLY A 131 ? 0.4233 0.4221 0.3431 0.0141 0.0677 -0.0567 172 GLY A C 976 O O . GLY A 131 ? 0.4271 0.4277 0.3541 0.0137 0.0679 -0.0585 172 GLY A O 977 N N . ASP A 132 ? 0.4236 0.4223 0.3418 0.0141 0.0722 -0.0532 173 ASP A N 978 C CA . ASP A 132 ? 0.4313 0.4324 0.3573 0.0134 0.0778 -0.0513 173 ASP A CA 979 C C . ASP A 132 ? 0.4156 0.4207 0.3531 0.0103 0.0762 -0.0489 173 ASP A C 980 O O . ASP A 132 ? 0.4111 0.4164 0.3478 0.0089 0.0733 -0.0470 173 ASP A O 981 C CB . ASP A 132 ? 0.4456 0.4446 0.3649 0.0151 0.0837 -0.0486 173 ASP A CB 982 C CG . ASP A 132 ? 0.5090 0.5034 0.4151 0.0187 0.0854 -0.0508 173 ASP A CG 983 O OD1 . ASP A 132 ? 0.5306 0.5246 0.4365 0.0200 0.0845 -0.0544 173 ASP A OD1 984 O OD2 . ASP A 132 ? 0.5244 0.5156 0.4205 0.0205 0.0874 -0.0490 173 ASP A OD2 985 N N . LEU A 133 ? 0.3977 0.4058 0.3456 0.0093 0.0780 -0.0491 174 LEU A N 986 C CA . LEU A 133 ? 0.3743 0.3860 0.3333 0.0067 0.0765 -0.0472 174 LEU A CA 987 C C . LEU A 133 ? 0.3837 0.3964 0.3455 0.0058 0.0805 -0.0434 174 LEU A C 988 O O . LEU A 133 ? 0.3769 0.3886 0.3367 0.0071 0.0863 -0.0424 174 LEU A O 989 C CB . LEU A 133 ? 0.3710 0.3854 0.3399 0.0063 0.0771 -0.0489 174 LEU A CB 990 C CG A LEU A 133 ? 0.3759 0.3933 0.3548 0.0045 0.0730 -0.0494 174 LEU A CG 991 C CG B LEU A 133 ? 0.3260 0.3406 0.2965 0.0064 0.0725 -0.0521 174 LEU A CG 992 C CD1 A LEU A 133 ? 0.3524 0.3689 0.3281 0.0039 0.0669 -0.0502 174 LEU A CD1 993 C CD1 B LEU A 133 ? 0.3379 0.3552 0.3188 0.0061 0.0737 -0.0532 174 LEU A CD1 994 C CD2 A LEU A 133 ? 0.3649 0.3834 0.3494 0.0053 0.0740 -0.0520 174 LEU A CD2 995 C CD2 B LEU A 133 ? 0.3110 0.3258 0.2819 0.0049 0.0665 -0.0518 174 LEU A CD2 996 N N . VAL A 134 ? 0.3635 0.3779 0.3303 0.0037 0.0777 -0.0414 175 VAL A N 997 C CA . VAL A 134 ? 0.3534 0.3696 0.3270 0.0025 0.0808 -0.0382 175 VAL A CA 998 C C . VAL A 134 ? 0.3462 0.3660 0.3317 0.0005 0.0776 -0.0384 175 VAL A C 999 O O . VAL A 134 ? 0.3385 0.3586 0.3241 -0.0002 0.0722 -0.0392 175 VAL A O 1000 C CB . VAL A 134 ? 0.3687 0.3831 0.3361 0.0020 0.0805 -0.0353 175 VAL A CB 1001 C CG1 . VAL A 134 ? 0.3586 0.3750 0.3346 0.0004 0.0828 -0.0322 175 VAL A CG1 1002 C CG2 . VAL A 134 ? 0.3835 0.3940 0.3389 0.0044 0.0844 -0.0349 175 VAL A CG2 1003 N N . TYR A 135 ? 0.3237 0.3460 0.3191 0.0000 0.0807 -0.0377 176 TYR A N 1004 C CA . TYR A 135 ? 0.3087 0.3342 0.3155 -0.0015 0.0776 -0.0378 176 TYR A CA 1005 C C . TYR A 135 ? 0.3097 0.3361 0.3203 -0.0031 0.0768 -0.0350 176 TYR A C 1006 O O . TYR A 135 ? 0.3025 0.3288 0.3147 -0.0033 0.0811 -0.0328 176 TYR A O 1007 C CB . TYR A 135 ? 0.3088 0.3367 0.3251 -0.0012 0.0810 -0.0388 176 TYR A CB 1008 C CG . TYR A 135 ? 0.3088 0.3399 0.3373 -0.0025 0.0785 -0.0386 176 TYR A CG 1009 C CD1 . TYR A 135 ? 0.2905 0.3224 0.3212 -0.0028 0.0729 -0.0400 176 TYR A CD1 1010 C CD2 . TYR A 135 ? 0.3152 0.3483 0.3533 -0.0031 0.0818 -0.0371 176 TYR A CD2 1011 C CE1 . TYR A 135 ? 0.2878 0.3223 0.3289 -0.0036 0.0702 -0.0400 176 TYR A CE1 1012 C CE2 . TYR A 135 ? 0.3306 0.3666 0.3799 -0.0041 0.0790 -0.0373 176 TYR A CE2 1013 C CZ . TYR A 135 ? 0.2827 0.3192 0.3330 -0.0042 0.0730 -0.0388 176 TYR A CZ 1014 O OH . TYR A 135 ? 0.2871 0.3259 0.3477 -0.0047 0.0700 -0.0390 176 TYR A OH 1015 N N . VAL A 136 ? 0.2847 0.3119 0.2973 -0.0041 0.0713 -0.0350 177 VAL A N 1016 C CA . VAL A 136 ? 0.2969 0.3242 0.3110 -0.0054 0.0698 -0.0325 177 VAL A CA 1017 C C . VAL A 136 ? 0.2788 0.3090 0.3043 -0.0064 0.0669 -0.0325 177 VAL A C 1018 O O . VAL A 136 ? 0.2766 0.3070 0.3033 -0.0073 0.0637 -0.0312 177 VAL A O 1019 C CB . VAL A 136 ? 0.2908 0.3159 0.2952 -0.0054 0.0660 -0.0321 177 VAL A CB 1020 C CG1 . VAL A 136 ? 0.3143 0.3364 0.3076 -0.0042 0.0686 -0.0320 177 VAL A CG1 1021 C CG2 . VAL A 136 ? 0.3190 0.3445 0.3234 -0.0053 0.0609 -0.0342 177 VAL A CG2 1022 N N . ASN A 137 ? 0.2814 0.3137 0.3152 -0.0061 0.0679 -0.0340 178 ASN A N 1023 C CA . ASN A 137 ? 0.2576 0.2924 0.3021 -0.0067 0.0651 -0.0343 178 ASN A CA 1024 C C . ASN A 137 ? 0.2683 0.3026 0.3100 -0.0066 0.0590 -0.0350 178 ASN A C 1025 O O . ASN A 137 ? 0.2600 0.2933 0.2966 -0.0059 0.0575 -0.0365 178 ASN A O 1026 C CB . ASN A 137 ? 0.2601 0.2960 0.3117 -0.0078 0.0666 -0.0322 178 ASN A CB 1027 C CG . ASN A 137 ? 0.2527 0.2914 0.3171 -0.0080 0.0652 -0.0331 178 ASN A CG 1028 O OD1 . ASN A 137 ? 0.2730 0.3130 0.3414 -0.0072 0.0644 -0.0351 178 ASN A OD1 1029 N ND2 . ASN A 137 ? 0.2798 0.3194 0.3510 -0.0090 0.0646 -0.0317 178 ASN A ND2 1030 N N . TYR A 138 ? 0.2614 0.2963 0.3065 -0.0073 0.0558 -0.0339 179 TYR A N 1031 C CA . TYR A 138 ? 0.2475 0.2819 0.2904 -0.0071 0.0503 -0.0343 179 TYR A CA 1032 C C . TYR A 138 ? 0.2514 0.2835 0.2845 -0.0074 0.0490 -0.0331 179 TYR A C 1033 O O . TYR A 138 ? 0.2428 0.2743 0.2735 -0.0072 0.0448 -0.0331 179 TYR A O 1034 C CB . TYR A 138 ? 0.2367 0.2724 0.2876 -0.0073 0.0470 -0.0340 179 TYR A CB 1035 C CG . TYR A 138 ? 0.2379 0.2759 0.2989 -0.0067 0.0471 -0.0355 179 TYR A CG 1036 C CD1 . TYR A 138 ? 0.2420 0.2802 0.3040 -0.0054 0.0446 -0.0374 179 TYR A CD1 1037 C CD2 . TYR A 138 ? 0.2711 0.3108 0.3411 -0.0073 0.0495 -0.0351 179 TYR A CD2 1038 C CE1 . TYR A 138 ? 0.2712 0.3114 0.3425 -0.0047 0.0442 -0.0389 179 TYR A CE1 1039 C CE2 . TYR A 138 ? 0.2802 0.3220 0.3603 -0.0067 0.0491 -0.0367 179 TYR A CE2 1040 C CZ . TYR A 138 ? 0.2955 0.3375 0.3759 -0.0053 0.0463 -0.0386 179 TYR A CZ 1041 O OH . TYR A 138 ? 0.2995 0.3435 0.3896 -0.0045 0.0457 -0.0402 179 TYR A OH 1042 N N . ALA A 139 ? 0.2396 0.2704 0.2668 -0.0077 0.0525 -0.0320 180 ALA A N 1043 C CA . ALA A 139 ? 0.2453 0.2739 0.2632 -0.0079 0.0512 -0.0309 180 ALA A CA 1044 C C . ALA A 139 ? 0.2477 0.2762 0.2669 -0.0087 0.0483 -0.0291 180 ALA A C 1045 O O . ALA A 139 ? 0.2552 0.2823 0.2681 -0.0088 0.0455 -0.0285 180 ALA A O 1046 C CB . ALA A 139 ? 0.2592 0.2866 0.2709 -0.0072 0.0487 -0.0325 180 ALA A CB 1047 N N . ARG A 140 ? 0.2427 0.2727 0.2703 -0.0093 0.0488 -0.0284 181 ARG A N 1048 C CA . ARG A 140 ? 0.2426 0.2726 0.2720 -0.0100 0.0462 -0.0268 181 ARG A CA 1049 C C . ARG A 140 ? 0.2526 0.2809 0.2771 -0.0108 0.0488 -0.0245 181 ARG A C 1050 O O . ARG A 140 ? 0.2478 0.2754 0.2696 -0.0107 0.0534 -0.0239 181 ARG A O 1051 C CB . ARG A 140 ? 0.2322 0.2641 0.2727 -0.0103 0.0455 -0.0270 181 ARG A CB 1052 C CG . ARG A 140 ? 0.2459 0.2792 0.2913 -0.0093 0.0423 -0.0291 181 ARG A CG 1053 C CD . ARG A 140 ? 0.2703 0.3057 0.3270 -0.0094 0.0423 -0.0298 181 ARG A CD 1054 N NE . ARG A 140 ? 0.2734 0.3098 0.3344 -0.0098 0.0476 -0.0297 181 ARG A NE 1055 C CZ . ARG A 140 ? 0.2950 0.3335 0.3670 -0.0100 0.0488 -0.0302 181 ARG A CZ 1056 N NH1 . ARG A 140 ? 0.2968 0.3365 0.3766 -0.0097 0.0447 -0.0312 181 ARG A NH1 1057 N NH2 . ARG A 140 ? 0.3044 0.3436 0.3797 -0.0104 0.0543 -0.0299 181 ARG A NH2 1058 N N . THR A 141 ? 0.2481 0.2756 0.2715 -0.0113 0.0461 -0.0231 182 THR A N 1059 C CA . THR A 141 ? 0.2592 0.2852 0.2789 -0.0120 0.0483 -0.0207 182 THR A CA 1060 C C . THR A 141 ? 0.2669 0.2935 0.2925 -0.0125 0.0535 -0.0196 182 THR A C 1061 O O . THR A 141 ? 0.2778 0.3028 0.2981 -0.0124 0.0577 -0.0181 182 THR A O 1062 C CB . THR A 141 ? 0.2646 0.2902 0.2855 -0.0125 0.0445 -0.0196 182 THR A CB 1063 O OG1 . THR A 141 ? 0.2677 0.2925 0.2821 -0.0118 0.0406 -0.0203 182 THR A OG1 1064 C CG2 . THR A 141 ? 0.2681 0.2920 0.2861 -0.0132 0.0471 -0.0170 182 THR A CG2 1065 N N . GLU A 142 ? 0.2712 0.3000 0.3078 -0.0129 0.0533 -0.0203 183 GLU A N 1066 C CA . GLU A 142 ? 0.2805 0.3101 0.3244 -0.0135 0.0584 -0.0192 183 GLU A CA 1067 C C . GLU A 142 ? 0.2934 0.3231 0.3353 -0.0128 0.0631 -0.0199 183 GLU A C 1068 O O . GLU A 142 ? 0.2981 0.3273 0.3412 -0.0130 0.0686 -0.0182 183 GLU A O 1069 C CB . GLU A 142 ? 0.2748 0.3068 0.3318 -0.0140 0.0565 -0.0200 183 GLU A CB 1070 C CG . GLU A 142 ? 0.3185 0.3525 0.3802 -0.0132 0.0537 -0.0228 183 GLU A CG 1071 C CD . GLU A 142 ? 0.3563 0.3902 0.4170 -0.0126 0.0471 -0.0241 183 GLU A CD 1072 O OE1 . GLU A 142 ? 0.3046 0.3366 0.3568 -0.0126 0.0448 -0.0232 183 GLU A OE1 1073 O OE2 . GLU A 142 ? 0.3192 0.3548 0.3876 -0.0120 0.0443 -0.0259 183 GLU A OE2 1074 N N . ASP A 143 ? 0.2851 0.3152 0.3236 -0.0118 0.0613 -0.0222 184 ASP A N 1075 C CA . ASP A 143 ? 0.3001 0.3301 0.3361 -0.0109 0.0657 -0.0231 184 ASP A CA 1076 C C . ASP A 143 ? 0.3150 0.3421 0.3394 -0.0103 0.0689 -0.0216 184 ASP A C 1077 O O . ASP A 143 ? 0.3160 0.3424 0.3391 -0.0098 0.0744 -0.0208 184 ASP A O 1078 C CB . ASP A 143 ? 0.3055 0.3363 0.3406 -0.0100 0.0628 -0.0259 184 ASP A CB 1079 C CG . ASP A 143 ? 0.2886 0.3221 0.3348 -0.0101 0.0601 -0.0274 184 ASP A CG 1080 O OD1 . ASP A 143 ? 0.2918 0.3270 0.3477 -0.0107 0.0625 -0.0269 184 ASP A OD1 1081 O OD2 . ASP A 143 ? 0.2769 0.3107 0.3226 -0.0096 0.0557 -0.0291 184 ASP A OD2 1082 N N . PHE A 144 ? 0.3062 0.3315 0.3221 -0.0103 0.0653 -0.0212 185 PHE A N 1083 C CA . PHE A 144 ? 0.3155 0.3377 0.3202 -0.0096 0.0676 -0.0199 185 PHE A CA 1084 C C . PHE A 144 ? 0.3190 0.3401 0.3245 -0.0101 0.0715 -0.0167 185 PHE A C 1085 O O . PHE A 144 ? 0.3356 0.3543 0.3340 -0.0091 0.0761 -0.0154 185 PHE A O 1086 C CB . PHE A 144 ? 0.3055 0.3263 0.3016 -0.0093 0.0628 -0.0205 185 PHE A CB 1087 C CG . PHE A 144 ? 0.2915 0.3124 0.2843 -0.0083 0.0606 -0.0234 185 PHE A CG 1088 C CD1 . PHE A 144 ? 0.2903 0.3129 0.2877 -0.0086 0.0561 -0.0250 185 PHE A CD1 1089 C CD2 . PHE A 144 ? 0.2658 0.2850 0.2512 -0.0070 0.0633 -0.0245 185 PHE A CD2 1090 C CE1 . PHE A 144 ? 0.2751 0.2978 0.2703 -0.0078 0.0543 -0.0275 185 PHE A CE1 1091 C CE2 . PHE A 144 ? 0.2732 0.2926 0.2566 -0.0062 0.0612 -0.0273 185 PHE A CE2 1092 C CZ . PHE A 144 ? 0.2982 0.3194 0.2868 -0.0067 0.0567 -0.0288 185 PHE A CZ 1093 N N . PHE A 145 ? 0.3168 0.3391 0.3301 -0.0115 0.0698 -0.0155 186 PHE A N 1094 C CA . PHE A 145 ? 0.3312 0.3525 0.3472 -0.0121 0.0739 -0.0124 186 PHE A CA 1095 C C . PHE A 145 ? 0.3536 0.3753 0.3739 -0.0117 0.0806 -0.0118 186 PHE A C 1096 O O . PHE A 145 ? 0.3695 0.3890 0.3851 -0.0111 0.0859 -0.0094 186 PHE A O 1097 C CB . PHE A 145 ? 0.3222 0.3453 0.3491 -0.0137 0.0713 -0.0117 186 PHE A CB 1098 C CG . PHE A 145 ? 0.3410 0.3629 0.3638 -0.0141 0.0661 -0.0112 186 PHE A CG 1099 C CD1 . PHE A 145 ? 0.3205 0.3399 0.3311 -0.0134 0.0649 -0.0106 186 PHE A CD1 1100 C CD2 . PHE A 145 ? 0.3305 0.3539 0.3621 -0.0151 0.0624 -0.0114 186 PHE A CD2 1101 C CE1 . PHE A 145 ? 0.3402 0.3588 0.3476 -0.0138 0.0602 -0.0101 186 PHE A CE1 1102 C CE2 . PHE A 145 ? 0.2916 0.3140 0.3195 -0.0154 0.0578 -0.0109 186 PHE A CE2 1103 C CZ . PHE A 145 ? 0.3104 0.3304 0.3264 -0.0148 0.0569 -0.0101 186 PHE A CZ 1104 N N . LYS A 146 ? 0.3560 0.3805 0.3852 -0.0118 0.0805 -0.0139 187 LYS A N 1105 C CA . LYS A 146 ? 0.3715 0.3970 0.4070 -0.0115 0.0869 -0.0134 187 LYS A CA 1106 C C . LYS A 146 ? 0.3898 0.4127 0.4140 -0.0096 0.0912 -0.0134 187 LYS A C 1107 O O . LYS A 146 ? 0.3969 0.4185 0.4201 -0.0090 0.0976 -0.0111 187 LYS A O 1108 C CB . LYS A 146 ? 0.3649 0.3938 0.4115 -0.0118 0.0852 -0.0161 187 LYS A CB 1109 C CG . LYS A 146 ? 0.4243 0.4543 0.4772 -0.0112 0.0917 -0.0159 187 LYS A CG 1110 C CD . LYS A 146 ? 0.5045 0.5381 0.5732 -0.0122 0.0907 -0.0170 187 LYS A CD 1111 C CE . LYS A 146 ? 0.5628 0.5967 0.6406 -0.0136 0.0931 -0.0143 187 LYS A CE 1112 N NZ . LYS A 146 ? 0.6072 0.6441 0.6984 -0.0148 0.0882 -0.0159 187 LYS A NZ 1113 N N . LEU A 147 ? 0.3808 0.4031 0.3968 -0.0086 0.0879 -0.0158 188 LEU A N 1114 C CA . LEU A 147 ? 0.4051 0.4248 0.4094 -0.0066 0.0910 -0.0163 188 LEU A CA 1115 C C . LEU A 147 ? 0.4282 0.4441 0.4217 -0.0057 0.0936 -0.0136 188 LEU A C 1116 O O . LEU A 147 ? 0.4375 0.4514 0.4264 -0.0043 0.0996 -0.0122 188 LEU A O 1117 C CB . LEU A 147 ? 0.4019 0.4213 0.3996 -0.0059 0.0858 -0.0195 188 LEU A CB 1118 C CG . LEU A 147 ? 0.3991 0.4212 0.4035 -0.0058 0.0843 -0.0225 188 LEU A CG 1119 C CD1 . LEU A 147 ? 0.4313 0.4531 0.4302 -0.0056 0.0781 -0.0250 188 LEU A CD1 1120 C CD2 . LEU A 147 ? 0.4230 0.4445 0.4260 -0.0043 0.0899 -0.0232 188 LEU A CD2 1121 N N . GLU A 148 ? 0.4285 0.4433 0.4176 -0.0064 0.0891 -0.0128 189 GLU A N 1122 C CA . GLU A 148 ? 0.4569 0.4679 0.4348 -0.0054 0.0908 -0.0103 189 GLU A CA 1123 C C . GLU A 148 ? 0.4631 0.4732 0.4452 -0.0060 0.0960 -0.0065 189 GLU A C 1124 O O . GLU A 148 ? 0.4797 0.4866 0.4540 -0.0043 0.1014 -0.0044 189 GLU A O 1125 C CB . GLU A 148 ? 0.4641 0.4741 0.4359 -0.0059 0.0844 -0.0106 189 GLU A CB 1126 C CG . GLU A 148 ? 0.5460 0.5521 0.5076 -0.0049 0.0864 -0.0076 189 GLU A CG 1127 C CD . GLU A 148 ? 0.6277 0.6327 0.5833 -0.0052 0.0806 -0.0076 189 GLU A CD 1128 O OE1 . GLU A 148 ? 0.6586 0.6629 0.6072 -0.0043 0.0766 -0.0100 189 GLU A OE1 1129 O OE2 . GLU A 148 ? 0.6572 0.6618 0.6154 -0.0063 0.0801 -0.0051 189 GLU A OE2 1130 N N . ARG A 149 ? 0.4371 0.4497 0.4313 -0.0081 0.0947 -0.0056 190 ARG A N 1131 C CA . ARG A 149 ? 0.4450 0.4568 0.4440 -0.0089 0.0988 -0.0019 190 ARG A CA 1132 C C . ARG A 149 ? 0.4540 0.4668 0.4617 -0.0088 0.1060 -0.0007 190 ARG A C 1133 O O . ARG A 149 ? 0.4774 0.4877 0.4826 -0.0081 0.1120 0.0027 190 ARG A O 1134 C CB . ARG A 149 ? 0.4276 0.4412 0.4355 -0.0111 0.0940 -0.0016 190 ARG A CB 1135 C CG . ARG A 149 ? 0.3850 0.3974 0.3843 -0.0111 0.0876 -0.0022 190 ARG A CG 1136 C CD . ARG A 149 ? 0.3747 0.3892 0.3834 -0.0130 0.0824 -0.0025 190 ARG A CD 1137 N NE . ARG A 149 ? 0.3943 0.4073 0.3950 -0.0129 0.0771 -0.0026 190 ARG A NE 1138 C CZ . ARG A 149 ? 0.3890 0.4029 0.3948 -0.0142 0.0727 -0.0025 190 ARG A CZ 1139 N NH1 . ARG A 149 ? 0.3564 0.3726 0.3751 -0.0155 0.0725 -0.0025 190 ARG A NH1 1140 N NH2 . ARG A 149 ? 0.3929 0.4053 0.3910 -0.0140 0.0683 -0.0025 190 ARG A NH2 1141 N N . ASP A 150 ? 0.4536 0.4698 0.4712 -0.0094 0.1054 -0.0031 191 ASP A N 1142 C CA . ASP A 150 ? 0.4669 0.4847 0.4952 -0.0095 0.1118 -0.0022 191 ASP A CA 1143 C C . ASP A 150 ? 0.4729 0.4895 0.4945 -0.0073 0.1168 -0.0030 191 ASP A C 1144 O O . ASP A 150 ? 0.4833 0.4984 0.5052 -0.0063 0.1243 -0.0005 191 ASP A O 1145 C CB . ASP A 150 ? 0.4691 0.4914 0.5131 -0.0112 0.1086 -0.0044 191 ASP A CB 1146 C CG . ASP A 150 ? 0.5140 0.5374 0.5653 -0.0132 0.1036 -0.0039 191 ASP A CG 1147 O OD1 . ASP A 150 ? 0.5560 0.5769 0.6027 -0.0135 0.1042 -0.0012 191 ASP A OD1 1148 O OD2 . ASP A 150 ? 0.5576 0.5842 0.6189 -0.0142 0.0989 -0.0063 191 ASP A OD2 1149 N N . MET A 151 ? 0.4601 0.4771 0.4756 -0.0063 0.1130 -0.0064 192 MET A N 1150 C CA . MET A 151 ? 0.4654 0.4815 0.4755 -0.0042 0.1173 -0.0077 192 MET A CA 1151 C C . MET A 151 ? 0.4762 0.4877 0.4689 -0.0017 0.1189 -0.0070 192 MET A C 1152 O O . MET A 151 ? 0.4860 0.4958 0.4727 0.0005 0.1235 -0.0076 192 MET A O 1153 C CB . MET A 151 ? 0.4520 0.4708 0.4652 -0.0043 0.1127 -0.0119 192 MET A CB 1154 C CG . MET A 151 ? 0.4460 0.4691 0.4757 -0.0061 0.1111 -0.0129 192 MET A CG 1155 S SD . MET A 151 ? 0.1630 0.1886 0.1947 -0.0057 0.1062 -0.0176 192 MET A SD 1156 C CE . MET A 151 ? 0.4669 0.4922 0.4988 -0.0037 0.1142 -0.0180 192 MET A CE 1157 N N . LYS A 152 ? 0.4761 0.4854 0.4607 -0.0019 0.1151 -0.0060 193 LYS A N 1158 C CA . LYS A 152 ? 0.4959 0.5007 0.4639 0.0005 0.1155 -0.0055 193 LYS A CA 1159 C C . LYS A 152 ? 0.5041 0.5082 0.4635 0.0022 0.1127 -0.0094 193 LYS A C 1160 O O . LYS A 152 ? 0.5342 0.5348 0.4817 0.0050 0.1156 -0.0094 193 LYS A O 1161 C CB . LYS A 152 ? 0.5106 0.5120 0.4733 0.0024 0.1239 -0.0019 193 LYS A CB 1162 C CG . LYS A 152 ? 0.5613 0.5606 0.5230 0.0017 0.1253 0.0022 193 LYS A CG 1163 C CD . LYS A 152 ? 0.6018 0.6045 0.5801 -0.0013 0.1256 0.0039 193 LYS A CD 1164 C CE . LYS A 152 ? 0.6344 0.6348 0.6103 -0.0020 0.1254 0.0075 193 LYS A CE 1165 N NZ . LYS A 152 ? 0.6348 0.6381 0.6268 -0.0048 0.1260 0.0092 193 LYS A NZ 1166 N N . ILE A 153 ? 0.4819 0.4892 0.4473 0.0009 0.1070 -0.0126 194 ILE A N 1167 C CA . ILE A 153 ? 0.4829 0.4897 0.4415 0.0023 0.1038 -0.0164 194 ILE A CA 1168 C C . ILE A 153 ? 0.4881 0.4936 0.4389 0.0022 0.0969 -0.0176 194 ILE A C 1169 O O . ILE A 153 ? 0.4786 0.4860 0.4350 0.0001 0.0925 -0.0171 194 ILE A O 1170 C CB . ILE A 153 ? 0.4775 0.4882 0.4473 0.0014 0.1027 -0.0191 194 ILE A CB 1171 C CG1 . ILE A 153 ? 0.4917 0.5026 0.4653 0.0026 0.1101 -0.0186 194 ILE A CG1 1172 C CG2 . ILE A 153 ? 0.4730 0.4835 0.4375 0.0022 0.0976 -0.0230 194 ILE A CG2 1173 C CD1 . ILE A 153 ? 0.5154 0.5306 0.5041 0.0010 0.1105 -0.0197 194 ILE A CD1 1174 N N . ASN A 154 ? 0.4940 0.4963 0.4322 0.0044 0.0959 -0.0192 195 ASN A N 1175 C CA . ASN A 154 ? 0.5009 0.5017 0.4312 0.0045 0.0896 -0.0202 195 ASN A CA 1176 C C . ASN A 154 ? 0.4852 0.4873 0.4161 0.0045 0.0845 -0.0244 195 ASN A C 1177 O O . ASN A 154 ? 0.4682 0.4694 0.3955 0.0063 0.0861 -0.0268 195 ASN A O 1178 C CB . ASN A 154 ? 0.5298 0.5256 0.4453 0.0073 0.0917 -0.0191 195 ASN A CB 1179 C CG . ASN A 154 ? 0.5904 0.5844 0.4977 0.0075 0.0854 -0.0199 195 ASN A CG 1180 O OD1 . ASN A 154 ? 0.5859 0.5823 0.4983 0.0057 0.0797 -0.0213 195 ASN A OD1 1181 N ND2 . ASN A 154 ? 0.6831 0.6727 0.5775 0.0101 0.0867 -0.0188 195 ASN A ND2 1182 N N . CYS A 155 ? 0.4574 0.4618 0.3936 0.0026 0.0786 -0.0252 196 CYS A N 1183 C CA . CYS A 155 ? 0.4415 0.4472 0.3792 0.0024 0.0739 -0.0289 196 CYS A CA 1184 C C . CYS A 155 ? 0.4509 0.4539 0.3780 0.0038 0.0696 -0.0307 196 CYS A C 1185 O O . CYS A 155 ? 0.4367 0.4404 0.3646 0.0037 0.0654 -0.0337 196 CYS A O 1186 C CB . CYS A 155 ? 0.4279 0.4373 0.3765 -0.0001 0.0698 -0.0289 196 CYS A CB 1187 S SG . CYS A 155 ? 0.1573 0.1701 0.1194 -0.0015 0.0735 -0.0278 196 CYS A SG 1188 N N . SER A 156 ? 0.4576 0.4575 0.3754 0.0049 0.0703 -0.0289 197 SER A N 1189 C CA . SER A 156 ? 0.4733 0.4704 0.3812 0.0063 0.0658 -0.0306 197 SER A CA 1190 C C . SER A 156 ? 0.4758 0.4715 0.3787 0.0084 0.0652 -0.0345 197 SER A C 1191 O O . SER A 156 ? 0.4992 0.4928 0.3968 0.0105 0.0697 -0.0348 197 SER A O 1192 C CB . SER A 156 ? 0.4876 0.4811 0.3853 0.0079 0.0675 -0.0281 197 SER A CB 1193 O OG . SER A 156 ? 0.5146 0.5057 0.4033 0.0092 0.0626 -0.0298 197 SER A OG 1194 N N . GLY A 157 ? 0.4606 0.4572 0.3651 0.0079 0.0596 -0.0374 198 GLY A N 1195 C CA . GLY A 157 ? 0.4459 0.4408 0.3459 0.0098 0.0582 -0.0414 198 GLY A CA 1196 C C . GLY A 157 ? 0.4393 0.4364 0.3466 0.0096 0.0608 -0.0430 198 GLY A C 1197 O O . GLY A 157 ? 0.4532 0.4489 0.3571 0.0113 0.0604 -0.0463 198 GLY A O 1198 N N . LYS A 158 ? 0.4195 0.4199 0.3370 0.0075 0.0632 -0.0410 199 LYS A N 1199 C CA . LYS A 158 ? 0.4176 0.4203 0.3432 0.0072 0.0655 -0.0424 199 LYS A CA 1200 C C . LYS A 158 ? 0.4111 0.4168 0.3459 0.0052 0.0609 -0.0438 199 LYS A C 1201 O O . LYS A 158 ? 0.3957 0.4022 0.3326 0.0037 0.0571 -0.0427 199 LYS A O 1202 C CB . LYS A 158 ? 0.4201 0.4246 0.3522 0.0063 0.0710 -0.0395 199 LYS A CB 1203 C CG . LYS A 158 ? 0.4702 0.4719 0.3944 0.0081 0.0765 -0.0373 199 LYS A CG 1204 C CD . LYS A 158 ? 0.5131 0.5123 0.4300 0.0110 0.0793 -0.0399 199 LYS A CD 1205 C CE . LYS A 158 ? 0.5680 0.5645 0.4785 0.0130 0.0860 -0.0373 199 LYS A CE 1206 N NZ . LYS A 158 ? 0.5738 0.5663 0.4715 0.0147 0.0847 -0.0365 199 LYS A NZ 1207 N N . ILE A 159 ? 0.3968 0.4038 0.3369 0.0054 0.0616 -0.0461 200 ILE A N 1208 C CA . ILE A 159 ? 0.3838 0.3936 0.3335 0.0037 0.0582 -0.0469 200 ILE A CA 1209 C C . ILE A 159 ? 0.3772 0.3900 0.3363 0.0023 0.0612 -0.0447 200 ILE A C 1210 O O . ILE A 159 ? 0.3845 0.3976 0.3453 0.0030 0.0659 -0.0445 200 ILE A O 1211 C CB . ILE A 159 ? 0.3949 0.4044 0.3458 0.0046 0.0568 -0.0506 200 ILE A CB 1212 C CG1 . ILE A 159 ? 0.4156 0.4223 0.3583 0.0057 0.0529 -0.0529 200 ILE A CG1 1213 C CG2 . ILE A 159 ? 0.3789 0.3913 0.3403 0.0031 0.0544 -0.0510 200 ILE A CG2 1214 C CD1 . ILE A 159 ? 0.4307 0.4363 0.3728 0.0071 0.0520 -0.0569 200 ILE A CD1 1215 N N . VAL A 160 ? 0.3502 0.3651 0.3155 0.0005 0.0585 -0.0430 201 VAL A N 1216 C CA . VAL A 160 ? 0.3446 0.3621 0.3191 -0.0006 0.0608 -0.0412 201 VAL A CA 1217 C C . VAL A 160 ? 0.3260 0.3457 0.3091 -0.0011 0.0589 -0.0428 201 VAL A C 1218 O O . VAL A 160 ? 0.3208 0.3405 0.3042 -0.0012 0.0548 -0.0442 201 VAL A O 1219 C CB . VAL A 160 ? 0.3621 0.3803 0.3384 -0.0020 0.0598 -0.0382 201 VAL A CB 1220 C CG1 . VAL A 160 ? 0.3609 0.3768 0.3290 -0.0015 0.0622 -0.0362 201 VAL A CG1 1221 C CG2 . VAL A 160 ? 0.3643 0.3830 0.3416 -0.0029 0.0543 -0.0383 201 VAL A CG2 1222 N N . ILE A 161 ? 0.3011 0.3229 0.2917 -0.0011 0.0619 -0.0427 202 ILE A N 1223 C CA . ILE A 161 ? 0.3016 0.3255 0.3009 -0.0015 0.0602 -0.0439 202 ILE A CA 1224 C C . ILE A 161 ? 0.2985 0.3248 0.3061 -0.0027 0.0601 -0.0417 202 ILE A C 1225 O O . ILE A 161 ? 0.2879 0.3149 0.2979 -0.0029 0.0637 -0.0402 202 ILE A O 1226 C CB . ILE A 161 ? 0.3070 0.3311 0.3083 -0.0003 0.0632 -0.0461 202 ILE A CB 1227 C CG1 . ILE A 161 ? 0.3025 0.3288 0.3130 -0.0005 0.0612 -0.0473 202 ILE A CG1 1228 C CG2 . ILE A 161 ? 0.3038 0.3281 0.3056 0.0003 0.0691 -0.0451 202 ILE A CG2 1229 C CD1 . ILE A 161 ? 0.2859 0.3118 0.2970 0.0009 0.0628 -0.0502 202 ILE A CD1 1230 N N . ALA A 162 ? 0.2698 0.2971 0.2815 -0.0033 0.0558 -0.0416 203 ALA A N 1231 C CA . ALA A 162 ? 0.2647 0.2939 0.2836 -0.0042 0.0547 -0.0399 203 ALA A CA 1232 C C . ALA A 162 ? 0.2617 0.2926 0.2883 -0.0038 0.0523 -0.0412 203 ALA A C 1233 O O . ALA A 162 ? 0.2538 0.2840 0.2788 -0.0032 0.0499 -0.0427 203 ALA A O 1234 C CB . ALA A 162 ? 0.2538 0.2821 0.2687 -0.0049 0.0514 -0.0382 203 ALA A CB 1235 N N . ARG A 163 ? 0.2635 0.2964 0.2986 -0.0041 0.0529 -0.0407 204 ARG A N 1236 C CA . ARG A 163 ? 0.2627 0.2970 0.3047 -0.0035 0.0500 -0.0417 204 ARG A CA 1237 C C . ARG A 163 ? 0.2560 0.2899 0.2976 -0.0037 0.0454 -0.0405 204 ARG A C 1238 O O . ARG A 163 ? 0.2356 0.2693 0.2757 -0.0045 0.0449 -0.0388 204 ARG A O 1239 C CB . ARG A 163 ? 0.2728 0.3095 0.3247 -0.0033 0.0520 -0.0421 204 ARG A CB 1240 C CG . ARG A 163 ? 0.2905 0.3282 0.3466 -0.0043 0.0536 -0.0404 204 ARG A CG 1241 C CD . ARG A 163 ? 0.3145 0.3547 0.3817 -0.0040 0.0551 -0.0414 204 ARG A CD 1242 N NE . ARG A 163 ? 0.2853 0.3267 0.3581 -0.0050 0.0579 -0.0399 204 ARG A NE 1243 C CZ . ARG A 163 ? 0.3151 0.3589 0.3991 -0.0050 0.0581 -0.0403 204 ARG A CZ 1244 N NH1 . ARG A 163 ? 0.2727 0.3176 0.3625 -0.0039 0.0552 -0.0421 204 ARG A NH1 1245 N NH2 . ARG A 163 ? 0.3016 0.3463 0.3910 -0.0060 0.0609 -0.0388 204 ARG A NH2 1246 N N . TYR A 164 ? 0.2386 0.2723 0.2812 -0.0027 0.0423 -0.0415 205 TYR A N 1247 C CA . TYR A 164 ? 0.2398 0.2731 0.2824 -0.0024 0.0380 -0.0405 205 TYR A CA 1248 C C . TYR A 164 ? 0.2406 0.2754 0.2906 -0.0024 0.0370 -0.0400 205 TYR A C 1249 O O . TYR A 164 ? 0.2329 0.2694 0.2896 -0.0023 0.0391 -0.0409 205 TYR A O 1250 C CB . TYR A 164 ? 0.2294 0.2619 0.2724 -0.0011 0.0358 -0.0415 205 TYR A CB 1251 C CG . TYR A 164 ? 0.2157 0.2463 0.2519 -0.0011 0.0347 -0.0416 205 TYR A CG 1252 C CD1 . TYR A 164 ? 0.2163 0.2463 0.2523 -0.0004 0.0353 -0.0432 205 TYR A CD1 1253 C CD2 . TYR A 164 ? 0.2094 0.2388 0.2406 -0.0015 0.0327 -0.0400 205 TYR A CD2 1254 C CE1 . TYR A 164 ? 0.1826 0.2108 0.2137 -0.0003 0.0341 -0.0434 205 TYR A CE1 1255 C CE2 . TYR A 164 ? 0.1817 0.2094 0.2080 -0.0014 0.0315 -0.0401 205 TYR A CE2 1256 C CZ . TYR A 164 ? 0.2139 0.2410 0.2405 -0.0008 0.0320 -0.0417 205 TYR A CZ 1257 O OH . TYR A 164 ? 0.2261 0.2516 0.2491 -0.0007 0.0307 -0.0418 205 TYR A OH 1258 N N . GLY A 165 ? 0.2237 0.2581 0.2731 -0.0023 0.0337 -0.0388 206 GLY A N 1259 C CA . GLY A 165 ? 0.2180 0.2536 0.2745 -0.0019 0.0318 -0.0387 206 GLY A CA 1260 C C . GLY A 165 ? 0.2248 0.2602 0.2803 -0.0031 0.0315 -0.0370 206 GLY A C 1261 O O . GLY A 165 ? 0.2249 0.2596 0.2751 -0.0043 0.0338 -0.0359 206 GLY A O 1262 N N . LYS A 166 ? 0.2229 0.2588 0.2837 -0.0026 0.0285 -0.0369 207 LYS A N 1263 C CA . LYS A 166 ? 0.2193 0.2553 0.2813 -0.0036 0.0280 -0.0356 207 LYS A CA 1264 C C . LYS A 166 ? 0.2232 0.2572 0.2771 -0.0038 0.0260 -0.0341 207 LYS A C 1265 O O . LYS A 166 ? 0.2485 0.2821 0.3036 -0.0034 0.0229 -0.0336 207 LYS A O 1266 C CB . LYS A 166 ? 0.2175 0.2544 0.2816 -0.0054 0.0327 -0.0348 207 LYS A CB 1267 C CG . LYS A 166 ? 0.2372 0.2763 0.3103 -0.0054 0.0355 -0.0361 207 LYS A CG 1268 C CD . LYS A 166 ? 0.2947 0.3353 0.3779 -0.0047 0.0326 -0.0370 207 LYS A CD 1269 C CE . LYS A 166 ? 0.3496 0.3925 0.4422 -0.0050 0.0360 -0.0381 207 LYS A CE 1270 N NZ . LYS A 166 ? 0.4127 0.4571 0.5160 -0.0043 0.0325 -0.0394 207 LYS A NZ 1271 N N . VAL A 167 ? 0.2125 0.2454 0.2587 -0.0042 0.0275 -0.0335 208 VAL A N 1272 C CA . VAL A 167 ? 0.2041 0.2351 0.2428 -0.0044 0.0257 -0.0321 208 VAL A CA 1273 C C . VAL A 167 ? 0.2029 0.2327 0.2357 -0.0037 0.0251 -0.0324 208 VAL A C 1274 O O . VAL A 167 ? 0.1952 0.2254 0.2282 -0.0035 0.0271 -0.0336 208 VAL A O 1275 C CB . VAL A 167 ? 0.2205 0.2512 0.2558 -0.0061 0.0283 -0.0305 208 VAL A CB 1276 C CG1 . VAL A 167 ? 0.2070 0.2387 0.2492 -0.0069 0.0292 -0.0300 208 VAL A CG1 1277 C CG2 . VAL A 167 ? 0.2238 0.2542 0.2547 -0.0067 0.0321 -0.0308 208 VAL A CG2 1278 N N . PHE A 168 ? 0.1871 0.2155 0.2148 -0.0033 0.0227 -0.0313 209 PHE A N 1279 C CA . PHE A 168 ? 0.1816 0.2087 0.2039 -0.0028 0.0222 -0.0313 209 PHE A CA 1280 C C . PHE A 168 ? 0.1861 0.2131 0.2047 -0.0040 0.0253 -0.0318 209 PHE A C 1281 O O . PHE A 168 ? 0.1946 0.2215 0.2107 -0.0052 0.0271 -0.0311 209 PHE A O 1282 C CB . PHE A 168 ? 0.1821 0.2078 0.1999 -0.0026 0.0198 -0.0298 209 PHE A CB 1283 C CG . PHE A 168 ? 0.1717 0.1962 0.1846 -0.0023 0.0194 -0.0296 209 PHE A CG 1284 C CD1 . PHE A 168 ? 0.1835 0.2075 0.1976 -0.0010 0.0187 -0.0303 209 PHE A CD1 1285 C CD2 . PHE A 168 ? 0.1901 0.2138 0.1976 -0.0033 0.0194 -0.0286 209 PHE A CD2 1286 C CE1 . PHE A 168 ? 0.2020 0.2249 0.2128 -0.0007 0.0184 -0.0300 209 PHE A CE1 1287 C CE2 . PHE A 168 ? 0.2046 0.2272 0.2087 -0.0030 0.0188 -0.0285 209 PHE A CE2 1288 C CZ . PHE A 168 ? 0.2162 0.2384 0.2222 -0.0018 0.0184 -0.0293 209 PHE A CZ 1289 N N . ARG A 169 ? 0.1904 0.2171 0.2083 -0.0034 0.0256 -0.0330 210 ARG A N 1290 C CA . ARG A 169 ? 0.1841 0.2104 0.1985 -0.0041 0.0281 -0.0340 210 ARG A CA 1291 C C . ARG A 169 ? 0.1976 0.2226 0.2052 -0.0049 0.0278 -0.0331 210 ARG A C 1292 O O . ARG A 169 ? 0.2061 0.2307 0.2100 -0.0055 0.0300 -0.0335 210 ARG A O 1293 C CB . ARG A 169 ? 0.1822 0.2082 0.1975 -0.0033 0.0282 -0.0356 210 ARG A CB 1294 C CG . ARG A 169 ? 0.1882 0.2129 0.2012 -0.0026 0.0256 -0.0351 210 ARG A CG 1295 C CD . ARG A 169 ? 0.2027 0.2270 0.2179 -0.0017 0.0258 -0.0366 210 ARG A CD 1296 N NE . ARG A 169 ? 0.1856 0.2104 0.2059 -0.0004 0.0249 -0.0366 210 ARG A NE 1297 C CZ . ARG A 169 ? 0.1954 0.2194 0.2159 0.0008 0.0225 -0.0352 210 ARG A CZ 1298 N NH1 . ARG A 169 ? 0.1862 0.2092 0.2028 0.0005 0.0212 -0.0337 210 ARG A NH1 1299 N NH2 . ARG A 169 ? 0.1896 0.2137 0.2141 0.0024 0.0215 -0.0353 210 ARG A NH2 1300 N N . GLY A 170 ? 0.1967 0.2210 0.2023 -0.0047 0.0252 -0.0318 211 GLY A N 1301 C CA . GLY A 170 ? 0.2203 0.2435 0.2202 -0.0053 0.0246 -0.0309 211 GLY A CA 1302 C C . GLY A 170 ? 0.2147 0.2380 0.2129 -0.0063 0.0262 -0.0298 211 GLY A C 1303 O O . GLY A 170 ? 0.2170 0.2393 0.2100 -0.0068 0.0272 -0.0297 211 GLY A O 1304 N N . ASN A 171 ? 0.2160 0.2402 0.2187 -0.0064 0.0264 -0.0291 212 ASN A N 1305 C CA . ASN A 171 ? 0.2217 0.2460 0.2238 -0.0074 0.0284 -0.0280 212 ASN A CA 1306 C C . ASN A 171 ? 0.2350 0.2594 0.2362 -0.0077 0.0322 -0.0287 212 ASN A C 1307 O O . ASN A 171 ? 0.2290 0.2525 0.2260 -0.0082 0.0342 -0.0278 212 ASN A O 1308 C CB . ASN A 171 ? 0.2156 0.2409 0.2239 -0.0074 0.0277 -0.0273 212 ASN A CB 1309 C CG . ASN A 171 ? 0.2331 0.2579 0.2409 -0.0069 0.0241 -0.0263 212 ASN A CG 1310 O OD1 . ASN A 171 ? 0.2431 0.2679 0.2530 -0.0058 0.0218 -0.0268 212 ASN A OD1 1311 N ND2 . ASN A 171 ? 0.2095 0.2333 0.2136 -0.0076 0.0236 -0.0247 212 ASN A ND2 1312 N N . LYS A 172 ? 0.2194 0.2448 0.2243 -0.0072 0.0333 -0.0304 213 LYS A N 1313 C CA . LYS A 172 ? 0.2312 0.2565 0.2350 -0.0072 0.0370 -0.0314 213 LYS A CA 1314 C C . LYS A 172 ? 0.2286 0.2521 0.2242 -0.0071 0.0375 -0.0318 213 LYS A C 1315 O O . LYS A 172 ? 0.2388 0.2615 0.2304 -0.0072 0.0406 -0.0314 213 LYS A O 1316 C CB . LYS A 172 ? 0.2116 0.2380 0.2202 -0.0065 0.0377 -0.0333 213 LYS A CB 1317 C CG . LYS A 172 ? 0.2181 0.2464 0.2354 -0.0063 0.0371 -0.0334 213 LYS A CG 1318 C CD . LYS A 172 ? 0.2211 0.2502 0.2422 -0.0055 0.0376 -0.0354 213 LYS A CD 1319 C CE . LYS A 172 ? 0.2146 0.2452 0.2437 -0.0049 0.0360 -0.0356 213 LYS A CE 1320 N NZ . LYS A 172 ? 0.2170 0.2495 0.2533 -0.0052 0.0387 -0.0359 213 LYS A NZ 1321 N N . VAL A 173 ? 0.2174 0.2401 0.2103 -0.0067 0.0347 -0.0326 214 VAL A N 1322 C CA . VAL A 173 ? 0.2409 0.2620 0.2269 -0.0064 0.0344 -0.0335 214 VAL A CA 1323 C C . VAL A 173 ? 0.2527 0.2725 0.2329 -0.0069 0.0341 -0.0317 214 VAL A C 1324 O O . VAL A 173 ? 0.2570 0.2752 0.2309 -0.0065 0.0356 -0.0319 214 VAL A O 1325 C CB . VAL A 173 ? 0.2570 0.2777 0.2433 -0.0060 0.0314 -0.0347 214 VAL A CB 1326 C CG1 . VAL A 173 ? 0.2671 0.2860 0.2466 -0.0058 0.0303 -0.0357 214 VAL A CG1 1327 C CG2 . VAL A 173 ? 0.2317 0.2534 0.2232 -0.0055 0.0323 -0.0365 214 VAL A CG2 1328 N N . LYS A 174 ? 0.2297 0.2499 0.2118 -0.0074 0.0321 -0.0299 215 LYS A N 1329 C CA . LYS A 174 ? 0.2451 0.2641 0.2222 -0.0078 0.0317 -0.0281 215 LYS A CA 1330 C C . LYS A 174 ? 0.2480 0.2665 0.2238 -0.0080 0.0356 -0.0271 215 LYS A C 1331 O O . LYS A 174 ? 0.2631 0.2798 0.2320 -0.0077 0.0367 -0.0265 215 LYS A O 1332 C CB . LYS A 174 ? 0.2307 0.2503 0.2112 -0.0082 0.0295 -0.0264 215 LYS A CB 1333 C CG . LYS A 174 ? 0.2829 0.3013 0.2587 -0.0086 0.0288 -0.0244 215 LYS A CG 1334 C CD . LYS A 174 ? 0.3117 0.3306 0.2910 -0.0089 0.0264 -0.0230 215 LYS A CD 1335 C CE . LYS A 174 ? 0.4066 0.4244 0.3827 -0.0095 0.0267 -0.0209 215 LYS A CE 1336 N NZ . LYS A 174 ? 0.5006 0.5187 0.4799 -0.0096 0.0244 -0.0196 215 LYS A NZ 1337 N N . ASN A 175 ? 0.2560 0.2761 0.2384 -0.0083 0.0377 -0.0269 216 ASN A N 1338 C CA . ASN A 175 ? 0.2430 0.2629 0.2256 -0.0085 0.0420 -0.0258 216 ASN A CA 1339 C C . ASN A 175 ? 0.2570 0.2755 0.2337 -0.0076 0.0450 -0.0269 216 ASN A C 1340 O O . ASN A 175 ? 0.2854 0.3022 0.2568 -0.0073 0.0477 -0.0256 216 ASN A O 1341 C CB . ASN A 175 ? 0.2358 0.2578 0.2279 -0.0090 0.0436 -0.0257 216 ASN A CB 1342 C CG . ASN A 175 ? 0.2398 0.2629 0.2373 -0.0096 0.0406 -0.0247 216 ASN A CG 1343 O OD1 . ASN A 175 ? 0.2652 0.2872 0.2591 -0.0098 0.0382 -0.0234 216 ASN A OD1 1344 N ND2 . ASN A 175 ? 0.2303 0.2553 0.2364 -0.0097 0.0406 -0.0252 216 ASN A ND2 1345 N N . ALA A 176 ? 0.2566 0.2755 0.2339 -0.0069 0.0446 -0.0293 217 ALA A N 1346 C CA . ALA A 176 ? 0.2764 0.2937 0.2476 -0.0058 0.0472 -0.0308 217 ALA A CA 1347 C C . ALA A 176 ? 0.3004 0.3151 0.2618 -0.0051 0.0455 -0.0308 217 ALA A C 1348 O O . ALA A 176 ? 0.3198 0.3325 0.2744 -0.0040 0.0482 -0.0308 217 ALA A O 1349 C CB . ALA A 176 ? 0.2732 0.2914 0.2473 -0.0052 0.0464 -0.0336 217 ALA A CB 1350 N N . GLN A 177 ? 0.3137 0.3283 0.2744 -0.0055 0.0411 -0.0310 218 GLN A N 1351 C CA . GLN A 177 ? 0.3416 0.3540 0.2940 -0.0048 0.0390 -0.0312 218 GLN A CA 1352 C C . GLN A 177 ? 0.3576 0.3685 0.3052 -0.0048 0.0409 -0.0287 218 GLN A C 1353 O O . GLN A 177 ? 0.3694 0.3779 0.3087 -0.0036 0.0417 -0.0289 218 GLN A O 1354 C CB . GLN A 177 ? 0.3539 0.3668 0.3078 -0.0054 0.0343 -0.0312 218 GLN A CB 1355 C CG . GLN A 177 ? 0.3856 0.3992 0.3422 -0.0052 0.0322 -0.0336 218 GLN A CG 1356 C CD . GLN A 177 ? 0.4236 0.4372 0.3810 -0.0055 0.0279 -0.0335 218 GLN A CD 1357 O OE1 . GLN A 177 ? 0.4532 0.4678 0.4150 -0.0056 0.0263 -0.0348 218 GLN A OE1 1358 N NE2 . GLN A 177 ? 0.4787 0.4914 0.4321 -0.0057 0.0264 -0.0319 218 GLN A NE2 1359 N N . LEU A 178 ? 0.3470 0.3591 0.2995 -0.0059 0.0413 -0.0264 219 LEU A N 1360 C CA . LEU A 178 ? 0.3708 0.3813 0.3193 -0.0060 0.0431 -0.0237 219 LEU A CA 1361 C C . LEU A 178 ? 0.3808 0.3901 0.3267 -0.0052 0.0484 -0.0230 219 LEU A C 1362 O O . LEU A 178 ? 0.3934 0.4004 0.3326 -0.0045 0.0502 -0.0212 219 LEU A O 1363 C CB . LEU A 178 ? 0.3748 0.3868 0.3295 -0.0074 0.0420 -0.0216 219 LEU A CB 1364 C CG . LEU A 178 ? 0.4368 0.4493 0.3920 -0.0078 0.0369 -0.0220 219 LEU A CG 1365 C CD1 . LEU A 178 ? 0.4814 0.4951 0.4424 -0.0089 0.0358 -0.0200 219 LEU A CD1 1366 C CD2 . LEU A 178 ? 0.4866 0.4970 0.4335 -0.0070 0.0345 -0.0221 219 LEU A CD2 1367 N N . ALA A 179 ? 0.3569 0.3677 0.3078 -0.0051 0.0512 -0.0242 220 ALA A N 1368 C CA . ALA A 179 ? 0.3671 0.3766 0.3152 -0.0040 0.0566 -0.0237 220 ALA A CA 1369 C C . ALA A 179 ? 0.3745 0.3814 0.3126 -0.0020 0.0568 -0.0257 220 ALA A C 1370 O O . ALA A 179 ? 0.3990 0.4043 0.3330 -0.0007 0.0613 -0.0255 220 ALA A O 1371 C CB . ALA A 179 ? 0.3553 0.3673 0.3124 -0.0045 0.0592 -0.0246 220 ALA A CB 1372 N N . GLY A 180 ? 0.3605 0.3668 0.2948 -0.0017 0.0521 -0.0277 221 GLY A N 1373 C CA . GLY A 180 ? 0.3572 0.3607 0.2821 0.0004 0.0515 -0.0300 221 GLY A CA 1374 C C . GLY A 180 ? 0.3631 0.3672 0.2897 0.0011 0.0517 -0.0333 221 GLY A C 1375 O O . GLY A 180 ? 0.3803 0.3820 0.2992 0.0031 0.0519 -0.0353 221 GLY A O 1376 N N . ALA A 181 ? 0.3490 0.3562 0.2854 -0.0002 0.0514 -0.0339 222 ALA A N 1377 C CA . ALA A 181 ? 0.3538 0.3616 0.2926 0.0004 0.0513 -0.0370 222 ALA A CA 1378 C C . ALA A 181 ? 0.3494 0.3559 0.2839 0.0012 0.0467 -0.0398 222 ALA A C 1379 O O . ALA A 181 ? 0.3488 0.3552 0.2823 0.0005 0.0429 -0.0392 222 ALA A O 1380 C CB . ALA A 181 ? 0.3471 0.3584 0.2974 -0.0011 0.0511 -0.0370 222 ALA A CB 1381 N N . LYS A 182 ? 0.3461 0.3517 0.2787 0.0025 0.0471 -0.0428 223 LYS A N 1382 C CA . LYS A 182 ? 0.3516 0.3560 0.2819 0.0031 0.0425 -0.0457 223 LYS A CA 1383 C C . LYS A 182 ? 0.3352 0.3419 0.2743 0.0021 0.0407 -0.0475 223 LYS A C 1384 O O . LYS A 182 ? 0.3400 0.3461 0.2791 0.0024 0.0371 -0.0499 223 LYS A O 1385 C CB . LYS A 182 ? 0.3950 0.3961 0.3153 0.0056 0.0430 -0.0482 223 LYS A CB 1386 C CG . LYS A 182 ? 0.4228 0.4234 0.3432 0.0069 0.0461 -0.0504 223 LYS A CG 1387 C CD . LYS A 182 ? 0.4836 0.4804 0.3931 0.0097 0.0452 -0.0532 223 LYS A CD 1388 C CE . LYS A 182 ? 0.5260 0.5217 0.4330 0.0116 0.0495 -0.0548 223 LYS A CE 1389 N NZ . LYS A 182 ? 0.5553 0.5466 0.4502 0.0147 0.0485 -0.0575 223 LYS A NZ 1390 N N . GLY A 183 ? 0.3262 0.3354 0.2732 0.0011 0.0432 -0.0463 224 GLY A N 1391 C CA . GLY A 183 ? 0.3001 0.3114 0.2557 0.0002 0.0414 -0.0475 224 GLY A CA 1392 C C . GLY A 183 ? 0.3036 0.3174 0.2667 -0.0007 0.0441 -0.0457 224 GLY A C 1393 O O . GLY A 183 ? 0.3027 0.3166 0.2649 -0.0006 0.0479 -0.0442 224 GLY A O 1394 N N . VAL A 184 ? 0.2867 0.3024 0.2576 -0.0016 0.0423 -0.0458 225 VAL A N 1395 C CA . VAL A 184 ? 0.2734 0.2915 0.2519 -0.0022 0.0443 -0.0444 225 VAL A CA 1396 C C . VAL A 184 ? 0.2674 0.2866 0.2522 -0.0019 0.0438 -0.0464 225 VAL A C 1397 O O . VAL A 184 ? 0.2689 0.2877 0.2548 -0.0019 0.0408 -0.0475 225 VAL A O 1398 C CB . VAL A 184 ? 0.2852 0.3046 0.2675 -0.0035 0.0418 -0.0419 225 VAL A CB 1399 C CG1 . VAL A 184 ? 0.2958 0.3174 0.2859 -0.0039 0.0434 -0.0408 225 VAL A CG1 1400 C CG2 . VAL A 184 ? 0.2991 0.3174 0.2755 -0.0039 0.0415 -0.0400 225 VAL A CG2 1401 N N . ILE A 185 ? 0.2764 0.2968 0.2655 -0.0016 0.0470 -0.0467 226 ILE A N 1402 C CA . ILE A 185 ? 0.2726 0.2943 0.2686 -0.0013 0.0468 -0.0482 226 ILE A CA 1403 C C . ILE A 185 ? 0.2667 0.2907 0.2704 -0.0020 0.0469 -0.0464 226 ILE A C 1404 O O . ILE A 185 ? 0.2746 0.2995 0.2798 -0.0023 0.0497 -0.0451 226 ILE A O 1405 C CB . ILE A 185 ? 0.2960 0.3172 0.2911 -0.0002 0.0503 -0.0504 226 ILE A CB 1406 C CG1 . ILE A 185 ? 0.3037 0.3222 0.2906 0.0008 0.0495 -0.0525 226 ILE A CG1 1407 C CG2 . ILE A 185 ? 0.2870 0.3096 0.2898 0.0002 0.0503 -0.0518 226 ILE A CG2 1408 C CD1 . ILE A 185 ? 0.3282 0.3456 0.3118 0.0023 0.0535 -0.0544 226 ILE A CD1 1409 N N . LEU A 186 ? 0.2558 0.2805 0.2642 -0.0021 0.0439 -0.0462 227 LEU A N 1410 C CA . LEU A 186 ? 0.2424 0.2691 0.2580 -0.0024 0.0433 -0.0449 227 LEU A CA 1411 C C . LEU A 186 ? 0.2319 0.2595 0.2535 -0.0015 0.0440 -0.0465 227 LEU A C 1412 O O . LEU A 186 ? 0.2488 0.2755 0.2697 -0.0009 0.0431 -0.0482 227 LEU A O 1413 C CB . LEU A 186 ? 0.2363 0.2627 0.2522 -0.0026 0.0393 -0.0435 227 LEU A CB 1414 C CG . LEU A 186 ? 0.2360 0.2615 0.2461 -0.0034 0.0381 -0.0419 227 LEU A CG 1415 C CD1 . LEU A 186 ? 0.2501 0.2749 0.2600 -0.0034 0.0343 -0.0409 227 LEU A CD1 1416 C CD2 . LEU A 186 ? 0.2459 0.2723 0.2573 -0.0041 0.0396 -0.0401 227 LEU A CD2 1417 N N . TYR A 187 ? 0.2366 0.2662 0.2648 -0.0015 0.0455 -0.0462 228 TYR A N 1418 C CA . TYR A 187 ? 0.2409 0.2715 0.2754 -0.0005 0.0458 -0.0478 228 TYR A CA 1419 C C . TYR A 187 ? 0.2390 0.2714 0.2811 -0.0004 0.0447 -0.0469 228 TYR A C 1420 O O . TYR A 187 ? 0.2524 0.2857 0.2957 -0.0011 0.0448 -0.0453 228 TYR A O 1421 C CB . TYR A 187 ? 0.2410 0.2718 0.2757 -0.0001 0.0499 -0.0495 228 TYR A CB 1422 C CG . TYR A 187 ? 0.2246 0.2571 0.2638 -0.0004 0.0532 -0.0487 228 TYR A CG 1423 C CD1 . TYR A 187 ? 0.2344 0.2690 0.2826 0.0001 0.0540 -0.0494 228 TYR A CD1 1424 C CD2 . TYR A 187 ? 0.2400 0.2722 0.2753 -0.0012 0.0555 -0.0472 228 TYR A CD2 1425 C CE1 . TYR A 187 ? 0.2296 0.2661 0.2834 -0.0002 0.0571 -0.0486 228 TYR A CE1 1426 C CE2 . TYR A 187 ? 0.2269 0.2608 0.2674 -0.0015 0.0588 -0.0462 228 TYR A CE2 1427 C CZ . TYR A 187 ? 0.2469 0.2830 0.2969 -0.0011 0.0596 -0.0469 228 TYR A CZ 1428 O OH . TYR A 187 ? 0.2644 0.3023 0.3207 -0.0016 0.0627 -0.0459 228 TYR A OH 1429 N N . SER A 188 ? 0.2346 0.2676 0.2821 0.0007 0.0434 -0.0480 229 SER A N 1430 C CA . SER A 188 ? 0.2367 0.2713 0.2916 0.0013 0.0418 -0.0476 229 SER A CA 1431 C C . SER A 188 ? 0.2316 0.2682 0.2933 0.0014 0.0449 -0.0487 229 SER A C 1432 O O . SER A 188 ? 0.2447 0.2814 0.3085 0.0023 0.0462 -0.0504 229 SER A O 1433 C CB . SER A 188 ? 0.2296 0.2633 0.2861 0.0027 0.0384 -0.0479 229 SER A CB 1434 O OG . SER A 188 ? 0.2512 0.2831 0.3020 0.0026 0.0358 -0.0466 229 SER A OG 1435 N N . ASP A 189 ? 0.2355 0.2737 0.3011 0.0007 0.0461 -0.0477 230 ASP A N 1436 C CA . ASP A 189 ? 0.2548 0.2951 0.3283 0.0009 0.0492 -0.0486 230 ASP A CA 1437 C C . ASP A 189 ? 0.2556 0.2973 0.3376 0.0020 0.0463 -0.0494 230 ASP A C 1438 O O . ASP A 189 ? 0.2562 0.2978 0.3394 0.0023 0.0424 -0.0486 230 ASP A O 1439 C CB . ASP A 189 ? 0.2630 0.3044 0.3380 -0.0004 0.0522 -0.0471 230 ASP A CB 1440 C CG . ASP A 189 ? 0.2841 0.3273 0.3658 -0.0004 0.0570 -0.0479 230 ASP A CG 1441 O OD1 . ASP A 189 ? 0.2768 0.3192 0.3537 -0.0007 0.0612 -0.0477 230 ASP A OD1 1442 O OD2 . ASP A 189 ? 0.2631 0.3084 0.3544 0.0002 0.0564 -0.0487 230 ASP A OD2 1443 N N . PRO A 190 ? 0.2640 0.3070 0.3523 0.0029 0.0480 -0.0511 231 PRO A N 1444 C CA . PRO A 190 ? 0.2689 0.3133 0.3657 0.0042 0.0450 -0.0519 231 PRO A CA 1445 C C . PRO A 190 ? 0.2832 0.3293 0.3867 0.0037 0.0436 -0.0511 231 PRO A C 1446 O O . PRO A 190 ? 0.2824 0.3288 0.3904 0.0049 0.0394 -0.0514 231 PRO A O 1447 C CB . PRO A 190 ? 0.2746 0.3204 0.3773 0.0049 0.0483 -0.0537 231 PRO A CB 1448 C CG . PRO A 190 ? 0.2983 0.3425 0.3935 0.0045 0.0516 -0.0541 231 PRO A CG 1449 C CD . PRO A 190 ? 0.2697 0.3127 0.3569 0.0031 0.0523 -0.0524 231 PRO A CD 1450 N N . ALA A 191 ? 0.2793 0.3263 0.3834 0.0021 0.0469 -0.0500 232 ALA A N 1451 C CA . ALA A 191 ? 0.2936 0.3419 0.4040 0.0015 0.0454 -0.0491 232 ALA A CA 1452 C C . ALA A 191 ? 0.2880 0.3348 0.3947 0.0020 0.0399 -0.0483 232 ALA A C 1453 O O . ALA A 191 ? 0.3115 0.3593 0.4247 0.0026 0.0364 -0.0485 232 ALA A O 1454 C CB . ALA A 191 ? 0.2973 0.3461 0.4070 -0.0003 0.0500 -0.0476 232 ALA A CB 1455 N N . ASP A 192 ? 0.2842 0.3287 0.3807 0.0019 0.0389 -0.0475 233 ASP A N 1456 C CA . ASP A 192 ? 0.2761 0.3190 0.3679 0.0023 0.0345 -0.0463 233 ASP A CA 1457 C C . ASP A 192 ? 0.2726 0.3138 0.3612 0.0042 0.0310 -0.0469 233 ASP A C 1458 O O . ASP A 192 ? 0.2919 0.3317 0.3775 0.0051 0.0271 -0.0461 233 ASP A O 1459 C CB . ASP A 192 ? 0.2783 0.3197 0.3610 0.0007 0.0363 -0.0447 233 ASP A CB 1460 C CG . ASP A 192 ? 0.2615 0.3041 0.3464 -0.0010 0.0404 -0.0438 233 ASP A CG 1461 O OD1 . ASP A 192 ? 0.2949 0.3385 0.3850 -0.0015 0.0393 -0.0431 233 ASP A OD1 1462 O OD2 . ASP A 192 ? 0.2649 0.3073 0.3464 -0.0016 0.0447 -0.0438 233 ASP A OD2 1463 N N . TYR A 193 ? 0.2669 0.3081 0.3560 0.0050 0.0324 -0.0482 234 TYR A N 1464 C CA . TYR A 193 ? 0.2587 0.2980 0.3446 0.0068 0.0296 -0.0485 234 TYR A CA 1465 C C . TYR A 193 ? 0.2742 0.3142 0.3663 0.0086 0.0293 -0.0502 234 TYR A C 1466 O O . TYR A 193 ? 0.2702 0.3085 0.3595 0.0099 0.0282 -0.0505 234 TYR A O 1467 C CB . TYR A 193 ? 0.2720 0.3093 0.3491 0.0061 0.0311 -0.0479 234 TYR A CB 1468 C CG . TYR A 193 ? 0.2568 0.2931 0.3275 0.0049 0.0304 -0.0461 234 TYR A CG 1469 C CD1 . TYR A 193 ? 0.2691 0.3060 0.3375 0.0030 0.0335 -0.0455 234 TYR A CD1 1470 C CD2 . TYR A 193 ? 0.2466 0.2812 0.3138 0.0059 0.0267 -0.0448 234 TYR A CD2 1471 C CE1 . TYR A 193 ? 0.2542 0.2901 0.3170 0.0019 0.0327 -0.0438 234 TYR A CE1 1472 C CE2 . TYR A 193 ? 0.2724 0.3062 0.3343 0.0049 0.0260 -0.0432 234 TYR A CE2 1473 C CZ . TYR A 193 ? 0.2813 0.3157 0.3411 0.0028 0.0289 -0.0428 234 TYR A CZ 1474 O OH . TYR A 193 ? 0.2599 0.2935 0.3147 0.0019 0.0281 -0.0412 234 TYR A OH 1475 N N . PHE A 194 ? 0.2697 0.3122 0.3706 0.0085 0.0305 -0.0514 235 PHE A N 1476 C CA . PHE A 194 ? 0.2922 0.3354 0.3995 0.0102 0.0299 -0.0531 235 PHE A CA 1477 C C . PHE A 194 ? 0.3041 0.3494 0.4211 0.0109 0.0277 -0.0539 235 PHE A C 1478 O O . PHE A 194 ? 0.3204 0.3681 0.4435 0.0095 0.0303 -0.0542 235 PHE A O 1479 C CB . PHE A 194 ? 0.3028 0.3472 0.4119 0.0094 0.0348 -0.0543 235 PHE A CB 1480 C CG . PHE A 194 ? 0.2790 0.3237 0.3932 0.0112 0.0345 -0.0560 235 PHE A CG 1481 C CD1 . PHE A 194 ? 0.2925 0.3351 0.4018 0.0122 0.0344 -0.0564 235 PHE A CD1 1482 C CD2 . PHE A 194 ? 0.3087 0.3559 0.4334 0.0120 0.0341 -0.0573 235 PHE A CD2 1483 C CE1 . PHE A 194 ? 0.2972 0.3400 0.4113 0.0139 0.0341 -0.0579 235 PHE A CE1 1484 C CE2 . PHE A 194 ? 0.2676 0.3150 0.3971 0.0139 0.0336 -0.0590 235 PHE A CE2 1485 C CZ . PHE A 194 ? 0.2990 0.3441 0.4229 0.0148 0.0336 -0.0592 235 PHE A CZ 1486 N N . ALA A 195 ? 0.2988 0.3431 0.4170 0.0132 0.0227 -0.0542 236 ALA A N 1487 C CA . ALA A 195 ? 0.3142 0.3603 0.4416 0.0142 0.0196 -0.0553 236 ALA A CA 1488 C C . ALA A 195 ? 0.3354 0.3836 0.4723 0.0150 0.0210 -0.0573 236 ALA A C 1489 O O . ALA A 195 ? 0.3300 0.3773 0.4657 0.0165 0.0210 -0.0580 236 ALA A O 1490 C CB . ALA A 195 ? 0.3178 0.3615 0.4423 0.0170 0.0137 -0.0552 236 ALA A CB 1491 N N . PRO A 196 ? 0.3543 0.4055 0.5011 0.0139 0.0225 -0.0581 237 PRO A N 1492 C CA . PRO A 196 ? 0.3608 0.4144 0.5180 0.0146 0.0239 -0.0601 237 PRO A CA 1493 C C . PRO A 196 ? 0.3537 0.4063 0.5135 0.0179 0.0187 -0.0616 237 PRO A C 1494 O O . PRO A 196 ? 0.3572 0.4085 0.5162 0.0196 0.0133 -0.0616 237 PRO A O 1495 C CB . PRO A 196 ? 0.3769 0.4335 0.5446 0.0132 0.0247 -0.0604 237 PRO A CB 1496 C CG . PRO A 196 ? 0.3862 0.4420 0.5469 0.0107 0.0274 -0.0582 237 PRO A CG 1497 C CD . PRO A 196 ? 0.3629 0.4154 0.5125 0.0119 0.0233 -0.0572 237 PRO A CD 1498 N N . GLY A 197 ? 0.3573 0.4103 0.5196 0.0189 0.0204 -0.0627 238 GLY A N 1499 C CA . GLY A 197 ? 0.3435 0.3958 0.5095 0.0221 0.0160 -0.0642 238 GLY A CA 1500 C C . GLY A 197 ? 0.3582 0.4068 0.5145 0.0243 0.0129 -0.0634 238 GLY A C 1501 O O . GLY A 197 ? 0.3744 0.4219 0.5329 0.0274 0.0088 -0.0644 238 GLY A O 1502 N N . VAL A 198 ? 0.3199 0.3663 0.4654 0.0231 0.0148 -0.0615 239 VAL A N 1503 C CA . VAL A 198 ? 0.3057 0.3483 0.4419 0.0249 0.0127 -0.0603 239 VAL A CA 1504 C C . VAL A 198 ? 0.2918 0.3336 0.4231 0.0236 0.0173 -0.0598 239 VAL A C 1505 O O . VAL A 198 ? 0.2974 0.3408 0.4287 0.0209 0.0217 -0.0598 239 VAL A O 1506 C CB . VAL A 198 ? 0.3111 0.3514 0.4392 0.0251 0.0097 -0.0584 239 VAL A CB 1507 C CG1 A VAL A 198 ? 0.2953 0.3378 0.4285 0.0237 0.0086 -0.0587 239 VAL A CG1 1508 C CG1 B VAL A 198 ? 0.2825 0.3190 0.4005 0.0266 0.0089 -0.0567 239 VAL A CG1 1509 C CG2 A VAL A 198 ? 0.3082 0.3464 0.4261 0.0237 0.0122 -0.0564 239 VAL A CG2 1510 C CG2 B VAL A 198 ? 0.2806 0.3213 0.4134 0.0270 0.0044 -0.0592 239 VAL A CG2 1511 N N . LYS A 199 ? 0.2980 0.3372 0.4251 0.0256 0.0163 -0.0595 240 LYS A N 1512 C CA . LYS A 199 ? 0.3128 0.3510 0.4364 0.0246 0.0201 -0.0595 240 LYS A CA 1513 C C . LYS A 199 ? 0.3214 0.3573 0.4350 0.0233 0.0210 -0.0575 240 LYS A C 1514 O O . LYS A 199 ? 0.3293 0.3635 0.4383 0.0241 0.0181 -0.0560 240 LYS A O 1515 C CB . LYS A 199 ? 0.3228 0.3590 0.4474 0.0275 0.0185 -0.0601 240 LYS A CB 1516 C CG . LYS A 199 ? 0.3528 0.3915 0.4879 0.0286 0.0186 -0.0625 240 LYS A CG 1517 C CD . LYS A 199 ? 0.4263 0.4681 0.5658 0.0260 0.0238 -0.0638 240 LYS A CD 1518 C CE . LYS A 199 ? 0.4838 0.5280 0.6341 0.0272 0.0243 -0.0660 240 LYS A CE 1519 N NZ . LYS A 199 ? 0.5102 0.5575 0.6654 0.0249 0.0297 -0.0672 240 LYS A NZ 1520 N N . SER A 200 ? 0.3242 0.3600 0.4350 0.0215 0.0249 -0.0578 241 SER A N 1521 C CA . SER A 200 ? 0.3221 0.3557 0.4244 0.0202 0.0260 -0.0563 241 SER A CA 1522 C C . SER A 200 ? 0.3161 0.3464 0.4143 0.0223 0.0239 -0.0552 241 SER A C 1523 O O . SER A 200 ? 0.3121 0.3415 0.4137 0.0244 0.0231 -0.0559 241 SER A O 1524 C CB . SER A 200 ? 0.3536 0.3877 0.4550 0.0184 0.0303 -0.0576 241 SER A CB 1525 O OG . SER A 200 ? 0.3979 0.4345 0.5012 0.0164 0.0332 -0.0582 241 SER A OG 1526 N N . TYR A 201 ? 0.2862 0.3144 0.3773 0.0218 0.0233 -0.0533 242 TYR A N 1527 C CA . TYR A 201 ? 0.2784 0.3032 0.3656 0.0235 0.0222 -0.0519 242 TYR A CA 1528 C C . TYR A 201 ? 0.2828 0.3069 0.3718 0.0235 0.0246 -0.0532 242 TYR A C 1529 O O . TYR A 201 ? 0.2877 0.3130 0.3768 0.0213 0.0275 -0.0545 242 TYR A O 1530 C CB . TYR A 201 ? 0.2781 0.3012 0.3580 0.0223 0.0223 -0.0498 242 TYR A CB 1531 C CG . TYR A 201 ? 0.2536 0.2733 0.3301 0.0247 0.0204 -0.0478 242 TYR A CG 1532 C CD1 . TYR A 201 ? 0.2678 0.2863 0.3436 0.0275 0.0171 -0.0467 242 TYR A CD1 1533 C CD2 . TYR A 201 ? 0.2803 0.2977 0.3548 0.0246 0.0221 -0.0472 242 TYR A CD2 1534 C CE1 . TYR A 201 ? 0.2854 0.3004 0.3578 0.0302 0.0158 -0.0447 242 TYR A CE1 1535 C CE2 . TYR A 201 ? 0.2790 0.2931 0.3510 0.0271 0.0209 -0.0451 242 TYR A CE2 1536 C CZ . TYR A 201 ? 0.3005 0.3133 0.3710 0.0299 0.0179 -0.0437 242 TYR A CZ 1537 O OH . TYR A 201 ? 0.3573 0.3665 0.4249 0.0326 0.0172 -0.0415 242 TYR A OH 1538 N N . PRO A 202 ? 0.2952 0.3169 0.3852 0.0260 0.0235 -0.0528 243 PRO A N 1539 C CA . PRO A 202 ? 0.2958 0.3148 0.3841 0.0292 0.0204 -0.0509 243 PRO A CA 1540 C C . PRO A 202 ? 0.3120 0.3319 0.4050 0.0317 0.0175 -0.0518 243 PRO A C 1541 O O . PRO A 202 ? 0.3282 0.3456 0.4192 0.0348 0.0147 -0.0503 243 PRO A O 1542 C CB . PRO A 202 ? 0.3043 0.3203 0.3917 0.0303 0.0215 -0.0503 243 PRO A CB 1543 C CG . PRO A 202 ? 0.3038 0.3217 0.3963 0.0289 0.0242 -0.0530 243 PRO A CG 1544 C CD . PRO A 202 ? 0.3027 0.3238 0.3949 0.0258 0.0259 -0.0542 243 PRO A CD 1545 N N . ASP A 203 ? 0.3067 0.3300 0.4058 0.0307 0.0182 -0.0540 244 ASP A N 1546 C CA . ASP A 203 ? 0.3316 0.3559 0.4368 0.0330 0.0156 -0.0552 244 ASP A CA 1547 C C . ASP A 203 ? 0.3232 0.3491 0.4293 0.0331 0.0127 -0.0552 244 ASP A C 1548 O O . ASP A 203 ? 0.3188 0.3454 0.4298 0.0353 0.0097 -0.0562 244 ASP A O 1549 C CB . ASP A 203 ? 0.3392 0.3662 0.4518 0.0321 0.0180 -0.0577 244 ASP A CB 1550 C CG . ASP A 203 ? 0.3957 0.4210 0.5077 0.0322 0.0205 -0.0581 244 ASP A CG 1551 O OD1 . ASP A 203 ? 0.4363 0.4582 0.5460 0.0348 0.0190 -0.0569 244 ASP A OD1 1552 O OD2 . ASP A 203 ? 0.4913 0.5181 0.6043 0.0298 0.0241 -0.0594 244 ASP A OD2 1553 N N . GLY A 204 ? 0.3074 0.3338 0.4091 0.0309 0.0135 -0.0540 245 GLY A N 1554 C CA . GLY A 204 ? 0.2936 0.3211 0.3957 0.0310 0.0107 -0.0538 245 GLY A CA 1555 C C . GLY A 204 ? 0.2913 0.3180 0.3863 0.0288 0.0119 -0.0520 245 GLY A C 1556 O O . GLY A 204 ? 0.3108 0.3357 0.4006 0.0281 0.0140 -0.0508 245 GLY A O 1557 N N . TRP A 205 ? 0.2761 0.3042 0.3714 0.0279 0.0104 -0.0519 246 TRP A N 1558 C CA . TRP A 205 ? 0.2596 0.2867 0.3478 0.0263 0.0108 -0.0500 246 TRP A CA 1559 C C . TRP A 205 ? 0.2644 0.2941 0.3532 0.0226 0.0142 -0.0503 246 TRP A C 1560 O O . TRP A 205 ? 0.2464 0.2756 0.3300 0.0211 0.0144 -0.0489 246 TRP A O 1561 C CB . TRP A 205 ? 0.2631 0.2888 0.3488 0.0284 0.0065 -0.0491 246 TRP A CB 1562 C CG . TRP A 205 ? 0.2990 0.3269 0.3919 0.0293 0.0036 -0.0508 246 TRP A CG 1563 C CD1 . TRP A 205 ? 0.3406 0.3679 0.4378 0.0325 0.0002 -0.0521 246 TRP A CD1 1564 C CD2 . TRP A 205 ? 0.2893 0.3200 0.3863 0.0270 0.0037 -0.0515 246 TRP A CD2 1565 N NE1 . TRP A 205 ? 0.3265 0.3564 0.4308 0.0323 -0.0021 -0.0538 246 TRP A NE1 1566 C CE2 . TRP A 205 ? 0.2866 0.3184 0.3910 0.0289 0.0002 -0.0534 246 TRP A CE2 1567 C CE3 . TRP A 205 ? 0.2840 0.3161 0.3791 0.0237 0.0064 -0.0508 246 TRP A CE3 1568 C CZ2 . TRP A 205 ? 0.2738 0.3083 0.3846 0.0274 -0.0005 -0.0544 246 TRP A CZ2 1569 C CZ3 . TRP A 205 ? 0.3029 0.3375 0.4037 0.0223 0.0060 -0.0516 246 TRP A CZ3 1570 C CH2 . TRP A 205 ? 0.2841 0.3200 0.3931 0.0240 0.0026 -0.0534 246 TRP A CH2 1571 N N . ASN A 206 ? 0.2495 0.2815 0.3437 0.0212 0.0171 -0.0520 247 ASN A N 1572 C CA . ASN A 206 ? 0.2540 0.2881 0.3482 0.0180 0.0209 -0.0523 247 ASN A CA 1573 C C . ASN A 206 ? 0.2454 0.2783 0.3337 0.0165 0.0239 -0.0518 247 ASN A C 1574 O O . ASN A 206 ? 0.2447 0.2755 0.3309 0.0176 0.0239 -0.0518 247 ASN A O 1575 C CB . ASN A 206 ? 0.2622 0.2994 0.3651 0.0173 0.0231 -0.0543 247 ASN A CB 1576 C CG . ASN A 206 ? 0.2786 0.3180 0.3872 0.0170 0.0216 -0.0546 247 ASN A CG 1577 O OD1 . ASN A 206 ? 0.2629 0.3017 0.3684 0.0167 0.0194 -0.0533 247 ASN A OD1 1578 N ND2 . ASN A 206 ? 0.2755 0.3175 0.3934 0.0170 0.0227 -0.0563 247 ASN A ND2 1579 N N . LEU A 207 ? 0.2516 0.2855 0.3371 0.0139 0.0264 -0.0515 248 LEU A N 1580 C CA . LEU A 207 ? 0.2470 0.2797 0.3268 0.0125 0.0290 -0.0514 248 LEU A CA 1581 C C . LEU A 207 ? 0.2452 0.2790 0.3284 0.0121 0.0323 -0.0534 248 LEU A C 1582 O O . LEU A 207 ? 0.2511 0.2873 0.3389 0.0113 0.0344 -0.0543 248 LEU A O 1583 C CB . LEU A 207 ? 0.2480 0.2814 0.3237 0.0102 0.0303 -0.0504 248 LEU A CB 1584 C CG . LEU A 207 ? 0.2427 0.2746 0.3116 0.0088 0.0322 -0.0502 248 LEU A CG 1585 C CD1 . LEU A 207 ? 0.2343 0.2636 0.2986 0.0097 0.0299 -0.0489 248 LEU A CD1 1586 C CD2 . LEU A 207 ? 0.2734 0.3062 0.3390 0.0068 0.0337 -0.0495 248 LEU A CD2 1587 N N . PRO A 208 ? 0.2495 0.2815 0.3307 0.0127 0.0329 -0.0540 249 PRO A N 1588 C CA . PRO A 208 ? 0.2475 0.2800 0.3306 0.0123 0.0361 -0.0560 249 PRO A CA 1589 C C . PRO A 208 ? 0.2538 0.2866 0.3322 0.0103 0.0391 -0.0564 249 PRO A C 1590 O O . PRO A 208 ? 0.2550 0.2870 0.3278 0.0091 0.0384 -0.0550 249 PRO A O 1591 C CB . PRO A 208 ? 0.2568 0.2869 0.3386 0.0135 0.0353 -0.0563 249 PRO A CB 1592 C CG . PRO A 208 ? 0.2805 0.3085 0.3582 0.0141 0.0325 -0.0542 249 PRO A CG 1593 C CD . PRO A 208 ? 0.2529 0.2822 0.3308 0.0140 0.0306 -0.0528 249 PRO A CD 1594 N N . GLY A 209 ? 0.2372 0.2708 0.3172 0.0100 0.0424 -0.0583 250 GLY A N 1595 C CA . GLY A 209 ? 0.2524 0.2861 0.3275 0.0085 0.0454 -0.0587 250 GLY A CA 1596 C C . GLY A 209 ? 0.2404 0.2716 0.3081 0.0079 0.0447 -0.0587 250 GLY A C 1597 O O . GLY A 209 ? 0.2627 0.2935 0.3250 0.0068 0.0462 -0.0587 250 GLY A O 1598 N N . GLY A 210 ? 0.2374 0.2668 0.3053 0.0088 0.0426 -0.0589 251 GLY A N 1599 C CA . GLY A 210 ? 0.2363 0.2632 0.2985 0.0083 0.0415 -0.0589 251 GLY A CA 1600 C C . GLY A 210 ? 0.2409 0.2670 0.3001 0.0079 0.0387 -0.0564 251 GLY A C 1601 O O . GLY A 210 ? 0.2458 0.2701 0.3009 0.0074 0.0378 -0.0561 251 GLY A O 1602 N N . GLY A 211 ? 0.2374 0.2647 0.2990 0.0083 0.0374 -0.0547 252 GLY A N 1603 C CA . GLY A 211 ? 0.2291 0.2556 0.2878 0.0082 0.0347 -0.0523 252 GLY A CA 1604 C C . GLY A 211 ? 0.2313 0.2581 0.2848 0.0065 0.0352 -0.0516 252 GLY A C 1605 O O . GLY A 211 ? 0.2302 0.2584 0.2834 0.0056 0.0374 -0.0523 252 GLY A O 1606 N N . VAL A 212 ? 0.2194 0.2449 0.2689 0.0061 0.0334 -0.0500 253 VAL A N 1607 C CA . VAL A 212 ? 0.2097 0.2352 0.2539 0.0046 0.0336 -0.0492 253 VAL A CA 1608 C C . VAL A 212 ? 0.2107 0.2355 0.2531 0.0048 0.0310 -0.0468 253 VAL A C 1609 O O . VAL A 212 ? 0.2148 0.2381 0.2576 0.0059 0.0294 -0.0459 253 VAL A O 1610 C CB . VAL A 212 ? 0.2160 0.2400 0.2559 0.0038 0.0342 -0.0504 253 VAL A CB 1611 C CG1 . VAL A 212 ? 0.2460 0.2701 0.2804 0.0024 0.0346 -0.0500 253 VAL A CG1 1612 C CG2 . VAL A 212 ? 0.2263 0.2503 0.2678 0.0041 0.0365 -0.0531 253 VAL A CG2 1613 N N . GLN A 213 ? 0.2033 0.2291 0.2434 0.0038 0.0309 -0.0457 254 GLN A N 1614 C CA . GLN A 213 ? 0.1886 0.2137 0.2265 0.0040 0.0286 -0.0435 254 GLN A CA 1615 C C . GLN A 213 ? 0.1966 0.2205 0.2290 0.0029 0.0283 -0.0429 254 GLN A C 1616 O O . GLN A 213 ? 0.2193 0.2437 0.2484 0.0015 0.0295 -0.0434 254 GLN A O 1617 C CB . GLN A 213 ? 0.1916 0.2184 0.2305 0.0034 0.0286 -0.0428 254 GLN A CB 1618 C CG . GLN A 213 ? 0.1804 0.2066 0.2167 0.0036 0.0261 -0.0407 254 GLN A CG 1619 C CD . GLN A 213 ? 0.2153 0.2429 0.2522 0.0026 0.0263 -0.0401 254 GLN A CD 1620 O OE1 . GLN A 213 ? 0.2174 0.2445 0.2507 0.0020 0.0253 -0.0386 254 GLN A OE1 1621 N NE2 . GLN A 213 ? 0.2081 0.2374 0.2503 0.0027 0.0274 -0.0410 254 GLN A NE2 1622 N N . ARG A 214 ? 0.2026 0.2249 0.2342 0.0036 0.0267 -0.0419 255 ARG A N 1623 C CA . ARG A 214 ? 0.1964 0.2176 0.2238 0.0028 0.0259 -0.0409 255 ARG A CA 1624 C C . ARG A 214 ? 0.1893 0.2109 0.2141 0.0024 0.0246 -0.0390 255 ARG A C 1625 O O . ARG A 214 ? 0.2020 0.2243 0.2285 0.0031 0.0240 -0.0383 255 ARG A O 1626 C CB . ARG A 214 ? 0.1861 0.2055 0.2147 0.0038 0.0249 -0.0401 255 ARG A CB 1627 C CG . ARG A 214 ? 0.1908 0.2094 0.2219 0.0039 0.0260 -0.0420 255 ARG A CG 1628 C CD . ARG A 214 ? 0.2038 0.2206 0.2377 0.0055 0.0254 -0.0409 255 ARG A CD 1629 N NE . ARG A 214 ? 0.2267 0.2429 0.2640 0.0057 0.0265 -0.0428 255 ARG A NE 1630 C CZ . ARG A 214 ? 0.2514 0.2683 0.2916 0.0065 0.0274 -0.0442 255 ARG A CZ 1631 N NH1 . ARG A 214 ? 0.2279 0.2463 0.2684 0.0069 0.0274 -0.0440 255 ARG A NH1 1632 N NH2 . ARG A 214 ? 0.2097 0.2257 0.2528 0.0067 0.0283 -0.0460 255 ARG A NH2 1633 N N . GLY A 215 ? 0.1920 0.2129 0.2129 0.0014 0.0240 -0.0383 256 GLY A N 1634 C CA . GLY A 215 ? 0.1940 0.2150 0.2123 0.0013 0.0227 -0.0363 256 GLY A CA 1635 C C . GLY A 215 ? 0.1978 0.2186 0.2117 -0.0001 0.0226 -0.0362 256 GLY A C 1636 O O . GLY A 215 ? 0.1794 0.2004 0.1916 -0.0011 0.0238 -0.0377 256 GLY A O 1637 N N . ASN A 216 ? 0.1896 0.2099 0.2014 -0.0001 0.0210 -0.0343 257 ASN A N 1638 C CA . ASN A 216 ? 0.1860 0.2060 0.1936 -0.0013 0.0206 -0.0340 257 ASN A CA 1639 C C . ASN A 216 ? 0.1869 0.2078 0.1922 -0.0022 0.0214 -0.0339 257 ASN A C 1640 O O . ASN A 216 ? 0.2002 0.2221 0.2076 -0.0020 0.0218 -0.0335 257 ASN A O 1641 C CB . ASN A 216 ? 0.1629 0.1819 0.1692 -0.0009 0.0189 -0.0320 257 ASN A CB 1642 C CG . ASN A 216 ? 0.1424 0.1617 0.1475 -0.0005 0.0179 -0.0302 257 ASN A CG 1643 O OD1 . ASN A 216 ? 0.1862 0.2060 0.1885 -0.0016 0.0179 -0.0299 257 ASN A OD1 1644 N ND2 . ASN A 216 ? 0.1890 0.2077 0.1957 0.0011 0.0170 -0.0289 257 ASN A ND2 1645 N N . ILE A 217 ? 0.1868 0.2074 0.1880 -0.0033 0.0216 -0.0344 258 ILE A N 1646 C CA . ILE A 217 ? 0.1950 0.2160 0.1931 -0.0041 0.0227 -0.0342 258 ILE A CA 1647 C C . ILE A 217 ? 0.2081 0.2285 0.2020 -0.0047 0.0213 -0.0327 258 ILE A C 1648 O O . ILE A 217 ? 0.2150 0.2351 0.2048 -0.0054 0.0221 -0.0328 258 ILE A O 1649 C CB . ILE A 217 ? 0.1979 0.2188 0.1941 -0.0045 0.0248 -0.0362 258 ILE A CB 1650 C CG1 . ILE A 217 ? 0.1928 0.2125 0.1871 -0.0044 0.0237 -0.0377 258 ILE A CG1 1651 C CG2 . ILE A 217 ? 0.2003 0.2222 0.2010 -0.0040 0.0266 -0.0374 258 ILE A CG2 1652 C CD1 . ILE A 217 ? 0.2624 0.2814 0.2524 -0.0045 0.0253 -0.0399 258 ILE A CD1 1653 N N . LEU A 218 ? 0.1955 0.2156 0.1901 -0.0042 0.0194 -0.0313 259 LEU A N 1654 C CA . LEU A 218 ? 0.2122 0.2316 0.2033 -0.0047 0.0179 -0.0298 259 LEU A CA 1655 C C . LEU A 218 ? 0.1979 0.2178 0.1884 -0.0049 0.0180 -0.0284 259 LEU A C 1656 O O . LEU A 218 ? 0.2095 0.2301 0.2032 -0.0046 0.0186 -0.0282 259 LEU A O 1657 C CB . LEU A 218 ? 0.1983 0.2172 0.1909 -0.0038 0.0161 -0.0286 259 LEU A CB 1658 C CG . LEU A 218 ? 0.2043 0.2226 0.1984 -0.0036 0.0158 -0.0297 259 LEU A CG 1659 C CD1 . LEU A 218 ? 0.2058 0.2235 0.2021 -0.0026 0.0148 -0.0281 259 LEU A CD1 1660 C CD2 . LEU A 218 ? 0.2138 0.2316 0.2047 -0.0045 0.0152 -0.0309 259 LEU A CD2 1661 N N . ASN A 219 ? 0.1963 0.2157 0.1830 -0.0055 0.0172 -0.0272 260 ASN A N 1662 C CA . ASN A 219 ? 0.2004 0.2198 0.1864 -0.0057 0.0168 -0.0256 260 ASN A CA 1663 C C . ASN A 219 ? 0.1885 0.2072 0.1728 -0.0054 0.0146 -0.0242 260 ASN A C 1664 O O . ASN A 219 ? 0.1973 0.2154 0.1778 -0.0059 0.0140 -0.0234 260 ASN A O 1665 C CB . ASN A 219 ? 0.2209 0.2402 0.2037 -0.0067 0.0185 -0.0255 260 ASN A CB 1666 C CG . ASN A 219 ? 0.2372 0.2574 0.2228 -0.0069 0.0210 -0.0264 260 ASN A CG 1667 O OD1 . ASN A 219 ? 0.2530 0.2740 0.2422 -0.0070 0.0215 -0.0258 260 ASN A OD1 1668 N ND2 . ASN A 219 ? 0.2265 0.2466 0.2110 -0.0069 0.0224 -0.0281 260 ASN A ND2 1669 N N . LEU A 220 ? 0.1852 0.2038 0.1720 -0.0043 0.0135 -0.0237 261 LEU A N 1670 C CA . LEU A 220 ? 0.1845 0.2023 0.1700 -0.0037 0.0117 -0.0223 261 LEU A CA 1671 C C . LEU A 220 ? 0.1835 0.2010 0.1679 -0.0034 0.0106 -0.0207 261 LEU A C 1672 O O . LEU A 220 ? 0.1750 0.1919 0.1575 -0.0032 0.0094 -0.0195 261 LEU A O 1673 C CB . LEU A 220 ? 0.1761 0.1936 0.1646 -0.0022 0.0113 -0.0220 261 LEU A CB 1674 C CG . LEU A 220 ? 0.1810 0.1985 0.1713 -0.0023 0.0122 -0.0234 261 LEU A CG 1675 C CD1 . LEU A 220 ? 0.1612 0.1780 0.1545 -0.0006 0.0121 -0.0227 261 LEU A CD1 1676 C CD2 . LEU A 220 ? 0.1950 0.2121 0.1834 -0.0031 0.0114 -0.0235 261 LEU A CD2 1677 N N . ASN A 221 ? 0.1786 0.1965 0.1647 -0.0034 0.0109 -0.0207 262 ASN A N 1678 C CA . ASN A 221 ? 0.1977 0.2152 0.1835 -0.0030 0.0095 -0.0194 262 ASN A CA 1679 C C . ASN A 221 ? 0.1924 0.2089 0.1775 -0.0013 0.0077 -0.0182 262 ASN A C 1680 O O . ASN A 221 ? 0.1922 0.2081 0.1752 -0.0012 0.0065 -0.0170 262 ASN A O 1681 C CB . ASN A 221 ? 0.1995 0.2168 0.1821 -0.0044 0.0098 -0.0187 262 ASN A CB 1682 C CG . ASN A 221 ? 0.2245 0.2425 0.2077 -0.0056 0.0119 -0.0194 262 ASN A CG 1683 O OD1 . ASN A 221 ? 0.2420 0.2608 0.2290 -0.0055 0.0128 -0.0202 262 ASN A OD1 1684 N ND2 . ASN A 221 ? 0.2549 0.2724 0.2342 -0.0066 0.0128 -0.0192 262 ASN A ND2 1685 N N . GLY A 222 ? 0.1700 0.1862 0.1567 0.0000 0.0078 -0.0185 263 GLY A N 1686 C CA . GLY A 222 ? 0.1740 0.1890 0.1599 0.0020 0.0065 -0.0172 263 GLY A CA 1687 C C . GLY A 222 ? 0.1798 0.1943 0.1645 0.0020 0.0068 -0.0164 263 GLY A C 1688 O O . GLY A 222 ? 0.1803 0.1937 0.1645 0.0038 0.0062 -0.0151 263 GLY A O 1689 N N . ALA A 223 ? 0.1579 0.1732 0.1425 0.0004 0.0076 -0.0172 264 ALA A N 1690 C CA . ALA A 223 ? 0.1717 0.1866 0.1556 0.0003 0.0074 -0.0165 264 ALA A CA 1691 C C . ALA A 223 ? 0.1792 0.1935 0.1658 0.0016 0.0081 -0.0161 264 ALA A C 1692 O O . ALA A 223 ? 0.1968 0.2107 0.1837 0.0020 0.0079 -0.0150 264 ALA A O 1693 C CB . ALA A 223 ? 0.1688 0.1844 0.1515 -0.0016 0.0075 -0.0177 264 ALA A CB 1694 N N . GLY A 224 ? 0.1708 0.1852 0.1597 0.0021 0.0090 -0.0170 265 GLY A N 1695 C CA . GLY A 224 ? 0.1754 0.1892 0.1672 0.0031 0.0101 -0.0167 265 GLY A CA 1696 C C . GLY A 224 ? 0.1847 0.1991 0.1784 0.0015 0.0106 -0.0181 265 GLY A C 1697 O O . GLY A 224 ? 0.1863 0.2016 0.1791 0.0000 0.0105 -0.0199 265 GLY A O 1698 N N . ASP A 225 ? 0.1616 0.1754 0.1581 0.0020 0.0111 -0.0174 266 ASP A N 1699 C CA . ASP A 225 ? 0.1726 0.1870 0.1717 0.0006 0.0111 -0.0191 266 ASP A CA 1700 C C . ASP A 225 ? 0.1737 0.1889 0.1698 -0.0011 0.0097 -0.0204 266 ASP A C 1701 O O . ASP A 225 ? 0.1896 0.2047 0.1834 -0.0012 0.0087 -0.0193 266 ASP A O 1702 C CB . ASP A 225 ? 0.1767 0.1904 0.1794 0.0012 0.0115 -0.0178 266 ASP A CB 1703 C CG . ASP A 225 ? 0.1961 0.2103 0.2019 -0.0002 0.0108 -0.0196 266 ASP A CG 1704 O OD1 . ASP A 225 ? 0.2014 0.2159 0.2081 -0.0011 0.0109 -0.0219 266 ASP A OD1 1705 O OD2 . ASP A 225 ? 0.2021 0.2163 0.2098 -0.0003 0.0103 -0.0187 266 ASP A OD2 1706 N N . PRO A 226 ? 0.1837 0.1994 0.1794 -0.0023 0.0098 -0.0228 267 PRO A N 1707 C CA . PRO A 226 ? 0.1948 0.2108 0.1867 -0.0035 0.0086 -0.0239 267 PRO A CA 1708 C C . PRO A 226 ? 0.1891 0.2049 0.1811 -0.0039 0.0069 -0.0237 267 PRO A C 1709 O O . PRO A 226 ? 0.2092 0.2251 0.1971 -0.0045 0.0058 -0.0238 267 PRO A O 1710 C CB . PRO A 226 ? 0.2052 0.2213 0.1975 -0.0042 0.0090 -0.0266 267 PRO A CB 1711 C CG . PRO A 226 ? 0.2032 0.2194 0.1978 -0.0035 0.0107 -0.0266 267 PRO A CG 1712 C CD . PRO A 226 ? 0.1995 0.2152 0.1971 -0.0022 0.0110 -0.0242 267 PRO A CD 1713 N N . LEU A 227 ? 0.2003 0.2160 0.1971 -0.0035 0.0069 -0.0234 268 LEU A N 1714 C CA . LEU A 227 ? 0.2006 0.2163 0.1986 -0.0039 0.0052 -0.0236 268 LEU A CA 1715 C C . LEU A 227 ? 0.1949 0.2105 0.1930 -0.0032 0.0049 -0.0210 268 LEU A C 1716 O O . LEU A 227 ? 0.1928 0.2085 0.1917 -0.0035 0.0033 -0.0210 268 LEU A O 1717 C CB . LEU A 227 ? 0.1859 0.2015 0.1902 -0.0040 0.0051 -0.0248 268 LEU A CB 1718 C CG . LEU A 227 ? 0.1913 0.2068 0.1960 -0.0046 0.0053 -0.0277 268 LEU A CG 1719 C CD1 . LEU A 227 ? 0.2364 0.2516 0.2482 -0.0046 0.0050 -0.0288 268 LEU A CD1 1720 C CD2 . LEU A 227 ? 0.2335 0.2489 0.2326 -0.0053 0.0035 -0.0299 268 LEU A CD2 1721 N N . THR A 228 ? 0.1839 0.1991 0.1814 -0.0020 0.0063 -0.0189 269 THR A N 1722 C CA . THR A 228 ? 0.1896 0.2046 0.1874 -0.0010 0.0063 -0.0164 269 THR A CA 1723 C C . THR A 228 ? 0.1867 0.2012 0.1798 -0.0002 0.0063 -0.0149 269 THR A C 1724 O O . THR A 228 ? 0.1791 0.1929 0.1726 0.0015 0.0073 -0.0129 269 THR A O 1725 C CB . THR A 228 ? 0.1810 0.1953 0.1839 0.0004 0.0082 -0.0148 269 THR A CB 1726 O OG1 . THR A 228 ? 0.1809 0.1946 0.1837 0.0014 0.0097 -0.0146 269 THR A OG1 1727 C CG2 . THR A 228 ? 0.1833 0.1979 0.1922 -0.0004 0.0080 -0.0160 269 THR A CG2 1728 N N . PRO A 229 ? 0.1819 0.1968 0.1708 -0.0012 0.0054 -0.0158 270 PRO A N 1729 C CA . PRO A 229 ? 0.1847 0.1992 0.1701 -0.0005 0.0053 -0.0145 270 PRO A CA 1730 C C . PRO A 229 ? 0.1828 0.1967 0.1675 0.0007 0.0048 -0.0124 270 PRO A C 1731 O O . PRO A 229 ? 0.2159 0.2300 0.2006 0.0001 0.0037 -0.0122 270 PRO A O 1732 C CB . PRO A 229 ? 0.1981 0.2130 0.1798 -0.0019 0.0045 -0.0156 270 PRO A CB 1733 C CG . PRO A 229 ? 0.1846 0.1998 0.1666 -0.0030 0.0035 -0.0170 270 PRO A CG 1734 C CD . PRO A 229 ? 0.1792 0.1946 0.1660 -0.0027 0.0042 -0.0178 270 PRO A CD 1735 N N . GLY A 230 ? 0.1763 0.1893 0.1605 0.0025 0.0054 -0.0110 271 GLY A N 1736 C CA . GLY A 230 ? 0.1868 0.1990 0.1697 0.0040 0.0050 -0.0090 271 GLY A CA 1737 C C . GLY A 230 ? 0.1920 0.2034 0.1778 0.0057 0.0064 -0.0074 271 GLY A C 1738 O O . GLY A 230 ? 0.2158 0.2260 0.2001 0.0077 0.0066 -0.0056 271 GLY A O 1739 N N . TYR A 231 ? 0.1747 0.1865 0.1648 0.0053 0.0076 -0.0079 272 TYR A N 1740 C CA . TYR A 231 ? 0.1904 0.2015 0.1843 0.0067 0.0093 -0.0062 272 TYR A CA 1741 C C . TYR A 231 ? 0.1827 0.1935 0.1803 0.0070 0.0110 -0.0066 272 TYR A C 1742 O O . TYR A 231 ? 0.1836 0.1952 0.1821 0.0054 0.0106 -0.0087 272 TYR A O 1743 C CB . TYR A 231 ? 0.1804 0.1925 0.1775 0.0054 0.0084 -0.0064 272 TYR A CB 1744 C CG . TYR A 231 ? 0.1911 0.2035 0.1844 0.0048 0.0065 -0.0063 272 TYR A CG 1745 C CD1 . TYR A 231 ? 0.2012 0.2127 0.1928 0.0066 0.0068 -0.0042 272 TYR A CD1 1746 C CD2 . TYR A 231 ? 0.1905 0.2039 0.1813 0.0028 0.0045 -0.0082 272 TYR A CD2 1747 C CE1 . TYR A 231 ? 0.1952 0.2069 0.1834 0.0062 0.0049 -0.0040 272 TYR A CE1 1748 C CE2 . TYR A 231 ? 0.1900 0.2034 0.1771 0.0025 0.0028 -0.0078 272 TYR A CE2 1749 C CZ . TYR A 231 ? 0.1872 0.1998 0.1733 0.0041 0.0029 -0.0058 272 TYR A CZ 1750 O OH . TYR A 231 ? 0.2139 0.2264 0.1964 0.0037 0.0013 -0.0055 272 TYR A OH 1751 N N . PRO A 232 ? 0.1923 0.2016 0.1917 0.0092 0.0132 -0.0045 273 PRO A N 1752 C CA . PRO A 232 ? 0.1900 0.1988 0.1930 0.0096 0.0150 -0.0048 273 PRO A CA 1753 C C . PRO A 232 ? 0.1957 0.2057 0.2049 0.0077 0.0151 -0.0061 273 PRO A C 1754 O O . PRO A 232 ? 0.1941 0.2047 0.2065 0.0070 0.0149 -0.0056 273 PRO A O 1755 C CB . PRO A 232 ? 0.1828 0.1895 0.1860 0.0127 0.0175 -0.0018 273 PRO A CB 1756 C CG . PRO A 232 ? 0.1977 0.2044 0.2006 0.0133 0.0174 -0.0001 273 PRO A CG 1757 C CD . PRO A 232 ? 0.2113 0.2193 0.2097 0.0116 0.0144 -0.0018 273 PRO A CD 1758 N N . ALA A 233 ? 0.1875 0.1976 0.1986 0.0070 0.0155 -0.0077 274 ALA A N 1759 C CA . ALA A 233 ? 0.1869 0.1979 0.2038 0.0051 0.0154 -0.0095 274 ALA A CA 1760 C C . ALA A 233 ? 0.2006 0.2104 0.2239 0.0064 0.0180 -0.0075 274 ALA A C 1761 O O . ALA A 233 ? 0.2041 0.2133 0.2310 0.0066 0.0195 -0.0077 274 ALA A O 1762 C CB . ALA A 233 ? 0.1939 0.2053 0.2099 0.0041 0.0149 -0.0119 274 ALA A CB 1763 N N . ASN A 234 ? 0.2125 0.2221 0.2375 0.0073 0.0188 -0.0053 275 ASN A N 1764 C CA . ASN A 234 ? 0.2453 0.2536 0.2764 0.0087 0.0219 -0.0028 275 ASN A CA 1765 C C . ASN A 234 ? 0.2646 0.2742 0.3043 0.0067 0.0213 -0.0043 275 ASN A C 1766 O O . ASN A 234 ? 0.2401 0.2511 0.2800 0.0044 0.0185 -0.0075 275 ASN A O 1767 C CB . ASN A 234 ? 0.2458 0.2531 0.2745 0.0109 0.0234 0.0004 275 ASN A CB 1768 C CG . ASN A 234 ? 0.2666 0.2754 0.2947 0.0097 0.0211 -0.0003 275 ASN A CG 1769 O OD1 . ASN A 234 ? 0.2745 0.2851 0.3065 0.0073 0.0190 -0.0025 275 ASN A OD1 1770 N ND2 . ASN A 234 ? 0.3152 0.3233 0.3382 0.0114 0.0213 0.0017 275 ASN A ND2 1771 N N A GLU A 235 ? 0.2762 0.2851 0.3228 0.0076 0.0239 -0.0020 276 GLU A N 1772 N N B GLU A 235 ? 0.2800 0.2889 0.3270 0.0075 0.0239 -0.0022 276 GLU A N 1773 C CA A GLU A 235 ? 0.2924 0.3021 0.3491 0.0060 0.0239 -0.0031 276 GLU A CA 1774 C CA B GLU A 235 ? 0.2967 0.3067 0.3531 0.0055 0.0232 -0.0040 276 GLU A CA 1775 C C A GLU A 235 ? 0.2901 0.3019 0.3492 0.0040 0.0206 -0.0052 276 GLU A C 1776 C C B GLU A 235 ? 0.2955 0.3075 0.3526 0.0037 0.0197 -0.0061 276 GLU A C 1777 O O A GLU A 235 ? 0.2941 0.3069 0.3604 0.0023 0.0190 -0.0076 276 GLU A O 1778 O O B GLU A 235 ? 0.3086 0.3217 0.3692 0.0017 0.0171 -0.0093 276 GLU A O 1779 C CB A GLU A 235 ? 0.3016 0.3099 0.3652 0.0078 0.0281 0.0005 276 GLU A CB 1780 C CB B GLU A 235 ? 0.3095 0.3184 0.3748 0.0067 0.0270 -0.0011 276 GLU A CB 1781 C CG A GLU A 235 ? 0.3258 0.3336 0.3990 0.0071 0.0297 0.0001 276 GLU A CG 1782 C CG B GLU A 235 ? 0.3588 0.3657 0.4257 0.0078 0.0298 -0.0001 276 GLU A CG 1783 C CD A GLU A 235 ? 0.3582 0.3642 0.4285 0.0082 0.0315 0.0004 276 GLU A CD 1784 C CD B GLU A 235 ? 0.3960 0.4035 0.4719 0.0059 0.0291 -0.0026 276 GLU A CD 1785 O OE1 A GLU A 235 ? 0.3786 0.3825 0.4444 0.0109 0.0345 0.0036 276 GLU A OE1 1786 O OE1 B GLU A 235 ? 0.4005 0.4099 0.4805 0.0036 0.0259 -0.0056 276 GLU A OE1 1787 O OE2 A GLU A 235 ? 0.3249 0.3315 0.3972 0.0065 0.0298 -0.0026 276 GLU A OE2 1788 O OE2 B GLU A 235 ? 0.4281 0.4340 0.5068 0.0067 0.0316 -0.0017 276 GLU A OE2 1789 N N . TYR A 236 ? 0.2790 0.2912 0.3324 0.0045 0.0195 -0.0044 277 TYR A N 1790 C CA . TYR A 236 ? 0.2766 0.2906 0.3315 0.0029 0.0162 -0.0061 277 TYR A CA 1791 C C . TYR A 236 ? 0.2797 0.2944 0.3257 0.0020 0.0129 -0.0082 277 TYR A C 1792 O O . TYR A 236 ? 0.2773 0.2931 0.3223 0.0012 0.0103 -0.0092 277 TYR A O 1793 C CB . TYR A 236 ? 0.2861 0.3001 0.3440 0.0042 0.0178 -0.0032 277 TYR A CB 1794 C CG . TYR A 236 ? 0.2671 0.2798 0.3170 0.0064 0.0196 -0.0004 277 TYR A CG 1795 C CD1 . TYR A 236 ? 0.2952 0.3084 0.3376 0.0062 0.0171 -0.0010 277 TYR A CD1 1796 C CD2 . TYR A 236 ? 0.2550 0.2657 0.3048 0.0089 0.0237 0.0028 277 TYR A CD2 1797 C CE1 . TYR A 236 ? 0.3056 0.3176 0.3408 0.0083 0.0183 0.0013 277 TYR A CE1 1798 C CE2 . TYR A 236 ? 0.3069 0.3161 0.3487 0.0113 0.0249 0.0050 277 TYR A CE2 1799 C CZ . TYR A 236 ? 0.3166 0.3265 0.3513 0.0108 0.0219 0.0040 277 TYR A CZ 1800 O OH . TYR A 236 ? 0.3523 0.3607 0.3795 0.0132 0.0228 0.0060 277 TYR A OH 1801 N N . ALA A 237 ? 0.2569 0.2710 0.2967 0.0021 0.0130 -0.0090 278 ALA A N 1802 C CA . ALA A 237 ? 0.2736 0.2882 0.3050 0.0014 0.0105 -0.0104 278 ALA A CA 1803 C C . ALA A 237 ? 0.2707 0.2865 0.3028 -0.0006 0.0071 -0.0137 278 ALA A C 1804 O O . ALA A 237 ? 0.2982 0.3142 0.3360 -0.0015 0.0066 -0.0157 278 ALA A O 1805 C CB . ALA A 237 ? 0.2711 0.2849 0.2974 0.0018 0.0113 -0.0109 278 ALA A CB 1806 N N . TYR A 238 ? 0.2800 0.2963 0.3064 -0.0010 0.0048 -0.0143 279 TYR A N 1807 C CA . TYR A 238 ? 0.2845 0.3014 0.3090 -0.0025 0.0015 -0.0174 279 TYR A CA 1808 C C . TYR A 238 ? 0.2937 0.3103 0.3117 -0.0030 0.0013 -0.0189 279 TYR A C 1809 O O . TYR A 238 ? 0.3189 0.3351 0.3315 -0.0024 0.0025 -0.0174 279 TYR A O 1810 C CB . TYR A 238 ? 0.3252 0.3426 0.3466 -0.0027 -0.0009 -0.0170 279 TYR A CB 1811 C CG A TYR A 238 ? 0.2972 0.3150 0.3177 -0.0038 -0.0044 -0.0202 279 TYR A CG 1812 C CG B TYR A 238 ? 0.3438 0.3611 0.3579 -0.0036 -0.0036 -0.0194 279 TYR A CG 1813 C CD1 A TYR A 238 ? 0.3070 0.3253 0.3350 -0.0043 -0.0062 -0.0220 279 TYR A CD1 1814 C CD1 B TYR A 238 ? 0.3611 0.3788 0.3762 -0.0043 -0.0068 -0.0219 279 TYR A CD1 1815 C CD2 A TYR A 238 ? 0.3223 0.3398 0.3346 -0.0042 -0.0060 -0.0214 279 TYR A CD2 1816 C CD2 B TYR A 238 ? 0.3717 0.3886 0.3784 -0.0035 -0.0028 -0.0190 279 TYR A CD2 1817 C CE1 A TYR A 238 ? 0.3568 0.3752 0.3834 -0.0050 -0.0099 -0.0252 279 TYR A CE1 1818 C CE1 B TYR A 238 ? 0.3909 0.4081 0.3987 -0.0048 -0.0089 -0.0238 279 TYR A CE1 1819 C CE2 A TYR A 238 ? 0.3537 0.3710 0.3640 -0.0049 -0.0092 -0.0243 279 TYR A CE2 1820 C CE2 B TYR A 238 ? 0.4059 0.4225 0.4062 -0.0042 -0.0046 -0.0208 279 TYR A CE2 1821 C CZ A TYR A 238 ? 0.3745 0.3922 0.3916 -0.0052 -0.0113 -0.0262 279 TYR A CZ 1822 C CZ B TYR A 238 ? 0.3950 0.4116 0.3955 -0.0048 -0.0076 -0.0231 279 TYR A CZ 1823 O OH A TYR A 238 ? 0.4002 0.4176 0.4147 -0.0054 -0.0148 -0.0293 279 TYR A OH 1824 O OH B TYR A 238 ? 0.4480 0.4640 0.4415 -0.0051 -0.0092 -0.0247 279 TYR A OH 1825 N N . ARG A 239 ? 0.2516 0.2683 0.2705 -0.0039 0.0001 -0.0218 280 ARG A N 1826 C CA . ARG A 239 ? 0.2509 0.2672 0.2643 -0.0043 0.0004 -0.0233 280 ARG A CA 1827 C C . ARG A 239 ? 0.2733 0.2896 0.2810 -0.0050 -0.0022 -0.0254 280 ARG A C 1828 O O . ARG A 239 ? 0.2828 0.2992 0.2923 -0.0054 -0.0048 -0.0274 280 ARG A O 1829 C CB A ARG A 239 ? 0.2455 0.2616 0.2634 -0.0045 0.0012 -0.0251 280 ARG A CB 1830 C CB B ARG A 239 ? 0.2507 0.2668 0.2689 -0.0045 0.0014 -0.0249 280 ARG A CB 1831 C CG A ARG A 239 ? 0.2339 0.2496 0.2565 -0.0036 0.0041 -0.0228 280 ARG A CG 1832 C CG B ARG A 239 ? 0.2391 0.2547 0.2598 -0.0035 0.0046 -0.0229 280 ARG A CG 1833 C CD A ARG A 239 ? 0.2055 0.2208 0.2327 -0.0038 0.0052 -0.0243 280 ARG A CD 1834 C CD B ARG A 239 ? 0.2194 0.2346 0.2463 -0.0025 0.0065 -0.0201 280 ARG A CD 1835 N NE A ARG A 239 ? 0.2313 0.2459 0.2608 -0.0025 0.0082 -0.0216 280 ARG A NE 1836 N NE B ARG A 239 ? 0.2125 0.2269 0.2408 -0.0012 0.0095 -0.0182 280 ARG A NE 1837 C CZ A ARG A 239 ? 0.2643 0.2785 0.2999 -0.0017 0.0098 -0.0194 280 ARG A CZ 1838 C CZ B ARG A 239 ? 0.1986 0.2122 0.2324 -0.0001 0.0118 -0.0159 280 ARG A CZ 1839 N NH1 A ARG A 239 ? 0.2632 0.2780 0.3044 -0.0023 0.0086 -0.0197 280 ARG A NH1 1840 N NH1 B ARG A 239 ? 0.1855 0.1995 0.2248 -0.0002 0.0116 -0.0151 280 ARG A NH1 1841 N NH2 A ARG A 239 ? 0.2540 0.2672 0.2900 -0.0001 0.0127 -0.0168 280 ARG A NH2 1842 N NH2 B ARG A 239 ? 0.1183 0.1307 0.1522 0.0014 0.0145 -0.0141 280 ARG A NH2 1843 N N . ARG A 240 ? 0.2591 0.2751 0.2600 -0.0050 -0.0015 -0.0252 281 ARG A N 1844 C CA . ARG A 240 ? 0.2751 0.2908 0.2699 -0.0055 -0.0033 -0.0273 281 ARG A CA 1845 C C . ARG A 240 ? 0.2840 0.2993 0.2805 -0.0059 -0.0041 -0.0305 281 ARG A C 1846 O O . ARG A 240 ? 0.2786 0.2940 0.2798 -0.0058 -0.0026 -0.0310 281 ARG A O 1847 C CB . ARG A 240 ? 0.2660 0.2814 0.2547 -0.0055 -0.0017 -0.0264 281 ARG A CB 1848 C CG . ARG A 240 ? 0.2585 0.2740 0.2448 -0.0052 -0.0014 -0.0237 281 ARG A CG 1849 C CD . ARG A 240 ? 0.2654 0.2807 0.2462 -0.0053 -0.0002 -0.0231 281 ARG A CD 1850 N NE . ARG A 240 ? 0.2847 0.2999 0.2633 -0.0050 -0.0004 -0.0207 281 ARG A NE 1851 C CZ . ARG A 240 ? 0.3273 0.3422 0.3014 -0.0052 0.0001 -0.0199 281 ARG A CZ 1852 N NH1 . ARG A 240 ? 0.3236 0.3383 0.2951 -0.0056 0.0012 -0.0211 281 ARG A NH1 1853 N NH2 . ARG A 240 ? 0.3469 0.3615 0.3195 -0.0048 -0.0002 -0.0179 281 ARG A NH2 1854 N N . GLY A 241 ? 0.3106 0.3253 0.3031 -0.0060 -0.0066 -0.0328 282 GLY A N 1855 C CA . GLY A 241 ? 0.3371 0.3511 0.3292 -0.0060 -0.0073 -0.0361 282 GLY A CA 1856 C C . GLY A 241 ? 0.3431 0.3568 0.3303 -0.0060 -0.0048 -0.0361 282 GLY A C 1857 O O . GLY A 241 ? 0.3368 0.3507 0.3197 -0.0060 -0.0033 -0.0339 282 GLY A O 1858 N N . ILE A 242 ? 0.3648 0.3781 0.3532 -0.0059 -0.0043 -0.0385 283 ILE A N 1859 C CA . ILE A 242 ? 0.3773 0.3905 0.3618 -0.0059 -0.0018 -0.0387 283 ILE A CA 1860 C C . ILE A 242 ? 0.3817 0.3942 0.3576 -0.0057 -0.0014 -0.0382 283 ILE A C 1861 O O . ILE A 242 ? 0.3758 0.3886 0.3494 -0.0058 0.0010 -0.0365 283 ILE A O 1862 C CB . ILE A 242 ? 0.3916 0.4041 0.3777 -0.0057 -0.0016 -0.0419 283 ILE A CB 1863 C CG1 . ILE A 242 ? 0.4108 0.4240 0.4051 -0.0059 -0.0003 -0.0414 283 ILE A CG1 1864 C CG2 . ILE A 242 ? 0.4130 0.4251 0.3935 -0.0054 0.0009 -0.0423 283 ILE A CG2 1865 C CD1 . ILE A 242 ? 0.3822 0.3961 0.3767 -0.0058 0.0030 -0.0393 283 ILE A CD1 1866 N N . ALA A 243 ? 0.3893 0.4007 0.3607 -0.0053 -0.0039 -0.0395 284 ALA A N 1867 C CA . ALA A 243 ? 0.3994 0.4099 0.3623 -0.0049 -0.0033 -0.0389 284 ALA A CA 1868 C C . ALA A 243 ? 0.3963 0.4075 0.3580 -0.0053 -0.0020 -0.0354 284 ALA A C 1869 O O . ALA A 243 ? 0.4098 0.4204 0.3661 -0.0052 -0.0003 -0.0344 284 ALA A O 1870 C CB . ALA A 243 ? 0.4175 0.4262 0.3750 -0.0040 -0.0065 -0.0410 284 ALA A CB 1871 N N . GLU A 244 ? 0.3794 0.3916 0.3463 -0.0057 -0.0028 -0.0336 285 GLU A N 1872 C CA . GLU A 244 ? 0.3752 0.3879 0.3412 -0.0059 -0.0019 -0.0305 285 GLU A CA 1873 C C . GLU A 244 ? 0.3570 0.3709 0.3276 -0.0061 0.0005 -0.0289 285 GLU A C 1874 O O . GLU A 244 ? 0.3550 0.3692 0.3257 -0.0061 0.0011 -0.0265 285 GLU A O 1875 C CB . GLU A 244 ? 0.3920 0.4048 0.3597 -0.0058 -0.0043 -0.0295 285 GLU A CB 1876 C CG . GLU A 244 ? 0.4454 0.4570 0.4078 -0.0054 -0.0070 -0.0306 285 GLU A CG 1877 C CD . GLU A 244 ? 0.5264 0.5372 0.4888 -0.0049 -0.0091 -0.0340 285 GLU A CD 1878 O OE1 . GLU A 244 ? 0.5941 0.6033 0.5495 -0.0043 -0.0097 -0.0355 285 GLU A OE1 1879 O OE2 . GLU A 244 ? 0.5194 0.5310 0.4887 -0.0051 -0.0100 -0.0353 285 GLU A OE2 1880 N N . ALA A 245 ? 0.3298 0.3440 0.3041 -0.0061 0.0017 -0.0302 286 ALA A N 1881 C CA . ALA A 245 ? 0.2999 0.3149 0.2785 -0.0060 0.0037 -0.0288 286 ALA A CA 1882 C C . ALA A 245 ? 0.3095 0.3247 0.2848 -0.0061 0.0055 -0.0274 286 ALA A C 1883 O O . ALA A 245 ? 0.3096 0.3243 0.2800 -0.0063 0.0061 -0.0279 286 ALA A O 1884 C CB . ALA A 245 ? 0.3055 0.3206 0.2879 -0.0059 0.0046 -0.0307 286 ALA A CB 1885 N N . VAL A 246 ? 0.2611 0.2768 0.2392 -0.0057 0.0065 -0.0257 287 VAL A N 1886 C CA . VAL A 246 ? 0.2462 0.2621 0.2226 -0.0058 0.0079 -0.0246 287 VAL A CA 1887 C C . VAL A 246 ? 0.2613 0.2777 0.2394 -0.0058 0.0098 -0.0258 287 VAL A C 1888 O O . VAL A 246 ? 0.2601 0.2767 0.2421 -0.0053 0.0102 -0.0264 287 VAL A O 1889 C CB . VAL A 246 ? 0.2585 0.2746 0.2367 -0.0051 0.0076 -0.0223 287 VAL A CB 1890 C CG1 . VAL A 246 ? 0.2397 0.2560 0.2167 -0.0052 0.0087 -0.0215 287 VAL A CG1 1891 C CG2 . VAL A 246 ? 0.2905 0.3062 0.2673 -0.0050 0.0059 -0.0210 287 VAL A CG2 1892 N N . GLY A 247 ? 0.2453 0.2616 0.2203 -0.0062 0.0110 -0.0261 288 GLY A N 1893 C CA . GLY A 247 ? 0.2363 0.2533 0.2134 -0.0062 0.0131 -0.0267 288 GLY A CA 1894 C C . GLY A 247 ? 0.2364 0.2535 0.2142 -0.0062 0.0143 -0.0291 288 GLY A C 1895 O O . GLY A 247 ? 0.2333 0.2510 0.2134 -0.0061 0.0160 -0.0296 288 GLY A O 1896 N N . LEU A 248 ? 0.2531 0.2693 0.2289 -0.0062 0.0132 -0.0306 289 LEU A N 1897 C CA . LEU A 248 ? 0.2486 0.2647 0.2252 -0.0060 0.0141 -0.0331 289 LEU A CA 1898 C C . LEU A 248 ? 0.2596 0.2753 0.2317 -0.0061 0.0161 -0.0339 289 LEU A C 1899 O O . LEU A 248 ? 0.2709 0.2858 0.2379 -0.0062 0.0160 -0.0331 289 LEU A O 1900 C CB . LEU A 248 ? 0.2598 0.2750 0.2360 -0.0059 0.0120 -0.0348 289 LEU A CB 1901 C CG . LEU A 248 ? 0.3207 0.3362 0.3015 -0.0058 0.0102 -0.0340 289 LEU A CG 1902 C CD1 . LEU A 248 ? 0.3299 0.3445 0.3108 -0.0058 0.0081 -0.0361 289 LEU A CD1 1903 C CD2 . LEU A 248 ? 0.3367 0.3527 0.3229 -0.0055 0.0115 -0.0338 289 LEU A CD2 1904 N N . PRO A 249 ? 0.2642 0.2801 0.2379 -0.0059 0.0180 -0.0355 290 PRO A N 1905 C CA . PRO A 249 ? 0.2794 0.2948 0.2491 -0.0057 0.0204 -0.0363 290 PRO A CA 1906 C C . PRO A 249 ? 0.2918 0.3055 0.2561 -0.0051 0.0194 -0.0384 290 PRO A C 1907 O O . PRO A 249 ? 0.2942 0.3075 0.2599 -0.0049 0.0171 -0.0400 290 PRO A O 1908 C CB . PRO A 249 ? 0.2865 0.3029 0.2608 -0.0055 0.0224 -0.0374 290 PRO A CB 1909 C CG . PRO A 249 ? 0.2737 0.2904 0.2530 -0.0053 0.0206 -0.0382 290 PRO A CG 1910 C CD . PRO A 249 ? 0.2737 0.2903 0.2532 -0.0056 0.0182 -0.0363 290 PRO A CD 1911 N N . SER A 250 ? 0.3047 0.3173 0.2629 -0.0047 0.0212 -0.0384 291 SER A N 1912 C CA A SER A 250 ? 0.3083 0.3188 0.2597 -0.0037 0.0202 -0.0403 291 SER A CA 1913 C CA B SER A 250 ? 0.3187 0.3293 0.2704 -0.0037 0.0200 -0.0404 291 SER A CA 1914 C C . SER A 250 ? 0.3141 0.3237 0.2636 -0.0027 0.0222 -0.0429 291 SER A C 1915 O O . SER A 250 ? 0.3337 0.3412 0.2772 -0.0016 0.0212 -0.0449 291 SER A O 1916 C CB A SER A 250 ? 0.3193 0.3284 0.2638 -0.0034 0.0208 -0.0386 291 SER A CB 1917 C CB B SER A 250 ? 0.3312 0.3404 0.2760 -0.0035 0.0198 -0.0388 291 SER A CB 1918 O OG A SER A 250 ? 0.3046 0.3139 0.2482 -0.0035 0.0248 -0.0372 291 SER A OG 1919 O OG B SER A 250 ? 0.3717 0.3812 0.3178 -0.0040 0.0167 -0.0376 291 SER A OG 1920 N N . ILE A 251 ? 0.2923 0.3033 0.2465 -0.0030 0.0249 -0.0427 292 ILE A N 1921 C CA . ILE A 251 ? 0.2883 0.2987 0.2412 -0.0020 0.0274 -0.0450 292 ILE A CA 1922 C C . ILE A 251 ? 0.2884 0.3003 0.2490 -0.0024 0.0274 -0.0462 292 ILE A C 1923 O O . ILE A 251 ? 0.2814 0.2951 0.2482 -0.0033 0.0268 -0.0446 292 ILE A O 1924 C CB . ILE A 251 ? 0.2957 0.3060 0.2459 -0.0017 0.0317 -0.0436 292 ILE A CB 1925 C CG1 . ILE A 251 ? 0.2873 0.2999 0.2441 -0.0030 0.0332 -0.0409 292 ILE A CG1 1926 C CG2 . ILE A 251 ? 0.3290 0.3371 0.2705 -0.0010 0.0318 -0.0425 292 ILE A CG2 1927 C CD1 . ILE A 251 ? 0.2983 0.3110 0.2541 -0.0029 0.0377 -0.0394 292 ILE A CD1 1928 N N . PRO A 252 ? 0.2866 0.2976 0.2467 -0.0014 0.0278 -0.0491 293 PRO A N 1929 C CA . PRO A 252 ? 0.2828 0.2950 0.2504 -0.0017 0.0277 -0.0502 293 PRO A CA 1930 C C . PRO A 252 ? 0.2720 0.2862 0.2445 -0.0021 0.0309 -0.0488 293 PRO A C 1931 O O . PRO A 252 ? 0.2745 0.2887 0.2443 -0.0018 0.0340 -0.0480 293 PRO A O 1932 C CB . PRO A 252 ? 0.2986 0.3091 0.2636 -0.0004 0.0277 -0.0539 293 PRO A CB 1933 C CG . PRO A 252 ? 0.3105 0.3187 0.2670 0.0004 0.0257 -0.0548 293 PRO A CG 1934 C CD . PRO A 252 ? 0.2929 0.3014 0.2455 0.0000 0.0276 -0.0517 293 PRO A CD 1935 N N . VAL A 253 ? 0.2545 0.2701 0.2343 -0.0025 0.0302 -0.0485 294 VAL A N 1936 C CA . VAL A 253 ? 0.2452 0.2626 0.2303 -0.0027 0.0324 -0.0473 294 VAL A CA 1937 C C . VAL A 253 ? 0.2427 0.2606 0.2339 -0.0023 0.0320 -0.0487 294 VAL A C 1938 O O . VAL A 253 ? 0.2333 0.2506 0.2263 -0.0024 0.0295 -0.0492 294 VAL A O 1939 C CB . VAL A 253 ? 0.2342 0.2529 0.2220 -0.0036 0.0313 -0.0443 294 VAL A CB 1940 C CG1 . VAL A 253 ? 0.2550 0.2754 0.2486 -0.0036 0.0330 -0.0433 294 VAL A CG1 1941 C CG2 . VAL A 253 ? 0.2541 0.2721 0.2361 -0.0040 0.0313 -0.0427 294 VAL A CG2 1942 N N . HIS A 254 ? 0.2420 0.2610 0.2369 -0.0020 0.0345 -0.0492 295 HIS A N 1943 C CA . HIS A 254 ? 0.2320 0.2513 0.2327 -0.0015 0.0342 -0.0505 295 HIS A CA 1944 C C . HIS A 254 ? 0.2356 0.2567 0.2415 -0.0013 0.0364 -0.0498 295 HIS A C 1945 O O . HIS A 254 ? 0.2488 0.2705 0.2534 -0.0013 0.0391 -0.0496 295 HIS A O 1946 C CB . HIS A 254 ? 0.2579 0.2758 0.2566 -0.0007 0.0348 -0.0537 295 HIS A CB 1947 C CG . HIS A 254 ? 0.2506 0.2683 0.2548 -0.0002 0.0341 -0.0551 295 HIS A CG 1948 N ND1 . HIS A 254 ? 0.2425 0.2597 0.2496 -0.0004 0.0314 -0.0547 295 HIS A ND1 1949 C CD2 . HIS A 254 ? 0.2718 0.2897 0.2793 0.0006 0.0358 -0.0570 295 HIS A CD2 1950 C CE1 . HIS A 254 ? 0.2638 0.2807 0.2757 0.0002 0.0315 -0.0561 295 HIS A CE1 1951 N NE2 . HIS A 254 ? 0.2720 0.2894 0.2843 0.0008 0.0340 -0.0576 295 HIS A NE2 1952 N N . PRO A 255 ? 0.2314 0.2532 0.2433 -0.0010 0.0353 -0.0494 296 PRO A N 1953 C CA . PRO A 255 ? 0.2185 0.2421 0.2360 -0.0006 0.0369 -0.0490 296 PRO A CA 1954 C C . PRO A 255 ? 0.2372 0.2607 0.2583 0.0003 0.0382 -0.0513 296 PRO A C 1955 O O . PRO A 255 ? 0.2485 0.2708 0.2697 0.0007 0.0370 -0.0526 296 PRO A O 1956 C CB . PRO A 255 ? 0.2234 0.2473 0.2444 -0.0004 0.0343 -0.0471 296 PRO A CB 1957 C CG . PRO A 255 ? 0.2346 0.2568 0.2540 -0.0003 0.0321 -0.0475 296 PRO A CG 1958 C CD . PRO A 255 ? 0.2320 0.2531 0.2458 -0.0008 0.0325 -0.0489 296 PRO A CD 1959 N N . ILE A 256 ? 0.2434 0.2685 0.2680 0.0006 0.0407 -0.0516 297 ILE A N 1960 C CA . ILE A 256 ? 0.2548 0.2801 0.2833 0.0015 0.0424 -0.0536 297 ILE A CA 1961 C C . ILE A 256 ? 0.2530 0.2804 0.2887 0.0020 0.0430 -0.0530 297 ILE A C 1962 O O . ILE A 256 ? 0.2406 0.2693 0.2782 0.0015 0.0426 -0.0511 297 ILE A O 1963 C CB . ILE A 256 ? 0.2632 0.2879 0.2877 0.0018 0.0455 -0.0556 297 ILE A CB 1964 C CG1 . ILE A 256 ? 0.2733 0.2994 0.2979 0.0014 0.0486 -0.0544 297 ILE A CG1 1965 C CG2 . ILE A 256 ? 0.2646 0.2870 0.2817 0.0016 0.0442 -0.0566 297 ILE A CG2 1966 C CD1 . ILE A 256 ? 0.2899 0.3153 0.3102 0.0020 0.0525 -0.0560 297 ILE A CD1 1967 N N . GLY A 257 ? 0.2516 0.2792 0.2919 0.0030 0.0438 -0.0547 298 GLY A N 1968 C CA . GLY A 257 ? 0.2500 0.2795 0.2976 0.0036 0.0443 -0.0545 298 GLY A CA 1969 C C . GLY A 257 ? 0.2552 0.2862 0.3047 0.0036 0.0482 -0.0554 298 GLY A C 1970 O O . GLY A 257 ? 0.2659 0.2962 0.3100 0.0032 0.0506 -0.0560 298 GLY A O 1971 N N . TYR A 258 ? 0.2549 0.2879 0.3117 0.0041 0.0488 -0.0554 299 TYR A N 1972 C CA . TYR A 258 ? 0.2494 0.2840 0.3092 0.0039 0.0527 -0.0558 299 TYR A CA 1973 C C . TYR A 258 ? 0.2611 0.2954 0.3212 0.0048 0.0559 -0.0582 299 TYR A C 1974 O O . TYR A 258 ? 0.2799 0.3148 0.3394 0.0047 0.0598 -0.0584 299 TYR A O 1975 C CB . TYR A 258 ? 0.2609 0.2981 0.3292 0.0040 0.0525 -0.0549 299 TYR A CB 1976 C CG . TYR A 258 ? 0.2600 0.2980 0.3354 0.0052 0.0498 -0.0556 299 TYR A CG 1977 C CD1 . TYR A 258 ? 0.2641 0.3017 0.3403 0.0056 0.0455 -0.0543 299 TYR A CD1 1978 C CD2 . TYR A 258 ? 0.2739 0.3129 0.3553 0.0063 0.0517 -0.0574 299 TYR A CD2 1979 C CE1 . TYR A 258 ? 0.2364 0.2744 0.3184 0.0071 0.0430 -0.0548 299 TYR A CE1 1980 C CE2 . TYR A 258 ? 0.2567 0.2963 0.3445 0.0076 0.0491 -0.0579 299 TYR A CE2 1981 C CZ . TYR A 258 ? 0.2702 0.3093 0.3581 0.0081 0.0446 -0.0566 299 TYR A CZ 1982 O OH . TYR A 258 ? 0.2666 0.3058 0.3601 0.0099 0.0419 -0.0572 299 TYR A OH 1983 N N . TYR A 259 ? 0.2647 0.2979 0.3256 0.0058 0.0544 -0.0598 300 TYR A N 1984 C CA . TYR A 259 ? 0.2746 0.3070 0.3343 0.0067 0.0573 -0.0623 300 TYR A CA 1985 C C . TYR A 259 ? 0.2986 0.3291 0.3492 0.0063 0.0588 -0.0628 300 TYR A C 1986 O O . TYR A 259 ? 0.3129 0.3433 0.3614 0.0068 0.0627 -0.0638 300 TYR A O 1987 C CB . TYR A 259 ? 0.2860 0.3171 0.3475 0.0077 0.0552 -0.0639 300 TYR A CB 1988 C CG . TYR A 259 ? 0.2876 0.3201 0.3576 0.0086 0.0541 -0.0640 300 TYR A CG 1989 C CD1 . TYR A 259 ? 0.2971 0.3323 0.3741 0.0088 0.0559 -0.0637 300 TYR A CD1 1990 C CD2 . TYR A 259 ? 0.2937 0.3249 0.3654 0.0095 0.0513 -0.0645 300 TYR A CD2 1991 C CE1 . TYR A 259 ? 0.2891 0.3256 0.3740 0.0099 0.0544 -0.0640 300 TYR A CE1 1992 C CE2 . TYR A 259 ? 0.2943 0.3265 0.3734 0.0107 0.0501 -0.0646 300 TYR A CE2 1993 C CZ . TYR A 259 ? 0.2998 0.3346 0.3852 0.0110 0.0515 -0.0644 300 TYR A CZ 1994 O OH . TYR A 259 ? 0.3408 0.3765 0.4335 0.0124 0.0499 -0.0647 300 TYR A OH 1995 N N . ASP A 260 ? 0.2941 0.3229 0.3391 0.0056 0.0559 -0.0621 301 ASP A N 1996 C CA . ASP A 260 ? 0.3081 0.3349 0.3443 0.0054 0.0567 -0.0626 301 ASP A CA 1997 C C . ASP A 260 ? 0.3165 0.3440 0.3496 0.0048 0.0594 -0.0608 301 ASP A C 1998 O O . ASP A 260 ? 0.3106 0.3368 0.3375 0.0053 0.0622 -0.0616 301 ASP A O 1999 C CB . ASP A 260 ? 0.3049 0.3300 0.3369 0.0048 0.0527 -0.0622 301 ASP A CB 2000 C CG . ASP A 260 ? 0.3263 0.3497 0.3592 0.0055 0.0508 -0.0643 301 ASP A CG 2001 O OD1 . ASP A 260 ? 0.3360 0.3591 0.3703 0.0066 0.0528 -0.0667 301 ASP A OD1 2002 O OD2 . ASP A 260 ? 0.2996 0.3220 0.3321 0.0050 0.0475 -0.0637 301 ASP A OD2 2003 N N . ALA A 261 ? 0.2913 0.3206 0.3282 0.0038 0.0585 -0.0584 302 ALA A N 2004 C CA . ALA A 261 ? 0.2984 0.3283 0.3334 0.0031 0.0612 -0.0565 302 ALA A CA 2005 C C . ALA A 261 ? 0.3087 0.3396 0.3461 0.0039 0.0664 -0.0572 302 ALA A C 2006 O O . ALA A 261 ? 0.3293 0.3594 0.3617 0.0040 0.0698 -0.0564 302 ALA A O 2007 C CB . ALA A 261 ? 0.2831 0.3149 0.3233 0.0021 0.0594 -0.0541 302 ALA A CB 2008 N N . GLN A 262 ? 0.3033 0.3358 0.3485 0.0046 0.0672 -0.0584 303 GLN A N 2009 C CA . GLN A 262 ? 0.3277 0.3613 0.3764 0.0054 0.0723 -0.0590 303 GLN A CA 2010 C C . GLN A 262 ? 0.3405 0.3715 0.3803 0.0066 0.0754 -0.0607 303 GLN A C 2011 O O . GLN A 262 ? 0.3467 0.3775 0.3842 0.0071 0.0802 -0.0600 303 GLN A O 2012 C CB . GLN A 262 ? 0.3198 0.3554 0.3782 0.0060 0.0721 -0.0603 303 GLN A CB 2013 C CG . GLN A 262 ? 0.3612 0.3978 0.4229 0.0071 0.0778 -0.0612 303 GLN A CG 2014 C CD . GLN A 262 ? 0.4413 0.4810 0.5151 0.0071 0.0785 -0.0612 303 GLN A CD 2015 O OE1 . GLN A 262 ? 0.5253 0.5662 0.6036 0.0078 0.0832 -0.0616 303 GLN A OE1 2016 N NE2 . GLN A 262 ? 0.4190 0.4598 0.4984 0.0067 0.0739 -0.0608 303 GLN A NE2 2017 N N . LYS A 263 ? 0.3536 0.3825 0.3883 0.0072 0.0726 -0.0627 304 LYS A N 2018 C CA . LYS A 263 ? 0.3604 0.3864 0.3861 0.0086 0.0747 -0.0647 304 LYS A CA 2019 C C . LYS A 263 ? 0.3760 0.4001 0.3921 0.0084 0.0755 -0.0633 304 LYS A C 2020 O O . LYS A 263 ? 0.3868 0.4089 0.3958 0.0099 0.0788 -0.0642 304 LYS A O 2021 C CB . LYS A 263 ? 0.3655 0.3897 0.3890 0.0091 0.0710 -0.0674 304 LYS A CB 2022 C CG . LYS A 263 ? 0.3918 0.4172 0.4237 0.0096 0.0704 -0.0689 304 LYS A CG 2023 C CD . LYS A 263 ? 0.4951 0.5200 0.5267 0.0114 0.0748 -0.0712 304 LYS A CD 2024 C CE . LYS A 263 ? 0.5526 0.5799 0.5948 0.0118 0.0756 -0.0718 304 LYS A CE 2025 N NZ . LYS A 263 ? 0.6377 0.6638 0.6792 0.0137 0.0785 -0.0748 304 LYS A NZ 2026 N N . LEU A 264 ? 0.3391 0.3635 0.3543 0.0069 0.0725 -0.0611 305 LEU A N 2027 C CA . LEU A 264 ? 0.3596 0.3823 0.3660 0.0068 0.0733 -0.0595 305 LEU A CA 2028 C C . LEU A 264 ? 0.3569 0.3807 0.3650 0.0065 0.0780 -0.0569 305 LEU A C 2029 O O . LEU A 264 ? 0.3872 0.4090 0.3872 0.0073 0.0808 -0.0560 305 LEU A O 2030 C CB . LEU A 264 ? 0.3275 0.3500 0.3322 0.0053 0.0683 -0.0582 305 LEU A CB 2031 C CG . LEU A 264 ? 0.3442 0.3651 0.3466 0.0055 0.0636 -0.0604 305 LEU A CG 2032 C CD1 . LEU A 264 ? 0.3461 0.3669 0.3468 0.0041 0.0593 -0.0586 305 LEU A CD1 2033 C CD2 . LEU A 264 ? 0.3709 0.3887 0.3645 0.0071 0.0642 -0.0630 305 LEU A CD2 2034 N N . LEU A 265 ? 0.3381 0.3651 0.3568 0.0055 0.0788 -0.0556 306 LEU A N 2035 C CA . LEU A 265 ? 0.3367 0.3651 0.3593 0.0050 0.0829 -0.0530 306 LEU A CA 2036 C C . LEU A 265 ? 0.3483 0.3772 0.3735 0.0064 0.0891 -0.0536 306 LEU A C 2037 O O . LEU A 265 ? 0.3679 0.3970 0.3935 0.0064 0.0937 -0.0515 306 LEU A O 2038 C CB . LEU A 265 ? 0.3253 0.3570 0.3590 0.0034 0.0808 -0.0516 306 LEU A CB 2039 C CG . LEU A 265 ? 0.3228 0.3543 0.3550 0.0021 0.0752 -0.0505 306 LEU A CG 2040 C CD1 . LEU A 265 ? 0.2933 0.3277 0.3367 0.0011 0.0725 -0.0498 306 LEU A CD1 2041 C CD2 . LEU A 265 ? 0.3217 0.3517 0.3470 0.0014 0.0757 -0.0481 306 LEU A CD2 2042 N N . GLU A 266 ? 0.3598 0.3890 0.3878 0.0075 0.0892 -0.0563 307 GLU A N 2043 C CA . GLU A 266 ? 0.3723 0.4025 0.4051 0.0087 0.0950 -0.0568 307 GLU A CA 2044 C C . GLU A 266 ? 0.3874 0.4149 0.4108 0.0104 0.1006 -0.0563 307 GLU A C 2045 O O . GLU A 266 ? 0.3883 0.4167 0.4157 0.0111 0.1065 -0.0553 307 GLU A O 2046 C CB . GLU A 266 ? 0.3661 0.3969 0.4034 0.0097 0.0940 -0.0599 307 GLU A CB 2047 C CG . GLU A 266 ? 0.4047 0.4323 0.4323 0.0111 0.0921 -0.0627 307 GLU A CG 2048 C CD . GLU A 266 ? 0.4273 0.4555 0.4603 0.0120 0.0909 -0.0656 307 GLU A CD 2049 O OE1 . GLU A 266 ? 0.4797 0.5110 0.5238 0.0114 0.0907 -0.0653 307 GLU A OE1 2050 O OE2 . GLU A 266 ? 0.4434 0.4690 0.4696 0.0133 0.0898 -0.0682 307 GLU A OE2 2051 N N . LYS A 267 ? 0.3964 0.4205 0.4077 0.0112 0.0988 -0.0570 308 LYS A N 2052 C CA . LYS A 267 ? 0.4192 0.4400 0.4196 0.0133 0.1034 -0.0569 308 LYS A CA 2053 C C . LYS A 267 ? 0.4234 0.4432 0.4190 0.0127 0.1054 -0.0534 308 LYS A C 2054 O O . LYS A 267 ? 0.4182 0.4350 0.4039 0.0146 0.1094 -0.0528 308 LYS A O 2055 C CB . LYS A 267 ? 0.4252 0.4425 0.4146 0.0150 0.1003 -0.0600 308 LYS A CB 2056 C CG . LYS A 267 ? 0.4425 0.4597 0.4342 0.0165 0.1006 -0.0636 308 LYS A CG 2057 C CD . LYS A 267 ? 0.4792 0.4933 0.4621 0.0176 0.0960 -0.0669 308 LYS A CD 2058 C CE . LYS A 267 ? 0.5036 0.5169 0.4874 0.0195 0.0968 -0.0706 308 LYS A CE 2059 N NZ . LYS A 267 ? 0.5277 0.5375 0.5023 0.0207 0.0923 -0.0737 308 LYS A NZ 2060 N N . MET A 268 ? 0.3992 0.4213 0.4010 0.0103 0.1024 -0.0512 309 MET A N 2061 C CA . MET A 268 ? 0.4128 0.4338 0.4102 0.0096 0.1037 -0.0479 309 MET A CA 2062 C C . MET A 268 ? 0.4211 0.4417 0.4191 0.0105 0.1114 -0.0453 309 MET A C 2063 O O . MET A 268 ? 0.4125 0.4359 0.4211 0.0101 0.1151 -0.0447 309 MET A O 2064 C CB . MET A 268 ? 0.3987 0.4222 0.4033 0.0069 0.0991 -0.0462 309 MET A CB 2065 C CG A MET A 268 ? 0.3921 0.4143 0.3908 0.0066 0.0922 -0.0480 309 MET A CG 2066 C CG B MET A 268 ? 0.4069 0.4301 0.4092 0.0062 0.0920 -0.0479 309 MET A CG 2067 S SD A MET A 268 ? 0.1263 0.1495 0.1271 0.0042 0.0862 -0.0462 309 MET A SD 2068 S SD B MET A 268 ? 0.1491 0.1685 0.1371 0.0066 0.0897 -0.0471 309 MET A SD 2069 C CE A MET A 268 ? 0.3748 0.3959 0.3679 0.0042 0.0894 -0.0427 309 MET A CE 2070 C CE B MET A 268 ? 0.4117 0.4319 0.4024 0.0051 0.0920 -0.0427 309 MET A CE 2071 N N . GLY A 269 ? 0.4383 0.4556 0.4251 0.0117 0.1136 -0.0436 310 GLY A N 2072 C CA . GLY A 269 ? 0.4492 0.4655 0.4351 0.0127 0.1212 -0.0405 310 GLY A CA 2073 C C . GLY A 269 ? 0.4618 0.4776 0.4468 0.0112 0.1213 -0.0368 310 GLY A C 2074 O O . GLY A 269 ? 0.4480 0.4662 0.4397 0.0087 0.1165 -0.0361 310 GLY A O 2075 N N . GLY A 270 ? 0.4670 0.4797 0.4437 0.0130 0.1269 -0.0343 311 GLY A N 2076 C CA . GLY A 270 ? 0.4745 0.4863 0.4500 0.0118 0.1278 -0.0305 311 GLY A CA 2077 C C . GLY A 270 ? 0.4770 0.4928 0.4683 0.0094 0.1303 -0.0280 311 GLY A C 2078 O O . GLY A 270 ? 0.4789 0.4968 0.4794 0.0097 0.1349 -0.0281 311 GLY A O 2079 N N . SER A 271 ? 0.4671 0.4838 0.4621 0.0071 0.1270 -0.0259 312 SER A N 2080 C CA . SER A 271 ? 0.4702 0.4902 0.4796 0.0050 0.1292 -0.0234 312 SER A CA 2081 C C . SER A 271 ? 0.4569 0.4814 0.4807 0.0032 0.1257 -0.0257 312 SER A C 2082 O O . SER A 271 ? 0.4625 0.4879 0.4853 0.0028 0.1193 -0.0286 312 SER A O 2083 C CB . SER A 271 ? 0.4739 0.4932 0.4821 0.0032 0.1262 -0.0208 312 SER A CB 2084 O OG . SER A 271 ? 0.5145 0.5294 0.5099 0.0050 0.1301 -0.0183 312 SER A OG 2085 N N . ALA A 272 ? 0.4521 0.4795 0.4897 0.0023 0.1298 -0.0243 313 ALA A N 2086 C CA . ALA A 272 ? 0.4377 0.4695 0.4901 0.0006 0.1261 -0.0262 313 ALA A CA 2087 C C . ALA A 272 ? 0.4218 0.4549 0.4775 -0.0016 0.1190 -0.0259 313 ALA A C 2088 O O . ALA A 272 ? 0.4155 0.4465 0.4655 -0.0022 0.1187 -0.0235 313 ALA A O 2089 C CB . ALA A 272 ? 0.4348 0.4692 0.5015 0.0001 0.1321 -0.0245 313 ALA A CB 2090 N N . PRO A 273 ? 0.4161 0.4523 0.4810 -0.0027 0.1134 -0.0283 314 PRO A N 2091 C CA . PRO A 273 ? 0.4142 0.4516 0.4837 -0.0046 0.1071 -0.0279 314 PRO A CA 2092 C C . PRO A 273 ? 0.4180 0.4564 0.4969 -0.0060 0.1104 -0.0249 314 PRO A C 2093 O O . PRO A 273 ? 0.4168 0.4567 0.5046 -0.0058 0.1161 -0.0241 314 PRO A O 2094 C CB . PRO A 273 ? 0.4035 0.4441 0.4827 -0.0049 0.1024 -0.0309 314 PRO A CB 2095 C CG . PRO A 273 ? 0.4158 0.4577 0.5006 -0.0036 0.1079 -0.0320 314 PRO A CG 2096 C CD . PRO A 273 ? 0.4133 0.4517 0.4849 -0.0020 0.1129 -0.0313 314 PRO A CD 2097 N N . PRO A 274 ? 0.4179 0.4555 0.4950 -0.0073 0.1071 -0.0232 315 PRO A N 2098 C CA . PRO A 274 ? 0.4193 0.4573 0.5044 -0.0085 0.1105 -0.0202 315 PRO A CA 2099 C C . PRO A 274 ? 0.4172 0.4591 0.5202 -0.0098 0.1092 -0.0209 315 PRO A C 2100 O O . PRO A 274 ? 0.4229 0.4657 0.5355 -0.0107 0.1133 -0.0187 315 PRO A O 2101 C CB . PRO A 274 ? 0.4094 0.4453 0.4869 -0.0094 0.1061 -0.0188 315 PRO A CB 2102 C CG . PRO A 274 ? 0.4138 0.4499 0.4855 -0.0091 0.0988 -0.0217 315 PRO A CG 2103 C CD . PRO A 274 ? 0.4077 0.4434 0.4741 -0.0074 0.1010 -0.0238 315 PRO A CD 2104 N N . ASP A 275 ? 0.4098 0.4539 0.5175 -0.0098 0.1034 -0.0240 316 ASP A N 2105 C CA . ASP A 275 ? 0.4097 0.4574 0.5341 -0.0107 0.1012 -0.0253 316 ASP A CA 2106 C C . ASP A 275 ? 0.4065 0.4557 0.5318 -0.0099 0.0951 -0.0288 316 ASP A C 2107 O O . ASP A 275 ? 0.4036 0.4511 0.5172 -0.0090 0.0928 -0.0300 316 ASP A O 2108 C CB . ASP A 275 ? 0.4134 0.4616 0.5449 -0.0124 0.0982 -0.0238 316 ASP A CB 2109 C CG . ASP A 275 ? 0.4365 0.4833 0.5598 -0.0126 0.0908 -0.0245 316 ASP A CG 2110 O OD1 . ASP A 275 ? 0.4424 0.4900 0.5645 -0.0119 0.0853 -0.0272 316 ASP A OD1 2111 O OD2 . ASP A 275 ? 0.4612 0.5061 0.5797 -0.0134 0.0904 -0.0223 316 ASP A OD2 2112 N N . SER A 276 ? 0.3998 0.4521 0.5391 -0.0103 0.0924 -0.0304 317 SER A N 2113 C CA . SER A 276 ? 0.4016 0.4553 0.5428 -0.0092 0.0874 -0.0337 317 SER A CA 2114 C C . SER A 276 ? 0.3865 0.4387 0.5191 -0.0090 0.0799 -0.0347 317 SER A C 2115 O O . SER A 276 ? 0.3890 0.4412 0.5182 -0.0079 0.0768 -0.0369 317 SER A O 2116 C CB . SER A 276 ? 0.4030 0.4602 0.5614 -0.0094 0.0860 -0.0352 317 SER A CB 2117 O OG . SER A 276 ? 0.4234 0.4812 0.5883 -0.0104 0.0812 -0.0349 317 SER A OG 2118 N N . SER A 277 ? 0.3794 0.4304 0.5089 -0.0100 0.0772 -0.0331 318 SER A N 2119 C CA . SER A 277 ? 0.3582 0.4076 0.4795 -0.0098 0.0705 -0.0338 318 SER A CA 2120 C C . SER A 277 ? 0.3506 0.3975 0.4571 -0.0090 0.0708 -0.0339 318 SER A C 2121 O O . SER A 277 ? 0.3533 0.3990 0.4527 -0.0086 0.0658 -0.0345 318 SER A O 2122 C CB . SER A 277 ? 0.3563 0.4048 0.4775 -0.0110 0.0684 -0.0319 318 SER A CB 2123 O OG . SER A 277 ? 0.3654 0.4116 0.4775 -0.0116 0.0729 -0.0293 318 SER A OG 2124 N N . TRP A 278 ? 0.3305 0.3765 0.4323 -0.0087 0.0769 -0.0332 319 TRP A N 2125 C CA . TRP A 278 ? 0.3211 0.3647 0.4095 -0.0078 0.0778 -0.0336 319 TRP A CA 2126 C C . TRP A 278 ? 0.3154 0.3599 0.4048 -0.0065 0.0782 -0.0362 319 TRP A C 2127 O O . TRP A 278 ? 0.3092 0.3519 0.3887 -0.0056 0.0778 -0.0372 319 TRP A O 2128 C CB . TRP A 278 ? 0.3300 0.3716 0.4112 -0.0078 0.0838 -0.0313 319 TRP A CB 2129 C CG . TRP A 278 ? 0.3222 0.3617 0.3967 -0.0087 0.0824 -0.0291 319 TRP A CG 2130 C CD1 . TRP A 278 ? 0.3177 0.3580 0.3985 -0.0100 0.0804 -0.0276 319 TRP A CD1 2131 C CD2 . TRP A 278 ? 0.3017 0.3382 0.3622 -0.0082 0.0823 -0.0283 319 TRP A CD2 2132 N NE1 . TRP A 278 ? 0.3336 0.3713 0.4049 -0.0104 0.0794 -0.0257 319 TRP A NE1 2133 C CE2 . TRP A 278 ? 0.3328 0.3683 0.3916 -0.0093 0.0803 -0.0262 319 TRP A CE2 2134 C CE3 . TRP A 278 ? 0.2822 0.3166 0.3317 -0.0069 0.0833 -0.0294 319 TRP A CE3 2135 C CZ2 . TRP A 278 ? 0.3092 0.3417 0.3557 -0.0091 0.0797 -0.0249 319 TRP A CZ2 2136 C CZ3 . TRP A 278 ? 0.2963 0.3278 0.3336 -0.0067 0.0824 -0.0283 319 TRP A CZ3 2137 C CH2 . TRP A 278 ? 0.3030 0.3336 0.3390 -0.0078 0.0805 -0.0261 319 TRP A CH2 2138 N N . ARG A 279 ? 0.3137 0.3609 0.4152 -0.0063 0.0789 -0.0373 320 ARG A N 2139 C CA . ARG A 279 ? 0.3168 0.3650 0.4205 -0.0050 0.0793 -0.0398 320 ARG A CA 2140 C C . ARG A 279 ? 0.3063 0.3553 0.4129 -0.0044 0.0728 -0.0419 320 ARG A C 2141 O O . ARG A 279 ? 0.3149 0.3656 0.4305 -0.0047 0.0693 -0.0421 320 ARG A O 2142 C CB . ARG A 279 ? 0.3100 0.3606 0.4254 -0.0049 0.0845 -0.0399 320 ARG A CB 2143 C CG . ARG A 279 ? 0.3550 0.4042 0.4657 -0.0047 0.0921 -0.0381 320 ARG A CG 2144 C CD . ARG A 279 ? 0.4908 0.5422 0.6113 -0.0041 0.0978 -0.0387 320 ARG A CD 2145 N NE . ARG A 279 ? 0.6116 0.6644 0.7419 -0.0052 0.1018 -0.0364 320 ARG A NE 2146 C CZ . ARG A 279 ? 0.6568 0.7125 0.8013 -0.0061 0.0995 -0.0366 320 ARG A CZ 2147 N NH1 . ARG A 279 ? 0.6739 0.7313 0.8240 -0.0058 0.0931 -0.0391 320 ARG A NH1 2148 N NH2 . ARG A 279 ? 0.6789 0.7356 0.8322 -0.0072 0.1036 -0.0344 320 ARG A NH2 2149 N N . GLY A 280 ? 0.3220 0.3696 0.4207 -0.0034 0.0710 -0.0434 321 GLY A N 2150 C CA . GLY A 280 ? 0.3149 0.3630 0.4162 -0.0024 0.0660 -0.0454 321 GLY A CA 2151 C C . GLY A 280 ? 0.3316 0.3817 0.4417 -0.0014 0.0678 -0.0473 321 GLY A C 2152 O O . GLY A 280 ? 0.3274 0.3792 0.4449 -0.0017 0.0723 -0.0469 321 GLY A O 2153 N N . SER A 281 ? 0.3216 0.3714 0.4312 -0.0001 0.0645 -0.0492 322 SER A N 2154 C CA . SER A 281 ? 0.3544 0.4062 0.4731 0.0010 0.0654 -0.0511 322 SER A CA 2155 C C . SER A 281 ? 0.3489 0.3997 0.4630 0.0019 0.0687 -0.0525 322 SER A C 2156 O O . SER A 281 ? 0.3701 0.4223 0.4910 0.0030 0.0696 -0.0542 322 SER A O 2157 C CB . SER A 281 ? 0.3472 0.3994 0.4704 0.0021 0.0592 -0.0523 322 SER A CB 2158 O OG . SER A 281 ? 0.4294 0.4829 0.5589 0.0015 0.0562 -0.0515 322 SER A OG 2159 N N . LEU A 282 ? 0.3349 0.3832 0.4376 0.0017 0.0704 -0.0521 323 LEU A N 2160 C CA . LEU A 282 ? 0.3422 0.3894 0.4406 0.0028 0.0732 -0.0538 323 LEU A CA 2161 C C . LEU A 282 ? 0.3508 0.3992 0.4531 0.0031 0.0799 -0.0537 323 LEU A C 2162 O O . LEU A 282 ? 0.3459 0.3952 0.4512 0.0021 0.0828 -0.0518 323 LEU A O 2163 C CB . LEU A 282 ? 0.3424 0.3865 0.4277 0.0028 0.0727 -0.0537 323 LEU A CB 2164 C CG . LEU A 282 ? 0.3217 0.3644 0.4027 0.0027 0.0668 -0.0538 323 LEU A CG 2165 C CD1 . LEU A 282 ? 0.3248 0.3648 0.3940 0.0023 0.0668 -0.0532 323 LEU A CD1 2166 C CD2 . LEU A 282 ? 0.3202 0.3628 0.4040 0.0040 0.0644 -0.0559 323 LEU A CD2 2167 N N . LYS A 283 ? 0.3663 0.4144 0.4683 0.0044 0.0824 -0.0557 324 LYS A N 2168 C CA . LYS A 283 ? 0.3923 0.4411 0.4971 0.0049 0.0892 -0.0557 324 LYS A CA 2169 C C . LYS A 283 ? 0.3884 0.4344 0.4811 0.0052 0.0931 -0.0549 324 LYS A C 2170 O O . LYS A 283 ? 0.4038 0.4482 0.4909 0.0066 0.0960 -0.0564 324 LYS A O 2171 C CB . LYS A 283 ? 0.4000 0.4499 0.5103 0.0064 0.0902 -0.0582 324 LYS A CB 2172 C CG . LYS A 283 ? 0.4587 0.5114 0.5817 0.0064 0.0866 -0.0589 324 LYS A CG 2173 C CD . LYS A 283 ? 0.5281 0.5837 0.6621 0.0055 0.0892 -0.0573 324 LYS A CD 2174 C CE . LYS A 283 ? 0.5608 0.6181 0.7025 0.0048 0.0832 -0.0569 324 LYS A CE 2175 N NZ . LYS A 283 ? 0.5928 0.6533 0.7483 0.0042 0.0851 -0.0563 324 LYS A NZ 2176 N N . VAL A 284 ? 0.3726 0.4178 0.4614 0.0040 0.0930 -0.0524 325 VAL A N 2177 C CA . VAL A 284 ? 0.3740 0.4165 0.4516 0.0042 0.0966 -0.0512 325 VAL A CA 2178 C C . VAL A 284 ? 0.3614 0.4048 0.4429 0.0030 0.0996 -0.0482 325 VAL A C 2179 O O . VAL A 284 ? 0.3585 0.4044 0.4498 0.0017 0.0971 -0.0473 325 VAL A O 2180 C CB . VAL A 284 ? 0.3662 0.4057 0.4316 0.0041 0.0921 -0.0515 325 VAL A CB 2181 C CG1 . VAL A 284 ? 0.3877 0.4261 0.4498 0.0052 0.0890 -0.0545 325 VAL A CG1 2182 C CG2 . VAL A 284 ? 0.3642 0.4044 0.4312 0.0024 0.0870 -0.0498 325 VAL A CG2 2183 N N . PRO A 285 ? 0.3747 0.4159 0.4483 0.0035 0.1046 -0.0465 326 PRO A N 2184 C CA . PRO A 285 ? 0.3713 0.4131 0.4484 0.0025 0.1084 -0.0434 326 PRO A CA 2185 C C . PRO A 285 ? 0.3655 0.4066 0.4393 0.0009 0.1042 -0.0415 326 PRO A C 2186 O O . PRO A 285 ? 0.3614 0.4034 0.4406 -0.0003 0.1060 -0.0390 326 PRO A O 2187 C CB . PRO A 285 ? 0.3879 0.4267 0.4548 0.0041 0.1150 -0.0424 326 PRO A CB 2188 C CG . PRO A 285 ? 0.4089 0.4450 0.4639 0.0057 0.1126 -0.0450 326 PRO A CG 2189 C CD . PRO A 285 ? 0.3897 0.4278 0.4514 0.0054 0.1076 -0.0478 326 PRO A CD 2190 N N . TYR A 286 ? 0.3620 0.4013 0.4271 0.0009 0.0988 -0.0426 327 TYR A N 2191 C CA . TYR A 286 ? 0.3557 0.3939 0.4160 -0.0004 0.0948 -0.0409 327 TYR A CA 2192 C C . TYR A 286 ? 0.3659 0.4016 0.4181 -0.0003 0.0992 -0.0382 327 TYR A C 2193 O O . TYR A 286 ? 0.3676 0.4033 0.4206 -0.0016 0.0984 -0.0359 327 TYR A O 2194 C CB . TYR A 286 ? 0.3491 0.3901 0.4208 -0.0020 0.0910 -0.0401 327 TYR A CB 2195 C CG . TYR A 286 ? 0.3467 0.3890 0.4224 -0.0018 0.0854 -0.0426 327 TYR A CG 2196 C CD1 . TYR A 286 ? 0.3209 0.3618 0.3897 -0.0020 0.0798 -0.0431 327 TYR A CD1 2197 C CD2 . TYR A 286 ? 0.3327 0.3775 0.4188 -0.0013 0.0859 -0.0442 327 TYR A CD2 2198 C CE1 . TYR A 286 ? 0.2915 0.3332 0.3635 -0.0016 0.0751 -0.0451 327 TYR A CE1 2199 C CE2 . TYR A 286 ? 0.3075 0.3532 0.3967 -0.0008 0.0810 -0.0463 327 TYR A CE2 2200 C CZ . TYR A 286 ? 0.3073 0.3513 0.3892 -0.0009 0.0756 -0.0466 327 TYR A CZ 2201 O OH . TYR A 286 ? 0.2985 0.3430 0.3831 -0.0003 0.0710 -0.0484 327 TYR A OH 2202 N N . ASN A 287 ? 0.3685 0.4020 0.4126 0.0015 0.1039 -0.0386 328 ASN A N 2203 C CA . ASN A 287 ? 0.3797 0.4101 0.4137 0.0021 0.1077 -0.0363 328 ASN A CA 2204 C C . ASN A 287 ? 0.3765 0.4047 0.4007 0.0016 0.1025 -0.0360 328 ASN A C 2205 O O . ASN A 287 ? 0.3725 0.4003 0.3930 0.0017 0.0973 -0.0383 328 ASN A O 2206 C CB . ASN A 287 ? 0.3808 0.4087 0.4061 0.0046 0.1127 -0.0373 328 ASN A CB 2207 C CG . ASN A 287 ? 0.3928 0.4224 0.4270 0.0053 0.1194 -0.0369 328 ASN A CG 2208 O OD1 . ASN A 287 ? 0.4010 0.4328 0.4456 0.0040 0.1220 -0.0346 328 ASN A OD1 2209 N ND2 . ASN A 287 ? 0.4031 0.4317 0.4339 0.0074 0.1221 -0.0392 328 ASN A ND2 2210 N N . VAL A 288 ? 0.3956 0.4222 0.4156 0.0011 0.1041 -0.0331 329 VAL A N 2211 C CA . VAL A 288 ? 0.4050 0.4297 0.4165 0.0005 0.0993 -0.0324 329 VAL A CA 2212 C C . VAL A 288 ? 0.4120 0.4330 0.4087 0.0025 0.0992 -0.0337 329 VAL A C 2213 O O . VAL A 288 ? 0.3988 0.4183 0.3884 0.0023 0.0942 -0.0343 329 VAL A O 2214 C CB . VAL A 288 ? 0.4225 0.4470 0.4358 -0.0007 0.1009 -0.0288 329 VAL A CB 2215 C CG1 . VAL A 288 ? 0.4282 0.4500 0.4306 -0.0008 0.0972 -0.0280 329 VAL A CG1 2216 C CG2 . VAL A 288 ? 0.4179 0.4461 0.4453 -0.0029 0.0983 -0.0283 329 VAL A CG2 2217 N N . GLY A 289 ? 0.4174 0.4366 0.4093 0.0046 0.1047 -0.0341 330 GLY A N 2218 C CA . GLY A 289 ? 0.4240 0.4390 0.4010 0.0069 0.1048 -0.0352 330 GLY A CA 2219 C C . GLY A 289 ? 0.4288 0.4409 0.3974 0.0077 0.1080 -0.0320 330 GLY A C 2220 O O . GLY A 289 ? 0.4315 0.4443 0.4055 0.0070 0.1126 -0.0289 330 GLY A O 2221 N N . PRO A 290 ? 0.4452 0.4536 0.4004 0.0092 0.1055 -0.0327 331 PRO A N 2222 C CA . PRO A 290 ? 0.4495 0.4567 0.3982 0.0100 0.1000 -0.0364 331 PRO A CA 2223 C C . PRO A 290 ? 0.4640 0.4701 0.4097 0.0123 0.1024 -0.0394 331 PRO A C 2224 O O . PRO A 290 ? 0.4738 0.4785 0.4168 0.0143 0.1090 -0.0385 331 PRO A O 2225 C CB . PRO A 290 ? 0.4610 0.4642 0.3962 0.0113 0.0983 -0.0356 331 PRO A CB 2226 C CG . PRO A 290 ? 0.4892 0.4902 0.4202 0.0127 0.1053 -0.0322 331 PRO A CG 2227 C CD . PRO A 290 ? 0.4688 0.4737 0.4142 0.0104 0.1087 -0.0297 331 PRO A CD 2228 N N . GLY A 291 ? 0.4602 0.4668 0.4065 0.0123 0.0974 -0.0430 332 GLY A N 2229 C CA . GLY A 291 ? 0.4603 0.4655 0.4025 0.0146 0.0986 -0.0464 332 GLY A CA 2230 C C . GLY A 291 ? 0.4623 0.4701 0.4145 0.0146 0.1027 -0.0471 332 GLY A C 2231 O O . GLY A 291 ? 0.4490 0.4602 0.4127 0.0126 0.1043 -0.0450 332 GLY A O 2232 N N . PHE A 292 ? 0.4696 0.4757 0.4174 0.0170 0.1042 -0.0502 333 PHE A N 2233 C CA . PHE A 292 ? 0.4769 0.4852 0.4333 0.0173 0.1074 -0.0516 333 PHE A CA 2234 C C . PHE A 292 ? 0.4951 0.5020 0.4488 0.0195 0.1158 -0.0500 333 PHE A C 2235 O O . PHE A 292 ? 0.4994 0.5027 0.4421 0.0214 0.1186 -0.0484 333 PHE A O 2236 C CB . PHE A 292 ? 0.4787 0.4858 0.4322 0.0187 0.1040 -0.0561 333 PHE A CB 2237 C CG . PHE A 292 ? 0.4807 0.4895 0.4388 0.0166 0.0965 -0.0578 333 PHE A CG 2238 C CD1 . PHE A 292 ? 0.4809 0.4874 0.4329 0.0177 0.0920 -0.0614 333 PHE A CD1 2239 C CD2 . PHE A 292 ? 0.4680 0.4804 0.4366 0.0136 0.0941 -0.0558 333 PHE A CD2 2240 C CE1 . PHE A 292 ? 0.4911 0.4991 0.4478 0.0158 0.0856 -0.0626 333 PHE A CE1 2241 C CE2 . PHE A 292 ? 0.4392 0.4528 0.4116 0.0120 0.0876 -0.0571 333 PHE A CE2 2242 C CZ . PHE A 292 ? 0.4186 0.4300 0.3853 0.0130 0.0836 -0.0603 333 PHE A CZ 2243 N N . THR A 293 ? 0.5022 0.5118 0.4661 0.0195 0.1198 -0.0503 334 THR A N 2244 C CA . THR A 293 ? 0.5383 0.5468 0.5008 0.0217 0.1283 -0.0487 334 THR A CA 2245 C C . THR A 293 ? 0.5676 0.5714 0.5162 0.0256 0.1305 -0.0513 334 THR A C 2246 O O . THR A 293 ? 0.5688 0.5711 0.5120 0.0265 0.1254 -0.0550 334 THR A O 2247 C CB . THR A 293 ? 0.5322 0.5447 0.5094 0.0208 0.1320 -0.0488 334 THR A CB 2248 O OG1 . THR A 293 ? 0.5311 0.5450 0.5126 0.0207 0.1278 -0.0527 334 THR A OG1 2249 C CG2 . THR A 293 ? 0.5306 0.5471 0.5211 0.0177 0.1318 -0.0457 334 THR A CG2 2250 N N . GLY A 294 ? 0.5891 0.5906 0.5326 0.0281 0.1382 -0.0493 335 GLY A N 2251 C CA . GLY A 294 ? 0.6206 0.6169 0.5488 0.0324 0.1410 -0.0511 335 GLY A CA 2252 C C . GLY A 294 ? 0.6353 0.6299 0.5582 0.0343 0.1370 -0.0563 335 GLY A C 2253 O O . GLY A 294 ? 0.6532 0.6436 0.5626 0.0365 0.1338 -0.0584 335 GLY A O 2254 N N . ASN A 295 ? 0.6341 0.6319 0.5677 0.0336 0.1371 -0.0585 336 ASN A N 2255 C CA . ASN A 295 ? 0.6485 0.6447 0.5784 0.0353 0.1335 -0.0635 336 ASN A CA 2256 C C . ASN A 295 ? 0.6374 0.6328 0.5636 0.0339 0.1244 -0.0660 336 ASN A C 2257 O O . ASN A 295 ? 0.6457 0.6380 0.5636 0.0361 0.1210 -0.0700 336 ASN A O 2258 C CB . ASN A 295 ? 0.6500 0.6503 0.5941 0.0341 0.1344 -0.0651 336 ASN A CB 2259 C CG . ASN A 295 ? 0.7085 0.7091 0.6556 0.0362 0.1435 -0.0638 336 ASN A CG 2260 O OD1 . ASN A 295 ? 0.7521 0.7503 0.6925 0.0380 0.1497 -0.0609 336 ASN A OD1 2261 N ND2 . ASN A 295 ? 0.7479 0.7512 0.7053 0.0360 0.1444 -0.0659 336 ASN A ND2 2262 N N . PHE A 296 ? 0.6147 0.6129 0.5474 0.0305 0.1204 -0.0638 337 PHE A N 2263 C CA . PHE A 296 ? 0.5960 0.5943 0.5281 0.0288 0.1121 -0.0657 337 PHE A CA 2264 C C . PHE A 296 ? 0.5954 0.5916 0.5189 0.0283 0.1094 -0.0636 337 PHE A C 2265 O O . PHE A 296 ? 0.5873 0.5840 0.5113 0.0265 0.1028 -0.0644 337 PHE A O 2266 C CB . PHE A 296 ? 0.5791 0.5824 0.5265 0.0252 0.1089 -0.0652 337 PHE A CB 2267 C CG . PHE A 296 ? 0.5679 0.5737 0.5251 0.0254 0.1117 -0.0667 337 PHE A CG 2268 C CD1 . PHE A 296 ? 0.5597 0.5689 0.5275 0.0243 0.1167 -0.0640 337 PHE A CD1 2269 C CD2 . PHE A 296 ? 0.5643 0.5689 0.5205 0.0268 0.1093 -0.0710 337 PHE A CD2 2270 C CE1 . PHE A 296 ? 0.5533 0.5649 0.5308 0.0246 0.1192 -0.0655 337 PHE A CE1 2271 C CE2 . PHE A 296 ? 0.5614 0.5683 0.5269 0.0271 0.1119 -0.0724 337 PHE A CE2 2272 C CZ . PHE A 296 ? 0.5627 0.5731 0.5387 0.0260 0.1168 -0.0696 337 PHE A CZ 2273 N N . SER A 297 ? 0.5926 0.5864 0.5084 0.0301 0.1149 -0.0608 338 SER A N 2274 C CA . SER A 297 ? 0.5935 0.5853 0.5014 0.0299 0.1134 -0.0582 338 SER A CA 2275 C C . SER A 297 ? 0.5872 0.5757 0.4844 0.0310 0.1065 -0.0612 338 SER A C 2276 O O . SER A 297 ? 0.5957 0.5839 0.4903 0.0296 0.1028 -0.0596 338 SER A O 2277 C CB . SER A 297 ? 0.6087 0.5975 0.5082 0.0326 0.1210 -0.0552 338 SER A CB 2278 O OG . SER A 297 ? 0.6451 0.6291 0.5316 0.0369 0.1227 -0.0580 338 SER A OG 2279 N N . THR A 298 ? 0.5746 0.5608 0.4666 0.0334 0.1045 -0.0657 339 THR A N 2280 C CA . THR A 298 ? 0.5643 0.5472 0.4468 0.0346 0.0977 -0.0689 339 THR A CA 2281 C C . THR A 298 ? 0.5518 0.5375 0.4433 0.0316 0.0904 -0.0713 339 THR A C 2282 O O . THR A 298 ? 0.5512 0.5348 0.4373 0.0321 0.0843 -0.0738 339 THR A O 2283 C CB . THR A 298 ? 0.5815 0.5594 0.4515 0.0391 0.0986 -0.0728 339 THR A CB 2284 O OG1 . THR A 298 ? 0.5873 0.5667 0.4641 0.0395 0.1001 -0.0756 339 THR A OG1 2285 C CG2 . THR A 298 ? 0.5891 0.5635 0.4479 0.0424 0.1054 -0.0702 339 THR A CG2 2286 N N . GLN A 299 ? 0.5200 0.5103 0.4253 0.0289 0.0911 -0.0704 340 GLN A N 2287 C CA . GLN A 299 ? 0.5079 0.5009 0.4224 0.0261 0.0849 -0.0719 340 GLN A CA 2288 C C . GLN A 299 ? 0.4976 0.4922 0.4143 0.0234 0.0819 -0.0686 340 GLN A C 2289 O O . GLN A 299 ? 0.4895 0.4844 0.4046 0.0231 0.0855 -0.0649 340 GLN A O 2290 C CB . GLN A 299 ? 0.4915 0.4883 0.4189 0.0246 0.0868 -0.0721 340 GLN A CB 2291 C CG . GLN A 299 ? 0.5040 0.4990 0.4291 0.0274 0.0896 -0.0755 340 GLN A CG 2292 C CD . GLN A 299 ? 0.5235 0.5220 0.4613 0.0262 0.0910 -0.0761 340 GLN A CD 2293 O OE1 . GLN A 299 ? 0.5215 0.5239 0.4701 0.0234 0.0910 -0.0736 340 GLN A OE1 2294 N NE2 . GLN A 299 ? 0.5542 0.5511 0.4905 0.0284 0.0922 -0.0797 340 GLN A NE2 2295 N N . LYS A 300 ? 0.4825 0.4780 0.4026 0.0217 0.0754 -0.0701 341 LYS A N 2296 C CA . LYS A 300 ? 0.4679 0.4649 0.3903 0.0192 0.0721 -0.0673 341 LYS A CA 2297 C C . LYS A 300 ? 0.4470 0.4473 0.3808 0.0165 0.0678 -0.0678 341 LYS A C 2298 O O . LYS A 300 ? 0.4300 0.4308 0.3686 0.0167 0.0668 -0.0706 341 LYS A O 2299 C CB . LYS A 300 ? 0.4862 0.4796 0.3974 0.0205 0.0682 -0.0682 341 LYS A CB 2300 C CG . LYS A 300 ? 0.5353 0.5252 0.4342 0.0232 0.0724 -0.0668 341 LYS A CG 2301 C CD . LYS A 300 ? 0.6192 0.6066 0.5092 0.0236 0.0686 -0.0660 341 LYS A CD 2302 C CE . LYS A 300 ? 0.6879 0.6707 0.5637 0.0272 0.0721 -0.0655 341 LYS A CE 2303 N NZ . LYS A 300 ? 0.7065 0.6900 0.5828 0.0275 0.0798 -0.0615 341 LYS A NZ 2304 N N . VAL A 301 ? 0.4146 0.4168 0.3525 0.0141 0.0655 -0.0650 342 VAL A N 2305 C CA . VAL A 301 ? 0.3976 0.4025 0.3451 0.0118 0.0613 -0.0652 342 VAL A CA 2306 C C . VAL A 301 ? 0.3889 0.3923 0.3326 0.0114 0.0555 -0.0661 342 VAL A C 2307 O O . VAL A 301 ? 0.4077 0.4095 0.3444 0.0116 0.0548 -0.0647 342 VAL A O 2308 C CB . VAL A 301 ? 0.3908 0.3991 0.3468 0.0095 0.0627 -0.0615 342 VAL A CB 2309 C CG1 . VAL A 301 ? 0.3555 0.3657 0.3188 0.0075 0.0578 -0.0612 342 VAL A CG1 2310 C CG2 . VAL A 301 ? 0.3894 0.3997 0.3521 0.0098 0.0675 -0.0613 342 VAL A CG2 2311 N N . LYS A 302 ? 0.3752 0.3789 0.3237 0.0108 0.0516 -0.0685 343 LYS A N 2312 C CA . LYS A 302 ? 0.3848 0.3873 0.3312 0.0104 0.0462 -0.0697 343 LYS A CA 2313 C C . LYS A 302 ? 0.3762 0.3813 0.3326 0.0081 0.0432 -0.0686 343 LYS A C 2314 O O . LYS A 302 ? 0.3677 0.3739 0.3312 0.0078 0.0434 -0.0697 343 LYS A O 2315 C CB . LYS A 302 ? 0.4077 0.4073 0.3500 0.0124 0.0439 -0.0742 343 LYS A CB 2316 C CG . LYS A 302 ? 0.4252 0.4232 0.3652 0.0121 0.0382 -0.0757 343 LYS A CG 2317 C CD . LYS A 302 ? 0.4736 0.4684 0.4092 0.0143 0.0357 -0.0806 343 LYS A CD 2318 C CE . LYS A 302 ? 0.5200 0.5135 0.4541 0.0141 0.0298 -0.0821 343 LYS A CE 2319 N NZ . LYS A 302 ? 0.5652 0.5547 0.4910 0.0168 0.0273 -0.0866 343 LYS A NZ 2320 N N . MET A 303 ? 0.3696 0.3753 0.3262 0.0067 0.0406 -0.0664 344 MET A N 2321 C CA . MET A 303 ? 0.3537 0.3613 0.3186 0.0049 0.0375 -0.0654 344 MET A CA 2322 C C . MET A 303 ? 0.3652 0.3711 0.3300 0.0051 0.0330 -0.0681 344 MET A C 2323 O O . MET A 303 ? 0.3890 0.3926 0.3467 0.0063 0.0312 -0.0699 344 MET A O 2324 C CB . MET A 303 ? 0.3309 0.3399 0.2962 0.0035 0.0370 -0.0616 344 MET A CB 2325 C CG . MET A 303 ? 0.3222 0.3326 0.2877 0.0033 0.0412 -0.0591 344 MET A CG 2326 S SD . MET A 303 ? 0.1119 0.1240 0.0787 0.0015 0.0405 -0.0548 344 MET A SD 2327 C CE . MET A 303 ? 0.3182 0.3325 0.2953 0.0002 0.0379 -0.0543 344 MET A CE 2328 N N . HIS A 304 ? 0.3512 0.3582 0.3242 0.0041 0.0310 -0.0682 345 HIS A N 2329 C CA . HIS A 304 ? 0.3421 0.3479 0.3167 0.0040 0.0268 -0.0702 345 HIS A CA 2330 C C . HIS A 304 ? 0.3287 0.3363 0.3105 0.0023 0.0252 -0.0675 345 HIS A C 2331 O O . HIS A 304 ? 0.3240 0.3328 0.3131 0.0018 0.0259 -0.0669 345 HIS A O 2332 C CB . HIS A 304 ? 0.3607 0.3652 0.3384 0.0049 0.0263 -0.0739 345 HIS A CB 2333 C CG . HIS A 304 ? 0.3887 0.3921 0.3615 0.0067 0.0294 -0.0761 345 HIS A CG 2334 N ND1 . HIS A 304 ? 0.4545 0.4550 0.4206 0.0085 0.0282 -0.0798 345 HIS A ND1 2335 C CD2 . HIS A 304 ? 0.3867 0.3913 0.3608 0.0070 0.0336 -0.0752 345 HIS A CD2 2336 C CE1 . HIS A 304 ? 0.4235 0.4234 0.3862 0.0100 0.0318 -0.0809 345 HIS A CE1 2337 N NE2 . HIS A 304 ? 0.4548 0.4573 0.4228 0.0091 0.0352 -0.0781 345 HIS A NE2 2338 N N . ILE A 305 ? 0.3191 0.3268 0.2987 0.0016 0.0231 -0.0658 346 ILE A N 2339 C CA . ILE A 305 ? 0.3094 0.3187 0.2949 0.0002 0.0219 -0.0628 346 ILE A CA 2340 C C . ILE A 305 ? 0.3142 0.3224 0.3011 -0.0001 0.0180 -0.0639 346 ILE A C 2341 O O . ILE A 305 ? 0.3190 0.3260 0.3001 0.0002 0.0161 -0.0648 346 ILE A O 2342 C CB . ILE A 305 ? 0.3163 0.3269 0.2990 -0.0005 0.0233 -0.0593 346 ILE A CB 2343 C CG1 . ILE A 305 ? 0.2894 0.3011 0.2711 -0.0001 0.0272 -0.0585 346 ILE A CG1 2344 C CG2 . ILE A 305 ? 0.3193 0.3314 0.3077 -0.0016 0.0221 -0.0564 346 ILE A CG2 2345 C CD1 . ILE A 305 ? 0.3396 0.3525 0.3285 -0.0001 0.0290 -0.0586 346 ILE A CD1 2346 N N . HIS A 306 ? 0.3113 0.3199 0.3060 -0.0007 0.0170 -0.0636 347 HIS A N 2347 C CA . HIS A 306 ? 0.3100 0.3178 0.3083 -0.0011 0.0135 -0.0647 347 HIS A CA 2348 C C . HIS A 306 ? 0.3004 0.3093 0.3053 -0.0021 0.0130 -0.0616 347 HIS A C 2349 O O . HIS A 306 ? 0.2961 0.3044 0.3062 -0.0024 0.0108 -0.0621 347 HIS A O 2350 C CB . HIS A 306 ? 0.3308 0.3370 0.3325 -0.0004 0.0125 -0.0685 347 HIS A CB 2351 C CG . HIS A 306 ? 0.4001 0.4048 0.3950 0.0009 0.0131 -0.0717 347 HIS A CG 2352 N ND1 . HIS A 306 ? 0.4536 0.4583 0.4496 0.0017 0.0156 -0.0731 347 HIS A ND1 2353 C CD2 . HIS A 306 ? 0.4557 0.4589 0.4424 0.0019 0.0118 -0.0737 347 HIS A CD2 2354 C CE1 . HIS A 306 ? 0.4511 0.4542 0.4397 0.0030 0.0160 -0.0758 347 HIS A CE1 2355 N NE2 . HIS A 306 ? 0.4844 0.4864 0.4670 0.0033 0.0137 -0.0762 347 HIS A NE2 2356 N N . SER A 307 ? 0.2780 0.2885 0.2826 -0.0024 0.0151 -0.0583 348 SER A N 2357 C CA . SER A 307 ? 0.2503 0.2616 0.2597 -0.0030 0.0149 -0.0550 348 SER A CA 2358 C C . SER A 307 ? 0.2776 0.2887 0.2861 -0.0035 0.0124 -0.0543 348 SER A C 2359 O O . SER A 307 ? 0.2804 0.2910 0.2829 -0.0034 0.0111 -0.0555 348 SER A O 2360 C CB . SER A 307 ? 0.2544 0.2672 0.2619 -0.0030 0.0171 -0.0520 348 SER A CB 2361 O OG . SER A 307 ? 0.2516 0.2648 0.2602 -0.0024 0.0194 -0.0528 348 SER A OG 2362 N N . THR A 308 ? 0.2595 0.2708 0.2736 -0.0038 0.0119 -0.0522 349 THR A N 2363 C CA . THR A 308 ? 0.2637 0.2750 0.2779 -0.0043 0.0096 -0.0514 349 THR A CA 2364 C C . THR A 308 ? 0.2680 0.2802 0.2834 -0.0044 0.0105 -0.0474 349 THR A C 2365 O O . THR A 308 ? 0.2736 0.2861 0.2927 -0.0040 0.0123 -0.0455 349 THR A O 2366 C CB . THR A 308 ? 0.2859 0.2963 0.3069 -0.0045 0.0077 -0.0531 349 THR A CB 2367 O OG1 . THR A 308 ? 0.3544 0.3648 0.3824 -0.0043 0.0094 -0.0514 349 THR A OG1 2368 C CG2 . THR A 308 ? 0.2719 0.2810 0.2915 -0.0042 0.0063 -0.0574 349 THR A CG2 2369 N N . ASN A 309 ? 0.2544 0.2670 0.2665 -0.0048 0.0091 -0.0462 350 ASN A N 2370 C CA . ASN A 309 ? 0.2569 0.2702 0.2699 -0.0048 0.0097 -0.0426 350 ASN A CA 2371 C C . ASN A 309 ? 0.2650 0.2780 0.2844 -0.0049 0.0085 -0.0420 350 ASN A C 2372 O O . ASN A 309 ? 0.2848 0.2973 0.3054 -0.0053 0.0062 -0.0442 350 ASN A O 2373 C CB . ASN A 309 ? 0.2541 0.2678 0.2605 -0.0051 0.0088 -0.0417 350 ASN A CB 2374 C CG . ASN A 309 ? 0.2863 0.3005 0.2871 -0.0050 0.0103 -0.0419 350 ASN A CG 2375 O OD1 . ASN A 309 ? 0.2713 0.2858 0.2734 -0.0046 0.0122 -0.0414 350 ASN A OD1 2376 N ND2 . ASN A 309 ? 0.3307 0.3447 0.3253 -0.0052 0.0094 -0.0424 350 ASN A ND2 2377 N N . GLU A 310 ? 0.2576 0.2706 0.2812 -0.0044 0.0100 -0.0391 351 GLU A N 2378 C CA . GLU A 310 ? 0.2618 0.2743 0.2923 -0.0045 0.0095 -0.0383 351 GLU A CA 2379 C C . GLU A 310 ? 0.2461 0.2587 0.2776 -0.0037 0.0110 -0.0344 351 GLU A C 2380 O O . GLU A 310 ? 0.2351 0.2476 0.2650 -0.0028 0.0129 -0.0325 351 GLU A O 2381 C CB . GLU A 310 ? 0.2931 0.3047 0.3303 -0.0042 0.0107 -0.0392 351 GLU A CB 2382 C CG . GLU A 310 ? 0.3837 0.3950 0.4194 -0.0043 0.0106 -0.0424 351 GLU A CG 2383 C CD . GLU A 310 ? 0.5220 0.5323 0.5653 -0.0043 0.0109 -0.0439 351 GLU A CD 2384 O OE1 . GLU A 310 ? 0.6059 0.6157 0.6499 -0.0048 0.0088 -0.0475 351 GLU A OE1 2385 O OE2 . GLU A 310 ? 0.5103 0.5200 0.5586 -0.0036 0.0130 -0.0415 351 GLU A OE2 2386 N N . VAL A 311 ? 0.2246 0.2374 0.2587 -0.0040 0.0099 -0.0334 352 VAL A N 2387 C CA . VAL A 311 ? 0.2066 0.2193 0.2419 -0.0031 0.0115 -0.0296 352 VAL A CA 2388 C C . VAL A 311 ? 0.2213 0.2328 0.2629 -0.0021 0.0140 -0.0280 352 VAL A C 2389 O O . VAL A 311 ? 0.2267 0.2377 0.2753 -0.0025 0.0139 -0.0292 352 VAL A O 2390 C CB . VAL A 311 ? 0.2116 0.2247 0.2487 -0.0035 0.0100 -0.0288 352 VAL A CB 2391 C CG1 . VAL A 311 ? 0.2116 0.2244 0.2504 -0.0022 0.0120 -0.0249 352 VAL A CG1 2392 C CG2 . VAL A 311 ? 0.2219 0.2359 0.2518 -0.0042 0.0077 -0.0300 352 VAL A CG2 2393 N N . THR A 312 ? 0.2026 0.2136 0.2421 -0.0006 0.0161 -0.0253 353 THR A N 2394 C CA . THR A 312 ? 0.2060 0.2155 0.2497 0.0007 0.0186 -0.0238 353 THR A CA 2395 C C . THR A 312 ? 0.2087 0.2173 0.2508 0.0027 0.0206 -0.0198 353 THR A C 2396 O O . THR A 312 ? 0.2148 0.2239 0.2508 0.0032 0.0199 -0.0188 353 THR A O 2397 C CB . THR A 312 ? 0.2190 0.2284 0.2604 0.0009 0.0189 -0.0256 353 THR A CB 2398 O OG1 . THR A 312 ? 0.2359 0.2462 0.2773 -0.0008 0.0170 -0.0294 353 THR A OG1 2399 C CG2 . THR A 312 ? 0.2242 0.2320 0.2703 0.0022 0.0213 -0.0243 353 THR A CG2 2400 N N . ARG A 313 ? 0.2057 0.2126 0.2530 0.0040 0.0230 -0.0176 354 ARG A N 2401 C CA . ARG A 313 ? 0.1981 0.2037 0.2434 0.0064 0.0251 -0.0136 354 ARG A CA 2402 C C . ARG A 313 ? 0.2083 0.2127 0.2486 0.0083 0.0259 -0.0128 354 ARG A C 2403 O O . ARG A 313 ? 0.1967 0.2007 0.2389 0.0083 0.0264 -0.0141 354 ARG A O 2404 C CB . ARG A 313 ? 0.2052 0.2091 0.2579 0.0073 0.0279 -0.0110 354 ARG A CB 2405 C CG . ARG A 313 ? 0.2310 0.2330 0.2810 0.0101 0.0303 -0.0068 354 ARG A CG 2406 C CD . ARG A 313 ? 0.2398 0.2409 0.2976 0.0105 0.0328 -0.0044 354 ARG A CD 2407 N NE . ARG A 313 ? 0.2238 0.2270 0.2834 0.0085 0.0307 -0.0056 354 ARG A NE 2408 C CZ . ARG A 313 ? 0.2863 0.2894 0.3523 0.0085 0.0322 -0.0038 354 ARG A CZ 2409 N NH1 . ARG A 313 ? 0.2640 0.2650 0.3352 0.0103 0.0361 -0.0005 354 ARG A NH1 2410 N NH2 . ARG A 313 ? 0.3151 0.3201 0.3823 0.0068 0.0298 -0.0051 354 ARG A NH2 2411 N N . ILE A 314 ? 0.1934 0.1974 0.2277 0.0100 0.0259 -0.0108 355 ILE A N 2412 C CA . ILE A 314 ? 0.1936 0.1965 0.2230 0.0122 0.0262 -0.0100 355 ILE A CA 2413 C C . ILE A 314 ? 0.2018 0.2024 0.2291 0.0153 0.0281 -0.0062 355 ILE A C 2414 O O . ILE A 314 ? 0.1991 0.1996 0.2274 0.0153 0.0288 -0.0045 355 ILE A O 2415 C CB . ILE A 314 ? 0.1800 0.1846 0.2035 0.0113 0.0237 -0.0119 355 ILE A CB 2416 C CG1 . ILE A 314 ? 0.1861 0.1915 0.2063 0.0109 0.0225 -0.0110 355 ILE A CG1 2417 C CG2 . ILE A 314 ? 0.1869 0.1935 0.2123 0.0086 0.0223 -0.0155 355 ILE A CG2 2418 C CD1 . ILE A 314 ? 0.1892 0.1954 0.2033 0.0110 0.0205 -0.0118 355 ILE A CD1 2419 N N . TYR A 315 ? 0.1927 0.1913 0.2168 0.0180 0.0289 -0.0050 356 TYR A N 2420 C CA . TYR A 315 ? 0.1994 0.1951 0.2210 0.0216 0.0311 -0.0012 356 TYR A CA 2421 C C . TYR A 315 ? 0.1924 0.1870 0.2067 0.0242 0.0297 -0.0009 356 TYR A C 2422 O O . TYR A 315 ? 0.2035 0.1976 0.2170 0.0251 0.0291 -0.0020 356 TYR A O 2423 C CB . TYR A 315 ? 0.1921 0.1854 0.2182 0.0231 0.0341 0.0005 356 TYR A CB 2424 C CG . TYR A 315 ? 0.2147 0.2088 0.2493 0.0208 0.0356 0.0003 356 TYR A CG 2425 C CD1 . TYR A 315 ? 0.2454 0.2384 0.2833 0.0215 0.0381 0.0031 356 TYR A CD1 2426 C CD2 . TYR A 315 ? 0.2307 0.2265 0.2702 0.0180 0.0345 -0.0030 356 TYR A CD2 2427 C CE1 . TYR A 315 ? 0.2340 0.2277 0.2807 0.0194 0.0392 0.0027 356 TYR A CE1 2428 C CE2 . TYR A 315 ? 0.2215 0.2178 0.2690 0.0159 0.0353 -0.0036 356 TYR A CE2 2429 C CZ . TYR A 315 ? 0.2531 0.2485 0.3045 0.0166 0.0375 -0.0008 356 TYR A CZ 2430 O OH . TYR A 315 ? 0.2835 0.2796 0.3441 0.0144 0.0381 -0.0016 356 TYR A OH 2431 N N . ASN A 316 ? 0.2058 0.1997 0.2152 0.0258 0.0291 0.0006 357 ASN A N 2432 C CA . ASN A 316 ? 0.2095 0.2016 0.2120 0.0290 0.0278 0.0011 357 ASN A CA 2433 C C . ASN A 316 ? 0.2123 0.2005 0.2126 0.0333 0.0306 0.0047 357 ASN A C 2434 O O . ASN A 316 ? 0.2379 0.2251 0.2404 0.0338 0.0333 0.0073 357 ASN A O 2435 C CB . ASN A 316 ? 0.2024 0.1954 0.2003 0.0289 0.0257 0.0010 357 ASN A CB 2436 C CG . ASN A 316 ? 0.2088 0.2054 0.2078 0.0250 0.0231 -0.0021 357 ASN A CG 2437 O OD1 . ASN A 316 ? 0.2177 0.2159 0.2188 0.0232 0.0220 -0.0046 357 ASN A OD1 2438 N ND2 . ASN A 316 ? 0.2219 0.2195 0.2193 0.0240 0.0221 -0.0019 357 ASN A ND2 2439 N N . VAL A 317 ? 0.2113 0.1973 0.2073 0.0366 0.0299 0.0051 358 VAL A N 2440 C CA . VAL A 317 ? 0.2146 0.1962 0.2065 0.0414 0.0325 0.0087 358 VAL A CA 2441 C C . VAL A 317 ? 0.2202 0.2005 0.2042 0.0441 0.0303 0.0091 358 VAL A C 2442 O O . VAL A 317 ? 0.2394 0.2208 0.2205 0.0440 0.0267 0.0065 358 VAL A O 2443 C CB . VAL A 317 ? 0.2244 0.2034 0.2157 0.0441 0.0333 0.0093 358 VAL A CB 2444 C CG1 . VAL A 317 ? 0.2401 0.2141 0.2272 0.0492 0.0368 0.0136 358 VAL A CG1 2445 C CG2 . VAL A 317 ? 0.2419 0.2224 0.2411 0.0411 0.0347 0.0081 358 VAL A CG2 2446 N N . ILE A 318 ? 0.2294 0.2075 0.2104 0.0465 0.0325 0.0121 359 ILE A N 2447 C CA . ILE A 318 ? 0.2245 0.2011 0.1978 0.0493 0.0304 0.0124 359 ILE A CA 2448 C C . ILE A 318 ? 0.2318 0.2033 0.1989 0.0552 0.0329 0.0159 359 ILE A C 2449 O O . ILE A 318 ? 0.2578 0.2276 0.2265 0.0563 0.0371 0.0192 359 ILE A O 2450 C CB . ILE A 318 ? 0.2383 0.2170 0.2128 0.0470 0.0305 0.0126 359 ILE A CB 2451 C CG1 . ILE A 318 ? 0.2327 0.2162 0.2135 0.0413 0.0286 0.0095 359 ILE A CG1 2452 C CG2 . ILE A 318 ? 0.2417 0.2188 0.2083 0.0499 0.0283 0.0128 359 ILE A CG2 2453 C CD1 . ILE A 318 ? 0.2814 0.2669 0.2600 0.0400 0.0243 0.0061 359 ILE A CD1 2454 N N . GLY A 319 ? 0.2548 0.2239 0.2154 0.0588 0.0304 0.0151 360 GLY A N 2455 C CA . GLY A 319 ? 0.2627 0.2263 0.2155 0.0652 0.0321 0.0181 360 GLY A CA 2456 C C . GLY A 319 ? 0.2790 0.2408 0.2238 0.0682 0.0297 0.0180 360 GLY A C 2457 O O . GLY A 319 ? 0.2713 0.2354 0.2152 0.0665 0.0253 0.0148 360 GLY A O 2458 N N . THR A 320 ? 0.2801 0.2375 0.2189 0.0730 0.0328 0.0216 361 THR A N 2459 C CA . THR A 320 ? 0.2943 0.2497 0.2250 0.0763 0.0308 0.0216 361 THR A CA 2460 C C . THR A 320 ? 0.3098 0.2591 0.2307 0.0835 0.0311 0.0235 361 THR A C 2461 O O . THR A 320 ? 0.3238 0.2698 0.2438 0.0864 0.0356 0.0270 361 THR A O 2462 C CB . THR A 320 ? 0.3104 0.2660 0.2425 0.0757 0.0346 0.0244 361 THR A CB 2463 O OG1 . THR A 320 ? 0.3149 0.2760 0.2557 0.0692 0.0340 0.0225 361 THR A OG1 2464 C CG2 . THR A 320 ? 0.3199 0.2730 0.2432 0.0794 0.0329 0.0246 361 THR A CG2 2465 N N . LEU A 321 ? 0.3034 0.2511 0.2170 0.0864 0.0262 0.0211 362 LEU A N 2466 C CA . LEU A 321 ? 0.3049 0.2463 0.2073 0.0941 0.0257 0.0226 362 LEU A CA 2467 C C . LEU A 321 ? 0.3251 0.2654 0.2213 0.0961 0.0240 0.0223 362 LEU A C 2468 O O . LEU A 321 ? 0.3171 0.2594 0.2127 0.0948 0.0186 0.0185 362 LEU A O 2469 C CB . LEU A 321 ? 0.3225 0.2633 0.2228 0.0956 0.0205 0.0193 362 LEU A CB 2470 C CG . LEU A 321 ? 0.3888 0.3230 0.2772 0.1037 0.0188 0.0202 362 LEU A CG 2471 C CD1 . LEU A 321 ? 0.4221 0.3514 0.3062 0.1081 0.0250 0.0252 362 LEU A CD1 2472 C CD2 . LEU A 321 ? 0.3834 0.3177 0.2720 0.1045 0.0138 0.0168 362 LEU A CD2 2473 N N . ARG A 322 ? 0.3169 0.2543 0.2096 0.0988 0.0289 0.0262 363 ARG A N 2474 C CA . ARG A 322 ? 0.3375 0.2739 0.2251 0.1004 0.0282 0.0263 363 ARG A CA 2475 C C . ARG A 322 ? 0.3481 0.2804 0.2246 0.1062 0.0231 0.0242 363 ARG A C 2476 O O . ARG A 322 ? 0.3554 0.2826 0.2242 0.1121 0.0230 0.0252 363 ARG A O 2477 C CB . ARG A 322 ? 0.3486 0.2824 0.2349 0.1028 0.0351 0.0313 363 ARG A CB 2478 C CG . ARG A 322 ? 0.4036 0.3355 0.2834 0.1056 0.0350 0.0319 363 ARG A CG 2479 C CD . ARG A 322 ? 0.4940 0.4245 0.3753 0.1067 0.0424 0.0368 363 ARG A CD 2480 N NE . ARG A 322 ? 0.6036 0.5317 0.4868 0.1084 0.0477 0.0405 363 ARG A NE 2481 C CZ . ARG A 322 ? 0.6561 0.5778 0.5300 0.1153 0.0501 0.0432 363 ARG A CZ 2482 N NH1 . ARG A 322 ? 0.7065 0.6233 0.5679 0.1216 0.0474 0.0427 363 ARG A NH1 2483 N NH2 . ARG A 322 ? 0.6752 0.5952 0.5524 0.1160 0.0551 0.0466 363 ARG A NH2 2484 N N . GLY A 323 ? 0.3330 0.2672 0.2088 0.1048 0.0186 0.0211 364 GLY A N 2485 C CA . GLY A 323 ? 0.3383 0.2687 0.2042 0.1101 0.0132 0.0187 364 GLY A CA 2486 C C . GLY A 323 ? 0.3506 0.2747 0.2053 0.1173 0.0163 0.0219 364 GLY A C 2487 O O . GLY A 323 ? 0.3668 0.2908 0.2223 0.1168 0.0215 0.0253 364 GLY A O 2488 N N . ALA A 324 ? 0.3714 0.2901 0.2156 0.1240 0.0128 0.0209 365 ALA A N 2489 C CA . ALA A 324 ? 0.3865 0.2984 0.2182 0.1317 0.0151 0.0236 365 ALA A CA 2490 C C . ALA A 324 ? 0.4060 0.3177 0.2340 0.1324 0.0129 0.0221 365 ALA A C 2491 O O . ALA A 324 ? 0.4239 0.3314 0.2443 0.1371 0.0169 0.0253 365 ALA A O 2492 C CB . ALA A 324 ? 0.3875 0.2936 0.2089 0.1388 0.0114 0.0224 365 ALA A CB 2493 N N . VAL A 325 ? 0.3726 0.2881 0.2050 0.1285 0.0065 0.0174 366 VAL A N 2494 C CA . VAL A 325 ? 0.3921 0.3068 0.2202 0.1298 0.0035 0.0156 366 VAL A CA 2495 C C . VAL A 325 ? 0.3842 0.3055 0.2230 0.1221 0.0037 0.0146 366 VAL A C 2496 O O . VAL A 325 ? 0.3851 0.3064 0.2227 0.1221 0.0058 0.0159 366 VAL A O 2497 C CB . VAL A 325 ? 0.4093 0.3214 0.2312 0.1336 -0.0047 0.0108 366 VAL A CB 2498 C CG1 . VAL A 325 ? 0.4094 0.3209 0.2280 0.1345 -0.0081 0.0086 366 VAL A CG1 2499 C CG2 . VAL A 325 ? 0.4411 0.3458 0.2506 0.1423 -0.0051 0.0119 366 VAL A CG2 2500 N N . GLU A 326 ? 0.3542 0.2810 0.2034 0.1156 0.0017 0.0124 367 GLU A N 2501 C CA . GLU A 326 ? 0.3555 0.2886 0.2148 0.1082 0.0015 0.0112 367 GLU A CA 2502 C C . GLU A 326 ? 0.3291 0.2666 0.1982 0.1026 0.0059 0.0131 367 GLU A C 2503 O O . GLU A 326 ? 0.3155 0.2574 0.1925 0.0975 0.0033 0.0105 367 GLU A O 2504 C CB . GLU A 326 ? 0.3506 0.2863 0.2133 0.1054 -0.0056 0.0062 367 GLU A CB 2505 C CG . GLU A 326 ? 0.3984 0.3302 0.2528 0.1103 -0.0105 0.0038 367 GLU A CG 2506 C CD . GLU A 326 ? 0.3626 0.2978 0.2227 0.1065 -0.0170 -0.0009 367 GLU A CD 2507 O OE1 . GLU A 326 ? 0.3812 0.3194 0.2457 0.1025 -0.0173 -0.0016 367 GLU A OE1 2508 O OE2 . GLU A 326 ? 0.4190 0.3535 0.2792 0.1077 -0.0217 -0.0040 367 GLU A OE2 2509 N N . PRO A 327 ? 0.3288 0.2651 0.1979 0.1035 0.0125 0.0175 368 PRO A N 2510 C CA . PRO A 327 ? 0.3174 0.2575 0.1961 0.0986 0.0168 0.0194 368 PRO A CA 2511 C C . PRO A 327 ? 0.2963 0.2427 0.1850 0.0911 0.0160 0.0178 368 PRO A C 2512 O O . PRO A 327 ? 0.3021 0.2521 0.1990 0.0864 0.0174 0.0176 368 PRO A O 2513 C CB . PRO A 327 ? 0.3375 0.2744 0.2135 0.1019 0.0239 0.0244 368 PRO A CB 2514 C CG . PRO A 327 ? 0.3404 0.2735 0.2073 0.1067 0.0233 0.0249 368 PRO A CG 2515 C CD . PRO A 327 ? 0.3584 0.2893 0.2185 0.1098 0.0165 0.0210 368 PRO A CD 2516 N N . ASP A 328 ? 0.2894 0.2368 0.1770 0.0903 0.0137 0.0163 369 ASP A N 2517 C CA . ASP A 328 ? 0.2970 0.2500 0.1933 0.0835 0.0127 0.0148 369 ASP A CA 2518 C C . ASP A 328 ? 0.2903 0.2459 0.1893 0.0805 0.0066 0.0104 369 ASP A C 2519 O O . ASP A 328 ? 0.2657 0.2250 0.1694 0.0761 0.0047 0.0087 369 ASP A O 2520 C CB . ASP A 328 ? 0.3129 0.2655 0.2072 0.0840 0.0137 0.0159 369 ASP A CB 2521 C CG . ASP A 328 ? 0.3704 0.3202 0.2571 0.0876 0.0090 0.0136 369 ASP A CG 2522 O OD1 . ASP A 328 ? 0.3659 0.3126 0.2469 0.0915 0.0057 0.0119 369 ASP A OD1 2523 O OD2 . ASP A 328 ? 0.3766 0.3272 0.2631 0.0868 0.0082 0.0133 369 ASP A OD2 2524 N N . ARG A 329 ? 0.2804 0.2345 0.1773 0.0825 0.0039 0.0087 370 ARG A N 2525 C CA . ARG A 329 ? 0.2647 0.2217 0.1658 0.0793 -0.0012 0.0047 370 ARG A CA 2526 C C . ARG A 329 ? 0.2712 0.2297 0.1769 0.0776 -0.0001 0.0046 370 ARG A C 2527 O O . ARG A 329 ? 0.2677 0.2227 0.1690 0.0819 0.0013 0.0061 370 ARG A O 2528 C CB . ARG A 329 ? 0.2680 0.2214 0.1620 0.0841 -0.0066 0.0021 370 ARG A CB 2529 C CG . ARG A 329 ? 0.2696 0.2219 0.1599 0.0852 -0.0082 0.0016 370 ARG A CG 2530 C CD . ARG A 329 ? 0.2913 0.2485 0.1894 0.0790 -0.0105 -0.0007 370 ARG A CD 2531 N NE . ARG A 329 ? 0.2761 0.2328 0.1718 0.0793 -0.0119 -0.0011 370 ARG A NE 2532 C CZ . ARG A 329 ? 0.2667 0.2248 0.1638 0.0773 -0.0085 0.0012 370 ARG A CZ 2533 N NH1 . ARG A 329 ? 0.2640 0.2237 0.1646 0.0753 -0.0032 0.0043 370 ARG A NH1 2534 N NH2 . ARG A 329 ? 0.2813 0.2393 0.1772 0.0770 -0.0105 0.0003 370 ARG A NH2 2535 N N . TYR A 330 ? 0.2320 0.1954 0.1463 0.0716 -0.0008 0.0029 371 TYR A N 2536 C CA . TYR A 330 ? 0.2384 0.2036 0.1578 0.0696 0.0009 0.0030 371 TYR A CA 2537 C C . TYR A 330 ? 0.2479 0.2150 0.1707 0.0679 -0.0034 -0.0006 371 TYR A C 2538 O O . TYR A 330 ? 0.2592 0.2295 0.1862 0.0641 -0.0061 -0.0030 371 TYR A O 2539 C CB . TYR A 330 ? 0.2346 0.2040 0.1618 0.0639 0.0043 0.0040 371 TYR A CB 2540 C CG . TYR A 330 ? 0.2494 0.2181 0.1760 0.0642 0.0087 0.0073 371 TYR A CG 2541 C CD1 . TYR A 330 ? 0.2604 0.2246 0.1808 0.0695 0.0117 0.0104 371 TYR A CD1 2542 C CD2 . TYR A 330 ? 0.2364 0.2088 0.1689 0.0594 0.0102 0.0075 371 TYR A CD2 2543 C CE1 . TYR A 330 ? 0.2639 0.2277 0.1849 0.0697 0.0162 0.0136 371 TYR A CE1 2544 C CE2 . TYR A 330 ? 0.2242 0.1963 0.1573 0.0595 0.0141 0.0105 371 TYR A CE2 2545 C CZ . TYR A 330 ? 0.2665 0.2343 0.1942 0.0646 0.0173 0.0136 371 TYR A CZ 2546 O OH . TYR A 330 ? 0.2577 0.2253 0.1869 0.0647 0.0215 0.0165 371 TYR A OH 2547 N N . VAL A 331 ? 0.2269 0.1921 0.1484 0.0705 -0.0038 -0.0008 372 VAL A N 2548 C CA . VAL A 331 ? 0.2339 0.2011 0.1598 0.0690 -0.0074 -0.0041 372 VAL A CA 2549 C C . VAL A 331 ? 0.2370 0.2065 0.1687 0.0660 -0.0037 -0.0029 372 VAL A C 2550 O O . VAL A 331 ? 0.2563 0.2231 0.1854 0.0686 -0.0004 -0.0003 372 VAL A O 2551 C CB . VAL A 331 ? 0.2607 0.2238 0.1806 0.0748 -0.0112 -0.0054 372 VAL A CB 2552 C CG1 . VAL A 331 ? 0.2580 0.2235 0.1837 0.0729 -0.0143 -0.0085 372 VAL A CG1 2553 C CG2 . VAL A 331 ? 0.2541 0.2152 0.1690 0.0773 -0.0152 -0.0070 372 VAL A CG2 2554 N N . ILE A 332 ? 0.2155 0.1895 0.1550 0.0605 -0.0041 -0.0048 373 ILE A N 2555 C CA . ILE A 332 ? 0.2105 0.1869 0.1557 0.0573 -0.0005 -0.0039 373 ILE A CA 2556 C C . ILE A 332 ? 0.2171 0.1950 0.1666 0.0563 -0.0024 -0.0063 373 ILE A C 2557 O O . ILE A 332 ? 0.2201 0.2003 0.1726 0.0544 -0.0058 -0.0092 373 ILE A O 2558 C CB . ILE A 332 ? 0.2083 0.1888 0.1590 0.0516 0.0011 -0.0040 373 ILE A CB 2559 C CG1 . ILE A 332 ? 0.2266 0.2058 0.1736 0.0525 0.0028 -0.0017 373 ILE A CG1 2560 C CG2 . ILE A 332 ? 0.2353 0.2180 0.1917 0.0484 0.0046 -0.0032 373 ILE A CG2 2561 C CD1 . ILE A 332 ? 0.2700 0.2530 0.2214 0.0475 0.0033 -0.0022 373 ILE A CD1 2562 N N . LEU A 333 ? 0.2118 0.1884 0.1618 0.0576 -0.0001 -0.0051 374 LEU A N 2563 C CA . LEU A 333 ? 0.2100 0.1884 0.1650 0.0563 -0.0013 -0.0072 374 LEU A CA 2564 C C . LEU A 333 ? 0.2175 0.1986 0.1785 0.0521 0.0026 -0.0063 374 LEU A C 2565 O O . LEU A 333 ? 0.2306 0.2099 0.1907 0.0533 0.0062 -0.0037 374 LEU A O 2566 C CB . LEU A 333 ? 0.2300 0.2043 0.1807 0.0616 -0.0020 -0.0066 374 LEU A CB 2567 C CG . LEU A 333 ? 0.2231 0.1991 0.1791 0.0606 -0.0029 -0.0085 374 LEU A CG 2568 C CD1 . LEU A 333 ? 0.2534 0.2323 0.2134 0.0587 -0.0074 -0.0124 374 LEU A CD1 2569 C CD2 . LEU A 333 ? 0.2611 0.2322 0.2113 0.0667 -0.0034 -0.0073 374 LEU A CD2 2570 N N . GLY A 334 ? 0.2043 0.1896 0.1714 0.0473 0.0020 -0.0086 375 GLY A N 2571 C CA . GLY A 334 ? 0.1983 0.1862 0.1707 0.0433 0.0054 -0.0081 375 GLY A CA 2572 C C . GLY A 334 ? 0.2271 0.2179 0.2054 0.0405 0.0047 -0.0107 375 GLY A C 2573 O O . GLY A 334 ? 0.2141 0.2066 0.1939 0.0396 0.0018 -0.0131 375 GLY A O 2574 N N . GLY A 335 ? 0.2055 0.1969 0.1874 0.0391 0.0074 -0.0102 376 GLY A N 2575 C CA . GLY A 335 ? 0.2104 0.2049 0.1981 0.0359 0.0072 -0.0127 376 GLY A CA 2576 C C . GLY A 335 ? 0.2080 0.2033 0.1993 0.0336 0.0107 -0.0118 376 GLY A C 2577 O O . GLY A 335 ? 0.2112 0.2042 0.2009 0.0352 0.0131 -0.0093 376 GLY A O 2578 N N . HIS A 336 ? 0.1916 0.1899 0.1878 0.0301 0.0112 -0.0140 377 HIS A N 2579 C CA . HIS A 336 ? 0.1843 0.1833 0.1839 0.0279 0.0140 -0.0135 377 HIS A CA 2580 C C . HIS A 336 ? 0.2020 0.1996 0.2042 0.0293 0.0155 -0.0133 377 HIS A C 2581 O O . HIS A 336 ? 0.2112 0.2077 0.2129 0.0317 0.0142 -0.0140 377 HIS A O 2582 C CB . HIS A 336 ? 0.1812 0.1836 0.1840 0.0235 0.0141 -0.0157 377 HIS A CB 2583 C CG . HIS A 336 ? 0.1797 0.1842 0.1859 0.0222 0.0134 -0.0183 377 HIS A CG 2584 N ND1 . HIS A 336 ? 0.1724 0.1779 0.1826 0.0204 0.0151 -0.0195 377 HIS A ND1 2585 C CD2 . HIS A 336 ? 0.1809 0.1869 0.1876 0.0219 0.0114 -0.0201 377 HIS A CD2 2586 C CE1 . HIS A 336 ? 0.1663 0.1737 0.1789 0.0194 0.0143 -0.0218 377 HIS A CE1 2587 N NE2 . HIS A 336 ? 0.1722 0.1800 0.1831 0.0201 0.0121 -0.0222 377 HIS A NE2 2588 N N . ARG A 337 ? 0.1765 0.1740 0.1817 0.0279 0.0182 -0.0125 378 ARG A N 2589 C CA . ARG A 337 ? 0.1956 0.1914 0.2037 0.0291 0.0201 -0.0118 378 ARG A CA 2590 C C . ARG A 337 ? 0.1936 0.1917 0.2071 0.0256 0.0211 -0.0141 378 ARG A C 2591 O O . ARG A 337 ? 0.1972 0.1947 0.2137 0.0262 0.0219 -0.0148 378 ARG A O 2592 C CB . ARG A 337 ? 0.2152 0.2084 0.2226 0.0306 0.0227 -0.0086 378 ARG A CB 2593 C CG . ARG A 337 ? 0.2231 0.2140 0.2339 0.0320 0.0252 -0.0073 378 ARG A CG 2594 C CD . ARG A 337 ? 0.2326 0.2212 0.2437 0.0331 0.0282 -0.0039 378 ARG A CD 2595 N NE . ARG A 337 ? 0.2423 0.2332 0.2578 0.0293 0.0291 -0.0047 378 ARG A NE 2596 C CZ . ARG A 337 ? 0.2291 0.2210 0.2432 0.0281 0.0288 -0.0040 378 ARG A CZ 2597 N NH1 . ARG A 337 ? 0.2160 0.2066 0.2242 0.0305 0.0280 -0.0024 378 ARG A NH1 2598 N NH2 . ARG A 337 ? 0.2225 0.2165 0.2411 0.0248 0.0292 -0.0051 378 ARG A NH2 2599 N N . ASP A 338 ? 0.1814 0.1819 0.1961 0.0222 0.0210 -0.0152 379 ASP A N 2600 C CA . ASP A 338 ? 0.1844 0.1870 0.2036 0.0191 0.0217 -0.0177 379 ASP A CA 2601 C C . ASP A 338 ? 0.1912 0.1955 0.2112 0.0186 0.0205 -0.0203 379 ASP A C 2602 O O . ASP A 338 ? 0.1847 0.1899 0.2022 0.0190 0.0187 -0.0209 379 ASP A O 2603 C CB . ASP A 338 ? 0.1846 0.1891 0.2038 0.0161 0.0215 -0.0185 379 ASP A CB 2604 C CG . ASP A 338 ? 0.1889 0.1953 0.2047 0.0152 0.0196 -0.0194 379 ASP A CG 2605 O OD1 . ASP A 338 ? 0.1799 0.1852 0.1920 0.0171 0.0185 -0.0178 379 ASP A OD1 2606 O OD2 . ASP A 338 ? 0.1788 0.1872 0.1952 0.0126 0.0192 -0.0215 379 ASP A OD2 2607 N N . SER A 339 ? 0.1983 0.2033 0.2223 0.0174 0.0214 -0.0222 380 SER A N 2608 C CA . SER A 339 ? 0.1829 0.1896 0.2084 0.0170 0.0207 -0.0246 380 SER A CA 2609 C C . SER A 339 ? 0.2008 0.2094 0.2289 0.0139 0.0216 -0.0272 380 SER A C 2610 O O . SER A 339 ? 0.2008 0.2089 0.2303 0.0127 0.0226 -0.0270 380 SER A O 2611 C CB . SER A 339 ? 0.2019 0.2068 0.2292 0.0197 0.0210 -0.0242 380 SER A CB 2612 O OG . SER A 339 ? 0.2093 0.2127 0.2397 0.0197 0.0229 -0.0238 380 SER A OG 2613 N N . TRP A 340 ? 0.1878 0.1984 0.2168 0.0128 0.0212 -0.0295 381 TRP A N 2614 C CA . TRP A 340 ? 0.1650 0.1770 0.1960 0.0105 0.0223 -0.0320 381 TRP A CA 2615 C C . TRP A 340 ? 0.1960 0.2067 0.2310 0.0112 0.0235 -0.0327 381 TRP A C 2616 O O . TRP A 340 ? 0.2094 0.2197 0.2460 0.0099 0.0243 -0.0336 381 TRP A O 2617 C CB . TRP A 340 ? 0.1882 0.2026 0.2190 0.0093 0.0222 -0.0341 381 TRP A CB 2618 C CG . TRP A 340 ? 0.1809 0.1964 0.2081 0.0077 0.0215 -0.0337 381 TRP A CG 2619 C CD1 . TRP A 340 ? 0.1962 0.2128 0.2216 0.0078 0.0204 -0.0330 381 TRP A CD1 2620 C CD2 . TRP A 340 ? 0.1840 0.1996 0.2093 0.0059 0.0217 -0.0339 381 TRP A CD2 2621 N NE1 . TRP A 340 ? 0.1871 0.2043 0.2092 0.0061 0.0201 -0.0327 381 TRP A NE1 2622 C CE2 . TRP A 340 ? 0.1794 0.1960 0.2013 0.0050 0.0209 -0.0333 381 TRP A CE2 2623 C CE3 . TRP A 340 ? 0.1916 0.2064 0.2179 0.0050 0.0223 -0.0348 381 TRP A CE3 2624 C CZ2 . TRP A 340 ? 0.1997 0.2165 0.2188 0.0034 0.0206 -0.0332 381 TRP A CZ2 2625 C CZ3 . TRP A 340 ? 0.2025 0.2175 0.2263 0.0034 0.0218 -0.0350 381 TRP A CZ3 2626 C CH2 . TRP A 340 ? 0.2052 0.2212 0.2252 0.0027 0.0210 -0.0342 381 TRP A CH2 2627 N N . VAL A 341 ? 0.2029 0.2129 0.2395 0.0133 0.0234 -0.0325 382 VAL A N 2628 C CA . VAL A 341 ? 0.2024 0.2108 0.2429 0.0144 0.0246 -0.0327 382 VAL A CA 2629 C C . VAL A 341 ? 0.2008 0.2067 0.2406 0.0177 0.0243 -0.0300 382 VAL A C 2630 O O . VAL A 341 ? 0.2069 0.2110 0.2450 0.0185 0.0246 -0.0275 382 VAL A O 2631 C CB . VAL A 341 ? 0.1995 0.2093 0.2431 0.0138 0.0252 -0.0357 382 VAL A CB 2632 C CG1 . VAL A 341 ? 0.2134 0.2214 0.2610 0.0143 0.0265 -0.0362 382 VAL A CG1 2633 C CG2 . VAL A 341 ? 0.2259 0.2378 0.2686 0.0110 0.0256 -0.0381 382 VAL A CG2 2634 N N . PHE A 342 ? 0.1910 0.1965 0.2321 0.0196 0.0237 -0.0305 383 PHE A N 2635 C CA . PHE A 342 ? 0.1928 0.1955 0.2328 0.0231 0.0234 -0.0280 383 PHE A CA 2636 C C . PHE A 342 ? 0.2030 0.2054 0.2384 0.0249 0.0214 -0.0266 383 PHE A C 2637 O O . PHE A 342 ? 0.2207 0.2203 0.2535 0.0278 0.0212 -0.0240 383 PHE A O 2638 C CB . PHE A 342 ? 0.2029 0.2050 0.2460 0.0249 0.0233 -0.0291 383 PHE A CB 2639 C CG . PHE A 342 ? 0.2328 0.2348 0.2805 0.0235 0.0252 -0.0306 383 PHE A CG 2640 C CD1 . PHE A 342 ? 0.2536 0.2529 0.3025 0.0241 0.0269 -0.0287 383 PHE A CD1 2641 C CD2 . PHE A 342 ? 0.2476 0.2521 0.2982 0.0215 0.0255 -0.0338 383 PHE A CD2 2642 C CE1 . PHE A 342 ? 0.2604 0.2595 0.3140 0.0227 0.0285 -0.0304 383 PHE A CE1 2643 C CE2 . PHE A 342 ? 0.2439 0.2480 0.2983 0.0204 0.0271 -0.0354 383 PHE A CE2 2644 C CZ . PHE A 342 ? 0.2384 0.2399 0.2944 0.0209 0.0283 -0.0337 383 PHE A CZ 2645 N N . GLY A 343 ? 0.2046 0.2097 0.2390 0.0232 0.0200 -0.0280 384 GLY A N 2646 C CA . GLY A 343 ? 0.1992 0.2041 0.2296 0.0246 0.0179 -0.0269 384 GLY A CA 2647 C C . GLY A 343 ? 0.2219 0.2251 0.2515 0.0283 0.0159 -0.0264 384 GLY A C 2648 O O . GLY A 343 ? 0.2134 0.2147 0.2388 0.0308 0.0144 -0.0247 384 GLY A O 2649 N N . GLY A 344 ? 0.2188 0.2226 0.2523 0.0289 0.0158 -0.0282 385 GLY A N 2650 C CA . GLY A 344 ? 0.2183 0.2208 0.2518 0.0324 0.0136 -0.0282 385 GLY A CA 2651 C C . GLY A 344 ? 0.2149 0.2179 0.2458 0.0335 0.0105 -0.0284 385 GLY A C 2652 O O . GLY A 344 ? 0.2238 0.2242 0.2514 0.0372 0.0085 -0.0272 385 GLY A O 2653 N N . ILE A 345 ? 0.2054 0.2116 0.2380 0.0305 0.0102 -0.0301 386 ILE A N 2654 C CA . ILE A 345 ? 0.1915 0.1982 0.2222 0.0314 0.0072 -0.0303 386 ILE A CA 2655 C C . ILE A 345 ? 0.1998 0.2062 0.2260 0.0299 0.0080 -0.0286 386 ILE A C 2656 O O . ILE A 345 ? 0.2067 0.2107 0.2281 0.0323 0.0065 -0.0268 386 ILE A O 2657 C CB . ILE A 345 ? 0.2023 0.2125 0.2382 0.0294 0.0062 -0.0330 386 ILE A CB 2658 C CG1 . ILE A 345 ? 0.2202 0.2303 0.2603 0.0318 0.0046 -0.0346 386 ILE A CG1 2659 C CG2 . ILE A 345 ? 0.2066 0.2174 0.2409 0.0295 0.0035 -0.0331 386 ILE A CG2 2660 C CD1 . ILE A 345 ? 0.2184 0.2322 0.2652 0.0299 0.0040 -0.0373 386 ILE A CD1 2661 N N . ASP A 346 ? 0.1963 0.2048 0.2238 0.0262 0.0103 -0.0291 387 ASP A N 2662 C CA . ASP A 346 ? 0.1874 0.1962 0.2114 0.0244 0.0108 -0.0279 387 ASP A CA 2663 C C . ASP A 346 ? 0.1966 0.2039 0.2191 0.0238 0.0132 -0.0262 387 ASP A C 2664 O O . ASP A 346 ? 0.2006 0.2091 0.2259 0.0215 0.0152 -0.0272 387 ASP A O 2665 C CB . ASP A 346 ? 0.1838 0.1960 0.2106 0.0208 0.0114 -0.0298 387 ASP A CB 2666 C CG . ASP A 346 ? 0.2164 0.2292 0.2400 0.0187 0.0118 -0.0289 387 ASP A CG 2667 O OD1 . ASP A 346 ? 0.1831 0.1938 0.2028 0.0201 0.0115 -0.0269 387 ASP A OD1 2668 O OD2 . ASP A 346 ? 0.2325 0.2476 0.2575 0.0158 0.0127 -0.0302 387 ASP A OD2 2669 N N . PRO A 347 ? 0.1836 0.1881 0.2020 0.0260 0.0132 -0.0236 388 PRO A N 2670 C CA . PRO A 347 ? 0.1843 0.1869 0.1982 0.0290 0.0109 -0.0222 388 PRO A CA 2671 C C . PRO A 347 ? 0.1932 0.1923 0.2050 0.0333 0.0104 -0.0208 388 PRO A C 2672 O O . PRO A 347 ? 0.1936 0.1906 0.2009 0.0363 0.0086 -0.0195 388 PRO A O 2673 C CB . PRO A 347 ? 0.1843 0.1860 0.1947 0.0282 0.0121 -0.0201 388 PRO A CB 2674 C CG . PRO A 347 ? 0.2105 0.2116 0.2233 0.0272 0.0151 -0.0192 388 PRO A CG 2675 C CD . PRO A 347 ? 0.1889 0.1923 0.2067 0.0251 0.0156 -0.0219 388 PRO A CD 2676 N N . GLN A 348 ? 0.1938 0.1922 0.2085 0.0339 0.0120 -0.0208 389 GLN A N 2677 C CA . GLN A 348 ? 0.2179 0.2122 0.2294 0.0381 0.0123 -0.0185 389 GLN A CA 2678 C C . GLN A 348 ? 0.2061 0.1987 0.2150 0.0422 0.0089 -0.0189 389 GLN A C 2679 O O . GLN A 348 ? 0.2175 0.2062 0.2213 0.0462 0.0086 -0.0167 389 GLN A O 2680 C CB . GLN A 348 ? 0.2175 0.2107 0.2325 0.0382 0.0149 -0.0180 389 GLN A CB 2681 C CG . GLN A 348 ? 0.2310 0.2255 0.2490 0.0346 0.0179 -0.0177 389 GLN A CG 2682 C CD . GLN A 348 ? 0.2396 0.2328 0.2544 0.0344 0.0193 -0.0151 389 GLN A CD 2683 O OE1 . GLN A 348 ? 0.2189 0.2097 0.2285 0.0374 0.0186 -0.0130 389 GLN A OE1 2684 N NE2 . GLN A 348 ? 0.2305 0.2253 0.2484 0.0311 0.0211 -0.0154 389 GLN A NE2 2685 N N . SER A 349 ? 0.2156 0.2107 0.2275 0.0412 0.0064 -0.0218 390 SER A N 2686 C CA . SER A 349 ? 0.2368 0.2305 0.2467 0.0449 0.0026 -0.0226 390 SER A CA 2687 C C . SER A 349 ? 0.2277 0.2198 0.2317 0.0466 0.0008 -0.0214 390 SER A C 2688 O O . SER A 349 ? 0.2481 0.2372 0.2478 0.0510 -0.0019 -0.0210 390 SER A O 2689 C CB . SER A 349 ? 0.2440 0.2412 0.2598 0.0433 0.0003 -0.0260 390 SER A CB 2690 O OG . SER A 349 ? 0.2261 0.2265 0.2437 0.0396 0.0000 -0.0272 390 SER A OG 2691 N N . GLY A 350 ? 0.2138 0.2077 0.2174 0.0434 0.0020 -0.0209 391 GLY A N 2692 C CA . GLY A 350 ? 0.2069 0.1991 0.2046 0.0450 0.0008 -0.0194 391 GLY A CA 2693 C C . GLY A 350 ? 0.2065 0.1949 0.1989 0.0475 0.0034 -0.0160 391 GLY A C 2694 O O . GLY A 350 ? 0.2228 0.2079 0.2090 0.0516 0.0020 -0.0145 391 GLY A O 2695 N N . ALA A 351 ? 0.2053 0.1942 0.2002 0.0452 0.0072 -0.0147 392 ALA A N 2696 C CA . ALA A 351 ? 0.2314 0.2170 0.2226 0.0473 0.0102 -0.0111 392 ALA A CA 2697 C C . ALA A 351 ? 0.2354 0.2165 0.2226 0.0526 0.0100 -0.0094 392 ALA A C 2698 O O . ALA A 351 ? 0.2434 0.2209 0.2250 0.0559 0.0112 -0.0066 392 ALA A O 2699 C CB . ALA A 351 ? 0.2313 0.2182 0.2272 0.0438 0.0140 -0.0104 392 ALA A CB 2700 N N . ALA A 352 ? 0.2363 0.2175 0.2262 0.0536 0.0086 -0.0111 393 ALA A N 2701 C CA . ALA A 352 ? 0.2495 0.2263 0.2353 0.0590 0.0081 -0.0096 393 ALA A CA 2702 C C . ALA A 352 ? 0.2552 0.2293 0.2339 0.0634 0.0044 -0.0097 393 ALA A C 2703 O O . ALA A 352 ? 0.2680 0.2374 0.2402 0.0684 0.0047 -0.0072 393 ALA A O 2704 C CB . ALA A 352 ? 0.2490 0.2270 0.2398 0.0588 0.0070 -0.0119 393 ALA A CB 2705 N N . VAL A 353 ? 0.2541 0.2312 0.2342 0.0616 0.0010 -0.0125 394 VAL A N 2706 C CA . VAL A 353 ? 0.2571 0.2320 0.2313 0.0654 -0.0031 -0.0131 394 VAL A CA 2707 C C . VAL A 353 ? 0.2615 0.2339 0.2291 0.0668 -0.0013 -0.0101 394 VAL A C 2708 O O . VAL A 353 ? 0.2577 0.2256 0.2174 0.0721 -0.0026 -0.0087 394 VAL A O 2709 C CB . VAL A 353 ? 0.2488 0.2278 0.2278 0.0624 -0.0069 -0.0169 394 VAL A CB 2710 C CG1 . VAL A 353 ? 0.2475 0.2252 0.2212 0.0646 -0.0104 -0.0174 394 VAL A CG1 2711 C CG2 . VAL A 353 ? 0.2327 0.2125 0.2162 0.0636 -0.0098 -0.0196 394 VAL A CG2 2712 N N . VAL A 354 ? 0.2515 0.2265 0.2218 0.0624 0.0017 -0.0093 395 VAL A N 2713 C CA . VAL A 354 ? 0.2546 0.2274 0.2193 0.0636 0.0037 -0.0065 395 VAL A CA 2714 C C . VAL A 354 ? 0.2581 0.2262 0.2184 0.0678 0.0070 -0.0028 395 VAL A C 2715 O O . VAL A 354 ? 0.2714 0.2357 0.2242 0.0721 0.0071 -0.0007 395 VAL A O 2716 C CB . VAL A 354 ? 0.2593 0.2357 0.2285 0.0583 0.0066 -0.0061 395 VAL A CB 2717 C CG1 . VAL A 354 ? 0.2493 0.2232 0.2134 0.0598 0.0091 -0.0028 395 VAL A CG1 2718 C CG2 . VAL A 354 ? 0.2775 0.2583 0.2506 0.0543 0.0035 -0.0094 395 VAL A CG2 2719 N N . HIS A 355 ? 0.2586 0.2268 0.2233 0.0668 0.0098 -0.0020 396 HIS A N 2720 C CA . HIS A 355 ? 0.2599 0.2236 0.2214 0.0704 0.0137 0.0018 396 HIS A CA 2721 C C . HIS A 355 ? 0.2883 0.2470 0.2415 0.0771 0.0114 0.0026 396 HIS A C 2722 O O . HIS A 355 ? 0.2999 0.2540 0.2460 0.0814 0.0135 0.0060 396 HIS A O 2723 C CB . HIS A 355 ? 0.2772 0.2423 0.2460 0.0679 0.0162 0.0016 396 HIS A CB 2724 C CG . HIS A 355 ? 0.2763 0.2392 0.2464 0.0680 0.0216 0.0054 396 HIS A CG 2725 N ND1 . HIS A 355 ? 0.2997 0.2633 0.2706 0.0659 0.0246 0.0073 396 HIS A ND1 2726 C CD2 . HIS A 355 ? 0.3162 0.2764 0.2878 0.0698 0.0245 0.0074 396 HIS A CD2 2727 C CE1 . HIS A 355 ? 0.3129 0.2743 0.2862 0.0664 0.0292 0.0104 396 HIS A CE1 2728 N NE2 . HIS A 355 ? 0.3105 0.2699 0.2844 0.0686 0.0293 0.0106 396 HIS A NE2 2729 N N . GLU A 356 ? 0.2819 0.2412 0.2356 0.0783 0.0069 -0.0005 397 GLU A N 2730 C CA . GLU A 356 ? 0.2928 0.2472 0.2384 0.0850 0.0038 -0.0002 397 GLU A CA 2731 C C . GLU A 356 ? 0.3005 0.2528 0.2383 0.0880 0.0013 -0.0002 397 GLU A C 2732 O O . GLU A 356 ? 0.3180 0.2648 0.2467 0.0942 0.0008 0.0018 397 GLU A O 2733 C CB . GLU A 356 ? 0.3095 0.2656 0.2591 0.0851 -0.0006 -0.0039 397 GLU A CB 2734 C CG . GLU A 356 ? 0.3147 0.2659 0.2566 0.0921 -0.0047 -0.0043 397 GLU A CG 2735 C CD . GLU A 356 ? 0.3647 0.3100 0.3004 0.0973 -0.0015 -0.0004 397 GLU A CD 2736 O OE1 . GLU A 356 ? 0.3347 0.2794 0.2720 0.0957 0.0042 0.0029 397 GLU A OE1 2737 O OE2 . GLU A 356 ? 0.3712 0.3123 0.3004 0.1033 -0.0049 -0.0008 397 GLU A OE2 2738 N N . ILE A 357 ? 0.2772 0.2335 0.2181 0.0839 -0.0004 -0.0023 398 ILE A N 2739 C CA . ILE A 357 ? 0.2850 0.2394 0.2190 0.0864 -0.0025 -0.0022 398 ILE A CA 2740 C C . ILE A 357 ? 0.2898 0.2407 0.2177 0.0887 0.0022 0.0022 398 ILE A C 2741 O O . ILE A 357 ? 0.3279 0.2739 0.2464 0.0944 0.0013 0.0037 398 ILE A O 2742 C CB . ILE A 357 ? 0.2596 0.2193 0.1992 0.0810 -0.0049 -0.0052 398 ILE A CB 2743 C CG1 . ILE A 357 ? 0.2476 0.2095 0.1911 0.0807 -0.0105 -0.0096 398 ILE A CG1 2744 C CG2 . ILE A 357 ? 0.2775 0.2356 0.2107 0.0827 -0.0060 -0.0046 398 ILE A CG2 2745 C CD1 . ILE A 357 ? 0.2571 0.2253 0.2093 0.0740 -0.0116 -0.0125 398 ILE A CD1 2746 N N . VAL A 358 ? 0.2895 0.2426 0.2228 0.0846 0.0072 0.0043 399 VAL A N 2747 C CA . VAL A 358 ? 0.2978 0.2478 0.2272 0.0864 0.0124 0.0087 399 VAL A CA 2748 C C . VAL A 358 ? 0.3095 0.2533 0.2317 0.0930 0.0141 0.0117 399 VAL A C 2749 O O . VAL A 358 ? 0.3213 0.2605 0.2350 0.0978 0.0156 0.0145 399 VAL A O 2750 C CB . VAL A 358 ? 0.2851 0.2383 0.2228 0.0811 0.0173 0.0103 399 VAL A CB 2751 C CG1 . VAL A 358 ? 0.3011 0.2509 0.2354 0.0834 0.0227 0.0150 399 VAL A CG1 2752 C CG2 . VAL A 358 ? 0.2862 0.2455 0.2304 0.0746 0.0156 0.0074 399 VAL A CG2 2753 N N . ARG A 359 ? 0.3125 0.2560 0.2378 0.0934 0.0140 0.0112 400 ARG A N 2754 C CA . ARG A 359 ? 0.3332 0.2706 0.2518 0.0997 0.0157 0.0142 400 ARG A CA 2755 C C . ARG A 359 ? 0.3475 0.2801 0.2549 0.1064 0.0115 0.0136 400 ARG A C 2756 O O . ARG A 359 ? 0.3687 0.2955 0.2672 0.1122 0.0142 0.0173 400 ARG A O 2757 C CB . ARG A 359 ? 0.3317 0.2697 0.2557 0.0990 0.0155 0.0132 400 ARG A CB 2758 C CG . ARG A 359 ? 0.3351 0.2666 0.2531 0.1050 0.0190 0.0173 400 ARG A CG 2759 C CD . ARG A 359 ? 0.3571 0.2887 0.2790 0.1053 0.0169 0.0155 400 ARG A CD 2760 N NE . ARG A 359 ? 0.3691 0.3013 0.2882 0.1074 0.0099 0.0113 400 ARG A NE 2761 C CZ . ARG A 359 ? 0.3915 0.3184 0.3002 0.1143 0.0066 0.0115 400 ARG A CZ 2762 N NH1 . ARG A 359 ? 0.3852 0.3131 0.2930 0.1157 -0.0001 0.0073 400 ARG A NH1 2763 N NH2 . ARG A 359 ? 0.4145 0.3351 0.3138 0.1201 0.0100 0.0159 400 ARG A NH2 2764 N N . SER A 360 ? 0.3488 0.2838 0.2567 0.1059 0.0051 0.0091 401 SER A N 2765 C CA A SER A 360 ? 0.3575 0.2880 0.2552 0.1123 0.0002 0.0079 401 SER A CA 2766 C CA B SER A 360 ? 0.3742 0.3048 0.2721 0.1122 0.0003 0.0079 401 SER A CA 2767 C C . SER A 360 ? 0.3757 0.3039 0.2661 0.1145 0.0014 0.0097 401 SER A C 2768 O O . SER A 360 ? 0.3854 0.3074 0.2648 0.1214 0.0015 0.0118 401 SER A O 2769 C CB A SER A 360 ? 0.3549 0.2884 0.2559 0.1112 -0.0071 0.0025 401 SER A CB 2770 C CB B SER A 360 ? 0.3724 0.3064 0.2745 0.1106 -0.0067 0.0026 401 SER A CB 2771 O OG A SER A 360 ? 0.3038 0.2329 0.1950 0.1176 -0.0121 0.0012 401 SER A OG 2772 O OG B SER A 360 ? 0.4183 0.3546 0.3278 0.1082 -0.0068 0.0012 401 SER A OG 2773 N N . PHE A 361 ? 0.3527 0.2856 0.2487 0.1089 0.0022 0.0089 402 PHE A N 2774 C CA . PHE A 361 ? 0.3697 0.3003 0.2589 0.1110 0.0038 0.0109 402 PHE A CA 2775 C C . PHE A 361 ? 0.3968 0.3226 0.2805 0.1147 0.0104 0.0164 402 PHE A C 2776 O O . PHE A 361 ? 0.4057 0.3265 0.2793 0.1203 0.0110 0.0183 402 PHE A O 2777 C CB . PHE A 361 ? 0.3602 0.2967 0.2568 0.1042 0.0044 0.0096 402 PHE A CB 2778 C CG . PHE A 361 ? 0.3312 0.2707 0.2294 0.1023 -0.0019 0.0050 402 PHE A CG 2779 C CD1 . PHE A 361 ? 0.3103 0.2464 0.2000 0.1070 -0.0060 0.0037 402 PHE A CD1 2780 C CD2 . PHE A 361 ? 0.3338 0.2796 0.2426 0.0955 -0.0035 0.0019 402 PHE A CD2 2781 C CE1 . PHE A 361 ? 0.3263 0.2653 0.2186 0.1050 -0.0118 -0.0006 402 PHE A CE1 2782 C CE2 . PHE A 361 ? 0.3362 0.2849 0.2474 0.0935 -0.0089 -0.0021 402 PHE A CE2 2783 C CZ . PHE A 361 ? 0.3260 0.2714 0.2294 0.0981 -0.0131 -0.0034 402 PHE A CZ 2784 N N . GLY A 362 ? 0.3920 0.3191 0.2824 0.1119 0.0155 0.0188 403 GLY A N 2785 C CA . GLY A 362 ? 0.4004 0.3233 0.2875 0.1148 0.0224 0.0243 403 GLY A CA 2786 C C . GLY A 362 ? 0.4106 0.3262 0.2870 0.1230 0.0225 0.0265 403 GLY A C 2787 O O . GLY A 362 ? 0.4351 0.3454 0.3036 0.1280 0.0268 0.0307 403 GLY A O 2788 N N . THR A 363 ? 0.4244 0.3393 0.2997 0.1249 0.0176 0.0236 404 THR A N 2789 C CA . THR A 363 ? 0.4413 0.3490 0.3053 0.1332 0.0166 0.0252 404 THR A CA 2790 C C . THR A 363 ? 0.4647 0.3677 0.3162 0.1393 0.0143 0.0253 404 THR A C 2791 O O . THR A 363 ? 0.4933 0.3895 0.3341 0.1462 0.0175 0.0293 404 THR A O 2792 C CB . THR A 363 ? 0.4440 0.3519 0.3092 0.1344 0.0109 0.0216 404 THR A CB 2793 O OG1 A THR A 363 ? 0.4359 0.3475 0.3120 0.1293 0.0136 0.0218 404 THR A OG1 2794 O OG1 B THR A 363 ? 0.4519 0.3617 0.3157 0.1345 0.0033 0.0165 404 THR A OG1 2795 C CG2 A THR A 363 ? 0.4426 0.3425 0.2951 0.1435 0.0096 0.0232 404 THR A CG2 2796 C CG2 B THR A 363 ? 0.4310 0.3441 0.3091 0.1279 0.0126 0.0207 404 THR A CG2 2797 N N . LEU A 364 ? 0.4479 0.3542 0.3003 0.1371 0.0089 0.0211 405 LEU A N 2798 C CA . LEU A 364 ? 0.4560 0.3582 0.2971 0.1425 0.0062 0.0207 405 LEU A CA 2799 C C . LEU A 364 ? 0.4650 0.3652 0.3027 0.1434 0.0130 0.0254 405 LEU A C 2800 O O . LEU A 364 ? 0.4560 0.3498 0.2817 0.1503 0.0144 0.0280 405 LEU A O 2801 C CB . LEU A 364 ? 0.4642 0.3711 0.3092 0.1389 -0.0007 0.0153 405 LEU A CB 2802 C CG A LEU A 364 ? 0.4572 0.3638 0.3009 0.1413 -0.0090 0.0102 405 LEU A CG 2803 C CG B LEU A 364 ? 0.4562 0.3651 0.3047 0.1385 -0.0082 0.0101 405 LEU A CG 2804 C CD1 A LEU A 364 ? 0.4526 0.3628 0.3060 0.1376 -0.0101 0.0085 405 LEU A CD1 2805 C CD1 B LEU A 364 ? 0.4574 0.3715 0.3116 0.1339 -0.0135 0.0054 405 LEU A CD1 2806 C CD2 A LEU A 364 ? 0.4578 0.3678 0.3038 0.1388 -0.0150 0.0056 405 LEU A CD2 2807 C CD2 B LEU A 364 ? 0.4935 0.3954 0.3300 0.1473 -0.0123 0.0096 405 LEU A CD2 2808 N N . LYS A 365 ? 0.4349 0.3406 0.2831 0.1363 0.0171 0.0264 406 LYS A N 2809 C CA . LYS A 365 ? 0.4602 0.3647 0.3073 0.1362 0.0236 0.0307 406 LYS A CA 2810 C C . LYS A 365 ? 0.4792 0.3772 0.3196 0.1421 0.0303 0.0365 406 LYS A C 2811 O O . LYS A 365 ? 0.4719 0.3654 0.3041 0.1467 0.0340 0.0399 406 LYS A O 2812 C CB . LYS A 365 ? 0.4550 0.3668 0.3160 0.1274 0.0266 0.0306 406 LYS A CB 2813 C CG . LYS A 365 ? 0.5123 0.4244 0.3741 0.1262 0.0320 0.0339 406 LYS A CG 2814 C CD . LYS A 365 ? 0.5800 0.4913 0.4469 0.1253 0.0398 0.0388 406 LYS A CD 2815 C CE . LYS A 365 ? 0.6059 0.5193 0.4772 0.1223 0.0447 0.0413 406 LYS A CE 2816 N NZ . LYS A 365 ? 0.6610 0.5755 0.5416 0.1193 0.0513 0.0449 406 LYS A NZ 2817 N N . LYS A 366 ? 0.4734 0.3708 0.3175 0.1420 0.0318 0.0376 407 LYS A N 2818 C CA . LYS A 366 ? 0.4999 0.3909 0.3383 0.1474 0.0384 0.0433 407 LYS A CA 2819 C C . LYS A 366 ? 0.5335 0.4164 0.3555 0.1572 0.0366 0.0444 407 LYS A C 2820 O O . LYS A 366 ? 0.5508 0.4276 0.3653 0.1627 0.0427 0.0497 407 LYS A O 2821 C CB . LYS A 366 ? 0.4897 0.3818 0.3358 0.1452 0.0401 0.0440 407 LYS A CB 2822 C CG . LYS A 366 ? 0.5104 0.4088 0.3714 0.1368 0.0442 0.0446 407 LYS A CG 2823 C CD . LYS A 366 ? 0.5300 0.4296 0.3989 0.1343 0.0455 0.0448 407 LYS A CD 2824 C CE . LYS A 366 ? 0.5526 0.4581 0.4357 0.1264 0.0495 0.0453 407 LYS A CE 2825 N NZ . LYS A 366 ? 0.5980 0.5048 0.4889 0.1240 0.0502 0.0450 407 LYS A NZ 2826 N N . GLU A 367 ? 0.5322 0.4149 0.3488 0.1594 0.0284 0.0395 408 GLU A N 2827 C CA . GLU A 367 ? 0.5695 0.4444 0.3699 0.1688 0.0253 0.0396 408 GLU A CA 2828 C C . GLU A 367 ? 0.5675 0.4408 0.3604 0.1712 0.0250 0.0396 408 GLU A C 2829 O O . GLU A 367 ? 0.5958 0.4628 0.3748 0.1791 0.0222 0.0393 408 GLU A O 2830 C CB . GLU A 367 ? 0.5757 0.4508 0.3742 0.1705 0.0163 0.0342 408 GLU A CB 2831 C CG . GLU A 367 ? 0.6527 0.5285 0.4574 0.1691 0.0168 0.0345 408 GLU A CG 2832 C CD . GLU A 367 ? 0.7495 0.6269 0.5554 0.1694 0.0080 0.0288 408 GLU A CD 2833 O OE1 . GLU A 367 ? 0.8184 0.6960 0.6286 0.1689 0.0079 0.0289 408 GLU A OE1 2834 O OE2 . GLU A 367 ? 0.7906 0.6690 0.5937 0.1701 0.0011 0.0243 408 GLU A OE2 2835 N N . GLY A 368 ? 0.5351 0.4139 0.3368 0.1648 0.0278 0.0398 409 GLY A N 2836 C CA . GLY A 368 ? 0.5313 0.4087 0.3268 0.1668 0.0288 0.0405 409 GLY A CA 2837 C C . GLY A 368 ? 0.5145 0.3967 0.3133 0.1628 0.0219 0.0350 409 GLY A C 2838 O O . GLY A 368 ? 0.5240 0.4050 0.3172 0.1648 0.0217 0.0350 409 GLY A O 2839 N N . TRP A 369 ? 0.5000 0.3879 0.3081 0.1574 0.0163 0.0304 410 TRP A N 2840 C CA . TRP A 369 ? 0.4765 0.3690 0.2885 0.1535 0.0097 0.0251 410 TRP A CA 2841 C C . TRP A 369 ? 0.4483 0.3480 0.2728 0.1448 0.0130 0.0254 410 TRP A C 2842 O O . TRP A 369 ? 0.4446 0.3471 0.2777 0.1404 0.0185 0.0281 410 TRP A O 2843 C CB . TRP A 369 ? 0.4758 0.3709 0.2925 0.1518 0.0025 0.0201 410 TRP A CB 2844 C CG . TRP A 369 ? 0.4826 0.3833 0.3060 0.1468 -0.0042 0.0146 410 TRP A CG 2845 C CD1 . TRP A 369 ? 0.4866 0.3855 0.3038 0.1501 -0.0109 0.0107 410 TRP A CD1 2846 C CD2 . TRP A 369 ? 0.4608 0.3695 0.2984 0.1378 -0.0045 0.0124 410 TRP A CD2 2847 N NE1 . TRP A 369 ? 0.4767 0.3822 0.3042 0.1434 -0.0153 0.0064 410 TRP A NE1 2848 C CE2 . TRP A 369 ? 0.4525 0.3640 0.2921 0.1359 -0.0114 0.0074 410 TRP A CE2 2849 C CE3 . TRP A 369 ? 0.4507 0.3643 0.2994 0.1312 0.0003 0.0141 410 TRP A CE3 2850 C CZ2 . TRP A 369 ? 0.4125 0.3314 0.2647 0.1278 -0.0131 0.0045 410 TRP A CZ2 2851 C CZ3 . TRP A 369 ? 0.4111 0.3320 0.2717 0.1233 -0.0018 0.0109 410 TRP A CZ3 2852 C CH2 . TRP A 369 ? 0.4252 0.3485 0.2870 0.1218 -0.0083 0.0063 410 TRP A CH2 2853 N N . ARG A 370 ? 0.4315 0.3338 0.2567 0.1427 0.0096 0.0226 411 ARG A N 2854 C CA . ARG A 370 ? 0.4064 0.3161 0.2440 0.1340 0.0106 0.0215 411 ARG A CA 2855 C C . ARG A 370 ? 0.3786 0.2915 0.2181 0.1317 0.0031 0.0160 411 ARG A C 2856 O O . ARG A 370 ? 0.3886 0.2977 0.2193 0.1368 -0.0015 0.0140 411 ARG A O 2857 C CB . ARG A 370 ? 0.4251 0.3345 0.2617 0.1336 0.0163 0.0250 411 ARG A CB 2858 C CG . ARG A 370 ? 0.4334 0.3416 0.2725 0.1336 0.0248 0.0306 411 ARG A CG 2859 C CD . ARG A 370 ? 0.4253 0.3346 0.2661 0.1319 0.0300 0.0335 411 ARG A CD 2860 N NE . ARG A 370 ? 0.4247 0.3333 0.2701 0.1313 0.0377 0.0384 411 ARG A NE 2861 C CZ . ARG A 370 ? 0.4517 0.3655 0.3095 0.1247 0.0397 0.0385 411 ARG A CZ 2862 N NH1 . ARG A 370 ? 0.4009 0.3211 0.2677 0.1179 0.0352 0.0342 411 ARG A NH1 2863 N NH2 . ARG A 370 ? 0.4533 0.3657 0.3148 0.1249 0.0465 0.0429 411 ARG A NH2 2864 N N . PRO A 371 ? 0.3482 0.2681 0.1998 0.1238 0.0018 0.0136 412 PRO A N 2865 C CA . PRO A 371 ? 0.3433 0.2663 0.1976 0.1212 -0.0048 0.0088 412 PRO A CA 2866 C C . PRO A 371 ? 0.3356 0.2581 0.1863 0.1216 -0.0045 0.0091 412 PRO A C 2867 O O . PRO A 371 ? 0.3545 0.2762 0.2039 0.1218 0.0013 0.0130 412 PRO A O 2868 C CB . PRO A 371 ? 0.3306 0.2610 0.1987 0.1125 -0.0044 0.0072 412 PRO A CB 2869 C CG . PRO A 371 ? 0.3224 0.2538 0.1942 0.1101 0.0034 0.0118 412 PRO A CG 2870 C CD . PRO A 371 ? 0.3366 0.2614 0.1993 0.1172 0.0067 0.0154 412 PRO A CD 2871 N N . ARG A 372 ? 0.3313 0.2547 0.1814 0.1215 -0.0106 0.0051 413 ARG A N 2872 C CA . ARG A 372 ? 0.3330 0.2557 0.1795 0.1220 -0.0109 0.0051 413 ARG A CA 2873 C C . ARG A 372 ? 0.3353 0.2636 0.1911 0.1148 -0.0064 0.0068 413 ARG A C 2874 O O . ARG A 372 ? 0.3442 0.2714 0.1974 0.1156 -0.0019 0.0099 413 ARG A O 2875 C CB . ARG A 372 ? 0.3270 0.2505 0.1736 0.1220 -0.0187 -0.0001 413 ARG A CB 2876 C CG . ARG A 372 ? 0.3594 0.2823 0.2028 0.1224 -0.0194 -0.0004 413 ARG A CG 2877 C CD . ARG A 372 ? 0.3788 0.3027 0.2238 0.1217 -0.0270 -0.0055 413 ARG A CD 2878 N NE . ARG A 372 ? 0.3857 0.3098 0.2292 0.1211 -0.0272 -0.0057 413 ARG A NE 2879 C CZ . ARG A 372 ? 0.4351 0.3537 0.2677 0.1275 -0.0283 -0.0055 413 ARG A CZ 2880 N NH1 . ARG A 372 ? 0.4434 0.3556 0.2650 0.1353 -0.0291 -0.0049 413 ARG A NH1 2881 N NH2 . ARG A 372 ? 0.4369 0.3562 0.2694 0.1263 -0.0285 -0.0058 413 ARG A NH2 2882 N N . ARG A 373 ? 0.3157 0.2499 0.1824 0.1082 -0.0079 0.0045 414 ARG A N 2883 C CA . ARG A 373 ? 0.3067 0.2465 0.1828 0.1010 -0.0044 0.0056 414 ARG A CA 2884 C C . ARG A 373 ? 0.3105 0.2523 0.1928 0.0981 0.0006 0.0081 414 ARG A C 2885 O O . ARG A 373 ? 0.3176 0.2576 0.1989 0.1002 0.0006 0.0083 414 ARG A O 2886 C CB . ARG A 373 ? 0.3070 0.2518 0.1909 0.0955 -0.0093 0.0014 414 ARG A CB 2887 C CG . ARG A 373 ? 0.3080 0.2511 0.1874 0.0979 -0.0150 -0.0017 414 ARG A CG 2888 C CD . ARG A 373 ? 0.2935 0.2415 0.1814 0.0923 -0.0195 -0.0056 414 ARG A CD 2889 N NE . ARG A 373 ? 0.3069 0.2522 0.1893 0.0957 -0.0243 -0.0080 414 ARG A NE 2890 C CZ . ARG A 373 ? 0.3406 0.2825 0.2184 0.1004 -0.0298 -0.0109 414 ARG A CZ 2891 N NH1 . ARG A 373 ? 0.3180 0.2596 0.1970 0.1016 -0.0315 -0.0121 414 ARG A NH1 2892 N NH2 . ARG A 373 ? 0.3376 0.2766 0.2099 0.1038 -0.0340 -0.0129 414 ARG A NH2 2893 N N . THR A 374 ? 0.2887 0.2342 0.1778 0.0930 0.0046 0.0099 415 THR A N 2894 C CA . THR A 374 ? 0.2828 0.2305 0.1787 0.0898 0.0092 0.0120 415 THR A CA 2895 C C . THR A 374 ? 0.2874 0.2393 0.1910 0.0852 0.0061 0.0087 415 THR A C 2896 O O . THR A 374 ? 0.2800 0.2355 0.1876 0.0815 0.0024 0.0056 415 THR A O 2897 C CB . THR A 374 ? 0.2803 0.2311 0.1818 0.0856 0.0136 0.0142 415 THR A CB 2898 O OG1 . THR A 374 ? 0.2861 0.2328 0.1814 0.0902 0.0178 0.0180 415 THR A OG1 2899 C CG2 . THR A 374 ? 0.2802 0.2345 0.1910 0.0809 0.0171 0.0153 415 THR A CG2 2900 N N . ILE A 375 ? 0.2649 0.2164 0.1707 0.0855 0.0081 0.0097 416 ILE A N 2901 C CA . ILE A 375 ? 0.2572 0.2129 0.1712 0.0807 0.0064 0.0071 416 ILE A CA 2902 C C . ILE A 375 ? 0.2579 0.2167 0.1796 0.0763 0.0113 0.0090 416 ILE A C 2903 O O . ILE A 375 ? 0.2704 0.2266 0.1910 0.0784 0.0159 0.0126 416 ILE A O 2904 C CB . ILE A 375 ? 0.2556 0.2088 0.1672 0.0843 0.0040 0.0059 416 ILE A CB 2905 C CG1 . ILE A 375 ? 0.2896 0.2393 0.1931 0.0895 -0.0013 0.0038 416 ILE A CG1 2906 C CG2 . ILE A 375 ? 0.2755 0.2334 0.1961 0.0792 0.0024 0.0032 416 ILE A CG2 2907 C CD1 . ILE A 375 ? 0.3020 0.2480 0.2012 0.0945 -0.0036 0.0031 416 ILE A CD1 2908 N N . LEU A 376 ? 0.2356 0.1996 0.1653 0.0701 0.0102 0.0068 417 LEU A N 2909 C CA . LEU A 376 ? 0.2430 0.2101 0.1806 0.0655 0.0140 0.0079 417 LEU A CA 2910 C C . LEU A 376 ? 0.2458 0.2152 0.1885 0.0632 0.0123 0.0054 417 LEU A C 2911 O O . LEU A 376 ? 0.2456 0.2167 0.1889 0.0621 0.0080 0.0021 417 LEU A O 2912 C CB . LEU A 376 ? 0.2304 0.2017 0.1729 0.0604 0.0142 0.0071 417 LEU A CB 2913 C CG . LEU A 376 ? 0.2733 0.2426 0.2110 0.0625 0.0154 0.0093 417 LEU A CG 2914 C CD1 . LEU A 376 ? 0.2373 0.2109 0.1802 0.0573 0.0153 0.0084 417 LEU A CD1 2915 C CD2 . LEU A 376 ? 0.2977 0.2639 0.2336 0.0656 0.0206 0.0134 417 LEU A CD2 2916 N N . PHE A 377 ? 0.2380 0.2072 0.1843 0.0626 0.0157 0.0069 418 PHE A N 2917 C CA . PHE A 377 ? 0.2277 0.1990 0.1794 0.0603 0.0147 0.0048 418 PHE A CA 2918 C C . PHE A 377 ? 0.2336 0.2088 0.1934 0.0549 0.0174 0.0047 418 PHE A C 2919 O O . PHE A 377 ? 0.2224 0.1969 0.1838 0.0546 0.0212 0.0074 418 PHE A O 2920 C CB . PHE A 377 ? 0.2409 0.2082 0.1899 0.0647 0.0165 0.0067 418 PHE A CB 2921 C CG . PHE A 377 ? 0.2578 0.2207 0.1980 0.0708 0.0138 0.0068 418 PHE A CG 2922 C CD1 . PHE A 377 ? 0.2551 0.2184 0.1947 0.0717 0.0089 0.0035 418 PHE A CD1 2923 C CD2 . PHE A 377 ? 0.2920 0.2502 0.2245 0.0758 0.0159 0.0101 418 PHE A CD2 2924 C CE1 . PHE A 377 ? 0.2881 0.2471 0.2193 0.0777 0.0057 0.0032 418 PHE A CE1 2925 C CE2 . PHE A 377 ? 0.2861 0.2398 0.2095 0.0819 0.0130 0.0099 418 PHE A CE2 2926 C CZ . PHE A 377 ? 0.2960 0.2501 0.2190 0.0828 0.0077 0.0063 418 PHE A CZ 2927 N N . ALA A 378 ? 0.2196 0.1987 0.1847 0.0508 0.0153 0.0016 419 ALA A N 2928 C CA . ALA A 378 ? 0.2107 0.1932 0.1828 0.0458 0.0174 0.0012 419 ALA A CA 2929 C C . ALA A 378 ? 0.2093 0.1937 0.1865 0.0437 0.0171 -0.0009 419 ALA A C 2930 O O . ALA A 378 ? 0.2064 0.1916 0.1835 0.0439 0.0141 -0.0033 419 ALA A O 2931 C CB . ALA A 378 ? 0.1942 0.1801 0.1676 0.0421 0.0156 -0.0005 419 ALA A CB 2932 N N . SER A 379 ? 0.2051 0.1901 0.1873 0.0418 0.0202 0.0000 420 SER A N 2933 C CA . SER A 379 ? 0.1913 0.1784 0.1793 0.0390 0.0205 -0.0020 420 SER A CA 2934 C C . SER A 379 ? 0.1962 0.1869 0.1890 0.0341 0.0210 -0.0033 420 SER A C 2935 O O . SER A 379 ? 0.2078 0.1984 0.2036 0.0331 0.0236 -0.0018 420 SER A O 2936 C CB . SER A 379 ? 0.2079 0.1923 0.1980 0.0410 0.0239 0.0003 420 SER A CB 2937 O OG . SER A 379 ? 0.1909 0.1775 0.1872 0.0381 0.0243 -0.0018 420 SER A OG 2938 N N . TRP A 380 ? 0.1866 0.1803 0.1800 0.0315 0.0184 -0.0061 421 TRP A N 2939 C CA . TRP A 380 ? 0.1683 0.1649 0.1645 0.0274 0.0186 -0.0072 421 TRP A CA 2940 C C . TRP A 380 ? 0.1912 0.1895 0.1931 0.0246 0.0198 -0.0088 421 TRP A C 2941 O O . TRP A 380 ? 0.1968 0.1952 0.2005 0.0251 0.0196 -0.0101 421 TRP A O 2942 C CB . TRP A 380 ? 0.1822 0.1811 0.1769 0.0256 0.0157 -0.0094 421 TRP A CB 2943 C CG . TRP A 380 ? 0.1721 0.1697 0.1617 0.0280 0.0138 -0.0086 421 TRP A CG 2944 C CD1 . TRP A 380 ? 0.1836 0.1813 0.1713 0.0291 0.0110 -0.0102 421 TRP A CD1 2945 C CD2 . TRP A 380 ? 0.1659 0.1620 0.1520 0.0294 0.0142 -0.0064 421 TRP A CD2 2946 N NE1 . TRP A 380 ? 0.1895 0.1858 0.1726 0.0311 0.0095 -0.0092 421 TRP A NE1 2947 C CE2 . TRP A 380 ? 0.1801 0.1753 0.1618 0.0314 0.0115 -0.0068 421 TRP A CE2 2948 C CE3 . TRP A 380 ? 0.1861 0.1816 0.1729 0.0290 0.0166 -0.0043 421 TRP A CE3 2949 C CZ2 . TRP A 380 ? 0.1856 0.1791 0.1628 0.0334 0.0112 -0.0051 421 TRP A CZ2 2950 C CZ3 . TRP A 380 ? 0.2014 0.1954 0.1841 0.0310 0.0166 -0.0023 421 TRP A CZ3 2951 C CH2 . TRP A 380 ? 0.1958 0.1887 0.1734 0.0332 0.0139 -0.0028 421 TRP A CH2 2952 N N . ASP A 381 ? 0.1790 0.1789 0.1837 0.0218 0.0207 -0.0091 422 ASP A N 2953 C CA . ASP A 381 ? 0.1613 0.1629 0.1712 0.0190 0.0214 -0.0111 422 ASP A CA 2954 C C . ASP A 381 ? 0.1680 0.1724 0.1776 0.0158 0.0197 -0.0137 422 ASP A C 2955 O O . ASP A 381 ? 0.1862 0.1915 0.1926 0.0153 0.0183 -0.0135 422 ASP A O 2956 C CB . ASP A 381 ? 0.1707 0.1716 0.1845 0.0183 0.0236 -0.0097 422 ASP A CB 2957 C CG . ASP A 381 ? 0.1811 0.1824 0.2006 0.0168 0.0247 -0.0112 422 ASP A CG 2958 O OD1 . ASP A 381 ? 0.1917 0.1942 0.2120 0.0158 0.0239 -0.0137 422 ASP A OD1 2959 O OD2 . ASP A 381 ? 0.1896 0.1899 0.2133 0.0167 0.0266 -0.0099 422 ASP A OD2 2960 N N . ALA A 382 ? 0.1633 0.1692 0.1763 0.0138 0.0199 -0.0160 423 ALA A N 2961 C CA . ALA A 382 ? 0.1630 0.1713 0.1759 0.0108 0.0188 -0.0184 423 ALA A CA 2962 C C . ALA A 382 ? 0.1620 0.1715 0.1714 0.0106 0.0172 -0.0191 423 ALA A C 2963 O O . ALA A 382 ? 0.1650 0.1761 0.1729 0.0086 0.0163 -0.0201 423 ALA A O 2964 C CB . ALA A 382 ? 0.1776 0.1865 0.1911 0.0090 0.0188 -0.0182 423 ALA A CB 2965 N N . GLU A 383 ? 0.1686 0.1773 0.1769 0.0128 0.0166 -0.0188 424 GLU A N 2966 C CA . GLU A 383 ? 0.1691 0.1791 0.1755 0.0124 0.0149 -0.0198 424 GLU A CA 2967 C C . GLU A 383 ? 0.1663 0.1785 0.1747 0.0099 0.0152 -0.0223 424 GLU A C 2968 O O . GLU A 383 ? 0.1693 0.1829 0.1764 0.0083 0.0145 -0.0232 424 GLU A O 2969 C CB . GLU A 383 ? 0.1724 0.1811 0.1779 0.0154 0.0138 -0.0193 424 GLU A CB 2970 C CG . GLU A 383 ? 0.1703 0.1802 0.1747 0.0152 0.0117 -0.0204 424 GLU A CG 2971 C CD . GLU A 383 ? 0.1835 0.1955 0.1912 0.0136 0.0118 -0.0228 424 GLU A CD 2972 O OE1 . GLU A 383 ? 0.1886 0.2009 0.1991 0.0130 0.0132 -0.0238 424 GLU A OE1 2973 O OE2 . GLU A 383 ? 0.1808 0.1938 0.1886 0.0132 0.0104 -0.0236 424 GLU A OE2 2974 N N . GLU A 384 ? 0.1548 0.1670 0.1664 0.0097 0.0164 -0.0235 425 GLU A N 2975 C CA . GLU A 384 ? 0.1726 0.1867 0.1860 0.0078 0.0170 -0.0260 425 GLU A CA 2976 C C . GLU A 384 ? 0.1578 0.1730 0.1698 0.0053 0.0172 -0.0269 425 GLU A C 2977 O O . GLU A 384 ? 0.1879 0.2045 0.1999 0.0038 0.0177 -0.0287 425 GLU A O 2978 C CB . GLU A 384 ? 0.1768 0.1904 0.1938 0.0084 0.0182 -0.0270 425 GLU A CB 2979 C CG . GLU A 384 ? 0.1779 0.1903 0.1961 0.0111 0.0178 -0.0264 425 GLU A CG 2980 C CD . GLU A 384 ? 0.1914 0.2054 0.2103 0.0112 0.0167 -0.0278 425 GLU A CD 2981 O OE1 . GLU A 384 ? 0.1708 0.1864 0.1887 0.0094 0.0165 -0.0286 425 GLU A OE1 2982 O OE2 . GLU A 384 ? 0.2110 0.2243 0.2314 0.0133 0.0161 -0.0278 425 GLU A OE2 2983 N N . PHE A 385 ? 0.1650 0.1794 0.1759 0.0050 0.0170 -0.0257 426 PHE A N 2984 C CA . PHE A 385 ? 0.1616 0.1767 0.1710 0.0030 0.0169 -0.0266 426 PHE A CA 2985 C C . PHE A 385 ? 0.1816 0.1972 0.1873 0.0024 0.0158 -0.0256 426 PHE A C 2986 O O . PHE A 385 ? 0.1894 0.2053 0.1935 0.0010 0.0153 -0.0258 426 PHE A O 2987 C CB . PHE A 385 ? 0.1897 0.2039 0.2013 0.0028 0.0172 -0.0264 426 PHE A CB 2988 C CG . PHE A 385 ? 0.1703 0.1842 0.1857 0.0027 0.0183 -0.0280 426 PHE A CG 2989 C CD1 . PHE A 385 ? 0.1805 0.1950 0.1961 0.0011 0.0183 -0.0305 426 PHE A CD1 2990 C CD2 . PHE A 385 ? 0.1938 0.2065 0.2119 0.0045 0.0192 -0.0271 426 PHE A CD2 2991 C CE1 . PHE A 385 ? 0.1895 0.2036 0.2088 0.0011 0.0191 -0.0324 426 PHE A CE1 2992 C CE2 . PHE A 385 ? 0.1972 0.2095 0.2192 0.0045 0.0202 -0.0287 426 PHE A CE2 2993 C CZ . PHE A 385 ? 0.1969 0.2100 0.2197 0.0027 0.0201 -0.0314 426 PHE A CZ 2994 N N . GLY A 386 ? 0.1761 0.1917 0.1807 0.0035 0.0150 -0.0245 427 GLY A N 2995 C CA . GLY A 386 ? 0.1603 0.1762 0.1617 0.0030 0.0139 -0.0236 427 GLY A CA 2996 C C . GLY A 386 ? 0.1674 0.1821 0.1674 0.0048 0.0129 -0.0214 427 GLY A C 2997 O O . GLY A 386 ? 0.1643 0.1789 0.1617 0.0044 0.0120 -0.0204 427 GLY A O 2998 N N A LEU A 387 ? 0.1450 0.1585 0.1460 0.0071 0.0128 -0.0207 428 LEU A N 2999 N N B LEU A 387 ? 0.1462 0.1597 0.1473 0.0071 0.0129 -0.0208 428 LEU A N 3000 C CA A LEU A 387 ? 0.1558 0.1678 0.1545 0.0093 0.0118 -0.0187 428 LEU A CA 3001 C CA B LEU A 387 ? 0.1589 0.1708 0.1579 0.0094 0.0119 -0.0188 428 LEU A CA 3002 C C A LEU A 387 ? 0.1489 0.1599 0.1469 0.0095 0.0125 -0.0170 428 LEU A C 3003 C C B LEU A 387 ? 0.1522 0.1634 0.1502 0.0093 0.0125 -0.0171 428 LEU A C 3004 O O A LEU A 387 ? 0.1394 0.1494 0.1349 0.0108 0.0118 -0.0153 428 LEU A O 3005 O O B LEU A 387 ? 0.1594 0.1698 0.1547 0.0101 0.0116 -0.0157 428 LEU A O 3006 C CB A LEU A 387 ? 0.1564 0.1689 0.1527 0.0090 0.0101 -0.0187 428 LEU A CB 3007 C CB B LEU A 387 ? 0.1586 0.1709 0.1555 0.0095 0.0101 -0.0188 428 LEU A CB 3008 C CG A LEU A 387 ? 0.1491 0.1629 0.1472 0.0083 0.0096 -0.0204 428 LEU A CG 3009 C CG B LEU A 387 ? 0.1426 0.1567 0.1414 0.0080 0.0099 -0.0208 428 LEU A CG 3010 C CD1 A LEU A 387 ? 0.1305 0.1443 0.1269 0.0087 0.0077 -0.0200 428 LEU A CD1 3011 C CD1 B LEU A 387 ? 0.1516 0.1661 0.1491 0.0077 0.0083 -0.0207 428 LEU A CD1 3012 C CD2 A LEU A 387 ? 0.1591 0.1723 0.1595 0.0102 0.0096 -0.0210 428 LEU A CD2 3013 C CD2 B LEU A 387 ? 0.1525 0.1664 0.1541 0.0096 0.0100 -0.0217 428 LEU A CD2 3014 N N . LEU A 388 ? 0.1448 0.1559 0.1455 0.0085 0.0138 -0.0174 429 LEU A N 3015 C CA . LEU A 388 ? 0.1553 0.1661 0.1564 0.0080 0.0143 -0.0162 429 LEU A CA 3016 C C . LEU A 388 ? 0.1567 0.1654 0.1574 0.0107 0.0151 -0.0136 429 LEU A C 3017 O O . LEU A 388 ? 0.1686 0.1770 0.1679 0.0108 0.0149 -0.0121 429 LEU A O 3018 C CB . LEU A 388 ? 0.1466 0.1581 0.1512 0.0062 0.0151 -0.0177 429 LEU A CB 3019 C CG . LEU A 388 ? 0.1806 0.1937 0.1849 0.0040 0.0147 -0.0204 429 LEU A CG 3020 C CD1 . LEU A 388 ? 0.2074 0.2208 0.2151 0.0027 0.0152 -0.0219 429 LEU A CD1 3021 C CD2 . LEU A 388 ? 0.1852 0.1994 0.1859 0.0026 0.0134 -0.0206 429 LEU A CD2 3022 N N . GLY A 389 ? 0.1786 0.1857 0.1804 0.0128 0.0162 -0.0128 430 GLY A N 3023 C CA . GLY A 389 ? 0.1831 0.1880 0.1844 0.0156 0.0175 -0.0101 430 GLY A CA 3024 C C . GLY A 389 ? 0.1806 0.1843 0.1769 0.0177 0.0162 -0.0087 430 GLY A C 3025 O O . GLY A 389 ? 0.1887 0.1912 0.1835 0.0189 0.0169 -0.0066 430 GLY A O 3026 N N . SER A 390 ? 0.1741 0.1781 0.1680 0.0182 0.0144 -0.0100 431 SER A N 3027 C CA . SER A 390 ? 0.1744 0.1771 0.1637 0.0204 0.0127 -0.0090 431 SER A CA 3028 C C . SER A 390 ? 0.1631 0.1671 0.1513 0.0185 0.0120 -0.0089 431 SER A C 3029 O O . SER A 390 ? 0.1741 0.1767 0.1593 0.0202 0.0118 -0.0072 431 SER A O 3030 C CB . SER A 390 ? 0.1814 0.1845 0.1697 0.0209 0.0105 -0.0108 431 SER A CB 3031 O OG . SER A 390 ? 0.1915 0.1974 0.1821 0.0176 0.0098 -0.0130 431 SER A OG 3032 N N . THR A 391 ? 0.1553 0.1617 0.1454 0.0151 0.0115 -0.0106 432 THR A N 3033 C CA . THR A 391 ? 0.1558 0.1632 0.1443 0.0134 0.0105 -0.0105 432 THR A CA 3034 C C . THR A 391 ? 0.1369 0.1438 0.1263 0.0135 0.0118 -0.0088 432 THR A C 3035 O O . THR A 391 ? 0.1590 0.1655 0.1459 0.0141 0.0111 -0.0076 432 THR A O 3036 C CB . THR A 391 ? 0.1454 0.1552 0.1351 0.0102 0.0099 -0.0127 432 THR A CB 3037 O OG1 . THR A 391 ? 0.1750 0.1851 0.1647 0.0105 0.0090 -0.0141 432 THR A OG1 3038 C CG2 . THR A 391 ? 0.1695 0.1799 0.1569 0.0089 0.0087 -0.0125 432 THR A CG2 3039 N N . GLU A 392 ? 0.1424 0.1494 0.1355 0.0129 0.0135 -0.0087 433 GLU A N 3040 C CA . GLU A 392 ? 0.1629 0.1697 0.1582 0.0128 0.0147 -0.0072 433 GLU A CA 3041 C C . GLU A 392 ? 0.1560 0.1604 0.1491 0.0161 0.0159 -0.0044 433 GLU A C 3042 O O . GLU A 392 ? 0.1756 0.1797 0.1682 0.0164 0.0161 -0.0030 433 GLU A O 3043 C CB . GLU A 392 ? 0.1620 0.1691 0.1626 0.0116 0.0162 -0.0077 433 GLU A CB 3044 C CG . GLU A 392 ? 0.1679 0.1771 0.1701 0.0086 0.0151 -0.0105 433 GLU A CG 3045 C CD . GLU A 392 ? 0.1713 0.1818 0.1718 0.0068 0.0134 -0.0111 433 GLU A CD 3046 O OE1 . GLU A 392 ? 0.1898 0.2002 0.1920 0.0069 0.0136 -0.0098 433 GLU A OE1 3047 O OE2 . GLU A 392 ? 0.2034 0.2150 0.2011 0.0055 0.0120 -0.0127 433 GLU A OE2 3048 N N . TRP A 393 ? 0.1658 0.1683 0.1575 0.0188 0.0166 -0.0036 434 TRP A N 3049 C CA . TRP A 393 ? 0.1823 0.1820 0.1707 0.0226 0.0178 -0.0009 434 TRP A CA 3050 C C . TRP A 393 ? 0.1869 0.1862 0.1703 0.0235 0.0158 -0.0008 434 TRP A C 3051 O O . TRP A 393 ? 0.1826 0.1806 0.1643 0.0252 0.0167 0.0012 434 TRP A O 3052 C CB . TRP A 393 ? 0.1869 0.1845 0.1743 0.0253 0.0187 -0.0005 434 TRP A CB 3053 C CG . TRP A 393 ? 0.1711 0.1653 0.1546 0.0296 0.0202 0.0024 434 TRP A CG 3054 C CD1 . TRP A 393 ? 0.1810 0.1733 0.1663 0.0314 0.0236 0.0052 434 TRP A CD1 3055 C CD2 . TRP A 393 ? 0.2073 0.1995 0.1845 0.0328 0.0185 0.0027 434 TRP A CD2 3056 N NE1 . TRP A 393 ? 0.2097 0.1987 0.1893 0.0358 0.0244 0.0074 434 TRP A NE1 3057 C CE2 . TRP A 393 ? 0.2124 0.2012 0.1868 0.0368 0.0210 0.0058 434 TRP A CE2 3058 C CE3 . TRP A 393 ? 0.1967 0.1894 0.1705 0.0328 0.0151 0.0007 434 TRP A CE3 3059 C CZ2 . TRP A 393 ? 0.2179 0.2036 0.1853 0.0411 0.0200 0.0067 434 TRP A CZ2 3060 C CZ3 . TRP A 393 ? 0.2108 0.2005 0.1783 0.0370 0.0137 0.0015 434 TRP A CZ3 3061 C CH2 . TRP A 393 ? 0.2279 0.2141 0.1919 0.0412 0.0161 0.0044 434 TRP A CH2 3062 N N . ALA A 394 ? 0.1698 0.1703 0.1514 0.0224 0.0132 -0.0029 435 ALA A N 3063 C CA . ALA A 394 ? 0.1817 0.1817 0.1591 0.0232 0.0110 -0.0029 435 ALA A CA 3064 C C . ALA A 394 ? 0.1800 0.1814 0.1582 0.0211 0.0109 -0.0026 435 ALA A C 3065 O O . ALA A 394 ? 0.1889 0.1893 0.1640 0.0225 0.0103 -0.0015 435 ALA A O 3066 C CB . ALA A 394 ? 0.1906 0.1917 0.1672 0.0223 0.0084 -0.0053 435 ALA A CB 3067 N N . GLU A 395 ? 0.1663 0.1701 0.1484 0.0178 0.0113 -0.0037 436 GLU A N 3068 C CA . GLU A 395 ? 0.1838 0.1887 0.1667 0.0160 0.0110 -0.0033 436 GLU A CA 3069 C C . GLU A 395 ? 0.1832 0.1868 0.1670 0.0179 0.0130 -0.0008 436 GLU A C 3070 O O . GLU A 395 ? 0.1995 0.2029 0.1819 0.0182 0.0125 0.0002 436 GLU A O 3071 C CB . GLU A 395 ? 0.1700 0.1772 0.1566 0.0126 0.0108 -0.0050 436 GLU A CB 3072 C CG . GLU A 395 ? 0.1763 0.1848 0.1612 0.0106 0.0090 -0.0072 436 GLU A CG 3073 C CD . GLU A 395 ? 0.2123 0.2227 0.1994 0.0076 0.0087 -0.0090 436 GLU A CD 3074 O OE1 . GLU A 395 ? 0.1846 0.1959 0.1696 0.0060 0.0073 -0.0100 436 GLU A OE1 3075 O OE2 . GLU A 395 ? 0.2007 0.2113 0.1914 0.0071 0.0099 -0.0092 436 GLU A OE2 3076 N N . GLU A 396 ? 0.1826 0.1851 0.1691 0.0192 0.0153 0.0003 437 GLU A N 3077 C CA . GLU A 396 ? 0.1767 0.1779 0.1650 0.0210 0.0179 0.0029 437 GLU A CA 3078 C C . GLU A 396 ? 0.1824 0.1810 0.1650 0.0247 0.0180 0.0048 437 GLU A C 3079 O O . GLU A 396 ? 0.2041 0.2022 0.1865 0.0257 0.0190 0.0066 437 GLU A O 3080 C CB . GLU A 396 ? 0.2004 0.2007 0.1928 0.0218 0.0206 0.0038 437 GLU A CB 3081 C CG . GLU A 396 ? 0.2314 0.2301 0.2265 0.0238 0.0239 0.0069 437 GLU A CG 3082 C CD . GLU A 396 ? 0.3893 0.3872 0.3899 0.0242 0.0269 0.0080 437 GLU A CD 3083 O OE1 . GLU A 396 ? 0.4914 0.4882 0.4953 0.0256 0.0300 0.0107 437 GLU A OE1 3084 O OE2 . GLU A 396 ? 0.3142 0.3122 0.3158 0.0236 0.0267 0.0067 437 GLU A OE2 3085 N N . ASN A 397 ? 0.1746 0.1717 0.1527 0.0267 0.0169 0.0043 438 ASN A N 3086 C CA . ASN A 397 ? 0.1816 0.1757 0.1538 0.0309 0.0170 0.0059 438 ASN A CA 3087 C C . ASN A 397 ? 0.1771 0.1713 0.1449 0.0310 0.0135 0.0044 438 ASN A C 3088 O O . ASN A 397 ? 0.1999 0.1915 0.1624 0.0345 0.0127 0.0049 438 ASN A O 3089 C CB . ASN A 397 ? 0.1917 0.1833 0.1621 0.0339 0.0181 0.0065 438 ASN A CB 3090 C CG . ASN A 397 ? 0.2191 0.2099 0.1937 0.0345 0.0220 0.0087 438 ASN A CG 3091 O OD1 . ASN A 397 ? 0.2442 0.2335 0.2187 0.0365 0.0246 0.0113 438 ASN A OD1 3092 N ND2 . ASN A 397 ? 0.2137 0.2058 0.1928 0.0326 0.0226 0.0076 438 ASN A ND2 3093 N N . SER A 398 ? 0.1730 0.1699 0.1428 0.0273 0.0117 0.0027 439 SER A N 3094 C CA . SER A 398 ? 0.1782 0.1752 0.1445 0.0271 0.0085 0.0011 439 SER A CA 3095 C C . SER A 398 ? 0.1740 0.1687 0.1355 0.0302 0.0078 0.0024 439 SER A C 3096 O O . SER A 398 ? 0.2126 0.2061 0.1705 0.0317 0.0053 0.0013 439 SER A O 3097 C CB . SER A 398 ? 0.1737 0.1736 0.1425 0.0229 0.0071 -0.0003 439 SER A CB 3098 O OG . SER A 398 ? 0.2113 0.2119 0.1818 0.0221 0.0082 0.0010 439 SER A OG 3099 N N . ARG A 399 ? 0.1697 0.1637 0.1313 0.0312 0.0098 0.0045 440 ARG A N 3100 C CA . ARG A 399 ? 0.1736 0.1654 0.1304 0.0343 0.0093 0.0057 440 ARG A CA 3101 C C . ARG A 399 ? 0.1950 0.1831 0.1466 0.0391 0.0097 0.0065 440 ARG A C 3102 O O . ARG A 399 ? 0.2149 0.2010 0.1613 0.0418 0.0075 0.0061 440 ARG A O 3103 C CB . ARG A 399 ? 0.1867 0.1787 0.1456 0.0344 0.0118 0.0079 440 ARG A CB 3104 C CG . ARG A 399 ? 0.2117 0.2070 0.1747 0.0300 0.0106 0.0069 440 ARG A CG 3105 C CD . ARG A 399 ? 0.2479 0.2444 0.2162 0.0288 0.0132 0.0084 440 ARG A CD 3106 N NE . ARG A 399 ? 0.2251 0.2245 0.1964 0.0249 0.0113 0.0069 440 ARG A NE 3107 C CZ . ARG A 399 ? 0.2476 0.2493 0.2221 0.0216 0.0103 0.0051 440 ARG A CZ 3108 N NH1 . ARG A 399 ? 0.2694 0.2712 0.2454 0.0212 0.0110 0.0043 440 ARG A NH1 3109 N NH2 . ARG A 399 ? 0.2367 0.2402 0.2124 0.0189 0.0085 0.0041 440 ARG A NH2 3110 N N . LEU A 400 ? 0.1834 0.1706 0.1362 0.0404 0.0123 0.0077 441 LEU A N 3111 C CA . LEU A 400 ? 0.2110 0.1945 0.1584 0.0452 0.0128 0.0086 441 LEU A CA 3112 C C . LEU A 400 ? 0.2205 0.2038 0.1657 0.0454 0.0088 0.0058 441 LEU A C 3113 O O . LEU A 400 ? 0.2271 0.2075 0.1665 0.0492 0.0068 0.0054 441 LEU A O 3114 C CB . LEU A 400 ? 0.2174 0.2000 0.1673 0.0463 0.0164 0.0104 441 LEU A CB 3115 C CG . LEU A 400 ? 0.2243 0.2075 0.1785 0.0456 0.0205 0.0131 441 LEU A CG 3116 C CD1 . LEU A 400 ? 0.2260 0.2076 0.1823 0.0472 0.0242 0.0151 441 LEU A CD1 3117 C CD2 . LEU A 400 ? 0.2632 0.2443 0.2133 0.0486 0.0217 0.0152 441 LEU A CD2 3118 N N . LEU A 401 ? 0.2020 0.1883 0.1520 0.0415 0.0077 0.0038 442 LEU A N 3119 C CA . LEU A 401 ? 0.2185 0.2049 0.1678 0.0415 0.0044 0.0012 442 LEU A CA 3120 C C . LEU A 401 ? 0.2312 0.2177 0.1784 0.0412 0.0009 -0.0004 442 LEU A C 3121 O O . LEU A 401 ? 0.2618 0.2466 0.2059 0.0437 -0.0020 -0.0019 442 LEU A O 3122 C CB . LEU A 401 ? 0.2081 0.1978 0.1634 0.0373 0.0047 -0.0003 442 LEU A CB 3123 C CG . LEU A 401 ? 0.2019 0.1913 0.1596 0.0377 0.0078 0.0009 442 LEU A CG 3124 C CD1 . LEU A 401 ? 0.2050 0.1980 0.1689 0.0331 0.0081 -0.0007 442 LEU A CD1 3125 C CD2 . LEU A 401 ? 0.2369 0.2236 0.1914 0.0415 0.0070 0.0006 442 LEU A CD2 3126 N N A GLN A 402 ? 0.2108 0.1993 0.1597 0.0384 0.0007 -0.0004 443 GLN A N 3127 N N B GLN A 402 ? 0.2181 0.2067 0.1673 0.0383 0.0009 -0.0003 443 GLN A N 3128 C CA A GLN A 402 ? 0.2167 0.2051 0.1641 0.0381 -0.0028 -0.0021 443 GLN A CA 3129 C CA B GLN A 402 ? 0.2276 0.2164 0.1754 0.0376 -0.0021 -0.0016 443 GLN A CA 3130 C C A GLN A 402 ? 0.2194 0.2043 0.1606 0.0426 -0.0040 -0.0014 443 GLN A C 3131 C C B GLN A 402 ? 0.2291 0.2141 0.1706 0.0425 -0.0038 -0.0013 443 GLN A C 3132 O O A GLN A 402 ? 0.2096 0.1936 0.1489 0.0434 -0.0074 -0.0031 443 GLN A O 3133 O O B GLN A 402 ? 0.2201 0.2041 0.1599 0.0436 -0.0073 -0.0033 443 GLN A O 3134 C CB A GLN A 402 ? 0.1988 0.1902 0.1497 0.0337 -0.0030 -0.0025 443 GLN A CB 3135 C CB B GLN A 402 ? 0.2277 0.2184 0.1774 0.0347 -0.0011 -0.0006 443 GLN A CB 3136 C CG A GLN A 402 ? 0.1807 0.1722 0.1313 0.0335 -0.0009 -0.0005 443 GLN A CG 3137 C CG B GLN A 402 ? 0.2429 0.2326 0.1898 0.0354 -0.0034 -0.0010 443 GLN A CG 3138 C CD A GLN A 402 ? 0.2076 0.2023 0.1622 0.0290 -0.0010 -0.0010 443 GLN A CD 3139 C CD B GLN A 402 ? 0.2752 0.2668 0.2245 0.0324 -0.0062 -0.0032 443 GLN A CD 3140 O OE1 A GLN A 402 ? 0.1997 0.1963 0.1571 0.0261 -0.0019 -0.0026 443 GLN A OE1 3141 O OE1 B GLN A 402 ? 0.2733 0.2674 0.2267 0.0289 -0.0057 -0.0040 443 GLN A OE1 3142 N NE2 A GLN A 402 ? 0.2180 0.2130 0.1728 0.0285 0.0002 0.0005 443 GLN A NE2 3143 N NE2 B GLN A 402 ? 0.1685 0.1585 0.1152 0.0338 -0.0091 -0.0041 443 GLN A NE2 3144 N N . GLU A 403 ? 0.2205 0.2033 0.1587 0.0455 -0.0011 0.0011 444 GLU A N 3145 C CA . GLU A 403 ? 0.2122 0.1913 0.1438 0.0502 -0.0022 0.0017 444 GLU A CA 3146 C C . GLU A 403 ? 0.2334 0.2088 0.1599 0.0552 -0.0024 0.0018 444 GLU A C 3147 O O . GLU A 403 ? 0.2266 0.1986 0.1469 0.0595 -0.0044 0.0015 444 GLU A O 3148 C CB . GLU A 403 ? 0.2246 0.2030 0.1550 0.0512 0.0010 0.0044 444 GLU A CB 3149 C CG . GLU A 403 ? 0.2442 0.2262 0.1797 0.0464 0.0013 0.0044 444 GLU A CG 3150 C CD . GLU A 403 ? 0.3055 0.2885 0.2411 0.0445 -0.0027 0.0021 444 GLU A CD 3151 O OE1 . GLU A 403 ? 0.2453 0.2265 0.1780 0.0464 -0.0060 0.0003 444 GLU A OE1 3152 O OE2 . GLU A 403 ? 0.2940 0.2795 0.2331 0.0409 -0.0027 0.0022 444 GLU A OE2 3153 N N . ARG A 404 ? 0.2225 0.1984 0.1512 0.0549 -0.0007 0.0022 445 ARG A N 3154 C CA . ARG A 404 ? 0.2157 0.1878 0.1392 0.0599 -0.0005 0.0027 445 ARG A CA 3155 C C . ARG A 404 ? 0.2381 0.2109 0.1637 0.0593 -0.0030 0.0004 445 ARG A C 3156 O O . ARG A 404 ? 0.2361 0.2057 0.1572 0.0637 -0.0037 0.0004 445 ARG A O 3157 C CB . ARG A 404 ? 0.2182 0.1892 0.1416 0.0613 0.0046 0.0061 445 ARG A CB 3158 C CG . ARG A 404 ? 0.2311 0.2010 0.1526 0.0626 0.0075 0.0087 445 ARG A CG 3159 C CD . ARG A 404 ? 0.2446 0.2136 0.1674 0.0638 0.0129 0.0122 445 ARG A CD 3160 N NE . ARG A 404 ? 0.2255 0.1948 0.1493 0.0635 0.0159 0.0145 445 ARG A NE 3161 C CZ . ARG A 404 ? 0.2507 0.2202 0.1783 0.0632 0.0208 0.0175 445 ARG A CZ 3162 N NH1 . ARG A 404 ? 0.2389 0.2082 0.1694 0.0632 0.0235 0.0187 445 ARG A NH1 3163 N NH2 . ARG A 404 ? 0.2590 0.2290 0.1879 0.0629 0.0229 0.0192 445 ARG A NH2 3164 N N . GLY A 405 ? 0.2185 0.1954 0.1508 0.0543 -0.0042 -0.0015 446 GLY A N 3165 C CA . GLY A 405 ? 0.2090 0.1869 0.1444 0.0534 -0.0057 -0.0035 446 GLY A CA 3166 C C . GLY A 405 ? 0.2204 0.1970 0.1539 0.0554 -0.0107 -0.0064 446 GLY A C 3167 O O . GLY A 405 ? 0.2494 0.2277 0.1852 0.0531 -0.0135 -0.0083 446 GLY A O 3168 N N . VAL A 406 ? 0.2283 0.2019 0.1580 0.0597 -0.0120 -0.0068 447 VAL A N 3169 C CA . VAL A 406 ? 0.2364 0.2088 0.1651 0.0618 -0.0171 -0.0098 447 VAL A CA 3170 C C . VAL A 406 ? 0.2313 0.2071 0.1674 0.0583 -0.0189 -0.0123 447 VAL A C 3171 O O . VAL A 406 ? 0.2331 0.2105 0.1728 0.0564 -0.0223 -0.0149 447 VAL A O 3172 C CB . VAL A 406 ? 0.2570 0.2243 0.1779 0.0686 -0.0183 -0.0095 447 VAL A CB 3173 C CG1 . VAL A 406 ? 0.2806 0.2467 0.2014 0.0708 -0.0242 -0.0131 447 VAL A CG1 3174 C CG2 . VAL A 406 ? 0.2809 0.2444 0.1938 0.0726 -0.0173 -0.0074 447 VAL A CG2 3175 N N . ALA A 407 ? 0.2236 0.2005 0.1625 0.0573 -0.0163 -0.0115 448 ALA A N 3176 C CA . ALA A 407 ? 0.2211 0.2009 0.1668 0.0544 -0.0178 -0.0139 448 ALA A CA 3177 C C . ALA A 407 ? 0.2231 0.2044 0.1717 0.0526 -0.0138 -0.0125 448 ALA A C 3178 O O . ALA A 407 ? 0.2289 0.2081 0.1738 0.0547 -0.0107 -0.0098 448 ALA A O 3179 C CB . ALA A 407 ? 0.2497 0.2271 0.1936 0.0586 -0.0221 -0.0162 448 ALA A CB 3180 N N . TYR A 408 ? 0.2114 0.1963 0.1670 0.0486 -0.0140 -0.0142 449 TYR A N 3181 C CA . TYR A 408 ? 0.1896 0.1763 0.1490 0.0463 -0.0105 -0.0133 449 TYR A CA 3182 C C . TYR A 408 ? 0.2040 0.1916 0.1674 0.0464 -0.0129 -0.0159 449 TYR A C 3183 O O . TYR A 408 ? 0.2064 0.1964 0.1743 0.0442 -0.0153 -0.0182 449 TYR A O 3184 C CB . TYR A 408 ? 0.1871 0.1777 0.1513 0.0408 -0.0079 -0.0130 449 TYR A CB 3185 C CG . TYR A 408 ? 0.1728 0.1651 0.1411 0.0387 -0.0050 -0.0127 449 TYR A CG 3186 C CD1 . TYR A 408 ? 0.1903 0.1814 0.1572 0.0394 -0.0015 -0.0103 449 TYR A CD1 3187 C CD2 . TYR A 408 ? 0.1903 0.1853 0.1643 0.0360 -0.0057 -0.0150 449 TYR A CD2 3188 C CE1 . TYR A 408 ? 0.1949 0.1873 0.1658 0.0376 0.0010 -0.0101 449 TYR A CE1 3189 C CE2 . TYR A 408 ? 0.1996 0.1960 0.1772 0.0342 -0.0031 -0.0149 449 TYR A CE2 3190 C CZ . TYR A 408 ? 0.1889 0.1841 0.1649 0.0350 0.0001 -0.0126 449 TYR A CZ 3191 O OH . TYR A 408 ? 0.2050 0.2015 0.1852 0.0331 0.0024 -0.0128 449 TYR A OH 3192 N N . ILE A 409 ? 0.1952 0.1813 0.1578 0.0488 -0.0118 -0.0152 450 ILE A N 3193 C CA . ILE A 409 ? 0.2006 0.1877 0.1676 0.0490 -0.0137 -0.0175 450 ILE A CA 3194 C C . ILE A 409 ? 0.2111 0.2005 0.1826 0.0459 -0.0099 -0.0168 450 ILE A C 3195 O O . ILE A 409 ? 0.1989 0.1865 0.1679 0.0472 -0.0067 -0.0144 450 ILE A O 3196 C CB . ILE A 409 ? 0.2053 0.1882 0.1671 0.0549 -0.0160 -0.0176 450 ILE A CB 3197 C CG1 . ILE A 409 ? 0.2277 0.2079 0.1844 0.0584 -0.0203 -0.0186 450 ILE A CG1 3198 C CG2 . ILE A 409 ? 0.2208 0.2049 0.1877 0.0549 -0.0178 -0.0199 450 ILE A CG2 3199 C CD1 . ILE A 409 ? 0.2581 0.2411 0.2204 0.0559 -0.0241 -0.0218 450 ILE A CD1 3200 N N . ASN A 410 ? 0.1987 0.1918 0.1769 0.0420 -0.0100 -0.0188 451 ASN A N 3201 C CA . ASN A 410 ? 0.1792 0.1744 0.1617 0.0391 -0.0066 -0.0185 451 ASN A CA 3202 C C . ASN A 410 ? 0.2090 0.2029 0.1924 0.0416 -0.0068 -0.0190 451 ASN A C 3203 O O . ASN A 410 ? 0.2222 0.2145 0.2046 0.0449 -0.0102 -0.0203 451 ASN A O 3204 C CB . ASN A 410 ? 0.1721 0.1714 0.1608 0.0343 -0.0063 -0.0204 451 ASN A CB 3205 C CG . ASN A 410 ? 0.1899 0.1912 0.1811 0.0308 -0.0025 -0.0197 451 ASN A CG 3206 O OD1 . ASN A 410 ? 0.2046 0.2053 0.1932 0.0302 -0.0003 -0.0177 451 ASN A OD1 3207 N ND2 . ASN A 410 ? 0.2067 0.2105 0.2032 0.0285 -0.0018 -0.0214 451 ASN A ND2 3208 N N . ALA A 411 ? 0.2093 0.2038 0.1950 0.0402 -0.0035 -0.0181 452 ALA A N 3209 C CA . ALA A 411 ? 0.2173 0.2105 0.2042 0.0425 -0.0035 -0.0184 452 ALA A CA 3210 C C . ALA A 411 ? 0.2113 0.2071 0.2039 0.0391 -0.0006 -0.0189 452 ALA A C 3211 O O . ALA A 411 ? 0.2156 0.2100 0.2079 0.0399 0.0021 -0.0174 452 ALA A O 3212 C CB . ALA A 411 ? 0.2395 0.2281 0.2198 0.0473 -0.0027 -0.0157 452 ALA A CB 3213 N N . ASP A 412 ? 0.2003 0.1998 0.1979 0.0352 -0.0008 -0.0211 453 ASP A N 3214 C CA . ASP A 412 ? 0.1968 0.1986 0.1998 0.0325 0.0016 -0.0221 453 ASP A CA 3215 C C . ASP A 412 ? 0.2088 0.2105 0.2149 0.0345 -0.0003 -0.0239 453 ASP A C 3216 O O . ASP A 412 ? 0.1968 0.1958 0.1998 0.0386 -0.0028 -0.0236 453 ASP A O 3217 C CB . ASP A 412 ? 0.1884 0.1937 0.1948 0.0280 0.0026 -0.0234 453 ASP A CB 3218 C CG . ASP A 412 ? 0.2120 0.2191 0.2219 0.0251 0.0057 -0.0238 453 ASP A CG 3219 O OD1 . ASP A 412 ? 0.2359 0.2417 0.2467 0.0265 0.0069 -0.0235 453 ASP A OD1 3220 O OD2 . ASP A 412 ? 0.1974 0.2068 0.2090 0.0217 0.0068 -0.0247 453 ASP A OD2 3221 N N . SER A 413 ? 0.1928 0.1973 0.2048 0.0318 0.0007 -0.0258 454 SER A N 3222 C CA . SER A 413 ? 0.2074 0.2122 0.2235 0.0334 -0.0006 -0.0276 454 SER A CA 3223 C C . SER A 413 ? 0.2180 0.2213 0.2329 0.0370 -0.0049 -0.0285 454 SER A C 3224 O O . SER A 413 ? 0.2088 0.2130 0.2240 0.0366 -0.0072 -0.0294 454 SER A O 3225 C CB . SER A 413 ? 0.2232 0.2319 0.2457 0.0298 0.0004 -0.0298 454 SER A CB 3226 O OG . SER A 413 ? 0.2016 0.2112 0.2243 0.0270 0.0039 -0.0292 454 SER A OG 3227 N N . SER A 414 ? 0.2302 0.2307 0.2435 0.0409 -0.0060 -0.0281 455 SER A N 3228 C CA . SER A 414 ? 0.2441 0.2427 0.2558 0.0450 -0.0105 -0.0292 455 SER A CA 3229 C C . SER A 414 ? 0.2386 0.2399 0.2579 0.0443 -0.0130 -0.0323 455 SER A C 3230 O O . SER A 414 ? 0.2294 0.2301 0.2492 0.0466 -0.0172 -0.0339 455 SER A O 3231 C CB . SER A 414 ? 0.2541 0.2483 0.2606 0.0500 -0.0111 -0.0276 455 SER A CB 3232 O OG . SER A 414 ? 0.2608 0.2521 0.2602 0.0513 -0.0092 -0.0246 455 SER A OG 3233 N N . ILE A 415 ? 0.2422 0.2465 0.2676 0.0411 -0.0104 -0.0333 456 ILE A N 3234 C CA . ILE A 415 ? 0.2416 0.2485 0.2748 0.0405 -0.0120 -0.0362 456 ILE A CA 3235 C C . ILE A 415 ? 0.2520 0.2630 0.2909 0.0355 -0.0086 -0.0370 456 ILE A C 3236 O O . ILE A 415 ? 0.2659 0.2773 0.3034 0.0333 -0.0049 -0.0358 456 ILE A O 3237 C CB . ILE A 415 ? 0.2359 0.2414 0.2707 0.0435 -0.0126 -0.0367 456 ILE A CB 3238 C CG1 . ILE A 415 ? 0.2715 0.2761 0.3043 0.0425 -0.0082 -0.0348 456 ILE A CG1 3239 C CG2 . ILE A 415 ? 0.2550 0.2563 0.2842 0.0490 -0.0167 -0.0362 456 ILE A CG2 3240 C CD1 . ILE A 415 ? 0.3463 0.3515 0.3840 0.0429 -0.0072 -0.0359 456 ILE A CD1 3241 N N . GLU A 416 ? 0.2429 0.2569 0.2886 0.0338 -0.0099 -0.0392 457 GLU A N 3242 C CA . GLU A 416 ? 0.2393 0.2569 0.2910 0.0297 -0.0064 -0.0402 457 GLU A CA 3243 C C . GLU A 416 ? 0.2442 0.2640 0.3047 0.0302 -0.0082 -0.0428 457 GLU A C 3244 O O . GLU A 416 ? 0.2418 0.2648 0.3086 0.0274 -0.0059 -0.0440 457 GLU A O 3245 C CB . GLU A 416 ? 0.2500 0.2694 0.3013 0.0264 -0.0049 -0.0397 457 GLU A CB 3246 C CG . GLU A 416 ? 0.2625 0.2822 0.3159 0.0270 -0.0087 -0.0407 457 GLU A CG 3247 C CD . GLU A 416 ? 0.2734 0.2941 0.3251 0.0240 -0.0074 -0.0397 457 GLU A CD 3248 O OE1 . GLU A 416 ? 0.2798 0.3003 0.3269 0.0221 -0.0042 -0.0381 457 GLU A OE1 3249 O OE2 . GLU A 416 ? 0.2821 0.3036 0.3372 0.0239 -0.0098 -0.0407 457 GLU A OE2 3250 N N . GLY A 417 ? 0.2479 0.2658 0.3085 0.0342 -0.0122 -0.0436 458 GLY A N 3251 C CA . GLY A 417 ? 0.2437 0.2632 0.3127 0.0355 -0.0149 -0.0463 458 GLY A CA 3252 C C . GLY A 417 ? 0.2587 0.2748 0.3247 0.0406 -0.0200 -0.0467 458 GLY A C 3253 O O . GLY A 417 ? 0.2638 0.2762 0.3207 0.0432 -0.0207 -0.0447 458 GLY A O 3254 N N . ASN A 418 ? 0.2646 0.2816 0.3376 0.0424 -0.0234 -0.0492 459 ASN A N 3255 C CA . ASN A 418 ? 0.2755 0.2890 0.3451 0.0477 -0.0285 -0.0498 459 ASN A CA 3256 C C . ASN A 418 ? 0.2867 0.3012 0.3627 0.0491 -0.0339 -0.0527 459 ASN A C 3257 O O . ASN A 418 ? 0.3110 0.3239 0.3886 0.0532 -0.0386 -0.0544 459 ASN A O 3258 C CB . ASN A 418 ? 0.2948 0.3074 0.3657 0.0500 -0.0279 -0.0501 459 ASN A CB 3259 C CG . ASN A 418 ? 0.3326 0.3492 0.4152 0.0481 -0.0274 -0.0527 459 ASN A CG 3260 O OD1 . ASN A 418 ? 0.3498 0.3698 0.4399 0.0454 -0.0276 -0.0542 459 ASN A OD1 3261 N ND2 . ASN A 418 ? 0.4445 0.4608 0.5291 0.0497 -0.0267 -0.0530 459 ASN A ND2 3262 N N . TYR A 419 ? 0.2566 0.2736 0.3365 0.0459 -0.0336 -0.0532 460 TYR A N 3263 C CA . TYR A 419 ? 0.2612 0.2798 0.3496 0.0465 -0.0382 -0.0561 460 TYR A CA 3264 C C . TYR A 419 ? 0.2530 0.2686 0.3356 0.0492 -0.0430 -0.0563 460 TYR A C 3265 O O . TYR A 419 ? 0.2549 0.2687 0.3388 0.0532 -0.0490 -0.0585 460 TYR A O 3266 C CB . TYR A 419 ? 0.2556 0.2788 0.3536 0.0414 -0.0349 -0.0567 460 TYR A CB 3267 C CG . TYR A 419 ? 0.2821 0.3072 0.3905 0.0414 -0.0391 -0.0596 460 TYR A CG 3268 C CD1 . TYR A 419 ? 0.3138 0.3400 0.4311 0.0437 -0.0427 -0.0624 460 TYR A CD1 3269 C CD2 . TYR A 419 ? 0.3139 0.3400 0.4243 0.0391 -0.0395 -0.0596 460 TYR A CD2 3270 C CE1 . TYR A 419 ? 0.3282 0.3564 0.4564 0.0436 -0.0467 -0.0653 460 TYR A CE1 3271 C CE2 . TYR A 419 ? 0.3139 0.3418 0.4349 0.0390 -0.0433 -0.0623 460 TYR A CE2 3272 C CZ . TYR A 419 ? 0.3551 0.3841 0.4853 0.0412 -0.0469 -0.0652 460 TYR A CZ 3273 O OH . TYR A 419 ? 0.4183 0.4492 0.5601 0.0411 -0.0508 -0.0680 460 TYR A OH 3274 N N . THR A 420 ? 0.2388 0.2535 0.3148 0.0473 -0.0408 -0.0541 461 THR A N 3275 C CA . THR A 420 ? 0.2232 0.2350 0.2935 0.0500 -0.0454 -0.0544 461 THR A CA 3276 C C . THR A 420 ? 0.2321 0.2421 0.2923 0.0487 -0.0420 -0.0512 461 THR A C 3277 O O . THR A 420 ? 0.2318 0.2429 0.2897 0.0458 -0.0365 -0.0489 461 THR A O 3278 C CB . THR A 420 ? 0.2387 0.2528 0.3184 0.0486 -0.0488 -0.0570 461 THR A CB 3279 O OG1 . THR A 420 ? 0.2507 0.2613 0.3251 0.0523 -0.0544 -0.0580 461 THR A OG1 3280 C CG2 . THR A 420 ? 0.2379 0.2554 0.3219 0.0429 -0.0441 -0.0559 461 THR A CG2 3281 N N . LEU A 421 ? 0.2293 0.2366 0.2838 0.0510 -0.0455 -0.0512 462 LEU A N 3282 C CA . LEU A 421 ? 0.2262 0.2316 0.2711 0.0502 -0.0427 -0.0482 462 LEU A CA 3283 C C . LEU A 421 ? 0.2339 0.2428 0.2834 0.0448 -0.0394 -0.0477 462 LEU A C 3284 O O . LEU A 421 ? 0.2379 0.2495 0.2966 0.0427 -0.0410 -0.0498 462 LEU A O 3285 C CB . LEU A 421 ? 0.2468 0.2479 0.2839 0.0548 -0.0476 -0.0485 462 LEU A CB 3286 C CG . LEU A 421 ? 0.2550 0.2533 0.2809 0.0552 -0.0449 -0.0452 462 LEU A CG 3287 C CD1 . LEU A 421 ? 0.2753 0.2713 0.2942 0.0572 -0.0417 -0.0427 462 LEU A CD1 3288 C CD2 . LEU A 421 ? 0.2382 0.2328 0.2583 0.0597 -0.0504 -0.0463 462 LEU A CD2 3289 N N . ARG A 422 ? 0.2189 0.2274 0.2619 0.0427 -0.0351 -0.0448 463 ARG A N 3290 C CA A ARG A 422 ? 0.2144 0.2253 0.2591 0.0382 -0.0320 -0.0438 463 ARG A CA 3291 C CA B ARG A 422 ? 0.2129 0.2237 0.2575 0.0383 -0.0322 -0.0439 463 ARG A CA 3292 C C . ARG A 422 ? 0.2175 0.2253 0.2521 0.0396 -0.0321 -0.0417 463 ARG A C 3293 O O . ARG A 422 ? 0.2392 0.2446 0.2662 0.0414 -0.0303 -0.0396 463 ARG A O 3294 C CB A ARG A 422 ? 0.2100 0.2238 0.2571 0.0340 -0.0261 -0.0425 463 ARG A CB 3295 C CB B ARG A 422 ? 0.2088 0.2226 0.2560 0.0340 -0.0263 -0.0426 463 ARG A CB 3296 C CG A ARG A 422 ? 0.2300 0.2466 0.2800 0.0292 -0.0228 -0.0417 463 ARG A CG 3297 C CG B ARG A 422 ? 0.2186 0.2334 0.2631 0.0304 -0.0231 -0.0407 463 ARG A CG 3298 C CD A ARG A 422 ? 0.2536 0.2724 0.3045 0.0259 -0.0173 -0.0406 463 ARG A CD 3299 C CD B ARG A 422 ? 0.1944 0.2114 0.2401 0.0269 -0.0178 -0.0396 463 ARG A CD 3300 N NE A ARG A 422 ? 0.2843 0.3051 0.3367 0.0218 -0.0142 -0.0398 463 ARG A NE 3301 N NE B ARG A 422 ? 0.2050 0.2224 0.2467 0.0241 -0.0150 -0.0377 463 ARG A NE 3302 C CZ A ARG A 422 ? 0.2965 0.3188 0.3479 0.0189 -0.0096 -0.0386 463 ARG A CZ 3303 C CZ B ARG A 422 ? 0.2186 0.2372 0.2589 0.0214 -0.0106 -0.0364 463 ARG A CZ 3304 N NH1 A ARG A 422 ? 0.3001 0.3222 0.3498 0.0193 -0.0075 -0.0383 463 ARG A NH1 3305 N NH1 B ARG A 422 ? 0.2010 0.2206 0.2436 0.0212 -0.0084 -0.0369 463 ARG A NH1 3306 N NH2 A ARG A 422 ? 0.3095 0.3333 0.3617 0.0157 -0.0071 -0.0378 463 ARG A NH2 3307 N NH2 B ARG A 422 ? 0.2015 0.2202 0.2380 0.0191 -0.0085 -0.0348 463 ARG A NH2 3308 N N . VAL A 423 ? 0.2126 0.2203 0.2474 0.0390 -0.0343 -0.0421 464 VAL A N 3309 C CA . VAL A 423 ? 0.2034 0.2085 0.2291 0.0398 -0.0339 -0.0400 464 VAL A CA 3310 C C . VAL A 423 ? 0.2144 0.2219 0.2428 0.0353 -0.0315 -0.0393 464 VAL A C 3311 O O . VAL A 423 ? 0.2057 0.2152 0.2416 0.0336 -0.0332 -0.0411 464 VAL A O 3312 C CB . VAL A 423 ? 0.2113 0.2127 0.2325 0.0447 -0.0396 -0.0413 464 VAL A CB 3313 C CG1 . VAL A 423 ? 0.2167 0.2155 0.2292 0.0456 -0.0391 -0.0392 464 VAL A CG1 3314 C CG2 . VAL A 423 ? 0.2665 0.2650 0.2844 0.0496 -0.0421 -0.0419 464 VAL A CG2 3315 N N . ASP A 424 ? 0.1996 0.2068 0.2220 0.0337 -0.0279 -0.0366 465 ASP A N 3316 C CA . ASP A 424 ? 0.1972 0.2059 0.2201 0.0300 -0.0260 -0.0356 465 ASP A CA 3317 C C . ASP A 424 ? 0.2028 0.2082 0.2165 0.0323 -0.0267 -0.0339 465 ASP A C 3318 O O . ASP A 424 ? 0.2006 0.2043 0.2080 0.0340 -0.0250 -0.0320 465 ASP A O 3319 C CB . ASP A 424 ? 0.2024 0.2136 0.2262 0.0258 -0.0205 -0.0340 465 ASP A CB 3320 C CG . ASP A 424 ? 0.2597 0.2737 0.2908 0.0240 -0.0186 -0.0353 465 ASP A CG 3321 O OD1 . ASP A 424 ? 0.2957 0.3103 0.3328 0.0253 -0.0212 -0.0374 465 ASP A OD1 3322 O OD2 . ASP A 424 ? 0.2414 0.2570 0.2723 0.0212 -0.0143 -0.0341 465 ASP A OD2 3323 N N . CYS A 425 ? 0.2028 0.2076 0.2162 0.0323 -0.0291 -0.0342 466 CYS A N 3324 C CA . CYS A 425 ? 0.2077 0.2094 0.2124 0.0345 -0.0296 -0.0326 466 CYS A CA 3325 C C . CYS A 425 ? 0.2042 0.2060 0.2098 0.0332 -0.0313 -0.0329 466 CYS A C 3326 O O . CYS A 425 ? 0.2237 0.2274 0.2365 0.0312 -0.0326 -0.0345 466 CYS A O 3327 C CB . CYS A 425 ? 0.2127 0.2105 0.2115 0.0402 -0.0333 -0.0331 466 CYS A CB 3328 S SG . CYS A 425 ? 0.0558 0.0524 0.0592 0.0433 -0.0402 -0.0370 466 CYS A SG 3329 N N . THR A 426 ? 0.1912 0.1906 0.1893 0.0346 -0.0311 -0.0311 467 THR A N 3330 C CA . THR A 426 ? 0.1940 0.1927 0.1918 0.0343 -0.0333 -0.0315 467 THR A CA 3331 C C . THR A 426 ? 0.2215 0.2185 0.2218 0.0374 -0.0390 -0.0345 467 THR A C 3332 O O . THR A 426 ? 0.2132 0.2079 0.2109 0.0415 -0.0417 -0.0356 467 THR A O 3333 C CB . THR A 426 ? 0.1847 0.1808 0.1733 0.0361 -0.0323 -0.0292 467 THR A CB 3334 O OG1 . THR A 426 ? 0.2061 0.2012 0.1946 0.0363 -0.0351 -0.0299 467 THR A OG1 3335 C CG2 . THR A 426 ? 0.2155 0.2079 0.1967 0.0414 -0.0336 -0.0288 467 THR A CG2 3336 N N . PRO A 427 ? 0.2045 0.2023 0.2098 0.0357 -0.0411 -0.0358 468 PRO A N 3337 C CA . PRO A 427 ? 0.2191 0.2149 0.2267 0.0388 -0.0471 -0.0387 468 PRO A CA 3338 C C . PRO A 427 ? 0.2157 0.2069 0.2134 0.0443 -0.0501 -0.0388 468 PRO A C 3339 O O . PRO A 427 ? 0.2332 0.2221 0.2309 0.0483 -0.0552 -0.0414 468 PRO A O 3340 C CB . PRO A 427 ? 0.2246 0.2214 0.2370 0.0358 -0.0476 -0.0391 468 PRO A CB 3341 C CG . PRO A 427 ? 0.2127 0.2133 0.2297 0.0305 -0.0422 -0.0372 468 PRO A CG 3342 C CD . PRO A 427 ? 0.2125 0.2128 0.2217 0.0309 -0.0382 -0.0346 468 PRO A CD 3343 N N . LEU A 428 ? 0.2078 0.1975 0.1970 0.0449 -0.0472 -0.0360 469 LEU A N 3344 C CA . LEU A 428 ? 0.2281 0.2132 0.2075 0.0505 -0.0497 -0.0358 469 LEU A CA 3345 C C . LEU A 428 ? 0.2245 0.2075 0.2004 0.0549 -0.0510 -0.0364 469 LEU A C 3346 O O . LEU A 428 ? 0.2547 0.2334 0.2234 0.0603 -0.0544 -0.0372 469 LEU A O 3347 C CB . LEU A 428 ? 0.2157 0.1998 0.1873 0.0504 -0.0456 -0.0324 469 LEU A CB 3348 C CG . LEU A 428 ? 0.2365 0.2215 0.2093 0.0474 -0.0450 -0.0317 469 LEU A CG 3349 C CD1 . LEU A 428 ? 0.2240 0.2080 0.1894 0.0475 -0.0410 -0.0284 469 LEU A CD1 3350 C CD2 . LEU A 428 ? 0.2258 0.2083 0.1984 0.0501 -0.0506 -0.0344 469 LEU A CD2 3351 N N . MET A 429 ? 0.2263 0.2117 0.2065 0.0530 -0.0485 -0.0361 470 MET A N 3352 C CA . MET A 429 ? 0.2247 0.2082 0.2022 0.0569 -0.0497 -0.0367 470 MET A CA 3353 C C . MET A 429 ? 0.2501 0.2344 0.2352 0.0577 -0.0542 -0.0403 470 MET A C 3354 O O . MET A 429 ? 0.2370 0.2197 0.2202 0.0612 -0.0555 -0.0409 470 MET A O 3355 C CB . MET A 429 ? 0.2313 0.2164 0.2079 0.0549 -0.0440 -0.0339 470 MET A CB 3356 C CG . MET A 429 ? 0.2718 0.2550 0.2399 0.0557 -0.0401 -0.0304 470 MET A CG 3357 S SD . MET A 429 ? 0.0864 0.0722 0.0565 0.0527 -0.0340 -0.0279 470 MET A SD 3358 C CE . MET A 429 ? 0.2830 0.2676 0.2461 0.0522 -0.0295 -0.0241 470 MET A CE 3359 N N . TYR A 430 ? 0.2323 0.2192 0.2265 0.0549 -0.0566 -0.0426 471 TYR A N 3360 C CA . TYR A 430 ? 0.2436 0.2318 0.2467 0.0552 -0.0605 -0.0460 471 TYR A CA 3361 C C . TYR A 430 ? 0.2588 0.2427 0.2569 0.0618 -0.0665 -0.0483 471 TYR A C 3362 O O . TYR A 430 ? 0.2714 0.2551 0.2718 0.0640 -0.0685 -0.0499 471 TYR A O 3363 C CB . TYR A 430 ? 0.2366 0.2273 0.2497 0.0519 -0.0626 -0.0481 471 TYR A CB 3364 C CG . TYR A 430 ? 0.2081 0.2033 0.2286 0.0455 -0.0574 -0.0465 471 TYR A CG 3365 C CD1 . TYR A 430 ? 0.2115 0.2087 0.2302 0.0429 -0.0516 -0.0437 471 TYR A CD1 3366 C CD2 . TYR A 430 ? 0.2368 0.2340 0.2658 0.0423 -0.0585 -0.0477 471 TYR A CD2 3367 C CE1 . TYR A 430 ? 0.2189 0.2200 0.2439 0.0373 -0.0470 -0.0425 471 TYR A CE1 3368 C CE2 . TYR A 430 ? 0.2412 0.2421 0.2764 0.0369 -0.0537 -0.0462 471 TYR A CE2 3369 C CZ . TYR A 430 ? 0.2433 0.2460 0.2761 0.0345 -0.0481 -0.0436 471 TYR A CZ 3370 O OH . TYR A 430 ? 0.2477 0.2538 0.2862 0.0294 -0.0435 -0.0423 471 TYR A OH 3371 N N . SER A 431 ? 0.2668 0.2470 0.2579 0.0651 -0.0697 -0.0488 472 SER A N 3372 C CA . SER A 431 ? 0.2684 0.2440 0.2543 0.0718 -0.0762 -0.0516 472 SER A CA 3373 C C . SER A 431 ? 0.2821 0.2545 0.2580 0.0762 -0.0746 -0.0496 472 SER A C 3374 O O . SER A 431 ? 0.2925 0.2627 0.2674 0.0806 -0.0787 -0.0517 472 SER A O 3375 C CB . SER A 431 ? 0.2957 0.2681 0.2762 0.0742 -0.0796 -0.0524 472 SER A CB 3376 O OG A SER A 431 ? 0.3140 0.2889 0.3056 0.0710 -0.0828 -0.0553 472 SER A OG 3377 O OG B SER A 431 ? 0.2519 0.2191 0.2254 0.0813 -0.0858 -0.0550 472 SER A OG 3378 N N . LEU A 432 ? 0.2759 0.2480 0.2448 0.0753 -0.0687 -0.0455 473 LEU A N 3379 C CA . LEU A 432 ? 0.2859 0.2551 0.2463 0.0789 -0.0661 -0.0431 473 LEU A CA 3380 C C . LEU A 432 ? 0.2820 0.2537 0.2492 0.0778 -0.0656 -0.0440 473 LEU A C 3381 O O . LEU A 432 ? 0.3011 0.2697 0.2637 0.0826 -0.0675 -0.0443 473 LEU A O 3382 C CB . LEU A 432 ? 0.2888 0.2587 0.2442 0.0764 -0.0591 -0.0387 473 LEU A CB 3383 C CG . LEU A 432 ? 0.3018 0.2704 0.2521 0.0780 -0.0547 -0.0357 473 LEU A CG 3384 C CD1 . LEU A 432 ? 0.3417 0.3043 0.2810 0.0855 -0.0570 -0.0353 473 LEU A CD1 3385 C CD2 . LEU A 432 ? 0.3285 0.2987 0.2772 0.0743 -0.0483 -0.0319 473 LEU A CD2 3386 N N . VAL A 433 ? 0.2568 0.2337 0.2344 0.0717 -0.0629 -0.0441 474 VAL A N 3387 C CA . VAL A 433 ? 0.2508 0.2303 0.2353 0.0703 -0.0618 -0.0448 474 VAL A CA 3388 C C . VAL A 433 ? 0.2734 0.2521 0.2630 0.0734 -0.0685 -0.0489 474 VAL A C 3389 O O . VAL A 433 ? 0.2864 0.2640 0.2755 0.0763 -0.0697 -0.0495 474 VAL A O 3390 C CB . VAL A 433 ? 0.2509 0.2361 0.2451 0.0630 -0.0571 -0.0440 474 VAL A CB 3391 C CG1 . VAL A 433 ? 0.2702 0.2583 0.2730 0.0616 -0.0568 -0.0454 474 VAL A CG1 3392 C CG2 . VAL A 433 ? 0.2650 0.2505 0.2534 0.0607 -0.0506 -0.0399 474 VAL A CG2 3393 N N . HIS A 434 ? 0.2688 0.2482 0.2639 0.0728 -0.0730 -0.0518 475 HIS A N 3394 C CA . HIS A 434 ? 0.3024 0.2811 0.3035 0.0759 -0.0800 -0.0562 475 HIS A CA 3395 C C . HIS A 434 ? 0.3062 0.2791 0.2961 0.0834 -0.0840 -0.0567 475 HIS A C 3396 O O . HIS A 434 ? 0.3190 0.2910 0.3105 0.0865 -0.0870 -0.0585 475 HIS A O 3397 C CB . HIS A 434 ? 0.3030 0.2825 0.3110 0.0747 -0.0847 -0.0593 475 HIS A CB 3398 C CG . HIS A 434 ? 0.3373 0.3223 0.3573 0.0677 -0.0813 -0.0591 475 HIS A CG 3399 N ND1 . HIS A 434 ? 0.4648 0.4508 0.4906 0.0654 -0.0833 -0.0605 475 HIS A ND1 3400 C CD2 . HIS A 434 ? 0.3524 0.3418 0.3789 0.0627 -0.0757 -0.0573 475 HIS A CD2 3401 C CE1 . HIS A 434 ? 0.4411 0.4320 0.4766 0.0593 -0.0790 -0.0596 475 HIS A CE1 3402 N NE2 . HIS A 434 ? 0.3583 0.3512 0.3942 0.0576 -0.0744 -0.0578 475 HIS A NE2 3403 N N . ASN A 435 ? 0.3048 0.2736 0.2835 0.0867 -0.0841 -0.0552 476 ASN A N 3404 C CA . ASN A 435 ? 0.3271 0.2897 0.2938 0.0944 -0.0879 -0.0556 476 ASN A CA 3405 C C . ASN A 435 ? 0.3302 0.2913 0.2912 0.0967 -0.0843 -0.0530 476 ASN A C 3406 O O . ASN A 435 ? 0.3543 0.3119 0.3112 0.1023 -0.0885 -0.0545 476 ASN A O 3407 C CB . ASN A 435 ? 0.3305 0.2888 0.2856 0.0975 -0.0878 -0.0541 476 ASN A CB 3408 C CG . ASN A 435 ? 0.3488 0.3069 0.3076 0.0974 -0.0933 -0.0575 476 ASN A CG 3409 O OD1 . ASN A 435 ? 0.3312 0.2925 0.3019 0.0948 -0.0970 -0.0610 476 ASN A OD1 3410 N ND2 . ASN A 435 ? 0.3460 0.3003 0.2948 0.1003 -0.0936 -0.0565 476 ASN A ND2 3411 N N . LEU A 436 ? 0.3078 0.2711 0.2682 0.0927 -0.0769 -0.0490 477 LEU A N 3412 C CA . LEU A 436 ? 0.3109 0.2727 0.2662 0.0947 -0.0731 -0.0462 477 LEU A CA 3413 C C . LEU A 436 ? 0.3057 0.2698 0.2695 0.0942 -0.0750 -0.0484 477 LEU A C 3414 O O . LEU A 436 ? 0.3204 0.2812 0.2792 0.0990 -0.0765 -0.0483 477 LEU A O 3415 C CB . LEU A 436 ? 0.3048 0.2691 0.2596 0.0898 -0.0649 -0.0419 477 LEU A CB 3416 C CG . LEU A 436 ? 0.3193 0.2825 0.2708 0.0910 -0.0607 -0.0391 477 LEU A CG 3417 C CD1 . LEU A 436 ? 0.3301 0.2864 0.2682 0.0989 -0.0621 -0.0376 477 LEU A CD1 3418 C CD2 . LEU A 436 ? 0.3541 0.3204 0.3070 0.0857 -0.0532 -0.0354 477 LEU A CD2 3419 N N . THR A 437 ? 0.2922 0.2619 0.2689 0.0883 -0.0747 -0.0502 478 THR A N 3420 C CA . THR A 437 ? 0.2920 0.2644 0.2780 0.0873 -0.0758 -0.0522 478 THR A CA 3421 C C . THR A 437 ? 0.3103 0.2804 0.2980 0.0925 -0.0839 -0.0564 478 THR A C 3422 O O . THR A 437 ? 0.3121 0.2828 0.3041 0.0938 -0.0853 -0.0577 478 THR A O 3423 C CB . THR A 437 ? 0.2978 0.2769 0.2975 0.0799 -0.0729 -0.0529 478 THR A CB 3424 O OG1 . THR A 437 ? 0.2920 0.2727 0.2980 0.0780 -0.0765 -0.0555 478 THR A OG1 3425 C CG2 . THR A 437 ? 0.3092 0.2907 0.3074 0.0748 -0.0647 -0.0488 478 THR A CG2 3426 N N . LYS A 438 ? 0.3174 0.2846 0.3017 0.0956 -0.0893 -0.0587 479 LYS A N 3427 C CA . LYS A 438 ? 0.3426 0.3067 0.3270 0.1014 -0.0978 -0.0629 479 LYS A CA 3428 C C . LYS A 438 ? 0.3580 0.3161 0.3292 0.1087 -0.0989 -0.0615 479 LYS A C 3429 O O . LYS A 438 ? 0.3724 0.3279 0.3434 0.1138 -0.1052 -0.0647 479 LYS A O 3430 C CB . LYS A 438 ? 0.3495 0.3119 0.3334 0.1031 -0.1035 -0.0658 479 LYS A CB 3431 C CG . LYS A 438 ? 0.3537 0.3217 0.3524 0.0967 -0.1039 -0.0680 479 LYS A CG 3432 C CD . LYS A 438 ? 0.3667 0.3329 0.3651 0.0978 -0.1089 -0.0705 479 LYS A CD 3433 C CE . LYS A 438 ? 0.3789 0.3508 0.3926 0.0911 -0.1082 -0.0720 479 LYS A CE 3434 N NZ . LYS A 438 ? 0.4379 0.4083 0.4523 0.0917 -0.1128 -0.0745 479 LYS A NZ 3435 N N . GLU A 439 ? 0.3562 0.3118 0.3165 0.1095 -0.0929 -0.0570 480 GLU A N 3436 C CA . GLU A 439 ? 0.4027 0.3521 0.3495 0.1165 -0.0929 -0.0549 480 GLU A CA 3437 C C . GLU A 439 ? 0.3987 0.3491 0.3464 0.1154 -0.0879 -0.0521 480 GLU A C 3438 O O . GLU A 439 ? 0.4249 0.3704 0.3625 0.1210 -0.0873 -0.0502 480 GLU A O 3439 C CB . GLU A 439 ? 0.4092 0.3546 0.3429 0.1186 -0.0893 -0.0513 480 GLU A CB 3440 C CG . GLU A 439 ? 0.4983 0.4414 0.4284 0.1208 -0.0942 -0.0537 480 GLU A CG 3441 C CD . GLU A 439 ? 0.6188 0.5571 0.5445 0.1282 -0.1030 -0.0578 480 GLU A CD 3442 O OE1 . GLU A 439 ? 0.6669 0.6005 0.5838 0.1342 -0.1040 -0.0570 480 GLU A OE1 3443 O OE2 . GLU A 439 ? 0.6911 0.6301 0.6219 0.1280 -0.1091 -0.0619 480 GLU A OE2 3444 N N . LEU A 440 ? 0.3637 0.3203 0.3230 0.1084 -0.0837 -0.0517 481 LEU A N 3445 C CA . LEU A 440 ? 0.3516 0.3096 0.3129 0.1070 -0.0789 -0.0494 481 LEU A CA 3446 C C . LEU A 440 ? 0.3535 0.3139 0.3250 0.1070 -0.0830 -0.0529 481 LEU A C 3447 O O . LEU A 440 ? 0.3609 0.3244 0.3423 0.1050 -0.0874 -0.0567 481 LEU A O 3448 C CB . LEU A 440 ? 0.3253 0.2883 0.2924 0.0994 -0.0714 -0.0466 481 LEU A CB 3449 C CG . LEU A 440 ? 0.3346 0.2961 0.2934 0.0985 -0.0667 -0.0430 481 LEU A CG 3450 C CD1 . LEU A 440 ? 0.3131 0.2800 0.2792 0.0908 -0.0602 -0.0410 481 LEU A CD1 3451 C CD2 . LEU A 440 ? 0.3348 0.2904 0.2806 0.1041 -0.0642 -0.0394 481 LEU A CD2 3452 N N . LYS A 441 ? 0.3565 0.3155 0.3262 0.1091 -0.0811 -0.0514 482 LYS A N 3453 C CA . LYS A 441 ? 0.3695 0.3307 0.3486 0.1093 -0.0844 -0.0544 482 LYS A CA 3454 C C . LYS A 441 ? 0.3609 0.3291 0.3537 0.1016 -0.0800 -0.0546 482 LYS A C 3455 O O . LYS A 441 ? 0.3725 0.3425 0.3644 0.0975 -0.0729 -0.0511 482 LYS A O 3456 C CB . LYS A 441 ? 0.3805 0.3373 0.3519 0.1145 -0.0836 -0.0525 482 LYS A CB 3457 C CG . LYS A 441 ? 0.4350 0.3844 0.3926 0.1230 -0.0885 -0.0525 482 LYS A CG 3458 C CD . LYS A 441 ? 0.5556 0.5007 0.5078 0.1288 -0.0898 -0.0519 482 LYS A CD 3459 C CE . LYS A 441 ? 0.5929 0.5367 0.5398 0.1278 -0.0818 -0.0467 482 LYS A CE 3460 N NZ . LYS A 441 ? 0.6888 0.6265 0.6265 0.1352 -0.0833 -0.0454 482 LYS A NZ 3461 N N . SER A 442 ? 0.3377 0.3098 0.3429 0.0997 -0.0839 -0.0585 483 SER A N 3462 C CA . SER A 442 ? 0.3302 0.3086 0.3478 0.0929 -0.0793 -0.0585 483 SER A CA 3463 C C . SER A 442 ? 0.3366 0.3148 0.3541 0.0936 -0.0760 -0.0569 483 SER A C 3464 O O . SER A 442 ? 0.3448 0.3198 0.3599 0.0990 -0.0802 -0.0582 483 SER A O 3465 C CB . SER A 442 ? 0.3266 0.3094 0.3588 0.0906 -0.0837 -0.0630 483 SER A CB 3466 O OG . SER A 442 ? 0.3122 0.3006 0.3552 0.0846 -0.0787 -0.0626 483 SER A OG 3467 N N . PRO A 443 ? 0.3233 0.3048 0.3438 0.0883 -0.0689 -0.0543 484 PRO A N 3468 C CA . PRO A 443 ? 0.3234 0.3049 0.3449 0.0887 -0.0657 -0.0530 484 PRO A CA 3469 C C . PRO A 443 ? 0.3268 0.3134 0.3625 0.0856 -0.0666 -0.0560 484 PRO A C 3470 O O . PRO A 443 ? 0.3202 0.3075 0.3586 0.0852 -0.0638 -0.0553 484 PRO A O 3471 C CB . PRO A 443 ? 0.3184 0.3011 0.3367 0.0843 -0.0579 -0.0491 484 PRO A CB 3472 C CG . PRO A 443 ? 0.3069 0.2936 0.3305 0.0790 -0.0567 -0.0498 484 PRO A CG 3473 C CD . PRO A 443 ? 0.3232 0.3079 0.3449 0.0824 -0.0634 -0.0523 484 PRO A CD 3474 N N . ASP A 444 ? 0.3258 0.3159 0.3710 0.0833 -0.0699 -0.0592 485 ASP A N 3475 C CA . ASP A 444 ? 0.3295 0.3252 0.3894 0.0791 -0.0689 -0.0616 485 ASP A CA 3476 C C . ASP A 444 ? 0.3432 0.3381 0.4084 0.0834 -0.0746 -0.0647 485 ASP A C 3477 O O . ASP A 444 ? 0.3438 0.3352 0.4051 0.0887 -0.0813 -0.0667 485 ASP A O 3478 C CB . ASP A 444 ? 0.3163 0.3159 0.3854 0.0752 -0.0703 -0.0638 485 ASP A CB 3479 C CG . ASP A 444 ? 0.3155 0.3164 0.3808 0.0706 -0.0650 -0.0610 485 ASP A CG 3480 O OD1 . ASP A 444 ? 0.3471 0.3459 0.4029 0.0704 -0.0604 -0.0575 485 ASP A OD1 3481 O OD2 . ASP A 444 ? 0.3160 0.3198 0.3881 0.0671 -0.0653 -0.0623 485 ASP A OD2 3482 N N . GLU A 445 ? 0.3532 0.3514 0.4271 0.0812 -0.0720 -0.0653 486 GLU A N 3483 C CA . GLU A 445 ? 0.3776 0.3765 0.4599 0.0842 -0.0773 -0.0687 486 GLU A CA 3484 C C . GLU A 445 ? 0.3691 0.3702 0.4612 0.0840 -0.0832 -0.0727 486 GLU A C 3485 O O . GLU A 445 ? 0.3764 0.3816 0.4763 0.0790 -0.0809 -0.0732 486 GLU A O 3486 C CB . GLU A 445 ? 0.3801 0.3834 0.4723 0.0804 -0.0726 -0.0688 486 GLU A CB 3487 C CG . GLU A 445 ? 0.4975 0.4979 0.5844 0.0838 -0.0715 -0.0673 486 GLU A CG 3488 C CD . GLU A 445 ? 0.6027 0.6068 0.7024 0.0829 -0.0716 -0.0697 486 GLU A CD 3489 O OE1 . GLU A 445 ? 0.6345 0.6362 0.7344 0.0879 -0.0763 -0.0714 486 GLU A OE1 3490 O OE2 . GLU A 445 ? 0.6428 0.6521 0.7523 0.0773 -0.0670 -0.0700 486 GLU A OE2 3491 N N . GLY A 446 ? 0.3798 0.3781 0.4721 0.0897 -0.0910 -0.0758 487 GLY A N 3492 C CA . GLY A 446 ? 0.3635 0.3638 0.4659 0.0897 -0.0972 -0.0799 487 GLY A CA 3493 C C . GLY A 446 ? 0.3802 0.3765 0.4734 0.0925 -0.1013 -0.0801 487 GLY A C 3494 O O . GLY A 446 ? 0.3931 0.3893 0.4920 0.0944 -0.1082 -0.0839 487 GLY A O 3495 N N . PHE A 447 ? 0.3690 0.3622 0.4485 0.0926 -0.0972 -0.0763 488 PHE A N 3496 C CA . PHE A 447 ? 0.3670 0.3564 0.4370 0.0952 -0.1005 -0.0762 488 PHE A CA 3497 C C . PHE A 447 ? 0.3897 0.3720 0.4429 0.1020 -0.1024 -0.0743 488 PHE A C 3498 O O . PHE A 447 ? 0.3893 0.3680 0.4312 0.1037 -0.1021 -0.0725 488 PHE A O 3499 C CB . PHE A 447 ? 0.3616 0.3533 0.4304 0.0894 -0.0944 -0.0735 488 PHE A CB 3500 C CG . PHE A 447 ? 0.3130 0.3107 0.3970 0.0836 -0.0934 -0.0754 488 PHE A CG 3501 C CD1 . PHE A 447 ? 0.3398 0.3378 0.4283 0.0833 -0.0980 -0.0780 488 PHE A CD1 3502 C CD2 . PHE A 447 ? 0.3260 0.3287 0.4198 0.0785 -0.0877 -0.0747 488 PHE A CD2 3503 C CE1 . PHE A 447 ? 0.3407 0.3442 0.4440 0.0779 -0.0968 -0.0797 488 PHE A CE1 3504 C CE2 . PHE A 447 ? 0.3048 0.3129 0.4127 0.0732 -0.0863 -0.0763 488 PHE A CE2 3505 C CZ . PHE A 447 ? 0.3139 0.3223 0.4266 0.0729 -0.0907 -0.0786 488 PHE A CZ 3506 N N . GLU A 448 ? 0.3925 0.3727 0.4440 0.1061 -0.1041 -0.0746 489 GLU A N 3507 C CA . GLU A 448 ? 0.4213 0.3946 0.4573 0.1131 -0.1058 -0.0728 489 GLU A CA 3508 C C . GLU A 448 ? 0.4300 0.3988 0.4593 0.1185 -0.1135 -0.0753 489 GLU A C 3509 O O . GLU A 448 ? 0.4483 0.4183 0.4865 0.1198 -0.1207 -0.0800 489 GLU A O 3510 C CB . GLU A 448 ? 0.4250 0.3969 0.4625 0.1169 -0.1079 -0.0736 489 GLU A CB 3511 C CG . GLU A 448 ? 0.4273 0.4028 0.4700 0.1122 -0.1003 -0.0709 489 GLU A CG 3512 C CD . GLU A 448 ? 0.4163 0.3991 0.4770 0.1062 -0.0992 -0.0736 489 GLU A CD 3513 O OE1 . GLU A 448 ? 0.4399 0.4258 0.5050 0.1022 -0.0930 -0.0717 489 GLU A OE1 3514 O OE2 . GLU A 448 ? 0.4273 0.4126 0.4976 0.1056 -0.1045 -0.0775 489 GLU A OE2 3515 N N . GLY A 449 ? 0.4294 0.3930 0.4433 0.1217 -0.1121 -0.0724 490 GLY A N 3516 C CA . GLY A 449 ? 0.4331 0.3918 0.4388 0.1273 -0.1190 -0.0745 490 GLY A CA 3517 C C . GLY A 449 ? 0.4231 0.3844 0.4334 0.1235 -0.1200 -0.0760 490 GLY A C 3518 O O . GLY A 449 ? 0.4396 0.3969 0.4432 0.1278 -0.1256 -0.0780 490 GLY A O 3519 N N . LYS A 450 ? 0.3949 0.3626 0.4163 0.1156 -0.1146 -0.0752 491 LYS A N 3520 C CA . LYS A 450 ? 0.3809 0.3511 0.4071 0.1116 -0.1150 -0.0764 491 LYS A CA 3521 C C . LYS A 450 ? 0.3594 0.3292 0.3766 0.1084 -0.1073 -0.0715 491 LYS A C 3522 O O . LYS A 450 ? 0.3674 0.3366 0.3788 0.1078 -0.1012 -0.0677 491 LYS A O 3523 C CB . LYS A 450 ? 0.3737 0.3511 0.4185 0.1049 -0.1139 -0.0786 491 LYS A CB 3524 C CG . LYS A 450 ? 0.4067 0.3856 0.4633 0.1072 -0.1207 -0.0834 491 LYS A CG 3525 C CD . LYS A 450 ? 0.4773 0.4519 0.5307 0.1134 -0.1305 -0.0875 491 LYS A CD 3526 C CE . LYS A 450 ? 0.5312 0.5076 0.5981 0.1153 -0.1379 -0.0927 491 LYS A CE 3527 N NZ . LYS A 450 ? 0.5717 0.5557 0.6573 0.1077 -0.1347 -0.0938 491 LYS A NZ 3528 N N . SER A 451 ? 0.3503 0.3206 0.3671 0.1065 -0.1078 -0.0719 492 SER A N 3529 C CA . SER A 451 ? 0.3340 0.3041 0.3431 0.1033 -0.1009 -0.0675 492 SER A CA 3530 C C . SER A 451 ? 0.3286 0.3050 0.3477 0.0953 -0.0937 -0.0657 492 SER A C 3531 O O . SER A 451 ? 0.3072 0.2885 0.3401 0.0915 -0.0944 -0.0680 492 SER A O 3532 C CB . SER A 451 ? 0.3453 0.3139 0.3513 0.1038 -0.1041 -0.0688 492 SER A CB 3533 O OG . SER A 451 ? 0.3566 0.3304 0.3767 0.0983 -0.1050 -0.0713 492 SER A OG 3534 N N . LEU A 452 ? 0.3286 0.3047 0.3404 0.0929 -0.0869 -0.0614 493 LEU A N 3535 C CA . LEU A 452 ? 0.3046 0.2862 0.3237 0.0855 -0.0800 -0.0593 493 LEU A CA 3536 C C . LEU A 452 ? 0.3019 0.2869 0.3299 0.0813 -0.0814 -0.0614 493 LEU A C 3537 O O . LEU A 452 ? 0.2974 0.2877 0.3367 0.0757 -0.0784 -0.0618 493 LEU A O 3538 C CB . LEU A 452 ? 0.2954 0.2751 0.3037 0.0848 -0.0735 -0.0546 493 LEU A CB 3539 C CG . LEU A 452 ? 0.3269 0.3114 0.3406 0.0776 -0.0664 -0.0523 493 LEU A CG 3540 C CD1 . LEU A 452 ? 0.3076 0.2962 0.3310 0.0743 -0.0636 -0.0528 493 LEU A CD1 3541 C CD2 . LEU A 452 ? 0.2843 0.2664 0.2872 0.0778 -0.0612 -0.0480 493 LEU A CD2 3542 N N . TYR A 453 ? 0.2870 0.2691 0.3097 0.0841 -0.0857 -0.0625 494 TYR A N 3543 C CA . TYR A 453 ? 0.2926 0.2776 0.3242 0.0804 -0.0874 -0.0646 494 TYR A CA 3544 C C . TYR A 453 ? 0.2822 0.2711 0.3292 0.0787 -0.0911 -0.0685 494 TYR A C 3545 O O . TYR A 453 ? 0.2959 0.2895 0.3541 0.0732 -0.0888 -0.0690 494 TYR A O 3546 C CB . TYR A 453 ? 0.2945 0.2753 0.3189 0.0845 -0.0929 -0.0661 494 TYR A CB 3547 C CG . TYR A 453 ? 0.2941 0.2776 0.3273 0.0806 -0.0946 -0.0680 494 TYR A CG 3548 C CD1 . TYR A 453 ? 0.2818 0.2662 0.3119 0.0769 -0.0900 -0.0653 494 TYR A CD1 3549 C CD2 . TYR A 453 ? 0.3169 0.3018 0.3614 0.0810 -0.1008 -0.0725 494 TYR A CD2 3550 C CE1 . TYR A 453 ? 0.2911 0.2778 0.3291 0.0735 -0.0914 -0.0669 494 TYR A CE1 3551 C CE2 . TYR A 453 ? 0.2871 0.2742 0.3400 0.0776 -0.1022 -0.0741 494 TYR A CE2 3552 C CZ . TYR A 453 ? 0.2955 0.2833 0.3447 0.0739 -0.0975 -0.0712 494 TYR A CZ 3553 O OH . TYR A 453 ? 0.3279 0.3177 0.3855 0.0706 -0.0986 -0.0726 494 TYR A OH 3554 N N . GLU A 454 ? 0.3060 0.2926 0.3535 0.0838 -0.0969 -0.0713 495 GLU A N 3555 C CA . GLU A 454 ? 0.3060 0.2961 0.3685 0.0827 -0.1010 -0.0753 495 GLU A CA 3556 C C . GLU A 454 ? 0.2967 0.2922 0.3695 0.0774 -0.0948 -0.0740 495 GLU A C 3557 O O . GLU A 454 ? 0.3005 0.3006 0.3869 0.0730 -0.0943 -0.0757 495 GLU A O 3558 C CB . GLU A 454 ? 0.3391 0.3254 0.3995 0.0897 -0.1087 -0.0786 495 GLU A CB 3559 C CG . GLU A 454 ? 0.3746 0.3648 0.4518 0.0885 -0.1128 -0.0827 495 GLU A CG 3560 C CD . GLU A 454 ? 0.4663 0.4527 0.5423 0.0956 -0.1216 -0.0867 495 GLU A CD 3561 O OE1 . GLU A 454 ? 0.4878 0.4688 0.5524 0.1011 -0.1266 -0.0875 495 GLU A OE1 3562 O OE2 . GLU A 454 ? 0.4885 0.4774 0.5749 0.0957 -0.1236 -0.0889 495 GLU A OE2 3563 N N . SER A 455 ? 0.2849 0.2796 0.3509 0.0777 -0.0900 -0.0711 496 SER A N 3564 C CA . SER A 455 ? 0.2843 0.2838 0.3594 0.0731 -0.0845 -0.0701 496 SER A CA 3565 C C . SER A 455 ? 0.2854 0.2889 0.3644 0.0664 -0.0780 -0.0679 496 SER A C 3566 O O . SER A 455 ? 0.2742 0.2824 0.3655 0.0619 -0.0755 -0.0687 496 SER A O 3567 C CB . SER A 455 ? 0.2978 0.2955 0.3654 0.0751 -0.0811 -0.0677 496 SER A CB 3568 O OG . SER A 455 ? 0.3253 0.3199 0.3795 0.0758 -0.0771 -0.0638 496 SER A OG 3569 N N . TRP A 456 ? 0.2694 0.2706 0.3376 0.0661 -0.0753 -0.0650 497 TRP A N 3570 C CA . TRP A 456 ? 0.2725 0.2768 0.3426 0.0603 -0.0695 -0.0627 497 TRP A CA 3571 C C . TRP A 456 ? 0.2649 0.2722 0.3462 0.0571 -0.0715 -0.0650 497 TRP A C 3572 O O . TRP A 456 ? 0.2720 0.2835 0.3618 0.0519 -0.0670 -0.0644 497 TRP A O 3573 C CB . TRP A 456 ? 0.2657 0.2663 0.3216 0.0616 -0.0676 -0.0597 497 TRP A CB 3574 C CG . TRP A 456 ? 0.2656 0.2685 0.3211 0.0563 -0.0620 -0.0571 497 TRP A CG 3575 C CD1 . TRP A 456 ? 0.2682 0.2756 0.3314 0.0507 -0.0567 -0.0562 497 TRP A CD1 3576 C CD2 . TRP A 456 ? 0.2909 0.2915 0.3376 0.0565 -0.0614 -0.0552 497 TRP A CD2 3577 N NE1 . TRP A 456 ? 0.2937 0.3016 0.3528 0.0474 -0.0529 -0.0537 497 TRP A NE1 3578 C CE2 . TRP A 456 ? 0.2764 0.2803 0.3259 0.0508 -0.0557 -0.0531 497 TRP A CE2 3579 C CE3 . TRP A 456 ? 0.2865 0.2823 0.3227 0.0611 -0.0650 -0.0550 497 TRP A CE3 3580 C CZ2 . TRP A 456 ? 0.2773 0.2800 0.3199 0.0495 -0.0538 -0.0510 497 TRP A CZ2 3581 C CZ3 . TRP A 456 ? 0.2975 0.2922 0.3271 0.0598 -0.0628 -0.0528 497 TRP A CZ3 3582 C CH2 . TRP A 456 ? 0.2829 0.2812 0.3161 0.0539 -0.0573 -0.0508 497 TRP A CH2 3583 N N . THR A 457 ? 0.2813 0.2861 0.3624 0.0605 -0.0782 -0.0676 498 THR A N 3584 C CA . THR A 457 ? 0.2892 0.2964 0.3811 0.0578 -0.0805 -0.0699 498 THR A CA 3585 C C . THR A 457 ? 0.2995 0.3110 0.4077 0.0556 -0.0811 -0.0725 498 THR A C 3586 O O . THR A 457 ? 0.2870 0.3024 0.4061 0.0510 -0.0785 -0.0727 498 THR A O 3587 C CB . THR A 457 ? 0.3055 0.3085 0.3934 0.0627 -0.0883 -0.0725 498 THR A CB 3588 O OG1 . THR A 457 ? 0.2959 0.2952 0.3693 0.0643 -0.0870 -0.0699 498 THR A OG1 3589 C CG2 . THR A 457 ? 0.3227 0.3281 0.4235 0.0602 -0.0915 -0.0754 498 THR A CG2 3590 N N . LYS A 458 ? 0.3111 0.3220 0.4211 0.0591 -0.0841 -0.0743 499 LYS A N 3591 C CA . LYS A 458 ? 0.3268 0.3419 0.4524 0.0573 -0.0847 -0.0768 499 LYS A CA 3592 C C . LYS A 458 ? 0.3207 0.3401 0.4511 0.0517 -0.0761 -0.0741 499 LYS A C 3593 O O . LYS A 458 ? 0.3330 0.3565 0.4764 0.0478 -0.0741 -0.0749 499 LYS A O 3594 C CB . LYS A 458 ? 0.3388 0.3520 0.4642 0.0626 -0.0899 -0.0792 499 LYS A CB 3595 C CG . LYS A 458 ? 0.3908 0.4082 0.5316 0.0609 -0.0897 -0.0815 499 LYS A CG 3596 C CD . LYS A 458 ? 0.4797 0.5001 0.6360 0.0588 -0.0931 -0.0846 499 LYS A CD 3597 C CE . LYS A 458 ? 0.5324 0.5563 0.7044 0.0588 -0.0950 -0.0877 499 LYS A CE 3598 N NZ . LYS A 458 ? 0.5787 0.6042 0.7651 0.0583 -0.1005 -0.0915 499 LYS A NZ 3599 N N . LYS A 459 ? 0.3025 0.3208 0.4224 0.0516 -0.0712 -0.0709 500 LYS A N 3600 C CA . LYS A 459 ? 0.3021 0.3240 0.4249 0.0469 -0.0633 -0.0685 500 LYS A CA 3601 C C . LYS A 459 ? 0.3108 0.3345 0.4330 0.0419 -0.0578 -0.0659 500 LYS A C 3602 O O . LYS A 459 ? 0.3165 0.3438 0.4451 0.0376 -0.0521 -0.0649 500 LYS A O 3603 C CB . LYS A 459 ? 0.2995 0.3192 0.4114 0.0489 -0.0606 -0.0662 500 LYS A CB 3604 C CG . LYS A 459 ? 0.2835 0.3022 0.3979 0.0530 -0.0645 -0.0684 500 LYS A CG 3605 C CD . LYS A 459 ? 0.2644 0.2807 0.3678 0.0548 -0.0612 -0.0658 500 LYS A CD 3606 C CE . LYS A 459 ? 0.3032 0.3190 0.4102 0.0583 -0.0641 -0.0677 500 LYS A CE 3607 N NZ . LYS A 459 ? 0.3136 0.3275 0.4116 0.0595 -0.0602 -0.0650 500 LYS A NZ 3608 N N . SER A 460 ? 0.3068 0.3278 0.4206 0.0426 -0.0593 -0.0649 501 SER A N 3609 C CA . SER A 460 ? 0.3098 0.3319 0.4211 0.0384 -0.0543 -0.0623 501 SER A CA 3610 C C . SER A 460 ? 0.3167 0.3375 0.4289 0.0386 -0.0583 -0.0633 501 SER A C 3611 O O . SER A 460 ? 0.3018 0.3196 0.4033 0.0397 -0.0587 -0.0617 501 SER A O 3612 C CB . SER A 460 ? 0.3128 0.3326 0.4101 0.0385 -0.0503 -0.0588 501 SER A CB 3613 O OG . SER A 460 ? 0.3400 0.3618 0.4368 0.0339 -0.0447 -0.0564 501 SER A OG 3614 N N . PRO A 461 ? 0.3155 0.3385 0.4410 0.0377 -0.0613 -0.0661 502 PRO A N 3615 C CA . PRO A 461 ? 0.3295 0.3510 0.4566 0.0383 -0.0658 -0.0675 502 PRO A CA 3616 C C . PRO A 461 ? 0.3381 0.3601 0.4619 0.0343 -0.0611 -0.0646 502 PRO A C 3617 O O . PRO A 461 ? 0.3269 0.3518 0.4535 0.0301 -0.0546 -0.0624 502 PRO A O 3618 C CB . PRO A 461 ? 0.3298 0.3542 0.4741 0.0373 -0.0689 -0.0709 502 PRO A CB 3619 C CG . PRO A 461 ? 0.3306 0.3589 0.4826 0.0345 -0.0635 -0.0701 502 PRO A CG 3620 C CD . PRO A 461 ? 0.3218 0.3484 0.4615 0.0365 -0.0611 -0.0682 502 PRO A CD 3621 N N . SER A 462 ? 0.3563 0.3753 0.4738 0.0360 -0.0645 -0.0648 503 SER A N 3622 C CA . SER A 462 ? 0.4072 0.4263 0.5225 0.0327 -0.0613 -0.0625 503 SER A CA 3623 C C . SER A 462 ? 0.4314 0.4542 0.5615 0.0284 -0.0593 -0.0631 503 SER A C 3624 O O . SER A 462 ? 0.4432 0.4669 0.5849 0.0293 -0.0637 -0.0663 503 SER A O 3625 C CB . SER A 462 ? 0.4004 0.4157 0.5092 0.0358 -0.0668 -0.0636 503 SER A CB 3626 O OG . SER A 462 ? 0.4544 0.4703 0.5654 0.0325 -0.0648 -0.0623 503 SER A OG 3627 N N . PRO A 463 ? 0.4565 0.4812 0.5864 0.0240 -0.0527 -0.0601 504 PRO A N 3628 C CA . PRO A 463 ? 0.4807 0.5084 0.6238 0.0201 -0.0503 -0.0602 504 PRO A CA 3629 C C . PRO A 463 ? 0.5118 0.5379 0.6590 0.0205 -0.0550 -0.0617 504 PRO A C 3630 O O . PRO A 463 ? 0.5194 0.5476 0.6805 0.0185 -0.0556 -0.0631 504 PRO A O 3631 C CB . PRO A 463 ? 0.4738 0.5028 0.6119 0.0161 -0.0424 -0.0562 504 PRO A CB 3632 C CG . PRO A 463 ? 0.4677 0.4938 0.5897 0.0180 -0.0421 -0.0543 504 PRO A CG 3633 C CD . PRO A 463 ? 0.4588 0.4830 0.5767 0.0226 -0.0471 -0.0564 504 PRO A CD 3634 N N . GLU A 464 ? 0.5369 0.5594 0.6728 0.0230 -0.0583 -0.0615 505 GLU A N 3635 C CA . GLU A 464 ? 0.5569 0.5777 0.6960 0.0233 -0.0625 -0.0628 505 GLU A CA 3636 C C . GLU A 464 ? 0.5627 0.5812 0.7049 0.0279 -0.0713 -0.0672 505 GLU A C 3637 O O . GLU A 464 ? 0.5729 0.5912 0.7243 0.0277 -0.0753 -0.0695 505 GLU A O 3638 C CB . GLU A 464 ? 0.5640 0.5822 0.6906 0.0230 -0.0609 -0.0601 505 GLU A CB 3639 C CG . GLU A 464 ? 0.6063 0.6264 0.7298 0.0185 -0.0527 -0.0560 505 GLU A CG 3640 C CD . GLU A 464 ? 0.6524 0.6718 0.7626 0.0192 -0.0492 -0.0534 505 GLU A CD 3641 O OE1 . GLU A 464 ? 0.6765 0.6977 0.7845 0.0160 -0.0427 -0.0505 505 GLU A OE1 3642 O OE2 . GLU A 464 ? 0.6822 0.6989 0.7838 0.0233 -0.0529 -0.0544 505 GLU A OE2 3643 N N . PHE A 465 ? 0.5533 0.5699 0.6880 0.0322 -0.0746 -0.0685 506 PHE A N 3644 C CA . PHE A 465 ? 0.5626 0.5759 0.6964 0.0373 -0.0832 -0.0723 506 PHE A CA 3645 C C . PHE A 465 ? 0.5526 0.5662 0.6902 0.0406 -0.0870 -0.0751 506 PHE A C 3646 O O . PHE A 465 ? 0.5430 0.5568 0.6740 0.0415 -0.0841 -0.0736 506 PHE A O 3647 C CB . PHE A 465 ? 0.5786 0.5873 0.6958 0.0409 -0.0852 -0.0713 506 PHE A CB 3648 C CG . PHE A 465 ? 0.6041 0.6121 0.7175 0.0383 -0.0826 -0.0689 506 PHE A CG 3649 C CD1 . PHE A 465 ? 0.6219 0.6303 0.7258 0.0358 -0.0758 -0.0646 506 PHE A CD1 3650 C CD2 . PHE A 465 ? 0.6295 0.6363 0.7489 0.0385 -0.0872 -0.0712 506 PHE A CD2 3651 C CE1 . PHE A 465 ? 0.6262 0.6339 0.7265 0.0336 -0.0736 -0.0625 506 PHE A CE1 3652 C CE2 . PHE A 465 ? 0.6407 0.6467 0.7567 0.0361 -0.0849 -0.0690 506 PHE A CE2 3653 C CZ . PHE A 465 ? 0.6388 0.6452 0.7449 0.0337 -0.0780 -0.0646 506 PHE A CZ 3654 N N . SER A 466 ? 0.5447 0.5582 0.6933 0.0425 -0.0937 -0.0794 507 SER A N 3655 C CA . SER A 466 ? 0.5318 0.5455 0.6852 0.0459 -0.0984 -0.0826 507 SER A CA 3656 C C . SER A 466 ? 0.5048 0.5135 0.6421 0.0520 -0.1026 -0.0831 507 SER A C 3657 O O . SER A 466 ? 0.5169 0.5217 0.6452 0.0550 -0.1064 -0.0836 507 SER A O 3658 C CB . SER A 466 ? 0.5433 0.5578 0.7127 0.0466 -0.1052 -0.0873 507 SER A CB 3659 O OG . SER A 466 ? 0.5736 0.5931 0.7595 0.0414 -0.1007 -0.0869 507 SER A OG 3660 N N . GLY A 467 ? 0.4599 0.4688 0.5934 0.0540 -0.1016 -0.0826 508 GLY A N 3661 C CA . GLY A 467 ? 0.4158 0.4199 0.5360 0.0604 -0.1062 -0.0835 508 GLY A CA 3662 C C . GLY A 467 ? 0.3887 0.3903 0.4919 0.0609 -0.1012 -0.0792 508 GLY A C 3663 O O . GLY A 467 ? 0.3839 0.3809 0.4741 0.0662 -0.1043 -0.0793 508 GLY A O 3664 N N A MET A 468 ? 0.3692 0.3736 0.4725 0.0555 -0.0937 -0.0756 509 MET A N 3665 N N B MET A 468 ? 0.3681 0.3726 0.4716 0.0554 -0.0937 -0.0756 509 MET A N 3666 C CA A MET A 468 ? 0.3595 0.3622 0.4485 0.0551 -0.0881 -0.0713 509 MET A CA 3667 C CA B MET A 468 ? 0.3552 0.3581 0.4446 0.0547 -0.0879 -0.0712 509 MET A CA 3668 C C A MET A 468 ? 0.3430 0.3496 0.4344 0.0509 -0.0804 -0.0683 509 MET A C 3669 C C B MET A 468 ? 0.3404 0.3469 0.4318 0.0509 -0.0805 -0.0684 509 MET A C 3670 O O A MET A 468 ? 0.3277 0.3384 0.4317 0.0469 -0.0781 -0.0689 509 MET A O 3671 O O B MET A 468 ? 0.3289 0.3396 0.4331 0.0472 -0.0783 -0.0691 509 MET A O 3672 C CB A MET A 468 ? 0.3604 0.3622 0.4448 0.0531 -0.0864 -0.0695 509 MET A CB 3673 C CB B MET A 468 ? 0.3528 0.3557 0.4403 0.0517 -0.0857 -0.0695 509 MET A CB 3674 C CG A MET A 468 ? 0.4126 0.4099 0.4913 0.0579 -0.0934 -0.0719 509 MET A CG 3675 C CG B MET A 468 ? 0.3833 0.3834 0.4723 0.0544 -0.0928 -0.0726 509 MET A CG 3676 S SD A MET A 468 ? 0.4764 0.4735 0.5534 0.0546 -0.0913 -0.0701 509 MET A SD 3677 S SD B MET A 468 ? 0.4383 0.4318 0.5101 0.0619 -0.0981 -0.0733 509 MET A SD 3678 C CE A MET A 468 ? 0.4666 0.4580 0.5363 0.0612 -0.1003 -0.0736 509 MET A CE 3679 C CE B MET A 468 ? 0.4456 0.4380 0.5049 0.0597 -0.0916 -0.0684 509 MET A CE 3680 N N . PRO A 469 ? 0.3261 0.3310 0.4053 0.0518 -0.0764 -0.0652 510 PRO A N 3681 C CA . PRO A 469 ? 0.3141 0.3220 0.3944 0.0482 -0.0694 -0.0625 510 PRO A CA 3682 C C . PRO A 469 ? 0.3110 0.3210 0.3901 0.0431 -0.0631 -0.0594 510 PRO A C 3683 O O . PRO A 469 ? 0.3085 0.3167 0.3824 0.0430 -0.0638 -0.0585 510 PRO A O 3684 C CB . PRO A 469 ? 0.3111 0.3156 0.3785 0.0521 -0.0688 -0.0608 510 PRO A CB 3685 C CG . PRO A 469 ? 0.3164 0.3166 0.3727 0.0552 -0.0715 -0.0601 510 PRO A CG 3686 C CD . PRO A 469 ? 0.3326 0.3325 0.3970 0.0570 -0.0787 -0.0643 510 PRO A CD 3687 N N . ARG A 470 ? 0.2880 0.3014 0.3712 0.0392 -0.0572 -0.0577 511 ARG A N 3688 C CA . ARG A 470 ? 0.2755 0.2907 0.3569 0.0345 -0.0511 -0.0547 511 ARG A CA 3689 C C . ARG A 470 ? 0.2636 0.2761 0.3312 0.0358 -0.0486 -0.0518 511 ARG A C 3690 O O . ARG A 470 ? 0.2683 0.2796 0.3303 0.0379 -0.0477 -0.0510 511 ARG A O 3691 C CB . ARG A 470 ? 0.2893 0.3085 0.3781 0.0307 -0.0457 -0.0540 511 ARG A CB 3692 C CG . ARG A 470 ? 0.3118 0.3328 0.3988 0.0262 -0.0393 -0.0510 511 ARG A CG 3693 C CD . ARG A 470 ? 0.3517 0.3760 0.4445 0.0233 -0.0342 -0.0505 511 ARG A CD 3694 N NE . ARG A 470 ? 0.3442 0.3714 0.4508 0.0216 -0.0347 -0.0525 511 ARG A NE 3695 C CZ . ARG A 470 ? 0.4122 0.4415 0.5255 0.0180 -0.0319 -0.0519 511 ARG A CZ 3696 N NH1 . ARG A 470 ? 0.4129 0.4416 0.5199 0.0157 -0.0286 -0.0493 511 ARG A NH1 3697 N NH2 . ARG A 470 ? 0.4360 0.4680 0.5628 0.0167 -0.0322 -0.0537 511 ARG A NH2 3698 N N . ILE A 471 ? 0.2474 0.2590 0.3099 0.0343 -0.0474 -0.0500 512 ILE A N 3699 C CA . ILE A 471 ? 0.2606 0.2705 0.3116 0.0344 -0.0438 -0.0468 512 ILE A CA 3700 C C . ILE A 471 ? 0.2566 0.2689 0.3092 0.0295 -0.0390 -0.0448 512 ILE A C 3701 O O . ILE A 471 ? 0.2726 0.2854 0.3296 0.0279 -0.0403 -0.0454 512 ILE A O 3702 C CB . ILE A 471 ? 0.2569 0.2626 0.2983 0.0384 -0.0474 -0.0466 512 ILE A CB 3703 C CG1 . ILE A 471 ? 0.2760 0.2785 0.3144 0.0440 -0.0526 -0.0486 512 ILE A CG1 3704 C CG2 . ILE A 471 ? 0.2721 0.2763 0.3027 0.0380 -0.0432 -0.0431 512 ILE A CG2 3705 C CD1 . ILE A 471 ? 0.3249 0.3228 0.3529 0.0485 -0.0562 -0.0484 512 ILE A CD1 3706 N N . SER A 472 ? 0.2553 0.2688 0.3047 0.0272 -0.0337 -0.0425 513 SER A N 3707 C CA . SER A 472 ? 0.2480 0.2639 0.2989 0.0227 -0.0289 -0.0407 513 SER A CA 3708 C C . SER A 472 ? 0.2407 0.2545 0.2818 0.0226 -0.0276 -0.0382 513 SER A C 3709 O O . SER A 472 ? 0.2378 0.2489 0.2710 0.0257 -0.0289 -0.0375 513 SER A O 3710 C CB . SER A 472 ? 0.2594 0.2776 0.3122 0.0204 -0.0241 -0.0399 513 SER A CB 3711 O OG . SER A 472 ? 0.3052 0.3255 0.3677 0.0203 -0.0251 -0.0422 513 SER A OG 3712 N N . LYS A 473 ? 0.2308 0.2461 0.2730 0.0190 -0.0246 -0.0369 514 LYS A N 3713 C CA A LYS A 473 ? 0.2304 0.2446 0.2646 0.0181 -0.0224 -0.0344 514 LYS A CA 3714 C CA B LYS A 473 ? 0.2075 0.2215 0.2414 0.0184 -0.0227 -0.0345 514 LYS A CA 3715 C C . LYS A 473 ? 0.2116 0.2259 0.2407 0.0180 -0.0189 -0.0329 514 LYS A C 3716 O O . LYS A 473 ? 0.2154 0.2315 0.2482 0.0171 -0.0170 -0.0335 514 LYS A O 3717 C CB A LYS A 473 ? 0.2438 0.2598 0.2811 0.0141 -0.0195 -0.0333 514 LYS A CB 3718 C CB B LYS A 473 ? 0.2067 0.2220 0.2431 0.0149 -0.0207 -0.0335 514 LYS A CB 3719 C CG A LYS A 473 ? 0.2743 0.2909 0.3195 0.0133 -0.0219 -0.0348 514 LYS A CG 3720 C CG B LYS A 473 ? 0.1257 0.1439 0.1666 0.0113 -0.0159 -0.0329 514 LYS A CG 3721 C CD A LYS A 473 ? 0.2960 0.3139 0.3429 0.0096 -0.0186 -0.0332 514 LYS A CD 3722 C CD B LYS A 473 ? 0.1715 0.1905 0.2135 0.0081 -0.0137 -0.0315 514 LYS A CD 3723 C CE A LYS A 473 ? 0.2882 0.3087 0.3392 0.0065 -0.0137 -0.0325 514 LYS A CE 3724 C CE B LYS A 473 ? 0.1923 0.2115 0.2419 0.0076 -0.0162 -0.0327 514 LYS A CE 3725 N NZ A LYS A 473 ? 0.2696 0.2919 0.3318 0.0056 -0.0142 -0.0343 514 LYS A NZ 3726 N NZ B LYS A 473 ? 0.2007 0.2216 0.2599 0.0079 -0.0173 -0.0349 514 LYS A NZ 3727 N N . LEU A 474 ? 0.2025 0.2152 0.2236 0.0185 -0.0179 -0.0309 515 LEU A N 3728 C CA . LEU A 474 ? 0.2096 0.2225 0.2268 0.0178 -0.0143 -0.0294 515 LEU A CA 3729 C C . LEU A 474 ? 0.2086 0.2240 0.2279 0.0137 -0.0105 -0.0286 515 LEU A C 3730 O O . LEU A 474 ? 0.2276 0.2433 0.2472 0.0118 -0.0102 -0.0280 515 LEU A O 3731 C CB . LEU A 474 ? 0.1880 0.1985 0.1969 0.0195 -0.0142 -0.0275 515 LEU A CB 3732 C CG . LEU A 474 ? 0.1865 0.1941 0.1913 0.0241 -0.0170 -0.0277 515 LEU A CG 3733 C CD1 . LEU A 474 ? 0.2268 0.2317 0.2239 0.0260 -0.0172 -0.0257 515 LEU A CD1 3734 C CD2 . LEU A 474 ? 0.2085 0.2161 0.2135 0.0252 -0.0154 -0.0276 515 LEU A CD2 3735 N N . GLY A 475 ? 0.2164 0.2332 0.2369 0.0125 -0.0075 -0.0286 516 GLY A N 3736 C CA . GLY A 475 ? 0.2054 0.2239 0.2259 0.0092 -0.0036 -0.0278 516 GLY A CA 3737 C C . GLY A 475 ? 0.2162 0.2336 0.2302 0.0092 -0.0020 -0.0262 516 GLY A C 3738 O O . GLY A 475 ? 0.2117 0.2274 0.2210 0.0106 -0.0033 -0.0250 516 GLY A O 3739 N N . SER A 476 ? 0.1931 0.2116 0.2072 0.0078 0.0010 -0.0262 517 SER A N 3740 C CA . SER A 476 ? 0.1967 0.2142 0.2059 0.0081 0.0023 -0.0250 517 SER A CA 3741 C C . SER A 476 ? 0.1893 0.2076 0.2003 0.0079 0.0044 -0.0258 517 SER A C 3742 O O . SER A 476 ? 0.1870 0.2062 0.2025 0.0085 0.0041 -0.0272 517 SER A O 3743 C CB . SER A 476 ? 0.1931 0.2108 0.1988 0.0060 0.0037 -0.0237 517 SER A CB 3744 O OG . SER A 476 ? 0.2141 0.2306 0.2157 0.0066 0.0043 -0.0225 517 SER A OG 3745 N N . GLY A 477 ? 0.1733 0.1914 0.1813 0.0071 0.0063 -0.0250 518 GLY A N 3746 C CA . GLY A 477 ? 0.1784 0.1967 0.1878 0.0071 0.0080 -0.0257 518 GLY A CA 3747 C C . GLY A 477 ? 0.1721 0.1886 0.1807 0.0101 0.0068 -0.0252 518 GLY A C 3748 O O . GLY A 477 ? 0.1795 0.1961 0.1905 0.0108 0.0076 -0.0260 518 GLY A O 3749 N N . ASN A 478 ? 0.1613 0.1759 0.1664 0.0120 0.0052 -0.0238 519 ASN A N 3750 C CA . ASN A 478 ? 0.1761 0.1885 0.1793 0.0150 0.0047 -0.0228 519 ASN A CA 3751 C C . ASN A 478 ? 0.1802 0.1908 0.1788 0.0162 0.0042 -0.0207 519 ASN A C 3752 O O . ASN A 478 ? 0.1682 0.1793 0.1653 0.0148 0.0037 -0.0203 519 ASN A O 3753 C CB . ASN A 478 ? 0.1729 0.1845 0.1780 0.0177 0.0027 -0.0237 519 ASN A CB 3754 C CG . ASN A 478 ? 0.1950 0.2053 0.2004 0.0196 0.0037 -0.0235 519 ASN A CG 3755 O OD1 . ASN A 478 ? 0.1923 0.2005 0.1945 0.0213 0.0044 -0.0217 519 ASN A OD1 3756 N ND2 . ASN A 478 ? 0.1781 0.1898 0.1880 0.0190 0.0043 -0.0251 519 ASN A ND2 3757 N N . ASP A 479 ? 0.1617 0.1699 0.1580 0.0190 0.0043 -0.0194 520 ASP A N 3758 C CA . ASP A 479 ? 0.1786 0.1851 0.1711 0.0199 0.0050 -0.0172 520 ASP A CA 3759 C C . ASP A 479 ? 0.1762 0.1815 0.1650 0.0216 0.0028 -0.0164 520 ASP A C 3760 O O . ASP A 479 ? 0.1832 0.1873 0.1689 0.0221 0.0034 -0.0147 520 ASP A O 3761 C CB . ASP A 479 ? 0.1890 0.1933 0.1805 0.0226 0.0064 -0.0156 520 ASP A CB 3762 C CG . ASP A 479 ? 0.2137 0.2189 0.2085 0.0206 0.0091 -0.0158 520 ASP A CG 3763 O OD1 . ASP A 479 ? 0.1848 0.1916 0.1805 0.0178 0.0100 -0.0159 520 ASP A OD1 3764 O OD2 . ASP A 479 ? 0.2080 0.2123 0.2044 0.0220 0.0099 -0.0159 520 ASP A OD2 3765 N N . PHE A 480 ? 0.1711 0.1765 0.1606 0.0224 0.0003 -0.0179 521 PHE A N 3766 C CA . PHE A 480 ? 0.1639 0.1682 0.1503 0.0237 -0.0020 -0.0175 521 PHE A CA 3767 C C . PHE A 480 ? 0.1720 0.1779 0.1585 0.0206 -0.0018 -0.0174 521 PHE A C 3768 O O . PHE A 480 ? 0.1815 0.1864 0.1654 0.0215 -0.0034 -0.0168 521 PHE A O 3769 C CB . PHE A 480 ? 0.1880 0.1918 0.1757 0.0255 -0.0053 -0.0193 521 PHE A CB 3770 C CG . PHE A 480 ? 0.1600 0.1667 0.1537 0.0226 -0.0054 -0.0214 521 PHE A CG 3771 C CD1 . PHE A 480 ? 0.1893 0.1978 0.1849 0.0197 -0.0057 -0.0220 521 PHE A CD1 3772 C CD2 . PHE A 480 ? 0.1730 0.1805 0.1704 0.0229 -0.0050 -0.0227 521 PHE A CD2 3773 C CE1 . PHE A 480 ? 0.1886 0.1997 0.1899 0.0172 -0.0051 -0.0236 521 PHE A CE1 3774 C CE2 . PHE A 480 ? 0.1849 0.1951 0.1880 0.0204 -0.0047 -0.0245 521 PHE A CE2 3775 C CZ . PHE A 480 ? 0.1927 0.2047 0.1977 0.0175 -0.0045 -0.0249 521 PHE A CZ 3776 N N . GLU A 481 ? 0.1591 0.1674 0.1486 0.0171 0.0001 -0.0180 522 GLU A N 3777 C CA . GLU A 481 ? 0.1740 0.1838 0.1636 0.0142 0.0002 -0.0180 522 GLU A CA 3778 C C . GLU A 481 ? 0.1621 0.1707 0.1477 0.0146 0.0002 -0.0162 522 GLU A C 3779 O O . GLU A 481 ? 0.1796 0.1882 0.1640 0.0142 -0.0012 -0.0161 522 GLU A O 3780 C CB . GLU A 481 ? 0.1729 0.1849 0.1650 0.0110 0.0026 -0.0187 522 GLU A CB 3781 C CG . GLU A 481 ? 0.1600 0.1734 0.1522 0.0083 0.0027 -0.0189 522 GLU A CG 3782 C CD . GLU A 481 ? 0.1841 0.1991 0.1772 0.0056 0.0051 -0.0195 522 GLU A CD 3783 O OE1 . GLU A 481 ? 0.2026 0.2173 0.1942 0.0054 0.0061 -0.0188 522 GLU A OE1 3784 O OE2 . GLU A 481 ? 0.2079 0.2243 0.2034 0.0039 0.0059 -0.0206 522 GLU A OE2 3785 N N . VAL A 482 ? 0.1471 0.1549 0.1312 0.0154 0.0019 -0.0148 523 VAL A N 3786 C CA . VAL A 482 ? 0.1614 0.1683 0.1424 0.0157 0.0020 -0.0131 523 VAL A CA 3787 C C . VAL A 482 ? 0.1721 0.1767 0.1497 0.0188 -0.0001 -0.0124 523 VAL A C 3788 O O . VAL A 482 ? 0.1875 0.1918 0.1630 0.0186 -0.0010 -0.0117 523 VAL A O 3789 C CB . VAL A 482 ? 0.1662 0.1727 0.1474 0.0158 0.0043 -0.0117 523 VAL A CB 3790 C CG1 . VAL A 482 ? 0.1684 0.1727 0.1487 0.0192 0.0050 -0.0107 523 VAL A CG1 3791 C CG2 . VAL A 482 ? 0.1816 0.1879 0.1609 0.0153 0.0046 -0.0103 523 VAL A CG2 3792 N N . PHE A 483 ? 0.1765 0.1794 0.1533 0.0219 -0.0009 -0.0126 524 PHE A N 3793 C CA . PHE A 483 ? 0.1741 0.1743 0.1468 0.0255 -0.0030 -0.0121 524 PHE A CA 3794 C C . PHE A 483 ? 0.1824 0.1831 0.1558 0.0249 -0.0059 -0.0136 524 PHE A C 3795 O O . PHE A 483 ? 0.2036 0.2027 0.1737 0.0264 -0.0074 -0.0131 524 PHE A O 3796 C CB . PHE A 483 ? 0.1929 0.1910 0.1644 0.0290 -0.0033 -0.0121 524 PHE A CB 3797 C CG . PHE A 483 ? 0.1780 0.1753 0.1491 0.0298 -0.0001 -0.0102 524 PHE A CG 3798 C CD1 . PHE A 483 ? 0.2135 0.2086 0.1808 0.0320 0.0013 -0.0078 524 PHE A CD1 3799 C CD2 . PHE A 483 ? 0.1889 0.1876 0.1638 0.0282 0.0016 -0.0108 524 PHE A CD2 3800 C CE1 . PHE A 483 ? 0.2311 0.2254 0.1991 0.0327 0.0046 -0.0059 524 PHE A CE1 3801 C CE2 . PHE A 483 ? 0.2049 0.2027 0.1802 0.0289 0.0045 -0.0091 524 PHE A CE2 3802 C CZ . PHE A 483 ? 0.2138 0.2094 0.1859 0.0310 0.0061 -0.0066 524 PHE A CZ 3803 N N . PHE A 484 ? 0.1763 0.1790 0.1540 0.0229 -0.0066 -0.0155 525 PHE A N 3804 C CA . PHE A 484 ? 0.1657 0.1686 0.1450 0.0226 -0.0095 -0.0171 525 PHE A CA 3805 C C . PHE A 484 ? 0.1807 0.1854 0.1614 0.0190 -0.0088 -0.0168 525 PHE A C 3806 O O . PHE A 484 ? 0.1935 0.1973 0.1720 0.0194 -0.0102 -0.0163 525 PHE A O 3807 C CB . PHE A 484 ? 0.1729 0.1770 0.1571 0.0223 -0.0104 -0.0192 525 PHE A CB 3808 C CG . PHE A 484 ? 0.1789 0.1830 0.1658 0.0225 -0.0136 -0.0209 525 PHE A CG 3809 C CD1 . PHE A 484 ? 0.1801 0.1815 0.1637 0.0262 -0.0170 -0.0213 525 PHE A CD1 3810 C CD2 . PHE A 484 ? 0.2250 0.2317 0.2179 0.0194 -0.0133 -0.0222 525 PHE A CD2 3811 C CE1 . PHE A 484 ? 0.1839 0.1851 0.1706 0.0265 -0.0204 -0.0232 525 PHE A CE1 3812 C CE2 . PHE A 484 ? 0.2043 0.2110 0.2010 0.0196 -0.0164 -0.0239 525 PHE A CE2 3813 C CZ . PHE A 484 ? 0.1756 0.1796 0.1694 0.0230 -0.0201 -0.0245 525 PHE A CZ 3814 N N . GLN A 485 ? 0.1671 0.1742 0.1509 0.0158 -0.0066 -0.0171 526 GLN A N 3815 C CA . GLN A 485 ? 0.1592 0.1677 0.1440 0.0127 -0.0060 -0.0169 526 GLN A CA 3816 C C . GLN A 485 ? 0.1554 0.1635 0.1364 0.0120 -0.0049 -0.0151 526 GLN A C 3817 O O . GLN A 485 ? 0.1833 0.1919 0.1640 0.0102 -0.0051 -0.0148 526 GLN A O 3818 C CB . GLN A 485 ? 0.1678 0.1787 0.1566 0.0097 -0.0041 -0.0179 526 GLN A CB 3819 C CG . GLN A 485 ? 0.1870 0.1987 0.1810 0.0098 -0.0053 -0.0198 526 GLN A CG 3820 C CD . GLN A 485 ? 0.2257 0.2376 0.2215 0.0110 -0.0048 -0.0207 526 GLN A CD 3821 O OE1 . GLN A 485 ? 0.2169 0.2277 0.2098 0.0128 -0.0043 -0.0199 526 GLN A OE1 3822 N NE2 . GLN A 485 ? 0.2079 0.2212 0.2091 0.0104 -0.0050 -0.0223 526 GLN A NE2 3823 N N . ARG A 486 ? 0.1555 0.1630 0.1345 0.0131 -0.0034 -0.0140 527 ARG A N 3824 C CA . ARG A 486 ? 0.1582 0.1654 0.1344 0.0125 -0.0027 -0.0124 527 ARG A CA 3825 C C . ARG A 486 ? 0.1691 0.1740 0.1418 0.0155 -0.0042 -0.0114 527 ARG A C 3826 O O . ARG A 486 ? 0.1845 0.1891 0.1555 0.0150 -0.0050 -0.0107 527 ARG A O 3827 C CB . ARG A 486 ? 0.1717 0.1796 0.1482 0.0117 -0.0003 -0.0117 527 ARG A CB 3828 C CG . ARG A 486 ? 0.1629 0.1709 0.1377 0.0106 0.0002 -0.0104 527 ARG A CG 3829 C CD . ARG A 486 ? 0.1902 0.1984 0.1658 0.0106 0.0021 -0.0095 527 ARG A CD 3830 N NE . ARG A 486 ? 0.1758 0.1856 0.1541 0.0086 0.0035 -0.0107 527 ARG A NE 3831 C CZ . ARG A 486 ? 0.1801 0.1905 0.1596 0.0075 0.0047 -0.0105 527 ARG A CZ 3832 N NH1 . ARG A 486 ? 0.1869 0.1967 0.1658 0.0081 0.0049 -0.0090 527 ARG A NH1 3833 N NH2 . ARG A 486 ? 0.1627 0.1742 0.1445 0.0060 0.0057 -0.0118 527 ARG A NH2 3834 N N . LEU A 487 ? 0.1699 0.1730 0.1411 0.0187 -0.0044 -0.0111 528 LEU A N 3835 C CA . LEU A 487 ? 0.1948 0.1955 0.1620 0.0219 -0.0053 -0.0098 528 LEU A CA 3836 C C . LEU A 487 ? 0.1993 0.1981 0.1647 0.0244 -0.0085 -0.0109 528 LEU A C 3837 O O . LEU A 487 ? 0.2112 0.2079 0.1728 0.0268 -0.0094 -0.0101 528 LEU A O 3838 C CB . LEU A 487 ? 0.1794 0.1785 0.1449 0.0246 -0.0033 -0.0084 528 LEU A CB 3839 C CG . LEU A 487 ? 0.2061 0.2066 0.1736 0.0226 -0.0003 -0.0072 528 LEU A CG 3840 C CD1 . LEU A 487 ? 0.2347 0.2334 0.2014 0.0253 0.0018 -0.0058 528 LEU A CD1 3841 C CD2 . LEU A 487 ? 0.2133 0.2143 0.1800 0.0212 0.0003 -0.0059 528 LEU A CD2 3842 N N . GLY A 488 ? 0.1780 0.1776 0.1465 0.0238 -0.0102 -0.0129 529 GLY A N 3843 C CA . GLY A 488 ? 0.1808 0.1786 0.1484 0.0261 -0.0137 -0.0143 529 GLY A CA 3844 C C . GLY A 488 ? 0.1681 0.1629 0.1317 0.0309 -0.0150 -0.0142 529 GLY A C 3845 O O . GLY A 488 ? 0.1833 0.1757 0.1437 0.0336 -0.0177 -0.0147 529 GLY A O 3846 N N . ILE A 489 ? 0.1781 0.1727 0.1419 0.0319 -0.0134 -0.0140 530 ILE A N 3847 C CA . ILE A 489 ? 0.1747 0.1662 0.1344 0.0367 -0.0146 -0.0139 530 ILE A CA 3848 C C . ILE A 489 ? 0.1914 0.1835 0.1549 0.0371 -0.0171 -0.0165 530 ILE A C 3849 O O . ILE A 489 ? 0.1884 0.1831 0.1569 0.0342 -0.0158 -0.0172 530 ILE A O 3850 C CB . ILE A 489 ? 0.1869 0.1778 0.1449 0.0376 -0.0110 -0.0118 530 ILE A CB 3851 C CG1 . ILE A 489 ? 0.1843 0.1745 0.1392 0.0377 -0.0087 -0.0094 530 ILE A CG1 3852 C CG2 . ILE A 489 ? 0.1970 0.1845 0.1509 0.0426 -0.0119 -0.0117 530 ILE A CG2 3853 C CD1 . ILE A 489 ? 0.2106 0.2012 0.1663 0.0372 -0.0046 -0.0072 530 ILE A CD1 3854 N N . ALA A 490 ? 0.1928 0.1822 0.1537 0.0408 -0.0209 -0.0179 531 ALA A N 3855 C CA . ALA A 490 ? 0.1858 0.1755 0.1506 0.0416 -0.0240 -0.0206 531 ALA A CA 3856 C C . ALA A 490 ? 0.1980 0.1885 0.1645 0.0416 -0.0218 -0.0202 531 ALA A C 3857 O O . ALA A 490 ? 0.2037 0.1920 0.1654 0.0445 -0.0201 -0.0185 531 ALA A O 3858 C CB . ALA A 490 ? 0.2144 0.2001 0.1741 0.0471 -0.0282 -0.0218 531 ALA A CB 3859 N N . SER A 491 ? 0.1851 0.1786 0.1585 0.0386 -0.0218 -0.0219 532 SER A N 3860 C CA . SER A 491 ? 0.1735 0.1679 0.1489 0.0382 -0.0194 -0.0216 532 SER A CA 3861 C C . SER A 491 ? 0.1941 0.1895 0.1749 0.0386 -0.0220 -0.0243 532 SER A C 3862 O O . SER A 491 ? 0.1931 0.1898 0.1785 0.0375 -0.0248 -0.0263 532 SER A O 3863 C CB . SER A 491 ? 0.1834 0.1811 0.1622 0.0334 -0.0153 -0.0205 532 SER A CB 3864 O OG . SER A 491 ? 0.1964 0.1933 0.1710 0.0331 -0.0129 -0.0181 532 SER A OG 3865 N N . GLY A 492 ? 0.1903 0.1853 0.1713 0.0401 -0.0210 -0.0241 533 GLY A N 3866 C CA . GLY A 492 ? 0.1867 0.1828 0.1734 0.0405 -0.0233 -0.0267 533 GLY A CA 3867 C C . GLY A 492 ? 0.1942 0.1911 0.1826 0.0401 -0.0204 -0.0261 533 GLY A C 3868 O O . GLY A 492 ? 0.2159 0.2116 0.2003 0.0405 -0.0173 -0.0238 533 GLY A O 3869 N N . ARG A 493 ? 0.1962 0.1949 0.1909 0.0395 -0.0217 -0.0283 534 ARG A N 3870 C CA . ARG A 493 ? 0.1820 0.1814 0.1789 0.0393 -0.0194 -0.0281 534 ARG A CA 3871 C C . ARG A 493 ? 0.2013 0.2011 0.2033 0.0410 -0.0229 -0.0308 534 ARG A C 3872 O O . ARG A 493 ? 0.2018 0.2024 0.2077 0.0407 -0.0261 -0.0329 534 ARG A O 3873 C CB . ARG A 493 ? 0.1886 0.1916 0.1902 0.0343 -0.0153 -0.0278 534 ARG A CB 3874 C CG . ARG A 493 ? 0.1870 0.1933 0.1960 0.0310 -0.0161 -0.0299 534 ARG A CG 3875 C CD . ARG A 493 ? 0.1954 0.2047 0.2072 0.0263 -0.0119 -0.0292 534 ARG A CD 3876 N NE . ARG A 493 ? 0.1969 0.2066 0.2089 0.0257 -0.0088 -0.0286 534 ARG A NE 3877 C CZ . ARG A 493 ? 0.2230 0.2353 0.2381 0.0222 -0.0055 -0.0288 534 ARG A CZ 3878 N NH1 . ARG A 493 ? 0.2201 0.2345 0.2377 0.0190 -0.0047 -0.0292 534 ARG A NH1 3879 N NH2 . ARG A 493 ? 0.2087 0.2211 0.2239 0.0219 -0.0030 -0.0284 534 ARG A NH2 3880 N N . ALA A 494 ? 0.1958 0.1945 0.1976 0.0431 -0.0223 -0.0308 535 ALA A N 3881 C CA . ALA A 494 ? 0.1922 0.1912 0.1990 0.0451 -0.0258 -0.0334 535 ALA A CA 3882 C C . ALA A 494 ? 0.2052 0.2047 0.2141 0.0451 -0.0233 -0.0331 535 ALA A C 3883 O O . ALA A 494 ? 0.2114 0.2090 0.2152 0.0461 -0.0204 -0.0307 535 ALA A O 3884 C CB . ALA A 494 ? 0.2014 0.1962 0.2023 0.0508 -0.0304 -0.0339 535 ALA A CB 3885 N N . ARG A 495 ? 0.2069 0.2089 0.2237 0.0441 -0.0245 -0.0355 536 ARG A N 3886 C CA . ARG A 495 ? 0.2104 0.2129 0.2298 0.0442 -0.0224 -0.0356 536 ARG A CA 3887 C C . ARG A 495 ? 0.2218 0.2260 0.2490 0.0449 -0.0256 -0.0386 536 ARG A C 3888 O O . ARG A 495 ? 0.2257 0.2313 0.2574 0.0443 -0.0286 -0.0405 536 ARG A O 3889 C CB . ARG A 495 ? 0.2124 0.2180 0.2347 0.0394 -0.0172 -0.0346 536 ARG A CB 3890 C CG . ARG A 495 ? 0.2026 0.2124 0.2325 0.0348 -0.0163 -0.0362 536 ARG A CG 3891 C CD . ARG A 495 ? 0.2434 0.2557 0.2755 0.0309 -0.0113 -0.0355 536 ARG A CD 3892 N NE . ARG A 495 ? 0.2413 0.2520 0.2667 0.0302 -0.0086 -0.0330 536 ARG A NE 3893 C CZ . ARG A 495 ? 0.2367 0.2493 0.2624 0.0266 -0.0050 -0.0322 536 ARG A CZ 3894 N NH1 . ARG A 495 ? 0.2686 0.2844 0.3000 0.0234 -0.0033 -0.0336 536 ARG A NH1 3895 N NH2 . ARG A 495 ? 0.2288 0.2399 0.2489 0.0263 -0.0030 -0.0301 536 ARG A NH2 3896 N N . TYR A 496 ? 0.2260 0.2302 0.2556 0.0460 -0.0249 -0.0390 537 TYR A N 3897 C CA . TYR A 496 ? 0.2374 0.2439 0.2760 0.0460 -0.0271 -0.0419 537 TYR A CA 3898 C C . TYR A 496 ? 0.2483 0.2594 0.2948 0.0408 -0.0232 -0.0426 537 TYR A C 3899 O O . TYR A 496 ? 0.2394 0.2513 0.2839 0.0381 -0.0186 -0.0409 537 TYR A O 3900 C CB . TYR A 496 ? 0.2365 0.2408 0.2742 0.0501 -0.0287 -0.0423 537 TYR A CB 3901 C CG . TYR A 496 ? 0.2415 0.2441 0.2804 0.0543 -0.0350 -0.0447 537 TYR A CG 3902 C CD1 . TYR A 496 ? 0.2353 0.2340 0.2663 0.0581 -0.0385 -0.0442 537 TYR A CD1 3903 C CD2 . TYR A 496 ? 0.2580 0.2628 0.3062 0.0546 -0.0375 -0.0477 537 TYR A CD2 3904 C CE1 . TYR A 496 ? 0.2517 0.2486 0.2835 0.0622 -0.0448 -0.0467 537 TYR A CE1 3905 C CE2 . TYR A 496 ? 0.2562 0.2595 0.3061 0.0585 -0.0439 -0.0502 537 TYR A CE2 3906 C CZ . TYR A 496 ? 0.2465 0.2458 0.2879 0.0624 -0.0475 -0.0498 537 TYR A CZ 3907 O OH . TYR A 496 ? 0.2882 0.2856 0.3308 0.0665 -0.0542 -0.0526 537 TYR A OH 3908 N N . THR A 497 ? 0.2367 0.2506 0.2921 0.0395 -0.0251 -0.0451 538 THR A N 3909 C CA . THR A 497 ? 0.2420 0.2600 0.3047 0.0348 -0.0213 -0.0456 538 THR A CA 3910 C C . THR A 497 ? 0.2581 0.2788 0.3313 0.0347 -0.0224 -0.0482 538 THR A C 3911 O O . THR A 497 ? 0.2498 0.2690 0.3245 0.0383 -0.0265 -0.0498 538 THR A O 3912 C CB . THR A 497 ? 0.2470 0.2663 0.3104 0.0320 -0.0212 -0.0453 538 THR A CB 3913 O OG1 . THR A 497 ? 0.2513 0.2740 0.3194 0.0275 -0.0165 -0.0450 538 THR A OG1 3914 C CG2 . THR A 497 ? 0.2422 0.2618 0.3115 0.0334 -0.0262 -0.0477 538 THR A CG2 3915 N N . LYS A 498 ? 0.2662 0.2904 0.3461 0.0308 -0.0185 -0.0486 539 LYS A N 3916 C CA . LYS A 498 ? 0.2895 0.3168 0.3803 0.0301 -0.0185 -0.0509 539 LYS A CA 3917 C C . LYS A 498 ? 0.3012 0.3303 0.4001 0.0295 -0.0215 -0.0527 539 LYS A C 3918 O O . LYS A 498 ? 0.2884 0.3164 0.3843 0.0295 -0.0234 -0.0522 539 LYS A O 3919 C CB . LYS A 498 ? 0.2977 0.3278 0.3914 0.0262 -0.0124 -0.0503 539 LYS A CB 3920 C CG . LYS A 498 ? 0.3528 0.3842 0.4455 0.0227 -0.0095 -0.0491 539 LYS A CG 3921 C CD . LYS A 498 ? 0.4687 0.5023 0.5626 0.0192 -0.0037 -0.0484 539 LYS A CD 3922 C CE . LYS A 498 ? 0.5116 0.5451 0.6004 0.0165 -0.0012 -0.0465 539 LYS A CE 3923 N NZ . LYS A 498 ? 0.5831 0.6187 0.6736 0.0132 0.0043 -0.0461 539 LYS A NZ 3924 N N . ASN A 499 ? 0.3213 0.3531 0.4312 0.0292 -0.0219 -0.0549 540 ASN A N 3925 C CA . ASN A 499 ? 0.3617 0.3957 0.4817 0.0281 -0.0241 -0.0568 540 ASN A CA 3926 C C . ASN A 499 ? 0.3910 0.4278 0.5142 0.0235 -0.0184 -0.0555 540 ASN A C 3927 O O . ASN A 499 ? 0.3976 0.4368 0.5253 0.0214 -0.0139 -0.0554 540 ASN A O 3928 C CB . ASN A 499 ? 0.3627 0.3986 0.4939 0.0296 -0.0264 -0.0596 540 ASN A CB 3929 C CG . ASN A 499 ? 0.3637 0.4021 0.5070 0.0286 -0.0289 -0.0616 540 ASN A CG 3930 O OD1 . ASN A 499 ? 0.3806 0.4197 0.5249 0.0259 -0.0274 -0.0608 540 ASN A OD1 3931 N ND2 . ASN A 499 ? 0.3903 0.4297 0.5431 0.0308 -0.0328 -0.0645 540 ASN A ND2 3932 N N . TRP A 500 ? 0.4318 0.4680 0.5525 0.0220 -0.0187 -0.0545 541 TRP A N 3933 C CA . TRP A 500 ? 0.4838 0.5221 0.6059 0.0179 -0.0134 -0.0529 541 TRP A CA 3934 C C . TRP A 500 ? 0.5207 0.5626 0.6565 0.0158 -0.0115 -0.0543 541 TRP A C 3935 O O . TRP A 500 ? 0.5315 0.5753 0.6692 0.0127 -0.0058 -0.0530 541 TRP A O 3936 C CB . TRP A 500 ? 0.4858 0.5223 0.6020 0.0172 -0.0147 -0.0515 541 TRP A CB 3937 C CG . TRP A 500 ? 0.5009 0.5344 0.6037 0.0182 -0.0143 -0.0494 541 TRP A CG 3938 C CD1 . TRP A 500 ? 0.5041 0.5351 0.6000 0.0215 -0.0165 -0.0494 541 TRP A CD1 3939 C CD2 . TRP A 500 ? 0.5185 0.5513 0.6137 0.0160 -0.0114 -0.0470 541 TRP A CD2 3940 N NE1 . TRP A 500 ? 0.4639 0.4928 0.5490 0.0213 -0.0148 -0.0470 541 TRP A NE1 3941 C CE2 . TRP A 500 ? 0.5108 0.5407 0.5953 0.0180 -0.0119 -0.0457 541 TRP A CE2 3942 C CE3 . TRP A 500 ? 0.5421 0.5761 0.6385 0.0127 -0.0083 -0.0458 541 TRP A CE3 3943 C CZ2 . TRP A 500 ? 0.5339 0.5626 0.6098 0.0166 -0.0097 -0.0434 541 TRP A CZ2 3944 C CZ3 . TRP A 500 ? 0.5406 0.5732 0.6277 0.0115 -0.0062 -0.0435 541 TRP A CZ3 3945 C CH2 . TRP A 500 ? 0.5509 0.5810 0.6281 0.0134 -0.0070 -0.0424 541 TRP A CH2 3946 N N . GLU A 501 ? 0.5557 0.5984 0.7009 0.0177 -0.0161 -0.0568 542 GLU A N 3947 C CA . GLU A 501 ? 0.5937 0.6399 0.7536 0.0160 -0.0148 -0.0584 542 GLU A CA 3948 C C . GLU A 501 ? 0.6050 0.6535 0.7694 0.0151 -0.0102 -0.0586 542 GLU A C 3949 O O . GLU A 501 ? 0.6150 0.6661 0.7863 0.0122 -0.0051 -0.0580 542 GLU A O 3950 C CB . GLU A 501 ? 0.6042 0.6504 0.7732 0.0187 -0.0218 -0.0615 542 GLU A CB 3951 C CG . GLU A 501 ? 0.6590 0.7025 0.8234 0.0205 -0.0275 -0.0619 542 GLU A CG 3952 C CD . GLU A 501 ? 0.7307 0.7752 0.9002 0.0176 -0.0262 -0.0612 542 GLU A CD 3953 O OE1 . GLU A 501 ? 0.7643 0.8114 0.9478 0.0165 -0.0268 -0.0629 542 GLU A OE1 3954 O OE2 . GLU A 501 ? 0.7647 0.8075 0.9247 0.0163 -0.0245 -0.0589 542 GLU A OE2 3955 N N . THR A 502 ? 0.6164 0.6637 0.7769 0.0177 -0.0119 -0.0594 543 THR A N 3956 C CA . THR A 502 ? 0.6262 0.6756 0.7920 0.0175 -0.0086 -0.0601 543 THR A CA 3957 C C . THR A 502 ? 0.6317 0.6803 0.7879 0.0160 -0.0030 -0.0580 543 THR A C 3958 O O . THR A 502 ? 0.6256 0.6760 0.7853 0.0154 0.0008 -0.0583 543 THR A O 3959 C CB . THR A 502 ? 0.6317 0.6803 0.8004 0.0213 -0.0138 -0.0624 543 THR A CB 3960 O OG1 . THR A 502 ? 0.6395 0.6844 0.7954 0.0240 -0.0165 -0.0615 543 THR A OG1 3961 C CG2 . THR A 502 ? 0.6300 0.6795 0.8092 0.0229 -0.0198 -0.0650 543 THR A CG2 3962 N N . ASN A 503 ? 0.6436 0.6898 0.7880 0.0156 -0.0027 -0.0559 544 ASN A N 3963 C CA . ASN A 503 ? 0.6522 0.6973 0.7869 0.0145 0.0018 -0.0540 544 ASN A CA 3964 C C . ASN A 503 ? 0.6555 0.7009 0.7859 0.0113 0.0062 -0.0519 544 ASN A C 3965 O O . ASN A 503 ? 0.6605 0.7042 0.7851 0.0110 0.0044 -0.0507 544 ASN A O 3966 C CB . ASN A 503 ? 0.6535 0.6951 0.7774 0.0172 -0.0013 -0.0533 544 ASN A CB 3967 C CG . ASN A 503 ? 0.6799 0.7208 0.8066 0.0206 -0.0048 -0.0551 544 ASN A CG 3968 O OD1 . ASN A 503 ? 0.7229 0.7649 0.8528 0.0206 -0.0024 -0.0558 544 ASN A OD1 3969 N ND2 . ASN A 503 ? 0.6774 0.7163 0.8027 0.0237 -0.0107 -0.0559 544 ASN A ND2 3970 N N . LYS A 504 ? 0.6548 0.7021 0.7878 0.0091 0.0119 -0.0515 545 LYS A N 3971 C CA . LYS A 504 ? 0.6569 0.7045 0.7864 0.0062 0.0166 -0.0496 545 LYS A CA 3972 C C . LYS A 504 ? 0.6451 0.6907 0.7623 0.0056 0.0192 -0.0480 545 LYS A C 3973 O O . LYS A 504 ? 0.6552 0.7004 0.7673 0.0035 0.0224 -0.0464 545 LYS A O 3974 C CB . LYS A 504 ? 0.6638 0.7144 0.8031 0.0044 0.0215 -0.0501 545 LYS A CB 3975 C CG . LYS A 504 ? 0.6951 0.7458 0.8291 0.0022 0.0281 -0.0485 545 LYS A CG 3976 C CD . LYS A 504 ? 0.7306 0.7837 0.8730 0.0017 0.0327 -0.0494 545 LYS A CD 3977 C CE . LYS A 504 ? 0.7377 0.7902 0.8723 0.0009 0.0380 -0.0486 545 LYS A CE 3978 N NZ . LYS A 504 ? 0.7352 0.7893 0.8757 0.0016 0.0407 -0.0503 545 LYS A NZ 3979 N N . PHE A 505 ? 0.6222 0.6663 0.7347 0.0074 0.0178 -0.0486 546 PHE A N 3980 C CA . PHE A 505 ? 0.5896 0.6317 0.6915 0.0070 0.0196 -0.0473 546 PHE A CA 3981 C C . PHE A 505 ? 0.5730 0.6128 0.6665 0.0072 0.0170 -0.0457 546 PHE A C 3982 O O . PHE A 505 ? 0.5668 0.6061 0.6618 0.0082 0.0130 -0.0457 546 PHE A O 3983 C CB . PHE A 505 ? 0.5920 0.6334 0.6926 0.0089 0.0191 -0.0483 546 PHE A CB 3984 C CG . PHE A 505 ? 0.5820 0.6219 0.6832 0.0119 0.0139 -0.0490 546 PHE A CG 3985 C CD1 . PHE A 505 ? 0.5881 0.6252 0.6808 0.0133 0.0112 -0.0477 546 PHE A CD1 3986 C CD2 . PHE A 505 ? 0.6017 0.6429 0.7118 0.0135 0.0117 -0.0508 546 PHE A CD2 3987 C CE1 . PHE A 505 ? 0.5804 0.6156 0.6727 0.0165 0.0066 -0.0481 546 PHE A CE1 3988 C CE2 . PHE A 505 ? 0.6010 0.6405 0.7109 0.0167 0.0066 -0.0515 546 PHE A CE2 3989 C CZ . PHE A 505 ? 0.5994 0.6358 0.7000 0.0183 0.0041 -0.0501 546 PHE A CZ 3990 N N . SER A 506 ? 0.5479 0.5864 0.6328 0.0062 0.0192 -0.0444 547 SER A N 3991 C CA . SER A 506 ? 0.5199 0.5562 0.5967 0.0061 0.0173 -0.0427 547 SER A CA 3992 C C . SER A 506 ? 0.4896 0.5236 0.5610 0.0084 0.0146 -0.0424 547 SER A C 3993 O O . SER A 506 ? 0.4960 0.5296 0.5662 0.0089 0.0161 -0.0429 547 SER A O 3994 C CB . SER A 506 ? 0.5326 0.5686 0.6031 0.0039 0.0210 -0.0414 547 SER A CB 3995 O OG . SER A 506 ? 0.5561 0.5939 0.6305 0.0025 0.0252 -0.0422 547 SER A OG 3996 N N . GLY A 507 ? 0.4413 0.4735 0.5093 0.0098 0.0110 -0.0415 548 GLY A N 3997 C CA . GLY A 507 ? 0.4005 0.4302 0.4634 0.0124 0.0085 -0.0410 548 GLY A CA 3998 C C . GLY A 507 ? 0.3790 0.4086 0.4458 0.0145 0.0079 -0.0424 548 GLY A C 3999 O O . GLY A 507 ? 0.3981 0.4293 0.4722 0.0152 0.0065 -0.0439 548 GLY A O 4000 N N . TYR A 508 ? 0.3123 0.3404 0.3752 0.0153 0.0089 -0.0419 549 TYR A N 4001 C CA . TYR A 508 ? 0.2677 0.2959 0.3345 0.0169 0.0090 -0.0432 549 TYR A CA 4002 C C . TYR A 508 ? 0.2463 0.2754 0.3131 0.0149 0.0133 -0.0436 549 TYR A C 4003 O O . TYR A 508 ? 0.2395 0.2680 0.3010 0.0131 0.0154 -0.0425 549 TYR A O 4004 C CB . TYR A 508 ? 0.2593 0.2845 0.3222 0.0203 0.0064 -0.0424 549 TYR A CB 4005 C CG . TYR A 508 ? 0.2354 0.2582 0.2906 0.0202 0.0075 -0.0403 549 TYR A CG 4006 C CD1 . TYR A 508 ? 0.2223 0.2441 0.2759 0.0201 0.0098 -0.0400 549 TYR A CD1 4007 C CD2 . TYR A 508 ? 0.2218 0.2435 0.2720 0.0201 0.0062 -0.0387 549 TYR A CD2 4008 C CE1 . TYR A 508 ? 0.1984 0.2182 0.2461 0.0199 0.0109 -0.0381 549 TYR A CE1 4009 C CE2 . TYR A 508 ? 0.2216 0.2412 0.2654 0.0199 0.0074 -0.0368 549 TYR A CE2 4010 C CZ . TYR A 508 ? 0.2143 0.2331 0.2572 0.0198 0.0097 -0.0365 549 TYR A CZ 4011 O OH . TYR A 508 ? 0.2097 0.2267 0.2476 0.0196 0.0108 -0.0347 549 TYR A OH 4012 N N . PRO A 509 ? 0.2323 0.2629 0.3050 0.0152 0.0145 -0.0453 550 PRO A N 4013 C CA . PRO A 509 ? 0.2197 0.2513 0.2927 0.0132 0.0186 -0.0460 550 PRO A CA 4014 C C . PRO A 509 ? 0.2083 0.2378 0.2752 0.0130 0.0200 -0.0452 550 PRO A C 4015 O O . PRO A 509 ? 0.2273 0.2574 0.2923 0.0110 0.0229 -0.0455 550 PRO A O 4016 C CB . PRO A 509 ? 0.2124 0.2454 0.2930 0.0143 0.0190 -0.0479 550 PRO A CB 4017 C CG . PRO A 509 ? 0.2360 0.2703 0.3223 0.0154 0.0158 -0.0484 550 PRO A CG 4018 C CD . PRO A 509 ? 0.2425 0.2742 0.3227 0.0171 0.0122 -0.0468 550 PRO A CD 4019 N N . LEU A 510 ? 0.2004 0.2275 0.2648 0.0153 0.0180 -0.0443 551 LEU A N 4020 C CA . LEU A 510 ? 0.2046 0.2298 0.2651 0.0152 0.0194 -0.0437 551 LEU A CA 4021 C C . LEU A 510 ? 0.2028 0.2265 0.2568 0.0144 0.0191 -0.0418 551 LEU A C 4022 O O . LEU A 510 ? 0.2252 0.2470 0.2760 0.0145 0.0198 -0.0410 551 LEU A O 4023 C CB . LEU A 510 ? 0.1978 0.2209 0.2593 0.0180 0.0180 -0.0436 551 LEU A CB 4024 C CG . LEU A 510 ? 0.2007 0.2255 0.2688 0.0185 0.0189 -0.0458 551 LEU A CG 4025 C CD1 . LEU A 510 ? 0.2335 0.2563 0.3031 0.0215 0.0172 -0.0456 551 LEU A CD1 4026 C CD2 . LEU A 510 ? 0.1870 0.2130 0.2561 0.0162 0.0226 -0.0472 551 LEU A CD2 4027 N N . TYR A 511 ? 0.1917 0.2162 0.2444 0.0136 0.0180 -0.0411 552 TYR A N 4028 C CA . TYR A 511 ? 0.1868 0.2101 0.2335 0.0127 0.0177 -0.0393 552 TYR A CA 4029 C C . TYR A 511 ? 0.1795 0.2024 0.2231 0.0109 0.0201 -0.0393 552 TYR A C 4030 O O . TYR A 511 ? 0.1935 0.2179 0.2378 0.0089 0.0223 -0.0406 552 TYR A O 4031 C CB . TYR A 511 ? 0.1846 0.2094 0.2316 0.0115 0.0170 -0.0392 552 TYR A CB 4032 C CG . TYR A 511 ? 0.1837 0.2078 0.2251 0.0102 0.0168 -0.0376 552 TYR A CG 4033 C CD1 . TYR A 511 ? 0.1971 0.2192 0.2345 0.0118 0.0147 -0.0358 552 TYR A CD1 4034 C CD2 . TYR A 511 ? 0.2228 0.2482 0.2629 0.0076 0.0189 -0.0378 552 TYR A CD2 4035 C CE1 . TYR A 511 ? 0.1695 0.1910 0.2022 0.0105 0.0146 -0.0344 552 TYR A CE1 4036 C CE2 . TYR A 511 ? 0.2048 0.2297 0.2402 0.0065 0.0186 -0.0364 552 TYR A CE2 4037 C CZ . TYR A 511 ? 0.1931 0.2162 0.2251 0.0079 0.0165 -0.0348 552 TYR A CZ 4038 O OH . TYR A 511 ? 0.1903 0.2129 0.2178 0.0067 0.0164 -0.0335 552 TYR A OH 4039 N N . HIS A 512 ? 0.1993 0.2199 0.2394 0.0117 0.0196 -0.0379 553 HIS A N 4040 C CA . HIS A 512 ? 0.1861 0.2060 0.2234 0.0101 0.0212 -0.0377 553 HIS A CA 4041 C C . HIS A 512 ? 0.2050 0.2251 0.2448 0.0095 0.0232 -0.0396 553 HIS A C 4042 O O . HIS A 512 ? 0.2051 0.2250 0.2430 0.0079 0.0245 -0.0403 553 HIS A O 4043 C CB . HIS A 512 ? 0.1958 0.2167 0.2298 0.0079 0.0216 -0.0375 553 HIS A CB 4044 C CG . HIS A 512 ? 0.1797 0.1999 0.2102 0.0083 0.0198 -0.0354 553 HIS A CG 4045 N ND1 . HIS A 512 ? 0.1757 0.1965 0.2029 0.0065 0.0199 -0.0349 553 HIS A ND1 4046 C CD2 . HIS A 512 ? 0.1900 0.2086 0.2194 0.0104 0.0178 -0.0338 553 HIS A CD2 4047 C CE1 . HIS A 512 ? 0.2011 0.2209 0.2258 0.0073 0.0181 -0.0331 553 HIS A CE1 4048 N NE2 . HIS A 512 ? 0.1534 0.1718 0.1790 0.0097 0.0170 -0.0323 553 HIS A NE2 4049 N N . SER A 513 ? 0.1976 0.2179 0.2415 0.0109 0.0232 -0.0406 554 SER A N 4050 C CA . SER A 513 ? 0.2005 0.2207 0.2472 0.0108 0.0250 -0.0424 554 SER A CA 4051 C C . SER A 513 ? 0.2115 0.2293 0.2591 0.0126 0.0246 -0.0415 554 SER A C 4052 O O . SER A 513 ? 0.2151 0.2314 0.2618 0.0146 0.0230 -0.0396 554 SER A O 4053 C CB . SER A 513 ? 0.1957 0.2178 0.2470 0.0111 0.0256 -0.0441 554 SER A CB 4054 O OG A SER A 513 ? 0.2242 0.2456 0.2785 0.0135 0.0240 -0.0437 554 SER A OG 4055 O OG B SER A 513 ? 0.2012 0.2228 0.2560 0.0121 0.0266 -0.0455 554 SER A OG 4056 N N . VAL A 514 ? 0.2119 0.2291 0.2616 0.0123 0.0261 -0.0430 555 VAL A N 4057 C CA . VAL A 514 ? 0.2267 0.2413 0.2780 0.0140 0.0261 -0.0421 555 VAL A CA 4058 C C . VAL A 514 ? 0.2251 0.2393 0.2791 0.0167 0.0250 -0.0417 555 VAL A C 4059 O O . VAL A 514 ? 0.2403 0.2521 0.2947 0.0188 0.0246 -0.0401 555 VAL A O 4060 C CB . VAL A 514 ? 0.2285 0.2428 0.2822 0.0131 0.0277 -0.0442 555 VAL A CB 4061 C CG1 . VAL A 514 ? 0.2184 0.2343 0.2759 0.0135 0.0286 -0.0465 555 VAL A CG1 4062 C CG2 . VAL A 514 ? 0.2400 0.2515 0.2955 0.0144 0.0279 -0.0431 555 VAL A CG2 4063 N N . TYR A 515 ? 0.2007 0.2172 0.2567 0.0167 0.0245 -0.0429 556 TYR A N 4064 C CA . TYR A 515 ? 0.2299 0.2462 0.2892 0.0192 0.0231 -0.0431 556 TYR A CA 4065 C C . TYR A 515 ? 0.2422 0.2572 0.2989 0.0214 0.0205 -0.0409 556 TYR A C 4066 O O . TYR A 515 ? 0.2579 0.2721 0.3166 0.0241 0.0189 -0.0408 556 TYR A O 4067 C CB . TYR A 515 ? 0.2207 0.2399 0.2845 0.0185 0.0237 -0.0455 556 TYR A CB 4068 C CG . TYR A 515 ? 0.2255 0.2456 0.2911 0.0168 0.0264 -0.0475 556 TYR A CG 4069 C CD1 . TYR A 515 ? 0.2318 0.2501 0.2995 0.0178 0.0272 -0.0482 556 TYR A CD1 4070 C CD2 . TYR A 515 ? 0.2363 0.2584 0.3011 0.0145 0.0281 -0.0488 556 TYR A CD2 4071 C CE1 . TYR A 515 ? 0.2063 0.2251 0.2752 0.0164 0.0295 -0.0504 556 TYR A CE1 4072 C CE2 . TYR A 515 ? 0.2477 0.2702 0.3133 0.0133 0.0306 -0.0510 556 TYR A CE2 4073 C CZ . TYR A 515 ? 0.2466 0.2674 0.3142 0.0142 0.0311 -0.0518 556 TYR A CZ 4074 O OH . TYR A 515 ? 0.2586 0.2795 0.3266 0.0132 0.0333 -0.0541 556 TYR A OH 4075 N N . GLU A 516 ? 0.2319 0.2466 0.2842 0.0206 0.0200 -0.0393 557 GLU A N 4076 C CA . GLU A 516 ? 0.2444 0.2575 0.2936 0.0228 0.0176 -0.0373 557 GLU A CA 4077 C C . GLU A 516 ? 0.2297 0.2393 0.2766 0.0254 0.0176 -0.0351 557 GLU A C 4078 O O . GLU A 516 ? 0.2276 0.2357 0.2715 0.0247 0.0187 -0.0334 557 GLU A O 4079 C CB . GLU A 516 ? 0.2739 0.2878 0.3191 0.0209 0.0174 -0.0364 557 GLU A CB 4080 C CG . GLU A 516 ? 0.3263 0.3412 0.3709 0.0214 0.0152 -0.0364 557 GLU A CG 4081 C CD . GLU A 516 ? 0.2647 0.2790 0.3042 0.0206 0.0148 -0.0346 557 GLU A CD 4082 O OE1 . GLU A 516 ? 0.2905 0.3067 0.3294 0.0178 0.0156 -0.0351 557 GLU A OE1 4083 O OE2 . GLU A 516 ? 0.2444 0.2562 0.2806 0.0227 0.0139 -0.0326 557 GLU A OE2 4084 N N . THR A 517 ? 0.2190 0.2270 0.2677 0.0283 0.0167 -0.0351 558 THR A N 4085 C CA . THR A 517 ? 0.2279 0.2324 0.2752 0.0308 0.0173 -0.0330 558 THR A CA 4086 C C . THR A 517 ? 0.2213 0.2232 0.2657 0.0349 0.0147 -0.0315 558 THR A C 4087 O O . THR A 517 ? 0.2329 0.2362 0.2777 0.0358 0.0121 -0.0327 558 THR A O 4088 C CB . THR A 517 ? 0.2249 0.2293 0.2771 0.0309 0.0188 -0.0345 558 THR A CB 4089 O OG1 . THR A 517 ? 0.2613 0.2674 0.3169 0.0319 0.0171 -0.0365 558 THR A OG1 4090 C CG2 . THR A 517 ? 0.2406 0.2468 0.2952 0.0272 0.0213 -0.0362 558 THR A CG2 4091 N N . TYR A 518 ? 0.2229 0.2211 0.2648 0.0377 0.0155 -0.0290 559 TYR A N 4092 C CA . TYR A 518 ? 0.2323 0.2275 0.2711 0.0422 0.0132 -0.0276 559 TYR A CA 4093 C C . TYR A 518 ? 0.2400 0.2364 0.2830 0.0436 0.0110 -0.0301 559 TYR A C 4094 O O . TYR A 518 ? 0.2524 0.2486 0.2942 0.0461 0.0077 -0.0307 559 TYR A O 4095 C CB . TYR A 518 ? 0.2387 0.2295 0.2751 0.0448 0.0152 -0.0246 559 TYR A CB 4096 C CG . TYR A 518 ? 0.2505 0.2377 0.2835 0.0500 0.0131 -0.0233 559 TYR A CG 4097 C CD1 . TYR A 518 ? 0.2811 0.2660 0.3076 0.0530 0.0112 -0.0215 559 TYR A CD1 4098 C CD2 . TYR A 518 ? 0.2766 0.2628 0.3128 0.0521 0.0127 -0.0241 559 TYR A CD2 4099 C CE1 . TYR A 518 ? 0.3124 0.2936 0.3349 0.0582 0.0089 -0.0204 559 TYR A CE1 4100 C CE2 . TYR A 518 ? 0.3155 0.2980 0.3480 0.0573 0.0104 -0.0229 559 TYR A CE2 4101 C CZ . TYR A 518 ? 0.3356 0.3157 0.3611 0.0604 0.0085 -0.0211 559 TYR A CZ 4102 O OH . TYR A 518 ? 0.3422 0.3182 0.3629 0.0660 0.0060 -0.0199 559 TYR A OH 4103 N N . GLU A 519 ? 0.2321 0.2300 0.2806 0.0420 0.0128 -0.0318 560 GLU A N 4104 C CA . GLU A 519 ? 0.2439 0.2429 0.2970 0.0434 0.0110 -0.0341 560 GLU A CA 4105 C C . GLU A 519 ? 0.2463 0.2490 0.3021 0.0420 0.0087 -0.0366 560 GLU A C 4106 O O . GLU A 519 ? 0.2628 0.2660 0.3212 0.0442 0.0058 -0.0380 560 GLU A O 4107 C CB . GLU A 519 ? 0.2647 0.2647 0.3234 0.0417 0.0135 -0.0357 560 GLU A CB 4108 C CG . GLU A 519 ? 0.2707 0.2667 0.3282 0.0437 0.0154 -0.0334 560 GLU A CG 4109 C CD . GLU A 519 ? 0.2888 0.2833 0.3432 0.0421 0.0180 -0.0312 560 GLU A CD 4110 O OE1 . GLU A 519 ? 0.2890 0.2861 0.3441 0.0384 0.0192 -0.0323 560 GLU A OE1 4111 O OE2 . GLU A 519 ? 0.3168 0.3074 0.3683 0.0446 0.0190 -0.0283 560 GLU A OE2 4112 N N . LEU A 520 ? 0.2339 0.2394 0.2899 0.0382 0.0100 -0.0372 561 LEU A N 4113 C CA . LEU A 520 ? 0.2380 0.2468 0.2967 0.0369 0.0082 -0.0392 561 LEU A CA 4114 C C . LEU A 520 ? 0.2377 0.2450 0.2934 0.0400 0.0042 -0.0386 561 LEU A C 4115 O O . LEU A 520 ? 0.2391 0.2480 0.2989 0.0411 0.0014 -0.0405 561 LEU A O 4116 C CB . LEU A 520 ? 0.2236 0.2347 0.2812 0.0328 0.0102 -0.0393 561 LEU A CB 4117 C CG . LEU A 520 ? 0.2330 0.2473 0.2929 0.0312 0.0087 -0.0408 561 LEU A CG 4118 C CD1 . LEU A 520 ? 0.2469 0.2640 0.3143 0.0308 0.0087 -0.0434 561 LEU A CD1 4119 C CD2 . LEU A 520 ? 0.2475 0.2633 0.3049 0.0276 0.0108 -0.0403 561 LEU A CD2 4120 N N . VAL A 521 ? 0.2416 0.2459 0.2905 0.0416 0.0039 -0.0359 562 VAL A N 4121 C CA . VAL A 521 ? 0.2381 0.2405 0.2828 0.0448 0.0002 -0.0353 562 VAL A CA 4122 C C . VAL A 521 ? 0.2675 0.2672 0.3121 0.0496 -0.0027 -0.0355 562 VAL A C 4123 O O . VAL A 521 ? 0.2824 0.2828 0.3291 0.0515 -0.0065 -0.0373 562 VAL A O 4124 C CB . VAL A 521 ? 0.2578 0.2573 0.2948 0.0456 0.0011 -0.0322 562 VAL A CB 4125 C CG1 . VAL A 521 ? 0.2466 0.2436 0.2786 0.0495 -0.0029 -0.0316 562 VAL A CG1 4126 C CG2 . VAL A 521 ? 0.2561 0.2584 0.2934 0.0410 0.0033 -0.0323 562 VAL A CG2 4127 N N . GLU A 522 ? 0.2779 0.2746 0.3208 0.0515 -0.0008 -0.0338 563 GLU A N 4128 C CA . GLU A 522 ? 0.2967 0.2901 0.3383 0.0564 -0.0032 -0.0334 563 GLU A CA 4129 C C . GLU A 522 ? 0.2965 0.2925 0.3457 0.0566 -0.0052 -0.0366 563 GLU A C 4130 O O . GLU A 522 ? 0.3065 0.3009 0.3555 0.0605 -0.0092 -0.0375 563 GLU A O 4131 C CB . GLU A 522 ? 0.3141 0.3041 0.3532 0.0577 0.0001 -0.0308 563 GLU A CB 4132 C CG . GLU A 522 ? 0.3790 0.3641 0.4139 0.0635 -0.0019 -0.0293 563 GLU A CG 4133 C CD . GLU A 522 ? 0.4750 0.4608 0.5160 0.0647 -0.0029 -0.0314 563 GLU A CD 4134 O OE1 . GLU A 522 ? 0.4726 0.4616 0.5203 0.0610 -0.0004 -0.0330 563 GLU A OE1 4135 O OE2 . GLU A 522 ? 0.4913 0.4744 0.5301 0.0694 -0.0064 -0.0315 563 GLU A OE2 4136 N N . LYS A 523 ? 0.2709 0.2707 0.3268 0.0525 -0.0026 -0.0385 564 LYS A N 4137 C CA . LYS A 523 ? 0.2775 0.2798 0.3413 0.0527 -0.0040 -0.0414 564 LYS A CA 4138 C C . LYS A 523 ? 0.2880 0.2940 0.3567 0.0513 -0.0066 -0.0439 564 LYS A C 4139 O O . LYS A 523 ? 0.3118 0.3187 0.3855 0.0534 -0.0100 -0.0460 564 LYS A O 4140 C CB . LYS A 523 ? 0.2675 0.2719 0.3364 0.0494 0.0002 -0.0423 564 LYS A CB 4141 C CG . LYS A 523 ? 0.3031 0.3041 0.3697 0.0511 0.0024 -0.0404 564 LYS A CG 4142 C CD . LYS A 523 ? 0.3302 0.3336 0.4026 0.0476 0.0062 -0.0419 564 LYS A CD 4143 C CE . LYS A 523 ? 0.3981 0.3982 0.4689 0.0483 0.0090 -0.0401 564 LYS A CE 4144 N NZ . LYS A 523 ? 0.4552 0.4509 0.5233 0.0532 0.0073 -0.0383 564 LYS A NZ 4145 N N . PHE A 524 ? 0.2751 0.2834 0.3430 0.0478 -0.0053 -0.0438 565 PHE A N 4146 C CA . PHE A 524 ? 0.2676 0.2799 0.3419 0.0455 -0.0065 -0.0463 565 PHE A CA 4147 C C . PHE A 524 ? 0.2752 0.2873 0.3462 0.0460 -0.0096 -0.0459 565 PHE A C 4148 O O . PHE A 524 ? 0.3202 0.3346 0.3969 0.0459 -0.0123 -0.0480 565 PHE A O 4149 C CB . PHE A 524 ? 0.2737 0.2898 0.3522 0.0406 -0.0021 -0.0471 565 PHE A CB 4150 C CG . PHE A 524 ? 0.2849 0.3017 0.3677 0.0400 0.0007 -0.0480 565 PHE A CG 4151 C CD1 . PHE A 524 ? 0.3176 0.3358 0.4078 0.0415 -0.0009 -0.0502 565 PHE A CD1 4152 C CD2 . PHE A 524 ? 0.2791 0.2949 0.3589 0.0383 0.0046 -0.0468 565 PHE A CD2 4153 C CE1 . PHE A 524 ? 0.3319 0.3507 0.4260 0.0412 0.0016 -0.0511 565 PHE A CE1 4154 C CE2 . PHE A 524 ? 0.3004 0.3166 0.3841 0.0379 0.0070 -0.0478 565 PHE A CE2 4155 C CZ . PHE A 524 ? 0.3215 0.3391 0.4122 0.0394 0.0056 -0.0500 565 PHE A CZ 4156 N N . TYR A 525 ? 0.2631 0.2724 0.3258 0.0465 -0.0091 -0.0434 566 TYR A N 4157 C CA . TYR A 525 ? 0.2448 0.2539 0.3046 0.0470 -0.0121 -0.0434 566 TYR A CA 4158 C C . TYR A 525 ? 0.2324 0.2376 0.2870 0.0522 -0.0167 -0.0429 566 TYR A C 4159 O O . TYR A 525 ? 0.2608 0.2666 0.3171 0.0534 -0.0209 -0.0445 566 TYR A O 4160 C CB . TYR A 525 ? 0.2257 0.2347 0.2799 0.0441 -0.0091 -0.0412 566 TYR A CB 4161 C CG . TYR A 525 ? 0.2359 0.2492 0.2953 0.0391 -0.0061 -0.0423 566 TYR A CG 4162 C CD1 . TYR A 525 ? 0.2425 0.2575 0.3050 0.0365 -0.0022 -0.0427 566 TYR A CD1 4163 C CD2 . TYR A 525 ? 0.2468 0.2621 0.3076 0.0372 -0.0073 -0.0430 566 TYR A CD2 4164 C CE1 . TYR A 525 ? 0.2292 0.2476 0.2955 0.0323 0.0007 -0.0437 566 TYR A CE1 4165 C CE2 . TYR A 525 ? 0.2434 0.2623 0.3083 0.0328 -0.0043 -0.0438 566 TYR A CE2 4166 C CZ . TYR A 525 ? 0.2324 0.2528 0.2999 0.0305 -0.0002 -0.0441 566 TYR A CZ 4167 O OH . TYR A 525 ? 0.2664 0.2899 0.3373 0.0267 0.0028 -0.0449 566 TYR A OH 4168 N N . ASP A 526 ? 0.2427 0.2437 0.2905 0.0554 -0.0161 -0.0405 567 ASP A N 4169 C CA . ASP A 526 ? 0.2550 0.2516 0.2955 0.0606 -0.0200 -0.0395 567 ASP A CA 4170 C C . ASP A 526 ? 0.2729 0.2650 0.3086 0.0648 -0.0194 -0.0376 567 ASP A C 4171 O O . ASP A 526 ? 0.2839 0.2724 0.3118 0.0667 -0.0177 -0.0346 567 ASP A O 4172 C CB . ASP A 526 ? 0.2358 0.2309 0.2689 0.0601 -0.0193 -0.0374 567 ASP A CB 4173 C CG . ASP A 526 ? 0.2627 0.2537 0.2884 0.0653 -0.0238 -0.0369 567 ASP A CG 4174 O OD1 . ASP A 526 ? 0.3132 0.3028 0.3398 0.0692 -0.0284 -0.0387 567 ASP A OD1 4175 O OD2 . ASP A 526 ? 0.2758 0.2648 0.2945 0.0655 -0.0228 -0.0347 567 ASP A OD2 4176 N N . PRO A 527 ? 0.2840 0.2766 0.3251 0.0663 -0.0206 -0.0393 568 PRO A N 4177 C CA . PRO A 527 ? 0.2921 0.2808 0.3295 0.0697 -0.0194 -0.0373 568 PRO A CA 4178 C C . PRO A 527 ? 0.2973 0.2802 0.3246 0.0755 -0.0219 -0.0351 568 PRO A C 4179 O O . PRO A 527 ? 0.3220 0.3010 0.3438 0.0776 -0.0191 -0.0320 568 PRO A O 4180 C CB . PRO A 527 ? 0.3008 0.2909 0.3458 0.0710 -0.0219 -0.0401 568 PRO A CB 4181 C CG . PRO A 527 ? 0.3090 0.3047 0.3631 0.0668 -0.0225 -0.0433 568 PRO A CG 4182 C CD . PRO A 527 ? 0.3060 0.3030 0.3573 0.0643 -0.0224 -0.0428 568 PRO A CD 4183 N N A MET A 528 ? 0.2988 0.2809 0.3236 0.0782 -0.0269 -0.0365 569 MET A N 4184 N N B MET A 528 ? 0.2982 0.2804 0.3232 0.0780 -0.0269 -0.0366 569 MET A N 4185 C CA A MET A 528 ? 0.3061 0.2823 0.3203 0.0843 -0.0295 -0.0345 569 MET A CA 4186 C CA B MET A 528 ? 0.3033 0.2799 0.3183 0.0841 -0.0300 -0.0350 569 MET A CA 4187 C C A MET A 528 ? 0.3027 0.2772 0.3092 0.0836 -0.0274 -0.0319 569 MET A C 4188 C C B MET A 528 ? 0.2981 0.2732 0.3055 0.0836 -0.0284 -0.0326 569 MET A C 4189 O O A MET A 528 ? 0.2902 0.2595 0.2869 0.0883 -0.0281 -0.0295 569 MET A O 4190 O O B MET A 528 ? 0.2895 0.2598 0.2877 0.0884 -0.0305 -0.0311 569 MET A O 4191 C CB A MET A 528 ? 0.3283 0.3035 0.3427 0.0885 -0.0366 -0.0376 569 MET A CB 4192 C CB B MET A 528 ? 0.3210 0.2976 0.3378 0.0874 -0.0370 -0.0384 569 MET A CB 4193 C CG A MET A 528 ? 0.3623 0.3386 0.3840 0.0901 -0.0394 -0.0402 569 MET A CG 4194 C CG B MET A 528 ? 0.3405 0.3195 0.3665 0.0877 -0.0394 -0.0415 569 MET A CG 4195 S SD A MET A 528 ? 0.4324 0.4046 0.4507 0.0932 -0.0362 -0.0374 569 MET A SD 4196 S SD B MET A 528 ? 0.4421 0.4188 0.4673 0.0938 -0.0483 -0.0448 569 MET A SD 4197 C CE A MET A 528 ? 0.4132 0.3773 0.4161 0.1003 -0.0371 -0.0337 569 MET A CE 4198 C CE B MET A 528 ? 0.3961 0.3799 0.4349 0.0886 -0.0507 -0.0492 569 MET A CE 4199 N N . PHE A 529 ? 0.2838 0.2626 0.2947 0.0779 -0.0246 -0.0323 570 PHE A N 4200 C CA . PHE A 529 ? 0.2822 0.2600 0.2868 0.0769 -0.0229 -0.0301 570 PHE A CA 4201 C C . PHE A 529 ? 0.2963 0.2725 0.2961 0.0800 -0.0279 -0.0312 570 PHE A C 4202 O O . PHE A 529 ? 0.2980 0.2719 0.2905 0.0810 -0.0272 -0.0292 570 PHE A O 4203 C CB . PHE A 529 ? 0.2962 0.2702 0.2941 0.0781 -0.0181 -0.0258 570 PHE A CB 4204 C CG . PHE A 529 ? 0.2906 0.2677 0.2945 0.0730 -0.0129 -0.0251 570 PHE A CG 4205 C CD1 . PHE A 529 ? 0.2883 0.2678 0.2930 0.0683 -0.0095 -0.0242 570 PHE A CD1 4206 C CD2 . PHE A 529 ? 0.2782 0.2558 0.2873 0.0729 -0.0118 -0.0258 570 PHE A CD2 4207 C CE1 . PHE A 529 ? 0.2896 0.2720 0.2999 0.0637 -0.0052 -0.0241 570 PHE A CE1 4208 C CE2 . PHE A 529 ? 0.3090 0.2895 0.3240 0.0682 -0.0073 -0.0257 570 PHE A CE2 4209 C CZ . PHE A 529 ? 0.2982 0.2810 0.3136 0.0636 -0.0041 -0.0249 570 PHE A CZ 4210 N N . LYS A 530 ? 0.2814 0.2589 0.2860 0.0814 -0.0331 -0.0347 571 LYS A N 4211 C CA . LYS A 530 ? 0.2979 0.2741 0.2993 0.0841 -0.0385 -0.0365 571 LYS A CA 4212 C C . LYS A 530 ? 0.2853 0.2654 0.2901 0.0794 -0.0381 -0.0375 571 LYS A C 4213 O O . LYS A 530 ? 0.2903 0.2683 0.2891 0.0814 -0.0407 -0.0373 571 LYS A O 4214 C CB . LYS A 530 ? 0.3025 0.2792 0.3093 0.0870 -0.0446 -0.0403 571 LYS A CB 4215 C CG . LYS A 530 ? 0.3124 0.2952 0.3324 0.0821 -0.0445 -0.0433 571 LYS A CG 4216 C CD . LYS A 530 ? 0.3307 0.3132 0.3555 0.0858 -0.0510 -0.0469 571 LYS A CD 4217 C CE . LYS A 530 ? 0.3559 0.3445 0.3945 0.0812 -0.0511 -0.0501 571 LYS A CE 4218 N NZ . LYS A 530 ? 0.3913 0.3801 0.4360 0.0846 -0.0580 -0.0540 571 LYS A NZ 4219 N N . TYR A 531 ? 0.2795 0.2648 0.2931 0.0734 -0.0351 -0.0384 572 TYR A N 4220 C CA . TYR A 531 ? 0.2649 0.2535 0.2811 0.0690 -0.0344 -0.0390 572 TYR A CA 4221 C C . TYR A 531 ? 0.2659 0.2527 0.2743 0.0680 -0.0302 -0.0355 572 TYR A C 4222 O O . TYR A 531 ? 0.2666 0.2531 0.2717 0.0676 -0.0313 -0.0352 572 TYR A O 4223 C CB . TYR A 531 ? 0.2668 0.2612 0.2940 0.0632 -0.0320 -0.0408 572 TYR A CB 4224 C CG . TYR A 531 ? 0.2697 0.2661 0.3056 0.0642 -0.0358 -0.0442 572 TYR A CG 4225 C CD1 . TYR A 531 ? 0.3042 0.3004 0.3423 0.0665 -0.0416 -0.0469 572 TYR A CD1 4226 C CD2 . TYR A 531 ? 0.3004 0.2986 0.3424 0.0631 -0.0337 -0.0449 572 TYR A CD2 4227 C CE1 . TYR A 531 ? 0.3263 0.3244 0.3733 0.0674 -0.0453 -0.0501 572 TYR A CE1 4228 C CE2 . TYR A 531 ? 0.3124 0.3125 0.3628 0.0641 -0.0371 -0.0480 572 TYR A CE2 4229 C CZ . TYR A 531 ? 0.3206 0.3206 0.3736 0.0662 -0.0430 -0.0506 572 TYR A CZ 4230 O OH . TYR A 531 ? 0.3845 0.3866 0.4469 0.0672 -0.0465 -0.0538 572 TYR A OH 4231 N N . HIS A 532 ? 0.2610 0.2465 0.2670 0.0677 -0.0257 -0.0328 573 HIS A N 4232 C CA . HIS A 532 ? 0.2639 0.2471 0.2625 0.0675 -0.0219 -0.0293 573 HIS A CA 4233 C C . HIS A 532 ? 0.2661 0.2444 0.2549 0.0729 -0.0247 -0.0279 573 HIS A C 4234 O O . HIS A 532 ? 0.2547 0.2322 0.2388 0.0724 -0.0238 -0.0265 573 HIS A O 4235 C CB . HIS A 532 ? 0.2583 0.2400 0.2557 0.0676 -0.0173 -0.0267 573 HIS A CB 4236 C CG . HIS A 532 ? 0.2675 0.2534 0.2722 0.0619 -0.0134 -0.0271 573 HIS A CG 4237 N ND1 . HIS A 532 ? 0.2549 0.2441 0.2678 0.0598 -0.0139 -0.0297 573 HIS A ND1 4238 C CD2 . HIS A 532 ? 0.2761 0.2634 0.2810 0.0582 -0.0090 -0.0253 573 HIS A CD2 4239 C CE1 . HIS A 532 ? 0.2841 0.2763 0.3013 0.0552 -0.0097 -0.0295 573 HIS A CE1 4240 N NE2 . HIS A 532 ? 0.2801 0.2711 0.2926 0.0541 -0.0069 -0.0269 573 HIS A NE2 4241 N N . LEU A 533 ? 0.2724 0.2469 0.2576 0.0785 -0.0279 -0.0283 574 LEU A N 4242 C CA . LEU A 533 ? 0.2689 0.2382 0.2439 0.0842 -0.0306 -0.0271 574 LEU A CA 4243 C C . LEU A 533 ? 0.2722 0.2425 0.2471 0.0841 -0.0351 -0.0296 574 LEU A C 4244 O O . LEU A 533 ? 0.2786 0.2463 0.2460 0.0858 -0.0349 -0.0279 574 LEU A O 4245 C CB . LEU A 533 ? 0.2902 0.2552 0.2613 0.0904 -0.0338 -0.0275 574 LEU A CB 4246 C CG . LEU A 533 ? 0.3065 0.2655 0.2658 0.0971 -0.0368 -0.0264 574 LEU A CG 4247 C CD1 . LEU A 533 ? 0.3219 0.2774 0.2726 0.0982 -0.0316 -0.0217 574 LEU A CD1 4248 C CD2 . LEU A 533 ? 0.3486 0.3035 0.3046 0.1032 -0.0404 -0.0271 574 LEU A CD2 4249 N N . THR A 534 ? 0.2634 0.2375 0.2470 0.0818 -0.0386 -0.0333 575 THR A N 4250 C CA . THR A 534 ? 0.2595 0.2352 0.2451 0.0810 -0.0428 -0.0359 575 THR A CA 4251 C C . THR A 534 ? 0.2571 0.2348 0.2420 0.0765 -0.0391 -0.0342 575 THR A C 4252 O O . THR A 534 ? 0.2695 0.2455 0.2491 0.0779 -0.0409 -0.0340 575 THR A O 4253 C CB . THR A 534 ? 0.2872 0.2670 0.2839 0.0789 -0.0464 -0.0400 575 THR A CB 4254 O OG1 . THR A 534 ? 0.2856 0.2625 0.2812 0.0843 -0.0511 -0.0417 575 THR A OG1 4255 C CG2 . THR A 534 ? 0.2862 0.2681 0.2867 0.0771 -0.0500 -0.0424 575 THR A CG2 4256 N N . VAL A 535 ? 0.2514 0.2328 0.2415 0.0713 -0.0340 -0.0330 576 VAL A N 4257 C CA . VAL A 535 ? 0.2495 0.2329 0.2390 0.0670 -0.0304 -0.0314 576 VAL A CA 4258 C C . VAL A 535 ? 0.2610 0.2400 0.2402 0.0699 -0.0281 -0.0278 576 VAL A C 4259 O O . VAL A 535 ? 0.2676 0.2466 0.2436 0.0690 -0.0278 -0.0270 576 VAL A O 4260 C CB . VAL A 535 ? 0.2513 0.2391 0.2482 0.0611 -0.0257 -0.0311 576 VAL A CB 4261 C CG1 . VAL A 535 ? 0.2407 0.2301 0.2362 0.0571 -0.0220 -0.0292 576 VAL A CG1 4262 C CG2 . VAL A 535 ? 0.2531 0.2451 0.2599 0.0584 -0.0280 -0.0346 576 VAL A CG2 4263 N N . ALA A 536 ? 0.2555 0.2309 0.2295 0.0736 -0.0264 -0.0256 577 ALA A N 4264 C CA . ALA A 536 ? 0.2688 0.2397 0.2331 0.0769 -0.0240 -0.0221 577 ALA A CA 4265 C C . ALA A 536 ? 0.2790 0.2464 0.2360 0.0816 -0.0285 -0.0228 577 ALA A C 4266 O O . ALA A 536 ? 0.2633 0.2289 0.2143 0.0822 -0.0271 -0.0209 577 ALA A O 4267 C CB . ALA A 536 ? 0.2730 0.2403 0.2336 0.0803 -0.0214 -0.0195 577 ALA A CB 4268 N N . GLN A 537 ? 0.2796 0.2458 0.2369 0.0850 -0.0340 -0.0257 578 GLN A N 4269 C CA . GLN A 537 ? 0.2801 0.2430 0.2311 0.0895 -0.0392 -0.0272 578 GLN A CA 4270 C C . GLN A 537 ? 0.2874 0.2533 0.2415 0.0859 -0.0407 -0.0288 578 GLN A C 4271 O O . GLN A 537 ? 0.2941 0.2570 0.2410 0.0886 -0.0422 -0.0283 578 GLN A O 4272 C CB . GLN A 537 ? 0.3022 0.2635 0.2543 0.0938 -0.0454 -0.0305 578 GLN A CB 4273 C CG . GLN A 537 ? 0.3005 0.2575 0.2470 0.0988 -0.0445 -0.0287 578 GLN A CG 4274 C CD . GLN A 537 ? 0.3731 0.3290 0.3219 0.1025 -0.0507 -0.0322 578 GLN A CD 4275 O OE1 . GLN A 537 ? 0.3465 0.3053 0.3021 0.1011 -0.0556 -0.0361 578 GLN A OE1 4276 N NE2 . GLN A 537 ? 0.3800 0.3318 0.3234 0.1075 -0.0506 -0.0307 578 GLN A NE2 4277 N N . VAL A 538 ? 0.2682 0.2397 0.2327 0.0800 -0.0401 -0.0307 579 VAL A N 4278 C CA . VAL A 538 ? 0.2696 0.2439 0.2377 0.0764 -0.0414 -0.0321 579 VAL A CA 4279 C C . VAL A 538 ? 0.2579 0.2321 0.2215 0.0741 -0.0363 -0.0287 579 VAL A C 4280 O O . VAL A 538 ? 0.2631 0.2355 0.2214 0.0754 -0.0374 -0.0282 579 VAL A O 4281 C CB . VAL A 538 ? 0.2552 0.2353 0.2356 0.0708 -0.0416 -0.0347 579 VAL A CB 4282 C CG1 . VAL A 538 ? 0.2548 0.2375 0.2381 0.0669 -0.0418 -0.0354 579 VAL A CG1 4283 C CG2 . VAL A 538 ? 0.2643 0.2446 0.2502 0.0731 -0.0470 -0.0384 579 VAL A CG2 4284 N N . ARG A 539 ? 0.2476 0.2237 0.2135 0.0708 -0.0309 -0.0264 580 ARG A N 4285 C CA . ARG A 539 ? 0.2440 0.2204 0.2068 0.0683 -0.0263 -0.0234 580 ARG A CA 4286 C C . ARG A 539 ? 0.2709 0.2420 0.2230 0.0735 -0.0256 -0.0207 580 ARG A C 4287 O O . ARG A 539 ? 0.2605 0.2309 0.2088 0.0734 -0.0250 -0.0195 580 ARG A O 4288 C CB . ARG A 539 ? 0.2513 0.2303 0.2186 0.0643 -0.0210 -0.0217 580 ARG A CB 4289 C CG . ARG A 539 ? 0.2356 0.2198 0.2125 0.0589 -0.0208 -0.0239 580 ARG A CG 4290 C CD . ARG A 539 ? 0.2660 0.2520 0.2465 0.0559 -0.0160 -0.0225 580 ARG A CD 4291 N NE . ARG A 539 ? 0.2183 0.2092 0.2075 0.0509 -0.0155 -0.0247 580 ARG A NE 4292 C CZ . ARG A 539 ? 0.2470 0.2402 0.2406 0.0477 -0.0119 -0.0244 580 ARG A CZ 4293 N NH1 . ARG A 539 ? 0.2618 0.2530 0.2527 0.0488 -0.0087 -0.0220 580 ARG A NH1 4294 N NH2 . ARG A 539 ? 0.2113 0.2085 0.2121 0.0436 -0.0115 -0.0264 580 ARG A NH2 4295 N N . GLY A 540 ? 0.2588 0.2261 0.2062 0.0783 -0.0255 -0.0194 581 GLY A N 4296 C CA . GLY A 540 ? 0.2745 0.2363 0.2113 0.0837 -0.0243 -0.0165 581 GLY A CA 4297 C C . GLY A 540 ? 0.2787 0.2371 0.2087 0.0882 -0.0293 -0.0181 581 GLY A C 4298 O O . GLY A 540 ? 0.2764 0.2320 0.1991 0.0906 -0.0279 -0.0160 581 GLY A O 4299 N N . GLY A 541 ? 0.2808 0.2399 0.2139 0.0894 -0.0351 -0.0220 582 GLY A N 4300 C CA . GLY A 541 ? 0.2773 0.2334 0.2052 0.0935 -0.0407 -0.0242 582 GLY A CA 4301 C C . GLY A 541 ? 0.2817 0.2402 0.2112 0.0899 -0.0405 -0.0245 582 GLY A C 4302 O O . GLY A 541 ? 0.2970 0.2522 0.2190 0.0933 -0.0420 -0.0241 582 GLY A O 4303 N N . MET A 542 ? 0.2596 0.2238 0.1987 0.0831 -0.0385 -0.0252 583 MET A N 4304 C CA . MET A 542 ? 0.2532 0.2195 0.1938 0.0795 -0.0381 -0.0252 583 MET A CA 4305 C C . MET A 542 ? 0.2678 0.2318 0.2010 0.0806 -0.0335 -0.0213 583 MET A C 4306 O O . MET A 542 ? 0.2688 0.2308 0.1968 0.0823 -0.0349 -0.0212 583 MET A O 4307 C CB . MET A 542 ? 0.2397 0.2121 0.1913 0.0723 -0.0361 -0.0262 583 MET A CB 4308 C CG . MET A 542 ? 0.2586 0.2335 0.2182 0.0710 -0.0408 -0.0302 583 MET A CG 4309 S SD . MET A 542 ? 0.0892 0.0709 0.0611 0.0631 -0.0380 -0.0311 583 MET A SD 4310 C CE . MET A 542 ? 0.2869 0.2700 0.2590 0.0599 -0.0379 -0.0308 583 MET A CE 4311 N N . VAL A 543 ? 0.2568 0.2208 0.1896 0.0797 -0.0282 -0.0182 584 VAL A N 4312 C CA . VAL A 543 ? 0.2701 0.2319 0.1968 0.0807 -0.0235 -0.0143 584 VAL A CA 4313 C C . VAL A 543 ? 0.2780 0.2337 0.1935 0.0880 -0.0252 -0.0133 584 VAL A C 4314 O O . VAL A 543 ? 0.2851 0.2391 0.1955 0.0890 -0.0241 -0.0118 584 VAL A O 4315 C CB . VAL A 543 ? 0.2612 0.2236 0.1900 0.0791 -0.0179 -0.0114 584 VAL A CB 4316 C CG1 . VAL A 543 ? 0.2836 0.2430 0.2060 0.0813 -0.0131 -0.0072 584 VAL A CG1 4317 C CG2 . VAL A 543 ? 0.2437 0.2122 0.1828 0.0718 -0.0160 -0.0124 584 VAL A CG2 4318 N N . PHE A 544 ? 0.2982 0.2504 0.2098 0.0930 -0.0278 -0.0142 585 PHE A N 4319 C CA . PHE A 544 ? 0.2982 0.2440 0.1982 0.1004 -0.0297 -0.0134 585 PHE A CA 4320 C C . PHE A 544 ? 0.3110 0.2558 0.2077 0.1020 -0.0342 -0.0156 585 PHE A C 4321 O O . PHE A 544 ? 0.3168 0.2580 0.2051 0.1054 -0.0328 -0.0136 585 PHE A O 4322 C CB . PHE A 544 ? 0.3125 0.2551 0.2097 0.1055 -0.0334 -0.0149 585 PHE A CB 4323 C CG . PHE A 544 ? 0.3462 0.2815 0.2301 0.1138 -0.0341 -0.0132 585 PHE A CG 4324 C CD1 . PHE A 544 ? 0.3628 0.2943 0.2409 0.1173 -0.0293 -0.0092 585 PHE A CD1 4325 C CD2 . PHE A 544 ? 0.3649 0.2970 0.2422 0.1181 -0.0393 -0.0155 585 PHE A CD2 4326 C CE1 . PHE A 544 ? 0.3955 0.3199 0.2606 0.1252 -0.0294 -0.0073 585 PHE A CE1 4327 C CE2 . PHE A 544 ? 0.3676 0.2924 0.2314 0.1263 -0.0399 -0.0139 585 PHE A CE2 4328 C CZ . PHE A 544 ? 0.3659 0.2870 0.2237 0.1297 -0.0346 -0.0096 585 PHE A CZ 4329 N N A GLU A 545 ? 0.3062 0.2539 0.2094 0.0997 -0.0395 -0.0198 586 GLU A N 4330 N N B GLU A 545 ? 0.3074 0.2552 0.2107 0.0995 -0.0394 -0.0198 586 GLU A N 4331 C CA A GLU A 545 ? 0.3118 0.2585 0.2128 0.1010 -0.0443 -0.0224 586 GLU A CA 4332 C CA B GLU A 545 ? 0.3136 0.2602 0.2146 0.1011 -0.0444 -0.0225 586 GLU A CA 4333 C C A GLU A 545 ? 0.3000 0.2487 0.2015 0.0973 -0.0407 -0.0204 586 GLU A C 4334 C C B GLU A 545 ? 0.3016 0.2506 0.2040 0.0969 -0.0415 -0.0210 586 GLU A C 4335 O O A GLU A 545 ? 0.3107 0.2559 0.2045 0.1007 -0.0412 -0.0197 586 GLU A O 4336 O O B GLU A 545 ? 0.3096 0.2559 0.2061 0.0997 -0.0434 -0.0214 586 GLU A O 4337 C CB A GLU A 545 ? 0.3120 0.2622 0.2223 0.0982 -0.0500 -0.0271 586 GLU A CB 4338 C CB B GLU A 545 ? 0.3180 0.2675 0.2273 0.0992 -0.0505 -0.0272 586 GLU A CB 4339 C CG A GLU A 545 ? 0.3542 0.3020 0.2638 0.1027 -0.0551 -0.0298 586 GLU A CG 4340 C CG B GLU A 545 ? 0.3520 0.2988 0.2577 0.1027 -0.0569 -0.0305 586 GLU A CG 4341 C CD A GLU A 545 ? 0.4535 0.3951 0.3526 0.1104 -0.0604 -0.0314 586 GLU A CD 4342 C CD B GLU A 545 ? 0.3928 0.3328 0.2872 0.1113 -0.0605 -0.0310 586 GLU A CD 4343 O OE1 A GLU A 545 ? 0.4900 0.4282 0.3802 0.1132 -0.0590 -0.0295 586 GLU A OE1 4344 O OE1 B GLU A 545 ? 0.3789 0.3164 0.2690 0.1146 -0.0587 -0.0292 586 GLU A OE1 4345 O OE2 A GLU A 545 ? 0.4878 0.4279 0.3877 0.1137 -0.0662 -0.0348 586 GLU A OE2 4346 O OE2 B GLU A 545 ? 0.4299 0.3669 0.3194 0.1149 -0.0653 -0.0333 586 GLU A OE2 4347 N N . LEU A 546 ? 0.2901 0.2440 0.2003 0.0905 -0.0370 -0.0195 587 LEU A N 4348 C CA . LEU A 546 ? 0.2739 0.2301 0.1854 0.0866 -0.0338 -0.0178 587 LEU A CA 4349 C C . LEU A 546 ? 0.2918 0.2441 0.1943 0.0902 -0.0294 -0.0139 587 LEU A C 4350 O O . LEU A 546 ? 0.3085 0.2599 0.2075 0.0905 -0.0289 -0.0130 587 LEU A O 4351 C CB . LEU A 546 ? 0.2635 0.2256 0.1850 0.0792 -0.0301 -0.0172 587 LEU A CB 4352 C CG . LEU A 546 ? 0.2500 0.2161 0.1808 0.0752 -0.0338 -0.0209 587 LEU A CG 4353 C CD1 . LEU A 546 ? 0.2318 0.2027 0.1711 0.0697 -0.0302 -0.0204 587 LEU A CD1 4354 C CD2 . LEU A 546 ? 0.2867 0.2544 0.2194 0.0728 -0.0360 -0.0223 587 LEU A CD2 4355 N N . ALA A 547 ? 0.2806 0.2305 0.1795 0.0930 -0.0261 -0.0113 588 ALA A N 4356 C CA . ALA A 547 ? 0.2969 0.2432 0.1883 0.0962 -0.0210 -0.0070 588 ALA A CA 4357 C C . ALA A 547 ? 0.3061 0.2457 0.1853 0.1043 -0.0233 -0.0067 588 ALA A C 4358 O O . ALA A 547 ? 0.3305 0.2671 0.2032 0.1070 -0.0194 -0.0035 588 ALA A O 4359 C CB . ALA A 547 ? 0.2988 0.2453 0.1922 0.0955 -0.0156 -0.0039 588 ALA A CB 4360 N N A ASN A 548 ? 0.3186 0.2558 0.1949 0.1082 -0.0291 -0.0099 589 ASN A N 4361 N N B ASN A 548 ? 0.3170 0.2544 0.1936 0.1079 -0.0294 -0.0102 589 ASN A N 4362 C CA A ASN A 548 ? 0.3286 0.2588 0.1923 0.1166 -0.0312 -0.0096 589 ASN A CA 4363 C CA B ASN A 548 ? 0.3257 0.2562 0.1900 0.1163 -0.0321 -0.0103 589 ASN A CA 4364 C C A ASN A 548 ? 0.3438 0.2721 0.2037 0.1193 -0.0377 -0.0133 589 ASN A C 4365 C C B ASN A 548 ? 0.3393 0.2679 0.2003 0.1193 -0.0395 -0.0145 589 ASN A C 4366 O O A ASN A 548 ? 0.3424 0.2650 0.1911 0.1257 -0.0383 -0.0125 589 ASN A O 4367 O O B ASN A 548 ? 0.3386 0.2611 0.1884 0.1265 -0.0415 -0.0145 589 ASN A O 4368 C CB A ASN A 548 ? 0.3333 0.2602 0.1934 0.1211 -0.0327 -0.0098 589 ASN A CB 4369 C CB B ASN A 548 ? 0.3303 0.2576 0.1911 0.1206 -0.0325 -0.0098 589 ASN A CB 4370 C CG A ASN A 548 ? 0.3792 0.2993 0.2268 0.1285 -0.0295 -0.0062 589 ASN A CG 4371 C CG B ASN A 548 ? 0.3347 0.2616 0.1952 0.1201 -0.0250 -0.0050 589 ASN A CG 4372 O OD1 A ASN A 548 ? 0.3825 0.3019 0.2278 0.1283 -0.0230 -0.0019 589 ASN A OD1 4373 O OD1 B ASN A 548 ? 0.3720 0.2945 0.2241 0.1243 -0.0208 -0.0013 589 ASN A OD1 4374 N ND2 A ASN A 548 ? 0.4404 0.3552 0.2798 0.1355 -0.0339 -0.0078 589 ASN A ND2 4375 N ND2 B ASN A 548 ? 0.3573 0.2885 0.2272 0.1152 -0.0232 -0.0050 589 ASN A ND2 4376 N N A SER A 549 ? 0.3240 0.2567 0.1930 0.1149 -0.0425 -0.0174 590 SER A N 4377 N N B SER A 549 ? 0.3264 0.2596 0.1967 0.1143 -0.0435 -0.0182 590 SER A N 4378 C CA A SER A 549 ? 0.3340 0.2651 0.2010 0.1171 -0.0493 -0.0214 590 SER A CA 4379 C CA B SER A 549 ? 0.3410 0.2723 0.2089 0.1171 -0.0505 -0.0222 590 SER A CA 4380 C C A SER A 549 ? 0.3329 0.2620 0.1938 0.1184 -0.0476 -0.0198 590 SER A C 4381 C C B SER A 549 ? 0.3346 0.2645 0.1975 0.1177 -0.0491 -0.0210 590 SER A C 4382 O O A SER A 549 ? 0.3146 0.2465 0.1784 0.1142 -0.0420 -0.0168 590 SER A O 4383 O O B SER A 549 ? 0.3164 0.2504 0.1851 0.1120 -0.0452 -0.0193 590 SER A O 4384 C CB A SER A 549 ? 0.3215 0.2583 0.2012 0.1109 -0.0533 -0.0253 590 SER A CB 4385 C CB B SER A 549 ? 0.3331 0.2696 0.2130 0.1117 -0.0551 -0.0264 590 SER A CB 4386 O OG A SER A 549 ? 0.3057 0.2410 0.1849 0.1132 -0.0603 -0.0296 590 SER A OG 4387 O OG B SER A 549 ? 0.3678 0.3054 0.2524 0.1116 -0.0566 -0.0278 590 SER A OG 4388 N N . ILE A 550 ? 0.3402 0.2642 0.1923 0.1247 -0.0524 -0.0220 591 ILE A N 4389 C CA A ILE A 550 ? 0.3425 0.2644 0.1886 0.1263 -0.0512 -0.0209 591 ILE A CA 4390 C CA B ILE A 550 ? 0.3388 0.2608 0.1851 0.1261 -0.0509 -0.0207 591 ILE A CA 4391 C C . ILE A 550 ? 0.3260 0.2532 0.1818 0.1193 -0.0521 -0.0224 591 ILE A C 4392 O O . ILE A 550 ? 0.3332 0.2624 0.1902 0.1161 -0.0471 -0.0196 591 ILE A O 4393 C CB A ILE A 550 ? 0.3534 0.2685 0.1880 0.1345 -0.0569 -0.0234 591 ILE A CB 4394 C CB B ILE A 550 ? 0.3459 0.2609 0.1798 0.1346 -0.0559 -0.0227 591 ILE A CB 4395 C CG1 A ILE A 550 ? 0.4102 0.3192 0.2330 0.1419 -0.0547 -0.0207 591 ILE A CG1 4396 C CG1 B ILE A 550 ? 0.3566 0.2662 0.1812 0.1414 -0.0558 -0.0215 591 ILE A CG1 4397 C CG2 A ILE A 550 ? 0.3406 0.2543 0.1710 0.1352 -0.0565 -0.0231 591 ILE A CG2 4398 C CG2 B ILE A 550 ? 0.3528 0.2651 0.1792 0.1367 -0.0528 -0.0203 591 ILE A CG2 4399 C CD1 A ILE A 550 ? 0.4199 0.3287 0.2401 0.1413 -0.0457 -0.0148 591 ILE A CD1 4400 C CD1 B ILE A 550 ? 0.2814 0.1838 0.0933 0.1503 -0.0611 -0.0238 591 ILE A CD1 4401 N N . VAL A 551 ? 0.3394 0.2689 0.2025 0.1172 -0.0583 -0.0270 592 VAL A N 4402 C CA . VAL A 551 ? 0.3310 0.2660 0.2049 0.1102 -0.0591 -0.0286 592 VAL A CA 4403 C C . VAL A 551 ? 0.3151 0.2559 0.2001 0.1037 -0.0564 -0.0280 592 VAL A C 4404 O O . VAL A 551 ? 0.3214 0.2624 0.2091 0.1046 -0.0586 -0.0296 592 VAL A O 4405 C CB . VAL A 551 ? 0.3417 0.2759 0.2183 0.1114 -0.0670 -0.0336 592 VAL A CB 4406 C CG1 . VAL A 551 ? 0.3604 0.2998 0.2482 0.1044 -0.0676 -0.0351 592 VAL A CG1 4407 C CG2 . VAL A 551 ? 0.3942 0.3222 0.2592 0.1183 -0.0700 -0.0345 592 VAL A CG2 4408 N N . GLN A 552 ? 0.3147 0.2600 0.2061 0.0974 -0.0519 -0.0259 593 GLN A N 4409 C CA . GLN A 552 ? 0.2920 0.2428 0.1937 0.0912 -0.0493 -0.0255 593 GLN A CA 4410 C C . GLN A 552 ? 0.2928 0.2458 0.2027 0.0896 -0.0549 -0.0298 593 GLN A C 4411 O O . GLN A 552 ? 0.2968 0.2497 0.2093 0.0895 -0.0597 -0.0329 593 GLN A O 4412 C CB . GLN A 552 ? 0.2839 0.2392 0.1913 0.0848 -0.0450 -0.0235 593 GLN A CB 4413 C CG . GLN A 552 ? 0.3333 0.2875 0.2354 0.0854 -0.0388 -0.0192 593 GLN A CG 4414 C CD . GLN A 552 ? 0.4048 0.3629 0.3120 0.0798 -0.0354 -0.0176 593 GLN A CD 4415 O OE1 . GLN A 552 ? 0.5747 0.5350 0.4866 0.0767 -0.0379 -0.0196 593 GLN A OE1 4416 N NE2 . GLN A 552 ? 0.5603 0.5193 0.4667 0.0785 -0.0297 -0.0141 593 GLN A NE2 4417 N N . PRO A 553 ? 0.2916 0.2467 0.2066 0.0881 -0.0542 -0.0301 594 PRO A N 4418 C CA . PRO A 553 ? 0.2936 0.2504 0.2163 0.0874 -0.0595 -0.0342 594 PRO A CA 4419 C C . PRO A 553 ? 0.3063 0.2690 0.2413 0.0800 -0.0587 -0.0352 594 PRO A C 4420 O O . PRO A 553 ? 0.2965 0.2626 0.2393 0.0768 -0.0580 -0.0359 594 PRO A O 4421 C CB . PRO A 553 ? 0.3083 0.2644 0.2303 0.0893 -0.0583 -0.0335 594 PRO A CB 4422 C CG . PRO A 553 ? 0.3117 0.2692 0.2320 0.0868 -0.0510 -0.0291 594 PRO A CG 4423 C CD . PRO A 553 ? 0.2985 0.2534 0.2110 0.0885 -0.0490 -0.0269 594 PRO A CD 4424 N N . PHE A 554 ? 0.2752 0.2388 0.2114 0.0775 -0.0588 -0.0352 595 PHE A N 4425 C CA . PHE A 554 ? 0.2867 0.2553 0.2334 0.0710 -0.0581 -0.0360 595 PHE A CA 4426 C C . PHE A 554 ? 0.2890 0.2568 0.2393 0.0718 -0.0642 -0.0397 595 PHE A C 4427 O O . PHE A 554 ? 0.3165 0.2803 0.2597 0.0759 -0.0670 -0.0403 595 PHE A O 4428 C CB . PHE A 554 ? 0.2680 0.2382 0.2133 0.0674 -0.0531 -0.0328 595 PHE A CB 4429 C CG . PHE A 554 ? 0.2654 0.2371 0.2088 0.0656 -0.0468 -0.0292 595 PHE A CG 4430 C CD1 . PHE A 554 ? 0.2697 0.2429 0.2163 0.0647 -0.0451 -0.0290 595 PHE A CD1 4431 C CD2 . PHE A 554 ? 0.2922 0.2637 0.2312 0.0646 -0.0427 -0.0261 595 PHE A CD2 4432 C CE1 . PHE A 554 ? 0.2765 0.2510 0.2220 0.0629 -0.0394 -0.0258 595 PHE A CE1 4433 C CE2 . PHE A 554 ? 0.2731 0.2459 0.2113 0.0628 -0.0370 -0.0229 595 PHE A CE2 4434 C CZ . PHE A 554 ? 0.2519 0.2263 0.1935 0.0619 -0.0355 -0.0228 595 PHE A CZ 4435 N N . ASP A 555 ? 0.2777 0.2490 0.2391 0.0679 -0.0660 -0.0420 596 ASP A N 4436 C CA . ASP A 555 ? 0.2696 0.2406 0.2364 0.0679 -0.0714 -0.0454 596 ASP A CA 4437 C C . ASP A 555 ? 0.2734 0.2484 0.2481 0.0616 -0.0686 -0.0445 596 ASP A C 4438 O O . ASP A 555 ? 0.2672 0.2462 0.2512 0.0569 -0.0666 -0.0445 596 ASP A O 4439 C CB . ASP A 555 ? 0.2528 0.2241 0.2270 0.0693 -0.0766 -0.0493 596 ASP A CB 4440 C CG . ASP A 555 ? 0.3277 0.2974 0.3059 0.0709 -0.0833 -0.0532 596 ASP A CG 4441 O OD1 . ASP A 555 ? 0.3124 0.2819 0.2907 0.0692 -0.0832 -0.0528 596 ASP A OD1 4442 O OD2 . ASP A 555 ? 0.3602 0.3287 0.3421 0.0738 -0.0889 -0.0568 596 ASP A OD2 4443 N N . CYS A 556 ? 0.2598 0.2333 0.2302 0.0615 -0.0683 -0.0434 597 CYS A N 4444 C CA . CYS A 556 ? 0.2664 0.2432 0.2433 0.0558 -0.0656 -0.0423 597 CYS A CA 4445 C C . CYS A 556 ? 0.2614 0.2404 0.2504 0.0530 -0.0689 -0.0452 597 CYS A C 4446 O O . CYS A 556 ? 0.2614 0.2440 0.2579 0.0477 -0.0659 -0.0442 597 CYS A O 4447 C CB . CYS A 556 ? 0.2655 0.2400 0.2359 0.0568 -0.0654 -0.0410 597 CYS A CB 4448 S SG . CYS A 556 ? 0.1113 0.0804 0.0774 0.0630 -0.0732 -0.0448 597 CYS A SG 4449 N N . ARG A 557 ? 0.2782 0.2551 0.2696 0.0566 -0.0751 -0.0490 598 ARG A N 4450 C CA . ARG A 557 ? 0.2739 0.2530 0.2780 0.0540 -0.0783 -0.0520 598 ARG A CA 4451 C C . ARG A 557 ? 0.2726 0.2563 0.2863 0.0496 -0.0749 -0.0514 598 ARG A C 4452 O O . ARG A 557 ? 0.2810 0.2676 0.3059 0.0455 -0.0747 -0.0523 598 ARG A O 4453 C CB . ARG A 557 ? 0.2863 0.2621 0.2910 0.0591 -0.0861 -0.0564 598 ARG A CB 4454 C CG . ARG A 557 ? 0.2838 0.2549 0.2799 0.0633 -0.0897 -0.0573 598 ARG A CG 4455 C CD . ARG A 557 ? 0.3084 0.2756 0.3032 0.0693 -0.0977 -0.0618 598 ARG A CD 4456 N NE . ARG A 557 ? 0.3134 0.2791 0.3014 0.0733 -0.0976 -0.0615 598 ARG A NE 4457 C CZ . ARG A 557 ? 0.3879 0.3499 0.3724 0.0792 -0.1039 -0.0649 598 ARG A CZ 4458 N NH1 . ARG A 557 ? 0.3727 0.3324 0.3607 0.0816 -0.1108 -0.0691 598 ARG A NH1 4459 N NH2 . ARG A 557 ? 0.3657 0.3261 0.3434 0.0829 -0.1034 -0.0642 598 ARG A NH2 4460 N N . ASP A 558 ? 0.2563 0.2405 0.2658 0.0506 -0.0722 -0.0500 599 ASP A N 4461 C CA . ASP A 558 ? 0.2472 0.2356 0.2652 0.0468 -0.0690 -0.0497 599 ASP A CA 4462 C C . ASP A 558 ? 0.2369 0.2285 0.2571 0.0411 -0.0627 -0.0464 599 ASP A C 4463 O O . ASP A 558 ? 0.2459 0.2411 0.2755 0.0371 -0.0604 -0.0464 599 ASP A O 4464 C CB . ASP A 558 ? 0.2463 0.2341 0.2589 0.0493 -0.0676 -0.0489 599 ASP A CB 4465 C CG . ASP A 558 ? 0.3008 0.2862 0.3139 0.0544 -0.0738 -0.0524 599 ASP A CG 4466 O OD1 . ASP A 558 ? 0.4308 0.4169 0.4533 0.0541 -0.0783 -0.0557 599 ASP A OD1 4467 O OD2 . ASP A 558 ? 0.2971 0.2795 0.3013 0.0589 -0.0746 -0.0521 599 ASP A OD2 4468 N N . TYR A 559 ? 0.2402 0.2305 0.2519 0.0410 -0.0601 -0.0437 600 TYR A N 4469 C CA . TYR A 559 ? 0.2125 0.2056 0.2264 0.0359 -0.0547 -0.0410 600 TYR A CA 4470 C C . TYR A 559 ? 0.2185 0.2126 0.2410 0.0331 -0.0563 -0.0422 600 TYR A C 4471 O O . TYR A 559 ? 0.2234 0.2206 0.2526 0.0285 -0.0527 -0.0410 600 TYR A O 4472 C CB . TYR A 559 ? 0.2198 0.2112 0.2233 0.0364 -0.0519 -0.0380 600 TYR A CB 4473 C CG . TYR A 559 ? 0.2159 0.2100 0.2176 0.0332 -0.0457 -0.0349 600 TYR A CG 4474 C CD1 . TYR A 559 ? 0.1969 0.1945 0.2056 0.0283 -0.0422 -0.0340 600 TYR A CD1 4475 C CD2 . TYR A 559 ? 0.2153 0.2080 0.2083 0.0353 -0.0434 -0.0329 600 TYR A CD2 4476 C CE1 . TYR A 559 ? 0.2099 0.2096 0.2165 0.0256 -0.0369 -0.0315 600 TYR A CE1 4477 C CE2 . TYR A 559 ? 0.2192 0.2141 0.2111 0.0325 -0.0382 -0.0304 600 TYR A CE2 4478 C CZ . TYR A 559 ? 0.2252 0.2236 0.2238 0.0277 -0.0352 -0.0299 600 TYR A CZ 4479 O OH . TYR A 559 ? 0.2168 0.2171 0.2139 0.0252 -0.0305 -0.0278 600 TYR A OH 4480 N N . ALA A 560 ? 0.2159 0.2073 0.2385 0.0359 -0.0617 -0.0446 601 ALA A N 4481 C CA . ALA A 560 ? 0.2273 0.2194 0.2587 0.0332 -0.0632 -0.0456 601 ALA A CA 4482 C C . ALA A 560 ? 0.2343 0.2297 0.2790 0.0304 -0.0632 -0.0473 601 ALA A C 4483 O O . ALA A 560 ? 0.2249 0.2226 0.2772 0.0261 -0.0603 -0.0462 601 ALA A O 4484 C CB . ALA A 560 ? 0.2280 0.2163 0.2574 0.0372 -0.0696 -0.0484 601 ALA A CB 4485 N N . VAL A 561 ? 0.2362 0.2315 0.2833 0.0329 -0.0661 -0.0497 602 VAL A N 4486 C CA . VAL A 561 ? 0.2389 0.2373 0.2989 0.0307 -0.0662 -0.0514 602 VAL A CA 4487 C C . VAL A 561 ? 0.2374 0.2396 0.3002 0.0259 -0.0590 -0.0484 602 VAL A C 4488 O O . VAL A 561 ? 0.2466 0.2513 0.3195 0.0221 -0.0568 -0.0482 602 VAL A O 4489 C CB . VAL A 561 ? 0.2626 0.2603 0.3232 0.0345 -0.0703 -0.0543 602 VAL A CB 4490 C CG1 . VAL A 561 ? 0.2689 0.2702 0.3429 0.0318 -0.0694 -0.0556 602 VAL A CG1 4491 C CG2 . VAL A 561 ? 0.2844 0.2783 0.3442 0.0390 -0.0779 -0.0578 602 VAL A CG2 4492 N N . VAL A 562 ? 0.2262 0.2285 0.2800 0.0262 -0.0552 -0.0460 603 VAL A N 4493 C CA . VAL A 562 ? 0.2169 0.2227 0.2732 0.0220 -0.0488 -0.0435 603 VAL A CA 4494 C C . VAL A 562 ? 0.2179 0.2244 0.2741 0.0182 -0.0450 -0.0409 603 VAL A C 4495 O O . VAL A 562 ? 0.2168 0.2261 0.2792 0.0144 -0.0407 -0.0397 603 VAL A O 4496 C CB . VAL A 562 ? 0.2575 0.2636 0.3064 0.0229 -0.0458 -0.0420 603 VAL A CB 4497 C CG1 . VAL A 562 ? 0.2377 0.2425 0.2861 0.0272 -0.0499 -0.0445 603 VAL A CG1 4498 C CG2 . VAL A 562 ? 0.2993 0.3036 0.3370 0.0235 -0.0437 -0.0394 603 VAL A CG2 4499 N N . LEU A 563 ? 0.2031 0.2071 0.2519 0.0194 -0.0461 -0.0399 604 LEU A N 4500 C CA . LEU A 563 ? 0.2140 0.2185 0.2623 0.0160 -0.0426 -0.0374 604 LEU A CA 4501 C C . LEU A 563 ? 0.2130 0.2189 0.2732 0.0132 -0.0428 -0.0383 604 LEU A C 4502 O O . LEU A 563 ? 0.2206 0.2283 0.2837 0.0095 -0.0382 -0.0361 604 LEU A O 4503 C CB . LEU A 563 ? 0.2084 0.2099 0.2479 0.0180 -0.0445 -0.0366 604 LEU A CB 4504 C CG . LEU A 563 ? 0.2050 0.2054 0.2330 0.0199 -0.0427 -0.0347 604 LEU A CG 4505 C CD1 . LEU A 563 ? 0.2136 0.2108 0.2339 0.0226 -0.0453 -0.0345 604 LEU A CD1 4506 C CD2 . LEU A 563 ? 0.2297 0.2326 0.2560 0.0160 -0.0365 -0.0316 604 LEU A CD2 4507 N N . ARG A 564 ? 0.2197 0.2247 0.2870 0.0151 -0.0481 -0.0415 605 ARG A N 4508 C CA . ARG A 564 ? 0.2218 0.2281 0.3020 0.0125 -0.0484 -0.0424 605 ARG A CA 4509 C C . ARG A 564 ? 0.2203 0.2301 0.3091 0.0096 -0.0442 -0.0420 605 ARG A C 4510 O O . ARG A 564 ? 0.2235 0.2350 0.3187 0.0059 -0.0401 -0.0402 605 ARG A O 4511 C CB . ARG A 564 ? 0.2230 0.2275 0.3095 0.0153 -0.0555 -0.0464 605 ARG A CB 4512 C CG . ARG A 564 ? 0.2644 0.2705 0.3661 0.0127 -0.0559 -0.0477 605 ARG A CG 4513 C CD . ARG A 564 ? 0.3227 0.3286 0.4260 0.0093 -0.0525 -0.0450 605 ARG A CD 4514 N NE . ARG A 564 ? 0.3577 0.3650 0.4763 0.0067 -0.0524 -0.0459 605 ARG A NE 4515 C CZ . ARG A 564 ? 0.4388 0.4445 0.5651 0.0077 -0.0577 -0.0486 605 ARG A CZ 4516 N NH1 . ARG A 564 ? 0.4101 0.4126 0.5294 0.0114 -0.0635 -0.0507 605 ARG A NH1 4517 N NH2 . ARG A 564 ? 0.4432 0.4505 0.5845 0.0051 -0.0571 -0.0493 605 ARG A NH2 4518 N N . LYS A 565 ? 0.2167 0.2276 0.3050 0.0113 -0.0448 -0.0433 606 LYS A N 4519 C CA . LYS A 565 ? 0.2168 0.2309 0.3118 0.0089 -0.0406 -0.0428 606 LYS A CA 4520 C C . LYS A 565 ? 0.2201 0.2356 0.3103 0.0055 -0.0336 -0.0390 606 LYS A C 4521 O O . LYS A 565 ? 0.2063 0.2239 0.3038 0.0024 -0.0294 -0.0378 606 LYS A O 4522 C CB . LYS A 565 ? 0.2323 0.2467 0.3242 0.0118 -0.0423 -0.0444 606 LYS A CB 4523 C CG . LYS A 565 ? 0.2611 0.2787 0.3598 0.0097 -0.0382 -0.0442 606 LYS A CG 4524 C CD . LYS A 565 ? 0.3030 0.3207 0.3988 0.0126 -0.0401 -0.0457 606 LYS A CD 4525 C CE . LYS A 565 ? 0.3057 0.3218 0.3876 0.0142 -0.0385 -0.0438 606 LYS A CE 4526 N NZ . LYS A 565 ? 0.3337 0.3492 0.4125 0.0176 -0.0409 -0.0454 606 LYS A NZ 4527 N N . TYR A 566 ? 0.1968 0.2109 0.2745 0.0064 -0.0323 -0.0371 607 TYR A N 4528 C CA . TYR A 566 ? 0.1908 0.2060 0.2637 0.0035 -0.0261 -0.0338 607 TYR A CA 4529 C C . TYR A 566 ? 0.1874 0.2022 0.2628 0.0008 -0.0241 -0.0319 607 TYR A C 4530 O O . TYR A 566 ? 0.1915 0.2078 0.2683 -0.0020 -0.0189 -0.0298 607 TYR A O 4531 C CB . TYR A 566 ? 0.1965 0.2102 0.2564 0.0051 -0.0257 -0.0323 607 TYR A CB 4532 C CG . TYR A 566 ? 0.1888 0.2025 0.2450 0.0078 -0.0270 -0.0336 607 TYR A CG 4533 C CD1 . TYR A 566 ? 0.1862 0.2020 0.2496 0.0077 -0.0267 -0.0352 607 TYR A CD1 4534 C CD2 . TYR A 566 ? 0.2169 0.2285 0.2627 0.0104 -0.0284 -0.0330 607 TYR A CD2 4535 C CE1 . TYR A 566 ? 0.2188 0.2343 0.2784 0.0103 -0.0278 -0.0362 607 TYR A CE1 4536 C CE2 . TYR A 566 ? 0.2149 0.2262 0.2569 0.0130 -0.0292 -0.0338 607 TYR A CE2 4537 C CZ . TYR A 566 ? 0.2267 0.2398 0.2754 0.0130 -0.0291 -0.0354 607 TYR A CZ 4538 O OH . TYR A 566 ? 0.2407 0.2533 0.2855 0.0157 -0.0300 -0.0361 607 TYR A OH 4539 N N . ALA A 567 ? 0.1964 0.2091 0.2722 0.0019 -0.0280 -0.0327 608 ALA A N 4540 C CA . ALA A 567 ? 0.1918 0.2039 0.2706 -0.0006 -0.0262 -0.0309 608 ALA A CA 4541 C C . ALA A 567 ? 0.2018 0.2159 0.2939 -0.0031 -0.0241 -0.0312 608 ALA A C 4542 O O . ALA A 567 ? 0.2114 0.2262 0.3055 -0.0060 -0.0191 -0.0286 608 ALA A O 4543 C CB . ALA A 567 ? 0.2033 0.2126 0.2808 0.0015 -0.0315 -0.0322 608 ALA A CB 4544 N N . ASP A 568 ? 0.2198 0.2347 0.3212 -0.0018 -0.0278 -0.0343 609 ASP A N 4545 C CA . ASP A 568 ? 0.2249 0.2420 0.3405 -0.0041 -0.0256 -0.0348 609 ASP A CA 4546 C C . ASP A 568 ? 0.2184 0.2379 0.3336 -0.0065 -0.0187 -0.0324 609 ASP A C 4547 O O . ASP A 568 ? 0.2086 0.2292 0.3304 -0.0093 -0.0139 -0.0305 609 ASP A O 4548 C CB . ASP A 568 ? 0.2379 0.2557 0.3628 -0.0021 -0.0307 -0.0387 609 ASP A CB 4549 C CG . ASP A 568 ? 0.2978 0.3133 0.4262 0.0001 -0.0376 -0.0415 609 ASP A CG 4550 O OD1 . ASP A 568 ? 0.3038 0.3175 0.4307 -0.0006 -0.0380 -0.0404 609 ASP A OD1 4551 O OD2 . ASP A 568 ? 0.3539 0.3694 0.4867 0.0027 -0.0428 -0.0450 609 ASP A OD2 4552 N N . LYS A 569 ? 0.2010 0.2211 0.3079 -0.0051 -0.0180 -0.0325 610 LYS A N 4553 C CA A LYS A 569 ? 0.2083 0.2306 0.3145 -0.0069 -0.0122 -0.0308 610 LYS A CA 4554 C CA B LYS A 569 ? 0.2072 0.2294 0.3133 -0.0069 -0.0122 -0.0309 610 LYS A CA 4555 C C . LYS A 569 ? 0.2106 0.2322 0.3104 -0.0092 -0.0068 -0.0272 610 LYS A C 4556 O O . LYS A 569 ? 0.2265 0.2495 0.3307 -0.0115 -0.0015 -0.0255 610 LYS A O 4557 C CB A LYS A 569 ? 0.2156 0.2383 0.3142 -0.0048 -0.0129 -0.0318 610 LYS A CB 4558 C CB B LYS A 569 ? 0.2072 0.2297 0.3055 -0.0047 -0.0132 -0.0318 610 LYS A CB 4559 C CG A LYS A 569 ? 0.2308 0.2553 0.3265 -0.0066 -0.0067 -0.0300 610 LYS A CG 4560 C CG B LYS A 569 ? 0.2115 0.2365 0.3125 -0.0058 -0.0088 -0.0316 610 LYS A CG 4561 C CD A LYS A 569 ? 0.2709 0.2951 0.3566 -0.0046 -0.0073 -0.0303 610 LYS A CD 4562 C CD B LYS A 569 ? 0.2002 0.2250 0.2919 -0.0037 -0.0096 -0.0321 610 LYS A CD 4563 C CE A LYS A 569 ? 0.2916 0.3176 0.3751 -0.0061 -0.0017 -0.0290 610 LYS A CE 4564 C CE B LYS A 569 ? 0.2221 0.2490 0.3143 -0.0048 -0.0050 -0.0316 610 LYS A CE 4565 N NZ A LYS A 569 ? 0.3188 0.3439 0.3921 -0.0073 0.0021 -0.0264 610 LYS A NZ 4566 N NZ B LYS A 569 ? 0.2307 0.2568 0.3111 -0.0037 -0.0042 -0.0308 610 LYS A NZ 4567 N N . ILE A 570 ? 0.1959 0.2154 0.2850 -0.0084 -0.0081 -0.0260 611 ILE A N 4568 C CA . ILE A 570 ? 0.1932 0.2121 0.2756 -0.0104 -0.0032 -0.0227 611 ILE A CA 4569 C C . ILE A 570 ? 0.1999 0.2182 0.2894 -0.0125 -0.0013 -0.0211 611 ILE A C 4570 O O . ILE A 570 ? 0.2067 0.2251 0.2953 -0.0145 0.0042 -0.0184 611 ILE A O 4571 C CB . ILE A 570 ? 0.2117 0.2287 0.2811 -0.0090 -0.0049 -0.0218 611 ILE A CB 4572 C CG1 . ILE A 570 ? 0.2382 0.2548 0.2997 -0.0106 -0.0001 -0.0187 611 ILE A CG1 4573 C CG2 . ILE A 570 ? 0.2038 0.2185 0.2728 -0.0076 -0.0098 -0.0226 611 ILE A CG2 4574 C CD1 . ILE A 570 ? 0.2330 0.2514 0.2925 -0.0113 0.0039 -0.0184 611 ILE A CD1 4575 N N . TYR A 571 ? 0.1989 0.2162 0.2952 -0.0119 -0.0057 -0.0227 612 TYR A N 4576 C CA . TYR A 571 ? 0.2243 0.2410 0.3292 -0.0139 -0.0041 -0.0214 612 TYR A CA 4577 C C . TYR A 571 ? 0.2203 0.2393 0.3360 -0.0159 0.0008 -0.0208 612 TYR A C 4578 O O . TYR A 571 ? 0.2183 0.2371 0.3360 -0.0180 0.0061 -0.0179 612 TYR A O 4579 C CB . TYR A 571 ? 0.2110 0.2264 0.3228 -0.0125 -0.0103 -0.0240 612 TYR A CB 4580 C CG . TYR A 571 ? 0.2858 0.3012 0.4107 -0.0146 -0.0090 -0.0235 612 TYR A CG 4581 C CD1 . TYR A 571 ? 0.3178 0.3314 0.4414 -0.0162 -0.0067 -0.0207 612 TYR A CD1 4582 C CD2 . TYR A 571 ? 0.3429 0.3603 0.4817 -0.0150 -0.0097 -0.0257 612 TYR A CD2 4583 C CE1 . TYR A 571 ? 0.3497 0.3632 0.4866 -0.0182 -0.0051 -0.0200 612 TYR A CE1 4584 C CE2 . TYR A 571 ? 0.3722 0.3897 0.5243 -0.0170 -0.0083 -0.0252 612 TYR A CE2 4585 C CZ . TYR A 571 ? 0.4045 0.4200 0.5555 -0.0186 -0.0058 -0.0223 612 TYR A CZ 4586 O OH . TYR A 571 ? 0.4974 0.5130 0.6626 -0.0206 -0.0040 -0.0216 612 TYR A OH 4587 N N . SER A 572 ? 0.2310 0.2521 0.3527 -0.0150 -0.0007 -0.0234 613 SER A N 4588 C CA . SER A 572 ? 0.2387 0.2622 0.3713 -0.0167 0.0038 -0.0231 613 SER A CA 4589 C C . SER A 572 ? 0.2499 0.2739 0.3756 -0.0181 0.0109 -0.0200 613 SER A C 4590 O O . SER A 572 ? 0.2597 0.2844 0.3921 -0.0200 0.0163 -0.0181 613 SER A O 4591 C CB . SER A 572 ? 0.2545 0.2801 0.3944 -0.0152 0.0006 -0.0265 613 SER A CB 4592 O OG A SER A 572 ? 0.2387 0.2637 0.3868 -0.0139 -0.0059 -0.0295 613 SER A OG 4593 O OG B SER A 572 ? 0.2800 0.3062 0.4102 -0.0140 0.0012 -0.0269 613 SER A OG 4594 N N . ILE A 573 ? 0.2248 0.2482 0.3371 -0.0170 0.0110 -0.0195 614 ILE A N 4595 C CA . ILE A 573 ? 0.2231 0.2466 0.3281 -0.0181 0.0171 -0.0169 614 ILE A CA 4596 C C . ILE A 573 ? 0.2298 0.2514 0.3325 -0.0197 0.0209 -0.0135 614 ILE A C 4597 O O . ILE A 573 ? 0.2426 0.2644 0.3466 -0.0211 0.0269 -0.0111 614 ILE A O 4598 C CB . ILE A 573 ? 0.2330 0.2562 0.3246 -0.0165 0.0158 -0.0173 614 ILE A CB 4599 C CG1 . ILE A 573 ? 0.2474 0.2726 0.3421 -0.0151 0.0137 -0.0202 614 ILE A CG1 4600 C CG2 . ILE A 573 ? 0.2438 0.2663 0.3261 -0.0175 0.0215 -0.0144 614 ILE A CG2 4601 C CD1 . ILE A 573 ? 0.2490 0.2737 0.3321 -0.0133 0.0115 -0.0209 614 ILE A CD1 4602 N N . SER A 574 ? 0.2354 0.2549 0.3341 -0.0193 0.0173 -0.0132 615 SER A N 4603 C CA . SER A 574 ? 0.2407 0.2580 0.3358 -0.0205 0.0203 -0.0099 615 SER A CA 4604 C C . SER A 574 ? 0.2581 0.2756 0.3658 -0.0223 0.0237 -0.0086 615 SER A C 4605 O O . SER A 574 ? 0.2563 0.2726 0.3623 -0.0236 0.0293 -0.0053 615 SER A O 4606 C CB . SER A 574 ? 0.2417 0.2569 0.3317 -0.0195 0.0152 -0.0103 615 SER A CB 4607 O OG . SER A 574 ? 0.2508 0.2637 0.3356 -0.0206 0.0181 -0.0070 615 SER A OG 4608 N N . MET A 575 ? 0.2548 0.2736 0.3750 -0.0222 0.0204 -0.0111 616 MET A N 4609 C CA . MET A 575 ? 0.2856 0.3045 0.4203 -0.0239 0.0226 -0.0103 616 MET A CA 4610 C C . MET A 575 ? 0.2933 0.3139 0.4343 -0.0253 0.0296 -0.0087 616 MET A C 4611 O O . MET A 575 ? 0.3089 0.3298 0.4623 -0.0268 0.0327 -0.0075 616 MET A O 4612 C CB . MET A 575 ? 0.2949 0.3146 0.4410 -0.0232 0.0162 -0.0140 616 MET A CB 4613 C CG . MET A 575 ? 0.3551 0.3723 0.4988 -0.0225 0.0111 -0.0145 616 MET A CG 4614 S SD . MET A 575 ? 0.1357 0.1503 0.2831 -0.0247 0.0151 -0.0105 616 MET A SD 4615 C CE . MET A 575 ? 0.4480 0.4644 0.6167 -0.0265 0.0173 -0.0111 616 MET A CE 4616 N N . LYS A 576 ? 0.3023 0.3241 0.4354 -0.0247 0.0324 -0.0085 617 LYS A N 4617 C CA . LYS A 576 ? 0.3180 0.3408 0.4534 -0.0257 0.0399 -0.0063 617 LYS A CA 4618 C C . LYS A 576 ? 0.3097 0.3298 0.4382 -0.0267 0.0458 -0.0019 617 LYS A C 4619 O O . LYS A 576 ? 0.3080 0.3283 0.4395 -0.0275 0.0527 0.0005 617 LYS A O 4620 C CB . LYS A 576 ? 0.3397 0.3640 0.4673 -0.0246 0.0408 -0.0076 617 LYS A CB 4621 C CG . LYS A 576 ? 0.3837 0.4104 0.5168 -0.0233 0.0353 -0.0118 617 LYS A CG 4622 C CD . LYS A 576 ? 0.4908 0.5202 0.6393 -0.0240 0.0372 -0.0131 617 LYS A CD 4623 C CE . LYS A 576 ? 0.5279 0.5594 0.6803 -0.0224 0.0313 -0.0173 617 LYS A CE 4624 N NZ . LYS A 576 ? 0.5454 0.5764 0.7028 -0.0214 0.0235 -0.0201 617 LYS A NZ 4625 N N . HIS A 577 ? 0.2846 0.3022 0.4045 -0.0264 0.0431 -0.0009 618 HIS A N 4626 C CA . HIS A 577 ? 0.2812 0.2958 0.3928 -0.0269 0.0478 0.0032 618 HIS A CA 4627 C C . HIS A 577 ? 0.2772 0.2897 0.3941 -0.0277 0.0458 0.0045 618 HIS A C 4628 O O . HIS A 577 ? 0.2666 0.2767 0.3735 -0.0272 0.0438 0.0056 618 HIS A O 4629 C CB . HIS A 577 ? 0.2808 0.2941 0.3753 -0.0256 0.0464 0.0035 618 HIS A CB 4630 C CG . HIS A 577 ? 0.2967 0.3119 0.3855 -0.0246 0.0474 0.0019 618 HIS A CG 4631 N ND1 . HIS A 577 ? 0.3561 0.3730 0.4431 -0.0235 0.0420 -0.0015 618 HIS A ND1 4632 C CD2 . HIS A 577 ? 0.2947 0.3101 0.3792 -0.0245 0.0531 0.0033 618 HIS A CD2 4633 C CE1 . HIS A 577 ? 0.3263 0.3445 0.4087 -0.0229 0.0443 -0.0022 618 HIS A CE1 4634 N NE2 . HIS A 577 ? 0.3668 0.3840 0.4474 -0.0235 0.0510 0.0006 618 HIS A NE2 4635 N N . PRO A 578 ? 0.2733 0.2865 0.4062 -0.0290 0.0464 0.0042 619 PRO A N 4636 C CA . PRO A 578 ? 0.2684 0.2798 0.4077 -0.0297 0.0436 0.0047 619 PRO A CA 4637 C C . PRO A 578 ? 0.2792 0.2871 0.4114 -0.0303 0.0478 0.0091 619 PRO A C 4638 O O . PRO A 578 ? 0.2777 0.2836 0.4066 -0.0300 0.0440 0.0092 619 PRO A O 4639 C CB . PRO A 578 ? 0.2779 0.2910 0.4367 -0.0311 0.0446 0.0038 619 PRO A CB 4640 C CG . PRO A 578 ? 0.2850 0.3001 0.4456 -0.0314 0.0512 0.0049 619 PRO A CG 4641 C CD . PRO A 578 ? 0.2799 0.2959 0.4262 -0.0297 0.0491 0.0032 619 PRO A CD 4642 N N . GLN A 579 ? 0.2912 0.2983 0.4201 -0.0307 0.0556 0.0127 620 GLN A N 4643 C CA A GLN A 579 ? 0.2970 0.3005 0.4180 -0.0309 0.0598 0.0171 620 GLN A CA 4644 C CA B GLN A 579 ? 0.2919 0.2954 0.4130 -0.0309 0.0597 0.0170 620 GLN A CA 4645 C C . GLN A 579 ? 0.2977 0.2994 0.4021 -0.0295 0.0561 0.0170 620 GLN A C 4646 O O . GLN A 579 ? 0.2956 0.2946 0.3963 -0.0295 0.0547 0.0186 620 GLN A O 4647 C CB A GLN A 579 ? 0.3149 0.3176 0.4334 -0.0310 0.0688 0.0207 620 GLN A CB 4648 C CB B GLN A 579 ? 0.3058 0.3083 0.4244 -0.0310 0.0687 0.0209 620 GLN A CB 4649 C CG A GLN A 579 ? 0.3375 0.3414 0.4733 -0.0325 0.0737 0.0218 620 GLN A CG 4650 C CG B GLN A 579 ? 0.3140 0.3122 0.4228 -0.0308 0.0726 0.0254 620 GLN A CG 4651 C CD A GLN A 579 ? 0.4080 0.4110 0.5415 -0.0324 0.0831 0.0256 620 GLN A CD 4652 C CD B GLN A 579 ? 0.3343 0.3305 0.4538 -0.0321 0.0730 0.0275 620 GLN A CD 4653 O OE1 A GLN A 579 ? 0.4399 0.4414 0.5584 -0.0310 0.0859 0.0270 620 GLN A OE1 4654 O OE1 B GLN A 579 ? 0.3901 0.3863 0.5217 -0.0333 0.0784 0.0295 620 GLN A OE1 4655 N NE2 A GLN A 579 ? 0.4185 0.4222 0.5674 -0.0337 0.0882 0.0271 620 GLN A NE2 4656 N NE2 B GLN A 579 ? 0.2665 0.2611 0.3825 -0.0320 0.0674 0.0268 620 GLN A NE2 4657 N N . GLU A 580 ? 0.2699 0.2732 0.3646 -0.0282 0.0543 0.0149 621 GLU A N 4658 C CA . GLU A 580 ? 0.2575 0.2593 0.3374 -0.0269 0.0510 0.0148 621 GLU A CA 4659 C C . GLU A 580 ? 0.2462 0.2479 0.3274 -0.0266 0.0434 0.0123 621 GLU A C 4660 O O . GLU A 580 ? 0.2701 0.2696 0.3421 -0.0259 0.0411 0.0132 621 GLU A O 4661 C CB . GLU A 580 ? 0.2706 0.2741 0.3413 -0.0257 0.0507 0.0130 621 GLU A CB 4662 C CG . GLU A 580 ? 0.3302 0.3329 0.3948 -0.0255 0.0580 0.0156 621 GLU A CG 4663 C CD . GLU A 580 ? 0.4092 0.4132 0.4854 -0.0265 0.0635 0.0164 621 GLU A CD 4664 O OE1 . GLU A 580 ? 0.3965 0.4034 0.4854 -0.0272 0.0614 0.0138 621 GLU A OE1 4665 O OE2 . GLU A 580 ? 0.5042 0.5064 0.5770 -0.0264 0.0702 0.0198 621 GLU A OE2 4666 N N . MET A 581 ? 0.2348 0.2388 0.3269 -0.0268 0.0393 0.0090 622 MET A N 4667 C CA . MET A 581 ? 0.2382 0.2418 0.3314 -0.0261 0.0321 0.0065 622 MET A CA 4668 C C . MET A 581 ? 0.2520 0.2528 0.3494 -0.0270 0.0322 0.0087 622 MET A C 4669 O O . MET A 581 ? 0.2497 0.2488 0.3416 -0.0262 0.0279 0.0083 622 MET A O 4670 C CB . MET A 581 ? 0.2373 0.2435 0.3410 -0.0258 0.0275 0.0023 622 MET A CB 4671 C CG . MET A 581 ? 0.2262 0.2349 0.3247 -0.0246 0.0266 0.0000 622 MET A CG 4672 S SD . MET A 581 ? 0.0618 0.0732 0.1720 -0.0237 0.0205 -0.0049 622 MET A SD 4673 C CE . MET A 581 ? 0.2466 0.2559 0.3544 -0.0223 0.0128 -0.0069 622 MET A CE 4674 N N . LYS A 582 ? 0.2532 0.2534 0.3601 -0.0285 0.0375 0.0112 623 LYS A N 4675 C CA . LYS A 582 ? 0.2670 0.2643 0.3785 -0.0295 0.0386 0.0138 623 LYS A CA 4676 C C . LYS A 582 ? 0.2680 0.2623 0.3651 -0.0289 0.0411 0.0173 623 LYS A C 4677 O O . LYS A 582 ? 0.2762 0.2682 0.3694 -0.0285 0.0377 0.0177 623 LYS A O 4678 C CB . LYS A 582 ? 0.2785 0.2759 0.4043 -0.0313 0.0442 0.0159 623 LYS A CB 4679 C CG . LYS A 582 ? 0.2615 0.2617 0.4030 -0.0319 0.0413 0.0123 623 LYS A CG 4680 C CD . LYS A 582 ? 0.3230 0.3233 0.4799 -0.0338 0.0471 0.0146 623 LYS A CD 4681 C CE . LYS A 582 ? 0.4049 0.4083 0.5775 -0.0342 0.0433 0.0105 623 LYS A CE 4682 N NZ . LYS A 582 ? 0.4954 0.5011 0.6780 -0.0352 0.0492 0.0113 623 LYS A NZ 4683 N N . THR A 583 ? 0.2878 0.2818 0.3767 -0.0287 0.0467 0.0197 624 THR A N 4684 C CA . THR A 583 ? 0.3126 0.3036 0.3875 -0.0279 0.0493 0.0231 624 THR A CA 4685 C C . THR A 583 ? 0.3124 0.3028 0.3759 -0.0265 0.0435 0.0214 624 THR A C 4686 O O . THR A 583 ? 0.3113 0.2989 0.3687 -0.0261 0.0427 0.0234 624 THR A O 4687 C CB . THR A 583 ? 0.3344 0.3254 0.4016 -0.0273 0.0556 0.0250 624 THR A CB 4688 O OG1 . THR A 583 ? 0.3858 0.3769 0.4638 -0.0285 0.0617 0.0271 624 THR A OG1 4689 C CG2 . THR A 583 ? 0.3750 0.3626 0.4272 -0.0262 0.0579 0.0283 624 THR A CG2 4690 N N . TYR A 584 ? 0.2945 0.2877 0.3555 -0.0257 0.0394 0.0178 625 TYR A N 4691 C CA . TYR A 584 ? 0.2965 0.2893 0.3463 -0.0242 0.0345 0.0164 625 TYR A CA 4692 C C . TYR A 584 ? 0.2908 0.2843 0.3455 -0.0238 0.0276 0.0133 625 TYR A C 4693 O O . TYR A 584 ? 0.2892 0.2828 0.3357 -0.0225 0.0235 0.0118 625 TYR A O 4694 C CB . TYR A 584 ? 0.2932 0.2881 0.3347 -0.0233 0.0348 0.0149 625 TYR A CB 4695 C CG . TYR A 584 ? 0.2931 0.2868 0.3282 -0.0233 0.0412 0.0178 625 TYR A CG 4696 C CD1 . TYR A 584 ? 0.3405 0.3311 0.3655 -0.0227 0.0430 0.0209 625 TYR A CD1 4697 C CD2 . TYR A 584 ? 0.3139 0.3093 0.3534 -0.0237 0.0455 0.0177 625 TYR A CD2 4698 C CE1 . TYR A 584 ? 0.3578 0.3467 0.3762 -0.0223 0.0489 0.0237 625 TYR A CE1 4699 C CE2 . TYR A 584 ? 0.3721 0.3661 0.4053 -0.0234 0.0516 0.0205 625 TYR A CE2 4700 C CZ . TYR A 584 ? 0.3812 0.3719 0.4036 -0.0226 0.0533 0.0234 625 TYR A CZ 4701 O OH . TYR A 584 ? 0.4219 0.4107 0.4373 -0.0219 0.0593 0.0261 625 TYR A OH 4702 N N . SER A 585 ? 0.2625 0.2563 0.3304 -0.0248 0.0265 0.0123 626 SER A N 4703 C CA . SER A 585 ? 0.2620 0.2559 0.3347 -0.0241 0.0200 0.0093 626 SER A CA 4704 C C . SER A 585 ? 0.2519 0.2481 0.3206 -0.0225 0.0154 0.0057 626 SER A C 4705 O O . SER A 585 ? 0.2451 0.2406 0.3078 -0.0211 0.0106 0.0042 626 SER A O 4706 C CB A SER A 585 ? 0.2759 0.2667 0.3431 -0.0237 0.0179 0.0109 626 SER A CB 4707 C CB B SER A 585 ? 0.2682 0.2591 0.3341 -0.0235 0.0178 0.0109 626 SER A CB 4708 O OG A SER A 585 ? 0.2841 0.2727 0.3565 -0.0251 0.0221 0.0143 626 SER A OG 4709 O OG B SER A 585 ? 0.2844 0.2748 0.3562 -0.0230 0.0121 0.0083 626 SER A OG 4710 N N . VAL A 586 ? 0.2371 0.2358 0.3095 -0.0227 0.0170 0.0043 627 VAL A N 4711 C CA . VAL A 586 ? 0.2302 0.2311 0.2987 -0.0212 0.0135 0.0011 627 VAL A CA 4712 C C . VAL A 586 ? 0.2388 0.2406 0.3175 -0.0206 0.0082 -0.0024 627 VAL A C 4713 O O . VAL A 586 ? 0.2644 0.2675 0.3551 -0.0215 0.0092 -0.0033 627 VAL A O 4714 C CB . VAL A 586 ? 0.2210 0.2241 0.2888 -0.0217 0.0178 0.0013 627 VAL A CB 4715 C CG1 . VAL A 586 ? 0.2267 0.2318 0.2901 -0.0200 0.0142 -0.0018 627 VAL A CG1 4716 C CG2 . VAL A 586 ? 0.2362 0.2381 0.2945 -0.0221 0.0232 0.0047 627 VAL A CG2 4717 N N . SER A 587 ? 0.2515 0.2523 0.3259 -0.0188 0.0026 -0.0043 628 SER A N 4718 C CA . SER A 587 ? 0.2672 0.2684 0.3497 -0.0176 -0.0031 -0.0080 628 SER A CA 4719 C C . SER A 587 ? 0.2549 0.2572 0.3316 -0.0153 -0.0070 -0.0108 628 SER A C 4720 O O . SER A 587 ? 0.2559 0.2576 0.3212 -0.0141 -0.0075 -0.0102 628 SER A O 4721 C CB . SER A 587 ? 0.2914 0.2899 0.3747 -0.0169 -0.0072 -0.0084 628 SER A CB 4722 O OG . SER A 587 ? 0.3298 0.3287 0.4224 -0.0158 -0.0123 -0.0121 628 SER A OG 4723 N N . PHE A 588 ? 0.2514 0.2552 0.3360 -0.0145 -0.0098 -0.0139 629 PHE A N 4724 C CA . PHE A 588 ? 0.2258 0.2302 0.3060 -0.0118 -0.0142 -0.0169 629 PHE A CA 4725 C C . PHE A 588 ? 0.2331 0.2355 0.3141 -0.0096 -0.0207 -0.0195 629 PHE A C 4726 O O . PHE A 588 ? 0.2159 0.2184 0.2941 -0.0070 -0.0247 -0.0221 629 PHE A O 4727 C CB . PHE A 588 ? 0.2276 0.2347 0.3143 -0.0118 -0.0137 -0.0188 629 PHE A CB 4728 C CG . PHE A 588 ? 0.2263 0.2351 0.3083 -0.0131 -0.0081 -0.0168 629 PHE A CG 4729 C CD1 . PHE A 588 ? 0.2111 0.2208 0.2845 -0.0115 -0.0085 -0.0175 629 PHE A CD1 4730 C CD2 . PHE A 588 ? 0.2562 0.2655 0.3415 -0.0156 -0.0023 -0.0140 629 PHE A CD2 4731 C CE1 . PHE A 588 ? 0.2240 0.2352 0.2928 -0.0126 -0.0037 -0.0158 629 PHE A CE1 4732 C CE2 . PHE A 588 ? 0.2559 0.2665 0.3360 -0.0164 0.0027 -0.0123 629 PHE A CE2 4733 C CZ . PHE A 588 ? 0.2019 0.2135 0.2735 -0.0149 0.0018 -0.0134 629 PHE A CZ 4734 N N . ASP A 589 ? 0.2365 0.2370 0.3214 -0.0103 -0.0217 -0.0188 630 ASP A N 4735 C CA . ASP A 589 ? 0.2423 0.2406 0.3291 -0.0080 -0.0281 -0.0216 630 ASP A CA 4736 C C . ASP A 589 ? 0.2411 0.2381 0.3156 -0.0050 -0.0314 -0.0226 630 ASP A C 4737 O O . ASP A 589 ? 0.2536 0.2497 0.3283 -0.0021 -0.0368 -0.0258 630 ASP A O 4738 C CB . ASP A 589 ? 0.2433 0.2394 0.3347 -0.0093 -0.0283 -0.0204 630 ASP A CB 4739 C CG . ASP A 589 ? 0.3142 0.3111 0.4208 -0.0118 -0.0264 -0.0203 630 ASP A CG 4740 O OD1 . ASP A 589 ? 0.3314 0.3306 0.4458 -0.0124 -0.0256 -0.0217 630 ASP A OD1 4741 O OD2 . ASP A 589 ? 0.3327 0.3277 0.4434 -0.0132 -0.0256 -0.0187 630 ASP A OD2 4742 N N . SER A 590 ? 0.2303 0.2272 0.2943 -0.0054 -0.0282 -0.0197 631 SER A N 4743 C CA . SER A 590 ? 0.2331 0.2288 0.2861 -0.0025 -0.0308 -0.0203 631 SER A CA 4744 C C . SER A 590 ? 0.2251 0.2222 0.2757 -0.0005 -0.0321 -0.0223 631 SER A C 4745 O O . SER A 590 ? 0.2211 0.2168 0.2668 0.0026 -0.0362 -0.0242 631 SER A O 4746 C CB . SER A 590 ? 0.2266 0.2221 0.2696 -0.0034 -0.0273 -0.0170 631 SER A CB 4747 O OG . SER A 590 ? 0.2472 0.2449 0.2887 -0.0053 -0.0223 -0.0151 631 SER A OG 4748 N N . LEU A 591 ? 0.2056 0.2053 0.2593 -0.0022 -0.0286 -0.0218 632 LEU A N 4749 C CA . LEU A 591 ? 0.2172 0.2182 0.2687 -0.0002 -0.0298 -0.0237 632 LEU A CA 4750 C C . LEU A 591 ? 0.2147 0.2151 0.2734 0.0020 -0.0351 -0.0274 632 LEU A C 4751 O O . LEU A 591 ? 0.2175 0.2169 0.2713 0.0053 -0.0388 -0.0294 632 LEU A O 4752 C CB . LEU A 591 ? 0.2106 0.2143 0.2637 -0.0024 -0.0249 -0.0224 632 LEU A CB 4753 C CG . LEU A 591 ? 0.1939 0.1989 0.2452 -0.0006 -0.0258 -0.0242 632 LEU A CG 4754 C CD1 . LEU A 591 ? 0.1952 0.1992 0.2350 0.0018 -0.0267 -0.0237 632 LEU A CD1 4755 C CD2 . LEU A 591 ? 0.2164 0.2240 0.2699 -0.0030 -0.0205 -0.0228 632 LEU A CD2 4756 N N . PHE A 592 ? 0.2033 0.2041 0.2736 0.0004 -0.0358 -0.0285 633 PHE A N 4757 C CA . PHE A 592 ? 0.2121 0.2122 0.2896 0.0027 -0.0416 -0.0324 633 PHE A CA 4758 C C . PHE A 592 ? 0.2077 0.2045 0.2800 0.0060 -0.0471 -0.0342 633 PHE A C 4759 O O . PHE A 592 ? 0.2405 0.2362 0.3121 0.0095 -0.0522 -0.0373 633 PHE A O 4760 C CB . PHE A 592 ? 0.2280 0.2292 0.3200 0.0002 -0.0410 -0.0330 633 PHE A CB 4761 C CG . PHE A 592 ? 0.2313 0.2357 0.3294 -0.0018 -0.0369 -0.0325 633 PHE A CG 4762 C CD1 . PHE A 592 ? 0.2454 0.2510 0.3466 0.0001 -0.0396 -0.0353 633 PHE A CD1 4763 C CD2 . PHE A 592 ? 0.2620 0.2679 0.3623 -0.0053 -0.0305 -0.0292 633 PHE A CD2 4764 C CE1 . PHE A 592 ? 0.2457 0.2543 0.3528 -0.0017 -0.0357 -0.0349 633 PHE A CE1 4765 C CE2 . PHE A 592 ? 0.2576 0.2664 0.3635 -0.0070 -0.0264 -0.0287 633 PHE A CE2 4766 C CZ . PHE A 592 ? 0.2451 0.2554 0.3542 -0.0052 -0.0290 -0.0316 633 PHE A CZ 4767 N N . SER A 593 ? 0.2216 0.2167 0.2902 0.0052 -0.0463 -0.0322 634 SER A N 4768 C CA . SER A 593 ? 0.2295 0.2213 0.2921 0.0083 -0.0510 -0.0336 634 SER A CA 4769 C C . SER A 593 ? 0.2220 0.2130 0.2727 0.0118 -0.0522 -0.0339 634 SER A C 4770 O O . SER A 593 ? 0.2394 0.2281 0.2870 0.0156 -0.0572 -0.0366 634 SER A O 4771 C CB . SER A 593 ? 0.2232 0.2136 0.2837 0.0065 -0.0491 -0.0310 634 SER A CB 4772 O OG . SER A 593 ? 0.2587 0.2460 0.3128 0.0096 -0.0533 -0.0322 634 SER A OG 4773 N N . ALA A 594 ? 0.2178 0.2104 0.2618 0.0105 -0.0474 -0.0311 635 ALA A N 4774 C CA . ALA A 594 ? 0.2228 0.2148 0.2561 0.0135 -0.0476 -0.0309 635 ALA A CA 4775 C C . ALA A 594 ? 0.2136 0.2058 0.2483 0.0162 -0.0507 -0.0338 635 ALA A C 4776 O O . ALA A 594 ? 0.2311 0.2211 0.2589 0.0204 -0.0540 -0.0352 635 ALA A O 4777 C CB . ALA A 594 ? 0.2284 0.2224 0.2557 0.0112 -0.0418 -0.0275 635 ALA A CB 4778 N N . VAL A 595 ? 0.2136 0.2082 0.2573 0.0142 -0.0496 -0.0346 636 VAL A N 4779 C CA . VAL A 595 ? 0.2058 0.2009 0.2520 0.0166 -0.0523 -0.0373 636 VAL A CA 4780 C C . VAL A 595 ? 0.2203 0.2127 0.2695 0.0200 -0.0592 -0.0411 636 VAL A C 4781 O O . VAL A 595 ? 0.2398 0.2305 0.2843 0.0241 -0.0628 -0.0432 636 VAL A O 4782 C CB . VAL A 595 ? 0.2090 0.2074 0.2646 0.0135 -0.0494 -0.0373 636 VAL A CB 4783 C CG1 . VAL A 595 ? 0.2354 0.2342 0.2953 0.0160 -0.0530 -0.0405 636 VAL A CG1 4784 C CG2 . VAL A 595 ? 0.2043 0.2048 0.2543 0.0113 -0.0432 -0.0340 636 VAL A CG2 4785 N N . LYS A 596 ? 0.2342 0.2260 0.2913 0.0185 -0.0610 -0.0419 637 LYS A N 4786 C CA . LYS A 596 ? 0.2410 0.2299 0.3011 0.0218 -0.0679 -0.0457 637 LYS A CA 4787 C C . LYS A 596 ? 0.2379 0.2232 0.2855 0.0261 -0.0707 -0.0460 637 LYS A C 4788 O O . LYS A 596 ? 0.2426 0.2255 0.2870 0.0306 -0.0759 -0.0491 637 LYS A O 4789 C CB . LYS A 596 ? 0.2544 0.2431 0.3248 0.0190 -0.0685 -0.0459 637 LYS A CB 4790 C CG . LYS A 596 ? 0.3007 0.2861 0.3742 0.0222 -0.0758 -0.0498 637 LYS A CG 4791 C CD . LYS A 596 ? 0.3668 0.3523 0.4514 0.0188 -0.0755 -0.0496 637 LYS A CD 4792 C CE . LYS A 596 ? 0.4003 0.3827 0.4901 0.0217 -0.0831 -0.0539 637 LYS A CE 4793 N NZ . LYS A 596 ? 0.4561 0.4349 0.5345 0.0247 -0.0853 -0.0538 637 LYS A NZ 4794 N N . ASN A 597 ? 0.2349 0.2197 0.2748 0.0250 -0.0672 -0.0428 638 ASN A N 4795 C CA . ASN A 597 ? 0.2434 0.2250 0.2715 0.0289 -0.0690 -0.0426 638 ASN A CA 4796 C C . ASN A 597 ? 0.2440 0.2252 0.2634 0.0323 -0.0688 -0.0427 638 ASN A C 4797 O O . ASN A 597 ? 0.2663 0.2441 0.2789 0.0372 -0.0729 -0.0446 638 ASN A O 4798 C CB . ASN A 597 ? 0.2263 0.2081 0.2488 0.0267 -0.0646 -0.0390 638 ASN A CB 4799 C CG . ASN A 597 ? 0.2685 0.2494 0.2972 0.0245 -0.0656 -0.0389 638 ASN A CG 4800 O OD1 . ASN A 597 ? 0.2800 0.2598 0.3169 0.0251 -0.0700 -0.0420 638 ASN A OD1 4801 N ND2 . ASN A 597 ? 0.2729 0.2543 0.2982 0.0221 -0.0617 -0.0357 638 ASN A ND2 4802 N N . PHE A 598 ? 0.2257 0.2099 0.2454 0.0301 -0.0643 -0.0407 639 PHE A N 4803 C CA . PHE A 598 ? 0.2304 0.2143 0.2429 0.0330 -0.0638 -0.0406 639 PHE A CA 4804 C C . PHE A 598 ? 0.2491 0.2313 0.2640 0.0369 -0.0695 -0.0445 639 PHE A C 4805 O O . PHE A 598 ? 0.2475 0.2269 0.2538 0.0418 -0.0719 -0.0455 639 PHE A O 4806 C CB . PHE A 598 ? 0.2169 0.2045 0.2315 0.0295 -0.0583 -0.0384 639 PHE A CB 4807 C CG . PHE A 598 ? 0.2193 0.2066 0.2260 0.0321 -0.0568 -0.0375 639 PHE A CG 4808 C CD1 . PHE A 598 ? 0.2281 0.2160 0.2272 0.0313 -0.0522 -0.0342 639 PHE A CD1 4809 C CD2 . PHE A 598 ? 0.2259 0.2126 0.2336 0.0351 -0.0598 -0.0400 639 PHE A CD2 4810 C CE1 . PHE A 598 ? 0.2445 0.2321 0.2373 0.0334 -0.0505 -0.0333 639 PHE A CE1 4811 C CE2 . PHE A 598 ? 0.2471 0.2334 0.2478 0.0374 -0.0582 -0.0390 639 PHE A CE2 4812 C CZ . PHE A 598 ? 0.2350 0.2217 0.2282 0.0366 -0.0534 -0.0356 639 PHE A CZ 4813 N N . THR A 599 ? 0.2445 0.2282 0.2712 0.0350 -0.0716 -0.0468 640 THR A N 4814 C CA . THR A 599 ? 0.2586 0.2411 0.2895 0.0384 -0.0774 -0.0509 640 THR A CA 4815 C C . THR A 599 ? 0.2746 0.2525 0.3000 0.0434 -0.0836 -0.0536 640 THR A C 4816 O O . THR A 599 ? 0.2852 0.2605 0.3046 0.0484 -0.0873 -0.0557 640 THR A O 4817 C CB . THR A 599 ? 0.2704 0.2555 0.3162 0.0351 -0.0785 -0.0528 640 THR A CB 4818 O OG1 . THR A 599 ? 0.2649 0.2540 0.3151 0.0306 -0.0725 -0.0502 640 THR A OG1 4819 C CG2 . THR A 599 ? 0.2536 0.2375 0.3044 0.0388 -0.0850 -0.0573 640 THR A CG2 4820 N N . GLU A 600 ? 0.2714 0.2481 0.2979 0.0422 -0.0843 -0.0534 641 GLU A N 4821 C CA . GLU A 600 ? 0.2927 0.2648 0.3140 0.0469 -0.0901 -0.0561 641 GLU A CA 4822 C C . GLU A 600 ? 0.2830 0.2520 0.2889 0.0514 -0.0893 -0.0545 641 GLU A C 4823 O O . GLU A 600 ? 0.2931 0.2583 0.2923 0.0571 -0.0941 -0.0571 641 GLU A O 4824 C CB . GLU A 600 ? 0.3001 0.2717 0.3268 0.0444 -0.0908 -0.0560 641 GLU A CB 4825 C CG . GLU A 600 ? 0.3752 0.3489 0.4178 0.0412 -0.0930 -0.0584 641 GLU A CG 4826 C CD . GLU A 600 ? 0.4744 0.4480 0.5238 0.0379 -0.0926 -0.0577 641 GLU A CD 4827 O OE1 . GLU A 600 ? 0.5143 0.4896 0.5774 0.0350 -0.0937 -0.0592 641 GLU A OE1 4828 O OE2 . GLU A 600 ? 0.5134 0.4854 0.5549 0.0381 -0.0908 -0.0556 641 GLU A OE2 4829 N N . ILE A 601 ? 0.2683 0.2389 0.2684 0.0490 -0.0831 -0.0503 642 ILE A N 4830 C CA . ILE A 601 ? 0.2750 0.2430 0.2619 0.0527 -0.0815 -0.0484 642 ILE A CA 4831 C C . ILE A 601 ? 0.2730 0.2404 0.2543 0.0562 -0.0815 -0.0487 642 ILE A C 4832 O O . ILE A 601 ? 0.2862 0.2497 0.2572 0.0617 -0.0835 -0.0492 642 ILE A O 4833 C CB . ILE A 601 ? 0.2664 0.2365 0.2499 0.0490 -0.0750 -0.0439 642 ILE A CB 4834 C CG1 . ILE A 601 ? 0.2482 0.2180 0.2357 0.0466 -0.0756 -0.0437 642 ILE A CG1 4835 C CG2 . ILE A 601 ? 0.3040 0.2719 0.2749 0.0526 -0.0727 -0.0417 642 ILE A CG2 4836 C CD1 . ILE A 601 ? 0.2834 0.2557 0.2695 0.0421 -0.0693 -0.0394 642 ILE A CD1 4837 N N . ALA A 602 ? 0.2494 0.2202 0.2371 0.0534 -0.0794 -0.0483 643 ALA A N 4838 C CA . ALA A 602 ? 0.2749 0.2451 0.2579 0.0565 -0.0794 -0.0486 643 ALA A CA 4839 C C . ALA A 602 ? 0.2967 0.2633 0.2789 0.0620 -0.0867 -0.0529 643 ALA A C 4840 O O . ALA A 602 ? 0.3109 0.2743 0.2838 0.0673 -0.0881 -0.0532 643 ALA A O 4841 C CB . ALA A 602 ? 0.2792 0.2540 0.2707 0.0522 -0.0760 -0.0477 643 ALA A CB 4842 N N . SER A 603 ? 0.3104 0.2773 0.3026 0.0610 -0.0914 -0.0563 644 SER A N 4843 C CA . SER A 603 ? 0.3400 0.3033 0.3321 0.0663 -0.0991 -0.0609 644 SER A CA 4844 C C . SER A 603 ? 0.3405 0.2983 0.3197 0.0723 -0.1020 -0.0616 644 SER A C 4845 O O . SER A 603 ? 0.3482 0.3023 0.3197 0.0783 -0.1058 -0.0635 644 SER A O 4846 C CB . SER A 603 ? 0.3441 0.3087 0.3499 0.0639 -0.1036 -0.0645 644 SER A CB 4847 O OG . SER A 603 ? 0.4204 0.3812 0.4255 0.0695 -0.1116 -0.0692 644 SER A OG 4848 N N . LYS A 604 ? 0.3286 0.2857 0.3052 0.0708 -0.1001 -0.0599 645 LYS A N 4849 C CA A LYS A 604 ? 0.3423 0.2944 0.3068 0.0763 -0.1023 -0.0603 645 LYS A CA 4850 C CA B LYS A 604 ? 0.3397 0.2918 0.3043 0.0763 -0.1023 -0.0602 645 LYS A CA 4851 C C . LYS A 604 ? 0.3432 0.2935 0.2946 0.0798 -0.0982 -0.0570 645 LYS A C 4852 O O . LYS A 604 ? 0.3456 0.2912 0.2866 0.0862 -0.1011 -0.0583 645 LYS A O 4853 C CB A LYS A 604 ? 0.3448 0.2967 0.3104 0.0738 -0.1013 -0.0592 645 LYS A CB 4854 C CB B LYS A 604 ? 0.3401 0.2922 0.3058 0.0737 -0.1011 -0.0591 645 LYS A CB 4855 C CG A LYS A 604 ? 0.3731 0.3256 0.3510 0.0715 -0.1062 -0.0627 645 LYS A CG 4856 C CG B LYS A 604 ? 0.3589 0.3109 0.3358 0.0720 -0.1065 -0.0628 645 LYS A CG 4857 C CD A LYS A 604 ? 0.4367 0.3896 0.4164 0.0684 -0.1043 -0.0611 645 LYS A CD 4858 C CD B LYS A 604 ? 0.3994 0.3466 0.3730 0.0786 -0.1147 -0.0678 645 LYS A CD 4859 C CE A LYS A 604 ? 0.4749 0.4278 0.4669 0.0665 -0.1094 -0.0647 645 LYS A CE 4860 C CE B LYS A 604 ? 0.4478 0.3956 0.4354 0.0769 -0.1207 -0.0722 645 LYS A CE 4861 N NZ A LYS A 604 ? 0.5170 0.4706 0.5120 0.0627 -0.1068 -0.0626 645 LYS A NZ 4862 N NZ B LYS A 604 ? 0.4610 0.4120 0.4589 0.0705 -0.1177 -0.0706 645 LYS A NZ 4863 N N . PHE A 605 ? 0.3084 0.2625 0.2604 0.0756 -0.0912 -0.0529 646 PHE A N 4864 C CA . PHE A 605 ? 0.3131 0.2659 0.2543 0.0784 -0.0870 -0.0498 646 PHE A CA 4865 C C . PHE A 605 ? 0.3224 0.2729 0.2599 0.0833 -0.0901 -0.0517 646 PHE A C 4866 O O . PHE A 605 ? 0.3465 0.2928 0.2722 0.0891 -0.0901 -0.0510 646 PHE A O 4867 C CB . PHE A 605 ? 0.2962 0.2540 0.2413 0.0725 -0.0797 -0.0457 646 PHE A CB 4868 C CG . PHE A 605 ? 0.2883 0.2451 0.2242 0.0748 -0.0750 -0.0424 646 PHE A CG 4869 C CD1 . PHE A 605 ? 0.2880 0.2430 0.2152 0.0763 -0.0716 -0.0395 646 PHE A CD1 4870 C CD2 . PHE A 605 ? 0.3272 0.2849 0.2633 0.0756 -0.0741 -0.0423 646 PHE A CD2 4871 C CE1 . PHE A 605 ? 0.3154 0.2694 0.2347 0.0785 -0.0670 -0.0363 646 PHE A CE1 4872 C CE2 . PHE A 605 ? 0.3360 0.2925 0.2638 0.0778 -0.0697 -0.0391 646 PHE A CE2 4873 C CZ . PHE A 605 ? 0.2962 0.2510 0.2160 0.0792 -0.0660 -0.0360 646 PHE A CZ 4874 N N . SER A 606 ? 0.3155 0.2685 0.2629 0.0812 -0.0927 -0.0542 647 SER A N 4875 C CA . SER A 606 ? 0.3365 0.2875 0.2815 0.0856 -0.0960 -0.0563 647 SER A CA 4876 C C . SER A 606 ? 0.3645 0.3094 0.3013 0.0931 -0.1030 -0.0599 647 SER A C 4877 O O . SER A 606 ? 0.3787 0.3200 0.3060 0.0987 -0.1038 -0.0598 647 SER A O 4878 C CB . SER A 606 ? 0.3448 0.2997 0.3035 0.0819 -0.0983 -0.0588 647 SER A CB 4879 O OG A SER A 606 ? 0.3431 0.3032 0.3080 0.0758 -0.0919 -0.0556 647 SER A OG 4880 O OG B SER A 606 ? 0.3545 0.3087 0.3115 0.0849 -0.0995 -0.0597 647 SER A OG 4881 N N . GLU A 607 ? 0.3555 0.2992 0.2961 0.0932 -0.1076 -0.0628 648 GLU A N 4882 C CA . GLU A 607 ? 0.3967 0.3344 0.3294 0.1004 -0.1145 -0.0665 648 GLU A CA 4883 C C . GLU A 607 ? 0.4027 0.3359 0.3193 0.1055 -0.1114 -0.0636 648 GLU A C 4884 O O . GLU A 607 ? 0.4290 0.3571 0.3348 0.1127 -0.1144 -0.0648 648 GLU A O 4885 C CB . GLU A 607 ? 0.4236 0.3610 0.3635 0.0986 -0.1189 -0.0694 648 GLU A CB 4886 C CG . GLU A 607 ? 0.4925 0.4334 0.4486 0.0947 -0.1230 -0.0730 648 GLU A CG 4887 C CD . GLU A 607 ? 0.5951 0.5355 0.5590 0.0930 -0.1273 -0.0758 648 GLU A CD 4888 O OE1 . GLU A 607 ? 0.6235 0.5606 0.5799 0.0952 -0.1278 -0.0756 648 GLU A OE1 4889 O OE2 . GLU A 607 ? 0.6592 0.6027 0.6375 0.0892 -0.1299 -0.0783 648 GLU A OE2 4890 N N . ARG A 608 ? 0.3862 0.3212 0.3009 0.1020 -0.1053 -0.0596 649 ARG A N 4891 C CA . ARG A 608 ? 0.3806 0.3117 0.2812 0.1065 -0.1017 -0.0565 649 ARG A CA 4892 C C . ARG A 608 ? 0.4003 0.3304 0.2935 0.1093 -0.0980 -0.0538 649 ARG A C 4893 O O . ARG A 608 ? 0.4187 0.3438 0.2993 0.1158 -0.0979 -0.0531 649 ARG A O 4894 C CB . ARG A 608 ? 0.3646 0.2983 0.2661 0.1017 -0.0957 -0.0527 649 ARG A CB 4895 C CG . ARG A 608 ? 0.3669 0.3008 0.2745 0.0996 -0.0992 -0.0551 649 ARG A CG 4896 C CD . ARG A 608 ? 0.3652 0.2997 0.2693 0.0975 -0.0942 -0.0515 649 ARG A CD 4897 N NE . ARG A 608 ? 0.3680 0.3073 0.2754 0.0918 -0.0867 -0.0469 649 ARG A NE 4898 C CZ . ARG A 608 ? 0.3803 0.3248 0.2992 0.0849 -0.0849 -0.0463 649 ARG A CZ 4899 N NH1 . ARG A 608 ? 0.3668 0.3123 0.2952 0.0826 -0.0896 -0.0497 649 ARG A NH1 4900 N NH2 . ARG A 608 ? 0.3726 0.3211 0.2936 0.0803 -0.0783 -0.0424 649 ARG A NH2 4901 N N . LEU A 609 ? 0.3936 0.3285 0.2947 0.1045 -0.0947 -0.0523 650 LEU A N 4902 C CA . LEU A 609 ? 0.4267 0.3611 0.3219 0.1065 -0.0906 -0.0495 650 LEU A CA 4903 C C . LEU A 609 ? 0.4716 0.4011 0.3602 0.1137 -0.0964 -0.0526 650 LEU A C 4904 O O . LEU A 609 ? 0.4805 0.4065 0.3587 0.1186 -0.0942 -0.0505 650 LEU A O 4905 C CB . LEU A 609 ? 0.4172 0.3578 0.3236 0.0996 -0.0868 -0.0480 650 LEU A CB 4906 C CG . LEU A 609 ? 0.4393 0.3806 0.3413 0.0997 -0.0808 -0.0441 650 LEU A CG 4907 C CD1 . LEU A 609 ? 0.4177 0.3590 0.3135 0.0990 -0.0741 -0.0395 650 LEU A CD1 4908 C CD2 . LEU A 609 ? 0.4472 0.3943 0.3612 0.0936 -0.0789 -0.0440 650 LEU A CD2 4909 N N . GLN A 610 ? 0.5122 0.4415 0.4075 0.1142 -0.1037 -0.0575 651 GLN A N 4910 C CA . GLN A 610 ? 0.5743 0.4994 0.4647 0.1208 -0.1097 -0.0609 651 GLN A CA 4911 C C . GLN A 610 ? 0.5912 0.5093 0.4687 0.1286 -0.1139 -0.0627 651 GLN A C 4912 O O . GLN A 610 ? 0.6197 0.5328 0.4870 0.1355 -0.1162 -0.0634 651 GLN A O 4913 C CB . GLN A 610 ? 0.5769 0.5048 0.4806 0.1183 -0.1158 -0.0655 651 GLN A CB 4914 C CG . GLN A 610 ? 0.6351 0.5680 0.5469 0.1136 -0.1117 -0.0635 651 GLN A CG 4915 C CD . GLN A 610 ? 0.7038 0.6395 0.6288 0.1115 -0.1172 -0.0678 651 GLN A CD 4916 O OE1 . GLN A 610 ? 0.7621 0.6944 0.6864 0.1165 -0.1248 -0.0723 651 GLN A OE1 4917 N NE2 . GLN A 610 ? 0.7302 0.6722 0.6676 0.1042 -0.1132 -0.0664 651 GLN A NE2 4918 N N . ASP A 611 ? 0.5998 0.5175 0.4776 0.1274 -0.1144 -0.0631 652 ASP A N 4919 C CA . ASP A 611 ? 0.6245 0.5359 0.4918 0.1339 -0.1188 -0.0653 652 ASP A CA 4920 C C . ASP A 611 ? 0.6198 0.5280 0.4736 0.1372 -0.1128 -0.0610 652 ASP A C 4921 O O . ASP A 611 ? 0.6190 0.5217 0.4630 0.1430 -0.1158 -0.0625 652 ASP A O 4922 C CB . ASP A 611 ? 0.6366 0.5500 0.5126 0.1298 -0.1214 -0.0676 652 ASP A CB 4923 C CG . ASP A 611 ? 0.7026 0.6161 0.5887 0.1297 -0.1302 -0.0736 652 ASP A CG 4924 O OD1 . ASP A 611 ? 0.7666 0.6802 0.6580 0.1279 -0.1332 -0.0759 652 ASP A OD1 4925 O OD2 . ASP A 611 ? 0.7720 0.6855 0.6612 0.1313 -0.1339 -0.0760 652 ASP A OD2 4926 N N . PHE A 612 ? 0.5974 0.5090 0.4516 0.1331 -0.1044 -0.0557 653 PHE A N 4927 C CA . PHE A 612 ? 0.5844 0.4935 0.4284 0.1353 -0.0988 -0.0517 653 PHE A CA 4928 C C . PHE A 612 ? 0.5972 0.4998 0.4254 0.1438 -0.0978 -0.0502 653 PHE A C 4929 O O . PHE A 612 ? 0.6220 0.5212 0.4409 0.1471 -0.0952 -0.0483 653 PHE A O 4930 C CB . PHE A 612 ? 0.5577 0.4723 0.4070 0.1284 -0.0902 -0.0466 653 PHE A CB 4931 C CG . PHE A 612 ? 0.5230 0.4387 0.3701 0.1282 -0.0845 -0.0427 653 PHE A CG 4932 C CD1 . PHE A 612 ? 0.4829 0.3954 0.3189 0.1321 -0.0786 -0.0384 653 PHE A CD1 4933 C CD2 . PHE A 612 ? 0.5014 0.4216 0.3584 0.1236 -0.0844 -0.0432 653 PHE A CD2 4934 C CE1 . PHE A 612 ? 0.5410 0.4548 0.3761 0.1315 -0.0730 -0.0347 653 PHE A CE1 4935 C CE2 . PHE A 612 ? 0.5410 0.4625 0.3967 0.1230 -0.0790 -0.0397 653 PHE A CE2 4936 C CZ . PHE A 612 ? 0.5492 0.4675 0.3942 0.1268 -0.0733 -0.0354 653 PHE A CZ 4937 N N A SER A 615 ? 0.4061 0.2883 0.1789 0.1699 -0.0786 -0.0349 656 SER A N 4938 N N B SER A 615 ? 0.3825 0.2701 0.1602 0.1640 -0.0626 -0.0245 656 SER A N 4939 C CA A SER A 615 ? 0.4068 0.2856 0.1693 0.1737 -0.0705 -0.0293 656 SER A CA 4940 C CA B SER A 615 ? 0.3866 0.2695 0.1527 0.1694 -0.0554 -0.0193 656 SER A CA 4941 C C A SER A 615 ? 0.3901 0.2737 0.1587 0.1676 -0.0628 -0.0250 656 SER A C 4942 C C B SER A 615 ? 0.3907 0.2748 0.1569 0.1673 -0.0505 -0.0166 656 SER A C 4943 O O A SER A 615 ? 0.4048 0.2861 0.1664 0.1701 -0.0555 -0.0201 656 SER A O 4944 O O B SER A 615 ? 0.4063 0.2868 0.1638 0.1715 -0.0443 -0.0123 656 SER A O 4945 C CB A SER A 615 ? 0.3846 0.2549 0.1309 0.1836 -0.0733 -0.0306 656 SER A CB 4946 C CB B SER A 615 ? 0.3810 0.2549 0.1306 0.1804 -0.0591 -0.0206 656 SER A CB 4947 O OG A SER A 615 ? 0.3982 0.2692 0.1470 0.1821 -0.0769 -0.0335 656 SER A OG 4948 O OG B SER A 615 ? 0.4250 0.2954 0.1681 0.1840 -0.0625 -0.0230 656 SER A OG 4949 N N A ASN A 616 ? 0.3700 0.2597 0.1512 0.1598 -0.0642 -0.0267 657 ASN A N 4950 N N B ASN A 616 ? 0.3841 0.2734 0.1606 0.1609 -0.0529 -0.0190 657 ASN A N 4951 C CA A ASN A 616 ? 0.3784 0.2723 0.1651 0.1543 -0.0579 -0.0231 657 ASN A CA 4952 C CA B ASN A 616 ? 0.4007 0.2921 0.1795 0.1577 -0.0482 -0.0164 657 ASN A CA 4953 C C A ASN A 616 ? 0.3804 0.2810 0.1785 0.1465 -0.0526 -0.0201 657 ASN A C 4954 C C B ASN A 616 ? 0.3948 0.2934 0.1858 0.1492 -0.0422 -0.0131 657 ASN A C 4955 O O A ASN A 616 ? 0.3693 0.2752 0.1791 0.1402 -0.0555 -0.0225 657 ASN A O 4956 O O B ASN A 616 ? 0.3918 0.2962 0.1947 0.1421 -0.0445 -0.0151 657 ASN A O 4957 C CB A ASN A 616 ? 0.3777 0.2737 0.1702 0.1509 -0.0622 -0.0264 657 ASN A CB 4958 C CB B ASN A 616 ? 0.3869 0.2792 0.1691 0.1561 -0.0547 -0.0210 657 ASN A CB 4959 C CG A ASN A 616 ? 0.3919 0.2903 0.1865 0.1475 -0.0561 -0.0229 657 ASN A CG 4960 C CG B ASN A 616 ? 0.4344 0.3290 0.2193 0.1528 -0.0506 -0.0189 657 ASN A CG 4961 O OD1 A ASN A 616 ? 0.3783 0.2807 0.1781 0.1430 -0.0496 -0.0188 657 ASN A OD1 4962 O OD1 B ASN A 616 ? 0.4546 0.3537 0.2462 0.1474 -0.0441 -0.0150 657 ASN A OD1 4963 N ND2 A ASN A 616 ? 0.4367 0.3327 0.2274 0.1497 -0.0584 -0.0244 657 ASN A ND2 4964 N ND2 B ASN A 616 ? 0.4613 0.3531 0.2423 0.1555 -0.0549 -0.0218 657 ASN A ND2 4965 N N A PRO A 617 ? 0.3706 0.2709 0.1656 0.1471 -0.0447 -0.0149 658 PRO A N 4966 N N B PRO A 617 ? 0.4076 0.3057 0.1960 0.1500 -0.0342 -0.0078 658 PRO A N 4967 C CA A PRO A 617 ? 0.3591 0.2651 0.1642 0.1405 -0.0400 -0.0122 658 PRO A CA 4968 C CA B PRO A 617 ? 0.3938 0.2983 0.1935 0.1424 -0.0286 -0.0047 658 PRO A CA 4969 C C A PRO A 617 ? 0.3505 0.2630 0.1670 0.1323 -0.0379 -0.0116 658 PRO A C 4970 C C B PRO A 617 ? 0.3894 0.3007 0.2014 0.1340 -0.0288 -0.0056 658 PRO A C 4971 O O A PRO A 617 ? 0.3361 0.2542 0.1628 0.1258 -0.0359 -0.0109 658 PRO A O 4972 O O B PRO A 617 ? 0.3627 0.2794 0.1853 0.1275 -0.0286 -0.0059 658 PRO A O 4973 C CB A PRO A 617 ? 0.3624 0.2653 0.1602 0.1444 -0.0323 -0.0068 658 PRO A CB 4974 C CB B PRO A 617 ? 0.4074 0.3092 0.2011 0.1457 -0.0203 0.0009 658 PRO A CB 4975 C CG A PRO A 617 ? 0.3545 0.2527 0.1422 0.1498 -0.0309 -0.0057 658 PRO A CG 4976 C CG B PRO A 617 ? 0.4296 0.3233 0.2084 0.1554 -0.0214 0.0010 658 PRO A CG 4977 C CD A PRO A 617 ? 0.3980 0.2929 0.1810 0.1535 -0.0396 -0.0112 658 PRO A CD 4978 C CD B PRO A 617 ? 0.4199 0.3110 0.1945 0.1583 -0.0301 -0.0045 658 PRO A CD 4979 N N A ILE A 618 ? 0.3536 0.2653 0.1679 0.1328 -0.0381 -0.0118 659 ILE A N 4980 N N B ILE A 618 ? 0.3811 0.2920 0.1917 0.1340 -0.0288 -0.0057 659 ILE A N 4981 C CA A ILE A 618 ? 0.3570 0.2743 0.1813 0.1255 -0.0364 -0.0112 659 ILE A CA 4982 C CA B ILE A 618 ? 0.3733 0.2905 0.1953 0.1262 -0.0287 -0.0062 659 ILE A CA 4983 C C A ILE A 618 ? 0.3510 0.2720 0.1844 0.1207 -0.0428 -0.0158 659 ILE A C 4984 C C B ILE A 618 ? 0.3606 0.2801 0.1890 0.1228 -0.0360 -0.0112 659 ILE A C 4985 O O A ILE A 618 ? 0.3250 0.2517 0.1691 0.1135 -0.0416 -0.0155 659 ILE A O 4986 O O B ILE A 618 ? 0.3607 0.2860 0.2000 0.1156 -0.0361 -0.0118 659 ILE A O 4987 C CB A ILE A 618 ? 0.3716 0.2871 0.1915 0.1273 -0.0346 -0.0100 659 ILE A CB 4988 C CB B ILE A 618 ? 0.3673 0.2841 0.1876 0.1263 -0.0257 -0.0044 659 ILE A CB 4989 C CG1 A ILE A 618 ? 0.4207 0.3324 0.2318 0.1324 -0.0277 -0.0053 659 ILE A CG1 4990 C CG1 B ILE A 618 ? 0.4214 0.3393 0.2425 0.1255 -0.0174 0.0009 659 ILE A CG1 4991 C CG2 A ILE A 618 ? 0.3617 0.2833 0.1926 0.1194 -0.0334 -0.0097 659 ILE A CG2 4992 C CG2 B ILE A 618 ? 0.3876 0.3100 0.2184 0.1190 -0.0278 -0.0061 659 ILE A CG2 4993 C CD1 A ILE A 618 ? 0.4042 0.3190 0.2202 0.1293 -0.0214 -0.0014 659 ILE A CD1 4994 C CD1 B ILE A 618 ? 0.4546 0.3796 0.2885 0.1169 -0.0147 0.0021 659 ILE A CD1 4995 N N A VAL A 619 ? 0.3390 0.2563 0.1682 0.1248 -0.0497 -0.0200 660 VAL A N 4996 N N B VAL A 619 ? 0.3639 0.2790 0.1858 0.1280 -0.0423 -0.0149 660 VAL A N 4997 C CA A VAL A 619 ? 0.3439 0.2645 0.1826 0.1205 -0.0557 -0.0242 660 VAL A CA 4998 C CA B VAL A 619 ? 0.3383 0.2557 0.1675 0.1249 -0.0493 -0.0197 660 VAL A CA 4999 C C A VAL A 619 ? 0.3242 0.2483 0.1701 0.1169 -0.0557 -0.0245 660 VAL A C 5000 C C B VAL A 619 ? 0.3327 0.2539 0.1699 0.1209 -0.0498 -0.0203 660 VAL A C 5001 O O A VAL A 619 ? 0.3194 0.2488 0.1766 0.1103 -0.0566 -0.0258 660 VAL A O 5002 O O B VAL A 619 ? 0.3275 0.2540 0.1758 0.1142 -0.0513 -0.0219 660 VAL A O 5003 C CB A VAL A 619 ? 0.3422 0.2580 0.1754 0.1260 -0.0635 -0.0290 660 VAL A CB 5004 C CB B VAL A 619 ? 0.3633 0.2751 0.1846 0.1314 -0.0564 -0.0240 660 VAL A CB 5005 C CG1 A VAL A 619 ? 0.3754 0.2946 0.2196 0.1213 -0.0694 -0.0332 660 VAL A CG1 5006 C CG1 B VAL A 619 ? 0.3385 0.2529 0.1690 0.1278 -0.0636 -0.0289 660 VAL A CG1 5007 C CG2 A VAL A 619 ? 0.3557 0.2678 0.1814 0.1297 -0.0635 -0.0287 660 VAL A CG2 5008 C CG2 B VAL A 619 ? 0.3400 0.2487 0.1550 0.1344 -0.0561 -0.0236 660 VAL A CG2 5009 N N A LEU A 620 ? 0.3156 0.2366 0.1549 0.1216 -0.0544 -0.0233 661 LEU A N 5010 N N B LEU A 620 ? 0.3116 0.2302 0.1432 0.1248 -0.0478 -0.0187 661 LEU A N 5011 C CA A LEU A 620 ? 0.2938 0.2175 0.1387 0.1191 -0.0537 -0.0232 661 LEU A CA 5012 C CA B LEU A 620 ? 0.3148 0.2367 0.1534 0.1214 -0.0479 -0.0191 661 LEU A CA 5013 C C A LEU A 620 ? 0.3050 0.2349 0.1592 0.1115 -0.0477 -0.0199 661 LEU A C 5014 C C B LEU A 620 ? 0.3058 0.2340 0.1545 0.1136 -0.0424 -0.0162 661 LEU A C 5015 O O A LEU A 620 ? 0.3006 0.2352 0.1649 0.1059 -0.0488 -0.0214 661 LEU A O 5016 O O B LEU A 620 ? 0.3134 0.2463 0.1719 0.1081 -0.0435 -0.0176 661 LEU A O 5017 C CB A LEU A 620 ? 0.3186 0.2371 0.1529 0.1261 -0.0524 -0.0216 661 LEU A CB 5018 C CB B LEU A 620 ? 0.3180 0.2356 0.1480 0.1273 -0.0458 -0.0171 661 LEU A CB 5019 C CG A LEU A 620 ? 0.3178 0.2386 0.1564 0.1241 -0.0499 -0.0201 661 LEU A CG 5020 C CG B LEU A 620 ? 0.3403 0.2610 0.1772 0.1242 -0.0456 -0.0173 661 LEU A CG 5021 C CD1 A LEU A 620 ? 0.3187 0.2432 0.1673 0.1201 -0.0552 -0.0241 661 LEU A CD1 5022 C CD1 B LEU A 620 ? 0.3368 0.2599 0.1814 0.1217 -0.0527 -0.0223 661 LEU A CD1 5023 C CD2 A LEU A 620 ? 0.3207 0.2355 0.1478 0.1319 -0.0489 -0.0186 661 LEU A CD2 5024 C CD2 B LEU A 620 ? 0.3202 0.2359 0.1476 0.1306 -0.0435 -0.0151 661 LEU A CD2 5025 N N A ARG A 621 ? 0.3061 0.2357 0.1569 0.1117 -0.0413 -0.0157 662 ARG A N 5026 N N B ARG A 621 ? 0.3014 0.2296 0.1476 0.1134 -0.0363 -0.0122 662 ARG A N 5027 C CA A ARG A 621 ? 0.3186 0.2534 0.1772 0.1055 -0.0354 -0.0125 662 ARG A CA 5028 C CA B ARG A 621 ? 0.3018 0.2359 0.1575 0.1063 -0.0314 -0.0098 662 ARG A CA 5029 C C A ARG A 621 ? 0.3059 0.2452 0.1730 0.0992 -0.0366 -0.0138 662 ARG A C 5030 C C B ARG A 621 ? 0.3002 0.2392 0.1658 0.0995 -0.0341 -0.0121 662 ARG A C 5031 O O A ARG A 621 ? 0.2840 0.2284 0.1605 0.0932 -0.0357 -0.0139 662 ARG A O 5032 O O B ARG A 621 ? 0.2883 0.2324 0.1629 0.0935 -0.0325 -0.0117 662 ARG A O 5033 C CB A ARG A 621 ? 0.3213 0.2542 0.1743 0.1077 -0.0286 -0.0078 662 ARG A CB 5034 C CB B ARG A 621 ? 0.3005 0.2333 0.1521 0.1077 -0.0247 -0.0052 662 ARG A CB 5035 C CG A ARG A 621 ? 0.3228 0.2612 0.1844 0.1011 -0.0230 -0.0048 662 ARG A CG 5036 C CG B ARG A 621 ? 0.3039 0.2422 0.1646 0.1011 -0.0196 -0.0025 662 ARG A CG 5037 C CD A ARG A 621 ? 0.3537 0.2942 0.2193 0.0988 -0.0187 -0.0024 662 ARG A CD 5038 C CD B ARG A 621 ? 0.4023 0.3437 0.2695 0.0976 -0.0186 -0.0024 662 ARG A CD 5039 N NE A ARG A 621 ? 0.3678 0.3113 0.2379 0.0952 -0.0127 0.0012 662 ARG A NE 5040 N NE B ARG A 621 ? 0.4379 0.3824 0.3100 0.0939 -0.0123 0.0012 662 ARG A NE 5041 C CZ A ARG A 621 ? 0.3042 0.2484 0.1762 0.0945 -0.0073 0.0044 662 ARG A CZ 5042 C CZ B ARG A 621 ? 0.4326 0.3766 0.3047 0.0947 -0.0078 0.0041 662 ARG A CZ 5043 N NH1 A ARG A 621 ? 0.3360 0.2783 0.2058 0.0970 -0.0068 0.0049 662 ARG A NH1 5044 N NH1 B ARG A 621 ? 0.4166 0.3573 0.2838 0.0989 -0.0087 0.0038 662 ARG A NH1 5045 N NH2 A ARG A 621 ? 0.2788 0.2256 0.1554 0.0911 -0.0025 0.0072 662 ARG A NH2 5046 N NH2 B ARG A 621 ? 0.4567 0.4036 0.3340 0.0912 -0.0025 0.0071 662 ARG A NH2 5047 N N . MET A 622 ? 0.3129 0.2504 0.1767 0.1008 -0.0384 -0.0146 663 MET A N 5048 C CA . MET A 622 ? 0.3091 0.2505 0.1813 0.0951 -0.0410 -0.0167 663 MET A CA 5049 C C . MET A 622 ? 0.3197 0.2641 0.2002 0.0916 -0.0452 -0.0199 663 MET A C 5050 O O . MET A 622 ? 0.3006 0.2500 0.1905 0.0851 -0.0440 -0.0198 663 MET A O 5051 C CB A MET A 622 ? 0.3063 0.2443 0.1739 0.0984 -0.0452 -0.0189 663 MET A CB 5052 C CB B MET A 622 ? 0.3178 0.2561 0.1851 0.0981 -0.0439 -0.0180 663 MET A CB 5053 C CG A MET A 622 ? 0.3004 0.2419 0.1769 0.0931 -0.0488 -0.0215 663 MET A CG 5054 C CG B MET A 622 ? 0.3225 0.2587 0.1831 0.1008 -0.0385 -0.0142 663 MET A CG 5055 S SD A MET A 622 ? 0.1311 0.0685 0.0025 0.0969 -0.0534 -0.0240 663 MET A SD 5056 S SD B MET A 622 ? 0.1650 0.0982 0.0203 0.1036 -0.0399 -0.0147 663 MET A SD 5057 C CE A MET A 622 ? 0.3881 0.3206 0.2541 0.1033 -0.0603 -0.0283 663 MET A CE 5058 C CE B MET A 622 ? 0.3089 0.2347 0.1527 0.1126 -0.0460 -0.0182 663 MET A CE 5059 N N . MET A 623 ? 0.3087 0.2500 0.1861 0.0959 -0.0502 -0.0229 664 MET A N 5060 C CA . MET A 623 ? 0.3115 0.2556 0.1975 0.0927 -0.0542 -0.0262 664 MET A CA 5061 C C . MET A 623 ? 0.3069 0.2547 0.1984 0.0891 -0.0505 -0.0245 664 MET A C 5062 O O . MET A 623 ? 0.3052 0.2574 0.2065 0.0836 -0.0512 -0.0257 664 MET A O 5063 C CB A MET A 623 ? 0.3321 0.2714 0.2122 0.0992 -0.0601 -0.0295 664 MET A CB 5064 C CB B MET A 623 ? 0.3234 0.2636 0.2064 0.0978 -0.0614 -0.0305 664 MET A CB 5065 C CG A MET A 623 ? 0.3810 0.3150 0.2524 0.1049 -0.0637 -0.0311 664 MET A CG 5066 C CG B MET A 623 ? 0.2879 0.2257 0.1692 0.0995 -0.0659 -0.0330 664 MET A CG 5067 S SD A MET A 623 ? 0.1756 0.1124 0.0556 0.1001 -0.0671 -0.0336 664 MET A SD 5068 S SD B MET A 623 ? 0.1444 0.0787 0.0259 0.1039 -0.0754 -0.0390 664 MET A SD 5069 C CE A MET A 623 ? 0.3975 0.3339 0.2839 0.1007 -0.0755 -0.0393 664 MET A CE 5070 C CE B MET A 623 ? 0.2915 0.2321 0.1894 0.0956 -0.0774 -0.0412 664 MET A CE 5071 N N . ASN A 624 ? 0.3094 0.2551 0.1946 0.0922 -0.0466 -0.0216 665 ASN A N 5072 C CA . ASN A 624 ? 0.3045 0.2535 0.1948 0.0888 -0.0427 -0.0198 665 ASN A CA 5073 C C . ASN A 624 ? 0.2945 0.2487 0.1922 0.0820 -0.0383 -0.0177 665 ASN A C 5074 O O . ASN A 624 ? 0.2922 0.2505 0.1978 0.0772 -0.0373 -0.0179 665 ASN A O 5075 C CB . ASN A 624 ? 0.3196 0.2653 0.2021 0.0935 -0.0389 -0.0168 665 ASN A CB 5076 C CG . ASN A 624 ? 0.3171 0.2590 0.1950 0.0989 -0.0431 -0.0191 665 ASN A CG 5077 O OD1 . ASN A 624 ? 0.3001 0.2437 0.1838 0.0973 -0.0479 -0.0226 665 ASN A OD1 5078 N ND2 . ASN A 624 ? 0.3196 0.2565 0.1873 0.1052 -0.0413 -0.0170 665 ASN A ND2 5079 N N . ASP A 625 ? 0.2778 0.2315 0.1727 0.0818 -0.0359 -0.0157 666 ASP A N 5080 C CA . ASP A 625 ? 0.2760 0.2345 0.1781 0.0754 -0.0323 -0.0140 666 ASP A CA 5081 C C . ASP A 625 ? 0.2745 0.2365 0.1848 0.0705 -0.0357 -0.0167 666 ASP A C 5082 O O . ASP A 625 ? 0.2855 0.2519 0.2030 0.0650 -0.0335 -0.0161 666 ASP A O 5083 C CB . ASP A 625 ? 0.2886 0.2458 0.1863 0.0764 -0.0295 -0.0115 666 ASP A CB 5084 C CG . ASP A 625 ? 0.2894 0.2447 0.1818 0.0794 -0.0243 -0.0078 666 ASP A CG 5085 O OD1 . ASP A 625 ? 0.3133 0.2684 0.2056 0.0803 -0.0223 -0.0069 666 ASP A OD1 5086 O OD2 . ASP A 625 ? 0.3176 0.2719 0.2069 0.0805 -0.0217 -0.0057 666 ASP A OD2 5087 N N . GLN A 626 ? 0.2547 0.2147 0.1641 0.0725 -0.0409 -0.0197 667 GLN A N 5088 C CA . GLN A 626 ? 0.2673 0.2303 0.1852 0.0680 -0.0440 -0.0222 667 GLN A CA 5089 C C . GLN A 626 ? 0.2560 0.2217 0.1805 0.0656 -0.0445 -0.0236 667 GLN A C 5090 O O . GLN A 626 ? 0.2716 0.2415 0.2043 0.0601 -0.0435 -0.0238 667 GLN A O 5091 C CB . GLN A 626 ? 0.2637 0.2237 0.1800 0.0710 -0.0498 -0.0254 667 GLN A CB 5092 C CG . GLN A 626 ? 0.2558 0.2141 0.1677 0.0720 -0.0492 -0.0242 667 GLN A CG 5093 C CD . GLN A 626 ? 0.2897 0.2447 0.1999 0.0751 -0.0551 -0.0276 667 GLN A CD 5094 O OE1 . GLN A 626 ? 0.3233 0.2738 0.2260 0.0812 -0.0579 -0.0289 667 GLN A OE1 5095 N NE2 . GLN A 626 ? 0.3092 0.2663 0.2264 0.0712 -0.0572 -0.0290 667 GLN A NE2 5096 N N . LEU A 627 ? 0.2793 0.2425 0.2001 0.0698 -0.0460 -0.0244 668 LEU A N 5097 C CA . LEU A 627 ? 0.2760 0.2418 0.2030 0.0677 -0.0462 -0.0256 668 LEU A CA 5098 C C . LEU A 627 ? 0.2670 0.2365 0.1976 0.0634 -0.0405 -0.0227 668 LEU A C 5099 O O . LEU A 627 ? 0.2824 0.2558 0.2209 0.0587 -0.0398 -0.0234 668 LEU A O 5100 C CB . LEU A 627 ? 0.2945 0.2566 0.2159 0.0735 -0.0487 -0.0267 668 LEU A CB 5101 C CG . LEU A 627 ? 0.3100 0.2695 0.2313 0.0768 -0.0557 -0.0308 668 LEU A CG 5102 C CD1 . LEU A 627 ? 0.3538 0.3089 0.2680 0.0833 -0.0584 -0.0319 668 LEU A CD1 5103 C CD2 . LEU A 627 ? 0.3799 0.3431 0.3126 0.0723 -0.0587 -0.0337 668 LEU A CD2 5104 N N . MET A 628 ? 0.2736 0.2418 0.1983 0.0648 -0.0362 -0.0195 669 MET A N 5105 C CA . MET A 628 ? 0.2503 0.2215 0.1780 0.0613 -0.0309 -0.0168 669 MET A CA 5106 C C . MET A 628 ? 0.2383 0.2137 0.1723 0.0553 -0.0291 -0.0163 669 MET A C 5107 O O . MET A 628 ? 0.2416 0.2204 0.1813 0.0511 -0.0268 -0.0159 669 MET A O 5108 C CB . MET A 628 ? 0.2741 0.2428 0.1949 0.0644 -0.0269 -0.0135 669 MET A CB 5109 C CG . MET A 628 ? 0.3037 0.2754 0.2282 0.0606 -0.0214 -0.0108 669 MET A CG 5110 S SD . MET A 628 ? 0.1061 0.0746 0.0236 0.0647 -0.0166 -0.0068 669 MET A SD 5111 C CE . MET A 628 ? 0.2942 0.2627 0.2098 0.0640 -0.0159 -0.0056 669 MET A CE 5112 N N . PHE A 629 ? 0.2279 0.2025 0.1602 0.0553 -0.0302 -0.0162 670 PHE A N 5113 C CA . PHE A 629 ? 0.2307 0.2088 0.1680 0.0500 -0.0285 -0.0155 670 PHE A CA 5114 C C . PHE A 629 ? 0.2185 0.1989 0.1628 0.0464 -0.0313 -0.0179 670 PHE A C 5115 O O . PHE A 629 ? 0.2207 0.2038 0.1691 0.0422 -0.0300 -0.0174 670 PHE A O 5116 C CB . PHE A 629 ? 0.2361 0.2127 0.1692 0.0509 -0.0276 -0.0139 670 PHE A CB 5117 C CG . PHE A 629 ? 0.2604 0.2361 0.1892 0.0525 -0.0234 -0.0108 670 PHE A CG 5118 C CD1 . PHE A 629 ? 0.2487 0.2274 0.1812 0.0489 -0.0193 -0.0089 670 PHE A CD1 5119 C CD2 . PHE A 629 ? 0.2488 0.2205 0.1700 0.0576 -0.0232 -0.0097 670 PHE A CD2 5120 C CE1 . PHE A 629 ? 0.2772 0.2552 0.2069 0.0503 -0.0153 -0.0060 670 PHE A CE1 5121 C CE2 . PHE A 629 ? 0.2863 0.2573 0.2044 0.0590 -0.0187 -0.0065 670 PHE A CE2 5122 C CZ . PHE A 629 ? 0.2807 0.2549 0.2036 0.0552 -0.0148 -0.0047 670 PHE A CZ 5123 N N . LEU A 630 ? 0.2277 0.2072 0.1739 0.0482 -0.0351 -0.0207 671 LEU A N 5124 C CA . LEU A 630 ? 0.2282 0.2099 0.1821 0.0449 -0.0375 -0.0229 671 LEU A CA 5125 C C . LEU A 630 ? 0.2018 0.1877 0.1621 0.0400 -0.0343 -0.0223 671 LEU A C 5126 O O . LEU A 630 ? 0.2098 0.1980 0.1747 0.0359 -0.0333 -0.0220 671 LEU A O 5127 C CB . LEU A 630 ? 0.2397 0.2195 0.1950 0.0481 -0.0427 -0.0262 671 LEU A CB 5128 C CG . LEU A 630 ? 0.2530 0.2352 0.2176 0.0448 -0.0451 -0.0286 671 LEU A CG 5129 C CD1 . LEU A 630 ? 0.2679 0.2504 0.2347 0.0423 -0.0458 -0.0286 671 LEU A CD1 5130 C CD2 . LEU A 630 ? 0.2691 0.2489 0.2346 0.0488 -0.0507 -0.0321 671 LEU A CD2 5131 N N . GLU A 631 ? 0.1934 0.1799 0.1537 0.0405 -0.0324 -0.0218 672 GLU A N 5132 C CA . GLU A 631 ? 0.2028 0.1930 0.1684 0.0360 -0.0290 -0.0211 672 GLU A CA 5133 C C . GLU A 631 ? 0.1821 0.1738 0.1465 0.0330 -0.0254 -0.0186 672 GLU A C 5134 O O . GLU A 631 ? 0.1934 0.1880 0.1626 0.0286 -0.0237 -0.0184 672 GLU A O 5135 C CB . GLU A 631 ? 0.1998 0.1902 0.1647 0.0373 -0.0271 -0.0206 672 GLU A CB 5136 C CG . GLU A 631 ? 0.1861 0.1800 0.1572 0.0331 -0.0247 -0.0208 672 GLU A CG 5137 C CD . GLU A 631 ? 0.2417 0.2369 0.2195 0.0323 -0.0276 -0.0236 672 GLU A CD 5138 O OE1 . GLU A 631 ? 0.2377 0.2313 0.2150 0.0355 -0.0300 -0.0250 672 GLU A OE1 5139 O OE2 . GLU A 631 ? 0.2189 0.2165 0.2025 0.0286 -0.0272 -0.0242 672 GLU A OE2 5140 N N . ARG A 632 ? 0.2051 0.1947 0.1634 0.0354 -0.0244 -0.0168 673 ARG A N 5141 C CA . ARG A 632 ? 0.1787 0.1696 0.1361 0.0330 -0.0213 -0.0146 673 ARG A CA 5142 C C . ARG A 632 ? 0.1892 0.1812 0.1491 0.0300 -0.0223 -0.0149 673 ARG A C 5143 O O . ARG A 632 ? 0.2004 0.1945 0.1618 0.0266 -0.0199 -0.0136 673 ARG A O 5144 C CB . ARG A 632 ? 0.1994 0.1876 0.1502 0.0364 -0.0200 -0.0125 673 ARG A CB 5145 C CG . ARG A 632 ? 0.1975 0.1875 0.1485 0.0342 -0.0159 -0.0101 673 ARG A CG 5146 C CD . ARG A 632 ? 0.2143 0.2046 0.1659 0.0347 -0.0134 -0.0094 673 ARG A CD 5147 N NE . ARG A 632 ? 0.1886 0.1755 0.1347 0.0397 -0.0130 -0.0083 673 ARG A NE 5148 C CZ . ARG A 632 ? 0.2121 0.1970 0.1562 0.0430 -0.0144 -0.0092 673 ARG A CZ 5149 N NH1 . ARG A 632 ? 0.2195 0.2053 0.1671 0.0422 -0.0168 -0.0116 673 ARG A NH1 5150 N NH2 . ARG A 632 ? 0.2221 0.2035 0.1603 0.0476 -0.0133 -0.0076 673 ARG A NH2 5151 N N . ALA A 633 ? 0.1803 0.1707 0.1407 0.0315 -0.0260 -0.0166 674 ALA A N 5152 C CA . ALA A 633 ? 0.1887 0.1796 0.1512 0.0293 -0.0270 -0.0168 674 ALA A CA 5153 C C . ALA A 633 ? 0.1858 0.1798 0.1549 0.0247 -0.0259 -0.0172 674 ALA A C 5154 O O . ALA A 633 ? 0.2191 0.2138 0.1899 0.0221 -0.0256 -0.0167 674 ALA A O 5155 C CB . ALA A 633 ? 0.2062 0.1945 0.1681 0.0321 -0.0314 -0.0188 674 ALA A CB 5156 N N . PHE A 634 ? 0.1872 0.1828 0.1600 0.0238 -0.0251 -0.0182 675 PHE A N 5157 C CA . PHE A 634 ? 0.1757 0.1741 0.1545 0.0197 -0.0236 -0.0184 675 PHE A CA 5158 C C . PHE A 634 ? 0.1837 0.1840 0.1615 0.0168 -0.0196 -0.0165 675 PHE A C 5159 O O . PHE A 634 ? 0.1896 0.1920 0.1712 0.0136 -0.0179 -0.0165 675 PHE A O 5160 C CB . PHE A 634 ? 0.1827 0.1822 0.1664 0.0198 -0.0243 -0.0204 675 PHE A CB 5161 C CG . PHE A 634 ? 0.1852 0.1831 0.1716 0.0220 -0.0286 -0.0227 675 PHE A CG 5162 C CD1 . PHE A 634 ? 0.1900 0.1881 0.1810 0.0202 -0.0302 -0.0234 675 PHE A CD1 5163 C CD2 . PHE A 634 ? 0.2286 0.2246 0.2131 0.0259 -0.0312 -0.0242 675 PHE A CD2 5164 C CE1 . PHE A 634 ? 0.2011 0.1976 0.1957 0.0223 -0.0347 -0.0260 675 PHE A CE1 5165 C CE2 . PHE A 634 ? 0.2128 0.2071 0.1997 0.0283 -0.0359 -0.0267 675 PHE A CE2 5166 C CZ . PHE A 634 ? 0.1955 0.1902 0.1879 0.0264 -0.0378 -0.0278 675 PHE A CZ 5167 N N . ILE A 635 ? 0.1754 0.1751 0.1482 0.0181 -0.0182 -0.0149 676 ILE A N 5168 C CA . ILE A 635 ? 0.1818 0.1832 0.1539 0.0156 -0.0149 -0.0133 676 ILE A CA 5169 C C . ILE A 635 ? 0.1850 0.1866 0.1563 0.0136 -0.0147 -0.0122 676 ILE A C 5170 O O . ILE A 635 ? 0.2227 0.2224 0.1914 0.0152 -0.0164 -0.0118 676 ILE A O 5171 C CB . ILE A 635 ? 0.1849 0.1853 0.1528 0.0179 -0.0136 -0.0120 676 ILE A CB 5172 C CG1 . ILE A 635 ? 0.1880 0.1883 0.1569 0.0196 -0.0133 -0.0129 676 ILE A CG1 5173 C CG2 . ILE A 635 ? 0.2063 0.2081 0.1733 0.0157 -0.0107 -0.0104 676 ILE A CG2 5174 C CD1 . ILE A 635 ? 0.1928 0.1957 0.1659 0.0167 -0.0115 -0.0137 676 ILE A CD1 5175 N N . ASP A 636 ? 0.1899 0.1934 0.1629 0.0103 -0.0126 -0.0117 677 ASP A N 5176 C CA . ASP A 636 ? 0.2022 0.2058 0.1738 0.0085 -0.0120 -0.0104 677 ASP A CA 5177 C C . ASP A 636 ? 0.1964 0.2008 0.1654 0.0079 -0.0099 -0.0092 677 ASP A C 5178 O O . ASP A 636 ? 0.1869 0.1928 0.1572 0.0066 -0.0081 -0.0095 677 ASP A O 5179 C CB . ASP A 636 ? 0.1990 0.2038 0.1741 0.0056 -0.0111 -0.0107 677 ASP A CB 5180 C CG . ASP A 636 ? 0.1865 0.1910 0.1599 0.0039 -0.0108 -0.0093 677 ASP A CG 5181 O OD1 . ASP A 636 ? 0.2068 0.2110 0.1766 0.0044 -0.0105 -0.0081 677 ASP A OD1 5182 O OD2 . ASP A 636 ? 0.2073 0.2120 0.1836 0.0023 -0.0106 -0.0094 677 ASP A OD2 5183 N N . PRO A 637 ? 0.2325 0.2360 0.1985 0.0089 -0.0102 -0.0079 678 PRO A N 5184 C CA . PRO A 637 ? 0.2412 0.2455 0.2059 0.0086 -0.0084 -0.0069 678 PRO A CA 5185 C C . PRO A 637 ? 0.2632 0.2691 0.2285 0.0055 -0.0071 -0.0068 678 PRO A C 5186 O O . PRO A 637 ? 0.3125 0.3194 0.2777 0.0047 -0.0056 -0.0067 678 PRO A O 5187 C CB . PRO A 637 ? 0.2455 0.2484 0.2073 0.0102 -0.0093 -0.0056 678 PRO A CB 5188 C CG . PRO A 637 ? 0.2745 0.2761 0.2359 0.0106 -0.0113 -0.0059 678 PRO A CG 5189 C CD . PRO A 637 ? 0.2458 0.2475 0.2099 0.0105 -0.0122 -0.0075 678 PRO A CD 5190 N N . LEU A 638 ? 0.2188 0.2248 0.1849 0.0038 -0.0074 -0.0070 679 LEU A N 5191 C CA . LEU A 638 ? 0.2154 0.2225 0.1811 0.0013 -0.0059 -0.0068 679 LEU A CA 5192 C C . LEU A 638 ? 0.2230 0.2314 0.1909 0.0001 -0.0042 -0.0079 679 LEU A C 5193 O O . LEU A 638 ? 0.2276 0.2367 0.1947 -0.0017 -0.0028 -0.0079 679 LEU A O 5194 C CB . LEU A 638 ? 0.2246 0.2309 0.1897 0.0001 -0.0065 -0.0060 679 LEU A CB 5195 C CG . LEU A 638 ? 0.2515 0.2565 0.2142 0.0012 -0.0081 -0.0049 679 LEU A CG 5196 C CD1 . LEU A 638 ? 0.2618 0.2658 0.2241 0.0000 -0.0086 -0.0040 679 LEU A CD1 5197 C CD2 . LEU A 638 ? 0.2682 0.2736 0.2286 0.0013 -0.0077 -0.0042 679 LEU A CD2 5198 N N . GLY A 639 ? 0.2137 0.2222 0.1842 0.0011 -0.0045 -0.0090 680 GLY A N 5199 C CA . GLY A 639 ? 0.2172 0.2270 0.1903 0.0002 -0.0029 -0.0101 680 GLY A CA 5200 C C . GLY A 639 ? 0.2310 0.2411 0.2062 -0.0016 -0.0021 -0.0104 680 GLY A C 5201 O O . GLY A 639 ? 0.2464 0.2557 0.2211 -0.0023 -0.0027 -0.0095 680 GLY A O 5202 N N . LEU A 640 ? 0.2131 0.2245 0.1910 -0.0025 -0.0005 -0.0114 681 LEU A N 5203 C CA . LEU A 640 ? 0.2127 0.2245 0.1930 -0.0042 0.0010 -0.0114 681 LEU A CA 5204 C C . LEU A 640 ? 0.2222 0.2342 0.1991 -0.0057 0.0032 -0.0108 681 LEU A C 5205 O O . LEU A 640 ? 0.2237 0.2359 0.1976 -0.0055 0.0034 -0.0109 681 LEU A O 5206 C CB . LEU A 640 ? 0.2049 0.2179 0.1899 -0.0042 0.0019 -0.0129 681 LEU A CB 5207 C CG . LEU A 640 ? 0.2033 0.2159 0.1919 -0.0025 -0.0007 -0.0138 681 LEU A CG 5208 C CD1 . LEU A 640 ? 0.2537 0.2674 0.2464 -0.0021 -0.0001 -0.0154 681 LEU A CD1 5209 C CD2 . LEU A 640 ? 0.2564 0.2682 0.2481 -0.0031 -0.0017 -0.0135 681 LEU A CD2 5210 N N . PRO A 641 ? 0.2526 0.2644 0.2299 -0.0072 0.0049 -0.0101 682 PRO A N 5211 C CA . PRO A 641 ? 0.2478 0.2593 0.2208 -0.0082 0.0068 -0.0094 682 PRO A CA 5212 C C . PRO A 641 ? 0.2465 0.2589 0.2180 -0.0083 0.0083 -0.0105 682 PRO A C 5213 O O . PRO A 641 ? 0.2525 0.2660 0.2272 -0.0085 0.0098 -0.0116 682 PRO A O 5214 C CB . PRO A 641 ? 0.2664 0.2775 0.2414 -0.0095 0.0091 -0.0085 682 PRO A CB 5215 C CG . PRO A 641 ? 0.2700 0.2807 0.2494 -0.0092 0.0072 -0.0083 682 PRO A CG 5216 C CD . PRO A 641 ? 0.2623 0.2740 0.2443 -0.0077 0.0051 -0.0099 682 PRO A CD 5217 N N . ASP A 642 ? 0.2610 0.2730 0.2281 -0.0080 0.0075 -0.0105 683 ASP A N 5218 C CA . ASP A 642 ? 0.2628 0.2754 0.2283 -0.0080 0.0084 -0.0117 683 ASP A CA 5219 C C . ASP A 642 ? 0.2338 0.2476 0.2029 -0.0073 0.0080 -0.0131 683 ASP A C 5220 O O . ASP A 642 ? 0.2494 0.2637 0.2181 -0.0073 0.0089 -0.0143 683 ASP A O 5221 C CB . ASP A 642 ? 0.2897 0.3021 0.2534 -0.0089 0.0112 -0.0120 683 ASP A CB 5222 C CG . ASP A 642 ? 0.3914 0.4023 0.3506 -0.0094 0.0118 -0.0105 683 ASP A CG 5223 O OD1 . ASP A 642 ? 0.4017 0.4117 0.3570 -0.0090 0.0100 -0.0100 683 ASP A OD1 5224 O OD2 . ASP A 642 ? 0.4823 0.4928 0.4421 -0.0100 0.0141 -0.0098 683 ASP A OD2 5225 N N . ARG A 643 ? 0.2153 0.2292 0.1875 -0.0064 0.0066 -0.0129 684 ARG A N 5226 C CA . ARG A 643 ? 0.2023 0.2168 0.1774 -0.0052 0.0061 -0.0139 684 ARG A CA 5227 C C . ARG A 643 ? 0.1963 0.2101 0.1711 -0.0037 0.0039 -0.0131 684 ARG A C 5228 O O . ARG A 643 ? 0.1869 0.2003 0.1638 -0.0026 0.0027 -0.0131 684 ARG A O 5229 C CB . ARG A 643 ? 0.1937 0.2090 0.1732 -0.0052 0.0069 -0.0148 684 ARG A CB 5230 C CG . ARG A 643 ? 0.1919 0.2080 0.1718 -0.0066 0.0096 -0.0155 684 ARG A CG 5231 C CD . ARG A 643 ? 0.1919 0.2090 0.1771 -0.0065 0.0106 -0.0166 684 ARG A CD 5232 N NE . ARG A 643 ? 0.2226 0.2397 0.2115 -0.0064 0.0096 -0.0162 684 ARG A NE 5233 C CZ . ARG A 643 ? 0.2274 0.2452 0.2217 -0.0060 0.0093 -0.0172 684 ARG A CZ 5234 N NH1 . ARG A 643 ? 0.1906 0.2094 0.1875 -0.0055 0.0100 -0.0185 684 ARG A NH1 5235 N NH2 . ARG A 643 ? 0.2004 0.2179 0.1980 -0.0060 0.0081 -0.0168 684 ARG A NH2 5236 N N . PRO A 644 ? 0.1935 0.2069 0.1656 -0.0034 0.0032 -0.0125 685 PRO A N 5237 C CA . PRO A 644 ? 0.1874 0.1999 0.1587 -0.0020 0.0015 -0.0114 685 PRO A CA 5238 C C . PRO A 644 ? 0.1773 0.1897 0.1507 -0.0001 0.0011 -0.0117 685 PRO A C 5239 O O . PRO A 644 ? 0.2056 0.2169 0.1782 0.0015 -0.0003 -0.0108 685 PRO A O 5240 C CB . PRO A 644 ? 0.1969 0.2094 0.1661 -0.0022 0.0013 -0.0111 685 PRO A CB 5241 C CG . PRO A 644 ? 0.2078 0.2212 0.1771 -0.0035 0.0027 -0.0123 685 PRO A CG 5242 C CD . PRO A 644 ? 0.2074 0.2211 0.1774 -0.0044 0.0040 -0.0130 685 PRO A CD 5243 N N . PHE A 645 ? 0.1718 0.1849 0.1474 0.0000 0.0022 -0.0128 686 PHE A N 5244 C CA . PHE A 645 ? 0.1554 0.1679 0.1324 0.0021 0.0019 -0.0129 686 PHE A CA 5245 C C . PHE A 645 ? 0.1722 0.1847 0.1515 0.0029 0.0012 -0.0137 686 PHE A C 5246 O O . PHE A 645 ? 0.1850 0.1967 0.1649 0.0050 0.0006 -0.0138 686 PHE A O 5247 C CB . PHE A 645 ? 0.1696 0.1827 0.1480 0.0021 0.0033 -0.0135 686 PHE A CB 5248 C CG . PHE A 645 ? 0.1817 0.1948 0.1589 0.0016 0.0036 -0.0128 686 PHE A CG 5249 C CD1 . PHE A 645 ? 0.2029 0.2150 0.1791 0.0029 0.0028 -0.0114 686 PHE A CD1 5250 C CD2 . PHE A 645 ? 0.1931 0.2071 0.1704 -0.0002 0.0044 -0.0138 686 PHE A CD2 5251 C CE1 . PHE A 645 ? 0.1748 0.1871 0.1508 0.0024 0.0029 -0.0108 686 PHE A CE1 5252 C CE2 . PHE A 645 ? 0.1808 0.1949 0.1576 -0.0006 0.0041 -0.0135 686 PHE A CE2 5253 C CZ . PHE A 645 ? 0.1730 0.1863 0.1496 0.0006 0.0034 -0.0120 686 PHE A CZ 5254 N N . TYR A 646 ? 0.1516 0.1646 0.1319 0.0015 0.0011 -0.0141 687 TYR A N 5255 C CA . TYR A 646 ? 0.1623 0.1751 0.1453 0.0022 0.0000 -0.0149 687 TYR A CA 5256 C C . TYR A 646 ? 0.1761 0.1878 0.1578 0.0026 -0.0019 -0.0140 687 TYR A C 5257 O O . TYR A 646 ? 0.1878 0.1997 0.1692 0.0009 -0.0015 -0.0135 687 TYR A O 5258 C CB . TYR A 646 ? 0.1602 0.1745 0.1467 0.0004 0.0015 -0.0159 687 TYR A CB 5259 C CG . TYR A 646 ? 0.1669 0.1822 0.1552 0.0002 0.0032 -0.0170 687 TYR A CG 5260 C CD1 . TYR A 646 ? 0.1868 0.2016 0.1749 0.0020 0.0028 -0.0173 687 TYR A CD1 5261 C CD2 . TYR A 646 ? 0.1653 0.1819 0.1552 -0.0017 0.0054 -0.0177 687 TYR A CD2 5262 C CE1 . TYR A 646 ? 0.1774 0.1931 0.1674 0.0019 0.0043 -0.0182 687 TYR A CE1 5263 C CE2 . TYR A 646 ? 0.1724 0.1898 0.1639 -0.0018 0.0069 -0.0188 687 TYR A CE2 5264 C CZ . TYR A 646 ? 0.1833 0.2003 0.1750 0.0000 0.0062 -0.0192 687 TYR A CZ 5265 O OH . TYR A 646 ? 0.1909 0.2087 0.1845 -0.0001 0.0077 -0.0203 687 TYR A OH 5266 N N . ARG A 647 ? 0.1559 0.1661 0.1362 0.0051 -0.0038 -0.0137 688 ARG A N 5267 C CA A ARG A 647 ? 0.1617 0.1705 0.1400 0.0059 -0.0056 -0.0129 688 ARG A CA 5268 C CA B ARG A 647 ? 0.1722 0.1810 0.1504 0.0060 -0.0056 -0.0129 688 ARG A CA 5269 C C . ARG A 647 ? 0.1721 0.1799 0.1525 0.0074 -0.0081 -0.0139 688 ARG A C 5270 O O . ARG A 647 ? 0.1915 0.1982 0.1710 0.0079 -0.0098 -0.0136 688 ARG A O 5271 C CB A ARG A 647 ? 0.1700 0.1776 0.1446 0.0079 -0.0058 -0.0117 688 ARG A CB 5272 C CB B ARG A 647 ? 0.1831 0.1906 0.1575 0.0080 -0.0059 -0.0117 688 ARG A CB 5273 C CG A ARG A 647 ? 0.1146 0.1232 0.0882 0.0065 -0.0037 -0.0110 688 ARG A CG 5274 C CG B ARG A 647 ? 0.1858 0.1942 0.1586 0.0064 -0.0041 -0.0106 688 ARG A CG 5275 C CD A ARG A 647 ? 0.1301 0.1378 0.1007 0.0076 -0.0038 -0.0095 688 ARG A CD 5276 C CD B ARG A 647 ? 0.2530 0.2605 0.2237 0.0083 -0.0036 -0.0095 688 ARG A CD 5277 N NE A ARG A 647 ? 0.1158 0.1219 0.0853 0.0108 -0.0043 -0.0091 688 ARG A NE 5278 N NE B ARG A 647 ? 0.2411 0.2496 0.2118 0.0069 -0.0020 -0.0089 688 ARG A NE 5279 C CZ A ARG A 647 ? 0.1587 0.1633 0.1256 0.0129 -0.0046 -0.0078 688 ARG A CZ 5280 C CZ B ARG A 647 ? 0.2515 0.2595 0.2218 0.0083 -0.0012 -0.0079 688 ARG A CZ 5281 N NH1 A ARG A 647 ? 0.1082 0.1111 0.0738 0.0161 -0.0049 -0.0075 688 ARG A NH1 5282 N NH1 B ARG A 647 ? 0.1927 0.2017 0.1639 0.0071 0.0000 -0.0076 688 ARG A NH1 5283 N NH2 A ARG A 647 ? 0.1521 0.1569 0.1178 0.0120 -0.0046 -0.0067 688 ARG A NH2 5284 N NH2 B ARG A 647 ? 0.2896 0.2960 0.2588 0.0111 -0.0015 -0.0072 688 ARG A NH2 5285 N N . HIS A 648 ? 0.1677 0.1759 0.1512 0.0083 -0.0086 -0.0154 689 HIS A N 5286 C CA . HIS A 648 ? 0.1703 0.1775 0.1561 0.0101 -0.0115 -0.0167 689 HIS A CA 5287 C C . HIS A 648 ? 0.1823 0.1906 0.1728 0.0075 -0.0113 -0.0172 689 HIS A C 5288 O O . HIS A 648 ? 0.1874 0.1974 0.1807 0.0052 -0.0090 -0.0173 689 HIS A O 5289 C CB . HIS A 648 ? 0.1648 0.1723 0.1530 0.0116 -0.0118 -0.0181 689 HIS A CB 5290 C CG . HIS A 648 ? 0.1741 0.1798 0.1630 0.0146 -0.0154 -0.0195 689 HIS A CG 5291 N ND1 . HIS A 648 ? 0.1656 0.1714 0.1592 0.0142 -0.0177 -0.0210 689 HIS A ND1 5292 C CD2 . HIS A 648 ? 0.1786 0.1823 0.1641 0.0183 -0.0171 -0.0198 689 HIS A CD2 5293 C CE1 . HIS A 648 ? 0.1971 0.2010 0.1902 0.0176 -0.0211 -0.0224 689 HIS A CE1 5294 N NE2 . HIS A 648 ? 0.1783 0.1807 0.1659 0.0202 -0.0208 -0.0216 689 HIS A NE2 5295 N N . VAL A 649 ? 0.1671 0.1741 0.1584 0.0080 -0.0137 -0.0175 690 VAL A N 5296 C CA . VAL A 649 ? 0.1651 0.1729 0.1609 0.0055 -0.0133 -0.0175 690 VAL A CA 5297 C C . VAL A 649 ? 0.1764 0.1851 0.1793 0.0055 -0.0143 -0.0194 690 VAL A C 5298 O O . VAL A 649 ? 0.1905 0.2004 0.1986 0.0031 -0.0129 -0.0194 690 VAL A O 5299 C CB . VAL A 649 ? 0.1708 0.1769 0.1649 0.0060 -0.0153 -0.0168 690 VAL A CB 5300 C CG1 . VAL A 649 ? 0.1731 0.1796 0.1728 0.0036 -0.0151 -0.0168 690 VAL A CG1 5301 C CG2 . VAL A 649 ? 0.1902 0.1958 0.1782 0.0055 -0.0138 -0.0148 690 VAL A CG2 5302 N N . ILE A 650 ? 0.1618 0.1698 0.1652 0.0082 -0.0168 -0.0210 691 ILE A N 5303 C CA . ILE A 650 ? 0.1632 0.1720 0.1740 0.0083 -0.0182 -0.0231 691 ILE A CA 5304 C C . ILE A 650 ? 0.1819 0.1929 0.1954 0.0071 -0.0154 -0.0234 691 ILE A C 5305 O O . ILE A 650 ? 0.1794 0.1919 0.1998 0.0057 -0.0148 -0.0244 691 ILE A O 5306 C CB . ILE A 650 ? 0.1658 0.1727 0.1763 0.0121 -0.0228 -0.0250 691 ILE A CB 5307 C CG1 . ILE A 650 ? 0.1736 0.1779 0.1802 0.0139 -0.0257 -0.0248 691 ILE A CG1 5308 C CG2 . ILE A 650 ? 0.2004 0.2083 0.2202 0.0120 -0.0248 -0.0274 691 ILE A CG2 5309 C CD1 . ILE A 650 ? 0.1904 0.1948 0.2011 0.0116 -0.0259 -0.0245 691 ILE A CD1 5310 N N . TYR A 651 ? 0.1740 0.1850 0.1823 0.0080 -0.0140 -0.0227 692 TYR A N 5311 C CA . TYR A 651 ? 0.1729 0.1855 0.1833 0.0075 -0.0118 -0.0232 692 TYR A CA 5312 C C . TYR A 651 ? 0.1916 0.2050 0.1977 0.0058 -0.0082 -0.0217 692 TYR A C 5313 O O . TYR A 651 ? 0.1953 0.2075 0.1955 0.0069 -0.0082 -0.0205 692 TYR A O 5314 C CB . TYR A 651 ? 0.1745 0.1859 0.1833 0.0109 -0.0141 -0.0243 692 TYR A CB 5315 C CG . TYR A 651 ? 0.1696 0.1803 0.1830 0.0130 -0.0180 -0.0265 692 TYR A CG 5316 C CD1 . TYR A 651 ? 0.1931 0.2057 0.2148 0.0116 -0.0180 -0.0281 692 TYR A CD1 5317 C CD2 . TYR A 651 ? 0.1768 0.1847 0.1860 0.0167 -0.0217 -0.0270 692 TYR A CD2 5318 C CE1 . TYR A 651 ? 0.2042 0.2161 0.2307 0.0137 -0.0221 -0.0303 692 TYR A CE1 5319 C CE2 . TYR A 651 ? 0.1987 0.2057 0.2118 0.0189 -0.0258 -0.0293 692 TYR A CE2 5320 C CZ . TYR A 651 ? 0.2185 0.2276 0.2405 0.0174 -0.0261 -0.0311 692 TYR A CZ 5321 O OH . TYR A 651 ? 0.2243 0.2326 0.2511 0.0197 -0.0305 -0.0336 692 TYR A OH 5322 N N . ALA A 652 ? 0.1674 0.1827 0.1764 0.0034 -0.0051 -0.0217 693 ALA A N 5323 C CA . ALA A 652 ? 0.1830 0.1990 0.1884 0.0024 -0.0022 -0.0208 693 ALA A CA 5324 C C . ALA A 652 ? 0.1845 0.2022 0.1941 0.0015 -0.0001 -0.0220 693 ALA A C 5325 O O . ALA A 652 ? 0.1894 0.2081 0.2051 0.0012 -0.0004 -0.0231 693 ALA A O 5326 C CB . ALA A 652 ? 0.1877 0.2038 0.1903 0.0000 -0.0001 -0.0193 693 ALA A CB 5327 N N . PRO A 653 ? 0.1723 0.1904 0.1793 0.0013 0.0019 -0.0218 694 PRO A N 5328 C CA . PRO A 653 ? 0.1790 0.1988 0.1897 0.0003 0.0042 -0.0229 694 PRO A CA 5329 C C . PRO A 653 ? 0.1861 0.2070 0.1989 -0.0022 0.0068 -0.0226 694 PRO A C 5330 O O . PRO A 653 ? 0.1893 0.2096 0.1983 -0.0034 0.0077 -0.0212 694 PRO A O 5331 C CB . PRO A 653 ? 0.1889 0.2085 0.1953 0.0004 0.0058 -0.0226 694 PRO A CB 5332 C CG . PRO A 653 ? 0.1993 0.2171 0.2013 0.0022 0.0036 -0.0216 694 PRO A CG 5333 C CD . PRO A 653 ? 0.1798 0.1970 0.1809 0.0018 0.0023 -0.0207 694 PRO A CD 5334 N N . SER A 654 ? 0.1637 0.1860 0.1825 -0.0028 0.0081 -0.0237 695 SER A N 5335 C CA . SER A 654 ? 0.1757 0.1989 0.1966 -0.0049 0.0112 -0.0231 695 SER A CA 5336 C C . SER A 654 ? 0.1876 0.2105 0.2026 -0.0061 0.0141 -0.0222 695 SER A C 5337 O O . SER A 654 ? 0.1826 0.2058 0.1953 -0.0058 0.0150 -0.0229 695 SER A O 5338 C CB . SER A 654 ? 0.1840 0.2089 0.2127 -0.0053 0.0126 -0.0245 695 SER A CB 5339 O OG . SER A 654 ? 0.2110 0.2366 0.2408 -0.0072 0.0166 -0.0237 695 SER A OG 5340 N N . SER A 655 ? 0.1858 0.2082 0.1984 -0.0075 0.0157 -0.0208 696 SER A N 5341 C CA . SER A 655 ? 0.2107 0.2326 0.2172 -0.0084 0.0183 -0.0201 696 SER A CA 5342 C C . SER A 655 ? 0.2095 0.2325 0.2178 -0.0090 0.0218 -0.0210 696 SER A C 5343 O O . SER A 655 ? 0.2251 0.2476 0.2281 -0.0093 0.0237 -0.0210 696 SER A O 5344 C CB . SER A 655 ? 0.2210 0.2418 0.2245 -0.0095 0.0192 -0.0182 696 SER A CB 5345 O OG A SER A 655 ? 0.1324 0.1520 0.1330 -0.0089 0.0161 -0.0174 696 SER A OG 5346 O OG B SER A 655 ? 0.3044 0.3256 0.3130 -0.0105 0.0212 -0.0177 696 SER A OG 5347 N N . HIS A 656 ? 0.2060 0.2304 0.2218 -0.0090 0.0224 -0.0220 697 HIS A N 5348 C CA . HIS A 656 ? 0.2131 0.2387 0.2317 -0.0093 0.0258 -0.0229 697 HIS A CA 5349 C C . HIS A 656 ? 0.2242 0.2507 0.2454 -0.0082 0.0247 -0.0248 697 HIS A C 5350 O O . HIS A 656 ? 0.2392 0.2666 0.2622 -0.0083 0.0274 -0.0258 697 HIS A O 5351 C CB . HIS A 656 ? 0.2252 0.2517 0.2509 -0.0102 0.0280 -0.0225 697 HIS A CB 5352 C CG . HIS A 656 ? 0.2289 0.2542 0.2520 -0.0113 0.0294 -0.0204 697 HIS A CG 5353 N ND1 . HIS A 656 ? 0.2599 0.2843 0.2778 -0.0120 0.0332 -0.0192 697 HIS A ND1 5354 C CD2 . HIS A 656 ? 0.2298 0.2543 0.2540 -0.0116 0.0273 -0.0193 697 HIS A CD2 5355 C CE1 . HIS A 656 ? 0.2658 0.2889 0.2819 -0.0127 0.0335 -0.0173 697 HIS A CE1 5356 N NE2 . HIS A 656 ? 0.2556 0.2788 0.2755 -0.0126 0.0299 -0.0173 697 HIS A NE2 5357 N N . ASN A 657 ? 0.1949 0.2210 0.2163 -0.0069 0.0210 -0.0252 698 ASN A N 5358 C CA . ASN A 657 ? 0.1914 0.2182 0.2156 -0.0055 0.0199 -0.0268 698 ASN A CA 5359 C C . ASN A 657 ? 0.1762 0.2018 0.1980 -0.0039 0.0161 -0.0266 698 ASN A C 5360 O O . ASN A 657 ? 0.1916 0.2170 0.2163 -0.0030 0.0134 -0.0267 698 ASN A O 5361 C CB . ASN A 657 ? 0.1939 0.2222 0.2268 -0.0053 0.0198 -0.0279 698 ASN A CB 5362 C CG . ASN A 657 ? 0.1883 0.2170 0.2243 -0.0035 0.0180 -0.0295 698 ASN A CG 5363 O OD1 . ASN A 657 ? 0.2009 0.2289 0.2326 -0.0027 0.0176 -0.0298 698 ASN A OD1 5364 N ND2 . ASN A 657 ? 0.2129 0.2428 0.2567 -0.0028 0.0168 -0.0307 698 ASN A ND2 5365 N N . LYS A 658 ? 0.1899 0.2145 0.2063 -0.0034 0.0159 -0.0264 699 LYS A N 5366 C CA . LYS A 658 ? 0.1930 0.2163 0.2066 -0.0018 0.0129 -0.0259 699 LYS A CA 5367 C C . LYS A 658 ? 0.1901 0.2134 0.2077 0.0003 0.0105 -0.0268 699 LYS A C 5368 O O . LYS A 658 ? 0.1888 0.2107 0.2046 0.0019 0.0078 -0.0262 699 LYS A O 5369 C CB . LYS A 658 ? 0.2073 0.2300 0.2167 -0.0017 0.0138 -0.0259 699 LYS A CB 5370 C CG . LYS A 658 ? 0.1993 0.2204 0.2053 -0.0002 0.0114 -0.0249 699 LYS A CG 5371 C CD . LYS A 658 ? 0.1956 0.2163 0.1987 -0.0004 0.0126 -0.0249 699 LYS A CD 5372 C CE . LYS A 658 ? 0.2140 0.2332 0.2135 0.0007 0.0109 -0.0235 699 LYS A CE 5373 N NZ . LYS A 658 ? 0.2016 0.2203 0.1998 0.0007 0.0118 -0.0236 699 LYS A NZ 5374 N N . TYR A 659 ? 0.1763 0.2008 0.1991 0.0004 0.0114 -0.0282 700 TYR A N 5375 C CA . TYR A 659 ? 0.1764 0.2006 0.2025 0.0028 0.0086 -0.0292 700 TYR A CA 5376 C C . TYR A 659 ? 0.1930 0.2171 0.2226 0.0034 0.0059 -0.0294 700 TYR A C 5377 O O . TYR A 659 ? 0.2059 0.2289 0.2361 0.0058 0.0027 -0.0299 700 TYR A O 5378 C CB . TYR A 659 ? 0.1871 0.2126 0.2185 0.0031 0.0098 -0.0308 700 TYR A CB 5379 C CG . TYR A 659 ? 0.1771 0.2025 0.2060 0.0031 0.0119 -0.0310 700 TYR A CG 5380 C CD1 . TYR A 659 ? 0.1722 0.1958 0.1961 0.0043 0.0110 -0.0302 700 TYR A CD1 5381 C CD2 . TYR A 659 ? 0.2039 0.2308 0.2360 0.0019 0.0148 -0.0322 700 TYR A CD2 5382 C CE1 . TYR A 659 ? 0.1816 0.2051 0.2042 0.0042 0.0129 -0.0305 700 TYR A CE1 5383 C CE2 . TYR A 659 ? 0.2031 0.2297 0.2332 0.0019 0.0165 -0.0327 700 TYR A CE2 5384 C CZ . TYR A 659 ? 0.2498 0.2747 0.2755 0.0030 0.0154 -0.0319 700 TYR A CZ 5385 O OH . TYR A 659 ? 0.2119 0.2365 0.2365 0.0029 0.0170 -0.0325 700 TYR A OH 5386 N N . ALA A 660 ? 0.1888 0.2139 0.2210 0.0014 0.0072 -0.0291 701 ALA A N 5387 C CA . ALA A 660 ? 0.1947 0.2200 0.2317 0.0017 0.0048 -0.0295 701 ALA A CA 5388 C C . ALA A 660 ? 0.2016 0.2251 0.2338 0.0020 0.0028 -0.0282 701 ALA A C 5389 O O . ALA A 660 ? 0.2176 0.2406 0.2443 0.0008 0.0044 -0.0267 701 ALA A O 5390 C CB . ALA A 660 ? 0.1937 0.2207 0.2364 -0.0007 0.0077 -0.0296 701 ALA A CB 5391 N N . GLY A 661 ? 0.1828 0.2054 0.2173 0.0036 -0.0009 -0.0289 702 GLY A N 5392 C CA . GLY A 661 ? 0.1962 0.2172 0.2268 0.0038 -0.0028 -0.0277 702 GLY A CA 5393 C C . GLY A 661 ? 0.1961 0.2180 0.2316 0.0017 -0.0019 -0.0275 702 GLY A C 5394 O O . GLY A 661 ? 0.2194 0.2429 0.2629 0.0009 -0.0015 -0.0287 702 GLY A O 5395 N N . GLU A 662 ? 0.1920 0.2129 0.2232 0.0007 -0.0016 -0.0259 703 GLU A N 5396 C CA . GLU A 662 ? 0.1858 0.2069 0.2210 -0.0011 -0.0012 -0.0254 703 GLU A CA 5397 C C . GLU A 662 ? 0.1824 0.2015 0.2155 0.0003 -0.0050 -0.0252 703 GLU A C 5398 O O . GLU A 662 ? 0.1931 0.2107 0.2190 0.0016 -0.0060 -0.0244 703 GLU A O 5399 C CB . GLU A 662 ? 0.1955 0.2169 0.2273 -0.0036 0.0029 -0.0234 703 GLU A CB 5400 C CG . GLU A 662 ? 0.2083 0.2300 0.2451 -0.0055 0.0044 -0.0226 703 GLU A CG 5401 C CD . GLU A 662 ? 0.2343 0.2577 0.2813 -0.0059 0.0048 -0.0241 703 GLU A CD 5402 O OE1 . GLU A 662 ? 0.2153 0.2402 0.2644 -0.0068 0.0082 -0.0242 703 GLU A OE1 5403 O OE2 . GLU A 662 ? 0.2408 0.2640 0.2938 -0.0050 0.0014 -0.0254 703 GLU A OE2 5404 N N . SER A 663 ? 0.1744 0.1936 0.2142 0.0001 -0.0069 -0.0260 704 SER A N 5405 C CA . SER A 663 ? 0.1806 0.1978 0.2188 0.0014 -0.0106 -0.0261 704 SER A CA 5406 C C . SER A 663 ? 0.1959 0.2126 0.2330 -0.0009 -0.0086 -0.0241 704 SER A C 5407 O O . SER A 663 ? 0.1898 0.2079 0.2302 -0.0034 -0.0048 -0.0231 704 SER A O 5408 C CB . SER A 663 ? 0.2117 0.2287 0.2578 0.0029 -0.0147 -0.0285 704 SER A CB 5409 O OG . SER A 663 ? 0.2157 0.2347 0.2714 0.0006 -0.0127 -0.0289 704 SER A OG 5410 N N . PHE A 664 ? 0.1790 0.1937 0.2108 0.0000 -0.0108 -0.0233 705 PHE A N 5411 C CA . PHE A 664 ? 0.1801 0.1941 0.2094 -0.0019 -0.0090 -0.0212 705 PHE A CA 5412 C C . PHE A 664 ? 0.1823 0.1976 0.2090 -0.0041 -0.0041 -0.0195 705 PHE A C 5413 O O . PHE A 664 ? 0.1859 0.2016 0.2153 -0.0063 -0.0012 -0.0183 705 PHE A O 5414 C CB . PHE A 664 ? 0.1752 0.1889 0.2121 -0.0029 -0.0101 -0.0215 705 PHE A CB 5415 C CG . PHE A 664 ? 0.1658 0.1777 0.2033 -0.0005 -0.0153 -0.0231 705 PHE A CG 5416 C CD1 . PHE A 664 ? 0.1833 0.1932 0.2130 0.0011 -0.0171 -0.0223 705 PHE A CD1 5417 C CD2 . PHE A 664 ? 0.1820 0.1941 0.2281 0.0003 -0.0183 -0.0254 705 PHE A CD2 5418 C CE1 . PHE A 664 ? 0.1658 0.1737 0.1950 0.0037 -0.0219 -0.0238 705 PHE A CE1 5419 C CE2 . PHE A 664 ? 0.1877 0.1976 0.2338 0.0029 -0.0236 -0.0272 705 PHE A CE2 5420 C CZ . PHE A 664 ? 0.1911 0.1988 0.2284 0.0047 -0.0253 -0.0264 705 PHE A CZ 5421 N N . PRO A 665 ? 0.1690 0.1846 0.1898 -0.0034 -0.0031 -0.0193 706 PRO A N 5422 C CA . PRO A 665 ? 0.1749 0.1915 0.1931 -0.0052 0.0011 -0.0182 706 PRO A CA 5423 C C . PRO A 665 ? 0.1729 0.1888 0.1873 -0.0069 0.0032 -0.0161 706 PRO A C 5424 O O . PRO A 665 ? 0.1864 0.2030 0.2008 -0.0085 0.0069 -0.0153 706 PRO A O 5425 C CB . PRO A 665 ? 0.1845 0.2011 0.1968 -0.0038 0.0007 -0.0185 706 PRO A CB 5426 C CG . PRO A 665 ? 0.1858 0.2007 0.1954 -0.0014 -0.0031 -0.0188 706 PRO A CG 5427 C CD . PRO A 665 ? 0.1972 0.2119 0.2135 -0.0008 -0.0057 -0.0201 706 PRO A CD 5428 N N . GLY A 666 ? 0.1721 0.1863 0.1825 -0.0063 0.0011 -0.0152 707 GLY A N 5429 C CA . GLY A 666 ? 0.1790 0.1923 0.1852 -0.0078 0.0031 -0.0131 707 GLY A CA 5430 C C . GLY A 666 ? 0.1811 0.1945 0.1930 -0.0094 0.0050 -0.0124 707 GLY A C 5431 O O . GLY A 666 ? 0.1957 0.2089 0.2056 -0.0109 0.0086 -0.0108 707 GLY A O 5432 N N . ILE A 667 ? 0.1744 0.1877 0.1934 -0.0091 0.0028 -0.0134 708 ILE A N 5433 C CA . ILE A 667 ? 0.1868 0.2002 0.2127 -0.0108 0.0050 -0.0126 708 ILE A CA 5434 C C . ILE A 667 ? 0.1977 0.2130 0.2281 -0.0119 0.0088 -0.0130 708 ILE A C 5435 O O . ILE A 667 ? 0.2076 0.2229 0.2391 -0.0136 0.0129 -0.0113 708 ILE A O 5436 C CB . ILE A 667 ? 0.1778 0.1908 0.2116 -0.0102 0.0014 -0.0140 708 ILE A CB 5437 C CG1 . ILE A 667 ? 0.2066 0.2177 0.2359 -0.0087 -0.0027 -0.0141 708 ILE A CG1 5438 C CG2 . ILE A 667 ? 0.2026 0.2155 0.2438 -0.0122 0.0040 -0.0128 708 ILE A CG2 5439 C CD1 . ILE A 667 ? 0.2040 0.2145 0.2408 -0.0074 -0.0071 -0.0162 708 ILE A CD1 5440 N N . TYR A 668 ? 0.1957 0.2124 0.2279 -0.0109 0.0077 -0.0150 709 TYR A N 5441 C CA . TYR A 668 ? 0.1966 0.2152 0.2333 -0.0117 0.0111 -0.0155 709 TYR A CA 5442 C C . TYR A 668 ? 0.1917 0.2101 0.2219 -0.0128 0.0157 -0.0137 709 TYR A C 5443 O O . TYR A 668 ? 0.2038 0.2226 0.2369 -0.0142 0.0198 -0.0126 709 TYR A O 5444 C CB . TYR A 668 ? 0.1893 0.2092 0.2274 -0.0101 0.0091 -0.0178 709 TYR A CB 5445 C CG . TYR A 668 ? 0.1946 0.2163 0.2379 -0.0110 0.0126 -0.0184 709 TYR A CG 5446 C CD1 . TYR A 668 ? 0.2051 0.2282 0.2589 -0.0111 0.0122 -0.0198 709 TYR A CD1 5447 C CD2 . TYR A 668 ? 0.2105 0.2327 0.2483 -0.0115 0.0164 -0.0177 709 TYR A CD2 5448 C CE1 . TYR A 668 ? 0.2072 0.2323 0.2664 -0.0119 0.0158 -0.0203 709 TYR A CE1 5449 C CE2 . TYR A 668 ? 0.1918 0.2157 0.2342 -0.0122 0.0199 -0.0183 709 TYR A CE2 5450 C CZ . TYR A 668 ? 0.2167 0.2420 0.2699 -0.0124 0.0198 -0.0195 709 TYR A CZ 5451 O OH . TYR A 668 ? 0.2319 0.2590 0.2903 -0.0129 0.0233 -0.0201 709 TYR A OH 5452 N N . ASP A 669 ? 0.1915 0.2092 0.2127 -0.0121 0.0150 -0.0134 710 ASP A N 5453 C CA . ASP A 669 ? 0.1951 0.2125 0.2100 -0.0128 0.0187 -0.0122 710 ASP A CA 5454 C C . ASP A 669 ? 0.2104 0.2262 0.2230 -0.0140 0.0210 -0.0097 710 ASP A C 5455 O O . ASP A 669 ? 0.2379 0.2533 0.2477 -0.0146 0.0249 -0.0086 710 ASP A O 5456 C CB . ASP A 669 ? 0.2064 0.2234 0.2133 -0.0117 0.0169 -0.0126 710 ASP A CB 5457 C CG . ASP A 669 ? 0.2358 0.2542 0.2441 -0.0108 0.0162 -0.0147 710 ASP A CG 5458 O OD1 . ASP A 669 ? 0.2276 0.2474 0.2418 -0.0110 0.0178 -0.0157 710 ASP A OD1 5459 O OD2 . ASP A 669 ? 0.2510 0.2690 0.2544 -0.0097 0.0142 -0.0151 710 ASP A OD2 5460 N N . ALA A 670 ? 0.2118 0.2263 0.2248 -0.0139 0.0186 -0.0089 711 ALA A N 5461 C CA . ALA A 670 ? 0.2107 0.2235 0.2220 -0.0150 0.0208 -0.0064 711 ALA A CA 5462 C C . ALA A 670 ? 0.2156 0.2288 0.2349 -0.0163 0.0247 -0.0056 711 ALA A C 5463 O O . ALA A 670 ? 0.2327 0.2447 0.2498 -0.0171 0.0288 -0.0033 711 ALA A O 5464 C CB . ALA A 670 ? 0.2115 0.2228 0.2230 -0.0147 0.0173 -0.0059 711 ALA A CB 5465 N N . LEU A 671 ? 0.2172 0.2321 0.2458 -0.0163 0.0237 -0.0073 712 LEU A N 5466 C CA . LEU A 671 ? 0.2218 0.2375 0.2597 -0.0175 0.0273 -0.0067 712 LEU A CA 5467 C C . LEU A 671 ? 0.2315 0.2486 0.2697 -0.0177 0.0316 -0.0070 712 LEU A C 5468 O O . LEU A 671 ? 0.2544 0.2719 0.2987 -0.0187 0.0359 -0.0059 712 LEU A O 5469 C CB . LEU A 671 ? 0.2186 0.2355 0.2673 -0.0173 0.0239 -0.0088 712 LEU A CB 5470 C CG . LEU A 671 ? 0.2168 0.2322 0.2684 -0.0175 0.0206 -0.0083 712 LEU A CG 5471 C CD1 . LEU A 671 ? 0.2128 0.2292 0.2727 -0.0166 0.0158 -0.0111 712 LEU A CD1 5472 C CD2 . LEU A 671 ? 0.2445 0.2588 0.3006 -0.0191 0.0247 -0.0057 712 LEU A CD2 5473 N N . PHE A 672 ? 0.2260 0.2439 0.2587 -0.0167 0.0305 -0.0085 713 PHE A N 5474 C CA . PHE A 672 ? 0.2333 0.2526 0.2674 -0.0167 0.0339 -0.0094 713 PHE A CA 5475 C C . PHE A 672 ? 0.2369 0.2550 0.2662 -0.0173 0.0396 -0.0071 713 PHE A C 5476 O O . PHE A 672 ? 0.2473 0.2635 0.2668 -0.0169 0.0400 -0.0058 713 PHE A O 5477 C CB . PHE A 672 ? 0.2434 0.2636 0.2722 -0.0155 0.0316 -0.0114 713 PHE A CB 5478 C CG . PHE A 672 ? 0.2341 0.2559 0.2649 -0.0154 0.0349 -0.0125 713 PHE A CG 5479 C CD1 . PHE A 672 ? 0.2381 0.2619 0.2786 -0.0153 0.0343 -0.0143 713 PHE A CD1 5480 C CD2 . PHE A 672 ? 0.2477 0.2686 0.2711 -0.0153 0.0386 -0.0118 713 PHE A CD2 5481 C CE1 . PHE A 672 ? 0.2725 0.2979 0.3156 -0.0152 0.0374 -0.0153 713 PHE A CE1 5482 C CE2 . PHE A 672 ? 0.2595 0.2817 0.2848 -0.0151 0.0417 -0.0129 713 PHE A CE2 5483 C CZ . PHE A 672 ? 0.2778 0.3023 0.3133 -0.0152 0.0413 -0.0145 713 PHE A CZ 5484 N N . ASP A 673 ? 0.2467 0.2657 0.2829 -0.0179 0.0440 -0.0066 714 ASP A N 5485 C CA . ASP A 673 ? 0.2700 0.2876 0.3015 -0.0181 0.0500 -0.0043 714 ASP A CA 5486 C C . ASP A 673 ? 0.2817 0.2964 0.3077 -0.0184 0.0513 -0.0014 714 ASP A C 5487 O O . ASP A 673 ? 0.2971 0.3099 0.3146 -0.0179 0.0548 0.0004 714 ASP A O 5488 C CB . ASP A 673 ? 0.2725 0.2899 0.2945 -0.0170 0.0510 -0.0054 714 ASP A CB 5489 C CG . ASP A 673 ? 0.3016 0.3178 0.3197 -0.0167 0.0575 -0.0037 714 ASP A CG 5490 O OD1 . ASP A 673 ? 0.3058 0.3226 0.3319 -0.0174 0.0618 -0.0027 714 ASP A OD1 5491 O OD2 . ASP A 673 ? 0.3298 0.3442 0.3369 -0.0158 0.0582 -0.0034 714 ASP A OD2 5492 N N . ILE A 674 ? 0.2753 0.2896 0.3063 -0.0191 0.0483 -0.0008 715 ILE A N 5493 C CA . ILE A 674 ? 0.2674 0.2790 0.2929 -0.0193 0.0486 0.0018 715 ILE A CA 5494 C C . ILE A 674 ? 0.3007 0.3106 0.3267 -0.0198 0.0551 0.0050 715 ILE A C 5495 O O . ILE A 674 ? 0.3036 0.3107 0.3212 -0.0194 0.0566 0.0075 715 ILE A O 5496 C CB . ILE A 674 ? 0.2671 0.2786 0.2986 -0.0198 0.0441 0.0016 715 ILE A CB 5497 C CG1 . ILE A 674 ? 0.2683 0.2769 0.2927 -0.0198 0.0436 0.0040 715 ILE A CG1 5498 C CG2 . ILE A 674 ? 0.2456 0.2584 0.2909 -0.0210 0.0453 0.0015 715 ILE A CG2 5499 C CD1 . ILE A 674 ? 0.2976 0.3061 0.3250 -0.0198 0.0380 0.0030 715 ILE A CD1 5500 N N . GLU A 675 ? 0.3064 0.3177 0.3422 -0.0205 0.0589 0.0051 716 GLU A N 5501 C CA . GLU A 675 ? 0.3422 0.3519 0.3796 -0.0209 0.0658 0.0084 716 GLU A CA 5502 C C . GLU A 675 ? 0.3654 0.3731 0.3903 -0.0195 0.0700 0.0096 716 GLU A C 5503 O O . GLU A 675 ? 0.3872 0.3925 0.4097 -0.0192 0.0758 0.0128 716 GLU A O 5504 C CB . GLU A 675 ? 0.3387 0.3507 0.3902 -0.0218 0.0690 0.0079 716 GLU A CB 5505 C CG . GLU A 675 ? 0.3574 0.3717 0.4091 -0.0211 0.0706 0.0057 716 GLU A CG 5506 C CD . GLU A 675 ? 0.3946 0.4118 0.4511 -0.0210 0.0644 0.0018 716 GLU A CD 5507 O OE1 . GLU A 675 ? 0.3385 0.3557 0.3938 -0.0210 0.0586 0.0006 716 GLU A OE1 5508 O OE2 . GLU A 675 ? 0.4219 0.4413 0.4830 -0.0208 0.0657 0.0000 716 GLU A OE2 5509 N N . SER A 676 ? 0.3734 0.3818 0.3902 -0.0184 0.0671 0.0072 717 SER A N 5510 C CA A SER A 676 ? 0.3873 0.3937 0.3918 -0.0168 0.0700 0.0077 717 SER A CA 5511 C CA B SER A 676 ? 0.3993 0.4058 0.4038 -0.0168 0.0700 0.0077 717 SER A CA 5512 C C . SER A 676 ? 0.4078 0.4115 0.3999 -0.0159 0.0672 0.0085 717 SER A C 5513 O O . SER A 676 ? 0.4307 0.4322 0.4118 -0.0144 0.0693 0.0091 717 SER A O 5514 C CB A SER A 676 ? 0.3784 0.3872 0.3822 -0.0162 0.0690 0.0044 717 SER A CB 5515 C CB B SER A 676 ? 0.3942 0.4028 0.3977 -0.0162 0.0690 0.0045 717 SER A CB 5516 O OG A SER A 676 ? 0.3254 0.3366 0.3401 -0.0168 0.0722 0.0037 717 SER A OG 5517 O OG B SER A 676 ? 0.4135 0.4224 0.4104 -0.0156 0.0632 0.0023 717 SER A OG 5518 N N . LYS A 677 ? 0.4062 0.4098 0.3997 -0.0166 0.0625 0.0085 718 LYS A N 5519 C CA . LYS A 677 ? 0.4173 0.4186 0.3999 -0.0157 0.0595 0.0092 718 LYS A CA 5520 C C . LYS A 677 ? 0.4343 0.4319 0.4109 -0.0152 0.0635 0.0129 718 LYS A C 5521 O O . LYS A 677 ? 0.4310 0.4279 0.4144 -0.0161 0.0669 0.0154 718 LYS A O 5522 C CB . LYS A 677 ? 0.4150 0.4172 0.4006 -0.0164 0.0534 0.0082 718 LYS A CB 5523 C CG . LYS A 677 ? 0.4210 0.4262 0.4106 -0.0165 0.0489 0.0047 718 LYS A CG 5524 C CD . LYS A 677 ? 0.4880 0.4934 0.4690 -0.0153 0.0478 0.0028 718 LYS A CD 5525 C CE . LYS A 677 ? 0.5161 0.5246 0.5026 -0.0154 0.0447 -0.0004 718 LYS A CE 5526 N NZ . LYS A 677 ? 0.4971 0.5063 0.4857 -0.0155 0.0392 -0.0014 718 LYS A NZ 5527 N N . VAL A 678 ? 0.4525 0.4476 0.4166 -0.0136 0.0628 0.0133 719 VAL A N 5528 C CA . VAL A 678 ? 0.4770 0.4682 0.4332 -0.0125 0.0671 0.0168 719 VAL A CA 5529 C C . VAL A 678 ? 0.4713 0.4607 0.4287 -0.0131 0.0655 0.0192 719 VAL A C 5530 O O . VAL A 678 ? 0.4784 0.4650 0.4354 -0.0130 0.0699 0.0227 719 VAL A O 5531 C CB . VAL A 678 ? 0.4928 0.4820 0.4351 -0.0103 0.0664 0.0158 719 VAL A CB 5532 C CG1 . VAL A 678 ? 0.5222 0.5078 0.4544 -0.0091 0.0647 0.0178 719 VAL A CG1 5533 C CG2 . VAL A 678 ? 0.5156 0.5038 0.4545 -0.0089 0.0723 0.0161 719 VAL A CG2 5534 N N . ASP A 679 ? 0.4511 0.4420 0.4107 -0.0139 0.0594 0.0174 720 ASP A N 5535 C CA . ASP A 679 ? 0.4356 0.4250 0.3964 -0.0145 0.0570 0.0192 720 ASP A CA 5536 C C . ASP A 679 ? 0.4161 0.4083 0.3897 -0.0163 0.0541 0.0179 720 ASP A C 5537 O O . ASP A 679 ? 0.3998 0.3939 0.3744 -0.0164 0.0486 0.0154 720 ASP A O 5538 C CB . ASP A 679 ? 0.4407 0.4290 0.3914 -0.0133 0.0521 0.0183 720 ASP A CB 5539 C CG . ASP A 679 ? 0.4543 0.4410 0.4053 -0.0137 0.0495 0.0201 720 ASP A CG 5540 O OD1 . ASP A 679 ? 0.4577 0.4443 0.4174 -0.0150 0.0506 0.0216 720 ASP A OD1 5541 O OD2 . ASP A 679 ? 0.5164 0.5018 0.4590 -0.0126 0.0461 0.0198 720 ASP A OD2 5542 N N . PRO A 680 ? 0.3992 0.3916 0.3829 -0.0175 0.0577 0.0194 721 PRO A N 5543 C CA . PRO A 680 ? 0.3878 0.3827 0.3842 -0.0190 0.0548 0.0178 721 PRO A CA 5544 C C . PRO A 680 ? 0.3747 0.3690 0.3716 -0.0193 0.0495 0.0176 721 PRO A C 5545 O O . PRO A 680 ? 0.3536 0.3501 0.3568 -0.0197 0.0449 0.0150 721 PRO A O 5546 C CB . PRO A 680 ? 0.4004 0.3949 0.4068 -0.0201 0.0602 0.0201 721 PRO A CB 5547 C CG . PRO A 680 ? 0.4259 0.4169 0.4239 -0.0192 0.0660 0.0237 721 PRO A CG 5548 C CD . PRO A 680 ? 0.4185 0.4086 0.4024 -0.0173 0.0648 0.0228 721 PRO A CD 5549 N N . SER A 681 ? 0.3688 0.3598 0.3588 -0.0187 0.0500 0.0203 722 SER A N 5550 C CA . SER A 681 ? 0.3682 0.3586 0.3583 -0.0188 0.0450 0.0201 722 SER A CA 5551 C C . SER A 681 ? 0.3578 0.3500 0.3431 -0.0180 0.0393 0.0169 722 SER A C 5552 O O . SER A 681 ? 0.3413 0.3347 0.3314 -0.0183 0.0348 0.0151 722 SER A O 5553 C CB . SER A 681 ? 0.3877 0.3742 0.3698 -0.0182 0.0465 0.0235 722 SER A CB 5554 O OG . SER A 681 ? 0.4442 0.4300 0.4281 -0.0184 0.0421 0.0234 722 SER A OG 5555 N N . LYS A 682 ? 0.3499 0.3420 0.3257 -0.0169 0.0397 0.0163 723 LYS A N 5556 C CA . LYS A 682 ? 0.3586 0.3526 0.3305 -0.0161 0.0351 0.0135 723 LYS A CA 5557 C C . LYS A 682 ? 0.3295 0.3268 0.3097 -0.0167 0.0332 0.0105 723 LYS A C 5558 O O . LYS A 682 ? 0.3183 0.3169 0.2999 -0.0164 0.0286 0.0085 723 LYS A O 5559 C CB . LYS A 682 ? 0.3822 0.3754 0.3436 -0.0149 0.0363 0.0133 723 LYS A CB 5560 C CG . LYS A 682 ? 0.4413 0.4359 0.3981 -0.0141 0.0317 0.0108 723 LYS A CG 5561 C CD . LYS A 682 ? 0.5302 0.5238 0.4771 -0.0128 0.0327 0.0104 723 LYS A CD 5562 C CE . LYS A 682 ? 0.5804 0.5755 0.5241 -0.0121 0.0280 0.0079 723 LYS A CE 5563 N NZ . LYS A 682 ? 0.6562 0.6505 0.5914 -0.0109 0.0287 0.0070 723 LYS A NZ 5564 N N . ALA A 683 ? 0.3112 0.3096 0.2961 -0.0172 0.0370 0.0103 724 ALA A N 5565 C CA . ALA A 683 ? 0.2906 0.2921 0.2828 -0.0175 0.0355 0.0074 724 ALA A CA 5566 C C . ALA A 683 ? 0.2843 0.2867 0.2862 -0.0182 0.0323 0.0066 724 ALA A C 5567 O O . ALA A 683 ? 0.2607 0.2649 0.2653 -0.0177 0.0283 0.0040 724 ALA A O 5568 C CB . ALA A 683 ? 0.3014 0.3039 0.2975 -0.0179 0.0405 0.0076 724 ALA A CB 5569 N N . TRP A 684 ? 0.2572 0.2583 0.2649 -0.0191 0.0343 0.0086 725 TRP A N 5570 C CA . TRP A 684 ? 0.2488 0.2505 0.2661 -0.0197 0.0309 0.0075 725 TRP A CA 5571 C C . TRP A 684 ? 0.2382 0.2389 0.2513 -0.0189 0.0257 0.0069 725 TRP A C 5572 O O . TRP A 684 ? 0.2327 0.2343 0.2509 -0.0185 0.0213 0.0048 725 TRP A O 5573 C CB . TRP A 684 ? 0.2367 0.2373 0.2625 -0.0210 0.0344 0.0097 725 TRP A CB 5574 C CG . TRP A 684 ? 0.2546 0.2570 0.2883 -0.0217 0.0382 0.0092 725 TRP A CG 5575 C CD1 . TRP A 684 ? 0.2433 0.2453 0.2751 -0.0219 0.0443 0.0112 725 TRP A CD1 5576 C CD2 . TRP A 684 ? 0.2432 0.2483 0.2874 -0.0220 0.0361 0.0064 725 TRP A CD2 5577 N NE1 . TRP A 684 ? 0.2696 0.2740 0.3111 -0.0225 0.0463 0.0098 725 TRP A NE1 5578 C CE2 . TRP A 684 ? 0.2513 0.2577 0.3005 -0.0226 0.0411 0.0068 725 TRP A CE2 5579 C CE3 . TRP A 684 ? 0.2289 0.2353 0.2787 -0.0216 0.0303 0.0035 725 TRP A CE3 5580 C CZ2 . TRP A 684 ? 0.2480 0.2572 0.3084 -0.0230 0.0404 0.0044 725 TRP A CZ2 5581 C CZ3 . TRP A 684 ? 0.2367 0.2456 0.2968 -0.0218 0.0294 0.0010 725 TRP A CZ3 5582 C CH2 . TRP A 684 ? 0.2542 0.2645 0.3198 -0.0225 0.0343 0.0015 725 TRP A CH2 5583 N N . GLY A 685 ? 0.2511 0.2498 0.2545 -0.0183 0.0260 0.0087 726 GLY A N 5584 C CA . GLY A 685 ? 0.2495 0.2473 0.2477 -0.0174 0.0213 0.0082 726 GLY A CA 5585 C C . GLY A 685 ? 0.2434 0.2434 0.2403 -0.0163 0.0178 0.0052 726 GLY A C 5586 O O . GLY A 685 ? 0.2515 0.2517 0.2500 -0.0156 0.0135 0.0038 726 GLY A O 5587 N N . GLU A 686 ? 0.2379 0.2393 0.2319 -0.0161 0.0196 0.0043 727 GLU A N 5588 C CA . GLU A 686 ? 0.2429 0.2462 0.2356 -0.0151 0.0165 0.0017 727 GLU A CA 5589 C C . GLU A 686 ? 0.2330 0.2381 0.2349 -0.0151 0.0147 -0.0004 727 GLU A C 5590 O O . GLU A 686 ? 0.2133 0.2191 0.2155 -0.0140 0.0109 -0.0023 727 GLU A O 5591 C CB . GLU A 686 ? 0.2607 0.2648 0.2478 -0.0149 0.0189 0.0014 727 GLU A CB 5592 C CG A GLU A 686 ? 0.2745 0.2805 0.2608 -0.0139 0.0163 -0.0012 727 GLU A CG 5593 C CD A GLU A 686 ? 0.3081 0.3137 0.2894 -0.0128 0.0124 -0.0015 727 GLU A CD 5594 O OE1 A GLU A 686 ? 0.2852 0.2890 0.2627 -0.0127 0.0116 0.0000 727 GLU A OE1 5595 O OE2 A GLU A 686 ? 0.2927 0.2996 0.2744 -0.0119 0.0103 -0.0034 727 GLU A OE2 5596 N N . VAL A 687 ? 0.2164 0.2220 0.2263 -0.0162 0.0173 -0.0002 728 VAL A N 5597 C CA . VAL A 687 ? 0.2194 0.2264 0.2387 -0.0160 0.0148 -0.0023 728 VAL A CA 5598 C C . VAL A 687 ? 0.2172 0.2228 0.2380 -0.0153 0.0102 -0.0028 728 VAL A C 5599 O O . VAL A 687 ? 0.2183 0.2247 0.2411 -0.0140 0.0063 -0.0051 728 VAL A O 5600 C CB . VAL A 687 ? 0.2115 0.2192 0.2407 -0.0174 0.0181 -0.0019 728 VAL A CB 5601 C CG1 . VAL A 687 ? 0.2189 0.2276 0.2584 -0.0172 0.0147 -0.0043 728 VAL A CG1 5602 C CG2 . VAL A 687 ? 0.2232 0.2322 0.2510 -0.0179 0.0228 -0.0016 728 VAL A CG2 5603 N N . LYS A 688 ? 0.2113 0.2148 0.2311 -0.0160 0.0109 -0.0007 729 LYS A N 5604 C CA . LYS A 688 ? 0.2100 0.2121 0.2312 -0.0152 0.0067 -0.0011 729 LYS A CA 5605 C C . LYS A 688 ? 0.2111 0.2130 0.2245 -0.0134 0.0030 -0.0022 729 LYS A C 5606 O O . LYS A 688 ? 0.2064 0.2080 0.2215 -0.0120 -0.0011 -0.0040 729 LYS A O 5607 C CB B LYS A 688 ? 0.2146 0.2144 0.2360 -0.0163 0.0086 0.0016 729 LYS A CB 5608 C CB C LYS A 688 ? 0.2152 0.2148 0.2354 -0.0162 0.0084 0.0017 729 LYS A CB 5609 C CG B LYS A 688 ? 0.1693 0.1693 0.2008 -0.0180 0.0119 0.0024 729 LYS A CG 5610 C CG C LYS A 688 ? 0.2204 0.2196 0.2509 -0.0177 0.0107 0.0026 729 LYS A CG 5611 C CD B LYS A 688 ? 0.2412 0.2386 0.2732 -0.0191 0.0144 0.0056 729 LYS A CD 5612 C CD C LYS A 688 ? 0.2408 0.2373 0.2695 -0.0186 0.0128 0.0058 729 LYS A CD 5613 C CE B LYS A 688 ? 0.2613 0.2568 0.2943 -0.0184 0.0099 0.0052 729 LYS A CE 5614 C CE C LYS A 688 ? 0.2490 0.2449 0.2714 -0.0192 0.0182 0.0086 729 LYS A CE 5615 N NZ B LYS A 688 ? 0.2970 0.2898 0.3315 -0.0196 0.0125 0.0083 729 LYS A NZ 5616 N NZ C LYS A 688 ? 0.2585 0.2515 0.2803 -0.0200 0.0211 0.0120 729 LYS A NZ 5617 N N . ARG A 689 ? 0.2071 0.2091 0.2120 -0.0132 0.0046 -0.0011 730 ARG A N 5618 C CA . ARG A 689 ? 0.2089 0.2109 0.2072 -0.0116 0.0017 -0.0020 730 ARG A CA 5619 C C . ARG A 689 ? 0.2044 0.2080 0.2050 -0.0103 -0.0005 -0.0046 730 ARG A C 5620 O O . ARG A 689 ? 0.2053 0.2084 0.2047 -0.0086 -0.0041 -0.0057 730 ARG A O 5621 C CB . ARG A 689 ? 0.2283 0.2304 0.2186 -0.0118 0.0038 -0.0008 730 ARG A CB 5622 C CG . ARG A 689 ? 0.2337 0.2355 0.2180 -0.0103 0.0009 -0.0011 730 ARG A CG 5623 C CD . ARG A 689 ? 0.2837 0.2854 0.2604 -0.0104 0.0025 -0.0001 730 ARG A CD 5624 N NE . ARG A 689 ? 0.2594 0.2629 0.2353 -0.0104 0.0039 -0.0014 730 ARG A NE 5625 C CZ . ARG A 689 ? 0.2951 0.2996 0.2696 -0.0092 0.0021 -0.0028 730 ARG A CZ 5626 N NH1 . ARG A 689 ? 0.3130 0.3171 0.2871 -0.0078 -0.0010 -0.0032 730 ARG A NH1 5627 N NH2 . ARG A 689 ? 0.3265 0.3325 0.3005 -0.0093 0.0036 -0.0039 730 ARG A NH2 5628 N N . GLN A 690 ? 0.1903 0.1956 0.1945 -0.0109 0.0016 -0.0055 731 GLN A N 5629 C CA . GLN A 690 ? 0.1926 0.1994 0.1990 -0.0096 -0.0005 -0.0079 731 GLN A CA 5630 C C . GLN A 690 ? 0.2065 0.2129 0.2199 -0.0086 -0.0039 -0.0096 731 GLN A C 5631 O O . GLN A 690 ? 0.1908 0.1972 0.2036 -0.0066 -0.0071 -0.0114 731 GLN A O 5632 C CB . GLN A 690 ? 0.2116 0.2203 0.2199 -0.0104 0.0026 -0.0084 731 GLN A CB 5633 C CG . GLN A 690 ? 0.1898 0.1986 0.1906 -0.0109 0.0054 -0.0072 731 GLN A CG 5634 C CD . GLN A 690 ? 0.2292 0.2381 0.2242 -0.0093 0.0030 -0.0079 731 GLN A CD 5635 O OE1 . GLN A 690 ? 0.2028 0.2121 0.1996 -0.0077 0.0003 -0.0096 731 GLN A OE1 5636 N NE2 . GLN A 690 ? 0.2678 0.2761 0.2558 -0.0094 0.0039 -0.0067 731 GLN A NE2 5637 N N . ILE A 691 ? 0.2005 0.2062 0.2204 -0.0099 -0.0033 -0.0091 732 ILE A N 5638 C CA . ILE A 691 ? 0.1950 0.2001 0.2217 -0.0089 -0.0073 -0.0110 732 ILE A CA 5639 C C . ILE A 691 ? 0.2071 0.2102 0.2286 -0.0070 -0.0112 -0.0113 732 ILE A C 5640 O O . ILE A 691 ? 0.2160 0.2187 0.2383 -0.0048 -0.0150 -0.0135 732 ILE A O 5641 C CB . ILE A 691 ? 0.1893 0.1940 0.2246 -0.0108 -0.0058 -0.0102 732 ILE A CB 5642 C CG1 . ILE A 691 ? 0.1898 0.1965 0.2317 -0.0123 -0.0022 -0.0103 732 ILE A CG1 5643 C CG2 . ILE A 691 ? 0.2177 0.2212 0.2596 -0.0096 -0.0106 -0.0123 732 ILE A CG2 5644 C CD1 . ILE A 691 ? 0.2100 0.2163 0.2604 -0.0145 0.0007 -0.0087 732 ILE A CD1 5645 N N . TYR A 692 ? 0.2015 0.2034 0.2174 -0.0075 -0.0101 -0.0091 733 TYR A N 5646 C CA . TYR A 692 ? 0.2085 0.2085 0.2189 -0.0057 -0.0133 -0.0091 733 TYR A CA 5647 C C . TYR A 692 ? 0.2022 0.2027 0.2068 -0.0035 -0.0148 -0.0102 733 TYR A C 5648 O O . TYR A 692 ? 0.2185 0.2179 0.2222 -0.0011 -0.0184 -0.0117 733 TYR A O 5649 C CB . TYR A 692 ? 0.2330 0.2319 0.2379 -0.0068 -0.0112 -0.0064 733 TYR A CB 5650 C CG . TYR A 692 ? 0.2755 0.2730 0.2730 -0.0052 -0.0132 -0.0058 733 TYR A CG 5651 C CD1 . TYR A 692 ? 0.2963 0.2922 0.2942 -0.0032 -0.0172 -0.0070 733 TYR A CD1 5652 C CD2 . TYR A 692 ? 0.2688 0.2666 0.2595 -0.0058 -0.0111 -0.0039 733 TYR A CD2 5653 C CE1 . TYR A 692 ? 0.2879 0.2824 0.2791 -0.0018 -0.0185 -0.0061 733 TYR A CE1 5654 C CE2 . TYR A 692 ? 0.2780 0.2747 0.2629 -0.0045 -0.0126 -0.0032 733 TYR A CE2 5655 C CZ . TYR A 692 ? 0.3110 0.3061 0.2963 -0.0026 -0.0161 -0.0041 733 TYR A CZ 5656 O OH . TYR A 692 ? 0.3396 0.3336 0.3192 -0.0014 -0.0172 -0.0032 733 TYR A OH 5657 N N . VAL A 693 ? 0.2100 0.2121 0.2109 -0.0041 -0.0121 -0.0096 734 VAL A N 5658 C CA . VAL A 693 ? 0.1945 0.1970 0.1907 -0.0020 -0.0133 -0.0105 734 VAL A CA 5659 C C . VAL A 693 ? 0.1969 0.1995 0.1967 0.0000 -0.0159 -0.0129 734 VAL A C 5660 O O . VAL A 693 ? 0.2048 0.2063 0.2015 0.0026 -0.0186 -0.0139 734 VAL A O 5661 C CB . VAL A 693 ? 0.2078 0.2119 0.2004 -0.0031 -0.0100 -0.0096 734 VAL A CB 5662 C CG1 . VAL A 693 ? 0.2025 0.2071 0.1918 -0.0010 -0.0110 -0.0106 734 VAL A CG1 5663 C CG2 . VAL A 693 ? 0.2294 0.2328 0.2167 -0.0042 -0.0084 -0.0074 734 VAL A CG2 5664 N N . ALA A 694 ? 0.1762 0.1800 0.1830 -0.0012 -0.0152 -0.0140 735 ALA A N 5665 C CA . ALA A 694 ? 0.1699 0.1741 0.1808 0.0007 -0.0179 -0.0165 735 ALA A CA 5666 C C . ALA A 694 ? 0.1623 0.1643 0.1753 0.0028 -0.0224 -0.0181 735 ALA A C 5667 O O . ALA A 694 ? 0.1901 0.1911 0.2008 0.0058 -0.0256 -0.0197 735 ALA A O 5668 C CB . ALA A 694 ? 0.1836 0.1896 0.2022 -0.0011 -0.0160 -0.0173 735 ALA A CB 5669 N N . ALA A 695 ? 0.1794 0.1806 0.1964 0.0014 -0.0228 -0.0176 736 ALA A N 5670 C CA . ALA A 695 ? 0.1874 0.1863 0.2067 0.0033 -0.0273 -0.0192 736 ALA A CA 5671 C C . ALA A 695 ? 0.1877 0.1846 0.1983 0.0060 -0.0294 -0.0190 736 ALA A C 5672 O O . ALA A 695 ? 0.2001 0.1953 0.2093 0.0092 -0.0334 -0.0210 736 ALA A O 5673 C CB . ALA A 695 ? 0.2013 0.1996 0.2262 0.0010 -0.0267 -0.0182 736 ALA A CB 5674 N N . PHE A 696 ? 0.1889 0.1860 0.1935 0.0050 -0.0267 -0.0165 737 PHE A N 5675 C CA . PHE A 696 ? 0.1865 0.1818 0.1833 0.0074 -0.0281 -0.0159 737 PHE A CA 5676 C C . PHE A 696 ? 0.1831 0.1784 0.1759 0.0102 -0.0290 -0.0171 737 PHE A C 5677 O O . PHE A 696 ? 0.1931 0.1864 0.1825 0.0136 -0.0321 -0.0182 737 PHE A O 5678 C CB . PHE A 696 ? 0.1839 0.1797 0.1756 0.0057 -0.0250 -0.0132 737 PHE A CB 5679 C CG . PHE A 696 ? 0.1991 0.1939 0.1834 0.0081 -0.0256 -0.0126 737 PHE A CG 5680 C CD1 . PHE A 696 ? 0.2304 0.2227 0.2121 0.0107 -0.0287 -0.0131 737 PHE A CD1 5681 C CD2 . PHE A 696 ? 0.2204 0.2166 0.2008 0.0083 -0.0233 -0.0118 737 PHE A CD2 5682 C CE1 . PHE A 696 ? 0.2638 0.2551 0.2388 0.0133 -0.0289 -0.0125 737 PHE A CE1 5683 C CE2 . PHE A 696 ? 0.2127 0.2079 0.1868 0.0107 -0.0236 -0.0111 737 PHE A CE2 5684 C CZ . PHE A 696 ? 0.2312 0.2241 0.2029 0.0132 -0.0263 -0.0114 737 PHE A CZ 5685 N N . THR A 697 ? 0.1804 0.1779 0.1738 0.0092 -0.0265 -0.0169 738 THR A N 5686 C CA . THR A 697 ? 0.1775 0.1748 0.1669 0.0119 -0.0269 -0.0175 738 THR A CA 5687 C C . THR A 697 ? 0.2015 0.1976 0.1936 0.0147 -0.0308 -0.0202 738 THR A C 5688 O O . THR A 697 ? 0.2028 0.1970 0.1899 0.0182 -0.0328 -0.0209 738 THR A O 5689 C CB . THR A 697 ? 0.1840 0.1838 0.1739 0.0101 -0.0235 -0.0169 738 THR A CB 5690 O OG1 . THR A 697 ? 0.1816 0.1824 0.1689 0.0076 -0.0202 -0.0147 738 THR A OG1 5691 C CG2 . THR A 697 ? 0.1899 0.1892 0.1756 0.0130 -0.0238 -0.0174 738 THR A CG2 5692 N N . VAL A 698 ? 0.1922 0.1890 0.1921 0.0134 -0.0320 -0.0219 739 VAL A N 5693 C CA . VAL A 698 ? 0.2018 0.1973 0.2048 0.0163 -0.0364 -0.0248 739 VAL A CA 5694 C C . VAL A 698 ? 0.2040 0.1963 0.2036 0.0193 -0.0404 -0.0257 739 VAL A C 5695 O O . VAL A 698 ? 0.2149 0.2052 0.2110 0.0232 -0.0435 -0.0274 739 VAL A O 5696 C CB . VAL A 698 ? 0.2071 0.2042 0.2204 0.0141 -0.0369 -0.0263 739 VAL A CB 5697 C CG1 . VAL A 698 ? 0.2224 0.2178 0.2397 0.0171 -0.0422 -0.0297 739 VAL A CG1 5698 C CG2 . VAL A 698 ? 0.1861 0.1860 0.2018 0.0120 -0.0332 -0.0257 739 VAL A CG2 5699 N N . GLN A 699 ? 0.2115 0.2031 0.2119 0.0176 -0.0402 -0.0247 740 GLN A N 5700 C CA . GLN A 699 ? 0.2168 0.2053 0.2139 0.0204 -0.0439 -0.0256 740 GLN A CA 5701 C C . GLN A 699 ? 0.2057 0.1925 0.1926 0.0235 -0.0434 -0.0244 740 GLN A C 5702 O O . GLN A 699 ? 0.2199 0.2041 0.2028 0.0276 -0.0467 -0.0260 740 GLN A O 5703 C CB . GLN A 699 ? 0.2271 0.2153 0.2268 0.0179 -0.0433 -0.0243 740 GLN A CB 5704 C CG . GLN A 699 ? 0.2298 0.2147 0.2262 0.0207 -0.0470 -0.0253 740 GLN A CG 5705 C CD . GLN A 699 ? 0.2403 0.2234 0.2421 0.0228 -0.0522 -0.0288 740 GLN A CD 5706 O OE1 . GLN A 699 ? 0.2477 0.2322 0.2581 0.0211 -0.0529 -0.0303 740 GLN A OE1 5707 N NE2 . GLN A 699 ? 0.2486 0.2283 0.2455 0.0267 -0.0561 -0.0304 740 GLN A NE2 5708 N N . ALA A 700 ? 0.1993 0.1878 0.1825 0.0218 -0.0392 -0.0218 741 ALA A N 5709 C CA . ALA A 700 ? 0.2124 0.1997 0.1872 0.0245 -0.0382 -0.0204 741 ALA A CA 5710 C C . ALA A 700 ? 0.2104 0.1967 0.1823 0.0281 -0.0394 -0.0217 741 ALA A C 5711 O O . ALA A 700 ? 0.2255 0.2091 0.1911 0.0321 -0.0409 -0.0219 741 ALA A O 5712 C CB . ALA A 700 ? 0.2104 0.1999 0.1833 0.0217 -0.0336 -0.0176 741 ALA A CB 5713 N N . ALA A 701 ? 0.2040 0.1921 0.1802 0.0269 -0.0388 -0.0226 742 ALA A N 5714 C CA . ALA A 701 ? 0.2040 0.1911 0.1776 0.0304 -0.0401 -0.0239 742 ALA A CA 5715 C C . ALA A 701 ? 0.2077 0.1917 0.1811 0.0343 -0.0454 -0.0267 742 ALA A C 5716 O O . ALA A 701 ? 0.2202 0.2015 0.1872 0.0387 -0.0470 -0.0272 742 ALA A O 5717 C CB . ALA A 701 ? 0.2049 0.1947 0.1842 0.0282 -0.0386 -0.0245 742 ALA A CB 5718 N N . ALA A 702 ? 0.1907 0.1748 0.1710 0.0327 -0.0482 -0.0286 743 ALA A N 5719 C CA . ALA A 702 ? 0.2300 0.2110 0.2103 0.0365 -0.0538 -0.0317 743 ALA A CA 5720 C C . ALA A 702 ? 0.2242 0.2018 0.1959 0.0402 -0.0550 -0.0311 743 ALA A C 5721 O O . ALA A 702 ? 0.2377 0.2120 0.2039 0.0452 -0.0584 -0.0328 743 ALA A O 5722 C CB . ALA A 702 ? 0.2316 0.2134 0.2215 0.0339 -0.0562 -0.0334 743 ALA A CB 5723 N N . GLU A 703 ? 0.2218 0.1999 0.1915 0.0380 -0.0523 -0.0287 744 GLU A N 5724 C CA . GLU A 703 ? 0.2389 0.2138 0.2012 0.0413 -0.0533 -0.0281 744 GLU A CA 5725 C C . GLU A 703 ? 0.2434 0.2167 0.1968 0.0451 -0.0517 -0.0268 744 GLU A C 5726 O O . GLU A 703 ? 0.2556 0.2255 0.2022 0.0493 -0.0533 -0.0270 744 GLU A O 5727 C CB . GLU A 703 ? 0.2551 0.2311 0.2182 0.0379 -0.0509 -0.0258 744 GLU A CB 5728 C CG . GLU A 703 ? 0.2533 0.2297 0.2246 0.0352 -0.0534 -0.0275 744 GLU A CG 5729 C CD . GLU A 703 ? 0.3385 0.3155 0.3106 0.0323 -0.0514 -0.0253 744 GLU A CD 5730 O OE1 . GLU A 703 ? 0.3316 0.3094 0.2988 0.0316 -0.0478 -0.0226 744 GLU A OE1 5731 O OE2 . GLU A 703 ? 0.3372 0.3140 0.3156 0.0304 -0.0533 -0.0264 744 GLU A OE2 5732 N N . THR A 704 ? 0.2338 0.2091 0.1869 0.0442 -0.0484 -0.0255 745 THR A N 5733 C CA . THR A 704 ? 0.2337 0.2070 0.1788 0.0482 -0.0469 -0.0242 745 THR A CA 5734 C C . THR A 704 ? 0.2482 0.2179 0.1894 0.0537 -0.0512 -0.0269 745 THR A C 5735 O O . THR A 704 ? 0.2592 0.2262 0.1926 0.0581 -0.0505 -0.0260 745 THR A O 5736 C CB . THR A 704 ? 0.2289 0.2049 0.1746 0.0463 -0.0424 -0.0222 745 THR A CB 5737 O OG1 . THR A 704 ? 0.2169 0.1941 0.1672 0.0459 -0.0439 -0.0241 745 THR A OG1 5738 C CG2 . THR A 704 ? 0.2172 0.1969 0.1668 0.0409 -0.0385 -0.0199 745 THR A CG2 5739 N N . LEU A 705 ? 0.2439 0.2136 0.1910 0.0534 -0.0555 -0.0301 746 LEU A N 5740 C CA . LEU A 705 ? 0.2567 0.2229 0.2008 0.0587 -0.0605 -0.0331 746 LEU A CA 5741 C C . LEU A 705 ? 0.2639 0.2265 0.2056 0.0619 -0.0652 -0.0354 746 LEU A C 5742 O O . LEU A 705 ? 0.2808 0.2397 0.2186 0.0670 -0.0699 -0.0382 746 LEU A O 5743 C CB . LEU A 705 ? 0.2527 0.2211 0.2056 0.0568 -0.0629 -0.0356 746 LEU A CB 5744 C CG . LEU A 705 ? 0.2533 0.2250 0.2087 0.0540 -0.0586 -0.0338 746 LEU A CG 5745 C CD1 . LEU A 705 ? 0.2432 0.2169 0.2081 0.0522 -0.0613 -0.0366 746 LEU A CD1 5746 C CD2 . LEU A 705 ? 0.2705 0.2400 0.2171 0.0584 -0.0570 -0.0325 746 LEU A CD2 5747 N N . SER A 706 ? 0.2783 0.2418 0.2224 0.0590 -0.0645 -0.0345 747 SER A N 5748 C CA . SER A 706 ? 0.2817 0.2414 0.2228 0.0621 -0.0687 -0.0365 747 SER A CA 5749 C C . SER A 706 ? 0.3061 0.2617 0.2352 0.0679 -0.0682 -0.0355 747 SER A C 5750 O O . SER A 706 ? 0.2977 0.2538 0.2215 0.0686 -0.0636 -0.0325 747 SER A O 5751 C CB . SER A 706 ? 0.2962 0.2578 0.2414 0.0577 -0.0668 -0.0349 747 SER A CB 5752 O OG . SER A 706 ? 0.3151 0.2798 0.2710 0.0529 -0.0674 -0.0359 747 SER A OG 5753 N N . GLU A 707 ? 0.3018 0.2531 0.2263 0.0725 -0.0728 -0.0379 748 GLU A N 5754 C CA . GLU A 707 ? 0.3376 0.2850 0.2506 0.0778 -0.0716 -0.0366 748 GLU A CA 5755 C C . GLU A 707 ? 0.3062 0.2556 0.2176 0.0749 -0.0656 -0.0324 748 GLU A C 5756 O O . GLU A 707 ? 0.3192 0.2716 0.2372 0.0699 -0.0644 -0.0315 748 GLU A O 5757 C CB . GLU A 707 ? 0.3482 0.2908 0.2571 0.0824 -0.0773 -0.0398 748 GLU A CB 5758 C CG . GLU A 707 ? 0.4161 0.3567 0.3269 0.0855 -0.0836 -0.0442 748 GLU A CG 5759 C CD . GLU A 707 ? 0.5571 0.4920 0.4613 0.0918 -0.0895 -0.0477 748 GLU A CD 5760 O OE1 . GLU A 707 ? 0.6016 0.5361 0.5115 0.0905 -0.0935 -0.0503 748 GLU A OE1 5761 O OE2 . GLU A 707 ? 0.6183 0.5492 0.5121 0.0980 -0.0901 -0.0479 748 GLU A OE2 5762 N N . VAL A 708 ? 0.3161 0.2640 0.2192 0.0781 -0.0618 -0.0297 749 VAL A N 5763 C CA . VAL A 708 ? 0.3133 0.2640 0.2164 0.0749 -0.0556 -0.0256 749 VAL A CA 5764 C C . VAL A 708 ? 0.3303 0.2797 0.2308 0.0754 -0.0552 -0.0247 749 VAL A C 5765 O O . VAL A 708 ? 0.3248 0.2766 0.2269 0.0722 -0.0511 -0.0218 749 VAL A O 5766 C CB . VAL A 708 ? 0.3037 0.2535 0.2001 0.0779 -0.0512 -0.0228 749 VAL A CB 5767 C CG1 . VAL A 708 ? 0.3267 0.2781 0.2261 0.0771 -0.0514 -0.0235 749 VAL A CG1 5768 C CG2 . VAL A 708 ? 0.3176 0.2614 0.2025 0.0857 -0.0525 -0.0232 749 VAL A CG2 5769 N N . ALA A 709 ? 0.3375 0.2826 0.2336 0.0798 -0.0598 -0.0274 750 ALA A N 5770 C CA . ALA A 709 ? 0.3689 0.3122 0.2621 0.0809 -0.0598 -0.0269 750 ALA A CA 5771 C C . ALA A 709 ? 0.3905 0.3292 0.2804 0.0856 -0.0662 -0.0309 750 ALA A C 5772 O O . ALA A 709 ? 0.4335 0.3698 0.3205 0.0874 -0.0674 -0.0313 750 ALA A O 5773 C CB . ALA A 709 ? 0.3714 0.3131 0.2563 0.0843 -0.0550 -0.0236 750 ALA A CB 5774 O OXT . ALA A 709 ? 0.4053 0.3422 0.2949 0.0881 -0.0702 -0.0339 750 ALA A OXT # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ARG 1 42 ? ? ? A . n A 1 2 SER 2 43 ? ? ? A . n A 1 3 LYS 3 44 ? ? ? A . n A 1 4 SER 4 45 ? ? ? A . n A 1 5 SER 5 46 ? ? ? A . n A 1 6 ASN 6 47 ? ? ? A . n A 1 7 GLU 7 48 ? ? ? A . n A 1 8 ALA 8 49 ? ? ? A . n A 1 9 THR 9 50 ? ? ? A . n A 1 10 ASN 10 51 ? ? ? A . n A 1 11 ILE 11 52 ? ? ? A . n A 1 12 THR 12 53 ? ? ? A . n A 1 13 PRO 13 54 ? ? ? A . n A 1 14 LYS 14 55 55 LYS LYS A . n A 1 15 HIS 15 56 56 HIS HIS A . n A 1 16 ASN 16 57 57 ASN ASN A . n A 1 17 MET 17 58 58 MET MET A . n A 1 18 LYS 18 59 59 LYS LYS A . n A 1 19 ALA 19 60 60 ALA ALA A . n A 1 20 PHE 20 61 61 PHE PHE A . n A 1 21 LEU 21 62 62 LEU LEU A . n A 1 22 ASP 22 63 63 ASP ASP A . n A 1 23 GLU 23 64 64 GLU GLU A . n A 1 24 LEU 24 65 65 LEU LEU A . n A 1 25 LYS 25 66 66 LYS LYS A . n A 1 26 ALA 26 67 67 ALA ALA A . n A 1 27 GLU 27 68 68 GLU GLU A . n A 1 28 ASN 28 69 69 ASN ASN A . n A 1 29 ILE 29 70 70 ILE ILE A . n A 1 30 LYS 30 71 71 LYS LYS A . n A 1 31 LYS 31 72 72 LYS LYS A . n A 1 32 PHE 32 73 73 PHE PHE A . n A 1 33 LEU 33 74 74 LEU LEU A . n A 1 34 TYR 34 75 75 TYR TYR A . n A 1 35 ASN 35 76 76 ASN ASN A . n A 1 36 PHE 36 77 77 PHE PHE A . n A 1 37 THR 37 78 78 THR THR A . n A 1 38 GLN 38 79 79 GLN GLN A . n A 1 39 ILE 39 80 80 ILE ILE A . n A 1 40 PRO 40 81 81 PRO PRO A . n A 1 41 HIS 41 82 82 HIS HIS A . n A 1 42 LEU 42 83 83 LEU LEU A . n A 1 43 ALA 43 84 84 ALA ALA A . n A 1 44 GLY 44 85 85 GLY GLY A . n A 1 45 THR 45 86 86 THR THR A . n A 1 46 GLU 46 87 87 GLU GLU A . n A 1 47 GLN 47 88 88 GLN GLN A . n A 1 48 ASN 48 89 89 ASN ASN A . n A 1 49 PHE 49 90 90 PHE PHE A . n A 1 50 GLN 50 91 91 GLN GLN A . n A 1 51 LEU 51 92 92 LEU LEU A . n A 1 52 ALA 52 93 93 ALA ALA A . n A 1 53 LYS 53 94 94 LYS LYS A . n A 1 54 GLN 54 95 95 GLN GLN A . n A 1 55 ILE 55 96 96 ILE ILE A . n A 1 56 GLN 56 97 97 GLN GLN A . n A 1 57 SER 57 98 98 SER SER A . n A 1 58 GLN 58 99 99 GLN GLN A . n A 1 59 TRP 59 100 100 TRP TRP A . n A 1 60 LYS 60 101 101 LYS LYS A . n A 1 61 GLU 61 102 102 GLU GLU A . n A 1 62 PHE 62 103 103 PHE PHE A . n A 1 63 GLY 63 104 104 GLY GLY A . n A 1 64 LEU 64 105 105 LEU LEU A . n A 1 65 ASP 65 106 106 ASP ASP A . n A 1 66 SER 66 107 107 SER SER A . n A 1 67 VAL 67 108 108 VAL VAL A . n A 1 68 GLU 68 109 109 GLU GLU A . n A 1 69 LEU 69 110 110 LEU LEU A . n A 1 70 ALA 70 111 111 ALA ALA A . n A 1 71 HIS 71 112 112 HIS HIS A . n A 1 72 TYR 72 113 113 TYR TYR A . n A 1 73 ASP 73 114 114 ASP ASP A . n A 1 74 VAL 74 115 115 VAL VAL A . n A 1 75 LEU 75 116 116 LEU LEU A . n A 1 76 LEU 76 117 117 LEU LEU A . n A 1 77 SER 77 118 118 SER SER A . n A 1 78 TYR 78 119 119 TYR TYR A . n A 1 79 PRO 79 120 120 PRO PRO A . n A 1 80 ASN 80 121 121 ASN ASN A . n A 1 81 LYS 81 122 122 LYS LYS A . n A 1 82 THR 82 123 123 THR THR A . n A 1 83 HIS 83 124 124 HIS HIS A . n A 1 84 PRO 84 125 125 PRO PRO A . n A 1 85 ASN 85 126 126 ASN ASN A . n A 1 86 TYR 86 127 127 TYR TYR A . n A 1 87 ILE 87 128 128 ILE ILE A . n A 1 88 SER 88 129 129 SER SER A . n A 1 89 ILE 89 130 130 ILE ILE A . n A 1 90 ILE 90 131 131 ILE ILE A . n A 1 91 ASN 91 132 132 ASN ASN A . n A 1 92 GLU 92 133 133 GLU GLU A . n A 1 93 ASP 93 134 134 ASP ASP A . n A 1 94 GLY 94 135 135 GLY GLY A . n A 1 95 ASN 95 136 136 ASN ASN A . n A 1 96 GLU 96 137 137 GLU GLU A . n A 1 97 ILE 97 138 138 ILE ILE A . n A 1 98 PHE 98 139 139 PHE PHE A . n A 1 99 ASN 99 140 140 ASN ASN A . n A 1 100 THR 100 141 141 THR THR A . n A 1 101 SER 101 142 142 SER SER A . n A 1 102 LEU 102 143 143 LEU LEU A . n A 1 103 PHE 103 144 144 PHE PHE A . n A 1 104 GLU 104 145 145 GLU GLU A . n A 1 105 PRO 105 146 146 PRO PRO A . n A 1 106 PRO 106 147 147 PRO PRO A . n A 1 107 PRO 107 148 148 PRO PRO A . n A 1 108 PRO 108 149 149 PRO PRO A . n A 1 109 GLY 109 150 150 GLY GLY A . n A 1 110 TYR 110 151 151 TYR TYR A . n A 1 111 GLU 111 152 152 GLU GLU A . n A 1 112 ASN 112 153 153 ASN ASN A . n A 1 113 VAL 113 154 154 VAL VAL A . n A 1 114 SER 114 155 155 SER SER A . n A 1 115 ASP 115 156 156 ASP ASP A . n A 1 116 ILE 116 157 157 ILE ILE A . n A 1 117 VAL 117 158 158 VAL VAL A . n A 1 118 PRO 118 159 159 PRO PRO A . n A 1 119 PRO 119 160 160 PRO PRO A . n A 1 120 PHE 120 161 161 PHE PHE A . n A 1 121 SER 121 162 162 SER SER A . n A 1 122 ALA 122 163 163 ALA ALA A . n A 1 123 PHE 123 164 164 PHE PHE A . n A 1 124 SER 124 165 165 SER SER A . n A 1 125 PRO 125 166 166 PRO PRO A . n A 1 126 GLN 126 167 167 GLN GLN A . n A 1 127 GLY 127 168 168 GLY GLY A . n A 1 128 MET 128 169 169 MET MET A . n A 1 129 PRO 129 170 170 PRO PRO A . n A 1 130 GLU 130 171 171 GLU GLU A . n A 1 131 GLY 131 172 172 GLY GLY A . n A 1 132 ASP 132 173 173 ASP ASP A . n A 1 133 LEU 133 174 174 LEU LEU A . n A 1 134 VAL 134 175 175 VAL VAL A . n A 1 135 TYR 135 176 176 TYR TYR A . n A 1 136 VAL 136 177 177 VAL VAL A . n A 1 137 ASN 137 178 178 ASN ASN A . n A 1 138 TYR 138 179 179 TYR TYR A . n A 1 139 ALA 139 180 180 ALA ALA A . n A 1 140 ARG 140 181 181 ARG ARG A . n A 1 141 THR 141 182 182 THR THR A . n A 1 142 GLU 142 183 183 GLU GLU A . n A 1 143 ASP 143 184 184 ASP ASP A . n A 1 144 PHE 144 185 185 PHE PHE A . n A 1 145 PHE 145 186 186 PHE PHE A . n A 1 146 LYS 146 187 187 LYS LYS A . n A 1 147 LEU 147 188 188 LEU LEU A . n A 1 148 GLU 148 189 189 GLU GLU A . n A 1 149 ARG 149 190 190 ARG ARG A . n A 1 150 ASP 150 191 191 ASP ASP A . n A 1 151 MET 151 192 192 MET MET A . n A 1 152 LYS 152 193 193 LYS LYS A . n A 1 153 ILE 153 194 194 ILE ILE A . n A 1 154 ASN 154 195 195 ASN ASN A . n A 1 155 CYS 155 196 196 CYS CYS A . n A 1 156 SER 156 197 197 SER SER A . n A 1 157 GLY 157 198 198 GLY GLY A . n A 1 158 LYS 158 199 199 LYS LYS A . n A 1 159 ILE 159 200 200 ILE ILE A . n A 1 160 VAL 160 201 201 VAL VAL A . n A 1 161 ILE 161 202 202 ILE ILE A . n A 1 162 ALA 162 203 203 ALA ALA A . n A 1 163 ARG 163 204 204 ARG ARG A . n A 1 164 TYR 164 205 205 TYR TYR A . n A 1 165 GLY 165 206 206 GLY GLY A . n A 1 166 LYS 166 207 207 LYS LYS A . n A 1 167 VAL 167 208 208 VAL VAL A . n A 1 168 PHE 168 209 209 PHE PHE A . n A 1 169 ARG 169 210 210 ARG ARG A . n A 1 170 GLY 170 211 211 GLY GLY A . n A 1 171 ASN 171 212 212 ASN ASN A . n A 1 172 LYS 172 213 213 LYS LYS A . n A 1 173 VAL 173 214 214 VAL VAL A . n A 1 174 LYS 174 215 215 LYS LYS A . n A 1 175 ASN 175 216 216 ASN ASN A . n A 1 176 ALA 176 217 217 ALA ALA A . n A 1 177 GLN 177 218 218 GLN GLN A . n A 1 178 LEU 178 219 219 LEU LEU A . n A 1 179 ALA 179 220 220 ALA ALA A . n A 1 180 GLY 180 221 221 GLY GLY A . n A 1 181 ALA 181 222 222 ALA ALA A . n A 1 182 LYS 182 223 223 LYS LYS A . n A 1 183 GLY 183 224 224 GLY GLY A . n A 1 184 VAL 184 225 225 VAL VAL A . n A 1 185 ILE 185 226 226 ILE ILE A . n A 1 186 LEU 186 227 227 LEU LEU A . n A 1 187 TYR 187 228 228 TYR TYR A . n A 1 188 SER 188 229 229 SER SER A . n A 1 189 ASP 189 230 230 ASP ASP A . n A 1 190 PRO 190 231 231 PRO PRO A . n A 1 191 ALA 191 232 232 ALA ALA A . n A 1 192 ASP 192 233 233 ASP ASP A . n A 1 193 TYR 193 234 234 TYR TYR A . n A 1 194 PHE 194 235 235 PHE PHE A . n A 1 195 ALA 195 236 236 ALA ALA A . n A 1 196 PRO 196 237 237 PRO PRO A . n A 1 197 GLY 197 238 238 GLY GLY A . n A 1 198 VAL 198 239 239 VAL VAL A . n A 1 199 LYS 199 240 240 LYS LYS A . n A 1 200 SER 200 241 241 SER SER A . n A 1 201 TYR 201 242 242 TYR TYR A . n A 1 202 PRO 202 243 243 PRO PRO A . n A 1 203 ASP 203 244 244 ASP ASP A . n A 1 204 GLY 204 245 245 GLY GLY A . n A 1 205 TRP 205 246 246 TRP TRP A . n A 1 206 ASN 206 247 247 ASN ASN A . n A 1 207 LEU 207 248 248 LEU LEU A . n A 1 208 PRO 208 249 249 PRO PRO A . n A 1 209 GLY 209 250 250 GLY GLY A . n A 1 210 GLY 210 251 251 GLY GLY A . n A 1 211 GLY 211 252 252 GLY GLY A . n A 1 212 VAL 212 253 253 VAL VAL A . n A 1 213 GLN 213 254 254 GLN GLN A . n A 1 214 ARG 214 255 255 ARG ARG A . n A 1 215 GLY 215 256 256 GLY GLY A . n A 1 216 ASN 216 257 257 ASN ASN A . n A 1 217 ILE 217 258 258 ILE ILE A . n A 1 218 LEU 218 259 259 LEU LEU A . n A 1 219 ASN 219 260 260 ASN ASN A . n A 1 220 LEU 220 261 261 LEU LEU A . n A 1 221 ASN 221 262 262 ASN ASN A . n A 1 222 GLY 222 263 263 GLY GLY A . n A 1 223 ALA 223 264 264 ALA ALA A . n A 1 224 GLY 224 265 265 GLY GLY A . n A 1 225 ASP 225 266 266 ASP ASP A . n A 1 226 PRO 226 267 267 PRO PRO A . n A 1 227 LEU 227 268 268 LEU LEU A . n A 1 228 THR 228 269 269 THR THR A . n A 1 229 PRO 229 270 270 PRO PRO A . n A 1 230 GLY 230 271 271 GLY GLY A . n A 1 231 TYR 231 272 272 TYR TYR A . n A 1 232 PRO 232 273 273 PRO PRO A . n A 1 233 ALA 233 274 274 ALA ALA A . n A 1 234 ASN 234 275 275 ASN ASN A . n A 1 235 GLU 235 276 276 GLU GLU A . n A 1 236 TYR 236 277 277 TYR TYR A . n A 1 237 ALA 237 278 278 ALA ALA A . n A 1 238 TYR 238 279 279 TYR TYR A . n A 1 239 ARG 239 280 280 ARG ARG A . n A 1 240 ARG 240 281 281 ARG ARG A . n A 1 241 GLY 241 282 282 GLY GLY A . n A 1 242 ILE 242 283 283 ILE ILE A . n A 1 243 ALA 243 284 284 ALA ALA A . n A 1 244 GLU 244 285 285 GLU GLU A . n A 1 245 ALA 245 286 286 ALA ALA A . n A 1 246 VAL 246 287 287 VAL VAL A . n A 1 247 GLY 247 288 288 GLY GLY A . n A 1 248 LEU 248 289 289 LEU LEU A . n A 1 249 PRO 249 290 290 PRO PRO A . n A 1 250 SER 250 291 291 SER SER A . n A 1 251 ILE 251 292 292 ILE ILE A . n A 1 252 PRO 252 293 293 PRO PRO A . n A 1 253 VAL 253 294 294 VAL VAL A . n A 1 254 HIS 254 295 295 HIS HIS A . n A 1 255 PRO 255 296 296 PRO PRO A . n A 1 256 ILE 256 297 297 ILE ILE A . n A 1 257 GLY 257 298 298 GLY GLY A . n A 1 258 TYR 258 299 299 TYR TYR A . n A 1 259 TYR 259 300 300 TYR TYR A . n A 1 260 ASP 260 301 301 ASP ASP A . n A 1 261 ALA 261 302 302 ALA ALA A . n A 1 262 GLN 262 303 303 GLN GLN A . n A 1 263 LYS 263 304 304 LYS LYS A . n A 1 264 LEU 264 305 305 LEU LEU A . n A 1 265 LEU 265 306 306 LEU LEU A . n A 1 266 GLU 266 307 307 GLU GLU A . n A 1 267 LYS 267 308 308 LYS LYS A . n A 1 268 MET 268 309 309 MET MET A . n A 1 269 GLY 269 310 310 GLY GLY A . n A 1 270 GLY 270 311 311 GLY GLY A . n A 1 271 SER 271 312 312 SER SER A . n A 1 272 ALA 272 313 313 ALA ALA A . n A 1 273 PRO 273 314 314 PRO PRO A . n A 1 274 PRO 274 315 315 PRO PRO A . n A 1 275 ASP 275 316 316 ASP ASP A . n A 1 276 SER 276 317 317 SER SER A . n A 1 277 SER 277 318 318 SER SER A . n A 1 278 TRP 278 319 319 TRP TRP A . n A 1 279 ARG 279 320 320 ARG ARG A . n A 1 280 GLY 280 321 321 GLY GLY A . n A 1 281 SER 281 322 322 SER SER A . n A 1 282 LEU 282 323 323 LEU LEU A . n A 1 283 LYS 283 324 324 LYS LYS A . n A 1 284 VAL 284 325 325 VAL VAL A . n A 1 285 PRO 285 326 326 PRO PRO A . n A 1 286 TYR 286 327 327 TYR TYR A . n A 1 287 ASN 287 328 328 ASN ASN A . n A 1 288 VAL 288 329 329 VAL VAL A . n A 1 289 GLY 289 330 330 GLY GLY A . n A 1 290 PRO 290 331 331 PRO PRO A . n A 1 291 GLY 291 332 332 GLY GLY A . n A 1 292 PHE 292 333 333 PHE PHE A . n A 1 293 THR 293 334 334 THR THR A . n A 1 294 GLY 294 335 335 GLY GLY A . n A 1 295 ASN 295 336 336 ASN ASN A . n A 1 296 PHE 296 337 337 PHE PHE A . n A 1 297 SER 297 338 338 SER SER A . n A 1 298 THR 298 339 339 THR THR A . n A 1 299 GLN 299 340 340 GLN GLN A . n A 1 300 LYS 300 341 341 LYS LYS A . n A 1 301 VAL 301 342 342 VAL VAL A . n A 1 302 LYS 302 343 343 LYS LYS A . n A 1 303 MET 303 344 344 MET MET A . n A 1 304 HIS 304 345 345 HIS HIS A . n A 1 305 ILE 305 346 346 ILE ILE A . n A 1 306 HIS 306 347 347 HIS HIS A . n A 1 307 SER 307 348 348 SER SER A . n A 1 308 THR 308 349 349 THR THR A . n A 1 309 ASN 309 350 350 ASN ASN A . n A 1 310 GLU 310 351 351 GLU GLU A . n A 1 311 VAL 311 352 352 VAL VAL A . n A 1 312 THR 312 353 353 THR THR A . n A 1 313 ARG 313 354 354 ARG ARG A . n A 1 314 ILE 314 355 355 ILE ILE A . n A 1 315 TYR 315 356 356 TYR TYR A . n A 1 316 ASN 316 357 357 ASN ASN A . n A 1 317 VAL 317 358 358 VAL VAL A . n A 1 318 ILE 318 359 359 ILE ILE A . n A 1 319 GLY 319 360 360 GLY GLY A . n A 1 320 THR 320 361 361 THR THR A . n A 1 321 LEU 321 362 362 LEU LEU A . n A 1 322 ARG 322 363 363 ARG ARG A . n A 1 323 GLY 323 364 364 GLY GLY A . n A 1 324 ALA 324 365 365 ALA ALA A . n A 1 325 VAL 325 366 366 VAL VAL A . n A 1 326 GLU 326 367 367 GLU GLU A . n A 1 327 PRO 327 368 368 PRO PRO A . n A 1 328 ASP 328 369 369 ASP ASP A . n A 1 329 ARG 329 370 370 ARG ARG A . n A 1 330 TYR 330 371 371 TYR TYR A . n A 1 331 VAL 331 372 372 VAL VAL A . n A 1 332 ILE 332 373 373 ILE ILE A . n A 1 333 LEU 333 374 374 LEU LEU A . n A 1 334 GLY 334 375 375 GLY GLY A . n A 1 335 GLY 335 376 376 GLY GLY A . n A 1 336 HIS 336 377 377 HIS HIS A . n A 1 337 ARG 337 378 378 ARG ARG A . n A 1 338 ASP 338 379 379 ASP ASP A . n A 1 339 SER 339 380 380 SER SER A . n A 1 340 TRP 340 381 381 TRP TRP A . n A 1 341 VAL 341 382 382 VAL VAL A . n A 1 342 PHE 342 383 383 PHE PHE A . n A 1 343 GLY 343 384 384 GLY GLY A . n A 1 344 GLY 344 385 385 GLY GLY A . n A 1 345 ILE 345 386 386 ILE ILE A . n A 1 346 ASP 346 387 387 ASP ASP A . n A 1 347 PRO 347 388 388 PRO PRO A . n A 1 348 GLN 348 389 389 GLN GLN A . n A 1 349 SER 349 390 390 SER SER A . n A 1 350 GLY 350 391 391 GLY GLY A . n A 1 351 ALA 351 392 392 ALA ALA A . n A 1 352 ALA 352 393 393 ALA ALA A . n A 1 353 VAL 353 394 394 VAL VAL A . n A 1 354 VAL 354 395 395 VAL VAL A . n A 1 355 HIS 355 396 396 HIS HIS A . n A 1 356 GLU 356 397 397 GLU GLU A . n A 1 357 ILE 357 398 398 ILE ILE A . n A 1 358 VAL 358 399 399 VAL VAL A . n A 1 359 ARG 359 400 400 ARG ARG A . n A 1 360 SER 360 401 401 SER SER A . n A 1 361 PHE 361 402 402 PHE PHE A . n A 1 362 GLY 362 403 403 GLY GLY A . n A 1 363 THR 363 404 404 THR THR A . n A 1 364 LEU 364 405 405 LEU LEU A . n A 1 365 LYS 365 406 406 LYS LYS A . n A 1 366 LYS 366 407 407 LYS LYS A . n A 1 367 GLU 367 408 408 GLU GLU A . n A 1 368 GLY 368 409 409 GLY GLY A . n A 1 369 TRP 369 410 410 TRP TRP A . n A 1 370 ARG 370 411 411 ARG ARG A . n A 1 371 PRO 371 412 412 PRO PRO A . n A 1 372 ARG 372 413 413 ARG ARG A . n A 1 373 ARG 373 414 414 ARG ARG A . n A 1 374 THR 374 415 415 THR THR A . n A 1 375 ILE 375 416 416 ILE ILE A . n A 1 376 LEU 376 417 417 LEU LEU A . n A 1 377 PHE 377 418 418 PHE PHE A . n A 1 378 ALA 378 419 419 ALA ALA A . n A 1 379 SER 379 420 420 SER SER A . n A 1 380 TRP 380 421 421 TRP TRP A . n A 1 381 ASP 381 422 422 ASP ASP A . n A 1 382 ALA 382 423 423 ALA ALA A . n A 1 383 GLU 383 424 424 GLU GLU A . n A 1 384 GLU 384 425 425 GLU GLU A . n A 1 385 PHE 385 426 426 PHE PHE A . n A 1 386 GLY 386 427 427 GLY GLY A . n A 1 387 LEU 387 428 428 LEU LEU A . n A 1 388 LEU 388 429 429 LEU LEU A . n A 1 389 GLY 389 430 430 GLY GLY A . n A 1 390 SER 390 431 431 SER SER A . n A 1 391 THR 391 432 432 THR THR A . n A 1 392 GLU 392 433 433 GLU GLU A . n A 1 393 TRP 393 434 434 TRP TRP A . n A 1 394 ALA 394 435 435 ALA ALA A . n A 1 395 GLU 395 436 436 GLU GLU A . n A 1 396 GLU 396 437 437 GLU GLU A . n A 1 397 ASN 397 438 438 ASN ASN A . n A 1 398 SER 398 439 439 SER SER A . n A 1 399 ARG 399 440 440 ARG ARG A . n A 1 400 LEU 400 441 441 LEU LEU A . n A 1 401 LEU 401 442 442 LEU LEU A . n A 1 402 GLN 402 443 443 GLN GLN A . n A 1 403 GLU 403 444 444 GLU GLU A . n A 1 404 ARG 404 445 445 ARG ARG A . n A 1 405 GLY 405 446 446 GLY GLY A . n A 1 406 VAL 406 447 447 VAL VAL A . n A 1 407 ALA 407 448 448 ALA ALA A . n A 1 408 TYR 408 449 449 TYR TYR A . n A 1 409 ILE 409 450 450 ILE ILE A . n A 1 410 ASN 410 451 451 ASN ASN A . n A 1 411 ALA 411 452 452 ALA ALA A . n A 1 412 ASP 412 453 453 ASP ASP A . n A 1 413 SER 413 454 454 SER SER A . n A 1 414 SER 414 455 455 SER SER A . n A 1 415 ILE 415 456 456 ILE ILE A . n A 1 416 GLU 416 457 457 GLU GLU A . n A 1 417 GLY 417 458 458 GLY GLY A . n A 1 418 ASN 418 459 459 ASN ASN A . n A 1 419 TYR 419 460 460 TYR TYR A . n A 1 420 THR 420 461 461 THR THR A . n A 1 421 LEU 421 462 462 LEU LEU A . n A 1 422 ARG 422 463 463 ARG ARG A . n A 1 423 VAL 423 464 464 VAL VAL A . n A 1 424 ASP 424 465 465 ASP ASP A . n A 1 425 CYS 425 466 466 CYS CYS A . n A 1 426 THR 426 467 467 THR THR A . n A 1 427 PRO 427 468 468 PRO PRO A . n A 1 428 LEU 428 469 469 LEU LEU A . n A 1 429 MET 429 470 470 MET MET A . n A 1 430 TYR 430 471 471 TYR TYR A . n A 1 431 SER 431 472 472 SER SER A . n A 1 432 LEU 432 473 473 LEU LEU A . n A 1 433 VAL 433 474 474 VAL VAL A . n A 1 434 HIS 434 475 475 HIS HIS A . n A 1 435 ASN 435 476 476 ASN ASN A . n A 1 436 LEU 436 477 477 LEU LEU A . n A 1 437 THR 437 478 478 THR THR A . n A 1 438 LYS 438 479 479 LYS LYS A . n A 1 439 GLU 439 480 480 GLU GLU A . n A 1 440 LEU 440 481 481 LEU LEU A . n A 1 441 LYS 441 482 482 LYS LYS A . n A 1 442 SER 442 483 483 SER SER A . n A 1 443 PRO 443 484 484 PRO PRO A . n A 1 444 ASP 444 485 485 ASP ASP A . n A 1 445 GLU 445 486 486 GLU GLU A . n A 1 446 GLY 446 487 487 GLY GLY A . n A 1 447 PHE 447 488 488 PHE PHE A . n A 1 448 GLU 448 489 489 GLU GLU A . n A 1 449 GLY 449 490 490 GLY GLY A . n A 1 450 LYS 450 491 491 LYS LYS A . n A 1 451 SER 451 492 492 SER SER A . n A 1 452 LEU 452 493 493 LEU LEU A . n A 1 453 TYR 453 494 494 TYR TYR A . n A 1 454 GLU 454 495 495 GLU GLU A . n A 1 455 SER 455 496 496 SER SER A . n A 1 456 TRP 456 497 497 TRP TRP A . n A 1 457 THR 457 498 498 THR THR A . n A 1 458 LYS 458 499 499 LYS LYS A . n A 1 459 LYS 459 500 500 LYS LYS A . n A 1 460 SER 460 501 501 SER SER A . n A 1 461 PRO 461 502 502 PRO PRO A . n A 1 462 SER 462 503 503 SER SER A . n A 1 463 PRO 463 504 504 PRO PRO A . n A 1 464 GLU 464 505 505 GLU GLU A . n A 1 465 PHE 465 506 506 PHE PHE A . n A 1 466 SER 466 507 507 SER SER A . n A 1 467 GLY 467 508 508 GLY GLY A . n A 1 468 MET 468 509 509 MET MET A . n A 1 469 PRO 469 510 510 PRO PRO A . n A 1 470 ARG 470 511 511 ARG ARG A . n A 1 471 ILE 471 512 512 ILE ILE A . n A 1 472 SER 472 513 513 SER SER A . n A 1 473 LYS 473 514 514 LYS LYS A . n A 1 474 LEU 474 515 515 LEU LEU A . n A 1 475 GLY 475 516 516 GLY GLY A . n A 1 476 SER 476 517 517 SER SER A . n A 1 477 GLY 477 518 518 GLY GLY A . n A 1 478 ASN 478 519 519 ASN ASN A . n A 1 479 ASP 479 520 520 ASP ASP A . n A 1 480 PHE 480 521 521 PHE PHE A . n A 1 481 GLU 481 522 522 GLU GLU A . n A 1 482 VAL 482 523 523 VAL VAL A . n A 1 483 PHE 483 524 524 PHE PHE A . n A 1 484 PHE 484 525 525 PHE PHE A . n A 1 485 GLN 485 526 526 GLN GLN A . n A 1 486 ARG 486 527 527 ARG ARG A . n A 1 487 LEU 487 528 528 LEU LEU A . n A 1 488 GLY 488 529 529 GLY GLY A . n A 1 489 ILE 489 530 530 ILE ILE A . n A 1 490 ALA 490 531 531 ALA ALA A . n A 1 491 SER 491 532 532 SER SER A . n A 1 492 GLY 492 533 533 GLY GLY A . n A 1 493 ARG 493 534 534 ARG ARG A . n A 1 494 ALA 494 535 535 ALA ALA A . n A 1 495 ARG 495 536 536 ARG ARG A . n A 1 496 TYR 496 537 537 TYR TYR A . n A 1 497 THR 497 538 538 THR THR A . n A 1 498 LYS 498 539 539 LYS LYS A . n A 1 499 ASN 499 540 540 ASN ASN A . n A 1 500 TRP 500 541 541 TRP TRP A . n A 1 501 GLU 501 542 542 GLU GLU A . n A 1 502 THR 502 543 543 THR THR A . n A 1 503 ASN 503 544 544 ASN ASN A . n A 1 504 LYS 504 545 545 LYS LYS A . n A 1 505 PHE 505 546 546 PHE PHE A . n A 1 506 SER 506 547 547 SER SER A . n A 1 507 GLY 507 548 548 GLY GLY A . n A 1 508 TYR 508 549 549 TYR TYR A . n A 1 509 PRO 509 550 550 PRO PRO A . n A 1 510 LEU 510 551 551 LEU LEU A . n A 1 511 TYR 511 552 552 TYR TYR A . n A 1 512 HIS 512 553 553 HIS HIS A . n A 1 513 SER 513 554 554 SER SER A . n A 1 514 VAL 514 555 555 VAL VAL A . n A 1 515 TYR 515 556 556 TYR TYR A . n A 1 516 GLU 516 557 557 GLU GLU A . n A 1 517 THR 517 558 558 THR THR A . n A 1 518 TYR 518 559 559 TYR TYR A . n A 1 519 GLU 519 560 560 GLU GLU A . n A 1 520 LEU 520 561 561 LEU LEU A . n A 1 521 VAL 521 562 562 VAL VAL A . n A 1 522 GLU 522 563 563 GLU GLU A . n A 1 523 LYS 523 564 564 LYS LYS A . n A 1 524 PHE 524 565 565 PHE PHE A . n A 1 525 TYR 525 566 566 TYR TYR A . n A 1 526 ASP 526 567 567 ASP ASP A . n A 1 527 PRO 527 568 568 PRO PRO A . n A 1 528 MET 528 569 569 MET MET A . n A 1 529 PHE 529 570 570 PHE PHE A . n A 1 530 LYS 530 571 571 LYS LYS A . n A 1 531 TYR 531 572 572 TYR TYR A . n A 1 532 HIS 532 573 573 HIS HIS A . n A 1 533 LEU 533 574 574 LEU LEU A . n A 1 534 THR 534 575 575 THR THR A . n A 1 535 VAL 535 576 576 VAL VAL A . n A 1 536 ALA 536 577 577 ALA ALA A . n A 1 537 GLN 537 578 578 GLN GLN A . n A 1 538 VAL 538 579 579 VAL VAL A . n A 1 539 ARG 539 580 580 ARG ARG A . n A 1 540 GLY 540 581 581 GLY GLY A . n A 1 541 GLY 541 582 582 GLY GLY A . n A 1 542 MET 542 583 583 MET MET A . n A 1 543 VAL 543 584 584 VAL VAL A . n A 1 544 PHE 544 585 585 PHE PHE A . n A 1 545 GLU 545 586 586 GLU GLU A . n A 1 546 LEU 546 587 587 LEU LEU A . n A 1 547 ALA 547 588 588 ALA ALA A . n A 1 548 ASN 548 589 589 ASN ASN A . n A 1 549 SER 549 590 590 SER SER A . n A 1 550 ILE 550 591 591 ILE ILE A . n A 1 551 VAL 551 592 592 VAL VAL A . n A 1 552 GLN 552 593 593 GLN GLN A . n A 1 553 PRO 553 594 594 PRO PRO A . n A 1 554 PHE 554 595 595 PHE PHE A . n A 1 555 ASP 555 596 596 ASP ASP A . n A 1 556 CYS 556 597 597 CYS CYS A . n A 1 557 ARG 557 598 598 ARG ARG A . n A 1 558 ASP 558 599 599 ASP ASP A . n A 1 559 TYR 559 600 600 TYR TYR A . n A 1 560 ALA 560 601 601 ALA ALA A . n A 1 561 VAL 561 602 602 VAL VAL A . n A 1 562 VAL 562 603 603 VAL VAL A . n A 1 563 LEU 563 604 604 LEU LEU A . n A 1 564 ARG 564 605 605 ARG ARG A . n A 1 565 LYS 565 606 606 LYS LYS A . n A 1 566 TYR 566 607 607 TYR TYR A . n A 1 567 ALA 567 608 608 ALA ALA A . n A 1 568 ASP 568 609 609 ASP ASP A . n A 1 569 LYS 569 610 610 LYS LYS A . n A 1 570 ILE 570 611 611 ILE ILE A . n A 1 571 TYR 571 612 612 TYR TYR A . n A 1 572 SER 572 613 613 SER SER A . n A 1 573 ILE 573 614 614 ILE ILE A . n A 1 574 SER 574 615 615 SER SER A . n A 1 575 MET 575 616 616 MET MET A . n A 1 576 LYS 576 617 617 LYS LYS A . n A 1 577 HIS 577 618 618 HIS HIS A . n A 1 578 PRO 578 619 619 PRO PRO A . n A 1 579 GLN 579 620 620 GLN GLN A . n A 1 580 GLU 580 621 621 GLU GLU A . n A 1 581 MET 581 622 622 MET MET A . n A 1 582 LYS 582 623 623 LYS LYS A . n A 1 583 THR 583 624 624 THR THR A . n A 1 584 TYR 584 625 625 TYR TYR A . n A 1 585 SER 585 626 626 SER SER A . n A 1 586 VAL 586 627 627 VAL VAL A . n A 1 587 SER 587 628 628 SER SER A . n A 1 588 PHE 588 629 629 PHE PHE A . n A 1 589 ASP 589 630 630 ASP ASP A . n A 1 590 SER 590 631 631 SER SER A . n A 1 591 LEU 591 632 632 LEU LEU A . n A 1 592 PHE 592 633 633 PHE PHE A . n A 1 593 SER 593 634 634 SER SER A . n A 1 594 ALA 594 635 635 ALA ALA A . n A 1 595 VAL 595 636 636 VAL VAL A . n A 1 596 LYS 596 637 637 LYS LYS A . n A 1 597 ASN 597 638 638 ASN ASN A . n A 1 598 PHE 598 639 639 PHE PHE A . n A 1 599 THR 599 640 640 THR THR A . n A 1 600 GLU 600 641 641 GLU GLU A . n A 1 601 ILE 601 642 642 ILE ILE A . n A 1 602 ALA 602 643 643 ALA ALA A . n A 1 603 SER 603 644 644 SER SER A . n A 1 604 LYS 604 645 645 LYS LYS A . n A 1 605 PHE 605 646 646 PHE PHE A . n A 1 606 SER 606 647 647 SER SER A . n A 1 607 GLU 607 648 648 GLU GLU A . n A 1 608 ARG 608 649 649 ARG ARG A . n A 1 609 LEU 609 650 650 LEU LEU A . n A 1 610 GLN 610 651 651 GLN GLN A . n A 1 611 ASP 611 652 652 ASP ASP A . n A 1 612 PHE 612 653 653 PHE PHE A . n A 1 613 ASP 613 654 ? ? ? A . n A 1 614 LYS 614 655 ? ? ? A . n A 1 615 SER 615 656 656 SER SER A . n A 1 616 ASN 616 657 657 ASN ASN A . n A 1 617 PRO 617 658 658 PRO PRO A . n A 1 618 ILE 618 659 659 ILE ILE A . n A 1 619 VAL 619 660 660 VAL VAL A . n A 1 620 LEU 620 661 661 LEU LEU A . n A 1 621 ARG 621 662 662 ARG ARG A . n A 1 622 MET 622 663 663 MET MET A . n A 1 623 MET 623 664 664 MET MET A . n A 1 624 ASN 624 665 665 ASN ASN A . n A 1 625 ASP 625 666 666 ASP ASP A . n A 1 626 GLN 626 667 667 GLN GLN A . n A 1 627 LEU 627 668 668 LEU LEU A . n A 1 628 MET 628 669 669 MET MET A . n A 1 629 PHE 629 670 670 PHE PHE A . n A 1 630 LEU 630 671 671 LEU LEU A . n A 1 631 GLU 631 672 672 GLU GLU A . n A 1 632 ARG 632 673 673 ARG ARG A . n A 1 633 ALA 633 674 674 ALA ALA A . n A 1 634 PHE 634 675 675 PHE PHE A . n A 1 635 ILE 635 676 676 ILE ILE A . n A 1 636 ASP 636 677 677 ASP ASP A . n A 1 637 PRO 637 678 678 PRO PRO A . n A 1 638 LEU 638 679 679 LEU LEU A . n A 1 639 GLY 639 680 680 GLY GLY A . n A 1 640 LEU 640 681 681 LEU LEU A . n A 1 641 PRO 641 682 682 PRO PRO A . n A 1 642 ASP 642 683 683 ASP ASP A . n A 1 643 ARG 643 684 684 ARG ARG A . n A 1 644 PRO 644 685 685 PRO PRO A . n A 1 645 PHE 645 686 686 PHE PHE A . n A 1 646 TYR 646 687 687 TYR TYR A . n A 1 647 ARG 647 688 688 ARG ARG A . n A 1 648 HIS 648 689 689 HIS HIS A . n A 1 649 VAL 649 690 690 VAL VAL A . n A 1 650 ILE 650 691 691 ILE ILE A . n A 1 651 TYR 651 692 692 TYR TYR A . n A 1 652 ALA 652 693 693 ALA ALA A . n A 1 653 PRO 653 694 694 PRO PRO A . n A 1 654 SER 654 695 695 SER SER A . n A 1 655 SER 655 696 696 SER SER A . n A 1 656 HIS 656 697 697 HIS HIS A . n A 1 657 ASN 657 698 698 ASN ASN A . n A 1 658 LYS 658 699 699 LYS LYS A . n A 1 659 TYR 659 700 700 TYR TYR A . n A 1 660 ALA 660 701 701 ALA ALA A . n A 1 661 GLY 661 702 702 GLY GLY A . n A 1 662 GLU 662 703 703 GLU GLU A . n A 1 663 SER 663 704 704 SER SER A . n A 1 664 PHE 664 705 705 PHE PHE A . n A 1 665 PRO 665 706 706 PRO PRO A . n A 1 666 GLY 666 707 707 GLY GLY A . n A 1 667 ILE 667 708 708 ILE ILE A . n A 1 668 TYR 668 709 709 TYR TYR A . n A 1 669 ASP 669 710 710 ASP ASP A . n A 1 670 ALA 670 711 711 ALA ALA A . n A 1 671 LEU 671 712 712 LEU LEU A . n A 1 672 PHE 672 713 713 PHE PHE A . n A 1 673 ASP 673 714 714 ASP ASP A . n A 1 674 ILE 674 715 715 ILE ILE A . n A 1 675 GLU 675 716 716 GLU GLU A . n A 1 676 SER 676 717 717 SER SER A . n A 1 677 LYS 677 718 718 LYS LYS A . n A 1 678 VAL 678 719 719 VAL VAL A . n A 1 679 ASP 679 720 720 ASP ASP A . n A 1 680 PRO 680 721 721 PRO PRO A . n A 1 681 SER 681 722 722 SER SER A . n A 1 682 LYS 682 723 723 LYS LYS A . n A 1 683 ALA 683 724 724 ALA ALA A . n A 1 684 TRP 684 725 725 TRP TRP A . n A 1 685 GLY 685 726 726 GLY GLY A . n A 1 686 GLU 686 727 727 GLU GLU A . n A 1 687 VAL 687 728 728 VAL VAL A . n A 1 688 LYS 688 729 729 LYS LYS A . n A 1 689 ARG 689 730 730 ARG ARG A . n A 1 690 GLN 690 731 731 GLN GLN A . n A 1 691 ILE 691 732 732 ILE ILE A . n A 1 692 TYR 692 733 733 TYR TYR A . n A 1 693 VAL 693 734 734 VAL VAL A . n A 1 694 ALA 694 735 735 ALA ALA A . n A 1 695 ALA 695 736 736 ALA ALA A . n A 1 696 PHE 696 737 737 PHE PHE A . n A 1 697 THR 697 738 738 THR THR A . n A 1 698 VAL 698 739 739 VAL VAL A . n A 1 699 GLN 699 740 740 GLN GLN A . n A 1 700 ALA 700 741 741 ALA ALA A . n A 1 701 ALA 701 742 742 ALA ALA A . n A 1 702 ALA 702 743 743 ALA ALA A . n A 1 703 GLU 703 744 744 GLU GLU A . n A 1 704 THR 704 745 745 THR THR A . n A 1 705 LEU 705 746 746 LEU LEU A . n A 1 706 SER 706 747 747 SER SER A . n A 1 707 GLU 707 748 748 GLU GLU A . n A 1 708 VAL 708 749 749 VAL VAL A . n A 1 709 ALA 709 750 750 ALA ALA A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 ZN 1 1751 1751 ZN ZN A . C 2 ZN 1 1752 1752 ZN ZN A . D 3 CA 1 1753 1753 CA CA A . E 4 CL 1 1754 1754 CL CL A . F 5 NAG 1 1755 1755 NAG NAG A . G 5 NAG 2 1756 1756 NAG NAG A . H 5 NAG 1 1757 1757 NAG NAG A . I 5 NAG 1 1758 1758 NAG NAG A . J 5 NAG 2 1767 1767 NAG NAG A . K 5 NAG 1 1759 1759 NAG NAG A . L 5 NAG 1 1760 1760 NAG NAG A . M 5 NAG 1 1761 1761 NAG NAG A . N 5 NAG 2 1762 1762 NAG NAG A . O 5 NAG 1 1763 1763 NAG NAG A . P 5 NAG 2 1764 1764 NAG NAG A . Q 6 BMA 3 1765 1765 BMA BMA A . R 7 MAN 4 1766 1766 MAN MAN A . S 8 CI9 1 1768 1768 CI9 CI9 A . T 9 HOH 1 2001 2001 HOH HOH A . T 9 HOH 2 2002 2002 HOH HOH A . T 9 HOH 3 2003 2003 HOH HOH A . T 9 HOH 4 2004 2004 HOH HOH A . T 9 HOH 5 2005 2005 HOH HOH A . T 9 HOH 6 2006 2006 HOH HOH A . T 9 HOH 7 2007 2007 HOH HOH A . T 9 HOH 8 2008 2008 HOH HOH A . T 9 HOH 9 2009 2009 HOH HOH A . T 9 HOH 10 2010 2010 HOH HOH A . T 9 HOH 11 2011 2011 HOH HOH A . T 9 HOH 12 2012 2012 HOH HOH A . T 9 HOH 13 2013 2013 HOH HOH A . T 9 HOH 14 2014 2014 HOH HOH A . T 9 HOH 15 2015 2015 HOH HOH A . T 9 HOH 16 2016 2016 HOH HOH A . T 9 HOH 17 2017 2017 HOH HOH A . T 9 HOH 18 2018 2018 HOH HOH A . T 9 HOH 19 2019 2019 HOH HOH A . T 9 HOH 20 2020 2020 HOH HOH A . T 9 HOH 21 2021 2021 HOH HOH A . T 9 HOH 22 2022 2022 HOH HOH A . T 9 HOH 23 2023 2023 HOH HOH A . T 9 HOH 24 2024 2024 HOH HOH A . T 9 HOH 25 2025 2025 HOH HOH A . T 9 HOH 26 2026 2026 HOH HOH A . T 9 HOH 27 2027 2027 HOH HOH A . T 9 HOH 28 2028 2028 HOH HOH A . T 9 HOH 29 2029 2029 HOH HOH A . T 9 HOH 30 2030 2030 HOH HOH A . T 9 HOH 31 2031 2031 HOH HOH A . T 9 HOH 32 2032 2032 HOH HOH A . T 9 HOH 33 2033 2033 HOH HOH A . T 9 HOH 34 2034 2034 HOH HOH A . T 9 HOH 35 2035 2035 HOH HOH A . T 9 HOH 36 2036 2036 HOH HOH A . T 9 HOH 37 2037 2037 HOH HOH A . T 9 HOH 38 2038 2038 HOH HOH A . T 9 HOH 39 2039 2039 HOH HOH A . T 9 HOH 40 2040 2040 HOH HOH A . T 9 HOH 41 2041 2041 HOH HOH A . T 9 HOH 42 2042 2042 HOH HOH A . T 9 HOH 43 2043 2043 HOH HOH A . T 9 HOH 44 2044 2044 HOH HOH A . T 9 HOH 45 2045 2045 HOH HOH A . T 9 HOH 46 2046 2046 HOH HOH A . T 9 HOH 47 2047 2047 HOH HOH A . T 9 HOH 48 2048 2048 HOH HOH A . T 9 HOH 49 2049 2049 HOH HOH A . T 9 HOH 50 2050 2050 HOH HOH A . T 9 HOH 51 2051 2051 HOH HOH A . T 9 HOH 52 2052 2052 HOH HOH A . T 9 HOH 53 2053 2053 HOH HOH A . T 9 HOH 54 2054 2054 HOH HOH A . T 9 HOH 55 2055 2055 HOH HOH A . T 9 HOH 56 2056 2056 HOH HOH A . T 9 HOH 57 2057 2057 HOH HOH A . T 9 HOH 58 2058 2058 HOH HOH A . T 9 HOH 59 2059 2059 HOH HOH A . T 9 HOH 60 2060 2060 HOH HOH A . T 9 HOH 61 2061 2061 HOH HOH A . T 9 HOH 62 2062 2062 HOH HOH A . T 9 HOH 63 2063 2063 HOH HOH A . T 9 HOH 64 2064 2064 HOH HOH A . T 9 HOH 65 2065 2065 HOH HOH A . T 9 HOH 66 2066 2066 HOH HOH A . T 9 HOH 67 2067 2067 HOH HOH A . T 9 HOH 68 2068 2068 HOH HOH A . T 9 HOH 69 2069 2069 HOH HOH A . T 9 HOH 70 2070 2070 HOH HOH A . T 9 HOH 71 2071 2071 HOH HOH A . T 9 HOH 72 2072 2072 HOH HOH A . T 9 HOH 73 2073 2073 HOH HOH A . T 9 HOH 74 2074 2074 HOH HOH A . T 9 HOH 75 2075 2075 HOH HOH A . T 9 HOH 76 2076 2076 HOH HOH A . T 9 HOH 77 2077 2077 HOH HOH A . T 9 HOH 78 2078 2078 HOH HOH A . T 9 HOH 79 2079 2079 HOH HOH A . T 9 HOH 80 2080 2080 HOH HOH A . T 9 HOH 81 2081 2081 HOH HOH A . T 9 HOH 82 2082 2082 HOH HOH A . T 9 HOH 83 2083 2083 HOH HOH A . T 9 HOH 84 2084 2084 HOH HOH A . T 9 HOH 85 2085 2085 HOH HOH A . T 9 HOH 86 2086 2086 HOH HOH A . T 9 HOH 87 2087 2087 HOH HOH A . T 9 HOH 88 2088 2088 HOH HOH A . T 9 HOH 89 2089 2089 HOH HOH A . T 9 HOH 90 2090 2090 HOH HOH A . T 9 HOH 91 2091 2091 HOH HOH A . T 9 HOH 92 2092 2092 HOH HOH A . T 9 HOH 93 2093 2093 HOH HOH A . T 9 HOH 94 2094 2094 HOH HOH A . T 9 HOH 95 2095 2095 HOH HOH A . T 9 HOH 96 2096 2096 HOH HOH A . T 9 HOH 97 2097 2097 HOH HOH A . T 9 HOH 98 2098 2098 HOH HOH A . T 9 HOH 99 2099 2099 HOH HOH A . T 9 HOH 100 2100 2100 HOH HOH A . T 9 HOH 101 2101 2101 HOH HOH A . T 9 HOH 102 2102 2102 HOH HOH A . T 9 HOH 103 2103 2103 HOH HOH A . T 9 HOH 104 2104 2104 HOH HOH A . T 9 HOH 105 2105 2105 HOH HOH A . T 9 HOH 106 2106 2106 HOH HOH A . T 9 HOH 107 2107 2107 HOH HOH A . T 9 HOH 108 2108 2108 HOH HOH A . T 9 HOH 109 2109 2109 HOH HOH A . T 9 HOH 110 2110 2110 HOH HOH A . T 9 HOH 111 2111 2111 HOH HOH A . T 9 HOH 112 2112 2112 HOH HOH A . T 9 HOH 113 2113 2113 HOH HOH A . T 9 HOH 114 2114 2114 HOH HOH A . T 9 HOH 115 2115 2115 HOH HOH A . T 9 HOH 116 2116 2116 HOH HOH A . T 9 HOH 117 2117 2117 HOH HOH A . T 9 HOH 118 2118 2118 HOH HOH A . T 9 HOH 119 2119 2119 HOH HOH A . T 9 HOH 120 2120 2120 HOH HOH A . T 9 HOH 121 2121 2121 HOH HOH A . T 9 HOH 122 2122 2122 HOH HOH A . T 9 HOH 123 2123 2123 HOH HOH A . T 9 HOH 124 2124 2124 HOH HOH A . T 9 HOH 125 2125 2125 HOH HOH A . T 9 HOH 126 2126 2126 HOH HOH A . T 9 HOH 127 2127 2127 HOH HOH A . T 9 HOH 128 2128 2128 HOH HOH A . T 9 HOH 129 2129 2129 HOH HOH A . T 9 HOH 130 2130 2130 HOH HOH A . T 9 HOH 131 2131 2131 HOH HOH A . T 9 HOH 132 2132 2132 HOH HOH A . T 9 HOH 133 2133 2133 HOH HOH A . T 9 HOH 134 2134 2134 HOH HOH A . T 9 HOH 135 2135 2135 HOH HOH A . T 9 HOH 136 2136 2136 HOH HOH A . T 9 HOH 137 2137 2137 HOH HOH A . T 9 HOH 138 2138 2138 HOH HOH A . T 9 HOH 139 2139 2139 HOH HOH A . T 9 HOH 140 2140 2140 HOH HOH A . T 9 HOH 141 2141 2141 HOH HOH A . T 9 HOH 142 2142 2142 HOH HOH A . T 9 HOH 143 2143 2143 HOH HOH A . T 9 HOH 144 2144 2144 HOH HOH A . T 9 HOH 145 2145 2145 HOH HOH A . T 9 HOH 146 2146 2146 HOH HOH A . T 9 HOH 147 2147 2147 HOH HOH A . T 9 HOH 148 2148 2148 HOH HOH A . T 9 HOH 149 2149 2149 HOH HOH A . T 9 HOH 150 2150 2150 HOH HOH A . T 9 HOH 151 2151 2151 HOH HOH A . T 9 HOH 152 2152 2152 HOH HOH A . T 9 HOH 153 2153 2153 HOH HOH A . T 9 HOH 154 2154 2154 HOH HOH A . T 9 HOH 155 2155 2155 HOH HOH A . T 9 HOH 156 2156 2156 HOH HOH A . T 9 HOH 157 2157 2157 HOH HOH A . T 9 HOH 158 2158 2158 HOH HOH A . T 9 HOH 159 2159 2159 HOH HOH A . T 9 HOH 160 2160 2160 HOH HOH A . T 9 HOH 161 2161 2161 HOH HOH A . T 9 HOH 162 2162 2162 HOH HOH A . T 9 HOH 163 2163 2163 HOH HOH A . T 9 HOH 164 2164 2164 HOH HOH A . T 9 HOH 165 2165 2165 HOH HOH A . T 9 HOH 166 2166 2166 HOH HOH A . T 9 HOH 167 2167 2167 HOH HOH A . T 9 HOH 168 2168 2168 HOH HOH A . T 9 HOH 169 2169 2169 HOH HOH A . T 9 HOH 170 2170 2170 HOH HOH A . T 9 HOH 171 2171 2171 HOH HOH A . T 9 HOH 172 2172 2172 HOH HOH A . T 9 HOH 173 2173 2173 HOH HOH A . T 9 HOH 174 2174 2174 HOH HOH A . T 9 HOH 175 2175 2175 HOH HOH A . T 9 HOH 176 2176 2176 HOH HOH A . T 9 HOH 177 2177 2177 HOH HOH A . T 9 HOH 178 2178 2178 HOH HOH A . T 9 HOH 179 2179 2179 HOH HOH A . T 9 HOH 180 2180 2180 HOH HOH A . T 9 HOH 181 2181 2181 HOH HOH A . T 9 HOH 182 2182 2182 HOH HOH A . T 9 HOH 183 2183 2183 HOH HOH A . T 9 HOH 184 2184 2184 HOH HOH A . T 9 HOH 185 2185 2185 HOH HOH A . T 9 HOH 186 2186 2186 HOH HOH A . T 9 HOH 187 2187 2187 HOH HOH A . T 9 HOH 188 2188 2188 HOH HOH A . T 9 HOH 189 2189 2189 HOH HOH A . T 9 HOH 190 2190 2190 HOH HOH A . T 9 HOH 191 2191 2191 HOH HOH A . T 9 HOH 192 2192 2192 HOH HOH A . T 9 HOH 193 2193 2193 HOH HOH A . T 9 HOH 194 2194 2194 HOH HOH A . T 9 HOH 195 2195 2195 HOH HOH A . T 9 HOH 196 2196 2196 HOH HOH A . T 9 HOH 197 2197 2197 HOH HOH A . T 9 HOH 198 2198 2198 HOH HOH A . T 9 HOH 199 2199 2199 HOH HOH A . T 9 HOH 200 2200 2200 HOH HOH A . T 9 HOH 201 2201 2201 HOH HOH A . T 9 HOH 202 2202 2202 HOH HOH A . T 9 HOH 203 2203 2203 HOH HOH A . T 9 HOH 204 2204 2204 HOH HOH A . T 9 HOH 205 2205 2205 HOH HOH A . T 9 HOH 206 2206 2206 HOH HOH A . T 9 HOH 207 2207 2207 HOH HOH A . T 9 HOH 208 2208 2208 HOH HOH A . T 9 HOH 209 2209 2209 HOH HOH A . T 9 HOH 210 2210 2210 HOH HOH A . T 9 HOH 211 2211 2211 HOH HOH A . T 9 HOH 212 2212 2212 HOH HOH A . T 9 HOH 213 2213 2213 HOH HOH A . T 9 HOH 214 2214 2214 HOH HOH A . T 9 HOH 215 2215 2215 HOH HOH A . T 9 HOH 216 2216 2216 HOH HOH A . T 9 HOH 217 2217 2217 HOH HOH A . T 9 HOH 218 2218 2218 HOH HOH A . T 9 HOH 219 2219 2219 HOH HOH A . T 9 HOH 220 2220 2220 HOH HOH A . T 9 HOH 221 2221 2221 HOH HOH A . T 9 HOH 222 2222 2222 HOH HOH A . T 9 HOH 223 2223 2223 HOH HOH A . T 9 HOH 224 2224 2224 HOH HOH A . T 9 HOH 225 2225 2225 HOH HOH A . T 9 HOH 226 2226 2226 HOH HOH A . T 9 HOH 227 2227 2227 HOH HOH A . T 9 HOH 228 2228 2228 HOH HOH A . T 9 HOH 229 2229 2229 HOH HOH A . T 9 HOH 230 2230 2230 HOH HOH A . T 9 HOH 231 2231 2231 HOH HOH A . T 9 HOH 232 2232 2232 HOH HOH A . T 9 HOH 233 2233 2233 HOH HOH A . T 9 HOH 234 2234 2234 HOH HOH A . T 9 HOH 235 2235 2235 HOH HOH A . T 9 HOH 236 2236 2236 HOH HOH A . T 9 HOH 237 2237 2237 HOH HOH A . T 9 HOH 238 2238 2238 HOH HOH A . T 9 HOH 239 2239 2239 HOH HOH A . T 9 HOH 240 2240 2240 HOH HOH A . T 9 HOH 241 2241 2241 HOH HOH A . T 9 HOH 242 2242 2242 HOH HOH A . T 9 HOH 243 2243 2243 HOH HOH A . T 9 HOH 244 2244 2244 HOH HOH A . T 9 HOH 245 2245 2245 HOH HOH A . T 9 HOH 246 2246 2246 HOH HOH A . T 9 HOH 247 2247 2247 HOH HOH A . T 9 HOH 248 2248 2248 HOH HOH A . T 9 HOH 249 2249 2249 HOH HOH A . T 9 HOH 250 2250 2250 HOH HOH A . T 9 HOH 251 2251 2251 HOH HOH A . T 9 HOH 252 2252 2252 HOH HOH A . T 9 HOH 253 2253 2253 HOH HOH A . T 9 HOH 254 2254 2254 HOH HOH A . T 9 HOH 255 2255 2255 HOH HOH A . T 9 HOH 256 2256 2256 HOH HOH A . T 9 HOH 257 2257 2257 HOH HOH A . T 9 HOH 258 2258 2258 HOH HOH A . T 9 HOH 259 2259 2259 HOH HOH A . T 9 HOH 260 2260 2260 HOH HOH A . T 9 HOH 261 2261 2261 HOH HOH A . T 9 HOH 262 2262 2262 HOH HOH A . T 9 HOH 263 2263 2263 HOH HOH A . T 9 HOH 264 2264 2264 HOH HOH A . T 9 HOH 265 2265 2265 HOH HOH A . T 9 HOH 266 2266 2266 HOH HOH A . T 9 HOH 267 2267 2267 HOH HOH A . T 9 HOH 268 2268 2268 HOH HOH A . T 9 HOH 269 2269 2269 HOH HOH A . T 9 HOH 270 2270 2270 HOH HOH A . T 9 HOH 271 2271 2271 HOH HOH A . T 9 HOH 272 2272 2272 HOH HOH A . T 9 HOH 273 2273 2273 HOH HOH A . T 9 HOH 274 2274 2274 HOH HOH A . T 9 HOH 275 2275 2275 HOH HOH A . T 9 HOH 276 2276 2276 HOH HOH A . T 9 HOH 277 2277 2277 HOH HOH A . T 9 HOH 278 2278 2278 HOH HOH A . T 9 HOH 279 2279 2279 HOH HOH A . T 9 HOH 280 2280 2280 HOH HOH A . T 9 HOH 281 2281 2281 HOH HOH A . T 9 HOH 282 2282 2282 HOH HOH A . T 9 HOH 283 2283 2283 HOH HOH A . T 9 HOH 284 2284 2284 HOH HOH A . T 9 HOH 285 2285 2285 HOH HOH A . T 9 HOH 286 2286 2286 HOH HOH A . T 9 HOH 287 2287 2287 HOH HOH A . T 9 HOH 288 2288 2288 HOH HOH A . T 9 HOH 289 2289 2289 HOH HOH A . T 9 HOH 290 2290 2290 HOH HOH A . T 9 HOH 291 2291 2291 HOH HOH A . T 9 HOH 292 2292 2292 HOH HOH A . T 9 HOH 293 2293 2293 HOH HOH A . T 9 HOH 294 2294 2294 HOH HOH A . T 9 HOH 295 2295 2295 HOH HOH A . T 9 HOH 296 2296 2296 HOH HOH A . T 9 HOH 297 2297 2297 HOH HOH A . T 9 HOH 298 2298 2298 HOH HOH A . T 9 HOH 299 2299 2299 HOH HOH A . T 9 HOH 300 2300 2300 HOH HOH A . T 9 HOH 301 2301 2301 HOH HOH A . T 9 HOH 302 2302 2302 HOH HOH A . T 9 HOH 303 2303 2303 HOH HOH A . T 9 HOH 304 2304 2304 HOH HOH A . T 9 HOH 305 2305 2305 HOH HOH A . T 9 HOH 306 2306 2306 HOH HOH A . T 9 HOH 307 2307 2307 HOH HOH A . T 9 HOH 308 2308 2308 HOH HOH A . T 9 HOH 309 2309 2309 HOH HOH A . T 9 HOH 310 2310 2310 HOH HOH A . T 9 HOH 311 2311 2311 HOH HOH A . T 9 HOH 312 2312 2312 HOH HOH A . T 9 HOH 313 2313 2313 HOH HOH A . T 9 HOH 314 2314 2314 HOH HOH A . T 9 HOH 315 2315 2315 HOH HOH A . T 9 HOH 316 2316 2316 HOH HOH A . T 9 HOH 317 2317 2317 HOH HOH A . T 9 HOH 318 2318 2318 HOH HOH A . T 9 HOH 319 2319 2319 HOH HOH A . T 9 HOH 320 2320 2320 HOH HOH A . T 9 HOH 321 2321 2321 HOH HOH A . T 9 HOH 322 2322 2322 HOH HOH A . T 9 HOH 323 2323 2323 HOH HOH A . T 9 HOH 324 2324 2324 HOH HOH A . T 9 HOH 325 2325 2325 HOH HOH A . T 9 HOH 326 2326 2326 HOH HOH A . T 9 HOH 327 2327 2327 HOH HOH A . T 9 HOH 328 2328 2328 HOH HOH A . T 9 HOH 329 2329 2329 HOH HOH A . T 9 HOH 330 2330 2330 HOH HOH A . T 9 HOH 331 2331 2331 HOH HOH A . T 9 HOH 332 2332 2332 HOH HOH A . T 9 HOH 333 2333 2333 HOH HOH A . T 9 HOH 334 2334 2334 HOH HOH A . T 9 HOH 335 2335 2335 HOH HOH A . T 9 HOH 336 2336 2336 HOH HOH A . T 9 HOH 337 2337 2337 HOH HOH A . T 9 HOH 338 2338 2338 HOH HOH A . T 9 HOH 339 2339 2339 HOH HOH A . T 9 HOH 340 2340 2340 HOH HOH A . T 9 HOH 341 2341 2341 HOH HOH A . T 9 HOH 342 2342 2342 HOH HOH A . T 9 HOH 343 2343 2343 HOH HOH A . T 9 HOH 344 2344 2344 HOH HOH A . T 9 HOH 345 2345 2345 HOH HOH A . T 9 HOH 346 2346 2346 HOH HOH A . T 9 HOH 347 2347 2347 HOH HOH A . T 9 HOH 348 2348 2348 HOH HOH A . T 9 HOH 349 2349 2349 HOH HOH A . T 9 HOH 350 2350 2350 HOH HOH A . T 9 HOH 351 2351 2351 HOH HOH A . T 9 HOH 352 2352 2352 HOH HOH A . T 9 HOH 353 2353 2353 HOH HOH A . T 9 HOH 354 2354 2354 HOH HOH A . T 9 HOH 355 2355 2355 HOH HOH A . T 9 HOH 356 2356 2356 HOH HOH A . T 9 HOH 357 2357 2357 HOH HOH A . T 9 HOH 358 2358 2358 HOH HOH A . T 9 HOH 359 2359 2359 HOH HOH A . T 9 HOH 360 2360 2360 HOH HOH A . T 9 HOH 361 2361 2361 HOH HOH A . T 9 HOH 362 2362 2362 HOH HOH A . T 9 HOH 363 2363 2363 HOH HOH A . T 9 HOH 364 2364 2364 HOH HOH A . T 9 HOH 365 2365 2365 HOH HOH A . T 9 HOH 366 2366 2366 HOH HOH A . T 9 HOH 367 2367 2367 HOH HOH A . T 9 HOH 368 2368 2368 HOH HOH A . T 9 HOH 369 2369 2369 HOH HOH A . T 9 HOH 370 2370 2370 HOH HOH A . T 9 HOH 371 2371 2371 HOH HOH A . T 9 HOH 372 2372 2372 HOH HOH A . T 9 HOH 373 2373 2373 HOH HOH A . T 9 HOH 374 2374 2374 HOH HOH A . T 9 HOH 375 2375 2375 HOH HOH A . T 9 HOH 376 2376 2376 HOH HOH A . T 9 HOH 377 2377 2377 HOH HOH A . T 9 HOH 378 2378 2378 HOH HOH A . T 9 HOH 379 2379 2379 HOH HOH A . T 9 HOH 380 2380 2380 HOH HOH A . T 9 HOH 381 2381 2381 HOH HOH A . T 9 HOH 382 2382 2382 HOH HOH A . T 9 HOH 383 2383 2383 HOH HOH A . T 9 HOH 384 2384 2384 HOH HOH A . T 9 HOH 385 2385 2385 HOH HOH A . T 9 HOH 386 2386 2386 HOH HOH A . T 9 HOH 387 2387 2387 HOH HOH A . T 9 HOH 388 2388 2388 HOH HOH A . T 9 HOH 389 2389 2389 HOH HOH A . T 9 HOH 390 2390 2390 HOH HOH A . T 9 HOH 391 2391 2391 HOH HOH A . T 9 HOH 392 2392 2392 HOH HOH A . T 9 HOH 393 2393 2393 HOH HOH A . T 9 HOH 394 2394 2394 HOH HOH A . T 9 HOH 395 2395 2395 HOH HOH A . T 9 HOH 396 2396 2396 HOH HOH A . T 9 HOH 397 2397 2397 HOH HOH A . T 9 HOH 398 2398 2398 HOH HOH A . T 9 HOH 399 2399 2399 HOH HOH A . T 9 HOH 400 2400 2400 HOH HOH A . T 9 HOH 401 2401 2401 HOH HOH A . T 9 HOH 402 2402 2402 HOH HOH A . T 9 HOH 403 2403 2403 HOH HOH A . T 9 HOH 404 2404 2404 HOH HOH A . T 9 HOH 405 2405 2405 HOH HOH A . T 9 HOH 406 2406 2406 HOH HOH A . T 9 HOH 407 2407 2407 HOH HOH A . T 9 HOH 408 2408 2408 HOH HOH A . T 9 HOH 409 2409 2409 HOH HOH A . T 9 HOH 410 2410 2410 HOH HOH A . T 9 HOH 411 2411 2411 HOH HOH A . T 9 HOH 412 2412 2412 HOH HOH A . T 9 HOH 413 2413 2413 HOH HOH A . T 9 HOH 414 2414 2414 HOH HOH A . T 9 HOH 415 2415 2415 HOH HOH A . T 9 HOH 416 2416 2416 HOH HOH A . T 9 HOH 417 2417 2417 HOH HOH A . T 9 HOH 418 2418 2418 HOH HOH A . T 9 HOH 419 2419 2419 HOH HOH A . T 9 HOH 420 2420 2420 HOH HOH A . T 9 HOH 421 2421 2421 HOH HOH A . T 9 HOH 422 2422 2422 HOH HOH A . T 9 HOH 423 2423 2423 HOH HOH A . T 9 HOH 424 2424 2424 HOH HOH A . T 9 HOH 425 2425 2425 HOH HOH A . T 9 HOH 426 2426 2426 HOH HOH A . T 9 HOH 427 2427 2427 HOH HOH A . T 9 HOH 428 2428 2428 HOH HOH A . T 9 HOH 429 2429 2429 HOH HOH A . T 9 HOH 430 2430 2430 HOH HOH A . T 9 HOH 431 2431 2431 HOH HOH A . T 9 HOH 432 2432 2432 HOH HOH A . T 9 HOH 433 2433 2433 HOH HOH A . T 9 HOH 434 2434 2434 HOH HOH A . T 9 HOH 435 2435 2435 HOH HOH A . T 9 HOH 436 2436 2436 HOH HOH A . T 9 HOH 437 2437 2437 HOH HOH A . T 9 HOH 438 2438 2438 HOH HOH A . T 9 HOH 439 2439 2439 HOH HOH A . T 9 HOH 440 2440 2440 HOH HOH A . T 9 HOH 441 2441 2441 HOH HOH A . T 9 HOH 442 2442 2442 HOH HOH A . T 9 HOH 443 2443 2443 HOH HOH A . T 9 HOH 444 2444 2444 HOH HOH A . T 9 HOH 445 2445 2445 HOH HOH A . T 9 HOH 446 2446 2446 HOH HOH A . T 9 HOH 447 2447 2447 HOH HOH A . T 9 HOH 448 2448 2448 HOH HOH A . T 9 HOH 449 2449 2449 HOH HOH A . T 9 HOH 450 2450 2450 HOH HOH A . T 9 HOH 451 2451 2451 HOH HOH A . T 9 HOH 452 2452 2452 HOH HOH A . T 9 HOH 453 2453 2453 HOH HOH A . T 9 HOH 454 2454 2454 HOH HOH A . T 9 HOH 455 2455 2455 HOH HOH A . T 9 HOH 456 2456 2456 HOH HOH A . T 9 HOH 457 2457 2457 HOH HOH A . T 9 HOH 458 2458 2458 HOH HOH A . T 9 HOH 459 2459 2459 HOH HOH A . T 9 HOH 460 2460 2460 HOH HOH A . T 9 HOH 461 2461 2461 HOH HOH A . T 9 HOH 462 2462 2462 HOH HOH A . T 9 HOH 463 2463 2463 HOH HOH A . T 9 HOH 464 2464 2464 HOH HOH A . T 9 HOH 465 2465 2465 HOH HOH A . T 9 HOH 466 2466 2466 HOH HOH A . T 9 HOH 467 2467 2467 HOH HOH A . T 9 HOH 468 2468 2468 HOH HOH A . T 9 HOH 469 2469 2469 HOH HOH A . T 9 HOH 470 2470 2470 HOH HOH A . T 9 HOH 471 2471 2471 HOH HOH A . T 9 HOH 472 2472 2472 HOH HOH A . T 9 HOH 473 2473 2473 HOH HOH A . T 9 HOH 474 2474 2474 HOH HOH A . T 9 HOH 475 2475 2475 HOH HOH A . T 9 HOH 476 2476 2476 HOH HOH A . T 9 HOH 477 2477 2477 HOH HOH A . T 9 HOH 478 2478 2478 HOH HOH A . T 9 HOH 479 2479 2479 HOH HOH A . T 9 HOH 480 2480 2480 HOH HOH A . T 9 HOH 481 2481 2481 HOH HOH A . T 9 HOH 482 2482 2482 HOH HOH A . T 9 HOH 483 2483 2483 HOH HOH A . T 9 HOH 484 2484 2484 HOH HOH A . T 9 HOH 485 2485 2485 HOH HOH A . T 9 HOH 486 2486 2486 HOH HOH A . T 9 HOH 487 2487 2487 HOH HOH A . T 9 HOH 488 2488 2488 HOH HOH A . T 9 HOH 489 2489 2489 HOH HOH A . T 9 HOH 490 2490 2490 HOH HOH A . T 9 HOH 491 2491 2491 HOH HOH A . T 9 HOH 492 2492 2492 HOH HOH A . T 9 HOH 493 2493 2493 HOH HOH A . T 9 HOH 494 2494 2494 HOH HOH A . T 9 HOH 495 2495 2495 HOH HOH A . T 9 HOH 496 2496 2496 HOH HOH A . T 9 HOH 497 2497 2497 HOH HOH A . T 9 HOH 498 2498 2498 HOH HOH A . T 9 HOH 499 2499 2499 HOH HOH A . T 9 HOH 500 2500 2500 HOH HOH A . T 9 HOH 501 2501 2501 HOH HOH A . T 9 HOH 502 2502 2502 HOH HOH A . T 9 HOH 503 2503 2503 HOH HOH A . T 9 HOH 504 2504 2504 HOH HOH A . T 9 HOH 505 2505 2505 HOH HOH A . T 9 HOH 506 2506 2506 HOH HOH A . T 9 HOH 507 2507 2507 HOH HOH A . T 9 HOH 508 2508 2508 HOH HOH A . T 9 HOH 509 2509 2509 HOH HOH A . T 9 HOH 510 2510 2510 HOH HOH A . T 9 HOH 511 2511 2511 HOH HOH A . T 9 HOH 512 2512 2512 HOH HOH A . T 9 HOH 513 2513 2513 HOH HOH A . T 9 HOH 514 2514 2514 HOH HOH A . T 9 HOH 515 2515 2515 HOH HOH A . T 9 HOH 516 2516 2516 HOH HOH A . T 9 HOH 517 2517 2517 HOH HOH A . T 9 HOH 518 2518 2518 HOH HOH A . T 9 HOH 519 2519 2519 HOH HOH A . T 9 HOH 520 2520 2520 HOH HOH A . T 9 HOH 521 2521 2521 HOH HOH A . T 9 HOH 522 2522 2522 HOH HOH A . T 9 HOH 523 2523 2523 HOH HOH A . T 9 HOH 524 2524 2524 HOH HOH A . T 9 HOH 525 2525 2525 HOH HOH A . T 9 HOH 526 2526 2526 HOH HOH A . T 9 HOH 527 2527 2527 HOH HOH A . T 9 HOH 528 2528 2528 HOH HOH A . T 9 HOH 529 2529 2529 HOH HOH A . T 9 HOH 530 2530 2530 HOH HOH A . T 9 HOH 531 2531 2531 HOH HOH A . T 9 HOH 532 2532 2532 HOH HOH A . T 9 HOH 533 2533 2533 HOH HOH A . T 9 HOH 534 2534 2534 HOH HOH A . T 9 HOH 535 2535 2535 HOH HOH A . T 9 HOH 536 2536 2536 HOH HOH A . T 9 HOH 537 2537 2537 HOH HOH A . T 9 HOH 538 2538 2538 HOH HOH A . T 9 HOH 539 2539 2539 HOH HOH A . T 9 HOH 540 2540 2540 HOH HOH A . T 9 HOH 541 2541 2541 HOH HOH A . T 9 HOH 542 2542 2542 HOH HOH A . T 9 HOH 543 2543 2543 HOH HOH A . T 9 HOH 544 2544 2544 HOH HOH A . T 9 HOH 545 2545 2545 HOH HOH A . T 9 HOH 546 2546 2546 HOH HOH A . T 9 HOH 547 2547 2547 HOH HOH A . T 9 HOH 548 2548 2548 HOH HOH A . T 9 HOH 549 2549 2549 HOH HOH A . T 9 HOH 550 2550 2550 HOH HOH A . T 9 HOH 551 2551 2551 HOH HOH A . T 9 HOH 552 2552 2552 HOH HOH A . T 9 HOH 553 2553 2553 HOH HOH A . T 9 HOH 554 2554 2554 HOH HOH A . T 9 HOH 555 2555 2555 HOH HOH A . T 9 HOH 556 2556 2556 HOH HOH A . T 9 HOH 557 2557 2557 HOH HOH A . T 9 HOH 558 2558 2558 HOH HOH A . T 9 HOH 559 2559 2559 HOH HOH A . T 9 HOH 560 2560 2560 HOH HOH A . T 9 HOH 561 2561 2561 HOH HOH A . T 9 HOH 562 2562 2562 HOH HOH A . T 9 HOH 563 2563 2563 HOH HOH A . T 9 HOH 564 2564 2564 HOH HOH A . T 9 HOH 565 2565 2565 HOH HOH A . T 9 HOH 566 2566 2566 HOH HOH A . T 9 HOH 567 2567 2567 HOH HOH A . T 9 HOH 568 2568 2568 HOH HOH A . T 9 HOH 569 2569 2569 HOH HOH A . T 9 HOH 570 2570 2570 HOH HOH A . T 9 HOH 571 2571 2571 HOH HOH A . T 9 HOH 572 2572 2572 HOH HOH A . T 9 HOH 573 2573 2573 HOH HOH A . T 9 HOH 574 2574 2574 HOH HOH A . T 9 HOH 575 2575 2575 HOH HOH A . T 9 HOH 576 2576 2576 HOH HOH A . T 9 HOH 577 2577 2577 HOH HOH A . T 9 HOH 578 2578 2578 HOH HOH A . T 9 HOH 579 2579 2579 HOH HOH A . T 9 HOH 580 2580 2580 HOH HOH A . T 9 HOH 581 2581 2581 HOH HOH A . T 9 HOH 582 2582 2582 HOH HOH A . T 9 HOH 583 2583 2583 HOH HOH A . T 9 HOH 584 2584 2584 HOH HOH A . T 9 HOH 585 2585 2585 HOH HOH A . T 9 HOH 586 2586 2586 HOH HOH A . T 9 HOH 587 2587 2587 HOH HOH A . T 9 HOH 588 2588 2588 HOH HOH A . T 9 HOH 589 2589 2589 HOH HOH A . T 9 HOH 590 2590 2590 HOH HOH A . T 9 HOH 591 2591 2591 HOH HOH A . T 9 HOH 592 2592 2592 HOH HOH A . T 9 HOH 593 2593 2593 HOH HOH A . T 9 HOH 594 2594 2594 HOH HOH A . T 9 HOH 595 2595 2595 HOH HOH A . T 9 HOH 596 2596 2596 HOH HOH A . T 9 HOH 597 2597 2597 HOH HOH A . T 9 HOH 598 2598 2598 HOH HOH A . T 9 HOH 599 2599 2599 HOH HOH A . T 9 HOH 600 2600 2600 HOH HOH A . T 9 HOH 601 2601 2601 HOH HOH A . T 9 HOH 602 2602 2602 HOH HOH A . T 9 HOH 603 2603 2603 HOH HOH A . T 9 HOH 604 2604 2604 HOH HOH A . T 9 HOH 605 2605 2605 HOH HOH A . T 9 HOH 606 2606 2606 HOH HOH A . T 9 HOH 607 2607 2607 HOH HOH A . T 9 HOH 608 2608 2608 HOH HOH A . T 9 HOH 609 2609 2609 HOH HOH A . T 9 HOH 610 2610 2610 HOH HOH A . T 9 HOH 611 2611 2611 HOH HOH A . T 9 HOH 612 2612 2612 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 35 A ASN 76 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 80 A ASN 121 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 99 A ASN 140 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 154 A ASN 195 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 418 A ASN 459 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 435 A ASN 476 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 597 A ASN 638 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 11690 ? 1 MORE 36.0 ? 1 'SSA (A^2)' 49480 ? # 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 130.0390000000 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 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 56.6 ? 2 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 86.7 ? 3 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 99.9 ? 4 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OAD ? S CI9 . ? A CI9 1768 ? 1_555 99.7 ? 5 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OAD ? S CI9 . ? A CI9 1768 ? 1_555 153.8 ? 6 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OAD ? S CI9 . ? A CI9 1768 ? 1_555 88.5 ? 7 OE1 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 156.6 ? 8 OE2 ? A GLU 384 ? A GLU 425 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 100.7 ? 9 NE2 ? A HIS 512 ? A HIS 553 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 92.4 ? 10 OAD ? S CI9 . ? A CI9 1768 ? 1_555 ZN ? B ZN . ? A ZN 1751 ? 1_555 OD2 ? A ASP 346 ? A ASP 387 ? 1_555 103.7 ? 11 OD2 ? A ASP 412 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 1752 ? 1_555 OD1 ? A ASP 346 ? A ASP 387 ? 1_555 120.2 ? 12 OD2 ? A ASP 412 ? A ASP 453 ? 1_555 ZN ? C ZN . ? A ZN 1752 ? 1_555 NE2 ? A HIS 336 ? A HIS 377 ? 1_555 101.6 ? 13 OD1 ? A ASP 346 ? A ASP 387 ? 1_555 ZN ? C ZN . ? A ZN 1752 ? 1_555 NE2 ? A HIS 336 ? A HIS 377 ? 1_555 107.1 ? 14 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? A TYR 231 ? A TYR 272 ? 1_555 84.7 ? 15 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 53.8 ? 16 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 136.0 ? 17 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 86.9 ? 18 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 91.1 ? 19 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OG1 ? A THR 228 ? A THR 269 ? 1_555 99.3 ? 20 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 91.6 ? 21 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 80.0 ? 22 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 86.9 ? 23 OG1 ? A THR 228 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 171.0 ? 24 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 150.0 ? 25 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 73.8 ? 26 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 150.0 ? 27 OG1 ? A THR 228 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 73.2 ? 28 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? A THR 228 ? A THR 269 ? 1_555 104.6 ? 29 OE1 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? T HOH . ? A HOH 2196 ? 1_555 129.1 ? 30 O ? A TYR 231 ? A TYR 272 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? T HOH . ? A HOH 2196 ? 1_555 146.2 ? 31 OE2 ? A GLU 392 ? A GLU 433 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? T HOH . ? A HOH 2196 ? 1_555 76.8 ? 32 OG1 ? A THR 228 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? T HOH . ? A HOH 2196 ? 1_555 90.0 ? 33 OE2 ? A GLU 395 ? A GLU 436 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? T HOH . ? A HOH 2196 ? 1_555 97.9 ? 34 O ? A THR 228 ? A THR 269 ? 1_555 CA ? D CA . ? A CA 1753 ? 1_555 O ? T HOH . ? A HOH 2196 ? 1_555 74.2 ? # 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 2010-09-08 2 'Structure model' 1 1 2011-05-08 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Version format compliance' # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 17.7700 _pdbx_refine_tls.origin_y 49.3530 _pdbx_refine_tls.origin_z 44.8400 _pdbx_refine_tls.T[1][1] -0.0635 _pdbx_refine_tls.T[2][2] -0.0466 _pdbx_refine_tls.T[3][3] -0.0502 _pdbx_refine_tls.T[1][2] 0.0120 _pdbx_refine_tls.T[1][3] 0.0038 _pdbx_refine_tls.T[2][3] -0.0268 _pdbx_refine_tls.L[1][1] 0.2596 _pdbx_refine_tls.L[2][2] 0.4792 _pdbx_refine_tls.L[3][3] 0.0801 _pdbx_refine_tls.L[1][2] -0.2253 _pdbx_refine_tls.L[1][3] 0.0015 _pdbx_refine_tls.L[2][3] 0.0261 _pdbx_refine_tls.S[1][1] -0.0635 _pdbx_refine_tls.S[1][2] 0.0105 _pdbx_refine_tls.S[1][3] -0.0173 _pdbx_refine_tls.S[2][1] 0.0306 _pdbx_refine_tls.S[2][2] 0.0671 _pdbx_refine_tls.S[2][3] -0.1042 _pdbx_refine_tls.S[3][1] 0.0046 _pdbx_refine_tls.S[3][2] 0.0263 _pdbx_refine_tls.S[3][3] -0.0035 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id A _pdbx_refine_tls_group.beg_auth_seq_id 55 _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id A _pdbx_refine_tls_group.end_auth_seq_id 750 _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.4.0057 ? 1 HKL-2000 'data reduction' . ? 2 HKL-2000 'data scaling' . ? 3 REFMAC phasing . ? 4 # _pdbx_entry_details.entry_id 2XEG _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details 'CI9: ANTIBODY-RECRUITING MOLECULE ARM-P4 IS A UREA-BASED COMPOUND.' _pdbx_entry_details.sequence_details 'RS - CLONING ARTIFACT AT THE N-TERMINUS' # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A HOH 2507 ? ? 1_555 O A HOH 2507 ? ? 2_565 1.07 2 1 OE1 A GLU 276 ? A 1_555 O2 A BMA 1765 ? ? 2_565 1.97 3 1 O A HOH 2319 ? ? 1_555 O A HOH 2580 ? ? 2_565 2.02 # _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 GLU _pdbx_validate_rmsd_bond.auth_seq_id_1 557 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 CG _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 GLU _pdbx_validate_rmsd_bond.auth_seq_id_2 557 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.397 _pdbx_validate_rmsd_bond.bond_target_value 1.517 _pdbx_validate_rmsd_bond.bond_deviation -0.120 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.019 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 NE A ARG 440 ? ? CZ A ARG 440 ? ? NH2 A ARG 440 ? ? 116.29 120.30 -4.01 0.50 N 2 1 NE A ARG 673 ? ? CZ A ARG 673 ? ? NH2 A ARG 673 ? ? 116.15 120.30 -4.15 0.50 N 3 1 NE A ARG 688 ? B CZ A ARG 688 ? B NH1 A ARG 688 ? B 124.49 120.30 4.19 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 PHE A 164 ? ? 84.89 3.24 2 1 ASN A 178 ? ? 57.72 -126.34 3 1 LYS A 207 ? ? 73.64 -46.46 4 1 VAL A 382 ? ? -128.31 -108.70 5 1 ALA A 452 ? ? -149.24 56.94 6 1 ASP A 453 ? ? -84.62 -153.46 7 1 SER A 454 ? ? -36.96 124.03 8 1 SER A 517 ? ? -150.13 -157.58 9 1 ASP A 567 ? ? -155.22 66.02 10 1 ASN A 698 ? ? -169.79 98.17 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A ARG 42 ? A ARG 1 2 1 Y 1 A SER 43 ? A SER 2 3 1 Y 1 A LYS 44 ? A LYS 3 4 1 Y 1 A SER 45 ? A SER 4 5 1 Y 1 A SER 46 ? A SER 5 6 1 Y 1 A ASN 47 ? A ASN 6 7 1 Y 1 A GLU 48 ? A GLU 7 8 1 Y 1 A ALA 49 ? A ALA 8 9 1 Y 1 A THR 50 ? A THR 9 10 1 Y 1 A ASN 51 ? A ASN 10 11 1 Y 1 A ILE 52 ? A ILE 11 12 1 Y 1 A THR 53 ? A THR 12 13 1 Y 1 A PRO 54 ? A PRO 13 14 1 Y 1 A ASP 654 ? A ASP 613 15 1 Y 1 A LYS 655 ? A LYS 614 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'ZINC ION' ZN 3 'CALCIUM ION' CA 4 'CHLORIDE ION' CL 5 N-ACETYL-D-GLUCOSAMINE NAG 6 BETA-D-MANNOSE BMA 7 ALPHA-D-MANNOSE MAN 8 ;N-({(1S)-5-[4-(13-{[2,4-BIS(DIHYDROXYAMINO)PHENYL]AMINO}-2,5,8,11-TETRAOXATRIDEC-1-YL)-1H-1,2,3-TRIAZOL-1-YL]-1-CARBOXYPENTYL}CARBAMOYL)-L-GLUTAMIC ACID ; CI9 9 water HOH #